data_9EY9
# 
_entry.id   9EY9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EY9         pdb_00009ey9 10.2210/pdb9ey9/pdb 
WWPDB D_1292137791 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-19 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EY9 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '20S yeast proteasome in complex with cepafungin I' 
_pdbx_database_related.db_id          4FZC 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michael.groll@tum.de 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Groll 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1660-340X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Praeve, L.'        1 ? 
'Kuttenlochner, W.' 2 ? 
'Tabak, W.W.A.'     3 ? 
'Langer, C.'        4 ? 
'Kaiser, M.'        5 ? 
'Groll, M.'         6 ? 
'Bode, H.B.'        7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2451-9294 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                3212 
_citation.page_last                 3223 
_citation.title                     'Bioengineering of syrbactin megasynthetases for immunoproteasome inhibitor production' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.chempr.2024.07.013 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Prave, L.'         1 ? 
primary 'Kuttenlochner, W.' 2 ? 
primary 'Tabak, W.W.'       3 ? 
primary 'Langer, C.'        4 ? 
primary 'Kaiser, M.'        5 ? 
primary 'Groll, M.'         6 ? 
primary 'Bode, H.B.'        7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     nat 'Proteasome subunit alpha type-2'          27191.828 2 ?        ? ? ? 
2  polymer     nat 'Proteasome subunit alpha type-3'          28748.230 2 ?        ? ? ? 
3  polymer     nat 'Proteasome subunit alpha type-4'          28478.111 2 ?        ? ? ? 
4  polymer     nat 'Proteasome subunit alpha type-5'          28649.086 2 ?        ? ? ? 
5  polymer     nat 'Proteasome subunit alpha type-6'          25634.000 2 ?        ? ? ? 
6  polymer     nat 'Probable proteasome subunit alpha type-7' 31575.068 2 ?        ? ? ? 
7  polymer     nat 'Proteasome subunit alpha type-1'          28033.830 2 ?        ? ? ? 
8  polymer     nat 'proteasome endopeptidase complex'         25013.355 2 3.4.25.1 ? ? ? 
9  polymer     nat 'Proteasome subunit beta type-3'           22627.842 2 ?        ? ? ? 
10 polymer     nat 'Proteasome subunit beta type-4'           22545.676 2 ?        ? ? ? 
11 polymer     nat 'proteasome endopeptidase complex'         23224.146 2 3.4.25.1 ? ? ? 
12 polymer     nat 'Proteasome subunit beta type-6'           24883.928 2 ?        ? ? ? 
13 polymer     nat 'Proteasome subunit beta type-7'           27200.893 2 ?        ? ? ? 
14 polymer     nat 'Proteasome subunit beta type-1'           21517.186 2 3.4.25.1 ? ? ? 
15 non-polymer syn 'MAGNESIUM ION'                            24.305    8 ?        ? ? ? 
16 non-polymer syn 'sybactin derivative'                      603.750   4 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1  'Macropain subunit Y7,Multicatalytic endopeptidase complex subunit Y7,Proteasome component Y7,Proteinase YSCE subunit 7' 
2  'Macropain subunit Y13,Multicatalytic endopeptidase complex subunit Y13,Proteasome component Y13,Proteinase YSCE subunit 13' 
3  
'Macropain subunit PRE6,Multicatalytic endopeptidase complex subunit PRE6,Proteasome component PRE6,Proteinase YSCE subunit PRE6' 
4  
'Macropain subunit PUP2,Multicatalytic endopeptidase complex subunit PUP2,Proteasome component PUP2,Proteinase YSCE subunit PUP2' 
5  
'Macropain subunit PRE5,Multicatalytic endopeptidase complex subunit PRE5,Proteasome component PRE5,Proteinase YSCE subunit PRE5' 
6  'Macropain subunit C1,Multicatalytic endopeptidase complex subunit C1,Proteasome component C1,Proteinase YSCE subunit 1' 
7  
;Macropain subunit C7-alpha,Multicatalytic endopeptidase complex C7,Proteasome component C7-alpha,Proteasome component Y8,Proteinase YSCE subunit 7,SCL1 suppressor protein
;
9  'Macropain subunit PUP3,Multicatalytic endopeptidase complex subunit PUP3,Proteasome component PUP3' 
10 'Macropain subunit C11,Multicatalytic endopeptidase complex subunit C11,Proteasome component C11,Proteinase YSCE subunit 11' 
12 'Multicatalytic endopeptidase complex subunit C5,Proteasome component C5' 
13 
'Macropain subunit PRE4,Multicatalytic endopeptidase complex subunit PRE4,Proteasome component PRE4,Proteinase YSCE subunit PRE4' 
14 
'Macropain subunit PRE3,Multicatalytic endopeptidase complex subunit PRE3,Proteasome component PRE3,Proteinase YSCE subunit PRE3' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1  'polypeptide(L)' no no 
;MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGP
DYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWK
ATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
;
;MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGP
DYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWK
ATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
;
A,O ? 
2  'polypeptide(L)' no no 
;MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGL
TADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGW
KAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
;
;MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGL
TADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGW
KAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
;
B,P ? 
3  'polypeptide(L)' no no 
;MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNA
DSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWS
AQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
;
;MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNA
DSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWS
AQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
;
C,Q ? 
4  'polypeptide(L)' no no 
;MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSG
LTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEP
SGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
;
;MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSG
LTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEP
SGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
;
D,R ? 
5  'polypeptide(L)' no no 
;MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPD
ARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTA
IGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
;
;MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPD
ARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTA
IGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
;
E,S ? 
6  'polypeptide(L)' no no 
;MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSG
LIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGY
KGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
;
;MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSG
LIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGY
KGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
;
F,T ? 
7  'polypeptide(L)' no no 
;MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIG
MVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPA
GYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
;
;MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIG
MVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPA
GYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
;
G,U ? 
8  'polypeptide(L)' no no 
;TIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQ
MLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQA
GIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA
;
;TIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQ
MLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQA
GIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA
;
H,V ? 
9  'polypeptide(L)' no no 
;MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEER
AIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEP
EDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD
;
;MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEER
AIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEP
EDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD
;
I,W ? 
10 'polypeptide(L)' no no 
;MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV
SSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL
LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDFQAQ
;
;MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV
SSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL
LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDFQAQ
;
J,X ? 
11 'polypeptide(L)' no no 
;TTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASK
ILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSI
LAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
;
;TTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASK
ILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSI
LAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
;
K,Y ? 
12 'polypeptide(L)' no no 
;QFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHN
DKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQY
EPGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD
;
;QFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHN
DKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQY
EPGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD
;
L,Z ? 
13 'polypeptide(L)' no no 
;TQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL
KDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFG
AHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKG
YGTQKI
;
;TQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL
KDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFG
AHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKG
YGTQKI
;
M,a ? 
14 'polypeptide(L)' no no 
;TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAAS
VFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLS
QAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
;
;TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAAS
VFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLS
QAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
;
N,b ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
15 'MAGNESIUM ION'       MG    
16 'sybactin derivative' A1H71 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1  1   MET n 
1  2   THR n 
1  3   ASP n 
1  4   ARG n 
1  5   TYR n 
1  6   SER n 
1  7   PHE n 
1  8   SER n 
1  9   LEU n 
1  10  THR n 
1  11  THR n 
1  12  PHE n 
1  13  SER n 
1  14  PRO n 
1  15  SER n 
1  16  GLY n 
1  17  LYS n 
1  18  LEU n 
1  19  GLY n 
1  20  GLN n 
1  21  ILE n 
1  22  ASP n 
1  23  TYR n 
1  24  ALA n 
1  25  LEU n 
1  26  THR n 
1  27  ALA n 
1  28  VAL n 
1  29  LYS n 
1  30  GLN n 
1  31  GLY n 
1  32  VAL n 
1  33  THR n 
1  34  SER n 
1  35  LEU n 
1  36  GLY n 
1  37  ILE n 
1  38  LYS n 
1  39  ALA n 
1  40  THR n 
1  41  ASN n 
1  42  GLY n 
1  43  VAL n 
1  44  VAL n 
1  45  ILE n 
1  46  ALA n 
1  47  THR n 
1  48  GLU n 
1  49  LYS n 
1  50  LYS n 
1  51  SER n 
1  52  SER n 
1  53  SER n 
1  54  PRO n 
1  55  LEU n 
1  56  ALA n 
1  57  MET n 
1  58  SER n 
1  59  GLU n 
1  60  THR n 
1  61  LEU n 
1  62  SER n 
1  63  LYS n 
1  64  VAL n 
1  65  SER n 
1  66  LEU n 
1  67  LEU n 
1  68  THR n 
1  69  PRO n 
1  70  ASP n 
1  71  ILE n 
1  72  GLY n 
1  73  ALA n 
1  74  VAL n 
1  75  TYR n 
1  76  SER n 
1  77  GLY n 
1  78  MET n 
1  79  GLY n 
1  80  PRO n 
1  81  ASP n 
1  82  TYR n 
1  83  ARG n 
1  84  VAL n 
1  85  LEU n 
1  86  VAL n 
1  87  ASP n 
1  88  LYS n 
1  89  SER n 
1  90  ARG n 
1  91  LYS n 
1  92  VAL n 
1  93  ALA n 
1  94  HIS n 
1  95  THR n 
1  96  SER n 
1  97  TYR n 
1  98  LYS n 
1  99  ARG n 
1  100 ILE n 
1  101 TYR n 
1  102 GLY n 
1  103 GLU n 
1  104 TYR n 
1  105 PRO n 
1  106 PRO n 
1  107 THR n 
1  108 LYS n 
1  109 LEU n 
1  110 LEU n 
1  111 VAL n 
1  112 SER n 
1  113 GLU n 
1  114 VAL n 
1  115 ALA n 
1  116 LYS n 
1  117 ILE n 
1  118 MET n 
1  119 GLN n 
1  120 GLU n 
1  121 ALA n 
1  122 THR n 
1  123 GLN n 
1  124 SER n 
1  125 GLY n 
1  126 GLY n 
1  127 VAL n 
1  128 ARG n 
1  129 PRO n 
1  130 PHE n 
1  131 GLY n 
1  132 VAL n 
1  133 SER n 
1  134 LEU n 
1  135 LEU n 
1  136 ILE n 
1  137 ALA n 
1  138 GLY n 
1  139 HIS n 
1  140 ASP n 
1  141 GLU n 
1  142 PHE n 
1  143 ASN n 
1  144 GLY n 
1  145 PHE n 
1  146 SER n 
1  147 LEU n 
1  148 TYR n 
1  149 GLN n 
1  150 VAL n 
1  151 ASP n 
1  152 PRO n 
1  153 SER n 
1  154 GLY n 
1  155 SER n 
1  156 TYR n 
1  157 PHE n 
1  158 PRO n 
1  159 TRP n 
1  160 LYS n 
1  161 ALA n 
1  162 THR n 
1  163 ALA n 
1  164 ILE n 
1  165 GLY n 
1  166 LYS n 
1  167 GLY n 
1  168 SER n 
1  169 VAL n 
1  170 ALA n 
1  171 ALA n 
1  172 LYS n 
1  173 THR n 
1  174 PHE n 
1  175 LEU n 
1  176 GLU n 
1  177 LYS n 
1  178 ARG n 
1  179 TRP n 
1  180 ASN n 
1  181 ASP n 
1  182 GLU n 
1  183 LEU n 
1  184 GLU n 
1  185 LEU n 
1  186 GLU n 
1  187 ASP n 
1  188 ALA n 
1  189 ILE n 
1  190 HIS n 
1  191 ILE n 
1  192 ALA n 
1  193 LEU n 
1  194 LEU n 
1  195 THR n 
1  196 LEU n 
1  197 LYS n 
1  198 GLU n 
1  199 SER n 
1  200 VAL n 
1  201 GLU n 
1  202 GLY n 
1  203 GLU n 
1  204 PHE n 
1  205 ASN n 
1  206 GLY n 
1  207 ASP n 
1  208 THR n 
1  209 ILE n 
1  210 GLU n 
1  211 LEU n 
1  212 ALA n 
1  213 ILE n 
1  214 ILE n 
1  215 GLY n 
1  216 ASP n 
1  217 GLU n 
1  218 ASN n 
1  219 PRO n 
1  220 ASP n 
1  221 LEU n 
1  222 LEU n 
1  223 GLY n 
1  224 TYR n 
1  225 THR n 
1  226 GLY n 
1  227 ILE n 
1  228 PRO n 
1  229 THR n 
1  230 ASP n 
1  231 LYS n 
1  232 GLY n 
1  233 PRO n 
1  234 ARG n 
1  235 PHE n 
1  236 ARG n 
1  237 LYS n 
1  238 LEU n 
1  239 THR n 
1  240 SER n 
1  241 GLN n 
1  242 GLU n 
1  243 ILE n 
1  244 ASN n 
1  245 ASP n 
1  246 ARG n 
1  247 LEU n 
1  248 GLU n 
1  249 ALA n 
1  250 LEU n 
2  1   MET n 
2  2   GLY n 
2  3   SER n 
2  4   ARG n 
2  5   ARG n 
2  6   TYR n 
2  7   ASP n 
2  8   SER n 
2  9   ARG n 
2  10  THR n 
2  11  THR n 
2  12  ILE n 
2  13  PHE n 
2  14  SER n 
2  15  PRO n 
2  16  GLU n 
2  17  GLY n 
2  18  ARG n 
2  19  LEU n 
2  20  TYR n 
2  21  GLN n 
2  22  VAL n 
2  23  GLU n 
2  24  TYR n 
2  25  ALA n 
2  26  LEU n 
2  27  GLU n 
2  28  SER n 
2  29  ILE n 
2  30  SER n 
2  31  HIS n 
2  32  ALA n 
2  33  GLY n 
2  34  THR n 
2  35  ALA n 
2  36  ILE n 
2  37  GLY n 
2  38  ILE n 
2  39  MET n 
2  40  ALA n 
2  41  SER n 
2  42  ASP n 
2  43  GLY n 
2  44  ILE n 
2  45  VAL n 
2  46  LEU n 
2  47  ALA n 
2  48  ALA n 
2  49  GLU n 
2  50  ARG n 
2  51  LYS n 
2  52  VAL n 
2  53  THR n 
2  54  SER n 
2  55  THR n 
2  56  LEU n 
2  57  LEU n 
2  58  GLU n 
2  59  GLN n 
2  60  ASP n 
2  61  THR n 
2  62  SER n 
2  63  THR n 
2  64  GLU n 
2  65  LYS n 
2  66  LEU n 
2  67  TYR n 
2  68  LYS n 
2  69  LEU n 
2  70  ASN n 
2  71  ASP n 
2  72  LYS n 
2  73  ILE n 
2  74  ALA n 
2  75  VAL n 
2  76  ALA n 
2  77  VAL n 
2  78  ALA n 
2  79  GLY n 
2  80  LEU n 
2  81  THR n 
2  82  ALA n 
2  83  ASP n 
2  84  ALA n 
2  85  GLU n 
2  86  ILE n 
2  87  LEU n 
2  88  ILE n 
2  89  ASN n 
2  90  THR n 
2  91  ALA n 
2  92  ARG n 
2  93  ILE n 
2  94  HIS n 
2  95  ALA n 
2  96  GLN n 
2  97  ASN n 
2  98  TYR n 
2  99  LEU n 
2  100 LYS n 
2  101 THR n 
2  102 TYR n 
2  103 ASN n 
2  104 GLU n 
2  105 ASP n 
2  106 ILE n 
2  107 PRO n 
2  108 VAL n 
2  109 GLU n 
2  110 ILE n 
2  111 LEU n 
2  112 VAL n 
2  113 ARG n 
2  114 ARG n 
2  115 LEU n 
2  116 SER n 
2  117 ASP n 
2  118 ILE n 
2  119 LYS n 
2  120 GLN n 
2  121 GLY n 
2  122 TYR n 
2  123 THR n 
2  124 GLN n 
2  125 HIS n 
2  126 GLY n 
2  127 GLY n 
2  128 LEU n 
2  129 ARG n 
2  130 PRO n 
2  131 PHE n 
2  132 GLY n 
2  133 VAL n 
2  134 SER n 
2  135 PHE n 
2  136 ILE n 
2  137 TYR n 
2  138 ALA n 
2  139 GLY n 
2  140 TYR n 
2  141 ASP n 
2  142 ASP n 
2  143 ARG n 
2  144 TYR n 
2  145 GLY n 
2  146 TYR n 
2  147 GLN n 
2  148 LEU n 
2  149 TYR n 
2  150 THR n 
2  151 SER n 
2  152 ASN n 
2  153 PRO n 
2  154 SER n 
2  155 GLY n 
2  156 ASN n 
2  157 TYR n 
2  158 THR n 
2  159 GLY n 
2  160 TRP n 
2  161 LYS n 
2  162 ALA n 
2  163 ILE n 
2  164 SER n 
2  165 VAL n 
2  166 GLY n 
2  167 ALA n 
2  168 ASN n 
2  169 THR n 
2  170 SER n 
2  171 ALA n 
2  172 ALA n 
2  173 GLN n 
2  174 THR n 
2  175 LEU n 
2  176 LEU n 
2  177 GLN n 
2  178 MET n 
2  179 ASP n 
2  180 TYR n 
2  181 LYS n 
2  182 ASP n 
2  183 ASP n 
2  184 MET n 
2  185 LYS n 
2  186 VAL n 
2  187 ASP n 
2  188 ASP n 
2  189 ALA n 
2  190 ILE n 
2  191 GLU n 
2  192 LEU n 
2  193 ALA n 
2  194 LEU n 
2  195 LYS n 
2  196 THR n 
2  197 LEU n 
2  198 SER n 
2  199 LYS n 
2  200 THR n 
2  201 THR n 
2  202 ASP n 
2  203 SER n 
2  204 SER n 
2  205 ALA n 
2  206 LEU n 
2  207 THR n 
2  208 TYR n 
2  209 ASP n 
2  210 ARG n 
2  211 LEU n 
2  212 GLU n 
2  213 PHE n 
2  214 ALA n 
2  215 THR n 
2  216 ILE n 
2  217 ARG n 
2  218 LYS n 
2  219 GLY n 
2  220 ALA n 
2  221 ASN n 
2  222 ASP n 
2  223 GLY n 
2  224 GLU n 
2  225 VAL n 
2  226 TYR n 
2  227 GLN n 
2  228 LYS n 
2  229 ILE n 
2  230 PHE n 
2  231 LYS n 
2  232 PRO n 
2  233 GLN n 
2  234 GLU n 
2  235 ILE n 
2  236 LYS n 
2  237 ASP n 
2  238 ILE n 
2  239 LEU n 
2  240 VAL n 
2  241 LYS n 
2  242 THR n 
2  243 GLY n 
2  244 ILE n 
2  245 THR n 
2  246 LYS n 
2  247 LYS n 
2  248 ASP n 
2  249 GLU n 
2  250 ASP n 
2  251 GLU n 
2  252 GLU n 
2  253 ALA n 
2  254 ASP n 
2  255 GLU n 
2  256 ASP n 
2  257 MET n 
2  258 LYS n 
3  1   MET n 
3  2   SER n 
3  3   GLY n 
3  4   TYR n 
3  5   ASP n 
3  6   ARG n 
3  7   ALA n 
3  8   LEU n 
3  9   SER n 
3  10  ILE n 
3  11  PHE n 
3  12  SER n 
3  13  PRO n 
3  14  ASP n 
3  15  GLY n 
3  16  HIS n 
3  17  ILE n 
3  18  PHE n 
3  19  GLN n 
3  20  VAL n 
3  21  GLU n 
3  22  TYR n 
3  23  ALA n 
3  24  LEU n 
3  25  GLU n 
3  26  ALA n 
3  27  VAL n 
3  28  LYS n 
3  29  ARG n 
3  30  GLY n 
3  31  THR n 
3  32  CYS n 
3  33  ALA n 
3  34  VAL n 
3  35  GLY n 
3  36  VAL n 
3  37  LYS n 
3  38  GLY n 
3  39  LYS n 
3  40  ASN n 
3  41  CYS n 
3  42  VAL n 
3  43  VAL n 
3  44  LEU n 
3  45  GLY n 
3  46  CYS n 
3  47  GLU n 
3  48  ARG n 
3  49  ARG n 
3  50  SER n 
3  51  THR n 
3  52  LEU n 
3  53  LYS n 
3  54  LEU n 
3  55  GLN n 
3  56  ASP n 
3  57  THR n 
3  58  ARG n 
3  59  ILE n 
3  60  THR n 
3  61  PRO n 
3  62  SER n 
3  63  LYS n 
3  64  VAL n 
3  65  SER n 
3  66  LYS n 
3  67  ILE n 
3  68  ASP n 
3  69  SER n 
3  70  HIS n 
3  71  VAL n 
3  72  VAL n 
3  73  LEU n 
3  74  SER n 
3  75  PHE n 
3  76  SER n 
3  77  GLY n 
3  78  LEU n 
3  79  ASN n 
3  80  ALA n 
3  81  ASP n 
3  82  SER n 
3  83  ARG n 
3  84  ILE n 
3  85  LEU n 
3  86  ILE n 
3  87  GLU n 
3  88  LYS n 
3  89  ALA n 
3  90  ARG n 
3  91  VAL n 
3  92  GLU n 
3  93  ALA n 
3  94  GLN n 
3  95  SER n 
3  96  HIS n 
3  97  ARG n 
3  98  LEU n 
3  99  THR n 
3  100 LEU n 
3  101 GLU n 
3  102 ASP n 
3  103 PRO n 
3  104 VAL n 
3  105 THR n 
3  106 VAL n 
3  107 GLU n 
3  108 TYR n 
3  109 LEU n 
3  110 THR n 
3  111 ARG n 
3  112 TYR n 
3  113 VAL n 
3  114 ALA n 
3  115 GLY n 
3  116 VAL n 
3  117 GLN n 
3  118 GLN n 
3  119 ARG n 
3  120 TYR n 
3  121 THR n 
3  122 GLN n 
3  123 SER n 
3  124 GLY n 
3  125 GLY n 
3  126 VAL n 
3  127 ARG n 
3  128 PRO n 
3  129 PHE n 
3  130 GLY n 
3  131 VAL n 
3  132 SER n 
3  133 THR n 
3  134 LEU n 
3  135 ILE n 
3  136 ALA n 
3  137 GLY n 
3  138 PHE n 
3  139 ASP n 
3  140 PRO n 
3  141 ARG n 
3  142 ASP n 
3  143 ASP n 
3  144 GLU n 
3  145 PRO n 
3  146 LYS n 
3  147 LEU n 
3  148 TYR n 
3  149 GLN n 
3  150 THR n 
3  151 GLU n 
3  152 PRO n 
3  153 SER n 
3  154 GLY n 
3  155 ILE n 
3  156 TYR n 
3  157 SER n 
3  158 SER n 
3  159 TRP n 
3  160 SER n 
3  161 ALA n 
3  162 GLN n 
3  163 THR n 
3  164 ILE n 
3  165 GLY n 
3  166 ARG n 
3  167 ASN n 
3  168 SER n 
3  169 LYS n 
3  170 THR n 
3  171 VAL n 
3  172 ARG n 
3  173 GLU n 
3  174 PHE n 
3  175 LEU n 
3  176 GLU n 
3  177 LYS n 
3  178 ASN n 
3  179 TYR n 
3  180 ASP n 
3  181 ARG n 
3  182 LYS n 
3  183 GLU n 
3  184 PRO n 
3  185 PRO n 
3  186 ALA n 
3  187 THR n 
3  188 VAL n 
3  189 GLU n 
3  190 GLU n 
3  191 CYS n 
3  192 VAL n 
3  193 LYS n 
3  194 LEU n 
3  195 THR n 
3  196 VAL n 
3  197 ARG n 
3  198 SER n 
3  199 LEU n 
3  200 LEU n 
3  201 GLU n 
3  202 VAL n 
3  203 VAL n 
3  204 GLN n 
3  205 THR n 
3  206 GLY n 
3  207 ALA n 
3  208 LYS n 
3  209 ASN n 
3  210 ILE n 
3  211 GLU n 
3  212 ILE n 
3  213 THR n 
3  214 VAL n 
3  215 VAL n 
3  216 LYS n 
3  217 PRO n 
3  218 ASP n 
3  219 SER n 
3  220 ASP n 
3  221 ILE n 
3  222 VAL n 
3  223 ALA n 
3  224 LEU n 
3  225 SER n 
3  226 SER n 
3  227 GLU n 
3  228 GLU n 
3  229 ILE n 
3  230 ASN n 
3  231 GLN n 
3  232 TYR n 
3  233 VAL n 
3  234 THR n 
3  235 GLN n 
3  236 ILE n 
3  237 GLU n 
3  238 GLN n 
3  239 GLU n 
3  240 LYS n 
3  241 GLN n 
3  242 GLU n 
3  243 GLN n 
3  244 GLN n 
3  245 GLU n 
3  246 GLN n 
3  247 ASP n 
3  248 LYS n 
3  249 LYS n 
3  250 LYS n 
3  251 LYS n 
3  252 SER n 
3  253 ASN n 
3  254 HIS n 
4  1   MET n 
4  2   PHE n 
4  3   LEU n 
4  4   THR n 
4  5   ARG n 
4  6   SER n 
4  7   GLU n 
4  8   TYR n 
4  9   ASP n 
4  10  ARG n 
4  11  GLY n 
4  12  VAL n 
4  13  SER n 
4  14  THR n 
4  15  PHE n 
4  16  SER n 
4  17  PRO n 
4  18  GLU n 
4  19  GLY n 
4  20  ARG n 
4  21  LEU n 
4  22  PHE n 
4  23  GLN n 
4  24  VAL n 
4  25  GLU n 
4  26  TYR n 
4  27  SER n 
4  28  LEU n 
4  29  GLU n 
4  30  ALA n 
4  31  ILE n 
4  32  LYS n 
4  33  LEU n 
4  34  GLY n 
4  35  SER n 
4  36  THR n 
4  37  ALA n 
4  38  ILE n 
4  39  GLY n 
4  40  ILE n 
4  41  ALA n 
4  42  THR n 
4  43  LYS n 
4  44  GLU n 
4  45  GLY n 
4  46  VAL n 
4  47  VAL n 
4  48  LEU n 
4  49  GLY n 
4  50  VAL n 
4  51  GLU n 
4  52  LYS n 
4  53  ARG n 
4  54  ALA n 
4  55  THR n 
4  56  SER n 
4  57  PRO n 
4  58  LEU n 
4  59  LEU n 
4  60  GLU n 
4  61  SER n 
4  62  ASP n 
4  63  SER n 
4  64  ILE n 
4  65  GLU n 
4  66  LYS n 
4  67  ILE n 
4  68  VAL n 
4  69  GLU n 
4  70  ILE n 
4  71  ASP n 
4  72  ARG n 
4  73  HIS n 
4  74  ILE n 
4  75  GLY n 
4  76  CYS n 
4  77  ALA n 
4  78  MET n 
4  79  SER n 
4  80  GLY n 
4  81  LEU n 
4  82  THR n 
4  83  ALA n 
4  84  ASP n 
4  85  ALA n 
4  86  ARG n 
4  87  SER n 
4  88  MET n 
4  89  ILE n 
4  90  GLU n 
4  91  HIS n 
4  92  ALA n 
4  93  ARG n 
4  94  THR n 
4  95  ALA n 
4  96  ALA n 
4  97  VAL n 
4  98  THR n 
4  99  HIS n 
4  100 ASN n 
4  101 LEU n 
4  102 TYR n 
4  103 TYR n 
4  104 ASP n 
4  105 GLU n 
4  106 ASP n 
4  107 ILE n 
4  108 ASN n 
4  109 VAL n 
4  110 GLU n 
4  111 SER n 
4  112 LEU n 
4  113 THR n 
4  114 GLN n 
4  115 SER n 
4  116 VAL n 
4  117 CYS n 
4  118 ASP n 
4  119 LEU n 
4  120 ALA n 
4  121 LEU n 
4  122 ARG n 
4  123 PHE n 
4  124 GLY n 
4  125 GLU n 
4  126 GLY n 
4  127 ALA n 
4  128 SER n 
4  129 GLY n 
4  130 GLU n 
4  131 GLU n 
4  132 ARG n 
4  133 LEU n 
4  134 MET n 
4  135 SER n 
4  136 ARG n 
4  137 PRO n 
4  138 PHE n 
4  139 GLY n 
4  140 VAL n 
4  141 ALA n 
4  142 LEU n 
4  143 LEU n 
4  144 ILE n 
4  145 ALA n 
4  146 GLY n 
4  147 HIS n 
4  148 ASP n 
4  149 ALA n 
4  150 ASP n 
4  151 ASP n 
4  152 GLY n 
4  153 TYR n 
4  154 GLN n 
4  155 LEU n 
4  156 PHE n 
4  157 HIS n 
4  158 ALA n 
4  159 GLU n 
4  160 PRO n 
4  161 SER n 
4  162 GLY n 
4  163 THR n 
4  164 PHE n 
4  165 TYR n 
4  166 ARG n 
4  167 TYR n 
4  168 ASN n 
4  169 ALA n 
4  170 LYS n 
4  171 ALA n 
4  172 ILE n 
4  173 GLY n 
4  174 SER n 
4  175 GLY n 
4  176 SER n 
4  177 GLU n 
4  178 GLY n 
4  179 ALA n 
4  180 GLN n 
4  181 ALA n 
4  182 GLU n 
4  183 LEU n 
4  184 LEU n 
4  185 ASN n 
4  186 GLU n 
4  187 TRP n 
4  188 HIS n 
4  189 SER n 
4  190 SER n 
4  191 LEU n 
4  192 THR n 
4  193 LEU n 
4  194 LYS n 
4  195 GLU n 
4  196 ALA n 
4  197 GLU n 
4  198 LEU n 
4  199 LEU n 
4  200 VAL n 
4  201 LEU n 
4  202 LYS n 
4  203 ILE n 
4  204 LEU n 
4  205 LYS n 
4  206 GLN n 
4  207 VAL n 
4  208 MET n 
4  209 GLU n 
4  210 GLU n 
4  211 LYS n 
4  212 LEU n 
4  213 ASP n 
4  214 GLU n 
4  215 ASN n 
4  216 ASN n 
4  217 ALA n 
4  218 GLN n 
4  219 LEU n 
4  220 SER n 
4  221 CYS n 
4  222 ILE n 
4  223 THR n 
4  224 LYS n 
4  225 GLN n 
4  226 ASP n 
4  227 GLY n 
4  228 PHE n 
4  229 LYS n 
4  230 ILE n 
4  231 TYR n 
4  232 ASP n 
4  233 ASN n 
4  234 GLU n 
4  235 LYS n 
4  236 THR n 
4  237 ALA n 
4  238 GLU n 
4  239 LEU n 
4  240 ILE n 
4  241 LYS n 
4  242 GLU n 
4  243 LEU n 
4  244 LYS n 
4  245 GLU n 
4  246 LYS n 
4  247 GLU n 
4  248 ALA n 
4  249 ALA n 
4  250 GLU n 
4  251 SER n 
4  252 PRO n 
4  253 GLU n 
4  254 GLU n 
4  255 ALA n 
4  256 ASP n 
4  257 VAL n 
4  258 GLU n 
4  259 MET n 
4  260 SER n 
5  1   MET n 
5  2   PHE n 
5  3   ARG n 
5  4   ASN n 
5  5   ASN n 
5  6   TYR n 
5  7   ASP n 
5  8   GLY n 
5  9   ASP n 
5  10  THR n 
5  11  VAL n 
5  12  THR n 
5  13  PHE n 
5  14  SER n 
5  15  PRO n 
5  16  THR n 
5  17  GLY n 
5  18  ARG n 
5  19  LEU n 
5  20  PHE n 
5  21  GLN n 
5  22  VAL n 
5  23  GLU n 
5  24  TYR n 
5  25  ALA n 
5  26  LEU n 
5  27  GLU n 
5  28  ALA n 
5  29  ILE n 
5  30  LYS n 
5  31  GLN n 
5  32  GLY n 
5  33  SER n 
5  34  VAL n 
5  35  THR n 
5  36  VAL n 
5  37  GLY n 
5  38  LEU n 
5  39  ARG n 
5  40  SER n 
5  41  ASN n 
5  42  THR n 
5  43  HIS n 
5  44  ALA n 
5  45  VAL n 
5  46  LEU n 
5  47  VAL n 
5  48  ALA n 
5  49  LEU n 
5  50  LYS n 
5  51  ARG n 
5  52  ASN n 
5  53  ALA n 
5  54  ASP n 
5  55  GLU n 
5  56  LEU n 
5  57  SER n 
5  58  SER n 
5  59  TYR n 
5  60  GLN n 
5  61  LYS n 
5  62  LYS n 
5  63  ILE n 
5  64  ILE n 
5  65  LYS n 
5  66  CYS n 
5  67  ASP n 
5  68  GLU n 
5  69  HIS n 
5  70  MET n 
5  71  GLY n 
5  72  LEU n 
5  73  SER n 
5  74  LEU n 
5  75  ALA n 
5  76  GLY n 
5  77  LEU n 
5  78  ALA n 
5  79  PRO n 
5  80  ASP n 
5  81  ALA n 
5  82  ARG n 
5  83  VAL n 
5  84  LEU n 
5  85  SER n 
5  86  ASN n 
5  87  TYR n 
5  88  LEU n 
5  89  ARG n 
5  90  GLN n 
5  91  GLN n 
5  92  CYS n 
5  93  ASN n 
5  94  TYR n 
5  95  SER n 
5  96  SER n 
5  97  LEU n 
5  98  VAL n 
5  99  PHE n 
5  100 ASN n 
5  101 ARG n 
5  102 LYS n 
5  103 LEU n 
5  104 ALA n 
5  105 VAL n 
5  106 GLU n 
5  107 ARG n 
5  108 ALA n 
5  109 GLY n 
5  110 HIS n 
5  111 LEU n 
5  112 LEU n 
5  113 CYS n 
5  114 ASP n 
5  115 LYS n 
5  116 ALA n 
5  117 GLN n 
5  118 LYS n 
5  119 ASN n 
5  120 THR n 
5  121 GLN n 
5  122 SER n 
5  123 TYR n 
5  124 GLY n 
5  125 GLY n 
5  126 ARG n 
5  127 PRO n 
5  128 TYR n 
5  129 GLY n 
5  130 VAL n 
5  131 GLY n 
5  132 LEU n 
5  133 LEU n 
5  134 ILE n 
5  135 ILE n 
5  136 GLY n 
5  137 TYR n 
5  138 ASP n 
5  139 LYS n 
5  140 SER n 
5  141 GLY n 
5  142 ALA n 
5  143 HIS n 
5  144 LEU n 
5  145 LEU n 
5  146 GLU n 
5  147 PHE n 
5  148 GLN n 
5  149 PRO n 
5  150 SER n 
5  151 GLY n 
5  152 ASN n 
5  153 VAL n 
5  154 THR n 
5  155 GLU n 
5  156 LEU n 
5  157 TYR n 
5  158 GLY n 
5  159 THR n 
5  160 ALA n 
5  161 ILE n 
5  162 GLY n 
5  163 ALA n 
5  164 ARG n 
5  165 SER n 
5  166 GLN n 
5  167 GLY n 
5  168 ALA n 
5  169 LYS n 
5  170 THR n 
5  171 TYR n 
5  172 LEU n 
5  173 GLU n 
5  174 ARG n 
5  175 THR n 
5  176 LEU n 
5  177 ASP n 
5  178 THR n 
5  179 PHE n 
5  180 ILE n 
5  181 LYS n 
5  182 ILE n 
5  183 ASP n 
5  184 GLY n 
5  185 ASN n 
5  186 PRO n 
5  187 ASP n 
5  188 GLU n 
5  189 LEU n 
5  190 ILE n 
5  191 LYS n 
5  192 ALA n 
5  193 GLY n 
5  194 VAL n 
5  195 GLU n 
5  196 ALA n 
5  197 ILE n 
5  198 SER n 
5  199 GLN n 
5  200 SER n 
5  201 LEU n 
5  202 ARG n 
5  203 ASP n 
5  204 GLU n 
5  205 SER n 
5  206 LEU n 
5  207 THR n 
5  208 VAL n 
5  209 ASP n 
5  210 ASN n 
5  211 LEU n 
5  212 SER n 
5  213 ILE n 
5  214 ALA n 
5  215 ILE n 
5  216 VAL n 
5  217 GLY n 
5  218 LYS n 
5  219 ASP n 
5  220 THR n 
5  221 PRO n 
5  222 PHE n 
5  223 THR n 
5  224 ILE n 
5  225 TYR n 
5  226 ASP n 
5  227 GLY n 
5  228 GLU n 
5  229 ALA n 
5  230 VAL n 
5  231 ALA n 
5  232 LYS n 
5  233 TYR n 
5  234 ILE n 
6  1   MET n 
6  2   THR n 
6  3   SER n 
6  4   ILE n 
6  5   GLY n 
6  6   THR n 
6  7   GLY n 
6  8   TYR n 
6  9   ASP n 
6  10  LEU n 
6  11  SER n 
6  12  ASN n 
6  13  SER n 
6  14  VAL n 
6  15  PHE n 
6  16  SER n 
6  17  PRO n 
6  18  ASP n 
6  19  GLY n 
6  20  ARG n 
6  21  ASN n 
6  22  PHE n 
6  23  GLN n 
6  24  VAL n 
6  25  GLU n 
6  26  TYR n 
6  27  ALA n 
6  28  VAL n 
6  29  LYS n 
6  30  ALA n 
6  31  VAL n 
6  32  GLU n 
6  33  ASN n 
6  34  GLY n 
6  35  THR n 
6  36  THR n 
6  37  SER n 
6  38  ILE n 
6  39  GLY n 
6  40  ILE n 
6  41  LYS n 
6  42  CYS n 
6  43  ASN n 
6  44  ASP n 
6  45  GLY n 
6  46  VAL n 
6  47  VAL n 
6  48  PHE n 
6  49  ALA n 
6  50  VAL n 
6  51  GLU n 
6  52  LYS n 
6  53  LEU n 
6  54  ILE n 
6  55  THR n 
6  56  SER n 
6  57  LYS n 
6  58  LEU n 
6  59  LEU n 
6  60  VAL n 
6  61  PRO n 
6  62  GLN n 
6  63  LYS n 
6  64  ASN n 
6  65  VAL n 
6  66  LYS n 
6  67  ILE n 
6  68  GLN n 
6  69  VAL n 
6  70  VAL n 
6  71  ASP n 
6  72  ARG n 
6  73  HIS n 
6  74  ILE n 
6  75  GLY n 
6  76  CYS n 
6  77  VAL n 
6  78  TYR n 
6  79  SER n 
6  80  GLY n 
6  81  LEU n 
6  82  ILE n 
6  83  PRO n 
6  84  ASP n 
6  85  GLY n 
6  86  ARG n 
6  87  HIS n 
6  88  LEU n 
6  89  VAL n 
6  90  ASN n 
6  91  ARG n 
6  92  GLY n 
6  93  ARG n 
6  94  GLU n 
6  95  GLU n 
6  96  ALA n 
6  97  ALA n 
6  98  SER n 
6  99  PHE n 
6  100 LYS n 
6  101 LYS n 
6  102 LEU n 
6  103 TYR n 
6  104 LYS n 
6  105 THR n 
6  106 PRO n 
6  107 ILE n 
6  108 PRO n 
6  109 ILE n 
6  110 PRO n 
6  111 ALA n 
6  112 PHE n 
6  113 ALA n 
6  114 ASP n 
6  115 ARG n 
6  116 LEU n 
6  117 GLY n 
6  118 GLN n 
6  119 TYR n 
6  120 VAL n 
6  121 GLN n 
6  122 ALA n 
6  123 HIS n 
6  124 THR n 
6  125 LEU n 
6  126 TYR n 
6  127 ASN n 
6  128 SER n 
6  129 VAL n 
6  130 ARG n 
6  131 PRO n 
6  132 PHE n 
6  133 GLY n 
6  134 VAL n 
6  135 SER n 
6  136 THR n 
6  137 ILE n 
6  138 PHE n 
6  139 GLY n 
6  140 GLY n 
6  141 VAL n 
6  142 ASP n 
6  143 LYS n 
6  144 ASN n 
6  145 GLY n 
6  146 ALA n 
6  147 HIS n 
6  148 LEU n 
6  149 TYR n 
6  150 MET n 
6  151 LEU n 
6  152 GLU n 
6  153 PRO n 
6  154 SER n 
6  155 GLY n 
6  156 SER n 
6  157 TYR n 
6  158 TRP n 
6  159 GLY n 
6  160 TYR n 
6  161 LYS n 
6  162 GLY n 
6  163 ALA n 
6  164 ALA n 
6  165 THR n 
6  166 GLY n 
6  167 LYS n 
6  168 GLY n 
6  169 ARG n 
6  170 GLN n 
6  171 SER n 
6  172 ALA n 
6  173 LYS n 
6  174 ALA n 
6  175 GLU n 
6  176 LEU n 
6  177 GLU n 
6  178 LYS n 
6  179 LEU n 
6  180 VAL n 
6  181 ASP n 
6  182 HIS n 
6  183 HIS n 
6  184 PRO n 
6  185 GLU n 
6  186 GLY n 
6  187 LEU n 
6  188 SER n 
6  189 ALA n 
6  190 ARG n 
6  191 GLU n 
6  192 ALA n 
6  193 VAL n 
6  194 LYS n 
6  195 GLN n 
6  196 ALA n 
6  197 ALA n 
6  198 LYS n 
6  199 ILE n 
6  200 ILE n 
6  201 TYR n 
6  202 LEU n 
6  203 ALA n 
6  204 HIS n 
6  205 GLU n 
6  206 ASP n 
6  207 ASN n 
6  208 LYS n 
6  209 GLU n 
6  210 LYS n 
6  211 ASP n 
6  212 PHE n 
6  213 GLU n 
6  214 LEU n 
6  215 GLU n 
6  216 ILE n 
6  217 SER n 
6  218 TRP n 
6  219 CYS n 
6  220 SER n 
6  221 LEU n 
6  222 SER n 
6  223 GLU n 
6  224 THR n 
6  225 ASN n 
6  226 GLY n 
6  227 LEU n 
6  228 HIS n 
6  229 LYS n 
6  230 PHE n 
6  231 VAL n 
6  232 LYS n 
6  233 GLY n 
6  234 ASP n 
6  235 LEU n 
6  236 LEU n 
6  237 GLN n 
6  238 GLU n 
6  239 ALA n 
6  240 ILE n 
6  241 ASP n 
6  242 PHE n 
6  243 ALA n 
6  244 GLN n 
6  245 LYS n 
6  246 GLU n 
6  247 ILE n 
6  248 ASN n 
6  249 GLY n 
6  250 ASP n 
6  251 ASP n 
6  252 ASP n 
6  253 GLU n 
6  254 ASP n 
6  255 GLU n 
6  256 ASP n 
6  257 ASP n 
6  258 SER n 
6  259 ASP n 
6  260 ASN n 
6  261 VAL n 
6  262 MET n 
6  263 SER n 
6  264 SER n 
6  265 ASP n 
6  266 ASP n 
6  267 GLU n 
6  268 ASN n 
6  269 ALA n 
6  270 PRO n 
6  271 VAL n 
6  272 ALA n 
6  273 THR n 
6  274 ASN n 
6  275 ALA n 
6  276 ASN n 
6  277 ALA n 
6  278 THR n 
6  279 THR n 
6  280 ASP n 
6  281 GLN n 
6  282 GLU n 
6  283 GLY n 
6  284 ASP n 
6  285 ILE n 
6  286 HIS n 
6  287 LEU n 
6  288 GLU n 
7  1   MET n 
7  2   SER n 
7  3   GLY n 
7  4   ALA n 
7  5   ALA n 
7  6   ALA n 
7  7   ALA n 
7  8   SER n 
7  9   ALA n 
7  10  ALA n 
7  11  GLY n 
7  12  TYR n 
7  13  ASP n 
7  14  ARG n 
7  15  HIS n 
7  16  ILE n 
7  17  THR n 
7  18  ILE n 
7  19  PHE n 
7  20  SER n 
7  21  PRO n 
7  22  GLU n 
7  23  GLY n 
7  24  ARG n 
7  25  LEU n 
7  26  TYR n 
7  27  GLN n 
7  28  VAL n 
7  29  GLU n 
7  30  TYR n 
7  31  ALA n 
7  32  PHE n 
7  33  LYS n 
7  34  ALA n 
7  35  THR n 
7  36  ASN n 
7  37  GLN n 
7  38  THR n 
7  39  ASN n 
7  40  ILE n 
7  41  ASN n 
7  42  SER n 
7  43  LEU n 
7  44  ALA n 
7  45  VAL n 
7  46  ARG n 
7  47  GLY n 
7  48  LYS n 
7  49  ASP n 
7  50  CYS n 
7  51  THR n 
7  52  VAL n 
7  53  VAL n 
7  54  ILE n 
7  55  SER n 
7  56  GLN n 
7  57  LYS n 
7  58  LYS n 
7  59  VAL n 
7  60  PRO n 
7  61  ASP n 
7  62  LYS n 
7  63  LEU n 
7  64  LEU n 
7  65  ASP n 
7  66  PRO n 
7  67  THR n 
7  68  THR n 
7  69  VAL n 
7  70  SER n 
7  71  TYR n 
7  72  ILE n 
7  73  PHE n 
7  74  CYS n 
7  75  ILE n 
7  76  SER n 
7  77  ARG n 
7  78  THR n 
7  79  ILE n 
7  80  GLY n 
7  81  MET n 
7  82  VAL n 
7  83  VAL n 
7  84  ASN n 
7  85  GLY n 
7  86  PRO n 
7  87  ILE n 
7  88  PRO n 
7  89  ASP n 
7  90  ALA n 
7  91  ARG n 
7  92  ASN n 
7  93  ALA n 
7  94  ALA n 
7  95  LEU n 
7  96  ARG n 
7  97  ALA n 
7  98  LYS n 
7  99  ALA n 
7  100 GLU n 
7  101 ALA n 
7  102 ALA n 
7  103 GLU n 
7  104 PHE n 
7  105 ARG n 
7  106 TYR n 
7  107 LYS n 
7  108 TYR n 
7  109 GLY n 
7  110 TYR n 
7  111 ASP n 
7  112 MET n 
7  113 PRO n 
7  114 CYS n 
7  115 ASP n 
7  116 VAL n 
7  117 LEU n 
7  118 ALA n 
7  119 LYS n 
7  120 ARG n 
7  121 MET n 
7  122 ALA n 
7  123 ASN n 
7  124 LEU n 
7  125 SER n 
7  126 GLN n 
7  127 ILE n 
7  128 TYR n 
7  129 THR n 
7  130 GLN n 
7  131 ARG n 
7  132 ALA n 
7  133 TYR n 
7  134 MET n 
7  135 ARG n 
7  136 PRO n 
7  137 LEU n 
7  138 GLY n 
7  139 VAL n 
7  140 ILE n 
7  141 LEU n 
7  142 THR n 
7  143 PHE n 
7  144 VAL n 
7  145 SER n 
7  146 VAL n 
7  147 ASP n 
7  148 GLU n 
7  149 GLU n 
7  150 LEU n 
7  151 GLY n 
7  152 PRO n 
7  153 SER n 
7  154 ILE n 
7  155 TYR n 
7  156 LYS n 
7  157 THR n 
7  158 ASP n 
7  159 PRO n 
7  160 ALA n 
7  161 GLY n 
7  162 TYR n 
7  163 TYR n 
7  164 VAL n 
7  165 GLY n 
7  166 TYR n 
7  167 LYS n 
7  168 ALA n 
7  169 THR n 
7  170 ALA n 
7  171 THR n 
7  172 GLY n 
7  173 PRO n 
7  174 LYS n 
7  175 GLN n 
7  176 GLN n 
7  177 GLU n 
7  178 ILE n 
7  179 THR n 
7  180 THR n 
7  181 ASN n 
7  182 LEU n 
7  183 GLU n 
7  184 ASN n 
7  185 HIS n 
7  186 PHE n 
7  187 LYS n 
7  188 LYS n 
7  189 SER n 
7  190 LYS n 
7  191 ILE n 
7  192 ASP n 
7  193 HIS n 
7  194 ILE n 
7  195 ASN n 
7  196 GLU n 
7  197 GLU n 
7  198 SER n 
7  199 TRP n 
7  200 GLU n 
7  201 LYS n 
7  202 VAL n 
7  203 VAL n 
7  204 GLU n 
7  205 PHE n 
7  206 ALA n 
7  207 ILE n 
7  208 THR n 
7  209 HIS n 
7  210 MET n 
7  211 ILE n 
7  212 ASP n 
7  213 ALA n 
7  214 LEU n 
7  215 GLY n 
7  216 THR n 
7  217 GLU n 
7  218 PHE n 
7  219 SER n 
7  220 LYS n 
7  221 ASN n 
7  222 ASP n 
7  223 LEU n 
7  224 GLU n 
7  225 VAL n 
7  226 GLY n 
7  227 VAL n 
7  228 ALA n 
7  229 THR n 
7  230 LYS n 
7  231 ASP n 
7  232 LYS n 
7  233 PHE n 
7  234 PHE n 
7  235 THR n 
7  236 LEU n 
7  237 SER n 
7  238 ALA n 
7  239 GLU n 
7  240 ASN n 
7  241 ILE n 
7  242 GLU n 
7  243 GLU n 
7  244 ARG n 
7  245 LEU n 
7  246 VAL n 
7  247 ALA n 
7  248 ILE n 
7  249 ALA n 
7  250 GLU n 
7  251 GLN n 
7  252 ASP n 
8  1   THR n 
8  2   ILE n 
8  3   VAL n 
8  4   GLY n 
8  5   VAL n 
8  6   LYS n 
8  7   PHE n 
8  8   ASN n 
8  9   ASN n 
8  10  GLY n 
8  11  VAL n 
8  12  VAL n 
8  13  ILE n 
8  14  ALA n 
8  15  ALA n 
8  16  ASP n 
8  17  THR n 
8  18  ARG n 
8  19  SER n 
8  20  THR n 
8  21  GLN n 
8  22  GLY n 
8  23  PRO n 
8  24  ILE n 
8  25  VAL n 
8  26  ALA n 
8  27  ASP n 
8  28  LYS n 
8  29  ASN n 
8  30  CYS n 
8  31  ALA n 
8  32  LYS n 
8  33  LEU n 
8  34  HIS n 
8  35  ARG n 
8  36  ILE n 
8  37  SER n 
8  38  PRO n 
8  39  LYS n 
8  40  ILE n 
8  41  TRP n 
8  42  CYS n 
8  43  ALA n 
8  44  GLY n 
8  45  ALA n 
8  46  GLY n 
8  47  THR n 
8  48  ALA n 
8  49  ALA n 
8  50  ASP n 
8  51  THR n 
8  52  GLU n 
8  53  ALA n 
8  54  VAL n 
8  55  THR n 
8  56  GLN n 
8  57  LEU n 
8  58  ILE n 
8  59  GLY n 
8  60  SER n 
8  61  ASN n 
8  62  ILE n 
8  63  GLU n 
8  64  LEU n 
8  65  HIS n 
8  66  SER n 
8  67  LEU n 
8  68  TYR n 
8  69  THR n 
8  70  SER n 
8  71  ARG n 
8  72  GLU n 
8  73  PRO n 
8  74  ARG n 
8  75  VAL n 
8  76  VAL n 
8  77  SER n 
8  78  ALA n 
8  79  LEU n 
8  80  GLN n 
8  81  MET n 
8  82  LEU n 
8  83  LYS n 
8  84  GLN n 
8  85  HIS n 
8  86  LEU n 
8  87  PHE n 
8  88  LYS n 
8  89  TYR n 
8  90  GLN n 
8  91  GLY n 
8  92  HIS n 
8  93  ILE n 
8  94  GLY n 
8  95  ALA n 
8  96  TYR n 
8  97  LEU n 
8  98  ILE n 
8  99  VAL n 
8  100 ALA n 
8  101 GLY n 
8  102 VAL n 
8  103 ASP n 
8  104 PRO n 
8  105 THR n 
8  106 GLY n 
8  107 SER n 
8  108 HIS n 
8  109 LEU n 
8  110 PHE n 
8  111 SER n 
8  112 ILE n 
8  113 HIS n 
8  114 ALA n 
8  115 HIS n 
8  116 GLY n 
8  117 SER n 
8  118 THR n 
8  119 ASP n 
8  120 VAL n 
8  121 GLY n 
8  122 TYR n 
8  123 TYR n 
8  124 LEU n 
8  125 SER n 
8  126 LEU n 
8  127 GLY n 
8  128 SER n 
8  129 GLY n 
8  130 SER n 
8  131 LEU n 
8  132 ALA n 
8  133 ALA n 
8  134 MET n 
8  135 ALA n 
8  136 VAL n 
8  137 LEU n 
8  138 GLU n 
8  139 SER n 
8  140 HIS n 
8  141 TRP n 
8  142 LYS n 
8  143 GLN n 
8  144 ASP n 
8  145 LEU n 
8  146 THR n 
8  147 LYS n 
8  148 GLU n 
8  149 GLU n 
8  150 ALA n 
8  151 ILE n 
8  152 LYS n 
8  153 LEU n 
8  154 ALA n 
8  155 SER n 
8  156 ASP n 
8  157 ALA n 
8  158 ILE n 
8  159 GLN n 
8  160 ALA n 
8  161 GLY n 
8  162 ILE n 
8  163 TRP n 
8  164 ASN n 
8  165 ASP n 
8  166 LEU n 
8  167 GLY n 
8  168 SER n 
8  169 GLY n 
8  170 SER n 
8  171 ASN n 
8  172 VAL n 
8  173 ASP n 
8  174 VAL n 
8  175 CYS n 
8  176 VAL n 
8  177 MET n 
8  178 GLU n 
8  179 ILE n 
8  180 GLY n 
8  181 LYS n 
8  182 ASP n 
8  183 ALA n 
8  184 GLU n 
8  185 TYR n 
8  186 LEU n 
8  187 ARG n 
8  188 ASN n 
8  189 TYR n 
8  190 LEU n 
8  191 THR n 
8  192 PRO n 
8  193 ASN n 
8  194 VAL n 
8  195 ARG n 
8  196 GLU n 
8  197 GLU n 
8  198 LYS n 
8  199 GLN n 
8  200 LYS n 
8  201 SER n 
8  202 TYR n 
8  203 LYS n 
8  204 PHE n 
8  205 PRO n 
8  206 ARG n 
8  207 GLY n 
8  208 THR n 
8  209 THR n 
8  210 ALA n 
8  211 VAL n 
8  212 LEU n 
8  213 LYS n 
8  214 GLU n 
8  215 SER n 
8  216 ILE n 
8  217 VAL n 
8  218 ASN n 
8  219 ILE n 
8  220 CYS n 
8  221 ASP n 
8  222 ILE n 
8  223 GLN n 
8  224 GLU n 
8  225 GLU n 
8  226 GLN n 
8  227 VAL n 
8  228 ASP n 
8  229 ILE n 
8  230 THR n 
8  231 ALA n 
9  1   MET n 
9  2   SER n 
9  3   ASP n 
9  4   PRO n 
9  5   SER n 
9  6   SER n 
9  7   ILE n 
9  8   ASN n 
9  9   GLY n 
9  10  GLY n 
9  11  ILE n 
9  12  VAL n 
9  13  VAL n 
9  14  ALA n 
9  15  MET n 
9  16  THR n 
9  17  GLY n 
9  18  LYS n 
9  19  ASP n 
9  20  CYS n 
9  21  VAL n 
9  22  ALA n 
9  23  ILE n 
9  24  ALA n 
9  25  CYS n 
9  26  ASP n 
9  27  LEU n 
9  28  ARG n 
9  29  LEU n 
9  30  GLY n 
9  31  SER n 
9  32  GLN n 
9  33  SER n 
9  34  LEU n 
9  35  GLY n 
9  36  VAL n 
9  37  SER n 
9  38  ASN n 
9  39  LYS n 
9  40  PHE n 
9  41  GLU n 
9  42  LYS n 
9  43  ILE n 
9  44  PHE n 
9  45  HIS n 
9  46  TYR n 
9  47  GLY n 
9  48  HIS n 
9  49  VAL n 
9  50  PHE n 
9  51  LEU n 
9  52  GLY n 
9  53  ILE n 
9  54  THR n 
9  55  GLY n 
9  56  LEU n 
9  57  ALA n 
9  58  THR n 
9  59  ASP n 
9  60  VAL n 
9  61  THR n 
9  62  THR n 
9  63  LEU n 
9  64  ASN n 
9  65  GLU n 
9  66  MET n 
9  67  PHE n 
9  68  ARG n 
9  69  TYR n 
9  70  LYS n 
9  71  THR n 
9  72  ASN n 
9  73  LEU n 
9  74  TYR n 
9  75  LYS n 
9  76  LEU n 
9  77  LYS n 
9  78  GLU n 
9  79  GLU n 
9  80  ARG n 
9  81  ALA n 
9  82  ILE n 
9  83  GLU n 
9  84  PRO n 
9  85  GLU n 
9  86  THR n 
9  87  PHE n 
9  88  THR n 
9  89  GLN n 
9  90  LEU n 
9  91  VAL n 
9  92  SER n 
9  93  SER n 
9  94  SER n 
9  95  LEU n 
9  96  TYR n 
9  97  GLU n 
9  98  ARG n 
9  99  ARG n 
9  100 PHE n 
9  101 GLY n 
9  102 PRO n 
9  103 TYR n 
9  104 PHE n 
9  105 VAL n 
9  106 GLY n 
9  107 PRO n 
9  108 VAL n 
9  109 VAL n 
9  110 ALA n 
9  111 GLY n 
9  112 ILE n 
9  113 ASN n 
9  114 SER n 
9  115 LYS n 
9  116 SER n 
9  117 GLY n 
9  118 LYS n 
9  119 PRO n 
9  120 PHE n 
9  121 ILE n 
9  122 ALA n 
9  123 GLY n 
9  124 PHE n 
9  125 ASP n 
9  126 LEU n 
9  127 ILE n 
9  128 GLY n 
9  129 CYS n 
9  130 ILE n 
9  131 ASP n 
9  132 GLU n 
9  133 ALA n 
9  134 LYS n 
9  135 ASP n 
9  136 PHE n 
9  137 ILE n 
9  138 VAL n 
9  139 SER n 
9  140 GLY n 
9  141 THR n 
9  142 ALA n 
9  143 SER n 
9  144 ASP n 
9  145 GLN n 
9  146 LEU n 
9  147 PHE n 
9  148 GLY n 
9  149 MET n 
9  150 CYS n 
9  151 GLU n 
9  152 SER n 
9  153 LEU n 
9  154 TYR n 
9  155 GLU n 
9  156 PRO n 
9  157 ASN n 
9  158 LEU n 
9  159 GLU n 
9  160 PRO n 
9  161 GLU n 
9  162 ASP n 
9  163 LEU n 
9  164 PHE n 
9  165 GLU n 
9  166 THR n 
9  167 ILE n 
9  168 SER n 
9  169 GLN n 
9  170 ALA n 
9  171 LEU n 
9  172 LEU n 
9  173 ASN n 
9  174 ALA n 
9  175 ALA n 
9  176 ASP n 
9  177 ARG n 
9  178 ASP n 
9  179 ALA n 
9  180 LEU n 
9  181 SER n 
9  182 GLY n 
9  183 TRP n 
9  184 GLY n 
9  185 ALA n 
9  186 VAL n 
9  187 VAL n 
9  188 TYR n 
9  189 ILE n 
9  190 ILE n 
9  191 LYS n 
9  192 LYS n 
9  193 ASP n 
9  194 GLU n 
9  195 VAL n 
9  196 VAL n 
9  197 LYS n 
9  198 ARG n 
9  199 TYR n 
9  200 LEU n 
9  201 LYS n 
9  202 MET n 
9  203 ARG n 
9  204 GLN n 
9  205 ASP n 
10 1   MET n 
10 2   ASP n 
10 3   ILE n 
10 4   ILE n 
10 5   LEU n 
10 6   GLY n 
10 7   ILE n 
10 8   ARG n 
10 9   VAL n 
10 10  GLN n 
10 11  ASP n 
10 12  SER n 
10 13  VAL n 
10 14  ILE n 
10 15  LEU n 
10 16  ALA n 
10 17  SER n 
10 18  SER n 
10 19  LYS n 
10 20  ALA n 
10 21  VAL n 
10 22  THR n 
10 23  ARG n 
10 24  GLY n 
10 25  ILE n 
10 26  SER n 
10 27  VAL n 
10 28  LEU n 
10 29  LYS n 
10 30  ASP n 
10 31  SER n 
10 32  ASP n 
10 33  ASP n 
10 34  LYS n 
10 35  THR n 
10 36  ARG n 
10 37  GLN n 
10 38  LEU n 
10 39  SER n 
10 40  PRO n 
10 41  HIS n 
10 42  THR n 
10 43  LEU n 
10 44  MET n 
10 45  SER n 
10 46  PHE n 
10 47  ALA n 
10 48  GLY n 
10 49  GLU n 
10 50  ALA n 
10 51  GLY n 
10 52  ASP n 
10 53  THR n 
10 54  VAL n 
10 55  GLN n 
10 56  PHE n 
10 57  ALA n 
10 58  GLU n 
10 59  TYR n 
10 60  ILE n 
10 61  GLN n 
10 62  ALA n 
10 63  ASN n 
10 64  ILE n 
10 65  GLN n 
10 66  LEU n 
10 67  TYR n 
10 68  SER n 
10 69  ILE n 
10 70  ARG n 
10 71  GLU n 
10 72  ASP n 
10 73  TYR n 
10 74  GLU n 
10 75  LEU n 
10 76  SER n 
10 77  PRO n 
10 78  GLN n 
10 79  ALA n 
10 80  VAL n 
10 81  SER n 
10 82  SER n 
10 83  PHE n 
10 84  VAL n 
10 85  ARG n 
10 86  GLN n 
10 87  GLU n 
10 88  LEU n 
10 89  ALA n 
10 90  LYS n 
10 91  SER n 
10 92  ILE n 
10 93  ARG n 
10 94  SER n 
10 95  ARG n 
10 96  ARG n 
10 97  PRO n 
10 98  TYR n 
10 99  GLN n 
10 100 VAL n 
10 101 ASN n 
10 102 VAL n 
10 103 LEU n 
10 104 ILE n 
10 105 GLY n 
10 106 GLY n 
10 107 TYR n 
10 108 ASP n 
10 109 LYS n 
10 110 LYS n 
10 111 LYS n 
10 112 ASN n 
10 113 LYS n 
10 114 PRO n 
10 115 GLU n 
10 116 LEU n 
10 117 TYR n 
10 118 GLN n 
10 119 ILE n 
10 120 ASP n 
10 121 TYR n 
10 122 LEU n 
10 123 GLY n 
10 124 THR n 
10 125 LYS n 
10 126 VAL n 
10 127 GLU n 
10 128 LEU n 
10 129 PRO n 
10 130 TYR n 
10 131 GLY n 
10 132 ALA n 
10 133 HIS n 
10 134 GLY n 
10 135 TYR n 
10 136 SER n 
10 137 GLY n 
10 138 PHE n 
10 139 TYR n 
10 140 THR n 
10 141 PHE n 
10 142 SER n 
10 143 LEU n 
10 144 LEU n 
10 145 ASP n 
10 146 HIS n 
10 147 HIS n 
10 148 TYR n 
10 149 ARG n 
10 150 PRO n 
10 151 ASP n 
10 152 MET n 
10 153 THR n 
10 154 THR n 
10 155 GLU n 
10 156 GLU n 
10 157 GLY n 
10 158 LEU n 
10 159 ASP n 
10 160 LEU n 
10 161 LEU n 
10 162 LYS n 
10 163 LEU n 
10 164 CYS n 
10 165 VAL n 
10 166 GLN n 
10 167 GLU n 
10 168 LEU n 
10 169 GLU n 
10 170 LYS n 
10 171 ARG n 
10 172 MET n 
10 173 PRO n 
10 174 MET n 
10 175 ASP n 
10 176 PHE n 
10 177 LYS n 
10 178 GLY n 
10 179 VAL n 
10 180 ILE n 
10 181 VAL n 
10 182 LYS n 
10 183 ILE n 
10 184 VAL n 
10 185 ASP n 
10 186 LYS n 
10 187 ASP n 
10 188 GLY n 
10 189 ILE n 
10 190 ARG n 
10 191 GLN n 
10 192 VAL n 
10 193 ASP n 
10 194 ASP n 
10 195 PHE n 
10 196 GLN n 
10 197 ALA n 
10 198 GLN n 
11 1   THR n 
11 2   THR n 
11 3   LEU n 
11 4   ALA n 
11 5   PHE n 
11 6   ARG n 
11 7   PHE n 
11 8   GLN n 
11 9   GLY n 
11 10  GLY n 
11 11  ILE n 
11 12  ILE n 
11 13  VAL n 
11 14  ALA n 
11 15  VAL n 
11 16  ASP n 
11 17  SER n 
11 18  ARG n 
11 19  ALA n 
11 20  THR n 
11 21  ALA n 
11 22  GLY n 
11 23  ASN n 
11 24  TRP n 
11 25  VAL n 
11 26  ALA n 
11 27  SER n 
11 28  GLN n 
11 29  THR n 
11 30  VAL n 
11 31  LYS n 
11 32  LYS n 
11 33  VAL n 
11 34  ILE n 
11 35  GLU n 
11 36  ILE n 
11 37  ASN n 
11 38  PRO n 
11 39  PHE n 
11 40  LEU n 
11 41  LEU n 
11 42  GLY n 
11 43  THR n 
11 44  MET n 
11 45  ALA n 
11 46  GLY n 
11 47  GLY n 
11 48  ALA n 
11 49  ALA n 
11 50  ASP n 
11 51  CYS n 
11 52  GLN n 
11 53  PHE n 
11 54  TRP n 
11 55  GLU n 
11 56  THR n 
11 57  TRP n 
11 58  LEU n 
11 59  GLY n 
11 60  SER n 
11 61  GLN n 
11 62  CYS n 
11 63  ARG n 
11 64  LEU n 
11 65  HIS n 
11 66  GLU n 
11 67  LEU n 
11 68  ARG n 
11 69  GLU n 
11 70  LYS n 
11 71  GLU n 
11 72  ARG n 
11 73  ILE n 
11 74  SER n 
11 75  VAL n 
11 76  ALA n 
11 77  ALA n 
11 78  ALA n 
11 79  SER n 
11 80  LYS n 
11 81  ILE n 
11 82  LEU n 
11 83  SER n 
11 84  ASN n 
11 85  LEU n 
11 86  VAL n 
11 87  TYR n 
11 88  GLN n 
11 89  TYR n 
11 90  LYS n 
11 91  GLY n 
11 92  ALA n 
11 93  GLY n 
11 94  LEU n 
11 95  SER n 
11 96  MET n 
11 97  GLY n 
11 98  THR n 
11 99  MET n 
11 100 ILE n 
11 101 CYS n 
11 102 GLY n 
11 103 TYR n 
11 104 THR n 
11 105 ARG n 
11 106 LYS n 
11 107 GLU n 
11 108 GLY n 
11 109 PRO n 
11 110 THR n 
11 111 ILE n 
11 112 TYR n 
11 113 TYR n 
11 114 VAL n 
11 115 ASP n 
11 116 SER n 
11 117 ASP n 
11 118 GLY n 
11 119 THR n 
11 120 ARG n 
11 121 LEU n 
11 122 LYS n 
11 123 GLY n 
11 124 ASP n 
11 125 ILE n 
11 126 PHE n 
11 127 CYS n 
11 128 VAL n 
11 129 GLY n 
11 130 SER n 
11 131 GLY n 
11 132 GLN n 
11 133 THR n 
11 134 PHE n 
11 135 ALA n 
11 136 TYR n 
11 137 GLY n 
11 138 VAL n 
11 139 LEU n 
11 140 ASP n 
11 141 SER n 
11 142 ASN n 
11 143 TYR n 
11 144 LYS n 
11 145 TRP n 
11 146 ASP n 
11 147 LEU n 
11 148 SER n 
11 149 VAL n 
11 150 GLU n 
11 151 ASP n 
11 152 ALA n 
11 153 LEU n 
11 154 TYR n 
11 155 LEU n 
11 156 GLY n 
11 157 LYS n 
11 158 ARG n 
11 159 SER n 
11 160 ILE n 
11 161 LEU n 
11 162 ALA n 
11 163 ALA n 
11 164 ALA n 
11 165 HIS n 
11 166 ARG n 
11 167 ASP n 
11 168 ALA n 
11 169 TYR n 
11 170 SER n 
11 171 GLY n 
11 172 GLY n 
11 173 SER n 
11 174 VAL n 
11 175 ASN n 
11 176 LEU n 
11 177 TYR n 
11 178 HIS n 
11 179 VAL n 
11 180 THR n 
11 181 GLU n 
11 182 ASP n 
11 183 GLY n 
11 184 TRP n 
11 185 ILE n 
11 186 TYR n 
11 187 HIS n 
11 188 GLY n 
11 189 ASN n 
11 190 HIS n 
11 191 ASP n 
11 192 VAL n 
11 193 GLY n 
11 194 GLU n 
11 195 LEU n 
11 196 PHE n 
11 197 TRP n 
11 198 LYS n 
11 199 VAL n 
11 200 LYS n 
11 201 GLU n 
11 202 GLU n 
11 203 GLU n 
11 204 GLY n 
11 205 SER n 
11 206 PHE n 
11 207 ASN n 
11 208 ASN n 
11 209 VAL n 
11 210 ILE n 
11 211 GLY n 
12 1   GLN n 
12 2   PHE n 
12 3   ASN n 
12 4   PRO n 
12 5   TYR n 
12 6   GLY n 
12 7   ASP n 
12 8   ASN n 
12 9   GLY n 
12 10  GLY n 
12 11  THR n 
12 12  ILE n 
12 13  LEU n 
12 14  GLY n 
12 15  ILE n 
12 16  ALA n 
12 17  GLY n 
12 18  GLU n 
12 19  ASP n 
12 20  PHE n 
12 21  ALA n 
12 22  VAL n 
12 23  LEU n 
12 24  ALA n 
12 25  GLY n 
12 26  ASP n 
12 27  THR n 
12 28  ARG n 
12 29  ASN n 
12 30  ILE n 
12 31  THR n 
12 32  ASP n 
12 33  TYR n 
12 34  SER n 
12 35  ILE n 
12 36  ASN n 
12 37  SER n 
12 38  ARG n 
12 39  TYR n 
12 40  GLU n 
12 41  PRO n 
12 42  LYS n 
12 43  VAL n 
12 44  PHE n 
12 45  ASP n 
12 46  CYS n 
12 47  GLY n 
12 48  ASP n 
12 49  ASN n 
12 50  ILE n 
12 51  VAL n 
12 52  MET n 
12 53  SER n 
12 54  ALA n 
12 55  ASN n 
12 56  GLY n 
12 57  PHE n 
12 58  ALA n 
12 59  ALA n 
12 60  ASP n 
12 61  GLY n 
12 62  ASP n 
12 63  ALA n 
12 64  LEU n 
12 65  VAL n 
12 66  LYS n 
12 67  ARG n 
12 68  PHE n 
12 69  LYS n 
12 70  ASN n 
12 71  SER n 
12 72  VAL n 
12 73  LYS n 
12 74  TRP n 
12 75  TYR n 
12 76  HIS n 
12 77  PHE n 
12 78  ASP n 
12 79  HIS n 
12 80  ASN n 
12 81  ASP n 
12 82  LYS n 
12 83  LYS n 
12 84  LEU n 
12 85  SER n 
12 86  ILE n 
12 87  ASN n 
12 88  SER n 
12 89  ALA n 
12 90  ALA n 
12 91  ARG n 
12 92  ASN n 
12 93  ILE n 
12 94  GLN n 
12 95  HIS n 
12 96  LEU n 
12 97  LEU n 
12 98  TYR n 
12 99  GLY n 
12 100 LYS n 
12 101 ARG n 
12 102 PHE n 
12 103 PHE n 
12 104 PRO n 
12 105 TYR n 
12 106 TYR n 
12 107 VAL n 
12 108 HIS n 
12 109 THR n 
12 110 ILE n 
12 111 ILE n 
12 112 ALA n 
12 113 GLY n 
12 114 LEU n 
12 115 ASP n 
12 116 GLU n 
12 117 ASP n 
12 118 GLY n 
12 119 LYS n 
12 120 GLY n 
12 121 ALA n 
12 122 VAL n 
12 123 TYR n 
12 124 SER n 
12 125 PHE n 
12 126 ASP n 
12 127 PRO n 
12 128 VAL n 
12 129 GLY n 
12 130 SER n 
12 131 TYR n 
12 132 GLU n 
12 133 ARG n 
12 134 GLU n 
12 135 GLN n 
12 136 CYS n 
12 137 ARG n 
12 138 ALA n 
12 139 GLY n 
12 140 GLY n 
12 141 ALA n 
12 142 ALA n 
12 143 ALA n 
12 144 SER n 
12 145 LEU n 
12 146 ILE n 
12 147 MET n 
12 148 PRO n 
12 149 PHE n 
12 150 LEU n 
12 151 ASP n 
12 152 ASN n 
12 153 GLN n 
12 154 VAL n 
12 155 ASN n 
12 156 PHE n 
12 157 LYS n 
12 158 ASN n 
12 159 GLN n 
12 160 TYR n 
12 161 GLU n 
12 162 PRO n 
12 163 GLY n 
12 164 THR n 
12 165 ASN n 
12 166 GLY n 
12 167 LYS n 
12 168 VAL n 
12 169 LYS n 
12 170 LYS n 
12 171 PRO n 
12 172 LEU n 
12 173 LYS n 
12 174 TYR n 
12 175 LEU n 
12 176 SER n 
12 177 VAL n 
12 178 GLU n 
12 179 GLU n 
12 180 VAL n 
12 181 ILE n 
12 182 LYS n 
12 183 LEU n 
12 184 VAL n 
12 185 ARG n 
12 186 ASP n 
12 187 SER n 
12 188 PHE n 
12 189 THR n 
12 190 SER n 
12 191 ALA n 
12 192 THR n 
12 193 GLU n 
12 194 ARG n 
12 195 HIS n 
12 196 ILE n 
12 197 GLN n 
12 198 VAL n 
12 199 GLY n 
12 200 ASP n 
12 201 GLY n 
12 202 LEU n 
12 203 GLU n 
12 204 ILE n 
12 205 LEU n 
12 206 ILE n 
12 207 VAL n 
12 208 THR n 
12 209 LYS n 
12 210 ASP n 
12 211 GLY n 
12 212 VAL n 
12 213 ARG n 
12 214 LYS n 
12 215 GLU n 
12 216 PHE n 
12 217 TYR n 
12 218 GLU n 
12 219 LEU n 
12 220 LYS n 
12 221 ARG n 
12 222 ASP n 
13 1   THR n 
13 2   GLN n 
13 3   ILE n 
13 4   ALA n 
13 5   ASN n 
13 6   ALA n 
13 7   GLY n 
13 8   ALA n 
13 9   SER n 
13 10  PRO n 
13 11  MET n 
13 12  VAL n 
13 13  ASN n 
13 14  THR n 
13 15  GLN n 
13 16  GLN n 
13 17  PRO n 
13 18  ILE n 
13 19  VAL n 
13 20  THR n 
13 21  GLY n 
13 22  THR n 
13 23  SER n 
13 24  VAL n 
13 25  ILE n 
13 26  SER n 
13 27  MET n 
13 28  LYS n 
13 29  TYR n 
13 30  ASP n 
13 31  ASN n 
13 32  GLY n 
13 33  VAL n 
13 34  ILE n 
13 35  ILE n 
13 36  ALA n 
13 37  ALA n 
13 38  ASP n 
13 39  ASN n 
13 40  LEU n 
13 41  GLY n 
13 42  SER n 
13 43  TYR n 
13 44  GLY n 
13 45  SER n 
13 46  LEU n 
13 47  LEU n 
13 48  ARG n 
13 49  PHE n 
13 50  ASN n 
13 51  GLY n 
13 52  VAL n 
13 53  GLU n 
13 54  ARG n 
13 55  LEU n 
13 56  ILE n 
13 57  PRO n 
13 58  VAL n 
13 59  GLY n 
13 60  ASP n 
13 61  ASN n 
13 62  THR n 
13 63  VAL n 
13 64  VAL n 
13 65  GLY n 
13 66  ILE n 
13 67  SER n 
13 68  GLY n 
13 69  ASP n 
13 70  ILE n 
13 71  SER n 
13 72  ASP n 
13 73  MET n 
13 74  GLN n 
13 75  HIS n 
13 76  ILE n 
13 77  GLU n 
13 78  ARG n 
13 79  LEU n 
13 80  LEU n 
13 81  LYS n 
13 82  ASP n 
13 83  LEU n 
13 84  VAL n 
13 85  THR n 
13 86  GLU n 
13 87  ASN n 
13 88  ALA n 
13 89  TYR n 
13 90  ASP n 
13 91  ASN n 
13 92  PRO n 
13 93  LEU n 
13 94  ALA n 
13 95  ASP n 
13 96  ALA n 
13 97  GLU n 
13 98  GLU n 
13 99  ALA n 
13 100 LEU n 
13 101 GLU n 
13 102 PRO n 
13 103 SER n 
13 104 TYR n 
13 105 ILE n 
13 106 PHE n 
13 107 GLU n 
13 108 TYR n 
13 109 LEU n 
13 110 ALA n 
13 111 THR n 
13 112 VAL n 
13 113 MET n 
13 114 TYR n 
13 115 GLN n 
13 116 ARG n 
13 117 ARG n 
13 118 SER n 
13 119 LYS n 
13 120 MET n 
13 121 ASN n 
13 122 PRO n 
13 123 LEU n 
13 124 TRP n 
13 125 ASN n 
13 126 ALA n 
13 127 ILE n 
13 128 ILE n 
13 129 VAL n 
13 130 ALA n 
13 131 GLY n 
13 132 VAL n 
13 133 GLN n 
13 134 SER n 
13 135 ASN n 
13 136 GLY n 
13 137 ASP n 
13 138 GLN n 
13 139 PHE n 
13 140 LEU n 
13 141 ARG n 
13 142 TYR n 
13 143 VAL n 
13 144 ASN n 
13 145 LEU n 
13 146 LEU n 
13 147 GLY n 
13 148 VAL n 
13 149 THR n 
13 150 TYR n 
13 151 SER n 
13 152 SER n 
13 153 PRO n 
13 154 THR n 
13 155 LEU n 
13 156 ALA n 
13 157 THR n 
13 158 GLY n 
13 159 PHE n 
13 160 GLY n 
13 161 ALA n 
13 162 HIS n 
13 163 MET n 
13 164 ALA n 
13 165 ASN n 
13 166 PRO n 
13 167 LEU n 
13 168 LEU n 
13 169 ARG n 
13 170 LYS n 
13 171 VAL n 
13 172 VAL n 
13 173 ASP n 
13 174 ARG n 
13 175 GLU n 
13 176 SER n 
13 177 ASP n 
13 178 ILE n 
13 179 PRO n 
13 180 LYS n 
13 181 THR n 
13 182 THR n 
13 183 VAL n 
13 184 GLN n 
13 185 VAL n 
13 186 ALA n 
13 187 GLU n 
13 188 GLU n 
13 189 ALA n 
13 190 ILE n 
13 191 VAL n 
13 192 ASN n 
13 193 ALA n 
13 194 MET n 
13 195 ARG n 
13 196 VAL n 
13 197 LEU n 
13 198 TYR n 
13 199 TYR n 
13 200 ARG n 
13 201 ASP n 
13 202 ALA n 
13 203 ARG n 
13 204 SER n 
13 205 SER n 
13 206 ARG n 
13 207 ASN n 
13 208 PHE n 
13 209 SER n 
13 210 LEU n 
13 211 ALA n 
13 212 ILE n 
13 213 ILE n 
13 214 ASP n 
13 215 LYS n 
13 216 ASN n 
13 217 THR n 
13 218 GLY n 
13 219 LEU n 
13 220 THR n 
13 221 PHE n 
13 222 LYS n 
13 223 LYS n 
13 224 ASN n 
13 225 LEU n 
13 226 GLN n 
13 227 VAL n 
13 228 GLU n 
13 229 ASN n 
13 230 MET n 
13 231 LYS n 
13 232 TRP n 
13 233 ASP n 
13 234 PHE n 
13 235 ALA n 
13 236 LYS n 
13 237 ASP n 
13 238 ILE n 
13 239 LYS n 
13 240 GLY n 
13 241 TYR n 
13 242 GLY n 
13 243 THR n 
13 244 GLN n 
13 245 LYS n 
13 246 ILE n 
14 1   THR n 
14 2   SER n 
14 3   ILE n 
14 4   MET n 
14 5   ALA n 
14 6   VAL n 
14 7   THR n 
14 8   PHE n 
14 9   LYS n 
14 10  ASP n 
14 11  GLY n 
14 12  VAL n 
14 13  ILE n 
14 14  LEU n 
14 15  GLY n 
14 16  ALA n 
14 17  ASP n 
14 18  SER n 
14 19  ARG n 
14 20  THR n 
14 21  THR n 
14 22  THR n 
14 23  GLY n 
14 24  ALA n 
14 25  TYR n 
14 26  ILE n 
14 27  ALA n 
14 28  ASN n 
14 29  ARG n 
14 30  VAL n 
14 31  THR n 
14 32  ASP n 
14 33  LYS n 
14 34  LEU n 
14 35  THR n 
14 36  ARG n 
14 37  VAL n 
14 38  HIS n 
14 39  ASP n 
14 40  LYS n 
14 41  ILE n 
14 42  TRP n 
14 43  CYS n 
14 44  CYS n 
14 45  ARG n 
14 46  SER n 
14 47  GLY n 
14 48  SER n 
14 49  ALA n 
14 50  ALA n 
14 51  ASP n 
14 52  THR n 
14 53  GLN n 
14 54  ALA n 
14 55  ILE n 
14 56  ALA n 
14 57  ASP n 
14 58  ILE n 
14 59  VAL n 
14 60  GLN n 
14 61  TYR n 
14 62  HIS n 
14 63  LEU n 
14 64  GLU n 
14 65  LEU n 
14 66  TYR n 
14 67  THR n 
14 68  SER n 
14 69  GLN n 
14 70  TYR n 
14 71  GLY n 
14 72  THR n 
14 73  PRO n 
14 74  SER n 
14 75  THR n 
14 76  GLU n 
14 77  THR n 
14 78  ALA n 
14 79  ALA n 
14 80  SER n 
14 81  VAL n 
14 82  PHE n 
14 83  LYS n 
14 84  GLU n 
14 85  LEU n 
14 86  CYS n 
14 87  TYR n 
14 88  GLU n 
14 89  ASN n 
14 90  LYS n 
14 91  ASP n 
14 92  ASN n 
14 93  LEU n 
14 94  THR n 
14 95  ALA n 
14 96  GLY n 
14 97  ILE n 
14 98  ILE n 
14 99  VAL n 
14 100 ALA n 
14 101 GLY n 
14 102 TYR n 
14 103 ASP n 
14 104 ASP n 
14 105 LYS n 
14 106 ASN n 
14 107 LYS n 
14 108 GLY n 
14 109 GLU n 
14 110 VAL n 
14 111 TYR n 
14 112 THR n 
14 113 ILE n 
14 114 PRO n 
14 115 LEU n 
14 116 GLY n 
14 117 GLY n 
14 118 SER n 
14 119 VAL n 
14 120 HIS n 
14 121 LYS n 
14 122 LEU n 
14 123 PRO n 
14 124 TYR n 
14 125 ALA n 
14 126 ILE n 
14 127 ALA n 
14 128 GLY n 
14 129 SER n 
14 130 GLY n 
14 131 SER n 
14 132 THR n 
14 133 PHE n 
14 134 ILE n 
14 135 TYR n 
14 136 GLY n 
14 137 TYR n 
14 138 CYS n 
14 139 ASP n 
14 140 LYS n 
14 141 ASN n 
14 142 PHE n 
14 143 ARG n 
14 144 GLU n 
14 145 ASN n 
14 146 MET n 
14 147 SER n 
14 148 LYS n 
14 149 GLU n 
14 150 GLU n 
14 151 THR n 
14 152 VAL n 
14 153 ASP n 
14 154 PHE n 
14 155 ILE n 
14 156 LYS n 
14 157 HIS n 
14 158 SER n 
14 159 LEU n 
14 160 SER n 
14 161 GLN n 
14 162 ALA n 
14 163 ILE n 
14 164 LYS n 
14 165 TRP n 
14 166 ASP n 
14 167 GLY n 
14 168 SER n 
14 169 SER n 
14 170 GLY n 
14 171 GLY n 
14 172 VAL n 
14 173 ILE n 
14 174 ARG n 
14 175 MET n 
14 176 VAL n 
14 177 VAL n 
14 178 LEU n 
14 179 THR n 
14 180 ALA n 
14 181 ALA n 
14 182 GLY n 
14 183 VAL n 
14 184 GLU n 
14 185 ARG n 
14 186 LEU n 
14 187 ILE n 
14 188 PHE n 
14 189 TYR n 
14 190 PRO n 
14 191 ASP n 
14 192 GLU n 
14 193 TYR n 
14 194 GLU n 
14 195 GLN n 
14 196 LEU n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1  1 sample 1 250 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2  1 sample 1 258 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3  1 sample 1 254 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4  1 sample 1 260 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5  1 sample 1 234 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
6  1 sample 1 288 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
7  1 sample 1 252 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
8  1 sample 1 231 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
9  1 sample 1 205 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
10 1 sample 1 198 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
11 1 sample 1 211 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
12 1 sample 1 222 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
13 1 sample 1 246 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
14 1 sample 1 196 
;brewer's yeast
;
'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H71 non-polymer         . 'sybactin derivative' 
;~{N}-[(2~{S},3~{R})-1-[[(4~{R},5~{S},8~{S})-4-[(2~{R},3~{S})-3-azanyl-4-oxidanylidene-butan-2-yl]oxy-2,7-bis(oxidanylidene)-5-(phenylmethyl)-1,6-diazacyclododec-8-yl]amino]-3-oxidanyl-1-oxidanylidene-butan-2-yl]hexanamide
;
'C31 H49 N5 O7'  603.750 
ALA   'L-peptide linking' y ALANINE               ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE              ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE            ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'       ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE              ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE             ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'       ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE               ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE             ? 'C6 H10 N3 O2 1' 156.162 
ILE   'L-peptide linking' y ISOLEUCINE            ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE               ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE            ? 'C5 H11 N O2 S'  149.211 
MG    non-polymer         . 'MAGNESIUM ION'       ? 'Mg 2'           24.305  
PHE   'L-peptide linking' y PHENYLALANINE         ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE               ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE             ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN            ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE              ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A  1  1   MET 1   1   1   MET MET A . n 
A  1  2   THR 2   2   2   THR THR A . n 
A  1  3   ASP 3   3   3   ASP ASP A . n 
A  1  4   ARG 4   4   4   ARG ARG A . n 
A  1  5   TYR 5   5   5   TYR TYR A . n 
A  1  6   SER 6   6   6   SER SER A . n 
A  1  7   PHE 7   7   7   PHE PHE A . n 
A  1  8   SER 8   8   8   SER SER A . n 
A  1  9   LEU 9   9   9   LEU LEU A . n 
A  1  10  THR 10  10  10  THR THR A . n 
A  1  11  THR 11  11  11  THR THR A . n 
A  1  12  PHE 12  12  12  PHE PHE A . n 
A  1  13  SER 13  13  13  SER SER A . n 
A  1  14  PRO 14  14  14  PRO PRO A . n 
A  1  15  SER 15  15  15  SER SER A . n 
A  1  16  GLY 16  16  16  GLY GLY A . n 
A  1  17  LYS 17  17  17  LYS LYS A . n 
A  1  18  LEU 18  18  18  LEU LEU A . n 
A  1  19  GLY 19  19  19  GLY GLY A . n 
A  1  20  GLN 20  20  20  GLN GLN A . n 
A  1  21  ILE 21  21  21  ILE ILE A . n 
A  1  22  ASP 22  22  22  ASP ASP A . n 
A  1  23  TYR 23  23  23  TYR TYR A . n 
A  1  24  ALA 24  24  24  ALA ALA A . n 
A  1  25  LEU 25  25  25  LEU LEU A . n 
A  1  26  THR 26  26  26  THR THR A . n 
A  1  27  ALA 27  27  27  ALA ALA A . n 
A  1  28  VAL 28  28  28  VAL VAL A . n 
A  1  29  LYS 29  29  29  LYS LYS A . n 
A  1  30  GLN 30  30  30  GLN GLN A . n 
A  1  31  GLY 31  31  31  GLY GLY A . n 
A  1  32  VAL 32  32  32  VAL VAL A . n 
A  1  33  THR 33  33  33  THR THR A . n 
A  1  34  SER 34  34  34  SER SER A . n 
A  1  35  LEU 35  35  35  LEU LEU A . n 
A  1  36  GLY 36  36  36  GLY GLY A . n 
A  1  37  ILE 37  37  37  ILE ILE A . n 
A  1  38  LYS 38  38  38  LYS LYS A . n 
A  1  39  ALA 39  39  39  ALA ALA A . n 
A  1  40  THR 40  40  40  THR THR A . n 
A  1  41  ASN 41  41  41  ASN ASN A . n 
A  1  42  GLY 42  42  42  GLY GLY A . n 
A  1  43  VAL 43  43  43  VAL VAL A . n 
A  1  44  VAL 44  44  44  VAL VAL A . n 
A  1  45  ILE 45  45  45  ILE ILE A . n 
A  1  46  ALA 46  46  46  ALA ALA A . n 
A  1  47  THR 47  47  47  THR THR A . n 
A  1  48  GLU 48  48  48  GLU GLU A . n 
A  1  49  LYS 49  49  49  LYS LYS A . n 
A  1  50  LYS 50  50  50  LYS LYS A . n 
A  1  51  SER 51  51  51  SER SER A . n 
A  1  52  SER 52  52  52  SER SER A . n 
A  1  53  SER 53  53  53  SER SER A . n 
A  1  54  PRO 54  54  54  PRO PRO A . n 
A  1  55  LEU 55  55  55  LEU LEU A . n 
A  1  56  ALA 56  56  56  ALA ALA A . n 
A  1  57  MET 57  57  57  MET MET A . n 
A  1  58  SER 58  58  58  SER SER A . n 
A  1  59  GLU 59  59  59  GLU GLU A . n 
A  1  60  THR 60  60  60  THR THR A . n 
A  1  61  LEU 61  61  61  LEU LEU A . n 
A  1  62  SER 62  62  62  SER SER A . n 
A  1  63  LYS 63  63  63  LYS LYS A . n 
A  1  64  VAL 64  64  64  VAL VAL A . n 
A  1  65  SER 65  65  65  SER SER A . n 
A  1  66  LEU 66  66  66  LEU LEU A . n 
A  1  67  LEU 67  67  67  LEU LEU A . n 
A  1  68  THR 68  68  68  THR THR A . n 
A  1  69  PRO 69  69  69  PRO PRO A . n 
A  1  70  ASP 70  70  70  ASP ASP A . n 
A  1  71  ILE 71  71  71  ILE ILE A . n 
A  1  72  GLY 72  72  72  GLY GLY A . n 
A  1  73  ALA 73  73  73  ALA ALA A . n 
A  1  74  VAL 74  74  74  VAL VAL A . n 
A  1  75  TYR 75  75  75  TYR TYR A . n 
A  1  76  SER 76  76  76  SER SER A . n 
A  1  77  GLY 77  77  77  GLY GLY A . n 
A  1  78  MET 78  78  78  MET MET A . n 
A  1  79  GLY 79  79  79  GLY GLY A . n 
A  1  80  PRO 80  80  80  PRO PRO A . n 
A  1  81  ASP 81  81  81  ASP ASP A . n 
A  1  82  TYR 82  82  82  TYR TYR A . n 
A  1  83  ARG 83  83  83  ARG ARG A . n 
A  1  84  VAL 84  84  84  VAL VAL A . n 
A  1  85  LEU 85  85  85  LEU LEU A . n 
A  1  86  VAL 86  86  86  VAL VAL A . n 
A  1  87  ASP 87  87  87  ASP ASP A . n 
A  1  88  LYS 88  88  88  LYS LYS A . n 
A  1  89  SER 89  89  89  SER SER A . n 
A  1  90  ARG 90  90  90  ARG ARG A . n 
A  1  91  LYS 91  91  91  LYS LYS A . n 
A  1  92  VAL 92  92  92  VAL VAL A . n 
A  1  93  ALA 93  93  93  ALA ALA A . n 
A  1  94  HIS 94  94  94  HIS HIS A . n 
A  1  95  THR 95  95  95  THR THR A . n 
A  1  96  SER 96  96  96  SER SER A . n 
A  1  97  TYR 97  97  97  TYR TYR A . n 
A  1  98  LYS 98  98  98  LYS LYS A . n 
A  1  99  ARG 99  99  99  ARG ARG A . n 
A  1  100 ILE 100 100 100 ILE ILE A . n 
A  1  101 TYR 101 101 101 TYR TYR A . n 
A  1  102 GLY 102 102 102 GLY GLY A . n 
A  1  103 GLU 103 103 103 GLU GLU A . n 
A  1  104 TYR 104 104 104 TYR TYR A . n 
A  1  105 PRO 105 105 105 PRO PRO A . n 
A  1  106 PRO 106 106 106 PRO PRO A . n 
A  1  107 THR 107 107 107 THR THR A . n 
A  1  108 LYS 108 108 108 LYS LYS A . n 
A  1  109 LEU 109 109 109 LEU LEU A . n 
A  1  110 LEU 110 110 110 LEU LEU A . n 
A  1  111 VAL 111 111 111 VAL VAL A . n 
A  1  112 SER 112 112 112 SER SER A . n 
A  1  113 GLU 113 113 113 GLU GLU A . n 
A  1  114 VAL 114 114 114 VAL VAL A . n 
A  1  115 ALA 115 115 115 ALA ALA A . n 
A  1  116 LYS 116 116 116 LYS LYS A . n 
A  1  117 ILE 117 117 117 ILE ILE A . n 
A  1  118 MET 118 118 118 MET MET A . n 
A  1  119 GLN 119 119 119 GLN GLN A . n 
A  1  120 GLU 120 120 120 GLU GLU A . n 
A  1  121 ALA 121 121 121 ALA ALA A . n 
A  1  122 THR 122 122 122 THR THR A . n 
A  1  123 GLN 123 123 123 GLN GLN A . n 
A  1  124 SER 124 124 124 SER SER A . n 
A  1  125 GLY 125 125 125 GLY GLY A . n 
A  1  126 GLY 126 126 126 GLY GLY A . n 
A  1  127 VAL 127 127 127 VAL VAL A . n 
A  1  128 ARG 128 128 128 ARG ARG A . n 
A  1  129 PRO 129 129 129 PRO PRO A . n 
A  1  130 PHE 130 130 130 PHE PHE A . n 
A  1  131 GLY 131 131 131 GLY GLY A . n 
A  1  132 VAL 132 132 132 VAL VAL A . n 
A  1  133 SER 133 133 133 SER SER A . n 
A  1  134 LEU 134 134 134 LEU LEU A . n 
A  1  135 LEU 135 135 135 LEU LEU A . n 
A  1  136 ILE 136 136 136 ILE ILE A . n 
A  1  137 ALA 137 137 137 ALA ALA A . n 
A  1  138 GLY 138 138 138 GLY GLY A . n 
A  1  139 HIS 139 139 139 HIS HIS A . n 
A  1  140 ASP 140 140 140 ASP ASP A . n 
A  1  141 GLU 141 141 141 GLU GLU A . n 
A  1  142 PHE 142 142 142 PHE PHE A . n 
A  1  143 ASN 143 143 143 ASN ASN A . n 
A  1  144 GLY 144 144 144 GLY GLY A . n 
A  1  145 PHE 145 145 145 PHE PHE A . n 
A  1  146 SER 146 146 146 SER SER A . n 
A  1  147 LEU 147 147 147 LEU LEU A . n 
A  1  148 TYR 148 148 148 TYR TYR A . n 
A  1  149 GLN 149 149 149 GLN GLN A . n 
A  1  150 VAL 150 150 150 VAL VAL A . n 
A  1  151 ASP 151 151 151 ASP ASP A . n 
A  1  152 PRO 152 152 152 PRO PRO A . n 
A  1  153 SER 153 153 153 SER SER A . n 
A  1  154 GLY 154 154 154 GLY GLY A . n 
A  1  155 SER 155 155 155 SER SER A . n 
A  1  156 TYR 156 156 156 TYR TYR A . n 
A  1  157 PHE 157 157 157 PHE PHE A . n 
A  1  158 PRO 158 158 158 PRO PRO A . n 
A  1  159 TRP 159 159 159 TRP TRP A . n 
A  1  160 LYS 160 160 160 LYS LYS A . n 
A  1  161 ALA 161 161 161 ALA ALA A . n 
A  1  162 THR 162 162 162 THR THR A . n 
A  1  163 ALA 163 163 163 ALA ALA A . n 
A  1  164 ILE 164 164 164 ILE ILE A . n 
A  1  165 GLY 165 165 165 GLY GLY A . n 
A  1  166 LYS 166 166 166 LYS LYS A . n 
A  1  167 GLY 167 167 167 GLY GLY A . n 
A  1  168 SER 168 168 168 SER SER A . n 
A  1  169 VAL 169 169 169 VAL VAL A . n 
A  1  170 ALA 170 170 170 ALA ALA A . n 
A  1  171 ALA 171 171 171 ALA ALA A . n 
A  1  172 LYS 172 172 172 LYS LYS A . n 
A  1  173 THR 173 173 173 THR THR A . n 
A  1  174 PHE 174 174 174 PHE PHE A . n 
A  1  175 LEU 175 175 175 LEU LEU A . n 
A  1  176 GLU 176 176 176 GLU GLU A . n 
A  1  177 LYS 177 177 177 LYS LYS A . n 
A  1  178 ARG 178 178 178 ARG ARG A . n 
A  1  179 TRP 179 179 179 TRP TRP A . n 
A  1  180 ASN 180 180 180 ASN ASN A . n 
A  1  181 ASP 181 181 181 ASP ASP A . n 
A  1  182 GLU 182 182 182 GLU GLU A . n 
A  1  183 LEU 183 183 183 LEU LEU A . n 
A  1  184 GLU 184 184 184 GLU GLU A . n 
A  1  185 LEU 185 185 185 LEU LEU A . n 
A  1  186 GLU 186 186 186 GLU GLU A . n 
A  1  187 ASP 187 187 187 ASP ASP A . n 
A  1  188 ALA 188 188 188 ALA ALA A . n 
A  1  189 ILE 189 189 189 ILE ILE A . n 
A  1  190 HIS 190 190 190 HIS HIS A . n 
A  1  191 ILE 191 191 191 ILE ILE A . n 
A  1  192 ALA 192 192 192 ALA ALA A . n 
A  1  193 LEU 193 193 193 LEU LEU A . n 
A  1  194 LEU 194 194 194 LEU LEU A . n 
A  1  195 THR 195 195 195 THR THR A . n 
A  1  196 LEU 196 196 196 LEU LEU A . n 
A  1  197 LYS 197 197 197 LYS LYS A . n 
A  1  198 GLU 198 198 198 GLU GLU A . n 
A  1  199 SER 199 199 199 SER SER A . n 
A  1  200 VAL 200 200 200 VAL VAL A . n 
A  1  201 GLU 201 201 201 GLU GLU A . n 
A  1  202 GLY 202 202 202 GLY GLY A . n 
A  1  203 GLU 203 203 203 GLU GLU A . n 
A  1  204 PHE 204 204 204 PHE PHE A . n 
A  1  205 ASN 205 205 205 ASN ASN A . n 
A  1  206 GLY 206 206 206 GLY GLY A . n 
A  1  207 ASP 207 207 207 ASP ASP A . n 
A  1  208 THR 208 208 208 THR THR A . n 
A  1  209 ILE 209 209 209 ILE ILE A . n 
A  1  210 GLU 210 210 210 GLU GLU A . n 
A  1  211 LEU 211 211 211 LEU LEU A . n 
A  1  212 ALA 212 212 212 ALA ALA A . n 
A  1  213 ILE 213 213 213 ILE ILE A . n 
A  1  214 ILE 214 214 214 ILE ILE A . n 
A  1  215 GLY 215 215 215 GLY GLY A . n 
A  1  216 ASP 216 216 216 ASP ASP A . n 
A  1  217 GLU 217 217 217 GLU GLU A . n 
A  1  218 ASN 218 218 218 ASN ASN A . n 
A  1  219 PRO 219 219 219 PRO PRO A . n 
A  1  220 ASP 220 220 220 ASP ASP A . n 
A  1  221 LEU 221 221 221 LEU LEU A . n 
A  1  222 LEU 222 222 222 LEU LEU A . n 
A  1  223 GLY 223 223 223 GLY GLY A . n 
A  1  224 TYR 224 224 224 TYR TYR A . n 
A  1  225 THR 225 225 225 THR THR A . n 
A  1  226 GLY 226 226 226 GLY GLY A . n 
A  1  227 ILE 227 227 227 ILE ILE A . n 
A  1  228 PRO 228 228 228 PRO PRO A . n 
A  1  229 THR 229 229 229 THR THR A . n 
A  1  230 ASP 230 230 230 ASP ASP A . n 
A  1  231 LYS 231 231 231 LYS LYS A . n 
A  1  232 GLY 232 232 232 GLY GLY A . n 
A  1  233 PRO 233 233 233 PRO PRO A . n 
A  1  234 ARG 234 234 234 ARG ARG A . n 
A  1  235 PHE 235 235 235 PHE PHE A . n 
A  1  236 ARG 236 236 236 ARG ARG A . n 
A  1  237 LYS 237 237 237 LYS LYS A . n 
A  1  238 LEU 238 238 238 LEU LEU A . n 
A  1  239 THR 239 239 239 THR THR A . n 
A  1  240 SER 240 240 240 SER SER A . n 
A  1  241 GLN 241 241 241 GLN GLN A . n 
A  1  242 GLU 242 242 242 GLU GLU A . n 
A  1  243 ILE 243 243 243 ILE ILE A . n 
A  1  244 ASN 244 244 244 ASN ASN A . n 
A  1  245 ASP 245 245 245 ASP ASP A . n 
A  1  246 ARG 246 246 246 ARG ARG A . n 
A  1  247 LEU 247 247 247 LEU LEU A . n 
A  1  248 GLU 248 248 248 GLU GLU A . n 
A  1  249 ALA 249 249 249 ALA ALA A . n 
A  1  250 LEU 250 250 250 LEU LEU A . n 
B  2  1   MET 1   0   ?   ?   ?   B . n 
B  2  2   GLY 2   1   1   GLY GLY B . n 
B  2  3   SER 3   2   2   SER SER B . n 
B  2  4   ARG 4   3   3   ARG ARG B . n 
B  2  5   ARG 5   4   4   ARG ARG B . n 
B  2  6   TYR 6   5   5   TYR TYR B . n 
B  2  7   ASP 7   6   6   ASP ASP B . n 
B  2  8   SER 8   7   7   SER SER B . n 
B  2  9   ARG 9   8   8   ARG ARG B . n 
B  2  10  THR 10  9   9   THR THR B . n 
B  2  11  THR 11  10  10  THR THR B . n 
B  2  12  ILE 12  11  11  ILE ILE B . n 
B  2  13  PHE 13  12  12  PHE PHE B . n 
B  2  14  SER 14  13  13  SER SER B . n 
B  2  15  PRO 15  14  14  PRO PRO B . n 
B  2  16  GLU 16  15  15  GLU GLU B . n 
B  2  17  GLY 17  16  16  GLY GLY B . n 
B  2  18  ARG 18  17  17  ARG ARG B . n 
B  2  19  LEU 19  18  18  LEU LEU B . n 
B  2  20  TYR 20  19  19  TYR TYR B . n 
B  2  21  GLN 21  20  20  GLN GLN B . n 
B  2  22  VAL 22  21  21  VAL VAL B . n 
B  2  23  GLU 23  22  22  GLU GLU B . n 
B  2  24  TYR 24  23  23  TYR TYR B . n 
B  2  25  ALA 25  24  24  ALA ALA B . n 
B  2  26  LEU 26  25  25  LEU LEU B . n 
B  2  27  GLU 27  26  26  GLU GLU B . n 
B  2  28  SER 28  27  27  SER SER B . n 
B  2  29  ILE 29  28  28  ILE ILE B . n 
B  2  30  SER 30  29  29  SER SER B . n 
B  2  31  HIS 31  30  30  HIS HIS B . n 
B  2  32  ALA 32  31  31  ALA ALA B . n 
B  2  33  GLY 33  32  32  GLY GLY B . n 
B  2  34  THR 34  33  33  THR THR B . n 
B  2  35  ALA 35  34  34  ALA ALA B . n 
B  2  36  ILE 36  35  35  ILE ILE B . n 
B  2  37  GLY 37  36  36  GLY GLY B . n 
B  2  38  ILE 38  37  37  ILE ILE B . n 
B  2  39  MET 39  38  38  MET MET B . n 
B  2  40  ALA 40  39  39  ALA ALA B . n 
B  2  41  SER 41  40  40  SER SER B . n 
B  2  42  ASP 42  41  41  ASP ASP B . n 
B  2  43  GLY 43  42  42  GLY GLY B . n 
B  2  44  ILE 44  43  43  ILE ILE B . n 
B  2  45  VAL 45  44  44  VAL VAL B . n 
B  2  46  LEU 46  45  45  LEU LEU B . n 
B  2  47  ALA 47  46  46  ALA ALA B . n 
B  2  48  ALA 48  47  47  ALA ALA B . n 
B  2  49  GLU 49  48  48  GLU GLU B . n 
B  2  50  ARG 50  49  49  ARG ARG B . n 
B  2  51  LYS 51  50  50  LYS LYS B . n 
B  2  52  VAL 52  51  51  VAL VAL B . n 
B  2  53  THR 53  52  52  THR THR B . n 
B  2  54  SER 54  53  53  SER SER B . n 
B  2  55  THR 55  54  54  THR THR B . n 
B  2  56  LEU 56  55  55  LEU LEU B . n 
B  2  57  LEU 57  56  56  LEU LEU B . n 
B  2  58  GLU 58  57  57  GLU GLU B . n 
B  2  59  GLN 59  58  58  GLN GLN B . n 
B  2  60  ASP 60  59  59  ASP ASP B . n 
B  2  61  THR 61  60  60  THR THR B . n 
B  2  62  SER 62  61  61  SER SER B . n 
B  2  63  THR 63  62  62  THR THR B . n 
B  2  64  GLU 64  63  63  GLU GLU B . n 
B  2  65  LYS 65  64  64  LYS LYS B . n 
B  2  66  LEU 66  65  65  LEU LEU B . n 
B  2  67  TYR 67  66  66  TYR TYR B . n 
B  2  68  LYS 68  67  67  LYS LYS B . n 
B  2  69  LEU 69  68  68  LEU LEU B . n 
B  2  70  ASN 70  69  69  ASN ASN B . n 
B  2  71  ASP 71  70  70  ASP ASP B . n 
B  2  72  LYS 72  71  71  LYS LYS B . n 
B  2  73  ILE 73  72  72  ILE ILE B . n 
B  2  74  ALA 74  73  73  ALA ALA B . n 
B  2  75  VAL 75  74  74  VAL VAL B . n 
B  2  76  ALA 76  75  75  ALA ALA B . n 
B  2  77  VAL 77  76  76  VAL VAL B . n 
B  2  78  ALA 78  77  77  ALA ALA B . n 
B  2  79  GLY 79  78  78  GLY GLY B . n 
B  2  80  LEU 80  79  79  LEU LEU B . n 
B  2  81  THR 81  80  80  THR THR B . n 
B  2  82  ALA 82  81  81  ALA ALA B . n 
B  2  83  ASP 83  82  82  ASP ASP B . n 
B  2  84  ALA 84  83  83  ALA ALA B . n 
B  2  85  GLU 85  84  84  GLU GLU B . n 
B  2  86  ILE 86  85  85  ILE ILE B . n 
B  2  87  LEU 87  86  86  LEU LEU B . n 
B  2  88  ILE 88  87  87  ILE ILE B . n 
B  2  89  ASN 89  88  88  ASN ASN B . n 
B  2  90  THR 90  89  89  THR THR B . n 
B  2  91  ALA 91  90  90  ALA ALA B . n 
B  2  92  ARG 92  91  91  ARG ARG B . n 
B  2  93  ILE 93  92  92  ILE ILE B . n 
B  2  94  HIS 94  93  93  HIS HIS B . n 
B  2  95  ALA 95  94  94  ALA ALA B . n 
B  2  96  GLN 96  95  95  GLN GLN B . n 
B  2  97  ASN 97  96  96  ASN ASN B . n 
B  2  98  TYR 98  97  97  TYR TYR B . n 
B  2  99  LEU 99  98  98  LEU LEU B . n 
B  2  100 LYS 100 99  99  LYS LYS B . n 
B  2  101 THR 101 100 100 THR THR B . n 
B  2  102 TYR 102 101 101 TYR TYR B . n 
B  2  103 ASN 103 102 102 ASN ASN B . n 
B  2  104 GLU 104 103 103 GLU GLU B . n 
B  2  105 ASP 105 104 104 ASP ASP B . n 
B  2  106 ILE 106 105 105 ILE ILE B . n 
B  2  107 PRO 107 106 106 PRO PRO B . n 
B  2  108 VAL 108 107 107 VAL VAL B . n 
B  2  109 GLU 109 108 108 GLU GLU B . n 
B  2  110 ILE 110 109 109 ILE ILE B . n 
B  2  111 LEU 111 110 110 LEU LEU B . n 
B  2  112 VAL 112 111 111 VAL VAL B . n 
B  2  113 ARG 113 112 112 ARG ARG B . n 
B  2  114 ARG 114 113 113 ARG ARG B . n 
B  2  115 LEU 115 114 114 LEU LEU B . n 
B  2  116 SER 116 115 115 SER SER B . n 
B  2  117 ASP 117 116 116 ASP ASP B . n 
B  2  118 ILE 118 117 117 ILE ILE B . n 
B  2  119 LYS 119 118 118 LYS LYS B . n 
B  2  120 GLN 120 119 119 GLN GLN B . n 
B  2  121 GLY 121 120 120 GLY GLY B . n 
B  2  122 TYR 122 121 121 TYR TYR B . n 
B  2  123 THR 123 122 122 THR THR B . n 
B  2  124 GLN 124 123 123 GLN GLN B . n 
B  2  125 HIS 125 124 124 HIS HIS B . n 
B  2  126 GLY 126 125 125 GLY GLY B . n 
B  2  127 GLY 127 126 126 GLY GLY B . n 
B  2  128 LEU 128 127 127 LEU LEU B . n 
B  2  129 ARG 129 128 128 ARG ARG B . n 
B  2  130 PRO 130 129 129 PRO PRO B . n 
B  2  131 PHE 131 130 130 PHE PHE B . n 
B  2  132 GLY 132 131 131 GLY GLY B . n 
B  2  133 VAL 133 132 132 VAL VAL B . n 
B  2  134 SER 134 133 133 SER SER B . n 
B  2  135 PHE 135 134 134 PHE PHE B . n 
B  2  136 ILE 136 135 135 ILE ILE B . n 
B  2  137 TYR 137 136 136 TYR TYR B . n 
B  2  138 ALA 138 137 137 ALA ALA B . n 
B  2  139 GLY 139 138 138 GLY GLY B . n 
B  2  140 TYR 140 139 139 TYR TYR B . n 
B  2  141 ASP 141 140 140 ASP ASP B . n 
B  2  142 ASP 142 141 141 ASP ASP B . n 
B  2  143 ARG 143 142 142 ARG ARG B . n 
B  2  144 TYR 144 143 143 TYR TYR B . n 
B  2  145 GLY 145 144 144 GLY GLY B . n 
B  2  146 TYR 146 145 145 TYR TYR B . n 
B  2  147 GLN 147 146 146 GLN GLN B . n 
B  2  148 LEU 148 147 147 LEU LEU B . n 
B  2  149 TYR 149 148 148 TYR TYR B . n 
B  2  150 THR 150 149 149 THR THR B . n 
B  2  151 SER 151 150 150 SER SER B . n 
B  2  152 ASN 152 151 151 ASN ASN B . n 
B  2  153 PRO 153 152 152 PRO PRO B . n 
B  2  154 SER 154 153 153 SER SER B . n 
B  2  155 GLY 155 154 154 GLY GLY B . n 
B  2  156 ASN 156 155 155 ASN ASN B . n 
B  2  157 TYR 157 156 156 TYR TYR B . n 
B  2  158 THR 158 157 157 THR THR B . n 
B  2  159 GLY 159 158 158 GLY GLY B . n 
B  2  160 TRP 160 159 159 TRP TRP B . n 
B  2  161 LYS 161 160 160 LYS LYS B . n 
B  2  162 ALA 162 161 161 ALA ALA B . n 
B  2  163 ILE 163 162 162 ILE ILE B . n 
B  2  164 SER 164 163 163 SER SER B . n 
B  2  165 VAL 165 164 164 VAL VAL B . n 
B  2  166 GLY 166 165 165 GLY GLY B . n 
B  2  167 ALA 167 166 166 ALA ALA B . n 
B  2  168 ASN 168 167 167 ASN ASN B . n 
B  2  169 THR 169 168 168 THR THR B . n 
B  2  170 SER 170 169 169 SER SER B . n 
B  2  171 ALA 171 170 170 ALA ALA B . n 
B  2  172 ALA 172 171 171 ALA ALA B . n 
B  2  173 GLN 173 172 172 GLN GLN B . n 
B  2  174 THR 174 173 173 THR THR B . n 
B  2  175 LEU 175 174 174 LEU LEU B . n 
B  2  176 LEU 176 175 175 LEU LEU B . n 
B  2  177 GLN 177 176 176 GLN GLN B . n 
B  2  178 MET 178 177 177 MET MET B . n 
B  2  179 ASP 179 178 178 ASP ASP B . n 
B  2  180 TYR 180 179 179 TYR TYR B . n 
B  2  181 LYS 181 180 180 LYS LYS B . n 
B  2  182 ASP 182 181 181 ASP ASP B . n 
B  2  183 ASP 183 182 182 ASP ASP B . n 
B  2  184 MET 184 183 183 MET MET B . n 
B  2  185 LYS 185 184 184 LYS LYS B . n 
B  2  186 VAL 186 185 185 VAL VAL B . n 
B  2  187 ASP 187 186 186 ASP ASP B . n 
B  2  188 ASP 188 187 187 ASP ASP B . n 
B  2  189 ALA 189 188 188 ALA ALA B . n 
B  2  190 ILE 190 189 189 ILE ILE B . n 
B  2  191 GLU 191 190 190 GLU GLU B . n 
B  2  192 LEU 192 191 191 LEU LEU B . n 
B  2  193 ALA 193 192 192 ALA ALA B . n 
B  2  194 LEU 194 193 193 LEU LEU B . n 
B  2  195 LYS 195 194 194 LYS LYS B . n 
B  2  196 THR 196 195 195 THR THR B . n 
B  2  197 LEU 197 196 196 LEU LEU B . n 
B  2  198 SER 198 197 197 SER SER B . n 
B  2  199 LYS 199 198 198 LYS LYS B . n 
B  2  200 THR 200 199 199 THR THR B . n 
B  2  201 THR 201 200 200 THR THR B . n 
B  2  202 ASP 202 201 201 ASP ASP B . n 
B  2  203 SER 203 202 202 SER SER B . n 
B  2  204 SER 204 203 203 SER SER B . n 
B  2  205 ALA 205 204 204 ALA ALA B . n 
B  2  206 LEU 206 205 205 LEU LEU B . n 
B  2  207 THR 207 206 206 THR THR B . n 
B  2  208 TYR 208 207 207 TYR TYR B . n 
B  2  209 ASP 209 208 208 ASP ASP B . n 
B  2  210 ARG 210 209 209 ARG ARG B . n 
B  2  211 LEU 211 210 210 LEU LEU B . n 
B  2  212 GLU 212 211 211 GLU GLU B . n 
B  2  213 PHE 213 212 212 PHE PHE B . n 
B  2  214 ALA 214 213 213 ALA ALA B . n 
B  2  215 THR 215 214 214 THR THR B . n 
B  2  216 ILE 216 215 215 ILE ILE B . n 
B  2  217 ARG 217 216 216 ARG ARG B . n 
B  2  218 LYS 218 217 217 LYS LYS B . n 
B  2  219 GLY 219 218 218 GLY GLY B . n 
B  2  220 ALA 220 219 219 ALA ALA B . n 
B  2  221 ASN 221 220 220 ASN ASN B . n 
B  2  222 ASP 222 221 221 ASP ASP B . n 
B  2  223 GLY 223 222 222 GLY GLY B . n 
B  2  224 GLU 224 223 223 GLU GLU B . n 
B  2  225 VAL 225 224 224 VAL VAL B . n 
B  2  226 TYR 226 225 225 TYR TYR B . n 
B  2  227 GLN 227 226 226 GLN GLN B . n 
B  2  228 LYS 228 227 227 LYS LYS B . n 
B  2  229 ILE 229 228 228 ILE ILE B . n 
B  2  230 PHE 230 229 229 PHE PHE B . n 
B  2  231 LYS 231 230 230 LYS LYS B . n 
B  2  232 PRO 232 231 231 PRO PRO B . n 
B  2  233 GLN 233 232 232 GLN GLN B . n 
B  2  234 GLU 234 233 233 GLU GLU B . n 
B  2  235 ILE 235 234 234 ILE ILE B . n 
B  2  236 LYS 236 235 235 LYS LYS B . n 
B  2  237 ASP 237 236 236 ASP ASP B . n 
B  2  238 ILE 238 237 237 ILE ILE B . n 
B  2  239 LEU 239 238 238 LEU LEU B . n 
B  2  240 VAL 240 239 239 VAL VAL B . n 
B  2  241 LYS 241 240 240 LYS LYS B . n 
B  2  242 THR 242 241 241 THR THR B . n 
B  2  243 GLY 243 242 242 GLY GLY B . n 
B  2  244 ILE 244 243 243 ILE ILE B . n 
B  2  245 THR 245 244 244 THR THR B . n 
B  2  246 LYS 246 245 ?   ?   ?   B . n 
B  2  247 LYS 247 246 ?   ?   ?   B . n 
B  2  248 ASP 248 247 ?   ?   ?   B . n 
B  2  249 GLU 249 248 ?   ?   ?   B . n 
B  2  250 ASP 250 249 ?   ?   ?   B . n 
B  2  251 GLU 251 250 ?   ?   ?   B . n 
B  2  252 GLU 252 251 ?   ?   ?   B . n 
B  2  253 ALA 253 252 ?   ?   ?   B . n 
B  2  254 ASP 254 253 ?   ?   ?   B . n 
B  2  255 GLU 255 254 ?   ?   ?   B . n 
B  2  256 ASP 256 255 ?   ?   ?   B . n 
B  2  257 MET 257 256 ?   ?   ?   B . n 
B  2  258 LYS 258 257 ?   ?   ?   B . n 
C  3  1   MET 1   -1  ?   ?   ?   C . n 
C  3  2   SER 2   0   ?   ?   ?   C . n 
C  3  3   GLY 3   1   1   GLY GLY C . n 
C  3  4   TYR 4   2   2   TYR TYR C . n 
C  3  5   ASP 5   3   3   ASP ASP C . n 
C  3  6   ARG 6   4   4   ARG ARG C . n 
C  3  7   ALA 7   5   5   ALA ALA C . n 
C  3  8   LEU 8   6   6   LEU LEU C . n 
C  3  9   SER 9   7   7   SER SER C . n 
C  3  10  ILE 10  8   8   ILE ILE C . n 
C  3  11  PHE 11  9   9   PHE PHE C . n 
C  3  12  SER 12  10  10  SER SER C . n 
C  3  13  PRO 13  11  11  PRO PRO C . n 
C  3  14  ASP 14  12  12  ASP ASP C . n 
C  3  15  GLY 15  13  13  GLY GLY C . n 
C  3  16  HIS 16  14  14  HIS HIS C . n 
C  3  17  ILE 17  15  15  ILE ILE C . n 
C  3  18  PHE 18  16  16  PHE PHE C . n 
C  3  19  GLN 19  17  17  GLN GLN C . n 
C  3  20  VAL 20  18  18  VAL VAL C . n 
C  3  21  GLU 21  19  19  GLU GLU C . n 
C  3  22  TYR 22  20  20  TYR TYR C . n 
C  3  23  ALA 23  21  21  ALA ALA C . n 
C  3  24  LEU 24  22  22  LEU LEU C . n 
C  3  25  GLU 25  23  23  GLU GLU C . n 
C  3  26  ALA 26  24  24  ALA ALA C . n 
C  3  27  VAL 27  25  25  VAL VAL C . n 
C  3  28  LYS 28  26  26  LYS LYS C . n 
C  3  29  ARG 29  27  27  ARG ARG C . n 
C  3  30  GLY 30  28  28  GLY GLY C . n 
C  3  31  THR 31  29  29  THR THR C . n 
C  3  32  CYS 32  30  30  CYS CYS C . n 
C  3  33  ALA 33  31  31  ALA ALA C . n 
C  3  34  VAL 34  32  32  VAL VAL C . n 
C  3  35  GLY 35  33  33  GLY GLY C . n 
C  3  36  VAL 36  34  34  VAL VAL C . n 
C  3  37  LYS 37  35  35  LYS LYS C . n 
C  3  38  GLY 38  36  36  GLY GLY C . n 
C  3  39  LYS 39  37  37  LYS LYS C . n 
C  3  40  ASN 40  38  38  ASN ASN C . n 
C  3  41  CYS 41  39  39  CYS CYS C . n 
C  3  42  VAL 42  40  40  VAL VAL C . n 
C  3  43  VAL 43  41  41  VAL VAL C . n 
C  3  44  LEU 44  42  42  LEU LEU C . n 
C  3  45  GLY 45  43  43  GLY GLY C . n 
C  3  46  CYS 46  44  44  CYS CYS C . n 
C  3  47  GLU 47  45  45  GLU GLU C . n 
C  3  48  ARG 48  46  46  ARG ARG C . n 
C  3  49  ARG 49  47  47  ARG ARG C . n 
C  3  50  SER 50  48  48  SER SER C . n 
C  3  51  THR 51  49  49  THR THR C . n 
C  3  52  LEU 52  50  50  LEU LEU C . n 
C  3  53  LYS 53  51  51  LYS LYS C . n 
C  3  54  LEU 54  52  52  LEU LEU C . n 
C  3  55  GLN 55  53  53  GLN GLN C . n 
C  3  56  ASP 56  54  54  ASP ASP C . n 
C  3  57  THR 57  55  55  THR THR C . n 
C  3  58  ARG 58  56  56  ARG ARG C . n 
C  3  59  ILE 59  57  57  ILE ILE C . n 
C  3  60  THR 60  58  58  THR THR C . n 
C  3  61  PRO 61  59  59  PRO PRO C . n 
C  3  62  SER 62  60  60  SER SER C . n 
C  3  63  LYS 63  61  61  LYS LYS C . n 
C  3  64  VAL 64  62  62  VAL VAL C . n 
C  3  65  SER 65  63  63  SER SER C . n 
C  3  66  LYS 66  64  64  LYS LYS C . n 
C  3  67  ILE 67  65  65  ILE ILE C . n 
C  3  68  ASP 68  66  66  ASP ASP C . n 
C  3  69  SER 69  67  67  SER SER C . n 
C  3  70  HIS 70  68  68  HIS HIS C . n 
C  3  71  VAL 71  69  69  VAL VAL C . n 
C  3  72  VAL 72  70  70  VAL VAL C . n 
C  3  73  LEU 73  71  71  LEU LEU C . n 
C  3  74  SER 74  72  72  SER SER C . n 
C  3  75  PHE 75  73  73  PHE PHE C . n 
C  3  76  SER 76  74  74  SER SER C . n 
C  3  77  GLY 77  75  75  GLY GLY C . n 
C  3  78  LEU 78  76  76  LEU LEU C . n 
C  3  79  ASN 79  77  77  ASN ASN C . n 
C  3  80  ALA 80  78  78  ALA ALA C . n 
C  3  81  ASP 81  79  79  ASP ASP C . n 
C  3  82  SER 82  80  80  SER SER C . n 
C  3  83  ARG 83  81  81  ARG ARG C . n 
C  3  84  ILE 84  82  82  ILE ILE C . n 
C  3  85  LEU 85  83  83  LEU LEU C . n 
C  3  86  ILE 86  84  84  ILE ILE C . n 
C  3  87  GLU 87  85  85  GLU GLU C . n 
C  3  88  LYS 88  86  86  LYS LYS C . n 
C  3  89  ALA 89  87  87  ALA ALA C . n 
C  3  90  ARG 90  88  88  ARG ARG C . n 
C  3  91  VAL 91  89  89  VAL VAL C . n 
C  3  92  GLU 92  90  90  GLU GLU C . n 
C  3  93  ALA 93  91  91  ALA ALA C . n 
C  3  94  GLN 94  92  92  GLN GLN C . n 
C  3  95  SER 95  93  93  SER SER C . n 
C  3  96  HIS 96  94  94  HIS HIS C . n 
C  3  97  ARG 97  95  95  ARG ARG C . n 
C  3  98  LEU 98  96  96  LEU LEU C . n 
C  3  99  THR 99  97  97  THR THR C . n 
C  3  100 LEU 100 98  98  LEU LEU C . n 
C  3  101 GLU 101 99  99  GLU GLU C . n 
C  3  102 ASP 102 100 100 ASP ASP C . n 
C  3  103 PRO 103 101 101 PRO PRO C . n 
C  3  104 VAL 104 102 102 VAL VAL C . n 
C  3  105 THR 105 103 103 THR THR C . n 
C  3  106 VAL 106 104 104 VAL VAL C . n 
C  3  107 GLU 107 105 105 GLU GLU C . n 
C  3  108 TYR 108 106 106 TYR TYR C . n 
C  3  109 LEU 109 107 107 LEU LEU C . n 
C  3  110 THR 110 108 108 THR THR C . n 
C  3  111 ARG 111 109 109 ARG ARG C . n 
C  3  112 TYR 112 110 110 TYR TYR C . n 
C  3  113 VAL 113 111 111 VAL VAL C . n 
C  3  114 ALA 114 112 112 ALA ALA C . n 
C  3  115 GLY 115 113 113 GLY GLY C . n 
C  3  116 VAL 116 114 114 VAL VAL C . n 
C  3  117 GLN 117 115 115 GLN GLN C . n 
C  3  118 GLN 118 116 116 GLN GLN C . n 
C  3  119 ARG 119 117 117 ARG ARG C . n 
C  3  120 TYR 120 118 118 TYR TYR C . n 
C  3  121 THR 121 119 119 THR THR C . n 
C  3  122 GLN 122 120 120 GLN GLN C . n 
C  3  123 SER 123 121 121 SER SER C . n 
C  3  124 GLY 124 122 122 GLY GLY C . n 
C  3  125 GLY 125 123 123 GLY GLY C . n 
C  3  126 VAL 126 124 124 VAL VAL C . n 
C  3  127 ARG 127 125 125 ARG ARG C . n 
C  3  128 PRO 128 126 126 PRO PRO C . n 
C  3  129 PHE 129 127 127 PHE PHE C . n 
C  3  130 GLY 130 128 128 GLY GLY C . n 
C  3  131 VAL 131 129 129 VAL VAL C . n 
C  3  132 SER 132 130 130 SER SER C . n 
C  3  133 THR 133 131 131 THR THR C . n 
C  3  134 LEU 134 132 132 LEU LEU C . n 
C  3  135 ILE 135 133 133 ILE ILE C . n 
C  3  136 ALA 136 134 134 ALA ALA C . n 
C  3  137 GLY 137 135 135 GLY GLY C . n 
C  3  138 PHE 138 136 136 PHE PHE C . n 
C  3  139 ASP 139 137 137 ASP ASP C . n 
C  3  140 PRO 140 138 138 PRO PRO C . n 
C  3  141 ARG 141 139 139 ARG ARG C . n 
C  3  142 ASP 142 140 140 ASP ASP C . n 
C  3  143 ASP 143 141 141 ASP ASP C . n 
C  3  144 GLU 144 142 142 GLU GLU C . n 
C  3  145 PRO 145 143 143 PRO PRO C . n 
C  3  146 LYS 146 144 144 LYS LYS C . n 
C  3  147 LEU 147 145 145 LEU LEU C . n 
C  3  148 TYR 148 146 146 TYR TYR C . n 
C  3  149 GLN 149 147 147 GLN GLN C . n 
C  3  150 THR 150 148 148 THR THR C . n 
C  3  151 GLU 151 149 149 GLU GLU C . n 
C  3  152 PRO 152 150 150 PRO PRO C . n 
C  3  153 SER 153 151 151 SER SER C . n 
C  3  154 GLY 154 152 152 GLY GLY C . n 
C  3  155 ILE 155 153 153 ILE ILE C . n 
C  3  156 TYR 156 154 154 TYR TYR C . n 
C  3  157 SER 157 155 155 SER SER C . n 
C  3  158 SER 158 156 156 SER SER C . n 
C  3  159 TRP 159 157 157 TRP TRP C . n 
C  3  160 SER 160 158 158 SER SER C . n 
C  3  161 ALA 161 159 159 ALA ALA C . n 
C  3  162 GLN 162 160 160 GLN GLN C . n 
C  3  163 THR 163 161 161 THR THR C . n 
C  3  164 ILE 164 162 162 ILE ILE C . n 
C  3  165 GLY 165 163 163 GLY GLY C . n 
C  3  166 ARG 166 164 164 ARG ARG C . n 
C  3  167 ASN 167 165 165 ASN ASN C . n 
C  3  168 SER 168 166 166 SER SER C . n 
C  3  169 LYS 169 167 167 LYS LYS C . n 
C  3  170 THR 170 168 168 THR THR C . n 
C  3  171 VAL 171 169 169 VAL VAL C . n 
C  3  172 ARG 172 170 170 ARG ARG C . n 
C  3  173 GLU 173 171 171 GLU GLU C . n 
C  3  174 PHE 174 172 172 PHE PHE C . n 
C  3  175 LEU 175 173 173 LEU LEU C . n 
C  3  176 GLU 176 174 174 GLU GLU C . n 
C  3  177 LYS 177 175 175 LYS LYS C . n 
C  3  178 ASN 178 176 176 ASN ASN C . n 
C  3  179 TYR 179 177 177 TYR TYR C . n 
C  3  180 ASP 180 178 178 ASP ASP C . n 
C  3  181 ARG 181 179 179 ARG ARG C . n 
C  3  182 LYS 182 180 180 LYS LYS C . n 
C  3  183 GLU 183 181 181 GLU GLU C . n 
C  3  184 PRO 184 182 182 PRO PRO C . n 
C  3  185 PRO 185 183 183 PRO PRO C . n 
C  3  186 ALA 186 184 184 ALA ALA C . n 
C  3  187 THR 187 185 185 THR THR C . n 
C  3  188 VAL 188 186 186 VAL VAL C . n 
C  3  189 GLU 189 187 187 GLU GLU C . n 
C  3  190 GLU 190 188 188 GLU GLU C . n 
C  3  191 CYS 191 189 189 CYS CYS C . n 
C  3  192 VAL 192 190 190 VAL VAL C . n 
C  3  193 LYS 193 191 191 LYS LYS C . n 
C  3  194 LEU 194 192 192 LEU LEU C . n 
C  3  195 THR 195 193 193 THR THR C . n 
C  3  196 VAL 196 194 194 VAL VAL C . n 
C  3  197 ARG 197 195 195 ARG ARG C . n 
C  3  198 SER 198 196 196 SER SER C . n 
C  3  199 LEU 199 197 197 LEU LEU C . n 
C  3  200 LEU 200 198 198 LEU LEU C . n 
C  3  201 GLU 201 199 199 GLU GLU C . n 
C  3  202 VAL 202 200 200 VAL VAL C . n 
C  3  203 VAL 203 201 201 VAL VAL C . n 
C  3  204 GLN 204 202 202 GLN GLN C . n 
C  3  205 THR 205 203 203 THR THR C . n 
C  3  206 GLY 206 204 204 GLY GLY C . n 
C  3  207 ALA 207 205 205 ALA ALA C . n 
C  3  208 LYS 208 206 206 LYS LYS C . n 
C  3  209 ASN 209 207 207 ASN ASN C . n 
C  3  210 ILE 210 208 208 ILE ILE C . n 
C  3  211 GLU 211 209 209 GLU GLU C . n 
C  3  212 ILE 212 210 210 ILE ILE C . n 
C  3  213 THR 213 211 211 THR THR C . n 
C  3  214 VAL 214 212 212 VAL VAL C . n 
C  3  215 VAL 215 213 213 VAL VAL C . n 
C  3  216 LYS 216 214 214 LYS LYS C . n 
C  3  217 PRO 217 215 215 PRO PRO C . n 
C  3  218 ASP 218 216 216 ASP ASP C . n 
C  3  219 SER 219 217 217 SER SER C . n 
C  3  220 ASP 220 218 218 ASP ASP C . n 
C  3  221 ILE 221 219 219 ILE ILE C . n 
C  3  222 VAL 222 220 220 VAL VAL C . n 
C  3  223 ALA 223 221 221 ALA ALA C . n 
C  3  224 LEU 224 222 222 LEU LEU C . n 
C  3  225 SER 225 223 223 SER SER C . n 
C  3  226 SER 226 224 224 SER SER C . n 
C  3  227 GLU 227 225 225 GLU GLU C . n 
C  3  228 GLU 228 226 226 GLU GLU C . n 
C  3  229 ILE 229 227 227 ILE ILE C . n 
C  3  230 ASN 230 228 228 ASN ASN C . n 
C  3  231 GLN 231 229 229 GLN GLN C . n 
C  3  232 TYR 232 230 230 TYR TYR C . n 
C  3  233 VAL 233 231 231 VAL VAL C . n 
C  3  234 THR 234 232 232 THR THR C . n 
C  3  235 GLN 235 233 233 GLN GLN C . n 
C  3  236 ILE 236 234 234 ILE ILE C . n 
C  3  237 GLU 237 235 235 GLU GLU C . n 
C  3  238 GLN 238 236 236 GLN GLN C . n 
C  3  239 GLU 239 237 237 GLU GLU C . n 
C  3  240 LYS 240 238 238 LYS LYS C . n 
C  3  241 GLN 241 239 239 GLN GLN C . n 
C  3  242 GLU 242 240 240 GLU GLU C . n 
C  3  243 GLN 243 241 ?   ?   ?   C . n 
C  3  244 GLN 244 242 ?   ?   ?   C . n 
C  3  245 GLU 245 243 ?   ?   ?   C . n 
C  3  246 GLN 246 244 ?   ?   ?   C . n 
C  3  247 ASP 247 245 ?   ?   ?   C . n 
C  3  248 LYS 248 246 ?   ?   ?   C . n 
C  3  249 LYS 249 247 ?   ?   ?   C . n 
C  3  250 LYS 250 248 ?   ?   ?   C . n 
C  3  251 LYS 251 249 ?   ?   ?   C . n 
C  3  252 SER 252 250 ?   ?   ?   C . n 
C  3  253 ASN 253 251 ?   ?   ?   C . n 
C  3  254 HIS 254 252 ?   ?   ?   C . n 
D  4  1   MET 1   -7  ?   ?   ?   D . n 
D  4  2   PHE 2   -6  ?   ?   ?   D . n 
D  4  3   LEU 3   -5  ?   ?   ?   D . n 
D  4  4   THR 4   -4  ?   ?   ?   D . n 
D  4  5   ARG 5   -3  ?   ?   ?   D . n 
D  4  6   SER 6   -2  ?   ?   ?   D . n 
D  4  7   GLU 7   -1  ?   ?   ?   D . n 
D  4  8   TYR 8   0   ?   ?   ?   D . n 
D  4  9   ASP 9   1   1   ASP ASP D . n 
D  4  10  ARG 10  2   2   ARG ARG D . n 
D  4  11  GLY 11  3   3   GLY GLY D . n 
D  4  12  VAL 12  4   4   VAL VAL D . n 
D  4  13  SER 13  5   5   SER SER D . n 
D  4  14  THR 14  6   6   THR THR D . n 
D  4  15  PHE 15  7   7   PHE PHE D . n 
D  4  16  SER 16  8   8   SER SER D . n 
D  4  17  PRO 17  9   9   PRO PRO D . n 
D  4  18  GLU 18  10  10  GLU GLU D . n 
D  4  19  GLY 19  11  11  GLY GLY D . n 
D  4  20  ARG 20  12  12  ARG ARG D . n 
D  4  21  LEU 21  13  13  LEU LEU D . n 
D  4  22  PHE 22  14  14  PHE PHE D . n 
D  4  23  GLN 23  15  15  GLN GLN D . n 
D  4  24  VAL 24  16  16  VAL VAL D . n 
D  4  25  GLU 25  17  17  GLU GLU D . n 
D  4  26  TYR 26  18  18  TYR TYR D . n 
D  4  27  SER 27  19  19  SER SER D . n 
D  4  28  LEU 28  20  20  LEU LEU D . n 
D  4  29  GLU 29  21  21  GLU GLU D . n 
D  4  30  ALA 30  22  22  ALA ALA D . n 
D  4  31  ILE 31  23  23  ILE ILE D . n 
D  4  32  LYS 32  24  24  LYS LYS D . n 
D  4  33  LEU 33  25  25  LEU LEU D . n 
D  4  34  GLY 34  26  26  GLY GLY D . n 
D  4  35  SER 35  27  27  SER SER D . n 
D  4  36  THR 36  28  28  THR THR D . n 
D  4  37  ALA 37  29  29  ALA ALA D . n 
D  4  38  ILE 38  30  30  ILE ILE D . n 
D  4  39  GLY 39  31  31  GLY GLY D . n 
D  4  40  ILE 40  32  32  ILE ILE D . n 
D  4  41  ALA 41  33  33  ALA ALA D . n 
D  4  42  THR 42  34  34  THR THR D . n 
D  4  43  LYS 43  35  35  LYS LYS D . n 
D  4  44  GLU 44  36  36  GLU GLU D . n 
D  4  45  GLY 45  37  37  GLY GLY D . n 
D  4  46  VAL 46  38  38  VAL VAL D . n 
D  4  47  VAL 47  39  39  VAL VAL D . n 
D  4  48  LEU 48  40  40  LEU LEU D . n 
D  4  49  GLY 49  41  41  GLY GLY D . n 
D  4  50  VAL 50  42  42  VAL VAL D . n 
D  4  51  GLU 51  43  43  GLU GLU D . n 
D  4  52  LYS 52  44  44  LYS LYS D . n 
D  4  53  ARG 53  45  45  ARG ARG D . n 
D  4  54  ALA 54  46  46  ALA ALA D . n 
D  4  55  THR 55  47  47  THR THR D . n 
D  4  56  SER 56  48  48  SER SER D . n 
D  4  57  PRO 57  49  49  PRO PRO D . n 
D  4  58  LEU 58  50  50  LEU LEU D . n 
D  4  59  LEU 59  51  51  LEU LEU D . n 
D  4  60  GLU 60  52  52  GLU GLU D . n 
D  4  61  SER 61  53  53  SER SER D . n 
D  4  62  ASP 62  54  54  ASP ASP D . n 
D  4  63  SER 63  55  55  SER SER D . n 
D  4  64  ILE 64  56  56  ILE ILE D . n 
D  4  65  GLU 65  57  57  GLU GLU D . n 
D  4  66  LYS 66  58  58  LYS LYS D . n 
D  4  67  ILE 67  59  59  ILE ILE D . n 
D  4  68  VAL 68  60  60  VAL VAL D . n 
D  4  69  GLU 69  61  61  GLU GLU D . n 
D  4  70  ILE 70  62  62  ILE ILE D . n 
D  4  71  ASP 71  63  63  ASP ASP D . n 
D  4  72  ARG 72  64  64  ARG ARG D . n 
D  4  73  HIS 73  65  65  HIS HIS D . n 
D  4  74  ILE 74  66  66  ILE ILE D . n 
D  4  75  GLY 75  67  67  GLY GLY D . n 
D  4  76  CYS 76  68  68  CYS CYS D . n 
D  4  77  ALA 77  69  69  ALA ALA D . n 
D  4  78  MET 78  70  70  MET MET D . n 
D  4  79  SER 79  71  71  SER SER D . n 
D  4  80  GLY 80  72  72  GLY GLY D . n 
D  4  81  LEU 81  73  73  LEU LEU D . n 
D  4  82  THR 82  74  74  THR THR D . n 
D  4  83  ALA 83  75  75  ALA ALA D . n 
D  4  84  ASP 84  76  76  ASP ASP D . n 
D  4  85  ALA 85  77  77  ALA ALA D . n 
D  4  86  ARG 86  78  78  ARG ARG D . n 
D  4  87  SER 87  79  79  SER SER D . n 
D  4  88  MET 88  80  80  MET MET D . n 
D  4  89  ILE 89  81  81  ILE ILE D . n 
D  4  90  GLU 90  82  82  GLU GLU D . n 
D  4  91  HIS 91  83  83  HIS HIS D . n 
D  4  92  ALA 92  84  84  ALA ALA D . n 
D  4  93  ARG 93  85  85  ARG ARG D . n 
D  4  94  THR 94  86  86  THR THR D . n 
D  4  95  ALA 95  87  87  ALA ALA D . n 
D  4  96  ALA 96  88  88  ALA ALA D . n 
D  4  97  VAL 97  89  89  VAL VAL D . n 
D  4  98  THR 98  90  90  THR THR D . n 
D  4  99  HIS 99  91  91  HIS HIS D . n 
D  4  100 ASN 100 92  92  ASN ASN D . n 
D  4  101 LEU 101 93  93  LEU LEU D . n 
D  4  102 TYR 102 94  94  TYR TYR D . n 
D  4  103 TYR 103 95  95  TYR TYR D . n 
D  4  104 ASP 104 96  96  ASP ASP D . n 
D  4  105 GLU 105 97  97  GLU GLU D . n 
D  4  106 ASP 106 98  98  ASP ASP D . n 
D  4  107 ILE 107 99  99  ILE ILE D . n 
D  4  108 ASN 108 100 100 ASN ASN D . n 
D  4  109 VAL 109 101 101 VAL VAL D . n 
D  4  110 GLU 110 102 102 GLU GLU D . n 
D  4  111 SER 111 103 103 SER SER D . n 
D  4  112 LEU 112 104 104 LEU LEU D . n 
D  4  113 THR 113 105 105 THR THR D . n 
D  4  114 GLN 114 106 106 GLN GLN D . n 
D  4  115 SER 115 107 107 SER SER D . n 
D  4  116 VAL 116 108 108 VAL VAL D . n 
D  4  117 CYS 117 109 109 CYS CYS D . n 
D  4  118 ASP 118 110 110 ASP ASP D . n 
D  4  119 LEU 119 111 111 LEU LEU D . n 
D  4  120 ALA 120 112 112 ALA ALA D . n 
D  4  121 LEU 121 113 113 LEU LEU D . n 
D  4  122 ARG 122 114 114 ARG ARG D . n 
D  4  123 PHE 123 115 115 PHE PHE D . n 
D  4  124 GLY 124 116 116 GLY GLY D . n 
D  4  125 GLU 125 117 117 GLU GLU D . n 
D  4  126 GLY 126 118 ?   ?   ?   D . n 
D  4  127 ALA 127 119 ?   ?   ?   D . n 
D  4  128 SER 128 120 ?   ?   ?   D . n 
D  4  129 GLY 129 121 ?   ?   ?   D . n 
D  4  130 GLU 130 122 ?   ?   ?   D . n 
D  4  131 GLU 131 123 ?   ?   ?   D . n 
D  4  132 ARG 132 124 ?   ?   ?   D . n 
D  4  133 LEU 133 125 125 LEU LEU D . n 
D  4  134 MET 134 126 126 MET MET D . n 
D  4  135 SER 135 127 127 SER SER D . n 
D  4  136 ARG 136 128 128 ARG ARG D . n 
D  4  137 PRO 137 129 129 PRO PRO D . n 
D  4  138 PHE 138 130 130 PHE PHE D . n 
D  4  139 GLY 139 131 131 GLY GLY D . n 
D  4  140 VAL 140 132 132 VAL VAL D . n 
D  4  141 ALA 141 133 133 ALA ALA D . n 
D  4  142 LEU 142 134 134 LEU LEU D . n 
D  4  143 LEU 143 135 135 LEU LEU D . n 
D  4  144 ILE 144 136 136 ILE ILE D . n 
D  4  145 ALA 145 137 137 ALA ALA D . n 
D  4  146 GLY 146 138 138 GLY GLY D . n 
D  4  147 HIS 147 139 139 HIS HIS D . n 
D  4  148 ASP 148 140 140 ASP ASP D . n 
D  4  149 ALA 149 141 141 ALA ALA D . n 
D  4  150 ASP 150 142 142 ASP ASP D . n 
D  4  151 ASP 151 143 143 ASP ASP D . n 
D  4  152 GLY 152 144 144 GLY GLY D . n 
D  4  153 TYR 153 145 145 TYR TYR D . n 
D  4  154 GLN 154 146 146 GLN GLN D . n 
D  4  155 LEU 155 147 147 LEU LEU D . n 
D  4  156 PHE 156 148 148 PHE PHE D . n 
D  4  157 HIS 157 149 149 HIS HIS D . n 
D  4  158 ALA 158 150 150 ALA ALA D . n 
D  4  159 GLU 159 151 151 GLU GLU D . n 
D  4  160 PRO 160 152 152 PRO PRO D . n 
D  4  161 SER 161 153 153 SER SER D . n 
D  4  162 GLY 162 154 154 GLY GLY D . n 
D  4  163 THR 163 155 155 THR THR D . n 
D  4  164 PHE 164 156 156 PHE PHE D . n 
D  4  165 TYR 165 157 157 TYR TYR D . n 
D  4  166 ARG 166 158 158 ARG ARG D . n 
D  4  167 TYR 167 159 159 TYR TYR D . n 
D  4  168 ASN 168 160 160 ASN ASN D . n 
D  4  169 ALA 169 161 161 ALA ALA D . n 
D  4  170 LYS 170 162 162 LYS LYS D . n 
D  4  171 ALA 171 163 163 ALA ALA D . n 
D  4  172 ILE 172 164 164 ILE ILE D . n 
D  4  173 GLY 173 165 165 GLY GLY D . n 
D  4  174 SER 174 166 166 SER SER D . n 
D  4  175 GLY 175 167 167 GLY GLY D . n 
D  4  176 SER 176 168 168 SER SER D . n 
D  4  177 GLU 177 169 169 GLU GLU D . n 
D  4  178 GLY 178 170 170 GLY GLY D . n 
D  4  179 ALA 179 171 171 ALA ALA D . n 
D  4  180 GLN 180 172 172 GLN GLN D . n 
D  4  181 ALA 181 173 173 ALA ALA D . n 
D  4  182 GLU 182 174 174 GLU GLU D . n 
D  4  183 LEU 183 175 175 LEU LEU D . n 
D  4  184 LEU 184 176 176 LEU LEU D . n 
D  4  185 ASN 185 177 177 ASN ASN D . n 
D  4  186 GLU 186 178 178 GLU GLU D . n 
D  4  187 TRP 187 179 179 TRP TRP D . n 
D  4  188 HIS 188 180 180 HIS HIS D . n 
D  4  189 SER 189 181 181 SER SER D . n 
D  4  190 SER 190 182 182 SER SER D . n 
D  4  191 LEU 191 183 183 LEU LEU D . n 
D  4  192 THR 192 184 184 THR THR D . n 
D  4  193 LEU 193 185 185 LEU LEU D . n 
D  4  194 LYS 194 186 186 LYS LYS D . n 
D  4  195 GLU 195 187 187 GLU GLU D . n 
D  4  196 ALA 196 188 188 ALA ALA D . n 
D  4  197 GLU 197 189 189 GLU GLU D . n 
D  4  198 LEU 198 190 190 LEU LEU D . n 
D  4  199 LEU 199 191 191 LEU LEU D . n 
D  4  200 VAL 200 192 192 VAL VAL D . n 
D  4  201 LEU 201 193 193 LEU LEU D . n 
D  4  202 LYS 202 194 194 LYS LYS D . n 
D  4  203 ILE 203 195 195 ILE ILE D . n 
D  4  204 LEU 204 196 196 LEU LEU D . n 
D  4  205 LYS 205 197 197 LYS LYS D . n 
D  4  206 GLN 206 198 198 GLN GLN D . n 
D  4  207 VAL 207 199 199 VAL VAL D . n 
D  4  208 MET 208 200 200 MET MET D . n 
D  4  209 GLU 209 201 201 GLU GLU D . n 
D  4  210 GLU 210 202 202 GLU GLU D . n 
D  4  211 LYS 211 203 203 LYS LYS D . n 
D  4  212 LEU 212 204 204 LEU LEU D . n 
D  4  213 ASP 213 205 205 ASP ASP D . n 
D  4  214 GLU 214 206 206 GLU GLU D . n 
D  4  215 ASN 215 207 207 ASN ASN D . n 
D  4  216 ASN 216 208 208 ASN ASN D . n 
D  4  217 ALA 217 209 209 ALA ALA D . n 
D  4  218 GLN 218 210 210 GLN GLN D . n 
D  4  219 LEU 219 211 211 LEU LEU D . n 
D  4  220 SER 220 212 212 SER SER D . n 
D  4  221 CYS 221 213 213 CYS CYS D . n 
D  4  222 ILE 222 214 214 ILE ILE D . n 
D  4  223 THR 223 215 215 THR THR D . n 
D  4  224 LYS 224 216 216 LYS LYS D . n 
D  4  225 GLN 225 217 217 GLN GLN D . n 
D  4  226 ASP 226 218 218 ASP ASP D . n 
D  4  227 GLY 227 219 219 GLY GLY D . n 
D  4  228 PHE 228 220 220 PHE PHE D . n 
D  4  229 LYS 229 221 221 LYS LYS D . n 
D  4  230 ILE 230 222 222 ILE ILE D . n 
D  4  231 TYR 231 223 223 TYR TYR D . n 
D  4  232 ASP 232 224 224 ASP ASP D . n 
D  4  233 ASN 233 225 225 ASN ASN D . n 
D  4  234 GLU 234 226 226 GLU GLU D . n 
D  4  235 LYS 235 227 227 LYS LYS D . n 
D  4  236 THR 236 228 228 THR THR D . n 
D  4  237 ALA 237 229 229 ALA ALA D . n 
D  4  238 GLU 238 230 230 GLU GLU D . n 
D  4  239 LEU 239 231 231 LEU LEU D . n 
D  4  240 ILE 240 232 232 ILE ILE D . n 
D  4  241 LYS 241 233 233 LYS LYS D . n 
D  4  242 GLU 242 234 234 GLU GLU D . n 
D  4  243 LEU 243 235 235 LEU LEU D . n 
D  4  244 LYS 244 236 236 LYS LYS D . n 
D  4  245 GLU 245 237 237 GLU GLU D . n 
D  4  246 LYS 246 238 238 LYS LYS D . n 
D  4  247 GLU 247 239 239 GLU GLU D . n 
D  4  248 ALA 248 240 240 ALA ALA D . n 
D  4  249 ALA 249 241 241 ALA ALA D . n 
D  4  250 GLU 250 242 242 GLU GLU D . n 
D  4  251 SER 251 243 ?   ?   ?   D . n 
D  4  252 PRO 252 244 ?   ?   ?   D . n 
D  4  253 GLU 253 245 ?   ?   ?   D . n 
D  4  254 GLU 254 246 ?   ?   ?   D . n 
D  4  255 ALA 255 247 ?   ?   ?   D . n 
D  4  256 ASP 256 248 ?   ?   ?   D . n 
D  4  257 VAL 257 249 ?   ?   ?   D . n 
D  4  258 GLU 258 250 ?   ?   ?   D . n 
D  4  259 MET 259 251 ?   ?   ?   D . n 
D  4  260 SER 260 252 ?   ?   ?   D . n 
E  5  1   MET 1   0   ?   ?   ?   E . n 
E  5  2   PHE 2   1   ?   ?   ?   E . n 
E  5  3   ARG 3   2   ?   ?   ?   E . n 
E  5  4   ASN 4   3   3   ASN ASN E . n 
E  5  5   ASN 5   4   4   ASN ASN E . n 
E  5  6   TYR 6   5   5   TYR TYR E . n 
E  5  7   ASP 7   6   6   ASP ASP E . n 
E  5  8   GLY 8   7   7   GLY GLY E . n 
E  5  9   ASP 9   8   8   ASP ASP E . n 
E  5  10  THR 10  9   9   THR THR E . n 
E  5  11  VAL 11  10  10  VAL VAL E . n 
E  5  12  THR 12  11  11  THR THR E . n 
E  5  13  PHE 13  12  12  PHE PHE E . n 
E  5  14  SER 14  13  13  SER SER E . n 
E  5  15  PRO 15  14  14  PRO PRO E . n 
E  5  16  THR 16  15  15  THR THR E . n 
E  5  17  GLY 17  16  16  GLY GLY E . n 
E  5  18  ARG 18  17  17  ARG ARG E . n 
E  5  19  LEU 19  18  18  LEU LEU E . n 
E  5  20  PHE 20  19  19  PHE PHE E . n 
E  5  21  GLN 21  20  20  GLN GLN E . n 
E  5  22  VAL 22  21  21  VAL VAL E . n 
E  5  23  GLU 23  22  22  GLU GLU E . n 
E  5  24  TYR 24  23  23  TYR TYR E . n 
E  5  25  ALA 25  24  24  ALA ALA E . n 
E  5  26  LEU 26  25  25  LEU LEU E . n 
E  5  27  GLU 27  26  26  GLU GLU E . n 
E  5  28  ALA 28  27  27  ALA ALA E . n 
E  5  29  ILE 29  28  28  ILE ILE E . n 
E  5  30  LYS 30  29  29  LYS LYS E . n 
E  5  31  GLN 31  30  30  GLN GLN E . n 
E  5  32  GLY 32  31  31  GLY GLY E . n 
E  5  33  SER 33  32  32  SER SER E . n 
E  5  34  VAL 34  33  33  VAL VAL E . n 
E  5  35  THR 35  34  34  THR THR E . n 
E  5  36  VAL 36  35  35  VAL VAL E . n 
E  5  37  GLY 37  36  36  GLY GLY E . n 
E  5  38  LEU 38  37  37  LEU LEU E . n 
E  5  39  ARG 39  38  38  ARG ARG E . n 
E  5  40  SER 40  39  39  SER SER E . n 
E  5  41  ASN 41  40  40  ASN ASN E . n 
E  5  42  THR 42  41  41  THR THR E . n 
E  5  43  HIS 43  42  42  HIS HIS E . n 
E  5  44  ALA 44  43  43  ALA ALA E . n 
E  5  45  VAL 45  44  44  VAL VAL E . n 
E  5  46  LEU 46  45  45  LEU LEU E . n 
E  5  47  VAL 47  46  46  VAL VAL E . n 
E  5  48  ALA 48  47  47  ALA ALA E . n 
E  5  49  LEU 49  48  48  LEU LEU E . n 
E  5  50  LYS 50  49  49  LYS LYS E . n 
E  5  51  ARG 51  50  50  ARG ARG E . n 
E  5  52  ASN 52  51  51  ASN ASN E . n 
E  5  53  ALA 53  52  52  ALA ALA E . n 
E  5  54  ASP 54  53  53  ASP ASP E . n 
E  5  55  GLU 55  54  54  GLU GLU E . n 
E  5  56  LEU 56  55  55  LEU LEU E . n 
E  5  57  SER 57  56  56  SER SER E . n 
E  5  58  SER 58  57  57  SER SER E . n 
E  5  59  TYR 59  58  58  TYR TYR E . n 
E  5  60  GLN 60  59  59  GLN GLN E . n 
E  5  61  LYS 61  60  60  LYS LYS E . n 
E  5  62  LYS 62  61  61  LYS LYS E . n 
E  5  63  ILE 63  62  62  ILE ILE E . n 
E  5  64  ILE 64  63  63  ILE ILE E . n 
E  5  65  LYS 65  64  64  LYS LYS E . n 
E  5  66  CYS 66  65  65  CYS CYS E . n 
E  5  67  ASP 67  66  66  ASP ASP E . n 
E  5  68  GLU 68  67  67  GLU GLU E . n 
E  5  69  HIS 69  68  68  HIS HIS E . n 
E  5  70  MET 70  69  69  MET MET E . n 
E  5  71  GLY 71  70  70  GLY GLY E . n 
E  5  72  LEU 72  71  71  LEU LEU E . n 
E  5  73  SER 73  72  72  SER SER E . n 
E  5  74  LEU 74  73  73  LEU LEU E . n 
E  5  75  ALA 75  74  74  ALA ALA E . n 
E  5  76  GLY 76  75  75  GLY GLY E . n 
E  5  77  LEU 77  76  76  LEU LEU E . n 
E  5  78  ALA 78  77  77  ALA ALA E . n 
E  5  79  PRO 79  78  78  PRO PRO E . n 
E  5  80  ASP 80  79  79  ASP ASP E . n 
E  5  81  ALA 81  80  80  ALA ALA E . n 
E  5  82  ARG 82  81  81  ARG ARG E . n 
E  5  83  VAL 83  82  82  VAL VAL E . n 
E  5  84  LEU 84  83  83  LEU LEU E . n 
E  5  85  SER 85  84  84  SER SER E . n 
E  5  86  ASN 86  85  85  ASN ASN E . n 
E  5  87  TYR 87  86  86  TYR TYR E . n 
E  5  88  LEU 88  87  87  LEU LEU E . n 
E  5  89  ARG 89  88  88  ARG ARG E . n 
E  5  90  GLN 90  89  89  GLN GLN E . n 
E  5  91  GLN 91  90  90  GLN GLN E . n 
E  5  92  CYS 92  91  91  CYS CYS E . n 
E  5  93  ASN 93  92  92  ASN ASN E . n 
E  5  94  TYR 94  93  93  TYR TYR E . n 
E  5  95  SER 95  94  94  SER SER E . n 
E  5  96  SER 96  95  95  SER SER E . n 
E  5  97  LEU 97  96  96  LEU LEU E . n 
E  5  98  VAL 98  97  97  VAL VAL E . n 
E  5  99  PHE 99  98  98  PHE PHE E . n 
E  5  100 ASN 100 99  99  ASN ASN E . n 
E  5  101 ARG 101 100 100 ARG ARG E . n 
E  5  102 LYS 102 101 101 LYS LYS E . n 
E  5  103 LEU 103 102 102 LEU LEU E . n 
E  5  104 ALA 104 103 103 ALA ALA E . n 
E  5  105 VAL 105 104 104 VAL VAL E . n 
E  5  106 GLU 106 105 105 GLU GLU E . n 
E  5  107 ARG 107 106 106 ARG ARG E . n 
E  5  108 ALA 108 107 107 ALA ALA E . n 
E  5  109 GLY 109 108 108 GLY GLY E . n 
E  5  110 HIS 110 109 109 HIS HIS E . n 
E  5  111 LEU 111 110 110 LEU LEU E . n 
E  5  112 LEU 112 111 111 LEU LEU E . n 
E  5  113 CYS 113 112 112 CYS CYS E . n 
E  5  114 ASP 114 113 113 ASP ASP E . n 
E  5  115 LYS 115 114 114 LYS LYS E . n 
E  5  116 ALA 116 115 115 ALA ALA E . n 
E  5  117 GLN 117 116 116 GLN GLN E . n 
E  5  118 LYS 118 117 117 LYS LYS E . n 
E  5  119 ASN 119 118 118 ASN ASN E . n 
E  5  120 THR 120 119 119 THR THR E . n 
E  5  121 GLN 121 120 120 GLN GLN E . n 
E  5  122 SER 122 121 121 SER SER E . n 
E  5  123 TYR 123 122 122 TYR TYR E . n 
E  5  124 GLY 124 123 123 GLY GLY E . n 
E  5  125 GLY 125 124 124 GLY GLY E . n 
E  5  126 ARG 126 125 125 ARG ARG E . n 
E  5  127 PRO 127 126 126 PRO PRO E . n 
E  5  128 TYR 128 127 127 TYR TYR E . n 
E  5  129 GLY 129 128 128 GLY GLY E . n 
E  5  130 VAL 130 129 129 VAL VAL E . n 
E  5  131 GLY 131 130 130 GLY GLY E . n 
E  5  132 LEU 132 131 131 LEU LEU E . n 
E  5  133 LEU 133 132 132 LEU LEU E . n 
E  5  134 ILE 134 133 133 ILE ILE E . n 
E  5  135 ILE 135 134 134 ILE ILE E . n 
E  5  136 GLY 136 135 135 GLY GLY E . n 
E  5  137 TYR 137 136 136 TYR TYR E . n 
E  5  138 ASP 138 137 137 ASP ASP E . n 
E  5  139 LYS 139 138 138 LYS LYS E . n 
E  5  140 SER 140 139 139 SER SER E . n 
E  5  141 GLY 141 140 140 GLY GLY E . n 
E  5  142 ALA 142 141 141 ALA ALA E . n 
E  5  143 HIS 143 142 142 HIS HIS E . n 
E  5  144 LEU 144 143 143 LEU LEU E . n 
E  5  145 LEU 145 144 144 LEU LEU E . n 
E  5  146 GLU 146 145 145 GLU GLU E . n 
E  5  147 PHE 147 146 146 PHE PHE E . n 
E  5  148 GLN 148 147 147 GLN GLN E . n 
E  5  149 PRO 149 148 148 PRO PRO E . n 
E  5  150 SER 150 149 149 SER SER E . n 
E  5  151 GLY 151 150 150 GLY GLY E . n 
E  5  152 ASN 152 151 151 ASN ASN E . n 
E  5  153 VAL 153 152 152 VAL VAL E . n 
E  5  154 THR 154 153 153 THR THR E . n 
E  5  155 GLU 155 154 154 GLU GLU E . n 
E  5  156 LEU 156 155 155 LEU LEU E . n 
E  5  157 TYR 157 156 156 TYR TYR E . n 
E  5  158 GLY 158 157 157 GLY GLY E . n 
E  5  159 THR 159 158 158 THR THR E . n 
E  5  160 ALA 160 159 159 ALA ALA E . n 
E  5  161 ILE 161 160 160 ILE ILE E . n 
E  5  162 GLY 162 161 161 GLY GLY E . n 
E  5  163 ALA 163 162 162 ALA ALA E . n 
E  5  164 ARG 164 163 163 ARG ARG E . n 
E  5  165 SER 165 164 164 SER SER E . n 
E  5  166 GLN 166 165 165 GLN GLN E . n 
E  5  167 GLY 167 166 166 GLY GLY E . n 
E  5  168 ALA 168 167 167 ALA ALA E . n 
E  5  169 LYS 169 168 168 LYS LYS E . n 
E  5  170 THR 170 169 169 THR THR E . n 
E  5  171 TYR 171 170 170 TYR TYR E . n 
E  5  172 LEU 172 171 171 LEU LEU E . n 
E  5  173 GLU 173 172 172 GLU GLU E . n 
E  5  174 ARG 174 173 173 ARG ARG E . n 
E  5  175 THR 175 174 174 THR THR E . n 
E  5  176 LEU 176 175 175 LEU LEU E . n 
E  5  177 ASP 177 176 176 ASP ASP E . n 
E  5  178 THR 178 177 177 THR THR E . n 
E  5  179 PHE 179 178 178 PHE PHE E . n 
E  5  180 ILE 180 179 179 ILE ILE E . n 
E  5  181 LYS 181 180 180 LYS LYS E . n 
E  5  182 ILE 182 181 181 ILE ILE E . n 
E  5  183 ASP 183 182 182 ASP ASP E . n 
E  5  184 GLY 184 183 183 GLY GLY E . n 
E  5  185 ASN 185 184 184 ASN ASN E . n 
E  5  186 PRO 186 185 185 PRO PRO E . n 
E  5  187 ASP 187 186 186 ASP ASP E . n 
E  5  188 GLU 188 187 187 GLU GLU E . n 
E  5  189 LEU 189 188 188 LEU LEU E . n 
E  5  190 ILE 190 189 189 ILE ILE E . n 
E  5  191 LYS 191 190 190 LYS LYS E . n 
E  5  192 ALA 192 191 191 ALA ALA E . n 
E  5  193 GLY 193 192 192 GLY GLY E . n 
E  5  194 VAL 194 193 193 VAL VAL E . n 
E  5  195 GLU 195 194 194 GLU GLU E . n 
E  5  196 ALA 196 195 195 ALA ALA E . n 
E  5  197 ILE 197 196 196 ILE ILE E . n 
E  5  198 SER 198 197 197 SER SER E . n 
E  5  199 GLN 199 198 198 GLN GLN E . n 
E  5  200 SER 200 199 199 SER SER E . n 
E  5  201 LEU 201 200 200 LEU LEU E . n 
E  5  202 ARG 202 201 201 ARG ARG E . n 
E  5  203 ASP 203 202 202 ASP ASP E . n 
E  5  204 GLU 204 203 203 GLU GLU E . n 
E  5  205 SER 205 204 204 SER SER E . n 
E  5  206 LEU 206 205 205 LEU LEU E . n 
E  5  207 THR 207 206 206 THR THR E . n 
E  5  208 VAL 208 207 207 VAL VAL E . n 
E  5  209 ASP 209 208 208 ASP ASP E . n 
E  5  210 ASN 210 209 209 ASN ASN E . n 
E  5  211 LEU 211 210 210 LEU LEU E . n 
E  5  212 SER 212 211 211 SER SER E . n 
E  5  213 ILE 213 212 212 ILE ILE E . n 
E  5  214 ALA 214 213 213 ALA ALA E . n 
E  5  215 ILE 215 214 214 ILE ILE E . n 
E  5  216 VAL 216 215 215 VAL VAL E . n 
E  5  217 GLY 217 216 216 GLY GLY E . n 
E  5  218 LYS 218 217 217 LYS LYS E . n 
E  5  219 ASP 219 218 218 ASP ASP E . n 
E  5  220 THR 220 219 219 THR THR E . n 
E  5  221 PRO 221 220 220 PRO PRO E . n 
E  5  222 PHE 222 221 221 PHE PHE E . n 
E  5  223 THR 223 222 222 THR THR E . n 
E  5  224 ILE 224 223 223 ILE ILE E . n 
E  5  225 TYR 225 224 224 TYR TYR E . n 
E  5  226 ASP 226 225 225 ASP ASP E . n 
E  5  227 GLY 227 226 226 GLY GLY E . n 
E  5  228 GLU 228 227 227 GLU GLU E . n 
E  5  229 ALA 229 228 228 ALA ALA E . n 
E  5  230 VAL 230 229 229 VAL VAL E . n 
E  5  231 ALA 231 230 230 ALA ALA E . n 
E  5  232 LYS 232 231 231 LYS LYS E . n 
E  5  233 TYR 233 232 232 TYR TYR E . n 
E  5  234 ILE 234 233 233 ILE ILE E . n 
F  6  1   MET 1   -3  ?   ?   ?   F . n 
F  6  2   THR 2   -2  ?   ?   ?   F . n 
F  6  3   SER 3   -1  ?   ?   ?   F . n 
F  6  4   ILE 4   0   ?   ?   ?   F . n 
F  6  5   GLY 5   1   ?   ?   ?   F . n 
F  6  6   THR 6   2   2   THR THR F . n 
F  6  7   GLY 7   3   3   GLY GLY F . n 
F  6  8   TYR 8   4   4   TYR TYR F . n 
F  6  9   ASP 9   5   5   ASP ASP F . n 
F  6  10  LEU 10  6   6   LEU LEU F . n 
F  6  11  SER 11  7   7   SER SER F . n 
F  6  12  ASN 12  8   8   ASN ASN F . n 
F  6  13  SER 13  9   9   SER SER F . n 
F  6  14  VAL 14  10  10  VAL VAL F . n 
F  6  15  PHE 15  11  11  PHE PHE F . n 
F  6  16  SER 16  12  12  SER SER F . n 
F  6  17  PRO 17  13  13  PRO PRO F . n 
F  6  18  ASP 18  14  14  ASP ASP F . n 
F  6  19  GLY 19  15  15  GLY GLY F . n 
F  6  20  ARG 20  16  16  ARG ARG F . n 
F  6  21  ASN 21  17  17  ASN ASN F . n 
F  6  22  PHE 22  18  18  PHE PHE F . n 
F  6  23  GLN 23  19  19  GLN GLN F . n 
F  6  24  VAL 24  20  20  VAL VAL F . n 
F  6  25  GLU 25  21  21  GLU GLU F . n 
F  6  26  TYR 26  22  22  TYR TYR F . n 
F  6  27  ALA 27  23  23  ALA ALA F . n 
F  6  28  VAL 28  24  24  VAL VAL F . n 
F  6  29  LYS 29  25  25  LYS LYS F . n 
F  6  30  ALA 30  26  26  ALA ALA F . n 
F  6  31  VAL 31  27  27  VAL VAL F . n 
F  6  32  GLU 32  28  28  GLU GLU F . n 
F  6  33  ASN 33  29  29  ASN ASN F . n 
F  6  34  GLY 34  30  30  GLY GLY F . n 
F  6  35  THR 35  31  31  THR THR F . n 
F  6  36  THR 36  32  32  THR THR F . n 
F  6  37  SER 37  33  33  SER SER F . n 
F  6  38  ILE 38  34  34  ILE ILE F . n 
F  6  39  GLY 39  35  35  GLY GLY F . n 
F  6  40  ILE 40  36  36  ILE ILE F . n 
F  6  41  LYS 41  37  37  LYS LYS F . n 
F  6  42  CYS 42  38  38  CYS CYS F . n 
F  6  43  ASN 43  39  39  ASN ASN F . n 
F  6  44  ASP 44  40  40  ASP ASP F . n 
F  6  45  GLY 45  41  41  GLY GLY F . n 
F  6  46  VAL 46  42  42  VAL VAL F . n 
F  6  47  VAL 47  43  43  VAL VAL F . n 
F  6  48  PHE 48  44  44  PHE PHE F . n 
F  6  49  ALA 49  45  45  ALA ALA F . n 
F  6  50  VAL 50  46  46  VAL VAL F . n 
F  6  51  GLU 51  47  47  GLU GLU F . n 
F  6  52  LYS 52  48  48  LYS LYS F . n 
F  6  53  LEU 53  49  49  LEU LEU F . n 
F  6  54  ILE 54  50  50  ILE ILE F . n 
F  6  55  THR 55  51  51  THR THR F . n 
F  6  56  SER 56  52  52  SER SER F . n 
F  6  57  LYS 57  53  53  LYS LYS F . n 
F  6  58  LEU 58  54  54  LEU LEU F . n 
F  6  59  LEU 59  55  55  LEU LEU F . n 
F  6  60  VAL 60  56  56  VAL VAL F . n 
F  6  61  PRO 61  57  57  PRO PRO F . n 
F  6  62  GLN 62  58  58  GLN GLN F . n 
F  6  63  LYS 63  59  59  LYS LYS F . n 
F  6  64  ASN 64  60  60  ASN ASN F . n 
F  6  65  VAL 65  61  61  VAL VAL F . n 
F  6  66  LYS 66  62  62  LYS LYS F . n 
F  6  67  ILE 67  63  63  ILE ILE F . n 
F  6  68  GLN 68  64  64  GLN GLN F . n 
F  6  69  VAL 69  65  65  VAL VAL F . n 
F  6  70  VAL 70  66  66  VAL VAL F . n 
F  6  71  ASP 71  67  67  ASP ASP F . n 
F  6  72  ARG 72  68  68  ARG ARG F . n 
F  6  73  HIS 73  69  69  HIS HIS F . n 
F  6  74  ILE 74  70  70  ILE ILE F . n 
F  6  75  GLY 75  71  71  GLY GLY F . n 
F  6  76  CYS 76  72  72  CYS CYS F . n 
F  6  77  VAL 77  73  73  VAL VAL F . n 
F  6  78  TYR 78  74  74  TYR TYR F . n 
F  6  79  SER 79  75  75  SER SER F . n 
F  6  80  GLY 80  76  76  GLY GLY F . n 
F  6  81  LEU 81  77  77  LEU LEU F . n 
F  6  82  ILE 82  78  78  ILE ILE F . n 
F  6  83  PRO 83  79  79  PRO PRO F . n 
F  6  84  ASP 84  80  80  ASP ASP F . n 
F  6  85  GLY 85  81  81  GLY GLY F . n 
F  6  86  ARG 86  82  82  ARG ARG F . n 
F  6  87  HIS 87  83  83  HIS HIS F . n 
F  6  88  LEU 88  84  84  LEU LEU F . n 
F  6  89  VAL 89  85  85  VAL VAL F . n 
F  6  90  ASN 90  86  86  ASN ASN F . n 
F  6  91  ARG 91  87  87  ARG ARG F . n 
F  6  92  GLY 92  88  88  GLY GLY F . n 
F  6  93  ARG 93  89  89  ARG ARG F . n 
F  6  94  GLU 94  90  90  GLU GLU F . n 
F  6  95  GLU 95  91  91  GLU GLU F . n 
F  6  96  ALA 96  92  92  ALA ALA F . n 
F  6  97  ALA 97  93  93  ALA ALA F . n 
F  6  98  SER 98  94  94  SER SER F . n 
F  6  99  PHE 99  95  95  PHE PHE F . n 
F  6  100 LYS 100 96  96  LYS LYS F . n 
F  6  101 LYS 101 97  97  LYS LYS F . n 
F  6  102 LEU 102 98  98  LEU LEU F . n 
F  6  103 TYR 103 99  99  TYR TYR F . n 
F  6  104 LYS 104 100 100 LYS LYS F . n 
F  6  105 THR 105 101 101 THR THR F . n 
F  6  106 PRO 106 102 102 PRO PRO F . n 
F  6  107 ILE 107 103 103 ILE ILE F . n 
F  6  108 PRO 108 104 104 PRO PRO F . n 
F  6  109 ILE 109 105 105 ILE ILE F . n 
F  6  110 PRO 110 106 106 PRO PRO F . n 
F  6  111 ALA 111 107 107 ALA ALA F . n 
F  6  112 PHE 112 108 108 PHE PHE F . n 
F  6  113 ALA 113 109 109 ALA ALA F . n 
F  6  114 ASP 114 110 110 ASP ASP F . n 
F  6  115 ARG 115 111 111 ARG ARG F . n 
F  6  116 LEU 116 112 112 LEU LEU F . n 
F  6  117 GLY 117 113 113 GLY GLY F . n 
F  6  118 GLN 118 114 114 GLN GLN F . n 
F  6  119 TYR 119 115 115 TYR TYR F . n 
F  6  120 VAL 120 116 116 VAL VAL F . n 
F  6  121 GLN 121 117 117 GLN GLN F . n 
F  6  122 ALA 122 118 118 ALA ALA F . n 
F  6  123 HIS 123 119 119 HIS HIS F . n 
F  6  124 THR 124 120 120 THR THR F . n 
F  6  125 LEU 125 121 121 LEU LEU F . n 
F  6  126 TYR 126 122 122 TYR TYR F . n 
F  6  127 ASN 127 123 123 ASN ASN F . n 
F  6  128 SER 128 124 124 SER SER F . n 
F  6  129 VAL 129 125 125 VAL VAL F . n 
F  6  130 ARG 130 126 126 ARG ARG F . n 
F  6  131 PRO 131 127 127 PRO PRO F . n 
F  6  132 PHE 132 128 128 PHE PHE F . n 
F  6  133 GLY 133 129 129 GLY GLY F . n 
F  6  134 VAL 134 130 130 VAL VAL F . n 
F  6  135 SER 135 131 131 SER SER F . n 
F  6  136 THR 136 132 132 THR THR F . n 
F  6  137 ILE 137 133 133 ILE ILE F . n 
F  6  138 PHE 138 134 134 PHE PHE F . n 
F  6  139 GLY 139 135 135 GLY GLY F . n 
F  6  140 GLY 140 136 136 GLY GLY F . n 
F  6  141 VAL 141 137 137 VAL VAL F . n 
F  6  142 ASP 142 138 138 ASP ASP F . n 
F  6  143 LYS 143 139 139 LYS LYS F . n 
F  6  144 ASN 144 140 140 ASN ASN F . n 
F  6  145 GLY 145 141 141 GLY GLY F . n 
F  6  146 ALA 146 142 142 ALA ALA F . n 
F  6  147 HIS 147 143 143 HIS HIS F . n 
F  6  148 LEU 148 144 144 LEU LEU F . n 
F  6  149 TYR 149 145 145 TYR TYR F . n 
F  6  150 MET 150 146 146 MET MET F . n 
F  6  151 LEU 151 147 147 LEU LEU F . n 
F  6  152 GLU 152 148 148 GLU GLU F . n 
F  6  153 PRO 153 149 149 PRO PRO F . n 
F  6  154 SER 154 150 150 SER SER F . n 
F  6  155 GLY 155 151 151 GLY GLY F . n 
F  6  156 SER 156 152 152 SER SER F . n 
F  6  157 TYR 157 153 153 TYR TYR F . n 
F  6  158 TRP 158 154 154 TRP TRP F . n 
F  6  159 GLY 159 155 155 GLY GLY F . n 
F  6  160 TYR 160 156 156 TYR TYR F . n 
F  6  161 LYS 161 157 157 LYS LYS F . n 
F  6  162 GLY 162 158 158 GLY GLY F . n 
F  6  163 ALA 163 159 159 ALA ALA F . n 
F  6  164 ALA 164 160 160 ALA ALA F . n 
F  6  165 THR 165 161 161 THR THR F . n 
F  6  166 GLY 166 162 162 GLY GLY F . n 
F  6  167 LYS 167 163 163 LYS LYS F . n 
F  6  168 GLY 168 164 164 GLY GLY F . n 
F  6  169 ARG 169 165 165 ARG ARG F . n 
F  6  170 GLN 170 166 166 GLN GLN F . n 
F  6  171 SER 171 167 167 SER SER F . n 
F  6  172 ALA 172 168 168 ALA ALA F . n 
F  6  173 LYS 173 169 169 LYS LYS F . n 
F  6  174 ALA 174 170 170 ALA ALA F . n 
F  6  175 GLU 175 171 171 GLU GLU F . n 
F  6  176 LEU 176 172 172 LEU LEU F . n 
F  6  177 GLU 177 173 173 GLU GLU F . n 
F  6  178 LYS 178 174 174 LYS LYS F . n 
F  6  179 LEU 179 175 175 LEU LEU F . n 
F  6  180 VAL 180 176 176 VAL VAL F . n 
F  6  181 ASP 181 177 177 ASP ASP F . n 
F  6  182 HIS 182 178 178 HIS HIS F . n 
F  6  183 HIS 183 179 179 HIS HIS F . n 
F  6  184 PRO 184 180 180 PRO PRO F . n 
F  6  185 GLU 185 181 181 GLU GLU F . n 
F  6  186 GLY 186 182 182 GLY GLY F . n 
F  6  187 LEU 187 183 183 LEU LEU F . n 
F  6  188 SER 188 184 184 SER SER F . n 
F  6  189 ALA 189 185 185 ALA ALA F . n 
F  6  190 ARG 190 186 186 ARG ARG F . n 
F  6  191 GLU 191 187 187 GLU GLU F . n 
F  6  192 ALA 192 188 188 ALA ALA F . n 
F  6  193 VAL 193 189 189 VAL VAL F . n 
F  6  194 LYS 194 190 190 LYS LYS F . n 
F  6  195 GLN 195 191 191 GLN GLN F . n 
F  6  196 ALA 196 192 192 ALA ALA F . n 
F  6  197 ALA 197 193 193 ALA ALA F . n 
F  6  198 LYS 198 194 194 LYS LYS F . n 
F  6  199 ILE 199 195 195 ILE ILE F . n 
F  6  200 ILE 200 196 196 ILE ILE F . n 
F  6  201 TYR 201 197 197 TYR TYR F . n 
F  6  202 LEU 202 198 198 LEU LEU F . n 
F  6  203 ALA 203 199 199 ALA ALA F . n 
F  6  204 HIS 204 200 200 HIS HIS F . n 
F  6  205 GLU 205 201 201 GLU GLU F . n 
F  6  206 ASP 206 202 202 ASP ASP F . n 
F  6  207 ASN 207 203 203 ASN ASN F . n 
F  6  208 LYS 208 204 204 LYS LYS F . n 
F  6  209 GLU 209 205 205 GLU GLU F . n 
F  6  210 LYS 210 206 206 LYS LYS F . n 
F  6  211 ASP 211 207 207 ASP ASP F . n 
F  6  212 PHE 212 208 208 PHE PHE F . n 
F  6  213 GLU 213 209 209 GLU GLU F . n 
F  6  214 LEU 214 210 210 LEU LEU F . n 
F  6  215 GLU 215 211 211 GLU GLU F . n 
F  6  216 ILE 216 212 212 ILE ILE F . n 
F  6  217 SER 217 213 213 SER SER F . n 
F  6  218 TRP 218 214 214 TRP TRP F . n 
F  6  219 CYS 219 215 215 CYS CYS F . n 
F  6  220 SER 220 216 216 SER SER F . n 
F  6  221 LEU 221 217 217 LEU LEU F . n 
F  6  222 SER 222 218 218 SER SER F . n 
F  6  223 GLU 223 219 219 GLU GLU F . n 
F  6  224 THR 224 220 220 THR THR F . n 
F  6  225 ASN 225 221 221 ASN ASN F . n 
F  6  226 GLY 226 222 222 GLY GLY F . n 
F  6  227 LEU 227 223 223 LEU LEU F . n 
F  6  228 HIS 228 224 224 HIS HIS F . n 
F  6  229 LYS 229 225 225 LYS LYS F . n 
F  6  230 PHE 230 226 226 PHE PHE F . n 
F  6  231 VAL 231 227 227 VAL VAL F . n 
F  6  232 LYS 232 228 228 LYS LYS F . n 
F  6  233 GLY 233 229 229 GLY GLY F . n 
F  6  234 ASP 234 230 230 ASP ASP F . n 
F  6  235 LEU 235 231 231 LEU LEU F . n 
F  6  236 LEU 236 232 232 LEU LEU F . n 
F  6  237 GLN 237 233 233 GLN GLN F . n 
F  6  238 GLU 238 234 234 GLU GLU F . n 
F  6  239 ALA 239 235 235 ALA ALA F . n 
F  6  240 ILE 240 236 236 ILE ILE F . n 
F  6  241 ASP 241 237 237 ASP ASP F . n 
F  6  242 PHE 242 238 238 PHE PHE F . n 
F  6  243 ALA 243 239 239 ALA ALA F . n 
F  6  244 GLN 244 240 240 GLN GLN F . n 
F  6  245 LYS 245 241 241 LYS LYS F . n 
F  6  246 GLU 246 242 242 GLU GLU F . n 
F  6  247 ILE 247 243 243 ILE ILE F . n 
F  6  248 ASN 248 244 244 ASN ASN F . n 
F  6  249 GLY 249 245 ?   ?   ?   F . n 
F  6  250 ASP 250 246 ?   ?   ?   F . n 
F  6  251 ASP 251 247 ?   ?   ?   F . n 
F  6  252 ASP 252 248 ?   ?   ?   F . n 
F  6  253 GLU 253 249 ?   ?   ?   F . n 
F  6  254 ASP 254 250 ?   ?   ?   F . n 
F  6  255 GLU 255 251 ?   ?   ?   F . n 
F  6  256 ASP 256 252 ?   ?   ?   F . n 
F  6  257 ASP 257 253 ?   ?   ?   F . n 
F  6  258 SER 258 254 ?   ?   ?   F . n 
F  6  259 ASP 259 255 ?   ?   ?   F . n 
F  6  260 ASN 260 256 ?   ?   ?   F . n 
F  6  261 VAL 261 257 ?   ?   ?   F . n 
F  6  262 MET 262 258 ?   ?   ?   F . n 
F  6  263 SER 263 259 ?   ?   ?   F . n 
F  6  264 SER 264 260 ?   ?   ?   F . n 
F  6  265 ASP 265 261 ?   ?   ?   F . n 
F  6  266 ASP 266 262 ?   ?   ?   F . n 
F  6  267 GLU 267 263 ?   ?   ?   F . n 
F  6  268 ASN 268 264 ?   ?   ?   F . n 
F  6  269 ALA 269 265 ?   ?   ?   F . n 
F  6  270 PRO 270 266 ?   ?   ?   F . n 
F  6  271 VAL 271 267 ?   ?   ?   F . n 
F  6  272 ALA 272 268 ?   ?   ?   F . n 
F  6  273 THR 273 269 ?   ?   ?   F . n 
F  6  274 ASN 274 270 ?   ?   ?   F . n 
F  6  275 ALA 275 271 ?   ?   ?   F . n 
F  6  276 ASN 276 272 ?   ?   ?   F . n 
F  6  277 ALA 277 273 ?   ?   ?   F . n 
F  6  278 THR 278 274 ?   ?   ?   F . n 
F  6  279 THR 279 275 ?   ?   ?   F . n 
F  6  280 ASP 280 276 ?   ?   ?   F . n 
F  6  281 GLN 281 277 ?   ?   ?   F . n 
F  6  282 GLU 282 278 ?   ?   ?   F . n 
F  6  283 GLY 283 279 ?   ?   ?   F . n 
F  6  284 ASP 284 280 ?   ?   ?   F . n 
F  6  285 ILE 285 281 ?   ?   ?   F . n 
F  6  286 HIS 286 282 ?   ?   ?   F . n 
F  6  287 LEU 287 283 ?   ?   ?   F . n 
F  6  288 GLU 288 284 ?   ?   ?   F . n 
G  7  1   MET 1   -8  ?   ?   ?   G . n 
G  7  2   SER 2   -7  ?   ?   ?   G . n 
G  7  3   GLY 3   -6  ?   ?   ?   G . n 
G  7  4   ALA 4   -5  ?   ?   ?   G . n 
G  7  5   ALA 5   -4  ?   ?   ?   G . n 
G  7  6   ALA 6   -3  ?   ?   ?   G . n 
G  7  7   ALA 7   -2  ?   ?   ?   G . n 
G  7  8   SER 8   -1  ?   ?   ?   G . n 
G  7  9   ALA 9   0   ?   ?   ?   G . n 
G  7  10  ALA 10  1   ?   ?   ?   G . n 
G  7  11  GLY 11  2   2   GLY GLY G . n 
G  7  12  TYR 12  3   3   TYR TYR G . n 
G  7  13  ASP 13  4   4   ASP ASP G . n 
G  7  14  ARG 14  5   5   ARG ARG G . n 
G  7  15  HIS 15  6   6   HIS HIS G . n 
G  7  16  ILE 16  7   7   ILE ILE G . n 
G  7  17  THR 17  8   8   THR THR G . n 
G  7  18  ILE 18  9   9   ILE ILE G . n 
G  7  19  PHE 19  10  10  PHE PHE G . n 
G  7  20  SER 20  11  11  SER SER G . n 
G  7  21  PRO 21  12  12  PRO PRO G . n 
G  7  22  GLU 22  13  13  GLU GLU G . n 
G  7  23  GLY 23  14  14  GLY GLY G . n 
G  7  24  ARG 24  15  15  ARG ARG G . n 
G  7  25  LEU 25  16  16  LEU LEU G . n 
G  7  26  TYR 26  17  17  TYR TYR G . n 
G  7  27  GLN 27  18  18  GLN GLN G . n 
G  7  28  VAL 28  19  19  VAL VAL G . n 
G  7  29  GLU 29  20  20  GLU GLU G . n 
G  7  30  TYR 30  21  21  TYR TYR G . n 
G  7  31  ALA 31  22  22  ALA ALA G . n 
G  7  32  PHE 32  23  23  PHE PHE G . n 
G  7  33  LYS 33  24  24  LYS LYS G . n 
G  7  34  ALA 34  25  25  ALA ALA G . n 
G  7  35  THR 35  26  26  THR THR G . n 
G  7  36  ASN 36  27  27  ASN ASN G . n 
G  7  37  GLN 37  28  28  GLN GLN G . n 
G  7  38  THR 38  29  29  THR THR G . n 
G  7  39  ASN 39  30  30  ASN ASN G . n 
G  7  40  ILE 40  31  31  ILE ILE G . n 
G  7  41  ASN 41  32  32  ASN ASN G . n 
G  7  42  SER 42  33  33  SER SER G . n 
G  7  43  LEU 43  34  34  LEU LEU G . n 
G  7  44  ALA 44  35  35  ALA ALA G . n 
G  7  45  VAL 45  36  36  VAL VAL G . n 
G  7  46  ARG 46  37  37  ARG ARG G . n 
G  7  47  GLY 47  38  38  GLY GLY G . n 
G  7  48  LYS 48  39  39  LYS LYS G . n 
G  7  49  ASP 49  40  40  ASP ASP G . n 
G  7  50  CYS 50  41  41  CYS CYS G . n 
G  7  51  THR 51  42  42  THR THR G . n 
G  7  52  VAL 52  43  43  VAL VAL G . n 
G  7  53  VAL 53  44  44  VAL VAL G . n 
G  7  54  ILE 54  45  45  ILE ILE G . n 
G  7  55  SER 55  46  46  SER SER G . n 
G  7  56  GLN 56  47  47  GLN GLN G . n 
G  7  57  LYS 57  48  48  LYS LYS G . n 
G  7  58  LYS 58  49  49  LYS LYS G . n 
G  7  59  VAL 59  50  50  VAL VAL G . n 
G  7  60  PRO 60  51  51  PRO PRO G . n 
G  7  61  ASP 61  52  52  ASP ASP G . n 
G  7  62  LYS 62  53  53  LYS LYS G . n 
G  7  63  LEU 63  54  54  LEU LEU G . n 
G  7  64  LEU 64  55  55  LEU LEU G . n 
G  7  65  ASP 65  56  56  ASP ASP G . n 
G  7  66  PRO 66  57  57  PRO PRO G . n 
G  7  67  THR 67  58  58  THR THR G . n 
G  7  68  THR 68  59  59  THR THR G . n 
G  7  69  VAL 69  60  60  VAL VAL G . n 
G  7  70  SER 70  61  61  SER SER G . n 
G  7  71  TYR 71  62  62  TYR TYR G . n 
G  7  72  ILE 72  63  63  ILE ILE G . n 
G  7  73  PHE 73  64  64  PHE PHE G . n 
G  7  74  CYS 74  65  65  CYS CYS G . n 
G  7  75  ILE 75  66  66  ILE ILE G . n 
G  7  76  SER 76  67  67  SER SER G . n 
G  7  77  ARG 77  68  68  ARG ARG G . n 
G  7  78  THR 78  69  69  THR THR G . n 
G  7  79  ILE 79  70  70  ILE ILE G . n 
G  7  80  GLY 80  71  71  GLY GLY G . n 
G  7  81  MET 81  72  72  MET MET G . n 
G  7  82  VAL 82  73  73  VAL VAL G . n 
G  7  83  VAL 83  74  74  VAL VAL G . n 
G  7  84  ASN 84  75  75  ASN ASN G . n 
G  7  85  GLY 85  76  76  GLY GLY G . n 
G  7  86  PRO 86  77  77  PRO PRO G . n 
G  7  87  ILE 87  78  78  ILE ILE G . n 
G  7  88  PRO 88  79  79  PRO PRO G . n 
G  7  89  ASP 89  80  80  ASP ASP G . n 
G  7  90  ALA 90  81  81  ALA ALA G . n 
G  7  91  ARG 91  82  82  ARG ARG G . n 
G  7  92  ASN 92  83  83  ASN ASN G . n 
G  7  93  ALA 93  84  84  ALA ALA G . n 
G  7  94  ALA 94  85  85  ALA ALA G . n 
G  7  95  LEU 95  86  86  LEU LEU G . n 
G  7  96  ARG 96  87  87  ARG ARG G . n 
G  7  97  ALA 97  88  88  ALA ALA G . n 
G  7  98  LYS 98  89  89  LYS LYS G . n 
G  7  99  ALA 99  90  90  ALA ALA G . n 
G  7  100 GLU 100 91  91  GLU GLU G . n 
G  7  101 ALA 101 92  92  ALA ALA G . n 
G  7  102 ALA 102 93  93  ALA ALA G . n 
G  7  103 GLU 103 94  94  GLU GLU G . n 
G  7  104 PHE 104 95  95  PHE PHE G . n 
G  7  105 ARG 105 96  96  ARG ARG G . n 
G  7  106 TYR 106 97  97  TYR TYR G . n 
G  7  107 LYS 107 98  98  LYS LYS G . n 
G  7  108 TYR 108 99  99  TYR TYR G . n 
G  7  109 GLY 109 100 100 GLY GLY G . n 
G  7  110 TYR 110 101 101 TYR TYR G . n 
G  7  111 ASP 111 102 102 ASP ASP G . n 
G  7  112 MET 112 103 103 MET MET G . n 
G  7  113 PRO 113 104 104 PRO PRO G . n 
G  7  114 CYS 114 105 105 CYS CYS G . n 
G  7  115 ASP 115 106 106 ASP ASP G . n 
G  7  116 VAL 116 107 107 VAL VAL G . n 
G  7  117 LEU 117 108 108 LEU LEU G . n 
G  7  118 ALA 118 109 109 ALA ALA G . n 
G  7  119 LYS 119 110 110 LYS LYS G . n 
G  7  120 ARG 120 111 111 ARG ARG G . n 
G  7  121 MET 121 112 112 MET MET G . n 
G  7  122 ALA 122 113 113 ALA ALA G . n 
G  7  123 ASN 123 114 114 ASN ASN G . n 
G  7  124 LEU 124 115 115 LEU LEU G . n 
G  7  125 SER 125 116 116 SER SER G . n 
G  7  126 GLN 126 117 117 GLN GLN G . n 
G  7  127 ILE 127 118 118 ILE ILE G . n 
G  7  128 TYR 128 119 119 TYR TYR G . n 
G  7  129 THR 129 120 120 THR THR G . n 
G  7  130 GLN 130 121 121 GLN GLN G . n 
G  7  131 ARG 131 122 122 ARG ARG G . n 
G  7  132 ALA 132 123 123 ALA ALA G . n 
G  7  133 TYR 133 124 124 TYR TYR G . n 
G  7  134 MET 134 125 125 MET MET G . n 
G  7  135 ARG 135 126 126 ARG ARG G . n 
G  7  136 PRO 136 127 127 PRO PRO G . n 
G  7  137 LEU 137 128 128 LEU LEU G . n 
G  7  138 GLY 138 129 129 GLY GLY G . n 
G  7  139 VAL 139 130 130 VAL VAL G . n 
G  7  140 ILE 140 131 131 ILE ILE G . n 
G  7  141 LEU 141 132 132 LEU LEU G . n 
G  7  142 THR 142 133 133 THR THR G . n 
G  7  143 PHE 143 134 134 PHE PHE G . n 
G  7  144 VAL 144 135 135 VAL VAL G . n 
G  7  145 SER 145 136 136 SER SER G . n 
G  7  146 VAL 146 137 137 VAL VAL G . n 
G  7  147 ASP 147 138 138 ASP ASP G . n 
G  7  148 GLU 148 139 139 GLU GLU G . n 
G  7  149 GLU 149 140 140 GLU GLU G . n 
G  7  150 LEU 150 141 141 LEU LEU G . n 
G  7  151 GLY 151 142 142 GLY GLY G . n 
G  7  152 PRO 152 143 143 PRO PRO G . n 
G  7  153 SER 153 144 144 SER SER G . n 
G  7  154 ILE 154 145 145 ILE ILE G . n 
G  7  155 TYR 155 146 146 TYR TYR G . n 
G  7  156 LYS 156 147 147 LYS LYS G . n 
G  7  157 THR 157 148 148 THR THR G . n 
G  7  158 ASP 158 149 149 ASP ASP G . n 
G  7  159 PRO 159 150 150 PRO PRO G . n 
G  7  160 ALA 160 151 151 ALA ALA G . n 
G  7  161 GLY 161 152 152 GLY GLY G . n 
G  7  162 TYR 162 153 153 TYR TYR G . n 
G  7  163 TYR 163 154 154 TYR TYR G . n 
G  7  164 VAL 164 155 155 VAL VAL G . n 
G  7  165 GLY 165 156 156 GLY GLY G . n 
G  7  166 TYR 166 157 157 TYR TYR G . n 
G  7  167 LYS 167 158 158 LYS LYS G . n 
G  7  168 ALA 168 159 159 ALA ALA G . n 
G  7  169 THR 169 160 160 THR THR G . n 
G  7  170 ALA 170 161 161 ALA ALA G . n 
G  7  171 THR 171 162 162 THR THR G . n 
G  7  172 GLY 172 163 163 GLY GLY G . n 
G  7  173 PRO 173 164 164 PRO PRO G . n 
G  7  174 LYS 174 165 165 LYS LYS G . n 
G  7  175 GLN 175 166 166 GLN GLN G . n 
G  7  176 GLN 176 167 167 GLN GLN G . n 
G  7  177 GLU 177 168 168 GLU GLU G . n 
G  7  178 ILE 178 169 169 ILE ILE G . n 
G  7  179 THR 179 170 170 THR THR G . n 
G  7  180 THR 180 171 171 THR THR G . n 
G  7  181 ASN 181 172 172 ASN ASN G . n 
G  7  182 LEU 182 173 173 LEU LEU G . n 
G  7  183 GLU 183 174 174 GLU GLU G . n 
G  7  184 ASN 184 175 175 ASN ASN G . n 
G  7  185 HIS 185 176 176 HIS HIS G . n 
G  7  186 PHE 186 177 177 PHE PHE G . n 
G  7  187 LYS 187 178 178 LYS LYS G . n 
G  7  188 LYS 188 179 179 LYS LYS G . n 
G  7  189 SER 189 180 180 SER SER G . n 
G  7  190 LYS 190 181 181 LYS LYS G . n 
G  7  191 ILE 191 182 182 ILE ILE G . n 
G  7  192 ASP 192 183 183 ASP ASP G . n 
G  7  193 HIS 193 184 184 HIS HIS G . n 
G  7  194 ILE 194 185 185 ILE ILE G . n 
G  7  195 ASN 195 186 186 ASN ASN G . n 
G  7  196 GLU 196 187 187 GLU GLU G . n 
G  7  197 GLU 197 188 188 GLU GLU G . n 
G  7  198 SER 198 189 189 SER SER G . n 
G  7  199 TRP 199 190 190 TRP TRP G . n 
G  7  200 GLU 200 191 191 GLU GLU G . n 
G  7  201 LYS 201 192 192 LYS LYS G . n 
G  7  202 VAL 202 193 193 VAL VAL G . n 
G  7  203 VAL 203 194 194 VAL VAL G . n 
G  7  204 GLU 204 195 195 GLU GLU G . n 
G  7  205 PHE 205 196 196 PHE PHE G . n 
G  7  206 ALA 206 197 197 ALA ALA G . n 
G  7  207 ILE 207 198 198 ILE ILE G . n 
G  7  208 THR 208 199 199 THR THR G . n 
G  7  209 HIS 209 200 200 HIS HIS G . n 
G  7  210 MET 210 201 201 MET MET G . n 
G  7  211 ILE 211 202 202 ILE ILE G . n 
G  7  212 ASP 212 203 203 ASP ASP G . n 
G  7  213 ALA 213 204 204 ALA ALA G . n 
G  7  214 LEU 214 205 205 LEU LEU G . n 
G  7  215 GLY 215 206 206 GLY GLY G . n 
G  7  216 THR 216 207 207 THR THR G . n 
G  7  217 GLU 217 208 208 GLU GLU G . n 
G  7  218 PHE 218 209 209 PHE PHE G . n 
G  7  219 SER 219 210 210 SER SER G . n 
G  7  220 LYS 220 211 211 LYS LYS G . n 
G  7  221 ASN 221 212 212 ASN ASN G . n 
G  7  222 ASP 222 213 213 ASP ASP G . n 
G  7  223 LEU 223 214 214 LEU LEU G . n 
G  7  224 GLU 224 215 215 GLU GLU G . n 
G  7  225 VAL 225 216 216 VAL VAL G . n 
G  7  226 GLY 226 217 217 GLY GLY G . n 
G  7  227 VAL 227 218 218 VAL VAL G . n 
G  7  228 ALA 228 219 219 ALA ALA G . n 
G  7  229 THR 229 220 220 THR THR G . n 
G  7  230 LYS 230 221 221 LYS LYS G . n 
G  7  231 ASP 231 222 222 ASP ASP G . n 
G  7  232 LYS 232 223 223 LYS LYS G . n 
G  7  233 PHE 233 224 224 PHE PHE G . n 
G  7  234 PHE 234 225 225 PHE PHE G . n 
G  7  235 THR 235 226 226 THR THR G . n 
G  7  236 LEU 236 227 227 LEU LEU G . n 
G  7  237 SER 237 228 228 SER SER G . n 
G  7  238 ALA 238 229 229 ALA ALA G . n 
G  7  239 GLU 239 230 230 GLU GLU G . n 
G  7  240 ASN 240 231 231 ASN ASN G . n 
G  7  241 ILE 241 232 232 ILE ILE G . n 
G  7  242 GLU 242 233 233 GLU GLU G . n 
G  7  243 GLU 243 234 234 GLU GLU G . n 
G  7  244 ARG 244 235 235 ARG ARG G . n 
G  7  245 LEU 245 236 236 LEU LEU G . n 
G  7  246 VAL 246 237 237 VAL VAL G . n 
G  7  247 ALA 247 238 238 ALA ALA G . n 
G  7  248 ILE 248 239 239 ILE ILE G . n 
G  7  249 ALA 249 240 240 ALA ALA G . n 
G  7  250 GLU 250 241 241 GLU GLU G . n 
G  7  251 GLN 251 242 242 GLN GLN G . n 
G  7  252 ASP 252 243 ?   ?   ?   G . n 
H  8  1   THR 1   2   2   THR THR H . n 
H  8  2   ILE 2   3   3   ILE ILE H . n 
H  8  3   VAL 3   4   4   VAL VAL H . n 
H  8  4   GLY 4   5   5   GLY GLY H . n 
H  8  5   VAL 5   6   6   VAL VAL H . n 
H  8  6   LYS 6   7   7   LYS LYS H . n 
H  8  7   PHE 7   8   8   PHE PHE H . n 
H  8  8   ASN 8   9   9   ASN ASN H . n 
H  8  9   ASN 9   10  10  ASN ASN H . n 
H  8  10  GLY 10  11  11  GLY GLY H . n 
H  8  11  VAL 11  12  12  VAL VAL H . n 
H  8  12  VAL 12  13  13  VAL VAL H . n 
H  8  13  ILE 13  14  14  ILE ILE H . n 
H  8  14  ALA 14  15  15  ALA ALA H . n 
H  8  15  ALA 15  16  16  ALA ALA H . n 
H  8  16  ASP 16  17  17  ASP ASP H . n 
H  8  17  THR 17  18  18  THR THR H . n 
H  8  18  ARG 18  19  19  ARG ARG H . n 
H  8  19  SER 19  20  20  SER SER H . n 
H  8  20  THR 20  21  21  THR THR H . n 
H  8  21  GLN 21  22  22  GLN GLN H . n 
H  8  22  GLY 22  23  23  GLY GLY H . n 
H  8  23  PRO 23  24  24  PRO PRO H . n 
H  8  24  ILE 24  25  25  ILE ILE H . n 
H  8  25  VAL 25  26  26  VAL VAL H . n 
H  8  26  ALA 26  27  27  ALA ALA H . n 
H  8  27  ASP 27  28  28  ASP ASP H . n 
H  8  28  LYS 28  29  29  LYS LYS H . n 
H  8  29  ASN 29  30  30  ASN ASN H . n 
H  8  30  CYS 30  31  31  CYS CYS H . n 
H  8  31  ALA 31  32  32  ALA ALA H . n 
H  8  32  LYS 32  33  33  LYS LYS H . n 
H  8  33  LEU 33  34  34  LEU LEU H . n 
H  8  34  HIS 34  35  35  HIS HIS H . n 
H  8  35  ARG 35  36  36  ARG ARG H . n 
H  8  36  ILE 36  37  37  ILE ILE H . n 
H  8  37  SER 37  38  38  SER SER H . n 
H  8  38  PRO 38  39  39  PRO PRO H . n 
H  8  39  LYS 39  40  40  LYS LYS H . n 
H  8  40  ILE 40  41  41  ILE ILE H . n 
H  8  41  TRP 41  42  42  TRP TRP H . n 
H  8  42  CYS 42  43  43  CYS CYS H . n 
H  8  43  ALA 43  44  44  ALA ALA H . n 
H  8  44  GLY 44  45  45  GLY GLY H . n 
H  8  45  ALA 45  46  46  ALA ALA H . n 
H  8  46  GLY 46  47  47  GLY GLY H . n 
H  8  47  THR 47  48  48  THR THR H . n 
H  8  48  ALA 48  49  49  ALA ALA H . n 
H  8  49  ALA 49  50  50  ALA ALA H . n 
H  8  50  ASP 50  51  51  ASP ASP H . n 
H  8  51  THR 51  52  52  THR THR H . n 
H  8  52  GLU 52  53  53  GLU GLU H . n 
H  8  53  ALA 53  54  54  ALA ALA H . n 
H  8  54  VAL 54  55  55  VAL VAL H . n 
H  8  55  THR 55  56  56  THR THR H . n 
H  8  56  GLN 56  57  57  GLN GLN H . n 
H  8  57  LEU 57  58  58  LEU LEU H . n 
H  8  58  ILE 58  59  59  ILE ILE H . n 
H  8  59  GLY 59  60  60  GLY GLY H . n 
H  8  60  SER 60  61  61  SER SER H . n 
H  8  61  ASN 61  62  62  ASN ASN H . n 
H  8  62  ILE 62  63  63  ILE ILE H . n 
H  8  63  GLU 63  64  64  GLU GLU H . n 
H  8  64  LEU 64  65  65  LEU LEU H . n 
H  8  65  HIS 65  66  66  HIS HIS H . n 
H  8  66  SER 66  67  67  SER SER H . n 
H  8  67  LEU 67  68  68  LEU LEU H . n 
H  8  68  TYR 68  69  69  TYR TYR H . n 
H  8  69  THR 69  70  70  THR THR H . n 
H  8  70  SER 70  71  71  SER SER H . n 
H  8  71  ARG 71  72  72  ARG ARG H . n 
H  8  72  GLU 72  73  73  GLU GLU H . n 
H  8  73  PRO 73  74  74  PRO PRO H . n 
H  8  74  ARG 74  75  75  ARG ARG H . n 
H  8  75  VAL 75  76  76  VAL VAL H . n 
H  8  76  VAL 76  77  77  VAL VAL H . n 
H  8  77  SER 77  78  78  SER SER H . n 
H  8  78  ALA 78  79  79  ALA ALA H . n 
H  8  79  LEU 79  80  80  LEU LEU H . n 
H  8  80  GLN 80  81  81  GLN GLN H . n 
H  8  81  MET 81  82  82  MET MET H . n 
H  8  82  LEU 82  83  83  LEU LEU H . n 
H  8  83  LYS 83  84  84  LYS LYS H . n 
H  8  84  GLN 84  85  85  GLN GLN H . n 
H  8  85  HIS 85  86  86  HIS HIS H . n 
H  8  86  LEU 86  87  87  LEU LEU H . n 
H  8  87  PHE 87  88  88  PHE PHE H . n 
H  8  88  LYS 88  89  89  LYS LYS H . n 
H  8  89  TYR 89  90  90  TYR TYR H . n 
H  8  90  GLN 90  91  91  GLN GLN H . n 
H  8  91  GLY 91  92  92  GLY GLY H . n 
H  8  92  HIS 92  93  93  HIS HIS H . n 
H  8  93  ILE 93  94  94  ILE ILE H . n 
H  8  94  GLY 94  95  95  GLY GLY H . n 
H  8  95  ALA 95  96  96  ALA ALA H . n 
H  8  96  TYR 96  97  97  TYR TYR H . n 
H  8  97  LEU 97  98  98  LEU LEU H . n 
H  8  98  ILE 98  99  99  ILE ILE H . n 
H  8  99  VAL 99  100 100 VAL VAL H . n 
H  8  100 ALA 100 101 101 ALA ALA H . n 
H  8  101 GLY 101 102 102 GLY GLY H . n 
H  8  102 VAL 102 103 103 VAL VAL H . n 
H  8  103 ASP 103 104 104 ASP ASP H . n 
H  8  104 PRO 104 105 105 PRO PRO H . n 
H  8  105 THR 105 106 106 THR THR H . n 
H  8  106 GLY 106 107 107 GLY GLY H . n 
H  8  107 SER 107 108 108 SER SER H . n 
H  8  108 HIS 108 109 109 HIS HIS H . n 
H  8  109 LEU 109 110 110 LEU LEU H . n 
H  8  110 PHE 110 111 111 PHE PHE H . n 
H  8  111 SER 111 112 112 SER SER H . n 
H  8  112 ILE 112 113 113 ILE ILE H . n 
H  8  113 HIS 113 114 114 HIS HIS H . n 
H  8  114 ALA 114 115 115 ALA ALA H . n 
H  8  115 HIS 115 116 116 HIS HIS H . n 
H  8  116 GLY 116 117 117 GLY GLY H . n 
H  8  117 SER 117 118 118 SER SER H . n 
H  8  118 THR 118 119 119 THR THR H . n 
H  8  119 ASP 119 120 120 ASP ASP H . n 
H  8  120 VAL 120 121 121 VAL VAL H . n 
H  8  121 GLY 121 122 122 GLY GLY H . n 
H  8  122 TYR 122 123 123 TYR TYR H . n 
H  8  123 TYR 123 124 124 TYR TYR H . n 
H  8  124 LEU 124 125 125 LEU LEU H . n 
H  8  125 SER 125 126 126 SER SER H . n 
H  8  126 LEU 126 127 127 LEU LEU H . n 
H  8  127 GLY 127 128 128 GLY GLY H . n 
H  8  128 SER 128 129 129 SER SER H . n 
H  8  129 GLY 129 130 130 GLY GLY H . n 
H  8  130 SER 130 131 131 SER SER H . n 
H  8  131 LEU 131 132 132 LEU LEU H . n 
H  8  132 ALA 132 133 133 ALA ALA H . n 
H  8  133 ALA 133 134 134 ALA ALA H . n 
H  8  134 MET 134 135 135 MET MET H . n 
H  8  135 ALA 135 136 136 ALA ALA H . n 
H  8  136 VAL 136 137 137 VAL VAL H . n 
H  8  137 LEU 137 138 138 LEU LEU H . n 
H  8  138 GLU 138 139 139 GLU GLU H . n 
H  8  139 SER 139 140 140 SER SER H . n 
H  8  140 HIS 140 141 141 HIS HIS H . n 
H  8  141 TRP 141 142 142 TRP TRP H . n 
H  8  142 LYS 142 143 143 LYS LYS H . n 
H  8  143 GLN 143 144 144 GLN GLN H . n 
H  8  144 ASP 144 145 145 ASP ASP H . n 
H  8  145 LEU 145 146 146 LEU LEU H . n 
H  8  146 THR 146 147 147 THR THR H . n 
H  8  147 LYS 147 148 148 LYS LYS H . n 
H  8  148 GLU 148 149 149 GLU GLU H . n 
H  8  149 GLU 149 150 150 GLU GLU H . n 
H  8  150 ALA 150 151 151 ALA ALA H . n 
H  8  151 ILE 151 152 152 ILE ILE H . n 
H  8  152 LYS 152 153 153 LYS LYS H . n 
H  8  153 LEU 153 154 154 LEU LEU H . n 
H  8  154 ALA 154 155 155 ALA ALA H . n 
H  8  155 SER 155 156 156 SER SER H . n 
H  8  156 ASP 156 157 157 ASP ASP H . n 
H  8  157 ALA 157 158 158 ALA ALA H . n 
H  8  158 ILE 158 159 159 ILE ILE H . n 
H  8  159 GLN 159 160 160 GLN GLN H . n 
H  8  160 ALA 160 161 161 ALA ALA H . n 
H  8  161 GLY 161 162 162 GLY GLY H . n 
H  8  162 ILE 162 163 163 ILE ILE H . n 
H  8  163 TRP 163 164 164 TRP TRP H . n 
H  8  164 ASN 164 165 165 ASN ASN H . n 
H  8  165 ASP 165 166 166 ASP ASP H . n 
H  8  166 LEU 166 167 167 LEU LEU H . n 
H  8  167 GLY 167 168 168 GLY GLY H . n 
H  8  168 SER 168 169 169 SER SER H . n 
H  8  169 GLY 169 170 170 GLY GLY H . n 
H  8  170 SER 170 171 171 SER SER H . n 
H  8  171 ASN 171 172 172 ASN ASN H . n 
H  8  172 VAL 172 173 173 VAL VAL H . n 
H  8  173 ASP 173 174 174 ASP ASP H . n 
H  8  174 VAL 174 175 175 VAL VAL H . n 
H  8  175 CYS 175 176 176 CYS CYS H . n 
H  8  176 VAL 176 177 177 VAL VAL H . n 
H  8  177 MET 177 178 178 MET MET H . n 
H  8  178 GLU 178 179 179 GLU GLU H . n 
H  8  179 ILE 179 180 180 ILE ILE H . n 
H  8  180 GLY 180 181 181 GLY GLY H . n 
H  8  181 LYS 181 182 182 LYS LYS H . n 
H  8  182 ASP 182 183 183 ASP ASP H . n 
H  8  183 ALA 183 184 184 ALA ALA H . n 
H  8  184 GLU 184 185 185 GLU GLU H . n 
H  8  185 TYR 185 186 186 TYR TYR H . n 
H  8  186 LEU 186 187 187 LEU LEU H . n 
H  8  187 ARG 187 188 188 ARG ARG H . n 
H  8  188 ASN 188 189 189 ASN ASN H . n 
H  8  189 TYR 189 190 190 TYR TYR H . n 
H  8  190 LEU 190 191 191 LEU LEU H . n 
H  8  191 THR 191 192 192 THR THR H . n 
H  8  192 PRO 192 193 193 PRO PRO H . n 
H  8  193 ASN 193 194 194 ASN ASN H . n 
H  8  194 VAL 194 195 195 VAL VAL H . n 
H  8  195 ARG 195 196 196 ARG ARG H . n 
H  8  196 GLU 196 197 197 GLU GLU H . n 
H  8  197 GLU 197 198 198 GLU GLU H . n 
H  8  198 LYS 198 199 199 LYS LYS H . n 
H  8  199 GLN 199 200 200 GLN GLN H . n 
H  8  200 LYS 200 201 201 LYS LYS H . n 
H  8  201 SER 201 202 202 SER SER H . n 
H  8  202 TYR 202 203 203 TYR TYR H . n 
H  8  203 LYS 203 204 204 LYS LYS H . n 
H  8  204 PHE 204 205 205 PHE PHE H . n 
H  8  205 PRO 205 206 206 PRO PRO H . n 
H  8  206 ARG 206 207 207 ARG ARG H . n 
H  8  207 GLY 207 208 208 GLY GLY H . n 
H  8  208 THR 208 209 209 THR THR H . n 
H  8  209 THR 209 210 210 THR THR H . n 
H  8  210 ALA 210 211 211 ALA ALA H . n 
H  8  211 VAL 211 212 212 VAL VAL H . n 
H  8  212 LEU 212 213 213 LEU LEU H . n 
H  8  213 LYS 213 214 214 LYS LYS H . n 
H  8  214 GLU 214 215 215 GLU GLU H . n 
H  8  215 SER 215 216 216 SER SER H . n 
H  8  216 ILE 216 217 217 ILE ILE H . n 
H  8  217 VAL 217 218 218 VAL VAL H . n 
H  8  218 ASN 218 219 219 ASN ASN H . n 
H  8  219 ILE 219 220 220 ILE ILE H . n 
H  8  220 CYS 220 221 221 CYS CYS H . n 
H  8  221 ASP 221 222 222 ASP ASP H . n 
H  8  222 ILE 222 223 ?   ?   ?   H . n 
H  8  223 GLN 223 224 ?   ?   ?   H . n 
H  8  224 GLU 224 225 ?   ?   ?   H . n 
H  8  225 GLU 225 226 ?   ?   ?   H . n 
H  8  226 GLN 226 227 ?   ?   ?   H . n 
H  8  227 VAL 227 228 ?   ?   ?   H . n 
H  8  228 ASP 228 229 ?   ?   ?   H . n 
H  8  229 ILE 229 230 ?   ?   ?   H . n 
H  8  230 THR 230 231 ?   ?   ?   H . n 
H  8  231 ALA 231 232 ?   ?   ?   H . n 
I  9  1   MET 1   0   ?   ?   ?   I . n 
I  9  2   SER 2   1   1   SER SER I . n 
I  9  3   ASP 3   2   2   ASP ASP I . n 
I  9  4   PRO 4   3   3   PRO PRO I . n 
I  9  5   SER 5   4   4   SER SER I . n 
I  9  6   SER 6   5   5   SER SER I . n 
I  9  7   ILE 7   6   6   ILE ILE I . n 
I  9  8   ASN 8   7   7   ASN ASN I . n 
I  9  9   GLY 9   8   8   GLY GLY I . n 
I  9  10  GLY 10  9   9   GLY GLY I . n 
I  9  11  ILE 11  10  10  ILE ILE I . n 
I  9  12  VAL 12  11  11  VAL VAL I . n 
I  9  13  VAL 13  12  12  VAL VAL I . n 
I  9  14  ALA 14  13  13  ALA ALA I . n 
I  9  15  MET 15  14  14  MET MET I . n 
I  9  16  THR 16  15  15  THR THR I . n 
I  9  17  GLY 17  16  16  GLY GLY I . n 
I  9  18  LYS 18  17  17  LYS LYS I . n 
I  9  19  ASP 19  18  18  ASP ASP I . n 
I  9  20  CYS 20  19  19  CYS CYS I . n 
I  9  21  VAL 21  20  20  VAL VAL I . n 
I  9  22  ALA 22  21  21  ALA ALA I . n 
I  9  23  ILE 23  22  22  ILE ILE I . n 
I  9  24  ALA 24  23  23  ALA ALA I . n 
I  9  25  CYS 25  24  24  CYS CYS I . n 
I  9  26  ASP 26  25  25  ASP ASP I . n 
I  9  27  LEU 27  26  26  LEU LEU I . n 
I  9  28  ARG 28  27  27  ARG ARG I . n 
I  9  29  LEU 29  28  28  LEU LEU I . n 
I  9  30  GLY 30  29  29  GLY GLY I . n 
I  9  31  SER 31  30  30  SER SER I . n 
I  9  32  GLN 32  31  31  GLN GLN I . n 
I  9  33  SER 33  32  32  SER SER I . n 
I  9  34  LEU 34  33  33  LEU LEU I . n 
I  9  35  GLY 35  34  34  GLY GLY I . n 
I  9  36  VAL 36  35  35  VAL VAL I . n 
I  9  37  SER 37  36  36  SER SER I . n 
I  9  38  ASN 38  37  37  ASN ASN I . n 
I  9  39  LYS 39  38  38  LYS LYS I . n 
I  9  40  PHE 40  39  39  PHE PHE I . n 
I  9  41  GLU 41  40  40  GLU GLU I . n 
I  9  42  LYS 42  41  41  LYS LYS I . n 
I  9  43  ILE 43  42  42  ILE ILE I . n 
I  9  44  PHE 44  43  43  PHE PHE I . n 
I  9  45  HIS 45  44  44  HIS HIS I . n 
I  9  46  TYR 46  45  45  TYR TYR I . n 
I  9  47  GLY 47  46  46  GLY GLY I . n 
I  9  48  HIS 48  47  47  HIS HIS I . n 
I  9  49  VAL 49  48  48  VAL VAL I . n 
I  9  50  PHE 50  49  49  PHE PHE I . n 
I  9  51  LEU 51  50  50  LEU LEU I . n 
I  9  52  GLY 52  51  51  GLY GLY I . n 
I  9  53  ILE 53  52  52  ILE ILE I . n 
I  9  54  THR 54  53  53  THR THR I . n 
I  9  55  GLY 55  54  54  GLY GLY I . n 
I  9  56  LEU 56  55  55  LEU LEU I . n 
I  9  57  ALA 57  56  56  ALA ALA I . n 
I  9  58  THR 58  57  57  THR THR I . n 
I  9  59  ASP 59  58  58  ASP ASP I . n 
I  9  60  VAL 60  59  59  VAL VAL I . n 
I  9  61  THR 61  60  60  THR THR I . n 
I  9  62  THR 62  61  61  THR THR I . n 
I  9  63  LEU 63  62  62  LEU LEU I . n 
I  9  64  ASN 64  63  63  ASN ASN I . n 
I  9  65  GLU 65  64  64  GLU GLU I . n 
I  9  66  MET 66  65  65  MET MET I . n 
I  9  67  PHE 67  66  66  PHE PHE I . n 
I  9  68  ARG 68  67  67  ARG ARG I . n 
I  9  69  TYR 69  68  68  TYR TYR I . n 
I  9  70  LYS 70  69  69  LYS LYS I . n 
I  9  71  THR 71  70  70  THR THR I . n 
I  9  72  ASN 72  71  71  ASN ASN I . n 
I  9  73  LEU 73  72  72  LEU LEU I . n 
I  9  74  TYR 74  73  73  TYR TYR I . n 
I  9  75  LYS 75  74  74  LYS LYS I . n 
I  9  76  LEU 76  75  75  LEU LEU I . n 
I  9  77  LYS 77  76  76  LYS LYS I . n 
I  9  78  GLU 78  77  77  GLU GLU I . n 
I  9  79  GLU 79  78  78  GLU GLU I . n 
I  9  80  ARG 80  79  79  ARG ARG I . n 
I  9  81  ALA 81  80  80  ALA ALA I . n 
I  9  82  ILE 82  81  81  ILE ILE I . n 
I  9  83  GLU 83  82  82  GLU GLU I . n 
I  9  84  PRO 84  83  83  PRO PRO I . n 
I  9  85  GLU 85  84  84  GLU GLU I . n 
I  9  86  THR 86  85  85  THR THR I . n 
I  9  87  PHE 87  86  86  PHE PHE I . n 
I  9  88  THR 88  87  87  THR THR I . n 
I  9  89  GLN 89  88  88  GLN GLN I . n 
I  9  90  LEU 90  89  89  LEU LEU I . n 
I  9  91  VAL 91  90  90  VAL VAL I . n 
I  9  92  SER 92  91  91  SER SER I . n 
I  9  93  SER 93  92  92  SER SER I . n 
I  9  94  SER 94  93  93  SER SER I . n 
I  9  95  LEU 95  94  94  LEU LEU I . n 
I  9  96  TYR 96  95  95  TYR TYR I . n 
I  9  97  GLU 97  96  96  GLU GLU I . n 
I  9  98  ARG 98  97  97  ARG ARG I . n 
I  9  99  ARG 99  98  98  ARG ARG I . n 
I  9  100 PHE 100 99  99  PHE PHE I . n 
I  9  101 GLY 101 100 100 GLY GLY I . n 
I  9  102 PRO 102 101 101 PRO PRO I . n 
I  9  103 TYR 103 102 102 TYR TYR I . n 
I  9  104 PHE 104 103 103 PHE PHE I . n 
I  9  105 VAL 105 104 104 VAL VAL I . n 
I  9  106 GLY 106 105 105 GLY GLY I . n 
I  9  107 PRO 107 106 106 PRO PRO I . n 
I  9  108 VAL 108 107 107 VAL VAL I . n 
I  9  109 VAL 109 108 108 VAL VAL I . n 
I  9  110 ALA 110 109 109 ALA ALA I . n 
I  9  111 GLY 111 110 110 GLY GLY I . n 
I  9  112 ILE 112 111 111 ILE ILE I . n 
I  9  113 ASN 113 112 112 ASN ASN I . n 
I  9  114 SER 114 113 113 SER SER I . n 
I  9  115 LYS 115 114 114 LYS LYS I . n 
I  9  116 SER 116 115 115 SER SER I . n 
I  9  117 GLY 117 116 116 GLY GLY I . n 
I  9  118 LYS 118 117 117 LYS LYS I . n 
I  9  119 PRO 119 118 118 PRO PRO I . n 
I  9  120 PHE 120 119 119 PHE PHE I . n 
I  9  121 ILE 121 120 120 ILE ILE I . n 
I  9  122 ALA 122 121 121 ALA ALA I . n 
I  9  123 GLY 123 122 122 GLY GLY I . n 
I  9  124 PHE 124 123 123 PHE PHE I . n 
I  9  125 ASP 125 124 124 ASP ASP I . n 
I  9  126 LEU 126 125 125 LEU LEU I . n 
I  9  127 ILE 127 126 126 ILE ILE I . n 
I  9  128 GLY 128 127 127 GLY GLY I . n 
I  9  129 CYS 129 128 128 CYS CYS I . n 
I  9  130 ILE 130 129 129 ILE ILE I . n 
I  9  131 ASP 131 130 130 ASP ASP I . n 
I  9  132 GLU 132 131 131 GLU GLU I . n 
I  9  133 ALA 133 132 132 ALA ALA I . n 
I  9  134 LYS 134 133 133 LYS LYS I . n 
I  9  135 ASP 135 134 134 ASP ASP I . n 
I  9  136 PHE 136 135 135 PHE PHE I . n 
I  9  137 ILE 137 136 136 ILE ILE I . n 
I  9  138 VAL 138 137 137 VAL VAL I . n 
I  9  139 SER 139 138 138 SER SER I . n 
I  9  140 GLY 140 139 139 GLY GLY I . n 
I  9  141 THR 141 140 140 THR THR I . n 
I  9  142 ALA 142 141 141 ALA ALA I . n 
I  9  143 SER 143 142 142 SER SER I . n 
I  9  144 ASP 144 143 143 ASP ASP I . n 
I  9  145 GLN 145 144 144 GLN GLN I . n 
I  9  146 LEU 146 145 145 LEU LEU I . n 
I  9  147 PHE 147 146 146 PHE PHE I . n 
I  9  148 GLY 148 147 147 GLY GLY I . n 
I  9  149 MET 149 148 148 MET MET I . n 
I  9  150 CYS 150 149 149 CYS CYS I . n 
I  9  151 GLU 151 150 150 GLU GLU I . n 
I  9  152 SER 152 151 151 SER SER I . n 
I  9  153 LEU 153 152 152 LEU LEU I . n 
I  9  154 TYR 154 153 153 TYR TYR I . n 
I  9  155 GLU 155 154 154 GLU GLU I . n 
I  9  156 PRO 156 155 155 PRO PRO I . n 
I  9  157 ASN 157 156 156 ASN ASN I . n 
I  9  158 LEU 158 157 157 LEU LEU I . n 
I  9  159 GLU 159 158 158 GLU GLU I . n 
I  9  160 PRO 160 159 159 PRO PRO I . n 
I  9  161 GLU 161 160 160 GLU GLU I . n 
I  9  162 ASP 162 161 161 ASP ASP I . n 
I  9  163 LEU 163 162 162 LEU LEU I . n 
I  9  164 PHE 164 163 163 PHE PHE I . n 
I  9  165 GLU 165 164 164 GLU GLU I . n 
I  9  166 THR 166 165 165 THR THR I . n 
I  9  167 ILE 167 166 166 ILE ILE I . n 
I  9  168 SER 168 167 167 SER SER I . n 
I  9  169 GLN 169 168 168 GLN GLN I . n 
I  9  170 ALA 170 169 169 ALA ALA I . n 
I  9  171 LEU 171 170 170 LEU LEU I . n 
I  9  172 LEU 172 171 171 LEU LEU I . n 
I  9  173 ASN 173 172 172 ASN ASN I . n 
I  9  174 ALA 174 173 173 ALA ALA I . n 
I  9  175 ALA 175 174 174 ALA ALA I . n 
I  9  176 ASP 176 175 175 ASP ASP I . n 
I  9  177 ARG 177 176 176 ARG ARG I . n 
I  9  178 ASP 178 177 177 ASP ASP I . n 
I  9  179 ALA 179 178 178 ALA ALA I . n 
I  9  180 LEU 180 179 179 LEU LEU I . n 
I  9  181 SER 181 180 180 SER SER I . n 
I  9  182 GLY 182 181 181 GLY GLY I . n 
I  9  183 TRP 183 182 182 TRP TRP I . n 
I  9  184 GLY 184 183 183 GLY GLY I . n 
I  9  185 ALA 185 184 184 ALA ALA I . n 
I  9  186 VAL 186 185 185 VAL VAL I . n 
I  9  187 VAL 187 186 186 VAL VAL I . n 
I  9  188 TYR 188 187 187 TYR TYR I . n 
I  9  189 ILE 189 188 188 ILE ILE I . n 
I  9  190 ILE 190 189 189 ILE ILE I . n 
I  9  191 LYS 191 190 190 LYS LYS I . n 
I  9  192 LYS 192 191 191 LYS LYS I . n 
I  9  193 ASP 193 192 192 ASP ASP I . n 
I  9  194 GLU 194 193 193 GLU GLU I . n 
I  9  195 VAL 195 194 194 VAL VAL I . n 
I  9  196 VAL 196 195 195 VAL VAL I . n 
I  9  197 LYS 197 196 196 LYS LYS I . n 
I  9  198 ARG 198 197 197 ARG ARG I . n 
I  9  199 TYR 199 198 198 TYR TYR I . n 
I  9  200 LEU 200 199 199 LEU LEU I . n 
I  9  201 LYS 201 200 200 LYS LYS I . n 
I  9  202 MET 202 201 201 MET MET I . n 
I  9  203 ARG 203 202 202 ARG ARG I . n 
I  9  204 GLN 204 203 203 GLN GLN I . n 
I  9  205 ASP 205 204 204 ASP ASP I . n 
J  10 1   MET 1   1   1   MET MET J . n 
J  10 2   ASP 2   2   2   ASP ASP J . n 
J  10 3   ILE 3   3   3   ILE ILE J . n 
J  10 4   ILE 4   4   4   ILE ILE J . n 
J  10 5   LEU 5   5   5   LEU LEU J . n 
J  10 6   GLY 6   6   6   GLY GLY J . n 
J  10 7   ILE 7   7   7   ILE ILE J . n 
J  10 8   ARG 8   8   8   ARG ARG J . n 
J  10 9   VAL 9   9   9   VAL VAL J . n 
J  10 10  GLN 10  10  10  GLN GLN J . n 
J  10 11  ASP 11  11  11  ASP ASP J . n 
J  10 12  SER 12  12  12  SER SER J . n 
J  10 13  VAL 13  13  13  VAL VAL J . n 
J  10 14  ILE 14  14  14  ILE ILE J . n 
J  10 15  LEU 15  15  15  LEU LEU J . n 
J  10 16  ALA 16  16  16  ALA ALA J . n 
J  10 17  SER 17  17  17  SER SER J . n 
J  10 18  SER 18  18  18  SER SER J . n 
J  10 19  LYS 19  19  19  LYS LYS J . n 
J  10 20  ALA 20  20  20  ALA ALA J . n 
J  10 21  VAL 21  21  21  VAL VAL J . n 
J  10 22  THR 22  22  22  THR THR J . n 
J  10 23  ARG 23  23  23  ARG ARG J . n 
J  10 24  GLY 24  24  24  GLY GLY J . n 
J  10 25  ILE 25  25  25  ILE ILE J . n 
J  10 26  SER 26  26  26  SER SER J . n 
J  10 27  VAL 27  27  27  VAL VAL J . n 
J  10 28  LEU 28  28  28  LEU LEU J . n 
J  10 29  LYS 29  29  29  LYS LYS J . n 
J  10 30  ASP 30  30  30  ASP ASP J . n 
J  10 31  SER 31  31  31  SER SER J . n 
J  10 32  ASP 32  32  32  ASP ASP J . n 
J  10 33  ASP 33  33  33  ASP ASP J . n 
J  10 34  LYS 34  34  34  LYS LYS J . n 
J  10 35  THR 35  35  35  THR THR J . n 
J  10 36  ARG 36  36  36  ARG ARG J . n 
J  10 37  GLN 37  37  37  GLN GLN J . n 
J  10 38  LEU 38  38  38  LEU LEU J . n 
J  10 39  SER 39  39  39  SER SER J . n 
J  10 40  PRO 40  40  40  PRO PRO J . n 
J  10 41  HIS 41  41  41  HIS HIS J . n 
J  10 42  THR 42  42  42  THR THR J . n 
J  10 43  LEU 43  43  43  LEU LEU J . n 
J  10 44  MET 44  44  44  MET MET J . n 
J  10 45  SER 45  45  45  SER SER J . n 
J  10 46  PHE 46  46  46  PHE PHE J . n 
J  10 47  ALA 47  47  47  ALA ALA J . n 
J  10 48  GLY 48  48  48  GLY GLY J . n 
J  10 49  GLU 49  49  49  GLU GLU J . n 
J  10 50  ALA 50  50  50  ALA ALA J . n 
J  10 51  GLY 51  51  51  GLY GLY J . n 
J  10 52  ASP 52  52  52  ASP ASP J . n 
J  10 53  THR 53  53  53  THR THR J . n 
J  10 54  VAL 54  54  54  VAL VAL J . n 
J  10 55  GLN 55  55  55  GLN GLN J . n 
J  10 56  PHE 56  56  56  PHE PHE J . n 
J  10 57  ALA 57  57  57  ALA ALA J . n 
J  10 58  GLU 58  58  58  GLU GLU J . n 
J  10 59  TYR 59  59  59  TYR TYR J . n 
J  10 60  ILE 60  60  60  ILE ILE J . n 
J  10 61  GLN 61  61  61  GLN GLN J . n 
J  10 62  ALA 62  62  62  ALA ALA J . n 
J  10 63  ASN 63  63  63  ASN ASN J . n 
J  10 64  ILE 64  64  64  ILE ILE J . n 
J  10 65  GLN 65  65  65  GLN GLN J . n 
J  10 66  LEU 66  66  66  LEU LEU J . n 
J  10 67  TYR 67  67  67  TYR TYR J . n 
J  10 68  SER 68  68  68  SER SER J . n 
J  10 69  ILE 69  69  69  ILE ILE J . n 
J  10 70  ARG 70  70  70  ARG ARG J . n 
J  10 71  GLU 71  71  71  GLU GLU J . n 
J  10 72  ASP 72  72  72  ASP ASP J . n 
J  10 73  TYR 73  73  73  TYR TYR J . n 
J  10 74  GLU 74  74  74  GLU GLU J . n 
J  10 75  LEU 75  75  75  LEU LEU J . n 
J  10 76  SER 76  76  76  SER SER J . n 
J  10 77  PRO 77  77  77  PRO PRO J . n 
J  10 78  GLN 78  78  78  GLN GLN J . n 
J  10 79  ALA 79  79  79  ALA ALA J . n 
J  10 80  VAL 80  80  80  VAL VAL J . n 
J  10 81  SER 81  81  81  SER SER J . n 
J  10 82  SER 82  82  82  SER SER J . n 
J  10 83  PHE 83  83  83  PHE PHE J . n 
J  10 84  VAL 84  84  84  VAL VAL J . n 
J  10 85  ARG 85  85  85  ARG ARG J . n 
J  10 86  GLN 86  86  86  GLN GLN J . n 
J  10 87  GLU 87  87  87  GLU GLU J . n 
J  10 88  LEU 88  88  88  LEU LEU J . n 
J  10 89  ALA 89  89  89  ALA ALA J . n 
J  10 90  LYS 90  90  90  LYS LYS J . n 
J  10 91  SER 91  91  91  SER SER J . n 
J  10 92  ILE 92  92  92  ILE ILE J . n 
J  10 93  ARG 93  93  93  ARG ARG J . n 
J  10 94  SER 94  94  94  SER SER J . n 
J  10 95  ARG 95  95  95  ARG ARG J . n 
J  10 96  ARG 96  96  96  ARG ARG J . n 
J  10 97  PRO 97  97  97  PRO PRO J . n 
J  10 98  TYR 98  98  98  TYR TYR J . n 
J  10 99  GLN 99  99  99  GLN GLN J . n 
J  10 100 VAL 100 100 100 VAL VAL J . n 
J  10 101 ASN 101 101 101 ASN ASN J . n 
J  10 102 VAL 102 102 102 VAL VAL J . n 
J  10 103 LEU 103 103 103 LEU LEU J . n 
J  10 104 ILE 104 104 104 ILE ILE J . n 
J  10 105 GLY 105 105 105 GLY GLY J . n 
J  10 106 GLY 106 106 106 GLY GLY J . n 
J  10 107 TYR 107 107 107 TYR TYR J . n 
J  10 108 ASP 108 108 108 ASP ASP J . n 
J  10 109 LYS 109 109 109 LYS LYS J . n 
J  10 110 LYS 110 110 110 LYS LYS J . n 
J  10 111 LYS 111 111 111 LYS LYS J . n 
J  10 112 ASN 112 112 112 ASN ASN J . n 
J  10 113 LYS 113 113 113 LYS LYS J . n 
J  10 114 PRO 114 114 114 PRO PRO J . n 
J  10 115 GLU 115 115 115 GLU GLU J . n 
J  10 116 LEU 116 116 116 LEU LEU J . n 
J  10 117 TYR 117 117 117 TYR TYR J . n 
J  10 118 GLN 118 118 118 GLN GLN J . n 
J  10 119 ILE 119 119 119 ILE ILE J . n 
J  10 120 ASP 120 120 120 ASP ASP J . n 
J  10 121 TYR 121 121 121 TYR TYR J . n 
J  10 122 LEU 122 122 122 LEU LEU J . n 
J  10 123 GLY 123 123 123 GLY GLY J . n 
J  10 124 THR 124 124 124 THR THR J . n 
J  10 125 LYS 125 125 125 LYS LYS J . n 
J  10 126 VAL 126 126 126 VAL VAL J . n 
J  10 127 GLU 127 127 127 GLU GLU J . n 
J  10 128 LEU 128 128 128 LEU LEU J . n 
J  10 129 PRO 129 129 129 PRO PRO J . n 
J  10 130 TYR 130 130 130 TYR TYR J . n 
J  10 131 GLY 131 131 131 GLY GLY J . n 
J  10 132 ALA 132 132 132 ALA ALA J . n 
J  10 133 HIS 133 133 133 HIS HIS J . n 
J  10 134 GLY 134 134 134 GLY GLY J . n 
J  10 135 TYR 135 135 135 TYR TYR J . n 
J  10 136 SER 136 136 136 SER SER J . n 
J  10 137 GLY 137 137 137 GLY GLY J . n 
J  10 138 PHE 138 138 138 PHE PHE J . n 
J  10 139 TYR 139 139 139 TYR TYR J . n 
J  10 140 THR 140 140 140 THR THR J . n 
J  10 141 PHE 141 141 141 PHE PHE J . n 
J  10 142 SER 142 142 142 SER SER J . n 
J  10 143 LEU 143 143 143 LEU LEU J . n 
J  10 144 LEU 144 144 144 LEU LEU J . n 
J  10 145 ASP 145 145 145 ASP ASP J . n 
J  10 146 HIS 146 146 146 HIS HIS J . n 
J  10 147 HIS 147 147 147 HIS HIS J . n 
J  10 148 TYR 148 148 148 TYR TYR J . n 
J  10 149 ARG 149 149 149 ARG ARG J . n 
J  10 150 PRO 150 150 150 PRO PRO J . n 
J  10 151 ASP 151 151 151 ASP ASP J . n 
J  10 152 MET 152 152 152 MET MET J . n 
J  10 153 THR 153 153 153 THR THR J . n 
J  10 154 THR 154 154 154 THR THR J . n 
J  10 155 GLU 155 155 155 GLU GLU J . n 
J  10 156 GLU 156 156 156 GLU GLU J . n 
J  10 157 GLY 157 157 157 GLY GLY J . n 
J  10 158 LEU 158 158 158 LEU LEU J . n 
J  10 159 ASP 159 159 159 ASP ASP J . n 
J  10 160 LEU 160 160 160 LEU LEU J . n 
J  10 161 LEU 161 161 161 LEU LEU J . n 
J  10 162 LYS 162 162 162 LYS LYS J . n 
J  10 163 LEU 163 163 163 LEU LEU J . n 
J  10 164 CYS 164 164 164 CYS CYS J . n 
J  10 165 VAL 165 165 165 VAL VAL J . n 
J  10 166 GLN 166 166 166 GLN GLN J . n 
J  10 167 GLU 167 167 167 GLU GLU J . n 
J  10 168 LEU 168 168 168 LEU LEU J . n 
J  10 169 GLU 169 169 169 GLU GLU J . n 
J  10 170 LYS 170 170 170 LYS LYS J . n 
J  10 171 ARG 171 171 171 ARG ARG J . n 
J  10 172 MET 172 172 172 MET MET J . n 
J  10 173 PRO 173 173 173 PRO PRO J . n 
J  10 174 MET 174 174 174 MET MET J . n 
J  10 175 ASP 175 175 175 ASP ASP J . n 
J  10 176 PHE 176 176 176 PHE PHE J . n 
J  10 177 LYS 177 177 177 LYS LYS J . n 
J  10 178 GLY 178 178 178 GLY GLY J . n 
J  10 179 VAL 179 179 179 VAL VAL J . n 
J  10 180 ILE 180 180 180 ILE ILE J . n 
J  10 181 VAL 181 181 181 VAL VAL J . n 
J  10 182 LYS 182 182 182 LYS LYS J . n 
J  10 183 ILE 183 183 183 ILE ILE J . n 
J  10 184 VAL 184 184 184 VAL VAL J . n 
J  10 185 ASP 185 185 185 ASP ASP J . n 
J  10 186 LYS 186 186 186 LYS LYS J . n 
J  10 187 ASP 187 187 187 ASP ASP J . n 
J  10 188 GLY 188 188 188 GLY GLY J . n 
J  10 189 ILE 189 189 189 ILE ILE J . n 
J  10 190 ARG 190 190 190 ARG ARG J . n 
J  10 191 GLN 191 191 191 GLN GLN J . n 
J  10 192 VAL 192 192 192 VAL VAL J . n 
J  10 193 ASP 193 193 193 ASP ASP J . n 
J  10 194 ASP 194 194 194 ASP ASP J . n 
J  10 195 PHE 195 195 195 PHE PHE J . n 
J  10 196 GLN 196 196 ?   ?   ?   J . n 
J  10 197 ALA 197 197 ?   ?   ?   J . n 
J  10 198 GLN 198 198 ?   ?   ?   J . n 
K  11 1   THR 1   2   2   THR THR K . n 
K  11 2   THR 2   3   3   THR THR K . n 
K  11 3   LEU 3   4   4   LEU LEU K . n 
K  11 4   ALA 4   5   5   ALA ALA K . n 
K  11 5   PHE 5   6   6   PHE PHE K . n 
K  11 6   ARG 6   7   7   ARG ARG K . n 
K  11 7   PHE 7   8   8   PHE PHE K . n 
K  11 8   GLN 8   9   9   GLN GLN K . n 
K  11 9   GLY 9   10  10  GLY GLY K . n 
K  11 10  GLY 10  11  11  GLY GLY K . n 
K  11 11  ILE 11  12  12  ILE ILE K . n 
K  11 12  ILE 12  13  13  ILE ILE K . n 
K  11 13  VAL 13  14  14  VAL VAL K . n 
K  11 14  ALA 14  15  15  ALA ALA K . n 
K  11 15  VAL 15  16  16  VAL VAL K . n 
K  11 16  ASP 16  17  17  ASP ASP K . n 
K  11 17  SER 17  18  18  SER SER K . n 
K  11 18  ARG 18  19  19  ARG ARG K . n 
K  11 19  ALA 19  20  20  ALA ALA K . n 
K  11 20  THR 20  21  21  THR THR K . n 
K  11 21  ALA 21  22  22  ALA ALA K . n 
K  11 22  GLY 22  23  23  GLY GLY K . n 
K  11 23  ASN 23  24  24  ASN ASN K . n 
K  11 24  TRP 24  25  25  TRP TRP K . n 
K  11 25  VAL 25  26  26  VAL VAL K . n 
K  11 26  ALA 26  27  27  ALA ALA K . n 
K  11 27  SER 27  28  28  SER SER K . n 
K  11 28  GLN 28  29  29  GLN GLN K . n 
K  11 29  THR 29  30  30  THR THR K . n 
K  11 30  VAL 30  31  31  VAL VAL K . n 
K  11 31  LYS 31  32  32  LYS LYS K . n 
K  11 32  LYS 32  33  33  LYS LYS K . n 
K  11 33  VAL 33  34  34  VAL VAL K . n 
K  11 34  ILE 34  35  35  ILE ILE K . n 
K  11 35  GLU 35  36  36  GLU GLU K . n 
K  11 36  ILE 36  37  37  ILE ILE K . n 
K  11 37  ASN 37  38  38  ASN ASN K . n 
K  11 38  PRO 38  39  39  PRO PRO K . n 
K  11 39  PHE 39  40  40  PHE PHE K . n 
K  11 40  LEU 40  41  41  LEU LEU K . n 
K  11 41  LEU 41  42  42  LEU LEU K . n 
K  11 42  GLY 42  43  43  GLY GLY K . n 
K  11 43  THR 43  44  44  THR THR K . n 
K  11 44  MET 44  45  45  MET MET K . n 
K  11 45  ALA 45  46  46  ALA ALA K . n 
K  11 46  GLY 46  47  47  GLY GLY K . n 
K  11 47  GLY 47  48  48  GLY GLY K . n 
K  11 48  ALA 48  49  49  ALA ALA K . n 
K  11 49  ALA 49  50  50  ALA ALA K . n 
K  11 50  ASP 50  51  51  ASP ASP K . n 
K  11 51  CYS 51  52  52  CYS CYS K . n 
K  11 52  GLN 52  53  53  GLN GLN K . n 
K  11 53  PHE 53  54  54  PHE PHE K . n 
K  11 54  TRP 54  55  55  TRP TRP K . n 
K  11 55  GLU 55  56  56  GLU GLU K . n 
K  11 56  THR 56  57  57  THR THR K . n 
K  11 57  TRP 57  58  58  TRP TRP K . n 
K  11 58  LEU 58  59  59  LEU LEU K . n 
K  11 59  GLY 59  60  60  GLY GLY K . n 
K  11 60  SER 60  61  61  SER SER K . n 
K  11 61  GLN 61  62  62  GLN GLN K . n 
K  11 62  CYS 62  63  63  CYS CYS K . n 
K  11 63  ARG 63  64  64  ARG ARG K . n 
K  11 64  LEU 64  65  65  LEU LEU K . n 
K  11 65  HIS 65  66  66  HIS HIS K . n 
K  11 66  GLU 66  67  67  GLU GLU K . n 
K  11 67  LEU 67  68  68  LEU LEU K . n 
K  11 68  ARG 68  69  69  ARG ARG K . n 
K  11 69  GLU 69  70  70  GLU GLU K . n 
K  11 70  LYS 70  71  71  LYS LYS K . n 
K  11 71  GLU 71  72  72  GLU GLU K . n 
K  11 72  ARG 72  73  73  ARG ARG K . n 
K  11 73  ILE 73  74  74  ILE ILE K . n 
K  11 74  SER 74  75  75  SER SER K . n 
K  11 75  VAL 75  76  76  VAL VAL K . n 
K  11 76  ALA 76  77  77  ALA ALA K . n 
K  11 77  ALA 77  78  78  ALA ALA K . n 
K  11 78  ALA 78  79  79  ALA ALA K . n 
K  11 79  SER 79  80  80  SER SER K . n 
K  11 80  LYS 80  81  81  LYS LYS K . n 
K  11 81  ILE 81  82  82  ILE ILE K . n 
K  11 82  LEU 82  83  83  LEU LEU K . n 
K  11 83  SER 83  84  84  SER SER K . n 
K  11 84  ASN 84  85  85  ASN ASN K . n 
K  11 85  LEU 85  86  86  LEU LEU K . n 
K  11 86  VAL 86  87  87  VAL VAL K . n 
K  11 87  TYR 87  88  88  TYR TYR K . n 
K  11 88  GLN 88  89  89  GLN GLN K . n 
K  11 89  TYR 89  90  90  TYR TYR K . n 
K  11 90  LYS 90  91  91  LYS LYS K . n 
K  11 91  GLY 91  92  92  GLY GLY K . n 
K  11 92  ALA 92  93  93  ALA ALA K . n 
K  11 93  GLY 93  94  94  GLY GLY K . n 
K  11 94  LEU 94  95  95  LEU LEU K . n 
K  11 95  SER 95  96  96  SER SER K . n 
K  11 96  MET 96  97  97  MET MET K . n 
K  11 97  GLY 97  98  98  GLY GLY K . n 
K  11 98  THR 98  99  99  THR THR K . n 
K  11 99  MET 99  100 100 MET MET K . n 
K  11 100 ILE 100 101 101 ILE ILE K . n 
K  11 101 CYS 101 102 102 CYS CYS K . n 
K  11 102 GLY 102 103 103 GLY GLY K . n 
K  11 103 TYR 103 104 104 TYR TYR K . n 
K  11 104 THR 104 105 105 THR THR K . n 
K  11 105 ARG 105 106 106 ARG ARG K . n 
K  11 106 LYS 106 107 107 LYS LYS K . n 
K  11 107 GLU 107 108 108 GLU GLU K . n 
K  11 108 GLY 108 109 109 GLY GLY K . n 
K  11 109 PRO 109 110 110 PRO PRO K . n 
K  11 110 THR 110 111 111 THR THR K . n 
K  11 111 ILE 111 112 112 ILE ILE K . n 
K  11 112 TYR 112 113 113 TYR TYR K . n 
K  11 113 TYR 113 114 114 TYR TYR K . n 
K  11 114 VAL 114 115 115 VAL VAL K . n 
K  11 115 ASP 115 116 116 ASP ASP K . n 
K  11 116 SER 116 117 117 SER SER K . n 
K  11 117 ASP 117 118 118 ASP ASP K . n 
K  11 118 GLY 118 119 119 GLY GLY K . n 
K  11 119 THR 119 120 120 THR THR K . n 
K  11 120 ARG 120 121 121 ARG ARG K . n 
K  11 121 LEU 121 122 122 LEU LEU K . n 
K  11 122 LYS 122 123 123 LYS LYS K . n 
K  11 123 GLY 123 124 124 GLY GLY K . n 
K  11 124 ASP 124 125 125 ASP ASP K . n 
K  11 125 ILE 125 126 126 ILE ILE K . n 
K  11 126 PHE 126 127 127 PHE PHE K . n 
K  11 127 CYS 127 128 128 CYS CYS K . n 
K  11 128 VAL 128 129 129 VAL VAL K . n 
K  11 129 GLY 129 130 130 GLY GLY K . n 
K  11 130 SER 130 131 131 SER SER K . n 
K  11 131 GLY 131 132 132 GLY GLY K . n 
K  11 132 GLN 132 133 133 GLN GLN K . n 
K  11 133 THR 133 134 134 THR THR K . n 
K  11 134 PHE 134 135 135 PHE PHE K . n 
K  11 135 ALA 135 136 136 ALA ALA K . n 
K  11 136 TYR 136 137 137 TYR TYR K . n 
K  11 137 GLY 137 138 138 GLY GLY K . n 
K  11 138 VAL 138 139 139 VAL VAL K . n 
K  11 139 LEU 139 140 140 LEU LEU K . n 
K  11 140 ASP 140 141 141 ASP ASP K . n 
K  11 141 SER 141 142 142 SER SER K . n 
K  11 142 ASN 142 143 143 ASN ASN K . n 
K  11 143 TYR 143 144 144 TYR TYR K . n 
K  11 144 LYS 144 145 145 LYS LYS K . n 
K  11 145 TRP 145 146 146 TRP TRP K . n 
K  11 146 ASP 146 147 147 ASP ASP K . n 
K  11 147 LEU 147 148 148 LEU LEU K . n 
K  11 148 SER 148 149 149 SER SER K . n 
K  11 149 VAL 149 150 150 VAL VAL K . n 
K  11 150 GLU 150 151 151 GLU GLU K . n 
K  11 151 ASP 151 152 152 ASP ASP K . n 
K  11 152 ALA 152 153 153 ALA ALA K . n 
K  11 153 LEU 153 154 154 LEU LEU K . n 
K  11 154 TYR 154 155 155 TYR TYR K . n 
K  11 155 LEU 155 156 156 LEU LEU K . n 
K  11 156 GLY 156 157 157 GLY GLY K . n 
K  11 157 LYS 157 158 158 LYS LYS K . n 
K  11 158 ARG 158 159 159 ARG ARG K . n 
K  11 159 SER 159 160 160 SER SER K . n 
K  11 160 ILE 160 161 161 ILE ILE K . n 
K  11 161 LEU 161 162 162 LEU LEU K . n 
K  11 162 ALA 162 163 163 ALA ALA K . n 
K  11 163 ALA 163 164 164 ALA ALA K . n 
K  11 164 ALA 164 165 165 ALA ALA K . n 
K  11 165 HIS 165 166 166 HIS HIS K . n 
K  11 166 ARG 166 167 167 ARG ARG K . n 
K  11 167 ASP 167 168 168 ASP ASP K . n 
K  11 168 ALA 168 169 169 ALA ALA K . n 
K  11 169 TYR 169 170 170 TYR TYR K . n 
K  11 170 SER 170 171 171 SER SER K . n 
K  11 171 GLY 171 172 172 GLY GLY K . n 
K  11 172 GLY 172 173 173 GLY GLY K . n 
K  11 173 SER 173 174 174 SER SER K . n 
K  11 174 VAL 174 175 175 VAL VAL K . n 
K  11 175 ASN 175 176 176 ASN ASN K . n 
K  11 176 LEU 176 177 177 LEU LEU K . n 
K  11 177 TYR 177 178 178 TYR TYR K . n 
K  11 178 HIS 178 179 179 HIS HIS K . n 
K  11 179 VAL 179 180 180 VAL VAL K . n 
K  11 180 THR 180 181 181 THR THR K . n 
K  11 181 GLU 181 182 182 GLU GLU K . n 
K  11 182 ASP 182 183 183 ASP ASP K . n 
K  11 183 GLY 183 184 184 GLY GLY K . n 
K  11 184 TRP 184 185 185 TRP TRP K . n 
K  11 185 ILE 185 186 186 ILE ILE K . n 
K  11 186 TYR 186 187 187 TYR TYR K . n 
K  11 187 HIS 187 188 188 HIS HIS K . n 
K  11 188 GLY 188 189 189 GLY GLY K . n 
K  11 189 ASN 189 190 190 ASN ASN K . n 
K  11 190 HIS 190 191 191 HIS HIS K . n 
K  11 191 ASP 191 192 192 ASP ASP K . n 
K  11 192 VAL 192 193 193 VAL VAL K . n 
K  11 193 GLY 193 194 194 GLY GLY K . n 
K  11 194 GLU 194 195 195 GLU GLU K . n 
K  11 195 LEU 195 196 196 LEU LEU K . n 
K  11 196 PHE 196 197 197 PHE PHE K . n 
K  11 197 TRP 197 198 198 TRP TRP K . n 
K  11 198 LYS 198 199 199 LYS LYS K . n 
K  11 199 VAL 199 200 200 VAL VAL K . n 
K  11 200 LYS 200 201 201 LYS LYS K . n 
K  11 201 GLU 201 202 202 GLU GLU K . n 
K  11 202 GLU 202 203 203 GLU GLU K . n 
K  11 203 GLU 203 204 204 GLU GLU K . n 
K  11 204 GLY 204 205 205 GLY GLY K . n 
K  11 205 SER 205 206 206 SER SER K . n 
K  11 206 PHE 206 207 207 PHE PHE K . n 
K  11 207 ASN 207 208 208 ASN ASN K . n 
K  11 208 ASN 208 209 209 ASN ASN K . n 
K  11 209 VAL 209 210 210 VAL VAL K . n 
K  11 210 ILE 210 211 211 ILE ILE K . n 
K  11 211 GLY 211 212 212 GLY GLY K . n 
L  12 1   GLN 1   1   1   GLN GLN L . n 
L  12 2   PHE 2   2   2   PHE PHE L . n 
L  12 3   ASN 3   3   3   ASN ASN L . n 
L  12 4   PRO 4   4   4   PRO PRO L . n 
L  12 5   TYR 5   5   5   TYR TYR L . n 
L  12 6   GLY 6   6   6   GLY GLY L . n 
L  12 7   ASP 7   7   7   ASP ASP L . n 
L  12 8   ASN 8   8   8   ASN ASN L . n 
L  12 9   GLY 9   9   9   GLY GLY L . n 
L  12 10  GLY 10  10  10  GLY GLY L . n 
L  12 11  THR 11  11  11  THR THR L . n 
L  12 12  ILE 12  12  12  ILE ILE L . n 
L  12 13  LEU 13  13  13  LEU LEU L . n 
L  12 14  GLY 14  14  14  GLY GLY L . n 
L  12 15  ILE 15  15  15  ILE ILE L . n 
L  12 16  ALA 16  16  16  ALA ALA L . n 
L  12 17  GLY 17  17  17  GLY GLY L . n 
L  12 18  GLU 18  18  18  GLU GLU L . n 
L  12 19  ASP 19  19  19  ASP ASP L . n 
L  12 20  PHE 20  20  20  PHE PHE L . n 
L  12 21  ALA 21  21  21  ALA ALA L . n 
L  12 22  VAL 22  22  22  VAL VAL L . n 
L  12 23  LEU 23  23  23  LEU LEU L . n 
L  12 24  ALA 24  24  24  ALA ALA L . n 
L  12 25  GLY 25  25  25  GLY GLY L . n 
L  12 26  ASP 26  26  26  ASP ASP L . n 
L  12 27  THR 27  27  27  THR THR L . n 
L  12 28  ARG 28  28  28  ARG ARG L . n 
L  12 29  ASN 29  29  29  ASN ASN L . n 
L  12 30  ILE 30  30  30  ILE ILE L . n 
L  12 31  THR 31  31  31  THR THR L . n 
L  12 32  ASP 32  32  32  ASP ASP L . n 
L  12 33  TYR 33  33  33  TYR TYR L . n 
L  12 34  SER 34  34  34  SER SER L . n 
L  12 35  ILE 35  35  35  ILE ILE L . n 
L  12 36  ASN 36  36  36  ASN ASN L . n 
L  12 37  SER 37  37  37  SER SER L . n 
L  12 38  ARG 38  38  38  ARG ARG L . n 
L  12 39  TYR 39  39  39  TYR TYR L . n 
L  12 40  GLU 40  40  40  GLU GLU L . n 
L  12 41  PRO 41  41  41  PRO PRO L . n 
L  12 42  LYS 42  42  42  LYS LYS L . n 
L  12 43  VAL 43  43  43  VAL VAL L . n 
L  12 44  PHE 44  44  44  PHE PHE L . n 
L  12 45  ASP 45  45  45  ASP ASP L . n 
L  12 46  CYS 46  46  46  CYS CYS L . n 
L  12 47  GLY 47  47  47  GLY GLY L . n 
L  12 48  ASP 48  48  48  ASP ASP L . n 
L  12 49  ASN 49  49  49  ASN ASN L . n 
L  12 50  ILE 50  50  50  ILE ILE L . n 
L  12 51  VAL 51  51  51  VAL VAL L . n 
L  12 52  MET 52  52  52  MET MET L . n 
L  12 53  SER 53  53  53  SER SER L . n 
L  12 54  ALA 54  54  54  ALA ALA L . n 
L  12 55  ASN 55  55  55  ASN ASN L . n 
L  12 56  GLY 56  56  56  GLY GLY L . n 
L  12 57  PHE 57  57  57  PHE PHE L . n 
L  12 58  ALA 58  58  58  ALA ALA L . n 
L  12 59  ALA 59  59  59  ALA ALA L . n 
L  12 60  ASP 60  60  60  ASP ASP L . n 
L  12 61  GLY 61  61  61  GLY GLY L . n 
L  12 62  ASP 62  62  62  ASP ASP L . n 
L  12 63  ALA 63  63  63  ALA ALA L . n 
L  12 64  LEU 64  64  64  LEU LEU L . n 
L  12 65  VAL 65  65  65  VAL VAL L . n 
L  12 66  LYS 66  66  66  LYS LYS L . n 
L  12 67  ARG 67  67  67  ARG ARG L . n 
L  12 68  PHE 68  68  68  PHE PHE L . n 
L  12 69  LYS 69  69  69  LYS LYS L . n 
L  12 70  ASN 70  70  70  ASN ASN L . n 
L  12 71  SER 71  71  71  SER SER L . n 
L  12 72  VAL 72  72  72  VAL VAL L . n 
L  12 73  LYS 73  73  73  LYS LYS L . n 
L  12 74  TRP 74  74  74  TRP TRP L . n 
L  12 75  TYR 75  75  75  TYR TYR L . n 
L  12 76  HIS 76  76  76  HIS HIS L . n 
L  12 77  PHE 77  77  77  PHE PHE L . n 
L  12 78  ASP 78  78  78  ASP ASP L . n 
L  12 79  HIS 79  79  79  HIS HIS L . n 
L  12 80  ASN 80  80  80  ASN ASN L . n 
L  12 81  ASP 81  81  81  ASP ASP L . n 
L  12 82  LYS 82  82  82  LYS LYS L . n 
L  12 83  LYS 83  83  83  LYS LYS L . n 
L  12 84  LEU 84  84  84  LEU LEU L . n 
L  12 85  SER 85  85  85  SER SER L . n 
L  12 86  ILE 86  86  86  ILE ILE L . n 
L  12 87  ASN 87  87  87  ASN ASN L . n 
L  12 88  SER 88  88  88  SER SER L . n 
L  12 89  ALA 89  89  89  ALA ALA L . n 
L  12 90  ALA 90  90  90  ALA ALA L . n 
L  12 91  ARG 91  91  91  ARG ARG L . n 
L  12 92  ASN 92  92  92  ASN ASN L . n 
L  12 93  ILE 93  93  93  ILE ILE L . n 
L  12 94  GLN 94  94  94  GLN GLN L . n 
L  12 95  HIS 95  95  95  HIS HIS L . n 
L  12 96  LEU 96  96  96  LEU LEU L . n 
L  12 97  LEU 97  97  97  LEU LEU L . n 
L  12 98  TYR 98  98  98  TYR TYR L . n 
L  12 99  GLY 99  99  99  GLY GLY L . n 
L  12 100 LYS 100 100 100 LYS LYS L . n 
L  12 101 ARG 101 101 101 ARG ARG L . n 
L  12 102 PHE 102 102 102 PHE PHE L . n 
L  12 103 PHE 103 103 103 PHE PHE L . n 
L  12 104 PRO 104 104 104 PRO PRO L . n 
L  12 105 TYR 105 105 105 TYR TYR L . n 
L  12 106 TYR 106 106 106 TYR TYR L . n 
L  12 107 VAL 107 107 107 VAL VAL L . n 
L  12 108 HIS 108 108 108 HIS HIS L . n 
L  12 109 THR 109 109 109 THR THR L . n 
L  12 110 ILE 110 110 110 ILE ILE L . n 
L  12 111 ILE 111 111 111 ILE ILE L . n 
L  12 112 ALA 112 112 112 ALA ALA L . n 
L  12 113 GLY 113 113 113 GLY GLY L . n 
L  12 114 LEU 114 114 114 LEU LEU L . n 
L  12 115 ASP 115 115 115 ASP ASP L . n 
L  12 116 GLU 116 116 116 GLU GLU L . n 
L  12 117 ASP 117 117 117 ASP ASP L . n 
L  12 118 GLY 118 118 118 GLY GLY L . n 
L  12 119 LYS 119 119 119 LYS LYS L . n 
L  12 120 GLY 120 120 120 GLY GLY L . n 
L  12 121 ALA 121 121 121 ALA ALA L . n 
L  12 122 VAL 122 122 122 VAL VAL L . n 
L  12 123 TYR 123 123 123 TYR TYR L . n 
L  12 124 SER 124 124 124 SER SER L . n 
L  12 125 PHE 125 125 125 PHE PHE L . n 
L  12 126 ASP 126 126 126 ASP ASP L . n 
L  12 127 PRO 127 127 127 PRO PRO L . n 
L  12 128 VAL 128 128 128 VAL VAL L . n 
L  12 129 GLY 129 129 129 GLY GLY L . n 
L  12 130 SER 130 130 130 SER SER L . n 
L  12 131 TYR 131 131 131 TYR TYR L . n 
L  12 132 GLU 132 132 132 GLU GLU L . n 
L  12 133 ARG 133 133 133 ARG ARG L . n 
L  12 134 GLU 134 134 134 GLU GLU L . n 
L  12 135 GLN 135 135 135 GLN GLN L . n 
L  12 136 CYS 136 136 136 CYS CYS L . n 
L  12 137 ARG 137 137 137 ARG ARG L . n 
L  12 138 ALA 138 138 138 ALA ALA L . n 
L  12 139 GLY 139 139 139 GLY GLY L . n 
L  12 140 GLY 140 140 140 GLY GLY L . n 
L  12 141 ALA 141 141 141 ALA ALA L . n 
L  12 142 ALA 142 142 142 ALA ALA L . n 
L  12 143 ALA 143 143 143 ALA ALA L . n 
L  12 144 SER 144 144 144 SER SER L . n 
L  12 145 LEU 145 145 145 LEU LEU L . n 
L  12 146 ILE 146 146 146 ILE ILE L . n 
L  12 147 MET 147 147 147 MET MET L . n 
L  12 148 PRO 148 148 148 PRO PRO L . n 
L  12 149 PHE 149 149 149 PHE PHE L . n 
L  12 150 LEU 150 150 150 LEU LEU L . n 
L  12 151 ASP 151 151 151 ASP ASP L . n 
L  12 152 ASN 152 152 152 ASN ASN L . n 
L  12 153 GLN 153 153 153 GLN GLN L . n 
L  12 154 VAL 154 154 154 VAL VAL L . n 
L  12 155 ASN 155 155 155 ASN ASN L . n 
L  12 156 PHE 156 156 156 PHE PHE L . n 
L  12 157 LYS 157 157 157 LYS LYS L . n 
L  12 158 ASN 158 158 158 ASN ASN L . n 
L  12 159 GLN 159 159 159 GLN GLN L . n 
L  12 160 TYR 160 160 160 TYR TYR L . n 
L  12 161 GLU 161 161 161 GLU GLU L . n 
L  12 162 PRO 162 162 162 PRO PRO L . n 
L  12 163 GLY 163 163 163 GLY GLY L . n 
L  12 164 THR 164 164 164 THR THR L . n 
L  12 165 ASN 165 165 165 ASN ASN L . n 
L  12 166 GLY 166 166 166 GLY GLY L . n 
L  12 167 LYS 167 167 167 LYS LYS L . n 
L  12 168 VAL 168 168 168 VAL VAL L . n 
L  12 169 LYS 169 169 169 LYS LYS L . n 
L  12 170 LYS 170 170 170 LYS LYS L . n 
L  12 171 PRO 171 171 171 PRO PRO L . n 
L  12 172 LEU 172 172 172 LEU LEU L . n 
L  12 173 LYS 173 173 173 LYS LYS L . n 
L  12 174 TYR 174 174 174 TYR TYR L . n 
L  12 175 LEU 175 175 175 LEU LEU L . n 
L  12 176 SER 176 176 176 SER SER L . n 
L  12 177 VAL 177 177 177 VAL VAL L . n 
L  12 178 GLU 178 178 178 GLU GLU L . n 
L  12 179 GLU 179 179 179 GLU GLU L . n 
L  12 180 VAL 180 180 180 VAL VAL L . n 
L  12 181 ILE 181 181 181 ILE ILE L . n 
L  12 182 LYS 182 182 182 LYS LYS L . n 
L  12 183 LEU 183 183 183 LEU LEU L . n 
L  12 184 VAL 184 184 184 VAL VAL L . n 
L  12 185 ARG 185 185 185 ARG ARG L . n 
L  12 186 ASP 186 186 186 ASP ASP L . n 
L  12 187 SER 187 187 187 SER SER L . n 
L  12 188 PHE 188 188 188 PHE PHE L . n 
L  12 189 THR 189 189 189 THR THR L . n 
L  12 190 SER 190 190 190 SER SER L . n 
L  12 191 ALA 191 191 191 ALA ALA L . n 
L  12 192 THR 192 192 192 THR THR L . n 
L  12 193 GLU 193 193 193 GLU GLU L . n 
L  12 194 ARG 194 194 194 ARG ARG L . n 
L  12 195 HIS 195 195 195 HIS HIS L . n 
L  12 196 ILE 196 196 196 ILE ILE L . n 
L  12 197 GLN 197 197 197 GLN GLN L . n 
L  12 198 VAL 198 198 198 VAL VAL L . n 
L  12 199 GLY 199 199 199 GLY GLY L . n 
L  12 200 ASP 200 200 200 ASP ASP L . n 
L  12 201 GLY 201 201 201 GLY GLY L . n 
L  12 202 LEU 202 202 202 LEU LEU L . n 
L  12 203 GLU 203 203 203 GLU GLU L . n 
L  12 204 ILE 204 204 204 ILE ILE L . n 
L  12 205 LEU 205 205 205 LEU LEU L . n 
L  12 206 ILE 206 206 206 ILE ILE L . n 
L  12 207 VAL 207 207 207 VAL VAL L . n 
L  12 208 THR 208 208 208 THR THR L . n 
L  12 209 LYS 209 209 209 LYS LYS L . n 
L  12 210 ASP 210 210 210 ASP ASP L . n 
L  12 211 GLY 211 211 211 GLY GLY L . n 
L  12 212 VAL 212 212 212 VAL VAL L . n 
L  12 213 ARG 213 213 213 ARG ARG L . n 
L  12 214 LYS 214 214 214 LYS LYS L . n 
L  12 215 GLU 215 215 215 GLU GLU L . n 
L  12 216 PHE 216 216 216 PHE PHE L . n 
L  12 217 TYR 217 217 217 TYR TYR L . n 
L  12 218 GLU 218 218 218 GLU GLU L . n 
L  12 219 LEU 219 219 219 LEU LEU L . n 
L  12 220 LYS 220 220 220 LYS LYS L . n 
L  12 221 ARG 221 221 221 ARG ARG L . n 
L  12 222 ASP 222 222 222 ASP ASP L . n 
M  13 1   THR 1   -12 ?   ?   ?   M . n 
M  13 2   GLN 2   -11 ?   ?   ?   M . n 
M  13 3   ILE 3   -10 ?   ?   ?   M . n 
M  13 4   ALA 4   -9  ?   ?   ?   M . n 
M  13 5   ASN 5   -8  ?   ?   ?   M . n 
M  13 6   ALA 6   -7  ?   ?   ?   M . n 
M  13 7   GLY 7   -6  ?   ?   ?   M . n 
M  13 8   ALA 8   -5  ?   ?   ?   M . n 
M  13 9   SER 9   -4  ?   ?   ?   M . n 
M  13 10  PRO 10  -3  ?   ?   ?   M . n 
M  13 11  MET 11  -2  ?   ?   ?   M . n 
M  13 12  VAL 12  -1  ?   ?   ?   M . n 
M  13 13  ASN 13  0   ?   ?   ?   M . n 
M  13 14  THR 14  1   1   THR THR M . n 
M  13 15  GLN 15  2   2   GLN GLN M . n 
M  13 16  GLN 16  3   3   GLN GLN M . n 
M  13 17  PRO 17  4   4   PRO PRO M . n 
M  13 18  ILE 18  5   5   ILE ILE M . n 
M  13 19  VAL 19  6   6   VAL VAL M . n 
M  13 20  THR 20  7   7   THR THR M . n 
M  13 21  GLY 21  8   8   GLY GLY M . n 
M  13 22  THR 22  9   9   THR THR M . n 
M  13 23  SER 23  10  10  SER SER M . n 
M  13 24  VAL 24  11  11  VAL VAL M . n 
M  13 25  ILE 25  12  12  ILE ILE M . n 
M  13 26  SER 26  13  13  SER SER M . n 
M  13 27  MET 27  14  14  MET MET M . n 
M  13 28  LYS 28  15  15  LYS LYS M . n 
M  13 29  TYR 29  16  16  TYR TYR M . n 
M  13 30  ASP 30  17  17  ASP ASP M . n 
M  13 31  ASN 31  18  18  ASN ASN M . n 
M  13 32  GLY 32  19  19  GLY GLY M . n 
M  13 33  VAL 33  20  20  VAL VAL M . n 
M  13 34  ILE 34  21  21  ILE ILE M . n 
M  13 35  ILE 35  22  22  ILE ILE M . n 
M  13 36  ALA 36  23  23  ALA ALA M . n 
M  13 37  ALA 37  24  24  ALA ALA M . n 
M  13 38  ASP 38  25  25  ASP ASP M . n 
M  13 39  ASN 39  26  26  ASN ASN M . n 
M  13 40  LEU 40  27  27  LEU LEU M . n 
M  13 41  GLY 41  28  28  GLY GLY M . n 
M  13 42  SER 42  29  29  SER SER M . n 
M  13 43  TYR 43  30  30  TYR TYR M . n 
M  13 44  GLY 44  31  31  GLY GLY M . n 
M  13 45  SER 45  32  32  SER SER M . n 
M  13 46  LEU 46  33  33  LEU LEU M . n 
M  13 47  LEU 47  34  34  LEU LEU M . n 
M  13 48  ARG 48  35  35  ARG ARG M . n 
M  13 49  PHE 49  36  36  PHE PHE M . n 
M  13 50  ASN 50  37  37  ASN ASN M . n 
M  13 51  GLY 51  38  38  GLY GLY M . n 
M  13 52  VAL 52  39  39  VAL VAL M . n 
M  13 53  GLU 53  40  40  GLU GLU M . n 
M  13 54  ARG 54  41  41  ARG ARG M . n 
M  13 55  LEU 55  42  42  LEU LEU M . n 
M  13 56  ILE 56  43  43  ILE ILE M . n 
M  13 57  PRO 57  44  44  PRO PRO M . n 
M  13 58  VAL 58  45  45  VAL VAL M . n 
M  13 59  GLY 59  46  46  GLY GLY M . n 
M  13 60  ASP 60  47  47  ASP ASP M . n 
M  13 61  ASN 61  48  48  ASN ASN M . n 
M  13 62  THR 62  49  49  THR THR M . n 
M  13 63  VAL 63  50  50  VAL VAL M . n 
M  13 64  VAL 64  51  51  VAL VAL M . n 
M  13 65  GLY 65  52  52  GLY GLY M . n 
M  13 66  ILE 66  53  53  ILE ILE M . n 
M  13 67  SER 67  54  54  SER SER M . n 
M  13 68  GLY 68  55  55  GLY GLY M . n 
M  13 69  ASP 69  56  56  ASP ASP M . n 
M  13 70  ILE 70  57  57  ILE ILE M . n 
M  13 71  SER 71  58  58  SER SER M . n 
M  13 72  ASP 72  59  59  ASP ASP M . n 
M  13 73  MET 73  60  60  MET MET M . n 
M  13 74  GLN 74  61  61  GLN GLN M . n 
M  13 75  HIS 75  62  62  HIS HIS M . n 
M  13 76  ILE 76  63  63  ILE ILE M . n 
M  13 77  GLU 77  64  64  GLU GLU M . n 
M  13 78  ARG 78  65  65  ARG ARG M . n 
M  13 79  LEU 79  66  66  LEU LEU M . n 
M  13 80  LEU 80  67  67  LEU LEU M . n 
M  13 81  LYS 81  68  68  LYS LYS M . n 
M  13 82  ASP 82  69  69  ASP ASP M . n 
M  13 83  LEU 83  70  70  LEU LEU M . n 
M  13 84  VAL 84  71  71  VAL VAL M . n 
M  13 85  THR 85  72  72  THR THR M . n 
M  13 86  GLU 86  73  73  GLU GLU M . n 
M  13 87  ASN 87  74  74  ASN ASN M . n 
M  13 88  ALA 88  75  75  ALA ALA M . n 
M  13 89  TYR 89  76  76  TYR TYR M . n 
M  13 90  ASP 90  77  77  ASP ASP M . n 
M  13 91  ASN 91  78  78  ASN ASN M . n 
M  13 92  PRO 92  79  79  PRO PRO M . n 
M  13 93  LEU 93  80  80  LEU LEU M . n 
M  13 94  ALA 94  81  81  ALA ALA M . n 
M  13 95  ASP 95  82  82  ASP ASP M . n 
M  13 96  ALA 96  83  83  ALA ALA M . n 
M  13 97  GLU 97  84  84  GLU GLU M . n 
M  13 98  GLU 98  85  85  GLU GLU M . n 
M  13 99  ALA 99  86  86  ALA ALA M . n 
M  13 100 LEU 100 87  87  LEU LEU M . n 
M  13 101 GLU 101 88  88  GLU GLU M . n 
M  13 102 PRO 102 89  89  PRO PRO M . n 
M  13 103 SER 103 90  90  SER SER M . n 
M  13 104 TYR 104 91  91  TYR TYR M . n 
M  13 105 ILE 105 92  92  ILE ILE M . n 
M  13 106 PHE 106 93  93  PHE PHE M . n 
M  13 107 GLU 107 94  94  GLU GLU M . n 
M  13 108 TYR 108 95  95  TYR TYR M . n 
M  13 109 LEU 109 96  96  LEU LEU M . n 
M  13 110 ALA 110 97  97  ALA ALA M . n 
M  13 111 THR 111 98  98  THR THR M . n 
M  13 112 VAL 112 99  99  VAL VAL M . n 
M  13 113 MET 113 100 100 MET MET M . n 
M  13 114 TYR 114 101 101 TYR TYR M . n 
M  13 115 GLN 115 102 102 GLN GLN M . n 
M  13 116 ARG 116 103 103 ARG ARG M . n 
M  13 117 ARG 117 104 104 ARG ARG M . n 
M  13 118 SER 118 105 105 SER SER M . n 
M  13 119 LYS 119 106 106 LYS LYS M . n 
M  13 120 MET 120 107 107 MET MET M . n 
M  13 121 ASN 121 108 108 ASN ASN M . n 
M  13 122 PRO 122 109 109 PRO PRO M . n 
M  13 123 LEU 123 110 110 LEU LEU M . n 
M  13 124 TRP 124 111 111 TRP TRP M . n 
M  13 125 ASN 125 112 112 ASN ASN M . n 
M  13 126 ALA 126 113 113 ALA ALA M . n 
M  13 127 ILE 127 114 114 ILE ILE M . n 
M  13 128 ILE 128 115 115 ILE ILE M . n 
M  13 129 VAL 129 116 116 VAL VAL M . n 
M  13 130 ALA 130 117 117 ALA ALA M . n 
M  13 131 GLY 131 118 118 GLY GLY M . n 
M  13 132 VAL 132 119 119 VAL VAL M . n 
M  13 133 GLN 133 120 120 GLN GLN M . n 
M  13 134 SER 134 121 121 SER SER M . n 
M  13 135 ASN 135 122 122 ASN ASN M . n 
M  13 136 GLY 136 123 123 GLY GLY M . n 
M  13 137 ASP 137 124 124 ASP ASP M . n 
M  13 138 GLN 138 125 125 GLN GLN M . n 
M  13 139 PHE 139 126 126 PHE PHE M . n 
M  13 140 LEU 140 127 127 LEU LEU M . n 
M  13 141 ARG 141 128 128 ARG ARG M . n 
M  13 142 TYR 142 129 129 TYR TYR M . n 
M  13 143 VAL 143 130 130 VAL VAL M . n 
M  13 144 ASN 144 131 131 ASN ASN M . n 
M  13 145 LEU 145 132 132 LEU LEU M . n 
M  13 146 LEU 146 133 133 LEU LEU M . n 
M  13 147 GLY 147 134 134 GLY GLY M . n 
M  13 148 VAL 148 135 135 VAL VAL M . n 
M  13 149 THR 149 136 136 THR THR M . n 
M  13 150 TYR 150 137 137 TYR TYR M . n 
M  13 151 SER 151 138 138 SER SER M . n 
M  13 152 SER 152 139 139 SER SER M . n 
M  13 153 PRO 153 140 140 PRO PRO M . n 
M  13 154 THR 154 141 141 THR THR M . n 
M  13 155 LEU 155 142 142 LEU LEU M . n 
M  13 156 ALA 156 143 143 ALA ALA M . n 
M  13 157 THR 157 144 144 THR THR M . n 
M  13 158 GLY 158 145 145 GLY GLY M . n 
M  13 159 PHE 159 146 146 PHE PHE M . n 
M  13 160 GLY 160 147 147 GLY GLY M . n 
M  13 161 ALA 161 148 148 ALA ALA M . n 
M  13 162 HIS 162 149 149 HIS HIS M . n 
M  13 163 MET 163 150 150 MET MET M . n 
M  13 164 ALA 164 151 151 ALA ALA M . n 
M  13 165 ASN 165 152 152 ASN ASN M . n 
M  13 166 PRO 166 153 153 PRO PRO M . n 
M  13 167 LEU 167 154 154 LEU LEU M . n 
M  13 168 LEU 168 155 155 LEU LEU M . n 
M  13 169 ARG 169 156 156 ARG ARG M . n 
M  13 170 LYS 170 157 157 LYS LYS M . n 
M  13 171 VAL 171 158 158 VAL VAL M . n 
M  13 172 VAL 172 159 159 VAL VAL M . n 
M  13 173 ASP 173 160 160 ASP ASP M . n 
M  13 174 ARG 174 161 161 ARG ARG M . n 
M  13 175 GLU 175 162 162 GLU GLU M . n 
M  13 176 SER 176 163 163 SER SER M . n 
M  13 177 ASP 177 164 164 ASP ASP M . n 
M  13 178 ILE 178 165 165 ILE ILE M . n 
M  13 179 PRO 179 166 166 PRO PRO M . n 
M  13 180 LYS 180 167 167 LYS LYS M . n 
M  13 181 THR 181 168 168 THR THR M . n 
M  13 182 THR 182 169 169 THR THR M . n 
M  13 183 VAL 183 170 170 VAL VAL M . n 
M  13 184 GLN 184 171 171 GLN GLN M . n 
M  13 185 VAL 185 172 172 VAL VAL M . n 
M  13 186 ALA 186 173 173 ALA ALA M . n 
M  13 187 GLU 187 174 174 GLU GLU M . n 
M  13 188 GLU 188 175 175 GLU GLU M . n 
M  13 189 ALA 189 176 176 ALA ALA M . n 
M  13 190 ILE 190 177 177 ILE ILE M . n 
M  13 191 VAL 191 178 178 VAL VAL M . n 
M  13 192 ASN 192 179 179 ASN ASN M . n 
M  13 193 ALA 193 180 180 ALA ALA M . n 
M  13 194 MET 194 181 181 MET MET M . n 
M  13 195 ARG 195 182 182 ARG ARG M . n 
M  13 196 VAL 196 183 183 VAL VAL M . n 
M  13 197 LEU 197 184 184 LEU LEU M . n 
M  13 198 TYR 198 185 185 TYR TYR M . n 
M  13 199 TYR 199 186 186 TYR TYR M . n 
M  13 200 ARG 200 187 187 ARG ARG M . n 
M  13 201 ASP 201 188 188 ASP ASP M . n 
M  13 202 ALA 202 189 189 ALA ALA M . n 
M  13 203 ARG 203 190 190 ARG ARG M . n 
M  13 204 SER 204 191 191 SER SER M . n 
M  13 205 SER 205 192 192 SER SER M . n 
M  13 206 ARG 206 193 193 ARG ARG M . n 
M  13 207 ASN 207 194 194 ASN ASN M . n 
M  13 208 PHE 208 195 195 PHE PHE M . n 
M  13 209 SER 209 196 196 SER SER M . n 
M  13 210 LEU 210 197 197 LEU LEU M . n 
M  13 211 ALA 211 198 198 ALA ALA M . n 
M  13 212 ILE 212 199 199 ILE ILE M . n 
M  13 213 ILE 213 200 200 ILE ILE M . n 
M  13 214 ASP 214 201 201 ASP ASP M . n 
M  13 215 LYS 215 202 202 LYS LYS M . n 
M  13 216 ASN 216 203 203 ASN ASN M . n 
M  13 217 THR 217 204 204 THR THR M . n 
M  13 218 GLY 218 205 205 GLY GLY M . n 
M  13 219 LEU 219 206 206 LEU LEU M . n 
M  13 220 THR 220 207 207 THR THR M . n 
M  13 221 PHE 221 208 208 PHE PHE M . n 
M  13 222 LYS 222 209 209 LYS LYS M . n 
M  13 223 LYS 223 210 210 LYS LYS M . n 
M  13 224 ASN 224 211 211 ASN ASN M . n 
M  13 225 LEU 225 212 212 LEU LEU M . n 
M  13 226 GLN 226 213 213 GLN GLN M . n 
M  13 227 VAL 227 214 214 VAL VAL M . n 
M  13 228 GLU 228 215 215 GLU GLU M . n 
M  13 229 ASN 229 216 216 ASN ASN M . n 
M  13 230 MET 230 217 217 MET MET M . n 
M  13 231 LYS 231 218 218 LYS LYS M . n 
M  13 232 TRP 232 219 219 TRP TRP M . n 
M  13 233 ASP 233 220 220 ASP ASP M . n 
M  13 234 PHE 234 221 221 PHE PHE M . n 
M  13 235 ALA 235 222 222 ALA ALA M . n 
M  13 236 LYS 236 223 223 LYS LYS M . n 
M  13 237 ASP 237 224 224 ASP ASP M . n 
M  13 238 ILE 238 225 225 ILE ILE M . n 
M  13 239 LYS 239 226 226 LYS LYS M . n 
M  13 240 GLY 240 227 227 GLY GLY M . n 
M  13 241 TYR 241 228 228 TYR TYR M . n 
M  13 242 GLY 242 229 229 GLY GLY M . n 
M  13 243 THR 243 230 230 THR THR M . n 
M  13 244 GLN 244 231 231 GLN GLN M . n 
M  13 245 LYS 245 232 232 LYS LYS M . n 
M  13 246 ILE 246 233 233 ILE ILE M . n 
N  14 1   THR 1   1   1   THR THR N . n 
N  14 2   SER 2   2   2   SER SER N . n 
N  14 3   ILE 3   3   3   ILE ILE N . n 
N  14 4   MET 4   4   4   MET MET N . n 
N  14 5   ALA 5   5   5   ALA ALA N . n 
N  14 6   VAL 6   6   6   VAL VAL N . n 
N  14 7   THR 7   7   7   THR THR N . n 
N  14 8   PHE 8   8   8   PHE PHE N . n 
N  14 9   LYS 9   9   9   LYS LYS N . n 
N  14 10  ASP 10  10  10  ASP ASP N . n 
N  14 11  GLY 11  11  11  GLY GLY N . n 
N  14 12  VAL 12  12  12  VAL VAL N . n 
N  14 13  ILE 13  13  13  ILE ILE N . n 
N  14 14  LEU 14  14  14  LEU LEU N . n 
N  14 15  GLY 15  15  15  GLY GLY N . n 
N  14 16  ALA 16  16  16  ALA ALA N . n 
N  14 17  ASP 17  17  17  ASP ASP N . n 
N  14 18  SER 18  18  18  SER SER N . n 
N  14 19  ARG 19  19  19  ARG ARG N . n 
N  14 20  THR 20  20  20  THR THR N . n 
N  14 21  THR 21  21  21  THR THR N . n 
N  14 22  THR 22  22  22  THR THR N . n 
N  14 23  GLY 23  23  23  GLY GLY N . n 
N  14 24  ALA 24  24  24  ALA ALA N . n 
N  14 25  TYR 25  25  25  TYR TYR N . n 
N  14 26  ILE 26  26  26  ILE ILE N . n 
N  14 27  ALA 27  27  27  ALA ALA N . n 
N  14 28  ASN 28  28  28  ASN ASN N . n 
N  14 29  ARG 29  29  29  ARG ARG N . n 
N  14 30  VAL 30  30  30  VAL VAL N . n 
N  14 31  THR 31  31  31  THR THR N . n 
N  14 32  ASP 32  32  32  ASP ASP N . n 
N  14 33  LYS 33  33  33  LYS LYS N . n 
N  14 34  LEU 34  34  34  LEU LEU N . n 
N  14 35  THR 35  35  35  THR THR N . n 
N  14 36  ARG 36  36  36  ARG ARG N . n 
N  14 37  VAL 37  37  37  VAL VAL N . n 
N  14 38  HIS 38  38  38  HIS HIS N . n 
N  14 39  ASP 39  39  39  ASP ASP N . n 
N  14 40  LYS 40  40  40  LYS LYS N . n 
N  14 41  ILE 41  41  41  ILE ILE N . n 
N  14 42  TRP 42  42  42  TRP TRP N . n 
N  14 43  CYS 43  43  43  CYS CYS N . n 
N  14 44  CYS 44  44  44  CYS CYS N . n 
N  14 45  ARG 45  45  45  ARG ARG N . n 
N  14 46  SER 46  46  46  SER SER N . n 
N  14 47  GLY 47  47  47  GLY GLY N . n 
N  14 48  SER 48  48  48  SER SER N . n 
N  14 49  ALA 49  49  49  ALA ALA N . n 
N  14 50  ALA 50  50  50  ALA ALA N . n 
N  14 51  ASP 51  51  51  ASP ASP N . n 
N  14 52  THR 52  52  52  THR THR N . n 
N  14 53  GLN 53  53  53  GLN GLN N . n 
N  14 54  ALA 54  54  54  ALA ALA N . n 
N  14 55  ILE 55  55  55  ILE ILE N . n 
N  14 56  ALA 56  56  56  ALA ALA N . n 
N  14 57  ASP 57  57  57  ASP ASP N . n 
N  14 58  ILE 58  58  58  ILE ILE N . n 
N  14 59  VAL 59  59  59  VAL VAL N . n 
N  14 60  GLN 60  60  60  GLN GLN N . n 
N  14 61  TYR 61  61  61  TYR TYR N . n 
N  14 62  HIS 62  62  62  HIS HIS N . n 
N  14 63  LEU 63  63  63  LEU LEU N . n 
N  14 64  GLU 64  64  64  GLU GLU N . n 
N  14 65  LEU 65  65  65  LEU LEU N . n 
N  14 66  TYR 66  66  66  TYR TYR N . n 
N  14 67  THR 67  67  67  THR THR N . n 
N  14 68  SER 68  68  68  SER SER N . n 
N  14 69  GLN 69  69  69  GLN GLN N . n 
N  14 70  TYR 70  70  70  TYR TYR N . n 
N  14 71  GLY 71  71  71  GLY GLY N . n 
N  14 72  THR 72  72  72  THR THR N . n 
N  14 73  PRO 73  73  73  PRO PRO N . n 
N  14 74  SER 74  74  74  SER SER N . n 
N  14 75  THR 75  75  75  THR THR N . n 
N  14 76  GLU 76  76  76  GLU GLU N . n 
N  14 77  THR 77  77  77  THR THR N . n 
N  14 78  ALA 78  78  78  ALA ALA N . n 
N  14 79  ALA 79  79  79  ALA ALA N . n 
N  14 80  SER 80  80  80  SER SER N . n 
N  14 81  VAL 81  81  81  VAL VAL N . n 
N  14 82  PHE 82  82  82  PHE PHE N . n 
N  14 83  LYS 83  83  83  LYS LYS N . n 
N  14 84  GLU 84  84  84  GLU GLU N . n 
N  14 85  LEU 85  85  85  LEU LEU N . n 
N  14 86  CYS 86  86  86  CYS CYS N . n 
N  14 87  TYR 87  87  87  TYR TYR N . n 
N  14 88  GLU 88  88  88  GLU GLU N . n 
N  14 89  ASN 89  89  89  ASN ASN N . n 
N  14 90  LYS 90  90  90  LYS LYS N . n 
N  14 91  ASP 91  91  91  ASP ASP N . n 
N  14 92  ASN 92  92  92  ASN ASN N . n 
N  14 93  LEU 93  93  93  LEU LEU N . n 
N  14 94  THR 94  94  94  THR THR N . n 
N  14 95  ALA 95  95  95  ALA ALA N . n 
N  14 96  GLY 96  96  96  GLY GLY N . n 
N  14 97  ILE 97  97  97  ILE ILE N . n 
N  14 98  ILE 98  98  98  ILE ILE N . n 
N  14 99  VAL 99  99  99  VAL VAL N . n 
N  14 100 ALA 100 100 100 ALA ALA N . n 
N  14 101 GLY 101 101 101 GLY GLY N . n 
N  14 102 TYR 102 102 102 TYR TYR N . n 
N  14 103 ASP 103 103 103 ASP ASP N . n 
N  14 104 ASP 104 104 104 ASP ASP N . n 
N  14 105 LYS 105 105 105 LYS LYS N . n 
N  14 106 ASN 106 106 106 ASN ASN N . n 
N  14 107 LYS 107 107 107 LYS LYS N . n 
N  14 108 GLY 108 108 108 GLY GLY N . n 
N  14 109 GLU 109 109 109 GLU GLU N . n 
N  14 110 VAL 110 110 110 VAL VAL N . n 
N  14 111 TYR 111 111 111 TYR TYR N . n 
N  14 112 THR 112 112 112 THR THR N . n 
N  14 113 ILE 113 113 113 ILE ILE N . n 
N  14 114 PRO 114 114 114 PRO PRO N . n 
N  14 115 LEU 115 115 115 LEU LEU N . n 
N  14 116 GLY 116 116 116 GLY GLY N . n 
N  14 117 GLY 117 117 117 GLY GLY N . n 
N  14 118 SER 118 118 118 SER SER N . n 
N  14 119 VAL 119 119 119 VAL VAL N . n 
N  14 120 HIS 120 120 120 HIS HIS N . n 
N  14 121 LYS 121 121 121 LYS LYS N . n 
N  14 122 LEU 122 122 122 LEU LEU N . n 
N  14 123 PRO 123 123 123 PRO PRO N . n 
N  14 124 TYR 124 124 124 TYR TYR N . n 
N  14 125 ALA 125 125 125 ALA ALA N . n 
N  14 126 ILE 126 126 126 ILE ILE N . n 
N  14 127 ALA 127 127 127 ALA ALA N . n 
N  14 128 GLY 128 128 128 GLY GLY N . n 
N  14 129 SER 129 129 129 SER SER N . n 
N  14 130 GLY 130 130 130 GLY GLY N . n 
N  14 131 SER 131 131 131 SER SER N . n 
N  14 132 THR 132 132 132 THR THR N . n 
N  14 133 PHE 133 133 133 PHE PHE N . n 
N  14 134 ILE 134 134 134 ILE ILE N . n 
N  14 135 TYR 135 135 135 TYR TYR N . n 
N  14 136 GLY 136 136 136 GLY GLY N . n 
N  14 137 TYR 137 137 137 TYR TYR N . n 
N  14 138 CYS 138 138 138 CYS CYS N . n 
N  14 139 ASP 139 139 139 ASP ASP N . n 
N  14 140 LYS 140 140 140 LYS LYS N . n 
N  14 141 ASN 141 141 141 ASN ASN N . n 
N  14 142 PHE 142 142 142 PHE PHE N . n 
N  14 143 ARG 143 143 143 ARG ARG N . n 
N  14 144 GLU 144 144 144 GLU GLU N . n 
N  14 145 ASN 145 145 145 ASN ASN N . n 
N  14 146 MET 146 146 146 MET MET N . n 
N  14 147 SER 147 147 147 SER SER N . n 
N  14 148 LYS 148 148 148 LYS LYS N . n 
N  14 149 GLU 149 149 149 GLU GLU N . n 
N  14 150 GLU 150 150 150 GLU GLU N . n 
N  14 151 THR 151 151 151 THR THR N . n 
N  14 152 VAL 152 152 152 VAL VAL N . n 
N  14 153 ASP 153 153 153 ASP ASP N . n 
N  14 154 PHE 154 154 154 PHE PHE N . n 
N  14 155 ILE 155 155 155 ILE ILE N . n 
N  14 156 LYS 156 156 156 LYS LYS N . n 
N  14 157 HIS 157 157 157 HIS HIS N . n 
N  14 158 SER 158 158 158 SER SER N . n 
N  14 159 LEU 159 159 159 LEU LEU N . n 
N  14 160 SER 160 160 160 SER SER N . n 
N  14 161 GLN 161 161 161 GLN GLN N . n 
N  14 162 ALA 162 162 162 ALA ALA N . n 
N  14 163 ILE 163 163 163 ILE ILE N . n 
N  14 164 LYS 164 164 164 LYS LYS N . n 
N  14 165 TRP 165 165 165 TRP TRP N . n 
N  14 166 ASP 166 166 166 ASP ASP N . n 
N  14 167 GLY 167 167 167 GLY GLY N . n 
N  14 168 SER 168 168 168 SER SER N . n 
N  14 169 SER 169 169 169 SER SER N . n 
N  14 170 GLY 170 170 170 GLY GLY N . n 
N  14 171 GLY 171 171 171 GLY GLY N . n 
N  14 172 VAL 172 172 172 VAL VAL N . n 
N  14 173 ILE 173 173 173 ILE ILE N . n 
N  14 174 ARG 174 174 174 ARG ARG N . n 
N  14 175 MET 175 175 175 MET MET N . n 
N  14 176 VAL 176 176 176 VAL VAL N . n 
N  14 177 VAL 177 177 177 VAL VAL N . n 
N  14 178 LEU 178 178 178 LEU LEU N . n 
N  14 179 THR 179 179 179 THR THR N . n 
N  14 180 ALA 180 180 180 ALA ALA N . n 
N  14 181 ALA 181 181 181 ALA ALA N . n 
N  14 182 GLY 182 182 182 GLY GLY N . n 
N  14 183 VAL 183 183 183 VAL VAL N . n 
N  14 184 GLU 184 184 184 GLU GLU N . n 
N  14 185 ARG 185 185 185 ARG ARG N . n 
N  14 186 LEU 186 186 186 LEU LEU N . n 
N  14 187 ILE 187 187 187 ILE ILE N . n 
N  14 188 PHE 188 188 188 PHE PHE N . n 
N  14 189 TYR 189 189 189 TYR TYR N . n 
N  14 190 PRO 190 190 190 PRO PRO N . n 
N  14 191 ASP 191 191 191 ASP ASP N . n 
N  14 192 GLU 192 192 192 GLU GLU N . n 
N  14 193 TYR 193 193 193 TYR TYR N . n 
N  14 194 GLU 194 194 194 GLU GLU N . n 
N  14 195 GLN 195 195 195 GLN GLN N . n 
N  14 196 LEU 196 196 196 LEU LEU N . n 
O  1  1   MET 1   1   1   MET MET O . n 
O  1  2   THR 2   2   2   THR THR O . n 
O  1  3   ASP 3   3   3   ASP ASP O . n 
O  1  4   ARG 4   4   4   ARG ARG O . n 
O  1  5   TYR 5   5   5   TYR TYR O . n 
O  1  6   SER 6   6   6   SER SER O . n 
O  1  7   PHE 7   7   7   PHE PHE O . n 
O  1  8   SER 8   8   8   SER SER O . n 
O  1  9   LEU 9   9   9   LEU LEU O . n 
O  1  10  THR 10  10  10  THR THR O . n 
O  1  11  THR 11  11  11  THR THR O . n 
O  1  12  PHE 12  12  12  PHE PHE O . n 
O  1  13  SER 13  13  13  SER SER O . n 
O  1  14  PRO 14  14  14  PRO PRO O . n 
O  1  15  SER 15  15  15  SER SER O . n 
O  1  16  GLY 16  16  16  GLY GLY O . n 
O  1  17  LYS 17  17  17  LYS LYS O . n 
O  1  18  LEU 18  18  18  LEU LEU O . n 
O  1  19  GLY 19  19  19  GLY GLY O . n 
O  1  20  GLN 20  20  20  GLN GLN O . n 
O  1  21  ILE 21  21  21  ILE ILE O . n 
O  1  22  ASP 22  22  22  ASP ASP O . n 
O  1  23  TYR 23  23  23  TYR TYR O . n 
O  1  24  ALA 24  24  24  ALA ALA O . n 
O  1  25  LEU 25  25  25  LEU LEU O . n 
O  1  26  THR 26  26  26  THR THR O . n 
O  1  27  ALA 27  27  27  ALA ALA O . n 
O  1  28  VAL 28  28  28  VAL VAL O . n 
O  1  29  LYS 29  29  29  LYS LYS O . n 
O  1  30  GLN 30  30  30  GLN GLN O . n 
O  1  31  GLY 31  31  31  GLY GLY O . n 
O  1  32  VAL 32  32  32  VAL VAL O . n 
O  1  33  THR 33  33  33  THR THR O . n 
O  1  34  SER 34  34  34  SER SER O . n 
O  1  35  LEU 35  35  35  LEU LEU O . n 
O  1  36  GLY 36  36  36  GLY GLY O . n 
O  1  37  ILE 37  37  37  ILE ILE O . n 
O  1  38  LYS 38  38  38  LYS LYS O . n 
O  1  39  ALA 39  39  39  ALA ALA O . n 
O  1  40  THR 40  40  40  THR THR O . n 
O  1  41  ASN 41  41  41  ASN ASN O . n 
O  1  42  GLY 42  42  42  GLY GLY O . n 
O  1  43  VAL 43  43  43  VAL VAL O . n 
O  1  44  VAL 44  44  44  VAL VAL O . n 
O  1  45  ILE 45  45  45  ILE ILE O . n 
O  1  46  ALA 46  46  46  ALA ALA O . n 
O  1  47  THR 47  47  47  THR THR O . n 
O  1  48  GLU 48  48  48  GLU GLU O . n 
O  1  49  LYS 49  49  49  LYS LYS O . n 
O  1  50  LYS 50  50  50  LYS LYS O . n 
O  1  51  SER 51  51  51  SER SER O . n 
O  1  52  SER 52  52  52  SER SER O . n 
O  1  53  SER 53  53  53  SER SER O . n 
O  1  54  PRO 54  54  54  PRO PRO O . n 
O  1  55  LEU 55  55  55  LEU LEU O . n 
O  1  56  ALA 56  56  56  ALA ALA O . n 
O  1  57  MET 57  57  57  MET MET O . n 
O  1  58  SER 58  58  58  SER SER O . n 
O  1  59  GLU 59  59  59  GLU GLU O . n 
O  1  60  THR 60  60  60  THR THR O . n 
O  1  61  LEU 61  61  61  LEU LEU O . n 
O  1  62  SER 62  62  62  SER SER O . n 
O  1  63  LYS 63  63  63  LYS LYS O . n 
O  1  64  VAL 64  64  64  VAL VAL O . n 
O  1  65  SER 65  65  65  SER SER O . n 
O  1  66  LEU 66  66  66  LEU LEU O . n 
O  1  67  LEU 67  67  67  LEU LEU O . n 
O  1  68  THR 68  68  68  THR THR O . n 
O  1  69  PRO 69  69  69  PRO PRO O . n 
O  1  70  ASP 70  70  70  ASP ASP O . n 
O  1  71  ILE 71  71  71  ILE ILE O . n 
O  1  72  GLY 72  72  72  GLY GLY O . n 
O  1  73  ALA 73  73  73  ALA ALA O . n 
O  1  74  VAL 74  74  74  VAL VAL O . n 
O  1  75  TYR 75  75  75  TYR TYR O . n 
O  1  76  SER 76  76  76  SER SER O . n 
O  1  77  GLY 77  77  77  GLY GLY O . n 
O  1  78  MET 78  78  78  MET MET O . n 
O  1  79  GLY 79  79  79  GLY GLY O . n 
O  1  80  PRO 80  80  80  PRO PRO O . n 
O  1  81  ASP 81  81  81  ASP ASP O . n 
O  1  82  TYR 82  82  82  TYR TYR O . n 
O  1  83  ARG 83  83  83  ARG ARG O . n 
O  1  84  VAL 84  84  84  VAL VAL O . n 
O  1  85  LEU 85  85  85  LEU LEU O . n 
O  1  86  VAL 86  86  86  VAL VAL O . n 
O  1  87  ASP 87  87  87  ASP ASP O . n 
O  1  88  LYS 88  88  88  LYS LYS O . n 
O  1  89  SER 89  89  89  SER SER O . n 
O  1  90  ARG 90  90  90  ARG ARG O . n 
O  1  91  LYS 91  91  91  LYS LYS O . n 
O  1  92  VAL 92  92  92  VAL VAL O . n 
O  1  93  ALA 93  93  93  ALA ALA O . n 
O  1  94  HIS 94  94  94  HIS HIS O . n 
O  1  95  THR 95  95  95  THR THR O . n 
O  1  96  SER 96  96  96  SER SER O . n 
O  1  97  TYR 97  97  97  TYR TYR O . n 
O  1  98  LYS 98  98  98  LYS LYS O . n 
O  1  99  ARG 99  99  99  ARG ARG O . n 
O  1  100 ILE 100 100 100 ILE ILE O . n 
O  1  101 TYR 101 101 101 TYR TYR O . n 
O  1  102 GLY 102 102 102 GLY GLY O . n 
O  1  103 GLU 103 103 103 GLU GLU O . n 
O  1  104 TYR 104 104 104 TYR TYR O . n 
O  1  105 PRO 105 105 105 PRO PRO O . n 
O  1  106 PRO 106 106 106 PRO PRO O . n 
O  1  107 THR 107 107 107 THR THR O . n 
O  1  108 LYS 108 108 108 LYS LYS O . n 
O  1  109 LEU 109 109 109 LEU LEU O . n 
O  1  110 LEU 110 110 110 LEU LEU O . n 
O  1  111 VAL 111 111 111 VAL VAL O . n 
O  1  112 SER 112 112 112 SER SER O . n 
O  1  113 GLU 113 113 113 GLU GLU O . n 
O  1  114 VAL 114 114 114 VAL VAL O . n 
O  1  115 ALA 115 115 115 ALA ALA O . n 
O  1  116 LYS 116 116 116 LYS LYS O . n 
O  1  117 ILE 117 117 117 ILE ILE O . n 
O  1  118 MET 118 118 118 MET MET O . n 
O  1  119 GLN 119 119 119 GLN GLN O . n 
O  1  120 GLU 120 120 120 GLU GLU O . n 
O  1  121 ALA 121 121 121 ALA ALA O . n 
O  1  122 THR 122 122 122 THR THR O . n 
O  1  123 GLN 123 123 123 GLN GLN O . n 
O  1  124 SER 124 124 124 SER SER O . n 
O  1  125 GLY 125 125 125 GLY GLY O . n 
O  1  126 GLY 126 126 126 GLY GLY O . n 
O  1  127 VAL 127 127 127 VAL VAL O . n 
O  1  128 ARG 128 128 128 ARG ARG O . n 
O  1  129 PRO 129 129 129 PRO PRO O . n 
O  1  130 PHE 130 130 130 PHE PHE O . n 
O  1  131 GLY 131 131 131 GLY GLY O . n 
O  1  132 VAL 132 132 132 VAL VAL O . n 
O  1  133 SER 133 133 133 SER SER O . n 
O  1  134 LEU 134 134 134 LEU LEU O . n 
O  1  135 LEU 135 135 135 LEU LEU O . n 
O  1  136 ILE 136 136 136 ILE ILE O . n 
O  1  137 ALA 137 137 137 ALA ALA O . n 
O  1  138 GLY 138 138 138 GLY GLY O . n 
O  1  139 HIS 139 139 139 HIS HIS O . n 
O  1  140 ASP 140 140 140 ASP ASP O . n 
O  1  141 GLU 141 141 141 GLU GLU O . n 
O  1  142 PHE 142 142 142 PHE PHE O . n 
O  1  143 ASN 143 143 143 ASN ASN O . n 
O  1  144 GLY 144 144 144 GLY GLY O . n 
O  1  145 PHE 145 145 145 PHE PHE O . n 
O  1  146 SER 146 146 146 SER SER O . n 
O  1  147 LEU 147 147 147 LEU LEU O . n 
O  1  148 TYR 148 148 148 TYR TYR O . n 
O  1  149 GLN 149 149 149 GLN GLN O . n 
O  1  150 VAL 150 150 150 VAL VAL O . n 
O  1  151 ASP 151 151 151 ASP ASP O . n 
O  1  152 PRO 152 152 152 PRO PRO O . n 
O  1  153 SER 153 153 153 SER SER O . n 
O  1  154 GLY 154 154 154 GLY GLY O . n 
O  1  155 SER 155 155 155 SER SER O . n 
O  1  156 TYR 156 156 156 TYR TYR O . n 
O  1  157 PHE 157 157 157 PHE PHE O . n 
O  1  158 PRO 158 158 158 PRO PRO O . n 
O  1  159 TRP 159 159 159 TRP TRP O . n 
O  1  160 LYS 160 160 160 LYS LYS O . n 
O  1  161 ALA 161 161 161 ALA ALA O . n 
O  1  162 THR 162 162 162 THR THR O . n 
O  1  163 ALA 163 163 163 ALA ALA O . n 
O  1  164 ILE 164 164 164 ILE ILE O . n 
O  1  165 GLY 165 165 165 GLY GLY O . n 
O  1  166 LYS 166 166 166 LYS LYS O . n 
O  1  167 GLY 167 167 167 GLY GLY O . n 
O  1  168 SER 168 168 168 SER SER O . n 
O  1  169 VAL 169 169 169 VAL VAL O . n 
O  1  170 ALA 170 170 170 ALA ALA O . n 
O  1  171 ALA 171 171 171 ALA ALA O . n 
O  1  172 LYS 172 172 172 LYS LYS O . n 
O  1  173 THR 173 173 173 THR THR O . n 
O  1  174 PHE 174 174 174 PHE PHE O . n 
O  1  175 LEU 175 175 175 LEU LEU O . n 
O  1  176 GLU 176 176 176 GLU GLU O . n 
O  1  177 LYS 177 177 177 LYS LYS O . n 
O  1  178 ARG 178 178 178 ARG ARG O . n 
O  1  179 TRP 179 179 179 TRP TRP O . n 
O  1  180 ASN 180 180 180 ASN ASN O . n 
O  1  181 ASP 181 181 181 ASP ASP O . n 
O  1  182 GLU 182 182 182 GLU GLU O . n 
O  1  183 LEU 183 183 183 LEU LEU O . n 
O  1  184 GLU 184 184 184 GLU GLU O . n 
O  1  185 LEU 185 185 185 LEU LEU O . n 
O  1  186 GLU 186 186 186 GLU GLU O . n 
O  1  187 ASP 187 187 187 ASP ASP O . n 
O  1  188 ALA 188 188 188 ALA ALA O . n 
O  1  189 ILE 189 189 189 ILE ILE O . n 
O  1  190 HIS 190 190 190 HIS HIS O . n 
O  1  191 ILE 191 191 191 ILE ILE O . n 
O  1  192 ALA 192 192 192 ALA ALA O . n 
O  1  193 LEU 193 193 193 LEU LEU O . n 
O  1  194 LEU 194 194 194 LEU LEU O . n 
O  1  195 THR 195 195 195 THR THR O . n 
O  1  196 LEU 196 196 196 LEU LEU O . n 
O  1  197 LYS 197 197 197 LYS LYS O . n 
O  1  198 GLU 198 198 198 GLU GLU O . n 
O  1  199 SER 199 199 199 SER SER O . n 
O  1  200 VAL 200 200 200 VAL VAL O . n 
O  1  201 GLU 201 201 201 GLU GLU O . n 
O  1  202 GLY 202 202 202 GLY GLY O . n 
O  1  203 GLU 203 203 203 GLU GLU O . n 
O  1  204 PHE 204 204 204 PHE PHE O . n 
O  1  205 ASN 205 205 205 ASN ASN O . n 
O  1  206 GLY 206 206 206 GLY GLY O . n 
O  1  207 ASP 207 207 207 ASP ASP O . n 
O  1  208 THR 208 208 208 THR THR O . n 
O  1  209 ILE 209 209 209 ILE ILE O . n 
O  1  210 GLU 210 210 210 GLU GLU O . n 
O  1  211 LEU 211 211 211 LEU LEU O . n 
O  1  212 ALA 212 212 212 ALA ALA O . n 
O  1  213 ILE 213 213 213 ILE ILE O . n 
O  1  214 ILE 214 214 214 ILE ILE O . n 
O  1  215 GLY 215 215 215 GLY GLY O . n 
O  1  216 ASP 216 216 216 ASP ASP O . n 
O  1  217 GLU 217 217 217 GLU GLU O . n 
O  1  218 ASN 218 218 218 ASN ASN O . n 
O  1  219 PRO 219 219 219 PRO PRO O . n 
O  1  220 ASP 220 220 220 ASP ASP O . n 
O  1  221 LEU 221 221 221 LEU LEU O . n 
O  1  222 LEU 222 222 222 LEU LEU O . n 
O  1  223 GLY 223 223 223 GLY GLY O . n 
O  1  224 TYR 224 224 224 TYR TYR O . n 
O  1  225 THR 225 225 225 THR THR O . n 
O  1  226 GLY 226 226 226 GLY GLY O . n 
O  1  227 ILE 227 227 227 ILE ILE O . n 
O  1  228 PRO 228 228 228 PRO PRO O . n 
O  1  229 THR 229 229 229 THR THR O . n 
O  1  230 ASP 230 230 230 ASP ASP O . n 
O  1  231 LYS 231 231 231 LYS LYS O . n 
O  1  232 GLY 232 232 232 GLY GLY O . n 
O  1  233 PRO 233 233 233 PRO PRO O . n 
O  1  234 ARG 234 234 234 ARG ARG O . n 
O  1  235 PHE 235 235 235 PHE PHE O . n 
O  1  236 ARG 236 236 236 ARG ARG O . n 
O  1  237 LYS 237 237 237 LYS LYS O . n 
O  1  238 LEU 238 238 238 LEU LEU O . n 
O  1  239 THR 239 239 239 THR THR O . n 
O  1  240 SER 240 240 240 SER SER O . n 
O  1  241 GLN 241 241 241 GLN GLN O . n 
O  1  242 GLU 242 242 242 GLU GLU O . n 
O  1  243 ILE 243 243 243 ILE ILE O . n 
O  1  244 ASN 244 244 244 ASN ASN O . n 
O  1  245 ASP 245 245 245 ASP ASP O . n 
O  1  246 ARG 246 246 246 ARG ARG O . n 
O  1  247 LEU 247 247 247 LEU LEU O . n 
O  1  248 GLU 248 248 248 GLU GLU O . n 
O  1  249 ALA 249 249 249 ALA ALA O . n 
O  1  250 LEU 250 250 250 LEU LEU O . n 
P  2  1   MET 1   0   ?   ?   ?   P . n 
P  2  2   GLY 2   1   1   GLY GLY P . n 
P  2  3   SER 3   2   2   SER SER P . n 
P  2  4   ARG 4   3   3   ARG ARG P . n 
P  2  5   ARG 5   4   4   ARG ARG P . n 
P  2  6   TYR 6   5   5   TYR TYR P . n 
P  2  7   ASP 7   6   6   ASP ASP P . n 
P  2  8   SER 8   7   7   SER SER P . n 
P  2  9   ARG 9   8   8   ARG ARG P . n 
P  2  10  THR 10  9   9   THR THR P . n 
P  2  11  THR 11  10  10  THR THR P . n 
P  2  12  ILE 12  11  11  ILE ILE P . n 
P  2  13  PHE 13  12  12  PHE PHE P . n 
P  2  14  SER 14  13  13  SER SER P . n 
P  2  15  PRO 15  14  14  PRO PRO P . n 
P  2  16  GLU 16  15  15  GLU GLU P . n 
P  2  17  GLY 17  16  16  GLY GLY P . n 
P  2  18  ARG 18  17  17  ARG ARG P . n 
P  2  19  LEU 19  18  18  LEU LEU P . n 
P  2  20  TYR 20  19  19  TYR TYR P . n 
P  2  21  GLN 21  20  20  GLN GLN P . n 
P  2  22  VAL 22  21  21  VAL VAL P . n 
P  2  23  GLU 23  22  22  GLU GLU P . n 
P  2  24  TYR 24  23  23  TYR TYR P . n 
P  2  25  ALA 25  24  24  ALA ALA P . n 
P  2  26  LEU 26  25  25  LEU LEU P . n 
P  2  27  GLU 27  26  26  GLU GLU P . n 
P  2  28  SER 28  27  27  SER SER P . n 
P  2  29  ILE 29  28  28  ILE ILE P . n 
P  2  30  SER 30  29  29  SER SER P . n 
P  2  31  HIS 31  30  30  HIS HIS P . n 
P  2  32  ALA 32  31  31  ALA ALA P . n 
P  2  33  GLY 33  32  32  GLY GLY P . n 
P  2  34  THR 34  33  33  THR THR P . n 
P  2  35  ALA 35  34  34  ALA ALA P . n 
P  2  36  ILE 36  35  35  ILE ILE P . n 
P  2  37  GLY 37  36  36  GLY GLY P . n 
P  2  38  ILE 38  37  37  ILE ILE P . n 
P  2  39  MET 39  38  38  MET MET P . n 
P  2  40  ALA 40  39  39  ALA ALA P . n 
P  2  41  SER 41  40  40  SER SER P . n 
P  2  42  ASP 42  41  41  ASP ASP P . n 
P  2  43  GLY 43  42  42  GLY GLY P . n 
P  2  44  ILE 44  43  43  ILE ILE P . n 
P  2  45  VAL 45  44  44  VAL VAL P . n 
P  2  46  LEU 46  45  45  LEU LEU P . n 
P  2  47  ALA 47  46  46  ALA ALA P . n 
P  2  48  ALA 48  47  47  ALA ALA P . n 
P  2  49  GLU 49  48  48  GLU GLU P . n 
P  2  50  ARG 50  49  49  ARG ARG P . n 
P  2  51  LYS 51  50  50  LYS LYS P . n 
P  2  52  VAL 52  51  51  VAL VAL P . n 
P  2  53  THR 53  52  52  THR THR P . n 
P  2  54  SER 54  53  53  SER SER P . n 
P  2  55  THR 55  54  54  THR THR P . n 
P  2  56  LEU 56  55  55  LEU LEU P . n 
P  2  57  LEU 57  56  56  LEU LEU P . n 
P  2  58  GLU 58  57  57  GLU GLU P . n 
P  2  59  GLN 59  58  58  GLN GLN P . n 
P  2  60  ASP 60  59  59  ASP ASP P . n 
P  2  61  THR 61  60  60  THR THR P . n 
P  2  62  SER 62  61  61  SER SER P . n 
P  2  63  THR 63  62  62  THR THR P . n 
P  2  64  GLU 64  63  63  GLU GLU P . n 
P  2  65  LYS 65  64  64  LYS LYS P . n 
P  2  66  LEU 66  65  65  LEU LEU P . n 
P  2  67  TYR 67  66  66  TYR TYR P . n 
P  2  68  LYS 68  67  67  LYS LYS P . n 
P  2  69  LEU 69  68  68  LEU LEU P . n 
P  2  70  ASN 70  69  69  ASN ASN P . n 
P  2  71  ASP 71  70  70  ASP ASP P . n 
P  2  72  LYS 72  71  71  LYS LYS P . n 
P  2  73  ILE 73  72  72  ILE ILE P . n 
P  2  74  ALA 74  73  73  ALA ALA P . n 
P  2  75  VAL 75  74  74  VAL VAL P . n 
P  2  76  ALA 76  75  75  ALA ALA P . n 
P  2  77  VAL 77  76  76  VAL VAL P . n 
P  2  78  ALA 78  77  77  ALA ALA P . n 
P  2  79  GLY 79  78  78  GLY GLY P . n 
P  2  80  LEU 80  79  79  LEU LEU P . n 
P  2  81  THR 81  80  80  THR THR P . n 
P  2  82  ALA 82  81  81  ALA ALA P . n 
P  2  83  ASP 83  82  82  ASP ASP P . n 
P  2  84  ALA 84  83  83  ALA ALA P . n 
P  2  85  GLU 85  84  84  GLU GLU P . n 
P  2  86  ILE 86  85  85  ILE ILE P . n 
P  2  87  LEU 87  86  86  LEU LEU P . n 
P  2  88  ILE 88  87  87  ILE ILE P . n 
P  2  89  ASN 89  88  88  ASN ASN P . n 
P  2  90  THR 90  89  89  THR THR P . n 
P  2  91  ALA 91  90  90  ALA ALA P . n 
P  2  92  ARG 92  91  91  ARG ARG P . n 
P  2  93  ILE 93  92  92  ILE ILE P . n 
P  2  94  HIS 94  93  93  HIS HIS P . n 
P  2  95  ALA 95  94  94  ALA ALA P . n 
P  2  96  GLN 96  95  95  GLN GLN P . n 
P  2  97  ASN 97  96  96  ASN ASN P . n 
P  2  98  TYR 98  97  97  TYR TYR P . n 
P  2  99  LEU 99  98  98  LEU LEU P . n 
P  2  100 LYS 100 99  99  LYS LYS P . n 
P  2  101 THR 101 100 100 THR THR P . n 
P  2  102 TYR 102 101 101 TYR TYR P . n 
P  2  103 ASN 103 102 102 ASN ASN P . n 
P  2  104 GLU 104 103 103 GLU GLU P . n 
P  2  105 ASP 105 104 104 ASP ASP P . n 
P  2  106 ILE 106 105 105 ILE ILE P . n 
P  2  107 PRO 107 106 106 PRO PRO P . n 
P  2  108 VAL 108 107 107 VAL VAL P . n 
P  2  109 GLU 109 108 108 GLU GLU P . n 
P  2  110 ILE 110 109 109 ILE ILE P . n 
P  2  111 LEU 111 110 110 LEU LEU P . n 
P  2  112 VAL 112 111 111 VAL VAL P . n 
P  2  113 ARG 113 112 112 ARG ARG P . n 
P  2  114 ARG 114 113 113 ARG ARG P . n 
P  2  115 LEU 115 114 114 LEU LEU P . n 
P  2  116 SER 116 115 115 SER SER P . n 
P  2  117 ASP 117 116 116 ASP ASP P . n 
P  2  118 ILE 118 117 117 ILE ILE P . n 
P  2  119 LYS 119 118 118 LYS LYS P . n 
P  2  120 GLN 120 119 119 GLN GLN P . n 
P  2  121 GLY 121 120 120 GLY GLY P . n 
P  2  122 TYR 122 121 121 TYR TYR P . n 
P  2  123 THR 123 122 122 THR THR P . n 
P  2  124 GLN 124 123 123 GLN GLN P . n 
P  2  125 HIS 125 124 124 HIS HIS P . n 
P  2  126 GLY 126 125 125 GLY GLY P . n 
P  2  127 GLY 127 126 126 GLY GLY P . n 
P  2  128 LEU 128 127 127 LEU LEU P . n 
P  2  129 ARG 129 128 128 ARG ARG P . n 
P  2  130 PRO 130 129 129 PRO PRO P . n 
P  2  131 PHE 131 130 130 PHE PHE P . n 
P  2  132 GLY 132 131 131 GLY GLY P . n 
P  2  133 VAL 133 132 132 VAL VAL P . n 
P  2  134 SER 134 133 133 SER SER P . n 
P  2  135 PHE 135 134 134 PHE PHE P . n 
P  2  136 ILE 136 135 135 ILE ILE P . n 
P  2  137 TYR 137 136 136 TYR TYR P . n 
P  2  138 ALA 138 137 137 ALA ALA P . n 
P  2  139 GLY 139 138 138 GLY GLY P . n 
P  2  140 TYR 140 139 139 TYR TYR P . n 
P  2  141 ASP 141 140 140 ASP ASP P . n 
P  2  142 ASP 142 141 141 ASP ASP P . n 
P  2  143 ARG 143 142 142 ARG ARG P . n 
P  2  144 TYR 144 143 143 TYR TYR P . n 
P  2  145 GLY 145 144 144 GLY GLY P . n 
P  2  146 TYR 146 145 145 TYR TYR P . n 
P  2  147 GLN 147 146 146 GLN GLN P . n 
P  2  148 LEU 148 147 147 LEU LEU P . n 
P  2  149 TYR 149 148 148 TYR TYR P . n 
P  2  150 THR 150 149 149 THR THR P . n 
P  2  151 SER 151 150 150 SER SER P . n 
P  2  152 ASN 152 151 151 ASN ASN P . n 
P  2  153 PRO 153 152 152 PRO PRO P . n 
P  2  154 SER 154 153 153 SER SER P . n 
P  2  155 GLY 155 154 154 GLY GLY P . n 
P  2  156 ASN 156 155 155 ASN ASN P . n 
P  2  157 TYR 157 156 156 TYR TYR P . n 
P  2  158 THR 158 157 157 THR THR P . n 
P  2  159 GLY 159 158 158 GLY GLY P . n 
P  2  160 TRP 160 159 159 TRP TRP P . n 
P  2  161 LYS 161 160 160 LYS LYS P . n 
P  2  162 ALA 162 161 161 ALA ALA P . n 
P  2  163 ILE 163 162 162 ILE ILE P . n 
P  2  164 SER 164 163 163 SER SER P . n 
P  2  165 VAL 165 164 164 VAL VAL P . n 
P  2  166 GLY 166 165 165 GLY GLY P . n 
P  2  167 ALA 167 166 166 ALA ALA P . n 
P  2  168 ASN 168 167 167 ASN ASN P . n 
P  2  169 THR 169 168 168 THR THR P . n 
P  2  170 SER 170 169 169 SER SER P . n 
P  2  171 ALA 171 170 170 ALA ALA P . n 
P  2  172 ALA 172 171 171 ALA ALA P . n 
P  2  173 GLN 173 172 172 GLN GLN P . n 
P  2  174 THR 174 173 173 THR THR P . n 
P  2  175 LEU 175 174 174 LEU LEU P . n 
P  2  176 LEU 176 175 175 LEU LEU P . n 
P  2  177 GLN 177 176 176 GLN GLN P . n 
P  2  178 MET 178 177 177 MET MET P . n 
P  2  179 ASP 179 178 178 ASP ASP P . n 
P  2  180 TYR 180 179 179 TYR TYR P . n 
P  2  181 LYS 181 180 180 LYS LYS P . n 
P  2  182 ASP 182 181 181 ASP ASP P . n 
P  2  183 ASP 183 182 182 ASP ASP P . n 
P  2  184 MET 184 183 183 MET MET P . n 
P  2  185 LYS 185 184 184 LYS LYS P . n 
P  2  186 VAL 186 185 185 VAL VAL P . n 
P  2  187 ASP 187 186 186 ASP ASP P . n 
P  2  188 ASP 188 187 187 ASP ASP P . n 
P  2  189 ALA 189 188 188 ALA ALA P . n 
P  2  190 ILE 190 189 189 ILE ILE P . n 
P  2  191 GLU 191 190 190 GLU GLU P . n 
P  2  192 LEU 192 191 191 LEU LEU P . n 
P  2  193 ALA 193 192 192 ALA ALA P . n 
P  2  194 LEU 194 193 193 LEU LEU P . n 
P  2  195 LYS 195 194 194 LYS LYS P . n 
P  2  196 THR 196 195 195 THR THR P . n 
P  2  197 LEU 197 196 196 LEU LEU P . n 
P  2  198 SER 198 197 197 SER SER P . n 
P  2  199 LYS 199 198 198 LYS LYS P . n 
P  2  200 THR 200 199 199 THR THR P . n 
P  2  201 THR 201 200 200 THR THR P . n 
P  2  202 ASP 202 201 201 ASP ASP P . n 
P  2  203 SER 203 202 202 SER SER P . n 
P  2  204 SER 204 203 203 SER SER P . n 
P  2  205 ALA 205 204 204 ALA ALA P . n 
P  2  206 LEU 206 205 205 LEU LEU P . n 
P  2  207 THR 207 206 206 THR THR P . n 
P  2  208 TYR 208 207 207 TYR TYR P . n 
P  2  209 ASP 209 208 208 ASP ASP P . n 
P  2  210 ARG 210 209 209 ARG ARG P . n 
P  2  211 LEU 211 210 210 LEU LEU P . n 
P  2  212 GLU 212 211 211 GLU GLU P . n 
P  2  213 PHE 213 212 212 PHE PHE P . n 
P  2  214 ALA 214 213 213 ALA ALA P . n 
P  2  215 THR 215 214 214 THR THR P . n 
P  2  216 ILE 216 215 215 ILE ILE P . n 
P  2  217 ARG 217 216 216 ARG ARG P . n 
P  2  218 LYS 218 217 217 LYS LYS P . n 
P  2  219 GLY 219 218 218 GLY GLY P . n 
P  2  220 ALA 220 219 219 ALA ALA P . n 
P  2  221 ASN 221 220 220 ASN ASN P . n 
P  2  222 ASP 222 221 221 ASP ASP P . n 
P  2  223 GLY 223 222 222 GLY GLY P . n 
P  2  224 GLU 224 223 223 GLU GLU P . n 
P  2  225 VAL 225 224 224 VAL VAL P . n 
P  2  226 TYR 226 225 225 TYR TYR P . n 
P  2  227 GLN 227 226 226 GLN GLN P . n 
P  2  228 LYS 228 227 227 LYS LYS P . n 
P  2  229 ILE 229 228 228 ILE ILE P . n 
P  2  230 PHE 230 229 229 PHE PHE P . n 
P  2  231 LYS 231 230 230 LYS LYS P . n 
P  2  232 PRO 232 231 231 PRO PRO P . n 
P  2  233 GLN 233 232 232 GLN GLN P . n 
P  2  234 GLU 234 233 233 GLU GLU P . n 
P  2  235 ILE 235 234 234 ILE ILE P . n 
P  2  236 LYS 236 235 235 LYS LYS P . n 
P  2  237 ASP 237 236 236 ASP ASP P . n 
P  2  238 ILE 238 237 237 ILE ILE P . n 
P  2  239 LEU 239 238 238 LEU LEU P . n 
P  2  240 VAL 240 239 239 VAL VAL P . n 
P  2  241 LYS 241 240 240 LYS LYS P . n 
P  2  242 THR 242 241 241 THR THR P . n 
P  2  243 GLY 243 242 242 GLY GLY P . n 
P  2  244 ILE 244 243 243 ILE ILE P . n 
P  2  245 THR 245 244 244 THR THR P . n 
P  2  246 LYS 246 245 ?   ?   ?   P . n 
P  2  247 LYS 247 246 ?   ?   ?   P . n 
P  2  248 ASP 248 247 ?   ?   ?   P . n 
P  2  249 GLU 249 248 ?   ?   ?   P . n 
P  2  250 ASP 250 249 ?   ?   ?   P . n 
P  2  251 GLU 251 250 ?   ?   ?   P . n 
P  2  252 GLU 252 251 ?   ?   ?   P . n 
P  2  253 ALA 253 252 ?   ?   ?   P . n 
P  2  254 ASP 254 253 ?   ?   ?   P . n 
P  2  255 GLU 255 254 ?   ?   ?   P . n 
P  2  256 ASP 256 255 ?   ?   ?   P . n 
P  2  257 MET 257 256 ?   ?   ?   P . n 
P  2  258 LYS 258 257 ?   ?   ?   P . n 
Q  3  1   MET 1   -1  ?   ?   ?   Q . n 
Q  3  2   SER 2   0   ?   ?   ?   Q . n 
Q  3  3   GLY 3   1   1   GLY GLY Q . n 
Q  3  4   TYR 4   2   2   TYR TYR Q . n 
Q  3  5   ASP 5   3   3   ASP ASP Q . n 
Q  3  6   ARG 6   4   4   ARG ARG Q . n 
Q  3  7   ALA 7   5   5   ALA ALA Q . n 
Q  3  8   LEU 8   6   6   LEU LEU Q . n 
Q  3  9   SER 9   7   7   SER SER Q . n 
Q  3  10  ILE 10  8   8   ILE ILE Q . n 
Q  3  11  PHE 11  9   9   PHE PHE Q . n 
Q  3  12  SER 12  10  10  SER SER Q . n 
Q  3  13  PRO 13  11  11  PRO PRO Q . n 
Q  3  14  ASP 14  12  12  ASP ASP Q . n 
Q  3  15  GLY 15  13  13  GLY GLY Q . n 
Q  3  16  HIS 16  14  14  HIS HIS Q . n 
Q  3  17  ILE 17  15  15  ILE ILE Q . n 
Q  3  18  PHE 18  16  16  PHE PHE Q . n 
Q  3  19  GLN 19  17  17  GLN GLN Q . n 
Q  3  20  VAL 20  18  18  VAL VAL Q . n 
Q  3  21  GLU 21  19  19  GLU GLU Q . n 
Q  3  22  TYR 22  20  20  TYR TYR Q . n 
Q  3  23  ALA 23  21  21  ALA ALA Q . n 
Q  3  24  LEU 24  22  22  LEU LEU Q . n 
Q  3  25  GLU 25  23  23  GLU GLU Q . n 
Q  3  26  ALA 26  24  24  ALA ALA Q . n 
Q  3  27  VAL 27  25  25  VAL VAL Q . n 
Q  3  28  LYS 28  26  26  LYS LYS Q . n 
Q  3  29  ARG 29  27  27  ARG ARG Q . n 
Q  3  30  GLY 30  28  28  GLY GLY Q . n 
Q  3  31  THR 31  29  29  THR THR Q . n 
Q  3  32  CYS 32  30  30  CYS CYS Q . n 
Q  3  33  ALA 33  31  31  ALA ALA Q . n 
Q  3  34  VAL 34  32  32  VAL VAL Q . n 
Q  3  35  GLY 35  33  33  GLY GLY Q . n 
Q  3  36  VAL 36  34  34  VAL VAL Q . n 
Q  3  37  LYS 37  35  35  LYS LYS Q . n 
Q  3  38  GLY 38  36  36  GLY GLY Q . n 
Q  3  39  LYS 39  37  37  LYS LYS Q . n 
Q  3  40  ASN 40  38  38  ASN ASN Q . n 
Q  3  41  CYS 41  39  39  CYS CYS Q . n 
Q  3  42  VAL 42  40  40  VAL VAL Q . n 
Q  3  43  VAL 43  41  41  VAL VAL Q . n 
Q  3  44  LEU 44  42  42  LEU LEU Q . n 
Q  3  45  GLY 45  43  43  GLY GLY Q . n 
Q  3  46  CYS 46  44  44  CYS CYS Q . n 
Q  3  47  GLU 47  45  45  GLU GLU Q . n 
Q  3  48  ARG 48  46  46  ARG ARG Q . n 
Q  3  49  ARG 49  47  47  ARG ARG Q . n 
Q  3  50  SER 50  48  48  SER SER Q . n 
Q  3  51  THR 51  49  49  THR THR Q . n 
Q  3  52  LEU 52  50  50  LEU LEU Q . n 
Q  3  53  LYS 53  51  51  LYS LYS Q . n 
Q  3  54  LEU 54  52  52  LEU LEU Q . n 
Q  3  55  GLN 55  53  53  GLN GLN Q . n 
Q  3  56  ASP 56  54  54  ASP ASP Q . n 
Q  3  57  THR 57  55  55  THR THR Q . n 
Q  3  58  ARG 58  56  56  ARG ARG Q . n 
Q  3  59  ILE 59  57  57  ILE ILE Q . n 
Q  3  60  THR 60  58  58  THR THR Q . n 
Q  3  61  PRO 61  59  59  PRO PRO Q . n 
Q  3  62  SER 62  60  60  SER SER Q . n 
Q  3  63  LYS 63  61  61  LYS LYS Q . n 
Q  3  64  VAL 64  62  62  VAL VAL Q . n 
Q  3  65  SER 65  63  63  SER SER Q . n 
Q  3  66  LYS 66  64  64  LYS LYS Q . n 
Q  3  67  ILE 67  65  65  ILE ILE Q . n 
Q  3  68  ASP 68  66  66  ASP ASP Q . n 
Q  3  69  SER 69  67  67  SER SER Q . n 
Q  3  70  HIS 70  68  68  HIS HIS Q . n 
Q  3  71  VAL 71  69  69  VAL VAL Q . n 
Q  3  72  VAL 72  70  70  VAL VAL Q . n 
Q  3  73  LEU 73  71  71  LEU LEU Q . n 
Q  3  74  SER 74  72  72  SER SER Q . n 
Q  3  75  PHE 75  73  73  PHE PHE Q . n 
Q  3  76  SER 76  74  74  SER SER Q . n 
Q  3  77  GLY 77  75  75  GLY GLY Q . n 
Q  3  78  LEU 78  76  76  LEU LEU Q . n 
Q  3  79  ASN 79  77  77  ASN ASN Q . n 
Q  3  80  ALA 80  78  78  ALA ALA Q . n 
Q  3  81  ASP 81  79  79  ASP ASP Q . n 
Q  3  82  SER 82  80  80  SER SER Q . n 
Q  3  83  ARG 83  81  81  ARG ARG Q . n 
Q  3  84  ILE 84  82  82  ILE ILE Q . n 
Q  3  85  LEU 85  83  83  LEU LEU Q . n 
Q  3  86  ILE 86  84  84  ILE ILE Q . n 
Q  3  87  GLU 87  85  85  GLU GLU Q . n 
Q  3  88  LYS 88  86  86  LYS LYS Q . n 
Q  3  89  ALA 89  87  87  ALA ALA Q . n 
Q  3  90  ARG 90  88  88  ARG ARG Q . n 
Q  3  91  VAL 91  89  89  VAL VAL Q . n 
Q  3  92  GLU 92  90  90  GLU GLU Q . n 
Q  3  93  ALA 93  91  91  ALA ALA Q . n 
Q  3  94  GLN 94  92  92  GLN GLN Q . n 
Q  3  95  SER 95  93  93  SER SER Q . n 
Q  3  96  HIS 96  94  94  HIS HIS Q . n 
Q  3  97  ARG 97  95  95  ARG ARG Q . n 
Q  3  98  LEU 98  96  96  LEU LEU Q . n 
Q  3  99  THR 99  97  97  THR THR Q . n 
Q  3  100 LEU 100 98  98  LEU LEU Q . n 
Q  3  101 GLU 101 99  99  GLU GLU Q . n 
Q  3  102 ASP 102 100 100 ASP ASP Q . n 
Q  3  103 PRO 103 101 101 PRO PRO Q . n 
Q  3  104 VAL 104 102 102 VAL VAL Q . n 
Q  3  105 THR 105 103 103 THR THR Q . n 
Q  3  106 VAL 106 104 104 VAL VAL Q . n 
Q  3  107 GLU 107 105 105 GLU GLU Q . n 
Q  3  108 TYR 108 106 106 TYR TYR Q . n 
Q  3  109 LEU 109 107 107 LEU LEU Q . n 
Q  3  110 THR 110 108 108 THR THR Q . n 
Q  3  111 ARG 111 109 109 ARG ARG Q . n 
Q  3  112 TYR 112 110 110 TYR TYR Q . n 
Q  3  113 VAL 113 111 111 VAL VAL Q . n 
Q  3  114 ALA 114 112 112 ALA ALA Q . n 
Q  3  115 GLY 115 113 113 GLY GLY Q . n 
Q  3  116 VAL 116 114 114 VAL VAL Q . n 
Q  3  117 GLN 117 115 115 GLN GLN Q . n 
Q  3  118 GLN 118 116 116 GLN GLN Q . n 
Q  3  119 ARG 119 117 117 ARG ARG Q . n 
Q  3  120 TYR 120 118 118 TYR TYR Q . n 
Q  3  121 THR 121 119 119 THR THR Q . n 
Q  3  122 GLN 122 120 120 GLN GLN Q . n 
Q  3  123 SER 123 121 121 SER SER Q . n 
Q  3  124 GLY 124 122 122 GLY GLY Q . n 
Q  3  125 GLY 125 123 123 GLY GLY Q . n 
Q  3  126 VAL 126 124 124 VAL VAL Q . n 
Q  3  127 ARG 127 125 125 ARG ARG Q . n 
Q  3  128 PRO 128 126 126 PRO PRO Q . n 
Q  3  129 PHE 129 127 127 PHE PHE Q . n 
Q  3  130 GLY 130 128 128 GLY GLY Q . n 
Q  3  131 VAL 131 129 129 VAL VAL Q . n 
Q  3  132 SER 132 130 130 SER SER Q . n 
Q  3  133 THR 133 131 131 THR THR Q . n 
Q  3  134 LEU 134 132 132 LEU LEU Q . n 
Q  3  135 ILE 135 133 133 ILE ILE Q . n 
Q  3  136 ALA 136 134 134 ALA ALA Q . n 
Q  3  137 GLY 137 135 135 GLY GLY Q . n 
Q  3  138 PHE 138 136 136 PHE PHE Q . n 
Q  3  139 ASP 139 137 137 ASP ASP Q . n 
Q  3  140 PRO 140 138 138 PRO PRO Q . n 
Q  3  141 ARG 141 139 139 ARG ARG Q . n 
Q  3  142 ASP 142 140 140 ASP ASP Q . n 
Q  3  143 ASP 143 141 141 ASP ASP Q . n 
Q  3  144 GLU 144 142 142 GLU GLU Q . n 
Q  3  145 PRO 145 143 143 PRO PRO Q . n 
Q  3  146 LYS 146 144 144 LYS LYS Q . n 
Q  3  147 LEU 147 145 145 LEU LEU Q . n 
Q  3  148 TYR 148 146 146 TYR TYR Q . n 
Q  3  149 GLN 149 147 147 GLN GLN Q . n 
Q  3  150 THR 150 148 148 THR THR Q . n 
Q  3  151 GLU 151 149 149 GLU GLU Q . n 
Q  3  152 PRO 152 150 150 PRO PRO Q . n 
Q  3  153 SER 153 151 151 SER SER Q . n 
Q  3  154 GLY 154 152 152 GLY GLY Q . n 
Q  3  155 ILE 155 153 153 ILE ILE Q . n 
Q  3  156 TYR 156 154 154 TYR TYR Q . n 
Q  3  157 SER 157 155 155 SER SER Q . n 
Q  3  158 SER 158 156 156 SER SER Q . n 
Q  3  159 TRP 159 157 157 TRP TRP Q . n 
Q  3  160 SER 160 158 158 SER SER Q . n 
Q  3  161 ALA 161 159 159 ALA ALA Q . n 
Q  3  162 GLN 162 160 160 GLN GLN Q . n 
Q  3  163 THR 163 161 161 THR THR Q . n 
Q  3  164 ILE 164 162 162 ILE ILE Q . n 
Q  3  165 GLY 165 163 163 GLY GLY Q . n 
Q  3  166 ARG 166 164 164 ARG ARG Q . n 
Q  3  167 ASN 167 165 165 ASN ASN Q . n 
Q  3  168 SER 168 166 166 SER SER Q . n 
Q  3  169 LYS 169 167 167 LYS LYS Q . n 
Q  3  170 THR 170 168 168 THR THR Q . n 
Q  3  171 VAL 171 169 169 VAL VAL Q . n 
Q  3  172 ARG 172 170 170 ARG ARG Q . n 
Q  3  173 GLU 173 171 171 GLU GLU Q . n 
Q  3  174 PHE 174 172 172 PHE PHE Q . n 
Q  3  175 LEU 175 173 173 LEU LEU Q . n 
Q  3  176 GLU 176 174 174 GLU GLU Q . n 
Q  3  177 LYS 177 175 175 LYS LYS Q . n 
Q  3  178 ASN 178 176 176 ASN ASN Q . n 
Q  3  179 TYR 179 177 177 TYR TYR Q . n 
Q  3  180 ASP 180 178 178 ASP ASP Q . n 
Q  3  181 ARG 181 179 179 ARG ARG Q . n 
Q  3  182 LYS 182 180 180 LYS LYS Q . n 
Q  3  183 GLU 183 181 181 GLU GLU Q . n 
Q  3  184 PRO 184 182 182 PRO PRO Q . n 
Q  3  185 PRO 185 183 183 PRO PRO Q . n 
Q  3  186 ALA 186 184 184 ALA ALA Q . n 
Q  3  187 THR 187 185 185 THR THR Q . n 
Q  3  188 VAL 188 186 186 VAL VAL Q . n 
Q  3  189 GLU 189 187 187 GLU GLU Q . n 
Q  3  190 GLU 190 188 188 GLU GLU Q . n 
Q  3  191 CYS 191 189 189 CYS CYS Q . n 
Q  3  192 VAL 192 190 190 VAL VAL Q . n 
Q  3  193 LYS 193 191 191 LYS LYS Q . n 
Q  3  194 LEU 194 192 192 LEU LEU Q . n 
Q  3  195 THR 195 193 193 THR THR Q . n 
Q  3  196 VAL 196 194 194 VAL VAL Q . n 
Q  3  197 ARG 197 195 195 ARG ARG Q . n 
Q  3  198 SER 198 196 196 SER SER Q . n 
Q  3  199 LEU 199 197 197 LEU LEU Q . n 
Q  3  200 LEU 200 198 198 LEU LEU Q . n 
Q  3  201 GLU 201 199 199 GLU GLU Q . n 
Q  3  202 VAL 202 200 200 VAL VAL Q . n 
Q  3  203 VAL 203 201 201 VAL VAL Q . n 
Q  3  204 GLN 204 202 202 GLN GLN Q . n 
Q  3  205 THR 205 203 203 THR THR Q . n 
Q  3  206 GLY 206 204 204 GLY GLY Q . n 
Q  3  207 ALA 207 205 205 ALA ALA Q . n 
Q  3  208 LYS 208 206 206 LYS LYS Q . n 
Q  3  209 ASN 209 207 207 ASN ASN Q . n 
Q  3  210 ILE 210 208 208 ILE ILE Q . n 
Q  3  211 GLU 211 209 209 GLU GLU Q . n 
Q  3  212 ILE 212 210 210 ILE ILE Q . n 
Q  3  213 THR 213 211 211 THR THR Q . n 
Q  3  214 VAL 214 212 212 VAL VAL Q . n 
Q  3  215 VAL 215 213 213 VAL VAL Q . n 
Q  3  216 LYS 216 214 214 LYS LYS Q . n 
Q  3  217 PRO 217 215 215 PRO PRO Q . n 
Q  3  218 ASP 218 216 216 ASP ASP Q . n 
Q  3  219 SER 219 217 217 SER SER Q . n 
Q  3  220 ASP 220 218 218 ASP ASP Q . n 
Q  3  221 ILE 221 219 219 ILE ILE Q . n 
Q  3  222 VAL 222 220 220 VAL VAL Q . n 
Q  3  223 ALA 223 221 221 ALA ALA Q . n 
Q  3  224 LEU 224 222 222 LEU LEU Q . n 
Q  3  225 SER 225 223 223 SER SER Q . n 
Q  3  226 SER 226 224 224 SER SER Q . n 
Q  3  227 GLU 227 225 225 GLU GLU Q . n 
Q  3  228 GLU 228 226 226 GLU GLU Q . n 
Q  3  229 ILE 229 227 227 ILE ILE Q . n 
Q  3  230 ASN 230 228 228 ASN ASN Q . n 
Q  3  231 GLN 231 229 229 GLN GLN Q . n 
Q  3  232 TYR 232 230 230 TYR TYR Q . n 
Q  3  233 VAL 233 231 231 VAL VAL Q . n 
Q  3  234 THR 234 232 232 THR THR Q . n 
Q  3  235 GLN 235 233 233 GLN GLN Q . n 
Q  3  236 ILE 236 234 234 ILE ILE Q . n 
Q  3  237 GLU 237 235 235 GLU GLU Q . n 
Q  3  238 GLN 238 236 236 GLN GLN Q . n 
Q  3  239 GLU 239 237 237 GLU GLU Q . n 
Q  3  240 LYS 240 238 238 LYS LYS Q . n 
Q  3  241 GLN 241 239 239 GLN GLN Q . n 
Q  3  242 GLU 242 240 240 GLU GLU Q . n 
Q  3  243 GLN 243 241 ?   ?   ?   Q . n 
Q  3  244 GLN 244 242 ?   ?   ?   Q . n 
Q  3  245 GLU 245 243 ?   ?   ?   Q . n 
Q  3  246 GLN 246 244 ?   ?   ?   Q . n 
Q  3  247 ASP 247 245 ?   ?   ?   Q . n 
Q  3  248 LYS 248 246 ?   ?   ?   Q . n 
Q  3  249 LYS 249 247 ?   ?   ?   Q . n 
Q  3  250 LYS 250 248 ?   ?   ?   Q . n 
Q  3  251 LYS 251 249 ?   ?   ?   Q . n 
Q  3  252 SER 252 250 ?   ?   ?   Q . n 
Q  3  253 ASN 253 251 ?   ?   ?   Q . n 
Q  3  254 HIS 254 252 ?   ?   ?   Q . n 
R  4  1   MET 1   -7  ?   ?   ?   R . n 
R  4  2   PHE 2   -6  ?   ?   ?   R . n 
R  4  3   LEU 3   -5  ?   ?   ?   R . n 
R  4  4   THR 4   -4  ?   ?   ?   R . n 
R  4  5   ARG 5   -3  ?   ?   ?   R . n 
R  4  6   SER 6   -2  ?   ?   ?   R . n 
R  4  7   GLU 7   -1  ?   ?   ?   R . n 
R  4  8   TYR 8   0   ?   ?   ?   R . n 
R  4  9   ASP 9   1   1   ASP ASP R . n 
R  4  10  ARG 10  2   2   ARG ARG R . n 
R  4  11  GLY 11  3   3   GLY GLY R . n 
R  4  12  VAL 12  4   4   VAL VAL R . n 
R  4  13  SER 13  5   5   SER SER R . n 
R  4  14  THR 14  6   6   THR THR R . n 
R  4  15  PHE 15  7   7   PHE PHE R . n 
R  4  16  SER 16  8   8   SER SER R . n 
R  4  17  PRO 17  9   9   PRO PRO R . n 
R  4  18  GLU 18  10  10  GLU GLU R . n 
R  4  19  GLY 19  11  11  GLY GLY R . n 
R  4  20  ARG 20  12  12  ARG ARG R . n 
R  4  21  LEU 21  13  13  LEU LEU R . n 
R  4  22  PHE 22  14  14  PHE PHE R . n 
R  4  23  GLN 23  15  15  GLN GLN R . n 
R  4  24  VAL 24  16  16  VAL VAL R . n 
R  4  25  GLU 25  17  17  GLU GLU R . n 
R  4  26  TYR 26  18  18  TYR TYR R . n 
R  4  27  SER 27  19  19  SER SER R . n 
R  4  28  LEU 28  20  20  LEU LEU R . n 
R  4  29  GLU 29  21  21  GLU GLU R . n 
R  4  30  ALA 30  22  22  ALA ALA R . n 
R  4  31  ILE 31  23  23  ILE ILE R . n 
R  4  32  LYS 32  24  24  LYS LYS R . n 
R  4  33  LEU 33  25  25  LEU LEU R . n 
R  4  34  GLY 34  26  26  GLY GLY R . n 
R  4  35  SER 35  27  27  SER SER R . n 
R  4  36  THR 36  28  28  THR THR R . n 
R  4  37  ALA 37  29  29  ALA ALA R . n 
R  4  38  ILE 38  30  30  ILE ILE R . n 
R  4  39  GLY 39  31  31  GLY GLY R . n 
R  4  40  ILE 40  32  32  ILE ILE R . n 
R  4  41  ALA 41  33  33  ALA ALA R . n 
R  4  42  THR 42  34  34  THR THR R . n 
R  4  43  LYS 43  35  35  LYS LYS R . n 
R  4  44  GLU 44  36  36  GLU GLU R . n 
R  4  45  GLY 45  37  37  GLY GLY R . n 
R  4  46  VAL 46  38  38  VAL VAL R . n 
R  4  47  VAL 47  39  39  VAL VAL R . n 
R  4  48  LEU 48  40  40  LEU LEU R . n 
R  4  49  GLY 49  41  41  GLY GLY R . n 
R  4  50  VAL 50  42  42  VAL VAL R . n 
R  4  51  GLU 51  43  43  GLU GLU R . n 
R  4  52  LYS 52  44  44  LYS LYS R . n 
R  4  53  ARG 53  45  45  ARG ARG R . n 
R  4  54  ALA 54  46  46  ALA ALA R . n 
R  4  55  THR 55  47  47  THR THR R . n 
R  4  56  SER 56  48  48  SER SER R . n 
R  4  57  PRO 57  49  49  PRO PRO R . n 
R  4  58  LEU 58  50  50  LEU LEU R . n 
R  4  59  LEU 59  51  51  LEU LEU R . n 
R  4  60  GLU 60  52  52  GLU GLU R . n 
R  4  61  SER 61  53  53  SER SER R . n 
R  4  62  ASP 62  54  54  ASP ASP R . n 
R  4  63  SER 63  55  55  SER SER R . n 
R  4  64  ILE 64  56  56  ILE ILE R . n 
R  4  65  GLU 65  57  57  GLU GLU R . n 
R  4  66  LYS 66  58  58  LYS LYS R . n 
R  4  67  ILE 67  59  59  ILE ILE R . n 
R  4  68  VAL 68  60  60  VAL VAL R . n 
R  4  69  GLU 69  61  61  GLU GLU R . n 
R  4  70  ILE 70  62  62  ILE ILE R . n 
R  4  71  ASP 71  63  63  ASP ASP R . n 
R  4  72  ARG 72  64  64  ARG ARG R . n 
R  4  73  HIS 73  65  65  HIS HIS R . n 
R  4  74  ILE 74  66  66  ILE ILE R . n 
R  4  75  GLY 75  67  67  GLY GLY R . n 
R  4  76  CYS 76  68  68  CYS CYS R . n 
R  4  77  ALA 77  69  69  ALA ALA R . n 
R  4  78  MET 78  70  70  MET MET R . n 
R  4  79  SER 79  71  71  SER SER R . n 
R  4  80  GLY 80  72  72  GLY GLY R . n 
R  4  81  LEU 81  73  73  LEU LEU R . n 
R  4  82  THR 82  74  74  THR THR R . n 
R  4  83  ALA 83  75  75  ALA ALA R . n 
R  4  84  ASP 84  76  76  ASP ASP R . n 
R  4  85  ALA 85  77  77  ALA ALA R . n 
R  4  86  ARG 86  78  78  ARG ARG R . n 
R  4  87  SER 87  79  79  SER SER R . n 
R  4  88  MET 88  80  80  MET MET R . n 
R  4  89  ILE 89  81  81  ILE ILE R . n 
R  4  90  GLU 90  82  82  GLU GLU R . n 
R  4  91  HIS 91  83  83  HIS HIS R . n 
R  4  92  ALA 92  84  84  ALA ALA R . n 
R  4  93  ARG 93  85  85  ARG ARG R . n 
R  4  94  THR 94  86  86  THR THR R . n 
R  4  95  ALA 95  87  87  ALA ALA R . n 
R  4  96  ALA 96  88  88  ALA ALA R . n 
R  4  97  VAL 97  89  89  VAL VAL R . n 
R  4  98  THR 98  90  90  THR THR R . n 
R  4  99  HIS 99  91  91  HIS HIS R . n 
R  4  100 ASN 100 92  92  ASN ASN R . n 
R  4  101 LEU 101 93  93  LEU LEU R . n 
R  4  102 TYR 102 94  94  TYR TYR R . n 
R  4  103 TYR 103 95  95  TYR TYR R . n 
R  4  104 ASP 104 96  96  ASP ASP R . n 
R  4  105 GLU 105 97  97  GLU GLU R . n 
R  4  106 ASP 106 98  98  ASP ASP R . n 
R  4  107 ILE 107 99  99  ILE ILE R . n 
R  4  108 ASN 108 100 100 ASN ASN R . n 
R  4  109 VAL 109 101 101 VAL VAL R . n 
R  4  110 GLU 110 102 102 GLU GLU R . n 
R  4  111 SER 111 103 103 SER SER R . n 
R  4  112 LEU 112 104 104 LEU LEU R . n 
R  4  113 THR 113 105 105 THR THR R . n 
R  4  114 GLN 114 106 106 GLN GLN R . n 
R  4  115 SER 115 107 107 SER SER R . n 
R  4  116 VAL 116 108 108 VAL VAL R . n 
R  4  117 CYS 117 109 109 CYS CYS R . n 
R  4  118 ASP 118 110 110 ASP ASP R . n 
R  4  119 LEU 119 111 111 LEU LEU R . n 
R  4  120 ALA 120 112 112 ALA ALA R . n 
R  4  121 LEU 121 113 113 LEU LEU R . n 
R  4  122 ARG 122 114 114 ARG ARG R . n 
R  4  123 PHE 123 115 115 PHE PHE R . n 
R  4  124 GLY 124 116 116 GLY GLY R . n 
R  4  125 GLU 125 117 117 GLU GLU R . n 
R  4  126 GLY 126 118 ?   ?   ?   R . n 
R  4  127 ALA 127 119 ?   ?   ?   R . n 
R  4  128 SER 128 120 ?   ?   ?   R . n 
R  4  129 GLY 129 121 ?   ?   ?   R . n 
R  4  130 GLU 130 122 ?   ?   ?   R . n 
R  4  131 GLU 131 123 ?   ?   ?   R . n 
R  4  132 ARG 132 124 ?   ?   ?   R . n 
R  4  133 LEU 133 125 125 LEU LEU R . n 
R  4  134 MET 134 126 126 MET MET R . n 
R  4  135 SER 135 127 127 SER SER R . n 
R  4  136 ARG 136 128 128 ARG ARG R . n 
R  4  137 PRO 137 129 129 PRO PRO R . n 
R  4  138 PHE 138 130 130 PHE PHE R . n 
R  4  139 GLY 139 131 131 GLY GLY R . n 
R  4  140 VAL 140 132 132 VAL VAL R . n 
R  4  141 ALA 141 133 133 ALA ALA R . n 
R  4  142 LEU 142 134 134 LEU LEU R . n 
R  4  143 LEU 143 135 135 LEU LEU R . n 
R  4  144 ILE 144 136 136 ILE ILE R . n 
R  4  145 ALA 145 137 137 ALA ALA R . n 
R  4  146 GLY 146 138 138 GLY GLY R . n 
R  4  147 HIS 147 139 139 HIS HIS R . n 
R  4  148 ASP 148 140 140 ASP ASP R . n 
R  4  149 ALA 149 141 141 ALA ALA R . n 
R  4  150 ASP 150 142 142 ASP ASP R . n 
R  4  151 ASP 151 143 143 ASP ASP R . n 
R  4  152 GLY 152 144 144 GLY GLY R . n 
R  4  153 TYR 153 145 145 TYR TYR R . n 
R  4  154 GLN 154 146 146 GLN GLN R . n 
R  4  155 LEU 155 147 147 LEU LEU R . n 
R  4  156 PHE 156 148 148 PHE PHE R . n 
R  4  157 HIS 157 149 149 HIS HIS R . n 
R  4  158 ALA 158 150 150 ALA ALA R . n 
R  4  159 GLU 159 151 151 GLU GLU R . n 
R  4  160 PRO 160 152 152 PRO PRO R . n 
R  4  161 SER 161 153 153 SER SER R . n 
R  4  162 GLY 162 154 154 GLY GLY R . n 
R  4  163 THR 163 155 155 THR THR R . n 
R  4  164 PHE 164 156 156 PHE PHE R . n 
R  4  165 TYR 165 157 157 TYR TYR R . n 
R  4  166 ARG 166 158 158 ARG ARG R . n 
R  4  167 TYR 167 159 159 TYR TYR R . n 
R  4  168 ASN 168 160 160 ASN ASN R . n 
R  4  169 ALA 169 161 161 ALA ALA R . n 
R  4  170 LYS 170 162 162 LYS LYS R . n 
R  4  171 ALA 171 163 163 ALA ALA R . n 
R  4  172 ILE 172 164 164 ILE ILE R . n 
R  4  173 GLY 173 165 165 GLY GLY R . n 
R  4  174 SER 174 166 166 SER SER R . n 
R  4  175 GLY 175 167 167 GLY GLY R . n 
R  4  176 SER 176 168 168 SER SER R . n 
R  4  177 GLU 177 169 169 GLU GLU R . n 
R  4  178 GLY 178 170 170 GLY GLY R . n 
R  4  179 ALA 179 171 171 ALA ALA R . n 
R  4  180 GLN 180 172 172 GLN GLN R . n 
R  4  181 ALA 181 173 173 ALA ALA R . n 
R  4  182 GLU 182 174 174 GLU GLU R . n 
R  4  183 LEU 183 175 175 LEU LEU R . n 
R  4  184 LEU 184 176 176 LEU LEU R . n 
R  4  185 ASN 185 177 177 ASN ASN R . n 
R  4  186 GLU 186 178 178 GLU GLU R . n 
R  4  187 TRP 187 179 179 TRP TRP R . n 
R  4  188 HIS 188 180 180 HIS HIS R . n 
R  4  189 SER 189 181 181 SER SER R . n 
R  4  190 SER 190 182 182 SER SER R . n 
R  4  191 LEU 191 183 183 LEU LEU R . n 
R  4  192 THR 192 184 184 THR THR R . n 
R  4  193 LEU 193 185 185 LEU LEU R . n 
R  4  194 LYS 194 186 186 LYS LYS R . n 
R  4  195 GLU 195 187 187 GLU GLU R . n 
R  4  196 ALA 196 188 188 ALA ALA R . n 
R  4  197 GLU 197 189 189 GLU GLU R . n 
R  4  198 LEU 198 190 190 LEU LEU R . n 
R  4  199 LEU 199 191 191 LEU LEU R . n 
R  4  200 VAL 200 192 192 VAL VAL R . n 
R  4  201 LEU 201 193 193 LEU LEU R . n 
R  4  202 LYS 202 194 194 LYS LYS R . n 
R  4  203 ILE 203 195 195 ILE ILE R . n 
R  4  204 LEU 204 196 196 LEU LEU R . n 
R  4  205 LYS 205 197 197 LYS LYS R . n 
R  4  206 GLN 206 198 198 GLN GLN R . n 
R  4  207 VAL 207 199 199 VAL VAL R . n 
R  4  208 MET 208 200 200 MET MET R . n 
R  4  209 GLU 209 201 201 GLU GLU R . n 
R  4  210 GLU 210 202 202 GLU GLU R . n 
R  4  211 LYS 211 203 203 LYS LYS R . n 
R  4  212 LEU 212 204 204 LEU LEU R . n 
R  4  213 ASP 213 205 205 ASP ASP R . n 
R  4  214 GLU 214 206 206 GLU GLU R . n 
R  4  215 ASN 215 207 207 ASN ASN R . n 
R  4  216 ASN 216 208 208 ASN ASN R . n 
R  4  217 ALA 217 209 209 ALA ALA R . n 
R  4  218 GLN 218 210 210 GLN GLN R . n 
R  4  219 LEU 219 211 211 LEU LEU R . n 
R  4  220 SER 220 212 212 SER SER R . n 
R  4  221 CYS 221 213 213 CYS CYS R . n 
R  4  222 ILE 222 214 214 ILE ILE R . n 
R  4  223 THR 223 215 215 THR THR R . n 
R  4  224 LYS 224 216 216 LYS LYS R . n 
R  4  225 GLN 225 217 217 GLN GLN R . n 
R  4  226 ASP 226 218 218 ASP ASP R . n 
R  4  227 GLY 227 219 219 GLY GLY R . n 
R  4  228 PHE 228 220 220 PHE PHE R . n 
R  4  229 LYS 229 221 221 LYS LYS R . n 
R  4  230 ILE 230 222 222 ILE ILE R . n 
R  4  231 TYR 231 223 223 TYR TYR R . n 
R  4  232 ASP 232 224 224 ASP ASP R . n 
R  4  233 ASN 233 225 225 ASN ASN R . n 
R  4  234 GLU 234 226 226 GLU GLU R . n 
R  4  235 LYS 235 227 227 LYS LYS R . n 
R  4  236 THR 236 228 228 THR THR R . n 
R  4  237 ALA 237 229 229 ALA ALA R . n 
R  4  238 GLU 238 230 230 GLU GLU R . n 
R  4  239 LEU 239 231 231 LEU LEU R . n 
R  4  240 ILE 240 232 232 ILE ILE R . n 
R  4  241 LYS 241 233 233 LYS LYS R . n 
R  4  242 GLU 242 234 234 GLU GLU R . n 
R  4  243 LEU 243 235 235 LEU LEU R . n 
R  4  244 LYS 244 236 236 LYS LYS R . n 
R  4  245 GLU 245 237 237 GLU GLU R . n 
R  4  246 LYS 246 238 238 LYS LYS R . n 
R  4  247 GLU 247 239 239 GLU GLU R . n 
R  4  248 ALA 248 240 240 ALA ALA R . n 
R  4  249 ALA 249 241 241 ALA ALA R . n 
R  4  250 GLU 250 242 242 GLU GLU R . n 
R  4  251 SER 251 243 ?   ?   ?   R . n 
R  4  252 PRO 252 244 ?   ?   ?   R . n 
R  4  253 GLU 253 245 ?   ?   ?   R . n 
R  4  254 GLU 254 246 ?   ?   ?   R . n 
R  4  255 ALA 255 247 ?   ?   ?   R . n 
R  4  256 ASP 256 248 ?   ?   ?   R . n 
R  4  257 VAL 257 249 ?   ?   ?   R . n 
R  4  258 GLU 258 250 ?   ?   ?   R . n 
R  4  259 MET 259 251 ?   ?   ?   R . n 
R  4  260 SER 260 252 ?   ?   ?   R . n 
S  5  1   MET 1   0   ?   ?   ?   S . n 
S  5  2   PHE 2   1   ?   ?   ?   S . n 
S  5  3   ARG 3   2   ?   ?   ?   S . n 
S  5  4   ASN 4   3   3   ASN ASN S . n 
S  5  5   ASN 5   4   4   ASN ASN S . n 
S  5  6   TYR 6   5   5   TYR TYR S . n 
S  5  7   ASP 7   6   6   ASP ASP S . n 
S  5  8   GLY 8   7   7   GLY GLY S . n 
S  5  9   ASP 9   8   8   ASP ASP S . n 
S  5  10  THR 10  9   9   THR THR S . n 
S  5  11  VAL 11  10  10  VAL VAL S . n 
S  5  12  THR 12  11  11  THR THR S . n 
S  5  13  PHE 13  12  12  PHE PHE S . n 
S  5  14  SER 14  13  13  SER SER S . n 
S  5  15  PRO 15  14  14  PRO PRO S . n 
S  5  16  THR 16  15  15  THR THR S . n 
S  5  17  GLY 17  16  16  GLY GLY S . n 
S  5  18  ARG 18  17  17  ARG ARG S . n 
S  5  19  LEU 19  18  18  LEU LEU S . n 
S  5  20  PHE 20  19  19  PHE PHE S . n 
S  5  21  GLN 21  20  20  GLN GLN S . n 
S  5  22  VAL 22  21  21  VAL VAL S . n 
S  5  23  GLU 23  22  22  GLU GLU S . n 
S  5  24  TYR 24  23  23  TYR TYR S . n 
S  5  25  ALA 25  24  24  ALA ALA S . n 
S  5  26  LEU 26  25  25  LEU LEU S . n 
S  5  27  GLU 27  26  26  GLU GLU S . n 
S  5  28  ALA 28  27  27  ALA ALA S . n 
S  5  29  ILE 29  28  28  ILE ILE S . n 
S  5  30  LYS 30  29  29  LYS LYS S . n 
S  5  31  GLN 31  30  30  GLN GLN S . n 
S  5  32  GLY 32  31  31  GLY GLY S . n 
S  5  33  SER 33  32  32  SER SER S . n 
S  5  34  VAL 34  33  33  VAL VAL S . n 
S  5  35  THR 35  34  34  THR THR S . n 
S  5  36  VAL 36  35  35  VAL VAL S . n 
S  5  37  GLY 37  36  36  GLY GLY S . n 
S  5  38  LEU 38  37  37  LEU LEU S . n 
S  5  39  ARG 39  38  38  ARG ARG S . n 
S  5  40  SER 40  39  39  SER SER S . n 
S  5  41  ASN 41  40  40  ASN ASN S . n 
S  5  42  THR 42  41  41  THR THR S . n 
S  5  43  HIS 43  42  42  HIS HIS S . n 
S  5  44  ALA 44  43  43  ALA ALA S . n 
S  5  45  VAL 45  44  44  VAL VAL S . n 
S  5  46  LEU 46  45  45  LEU LEU S . n 
S  5  47  VAL 47  46  46  VAL VAL S . n 
S  5  48  ALA 48  47  47  ALA ALA S . n 
S  5  49  LEU 49  48  48  LEU LEU S . n 
S  5  50  LYS 50  49  49  LYS LYS S . n 
S  5  51  ARG 51  50  50  ARG ARG S . n 
S  5  52  ASN 52  51  51  ASN ASN S . n 
S  5  53  ALA 53  52  52  ALA ALA S . n 
S  5  54  ASP 54  53  53  ASP ASP S . n 
S  5  55  GLU 55  54  54  GLU GLU S . n 
S  5  56  LEU 56  55  55  LEU LEU S . n 
S  5  57  SER 57  56  56  SER SER S . n 
S  5  58  SER 58  57  57  SER SER S . n 
S  5  59  TYR 59  58  58  TYR TYR S . n 
S  5  60  GLN 60  59  59  GLN GLN S . n 
S  5  61  LYS 61  60  60  LYS LYS S . n 
S  5  62  LYS 62  61  61  LYS LYS S . n 
S  5  63  ILE 63  62  62  ILE ILE S . n 
S  5  64  ILE 64  63  63  ILE ILE S . n 
S  5  65  LYS 65  64  64  LYS LYS S . n 
S  5  66  CYS 66  65  65  CYS CYS S . n 
S  5  67  ASP 67  66  66  ASP ASP S . n 
S  5  68  GLU 68  67  67  GLU GLU S . n 
S  5  69  HIS 69  68  68  HIS HIS S . n 
S  5  70  MET 70  69  69  MET MET S . n 
S  5  71  GLY 71  70  70  GLY GLY S . n 
S  5  72  LEU 72  71  71  LEU LEU S . n 
S  5  73  SER 73  72  72  SER SER S . n 
S  5  74  LEU 74  73  73  LEU LEU S . n 
S  5  75  ALA 75  74  74  ALA ALA S . n 
S  5  76  GLY 76  75  75  GLY GLY S . n 
S  5  77  LEU 77  76  76  LEU LEU S . n 
S  5  78  ALA 78  77  77  ALA ALA S . n 
S  5  79  PRO 79  78  78  PRO PRO S . n 
S  5  80  ASP 80  79  79  ASP ASP S . n 
S  5  81  ALA 81  80  80  ALA ALA S . n 
S  5  82  ARG 82  81  81  ARG ARG S . n 
S  5  83  VAL 83  82  82  VAL VAL S . n 
S  5  84  LEU 84  83  83  LEU LEU S . n 
S  5  85  SER 85  84  84  SER SER S . n 
S  5  86  ASN 86  85  85  ASN ASN S . n 
S  5  87  TYR 87  86  86  TYR TYR S . n 
S  5  88  LEU 88  87  87  LEU LEU S . n 
S  5  89  ARG 89  88  88  ARG ARG S . n 
S  5  90  GLN 90  89  89  GLN GLN S . n 
S  5  91  GLN 91  90  90  GLN GLN S . n 
S  5  92  CYS 92  91  91  CYS CYS S . n 
S  5  93  ASN 93  92  92  ASN ASN S . n 
S  5  94  TYR 94  93  93  TYR TYR S . n 
S  5  95  SER 95  94  94  SER SER S . n 
S  5  96  SER 96  95  95  SER SER S . n 
S  5  97  LEU 97  96  96  LEU LEU S . n 
S  5  98  VAL 98  97  97  VAL VAL S . n 
S  5  99  PHE 99  98  98  PHE PHE S . n 
S  5  100 ASN 100 99  99  ASN ASN S . n 
S  5  101 ARG 101 100 100 ARG ARG S . n 
S  5  102 LYS 102 101 101 LYS LYS S . n 
S  5  103 LEU 103 102 102 LEU LEU S . n 
S  5  104 ALA 104 103 103 ALA ALA S . n 
S  5  105 VAL 105 104 104 VAL VAL S . n 
S  5  106 GLU 106 105 105 GLU GLU S . n 
S  5  107 ARG 107 106 106 ARG ARG S . n 
S  5  108 ALA 108 107 107 ALA ALA S . n 
S  5  109 GLY 109 108 108 GLY GLY S . n 
S  5  110 HIS 110 109 109 HIS HIS S . n 
S  5  111 LEU 111 110 110 LEU LEU S . n 
S  5  112 LEU 112 111 111 LEU LEU S . n 
S  5  113 CYS 113 112 112 CYS CYS S . n 
S  5  114 ASP 114 113 113 ASP ASP S . n 
S  5  115 LYS 115 114 114 LYS LYS S . n 
S  5  116 ALA 116 115 115 ALA ALA S . n 
S  5  117 GLN 117 116 116 GLN GLN S . n 
S  5  118 LYS 118 117 117 LYS LYS S . n 
S  5  119 ASN 119 118 118 ASN ASN S . n 
S  5  120 THR 120 119 119 THR THR S . n 
S  5  121 GLN 121 120 120 GLN GLN S . n 
S  5  122 SER 122 121 121 SER SER S . n 
S  5  123 TYR 123 122 122 TYR TYR S . n 
S  5  124 GLY 124 123 123 GLY GLY S . n 
S  5  125 GLY 125 124 124 GLY GLY S . n 
S  5  126 ARG 126 125 125 ARG ARG S . n 
S  5  127 PRO 127 126 126 PRO PRO S . n 
S  5  128 TYR 128 127 127 TYR TYR S . n 
S  5  129 GLY 129 128 128 GLY GLY S . n 
S  5  130 VAL 130 129 129 VAL VAL S . n 
S  5  131 GLY 131 130 130 GLY GLY S . n 
S  5  132 LEU 132 131 131 LEU LEU S . n 
S  5  133 LEU 133 132 132 LEU LEU S . n 
S  5  134 ILE 134 133 133 ILE ILE S . n 
S  5  135 ILE 135 134 134 ILE ILE S . n 
S  5  136 GLY 136 135 135 GLY GLY S . n 
S  5  137 TYR 137 136 136 TYR TYR S . n 
S  5  138 ASP 138 137 137 ASP ASP S . n 
S  5  139 LYS 139 138 138 LYS LYS S . n 
S  5  140 SER 140 139 139 SER SER S . n 
S  5  141 GLY 141 140 140 GLY GLY S . n 
S  5  142 ALA 142 141 141 ALA ALA S . n 
S  5  143 HIS 143 142 142 HIS HIS S . n 
S  5  144 LEU 144 143 143 LEU LEU S . n 
S  5  145 LEU 145 144 144 LEU LEU S . n 
S  5  146 GLU 146 145 145 GLU GLU S . n 
S  5  147 PHE 147 146 146 PHE PHE S . n 
S  5  148 GLN 148 147 147 GLN GLN S . n 
S  5  149 PRO 149 148 148 PRO PRO S . n 
S  5  150 SER 150 149 149 SER SER S . n 
S  5  151 GLY 151 150 150 GLY GLY S . n 
S  5  152 ASN 152 151 151 ASN ASN S . n 
S  5  153 VAL 153 152 152 VAL VAL S . n 
S  5  154 THR 154 153 153 THR THR S . n 
S  5  155 GLU 155 154 154 GLU GLU S . n 
S  5  156 LEU 156 155 155 LEU LEU S . n 
S  5  157 TYR 157 156 156 TYR TYR S . n 
S  5  158 GLY 158 157 157 GLY GLY S . n 
S  5  159 THR 159 158 158 THR THR S . n 
S  5  160 ALA 160 159 159 ALA ALA S . n 
S  5  161 ILE 161 160 160 ILE ILE S . n 
S  5  162 GLY 162 161 161 GLY GLY S . n 
S  5  163 ALA 163 162 162 ALA ALA S . n 
S  5  164 ARG 164 163 163 ARG ARG S . n 
S  5  165 SER 165 164 164 SER SER S . n 
S  5  166 GLN 166 165 165 GLN GLN S . n 
S  5  167 GLY 167 166 166 GLY GLY S . n 
S  5  168 ALA 168 167 167 ALA ALA S . n 
S  5  169 LYS 169 168 168 LYS LYS S . n 
S  5  170 THR 170 169 169 THR THR S . n 
S  5  171 TYR 171 170 170 TYR TYR S . n 
S  5  172 LEU 172 171 171 LEU LEU S . n 
S  5  173 GLU 173 172 172 GLU GLU S . n 
S  5  174 ARG 174 173 173 ARG ARG S . n 
S  5  175 THR 175 174 174 THR THR S . n 
S  5  176 LEU 176 175 175 LEU LEU S . n 
S  5  177 ASP 177 176 176 ASP ASP S . n 
S  5  178 THR 178 177 177 THR THR S . n 
S  5  179 PHE 179 178 178 PHE PHE S . n 
S  5  180 ILE 180 179 179 ILE ILE S . n 
S  5  181 LYS 181 180 180 LYS LYS S . n 
S  5  182 ILE 182 181 181 ILE ILE S . n 
S  5  183 ASP 183 182 182 ASP ASP S . n 
S  5  184 GLY 184 183 183 GLY GLY S . n 
S  5  185 ASN 185 184 184 ASN ASN S . n 
S  5  186 PRO 186 185 185 PRO PRO S . n 
S  5  187 ASP 187 186 186 ASP ASP S . n 
S  5  188 GLU 188 187 187 GLU GLU S . n 
S  5  189 LEU 189 188 188 LEU LEU S . n 
S  5  190 ILE 190 189 189 ILE ILE S . n 
S  5  191 LYS 191 190 190 LYS LYS S . n 
S  5  192 ALA 192 191 191 ALA ALA S . n 
S  5  193 GLY 193 192 192 GLY GLY S . n 
S  5  194 VAL 194 193 193 VAL VAL S . n 
S  5  195 GLU 195 194 194 GLU GLU S . n 
S  5  196 ALA 196 195 195 ALA ALA S . n 
S  5  197 ILE 197 196 196 ILE ILE S . n 
S  5  198 SER 198 197 197 SER SER S . n 
S  5  199 GLN 199 198 198 GLN GLN S . n 
S  5  200 SER 200 199 199 SER SER S . n 
S  5  201 LEU 201 200 200 LEU LEU S . n 
S  5  202 ARG 202 201 201 ARG ARG S . n 
S  5  203 ASP 203 202 202 ASP ASP S . n 
S  5  204 GLU 204 203 203 GLU GLU S . n 
S  5  205 SER 205 204 204 SER SER S . n 
S  5  206 LEU 206 205 205 LEU LEU S . n 
S  5  207 THR 207 206 206 THR THR S . n 
S  5  208 VAL 208 207 207 VAL VAL S . n 
S  5  209 ASP 209 208 208 ASP ASP S . n 
S  5  210 ASN 210 209 209 ASN ASN S . n 
S  5  211 LEU 211 210 210 LEU LEU S . n 
S  5  212 SER 212 211 211 SER SER S . n 
S  5  213 ILE 213 212 212 ILE ILE S . n 
S  5  214 ALA 214 213 213 ALA ALA S . n 
S  5  215 ILE 215 214 214 ILE ILE S . n 
S  5  216 VAL 216 215 215 VAL VAL S . n 
S  5  217 GLY 217 216 216 GLY GLY S . n 
S  5  218 LYS 218 217 217 LYS LYS S . n 
S  5  219 ASP 219 218 218 ASP ASP S . n 
S  5  220 THR 220 219 219 THR THR S . n 
S  5  221 PRO 221 220 220 PRO PRO S . n 
S  5  222 PHE 222 221 221 PHE PHE S . n 
S  5  223 THR 223 222 222 THR THR S . n 
S  5  224 ILE 224 223 223 ILE ILE S . n 
S  5  225 TYR 225 224 224 TYR TYR S . n 
S  5  226 ASP 226 225 225 ASP ASP S . n 
S  5  227 GLY 227 226 226 GLY GLY S . n 
S  5  228 GLU 228 227 227 GLU GLU S . n 
S  5  229 ALA 229 228 228 ALA ALA S . n 
S  5  230 VAL 230 229 229 VAL VAL S . n 
S  5  231 ALA 231 230 230 ALA ALA S . n 
S  5  232 LYS 232 231 231 LYS LYS S . n 
S  5  233 TYR 233 232 232 TYR TYR S . n 
S  5  234 ILE 234 233 233 ILE ILE S . n 
T  6  1   MET 1   -3  ?   ?   ?   T . n 
T  6  2   THR 2   -2  ?   ?   ?   T . n 
T  6  3   SER 3   -1  ?   ?   ?   T . n 
T  6  4   ILE 4   0   ?   ?   ?   T . n 
T  6  5   GLY 5   1   ?   ?   ?   T . n 
T  6  6   THR 6   2   2   THR THR T . n 
T  6  7   GLY 7   3   3   GLY GLY T . n 
T  6  8   TYR 8   4   4   TYR TYR T . n 
T  6  9   ASP 9   5   5   ASP ASP T . n 
T  6  10  LEU 10  6   6   LEU LEU T . n 
T  6  11  SER 11  7   7   SER SER T . n 
T  6  12  ASN 12  8   8   ASN ASN T . n 
T  6  13  SER 13  9   9   SER SER T . n 
T  6  14  VAL 14  10  10  VAL VAL T . n 
T  6  15  PHE 15  11  11  PHE PHE T . n 
T  6  16  SER 16  12  12  SER SER T . n 
T  6  17  PRO 17  13  13  PRO PRO T . n 
T  6  18  ASP 18  14  14  ASP ASP T . n 
T  6  19  GLY 19  15  15  GLY GLY T . n 
T  6  20  ARG 20  16  16  ARG ARG T . n 
T  6  21  ASN 21  17  17  ASN ASN T . n 
T  6  22  PHE 22  18  18  PHE PHE T . n 
T  6  23  GLN 23  19  19  GLN GLN T . n 
T  6  24  VAL 24  20  20  VAL VAL T . n 
T  6  25  GLU 25  21  21  GLU GLU T . n 
T  6  26  TYR 26  22  22  TYR TYR T . n 
T  6  27  ALA 27  23  23  ALA ALA T . n 
T  6  28  VAL 28  24  24  VAL VAL T . n 
T  6  29  LYS 29  25  25  LYS LYS T . n 
T  6  30  ALA 30  26  26  ALA ALA T . n 
T  6  31  VAL 31  27  27  VAL VAL T . n 
T  6  32  GLU 32  28  28  GLU GLU T . n 
T  6  33  ASN 33  29  29  ASN ASN T . n 
T  6  34  GLY 34  30  30  GLY GLY T . n 
T  6  35  THR 35  31  31  THR THR T . n 
T  6  36  THR 36  32  32  THR THR T . n 
T  6  37  SER 37  33  33  SER SER T . n 
T  6  38  ILE 38  34  34  ILE ILE T . n 
T  6  39  GLY 39  35  35  GLY GLY T . n 
T  6  40  ILE 40  36  36  ILE ILE T . n 
T  6  41  LYS 41  37  37  LYS LYS T . n 
T  6  42  CYS 42  38  38  CYS CYS T . n 
T  6  43  ASN 43  39  39  ASN ASN T . n 
T  6  44  ASP 44  40  40  ASP ASP T . n 
T  6  45  GLY 45  41  41  GLY GLY T . n 
T  6  46  VAL 46  42  42  VAL VAL T . n 
T  6  47  VAL 47  43  43  VAL VAL T . n 
T  6  48  PHE 48  44  44  PHE PHE T . n 
T  6  49  ALA 49  45  45  ALA ALA T . n 
T  6  50  VAL 50  46  46  VAL VAL T . n 
T  6  51  GLU 51  47  47  GLU GLU T . n 
T  6  52  LYS 52  48  48  LYS LYS T . n 
T  6  53  LEU 53  49  49  LEU LEU T . n 
T  6  54  ILE 54  50  50  ILE ILE T . n 
T  6  55  THR 55  51  51  THR THR T . n 
T  6  56  SER 56  52  52  SER SER T . n 
T  6  57  LYS 57  53  53  LYS LYS T . n 
T  6  58  LEU 58  54  54  LEU LEU T . n 
T  6  59  LEU 59  55  55  LEU LEU T . n 
T  6  60  VAL 60  56  56  VAL VAL T . n 
T  6  61  PRO 61  57  57  PRO PRO T . n 
T  6  62  GLN 62  58  58  GLN GLN T . n 
T  6  63  LYS 63  59  59  LYS LYS T . n 
T  6  64  ASN 64  60  60  ASN ASN T . n 
T  6  65  VAL 65  61  61  VAL VAL T . n 
T  6  66  LYS 66  62  62  LYS LYS T . n 
T  6  67  ILE 67  63  63  ILE ILE T . n 
T  6  68  GLN 68  64  64  GLN GLN T . n 
T  6  69  VAL 69  65  65  VAL VAL T . n 
T  6  70  VAL 70  66  66  VAL VAL T . n 
T  6  71  ASP 71  67  67  ASP ASP T . n 
T  6  72  ARG 72  68  68  ARG ARG T . n 
T  6  73  HIS 73  69  69  HIS HIS T . n 
T  6  74  ILE 74  70  70  ILE ILE T . n 
T  6  75  GLY 75  71  71  GLY GLY T . n 
T  6  76  CYS 76  72  72  CYS CYS T . n 
T  6  77  VAL 77  73  73  VAL VAL T . n 
T  6  78  TYR 78  74  74  TYR TYR T . n 
T  6  79  SER 79  75  75  SER SER T . n 
T  6  80  GLY 80  76  76  GLY GLY T . n 
T  6  81  LEU 81  77  77  LEU LEU T . n 
T  6  82  ILE 82  78  78  ILE ILE T . n 
T  6  83  PRO 83  79  79  PRO PRO T . n 
T  6  84  ASP 84  80  80  ASP ASP T . n 
T  6  85  GLY 85  81  81  GLY GLY T . n 
T  6  86  ARG 86  82  82  ARG ARG T . n 
T  6  87  HIS 87  83  83  HIS HIS T . n 
T  6  88  LEU 88  84  84  LEU LEU T . n 
T  6  89  VAL 89  85  85  VAL VAL T . n 
T  6  90  ASN 90  86  86  ASN ASN T . n 
T  6  91  ARG 91  87  87  ARG ARG T . n 
T  6  92  GLY 92  88  88  GLY GLY T . n 
T  6  93  ARG 93  89  89  ARG ARG T . n 
T  6  94  GLU 94  90  90  GLU GLU T . n 
T  6  95  GLU 95  91  91  GLU GLU T . n 
T  6  96  ALA 96  92  92  ALA ALA T . n 
T  6  97  ALA 97  93  93  ALA ALA T . n 
T  6  98  SER 98  94  94  SER SER T . n 
T  6  99  PHE 99  95  95  PHE PHE T . n 
T  6  100 LYS 100 96  96  LYS LYS T . n 
T  6  101 LYS 101 97  97  LYS LYS T . n 
T  6  102 LEU 102 98  98  LEU LEU T . n 
T  6  103 TYR 103 99  99  TYR TYR T . n 
T  6  104 LYS 104 100 100 LYS LYS T . n 
T  6  105 THR 105 101 101 THR THR T . n 
T  6  106 PRO 106 102 102 PRO PRO T . n 
T  6  107 ILE 107 103 103 ILE ILE T . n 
T  6  108 PRO 108 104 104 PRO PRO T . n 
T  6  109 ILE 109 105 105 ILE ILE T . n 
T  6  110 PRO 110 106 106 PRO PRO T . n 
T  6  111 ALA 111 107 107 ALA ALA T . n 
T  6  112 PHE 112 108 108 PHE PHE T . n 
T  6  113 ALA 113 109 109 ALA ALA T . n 
T  6  114 ASP 114 110 110 ASP ASP T . n 
T  6  115 ARG 115 111 111 ARG ARG T . n 
T  6  116 LEU 116 112 112 LEU LEU T . n 
T  6  117 GLY 117 113 113 GLY GLY T . n 
T  6  118 GLN 118 114 114 GLN GLN T . n 
T  6  119 TYR 119 115 115 TYR TYR T . n 
T  6  120 VAL 120 116 116 VAL VAL T . n 
T  6  121 GLN 121 117 117 GLN GLN T . n 
T  6  122 ALA 122 118 118 ALA ALA T . n 
T  6  123 HIS 123 119 119 HIS HIS T . n 
T  6  124 THR 124 120 120 THR THR T . n 
T  6  125 LEU 125 121 121 LEU LEU T . n 
T  6  126 TYR 126 122 122 TYR TYR T . n 
T  6  127 ASN 127 123 123 ASN ASN T . n 
T  6  128 SER 128 124 124 SER SER T . n 
T  6  129 VAL 129 125 125 VAL VAL T . n 
T  6  130 ARG 130 126 126 ARG ARG T . n 
T  6  131 PRO 131 127 127 PRO PRO T . n 
T  6  132 PHE 132 128 128 PHE PHE T . n 
T  6  133 GLY 133 129 129 GLY GLY T . n 
T  6  134 VAL 134 130 130 VAL VAL T . n 
T  6  135 SER 135 131 131 SER SER T . n 
T  6  136 THR 136 132 132 THR THR T . n 
T  6  137 ILE 137 133 133 ILE ILE T . n 
T  6  138 PHE 138 134 134 PHE PHE T . n 
T  6  139 GLY 139 135 135 GLY GLY T . n 
T  6  140 GLY 140 136 136 GLY GLY T . n 
T  6  141 VAL 141 137 137 VAL VAL T . n 
T  6  142 ASP 142 138 138 ASP ASP T . n 
T  6  143 LYS 143 139 139 LYS LYS T . n 
T  6  144 ASN 144 140 140 ASN ASN T . n 
T  6  145 GLY 145 141 141 GLY GLY T . n 
T  6  146 ALA 146 142 142 ALA ALA T . n 
T  6  147 HIS 147 143 143 HIS HIS T . n 
T  6  148 LEU 148 144 144 LEU LEU T . n 
T  6  149 TYR 149 145 145 TYR TYR T . n 
T  6  150 MET 150 146 146 MET MET T . n 
T  6  151 LEU 151 147 147 LEU LEU T . n 
T  6  152 GLU 152 148 148 GLU GLU T . n 
T  6  153 PRO 153 149 149 PRO PRO T . n 
T  6  154 SER 154 150 150 SER SER T . n 
T  6  155 GLY 155 151 151 GLY GLY T . n 
T  6  156 SER 156 152 152 SER SER T . n 
T  6  157 TYR 157 153 153 TYR TYR T . n 
T  6  158 TRP 158 154 154 TRP TRP T . n 
T  6  159 GLY 159 155 155 GLY GLY T . n 
T  6  160 TYR 160 156 156 TYR TYR T . n 
T  6  161 LYS 161 157 157 LYS LYS T . n 
T  6  162 GLY 162 158 158 GLY GLY T . n 
T  6  163 ALA 163 159 159 ALA ALA T . n 
T  6  164 ALA 164 160 160 ALA ALA T . n 
T  6  165 THR 165 161 161 THR THR T . n 
T  6  166 GLY 166 162 162 GLY GLY T . n 
T  6  167 LYS 167 163 163 LYS LYS T . n 
T  6  168 GLY 168 164 164 GLY GLY T . n 
T  6  169 ARG 169 165 165 ARG ARG T . n 
T  6  170 GLN 170 166 166 GLN GLN T . n 
T  6  171 SER 171 167 167 SER SER T . n 
T  6  172 ALA 172 168 168 ALA ALA T . n 
T  6  173 LYS 173 169 169 LYS LYS T . n 
T  6  174 ALA 174 170 170 ALA ALA T . n 
T  6  175 GLU 175 171 171 GLU GLU T . n 
T  6  176 LEU 176 172 172 LEU LEU T . n 
T  6  177 GLU 177 173 173 GLU GLU T . n 
T  6  178 LYS 178 174 174 LYS LYS T . n 
T  6  179 LEU 179 175 175 LEU LEU T . n 
T  6  180 VAL 180 176 176 VAL VAL T . n 
T  6  181 ASP 181 177 177 ASP ASP T . n 
T  6  182 HIS 182 178 178 HIS HIS T . n 
T  6  183 HIS 183 179 179 HIS HIS T . n 
T  6  184 PRO 184 180 180 PRO PRO T . n 
T  6  185 GLU 185 181 181 GLU GLU T . n 
T  6  186 GLY 186 182 182 GLY GLY T . n 
T  6  187 LEU 187 183 183 LEU LEU T . n 
T  6  188 SER 188 184 184 SER SER T . n 
T  6  189 ALA 189 185 185 ALA ALA T . n 
T  6  190 ARG 190 186 186 ARG ARG T . n 
T  6  191 GLU 191 187 187 GLU GLU T . n 
T  6  192 ALA 192 188 188 ALA ALA T . n 
T  6  193 VAL 193 189 189 VAL VAL T . n 
T  6  194 LYS 194 190 190 LYS LYS T . n 
T  6  195 GLN 195 191 191 GLN GLN T . n 
T  6  196 ALA 196 192 192 ALA ALA T . n 
T  6  197 ALA 197 193 193 ALA ALA T . n 
T  6  198 LYS 198 194 194 LYS LYS T . n 
T  6  199 ILE 199 195 195 ILE ILE T . n 
T  6  200 ILE 200 196 196 ILE ILE T . n 
T  6  201 TYR 201 197 197 TYR TYR T . n 
T  6  202 LEU 202 198 198 LEU LEU T . n 
T  6  203 ALA 203 199 199 ALA ALA T . n 
T  6  204 HIS 204 200 200 HIS HIS T . n 
T  6  205 GLU 205 201 201 GLU GLU T . n 
T  6  206 ASP 206 202 202 ASP ASP T . n 
T  6  207 ASN 207 203 203 ASN ASN T . n 
T  6  208 LYS 208 204 204 LYS LYS T . n 
T  6  209 GLU 209 205 205 GLU GLU T . n 
T  6  210 LYS 210 206 206 LYS LYS T . n 
T  6  211 ASP 211 207 207 ASP ASP T . n 
T  6  212 PHE 212 208 208 PHE PHE T . n 
T  6  213 GLU 213 209 209 GLU GLU T . n 
T  6  214 LEU 214 210 210 LEU LEU T . n 
T  6  215 GLU 215 211 211 GLU GLU T . n 
T  6  216 ILE 216 212 212 ILE ILE T . n 
T  6  217 SER 217 213 213 SER SER T . n 
T  6  218 TRP 218 214 214 TRP TRP T . n 
T  6  219 CYS 219 215 215 CYS CYS T . n 
T  6  220 SER 220 216 216 SER SER T . n 
T  6  221 LEU 221 217 217 LEU LEU T . n 
T  6  222 SER 222 218 218 SER SER T . n 
T  6  223 GLU 223 219 219 GLU GLU T . n 
T  6  224 THR 224 220 220 THR THR T . n 
T  6  225 ASN 225 221 221 ASN ASN T . n 
T  6  226 GLY 226 222 222 GLY GLY T . n 
T  6  227 LEU 227 223 223 LEU LEU T . n 
T  6  228 HIS 228 224 224 HIS HIS T . n 
T  6  229 LYS 229 225 225 LYS LYS T . n 
T  6  230 PHE 230 226 226 PHE PHE T . n 
T  6  231 VAL 231 227 227 VAL VAL T . n 
T  6  232 LYS 232 228 228 LYS LYS T . n 
T  6  233 GLY 233 229 229 GLY GLY T . n 
T  6  234 ASP 234 230 230 ASP ASP T . n 
T  6  235 LEU 235 231 231 LEU LEU T . n 
T  6  236 LEU 236 232 232 LEU LEU T . n 
T  6  237 GLN 237 233 233 GLN GLN T . n 
T  6  238 GLU 238 234 234 GLU GLU T . n 
T  6  239 ALA 239 235 235 ALA ALA T . n 
T  6  240 ILE 240 236 236 ILE ILE T . n 
T  6  241 ASP 241 237 237 ASP ASP T . n 
T  6  242 PHE 242 238 238 PHE PHE T . n 
T  6  243 ALA 243 239 239 ALA ALA T . n 
T  6  244 GLN 244 240 240 GLN GLN T . n 
T  6  245 LYS 245 241 241 LYS LYS T . n 
T  6  246 GLU 246 242 242 GLU GLU T . n 
T  6  247 ILE 247 243 243 ILE ILE T . n 
T  6  248 ASN 248 244 244 ASN ASN T . n 
T  6  249 GLY 249 245 ?   ?   ?   T . n 
T  6  250 ASP 250 246 ?   ?   ?   T . n 
T  6  251 ASP 251 247 ?   ?   ?   T . n 
T  6  252 ASP 252 248 ?   ?   ?   T . n 
T  6  253 GLU 253 249 ?   ?   ?   T . n 
T  6  254 ASP 254 250 ?   ?   ?   T . n 
T  6  255 GLU 255 251 ?   ?   ?   T . n 
T  6  256 ASP 256 252 ?   ?   ?   T . n 
T  6  257 ASP 257 253 ?   ?   ?   T . n 
T  6  258 SER 258 254 ?   ?   ?   T . n 
T  6  259 ASP 259 255 ?   ?   ?   T . n 
T  6  260 ASN 260 256 ?   ?   ?   T . n 
T  6  261 VAL 261 257 ?   ?   ?   T . n 
T  6  262 MET 262 258 ?   ?   ?   T . n 
T  6  263 SER 263 259 ?   ?   ?   T . n 
T  6  264 SER 264 260 ?   ?   ?   T . n 
T  6  265 ASP 265 261 ?   ?   ?   T . n 
T  6  266 ASP 266 262 ?   ?   ?   T . n 
T  6  267 GLU 267 263 ?   ?   ?   T . n 
T  6  268 ASN 268 264 ?   ?   ?   T . n 
T  6  269 ALA 269 265 ?   ?   ?   T . n 
T  6  270 PRO 270 266 ?   ?   ?   T . n 
T  6  271 VAL 271 267 ?   ?   ?   T . n 
T  6  272 ALA 272 268 ?   ?   ?   T . n 
T  6  273 THR 273 269 ?   ?   ?   T . n 
T  6  274 ASN 274 270 ?   ?   ?   T . n 
T  6  275 ALA 275 271 ?   ?   ?   T . n 
T  6  276 ASN 276 272 ?   ?   ?   T . n 
T  6  277 ALA 277 273 ?   ?   ?   T . n 
T  6  278 THR 278 274 ?   ?   ?   T . n 
T  6  279 THR 279 275 ?   ?   ?   T . n 
T  6  280 ASP 280 276 ?   ?   ?   T . n 
T  6  281 GLN 281 277 ?   ?   ?   T . n 
T  6  282 GLU 282 278 ?   ?   ?   T . n 
T  6  283 GLY 283 279 ?   ?   ?   T . n 
T  6  284 ASP 284 280 ?   ?   ?   T . n 
T  6  285 ILE 285 281 ?   ?   ?   T . n 
T  6  286 HIS 286 282 ?   ?   ?   T . n 
T  6  287 LEU 287 283 ?   ?   ?   T . n 
T  6  288 GLU 288 284 ?   ?   ?   T . n 
U  7  1   MET 1   -8  ?   ?   ?   U . n 
U  7  2   SER 2   -7  ?   ?   ?   U . n 
U  7  3   GLY 3   -6  ?   ?   ?   U . n 
U  7  4   ALA 4   -5  ?   ?   ?   U . n 
U  7  5   ALA 5   -4  ?   ?   ?   U . n 
U  7  6   ALA 6   -3  ?   ?   ?   U . n 
U  7  7   ALA 7   -2  ?   ?   ?   U . n 
U  7  8   SER 8   -1  ?   ?   ?   U . n 
U  7  9   ALA 9   0   ?   ?   ?   U . n 
U  7  10  ALA 10  1   ?   ?   ?   U . n 
U  7  11  GLY 11  2   2   GLY GLY U . n 
U  7  12  TYR 12  3   3   TYR TYR U . n 
U  7  13  ASP 13  4   4   ASP ASP U . n 
U  7  14  ARG 14  5   5   ARG ARG U . n 
U  7  15  HIS 15  6   6   HIS HIS U . n 
U  7  16  ILE 16  7   7   ILE ILE U . n 
U  7  17  THR 17  8   8   THR THR U . n 
U  7  18  ILE 18  9   9   ILE ILE U . n 
U  7  19  PHE 19  10  10  PHE PHE U . n 
U  7  20  SER 20  11  11  SER SER U . n 
U  7  21  PRO 21  12  12  PRO PRO U . n 
U  7  22  GLU 22  13  13  GLU GLU U . n 
U  7  23  GLY 23  14  14  GLY GLY U . n 
U  7  24  ARG 24  15  15  ARG ARG U . n 
U  7  25  LEU 25  16  16  LEU LEU U . n 
U  7  26  TYR 26  17  17  TYR TYR U . n 
U  7  27  GLN 27  18  18  GLN GLN U . n 
U  7  28  VAL 28  19  19  VAL VAL U . n 
U  7  29  GLU 29  20  20  GLU GLU U . n 
U  7  30  TYR 30  21  21  TYR TYR U . n 
U  7  31  ALA 31  22  22  ALA ALA U . n 
U  7  32  PHE 32  23  23  PHE PHE U . n 
U  7  33  LYS 33  24  24  LYS LYS U . n 
U  7  34  ALA 34  25  25  ALA ALA U . n 
U  7  35  THR 35  26  26  THR THR U . n 
U  7  36  ASN 36  27  27  ASN ASN U . n 
U  7  37  GLN 37  28  28  GLN GLN U . n 
U  7  38  THR 38  29  29  THR THR U . n 
U  7  39  ASN 39  30  30  ASN ASN U . n 
U  7  40  ILE 40  31  31  ILE ILE U . n 
U  7  41  ASN 41  32  32  ASN ASN U . n 
U  7  42  SER 42  33  33  SER SER U . n 
U  7  43  LEU 43  34  34  LEU LEU U . n 
U  7  44  ALA 44  35  35  ALA ALA U . n 
U  7  45  VAL 45  36  36  VAL VAL U . n 
U  7  46  ARG 46  37  37  ARG ARG U . n 
U  7  47  GLY 47  38  38  GLY GLY U . n 
U  7  48  LYS 48  39  39  LYS LYS U . n 
U  7  49  ASP 49  40  40  ASP ASP U . n 
U  7  50  CYS 50  41  41  CYS CYS U . n 
U  7  51  THR 51  42  42  THR THR U . n 
U  7  52  VAL 52  43  43  VAL VAL U . n 
U  7  53  VAL 53  44  44  VAL VAL U . n 
U  7  54  ILE 54  45  45  ILE ILE U . n 
U  7  55  SER 55  46  46  SER SER U . n 
U  7  56  GLN 56  47  47  GLN GLN U . n 
U  7  57  LYS 57  48  48  LYS LYS U . n 
U  7  58  LYS 58  49  49  LYS LYS U . n 
U  7  59  VAL 59  50  50  VAL VAL U . n 
U  7  60  PRO 60  51  51  PRO PRO U . n 
U  7  61  ASP 61  52  52  ASP ASP U . n 
U  7  62  LYS 62  53  53  LYS LYS U . n 
U  7  63  LEU 63  54  54  LEU LEU U . n 
U  7  64  LEU 64  55  55  LEU LEU U . n 
U  7  65  ASP 65  56  56  ASP ASP U . n 
U  7  66  PRO 66  57  57  PRO PRO U . n 
U  7  67  THR 67  58  58  THR THR U . n 
U  7  68  THR 68  59  59  THR THR U . n 
U  7  69  VAL 69  60  60  VAL VAL U . n 
U  7  70  SER 70  61  61  SER SER U . n 
U  7  71  TYR 71  62  62  TYR TYR U . n 
U  7  72  ILE 72  63  63  ILE ILE U . n 
U  7  73  PHE 73  64  64  PHE PHE U . n 
U  7  74  CYS 74  65  65  CYS CYS U . n 
U  7  75  ILE 75  66  66  ILE ILE U . n 
U  7  76  SER 76  67  67  SER SER U . n 
U  7  77  ARG 77  68  68  ARG ARG U . n 
U  7  78  THR 78  69  69  THR THR U . n 
U  7  79  ILE 79  70  70  ILE ILE U . n 
U  7  80  GLY 80  71  71  GLY GLY U . n 
U  7  81  MET 81  72  72  MET MET U . n 
U  7  82  VAL 82  73  73  VAL VAL U . n 
U  7  83  VAL 83  74  74  VAL VAL U . n 
U  7  84  ASN 84  75  75  ASN ASN U . n 
U  7  85  GLY 85  76  76  GLY GLY U . n 
U  7  86  PRO 86  77  77  PRO PRO U . n 
U  7  87  ILE 87  78  78  ILE ILE U . n 
U  7  88  PRO 88  79  79  PRO PRO U . n 
U  7  89  ASP 89  80  80  ASP ASP U . n 
U  7  90  ALA 90  81  81  ALA ALA U . n 
U  7  91  ARG 91  82  82  ARG ARG U . n 
U  7  92  ASN 92  83  83  ASN ASN U . n 
U  7  93  ALA 93  84  84  ALA ALA U . n 
U  7  94  ALA 94  85  85  ALA ALA U . n 
U  7  95  LEU 95  86  86  LEU LEU U . n 
U  7  96  ARG 96  87  87  ARG ARG U . n 
U  7  97  ALA 97  88  88  ALA ALA U . n 
U  7  98  LYS 98  89  89  LYS LYS U . n 
U  7  99  ALA 99  90  90  ALA ALA U . n 
U  7  100 GLU 100 91  91  GLU GLU U . n 
U  7  101 ALA 101 92  92  ALA ALA U . n 
U  7  102 ALA 102 93  93  ALA ALA U . n 
U  7  103 GLU 103 94  94  GLU GLU U . n 
U  7  104 PHE 104 95  95  PHE PHE U . n 
U  7  105 ARG 105 96  96  ARG ARG U . n 
U  7  106 TYR 106 97  97  TYR TYR U . n 
U  7  107 LYS 107 98  98  LYS LYS U . n 
U  7  108 TYR 108 99  99  TYR TYR U . n 
U  7  109 GLY 109 100 100 GLY GLY U . n 
U  7  110 TYR 110 101 101 TYR TYR U . n 
U  7  111 ASP 111 102 102 ASP ASP U . n 
U  7  112 MET 112 103 103 MET MET U . n 
U  7  113 PRO 113 104 104 PRO PRO U . n 
U  7  114 CYS 114 105 105 CYS CYS U . n 
U  7  115 ASP 115 106 106 ASP ASP U . n 
U  7  116 VAL 116 107 107 VAL VAL U . n 
U  7  117 LEU 117 108 108 LEU LEU U . n 
U  7  118 ALA 118 109 109 ALA ALA U . n 
U  7  119 LYS 119 110 110 LYS LYS U . n 
U  7  120 ARG 120 111 111 ARG ARG U . n 
U  7  121 MET 121 112 112 MET MET U . n 
U  7  122 ALA 122 113 113 ALA ALA U . n 
U  7  123 ASN 123 114 114 ASN ASN U . n 
U  7  124 LEU 124 115 115 LEU LEU U . n 
U  7  125 SER 125 116 116 SER SER U . n 
U  7  126 GLN 126 117 117 GLN GLN U . n 
U  7  127 ILE 127 118 118 ILE ILE U . n 
U  7  128 TYR 128 119 119 TYR TYR U . n 
U  7  129 THR 129 120 120 THR THR U . n 
U  7  130 GLN 130 121 121 GLN GLN U . n 
U  7  131 ARG 131 122 122 ARG ARG U . n 
U  7  132 ALA 132 123 123 ALA ALA U . n 
U  7  133 TYR 133 124 124 TYR TYR U . n 
U  7  134 MET 134 125 125 MET MET U . n 
U  7  135 ARG 135 126 126 ARG ARG U . n 
U  7  136 PRO 136 127 127 PRO PRO U . n 
U  7  137 LEU 137 128 128 LEU LEU U . n 
U  7  138 GLY 138 129 129 GLY GLY U . n 
U  7  139 VAL 139 130 130 VAL VAL U . n 
U  7  140 ILE 140 131 131 ILE ILE U . n 
U  7  141 LEU 141 132 132 LEU LEU U . n 
U  7  142 THR 142 133 133 THR THR U . n 
U  7  143 PHE 143 134 134 PHE PHE U . n 
U  7  144 VAL 144 135 135 VAL VAL U . n 
U  7  145 SER 145 136 136 SER SER U . n 
U  7  146 VAL 146 137 137 VAL VAL U . n 
U  7  147 ASP 147 138 138 ASP ASP U . n 
U  7  148 GLU 148 139 139 GLU GLU U . n 
U  7  149 GLU 149 140 140 GLU GLU U . n 
U  7  150 LEU 150 141 141 LEU LEU U . n 
U  7  151 GLY 151 142 142 GLY GLY U . n 
U  7  152 PRO 152 143 143 PRO PRO U . n 
U  7  153 SER 153 144 144 SER SER U . n 
U  7  154 ILE 154 145 145 ILE ILE U . n 
U  7  155 TYR 155 146 146 TYR TYR U . n 
U  7  156 LYS 156 147 147 LYS LYS U . n 
U  7  157 THR 157 148 148 THR THR U . n 
U  7  158 ASP 158 149 149 ASP ASP U . n 
U  7  159 PRO 159 150 150 PRO PRO U . n 
U  7  160 ALA 160 151 151 ALA ALA U . n 
U  7  161 GLY 161 152 152 GLY GLY U . n 
U  7  162 TYR 162 153 153 TYR TYR U . n 
U  7  163 TYR 163 154 154 TYR TYR U . n 
U  7  164 VAL 164 155 155 VAL VAL U . n 
U  7  165 GLY 165 156 156 GLY GLY U . n 
U  7  166 TYR 166 157 157 TYR TYR U . n 
U  7  167 LYS 167 158 158 LYS LYS U . n 
U  7  168 ALA 168 159 159 ALA ALA U . n 
U  7  169 THR 169 160 160 THR THR U . n 
U  7  170 ALA 170 161 161 ALA ALA U . n 
U  7  171 THR 171 162 162 THR THR U . n 
U  7  172 GLY 172 163 163 GLY GLY U . n 
U  7  173 PRO 173 164 164 PRO PRO U . n 
U  7  174 LYS 174 165 165 LYS LYS U . n 
U  7  175 GLN 175 166 166 GLN GLN U . n 
U  7  176 GLN 176 167 167 GLN GLN U . n 
U  7  177 GLU 177 168 168 GLU GLU U . n 
U  7  178 ILE 178 169 169 ILE ILE U . n 
U  7  179 THR 179 170 170 THR THR U . n 
U  7  180 THR 180 171 171 THR THR U . n 
U  7  181 ASN 181 172 172 ASN ASN U . n 
U  7  182 LEU 182 173 173 LEU LEU U . n 
U  7  183 GLU 183 174 174 GLU GLU U . n 
U  7  184 ASN 184 175 175 ASN ASN U . n 
U  7  185 HIS 185 176 176 HIS HIS U . n 
U  7  186 PHE 186 177 177 PHE PHE U . n 
U  7  187 LYS 187 178 178 LYS LYS U . n 
U  7  188 LYS 188 179 179 LYS LYS U . n 
U  7  189 SER 189 180 180 SER SER U . n 
U  7  190 LYS 190 181 181 LYS LYS U . n 
U  7  191 ILE 191 182 182 ILE ILE U . n 
U  7  192 ASP 192 183 183 ASP ASP U . n 
U  7  193 HIS 193 184 184 HIS HIS U . n 
U  7  194 ILE 194 185 185 ILE ILE U . n 
U  7  195 ASN 195 186 186 ASN ASN U . n 
U  7  196 GLU 196 187 187 GLU GLU U . n 
U  7  197 GLU 197 188 188 GLU GLU U . n 
U  7  198 SER 198 189 189 SER SER U . n 
U  7  199 TRP 199 190 190 TRP TRP U . n 
U  7  200 GLU 200 191 191 GLU GLU U . n 
U  7  201 LYS 201 192 192 LYS LYS U . n 
U  7  202 VAL 202 193 193 VAL VAL U . n 
U  7  203 VAL 203 194 194 VAL VAL U . n 
U  7  204 GLU 204 195 195 GLU GLU U . n 
U  7  205 PHE 205 196 196 PHE PHE U . n 
U  7  206 ALA 206 197 197 ALA ALA U . n 
U  7  207 ILE 207 198 198 ILE ILE U . n 
U  7  208 THR 208 199 199 THR THR U . n 
U  7  209 HIS 209 200 200 HIS HIS U . n 
U  7  210 MET 210 201 201 MET MET U . n 
U  7  211 ILE 211 202 202 ILE ILE U . n 
U  7  212 ASP 212 203 203 ASP ASP U . n 
U  7  213 ALA 213 204 204 ALA ALA U . n 
U  7  214 LEU 214 205 205 LEU LEU U . n 
U  7  215 GLY 215 206 206 GLY GLY U . n 
U  7  216 THR 216 207 207 THR THR U . n 
U  7  217 GLU 217 208 208 GLU GLU U . n 
U  7  218 PHE 218 209 209 PHE PHE U . n 
U  7  219 SER 219 210 210 SER SER U . n 
U  7  220 LYS 220 211 211 LYS LYS U . n 
U  7  221 ASN 221 212 212 ASN ASN U . n 
U  7  222 ASP 222 213 213 ASP ASP U . n 
U  7  223 LEU 223 214 214 LEU LEU U . n 
U  7  224 GLU 224 215 215 GLU GLU U . n 
U  7  225 VAL 225 216 216 VAL VAL U . n 
U  7  226 GLY 226 217 217 GLY GLY U . n 
U  7  227 VAL 227 218 218 VAL VAL U . n 
U  7  228 ALA 228 219 219 ALA ALA U . n 
U  7  229 THR 229 220 220 THR THR U . n 
U  7  230 LYS 230 221 221 LYS LYS U . n 
U  7  231 ASP 231 222 222 ASP ASP U . n 
U  7  232 LYS 232 223 223 LYS LYS U . n 
U  7  233 PHE 233 224 224 PHE PHE U . n 
U  7  234 PHE 234 225 225 PHE PHE U . n 
U  7  235 THR 235 226 226 THR THR U . n 
U  7  236 LEU 236 227 227 LEU LEU U . n 
U  7  237 SER 237 228 228 SER SER U . n 
U  7  238 ALA 238 229 229 ALA ALA U . n 
U  7  239 GLU 239 230 230 GLU GLU U . n 
U  7  240 ASN 240 231 231 ASN ASN U . n 
U  7  241 ILE 241 232 232 ILE ILE U . n 
U  7  242 GLU 242 233 233 GLU GLU U . n 
U  7  243 GLU 243 234 234 GLU GLU U . n 
U  7  244 ARG 244 235 235 ARG ARG U . n 
U  7  245 LEU 245 236 236 LEU LEU U . n 
U  7  246 VAL 246 237 237 VAL VAL U . n 
U  7  247 ALA 247 238 238 ALA ALA U . n 
U  7  248 ILE 248 239 239 ILE ILE U . n 
U  7  249 ALA 249 240 240 ALA ALA U . n 
U  7  250 GLU 250 241 241 GLU GLU U . n 
U  7  251 GLN 251 242 242 GLN GLN U . n 
U  7  252 ASP 252 243 ?   ?   ?   U . n 
V  8  1   THR 1   2   2   THR THR V . n 
V  8  2   ILE 2   3   3   ILE ILE V . n 
V  8  3   VAL 3   4   4   VAL VAL V . n 
V  8  4   GLY 4   5   5   GLY GLY V . n 
V  8  5   VAL 5   6   6   VAL VAL V . n 
V  8  6   LYS 6   7   7   LYS LYS V . n 
V  8  7   PHE 7   8   8   PHE PHE V . n 
V  8  8   ASN 8   9   9   ASN ASN V . n 
V  8  9   ASN 9   10  10  ASN ASN V . n 
V  8  10  GLY 10  11  11  GLY GLY V . n 
V  8  11  VAL 11  12  12  VAL VAL V . n 
V  8  12  VAL 12  13  13  VAL VAL V . n 
V  8  13  ILE 13  14  14  ILE ILE V . n 
V  8  14  ALA 14  15  15  ALA ALA V . n 
V  8  15  ALA 15  16  16  ALA ALA V . n 
V  8  16  ASP 16  17  17  ASP ASP V . n 
V  8  17  THR 17  18  18  THR THR V . n 
V  8  18  ARG 18  19  19  ARG ARG V . n 
V  8  19  SER 19  20  20  SER SER V . n 
V  8  20  THR 20  21  21  THR THR V . n 
V  8  21  GLN 21  22  22  GLN GLN V . n 
V  8  22  GLY 22  23  23  GLY GLY V . n 
V  8  23  PRO 23  24  24  PRO PRO V . n 
V  8  24  ILE 24  25  25  ILE ILE V . n 
V  8  25  VAL 25  26  26  VAL VAL V . n 
V  8  26  ALA 26  27  27  ALA ALA V . n 
V  8  27  ASP 27  28  28  ASP ASP V . n 
V  8  28  LYS 28  29  29  LYS LYS V . n 
V  8  29  ASN 29  30  30  ASN ASN V . n 
V  8  30  CYS 30  31  31  CYS CYS V . n 
V  8  31  ALA 31  32  32  ALA ALA V . n 
V  8  32  LYS 32  33  33  LYS LYS V . n 
V  8  33  LEU 33  34  34  LEU LEU V . n 
V  8  34  HIS 34  35  35  HIS HIS V . n 
V  8  35  ARG 35  36  36  ARG ARG V . n 
V  8  36  ILE 36  37  37  ILE ILE V . n 
V  8  37  SER 37  38  38  SER SER V . n 
V  8  38  PRO 38  39  39  PRO PRO V . n 
V  8  39  LYS 39  40  40  LYS LYS V . n 
V  8  40  ILE 40  41  41  ILE ILE V . n 
V  8  41  TRP 41  42  42  TRP TRP V . n 
V  8  42  CYS 42  43  43  CYS CYS V . n 
V  8  43  ALA 43  44  44  ALA ALA V . n 
V  8  44  GLY 44  45  45  GLY GLY V . n 
V  8  45  ALA 45  46  46  ALA ALA V . n 
V  8  46  GLY 46  47  47  GLY GLY V . n 
V  8  47  THR 47  48  48  THR THR V . n 
V  8  48  ALA 48  49  49  ALA ALA V . n 
V  8  49  ALA 49  50  50  ALA ALA V . n 
V  8  50  ASP 50  51  51  ASP ASP V . n 
V  8  51  THR 51  52  52  THR THR V . n 
V  8  52  GLU 52  53  53  GLU GLU V . n 
V  8  53  ALA 53  54  54  ALA ALA V . n 
V  8  54  VAL 54  55  55  VAL VAL V . n 
V  8  55  THR 55  56  56  THR THR V . n 
V  8  56  GLN 56  57  57  GLN GLN V . n 
V  8  57  LEU 57  58  58  LEU LEU V . n 
V  8  58  ILE 58  59  59  ILE ILE V . n 
V  8  59  GLY 59  60  60  GLY GLY V . n 
V  8  60  SER 60  61  61  SER SER V . n 
V  8  61  ASN 61  62  62  ASN ASN V . n 
V  8  62  ILE 62  63  63  ILE ILE V . n 
V  8  63  GLU 63  64  64  GLU GLU V . n 
V  8  64  LEU 64  65  65  LEU LEU V . n 
V  8  65  HIS 65  66  66  HIS HIS V . n 
V  8  66  SER 66  67  67  SER SER V . n 
V  8  67  LEU 67  68  68  LEU LEU V . n 
V  8  68  TYR 68  69  69  TYR TYR V . n 
V  8  69  THR 69  70  70  THR THR V . n 
V  8  70  SER 70  71  71  SER SER V . n 
V  8  71  ARG 71  72  72  ARG ARG V . n 
V  8  72  GLU 72  73  73  GLU GLU V . n 
V  8  73  PRO 73  74  74  PRO PRO V . n 
V  8  74  ARG 74  75  75  ARG ARG V . n 
V  8  75  VAL 75  76  76  VAL VAL V . n 
V  8  76  VAL 76  77  77  VAL VAL V . n 
V  8  77  SER 77  78  78  SER SER V . n 
V  8  78  ALA 78  79  79  ALA ALA V . n 
V  8  79  LEU 79  80  80  LEU LEU V . n 
V  8  80  GLN 80  81  81  GLN GLN V . n 
V  8  81  MET 81  82  82  MET MET V . n 
V  8  82  LEU 82  83  83  LEU LEU V . n 
V  8  83  LYS 83  84  84  LYS LYS V . n 
V  8  84  GLN 84  85  85  GLN GLN V . n 
V  8  85  HIS 85  86  86  HIS HIS V . n 
V  8  86  LEU 86  87  87  LEU LEU V . n 
V  8  87  PHE 87  88  88  PHE PHE V . n 
V  8  88  LYS 88  89  89  LYS LYS V . n 
V  8  89  TYR 89  90  90  TYR TYR V . n 
V  8  90  GLN 90  91  91  GLN GLN V . n 
V  8  91  GLY 91  92  92  GLY GLY V . n 
V  8  92  HIS 92  93  93  HIS HIS V . n 
V  8  93  ILE 93  94  94  ILE ILE V . n 
V  8  94  GLY 94  95  95  GLY GLY V . n 
V  8  95  ALA 95  96  96  ALA ALA V . n 
V  8  96  TYR 96  97  97  TYR TYR V . n 
V  8  97  LEU 97  98  98  LEU LEU V . n 
V  8  98  ILE 98  99  99  ILE ILE V . n 
V  8  99  VAL 99  100 100 VAL VAL V . n 
V  8  100 ALA 100 101 101 ALA ALA V . n 
V  8  101 GLY 101 102 102 GLY GLY V . n 
V  8  102 VAL 102 103 103 VAL VAL V . n 
V  8  103 ASP 103 104 104 ASP ASP V . n 
V  8  104 PRO 104 105 105 PRO PRO V . n 
V  8  105 THR 105 106 106 THR THR V . n 
V  8  106 GLY 106 107 107 GLY GLY V . n 
V  8  107 SER 107 108 108 SER SER V . n 
V  8  108 HIS 108 109 109 HIS HIS V . n 
V  8  109 LEU 109 110 110 LEU LEU V . n 
V  8  110 PHE 110 111 111 PHE PHE V . n 
V  8  111 SER 111 112 112 SER SER V . n 
V  8  112 ILE 112 113 113 ILE ILE V . n 
V  8  113 HIS 113 114 114 HIS HIS V . n 
V  8  114 ALA 114 115 115 ALA ALA V . n 
V  8  115 HIS 115 116 116 HIS HIS V . n 
V  8  116 GLY 116 117 117 GLY GLY V . n 
V  8  117 SER 117 118 118 SER SER V . n 
V  8  118 THR 118 119 119 THR THR V . n 
V  8  119 ASP 119 120 120 ASP ASP V . n 
V  8  120 VAL 120 121 121 VAL VAL V . n 
V  8  121 GLY 121 122 122 GLY GLY V . n 
V  8  122 TYR 122 123 123 TYR TYR V . n 
V  8  123 TYR 123 124 124 TYR TYR V . n 
V  8  124 LEU 124 125 125 LEU LEU V . n 
V  8  125 SER 125 126 126 SER SER V . n 
V  8  126 LEU 126 127 127 LEU LEU V . n 
V  8  127 GLY 127 128 128 GLY GLY V . n 
V  8  128 SER 128 129 129 SER SER V . n 
V  8  129 GLY 129 130 130 GLY GLY V . n 
V  8  130 SER 130 131 131 SER SER V . n 
V  8  131 LEU 131 132 132 LEU LEU V . n 
V  8  132 ALA 132 133 133 ALA ALA V . n 
V  8  133 ALA 133 134 134 ALA ALA V . n 
V  8  134 MET 134 135 135 MET MET V . n 
V  8  135 ALA 135 136 136 ALA ALA V . n 
V  8  136 VAL 136 137 137 VAL VAL V . n 
V  8  137 LEU 137 138 138 LEU LEU V . n 
V  8  138 GLU 138 139 139 GLU GLU V . n 
V  8  139 SER 139 140 140 SER SER V . n 
V  8  140 HIS 140 141 141 HIS HIS V . n 
V  8  141 TRP 141 142 142 TRP TRP V . n 
V  8  142 LYS 142 143 143 LYS LYS V . n 
V  8  143 GLN 143 144 144 GLN GLN V . n 
V  8  144 ASP 144 145 145 ASP ASP V . n 
V  8  145 LEU 145 146 146 LEU LEU V . n 
V  8  146 THR 146 147 147 THR THR V . n 
V  8  147 LYS 147 148 148 LYS LYS V . n 
V  8  148 GLU 148 149 149 GLU GLU V . n 
V  8  149 GLU 149 150 150 GLU GLU V . n 
V  8  150 ALA 150 151 151 ALA ALA V . n 
V  8  151 ILE 151 152 152 ILE ILE V . n 
V  8  152 LYS 152 153 153 LYS LYS V . n 
V  8  153 LEU 153 154 154 LEU LEU V . n 
V  8  154 ALA 154 155 155 ALA ALA V . n 
V  8  155 SER 155 156 156 SER SER V . n 
V  8  156 ASP 156 157 157 ASP ASP V . n 
V  8  157 ALA 157 158 158 ALA ALA V . n 
V  8  158 ILE 158 159 159 ILE ILE V . n 
V  8  159 GLN 159 160 160 GLN GLN V . n 
V  8  160 ALA 160 161 161 ALA ALA V . n 
V  8  161 GLY 161 162 162 GLY GLY V . n 
V  8  162 ILE 162 163 163 ILE ILE V . n 
V  8  163 TRP 163 164 164 TRP TRP V . n 
V  8  164 ASN 164 165 165 ASN ASN V . n 
V  8  165 ASP 165 166 166 ASP ASP V . n 
V  8  166 LEU 166 167 167 LEU LEU V . n 
V  8  167 GLY 167 168 168 GLY GLY V . n 
V  8  168 SER 168 169 169 SER SER V . n 
V  8  169 GLY 169 170 170 GLY GLY V . n 
V  8  170 SER 170 171 171 SER SER V . n 
V  8  171 ASN 171 172 172 ASN ASN V . n 
V  8  172 VAL 172 173 173 VAL VAL V . n 
V  8  173 ASP 173 174 174 ASP ASP V . n 
V  8  174 VAL 174 175 175 VAL VAL V . n 
V  8  175 CYS 175 176 176 CYS CYS V . n 
V  8  176 VAL 176 177 177 VAL VAL V . n 
V  8  177 MET 177 178 178 MET MET V . n 
V  8  178 GLU 178 179 179 GLU GLU V . n 
V  8  179 ILE 179 180 180 ILE ILE V . n 
V  8  180 GLY 180 181 181 GLY GLY V . n 
V  8  181 LYS 181 182 182 LYS LYS V . n 
V  8  182 ASP 182 183 183 ASP ASP V . n 
V  8  183 ALA 183 184 184 ALA ALA V . n 
V  8  184 GLU 184 185 185 GLU GLU V . n 
V  8  185 TYR 185 186 186 TYR TYR V . n 
V  8  186 LEU 186 187 187 LEU LEU V . n 
V  8  187 ARG 187 188 188 ARG ARG V . n 
V  8  188 ASN 188 189 189 ASN ASN V . n 
V  8  189 TYR 189 190 190 TYR TYR V . n 
V  8  190 LEU 190 191 191 LEU LEU V . n 
V  8  191 THR 191 192 192 THR THR V . n 
V  8  192 PRO 192 193 193 PRO PRO V . n 
V  8  193 ASN 193 194 194 ASN ASN V . n 
V  8  194 VAL 194 195 195 VAL VAL V . n 
V  8  195 ARG 195 196 196 ARG ARG V . n 
V  8  196 GLU 196 197 197 GLU GLU V . n 
V  8  197 GLU 197 198 198 GLU GLU V . n 
V  8  198 LYS 198 199 199 LYS LYS V . n 
V  8  199 GLN 199 200 200 GLN GLN V . n 
V  8  200 LYS 200 201 201 LYS LYS V . n 
V  8  201 SER 201 202 202 SER SER V . n 
V  8  202 TYR 202 203 203 TYR TYR V . n 
V  8  203 LYS 203 204 204 LYS LYS V . n 
V  8  204 PHE 204 205 205 PHE PHE V . n 
V  8  205 PRO 205 206 206 PRO PRO V . n 
V  8  206 ARG 206 207 207 ARG ARG V . n 
V  8  207 GLY 207 208 208 GLY GLY V . n 
V  8  208 THR 208 209 209 THR THR V . n 
V  8  209 THR 209 210 210 THR THR V . n 
V  8  210 ALA 210 211 211 ALA ALA V . n 
V  8  211 VAL 211 212 212 VAL VAL V . n 
V  8  212 LEU 212 213 213 LEU LEU V . n 
V  8  213 LYS 213 214 214 LYS LYS V . n 
V  8  214 GLU 214 215 215 GLU GLU V . n 
V  8  215 SER 215 216 216 SER SER V . n 
V  8  216 ILE 216 217 217 ILE ILE V . n 
V  8  217 VAL 217 218 218 VAL VAL V . n 
V  8  218 ASN 218 219 219 ASN ASN V . n 
V  8  219 ILE 219 220 220 ILE ILE V . n 
V  8  220 CYS 220 221 221 CYS CYS V . n 
V  8  221 ASP 221 222 222 ASP ASP V . n 
V  8  222 ILE 222 223 ?   ?   ?   V . n 
V  8  223 GLN 223 224 ?   ?   ?   V . n 
V  8  224 GLU 224 225 ?   ?   ?   V . n 
V  8  225 GLU 225 226 ?   ?   ?   V . n 
V  8  226 GLN 226 227 ?   ?   ?   V . n 
V  8  227 VAL 227 228 ?   ?   ?   V . n 
V  8  228 ASP 228 229 ?   ?   ?   V . n 
V  8  229 ILE 229 230 ?   ?   ?   V . n 
V  8  230 THR 230 231 ?   ?   ?   V . n 
V  8  231 ALA 231 232 ?   ?   ?   V . n 
W  9  1   MET 1   0   ?   ?   ?   W . n 
W  9  2   SER 2   1   1   SER SER W . n 
W  9  3   ASP 3   2   2   ASP ASP W . n 
W  9  4   PRO 4   3   3   PRO PRO W . n 
W  9  5   SER 5   4   4   SER SER W . n 
W  9  6   SER 6   5   5   SER SER W . n 
W  9  7   ILE 7   6   6   ILE ILE W . n 
W  9  8   ASN 8   7   7   ASN ASN W . n 
W  9  9   GLY 9   8   8   GLY GLY W . n 
W  9  10  GLY 10  9   9   GLY GLY W . n 
W  9  11  ILE 11  10  10  ILE ILE W . n 
W  9  12  VAL 12  11  11  VAL VAL W . n 
W  9  13  VAL 13  12  12  VAL VAL W . n 
W  9  14  ALA 14  13  13  ALA ALA W . n 
W  9  15  MET 15  14  14  MET MET W . n 
W  9  16  THR 16  15  15  THR THR W . n 
W  9  17  GLY 17  16  16  GLY GLY W . n 
W  9  18  LYS 18  17  17  LYS LYS W . n 
W  9  19  ASP 19  18  18  ASP ASP W . n 
W  9  20  CYS 20  19  19  CYS CYS W . n 
W  9  21  VAL 21  20  20  VAL VAL W . n 
W  9  22  ALA 22  21  21  ALA ALA W . n 
W  9  23  ILE 23  22  22  ILE ILE W . n 
W  9  24  ALA 24  23  23  ALA ALA W . n 
W  9  25  CYS 25  24  24  CYS CYS W . n 
W  9  26  ASP 26  25  25  ASP ASP W . n 
W  9  27  LEU 27  26  26  LEU LEU W . n 
W  9  28  ARG 28  27  27  ARG ARG W . n 
W  9  29  LEU 29  28  28  LEU LEU W . n 
W  9  30  GLY 30  29  29  GLY GLY W . n 
W  9  31  SER 31  30  30  SER SER W . n 
W  9  32  GLN 32  31  31  GLN GLN W . n 
W  9  33  SER 33  32  32  SER SER W . n 
W  9  34  LEU 34  33  33  LEU LEU W . n 
W  9  35  GLY 35  34  34  GLY GLY W . n 
W  9  36  VAL 36  35  35  VAL VAL W . n 
W  9  37  SER 37  36  36  SER SER W . n 
W  9  38  ASN 38  37  37  ASN ASN W . n 
W  9  39  LYS 39  38  38  LYS LYS W . n 
W  9  40  PHE 40  39  39  PHE PHE W . n 
W  9  41  GLU 41  40  40  GLU GLU W . n 
W  9  42  LYS 42  41  41  LYS LYS W . n 
W  9  43  ILE 43  42  42  ILE ILE W . n 
W  9  44  PHE 44  43  43  PHE PHE W . n 
W  9  45  HIS 45  44  44  HIS HIS W . n 
W  9  46  TYR 46  45  45  TYR TYR W . n 
W  9  47  GLY 47  46  46  GLY GLY W . n 
W  9  48  HIS 48  47  47  HIS HIS W . n 
W  9  49  VAL 49  48  48  VAL VAL W . n 
W  9  50  PHE 50  49  49  PHE PHE W . n 
W  9  51  LEU 51  50  50  LEU LEU W . n 
W  9  52  GLY 52  51  51  GLY GLY W . n 
W  9  53  ILE 53  52  52  ILE ILE W . n 
W  9  54  THR 54  53  53  THR THR W . n 
W  9  55  GLY 55  54  54  GLY GLY W . n 
W  9  56  LEU 56  55  55  LEU LEU W . n 
W  9  57  ALA 57  56  56  ALA ALA W . n 
W  9  58  THR 58  57  57  THR THR W . n 
W  9  59  ASP 59  58  58  ASP ASP W . n 
W  9  60  VAL 60  59  59  VAL VAL W . n 
W  9  61  THR 61  60  60  THR THR W . n 
W  9  62  THR 62  61  61  THR THR W . n 
W  9  63  LEU 63  62  62  LEU LEU W . n 
W  9  64  ASN 64  63  63  ASN ASN W . n 
W  9  65  GLU 65  64  64  GLU GLU W . n 
W  9  66  MET 66  65  65  MET MET W . n 
W  9  67  PHE 67  66  66  PHE PHE W . n 
W  9  68  ARG 68  67  67  ARG ARG W . n 
W  9  69  TYR 69  68  68  TYR TYR W . n 
W  9  70  LYS 70  69  69  LYS LYS W . n 
W  9  71  THR 71  70  70  THR THR W . n 
W  9  72  ASN 72  71  71  ASN ASN W . n 
W  9  73  LEU 73  72  72  LEU LEU W . n 
W  9  74  TYR 74  73  73  TYR TYR W . n 
W  9  75  LYS 75  74  74  LYS LYS W . n 
W  9  76  LEU 76  75  75  LEU LEU W . n 
W  9  77  LYS 77  76  76  LYS LYS W . n 
W  9  78  GLU 78  77  77  GLU GLU W . n 
W  9  79  GLU 79  78  78  GLU GLU W . n 
W  9  80  ARG 80  79  79  ARG ARG W . n 
W  9  81  ALA 81  80  80  ALA ALA W . n 
W  9  82  ILE 82  81  81  ILE ILE W . n 
W  9  83  GLU 83  82  82  GLU GLU W . n 
W  9  84  PRO 84  83  83  PRO PRO W . n 
W  9  85  GLU 85  84  84  GLU GLU W . n 
W  9  86  THR 86  85  85  THR THR W . n 
W  9  87  PHE 87  86  86  PHE PHE W . n 
W  9  88  THR 88  87  87  THR THR W . n 
W  9  89  GLN 89  88  88  GLN GLN W . n 
W  9  90  LEU 90  89  89  LEU LEU W . n 
W  9  91  VAL 91  90  90  VAL VAL W . n 
W  9  92  SER 92  91  91  SER SER W . n 
W  9  93  SER 93  92  92  SER SER W . n 
W  9  94  SER 94  93  93  SER SER W . n 
W  9  95  LEU 95  94  94  LEU LEU W . n 
W  9  96  TYR 96  95  95  TYR TYR W . n 
W  9  97  GLU 97  96  96  GLU GLU W . n 
W  9  98  ARG 98  97  97  ARG ARG W . n 
W  9  99  ARG 99  98  98  ARG ARG W . n 
W  9  100 PHE 100 99  99  PHE PHE W . n 
W  9  101 GLY 101 100 100 GLY GLY W . n 
W  9  102 PRO 102 101 101 PRO PRO W . n 
W  9  103 TYR 103 102 102 TYR TYR W . n 
W  9  104 PHE 104 103 103 PHE PHE W . n 
W  9  105 VAL 105 104 104 VAL VAL W . n 
W  9  106 GLY 106 105 105 GLY GLY W . n 
W  9  107 PRO 107 106 106 PRO PRO W . n 
W  9  108 VAL 108 107 107 VAL VAL W . n 
W  9  109 VAL 109 108 108 VAL VAL W . n 
W  9  110 ALA 110 109 109 ALA ALA W . n 
W  9  111 GLY 111 110 110 GLY GLY W . n 
W  9  112 ILE 112 111 111 ILE ILE W . n 
W  9  113 ASN 113 112 112 ASN ASN W . n 
W  9  114 SER 114 113 113 SER SER W . n 
W  9  115 LYS 115 114 114 LYS LYS W . n 
W  9  116 SER 116 115 115 SER SER W . n 
W  9  117 GLY 117 116 116 GLY GLY W . n 
W  9  118 LYS 118 117 117 LYS LYS W . n 
W  9  119 PRO 119 118 118 PRO PRO W . n 
W  9  120 PHE 120 119 119 PHE PHE W . n 
W  9  121 ILE 121 120 120 ILE ILE W . n 
W  9  122 ALA 122 121 121 ALA ALA W . n 
W  9  123 GLY 123 122 122 GLY GLY W . n 
W  9  124 PHE 124 123 123 PHE PHE W . n 
W  9  125 ASP 125 124 124 ASP ASP W . n 
W  9  126 LEU 126 125 125 LEU LEU W . n 
W  9  127 ILE 127 126 126 ILE ILE W . n 
W  9  128 GLY 128 127 127 GLY GLY W . n 
W  9  129 CYS 129 128 128 CYS CYS W . n 
W  9  130 ILE 130 129 129 ILE ILE W . n 
W  9  131 ASP 131 130 130 ASP ASP W . n 
W  9  132 GLU 132 131 131 GLU GLU W . n 
W  9  133 ALA 133 132 132 ALA ALA W . n 
W  9  134 LYS 134 133 133 LYS LYS W . n 
W  9  135 ASP 135 134 134 ASP ASP W . n 
W  9  136 PHE 136 135 135 PHE PHE W . n 
W  9  137 ILE 137 136 136 ILE ILE W . n 
W  9  138 VAL 138 137 137 VAL VAL W . n 
W  9  139 SER 139 138 138 SER SER W . n 
W  9  140 GLY 140 139 139 GLY GLY W . n 
W  9  141 THR 141 140 140 THR THR W . n 
W  9  142 ALA 142 141 141 ALA ALA W . n 
W  9  143 SER 143 142 142 SER SER W . n 
W  9  144 ASP 144 143 143 ASP ASP W . n 
W  9  145 GLN 145 144 144 GLN GLN W . n 
W  9  146 LEU 146 145 145 LEU LEU W . n 
W  9  147 PHE 147 146 146 PHE PHE W . n 
W  9  148 GLY 148 147 147 GLY GLY W . n 
W  9  149 MET 149 148 148 MET MET W . n 
W  9  150 CYS 150 149 149 CYS CYS W . n 
W  9  151 GLU 151 150 150 GLU GLU W . n 
W  9  152 SER 152 151 151 SER SER W . n 
W  9  153 LEU 153 152 152 LEU LEU W . n 
W  9  154 TYR 154 153 153 TYR TYR W . n 
W  9  155 GLU 155 154 154 GLU GLU W . n 
W  9  156 PRO 156 155 155 PRO PRO W . n 
W  9  157 ASN 157 156 156 ASN ASN W . n 
W  9  158 LEU 158 157 157 LEU LEU W . n 
W  9  159 GLU 159 158 158 GLU GLU W . n 
W  9  160 PRO 160 159 159 PRO PRO W . n 
W  9  161 GLU 161 160 160 GLU GLU W . n 
W  9  162 ASP 162 161 161 ASP ASP W . n 
W  9  163 LEU 163 162 162 LEU LEU W . n 
W  9  164 PHE 164 163 163 PHE PHE W . n 
W  9  165 GLU 165 164 164 GLU GLU W . n 
W  9  166 THR 166 165 165 THR THR W . n 
W  9  167 ILE 167 166 166 ILE ILE W . n 
W  9  168 SER 168 167 167 SER SER W . n 
W  9  169 GLN 169 168 168 GLN GLN W . n 
W  9  170 ALA 170 169 169 ALA ALA W . n 
W  9  171 LEU 171 170 170 LEU LEU W . n 
W  9  172 LEU 172 171 171 LEU LEU W . n 
W  9  173 ASN 173 172 172 ASN ASN W . n 
W  9  174 ALA 174 173 173 ALA ALA W . n 
W  9  175 ALA 175 174 174 ALA ALA W . n 
W  9  176 ASP 176 175 175 ASP ASP W . n 
W  9  177 ARG 177 176 176 ARG ARG W . n 
W  9  178 ASP 178 177 177 ASP ASP W . n 
W  9  179 ALA 179 178 178 ALA ALA W . n 
W  9  180 LEU 180 179 179 LEU LEU W . n 
W  9  181 SER 181 180 180 SER SER W . n 
W  9  182 GLY 182 181 181 GLY GLY W . n 
W  9  183 TRP 183 182 182 TRP TRP W . n 
W  9  184 GLY 184 183 183 GLY GLY W . n 
W  9  185 ALA 185 184 184 ALA ALA W . n 
W  9  186 VAL 186 185 185 VAL VAL W . n 
W  9  187 VAL 187 186 186 VAL VAL W . n 
W  9  188 TYR 188 187 187 TYR TYR W . n 
W  9  189 ILE 189 188 188 ILE ILE W . n 
W  9  190 ILE 190 189 189 ILE ILE W . n 
W  9  191 LYS 191 190 190 LYS LYS W . n 
W  9  192 LYS 192 191 191 LYS LYS W . n 
W  9  193 ASP 193 192 192 ASP ASP W . n 
W  9  194 GLU 194 193 193 GLU GLU W . n 
W  9  195 VAL 195 194 194 VAL VAL W . n 
W  9  196 VAL 196 195 195 VAL VAL W . n 
W  9  197 LYS 197 196 196 LYS LYS W . n 
W  9  198 ARG 198 197 197 ARG ARG W . n 
W  9  199 TYR 199 198 198 TYR TYR W . n 
W  9  200 LEU 200 199 199 LEU LEU W . n 
W  9  201 LYS 201 200 200 LYS LYS W . n 
W  9  202 MET 202 201 201 MET MET W . n 
W  9  203 ARG 203 202 202 ARG ARG W . n 
W  9  204 GLN 204 203 203 GLN GLN W . n 
W  9  205 ASP 205 204 204 ASP ASP W . n 
X  10 1   MET 1   1   1   MET MET X . n 
X  10 2   ASP 2   2   2   ASP ASP X . n 
X  10 3   ILE 3   3   3   ILE ILE X . n 
X  10 4   ILE 4   4   4   ILE ILE X . n 
X  10 5   LEU 5   5   5   LEU LEU X . n 
X  10 6   GLY 6   6   6   GLY GLY X . n 
X  10 7   ILE 7   7   7   ILE ILE X . n 
X  10 8   ARG 8   8   8   ARG ARG X . n 
X  10 9   VAL 9   9   9   VAL VAL X . n 
X  10 10  GLN 10  10  10  GLN GLN X . n 
X  10 11  ASP 11  11  11  ASP ASP X . n 
X  10 12  SER 12  12  12  SER SER X . n 
X  10 13  VAL 13  13  13  VAL VAL X . n 
X  10 14  ILE 14  14  14  ILE ILE X . n 
X  10 15  LEU 15  15  15  LEU LEU X . n 
X  10 16  ALA 16  16  16  ALA ALA X . n 
X  10 17  SER 17  17  17  SER SER X . n 
X  10 18  SER 18  18  18  SER SER X . n 
X  10 19  LYS 19  19  19  LYS LYS X . n 
X  10 20  ALA 20  20  20  ALA ALA X . n 
X  10 21  VAL 21  21  21  VAL VAL X . n 
X  10 22  THR 22  22  22  THR THR X . n 
X  10 23  ARG 23  23  23  ARG ARG X . n 
X  10 24  GLY 24  24  24  GLY GLY X . n 
X  10 25  ILE 25  25  25  ILE ILE X . n 
X  10 26  SER 26  26  26  SER SER X . n 
X  10 27  VAL 27  27  27  VAL VAL X . n 
X  10 28  LEU 28  28  28  LEU LEU X . n 
X  10 29  LYS 29  29  29  LYS LYS X . n 
X  10 30  ASP 30  30  30  ASP ASP X . n 
X  10 31  SER 31  31  31  SER SER X . n 
X  10 32  ASP 32  32  32  ASP ASP X . n 
X  10 33  ASP 33  33  33  ASP ASP X . n 
X  10 34  LYS 34  34  34  LYS LYS X . n 
X  10 35  THR 35  35  35  THR THR X . n 
X  10 36  ARG 36  36  36  ARG ARG X . n 
X  10 37  GLN 37  37  37  GLN GLN X . n 
X  10 38  LEU 38  38  38  LEU LEU X . n 
X  10 39  SER 39  39  39  SER SER X . n 
X  10 40  PRO 40  40  40  PRO PRO X . n 
X  10 41  HIS 41  41  41  HIS HIS X . n 
X  10 42  THR 42  42  42  THR THR X . n 
X  10 43  LEU 43  43  43  LEU LEU X . n 
X  10 44  MET 44  44  44  MET MET X . n 
X  10 45  SER 45  45  45  SER SER X . n 
X  10 46  PHE 46  46  46  PHE PHE X . n 
X  10 47  ALA 47  47  47  ALA ALA X . n 
X  10 48  GLY 48  48  48  GLY GLY X . n 
X  10 49  GLU 49  49  49  GLU GLU X . n 
X  10 50  ALA 50  50  50  ALA ALA X . n 
X  10 51  GLY 51  51  51  GLY GLY X . n 
X  10 52  ASP 52  52  52  ASP ASP X . n 
X  10 53  THR 53  53  53  THR THR X . n 
X  10 54  VAL 54  54  54  VAL VAL X . n 
X  10 55  GLN 55  55  55  GLN GLN X . n 
X  10 56  PHE 56  56  56  PHE PHE X . n 
X  10 57  ALA 57  57  57  ALA ALA X . n 
X  10 58  GLU 58  58  58  GLU GLU X . n 
X  10 59  TYR 59  59  59  TYR TYR X . n 
X  10 60  ILE 60  60  60  ILE ILE X . n 
X  10 61  GLN 61  61  61  GLN GLN X . n 
X  10 62  ALA 62  62  62  ALA ALA X . n 
X  10 63  ASN 63  63  63  ASN ASN X . n 
X  10 64  ILE 64  64  64  ILE ILE X . n 
X  10 65  GLN 65  65  65  GLN GLN X . n 
X  10 66  LEU 66  66  66  LEU LEU X . n 
X  10 67  TYR 67  67  67  TYR TYR X . n 
X  10 68  SER 68  68  68  SER SER X . n 
X  10 69  ILE 69  69  69  ILE ILE X . n 
X  10 70  ARG 70  70  70  ARG ARG X . n 
X  10 71  GLU 71  71  71  GLU GLU X . n 
X  10 72  ASP 72  72  72  ASP ASP X . n 
X  10 73  TYR 73  73  73  TYR TYR X . n 
X  10 74  GLU 74  74  74  GLU GLU X . n 
X  10 75  LEU 75  75  75  LEU LEU X . n 
X  10 76  SER 76  76  76  SER SER X . n 
X  10 77  PRO 77  77  77  PRO PRO X . n 
X  10 78  GLN 78  78  78  GLN GLN X . n 
X  10 79  ALA 79  79  79  ALA ALA X . n 
X  10 80  VAL 80  80  80  VAL VAL X . n 
X  10 81  SER 81  81  81  SER SER X . n 
X  10 82  SER 82  82  82  SER SER X . n 
X  10 83  PHE 83  83  83  PHE PHE X . n 
X  10 84  VAL 84  84  84  VAL VAL X . n 
X  10 85  ARG 85  85  85  ARG ARG X . n 
X  10 86  GLN 86  86  86  GLN GLN X . n 
X  10 87  GLU 87  87  87  GLU GLU X . n 
X  10 88  LEU 88  88  88  LEU LEU X . n 
X  10 89  ALA 89  89  89  ALA ALA X . n 
X  10 90  LYS 90  90  90  LYS LYS X . n 
X  10 91  SER 91  91  91  SER SER X . n 
X  10 92  ILE 92  92  92  ILE ILE X . n 
X  10 93  ARG 93  93  93  ARG ARG X . n 
X  10 94  SER 94  94  94  SER SER X . n 
X  10 95  ARG 95  95  95  ARG ARG X . n 
X  10 96  ARG 96  96  96  ARG ARG X . n 
X  10 97  PRO 97  97  97  PRO PRO X . n 
X  10 98  TYR 98  98  98  TYR TYR X . n 
X  10 99  GLN 99  99  99  GLN GLN X . n 
X  10 100 VAL 100 100 100 VAL VAL X . n 
X  10 101 ASN 101 101 101 ASN ASN X . n 
X  10 102 VAL 102 102 102 VAL VAL X . n 
X  10 103 LEU 103 103 103 LEU LEU X . n 
X  10 104 ILE 104 104 104 ILE ILE X . n 
X  10 105 GLY 105 105 105 GLY GLY X . n 
X  10 106 GLY 106 106 106 GLY GLY X . n 
X  10 107 TYR 107 107 107 TYR TYR X . n 
X  10 108 ASP 108 108 108 ASP ASP X . n 
X  10 109 LYS 109 109 109 LYS LYS X . n 
X  10 110 LYS 110 110 110 LYS LYS X . n 
X  10 111 LYS 111 111 111 LYS LYS X . n 
X  10 112 ASN 112 112 112 ASN ASN X . n 
X  10 113 LYS 113 113 113 LYS LYS X . n 
X  10 114 PRO 114 114 114 PRO PRO X . n 
X  10 115 GLU 115 115 115 GLU GLU X . n 
X  10 116 LEU 116 116 116 LEU LEU X . n 
X  10 117 TYR 117 117 117 TYR TYR X . n 
X  10 118 GLN 118 118 118 GLN GLN X . n 
X  10 119 ILE 119 119 119 ILE ILE X . n 
X  10 120 ASP 120 120 120 ASP ASP X . n 
X  10 121 TYR 121 121 121 TYR TYR X . n 
X  10 122 LEU 122 122 122 LEU LEU X . n 
X  10 123 GLY 123 123 123 GLY GLY X . n 
X  10 124 THR 124 124 124 THR THR X . n 
X  10 125 LYS 125 125 125 LYS LYS X . n 
X  10 126 VAL 126 126 126 VAL VAL X . n 
X  10 127 GLU 127 127 127 GLU GLU X . n 
X  10 128 LEU 128 128 128 LEU LEU X . n 
X  10 129 PRO 129 129 129 PRO PRO X . n 
X  10 130 TYR 130 130 130 TYR TYR X . n 
X  10 131 GLY 131 131 131 GLY GLY X . n 
X  10 132 ALA 132 132 132 ALA ALA X . n 
X  10 133 HIS 133 133 133 HIS HIS X . n 
X  10 134 GLY 134 134 134 GLY GLY X . n 
X  10 135 TYR 135 135 135 TYR TYR X . n 
X  10 136 SER 136 136 136 SER SER X . n 
X  10 137 GLY 137 137 137 GLY GLY X . n 
X  10 138 PHE 138 138 138 PHE PHE X . n 
X  10 139 TYR 139 139 139 TYR TYR X . n 
X  10 140 THR 140 140 140 THR THR X . n 
X  10 141 PHE 141 141 141 PHE PHE X . n 
X  10 142 SER 142 142 142 SER SER X . n 
X  10 143 LEU 143 143 143 LEU LEU X . n 
X  10 144 LEU 144 144 144 LEU LEU X . n 
X  10 145 ASP 145 145 145 ASP ASP X . n 
X  10 146 HIS 146 146 146 HIS HIS X . n 
X  10 147 HIS 147 147 147 HIS HIS X . n 
X  10 148 TYR 148 148 148 TYR TYR X . n 
X  10 149 ARG 149 149 149 ARG ARG X . n 
X  10 150 PRO 150 150 150 PRO PRO X . n 
X  10 151 ASP 151 151 151 ASP ASP X . n 
X  10 152 MET 152 152 152 MET MET X . n 
X  10 153 THR 153 153 153 THR THR X . n 
X  10 154 THR 154 154 154 THR THR X . n 
X  10 155 GLU 155 155 155 GLU GLU X . n 
X  10 156 GLU 156 156 156 GLU GLU X . n 
X  10 157 GLY 157 157 157 GLY GLY X . n 
X  10 158 LEU 158 158 158 LEU LEU X . n 
X  10 159 ASP 159 159 159 ASP ASP X . n 
X  10 160 LEU 160 160 160 LEU LEU X . n 
X  10 161 LEU 161 161 161 LEU LEU X . n 
X  10 162 LYS 162 162 162 LYS LYS X . n 
X  10 163 LEU 163 163 163 LEU LEU X . n 
X  10 164 CYS 164 164 164 CYS CYS X . n 
X  10 165 VAL 165 165 165 VAL VAL X . n 
X  10 166 GLN 166 166 166 GLN GLN X . n 
X  10 167 GLU 167 167 167 GLU GLU X . n 
X  10 168 LEU 168 168 168 LEU LEU X . n 
X  10 169 GLU 169 169 169 GLU GLU X . n 
X  10 170 LYS 170 170 170 LYS LYS X . n 
X  10 171 ARG 171 171 171 ARG ARG X . n 
X  10 172 MET 172 172 172 MET MET X . n 
X  10 173 PRO 173 173 173 PRO PRO X . n 
X  10 174 MET 174 174 174 MET MET X . n 
X  10 175 ASP 175 175 175 ASP ASP X . n 
X  10 176 PHE 176 176 176 PHE PHE X . n 
X  10 177 LYS 177 177 177 LYS LYS X . n 
X  10 178 GLY 178 178 178 GLY GLY X . n 
X  10 179 VAL 179 179 179 VAL VAL X . n 
X  10 180 ILE 180 180 180 ILE ILE X . n 
X  10 181 VAL 181 181 181 VAL VAL X . n 
X  10 182 LYS 182 182 182 LYS LYS X . n 
X  10 183 ILE 183 183 183 ILE ILE X . n 
X  10 184 VAL 184 184 184 VAL VAL X . n 
X  10 185 ASP 185 185 185 ASP ASP X . n 
X  10 186 LYS 186 186 186 LYS LYS X . n 
X  10 187 ASP 187 187 187 ASP ASP X . n 
X  10 188 GLY 188 188 188 GLY GLY X . n 
X  10 189 ILE 189 189 189 ILE ILE X . n 
X  10 190 ARG 190 190 190 ARG ARG X . n 
X  10 191 GLN 191 191 191 GLN GLN X . n 
X  10 192 VAL 192 192 192 VAL VAL X . n 
X  10 193 ASP 193 193 193 ASP ASP X . n 
X  10 194 ASP 194 194 194 ASP ASP X . n 
X  10 195 PHE 195 195 195 PHE PHE X . n 
X  10 196 GLN 196 196 ?   ?   ?   X . n 
X  10 197 ALA 197 197 ?   ?   ?   X . n 
X  10 198 GLN 198 198 ?   ?   ?   X . n 
Y  11 1   THR 1   2   2   THR THR Y . n 
Y  11 2   THR 2   3   3   THR THR Y . n 
Y  11 3   LEU 3   4   4   LEU LEU Y . n 
Y  11 4   ALA 4   5   5   ALA ALA Y . n 
Y  11 5   PHE 5   6   6   PHE PHE Y . n 
Y  11 6   ARG 6   7   7   ARG ARG Y . n 
Y  11 7   PHE 7   8   8   PHE PHE Y . n 
Y  11 8   GLN 8   9   9   GLN GLN Y . n 
Y  11 9   GLY 9   10  10  GLY GLY Y . n 
Y  11 10  GLY 10  11  11  GLY GLY Y . n 
Y  11 11  ILE 11  12  12  ILE ILE Y . n 
Y  11 12  ILE 12  13  13  ILE ILE Y . n 
Y  11 13  VAL 13  14  14  VAL VAL Y . n 
Y  11 14  ALA 14  15  15  ALA ALA Y . n 
Y  11 15  VAL 15  16  16  VAL VAL Y . n 
Y  11 16  ASP 16  17  17  ASP ASP Y . n 
Y  11 17  SER 17  18  18  SER SER Y . n 
Y  11 18  ARG 18  19  19  ARG ARG Y . n 
Y  11 19  ALA 19  20  20  ALA ALA Y . n 
Y  11 20  THR 20  21  21  THR THR Y . n 
Y  11 21  ALA 21  22  22  ALA ALA Y . n 
Y  11 22  GLY 22  23  23  GLY GLY Y . n 
Y  11 23  ASN 23  24  24  ASN ASN Y . n 
Y  11 24  TRP 24  25  25  TRP TRP Y . n 
Y  11 25  VAL 25  26  26  VAL VAL Y . n 
Y  11 26  ALA 26  27  27  ALA ALA Y . n 
Y  11 27  SER 27  28  28  SER SER Y . n 
Y  11 28  GLN 28  29  29  GLN GLN Y . n 
Y  11 29  THR 29  30  30  THR THR Y . n 
Y  11 30  VAL 30  31  31  VAL VAL Y . n 
Y  11 31  LYS 31  32  32  LYS LYS Y . n 
Y  11 32  LYS 32  33  33  LYS LYS Y . n 
Y  11 33  VAL 33  34  34  VAL VAL Y . n 
Y  11 34  ILE 34  35  35  ILE ILE Y . n 
Y  11 35  GLU 35  36  36  GLU GLU Y . n 
Y  11 36  ILE 36  37  37  ILE ILE Y . n 
Y  11 37  ASN 37  38  38  ASN ASN Y . n 
Y  11 38  PRO 38  39  39  PRO PRO Y . n 
Y  11 39  PHE 39  40  40  PHE PHE Y . n 
Y  11 40  LEU 40  41  41  LEU LEU Y . n 
Y  11 41  LEU 41  42  42  LEU LEU Y . n 
Y  11 42  GLY 42  43  43  GLY GLY Y . n 
Y  11 43  THR 43  44  44  THR THR Y . n 
Y  11 44  MET 44  45  45  MET MET Y . n 
Y  11 45  ALA 45  46  46  ALA ALA Y . n 
Y  11 46  GLY 46  47  47  GLY GLY Y . n 
Y  11 47  GLY 47  48  48  GLY GLY Y . n 
Y  11 48  ALA 48  49  49  ALA ALA Y . n 
Y  11 49  ALA 49  50  50  ALA ALA Y . n 
Y  11 50  ASP 50  51  51  ASP ASP Y . n 
Y  11 51  CYS 51  52  52  CYS CYS Y . n 
Y  11 52  GLN 52  53  53  GLN GLN Y . n 
Y  11 53  PHE 53  54  54  PHE PHE Y . n 
Y  11 54  TRP 54  55  55  TRP TRP Y . n 
Y  11 55  GLU 55  56  56  GLU GLU Y . n 
Y  11 56  THR 56  57  57  THR THR Y . n 
Y  11 57  TRP 57  58  58  TRP TRP Y . n 
Y  11 58  LEU 58  59  59  LEU LEU Y . n 
Y  11 59  GLY 59  60  60  GLY GLY Y . n 
Y  11 60  SER 60  61  61  SER SER Y . n 
Y  11 61  GLN 61  62  62  GLN GLN Y . n 
Y  11 62  CYS 62  63  63  CYS CYS Y . n 
Y  11 63  ARG 63  64  64  ARG ARG Y . n 
Y  11 64  LEU 64  65  65  LEU LEU Y . n 
Y  11 65  HIS 65  66  66  HIS HIS Y . n 
Y  11 66  GLU 66  67  67  GLU GLU Y . n 
Y  11 67  LEU 67  68  68  LEU LEU Y . n 
Y  11 68  ARG 68  69  69  ARG ARG Y . n 
Y  11 69  GLU 69  70  70  GLU GLU Y . n 
Y  11 70  LYS 70  71  71  LYS LYS Y . n 
Y  11 71  GLU 71  72  72  GLU GLU Y . n 
Y  11 72  ARG 72  73  73  ARG ARG Y . n 
Y  11 73  ILE 73  74  74  ILE ILE Y . n 
Y  11 74  SER 74  75  75  SER SER Y . n 
Y  11 75  VAL 75  76  76  VAL VAL Y . n 
Y  11 76  ALA 76  77  77  ALA ALA Y . n 
Y  11 77  ALA 77  78  78  ALA ALA Y . n 
Y  11 78  ALA 78  79  79  ALA ALA Y . n 
Y  11 79  SER 79  80  80  SER SER Y . n 
Y  11 80  LYS 80  81  81  LYS LYS Y . n 
Y  11 81  ILE 81  82  82  ILE ILE Y . n 
Y  11 82  LEU 82  83  83  LEU LEU Y . n 
Y  11 83  SER 83  84  84  SER SER Y . n 
Y  11 84  ASN 84  85  85  ASN ASN Y . n 
Y  11 85  LEU 85  86  86  LEU LEU Y . n 
Y  11 86  VAL 86  87  87  VAL VAL Y . n 
Y  11 87  TYR 87  88  88  TYR TYR Y . n 
Y  11 88  GLN 88  89  89  GLN GLN Y . n 
Y  11 89  TYR 89  90  90  TYR TYR Y . n 
Y  11 90  LYS 90  91  91  LYS LYS Y . n 
Y  11 91  GLY 91  92  92  GLY GLY Y . n 
Y  11 92  ALA 92  93  93  ALA ALA Y . n 
Y  11 93  GLY 93  94  94  GLY GLY Y . n 
Y  11 94  LEU 94  95  95  LEU LEU Y . n 
Y  11 95  SER 95  96  96  SER SER Y . n 
Y  11 96  MET 96  97  97  MET MET Y . n 
Y  11 97  GLY 97  98  98  GLY GLY Y . n 
Y  11 98  THR 98  99  99  THR THR Y . n 
Y  11 99  MET 99  100 100 MET MET Y . n 
Y  11 100 ILE 100 101 101 ILE ILE Y . n 
Y  11 101 CYS 101 102 102 CYS CYS Y . n 
Y  11 102 GLY 102 103 103 GLY GLY Y . n 
Y  11 103 TYR 103 104 104 TYR TYR Y . n 
Y  11 104 THR 104 105 105 THR THR Y . n 
Y  11 105 ARG 105 106 106 ARG ARG Y . n 
Y  11 106 LYS 106 107 107 LYS LYS Y . n 
Y  11 107 GLU 107 108 108 GLU GLU Y . n 
Y  11 108 GLY 108 109 109 GLY GLY Y . n 
Y  11 109 PRO 109 110 110 PRO PRO Y . n 
Y  11 110 THR 110 111 111 THR THR Y . n 
Y  11 111 ILE 111 112 112 ILE ILE Y . n 
Y  11 112 TYR 112 113 113 TYR TYR Y . n 
Y  11 113 TYR 113 114 114 TYR TYR Y . n 
Y  11 114 VAL 114 115 115 VAL VAL Y . n 
Y  11 115 ASP 115 116 116 ASP ASP Y . n 
Y  11 116 SER 116 117 117 SER SER Y . n 
Y  11 117 ASP 117 118 118 ASP ASP Y . n 
Y  11 118 GLY 118 119 119 GLY GLY Y . n 
Y  11 119 THR 119 120 120 THR THR Y . n 
Y  11 120 ARG 120 121 121 ARG ARG Y . n 
Y  11 121 LEU 121 122 122 LEU LEU Y . n 
Y  11 122 LYS 122 123 123 LYS LYS Y . n 
Y  11 123 GLY 123 124 124 GLY GLY Y . n 
Y  11 124 ASP 124 125 125 ASP ASP Y . n 
Y  11 125 ILE 125 126 126 ILE ILE Y . n 
Y  11 126 PHE 126 127 127 PHE PHE Y . n 
Y  11 127 CYS 127 128 128 CYS CYS Y . n 
Y  11 128 VAL 128 129 129 VAL VAL Y . n 
Y  11 129 GLY 129 130 130 GLY GLY Y . n 
Y  11 130 SER 130 131 131 SER SER Y . n 
Y  11 131 GLY 131 132 132 GLY GLY Y . n 
Y  11 132 GLN 132 133 133 GLN GLN Y . n 
Y  11 133 THR 133 134 134 THR THR Y . n 
Y  11 134 PHE 134 135 135 PHE PHE Y . n 
Y  11 135 ALA 135 136 136 ALA ALA Y . n 
Y  11 136 TYR 136 137 137 TYR TYR Y . n 
Y  11 137 GLY 137 138 138 GLY GLY Y . n 
Y  11 138 VAL 138 139 139 VAL VAL Y . n 
Y  11 139 LEU 139 140 140 LEU LEU Y . n 
Y  11 140 ASP 140 141 141 ASP ASP Y . n 
Y  11 141 SER 141 142 142 SER SER Y . n 
Y  11 142 ASN 142 143 143 ASN ASN Y . n 
Y  11 143 TYR 143 144 144 TYR TYR Y . n 
Y  11 144 LYS 144 145 145 LYS LYS Y . n 
Y  11 145 TRP 145 146 146 TRP TRP Y . n 
Y  11 146 ASP 146 147 147 ASP ASP Y . n 
Y  11 147 LEU 147 148 148 LEU LEU Y . n 
Y  11 148 SER 148 149 149 SER SER Y . n 
Y  11 149 VAL 149 150 150 VAL VAL Y . n 
Y  11 150 GLU 150 151 151 GLU GLU Y . n 
Y  11 151 ASP 151 152 152 ASP ASP Y . n 
Y  11 152 ALA 152 153 153 ALA ALA Y . n 
Y  11 153 LEU 153 154 154 LEU LEU Y . n 
Y  11 154 TYR 154 155 155 TYR TYR Y . n 
Y  11 155 LEU 155 156 156 LEU LEU Y . n 
Y  11 156 GLY 156 157 157 GLY GLY Y . n 
Y  11 157 LYS 157 158 158 LYS LYS Y . n 
Y  11 158 ARG 158 159 159 ARG ARG Y . n 
Y  11 159 SER 159 160 160 SER SER Y . n 
Y  11 160 ILE 160 161 161 ILE ILE Y . n 
Y  11 161 LEU 161 162 162 LEU LEU Y . n 
Y  11 162 ALA 162 163 163 ALA ALA Y . n 
Y  11 163 ALA 163 164 164 ALA ALA Y . n 
Y  11 164 ALA 164 165 165 ALA ALA Y . n 
Y  11 165 HIS 165 166 166 HIS HIS Y . n 
Y  11 166 ARG 166 167 167 ARG ARG Y . n 
Y  11 167 ASP 167 168 168 ASP ASP Y . n 
Y  11 168 ALA 168 169 169 ALA ALA Y . n 
Y  11 169 TYR 169 170 170 TYR TYR Y . n 
Y  11 170 SER 170 171 171 SER SER Y . n 
Y  11 171 GLY 171 172 172 GLY GLY Y . n 
Y  11 172 GLY 172 173 173 GLY GLY Y . n 
Y  11 173 SER 173 174 174 SER SER Y . n 
Y  11 174 VAL 174 175 175 VAL VAL Y . n 
Y  11 175 ASN 175 176 176 ASN ASN Y . n 
Y  11 176 LEU 176 177 177 LEU LEU Y . n 
Y  11 177 TYR 177 178 178 TYR TYR Y . n 
Y  11 178 HIS 178 179 179 HIS HIS Y . n 
Y  11 179 VAL 179 180 180 VAL VAL Y . n 
Y  11 180 THR 180 181 181 THR THR Y . n 
Y  11 181 GLU 181 182 182 GLU GLU Y . n 
Y  11 182 ASP 182 183 183 ASP ASP Y . n 
Y  11 183 GLY 183 184 184 GLY GLY Y . n 
Y  11 184 TRP 184 185 185 TRP TRP Y . n 
Y  11 185 ILE 185 186 186 ILE ILE Y . n 
Y  11 186 TYR 186 187 187 TYR TYR Y . n 
Y  11 187 HIS 187 188 188 HIS HIS Y . n 
Y  11 188 GLY 188 189 189 GLY GLY Y . n 
Y  11 189 ASN 189 190 190 ASN ASN Y . n 
Y  11 190 HIS 190 191 191 HIS HIS Y . n 
Y  11 191 ASP 191 192 192 ASP ASP Y . n 
Y  11 192 VAL 192 193 193 VAL VAL Y . n 
Y  11 193 GLY 193 194 194 GLY GLY Y . n 
Y  11 194 GLU 194 195 195 GLU GLU Y . n 
Y  11 195 LEU 195 196 196 LEU LEU Y . n 
Y  11 196 PHE 196 197 197 PHE PHE Y . n 
Y  11 197 TRP 197 198 198 TRP TRP Y . n 
Y  11 198 LYS 198 199 199 LYS LYS Y . n 
Y  11 199 VAL 199 200 200 VAL VAL Y . n 
Y  11 200 LYS 200 201 201 LYS LYS Y . n 
Y  11 201 GLU 201 202 202 GLU GLU Y . n 
Y  11 202 GLU 202 203 203 GLU GLU Y . n 
Y  11 203 GLU 203 204 204 GLU GLU Y . n 
Y  11 204 GLY 204 205 205 GLY GLY Y . n 
Y  11 205 SER 205 206 206 SER SER Y . n 
Y  11 206 PHE 206 207 207 PHE PHE Y . n 
Y  11 207 ASN 207 208 208 ASN ASN Y . n 
Y  11 208 ASN 208 209 209 ASN ASN Y . n 
Y  11 209 VAL 209 210 210 VAL VAL Y . n 
Y  11 210 ILE 210 211 211 ILE ILE Y . n 
Y  11 211 GLY 211 212 212 GLY GLY Y . n 
Z  12 1   GLN 1   1   1   GLN GLN Z . n 
Z  12 2   PHE 2   2   2   PHE PHE Z . n 
Z  12 3   ASN 3   3   3   ASN ASN Z . n 
Z  12 4   PRO 4   4   4   PRO PRO Z . n 
Z  12 5   TYR 5   5   5   TYR TYR Z . n 
Z  12 6   GLY 6   6   6   GLY GLY Z . n 
Z  12 7   ASP 7   7   7   ASP ASP Z . n 
Z  12 8   ASN 8   8   8   ASN ASN Z . n 
Z  12 9   GLY 9   9   9   GLY GLY Z . n 
Z  12 10  GLY 10  10  10  GLY GLY Z . n 
Z  12 11  THR 11  11  11  THR THR Z . n 
Z  12 12  ILE 12  12  12  ILE ILE Z . n 
Z  12 13  LEU 13  13  13  LEU LEU Z . n 
Z  12 14  GLY 14  14  14  GLY GLY Z . n 
Z  12 15  ILE 15  15  15  ILE ILE Z . n 
Z  12 16  ALA 16  16  16  ALA ALA Z . n 
Z  12 17  GLY 17  17  17  GLY GLY Z . n 
Z  12 18  GLU 18  18  18  GLU GLU Z . n 
Z  12 19  ASP 19  19  19  ASP ASP Z . n 
Z  12 20  PHE 20  20  20  PHE PHE Z . n 
Z  12 21  ALA 21  21  21  ALA ALA Z . n 
Z  12 22  VAL 22  22  22  VAL VAL Z . n 
Z  12 23  LEU 23  23  23  LEU LEU Z . n 
Z  12 24  ALA 24  24  24  ALA ALA Z . n 
Z  12 25  GLY 25  25  25  GLY GLY Z . n 
Z  12 26  ASP 26  26  26  ASP ASP Z . n 
Z  12 27  THR 27  27  27  THR THR Z . n 
Z  12 28  ARG 28  28  28  ARG ARG Z . n 
Z  12 29  ASN 29  29  29  ASN ASN Z . n 
Z  12 30  ILE 30  30  30  ILE ILE Z . n 
Z  12 31  THR 31  31  31  THR THR Z . n 
Z  12 32  ASP 32  32  32  ASP ASP Z . n 
Z  12 33  TYR 33  33  33  TYR TYR Z . n 
Z  12 34  SER 34  34  34  SER SER Z . n 
Z  12 35  ILE 35  35  35  ILE ILE Z . n 
Z  12 36  ASN 36  36  36  ASN ASN Z . n 
Z  12 37  SER 37  37  37  SER SER Z . n 
Z  12 38  ARG 38  38  38  ARG ARG Z . n 
Z  12 39  TYR 39  39  39  TYR TYR Z . n 
Z  12 40  GLU 40  40  40  GLU GLU Z . n 
Z  12 41  PRO 41  41  41  PRO PRO Z . n 
Z  12 42  LYS 42  42  42  LYS LYS Z . n 
Z  12 43  VAL 43  43  43  VAL VAL Z . n 
Z  12 44  PHE 44  44  44  PHE PHE Z . n 
Z  12 45  ASP 45  45  45  ASP ASP Z . n 
Z  12 46  CYS 46  46  46  CYS CYS Z . n 
Z  12 47  GLY 47  47  47  GLY GLY Z . n 
Z  12 48  ASP 48  48  48  ASP ASP Z . n 
Z  12 49  ASN 49  49  49  ASN ASN Z . n 
Z  12 50  ILE 50  50  50  ILE ILE Z . n 
Z  12 51  VAL 51  51  51  VAL VAL Z . n 
Z  12 52  MET 52  52  52  MET MET Z . n 
Z  12 53  SER 53  53  53  SER SER Z . n 
Z  12 54  ALA 54  54  54  ALA ALA Z . n 
Z  12 55  ASN 55  55  55  ASN ASN Z . n 
Z  12 56  GLY 56  56  56  GLY GLY Z . n 
Z  12 57  PHE 57  57  57  PHE PHE Z . n 
Z  12 58  ALA 58  58  58  ALA ALA Z . n 
Z  12 59  ALA 59  59  59  ALA ALA Z . n 
Z  12 60  ASP 60  60  60  ASP ASP Z . n 
Z  12 61  GLY 61  61  61  GLY GLY Z . n 
Z  12 62  ASP 62  62  62  ASP ASP Z . n 
Z  12 63  ALA 63  63  63  ALA ALA Z . n 
Z  12 64  LEU 64  64  64  LEU LEU Z . n 
Z  12 65  VAL 65  65  65  VAL VAL Z . n 
Z  12 66  LYS 66  66  66  LYS LYS Z . n 
Z  12 67  ARG 67  67  67  ARG ARG Z . n 
Z  12 68  PHE 68  68  68  PHE PHE Z . n 
Z  12 69  LYS 69  69  69  LYS LYS Z . n 
Z  12 70  ASN 70  70  70  ASN ASN Z . n 
Z  12 71  SER 71  71  71  SER SER Z . n 
Z  12 72  VAL 72  72  72  VAL VAL Z . n 
Z  12 73  LYS 73  73  73  LYS LYS Z . n 
Z  12 74  TRP 74  74  74  TRP TRP Z . n 
Z  12 75  TYR 75  75  75  TYR TYR Z . n 
Z  12 76  HIS 76  76  76  HIS HIS Z . n 
Z  12 77  PHE 77  77  77  PHE PHE Z . n 
Z  12 78  ASP 78  78  78  ASP ASP Z . n 
Z  12 79  HIS 79  79  79  HIS HIS Z . n 
Z  12 80  ASN 80  80  80  ASN ASN Z . n 
Z  12 81  ASP 81  81  81  ASP ASP Z . n 
Z  12 82  LYS 82  82  82  LYS LYS Z . n 
Z  12 83  LYS 83  83  83  LYS LYS Z . n 
Z  12 84  LEU 84  84  84  LEU LEU Z . n 
Z  12 85  SER 85  85  85  SER SER Z . n 
Z  12 86  ILE 86  86  86  ILE ILE Z . n 
Z  12 87  ASN 87  87  87  ASN ASN Z . n 
Z  12 88  SER 88  88  88  SER SER Z . n 
Z  12 89  ALA 89  89  89  ALA ALA Z . n 
Z  12 90  ALA 90  90  90  ALA ALA Z . n 
Z  12 91  ARG 91  91  91  ARG ARG Z . n 
Z  12 92  ASN 92  92  92  ASN ASN Z . n 
Z  12 93  ILE 93  93  93  ILE ILE Z . n 
Z  12 94  GLN 94  94  94  GLN GLN Z . n 
Z  12 95  HIS 95  95  95  HIS HIS Z . n 
Z  12 96  LEU 96  96  96  LEU LEU Z . n 
Z  12 97  LEU 97  97  97  LEU LEU Z . n 
Z  12 98  TYR 98  98  98  TYR TYR Z . n 
Z  12 99  GLY 99  99  99  GLY GLY Z . n 
Z  12 100 LYS 100 100 100 LYS LYS Z . n 
Z  12 101 ARG 101 101 101 ARG ARG Z . n 
Z  12 102 PHE 102 102 102 PHE PHE Z . n 
Z  12 103 PHE 103 103 103 PHE PHE Z . n 
Z  12 104 PRO 104 104 104 PRO PRO Z . n 
Z  12 105 TYR 105 105 105 TYR TYR Z . n 
Z  12 106 TYR 106 106 106 TYR TYR Z . n 
Z  12 107 VAL 107 107 107 VAL VAL Z . n 
Z  12 108 HIS 108 108 108 HIS HIS Z . n 
Z  12 109 THR 109 109 109 THR THR Z . n 
Z  12 110 ILE 110 110 110 ILE ILE Z . n 
Z  12 111 ILE 111 111 111 ILE ILE Z . n 
Z  12 112 ALA 112 112 112 ALA ALA Z . n 
Z  12 113 GLY 113 113 113 GLY GLY Z . n 
Z  12 114 LEU 114 114 114 LEU LEU Z . n 
Z  12 115 ASP 115 115 115 ASP ASP Z . n 
Z  12 116 GLU 116 116 116 GLU GLU Z . n 
Z  12 117 ASP 117 117 117 ASP ASP Z . n 
Z  12 118 GLY 118 118 118 GLY GLY Z . n 
Z  12 119 LYS 119 119 119 LYS LYS Z . n 
Z  12 120 GLY 120 120 120 GLY GLY Z . n 
Z  12 121 ALA 121 121 121 ALA ALA Z . n 
Z  12 122 VAL 122 122 122 VAL VAL Z . n 
Z  12 123 TYR 123 123 123 TYR TYR Z . n 
Z  12 124 SER 124 124 124 SER SER Z . n 
Z  12 125 PHE 125 125 125 PHE PHE Z . n 
Z  12 126 ASP 126 126 126 ASP ASP Z . n 
Z  12 127 PRO 127 127 127 PRO PRO Z . n 
Z  12 128 VAL 128 128 128 VAL VAL Z . n 
Z  12 129 GLY 129 129 129 GLY GLY Z . n 
Z  12 130 SER 130 130 130 SER SER Z . n 
Z  12 131 TYR 131 131 131 TYR TYR Z . n 
Z  12 132 GLU 132 132 132 GLU GLU Z . n 
Z  12 133 ARG 133 133 133 ARG ARG Z . n 
Z  12 134 GLU 134 134 134 GLU GLU Z . n 
Z  12 135 GLN 135 135 135 GLN GLN Z . n 
Z  12 136 CYS 136 136 136 CYS CYS Z . n 
Z  12 137 ARG 137 137 137 ARG ARG Z . n 
Z  12 138 ALA 138 138 138 ALA ALA Z . n 
Z  12 139 GLY 139 139 139 GLY GLY Z . n 
Z  12 140 GLY 140 140 140 GLY GLY Z . n 
Z  12 141 ALA 141 141 141 ALA ALA Z . n 
Z  12 142 ALA 142 142 142 ALA ALA Z . n 
Z  12 143 ALA 143 143 143 ALA ALA Z . n 
Z  12 144 SER 144 144 144 SER SER Z . n 
Z  12 145 LEU 145 145 145 LEU LEU Z . n 
Z  12 146 ILE 146 146 146 ILE ILE Z . n 
Z  12 147 MET 147 147 147 MET MET Z . n 
Z  12 148 PRO 148 148 148 PRO PRO Z . n 
Z  12 149 PHE 149 149 149 PHE PHE Z . n 
Z  12 150 LEU 150 150 150 LEU LEU Z . n 
Z  12 151 ASP 151 151 151 ASP ASP Z . n 
Z  12 152 ASN 152 152 152 ASN ASN Z . n 
Z  12 153 GLN 153 153 153 GLN GLN Z . n 
Z  12 154 VAL 154 154 154 VAL VAL Z . n 
Z  12 155 ASN 155 155 155 ASN ASN Z . n 
Z  12 156 PHE 156 156 156 PHE PHE Z . n 
Z  12 157 LYS 157 157 157 LYS LYS Z . n 
Z  12 158 ASN 158 158 158 ASN ASN Z . n 
Z  12 159 GLN 159 159 159 GLN GLN Z . n 
Z  12 160 TYR 160 160 160 TYR TYR Z . n 
Z  12 161 GLU 161 161 161 GLU GLU Z . n 
Z  12 162 PRO 162 162 162 PRO PRO Z . n 
Z  12 163 GLY 163 163 163 GLY GLY Z . n 
Z  12 164 THR 164 164 164 THR THR Z . n 
Z  12 165 ASN 165 165 165 ASN ASN Z . n 
Z  12 166 GLY 166 166 166 GLY GLY Z . n 
Z  12 167 LYS 167 167 167 LYS LYS Z . n 
Z  12 168 VAL 168 168 168 VAL VAL Z . n 
Z  12 169 LYS 169 169 169 LYS LYS Z . n 
Z  12 170 LYS 170 170 170 LYS LYS Z . n 
Z  12 171 PRO 171 171 171 PRO PRO Z . n 
Z  12 172 LEU 172 172 172 LEU LEU Z . n 
Z  12 173 LYS 173 173 173 LYS LYS Z . n 
Z  12 174 TYR 174 174 174 TYR TYR Z . n 
Z  12 175 LEU 175 175 175 LEU LEU Z . n 
Z  12 176 SER 176 176 176 SER SER Z . n 
Z  12 177 VAL 177 177 177 VAL VAL Z . n 
Z  12 178 GLU 178 178 178 GLU GLU Z . n 
Z  12 179 GLU 179 179 179 GLU GLU Z . n 
Z  12 180 VAL 180 180 180 VAL VAL Z . n 
Z  12 181 ILE 181 181 181 ILE ILE Z . n 
Z  12 182 LYS 182 182 182 LYS LYS Z . n 
Z  12 183 LEU 183 183 183 LEU LEU Z . n 
Z  12 184 VAL 184 184 184 VAL VAL Z . n 
Z  12 185 ARG 185 185 185 ARG ARG Z . n 
Z  12 186 ASP 186 186 186 ASP ASP Z . n 
Z  12 187 SER 187 187 187 SER SER Z . n 
Z  12 188 PHE 188 188 188 PHE PHE Z . n 
Z  12 189 THR 189 189 189 THR THR Z . n 
Z  12 190 SER 190 190 190 SER SER Z . n 
Z  12 191 ALA 191 191 191 ALA ALA Z . n 
Z  12 192 THR 192 192 192 THR THR Z . n 
Z  12 193 GLU 193 193 193 GLU GLU Z . n 
Z  12 194 ARG 194 194 194 ARG ARG Z . n 
Z  12 195 HIS 195 195 195 HIS HIS Z . n 
Z  12 196 ILE 196 196 196 ILE ILE Z . n 
Z  12 197 GLN 197 197 197 GLN GLN Z . n 
Z  12 198 VAL 198 198 198 VAL VAL Z . n 
Z  12 199 GLY 199 199 199 GLY GLY Z . n 
Z  12 200 ASP 200 200 200 ASP ASP Z . n 
Z  12 201 GLY 201 201 201 GLY GLY Z . n 
Z  12 202 LEU 202 202 202 LEU LEU Z . n 
Z  12 203 GLU 203 203 203 GLU GLU Z . n 
Z  12 204 ILE 204 204 204 ILE ILE Z . n 
Z  12 205 LEU 205 205 205 LEU LEU Z . n 
Z  12 206 ILE 206 206 206 ILE ILE Z . n 
Z  12 207 VAL 207 207 207 VAL VAL Z . n 
Z  12 208 THR 208 208 208 THR THR Z . n 
Z  12 209 LYS 209 209 209 LYS LYS Z . n 
Z  12 210 ASP 210 210 210 ASP ASP Z . n 
Z  12 211 GLY 211 211 211 GLY GLY Z . n 
Z  12 212 VAL 212 212 212 VAL VAL Z . n 
Z  12 213 ARG 213 213 213 ARG ARG Z . n 
Z  12 214 LYS 214 214 214 LYS LYS Z . n 
Z  12 215 GLU 215 215 215 GLU GLU Z . n 
Z  12 216 PHE 216 216 216 PHE PHE Z . n 
Z  12 217 TYR 217 217 217 TYR TYR Z . n 
Z  12 218 GLU 218 218 218 GLU GLU Z . n 
Z  12 219 LEU 219 219 219 LEU LEU Z . n 
Z  12 220 LYS 220 220 220 LYS LYS Z . n 
Z  12 221 ARG 221 221 221 ARG ARG Z . n 
Z  12 222 ASP 222 222 222 ASP ASP Z . n 
AA 13 1   THR 1   -12 ?   ?   ?   a . n 
AA 13 2   GLN 2   -11 ?   ?   ?   a . n 
AA 13 3   ILE 3   -10 ?   ?   ?   a . n 
AA 13 4   ALA 4   -9  ?   ?   ?   a . n 
AA 13 5   ASN 5   -8  ?   ?   ?   a . n 
AA 13 6   ALA 6   -7  ?   ?   ?   a . n 
AA 13 7   GLY 7   -6  ?   ?   ?   a . n 
AA 13 8   ALA 8   -5  ?   ?   ?   a . n 
AA 13 9   SER 9   -4  ?   ?   ?   a . n 
AA 13 10  PRO 10  -3  ?   ?   ?   a . n 
AA 13 11  MET 11  -2  ?   ?   ?   a . n 
AA 13 12  VAL 12  -1  ?   ?   ?   a . n 
AA 13 13  ASN 13  0   ?   ?   ?   a . n 
AA 13 14  THR 14  1   1   THR THR a . n 
AA 13 15  GLN 15  2   2   GLN GLN a . n 
AA 13 16  GLN 16  3   3   GLN GLN a . n 
AA 13 17  PRO 17  4   4   PRO PRO a . n 
AA 13 18  ILE 18  5   5   ILE ILE a . n 
AA 13 19  VAL 19  6   6   VAL VAL a . n 
AA 13 20  THR 20  7   7   THR THR a . n 
AA 13 21  GLY 21  8   8   GLY GLY a . n 
AA 13 22  THR 22  9   9   THR THR a . n 
AA 13 23  SER 23  10  10  SER SER a . n 
AA 13 24  VAL 24  11  11  VAL VAL a . n 
AA 13 25  ILE 25  12  12  ILE ILE a . n 
AA 13 26  SER 26  13  13  SER SER a . n 
AA 13 27  MET 27  14  14  MET MET a . n 
AA 13 28  LYS 28  15  15  LYS LYS a . n 
AA 13 29  TYR 29  16  16  TYR TYR a . n 
AA 13 30  ASP 30  17  17  ASP ASP a . n 
AA 13 31  ASN 31  18  18  ASN ASN a . n 
AA 13 32  GLY 32  19  19  GLY GLY a . n 
AA 13 33  VAL 33  20  20  VAL VAL a . n 
AA 13 34  ILE 34  21  21  ILE ILE a . n 
AA 13 35  ILE 35  22  22  ILE ILE a . n 
AA 13 36  ALA 36  23  23  ALA ALA a . n 
AA 13 37  ALA 37  24  24  ALA ALA a . n 
AA 13 38  ASP 38  25  25  ASP ASP a . n 
AA 13 39  ASN 39  26  26  ASN ASN a . n 
AA 13 40  LEU 40  27  27  LEU LEU a . n 
AA 13 41  GLY 41  28  28  GLY GLY a . n 
AA 13 42  SER 42  29  29  SER SER a . n 
AA 13 43  TYR 43  30  30  TYR TYR a . n 
AA 13 44  GLY 44  31  31  GLY GLY a . n 
AA 13 45  SER 45  32  32  SER SER a . n 
AA 13 46  LEU 46  33  33  LEU LEU a . n 
AA 13 47  LEU 47  34  34  LEU LEU a . n 
AA 13 48  ARG 48  35  35  ARG ARG a . n 
AA 13 49  PHE 49  36  36  PHE PHE a . n 
AA 13 50  ASN 50  37  37  ASN ASN a . n 
AA 13 51  GLY 51  38  38  GLY GLY a . n 
AA 13 52  VAL 52  39  39  VAL VAL a . n 
AA 13 53  GLU 53  40  40  GLU GLU a . n 
AA 13 54  ARG 54  41  41  ARG ARG a . n 
AA 13 55  LEU 55  42  42  LEU LEU a . n 
AA 13 56  ILE 56  43  43  ILE ILE a . n 
AA 13 57  PRO 57  44  44  PRO PRO a . n 
AA 13 58  VAL 58  45  45  VAL VAL a . n 
AA 13 59  GLY 59  46  46  GLY GLY a . n 
AA 13 60  ASP 60  47  47  ASP ASP a . n 
AA 13 61  ASN 61  48  48  ASN ASN a . n 
AA 13 62  THR 62  49  49  THR THR a . n 
AA 13 63  VAL 63  50  50  VAL VAL a . n 
AA 13 64  VAL 64  51  51  VAL VAL a . n 
AA 13 65  GLY 65  52  52  GLY GLY a . n 
AA 13 66  ILE 66  53  53  ILE ILE a . n 
AA 13 67  SER 67  54  54  SER SER a . n 
AA 13 68  GLY 68  55  55  GLY GLY a . n 
AA 13 69  ASP 69  56  56  ASP ASP a . n 
AA 13 70  ILE 70  57  57  ILE ILE a . n 
AA 13 71  SER 71  58  58  SER SER a . n 
AA 13 72  ASP 72  59  59  ASP ASP a . n 
AA 13 73  MET 73  60  60  MET MET a . n 
AA 13 74  GLN 74  61  61  GLN GLN a . n 
AA 13 75  HIS 75  62  62  HIS HIS a . n 
AA 13 76  ILE 76  63  63  ILE ILE a . n 
AA 13 77  GLU 77  64  64  GLU GLU a . n 
AA 13 78  ARG 78  65  65  ARG ARG a . n 
AA 13 79  LEU 79  66  66  LEU LEU a . n 
AA 13 80  LEU 80  67  67  LEU LEU a . n 
AA 13 81  LYS 81  68  68  LYS LYS a . n 
AA 13 82  ASP 82  69  69  ASP ASP a . n 
AA 13 83  LEU 83  70  70  LEU LEU a . n 
AA 13 84  VAL 84  71  71  VAL VAL a . n 
AA 13 85  THR 85  72  72  THR THR a . n 
AA 13 86  GLU 86  73  73  GLU GLU a . n 
AA 13 87  ASN 87  74  74  ASN ASN a . n 
AA 13 88  ALA 88  75  75  ALA ALA a . n 
AA 13 89  TYR 89  76  76  TYR TYR a . n 
AA 13 90  ASP 90  77  77  ASP ASP a . n 
AA 13 91  ASN 91  78  78  ASN ASN a . n 
AA 13 92  PRO 92  79  79  PRO PRO a . n 
AA 13 93  LEU 93  80  80  LEU LEU a . n 
AA 13 94  ALA 94  81  81  ALA ALA a . n 
AA 13 95  ASP 95  82  82  ASP ASP a . n 
AA 13 96  ALA 96  83  83  ALA ALA a . n 
AA 13 97  GLU 97  84  84  GLU GLU a . n 
AA 13 98  GLU 98  85  85  GLU GLU a . n 
AA 13 99  ALA 99  86  86  ALA ALA a . n 
AA 13 100 LEU 100 87  87  LEU LEU a . n 
AA 13 101 GLU 101 88  88  GLU GLU a . n 
AA 13 102 PRO 102 89  89  PRO PRO a . n 
AA 13 103 SER 103 90  90  SER SER a . n 
AA 13 104 TYR 104 91  91  TYR TYR a . n 
AA 13 105 ILE 105 92  92  ILE ILE a . n 
AA 13 106 PHE 106 93  93  PHE PHE a . n 
AA 13 107 GLU 107 94  94  GLU GLU a . n 
AA 13 108 TYR 108 95  95  TYR TYR a . n 
AA 13 109 LEU 109 96  96  LEU LEU a . n 
AA 13 110 ALA 110 97  97  ALA ALA a . n 
AA 13 111 THR 111 98  98  THR THR a . n 
AA 13 112 VAL 112 99  99  VAL VAL a . n 
AA 13 113 MET 113 100 100 MET MET a . n 
AA 13 114 TYR 114 101 101 TYR TYR a . n 
AA 13 115 GLN 115 102 102 GLN GLN a . n 
AA 13 116 ARG 116 103 103 ARG ARG a . n 
AA 13 117 ARG 117 104 104 ARG ARG a . n 
AA 13 118 SER 118 105 105 SER SER a . n 
AA 13 119 LYS 119 106 106 LYS LYS a . n 
AA 13 120 MET 120 107 107 MET MET a . n 
AA 13 121 ASN 121 108 108 ASN ASN a . n 
AA 13 122 PRO 122 109 109 PRO PRO a . n 
AA 13 123 LEU 123 110 110 LEU LEU a . n 
AA 13 124 TRP 124 111 111 TRP TRP a . n 
AA 13 125 ASN 125 112 112 ASN ASN a . n 
AA 13 126 ALA 126 113 113 ALA ALA a . n 
AA 13 127 ILE 127 114 114 ILE ILE a . n 
AA 13 128 ILE 128 115 115 ILE ILE a . n 
AA 13 129 VAL 129 116 116 VAL VAL a . n 
AA 13 130 ALA 130 117 117 ALA ALA a . n 
AA 13 131 GLY 131 118 118 GLY GLY a . n 
AA 13 132 VAL 132 119 119 VAL VAL a . n 
AA 13 133 GLN 133 120 120 GLN GLN a . n 
AA 13 134 SER 134 121 121 SER SER a . n 
AA 13 135 ASN 135 122 122 ASN ASN a . n 
AA 13 136 GLY 136 123 123 GLY GLY a . n 
AA 13 137 ASP 137 124 124 ASP ASP a . n 
AA 13 138 GLN 138 125 125 GLN GLN a . n 
AA 13 139 PHE 139 126 126 PHE PHE a . n 
AA 13 140 LEU 140 127 127 LEU LEU a . n 
AA 13 141 ARG 141 128 128 ARG ARG a . n 
AA 13 142 TYR 142 129 129 TYR TYR a . n 
AA 13 143 VAL 143 130 130 VAL VAL a . n 
AA 13 144 ASN 144 131 131 ASN ASN a . n 
AA 13 145 LEU 145 132 132 LEU LEU a . n 
AA 13 146 LEU 146 133 133 LEU LEU a . n 
AA 13 147 GLY 147 134 134 GLY GLY a . n 
AA 13 148 VAL 148 135 135 VAL VAL a . n 
AA 13 149 THR 149 136 136 THR THR a . n 
AA 13 150 TYR 150 137 137 TYR TYR a . n 
AA 13 151 SER 151 138 138 SER SER a . n 
AA 13 152 SER 152 139 139 SER SER a . n 
AA 13 153 PRO 153 140 140 PRO PRO a . n 
AA 13 154 THR 154 141 141 THR THR a . n 
AA 13 155 LEU 155 142 142 LEU LEU a . n 
AA 13 156 ALA 156 143 143 ALA ALA a . n 
AA 13 157 THR 157 144 144 THR THR a . n 
AA 13 158 GLY 158 145 145 GLY GLY a . n 
AA 13 159 PHE 159 146 146 PHE PHE a . n 
AA 13 160 GLY 160 147 147 GLY GLY a . n 
AA 13 161 ALA 161 148 148 ALA ALA a . n 
AA 13 162 HIS 162 149 149 HIS HIS a . n 
AA 13 163 MET 163 150 150 MET MET a . n 
AA 13 164 ALA 164 151 151 ALA ALA a . n 
AA 13 165 ASN 165 152 152 ASN ASN a . n 
AA 13 166 PRO 166 153 153 PRO PRO a . n 
AA 13 167 LEU 167 154 154 LEU LEU a . n 
AA 13 168 LEU 168 155 155 LEU LEU a . n 
AA 13 169 ARG 169 156 156 ARG ARG a . n 
AA 13 170 LYS 170 157 157 LYS LYS a . n 
AA 13 171 VAL 171 158 158 VAL VAL a . n 
AA 13 172 VAL 172 159 159 VAL VAL a . n 
AA 13 173 ASP 173 160 160 ASP ASP a . n 
AA 13 174 ARG 174 161 161 ARG ARG a . n 
AA 13 175 GLU 175 162 162 GLU GLU a . n 
AA 13 176 SER 176 163 163 SER SER a . n 
AA 13 177 ASP 177 164 164 ASP ASP a . n 
AA 13 178 ILE 178 165 165 ILE ILE a . n 
AA 13 179 PRO 179 166 166 PRO PRO a . n 
AA 13 180 LYS 180 167 167 LYS LYS a . n 
AA 13 181 THR 181 168 168 THR THR a . n 
AA 13 182 THR 182 169 169 THR THR a . n 
AA 13 183 VAL 183 170 170 VAL VAL a . n 
AA 13 184 GLN 184 171 171 GLN GLN a . n 
AA 13 185 VAL 185 172 172 VAL VAL a . n 
AA 13 186 ALA 186 173 173 ALA ALA a . n 
AA 13 187 GLU 187 174 174 GLU GLU a . n 
AA 13 188 GLU 188 175 175 GLU GLU a . n 
AA 13 189 ALA 189 176 176 ALA ALA a . n 
AA 13 190 ILE 190 177 177 ILE ILE a . n 
AA 13 191 VAL 191 178 178 VAL VAL a . n 
AA 13 192 ASN 192 179 179 ASN ASN a . n 
AA 13 193 ALA 193 180 180 ALA ALA a . n 
AA 13 194 MET 194 181 181 MET MET a . n 
AA 13 195 ARG 195 182 182 ARG ARG a . n 
AA 13 196 VAL 196 183 183 VAL VAL a . n 
AA 13 197 LEU 197 184 184 LEU LEU a . n 
AA 13 198 TYR 198 185 185 TYR TYR a . n 
AA 13 199 TYR 199 186 186 TYR TYR a . n 
AA 13 200 ARG 200 187 187 ARG ARG a . n 
AA 13 201 ASP 201 188 188 ASP ASP a . n 
AA 13 202 ALA 202 189 189 ALA ALA a . n 
AA 13 203 ARG 203 190 190 ARG ARG a . n 
AA 13 204 SER 204 191 191 SER SER a . n 
AA 13 205 SER 205 192 192 SER SER a . n 
AA 13 206 ARG 206 193 193 ARG ARG a . n 
AA 13 207 ASN 207 194 194 ASN ASN a . n 
AA 13 208 PHE 208 195 195 PHE PHE a . n 
AA 13 209 SER 209 196 196 SER SER a . n 
AA 13 210 LEU 210 197 197 LEU LEU a . n 
AA 13 211 ALA 211 198 198 ALA ALA a . n 
AA 13 212 ILE 212 199 199 ILE ILE a . n 
AA 13 213 ILE 213 200 200 ILE ILE a . n 
AA 13 214 ASP 214 201 201 ASP ASP a . n 
AA 13 215 LYS 215 202 202 LYS LYS a . n 
AA 13 216 ASN 216 203 203 ASN ASN a . n 
AA 13 217 THR 217 204 204 THR THR a . n 
AA 13 218 GLY 218 205 205 GLY GLY a . n 
AA 13 219 LEU 219 206 206 LEU LEU a . n 
AA 13 220 THR 220 207 207 THR THR a . n 
AA 13 221 PHE 221 208 208 PHE PHE a . n 
AA 13 222 LYS 222 209 209 LYS LYS a . n 
AA 13 223 LYS 223 210 210 LYS LYS a . n 
AA 13 224 ASN 224 211 211 ASN ASN a . n 
AA 13 225 LEU 225 212 212 LEU LEU a . n 
AA 13 226 GLN 226 213 213 GLN GLN a . n 
AA 13 227 VAL 227 214 214 VAL VAL a . n 
AA 13 228 GLU 228 215 215 GLU GLU a . n 
AA 13 229 ASN 229 216 216 ASN ASN a . n 
AA 13 230 MET 230 217 217 MET MET a . n 
AA 13 231 LYS 231 218 218 LYS LYS a . n 
AA 13 232 TRP 232 219 219 TRP TRP a . n 
AA 13 233 ASP 233 220 220 ASP ASP a . n 
AA 13 234 PHE 234 221 221 PHE PHE a . n 
AA 13 235 ALA 235 222 222 ALA ALA a . n 
AA 13 236 LYS 236 223 223 LYS LYS a . n 
AA 13 237 ASP 237 224 224 ASP ASP a . n 
AA 13 238 ILE 238 225 225 ILE ILE a . n 
AA 13 239 LYS 239 226 226 LYS LYS a . n 
AA 13 240 GLY 240 227 227 GLY GLY a . n 
AA 13 241 TYR 241 228 228 TYR TYR a . n 
AA 13 242 GLY 242 229 229 GLY GLY a . n 
AA 13 243 THR 243 230 230 THR THR a . n 
AA 13 244 GLN 244 231 231 GLN GLN a . n 
AA 13 245 LYS 245 232 232 LYS LYS a . n 
AA 13 246 ILE 246 233 233 ILE ILE a . n 
BA 14 1   THR 1   1   1   THR THR b . n 
BA 14 2   SER 2   2   2   SER SER b . n 
BA 14 3   ILE 3   3   3   ILE ILE b . n 
BA 14 4   MET 4   4   4   MET MET b . n 
BA 14 5   ALA 5   5   5   ALA ALA b . n 
BA 14 6   VAL 6   6   6   VAL VAL b . n 
BA 14 7   THR 7   7   7   THR THR b . n 
BA 14 8   PHE 8   8   8   PHE PHE b . n 
BA 14 9   LYS 9   9   9   LYS LYS b . n 
BA 14 10  ASP 10  10  10  ASP ASP b . n 
BA 14 11  GLY 11  11  11  GLY GLY b . n 
BA 14 12  VAL 12  12  12  VAL VAL b . n 
BA 14 13  ILE 13  13  13  ILE ILE b . n 
BA 14 14  LEU 14  14  14  LEU LEU b . n 
BA 14 15  GLY 15  15  15  GLY GLY b . n 
BA 14 16  ALA 16  16  16  ALA ALA b . n 
BA 14 17  ASP 17  17  17  ASP ASP b . n 
BA 14 18  SER 18  18  18  SER SER b . n 
BA 14 19  ARG 19  19  19  ARG ARG b . n 
BA 14 20  THR 20  20  20  THR THR b . n 
BA 14 21  THR 21  21  21  THR THR b . n 
BA 14 22  THR 22  22  22  THR THR b . n 
BA 14 23  GLY 23  23  23  GLY GLY b . n 
BA 14 24  ALA 24  24  24  ALA ALA b . n 
BA 14 25  TYR 25  25  25  TYR TYR b . n 
BA 14 26  ILE 26  26  26  ILE ILE b . n 
BA 14 27  ALA 27  27  27  ALA ALA b . n 
BA 14 28  ASN 28  28  28  ASN ASN b . n 
BA 14 29  ARG 29  29  29  ARG ARG b . n 
BA 14 30  VAL 30  30  30  VAL VAL b . n 
BA 14 31  THR 31  31  31  THR THR b . n 
BA 14 32  ASP 32  32  32  ASP ASP b . n 
BA 14 33  LYS 33  33  33  LYS LYS b . n 
BA 14 34  LEU 34  34  34  LEU LEU b . n 
BA 14 35  THR 35  35  35  THR THR b . n 
BA 14 36  ARG 36  36  36  ARG ARG b . n 
BA 14 37  VAL 37  37  37  VAL VAL b . n 
BA 14 38  HIS 38  38  38  HIS HIS b . n 
BA 14 39  ASP 39  39  39  ASP ASP b . n 
BA 14 40  LYS 40  40  40  LYS LYS b . n 
BA 14 41  ILE 41  41  41  ILE ILE b . n 
BA 14 42  TRP 42  42  42  TRP TRP b . n 
BA 14 43  CYS 43  43  43  CYS CYS b . n 
BA 14 44  CYS 44  44  44  CYS CYS b . n 
BA 14 45  ARG 45  45  45  ARG ARG b . n 
BA 14 46  SER 46  46  46  SER SER b . n 
BA 14 47  GLY 47  47  47  GLY GLY b . n 
BA 14 48  SER 48  48  48  SER SER b . n 
BA 14 49  ALA 49  49  49  ALA ALA b . n 
BA 14 50  ALA 50  50  50  ALA ALA b . n 
BA 14 51  ASP 51  51  51  ASP ASP b . n 
BA 14 52  THR 52  52  52  THR THR b . n 
BA 14 53  GLN 53  53  53  GLN GLN b . n 
BA 14 54  ALA 54  54  54  ALA ALA b . n 
BA 14 55  ILE 55  55  55  ILE ILE b . n 
BA 14 56  ALA 56  56  56  ALA ALA b . n 
BA 14 57  ASP 57  57  57  ASP ASP b . n 
BA 14 58  ILE 58  58  58  ILE ILE b . n 
BA 14 59  VAL 59  59  59  VAL VAL b . n 
BA 14 60  GLN 60  60  60  GLN GLN b . n 
BA 14 61  TYR 61  61  61  TYR TYR b . n 
BA 14 62  HIS 62  62  62  HIS HIS b . n 
BA 14 63  LEU 63  63  63  LEU LEU b . n 
BA 14 64  GLU 64  64  64  GLU GLU b . n 
BA 14 65  LEU 65  65  65  LEU LEU b . n 
BA 14 66  TYR 66  66  66  TYR TYR b . n 
BA 14 67  THR 67  67  67  THR THR b . n 
BA 14 68  SER 68  68  68  SER SER b . n 
BA 14 69  GLN 69  69  69  GLN GLN b . n 
BA 14 70  TYR 70  70  70  TYR TYR b . n 
BA 14 71  GLY 71  71  71  GLY GLY b . n 
BA 14 72  THR 72  72  72  THR THR b . n 
BA 14 73  PRO 73  73  73  PRO PRO b . n 
BA 14 74  SER 74  74  74  SER SER b . n 
BA 14 75  THR 75  75  75  THR THR b . n 
BA 14 76  GLU 76  76  76  GLU GLU b . n 
BA 14 77  THR 77  77  77  THR THR b . n 
BA 14 78  ALA 78  78  78  ALA ALA b . n 
BA 14 79  ALA 79  79  79  ALA ALA b . n 
BA 14 80  SER 80  80  80  SER SER b . n 
BA 14 81  VAL 81  81  81  VAL VAL b . n 
BA 14 82  PHE 82  82  82  PHE PHE b . n 
BA 14 83  LYS 83  83  83  LYS LYS b . n 
BA 14 84  GLU 84  84  84  GLU GLU b . n 
BA 14 85  LEU 85  85  85  LEU LEU b . n 
BA 14 86  CYS 86  86  86  CYS CYS b . n 
BA 14 87  TYR 87  87  87  TYR TYR b . n 
BA 14 88  GLU 88  88  88  GLU GLU b . n 
BA 14 89  ASN 89  89  89  ASN ASN b . n 
BA 14 90  LYS 90  90  90  LYS LYS b . n 
BA 14 91  ASP 91  91  91  ASP ASP b . n 
BA 14 92  ASN 92  92  92  ASN ASN b . n 
BA 14 93  LEU 93  93  93  LEU LEU b . n 
BA 14 94  THR 94  94  94  THR THR b . n 
BA 14 95  ALA 95  95  95  ALA ALA b . n 
BA 14 96  GLY 96  96  96  GLY GLY b . n 
BA 14 97  ILE 97  97  97  ILE ILE b . n 
BA 14 98  ILE 98  98  98  ILE ILE b . n 
BA 14 99  VAL 99  99  99  VAL VAL b . n 
BA 14 100 ALA 100 100 100 ALA ALA b . n 
BA 14 101 GLY 101 101 101 GLY GLY b . n 
BA 14 102 TYR 102 102 102 TYR TYR b . n 
BA 14 103 ASP 103 103 103 ASP ASP b . n 
BA 14 104 ASP 104 104 104 ASP ASP b . n 
BA 14 105 LYS 105 105 105 LYS LYS b . n 
BA 14 106 ASN 106 106 106 ASN ASN b . n 
BA 14 107 LYS 107 107 107 LYS LYS b . n 
BA 14 108 GLY 108 108 108 GLY GLY b . n 
BA 14 109 GLU 109 109 109 GLU GLU b . n 
BA 14 110 VAL 110 110 110 VAL VAL b . n 
BA 14 111 TYR 111 111 111 TYR TYR b . n 
BA 14 112 THR 112 112 112 THR THR b . n 
BA 14 113 ILE 113 113 113 ILE ILE b . n 
BA 14 114 PRO 114 114 114 PRO PRO b . n 
BA 14 115 LEU 115 115 115 LEU LEU b . n 
BA 14 116 GLY 116 116 116 GLY GLY b . n 
BA 14 117 GLY 117 117 117 GLY GLY b . n 
BA 14 118 SER 118 118 118 SER SER b . n 
BA 14 119 VAL 119 119 119 VAL VAL b . n 
BA 14 120 HIS 120 120 120 HIS HIS b . n 
BA 14 121 LYS 121 121 121 LYS LYS b . n 
BA 14 122 LEU 122 122 122 LEU LEU b . n 
BA 14 123 PRO 123 123 123 PRO PRO b . n 
BA 14 124 TYR 124 124 124 TYR TYR b . n 
BA 14 125 ALA 125 125 125 ALA ALA b . n 
BA 14 126 ILE 126 126 126 ILE ILE b . n 
BA 14 127 ALA 127 127 127 ALA ALA b . n 
BA 14 128 GLY 128 128 128 GLY GLY b . n 
BA 14 129 SER 129 129 129 SER SER b . n 
BA 14 130 GLY 130 130 130 GLY GLY b . n 
BA 14 131 SER 131 131 131 SER SER b . n 
BA 14 132 THR 132 132 132 THR THR b . n 
BA 14 133 PHE 133 133 133 PHE PHE b . n 
BA 14 134 ILE 134 134 134 ILE ILE b . n 
BA 14 135 TYR 135 135 135 TYR TYR b . n 
BA 14 136 GLY 136 136 136 GLY GLY b . n 
BA 14 137 TYR 137 137 137 TYR TYR b . n 
BA 14 138 CYS 138 138 138 CYS CYS b . n 
BA 14 139 ASP 139 139 139 ASP ASP b . n 
BA 14 140 LYS 140 140 140 LYS LYS b . n 
BA 14 141 ASN 141 141 141 ASN ASN b . n 
BA 14 142 PHE 142 142 142 PHE PHE b . n 
BA 14 143 ARG 143 143 143 ARG ARG b . n 
BA 14 144 GLU 144 144 144 GLU GLU b . n 
BA 14 145 ASN 145 145 145 ASN ASN b . n 
BA 14 146 MET 146 146 146 MET MET b . n 
BA 14 147 SER 147 147 147 SER SER b . n 
BA 14 148 LYS 148 148 148 LYS LYS b . n 
BA 14 149 GLU 149 149 149 GLU GLU b . n 
BA 14 150 GLU 150 150 150 GLU GLU b . n 
BA 14 151 THR 151 151 151 THR THR b . n 
BA 14 152 VAL 152 152 152 VAL VAL b . n 
BA 14 153 ASP 153 153 153 ASP ASP b . n 
BA 14 154 PHE 154 154 154 PHE PHE b . n 
BA 14 155 ILE 155 155 155 ILE ILE b . n 
BA 14 156 LYS 156 156 156 LYS LYS b . n 
BA 14 157 HIS 157 157 157 HIS HIS b . n 
BA 14 158 SER 158 158 158 SER SER b . n 
BA 14 159 LEU 159 159 159 LEU LEU b . n 
BA 14 160 SER 160 160 160 SER SER b . n 
BA 14 161 GLN 161 161 161 GLN GLN b . n 
BA 14 162 ALA 162 162 162 ALA ALA b . n 
BA 14 163 ILE 163 163 163 ILE ILE b . n 
BA 14 164 LYS 164 164 164 LYS LYS b . n 
BA 14 165 TRP 165 165 165 TRP TRP b . n 
BA 14 166 ASP 166 166 166 ASP ASP b . n 
BA 14 167 GLY 167 167 167 GLY GLY b . n 
BA 14 168 SER 168 168 168 SER SER b . n 
BA 14 169 SER 169 169 169 SER SER b . n 
BA 14 170 GLY 170 170 170 GLY GLY b . n 
BA 14 171 GLY 171 171 171 GLY GLY b . n 
BA 14 172 VAL 172 172 172 VAL VAL b . n 
BA 14 173 ILE 173 173 173 ILE ILE b . n 
BA 14 174 ARG 174 174 174 ARG ARG b . n 
BA 14 175 MET 175 175 175 MET MET b . n 
BA 14 176 VAL 176 176 176 VAL VAL b . n 
BA 14 177 VAL 177 177 177 VAL VAL b . n 
BA 14 178 LEU 178 178 178 LEU LEU b . n 
BA 14 179 THR 179 179 179 THR THR b . n 
BA 14 180 ALA 180 180 180 ALA ALA b . n 
BA 14 181 ALA 181 181 181 ALA ALA b . n 
BA 14 182 GLY 182 182 182 GLY GLY b . n 
BA 14 183 VAL 183 183 183 VAL VAL b . n 
BA 14 184 GLU 184 184 184 GLU GLU b . n 
BA 14 185 ARG 185 185 185 ARG ARG b . n 
BA 14 186 LEU 186 186 186 LEU LEU b . n 
BA 14 187 ILE 187 187 187 ILE ILE b . n 
BA 14 188 PHE 188 188 188 PHE PHE b . n 
BA 14 189 TYR 189 189 189 TYR TYR b . n 
BA 14 190 PRO 190 190 190 PRO PRO b . n 
BA 14 191 ASP 191 191 191 ASP ASP b . n 
BA 14 192 GLU 192 192 192 GLU GLU b . n 
BA 14 193 TYR 193 193 193 TYR TYR b . n 
BA 14 194 GLU 194 194 194 GLU GLU b . n 
BA 14 195 GLN 195 195 195 GLN GLN b . n 
BA 14 196 LEU 196 196 196 LEU LEU b . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H71 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H71 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
CA 15 MG    1 301 8 MG    MG  G . 
DA 16 A1H71 1 301 1 A1H71 LIG H . 
EA 15 MG    1 302 7 MG    MG  H . 
FA 15 MG    1 301 9 MG    MG  I . 
GA 16 A1H71 1 301 1 A1H71 LIG K . 
HA 15 MG    1 302 1 MG    MG  K . 
IA 15 MG    1 201 5 MG    MG  N . 
JA 16 A1H71 1 301 1 A1H71 LIG V . 
KA 15 MG    1 302 2 MG    MG  V . 
LA 16 A1H71 1 301 1 A1H71 LIG Y . 
MA 15 MG    1 302 4 MG    MG  Y . 
NA 15 MG    1 301 3 MG    MG  Z . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.65 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EY9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     135.580 
_cell.length_a_esd                 ? 
_cell.length_b                     301.800 
_cell.length_b_esd                 ? 
_cell.length_c                     144.370 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EY9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EY9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.99 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.80 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20 mM MgAC2, 13% MPD, 0.1 M MES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100.000 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'LN2 COOLED FIXED-EXIT. SI(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.87313 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.87313 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EY9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.1 
_reflns.d_resolution_low                               30 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     194950 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                30.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.097 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.1 
_reflns_shell.d_res_low                                     3.2 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17800 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.691 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.41 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.07 
_refine.aniso_B[2][2]                            -0.12 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.26 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               100.593 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.931 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EY9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.10 
_refine.ls_d_res_low                             30.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     180564 
_refine.ls_number_reflns_R_free                  9504 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.41 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19514 
_refine.ls_R_factor_R_free                       0.24117 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19275 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.400 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             61.832 
_refine.overall_SU_ML                            0.426 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.10 
_refine_hist.d_res_low                        30.00 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               49456 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        49448 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         8 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  0.013  50354  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.015  47918  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.254  1.645  68112  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.146  1.590  110434 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.356  5.000  6306   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.940 22.791 2530   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.912 15.000 8738   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.739 15.000 284    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.041  0.200  6654   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  57224  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  11336  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.275  5.506  25314  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.275  5.506  25313  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.896  8.253  31590  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.896  8.253  31591  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.930  5.916  25040  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.930  5.916  25040  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.379  ?      36522  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.683  ?      52364  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.683  ?      52365  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 0.530  3.000  98172  ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?      ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 10 ? ? 0.01  ? 0.05 1  'tight positional' ? A 3091 ? ? 10 
'X-RAY DIFFRACTION' 11 ? ? 0.01  ? 0.05 2  'tight positional' ? A 3269 ? ? 11 
'X-RAY DIFFRACTION' 12 ? ? 0.01  ? 0.05 3  'tight positional' ? A 3429 ? ? 12 
'X-RAY DIFFRACTION' 13 ? ? 0.01  ? 0.05 4  'tight positional' ? A 3614 ? ? 13 
'X-RAY DIFFRACTION' 14 ? ? 0.03  ? 0.05 5  'tight positional' ? A 2941 ? ? 14 
'X-RAY DIFFRACTION' 1  ? ? 9.10  ? 0.50 6  'tight thermal'    ? A 3789 ? ? 1  
'X-RAY DIFFRACTION' 2  ? ? 10.10 ? 0.50 7  'tight thermal'    ? A 3750 ? ? 2  
'X-RAY DIFFRACTION' 3  ? ? 10.24 ? 0.50 8  'tight thermal'    ? A 3723 ? ? 3  
'X-RAY DIFFRACTION' 4  ? ? 10.97 ? 0.50 9  'tight thermal'    ? A 3568 ? ? 4  
'X-RAY DIFFRACTION' 5  ? ? 9.96  ? 0.50 10 'tight thermal'    ? A 3501 ? ? 5  
'X-RAY DIFFRACTION' 6  ? ? 11.59 ? 0.50 11 'tight thermal'    ? A 3733 ? ? 6  
'X-RAY DIFFRACTION' 7  ? ? 9.39  ? 0.50 12 'tight thermal'    ? A 3762 ? ? 7  
'X-RAY DIFFRACTION' 8  ? ? 9.03  ? 0.50 13 'tight thermal'    ? A 3398 ? ? 8  
'X-RAY DIFFRACTION' 9  ? ? 8.67  ? 0.50 14 'tight thermal'    ? A 3115 ? ? 9  
'X-RAY DIFFRACTION' 10 ? ? 8.02  ? 0.50 15 'tight thermal'    ? A 3091 ? ? 10 
'X-RAY DIFFRACTION' 11 ? ? 9.50  ? 0.50 16 'tight thermal'    ? A 3269 ? ? 11 
'X-RAY DIFFRACTION' 12 ? ? 9.10  ? 0.50 17 'tight thermal'    ? A 3429 ? ? 12 
'X-RAY DIFFRACTION' 13 ? ? 8.74  ? 0.50 18 'tight thermal'    ? A 3614 ? ? 13 
'X-RAY DIFFRACTION' 14 ? ? 8.49  ? 0.50 19 'tight thermal'    ? A 2941 ? ? 14 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.100 
_refine_ls_shell.d_res_low                        3.180 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             703 
_refine_ls_shell.number_reflns_R_work             13356 
_refine_ls_shell.percent_reflns_obs               99.49 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.346 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.358 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1  ? 1  
2  ? 2  
3  ? 3  
4  ? 4  
5  ? 5  
6  ? 6  
7  ? 7  
8  ? 8  
9  ? 9  
10 ? 10 
11 ? 11 
12 ? 12 
13 ? 13 
14 ? 14 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1  ? 
2  ? 
3  ? 
4  ? 
5  ? 
6  ? 
7  ? 
8  ? 
9  ? 
10 ? 
11 ? 
12 ? 
13 ? 
14 ? 
# 
_struct.entry_id                     9EY9 
_struct.title                        'Yeast 20S proteasome in complex with a sybactin derivative (PheSyr)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EY9 
_struct_keywords.text            
'HYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, Syrbactins, Natural Product Derivative, Binding Analysis, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 2  ? 
C  N N 3  ? 
D  N N 4  ? 
E  N N 5  ? 
F  N N 6  ? 
G  N N 7  ? 
H  N N 8  ? 
I  N N 9  ? 
J  N N 10 ? 
K  N N 11 ? 
L  N N 12 ? 
M  N N 13 ? 
N  N N 14 ? 
O  N N 1  ? 
P  N N 2  ? 
Q  N N 3  ? 
R  N N 4  ? 
S  N N 5  ? 
T  N N 6  ? 
U  N N 7  ? 
V  N N 8  ? 
W  N N 9  ? 
X  N N 10 ? 
Y  N N 11 ? 
Z  N N 12 ? 
AA N N 13 ? 
BA N N 14 ? 
CA N N 15 ? 
DA N N 16 ? 
EA N N 15 ? 
FA N N 15 ? 
GA N N 16 ? 
HA N N 15 ? 
IA N N 15 ? 
JA N N 16 ? 
KA N N 15 ? 
LA N N 16 ? 
MA N N 15 ? 
NA N N 15 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1  UNP PSA2_YEAST       P23639     ? 1  
;MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGP
DYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWK
ATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
;
1  
2  UNP PSA3_YEAST       P23638     ? 2  
;MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGL
TADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGW
KAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
;
1  
3  UNP PSA4_YEAST       P40303     ? 3  
;MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNA
DSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWS
AQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
;
1  
4  UNP PSA5_YEAST       P32379     ? 4  
;MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSG
LTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEP
SGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
;
1  
5  UNP PSA6_YEAST       P40302     ? 5  
;MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPD
ARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTA
IGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
;
1  
6  UNP PSA7_YEAST       P21242     ? 6  
;MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSG
LIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGY
KGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
;
1  
7  UNP PSA1_YEAST       P21243     ? 7  
;MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIG
MVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPA
GYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
;
1  
8  UNP A0A6A5Q449_YEASX A0A6A5Q449 ? 8  
;TIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQ
MLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQA
GIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA
;
31 
9  UNP PSB3_YEAST       P25451     ? 9  
;MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEER
AIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEP
EDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD
;
1  
10 UNP PSB4_YEAST       P22141     ? 10 
;MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV
SSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL
LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDFQAQ
;
1  
11 UNP A0A6A5Q5W3_YEASX A0A6A5Q5W3 ? 11 
;TTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASK
ILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSI
LAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
;
77 
12 UNP PSB6_YEAST       P23724     ? 12 
;QFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHN
DKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQY
EPGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD
;
20 
13 UNP PSB7_YEAST       P30657     ? 13 
;TQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL
KDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFG
AHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKG
YGTQKI
;
21 
14 UNP PSB1_YEAST       P38624     ? 14 
;TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAAS
VFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLS
QAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
;
20 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1  9EY9 A 1 ? 250 ? P23639     1  ? 250 ? 1   250 
2  2  9EY9 B 1 ? 258 ? P23638     1  ? 258 ? 0   257 
3  3  9EY9 C 1 ? 254 ? P40303     1  ? 254 ? -1  252 
4  4  9EY9 D 1 ? 260 ? P32379     1  ? 260 ? -7  252 
5  5  9EY9 E 1 ? 234 ? P40302     1  ? 234 ? 0   233 
6  6  9EY9 F 1 ? 288 ? P21242     1  ? 288 ? -3  284 
7  7  9EY9 G 1 ? 252 ? P21243     1  ? 252 ? -8  243 
8  8  9EY9 H 1 ? 231 ? A0A6A5Q449 31 ? 261 ? 2   232 
9  9  9EY9 I 1 ? 205 ? P25451     1  ? 205 ? 0   204 
10 10 9EY9 J 1 ? 198 ? P22141     1  ? 198 ? 1   198 
11 11 9EY9 K 1 ? 211 ? A0A6A5Q5W3 77 ? 287 ? 2   212 
12 12 9EY9 L 1 ? 222 ? P23724     20 ? 241 ? 1   222 
13 13 9EY9 M 1 ? 246 ? P30657     21 ? 266 ? -12 233 
14 14 9EY9 N 1 ? 196 ? P38624     20 ? 215 ? 1   196 
15 1  9EY9 O 1 ? 250 ? P23639     1  ? 250 ? 1   250 
16 2  9EY9 P 1 ? 258 ? P23638     1  ? 258 ? 0   257 
17 3  9EY9 Q 1 ? 254 ? P40303     1  ? 254 ? -1  252 
18 4  9EY9 R 1 ? 260 ? P32379     1  ? 260 ? -7  252 
19 5  9EY9 S 1 ? 234 ? P40302     1  ? 234 ? 0   233 
20 6  9EY9 T 1 ? 288 ? P21242     1  ? 288 ? -3  284 
21 7  9EY9 U 1 ? 252 ? P21243     1  ? 252 ? -8  243 
22 8  9EY9 V 1 ? 231 ? A0A6A5Q449 31 ? 261 ? 2   232 
23 9  9EY9 W 1 ? 205 ? P25451     1  ? 205 ? 0   204 
24 10 9EY9 X 1 ? 198 ? P22141     1  ? 198 ? 1   198 
25 11 9EY9 Y 1 ? 211 ? A0A6A5Q5W3 77 ? 287 ? 2   212 
26 12 9EY9 Z 1 ? 222 ? P23724     20 ? 241 ? 1   222 
27 13 9EY9 a 1 ? 246 ? P30657     21 ? 266 ? -12 233 
28 14 9EY9 b 1 ? 196 ? P38624     20 ? 215 ? 1   196 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   28-meric 
_pdbx_struct_assembly.oligomeric_count     28 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 123490 ? 
1 MORE         -441   ? 
1 'SSA (A^2)'  215440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'AU contains one biological assembly' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 LEU A  18  ? GLY A  31  ? LEU A 18  GLY A 31  1 ? 14 
HELX_P HELX_P2   AA2 MET A  78  ? SER A  96  ? MET A 78  SER A 96  1 ? 19 
HELX_P HELX_P3   AA3 TYR A  97  ? GLY A  102 ? TYR A 97  GLY A 102 1 ? 6  
HELX_P HELX_P4   AA4 PRO A  106 ? SER A  124 ? PRO A 106 SER A 124 1 ? 19 
HELX_P HELX_P5   AA5 GLY A  167 ? TRP A  179 ? GLY A 167 TRP A 179 1 ? 13 
HELX_P HELX_P6   AA6 GLU A  184 ? VAL A  200 ? GLU A 184 VAL A 200 1 ? 17 
HELX_P HELX_P7   AA7 ASN A  218 ? LEU A  222 ? ASN A 218 LEU A 222 5 ? 5  
HELX_P HELX_P8   AA8 THR A  239 ? LEU A  247 ? THR A 239 LEU A 247 1 ? 9  
HELX_P HELX_P9   AA9 SER B  3   ? ASP B  7   ? SER B 2   ASP B 6   5 ? 5  
HELX_P HELX_P10  AB1 LEU B  19  ? SER B  30  ? LEU B 18  SER B 29  1 ? 12 
HELX_P HELX_P11  AB2 LEU B  80  ? ASN B  103 ? LEU B 79  ASN B 102 1 ? 24 
HELX_P HELX_P12  AB3 PRO B  107 ? HIS B  125 ? PRO B 106 HIS B 124 1 ? 19 
HELX_P HELX_P13  AB4 ASN B  168 ? TYR B  180 ? ASN B 167 TYR B 179 1 ? 13 
HELX_P HELX_P14  AB5 LYS B  185 ? THR B  201 ? LYS B 184 THR B 200 1 ? 17 
HELX_P HELX_P15  AB6 THR B  207 ? ASP B  209 ? THR B 206 ASP B 208 5 ? 3  
HELX_P HELX_P16  AB7 LYS B  231 ? THR B  242 ? LYS B 230 THR B 241 1 ? 12 
HELX_P HELX_P17  AB8 ILE C  17  ? GLY C  30  ? ILE C 15  GLY C 28  1 ? 14 
HELX_P HELX_P18  AB9 LEU C  78  ? GLU C  101 ? LEU C 76  GLU C 99  1 ? 24 
HELX_P HELX_P19  AC1 THR C  105 ? TYR C  120 ? THR C 103 TYR C 118 1 ? 16 
HELX_P HELX_P20  AC2 ASN C  167 ? TYR C  179 ? ASN C 165 TYR C 177 1 ? 13 
HELX_P HELX_P21  AC3 THR C  187 ? GLU C  201 ? THR C 185 GLU C 199 1 ? 15 
HELX_P HELX_P22  AC4 SER C  225 ? GLN C  241 ? SER C 223 GLN C 239 1 ? 17 
HELX_P HELX_P23  AC5 LEU D  21  ? LEU D  33  ? LEU D 13  LEU D 25  1 ? 13 
HELX_P HELX_P24  AC6 GLU D  60  ? ILE D  64  ? GLU D 52  ILE D 56  5 ? 5  
HELX_P HELX_P25  AC7 ASP D  84  ? ASP D  104 ? ASP D 76  ASP D 96  1 ? 21 
HELX_P HELX_P26  AC8 ASN D  108 ? LEU D  121 ? ASN D 100 LEU D 113 1 ? 14 
HELX_P HELX_P27  AC9 GLY D  175 ? TRP D  187 ? GLY D 167 TRP D 179 1 ? 13 
HELX_P HELX_P28  AD1 THR D  192 ? MET D  208 ? THR D 184 MET D 200 1 ? 17 
HELX_P HELX_P29  AD2 ASP D  232 ? ALA D  249 ? ASP D 224 ALA D 241 1 ? 18 
HELX_P HELX_P30  AD3 LEU E  19  ? GLY E  32  ? LEU E 18  GLY E 31  1 ? 14 
HELX_P HELX_P31  AD4 LEU E  77  ? ASN E  100 ? LEU E 76  ASN E 99  1 ? 24 
HELX_P HELX_P32  AD5 ALA E  104 ? ASN E  119 ? ALA E 103 ASN E 118 1 ? 16 
HELX_P HELX_P33  AD6 ARG E  164 ? ILE E  180 ? ARG E 163 ILE E 179 1 ? 17 
HELX_P HELX_P34  AD7 ASN E  185 ? SER E  198 ? ASN E 184 SER E 197 1 ? 14 
HELX_P HELX_P35  AD8 GLN E  199 ? LEU E  201 ? GLN E 198 LEU E 200 5 ? 3  
HELX_P HELX_P36  AD9 ASP E  226 ? ILE E  234 ? ASP E 225 ILE E 233 5 ? 9  
HELX_P HELX_P37  AE1 ASN F  21  ? GLY F  34  ? ASN F 17  GLY F 30  1 ? 14 
HELX_P HELX_P38  AE2 LEU F  81  ? LYS F  104 ? LEU F 77  LYS F 100 1 ? 24 
HELX_P HELX_P39  AE3 PRO F  108 ? HIS F  123 ? PRO F 104 HIS F 119 1 ? 16 
HELX_P HELX_P40  AE4 GLY F  168 ? HIS F  183 ? GLY F 164 HIS F 179 1 ? 16 
HELX_P HELX_P41  AE5 SER F  188 ? HIS F  204 ? SER F 184 HIS F 200 1 ? 17 
HELX_P HELX_P42  AE6 GLU F  205 ? LYS F  208 ? GLU F 201 LYS F 204 5 ? 4  
HELX_P HELX_P43  AE7 GLY F  233 ? ASN F  248 ? GLY F 229 ASN F 244 1 ? 16 
HELX_P HELX_P44  AE8 GLY G  11  ? HIS G  15  ? GLY G 2   HIS G 6   5 ? 5  
HELX_P HELX_P45  AE9 LEU G  25  ? THR G  35  ? LEU G 16  THR G 26  1 ? 11 
HELX_P HELX_P46  AF1 ASN G  36  ? ASN G  39  ? ASN G 27  ASN G 30  5 ? 4  
HELX_P HELX_P47  AF2 ASP G  65  ? VAL G  69  ? ASP G 56  VAL G 60  5 ? 5  
HELX_P HELX_P48  AF3 PRO G  86  ? GLY G  109 ? PRO G 77  GLY G 100 1 ? 24 
HELX_P HELX_P49  AF4 PRO G  113 ? ARG G  131 ? PRO G 104 ARG G 122 1 ? 19 
HELX_P HELX_P50  AF5 LYS G  174 ? LYS G  190 ? LYS G 165 LYS G 181 1 ? 17 
HELX_P HELX_P51  AF6 SER G  198 ? GLY G  215 ? SER G 189 GLY G 206 1 ? 18 
HELX_P HELX_P52  AF7 SER G  237 ? GLU G  250 ? SER G 228 GLU G 241 1 ? 14 
HELX_P HELX_P53  AF8 THR H  47  ? SER H  70  ? THR H 48  SER H 71  1 ? 24 
HELX_P HELX_P54  AF9 ARG H  74  ? TYR H  89  ? ARG H 75  TYR H 90  1 ? 16 
HELX_P HELX_P55  AG1 GLY H  129 ? TRP H  141 ? GLY H 130 TRP H 142 1 ? 13 
HELX_P HELX_P56  AG2 THR H  146 ? ASP H  165 ? THR H 147 ASP H 166 1 ? 20 
HELX_P HELX_P57  AG3 ASP I  3   ? ILE I  7   ? ASP I 2   ILE I 6   5 ? 5  
HELX_P HELX_P58  AG4 LEU I  56  ? GLU I  79  ? LEU I 55  GLU I 78  1 ? 24 
HELX_P HELX_P59  AG5 GLU I  83  ? GLU I  97  ? GLU I 82  GLU I 96  1 ? 15 
HELX_P HELX_P60  AG6 ALA I  142 ? TYR I  154 ? ALA I 141 TYR I 153 1 ? 13 
HELX_P HELX_P61  AG7 GLU I  159 ? ASP I  176 ? GLU I 158 ASP I 175 1 ? 18 
HELX_P HELX_P62  AG8 GLY J  51  ? ASP J  72  ? GLY J 51  ASP J 72  1 ? 22 
HELX_P HELX_P63  AG9 SER J  76  ? ILE J  92  ? SER J 76  ILE J 92  1 ? 17 
HELX_P HELX_P64  AH1 SER J  136 ? TYR J  148 ? SER J 136 TYR J 148 1 ? 13 
HELX_P HELX_P65  AH2 THR J  153 ? MET J  172 ? THR J 153 MET J 172 1 ? 20 
HELX_P HELX_P66  AH3 GLY K  47  ? LYS K  70  ? GLY K 48  LYS K 71  1 ? 24 
HELX_P HELX_P67  AH4 SER K  74  ? TYR K  89  ? SER K 75  TYR K 90  1 ? 16 
HELX_P HELX_P68  AH5 GLY K  131 ? SER K  141 ? GLY K 132 SER K 142 1 ? 11 
HELX_P HELX_P69  AH6 SER K  148 ? ASP K  167 ? SER K 149 ASP K 168 1 ? 20 
HELX_P HELX_P70  AH7 VAL K  192 ? GLY K  204 ? VAL K 193 GLY K 205 1 ? 13 
HELX_P HELX_P71  AH8 PHE L  57  ? HIS L  79  ? PHE L 57  HIS L 79  1 ? 23 
HELX_P HELX_P72  AH9 SER L  85  ? GLY L  99  ? SER L 85  GLY L 99  1 ? 15 
HELX_P HELX_P73  AI1 ALA L  142 ? VAL L  154 ? ALA L 142 VAL L 154 1 ? 13 
HELX_P HELX_P74  AI2 SER L  176 ? HIS L  195 ? SER L 176 HIS L 195 1 ? 20 
HELX_P HELX_P75  AI3 ILE M  70  ? TYR M  89  ? ILE M 57  TYR M 76  1 ? 20 
HELX_P HELX_P76  AI4 GLU M  101 ? LYS M  119 ? GLU M 88  LYS M 106 1 ? 19 
HELX_P HELX_P77  AI5 PHE M  159 ? ARG M  169 ? PHE M 146 ARG M 156 1 ? 11 
HELX_P HELX_P78  AI6 ARG M  174 ? ILE M  178 ? ARG M 161 ILE M 165 5 ? 5  
HELX_P HELX_P79  AI7 THR M  182 ? ASP M  201 ? THR M 169 ASP M 188 1 ? 20 
HELX_P HELX_P80  AI8 TRP M  232 ? ILE M  238 ? TRP M 219 ILE M 225 5 ? 7  
HELX_P HELX_P81  AI9 SER N  48  ? GLY N  71  ? SER N 48  GLY N 71  1 ? 24 
HELX_P HELX_P82  AJ1 SER N  74  ? ASN N  89  ? SER N 74  ASN N 89  1 ? 16 
HELX_P HELX_P83  AJ2 LYS N  90  ? LEU N  93  ? LYS N 90  LEU N 93  5 ? 4  
HELX_P HELX_P84  AJ3 GLY N  128 ? PHE N  133 ? GLY N 128 PHE N 133 5 ? 6  
HELX_P HELX_P85  AJ4 ILE N  134 ? PHE N  142 ? ILE N 134 PHE N 142 1 ? 9  
HELX_P HELX_P86  AJ5 SER N  147 ? ASP N  166 ? SER N 147 ASP N 166 1 ? 20 
HELX_P HELX_P87  AJ6 TYR N  189 ? GLU N  194 ? TYR N 189 GLU N 194 1 ? 6  
HELX_P HELX_P88  AJ7 LEU O  18  ? GLY O  31  ? LEU O 18  GLY O 31  1 ? 14 
HELX_P HELX_P89  AJ8 MET O  78  ? SER O  96  ? MET O 78  SER O 96  1 ? 19 
HELX_P HELX_P90  AJ9 TYR O  97  ? GLY O  102 ? TYR O 97  GLY O 102 1 ? 6  
HELX_P HELX_P91  AK1 PRO O  106 ? SER O  124 ? PRO O 106 SER O 124 1 ? 19 
HELX_P HELX_P92  AK2 GLY O  167 ? TRP O  179 ? GLY O 167 TRP O 179 1 ? 13 
HELX_P HELX_P93  AK3 GLU O  184 ? VAL O  200 ? GLU O 184 VAL O 200 1 ? 17 
HELX_P HELX_P94  AK4 ASN O  218 ? LEU O  222 ? ASN O 218 LEU O 222 5 ? 5  
HELX_P HELX_P95  AK5 THR O  239 ? LEU O  247 ? THR O 239 LEU O 247 1 ? 9  
HELX_P HELX_P96  AK6 SER P  3   ? ASP P  7   ? SER P 2   ASP P 6   5 ? 5  
HELX_P HELX_P97  AK7 LEU P  19  ? SER P  30  ? LEU P 18  SER P 29  1 ? 12 
HELX_P HELX_P98  AK8 LEU P  80  ? ASN P  103 ? LEU P 79  ASN P 102 1 ? 24 
HELX_P HELX_P99  AK9 PRO P  107 ? HIS P  125 ? PRO P 106 HIS P 124 1 ? 19 
HELX_P HELX_P100 AL1 ASN P  168 ? TYR P  180 ? ASN P 167 TYR P 179 1 ? 13 
HELX_P HELX_P101 AL2 LYS P  185 ? THR P  201 ? LYS P 184 THR P 200 1 ? 17 
HELX_P HELX_P102 AL3 THR P  207 ? ASP P  209 ? THR P 206 ASP P 208 5 ? 3  
HELX_P HELX_P103 AL4 LYS P  231 ? THR P  242 ? LYS P 230 THR P 241 1 ? 12 
HELX_P HELX_P104 AL5 ILE Q  17  ? GLY Q  30  ? ILE Q 15  GLY Q 28  1 ? 14 
HELX_P HELX_P105 AL6 LEU Q  78  ? GLU Q  101 ? LEU Q 76  GLU Q 99  1 ? 24 
HELX_P HELX_P106 AL7 THR Q  105 ? TYR Q  120 ? THR Q 103 TYR Q 118 1 ? 16 
HELX_P HELX_P107 AL8 ASN Q  167 ? TYR Q  179 ? ASN Q 165 TYR Q 177 1 ? 13 
HELX_P HELX_P108 AL9 THR Q  187 ? GLU Q  201 ? THR Q 185 GLU Q 199 1 ? 15 
HELX_P HELX_P109 AM1 SER Q  225 ? GLN Q  241 ? SER Q 223 GLN Q 239 1 ? 17 
HELX_P HELX_P110 AM2 LEU R  21  ? LEU R  33  ? LEU R 13  LEU R 25  1 ? 13 
HELX_P HELX_P111 AM3 GLU R  60  ? ILE R  64  ? GLU R 52  ILE R 56  5 ? 5  
HELX_P HELX_P112 AM4 ASP R  84  ? ASP R  104 ? ASP R 76  ASP R 96  1 ? 21 
HELX_P HELX_P113 AM5 ASN R  108 ? LEU R  121 ? ASN R 100 LEU R 113 1 ? 14 
HELX_P HELX_P114 AM6 GLY R  175 ? TRP R  187 ? GLY R 167 TRP R 179 1 ? 13 
HELX_P HELX_P115 AM7 THR R  192 ? MET R  208 ? THR R 184 MET R 200 1 ? 17 
HELX_P HELX_P116 AM8 ASP R  232 ? ALA R  249 ? ASP R 224 ALA R 241 1 ? 18 
HELX_P HELX_P117 AM9 LEU S  19  ? GLY S  32  ? LEU S 18  GLY S 31  1 ? 14 
HELX_P HELX_P118 AN1 LEU S  77  ? ASN S  100 ? LEU S 76  ASN S 99  1 ? 24 
HELX_P HELX_P119 AN2 ALA S  104 ? ASN S  119 ? ALA S 103 ASN S 118 1 ? 16 
HELX_P HELX_P120 AN3 ARG S  164 ? ILE S  180 ? ARG S 163 ILE S 179 1 ? 17 
HELX_P HELX_P121 AN4 ASN S  185 ? SER S  198 ? ASN S 184 SER S 197 1 ? 14 
HELX_P HELX_P122 AN5 GLN S  199 ? LEU S  201 ? GLN S 198 LEU S 200 5 ? 3  
HELX_P HELX_P123 AN6 ASP S  226 ? ILE S  234 ? ASP S 225 ILE S 233 5 ? 9  
HELX_P HELX_P124 AN7 ASN T  21  ? GLY T  34  ? ASN T 17  GLY T 30  1 ? 14 
HELX_P HELX_P125 AN8 LEU T  81  ? LYS T  104 ? LEU T 77  LYS T 100 1 ? 24 
HELX_P HELX_P126 AN9 PRO T  108 ? HIS T  123 ? PRO T 104 HIS T 119 1 ? 16 
HELX_P HELX_P127 AO1 GLY T  168 ? HIS T  183 ? GLY T 164 HIS T 179 1 ? 16 
HELX_P HELX_P128 AO2 SER T  188 ? ALA T  203 ? SER T 184 ALA T 199 1 ? 16 
HELX_P HELX_P129 AO3 HIS T  204 ? LYS T  208 ? HIS T 200 LYS T 204 5 ? 5  
HELX_P HELX_P130 AO4 GLY T  233 ? ASN T  248 ? GLY T 229 ASN T 244 1 ? 16 
HELX_P HELX_P131 AO5 GLY U  11  ? HIS U  15  ? GLY U 2   HIS U 6   5 ? 5  
HELX_P HELX_P132 AO6 LEU U  25  ? THR U  35  ? LEU U 16  THR U 26  1 ? 11 
HELX_P HELX_P133 AO7 ASP U  65  ? VAL U  69  ? ASP U 56  VAL U 60  5 ? 5  
HELX_P HELX_P134 AO8 PRO U  86  ? GLY U  109 ? PRO U 77  GLY U 100 1 ? 24 
HELX_P HELX_P135 AO9 PRO U  113 ? ARG U  131 ? PRO U 104 ARG U 122 1 ? 19 
HELX_P HELX_P136 AP1 LYS U  174 ? LYS U  190 ? LYS U 165 LYS U 181 1 ? 17 
HELX_P HELX_P137 AP2 SER U  198 ? GLY U  215 ? SER U 189 GLY U 206 1 ? 18 
HELX_P HELX_P138 AP3 SER U  237 ? GLU U  250 ? SER U 228 GLU U 241 1 ? 14 
HELX_P HELX_P139 AP4 THR V  47  ? SER V  70  ? THR V 48  SER V 71  1 ? 24 
HELX_P HELX_P140 AP5 ARG V  74  ? TYR V  89  ? ARG V 75  TYR V 90  1 ? 16 
HELX_P HELX_P141 AP6 GLY V  129 ? TRP V  141 ? GLY V 130 TRP V 142 1 ? 13 
HELX_P HELX_P142 AP7 THR V  146 ? ASP V  165 ? THR V 147 ASP V 166 1 ? 20 
HELX_P HELX_P143 AP8 ASP W  3   ? ILE W  7   ? ASP W 2   ILE W 6   5 ? 5  
HELX_P HELX_P144 AP9 LEU W  56  ? GLU W  79  ? LEU W 55  GLU W 78  1 ? 24 
HELX_P HELX_P145 AQ1 GLU W  83  ? GLU W  97  ? GLU W 82  GLU W 96  1 ? 15 
HELX_P HELX_P146 AQ2 ALA W  142 ? TYR W  154 ? ALA W 141 TYR W 153 1 ? 13 
HELX_P HELX_P147 AQ3 GLU W  159 ? ASP W  176 ? GLU W 158 ASP W 175 1 ? 18 
HELX_P HELX_P148 AQ4 GLY X  51  ? ASP X  72  ? GLY X 51  ASP X 72  1 ? 22 
HELX_P HELX_P149 AQ5 SER X  76  ? ILE X  92  ? SER X 76  ILE X 92  1 ? 17 
HELX_P HELX_P150 AQ6 SER X  136 ? TYR X  148 ? SER X 136 TYR X 148 1 ? 13 
HELX_P HELX_P151 AQ7 THR X  153 ? MET X  172 ? THR X 153 MET X 172 1 ? 20 
HELX_P HELX_P152 AQ8 GLY Y  47  ? LYS Y  70  ? GLY Y 48  LYS Y 71  1 ? 24 
HELX_P HELX_P153 AQ9 SER Y  74  ? TYR Y  89  ? SER Y 75  TYR Y 90  1 ? 16 
HELX_P HELX_P154 AR1 GLY Y  131 ? SER Y  141 ? GLY Y 132 SER Y 142 1 ? 11 
HELX_P HELX_P155 AR2 SER Y  148 ? ASP Y  167 ? SER Y 149 ASP Y 168 1 ? 20 
HELX_P HELX_P156 AR3 VAL Y  192 ? GLY Y  204 ? VAL Y 193 GLY Y 205 1 ? 13 
HELX_P HELX_P157 AR4 PHE Z  57  ? HIS Z  79  ? PHE Z 57  HIS Z 79  1 ? 23 
HELX_P HELX_P158 AR5 SER Z  85  ? GLY Z  99  ? SER Z 85  GLY Z 99  1 ? 15 
HELX_P HELX_P159 AR6 ALA Z  142 ? VAL Z  154 ? ALA Z 142 VAL Z 154 1 ? 13 
HELX_P HELX_P160 AR7 SER Z  176 ? HIS Z  195 ? SER Z 176 HIS Z 195 1 ? 20 
HELX_P HELX_P161 AR8 ILE AA 70  ? TYR AA 89  ? ILE a 57  TYR a 76  1 ? 20 
HELX_P HELX_P162 AR9 GLU AA 101 ? LYS AA 119 ? GLU a 88  LYS a 106 1 ? 19 
HELX_P HELX_P163 AS1 PHE AA 159 ? ARG AA 169 ? PHE a 146 ARG a 156 1 ? 11 
HELX_P HELX_P164 AS2 ARG AA 174 ? ILE AA 178 ? ARG a 161 ILE a 165 5 ? 5  
HELX_P HELX_P165 AS3 THR AA 182 ? ASP AA 201 ? THR a 169 ASP a 188 1 ? 20 
HELX_P HELX_P166 AS4 TRP AA 232 ? ILE AA 238 ? TRP a 219 ILE a 225 5 ? 7  
HELX_P HELX_P167 AS5 SER BA 48  ? GLY BA 71  ? SER b 48  GLY b 71  1 ? 24 
HELX_P HELX_P168 AS6 SER BA 74  ? ASN BA 89  ? SER b 74  ASN b 89  1 ? 16 
HELX_P HELX_P169 AS7 LYS BA 90  ? LEU BA 93  ? LYS b 90  LEU b 93  5 ? 4  
HELX_P HELX_P170 AS8 GLY BA 128 ? PHE BA 133 ? GLY b 128 PHE b 133 5 ? 6  
HELX_P HELX_P171 AS9 ILE BA 134 ? PHE BA 142 ? ILE b 134 PHE b 142 1 ? 9  
HELX_P HELX_P172 AT1 SER BA 147 ? ASP BA 166 ? SER b 147 ASP b 166 1 ? 20 
HELX_P HELX_P173 AT2 TYR BA 189 ? GLU BA 194 ? TYR b 189 GLU b 194 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale one ? H  THR 1   N   ? ? ? 1_555 DA A1H71 .   C  ? ? H THR 2   H A1H71 301 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2  covale one ? K  THR 1   N   ? ? ? 1_555 GA A1H71 .   C  ? ? K THR 2   K A1H71 301 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale3  covale one ? V  THR 1   N   ? ? ? 1_555 JA A1H71 .   C  ? ? V THR 2   V A1H71 301 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale4  covale one ? Y  THR 1   N   ? ? ? 1_555 LA A1H71 .   C  ? ? Y THR 2   Y A1H71 301 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
metalc1  metalc ?   ? G  THR 17  OG1 ? ? ? 1_555 CA MG    .   MG ? ? G THR 8   G MG    301 1_555 ? ? ? ? ? ? ? 2.607 ? ? 
metalc2  metalc ?   ? G  TYR 128 O   ? ? ? 1_555 CA MG    .   MG ? ? G TYR 119 G MG    301 1_555 ? ? ? ? ? ? ? 2.900 ? ? 
metalc3  metalc ?   ? G  ARG 131 O   ? ? ? 1_555 CA MG    .   MG ? ? G ARG 122 G MG    301 1_555 ? ? ? ? ? ? ? 2.777 ? ? 
metalc4  metalc ?   ? G  MET 134 O   ? ? ? 1_555 CA MG    .   MG ? ? G MET 125 G MG    301 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc5  metalc ?   ? H  GLN 90  OE1 ? ? ? 1_555 EA MG    .   MG ? ? H GLN 91  H MG    302 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc6  metalc ?   ? I  SER 181 O   ? ? ? 1_555 FA MG    .   MG ? ? I SER 180 I MG    301 1_555 ? ? ? ? ? ? ? 2.488 ? ? 
metalc7  metalc ?   ? I  ASP 205 O   ? ? ? 1_555 MA MG    .   MG ? ? I ASP 204 Y MG    302 1_555 ? ? ? ? ? ? ? 2.879 ? ? 
metalc8  metalc ?   ? K  ALA 164 O   ? ? ? 1_555 HA MG    .   MG ? ? K ALA 165 K MG    302 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc9  metalc ?   ? K  ASP 167 O   ? ? ? 1_555 HA MG    .   MG ? ? K ASP 168 K MG    302 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc10 metalc ?   ? K  SER 170 O   ? ? ? 1_555 HA MG    .   MG ? ? K SER 171 K MG    302 1_555 ? ? ? ? ? ? ? 2.841 ? ? 
metalc11 metalc ?   ? HA MG  .   MG  ? ? ? 1_555 W  ASP   205 O  ? ? K MG  302 W ASP   204 1_555 ? ? ? ? ? ? ? 2.604 ? ? 
metalc12 metalc ?   ? L  ASP 222 OXT ? ? ? 1_555 KA MG    .   MG ? ? L ASP 222 V MG    302 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc13 metalc ?   ? N  ILE 163 O   ? ? ? 1_555 IA MG    .   MG ? ? N ILE 163 N MG    201 1_555 ? ? ? ? ? ? ? 2.659 ? ? 
metalc14 metalc ?   ? N  SER 169 O   ? ? ? 1_555 IA MG    .   MG ? ? N SER 169 N MG    201 1_555 ? ? ? ? ? ? ? 2.996 ? ? 
metalc15 metalc ?   ? V  ILE 162 O   ? ? ? 1_555 KA MG    .   MG ? ? V ILE 163 V MG    302 1_555 ? ? ? ? ? ? ? 2.588 ? ? 
metalc16 metalc ?   ? V  ASP 165 O   ? ? ? 1_555 KA MG    .   MG ? ? V ASP 166 V MG    302 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc17 metalc ?   ? Y  ALA 164 O   ? ? ? 1_555 MA MG    .   MG ? ? Y ALA 165 Y MG    302 1_555 ? ? ? ? ? ? ? 2.791 ? ? 
metalc18 metalc ?   ? Y  ASP 167 O   ? ? ? 1_555 MA MG    .   MG ? ? Y ASP 168 Y MG    302 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc19 metalc ?   ? Z  VAL 198 O   ? ? ? 1_555 NA MG    .   MG ? ? Z VAL 198 Z MG    301 1_555 ? ? ? ? ? ? ? 2.951 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? G THR 17  ? G THR 8   ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G TYR 128 ? G TYR 119 ? 1_555 75.0  ? 
2  OG1 ? G THR 17  ? G THR 8   ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G ARG 131 ? G ARG 122 ? 1_555 73.2  ? 
3  O   ? G TYR 128 ? G TYR 119 ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G ARG 131 ? G ARG 122 ? 1_555 63.8  ? 
4  OG1 ? G THR 17  ? G THR 8   ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G MET 134 ? G MET 125 ? 1_555 149.0 ? 
5  O   ? G TYR 128 ? G TYR 119 ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G MET 134 ? G MET 125 ? 1_555 77.2  ? 
6  O   ? G ARG 131 ? G ARG 122 ? 1_555 MG ? CA MG . ? G MG 301 ? 1_555 O ? G MET 134 ? G MET 125 ? 1_555 82.5  ? 
7  O   ? I ASP 205 ? I ASP 204 ? 1_555 MG ? MA MG . ? Y MG 302 ? 1_555 O ? Y ALA 164 ? Y ALA 165 ? 1_555 86.5  ? 
8  O   ? I ASP 205 ? I ASP 204 ? 1_555 MG ? MA MG . ? Y MG 302 ? 1_555 O ? Y ASP 167 ? Y ASP 168 ? 1_555 126.1 ? 
9  O   ? Y ALA 164 ? Y ALA 165 ? 1_555 MG ? MA MG . ? Y MG 302 ? 1_555 O ? Y ASP 167 ? Y ASP 168 ? 1_555 76.1  ? 
10 O   ? K ALA 164 ? K ALA 165 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? K ASP 167 ? K ASP 168 ? 1_555 101.2 ? 
11 O   ? K ALA 164 ? K ALA 165 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? K SER 170 ? K SER 171 ? 1_555 76.6  ? 
12 O   ? K ASP 167 ? K ASP 168 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? K SER 170 ? K SER 171 ? 1_555 78.0  ? 
13 O   ? K ALA 164 ? K ALA 165 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? W ASP 205 ? W ASP 204 ? 1_555 99.9  ? 
14 O   ? K ASP 167 ? K ASP 168 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? W ASP 205 ? W ASP 204 ? 1_555 149.0 ? 
15 O   ? K SER 170 ? K SER 171 ? 1_555 MG ? HA MG . ? K MG 302 ? 1_555 O ? W ASP 205 ? W ASP 204 ? 1_555 85.1  ? 
16 OXT ? L ASP 222 ? L ASP 222 ? 1_555 MG ? KA MG . ? V MG 302 ? 1_555 O ? V ILE 162 ? V ILE 163 ? 1_555 77.0  ? 
17 OXT ? L ASP 222 ? L ASP 222 ? 1_555 MG ? KA MG . ? V MG 302 ? 1_555 O ? V ASP 165 ? V ASP 166 ? 1_555 114.5 ? 
18 O   ? V ILE 162 ? V ILE 163 ? 1_555 MG ? KA MG . ? V MG 302 ? 1_555 O ? V ASP 165 ? V ASP 166 ? 1_555 96.1  ? 
19 O   ? N ILE 163 ? N ILE 163 ? 1_555 MG ? IA MG . ? N MG 201 ? 1_555 O ? N SER 169 ? N SER 169 ? 1_555 83.4  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1H71 DA . ? THR H 1 ? A1H71 H 301 ? 1_555 THR H 2 ? 1_555 C N THR 1 A1H71 None 'Covalent chemical modification' 
2 A1H71 GA . ? THR K 1 ? A1H71 K 301 ? 1_555 THR K 2 ? 1_555 C N THR 1 A1H71 None 'Covalent chemical modification' 
3 A1H71 JA . ? THR V 1 ? A1H71 V 301 ? 1_555 THR V 2 ? 1_555 C N THR 1 A1H71 None 'Covalent chemical modification' 
4 A1H71 LA . ? THR Y 1 ? A1H71 Y 301 ? 1_555 THR Y 2 ? 1_555 C N THR 1 A1H71 None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 5 ? 
AA8 ? 5 ? 
AA9 ? 5 ? 
AB1 ? 5 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 2 ? 
AB8 ? 5 ? 
AB9 ? 6 ? 
AC1 ? 2 ? 
AC2 ? 5 ? 
AC3 ? 5 ? 
AC4 ? 2 ? 
AC5 ? 5 ? 
AC6 ? 5 ? 
AC7 ? 2 ? 
AC8 ? 5 ? 
AC9 ? 5 ? 
AD1 ? 2 ? 
AD2 ? 5 ? 
AD3 ? 5 ? 
AD4 ? 7 ? 
AD5 ? 5 ? 
AD6 ? 5 ? 
AD7 ? 2 ? 
AD8 ? 5 ? 
AD9 ? 5 ? 
AE1 ? 6 ? 
AE2 ? 5 ? 
AE3 ? 6 ? 
AE4 ? 5 ? 
AE5 ? 5 ? 
AE6 ? 5 ? 
AE7 ? 5 ? 
AE8 ? 5 ? 
AE9 ? 5 ? 
AF1 ? 5 ? 
AF2 ? 5 ? 
AF3 ? 5 ? 
AF4 ? 5 ? 
AF5 ? 5 ? 
AF6 ? 2 ? 
AF7 ? 5 ? 
AF8 ? 6 ? 
AF9 ? 2 ? 
AG1 ? 5 ? 
AG2 ? 5 ? 
AG3 ? 2 ? 
AG4 ? 5 ? 
AG5 ? 5 ? 
AG6 ? 2 ? 
AG7 ? 5 ? 
AG8 ? 5 ? 
AG9 ? 2 ? 
AH1 ? 5 ? 
AH2 ? 5 ? 
AH3 ? 7 ? 
AH4 ? 5 ? 
AH5 ? 5 ? 
AH6 ? 2 ? 
AH7 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC2 4 5 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC3 4 5 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC6 4 5 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AC9 4 5 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD2 4 5 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD3 4 5 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD4 4 5 ? anti-parallel 
AD4 5 6 ? anti-parallel 
AD4 6 7 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD5 4 5 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD6 4 5 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD8 4 5 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AD9 4 5 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE1 4 5 ? anti-parallel 
AE1 5 6 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE2 4 5 ? anti-parallel 
AE3 1 2 ? parallel      
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE3 4 5 ? anti-parallel 
AE3 5 6 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE4 4 5 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE5 4 5 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE6 4 5 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? anti-parallel 
AE7 4 5 ? anti-parallel 
AE8 1 2 ? anti-parallel 
AE8 2 3 ? anti-parallel 
AE8 3 4 ? anti-parallel 
AE8 4 5 ? anti-parallel 
AE9 1 2 ? anti-parallel 
AE9 2 3 ? anti-parallel 
AE9 3 4 ? anti-parallel 
AE9 4 5 ? anti-parallel 
AF1 1 2 ? anti-parallel 
AF1 2 3 ? anti-parallel 
AF1 3 4 ? anti-parallel 
AF1 4 5 ? anti-parallel 
AF2 1 2 ? anti-parallel 
AF2 2 3 ? anti-parallel 
AF2 3 4 ? anti-parallel 
AF2 4 5 ? anti-parallel 
AF3 1 2 ? anti-parallel 
AF3 2 3 ? anti-parallel 
AF3 3 4 ? anti-parallel 
AF3 4 5 ? anti-parallel 
AF4 1 2 ? anti-parallel 
AF4 2 3 ? anti-parallel 
AF4 3 4 ? anti-parallel 
AF4 4 5 ? anti-parallel 
AF5 1 2 ? anti-parallel 
AF5 2 3 ? anti-parallel 
AF5 3 4 ? anti-parallel 
AF5 4 5 ? anti-parallel 
AF6 1 2 ? anti-parallel 
AF7 1 2 ? anti-parallel 
AF7 2 3 ? anti-parallel 
AF7 3 4 ? anti-parallel 
AF7 4 5 ? anti-parallel 
AF8 1 2 ? anti-parallel 
AF8 2 3 ? anti-parallel 
AF8 3 4 ? anti-parallel 
AF8 4 5 ? anti-parallel 
AF8 5 6 ? anti-parallel 
AF9 1 2 ? anti-parallel 
AG1 1 2 ? anti-parallel 
AG1 2 3 ? anti-parallel 
AG1 3 4 ? anti-parallel 
AG1 4 5 ? anti-parallel 
AG2 1 2 ? anti-parallel 
AG2 2 3 ? anti-parallel 
AG2 3 4 ? anti-parallel 
AG2 4 5 ? anti-parallel 
AG3 1 2 ? anti-parallel 
AG4 1 2 ? anti-parallel 
AG4 2 3 ? anti-parallel 
AG4 3 4 ? anti-parallel 
AG4 4 5 ? anti-parallel 
AG5 1 2 ? anti-parallel 
AG5 2 3 ? anti-parallel 
AG5 3 4 ? anti-parallel 
AG5 4 5 ? anti-parallel 
AG6 1 2 ? anti-parallel 
AG7 1 2 ? anti-parallel 
AG7 2 3 ? anti-parallel 
AG7 3 4 ? anti-parallel 
AG7 4 5 ? anti-parallel 
AG8 1 2 ? anti-parallel 
AG8 2 3 ? anti-parallel 
AG8 3 4 ? anti-parallel 
AG8 4 5 ? anti-parallel 
AG9 1 2 ? anti-parallel 
AH1 1 2 ? anti-parallel 
AH1 2 3 ? anti-parallel 
AH1 3 4 ? anti-parallel 
AH1 4 5 ? anti-parallel 
AH2 1 2 ? anti-parallel 
AH2 2 3 ? anti-parallel 
AH2 3 4 ? anti-parallel 
AH2 4 5 ? anti-parallel 
AH3 1 2 ? anti-parallel 
AH3 2 3 ? anti-parallel 
AH3 3 4 ? anti-parallel 
AH3 4 5 ? anti-parallel 
AH3 5 6 ? anti-parallel 
AH3 6 7 ? anti-parallel 
AH4 1 2 ? anti-parallel 
AH4 2 3 ? anti-parallel 
AH4 3 4 ? anti-parallel 
AH4 4 5 ? anti-parallel 
AH5 1 2 ? anti-parallel 
AH5 2 3 ? anti-parallel 
AH5 3 4 ? anti-parallel 
AH5 4 5 ? anti-parallel 
AH6 1 2 ? anti-parallel 
AH7 1 2 ? anti-parallel 
AH7 2 3 ? anti-parallel 
AH7 3 4 ? anti-parallel 
AH7 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A  161 ? ILE A  164 ? ALA A 161 ILE A 164 
AA1 2 SER A  34  ? LYS A  38  ? SER A 34  LYS A 38  
AA1 3 VAL A  43  ? GLU A  48  ? VAL A 43  GLU A 48  
AA1 4 ILE A  209 ? ILE A  214 ? ILE A 209 ILE A 214 
AA1 5 PHE A  235 ? LYS A  237 ? PHE A 235 LYS A 237 
AA2 1 SER A  65  ? THR A  68  ? SER A 65  THR A 68  
AA2 2 ILE A  71  ? GLY A  77  ? ILE A 71  GLY A 77  
AA2 3 VAL A  132 ? ASP A  140 ? VAL A 132 ASP A 140 
AA2 4 GLY A  144 ? VAL A  150 ? GLY A 144 VAL A 150 
AA2 5 TYR A  156 ? PRO A  158 ? TYR A 156 PRO A 158 
AA3 1 TYR A  224 ? THR A  225 ? TYR A 224 THR A 225 
AA3 2 ALA H  183 ? LEU H  190 ? ALA H 184 LEU H 191 
AA3 3 VAL H  172 ? GLU H  178 ? VAL H 173 GLU H 179 
AA3 4 GLY H  10  ? ASP H  16  ? GLY H 11  ASP H 17  
AA3 5 ILE H  2   ? LYS H  6   ? ILE H 3   LYS H 7   
AA3 6 TYR H  123 ? LEU H  126 ? TYR H 124 LEU H 127 
AA4 1 ALA B  162 ? VAL B  165 ? ALA B 161 VAL B 164 
AA4 2 ALA B  35  ? ALA B  40  ? ALA B 34  ALA B 39  
AA4 3 GLY B  43  ? GLU B  49  ? GLY B 42  GLU B 48  
AA4 4 LEU B  211 ? ARG B  217 ? LEU B 210 ARG B 216 
AA4 5 TYR B  226 ? ILE B  229 ? TYR B 225 ILE B 228 
AA5 1 LEU B  66  ? ASN B  70  ? LEU B 65  ASN B 69  
AA5 2 ILE B  73  ? GLY B  79  ? ILE B 72  GLY B 78  
AA5 3 VAL B  133 ? ASP B  141 ? VAL B 132 ASP B 140 
AA5 4 GLY B  145 ? SER B  151 ? GLY B 144 SER B 150 
AA5 5 TYR B  157 ? TRP B  160 ? TYR B 156 TRP B 159 
AA6 1 ALA C  161 ? ILE C  164 ? ALA C 159 ILE C 162 
AA6 2 ALA C  33  ? LYS C  37  ? ALA C 31  LYS C 35  
AA6 3 VAL C  42  ? GLU C  47  ? VAL C 40  GLU C 45  
AA6 4 ILE C  210 ? LYS C  216 ? ILE C 208 LYS C 214 
AA6 5 ASP C  220 ? ALA C  223 ? ASP C 218 ALA C 221 
AA7 1 SER C  65  ? LYS C  66  ? SER C 63  LYS C 64  
AA7 2 VAL C  71  ? GLY C  77  ? VAL C 69  GLY C 75  
AA7 3 VAL C  131 ? GLY C  137 ? VAL C 129 GLY C 135 
AA7 4 LYS C  146 ? THR C  150 ? LYS C 144 THR C 148 
AA7 5 TYR C  156 ? SER C  158 ? TYR C 154 SER C 156 
AA8 1 ALA D  169 ? ILE D  172 ? ALA D 161 ILE D 164 
AA8 2 ALA D  37  ? ALA D  41  ? ALA D 29  ALA D 33  
AA8 3 VAL D  46  ? GLU D  51  ? VAL D 38  GLU D 43  
AA8 4 ALA D  217 ? THR D  223 ? ALA D 209 THR D 215 
AA8 5 GLY D  227 ? ILE D  230 ? GLY D 219 ILE D 222 
AA9 1 ILE D  67  ? ASP D  71  ? ILE D 59  ASP D 63  
AA9 2 ILE D  74  ? GLY D  80  ? ILE D 66  GLY D 72  
AA9 3 VAL D  140 ? ASP D  148 ? VAL D 132 ASP D 140 
AA9 4 GLY D  152 ? ALA D  158 ? GLY D 144 ALA D 150 
AA9 5 PHE D  164 ? TYR D  167 ? PHE D 156 TYR D 159 
AB1 1 GLY E  158 ? ILE E  161 ? GLY E 157 ILE E 160 
AB1 2 THR E  35  ? ARG E  39  ? THR E 34  ARG E 38  
AB1 3 HIS E  43  ? LEU E  49  ? HIS E 42  LEU E 48  
AB1 4 LEU E  211 ? GLY E  217 ? LEU E 210 GLY E 216 
AB1 5 THR E  220 ? TYR E  225 ? THR E 219 TYR E 224 
AB2 1 ILE E  63  ? LYS E  65  ? ILE E 62  LYS E 64  
AB2 2 MET E  70  ? GLY E  76  ? MET E 69  GLY E 75  
AB2 3 VAL E  130 ? ASP E  138 ? VAL E 129 ASP E 137 
AB2 4 GLY E  141 ? PHE E  147 ? GLY E 140 PHE E 146 
AB2 5 VAL E  153 ? GLU E  155 ? VAL E 152 GLU E 154 
AB3 1 GLY F  162 ? THR F  165 ? GLY F 158 THR F 161 
AB3 2 SER F  37  ? CYS F  42  ? SER F 33  CYS F 38  
AB3 3 GLY F  45  ? LEU F  53  ? GLY F 41  LEU F 49  
AB3 4 PHE F  212 ? SER F  220 ? PHE F 208 SER F 216 
AB3 5 HIS F  228 ? VAL F  231 ? HIS F 224 VAL F 227 
AB4 1 GLN F  68  ? VAL F  70  ? GLN F 64  VAL F 66  
AB4 2 ILE F  74  ? GLY F  80  ? ILE F 70  GLY F 76  
AB4 3 VAL F  134 ? ASP F  142 ? VAL F 130 ASP F 138 
AB4 4 GLY F  145 ? LEU F  151 ? GLY F 141 LEU F 147 
AB4 5 TYR F  157 ? GLY F  159 ? TYR F 153 GLY F 155 
AB5 1 ALA G  168 ? THR G  171 ? ALA G 159 THR G 162 
AB5 2 SER G  42  ? ARG G  46  ? SER G 33  ARG G 37  
AB5 3 THR G  51  ? GLN G  56  ? THR G 42  GLN G 47  
AB5 4 LEU G  223 ? THR G  229 ? LEU G 214 THR G 220 
AB5 5 LYS G  232 ? THR G  235 ? LYS G 223 THR G 226 
AB6 1 ILE G  72  ? CYS G  74  ? ILE G 63  CYS G 65  
AB6 2 GLY G  80  ? ASN G  84  ? GLY G 71  ASN G 75  
AB6 3 ILE G  140 ? ASP G  147 ? ILE G 131 ASP G 138 
AB6 4 GLY G  151 ? THR G  157 ? GLY G 142 THR G 148 
AB6 5 TYR G  163 ? TYR G  166 ? TYR G 154 TYR G 157 
AB7 1 SER H  19  ? GLN H  21  ? SER H 20  GLN H 22  
AB7 2 ILE H  24  ? ASP H  27  ? ILE H 25  ASP H 28  
AB8 1 LEU H  33  ? SER H  37  ? LEU H 34  SER H 38  
AB8 2 ILE H  40  ? GLY H  46  ? ILE H 41  GLY H 47  
AB8 3 ALA H  95  ? ASP H  103 ? ALA H 96  ASP H 104 
AB8 4 GLY H  106 ? ILE H  112 ? GLY H 107 ILE H 113 
AB8 5 THR H  118 ? VAL H  120 ? THR H 119 VAL H 121 
AB9 1 VAL H  211 ? VAL H  217 ? VAL H 212 VAL H 218 
AB9 2 GLU I  194 ? LEU I  200 ? GLU I 193 LEU I 199 
AB9 3 ALA I  185 ? LYS I  191 ? ALA I 184 LYS I 190 
AB9 4 CYS I  20  ? ASP I  26  ? CYS I 19  ASP I 25  
AB9 5 ILE I  11  ? GLY I  17  ? ILE I 10  GLY I 16  
AB9 6 PHE I  136 ? GLY I  140 ? PHE I 135 GLY I 139 
AC1 1 LEU I  29  ? SER I  31  ? LEU I 28  SER I 30  
AC1 2 LEU I  34  ? SER I  37  ? LEU I 33  SER I 36  
AC2 1 ILE I  43  ? TYR I  46  ? ILE I 42  TYR I 45  
AC2 2 VAL I  49  ? GLY I  55  ? VAL I 48  GLY I 54  
AC2 3 VAL I  105 ? ILE I  112 ? VAL I 104 ILE I 111 
AC2 4 PRO I  119 ? PHE I  124 ? PRO I 118 PHE I 123 
AC2 5 ILE I  130 ? ALA I  133 ? ILE I 129 ALA I 132 
AC3 1 TYR J  130 ? HIS J  133 ? TYR J 130 HIS J 133 
AC3 2 ILE J  4   ? ARG J  8   ? ILE J 4   ARG J 8   
AC3 3 VAL J  13  ? SER J  18  ? VAL J 13  SER J 18  
AC3 4 VAL J  179 ? ASP J  185 ? VAL J 179 ASP J 185 
AC3 5 GLY J  188 ? VAL J  192 ? GLY J 188 VAL J 192 
AC4 1 VAL J  21  ? ARG J  23  ? VAL J 21  ARG J 23  
AC4 2 SER J  26  ? LYS J  29  ? SER J 26  LYS J 29  
AC5 1 THR J  35  ? SER J  39  ? THR J 35  SER J 39  
AC5 2 THR J  42  ? GLY J  48  ? THR J 42  GLY J 48  
AC5 3 VAL J  100 ? ASP J  108 ? VAL J 100 ASP J 108 
AC5 4 LYS J  113 ? ILE J  119 ? LYS J 113 ILE J 119 
AC5 5 LYS J  125 ? GLU J  127 ? LYS J 125 GLU J 127 
AC6 1 ILE K  125 ? VAL K  128 ? ILE K 126 VAL K 129 
AC6 2 THR K  2   ? PHE K  7   ? THR K 3   PHE K 8   
AC6 3 GLY K  10  ? VAL K  15  ? GLY K 11  VAL K 16  
AC6 4 SER K  173 ? THR K  180 ? SER K 174 THR K 181 
AC6 5 GLY K  183 ? ASP K  191 ? GLY K 184 ASP K 192 
AC7 1 ALA K  19  ? ALA K  21  ? ALA K 20  ALA K 22  
AC7 2 TRP K  24  ? SER K  27  ? TRP K 25  SER K 28  
AC8 1 VAL K  33  ? ASN K  37  ? VAL K 34  ASN K 38  
AC8 2 LEU K  40  ? THR K  43  ? LEU K 41  THR K 44  
AC8 3 GLY K  97  ? THR K  104 ? GLY K 98  THR K 105 
AC8 4 GLY K  108 ? ASP K  115 ? GLY K 109 ASP K 116 
AC8 5 ARG K  120 ? GLY K  123 ? ARG K 121 GLY K 124 
AC9 1 CYS L  136 ? GLY L  140 ? CYS L 136 GLY L 140 
AC9 2 THR L  11  ? ALA L  16  ? THR L 11  ALA L 16  
AC9 3 ALA L  21  ? ASP L  26  ? ALA L 21  ASP L 26  
AC9 4 GLY L  201 ? THR L  208 ? GLY L 201 THR L 208 
AC9 5 GLY L  211 ? GLU L  218 ? GLY L 211 GLU L 218 
AD1 1 ASN L  29  ? THR L  31  ? ASN L 29  THR L 31  
AD1 2 SER L  34  ? SER L  37  ? SER L 34  SER L 37  
AD2 1 PHE L  44  ? ASP L  45  ? PHE L 44  ASP L 45  
AD2 2 VAL L  51  ? GLY L  56  ? VAL L 51  GLY L 56  
AD2 3 VAL L  107 ? LEU L  114 ? VAL L 107 LEU L 114 
AD2 4 GLY L  120 ? PHE L  125 ? GLY L 120 PHE L 125 
AD2 5 TYR L  131 ? GLU L  134 ? TYR L 131 GLU L 134 
AD3 1 LEU M  46  ? PHE M  49  ? LEU M 33  PHE M 36  
AD3 2 GLY M  41  ? TYR M  43  ? GLY M 28  TYR M 30  
AD3 3 VAL M  19  ? GLY M  21  ? VAL M 6   GLY M 8   
AD3 4 THR M  62  ? ASP M  69  ? THR M 49  ASP M 56  
AD3 5 LEU M  55  ? VAL M  58  ? LEU M 42  VAL M 45  
AD4 1 LEU M  46  ? PHE M  49  ? LEU M 33  PHE M 36  
AD4 2 GLY M  41  ? TYR M  43  ? GLY M 28  TYR M 30  
AD4 3 VAL M  19  ? GLY M  21  ? VAL M 6   GLY M 8   
AD4 4 THR M  62  ? ASP M  69  ? THR M 49  ASP M 56  
AD4 5 ASN M  125 ? VAL M  132 ? ASN M 112 VAL M 119 
AD4 6 GLN M  138 ? ASN M  144 ? GLN M 125 ASN M 131 
AD4 7 THR M  149 ? TYR M  150 ? THR M 136 TYR M 137 
AD5 1 THR M  154 ? ALA M  156 ? THR M 141 ALA M 143 
AD5 2 VAL M  24  ? LYS M  28  ? VAL M 11  LYS M 15  
AD5 3 GLY M  32  ? ASP M  38  ? GLY M 19  ASP M 25  
AD5 4 ASN M  207 ? ASP M  214 ? ASN M 194 ASP M 201 
AD5 5 GLY M  218 ? GLN M  226 ? GLY M 205 GLN M 213 
AD6 1 TYR N  124 ? ALA N  127 ? TYR N 124 ALA N 127 
AD6 2 ILE N  3   ? THR N  7   ? ILE N 3   THR N 7   
AD6 3 VAL N  12  ? ALA N  16  ? VAL N 12  ALA N 16  
AD6 4 ILE N  173 ? THR N  179 ? ILE N 173 THR N 179 
AD6 5 GLY N  182 ? PHE N  188 ? GLY N 182 PHE N 188 
AD7 1 THR N  20  ? THR N  22  ? THR N 20  THR N 22  
AD7 2 TYR N  25  ? ASN N  28  ? TYR N 25  ASN N 28  
AD8 1 LEU N  34  ? HIS N  38  ? LEU N 34  HIS N 38  
AD8 2 ILE N  41  ? GLY N  47  ? ILE N 41  GLY N 47  
AD8 3 ALA N  95  ? TYR N  102 ? ALA N 95  TYR N 102 
AD8 4 GLY N  108 ? ILE N  113 ? GLY N 108 ILE N 113 
AD8 5 HIS N  120 ? LEU N  122 ? HIS N 120 LEU N 122 
AD9 1 ALA O  161 ? ILE O  164 ? ALA O 161 ILE O 164 
AD9 2 SER O  34  ? LYS O  38  ? SER O 34  LYS O 38  
AD9 3 VAL O  43  ? GLU O  48  ? VAL O 43  GLU O 48  
AD9 4 ILE O  209 ? ILE O  214 ? ILE O 209 ILE O 214 
AD9 5 PHE O  235 ? LYS O  237 ? PHE O 235 LYS O 237 
AE1 1 ALA O  56  ? MET O  57  ? ALA O 56  MET O 57  
AE1 2 TYR U  163 ? TYR U  166 ? TYR U 154 TYR U 157 
AE1 3 GLY U  151 ? THR U  157 ? GLY U 142 THR U 148 
AE1 4 ILE U  140 ? ASP U  147 ? ILE U 131 ASP U 138 
AE1 5 GLY U  80  ? ASN U  84  ? GLY U 71  ASN U 75  
AE1 6 ILE U  72  ? CYS U  74  ? ILE U 63  CYS U 65  
AE2 1 SER O  65  ? THR O  68  ? SER O 65  THR O 68  
AE2 2 ILE O  71  ? GLY O  77  ? ILE O 71  GLY O 77  
AE2 3 VAL O  132 ? ASP O  140 ? VAL O 132 ASP O 140 
AE2 4 GLY O  144 ? VAL O  150 ? GLY O 144 VAL O 150 
AE2 5 TYR O  156 ? PRO O  158 ? TYR O 156 PRO O 158 
AE3 1 TYR O  224 ? THR O  225 ? TYR O 224 THR O 225 
AE3 2 ALA V  183 ? LEU V  190 ? ALA V 184 LEU V 191 
AE3 3 VAL V  172 ? GLU V  178 ? VAL V 173 GLU V 179 
AE3 4 GLY V  10  ? ASP V  16  ? GLY V 11  ASP V 17  
AE3 5 ILE V  2   ? LYS V  6   ? ILE V 3   LYS V 7   
AE3 6 TYR V  123 ? LEU V  126 ? TYR V 124 LEU V 127 
AE4 1 ALA P  162 ? VAL P  165 ? ALA P 161 VAL P 164 
AE4 2 ALA P  35  ? ALA P  40  ? ALA P 34  ALA P 39  
AE4 3 GLY P  43  ? GLU P  49  ? GLY P 42  GLU P 48  
AE4 4 LEU P  211 ? ARG P  217 ? LEU P 210 ARG P 216 
AE4 5 TYR P  226 ? ILE P  229 ? TYR P 225 ILE P 228 
AE5 1 LEU P  66  ? LYS P  68  ? LEU P 65  LYS P 67  
AE5 2 ILE P  73  ? GLY P  79  ? ILE P 72  GLY P 78  
AE5 3 VAL P  133 ? ASP P  141 ? VAL P 132 ASP P 140 
AE5 4 GLY P  145 ? SER P  151 ? GLY P 144 SER P 150 
AE5 5 TYR P  157 ? TRP P  160 ? TYR P 156 TRP P 159 
AE6 1 ALA Q  161 ? ILE Q  164 ? ALA Q 159 ILE Q 162 
AE6 2 ALA Q  33  ? LYS Q  37  ? ALA Q 31  LYS Q 35  
AE6 3 VAL Q  42  ? GLU Q  47  ? VAL Q 40  GLU Q 45  
AE6 4 ILE Q  210 ? LYS Q  216 ? ILE Q 208 LYS Q 214 
AE6 5 ASP Q  220 ? ALA Q  223 ? ASP Q 218 ALA Q 221 
AE7 1 VAL Q  64  ? LYS Q  66  ? VAL Q 62  LYS Q 64  
AE7 2 VAL Q  71  ? GLY Q  77  ? VAL Q 69  GLY Q 75  
AE7 3 VAL Q  131 ? GLY Q  137 ? VAL Q 129 GLY Q 135 
AE7 4 LYS Q  146 ? THR Q  150 ? LYS Q 144 THR Q 148 
AE7 5 TYR Q  156 ? SER Q  158 ? TYR Q 154 SER Q 156 
AE8 1 ALA R  169 ? ILE R  172 ? ALA R 161 ILE R 164 
AE8 2 ALA R  37  ? ALA R  41  ? ALA R 29  ALA R 33  
AE8 3 VAL R  46  ? GLU R  51  ? VAL R 38  GLU R 43  
AE8 4 ALA R  217 ? THR R  223 ? ALA R 209 THR R 215 
AE8 5 GLY R  227 ? ILE R  230 ? GLY R 219 ILE R 222 
AE9 1 ILE R  67  ? ASP R  71  ? ILE R 59  ASP R 63  
AE9 2 ILE R  74  ? GLY R  80  ? ILE R 66  GLY R 72  
AE9 3 VAL R  140 ? ASP R  148 ? VAL R 132 ASP R 140 
AE9 4 GLY R  152 ? ALA R  158 ? GLY R 144 ALA R 150 
AE9 5 PHE R  164 ? TYR R  167 ? PHE R 156 TYR R 159 
AF1 1 GLY S  158 ? ILE S  161 ? GLY S 157 ILE S 160 
AF1 2 THR S  35  ? ARG S  39  ? THR S 34  ARG S 38  
AF1 3 HIS S  43  ? LEU S  49  ? HIS S 42  LEU S 48  
AF1 4 LEU S  211 ? GLY S  217 ? LEU S 210 GLY S 216 
AF1 5 THR S  220 ? TYR S  225 ? THR S 219 TYR S 224 
AF2 1 ILE S  63  ? LYS S  65  ? ILE S 62  LYS S 64  
AF2 2 MET S  70  ? GLY S  76  ? MET S 69  GLY S 75  
AF2 3 VAL S  130 ? ASP S  138 ? VAL S 129 ASP S 137 
AF2 4 GLY S  141 ? PHE S  147 ? GLY S 140 PHE S 146 
AF2 5 VAL S  153 ? GLU S  155 ? VAL S 152 GLU S 154 
AF3 1 GLY T  162 ? THR T  165 ? GLY T 158 THR T 161 
AF3 2 SER T  37  ? CYS T  42  ? SER T 33  CYS T 38  
AF3 3 GLY T  45  ? LEU T  53  ? GLY T 41  LEU T 49  
AF3 4 PHE T  212 ? SER T  220 ? PHE T 208 SER T 216 
AF3 5 HIS T  228 ? VAL T  231 ? HIS T 224 VAL T 227 
AF4 1 GLN T  68  ? VAL T  70  ? GLN T 64  VAL T 66  
AF4 2 ILE T  74  ? GLY T  80  ? ILE T 70  GLY T 76  
AF4 3 VAL T  134 ? ASP T  142 ? VAL T 130 ASP T 138 
AF4 4 GLY T  145 ? LEU T  151 ? GLY T 141 LEU T 147 
AF4 5 TYR T  157 ? GLY T  159 ? TYR T 153 GLY T 155 
AF5 1 ALA U  168 ? THR U  171 ? ALA U 159 THR U 162 
AF5 2 SER U  42  ? ARG U  46  ? SER U 33  ARG U 37  
AF5 3 THR U  51  ? GLN U  56  ? THR U 42  GLN U 47  
AF5 4 LEU U  223 ? THR U  229 ? LEU U 214 THR U 220 
AF5 5 LYS U  232 ? THR U  235 ? LYS U 223 THR U 226 
AF6 1 SER V  19  ? GLN V  21  ? SER V 20  GLN V 22  
AF6 2 ILE V  24  ? ASP V  27  ? ILE V 25  ASP V 28  
AF7 1 LEU V  33  ? SER V  37  ? LEU V 34  SER V 38  
AF7 2 ILE V  40  ? GLY V  46  ? ILE V 41  GLY V 47  
AF7 3 ALA V  95  ? ASP V  103 ? ALA V 96  ASP V 104 
AF7 4 GLY V  106 ? ILE V  112 ? GLY V 107 ILE V 113 
AF7 5 THR V  118 ? VAL V  120 ? THR V 119 VAL V 121 
AF8 1 VAL V  211 ? VAL V  217 ? VAL V 212 VAL V 218 
AF8 2 GLU W  194 ? LEU W  200 ? GLU W 193 LEU W 199 
AF8 3 ALA W  185 ? LYS W  191 ? ALA W 184 LYS W 190 
AF8 4 CYS W  20  ? ASP W  26  ? CYS W 19  ASP W 25  
AF8 5 ILE W  11  ? GLY W  17  ? ILE W 10  GLY W 16  
AF8 6 PHE W  136 ? GLY W  140 ? PHE W 135 GLY W 139 
AF9 1 LEU W  29  ? SER W  31  ? LEU W 28  SER W 30  
AF9 2 LEU W  34  ? SER W  37  ? LEU W 33  SER W 36  
AG1 1 ILE W  43  ? TYR W  46  ? ILE W 42  TYR W 45  
AG1 2 VAL W  49  ? GLY W  55  ? VAL W 48  GLY W 54  
AG1 3 VAL W  105 ? ILE W  112 ? VAL W 104 ILE W 111 
AG1 4 PRO W  119 ? PHE W  124 ? PRO W 118 PHE W 123 
AG1 5 ILE W  130 ? ALA W  133 ? ILE W 129 ALA W 132 
AG2 1 TYR X  130 ? HIS X  133 ? TYR X 130 HIS X 133 
AG2 2 ILE X  4   ? ARG X  8   ? ILE X 4   ARG X 8   
AG2 3 VAL X  13  ? SER X  18  ? VAL X 13  SER X 18  
AG2 4 VAL X  179 ? ASP X  185 ? VAL X 179 ASP X 185 
AG2 5 GLY X  188 ? VAL X  192 ? GLY X 188 VAL X 192 
AG3 1 VAL X  21  ? ARG X  23  ? VAL X 21  ARG X 23  
AG3 2 SER X  26  ? LYS X  29  ? SER X 26  LYS X 29  
AG4 1 THR X  35  ? SER X  39  ? THR X 35  SER X 39  
AG4 2 THR X  42  ? GLY X  48  ? THR X 42  GLY X 48  
AG4 3 VAL X  100 ? ASP X  108 ? VAL X 100 ASP X 108 
AG4 4 LYS X  113 ? ILE X  119 ? LYS X 113 ILE X 119 
AG4 5 LYS X  125 ? GLU X  127 ? LYS X 125 GLU X 127 
AG5 1 ILE Y  125 ? VAL Y  128 ? ILE Y 126 VAL Y 129 
AG5 2 THR Y  2   ? PHE Y  7   ? THR Y 3   PHE Y 8   
AG5 3 GLY Y  10  ? VAL Y  15  ? GLY Y 11  VAL Y 16  
AG5 4 SER Y  173 ? THR Y  180 ? SER Y 174 THR Y 181 
AG5 5 GLY Y  183 ? ASP Y  191 ? GLY Y 184 ASP Y 192 
AG6 1 ALA Y  19  ? ALA Y  21  ? ALA Y 20  ALA Y 22  
AG6 2 TRP Y  24  ? SER Y  27  ? TRP Y 25  SER Y 28  
AG7 1 VAL Y  33  ? ASN Y  37  ? VAL Y 34  ASN Y 38  
AG7 2 LEU Y  40  ? THR Y  43  ? LEU Y 41  THR Y 44  
AG7 3 GLY Y  97  ? THR Y  104 ? GLY Y 98  THR Y 105 
AG7 4 GLY Y  108 ? ASP Y  115 ? GLY Y 109 ASP Y 116 
AG7 5 ARG Y  120 ? GLY Y  123 ? ARG Y 121 GLY Y 124 
AG8 1 CYS Z  136 ? GLY Z  140 ? CYS Z 136 GLY Z 140 
AG8 2 THR Z  11  ? ALA Z  16  ? THR Z 11  ALA Z 16  
AG8 3 ALA Z  21  ? ASP Z  26  ? ALA Z 21  ASP Z 26  
AG8 4 GLY Z  201 ? THR Z  208 ? GLY Z 201 THR Z 208 
AG8 5 GLY Z  211 ? GLU Z  218 ? GLY Z 211 GLU Z 218 
AG9 1 ASN Z  29  ? THR Z  31  ? ASN Z 29  THR Z 31  
AG9 2 SER Z  34  ? SER Z  37  ? SER Z 34  SER Z 37  
AH1 1 PHE Z  44  ? ASP Z  45  ? PHE Z 44  ASP Z 45  
AH1 2 VAL Z  51  ? GLY Z  56  ? VAL Z 51  GLY Z 56  
AH1 3 VAL Z  107 ? LEU Z  114 ? VAL Z 107 LEU Z 114 
AH1 4 GLY Z  120 ? PHE Z  125 ? GLY Z 120 PHE Z 125 
AH1 5 TYR Z  131 ? GLU Z  134 ? TYR Z 131 GLU Z 134 
AH2 1 LEU AA 46  ? PHE AA 49  ? LEU a 33  PHE a 36  
AH2 2 GLY AA 41  ? TYR AA 43  ? GLY a 28  TYR a 30  
AH2 3 VAL AA 19  ? GLY AA 21  ? VAL a 6   GLY a 8   
AH2 4 THR AA 62  ? ASP AA 69  ? THR a 49  ASP a 56  
AH2 5 LEU AA 55  ? VAL AA 58  ? LEU a 42  VAL a 45  
AH3 1 LEU AA 46  ? PHE AA 49  ? LEU a 33  PHE a 36  
AH3 2 GLY AA 41  ? TYR AA 43  ? GLY a 28  TYR a 30  
AH3 3 VAL AA 19  ? GLY AA 21  ? VAL a 6   GLY a 8   
AH3 4 THR AA 62  ? ASP AA 69  ? THR a 49  ASP a 56  
AH3 5 ASN AA 125 ? VAL AA 132 ? ASN a 112 VAL a 119 
AH3 6 GLN AA 138 ? ASN AA 144 ? GLN a 125 ASN a 131 
AH3 7 THR AA 149 ? TYR AA 150 ? THR a 136 TYR a 137 
AH4 1 THR AA 154 ? ALA AA 156 ? THR a 141 ALA a 143 
AH4 2 VAL AA 24  ? LYS AA 28  ? VAL a 11  LYS a 15  
AH4 3 GLY AA 32  ? ASP AA 38  ? GLY a 19  ASP a 25  
AH4 4 ASN AA 207 ? ASP AA 214 ? ASN a 194 ASP a 201 
AH4 5 GLY AA 218 ? GLN AA 226 ? GLY a 205 GLN a 213 
AH5 1 TYR BA 124 ? ALA BA 127 ? TYR b 124 ALA b 127 
AH5 2 ILE BA 3   ? THR BA 7   ? ILE b 3   THR b 7   
AH5 3 VAL BA 12  ? ALA BA 16  ? VAL b 12  ALA b 16  
AH5 4 ILE BA 173 ? THR BA 179 ? ILE b 173 THR b 179 
AH5 5 GLY BA 182 ? PHE BA 188 ? GLY b 182 PHE b 188 
AH6 1 THR BA 20  ? THR BA 22  ? THR b 20  THR b 22  
AH6 2 TYR BA 25  ? ASN BA 28  ? TYR b 25  ASN b 28  
AH7 1 LEU BA 34  ? HIS BA 38  ? LEU b 34  HIS b 38  
AH7 2 ILE BA 41  ? GLY BA 47  ? ILE b 41  GLY b 47  
AH7 3 ALA BA 95  ? TYR BA 102 ? ALA b 95  TYR b 102 
AH7 4 GLY BA 108 ? ILE BA 113 ? GLY b 108 ILE b 113 
AH7 5 HIS BA 120 ? LEU BA 122 ? HIS b 120 LEU b 122 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A  164 ? O ILE A 164 N SER A  34  ? N SER A 34  
AA1 2 3 N ILE A  37  ? N ILE A 37  O VAL A  44  ? O VAL A 44  
AA1 3 4 N VAL A  43  ? N VAL A 43  O ILE A  214 ? O ILE A 214 
AA1 4 5 N ILE A  213 ? N ILE A 213 O ARG A  236 ? O ARG A 236 
AA2 1 2 N SER A  65  ? N SER A 65  O ALA A  73  ? O ALA A 73  
AA2 2 3 N VAL A  74  ? N VAL A 74  O LEU A  135 ? O LEU A 135 
AA2 3 4 N LEU A  134 ? N LEU A 134 O VAL A  150 ? O VAL A 150 
AA2 4 5 N GLN A  149 ? N GLN A 149 O PHE A  157 ? O PHE A 157 
AA3 1 2 N THR A  225 ? N THR A 225 O TYR H  185 ? O TYR H 186 
AA3 2 3 O LEU H  186 ? O LEU H 187 N VAL H  174 ? N VAL H 175 
AA3 3 4 O ASP H  173 ? O ASP H 174 N ALA H  15  ? N ALA H 16  
AA3 4 5 O VAL H  12  ? O VAL H 13  N VAL H  5   ? N VAL H 6   
AA3 5 6 N ILE H  2   ? N ILE H 3   O LEU H  126 ? O LEU H 127 
AA4 1 2 O ILE B  163 ? O ILE B 162 N GLY B  37  ? N GLY B 36  
AA4 2 3 N ILE B  36  ? N ILE B 35  O ALA B  47  ? O ALA B 46  
AA4 3 4 N LEU B  46  ? N LEU B 45  O ALA B  214 ? O ALA B 213 
AA4 4 5 N THR B  215 ? N THR B 214 O LYS B  228 ? O LYS B 227 
AA5 1 2 N TYR B  67  ? N TYR B 66  O VAL B  75  ? O VAL B 74  
AA5 2 3 N ALA B  74  ? N ALA B 73  O ALA B  138 ? O ALA B 137 
AA5 3 4 N GLY B  139 ? N GLY B 138 O GLN B  147 ? O GLN B 146 
AA5 4 5 N LEU B  148 ? N LEU B 147 O TRP B  160 ? O TRP B 159 
AA6 1 2 O GLN C  162 ? O GLN C 160 N GLY C  35  ? N GLY C 33  
AA6 2 3 N VAL C  36  ? N VAL C 34  O VAL C  43  ? O VAL C 41  
AA6 3 4 N LEU C  44  ? N LEU C 42  O THR C  213 ? O THR C 211 
AA6 4 5 N LYS C  216 ? N LYS C 214 O ASP C  220 ? O ASP C 218 
AA7 1 2 N SER C  65  ? N SER C 63  O LEU C  73  ? O LEU C 71  
AA7 2 3 N VAL C  72  ? N VAL C 70  O ALA C  136 ? O ALA C 134 
AA7 3 4 N ILE C  135 ? N ILE C 133 O TYR C  148 ? O TYR C 146 
AA7 4 5 N GLN C  149 ? N GLN C 147 O SER C  157 ? O SER C 155 
AA8 1 2 O ILE D  172 ? O ILE D 164 N ALA D  37  ? N ALA D 29  
AA8 2 3 N ILE D  38  ? N ILE D 30  O GLY D  49  ? O GLY D 41  
AA8 3 4 N LEU D  48  ? N LEU D 40  O SER D  220 ? O SER D 212 
AA8 4 5 N CYS D  221 ? N CYS D 213 O LYS D  229 ? O LYS D 221 
AA9 1 2 N VAL D  68  ? N VAL D 60  O CYS D  76  ? O CYS D 68  
AA9 2 3 N GLY D  75  ? N GLY D 67  O ALA D  145 ? O ALA D 137 
AA9 3 4 N LEU D  142 ? N LEU D 134 O ALA D  158 ? O ALA D 150 
AA9 4 5 N LEU D  155 ? N LEU D 147 O TYR D  167 ? O TYR D 159 
AB1 1 2 O THR E  159 ? O THR E 158 N GLY E  37  ? N GLY E 36  
AB1 2 3 N VAL E  36  ? N VAL E 35  O VAL E  47  ? O VAL E 46  
AB1 3 4 N ALA E  48  ? N ALA E 47  O SER E  212 ? O SER E 211 
AB1 4 5 N ILE E  213 ? N ILE E 212 O TYR E  225 ? O TYR E 224 
AB2 1 2 N ILE E  64  ? N ILE E 63  O LEU E  72  ? O LEU E 71  
AB2 2 3 N ALA E  75  ? N ALA E 74  O GLY E  131 ? O GLY E 130 
AB2 3 4 N LEU E  132 ? N LEU E 131 O PHE E  147 ? O PHE E 146 
AB2 4 5 N GLU E  146 ? N GLU E 145 O THR E  154 ? O THR E 153 
AB3 1 2 O ALA F  163 ? O ALA F 159 N GLY F  39  ? N GLY F 35  
AB3 2 3 N ILE F  40  ? N ILE F 36  O VAL F  47  ? O VAL F 43  
AB3 3 4 N PHE F  48  ? N PHE F 44  O SER F  217 ? O SER F 213 
AB3 4 5 N TRP F  218 ? N TRP F 214 O LYS F  229 ? O LYS F 225 
AB4 1 2 N GLN F  68  ? N GLN F 64  O CYS F  76  ? O CYS F 72  
AB4 2 3 N VAL F  77  ? N VAL F 73  O ILE F  137 ? O ILE F 133 
AB4 3 4 N PHE F  138 ? N PHE F 134 O TYR F  149 ? O TYR F 145 
AB4 4 5 N MET F  150 ? N MET F 146 O TRP F  158 ? O TRP F 154 
AB5 1 2 O THR G  169 ? O THR G 160 N ALA G  44  ? N ALA G 35  
AB5 2 3 N LEU G  43  ? N LEU G 34  O ILE G  54  ? O ILE G 45  
AB5 3 4 N VAL G  53  ? N VAL G 44  O GLY G  226 ? O GLY G 217 
AB5 4 5 N VAL G  227 ? N VAL G 218 O PHE G  234 ? O PHE G 225 
AB6 1 2 N PHE G  73  ? N PHE G 64  O MET G  81  ? O MET G 72  
AB6 2 3 N GLY G  80  ? N GLY G 71  O VAL G  144 ? O VAL G 135 
AB6 3 4 N PHE G  143 ? N PHE G 134 O TYR G  155 ? O TYR G 146 
AB6 4 5 N ILE G  154 ? N ILE G 145 O TYR G  166 ? O TYR G 157 
AB7 1 2 N GLN H  21  ? N GLN H 22  O ILE H  24  ? O ILE H 25  
AB8 1 2 N HIS H  34  ? N HIS H 35  O CYS H  42  ? O CYS H 43  
AB8 2 3 N ALA H  45  ? N ALA H 46  O TYR H  96  ? O TYR H 97  
AB8 3 4 N LEU H  97  ? N LEU H 98  O ILE H  112 ? O ILE H 113 
AB8 4 5 N SER H  111 ? N SER H 112 O ASP H  119 ? O ASP H 120 
AB9 1 2 N SER H  215 ? N SER H 216 O LYS I  197 ? O LYS I 196 
AB9 2 3 O ARG I  198 ? O ARG I 197 N VAL I  187 ? N VAL I 186 
AB9 3 4 O ILE I  190 ? O ILE I 189 N VAL I  21  ? N VAL I 20  
AB9 4 5 O ALA I  24  ? O ALA I 23  N VAL I  13  ? N VAL I 12  
AB9 5 6 N ALA I  14  ? N ALA I 13  O ILE I  137 ? O ILE I 136 
AC1 1 2 N SER I  31  ? N SER I 30  O LEU I  34  ? O LEU I 33  
AC2 1 2 N PHE I  44  ? N PHE I 43  O LEU I  51  ? O LEU I 50  
AC2 2 3 N GLY I  52  ? N GLY I 51  O VAL I  108 ? O VAL I 107 
AC2 3 4 N GLY I  111 ? N GLY I 110 O PHE I  120 ? O PHE I 119 
AC2 4 5 N GLY I  123 ? N GLY I 122 O ASP I  131 ? O ASP I 130 
AC3 1 2 O GLY J  131 ? O GLY J 131 N GLY J  6   ? N GLY J 6   
AC3 2 3 N LEU J  5   ? N LEU J 5   O ALA J  16  ? O ALA J 16  
AC3 3 4 N VAL J  13  ? N VAL J 13  O VAL J  184 ? O VAL J 184 
AC3 4 5 N ILE J  183 ? N ILE J 183 O ARG J  190 ? O ARG J 190 
AC4 1 2 N VAL J  21  ? N VAL J 21  O LYS J  29  ? O LYS J 29  
AC5 1 2 N ARG J  36  ? N ARG J 36  O MET J  44  ? O MET J 44  
AC5 2 3 N ALA J  47  ? N ALA J 47  O ASN J  101 ? O ASN J 101 
AC5 3 4 N VAL J  102 ? N VAL J 102 O ILE J  119 ? O ILE J 119 
AC5 4 5 N GLN J  118 ? N GLN J 118 O VAL J  126 ? O VAL J 126 
AC6 1 2 O VAL K  128 ? O VAL K 129 N THR K  2   ? N THR K 3   
AC6 2 3 N PHE K  7   ? N PHE K 8   O GLY K  10  ? O GLY K 11  
AC6 3 4 N ILE K  11  ? N ILE K 12  O VAL K  179 ? O VAL K 180 
AC6 4 5 N HIS K  178 ? N HIS K 179 O ILE K  185 ? O ILE K 186 
AC7 1 2 N ALA K  21  ? N ALA K 22  O TRP K  24  ? O TRP K 25  
AC8 1 2 N ILE K  34  ? N ILE K 35  O GLY K  42  ? O GLY K 43  
AC8 2 3 N LEU K  41  ? N LEU K 42  O CYS K  101 ? O CYS K 102 
AC8 3 4 N ILE K  100 ? N ILE K 101 O TYR K  112 ? O TYR K 113 
AC8 4 5 N TYR K  113 ? N TYR K 114 O LEU K  121 ? O LEU K 122 
AC9 1 2 O GLY L  139 ? O GLY L 139 N ILE L  12  ? N ILE L 12  
AC9 2 3 N LEU L  13  ? N LEU L 13  O ALA L  24  ? O ALA L 24  
AC9 3 4 N ALA L  21  ? N ALA L 21  O VAL L  207 ? O VAL L 207 
AC9 4 5 N LEU L  202 ? N LEU L 202 O TYR L  217 ? O TYR L 217 
AD1 1 2 N ASN L  29  ? N ASN L 29  O ASN L  36  ? O ASN L 36  
AD2 1 2 N PHE L  44  ? N PHE L 44  O MET L  52  ? O MET L 52  
AD2 2 3 N ASN L  55  ? N ASN L 55  O HIS L  108 ? O HIS L 108 
AD2 3 4 N THR L  109 ? N THR L 109 O PHE L  125 ? O PHE L 125 
AD2 4 5 N VAL L  122 ? N VAL L 122 O GLU L  134 ? O GLU L 134 
AD3 1 2 O LEU M  46  ? O LEU M 33  N TYR M  43  ? N TYR M 30  
AD3 2 3 O SER M  42  ? O SER M 29  N THR M  20  ? N THR M 7   
AD3 3 4 N GLY M  21  ? N GLY M 8   O GLY M  68  ? O GLY M 55  
AD3 4 5 O VAL M  64  ? O VAL M 51  N ILE M  56  ? N ILE M 43  
AD4 1 2 O LEU M  46  ? O LEU M 33  N TYR M  43  ? N TYR M 30  
AD4 2 3 O SER M  42  ? O SER M 29  N THR M  20  ? N THR M 7   
AD4 3 4 N GLY M  21  ? N GLY M 8   O GLY M  68  ? O GLY M 55  
AD4 4 5 N VAL M  63  ? N VAL M 50  O ALA M  130 ? O ALA M 117 
AD4 5 6 N ILE M  127 ? N ILE M 114 O VAL M  143 ? O VAL M 130 
AD4 6 7 N TYR M  142 ? N TYR M 129 O TYR M  150 ? O TYR M 137 
AD5 1 2 O LEU M  155 ? O LEU M 142 N SER M  26  ? N SER M 13  
AD5 2 3 N ILE M  25  ? N ILE M 12  O ALA M  36  ? O ALA M 23  
AD5 3 4 N ILE M  35  ? N ILE M 22  O ALA M  211 ? O ALA M 198 
AD5 4 5 N ILE M  212 ? N ILE M 199 O THR M  220 ? O THR M 207 
AD6 1 2 O ALA N  127 ? O ALA N 127 N ILE N  3   ? N ILE N 3   
AD6 2 3 N MET N  4   ? N MET N 4   O GLY N  15  ? O GLY N 15  
AD6 3 4 N VAL N  12  ? N VAL N 12  O LEU N  178 ? O LEU N 178 
AD6 4 5 N VAL N  177 ? N VAL N 177 O GLU N  184 ? O GLU N 184 
AD7 1 2 N THR N  22  ? N THR N 22  O TYR N  25  ? O TYR N 25  
AD8 1 2 N THR N  35  ? N THR N 35  O CYS N  43  ? O CYS N 43  
AD8 2 3 N SER N  46  ? N SER N 46  O GLY N  96  ? O GLY N 96  
AD8 3 4 N VAL N  99  ? N VAL N 99  O TYR N  111 ? O TYR N 111 
AD8 4 5 N THR N  112 ? N THR N 112 O HIS N  120 ? O HIS N 120 
AD9 1 2 O ILE O  164 ? O ILE O 164 N SER O  34  ? N SER O 34  
AD9 2 3 N ILE O  37  ? N ILE O 37  O VAL O  44  ? O VAL O 44  
AD9 3 4 N VAL O  43  ? N VAL O 43  O ILE O  214 ? O ILE O 214 
AD9 4 5 N ILE O  213 ? N ILE O 213 O ARG O  236 ? O ARG O 236 
AE1 1 2 N MET O  57  ? N MET O 57  O GLY U  165 ? O GLY U 156 
AE1 2 3 O TYR U  166 ? O TYR U 157 N ILE U  154 ? N ILE U 145 
AE1 3 4 O TYR U  155 ? O TYR U 146 N PHE U  143 ? N PHE U 134 
AE1 4 5 O VAL U  144 ? O VAL U 135 N GLY U  80  ? N GLY U 71  
AE1 5 6 O MET U  81  ? O MET U 72  N PHE U  73  ? N PHE U 64  
AE2 1 2 N SER O  65  ? N SER O 65  O ALA O  73  ? O ALA O 73  
AE2 2 3 N GLY O  72  ? N GLY O 72  O ALA O  137 ? O ALA O 137 
AE2 3 4 N LEU O  134 ? N LEU O 134 O VAL O  150 ? O VAL O 150 
AE2 4 5 N GLN O  149 ? N GLN O 149 O PHE O  157 ? O PHE O 157 
AE3 1 2 N THR O  225 ? N THR O 225 O TYR V  185 ? O TYR V 186 
AE3 2 3 O LEU V  186 ? O LEU V 187 N VAL V  174 ? N VAL V 175 
AE3 3 4 O ASP V  173 ? O ASP V 174 N ALA V  15  ? N ALA V 16  
AE3 4 5 O VAL V  12  ? O VAL V 13  N VAL V  5   ? N VAL V 6   
AE3 5 6 N GLY V  4   ? N GLY V 5   O LEU V  124 ? O LEU V 125 
AE4 1 2 O ILE P  163 ? O ILE P 162 N GLY P  37  ? N GLY P 36  
AE4 2 3 N ILE P  36  ? N ILE P 35  O ALA P  47  ? O ALA P 46  
AE4 3 4 N LEU P  46  ? N LEU P 45  O ALA P  214 ? O ALA P 213 
AE4 4 5 N THR P  215 ? N THR P 214 O LYS P  228 ? O LYS P 227 
AE5 1 2 N TYR P  67  ? N TYR P 66  O VAL P  75  ? O VAL P 74  
AE5 2 3 N ALA P  74  ? N ALA P 73  O ALA P  138 ? O ALA P 137 
AE5 3 4 N TYR P  137 ? N TYR P 136 O TYR P  149 ? O TYR P 148 
AE5 4 5 N LEU P  148 ? N LEU P 147 O TRP P  160 ? O TRP P 159 
AE6 1 2 O GLN Q  162 ? O GLN Q 160 N GLY Q  35  ? N GLY Q 33  
AE6 2 3 N VAL Q  34  ? N VAL Q 32  O GLY Q  45  ? O GLY Q 43  
AE6 3 4 N LEU Q  44  ? N LEU Q 42  O THR Q  213 ? O THR Q 211 
AE6 4 5 N LYS Q  216 ? N LYS Q 214 O ASP Q  220 ? O ASP Q 218 
AE7 1 2 N SER Q  65  ? N SER Q 63  O LEU Q  73  ? O LEU Q 71  
AE7 2 3 N VAL Q  72  ? N VAL Q 70  O ALA Q  136 ? O ALA Q 134 
AE7 3 4 N ILE Q  135 ? N ILE Q 133 O TYR Q  148 ? O TYR Q 146 
AE7 4 5 N GLN Q  149 ? N GLN Q 147 O SER Q  157 ? O SER Q 155 
AE8 1 2 O ILE R  172 ? O ILE R 164 N ALA R  37  ? N ALA R 29  
AE8 2 3 N ILE R  38  ? N ILE R 30  O GLY R  49  ? O GLY R 41  
AE8 3 4 N LEU R  48  ? N LEU R 40  O SER R  220 ? O SER R 212 
AE8 4 5 N CYS R  221 ? N CYS R 213 O LYS R  229 ? O LYS R 221 
AE9 1 2 N VAL R  68  ? N VAL R 60  O CYS R  76  ? O CYS R 68  
AE9 2 3 N GLY R  75  ? N GLY R 67  O ALA R  145 ? O ALA R 137 
AE9 3 4 N LEU R  142 ? N LEU R 134 O ALA R  158 ? O ALA R 150 
AE9 4 5 N LEU R  155 ? N LEU R 147 O TYR R  167 ? O TYR R 159 
AF1 1 2 O THR S  159 ? O THR S 158 N GLY S  37  ? N GLY S 36  
AF1 2 3 N VAL S  36  ? N VAL S 35  O VAL S  47  ? O VAL S 46  
AF1 3 4 N ALA S  48  ? N ALA S 47  O SER S  212 ? O SER S 211 
AF1 4 5 N ILE S  213 ? N ILE S 212 O TYR S  225 ? O TYR S 224 
AF2 1 2 N ILE S  64  ? N ILE S 63  O LEU S  72  ? O LEU S 71  
AF2 2 3 N ALA S  75  ? N ALA S 74  O GLY S  131 ? O GLY S 130 
AF2 3 4 N LEU S  132 ? N LEU S 131 O PHE S  147 ? O PHE S 146 
AF2 4 5 N GLU S  146 ? N GLU S 145 O THR S  154 ? O THR S 153 
AF3 1 2 O THR T  165 ? O THR T 161 N SER T  37  ? N SER T 33  
AF3 2 3 N ILE T  40  ? N ILE T 36  O VAL T  47  ? O VAL T 43  
AF3 3 4 N PHE T  48  ? N PHE T 44  O SER T  217 ? O SER T 213 
AF3 4 5 N TRP T  218 ? N TRP T 214 O LYS T  229 ? O LYS T 225 
AF4 1 2 N GLN T  68  ? N GLN T 64  O CYS T  76  ? O CYS T 72  
AF4 2 3 N VAL T  77  ? N VAL T 73  O ILE T  137 ? O ILE T 133 
AF4 3 4 N PHE T  138 ? N PHE T 134 O TYR T  149 ? O TYR T 145 
AF4 4 5 N MET T  150 ? N MET T 146 O TRP T  158 ? O TRP T 154 
AF5 1 2 O THR U  169 ? O THR U 160 N ALA U  44  ? N ALA U 35  
AF5 2 3 N LEU U  43  ? N LEU U 34  O ILE U  54  ? O ILE U 45  
AF5 3 4 N VAL U  53  ? N VAL U 44  O GLY U  226 ? O GLY U 217 
AF5 4 5 N VAL U  227 ? N VAL U 218 O PHE U  234 ? O PHE U 225 
AF6 1 2 N GLN V  21  ? N GLN V 22  O ILE V  24  ? O ILE V 25  
AF7 1 2 N HIS V  34  ? N HIS V 35  O CYS V  42  ? O CYS V 43  
AF7 2 3 N ALA V  43  ? N ALA V 44  O ILE V  98  ? O ILE V 99  
AF7 3 4 N LEU V  97  ? N LEU V 98  O ILE V  112 ? O ILE V 113 
AF7 4 5 N SER V  111 ? N SER V 112 O ASP V  119 ? O ASP V 120 
AF8 1 2 N SER V  215 ? N SER V 216 O LYS W  197 ? O LYS W 196 
AF8 2 3 O ARG W  198 ? O ARG W 197 N VAL W  187 ? N VAL W 186 
AF8 3 4 O ILE W  190 ? O ILE W 189 N VAL W  21  ? N VAL W 20  
AF8 4 5 O ALA W  24  ? O ALA W 23  N VAL W  13  ? N VAL W 12  
AF8 5 6 N ALA W  14  ? N ALA W 13  O ILE W  137 ? O ILE W 136 
AF9 1 2 N SER W  31  ? N SER W 30  O LEU W  34  ? O LEU W 33  
AG1 1 2 N PHE W  44  ? N PHE W 43  O LEU W  51  ? O LEU W 50  
AG1 2 3 N GLY W  52  ? N GLY W 51  O VAL W  108 ? O VAL W 107 
AG1 3 4 N GLY W  111 ? N GLY W 110 O PHE W  120 ? O PHE W 119 
AG1 4 5 N GLY W  123 ? N GLY W 122 O ASP W  131 ? O ASP W 130 
AG2 1 2 O GLY X  131 ? O GLY X 131 N GLY X  6   ? N GLY X 6   
AG2 2 3 N LEU X  5   ? N LEU X 5   O ALA X  16  ? O ALA X 16  
AG2 3 4 N VAL X  13  ? N VAL X 13  O VAL X  184 ? O VAL X 184 
AG2 4 5 N ILE X  183 ? N ILE X 183 O ARG X  190 ? O ARG X 190 
AG3 1 2 N VAL X  21  ? N VAL X 21  O LYS X  29  ? O LYS X 29  
AG4 1 2 N ARG X  36  ? N ARG X 36  O MET X  44  ? O MET X 44  
AG4 2 3 N ALA X  47  ? N ALA X 47  O ASN X  101 ? O ASN X 101 
AG4 3 4 N GLY X  106 ? N GLY X 106 O GLU X  115 ? O GLU X 115 
AG4 4 5 N GLN X  118 ? N GLN X 118 O VAL X  126 ? O VAL X 126 
AG5 1 2 O VAL Y  128 ? O VAL Y 129 N THR Y  2   ? N THR Y 3   
AG5 2 3 N PHE Y  7   ? N PHE Y 8   O GLY Y  10  ? O GLY Y 11  
AG5 3 4 N ILE Y  11  ? N ILE Y 12  O VAL Y  179 ? O VAL Y 180 
AG5 4 5 N HIS Y  178 ? N HIS Y 179 O ILE Y  185 ? O ILE Y 186 
AG6 1 2 N ALA Y  21  ? N ALA Y 22  O TRP Y  24  ? O TRP Y 25  
AG7 1 2 N ILE Y  34  ? N ILE Y 35  O GLY Y  42  ? O GLY Y 43  
AG7 2 3 N LEU Y  41  ? N LEU Y 42  O CYS Y  101 ? O CYS Y 102 
AG7 3 4 N THR Y  98  ? N THR Y 99  O VAL Y  114 ? O VAL Y 115 
AG7 4 5 N TYR Y  113 ? N TYR Y 114 O LEU Y  121 ? O LEU Y 122 
AG8 1 2 O GLY Z  139 ? O GLY Z 139 N ILE Z  12  ? N ILE Z 12  
AG8 2 3 N LEU Z  13  ? N LEU Z 13  O ALA Z  24  ? O ALA Z 24  
AG8 3 4 N ALA Z  21  ? N ALA Z 21  O VAL Z  207 ? O VAL Z 207 
AG8 4 5 N LEU Z  202 ? N LEU Z 202 O TYR Z  217 ? O TYR Z 217 
AG9 1 2 N ASN Z  29  ? N ASN Z 29  O ASN Z  36  ? O ASN Z 36  
AH1 1 2 N PHE Z  44  ? N PHE Z 44  O MET Z  52  ? O MET Z 52  
AH1 2 3 N ASN Z  55  ? N ASN Z 55  O HIS Z  108 ? O HIS Z 108 
AH1 3 4 N THR Z  109 ? N THR Z 109 O PHE Z  125 ? O PHE Z 125 
AH1 4 5 N VAL Z  122 ? N VAL Z 122 O GLU Z  134 ? O GLU Z 134 
AH2 1 2 O PHE AA 49  ? O PHE a 36  N GLY AA 41  ? N GLY a 28  
AH2 2 3 O SER AA 42  ? O SER a 29  N THR AA 20  ? N THR a 7   
AH2 3 4 N GLY AA 21  ? N GLY a 8   O GLY AA 68  ? O GLY a 55  
AH2 4 5 O VAL AA 64  ? O VAL a 51  N ILE AA 56  ? N ILE a 43  
AH3 1 2 O PHE AA 49  ? O PHE a 36  N GLY AA 41  ? N GLY a 28  
AH3 2 3 O SER AA 42  ? O SER a 29  N THR AA 20  ? N THR a 7   
AH3 3 4 N GLY AA 21  ? N GLY a 8   O GLY AA 68  ? O GLY a 55  
AH3 4 5 N VAL AA 63  ? N VAL a 50  O ALA AA 130 ? O ALA a 117 
AH3 5 6 N ILE AA 127 ? N ILE a 114 O VAL AA 143 ? O VAL a 130 
AH3 6 7 N TYR AA 142 ? N TYR a 129 O TYR AA 150 ? O TYR a 137 
AH4 1 2 O LEU AA 155 ? O LEU a 142 N SER AA 26  ? N SER a 13  
AH4 2 3 N ILE AA 25  ? N ILE a 12  O ALA AA 36  ? O ALA a 23  
AH4 3 4 N ILE AA 35  ? N ILE a 22  O ALA AA 211 ? O ALA a 198 
AH4 4 5 N ILE AA 212 ? N ILE a 199 O THR AA 220 ? O THR a 207 
AH5 1 2 O ALA BA 127 ? O ALA b 127 N ILE BA 3   ? N ILE b 3   
AH5 2 3 N MET BA 4   ? N MET b 4   O GLY BA 15  ? O GLY b 15  
AH5 3 4 N VAL BA 12  ? N VAL b 12  O LEU BA 178 ? O LEU b 178 
AH5 4 5 N MET BA 175 ? N MET b 175 O LEU BA 186 ? O LEU b 186 
AH6 1 2 N THR BA 22  ? N THR b 22  O TYR BA 25  ? O TYR b 25  
AH7 1 2 N THR BA 35  ? N THR b 35  O CYS BA 43  ? O CYS b 43  
AH7 2 3 N SER BA 46  ? N SER b 46  O GLY BA 96  ? O GLY b 96  
AH7 3 4 N VAL BA 99  ? N VAL b 99  O TYR BA 111 ? O TYR b 111 
AH7 4 5 N THR BA 112 ? N THR b 112 O HIS BA 120 ? O HIS b 120 
# 
_pdbx_entry_details.entry_id                   9EY9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 THR A 2   ? ? 64.57   151.98  
2   1 ASP A 3   ? ? -57.43  95.66   
3   1 TYR A 97  ? ? -145.30 -68.86  
4   1 LYS A 166 ? ? -42.25  -74.98  
5   1 ALA A 249 ? ? -92.19  54.03   
6   1 ARG B 8   ? ? 59.46   71.47   
7   1 THR B 10  ? ? -109.67 54.98   
8   1 VAL B 51  ? ? -17.14  106.73  
9   1 GLU B 63  ? ? -133.58 -40.81  
10  1 ALA B 219 ? ? -75.16  -155.04 
11  1 ASP B 221 ? ? 75.78   112.02  
12  1 ASN C 38  ? ? -149.94 25.04   
13  1 LEU C 52  ? ? 80.07   15.47   
14  1 PRO C 183 ? ? -39.11  108.07  
15  1 VAL C 201 ? ? -68.97  -71.03  
16  1 GLN C 202 ? ? 140.48  -101.48 
17  1 ALA C 205 ? ? -78.48  -125.75 
18  1 LYS C 206 ? ? -86.33  42.19   
19  1 GLN C 239 ? ? -65.98  82.19   
20  1 ARG D 45  ? ? 55.92   76.19   
21  1 LEU D 73  ? ? -69.45  85.59   
22  1 GLU D 201 ? ? -71.67  -70.27  
23  1 SER E 39  ? ? -104.32 -149.23 
24  1 ASP E 137 ? ? -129.48 -160.11 
25  1 ASP E 202 ? ? 71.11   -24.37  
26  1 SER F 9   ? ? 86.53   -3.71   
27  1 ASP F 67  ? ? 56.27   -127.48 
28  1 LYS F 100 ? ? 75.97   -55.23  
29  1 ASP F 138 ? ? -126.05 -168.54 
30  1 ASN F 203 ? ? -155.50 38.11   
31  1 LYS G 165 ? ? -103.96 48.06   
32  1 GLU G 241 ? ? -86.16  35.92   
33  1 SER H 171 ? ? 66.84   -114.29 
34  1 GLN I 31  ? ? 50.59   -111.06 
35  1 ARG I 97  ? ? -106.20 49.21   
36  1 ASP I 134 ? ? -102.93 -74.45  
37  1 ASP I 192 ? ? -149.33 41.77   
38  1 GLN I 203 ? ? -108.84 44.14   
39  1 ASP J 2   ? ? 128.32  -80.53  
40  1 VAL J 9   ? ? -119.03 -168.26 
41  1 SER J 31  ? ? -142.04 22.77   
42  1 GLU K 72  ? ? -174.73 136.44  
43  1 ASP L 32  ? ? 54.41   -119.33 
44  1 PHE L 103 ? ? -153.07 65.39   
45  1 ASP L 200 ? ? 74.67   -66.31  
46  1 ILE M 5   ? ? -108.22 -82.92  
47  1 THR M 9   ? ? -87.90  -152.39 
48  1 ASN M 26  ? ? -107.13 40.26   
49  1 ALA M 83  ? ? -139.32 -116.82 
50  1 PHE N 8   ? ? -116.01 -135.23 
51  1 LYS N 107 ? ? 61.48   -140.85 
52  1 PRO N 114 ? ? -72.40  -167.48 
53  1 THR O 2   ? ? 64.23   152.32  
54  1 ASP O 3   ? ? -57.79  95.35   
55  1 TYR O 97  ? ? -145.00 -69.30  
56  1 LYS O 166 ? ? -42.39  -74.97  
57  1 ALA O 249 ? ? -92.33  54.81   
58  1 ARG P 8   ? ? 60.02   71.24   
59  1 THR P 10  ? ? -108.35 54.45   
60  1 VAL P 51  ? ? -17.05  106.21  
61  1 GLU P 63  ? ? -133.17 -40.86  
62  1 ALA P 219 ? ? -75.61  -155.23 
63  1 ASP P 221 ? ? 75.97   111.38  
64  1 ARG Q 4   ? ? -39.94  127.44  
65  1 ASN Q 38  ? ? -150.21 24.37   
66  1 LEU Q 52  ? ? 80.88   15.41   
67  1 PRO Q 183 ? ? -38.84  108.11  
68  1 VAL Q 201 ? ? -69.26  -70.45  
69  1 GLN Q 202 ? ? 140.19  -100.79 
70  1 ALA Q 205 ? ? -78.76  -126.16 
71  1 LYS Q 206 ? ? -86.10  42.80   
72  1 GLN Q 239 ? ? -65.92  81.92   
73  1 ARG R 45  ? ? 55.94   76.56   
74  1 LEU R 73  ? ? -69.28  84.48   
75  1 SER S 39  ? ? -104.38 -147.85 
76  1 ASP S 137 ? ? -129.53 -161.12 
77  1 ASP S 202 ? ? 71.42   -24.57  
78  1 SER T 9   ? ? 85.21   -2.46   
79  1 ASP T 67  ? ? 56.11   -125.61 
80  1 LYS T 100 ? ? 75.74   -55.46  
81  1 ASP T 138 ? ? -127.16 -169.39 
82  1 ASN T 203 ? ? -155.32 37.85   
83  1 LYS U 165 ? ? -104.68 46.72   
84  1 GLU U 241 ? ? -85.28  35.71   
85  1 SER V 171 ? ? 67.32   -113.81 
86  1 GLN W 31  ? ? 50.84   -110.69 
87  1 ARG W 97  ? ? -107.33 47.01   
88  1 LEU W 125 ? ? -55.26  -5.48   
89  1 ASP W 134 ? ? -103.03 -73.77  
90  1 ASP W 192 ? ? -150.23 42.64   
91  1 GLN W 203 ? ? -109.03 44.27   
92  1 ASP X 2   ? ? 127.42  -80.14  
93  1 VAL X 9   ? ? -118.95 -167.86 
94  1 SER X 31  ? ? -141.37 22.79   
95  1 GLU Y 72  ? ? -175.19 136.12  
96  1 ASP Z 32  ? ? 54.76   -120.85 
97  1 PHE Z 103 ? ? -153.08 65.11   
98  1 ASP Z 200 ? ? 75.07   -67.00  
99  1 ILE a 5   ? ? -109.47 -82.89  
100 1 THR a 9   ? ? -87.57  -152.82 
101 1 ALA a 83  ? ? -139.16 -116.89 
102 1 PHE b 8   ? ? -110.20 -154.42 
103 1 LYS b 9   ? ? -66.91  -74.63  
104 1 LYS b 107 ? ? 60.96   -140.65 
105 1 PRO b 114 ? ? -72.95  -167.61 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 67.1582 -92.5087  46.1416 0.7969 ? -0.0737 ? -0.1354 ? 0.1488 ? -0.0591 ? 0.6807 ? 1.6536 ? 
-0.4019 ? -0.0101 ? 0.8722 ? -0.0421 ? 0.7137 ? -0.1719 ? -0.0140 ? 0.0426  ? 0.0631  ? 0.0552  ? -0.2333 ? -0.2180 ? 0.1873  ? 
0.1167  ? 
2  'X-RAY DIFFRACTION' ? refined 59.7209 -88.2147  16.3955 0.8936 ? -0.1180 ? -0.0592 ? 0.1688 ? 0.0639  ? 0.6593 ? 1.6554 ? 
0.0834  ? -0.1876 ? 0.6675 ? 0.1025  ? 1.7303 ? -0.1019 ? -0.1007 ? 0.1706  ? -0.2144 ? 0.0197  ? -0.2947 ? -0.2566 ? 0.4388  ? 
0.0822  ? 
3  'X-RAY DIFFRACTION' ? refined 32.3391 -87.7700  0.9066  0.9872 ? -0.0259 ? -0.1938 ? 0.2134 ? 0.0934  ? 0.6237 ? 1.0491 ? 
0.5741  ? -0.1752 ? 1.0008 ? -0.3679 ? 1.4743 ? -0.0677 ? 0.2954  ? 0.1667  ? -0.3416 ? 0.1432  ? -0.1636 ? -0.1152 ? 0.1024  ? 
-0.0754 ? 
4  'X-RAY DIFFRACTION' ? refined 3.1981  -90.6450  13.5315 0.9658 ? 0.1055  ? -0.3628 ? 0.1802 ? 0.1219  ? 0.7934 ? 1.1332 ? 
0.1207  ? 0.1478  ? 0.8201 ? -0.1906 ? 0.3398 ? -0.1277 ? -0.0966 ? 0.1799  ? -0.2008 ? 0.0385  ? 0.4016  ? -0.1951 ? -0.0783 ? 
0.0892  ? 
5  'X-RAY DIFFRACTION' ? refined -2.9845 -95.1472  45.5458 0.6622 ? 0.1325  ? -0.1356 ? 0.1522 ? -0.0258 ? 0.9122 ? 0.5744 ? 
0.1270  ? -0.1516 ? 0.4803 ? -0.1716 ? 1.0796 ? -0.1179 ? 0.0102  ? 0.1169  ? -0.1512 ? 0.0077  ? 0.3728  ? -0.2707 ? -0.2826 ? 
0.1102  ? 
6  'X-RAY DIFFRACTION' ? refined 15.5701 -95.8136  69.9020 0.8379 ? 0.0591  ? 0.0043  ? 0.0799 ? -0.1337 ? 0.5322 ? 0.9664 ? 
0.0522  ? 0.1214  ? 0.6518 ? -0.4503 ? 0.5019 ? 0.0221  ? -0.1960 ? 0.1912  ? 0.1675  ? 0.0043  ? 0.3805  ? -0.1241 ? -0.1139 ? 
-0.0263 ? 
7  'X-RAY DIFFRACTION' ? refined 48.0186 -94.0513  71.3167 0.9097 ? 0.0044  ? -0.2175 ? 0.0631 ? -0.0873 ? 0.4932 ? 0.6212 ? 
-0.0777 ? -0.2232 ? 1.3338 ? 0.0642  ? 1.4184 ? 0.1111  ? -0.0580 ? 0.0695  ? 0.2575  ? -0.0004 ? -0.0726 ? -0.0299 ? 0.0375  ? 
-0.1107 ? 
8  'X-RAY DIFFRACTION' ? refined 67.8864 -130.7517 47.9969 0.6982 ? 0.0038  ? -0.2035 ? 0.2513 ? -0.0694 ? 0.6581 ? 1.4419 ? 
-0.1595 ? -0.3173 ? 0.4668 ? 0.1199  ? 0.1271 ? 0.0952  ? 0.0586  ? -0.0770 ? 0.1175  ? -0.0207 ? -0.2930 ? -0.0528 ? 0.0822  ? 
-0.0746 ? 
9  'X-RAY DIFFRACTION' ? refined 68.7041 -127.8691 20.5888 0.6923 ? 0.0164  ? -0.0021 ? 0.2613 ? -0.0345 ? 0.6147 ? 2.4040 ? 
-0.2928 ? 0.0129  ? 2.6857 ? -0.2834 ? 0.1358 ? 0.0876  ? 0.1638  ? -0.0981 ? -0.1958 ? -0.1459 ? -0.4028 ? -0.0279 ? 0.1699  ? 
0.0584  ? 
10 'X-RAY DIFFRACTION' ? refined 44.8370 -127.1225 -0.9883 1.0110 ? -0.0392 ? -0.1088 ? 0.1482 ? 0.0376  ? 0.4856 ? 1.6122 ? 
0.0044  ? 0.1568  ? 1.9914 ? 0.0083  ? 1.3719 ? -0.0196 ? 0.2145  ? -0.1544 ? -0.4764 ? 0.0608  ? -0.0175 ? 0.1955  ? 0.0975  ? 
-0.0412 ? 
11 'X-RAY DIFFRACTION' ? refined 11.2217 -131.6752 2.2933  0.9211 ? 0.0104  ? -0.3917 ? 0.2467 ? 0.0401  ? 0.6771 ? 2.8708 ? 
1.8845  ? 0.0063  ? 2.1700 ? 0.7311  ? 0.7895 ? -0.1784 ? 0.4050  ? 0.0112  ? -0.5077 ? 0.1593  ? 0.4324  ? -0.0417 ? -0.1247 ? 
0.0191  ? 
12 'X-RAY DIFFRACTION' ? refined -4.0360 -135.3042 28.2404 0.6791 ? 0.0685  ? -0.2435 ? 0.1907 ? 0.0611  ? 0.7447 ? 1.5933 ? 
-0.0471 ? 0.1831  ? 1.0851 ? 0.3476  ? 0.3119 ? 0.1480  ? 0.1494  ? 0.0129  ? -0.2038 ? -0.0315 ? 0.4446  ? 0.0391  ? -0.1150 ? 
-0.1165 ? 
13 'X-RAY DIFFRACTION' ? refined 8.2359  -138.8546 60.2327 0.7321 ? -0.0256 ? -0.0609 ? 0.1301 ? -0.0055 ? 0.4901 ? 1.3115 ? 
-0.0777 ? -0.2918 ? 2.1324 ? -0.2395 ? 0.4088 ? 0.0476  ? -0.1649 ? -0.0258 ? 0.3183  ? -0.0219 ? 0.1943  ? 0.0864  ? -0.0979 ? 
-0.0257 ? 
14 'X-RAY DIFFRACTION' ? refined 40.3636 -134.9018 70.9145 0.8597 ? 0.0073  ? -0.2020 ? 0.1520 ? -0.0202 ? 0.3566 ? 1.5367 ? 
-0.0262 ? -0.6486 ? 1.5879 ? -0.1498 ? 0.3220 ? 0.0544  ? -0.1652 ? 0.0181  ? 0.3730  ? 0.0242  ? -0.0983 ? -0.0168 ? 0.0917  ? 
-0.0786 ? 
15 'X-RAY DIFFRACTION' ? refined 2.6744  -207.9212 36.4256 0.9119 ? -0.1180 ? -0.3106 ? 0.1320 ? 0.0829  ? 0.8362 ? 0.9211 ? 
-0.2765 ? -0.4918 ? 1.0135 ? 0.1647  ? 1.0229 ? -0.0296 ? 0.0484  ? -0.0469 ? 0.0576  ? 0.0296  ? 0.2809  ? 0.2831  ? -0.1825 ? 
-0.0001 ? 
16 'X-RAY DIFFRACTION' ? refined 8.8072  -206.6555 6.2679  1.0136 ? -0.0084 ? -0.3521 ? 0.2059 ? -0.0991 ? 0.7772 ? 0.6669 ? 
0.1529  ? 0.3590  ? 0.8962 ? -0.1789 ? 1.7377 ? -0.1075 ? -0.0270 ? -0.1507 ? -0.0633 ? 0.0602  ? 0.1740  ? 0.1286  ? -0.4299 ? 
0.0473  ? 
17 'X-RAY DIFFRACTION' ? refined 35.9258 -204.6529 -9.7508 1.3005 ? 0.1125  ? -0.3255 ? 0.2061 ? -0.1656 ? 0.7500 ? 0.7934 ? 
0.1566  ? 0.3176  ? 0.8438 ? -0.1402 ? 1.1392 ? 0.0671  ? 0.2302  ? -0.1569 ? -0.4965 ? 0.0581  ? 0.3773  ? 0.1845  ? -0.0105 ? 
-0.1253 ? 
18 'X-RAY DIFFRACTION' ? refined 65.4810 -204.0000 2.8499  1.0638 ? 0.2206  ? 0.0337  ? 0.1909 ? -0.1259 ? 0.7204 ? 0.9417 ? 
0.3451  ? 0.3724  ? 1.1153 ? 0.6117  ? 0.7751 ? 0.0428  ? -0.0040 ? -0.0653 ? -0.5297 ? -0.0654 ? -0.3169 ? 0.1252  ? 0.0867  ? 
0.0226  ? 
19 'X-RAY DIFFRACTION' ? refined 72.7157 -205.0976 34.7910 0.8352 ? 0.2267  ? -0.2371 ? 0.3083 ? -0.2190 ? 1.1680 ? 0.7550 ? 
0.7828  ? -0.0028 ? 0.9985 ? -0.2292 ? 0.7138 ? 0.0193  ? 0.1503  ? -0.3860 ? -0.1267 ? 0.1300  ? -0.5798 ? 0.3252  ? 0.3421  ? 
-0.1493 ? 
20 'X-RAY DIFFRACTION' ? refined 55.0707 -208.7744 59.2090 1.0936 ? 0.1153  ? -0.4846 ? 0.2124 ? 0.0961  ? 0.8074 ? 1.0470 ? 
0.7305  ? -0.0949 ? 0.6803 ? 0.1981  ? 0.4804 ? 0.1125  ? -0.2566 ? -0.4728 ? 0.1515  ? -0.0038 ? -0.4366 ? 0.2222  ? 0.2407  ? 
-0.1087 ? 
21 'X-RAY DIFFRACTION' ? refined 22.7115 -210.9465 60.8872 1.0837 ? -0.0198 ? -0.2912 ? 0.0647 ? 0.1184  ? 0.6662 ? 0.6921 ? 
-0.2916 ? 0.0103  ? 1.1314 ? -0.5557 ? 1.3038 ? 0.0424  ? -0.1430 ? -0.1364 ? 0.1525  ? 0.0258  ? 0.1681  ? 0.1712  ? 0.0095  ? 
-0.0682 ? 
22 'X-RAY DIFFRACTION' ? refined 2.1665  -170.6304 45.0332 0.7465 ? -0.0522 ? -0.1867 ? 0.2054 ? 0.0949  ? 0.7171 ? 0.8292 ? 
-0.3441 ? 0.0594  ? 0.2334 ? 0.0172  ? 0.0899 ? 0.0815  ? 0.0903  ? -0.0968 ? 0.0639  ? -0.0460 ? 0.2351  ? 0.1723  ? -0.0985 ? 
-0.0355 ? 
23 'X-RAY DIFFRACTION' ? refined 0.3906  -168.5135 17.5820 0.7908 ? 0.0083  ? -0.3844 ? 0.2365 ? -0.0165 ? 0.6570 ? 1.2968 ? 
-0.9990 ? 0.2824  ? 1.9837 ? 0.0631  ? 0.9552 ? 0.0329  ? 0.1846  ? -0.0562 ? -0.1204 ? -0.0199 ? 0.3785  ? -0.0336 ? -0.2182 ? 
-0.0130 ? 
24 'X-RAY DIFFRACTION' ? refined 23.5055 -165.4412 -4.2804 1.0735 ? -0.0109 ? -0.3338 ? 0.1807 ? -0.0371 ? 0.4854 ? 1.6079 ? 
-0.0879 ? -0.3669 ? 2.2099 ? 0.0056  ? 1.0812 ? -0.0446 ? 0.2894  ? 0.1116  ? -0.3926 ? 0.0727  ? 0.0371  ? -0.1824 ? 0.0266  ? 
-0.0280 ? 
25 'X-RAY DIFFRACTION' ? refined 57.3222 -161.5612 -0.7969 0.7793 ? 0.0932  ? 0.0829  ? 0.3817 ? -0.0982 ? 0.6246 ? 2.0346 ? 
1.6056  ? 0.1755  ? 3.0388 ? -0.5597 ? 1.0365 ? -0.1330 ? 0.3138  ? -0.0296 ? -0.5092 ? 0.1977  ? -0.3920 ? 0.0319  ? 0.3136  ? 
-0.0647 ? 
26 'X-RAY DIFFRACTION' ? refined 73.3271 -162.5366 25.0064 0.6817 ? 0.1141  ? -0.0509 ? 0.2346 ? -0.0736 ? 0.7119 ? 1.5602 ? 
-0.5165 ? -0.1112 ? 1.4712 ? -0.5330 ? 0.5040 ? 0.1125  ? 0.1191  ? 0.1062  ? -0.3023 ? -0.1292 ? -0.5111 ? -0.0074 ? 0.0918  ? 
0.0166  ? 
27 'X-RAY DIFFRACTION' ? refined 62.1800 -164.7204 57.3693 0.7515 ? 0.0538  ? -0.3153 ? 0.1711 ? -0.0378 ? 0.5743 ? 0.9672 ? 
0.2736  ? 0.3502  ? 1.5520 ? 0.1634  ? 0.8554 ? 0.0064  ? -0.0461 ? -0.0571 ? 0.3325  ? 0.0413  ? -0.3828 ? -0.0226 ? 0.0549  ? 
-0.0477 ? 
28 'X-RAY DIFFRACTION' ? refined 30.4593 -170.5491 67.7923 0.8766 ? 0.0052  ? -0.1654 ? 0.2023 ? 0.0735  ? 0.4118 ? 1.1856 ? 
-0.1202 ? 0.2169  ? 1.6291 ? 0.0929  ? 0.7137 ? 0.0538  ? -0.1458 ? -0.1286 ? 0.1643  ? 0.0685  ? 0.0979  ? 0.0959  ? -0.1077 ? 
-0.1224 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? A 1 ? ? ? A 250 ? ? ? 
2  'X-RAY DIFFRACTION' 2  ? ? B 1 ? ? ? B 244 ? ? ? 
3  'X-RAY DIFFRACTION' 3  ? ? C 1 ? ? ? C 240 ? ? ? 
4  'X-RAY DIFFRACTION' 4  ? ? D 1 ? ? ? D 242 ? ? ? 
5  'X-RAY DIFFRACTION' 5  ? ? E 3 ? ? ? E 233 ? ? ? 
6  'X-RAY DIFFRACTION' 6  ? ? F 2 ? ? ? F 244 ? ? ? 
7  'X-RAY DIFFRACTION' 7  ? ? G 2 ? ? ? G 242 ? ? ? 
8  'X-RAY DIFFRACTION' 8  ? ? H 1 ? ? ? H 222 ? ? ? 
9  'X-RAY DIFFRACTION' 9  ? ? I 1 ? ? ? I 204 ? ? ? 
10 'X-RAY DIFFRACTION' 10 ? ? J 1 ? ? ? J 195 ? ? ? 
11 'X-RAY DIFFRACTION' 11 ? ? K 1 ? ? ? K 212 ? ? ? 
12 'X-RAY DIFFRACTION' 12 ? ? L 1 ? ? ? L 222 ? ? ? 
13 'X-RAY DIFFRACTION' 13 ? ? M 1 ? ? ? M 233 ? ? ? 
14 'X-RAY DIFFRACTION' 14 ? ? N 1 ? ? ? N 196 ? ? ? 
15 'X-RAY DIFFRACTION' 15 ? ? O 1 ? ? ? O 250 ? ? ? 
16 'X-RAY DIFFRACTION' 16 ? ? P 1 ? ? ? P 244 ? ? ? 
17 'X-RAY DIFFRACTION' 17 ? ? Q 1 ? ? ? Q 240 ? ? ? 
18 'X-RAY DIFFRACTION' 18 ? ? R 1 ? ? ? R 242 ? ? ? 
19 'X-RAY DIFFRACTION' 19 ? ? S 3 ? ? ? S 233 ? ? ? 
20 'X-RAY DIFFRACTION' 20 ? ? T 2 ? ? ? T 244 ? ? ? 
21 'X-RAY DIFFRACTION' 21 ? ? U 2 ? ? ? U 242 ? ? ? 
22 'X-RAY DIFFRACTION' 22 ? ? V 1 ? ? ? V 222 ? ? ? 
23 'X-RAY DIFFRACTION' 23 ? ? W 1 ? ? ? W 204 ? ? ? 
24 'X-RAY DIFFRACTION' 24 ? ? X 1 ? ? ? X 195 ? ? ? 
25 'X-RAY DIFFRACTION' 25 ? ? Y 1 ? ? ? Y 212 ? ? ? 
26 'X-RAY DIFFRACTION' 26 ? ? Z 1 ? ? ? Z 222 ? ? ? 
27 'X-RAY DIFFRACTION' 27 ? ? a 1 ? ? ? a 233 ? ? ? 
28 'X-RAY DIFFRACTION' 28 ? ? b 1 ? ? ? b 196 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 B MET 0   ? B  MET 1   
2   1 Y 1 B LYS 245 ? B  LYS 246 
3   1 Y 1 B LYS 246 ? B  LYS 247 
4   1 Y 1 B ASP 247 ? B  ASP 248 
5   1 Y 1 B GLU 248 ? B  GLU 249 
6   1 Y 1 B ASP 249 ? B  ASP 250 
7   1 Y 1 B GLU 250 ? B  GLU 251 
8   1 Y 1 B GLU 251 ? B  GLU 252 
9   1 Y 1 B ALA 252 ? B  ALA 253 
10  1 Y 1 B ASP 253 ? B  ASP 254 
11  1 Y 1 B GLU 254 ? B  GLU 255 
12  1 Y 1 B ASP 255 ? B  ASP 256 
13  1 Y 1 B MET 256 ? B  MET 257 
14  1 Y 1 B LYS 257 ? B  LYS 258 
15  1 Y 1 C MET -1  ? C  MET 1   
16  1 Y 1 C SER 0   ? C  SER 2   
17  1 Y 1 C GLN 241 ? C  GLN 243 
18  1 Y 1 C GLN 242 ? C  GLN 244 
19  1 Y 1 C GLU 243 ? C  GLU 245 
20  1 Y 1 C GLN 244 ? C  GLN 246 
21  1 Y 1 C ASP 245 ? C  ASP 247 
22  1 Y 1 C LYS 246 ? C  LYS 248 
23  1 Y 1 C LYS 247 ? C  LYS 249 
24  1 Y 1 C LYS 248 ? C  LYS 250 
25  1 Y 1 C LYS 249 ? C  LYS 251 
26  1 Y 1 C SER 250 ? C  SER 252 
27  1 Y 1 C ASN 251 ? C  ASN 253 
28  1 Y 1 C HIS 252 ? C  HIS 254 
29  1 Y 1 D MET -7  ? D  MET 1   
30  1 Y 1 D PHE -6  ? D  PHE 2   
31  1 Y 1 D LEU -5  ? D  LEU 3   
32  1 Y 1 D THR -4  ? D  THR 4   
33  1 Y 1 D ARG -3  ? D  ARG 5   
34  1 Y 1 D SER -2  ? D  SER 6   
35  1 Y 1 D GLU -1  ? D  GLU 7   
36  1 Y 1 D TYR 0   ? D  TYR 8   
37  1 Y 1 D GLY 118 ? D  GLY 126 
38  1 Y 1 D ALA 119 ? D  ALA 127 
39  1 Y 1 D SER 120 ? D  SER 128 
40  1 Y 1 D GLY 121 ? D  GLY 129 
41  1 Y 1 D GLU 122 ? D  GLU 130 
42  1 Y 1 D GLU 123 ? D  GLU 131 
43  1 Y 1 D ARG 124 ? D  ARG 132 
44  1 Y 1 D SER 243 ? D  SER 251 
45  1 Y 1 D PRO 244 ? D  PRO 252 
46  1 Y 1 D GLU 245 ? D  GLU 253 
47  1 Y 1 D GLU 246 ? D  GLU 254 
48  1 Y 1 D ALA 247 ? D  ALA 255 
49  1 Y 1 D ASP 248 ? D  ASP 256 
50  1 Y 1 D VAL 249 ? D  VAL 257 
51  1 Y 1 D GLU 250 ? D  GLU 258 
52  1 Y 1 D MET 251 ? D  MET 259 
53  1 Y 1 D SER 252 ? D  SER 260 
54  1 Y 1 E MET 0   ? E  MET 1   
55  1 Y 1 E PHE 1   ? E  PHE 2   
56  1 Y 1 E ARG 2   ? E  ARG 3   
57  1 Y 1 F MET -3  ? F  MET 1   
58  1 Y 1 F THR -2  ? F  THR 2   
59  1 Y 1 F SER -1  ? F  SER 3   
60  1 Y 1 F ILE 0   ? F  ILE 4   
61  1 Y 1 F GLY 1   ? F  GLY 5   
62  1 Y 1 F GLY 245 ? F  GLY 249 
63  1 Y 1 F ASP 246 ? F  ASP 250 
64  1 Y 1 F ASP 247 ? F  ASP 251 
65  1 Y 1 F ASP 248 ? F  ASP 252 
66  1 Y 1 F GLU 249 ? F  GLU 253 
67  1 Y 1 F ASP 250 ? F  ASP 254 
68  1 Y 1 F GLU 251 ? F  GLU 255 
69  1 Y 1 F ASP 252 ? F  ASP 256 
70  1 Y 1 F ASP 253 ? F  ASP 257 
71  1 Y 1 F SER 254 ? F  SER 258 
72  1 Y 1 F ASP 255 ? F  ASP 259 
73  1 Y 1 F ASN 256 ? F  ASN 260 
74  1 Y 1 F VAL 257 ? F  VAL 261 
75  1 Y 1 F MET 258 ? F  MET 262 
76  1 Y 1 F SER 259 ? F  SER 263 
77  1 Y 1 F SER 260 ? F  SER 264 
78  1 Y 1 F ASP 261 ? F  ASP 265 
79  1 Y 1 F ASP 262 ? F  ASP 266 
80  1 Y 1 F GLU 263 ? F  GLU 267 
81  1 Y 1 F ASN 264 ? F  ASN 268 
82  1 Y 1 F ALA 265 ? F  ALA 269 
83  1 Y 1 F PRO 266 ? F  PRO 270 
84  1 Y 1 F VAL 267 ? F  VAL 271 
85  1 Y 1 F ALA 268 ? F  ALA 272 
86  1 Y 1 F THR 269 ? F  THR 273 
87  1 Y 1 F ASN 270 ? F  ASN 274 
88  1 Y 1 F ALA 271 ? F  ALA 275 
89  1 Y 1 F ASN 272 ? F  ASN 276 
90  1 Y 1 F ALA 273 ? F  ALA 277 
91  1 Y 1 F THR 274 ? F  THR 278 
92  1 Y 1 F THR 275 ? F  THR 279 
93  1 Y 1 F ASP 276 ? F  ASP 280 
94  1 Y 1 F GLN 277 ? F  GLN 281 
95  1 Y 1 F GLU 278 ? F  GLU 282 
96  1 Y 1 F GLY 279 ? F  GLY 283 
97  1 Y 1 F ASP 280 ? F  ASP 284 
98  1 Y 1 F ILE 281 ? F  ILE 285 
99  1 Y 1 F HIS 282 ? F  HIS 286 
100 1 Y 1 F LEU 283 ? F  LEU 287 
101 1 Y 1 F GLU 284 ? F  GLU 288 
102 1 Y 1 G MET -8  ? G  MET 1   
103 1 Y 1 G SER -7  ? G  SER 2   
104 1 Y 1 G GLY -6  ? G  GLY 3   
105 1 Y 1 G ALA -5  ? G  ALA 4   
106 1 Y 1 G ALA -4  ? G  ALA 5   
107 1 Y 1 G ALA -3  ? G  ALA 6   
108 1 Y 1 G ALA -2  ? G  ALA 7   
109 1 Y 1 G SER -1  ? G  SER 8   
110 1 Y 1 G ALA 0   ? G  ALA 9   
111 1 Y 1 G ALA 1   ? G  ALA 10  
112 1 Y 1 G ASP 243 ? G  ASP 252 
113 1 Y 1 H ILE 223 ? H  ILE 222 
114 1 Y 1 H GLN 224 ? H  GLN 223 
115 1 Y 1 H GLU 225 ? H  GLU 224 
116 1 Y 1 H GLU 226 ? H  GLU 225 
117 1 Y 1 H GLN 227 ? H  GLN 226 
118 1 Y 1 H VAL 228 ? H  VAL 227 
119 1 Y 1 H ASP 229 ? H  ASP 228 
120 1 Y 1 H ILE 230 ? H  ILE 229 
121 1 Y 1 H THR 231 ? H  THR 230 
122 1 Y 1 H ALA 232 ? H  ALA 231 
123 1 Y 1 I MET 0   ? I  MET 1   
124 1 Y 1 J GLN 196 ? J  GLN 196 
125 1 Y 1 J ALA 197 ? J  ALA 197 
126 1 Y 1 J GLN 198 ? J  GLN 198 
127 1 Y 1 M THR -12 ? M  THR 1   
128 1 Y 1 M GLN -11 ? M  GLN 2   
129 1 Y 1 M ILE -10 ? M  ILE 3   
130 1 Y 1 M ALA -9  ? M  ALA 4   
131 1 Y 1 M ASN -8  ? M  ASN 5   
132 1 Y 1 M ALA -7  ? M  ALA 6   
133 1 Y 1 M GLY -6  ? M  GLY 7   
134 1 Y 1 M ALA -5  ? M  ALA 8   
135 1 Y 1 M SER -4  ? M  SER 9   
136 1 Y 1 M PRO -3  ? M  PRO 10  
137 1 Y 1 M MET -2  ? M  MET 11  
138 1 Y 1 M VAL -1  ? M  VAL 12  
139 1 Y 1 M ASN 0   ? M  ASN 13  
140 1 Y 1 P MET 0   ? P  MET 1   
141 1 Y 1 P LYS 245 ? P  LYS 246 
142 1 Y 1 P LYS 246 ? P  LYS 247 
143 1 Y 1 P ASP 247 ? P  ASP 248 
144 1 Y 1 P GLU 248 ? P  GLU 249 
145 1 Y 1 P ASP 249 ? P  ASP 250 
146 1 Y 1 P GLU 250 ? P  GLU 251 
147 1 Y 1 P GLU 251 ? P  GLU 252 
148 1 Y 1 P ALA 252 ? P  ALA 253 
149 1 Y 1 P ASP 253 ? P  ASP 254 
150 1 Y 1 P GLU 254 ? P  GLU 255 
151 1 Y 1 P ASP 255 ? P  ASP 256 
152 1 Y 1 P MET 256 ? P  MET 257 
153 1 Y 1 P LYS 257 ? P  LYS 258 
154 1 Y 1 Q MET -1  ? Q  MET 1   
155 1 Y 1 Q SER 0   ? Q  SER 2   
156 1 Y 1 Q GLN 241 ? Q  GLN 243 
157 1 Y 1 Q GLN 242 ? Q  GLN 244 
158 1 Y 1 Q GLU 243 ? Q  GLU 245 
159 1 Y 1 Q GLN 244 ? Q  GLN 246 
160 1 Y 1 Q ASP 245 ? Q  ASP 247 
161 1 Y 1 Q LYS 246 ? Q  LYS 248 
162 1 Y 1 Q LYS 247 ? Q  LYS 249 
163 1 Y 1 Q LYS 248 ? Q  LYS 250 
164 1 Y 1 Q LYS 249 ? Q  LYS 251 
165 1 Y 1 Q SER 250 ? Q  SER 252 
166 1 Y 1 Q ASN 251 ? Q  ASN 253 
167 1 Y 1 Q HIS 252 ? Q  HIS 254 
168 1 Y 1 R MET -7  ? R  MET 1   
169 1 Y 1 R PHE -6  ? R  PHE 2   
170 1 Y 1 R LEU -5  ? R  LEU 3   
171 1 Y 1 R THR -4  ? R  THR 4   
172 1 Y 1 R ARG -3  ? R  ARG 5   
173 1 Y 1 R SER -2  ? R  SER 6   
174 1 Y 1 R GLU -1  ? R  GLU 7   
175 1 Y 1 R TYR 0   ? R  TYR 8   
176 1 Y 1 R GLY 118 ? R  GLY 126 
177 1 Y 1 R ALA 119 ? R  ALA 127 
178 1 Y 1 R SER 120 ? R  SER 128 
179 1 Y 1 R GLY 121 ? R  GLY 129 
180 1 Y 1 R GLU 122 ? R  GLU 130 
181 1 Y 1 R GLU 123 ? R  GLU 131 
182 1 Y 1 R ARG 124 ? R  ARG 132 
183 1 Y 1 R SER 243 ? R  SER 251 
184 1 Y 1 R PRO 244 ? R  PRO 252 
185 1 Y 1 R GLU 245 ? R  GLU 253 
186 1 Y 1 R GLU 246 ? R  GLU 254 
187 1 Y 1 R ALA 247 ? R  ALA 255 
188 1 Y 1 R ASP 248 ? R  ASP 256 
189 1 Y 1 R VAL 249 ? R  VAL 257 
190 1 Y 1 R GLU 250 ? R  GLU 258 
191 1 Y 1 R MET 251 ? R  MET 259 
192 1 Y 1 R SER 252 ? R  SER 260 
193 1 Y 1 S MET 0   ? S  MET 1   
194 1 Y 1 S PHE 1   ? S  PHE 2   
195 1 Y 1 S ARG 2   ? S  ARG 3   
196 1 Y 1 T MET -3  ? T  MET 1   
197 1 Y 1 T THR -2  ? T  THR 2   
198 1 Y 1 T SER -1  ? T  SER 3   
199 1 Y 1 T ILE 0   ? T  ILE 4   
200 1 Y 1 T GLY 1   ? T  GLY 5   
201 1 Y 1 T GLY 245 ? T  GLY 249 
202 1 Y 1 T ASP 246 ? T  ASP 250 
203 1 Y 1 T ASP 247 ? T  ASP 251 
204 1 Y 1 T ASP 248 ? T  ASP 252 
205 1 Y 1 T GLU 249 ? T  GLU 253 
206 1 Y 1 T ASP 250 ? T  ASP 254 
207 1 Y 1 T GLU 251 ? T  GLU 255 
208 1 Y 1 T ASP 252 ? T  ASP 256 
209 1 Y 1 T ASP 253 ? T  ASP 257 
210 1 Y 1 T SER 254 ? T  SER 258 
211 1 Y 1 T ASP 255 ? T  ASP 259 
212 1 Y 1 T ASN 256 ? T  ASN 260 
213 1 Y 1 T VAL 257 ? T  VAL 261 
214 1 Y 1 T MET 258 ? T  MET 262 
215 1 Y 1 T SER 259 ? T  SER 263 
216 1 Y 1 T SER 260 ? T  SER 264 
217 1 Y 1 T ASP 261 ? T  ASP 265 
218 1 Y 1 T ASP 262 ? T  ASP 266 
219 1 Y 1 T GLU 263 ? T  GLU 267 
220 1 Y 1 T ASN 264 ? T  ASN 268 
221 1 Y 1 T ALA 265 ? T  ALA 269 
222 1 Y 1 T PRO 266 ? T  PRO 270 
223 1 Y 1 T VAL 267 ? T  VAL 271 
224 1 Y 1 T ALA 268 ? T  ALA 272 
225 1 Y 1 T THR 269 ? T  THR 273 
226 1 Y 1 T ASN 270 ? T  ASN 274 
227 1 Y 1 T ALA 271 ? T  ALA 275 
228 1 Y 1 T ASN 272 ? T  ASN 276 
229 1 Y 1 T ALA 273 ? T  ALA 277 
230 1 Y 1 T THR 274 ? T  THR 278 
231 1 Y 1 T THR 275 ? T  THR 279 
232 1 Y 1 T ASP 276 ? T  ASP 280 
233 1 Y 1 T GLN 277 ? T  GLN 281 
234 1 Y 1 T GLU 278 ? T  GLU 282 
235 1 Y 1 T GLY 279 ? T  GLY 283 
236 1 Y 1 T ASP 280 ? T  ASP 284 
237 1 Y 1 T ILE 281 ? T  ILE 285 
238 1 Y 1 T HIS 282 ? T  HIS 286 
239 1 Y 1 T LEU 283 ? T  LEU 287 
240 1 Y 1 T GLU 284 ? T  GLU 288 
241 1 Y 1 U MET -8  ? U  MET 1   
242 1 Y 1 U SER -7  ? U  SER 2   
243 1 Y 1 U GLY -6  ? U  GLY 3   
244 1 Y 1 U ALA -5  ? U  ALA 4   
245 1 Y 1 U ALA -4  ? U  ALA 5   
246 1 Y 1 U ALA -3  ? U  ALA 6   
247 1 Y 1 U ALA -2  ? U  ALA 7   
248 1 Y 1 U SER -1  ? U  SER 8   
249 1 Y 1 U ALA 0   ? U  ALA 9   
250 1 Y 1 U ALA 1   ? U  ALA 10  
251 1 Y 1 U ASP 243 ? U  ASP 252 
252 1 Y 1 V ILE 223 ? V  ILE 222 
253 1 Y 1 V GLN 224 ? V  GLN 223 
254 1 Y 1 V GLU 225 ? V  GLU 224 
255 1 Y 1 V GLU 226 ? V  GLU 225 
256 1 Y 1 V GLN 227 ? V  GLN 226 
257 1 Y 1 V VAL 228 ? V  VAL 227 
258 1 Y 1 V ASP 229 ? V  ASP 228 
259 1 Y 1 V ILE 230 ? V  ILE 229 
260 1 Y 1 V THR 231 ? V  THR 230 
261 1 Y 1 V ALA 232 ? V  ALA 231 
262 1 Y 1 W MET 0   ? W  MET 1   
263 1 Y 1 X GLN 196 ? X  GLN 196 
264 1 Y 1 X ALA 197 ? X  ALA 197 
265 1 Y 1 X GLN 198 ? X  GLN 198 
266 1 Y 1 a THR -12 ? AA THR 1   
267 1 Y 1 a GLN -11 ? AA GLN 2   
268 1 Y 1 a ILE -10 ? AA ILE 3   
269 1 Y 1 a ALA -9  ? AA ALA 4   
270 1 Y 1 a ASN -8  ? AA ASN 5   
271 1 Y 1 a ALA -7  ? AA ALA 6   
272 1 Y 1 a GLY -6  ? AA GLY 7   
273 1 Y 1 a ALA -5  ? AA ALA 8   
274 1 Y 1 a SER -4  ? AA SER 9   
275 1 Y 1 a PRO -3  ? AA PRO 10  
276 1 Y 1 a MET -2  ? AA MET 11  
277 1 Y 1 a VAL -1  ? AA VAL 12  
278 1 Y 1 a ASN 0   ? AA ASN 13  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H71 C5   C  N N 1   
A1H71 C6   C  N N 2   
A1H71 C7   C  N N 3   
A1H71 C8   C  N N 4   
A1H71 C15  C  N N 5   
A1H71 C17  C  N N 6   
A1H71 C21  C  N R 7   
A1H71 C28  C  N S 8   
A1H71 C19  C  N N 9   
A1H71 C18  C  N N 10  
A1H71 C16  C  N N 11  
A1H71 C14  C  N N 12  
A1H71 O20  O  N N 13  
A1H71 N13  N  N N 14  
A1H71 C12  C  N S 15  
A1H71 C23  C  N N 16  
A1H71 O22  O  N N 17  
A1H71 C11  C  N N 18  
A1H71 O24  O  N N 19  
A1H71 N10  N  N N 20  
A1H71 C9   C  N S 21  
A1H71 C25  C  N N 22  
A1H71 O26  O  N N 23  
A1H71 N27  N  N N 24  
A1H71 N4   N  N N 25  
A1H71 C3   C  N N 26  
A1H71 O37  O  N N 27  
A1H71 C2   C  N N 28  
A1H71 C1   C  N R 29  
A1H71 OG1  O  N N 30  
A1H71 CB   C  N R 31  
A1H71 CG2  C  N N 32  
A1H71 CA   C  N S 33  
A1H71 C    C  N N 34  
A1H71 O    O  N N 35  
A1H71 N    N  N N 36  
A1H71 C29  C  N N 37  
A1H71 C30  C  Y N 38  
A1H71 C35  C  Y N 39  
A1H71 C34  C  Y N 40  
A1H71 C33  C  Y N 41  
A1H71 C32  C  Y N 42  
A1H71 C31  C  Y N 43  
A1H71 H1   H  N N 44  
A1H71 H2   H  N N 45  
A1H71 H3   H  N N 46  
A1H71 H4   H  N N 47  
A1H71 H5   H  N N 48  
A1H71 H6   H  N N 49  
A1H71 H7   H  N N 50  
A1H71 H8   H  N N 51  
A1H71 H9   H  N N 52  
A1H71 H10  H  N N 53  
A1H71 H11  H  N N 54  
A1H71 H12  H  N N 55  
A1H71 H13  H  N N 56  
A1H71 H14  H  N N 57  
A1H71 H15  H  N N 58  
A1H71 H16  H  N N 59  
A1H71 H17  H  N N 60  
A1H71 H18  H  N N 61  
A1H71 H19  H  N N 62  
A1H71 H20  H  N N 63  
A1H71 H21  H  N N 64  
A1H71 H22  H  N N 65  
A1H71 H23  H  N N 66  
A1H71 H24  H  N N 67  
A1H71 H25  H  N N 68  
A1H71 H26  H  N N 69  
A1H71 H27  H  N N 70  
A1H71 H28  H  N N 71  
A1H71 H29  H  N N 72  
A1H71 H30  H  N N 73  
A1H71 H31  H  N N 74  
A1H71 H32  H  N N 75  
A1H71 H33  H  N N 76  
A1H71 H34  H  N N 77  
A1H71 H35  H  N N 78  
A1H71 H36  H  N N 79  
A1H71 H37  H  N N 80  
A1H71 H38  H  N N 81  
A1H71 H39  H  N N 82  
A1H71 H40  H  N N 83  
A1H71 H41  H  N N 84  
A1H71 H42  H  N N 85  
A1H71 H44  H  N N 86  
A1H71 H45  H  N N 87  
A1H71 H46  H  N N 88  
A1H71 H47  H  N N 89  
A1H71 H48  H  N N 90  
A1H71 H49  H  N N 91  
A1H71 H50  H  N N 92  
ALA   N    N  N N 93  
ALA   CA   C  N S 94  
ALA   C    C  N N 95  
ALA   O    O  N N 96  
ALA   CB   C  N N 97  
ALA   OXT  O  N N 98  
ALA   H    H  N N 99  
ALA   H2   H  N N 100 
ALA   HA   H  N N 101 
ALA   HB1  H  N N 102 
ALA   HB2  H  N N 103 
ALA   HB3  H  N N 104 
ALA   HXT  H  N N 105 
ARG   N    N  N N 106 
ARG   CA   C  N S 107 
ARG   C    C  N N 108 
ARG   O    O  N N 109 
ARG   CB   C  N N 110 
ARG   CG   C  N N 111 
ARG   CD   C  N N 112 
ARG   NE   N  N N 113 
ARG   CZ   C  N N 114 
ARG   NH1  N  N N 115 
ARG   NH2  N  N N 116 
ARG   OXT  O  N N 117 
ARG   H    H  N N 118 
ARG   H2   H  N N 119 
ARG   HA   H  N N 120 
ARG   HB2  H  N N 121 
ARG   HB3  H  N N 122 
ARG   HG2  H  N N 123 
ARG   HG3  H  N N 124 
ARG   HD2  H  N N 125 
ARG   HD3  H  N N 126 
ARG   HE   H  N N 127 
ARG   HH11 H  N N 128 
ARG   HH12 H  N N 129 
ARG   HH21 H  N N 130 
ARG   HH22 H  N N 131 
ARG   HXT  H  N N 132 
ASN   N    N  N N 133 
ASN   CA   C  N S 134 
ASN   C    C  N N 135 
ASN   O    O  N N 136 
ASN   CB   C  N N 137 
ASN   CG   C  N N 138 
ASN   OD1  O  N N 139 
ASN   ND2  N  N N 140 
ASN   OXT  O  N N 141 
ASN   H    H  N N 142 
ASN   H2   H  N N 143 
ASN   HA   H  N N 144 
ASN   HB2  H  N N 145 
ASN   HB3  H  N N 146 
ASN   HD21 H  N N 147 
ASN   HD22 H  N N 148 
ASN   HXT  H  N N 149 
ASP   N    N  N N 150 
ASP   CA   C  N S 151 
ASP   C    C  N N 152 
ASP   O    O  N N 153 
ASP   CB   C  N N 154 
ASP   CG   C  N N 155 
ASP   OD1  O  N N 156 
ASP   OD2  O  N N 157 
ASP   OXT  O  N N 158 
ASP   H    H  N N 159 
ASP   H2   H  N N 160 
ASP   HA   H  N N 161 
ASP   HB2  H  N N 162 
ASP   HB3  H  N N 163 
ASP   HD2  H  N N 164 
ASP   HXT  H  N N 165 
CYS   N    N  N N 166 
CYS   CA   C  N R 167 
CYS   C    C  N N 168 
CYS   O    O  N N 169 
CYS   CB   C  N N 170 
CYS   SG   S  N N 171 
CYS   OXT  O  N N 172 
CYS   H    H  N N 173 
CYS   H2   H  N N 174 
CYS   HA   H  N N 175 
CYS   HB2  H  N N 176 
CYS   HB3  H  N N 177 
CYS   HG   H  N N 178 
CYS   HXT  H  N N 179 
GLN   N    N  N N 180 
GLN   CA   C  N S 181 
GLN   C    C  N N 182 
GLN   O    O  N N 183 
GLN   CB   C  N N 184 
GLN   CG   C  N N 185 
GLN   CD   C  N N 186 
GLN   OE1  O  N N 187 
GLN   NE2  N  N N 188 
GLN   OXT  O  N N 189 
GLN   H    H  N N 190 
GLN   H2   H  N N 191 
GLN   HA   H  N N 192 
GLN   HB2  H  N N 193 
GLN   HB3  H  N N 194 
GLN   HG2  H  N N 195 
GLN   HG3  H  N N 196 
GLN   HE21 H  N N 197 
GLN   HE22 H  N N 198 
GLN   HXT  H  N N 199 
GLU   N    N  N N 200 
GLU   CA   C  N S 201 
GLU   C    C  N N 202 
GLU   O    O  N N 203 
GLU   CB   C  N N 204 
GLU   CG   C  N N 205 
GLU   CD   C  N N 206 
GLU   OE1  O  N N 207 
GLU   OE2  O  N N 208 
GLU   OXT  O  N N 209 
GLU   H    H  N N 210 
GLU   H2   H  N N 211 
GLU   HA   H  N N 212 
GLU   HB2  H  N N 213 
GLU   HB3  H  N N 214 
GLU   HG2  H  N N 215 
GLU   HG3  H  N N 216 
GLU   HE2  H  N N 217 
GLU   HXT  H  N N 218 
GLY   N    N  N N 219 
GLY   CA   C  N N 220 
GLY   C    C  N N 221 
GLY   O    O  N N 222 
GLY   OXT  O  N N 223 
GLY   H    H  N N 224 
GLY   H2   H  N N 225 
GLY   HA2  H  N N 226 
GLY   HA3  H  N N 227 
GLY   HXT  H  N N 228 
HIS   N    N  N N 229 
HIS   CA   C  N S 230 
HIS   C    C  N N 231 
HIS   O    O  N N 232 
HIS   CB   C  N N 233 
HIS   CG   C  Y N 234 
HIS   ND1  N  Y N 235 
HIS   CD2  C  Y N 236 
HIS   CE1  C  Y N 237 
HIS   NE2  N  Y N 238 
HIS   OXT  O  N N 239 
HIS   H    H  N N 240 
HIS   H2   H  N N 241 
HIS   HA   H  N N 242 
HIS   HB2  H  N N 243 
HIS   HB3  H  N N 244 
HIS   HD1  H  N N 245 
HIS   HD2  H  N N 246 
HIS   HE1  H  N N 247 
HIS   HE2  H  N N 248 
HIS   HXT  H  N N 249 
ILE   N    N  N N 250 
ILE   CA   C  N S 251 
ILE   C    C  N N 252 
ILE   O    O  N N 253 
ILE   CB   C  N S 254 
ILE   CG1  C  N N 255 
ILE   CG2  C  N N 256 
ILE   CD1  C  N N 257 
ILE   OXT  O  N N 258 
ILE   H    H  N N 259 
ILE   H2   H  N N 260 
ILE   HA   H  N N 261 
ILE   HB   H  N N 262 
ILE   HG12 H  N N 263 
ILE   HG13 H  N N 264 
ILE   HG21 H  N N 265 
ILE   HG22 H  N N 266 
ILE   HG23 H  N N 267 
ILE   HD11 H  N N 268 
ILE   HD12 H  N N 269 
ILE   HD13 H  N N 270 
ILE   HXT  H  N N 271 
LEU   N    N  N N 272 
LEU   CA   C  N S 273 
LEU   C    C  N N 274 
LEU   O    O  N N 275 
LEU   CB   C  N N 276 
LEU   CG   C  N N 277 
LEU   CD1  C  N N 278 
LEU   CD2  C  N N 279 
LEU   OXT  O  N N 280 
LEU   H    H  N N 281 
LEU   H2   H  N N 282 
LEU   HA   H  N N 283 
LEU   HB2  H  N N 284 
LEU   HB3  H  N N 285 
LEU   HG   H  N N 286 
LEU   HD11 H  N N 287 
LEU   HD12 H  N N 288 
LEU   HD13 H  N N 289 
LEU   HD21 H  N N 290 
LEU   HD22 H  N N 291 
LEU   HD23 H  N N 292 
LEU   HXT  H  N N 293 
LYS   N    N  N N 294 
LYS   CA   C  N S 295 
LYS   C    C  N N 296 
LYS   O    O  N N 297 
LYS   CB   C  N N 298 
LYS   CG   C  N N 299 
LYS   CD   C  N N 300 
LYS   CE   C  N N 301 
LYS   NZ   N  N N 302 
LYS   OXT  O  N N 303 
LYS   H    H  N N 304 
LYS   H2   H  N N 305 
LYS   HA   H  N N 306 
LYS   HB2  H  N N 307 
LYS   HB3  H  N N 308 
LYS   HG2  H  N N 309 
LYS   HG3  H  N N 310 
LYS   HD2  H  N N 311 
LYS   HD3  H  N N 312 
LYS   HE2  H  N N 313 
LYS   HE3  H  N N 314 
LYS   HZ1  H  N N 315 
LYS   HZ2  H  N N 316 
LYS   HZ3  H  N N 317 
LYS   HXT  H  N N 318 
MET   N    N  N N 319 
MET   CA   C  N S 320 
MET   C    C  N N 321 
MET   O    O  N N 322 
MET   CB   C  N N 323 
MET   CG   C  N N 324 
MET   SD   S  N N 325 
MET   CE   C  N N 326 
MET   OXT  O  N N 327 
MET   H    H  N N 328 
MET   H2   H  N N 329 
MET   HA   H  N N 330 
MET   HB2  H  N N 331 
MET   HB3  H  N N 332 
MET   HG2  H  N N 333 
MET   HG3  H  N N 334 
MET   HE1  H  N N 335 
MET   HE2  H  N N 336 
MET   HE3  H  N N 337 
MET   HXT  H  N N 338 
MG    MG   MG N N 339 
PHE   N    N  N N 340 
PHE   CA   C  N S 341 
PHE   C    C  N N 342 
PHE   O    O  N N 343 
PHE   CB   C  N N 344 
PHE   CG   C  Y N 345 
PHE   CD1  C  Y N 346 
PHE   CD2  C  Y N 347 
PHE   CE1  C  Y N 348 
PHE   CE2  C  Y N 349 
PHE   CZ   C  Y N 350 
PHE   OXT  O  N N 351 
PHE   H    H  N N 352 
PHE   H2   H  N N 353 
PHE   HA   H  N N 354 
PHE   HB2  H  N N 355 
PHE   HB3  H  N N 356 
PHE   HD1  H  N N 357 
PHE   HD2  H  N N 358 
PHE   HE1  H  N N 359 
PHE   HE2  H  N N 360 
PHE   HZ   H  N N 361 
PHE   HXT  H  N N 362 
PRO   N    N  N N 363 
PRO   CA   C  N S 364 
PRO   C    C  N N 365 
PRO   O    O  N N 366 
PRO   CB   C  N N 367 
PRO   CG   C  N N 368 
PRO   CD   C  N N 369 
PRO   OXT  O  N N 370 
PRO   H    H  N N 371 
PRO   HA   H  N N 372 
PRO   HB2  H  N N 373 
PRO   HB3  H  N N 374 
PRO   HG2  H  N N 375 
PRO   HG3  H  N N 376 
PRO   HD2  H  N N 377 
PRO   HD3  H  N N 378 
PRO   HXT  H  N N 379 
SER   N    N  N N 380 
SER   CA   C  N S 381 
SER   C    C  N N 382 
SER   O    O  N N 383 
SER   CB   C  N N 384 
SER   OG   O  N N 385 
SER   OXT  O  N N 386 
SER   H    H  N N 387 
SER   H2   H  N N 388 
SER   HA   H  N N 389 
SER   HB2  H  N N 390 
SER   HB3  H  N N 391 
SER   HG   H  N N 392 
SER   HXT  H  N N 393 
THR   N    N  N N 394 
THR   CA   C  N S 395 
THR   C    C  N N 396 
THR   O    O  N N 397 
THR   CB   C  N R 398 
THR   OG1  O  N N 399 
THR   CG2  C  N N 400 
THR   OXT  O  N N 401 
THR   H    H  N N 402 
THR   H2   H  N N 403 
THR   HA   H  N N 404 
THR   HB   H  N N 405 
THR   HG1  H  N N 406 
THR   HG21 H  N N 407 
THR   HG22 H  N N 408 
THR   HG23 H  N N 409 
THR   HXT  H  N N 410 
TRP   N    N  N N 411 
TRP   CA   C  N S 412 
TRP   C    C  N N 413 
TRP   O    O  N N 414 
TRP   CB   C  N N 415 
TRP   CG   C  Y N 416 
TRP   CD1  C  Y N 417 
TRP   CD2  C  Y N 418 
TRP   NE1  N  Y N 419 
TRP   CE2  C  Y N 420 
TRP   CE3  C  Y N 421 
TRP   CZ2  C  Y N 422 
TRP   CZ3  C  Y N 423 
TRP   CH2  C  Y N 424 
TRP   OXT  O  N N 425 
TRP   H    H  N N 426 
TRP   H2   H  N N 427 
TRP   HA   H  N N 428 
TRP   HB2  H  N N 429 
TRP   HB3  H  N N 430 
TRP   HD1  H  N N 431 
TRP   HE1  H  N N 432 
TRP   HE3  H  N N 433 
TRP   HZ2  H  N N 434 
TRP   HZ3  H  N N 435 
TRP   HH2  H  N N 436 
TRP   HXT  H  N N 437 
TYR   N    N  N N 438 
TYR   CA   C  N S 439 
TYR   C    C  N N 440 
TYR   O    O  N N 441 
TYR   CB   C  N N 442 
TYR   CG   C  Y N 443 
TYR   CD1  C  Y N 444 
TYR   CD2  C  Y N 445 
TYR   CE1  C  Y N 446 
TYR   CE2  C  Y N 447 
TYR   CZ   C  Y N 448 
TYR   OH   O  N N 449 
TYR   OXT  O  N N 450 
TYR   H    H  N N 451 
TYR   H2   H  N N 452 
TYR   HA   H  N N 453 
TYR   HB2  H  N N 454 
TYR   HB3  H  N N 455 
TYR   HD1  H  N N 456 
TYR   HD2  H  N N 457 
TYR   HE1  H  N N 458 
TYR   HE2  H  N N 459 
TYR   HH   H  N N 460 
TYR   HXT  H  N N 461 
VAL   N    N  N N 462 
VAL   CA   C  N S 463 
VAL   C    C  N N 464 
VAL   O    O  N N 465 
VAL   CB   C  N N 466 
VAL   CG1  C  N N 467 
VAL   CG2  C  N N 468 
VAL   OXT  O  N N 469 
VAL   H    H  N N 470 
VAL   H2   H  N N 471 
VAL   HA   H  N N 472 
VAL   HB   H  N N 473 
VAL   HG11 H  N N 474 
VAL   HG12 H  N N 475 
VAL   HG13 H  N N 476 
VAL   HG21 H  N N 477 
VAL   HG22 H  N N 478 
VAL   HG23 H  N N 479 
VAL   HXT  H  N N 480 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1H71 C15 C16  sing N N 1   
A1H71 C15 C14  sing N N 2   
A1H71 C16 C17  sing N N 3   
A1H71 C23 C21  sing N N 4   
A1H71 C19 C18  sing N N 5   
A1H71 C14 N13  sing N N 6   
A1H71 C14 O20  doub N N 7   
A1H71 N13 C12  sing N N 8   
A1H71 C17 C18  sing N N 9   
A1H71 C21 C12  sing N N 10  
A1H71 C21 O22  sing N N 11  
A1H71 C12 C11  sing N N 12  
A1H71 C11 O24  doub N N 13  
A1H71 C11 N10  sing N N 14  
A1H71 N10 C9   sing N N 15  
A1H71 C9  C8   sing N N 16  
A1H71 C9  C25  sing N N 17  
A1H71 C8  C7   sing N N 18  
A1H71 O26 C25  doub N N 19  
A1H71 C7  C6   sing N N 20  
A1H71 C25 N27  sing N N 21  
A1H71 C6  C5   sing N N 22  
A1H71 C32 C33  doub Y N 23  
A1H71 C32 C31  sing Y N 24  
A1H71 C33 C34  sing Y N 25  
A1H71 N27 C28  sing N N 26  
A1H71 C5  N4   sing N N 27  
A1H71 C31 C30  doub Y N 28  
A1H71 N4  C3   sing N N 29  
A1H71 C34 C35  doub Y N 30  
A1H71 C28 C29  sing N N 31  
A1H71 C28 C1   sing N N 32  
A1H71 C30 C35  sing Y N 33  
A1H71 C30 C29  sing N N 34  
A1H71 C2  C3   sing N N 35  
A1H71 C2  C1   sing N N 36  
A1H71 C3  O37  doub N N 37  
A1H71 C1  OG1  sing N N 38  
A1H71 OG1 CB   sing N N 39  
A1H71 N   CA   sing N N 40  
A1H71 CB  CA   sing N N 41  
A1H71 CB  CG2  sing N N 42  
A1H71 CA  C    sing N N 43  
A1H71 C   O    doub N N 44  
A1H71 C5  H1   sing N N 45  
A1H71 C5  H2   sing N N 46  
A1H71 C6  H3   sing N N 47  
A1H71 C6  H4   sing N N 48  
A1H71 C7  H5   sing N N 49  
A1H71 C7  H6   sing N N 50  
A1H71 C8  H7   sing N N 51  
A1H71 C8  H8   sing N N 52  
A1H71 C15 H9   sing N N 53  
A1H71 C15 H10  sing N N 54  
A1H71 C17 H11  sing N N 55  
A1H71 C17 H12  sing N N 56  
A1H71 C21 H13  sing N N 57  
A1H71 C28 H14  sing N N 58  
A1H71 C19 H15  sing N N 59  
A1H71 C19 H16  sing N N 60  
A1H71 C19 H17  sing N N 61  
A1H71 C18 H18  sing N N 62  
A1H71 C18 H19  sing N N 63  
A1H71 C16 H20  sing N N 64  
A1H71 C16 H21  sing N N 65  
A1H71 N13 H22  sing N N 66  
A1H71 C12 H23  sing N N 67  
A1H71 C23 H24  sing N N 68  
A1H71 C23 H25  sing N N 69  
A1H71 C23 H26  sing N N 70  
A1H71 O22 H27  sing N N 71  
A1H71 N10 H28  sing N N 72  
A1H71 C9  H29  sing N N 73  
A1H71 N27 H30  sing N N 74  
A1H71 N4  H31  sing N N 75  
A1H71 C2  H32  sing N N 76  
A1H71 C2  H33  sing N N 77  
A1H71 C1  H34  sing N N 78  
A1H71 CB  H35  sing N N 79  
A1H71 CG2 H36  sing N N 80  
A1H71 CG2 H37  sing N N 81  
A1H71 CG2 H38  sing N N 82  
A1H71 CA  H39  sing N N 83  
A1H71 C   H40  sing N N 84  
A1H71 N   H41  sing N N 85  
A1H71 N   H42  sing N N 86  
A1H71 C29 H44  sing N N 87  
A1H71 C29 H45  sing N N 88  
A1H71 C35 H46  sing N N 89  
A1H71 C34 H47  sing N N 90  
A1H71 C33 H48  sing N N 91  
A1H71 C32 H49  sing N N 92  
A1H71 C31 H50  sing N N 93  
ALA   N   CA   sing N N 94  
ALA   N   H    sing N N 95  
ALA   N   H2   sing N N 96  
ALA   CA  C    sing N N 97  
ALA   CA  CB   sing N N 98  
ALA   CA  HA   sing N N 99  
ALA   C   O    doub N N 100 
ALA   C   OXT  sing N N 101 
ALA   CB  HB1  sing N N 102 
ALA   CB  HB2  sing N N 103 
ALA   CB  HB3  sing N N 104 
ALA   OXT HXT  sing N N 105 
ARG   N   CA   sing N N 106 
ARG   N   H    sing N N 107 
ARG   N   H2   sing N N 108 
ARG   CA  C    sing N N 109 
ARG   CA  CB   sing N N 110 
ARG   CA  HA   sing N N 111 
ARG   C   O    doub N N 112 
ARG   C   OXT  sing N N 113 
ARG   CB  CG   sing N N 114 
ARG   CB  HB2  sing N N 115 
ARG   CB  HB3  sing N N 116 
ARG   CG  CD   sing N N 117 
ARG   CG  HG2  sing N N 118 
ARG   CG  HG3  sing N N 119 
ARG   CD  NE   sing N N 120 
ARG   CD  HD2  sing N N 121 
ARG   CD  HD3  sing N N 122 
ARG   NE  CZ   sing N N 123 
ARG   NE  HE   sing N N 124 
ARG   CZ  NH1  sing N N 125 
ARG   CZ  NH2  doub N N 126 
ARG   NH1 HH11 sing N N 127 
ARG   NH1 HH12 sing N N 128 
ARG   NH2 HH21 sing N N 129 
ARG   NH2 HH22 sing N N 130 
ARG   OXT HXT  sing N N 131 
ASN   N   CA   sing N N 132 
ASN   N   H    sing N N 133 
ASN   N   H2   sing N N 134 
ASN   CA  C    sing N N 135 
ASN   CA  CB   sing N N 136 
ASN   CA  HA   sing N N 137 
ASN   C   O    doub N N 138 
ASN   C   OXT  sing N N 139 
ASN   CB  CG   sing N N 140 
ASN   CB  HB2  sing N N 141 
ASN   CB  HB3  sing N N 142 
ASN   CG  OD1  doub N N 143 
ASN   CG  ND2  sing N N 144 
ASN   ND2 HD21 sing N N 145 
ASN   ND2 HD22 sing N N 146 
ASN   OXT HXT  sing N N 147 
ASP   N   CA   sing N N 148 
ASP   N   H    sing N N 149 
ASP   N   H2   sing N N 150 
ASP   CA  C    sing N N 151 
ASP   CA  CB   sing N N 152 
ASP   CA  HA   sing N N 153 
ASP   C   O    doub N N 154 
ASP   C   OXT  sing N N 155 
ASP   CB  CG   sing N N 156 
ASP   CB  HB2  sing N N 157 
ASP   CB  HB3  sing N N 158 
ASP   CG  OD1  doub N N 159 
ASP   CG  OD2  sing N N 160 
ASP   OD2 HD2  sing N N 161 
ASP   OXT HXT  sing N N 162 
CYS   N   CA   sing N N 163 
CYS   N   H    sing N N 164 
CYS   N   H2   sing N N 165 
CYS   CA  C    sing N N 166 
CYS   CA  CB   sing N N 167 
CYS   CA  HA   sing N N 168 
CYS   C   O    doub N N 169 
CYS   C   OXT  sing N N 170 
CYS   CB  SG   sing N N 171 
CYS   CB  HB2  sing N N 172 
CYS   CB  HB3  sing N N 173 
CYS   SG  HG   sing N N 174 
CYS   OXT HXT  sing N N 175 
GLN   N   CA   sing N N 176 
GLN   N   H    sing N N 177 
GLN   N   H2   sing N N 178 
GLN   CA  C    sing N N 179 
GLN   CA  CB   sing N N 180 
GLN   CA  HA   sing N N 181 
GLN   C   O    doub N N 182 
GLN   C   OXT  sing N N 183 
GLN   CB  CG   sing N N 184 
GLN   CB  HB2  sing N N 185 
GLN   CB  HB3  sing N N 186 
GLN   CG  CD   sing N N 187 
GLN   CG  HG2  sing N N 188 
GLN   CG  HG3  sing N N 189 
GLN   CD  OE1  doub N N 190 
GLN   CD  NE2  sing N N 191 
GLN   NE2 HE21 sing N N 192 
GLN   NE2 HE22 sing N N 193 
GLN   OXT HXT  sing N N 194 
GLU   N   CA   sing N N 195 
GLU   N   H    sing N N 196 
GLU   N   H2   sing N N 197 
GLU   CA  C    sing N N 198 
GLU   CA  CB   sing N N 199 
GLU   CA  HA   sing N N 200 
GLU   C   O    doub N N 201 
GLU   C   OXT  sing N N 202 
GLU   CB  CG   sing N N 203 
GLU   CB  HB2  sing N N 204 
GLU   CB  HB3  sing N N 205 
GLU   CG  CD   sing N N 206 
GLU   CG  HG2  sing N N 207 
GLU   CG  HG3  sing N N 208 
GLU   CD  OE1  doub N N 209 
GLU   CD  OE2  sing N N 210 
GLU   OE2 HE2  sing N N 211 
GLU   OXT HXT  sing N N 212 
GLY   N   CA   sing N N 213 
GLY   N   H    sing N N 214 
GLY   N   H2   sing N N 215 
GLY   CA  C    sing N N 216 
GLY   CA  HA2  sing N N 217 
GLY   CA  HA3  sing N N 218 
GLY   C   O    doub N N 219 
GLY   C   OXT  sing N N 220 
GLY   OXT HXT  sing N N 221 
HIS   N   CA   sing N N 222 
HIS   N   H    sing N N 223 
HIS   N   H2   sing N N 224 
HIS   CA  C    sing N N 225 
HIS   CA  CB   sing N N 226 
HIS   CA  HA   sing N N 227 
HIS   C   O    doub N N 228 
HIS   C   OXT  sing N N 229 
HIS   CB  CG   sing N N 230 
HIS   CB  HB2  sing N N 231 
HIS   CB  HB3  sing N N 232 
HIS   CG  ND1  sing Y N 233 
HIS   CG  CD2  doub Y N 234 
HIS   ND1 CE1  doub Y N 235 
HIS   ND1 HD1  sing N N 236 
HIS   CD2 NE2  sing Y N 237 
HIS   CD2 HD2  sing N N 238 
HIS   CE1 NE2  sing Y N 239 
HIS   CE1 HE1  sing N N 240 
HIS   NE2 HE2  sing N N 241 
HIS   OXT HXT  sing N N 242 
ILE   N   CA   sing N N 243 
ILE   N   H    sing N N 244 
ILE   N   H2   sing N N 245 
ILE   CA  C    sing N N 246 
ILE   CA  CB   sing N N 247 
ILE   CA  HA   sing N N 248 
ILE   C   O    doub N N 249 
ILE   C   OXT  sing N N 250 
ILE   CB  CG1  sing N N 251 
ILE   CB  CG2  sing N N 252 
ILE   CB  HB   sing N N 253 
ILE   CG1 CD1  sing N N 254 
ILE   CG1 HG12 sing N N 255 
ILE   CG1 HG13 sing N N 256 
ILE   CG2 HG21 sing N N 257 
ILE   CG2 HG22 sing N N 258 
ILE   CG2 HG23 sing N N 259 
ILE   CD1 HD11 sing N N 260 
ILE   CD1 HD12 sing N N 261 
ILE   CD1 HD13 sing N N 262 
ILE   OXT HXT  sing N N 263 
LEU   N   CA   sing N N 264 
LEU   N   H    sing N N 265 
LEU   N   H2   sing N N 266 
LEU   CA  C    sing N N 267 
LEU   CA  CB   sing N N 268 
LEU   CA  HA   sing N N 269 
LEU   C   O    doub N N 270 
LEU   C   OXT  sing N N 271 
LEU   CB  CG   sing N N 272 
LEU   CB  HB2  sing N N 273 
LEU   CB  HB3  sing N N 274 
LEU   CG  CD1  sing N N 275 
LEU   CG  CD2  sing N N 276 
LEU   CG  HG   sing N N 277 
LEU   CD1 HD11 sing N N 278 
LEU   CD1 HD12 sing N N 279 
LEU   CD1 HD13 sing N N 280 
LEU   CD2 HD21 sing N N 281 
LEU   CD2 HD22 sing N N 282 
LEU   CD2 HD23 sing N N 283 
LEU   OXT HXT  sing N N 284 
LYS   N   CA   sing N N 285 
LYS   N   H    sing N N 286 
LYS   N   H2   sing N N 287 
LYS   CA  C    sing N N 288 
LYS   CA  CB   sing N N 289 
LYS   CA  HA   sing N N 290 
LYS   C   O    doub N N 291 
LYS   C   OXT  sing N N 292 
LYS   CB  CG   sing N N 293 
LYS   CB  HB2  sing N N 294 
LYS   CB  HB3  sing N N 295 
LYS   CG  CD   sing N N 296 
LYS   CG  HG2  sing N N 297 
LYS   CG  HG3  sing N N 298 
LYS   CD  CE   sing N N 299 
LYS   CD  HD2  sing N N 300 
LYS   CD  HD3  sing N N 301 
LYS   CE  NZ   sing N N 302 
LYS   CE  HE2  sing N N 303 
LYS   CE  HE3  sing N N 304 
LYS   NZ  HZ1  sing N N 305 
LYS   NZ  HZ2  sing N N 306 
LYS   NZ  HZ3  sing N N 307 
LYS   OXT HXT  sing N N 308 
MET   N   CA   sing N N 309 
MET   N   H    sing N N 310 
MET   N   H2   sing N N 311 
MET   CA  C    sing N N 312 
MET   CA  CB   sing N N 313 
MET   CA  HA   sing N N 314 
MET   C   O    doub N N 315 
MET   C   OXT  sing N N 316 
MET   CB  CG   sing N N 317 
MET   CB  HB2  sing N N 318 
MET   CB  HB3  sing N N 319 
MET   CG  SD   sing N N 320 
MET   CG  HG2  sing N N 321 
MET   CG  HG3  sing N N 322 
MET   SD  CE   sing N N 323 
MET   CE  HE1  sing N N 324 
MET   CE  HE2  sing N N 325 
MET   CE  HE3  sing N N 326 
MET   OXT HXT  sing N N 327 
PHE   N   CA   sing N N 328 
PHE   N   H    sing N N 329 
PHE   N   H2   sing N N 330 
PHE   CA  C    sing N N 331 
PHE   CA  CB   sing N N 332 
PHE   CA  HA   sing N N 333 
PHE   C   O    doub N N 334 
PHE   C   OXT  sing N N 335 
PHE   CB  CG   sing N N 336 
PHE   CB  HB2  sing N N 337 
PHE   CB  HB3  sing N N 338 
PHE   CG  CD1  doub Y N 339 
PHE   CG  CD2  sing Y N 340 
PHE   CD1 CE1  sing Y N 341 
PHE   CD1 HD1  sing N N 342 
PHE   CD2 CE2  doub Y N 343 
PHE   CD2 HD2  sing N N 344 
PHE   CE1 CZ   doub Y N 345 
PHE   CE1 HE1  sing N N 346 
PHE   CE2 CZ   sing Y N 347 
PHE   CE2 HE2  sing N N 348 
PHE   CZ  HZ   sing N N 349 
PHE   OXT HXT  sing N N 350 
PRO   N   CA   sing N N 351 
PRO   N   CD   sing N N 352 
PRO   N   H    sing N N 353 
PRO   CA  C    sing N N 354 
PRO   CA  CB   sing N N 355 
PRO   CA  HA   sing N N 356 
PRO   C   O    doub N N 357 
PRO   C   OXT  sing N N 358 
PRO   CB  CG   sing N N 359 
PRO   CB  HB2  sing N N 360 
PRO   CB  HB3  sing N N 361 
PRO   CG  CD   sing N N 362 
PRO   CG  HG2  sing N N 363 
PRO   CG  HG3  sing N N 364 
PRO   CD  HD2  sing N N 365 
PRO   CD  HD3  sing N N 366 
PRO   OXT HXT  sing N N 367 
SER   N   CA   sing N N 368 
SER   N   H    sing N N 369 
SER   N   H2   sing N N 370 
SER   CA  C    sing N N 371 
SER   CA  CB   sing N N 372 
SER   CA  HA   sing N N 373 
SER   C   O    doub N N 374 
SER   C   OXT  sing N N 375 
SER   CB  OG   sing N N 376 
SER   CB  HB2  sing N N 377 
SER   CB  HB3  sing N N 378 
SER   OG  HG   sing N N 379 
SER   OXT HXT  sing N N 380 
THR   N   CA   sing N N 381 
THR   N   H    sing N N 382 
THR   N   H2   sing N N 383 
THR   CA  C    sing N N 384 
THR   CA  CB   sing N N 385 
THR   CA  HA   sing N N 386 
THR   C   O    doub N N 387 
THR   C   OXT  sing N N 388 
THR   CB  OG1  sing N N 389 
THR   CB  CG2  sing N N 390 
THR   CB  HB   sing N N 391 
THR   OG1 HG1  sing N N 392 
THR   CG2 HG21 sing N N 393 
THR   CG2 HG22 sing N N 394 
THR   CG2 HG23 sing N N 395 
THR   OXT HXT  sing N N 396 
TRP   N   CA   sing N N 397 
TRP   N   H    sing N N 398 
TRP   N   H2   sing N N 399 
TRP   CA  C    sing N N 400 
TRP   CA  CB   sing N N 401 
TRP   CA  HA   sing N N 402 
TRP   C   O    doub N N 403 
TRP   C   OXT  sing N N 404 
TRP   CB  CG   sing N N 405 
TRP   CB  HB2  sing N N 406 
TRP   CB  HB3  sing N N 407 
TRP   CG  CD1  doub Y N 408 
TRP   CG  CD2  sing Y N 409 
TRP   CD1 NE1  sing Y N 410 
TRP   CD1 HD1  sing N N 411 
TRP   CD2 CE2  doub Y N 412 
TRP   CD2 CE3  sing Y N 413 
TRP   NE1 CE2  sing Y N 414 
TRP   NE1 HE1  sing N N 415 
TRP   CE2 CZ2  sing Y N 416 
TRP   CE3 CZ3  doub Y N 417 
TRP   CE3 HE3  sing N N 418 
TRP   CZ2 CH2  doub Y N 419 
TRP   CZ2 HZ2  sing N N 420 
TRP   CZ3 CH2  sing Y N 421 
TRP   CZ3 HZ3  sing N N 422 
TRP   CH2 HH2  sing N N 423 
TRP   OXT HXT  sing N N 424 
TYR   N   CA   sing N N 425 
TYR   N   H    sing N N 426 
TYR   N   H2   sing N N 427 
TYR   CA  C    sing N N 428 
TYR   CA  CB   sing N N 429 
TYR   CA  HA   sing N N 430 
TYR   C   O    doub N N 431 
TYR   C   OXT  sing N N 432 
TYR   CB  CG   sing N N 433 
TYR   CB  HB2  sing N N 434 
TYR   CB  HB3  sing N N 435 
TYR   CG  CD1  doub Y N 436 
TYR   CG  CD2  sing Y N 437 
TYR   CD1 CE1  sing Y N 438 
TYR   CD1 HD1  sing N N 439 
TYR   CD2 CE2  doub Y N 440 
TYR   CD2 HD2  sing N N 441 
TYR   CE1 CZ   doub Y N 442 
TYR   CE1 HE1  sing N N 443 
TYR   CE2 CZ   sing Y N 444 
TYR   CE2 HE2  sing N N 445 
TYR   CZ  OH   sing N N 446 
TYR   OH  HH   sing N N 447 
TYR   OXT HXT  sing N N 448 
VAL   N   CA   sing N N 449 
VAL   N   H    sing N N 450 
VAL   N   H2   sing N N 451 
VAL   CA  C    sing N N 452 
VAL   CA  CB   sing N N 453 
VAL   CA  HA   sing N N 454 
VAL   C   O    doub N N 455 
VAL   C   OXT  sing N N 456 
VAL   CB  CG1  sing N N 457 
VAL   CB  CG2  sing N N 458 
VAL   CB  HB   sing N N 459 
VAL   CG1 HG11 sing N N 460 
VAL   CG1 HG12 sing N N 461 
VAL   CG1 HG13 sing N N 462 
VAL   CG2 HG21 sing N N 463 
VAL   CG2 HG22 sing N N 464 
VAL   CG2 HG23 sing N N 465 
VAL   OXT HXT  sing N N 466 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           'GR 1861/10-3' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4FZC 
_pdbx_initial_refinement_model.details          '20S yeast proteasome in complex with cepafungin I' 
# 
_atom_sites.entry_id                    9EY9 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007376 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003077 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.003313 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007505 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . MET   A  1  1   ? 27.957  -95.780  46.208  1.00 171.45 ? 1   MET   A N   1 
ATOM   2     C  CA  . MET   A  1  1   ? 29.372  -95.946  46.678  1.00 168.00 ? 1   MET   A CA  1 
ATOM   3     C  C   . MET   A  1  1   ? 30.279  -96.237  45.469  1.00 162.77 ? 1   MET   A C   1 
ATOM   4     O  O   . MET   A  1  1   ? 29.923  -95.806  44.351  1.00 143.11 ? 1   MET   A O   1 
ATOM   5     C  CB  . MET   A  1  1   ? 29.478  -97.071  47.717  1.00 168.93 ? 1   MET   A CB  1 
ATOM   6     C  CG  . MET   A  1  1   ? 30.670  -96.931  48.659  1.00 172.80 ? 1   MET   A CG  1 
ATOM   7     S  SD  . MET   A  1  1   ? 31.691  -98.428  48.762  1.00 171.81 ? 1   MET   A SD  1 
ATOM   8     C  CE  . MET   A  1  1   ? 30.526  -99.590  49.472  1.00 177.26 ? 1   MET   A CE  1 
ATOM   9     N  N   . THR   A  1  2   ? 31.405  -96.928  45.691  1.00 160.34 ? 2   THR   A N   1 
ATOM   10    C  CA  . THR   A  1  2   ? 32.469  -97.254  44.699  1.00 153.87 ? 2   THR   A CA  1 
ATOM   11    C  C   . THR   A  1  2   ? 33.140  -95.962  44.215  1.00 152.67 ? 2   THR   A C   1 
ATOM   12    O  O   . THR   A  1  2   ? 32.488  -94.898  44.235  1.00 152.64 ? 2   THR   A O   1 
ATOM   13    C  CB  . THR   A  1  2   ? 31.942  -98.106  43.534  1.00 148.89 ? 2   THR   A CB  1 
ATOM   14    O  OG1 . THR   A  1  2   ? 31.120  -99.148  44.062  1.00 141.51 ? 2   THR   A OG1 1 
ATOM   15    C  CG2 . THR   A  1  2   ? 33.051  -98.727  42.710  1.00 139.75 ? 2   THR   A CG2 1 
ATOM   16    N  N   . ASP   A  1  3   ? 34.411  -96.069  43.817  1.00 150.57 ? 3   ASP   A N   1 
ATOM   17    C  CA  . ASP   A  1  3   ? 35.232  -94.971  43.242  1.00 138.55 ? 3   ASP   A CA  1 
ATOM   18    C  C   . ASP   A  1  3   ? 34.520  -94.424  41.998  1.00 137.74 ? 3   ASP   A C   1 
ATOM   19    O  O   . ASP   A  1  3   ? 34.682  -95.022  40.915  1.00 139.42 ? 3   ASP   A O   1 
ATOM   20    C  CB  . ASP   A  1  3   ? 36.646  -95.474  42.926  1.00 137.60 ? 3   ASP   A CB  1 
ATOM   21    C  CG  . ASP   A  1  3   ? 37.673  -94.379  42.700  1.00 134.06 ? 3   ASP   A CG  1 
ATOM   22    O  OD1 . ASP   A  1  3   ? 37.270  -93.258  42.339  1.00 137.23 ? 3   ASP   A OD1 1 
ATOM   23    O  OD2 . ASP   A  1  3   ? 38.874  -94.660  42.888  1.00 135.42 ? 3   ASP   A OD2 1 
ATOM   24    N  N   . ARG   A  1  4   ? 33.745  -93.344  42.155  1.00 131.30 ? 4   ARG   A N   1 
ATOM   25    C  CA  . ARG   A  1  4   ? 33.056  -92.643  41.035  1.00 126.94 ? 4   ARG   A CA  1 
ATOM   26    C  C   . ARG   A  1  4   ? 34.062  -91.757  40.286  1.00 114.65 ? 4   ARG   A C   1 
ATOM   27    O  O   . ARG   A  1  4   ? 33.735  -91.328  39.161  1.00 107.72 ? 4   ARG   A O   1 
ATOM   28    C  CB  . ARG   A  1  4   ? 31.864  -91.815  41.534  1.00 132.92 ? 4   ARG   A CB  1 
ATOM   29    C  CG  . ARG   A  1  4   ? 30.728  -92.624  42.148  1.00 143.10 ? 4   ARG   A CG  1 
ATOM   30    C  CD  . ARG   A  1  4   ? 30.242  -93.780  41.287  1.00 150.25 ? 4   ARG   A CD  1 
ATOM   31    N  NE  . ARG   A  1  4   ? 30.129  -93.441  39.870  1.00 159.38 ? 4   ARG   A NE  1 
ATOM   32    C  CZ  . ARG   A  1  4   ? 29.024  -93.026  39.249  1.00 166.68 ? 4   ARG   A CZ  1 
ATOM   33    N  NH1 . ARG   A  1  4   ? 27.885  -92.887  39.907  1.00 170.48 ? 4   ARG   A NH1 1 
ATOM   34    N  NH2 . ARG   A  1  4   ? 29.065  -92.752  37.956  1.00 168.34 ? 4   ARG   A NH2 1 
ATOM   35    N  N   . TYR   A  1  5   ? 35.237  -91.501  40.877  1.00 106.86 ? 5   TYR   A N   1 
ATOM   36    C  CA  . TYR   A  1  5   ? 36.336  -90.697  40.277  1.00 100.46 ? 5   TYR   A CA  1 
ATOM   37    C  C   . TYR   A  1  5   ? 37.086  -91.554  39.250  1.00 94.02  ? 5   TYR   A C   1 
ATOM   38    O  O   . TYR   A  1  5   ? 38.224  -91.974  39.532  1.00 89.93  ? 5   TYR   A O   1 
ATOM   39    C  CB  . TYR   A  1  5   ? 37.295  -90.172  41.351  1.00 100.46 ? 5   TYR   A CB  1 
ATOM   40    C  CG  . TYR   A  1  5   ? 36.707  -89.178  42.319  1.00 103.80 ? 5   TYR   A CG  1 
ATOM   41    C  CD1 . TYR   A  1  5   ? 35.995  -89.594  43.433  1.00 104.62 ? 5   TYR   A CD1 1 
ATOM   42    C  CD2 . TYR   A  1  5   ? 36.886  -87.816  42.137  1.00 104.45 ? 5   TYR   A CD2 1 
ATOM   43    C  CE1 . TYR   A  1  5   ? 35.461  -88.685  44.331  1.00 107.64 ? 5   TYR   A CE1 1 
ATOM   44    C  CE2 . TYR   A  1  5   ? 36.360  -86.893  43.026  1.00 106.79 ? 5   TYR   A CE2 1 
ATOM   45    C  CZ  . TYR   A  1  5   ? 35.645  -87.328  44.128  1.00 109.71 ? 5   TYR   A CZ  1 
ATOM   46    O  OH  . TYR   A  1  5   ? 35.127  -86.423  45.008  1.00 111.68 ? 5   TYR   A OH  1 
ATOM   47    N  N   . SER   A  1  6   ? 36.462  -91.799  38.094  1.00 92.08  ? 6   SER   A N   1 
ATOM   48    C  CA  . SER   A  1  6   ? 37.028  -92.591  36.968  1.00 93.03  ? 6   SER   A CA  1 
ATOM   49    C  C   . SER   A  1  6   ? 37.672  -91.668  35.924  1.00 92.46  ? 6   SER   A C   1 
ATOM   50    O  O   . SER   A  1  6   ? 38.082  -92.186  34.870  1.00 93.36  ? 6   SER   A O   1 
ATOM   51    C  CB  . SER   A  1  6   ? 35.971  -93.463  36.343  1.00 95.28  ? 6   SER   A CB  1 
ATOM   52    O  OG  . SER   A  1  6   ? 34.803  -92.708  36.064  1.00 99.79  ? 6   SER   A OG  1 
ATOM   53    N  N   . PHE   A  1  7   ? 37.775  -90.364  36.216  1.00 94.32  ? 7   PHE   A N   1 
ATOM   54    C  CA  . PHE   A  1  7   ? 38.291  -89.308  35.302  1.00 93.26  ? 7   PHE   A CA  1 
ATOM   55    C  C   . PHE   A  1  7   ? 39.596  -88.724  35.854  1.00 92.30  ? 7   PHE   A C   1 
ATOM   56    O  O   . PHE   A  1  7   ? 39.809  -88.772  37.080  1.00 99.25  ? 7   PHE   A O   1 
ATOM   57    C  CB  . PHE   A  1  7   ? 37.262  -88.190  35.121  1.00 91.35  ? 7   PHE   A CB  1 
ATOM   58    C  CG  . PHE   A  1  7   ? 36.715  -87.626  36.406  1.00 90.57  ? 7   PHE   A CG  1 
ATOM   59    C  CD1 . PHE   A  1  7   ? 37.397  -86.634  37.096  1.00 91.70  ? 7   PHE   A CD1 1 
ATOM   60    C  CD2 . PHE   A  1  7   ? 35.518  -88.091  36.929  1.00 89.85  ? 7   PHE   A CD2 1 
ATOM   61    C  CE1 . PHE   A  1  7   ? 36.890  -86.119  38.279  1.00 94.27  ? 7   PHE   A CE1 1 
ATOM   62    C  CE2 . PHE   A  1  7   ? 35.014  -87.576  38.113  1.00 91.89  ? 7   PHE   A CE2 1 
ATOM   63    C  CZ  . PHE   A  1  7   ? 35.700  -86.591  38.785  1.00 94.28  ? 7   PHE   A CZ  1 
ATOM   64    N  N   . SER   A  1  8   ? 40.426  -88.164  34.969  1.00 88.51  ? 8   SER   A N   1 
ATOM   65    C  CA  . SER   A  1  8   ? 41.755  -87.581  35.296  1.00 90.36  ? 8   SER   A CA  1 
ATOM   66    C  C   . SER   A  1  8   ? 41.587  -86.396  36.250  1.00 91.94  ? 8   SER   A C   1 
ATOM   67    O  O   . SER   A  1  8   ? 40.684  -85.573  36.005  1.00 95.90  ? 8   SER   A O   1 
ATOM   68    C  CB  . SER   A  1  8   ? 42.488  -87.161  34.052  1.00 91.45  ? 8   SER   A CB  1 
ATOM   69    O  OG  . SER   A  1  8   ? 43.073  -88.281  33.408  1.00 93.83  ? 8   SER   A OG  1 
ATOM   70    N  N   . LEU   A  1  9   ? 42.431  -86.323  37.286  1.00 91.65  ? 9   LEU   A N   1 
ATOM   71    C  CA  . LEU   A  1  9   ? 42.524  -85.163  38.216  1.00 88.89  ? 9   LEU   A CA  1 
ATOM   72    C  C   . LEU   A  1  9   ? 43.698  -84.260  37.817  1.00 86.58  ? 9   LEU   A C   1 
ATOM   73    O  O   . LEU   A  1  9   ? 43.779  -83.138  38.355  1.00 83.24  ? 9   LEU   A O   1 
ATOM   74    C  CB  . LEU   A  1  9   ? 42.697  -85.670  39.650  1.00 88.17  ? 9   LEU   A CB  1 
ATOM   75    C  CG  . LEU   A  1  9   ? 41.549  -86.507  40.211  1.00 87.50  ? 9   LEU   A CG  1 
ATOM   76    C  CD1 . LEU   A  1  9   ? 41.846  -86.900  41.649  1.00 87.40  ? 9   LEU   A CD1 1 
ATOM   77    C  CD2 . LEU   A  1  9   ? 40.222  -85.764  40.132  1.00 89.04  ? 9   LEU   A CD2 1 
ATOM   78    N  N   . THR   A  1  10  ? 44.586  -84.745  36.943  1.00 87.00  ? 10  THR   A N   1 
ATOM   79    C  CA  . THR   A  1  10  ? 45.659  -83.949  36.290  1.00 85.71  ? 10  THR   A CA  1 
ATOM   80    C  C   . THR   A  1  10  ? 45.262  -83.726  34.829  1.00 86.61  ? 10  THR   A C   1 
ATOM   81    O  O   . THR   A  1  10  ? 45.138  -84.729  34.103  1.00 81.38  ? 10  THR   A O   1 
ATOM   82    C  CB  . THR   A  1  10  ? 47.026  -84.637  36.387  1.00 85.35  ? 10  THR   A CB  1 
ATOM   83    O  OG1 . THR   A  1  10  ? 47.237  -85.052  37.737  1.00 86.75  ? 10  THR   A OG1 1 
ATOM   84    C  CG2 . THR   A  1  10  ? 48.163  -83.745  35.939  1.00 86.54  ? 10  THR   A CG2 1 
ATOM   85    N  N   . THR   A  1  11  ? 45.051  -82.466  34.435  1.00 87.83  ? 11  THR   A N   1 
ATOM   86    C  CA  . THR   A  1  11  ? 44.664  -82.058  33.059  1.00 88.10  ? 11  THR   A CA  1 
ATOM   87    C  C   . THR   A  1  11  ? 45.513  -80.860  32.629  1.00 91.26  ? 11  THR   A C   1 
ATOM   88    O  O   . THR   A  1  11  ? 46.070  -80.175  33.513  1.00 94.37  ? 11  THR   A O   1 
ATOM   89    C  CB  . THR   A  1  11  ? 43.163  -81.753  32.971  1.00 89.13  ? 11  THR   A CB  1 
ATOM   90    O  OG1 . THR   A  1  11  ? 42.890  -80.597  33.762  1.00 88.41  ? 11  THR   A OG1 1 
ATOM   91    C  CG2 . THR   A  1  11  ? 42.303  -82.905  33.442  1.00 89.89  ? 11  THR   A CG2 1 
ATOM   92    N  N   . PHE   A  1  12  ? 45.614  -80.642  31.317  1.00 91.53  ? 12  PHE   A N   1 
ATOM   93    C  CA  . PHE   A  1  12  ? 46.353  -79.520  30.683  1.00 95.00  ? 12  PHE   A CA  1 
ATOM   94    C  C   . PHE   A  1  12  ? 45.577  -78.213  30.884  1.00 96.19  ? 12  PHE   A C   1 
ATOM   95    O  O   . PHE   A  1  12  ? 44.363  -78.179  30.598  1.00 96.59  ? 12  PHE   A O   1 
ATOM   96    C  CB  . PHE   A  1  12  ? 46.570  -79.799  29.193  1.00 94.38  ? 12  PHE   A CB  1 
ATOM   97    C  CG  . PHE   A  1  12  ? 47.458  -80.982  28.899  1.00 94.06  ? 12  PHE   A CG  1 
ATOM   98    C  CD1 . PHE   A  1  12  ? 48.838  -80.857  28.938  1.00 93.67  ? 12  PHE   A CD1 1 
ATOM   99    C  CD2 . PHE   A  1  12  ? 46.915  -82.218  28.580  1.00 91.59  ? 12  PHE   A CD2 1 
ATOM   100   C  CE1 . PHE   A  1  12  ? 49.657  -81.942  28.666  1.00 92.30  ? 12  PHE   A CE1 1 
ATOM   101   C  CE2 . PHE   A  1  12  ? 47.735  -83.302  28.310  1.00 89.93  ? 12  PHE   A CE2 1 
ATOM   102   C  CZ  . PHE   A  1  12  ? 49.104  -83.162  28.352  1.00 90.63  ? 12  PHE   A CZ  1 
ATOM   103   N  N   . SER   A  1  13  ? 46.265  -77.176  31.370  1.00 99.92  ? 13  SER   A N   1 
ATOM   104   C  CA  . SER   A  1  13  ? 45.767  -75.777  31.436  1.00 100.36 ? 13  SER   A CA  1 
ATOM   105   C  C   . SER   A  1  13  ? 46.025  -75.109  30.089  1.00 99.38  ? 13  SER   A C   1 
ATOM   106   O  O   . SER   A  1  13  ? 46.911  -75.541  29.353  1.00 99.17  ? 13  SER   A O   1 
ATOM   107   C  CB  . SER   A  1  13  ? 46.419  -75.017  32.562  1.00 103.63 ? 13  SER   A CB  1 
ATOM   108   O  OG  . SER   A  1  13  ? 47.834  -75.065  32.450  1.00 106.34 ? 13  SER   A OG  1 
ATOM   109   N  N   . PRO   A  1  14  ? 45.264  -74.051  29.722  1.00 96.88  ? 14  PRO   A N   1 
ATOM   110   C  CA  . PRO   A  1  14  ? 45.444  -73.377  28.434  1.00 96.49  ? 14  PRO   A CA  1 
ATOM   111   C  C   . PRO   A  1  14  ? 46.904  -73.080  28.055  1.00 96.04  ? 14  PRO   A C   1 
ATOM   112   O  O   . PRO   A  1  14  ? 47.226  -73.196  26.889  1.00 98.67  ? 14  PRO   A O   1 
ATOM   113   C  CB  . PRO   A  1  14  ? 44.661  -72.073  28.626  1.00 96.93  ? 14  PRO   A CB  1 
ATOM   114   C  CG  . PRO   A  1  14  ? 43.545  -72.455  29.570  1.00 94.89  ? 14  PRO   A CG  1 
ATOM   115   C  CD  . PRO   A  1  14  ? 44.159  -73.475  30.506  1.00 94.02  ? 14  PRO   A CD  1 
ATOM   116   N  N   . SER   A  1  15  ? 47.743  -72.730  29.036  1.00 96.29  ? 15  SER   A N   1 
ATOM   117   C  CA  . SER   A  1  15  ? 49.181  -72.392  28.853  1.00 99.23  ? 15  SER   A CA  1 
ATOM   118   C  C   . SER   A  1  15  ? 50.004  -73.645  28.525  1.00 98.43  ? 15  SER   A C   1 
ATOM   119   O  O   . SER   A  1  15  ? 51.120  -73.484  27.993  1.00 94.95  ? 15  SER   A O   1 
ATOM   120   C  CB  . SER   A  1  15  ? 49.731  -71.688  30.067  1.00 99.64  ? 15  SER   A CB  1 
ATOM   121   O  OG  . SER   A  1  15  ? 49.417  -72.403  31.253  1.00 99.80  ? 15  SER   A OG  1 
ATOM   122   N  N   . GLY   A  1  16  ? 49.483  -74.835  28.840  1.00 98.55  ? 16  GLY   A N   1 
ATOM   123   C  CA  . GLY   A  1  16  ? 50.116  -76.132  28.529  1.00 100.99 ? 16  GLY   A CA  1 
ATOM   124   C  C   . GLY   A  1  16  ? 50.676  -76.810  29.767  1.00 101.84 ? 16  GLY   A C   1 
ATOM   125   O  O   . GLY   A  1  16  ? 51.125  -77.965  29.650  1.00 104.90 ? 16  GLY   A O   1 
ATOM   126   N  N   . LYS   A  1  17  ? 50.648  -76.132  30.918  1.00 103.34 ? 17  LYS   A N   1 
ATOM   127   C  CA  . LYS   A  1  17  ? 51.183  -76.671  32.197  1.00 104.78 ? 17  LYS   A CA  1 
ATOM   128   C  C   . LYS   A  1  17  ? 50.252  -77.793  32.669  1.00 99.61  ? 17  LYS   A C   1 
ATOM   129   O  O   . LYS   A  1  17  ? 49.033  -77.693  32.424  1.00 96.13  ? 17  LYS   A O   1 
ATOM   130   C  CB  . LYS   A  1  17  ? 51.286  -75.608  33.299  1.00 109.32 ? 17  LYS   A CB  1 
ATOM   131   C  CG  . LYS   A  1  17  ? 51.490  -74.163  32.853  1.00 116.73 ? 17  LYS   A CG  1 
ATOM   132   C  CD  . LYS   A  1  17  ? 52.921  -73.783  32.511  1.00 123.57 ? 17  LYS   A CD  1 
ATOM   133   C  CE  . LYS   A  1  17  ? 53.626  -73.017  33.612  1.00 124.95 ? 17  LYS   A CE  1 
ATOM   134   N  NZ  . LYS   A  1  17  ? 54.137  -73.919  34.671  1.00 127.27 ? 17  LYS   A NZ  1 
ATOM   135   N  N   . LEU   A  1  18  ? 50.811  -78.822  33.308  1.00 97.75  ? 18  LEU   A N   1 
ATOM   136   C  CA  . LEU   A  1  18  ? 50.038  -79.853  34.047  1.00 97.58  ? 18  LEU   A CA  1 
ATOM   137   C  C   . LEU   A  1  18  ? 50.085  -79.492  35.534  1.00 95.18  ? 18  LEU   A C   1 
ATOM   138   O  O   . LEU   A  1  18  ? 51.058  -79.877  36.213  1.00 96.35  ? 18  LEU   A O   1 
ATOM   139   C  CB  . LEU   A  1  18  ? 50.616  -81.241  33.751  1.00 96.89  ? 18  LEU   A CB  1 
ATOM   140   C  CG  . LEU   A  1  18  ? 50.276  -81.802  32.368  1.00 97.58  ? 18  LEU   A CG  1 
ATOM   141   C  CD1 . LEU   A  1  18  ? 51.146  -83.004  32.027  1.00 95.64  ? 18  LEU   A CD1 1 
ATOM   142   C  CD2 . LEU   A  1  18  ? 48.802  -82.171  32.277  1.00 96.54  ? 18  LEU   A CD2 1 
ATOM   143   N  N   . GLY   A  1  19  ? 49.075  -78.744  35.991  1.00 94.00  ? 19  GLY   A N   1 
ATOM   144   C  CA  . GLY   A  1  19  ? 49.009  -78.115  37.324  1.00 91.16  ? 19  GLY   A CA  1 
ATOM   145   C  C   . GLY   A  1  19  ? 49.549  -79.015  38.421  1.00 90.30  ? 19  GLY   A C   1 
ATOM   146   O  O   . GLY   A  1  19  ? 50.494  -78.588  39.116  1.00 86.84  ? 19  GLY   A O   1 
ATOM   147   N  N   . GLN   A  1  20  ? 48.986  -80.221  38.563  1.00 88.51  ? 20  GLN   A N   1 
ATOM   148   C  CA  . GLN   A  1  20  ? 49.241  -81.133  39.713  1.00 87.79  ? 20  GLN   A CA  1 
ATOM   149   C  C   . GLN   A  1  20  ? 50.708  -81.585  39.725  1.00 86.67  ? 20  GLN   A C   1 
ATOM   150   O  O   . GLN   A  1  20  ? 51.256  -81.749  40.833  1.00 87.88  ? 20  GLN   A O   1 
ATOM   151   C  CB  . GLN   A  1  20  ? 48.292  -82.333  39.683  1.00 87.36  ? 20  GLN   A CB  1 
ATOM   152   C  CG  . GLN   A  1  20  ? 46.856  -81.992  40.056  1.00 88.28  ? 20  GLN   A CG  1 
ATOM   153   C  CD  . GLN   A  1  20  ? 46.717  -81.528  41.487  1.00 87.88  ? 20  GLN   A CD  1 
ATOM   154   O  OE1 . GLN   A  1  20  ? 47.223  -82.153  42.417  1.00 87.44  ? 20  GLN   A OE1 1 
ATOM   155   N  NE2 . GLN   A  1  20  ? 46.022  -80.419  41.679  1.00 88.74  ? 20  GLN   A NE2 1 
ATOM   156   N  N   . ILE   A  1  21  ? 51.323  -81.779  38.555  1.00 84.65  ? 21  ILE   A N   1 
ATOM   157   C  CA  . ILE   A  1  21  ? 52.766  -82.151  38.439  1.00 86.43  ? 21  ILE   A CA  1 
ATOM   158   C  C   . ILE   A  1  21  ? 53.615  -80.975  38.932  1.00 88.65  ? 21  ILE   A C   1 
ATOM   159   O  O   . ILE   A  1  21  ? 54.533  -81.212  39.738  1.00 86.24  ? 21  ILE   A O   1 
ATOM   160   C  CB  . ILE   A  1  21  ? 53.131  -82.564  37.000  1.00 88.37  ? 21  ILE   A CB  1 
ATOM   161   C  CG1 . ILE   A  1  21  ? 52.442  -83.875  36.614  1.00 88.88  ? 21  ILE   A CG1 1 
ATOM   162   C  CG2 . ILE   A  1  21  ? 54.642  -82.649  36.825  1.00 88.09  ? 21  ILE   A CG2 1 
ATOM   163   C  CD1 . ILE   A  1  21  ? 52.490  -84.182  35.139  1.00 88.95  ? 21  ILE   A CD1 1 
ATOM   164   N  N   . ASP   A  1  22  ? 53.320  -79.763  38.455  1.00 92.36  ? 22  ASP   A N   1 
ATOM   165   C  CA  . ASP   A  1  22  ? 54.006  -78.513  38.881  1.00 95.95  ? 22  ASP   A CA  1 
ATOM   166   C  C   . ASP   A  1  22  ? 53.907  -78.382  40.405  1.00 94.58  ? 22  ASP   A C   1 
ATOM   167   O  O   . ASP   A  1  22  ? 54.953  -78.142  41.040  1.00 94.86  ? 22  ASP   A O   1 
ATOM   168   C  CB  . ASP   A  1  22  ? 53.427  -77.287  38.172  1.00 100.43 ? 22  ASP   A CB  1 
ATOM   169   C  CG  . ASP   A  1  22  ? 53.843  -77.163  36.715  1.00 103.85 ? 22  ASP   A CG  1 
ATOM   170   O  OD1 . ASP   A  1  22  ? 54.687  -77.969  36.270  1.00 104.36 ? 22  ASP   A OD1 1 
ATOM   171   O  OD2 . ASP   A  1  22  ? 53.322  -76.255  36.035  1.00 110.16 ? 22  ASP   A OD2 1 
ATOM   172   N  N   . TYR   A  1  23  ? 52.703  -78.552  40.966  1.00 93.24  ? 23  TYR   A N   1 
ATOM   173   C  CA  . TYR   A  1  23  ? 52.418  -78.398  42.419  1.00 93.05  ? 23  TYR   A CA  1 
ATOM   174   C  C   . TYR   A  1  23  ? 53.104  -79.521  43.211  1.00 91.70  ? 23  TYR   A C   1 
ATOM   175   O  O   . TYR   A  1  23  ? 53.486  -79.285  44.374  1.00 91.57  ? 23  TYR   A O   1 
ATOM   176   C  CB  . TYR   A  1  23  ? 50.912  -78.368  42.698  1.00 92.73  ? 23  TYR   A CB  1 
ATOM   177   C  CG  . TYR   A  1  23  ? 50.114  -77.329  41.946  1.00 95.42  ? 23  TYR   A CG  1 
ATOM   178   C  CD1 . TYR   A  1  23  ? 50.711  -76.212  41.377  1.00 97.24  ? 23  TYR   A CD1 1 
ATOM   179   C  CD2 . TYR   A  1  23  ? 48.738  -77.454  41.825  1.00 94.00  ? 23  TYR   A CD2 1 
ATOM   180   C  CE1 . TYR   A  1  23  ? 49.967  -75.263  40.692  1.00 98.88  ? 23  TYR   A CE1 1 
ATOM   181   C  CE2 . TYR   A  1  23  ? 47.980  -76.515  41.144  1.00 96.00  ? 23  TYR   A CE2 1 
ATOM   182   C  CZ  . TYR   A  1  23  ? 48.597  -75.414  40.577  1.00 99.52  ? 23  TYR   A CZ  1 
ATOM   183   O  OH  . TYR   A  1  23  ? 47.856  -74.483  39.909  1.00 104.55 ? 23  TYR   A OH  1 
ATOM   184   N  N   . ALA   A  1  24  ? 53.257  -80.704  42.612  1.00 89.54  ? 24  ALA   A N   1 
ATOM   185   C  CA  . ALA   A  1  24  ? 53.999  -81.840  43.208  1.00 89.34  ? 24  ALA   A CA  1 
ATOM   186   C  C   . ALA   A  1  24  ? 55.485  -81.477  43.313  1.00 87.61  ? 24  ALA   A C   1 
ATOM   187   O  O   . ALA   A  1  24  ? 56.068  -81.710  44.384  1.00 88.38  ? 24  ALA   A O   1 
ATOM   188   C  CB  . ALA   A  1  24  ? 53.789  -83.095  42.400  1.00 90.39  ? 24  ALA   A CB  1 
ATOM   189   N  N   . LEU   A  1  25  ? 56.069  -80.917  42.249  1.00 86.83  ? 25  LEU   A N   1 
ATOM   190   C  CA  . LEU   A  1  25  ? 57.483  -80.451  42.238  1.00 87.90  ? 25  LEU   A CA  1 
ATOM   191   C  C   . LEU   A  1  25  ? 57.673  -79.376  43.316  1.00 88.34  ? 25  LEU   A C   1 
ATOM   192   O  O   . LEU   A  1  25  ? 58.762  -79.356  43.923  1.00 86.01  ? 25  LEU   A O   1 
ATOM   193   C  CB  . LEU   A  1  25  ? 57.847  -79.914  40.851  1.00 90.12  ? 25  LEU   A CB  1 
ATOM   194   C  CG  . LEU   A  1  25  ? 58.056  -80.976  39.774  1.00 91.90  ? 25  LEU   A CG  1 
ATOM   195   C  CD1 . LEU   A  1  25  ? 57.823  -80.393  38.386  1.00 95.38  ? 25  LEU   A CD1 1 
ATOM   196   C  CD2 . LEU   A  1  25  ? 59.447  -81.587  39.879  1.00 90.93  ? 25  LEU   A CD2 1 
ATOM   197   N  N   . THR   A  1  26  ? 56.661  -78.527  43.547  1.00 91.31  ? 26  THR   A N   1 
ATOM   198   C  CA  . THR   A  1  26  ? 56.671  -77.471  44.601  1.00 93.81  ? 26  THR   A CA  1 
ATOM   199   C  C   . THR   A  1  26  ? 56.805  -78.141  45.974  1.00 93.02  ? 26  THR   A C   1 
ATOM   200   O  O   . THR   A  1  26  ? 57.579  -77.628  46.801  1.00 92.30  ? 26  THR   A O   1 
ATOM   201   C  CB  . THR   A  1  26  ? 55.432  -76.563  44.540  1.00 93.52  ? 26  THR   A CB  1 
ATOM   202   O  OG1 . THR   A  1  26  ? 55.444  -75.844  43.307  1.00 94.87  ? 26  THR   A OG1 1 
ATOM   203   C  CG2 . THR   A  1  26  ? 55.372  -75.572  45.683  1.00 93.37  ? 26  THR   A CG2 1 
ATOM   204   N  N   . ALA   A  1  27  ? 56.084  -79.245  46.200  1.00 94.91  ? 27  ALA   A N   1 
ATOM   205   C  CA  . ALA   A  1  27  ? 56.166  -80.064  47.435  1.00 95.58  ? 27  ALA   A CA  1 
ATOM   206   C  C   . ALA   A  1  27  ? 57.586  -80.625  47.593  1.00 95.91  ? 27  ALA   A C   1 
ATOM   207   O  O   . ALA   A  1  27  ? 58.078  -80.672  48.740  1.00 92.78  ? 27  ALA   A O   1 
ATOM   208   C  CB  . ALA   A  1  27  ? 55.142  -81.172  47.406  1.00 95.58  ? 27  ALA   A CB  1 
ATOM   209   N  N   . VAL   A  1  28  ? 58.215  -81.028  46.483  1.00 96.00  ? 28  VAL   A N   1 
ATOM   210   C  CA  . VAL   A  1  28  ? 59.602  -81.586  46.459  1.00 98.02  ? 28  VAL   A CA  1 
ATOM   211   C  C   . VAL   A  1  28  ? 60.587  -80.474  46.841  1.00 100.69 ? 28  VAL   A C   1 
ATOM   212   O  O   . VAL   A  1  28  ? 61.520  -80.772  47.614  1.00 97.13  ? 28  VAL   A O   1 
ATOM   213   C  CB  . VAL   A  1  28  ? 59.955  -82.215  45.096  1.00 98.00  ? 28  VAL   A CB  1 
ATOM   214   C  CG1 . VAL   A  1  28  ? 61.384  -82.735  45.065  1.00 96.56  ? 28  VAL   A CG1 1 
ATOM   215   C  CG2 . VAL   A  1  28  ? 58.986  -83.325  44.718  1.00 98.95  ? 28  VAL   A CG2 1 
ATOM   216   N  N   . LYS   A  1  29  ? 60.382  -79.252  46.327  1.00 103.96 ? 29  LYS   A N   1 
ATOM   217   C  CA  . LYS   A  1  29  ? 61.209  -78.055  46.650  1.00 105.60 ? 29  LYS   A CA  1 
ATOM   218   C  C   . LYS   A  1  29  ? 61.211  -77.839  48.168  1.00 102.57 ? 29  LYS   A C   1 
ATOM   219   O  O   . LYS   A  1  29  ? 62.310  -77.640  48.723  1.00 97.20  ? 29  LYS   A O   1 
ATOM   220   C  CB  . LYS   A  1  29  ? 60.709  -76.800  45.922  1.00 108.54 ? 29  LYS   A CB  1 
ATOM   221   C  CG  . LYS   A  1  29  ? 61.386  -76.498  44.589  1.00 114.60 ? 29  LYS   A CG  1 
ATOM   222   C  CD  . LYS   A  1  29  ? 62.693  -75.734  44.709  1.00 118.86 ? 29  LYS   A CD  1 
ATOM   223   C  CE  . LYS   A  1  29  ? 63.910  -76.630  44.815  1.00 122.25 ? 29  LYS   A CE  1 
ATOM   224   N  NZ  . LYS   A  1  29  ? 65.162  -75.845  44.946  1.00 124.59 ? 29  LYS   A NZ  1 
ATOM   225   N  N   . GLN   A  1  30  ? 60.035  -77.899  48.808  1.00 101.60 ? 30  GLN   A N   1 
ATOM   226   C  CA  . GLN   A  1  30  ? 59.870  -77.696  50.276  1.00 105.43 ? 30  GLN   A CA  1 
ATOM   227   C  C   . GLN   A  1  30  ? 60.600  -78.809  51.041  1.00 103.34 ? 30  GLN   A C   1 
ATOM   228   O  O   . GLN   A  1  30  ? 61.064  -78.539  52.163  1.00 103.87 ? 30  GLN   A O   1 
ATOM   229   C  CB  . GLN   A  1  30  ? 58.400  -77.691  50.716  1.00 107.39 ? 30  GLN   A CB  1 
ATOM   230   C  CG  . GLN   A  1  30  ? 57.464  -76.805  49.900  1.00 112.66 ? 30  GLN   A CG  1 
ATOM   231   C  CD  . GLN   A  1  30  ? 57.982  -75.421  49.584  1.00 120.14 ? 30  GLN   A CD  1 
ATOM   232   O  OE1 . GLN   A  1  30  ? 57.765  -74.899  48.492  1.00 127.40 ? 30  GLN   A OE1 1 
ATOM   233   N  NE2 . GLN   A  1  30  ? 58.651  -74.795  50.541  1.00 124.98 ? 30  GLN   A NE2 1 
ATOM   234   N  N   . GLY   A  1  31  ? 60.684  -80.011  50.458  1.00 101.79 ? 31  GLY   A N   1 
ATOM   235   C  CA  . GLY   A  1  31  ? 61.285  -81.210  51.079  1.00 100.30 ? 31  GLY   A CA  1 
ATOM   236   C  C   . GLY   A  1  31  ? 62.750  -81.015  51.444  1.00 97.70  ? 31  GLY   A C   1 
ATOM   237   O  O   . GLY   A  1  31  ? 63.417  -80.190  50.791  1.00 100.31 ? 31  GLY   A O   1 
ATOM   238   N  N   . VAL   A  1  32  ? 63.235  -81.765  52.440  1.00 95.74  ? 32  VAL   A N   1 
ATOM   239   C  CA  . VAL   A  1  32  ? 64.634  -81.704  52.963  1.00 96.92  ? 32  VAL   A CA  1 
ATOM   240   C  C   . VAL   A  1  32  ? 65.600  -82.179  51.874  1.00 94.93  ? 32  VAL   A C   1 
ATOM   241   O  O   . VAL   A  1  32  ? 65.237  -83.105  51.127  1.00 93.73  ? 32  VAL   A O   1 
ATOM   242   C  CB  . VAL   A  1  32  ? 64.787  -82.533  54.252  1.00 99.16  ? 32  VAL   A CB  1 
ATOM   243   C  CG1 . VAL   A  1  32  ? 66.238  -82.882  54.550  1.00 99.12  ? 32  VAL   A CG1 1 
ATOM   244   C  CG2 . VAL   A  1  32  ? 64.157  -81.820  55.437  1.00 103.37 ? 32  VAL   A CG2 1 
ATOM   245   N  N   . THR   A  1  33  ? 66.795  -81.582  51.816  1.00 94.36  ? 33  THR   A N   1 
ATOM   246   C  CA  . THR   A  1  33  ? 67.807  -81.829  50.756  1.00 94.46  ? 33  THR   A CA  1 
ATOM   247   C  C   . THR   A  1  33  ? 68.316  -83.268  50.853  1.00 94.39  ? 33  THR   A C   1 
ATOM   248   O  O   . THR   A  1  33  ? 68.672  -83.697  51.967  1.00 95.16  ? 33  THR   A O   1 
ATOM   249   C  CB  . THR   A  1  33  ? 69.004  -80.873  50.833  1.00 98.67  ? 33  THR   A CB  1 
ATOM   250   O  OG1 . THR   A  1  33  ? 68.528  -79.545  51.051  1.00 102.80 ? 33  THR   A OG1 1 
ATOM   251   C  CG2 . THR   A  1  33  ? 69.851  -80.922  49.579  1.00 96.13  ? 33  THR   A CG2 1 
ATOM   252   N  N   . SER   A  1  34  ? 68.338  -83.965  49.715  1.00 92.91  ? 34  SER   A N   1 
ATOM   253   C  CA  . SER   A  1  34  ? 69.045  -85.251  49.493  1.00 93.30  ? 34  SER   A CA  1 
ATOM   254   C  C   . SER   A  1  34  ? 69.904  -85.111  48.234  1.00 92.46  ? 34  SER   A C   1 
ATOM   255   O  O   . SER   A  1  34  ? 69.540  -84.297  47.360  1.00 87.70  ? 34  SER   A O   1 
ATOM   256   C  CB  . SER   A  1  34  ? 68.075  -86.400  49.389  1.00 93.86  ? 34  SER   A CB  1 
ATOM   257   O  OG  . SER   A  1  34  ? 67.093  -86.153  48.394  1.00 95.96  ? 34  SER   A OG  1 
ATOM   258   N  N   . LEU   A  1  35  ? 71.006  -85.859  48.152  1.00 93.68  ? 35  LEU   A N   1 
ATOM   259   C  CA  . LEU   A  1  35  ? 71.954  -85.793  47.008  1.00 93.54  ? 35  LEU   A CA  1 
ATOM   260   C  C   . LEU   A  1  35  ? 72.493  -87.190  46.673  1.00 91.65  ? 35  LEU   A C   1 
ATOM   261   O  O   . LEU   A  1  35  ? 72.325  -88.116  47.488  1.00 88.41  ? 35  LEU   A O   1 
ATOM   262   C  CB  . LEU   A  1  35  ? 73.084  -84.810  47.340  1.00 94.77  ? 35  LEU   A CB  1 
ATOM   263   C  CG  . LEU   A  1  35  ? 73.888  -85.091  48.611  1.00 95.34  ? 35  LEU   A CG  1 
ATOM   264   C  CD1 . LEU   A  1  35  ? 75.032  -86.060  48.345  1.00 96.00  ? 35  LEU   A CD1 1 
ATOM   265   C  CD2 . LEU   A  1  35  ? 74.434  -83.797  49.191  1.00 96.65  ? 35  LEU   A CD2 1 
ATOM   266   N  N   . GLY   A  1  36  ? 73.099  -87.312  45.490  1.00 91.27  ? 36  GLY   A N   1 
ATOM   267   C  CA  . GLY   A  1  36  ? 73.802  -88.514  45.012  1.00 91.44  ? 36  GLY   A CA  1 
ATOM   268   C  C   . GLY   A  1  36  ? 75.043  -88.133  44.225  1.00 94.16  ? 36  GLY   A C   1 
ATOM   269   O  O   . GLY   A  1  36  ? 74.958  -87.192  43.413  1.00 93.08  ? 36  GLY   A O   1 
ATOM   270   N  N   . ILE   A  1  37  ? 76.160  -88.820  44.467  1.00 94.40  ? 37  ILE   A N   1 
ATOM   271   C  CA  . ILE   A  1  37  ? 77.440  -88.634  43.722  1.00 95.88  ? 37  ILE   A CA  1 
ATOM   272   C  C   . ILE   A  1  37  ? 77.894  -89.999  43.202  1.00 95.38  ? 37  ILE   A C   1 
ATOM   273   O  O   . ILE   A  1  37  ? 77.862  -90.968  43.981  1.00 92.14  ? 37  ILE   A O   1 
ATOM   274   C  CB  . ILE   A  1  37  ? 78.518  -87.975  44.605  1.00 98.29  ? 37  ILE   A CB  1 
ATOM   275   C  CG1 . ILE   A  1  37  ? 77.958  -86.770  45.365  1.00 100.80 ? 37  ILE   A CG1 1 
ATOM   276   C  CG2 . ILE   A  1  37  ? 79.737  -87.608  43.769  1.00 97.77  ? 37  ILE   A CG2 1 
ATOM   277   C  CD1 . ILE   A  1  37  ? 78.922  -86.155  46.351  1.00 105.81 ? 37  ILE   A CD1 1 
ATOM   278   N  N   . LYS   A  1  38  ? 78.301  -90.055  41.933  1.00 98.74  ? 38  LYS   A N   1 
ATOM   279   C  CA  . LYS   A  1  38  ? 78.796  -91.281  41.257  1.00 101.99 ? 38  LYS   A CA  1 
ATOM   280   C  C   . LYS   A  1  38  ? 80.325  -91.218  41.159  1.00 103.27 ? 38  LYS   A C   1 
ATOM   281   O  O   . LYS   A  1  38  ? 80.834  -90.337  40.443  1.00 105.38 ? 38  LYS   A O   1 
ATOM   282   C  CB  . LYS   A  1  38  ? 78.162  -91.417  39.869  1.00 104.98 ? 38  LYS   A CB  1 
ATOM   283   C  CG  . LYS   A  1  38  ? 78.385  -92.763  39.197  1.00 107.06 ? 38  LYS   A CG  1 
ATOM   284   C  CD  . LYS   A  1  38  ? 77.520  -92.987  37.981  1.00 109.62 ? 38  LYS   A CD  1 
ATOM   285   C  CE  . LYS   A  1  38  ? 78.110  -92.397  36.720  1.00 110.25 ? 38  LYS   A CE  1 
ATOM   286   N  NZ  . LYS   A  1  38  ? 77.216  -92.616  35.560  1.00 111.37 ? 38  LYS   A NZ  1 
ATOM   287   N  N   . ALA   A  1  39  ? 81.024  -92.117  41.858  1.00 99.95  ? 39  ALA   A N   1 
ATOM   288   C  CA  . ALA   A  1  39  ? 82.487  -92.322  41.748  1.00 98.70  ? 39  ALA   A CA  1 
ATOM   289   C  C   . ALA   A  1  39  ? 82.757  -93.386  40.679  1.00 97.60  ? 39  ALA   A C   1 
ATOM   290   O  O   . ALA   A  1  39  ? 81.782  -93.906  40.106  1.00 94.48  ? 39  ALA   A O   1 
ATOM   291   C  CB  . ALA   A  1  39  ? 83.059  -92.716  43.086  1.00 98.56  ? 39  ALA   A CB  1 
ATOM   292   N  N   . THR   A  1  40  ? 84.031  -93.686  40.414  1.00 98.75  ? 40  THR   A N   1 
ATOM   293   C  CA  . THR   A  1  40  ? 84.466  -94.699  39.416  1.00 100.21 ? 40  THR   A CA  1 
ATOM   294   C  C   . THR   A  1  40  ? 84.153  -96.108  39.930  1.00 101.60 ? 40  THR   A C   1 
ATOM   295   O  O   . THR   A  1  40  ? 83.731  -96.944  39.107  1.00 101.47 ? 40  THR   A O   1 
ATOM   296   C  CB  . THR   A  1  40  ? 85.956  -94.557  39.087  1.00 102.01 ? 40  THR   A CB  1 
ATOM   297   O  OG1 . THR   A  1  40  ? 86.686  -94.639  40.311  1.00 103.63 ? 40  THR   A OG1 1 
ATOM   298   C  CG2 . THR   A  1  40  ? 86.273  -93.258  38.381  1.00 102.79 ? 40  THR   A CG2 1 
ATOM   299   N  N   . ASN   A  1  41  ? 84.350  -96.350  41.232  1.00 100.67 ? 41  ASN   A N   1 
ATOM   300   C  CA  . ASN   A  1  41  ? 84.211  -97.688  41.867  1.00 102.15 ? 41  ASN   A CA  1 
ATOM   301   C  C   . ASN   A  1  41  ? 83.076  -97.675  42.901  1.00 100.60 ? 41  ASN   A C   1 
ATOM   302   O  O   . ASN   A  1  41  ? 83.159  -98.447  43.875  1.00 104.70 ? 41  ASN   A O   1 
ATOM   303   C  CB  . ASN   A  1  41  ? 85.526  -98.134  42.509  1.00 104.81 ? 41  ASN   A CB  1 
ATOM   304   C  CG  . ASN   A  1  41  ? 85.918  -97.270  43.688  1.00 103.43 ? 41  ASN   A CG  1 
ATOM   305   O  OD1 . ASN   A  1  41  ? 85.684  -96.065  43.677  1.00 102.64 ? 41  ASN   A OD1 1 
ATOM   306   N  ND2 . ASN   A  1  41  ? 86.494  -97.874  44.713  1.00 107.61 ? 41  ASN   A ND2 1 
ATOM   307   N  N   . GLY   A  1  42  ? 82.048  -96.848  42.702  1.00 97.90  ? 42  GLY   A N   1 
ATOM   308   C  CA  . GLY   A  1  42  ? 80.847  -96.863  43.558  1.00 98.01  ? 42  GLY   A CA  1 
ATOM   309   C  C   . GLY   A  1  42  ? 79.993  -95.616  43.417  1.00 96.52  ? 42  GLY   A C   1 
ATOM   310   O  O   . GLY   A  1  42  ? 80.373  -94.707  42.650  1.00 96.01  ? 42  GLY   A O   1 
ATOM   311   N  N   . VAL   A  1  43  ? 78.866  -95.592  44.135  1.00 94.85  ? 43  VAL   A N   1 
ATOM   312   C  CA  . VAL   A  1  43  ? 77.908  -94.449  44.204  1.00 94.41  ? 43  VAL   A CA  1 
ATOM   313   C  C   . VAL   A  1  43  ? 77.551  -94.214  45.672  1.00 93.48  ? 43  VAL   A C   1 
ATOM   314   O  O   . VAL   A  1  43  ? 77.383  -95.205  46.402  1.00 88.55  ? 43  VAL   A O   1 
ATOM   315   C  CB  . VAL   A  1  43  ? 76.636  -94.713  43.377  1.00 95.30  ? 43  VAL   A CB  1 
ATOM   316   C  CG1 . VAL   A  1  43  ? 75.744  -93.482  43.318  1.00 97.62  ? 43  VAL   A CG1 1 
ATOM   317   C  CG2 . VAL   A  1  43  ? 76.958  -95.203  41.975  1.00 95.58  ? 43  VAL   A CG2 1 
ATOM   318   N  N   . VAL   A  1  44  ? 77.419  -92.946  46.066  1.00 94.81  ? 44  VAL   A N   1 
ATOM   319   C  CA  . VAL   A  1  44  ? 76.956  -92.530  47.423  1.00 95.96  ? 44  VAL   A CA  1 
ATOM   320   C  C   . VAL   A  1  44  ? 75.638  -91.764  47.264  1.00 95.43  ? 44  VAL   A C   1 
ATOM   321   O  O   . VAL   A  1  44  ? 75.543  -90.930  46.342  1.00 93.86  ? 44  VAL   A O   1 
ATOM   322   C  CB  . VAL   A  1  44  ? 78.017  -91.703  48.177  1.00 98.97  ? 44  VAL   A CB  1 
ATOM   323   C  CG1 . VAL   A  1  44  ? 78.580  -90.561  47.341  1.00 101.24 ? 44  VAL   A CG1 1 
ATOM   324   C  CG2 . VAL   A  1  44  ? 77.474  -91.177  49.497  1.00 99.63  ? 44  VAL   A CG2 1 
ATOM   325   N  N   . ILE   A  1  45  ? 74.659  -92.070  48.119  1.00 93.37  ? 45  ILE   A N   1 
ATOM   326   C  CA  . ILE   A  1  45  ? 73.381  -91.312  48.265  1.00 94.82  ? 45  ILE   A CA  1 
ATOM   327   C  C   . ILE   A  1  45  ? 73.218  -90.949  49.743  1.00 96.19  ? 45  ILE   A C   1 
ATOM   328   O  O   . ILE   A  1  45  ? 73.306  -91.862  50.589  1.00 94.95  ? 45  ILE   A O   1 
ATOM   329   C  CB  . ILE   A  1  45  ? 72.171  -92.104  47.730  1.00 95.49  ? 45  ILE   A CB  1 
ATOM   330   C  CG1 . ILE   A  1  45  ? 72.192  -93.568  48.181  1.00 98.32  ? 45  ILE   A CG1 1 
ATOM   331   C  CG2 . ILE   A  1  45  ? 72.087  -91.976  46.216  1.00 94.58  ? 45  ILE   A CG2 1 
ATOM   332   C  CD1 . ILE   A  1  45  ? 70.889  -94.309  47.961  1.00 98.38  ? 45  ILE   A CD1 1 
ATOM   333   N  N   . ALA   A  1  46  ? 72.996  -89.662  50.024  1.00 96.03  ? 46  ALA   A N   1 
ATOM   334   C  CA  . ALA   A  1  46  ? 72.969  -89.075  51.383  1.00 92.88  ? 46  ALA   A CA  1 
ATOM   335   C  C   . ALA   A  1  46  ? 71.736  -88.184  51.543  1.00 90.91  ? 46  ALA   A C   1 
ATOM   336   O  O   . ALA   A  1  46  ? 71.187  -87.734  50.518  1.00 89.56  ? 46  ALA   A O   1 
ATOM   337   C  CB  . ALA   A  1  46  ? 74.235  -88.291  51.618  1.00 94.40  ? 46  ALA   A CB  1 
ATOM   338   N  N   . THR   A  1  47  ? 71.330  -87.940  52.790  1.00 89.14  ? 47  THR   A N   1 
ATOM   339   C  CA  . THR   A  1  47  ? 70.255  -86.982  53.159  1.00 90.82  ? 47  THR   A CA  1 
ATOM   340   C  C   . THR   A  1  47  ? 70.342  -86.653  54.654  1.00 92.29  ? 47  THR   A C   1 
ATOM   341   O  O   . THR   A  1  47  ? 70.952  -87.435  55.405  1.00 89.43  ? 47  THR   A O   1 
ATOM   342   C  CB  . THR   A  1  47  ? 68.871  -87.523  52.770  1.00 89.37  ? 47  THR   A CB  1 
ATOM   343   O  OG1 . THR   A  1  47  ? 67.914  -86.481  52.960  1.00 91.16  ? 47  THR   A OG1 1 
ATOM   344   C  CG2 . THR   A  1  47  ? 68.452  -88.734  53.572  1.00 87.14  ? 47  THR   A CG2 1 
ATOM   345   N  N   . GLU   A  1  48  ? 69.766  -85.515  55.048  1.00 99.08  ? 48  GLU   A N   1 
ATOM   346   C  CA  . GLU   A  1  48  ? 69.571  -85.103  56.463  1.00 104.77 ? 48  GLU   A CA  1 
ATOM   347   C  C   . GLU   A  1  48  ? 68.363  -85.866  57.020  1.00 105.09 ? 48  GLU   A C   1 
ATOM   348   O  O   . GLU   A  1  48  ? 67.360  -85.990  56.291  1.00 104.80 ? 48  GLU   A O   1 
ATOM   349   C  CB  . GLU   A  1  48  ? 69.367  -83.586  56.533  1.00 111.39 ? 48  GLU   A CB  1 
ATOM   350   C  CG  . GLU   A  1  48  ? 69.200  -83.035  57.942  1.00 118.45 ? 48  GLU   A CG  1 
ATOM   351   C  CD  . GLU   A  1  48  ? 68.667  -81.610  58.022  1.00 124.25 ? 48  GLU   A CD  1 
ATOM   352   O  OE1 . GLU   A  1  48  ? 68.881  -80.836  57.062  1.00 125.15 ? 48  GLU   A OE1 1 
ATOM   353   O  OE2 . GLU   A  1  48  ? 68.031  -81.274  59.044  1.00 125.30 ? 48  GLU   A OE2 1 
ATOM   354   N  N   . LYS   A  1  49  ? 68.467  -86.377  58.250  1.00 106.61 ? 49  LYS   A N   1 
ATOM   355   C  CA  . LYS   A  1  49  ? 67.334  -86.986  59.000  1.00 111.67 ? 49  LYS   A CA  1 
ATOM   356   C  C   . LYS   A  1  49  ? 66.663  -85.900  59.845  1.00 115.62 ? 49  LYS   A C   1 
ATOM   357   O  O   . LYS   A  1  49  ? 67.023  -85.759  61.032  1.00 119.56 ? 49  LYS   A O   1 
ATOM   358   C  CB  . LYS   A  1  49  ? 67.802  -88.157  59.871  1.00 115.19 ? 49  LYS   A CB  1 
ATOM   359   C  CG  . LYS   A  1  49  ? 67.882  -89.495  59.151  1.00 116.93 ? 49  LYS   A CG  1 
ATOM   360   C  CD  . LYS   A  1  49  ? 67.789  -90.692  60.073  1.00 122.48 ? 49  LYS   A CD  1 
ATOM   361   C  CE  . LYS   A  1  49  ? 69.120  -91.080  60.679  1.00 128.64 ? 49  LYS   A CE  1 
ATOM   362   N  NZ  . LYS   A  1  49  ? 69.024  -92.357  61.426  1.00 133.76 ? 49  LYS   A NZ  1 
ATOM   363   N  N   . LYS   A  1  50  ? 65.733  -85.156  59.241  1.00 117.59 ? 50  LYS   A N   1 
ATOM   364   C  CA  . LYS   A  1  50  ? 64.913  -84.122  59.927  1.00 121.93 ? 50  LYS   A CA  1 
ATOM   365   C  C   . LYS   A  1  50  ? 64.021  -84.826  60.957  1.00 118.44 ? 50  LYS   A C   1 
ATOM   366   O  O   . LYS   A  1  50  ? 63.030  -85.455  60.546  1.00 116.54 ? 50  LYS   A O   1 
ATOM   367   C  CB  . LYS   A  1  50  ? 64.098  -83.319  58.906  1.00 126.76 ? 50  LYS   A CB  1 
ATOM   368   C  CG  . LYS   A  1  50  ? 62.992  -82.437  59.475  1.00 126.94 ? 50  LYS   A CG  1 
ATOM   369   C  CD  . LYS   A  1  50  ? 63.446  -81.062  59.909  1.00 129.27 ? 50  LYS   A CD  1 
ATOM   370   C  CE  . LYS   A  1  50  ? 62.288  -80.207  60.379  1.00 133.72 ? 50  LYS   A CE  1 
ATOM   371   N  NZ  . LYS   A  1  50  ? 62.678  -78.787  60.546  1.00 137.50 ? 50  LYS   A NZ  1 
ATOM   372   N  N   . SER   A  1  51  ? 64.377  -84.730  62.240  1.00 123.13 ? 51  SER   A N   1 
ATOM   373   C  CA  . SER   A  1  51  ? 63.623  -85.315  63.379  1.00 127.33 ? 51  SER   A CA  1 
ATOM   374   C  C   . SER   A  1  51  ? 62.374  -84.468  63.665  1.00 135.22 ? 51  SER   A C   1 
ATOM   375   O  O   . SER   A  1  51  ? 62.517  -83.235  63.795  1.00 141.56 ? 51  SER   A O   1 
ATOM   376   C  CB  . SER   A  1  51  ? 64.504  -85.433  64.594  1.00 131.41 ? 51  SER   A CB  1 
ATOM   377   O  OG  . SER   A  1  51  ? 63.866  -86.194  65.607  1.00 133.70 ? 51  SER   A OG  1 
ATOM   378   N  N   . SER   A  1  52  ? 61.202  -85.109  63.758  1.00 132.39 ? 52  SER   A N   1 
ATOM   379   C  CA  . SER   A  1  52  ? 59.880  -84.465  63.998  1.00 134.16 ? 52  SER   A CA  1 
ATOM   380   C  C   . SER   A  1  52  ? 59.747  -84.056  65.468  1.00 130.50 ? 52  SER   A C   1 
ATOM   381   O  O   . SER   A  1  52  ? 59.019  -83.083  65.744  1.00 133.89 ? 52  SER   A O   1 
ATOM   382   C  CB  . SER   A  1  52  ? 58.745  -85.372  63.601  1.00 134.75 ? 52  SER   A CB  1 
ATOM   383   O  OG  . SER   A  1  52  ? 58.765  -85.643  62.209  1.00 137.87 ? 52  SER   A OG  1 
ATOM   384   N  N   . SER   A  1  53  ? 60.400  -84.799  66.367  1.00 128.61 ? 53  SER   A N   1 
ATOM   385   C  CA  . SER   A  1  53  ? 60.449  -84.555  67.833  1.00 126.21 ? 53  SER   A CA  1 
ATOM   386   C  C   . SER   A  1  53  ? 61.719  -85.192  68.391  1.00 125.72 ? 53  SER   A C   1 
ATOM   387   O  O   . SER   A  1  53  ? 62.170  -86.208  67.869  1.00 123.03 ? 53  SER   A O   1 
ATOM   388   C  CB  . SER   A  1  53  ? 59.210  -85.104  68.501  1.00 123.12 ? 53  SER   A CB  1 
ATOM   389   O  OG  . SER   A  1  53  ? 59.276  -84.969  69.914  1.00 119.88 ? 53  SER   A OG  1 
ATOM   390   N  N   . PRO   A  1  54  ? 62.351  -84.627  69.448  1.00 128.99 ? 54  PRO   A N   1 
ATOM   391   C  CA  . PRO   A  1  54  ? 63.503  -85.278  70.074  1.00 126.08 ? 54  PRO   A CA  1 
ATOM   392   C  C   . PRO   A  1  54  ? 63.131  -86.567  70.827  1.00 120.92 ? 54  PRO   A C   1 
ATOM   393   O  O   . PRO   A  1  54  ? 64.034  -87.315  71.149  1.00 124.12 ? 54  PRO   A O   1 
ATOM   394   C  CB  . PRO   A  1  54  ? 64.065  -84.214  71.030  1.00 129.41 ? 54  PRO   A CB  1 
ATOM   395   C  CG  . PRO   A  1  54  ? 62.892  -83.304  71.315  1.00 131.67 ? 54  PRO   A CG  1 
ATOM   396   C  CD  . PRO   A  1  54  ? 62.026  -83.334  70.071  1.00 131.06 ? 54  PRO   A CD  1 
ATOM   397   N  N   . LEU   A  1  55  ? 61.836  -86.795  71.084  1.00 114.48 ? 55  LEU   A N   1 
ATOM   398   C  CA  . LEU   A  1  55  ? 61.306  -88.056  71.677  1.00 110.85 ? 55  LEU   A CA  1 
ATOM   399   C  C   . LEU   A  1  55  ? 61.202  -89.151  70.605  1.00 106.57 ? 55  LEU   A C   1 
ATOM   400   O  O   . LEU   A  1  55  ? 61.215  -90.338  70.981  1.00 102.71 ? 55  LEU   A O   1 
ATOM   401   C  CB  . LEU   A  1  55  ? 59.939  -87.794  72.315  1.00 106.58 ? 55  LEU   A CB  1 
ATOM   402   C  CG  . LEU   A  1  55  ? 59.940  -86.935  73.578  1.00 105.47 ? 55  LEU   A CG  1 
ATOM   403   C  CD1 . LEU   A  1  55  ? 58.530  -86.808  74.127  1.00 106.42 ? 55  LEU   A CD1 1 
ATOM   404   C  CD2 . LEU   A  1  55  ? 60.866  -87.504  74.642  1.00 105.07 ? 55  LEU   A CD2 1 
ATOM   405   N  N   . ALA   A  1  56  ? 61.087  -88.775  69.327  1.00 109.62 ? 56  ALA   A N   1 
ATOM   406   C  CA  . ALA   A  1  56  ? 61.079  -89.714  68.182  1.00 108.01 ? 56  ALA   A CA  1 
ATOM   407   C  C   . ALA   A  1  56  ? 62.441  -90.413  68.108  1.00 106.76 ? 56  ALA   A C   1 
ATOM   408   O  O   . ALA   A  1  56  ? 63.452  -89.788  68.484  1.00 103.68 ? 56  ALA   A O   1 
ATOM   409   C  CB  . ALA   A  1  56  ? 60.756  -88.990  66.895  1.00 109.53 ? 56  ALA   A CB  1 
ATOM   410   N  N   . MET   A  1  57  ? 62.449  -91.673  67.668  1.00 106.68 ? 57  MET   A N   1 
ATOM   411   C  CA  . MET   A  1  57  ? 63.675  -92.472  67.406  1.00 109.72 ? 57  MET   A CA  1 
ATOM   412   C  C   . MET   A  1  57  ? 63.910  -92.507  65.893  1.00 107.94 ? 57  MET   A C   1 
ATOM   413   O  O   . MET   A  1  57  ? 63.293  -93.353  65.223  1.00 100.86 ? 57  MET   A O   1 
ATOM   414   C  CB  . MET   A  1  57  ? 63.520  -93.897  67.943  1.00 110.19 ? 57  MET   A CB  1 
ATOM   415   C  CG  . MET   A  1  57  ? 63.241  -93.953  69.433  1.00 116.82 ? 57  MET   A CG  1 
ATOM   416   S  SD  . MET   A  1  57  ? 63.175  -95.647  70.085  1.00 121.64 ? 57  MET   A SD  1 
ATOM   417   C  CE  . MET   A  1  57  ? 61.717  -96.280  69.255  1.00 121.17 ? 57  MET   A CE  1 
ATOM   418   N  N   . SER   A  1  58  ? 64.764  -91.613  65.382  1.00 117.88 ? 58  SER   A N   1 
ATOM   419   C  CA  . SER   A  1  58  ? 64.969  -91.354  63.929  1.00 119.79 ? 58  SER   A CA  1 
ATOM   420   C  C   . SER   A  1  58  ? 65.603  -92.567  63.231  1.00 120.65 ? 58  SER   A C   1 
ATOM   421   O  O   . SER   A  1  58  ? 65.666  -92.550  61.986  1.00 125.04 ? 58  SER   A O   1 
ATOM   422   C  CB  . SER   A  1  58  ? 65.789  -90.107  63.708  1.00 123.36 ? 58  SER   A CB  1 
ATOM   423   O  OG  . SER   A  1  58  ? 67.044  -90.204  64.365  1.00 123.29 ? 58  SER   A OG  1 
ATOM   424   N  N   . GLU   A  1  59  ? 66.049  -93.574  63.991  1.00 118.18 ? 59  GLU   A N   1 
ATOM   425   C  CA  . GLU   A  1  59  ? 66.585  -94.855  63.449  1.00 118.41 ? 59  GLU   A CA  1 
ATOM   426   C  C   . GLU   A  1  59  ? 65.423  -95.676  62.871  1.00 111.73 ? 59  GLU   A C   1 
ATOM   427   O  O   . GLU   A  1  59  ? 65.634  -96.350  61.842  1.00 112.14 ? 59  GLU   A O   1 
ATOM   428   C  CB  . GLU   A  1  59  ? 67.327  -95.679  64.509  1.00 120.21 ? 59  GLU   A CB  1 
ATOM   429   C  CG  . GLU   A  1  59  ? 68.064  -94.859  65.558  1.00 125.52 ? 59  GLU   A CG  1 
ATOM   430   C  CD  . GLU   A  1  59  ? 67.252  -94.551  66.806  1.00 130.25 ? 59  GLU   A CD  1 
ATOM   431   O  OE1 . GLU   A  1  59  ? 66.798  -95.509  67.466  1.00 125.80 ? 59  GLU   A OE1 1 
ATOM   432   O  OE2 . GLU   A  1  59  ? 67.061  -93.354  67.108  1.00 138.43 ? 59  GLU   A OE2 1 
ATOM   433   N  N   . THR   A  1  60  ? 64.242  -95.604  63.499  1.00 108.08 ? 60  THR   A N   1 
ATOM   434   C  CA  . THR   A  1  60  ? 63.011  -96.337  63.093  1.00 104.78 ? 60  THR   A CA  1 
ATOM   435   C  C   . THR   A  1  60  ? 62.450  -95.759  61.786  1.00 109.06 ? 60  THR   A C   1 
ATOM   436   O  O   . THR   A  1  60  ? 61.638  -96.454  61.153  1.00 113.89 ? 60  THR   A O   1 
ATOM   437   C  CB  . THR   A  1  60  ? 61.947  -96.321  64.199  1.00 102.98 ? 60  THR   A CB  1 
ATOM   438   O  OG1 . THR   A  1  60  ? 61.548  -94.970  64.424  1.00 101.00 ? 60  THR   A OG1 1 
ATOM   439   C  CG2 . THR   A  1  60  ? 62.429  -96.938  65.494  1.00 101.82 ? 60  THR   A CG2 1 
ATOM   440   N  N   . LEU   A  1  61  ? 62.853  -94.543  61.401  1.00 112.89 ? 61  LEU   A N   1 
ATOM   441   C  CA  . LEU   A  1  61  ? 62.459  -93.899  60.119  1.00 116.86 ? 61  LEU   A CA  1 
ATOM   442   C  C   . LEU   A  1  61  ? 63.667  -93.913  59.174  1.00 113.39 ? 61  LEU   A C   1 
ATOM   443   O  O   . LEU   A  1  61  ? 64.621  -93.146  59.411  1.00 111.53 ? 61  LEU   A O   1 
ATOM   444   C  CB  . LEU   A  1  61  ? 61.968  -92.474  60.393  1.00 122.31 ? 61  LEU   A CB  1 
ATOM   445   C  CG  . LEU   A  1  61  ? 60.767  -92.012  59.566  1.00 128.30 ? 61  LEU   A CG  1 
ATOM   446   C  CD1 . LEU   A  1  61  ? 60.443  -90.555  59.860  1.00 130.23 ? 61  LEU   A CD1 1 
ATOM   447   C  CD2 . LEU   A  1  61  ? 61.001  -92.207  58.073  1.00 127.97 ? 61  LEU   A CD2 1 
ATOM   448   N  N   . SER   A  1  62  ? 63.626  -94.775  58.155  1.00 113.67 ? 62  SER   A N   1 
ATOM   449   C  CA  . SER   A  1  62  ? 64.696  -94.950  57.138  1.00 113.81 ? 62  SER   A CA  1 
ATOM   450   C  C   . SER   A  1  62  ? 64.329  -94.178  55.865  1.00 108.86 ? 62  SER   A C   1 
ATOM   451   O  O   . SER   A  1  62  ? 63.355  -94.569  55.192  1.00 115.14 ? 62  SER   A O   1 
ATOM   452   C  CB  . SER   A  1  62  ? 64.922  -96.411  56.853  1.00 116.01 ? 62  SER   A CB  1 
ATOM   453   O  OG  . SER   A  1  62  ? 66.015  -96.588  55.965  1.00 117.15 ? 62  SER   A OG  1 
ATOM   454   N  N   . LYS   A  1  63  ? 65.076  -93.113  55.562  1.00 104.20 ? 63  LYS   A N   1 
ATOM   455   C  CA  . LYS   A  1  63  ? 64.922  -92.298  54.327  1.00 102.22 ? 63  LYS   A CA  1 
ATOM   456   C  C   . LYS   A  1  63  ? 65.640  -92.995  53.164  1.00 97.53  ? 63  LYS   A C   1 
ATOM   457   O  O   . LYS   A  1  63  ? 65.139  -92.897  52.032  1.00 101.97 ? 63  LYS   A O   1 
ATOM   458   C  CB  . LYS   A  1  63  ? 65.452  -90.877  54.544  1.00 102.56 ? 63  LYS   A CB  1 
ATOM   459   C  CG  . LYS   A  1  63  ? 64.595  -90.000  55.449  1.00 101.16 ? 63  LYS   A CG  1 
ATOM   460   C  CD  . LYS   A  1  63  ? 65.071  -88.569  55.539  1.00 100.80 ? 63  LYS   A CD  1 
ATOM   461   C  CE  . LYS   A  1  63  ? 64.867  -87.796  54.254  1.00 102.93 ? 63  LYS   A CE  1 
ATOM   462   N  NZ  . LYS   A  1  63  ? 65.213  -86.365  54.414  1.00 105.70 ? 63  LYS   A NZ  1 
ATOM   463   N  N   . VAL   A  1  64  ? 66.767  -93.661  53.433  1.00 92.77  ? 64  VAL   A N   1 
ATOM   464   C  CA  . VAL   A  1  64  ? 67.536  -94.451  52.425  1.00 94.75  ? 64  VAL   A CA  1 
ATOM   465   C  C   . VAL   A  1  64  ? 67.103  -95.919  52.532  1.00 94.95  ? 64  VAL   A C   1 
ATOM   466   O  O   . VAL   A  1  64  ? 67.271  -96.500  53.623  1.00 94.90  ? 64  VAL   A O   1 
ATOM   467   C  CB  . VAL   A  1  64  ? 69.058  -94.304  52.617  1.00 97.50  ? 64  VAL   A CB  1 
ATOM   468   C  CG1 . VAL   A  1  64  ? 69.829  -95.051  51.541  1.00 101.16 ? 64  VAL   A CG1 1 
ATOM   469   C  CG2 . VAL   A  1  64  ? 69.494  -92.850  52.660  1.00 97.99  ? 64  VAL   A CG2 1 
ATOM   470   N  N   . SER   A  1  65  ? 66.590  -96.494  51.437  1.00 90.86  ? 65  SER   A N   1 
ATOM   471   C  CA  . SER   A  1  65  ? 65.995  -97.856  51.384  1.00 87.71  ? 65  SER   A CA  1 
ATOM   472   C  C   . SER   A  1  65  ? 66.720  -98.725  50.348  1.00 87.24  ? 65  SER   A C   1 
ATOM   473   O  O   . SER   A  1  65  ? 67.012  -98.218  49.250  1.00 84.74  ? 65  SER   A O   1 
ATOM   474   C  CB  . SER   A  1  65  ? 64.519  -97.785  51.091  1.00 86.02  ? 65  SER   A CB  1 
ATOM   475   O  OG  . SER   A  1  65  ? 63.848  -97.006  52.068  1.00 85.88  ? 65  SER   A OG  1 
ATOM   476   N  N   . LEU   A  1  66  ? 66.994  -99.986  50.705  1.00 87.75  ? 66  LEU   A N   1 
ATOM   477   C  CA  . LEU   A  1  66  ? 67.444  -101.065 49.782  1.00 87.87  ? 66  LEU   A CA  1 
ATOM   478   C  C   . LEU   A  1  66  ? 66.242  -101.508 48.938  1.00 87.18  ? 66  LEU   A C   1 
ATOM   479   O  O   . LEU   A  1  66  ? 65.201  -101.836 49.540  1.00 85.03  ? 66  LEU   A O   1 
ATOM   480   C  CB  . LEU   A  1  66  ? 68.003  -102.224 50.620  1.00 88.49  ? 66  LEU   A CB  1 
ATOM   481   C  CG  . LEU   A  1  66  ? 68.584  -103.420 49.859  1.00 89.59  ? 66  LEU   A CG  1 
ATOM   482   C  CD1 . LEU   A  1  66  ? 69.480  -104.251 50.767  1.00 90.10  ? 66  LEU   A CD1 1 
ATOM   483   C  CD2 . LEU   A  1  66  ? 67.490  -104.305 49.275  1.00 88.59  ? 66  LEU   A CD2 1 
ATOM   484   N  N   . LEU   A  1  67  ? 66.380  -101.515 47.606  1.00 88.92  ? 67  LEU   A N   1 
ATOM   485   C  CA  . LEU   A  1  67  ? 65.345  -102.010 46.654  1.00 90.29  ? 67  LEU   A CA  1 
ATOM   486   C  C   . LEU   A  1  67  ? 65.712  -103.420 46.186  1.00 90.36  ? 67  LEU   A C   1 
ATOM   487   O  O   . LEU   A  1  67  ? 64.824  -104.286 46.206  1.00 97.20  ? 67  LEU   A O   1 
ATOM   488   C  CB  . LEU   A  1  67  ? 65.242  -101.060 45.457  1.00 89.39  ? 67  LEU   A CB  1 
ATOM   489   C  CG  . LEU   A  1  67  ? 64.906  -99.603  45.773  1.00 89.10  ? 67  LEU   A CG  1 
ATOM   490   C  CD1 . LEU   A  1  67  ? 64.611  -98.844  44.488  1.00 87.24  ? 67  LEU   A CD1 1 
ATOM   491   C  CD2 . LEU   A  1  67  ? 63.733  -99.492  46.738  1.00 88.67  ? 67  LEU   A CD2 1 
ATOM   492   N  N   . THR   A  1  68  ? 66.961  -103.612 45.745  1.00 90.67  ? 68  THR   A N   1 
ATOM   493   C  CA  . THR   A  1  68  ? 67.599  -104.930 45.468  1.00 91.55  ? 68  THR   A CA  1 
ATOM   494   C  C   . THR   A  1  68  ? 68.965  -104.946 46.148  1.00 93.13  ? 68  THR   A C   1 
ATOM   495   O  O   . THR   A  1  68  ? 69.445  -103.901 46.580  1.00 93.46  ? 68  THR   A O   1 
ATOM   496   C  CB  . THR   A  1  68  ? 67.711  -105.209 43.961  1.00 89.68  ? 68  THR   A CB  1 
ATOM   497   O  OG1 . THR   A  1  68  ? 68.781  -104.435 43.416  1.00 86.77  ? 68  THR   A OG1 1 
ATOM   498   C  CG2 . THR   A  1  68  ? 66.425  -104.927 43.214  1.00 91.69  ? 68  THR   A CG2 1 
ATOM   499   N  N   . PRO   A  1  69  ? 69.638  -106.112 46.275  1.00 95.23  ? 69  PRO   A N   1 
ATOM   500   C  CA  . PRO   A  1  69  ? 70.984  -106.159 46.850  1.00 97.34  ? 69  PRO   A CA  1 
ATOM   501   C  C   . PRO   A  1  69  ? 72.005  -105.204 46.208  1.00 96.12  ? 69  PRO   A C   1 
ATOM   502   O  O   . PRO   A  1  69  ? 73.014  -104.956 46.843  1.00 102.23 ? 69  PRO   A O   1 
ATOM   503   C  CB  . PRO   A  1  69  ? 71.420  -107.612 46.609  1.00 99.33  ? 69  PRO   A CB  1 
ATOM   504   C  CG  . PRO   A  1  69  ? 70.120  -108.384 46.593  1.00 100.00 ? 69  PRO   A CG  1 
ATOM   505   C  CD  . PRO   A  1  69  ? 69.130  -107.450 45.929  1.00 97.47  ? 69  PRO   A CD  1 
ATOM   506   N  N   . ASP   A  1  70  ? 71.738  -104.708 44.992  1.00 94.73  ? 70  ASP   A N   1 
ATOM   507   C  CA  . ASP   A  1  70  ? 72.665  -103.829 44.226  1.00 96.53  ? 70  ASP   A CA  1 
ATOM   508   C  C   . ASP   A  1  70  ? 72.023  -102.469 43.905  1.00 93.56  ? 70  ASP   A C   1 
ATOM   509   O  O   . ASP   A  1  70  ? 72.652  -101.709 43.144  1.00 89.97  ? 70  ASP   A O   1 
ATOM   510   C  CB  . ASP   A  1  70  ? 73.112  -104.509 42.928  1.00 102.03 ? 70  ASP   A CB  1 
ATOM   511   C  CG  . ASP   A  1  70  ? 73.867  -105.812 43.128  1.00 104.32 ? 70  ASP   A CG  1 
ATOM   512   O  OD1 . ASP   A  1  70  ? 74.524  -105.958 44.180  1.00 113.70 ? 70  ASP   A OD1 1 
ATOM   513   O  OD2 . ASP   A  1  70  ? 73.795  -106.671 42.227  1.00 110.67 ? 70  ASP   A OD2 1 
ATOM   514   N  N   . ILE   A  1  71  ? 70.836  -102.159 44.442  1.00 91.42  ? 71  ILE   A N   1 
ATOM   515   C  CA  . ILE   A  1  71  ? 70.119  -100.872 44.174  1.00 91.11  ? 71  ILE   A CA  1 
ATOM   516   C  C   . ILE   A  1  71  ? 69.576  -100.295 45.488  1.00 91.72  ? 71  ILE   A C   1 
ATOM   517   O  O   . ILE   A  1  71  ? 68.940  -101.049 46.253  1.00 89.75  ? 71  ILE   A O   1 
ATOM   518   C  CB  . ILE   A  1  71  ? 68.991  -101.052 43.137  1.00 87.96  ? 71  ILE   A CB  1 
ATOM   519   C  CG1 . ILE   A  1  71  ? 69.531  -101.494 41.774  1.00 86.79  ? 71  ILE   A CG1 1 
ATOM   520   C  CG2 . ILE   A  1  71  ? 68.163  -99.780  43.022  1.00 87.65  ? 71  ILE   A CG2 1 
ATOM   521   C  CD1 . ILE   A  1  71  ? 68.482  -102.078 40.857  1.00 86.40  ? 71  ILE   A CD1 1 
ATOM   522   N  N   . GLY   A  1  72  ? 69.792  -98.992  45.700  1.00 93.58  ? 72  GLY   A N   1 
ATOM   523   C  CA  . GLY   A  1  72  ? 69.277  -98.219  46.848  1.00 91.28  ? 72  GLY   A CA  1 
ATOM   524   C  C   . GLY   A  1  72  ? 68.612  -96.930  46.391  1.00 88.26  ? 72  GLY   A C   1 
ATOM   525   O  O   . GLY   A  1  72  ? 68.979  -96.423  45.313  1.00 84.12  ? 72  GLY   A O   1 
ATOM   526   N  N   . ALA   A  1  73  ? 67.667  -96.419  47.183  1.00 86.01  ? 73  ALA   A N   1 
ATOM   527   C  CA  . ALA   A  1  73  ? 66.856  -95.223  46.863  1.00 86.04  ? 73  ALA   A CA  1 
ATOM   528   C  C   . ALA   A  1  73  ? 66.858  -94.244  48.040  1.00 87.32  ? 73  ALA   A C   1 
ATOM   529   O  O   . ALA   A  1  73  ? 66.874  -94.692  49.201  1.00 82.74  ? 73  ALA   A O   1 
ATOM   530   C  CB  . ALA   A  1  73  ? 65.450  -95.634  46.508  1.00 86.82  ? 73  ALA   A CB  1 
ATOM   531   N  N   . VAL   A  1  74  ? 66.838  -92.950  47.720  1.00 88.52  ? 74  VAL   A N   1 
ATOM   532   C  CA  . VAL   A  1  74  ? 66.616  -91.819  48.667  1.00 89.05  ? 74  VAL   A CA  1 
ATOM   533   C  C   . VAL   A  1  74  ? 65.701  -90.818  47.953  1.00 88.54  ? 74  VAL   A C   1 
ATOM   534   O  O   . VAL   A  1  74  ? 65.571  -90.920  46.711  1.00 85.69  ? 74  VAL   A O   1 
ATOM   535   C  CB  . VAL   A  1  74  ? 67.951  -91.193  49.117  1.00 91.22  ? 74  VAL   A CB  1 
ATOM   536   C  CG1 . VAL   A  1  74  ? 68.579  -90.333  48.031  1.00 92.46  ? 74  VAL   A CG1 1 
ATOM   537   C  CG2 . VAL   A  1  74  ? 67.805  -90.403  50.408  1.00 92.99  ? 74  VAL   A CG2 1 
ATOM   538   N  N   . TYR   A  1  75  ? 65.080  -89.899  48.693  1.00 87.10  ? 75  TYR   A N   1 
ATOM   539   C  CA  . TYR   A  1  75  ? 64.044  -88.987  48.151  1.00 86.28  ? 75  TYR   A CA  1 
ATOM   540   C  C   . TYR   A  1  75  ? 64.132  -87.599  48.789  1.00 86.43  ? 75  TYR   A C   1 
ATOM   541   O  O   . TYR   A  1  75  ? 64.788  -87.422  49.837  1.00 85.77  ? 75  TYR   A O   1 
ATOM   542   C  CB  . TYR   A  1  75  ? 62.654  -89.568  48.405  1.00 85.45  ? 75  TYR   A CB  1 
ATOM   543   C  CG  . TYR   A  1  75  ? 62.137  -89.309  49.796  1.00 84.32  ? 75  TYR   A CG  1 
ATOM   544   C  CD1 . TYR   A  1  75  ? 62.705  -89.928  50.896  1.00 83.85  ? 75  TYR   A CD1 1 
ATOM   545   C  CD2 . TYR   A  1  75  ? 61.097  -88.422  50.016  1.00 85.52  ? 75  TYR   A CD2 1 
ATOM   546   C  CE1 . TYR   A  1  75  ? 62.244  -89.687  52.179  1.00 84.28  ? 75  TYR   A CE1 1 
ATOM   547   C  CE2 . TYR   A  1  75  ? 60.621  -88.171  51.292  1.00 86.89  ? 75  TYR   A CE2 1 
ATOM   548   C  CZ  . TYR   A  1  75  ? 61.197  -88.806  52.378  1.00 85.34  ? 75  TYR   A CZ  1 
ATOM   549   O  OH  . TYR   A  1  75  ? 60.745  -88.564  53.642  1.00 86.49  ? 75  TYR   A OH  1 
ATOM   550   N  N   . SER   A  1  76  ? 63.463  -86.648  48.138  1.00 86.52  ? 76  SER   A N   1 
ATOM   551   C  CA  . SER   A  1  76  ? 63.047  -85.339  48.693  1.00 88.38  ? 76  SER   A CA  1 
ATOM   552   C  C   . SER   A  1  76  ? 61.543  -85.186  48.458  1.00 83.53  ? 76  SER   A C   1 
ATOM   553   O  O   . SER   A  1  76  ? 61.076  -85.569  47.368  1.00 85.91  ? 76  SER   A O   1 
ATOM   554   C  CB  . SER   A  1  76  ? 63.835  -84.216  48.079  1.00 88.90  ? 76  SER   A CB  1 
ATOM   555   O  OG  . SER   A  1  76  ? 65.152  -84.188  48.607  1.00 92.98  ? 76  SER   A OG  1 
ATOM   556   N  N   . GLY   A  1  77  ? 60.816  -84.684  49.455  1.00 83.91  ? 77  GLY   A N   1 
ATOM   557   C  CA  . GLY   A  1  77  ? 59.367  -84.435  49.365  1.00 84.03  ? 77  GLY   A CA  1 
ATOM   558   C  C   . GLY   A  1  77  ? 58.619  -85.154  50.467  1.00 82.17  ? 77  GLY   A C   1 
ATOM   559   O  O   . GLY   A  1  77  ? 59.088  -85.117  51.619  1.00 83.47  ? 77  GLY   A O   1 
ATOM   560   N  N   . MET   A  1  78  ? 57.510  -85.806  50.119  1.00 81.57  ? 78  MET   A N   1 
ATOM   561   C  CA  . MET   A  1  78  ? 56.538  -86.378  51.087  1.00 86.50  ? 78  MET   A CA  1 
ATOM   562   C  C   . MET   A  1  78  ? 56.929  -87.819  51.436  1.00 85.95  ? 78  MET   A C   1 
ATOM   563   O  O   . MET   A  1  78  ? 56.911  -88.672  50.530  1.00 87.86  ? 78  MET   A O   1 
ATOM   564   C  CB  . MET   A  1  78  ? 55.127  -86.358  50.499  1.00 88.86  ? 78  MET   A CB  1 
ATOM   565   C  CG  . MET   A  1  78  ? 54.659  -84.970  50.132  1.00 92.08  ? 78  MET   A CG  1 
ATOM   566   S  SD  . MET   A  1  78  ? 53.089  -85.016  49.250  1.00 97.14  ? 78  MET   A SD  1 
ATOM   567   C  CE  . MET   A  1  78  ? 51.984  -85.491  50.577  1.00 98.42  ? 78  MET   A CE  1 
ATOM   568   N  N   . GLY   A  1  79  ? 57.248  -88.069  52.711  1.00 89.37  ? 79  GLY   A N   1 
ATOM   569   C  CA  . GLY   A  1  79  ? 57.716  -89.367  53.239  1.00 86.89  ? 79  GLY   A CA  1 
ATOM   570   C  C   . GLY   A  1  79  ? 56.740  -90.506  52.958  1.00 84.27  ? 79  GLY   A C   1 
ATOM   571   O  O   . GLY   A  1  79  ? 57.123  -91.501  52.350  1.00 83.28  ? 79  GLY   A O   1 
ATOM   572   N  N   . PRO   A  1  80  ? 55.465  -90.414  53.403  1.00 83.88  ? 80  PRO   A N   1 
ATOM   573   C  CA  . PRO   A  1  80  ? 54.477  -91.465  53.146  1.00 84.83  ? 80  PRO   A CA  1 
ATOM   574   C  C   . PRO   A  1  80  ? 54.404  -91.922  51.677  1.00 85.63  ? 80  PRO   A C   1 
ATOM   575   O  O   . PRO   A  1  80  ? 54.350  -93.117  51.443  1.00 84.78  ? 80  PRO   A O   1 
ATOM   576   C  CB  . PRO   A  1  80  ? 53.159  -90.805  53.584  1.00 84.16  ? 80  PRO   A CB  1 
ATOM   577   C  CG  . PRO   A  1  80  ? 53.577  -89.849  54.673  1.00 85.74  ? 80  PRO   A CG  1 
ATOM   578   C  CD  . PRO   A  1  80  ? 54.913  -89.311  54.203  1.00 86.04  ? 80  PRO   A CD  1 
ATOM   579   N  N   . ASP   A  1  81  ? 54.408  -90.975  50.732  1.00 88.62  ? 81  ASP   A N   1 
ATOM   580   C  CA  . ASP   A  1  81  ? 54.383  -91.245  49.267  1.00 87.35  ? 81  ASP   A CA  1 
ATOM   581   C  C   . ASP   A  1  81  ? 55.614  -92.073  48.882  1.00 86.15  ? 81  ASP   A C   1 
ATOM   582   O  O   . ASP   A  1  81  ? 55.466  -92.988  48.057  1.00 85.31  ? 81  ASP   A O   1 
ATOM   583   C  CB  . ASP   A  1  81  ? 54.321  -89.950  48.448  1.00 90.81  ? 81  ASP   A CB  1 
ATOM   584   C  CG  . ASP   A  1  81  ? 52.937  -89.330  48.357  1.00 92.35  ? 81  ASP   A CG  1 
ATOM   585   O  OD1 . ASP   A  1  81  ? 52.070  -89.683  49.184  1.00 92.59  ? 81  ASP   A OD1 1 
ATOM   586   O  OD2 . ASP   A  1  81  ? 52.734  -88.495  47.455  1.00 96.22  ? 81  ASP   A OD2 1 
ATOM   587   N  N   . TYR   A  1  82  ? 56.780  -91.750  49.449  1.00 84.95  ? 82  TYR   A N   1 
ATOM   588   C  CA  . TYR   A  1  82  ? 58.069  -92.454  49.210  1.00 86.75  ? 82  TYR   A CA  1 
ATOM   589   C  C   . TYR   A  1  82  ? 57.978  -93.886  49.744  1.00 87.79  ? 82  TYR   A C   1 
ATOM   590   O  O   . TYR   A  1  82  ? 58.390  -94.817  49.026  1.00 89.77  ? 82  TYR   A O   1 
ATOM   591   C  CB  . TYR   A  1  82  ? 59.238  -91.713  49.867  1.00 87.10  ? 82  TYR   A CB  1 
ATOM   592   C  CG  . TYR   A  1  82  ? 60.523  -92.501  49.952  1.00 86.25  ? 82  TYR   A CG  1 
ATOM   593   C  CD1 . TYR   A  1  82  ? 61.273  -92.768  48.819  1.00 85.20  ? 82  TYR   A CD1 1 
ATOM   594   C  CD2 . TYR   A  1  82  ? 60.996  -92.975  51.165  1.00 86.20  ? 82  TYR   A CD2 1 
ATOM   595   C  CE1 . TYR   A  1  82  ? 62.458  -93.482  48.885  1.00 84.34  ? 82  TYR   A CE1 1 
ATOM   596   C  CE2 . TYR   A  1  82  ? 62.178  -93.695  51.250  1.00 84.93  ? 82  TYR   A CE2 1 
ATOM   597   C  CZ  . TYR   A  1  82  ? 62.914  -93.951  50.105  1.00 83.59  ? 82  TYR   A CZ  1 
ATOM   598   O  OH  . TYR   A  1  82  ? 64.080  -94.660  50.176  1.00 78.88  ? 82  TYR   A OH  1 
ATOM   599   N  N   . ARG   A  1  83  ? 57.456  -94.048  50.964  1.00 86.65  ? 83  ARG   A N   1 
ATOM   600   C  CA  . ARG   A  1  83  ? 57.378  -95.353  51.675  1.00 86.53  ? 83  ARG   A CA  1 
ATOM   601   C  C   . ARG   A  1  83  ? 56.623  -96.381  50.817  1.00 87.24  ? 83  ARG   A C   1 
ATOM   602   O  O   . ARG   A  1  83  ? 57.146  -97.507  50.666  1.00 88.62  ? 83  ARG   A O   1 
ATOM   603   C  CB  . ARG   A  1  83  ? 56.711  -95.196  53.044  1.00 84.11  ? 83  ARG   A CB  1 
ATOM   604   C  CG  . ARG   A  1  83  ? 56.882  -96.414  53.940  1.00 83.32  ? 83  ARG   A CG  1 
ATOM   605   C  CD  . ARG   A  1  83  ? 56.234  -96.250  55.298  1.00 83.17  ? 83  ARG   A CD  1 
ATOM   606   N  NE  . ARG   A  1  83  ? 54.812  -95.964  55.179  1.00 80.34  ? 83  ARG   A NE  1 
ATOM   607   C  CZ  . ARG   A  1  83  ? 54.217  -94.829  55.525  1.00 81.40  ? 83  ARG   A CZ  1 
ATOM   608   N  NH1 . ARG   A  1  83  ? 54.912  -93.830  56.046  1.00 83.78  ? 83  ARG   A NH1 1 
ATOM   609   N  NH2 . ARG   A  1  83  ? 52.911  -94.703  55.360  1.00 78.73  ? 83  ARG   A NH2 1 
ATOM   610   N  N   . VAL   A  1  84  ? 55.446  -96.022  50.284  1.00 85.64  ? 84  VAL   A N   1 
ATOM   611   C  CA  . VAL   A  1  84  ? 54.592  -96.942  49.468  1.00 83.38  ? 84  VAL   A CA  1 
ATOM   612   C  C   . VAL   A  1  84  ? 55.236  -97.158  48.093  1.00 84.61  ? 84  VAL   A C   1 
ATOM   613   O  O   . VAL   A  1  84  ? 55.024  -98.238  47.526  1.00 86.23  ? 84  VAL   A O   1 
ATOM   614   C  CB  . VAL   A  1  84  ? 53.136  -96.458  49.323  1.00 83.16  ? 84  VAL   A CB  1 
ATOM   615   C  CG1 . VAL   A  1  84  ? 52.456  -96.308  50.673  1.00 82.18  ? 84  VAL   A CG1 1 
ATOM   616   C  CG2 . VAL   A  1  84  ? 53.024  -95.174  48.519  1.00 84.54  ? 84  VAL   A CG2 1 
ATOM   617   N  N   . LEU   A  1  85  ? 55.967  -96.169  47.570  1.00 84.24  ? 85  LEU   A N   1 
ATOM   618   C  CA  . LEU   A  1  85  ? 56.720  -96.301  46.292  1.00 88.14  ? 85  LEU   A CA  1 
ATOM   619   C  C   . LEU   A  1  85  ? 57.854  -97.319  46.454  1.00 90.30  ? 85  LEU   A C   1 
ATOM   620   O  O   . LEU   A  1  85  ? 58.140  -98.017  45.466  1.00 96.28  ? 85  LEU   A O   1 
ATOM   621   C  CB  . LEU   A  1  85  ? 57.276  -94.946  45.849  1.00 89.83  ? 85  LEU   A CB  1 
ATOM   622   C  CG  . LEU   A  1  85  ? 56.390  -94.151  44.892  1.00 93.47  ? 85  LEU   A CG  1 
ATOM   623   C  CD1 . LEU   A  1  85  ? 56.974  -92.770  44.644  1.00 97.72  ? 85  LEU   A CD1 1 
ATOM   624   C  CD2 . LEU   A  1  85  ? 56.199  -94.887  43.573  1.00 95.31  ? 85  LEU   A CD2 1 
ATOM   625   N  N   . VAL   A  1  86  ? 58.476  -97.396  47.637  1.00 90.90  ? 86  VAL   A N   1 
ATOM   626   C  CA  . VAL   A  1  86  ? 59.565  -98.376  47.943  1.00 94.09  ? 86  VAL   A CA  1 
ATOM   627   C  C   . VAL   A  1  86  ? 58.967  -99.792  47.991  1.00 93.70  ? 86  VAL   A C   1 
ATOM   628   O  O   . VAL   A  1  86  ? 59.578  -100.709 47.400  1.00 92.26  ? 86  VAL   A O   1 
ATOM   629   C  CB  . VAL   A  1  86  ? 60.308  -98.024  49.248  1.00 93.23  ? 86  VAL   A CB  1 
ATOM   630   C  CG1 . VAL   A  1  86  ? 61.280  -99.119  49.665  1.00 94.37  ? 86  VAL   A CG1 1 
ATOM   631   C  CG2 . VAL   A  1  86  ? 61.037  -96.695  49.137  1.00 94.10  ? 86  VAL   A CG2 1 
ATOM   632   N  N   . ASP   A  1  87  ? 57.828  -99.965  48.674  1.00 95.51  ? 87  ASP   A N   1 
ATOM   633   C  CA  . ASP   A  1  87  ? 57.079  -101.250 48.756  1.00 96.07  ? 87  ASP   A CA  1 
ATOM   634   C  C   . ASP   A  1  87  ? 56.775  -101.745 47.334  1.00 95.83  ? 87  ASP   A C   1 
ATOM   635   O  O   . ASP   A  1  87  ? 57.102  -102.913 47.029  1.00 95.94  ? 87  ASP   A O   1 
ATOM   636   C  CB  . ASP   A  1  87  ? 55.789  -101.105 49.573  1.00 99.20  ? 87  ASP   A CB  1 
ATOM   637   C  CG  . ASP   A  1  87  ? 55.999  -100.852 51.059  1.00 103.61 ? 87  ASP   A CG  1 
ATOM   638   O  OD1 . ASP   A  1  87  ? 56.977  -101.398 51.620  1.00 105.83 ? 87  ASP   A OD1 1 
ATOM   639   O  OD2 . ASP   A  1  87  ? 55.175  -100.117 51.649  1.00 103.92 ? 87  ASP   A OD2 1 
ATOM   640   N  N   . LYS   A  1  88  ? 56.181  -100.881 46.502  1.00 89.40  ? 88  LYS   A N   1 
ATOM   641   C  CA  . LYS   A  1  88  ? 55.783  -101.180 45.098  1.00 87.41  ? 88  LYS   A CA  1 
ATOM   642   C  C   . LYS   A  1  88  ? 57.024  -101.448 44.238  1.00 85.31  ? 88  LYS   A C   1 
ATOM   643   O  O   . LYS   A  1  88  ? 56.959  -102.355 43.389  1.00 87.67  ? 88  LYS   A O   1 
ATOM   644   C  CB  . LYS   A  1  88  ? 54.984  -100.020 44.498  1.00 86.85  ? 88  LYS   A CB  1 
ATOM   645   C  CG  . LYS   A  1  88  ? 53.565  -99.867  45.026  1.00 90.07  ? 88  LYS   A CG  1 
ATOM   646   C  CD  . LYS   A  1  88  ? 52.955  -98.520  44.700  1.00 92.33  ? 88  LYS   A CD  1 
ATOM   647   C  CE  . LYS   A  1  88  ? 51.688  -98.229  45.476  1.00 95.44  ? 88  LYS   A CE  1 
ATOM   648   N  NZ  . LYS   A  1  88  ? 50.533  -98.985  44.938  1.00 99.68  ? 88  LYS   A NZ  1 
ATOM   649   N  N   . SER   A  1  89  ? 58.094  -100.671 44.432  1.00 83.32  ? 89  SER   A N   1 
ATOM   650   C  CA  . SER   A  1  89  ? 59.379  -100.791 43.692  1.00 84.39  ? 89  SER   A CA  1 
ATOM   651   C  C   . SER   A  1  89  ? 60.035  -102.146 43.983  1.00 84.35  ? 89  SER   A C   1 
ATOM   652   O  O   . SER   A  1  89  ? 60.514  -102.782 43.025  1.00 85.85  ? 89  SER   A O   1 
ATOM   653   C  CB  . SER   A  1  89  ? 60.322  -99.660  44.022  1.00 83.53  ? 89  SER   A CB  1 
ATOM   654   O  OG  . SER   A  1  89  ? 59.839  -98.427  43.510  1.00 81.13  ? 89  SER   A OG  1 
ATOM   655   N  N   . ARG   A  1  90  ? 60.079  -102.553 45.257  1.00 84.82  ? 90  ARG   A N   1 
ATOM   656   C  CA  . ARG   A  1  90  ? 60.690  -103.837 45.698  1.00 85.54  ? 90  ARG   A CA  1 
ATOM   657   C  C   . ARG   A  1  90  ? 59.934  -105.008 45.057  1.00 84.47  ? 90  ARG   A C   1 
ATOM   658   O  O   . ARG   A  1  90  ? 60.603  -105.948 44.581  1.00 83.48  ? 90  ARG   A O   1 
ATOM   659   C  CB  . ARG   A  1  90  ? 60.693  -103.943 47.226  1.00 85.43  ? 90  ARG   A CB  1 
ATOM   660   C  CG  . ARG   A  1  90  ? 61.755  -103.093 47.905  1.00 84.89  ? 90  ARG   A CG  1 
ATOM   661   C  CD  . ARG   A  1  90  ? 61.479  -102.957 49.387  1.00 85.75  ? 90  ARG   A CD  1 
ATOM   662   N  NE  . ARG   A  1  90  ? 62.572  -102.306 50.088  1.00 85.35  ? 90  ARG   A NE  1 
ATOM   663   C  CZ  . ARG   A  1  90  ? 62.539  -101.935 51.363  1.00 88.14  ? 90  ARG   A CZ  1 
ATOM   664   N  NH1 . ARG   A  1  90  ? 61.458  -102.155 52.097  1.00 87.16  ? 90  ARG   A NH1 1 
ATOM   665   N  NH2 . ARG   A  1  90  ? 63.591  -101.340 51.901  1.00 91.51  ? 90  ARG   A NH2 1 
ATOM   666   N  N   . LYS   A  1  91  ? 58.598  -104.944 45.035  1.00 84.87  ? 91  LYS   A N   1 
ATOM   667   C  CA  . LYS   A  1  91  ? 57.717  -106.032 44.527  1.00 84.31  ? 91  LYS   A CA  1 
ATOM   668   C  C   . LYS   A  1  91  ? 57.867  -106.173 43.010  1.00 83.61  ? 91  LYS   A C   1 
ATOM   669   O  O   . LYS   A  1  91  ? 57.887  -107.312 42.536  1.00 82.91  ? 91  LYS   A O   1 
ATOM   670   C  CB  . LYS   A  1  91  ? 56.248  -105.770 44.867  1.00 85.47  ? 91  LYS   A CB  1 
ATOM   671   C  CG  . LYS   A  1  91  ? 55.332  -106.964 44.648  1.00 86.07  ? 91  LYS   A CG  1 
ATOM   672   C  CD  . LYS   A  1  91  ? 53.876  -106.663 44.887  1.00 89.42  ? 91  LYS   A CD  1 
ATOM   673   C  CE  . LYS   A  1  91  ? 53.016  -107.905 44.838  1.00 94.16  ? 91  LYS   A CE  1 
ATOM   674   N  NZ  . LYS   A  1  91  ? 51.610  -107.613 45.201  1.00 99.35  ? 91  LYS   A NZ  1 
ATOM   675   N  N   . VAL   A  1  92  ? 57.948  -105.059 42.279  1.00 84.04  ? 92  VAL   A N   1 
ATOM   676   C  CA  . VAL   A  1  92  ? 57.984  -105.050 40.785  1.00 84.34  ? 92  VAL   A CA  1 
ATOM   677   C  C   . VAL   A  1  92  ? 59.346  -105.578 40.310  1.00 83.21  ? 92  VAL   A C   1 
ATOM   678   O  O   . VAL   A  1  92  ? 59.395  -106.132 39.199  1.00 83.84  ? 92  VAL   A O   1 
ATOM   679   C  CB  . VAL   A  1  92  ? 57.657  -103.657 40.207  1.00 84.56  ? 92  VAL   A CB  1 
ATOM   680   C  CG1 . VAL   A  1  92  ? 58.817  -102.682 40.329  1.00 85.50  ? 92  VAL   A CG1 1 
ATOM   681   C  CG2 . VAL   A  1  92  ? 57.193  -103.741 38.763  1.00 84.93  ? 92  VAL   A CG2 1 
ATOM   682   N  N   . ALA   A  1  93  ? 60.403  -105.433 41.119  1.00 82.22  ? 93  ALA   A N   1 
ATOM   683   C  CA  . ALA   A  1  93  ? 61.752  -105.983 40.840  1.00 85.53  ? 93  ALA   A CA  1 
ATOM   684   C  C   . ALA   A  1  93  ? 61.693  -107.515 40.832  1.00 85.63  ? 93  ALA   A C   1 
ATOM   685   O  O   . ALA   A  1  93  ? 62.538  -108.131 40.157  1.00 90.41  ? 93  ALA   A O   1 
ATOM   686   C  CB  . ALA   A  1  93  ? 62.751  -105.484 41.854  1.00 86.04  ? 93  ALA   A CB  1 
ATOM   687   N  N   . HIS   A  1  94  ? 60.738  -108.097 41.566  1.00 87.01  ? 94  HIS   A N   1 
ATOM   688   C  CA  . HIS   A  1  94  ? 60.496  -109.563 41.649  1.00 87.60  ? 94  HIS   A CA  1 
ATOM   689   C  C   . HIS   A  1  94  ? 59.522  -109.995 40.547  1.00 87.91  ? 94  HIS   A C   1 
ATOM   690   O  O   . HIS   A  1  94  ? 59.934  -110.803 39.692  1.00 91.67  ? 94  HIS   A O   1 
ATOM   691   C  CB  . HIS   A  1  94  ? 60.000  -109.955 43.050  1.00 86.85  ? 94  HIS   A CB  1 
ATOM   692   C  CG  . HIS   A  1  94  ? 61.094  -110.108 44.051  1.00 88.34  ? 94  HIS   A CG  1 
ATOM   693   N  ND1 . HIS   A  1  94  ? 61.652  -109.031 44.702  1.00 88.51  ? 94  HIS   A ND1 1 
ATOM   694   C  CD2 . HIS   A  1  94  ? 61.740  -111.201 44.509  1.00 91.53  ? 94  HIS   A CD2 1 
ATOM   695   C  CE1 . HIS   A  1  94  ? 62.592  -109.452 45.521  1.00 89.97  ? 94  HIS   A CE1 1 
ATOM   696   N  NE2 . HIS   A  1  94  ? 62.666  -110.778 45.423  1.00 91.13  ? 94  HIS   A NE2 1 
ATOM   697   N  N   . THR   A  1  95  ? 58.289  -109.473 40.565  1.00 85.59  ? 95  THR   A N   1 
ATOM   698   C  CA  . THR   A  1  95  ? 57.151  -109.951 39.729  1.00 87.35  ? 95  THR   A CA  1 
ATOM   699   C  C   . THR   A  1  95  ? 57.497  -109.814 38.245  1.00 88.47  ? 95  THR   A C   1 
ATOM   700   O  O   . THR   A  1  95  ? 57.304  -110.795 37.503  1.00 89.38  ? 95  THR   A O   1 
ATOM   701   C  CB  . THR   A  1  95  ? 55.840  -109.208 40.022  1.00 88.90  ? 95  THR   A CB  1 
ATOM   702   O  OG1 . THR   A  1  95  ? 56.032  -107.817 39.755  1.00 90.27  ? 95  THR   A OG1 1 
ATOM   703   C  CG2 . THR   A  1  95  ? 55.354  -109.414 41.441  1.00 89.79  ? 95  THR   A CG2 1 
ATOM   704   N  N   . SER   A  1  96  ? 57.990  -108.644 37.836  1.00 89.34  ? 96  SER   A N   1 
ATOM   705   C  CA  . SER   A  1  96  ? 58.196  -108.287 36.409  1.00 91.32  ? 96  SER   A CA  1 
ATOM   706   C  C   . SER   A  1  96  ? 59.632  -108.586 35.951  1.00 90.61  ? 96  SER   A C   1 
ATOM   707   O  O   . SER   A  1  96  ? 59.921  -108.296 34.774  1.00 92.73  ? 96  SER   A O   1 
ATOM   708   C  CB  . SER   A  1  96  ? 57.827  -106.848 36.163  1.00 91.44  ? 96  SER   A CB  1 
ATOM   709   O  OG  . SER   A  1  96  ? 58.798  -105.974 36.713  1.00 92.85  ? 96  SER   A OG  1 
ATOM   710   N  N   . TYR   A  1  97  ? 60.497  -109.149 36.806  1.00 89.24  ? 97  TYR   A N   1 
ATOM   711   C  CA  . TYR   A  1  97  ? 61.899  -109.467 36.419  1.00 90.28  ? 97  TYR   A CA  1 
ATOM   712   C  C   . TYR   A  1  97  ? 62.418  -110.747 37.089  1.00 91.01  ? 97  TYR   A C   1 
ATOM   713   O  O   . TYR   A  1  97  ? 62.652  -111.715 36.339  1.00 95.43  ? 97  TYR   A O   1 
ATOM   714   C  CB  . TYR   A  1  97  ? 62.825  -108.278 36.677  1.00 88.02  ? 97  TYR   A CB  1 
ATOM   715   C  CG  . TYR   A  1  97  ? 64.033  -108.270 35.777  1.00 88.74  ? 97  TYR   A CG  1 
ATOM   716   C  CD1 . TYR   A  1  97  ? 65.195  -108.931 36.138  1.00 90.87  ? 97  TYR   A CD1 1 
ATOM   717   C  CD2 . TYR   A  1  97  ? 64.006  -107.636 34.546  1.00 89.17  ? 97  TYR   A CD2 1 
ATOM   718   C  CE1 . TYR   A  1  97  ? 66.308  -108.946 35.311  1.00 91.44  ? 97  TYR   A CE1 1 
ATOM   719   C  CE2 . TYR   A  1  97  ? 65.110  -107.639 33.708  1.00 89.92  ? 97  TYR   A CE2 1 
ATOM   720   C  CZ  . TYR   A  1  97  ? 66.266  -108.296 34.090  1.00 89.58  ? 97  TYR   A CZ  1 
ATOM   721   O  OH  . TYR   A  1  97  ? 67.356  -108.303 33.268  1.00 89.23  ? 97  TYR   A OH  1 
ATOM   722   N  N   . LYS   A  1  98  ? 62.639  -110.767 38.410  1.00 88.32  ? 98  LYS   A N   1 
ATOM   723   C  CA  . LYS   A  1  98  ? 63.353  -111.894 39.079  1.00 90.41  ? 98  LYS   A CA  1 
ATOM   724   C  C   . LYS   A  1  98  ? 62.583  -113.204 38.859  1.00 88.90  ? 98  LYS   A C   1 
ATOM   725   O  O   . LYS   A  1  98  ? 63.236  -114.221 38.540  1.00 86.49  ? 98  LYS   A O   1 
ATOM   726   C  CB  . LYS   A  1  98  ? 63.582  -111.662 40.576  1.00 92.38  ? 98  LYS   A CB  1 
ATOM   727   C  CG  . LYS   A  1  98  ? 64.652  -112.570 41.171  1.00 94.65  ? 98  LYS   A CG  1 
ATOM   728   C  CD  . LYS   A  1  98  ? 64.839  -112.458 42.665  1.00 97.26  ? 98  LYS   A CD  1 
ATOM   729   C  CE  . LYS   A  1  98  ? 66.011  -113.284 43.155  1.00 101.40 ? 98  LYS   A CE  1 
ATOM   730   N  NZ  . LYS   A  1  98  ? 65.650  -114.116 44.328  1.00 107.38 ? 98  LYS   A NZ  1 
ATOM   731   N  N   . ARG   A  1  99  ? 61.254  -113.178 39.000  1.00 86.91  ? 99  ARG   A N   1 
ATOM   732   C  CA  . ARG   A  1  99  ? 60.378  -114.370 38.841  1.00 87.59  ? 99  ARG   A CA  1 
ATOM   733   C  C   . ARG   A  1  99  ? 60.378  -114.844 37.377  1.00 89.50  ? 99  ARG   A C   1 
ATOM   734   O  O   . ARG   A  1  99  ? 59.864  -115.960 37.124  1.00 89.19  ? 99  ARG   A O   1 
ATOM   735   C  CB  . ARG   A  1  99  ? 58.964  -114.067 39.351  1.00 88.15  ? 99  ARG   A CB  1 
ATOM   736   C  CG  . ARG   A  1  99  ? 58.865  -113.986 40.867  1.00 87.76  ? 99  ARG   A CG  1 
ATOM   737   C  CD  . ARG   A  1  99  ? 57.466  -113.681 41.367  1.00 88.03  ? 99  ARG   A CD  1 
ATOM   738   N  NE  . ARG   A  1  99  ? 57.478  -113.318 42.777  1.00 89.67  ? 99  ARG   A NE  1 
ATOM   739   C  CZ  . ARG   A  1  99  ? 56.399  -113.086 43.521  1.00 93.64  ? 99  ARG   A CZ  1 
ATOM   740   N  NH1 . ARG   A  1  99  ? 55.185  -113.181 43.001  1.00 93.14  ? 99  ARG   A NH1 1 
ATOM   741   N  NH2 . ARG   A  1  99  ? 56.541  -112.759 44.794  1.00 96.72  ? 99  ARG   A NH2 1 
ATOM   742   N  N   . ILE   A  1  100 ? 60.935  -114.050 36.451  1.00 87.08  ? 100 ILE   A N   1 
ATOM   743   C  CA  . ILE   A  1  100 ? 61.018  -114.391 34.998  1.00 89.00  ? 100 ILE   A CA  1 
ATOM   744   C  C   . ILE   A  1  100 ? 62.447  -114.813 34.625  1.00 88.96  ? 100 ILE   A C   1 
ATOM   745   O  O   . ILE   A  1  100 ? 62.577  -115.824 33.915  1.00 90.44  ? 100 ILE   A O   1 
ATOM   746   C  CB  . ILE   A  1  100 ? 60.526  -113.224 34.119  1.00 87.59  ? 100 ILE   A CB  1 
ATOM   747   C  CG1 . ILE   A  1  100 ? 59.055  -112.894 34.388  1.00 88.91  ? 100 ILE   A CG1 1 
ATOM   748   C  CG2 . ILE   A  1  100 ? 60.768  -113.524 32.647  1.00 89.91  ? 100 ILE   A CG2 1 
ATOM   749   C  CD1 . ILE   A  1  100 ? 58.607  -111.566 33.823  1.00 89.96  ? 100 ILE   A CD1 1 
ATOM   750   N  N   . TYR   A  1  101 ? 63.474  -114.064 35.043  1.00 87.82  ? 101 TYR   A N   1 
ATOM   751   C  CA  . TYR   A  1  101 ? 64.875  -114.236 34.564  1.00 91.74  ? 101 TYR   A CA  1 
ATOM   752   C  C   . TYR   A  1  101 ? 65.800  -114.809 35.644  1.00 91.99  ? 101 TYR   A C   1 
ATOM   753   O  O   . TYR   A  1  101 ? 66.989  -115.030 35.327  1.00 89.62  ? 101 TYR   A O   1 
ATOM   754   C  CB  . TYR   A  1  101 ? 65.454  -112.906 34.082  1.00 93.20  ? 101 TYR   A CB  1 
ATOM   755   C  CG  . TYR   A  1  101 ? 64.705  -112.285 32.933  1.00 97.52  ? 101 TYR   A CG  1 
ATOM   756   C  CD1 . TYR   A  1  101 ? 64.755  -112.843 31.666  1.00 97.79  ? 101 TYR   A CD1 1 
ATOM   757   C  CD2 . TYR   A  1  101 ? 63.945  -111.140 33.112  1.00 97.79  ? 101 TYR   A CD2 1 
ATOM   758   C  CE1 . TYR   A  1  101 ? 64.068  -112.281 30.603  1.00 98.75  ? 101 TYR   A CE1 1 
ATOM   759   C  CE2 . TYR   A  1  101 ? 63.251  -110.565 32.060  1.00 99.40  ? 101 TYR   A CE2 1 
ATOM   760   C  CZ  . TYR   A  1  101 ? 63.312  -111.140 30.802  1.00 99.55  ? 101 TYR   A CZ  1 
ATOM   761   O  OH  . TYR   A  1  101 ? 62.633  -110.590 29.754  1.00 103.05 ? 101 TYR   A OH  1 
ATOM   762   N  N   . GLY   A  1  102 ? 65.302  -115.017 36.867  1.00 94.41  ? 102 GLY   A N   1 
ATOM   763   C  CA  . GLY   A  1  102 ? 66.067  -115.639 37.967  1.00 98.78  ? 102 GLY   A CA  1 
ATOM   764   C  C   . GLY   A  1  102 ? 67.267  -114.802 38.382  1.00 99.64  ? 102 GLY   A C   1 
ATOM   765   O  O   . GLY   A  1  102 ? 68.223  -115.377 38.933  1.00 102.85 ? 102 GLY   A O   1 
ATOM   766   N  N   . GLU   A  1  103 ? 67.224  -113.492 38.122  1.00 100.72 ? 103 GLU   A N   1 
ATOM   767   C  CA  . GLU   A  1  103 ? 68.265  -112.514 38.538  1.00 99.84  ? 103 GLU   A CA  1 
ATOM   768   C  C   . GLU   A  1  103 ? 67.599  -111.147 38.725  1.00 97.73  ? 103 GLU   A C   1 
ATOM   769   O  O   . GLU   A  1  103 ? 66.471  -110.969 38.232  1.00 97.56  ? 103 GLU   A O   1 
ATOM   770   C  CB  . GLU   A  1  103 ? 69.407  -112.469 37.519  1.00 102.81 ? 103 GLU   A CB  1 
ATOM   771   C  CG  . GLU   A  1  103 ? 68.995  -111.963 36.146  1.00 104.00 ? 103 GLU   A CG  1 
ATOM   772   C  CD  . GLU   A  1  103 ? 69.911  -112.387 35.009  1.00 107.26 ? 103 GLU   A CD  1 
ATOM   773   O  OE1 . GLU   A  1  103 ? 69.921  -113.592 34.671  1.00 110.29 ? 103 GLU   A OE1 1 
ATOM   774   O  OE2 . GLU   A  1  103 ? 70.613  -111.512 34.461  1.00 105.85 ? 103 GLU   A OE2 1 
ATOM   775   N  N   . TYR   A  1  104 ? 68.268  -110.229 39.427  1.00 94.87  ? 104 TYR   A N   1 
ATOM   776   C  CA  . TYR   A  1  104 ? 67.731  -108.886 39.765  1.00 92.26  ? 104 TYR   A CA  1 
ATOM   777   C  C   . TYR   A  1  104 ? 67.821  -107.982 38.541  1.00 89.88  ? 104 TYR   A C   1 
ATOM   778   O  O   . TYR   A  1  104 ? 68.729  -108.118 37.725  1.00 89.76  ? 104 TYR   A O   1 
ATOM   779   C  CB  . TYR   A  1  104 ? 68.462  -108.300 40.974  1.00 91.89  ? 104 TYR   A CB  1 
ATOM   780   C  CG  . TYR   A  1  104 ? 68.116  -108.995 42.262  1.00 90.95  ? 104 TYR   A CG  1 
ATOM   781   C  CD1 . TYR   A  1  104 ? 66.918  -108.739 42.912  1.00 90.59  ? 104 TYR   A CD1 1 
ATOM   782   C  CD2 . TYR   A  1  104 ? 68.967  -109.938 42.812  1.00 92.44  ? 104 TYR   A CD2 1 
ATOM   783   C  CE1 . TYR   A  1  104 ? 66.583  -109.389 44.088  1.00 92.23  ? 104 TYR   A CE1 1 
ATOM   784   C  CE2 . TYR   A  1  104 ? 68.649  -110.596 43.987  1.00 94.62  ? 104 TYR   A CE2 1 
ATOM   785   C  CZ  . TYR   A  1  104 ? 67.454  -110.321 44.628  1.00 94.44  ? 104 TYR   A CZ  1 
ATOM   786   O  OH  . TYR   A  1  104 ? 67.151  -110.979 45.784  1.00 96.03  ? 104 TYR   A OH  1 
ATOM   787   N  N   . PRO   A  1  105 ? 66.882  -107.023 38.387  1.00 90.61  ? 105 PRO   A N   1 
ATOM   788   C  CA  . PRO   A  1  105 ? 66.877  -106.129 37.230  1.00 90.55  ? 105 PRO   A CA  1 
ATOM   789   C  C   . PRO   A  1  105 ? 68.066  -105.176 37.256  1.00 91.00  ? 105 PRO   A C   1 
ATOM   790   O  O   . PRO   A  1  105 ? 68.542  -104.822 38.333  1.00 88.02  ? 105 PRO   A O   1 
ATOM   791   C  CB  . PRO   A  1  105 ? 65.557  -105.358 37.387  1.00 89.61  ? 105 PRO   A CB  1 
ATOM   792   C  CG  . PRO   A  1  105 ? 65.315  -105.360 38.881  1.00 88.69  ? 105 PRO   A CG  1 
ATOM   793   C  CD  . PRO   A  1  105 ? 65.798  -106.721 39.336  1.00 89.61  ? 105 PRO   A CD  1 
ATOM   794   N  N   . PRO   A  1  106 ? 68.591  -104.746 36.085  1.00 92.97  ? 106 PRO   A N   1 
ATOM   795   C  CA  . PRO   A  1  106 ? 69.579  -103.669 36.043  1.00 94.85  ? 106 PRO   A CA  1 
ATOM   796   C  C   . PRO   A  1  106 ? 68.923  -102.338 36.442  1.00 96.35  ? 106 PRO   A C   1 
ATOM   797   O  O   . PRO   A  1  106 ? 67.727  -102.191 36.235  1.00 98.56  ? 106 PRO   A O   1 
ATOM   798   C  CB  . PRO   A  1  106 ? 70.063  -103.664 34.586  1.00 95.40  ? 106 PRO   A CB  1 
ATOM   799   C  CG  . PRO   A  1  106 ? 68.908  -104.261 33.808  1.00 94.75  ? 106 PRO   A CG  1 
ATOM   800   C  CD  . PRO   A  1  106 ? 68.275  -105.268 34.747  1.00 93.42  ? 106 PRO   A CD  1 
ATOM   801   N  N   . THR   A  1  107 ? 69.711  -101.418 37.007  1.00 97.79  ? 107 THR   A N   1 
ATOM   802   C  CA  . THR   A  1  107 ? 69.243  -100.144 37.617  1.00 96.59  ? 107 THR   A CA  1 
ATOM   803   C  C   . THR   A  1  107 ? 68.261  -99.437  36.672  1.00 95.49  ? 107 THR   A C   1 
ATOM   804   O  O   . THR   A  1  107 ? 67.142  -99.126  37.120  1.00 99.41  ? 107 THR   A O   1 
ATOM   805   C  CB  . THR   A  1  107 ? 70.423  -99.234  37.979  1.00 95.80  ? 107 THR   A CB  1 
ATOM   806   O  OG1 . THR   A  1  107 ? 71.328  -99.964  38.808  1.00 98.17  ? 107 THR   A OG1 1 
ATOM   807   C  CG2 . THR   A  1  107 ? 69.981  -97.968  38.681  1.00 95.54  ? 107 THR   A CG2 1 
ATOM   808   N  N   . LYS   A  1  108 ? 68.660  -99.210  35.416  1.00 96.48  ? 108 LYS   A N   1 
ATOM   809   C  CA  . LYS   A  1  108 ? 67.892  -98.408  34.422  1.00 97.56  ? 108 LYS   A CA  1 
ATOM   810   C  C   . LYS   A  1  108 ? 66.470  -98.966  34.261  1.00 95.52  ? 108 LYS   A C   1 
ATOM   811   O  O   . LYS   A  1  108 ? 65.541  -98.155  34.078  1.00 92.26  ? 108 LYS   A O   1 
ATOM   812   C  CB  . LYS   A  1  108 ? 68.626  -98.370  33.077  1.00 103.00 ? 108 LYS   A CB  1 
ATOM   813   C  CG  . LYS   A  1  108 ? 68.703  -99.698  32.336  1.00 106.46 ? 108 LYS   A CG  1 
ATOM   814   C  CD  . LYS   A  1  108 ? 69.600  -99.657  31.120  1.00 112.96 ? 108 LYS   A CD  1 
ATOM   815   C  CE  . LYS   A  1  108 ? 69.967  -101.034 30.610  1.00 117.37 ? 108 LYS   A CE  1 
ATOM   816   N  NZ  . LYS   A  1  108 ? 70.683  -100.963 29.314  1.00 121.49 ? 108 LYS   A NZ  1 
ATOM   817   N  N   . LEU   A  1  109 ? 66.300  -100.291 34.323  1.00 95.17  ? 109 LEU   A N   1 
ATOM   818   C  CA  . LEU   A  1  109 ? 64.991  -100.965 34.097  1.00 94.27  ? 109 LEU   A CA  1 
ATOM   819   C  C   . LEU   A  1  109 ? 64.120  -100.862 35.353  1.00 89.60  ? 109 LEU   A C   1 
ATOM   820   O  O   . LEU   A  1  109 ? 62.929  -100.544 35.195  1.00 86.85  ? 109 LEU   A O   1 
ATOM   821   C  CB  . LEU   A  1  109 ? 65.206  -102.426 33.687  1.00 94.95  ? 109 LEU   A CB  1 
ATOM   822   C  CG  . LEU   A  1  109 ? 65.654  -102.648 32.243  1.00 98.12  ? 109 LEU   A CG  1 
ATOM   823   C  CD1 . LEU   A  1  109 ? 65.761  -104.132 31.937  1.00 99.88  ? 109 LEU   A CD1 1 
ATOM   824   C  CD2 . LEU   A  1  109 ? 64.705  -101.979 31.258  1.00 100.07 ? 109 LEU   A CD2 1 
ATOM   825   N  N   . LEU   A  1  110 ? 64.667  -101.127 36.545  1.00 88.09  ? 110 LEU   A N   1 
ATOM   826   C  CA  . LEU   A  1  110 ? 63.911  -100.948 37.815  1.00 88.83  ? 110 LEU   A CA  1 
ATOM   827   C  C   . LEU   A  1  110 ? 63.441  -99.490  37.877  1.00 88.58  ? 110 LEU   A C   1 
ATOM   828   O  O   . LEU   A  1  110 ? 62.237  -99.268  38.117  1.00 88.42  ? 110 LEU   A O   1 
ATOM   829   C  CB  . LEU   A  1  110 ? 64.772  -101.310 39.032  1.00 87.53  ? 110 LEU   A CB  1 
ATOM   830   C  CG  . LEU   A  1  110 ? 64.091  -101.103 40.388  1.00 87.99  ? 110 LEU   A CG  1 
ATOM   831   C  CD1 . LEU   A  1  110 ? 62.779  -101.870 40.473  1.00 87.96  ? 110 LEU   A CD1 1 
ATOM   832   C  CD2 . LEU   A  1  110 ? 65.008  -101.504 41.533  1.00 88.97  ? 110 LEU   A CD2 1 
ATOM   833   N  N   . VAL   A  1  111 ? 64.359  -98.550  37.625  1.00 90.61  ? 111 VAL   A N   1 
ATOM   834   C  CA  . VAL   A  1  111 ? 64.080  -97.085  37.545  1.00 88.75  ? 111 VAL   A CA  1 
ATOM   835   C  C   . VAL   A  1  111 ? 62.915  -96.868  36.573  1.00 87.14  ? 111 VAL   A C   1 
ATOM   836   O  O   . VAL   A  1  111 ? 61.992  -96.113  36.929  1.00 88.72  ? 111 VAL   A O   1 
ATOM   837   C  CB  . VAL   A  1  111 ? 65.334  -96.287  37.131  1.00 90.16  ? 111 VAL   A CB  1 
ATOM   838   C  CG1 . VAL   A  1  111 ? 64.993  -94.881  36.659  1.00 89.51  ? 111 VAL   A CG1 1 
ATOM   839   C  CG2 . VAL   A  1  111 ? 66.358  -96.227  38.255  1.00 91.44  ? 111 VAL   A CG2 1 
ATOM   840   N  N   . SER   A  1  112 ? 62.957  -97.515  35.403  1.00 87.17  ? 112 SER   A N   1 
ATOM   841   C  CA  . SER   A  1  112 ? 61.908  -97.439  34.351  1.00 88.19  ? 112 SER   A CA  1 
ATOM   842   C  C   . SER   A  1  112 ? 60.546  -97.869  34.914  1.00 85.34  ? 112 SER   A C   1 
ATOM   843   O  O   . SER   A  1  112 ? 59.545  -97.202  34.596  1.00 82.52  ? 112 SER   A O   1 
ATOM   844   C  CB  . SER   A  1  112 ? 62.276  -98.260  33.144  1.00 90.49  ? 112 SER   A CB  1 
ATOM   845   O  OG  . SER   A  1  112 ? 61.205  -98.283  32.214  1.00 94.44  ? 112 SER   A OG  1 
ATOM   846   N  N   . GLU   A  1  113 ? 60.510  -98.946  35.707  1.00 86.91  ? 113 GLU   A N   1 
ATOM   847   C  CA  . GLU   A  1  113 ? 59.262  -99.523  36.280  1.00 88.57  ? 113 GLU   A CA  1 
ATOM   848   C  C   . GLU   A  1  113 ? 58.686  -98.576  37.337  1.00 86.40  ? 113 GLU   A C   1 
ATOM   849   O  O   . GLU   A  1  113 ? 57.447  -98.495  37.429  1.00 84.96  ? 113 GLU   A O   1 
ATOM   850   C  CB  . GLU   A  1  113 ? 59.515  -100.895 36.908  1.00 90.57  ? 113 GLU   A CB  1 
ATOM   851   C  CG  . GLU   A  1  113 ? 59.927  -101.967 35.912  1.00 92.77  ? 113 GLU   A CG  1 
ATOM   852   C  CD  . GLU   A  1  113 ? 58.848  -102.426 34.945  1.00 91.50  ? 113 GLU   A CD  1 
ATOM   853   O  OE1 . GLU   A  1  113 ? 57.683  -102.000 35.095  1.00 94.11  ? 113 GLU   A OE1 1 
ATOM   854   O  OE2 . GLU   A  1  113 ? 59.176  -103.212 34.038  1.00 91.65  ? 113 GLU   A OE2 1 
ATOM   855   N  N   . VAL   A  1  114 ? 59.546  -97.909  38.116  1.00 88.74  ? 114 VAL   A N   1 
ATOM   856   C  CA  . VAL   A  1  114 ? 59.127  -96.932  39.167  1.00 90.33  ? 114 VAL   A CA  1 
ATOM   857   C  C   . VAL   A  1  114 ? 58.530  -95.715  38.458  1.00 89.66  ? 114 VAL   A C   1 
ATOM   858   O  O   . VAL   A  1  114 ? 57.454  -95.255  38.881  1.00 92.08  ? 114 VAL   A O   1 
ATOM   859   C  CB  . VAL   A  1  114 ? 60.283  -96.516  40.101  1.00 92.70  ? 114 VAL   A CB  1 
ATOM   860   C  CG1 . VAL   A  1  114 ? 59.781  -95.645  41.243  1.00 93.66  ? 114 VAL   A CG1 1 
ATOM   861   C  CG2 . VAL   A  1  114 ? 61.041  -97.711  40.656  1.00 93.36  ? 114 VAL   A CG2 1 
ATOM   862   N  N   . ALA   A  1  115 ? 59.212  -95.234  37.413  1.00 90.07  ? 115 ALA   A N   1 
ATOM   863   C  CA  . ALA   A  1  115 ? 58.800  -94.091  36.564  1.00 87.97  ? 115 ALA   A CA  1 
ATOM   864   C  C   . ALA   A  1  115 ? 57.411  -94.357  35.971  1.00 88.22  ? 115 ALA   A C   1 
ATOM   865   O  O   . ALA   A  1  115 ? 56.618  -93.402  35.895  1.00 86.21  ? 115 ALA   A O   1 
ATOM   866   C  CB  . ALA   A  1  115 ? 59.827  -93.856  35.484  1.00 86.40  ? 115 ALA   A CB  1 
ATOM   867   N  N   . LYS   A  1  116 ? 57.134  -95.607  35.580  1.00 89.58  ? 116 LYS   A N   1 
ATOM   868   C  CA  . LYS   A  1  116 ? 55.824  -96.041  35.020  1.00 90.17  ? 116 LYS   A CA  1 
ATOM   869   C  C   . LYS   A  1  116 ? 54.734  -95.887  36.087  1.00 87.09  ? 116 LYS   A C   1 
ATOM   870   O  O   . LYS   A  1  116 ? 53.650  -95.376  35.746  1.00 82.57  ? 116 LYS   A O   1 
ATOM   871   C  CB  . LYS   A  1  116 ? 55.874  -97.495  34.539  1.00 91.80  ? 116 LYS   A CB  1 
ATOM   872   C  CG  . LYS   A  1  116 ? 54.627  -97.967  33.802  1.00 96.19  ? 116 LYS   A CG  1 
ATOM   873   C  CD  . LYS   A  1  116 ? 54.653  -99.435  33.439  1.00 98.13  ? 116 LYS   A CD  1 
ATOM   874   C  CE  . LYS   A  1  116 ? 53.573  -99.825  32.452  1.00 103.84 ? 116 LYS   A CE  1 
ATOM   875   N  NZ  . LYS   A  1  116 ? 52.492  -100.608 33.098  1.00 108.25 ? 116 LYS   A NZ  1 
ATOM   876   N  N   . ILE   A  1  117 ? 55.010  -96.339  37.316  1.00 87.52  ? 117 ILE   A N   1 
ATOM   877   C  CA  . ILE   A  1  117 ? 54.061  -96.294  38.471  1.00 88.12  ? 117 ILE   A CA  1 
ATOM   878   C  C   . ILE   A  1  117 ? 53.713  -94.829  38.766  1.00 87.37  ? 117 ILE   A C   1 
ATOM   879   O  O   . ILE   A  1  117 ? 52.531  -94.550  39.071  1.00 85.80  ? 117 ILE   A O   1 
ATOM   880   C  CB  . ILE   A  1  117 ? 54.645  -97.017  39.706  1.00 88.34  ? 117 ILE   A CB  1 
ATOM   881   C  CG1 . ILE   A  1  117 ? 54.727  -98.530  39.480  1.00 88.60  ? 117 ILE   A CG1 1 
ATOM   882   C  CG2 . ILE   A  1  117 ? 53.850  -96.683  40.962  1.00 88.06  ? 117 ILE   A CG2 1 
ATOM   883   C  CD1 . ILE   A  1  117 ? 55.488  -99.279  40.550  1.00 89.56  ? 117 ILE   A CD1 1 
ATOM   884   N  N   . MET   A  1  118 ? 54.704  -93.937  38.674  1.00 87.37  ? 118 MET   A N   1 
ATOM   885   C  CA  . MET   A  1  118 ? 54.551  -92.487  38.967  1.00 87.62  ? 118 MET   A CA  1 
ATOM   886   C  C   . MET   A  1  118 ? 53.843  -91.794  37.795  1.00 84.15  ? 118 MET   A C   1 
ATOM   887   O  O   . MET   A  1  118 ? 53.040  -90.879  38.063  1.00 85.16  ? 118 MET   A O   1 
ATOM   888   C  CB  . MET   A  1  118 ? 55.911  -91.836  39.246  1.00 89.11  ? 118 MET   A CB  1 
ATOM   889   C  CG  . MET   A  1  118 ? 56.459  -92.198  40.615  1.00 90.20  ? 118 MET   A CG  1 
ATOM   890   S  SD  . MET   A  1  118 ? 58.199  -91.764  40.824  1.00 93.25  ? 118 MET   A SD  1 
ATOM   891   C  CE  . MET   A  1  118 ? 58.063  -90.029  41.249  1.00 93.60  ? 118 MET   A CE  1 
ATOM   892   N  N   . GLN   A  1  119 ? 54.106  -92.220  36.555  1.00 82.04  ? 119 GLN   A N   1 
ATOM   893   C  CA  . GLN   A  1  119 ? 53.430  -91.693  35.339  1.00 83.13  ? 119 GLN   A CA  1 
ATOM   894   C  C   . GLN   A  1  119 ? 51.926  -91.976  35.426  1.00 85.21  ? 119 GLN   A C   1 
ATOM   895   O  O   . GLN   A  1  119 ? 51.143  -91.106  35.020  1.00 85.58  ? 119 GLN   A O   1 
ATOM   896   C  CB  . GLN   A  1  119 ? 53.997  -92.312  34.060  1.00 83.91  ? 119 GLN   A CB  1 
ATOM   897   C  CG  . GLN   A  1  119 ? 53.485  -91.651  32.784  1.00 85.32  ? 119 GLN   A CG  1 
ATOM   898   C  CD  . GLN   A  1  119 ? 52.104  -92.100  32.366  1.00 86.48  ? 119 GLN   A CD  1 
ATOM   899   O  OE1 . GLN   A  1  119 ? 51.679  -93.218  32.644  1.00 89.95  ? 119 GLN   A OE1 1 
ATOM   900   N  NE2 . GLN   A  1  119 ? 51.388  -91.229  31.672  1.00 86.41  ? 119 GLN   A NE2 1 
ATOM   901   N  N   . GLU   A  1  120 ? 51.540  -93.162  35.902  1.00 86.85  ? 120 GLU   A N   1 
ATOM   902   C  CA  . GLU   A  1  120 ? 50.122  -93.614  35.932  1.00 88.38  ? 120 GLU   A CA  1 
ATOM   903   C  C   . GLU   A  1  120 ? 49.334  -92.761  36.938  1.00 86.11  ? 120 GLU   A C   1 
ATOM   904   O  O   . GLU   A  1  120 ? 48.156  -92.464  36.654  1.00 80.19  ? 120 GLU   A O   1 
ATOM   905   C  CB  . GLU   A  1  120 ? 50.052  -95.118  36.210  1.00 92.33  ? 120 GLU   A CB  1 
ATOM   906   C  CG  . GLU   A  1  120 ? 50.470  -95.956  35.011  1.00 99.30  ? 120 GLU   A CG  1 
ATOM   907   C  CD  . GLU   A  1  120 ? 50.514  -97.460  35.231  1.00 107.98 ? 120 GLU   A CD  1 
ATOM   908   O  OE1 . GLU   A  1  120 ? 50.946  -98.180  34.301  1.00 115.38 ? 120 GLU   A OE1 1 
ATOM   909   O  OE2 . GLU   A  1  120 ? 50.115  -97.914  36.326  1.00 118.83 ? 120 GLU   A OE2 1 
ATOM   910   N  N   . ALA   A  1  121 ? 49.971  -92.334  38.036  1.00 87.53  ? 121 ALA   A N   1 
ATOM   911   C  CA  . ALA   A  1  121 ? 49.375  -91.460  39.077  1.00 88.74  ? 121 ALA   A CA  1 
ATOM   912   C  C   . ALA   A  1  121 ? 49.112  -90.065  38.499  1.00 89.79  ? 121 ALA   A C   1 
ATOM   913   O  O   . ALA   A  1  121 ? 48.425  -89.260  39.164  1.00 95.58  ? 121 ALA   A O   1 
ATOM   914   C  CB  . ALA   A  1  121 ? 50.283  -91.394  40.282  1.00 88.86  ? 121 ALA   A CB  1 
ATOM   915   N  N   . THR   A  1  122 ? 49.636  -89.806  37.297  1.00 90.03  ? 122 THR   A N   1 
ATOM   916   C  CA  . THR   A  1  122 ? 49.553  -88.517  36.562  1.00 90.34  ? 122 THR   A CA  1 
ATOM   917   C  C   . THR   A  1  122 ? 48.364  -88.546  35.591  1.00 91.38  ? 122 THR   A C   1 
ATOM   918   O  O   . THR   A  1  122 ? 47.865  -87.464  35.265  1.00 93.31  ? 122 THR   A O   1 
ATOM   919   C  CB  . THR   A  1  122 ? 50.896  -88.243  35.870  1.00 87.30  ? 122 THR   A CB  1 
ATOM   920   O  OG1 . THR   A  1  122 ? 51.776  -87.689  36.847  1.00 86.54  ? 122 THR   A OG1 1 
ATOM   921   C  CG2 . THR   A  1  122 ? 50.783  -87.324  34.677  1.00 88.10  ? 122 THR   A CG2 1 
ATOM   922   N  N   . GLN   A  1  123 ? 47.923  -89.731  35.153  1.00 91.35  ? 123 GLN   A N   1 
ATOM   923   C  CA  . GLN   A  1  123 ? 46.927  -89.889  34.056  1.00 91.26  ? 123 GLN   A CA  1 
ATOM   924   C  C   . GLN   A  1  123 ? 45.685  -90.675  34.511  1.00 91.55  ? 123 GLN   A C   1 
ATOM   925   O  O   . GLN   A  1  123 ? 44.594  -90.356  33.999  1.00 94.29  ? 123 GLN   A O   1 
ATOM   926   C  CB  . GLN   A  1  123 ? 47.582  -90.571  32.855  1.00 91.91  ? 123 GLN   A CB  1 
ATOM   927   C  CG  . GLN   A  1  123 ? 46.756  -90.470  31.580  1.00 90.83  ? 123 GLN   A CG  1 
ATOM   928   C  CD  . GLN   A  1  123 ? 47.547  -90.829  30.346  1.00 92.14  ? 123 GLN   A CD  1 
ATOM   929   O  OE1 . GLN   A  1  123 ? 48.591  -91.474  30.418  1.00 95.01  ? 123 GLN   A OE1 1 
ATOM   930   N  NE2 . GLN   A  1  123 ? 47.050  -90.411  29.193  1.00 91.37  ? 123 GLN   A NE2 1 
ATOM   931   N  N   . SER   A  1  124 ? 45.826  -91.666  35.403  1.00 88.14  ? 124 SER   A N   1 
ATOM   932   C  CA  . SER   A  1  124 ? 44.730  -92.585  35.820  1.00 88.93  ? 124 SER   A CA  1 
ATOM   933   C  C   . SER   A  1  124 ? 43.605  -91.810  36.513  1.00 87.51  ? 124 SER   A C   1 
ATOM   934   O  O   . SER   A  1  124 ? 43.826  -90.647  36.906  1.00 89.11  ? 124 SER   A O   1 
ATOM   935   C  CB  . SER   A  1  124 ? 45.229  -93.683  36.714  1.00 88.61  ? 124 SER   A CB  1 
ATOM   936   O  OG  . SER   A  1  124 ? 46.389  -94.285  36.170  1.00 96.66  ? 124 SER   A OG  1 
ATOM   937   N  N   . GLY   A  1  125 ? 42.448  -92.455  36.667  1.00 84.96  ? 125 GLY   A N   1 
ATOM   938   C  CA  . GLY   A  1  125 ? 41.239  -91.869  37.273  1.00 83.82  ? 125 GLY   A CA  1 
ATOM   939   C  C   . GLY   A  1  125 ? 41.382  -91.714  38.775  1.00 85.72  ? 125 GLY   A C   1 
ATOM   940   O  O   . GLY   A  1  125 ? 41.855  -92.671  39.421  1.00 88.21  ? 125 GLY   A O   1 
ATOM   941   N  N   . GLY   A  1  126 ? 41.014  -90.540  39.300  1.00 87.03  ? 126 GLY   A N   1 
ATOM   942   C  CA  . GLY   A  1  126 ? 40.780  -90.278  40.735  1.00 86.52  ? 126 GLY   A CA  1 
ATOM   943   C  C   . GLY   A  1  126 ? 42.021  -90.435  41.599  1.00 85.20  ? 126 GLY   A C   1 
ATOM   944   O  O   . GLY   A  1  126 ? 41.877  -90.938  42.735  1.00 84.66  ? 126 GLY   A O   1 
ATOM   945   N  N   . VAL   A  1  127 ? 43.190  -90.011  41.107  1.00 84.83  ? 127 VAL   A N   1 
ATOM   946   C  CA  . VAL   A  1  127 ? 44.455  -89.970  41.901  1.00 85.84  ? 127 VAL   A CA  1 
ATOM   947   C  C   . VAL   A  1  127 ? 45.224  -88.677  41.600  1.00 88.13  ? 127 VAL   A C   1 
ATOM   948   O  O   . VAL   A  1  127 ? 45.202  -88.204  40.435  1.00 88.24  ? 127 VAL   A O   1 
ATOM   949   C  CB  . VAL   A  1  127 ? 45.337  -91.205  41.647  1.00 85.20  ? 127 VAL   A CB  1 
ATOM   950   C  CG1 . VAL   A  1  127 ? 44.754  -92.450  42.297  1.00 86.58  ? 127 VAL   A CG1 1 
ATOM   951   C  CG2 . VAL   A  1  127 ? 45.589  -91.432  40.165  1.00 83.68  ? 127 VAL   A CG2 1 
ATOM   952   N  N   . ARG   A  1  128 ? 45.877  -88.134  42.631  1.00 84.80  ? 128 ARG   A N   1 
ATOM   953   C  CA  . ARG   A  1  128 ? 46.904  -87.071  42.502  1.00 82.36  ? 128 ARG   A CA  1 
ATOM   954   C  C   . ARG   A  1  128 ? 48.244  -87.730  42.192  1.00 80.35  ? 128 ARG   A C   1 
ATOM   955   O  O   . ARG   A  1  128 ? 48.466  -88.883  42.549  1.00 77.37  ? 128 ARG   A O   1 
ATOM   956   C  CB  . ARG   A  1  128 ? 46.996  -86.241  43.787  1.00 83.06  ? 128 ARG   A CB  1 
ATOM   957   C  CG  . ARG   A  1  128 ? 47.522  -87.006  44.994  1.00 83.34  ? 128 ARG   A CG  1 
ATOM   958   C  CD  . ARG   A  1  128 ? 47.973  -86.098  46.118  1.00 85.13  ? 128 ARG   A CD  1 
ATOM   959   N  NE  . ARG   A  1  128 ? 48.270  -86.869  47.319  1.00 86.52  ? 128 ARG   A NE  1 
ATOM   960   C  CZ  . ARG   A  1  128 ? 49.404  -87.535  47.548  1.00 88.87  ? 128 ARG   A CZ  1 
ATOM   961   N  NH1 . ARG   A  1  128 ? 50.383  -87.534  46.656  1.00 88.11  ? 128 ARG   A NH1 1 
ATOM   962   N  NH2 . ARG   A  1  128 ? 49.551  -88.204  48.680  1.00 89.01  ? 128 ARG   A NH2 1 
ATOM   963   N  N   . PRO   A  1  129 ? 49.176  -87.025  41.515  1.00 82.06  ? 129 PRO   A N   1 
ATOM   964   C  CA  . PRO   A  1  129 ? 50.548  -87.506  41.358  1.00 83.17  ? 129 PRO   A CA  1 
ATOM   965   C  C   . PRO   A  1  129 ? 51.253  -87.702  42.706  1.00 83.46  ? 129 PRO   A C   1 
ATOM   966   O  O   . PRO   A  1  129 ? 50.805  -87.136  43.684  1.00 85.01  ? 129 PRO   A O   1 
ATOM   967   C  CB  . PRO   A  1  129 ? 51.249  -86.381  40.584  1.00 84.60  ? 129 PRO   A CB  1 
ATOM   968   C  CG  . PRO   A  1  129 ? 50.123  -85.661  39.876  1.00 86.30  ? 129 PRO   A CG  1 
ATOM   969   C  CD  . PRO   A  1  129 ? 48.949  -85.746  40.829  1.00 84.78  ? 129 PRO   A CD  1 
ATOM   970   N  N   . PHE   A  1  130 ? 52.332  -88.488  42.719  1.00 86.04  ? 130 PHE   A N   1 
ATOM   971   C  CA  . PHE   A  1  130 ? 53.223  -88.666  43.897  1.00 86.64  ? 130 PHE   A CA  1 
ATOM   972   C  C   . PHE   A  1  130 ? 53.971  -87.354  44.157  1.00 85.11  ? 130 PHE   A C   1 
ATOM   973   O  O   . PHE   A  1  130 ? 54.400  -86.706  43.183  1.00 82.80  ? 130 PHE   A O   1 
ATOM   974   C  CB  . PHE   A  1  130 ? 54.203  -89.821  43.679  1.00 88.28  ? 130 PHE   A CB  1 
ATOM   975   C  CG  . PHE   A  1  130 ? 53.584  -91.193  43.728  1.00 88.14  ? 130 PHE   A CG  1 
ATOM   976   C  CD1 . PHE   A  1  130 ? 53.431  -91.862  44.933  1.00 88.83  ? 130 PHE   A CD1 1 
ATOM   977   C  CD2 . PHE   A  1  130 ? 53.159  -91.819  42.567  1.00 91.07  ? 130 PHE   A CD2 1 
ATOM   978   C  CE1 . PHE   A  1  130 ? 52.864  -93.127  44.973  1.00 88.01  ? 130 PHE   A CE1 1 
ATOM   979   C  CE2 . PHE   A  1  130 ? 52.592  -93.083  42.610  1.00 90.76  ? 130 PHE   A CE2 1 
ATOM   980   C  CZ  . PHE   A  1  130 ? 52.443  -93.734  43.813  1.00 89.40  ? 130 PHE   A CZ  1 
ATOM   981   N  N   . GLY   A  1  131 ? 54.123  -86.978  45.429  1.00 82.67  ? 131 GLY   A N   1 
ATOM   982   C  CA  . GLY   A  1  131 ? 54.769  -85.718  45.843  1.00 81.94  ? 131 GLY   A CA  1 
ATOM   983   C  C   . GLY   A  1  131 ? 56.222  -85.925  46.227  1.00 82.35  ? 131 GLY   A C   1 
ATOM   984   O  O   . GLY   A  1  131 ? 56.622  -85.411  47.295  1.00 80.71  ? 131 GLY   A O   1 
ATOM   985   N  N   . VAL   A  1  132 ? 56.990  -86.627  45.384  1.00 81.44  ? 132 VAL   A N   1 
ATOM   986   C  CA  . VAL   A  1  132 ? 58.412  -86.990  45.664  1.00 84.03  ? 132 VAL   A CA  1 
ATOM   987   C  C   . VAL   A  1  132 ? 59.236  -86.957  44.374  1.00 85.20  ? 132 VAL   A C   1 
ATOM   988   O  O   . VAL   A  1  132 ? 58.680  -87.260  43.301  1.00 86.23  ? 132 VAL   A O   1 
ATOM   989   C  CB  . VAL   A  1  132 ? 58.522  -88.372  46.336  1.00 83.61  ? 132 VAL   A CB  1 
ATOM   990   C  CG1 . VAL   A  1  132 ? 58.100  -88.318  47.792  1.00 84.32  ? 132 VAL   A CG1 1 
ATOM   991   C  CG2 . VAL   A  1  132 ? 57.735  -89.437  45.593  1.00 84.91  ? 132 VAL   A CG2 1 
ATOM   992   N  N   . SER   A  1  133 ? 60.517  -86.602  44.507  1.00 87.83  ? 133 SER   A N   1 
ATOM   993   C  CA  . SER   A  1  133 ? 61.601  -86.879  43.529  1.00 90.85  ? 133 SER   A CA  1 
ATOM   994   C  C   . SER   A  1  133 ? 62.534  -87.924  44.145  1.00 92.87  ? 133 SER   A C   1 
ATOM   995   O  O   . SER   A  1  133 ? 62.980  -87.706  45.287  1.00 94.95  ? 133 SER   A O   1 
ATOM   996   C  CB  . SER   A  1  133 ? 62.355  -85.630  43.151  1.00 92.08  ? 133 SER   A CB  1 
ATOM   997   O  OG  . SER   A  1  133 ? 61.658  -84.899  42.155  1.00 94.01  ? 133 SER   A OG  1 
ATOM   998   N  N   . LEU   A  1  134 ? 62.790  -89.021  43.428  1.00 94.71  ? 134 LEU   A N   1 
ATOM   999   C  CA  . LEU   A  1  134 ? 63.683  -90.118  43.881  1.00 93.95  ? 134 LEU   A CA  1 
ATOM   1000  C  C   . LEU   A  1  134 ? 65.076  -89.905  43.286  1.00 92.73  ? 134 LEU   A C   1 
ATOM   1001  O  O   . LEU   A  1  134 ? 65.158  -89.415  42.144  1.00 89.46  ? 134 LEU   A O   1 
ATOM   1002  C  CB  . LEU   A  1  134 ? 63.111  -91.465  43.429  1.00 95.57  ? 134 LEU   A CB  1 
ATOM   1003  C  CG  . LEU   A  1  134 ? 61.700  -91.798  43.912  1.00 96.30  ? 134 LEU   A CG  1 
ATOM   1004  C  CD1 . LEU   A  1  134 ? 61.229  -93.116  43.315  1.00 96.07  ? 134 LEU   A CD1 1 
ATOM   1005  C  CD2 . LEU   A  1  134 ? 61.639  -91.854  45.429  1.00 97.24  ? 134 LEU   A CD2 1 
ATOM   1006  N  N   . LEU   A  1  135 ? 66.115  -90.248  44.051  1.00 92.59  ? 135 LEU   A N   1 
ATOM   1007  C  CA  . LEU   A  1  135 ? 67.481  -90.536  43.541  1.00 93.73  ? 135 LEU   A CA  1 
ATOM   1008  C  C   . LEU   A  1  135 ? 67.762  -92.023  43.766  1.00 93.78  ? 135 LEU   A C   1 
ATOM   1009  O  O   . LEU   A  1  135 ? 67.837  -92.426  44.942  1.00 96.58  ? 135 LEU   A O   1 
ATOM   1010  C  CB  . LEU   A  1  135 ? 68.515  -89.676  44.274  1.00 94.49  ? 135 LEU   A CB  1 
ATOM   1011  C  CG  . LEU   A  1  135 ? 68.420  -88.166  44.062  1.00 96.10  ? 135 LEU   A CG  1 
ATOM   1012  C  CD1 . LEU   A  1  135 ? 69.497  -87.456  44.869  1.00 96.46  ? 135 LEU   A CD1 1 
ATOM   1013  C  CD2 . LEU   A  1  135 ? 68.530  -87.798  42.588  1.00 95.85  ? 135 LEU   A CD2 1 
ATOM   1014  N  N   . ILE   A  1  136 ? 67.886  -92.802  42.687  1.00 93.11  ? 136 ILE   A N   1 
ATOM   1015  C  CA  . ILE   A  1  136 ? 68.146  -94.272  42.738  1.00 91.84  ? 136 ILE   A CA  1 
ATOM   1016  C  C   . ILE   A  1  136 ? 69.573  -94.536  42.253  1.00 89.17  ? 136 ILE   A C   1 
ATOM   1017  O  O   . ILE   A  1  136 ? 69.859  -94.266  41.069  1.00 86.23  ? 136 ILE   A O   1 
ATOM   1018  C  CB  . ILE   A  1  136 ? 67.103  -95.056  41.918  1.00 92.17  ? 136 ILE   A CB  1 
ATOM   1019  C  CG1 . ILE   A  1  136 ? 65.681  -94.789  42.421  1.00 93.47  ? 136 ILE   A CG1 1 
ATOM   1020  C  CG2 . ILE   A  1  136 ? 67.427  -96.543  41.919  1.00 92.94  ? 136 ILE   A CG2 1 
ATOM   1021  C  CD1 . ILE   A  1  136 ? 64.599  -95.128  41.423  1.00 93.90  ? 136 ILE   A CD1 1 
ATOM   1022  N  N   . ALA   A  1  137 ? 70.422  -95.041  43.151  1.00 88.31  ? 137 ALA   A N   1 
ATOM   1023  C  CA  . ALA   A  1  137 ? 71.808  -95.483  42.878  1.00 91.15  ? 137 ALA   A CA  1 
ATOM   1024  C  C   . ALA   A  1  137 ? 71.820  -97.011  42.810  1.00 91.06  ? 137 ALA   A C   1 
ATOM   1025  O  O   . ALA   A  1  137 ? 71.104  -97.638  43.614  1.00 92.33  ? 137 ALA   A O   1 
ATOM   1026  C  CB  . ALA   A  1  137 ? 72.734  -94.974  43.953  1.00 91.86  ? 137 ALA   A CB  1 
ATOM   1027  N  N   . GLY   A  1  138 ? 72.593  -97.585  41.887  1.00 92.43  ? 138 GLY   A N   1 
ATOM   1028  C  CA  . GLY   A  1  138 ? 72.690  -99.048  41.742  1.00 94.31  ? 138 GLY   A CA  1 
ATOM   1029  C  C   . GLY   A  1  138 ? 73.832  -99.483  40.843  1.00 96.85  ? 138 GLY   A C   1 
ATOM   1030  O  O   . GLY   A  1  138 ? 74.444  -98.616  40.187  1.00 97.49  ? 138 GLY   A O   1 
ATOM   1031  N  N   . HIS   A  1  139 ? 74.102  -100.794 40.833  1.00 98.49  ? 139 HIS   A N   1 
ATOM   1032  C  CA  . HIS   A  1  139 ? 75.138  -101.465 40.007  1.00 100.47 ? 139 HIS   A CA  1 
ATOM   1033  C  C   . HIS   A  1  139 ? 74.526  -102.684 39.312  1.00 100.17 ? 139 HIS   A C   1 
ATOM   1034  O  O   . HIS   A  1  139 ? 73.595  -103.290 39.878  1.00 100.48 ? 139 HIS   A O   1 
ATOM   1035  C  CB  . HIS   A  1  139 ? 76.345  -101.875 40.863  1.00 100.08 ? 139 HIS   A CB  1 
ATOM   1036  C  CG  . HIS   A  1  139 ? 77.381  -102.640 40.107  1.00 101.22 ? 139 HIS   A CG  1 
ATOM   1037  N  ND1 . HIS   A  1  139 ? 77.351  -104.018 40.003  1.00 101.99 ? 139 HIS   A ND1 1 
ATOM   1038  C  CD2 . HIS   A  1  139 ? 78.460  -102.231 39.406  1.00 101.18 ? 139 HIS   A CD2 1 
ATOM   1039  C  CE1 . HIS   A  1  139 ? 78.373  -104.423 39.277  1.00 101.83 ? 139 HIS   A CE1 1 
ATOM   1040  N  NE2 . HIS   A  1  139 ? 79.069  -103.347 38.898  1.00 101.85 ? 139 HIS   A NE2 1 
ATOM   1041  N  N   . ASP   A  1  140 ? 75.044  -103.024 38.132  1.00 101.34 ? 140 ASP   A N   1 
ATOM   1042  C  CA  . ASP   A  1  140 ? 74.716  -104.279 37.410  1.00 103.40 ? 140 ASP   A CA  1 
ATOM   1043  C  C   . ASP   A  1  140 ? 75.878  -104.611 36.468  1.00 102.80 ? 140 ASP   A C   1 
ATOM   1044  O  O   . ASP   A  1  140 ? 76.593  -103.678 36.054  1.00 98.78  ? 140 ASP   A O   1 
ATOM   1045  C  CB  . ASP   A  1  140 ? 73.361  -104.170 36.708  1.00 106.24 ? 140 ASP   A CB  1 
ATOM   1046  C  CG  . ASP   A  1  140 ? 73.296  -103.069 35.666  1.00 110.13 ? 140 ASP   A CG  1 
ATOM   1047  O  OD1 . ASP   A  1  140 ? 73.683  -103.340 34.514  1.00 114.38 ? 140 ASP   A OD1 1 
ATOM   1048  O  OD2 . ASP   A  1  140 ? 72.870  -101.948 36.019  1.00 111.48 ? 140 ASP   A OD2 1 
ATOM   1049  N  N   . GLU   A  1  141 ? 76.044  -105.899 36.161  1.00 107.91 ? 141 GLU   A N   1 
ATOM   1050  C  CA  . GLU   A  1  141 ? 77.264  -106.487 35.544  1.00 109.82 ? 141 GLU   A CA  1 
ATOM   1051  C  C   . GLU   A  1  141 ? 77.599  -105.789 34.217  1.00 105.73 ? 141 GLU   A C   1 
ATOM   1052  O  O   . GLU   A  1  141 ? 78.804  -105.598 33.956  1.00 105.19 ? 141 GLU   A O   1 
ATOM   1053  C  CB  . GLU   A  1  141 ? 77.064  -107.990 35.347  1.00 113.89 ? 141 GLU   A CB  1 
ATOM   1054  C  CG  . GLU   A  1  141 ? 78.338  -108.735 34.993  1.00 117.48 ? 141 GLU   A CG  1 
ATOM   1055  C  CD  . GLU   A  1  141 ? 78.123  -110.198 34.653  1.00 119.91 ? 141 GLU   A CD  1 
ATOM   1056  O  OE1 . GLU   A  1  141 ? 78.873  -110.719 33.805  1.00 124.59 ? 141 GLU   A OE1 1 
ATOM   1057  O  OE2 . GLU   A  1  141 ? 77.206  -110.810 35.237  1.00 122.23 ? 141 GLU   A OE2 1 
ATOM   1058  N  N   . PHE   A  1  142 ? 76.590  -105.425 33.415  1.00 104.54 ? 142 PHE   A N   1 
ATOM   1059  C  CA  . PHE   A  1  142 ? 76.761  -104.994 31.999  1.00 104.79 ? 142 PHE   A CA  1 
ATOM   1060  C  C   . PHE   A  1  142 ? 76.687  -103.467 31.845  1.00 101.42 ? 142 PHE   A C   1 
ATOM   1061  O  O   . PHE   A  1  142 ? 77.021  -102.994 30.740  1.00 99.78  ? 142 PHE   A O   1 
ATOM   1062  C  CB  . PHE   A  1  142 ? 75.731  -105.684 31.100  1.00 106.24 ? 142 PHE   A CB  1 
ATOM   1063  C  CG  . PHE   A  1  142 ? 75.952  -107.166 30.923  1.00 109.51 ? 142 PHE   A CG  1 
ATOM   1064  C  CD1 . PHE   A  1  142 ? 75.524  -108.064 31.889  1.00 111.06 ? 142 PHE   A CD1 1 
ATOM   1065  C  CD2 . PHE   A  1  142 ? 76.594  -107.664 29.798  1.00 110.49 ? 142 PHE   A CD2 1 
ATOM   1066  C  CE1 . PHE   A  1  142 ? 75.729  -109.427 31.734  1.00 114.37 ? 142 PHE   A CE1 1 
ATOM   1067  C  CE2 . PHE   A  1  142 ? 76.797  -109.027 29.644  1.00 113.38 ? 142 PHE   A CE2 1 
ATOM   1068  C  CZ  . PHE   A  1  142 ? 76.365  -109.905 30.612  1.00 115.88 ? 142 PHE   A CZ  1 
ATOM   1069  N  N   . ASN   A  1  143 ? 76.269  -102.724 32.878  1.00 100.34 ? 143 ASN   A N   1 
ATOM   1070  C  CA  . ASN   A  1  143 ? 76.177  -101.235 32.844  1.00 102.13 ? 143 ASN   A CA  1 
ATOM   1071  C  C   . ASN   A  1  143 ? 77.100  -100.591 33.889  1.00 99.08  ? 143 ASN   A C   1 
ATOM   1072  O  O   . ASN   A  1  143 ? 77.300  -99.366  33.802  1.00 99.33  ? 143 ASN   A O   1 
ATOM   1073  C  CB  . ASN   A  1  143 ? 74.743  -100.744 33.055  1.00 100.75 ? 143 ASN   A CB  1 
ATOM   1074  C  CG  . ASN   A  1  143 ? 73.821  -101.133 31.921  1.00 103.37 ? 143 ASN   A CG  1 
ATOM   1075  O  OD1 . ASN   A  1  143 ? 73.785  -100.462 30.892  1.00 104.53 ? 143 ASN   A OD1 1 
ATOM   1076  N  ND2 . ASN   A  1  143 ? 73.077  -102.214 32.093  1.00 105.02 ? 143 ASN   A ND2 1 
ATOM   1077  N  N   . GLY   A  1  144 ? 77.640  -101.370 34.832  1.00 99.95  ? 144 GLY   A N   1 
ATOM   1078  C  CA  . GLY   A  1  144 ? 78.431  -100.853 35.965  1.00 99.21  ? 144 GLY   A CA  1 
ATOM   1079  C  C   . GLY   A  1  144 ? 77.575  -99.995  36.881  1.00 98.29  ? 144 GLY   A C   1 
ATOM   1080  O  O   . GLY   A  1  144 ? 76.364  -100.278 36.991  1.00 94.17  ? 144 GLY   A O   1 
ATOM   1081  N  N   . PHE   A  1  145 ? 78.172  -98.973  37.502  1.00 98.08  ? 145 PHE   A N   1 
ATOM   1082  C  CA  . PHE   A  1  145 ? 77.505  -98.069  38.477  1.00 96.28  ? 145 PHE   A CA  1 
ATOM   1083  C  C   . PHE   A  1  145 ? 76.725  -96.988  37.727  1.00 94.63  ? 145 PHE   A C   1 
ATOM   1084  O  O   . PHE   A  1  145 ? 77.190  -96.538  36.661  1.00 91.43  ? 145 PHE   A O   1 
ATOM   1085  C  CB  . PHE   A  1  145 ? 78.526  -97.447  39.430  1.00 97.80  ? 145 PHE   A CB  1 
ATOM   1086  C  CG  . PHE   A  1  145 ? 79.258  -98.454  40.279  1.00 98.63  ? 145 PHE   A CG  1 
ATOM   1087  C  CD1 . PHE   A  1  145 ? 78.663  -98.996  41.409  1.00 100.34 ? 145 PHE   A CD1 1 
ATOM   1088  C  CD2 . PHE   A  1  145 ? 80.531  -98.879  39.934  1.00 101.02 ? 145 PHE   A CD2 1 
ATOM   1089  C  CE1 . PHE   A  1  145 ? 79.332  -99.934  42.180  1.00 101.49 ? 145 PHE   A CE1 1 
ATOM   1090  C  CE2 . PHE   A  1  145 ? 81.200  -99.815  40.708  1.00 102.35 ? 145 PHE   A CE2 1 
ATOM   1091  C  CZ  . PHE   A  1  145 ? 80.600  -100.340 41.831  1.00 102.29 ? 145 PHE   A CZ  1 
ATOM   1092  N  N   . SER   A  1  146 ? 75.576  -96.589  38.281  1.00 95.30  ? 146 SER   A N   1 
ATOM   1093  C  CA  . SER   A  1  146 ? 74.668  -95.569  37.698  1.00 96.36  ? 146 SER   A CA  1 
ATOM   1094  C  C   . SER   A  1  146 ? 73.829  -94.895  38.792  1.00 95.93  ? 146 SER   A C   1 
ATOM   1095  O  O   . SER   A  1  146 ? 73.567  -95.530  39.832  1.00 95.31  ? 146 SER   A O   1 
ATOM   1096  C  CB  . SER   A  1  146 ? 73.799  -96.170  36.623  1.00 97.35  ? 146 SER   A CB  1 
ATOM   1097  O  OG  . SER   A  1  146 ? 73.128  -97.325  37.100  1.00 97.26  ? 146 SER   A OG  1 
ATOM   1098  N  N   . LEU   A  1  147 ? 73.438  -93.644  38.539  1.00 96.33  ? 147 LEU   A N   1 
ATOM   1099  C  CA  . LEU   A  1  147 ? 72.634  -92.776  39.440  1.00 94.81  ? 147 LEU   A CA  1 
ATOM   1100  C  C   . LEU   A  1  147 ? 71.524  -92.124  38.609  1.00 94.62  ? 147 LEU   A C   1 
ATOM   1101  O  O   . LEU   A  1  147 ? 71.851  -91.521  37.568  1.00 94.85  ? 147 LEU   A O   1 
ATOM   1102  C  CB  . LEU   A  1  147 ? 73.564  -91.726  40.058  1.00 93.81  ? 147 LEU   A CB  1 
ATOM   1103  C  CG  . LEU   A  1  147 ? 72.895  -90.632  40.888  1.00 92.04  ? 147 LEU   A CG  1 
ATOM   1104  C  CD1 . LEU   A  1  147 ? 72.382  -91.185  42.208  1.00 90.59  ? 147 LEU   A CD1 1 
ATOM   1105  C  CD2 . LEU   A  1  147 ? 73.863  -89.487  41.132  1.00 92.20  ? 147 LEU   A CD2 1 
ATOM   1106  N  N   . TYR   A  1  148 ? 70.268  -92.253  39.046  1.00 93.20  ? 148 TYR   A N   1 
ATOM   1107  C  CA  . TYR   A  1  148 ? 69.072  -91.751  38.323  1.00 92.11  ? 148 TYR   A CA  1 
ATOM   1108  C  C   . TYR   A  1  148 ? 68.238  -90.867  39.249  1.00 89.65  ? 148 TYR   A C   1 
ATOM   1109  O  O   . TYR   A  1  148 ? 68.194  -91.135  40.462  1.00 86.07  ? 148 TYR   A O   1 
ATOM   1110  C  CB  . TYR   A  1  148 ? 68.239  -92.916  37.784  1.00 92.87  ? 148 TYR   A CB  1 
ATOM   1111  C  CG  . TYR   A  1  148 ? 68.840  -93.583  36.575  1.00 94.89  ? 148 TYR   A CG  1 
ATOM   1112  C  CD1 . TYR   A  1  148 ? 69.788  -94.585  36.708  1.00 96.94  ? 148 TYR   A CD1 1 
ATOM   1113  C  CD2 . TYR   A  1  148 ? 68.479  -93.198  35.294  1.00 94.84  ? 148 TYR   A CD2 1 
ATOM   1114  C  CE1 . TYR   A  1  148 ? 70.354  -95.198  35.601  1.00 97.64  ? 148 TYR   A CE1 1 
ATOM   1115  C  CE2 . TYR   A  1  148 ? 69.036  -93.799  34.177  1.00 95.79  ? 148 TYR   A CE2 1 
ATOM   1116  C  CZ  . TYR   A  1  148 ? 69.977  -94.801  34.330  1.00 95.82  ? 148 TYR   A CZ  1 
ATOM   1117  O  OH  . TYR   A  1  148 ? 70.529  -95.396  33.234  1.00 102.96 ? 148 TYR   A OH  1 
ATOM   1118  N  N   . GLN   A  1  149 ? 67.609  -89.843  38.668  1.00 90.60  ? 149 GLN   A N   1 
ATOM   1119  C  CA  . GLN   A  1  149 ? 66.603  -88.974  39.328  1.00 92.18  ? 149 GLN   A CA  1 
ATOM   1120  C  C   . GLN   A  1  149 ? 65.246  -89.236  38.671  1.00 92.84  ? 149 GLN   A C   1 
ATOM   1121  O  O   . GLN   A  1  149 ? 65.174  -89.116  37.437  1.00 93.25  ? 149 GLN   A O   1 
ATOM   1122  C  CB  . GLN   A  1  149 ? 66.989  -87.501  39.187  1.00 93.73  ? 149 GLN   A CB  1 
ATOM   1123  C  CG  . GLN   A  1  149 ? 66.010  -86.548  39.863  1.00 94.83  ? 149 GLN   A CG  1 
ATOM   1124  C  CD  . GLN   A  1  149 ? 66.357  -85.093  39.660  1.00 94.25  ? 149 GLN   A CD  1 
ATOM   1125  O  OE1 . GLN   A  1  149 ? 67.511  -84.726  39.442  1.00 93.19  ? 149 GLN   A OE1 1 
ATOM   1126  N  NE2 . GLN   A  1  149 ? 65.348  -84.242  39.734  1.00 94.18  ? 149 GLN   A NE2 1 
ATOM   1127  N  N   . VAL   A  1  150 ? 64.226  -89.583  39.463  1.00 93.65  ? 150 VAL   A N   1 
ATOM   1128  C  CA  . VAL   A  1  150 ? 62.824  -89.791  38.988  1.00 92.61  ? 150 VAL   A CA  1 
ATOM   1129  C  C   . VAL   A  1  150 ? 61.949  -88.680  39.576  1.00 89.71  ? 150 VAL   A C   1 
ATOM   1130  O  O   . VAL   A  1  150 ? 61.912  -88.561  40.813  1.00 87.04  ? 150 VAL   A O   1 
ATOM   1131  C  CB  . VAL   A  1  150 ? 62.283  -91.184  39.366  1.00 93.16  ? 150 VAL   A CB  1 
ATOM   1132  C  CG1 . VAL   A  1  150 ? 60.970  -91.481  38.657  1.00 93.31  ? 150 VAL   A CG1 1 
ATOM   1133  C  CG2 . VAL   A  1  150 ? 63.294  -92.286  39.090  1.00 94.91  ? 150 VAL   A CG2 1 
ATOM   1134  N  N   . ASP   A  1  151 ? 61.270  -87.913  38.716  1.00 89.31  ? 151 ASP   A N   1 
ATOM   1135  C  CA  . ASP   A  1  151 ? 60.424  -86.750  39.102  1.00 89.92  ? 151 ASP   A CA  1 
ATOM   1136  C  C   . ASP   A  1  151 ? 58.955  -87.163  39.122  1.00 87.17  ? 151 ASP   A C   1 
ATOM   1137  O  O   . ASP   A  1  151 ? 58.568  -88.116  38.453  1.00 87.77  ? 151 ASP   A O   1 
ATOM   1138  C  CB  . ASP   A  1  151 ? 60.632  -85.567  38.152  1.00 93.42  ? 151 ASP   A CB  1 
ATOM   1139  C  CG  . ASP   A  1  151 ? 61.879  -84.748  38.431  1.00 97.01  ? 151 ASP   A CG  1 
ATOM   1140  O  OD1 . ASP   A  1  151 ? 62.544  -85.013  39.453  1.00 101.61 ? 151 ASP   A OD1 1 
ATOM   1141  O  OD2 . ASP   A  1  151 ? 62.172  -83.848  37.622  1.00 101.99 ? 151 ASP   A OD2 1 
ATOM   1142  N  N   . PRO   A  1  152 ? 58.097  -86.434  39.872  1.00 87.16  ? 152 PRO   A N   1 
ATOM   1143  C  CA  . PRO   A  1  152 ? 56.659  -86.710  39.939  1.00 86.69  ? 152 PRO   A CA  1 
ATOM   1144  C  C   . PRO   A  1  152 ? 55.959  -86.998  38.602  1.00 88.61  ? 152 PRO   A C   1 
ATOM   1145  O  O   . PRO   A  1  152 ? 55.000  -87.753  38.606  1.00 90.39  ? 152 PRO   A O   1 
ATOM   1146  C  CB  . PRO   A  1  152 ? 56.101  -85.399  40.509  1.00 87.05  ? 152 PRO   A CB  1 
ATOM   1147  C  CG  . PRO   A  1  152 ? 57.199  -84.904  41.419  1.00 89.45  ? 152 PRO   A CG  1 
ATOM   1148  C  CD  . PRO   A  1  152 ? 58.484  -85.294  40.719  1.00 89.17  ? 152 PRO   A CD  1 
ATOM   1149  N  N   . SER   A  1  153 ? 56.430  -86.380  37.513  1.00 90.19  ? 153 SER   A N   1 
ATOM   1150  C  CA  . SER   A  1  153 ? 55.920  -86.563  36.127  1.00 91.45  ? 153 SER   A CA  1 
ATOM   1151  C  C   . SER   A  1  153 ? 56.115  -88.017  35.680  1.00 90.77  ? 153 SER   A C   1 
ATOM   1152  O  O   . SER   A  1  153 ? 55.269  -88.516  34.912  1.00 93.40  ? 153 SER   A O   1 
ATOM   1153  C  CB  . SER   A  1  153 ? 56.599  -85.616  35.168  1.00 91.49  ? 153 SER   A CB  1 
ATOM   1154  O  OG  . SER   A  1  153 ? 58.001  -85.835  35.143  1.00 93.31  ? 153 SER   A OG  1 
ATOM   1155  N  N   . GLY   A  1  154 ? 57.193  -88.656  36.144  1.00 89.33  ? 154 GLY   A N   1 
ATOM   1156  C  CA  . GLY   A  1  154 ? 57.631  -89.994  35.703  1.00 90.42  ? 154 GLY   A CA  1 
ATOM   1157  C  C   . GLY   A  1  154 ? 58.854  -89.908  34.806  1.00 92.29  ? 154 GLY   A C   1 
ATOM   1158  O  O   . GLY   A  1  154 ? 59.267  -90.951  34.272  1.00 95.73  ? 154 GLY   A O   1 
ATOM   1159  N  N   . SER   A  1  155 ? 59.405  -88.704  34.623  1.00 93.35  ? 155 SER   A N   1 
ATOM   1160  C  CA  . SER   A  1  155 ? 60.664  -88.457  33.874  1.00 93.84  ? 155 SER   A CA  1 
ATOM   1161  C  C   . SER   A  1  155 ? 61.855  -88.862  34.742  1.00 90.23  ? 155 SER   A C   1 
ATOM   1162  O  O   . SER   A  1  155 ? 61.854  -88.513  35.937  1.00 88.43  ? 155 SER   A O   1 
ATOM   1163  C  CB  . SER   A  1  155 ? 60.780  -87.019  33.462  1.00 95.91  ? 155 SER   A CB  1 
ATOM   1164  O  OG  . SER   A  1  155 ? 59.675  -86.635  32.656  1.00 99.02  ? 155 SER   A OG  1 
ATOM   1165  N  N   . TYR   A  1  156 ? 62.829  -89.562  34.157  1.00 92.19  ? 156 TYR   A N   1 
ATOM   1166  C  CA  . TYR   A  1  156 ? 64.099  -89.939  34.827  1.00 92.73  ? 156 TYR   A CA  1 
ATOM   1167  C  C   . TYR   A  1  156 ? 65.275  -89.498  33.951  1.00 92.31  ? 156 TYR   A C   1 
ATOM   1168  O  O   . TYR   A  1  156 ? 65.161  -89.515  32.708  1.00 91.95  ? 156 TYR   A O   1 
ATOM   1169  C  CB  . TYR   A  1  156 ? 64.119  -91.431  35.183  1.00 92.60  ? 156 TYR   A CB  1 
ATOM   1170  C  CG  . TYR   A  1  156 ? 63.928  -92.388  34.033  1.00 91.68  ? 156 TYR   A CG  1 
ATOM   1171  C  CD1 . TYR   A  1  156 ? 62.660  -92.746  33.604  1.00 91.89  ? 156 TYR   A CD1 1 
ATOM   1172  C  CD2 . TYR   A  1  156 ? 65.014  -92.964  33.393  1.00 92.90  ? 156 TYR   A CD2 1 
ATOM   1173  C  CE1 . TYR   A  1  156 ? 62.475  -93.637  32.559  1.00 94.18  ? 156 TYR   A CE1 1 
ATOM   1174  C  CE2 . TYR   A  1  156 ? 64.847  -93.857  32.346  1.00 95.11  ? 156 TYR   A CE2 1 
ATOM   1175  C  CZ  . TYR   A  1  156 ? 63.573  -94.196  31.927  1.00 94.63  ? 156 TYR   A CZ  1 
ATOM   1176  O  OH  . TYR   A  1  156 ? 63.397  -95.075  30.895  1.00 96.48  ? 156 TYR   A OH  1 
ATOM   1177  N  N   . PHE   A  1  157 ? 66.362  -89.081  34.603  1.00 91.41  ? 157 PHE   A N   1 
ATOM   1178  C  CA  . PHE   A  1  157 ? 67.612  -88.596  33.967  1.00 97.12  ? 157 PHE   A CA  1 
ATOM   1179  C  C   . PHE   A  1  157 ? 68.797  -89.253  34.665  1.00 95.89  ? 157 PHE   A C   1 
ATOM   1180  O  O   . PHE   A  1  157 ? 68.795  -89.378  35.888  1.00 97.34  ? 157 PHE   A O   1 
ATOM   1181  C  CB  . PHE   A  1  157 ? 67.707  -87.069  34.055  1.00 100.04 ? 157 PHE   A CB  1 
ATOM   1182  C  CG  . PHE   A  1  157 ? 66.389  -86.359  34.252  1.00 102.55 ? 157 PHE   A CG  1 
ATOM   1183  C  CD1 . PHE   A  1  157 ? 65.960  -85.997  35.521  1.00 99.41  ? 157 PHE   A CD1 1 
ATOM   1184  C  CD2 . PHE   A  1  157 ? 65.574  -86.060  33.170  1.00 103.48 ? 157 PHE   A CD2 1 
ATOM   1185  C  CE1 . PHE   A  1  157 ? 64.747  -85.349  35.704  1.00 96.35  ? 157 PHE   A CE1 1 
ATOM   1186  C  CE2 . PHE   A  1  157 ? 64.362  -85.410  33.354  1.00 101.29 ? 157 PHE   A CE2 1 
ATOM   1187  C  CZ  . PHE   A  1  157 ? 63.950  -85.057  34.620  1.00 98.27  ? 157 PHE   A CZ  1 
ATOM   1188  N  N   . PRO   A  1  158 ? 69.837  -89.697  33.924  1.00 97.14  ? 158 PRO   A N   1 
ATOM   1189  C  CA  . PRO   A  1  158 ? 71.053  -90.212  34.545  1.00 98.70  ? 158 PRO   A CA  1 
ATOM   1190  C  C   . PRO   A  1  158 ? 71.970  -89.041  34.926  1.00 98.45  ? 158 PRO   A C   1 
ATOM   1191  O  O   . PRO   A  1  158 ? 72.062  -88.105  34.152  1.00 97.52  ? 158 PRO   A O   1 
ATOM   1192  C  CB  . PRO   A  1  158 ? 71.660  -91.111  33.460  1.00 101.30 ? 158 PRO   A CB  1 
ATOM   1193  C  CG  . PRO   A  1  158 ? 71.141  -90.547  32.142  1.00 102.06 ? 158 PRO   A CG  1 
ATOM   1194  C  CD  . PRO   A  1  158 ? 69.911  -89.716  32.457  1.00 98.99  ? 158 PRO   A CD  1 
ATOM   1195  N  N   . TRP   A  1  159 ? 72.600  -89.117  36.104  1.00 100.11 ? 159 TRP   A N   1 
ATOM   1196  C  CA  . TRP   A  1  159 ? 73.442  -88.039  36.689  1.00 101.25 ? 159 TRP   A CA  1 
ATOM   1197  C  C   . TRP   A  1  159 ? 74.828  -88.579  37.054  1.00 104.43 ? 159 TRP   A C   1 
ATOM   1198  O  O   . TRP   A  1  159 ? 74.918  -89.739  37.507  1.00 104.34 ? 159 TRP   A O   1 
ATOM   1199  C  CB  . TRP   A  1  159 ? 72.767  -87.433  37.925  1.00 99.22  ? 159 TRP   A CB  1 
ATOM   1200  C  CG  . TRP   A  1  159 ? 71.569  -86.585  37.632  1.00 99.43  ? 159 TRP   A CG  1 
ATOM   1201  C  CD1 . TRP   A  1  159 ? 70.259  -86.957  37.710  1.00 100.86 ? 159 TRP   A CD1 1 
ATOM   1202  C  CD2 . TRP   A  1  159 ? 71.570  -85.204  37.231  1.00 100.55 ? 159 TRP   A CD2 1 
ATOM   1203  N  NE1 . TRP   A  1  159 ? 69.445  -85.906  37.379  1.00 101.63 ? 159 TRP   A NE1 1 
ATOM   1204  C  CE2 . TRP   A  1  159 ? 70.220  -84.818  37.081  1.00 101.11 ? 159 TRP   A CE2 1 
ATOM   1205  C  CE3 . TRP   A  1  159 ? 72.573  -84.261  36.980  1.00 102.21 ? 159 TRP   A CE3 1 
ATOM   1206  C  CZ2 . TRP   A  1  159 ? 69.853  -83.532  36.689  1.00 102.24 ? 159 TRP   A CZ2 1 
ATOM   1207  C  CZ3 . TRP   A  1  159 ? 72.209  -82.990  36.596  1.00 105.09 ? 159 TRP   A CZ3 1 
ATOM   1208  C  CH2 . TRP   A  1  159 ? 70.868  -82.633  36.452  1.00 105.45 ? 159 TRP   A CH2 1 
ATOM   1209  N  N   . LYS   A  1  160 ? 75.860  -87.749  36.874  1.00 104.36 ? 160 LYS   A N   1 
ATOM   1210  C  CA  . LYS   A  1  160 ? 77.213  -87.958  37.454  1.00 104.59 ? 160 LYS   A CA  1 
ATOM   1211  C  C   . LYS   A  1  160 ? 77.154  -87.607  38.941  1.00 103.25 ? 160 LYS   A C   1 
ATOM   1212  O  O   . LYS   A  1  160 ? 77.753  -88.332  39.756  1.00 111.82 ? 160 LYS   A O   1 
ATOM   1213  C  CB  . LYS   A  1  160 ? 78.251  -87.088  36.743  1.00 107.08 ? 160 LYS   A CB  1 
ATOM   1214  C  CG  . LYS   A  1  160 ? 78.581  -87.522  35.325  1.00 109.43 ? 160 LYS   A CG  1 
ATOM   1215  C  CD  . LYS   A  1  160 ? 79.098  -86.400  34.468  1.00 112.66 ? 160 LYS   A CD  1 
ATOM   1216  C  CE  . LYS   A  1  160 ? 79.535  -86.865  33.097  1.00 116.51 ? 160 LYS   A CE  1 
ATOM   1217  N  NZ  . LYS   A  1  160 ? 79.766  -85.718  32.189  1.00 120.45 ? 160 LYS   A NZ  1 
ATOM   1218  N  N   . ALA   A  1  161 ? 76.456  -86.520  39.263  1.00 97.41  ? 161 ALA   A N   1 
ATOM   1219  C  CA  . ALA   A  1  161 ? 76.164  -86.072  40.641  1.00 98.31  ? 161 ALA   A CA  1 
ATOM   1220  C  C   . ALA   A  1  161 ? 75.043  -85.031  40.589  1.00 98.40  ? 161 ALA   A C   1 
ATOM   1221  O  O   . ALA   A  1  161 ? 75.004  -84.250  39.614  1.00 103.17 ? 161 ALA   A O   1 
ATOM   1222  C  CB  . ALA   A  1  161 ? 77.409  -85.510  41.280  1.00 97.99  ? 161 ALA   A CB  1 
ATOM   1223  N  N   . THR   A  1  162 ? 74.164  -85.024  41.591  1.00 93.63  ? 162 THR   A N   1 
ATOM   1224  C  CA  . THR   A  1  162 ? 73.066  -84.030  41.707  1.00 94.21  ? 162 THR   A CA  1 
ATOM   1225  C  C   . THR   A  1  162 ? 72.528  -83.991  43.135  1.00 92.31  ? 162 THR   A C   1 
ATOM   1226  O  O   . THR   A  1  162 ? 72.859  -84.891  43.928  1.00 93.04  ? 162 THR   A O   1 
ATOM   1227  C  CB  . THR   A  1  162 ? 71.915  -84.339  40.743  1.00 92.47  ? 162 THR   A CB  1 
ATOM   1228  O  OG1 . THR   A  1  162 ? 71.000  -83.242  40.780  1.00 90.54  ? 162 THR   A OG1 1 
ATOM   1229  C  CG2 . THR   A  1  162 ? 71.196  -85.627  41.081  1.00 92.80  ? 162 THR   A CG2 1 
ATOM   1230  N  N   . ALA   A  1  163 ? 71.714  -82.977  43.416  1.00 92.58  ? 163 ALA   A N   1 
ATOM   1231  C  CA  . ALA   A  1  163 ? 70.929  -82.825  44.659  1.00 91.51  ? 163 ALA   A CA  1 
ATOM   1232  C  C   . ALA   A  1  163 ? 69.482  -82.511  44.281  1.00 89.02  ? 163 ALA   A C   1 
ATOM   1233  O  O   . ALA   A  1  163 ? 69.245  -82.106  43.130  1.00 91.39  ? 163 ALA   A O   1 
ATOM   1234  C  CB  . ALA   A  1  163 ? 71.534  -81.747  45.520  1.00 94.16  ? 163 ALA   A CB  1 
ATOM   1235  N  N   . ILE   A  1  164 ? 68.557  -82.730  45.214  1.00 88.95  ? 164 ILE   A N   1 
ATOM   1236  C  CA  . ILE   A  1  164 ? 67.107  -82.407  45.071  1.00 92.02  ? 164 ILE   A CA  1 
ATOM   1237  C  C   . ILE   A  1  164 ? 66.598  -81.878  46.413  1.00 93.00  ? 164 ILE   A C   1 
ATOM   1238  O  O   . ILE   A  1  164 ? 67.156  -82.276  47.453  1.00 96.32  ? 164 ILE   A O   1 
ATOM   1239  C  CB  . ILE   A  1  164 ? 66.303  -83.641  44.618  1.00 91.05  ? 164 ILE   A CB  1 
ATOM   1240  C  CG1 . ILE   A  1  164 ? 66.696  -84.887  45.417  1.00 90.32  ? 164 ILE   A CG1 1 
ATOM   1241  C  CG2 . ILE   A  1  164 ? 66.445  -83.853  43.118  1.00 92.69  ? 164 ILE   A CG2 1 
ATOM   1242  C  CD1 . ILE   A  1  164 ? 65.719  -86.032  45.305  1.00 89.51  ? 164 ILE   A CD1 1 
ATOM   1243  N  N   . GLY   A  1  165 ? 65.580  -81.017  46.378  1.00 94.44  ? 165 GLY   A N   1 
ATOM   1244  C  CA  . GLY   A  1  165 ? 64.897  -80.503  47.578  1.00 95.26  ? 165 GLY   A CA  1 
ATOM   1245  C  C   . GLY   A  1  165 ? 65.349  -79.101  47.953  1.00 97.53  ? 165 GLY   A C   1 
ATOM   1246  O  O   . GLY   A  1  165 ? 65.755  -78.338  47.051  1.00 96.34  ? 165 GLY   A O   1 
ATOM   1247  N  N   . LYS   A  1  166 ? 65.294  -78.801  49.254  1.00 99.84  ? 166 LYS   A N   1 
ATOM   1248  C  CA  . LYS   A  1  166 ? 65.406  -77.449  49.867  1.00 104.45 ? 166 LYS   A CA  1 
ATOM   1249  C  C   . LYS   A  1  166 ? 66.520  -76.644  49.185  1.00 104.62 ? 166 LYS   A C   1 
ATOM   1250  O  O   . LYS   A  1  166 ? 66.182  -75.748  48.383  1.00 106.81 ? 166 LYS   A O   1 
ATOM   1251  C  CB  . LYS   A  1  166 ? 65.629  -77.591  51.377  1.00 105.97 ? 166 LYS   A CB  1 
ATOM   1252  C  CG  . LYS   A  1  166 ? 64.997  -76.507  52.237  1.00 113.29 ? 166 LYS   A CG  1 
ATOM   1253  C  CD  . LYS   A  1  166 ? 65.042  -76.837  53.714  1.00 120.02 ? 166 LYS   A CD  1 
ATOM   1254  C  CE  . LYS   A  1  166 ? 64.454  -75.751  54.589  1.00 126.82 ? 166 LYS   A CE  1 
ATOM   1255  N  NZ  . LYS   A  1  166 ? 62.977  -75.695  54.474  1.00 130.62 ? 166 LYS   A NZ  1 
ATOM   1256  N  N   . GLY   A  1  167 ? 67.788  -76.958  49.477  1.00 104.92 ? 167 GLY   A N   1 
ATOM   1257  C  CA  . GLY   A  1  167 ? 68.962  -76.187  49.021  1.00 108.38 ? 167 GLY   A CA  1 
ATOM   1258  C  C   . GLY   A  1  167 ? 69.679  -76.882  47.880  1.00 108.26 ? 167 GLY   A C   1 
ATOM   1259  O  O   . GLY   A  1  167 ? 70.923  -76.967  47.931  1.00 110.03 ? 167 GLY   A O   1 
ATOM   1260  N  N   . SER   A  1  168 ? 68.918  -77.352  46.885  1.00 111.14 ? 168 SER   A N   1 
ATOM   1261  C  CA  . SER   A  1  168 ? 69.412  -78.111  45.707  1.00 109.17 ? 168 SER   A CA  1 
ATOM   1262  C  C   . SER   A  1  168 ? 70.243  -77.195  44.802  1.00 112.28 ? 168 SER   A C   1 
ATOM   1263  O  O   . SER   A  1  168 ? 71.311  -77.645  44.340  1.00 109.91 ? 168 SER   A O   1 
ATOM   1264  C  CB  . SER   A  1  168 ? 68.272  -78.744  44.947  1.00 110.39 ? 168 SER   A CB  1 
ATOM   1265  O  OG  . SER   A  1  168 ? 67.322  -77.768  44.545  1.00 112.93 ? 168 SER   A OG  1 
ATOM   1266  N  N   . VAL   A  1  169 ? 69.777  -75.959  44.581  1.00 109.88 ? 169 VAL   A N   1 
ATOM   1267  C  CA  . VAL   A  1  169 ? 70.391  -74.983  43.629  1.00 109.81 ? 169 VAL   A CA  1 
ATOM   1268  C  C   . VAL   A  1  169 ? 71.851  -74.765  44.046  1.00 109.62 ? 169 VAL   A C   1 
ATOM   1269  O  O   . VAL   A  1  169 ? 72.734  -74.896  43.177  1.00 109.73 ? 169 VAL   A O   1 
ATOM   1270  C  CB  . VAL   A  1  169 ? 69.620  -73.648  43.564  1.00 109.83 ? 169 VAL   A CB  1 
ATOM   1271  C  CG1 . VAL   A  1  169 ? 70.111  -72.781  42.413  1.00 112.29 ? 169 VAL   A CG1 1 
ATOM   1272  C  CG2 . VAL   A  1  169 ? 68.114  -73.845  43.461  1.00 107.69 ? 169 VAL   A CG2 1 
ATOM   1273  N  N   . ALA   A  1  170 ? 72.087  -74.470  45.330  1.00 110.89 ? 170 ALA   A N   1 
ATOM   1274  C  CA  . ALA   A  1  170 ? 73.426  -74.210  45.916  1.00 112.50 ? 170 ALA   A CA  1 
ATOM   1275  C  C   . ALA   A  1  170 ? 74.259  -75.498  45.929  1.00 109.91 ? 170 ALA   A C   1 
ATOM   1276  O  O   . ALA   A  1  170 ? 75.460  -75.430  45.605  1.00 111.67 ? 170 ALA   A O   1 
ATOM   1277  C  CB  . ALA   A  1  170 ? 73.287  -73.639  47.306  1.00 115.13 ? 170 ALA   A CB  1 
ATOM   1278  N  N   . ALA   A  1  171 ? 73.642  -76.624  46.297  1.00 106.95 ? 171 ALA   A N   1 
ATOM   1279  C  CA  . ALA   A  1  171 ? 74.294  -77.952  46.393  1.00 105.63 ? 171 ALA   A CA  1 
ATOM   1280  C  C   . ALA   A  1  171 ? 74.818  -78.378  45.016  1.00 104.30 ? 171 ALA   A C   1 
ATOM   1281  O  O   . ALA   A  1  171 ? 75.974  -78.837  44.953  1.00 101.34 ? 171 ALA   A O   1 
ATOM   1282  C  CB  . ALA   A  1  171 ? 73.330  -78.966  46.956  1.00 102.21 ? 171 ALA   A CB  1 
ATOM   1283  N  N   . LYS   A  1  172 ? 74.002  -78.229  43.964  1.00 105.94 ? 172 LYS   A N   1 
ATOM   1284  C  CA  . LYS   A  1  172 ? 74.365  -78.608  42.569  1.00 109.46 ? 172 LYS   A CA  1 
ATOM   1285  C  C   . LYS   A  1  172 ? 75.598  -77.808  42.131  1.00 114.16 ? 172 LYS   A C   1 
ATOM   1286  O  O   . LYS   A  1  172 ? 76.521  -78.428  41.569  1.00 121.22 ? 172 LYS   A O   1 
ATOM   1287  C  CB  . LYS   A  1  172 ? 73.202  -78.389  41.594  1.00 109.30 ? 172 LYS   A CB  1 
ATOM   1288  C  CG  . LYS   A  1  172 ? 72.093  -79.435  41.652  1.00 108.22 ? 172 LYS   A CG  1 
ATOM   1289  C  CD  . LYS   A  1  172 ? 71.441  -79.725  40.310  1.00 107.93 ? 172 LYS   A CD  1 
ATOM   1290  C  CE  . LYS   A  1  172 ? 70.719  -78.536  39.710  1.00 109.38 ? 172 LYS   A CE  1 
ATOM   1291  N  NZ  . LYS   A  1  172 ? 69.461  -78.235  40.434  1.00 109.91 ? 172 LYS   A NZ  1 
ATOM   1292  N  N   . THR   A  1  173 ? 75.616  -76.494  42.385  1.00 114.91 ? 173 THR   A N   1 
ATOM   1293  C  CA  . THR   A  1  173 ? 76.758  -75.593  42.065  1.00 118.46 ? 173 THR   A CA  1 
ATOM   1294  C  C   . THR   A  1  173 ? 78.010  -76.072  42.809  1.00 119.70 ? 173 THR   A C   1 
ATOM   1295  O  O   . THR   A  1  173 ? 79.096  -76.049  42.197  1.00 126.94 ? 173 THR   A O   1 
ATOM   1296  C  CB  . THR   A  1  173 ? 76.470  -74.126  42.414  1.00 117.86 ? 173 THR   A CB  1 
ATOM   1297  O  OG1 . THR   A  1  173 ? 75.161  -73.788  41.955  1.00 120.99 ? 173 THR   A OG1 1 
ATOM   1298  C  CG2 . THR   A  1  173 ? 77.477  -73.177  41.801  1.00 118.20 ? 173 THR   A CG2 1 
ATOM   1299  N  N   . PHE   A  1  174 ? 77.863  -76.479  44.075  1.00 118.42 ? 174 PHE   A N   1 
ATOM   1300  C  CA  . PHE   A  1  174 ? 78.969  -77.005  44.919  1.00 119.17 ? 174 PHE   A CA  1 
ATOM   1301  C  C   . PHE   A  1  174 ? 79.530  -78.277  44.275  1.00 119.40 ? 174 PHE   A C   1 
ATOM   1302  O  O   . PHE   A  1  174 ? 80.765  -78.393  44.159  1.00 129.20 ? 174 PHE   A O   1 
ATOM   1303  C  CB  . PHE   A  1  174 ? 78.512  -77.271  46.358  1.00 116.83 ? 174 PHE   A CB  1 
ATOM   1304  C  CG  . PHE   A  1  174 ? 79.647  -77.509  47.324  1.00 118.35 ? 174 PHE   A CG  1 
ATOM   1305  C  CD1 . PHE   A  1  174 ? 80.252  -78.753  47.418  1.00 117.05 ? 174 PHE   A CD1 1 
ATOM   1306  C  CD2 . PHE   A  1  174 ? 80.127  -76.483  48.124  1.00 119.81 ? 174 PHE   A CD2 1 
ATOM   1307  C  CE1 . PHE   A  1  174 ? 81.304  -78.968  48.295  1.00 119.49 ? 174 PHE   A CE1 1 
ATOM   1308  C  CE2 . PHE   A  1  174 ? 81.178  -76.699  49.002  1.00 121.36 ? 174 PHE   A CE2 1 
ATOM   1309  C  CZ  . PHE   A  1  174 ? 81.765  -77.941  49.087  1.00 120.66 ? 174 PHE   A CZ  1 
ATOM   1310  N  N   . LEU   A  1  175 ? 78.648  -79.191  43.858  1.00 113.00 ? 175 LEU   A N   1 
ATOM   1311  C  CA  . LEU   A  1  175 ? 79.030  -80.504  43.274  1.00 111.46 ? 175 LEU   A CA  1 
ATOM   1312  C  C   . LEU   A  1  175 ? 79.758  -80.294  41.939  1.00 114.20 ? 175 LEU   A C   1 
ATOM   1313  O  O   . LEU   A  1  175 ? 80.684  -81.078  41.663  1.00 118.00 ? 175 LEU   A O   1 
ATOM   1314  C  CB  . LEU   A  1  175 ? 77.781  -81.376  43.102  1.00 109.58 ? 175 LEU   A CB  1 
ATOM   1315  C  CG  . LEU   A  1  175 ? 77.150  -81.907  44.392  1.00 106.92 ? 175 LEU   A CG  1 
ATOM   1316  C  CD1 . LEU   A  1  175 ? 75.826  -82.598  44.101  1.00 104.08 ? 175 LEU   A CD1 1 
ATOM   1317  C  CD2 . LEU   A  1  175 ? 78.090  -82.858  45.122  1.00 104.66 ? 175 LEU   A CD2 1 
ATOM   1318  N  N   . GLU   A  1  176 ? 79.375  -79.279  41.155  1.00 115.17 ? 176 GLU   A N   1 
ATOM   1319  C  CA  . GLU   A  1  176 ? 79.978  -78.985  39.823  1.00 121.07 ? 176 GLU   A CA  1 
ATOM   1320  C  C   . GLU   A  1  176 ? 81.462  -78.637  39.995  1.00 120.36 ? 176 GLU   A C   1 
ATOM   1321  O  O   . GLU   A  1  176 ? 82.273  -79.111  39.176  1.00 122.52 ? 176 GLU   A O   1 
ATOM   1322  C  CB  . GLU   A  1  176 ? 79.232  -77.856  39.107  1.00 124.85 ? 176 GLU   A CB  1 
ATOM   1323  C  CG  . GLU   A  1  176 ? 77.879  -78.279  38.569  1.00 128.91 ? 176 GLU   A CG  1 
ATOM   1324  C  CD  . GLU   A  1  176 ? 77.066  -77.188  37.897  1.00 136.84 ? 176 GLU   A CD  1 
ATOM   1325  O  OE1 . GLU   A  1  176 ? 77.673  -76.312  37.246  1.00 146.60 ? 176 GLU   A OE1 1 
ATOM   1326  O  OE2 . GLU   A  1  176 ? 75.825  -77.220  38.025  1.00 143.76 ? 176 GLU   A OE2 1 
ATOM   1327  N  N   . LYS   A  1  177 ? 81.798  -77.852  41.022  1.00 121.17 ? 177 LYS   A N   1 
ATOM   1328  C  CA  . LYS   A  1  177 ? 83.190  -77.416  41.315  1.00 125.63 ? 177 LYS   A CA  1 
ATOM   1329  C  C   . LYS   A  1  177 ? 84.049  -78.624  41.713  1.00 124.27 ? 177 LYS   A C   1 
ATOM   1330  O  O   . LYS   A  1  177 ? 85.239  -78.633  41.345  1.00 124.39 ? 177 LYS   A O   1 
ATOM   1331  C  CB  . LYS   A  1  177 ? 83.203  -76.339  42.406  1.00 132.18 ? 177 LYS   A CB  1 
ATOM   1332  C  CG  . LYS   A  1  177 ? 82.843  -74.938  41.927  1.00 135.98 ? 177 LYS   A CG  1 
ATOM   1333  C  CD  . LYS   A  1  177 ? 82.891  -73.882  43.011  1.00 140.94 ? 177 LYS   A CD  1 
ATOM   1334  C  CE  . LYS   A  1  177 ? 82.699  -72.482  42.468  1.00 142.44 ? 177 LYS   A CE  1 
ATOM   1335  N  NZ  . LYS   A  1  177 ? 82.472  -71.500  43.553  1.00 146.07 ? 177 LYS   A NZ  1 
ATOM   1336  N  N   . ARG   A  1  178 ? 83.475  -79.611  42.411  1.00 122.82 ? 178 ARG   A N   1 
ATOM   1337  C  CA  . ARG   A  1  178 ? 84.241  -80.691  43.094  1.00 126.40 ? 178 ARG   A CA  1 
ATOM   1338  C  C   . ARG   A  1  178 ? 84.274  -81.991  42.275  1.00 123.06 ? 178 ARG   A C   1 
ATOM   1339  O  O   . ARG   A  1  178 ? 85.225  -82.767  42.487  1.00 123.11 ? 178 ARG   A O   1 
ATOM   1340  C  CB  . ARG   A  1  178 ? 83.654  -80.980  44.479  1.00 127.17 ? 178 ARG   A CB  1 
ATOM   1341  C  CG  . ARG   A  1  178 ? 83.540  -79.763  45.384  1.00 128.90 ? 178 ARG   A CG  1 
ATOM   1342  C  CD  . ARG   A  1  178 ? 84.852  -79.024  45.559  1.00 133.60 ? 178 ARG   A CD  1 
ATOM   1343  N  NE  . ARG   A  1  178 ? 84.957  -78.422  46.881  1.00 138.43 ? 178 ARG   A NE  1 
ATOM   1344  C  CZ  . ARG   A  1  178 ? 85.511  -78.997  47.947  1.00 142.46 ? 178 ARG   A CZ  1 
ATOM   1345  N  NH1 . ARG   A  1  178 ? 86.033  -80.211  47.870  1.00 142.16 ? 178 ARG   A NH1 1 
ATOM   1346  N  NH2 . ARG   A  1  178 ? 85.543  -78.346  49.098  1.00 143.68 ? 178 ARG   A NH2 1 
ATOM   1347  N  N   . TRP   A  1  179 ? 83.290  -82.246  41.402  1.00 122.45 ? 179 TRP   A N   1 
ATOM   1348  C  CA  . TRP   A  1  179 ? 83.182  -83.531  40.654  1.00 121.34 ? 179 TRP   A CA  1 
ATOM   1349  C  C   . TRP   A  1  179 ? 84.185  -83.567  39.495  1.00 120.90 ? 179 TRP   A C   1 
ATOM   1350  O  O   . TRP   A  1  179 ? 84.232  -82.595  38.715  1.00 124.77 ? 179 TRP   A O   1 
ATOM   1351  C  CB  . TRP   A  1  179 ? 81.759  -83.794  40.143  1.00 120.87 ? 179 TRP   A CB  1 
ATOM   1352  C  CG  . TRP   A  1  179 ? 81.567  -85.207  39.680  1.00 121.31 ? 179 TRP   A CG  1 
ATOM   1353  C  CD1 . TRP   A  1  179 ? 81.137  -86.259  40.434  1.00 121.56 ? 179 TRP   A CD1 1 
ATOM   1354  C  CD2 . TRP   A  1  179 ? 81.837  -85.739  38.369  1.00 123.98 ? 179 TRP   A CD2 1 
ATOM   1355  N  NE1 . TRP   A  1  179 ? 81.106  -87.403  39.684  1.00 121.83 ? 179 TRP   A NE1 1 
ATOM   1356  C  CE2 . TRP   A  1  179 ? 81.531  -87.118  38.414  1.00 123.84 ? 179 TRP   A CE2 1 
ATOM   1357  C  CE3 . TRP   A  1  179 ? 82.298  -85.193  37.165  1.00 125.06 ? 179 TRP   A CE3 1 
ATOM   1358  C  CZ2 . TRP   A  1  179 ? 81.670  -87.950  37.303  1.00 124.29 ? 179 TRP   A CZ2 1 
ATOM   1359  C  CZ3 . TRP   A  1  179 ? 82.436  -86.016  36.067  1.00 126.95 ? 179 TRP   A CZ3 1 
ATOM   1360  C  CH2 . TRP   A  1  179 ? 82.124  -87.375  36.137  1.00 126.67 ? 179 TRP   A CH2 1 
ATOM   1361  N  N   . ASN   A  1  180 ? 84.940  -84.666  39.397  1.00 116.97 ? 180 ASN   A N   1 
ATOM   1362  C  CA  . ASN   A  1  180 ? 85.742  -85.061  38.208  1.00 120.70 ? 180 ASN   A CA  1 
ATOM   1363  C  C   . ASN   A  1  180 ? 85.450  -86.540  37.916  1.00 119.53 ? 180 ASN   A C   1 
ATOM   1364  O  O   . ASN   A  1  180 ? 84.829  -87.198  38.777  1.00 122.13 ? 180 ASN   A O   1 
ATOM   1365  C  CB  . ASN   A  1  180 ? 87.235  -84.774  38.404  1.00 118.64 ? 180 ASN   A CB  1 
ATOM   1366  C  CG  . ASN   A  1  180 ? 87.840  -85.488  39.595  1.00 116.65 ? 180 ASN   A CG  1 
ATOM   1367  O  OD1 . ASN   A  1  180 ? 88.064  -86.695  39.554  1.00 114.73 ? 180 ASN   A OD1 1 
ATOM   1368  N  ND2 . ASN   A  1  180 ? 88.130  -84.753  40.657  1.00 118.85 ? 180 ASN   A ND2 1 
ATOM   1369  N  N   . ASP   A  1  181 ? 85.887  -87.043  36.756  1.00 122.49 ? 181 ASP   A N   1 
ATOM   1370  C  CA  . ASP   A  1  181 ? 85.590  -88.422  36.278  1.00 119.87 ? 181 ASP   A CA  1 
ATOM   1371  C  C   . ASP   A  1  181 ? 86.594  -89.430  36.865  1.00 121.48 ? 181 ASP   A C   1 
ATOM   1372  O  O   . ASP   A  1  181 ? 86.526  -90.612  36.469  1.00 120.73 ? 181 ASP   A O   1 
ATOM   1373  C  CB  . ASP   A  1  181 ? 85.536  -88.478  34.745  1.00 121.11 ? 181 ASP   A CB  1 
ATOM   1374  C  CG  . ASP   A  1  181 ? 86.824  -88.101  34.026  1.00 121.31 ? 181 ASP   A CG  1 
ATOM   1375  O  OD1 . ASP   A  1  181 ? 87.833  -87.839  34.711  1.00 125.80 ? 181 ASP   A OD1 1 
ATOM   1376  O  OD2 . ASP   A  1  181 ? 86.805  -88.068  32.780  1.00 121.78 ? 181 ASP   A OD2 1 
ATOM   1377  N  N   . GLU   A  1  182 ? 87.472  -88.997  37.780  1.00 118.31 ? 182 GLU   A N   1 
ATOM   1378  C  CA  . GLU   A  1  182 ? 88.526  -89.840  38.415  1.00 119.34 ? 182 GLU   A CA  1 
ATOM   1379  C  C   . GLU   A  1  182 ? 88.281  -89.969  39.926  1.00 116.87 ? 182 GLU   A C   1 
ATOM   1380  O  O   . GLU   A  1  182 ? 89.196  -90.461  40.619  1.00 115.59 ? 182 GLU   A O   1 
ATOM   1381  C  CB  . GLU   A  1  182 ? 89.912  -89.244  38.145  1.00 120.40 ? 182 GLU   A CB  1 
ATOM   1382  C  CG  . GLU   A  1  182 ? 90.528  -89.700  36.834  1.00 120.81 ? 182 GLU   A CG  1 
ATOM   1383  C  CD  . GLU   A  1  182 ? 91.667  -88.827  36.331  1.00 122.18 ? 182 GLU   A CD  1 
ATOM   1384  O  OE1 . GLU   A  1  182 ? 91.410  -87.651  36.009  1.00 125.25 ? 182 GLU   A OE1 1 
ATOM   1385  O  OE2 . GLU   A  1  182 ? 92.809  -89.321  36.268  1.00 121.51 ? 182 GLU   A OE2 1 
ATOM   1386  N  N   . LEU   A  1  183 ? 87.107  -89.561  40.425  1.00 116.61 ? 183 LEU   A N   1 
ATOM   1387  C  CA  . LEU   A  1  183 ? 86.764  -89.639  41.873  1.00 116.79 ? 183 LEU   A CA  1 
ATOM   1388  C  C   . LEU   A  1  183 ? 86.686  -91.109  42.295  1.00 116.51 ? 183 LEU   A C   1 
ATOM   1389  O  O   . LEU   A  1  183 ? 85.999  -91.892  41.608  1.00 116.88 ? 183 LEU   A O   1 
ATOM   1390  C  CB  . LEU   A  1  183 ? 85.430  -88.939  42.156  1.00 114.79 ? 183 LEU   A CB  1 
ATOM   1391  C  CG  . LEU   A  1  183 ? 85.458  -87.413  42.198  1.00 115.79 ? 183 LEU   A CG  1 
ATOM   1392  C  CD1 . LEU   A  1  183 ? 84.052  -86.873  42.402  1.00 115.06 ? 183 LEU   A CD1 1 
ATOM   1393  C  CD2 . LEU   A  1  183 ? 86.382  -86.897  43.293  1.00 116.61 ? 183 LEU   A CD2 1 
ATOM   1394  N  N   . GLU   A  1  184 ? 87.373  -91.451  43.387  1.00 119.54 ? 184 GLU   A N   1 
ATOM   1395  C  CA  . GLU   A  1  184 ? 87.289  -92.767  44.071  1.00 118.19 ? 184 GLU   A CA  1 
ATOM   1396  C  C   . GLU   A  1  184 ? 86.142  -92.678  45.084  1.00 115.73 ? 184 GLU   A C   1 
ATOM   1397  O  O   . GLU   A  1  184 ? 85.824  -91.548  45.501  1.00 115.84 ? 184 GLU   A O   1 
ATOM   1398  C  CB  . GLU   A  1  184 ? 88.644  -93.090  44.705  1.00 120.13 ? 184 GLU   A CB  1 
ATOM   1399  C  CG  . GLU   A  1  184 ? 88.897  -94.572  44.899  1.00 122.67 ? 184 GLU   A CG  1 
ATOM   1400  C  CD  . GLU   A  1  184 ? 88.672  -95.071  46.316  1.00 126.86 ? 184 GLU   A CD  1 
ATOM   1401  O  OE1 . GLU   A  1  184 ? 89.224  -94.455  47.251  1.00 131.24 ? 184 GLU   A OE1 1 
ATOM   1402  O  OE2 . GLU   A  1  184 ? 87.944  -96.071  46.483  1.00 130.38 ? 184 GLU   A OE2 1 
ATOM   1403  N  N   . LEU   A  1  185 ? 85.531  -93.810  45.449  1.00 113.37 ? 185 LEU   A N   1 
ATOM   1404  C  CA  . LEU   A  1  185 ? 84.299  -93.853  46.287  1.00 113.13 ? 185 LEU   A CA  1 
ATOM   1405  C  C   . LEU   A  1  185 ? 84.505  -93.047  47.576  1.00 114.97 ? 185 LEU   A C   1 
ATOM   1406  O  O   . LEU   A  1  185 ? 83.564  -92.335  47.970  1.00 120.24 ? 185 LEU   A O   1 
ATOM   1407  C  CB  . LEU   A  1  185 ? 83.925  -95.307  46.599  1.00 111.04 ? 185 LEU   A CB  1 
ATOM   1408  C  CG  . LEU   A  1  185 ? 82.673  -95.499  47.458  1.00 107.82 ? 185 LEU   A CG  1 
ATOM   1409  C  CD1 . LEU   A  1  185 ? 81.464  -94.805  46.847  1.00 105.51 ? 185 LEU   A CD1 1 
ATOM   1410  C  CD2 . LEU   A  1  185 ? 82.381  -96.975  47.666  1.00 108.52 ? 185 LEU   A CD2 1 
ATOM   1411  N  N   . GLU   A  1  186 ? 85.680  -93.152  48.205  1.00 117.24 ? 186 GLU   A N   1 
ATOM   1412  C  CA  . GLU   A  1  186 ? 86.004  -92.450  49.480  1.00 121.10 ? 186 GLU   A CA  1 
ATOM   1413  C  C   . GLU   A  1  186 ? 86.055  -90.934  49.251  1.00 119.78 ? 186 GLU   A C   1 
ATOM   1414  O  O   . GLU   A  1  186 ? 85.688  -90.192  50.182  1.00 118.43 ? 186 GLU   A O   1 
ATOM   1415  C  CB  . GLU   A  1  186 ? 87.321  -92.959  50.072  1.00 124.66 ? 186 GLU   A CB  1 
ATOM   1416  C  CG  . GLU   A  1  186 ? 87.142  -94.152  50.993  1.00 127.84 ? 186 GLU   A CG  1 
ATOM   1417  C  CD  . GLU   A  1  186 ? 86.380  -93.866  52.278  1.00 128.11 ? 186 GLU   A CD  1 
ATOM   1418  O  OE1 . GLU   A  1  186 ? 86.040  -92.688  52.526  1.00 129.65 ? 186 GLU   A OE1 1 
ATOM   1419  O  OE2 . GLU   A  1  186 ? 86.124  -94.826  53.031  1.00 133.51 ? 186 GLU   A OE2 1 
ATOM   1420  N  N   . ASP   A  1  187 ? 86.490  -90.499  48.064  1.00 120.77 ? 187 ASP   A N   1 
ATOM   1421  C  CA  . ASP   A  1  187 ? 86.553  -89.065  47.671  1.00 123.61 ? 187 ASP   A CA  1 
ATOM   1422  C  C   . ASP   A  1  187 ? 85.128  -88.533  47.468  1.00 122.51 ? 187 ASP   A C   1 
ATOM   1423  O  O   . ASP   A  1  187 ? 84.892  -87.353  47.797  1.00 126.79 ? 187 ASP   A O   1 
ATOM   1424  C  CB  . ASP   A  1  187 ? 87.427  -88.866  46.428  1.00 123.94 ? 187 ASP   A CB  1 
ATOM   1425  C  CG  . ASP   A  1  187 ? 88.855  -89.362  46.592  1.00 124.73 ? 187 ASP   A CG  1 
ATOM   1426  O  OD1 . ASP   A  1  187 ? 89.410  -89.196  47.697  1.00 131.36 ? 187 ASP   A OD1 1 
ATOM   1427  O  OD2 . ASP   A  1  187 ? 89.399  -89.915  45.616  1.00 117.98 ? 187 ASP   A OD2 1 
ATOM   1428  N  N   . ALA   A  1  188 ? 84.216  -89.370  46.957  1.00 119.07 ? 188 ALA   A N   1 
ATOM   1429  C  CA  . ALA   A  1  188 ? 82.795  -89.026  46.705  1.00 114.99 ? 188 ALA   A CA  1 
ATOM   1430  C  C   . ALA   A  1  188 ? 82.038  -88.904  48.033  1.00 109.36 ? 188 ALA   A C   1 
ATOM   1431  O  O   . ALA   A  1  188 ? 81.188  -88.001  48.134  1.00 106.58 ? 188 ALA   A O   1 
ATOM   1432  C  CB  . ALA   A  1  188 ? 82.156  -90.052  45.799  1.00 116.82 ? 188 ALA   A CB  1 
ATOM   1433  N  N   . ILE   A  1  189 ? 82.324  -89.782  49.004  1.00 111.06 ? 189 ILE   A N   1 
ATOM   1434  C  CA  . ILE   A  1  189 ? 81.712  -89.754  50.370  1.00 111.14 ? 189 ILE   A CA  1 
ATOM   1435  C  C   . ILE   A  1  189 ? 82.118  -88.441  51.051  1.00 111.11 ? 189 ILE   A C   1 
ATOM   1436  O  O   . ILE   A  1  189 ? 81.250  -87.804  51.680  1.00 109.05 ? 189 ILE   A O   1 
ATOM   1437  C  CB  . ILE   A  1  189 ? 82.125  -90.977  51.219  1.00 113.12 ? 189 ILE   A CB  1 
ATOM   1438  C  CG1 . ILE   A  1  189 ? 81.613  -92.295  50.630  1.00 110.35 ? 189 ILE   A CG1 1 
ATOM   1439  C  CG2 . ILE   A  1  189 ? 81.667  -90.806  52.662  1.00 113.75 ? 189 ILE   A CG2 1 
ATOM   1440  C  CD1 . ILE   A  1  189 ? 82.282  -93.524  51.205  1.00 110.73 ? 189 ILE   A CD1 1 
ATOM   1441  N  N   . HIS   A  1  190 ? 83.395  -88.069  50.938  1.00 110.68 ? 190 HIS   A N   1 
ATOM   1442  C  CA  . HIS   A  1  190 ? 83.972  -86.832  51.528  1.00 114.11 ? 190 HIS   A CA  1 
ATOM   1443  C  C   . HIS   A  1  190 ? 83.219  -85.606  50.997  1.00 113.16 ? 190 HIS   A C   1 
ATOM   1444  O  O   . HIS   A  1  190 ? 82.877  -84.730  51.813  1.00 116.49 ? 190 HIS   A O   1 
ATOM   1445  C  CB  . HIS   A  1  190 ? 85.479  -86.753  51.250  1.00 118.10 ? 190 HIS   A CB  1 
ATOM   1446  C  CG  . HIS   A  1  190 ? 86.106  -85.497  51.752  1.00 120.77 ? 190 HIS   A CG  1 
ATOM   1447  N  ND1 . HIS   A  1  190 ? 86.375  -85.293  53.091  1.00 122.38 ? 190 HIS   A ND1 1 
ATOM   1448  C  CD2 . HIS   A  1  190 ? 86.504  -84.379  51.108  1.00 123.12 ? 190 HIS   A CD2 1 
ATOM   1449  C  CE1 . HIS   A  1  190 ? 86.920  -84.104  53.250  1.00 125.64 ? 190 HIS   A CE1 1 
ATOM   1450  N  NE2 . HIS   A  1  190 ? 87.010  -83.523  52.048  1.00 126.69 ? 190 HIS   A NE2 1 
ATOM   1451  N  N   . ILE   A  1  191 ? 82.966  -85.560  49.686  1.00 110.44 ? 191 ILE   A N   1 
ATOM   1452  C  CA  . ILE   A  1  191 ? 82.286  -84.423  48.995  1.00 107.96 ? 191 ILE   A CA  1 
ATOM   1453  C  C   . ILE   A  1  191 ? 80.803  -84.415  49.390  1.00 106.50 ? 191 ILE   A C   1 
ATOM   1454  O  O   . ILE   A  1  191 ? 80.254  -83.314  49.572  1.00 104.77 ? 191 ILE   A O   1 
ATOM   1455  C  CB  . ILE   A  1  191 ? 82.493  -84.497  47.467  1.00 109.00 ? 191 ILE   A CB  1 
ATOM   1456  C  CG1 . ILE   A  1  191 ? 83.970  -84.332  47.097  1.00 110.36 ? 191 ILE   A CG1 1 
ATOM   1457  C  CG2 . ILE   A  1  191 ? 81.624  -83.477  46.744  1.00 109.25 ? 191 ILE   A CG2 1 
ATOM   1458  C  CD1 . ILE   A  1  191 ? 84.328  -84.850  45.725  1.00 111.16 ? 191 ILE   A CD1 1 
ATOM   1459  N  N   . ALA   A  1  192 ? 80.185  -85.593  49.518  1.00 104.92 ? 192 ALA   A N   1 
ATOM   1460  C  CA  . ALA   A  1  192 ? 78.766  -85.764  49.911  1.00 103.81 ? 192 ALA   A CA  1 
ATOM   1461  C  C   . ALA   A  1  192 ? 78.535  -85.144  51.294  1.00 102.25 ? 192 ALA   A C   1 
ATOM   1462  O  O   . ALA   A  1  192 ? 77.498  -84.479  51.473  1.00 101.39 ? 192 ALA   A O   1 
ATOM   1463  C  CB  . ALA   A  1  192 ? 78.386  -87.225  49.896  1.00 102.39 ? 192 ALA   A CB  1 
ATOM   1464  N  N   . LEU   A  1  193 ? 79.465  -85.358  52.230  1.00 102.95 ? 193 LEU   A N   1 
ATOM   1465  C  CA  . LEU   A  1  193 ? 79.385  -84.832  53.620  1.00 106.23 ? 193 LEU   A CA  1 
ATOM   1466  C  C   . LEU   A  1  193 ? 79.595  -83.312  53.617  1.00 108.46 ? 193 LEU   A C   1 
ATOM   1467  O  O   . LEU   A  1  193 ? 78.862  -82.623  54.352  1.00 111.91 ? 193 LEU   A O   1 
ATOM   1468  C  CB  . LEU   A  1  193 ? 80.428  -85.533  54.494  1.00 107.41 ? 193 LEU   A CB  1 
ATOM   1469  C  CG  . LEU   A  1  193 ? 80.147  -87.001  54.812  1.00 106.19 ? 193 LEU   A CG  1 
ATOM   1470  C  CD1 . LEU   A  1  193 ? 81.380  -87.665  55.405  1.00 107.95 ? 193 LEU   A CD1 1 
ATOM   1471  C  CD2 . LEU   A  1  193 ? 78.960  -87.142  55.755  1.00 103.81 ? 193 LEU   A CD2 1 
ATOM   1472  N  N   . LEU   A  1  194 ? 80.560  -82.814  52.834  1.00 111.20 ? 194 LEU   A N   1 
ATOM   1473  C  CA  . LEU   A  1  194 ? 80.841  -81.359  52.680  1.00 111.52 ? 194 LEU   A CA  1 
ATOM   1474  C  C   . LEU   A  1  194 ? 79.589  -80.655  52.144  1.00 113.72 ? 194 LEU   A C   1 
ATOM   1475  O  O   . LEU   A  1  194 ? 79.183  -79.641  52.751  1.00 116.38 ? 194 LEU   A O   1 
ATOM   1476  C  CB  . LEU   A  1  194 ? 82.026  -81.146  51.731  1.00 112.83 ? 194 LEU   A CB  1 
ATOM   1477  C  CG  . LEU   A  1  194 ? 83.416  -81.236  52.360  1.00 114.03 ? 194 LEU   A CG  1 
ATOM   1478  C  CD1 . LEU   A  1  194 ? 84.479  -81.407  51.287  1.00 114.48 ? 194 LEU   A CD1 1 
ATOM   1479  C  CD2 . LEU   A  1  194 ? 83.713  -80.006  53.205  1.00 115.14 ? 194 LEU   A CD2 1 
ATOM   1480  N  N   . THR   A  1  195 ? 79.005  -81.179  51.059  1.00 109.03 ? 195 THR   A N   1 
ATOM   1481  C  CA  . THR   A  1  195 ? 77.849  -80.581  50.336  1.00 109.36 ? 195 THR   A CA  1 
ATOM   1482  C  C   . THR   A  1  195 ? 76.621  -80.532  51.250  1.00 109.69 ? 195 THR   A C   1 
ATOM   1483  O  O   . THR   A  1  195 ? 75.866  -79.544  51.165  1.00 111.05 ? 195 THR   A O   1 
ATOM   1484  C  CB  . THR   A  1  195 ? 77.499  -81.354  49.059  1.00 106.76 ? 195 THR   A CB  1 
ATOM   1485  O  OG1 . THR   A  1  195 ? 78.709  -81.619  48.351  1.00 108.11 ? 195 THR   A OG1 1 
ATOM   1486  C  CG2 . THR   A  1  195 ? 76.536  -80.597  48.169  1.00 106.78 ? 195 THR   A CG2 1 
ATOM   1487  N  N   . LEU   A  1  196 ? 76.432  -81.558  52.082  1.00 109.49 ? 196 LEU   A N   1 
ATOM   1488  C  CA  . LEU   A  1  196 ? 75.230  -81.705  52.946  1.00 110.10 ? 196 LEU   A CA  1 
ATOM   1489  C  C   . LEU   A  1  196 ? 75.304  -80.708  54.110  1.00 110.76 ? 196 LEU   A C   1 
ATOM   1490  O  O   . LEU   A  1  196 ? 74.236  -80.216  54.513  1.00 113.45 ? 196 LEU   A O   1 
ATOM   1491  C  CB  . LEU   A  1  196 ? 75.138  -83.153  53.445  1.00 109.33 ? 196 LEU   A CB  1 
ATOM   1492  C  CG  . LEU   A  1  196 ? 73.733  -83.674  53.749  1.00 107.26 ? 196 LEU   A CG  1 
ATOM   1493  C  CD1 . LEU   A  1  196 ? 72.794  -83.499  52.562  1.00 107.06 ? 196 LEU   A CD1 1 
ATOM   1494  C  CD2 . LEU   A  1  196 ? 73.795  -85.137  54.155  1.00 106.74 ? 196 LEU   A CD2 1 
ATOM   1495  N  N   . LYS   A  1  197 ? 76.509  -80.410  54.611  1.00 111.70 ? 197 LYS   A N   1 
ATOM   1496  C  CA  . LYS   A  1  197 ? 76.736  -79.478  55.752  1.00 114.51 ? 197 LYS   A CA  1 
ATOM   1497  C  C   . LYS   A  1  197 ? 76.189  -78.083  55.414  1.00 118.06 ? 197 LYS   A C   1 
ATOM   1498  O  O   . LYS   A  1  197 ? 75.673  -77.422  56.336  1.00 121.57 ? 197 LYS   A O   1 
ATOM   1499  C  CB  . LYS   A  1  197 ? 78.222  -79.403  56.115  1.00 114.40 ? 197 LYS   A CB  1 
ATOM   1500  C  CG  . LYS   A  1  197 ? 78.525  -78.582  57.361  1.00 117.17 ? 197 LYS   A CG  1 
ATOM   1501  C  CD  . LYS   A  1  197 ? 79.996  -78.466  57.680  1.00 120.52 ? 197 LYS   A CD  1 
ATOM   1502  C  CE  . LYS   A  1  197 ? 80.540  -79.675  58.407  1.00 121.14 ? 197 LYS   A CE  1 
ATOM   1503  N  NZ  . LYS   A  1  197 ? 81.927  -79.442  58.873  1.00 125.74 ? 197 LYS   A NZ  1 
ATOM   1504  N  N   . GLU   A  1  198 ? 76.294  -77.655  54.151  1.00 120.89 ? 198 GLU   A N   1 
ATOM   1505  C  CA  . GLU   A  1  198 ? 75.828  -76.321  53.679  1.00 126.76 ? 198 GLU   A CA  1 
ATOM   1506  C  C   . GLU   A  1  198 ? 74.315  -76.195  53.910  1.00 125.91 ? 198 GLU   A C   1 
ATOM   1507  O  O   . GLU   A  1  198 ? 73.880  -75.120  54.368  1.00 128.75 ? 198 GLU   A O   1 
ATOM   1508  C  CB  . GLU   A  1  198 ? 76.165  -76.106  52.199  1.00 129.92 ? 198 GLU   A CB  1 
ATOM   1509  C  CG  . GLU   A  1  198 ? 77.651  -76.177  51.876  1.00 132.21 ? 198 GLU   A CG  1 
ATOM   1510  C  CD  . GLU   A  1  198 ? 78.507  -75.102  52.523  1.00 134.06 ? 198 GLU   A CD  1 
ATOM   1511  O  OE1 . GLU   A  1  198 ? 78.314  -73.915  52.194  1.00 138.84 ? 198 GLU   A OE1 1 
ATOM   1512  O  OE2 . GLU   A  1  198 ? 79.364  -75.456  53.356  1.00 135.14 ? 198 GLU   A OE2 1 
ATOM   1513  N  N   . SER   A  1  199 ? 73.551  -77.252  53.610  1.00 122.70 ? 199 SER   A N   1 
ATOM   1514  C  CA  . SER   A  1  199 ? 72.062  -77.270  53.644  1.00 123.91 ? 199 SER   A CA  1 
ATOM   1515  C  C   . SER   A  1  199 ? 71.539  -77.668  55.033  1.00 121.64 ? 199 SER   A C   1 
ATOM   1516  O  O   . SER   A  1  199 ? 70.351  -77.406  55.300  1.00 118.36 ? 199 SER   A O   1 
ATOM   1517  C  CB  . SER   A  1  199 ? 71.501  -78.172  52.568  1.00 124.52 ? 199 SER   A CB  1 
ATOM   1518  O  OG  . SER   A  1  199 ? 72.070  -79.472  52.635  1.00 122.97 ? 199 SER   A OG  1 
ATOM   1519  N  N   . VAL   A  1  200 ? 72.371  -78.284  55.880  1.00 122.74 ? 200 VAL   A N   1 
ATOM   1520  C  CA  . VAL   A  1  200 ? 71.992  -78.683  57.271  1.00 126.52 ? 200 VAL   A CA  1 
ATOM   1521  C  C   . VAL   A  1  200 ? 72.290  -77.509  58.205  1.00 131.76 ? 200 VAL   A C   1 
ATOM   1522  O  O   . VAL   A  1  200 ? 73.390  -76.934  58.095  1.00 137.08 ? 200 VAL   A O   1 
ATOM   1523  C  CB  . VAL   A  1  200 ? 72.718  -79.960  57.737  1.00 123.58 ? 200 VAL   A CB  1 
ATOM   1524  C  CG1 . VAL   A  1  200 ? 72.400  -80.282  59.190  1.00 123.59 ? 200 VAL   A CG1 1 
ATOM   1525  C  CG2 . VAL   A  1  200 ? 72.391  -81.151  56.850  1.00 121.92 ? 200 VAL   A CG2 1 
ATOM   1526  N  N   . GLU   A  1  201 ? 71.351  -77.192  59.102  1.00 137.26 ? 201 GLU   A N   1 
ATOM   1527  C  CA  . GLU   A  1  201 ? 71.406  -76.003  59.994  1.00 139.73 ? 201 GLU   A CA  1 
ATOM   1528  C  C   . GLU   A  1  201 ? 71.845  -76.426  61.399  1.00 136.35 ? 201 GLU   A C   1 
ATOM   1529  O  O   . GLU   A  1  201 ? 72.830  -75.847  61.903  1.00 127.99 ? 201 GLU   A O   1 
ATOM   1530  C  CB  . GLU   A  1  201 ? 70.045  -75.305  60.027  1.00 145.02 ? 201 GLU   A CB  1 
ATOM   1531  C  CG  . GLU   A  1  201 ? 70.123  -73.869  60.512  1.00 150.04 ? 201 GLU   A CG  1 
ATOM   1532  C  CD  . GLU   A  1  201 ? 69.129  -72.929  59.855  1.00 155.32 ? 201 GLU   A CD  1 
ATOM   1533  O  OE1 . GLU   A  1  201 ? 69.564  -71.869  59.369  1.00 157.30 ? 201 GLU   A OE1 1 
ATOM   1534  O  OE2 . GLU   A  1  201 ? 67.927  -73.262  59.826  1.00 158.89 ? 201 GLU   A OE2 1 
ATOM   1535  N  N   . GLY   A  1  202 ? 71.141  -77.395  61.995  1.00 137.13 ? 202 GLY   A N   1 
ATOM   1536  C  CA  . GLY   A  1  202 ? 71.329  -77.827  63.395  1.00 129.04 ? 202 GLY   A CA  1 
ATOM   1537  C  C   . GLY   A  1  202 ? 72.504  -78.775  63.554  1.00 122.27 ? 202 GLY   A C   1 
ATOM   1538  O  O   . GLY   A  1  202 ? 73.587  -78.476  63.014  1.00 119.38 ? 202 GLY   A O   1 
ATOM   1539  N  N   . GLU   A  1  203 ? 72.297  -79.880  64.276  1.00 120.74 ? 203 GLU   A N   1 
ATOM   1540  C  CA  . GLU   A  1  203 ? 73.341  -80.897  64.580  1.00 121.65 ? 203 GLU   A CA  1 
ATOM   1541  C  C   . GLU   A  1  203 ? 73.760  -81.592  63.282  1.00 121.27 ? 203 GLU   A C   1 
ATOM   1542  O  O   . GLU   A  1  203 ? 72.865  -81.922  62.477  1.00 123.78 ? 203 GLU   A O   1 
ATOM   1543  C  CB  . GLU   A  1  203 ? 72.821  -81.939  65.572  1.00 122.36 ? 203 GLU   A CB  1 
ATOM   1544  C  CG  . GLU   A  1  203 ? 72.340  -81.363  66.892  1.00 126.05 ? 203 GLU   A CG  1 
ATOM   1545  C  CD  . GLU   A  1  203 ? 73.433  -80.799  67.785  1.00 128.93 ? 203 GLU   A CD  1 
ATOM   1546  O  OE1 . GLU   A  1  203 ? 73.620  -81.335  68.895  1.00 130.27 ? 203 GLU   A OE1 1 
ATOM   1547  O  OE2 . GLU   A  1  203 ? 74.088  -79.820  67.377  1.00 130.99 ? 203 GLU   A OE2 1 
ATOM   1548  N  N   . PHE   A  1  204 ? 75.067  -81.803  63.093  1.00 118.26 ? 204 PHE   A N   1 
ATOM   1549  C  CA  . PHE   A  1  204 ? 75.652  -82.503  61.918  1.00 120.82 ? 204 PHE   A CA  1 
ATOM   1550  C  C   . PHE   A  1  204 ? 76.552  -83.641  62.410  1.00 120.56 ? 204 PHE   A C   1 
ATOM   1551  O  O   . PHE   A  1  204 ? 77.755  -83.415  62.648  1.00 121.36 ? 204 PHE   A O   1 
ATOM   1552  C  CB  . PHE   A  1  204 ? 76.408  -81.525  61.015  1.00 120.57 ? 204 PHE   A CB  1 
ATOM   1553  C  CG  . PHE   A  1  204 ? 76.672  -82.051  59.626  1.00 118.65 ? 204 PHE   A CG  1 
ATOM   1554  C  CD1 . PHE   A  1  204 ? 75.638  -82.165  58.708  1.00 115.03 ? 204 PHE   A CD1 1 
ATOM   1555  C  CD2 . PHE   A  1  204 ? 77.947  -82.429  59.233  1.00 116.91 ? 204 PHE   A CD2 1 
ATOM   1556  C  CE1 . PHE   A  1  204 ? 75.873  -82.640  57.427  1.00 113.31 ? 204 PHE   A CE1 1 
ATOM   1557  C  CE2 . PHE   A  1  204 ? 78.180  -82.906  57.951  1.00 116.40 ? 204 PHE   A CE2 1 
ATOM   1558  C  CZ  . PHE   A  1  204 ? 77.143  -83.013  57.051  1.00 115.18 ? 204 PHE   A CZ  1 
ATOM   1559  N  N   . ASN   A  1  205 ? 75.966  -84.833  62.558  1.00 120.56 ? 205 ASN   A N   1 
ATOM   1560  C  CA  . ASN   A  1  205 ? 76.645  -86.055  63.065  1.00 121.97 ? 205 ASN   A CA  1 
ATOM   1561  C  C   . ASN   A  1  205 ? 76.006  -87.291  62.416  1.00 121.60 ? 205 ASN   A C   1 
ATOM   1562  O  O   . ASN   A  1  205 ? 75.103  -87.116  61.569  1.00 119.40 ? 205 ASN   A O   1 
ATOM   1563  C  CB  . ASN   A  1  205 ? 76.610  -86.102  64.595  1.00 124.10 ? 205 ASN   A CB  1 
ATOM   1564  C  CG  . ASN   A  1  205 ? 75.213  -85.967  65.168  1.00 123.57 ? 205 ASN   A CG  1 
ATOM   1565  O  OD1 . ASN   A  1  205 ? 74.286  -86.642  64.728  1.00 124.67 ? 205 ASN   A OD1 1 
ATOM   1566  N  ND2 . ASN   A  1  205 ? 75.051  -85.103  66.156  1.00 127.08 ? 205 ASN   A ND2 1 
ATOM   1567  N  N   . GLY   A  1  206 ? 76.454  -88.489  62.810  1.00 120.41 ? 206 GLY   A N   1 
ATOM   1568  C  CA  . GLY   A  1  206 ? 76.009  -89.780  62.250  1.00 116.02 ? 206 GLY   A CA  1 
ATOM   1569  C  C   . GLY   A  1  206 ? 74.588  -90.154  62.648  1.00 116.82 ? 206 GLY   A C   1 
ATOM   1570  O  O   . GLY   A  1  206 ? 74.076  -91.151  62.096  1.00 114.16 ? 206 GLY   A O   1 
ATOM   1571  N  N   . ASP   A  1  207 ? 73.972  -89.406  63.572  1.00 115.99 ? 207 ASP   A N   1 
ATOM   1572  C  CA  . ASP   A  1  207 ? 72.593  -89.654  64.077  1.00 116.57 ? 207 ASP   A CA  1 
ATOM   1573  C  C   . ASP   A  1  207 ? 71.586  -88.749  63.355  1.00 114.69 ? 207 ASP   A C   1 
ATOM   1574  O  O   . ASP   A  1  207 ? 70.385  -89.083  63.383  1.00 116.40 ? 207 ASP   A O   1 
ATOM   1575  C  CB  . ASP   A  1  207 ? 72.526  -89.458  65.593  1.00 118.83 ? 207 ASP   A CB  1 
ATOM   1576  C  CG  . ASP   A  1  207 ? 73.376  -90.450  66.370  1.00 120.82 ? 207 ASP   A CG  1 
ATOM   1577  O  OD1 . ASP   A  1  207 ? 73.174  -91.666  66.179  1.00 127.10 ? 207 ASP   A OD1 1 
ATOM   1578  O  OD2 . ASP   A  1  207 ? 74.239  -90.001  67.151  1.00 116.21 ? 207 ASP   A OD2 1 
ATOM   1579  N  N   . THR   A  1  208 ? 72.048  -87.649  62.747  1.00 114.99 ? 208 THR   A N   1 
ATOM   1580  C  CA  . THR   A  1  208 ? 71.208  -86.669  62.003  1.00 115.29 ? 208 THR   A CA  1 
ATOM   1581  C  C   . THR   A  1  208 ? 71.413  -86.820  60.492  1.00 109.23 ? 208 THR   A C   1 
ATOM   1582  O  O   . THR   A  1  208 ? 70.628  -86.215  59.739  1.00 105.54 ? 208 THR   A O   1 
ATOM   1583  C  CB  . THR   A  1  208 ? 71.512  -85.233  62.446  1.00 119.04 ? 208 THR   A CB  1 
ATOM   1584  O  OG1 . THR   A  1  208 ? 72.918  -85.017  62.326  1.00 123.27 ? 208 THR   A OG1 1 
ATOM   1585  C  CG2 . THR   A  1  208 ? 71.067  -84.961  63.866  1.00 121.20 ? 208 THR   A CG2 1 
ATOM   1586  N  N   . ILE   A  1  209 ? 72.425  -87.586  60.072  1.00 106.61 ? 209 ILE   A N   1 
ATOM   1587  C  CA  . ILE   A  1  209 ? 72.754  -87.840  58.639  1.00 108.22 ? 209 ILE   A CA  1 
ATOM   1588  C  C   . ILE   A  1  209 ? 72.502  -89.320  58.340  1.00 104.53 ? 209 ILE   A C   1 
ATOM   1589  O  O   . ILE   A  1  209 ? 72.887  -90.171  59.164  1.00 104.54 ? 209 ILE   A O   1 
ATOM   1590  C  CB  . ILE   A  1  209 ? 74.203  -87.406  58.326  1.00 108.91 ? 209 ILE   A CB  1 
ATOM   1591  C  CG1 . ILE   A  1  209 ? 74.413  -85.912  58.588  1.00 114.97 ? 209 ILE   A CG1 1 
ATOM   1592  C  CG2 . ILE   A  1  209 ? 74.601  -87.780  56.906  1.00 109.82 ? 209 ILE   A CG2 1 
ATOM   1593  C  CD1 . ILE   A  1  209 ? 73.420  -85.007  57.884  1.00 118.14 ? 209 ILE   A CD1 1 
ATOM   1594  N  N   . GLU   A  1  210 ? 71.851  -89.596  57.207  1.00 103.68 ? 210 GLU   A N   1 
ATOM   1595  C  CA  . GLU   A  1  210 ? 71.626  -90.959  56.661  1.00 104.35 ? 210 GLU   A CA  1 
ATOM   1596  C  C   . GLU   A  1  210 ? 72.371  -91.056  55.329  1.00 104.45 ? 210 GLU   A C   1 
ATOM   1597  O  O   . GLU   A  1  210 ? 72.131  -90.199  54.457  1.00 102.95 ? 210 GLU   A O   1 
ATOM   1598  C  CB  . GLU   A  1  210 ? 70.130  -91.220  56.488  1.00 105.41 ? 210 GLU   A CB  1 
ATOM   1599  C  CG  . GLU   A  1  210 ? 69.766  -92.690  56.542  1.00 108.01 ? 210 GLU   A CG  1 
ATOM   1600  C  CD  . GLU   A  1  210 ? 68.273  -92.967  56.582  1.00 113.16 ? 210 GLU   A CD  1 
ATOM   1601  O  OE1 . GLU   A  1  210 ? 67.838  -93.953  55.950  1.00 118.38 ? 210 GLU   A OE1 1 
ATOM   1602  O  OE2 . GLU   A  1  210 ? 67.546  -92.201  57.249  1.00 115.60 ? 210 GLU   A OE2 1 
ATOM   1603  N  N   . LEU   A  1  211 ? 73.246  -92.051  55.186  1.00 103.81 ? 211 LEU   A N   1 
ATOM   1604  C  CA  . LEU   A  1  211 ? 74.165  -92.178  54.026  1.00 105.74 ? 211 LEU   A CA  1 
ATOM   1605  C  C   . LEU   A  1  211 ? 74.405  -93.661  53.728  1.00 104.54 ? 211 LEU   A C   1 
ATOM   1606  O  O   . LEU   A  1  211 ? 74.763  -94.398  54.667  1.00 103.91 ? 211 LEU   A O   1 
ATOM   1607  C  CB  . LEU   A  1  211 ? 75.469  -91.447  54.363  1.00 107.82 ? 211 LEU   A CB  1 
ATOM   1608  C  CG  . LEU   A  1  211 ? 76.377  -91.122  53.177  1.00 111.09 ? 211 LEU   A CG  1 
ATOM   1609  C  CD1 . LEU   A  1  211 ? 77.187  -89.861  53.441  1.00 112.46 ? 211 LEU   A CD1 1 
ATOM   1610  C  CD2 . LEU   A  1  211 ? 77.300  -92.288  52.855  1.00 112.66 ? 211 LEU   A CD2 1 
ATOM   1611  N  N   . ALA   A  1  212 ? 74.206  -94.065  52.468  1.00 103.87 ? 212 ALA   A N   1 
ATOM   1612  C  CA  . ALA   A  1  212 ? 74.431  -95.440  51.963  1.00 102.06 ? 212 ALA   A CA  1 
ATOM   1613  C  C   . ALA   A  1  212 ? 75.283  -95.390  50.693  1.00 99.59  ? 212 ALA   A C   1 
ATOM   1614  O  O   . ALA   A  1  212 ? 75.275  -94.345  50.009  1.00 98.94  ? 212 ALA   A O   1 
ATOM   1615  C  CB  . ALA   A  1  212 ? 73.112  -96.121  51.701  1.00 103.86 ? 212 ALA   A CB  1 
ATOM   1616  N  N   . ILE   A  1  213 ? 75.973  -96.492  50.390  1.00 98.27  ? 213 ILE   A N   1 
ATOM   1617  C  CA  . ILE   A  1  213 ? 76.872  -96.619  49.206  1.00 97.04  ? 213 ILE   A CA  1 
ATOM   1618  C  C   . ILE   A  1  213 ? 76.454  -97.835  48.371  1.00 93.13  ? 213 ILE   A C   1 
ATOM   1619  O  O   . ILE   A  1  213 ? 75.880  -98.790  48.929  1.00 90.71  ? 213 ILE   A O   1 
ATOM   1620  C  CB  . ILE   A  1  213 ? 78.354  -96.693  49.634  1.00 99.16  ? 213 ILE   A CB  1 
ATOM   1621  C  CG1 . ILE   A  1  213 ? 78.635  -97.861  50.583  1.00 100.12 ? 213 ILE   A CG1 1 
ATOM   1622  C  CG2 . ILE   A  1  213 ? 78.799  -95.371  50.237  1.00 101.00 ? 213 ILE   A CG2 1 
ATOM   1623  C  CD1 . ILE   A  1  213 ? 79.982  -98.510  50.366  1.00 103.17 ? 213 ILE   A CD1 1 
ATOM   1624  N  N   . ILE   A  1  214 ? 76.711  -97.758  47.066  1.00 91.43  ? 214 ILE   A N   1 
ATOM   1625  C  CA  . ILE   A  1  214 ? 76.742  -98.904  46.112  1.00 91.13  ? 214 ILE   A CA  1 
ATOM   1626  C  C   . ILE   A  1  214 ? 78.207  -99.088  45.709  1.00 95.76  ? 214 ILE   A C   1 
ATOM   1627  O  O   . ILE   A  1  214 ? 78.721  -98.214  44.989  1.00 96.63  ? 214 ILE   A O   1 
ATOM   1628  C  CB  . ILE   A  1  214 ? 75.845  -98.626  44.889  1.00 86.95  ? 214 ILE   A CB  1 
ATOM   1629  C  CG1 . ILE   A  1  214 ? 74.442  -98.162  45.292  1.00 86.30  ? 214 ILE   A CG1 1 
ATOM   1630  C  CG2 . ILE   A  1  214 ? 75.805  -99.830  43.964  1.00 85.16  ? 214 ILE   A CG2 1 
ATOM   1631  C  CD1 . ILE   A  1  214 ? 73.685  -99.133  46.164  1.00 86.16  ? 214 ILE   A CD1 1 
ATOM   1632  N  N   . GLY   A  1  215 ? 78.859  -100.152 46.185  1.00 97.69  ? 215 GLY   A N   1 
ATOM   1633  C  CA  . GLY   A  1  215 ? 80.303  -100.375 45.976  1.00 101.05 ? 215 GLY   A CA  1 
ATOM   1634  C  C   . GLY   A  1  215 ? 80.627  -101.836 45.735  1.00 101.11 ? 215 GLY   A C   1 
ATOM   1635  O  O   . GLY   A  1  215 ? 79.942  -102.469 44.910  1.00 95.49  ? 215 GLY   A O   1 
ATOM   1636  N  N   . ASP   A  1  216 ? 81.646  -102.346 46.430  1.00 104.60 ? 216 ASP   A N   1 
ATOM   1637  C  CA  . ASP   A  1  216 ? 82.121  -103.748 46.317  1.00 107.19 ? 216 ASP   A CA  1 
ATOM   1638  C  C   . ASP   A  1  216 ? 81.046  -104.682 46.878  1.00 108.90 ? 216 ASP   A C   1 
ATOM   1639  O  O   . ASP   A  1  216 ? 80.208  -104.212 47.676  1.00 111.25 ? 216 ASP   A O   1 
ATOM   1640  C  CB  . ASP   A  1  216 ? 83.454  -103.946 47.046  1.00 108.71 ? 216 ASP   A CB  1 
ATOM   1641  C  CG  . ASP   A  1  216 ? 84.640  -103.295 46.358  1.00 113.01 ? 216 ASP   A CG  1 
ATOM   1642  O  OD1 . ASP   A  1  216 ? 84.460  -102.775 45.238  1.00 116.03 ? 216 ASP   A OD1 1 
ATOM   1643  O  OD2 . ASP   A  1  216 ? 85.737  -103.316 46.949  1.00 117.20 ? 216 ASP   A OD2 1 
ATOM   1644  N  N   . GLU   A  1  217 ? 81.076  -105.951 46.461  1.00 111.49 ? 217 GLU   A N   1 
ATOM   1645  C  CA  . GLU   A  1  217 ? 80.230  -107.039 47.020  1.00 109.83 ? 217 GLU   A CA  1 
ATOM   1646  C  C   . GLU   A  1  217 ? 80.650  -107.269 48.476  1.00 104.35 ? 217 GLU   A C   1 
ATOM   1647  O  O   . GLU   A  1  217 ? 81.866  -107.237 48.747  1.00 102.17 ? 217 GLU   A O   1 
ATOM   1648  C  CB  . GLU   A  1  217 ? 80.377  -108.314 46.187  1.00 110.89 ? 217 GLU   A CB  1 
ATOM   1649  C  CG  . GLU   A  1  217 ? 79.844  -108.185 44.770  1.00 113.20 ? 217 GLU   A CG  1 
ATOM   1650  C  CD  . GLU   A  1  217 ? 80.383  -109.209 43.784  1.00 114.24 ? 217 GLU   A CD  1 
ATOM   1651  O  OE1 . GLU   A  1  217 ? 79.586  -109.722 42.973  1.00 117.48 ? 217 GLU   A OE1 1 
ATOM   1652  O  OE2 . GLU   A  1  217 ? 81.599  -109.485 43.818  1.00 115.42 ? 217 GLU   A OE2 1 
ATOM   1653  N  N   . ASN   A  1  218 ? 79.679  -107.472 49.372  1.00 105.77 ? 218 ASN   A N   1 
ATOM   1654  C  CA  . ASN   A  1  218 ? 79.895  -107.681 50.829  1.00 110.42 ? 218 ASN   A CA  1 
ATOM   1655  C  C   . ASN   A  1  218 ? 79.552  -109.128 51.174  1.00 110.36 ? 218 ASN   A C   1 
ATOM   1656  O  O   . ASN   A  1  218 ? 78.415  -109.418 51.545  1.00 111.60 ? 218 ASN   A O   1 
ATOM   1657  C  CB  . ASN   A  1  218 ? 79.062  -106.709 51.670  1.00 112.66 ? 218 ASN   A CB  1 
ATOM   1658  C  CG  . ASN   A  1  218 ? 79.466  -105.259 51.497  1.00 116.74 ? 218 ASN   A CG  1 
ATOM   1659  O  OD1 . ASN   A  1  218 ? 80.087  -104.675 52.382  1.00 122.03 ? 218 ASN   A OD1 1 
ATOM   1660  N  ND2 . ASN   A  1  218 ? 79.112  -104.666 50.367  1.00 116.13 ? 218 ASN   A ND2 1 
ATOM   1661  N  N   . PRO   A  1  219 ? 80.508  -110.084 51.064  1.00 109.27 ? 219 PRO   A N   1 
ATOM   1662  C  CA  . PRO   A  1  219 ? 80.229  -111.487 51.369  1.00 108.47 ? 219 PRO   A CA  1 
ATOM   1663  C  C   . PRO   A  1  219 ? 79.757  -111.681 52.819  1.00 108.22 ? 219 PRO   A C   1 
ATOM   1664  O  O   . PRO   A  1  219 ? 78.920  -112.535 53.044  1.00 109.18 ? 219 PRO   A O   1 
ATOM   1665  C  CB  . PRO   A  1  219 ? 81.572  -112.198 51.133  1.00 107.25 ? 219 PRO   A CB  1 
ATOM   1666  C  CG  . PRO   A  1  219 ? 82.340  -111.263 50.227  1.00 108.16 ? 219 PRO   A CG  1 
ATOM   1667  C  CD  . PRO   A  1  219 ? 81.906  -109.877 50.654  1.00 109.04 ? 219 PRO   A CD  1 
ATOM   1668  N  N   . ASP   A  1  220 ? 80.290  -110.878 53.747  1.00 110.45 ? 220 ASP   A N   1 
ATOM   1669  C  CA  . ASP   A  1  220 ? 79.963  -110.918 55.199  1.00 115.51 ? 220 ASP   A CA  1 
ATOM   1670  C  C   . ASP   A  1  220 ? 78.471  -110.617 55.416  1.00 109.09 ? 220 ASP   A C   1 
ATOM   1671  O  O   . ASP   A  1  220 ? 77.919  -111.124 56.412  1.00 110.47 ? 220 ASP   A O   1 
ATOM   1672  C  CB  . ASP   A  1  220 ? 80.860  -109.971 56.006  1.00 123.65 ? 220 ASP   A CB  1 
ATOM   1673  C  CG  . ASP   A  1  220 ? 80.809  -108.511 55.575  1.00 129.43 ? 220 ASP   A CG  1 
ATOM   1674  O  OD1 . ASP   A  1  220 ? 80.984  -108.246 54.366  1.00 137.70 ? 220 ASP   A OD1 1 
ATOM   1675  O  OD2 . ASP   A  1  220 ? 80.602  -107.646 56.452  1.00 136.28 ? 220 ASP   A OD2 1 
ATOM   1676  N  N   . LEU   A  1  221 ? 77.841  -109.842 54.523  1.00 106.23 ? 221 LEU   A N   1 
ATOM   1677  C  CA  . LEU   A  1  221 ? 76.417  -109.413 54.644  1.00 106.42 ? 221 LEU   A CA  1 
ATOM   1678  C  C   . LEU   A  1  221 ? 75.482  -110.372 53.890  1.00 101.20 ? 221 LEU   A C   1 
ATOM   1679  O  O   . LEU   A  1  221 ? 74.266  -110.102 53.884  1.00 99.94  ? 221 LEU   A O   1 
ATOM   1680  C  CB  . LEU   A  1  221 ? 76.267  -107.982 54.109  1.00 108.27 ? 221 LEU   A CB  1 
ATOM   1681  C  CG  . LEU   A  1  221 ? 76.917  -106.873 54.937  1.00 111.42 ? 221 LEU   A CG  1 
ATOM   1682  C  CD1 . LEU   A  1  221 ? 76.777  -105.527 54.239  1.00 111.81 ? 221 LEU   A CD1 1 
ATOM   1683  C  CD2 . LEU   A  1  221 ? 76.321  -106.799 56.337  1.00 114.55 ? 221 LEU   A CD2 1 
ATOM   1684  N  N   . LEU   A  1  222 ? 76.002  -111.453 53.296  1.00 99.34  ? 222 LEU   A N   1 
ATOM   1685  C  CA  . LEU   A  1  222 ? 75.208  -112.386 52.446  1.00 97.37  ? 222 LEU   A CA  1 
ATOM   1686  C  C   . LEU   A  1  222 ? 74.351  -113.312 53.323  1.00 97.72  ? 222 LEU   A C   1 
ATOM   1687  O  O   . LEU   A  1  222 ? 73.201  -113.589 52.923  1.00 91.93  ? 222 LEU   A O   1 
ATOM   1688  C  CB  . LEU   A  1  222 ? 76.152  -113.194 51.550  1.00 97.55  ? 222 LEU   A CB  1 
ATOM   1689  C  CG  . LEU   A  1  222 ? 75.476  -114.132 50.549  1.00 96.02  ? 222 LEU   A CG  1 
ATOM   1690  C  CD1 . LEU   A  1  222 ? 74.473  -113.393 49.675  1.00 96.20  ? 222 LEU   A CD1 1 
ATOM   1691  C  CD2 . LEU   A  1  222 ? 76.512  -114.830 49.683  1.00 95.59  ? 222 LEU   A CD2 1 
ATOM   1692  N  N   . GLY   A  1  223 ? 74.900  -113.790 54.448  1.00 99.73  ? 223 GLY   A N   1 
ATOM   1693  C  CA  . GLY   A  1  223 ? 74.180  -114.593 55.459  1.00 101.32 ? 223 GLY   A CA  1 
ATOM   1694  C  C   . GLY   A  1  223 ? 74.323  -116.096 55.251  1.00 100.44 ? 223 GLY   A C   1 
ATOM   1695  O  O   . GLY   A  1  223 ? 73.683  -116.853 56.014  1.00 97.89  ? 223 GLY   A O   1 
ATOM   1696  N  N   . TYR   A  1  224 ? 75.122  -116.525 54.264  1.00 101.59 ? 224 TYR   A N   1 
ATOM   1697  C  CA  . TYR   A  1  224 ? 75.414  -117.953 53.959  1.00 102.46 ? 224 TYR   A CA  1 
ATOM   1698  C  C   . TYR   A  1  224 ? 76.646  -118.057 53.050  1.00 103.25 ? 224 TYR   A C   1 
ATOM   1699  O  O   . TYR   A  1  224 ? 77.006  -117.061 52.401  1.00 102.54 ? 224 TYR   A O   1 
ATOM   1700  C  CB  . TYR   A  1  224 ? 74.215  -118.614 53.277  1.00 101.90 ? 224 TYR   A CB  1 
ATOM   1701  C  CG  . TYR   A  1  224 ? 73.947  -118.056 51.906  1.00 102.80 ? 224 TYR   A CG  1 
ATOM   1702  C  CD1 . TYR   A  1  224 ? 73.178  -116.918 51.750  1.00 105.37 ? 224 TYR   A CD1 1 
ATOM   1703  C  CD2 . TYR   A  1  224 ? 74.514  -118.620 50.775  1.00 102.52 ? 224 TYR   A CD2 1 
ATOM   1704  C  CE1 . TYR   A  1  224 ? 72.944  -116.370 50.502  1.00 108.71 ? 224 TYR   A CE1 1 
ATOM   1705  C  CE2 . TYR   A  1  224 ? 74.298  -118.082 49.518  1.00 104.20 ? 224 TYR   A CE2 1 
ATOM   1706  C  CZ  . TYR   A  1  224 ? 73.518  -116.947 49.385  1.00 106.45 ? 224 TYR   A CZ  1 
ATOM   1707  O  OH  . TYR   A  1  224 ? 73.287  -116.406 48.153  1.00 110.04 ? 224 TYR   A OH  1 
ATOM   1708  N  N   . THR   A  1  225 ? 77.254  -119.245 52.986  1.00 104.67 ? 225 THR   A N   1 
ATOM   1709  C  CA  . THR   A  1  225 ? 78.416  -119.568 52.113  1.00 108.94 ? 225 THR   A CA  1 
ATOM   1710  C  C   . THR   A  1  225 ? 78.159  -120.890 51.382  1.00 112.77 ? 225 THR   A C   1 
ATOM   1711  O  O   . THR   A  1  225 ? 77.246  -121.625 51.803  1.00 116.42 ? 225 THR   A O   1 
ATOM   1712  C  CB  . THR   A  1  225 ? 79.717  -119.646 52.921  1.00 109.08 ? 225 THR   A CB  1 
ATOM   1713  O  OG1 . THR   A  1  225 ? 79.602  -120.719 53.856  1.00 108.10 ? 225 THR   A OG1 1 
ATOM   1714  C  CG2 . THR   A  1  225 ? 80.032  -118.357 53.648  1.00 108.23 ? 225 THR   A CG2 1 
ATOM   1715  N  N   . GLY   A  1  226 ? 78.934  -121.169 50.329  1.00 115.56 ? 226 GLY   A N   1 
ATOM   1716  C  CA  . GLY   A  1  226 ? 78.915  -122.457 49.608  1.00 116.27 ? 226 GLY   A CA  1 
ATOM   1717  C  C   . GLY   A  1  226 ? 78.599  -122.315 48.128  1.00 116.28 ? 226 GLY   A C   1 
ATOM   1718  O  O   . GLY   A  1  226 ? 78.859  -123.286 47.386  1.00 117.59 ? 226 GLY   A O   1 
ATOM   1719  N  N   . ILE   A  1  227 ? 78.036  -121.175 47.708  1.00 113.07 ? 227 ILE   A N   1 
ATOM   1720  C  CA  . ILE   A  1  227 ? 77.749  -120.859 46.276  1.00 111.45 ? 227 ILE   A CA  1 
ATOM   1721  C  C   . ILE   A  1  227 ? 78.749  -119.803 45.814  1.00 112.26 ? 227 ILE   A C   1 
ATOM   1722  O  O   . ILE   A  1  227 ? 78.623  -118.637 46.183  1.00 113.53 ? 227 ILE   A O   1 
ATOM   1723  C  CB  . ILE   A  1  227 ? 76.287  -120.409 46.075  1.00 109.00 ? 227 ILE   A CB  1 
ATOM   1724  C  CG1 . ILE   A  1  227 ? 75.300  -121.466 46.580  1.00 107.01 ? 227 ILE   A CG1 1 
ATOM   1725  C  CG2 . ILE   A  1  227 ? 76.035  -120.057 44.616  1.00 109.05 ? 227 ILE   A CG2 1 
ATOM   1726  C  CD1 . ILE   A  1  227 ? 73.864  -121.000 46.666  1.00 105.19 ? 227 ILE   A CD1 1 
ATOM   1727  N  N   . PRO   A  1  228 ? 79.768  -120.177 45.003  1.00 114.77 ? 228 PRO   A N   1 
ATOM   1728  C  CA  . PRO   A  1  228 ? 80.806  -119.239 44.567  1.00 115.69 ? 228 PRO   A CA  1 
ATOM   1729  C  C   . PRO   A  1  228 ? 80.288  -118.007 43.805  1.00 116.17 ? 228 PRO   A C   1 
ATOM   1730  O  O   . PRO   A  1  228 ? 80.871  -116.951 43.965  1.00 114.87 ? 228 PRO   A O   1 
ATOM   1731  C  CB  . PRO   A  1  228 ? 81.692  -120.071 43.624  1.00 117.14 ? 228 PRO   A CB  1 
ATOM   1732  C  CG  . PRO   A  1  228 ? 81.434  -121.505 44.028  1.00 118.39 ? 228 PRO   A CG  1 
ATOM   1733  C  CD  . PRO   A  1  228 ? 79.989  -121.533 44.478  1.00 116.18 ? 228 PRO   A CD  1 
ATOM   1734  N  N   . THR   A  1  229 ? 79.229  -118.169 43.004  1.00 119.01 ? 229 THR   A N   1 
ATOM   1735  C  CA  . THR   A  1  229 ? 78.669  -117.117 42.106  1.00 120.45 ? 229 THR   A CA  1 
ATOM   1736  C  C   . THR   A  1  229 ? 77.911  -116.051 42.914  1.00 119.92 ? 229 THR   A C   1 
ATOM   1737  O  O   . THR   A  1  229 ? 77.867  -114.897 42.447  1.00 123.00 ? 229 THR   A O   1 
ATOM   1738  C  CB  . THR   A  1  229 ? 77.796  -117.734 41.005  1.00 121.06 ? 229 THR   A CB  1 
ATOM   1739  O  OG1 . THR   A  1  229 ? 76.800  -118.564 41.602  1.00 123.50 ? 229 THR   A OG1 1 
ATOM   1740  C  CG2 . THR   A  1  229 ? 78.608  -118.544 40.018  1.00 119.44 ? 229 THR   A CG2 1 
ATOM   1741  N  N   . ASP   A  1  230 ? 77.334  -116.415 44.065  1.00 123.04 ? 230 ASP   A N   1 
ATOM   1742  C  CA  . ASP   A  1  230 ? 76.671  -115.478 45.015  1.00 124.78 ? 230 ASP   A CA  1 
ATOM   1743  C  C   . ASP   A  1  230 ? 77.741  -114.893 45.946  1.00 119.09 ? 230 ASP   A C   1 
ATOM   1744  O  O   . ASP   A  1  230 ? 78.304  -115.669 46.739  1.00 124.85 ? 230 ASP   A O   1 
ATOM   1745  C  CB  . ASP   A  1  230 ? 75.568  -116.189 45.807  1.00 127.49 ? 230 ASP   A CB  1 
ATOM   1746  C  CG  . ASP   A  1  230 ? 74.475  -116.797 44.942  1.00 129.88 ? 230 ASP   A CG  1 
ATOM   1747  O  OD1 . ASP   A  1  230 ? 74.600  -116.727 43.703  1.00 131.31 ? 230 ASP   A OD1 1 
ATOM   1748  O  OD2 . ASP   A  1  230 ? 73.510  -117.342 45.515  1.00 131.07 ? 230 ASP   A OD2 1 
ATOM   1749  N  N   . LYS   A  1  231 ? 78.018  -113.586 45.850  1.00 120.08 ? 231 LYS   A N   1 
ATOM   1750  C  CA  . LYS   A  1  231 ? 79.156  -112.928 46.559  1.00 115.78 ? 231 LYS   A CA  1 
ATOM   1751  C  C   . LYS   A  1  231 ? 78.688  -111.797 47.487  1.00 111.58 ? 231 LYS   A C   1 
ATOM   1752  O  O   . LYS   A  1  231 ? 79.566  -111.202 48.151  1.00 103.50 ? 231 LYS   A O   1 
ATOM   1753  C  CB  . LYS   A  1  231 ? 80.179  -112.414 45.543  1.00 119.36 ? 231 LYS   A CB  1 
ATOM   1754  C  CG  . LYS   A  1  231 ? 81.263  -113.417 45.175  1.00 119.44 ? 231 LYS   A CG  1 
ATOM   1755  C  CD  . LYS   A  1  231 ? 82.010  -113.063 43.914  1.00 121.01 ? 231 LYS   A CD  1 
ATOM   1756  C  CE  . LYS   A  1  231 ? 81.226  -113.392 42.663  1.00 122.11 ? 231 LYS   A CE  1 
ATOM   1757  N  NZ  . LYS   A  1  231 ? 81.939  -112.955 41.441  1.00 125.33 ? 231 LYS   A NZ  1 
ATOM   1758  N  N   . GLY   A  1  232 ? 77.382  -111.510 47.549  1.00 109.59 ? 232 GLY   A N   1 
ATOM   1759  C  CA  . GLY   A  1  232 ? 76.795  -110.610 48.562  1.00 106.82 ? 232 GLY   A CA  1 
ATOM   1760  C  C   . GLY   A  1  232 ? 76.356  -109.267 47.987  1.00 103.33 ? 232 GLY   A C   1 
ATOM   1761  O  O   . GLY   A  1  232 ? 76.703  -108.916 46.861  1.00 102.52 ? 232 GLY   A O   1 
ATOM   1762  N  N   . PRO   A  1  233 ? 75.589  -108.473 48.771  1.00 99.60  ? 233 PRO   A N   1 
ATOM   1763  C  CA  . PRO   A  1  233 ? 75.042  -107.200 48.301  1.00 98.67  ? 233 PRO   A CA  1 
ATOM   1764  C  C   . PRO   A  1  233 ? 76.114  -106.112 48.136  1.00 100.24 ? 233 PRO   A C   1 
ATOM   1765  O  O   . PRO   A  1  233 ? 77.034  -106.074 48.933  1.00 104.81 ? 233 PRO   A O   1 
ATOM   1766  C  CB  . PRO   A  1  233 ? 74.054  -106.816 49.414  1.00 96.98  ? 233 PRO   A CB  1 
ATOM   1767  C  CG  . PRO   A  1  233 ? 74.631  -107.459 50.655  1.00 97.80  ? 233 PRO   A CG  1 
ATOM   1768  C  CD  . PRO   A  1  233 ? 75.217  -108.764 50.164  1.00 99.41  ? 233 PRO   A CD  1 
ATOM   1769  N  N   . ARG   A  1  234 ? 75.963  -105.263 47.112  1.00 100.40 ? 234 ARG   A N   1 
ATOM   1770  C  CA  . ARG   A  1  234 ? 76.816  -104.066 46.869  1.00 100.96 ? 234 ARG   A CA  1 
ATOM   1771  C  C   . ARG   A  1  234 ? 76.221  -102.848 47.588  1.00 99.01  ? 234 ARG   A C   1 
ATOM   1772  O  O   . ARG   A  1  234 ? 76.989  -101.906 47.871  1.00 98.91  ? 234 ARG   A O   1 
ATOM   1773  C  CB  . ARG   A  1  234 ? 76.958  -103.793 45.370  1.00 99.33  ? 234 ARG   A CB  1 
ATOM   1774  C  CG  . ARG   A  1  234 ? 77.765  -104.844 44.624  1.00 101.22 ? 234 ARG   A CG  1 
ATOM   1775  C  CD  . ARG   A  1  234 ? 77.757  -104.591 43.131  1.00 101.58 ? 234 ARG   A CD  1 
ATOM   1776  N  NE  . ARG   A  1  234 ? 78.638  -105.505 42.416  1.00 105.17 ? 234 ARG   A NE  1 
ATOM   1777  C  CZ  . ARG   A  1  234 ? 79.934  -105.308 42.185  1.00 107.06 ? 234 ARG   A CZ  1 
ATOM   1778  N  NH1 . ARG   A  1  234 ? 80.541  -104.212 42.608  1.00 105.95 ? 234 ARG   A NH1 1 
ATOM   1779  N  NH2 . ARG   A  1  234 ? 80.625  -106.220 41.522  1.00 111.68 ? 234 ARG   A NH2 1 
ATOM   1780  N  N   . PHE   A  1  235 ? 74.912  -102.861 47.865  1.00 96.07  ? 235 PHE   A N   1 
ATOM   1781  C  CA  . PHE   A  1  235 ? 74.239  -101.851 48.721  1.00 97.52  ? 235 PHE   A CA  1 
ATOM   1782  C  C   . PHE   A  1  235 ? 74.703  -102.054 50.164  1.00 99.55  ? 235 PHE   A C   1 
ATOM   1783  O  O   . PHE   A  1  235 ? 74.633  -103.198 50.659  1.00 97.18  ? 235 PHE   A O   1 
ATOM   1784  C  CB  . PHE   A  1  235 ? 72.713  -101.947 48.649  1.00 98.54  ? 235 PHE   A CB  1 
ATOM   1785  C  CG  . PHE   A  1  235 ? 71.998  -101.010 49.595  1.00 101.13 ? 235 PHE   A CG  1 
ATOM   1786  C  CD1 . PHE   A  1  235 ? 71.758  -101.377 50.912  1.00 102.42 ? 235 PHE   A CD1 1 
ATOM   1787  C  CD2 . PHE   A  1  235 ? 71.586  -99.751  49.179  1.00 100.96 ? 235 PHE   A CD2 1 
ATOM   1788  C  CE1 . PHE   A  1  235 ? 71.113  -100.513 51.785  1.00 102.49 ? 235 PHE   A CE1 1 
ATOM   1789  C  CE2 . PHE   A  1  235 ? 70.938  -98.890  50.053  1.00 99.67  ? 235 PHE   A CE2 1 
ATOM   1790  C  CZ  . PHE   A  1  235 ? 70.703  -99.272  51.354  1.00 101.14 ? 235 PHE   A CZ  1 
ATOM   1791  N  N   . ARG   A  1  236 ? 75.158  -100.978 50.809  1.00 101.93 ? 236 ARG   A N   1 
ATOM   1792  C  CA  . ARG   A  1  236 ? 75.468  -100.959 52.262  1.00 106.93 ? 236 ARG   A CA  1 
ATOM   1793  C  C   . ARG   A  1  236 ? 75.106  -99.592  52.847  1.00 107.17 ? 236 ARG   A C   1 
ATOM   1794  O  O   . ARG   A  1  236 ? 75.458  -98.563  52.235  1.00 108.43 ? 236 ARG   A O   1 
ATOM   1795  C  CB  . ARG   A  1  236 ? 76.940  -101.281 52.532  1.00 113.31 ? 236 ARG   A CB  1 
ATOM   1796  C  CG  . ARG   A  1  236 ? 77.229  -101.564 54.001  1.00 117.16 ? 236 ARG   A CG  1 
ATOM   1797  C  CD  . ARG   A  1  236 ? 78.682  -101.858 54.314  1.00 122.00 ? 236 ARG   A CD  1 
ATOM   1798  N  NE  . ARG   A  1  236 ? 79.527  -100.685 54.127  1.00 127.23 ? 236 ARG   A NE  1 
ATOM   1799  C  CZ  . ARG   A  1  236 ? 80.682  -100.458 54.751  1.00 133.00 ? 236 ARG   A CZ  1 
ATOM   1800  N  NH1 . ARG   A  1  236 ? 81.158  -101.323 55.633  1.00 133.71 ? 236 ARG   A NH1 1 
ATOM   1801  N  NH2 . ARG   A  1  236 ? 81.359  -99.351  54.492  1.00 138.84 ? 236 ARG   A NH2 1 
ATOM   1802  N  N   . LYS   A  1  237 ? 74.434  -99.608  53.998  1.00 104.61 ? 237 LYS   A N   1 
ATOM   1803  C  CA  . LYS   A  1  237 ? 74.109  -98.414  54.816  1.00 102.81 ? 237 LYS   A CA  1 
ATOM   1804  C  C   . LYS   A  1  237 ? 75.290  -98.175  55.760  1.00 104.04 ? 237 LYS   A C   1 
ATOM   1805  O  O   . LYS   A  1  237 ? 75.641  -99.117  56.498  1.00 106.21 ? 237 LYS   A O   1 
ATOM   1806  C  CB  . LYS   A  1  237 ? 72.801  -98.661  55.573  1.00 101.96 ? 237 LYS   A CB  1 
ATOM   1807  C  CG  . LYS   A  1  237 ? 71.931  -97.437  55.815  1.00 103.76 ? 237 LYS   A CG  1 
ATOM   1808  C  CD  . LYS   A  1  237 ? 70.470  -97.792  55.986  1.00 107.12 ? 237 LYS   A CD  1 
ATOM   1809  C  CE  . LYS   A  1  237 ? 69.568  -96.582  56.090  1.00 111.41 ? 237 LYS   A CE  1 
ATOM   1810  N  NZ  . LYS   A  1  237 ? 69.599  -95.990  57.449  1.00 114.78 ? 237 LYS   A NZ  1 
ATOM   1811  N  N   . LEU   A  1  238 ? 75.911  -96.993  55.706  1.00 103.89 ? 238 LEU   A N   1 
ATOM   1812  C  CA  . LEU   A  1  238 ? 76.997  -96.611  56.646  1.00 103.46 ? 238 LEU   A CA  1 
ATOM   1813  C  C   . LEU   A  1  238 ? 76.383  -96.458  58.040  1.00 100.32 ? 238 LEU   A C   1 
ATOM   1814  O  O   . LEU   A  1  238 ? 75.281  -95.889  58.138  1.00 101.00 ? 238 LEU   A O   1 
ATOM   1815  C  CB  . LEU   A  1  238 ? 77.672  -95.308  56.200  1.00 105.96 ? 238 LEU   A CB  1 
ATOM   1816  C  CG  . LEU   A  1  238 ? 78.429  -95.334  54.870  1.00 105.93 ? 238 LEU   A CG  1 
ATOM   1817  C  CD1 . LEU   A  1  238 ? 79.577  -94.336  54.899  1.00 108.73 ? 238 LEU   A CD1 1 
ATOM   1818  C  CD2 . LEU   A  1  238 ? 78.960  -96.719  54.531  1.00 105.35 ? 238 LEU   A CD2 1 
ATOM   1819  N  N   . THR   A  1  239 ? 77.065  -96.964  59.069  1.00 101.55 ? 239 THR   A N   1 
ATOM   1820  C  CA  . THR   A  1  239 ? 76.623  -96.884  60.486  1.00 105.08 ? 239 THR   A CA  1 
ATOM   1821  C  C   . THR   A  1  239 ? 76.849  -95.461  61.004  1.00 107.25 ? 239 THR   A C   1 
ATOM   1822  O  O   . THR   A  1  239 ? 77.692  -94.741  60.428  1.00 108.86 ? 239 THR   A O   1 
ATOM   1823  C  CB  . THR   A  1  239 ? 77.342  -97.915  61.364  1.00 106.52 ? 239 THR   A CB  1 
ATOM   1824  O  OG1 . THR   A  1  239 ? 78.745  -97.651  61.320  1.00 103.87 ? 239 THR   A OG1 1 
ATOM   1825  C  CG2 . THR   A  1  239 ? 77.068  -99.338  60.932  1.00 106.28 ? 239 THR   A CG2 1 
ATOM   1826  N  N   . SER   A  1  240 ? 76.118  -95.082  62.053  1.00 110.17 ? 240 SER   A N   1 
ATOM   1827  C  CA  . SER   A  1  240 ? 76.257  -93.786  62.764  1.00 112.38 ? 240 SER   A CA  1 
ATOM   1828  C  C   . SER   A  1  240 ? 77.726  -93.567  63.152  1.00 115.06 ? 240 SER   A C   1 
ATOM   1829  O  O   . SER   A  1  240 ? 78.193  -92.417  63.069  1.00 115.04 ? 240 SER   A O   1 
ATOM   1830  C  CB  . SER   A  1  240 ? 75.345  -93.741  63.962  1.00 113.99 ? 240 SER   A CB  1 
ATOM   1831  O  OG  . SER   A  1  240 ? 75.444  -92.497  64.636  1.00 115.71 ? 240 SER   A OG  1 
ATOM   1832  N  N   . GLN   A  1  241 ? 78.428  -94.639  63.533  1.00 115.15 ? 241 GLN   A N   1 
ATOM   1833  C  CA  . GLN   A  1  241 ? 79.861  -94.609  63.934  1.00 116.74 ? 241 GLN   A CA  1 
ATOM   1834  C  C   . GLN   A  1  241 ? 80.746  -94.351  62.707  1.00 116.35 ? 241 GLN   A C   1 
ATOM   1835  O  O   . GLN   A  1  241 ? 81.702  -93.562  62.836  1.00 119.01 ? 241 GLN   A O   1 
ATOM   1836  C  CB  . GLN   A  1  241 ? 80.251  -95.918  64.626  1.00 116.62 ? 241 GLN   A CB  1 
ATOM   1837  C  CG  . GLN   A  1  241 ? 81.702  -95.966  65.090  1.00 117.15 ? 241 GLN   A CG  1 
ATOM   1838  C  CD  . GLN   A  1  241 ? 82.042  -94.829  66.022  1.00 117.79 ? 241 GLN   A CD  1 
ATOM   1839  O  OE1 . GLN   A  1  241 ? 81.334  -94.567  66.992  1.00 120.29 ? 241 GLN   A OE1 1 
ATOM   1840  N  NE2 . GLN   A  1  241 ? 83.132  -94.135  65.733  1.00 120.10 ? 241 GLN   A NE2 1 
ATOM   1841  N  N   . GLU   A  1  242 ? 80.449  -94.992  61.571  1.00 114.59 ? 242 GLU   A N   1 
ATOM   1842  C  CA  . GLU   A  1  242 ? 81.257  -94.905  60.321  1.00 117.40 ? 242 GLU   A CA  1 
ATOM   1843  C  C   . GLU   A  1  242 ? 81.219  -93.479  59.753  1.00 119.01 ? 242 GLU   A C   1 
ATOM   1844  O  O   . GLU   A  1  242 ? 82.208  -93.082  59.102  1.00 123.87 ? 242 GLU   A O   1 
ATOM   1845  C  CB  . GLU   A  1  242 ? 80.759  -95.907  59.277  1.00 117.07 ? 242 GLU   A CB  1 
ATOM   1846  C  CG  . GLU   A  1  242 ? 81.292  -97.313  59.489  1.00 119.07 ? 242 GLU   A CG  1 
ATOM   1847  C  CD  . GLU   A  1  242 ? 80.678  -98.374  58.592  1.00 118.57 ? 242 GLU   A CD  1 
ATOM   1848  O  OE1 . GLU   A  1  242 ? 79.810  -98.024  57.769  1.00 119.34 ? 242 GLU   A OE1 1 
ATOM   1849  O  OE2 . GLU   A  1  242 ? 81.072  -99.550  58.717  1.00 120.09 ? 242 GLU   A OE2 1 
ATOM   1850  N  N   . ILE   A  1  243 ? 80.126  -92.744  59.980  1.00 117.87 ? 243 ILE   A N   1 
ATOM   1851  C  CA  . ILE   A  1  243 ? 79.955  -91.341  59.500  1.00 119.71 ? 243 ILE   A CA  1 
ATOM   1852  C  C   . ILE   A  1  243 ? 80.860  -90.433  60.344  1.00 119.17 ? 243 ILE   A C   1 
ATOM   1853  O  O   . ILE   A  1  243 ? 81.629  -89.657  59.743  1.00 125.68 ? 243 ILE   A O   1 
ATOM   1854  C  CB  . ILE   A  1  243 ? 78.469  -90.919  59.534  1.00 120.48 ? 243 ILE   A CB  1 
ATOM   1855  C  CG1 . ILE   A  1  243 ? 77.615  -91.801  58.618  1.00 117.26 ? 243 ILE   A CG1 1 
ATOM   1856  C  CG2 . ILE   A  1  243 ? 78.309  -89.444  59.188  1.00 121.92 ? 243 ILE   A CG2 1 
ATOM   1857  C  CD1 . ILE   A  1  243 ? 76.124  -91.702  58.863  1.00 117.52 ? 243 ILE   A CD1 1 
ATOM   1858  N  N   . ASN   A  1  244 ? 80.798  -90.560  61.676  1.00 118.09 ? 244 ASN   A N   1 
ATOM   1859  C  CA  . ASN   A  1  244 ? 81.531  -89.705  62.652  1.00 118.25 ? 244 ASN   A CA  1 
ATOM   1860  C  C   . ASN   A  1  244 ? 83.047  -89.866  62.478  1.00 123.42 ? 244 ASN   A C   1 
ATOM   1861  O  O   . ASN   A  1  244 ? 83.775  -88.896  62.780  1.00 126.95 ? 244 ASN   A O   1 
ATOM   1862  C  CB  . ASN   A  1  244 ? 81.124  -90.008  64.096  1.00 117.48 ? 244 ASN   A CB  1 
ATOM   1863  C  CG  . ASN   A  1  244 ? 79.691  -89.626  64.404  1.00 113.24 ? 244 ASN   A CG  1 
ATOM   1864  O  OD1 . ASN   A  1  244 ? 79.184  -88.621  63.908  1.00 112.12 ? 244 ASN   A OD1 1 
ATOM   1865  N  ND2 . ASN   A  1  244 ? 79.028  -90.415  65.233  1.00 112.75 ? 244 ASN   A ND2 1 
ATOM   1866  N  N   . ASP   A  1  245 ? 83.502  -91.039  62.026  1.00 122.23 ? 245 ASP   A N   1 
ATOM   1867  C  CA  . ASP   A  1  245 ? 84.932  -91.326  61.729  1.00 126.19 ? 245 ASP   A CA  1 
ATOM   1868  C  C   . ASP   A  1  245 ? 85.415  -90.420  60.591  1.00 128.89 ? 245 ASP   A C   1 
ATOM   1869  O  O   . ASP   A  1  245 ? 86.573  -89.964  60.655  1.00 131.73 ? 245 ASP   A O   1 
ATOM   1870  C  CB  . ASP   A  1  245 ? 85.141  -92.797  61.368  1.00 127.77 ? 245 ASP   A CB  1 
ATOM   1871  C  CG  . ASP   A  1  245 ? 84.882  -93.752  62.520  1.00 131.61 ? 245 ASP   A CG  1 
ATOM   1872  O  OD1 . ASP   A  1  245 ? 84.971  -93.308  63.682  1.00 137.01 ? 245 ASP   A OD1 1 
ATOM   1873  O  OD2 . ASP   A  1  245 ? 84.586  -94.931  62.244  1.00 136.97 ? 245 ASP   A OD2 1 
ATOM   1874  N  N   . ARG   A  1  246 ? 84.556  -90.171  59.598  1.00 128.06 ? 246 ARG   A N   1 
ATOM   1875  C  CA  . ARG   A  1  246 ? 84.880  -89.370  58.387  1.00 130.92 ? 246 ARG   A CA  1 
ATOM   1876  C  C   . ARG   A  1  246 ? 84.656  -87.870  58.641  1.00 138.87 ? 246 ARG   A C   1 
ATOM   1877  O  O   . ARG   A  1  246 ? 85.200  -87.068  57.855  1.00 141.91 ? 246 ARG   A O   1 
ATOM   1878  C  CB  . ARG   A  1  246 ? 84.049  -89.862  57.198  1.00 128.29 ? 246 ARG   A CB  1 
ATOM   1879  C  CG  . ARG   A  1  246 ? 84.560  -91.163  56.599  1.00 125.21 ? 246 ARG   A CG  1 
ATOM   1880  C  CD  . ARG   A  1  246 ? 83.548  -91.817  55.682  1.00 123.63 ? 246 ARG   A CD  1 
ATOM   1881  N  NE  . ARG   A  1  246 ? 84.050  -93.064  55.121  1.00 123.68 ? 246 ARG   A NE  1 
ATOM   1882  C  CZ  . ARG   A  1  246 ? 84.128  -94.222  55.775  1.00 123.89 ? 246 ARG   A CZ  1 
ATOM   1883  N  NH1 . ARG   A  1  246 ? 83.736  -94.318  57.036  1.00 123.45 ? 246 ARG   A NH1 1 
ATOM   1884  N  NH2 . ARG   A  1  246 ? 84.604  -95.290  55.160  1.00 125.88 ? 246 ARG   A NH2 1 
ATOM   1885  N  N   . LEU   A  1  247 ? 83.897  -87.500  59.681  1.00 138.21 ? 247 LEU   A N   1 
ATOM   1886  C  CA  . LEU   A  1  247 ? 83.579  -86.081  60.015  1.00 140.53 ? 247 LEU   A CA  1 
ATOM   1887  C  C   . LEU   A  1  247 ? 84.740  -85.429  60.782  1.00 146.59 ? 247 LEU   A C   1 
ATOM   1888  O  O   . LEU   A  1  247 ? 84.704  -84.193  60.944  1.00 143.10 ? 247 LEU   A O   1 
ATOM   1889  C  CB  . LEU   A  1  247 ? 82.280  -86.011  60.830  1.00 136.71 ? 247 LEU   A CB  1 
ATOM   1890  C  CG  . LEU   A  1  247 ? 80.978  -86.200  60.049  1.00 133.51 ? 247 LEU   A CG  1 
ATOM   1891  C  CD1 . LEU   A  1  247 ? 79.793  -86.300  60.998  1.00 128.04 ? 247 LEU   A CD1 1 
ATOM   1892  C  CD2 . LEU   A  1  247 ? 80.754  -85.069  59.053  1.00 135.53 ? 247 LEU   A CD2 1 
ATOM   1893  N  N   . GLU   A  1  248 ? 85.724  -86.212  61.241  1.00 152.79 ? 248 GLU   A N   1 
ATOM   1894  C  CA  . GLU   A  1  248 ? 86.930  -85.700  61.952  1.00 157.63 ? 248 GLU   A CA  1 
ATOM   1895  C  C   . GLU   A  1  248 ? 87.980  -85.250  60.928  1.00 164.14 ? 248 GLU   A C   1 
ATOM   1896  O  O   . GLU   A  1  248 ? 88.573  -84.173  61.137  1.00 173.56 ? 248 GLU   A O   1 
ATOM   1897  C  CB  . GLU   A  1  248 ? 87.487  -86.761  62.903  1.00 158.40 ? 248 GLU   A CB  1 
ATOM   1898  C  CG  . GLU   A  1  248 ? 86.778  -86.787  64.246  1.00 156.70 ? 248 GLU   A CG  1 
ATOM   1899  C  CD  . GLU   A  1  248 ? 86.496  -88.172  64.801  1.00 153.66 ? 248 GLU   A CD  1 
ATOM   1900  O  OE1 . GLU   A  1  248 ? 87.195  -89.124  64.403  1.00 153.22 ? 248 GLU   A OE1 1 
ATOM   1901  O  OE2 . GLU   A  1  248 ? 85.569  -88.297  65.625  1.00 147.53 ? 248 GLU   A OE2 1 
ATOM   1902  N  N   . ALA   A  1  249 ? 88.200  -86.042  59.872  1.00 164.56 ? 249 ALA   A N   1 
ATOM   1903  C  CA  . ALA   A  1  249 ? 89.081  -85.710  58.727  1.00 163.59 ? 249 ALA   A CA  1 
ATOM   1904  C  C   . ALA   A  1  249 ? 88.247  -85.040  57.625  1.00 163.26 ? 249 ALA   A C   1 
ATOM   1905  O  O   . ALA   A  1  249 ? 88.292  -85.514  56.472  1.00 165.25 ? 249 ALA   A O   1 
ATOM   1906  C  CB  . ALA   A  1  249 ? 89.777  -86.958  58.235  1.00 160.69 ? 249 ALA   A CB  1 
ATOM   1907  N  N   . LEU   A  1  250 ? 87.524  -83.970  57.977  1.00 162.52 ? 250 LEU   A N   1 
ATOM   1908  C  CA  . LEU   A  1  250 ? 86.566  -83.244  57.096  1.00 162.94 ? 250 LEU   A CA  1 
ATOM   1909  C  C   . LEU   A  1  250 ? 87.223  -81.943  56.613  1.00 160.74 ? 250 LEU   A C   1 
ATOM   1910  O  O   . LEU   A  1  250 ? 88.092  -81.968  55.741  1.00 156.57 ? 250 LEU   A O   1 
ATOM   1911  C  CB  . LEU   A  1  250 ? 85.276  -82.988  57.891  1.00 164.79 ? 250 LEU   A CB  1 
ATOM   1912  C  CG  . LEU   A  1  250 ? 83.973  -82.810  57.103  1.00 163.81 ? 250 LEU   A CG  1 
ATOM   1913  C  CD1 . LEU   A  1  250 ? 83.910  -81.454  56.417  1.00 165.04 ? 250 LEU   A CD1 1 
ATOM   1914  C  CD2 . LEU   A  1  250 ? 83.755  -83.933  56.097  1.00 158.95 ? 250 LEU   A CD2 1 
ATOM   1915  O  OXT . LEU   A  1  250 ? 86.927  -80.835  57.065  1.00 153.00 ? 250 LEU   A OXT 1 
ATOM   1916  N  N   . GLY   B  2  2   ? 27.643  -85.547  43.989  1.00 115.52 ? 1   GLY   B N   1 
ATOM   1917  C  CA  . GLY   B  2  2   ? 28.666  -86.610  43.763  1.00 114.00 ? 1   GLY   B CA  1 
ATOM   1918  C  C   . GLY   B  2  2   ? 29.986  -86.039  43.274  1.00 117.23 ? 1   GLY   B C   1 
ATOM   1919  O  O   . GLY   B  2  2   ? 30.349  -84.929  43.715  1.00 119.68 ? 1   GLY   B O   1 
ATOM   1920  N  N   . SER   B  2  3   ? 30.677  -86.769  42.392  1.00 115.01 ? 2   SER   B N   1 
ATOM   1921  C  CA  . SER   B  2  3   ? 32.019  -86.426  41.848  1.00 120.43 ? 2   SER   B CA  1 
ATOM   1922  C  C   . SER   B  2  3   ? 31.910  -85.570  40.577  1.00 122.19 ? 2   SER   B C   1 
ATOM   1923  O  O   . SER   B  2  3   ? 32.955  -85.034  40.151  1.00 118.52 ? 2   SER   B O   1 
ATOM   1924  C  CB  . SER   B  2  3   ? 32.826  -87.674  41.596  1.00 119.58 ? 2   SER   B CB  1 
ATOM   1925  O  OG  . SER   B  2  3   ? 32.098  -88.595  40.795  1.00 121.40 ? 2   SER   B OG  1 
ATOM   1926  N  N   . ARG   B  2  4   ? 30.709  -85.442  39.993  1.00 126.88 ? 3   ARG   B N   1 
ATOM   1927  C  CA  . ARG   B  2  4   ? 30.430  -84.595  38.796  1.00 131.08 ? 3   ARG   B CA  1 
ATOM   1928  C  C   . ARG   B  2  4   ? 31.110  -83.228  38.955  1.00 130.01 ? 3   ARG   B C   1 
ATOM   1929  O  O   . ARG   B  2  4   ? 31.659  -82.725  37.955  1.00 129.45 ? 3   ARG   B O   1 
ATOM   1930  C  CB  . ARG   B  2  4   ? 28.919  -84.434  38.583  1.00 140.47 ? 3   ARG   B CB  1 
ATOM   1931  C  CG  . ARG   B  2  4   ? 28.504  -83.109  37.956  1.00 151.34 ? 3   ARG   B CG  1 
ATOM   1932  C  CD  . ARG   B  2  4   ? 27.046  -83.072  37.535  1.00 163.08 ? 3   ARG   B CD  1 
ATOM   1933  N  NE  . ARG   B  2  4   ? 26.131  -83.365  38.634  1.00 172.20 ? 3   ARG   B NE  1 
ATOM   1934  C  CZ  . ARG   B  2  4   ? 25.464  -84.507  38.812  1.00 177.02 ? 3   ARG   B CZ  1 
ATOM   1935  N  NH1 . ARG   B  2  4   ? 25.589  -85.512  37.959  1.00 173.55 ? 3   ARG   B NH1 1 
ATOM   1936  N  NH2 . ARG   B  2  4   ? 24.661  -84.637  39.855  1.00 180.76 ? 3   ARG   B NH2 1 
ATOM   1937  N  N   . ARG   B  2  5   ? 31.055  -82.660  40.167  1.00 129.41 ? 4   ARG   B N   1 
ATOM   1938  C  CA  . ARG   B  2  5   ? 31.570  -81.310  40.531  1.00 131.14 ? 4   ARG   B CA  1 
ATOM   1939  C  C   . ARG   B  2  5   ? 33.000  -81.106  40.006  1.00 122.91 ? 4   ARG   B C   1 
ATOM   1940  O  O   . ARG   B  2  5   ? 33.283  -80.000  39.505  1.00 130.58 ? 4   ARG   B O   1 
ATOM   1941  C  CB  . ARG   B  2  5   ? 31.543  -81.131  42.054  1.00 135.78 ? 4   ARG   B CB  1 
ATOM   1942  C  CG  . ARG   B  2  5   ? 31.047  -79.770  42.524  1.00 142.08 ? 4   ARG   B CG  1 
ATOM   1943  C  CD  . ARG   B  2  5   ? 31.050  -79.651  44.040  1.00 145.39 ? 4   ARG   B CD  1 
ATOM   1944  N  NE  . ARG   B  2  5   ? 30.385  -80.778  44.690  1.00 149.88 ? 4   ARG   B NE  1 
ATOM   1945  C  CZ  . ARG   B  2  5   ? 29.072  -80.892  44.891  1.00 149.50 ? 4   ARG   B CZ  1 
ATOM   1946  N  NH1 . ARG   B  2  5   ? 28.239  -79.941  44.500  1.00 149.53 ? 4   ARG   B NH1 1 
ATOM   1947  N  NH2 . ARG   B  2  5   ? 28.594  -81.970  45.490  1.00 150.51 ? 4   ARG   B NH2 1 
ATOM   1948  N  N   . TYR   B  2  6   ? 33.859  -82.127  40.115  1.00 113.75 ? 5   TYR   B N   1 
ATOM   1949  C  CA  . TYR   B  2  6   ? 35.331  -82.032  39.909  1.00 112.49 ? 5   TYR   B CA  1 
ATOM   1950  C  C   . TYR   B  2  6   ? 35.748  -82.618  38.553  1.00 108.17 ? 5   TYR   B C   1 
ATOM   1951  O  O   . TYR   B  2  6   ? 36.965  -82.800  38.346  1.00 102.79 ? 5   TYR   B O   1 
ATOM   1952  C  CB  . TYR   B  2  6   ? 36.073  -82.755  41.037  1.00 113.29 ? 5   TYR   B CB  1 
ATOM   1953  C  CG  . TYR   B  2  6   ? 35.487  -82.545  42.411  1.00 117.24 ? 5   TYR   B CG  1 
ATOM   1954  C  CD1 . TYR   B  2  6   ? 35.814  -81.432  43.168  1.00 121.66 ? 5   TYR   B CD1 1 
ATOM   1955  C  CD2 . TYR   B  2  6   ? 34.593  -83.455  42.954  1.00 117.87 ? 5   TYR   B CD2 1 
ATOM   1956  C  CE1 . TYR   B  2  6   ? 35.273  -81.228  44.429  1.00 121.37 ? 5   TYR   B CE1 1 
ATOM   1957  C  CE2 . TYR   B  2  6   ? 34.043  -83.267  44.213  1.00 118.65 ? 5   TYR   B CE2 1 
ATOM   1958  C  CZ  . TYR   B  2  6   ? 34.384  -82.150  44.955  1.00 120.19 ? 5   TYR   B CZ  1 
ATOM   1959  O  OH  . TYR   B  2  6   ? 33.847  -81.956  46.195  1.00 119.23 ? 5   TYR   B OH  1 
ATOM   1960  N  N   . ASP   B  2  7   ? 34.786  -82.897  37.665  1.00 109.71 ? 6   ASP   B N   1 
ATOM   1961  C  CA  . ASP   B  2  7   ? 35.024  -83.470  36.312  1.00 108.66 ? 6   ASP   B CA  1 
ATOM   1962  C  C   . ASP   B  2  7   ? 35.365  -82.335  35.337  1.00 106.75 ? 6   ASP   B C   1 
ATOM   1963  O  O   . ASP   B  2  7   ? 34.487  -81.480  35.101  1.00 110.80 ? 6   ASP   B O   1 
ATOM   1964  C  CB  . ASP   B  2  7   ? 33.806  -84.265  35.832  1.00 106.38 ? 6   ASP   B CB  1 
ATOM   1965  C  CG  . ASP   B  2  7   ? 34.098  -85.234  34.698  1.00 104.62 ? 6   ASP   B CG  1 
ATOM   1966  O  OD1 . ASP   B  2  7   ? 35.019  -84.957  33.901  1.00 104.59 ? 6   ASP   B OD1 1 
ATOM   1967  O  OD2 . ASP   B  2  7   ? 33.404  -86.266  34.627  1.00 101.14 ? 6   ASP   B OD2 1 
ATOM   1968  N  N   . SER   B  2  8   ? 36.585  -82.340  34.785  1.00 104.39 ? 7   SER   B N   1 
ATOM   1969  C  CA  . SER   B  2  8   ? 37.077  -81.363  33.776  1.00 105.26 ? 7   SER   B CA  1 
ATOM   1970  C  C   . SER   B  2  8   ? 36.335  -81.548  32.448  1.00 108.87 ? 7   SER   B C   1 
ATOM   1971  O  O   . SER   B  2  8   ? 36.265  -80.567  31.685  1.00 112.95 ? 7   SER   B O   1 
ATOM   1972  C  CB  . SER   B  2  8   ? 38.562  -81.489  33.563  1.00 104.03 ? 7   SER   B CB  1 
ATOM   1973  O  OG  . SER   B  2  8   ? 39.268  -81.312  34.781  1.00 106.05 ? 7   SER   B OG  1 
ATOM   1974  N  N   . ARG   B  2  9   ? 35.822  -82.758  32.190  1.00 106.68 ? 8   ARG   B N   1 
ATOM   1975  C  CA  . ARG   B  2  9   ? 35.209  -83.175  30.899  1.00 106.52 ? 8   ARG   B CA  1 
ATOM   1976  C  C   . ARG   B  2  9   ? 36.265  -83.025  29.798  1.00 102.62 ? 8   ARG   B C   1 
ATOM   1977  O  O   . ARG   B  2  9   ? 36.146  -82.098  28.981  1.00 102.05 ? 8   ARG   B O   1 
ATOM   1978  C  CB  . ARG   B  2  9   ? 33.943  -82.360  30.605  1.00 112.62 ? 8   ARG   B CB  1 
ATOM   1979  C  CG  . ARG   B  2  9   ? 32.795  -82.616  31.572  1.00 120.24 ? 8   ARG   B CG  1 
ATOM   1980  C  CD  . ARG   B  2  9   ? 32.064  -81.337  31.938  1.00 127.53 ? 8   ARG   B CD  1 
ATOM   1981  N  NE  . ARG   B  2  9   ? 31.283  -80.791  30.834  1.00 134.69 ? 8   ARG   B NE  1 
ATOM   1982  C  CZ  . ARG   B  2  9   ? 30.875  -79.526  30.732  1.00 141.35 ? 8   ARG   B CZ  1 
ATOM   1983  N  NH1 . ARG   B  2  9   ? 31.179  -78.637  31.665  1.00 145.78 ? 8   ARG   B NH1 1 
ATOM   1984  N  NH2 . ARG   B  2  9   ? 30.166  -79.150  29.681  1.00 147.39 ? 8   ARG   B NH2 1 
ATOM   1985  N  N   . THR   B  2  10  ? 37.271  -83.902  29.800  1.00 99.85  ? 9   THR   B N   1 
ATOM   1986  C  CA  . THR   B  2  10  ? 38.476  -83.816  28.929  1.00 97.15  ? 9   THR   B CA  1 
ATOM   1987  C  C   . THR   B  2  10  ? 38.107  -84.071  27.464  1.00 94.67  ? 9   THR   B C   1 
ATOM   1988  O  O   . THR   B  2  10  ? 38.816  -83.542  26.591  1.00 98.13  ? 9   THR   B O   1 
ATOM   1989  C  CB  . THR   B  2  10  ? 39.562  -84.800  29.379  1.00 95.19  ? 9   THR   B CB  1 
ATOM   1990  O  OG1 . THR   B  2  10  ? 38.995  -86.109  29.387  1.00 94.06  ? 9   THR   B OG1 1 
ATOM   1991  C  CG2 . THR   B  2  10  ? 40.120  -84.475  30.747  1.00 96.02  ? 9   THR   B CG2 1 
ATOM   1992  N  N   . THR   B  2  11  ? 37.053  -84.851  27.207  1.00 92.37  ? 10  THR   B N   1 
ATOM   1993  C  CA  . THR   B  2  11  ? 36.670  -85.330  25.852  1.00 95.92  ? 10  THR   B CA  1 
ATOM   1994  C  C   . THR   B  2  11  ? 35.385  -84.640  25.385  1.00 96.25  ? 10  THR   B C   1 
ATOM   1995  O  O   . THR   B  2  11  ? 34.437  -85.365  25.030  1.00 98.66  ? 10  THR   B O   1 
ATOM   1996  C  CB  . THR   B  2  11  ? 36.485  -86.853  25.841  1.00 94.42  ? 10  THR   B CB  1 
ATOM   1997  O  OG1 . THR   B  2  11  ? 35.366  -87.178  26.668  1.00 96.95  ? 10  THR   B OG1 1 
ATOM   1998  C  CG2 . THR   B  2  11  ? 37.709  -87.595  26.329  1.00 95.46  ? 10  THR   B CG2 1 
ATOM   1999  N  N   . ILE   B  2  12  ? 35.350  -83.303  25.374  1.00 96.87  ? 11  ILE   B N   1 
ATOM   2000  C  CA  . ILE   B  2  12  ? 34.198  -82.524  24.824  1.00 96.72  ? 11  ILE   B CA  1 
ATOM   2001  C  C   . ILE   B  2  12  ? 34.695  -81.521  23.779  1.00 93.42  ? 11  ILE   B C   1 
ATOM   2002  O  O   . ILE   B  2  12  ? 35.916  -81.287  23.687  1.00 88.48  ? 11  ILE   B O   1 
ATOM   2003  C  CB  . ILE   B  2  12  ? 33.369  -81.830  25.928  1.00 100.05 ? 11  ILE   B CB  1 
ATOM   2004  C  CG1 . ILE   B  2  12  ? 34.160  -80.753  26.677  1.00 99.57  ? 11  ILE   B CG1 1 
ATOM   2005  C  CG2 . ILE   B  2  12  ? 32.776  -82.863  26.874  1.00 102.33 ? 11  ILE   B CG2 1 
ATOM   2006  C  CD1 . ILE   B  2  12  ? 33.289  -79.735  27.379  1.00 99.90  ? 11  ILE   B CD1 1 
ATOM   2007  N  N   . PHE   B  2  13  ? 33.741  -80.956  23.040  1.00 93.41  ? 12  PHE   B N   1 
ATOM   2008  C  CA  . PHE   B  2  13  ? 33.930  -79.966  21.953  1.00 96.23  ? 12  PHE   B CA  1 
ATOM   2009  C  C   . PHE   B  2  13  ? 33.751  -78.561  22.534  1.00 98.51  ? 12  PHE   B C   1 
ATOM   2010  O  O   . PHE   B  2  13  ? 32.902  -78.386  23.432  1.00 101.24 ? 12  PHE   B O   1 
ATOM   2011  C  CB  . PHE   B  2  13  ? 32.911  -80.196  20.831  1.00 94.61  ? 12  PHE   B CB  1 
ATOM   2012  C  CG  . PHE   B  2  13  ? 33.241  -81.300  19.859  1.00 91.25  ? 12  PHE   B CG  1 
ATOM   2013  C  CD1 . PHE   B  2  13  ? 34.323  -81.187  19.001  1.00 89.93  ? 12  PHE   B CD1 1 
ATOM   2014  C  CD2 . PHE   B  2  13  ? 32.447  -82.433  19.772  1.00 89.46  ? 12  PHE   B CD2 1 
ATOM   2015  C  CE1 . PHE   B  2  13  ? 34.621  -82.196  18.097  1.00 87.35  ? 12  PHE   B CE1 1 
ATOM   2016  C  CE2 . PHE   B  2  13  ? 32.745  -83.440  18.867  1.00 88.22  ? 12  PHE   B CE2 1 
ATOM   2017  C  CZ  . PHE   B  2  13  ? 33.831  -83.320  18.031  1.00 86.00  ? 12  PHE   B CZ  1 
ATOM   2018  N  N   . SER   B  2  14  ? 34.523  -77.595  22.032  1.00 100.95 ? 13  SER   B N   1 
ATOM   2019  C  CA  . SER   B  2  14  ? 34.285  -76.143  22.237  1.00 103.75 ? 13  SER   B CA  1 
ATOM   2020  C  C   . SER   B  2  14  ? 33.127  -75.723  21.338  1.00 105.50 ? 13  SER   B C   1 
ATOM   2021  O  O   . SER   B  2  14  ? 32.817  -76.420  20.373  1.00 104.22 ? 13  SER   B O   1 
ATOM   2022  C  CB  . SER   B  2  14  ? 35.524  -75.335  21.954  1.00 104.04 ? 13  SER   B CB  1 
ATOM   2023  O  OG  . SER   B  2  14  ? 35.840  -75.353  20.569  1.00 103.77 ? 13  SER   B OG  1 
ATOM   2024  N  N   . PRO   B  2  15  ? 32.451  -74.584  21.614  1.00 106.54 ? 14  PRO   B N   1 
ATOM   2025  C  CA  . PRO   B  2  15  ? 31.406  -74.084  20.719  1.00 106.37 ? 14  PRO   B CA  1 
ATOM   2026  C  C   . PRO   B  2  15  ? 31.864  -73.947  19.257  1.00 105.38 ? 14  PRO   B C   1 
ATOM   2027  O  O   . PRO   B  2  15  ? 31.013  -73.971  18.381  1.00 101.89 ? 14  PRO   B O   1 
ATOM   2028  C  CB  . PRO   B  2  15  ? 31.050  -72.714  21.311  1.00 110.13 ? 14  PRO   B CB  1 
ATOM   2029  C  CG  . PRO   B  2  15  ? 31.409  -72.836  22.778  1.00 110.84 ? 14  PRO   B CG  1 
ATOM   2030  C  CD  . PRO   B  2  15  ? 32.618  -73.748  22.811  1.00 107.29 ? 14  PRO   B CD  1 
ATOM   2031  N  N   . GLU   B  2  16  ? 33.179  -73.822  19.039  1.00 104.33 ? 15  GLU   B N   1 
ATOM   2032  C  CA  . GLU   B  2  16  ? 33.813  -73.661  17.702  1.00 105.72 ? 15  GLU   B CA  1 
ATOM   2033  C  C   . GLU   B  2  16  ? 34.118  -75.030  17.078  1.00 101.23 ? 15  GLU   B C   1 
ATOM   2034  O  O   . GLU   B  2  16  ? 34.577  -75.048  15.923  1.00 95.99  ? 15  GLU   B O   1 
ATOM   2035  C  CB  . GLU   B  2  16  ? 35.100  -72.840  17.815  1.00 112.66 ? 15  GLU   B CB  1 
ATOM   2036  C  CG  . GLU   B  2  16  ? 34.876  -71.410  18.280  1.00 119.43 ? 15  GLU   B CG  1 
ATOM   2037  C  CD  . GLU   B  2  16  ? 34.790  -71.222  19.785  1.00 125.48 ? 15  GLU   B CD  1 
ATOM   2038  O  OE1 . GLU   B  2  16  ? 33.903  -70.465  20.235  1.00 127.76 ? 15  GLU   B OE1 1 
ATOM   2039  O  OE2 . GLU   B  2  16  ? 35.615  -71.825  20.506  1.00 131.64 ? 15  GLU   B OE2 1 
ATOM   2040  N  N   . GLY   B  2  17  ? 33.887  -76.127  17.807  1.00 99.84  ? 16  GLY   B N   1 
ATOM   2041  C  CA  . GLY   B  2  17  ? 34.100  -77.503  17.315  1.00 99.80  ? 16  GLY   B CA  1 
ATOM   2042  C  C   . GLY   B  2  17  ? 35.563  -77.912  17.367  1.00 99.53  ? 16  GLY   B C   1 
ATOM   2043  O  O   . GLY   B  2  17  ? 36.012  -78.613  16.437  1.00 95.74  ? 16  GLY   B O   1 
ATOM   2044  N  N   . ARG   B  2  18  ? 36.282  -77.479  18.409  1.00 101.06 ? 17  ARG   B N   1 
ATOM   2045  C  CA  . ARG   B  2  18  ? 37.674  -77.903  18.721  1.00 103.15 ? 17  ARG   B CA  1 
ATOM   2046  C  C   . ARG   B  2  18  ? 37.674  -78.676  20.041  1.00 102.45 ? 17  ARG   B C   1 
ATOM   2047  O  O   . ARG   B  2  18  ? 36.780  -78.422  20.871  1.00 104.04 ? 17  ARG   B O   1 
ATOM   2048  C  CB  . ARG   B  2  18  ? 38.607  -76.700  18.858  1.00 107.26 ? 17  ARG   B CB  1 
ATOM   2049  C  CG  . ARG   B  2  18  ? 38.774  -75.882  17.588  1.00 117.04 ? 17  ARG   B CG  1 
ATOM   2050  C  CD  . ARG   B  2  18  ? 39.424  -74.544  17.886  1.00 122.95 ? 17  ARG   B CD  1 
ATOM   2051  N  NE  . ARG   B  2  18  ? 39.635  -73.759  16.677  1.00 129.59 ? 17  ARG   B NE  1 
ATOM   2052  C  CZ  . ARG   B  2  18  ? 40.639  -73.926  15.817  1.00 133.78 ? 17  ARG   B CZ  1 
ATOM   2053  N  NH1 . ARG   B  2  18  ? 41.556  -74.861  16.015  1.00 131.33 ? 17  ARG   B NH1 1 
ATOM   2054  N  NH2 . ARG   B  2  18  ? 40.722  -73.150  14.750  1.00 138.44 ? 17  ARG   B NH2 1 
ATOM   2055  N  N   . LEU   B  2  19  ? 38.652  -79.567  20.224  1.00 105.03 ? 18  LEU   B N   1 
ATOM   2056  C  CA  . LEU   B  2  19  ? 38.835  -80.371  21.462  1.00 102.83 ? 18  LEU   B CA  1 
ATOM   2057  C  C   . LEU   B  2  19  ? 39.811  -79.632  22.386  1.00 102.72 ? 18  LEU   B C   1 
ATOM   2058  O  O   . LEU   B  2  19  ? 41.027  -79.677  22.119  1.00 101.18 ? 18  LEU   B O   1 
ATOM   2059  C  CB  . LEU   B  2  19  ? 39.341  -81.768  21.086  1.00 102.50 ? 18  LEU   B CB  1 
ATOM   2060  C  CG  . LEU   B  2  19  ? 38.405  -82.591  20.200  1.00 101.44 ? 18  LEU   B CG  1 
ATOM   2061  C  CD1 . LEU   B  2  19  ? 39.088  -83.863  19.723  1.00 99.41  ? 18  LEU   B CD1 1 
ATOM   2062  C  CD2 . LEU   B  2  19  ? 37.110  -82.924  20.930  1.00 104.96 ? 18  LEU   B CD2 1 
ATOM   2063  N  N   . TYR   B  2  20  ? 39.278  -78.966  23.417  1.00 101.02 ? 19  TYR   B N   1 
ATOM   2064  C  CA  . TYR   B  2  20  ? 40.024  -78.127  24.396  1.00 100.00 ? 19  TYR   B CA  1 
ATOM   2065  C  C   . TYR   B  2  20  ? 41.369  -78.778  24.739  1.00 98.06  ? 19  TYR   B C   1 
ATOM   2066  O  O   . TYR   B  2  20  ? 42.422  -78.152  24.514  1.00 93.35  ? 19  TYR   B O   1 
ATOM   2067  C  CB  . TYR   B  2  20  ? 39.214  -77.934  25.681  1.00 101.26 ? 19  TYR   B CB  1 
ATOM   2068  C  CG  . TYR   B  2  20  ? 38.024  -77.015  25.565  1.00 105.03 ? 19  TYR   B CG  1 
ATOM   2069  C  CD1 . TYR   B  2  20  ? 38.186  -75.665  25.296  1.00 104.62 ? 19  TYR   B CD1 1 
ATOM   2070  C  CD2 . TYR   B  2  20  ? 36.733  -77.488  25.746  1.00 106.23 ? 19  TYR   B CD2 1 
ATOM   2071  C  CE1 . TYR   B  2  20  ? 37.097  -74.812  25.196  1.00 109.95 ? 19  TYR   B CE1 1 
ATOM   2072  C  CE2 . TYR   B  2  20  ? 35.633  -76.649  25.652  1.00 109.64 ? 19  TYR   B CE2 1 
ATOM   2073  C  CZ  . TYR   B  2  20  ? 35.816  -75.306  25.375  1.00 111.04 ? 19  TYR   B CZ  1 
ATOM   2074  O  OH  . TYR   B  2  20  ? 34.738  -74.474  25.280  1.00 119.06 ? 19  TYR   B OH  1 
ATOM   2075  N  N   . GLN   B  2  21  ? 41.319  -80.006  25.262  1.00 98.50  ? 20  GLN   B N   1 
ATOM   2076  C  CA  . GLN   B  2  21  ? 42.478  -80.723  25.862  1.00 97.66  ? 20  GLN   B CA  1 
ATOM   2077  C  C   . GLN   B  2  21  ? 43.546  -81.017  24.801  1.00 99.47  ? 20  GLN   B C   1 
ATOM   2078  O  O   . GLN   B  2  21  ? 44.744  -80.921  25.141  1.00 104.26 ? 20  GLN   B O   1 
ATOM   2079  C  CB  . GLN   B  2  21  ? 42.007  -82.006  26.545  1.00 96.23  ? 20  GLN   B CB  1 
ATOM   2080  C  CG  . GLN   B  2  21  ? 41.376  -81.751  27.903  1.00 95.49  ? 20  GLN   B CG  1 
ATOM   2081  C  CD  . GLN   B  2  21  ? 42.413  -81.360  28.927  1.00 96.17  ? 20  GLN   B CD  1 
ATOM   2082  O  OE1 . GLN   B  2  21  ? 42.520  -80.204  29.325  1.00 98.31  ? 20  GLN   B OE1 1 
ATOM   2083  N  NE2 . GLN   B  2  21  ? 43.202  -82.333  29.348  1.00 98.47  ? 20  GLN   B NE2 1 
ATOM   2084  N  N   . VAL   B  2  22  ? 43.135  -81.366  23.578  1.00 96.43  ? 21  VAL   B N   1 
ATOM   2085  C  CA  . VAL   B  2  22  ? 44.061  -81.632  22.437  1.00 96.26  ? 21  VAL   B CA  1 
ATOM   2086  C  C   . VAL   B  2  22  ? 44.799  -80.332  22.104  1.00 97.77  ? 21  VAL   B C   1 
ATOM   2087  O  O   . VAL   B  2  22  ? 46.037  -80.380  21.955  1.00 96.55  ? 21  VAL   B O   1 
ATOM   2088  C  CB  . VAL   B  2  22  ? 43.318  -82.183  21.205  1.00 97.00  ? 21  VAL   B CB  1 
ATOM   2089  C  CG1 . VAL   B  2  22  ? 44.231  -82.275  19.991  1.00 97.43  ? 21  VAL   B CG1 1 
ATOM   2090  C  CG2 . VAL   B  2  22  ? 42.674  -83.531  21.489  1.00 96.18  ? 21  VAL   B CG2 1 
ATOM   2091  N  N   . GLU   B  2  23  ? 44.058  -79.224  21.990  1.00 99.39  ? 22  GLU   B N   1 
ATOM   2092  C  CA  . GLU   B  2  23  ? 44.607  -77.876  21.686  1.00 100.56 ? 22  GLU   B CA  1 
ATOM   2093  C  C   . GLU   B  2  23  ? 45.638  -77.508  22.760  1.00 93.27  ? 22  GLU   B C   1 
ATOM   2094  O  O   . GLU   B  2  23  ? 46.751  -77.096  22.386  1.00 87.74  ? 22  GLU   B O   1 
ATOM   2095  C  CB  . GLU   B  2  23  ? 43.489  -76.832  21.600  1.00 106.60 ? 22  GLU   B CB  1 
ATOM   2096  C  CG  . GLU   B  2  23  ? 42.494  -77.085  20.477  1.00 114.55 ? 22  GLU   B CG  1 
ATOM   2097  C  CD  . GLU   B  2  23  ? 43.097  -77.159  19.084  1.00 121.37 ? 22  GLU   B CD  1 
ATOM   2098  O  OE1 . GLU   B  2  23  ? 42.764  -78.112  18.346  1.00 124.92 ? 22  GLU   B OE1 1 
ATOM   2099  O  OE2 . GLU   B  2  23  ? 43.895  -76.261  18.738  1.00 136.18 ? 22  GLU   B OE2 1 
ATOM   2100  N  N   . TYR   B  2  24  ? 45.291  -77.686  24.039  1.00 92.19  ? 23  TYR   B N   1 
ATOM   2101  C  CA  . TYR   B  2  24  ? 46.134  -77.290  25.201  1.00 94.83  ? 23  TYR   B CA  1 
ATOM   2102  C  C   . TYR   B  2  24  ? 47.357  -78.211  25.307  1.00 92.92  ? 23  TYR   B C   1 
ATOM   2103  O  O   . TYR   B  2  24  ? 48.408  -77.749  25.793  1.00 95.64  ? 23  TYR   B O   1 
ATOM   2104  C  CB  . TYR   B  2  24  ? 45.332  -77.302  26.506  1.00 95.39  ? 23  TYR   B CB  1 
ATOM   2105  C  CG  . TYR   B  2  24  ? 44.119  -76.405  26.549  1.00 96.20  ? 23  TYR   B CG  1 
ATOM   2106  C  CD1 . TYR   B  2  24  ? 43.948  -75.353  25.660  1.00 97.54  ? 23  TYR   B CD1 1 
ATOM   2107  C  CD2 . TYR   B  2  24  ? 43.141  -76.597  27.512  1.00 97.11  ? 23  TYR   B CD2 1 
ATOM   2108  C  CE1 . TYR   B  2  24  ? 42.831  -74.534  25.715  1.00 100.17 ? 23  TYR   B CE1 1 
ATOM   2109  C  CE2 . TYR   B  2  24  ? 42.020  -75.786  27.582  1.00 97.83  ? 23  TYR   B CE2 1 
ATOM   2110  C  CZ  . TYR   B  2  24  ? 41.864  -74.749  26.681  1.00 99.38  ? 23  TYR   B CZ  1 
ATOM   2111  O  OH  . TYR   B  2  24  ? 40.760  -73.950  26.754  1.00 101.42 ? 23  TYR   B OH  1 
ATOM   2112  N  N   . ALA   B  2  25  ? 47.230  -79.471  24.880  1.00 91.66  ? 24  ALA   B N   1 
ATOM   2113  C  CA  . ALA   B  2  25  ? 48.340  -80.450  24.827  1.00 90.55  ? 24  ALA   B CA  1 
ATOM   2114  C  C   . ALA   B  2  25  ? 49.345  -80.028  23.748  1.00 89.87  ? 24  ALA   B C   1 
ATOM   2115  O  O   . ALA   B  2  25  ? 50.558  -80.115  24.011  1.00 91.65  ? 24  ALA   B O   1 
ATOM   2116  C  CB  . ALA   B  2  25  ? 47.808  -81.837  24.574  1.00 89.59  ? 24  ALA   B CB  1 
ATOM   2117  N  N   . LEU   B  2  26  ? 48.857  -79.594  22.579  1.00 91.99  ? 25  LEU   B N   1 
ATOM   2118  C  CA  . LEU   B  2  26  ? 49.701  -79.084  21.462  1.00 93.84  ? 25  LEU   B CA  1 
ATOM   2119  C  C   . LEU   B  2  26  ? 50.464  -77.840  21.933  1.00 95.00  ? 25  LEU   B C   1 
ATOM   2120  O  O   . LEU   B  2  26  ? 51.658  -77.719  21.589  1.00 94.30  ? 25  LEU   B O   1 
ATOM   2121  C  CB  . LEU   B  2  26  ? 48.822  -78.764  20.248  1.00 92.81  ? 25  LEU   B CB  1 
ATOM   2122  C  CG  . LEU   B  2  26  ? 48.338  -79.971  19.448  1.00 91.87  ? 25  LEU   B CG  1 
ATOM   2123  C  CD1 . LEU   B  2  26  ? 47.181  -79.586  18.537  1.00 92.03  ? 25  LEU   B CD1 1 
ATOM   2124  C  CD2 . LEU   B  2  26  ? 49.476  -80.578  18.641  1.00 90.94  ? 25  LEU   B CD2 1 
ATOM   2125  N  N   . GLU   B  2  27  ? 49.796  -76.962  22.689  1.00 98.70  ? 26  GLU   B N   1 
ATOM   2126  C  CA  . GLU   B  2  27  ? 50.396  -75.736  23.283  1.00 103.71 ? 26  GLU   B CA  1 
ATOM   2127  C  C   . GLU   B  2  27  ? 51.542  -76.152  24.215  1.00 105.15 ? 26  GLU   B C   1 
ATOM   2128  O  O   . GLU   B  2  27  ? 52.577  -75.459  24.218  1.00 110.54 ? 26  GLU   B O   1 
ATOM   2129  C  CB  . GLU   B  2  27  ? 49.333  -74.906  24.011  1.00 107.94 ? 26  GLU   B CB  1 
ATOM   2130  C  CG  . GLU   B  2  27  ? 49.861  -73.617  24.626  1.00 112.50 ? 26  GLU   B CG  1 
ATOM   2131  C  CD  . GLU   B  2  27  ? 50.499  -72.635  23.655  1.00 114.63 ? 26  GLU   B CD  1 
ATOM   2132  O  OE1 . GLU   B  2  27  ? 51.517  -72.014  24.024  1.00 120.68 ? 26  GLU   B OE1 1 
ATOM   2133  O  OE2 . GLU   B  2  27  ? 49.972  -72.484  22.534  1.00 117.26 ? 26  GLU   B OE2 1 
ATOM   2134  N  N   . SER   B  2  28  ? 51.360  -77.244  24.967  1.00 101.67 ? 27  SER   B N   1 
ATOM   2135  C  CA  . SER   B  2  28  ? 52.382  -77.838  25.870  1.00 100.31 ? 27  SER   B CA  1 
ATOM   2136  C  C   . SER   B  2  28  ? 53.595  -78.297  25.054  1.00 98.96  ? 27  SER   B C   1 
ATOM   2137  O  O   . SER   B  2  28  ? 54.734  -78.011  25.473  1.00 93.83  ? 27  SER   B O   1 
ATOM   2138  C  CB  . SER   B  2  28  ? 51.804  -78.979  26.669  1.00 99.70  ? 27  SER   B CB  1 
ATOM   2139  O  OG  . SER   B  2  28  ? 52.787  -79.569  27.508  1.00 101.19 ? 27  SER   B OG  1 
ATOM   2140  N  N   . ILE   B  2  29  ? 53.343  -78.979  23.932  1.00 100.24 ? 28  ILE   B N   1 
ATOM   2141  C  CA  . ILE   B  2  29  ? 54.383  -79.597  23.055  1.00 103.49 ? 28  ILE   B CA  1 
ATOM   2142  C  C   . ILE   B  2  29  ? 55.222  -78.495  22.395  1.00 106.15 ? 28  ILE   B C   1 
ATOM   2143  O  O   . ILE   B  2  29  ? 56.425  -78.732  22.187  1.00 108.03 ? 28  ILE   B O   1 
ATOM   2144  C  CB  . ILE   B  2  29  ? 53.733  -80.544  22.024  1.00 105.24 ? 28  ILE   B CB  1 
ATOM   2145  C  CG1 . ILE   B  2  29  ? 53.205  -81.814  22.697  1.00 103.66 ? 28  ILE   B CG1 1 
ATOM   2146  C  CG2 . ILE   B  2  29  ? 54.695  -80.876  20.890  1.00 107.79 ? 28  ILE   B CG2 1 
ATOM   2147  C  CD1 . ILE   B  2  29  ? 52.078  -82.484  21.952  1.00 103.27 ? 28  ILE   B CD1 1 
ATOM   2148  N  N   . SER   B  2  30  ? 54.624  -77.336  22.099  1.00 107.39 ? 29  SER   B N   1 
ATOM   2149  C  CA  . SER   B  2  30  ? 55.292  -76.192  21.422  1.00 109.73 ? 29  SER   B CA  1 
ATOM   2150  C  C   . SER   B  2  30  ? 56.437  -75.630  22.282  1.00 109.91 ? 29  SER   B C   1 
ATOM   2151  O  O   . SER   B  2  30  ? 57.242  -74.859  21.732  1.00 115.07 ? 29  SER   B O   1 
ATOM   2152  C  CB  . SER   B  2  30  ? 54.297  -75.116  21.055  1.00 112.16 ? 29  SER   B CB  1 
ATOM   2153  O  OG  . SER   B  2  30  ? 53.905  -74.370  22.199  1.00 115.42 ? 29  SER   B OG  1 
ATOM   2154  N  N   . HIS   B  2  31  ? 56.510  -75.983  23.573  1.00 104.69 ? 30  HIS   B N   1 
ATOM   2155  C  CA  . HIS   B  2  31  ? 57.588  -75.554  24.508  1.00 106.07 ? 30  HIS   B CA  1 
ATOM   2156  C  C   . HIS   B  2  31  ? 58.649  -76.651  24.671  1.00 103.56 ? 30  HIS   B C   1 
ATOM   2157  O  O   . HIS   B  2  31  ? 59.684  -76.368  25.300  1.00 97.44  ? 30  HIS   B O   1 
ATOM   2158  C  CB  . HIS   B  2  31  ? 57.008  -75.154  25.871  1.00 107.96 ? 30  HIS   B CB  1 
ATOM   2159  C  CG  . HIS   B  2  31  ? 55.953  -74.103  25.796  1.00 110.97 ? 30  HIS   B CG  1 
ATOM   2160  N  ND1 . HIS   B  2  31  ? 56.183  -72.863  25.231  1.00 113.61 ? 30  HIS   B ND1 1 
ATOM   2161  C  CD2 . HIS   B  2  31  ? 54.672  -74.097  26.221  1.00 110.60 ? 30  HIS   B CD2 1 
ATOM   2162  C  CE1 . HIS   B  2  31  ? 55.082  -72.142  25.303  1.00 115.34 ? 30  HIS   B CE1 1 
ATOM   2163  N  NE2 . HIS   B  2  31  ? 54.140  -72.876  25.907  1.00 112.69 ? 30  HIS   B NE2 1 
ATOM   2164  N  N   . ALA   B  2  32  ? 58.405  -77.855  24.144  1.00 103.64 ? 31  ALA   B N   1 
ATOM   2165  C  CA  . ALA   B  2  32  ? 59.357  -78.991  24.176  1.00 103.97 ? 31  ALA   B CA  1 
ATOM   2166  C  C   . ALA   B  2  32  ? 60.435  -78.779  23.108  1.00 107.40 ? 31  ALA   B C   1 
ATOM   2167  O  O   . ALA   B  2  32  ? 60.118  -78.183  22.058  1.00 107.41 ? 31  ALA   B O   1 
ATOM   2168  C  CB  . ALA   B  2  32  ? 58.629  -80.296  23.971  1.00 102.75 ? 31  ALA   B CB  1 
ATOM   2169  N  N   . GLY   B  2  33  ? 61.655  -79.257  23.374  1.00 107.90 ? 32  GLY   B N   1 
ATOM   2170  C  CA  . GLY   B  2  33  ? 62.810  -79.151  22.462  1.00 110.07 ? 32  GLY   B CA  1 
ATOM   2171  C  C   . GLY   B  2  33  ? 62.443  -79.595  21.057  1.00 110.77 ? 32  GLY   B C   1 
ATOM   2172  O  O   . GLY   B  2  33  ? 61.720  -80.603  20.926  1.00 110.40 ? 32  GLY   B O   1 
ATOM   2173  N  N   . THR   B  2  34  ? 62.903  -78.862  20.040  1.00 112.55 ? 33  THR   B N   1 
ATOM   2174  C  CA  . THR   B  2  34  ? 62.608  -79.147  18.611  1.00 113.34 ? 33  THR   B CA  1 
ATOM   2175  C  C   . THR   B  2  34  ? 63.153  -80.537  18.261  1.00 111.11 ? 33  THR   B C   1 
ATOM   2176  O  O   . THR   B  2  34  ? 64.196  -80.932  18.824  1.00 113.22 ? 33  THR   B O   1 
ATOM   2177  C  CB  . THR   B  2  34  ? 63.172  -78.063  17.681  1.00 114.99 ? 33  THR   B CB  1 
ATOM   2178  O  OG1 . THR   B  2  34  ? 62.869  -76.782  18.236  1.00 116.41 ? 33  THR   B OG1 1 
ATOM   2179  C  CG2 . THR   B  2  34  ? 62.613  -78.149  16.277  1.00 116.49 ? 33  THR   B CG2 1 
ATOM   2180  N  N   . ALA   B  2  35  ? 62.446  -81.257  17.391  1.00 107.98 ? 34  ALA   B N   1 
ATOM   2181  C  CA  . ALA   B  2  35  ? 62.907  -82.507  16.747  1.00 108.37 ? 34  ALA   B CA  1 
ATOM   2182  C  C   . ALA   B  2  35  ? 62.609  -82.414  15.250  1.00 107.08 ? 34  ALA   B C   1 
ATOM   2183  O  O   . ALA   B  2  35  ? 61.494  -81.983  14.900  1.00 107.46 ? 34  ALA   B O   1 
ATOM   2184  C  CB  . ALA   B  2  35  ? 62.239  -83.701  17.379  1.00 109.07 ? 34  ALA   B CB  1 
ATOM   2185  N  N   . ILE   B  2  36  ? 63.583  -82.778  14.412  1.00 106.45 ? 35  ILE   B N   1 
ATOM   2186  C  CA  . ILE   B  2  36  ? 63.482  -82.709  12.926  1.00 106.82 ? 35  ILE   B CA  1 
ATOM   2187  C  C   . ILE   B  2  36  ? 63.680  -84.113  12.349  1.00 105.92 ? 35  ILE   B C   1 
ATOM   2188  O  O   . ILE   B  2  36  ? 64.558  -84.850  12.840  1.00 105.69 ? 35  ILE   B O   1 
ATOM   2189  C  CB  . ILE   B  2  36  ? 64.486  -81.685  12.357  1.00 107.74 ? 35  ILE   B CB  1 
ATOM   2190  C  CG1 . ILE   B  2  36  ? 64.052  -80.260  12.706  1.00 110.22 ? 35  ILE   B CG1 1 
ATOM   2191  C  CG2 . ILE   B  2  36  ? 64.670  -81.869  10.856  1.00 109.50 ? 35  ILE   B CG2 1 
ATOM   2192  C  CD1 . ILE   B  2  36  ? 65.046  -79.188  12.324  1.00 114.70 ? 35  ILE   B CD1 1 
ATOM   2193  N  N   . GLY   B  2  37  ? 62.861  -84.459  11.355  1.00 103.61 ? 36  GLY   B N   1 
ATOM   2194  C  CA  . GLY   B  2  37  ? 63.045  -85.630  10.481  1.00 105.88 ? 36  GLY   B CA  1 
ATOM   2195  C  C   . GLY   B  2  37  ? 63.193  -85.183  9.039   1.00 107.96 ? 36  GLY   B C   1 
ATOM   2196  O  O   . GLY   B  2  37  ? 62.404  -84.314  8.616   1.00 107.56 ? 36  GLY   B O   1 
ATOM   2197  N  N   . ILE   B  2  38  ? 64.183  -85.722  8.320   1.00 111.98 ? 37  ILE   B N   1 
ATOM   2198  C  CA  . ILE   B  2  38  ? 64.403  -85.453  6.867   1.00 113.34 ? 37  ILE   B CA  1 
ATOM   2199  C  C   . ILE   B  2  38  ? 64.615  -86.783  6.133   1.00 113.79 ? 37  ILE   B C   1 
ATOM   2200  O  O   . ILE   B  2  38  ? 65.565  -87.519  6.479   1.00 108.97 ? 37  ILE   B O   1 
ATOM   2201  C  CB  . ILE   B  2  38  ? 65.580  -84.485  6.643   1.00 114.61 ? 37  ILE   B CB  1 
ATOM   2202  C  CG1 . ILE   B  2  38  ? 65.325  -83.128  7.305   1.00 114.35 ? 37  ILE   B CG1 1 
ATOM   2203  C  CG2 . ILE   B  2  38  ? 65.872  -84.342  5.155   1.00 116.35 ? 37  ILE   B CG2 1 
ATOM   2204  C  CD1 . ILE   B  2  38  ? 66.519  -82.207  7.298   1.00 117.33 ? 37  ILE   B CD1 1 
ATOM   2205  N  N   . MET   B  2  39  ? 63.769  -87.047  5.135   1.00 113.24 ? 38  MET   B N   1 
ATOM   2206  C  CA  . MET   B  2  39  ? 63.771  -88.287  4.319   1.00 114.56 ? 38  MET   B CA  1 
ATOM   2207  C  C   . MET   B  2  39  ? 64.527  -88.021  3.013   1.00 111.23 ? 38  MET   B C   1 
ATOM   2208  O  O   . MET   B  2  39  ? 64.029  -87.229  2.189   1.00 106.26 ? 38  MET   B O   1 
ATOM   2209  C  CB  . MET   B  2  39  ? 62.334  -88.730  4.021   1.00 118.08 ? 38  MET   B CB  1 
ATOM   2210  C  CG  . MET   B  2  39  ? 62.227  -90.123  3.430   1.00 121.98 ? 38  MET   B CG  1 
ATOM   2211  S  SD  . MET   B  2  39  ? 62.103  -90.106  1.626   1.00 130.14 ? 38  MET   B SD  1 
ATOM   2212  C  CE  . MET   B  2  39  ? 60.450  -89.450  1.410   1.00 131.34 ? 38  MET   B CE  1 
ATOM   2213  N  N   . ALA   B  2  40  ? 65.700  -88.643  2.857   1.00 114.43 ? 39  ALA   B N   1 
ATOM   2214  C  CA  . ALA   B  2  40  ? 66.509  -88.654  1.616   1.00 118.14 ? 39  ALA   B CA  1 
ATOM   2215  C  C   . ALA   B  2  40  ? 66.164  -89.912  0.813   1.00 120.75 ? 39  ALA   B C   1 
ATOM   2216  O  O   . ALA   B  2  40  ? 65.409  -90.762  1.329   1.00 123.49 ? 39  ALA   B O   1 
ATOM   2217  C  CB  . ALA   B  2  40  ? 67.979  -88.596  1.951   1.00 115.80 ? 39  ALA   B CB  1 
ATOM   2218  N  N   . SER   B  2  41  ? 66.700  -90.025  -0.405  1.00 125.69 ? 40  SER   B N   1 
ATOM   2219  C  CA  . SER   B  2  41  ? 66.448  -91.155  -1.338  1.00 126.78 ? 40  SER   B CA  1 
ATOM   2220  C  C   . SER   B  2  41  ? 67.148  -92.429  -0.843  1.00 127.06 ? 40  SER   B C   1 
ATOM   2221  O  O   . SER   B  2  41  ? 66.637  -93.523  -1.149  1.00 128.74 ? 40  SER   B O   1 
ATOM   2222  C  CB  . SER   B  2  41  ? 66.869  -90.800  -2.741  1.00 129.27 ? 40  SER   B CB  1 
ATOM   2223  O  OG  . SER   B  2  41  ? 68.182  -90.260  -2.757  1.00 128.91 ? 40  SER   B OG  1 
ATOM   2224  N  N   . ASP   B  2  42  ? 68.255  -92.293  -0.101  1.00 128.64 ? 41  ASP   B N   1 
ATOM   2225  C  CA  . ASP   B  2  42  ? 69.111  -93.426  0.352   1.00 127.54 ? 41  ASP   B CA  1 
ATOM   2226  C  C   . ASP   B  2  42  ? 69.158  -93.493  1.886   1.00 125.29 ? 41  ASP   B C   1 
ATOM   2227  O  O   . ASP   B  2  42  ? 70.118  -94.093  2.412   1.00 129.51 ? 41  ASP   B O   1 
ATOM   2228  C  CB  . ASP   B  2  42  ? 70.526  -93.311  -0.223  1.00 127.73 ? 41  ASP   B CB  1 
ATOM   2229  C  CG  . ASP   B  2  42  ? 71.270  -92.069  0.235   1.00 129.02 ? 41  ASP   B CG  1 
ATOM   2230  O  OD1 . ASP   B  2  42  ? 70.656  -90.984  0.221   1.00 125.75 ? 41  ASP   B OD1 1 
ATOM   2231  O  OD2 . ASP   B  2  42  ? 72.450  -92.197  0.616   1.00 123.48 ? 41  ASP   B OD2 1 
ATOM   2232  N  N   . GLY   B  2  43  ? 68.168  -92.922  2.582   1.00 120.09 ? 42  GLY   B N   1 
ATOM   2233  C  CA  . GLY   B  2  43  ? 68.056  -93.026  4.051   1.00 117.37 ? 42  GLY   B CA  1 
ATOM   2234  C  C   . GLY   B  2  43  ? 67.267  -91.888  4.672   1.00 112.14 ? 42  GLY   B C   1 
ATOM   2235  O  O   . GLY   B  2  43  ? 66.803  -91.005  3.929   1.00 113.98 ? 42  GLY   B O   1 
ATOM   2236  N  N   . ILE   B  2  44  ? 67.118  -91.925  5.999   1.00 110.36 ? 43  ILE   B N   1 
ATOM   2237  C  CA  . ILE   B  2  44  ? 66.390  -90.905  6.812   1.00 110.85 ? 43  ILE   B CA  1 
ATOM   2238  C  C   . ILE   B  2  44  ? 67.326  -90.398  7.913   1.00 115.42 ? 43  ILE   B C   1 
ATOM   2239  O  O   . ILE   B  2  44  ? 68.104  -91.212  8.449   1.00 121.07 ? 43  ILE   B O   1 
ATOM   2240  C  CB  . ILE   B  2  44  ? 65.091  -91.486  7.407   1.00 107.43 ? 43  ILE   B CB  1 
ATOM   2241  C  CG1 . ILE   B  2  44  ? 64.187  -92.084  6.327   1.00 109.29 ? 43  ILE   B CG1 1 
ATOM   2242  C  CG2 . ILE   B  2  44  ? 64.361  -90.436  8.233   1.00 104.35 ? 43  ILE   B CG2 1 
ATOM   2243  C  CD1 . ILE   B  2  44  ? 63.063  -92.935  6.870   1.00 111.24 ? 43  ILE   B CD1 1 
ATOM   2244  N  N   . VAL   B  2  45  ? 67.233  -89.103  8.228   1.00 113.89 ? 44  VAL   B N   1 
ATOM   2245  C  CA  . VAL   B  2  45  ? 67.922  -88.442  9.375   1.00 113.19 ? 44  VAL   B CA  1 
ATOM   2246  C  C   . VAL   B  2  45  ? 66.877  -88.127  10.450  1.00 109.99 ? 44  VAL   B C   1 
ATOM   2247  O  O   . VAL   B  2  45  ? 65.796  -87.623  10.088  1.00 111.03 ? 44  VAL   B O   1 
ATOM   2248  C  CB  . VAL   B  2  45  ? 68.650  -87.162  8.926   1.00 114.76 ? 44  VAL   B CB  1 
ATOM   2249  C  CG1 . VAL   B  2  45  ? 69.299  -86.433  10.095  1.00 115.46 ? 44  VAL   B CG1 1 
ATOM   2250  C  CG2 . VAL   B  2  45  ? 69.674  -87.453  7.841   1.00 117.27 ? 44  VAL   B CG2 1 
ATOM   2251  N  N   . LEU   B  2  46  ? 67.195  -88.417  11.714  1.00 108.54 ? 45  LEU   B N   1 
ATOM   2252  C  CA  . LEU   B  2  46  ? 66.461  -87.913  12.905  1.00 106.94 ? 45  LEU   B CA  1 
ATOM   2253  C  C   . LEU   B  2  46  ? 67.417  -87.050  13.731  1.00 107.06 ? 45  LEU   B C   1 
ATOM   2254  O  O   . LEU   B  2  46  ? 68.489  -87.554  14.116  1.00 106.93 ? 45  LEU   B O   1 
ATOM   2255  C  CB  . LEU   B  2  46  ? 65.929  -89.083  13.739  1.00 106.20 ? 45  LEU   B CB  1 
ATOM   2256  C  CG  . LEU   B  2  46  ? 64.670  -89.776  13.219  1.00 104.98 ? 45  LEU   B CG  1 
ATOM   2257  C  CD1 . LEU   B  2  46  ? 64.257  -90.889  14.169  1.00 105.87 ? 45  LEU   B CD1 1 
ATOM   2258  C  CD2 . LEU   B  2  46  ? 63.518  -88.798  13.029  1.00 102.98 ? 45  LEU   B CD2 1 
ATOM   2259  N  N   . ALA   B  2  47  ? 67.032  -85.796  13.969  1.00 108.31 ? 46  ALA   B N   1 
ATOM   2260  C  CA  . ALA   B  2  47  ? 67.766  -84.807  14.790  1.00 111.60 ? 46  ALA   B CA  1 
ATOM   2261  C  C   . ALA   B  2  47  ? 66.797  -84.227  15.822  1.00 109.79 ? 46  ALA   B C   1 
ATOM   2262  O  O   . ALA   B  2  47  ? 65.634  -83.970  15.458  1.00 108.15 ? 46  ALA   B O   1 
ATOM   2263  C  CB  . ALA   B  2  47  ? 68.343  -83.730  13.903  1.00 112.81 ? 46  ALA   B CB  1 
ATOM   2264  N  N   . ALA   B  2  48  ? 67.248  -84.050  17.065  1.00 111.36 ? 47  ALA   B N   1 
ATOM   2265  C  CA  . ALA   B  2  48  ? 66.427  -83.483  18.157  1.00 110.77 ? 47  ALA   B CA  1 
ATOM   2266  C  C   . ALA   B  2  48  ? 67.310  -82.727  19.154  1.00 114.44 ? 47  ALA   B C   1 
ATOM   2267  O  O   . ALA   B  2  48  ? 68.429  -83.195  19.444  1.00 111.54 ? 47  ALA   B O   1 
ATOM   2268  C  CB  . ALA   B  2  48  ? 65.638  -84.578  18.824  1.00 110.05 ? 47  ALA   B CB  1 
ATOM   2269  N  N   . GLU   B  2  49  ? 66.800  -81.594  19.643  1.00 119.61 ? 48  GLU   B N   1 
ATOM   2270  C  CA  . GLU   B  2  49  ? 67.473  -80.694  20.613  1.00 126.81 ? 48  GLU   B CA  1 
ATOM   2271  C  C   . GLU   B  2  49  ? 67.001  -81.053  22.025  1.00 131.05 ? 48  GLU   B C   1 
ATOM   2272  O  O   . GLU   B  2  49  ? 65.784  -80.959  22.275  1.00 132.13 ? 48  GLU   B O   1 
ATOM   2273  C  CB  . GLU   B  2  49  ? 67.149  -79.234  20.285  1.00 129.91 ? 48  GLU   B CB  1 
ATOM   2274  C  CG  . GLU   B  2  49  ? 68.060  -78.237  20.980  1.00 133.69 ? 48  GLU   B CG  1 
ATOM   2275  C  CD  . GLU   B  2  49  ? 67.692  -76.775  20.790  1.00 135.69 ? 48  GLU   B CD  1 
ATOM   2276  O  OE1 . GLU   B  2  49  ? 66.659  -76.497  20.142  1.00 138.01 ? 48  GLU   B OE1 1 
ATOM   2277  O  OE2 . GLU   B  2  49  ? 68.441  -75.915  21.293  1.00 139.08 ? 48  GLU   B OE2 1 
ATOM   2278  N  N   . ARG   B  2  50  ? 67.929  -81.448  22.902  1.00 135.77 ? 49  ARG   B N   1 
ATOM   2279  C  CA  . ARG   B  2  50  ? 67.653  -81.751  24.333  1.00 141.93 ? 49  ARG   B CA  1 
ATOM   2280  C  C   . ARG   B  2  50  ? 67.195  -80.470  25.036  1.00 144.72 ? 49  ARG   B C   1 
ATOM   2281  O  O   . ARG   B  2  50  ? 67.710  -79.388  24.687  1.00 141.19 ? 49  ARG   B O   1 
ATOM   2282  C  CB  . ARG   B  2  50  ? 68.900  -82.302  25.030  1.00 147.06 ? 49  ARG   B CB  1 
ATOM   2283  C  CG  . ARG   B  2  50  ? 69.274  -83.717  24.619  1.00 151.90 ? 49  ARG   B CG  1 
ATOM   2284  C  CD  . ARG   B  2  50  ? 70.655  -84.082  25.127  1.00 154.00 ? 49  ARG   B CD  1 
ATOM   2285  N  NE  . ARG   B  2  50  ? 71.011  -85.458  24.808  1.00 153.42 ? 49  ARG   B NE  1 
ATOM   2286  C  CZ  . ARG   B  2  50  ? 70.779  -86.516  25.582  1.00 153.57 ? 49  ARG   B CZ  1 
ATOM   2287  N  NH1 . ARG   B  2  50  ? 70.185  -86.382  26.758  1.00 151.08 ? 49  ARG   B NH1 1 
ATOM   2288  N  NH2 . ARG   B  2  50  ? 71.150  -87.715  25.168  1.00 154.65 ? 49  ARG   B NH2 1 
ATOM   2289  N  N   . LYS   B  2  51  ? 66.275  -80.592  25.997  1.00 151.76 ? 50  LYS   B N   1 
ATOM   2290  C  CA  . LYS   B  2  51  ? 65.721  -79.433  26.746  1.00 156.83 ? 50  LYS   B CA  1 
ATOM   2291  C  C   . LYS   B  2  51  ? 66.793  -78.931  27.724  1.00 164.74 ? 50  LYS   B C   1 
ATOM   2292  O  O   . LYS   B  2  51  ? 67.423  -79.775  28.395  1.00 165.85 ? 50  LYS   B O   1 
ATOM   2293  C  CB  . LYS   B  2  51  ? 64.402  -79.801  27.435  1.00 154.23 ? 50  LYS   B CB  1 
ATOM   2294  C  CG  . LYS   B  2  51  ? 63.463  -78.631  27.709  1.00 149.04 ? 50  LYS   B CG  1 
ATOM   2295  C  CD  . LYS   B  2  51  ? 63.013  -77.890  26.459  1.00 144.93 ? 50  LYS   B CD  1 
ATOM   2296  C  CE  . LYS   B  2  51  ? 63.801  -76.626  26.184  1.00 143.59 ? 50  LYS   B CE  1 
ATOM   2297  N  NZ  . LYS   B  2  51  ? 63.535  -76.095  24.827  1.00 142.82 ? 50  LYS   B NZ  1 
ATOM   2298  N  N   . VAL   B  2  52  ? 66.970  -77.604  27.782  1.00 168.82 ? 51  VAL   B N   1 
ATOM   2299  C  CA  . VAL   B  2  52  ? 68.112  -76.868  28.412  1.00 166.14 ? 51  VAL   B CA  1 
ATOM   2300  C  C   . VAL   B  2  52  ? 68.875  -77.798  29.370  1.00 164.94 ? 51  VAL   B C   1 
ATOM   2301  O  O   . VAL   B  2  52  ? 68.358  -78.088  30.470  1.00 162.53 ? 51  VAL   B O   1 
ATOM   2302  C  CB  . VAL   B  2  52  ? 67.642  -75.576  29.114  1.00 165.47 ? 51  VAL   B CB  1 
ATOM   2303  C  CG1 . VAL   B  2  52  ? 68.800  -74.830  29.763  1.00 162.79 ? 51  VAL   B CG1 1 
ATOM   2304  C  CG2 . VAL   B  2  52  ? 66.892  -74.647  28.166  1.00 162.56 ? 51  VAL   B CG2 1 
ATOM   2305  N  N   . THR   B  2  53  ? 70.071  -78.225  28.954  1.00 158.81 ? 52  THR   B N   1 
ATOM   2306  C  CA  . THR   B  2  53  ? 70.947  -79.203  29.657  1.00 157.10 ? 52  THR   B CA  1 
ATOM   2307  C  C   . THR   B  2  53  ? 71.633  -78.527  30.853  1.00 153.75 ? 52  THR   B C   1 
ATOM   2308  O  O   . THR   B  2  53  ? 71.782  -77.288  30.832  1.00 156.70 ? 52  THR   B O   1 
ATOM   2309  C  CB  . THR   B  2  53  ? 71.942  -79.832  28.666  1.00 161.39 ? 52  THR   B CB  1 
ATOM   2310  O  OG1 . THR   B  2  53  ? 71.521  -81.175  28.424  1.00 162.60 ? 52  THR   B OG1 1 
ATOM   2311  C  CG2 . THR   B  2  53  ? 73.380  -79.835  29.143  1.00 161.46 ? 52  THR   B CG2 1 
ATOM   2312  N  N   . SER   B  2  54  ? 72.010  -79.330  31.855  1.00 145.38 ? 53  SER   B N   1 
ATOM   2313  C  CA  . SER   B  2  54  ? 72.953  -78.987  32.954  1.00 141.83 ? 53  SER   B CA  1 
ATOM   2314  C  C   . SER   B  2  54  ? 74.285  -79.709  32.711  1.00 139.69 ? 53  SER   B C   1 
ATOM   2315  O  O   . SER   B  2  54  ? 74.250  -80.853  32.218  1.00 133.33 ? 53  SER   B O   1 
ATOM   2316  C  CB  . SER   B  2  54  ? 72.369  -79.347  34.298  1.00 136.93 ? 53  SER   B CB  1 
ATOM   2317  O  OG  . SER   B  2  54  ? 73.347  -79.253  35.324  1.00 135.84 ? 53  SER   B OG  1 
ATOM   2318  N  N   . THR   B  2  55  ? 75.410  -79.070  33.051  1.00 141.23 ? 54  THR   B N   1 
ATOM   2319  C  CA  . THR   B  2  55  ? 76.791  -79.569  32.781  1.00 141.74 ? 54  THR   B CA  1 
ATOM   2320  C  C   . THR   B  2  55  ? 77.035  -80.911  33.492  1.00 141.19 ? 54  THR   B C   1 
ATOM   2321  O  O   . THR   B  2  55  ? 77.899  -81.669  33.006  1.00 141.32 ? 54  THR   B O   1 
ATOM   2322  C  CB  . THR   B  2  55  ? 77.873  -78.530  33.126  1.00 141.67 ? 54  THR   B CB  1 
ATOM   2323  O  OG1 . THR   B  2  55  ? 79.075  -79.231  33.446  1.00 139.78 ? 54  THR   B OG1 1 
ATOM   2324  C  CG2 . THR   B  2  55  ? 77.531  -77.614  34.282  1.00 142.54 ? 54  THR   B CG2 1 
ATOM   2325  N  N   . LEU   B  2  56  ? 76.307  -81.206  34.576  1.00 141.97 ? 55  LEU   B N   1 
ATOM   2326  C  CA  . LEU   B  2  56  ? 76.488  -82.441  35.395  1.00 141.21 ? 55  LEU   B CA  1 
ATOM   2327  C  C   . LEU   B  2  56  ? 75.553  -83.569  34.932  1.00 136.46 ? 55  LEU   B C   1 
ATOM   2328  O  O   . LEU   B  2  56  ? 75.565  -84.630  35.588  1.00 130.70 ? 55  LEU   B O   1 
ATOM   2329  C  CB  . LEU   B  2  56  ? 76.255  -82.104  36.873  1.00 141.63 ? 55  LEU   B CB  1 
ATOM   2330  C  CG  . LEU   B  2  56  ? 77.484  -82.182  37.781  1.00 144.28 ? 55  LEU   B CG  1 
ATOM   2331  C  CD1 . LEU   B  2  56  ? 78.704  -81.522  37.147  1.00 148.15 ? 55  LEU   B CD1 1 
ATOM   2332  C  CD2 . LEU   B  2  56  ? 77.181  -81.557  39.134  1.00 145.04 ? 55  LEU   B CD2 1 
ATOM   2333  N  N   . LEU   B  2  57  ? 74.793  -83.373  33.848  1.00 138.24 ? 56  LEU   B N   1 
ATOM   2334  C  CA  . LEU   B  2  57  ? 73.953  -84.439  33.234  1.00 136.50 ? 56  LEU   B CA  1 
ATOM   2335  C  C   . LEU   B  2  57  ? 74.876  -85.470  32.575  1.00 136.86 ? 56  LEU   B C   1 
ATOM   2336  O  O   . LEU   B  2  57  ? 75.858  -85.052  31.929  1.00 136.41 ? 56  LEU   B O   1 
ATOM   2337  C  CB  . LEU   B  2  57  ? 72.994  -83.831  32.204  1.00 138.28 ? 56  LEU   B CB  1 
ATOM   2338  C  CG  . LEU   B  2  57  ? 71.809  -84.717  31.812  1.00 136.92 ? 56  LEU   B CG  1 
ATOM   2339  C  CD1 . LEU   B  2  57  ? 70.604  -84.430  32.695  1.00 137.59 ? 56  LEU   B CD1 1 
ATOM   2340  C  CD2 . LEU   B  2  57  ? 71.445  -84.540  30.344  1.00 136.17 ? 56  LEU   B CD2 1 
ATOM   2341  N  N   . GLU   B  2  58  ? 74.575  -86.762  32.742  1.00 136.14 ? 57  GLU   B N   1 
ATOM   2342  C  CA  . GLU   B  2  58  ? 75.283  -87.882  32.063  1.00 137.66 ? 57  GLU   B CA  1 
ATOM   2343  C  C   . GLU   B  2  58  ? 74.743  -87.990  30.633  1.00 135.72 ? 57  GLU   B C   1 
ATOM   2344  O  O   . GLU   B  2  58  ? 73.574  -88.383  30.476  1.00 127.82 ? 57  GLU   B O   1 
ATOM   2345  C  CB  . GLU   B  2  58  ? 75.093  -89.187  32.838  1.00 136.28 ? 57  GLU   B CB  1 
ATOM   2346  C  CG  . GLU   B  2  58  ? 76.016  -90.302  32.380  1.00 141.78 ? 57  GLU   B CG  1 
ATOM   2347  C  CD  . GLU   B  2  58  ? 77.491  -90.055  32.648  1.00 145.22 ? 57  GLU   B CD  1 
ATOM   2348  O  OE1 . GLU   B  2  58  ? 78.224  -89.759  31.682  1.00 151.15 ? 57  GLU   B OE1 1 
ATOM   2349  O  OE2 . GLU   B  2  58  ? 77.904  -90.169  33.819  1.00 142.89 ? 57  GLU   B OE2 1 
ATOM   2350  N  N   . GLN   B  2  59  ? 75.564  -87.646  29.636  1.00 141.41 ? 58  GLN   B N   1 
ATOM   2351  C  CA  . GLN   B  2  59  ? 75.115  -87.383  28.241  1.00 150.93 ? 58  GLN   B CA  1 
ATOM   2352  C  C   . GLN   B  2  59  ? 75.123  -88.681  27.419  1.00 151.69 ? 58  GLN   B C   1 
ATOM   2353  O  O   . GLN   B  2  59  ? 74.249  -88.809  26.539  1.00 154.71 ? 58  GLN   B O   1 
ATOM   2354  C  CB  . GLN   B  2  59  ? 75.986  -86.294  27.606  1.00 156.68 ? 58  GLN   B CB  1 
ATOM   2355  C  CG  . GLN   B  2  59  ? 75.235  -85.394  26.631  1.00 163.77 ? 58  GLN   B CG  1 
ATOM   2356  C  CD  . GLN   B  2  59  ? 75.341  -85.854  25.197  1.00 165.47 ? 58  GLN   B CD  1 
ATOM   2357  O  OE1 . GLN   B  2  59  ? 74.360  -86.268  24.583  1.00 168.13 ? 58  GLN   B OE1 1 
ATOM   2358  N  NE2 . GLN   B  2  59  ? 76.542  -85.773  24.646  1.00 173.73 ? 58  GLN   B NE2 1 
ATOM   2359  N  N   . ASP   B  2  60  ? 76.054  -89.605  27.689  1.00 154.54 ? 59  ASP   B N   1 
ATOM   2360  C  CA  . ASP   B  2  60  ? 76.269  -90.830  26.864  1.00 156.77 ? 59  ASP   B CA  1 
ATOM   2361  C  C   . ASP   B  2  60  ? 75.210  -91.895  27.191  1.00 155.81 ? 59  ASP   B C   1 
ATOM   2362  O  O   . ASP   B  2  60  ? 74.616  -92.431  26.232  1.00 152.07 ? 59  ASP   B O   1 
ATOM   2363  C  CB  . ASP   B  2  60  ? 77.693  -91.382  26.995  1.00 162.70 ? 59  ASP   B CB  1 
ATOM   2364  C  CG  . ASP   B  2  60  ? 78.213  -91.522  28.415  1.00 166.03 ? 59  ASP   B CG  1 
ATOM   2365  O  OD1 . ASP   B  2  60  ? 77.398  -91.433  29.354  1.00 172.83 ? 59  ASP   B OD1 1 
ATOM   2366  O  OD2 . ASP   B  2  60  ? 79.435  -91.714  28.570  1.00 167.81 ? 59  ASP   B OD2 1 
ATOM   2367  N  N   . THR   B  2  61  ? 74.976  -92.193  28.476  1.00 154.84 ? 60  THR   B N   1 
ATOM   2368  C  CA  . THR   B  2  61  ? 73.993  -93.215  28.942  1.00 153.93 ? 60  THR   B CA  1 
ATOM   2369  C  C   . THR   B  2  61  ? 72.581  -92.614  28.995  1.00 154.39 ? 60  THR   B C   1 
ATOM   2370  O  O   . THR   B  2  61  ? 71.755  -93.131  29.778  1.00 143.43 ? 60  THR   B O   1 
ATOM   2371  C  CB  . THR   B  2  61  ? 74.369  -93.788  30.316  1.00 153.72 ? 60  THR   B CB  1 
ATOM   2372  O  OG1 . THR   B  2  61  ? 74.319  -92.737  31.281  1.00 155.25 ? 60  THR   B OG1 1 
ATOM   2373  C  CG2 . THR   B  2  61  ? 75.737  -94.433  30.343  1.00 154.48 ? 60  THR   B CG2 1 
ATOM   2374  N  N   . SER   B  2  62  ? 72.306  -91.585  28.186  1.00 159.98 ? 61  SER   B N   1 
ATOM   2375  C  CA  . SER   B  2  62  ? 71.047  -90.795  28.211  1.00 161.68 ? 61  SER   B CA  1 
ATOM   2376  C  C   . SER   B  2  62  ? 70.216  -91.078  26.955  1.00 159.36 ? 61  SER   B C   1 
ATOM   2377  O  O   . SER   B  2  62  ? 70.805  -91.270  25.871  1.00 162.47 ? 61  SER   B O   1 
ATOM   2378  C  CB  . SER   B  2  62  ? 71.334  -89.322  28.362  1.00 161.21 ? 61  SER   B CB  1 
ATOM   2379  O  OG  . SER   B  2  62  ? 70.131  -88.570  28.444  1.00 163.17 ? 61  SER   B OG  1 
ATOM   2380  N  N   . THR   B  2  63  ? 68.892  -91.115  27.123  1.00 151.06 ? 62  THR   B N   1 
ATOM   2381  C  CA  . THR   B  2  63  ? 67.881  -91.195  26.037  1.00 145.02 ? 62  THR   B CA  1 
ATOM   2382  C  C   . THR   B  2  63  ? 66.648  -90.396  26.469  1.00 141.75 ? 62  THR   B C   1 
ATOM   2383  O  O   . THR   B  2  63  ? 66.073  -90.723  27.527  1.00 143.45 ? 62  THR   B O   1 
ATOM   2384  C  CB  . THR   B  2  63  ? 67.521  -92.647  25.703  1.00 140.47 ? 62  THR   B CB  1 
ATOM   2385  O  OG1 . THR   B  2  63  ? 68.721  -93.415  25.608  1.00 131.75 ? 62  THR   B OG1 1 
ATOM   2386  C  CG2 . THR   B  2  63  ? 66.750  -92.762  24.407  1.00 139.46 ? 62  THR   B CG2 1 
ATOM   2387  N  N   . GLU   B  2  64  ? 66.276  -89.386  25.682  1.00 137.24 ? 63  GLU   B N   1 
ATOM   2388  C  CA  . GLU   B  2  64  ? 65.190  -88.418  25.997  1.00 137.36 ? 63  GLU   B CA  1 
ATOM   2389  C  C   . GLU   B  2  64  ? 64.289  -88.241  24.768  1.00 132.27 ? 63  GLU   B C   1 
ATOM   2390  O  O   . GLU   B  2  64  ? 63.055  -88.181  24.943  1.00 134.84 ? 63  GLU   B O   1 
ATOM   2391  C  CB  . GLU   B  2  64  ? 65.816  -87.092  26.442  1.00 145.06 ? 63  GLU   B CB  1 
ATOM   2392  C  CG  . GLU   B  2  64  ? 64.816  -85.990  26.756  1.00 149.39 ? 63  GLU   B CG  1 
ATOM   2393  C  CD  . GLU   B  2  64  ? 65.417  -84.594  26.804  1.00 152.58 ? 63  GLU   B CD  1 
ATOM   2394  O  OE1 . GLU   B  2  64  ? 64.707  -83.634  26.441  1.00 158.05 ? 63  GLU   B OE1 1 
ATOM   2395  O  OE2 . GLU   B  2  64  ? 66.593  -84.469  27.204  1.00 156.63 ? 63  GLU   B OE2 1 
ATOM   2396  N  N   . LYS   B  2  65  ? 64.894  -88.171  23.579  1.00 124.13 ? 64  LYS   B N   1 
ATOM   2397  C  CA  . LYS   B  2  65  ? 64.254  -87.719  22.318  1.00 117.46 ? 64  LYS   B CA  1 
ATOM   2398  C  C   . LYS   B  2  65  ? 64.079  -88.900  21.351  1.00 106.91 ? 64  LYS   B C   1 
ATOM   2399  O  O   . LYS   B  2  65  ? 62.964  -89.055  20.815  1.00 101.26 ? 64  LYS   B O   1 
ATOM   2400  C  CB  . LYS   B  2  65  ? 65.105  -86.595  21.717  1.00 119.93 ? 64  LYS   B CB  1 
ATOM   2401  C  CG  . LYS   B  2  65  ? 64.993  -85.252  22.428  1.00 123.42 ? 64  LYS   B CG  1 
ATOM   2402  C  CD  . LYS   B  2  65  ? 63.743  -84.506  22.027  1.00 121.23 ? 64  LYS   B CD  1 
ATOM   2403  C  CE  . LYS   B  2  65  ? 63.415  -83.310  22.891  1.00 120.65 ? 64  LYS   B CE  1 
ATOM   2404  N  NZ  . LYS   B  2  65  ? 62.184  -82.644  22.407  1.00 119.10 ? 64  LYS   B NZ  1 
ATOM   2405  N  N   . LEU   B  2  66  ? 65.130  -89.703  21.146  1.00 102.71 ? 65  LEU   B N   1 
ATOM   2406  C  CA  . LEU   B  2  66  ? 65.209  -90.745  20.081  1.00 102.26 ? 65  LEU   B CA  1 
ATOM   2407  C  C   . LEU   B  2  66  ? 65.120  -92.151  20.688  1.00 101.54 ? 65  LEU   B C   1 
ATOM   2408  O  O   . LEU   B  2  66  ? 66.017  -92.517  21.474  1.00 103.75 ? 65  LEU   B O   1 
ATOM   2409  C  CB  . LEU   B  2  66  ? 66.526  -90.573  19.319  1.00 99.51  ? 65  LEU   B CB  1 
ATOM   2410  C  CG  . LEU   B  2  66  ? 66.466  -89.703  18.067  1.00 97.35  ? 65  LEU   B CG  1 
ATOM   2411  C  CD1 . LEU   B  2  66  ? 65.675  -88.428  18.308  1.00 97.95  ? 65  LEU   B CD1 1 
ATOM   2412  C  CD2 . LEU   B  2  66  ? 67.870  -89.374  17.589  1.00 99.46  ? 65  LEU   B CD2 1 
ATOM   2413  N  N   . TYR   B  2  67  ? 64.103  -92.923  20.291  1.00 98.84  ? 66  TYR   B N   1 
ATOM   2414  C  CA  . TYR   B  2  67  ? 63.837  -94.302  20.779  1.00 97.08  ? 66  TYR   B CA  1 
ATOM   2415  C  C   . TYR   B  2  67  ? 63.695  -95.261  19.593  1.00 96.17  ? 66  TYR   B C   1 
ATOM   2416  O  O   . TYR   B  2  67  ? 63.199  -94.865  18.524  1.00 89.64  ? 66  TYR   B O   1 
ATOM   2417  C  CB  . TYR   B  2  67  ? 62.587  -94.332  21.661  1.00 94.86  ? 66  TYR   B CB  1 
ATOM   2418  C  CG  . TYR   B  2  67  ? 62.720  -93.568  22.954  1.00 96.87  ? 66  TYR   B CG  1 
ATOM   2419  C  CD1 . TYR   B  2  67  ? 62.349  -92.236  23.034  1.00 98.50  ? 66  TYR   B CD1 1 
ATOM   2420  C  CD2 . TYR   B  2  67  ? 63.215  -94.172  24.098  1.00 96.64  ? 66  TYR   B CD2 1 
ATOM   2421  C  CE1 . TYR   B  2  67  ? 62.465  -91.523  24.216  1.00 103.31 ? 66  TYR   B CE1 1 
ATOM   2422  C  CE2 . TYR   B  2  67  ? 63.336  -93.475  25.288  1.00 99.64  ? 66  TYR   B CE2 1 
ATOM   2423  C  CZ  . TYR   B  2  67  ? 62.959  -92.145  25.348  1.00 102.73 ? 66  TYR   B CZ  1 
ATOM   2424  O  OH  . TYR   B  2  67  ? 63.076  -91.448  26.516  1.00 109.26 ? 66  TYR   B OH  1 
ATOM   2425  N  N   . LYS   B  2  68  ? 64.121  -96.506  19.807  1.00 95.97  ? 67  LYS   B N   1 
ATOM   2426  C  CA  . LYS   B  2  68  ? 64.081  -97.618  18.823  1.00 97.07  ? 67  LYS   B CA  1 
ATOM   2427  C  C   . LYS   B  2  68  ? 62.807  -98.439  19.065  1.00 94.30  ? 67  LYS   B C   1 
ATOM   2428  O  O   . LYS   B  2  68  ? 62.614  -98.883  20.212  1.00 91.40  ? 67  LYS   B O   1 
ATOM   2429  C  CB  . LYS   B  2  68  ? 65.353  -98.454  18.992  1.00 99.10  ? 67  LYS   B CB  1 
ATOM   2430  C  CG  . LYS   B  2  68  ? 65.707  -99.356  17.821  1.00 102.43 ? 67  LYS   B CG  1 
ATOM   2431  C  CD  . LYS   B  2  68  ? 67.067  -100.012 17.960  1.00 107.36 ? 67  LYS   B CD  1 
ATOM   2432  C  CE  . LYS   B  2  68  ? 68.218  -99.047  17.762  1.00 109.31 ? 67  LYS   B CE  1 
ATOM   2433  N  NZ  . LYS   B  2  68  ? 69.527  -99.742  17.786  1.00 112.60 ? 67  LYS   B NZ  1 
ATOM   2434  N  N   . LEU   B  2  69  ? 61.957  -98.605  18.043  1.00 94.00  ? 68  LEU   B N   1 
ATOM   2435  C  CA  . LEU   B  2  69  ? 60.697  -99.399  18.128  1.00 97.22  ? 68  LEU   B CA  1 
ATOM   2436  C  C   . LEU   B  2  69  ? 60.971  -100.843 17.694  1.00 99.98  ? 68  LEU   B C   1 
ATOM   2437  O  O   . LEU   B  2  69  ? 60.505  -101.770 18.386  1.00 103.40 ? 68  LEU   B O   1 
ATOM   2438  C  CB  . LEU   B  2  69  ? 59.614  -98.764  17.249  1.00 96.77  ? 68  LEU   B CB  1 
ATOM   2439  C  CG  . LEU   B  2  69  ? 59.143  -97.366  17.652  1.00 97.17  ? 68  LEU   B CG  1 
ATOM   2440  C  CD1 . LEU   B  2  69  ? 57.845  -97.017  16.940  1.00 96.71  ? 68  LEU   B CD1 1 
ATOM   2441  C  CD2 . LEU   B  2  69  ? 58.958  -97.239  19.159  1.00 98.67  ? 68  LEU   B CD2 1 
ATOM   2442  N  N   . ASN   B  2  70  ? 61.672  -101.017 16.570  1.00 100.21 ? 69  ASN   B N   1 
ATOM   2443  C  CA  . ASN   B  2  70  ? 62.246  -102.314 16.119  1.00 102.06 ? 69  ASN   B CA  1 
ATOM   2444  C  C   . ASN   B  2  70  ? 63.506  -102.009 15.297  1.00 106.96 ? 69  ASN   B C   1 
ATOM   2445  O  O   . ASN   B  2  70  ? 63.944  -100.843 15.317  1.00 106.23 ? 69  ASN   B O   1 
ATOM   2446  C  CB  . ASN   B  2  70  ? 61.208  -103.164 15.379  1.00 102.27 ? 69  ASN   B CB  1 
ATOM   2447  C  CG  . ASN   B  2  70  ? 60.810  -102.607 14.028  1.00 100.46 ? 69  ASN   B CG  1 
ATOM   2448  O  OD1 . ASN   B  2  70  ? 61.255  -101.534 13.631  1.00 105.56 ? 69  ASN   B OD1 1 
ATOM   2449  N  ND2 . ASN   B  2  70  ? 59.971  -103.330 13.307  1.00 100.73 ? 69  ASN   B ND2 1 
ATOM   2450  N  N   . ASP   B  2  71  ? 64.057  -103.003 14.594  1.00 109.62 ? 70  ASP   B N   1 
ATOM   2451  C  CA  . ASP   B  2  71  ? 65.331  -102.876 13.833  1.00 114.00 ? 70  ASP   B CA  1 
ATOM   2452  C  C   . ASP   B  2  71  ? 65.141  -102.019 12.573  1.00 111.36 ? 70  ASP   B C   1 
ATOM   2453  O  O   . ASP   B  2  71  ? 66.167  -101.695 11.942  1.00 117.66 ? 70  ASP   B O   1 
ATOM   2454  C  CB  . ASP   B  2  71  ? 65.893  -104.249 13.455  1.00 118.32 ? 70  ASP   B CB  1 
ATOM   2455  C  CG  . ASP   B  2  71  ? 66.453  -105.023 14.635  1.00 124.71 ? 70  ASP   B CG  1 
ATOM   2456  O  OD1 . ASP   B  2  71  ? 67.050  -104.383 15.528  1.00 124.22 ? 70  ASP   B OD1 1 
ATOM   2457  O  OD2 . ASP   B  2  71  ? 66.281  -106.258 14.655  1.00 128.81 ? 70  ASP   B OD2 1 
ATOM   2458  N  N   . LYS   B  2  72  ? 63.900  -101.677 12.206  1.00 106.67 ? 71  LYS   B N   1 
ATOM   2459  C  CA  . LYS   B  2  72  ? 63.587  -100.944 10.949  1.00 106.05 ? 71  LYS   B CA  1 
ATOM   2460  C  C   . LYS   B  2  72  ? 62.848  -99.624  11.217  1.00 100.32 ? 71  LYS   B C   1 
ATOM   2461  O  O   . LYS   B  2  72  ? 62.659  -98.880  10.241  1.00 100.60 ? 71  LYS   B O   1 
ATOM   2462  C  CB  . LYS   B  2  72  ? 62.744  -101.827 10.025  1.00 107.36 ? 71  LYS   B CB  1 
ATOM   2463  C  CG  . LYS   B  2  72  ? 63.362  -103.177 9.685   1.00 113.52 ? 71  LYS   B CG  1 
ATOM   2464  C  CD  . LYS   B  2  72  ? 64.649  -103.074 8.889   1.00 117.39 ? 71  LYS   B CD  1 
ATOM   2465  C  CE  . LYS   B  2  72  ? 65.319  -104.412 8.657   1.00 120.28 ? 71  LYS   B CE  1 
ATOM   2466  N  NZ  . LYS   B  2  72  ? 64.495  -105.299 7.803   1.00 123.95 ? 71  LYS   B NZ  1 
ATOM   2467  N  N   . ILE   B  2  73  ? 62.438  -99.336  12.459  1.00 97.92  ? 72  ILE   B N   1 
ATOM   2468  C  CA  . ILE   B  2  73  ? 61.625  -98.128  12.805  1.00 96.15  ? 72  ILE   B CA  1 
ATOM   2469  C  C   . ILE   B  2  73  ? 62.165  -97.488  14.090  1.00 96.24  ? 72  ILE   B C   1 
ATOM   2470  O  O   . ILE   B  2  73  ? 62.439  -98.228  15.056  1.00 93.18  ? 72  ILE   B O   1 
ATOM   2471  C  CB  . ILE   B  2  73  ? 60.131  -98.490  12.944  1.00 95.10  ? 72  ILE   B CB  1 
ATOM   2472  C  CG1 . ILE   B  2  73  ? 59.574  -99.143  11.676  1.00 96.24  ? 72  ILE   B CG1 1 
ATOM   2473  C  CG2 . ILE   B  2  73  ? 59.311  -97.269  13.340  1.00 94.86  ? 72  ILE   B CG2 1 
ATOM   2474  C  CD1 . ILE   B  2  73  ? 58.464  -100.132 11.940  1.00 97.47  ? 72  ILE   B CD1 1 
ATOM   2475  N  N   . ALA   B  2  74  ? 62.295  -96.156  14.090  1.00 95.15  ? 73  ALA   B N   1 
ATOM   2476  C  CA  . ALA   B  2  74  ? 62.645  -95.316  15.261  1.00 95.29  ? 73  ALA   B CA  1 
ATOM   2477  C  C   . ALA   B  2  74  ? 61.695  -94.116  15.320  1.00 94.60  ? 73  ALA   B C   1 
ATOM   2478  O  O   . ALA   B  2  74  ? 61.057  -93.811  14.293  1.00 91.17  ? 73  ALA   B O   1 
ATOM   2479  C  CB  . ALA   B  2  74  ? 64.084  -94.866  15.177  1.00 95.73  ? 73  ALA   B CB  1 
ATOM   2480  N  N   . VAL   B  2  75  ? 61.613  -93.464  16.483  1.00 95.29  ? 74  VAL   B N   1 
ATOM   2481  C  CA  . VAL   B  2  75  ? 60.752  -92.266  16.712  1.00 96.88  ? 74  VAL   B CA  1 
ATOM   2482  C  C   . VAL   B  2  75  ? 61.583  -91.163  17.376  1.00 100.31 ? 74  VAL   B C   1 
ATOM   2483  O  O   . VAL   B  2  75  ? 62.417  -91.485  18.246  1.00 100.09 ? 74  VAL   B O   1 
ATOM   2484  C  CB  . VAL   B  2  75  ? 59.502  -92.600  17.550  1.00 96.56  ? 74  VAL   B CB  1 
ATOM   2485  C  CG1 . VAL   B  2  75  ? 58.476  -93.372  16.738  1.00 96.38  ? 74  VAL   B CG1 1 
ATOM   2486  C  CG2 . VAL   B  2  75  ? 59.841  -93.343  18.834  1.00 96.91  ? 74  VAL   B CG2 1 
ATOM   2487  N  N   . ALA   B  2  76  ? 61.361  -89.915  16.955  1.00 102.33 ? 75  ALA   B N   1 
ATOM   2488  C  CA  . ALA   B  2  76  ? 61.766  -88.687  17.678  1.00 103.62 ? 75  ALA   B CA  1 
ATOM   2489  C  C   . ALA   B  2  76  ? 60.565  -88.197  18.494  1.00 103.00 ? 75  ALA   B C   1 
ATOM   2490  O  O   . ALA   B  2  76  ? 59.433  -88.237  17.963  1.00 103.14 ? 75  ALA   B O   1 
ATOM   2491  C  CB  . ALA   B  2  76  ? 62.252  -87.641  16.707  1.00 105.33 ? 75  ALA   B CB  1 
ATOM   2492  N  N   . VAL   B  2  77  ? 60.806  -87.766  19.737  1.00 100.84 ? 76  VAL   B N   1 
ATOM   2493  C  CA  . VAL   B  2  77  ? 59.750  -87.414  20.734  1.00 98.42  ? 76  VAL   B CA  1 
ATOM   2494  C  C   . VAL   B  2  77  ? 59.781  -85.905  20.993  1.00 96.70  ? 76  VAL   B C   1 
ATOM   2495  O  O   . VAL   B  2  77  ? 60.883  -85.344  21.125  1.00 97.42  ? 76  VAL   B O   1 
ATOM   2496  C  CB  . VAL   B  2  77  ? 59.935  -88.211  22.041  1.00 96.85  ? 76  VAL   B CB  1 
ATOM   2497  C  CG1 . VAL   B  2  77  ? 59.009  -87.724  23.146  1.00 98.27  ? 76  VAL   B CG1 1 
ATOM   2498  C  CG2 . VAL   B  2  77  ? 59.750  -89.702  21.816  1.00 96.63  ? 76  VAL   B CG2 1 
ATOM   2499  N  N   . ALA   B  2  78  ? 58.601  -85.286  21.061  1.00 95.03  ? 77  ALA   B N   1 
ATOM   2500  C  CA  . ALA   B  2  78  ? 58.379  -83.917  21.577  1.00 96.49  ? 77  ALA   B CA  1 
ATOM   2501  C  C   . ALA   B  2  78  ? 57.178  -83.948  22.527  1.00 90.81  ? 77  ALA   B C   1 
ATOM   2502  O  O   . ALA   B  2  78  ? 56.091  -84.370  22.088  1.00 90.66  ? 77  ALA   B O   1 
ATOM   2503  C  CB  . ALA   B  2  78  ? 58.169  -82.957  20.431  1.00 98.52  ? 77  ALA   B CB  1 
ATOM   2504  N  N   . GLY   B  2  79  ? 57.384  -83.547  23.785  1.00 89.69  ? 78  GLY   B N   1 
ATOM   2505  C  CA  . GLY   B  2  79  ? 56.334  -83.490  24.822  1.00 91.40  ? 78  GLY   B CA  1 
ATOM   2506  C  C   . GLY   B  2  79  ? 56.806  -84.110  26.124  1.00 91.78  ? 78  GLY   B C   1 
ATOM   2507  O  O   . GLY   B  2  79  ? 58.032  -84.115  26.356  1.00 94.18  ? 78  GLY   B O   1 
ATOM   2508  N  N   . LEU   B  2  80  ? 55.873  -84.619  26.942  1.00 91.97  ? 79  LEU   B N   1 
ATOM   2509  C  CA  . LEU   B  2  80  ? 56.179  -85.344  28.207  1.00 92.40  ? 79  LEU   B CA  1 
ATOM   2510  C  C   . LEU   B  2  80  ? 56.834  -86.680  27.843  1.00 91.47  ? 79  LEU   B C   1 
ATOM   2511  O  O   . LEU   B  2  80  ? 56.195  -87.459  27.116  1.00 89.57  ? 79  LEU   B O   1 
ATOM   2512  C  CB  . LEU   B  2  80  ? 54.901  -85.597  29.018  1.00 92.29  ? 79  LEU   B CB  1 
ATOM   2513  C  CG  . LEU   B  2  80  ? 54.158  -84.387  29.592  1.00 96.21  ? 79  LEU   B CG  1 
ATOM   2514  C  CD1 . LEU   B  2  80  ? 55.078  -83.197  29.826  1.00 98.26  ? 79  LEU   B CD1 1 
ATOM   2515  C  CD2 . LEU   B  2  80  ? 52.987  -83.990  28.704  1.00 98.58  ? 79  LEU   B CD2 1 
ATOM   2516  N  N   . THR   B  2  81  ? 58.054  -86.933  28.328  1.00 94.50  ? 80  THR   B N   1 
ATOM   2517  C  CA  . THR   B  2  81  ? 58.825  -88.179  28.058  1.00 98.72  ? 80  THR   B CA  1 
ATOM   2518  C  C   . THR   B  2  81  ? 58.114  -89.386  28.682  1.00 97.58  ? 80  THR   B C   1 
ATOM   2519  O  O   . THR   B  2  81  ? 58.063  -90.441  28.022  1.00 100.47 ? 80  THR   B O   1 
ATOM   2520  C  CB  . THR   B  2  81  ? 60.258  -88.099  28.596  1.00 103.09 ? 80  THR   B CB  1 
ATOM   2521  O  OG1 . THR   B  2  81  ? 60.885  -86.943  28.044  1.00 111.09 ? 80  THR   B OG1 1 
ATOM   2522  C  CG2 . THR   B  2  81  ? 61.073  -89.328  28.258  1.00 103.49 ? 80  THR   B CG2 1 
ATOM   2523  N  N   . ALA   B  2  82  ? 57.617  -89.242  29.914  1.00 100.65 ? 81  ALA   B N   1 
ATOM   2524  C  CA  . ALA   B  2  82  ? 56.901  -90.300  30.667  1.00 98.89  ? 81  ALA   B CA  1 
ATOM   2525  C  C   . ALA   B  2  82  ? 55.704  -90.801  29.849  1.00 95.13  ? 81  ALA   B C   1 
ATOM   2526  O  O   . ALA   B  2  82  ? 55.515  -92.025  29.790  1.00 95.06  ? 81  ALA   B O   1 
ATOM   2527  C  CB  . ALA   B  2  82  ? 56.469  -89.775  32.014  1.00 99.68  ? 81  ALA   B CB  1 
ATOM   2528  N  N   . ASP   B  2  83  ? 54.935  -89.886  29.247  1.00 96.29  ? 82  ASP   B N   1 
ATOM   2529  C  CA  . ASP   B  2  83  ? 53.781  -90.197  28.359  1.00 94.31  ? 82  ASP   B CA  1 
ATOM   2530  C  C   . ASP   B  2  83  ? 54.266  -90.973  27.128  1.00 92.10  ? 82  ASP   B C   1 
ATOM   2531  O  O   . ASP   B  2  83  ? 53.573  -91.928  26.725  1.00 88.34  ? 82  ASP   B O   1 
ATOM   2532  C  CB  . ASP   B  2  83  ? 53.046  -88.927  27.914  1.00 96.46  ? 82  ASP   B CB  1 
ATOM   2533  C  CG  . ASP   B  2  83  ? 52.206  -88.273  28.998  1.00 97.98  ? 82  ASP   B CG  1 
ATOM   2534  O  OD1 . ASP   B  2  83  ? 52.308  -88.703  30.163  1.00 99.95  ? 82  ASP   B OD1 1 
ATOM   2535  O  OD2 . ASP   B  2  83  ? 51.450  -87.338  28.666  1.00 103.19 ? 82  ASP   B OD2 1 
ATOM   2536  N  N   . ALA   B  2  84  ? 55.398  -90.561  26.547  1.00 91.74  ? 83  ALA   B N   1 
ATOM   2537  C  CA  . ALA   B  2  84  ? 55.970  -91.132  25.305  1.00 91.78  ? 83  ALA   B CA  1 
ATOM   2538  C  C   . ALA   B  2  84  ? 56.355  -92.599  25.534  1.00 90.27  ? 83  ALA   B C   1 
ATOM   2539  O  O   . ALA   B  2  84  ? 56.044  -93.429  24.659  1.00 92.61  ? 83  ALA   B O   1 
ATOM   2540  C  CB  . ALA   B  2  84  ? 57.151  -90.311  24.841  1.00 91.68  ? 83  ALA   B CB  1 
ATOM   2541  N  N   . GLU   B  2  85  ? 56.990  -92.911  26.667  1.00 88.08  ? 84  GLU   B N   1 
ATOM   2542  C  CA  . GLU   B  2  85  ? 57.495  -94.277  26.975  1.00 89.03  ? 84  GLU   B CA  1 
ATOM   2543  C  C   . GLU   B  2  85  ? 56.315  -95.248  27.090  1.00 87.83  ? 84  GLU   B C   1 
ATOM   2544  O  O   . GLU   B  2  85  ? 56.461  -96.389  26.614  1.00 90.14  ? 84  GLU   B O   1 
ATOM   2545  C  CB  . GLU   B  2  85  ? 58.351  -94.285  28.241  1.00 90.50  ? 84  GLU   B CB  1 
ATOM   2546  C  CG  . GLU   B  2  85  ? 59.697  -93.604  28.052  1.00 95.19  ? 84  GLU   B CG  1 
ATOM   2547  C  CD  . GLU   B  2  85  ? 60.802  -94.044  29.000  1.00 96.03  ? 84  GLU   B CD  1 
ATOM   2548  O  OE1 . GLU   B  2  85  ? 61.843  -93.361  29.036  1.00 103.17 ? 84  GLU   B OE1 1 
ATOM   2549  O  OE2 . GLU   B  2  85  ? 60.627  -95.067  29.694  1.00 94.98  ? 84  GLU   B OE2 1 
ATOM   2550  N  N   . ILE   B  2  86  ? 55.198  -94.819  27.687  1.00 84.85  ? 85  ILE   B N   1 
ATOM   2551  C  CA  . ILE   B  2  86  ? 53.932  -95.611  27.736  1.00 85.96  ? 85  ILE   B CA  1 
ATOM   2552  C  C   . ILE   B  2  86  ? 53.589  -96.047  26.307  1.00 88.87  ? 85  ILE   B C   1 
ATOM   2553  O  O   . ILE   B  2  86  ? 53.354  -97.255  26.095  1.00 96.37  ? 85  ILE   B O   1 
ATOM   2554  C  CB  . ILE   B  2  86  ? 52.774  -94.812  28.372  1.00 85.21  ? 85  ILE   B CB  1 
ATOM   2555  C  CG1 . ILE   B  2  86  ? 53.005  -94.527  29.859  1.00 86.16  ? 85  ILE   B CG1 1 
ATOM   2556  C  CG2 . ILE   B  2  86  ? 51.437  -95.506  28.134  1.00 84.42  ? 85  ILE   B CG2 1 
ATOM   2557  C  CD1 . ILE   B  2  86  ? 52.921  -95.741  30.755  1.00 87.64  ? 85  ILE   B CD1 1 
ATOM   2558  N  N   . LEU   B  2  87  ? 53.570  -95.093  25.370  1.00 85.44  ? 86  LEU   B N   1 
ATOM   2559  C  CA  . LEU   B  2  87  ? 53.164  -95.308  23.953  1.00 83.73  ? 86  LEU   B CA  1 
ATOM   2560  C  C   . LEU   B  2  87  ? 54.238  -96.114  23.211  1.00 84.58  ? 86  LEU   B C   1 
ATOM   2561  O  O   . LEU   B  2  87  ? 53.854  -96.964  22.384  1.00 83.21  ? 86  LEU   B O   1 
ATOM   2562  C  CB  . LEU   B  2  87  ? 52.920  -93.950  23.285  1.00 81.67  ? 86  LEU   B CB  1 
ATOM   2563  C  CG  . LEU   B  2  87  ? 51.711  -93.168  23.799  1.00 79.91  ? 86  LEU   B CG  1 
ATOM   2564  C  CD1 . LEU   B  2  87  ? 51.621  -91.811  23.124  1.00 81.64  ? 86  LEU   B CD1 1 
ATOM   2565  C  CD2 . LEU   B  2  87  ? 50.417  -93.937  23.592  1.00 79.02  ? 86  LEU   B CD2 1 
ATOM   2566  N  N   . ILE   B  2  88  ? 55.522  -95.865  23.493  1.00 84.99  ? 87  ILE   B N   1 
ATOM   2567  C  CA  . ILE   B  2  88  ? 56.672  -96.563  22.840  1.00 86.79  ? 87  ILE   B CA  1 
ATOM   2568  C  C   . ILE   B  2  88  ? 56.602  -98.062  23.167  1.00 87.69  ? 87  ILE   B C   1 
ATOM   2569  O  O   . ILE   B  2  88  ? 56.801  -98.869  22.239  1.00 86.77  ? 87  ILE   B O   1 
ATOM   2570  C  CB  . ILE   B  2  88  ? 58.022  -95.928  23.242  1.00 86.20  ? 87  ILE   B CB  1 
ATOM   2571  C  CG1 . ILE   B  2  88  ? 58.237  -94.588  22.533  1.00 86.10  ? 87  ILE   B CG1 1 
ATOM   2572  C  CG2 . ILE   B  2  88  ? 59.185  -96.876  22.979  1.00 88.62  ? 87  ILE   B CG2 1 
ATOM   2573  C  CD1 . ILE   B  2  88  ? 59.219  -93.680  23.230  1.00 86.63  ? 87  ILE   B CD1 1 
ATOM   2574  N  N   . ASN   B  2  89  ? 56.324  -98.421  24.425  1.00 90.47  ? 88  ASN   B N   1 
ATOM   2575  C  CA  . ASN   B  2  89  ? 56.258  -99.837  24.884  1.00 93.88  ? 88  ASN   B CA  1 
ATOM   2576  C  C   . ASN   B  2  89  ? 55.078  -100.543 24.216  1.00 91.19  ? 88  ASN   B C   1 
ATOM   2577  O  O   . ASN   B  2  89  ? 55.240  -101.719 23.862  1.00 93.03  ? 88  ASN   B O   1 
ATOM   2578  C  CB  . ASN   B  2  89  ? 56.165  -99.965  26.406  1.00 99.45  ? 88  ASN   B CB  1 
ATOM   2579  C  CG  . ASN   B  2  89  ? 57.530  -100.052 27.053  1.00 105.11 ? 88  ASN   B CG  1 
ATOM   2580  O  OD1 . ASN   B  2  89  ? 58.316  -100.941 26.725  1.00 106.03 ? 88  ASN   B OD1 1 
ATOM   2581  N  ND2 . ASN   B  2  89  ? 57.824  -99.132  27.960  1.00 110.82 ? 88  ASN   B ND2 1 
ATOM   2582  N  N   . THR   B  2  90  ? 53.945  -99.856  24.060  1.00 89.46  ? 89  THR   B N   1 
ATOM   2583  C  CA  . THR   B  2  90  ? 52.762  -100.366 23.320  1.00 89.45  ? 89  THR   B CA  1 
ATOM   2584  C  C   . THR   B  2  90  ? 53.163  -100.636 21.866  1.00 90.18  ? 89  THR   B C   1 
ATOM   2585  O  O   . THR   B  2  90  ? 52.873  -101.739 21.376  1.00 88.33  ? 89  THR   B O   1 
ATOM   2586  C  CB  . THR   B  2  90  ? 51.581  -99.393  23.395  1.00 90.55  ? 89  THR   B CB  1 
ATOM   2587  O  OG1 . THR   B  2  90  ? 51.226  -99.238  24.769  1.00 90.05  ? 89  THR   B OG1 1 
ATOM   2588  C  CG2 . THR   B  2  90  ? 50.389  -99.874  22.597  1.00 92.00  ? 89  THR   B CG2 1 
ATOM   2589  N  N   . ALA   B  2  91  ? 53.803  -99.660  21.215  1.00 91.70  ? 90  ALA   B N   1 
ATOM   2590  C  CA  . ALA   B  2  91  ? 54.277  -99.733  19.812  1.00 92.94  ? 90  ALA   B CA  1 
ATOM   2591  C  C   . ALA   B  2  91  ? 55.251  -100.907 19.644  1.00 93.43  ? 90  ALA   B C   1 
ATOM   2592  O  O   . ALA   B  2  91  ? 55.125  -101.629 18.638  1.00 97.84  ? 90  ALA   B O   1 
ATOM   2593  C  CB  . ALA   B  2  91  ? 54.922  -98.430  19.410  1.00 93.68  ? 90  ALA   B CB  1 
ATOM   2594  N  N   . ARG   B  2  92  ? 56.185  -101.085 20.586  1.00 92.61  ? 91  ARG   B N   1 
ATOM   2595  C  CA  . ARG   B  2  92  ? 57.212  -102.166 20.553  1.00 93.74  ? 91  ARG   B CA  1 
ATOM   2596  C  C   . ARG   B  2  92  ? 56.519  -103.535 20.575  1.00 92.89  ? 91  ARG   B C   1 
ATOM   2597  O  O   . ARG   B  2  92  ? 56.898  -104.392 19.753  1.00 89.47  ? 91  ARG   B O   1 
ATOM   2598  C  CB  . ARG   B  2  92  ? 58.198  -102.029 21.719  1.00 93.80  ? 91  ARG   B CB  1 
ATOM   2599  C  CG  . ARG   B  2  92  ? 59.296  -101.001 21.486  1.00 93.36  ? 91  ARG   B CG  1 
ATOM   2600  C  CD  . ARG   B  2  92  ? 60.139  -100.770 22.725  1.00 93.82  ? 91  ARG   B CD  1 
ATOM   2601  N  NE  . ARG   B  2  92  ? 61.256  -99.871  22.477  1.00 94.08  ? 91  ARG   B NE  1 
ATOM   2602  C  CZ  . ARG   B  2  92  ? 62.150  -99.499  23.391  1.00 96.63  ? 91  ARG   B CZ  1 
ATOM   2603  N  NH1 . ARG   B  2  92  ? 62.069  -99.952  24.632  1.00 96.55  ? 91  ARG   B NH1 1 
ATOM   2604  N  NH2 . ARG   B  2  92  ? 63.125  -98.670  23.058  1.00 100.08 ? 91  ARG   B NH2 1 
ATOM   2605  N  N   . ILE   B  2  93  ? 55.550  -103.721 21.479  1.00 95.50  ? 92  ILE   B N   1 
ATOM   2606  C  CA  . ILE   B  2  93  ? 54.752  -104.976 21.639  1.00 97.16  ? 92  ILE   B CA  1 
ATOM   2607  C  C   . ILE   B  2  93  ? 53.947  -105.223 20.356  1.00 99.59  ? 92  ILE   B C   1 
ATOM   2608  O  O   . ILE   B  2  93  ? 53.944  -106.373 19.875  1.00 103.57 ? 92  ILE   B O   1 
ATOM   2609  C  CB  . ILE   B  2  93  ? 53.849  -104.910 22.891  1.00 96.59  ? 92  ILE   B CB  1 
ATOM   2610  C  CG1 . ILE   B  2  93  ? 54.668  -105.060 24.176  1.00 97.18  ? 92  ILE   B CG1 1 
ATOM   2611  C  CG2 . ILE   B  2  93  ? 52.730  -105.940 22.814  1.00 96.99  ? 92  ILE   B CG2 1 
ATOM   2612  C  CD1 . ILE   B  2  93  ? 53.914  -104.725 25.447  1.00 97.96  ? 92  ILE   B CD1 1 
ATOM   2613  N  N   . HIS   B  2  94  ? 53.281  -104.187 19.837  1.00 98.75  ? 93  HIS   B N   1 
ATOM   2614  C  CA  . HIS   B  2  94  ? 52.443  -104.235 18.607  1.00 100.48 ? 93  HIS   B CA  1 
ATOM   2615  C  C   . HIS   B  2  94  ? 53.271  -104.741 17.418  1.00 93.03  ? 93  HIS   B C   1 
ATOM   2616  O  O   . HIS   B  2  94  ? 52.731  -105.534 16.622  1.00 87.31  ? 93  HIS   B O   1 
ATOM   2617  C  CB  . HIS   B  2  94  ? 51.825  -102.859 18.320  1.00 108.81 ? 93  HIS   B CB  1 
ATOM   2618  C  CG  . HIS   B  2  94  ? 50.517  -102.610 18.999  1.00 122.95 ? 93  HIS   B CG  1 
ATOM   2619  N  ND1 . HIS   B  2  94  ? 49.548  -103.589 19.137  1.00 134.85 ? 93  HIS   B ND1 1 
ATOM   2620  C  CD2 . HIS   B  2  94  ? 49.995  -101.486 19.539  1.00 130.44 ? 93  HIS   B CD2 1 
ATOM   2621  C  CE1 . HIS   B  2  94  ? 48.498  -103.082 19.755  1.00 136.85 ? 93  HIS   B CE1 1 
ATOM   2622  N  NE2 . HIS   B  2  94  ? 48.746  -101.792 20.013  1.00 132.93 ? 93  HIS   B NE2 1 
ATOM   2623  N  N   . ALA   B  2  95  ? 54.524  -104.289 17.300  1.00 90.16  ? 94  ALA   B N   1 
ATOM   2624  C  CA  . ALA   B  2  95  ? 55.481  -104.702 16.246  1.00 90.13  ? 94  ALA   B CA  1 
ATOM   2625  C  C   . ALA   B  2  95  ? 55.757  -106.208 16.351  1.00 89.24  ? 94  ALA   B C   1 
ATOM   2626  O  O   . ALA   B  2  95  ? 55.754  -106.879 15.302  1.00 87.88  ? 94  ALA   B O   1 
ATOM   2627  C  CB  . ALA   B  2  95  ? 56.759  -103.906 16.358  1.00 90.19  ? 94  ALA   B CB  1 
ATOM   2628  N  N   . GLN   B  2  96  ? 55.990  -106.706 17.570  1.00 91.08  ? 95  GLN   B N   1 
ATOM   2629  C  CA  . GLN   B  2  96  ? 56.317  -108.132 17.849  1.00 91.99  ? 95  GLN   B CA  1 
ATOM   2630  C  C   . GLN   B  2  96  ? 55.093  -109.021 17.591  1.00 90.75  ? 95  GLN   B C   1 
ATOM   2631  O  O   . GLN   B  2  96  ? 55.289  -110.127 17.049  1.00 91.36  ? 95  GLN   B O   1 
ATOM   2632  C  CB  . GLN   B  2  96  ? 56.827  -108.301 19.282  1.00 93.74  ? 95  GLN   B CB  1 
ATOM   2633  C  CG  . GLN   B  2  96  ? 58.208  -107.703 19.516  1.00 93.76  ? 95  GLN   B CG  1 
ATOM   2634  C  CD  . GLN   B  2  96  ? 59.193  -108.033 18.420  1.00 94.38  ? 95  GLN   B CD  1 
ATOM   2635  O  OE1 . GLN   B  2  96  ? 59.852  -107.154 17.871  1.00 95.43  ? 95  GLN   B OE1 1 
ATOM   2636  N  NE2 . GLN   B  2  96  ? 59.291  -109.308 18.080  1.00 93.61  ? 95  GLN   B NE2 1 
ATOM   2637  N  N   . ASN   B  2  97  ? 53.892  -108.567 17.975  1.00 90.79  ? 96  ASN   B N   1 
ATOM   2638  C  CA  . ASN   B  2  97  ? 52.605  -109.278 17.739  1.00 89.03  ? 96  ASN   B CA  1 
ATOM   2639  C  C   . ASN   B  2  97  ? 52.425  -109.541 16.242  1.00 88.54  ? 96  ASN   B C   1 
ATOM   2640  O  O   . ASN   B  2  97  ? 52.003  -110.653 15.885  1.00 86.30  ? 96  ASN   B O   1 
ATOM   2641  C  CB  . ASN   B  2  97  ? 51.393  -108.490 18.242  1.00 92.62  ? 96  ASN   B CB  1 
ATOM   2642  C  CG  . ASN   B  2  97  ? 51.136  -108.645 19.726  1.00 96.10  ? 96  ASN   B CG  1 
ATOM   2643  O  OD1 . ASN   B  2  97  ? 51.645  -109.563 20.364  1.00 97.41  ? 96  ASN   B OD1 1 
ATOM   2644  N  ND2 . ASN   B  2  97  ? 50.325  -107.759 20.280  1.00 101.75 ? 96  ASN   B ND2 1 
ATOM   2645  N  N   . TYR   B  2  98  ? 52.711  -108.539 15.409  1.00 88.58  ? 97  TYR   B N   1 
ATOM   2646  C  CA  . TYR   B  2  98  ? 52.613  -108.615 13.928  1.00 89.14  ? 97  TYR   B CA  1 
ATOM   2647  C  C   . TYR   B  2  98  ? 53.632  -109.632 13.395  1.00 90.06  ? 97  TYR   B C   1 
ATOM   2648  O  O   . TYR   B  2  98  ? 53.267  -110.437 12.515  1.00 90.80  ? 97  TYR   B O   1 
ATOM   2649  C  CB  . TYR   B  2  98  ? 52.818  -107.234 13.298  1.00 87.95  ? 97  TYR   B CB  1 
ATOM   2650  C  CG  . TYR   B  2  98  ? 52.492  -107.170 11.828  1.00 86.84  ? 97  TYR   B CG  1 
ATOM   2651  C  CD1 . TYR   B  2  98  ? 53.417  -107.562 10.874  1.00 90.27  ? 97  TYR   B CD1 1 
ATOM   2652  C  CD2 . TYR   B  2  98  ? 51.254  -106.733 11.384  1.00 86.96  ? 97  TYR   B CD2 1 
ATOM   2653  C  CE1 . TYR   B  2  98  ? 53.127  -107.515 9.519   1.00 90.65  ? 97  TYR   B CE1 1 
ATOM   2654  C  CE2 . TYR   B  2  98  ? 50.947  -106.679 10.033  1.00 86.63  ? 97  TYR   B CE2 1 
ATOM   2655  C  CZ  . TYR   B  2  98  ? 51.886  -107.071 9.095   1.00 87.01  ? 97  TYR   B CZ  1 
ATOM   2656  O  OH  . TYR   B  2  98  ? 51.594  -107.018 7.762   1.00 85.79  ? 97  TYR   B OH  1 
ATOM   2657  N  N   . LEU   B  2  99  ? 54.867  -109.595 13.908  1.00 89.91  ? 98  LEU   B N   1 
ATOM   2658  C  CA  . LEU   B  2  99  ? 55.967  -110.508 13.493  1.00 92.23  ? 98  LEU   B CA  1 
ATOM   2659  C  C   . LEU   B  2  99  ? 55.607  -111.947 13.882  1.00 94.31  ? 98  LEU   B C   1 
ATOM   2660  O  O   . LEU   B  2  99  ? 55.811  -112.846 13.050  1.00 97.98  ? 98  LEU   B O   1 
ATOM   2661  C  CB  . LEU   B  2  99  ? 57.278  -110.071 14.154  1.00 90.98  ? 98  LEU   B CB  1 
ATOM   2662  C  CG  . LEU   B  2  99  ? 58.514  -110.877 13.756  1.00 91.29  ? 98  LEU   B CG  1 
ATOM   2663  C  CD1 . LEU   B  2  99  ? 58.738  -110.834 12.253  1.00 90.56  ? 98  LEU   B CD1 1 
ATOM   2664  C  CD2 . LEU   B  2  99  ? 59.749  -110.380 14.489  1.00 92.25  ? 98  LEU   B CD2 1 
ATOM   2665  N  N   . LYS   B  2  100 ? 55.098  -112.148 15.101  1.00 99.03  ? 99  LYS   B N   1 
ATOM   2666  C  CA  . LYS   B  2  100 ? 54.665  -113.472 15.626  1.00 101.70 ? 99  LYS   B CA  1 
ATOM   2667  C  C   . LYS   B  2  100 ? 53.532  -114.019 14.745  1.00 99.00  ? 99  LYS   B C   1 
ATOM   2668  O  O   . LYS   B  2  100 ? 53.560  -115.231 14.451  1.00 101.76 ? 99  LYS   B O   1 
ATOM   2669  C  CB  . LYS   B  2  100 ? 54.257  -113.350 17.100  1.00 104.87 ? 99  LYS   B CB  1 
ATOM   2670  C  CG  . LYS   B  2  100 ? 53.771  -114.631 17.769  1.00 109.54 ? 99  LYS   B CG  1 
ATOM   2671  C  CD  . LYS   B  2  100 ? 53.366  -114.440 19.220  1.00 112.56 ? 99  LYS   B CD  1 
ATOM   2672  C  CE  . LYS   B  2  100 ? 52.369  -115.470 19.713  1.00 119.68 ? 99  LYS   B CE  1 
ATOM   2673  N  NZ  . LYS   B  2  100 ? 52.831  -116.862 19.484  1.00 126.37 ? 99  LYS   B NZ  1 
ATOM   2674  N  N   . THR   B  2  101 ? 52.590  -113.168 14.319  1.00 94.88  ? 100 THR   B N   1 
ATOM   2675  C  CA  . THR   B  2  101 ? 51.382  -113.584 13.552  1.00 92.04  ? 100 THR   B CA  1 
ATOM   2676  C  C   . THR   B  2  101 ? 51.759  -113.934 12.105  1.00 94.19  ? 100 THR   B C   1 
ATOM   2677  O  O   . THR   B  2  101 ? 51.389  -115.039 11.660  1.00 97.14  ? 100 THR   B O   1 
ATOM   2678  C  CB  . THR   B  2  101 ? 50.272  -112.526 13.603  1.00 89.37  ? 100 THR   B CB  1 
ATOM   2679  O  OG1 . THR   B  2  101 ? 49.864  -112.407 14.966  1.00 88.67  ? 100 THR   B OG1 1 
ATOM   2680  C  CG2 . THR   B  2  101 ? 49.071  -112.881 12.751  1.00 88.61  ? 100 THR   B CG2 1 
ATOM   2681  N  N   . TYR   B  2  102 ? 52.452  -113.032 11.400  1.00 90.44  ? 101 TYR   B N   1 
ATOM   2682  C  CA  . TYR   B  2  102 ? 52.641  -113.075 9.924   1.00 90.25  ? 101 TYR   B CA  1 
ATOM   2683  C  C   . TYR   B  2  102 ? 54.074  -113.451 9.525   1.00 90.81  ? 101 TYR   B C   1 
ATOM   2684  O  O   . TYR   B  2  102 ? 54.316  -113.575 8.309   1.00 86.58  ? 101 TYR   B O   1 
ATOM   2685  C  CB  . TYR   B  2  102 ? 52.301  -111.719 9.298   1.00 87.88  ? 101 TYR   B CB  1 
ATOM   2686  C  CG  . TYR   B  2  102 ? 50.872  -111.275 9.483   1.00 85.59  ? 101 TYR   B CG  1 
ATOM   2687  C  CD1 . TYR   B  2  102 ? 49.841  -111.877 8.782   1.00 87.18  ? 101 TYR   B CD1 1 
ATOM   2688  C  CD2 . TYR   B  2  102 ? 50.547  -110.246 10.350  1.00 82.88  ? 101 TYR   B CD2 1 
ATOM   2689  C  CE1 . TYR   B  2  102 ? 48.524  -111.479 8.942   1.00 83.98  ? 101 TYR   B CE1 1 
ATOM   2690  C  CE2 . TYR   B  2  102 ? 49.235  -109.834 10.521  1.00 81.69  ? 101 TYR   B CE2 1 
ATOM   2691  C  CZ  . TYR   B  2  102 ? 48.219  -110.454 9.816   1.00 80.89  ? 101 TYR   B CZ  1 
ATOM   2692  O  OH  . TYR   B  2  102 ? 46.919  -110.071 9.966   1.00 81.34  ? 101 TYR   B OH  1 
ATOM   2693  N  N   . ASN   B  2  103 ? 54.992  -113.605 10.485  1.00 94.57  ? 102 ASN   B N   1 
ATOM   2694  C  CA  . ASN   B  2  103 ? 56.418  -113.953 10.226  1.00 98.74  ? 102 ASN   B CA  1 
ATOM   2695  C  C   . ASN   B  2  103 ? 57.016  -112.954 9.227   1.00 98.54  ? 102 ASN   B C   1 
ATOM   2696  O  O   . ASN   B  2  103 ? 57.841  -113.364 8.388   1.00 95.20  ? 102 ASN   B O   1 
ATOM   2697  C  CB  . ASN   B  2  103 ? 56.571  -115.403 9.756   1.00 102.11 ? 102 ASN   B CB  1 
ATOM   2698  C  CG  . ASN   B  2  103 ? 57.205  -116.286 10.809  1.00 104.05 ? 102 ASN   B CG  1 
ATOM   2699  O  OD1 . ASN   B  2  103 ? 56.575  -116.605 11.815  1.00 104.81 ? 102 ASN   B OD1 1 
ATOM   2700  N  ND2 . ASN   B  2  103 ? 58.455  -116.666 10.597  1.00 107.93 ? 102 ASN   B ND2 1 
ATOM   2701  N  N   . GLU   B  2  104 ? 56.611  -111.686 9.324   1.00 98.96  ? 103 GLU   B N   1 
ATOM   2702  C  CA  . GLU   B  2  104 ? 57.181  -110.555 8.548   1.00 101.91 ? 103 GLU   B CA  1 
ATOM   2703  C  C   . GLU   B  2  104 ? 57.201  -109.316 9.446   1.00 101.76 ? 103 GLU   B C   1 
ATOM   2704  O  O   . GLU   B  2  104 ? 56.253  -109.159 10.243  1.00 98.78  ? 103 GLU   B O   1 
ATOM   2705  C  CB  . GLU   B  2  104 ? 56.362  -110.309 7.281   1.00 105.89 ? 103 GLU   B CB  1 
ATOM   2706  C  CG  . GLU   B  2  104 ? 56.479  -111.426 6.257   1.00 109.62 ? 103 GLU   B CG  1 
ATOM   2707  C  CD  . GLU   B  2  104 ? 55.644  -111.237 5.000   1.00 111.67 ? 103 GLU   B CD  1 
ATOM   2708  O  OE1 . GLU   B  2  104 ? 55.724  -112.105 4.103   1.00 110.88 ? 103 GLU   B OE1 1 
ATOM   2709  O  OE2 . GLU   B  2  104 ? 54.914  -110.226 4.921   1.00 113.79 ? 103 GLU   B OE2 1 
ATOM   2710  N  N   . ASP   B  2  105 ? 58.246  -108.490 9.331   1.00 102.80 ? 104 ASP   B N   1 
ATOM   2711  C  CA  . ASP   B  2  105 ? 58.378  -107.200 10.062  1.00 101.15 ? 104 ASP   B CA  1 
ATOM   2712  C  C   . ASP   B  2  105 ? 57.171  -106.324 9.711   1.00 95.57  ? 104 ASP   B C   1 
ATOM   2713  O  O   . ASP   B  2  105 ? 56.731  -106.371 8.547   1.00 95.76  ? 104 ASP   B O   1 
ATOM   2714  C  CB  . ASP   B  2  105 ? 59.697  -106.494 9.731   1.00 105.09 ? 104 ASP   B CB  1 
ATOM   2715  C  CG  . ASP   B  2  105 ? 60.937  -107.190 10.268  1.00 108.59 ? 104 ASP   B CG  1 
ATOM   2716  O  OD1 . ASP   B  2  105 ? 60.834  -107.846 11.327  1.00 112.50 ? 104 ASP   B OD1 1 
ATOM   2717  O  OD2 . ASP   B  2  105 ? 61.999  -107.063 9.625   1.00 113.48 ? 104 ASP   B OD2 1 
ATOM   2718  N  N   . ILE   B  2  106 ? 56.648  -105.573 10.682  1.00 93.73  ? 105 ILE   B N   1 
ATOM   2719  C  CA  . ILE   B  2  106 ? 55.411  -104.752 10.511  1.00 92.40  ? 105 ILE   B CA  1 
ATOM   2720  C  C   . ILE   B  2  106 ? 55.703  -103.600 9.550   1.00 92.85  ? 105 ILE   B C   1 
ATOM   2721  O  O   . ILE   B  2  106 ? 56.698  -102.895 9.707   1.00 89.65  ? 105 ILE   B O   1 
ATOM   2722  C  CB  . ILE   B  2  106 ? 54.846  -104.262 11.861  1.00 91.65  ? 105 ILE   B CB  1 
ATOM   2723  C  CG1 . ILE   B  2  106 ? 53.474  -103.609 11.674  1.00 89.74  ? 105 ILE   B CG1 1 
ATOM   2724  C  CG2 . ILE   B  2  106 ? 55.818  -103.341 12.592  1.00 92.22  ? 105 ILE   B CG2 1 
ATOM   2725  C  CD1 . ILE   B  2  106 ? 52.697  -103.433 12.953  1.00 89.10  ? 105 ILE   B CD1 1 
ATOM   2726  N  N   . PRO   B  2  107 ? 54.871  -103.422 8.494   1.00 94.70  ? 106 PRO   B N   1 
ATOM   2727  C  CA  . PRO   B  2  107 ? 54.875  -102.202 7.684   1.00 94.71  ? 106 PRO   B CA  1 
ATOM   2728  C  C   . PRO   B  2  107 ? 54.668  -100.940 8.536   1.00 95.12  ? 106 PRO   B C   1 
ATOM   2729  O  O   . PRO   B  2  107 ? 53.808  -100.962 9.401   1.00 94.52  ? 106 PRO   B O   1 
ATOM   2730  C  CB  . PRO   B  2  107 ? 53.688  -102.397 6.727   1.00 93.71  ? 106 PRO   B CB  1 
ATOM   2731  C  CG  . PRO   B  2  107 ? 53.556  -103.896 6.609   1.00 95.61  ? 106 PRO   B CG  1 
ATOM   2732  C  CD  . PRO   B  2  107 ? 53.922  -104.423 7.981   1.00 96.63  ? 106 PRO   B CD  1 
ATOM   2733  N  N   . VAL   B  2  108 ? 55.432  -99.879  8.248   1.00 94.93  ? 107 VAL   B N   1 
ATOM   2734  C  CA  . VAL   B  2  108 ? 55.563  -98.663  9.110   1.00 93.49  ? 107 VAL   B CA  1 
ATOM   2735  C  C   . VAL   B  2  108 ? 54.177  -98.055  9.362   1.00 93.95  ? 107 VAL   B C   1 
ATOM   2736  O  O   . VAL   B  2  108 ? 53.877  -97.775  10.536  1.00 94.03  ? 107 VAL   B O   1 
ATOM   2737  C  CB  . VAL   B  2  108 ? 56.528  -97.620  8.511   1.00 91.17  ? 107 VAL   B CB  1 
ATOM   2738  C  CG1 . VAL   B  2  108 ? 56.622  -96.382  9.391   1.00 89.39  ? 107 VAL   B CG1 1 
ATOM   2739  C  CG2 . VAL   B  2  108 ? 57.917  -98.196  8.274   1.00 92.94  ? 107 VAL   B CG2 1 
ATOM   2740  N  N   . GLU   B  2  109 ? 53.367  -97.866  8.315   1.00 93.68  ? 108 GLU   B N   1 
ATOM   2741  C  CA  . GLU   B  2  109 ? 52.056  -97.165  8.407   1.00 95.53  ? 108 GLU   B CA  1 
ATOM   2742  C  C   . GLU   B  2  109 ? 51.109  -97.908  9.358   1.00 94.22  ? 108 GLU   B C   1 
ATOM   2743  O  O   . GLU   B  2  109 ? 50.342  -97.224  10.066  1.00 93.72  ? 108 GLU   B O   1 
ATOM   2744  C  CB  . GLU   B  2  109 ? 51.383  -97.028  7.041   1.00 100.17 ? 108 GLU   B CB  1 
ATOM   2745  C  CG  . GLU   B  2  109 ? 50.322  -95.936  7.019   1.00 104.60 ? 108 GLU   B CG  1 
ATOM   2746  C  CD  . GLU   B  2  109 ? 49.207  -96.110  6.002   1.00 107.09 ? 108 GLU   B CD  1 
ATOM   2747  O  OE1 . GLU   B  2  109 ? 49.276  -97.060  5.197   1.00 122.21 ? 108 GLU   B OE1 1 
ATOM   2748  O  OE2 . GLU   B  2  109 ? 48.265  -95.294  6.018   1.00 110.31 ? 108 GLU   B OE2 1 
ATOM   2749  N  N   . ILE   B  2  110 ? 51.139  -99.244  9.357   1.00 92.57  ? 109 ILE   B N   1 
ATOM   2750  C  CA  . ILE   B  2  110 ? 50.258  -100.094 10.215  1.00 91.24  ? 109 ILE   B CA  1 
ATOM   2751  C  C   . ILE   B  2  110 ? 50.584  -99.798  11.683  1.00 88.28  ? 109 ILE   B C   1 
ATOM   2752  O  O   . ILE   B  2  110 ? 49.629  -99.644  12.472  1.00 89.90  ? 109 ILE   B O   1 
ATOM   2753  C  CB  . ILE   B  2  110 ? 50.399  -101.592 9.873   1.00 91.09  ? 109 ILE   B CB  1 
ATOM   2754  C  CG1 . ILE   B  2  110 ? 49.963  -101.878 8.432   1.00 89.97  ? 109 ILE   B CG1 1 
ATOM   2755  C  CG2 . ILE   B  2  110 ? 49.636  -102.451 10.876  1.00 91.24  ? 109 ILE   B CG2 1 
ATOM   2756  C  CD1 . ILE   B  2  110 ? 50.191  -103.301 7.982   1.00 91.73  ? 109 ILE   B CD1 1 
ATOM   2757  N  N   . LEU   B  2  111 ? 51.876  -99.721  12.028  1.00 86.95  ? 110 LEU   B N   1 
ATOM   2758  C  CA  . LEU   B  2  111 ? 52.353  -99.406  13.402  1.00 88.67  ? 110 LEU   B CA  1 
ATOM   2759  C  C   . LEU   B  2  111 ? 51.908  -97.984  13.761  1.00 87.30  ? 110 LEU   B C   1 
ATOM   2760  O  O   . LEU   B  2  111 ? 51.364  -97.805  14.869  1.00 93.01  ? 110 LEU   B O   1 
ATOM   2761  C  CB  . LEU   B  2  111 ? 53.877  -99.566  13.475  1.00 87.10  ? 110 LEU   B CB  1 
ATOM   2762  C  CG  . LEU   B  2  111 ? 54.503  -99.338  14.853  1.00 89.12  ? 110 LEU   B CG  1 
ATOM   2763  C  CD1 . LEU   B  2  111 ? 55.759  -100.172 15.032  1.00 90.50  ? 110 LEU   B CD1 1 
ATOM   2764  C  CD2 . LEU   B  2  111 ? 54.824  -97.870  15.082  1.00 91.22  ? 110 LEU   B CD2 1 
ATOM   2765  N  N   . VAL   B  2  112 ? 52.108  -97.026  12.848  1.00 88.54  ? 111 VAL   B N   1 
ATOM   2766  C  CA  . VAL   B  2  112 ? 51.810  -95.577  13.064  1.00 88.81  ? 111 VAL   B CA  1 
ATOM   2767  C  C   . VAL   B  2  112 ? 50.299  -95.405  13.263  1.00 89.05  ? 111 VAL   B C   1 
ATOM   2768  O  O   . VAL   B  2  112 ? 49.911  -94.588  14.122  1.00 89.78  ? 111 VAL   B O   1 
ATOM   2769  C  CB  . VAL   B  2  112 ? 52.328  -94.692  11.910  1.00 90.25  ? 111 VAL   B CB  1 
ATOM   2770  C  CG1 . VAL   B  2  112 ? 51.962  -93.228  12.110  1.00 89.91  ? 111 VAL   B CG1 1 
ATOM   2771  C  CG2 . VAL   B  2  112 ? 53.831  -94.826  11.713  1.00 91.43  ? 111 VAL   B CG2 1 
ATOM   2772  N  N   . ARG   B  2  113 ? 49.482  -96.139  12.499  1.00 88.78  ? 112 ARG   B N   1 
ATOM   2773  C  CA  . ARG   B  2  113 ? 47.998  -96.049  12.560  1.00 88.48  ? 112 ARG   B CA  1 
ATOM   2774  C  C   . ARG   B  2  113 ? 47.516  -96.507  13.941  1.00 87.11  ? 112 ARG   B C   1 
ATOM   2775  O  O   . ARG   B  2  113 ? 46.691  -95.794  14.534  1.00 83.60  ? 112 ARG   B O   1 
ATOM   2776  C  CB  . ARG   B  2  113 ? 47.332  -96.885  11.462  1.00 90.11  ? 112 ARG   B CB  1 
ATOM   2777  C  CG  . ARG   B  2  113 ? 45.861  -96.552  11.256  1.00 90.14  ? 112 ARG   B CG  1 
ATOM   2778  C  CD  . ARG   B  2  113 ? 45.087  -97.649  10.552  1.00 90.93  ? 112 ARG   B CD  1 
ATOM   2779  N  NE  . ARG   B  2  113 ? 45.560  -97.865  9.190   1.00 94.41  ? 112 ARG   B NE  1 
ATOM   2780  C  CZ  . ARG   B  2  113 ? 46.083  -98.997  8.714   1.00 95.36  ? 112 ARG   B CZ  1 
ATOM   2781  N  NH1 . ARG   B  2  113 ? 46.474  -99.050  7.452   1.00 96.77  ? 112 ARG   B NH1 1 
ATOM   2782  N  NH2 . ARG   B  2  113 ? 46.211  -100.072 9.478   1.00 95.45  ? 112 ARG   B NH2 1 
ATOM   2783  N  N   . ARG   B  2  114 ? 48.012  -97.648  14.426  1.00 91.60  ? 113 ARG   B N   1 
ATOM   2784  C  CA  . ARG   B  2  114 ? 47.561  -98.270  15.701  1.00 97.88  ? 113 ARG   B CA  1 
ATOM   2785  C  C   . ARG   B  2  114 ? 47.941  -97.364  16.877  1.00 99.54  ? 113 ARG   B C   1 
ATOM   2786  O  O   . ARG   B  2  114 ? 47.114  -97.229  17.800  1.00 106.86 ? 113 ARG   B O   1 
ATOM   2787  C  CB  . ARG   B  2  114 ? 48.153  -99.672  15.879  1.00 107.67 ? 113 ARG   B CB  1 
ATOM   2788  C  CG  . ARG   B  2  114 ? 47.398  -100.548 16.870  1.00 109.07 ? 113 ARG   B CG  1 
ATOM   2789  C  CD  . ARG   B  2  114 ? 47.433  -102.007 16.450  1.00 114.08 ? 113 ARG   B CD  1 
ATOM   2790  N  NE  . ARG   B  2  114 ? 48.803  -102.475 16.242  1.00 116.68 ? 113 ARG   B NE  1 
ATOM   2791  C  CZ  . ARG   B  2  114 ? 49.204  -103.334 15.301  1.00 117.38 ? 113 ARG   B CZ  1 
ATOM   2792  N  NH1 . ARG   B  2  114 ? 48.349  -103.845 14.429  1.00 116.23 ? 113 ARG   B NH1 1 
ATOM   2793  N  NH2 . ARG   B  2  114 ? 50.479  -103.676 15.228  1.00 114.79 ? 113 ARG   B NH2 1 
ATOM   2794  N  N   . LEU   B  2  115 ? 49.137  -96.766  16.845  1.00 97.86  ? 114 LEU   B N   1 
ATOM   2795  C  CA  . LEU   B  2  115 ? 49.618  -95.853  17.918  1.00 93.96  ? 114 LEU   B CA  1 
ATOM   2796  C  C   . LEU   B  2  115 ? 48.758  -94.583  17.896  1.00 90.94  ? 114 LEU   B C   1 
ATOM   2797  O  O   . LEU   B  2  115 ? 48.402  -94.090  18.985  1.00 87.28  ? 114 LEU   B O   1 
ATOM   2798  C  CB  . LEU   B  2  115 ? 51.105  -95.528  17.722  1.00 94.80  ? 114 LEU   B CB  1 
ATOM   2799  C  CG  . LEU   B  2  115 ? 52.009  -95.785  18.930  1.00 96.43  ? 114 LEU   B CG  1 
ATOM   2800  C  CD1 . LEU   B  2  115 ? 53.353  -95.094  18.756  1.00 98.72  ? 114 LEU   B CD1 1 
ATOM   2801  C  CD2 . LEU   B  2  115 ? 51.361  -95.341  20.236  1.00 97.62  ? 114 LEU   B CD2 1 
ATOM   2802  N  N   . SER   B  2  116 ? 48.427  -94.096  16.696  1.00 89.28  ? 115 SER   B N   1 
ATOM   2803  C  CA  . SER   B  2  116 ? 47.568  -92.906  16.453  1.00 86.57  ? 115 SER   B CA  1 
ATOM   2804  C  C   . SER   B  2  116 ? 46.119  -93.200  16.861  1.00 85.05  ? 115 SER   B C   1 
ATOM   2805  O  O   . SER   B  2  116 ? 45.428  -92.261  17.301  1.00 82.01  ? 115 SER   B O   1 
ATOM   2806  C  CB  . SER   B  2  116 ? 47.650  -92.472  15.016  1.00 87.38  ? 115 SER   B CB  1 
ATOM   2807  O  OG  . SER   B  2  116 ? 48.984  -92.136  14.673  1.00 89.41  ? 115 SER   B OG  1 
ATOM   2808  N  N   . ASP   B  2  117 ? 45.677  -94.451  16.713  1.00 84.94  ? 116 ASP   B N   1 
ATOM   2809  C  CA  . ASP   B  2  117 ? 44.304  -94.899  17.072  1.00 84.13  ? 116 ASP   B CA  1 
ATOM   2810  C  C   . ASP   B  2  117 ? 44.156  -94.912  18.596  1.00 78.23  ? 116 ASP   B C   1 
ATOM   2811  O  O   . ASP   B  2  117 ? 43.044  -94.623  19.066  1.00 74.63  ? 116 ASP   B O   1 
ATOM   2812  C  CB  . ASP   B  2  117 ? 43.981  -96.270  16.470  1.00 89.69  ? 116 ASP   B CB  1 
ATOM   2813  C  CG  . ASP   B  2  117 ? 43.600  -96.242  14.995  1.00 93.09  ? 116 ASP   B CG  1 
ATOM   2814  O  OD1 . ASP   B  2  117 ? 43.319  -95.143  14.476  1.00 97.06  ? 116 ASP   B OD1 1 
ATOM   2815  O  OD2 . ASP   B  2  117 ? 43.582  -97.326  14.374  1.00 103.42 ? 116 ASP   B OD2 1 
ATOM   2816  N  N   . ILE   B  2  118 ? 45.225  -95.253  19.327  1.00 79.63  ? 117 ILE   B N   1 
ATOM   2817  C  CA  . ILE   B  2  118 ? 45.252  -95.268  20.822  1.00 83.59  ? 117 ILE   B CA  1 
ATOM   2818  C  C   . ILE   B  2  118 ? 45.063  -93.836  21.330  1.00 84.09  ? 117 ILE   B C   1 
ATOM   2819  O  O   . ILE   B  2  118 ? 44.249  -93.644  22.254  1.00 87.68  ? 117 ILE   B O   1 
ATOM   2820  C  CB  . ILE   B  2  118 ? 46.550  -95.911  21.353  1.00 84.60  ? 117 ILE   B CB  1 
ATOM   2821  C  CG1 . ILE   B  2  118 ? 46.523  -97.428  21.158  1.00 84.86  ? 117 ILE   B CG1 1 
ATOM   2822  C  CG2 . ILE   B  2  118 ? 46.796  -95.534  22.810  1.00 84.54  ? 117 ILE   B CG2 1 
ATOM   2823  C  CD1 . ILE   B  2  118 ? 47.867  -98.091  21.290  1.00 86.64  ? 117 ILE   B CD1 1 
ATOM   2824  N  N   . LYS   B  2  119 ? 45.792  -92.881  20.745  1.00 85.96  ? 118 LYS   B N   1 
ATOM   2825  C  CA  . LYS   B  2  119 ? 45.696  -91.433  21.072  1.00 86.91  ? 118 LYS   B CA  1 
ATOM   2826  C  C   . LYS   B  2  119 ? 44.266  -90.943  20.823  1.00 86.94  ? 118 LYS   B C   1 
ATOM   2827  O  O   . LYS   B  2  119 ? 43.727  -90.249  21.708  1.00 88.20  ? 118 LYS   B O   1 
ATOM   2828  C  CB  . LYS   B  2  119 ? 46.692  -90.624  20.239  1.00 88.76  ? 118 LYS   B CB  1 
ATOM   2829  C  CG  . LYS   B  2  119 ? 48.155  -90.801  20.619  1.00 91.23  ? 118 LYS   B CG  1 
ATOM   2830  C  CD  . LYS   B  2  119 ? 49.074  -90.050  19.688  1.00 93.92  ? 118 LYS   B CD  1 
ATOM   2831  C  CE  . LYS   B  2  119 ? 50.536  -90.139  20.067  1.00 98.03  ? 118 LYS   B CE  1 
ATOM   2832  N  NZ  . LYS   B  2  119 ? 51.352  -89.206  19.254  1.00 100.56 ? 118 LYS   B NZ  1 
ATOM   2833  N  N   . GLN   B  2  120 ? 43.686  -91.292  19.667  1.00 85.06  ? 119 GLN   B N   1 
ATOM   2834  C  CA  . GLN   B  2  120 ? 42.307  -90.903  19.258  1.00 86.05  ? 119 GLN   B CA  1 
ATOM   2835  C  C   . GLN   B  2  120 ? 41.320  -91.314  20.357  1.00 86.90  ? 119 GLN   B C   1 
ATOM   2836  O  O   . GLN   B  2  120 ? 40.453  -90.491  20.706  1.00 88.38  ? 119 GLN   B O   1 
ATOM   2837  C  CB  . GLN   B  2  120 ? 41.937  -91.542  17.915  1.00 85.96  ? 119 GLN   B CB  1 
ATOM   2838  C  CG  . GLN   B  2  120 ? 40.614  -91.055  17.324  1.00 86.52  ? 119 GLN   B CG  1 
ATOM   2839  C  CD  . GLN   B  2  120 ? 39.356  -91.617  17.951  1.00 87.90  ? 119 GLN   B CD  1 
ATOM   2840  O  OE1 . GLN   B  2  120 ? 38.329  -90.945  18.019  1.00 84.57  ? 119 GLN   B OE1 1 
ATOM   2841  N  NE2 . GLN   B  2  120 ? 39.405  -92.863  18.399  1.00 88.15  ? 119 GLN   B NE2 1 
ATOM   2842  N  N   . GLY   B  2  121 ? 41.448  -92.539  20.877  1.00 87.84  ? 120 GLY   B N   1 
ATOM   2843  C  CA  . GLY   B  2  121 ? 40.563  -93.095  21.919  1.00 88.65  ? 120 GLY   B CA  1 
ATOM   2844  C  C   . GLY   B  2  121 ? 40.475  -92.179  23.127  1.00 88.89  ? 120 GLY   B C   1 
ATOM   2845  O  O   . GLY   B  2  121 ? 39.344  -91.927  23.597  1.00 88.15  ? 120 GLY   B O   1 
ATOM   2846  N  N   . TYR   B  2  122 ? 41.623  -91.669  23.586  1.00 88.65  ? 121 TYR   B N   1 
ATOM   2847  C  CA  . TYR   B  2  122 ? 41.761  -90.816  24.798  1.00 89.43  ? 121 TYR   B CA  1 
ATOM   2848  C  C   . TYR   B  2  122 ? 41.102  -89.446  24.582  1.00 88.35  ? 121 TYR   B C   1 
ATOM   2849  O  O   . TYR   B  2  122 ? 40.992  -88.700  25.576  1.00 90.90  ? 121 TYR   B O   1 
ATOM   2850  C  CB  . TYR   B  2  122 ? 43.234  -90.664  25.190  1.00 89.30  ? 121 TYR   B CB  1 
ATOM   2851  C  CG  . TYR   B  2  122 ? 43.766  -91.776  26.058  1.00 88.72  ? 121 TYR   B CG  1 
ATOM   2852  C  CD1 . TYR   B  2  122 ? 43.891  -93.067  25.574  1.00 89.35  ? 121 TYR   B CD1 1 
ATOM   2853  C  CD2 . TYR   B  2  122 ? 44.140  -91.538  27.369  1.00 91.06  ? 121 TYR   B CD2 1 
ATOM   2854  C  CE1 . TYR   B  2  122 ? 44.369  -94.094  26.369  1.00 90.68  ? 121 TYR   B CE1 1 
ATOM   2855  C  CE2 . TYR   B  2  122 ? 44.625  -92.553  28.177  1.00 91.79  ? 121 TYR   B CE2 1 
ATOM   2856  C  CZ  . TYR   B  2  122 ? 44.741  -93.836  27.676  1.00 91.43  ? 121 TYR   B CZ  1 
ATOM   2857  O  OH  . TYR   B  2  122 ? 45.221  -94.832  28.476  1.00 92.11  ? 121 TYR   B OH  1 
ATOM   2858  N  N   . THR   B  2  123 ? 40.681  -89.126  23.349  1.00 86.96  ? 122 THR   B N   1 
ATOM   2859  C  CA  . THR   B  2  123 ? 40.015  -87.843  22.988  1.00 84.83  ? 122 THR   B CA  1 
ATOM   2860  C  C   . THR   B  2  123 ? 38.503  -88.031  22.806  1.00 86.27  ? 122 THR   B C   1 
ATOM   2861  O  O   . THR   B  2  123 ? 37.805  -87.000  22.763  1.00 84.00  ? 122 THR   B O   1 
ATOM   2862  C  CB  . THR   B  2  123 ? 40.618  -87.220  21.720  1.00 83.38  ? 122 THR   B CB  1 
ATOM   2863  O  OG1 . THR   B  2  123 ? 40.184  -87.945  20.569  1.00 82.34  ? 122 THR   B OG1 1 
ATOM   2864  C  CG2 . THR   B  2  123 ? 42.130  -87.165  21.753  1.00 84.83  ? 122 THR   B CG2 1 
ATOM   2865  N  N   . GLN   B  2  124 ? 38.012  -89.273  22.698  1.00 84.09  ? 123 GLN   B N   1 
ATOM   2866  C  CA  . GLN   B  2  124 ? 36.581  -89.557  22.394  1.00 85.53  ? 123 GLN   B CA  1 
ATOM   2867  C  C   . GLN   B  2  124 ? 35.867  -90.217  23.581  1.00 84.71  ? 123 GLN   B C   1 
ATOM   2868  O  O   . GLN   B  2  124 ? 34.661  -89.954  23.733  1.00 87.55  ? 123 GLN   B O   1 
ATOM   2869  C  CB  . GLN   B  2  124 ? 36.437  -90.432  21.150  1.00 85.98  ? 123 GLN   B CB  1 
ATOM   2870  C  CG  . GLN   B  2  124 ? 34.990  -90.576  20.697  1.00 86.13  ? 123 GLN   B CG  1 
ATOM   2871  C  CD  . GLN   B  2  124 ? 34.856  -90.922  19.235  1.00 86.51  ? 123 GLN   B CD  1 
ATOM   2872  O  OE1 . GLN   B  2  124 ? 34.072  -90.316  18.510  1.00 88.20  ? 123 GLN   B OE1 1 
ATOM   2873  N  NE2 . GLN   B  2  124 ? 35.615  -91.910  18.788  1.00 87.05  ? 123 GLN   B NE2 1 
ATOM   2874  N  N   . HIS   B  2  125 ? 36.550  -91.051  24.372  1.00 84.28  ? 124 HIS   B N   1 
ATOM   2875  C  CA  . HIS   B  2  125 ? 35.942  -91.758  25.533  1.00 87.85  ? 124 HIS   B CA  1 
ATOM   2876  C  C   . HIS   B  2  125 ? 36.935  -91.877  26.694  1.00 87.90  ? 124 HIS   B C   1 
ATOM   2877  O  O   . HIS   B  2  125 ? 38.146  -91.675  26.472  1.00 86.26  ? 124 HIS   B O   1 
ATOM   2878  C  CB  . HIS   B  2  125 ? 35.398  -93.126  25.096  1.00 90.52  ? 124 HIS   B CB  1 
ATOM   2879  C  CG  . HIS   B  2  125 ? 36.366  -93.951  24.315  1.00 90.21  ? 124 HIS   B CG  1 
ATOM   2880  N  ND1 . HIS   B  2  125 ? 37.364  -94.694  24.918  1.00 89.44  ? 124 HIS   B ND1 1 
ATOM   2881  C  CD2 . HIS   B  2  125 ? 36.489  -94.159  22.986  1.00 90.94  ? 124 HIS   B CD2 1 
ATOM   2882  C  CE1 . HIS   B  2  125 ? 38.064  -95.318  23.992  1.00 89.02  ? 124 HIS   B CE1 1 
ATOM   2883  N  NE2 . HIS   B  2  125 ? 37.547  -95.008  22.798  1.00 90.66  ? 124 HIS   B NE2 1 
ATOM   2884  N  N   . GLY   B  2  126 ? 36.415  -92.164  27.893  1.00 91.39  ? 125 GLY   B N   1 
ATOM   2885  C  CA  . GLY   B  2  126 ? 37.197  -92.587  29.071  1.00 92.02  ? 125 GLY   B CA  1 
ATOM   2886  C  C   . GLY   B  2  126 ? 37.445  -91.464  30.065  1.00 92.92  ? 125 GLY   B C   1 
ATOM   2887  O  O   . GLY   B  2  126 ? 37.858  -91.780  31.197  1.00 99.96  ? 125 GLY   B O   1 
ATOM   2888  N  N   . GLY   B  2  127 ? 37.224  -90.204  29.669  1.00 92.76  ? 126 GLY   B N   1 
ATOM   2889  C  CA  . GLY   B  2  127 ? 37.326  -89.028  30.557  1.00 90.86  ? 126 GLY   B CA  1 
ATOM   2890  C  C   . GLY   B  2  127 ? 38.719  -88.836  31.139  1.00 87.93  ? 126 GLY   B C   1 
ATOM   2891  O  O   . GLY   B  2  127 ? 38.817  -88.222  32.220  1.00 88.54  ? 126 GLY   B O   1 
ATOM   2892  N  N   . LEU   B  2  128 ? 39.759  -89.335  30.461  1.00 85.65  ? 127 LEU   B N   1 
ATOM   2893  C  CA  . LEU   B  2  128 ? 41.182  -89.153  30.860  1.00 87.12  ? 127 LEU   B CA  1 
ATOM   2894  C  C   . LEU   B  2  128 ? 41.813  -88.070  29.985  1.00 87.32  ? 127 LEU   B C   1 
ATOM   2895  O  O   . LEU   B  2  128 ? 41.322  -87.857  28.859  1.00 93.28  ? 127 LEU   B O   1 
ATOM   2896  C  CB  . LEU   B  2  128 ? 41.950  -90.468  30.698  1.00 86.75  ? 127 LEU   B CB  1 
ATOM   2897  C  CG  . LEU   B  2  128 ? 41.412  -91.677  31.462  1.00 86.43  ? 127 LEU   B CG  1 
ATOM   2898  C  CD1 . LEU   B  2  128 ? 42.355  -92.857  31.307  1.00 85.48  ? 127 LEU   B CD1 1 
ATOM   2899  C  CD2 . LEU   B  2  128 ? 41.199  -91.364  32.936  1.00 87.22  ? 127 LEU   B CD2 1 
ATOM   2900  N  N   . ARG   B  2  129 ? 42.873  -87.428  30.481  1.00 87.75  ? 128 ARG   B N   1 
ATOM   2901  C  CA  . ARG   B  2  129 ? 43.648  -86.420  29.712  1.00 87.09  ? 128 ARG   B CA  1 
ATOM   2902  C  C   . ARG   B  2  129 ? 44.325  -87.135  28.547  1.00 84.92  ? 128 ARG   B C   1 
ATOM   2903  O  O   . ARG   B  2  129 ? 44.711  -88.295  28.670  1.00 80.79  ? 128 ARG   B O   1 
ATOM   2904  C  CB  . ARG   B  2  129 ? 44.663  -85.689  30.600  1.00 86.32  ? 128 ARG   B CB  1 
ATOM   2905  C  CG  . ARG   B  2  129 ? 45.829  -86.539  31.087  1.00 86.41  ? 128 ARG   B CG  1 
ATOM   2906  C  CD  . ARG   B  2  129 ? 46.953  -85.694  31.661  1.00 85.61  ? 128 ARG   B CD  1 
ATOM   2907  N  NE  . ARG   B  2  129 ? 48.144  -86.484  31.941  1.00 85.36  ? 128 ARG   B NE  1 
ATOM   2908  C  CZ  . ARG   B  2  129 ? 49.107  -86.757  31.063  1.00 86.83  ? 128 ARG   B CZ  1 
ATOM   2909  N  NH1 . ARG   B  2  129 ? 49.042  -86.306  29.821  1.00 89.51  ? 128 ARG   B NH1 1 
ATOM   2910  N  NH2 . ARG   B  2  129 ? 50.142  -87.491  31.428  1.00 87.39  ? 128 ARG   B NH2 1 
ATOM   2911  N  N   . PRO   B  2  130 ? 44.477  -86.473  27.381  1.00 85.13  ? 129 PRO   B N   1 
ATOM   2912  C  CA  . PRO   B  2  130 ? 45.216  -87.055  26.265  1.00 84.77  ? 129 PRO   B CA  1 
ATOM   2913  C  C   . PRO   B  2  130 ? 46.712  -87.144  26.595  1.00 85.29  ? 129 PRO   B C   1 
ATOM   2914  O  O   . PRO   B  2  130 ? 47.144  -86.512  27.535  1.00 82.76  ? 129 PRO   B O   1 
ATOM   2915  C  CB  . PRO   B  2  130 ? 44.954  -86.087  25.103  1.00 86.89  ? 129 PRO   B CB  1 
ATOM   2916  C  CG  . PRO   B  2  130 ? 44.658  -84.766  25.779  1.00 88.57  ? 129 PRO   B CG  1 
ATOM   2917  C  CD  . PRO   B  2  130 ? 43.971  -85.126  27.080  1.00 88.04  ? 129 PRO   B CD  1 
ATOM   2918  N  N   . PHE   B  2  131 ? 47.451  -87.948  25.828  1.00 88.99  ? 130 PHE   B N   1 
ATOM   2919  C  CA  . PHE   B  2  131 ? 48.932  -88.032  25.884  1.00 89.85  ? 130 PHE   B CA  1 
ATOM   2920  C  C   . PHE   B  2  131 ? 49.509  -86.736  25.310  1.00 88.36  ? 130 PHE   B C   1 
ATOM   2921  O  O   . PHE   B  2  131 ? 49.202  -86.408  24.148  1.00 89.57  ? 130 PHE   B O   1 
ATOM   2922  C  CB  . PHE   B  2  131 ? 49.445  -89.252  25.115  1.00 92.70  ? 130 PHE   B CB  1 
ATOM   2923  C  CG  . PHE   B  2  131 ? 49.078  -90.584  25.724  1.00 95.03  ? 130 PHE   B CG  1 
ATOM   2924  C  CD1 . PHE   B  2  131 ? 49.865  -91.154  26.714  1.00 93.58  ? 130 PHE   B CD1 1 
ATOM   2925  C  CD2 . PHE   B  2  131 ? 47.947  -91.271  25.305  1.00 93.89  ? 130 PHE   B CD2 1 
ATOM   2926  C  CE1 . PHE   B  2  131 ? 49.526  -92.376  27.273  1.00 91.68  ? 130 PHE   B CE1 1 
ATOM   2927  C  CE2 . PHE   B  2  131 ? 47.611  -92.495  25.864  1.00 91.70  ? 130 PHE   B CE2 1 
ATOM   2928  C  CZ  . PHE   B  2  131 ? 48.400  -93.043  26.848  1.00 89.72  ? 130 PHE   B CZ  1 
ATOM   2929  N  N   . GLY   B  2  132 ? 50.300  -86.018  26.108  1.00 87.44  ? 131 GLY   B N   1 
ATOM   2930  C  CA  . GLY   B  2  132 ? 50.984  -84.783  25.686  1.00 88.96  ? 131 GLY   B CA  1 
ATOM   2931  C  C   . GLY   B  2  132 ? 52.249  -85.112  24.918  1.00 89.19  ? 131 GLY   B C   1 
ATOM   2932  O  O   . GLY   B  2  132 ? 53.345  -84.825  25.435  1.00 90.92  ? 131 GLY   B O   1 
ATOM   2933  N  N   . VAL   B  2  133 ? 52.104  -85.721  23.740  1.00 88.86  ? 132 VAL   B N   1 
ATOM   2934  C  CA  . VAL   B  2  133 ? 53.247  -86.221  22.920  1.00 92.20  ? 132 VAL   B CA  1 
ATOM   2935  C  C   . VAL   B  2  133 ? 52.935  -86.039  21.433  1.00 89.85  ? 132 VAL   B C   1 
ATOM   2936  O  O   . VAL   B  2  133 ? 51.793  -86.320  21.021  1.00 89.99  ? 132 VAL   B O   1 
ATOM   2937  C  CB  . VAL   B  2  133 ? 53.557  -87.694  23.241  1.00 92.15  ? 132 VAL   B CB  1 
ATOM   2938  C  CG1 . VAL   B  2  133 ? 54.424  -88.341  22.172  1.00 96.83  ? 132 VAL   B CG1 1 
ATOM   2939  C  CG2 . VAL   B  2  133 ? 54.201  -87.840  24.608  1.00 93.86  ? 132 VAL   B CG2 1 
ATOM   2940  N  N   . SER   B  2  134 ? 53.940  -85.590  20.678  1.00 92.77  ? 133 SER   B N   1 
ATOM   2941  C  CA  . SER   B  2  134 ? 54.001  -85.632  19.195  1.00 93.21  ? 133 SER   B CA  1 
ATOM   2942  C  C   . SER   B  2  134 ? 55.224  -86.463  18.791  1.00 92.64  ? 133 SER   B C   1 
ATOM   2943  O  O   . SER   B  2  134 ? 56.316  -86.206  19.335  1.00 91.28  ? 133 SER   B O   1 
ATOM   2944  C  CB  . SER   B  2  134 ? 54.045  -84.242  18.606  1.00 94.76  ? 133 SER   B CB  1 
ATOM   2945  O  OG  . SER   B  2  134 ? 52.757  -83.644  18.619  1.00 95.42  ? 133 SER   B OG  1 
ATOM   2946  N  N   . PHE   B  2  135 ? 55.033  -87.441  17.903  1.00 92.12  ? 134 PHE   B N   1 
ATOM   2947  C  CA  . PHE   B  2  135 ? 56.094  -88.352  17.401  1.00 92.23  ? 134 PHE   B CA  1 
ATOM   2948  C  C   . PHE   B  2  135 ? 56.478  -87.973  15.968  1.00 90.38  ? 134 PHE   B C   1 
ATOM   2949  O  O   . PHE   B  2  135 ? 55.581  -87.607  15.190  1.00 91.12  ? 134 PHE   B O   1 
ATOM   2950  C  CB  . PHE   B  2  135 ? 55.615  -89.806  17.407  1.00 90.86  ? 134 PHE   B CB  1 
ATOM   2951  C  CG  . PHE   B  2  135 ? 55.494  -90.442  18.767  1.00 90.51  ? 134 PHE   B CG  1 
ATOM   2952  C  CD1 . PHE   B  2  135 ? 56.613  -90.638  19.562  1.00 91.30  ? 134 PHE   B CD1 1 
ATOM   2953  C  CD2 . PHE   B  2  135 ? 54.266  -90.879  19.239  1.00 89.12  ? 134 PHE   B CD2 1 
ATOM   2954  C  CE1 . PHE   B  2  135 ? 56.500  -91.238  20.807  1.00 91.38  ? 134 PHE   B CE1 1 
ATOM   2955  C  CE2 . PHE   B  2  135 ? 54.155  -91.480  20.483  1.00 88.51  ? 134 PHE   B CE2 1 
ATOM   2956  C  CZ  . PHE   B  2  135 ? 55.272  -91.659  21.264  1.00 90.40  ? 134 PHE   B CZ  1 
ATOM   2957  N  N   . ILE   B  2  136 ? 57.771  -88.065  15.644  1.00 88.51  ? 135 ILE   B N   1 
ATOM   2958  C  CA  . ILE   B  2  136 ? 58.273  -88.216  14.246  1.00 92.02  ? 135 ILE   B CA  1 
ATOM   2959  C  C   . ILE   B  2  136 ? 58.698  -89.675  14.073  1.00 92.61  ? 135 ILE   B C   1 
ATOM   2960  O  O   . ILE   B  2  136 ? 59.683  -90.064  14.729  1.00 93.78  ? 135 ILE   B O   1 
ATOM   2961  C  CB  . ILE   B  2  136 ? 59.449  -87.273  13.929  1.00 93.84  ? 135 ILE   B CB  1 
ATOM   2962  C  CG1 . ILE   B  2  136 ? 59.073  -85.796  14.079  1.00 96.90  ? 135 ILE   B CG1 1 
ATOM   2963  C  CG2 . ILE   B  2  136 ? 59.998  -87.580  12.541  1.00 94.74  ? 135 ILE   B CG2 1 
ATOM   2964  C  CD1 . ILE   B  2  136 ? 60.225  -84.834  13.853  1.00 99.43  ? 135 ILE   B CD1 1 
ATOM   2965  N  N   . TYR   B  2  137 ? 57.997  -90.431  13.218  1.00 93.83  ? 136 TYR   B N   1 
ATOM   2966  C  CA  . TYR   B  2  137 ? 58.294  -91.853  12.892  1.00 91.78  ? 136 TYR   B CA  1 
ATOM   2967  C  C   . TYR   B  2  137 ? 59.191  -91.920  11.654  1.00 87.59  ? 136 TYR   B C   1 
ATOM   2968  O  O   . TYR   B  2  137 ? 58.758  -91.481  10.573  1.00 86.21  ? 136 TYR   B O   1 
ATOM   2969  C  CB  . TYR   B  2  137 ? 57.023  -92.655  12.603  1.00 88.92  ? 136 TYR   B CB  1 
ATOM   2970  C  CG  . TYR   B  2  137 ? 55.967  -92.597  13.674  1.00 89.83  ? 136 TYR   B CG  1 
ATOM   2971  C  CD1 . TYR   B  2  137 ? 55.052  -91.558  13.714  1.00 92.20  ? 136 TYR   B CD1 1 
ATOM   2972  C  CD2 . TYR   B  2  137 ? 55.863  -93.590  14.632  1.00 90.15  ? 136 TYR   B CD2 1 
ATOM   2973  C  CE1 . TYR   B  2  137 ? 54.071  -91.495  14.688  1.00 93.39  ? 136 TYR   B CE1 1 
ATOM   2974  C  CE2 . TYR   B  2  137 ? 54.885  -93.545  15.612  1.00 93.30  ? 136 TYR   B CE2 1 
ATOM   2975  C  CZ  . TYR   B  2  137 ? 53.985  -92.494  15.640  1.00 94.58  ? 136 TYR   B CZ  1 
ATOM   2976  O  OH  . TYR   B  2  137 ? 53.013  -92.430  16.596  1.00 98.39  ? 136 TYR   B OH  1 
ATOM   2977  N  N   . ALA   B  2  138 ? 60.395  -92.469  11.817  1.00 88.46  ? 137 ALA   B N   1 
ATOM   2978  C  CA  . ALA   B  2  138 ? 61.364  -92.739  10.733  1.00 90.94  ? 137 ALA   B CA  1 
ATOM   2979  C  C   . ALA   B  2  138 ? 61.539  -94.251  10.623  1.00 91.24  ? 137 ALA   B C   1 
ATOM   2980  O  O   . ALA   B  2  138 ? 61.904  -94.862  11.643  1.00 94.66  ? 137 ALA   B O   1 
ATOM   2981  C  CB  . ALA   B  2  138 ? 62.676  -92.059  11.029  1.00 94.41  ? 137 ALA   B CB  1 
ATOM   2982  N  N   . GLY   B  2  139 ? 61.267  -94.831  9.452   1.00 89.65  ? 138 GLY   B N   1 
ATOM   2983  C  CA  . GLY   B  2  139 ? 61.329  -96.291  9.268   1.00 91.67  ? 138 GLY   B CA  1 
ATOM   2984  C  C   . GLY   B  2  139 ? 61.405  -96.714  7.815   1.00 92.12  ? 138 GLY   B C   1 
ATOM   2985  O  O   . GLY   B  2  139 ? 61.255  -95.857  6.923   1.00 88.59  ? 138 GLY   B O   1 
ATOM   2986  N  N   . TYR   B  2  140 ? 61.634  -98.012  7.601   1.00 96.56  ? 139 TYR   B N   1 
ATOM   2987  C  CA  . TYR   B  2  140 ? 61.748  -98.665  6.273   1.00 99.00  ? 139 TYR   B CA  1 
ATOM   2988  C  C   . TYR   B  2  140 ? 60.941  -99.968  6.262   1.00 98.48  ? 139 TYR   B C   1 
ATOM   2989  O  O   . TYR   B  2  140 ? 60.983  -100.724 7.253   1.00 95.11  ? 139 TYR   B O   1 
ATOM   2990  C  CB  . TYR   B  2  140 ? 63.213  -98.950  5.934   1.00 102.48 ? 139 TYR   B CB  1 
ATOM   2991  C  CG  . TYR   B  2  140 ? 63.410  -99.671  4.625   1.00 104.92 ? 139 TYR   B CG  1 
ATOM   2992  C  CD1 . TYR   B  2  140 ? 63.296  -101.049 4.544   1.00 108.01 ? 139 TYR   B CD1 1 
ATOM   2993  C  CD2 . TYR   B  2  140 ? 63.697  -98.976  3.462   1.00 106.83 ? 139 TYR   B CD2 1 
ATOM   2994  C  CE1 . TYR   B  2  140 ? 63.467  -101.719 3.344   1.00 113.06 ? 139 TYR   B CE1 1 
ATOM   2995  C  CE2 . TYR   B  2  140 ? 63.873  -99.629  2.254   1.00 109.81 ? 139 TYR   B CE2 1 
ATOM   2996  C  CZ  . TYR   B  2  140 ? 63.756  -101.006 2.194   1.00 112.56 ? 139 TYR   B CZ  1 
ATOM   2997  O  OH  . TYR   B  2  140 ? 63.928  -101.656 1.006   1.00 120.30 ? 139 TYR   B OH  1 
ATOM   2998  N  N   . ASP   B  2  141 ? 60.235  -100.215 5.157   1.00 96.97  ? 140 ASP   B N   1 
ATOM   2999  C  CA  . ASP   B  2  141 ? 59.643  -101.533 4.808   1.00 99.64  ? 140 ASP   B CA  1 
ATOM   3000  C  C   . ASP   B  2  141 ? 59.787  -101.730 3.294   1.00 100.63 ? 140 ASP   B C   1 
ATOM   3001  O  O   . ASP   B  2  141 ? 60.058  -100.738 2.595   1.00 97.16  ? 140 ASP   B O   1 
ATOM   3002  C  CB  . ASP   B  2  141 ? 58.198  -101.645 5.303   1.00 100.07 ? 140 ASP   B CB  1 
ATOM   3003  C  CG  . ASP   B  2  141 ? 57.252  -100.614 4.710   1.00 96.91  ? 140 ASP   B CG  1 
ATOM   3004  O  OD1 . ASP   B  2  141 ? 57.179  -100.531 3.470   1.00 94.97  ? 140 ASP   B OD1 1 
ATOM   3005  O  OD2 . ASP   B  2  141 ? 56.597  -99.897  5.495   1.00 94.73  ? 140 ASP   B OD2 1 
ATOM   3006  N  N   . ASP   B  2  142 ? 59.608  -102.964 2.814   1.00 108.60 ? 141 ASP   B N   1 
ATOM   3007  C  CA  . ASP   B  2  142 ? 59.882  -103.355 1.404   1.00 113.17 ? 141 ASP   B CA  1 
ATOM   3008  C  C   . ASP   B  2  142 ? 58.724  -102.932 0.483   1.00 110.82 ? 141 ASP   B C   1 
ATOM   3009  O  O   . ASP   B  2  142 ? 58.814  -103.230 -0.724  1.00 113.30 ? 141 ASP   B O   1 
ATOM   3010  C  CB  . ASP   B  2  142 ? 60.185  -104.854 1.295   1.00 116.99 ? 141 ASP   B CB  1 
ATOM   3011  C  CG  . ASP   B  2  142 ? 59.034  -105.772 1.677   1.00 119.20 ? 141 ASP   B CG  1 
ATOM   3012  O  OD1 . ASP   B  2  142 ? 57.975  -105.255 2.091   1.00 116.48 ? 141 ASP   B OD1 1 
ATOM   3013  O  OD2 . ASP   B  2  142 ? 59.210  -107.004 1.563   1.00 122.90 ? 141 ASP   B OD2 1 
ATOM   3014  N  N   . ARG   B  2  143 ? 57.687  -102.266 1.005   1.00 108.56 ? 142 ARG   B N   1 
ATOM   3015  C  CA  . ARG   B  2  143 ? 56.523  -101.806 0.196   1.00 109.82 ? 142 ARG   B CA  1 
ATOM   3016  C  C   . ARG   B  2  143 ? 56.756  -100.372 -0.297  1.00 110.75 ? 142 ARG   B C   1 
ATOM   3017  O  O   . ARG   B  2  143 ? 56.675  -100.163 -1.522  1.00 117.43 ? 142 ARG   B O   1 
ATOM   3018  C  CB  . ARG   B  2  143 ? 55.214  -101.885 0.988   1.00 108.56 ? 142 ARG   B CB  1 
ATOM   3019  C  CG  . ARG   B  2  143 ? 53.985  -101.547 0.156   1.00 110.73 ? 142 ARG   B CG  1 
ATOM   3020  C  CD  . ARG   B  2  143 ? 52.707  -101.491 0.969   1.00 110.96 ? 142 ARG   B CD  1 
ATOM   3021  N  NE  . ARG   B  2  143 ? 51.561  -101.089 0.162   1.00 112.60 ? 142 ARG   B NE  1 
ATOM   3022  C  CZ  . ARG   B  2  143 ? 50.308  -100.997 0.605   1.00 112.36 ? 142 ARG   B CZ  1 
ATOM   3023  N  NH1 . ARG   B  2  143 ? 50.017  -101.275 1.865   1.00 116.32 ? 142 ARG   B NH1 1 
ATOM   3024  N  NH2 . ARG   B  2  143 ? 49.343  -100.627 -0.221  1.00 110.78 ? 142 ARG   B NH2 1 
ATOM   3025  N  N   . TYR   B  2  144 ? 57.004  -99.428  0.620   1.00 108.94 ? 143 TYR   B N   1 
ATOM   3026  C  CA  . TYR   B  2  144 ? 57.126  -97.970  0.339   1.00 106.79 ? 143 TYR   B CA  1 
ATOM   3027  C  C   . TYR   B  2  144 ? 58.572  -97.486  0.506   1.00 105.71 ? 143 TYR   B C   1 
ATOM   3028  O  O   . TYR   B  2  144 ? 58.829  -96.309  0.195   1.00 109.26 ? 143 TYR   B O   1 
ATOM   3029  C  CB  . TYR   B  2  144 ? 56.201  -97.166  1.257   1.00 101.79 ? 143 TYR   B CB  1 
ATOM   3030  C  CG  . TYR   B  2  144 ? 54.734  -97.284  0.930   1.00 101.13 ? 143 TYR   B CG  1 
ATOM   3031  C  CD1 . TYR   B  2  144 ? 54.246  -96.896  -0.307  1.00 98.97  ? 143 TYR   B CD1 1 
ATOM   3032  C  CD2 . TYR   B  2  144 ? 53.830  -97.775  1.859   1.00 102.33 ? 143 TYR   B CD2 1 
ATOM   3033  C  CE1 . TYR   B  2  144 ? 52.900  -97.001  -0.618  1.00 99.26  ? 143 TYR   B CE1 1 
ATOM   3034  C  CE2 . TYR   B  2  144 ? 52.481  -97.885  1.565   1.00 102.92 ? 143 TYR   B CE2 1 
ATOM   3035  C  CZ  . TYR   B  2  144 ? 52.014  -97.496  0.322   1.00 99.90  ? 143 TYR   B CZ  1 
ATOM   3036  O  OH  . TYR   B  2  144 ? 50.688  -97.598  0.022   1.00 102.93 ? 143 TYR   B OH  1 
ATOM   3037  N  N   . GLY   B  2  145 ? 59.482  -98.348  0.970   1.00 107.05 ? 144 GLY   B N   1 
ATOM   3038  C  CA  . GLY   B  2  145 ? 60.866  -97.966  1.310   1.00 106.16 ? 144 GLY   B CA  1 
ATOM   3039  C  C   . GLY   B  2  145 ? 60.892  -97.015  2.495   1.00 104.77 ? 144 GLY   B C   1 
ATOM   3040  O  O   . GLY   B  2  145 ? 60.181  -97.286  3.485   1.00 104.02 ? 144 GLY   B O   1 
ATOM   3041  N  N   . TYR   B  2  146 ? 61.656  -95.924  2.393   1.00 102.47 ? 145 TYR   B N   1 
ATOM   3042  C  CA  . TYR   B  2  146 ? 61.845  -94.926  3.477   1.00 101.12 ? 145 TYR   B CA  1 
ATOM   3043  C  C   . TYR   B  2  146 ? 60.569  -94.096  3.637   1.00 99.96  ? 145 TYR   B C   1 
ATOM   3044  O  O   . TYR   B  2  146 ? 59.985  -93.690  2.611   1.00 99.69  ? 145 TYR   B O   1 
ATOM   3045  C  CB  . TYR   B  2  146 ? 63.064  -94.051  3.186   1.00 102.04 ? 145 TYR   B CB  1 
ATOM   3046  C  CG  . TYR   B  2  146 ? 64.364  -94.812  3.185   1.00 103.07 ? 145 TYR   B CG  1 
ATOM   3047  C  CD1 . TYR   B  2  146 ? 64.893  -95.312  4.364   1.00 102.81 ? 145 TYR   B CD1 1 
ATOM   3048  C  CD2 . TYR   B  2  146 ? 65.056  -95.047  2.008   1.00 103.57 ? 145 TYR   B CD2 1 
ATOM   3049  C  CE1 . TYR   B  2  146 ? 66.084  -96.019  4.377   1.00 105.10 ? 145 TYR   B CE1 1 
ATOM   3050  C  CE2 . TYR   B  2  146 ? 66.249  -95.751  2.003   1.00 104.97 ? 145 TYR   B CE2 1 
ATOM   3051  C  CZ  . TYR   B  2  146 ? 66.765  -96.239  3.191   1.00 106.11 ? 145 TYR   B CZ  1 
ATOM   3052  O  OH  . TYR   B  2  146 ? 67.941  -96.928  3.192   1.00 111.54 ? 145 TYR   B OH  1 
ATOM   3053  N  N   . GLN   B  2  147 ? 60.149  -93.875  4.888   1.00 99.89  ? 146 GLN   B N   1 
ATOM   3054  C  CA  . GLN   B  2  147 ? 58.907  -93.140  5.252   1.00 101.12 ? 146 GLN   B CA  1 
ATOM   3055  C  C   . GLN   B  2  147 ? 59.152  -92.291  6.508   1.00 100.21 ? 146 GLN   B C   1 
ATOM   3056  O  O   . GLN   B  2  147 ? 59.699  -92.828  7.491   1.00 100.76 ? 146 GLN   B O   1 
ATOM   3057  C  CB  . GLN   B  2  147 ? 57.760  -94.124  5.497   1.00 98.76  ? 146 GLN   B CB  1 
ATOM   3058  C  CG  . GLN   B  2  147 ? 57.414  -94.989  4.291   1.00 102.22 ? 146 GLN   B CG  1 
ATOM   3059  C  CD  . GLN   B  2  147 ? 56.577  -96.192  4.660   1.00 100.93 ? 146 GLN   B CD  1 
ATOM   3060  O  OE1 . GLN   B  2  147 ? 55.360  -96.106  4.811   1.00 101.01 ? 146 GLN   B OE1 1 
ATOM   3061  N  NE2 . GLN   B  2  147 ? 57.226  -97.337  4.799   1.00 104.01 ? 146 GLN   B NE2 1 
ATOM   3062  N  N   . LEU   B  2  148 ? 58.768  -91.012  6.463   1.00 100.08 ? 147 LEU   B N   1 
ATOM   3063  C  CA  . LEU   B  2  148 ? 58.599  -90.146  7.660   1.00 99.04  ? 147 LEU   B CA  1 
ATOM   3064  C  C   . LEU   B  2  148 ? 57.104  -89.953  7.907   1.00 94.88  ? 147 LEU   B C   1 
ATOM   3065  O  O   . LEU   B  2  148 ? 56.381  -89.668  6.936   1.00 92.96  ? 147 LEU   B O   1 
ATOM   3066  C  CB  . LEU   B  2  148 ? 59.256  -88.781  7.444   1.00 102.04 ? 147 LEU   B CB  1 
ATOM   3067  C  CG  . LEU   B  2  148 ? 60.756  -88.682  7.714   1.00 104.27 ? 147 LEU   B CG  1 
ATOM   3068  C  CD1 . LEU   B  2  148 ? 61.265  -87.315  7.289   1.00 104.83 ? 147 LEU   B CD1 1 
ATOM   3069  C  CD2 . LEU   B  2  148 ? 61.081  -88.935  9.180   1.00 105.06 ? 147 LEU   B CD2 1 
ATOM   3070  N  N   . TYR   B  2  149 ? 56.676  -90.089  9.161   1.00 96.90  ? 148 TYR   B N   1 
ATOM   3071  C  CA  . TYR   B  2  149 ? 55.313  -89.739  9.631   1.00 94.78  ? 148 TYR   B CA  1 
ATOM   3072  C  C   . TYR   B  2  149 ? 55.427  -88.828  10.854  1.00 92.98  ? 148 TYR   B C   1 
ATOM   3073  O  O   . TYR   B  2  149 ? 56.518  -88.735  11.456  1.00 89.73  ? 148 TYR   B O   1 
ATOM   3074  C  CB  . TYR   B  2  149 ? 54.510  -90.995  9.974   1.00 93.58  ? 148 TYR   B CB  1 
ATOM   3075  C  CG  . TYR   B  2  149 ? 54.226  -91.908  8.811   1.00 92.45  ? 148 TYR   B CG  1 
ATOM   3076  C  CD1 . TYR   B  2  149 ? 53.129  -91.701  7.990   1.00 92.45  ? 148 TYR   B CD1 1 
ATOM   3077  C  CD2 . TYR   B  2  149 ? 55.044  -92.993  8.540   1.00 94.63  ? 148 TYR   B CD2 1 
ATOM   3078  C  CE1 . TYR   B  2  149 ? 52.856  -92.544  6.924   1.00 93.28  ? 148 TYR   B CE1 1 
ATOM   3079  C  CE2 . TYR   B  2  149 ? 54.785  -93.845  7.479   1.00 94.82  ? 148 TYR   B CE2 1 
ATOM   3080  C  CZ  . TYR   B  2  149 ? 53.687  -93.621  6.667   1.00 94.42  ? 148 TYR   B CZ  1 
ATOM   3081  O  OH  . TYR   B  2  149 ? 53.431  -94.462  5.623   1.00 92.10  ? 148 TYR   B OH  1 
ATOM   3082  N  N   . THR   B  2  150 ? 54.325  -88.164  11.194  1.00 89.62  ? 149 THR   B N   1 
ATOM   3083  C  CA  . THR   B  2  150 ? 54.116  -87.510  12.507  1.00 91.02  ? 149 THR   B CA  1 
ATOM   3084  C  C   . THR   B  2  150 ? 52.717  -87.859  13.007  1.00 89.18  ? 149 THR   B C   1 
ATOM   3085  O  O   . THR   B  2  150 ? 51.805  -87.954  12.171  1.00 89.05  ? 149 THR   B O   1 
ATOM   3086  C  CB  . THR   B  2  150 ? 54.301  -85.990  12.436  1.00 91.61  ? 149 THR   B CB  1 
ATOM   3087  O  OG1 . THR   B  2  150 ? 53.523  -85.515  11.340  1.00 92.48  ? 149 THR   B OG1 1 
ATOM   3088  C  CG2 . THR   B  2  150 ? 55.751  -85.587  12.283  1.00 93.83  ? 149 THR   B CG2 1 
ATOM   3089  N  N   . SER   B  2  151 ? 52.583  -88.061  14.317  1.00 90.64  ? 150 SER   B N   1 
ATOM   3090  C  CA  . SER   B  2  151 ? 51.290  -88.117  15.043  1.00 90.54  ? 150 SER   B CA  1 
ATOM   3091  C  C   . SER   B  2  151 ? 51.327  -87.098  16.189  1.00 88.60  ? 150 SER   B C   1 
ATOM   3092  O  O   . SER   B  2  151 ? 52.440  -86.748  16.636  1.00 87.22  ? 150 SER   B O   1 
ATOM   3093  C  CB  . SER   B  2  151 ? 50.995  -89.514  15.526  1.00 89.36  ? 150 SER   B CB  1 
ATOM   3094  O  OG  . SER   B  2  151 ? 51.850  -89.878  16.600  1.00 90.42  ? 150 SER   B OG  1 
ATOM   3095  N  N   . ASN   B  2  152 ? 50.156  -86.621  16.616  1.00 86.55  ? 151 ASN   B N   1 
ATOM   3096  C  CA  . ASN   B  2  152 ? 50.001  -85.612  17.698  1.00 86.44  ? 151 ASN   B CA  1 
ATOM   3097  C  C   . ASN   B  2  152 ? 48.868  -86.055  18.620  1.00 83.73  ? 151 ASN   B C   1 
ATOM   3098  O  O   . ASN   B  2  152 ? 48.145  -86.996  18.302  1.00 81.36  ? 151 ASN   B O   1 
ATOM   3099  C  CB  . ASN   B  2  152 ? 49.799  -84.215  17.105  1.00 87.62  ? 151 ASN   B CB  1 
ATOM   3100  C  CG  . ASN   B  2  152 ? 48.472  -84.046  16.395  1.00 89.48  ? 151 ASN   B CG  1 
ATOM   3101  O  OD1 . ASN   B  2  152 ? 47.432  -84.464  16.896  1.00 91.18  ? 151 ASN   B OD1 1 
ATOM   3102  N  ND2 . ASN   B  2  152 ? 48.493  -83.415  15.232  1.00 93.36  ? 151 ASN   B ND2 1 
ATOM   3103  N  N   . PRO   B  2  153 ? 48.666  -85.386  19.779  1.00 84.74  ? 152 PRO   B N   1 
ATOM   3104  C  CA  . PRO   B  2  153 ? 47.662  -85.808  20.762  1.00 86.23  ? 152 PRO   B CA  1 
ATOM   3105  C  C   . PRO   B  2  153 ? 46.231  -86.054  20.249  1.00 88.80  ? 152 PRO   B C   1 
ATOM   3106  O  O   . PRO   B  2  153 ? 45.495  -86.740  20.938  1.00 92.55  ? 152 PRO   B O   1 
ATOM   3107  C  CB  . PRO   B  2  153 ? 47.642  -84.633  21.753  1.00 86.15  ? 152 PRO   B CB  1 
ATOM   3108  C  CG  . PRO   B  2  153 ? 49.045  -84.080  21.685  1.00 85.80  ? 152 PRO   B CG  1 
ATOM   3109  C  CD  . PRO   B  2  153 ? 49.416  -84.199  20.224  1.00 85.73  ? 152 PRO   B CD  1 
ATOM   3110  N  N   . SER   B  2  154 ? 45.862  -85.497  19.089  1.00 90.28  ? 153 SER   B N   1 
ATOM   3111  C  CA  . SER   B  2  154 ? 44.531  -85.681  18.448  1.00 93.51  ? 153 SER   B CA  1 
ATOM   3112  C  C   . SER   B  2  154 ? 44.381  -87.112  17.928  1.00 94.90  ? 153 SER   B C   1 
ATOM   3113  O  O   . SER   B  2  154 ? 43.227  -87.558  17.776  1.00 98.94  ? 153 SER   B O   1 
ATOM   3114  C  CB  . SER   B  2  154 ? 44.306  -84.705  17.326  1.00 96.48  ? 153 SER   B CB  1 
ATOM   3115  O  OG  . SER   B  2  154 ? 45.087  -85.048  16.190  1.00 99.84  ? 153 SER   B OG  1 
ATOM   3116  N  N   . GLY   B  2  155 ? 45.502  -87.779  17.637  1.00 96.88  ? 154 GLY   B N   1 
ATOM   3117  C  CA  . GLY   B  2  155 ? 45.536  -89.110  17.002  1.00 97.57  ? 154 GLY   B CA  1 
ATOM   3118  C  C   . GLY   B  2  155 ? 45.477  -88.992  15.490  1.00 96.90  ? 154 GLY   B C   1 
ATOM   3119  O  O   . GLY   B  2  155 ? 45.122  -89.981  14.823  1.00 100.06 ? 154 GLY   B O   1 
ATOM   3120  N  N   . ASN   B  2  156 ? 45.799  -87.808  14.969  1.00 95.56  ? 155 ASN   B N   1 
ATOM   3121  C  CA  . ASN   B  2  156 ? 45.917  -87.541  13.515  1.00 97.10  ? 155 ASN   B CA  1 
ATOM   3122  C  C   . ASN   B  2  156 ? 47.382  -87.755  13.126  1.00 92.49  ? 155 ASN   B C   1 
ATOM   3123  O  O   . ASN   B  2  156 ? 48.258  -87.266  13.865  1.00 93.29  ? 155 ASN   B O   1 
ATOM   3124  C  CB  . ASN   B  2  156 ? 45.411  -86.137  13.170  1.00 100.58 ? 155 ASN   B CB  1 
ATOM   3125  C  CG  . ASN   B  2  156 ? 45.553  -85.787  11.703  1.00 105.63 ? 155 ASN   B CG  1 
ATOM   3126  O  OD1 . ASN   B  2  156 ? 45.928  -84.665  11.369  1.00 110.73 ? 155 ASN   B OD1 1 
ATOM   3127  N  ND2 . ASN   B  2  156 ? 45.259  -86.730  10.820  1.00 104.67 ? 155 ASN   B ND2 1 
ATOM   3128  N  N   . TYR   B  2  157 ? 47.634  -88.479  12.032  1.00 88.37  ? 156 TYR   B N   1 
ATOM   3129  C  CA  . TYR   B  2  157 ? 48.998  -88.732  11.501  1.00 88.27  ? 156 TYR   B CA  1 
ATOM   3130  C  C   . TYR   B  2  157 ? 49.045  -88.357  10.018  1.00 86.90  ? 156 TYR   B C   1 
ATOM   3131  O  O   . TYR   B  2  157 ? 48.008  -88.450  9.337   1.00 88.97  ? 156 TYR   B O   1 
ATOM   3132  C  CB  . TYR   B  2  157 ? 49.429  -90.178  11.768  1.00 88.61  ? 156 TYR   B CB  1 
ATOM   3133  C  CG  . TYR   B  2  157 ? 48.810  -91.230  10.880  1.00 88.04  ? 156 TYR   B CG  1 
ATOM   3134  C  CD1 . TYR   B  2  157 ? 47.570  -91.776  11.173  1.00 86.33  ? 156 TYR   B CD1 1 
ATOM   3135  C  CD2 . TYR   B  2  157 ? 49.479  -91.708  9.764   1.00 87.56  ? 156 TYR   B CD2 1 
ATOM   3136  C  CE1 . TYR   B  2  157 ? 47.001  -92.750  10.370  1.00 86.77  ? 156 TYR   B CE1 1 
ATOM   3137  C  CE2 . TYR   B  2  157 ? 48.924  -92.681  8.949   1.00 88.34  ? 156 TYR   B CE2 1 
ATOM   3138  C  CZ  . TYR   B  2  157 ? 47.680  -93.205  9.254   1.00 88.81  ? 156 TYR   B CZ  1 
ATOM   3139  O  OH  . TYR   B  2  157 ? 47.126  -94.168  8.459   1.00 94.39  ? 156 TYR   B OH  1 
ATOM   3140  N  N   . THR   B  2  158 ? 50.218  -87.920  9.551   1.00 87.74  ? 157 THR   B N   1 
ATOM   3141  C  CA  . THR   B  2  158 ? 50.483  -87.524  8.142   1.00 90.75  ? 157 THR   B CA  1 
ATOM   3142  C  C   . THR   B  2  158 ? 51.918  -87.899  7.760   1.00 92.90  ? 157 THR   B C   1 
ATOM   3143  O  O   . THR   B  2  158 ? 52.771  -87.988  8.669   1.00 92.41  ? 157 THR   B O   1 
ATOM   3144  C  CB  . THR   B  2  158 ? 50.235  -86.026  7.925   1.00 91.27  ? 157 THR   B CB  1 
ATOM   3145  O  OG1 . THR   B  2  158 ? 50.897  -85.299  8.959   1.00 91.80  ? 157 THR   B OG1 1 
ATOM   3146  C  CG2 . THR   B  2  158 ? 48.766  -85.665  7.925   1.00 91.24  ? 157 THR   B CG2 1 
ATOM   3147  N  N   . GLY   B  2  159 ? 52.156  -88.096  6.459   1.00 96.69  ? 158 GLY   B N   1 
ATOM   3148  C  CA  . GLY   B  2  159 ? 53.465  -88.455  5.878   1.00 98.55  ? 158 GLY   B CA  1 
ATOM   3149  C  C   . GLY   B  2  159 ? 54.196  -87.231  5.350   1.00 96.46  ? 158 GLY   B C   1 
ATOM   3150  O  O   . GLY   B  2  159 ? 53.523  -86.314  4.834   1.00 96.36  ? 158 GLY   B O   1 
ATOM   3151  N  N   . TRP   B  2  160 ? 55.529  -87.219  5.459   1.00 97.30  ? 159 TRP   B N   1 
ATOM   3152  C  CA  . TRP   B  2  160 ? 56.384  -86.045  5.145   1.00 97.81  ? 159 TRP   B CA  1 
ATOM   3153  C  C   . TRP   B  2  160 ? 57.652  -86.467  4.400   1.00 99.81  ? 159 TRP   B C   1 
ATOM   3154  O  O   . TRP   B  2  160 ? 58.066  -87.635  4.523   1.00 99.77  ? 159 TRP   B O   1 
ATOM   3155  C  CB  . TRP   B  2  160 ? 56.727  -85.296  6.435   1.00 97.23  ? 159 TRP   B CB  1 
ATOM   3156  C  CG  . TRP   B  2  160 ? 55.516  -84.817  7.171   1.00 99.64  ? 159 TRP   B CG  1 
ATOM   3157  C  CD1 . TRP   B  2  160 ? 54.890  -85.430  8.216   1.00 99.60  ? 159 TRP   B CD1 1 
ATOM   3158  C  CD2 . TRP   B  2  160 ? 54.761  -83.626  6.894   1.00 99.96  ? 159 TRP   B CD2 1 
ATOM   3159  N  NE1 . TRP   B  2  160 ? 53.806  -84.697  8.614   1.00 98.66  ? 159 TRP   B NE1 1 
ATOM   3160  C  CE2 . TRP   B  2  160 ? 53.700  -83.585  7.823   1.00 100.48 ? 159 TRP   B CE2 1 
ATOM   3161  C  CE3 . TRP   B  2  160 ? 54.881  -82.592  5.961   1.00 103.43 ? 159 TRP   B CE3 1 
ATOM   3162  C  CZ2 . TRP   B  2  160 ? 52.768  -82.550  7.843   1.00 100.93 ? 159 TRP   B CZ2 1 
ATOM   3163  C  CZ3 . TRP   B  2  160 ? 53.957  -81.570  5.979   1.00 105.37 ? 159 TRP   B CZ3 1 
ATOM   3164  C  CH2 . TRP   B  2  160 ? 52.917  -81.550  6.909   1.00 103.95 ? 159 TRP   B CH2 1 
ATOM   3165  N  N   . LYS   B  2  161 ? 58.226  -85.527  3.647   1.00 101.37 ? 160 LYS   B N   1 
ATOM   3166  C  CA  . LYS   B  2  161 ? 59.591  -85.606  3.062   1.00 105.77 ? 160 LYS   B CA  1 
ATOM   3167  C  C   . LYS   B  2  161 ? 60.589  -85.032  4.071   1.00 104.71 ? 160 LYS   B C   1 
ATOM   3168  O  O   . LYS   B  2  161 ? 61.706  -85.573  4.178   1.00 109.81 ? 160 LYS   B O   1 
ATOM   3169  C  CB  . LYS   B  2  161 ? 59.649  -84.819  1.752   1.00 108.23 ? 160 LYS   B CB  1 
ATOM   3170  C  CG  . LYS   B  2  161 ? 58.877  -85.436  0.598   1.00 109.43 ? 160 LYS   B CG  1 
ATOM   3171  C  CD  . LYS   B  2  161 ? 58.758  -84.514  -0.589  1.00 113.14 ? 160 LYS   B CD  1 
ATOM   3172  C  CE  . LYS   B  2  161 ? 58.031  -85.143  -1.757  1.00 116.32 ? 160 LYS   B CE  1 
ATOM   3173  N  NZ  . LYS   B  2  161 ? 57.872  -84.179  -2.871  1.00 119.51 ? 160 LYS   B NZ  1 
ATOM   3174  N  N   . ALA   B  2  162 ? 60.192  -83.951  4.748   1.00 104.08 ? 161 ALA   B N   1 
ATOM   3175  C  CA  . ALA   B  2  162 ? 60.888  -83.347  5.907   1.00 101.53 ? 161 ALA   B CA  1 
ATOM   3176  C  C   . ALA   B  2  162 ? 59.841  -82.694  6.815   1.00 98.27  ? 161 ALA   B C   1 
ATOM   3177  O  O   . ALA   B  2  162 ? 58.844  -82.169  6.282   1.00 99.61  ? 161 ALA   B O   1 
ATOM   3178  C  CB  . ALA   B  2  162 ? 61.920  -82.356  5.430   1.00 105.12 ? 161 ALA   B CB  1 
ATOM   3179  N  N   . ILE   B  2  163 ? 60.038  -82.752  8.134   1.00 95.48  ? 162 ILE   B N   1 
ATOM   3180  C  CA  . ILE   B  2  163 ? 59.060  -82.227  9.132   1.00 96.21  ? 162 ILE   B CA  1 
ATOM   3181  C  C   . ILE   B  2  163 ? 59.779  -81.957  10.458  1.00 96.35  ? 162 ILE   B C   1 
ATOM   3182  O  O   . ILE   B  2  163 ? 60.806  -82.613  10.727  1.00 99.42  ? 162 ILE   B O   1 
ATOM   3183  C  CB  . ILE   B  2  163 ? 57.875  -83.205  9.295   1.00 93.55  ? 162 ILE   B CB  1 
ATOM   3184  C  CG1 . ILE   B  2  163 ? 56.741  -82.621  10.144  1.00 93.03  ? 162 ILE   B CG1 1 
ATOM   3185  C  CG2 . ILE   B  2  163 ? 58.346  -84.547  9.837   1.00 91.42  ? 162 ILE   B CG2 1 
ATOM   3186  C  CD1 . ILE   B  2  163 ? 56.071  -81.406  9.542   1.00 93.99  ? 162 ILE   B CD1 1 
ATOM   3187  N  N   . SER   B  2  164 ? 59.246  -81.014  11.237  1.00 96.37  ? 163 SER   B N   1 
ATOM   3188  C  CA  . SER   B  2  164 ? 59.690  -80.666  12.610  1.00 97.03  ? 163 SER   B CA  1 
ATOM   3189  C  C   . SER   B  2  164 ? 58.505  -80.773  13.578  1.00 93.82  ? 163 SER   B C   1 
ATOM   3190  O  O   . SER   B  2  164 ? 57.352  -80.618  13.129  1.00 93.62  ? 163 SER   B O   1 
ATOM   3191  C  CB  . SER   B  2  164 ? 60.296  -79.288  12.632  1.00 99.55  ? 163 SER   B CB  1 
ATOM   3192  O  OG  . SER   B  2  164 ? 59.352  -78.316  12.203  1.00 101.17 ? 163 SER   B OG  1 
ATOM   3193  N  N   . VAL   B  2  165 ? 58.783  -81.044  14.856  1.00 92.74  ? 164 VAL   B N   1 
ATOM   3194  C  CA  . VAL   B  2  165 ? 57.781  -81.027  15.964  1.00 94.86  ? 164 VAL   B CA  1 
ATOM   3195  C  C   . VAL   B  2  165 ? 58.413  -80.370  17.190  1.00 95.19  ? 164 VAL   B C   1 
ATOM   3196  O  O   . VAL   B  2  165 ? 59.655  -80.385  17.296  1.00 97.09  ? 164 VAL   B O   1 
ATOM   3197  C  CB  . VAL   B  2  165 ? 57.287  -82.436  16.328  1.00 92.52  ? 164 VAL   B CB  1 
ATOM   3198  C  CG1 . VAL   B  2  165 ? 56.441  -83.036  15.220  1.00 95.40  ? 164 VAL   B CG1 1 
ATOM   3199  C  CG2 . VAL   B  2  165 ? 58.441  -83.355  16.701  1.00 93.01  ? 164 VAL   B CG2 1 
ATOM   3200  N  N   . GLY   B  2  166 ? 57.571  -79.869  18.095  1.00 97.20  ? 165 GLY   B N   1 
ATOM   3201  C  CA  . GLY   B  2  166 ? 57.993  -79.173  19.324  1.00 102.27 ? 165 GLY   B CA  1 
ATOM   3202  C  C   . GLY   B  2  166 ? 58.070  -77.671  19.114  1.00 105.04 ? 165 GLY   B C   1 
ATOM   3203  O  O   . GLY   B  2  166 ? 57.113  -77.105  18.550  1.00 108.78 ? 165 GLY   B O   1 
ATOM   3204  N  N   . ALA   B  2  167 ? 59.177  -77.051  19.535  1.00 108.38 ? 166 ALA   B N   1 
ATOM   3205  C  CA  . ALA   B  2  167 ? 59.379  -75.584  19.549  1.00 108.07 ? 166 ALA   B CA  1 
ATOM   3206  C  C   . ALA   B  2  167 ? 59.781  -75.086  18.156  1.00 111.18 ? 166 ALA   B C   1 
ATOM   3207  O  O   . ALA   B  2  167 ? 60.505  -75.815  17.447  1.00 111.22 ? 166 ALA   B O   1 
ATOM   3208  C  CB  . ALA   B  2  167 ? 60.416  -75.218  20.581  1.00 107.99 ? 166 ALA   B CB  1 
ATOM   3209  N  N   . ASN   B  2  168 ? 59.308  -73.888  17.793  1.00 112.36 ? 167 ASN   B N   1 
ATOM   3210  C  CA  . ASN   B  2  168 ? 59.754  -73.111  16.606  1.00 116.13 ? 167 ASN   B CA  1 
ATOM   3211  C  C   . ASN   B  2  168 ? 59.566  -73.937  15.328  1.00 112.10 ? 167 ASN   B C   1 
ATOM   3212  O  O   . ASN   B  2  168 ? 60.454  -73.883  14.457  1.00 112.56 ? 167 ASN   B O   1 
ATOM   3213  C  CB  . ASN   B  2  168 ? 61.214  -72.675  16.750  1.00 122.48 ? 167 ASN   B CB  1 
ATOM   3214  C  CG  . ASN   B  2  168 ? 61.489  -71.955  18.053  1.00 126.46 ? 167 ASN   B CG  1 
ATOM   3215  O  OD1 . ASN   B  2  168 ? 60.710  -71.101  18.472  1.00 132.84 ? 167 ASN   B OD1 1 
ATOM   3216  N  ND2 . ASN   B  2  168 ? 62.595  -72.287  18.700  1.00 130.41 ? 167 ASN   B ND2 1 
ATOM   3217  N  N   . THR   B  2  169 ? 58.457  -74.672  15.219  1.00 111.31 ? 168 THR   B N   1 
ATOM   3218  C  CA  . THR   B  2  169 ? 58.112  -75.481  14.019  1.00 114.42 ? 168 THR   B CA  1 
ATOM   3219  C  C   . THR   B  2  169 ? 57.871  -74.547  12.829  1.00 116.00 ? 168 THR   B C   1 
ATOM   3220  O  O   . THR   B  2  169 ? 58.294  -74.901  11.713  1.00 116.23 ? 168 THR   B O   1 
ATOM   3221  C  CB  . THR   B  2  169 ? 56.891  -76.376  14.266  1.00 113.75 ? 168 THR   B CB  1 
ATOM   3222  O  OG1 . THR   B  2  169 ? 55.829  -75.550  14.745  1.00 118.04 ? 168 THR   B OG1 1 
ATOM   3223  C  CG2 . THR   B  2  169 ? 57.169  -77.486  15.254  1.00 113.57 ? 168 THR   B CG2 1 
ATOM   3224  N  N   . SER   B  2  170 ? 57.227  -73.400  13.070  1.00 116.94 ? 169 SER   B N   1 
ATOM   3225  C  CA  . SER   B  2  170 ? 56.859  -72.391  12.041  1.00 118.63 ? 169 SER   B CA  1 
ATOM   3226  C  C   . SER   B  2  170 ? 58.117  -71.920  11.301  1.00 118.50 ? 169 SER   B C   1 
ATOM   3227  O  O   . SER   B  2  170 ? 58.109  -71.941  10.054  1.00 117.59 ? 169 SER   B O   1 
ATOM   3228  C  CB  . SER   B  2  170 ? 56.116  -71.230  12.656  1.00 120.25 ? 169 SER   B CB  1 
ATOM   3229  O  OG  . SER   B  2  170 ? 55.514  -70.422  11.657  1.00 121.70 ? 169 SER   B OG  1 
ATOM   3230  N  N   . ALA   B  2  171 ? 59.156  -71.524  12.043  1.00 118.59 ? 170 ALA   B N   1 
ATOM   3231  C  CA  . ALA   B  2  171 ? 60.455  -71.064  11.498  1.00 120.05 ? 170 ALA   B CA  1 
ATOM   3232  C  C   . ALA   B  2  171 ? 61.209  -72.249  10.880  1.00 118.85 ? 170 ALA   B C   1 
ATOM   3233  O  O   . ALA   B  2  171 ? 61.755  -72.086  9.773   1.00 121.46 ? 170 ALA   B O   1 
ATOM   3234  C  CB  . ALA   B  2  171 ? 61.269  -70.393  12.577  1.00 122.60 ? 170 ALA   B CB  1 
ATOM   3235  N  N   . ALA   B  2  172 ? 61.235  -73.393  11.572  1.00 115.18 ? 171 ALA   B N   1 
ATOM   3236  C  CA  . ALA   B  2  172 ? 61.946  -74.626  11.155  1.00 115.03 ? 171 ALA   B CA  1 
ATOM   3237  C  C   . ALA   B  2  172 ? 61.387  -75.132  9.820   1.00 113.94 ? 171 ALA   B C   1 
ATOM   3238  O  O   . ALA   B  2  172 ? 62.198  -75.483  8.942   1.00 116.53 ? 171 ALA   B O   1 
ATOM   3239  C  CB  . ALA   B  2  172 ? 61.841  -75.680  12.230  1.00 111.88 ? 171 ALA   B CB  1 
ATOM   3240  N  N   . GLN   B  2  173 ? 60.059  -75.157  9.672   1.00 111.83 ? 172 GLN   B N   1 
ATOM   3241  C  CA  . GLN   B  2  173 ? 59.367  -75.689  8.467   1.00 110.38 ? 172 GLN   B CA  1 
ATOM   3242  C  C   . GLN   B  2  173 ? 59.683  -74.805  7.255   1.00 113.43 ? 172 GLN   B C   1 
ATOM   3243  O  O   . GLN   B  2  173 ? 59.914  -75.370  6.170   1.00 114.90 ? 172 GLN   B O   1 
ATOM   3244  C  CB  . GLN   B  2  173 ? 57.855  -75.784  8.689   1.00 109.40 ? 172 GLN   B CB  1 
ATOM   3245  C  CG  . GLN   B  2  173 ? 57.171  -76.782  7.764   1.00 110.47 ? 172 GLN   B CG  1 
ATOM   3246  C  CD  . GLN   B  2  173 ? 57.613  -78.205  8.012   1.00 109.94 ? 172 GLN   B CD  1 
ATOM   3247  O  OE1 . GLN   B  2  173 ? 58.128  -78.543  9.077   1.00 108.43 ? 172 GLN   B OE1 1 
ATOM   3248  N  NE2 . GLN   B  2  173 ? 57.418  -79.058  7.019   1.00 110.92 ? 172 GLN   B NE2 1 
ATOM   3249  N  N   . THR   B  2  174 ? 59.688  -73.478  7.432   1.00 112.00 ? 173 THR   B N   1 
ATOM   3250  C  CA  . THR   B  2  174 ? 60.031  -72.490  6.373   1.00 116.17 ? 173 THR   B CA  1 
ATOM   3251  C  C   . THR   B  2  174 ? 61.449  -72.775  5.860   1.00 115.72 ? 173 THR   B C   1 
ATOM   3252  O  O   . THR   B  2  174 ? 61.624  -72.813  4.628   1.00 119.58 ? 173 THR   B O   1 
ATOM   3253  C  CB  . THR   B  2  174 ? 59.906  -71.044  6.870   1.00 114.68 ? 173 THR   B CB  1 
ATOM   3254  O  OG1 . THR   B  2  174 ? 58.691  -70.914  7.608   1.00 111.58 ? 173 THR   B OG1 1 
ATOM   3255  C  CG2 . THR   B  2  174 ? 59.917  -70.037  5.741   1.00 118.04 ? 173 THR   B CG2 1 
ATOM   3256  N  N   . LEU   B  2  175 ? 62.410  -72.978  6.772   1.00 116.40 ? 174 LEU   B N   1 
ATOM   3257  C  CA  . LEU   B  2  175 ? 63.849  -73.214  6.455   1.00 118.20 ? 174 LEU   B CA  1 
ATOM   3258  C  C   . LEU   B  2  175 ? 64.018  -74.541  5.707   1.00 119.07 ? 174 LEU   B C   1 
ATOM   3259  O  O   . LEU   B  2  175 ? 64.826  -74.574  4.756   1.00 115.45 ? 174 LEU   B O   1 
ATOM   3260  C  CB  . LEU   B  2  175 ? 64.677  -73.217  7.745   1.00 120.23 ? 174 LEU   B CB  1 
ATOM   3261  C  CG  . LEU   B  2  175 ? 64.870  -71.860  8.419   1.00 122.96 ? 174 LEU   B CG  1 
ATOM   3262  C  CD1 . LEU   B  2  175 ? 65.561  -72.017  9.765   1.00 123.04 ? 174 LEU   B CD1 1 
ATOM   3263  C  CD2 . LEU   B  2  175 ? 65.661  -70.913  7.534   1.00 126.90 ? 174 LEU   B CD2 1 
ATOM   3264  N  N   . LEU   B  2  176 ? 63.309  -75.592  6.138   1.00 117.70 ? 175 LEU   B N   1 
ATOM   3265  C  CA  . LEU   B  2  176 ? 63.328  -76.934  5.490   1.00 118.18 ? 175 LEU   B CA  1 
ATOM   3266  C  C   . LEU   B  2  176 ? 62.706  -76.824  4.093   1.00 118.29 ? 175 LEU   B C   1 
ATOM   3267  O  O   . LEU   B  2  176 ? 63.297  -77.371  3.140   1.00 114.72 ? 175 LEU   B O   1 
ATOM   3268  C  CB  . LEU   B  2  176 ? 62.567  -77.947  6.355   1.00 116.02 ? 175 LEU   B CB  1 
ATOM   3269  C  CG  . LEU   B  2  176 ? 63.259  -78.374  7.651   1.00 115.37 ? 175 LEU   B CG  1 
ATOM   3270  C  CD1 . LEU   B  2  176 ? 62.315  -79.191  8.519   1.00 113.28 ? 175 LEU   B CD1 1 
ATOM   3271  C  CD2 . LEU   B  2  176 ? 64.532  -79.159  7.368   1.00 116.54 ? 175 LEU   B CD2 1 
ATOM   3272  N  N   . GLN   B  2  177 ? 61.572  -76.124  3.984   1.00 119.47 ? 176 GLN   B N   1 
ATOM   3273  C  CA  . GLN   B  2  177 ? 60.832  -75.888  2.714   1.00 121.73 ? 176 GLN   B CA  1 
ATOM   3274  C  C   . GLN   B  2  177 ? 61.734  -75.155  1.712   1.00 124.20 ? 176 GLN   B C   1 
ATOM   3275  O  O   . GLN   B  2  177 ? 61.525  -75.327  0.497   1.00 131.20 ? 176 GLN   B O   1 
ATOM   3276  C  CB  . GLN   B  2  177 ? 59.563  -75.078  2.985   1.00 124.41 ? 176 GLN   B CB  1 
ATOM   3277  C  CG  . GLN   B  2  177 ? 58.590  -75.064  1.815   1.00 127.05 ? 176 GLN   B CG  1 
ATOM   3278  C  CD  . GLN   B  2  177 ? 57.256  -74.423  2.118   1.00 133.42 ? 176 GLN   B CD  1 
ATOM   3279  O  OE1 . GLN   B  2  177 ? 56.494  -74.101  1.208   1.00 140.63 ? 176 GLN   B OE1 1 
ATOM   3280  N  NE2 . GLN   B  2  177 ? 56.946  -74.229  3.392   1.00 131.44 ? 176 GLN   B NE2 1 
ATOM   3281  N  N   . MET   B  2  178 ? 62.694  -74.372  2.211   1.00 124.42 ? 177 MET   B N   1 
ATOM   3282  C  CA  . MET   B  2  178 ? 63.606  -73.519  1.406   1.00 128.79 ? 177 MET   B CA  1 
ATOM   3283  C  C   . MET   B  2  178 ? 64.712  -74.362  0.755   1.00 130.12 ? 177 MET   B C   1 
ATOM   3284  O  O   . MET   B  2  178 ? 64.926  -74.188  -0.459  1.00 133.79 ? 177 MET   B O   1 
ATOM   3285  C  CB  . MET   B  2  178 ? 64.239  -72.447  2.298   1.00 131.30 ? 177 MET   B CB  1 
ATOM   3286  C  CG  . MET   B  2  178 ? 64.955  -71.355  1.538   1.00 135.16 ? 177 MET   B CG  1 
ATOM   3287  S  SD  . MET   B  2  178 ? 65.319  -69.952  2.616   1.00 137.20 ? 177 MET   B SD  1 
ATOM   3288  C  CE  . MET   B  2  178 ? 63.741  -69.105  2.601   1.00 138.97 ? 177 MET   B CE  1 
ATOM   3289  N  N   . ASP   B  2  179 ? 65.385  -75.233  1.521   1.00 131.83 ? 178 ASP   B N   1 
ATOM   3290  C  CA  . ASP   B  2  179 ? 66.661  -75.896  1.122   1.00 131.19 ? 178 ASP   B CA  1 
ATOM   3291  C  C   . ASP   B  2  179 ? 66.486  -77.395  0.823   1.00 128.43 ? 178 ASP   B C   1 
ATOM   3292  O  O   . ASP   B  2  179 ? 67.497  -78.023  0.440   1.00 125.96 ? 178 ASP   B O   1 
ATOM   3293  C  CB  . ASP   B  2  179 ? 67.733  -75.718  2.201   1.00 129.20 ? 178 ASP   B CB  1 
ATOM   3294  C  CG  . ASP   B  2  179 ? 68.103  -74.271  2.470   1.00 130.97 ? 178 ASP   B CG  1 
ATOM   3295  O  OD1 . ASP   B  2  179 ? 67.746  -73.410  1.643   1.00 127.54 ? 178 ASP   B OD1 1 
ATOM   3296  O  OD2 . ASP   B  2  179 ? 68.749  -74.021  3.506   1.00 128.92 ? 178 ASP   B OD2 1 
ATOM   3297  N  N   . TYR   B  2  180 ? 65.286  -77.964  0.982   1.00 125.26 ? 179 TYR   B N   1 
ATOM   3298  C  CA  . TYR   B  2  180 ? 65.018  -79.389  0.652   1.00 124.64 ? 179 TYR   B CA  1 
ATOM   3299  C  C   . TYR   B  2  180 ? 64.786  -79.526  -0.858  1.00 127.80 ? 179 TYR   B C   1 
ATOM   3300  O  O   . TYR   B  2  180 ? 64.144  -78.639  -1.452  1.00 132.83 ? 179 TYR   B O   1 
ATOM   3301  C  CB  . TYR   B  2  180 ? 63.824  -79.947  1.434   1.00 122.09 ? 179 TYR   B CB  1 
ATOM   3302  C  CG  . TYR   B  2  180 ? 63.570  -81.415  1.193   1.00 119.70 ? 179 TYR   B CG  1 
ATOM   3303  C  CD1 . TYR   B  2  180 ? 64.239  -82.387  1.920   1.00 117.69 ? 179 TYR   B CD1 1 
ATOM   3304  C  CD2 . TYR   B  2  180 ? 62.681  -81.837  0.217   1.00 120.86 ? 179 TYR   B CD2 1 
ATOM   3305  C  CE1 . TYR   B  2  180 ? 64.023  -83.737  1.694   1.00 116.38 ? 179 TYR   B CE1 1 
ATOM   3306  C  CE2 . TYR   B  2  180 ? 62.453  -83.184  -0.023  1.00 117.98 ? 179 TYR   B CE2 1 
ATOM   3307  C  CZ  . TYR   B  2  180 ? 63.127  -84.138  0.719   1.00 115.70 ? 179 TYR   B CZ  1 
ATOM   3308  O  OH  . TYR   B  2  180 ? 62.907  -85.465  0.495   1.00 114.57 ? 179 TYR   B OH  1 
ATOM   3309  N  N   . LYS   B  2  181 ? 65.314  -80.603  -1.450  1.00 131.56 ? 180 LYS   B N   1 
ATOM   3310  C  CA  . LYS   B  2  181 ? 64.972  -81.078  -2.820  1.00 136.00 ? 180 LYS   B CA  1 
ATOM   3311  C  C   . LYS   B  2  181 ? 64.979  -82.613  -2.826  1.00 135.42 ? 180 LYS   B C   1 
ATOM   3312  O  O   . LYS   B  2  181 ? 65.603  -83.208  -1.927  1.00 134.27 ? 180 LYS   B O   1 
ATOM   3313  C  CB  . LYS   B  2  181 ? 65.903  -80.476  -3.880  1.00 140.95 ? 180 LYS   B CB  1 
ATOM   3314  C  CG  . LYS   B  2  181 ? 67.345  -80.224  -3.457  1.00 147.49 ? 180 LYS   B CG  1 
ATOM   3315  C  CD  . LYS   B  2  181 ? 68.040  -79.171  -4.305  1.00 153.45 ? 180 LYS   B CD  1 
ATOM   3316  C  CE  . LYS   B  2  181 ? 68.018  -79.467  -5.791  1.00 156.55 ? 180 LYS   B CE  1 
ATOM   3317  N  NZ  . LYS   B  2  181 ? 68.815  -80.668  -6.134  1.00 158.19 ? 180 LYS   B NZ  1 
ATOM   3318  N  N   . ASP   B  2  182 ? 64.302  -83.217  -3.807  1.00 138.73 ? 181 ASP   B N   1 
ATOM   3319  C  CA  . ASP   B  2  182 ? 63.868  -84.641  -3.796  1.00 133.39 ? 181 ASP   B CA  1 
ATOM   3320  C  C   . ASP   B  2  182 ? 65.062  -85.585  -3.989  1.00 136.78 ? 181 ASP   B C   1 
ATOM   3321  O  O   . ASP   B  2  182 ? 65.071  -86.645  -3.332  1.00 134.36 ? 181 ASP   B O   1 
ATOM   3322  C  CB  . ASP   B  2  182 ? 62.780  -84.879  -4.846  1.00 134.88 ? 181 ASP   B CB  1 
ATOM   3323  C  CG  . ASP   B  2  182 ? 61.478  -84.153  -4.545  1.00 130.28 ? 181 ASP   B CG  1 
ATOM   3324  O  OD1 . ASP   B  2  182 ? 61.257  -83.805  -3.367  1.00 127.61 ? 181 ASP   B OD1 1 
ATOM   3325  O  OD2 . ASP   B  2  182 ? 60.698  -83.935  -5.491  1.00 132.72 ? 181 ASP   B OD2 1 
ATOM   3326  N  N   . ASP   B  2  183 ? 66.028  -85.222  -4.840  1.00 138.79 ? 182 ASP   B N   1 
ATOM   3327  C  CA  . ASP   B  2  183 ? 67.197  -86.079  -5.194  1.00 143.87 ? 182 ASP   B CA  1 
ATOM   3328  C  C   . ASP   B  2  183 ? 68.276  -86.008  -4.100  1.00 139.72 ? 182 ASP   B C   1 
ATOM   3329  O  O   . ASP   B  2  183 ? 69.369  -86.565  -4.321  1.00 146.22 ? 182 ASP   B O   1 
ATOM   3330  C  CB  . ASP   B  2  183 ? 67.776  -85.694  -6.559  1.00 145.61 ? 182 ASP   B CB  1 
ATOM   3331  C  CG  . ASP   B  2  183 ? 68.197  -84.238  -6.677  1.00 150.61 ? 182 ASP   B CG  1 
ATOM   3332  O  OD1 . ASP   B  2  183 ? 68.755  -83.704  -5.698  1.00 153.98 ? 182 ASP   B OD1 1 
ATOM   3333  O  OD2 . ASP   B  2  183 ? 67.956  -83.645  -7.748  1.00 149.05 ? 182 ASP   B OD2 1 
ATOM   3334  N  N   . MET   B  2  184 ? 67.980  -85.358  -2.971  1.00 134.19 ? 183 MET   B N   1 
ATOM   3335  C  CA  . MET   B  2  184 ? 68.897  -85.172  -1.812  1.00 135.27 ? 183 MET   B CA  1 
ATOM   3336  C  C   . MET   B  2  184 ? 69.446  -86.524  -1.334  1.00 136.23 ? 183 MET   B C   1 
ATOM   3337  O  O   . MET   B  2  184 ? 68.725  -87.535  -1.458  1.00 136.44 ? 183 MET   B O   1 
ATOM   3338  C  CB  . MET   B  2  184 ? 68.144  -84.509  -0.657  1.00 132.62 ? 183 MET   B CB  1 
ATOM   3339  C  CG  . MET   B  2  184 ? 68.998  -83.616  0.199   1.00 133.07 ? 183 MET   B CG  1 
ATOM   3340  S  SD  . MET   B  2  184 ? 67.973  -82.673  1.348   1.00 135.61 ? 183 MET   B SD  1 
ATOM   3341  C  CE  . MET   B  2  184 ? 69.224  -81.641  2.109   1.00 138.54 ? 183 MET   B CE  1 
ATOM   3342  N  N   . LYS   B  2  185 ? 70.668  -86.525  -0.789  1.00 137.08 ? 184 LYS   B N   1 
ATOM   3343  C  CA  . LYS   B  2  185 ? 71.331  -87.712  -0.180  1.00 139.36 ? 184 LYS   B CA  1 
ATOM   3344  C  C   . LYS   B  2  185 ? 71.321  -87.566  1.347   1.00 137.12 ? 184 LYS   B C   1 
ATOM   3345  O  O   . LYS   B  2  185 ? 71.054  -86.448  1.827   1.00 142.54 ? 184 LYS   B O   1 
ATOM   3346  C  CB  . LYS   B  2  185 ? 72.764  -87.857  -0.703  1.00 141.18 ? 184 LYS   B CB  1 
ATOM   3347  C  CG  . LYS   B  2  185 ? 72.888  -88.309  -2.152  1.00 145.28 ? 184 LYS   B CG  1 
ATOM   3348  C  CD  . LYS   B  2  185 ? 72.583  -89.780  -2.369  1.00 147.07 ? 184 LYS   B CD  1 
ATOM   3349  C  CE  . LYS   B  2  185 ? 71.317  -90.029  -3.162  1.00 149.20 ? 184 LYS   B CE  1 
ATOM   3350  N  NZ  . LYS   B  2  185 ? 71.525  -89.787  -4.610  1.00 152.70 ? 184 LYS   B NZ  1 
ATOM   3351  N  N   . VAL   B  2  186 ? 71.610  -88.653  2.072   1.00 139.20 ? 185 VAL   B N   1 
ATOM   3352  C  CA  . VAL   B  2  186 ? 71.573  -88.717  3.565   1.00 137.30 ? 185 VAL   B CA  1 
ATOM   3353  C  C   . VAL   B  2  186 ? 72.514  -87.652  4.141   1.00 133.67 ? 185 VAL   B C   1 
ATOM   3354  O  O   . VAL   B  2  186 ? 72.087  -86.936  5.066   1.00 130.45 ? 185 VAL   B O   1 
ATOM   3355  C  CB  . VAL   B  2  186 ? 71.936  -90.121  4.090   1.00 140.13 ? 185 VAL   B CB  1 
ATOM   3356  C  CG1 . VAL   B  2  186 ? 72.231  -90.117  5.585   1.00 142.31 ? 185 VAL   B CG1 1 
ATOM   3357  C  CG2 . VAL   B  2  186 ? 70.854  -91.140  3.771   1.00 141.78 ? 185 VAL   B CG2 1 
ATOM   3358  N  N   . ASP   B  2  187 ? 73.743  -87.560  3.620   1.00 133.43 ? 186 ASP   B N   1 
ATOM   3359  C  CA  . ASP   B  2  187 ? 74.816  -86.676  4.156   1.00 135.32 ? 186 ASP   B CA  1 
ATOM   3360  C  C   . ASP   B  2  187 ? 74.404  -85.207  3.987   1.00 132.08 ? 186 ASP   B C   1 
ATOM   3361  O  O   . ASP   B  2  187 ? 74.747  -84.396  4.871   1.00 129.15 ? 186 ASP   B O   1 
ATOM   3362  C  CB  . ASP   B  2  187 ? 76.169  -86.966  3.501   1.00 137.69 ? 186 ASP   B CB  1 
ATOM   3363  C  CG  . ASP   B  2  187 ? 76.614  -88.413  3.638   1.00 137.07 ? 186 ASP   B CG  1 
ATOM   3364  O  OD1 . ASP   B  2  187 ? 75.937  -89.287  3.062   1.00 136.75 ? 186 ASP   B OD1 1 
ATOM   3365  O  OD2 . ASP   B  2  187 ? 77.624  -88.656  4.328   1.00 142.60 ? 186 ASP   B OD2 1 
ATOM   3366  N  N   . ASP   B  2  188 ? 73.696  -84.885  2.899   1.00 128.14 ? 187 ASP   B N   1 
ATOM   3367  C  CA  . ASP   B  2  188 ? 73.106  -83.543  2.645   1.00 126.27 ? 187 ASP   B CA  1 
ATOM   3368  C  C   . ASP   B  2  188 ? 72.009  -83.275  3.682   1.00 125.09 ? 187 ASP   B C   1 
ATOM   3369  O  O   . ASP   B  2  188 ? 71.965  -82.150  4.213   1.00 122.99 ? 187 ASP   B O   1 
ATOM   3370  C  CB  . ASP   B  2  188 ? 72.556  -83.432  1.219   1.00 126.49 ? 187 ASP   B CB  1 
ATOM   3371  C  CG  . ASP   B  2  188 ? 73.599  -83.613  0.129   1.00 127.73 ? 187 ASP   B CG  1 
ATOM   3372  O  OD1 . ASP   B  2  188 ? 74.763  -83.224  0.356   1.00 129.87 ? 187 ASP   B OD1 1 
ATOM   3373  O  OD2 . ASP   B  2  188 ? 73.237  -84.143  -0.940  1.00 126.95 ? 187 ASP   B OD2 1 
ATOM   3374  N  N   . ALA   B  2  189 ? 71.162  -84.275  3.954   1.00 123.74 ? 188 ALA   B N   1 
ATOM   3375  C  CA  . ALA   B  2  189 ? 70.019  -84.206  4.899   1.00 121.58 ? 188 ALA   B CA  1 
ATOM   3376  C  C   . ALA   B  2  189 ? 70.524  -84.026  6.336   1.00 118.24 ? 188 ALA   B C   1 
ATOM   3377  O  O   . ALA   B  2  189 ? 69.863  -83.298  7.101   1.00 113.81 ? 188 ALA   B O   1 
ATOM   3378  C  CB  . ALA   B  2  189 ? 69.164  -85.443  4.775   1.00 121.54 ? 188 ALA   B CB  1 
ATOM   3379  N  N   . ILE   B  2  190 ? 71.632  -84.686  6.692   1.00 120.07 ? 189 ILE   B N   1 
ATOM   3380  C  CA  . ILE   B  2  190 ? 72.317  -84.533  8.012   1.00 125.51 ? 189 ILE   B CA  1 
ATOM   3381  C  C   . ILE   B  2  190 ? 72.652  -83.050  8.211   1.00 124.67 ? 189 ILE   B C   1 
ATOM   3382  O  O   . ILE   B  2  190 ? 72.365  -82.518  9.302   1.00 125.53 ? 189 ILE   B O   1 
ATOM   3383  C  CB  . ILE   B  2  190 ? 73.572  -85.429  8.099   1.00 130.46 ? 189 ILE   B CB  1 
ATOM   3384  C  CG1 . ILE   B  2  190 ? 73.195  -86.905  8.266   1.00 132.34 ? 189 ILE   B CG1 1 
ATOM   3385  C  CG2 . ILE   B  2  190 ? 74.507  -84.958  9.206   1.00 132.44 ? 189 ILE   B CG2 1 
ATOM   3386  C  CD1 . ILE   B  2  190 ? 74.345  -87.875  8.075   1.00 133.55 ? 189 ILE   B CD1 1 
ATOM   3387  N  N   . GLU   B  2  191 ? 73.229  -82.417  7.185   1.00 125.46 ? 190 GLU   B N   1 
ATOM   3388  C  CA  . GLU   B  2  191 ? 73.679  -81.001  7.207   1.00 126.75 ? 190 GLU   B CA  1 
ATOM   3389  C  C   . GLU   B  2  191 ? 72.467  -80.074  7.364   1.00 122.83 ? 190 GLU   B C   1 
ATOM   3390  O  O   . GLU   B  2  191 ? 72.529  -79.182  8.232   1.00 124.09 ? 190 GLU   B O   1 
ATOM   3391  C  CB  . GLU   B  2  191 ? 74.465  -80.677  5.937   1.00 131.75 ? 190 GLU   B CB  1 
ATOM   3392  C  CG  . GLU   B  2  191 ? 75.242  -79.378  6.022   1.00 136.72 ? 190 GLU   B CG  1 
ATOM   3393  C  CD  . GLU   B  2  191 ? 76.219  -79.154  4.880   1.00 142.57 ? 190 GLU   B CD  1 
ATOM   3394  O  OE1 . GLU   B  2  191 ? 76.958  -80.102  4.542   1.00 145.03 ? 190 GLU   B OE1 1 
ATOM   3395  O  OE2 . GLU   B  2  191 ? 76.236  -78.034  4.329   1.00 144.37 ? 190 GLU   B OE2 1 
ATOM   3396  N  N   . LEU   B  2  192 ? 71.414  -80.279  6.562   1.00 120.31 ? 191 LEU   B N   1 
ATOM   3397  C  CA  . LEU   B  2  192 ? 70.174  -79.449  6.574   1.00 118.76 ? 191 LEU   B CA  1 
ATOM   3398  C  C   . LEU   B  2  192 ? 69.566  -79.486  7.984   1.00 117.72 ? 191 LEU   B C   1 
ATOM   3399  O  O   . LEU   B  2  192 ? 69.260  -78.402  8.520   1.00 117.94 ? 191 LEU   B O   1 
ATOM   3400  C  CB  . LEU   B  2  192 ? 69.176  -79.972  5.529   1.00 115.12 ? 191 LEU   B CB  1 
ATOM   3401  C  CG  . LEU   B  2  192 ? 68.268  -78.941  4.846   1.00 113.68 ? 191 LEU   B CG  1 
ATOM   3402  C  CD1 . LEU   B  2  192 ? 66.973  -79.590  4.380   1.00 113.21 ? 191 LEU   B CD1 1 
ATOM   3403  C  CD2 . LEU   B  2  192 ? 67.940  -77.757  5.743   1.00 113.37 ? 191 LEU   B CD2 1 
ATOM   3404  N  N   . ALA   B  2  193 ? 69.416  -80.687  8.556   1.00 117.36 ? 192 ALA   B N   1 
ATOM   3405  C  CA  . ALA   B  2  193 ? 68.838  -80.936  9.899   1.00 116.70 ? 192 ALA   B CA  1 
ATOM   3406  C  C   . ALA   B  2  193 ? 69.577  -80.103  10.951  1.00 118.60 ? 192 ALA   B C   1 
ATOM   3407  O  O   . ALA   B  2  193 ? 68.903  -79.370  11.701  1.00 117.49 ? 192 ALA   B O   1 
ATOM   3408  C  CB  . ALA   B  2  193 ? 68.906  -82.406  10.233  1.00 116.67 ? 192 ALA   B CB  1 
ATOM   3409  N  N   . LEU   B  2  194 ? 70.908  -80.219  10.998  1.00 123.18 ? 193 LEU   B N   1 
ATOM   3410  C  CA  . LEU   B  2  194 ? 71.783  -79.516  11.978  1.00 129.73 ? 193 LEU   B CA  1 
ATOM   3411  C  C   . LEU   B  2  194 ? 71.738  -78.001  11.732  1.00 130.14 ? 193 LEU   B C   1 
ATOM   3412  O  O   . LEU   B  2  194 ? 71.686  -77.250  12.726  1.00 125.64 ? 193 LEU   B O   1 
ATOM   3413  C  CB  . LEU   B  2  194 ? 73.217  -80.048  11.867  1.00 137.14 ? 193 LEU   B CB  1 
ATOM   3414  C  CG  . LEU   B  2  194 ? 73.442  -81.477  12.360  1.00 140.88 ? 193 LEU   B CG  1 
ATOM   3415  C  CD1 . LEU   B  2  194 ? 74.828  -81.968  11.967  1.00 146.06 ? 193 LEU   B CD1 1 
ATOM   3416  C  CD2 . LEU   B  2  194 ? 73.251  -81.581  13.867  1.00 142.35 ? 193 LEU   B CD2 1 
ATOM   3417  N  N   . LYS   B  2  195 ? 71.764  -77.571  10.464  1.00 132.13 ? 194 LYS   B N   1 
ATOM   3418  C  CA  . LYS   B  2  195 ? 71.740  -76.133  10.073  1.00 133.91 ? 194 LYS   B CA  1 
ATOM   3419  C  C   . LYS   B  2  195 ? 70.423  -75.497  10.534  1.00 132.13 ? 194 LYS   B C   1 
ATOM   3420  O  O   . LYS   B  2  195 ? 70.466  -74.341  11.001  1.00 131.66 ? 194 LYS   B O   1 
ATOM   3421  C  CB  . LYS   B  2  195 ? 71.917  -75.955  8.560   1.00 138.17 ? 194 LYS   B CB  1 
ATOM   3422  C  CG  . LYS   B  2  195 ? 73.357  -76.003  8.064   1.00 141.55 ? 194 LYS   B CG  1 
ATOM   3423  C  CD  . LYS   B  2  195 ? 73.474  -76.009  6.553   1.00 143.61 ? 194 LYS   B CD  1 
ATOM   3424  C  CE  . LYS   B  2  195 ? 73.330  -74.634  5.936   1.00 148.39 ? 194 LYS   B CE  1 
ATOM   3425  N  NZ  . LYS   B  2  195 ? 74.603  -73.876  5.992   1.00 152.65 ? 194 LYS   B NZ  1 
ATOM   3426  N  N   . THR   B  2  196 ? 69.301  -76.215  10.402  1.00 124.47 ? 195 THR   B N   1 
ATOM   3427  C  CA  . THR   B  2  196 ? 67.945  -75.722  10.766  1.00 122.38 ? 195 THR   B CA  1 
ATOM   3428  C  C   . THR   B  2  196 ? 67.860  -75.531  12.283  1.00 121.09 ? 195 THR   B C   1 
ATOM   3429  O  O   . THR   B  2  196 ? 67.458  -74.433  12.709  1.00 129.03 ? 195 THR   B O   1 
ATOM   3430  C  CB  . THR   B  2  196 ? 66.828  -76.660  10.290  1.00 121.26 ? 195 THR   B CB  1 
ATOM   3431  O  OG1 . THR   B  2  196 ? 67.062  -77.004  8.925   1.00 124.95 ? 195 THR   B OG1 1 
ATOM   3432  C  CG2 . THR   B  2  196 ? 65.456  -76.036  10.435  1.00 120.12 ? 195 THR   B CG2 1 
ATOM   3433  N  N   . LEU   B  2  197 ? 68.214  -76.561  13.057  1.00 117.18 ? 196 LEU   B N   1 
ATOM   3434  C  CA  . LEU   B  2  197 ? 68.201  -76.529  14.546  1.00 116.69 ? 196 LEU   B CA  1 
ATOM   3435  C  C   . LEU   B  2  197 ? 69.064  -75.364  15.042  1.00 116.50 ? 196 LEU   B C   1 
ATOM   3436  O  O   . LEU   B  2  197 ? 68.629  -74.677  15.982  1.00 117.30 ? 196 LEU   B O   1 
ATOM   3437  C  CB  . LEU   B  2  197 ? 68.728  -77.855  15.106  1.00 115.06 ? 196 LEU   B CB  1 
ATOM   3438  C  CG  . LEU   B  2  197 ? 67.774  -79.047  15.037  1.00 111.86 ? 196 LEU   B CG  1 
ATOM   3439  C  CD1 . LEU   B  2  197 ? 68.491  -80.322  15.450  1.00 111.11 ? 196 LEU   B CD1 1 
ATOM   3440  C  CD2 . LEU   B  2  197 ? 66.544  -78.829  15.906  1.00 109.04 ? 196 LEU   B CD2 1 
ATOM   3441  N  N   . SER   B  2  198 ? 70.237  -75.167  14.428  1.00 121.96 ? 197 SER   B N   1 
ATOM   3442  C  CA  . SER   B  2  198 ? 71.228  -74.110  14.769  1.00 125.84 ? 197 SER   B CA  1 
ATOM   3443  C  C   . SER   B  2  198 ? 70.599  -72.715  14.647  1.00 126.73 ? 197 SER   B C   1 
ATOM   3444  O  O   . SER   B  2  198 ? 70.961  -71.840  15.454  1.00 127.69 ? 197 SER   B O   1 
ATOM   3445  C  CB  . SER   B  2  198 ? 72.463  -74.218  13.907  1.00 127.93 ? 197 SER   B CB  1 
ATOM   3446  O  OG  . SER   B  2  198 ? 73.496  -73.379  14.400  1.00 129.08 ? 197 SER   B OG  1 
ATOM   3447  N  N   . LYS   B  2  199 ? 69.706  -72.517  13.672  1.00 125.24 ? 198 LYS   B N   1 
ATOM   3448  C  CA  . LYS   B  2  199 ? 69.087  -71.201  13.361  1.00 128.83 ? 198 LYS   B CA  1 
ATOM   3449  C  C   . LYS   B  2  199 ? 67.806  -71.000  14.182  1.00 128.06 ? 198 LYS   B C   1 
ATOM   3450  O  O   . LYS   B  2  199 ? 67.500  -69.834  14.496  1.00 129.80 ? 198 LYS   B O   1 
ATOM   3451  C  CB  . LYS   B  2  199 ? 68.824  -71.088  11.857  1.00 132.90 ? 198 LYS   B CB  1 
ATOM   3452  C  CG  . LYS   B  2  199 ? 70.082  -70.972  11.006  1.00 138.12 ? 198 LYS   B CG  1 
ATOM   3453  C  CD  . LYS   B  2  199 ? 69.805  -70.822  9.530   1.00 142.50 ? 198 LYS   B CD  1 
ATOM   3454  C  CE  . LYS   B  2  199 ? 69.063  -69.545  9.203   1.00 144.92 ? 198 LYS   B CE  1 
ATOM   3455  N  NZ  . LYS   B  2  199 ? 68.921  -69.362  7.740   1.00 146.29 ? 198 LYS   B NZ  1 
ATOM   3456  N  N   . THR   B  2  200 ? 67.096  -72.081  14.524  1.00 123.55 ? 199 THR   B N   1 
ATOM   3457  C  CA  . THR   B  2  200 ? 65.791  -72.044  15.244  1.00 124.88 ? 199 THR   B CA  1 
ATOM   3458  C  C   . THR   B  2  200 ? 65.968  -72.297  16.747  1.00 123.44 ? 199 THR   B C   1 
ATOM   3459  O  O   . THR   B  2  200 ? 64.962  -72.181  17.470  1.00 122.47 ? 199 THR   B O   1 
ATOM   3460  C  CB  . THR   B  2  200 ? 64.803  -73.081  14.695  1.00 127.28 ? 199 THR   B CB  1 
ATOM   3461  O  OG1 . THR   B  2  200 ? 65.392  -74.378  14.808  1.00 127.46 ? 199 THR   B OG1 1 
ATOM   3462  C  CG2 . THR   B  2  200 ? 64.401  -72.803  13.263  1.00 130.86 ? 199 THR   B CG2 1 
ATOM   3463  N  N   . THR   B  2  201 ? 67.174  -72.651  17.202  1.00 122.74 ? 200 THR   B N   1 
ATOM   3464  C  CA  . THR   B  2  201 ? 67.470  -72.918  18.638  1.00 126.22 ? 200 THR   B CA  1 
ATOM   3465  C  C   . THR   B  2  201 ? 67.204  -71.656  19.468  1.00 127.33 ? 200 THR   B C   1 
ATOM   3466  O  O   . THR   B  2  201 ? 67.437  -70.547  18.949  1.00 130.52 ? 200 THR   B O   1 
ATOM   3467  C  CB  . THR   B  2  201 ? 68.908  -73.411  18.852  1.00 121.98 ? 200 THR   B CB  1 
ATOM   3468  O  OG1 . THR   B  2  201 ? 69.070  -73.730  20.234  1.00 119.16 ? 200 THR   B OG1 1 
ATOM   3469  C  CG2 . THR   B  2  201 ? 69.960  -72.400  18.451  1.00 126.43 ? 200 THR   B CG2 1 
ATOM   3470  N  N   . ASP   B  2  202 ? 66.736  -71.834  20.708  1.00 130.80 ? 201 ASP   B N   1 
ATOM   3471  C  CA  . ASP   B  2  202 ? 66.556  -70.751  21.714  1.00 133.80 ? 201 ASP   B CA  1 
ATOM   3472  C  C   . ASP   B  2  202 ? 67.824  -70.635  22.572  1.00 130.79 ? 201 ASP   B C   1 
ATOM   3473  O  O   . ASP   B  2  202 ? 67.841  -69.781  23.478  1.00 131.40 ? 201 ASP   B O   1 
ATOM   3474  C  CB  . ASP   B  2  202 ? 65.320  -70.999  22.585  1.00 138.71 ? 201 ASP   B CB  1 
ATOM   3475  C  CG  . ASP   B  2  202 ? 63.996  -70.901  21.843  1.00 141.48 ? 201 ASP   B CG  1 
ATOM   3476  O  OD1 . ASP   B  2  202 ? 63.955  -70.225  20.795  1.00 148.85 ? 201 ASP   B OD1 1 
ATOM   3477  O  OD2 . ASP   B  2  202 ? 63.010  -71.500  22.322  1.00 139.92 ? 201 ASP   B OD2 1 
ATOM   3478  N  N   . SER   B  2  203 ? 68.836  -71.471  22.305  1.00 134.51 ? 202 SER   B N   1 
ATOM   3479  C  CA  . SER   B  2  203 ? 70.163  -71.454  22.975  1.00 140.89 ? 202 SER   B CA  1 
ATOM   3480  C  C   . SER   B  2  203 ? 71.079  -70.443  22.283  1.00 138.59 ? 202 SER   B C   1 
ATOM   3481  O  O   . SER   B  2  203 ? 70.729  -69.980  21.181  1.00 135.67 ? 202 SER   B O   1 
ATOM   3482  C  CB  . SER   B  2  203 ? 70.790  -72.824  22.984  1.00 145.98 ? 202 SER   B CB  1 
ATOM   3483  O  OG  . SER   B  2  203 ? 69.993  -73.742  23.716  1.00 151.78 ? 202 SER   B OG  1 
ATOM   3484  N  N   . SER   B  2  204 ? 72.216  -70.133  22.909  1.00 142.60 ? 203 SER   B N   1 
ATOM   3485  C  CA  . SER   B  2  204 ? 73.247  -69.203  22.379  1.00 148.67 ? 203 SER   B CA  1 
ATOM   3486  C  C   . SER   B  2  204 ? 73.947  -69.840  21.172  1.00 153.83 ? 203 SER   B C   1 
ATOM   3487  O  O   . SER   B  2  204 ? 74.041  -69.168  20.127  1.00 165.29 ? 203 SER   B O   1 
ATOM   3488  C  CB  . SER   B  2  204 ? 74.231  -68.815  23.449  1.00 150.35 ? 203 SER   B CB  1 
ATOM   3489  O  OG  . SER   B  2  204 ? 74.843  -69.965  24.012  1.00 147.18 ? 203 SER   B OG  1 
ATOM   3490  N  N   . ALA   B  2  205 ? 74.409  -71.087  21.313  1.00 154.38 ? 204 ALA   B N   1 
ATOM   3491  C  CA  . ALA   B  2  205 ? 75.096  -71.862  20.252  1.00 155.01 ? 204 ALA   B CA  1 
ATOM   3492  C  C   . ALA   B  2  205 ? 74.796  -73.357  20.415  1.00 151.45 ? 204 ALA   B C   1 
ATOM   3493  O  O   . ALA   B  2  205 ? 74.751  -73.836  21.565  1.00 145.24 ? 204 ALA   B O   1 
ATOM   3494  C  CB  . ALA   B  2  205 ? 76.580  -71.589  20.292  1.00 157.35 ? 204 ALA   B CB  1 
ATOM   3495  N  N   . LEU   B  2  206 ? 74.608  -74.058  19.295  1.00 150.76 ? 205 LEU   B N   1 
ATOM   3496  C  CA  . LEU   B  2  206 ? 74.299  -75.512  19.252  1.00 148.59 ? 205 LEU   B CA  1 
ATOM   3497  C  C   . LEU   B  2  206 ? 75.596  -76.293  19.494  1.00 148.15 ? 205 LEU   B C   1 
ATOM   3498  O  O   . LEU   B  2  206 ? 76.572  -76.048  18.756  1.00 147.83 ? 205 LEU   B O   1 
ATOM   3499  C  CB  . LEU   B  2  206 ? 73.681  -75.850  17.891  1.00 147.80 ? 205 LEU   B CB  1 
ATOM   3500  C  CG  . LEU   B  2  206 ? 72.741  -77.053  17.868  1.00 147.64 ? 205 LEU   B CG  1 
ATOM   3501  C  CD1 . LEU   B  2  206 ? 71.457  -76.758  18.631  1.00 147.42 ? 205 LEU   B CD1 1 
ATOM   3502  C  CD2 . LEU   B  2  206 ? 72.425  -77.460  16.437  1.00 149.47 ? 205 LEU   B CD2 1 
ATOM   3503  N  N   . THR   B  2  207 ? 75.606  -77.175  20.500  1.00 144.00 ? 206 THR   B N   1 
ATOM   3504  C  CA  . THR   B  2  207 ? 76.772  -78.017  20.889  1.00 144.61 ? 206 THR   B CA  1 
ATOM   3505  C  C   . THR   B  2  207 ? 76.349  -79.488  20.972  1.00 143.42 ? 206 THR   B C   1 
ATOM   3506  O  O   . THR   B  2  207 ? 75.132  -79.751  21.044  1.00 148.58 ? 206 THR   B O   1 
ATOM   3507  C  CB  . THR   B  2  207 ? 77.392  -77.544  22.210  1.00 146.69 ? 206 THR   B CB  1 
ATOM   3508  O  OG1 . THR   B  2  207 ? 76.353  -77.453  23.186  1.00 144.28 ? 206 THR   B OG1 1 
ATOM   3509  C  CG2 . THR   B  2  207 ? 78.102  -76.214  22.078  1.00 148.53 ? 206 THR   B CG2 1 
ATOM   3510  N  N   . TYR   B  2  208 ? 77.332  -80.396  20.978  1.00 141.38 ? 207 TYR   B N   1 
ATOM   3511  C  CA  . TYR   B  2  208 ? 77.158  -81.873  20.900  1.00 138.28 ? 207 TYR   B CA  1 
ATOM   3512  C  C   . TYR   B  2  208 ? 76.315  -82.383  22.078  1.00 132.72 ? 207 TYR   B C   1 
ATOM   3513  O  O   . TYR   B  2  208 ? 75.536  -83.337  21.883  1.00 126.16 ? 207 TYR   B O   1 
ATOM   3514  C  CB  . TYR   B  2  208 ? 78.519  -82.576  20.849  1.00 140.76 ? 207 TYR   B CB  1 
ATOM   3515  C  CG  . TYR   B  2  208 ? 79.275  -82.621  22.155  1.00 140.51 ? 207 TYR   B CG  1 
ATOM   3516  C  CD1 . TYR   B  2  208 ? 80.124  -81.592  22.531  1.00 142.58 ? 207 TYR   B CD1 1 
ATOM   3517  C  CD2 . TYR   B  2  208 ? 79.149  -83.701  23.015  1.00 139.71 ? 207 TYR   B CD2 1 
ATOM   3518  C  CE1 . TYR   B  2  208 ? 80.822  -81.630  23.728  1.00 142.57 ? 207 TYR   B CE1 1 
ATOM   3519  C  CE2 . TYR   B  2  208 ? 79.839  -83.754  24.216  1.00 139.55 ? 207 TYR   B CE2 1 
ATOM   3520  C  CZ  . TYR   B  2  208 ? 80.680  -82.715  24.574  1.00 140.94 ? 207 TYR   B CZ  1 
ATOM   3521  O  OH  . TYR   B  2  208 ? 81.364  -82.761  25.754  1.00 139.89 ? 207 TYR   B OH  1 
ATOM   3522  N  N   . ASP   B  2  209 ? 76.467  -81.768  23.255  1.00 133.59 ? 208 ASP   B N   1 
ATOM   3523  C  CA  . ASP   B  2  209 ? 75.862  -82.241  24.531  1.00 133.41 ? 208 ASP   B CA  1 
ATOM   3524  C  C   . ASP   B  2  209 ? 74.356  -81.946  24.569  1.00 134.32 ? 208 ASP   B C   1 
ATOM   3525  O  O   . ASP   B  2  209 ? 73.677  -82.571  25.405  1.00 135.59 ? 208 ASP   B O   1 
ATOM   3526  C  CB  . ASP   B  2  209 ? 76.568  -81.642  25.752  1.00 136.79 ? 208 ASP   B CB  1 
ATOM   3527  C  CG  . ASP   B  2  209 ? 76.535  -80.123  25.815  1.00 140.98 ? 208 ASP   B CG  1 
ATOM   3528  O  OD1 . ASP   B  2  209 ? 76.968  -79.485  24.833  1.00 143.90 ? 208 ASP   B OD1 1 
ATOM   3529  O  OD2 . ASP   B  2  209 ? 76.076  -79.588  26.845  1.00 135.85 ? 208 ASP   B OD2 1 
ATOM   3530  N  N   . ARG   B  2  210 ? 73.848  -81.040  23.723  1.00 136.92 ? 209 ARG   B N   1 
ATOM   3531  C  CA  . ARG   B  2  210 ? 72.408  -80.654  23.709  1.00 137.37 ? 209 ARG   B CA  1 
ATOM   3532  C  C   . ARG   B  2  210 ? 71.674  -81.324  22.535  1.00 129.69 ? 209 ARG   B C   1 
ATOM   3533  O  O   . ARG   B  2  210 ? 70.496  -80.978  22.321  1.00 124.47 ? 209 ARG   B O   1 
ATOM   3534  C  CB  . ARG   B  2  210 ? 72.249  -79.128  23.661  1.00 142.14 ? 209 ARG   B CB  1 
ATOM   3535  C  CG  . ARG   B  2  210 ? 71.090  -78.609  24.504  1.00 145.28 ? 209 ARG   B CG  1 
ATOM   3536  C  CD  . ARG   B  2  210 ? 70.559  -77.244  24.098  1.00 149.70 ? 209 ARG   B CD  1 
ATOM   3537  N  NE  . ARG   B  2  210 ? 71.572  -76.382  23.501  1.00 153.87 ? 209 ARG   B NE  1 
ATOM   3538  C  CZ  . ARG   B  2  210 ? 72.544  -75.758  24.165  1.00 157.57 ? 209 ARG   B CZ  1 
ATOM   3539  N  NH1 . ARG   B  2  210 ? 72.665  -75.894  25.476  1.00 159.34 ? 209 ARG   B NH1 1 
ATOM   3540  N  NH2 . ARG   B  2  210 ? 73.403  -74.998  23.506  1.00 155.86 ? 209 ARG   B NH2 1 
ATOM   3541  N  N   . LEU   B  2  211 ? 72.309  -82.266  21.825  1.00 128.17 ? 210 LEU   B N   1 
ATOM   3542  C  CA  . LEU   B  2  211 ? 71.718  -82.917  20.623  1.00 130.25 ? 210 LEU   B CA  1 
ATOM   3543  C  C   . LEU   B  2  211 ? 71.669  -84.438  20.789  1.00 128.71 ? 210 LEU   B C   1 
ATOM   3544  O  O   . LEU   B  2  211 ? 72.624  -85.012  21.347  1.00 132.69 ? 210 LEU   B O   1 
ATOM   3545  C  CB  . LEU   B  2  211 ? 72.543  -82.567  19.381  1.00 132.35 ? 210 LEU   B CB  1 
ATOM   3546  C  CG  . LEU   B  2  211 ? 72.357  -81.158  18.824  1.00 134.96 ? 210 LEU   B CG  1 
ATOM   3547  C  CD1 . LEU   B  2  211 ? 73.300  -80.929  17.653  1.00 139.68 ? 210 LEU   B CD1 1 
ATOM   3548  C  CD2 . LEU   B  2  211 ? 70.916  -80.912  18.399  1.00 136.04 ? 210 LEU   B CD2 1 
ATOM   3549  N  N   . GLU   B  2  212 ? 70.585  -85.043  20.294  1.00 130.06 ? 211 GLU   B N   1 
ATOM   3550  C  CA  . GLU   B  2  212 ? 70.488  -86.481  19.932  1.00 128.72 ? 211 GLU   B CA  1 
ATOM   3551  C  C   . GLU   B  2  212 ? 70.381  -86.569  18.408  1.00 122.48 ? 211 GLU   B C   1 
ATOM   3552  O  O   . GLU   B  2  212 ? 69.735  -85.685  17.806  1.00 117.93 ? 211 GLU   B O   1 
ATOM   3553  C  CB  . GLU   B  2  212 ? 69.279  -87.147  20.588  1.00 129.87 ? 211 GLU   B CB  1 
ATOM   3554  C  CG  . GLU   B  2  212 ? 69.348  -87.183  22.104  1.00 135.33 ? 211 GLU   B CG  1 
ATOM   3555  C  CD  . GLU   B  2  212 ? 68.388  -88.161  22.762  1.00 133.68 ? 211 GLU   B CD  1 
ATOM   3556  O  OE1 . GLU   B  2  212 ? 67.699  -87.757  23.719  1.00 142.14 ? 211 GLU   B OE1 1 
ATOM   3557  O  OE2 . GLU   B  2  212 ? 68.334  -89.328  22.323  1.00 139.24 ? 211 GLU   B OE2 1 
ATOM   3558  N  N   . PHE   B  2  213 ? 70.989  -87.594  17.813  1.00 120.69 ? 212 PHE   B N   1 
ATOM   3559  C  CA  . PHE   B  2  213 ? 71.099  -87.758  16.342  1.00 120.28 ? 212 PHE   B CA  1 
ATOM   3560  C  C   . PHE   B  2  213 ? 70.998  -89.243  15.981  1.00 115.62 ? 212 PHE   B C   1 
ATOM   3561  O  O   . PHE   B  2  213 ? 71.530  -90.080  16.733  1.00 114.54 ? 212 PHE   B O   1 
ATOM   3562  C  CB  . PHE   B  2  213 ? 72.407  -87.135  15.854  1.00 124.55 ? 212 PHE   B CB  1 
ATOM   3563  C  CG  . PHE   B  2  213 ? 72.306  -86.511  14.488  1.00 130.16 ? 212 PHE   B CG  1 
ATOM   3564  C  CD1 . PHE   B  2  213 ? 71.747  -85.254  14.328  1.00 133.47 ? 212 PHE   B CD1 1 
ATOM   3565  C  CD2 . PHE   B  2  213 ? 72.752  -87.190  13.366  1.00 133.24 ? 212 PHE   B CD2 1 
ATOM   3566  C  CE1 . PHE   B  2  213 ? 71.647  -84.681  13.071  1.00 137.15 ? 212 PHE   B CE1 1 
ATOM   3567  C  CE2 . PHE   B  2  213 ? 72.651  -86.616  12.109  1.00 136.63 ? 212 PHE   B CE2 1 
ATOM   3568  C  CZ  . PHE   B  2  213 ? 72.097  -85.364  11.964  1.00 140.53 ? 212 PHE   B CZ  1 
ATOM   3569  N  N   . ALA   B  2  214 ? 70.326  -89.556  14.870  1.00 111.70 ? 213 ALA   B N   1 
ATOM   3570  C  CA  . ALA   B  2  214 ? 70.168  -90.937  14.358  1.00 111.03 ? 213 ALA   B CA  1 
ATOM   3571  C  C   . ALA   B  2  214 ? 69.917  -90.932  12.848  1.00 110.67 ? 213 ALA   B C   1 
ATOM   3572  O  O   . ALA   B  2  214 ? 69.222  -90.021  12.359  1.00 108.62 ? 213 ALA   B O   1 
ATOM   3573  C  CB  . ALA   B  2  214 ? 69.050  -91.639  15.085  1.00 109.83 ? 213 ALA   B CB  1 
ATOM   3574  N  N   . THR   B  2  215 ? 70.463  -91.935  12.155  1.00 111.75 ? 214 THR   B N   1 
ATOM   3575  C  CA  . THR   B  2  215 ? 70.249  -92.199  10.710  1.00 114.68 ? 214 THR   B CA  1 
ATOM   3576  C  C   . THR   B  2  215 ? 69.697  -93.616  10.530  1.00 114.29 ? 214 THR   B C   1 
ATOM   3577  O  O   . THR   B  2  215 ? 70.118  -94.520  11.280  1.00 111.73 ? 214 THR   B O   1 
ATOM   3578  C  CB  . THR   B  2  215 ? 71.539  -92.011  9.902   1.00 117.23 ? 214 THR   B CB  1 
ATOM   3579  O  OG1 . THR   B  2  215 ? 72.563  -92.825  10.475  1.00 118.33 ? 214 THR   B OG1 1 
ATOM   3580  C  CG2 . THR   B  2  215 ? 71.997  -90.570  9.858   1.00 120.09 ? 214 THR   B CG2 1 
ATOM   3581  N  N   . ILE   B  2  216 ? 68.780  -93.784  9.575   1.00 116.29 ? 215 ILE   B N   1 
ATOM   3582  C  CA  . ILE   B  2  216 ? 68.292  -95.108  9.092   1.00 119.58 ? 215 ILE   B CA  1 
ATOM   3583  C  C   . ILE   B  2  216 ? 68.675  -95.226  7.615   1.00 123.94 ? 215 ILE   B C   1 
ATOM   3584  O  O   . ILE   B  2  216 ? 67.944  -94.681  6.765   1.00 123.71 ? 215 ILE   B O   1 
ATOM   3585  C  CB  . ILE   B  2  216 ? 66.780  -95.268  9.336   1.00 120.81 ? 215 ILE   B CB  1 
ATOM   3586  C  CG1 . ILE   B  2  216 ? 66.469  -95.215  10.834  1.00 123.46 ? 215 ILE   B CG1 1 
ATOM   3587  C  CG2 . ILE   B  2  216 ? 66.261  -96.546  8.688   1.00 120.05 ? 215 ILE   B CG2 1 
ATOM   3588  C  CD1 . ILE   B  2  216 ? 64.998  -95.248  11.172  1.00 125.56 ? 215 ILE   B CD1 1 
ATOM   3589  N  N   . ARG   B  2  217 ? 69.798  -95.895  7.345   1.00 129.59 ? 216 ARG   B N   1 
ATOM   3590  C  CA  . ARG   B  2  217 ? 70.379  -96.074  5.990   1.00 135.58 ? 216 ARG   B CA  1 
ATOM   3591  C  C   . ARG   B  2  217 ? 70.141  -97.510  5.514   1.00 142.71 ? 216 ARG   B C   1 
ATOM   3592  O  O   . ARG   B  2  217 ? 69.827  -98.373  6.359   1.00 143.85 ? 216 ARG   B O   1 
ATOM   3593  C  CB  . ARG   B  2  217 ? 71.887  -95.806  6.015   1.00 134.55 ? 216 ARG   B CB  1 
ATOM   3594  C  CG  . ARG   B  2  217 ? 72.298  -94.371  6.306   1.00 135.56 ? 216 ARG   B CG  1 
ATOM   3595  C  CD  . ARG   B  2  217 ? 73.801  -94.322  6.508   1.00 139.99 ? 216 ARG   B CD  1 
ATOM   3596  N  NE  . ARG   B  2  217 ? 74.381  -93.002  6.303   1.00 143.65 ? 216 ARG   B NE  1 
ATOM   3597  C  CZ  . ARG   B  2  217 ? 74.871  -92.541  5.152   1.00 146.22 ? 216 ARG   B CZ  1 
ATOM   3598  N  NH1 . ARG   B  2  217 ? 74.854  -93.286  4.057   1.00 145.08 ? 216 ARG   B NH1 1 
ATOM   3599  N  NH2 . ARG   B  2  217 ? 75.379  -91.321  5.099   1.00 150.57 ? 216 ARG   B NH2 1 
ATOM   3600  N  N   . LYS   B  2  218 ? 70.297  -97.741  4.206   1.00 149.37 ? 217 LYS   B N   1 
ATOM   3601  C  CA  . LYS   B  2  218 ? 70.590  -99.071  3.604   1.00 155.47 ? 217 LYS   B CA  1 
ATOM   3602  C  C   . LYS   B  2  218 ? 72.113  -99.189  3.452   1.00 161.05 ? 217 LYS   B C   1 
ATOM   3603  O  O   . LYS   B  2  218 ? 72.572  -99.957  2.584   1.00 164.42 ? 217 LYS   B O   1 
ATOM   3604  C  CB  . LYS   B  2  218 ? 69.876  -99.228  2.257   1.00 156.00 ? 217 LYS   B CB  1 
ATOM   3605  C  CG  . LYS   B  2  218 ? 69.665  -100.664 1.796   1.00 155.90 ? 217 LYS   B CG  1 
ATOM   3606  C  CD  . LYS   B  2  218 ? 68.716  -100.783 0.627   1.00 158.37 ? 217 LYS   B CD  1 
ATOM   3607  C  CE  . LYS   B  2  218 ? 67.263  -100.655 1.031   1.00 157.60 ? 217 LYS   B CE  1 
ATOM   3608  N  NZ  . LYS   B  2  218 ? 66.381  -100.542 -0.154  1.00 157.16 ? 217 LYS   B NZ  1 
ATOM   3609  N  N   . GLY   B  2  219 ? 72.857  -98.462  4.295   1.00 167.37 ? 218 GLY   B N   1 
ATOM   3610  C  CA  . GLY   B  2  219 ? 74.326  -98.342  4.258   1.00 177.72 ? 218 GLY   B CA  1 
ATOM   3611  C  C   . GLY   B  2  219 ? 74.997  -99.458  5.038   1.00 186.05 ? 218 GLY   B C   1 
ATOM   3612  O  O   . GLY   B  2  219 ? 76.181  -99.297  5.397   1.00 189.17 ? 218 GLY   B O   1 
ATOM   3613  N  N   . ALA   B  2  220 ? 74.260  -100.541 5.311   1.00 190.64 ? 219 ALA   B N   1 
ATOM   3614  C  CA  . ALA   B  2  220 ? 74.796  -101.859 5.722   1.00 191.49 ? 219 ALA   B CA  1 
ATOM   3615  C  C   . ALA   B  2  220 ? 75.390  -102.537 4.479   1.00 199.18 ? 219 ALA   B C   1 
ATOM   3616  O  O   . ALA   B  2  220 ? 75.776  -101.805 3.542   1.00 196.58 ? 219 ALA   B O   1 
ATOM   3617  C  CB  . ALA   B  2  220 ? 73.703  -102.678 6.369   1.00 186.23 ? 219 ALA   B CB  1 
ATOM   3618  N  N   . ASN   B  2  221 ? 75.468  -103.872 4.459   1.00 197.19 ? 220 ASN   B N   1 
ATOM   3619  C  CA  . ASN   B  2  221 ? 76.061  -104.649 3.337   1.00 194.73 ? 220 ASN   B CA  1 
ATOM   3620  C  C   . ASN   B  2  221 ? 74.950  -105.387 2.579   1.00 184.10 ? 220 ASN   B C   1 
ATOM   3621  O  O   . ASN   B  2  221 ? 74.583  -106.502 3.001   1.00 179.34 ? 220 ASN   B O   1 
ATOM   3622  C  CB  . ASN   B  2  221 ? 77.171  -105.579 3.835   1.00 204.46 ? 220 ASN   B CB  1 
ATOM   3623  C  CG  . ASN   B  2  221 ? 78.339  -104.821 4.434   1.00 207.77 ? 220 ASN   B CG  1 
ATOM   3624  O  OD1 . ASN   B  2  221 ? 78.147  -103.920 5.249   1.00 212.09 ? 220 ASN   B OD1 1 
ATOM   3625  N  ND2 . ASN   B  2  221 ? 79.553  -105.171 4.040   1.00 214.37 ? 220 ASN   B ND2 1 
ATOM   3626  N  N   . ASP   B  2  222 ? 74.439  -104.761 1.510   1.00 171.18 ? 221 ASP   B N   1 
ATOM   3627  C  CA  . ASP   B  2  222 ? 73.522  -105.342 0.488   1.00 169.22 ? 221 ASP   B CA  1 
ATOM   3628  C  C   . ASP   B  2  222 ? 72.094  -105.467 1.037   1.00 161.86 ? 221 ASP   B C   1 
ATOM   3629  O  O   . ASP   B  2  222 ? 71.875  -106.284 1.953   1.00 165.02 ? 221 ASP   B O   1 
ATOM   3630  C  CB  . ASP   B  2  222 ? 74.036  -106.686 -0.043  1.00 167.53 ? 221 ASP   B CB  1 
ATOM   3631  C  CG  . ASP   B  2  222 ? 74.943  -106.556 -1.255  1.00 171.66 ? 221 ASP   B CG  1 
ATOM   3632  O  OD1 . ASP   B  2  222 ? 75.753  -105.606 -1.282  1.00 171.16 ? 221 ASP   B OD1 1 
ATOM   3633  O  OD2 . ASP   B  2  222 ? 74.826  -107.401 -2.166  1.00 167.82 ? 221 ASP   B OD2 1 
ATOM   3634  N  N   . GLY   B  2  223 ? 71.173  -104.667 0.485   1.00 156.79 ? 222 GLY   B N   1 
ATOM   3635  C  CA  . GLY   B  2  223 ? 69.706  -104.844 0.544   1.00 153.53 ? 222 GLY   B CA  1 
ATOM   3636  C  C   . GLY   B  2  223 ? 69.152  -105.043 1.947   1.00 151.94 ? 222 GLY   B C   1 
ATOM   3637  O  O   . GLY   B  2  223 ? 68.097  -105.700 2.059   1.00 151.97 ? 222 GLY   B O   1 
ATOM   3638  N  N   . GLU   B  2  224 ? 69.806  -104.495 2.977   1.00 149.68 ? 223 GLU   B N   1 
ATOM   3639  C  CA  . GLU   B  2  224 ? 69.333  -104.561 4.388   1.00 147.08 ? 223 GLU   B CA  1 
ATOM   3640  C  C   . GLU   B  2  224 ? 69.596  -103.218 5.079   1.00 141.86 ? 223 GLU   B C   1 
ATOM   3641  O  O   . GLU   B  2  224 ? 70.535  -102.503 4.669   1.00 137.68 ? 223 GLU   B O   1 
ATOM   3642  C  CB  . GLU   B  2  224 ? 69.989  -105.730 5.127   1.00 149.78 ? 223 GLU   B CB  1 
ATOM   3643  C  CG  . GLU   B  2  224 ? 71.449  -105.501 5.472   1.00 152.17 ? 223 GLU   B CG  1 
ATOM   3644  C  CD  . GLU   B  2  224 ? 72.228  -106.768 5.780   1.00 155.93 ? 223 GLU   B CD  1 
ATOM   3645  O  OE1 . GLU   B  2  224 ? 71.589  -107.813 6.024   1.00 157.15 ? 223 GLU   B OE1 1 
ATOM   3646  O  OE2 . GLU   B  2  224 ? 73.472  -106.705 5.773   1.00 161.53 ? 223 GLU   B OE2 1 
ATOM   3647  N  N   . VAL   B  2  225 ? 68.792  -102.908 6.098   1.00 132.59 ? 224 VAL   B N   1 
ATOM   3648  C  CA  . VAL   B  2  225 ? 68.696  -101.561 6.732   1.00 127.46 ? 224 VAL   B CA  1 
ATOM   3649  C  C   . VAL   B  2  225 ? 69.399  -101.591 8.091   1.00 125.14 ? 224 VAL   B C   1 
ATOM   3650  O  O   . VAL   B  2  225 ? 69.220  -102.575 8.831   1.00 122.40 ? 224 VAL   B O   1 
ATOM   3651  C  CB  . VAL   B  2  225 ? 67.225  -101.121 6.851   1.00 128.36 ? 224 VAL   B CB  1 
ATOM   3652  C  CG1 . VAL   B  2  225 ? 67.025  -100.011 7.873   1.00 128.14 ? 224 VAL   B CG1 1 
ATOM   3653  C  CG2 . VAL   B  2  225 ? 66.674  -100.706 5.496   1.00 128.71 ? 224 VAL   B CG2 1 
ATOM   3654  N  N   . TYR   B  2  226 ? 70.156  -100.533 8.394   1.00 123.59 ? 225 TYR   B N   1 
ATOM   3655  C  CA  . TYR   B  2  226 ? 70.915  -100.350 9.657   1.00 125.96 ? 225 TYR   B CA  1 
ATOM   3656  C  C   . TYR   B  2  226 ? 70.419  -99.080  10.359  1.00 118.99 ? 225 TYR   B C   1 
ATOM   3657  O  O   . TYR   B  2  226 ? 70.271  -98.037  9.695   1.00 116.51 ? 225 TYR   B O   1 
ATOM   3658  C  CB  . TYR   B  2  226 ? 72.418  -100.314 9.366   1.00 134.76 ? 225 TYR   B CB  1 
ATOM   3659  C  CG  . TYR   B  2  226 ? 73.297  -100.095 10.573  1.00 143.62 ? 225 TYR   B CG  1 
ATOM   3660  C  CD1 . TYR   B  2  226 ? 73.206  -100.921 11.684  1.00 145.32 ? 225 TYR   B CD1 1 
ATOM   3661  C  CD2 . TYR   B  2  226 ? 74.234  -99.073  10.602  1.00 142.44 ? 225 TYR   B CD2 1 
ATOM   3662  C  CE1 . TYR   B  2  226 ? 74.011  -100.729 12.796  1.00 148.50 ? 225 TYR   B CE1 1 
ATOM   3663  C  CE2 . TYR   B  2  226 ? 75.047  -98.868  11.705  1.00 145.84 ? 225 TYR   B CE2 1 
ATOM   3664  C  CZ  . TYR   B  2  226 ? 74.935  -99.698  12.806  1.00 146.27 ? 225 TYR   B CZ  1 
ATOM   3665  O  OH  . TYR   B  2  226 ? 75.735  -99.500  13.893  1.00 149.80 ? 225 TYR   B OH  1 
ATOM   3666  N  N   . GLN   B  2  227 ? 70.148  -99.190  11.662  1.00 115.40 ? 226 GLN   B N   1 
ATOM   3667  C  CA  . GLN   B  2  227 ? 69.801  -98.059  12.562  1.00 117.75 ? 226 GLN   B CA  1 
ATOM   3668  C  C   . GLN   B  2  227 ? 71.058  -97.626  13.318  1.00 118.77 ? 226 GLN   B C   1 
ATOM   3669  O  O   . GLN   B  2  227 ? 71.655  -98.478  14.003  1.00 126.10 ? 226 GLN   B O   1 
ATOM   3670  C  CB  . GLN   B  2  227 ? 68.727  -98.471  13.566  1.00 113.69 ? 226 GLN   B CB  1 
ATOM   3671  C  CG  . GLN   B  2  227 ? 67.311  -98.227  13.079  1.00 111.67 ? 226 GLN   B CG  1 
ATOM   3672  C  CD  . GLN   B  2  227 ? 66.311  -98.688  14.108  1.00 111.15 ? 226 GLN   B CD  1 
ATOM   3673  O  OE1 . GLN   B  2  227 ? 66.504  -99.701  14.774  1.00 115.54 ? 226 GLN   B OE1 1 
ATOM   3674  N  NE2 . GLN   B  2  227 ? 65.233  -97.939  14.257  1.00 109.13 ? 226 GLN   B NE2 1 
ATOM   3675  N  N   . LYS   B  2  228 ? 71.430  -96.350  13.203  1.00 118.18 ? 227 LYS   B N   1 
ATOM   3676  C  CA  . LYS   B  2  228 ? 72.608  -95.761  13.888  1.00 117.79 ? 227 LYS   B CA  1 
ATOM   3677  C  C   . LYS   B  2  228 ? 72.114  -94.661  14.831  1.00 116.94 ? 227 LYS   B C   1 
ATOM   3678  O  O   . LYS   B  2  228 ? 71.732  -93.592  14.329  1.00 118.88 ? 227 LYS   B O   1 
ATOM   3679  C  CB  . LYS   B  2  228 ? 73.600  -95.228  12.849  1.00 119.32 ? 227 LYS   B CB  1 
ATOM   3680  C  CG  . LYS   B  2  228 ? 75.031  -95.050  13.341  1.00 121.80 ? 227 LYS   B CG  1 
ATOM   3681  C  CD  . LYS   B  2  228 ? 75.944  -94.439  12.297  1.00 122.65 ? 227 LYS   B CD  1 
ATOM   3682  C  CE  . LYS   B  2  228 ? 77.408  -94.744  12.528  1.00 124.85 ? 227 LYS   B CE  1 
ATOM   3683  N  NZ  . LYS   B  2  228 ? 77.918  -94.093  13.758  1.00 125.90 ? 227 LYS   B NZ  1 
ATOM   3684  N  N   . ILE   B  2  229 ? 72.083  -94.940  16.138  1.00 116.17 ? 228 ILE   B N   1 
ATOM   3685  C  CA  . ILE   B  2  229 ? 71.857  -93.923  17.210  1.00 115.11 ? 228 ILE   B CA  1 
ATOM   3686  C  C   . ILE   B  2  229 ? 73.232  -93.353  17.578  1.00 115.96 ? 228 ILE   B C   1 
ATOM   3687  O  O   . ILE   B  2  229 ? 74.027  -94.086  18.197  1.00 112.97 ? 228 ILE   B O   1 
ATOM   3688  C  CB  . ILE   B  2  229 ? 71.132  -94.519  18.436  1.00 114.30 ? 228 ILE   B CB  1 
ATOM   3689  C  CG1 . ILE   B  2  229 ? 69.921  -95.378  18.053  1.00 112.58 ? 228 ILE   B CG1 1 
ATOM   3690  C  CG2 . ILE   B  2  229 ? 70.752  -93.417  19.415  1.00 113.99 ? 228 ILE   B CG2 1 
ATOM   3691  C  CD1 . ILE   B  2  229 ? 68.803  -94.625  17.364  1.00 110.24 ? 228 ILE   B CD1 1 
ATOM   3692  N  N   . PHE   B  2  230 ? 73.501  -92.102  17.197  1.00 116.21 ? 229 PHE   B N   1 
ATOM   3693  C  CA  . PHE   B  2  230 ? 74.846  -91.470  17.258  1.00 120.91 ? 229 PHE   B CA  1 
ATOM   3694  C  C   . PHE   B  2  230 ? 75.307  -91.348  18.715  1.00 121.16 ? 229 PHE   B C   1 
ATOM   3695  O  O   . PHE   B  2  230 ? 74.513  -90.909  19.574  1.00 113.37 ? 229 PHE   B O   1 
ATOM   3696  C  CB  . PHE   B  2  230 ? 74.842  -90.098  16.579  1.00 121.11 ? 229 PHE   B CB  1 
ATOM   3697  C  CG  . PHE   B  2  230 ? 74.965  -90.135  15.076  1.00 123.06 ? 229 PHE   B CG  1 
ATOM   3698  C  CD1 . PHE   B  2  230 ? 74.012  -90.775  14.299  1.00 120.53 ? 229 PHE   B CD1 1 
ATOM   3699  C  CD2 . PHE   B  2  230 ? 76.030  -89.517  14.438  1.00 126.62 ? 229 PHE   B CD2 1 
ATOM   3700  C  CE1 . PHE   B  2  230 ? 74.128  -90.804  12.917  1.00 121.57 ? 229 PHE   B CE1 1 
ATOM   3701  C  CE2 . PHE   B  2  230 ? 76.143  -89.545  13.056  1.00 126.54 ? 229 PHE   B CE2 1 
ATOM   3702  C  CZ  . PHE   B  2  230 ? 75.192  -90.189  12.298  1.00 124.52 ? 229 PHE   B CZ  1 
ATOM   3703  N  N   . LYS   B  2  231 ? 76.562  -91.729  18.972  1.00 127.52 ? 230 LYS   B N   1 
ATOM   3704  C  CA  . LYS   B  2  231 ? 77.249  -91.552  20.278  1.00 133.00 ? 230 LYS   B CA  1 
ATOM   3705  C  C   . LYS   B  2  231 ? 77.657  -90.087  20.415  1.00 133.97 ? 230 LYS   B C   1 
ATOM   3706  O  O   . LYS   B  2  231 ? 77.825  -89.399  19.410  1.00 134.09 ? 230 LYS   B O   1 
ATOM   3707  C  CB  . LYS   B  2  231 ? 78.480  -92.460  20.376  1.00 134.43 ? 230 LYS   B CB  1 
ATOM   3708  C  CG  . LYS   B  2  231 ? 78.207  -93.952  20.249  1.00 134.49 ? 230 LYS   B CG  1 
ATOM   3709  C  CD  . LYS   B  2  231 ? 79.471  -94.786  20.247  1.00 137.14 ? 230 LYS   B CD  1 
ATOM   3710  C  CE  . LYS   B  2  231 ? 79.231  -96.241  19.904  1.00 139.46 ? 230 LYS   B CE  1 
ATOM   3711  N  NZ  . LYS   B  2  231 ? 78.477  -96.943  20.970  1.00 141.56 ? 230 LYS   B NZ  1 
ATOM   3712  N  N   . PRO   B  2  232 ? 77.827  -89.568  21.653  1.00 138.63 ? 231 PRO   B N   1 
ATOM   3713  C  CA  . PRO   B  2  232 ? 78.234  -88.177  21.867  1.00 140.48 ? 231 PRO   B CA  1 
ATOM   3714  C  C   . PRO   B  2  232 ? 79.391  -87.698  20.976  1.00 146.20 ? 231 PRO   B C   1 
ATOM   3715  O  O   . PRO   B  2  232 ? 79.272  -86.630  20.400  1.00 152.35 ? 231 PRO   B O   1 
ATOM   3716  C  CB  . PRO   B  2  232 ? 78.678  -88.185  23.336  1.00 140.29 ? 231 PRO   B CB  1 
ATOM   3717  C  CG  . PRO   B  2  232 ? 77.786  -89.221  23.977  1.00 138.17 ? 231 PRO   B CG  1 
ATOM   3718  C  CD  . PRO   B  2  232 ? 77.613  -90.290  22.918  1.00 136.44 ? 231 PRO   B CD  1 
ATOM   3719  N  N   . GLN   B  2  233 ? 80.467  -88.490  20.890  1.00 148.05 ? 232 GLN   B N   1 
ATOM   3720  C  CA  . GLN   B  2  233 ? 81.707  -88.165  20.130  1.00 148.44 ? 232 GLN   B CA  1 
ATOM   3721  C  C   . GLN   B  2  233 ? 81.404  -88.103  18.628  1.00 148.79 ? 232 GLN   B C   1 
ATOM   3722  O  O   . GLN   B  2  233 ? 82.075  -87.319  17.927  1.00 149.29 ? 232 GLN   B O   1 
ATOM   3723  C  CB  . GLN   B  2  233 ? 82.798  -89.199  20.424  1.00 150.60 ? 232 GLN   B CB  1 
ATOM   3724  C  CG  . GLN   B  2  233 ? 84.095  -88.973  19.655  1.00 154.55 ? 232 GLN   B CG  1 
ATOM   3725  C  CD  . GLN   B  2  233 ? 84.695  -87.607  19.883  1.00 155.71 ? 232 GLN   B CD  1 
ATOM   3726  O  OE1 . GLN   B  2  233 ? 84.909  -86.841  18.947  1.00 159.20 ? 232 GLN   B OE1 1 
ATOM   3727  N  NE2 . GLN   B  2  233 ? 84.974  -87.288  21.138  1.00 157.94 ? 232 GLN   B NE2 1 
ATOM   3728  N  N   . GLU   B  2  234 ? 80.441  -88.901  18.154  1.00 144.68 ? 233 GLU   B N   1 
ATOM   3729  C  CA  . GLU   B  2  234 ? 80.036  -88.963  16.723  1.00 144.87 ? 233 GLU   B CA  1 
ATOM   3730  C  C   . GLU   B  2  234 ? 79.247  -87.697  16.357  1.00 146.92 ? 233 GLU   B C   1 
ATOM   3731  O  O   . GLU   B  2  234 ? 79.379  -87.242  15.203  1.00 151.61 ? 233 GLU   B O   1 
ATOM   3732  C  CB  . GLU   B  2  234 ? 79.227  -90.230  16.446  1.00 140.28 ? 233 GLU   B CB  1 
ATOM   3733  C  CG  . GLU   B  2  234 ? 79.987  -91.507  16.758  1.00 141.08 ? 233 GLU   B CG  1 
ATOM   3734  C  CD  . GLU   B  2  234 ? 79.235  -92.792  16.456  1.00 139.96 ? 233 GLU   B CD  1 
ATOM   3735  O  OE1 . GLU   B  2  234 ? 78.017  -92.842  16.719  1.00 144.27 ? 233 GLU   B OE1 1 
ATOM   3736  O  OE2 . GLU   B  2  234 ? 79.872  -93.742  15.959  1.00 137.85 ? 233 GLU   B OE2 1 
ATOM   3737  N  N   . ILE   B  2  235 ? 78.468  -87.152  17.300  1.00 145.90 ? 234 ILE   B N   1 
ATOM   3738  C  CA  . ILE   B  2  235 ? 77.713  -85.872  17.131  1.00 144.37 ? 234 ILE   B CA  1 
ATOM   3739  C  C   . ILE   B  2  235 ? 78.722  -84.717  17.150  1.00 145.62 ? 234 ILE   B C   1 
ATOM   3740  O  O   . ILE   B  2  235 ? 78.568  -83.791  16.337  1.00 145.26 ? 234 ILE   B O   1 
ATOM   3741  C  CB  . ILE   B  2  235 ? 76.612  -85.696  18.200  1.00 142.25 ? 234 ILE   B CB  1 
ATOM   3742  C  CG1 . ILE   B  2  235 ? 75.616  -86.862  18.195  1.00 140.48 ? 234 ILE   B CG1 1 
ATOM   3743  C  CG2 . ILE   B  2  235 ? 75.900  -84.361  18.026  1.00 139.57 ? 234 ILE   B CG2 1 
ATOM   3744  C  CD1 . ILE   B  2  235 ? 74.736  -86.936  19.424  1.00 139.67 ? 234 ILE   B CD1 1 
ATOM   3745  N  N   . LYS   B  2  236 ? 79.715  -84.779  18.044  1.00 147.01 ? 235 LYS   B N   1 
ATOM   3746  C  CA  . LYS   B  2  236 ? 80.812  -83.777  18.151  1.00 151.07 ? 235 LYS   B CA  1 
ATOM   3747  C  C   . LYS   B  2  236 ? 81.555  -83.693  16.811  1.00 154.37 ? 235 LYS   B C   1 
ATOM   3748  O  O   . LYS   B  2  236 ? 81.866  -82.564  16.384  1.00 152.94 ? 235 LYS   B O   1 
ATOM   3749  C  CB  . LYS   B  2  236 ? 81.769  -84.143  19.291  1.00 154.61 ? 235 LYS   B CB  1 
ATOM   3750  C  CG  . LYS   B  2  236 ? 82.786  -83.069  19.655  1.00 158.55 ? 235 LYS   B CG  1 
ATOM   3751  C  CD  . LYS   B  2  236 ? 83.974  -83.597  20.433  1.00 162.75 ? 235 LYS   B CD  1 
ATOM   3752  C  CE  . LYS   B  2  236 ? 85.029  -82.544  20.703  1.00 163.79 ? 235 LYS   B CE  1 
ATOM   3753  N  NZ  . LYS   B  2  236 ? 84.630  -81.631  21.800  1.00 162.76 ? 235 LYS   B NZ  1 
ATOM   3754  N  N   . ASP   B  2  237 ? 81.814  -84.841  16.173  1.00 154.09 ? 236 ASP   B N   1 
ATOM   3755  C  CA  . ASP   B  2  237 ? 82.564  -84.948  14.890  1.00 155.00 ? 236 ASP   B CA  1 
ATOM   3756  C  C   . ASP   B  2  237 ? 81.709  -84.409  13.735  1.00 157.64 ? 236 ASP   B C   1 
ATOM   3757  O  O   . ASP   B  2  237 ? 82.257  -83.638  12.922  1.00 158.79 ? 236 ASP   B O   1 
ATOM   3758  C  CB  . ASP   B  2  237 ? 83.014  -86.386  14.614  1.00 150.44 ? 236 ASP   B CB  1 
ATOM   3759  C  CG  . ASP   B  2  237 ? 84.136  -86.873  15.517  1.00 147.43 ? 236 ASP   B CG  1 
ATOM   3760  O  OD1 . ASP   B  2  237 ? 84.884  -86.023  16.038  1.00 148.09 ? 236 ASP   B OD1 1 
ATOM   3761  O  OD2 . ASP   B  2  237 ? 84.252  -88.101  15.692  1.00 144.13 ? 236 ASP   B OD2 1 
ATOM   3762  N  N   . ILE   B  2  238 ? 80.429  -84.798  13.661  1.00 161.97 ? 237 ILE   B N   1 
ATOM   3763  C  CA  . ILE   B  2  238 ? 79.497  -84.409  12.554  1.00 162.70 ? 237 ILE   B CA  1 
ATOM   3764  C  C   . ILE   B  2  238 ? 79.187  -82.908  12.652  1.00 162.07 ? 237 ILE   B C   1 
ATOM   3765  O  O   . ILE   B  2  238 ? 78.852  -82.309  11.608  1.00 158.29 ? 237 ILE   B O   1 
ATOM   3766  C  CB  . ILE   B  2  238 ? 78.212  -85.268  12.556  1.00 165.37 ? 237 ILE   B CB  1 
ATOM   3767  C  CG1 . ILE   B  2  238 ? 77.587  -85.356  11.160  1.00 170.69 ? 237 ILE   B CG1 1 
ATOM   3768  C  CG2 . ILE   B  2  238 ? 77.205  -84.779  13.588  1.00 164.44 ? 237 ILE   B CG2 1 
ATOM   3769  C  CD1 . ILE   B  2  238 ? 78.174  -86.444  10.290  1.00 172.02 ? 237 ILE   B CD1 1 
ATOM   3770  N  N   . LEU   B  2  239 ? 79.286  -82.328  13.854  1.00 156.14 ? 238 LEU   B N   1 
ATOM   3771  C  CA  . LEU   B  2  239 ? 79.042  -80.882  14.114  1.00 156.10 ? 238 LEU   B CA  1 
ATOM   3772  C  C   . LEU   B  2  239 ? 80.252  -80.073  13.625  1.00 157.85 ? 238 LEU   B C   1 
ATOM   3773  O  O   . LEU   B  2  239 ? 80.044  -78.941  13.146  1.00 159.27 ? 238 LEU   B O   1 
ATOM   3774  C  CB  . LEU   B  2  239 ? 78.782  -80.674  15.613  1.00 149.79 ? 238 LEU   B CB  1 
ATOM   3775  C  CG  . LEU   B  2  239 ? 77.700  -79.659  15.985  1.00 146.54 ? 238 LEU   B CG  1 
ATOM   3776  C  CD1 . LEU   B  2  239 ? 76.362  -79.996  15.339  1.00 142.84 ? 238 LEU   B CD1 1 
ATOM   3777  C  CD2 . LEU   B  2  239 ? 77.542  -79.581  17.496  1.00 143.80 ? 238 LEU   B CD2 1 
ATOM   3778  N  N   . VAL   B  2  240 ? 81.462  -80.637  13.734  1.00 160.95 ? 239 VAL   B N   1 
ATOM   3779  C  CA  . VAL   B  2  240 ? 82.732  -80.038  13.219  1.00 163.04 ? 239 VAL   B CA  1 
ATOM   3780  C  C   . VAL   B  2  240 ? 82.783  -80.198  11.694  1.00 164.12 ? 239 VAL   B C   1 
ATOM   3781  O  O   . VAL   B  2  240 ? 83.184  -79.229  11.018  1.00 164.82 ? 239 VAL   B O   1 
ATOM   3782  C  CB  . VAL   B  2  240 ? 83.974  -80.665  13.887  1.00 164.84 ? 239 VAL   B CB  1 
ATOM   3783  C  CG1 . VAL   B  2  240 ? 85.255  -80.372  13.116  1.00 165.86 ? 239 VAL   B CG1 1 
ATOM   3784  C  CG2 . VAL   B  2  240 ? 84.115  -80.221  15.334  1.00 165.16 ? 239 VAL   B CG2 1 
ATOM   3785  N  N   . LYS   B  2  241 ? 82.402  -81.374  11.181  1.00 163.63 ? 240 LYS   B N   1 
ATOM   3786  C  CA  . LYS   B  2  241 ? 82.489  -81.736  9.738   1.00 163.16 ? 240 LYS   B CA  1 
ATOM   3787  C  C   . LYS   B  2  241 ? 81.669  -80.744  8.899   1.00 158.97 ? 240 LYS   B C   1 
ATOM   3788  O  O   . LYS   B  2  241 ? 82.120  -80.417  7.783   1.00 155.25 ? 240 LYS   B O   1 
ATOM   3789  C  CB  . LYS   B  2  241 ? 82.030  -83.182  9.509   1.00 163.18 ? 240 LYS   B CB  1 
ATOM   3790  C  CG  . LYS   B  2  241 ? 82.523  -83.820  8.215   1.00 163.97 ? 240 LYS   B CG  1 
ATOM   3791  C  CD  . LYS   B  2  241 ? 82.397  -85.332  8.186   1.00 162.26 ? 240 LYS   B CD  1 
ATOM   3792  C  CE  . LYS   B  2  241 ? 80.970  -85.817  8.042   1.00 159.70 ? 240 LYS   B CE  1 
ATOM   3793  N  NZ  . LYS   B  2  241 ? 80.460  -85.630  6.663   1.00 161.54 ? 240 LYS   B NZ  1 
ATOM   3794  N  N   . THR   B  2  242 ? 80.523  -80.278  9.415   1.00 156.93 ? 241 THR   B N   1 
ATOM   3795  C  CA  . THR   B  2  242 ? 79.621  -79.302  8.739   1.00 155.11 ? 241 THR   B CA  1 
ATOM   3796  C  C   . THR   B  2  242 ? 79.963  -77.867  9.171   1.00 155.93 ? 241 THR   B C   1 
ATOM   3797  O  O   . THR   B  2  242 ? 79.316  -76.935  8.654   1.00 155.58 ? 241 THR   B O   1 
ATOM   3798  C  CB  . THR   B  2  242 ? 78.144  -79.637  8.989   1.00 151.29 ? 241 THR   B CB  1 
ATOM   3799  O  OG1 . THR   B  2  242 ? 77.899  -79.613  10.395  1.00 149.31 ? 241 THR   B OG1 1 
ATOM   3800  C  CG2 . THR   B  2  242 ? 77.746  -80.985  8.426   1.00 148.51 ? 241 THR   B CG2 1 
ATOM   3801  N  N   . GLY   B  2  243 ? 80.931  -77.699  10.079  1.00 157.77 ? 242 GLY   B N   1 
ATOM   3802  C  CA  . GLY   B  2  243 ? 81.528  -76.398  10.443  1.00 160.29 ? 242 GLY   B CA  1 
ATOM   3803  C  C   . GLY   B  2  243 ? 80.591  -75.512  11.250  1.00 159.73 ? 242 GLY   B C   1 
ATOM   3804  O  O   . GLY   B  2  243 ? 80.674  -74.278  11.084  1.00 159.91 ? 242 GLY   B O   1 
ATOM   3805  N  N   . ILE   B  2  244 ? 79.739  -76.103  12.097  1.00 156.76 ? 243 ILE   B N   1 
ATOM   3806  C  CA  . ILE   B  2  244 ? 78.856  -75.366  13.054  1.00 153.86 ? 243 ILE   B CA  1 
ATOM   3807  C  C   . ILE   B  2  244 ? 79.672  -75.007  14.306  1.00 156.23 ? 243 ILE   B C   1 
ATOM   3808  O  O   . ILE   B  2  244 ? 79.365  -73.964  14.917  1.00 163.81 ? 243 ILE   B O   1 
ATOM   3809  C  CB  . ILE   B  2  244 ? 77.575  -76.170  13.378  1.00 147.66 ? 243 ILE   B CB  1 
ATOM   3810  C  CG1 . ILE   B  2  244 ? 76.655  -76.252  12.154  1.00 144.80 ? 243 ILE   B CG1 1 
ATOM   3811  C  CG2 . ILE   B  2  244 ? 76.847  -75.589  14.585  1.00 144.74 ? 243 ILE   B CG2 1 
ATOM   3812  C  CD1 . ILE   B  2  244 ? 75.466  -77.171  12.318  1.00 142.53 ? 243 ILE   B CD1 1 
ATOM   3813  N  N   . THR   B  2  245 ? 80.671  -75.825  14.666  1.00 158.48 ? 244 THR   B N   1 
ATOM   3814  C  CA  . THR   B  2  245 ? 81.627  -75.568  15.781  1.00 155.90 ? 244 THR   B CA  1 
ATOM   3815  C  C   . THR   B  2  245 ? 83.066  -75.821  15.312  1.00 157.48 ? 244 THR   B C   1 
ATOM   3816  O  O   . THR   B  2  245 ? 83.363  -76.753  14.566  1.00 154.07 ? 244 THR   B O   1 
ATOM   3817  C  CB  . THR   B  2  245 ? 81.284  -76.410  17.016  1.00 156.21 ? 244 THR   B CB  1 
ATOM   3818  O  OG1 . THR   B  2  245 ? 81.036  -77.752  16.595  1.00 153.42 ? 244 THR   B OG1 1 
ATOM   3819  C  CG2 . THR   B  2  245 ? 80.085  -75.876  17.770  1.00 151.88 ? 244 THR   B CG2 1 
ATOM   3820  N  N   . GLY   C  3  3   ? 34.015  -97.603  34.812  1.00 108.50 ? 1   GLY   C N   1 
ATOM   3821  C  CA  . GLY   C  3  3   ? 33.992  -96.960  33.469  1.00 107.15 ? 1   GLY   C CA  1 
ATOM   3822  C  C   . GLY   C  3  3   ? 33.531  -95.514  33.552  1.00 105.47 ? 1   GLY   C C   1 
ATOM   3823  O  O   . GLY   C  3  3   ? 32.679  -95.217  34.415  1.00 106.95 ? 1   GLY   C O   1 
ATOM   3824  N  N   . TYR   C  3  4   ? 34.074  -94.641  32.696  1.00 100.74 ? 2   TYR   C N   1 
ATOM   3825  C  CA  . TYR   C  3  4   ? 33.657  -93.220  32.571  1.00 99.69  ? 2   TYR   C CA  1 
ATOM   3826  C  C   . TYR   C  3  4   ? 32.231  -93.183  32.008  1.00 96.64  ? 2   TYR   C C   1 
ATOM   3827  O  O   . TYR   C  3  4   ? 31.991  -93.778  30.942  1.00 96.68  ? 2   TYR   C O   1 
ATOM   3828  C  CB  . TYR   C  3  4   ? 34.643  -92.429  31.708  1.00 100.30 ? 2   TYR   C CB  1 
ATOM   3829  C  CG  . TYR   C  3  4   ? 34.365  -90.947  31.657  1.00 99.27  ? 2   TYR   C CG  1 
ATOM   3830  C  CD1 . TYR   C  3  4   ? 34.563  -90.144  32.769  1.00 99.01  ? 2   TYR   C CD1 1 
ATOM   3831  C  CD2 . TYR   C  3  4   ? 33.894  -90.345  30.503  1.00 99.79  ? 2   TYR   C CD2 1 
ATOM   3832  C  CE1 . TYR   C  3  4   ? 34.304  -88.783  32.737  1.00 100.34 ? 2   TYR   C CE1 1 
ATOM   3833  C  CE2 . TYR   C  3  4   ? 33.630  -88.985  30.453  1.00 101.96 ? 2   TYR   C CE2 1 
ATOM   3834  C  CZ  . TYR   C  3  4   ? 33.838  -88.198  31.573  1.00 102.05 ? 2   TYR   C CZ  1 
ATOM   3835  O  OH  . TYR   C  3  4   ? 33.581  -86.856  31.540  1.00 104.81 ? 2   TYR   C OH  1 
ATOM   3836  N  N   . ASP   C  3  5   ? 31.323  -92.500  32.712  1.00 100.14 ? 3   ASP   C N   1 
ATOM   3837  C  CA  . ASP   C  3  5   ? 29.850  -92.622  32.541  1.00 102.86 ? 3   ASP   C CA  1 
ATOM   3838  C  C   . ASP   C  3  5   ? 29.213  -91.311  32.052  1.00 105.99 ? 3   ASP   C C   1 
ATOM   3839  O  O   . ASP   C  3  5   ? 28.115  -91.396  31.462  1.00 98.40  ? 3   ASP   C O   1 
ATOM   3840  C  CB  . ASP   C  3  5   ? 29.212  -93.048  33.864  1.00 108.56 ? 3   ASP   C CB  1 
ATOM   3841  C  CG  . ASP   C  3  5   ? 27.869  -93.739  33.714  1.00 113.13 ? 3   ASP   C CG  1 
ATOM   3842  O  OD1 . ASP   C  3  5   ? 27.083  -93.692  34.679  1.00 123.90 ? 3   ASP   C OD1 1 
ATOM   3843  O  OD2 . ASP   C  3  5   ? 27.625  -94.325  32.639  1.00 117.42 ? 3   ASP   C OD2 1 
ATOM   3844  N  N   . ARG   C  3  6   ? 29.855  -90.160  32.301  1.00 105.88 ? 4   ARG   C N   1 
ATOM   3845  C  CA  . ARG   C  3  6   ? 29.308  -88.786  32.092  1.00 108.16 ? 4   ARG   C CA  1 
ATOM   3846  C  C   . ARG   C  3  6   ? 28.499  -88.695  30.792  1.00 105.04 ? 4   ARG   C C   1 
ATOM   3847  O  O   . ARG   C  3  6   ? 29.041  -89.041  29.724  1.00 108.39 ? 4   ARG   C O   1 
ATOM   3848  C  CB  . ARG   C  3  6   ? 30.437  -87.750  32.051  1.00 108.19 ? 4   ARG   C CB  1 
ATOM   3849  C  CG  . ARG   C  3  6   ? 30.509  -86.841  33.270  1.00 115.76 ? 4   ARG   C CG  1 
ATOM   3850  C  CD  . ARG   C  3  6   ? 29.641  -85.599  33.141  1.00 120.67 ? 4   ARG   C CD  1 
ATOM   3851  N  NE  . ARG   C  3  6   ? 30.190  -84.446  33.849  1.00 125.87 ? 4   ARG   C NE  1 
ATOM   3852  C  CZ  . ARG   C  3  6   ? 29.652  -83.229  33.856  1.00 129.61 ? 4   ARG   C CZ  1 
ATOM   3853  N  NH1 . ARG   C  3  6   ? 28.533  -82.983  33.192  1.00 134.16 ? 4   ARG   C NH1 1 
ATOM   3854  N  NH2 . ARG   C  3  6   ? 30.237  -82.253  34.530  1.00 133.91 ? 4   ARG   C NH2 1 
ATOM   3855  N  N   . ALA   C  3  7   ? 27.254  -88.218  30.888  1.00 102.75 ? 5   ALA   C N   1 
ATOM   3856  C  CA  . ALA   C  3  7   ? 26.405  -87.828  29.739  1.00 106.04 ? 5   ALA   C CA  1 
ATOM   3857  C  C   . ALA   C  3  7   ? 26.924  -86.499  29.175  1.00 106.23 ? 5   ALA   C C   1 
ATOM   3858  O  O   . ALA   C  3  7   ? 26.582  -85.438  29.739  1.00 107.07 ? 5   ALA   C O   1 
ATOM   3859  C  CB  . ALA   C  3  7   ? 24.962  -87.726  30.172  1.00 105.62 ? 5   ALA   C CB  1 
ATOM   3860  N  N   . LEU   C  3  8   ? 27.736  -86.560  28.114  1.00 108.21 ? 6   LEU   C N   1 
ATOM   3861  C  CA  . LEU   C  3  8   ? 28.387  -85.378  27.486  1.00 104.38 ? 6   LEU   C CA  1 
ATOM   3862  C  C   . LEU   C  3  8   ? 27.435  -84.740  26.469  1.00 107.31 ? 6   LEU   C C   1 
ATOM   3863  O  O   . LEU   C  3  8   ? 27.431  -83.499  26.373  1.00 112.83 ? 6   LEU   C O   1 
ATOM   3864  C  CB  . LEU   C  3  8   ? 29.699  -85.813  26.826  1.00 103.33 ? 6   LEU   C CB  1 
ATOM   3865  C  CG  . LEU   C  3  8   ? 30.736  -86.434  27.764  1.00 101.98 ? 6   LEU   C CG  1 
ATOM   3866  C  CD1 . LEU   C  3  8   ? 31.995  -86.811  27.001  1.00 101.63 ? 6   LEU   C CD1 1 
ATOM   3867  C  CD2 . LEU   C  3  8   ? 31.078  -85.494  28.908  1.00 102.54 ? 6   LEU   C CD2 1 
ATOM   3868  N  N   . SER   C  3  9   ? 26.663  -85.553  25.743  1.00 101.83 ? 7   SER   C N   1 
ATOM   3869  C  CA  . SER   C  3  9   ? 25.598  -85.094  24.815  1.00 102.86 ? 7   SER   C CA  1 
ATOM   3870  C  C   . SER   C  3  9   ? 24.264  -85.058  25.570  1.00 102.18 ? 7   SER   C C   1 
ATOM   3871  O  O   . SER   C  3  9   ? 23.735  -86.145  25.877  1.00 98.44  ? 7   SER   C O   1 
ATOM   3872  C  CB  . SER   C  3  9   ? 25.528  -85.974  23.597  1.00 103.85 ? 7   SER   C CB  1 
ATOM   3873  O  OG  . SER   C  3  9   ? 26.811  -86.121  23.006  1.00 109.56 ? 7   SER   C OG  1 
ATOM   3874  N  N   . ILE   C  3  10  ? 23.770  -83.852  25.885  1.00 101.91 ? 8   ILE   C N   1 
ATOM   3875  C  CA  . ILE   C  3  10  ? 22.484  -83.617  26.610  1.00 99.76  ? 8   ILE   C CA  1 
ATOM   3876  C  C   . ILE   C  3  10  ? 21.725  -82.462  25.946  1.00 100.83 ? 8   ILE   C C   1 
ATOM   3877  O  O   . ILE   C  3  10  ? 22.357  -81.669  25.224  1.00 104.73 ? 8   ILE   C O   1 
ATOM   3878  C  CB  . ILE   C  3  10  ? 22.729  -83.337  28.107  1.00 99.17  ? 8   ILE   C CB  1 
ATOM   3879  C  CG1 . ILE   C  3  10  ? 23.647  -82.132  28.324  1.00 101.44 ? 8   ILE   C CG1 1 
ATOM   3880  C  CG2 . ILE   C  3  10  ? 23.256  -84.579  28.807  1.00 97.03  ? 8   ILE   C CG2 1 
ATOM   3881  C  CD1 . ILE   C  3  10  ? 23.565  -81.541  29.715  1.00 104.21 ? 8   ILE   C CD1 1 
ATOM   3882  N  N   . PHE   C  3  11  ? 20.417  -82.384  26.201  1.00 98.38  ? 9   PHE   C N   1 
ATOM   3883  C  CA  . PHE   C  3  11  ? 19.504  -81.309  25.737  1.00 100.23 ? 9   PHE   C CA  1 
ATOM   3884  C  C   . PHE   C  3  11  ? 19.757  -80.027  26.535  1.00 104.31 ? 9   PHE   C C   1 
ATOM   3885  O  O   . PHE   C  3  11  ? 19.964  -80.108  27.762  1.00 106.83 ? 9   PHE   C O   1 
ATOM   3886  C  CB  . PHE   C  3  11  ? 18.045  -81.743  25.886  1.00 95.53  ? 9   PHE   C CB  1 
ATOM   3887  C  CG  . PHE   C  3  11  ? 17.631  -82.831  24.934  1.00 92.06  ? 9   PHE   C CG  1 
ATOM   3888  C  CD1 . PHE   C  3  11  ? 17.325  -82.533  23.617  1.00 92.84  ? 9   PHE   C CD1 1 
ATOM   3889  C  CD2 . PHE   C  3  11  ? 17.558  -84.150  25.348  1.00 90.72  ? 9   PHE   C CD2 1 
ATOM   3890  C  CE1 . PHE   C  3  11  ? 16.946  -83.531  22.735  1.00 92.29  ? 9   PHE   C CE1 1 
ATOM   3891  C  CE2 . PHE   C  3  11  ? 17.182  -85.147  24.464  1.00 90.55  ? 9   PHE   C CE2 1 
ATOM   3892  C  CZ  . PHE   C  3  11  ? 16.876  -84.836  23.160  1.00 91.21  ? 9   PHE   C CZ  1 
ATOM   3893  N  N   . SER   C  3  12  ? 19.733  -78.884  25.843  1.00 107.49 ? 10  SER   C N   1 
ATOM   3894  C  CA  . SER   C  3  12  ? 19.723  -77.519  26.429  1.00 112.04 ? 10  SER   C CA  1 
ATOM   3895  C  C   . SER   C  3  12  ? 18.283  -77.018  26.498  1.00 109.90 ? 10  SER   C C   1 
ATOM   3896  O  O   . SER   C  3  12  ? 17.415  -77.539  25.800  1.00 112.01 ? 10  SER   C O   1 
ATOM   3897  C  CB  . SER   C  3  12  ? 20.604  -76.583  25.640  1.00 114.22 ? 10  SER   C CB  1 
ATOM   3898  O  OG  . SER   C  3  12  ? 21.966  -76.765  25.991  1.00 120.77 ? 10  SER   C OG  1 
ATOM   3899  N  N   . PRO   C  3  13  ? 17.985  -76.008  27.348  1.00 107.81 ? 11  PRO   C N   1 
ATOM   3900  C  CA  . PRO   C  3  13  ? 16.629  -75.465  27.477  1.00 107.47 ? 11  PRO   C CA  1 
ATOM   3901  C  C   . PRO   C  3  13  ? 15.857  -75.223  26.169  1.00 108.37 ? 11  PRO   C C   1 
ATOM   3902  O  O   . PRO   C  3  13  ? 14.657  -75.440  26.171  1.00 107.56 ? 11  PRO   C O   1 
ATOM   3903  C  CB  . PRO   C  3  13  ? 16.888  -74.134  28.193  1.00 109.69 ? 11  PRO   C CB  1 
ATOM   3904  C  CG  . PRO   C  3  13  ? 18.069  -74.432  29.087  1.00 108.30 ? 11  PRO   C CG  1 
ATOM   3905  C  CD  . PRO   C  3  13  ? 18.934  -75.373  28.276  1.00 105.45 ? 11  PRO   C CD  1 
ATOM   3906  N  N   . ASP   C  3  14  ? 16.546  -74.798  25.102  1.00 111.69 ? 12  ASP   C N   1 
ATOM   3907  C  CA  . ASP   C  3  14  ? 15.942  -74.469  23.779  1.00 119.60 ? 12  ASP   C CA  1 
ATOM   3908  C  C   . ASP   C  3  14  ? 15.716  -75.745  22.953  1.00 116.89 ? 12  ASP   C C   1 
ATOM   3909  O  O   . ASP   C  3  14  ? 15.104  -75.636  21.872  1.00 119.97 ? 12  ASP   C O   1 
ATOM   3910  C  CB  . ASP   C  3  14  ? 16.797  -73.459  23.005  1.00 128.29 ? 12  ASP   C CB  1 
ATOM   3911  C  CG  . ASP   C  3  14  ? 18.226  -73.903  22.733  1.00 132.68 ? 12  ASP   C CG  1 
ATOM   3912  O  OD1 . ASP   C  3  14  ? 18.656  -74.920  23.322  1.00 134.65 ? 12  ASP   C OD1 1 
ATOM   3913  O  OD2 . ASP   C  3  14  ? 18.904  -73.220  21.937  1.00 141.71 ? 12  ASP   C OD2 1 
ATOM   3914  N  N   . GLY   C  3  15  ? 16.201  -76.897  23.429  1.00 113.70 ? 13  GLY   C N   1 
ATOM   3915  C  CA  . GLY   C  3  15  ? 15.982  -78.219  22.809  1.00 110.29 ? 13  GLY   C CA  1 
ATOM   3916  C  C   . GLY   C  3  15  ? 17.086  -78.599  21.835  1.00 110.05 ? 13  GLY   C C   1 
ATOM   3917  O  O   . GLY   C  3  15  ? 16.818  -79.432  20.951  1.00 109.10 ? 13  GLY   C O   1 
ATOM   3918  N  N   . HIS   C  3  16  ? 18.280  -78.016  21.980  1.00 109.21 ? 14  HIS   C N   1 
ATOM   3919  C  CA  . HIS   C  3  16  ? 19.483  -78.338  21.165  1.00 110.47 ? 14  HIS   C CA  1 
ATOM   3920  C  C   . HIS   C  3  16  ? 20.399  -79.274  21.959  1.00 104.70 ? 14  HIS   C C   1 
ATOM   3921  O  O   . HIS   C  3  16  ? 20.411  -79.170  23.200  1.00 108.16 ? 14  HIS   C O   1 
ATOM   3922  C  CB  . HIS   C  3  16  ? 20.208  -77.054  20.734  1.00 112.91 ? 14  HIS   C CB  1 
ATOM   3923  C  CG  . HIS   C  3  16  ? 19.450  -76.237  19.742  1.00 118.17 ? 14  HIS   C CG  1 
ATOM   3924  N  ND1 . HIS   C  3  16  ? 19.410  -74.859  19.799  1.00 121.82 ? 14  HIS   C ND1 1 
ATOM   3925  C  CD2 . HIS   C  3  16  ? 18.699  -76.595  18.677  1.00 119.83 ? 14  HIS   C CD2 1 
ATOM   3926  C  CE1 . HIS   C  3  16  ? 18.670  -74.401  18.808  1.00 126.35 ? 14  HIS   C CE1 1 
ATOM   3927  N  NE2 . HIS   C  3  16  ? 18.223  -75.448  18.104  1.00 123.17 ? 14  HIS   C NE2 1 
ATOM   3928  N  N   . ILE   C  3  17  ? 21.118  -80.162  21.265  1.00 101.63 ? 15  ILE   C N   1 
ATOM   3929  C  CA  . ILE   C  3  17  ? 22.225  -80.991  21.831  1.00 101.77 ? 15  ILE   C CA  1 
ATOM   3930  C  C   . ILE   C  3  17  ? 23.548  -80.378  21.359  1.00 99.15  ? 15  ILE   C C   1 
ATOM   3931  O  O   . ILE   C  3  17  ? 24.006  -80.733  20.256  1.00 100.53 ? 15  ILE   C O   1 
ATOM   3932  C  CB  . ILE   C  3  17  ? 22.091  -82.476  21.426  1.00 99.38  ? 15  ILE   C CB  1 
ATOM   3933  C  CG1 . ILE   C  3  17  ? 20.667  -83.003  21.631  1.00 98.86  ? 15  ILE   C CG1 1 
ATOM   3934  C  CG2 . ILE   C  3  17  ? 23.117  -83.322  22.166  1.00 99.74  ? 15  ILE   C CG2 1 
ATOM   3935  C  CD1 . ILE   C  3  17  ? 20.442  -84.404  21.103  1.00 96.65  ? 15  ILE   C CD1 1 
ATOM   3936  N  N   . PHE   C  3  18  ? 24.131  -79.484  22.164  1.00 96.75  ? 16  PHE   C N   1 
ATOM   3937  C  CA  . PHE   C  3  18  ? 25.236  -78.576  21.755  1.00 99.46  ? 16  PHE   C CA  1 
ATOM   3938  C  C   . PHE   C  3  18  ? 26.448  -79.386  21.280  1.00 98.34  ? 16  PHE   C C   1 
ATOM   3939  O  O   . PHE   C  3  18  ? 27.097  -78.959  20.305  1.00 99.47  ? 16  PHE   C O   1 
ATOM   3940  C  CB  . PHE   C  3  18  ? 25.606  -77.602  22.882  1.00 100.64 ? 16  PHE   C CB  1 
ATOM   3941  C  CG  . PHE   C  3  18  ? 24.682  -76.418  23.039  1.00 103.27 ? 16  PHE   C CG  1 
ATOM   3942  C  CD1 . PHE   C  3  18  ? 24.050  -75.843  21.944  1.00 103.64 ? 16  PHE   C CD1 1 
ATOM   3943  C  CD2 . PHE   C  3  18  ? 24.461  -75.858  24.289  1.00 102.69 ? 16  PHE   C CD2 1 
ATOM   3944  C  CE1 . PHE   C  3  18  ? 23.201  -74.759  22.099  1.00 108.19 ? 16  PHE   C CE1 1 
ATOM   3945  C  CE2 . PHE   C  3  18  ? 23.617  -74.770  24.442  1.00 107.34 ? 16  PHE   C CE2 1 
ATOM   3946  C  CZ  . PHE   C  3  18  ? 22.988  -74.222  23.347  1.00 110.50 ? 16  PHE   C CZ  1 
ATOM   3947  N  N   . GLN   C  3  19  ? 26.737  -80.517  21.924  1.00 94.87  ? 17  GLN   C N   1 
ATOM   3948  C  CA  . GLN   C  3  19  ? 27.913  -81.362  21.586  1.00 95.88  ? 17  GLN   C CA  1 
ATOM   3949  C  C   . GLN   C  3  19  ? 27.767  -81.896  20.154  1.00 96.04  ? 17  GLN   C C   1 
ATOM   3950  O  O   . GLN   C  3  19  ? 28.797  -81.968  19.456  1.00 98.41  ? 17  GLN   C O   1 
ATOM   3951  C  CB  . GLN   C  3  19  ? 28.089  -82.477  22.619  1.00 93.86  ? 17  GLN   C CB  1 
ATOM   3952  C  CG  . GLN   C  3  19  ? 28.892  -82.041  23.838  1.00 93.67  ? 17  GLN   C CG  1 
ATOM   3953  C  CD  . GLN   C  3  19  ? 30.319  -81.701  23.490  1.00 92.97  ? 17  GLN   C CD  1 
ATOM   3954  O  OE1 . GLN   C  3  19  ? 30.788  -80.594  23.741  1.00 91.27  ? 17  GLN   C OE1 1 
ATOM   3955  N  NE2 . GLN   C  3  19  ? 31.017  -82.656  22.897  1.00 94.68  ? 17  GLN   C NE2 1 
ATOM   3956  N  N   . VAL   C  3  20  ? 26.543  -82.233  19.730  1.00 97.34  ? 18  VAL   C N   1 
ATOM   3957  C  CA  . VAL   C  3  20  ? 26.229  -82.666  18.333  1.00 100.19 ? 18  VAL   C CA  1 
ATOM   3958  C  C   . VAL   C  3  20  ? 26.427  -81.465  17.400  1.00 101.53 ? 18  VAL   C C   1 
ATOM   3959  O  O   . VAL   C  3  20  ? 27.044  -81.638  16.331  1.00 99.35  ? 18  VAL   C O   1 
ATOM   3960  C  CB  . VAL   C  3  20  ? 24.804  -83.247  18.211  1.00 103.01 ? 18  VAL   C CB  1 
ATOM   3961  C  CG1 . VAL   C  3  20  ? 24.408  -83.496  16.760  1.00 104.28 ? 18  VAL   C CG1 1 
ATOM   3962  C  CG2 . VAL   C  3  20  ? 24.640  -84.521  19.028  1.00 102.52 ? 18  VAL   C CG2 1 
ATOM   3963  N  N   . GLU   C  3  21  ? 25.916  -80.295  17.793  1.00 102.65 ? 19  GLU   C N   1 
ATOM   3964  C  CA  . GLU   C  3  21  ? 25.961  -79.049  16.981  1.00 103.68 ? 19  GLU   C CA  1 
ATOM   3965  C  C   . GLU   C  3  21  ? 27.405  -78.544  16.872  1.00 99.29  ? 19  GLU   C C   1 
ATOM   3966  O  O   . GLU   C  3  21  ? 27.756  -78.008  15.804  1.00 98.87  ? 19  GLU   C O   1 
ATOM   3967  C  CB  . GLU   C  3  21  ? 25.030  -77.987  17.567  1.00 106.15 ? 19  GLU   C CB  1 
ATOM   3968  C  CG  . GLU   C  3  21  ? 23.643  -78.015  16.955  1.00 113.32 ? 19  GLU   C CG  1 
ATOM   3969  C  CD  . GLU   C  3  21  ? 22.568  -77.341  17.789  1.00 119.13 ? 19  GLU   C CD  1 
ATOM   3970  O  OE1 . GLU   C  3  21  ? 22.836  -76.254  18.339  1.00 124.02 ? 19  GLU   C OE1 1 
ATOM   3971  O  OE2 . GLU   C  3  21  ? 21.464  -77.910  17.888  1.00 131.35 ? 19  GLU   C OE2 1 
ATOM   3972  N  N   . TYR   C  3  22  ? 28.211  -78.703  17.925  1.00 94.96  ? 20  TYR   C N   1 
ATOM   3973  C  CA  . TYR   C  3  22  ? 29.644  -78.304  17.930  1.00 96.38  ? 20  TYR   C CA  1 
ATOM   3974  C  C   . TYR   C  3  22  ? 30.452  -79.293  17.082  1.00 97.72  ? 20  TYR   C C   1 
ATOM   3975  O  O   . TYR   C  3  22  ? 31.458  -78.880  16.474  1.00 98.11  ? 20  TYR   C O   1 
ATOM   3976  C  CB  . TYR   C  3  22  ? 30.199  -78.202  19.353  1.00 97.47  ? 20  TYR   C CB  1 
ATOM   3977  C  CG  . TYR   C  3  22  ? 29.533  -77.183  20.247  1.00 99.72  ? 20  TYR   C CG  1 
ATOM   3978  C  CD1 . TYR   C  3  22  ? 28.736  -76.167  19.738  1.00 102.58 ? 20  TYR   C CD1 1 
ATOM   3979  C  CD2 . TYR   C  3  22  ? 29.726  -77.221  21.619  1.00 100.16 ? 20  TYR   C CD2 1 
ATOM   3980  C  CE1 . TYR   C  3  22  ? 28.133  -75.234  20.569  1.00 106.51 ? 20  TYR   C CE1 1 
ATOM   3981  C  CE2 . TYR   C  3  22  ? 29.134  -76.295  22.463  1.00 102.83 ? 20  TYR   C CE2 1 
ATOM   3982  C  CZ  . TYR   C  3  22  ? 28.333  -75.297  21.937  1.00 105.50 ? 20  TYR   C CZ  1 
ATOM   3983  O  OH  . TYR   C  3  22  ? 27.750  -74.383  22.765  1.00 111.77 ? 20  TYR   C OH  1 
ATOM   3984  N  N   . ALA   C  3  23  ? 30.030  -80.558  17.029  1.00 96.36  ? 21  ALA   C N   1 
ATOM   3985  C  CA  . ALA   C  3  23  ? 30.632  -81.585  16.148  1.00 96.20  ? 21  ALA   C CA  1 
ATOM   3986  C  C   . ALA   C  3  23  ? 30.464  -81.151  14.687  1.00 96.00  ? 21  ALA   C C   1 
ATOM   3987  O  O   . ALA   C  3  23  ? 31.396  -81.392  13.898  1.00 97.60  ? 21  ALA   C O   1 
ATOM   3988  C  CB  . ALA   C  3  23  ? 30.025  -82.942  16.411  1.00 96.04  ? 21  ALA   C CB  1 
ATOM   3989  N  N   . LEU   C  3  24  ? 29.334  -80.515  14.352  1.00 94.61  ? 22  LEU   C N   1 
ATOM   3990  C  CA  . LEU   C  3  24  ? 29.054  -79.990  12.986  1.00 94.34  ? 22  LEU   C CA  1 
ATOM   3991  C  C   . LEU   C  3  24  ? 30.039  -78.861  12.657  1.00 94.71  ? 22  LEU   C C   1 
ATOM   3992  O  O   . LEU   C  3  24  ? 30.422  -78.755  11.480  1.00 96.33  ? 22  LEU   C O   1 
ATOM   3993  C  CB  . LEU   C  3  24  ? 27.601  -79.509  12.884  1.00 95.19  ? 22  LEU   C CB  1 
ATOM   3994  C  CG  . LEU   C  3  24  ? 26.626  -80.499  12.250  1.00 96.21  ? 22  LEU   C CG  1 
ATOM   3995  C  CD1 . LEU   C  3  24  ? 25.186  -80.072  12.495  1.00 98.53  ? 22  LEU   C CD1 1 
ATOM   3996  C  CD2 . LEU   C  3  24  ? 26.892  -80.649  10.758  1.00 95.96  ? 22  LEU   C CD2 1 
ATOM   3997  N  N   . GLU   C  3  25  ? 30.434  -78.059  13.653  1.00 96.09  ? 23  GLU   C N   1 
ATOM   3998  C  CA  . GLU   C  3  25  ? 31.399  -76.938  13.476  1.00 99.39  ? 23  GLU   C CA  1 
ATOM   3999  C  C   . GLU   C  3  25  ? 32.769  -77.506  13.088  1.00 98.96  ? 23  GLU   C C   1 
ATOM   4000  O  O   . GLU   C  3  25  ? 33.463  -76.860  12.278  1.00 103.29 ? 23  GLU   C O   1 
ATOM   4001  C  CB  . GLU   C  3  25  ? 31.512  -76.077  14.737  1.00 101.27 ? 23  GLU   C CB  1 
ATOM   4002  C  CG  . GLU   C  3  25  ? 30.229  -75.355  15.114  1.00 103.36 ? 23  GLU   C CG  1 
ATOM   4003  C  CD  . GLU   C  3  25  ? 29.702  -74.380  14.075  1.00 103.35 ? 23  GLU   C CD  1 
ATOM   4004  O  OE1 . GLU   C  3  25  ? 30.524  -73.706  13.422  1.00 106.55 ? 23  GLU   C OE1 1 
ATOM   4005  O  OE2 . GLU   C  3  25  ? 28.469  -74.300  13.919  1.00 108.81 ? 23  GLU   C OE2 1 
ATOM   4006  N  N   . ALA   C  3  26  ? 33.143  -78.661  13.645  1.00 97.27  ? 24  ALA   C N   1 
ATOM   4007  C  CA  . ALA   C  3  26  ? 34.380  -79.397  13.293  1.00 97.42  ? 24  ALA   C CA  1 
ATOM   4008  C  C   . ALA   C  3  26  ? 34.322  -79.804  11.817  1.00 94.75  ? 24  ALA   C C   1 
ATOM   4009  O  O   . ALA   C  3  26  ? 35.364  -79.708  11.144  1.00 92.03  ? 24  ALA   C O   1 
ATOM   4010  C  CB  . ALA   C  3  26  ? 34.557  -80.598  14.188  1.00 98.24  ? 24  ALA   C CB  1 
ATOM   4011  N  N   . VAL   C  3  27  ? 33.145  -80.234  11.346  1.00 96.75  ? 25  VAL   C N   1 
ATOM   4012  C  CA  . VAL   C  3  27  ? 32.889  -80.613  9.922   1.00 99.33  ? 25  VAL   C CA  1 
ATOM   4013  C  C   . VAL   C  3  27  ? 33.073  -79.367  9.050   1.00 102.10 ? 25  VAL   C C   1 
ATOM   4014  O  O   . VAL   C  3  27  ? 33.734  -79.478  7.999   1.00 97.96  ? 25  VAL   C O   1 
ATOM   4015  C  CB  . VAL   C  3  27  ? 31.490  -81.235  9.725   1.00 101.01 ? 25  VAL   C CB  1 
ATOM   4016  C  CG1 . VAL   C  3  27  ? 31.155  -81.431  8.253   1.00 102.49 ? 25  VAL   C CG1 1 
ATOM   4017  C  CG2 . VAL   C  3  27  ? 31.343  -82.549  10.476  1.00 100.44 ? 25  VAL   C CG2 1 
ATOM   4018  N  N   . LYS   C  3  28  ? 32.516  -78.230  9.485   1.00 105.50 ? 26  LYS   C N   1 
ATOM   4019  C  CA  . LYS   C  3  28  ? 32.572  -76.927  8.764   1.00 106.06 ? 26  LYS   C CA  1 
ATOM   4020  C  C   . LYS   C  3  28  ? 34.022  -76.438  8.646   1.00 104.64 ? 26  LYS   C C   1 
ATOM   4021  O  O   . LYS   C  3  28  ? 34.290  -75.655  7.718   1.00 103.14 ? 26  LYS   C O   1 
ATOM   4022  C  CB  . LYS   C  3  28  ? 31.706  -75.872  9.461   1.00 109.96 ? 26  LYS   C CB  1 
ATOM   4023  C  CG  . LYS   C  3  28  ? 30.282  -75.760  8.932   1.00 117.29 ? 26  LYS   C CG  1 
ATOM   4024  C  CD  . LYS   C  3  28  ? 29.644  -74.411  9.192   1.00 120.26 ? 26  LYS   C CD  1 
ATOM   4025  C  CE  . LYS   C  3  28  ? 28.939  -74.335  10.529  1.00 125.29 ? 26  LYS   C CE  1 
ATOM   4026  N  NZ  . LYS   C  3  28  ? 27.591  -74.946  10.467  1.00 126.04 ? 26  LYS   C NZ  1 
ATOM   4027  N  N   . ARG   C  3  29  ? 34.910  -76.870  9.548   1.00 103.04 ? 27  ARG   C N   1 
ATOM   4028  C  CA  . ARG   C  3  29  ? 36.354  -76.511  9.545   1.00 104.62 ? 27  ARG   C CA  1 
ATOM   4029  C  C   . ARG   C  3  29  ? 37.120  -77.423  8.579   1.00 102.03 ? 27  ARG   C C   1 
ATOM   4030  O  O   . ARG   C  3  29  ? 38.132  -76.960  8.022   1.00 102.25 ? 27  ARG   C O   1 
ATOM   4031  C  CB  . ARG   C  3  29  ? 36.931  -76.610  10.961  1.00 109.03 ? 27  ARG   C CB  1 
ATOM   4032  C  CG  . ARG   C  3  29  ? 38.409  -76.257  11.067  1.00 115.91 ? 27  ARG   C CG  1 
ATOM   4033  C  CD  . ARG   C  3  29  ? 38.894  -76.176  12.504  1.00 121.51 ? 27  ARG   C CD  1 
ATOM   4034  N  NE  . ARG   C  3  29  ? 38.397  -74.981  13.179  1.00 125.92 ? 27  ARG   C NE  1 
ATOM   4035  C  CZ  . ARG   C  3  29  ? 37.286  -74.905  13.914  1.00 128.46 ? 27  ARG   C CZ  1 
ATOM   4036  N  NH1 . ARG   C  3  29  ? 36.514  -75.965  14.101  1.00 130.21 ? 27  ARG   C NH1 1 
ATOM   4037  N  NH2 . ARG   C  3  29  ? 36.948  -73.753  14.465  1.00 129.82 ? 27  ARG   C NH2 1 
ATOM   4038  N  N   . GLY   C  3  30  ? 36.662  -78.666  8.396   1.00 100.18 ? 28  GLY   C N   1 
ATOM   4039  C  CA  . GLY   C  3  30  ? 37.318  -79.677  7.542   1.00 102.00 ? 28  GLY   C CA  1 
ATOM   4040  C  C   . GLY   C  3  30  ? 37.372  -79.245  6.087   1.00 103.41 ? 28  GLY   C C   1 
ATOM   4041  O  O   . GLY   C  3  30  ? 36.579  -78.363  5.704   1.00 104.54 ? 28  GLY   C O   1 
ATOM   4042  N  N   . THR   C  3  31  ? 38.269  -79.852  5.302   1.00 105.25 ? 29  THR   C N   1 
ATOM   4043  C  CA  . THR   C  3  31  ? 38.481  -79.542  3.861   1.00 106.61 ? 29  THR   C CA  1 
ATOM   4044  C  C   . THR   C  3  31  ? 37.223  -79.947  3.090   1.00 105.20 ? 29  THR   C C   1 
ATOM   4045  O  O   . THR   C  3  31  ? 36.591  -80.949  3.476   1.00 103.62 ? 29  THR   C O   1 
ATOM   4046  C  CB  . THR   C  3  31  ? 39.737  -80.224  3.302   1.00 109.75 ? 29  THR   C CB  1 
ATOM   4047  O  OG1 . THR   C  3  31  ? 39.586  -81.640  3.411   1.00 109.21 ? 29  THR   C OG1 1 
ATOM   4048  C  CG2 . THR   C  3  31  ? 41.002  -79.787  4.010   1.00 112.92 ? 29  THR   C CG2 1 
ATOM   4049  N  N   . CYS   C  3  32  ? 36.867  -79.180  2.057   1.00 107.26 ? 30  CYS   C N   1 
ATOM   4050  C  CA  . CYS   C  3  32  ? 35.638  -79.384  1.248   1.00 108.40 ? 30  CYS   C CA  1 
ATOM   4051  C  C   . CYS   C  3  32  ? 35.698  -80.750  0.559   1.00 103.71 ? 30  CYS   C C   1 
ATOM   4052  O  O   . CYS   C  3  32  ? 36.752  -81.081  -0.023  1.00 100.24 ? 30  CYS   C O   1 
ATOM   4053  C  CB  . CYS   C  3  32  ? 35.449  -78.289  0.206   1.00 113.88 ? 30  CYS   C CB  1 
ATOM   4054  S  SG  . CYS   C  3  32  ? 33.919  -78.478  -0.746  1.00 119.84 ? 30  CYS   C SG  1 
ATOM   4055  N  N   . ALA   C  3  33  ? 34.606  -81.509  0.649   1.00 101.38 ? 31  ALA   C N   1 
ATOM   4056  C  CA  . ALA   C  3  33  ? 34.378  -82.777  -0.079  1.00 101.33 ? 31  ALA   C CA  1 
ATOM   4057  C  C   . ALA   C  3  33  ? 33.070  -82.650  -0.861  1.00 99.05  ? 31  ALA   C C   1 
ATOM   4058  O  O   . ALA   C  3  33  ? 32.102  -82.098  -0.301  1.00 98.36  ? 31  ALA   C O   1 
ATOM   4059  C  CB  . ALA   C  3  33  ? 34.343  -83.935  0.888   1.00 99.47  ? 31  ALA   C CB  1 
ATOM   4060  N  N   . VAL   C  3  34  ? 33.053  -83.129  -2.108  1.00 100.29 ? 32  VAL   C N   1 
ATOM   4061  C  CA  . VAL   C  3  34  ? 31.869  -83.054  -3.013  1.00 98.33  ? 32  VAL   C CA  1 
ATOM   4062  C  C   . VAL   C  3  34  ? 31.633  -84.431  -3.644  1.00 98.74  ? 32  VAL   C C   1 
ATOM   4063  O  O   . VAL   C  3  34  ? 32.621  -85.113  -3.991  1.00 95.51  ? 32  VAL   C O   1 
ATOM   4064  C  CB  . VAL   C  3  34  ? 32.034  -81.956  -4.081  1.00 97.19  ? 32  VAL   C CB  1 
ATOM   4065  C  CG1 . VAL   C  3  34  ? 33.304  -82.132  -4.899  1.00 98.19  ? 32  VAL   C CG1 1 
ATOM   4066  C  CG2 . VAL   C  3  34  ? 30.816  -81.868  -4.987  1.00 96.68  ? 32  VAL   C CG2 1 
ATOM   4067  N  N   . GLY   C  3  35  ? 30.358  -84.809  -3.756  1.00 100.10 ? 33  GLY   C N   1 
ATOM   4068  C  CA  . GLY   C  3  35  ? 29.881  -85.995  -4.489  1.00 99.70  ? 33  GLY   C CA  1 
ATOM   4069  C  C   . GLY   C  3  35  ? 28.910  -85.586  -5.579  1.00 101.89 ? 33  GLY   C C   1 
ATOM   4070  O  O   . GLY   C  3  35  ? 27.993  -84.795  -5.285  1.00 103.56 ? 33  GLY   C O   1 
ATOM   4071  N  N   . VAL   C  3  36  ? 29.128  -86.070  -6.802  1.00 101.54 ? 34  VAL   C N   1 
ATOM   4072  C  CA  . VAL   C  3  36  ? 28.237  -85.842  -7.976  1.00 103.06 ? 34  VAL   C CA  1 
ATOM   4073  C  C   . VAL   C  3  36  ? 28.032  -87.189  -8.667  1.00 102.74 ? 34  VAL   C C   1 
ATOM   4074  O  O   . VAL   C  3  36  ? 29.048  -87.812  -9.034  1.00 100.80 ? 34  VAL   C O   1 
ATOM   4075  C  CB  . VAL   C  3  36  ? 28.834  -84.810  -8.953  1.00 103.74 ? 34  VAL   C CB  1 
ATOM   4076  C  CG1 . VAL   C  3  36  ? 27.956  -84.619  -10.182 1.00 104.69 ? 34  VAL   C CG1 1 
ATOM   4077  C  CG2 . VAL   C  3  36  ? 29.102  -83.478  -8.273  1.00 103.77 ? 34  VAL   C CG2 1 
ATOM   4078  N  N   . LYS   C  3  37  ? 26.779  -87.616  -8.844  1.00 103.62 ? 35  LYS   C N   1 
ATOM   4079  C  CA  . LYS   C  3  37  ? 26.468  -88.885  -9.552  1.00 106.63 ? 35  LYS   C CA  1 
ATOM   4080  C  C   . LYS   C  3  37  ? 25.919  -88.554  -10.942 1.00 113.01 ? 35  LYS   C C   1 
ATOM   4081  O  O   . LYS   C  3  37  ? 25.055  -87.657  -11.050 1.00 115.38 ? 35  LYS   C O   1 
ATOM   4082  C  CB  . LYS   C  3  37  ? 25.552  -89.785  -8.715  1.00 104.49 ? 35  LYS   C CB  1 
ATOM   4083  C  CG  . LYS   C  3  37  ? 24.090  -89.383  -8.606  1.00 103.00 ? 35  LYS   C CG  1 
ATOM   4084  C  CD  . LYS   C  3  37  ? 23.399  -90.102  -7.467  1.00 100.19 ? 35  LYS   C CD  1 
ATOM   4085  C  CE  . LYS   C  3  37  ? 22.046  -90.665  -7.835  1.00 100.18 ? 35  LYS   C CE  1 
ATOM   4086  N  NZ  . LYS   C  3  37  ? 21.337  -91.174  -6.638  1.00 99.38  ? 35  LYS   C NZ  1 
ATOM   4087  N  N   . GLY   C  3  38  ? 26.457  -89.238  -11.956 1.00 115.12 ? 36  GLY   C N   1 
ATOM   4088  C  CA  . GLY   C  3  38  ? 26.067  -89.110  -13.371 1.00 117.30 ? 36  GLY   C CA  1 
ATOM   4089  C  C   . GLY   C  3  38  ? 24.993  -90.117  -13.734 1.00 119.56 ? 36  GLY   C C   1 
ATOM   4090  O  O   . GLY   C  3  38  ? 24.211  -90.499  -12.840 1.00 114.86 ? 36  GLY   C O   1 
ATOM   4091  N  N   . LYS   C  3  39  ? 24.964  -90.536  -15.001 1.00 125.16 ? 37  LYS   C N   1 
ATOM   4092  C  CA  . LYS   C  3  39  ? 23.954  -91.476  -15.555 1.00 128.92 ? 37  LYS   C CA  1 
ATOM   4093  C  C   . LYS   C  3  39  ? 24.414  -92.916  -15.296 1.00 126.28 ? 37  LYS   C C   1 
ATOM   4094  O  O   . LYS   C  3  39  ? 23.546  -93.809  -15.221 1.00 123.67 ? 37  LYS   C O   1 
ATOM   4095  C  CB  . LYS   C  3  39  ? 23.751  -91.191  -17.047 1.00 133.39 ? 37  LYS   C CB  1 
ATOM   4096  C  CG  . LYS   C  3  39  ? 22.321  -91.332  -17.553 1.00 139.49 ? 37  LYS   C CG  1 
ATOM   4097  C  CD  . LYS   C  3  39  ? 21.944  -92.746  -17.931 1.00 144.43 ? 37  LYS   C CD  1 
ATOM   4098  C  CE  . LYS   C  3  39  ? 20.457  -92.918  -18.154 1.00 150.88 ? 37  LYS   C CE  1 
ATOM   4099  N  NZ  . LYS   C  3  39  ? 20.096  -94.342  -18.353 1.00 154.21 ? 37  LYS   C NZ  1 
ATOM   4100  N  N   . ASN   C  3  40  ? 25.726  -93.119  -15.129 1.00 125.22 ? 38  ASN   C N   1 
ATOM   4101  C  CA  . ASN   C  3  40  ? 26.374  -94.459  -15.091 1.00 125.23 ? 38  ASN   C CA  1 
ATOM   4102  C  C   . ASN   C  3  40  ? 27.625  -94.448  -14.201 1.00 120.88 ? 38  ASN   C C   1 
ATOM   4103  O  O   . ASN   C  3  40  ? 28.510  -95.296  -14.432 1.00 117.82 ? 38  ASN   C O   1 
ATOM   4104  C  CB  . ASN   C  3  40  ? 26.727  -94.935  -16.505 1.00 130.34 ? 38  ASN   C CB  1 
ATOM   4105  C  CG  . ASN   C  3  40  ? 27.662  -94.022  -17.282 1.00 131.33 ? 38  ASN   C CG  1 
ATOM   4106  O  OD1 . ASN   C  3  40  ? 27.908  -94.269  -18.460 1.00 135.02 ? 38  ASN   C OD1 1 
ATOM   4107  N  ND2 . ASN   C  3  40  ? 28.198  -92.974  -16.672 1.00 131.58 ? 38  ASN   C ND2 1 
ATOM   4108  N  N   . CYS   C  3  41  ? 27.703  -93.534  -13.228 1.00 120.36 ? 39  CYS   C N   1 
ATOM   4109  C  CA  . CYS   C  3  41  ? 28.907  -93.316  -12.378 1.00 117.59 ? 39  CYS   C CA  1 
ATOM   4110  C  C   . CYS   C  3  41  ? 28.603  -92.327  -11.248 1.00 114.02 ? 39  CYS   C C   1 
ATOM   4111  O  O   . CYS   C  3  41  ? 27.657  -91.526  -11.391 1.00 110.23 ? 39  CYS   C O   1 
ATOM   4112  C  CB  . CYS   C  3  41  ? 30.080  -92.786  -13.196 1.00 121.47 ? 39  CYS   C CB  1 
ATOM   4113  S  SG  . CYS   C  3  41  ? 29.802  -91.142  -13.908 1.00 122.15 ? 39  CYS   C SG  1 
ATOM   4114  N  N   . VAL   C  3  42  ? 29.386  -92.407  -10.170 1.00 111.73 ? 40  VAL   C N   1 
ATOM   4115  C  CA  . VAL   C  3  42  ? 29.477  -91.379  -9.092  1.00 108.93 ? 40  VAL   C CA  1 
ATOM   4116  C  C   . VAL   C  3  42  ? 30.933  -90.914  -9.040  1.00 111.35 ? 40  VAL   C C   1 
ATOM   4117  O  O   . VAL   C  3  42  ? 31.831  -91.765  -9.191  1.00 106.52 ? 40  VAL   C O   1 
ATOM   4118  C  CB  . VAL   C  3  42  ? 29.009  -91.909  -7.722  1.00 106.91 ? 40  VAL   C CB  1 
ATOM   4119  C  CG1 . VAL   C  3  42  ? 28.753  -90.771  -6.747  1.00 105.94 ? 40  VAL   C CG1 1 
ATOM   4120  C  CG2 . VAL   C  3  42  ? 27.778  -92.797  -7.833  1.00 107.51 ? 40  VAL   C CG2 1 
ATOM   4121  N  N   . VAL   C  3  43  ? 31.150  -89.610  -8.866  1.00 113.98 ? 41  VAL   C N   1 
ATOM   4122  C  CA  . VAL   C  3  43  ? 32.505  -88.997  -8.744  1.00 115.88 ? 41  VAL   C CA  1 
ATOM   4123  C  C   . VAL   C  3  43  ? 32.598  -88.322  -7.373  1.00 119.05 ? 41  VAL   C C   1 
ATOM   4124  O  O   . VAL   C  3  43  ? 31.718  -87.494  -7.060  1.00 120.32 ? 41  VAL   C O   1 
ATOM   4125  C  CB  . VAL   C  3  43  ? 32.791  -88.006  -9.889  1.00 115.74 ? 41  VAL   C CB  1 
ATOM   4126  C  CG1 . VAL   C  3  43  ? 34.126  -87.300  -9.703  1.00 115.01 ? 41  VAL   C CG1 1 
ATOM   4127  C  CG2 . VAL   C  3  43  ? 32.738  -88.690  -11.246 1.00 115.51 ? 41  VAL   C CG2 1 
ATOM   4128  N  N   . LEU   C  3  44  ? 33.622  -88.682  -6.593  1.00 120.34 ? 42  LEU   C N   1 
ATOM   4129  C  CA  . LEU   C  3  44  ? 33.952  -88.038  -5.296  1.00 115.62 ? 42  LEU   C CA  1 
ATOM   4130  C  C   . LEU   C  3  44  ? 35.163  -87.121  -5.496  1.00 115.84 ? 42  LEU   C C   1 
ATOM   4131  O  O   . LEU   C  3  44  ? 36.249  -87.634  -5.833  1.00 117.05 ? 42  LEU   C O   1 
ATOM   4132  C  CB  . LEU   C  3  44  ? 34.227  -89.116  -4.242  1.00 114.97 ? 42  LEU   C CB  1 
ATOM   4133  C  CG  . LEU   C  3  44  ? 33.028  -89.976  -3.835  1.00 113.94 ? 42  LEU   C CG  1 
ATOM   4134  C  CD1 . LEU   C  3  44  ? 33.406  -90.910  -2.697  1.00 114.02 ? 42  LEU   C CD1 1 
ATOM   4135  C  CD2 . LEU   C  3  44  ? 31.830  -89.125  -3.435  1.00 111.98 ? 42  LEU   C CD2 1 
ATOM   4136  N  N   . GLY   C  3  45  ? 34.954  -85.813  -5.324  1.00 115.33 ? 43  GLY   C N   1 
ATOM   4137  C  CA  . GLY   C  3  45  ? 36.010  -84.785  -5.336  1.00 114.66 ? 43  GLY   C CA  1 
ATOM   4138  C  C   . GLY   C  3  45  ? 36.328  -84.337  -3.924  1.00 114.59 ? 43  GLY   C C   1 
ATOM   4139  O  O   . GLY   C  3  45  ? 35.399  -84.329  -3.092  1.00 113.18 ? 43  GLY   C O   1 
ATOM   4140  N  N   . CYS   C  3  46  ? 37.591  -84.000  -3.649  1.00 117.18 ? 44  CYS   C N   1 
ATOM   4141  C  CA  . CYS   C  3  46  ? 38.070  -83.616  -2.295  1.00 123.03 ? 44  CYS   C CA  1 
ATOM   4142  C  C   . CYS   C  3  46  ? 39.151  -82.535  -2.386  1.00 125.64 ? 44  CYS   C C   1 
ATOM   4143  O  O   . CYS   C  3  46  ? 40.119  -82.722  -3.149  1.00 129.34 ? 44  CYS   C O   1 
ATOM   4144  C  CB  . CYS   C  3  46  ? 38.594  -84.834  -1.546  1.00 127.53 ? 44  CYS   C CB  1 
ATOM   4145  S  SG  . CYS   C  3  46  ? 37.299  -86.052  -1.194  1.00 133.45 ? 44  CYS   C SG  1 
ATOM   4146  N  N   . GLU   C  3  47  ? 38.968  -81.447  -1.631  1.00 127.90 ? 45  GLU   C N   1 
ATOM   4147  C  CA  . GLU   C  3  47  ? 39.960  -80.356  -1.442  1.00 133.03 ? 45  GLU   C CA  1 
ATOM   4148  C  C   . GLU   C  3  47  ? 41.102  -80.877  -0.562  1.00 137.46 ? 45  GLU   C C   1 
ATOM   4149  O  O   . GLU   C  3  47  ? 40.816  -81.659  0.370   1.00 138.59 ? 45  GLU   C O   1 
ATOM   4150  C  CB  . GLU   C  3  47  ? 39.290  -79.143  -0.789  1.00 131.40 ? 45  GLU   C CB  1 
ATOM   4151  C  CG  . GLU   C  3  47  ? 40.197  -77.931  -0.662  1.00 134.88 ? 45  GLU   C CG  1 
ATOM   4152  C  CD  . GLU   C  3  47  ? 39.735  -76.872  0.326   1.00 132.61 ? 45  GLU   C CD  1 
ATOM   4153  O  OE1 . GLU   C  3  47  ? 40.527  -75.952  0.609   1.00 133.29 ? 45  GLU   C OE1 1 
ATOM   4154  O  OE2 . GLU   C  3  47  ? 38.589  -76.967  0.811   1.00 131.00 ? 45  GLU   C OE2 1 
ATOM   4155  N  N   . ARG   C  3  48  ? 42.340  -80.469  -0.857  1.00 138.54 ? 46  ARG   C N   1 
ATOM   4156  C  CA  . ARG   C  3  48  ? 43.528  -80.686  0.014   1.00 141.04 ? 46  ARG   C CA  1 
ATOM   4157  C  C   . ARG   C  3  48  ? 44.259  -79.352  0.192   1.00 140.96 ? 46  ARG   C C   1 
ATOM   4158  O  O   . ARG   C  3  48  ? 44.780  -78.827  -0.810  1.00 134.69 ? 46  ARG   C O   1 
ATOM   4159  C  CB  . ARG   C  3  48  ? 44.452  -81.762  -0.566  1.00 149.41 ? 46  ARG   C CB  1 
ATOM   4160  C  CG  . ARG   C  3  48  ? 44.019  -83.187  -0.250  1.00 153.24 ? 46  ARG   C CG  1 
ATOM   4161  C  CD  . ARG   C  3  48  ? 45.180  -84.163  -0.159  1.00 156.13 ? 46  ARG   C CD  1 
ATOM   4162  N  NE  . ARG   C  3  48  ? 45.839  -84.393  -1.443  1.00 160.05 ? 46  ARG   C NE  1 
ATOM   4163  C  CZ  . ARG   C  3  48  ? 46.985  -83.840  -1.845  1.00 161.70 ? 46  ARG   C CZ  1 
ATOM   4164  N  NH1 . ARG   C  3  48  ? 47.648  -82.995  -1.069  1.00 167.13 ? 46  ARG   C NH1 1 
ATOM   4165  N  NH2 . ARG   C  3  48  ? 47.472  -84.139  -3.038  1.00 162.04 ? 46  ARG   C NH2 1 
ATOM   4166  N  N   . ARG   C  3  49  ? 44.282  -78.835  1.424   1.00 145.81 ? 47  ARG   C N   1 
ATOM   4167  C  CA  . ARG   C  3  49  ? 44.839  -77.497  1.775   1.00 152.78 ? 47  ARG   C CA  1 
ATOM   4168  C  C   . ARG   C  3  49  ? 46.341  -77.463  1.464   1.00 153.72 ? 47  ARG   C C   1 
ATOM   4169  O  O   . ARG   C  3  49  ? 47.013  -78.498  1.660   1.00 153.57 ? 47  ARG   C O   1 
ATOM   4170  C  CB  . ARG   C  3  49  ? 44.534  -77.140  3.236   1.00 156.53 ? 47  ARG   C CB  1 
ATOM   4171  C  CG  . ARG   C  3  49  ? 45.038  -78.124  4.283   1.00 156.23 ? 47  ARG   C CG  1 
ATOM   4172  C  CD  . ARG   C  3  49  ? 44.384  -77.840  5.624   1.00 153.29 ? 47  ARG   C CD  1 
ATOM   4173  N  NE  . ARG   C  3  49  ? 44.822  -78.745  6.681   1.00 155.08 ? 47  ARG   C NE  1 
ATOM   4174  C  CZ  . ARG   C  3  49  ? 45.765  -78.483  7.589   1.00 160.52 ? 47  ARG   C CZ  1 
ATOM   4175  N  NH1 . ARG   C  3  49  ? 46.406  -77.324  7.596   1.00 164.21 ? 47  ARG   C NH1 1 
ATOM   4176  N  NH2 . ARG   C  3  49  ? 46.065  -79.394  8.499   1.00 160.18 ? 47  ARG   C NH2 1 
ATOM   4177  N  N   . SER   C  3  50  ? 46.832  -76.309  0.993   1.00 155.16 ? 48  SER   C N   1 
ATOM   4178  C  CA  . SER   C  3  50  ? 48.193  -76.119  0.421   1.00 152.74 ? 48  SER   C CA  1 
ATOM   4179  C  C   . SER   C  3  50  ? 49.106  -75.342  1.378   1.00 150.14 ? 48  SER   C C   1 
ATOM   4180  O  O   . SER   C  3  50  ? 50.179  -74.901  0.916   1.00 150.38 ? 48  SER   C O   1 
ATOM   4181  C  CB  . SER   C  3  50  ? 48.118  -75.430  -0.917  1.00 150.65 ? 48  SER   C CB  1 
ATOM   4182  O  OG  . SER   C  3  50  ? 49.357  -75.523  -1.603  1.00 151.95 ? 48  SER   C OG  1 
ATOM   4183  N  N   . THR   C  3  51  ? 48.722  -75.186  2.652   1.00 148.74 ? 49  THR   C N   1 
ATOM   4184  C  CA  . THR   C  3  51  ? 49.613  -74.670  3.730   1.00 148.51 ? 49  THR   C CA  1 
ATOM   4185  C  C   . THR   C  3  51  ? 50.629  -75.757  4.115   1.00 150.83 ? 49  THR   C C   1 
ATOM   4186  O  O   . THR   C  3  51  ? 51.531  -75.448  4.921   1.00 155.58 ? 49  THR   C O   1 
ATOM   4187  C  CB  . THR   C  3  51  ? 48.826  -74.181  4.954   1.00 144.57 ? 49  THR   C CB  1 
ATOM   4188  O  OG1 . THR   C  3  51  ? 47.755  -75.093  5.204   1.00 138.54 ? 49  THR   C OG1 1 
ATOM   4189  C  CG2 . THR   C  3  51  ? 48.277  -72.782  4.780   1.00 142.12 ? 49  THR   C CG2 1 
ATOM   4190  N  N   . LEU   C  3  52  ? 50.489  -76.968  3.557   1.00 153.32 ? 50  LEU   C N   1 
ATOM   4191  C  CA  . LEU   C  3  52  ? 51.396  -78.128  3.779   1.00 151.28 ? 50  LEU   C CA  1 
ATOM   4192  C  C   . LEU   C  3  52  ? 52.154  -78.441  2.479   1.00 146.29 ? 50  LEU   C C   1 
ATOM   4193  O  O   . LEU   C  3  52  ? 51.629  -79.222  1.659   1.00 143.95 ? 50  LEU   C O   1 
ATOM   4194  C  CB  . LEU   C  3  52  ? 50.583  -79.348  4.238   1.00 148.90 ? 50  LEU   C CB  1 
ATOM   4195  C  CG  . LEU   C  3  52  ? 49.317  -79.078  5.053   1.00 145.73 ? 50  LEU   C CG  1 
ATOM   4196  C  CD1 . LEU   C  3  52  ? 48.487  -80.347  5.183   1.00 140.49 ? 50  LEU   C CD1 1 
ATOM   4197  C  CD2 . LEU   C  3  52  ? 49.648  -78.516  6.427   1.00 146.11 ? 50  LEU   C CD2 1 
ATOM   4198  N  N   . LYS   C  3  53  ? 53.329  -77.832  2.286   1.00 148.03 ? 51  LYS   C N   1 
ATOM   4199  C  CA  . LYS   C  3  53  ? 54.333  -78.255  1.269   1.00 147.47 ? 51  LYS   C CA  1 
ATOM   4200  C  C   . LYS   C  3  53  ? 55.417  -79.064  1.987   1.00 139.93 ? 51  LYS   C C   1 
ATOM   4201  O  O   . LYS   C  3  53  ? 55.542  -78.909  3.219   1.00 134.23 ? 51  LYS   C O   1 
ATOM   4202  C  CB  . LYS   C  3  53  ? 54.891  -77.051  0.499   1.00 151.53 ? 51  LYS   C CB  1 
ATOM   4203  C  CG  . LYS   C  3  53  ? 54.464  -76.969  -0.963  1.00 157.49 ? 51  LYS   C CG  1 
ATOM   4204  C  CD  . LYS   C  3  53  ? 52.960  -77.024  -1.181  1.00 160.11 ? 51  LYS   C CD  1 
ATOM   4205  C  CE  . LYS   C  3  53  ? 52.575  -77.434  -2.588  1.00 156.97 ? 51  LYS   C CE  1 
ATOM   4206  N  NZ  . LYS   C  3  53  ? 51.164  -77.883  -2.657  1.00 154.95 ? 51  LYS   C NZ  1 
ATOM   4207  N  N   . LEU   C  3  54  ? 56.144  -79.903  1.241   1.00 135.31 ? 52  LEU   C N   1 
ATOM   4208  C  CA  . LEU   C  3  54  ? 57.070  -80.948  1.765   1.00 133.56 ? 52  LEU   C CA  1 
ATOM   4209  C  C   . LEU   C  3  54  ? 56.277  -82.192  2.200   1.00 132.03 ? 52  LEU   C C   1 
ATOM   4210  O  O   . LEU   C  3  54  ? 56.863  -83.041  2.904   1.00 129.21 ? 52  LEU   C O   1 
ATOM   4211  C  CB  . LEU   C  3  54  ? 57.897  -80.387  2.930   1.00 131.00 ? 52  LEU   C CB  1 
ATOM   4212  C  CG  . LEU   C  3  54  ? 59.346  -80.013  2.621   1.00 131.68 ? 52  LEU   C CG  1 
ATOM   4213  C  CD1 . LEU   C  3  54  ? 59.467  -79.229  1.322   1.00 131.85 ? 52  LEU   C CD1 1 
ATOM   4214  C  CD2 . LEU   C  3  54  ? 59.937  -79.223  3.778   1.00 130.98 ? 52  LEU   C CD2 1 
ATOM   4215  N  N   . GLN   C  3  55  ? 55.010  -82.317  1.784   1.00 131.00 ? 53  GLN   C N   1 
ATOM   4216  C  CA  . GLN   C  3  55  ? 54.183  -83.535  2.010   1.00 128.99 ? 53  GLN   C CA  1 
ATOM   4217  C  C   . GLN   C  3  55  ? 54.726  -84.689  1.159   1.00 131.68 ? 53  GLN   C C   1 
ATOM   4218  O  O   . GLN   C  3  55  ? 55.347  -84.413  0.112   1.00 124.81 ? 53  GLN   C O   1 
ATOM   4219  C  CB  . GLN   C  3  55  ? 52.713  -83.300  1.654   1.00 130.55 ? 53  GLN   C CB  1 
ATOM   4220  C  CG  . GLN   C  3  55  ? 51.902  -82.651  2.767   1.00 131.27 ? 53  GLN   C CG  1 
ATOM   4221  C  CD  . GLN   C  3  55  ? 50.683  -83.467  3.129   1.00 131.95 ? 53  GLN   C CD  1 
ATOM   4222  O  OE1 . GLN   C  3  55  ? 50.791  -84.592  3.616   1.00 136.03 ? 53  GLN   C OE1 1 
ATOM   4223  N  NE2 . GLN   C  3  55  ? 49.506  -82.909  2.898   1.00 130.61 ? 53  GLN   C NE2 1 
ATOM   4224  N  N   . ASP   C  3  56  ? 54.491  -85.928  1.606   1.00 130.75 ? 54  ASP   C N   1 
ATOM   4225  C  CA  . ASP   C  3  56  ? 54.729  -87.180  0.837   1.00 129.38 ? 54  ASP   C CA  1 
ATOM   4226  C  C   . ASP   C  3  56  ? 53.360  -87.788  0.509   1.00 122.37 ? 54  ASP   C C   1 
ATOM   4227  O  O   . ASP   C  3  56  ? 52.736  -88.359  1.420   1.00 121.07 ? 54  ASP   C O   1 
ATOM   4228  C  CB  . ASP   C  3  56  ? 55.641  -88.136  1.614   1.00 130.79 ? 54  ASP   C CB  1 
ATOM   4229  C  CG  . ASP   C  3  56  ? 56.200  -89.289  0.795   1.00 138.14 ? 54  ASP   C CG  1 
ATOM   4230  O  OD1 . ASP   C  3  56  ? 55.593  -89.627  -0.242  1.00 143.40 ? 54  ASP   C OD1 1 
ATOM   4231  O  OD2 . ASP   C  3  56  ? 57.240  -89.845  1.205   1.00 140.25 ? 54  ASP   C OD2 1 
ATOM   4232  N  N   . THR   C  3  57  ? 52.906  -87.643  -0.740  1.00 122.44 ? 55  THR   C N   1 
ATOM   4233  C  CA  . THR   C  3  57  ? 51.532  -87.993  -1.195  1.00 119.88 ? 55  THR   C CA  1 
ATOM   4234  C  C   . THR   C  3  57  ? 51.420  -89.493  -1.494  1.00 119.71 ? 55  THR   C C   1 
ATOM   4235  O  O   . THR   C  3  57  ? 50.280  -89.952  -1.693  1.00 123.79 ? 55  THR   C O   1 
ATOM   4236  C  CB  . THR   C  3  57  ? 51.115  -87.160  -2.414  1.00 119.22 ? 55  THR   C CB  1 
ATOM   4237  O  OG1 . THR   C  3  57  ? 52.227  -87.076  -3.307  1.00 115.72 ? 55  THR   C OG1 1 
ATOM   4238  C  CG2 . THR   C  3  57  ? 50.655  -85.770  -2.035  1.00 117.20 ? 55  THR   C CG2 1 
ATOM   4239  N  N   . ARG   C  3  58  ? 52.540  -90.223  -1.530  1.00 123.19 ? 56  ARG   C N   1 
ATOM   4240  C  CA  . ARG   C  3  58  ? 52.550  -91.702  -1.695  1.00 124.97 ? 56  ARG   C CA  1 
ATOM   4241  C  C   . ARG   C  3  58  ? 51.914  -92.345  -0.460  1.00 124.85 ? 56  ARG   C C   1 
ATOM   4242  O  O   . ARG   C  3  58  ? 51.072  -93.247  -0.629  1.00 123.01 ? 56  ARG   C O   1 
ATOM   4243  C  CB  . ARG   C  3  58  ? 53.967  -92.266  -1.836  1.00 127.23 ? 56  ARG   C CB  1 
ATOM   4244  C  CG  . ARG   C  3  58  ? 54.826  -91.633  -2.921  1.00 128.54 ? 56  ARG   C CG  1 
ATOM   4245  C  CD  . ARG   C  3  58  ? 56.211  -92.253  -2.901  1.00 132.03 ? 56  ARG   C CD  1 
ATOM   4246  N  NE  . ARG   C  3  58  ? 56.844  -92.084  -1.596  1.00 132.24 ? 56  ARG   C NE  1 
ATOM   4247  C  CZ  . ARG   C  3  58  ? 57.596  -92.990  -0.967  1.00 132.96 ? 56  ARG   C CZ  1 
ATOM   4248  N  NH1 . ARG   C  3  58  ? 57.830  -94.176  -1.507  1.00 133.52 ? 56  ARG   C NH1 1 
ATOM   4249  N  NH2 . ARG   C  3  58  ? 58.109  -92.704  0.218   1.00 130.53 ? 56  ARG   C NH2 1 
ATOM   4250  N  N   . ILE   C  3  59  ? 52.306  -91.875  0.729   1.00 125.92 ? 57  ILE   C N   1 
ATOM   4251  C  CA  . ILE   C  3  59  ? 52.076  -92.563  2.036   1.00 129.54 ? 57  ILE   C CA  1 
ATOM   4252  C  C   . ILE   C  3  59  ? 51.009  -91.834  2.863   1.00 132.40 ? 57  ILE   C C   1 
ATOM   4253  O  O   . ILE   C  3  59  ? 50.372  -92.511  3.696   1.00 138.45 ? 57  ILE   C O   1 
ATOM   4254  C  CB  . ILE   C  3  59  ? 53.399  -92.711  2.815   1.00 129.28 ? 57  ILE   C CB  1 
ATOM   4255  C  CG1 . ILE   C  3  59  ? 54.142  -91.379  2.958   1.00 127.24 ? 57  ILE   C CG1 1 
ATOM   4256  C  CG2 . ILE   C  3  59  ? 54.270  -93.779  2.171   1.00 135.29 ? 57  ILE   C CG2 1 
ATOM   4257  C  CD1 . ILE   C  3  59  ? 55.217  -91.381  4.020   1.00 126.32 ? 57  ILE   C CD1 1 
ATOM   4258  N  N   . THR   C  3  60  ? 50.825  -90.522  2.671   1.00 133.32 ? 58  THR   C N   1 
ATOM   4259  C  CA  . THR   C  3  60  ? 49.788  -89.719  3.377   1.00 134.07 ? 58  THR   C CA  1 
ATOM   4260  C  C   . THR   C  3  60  ? 48.424  -90.368  3.151   1.00 135.11 ? 58  THR   C C   1 
ATOM   4261  O  O   . THR   C  3  60  ? 48.070  -90.673  2.013   1.00 136.56 ? 58  THR   C O   1 
ATOM   4262  C  CB  . THR   C  3  60  ? 49.760  -88.255  2.916   1.00 137.42 ? 58  THR   C CB  1 
ATOM   4263  O  OG1 . THR   C  3  60  ? 50.973  -87.617  3.318   1.00 140.18 ? 58  THR   C OG1 1 
ATOM   4264  C  CG2 . THR   C  3  60  ? 48.583  -87.487  3.480   1.00 133.11 ? 58  THR   C CG2 1 
ATOM   4265  N  N   . PRO   C  3  61  ? 47.629  -90.610  4.220   1.00 134.02 ? 59  PRO   C N   1 
ATOM   4266  C  CA  . PRO   C  3  61  ? 46.266  -91.123  4.069   1.00 132.28 ? 59  PRO   C CA  1 
ATOM   4267  C  C   . PRO   C  3  61  ? 45.465  -90.374  2.992   1.00 131.79 ? 59  PRO   C C   1 
ATOM   4268  O  O   . PRO   C  3  61  ? 45.395  -89.157  3.059   1.00 132.88 ? 59  PRO   C O   1 
ATOM   4269  C  CB  . PRO   C  3  61  ? 45.653  -90.897  5.461   1.00 130.22 ? 59  PRO   C CB  1 
ATOM   4270  C  CG  . PRO   C  3  61  ? 46.832  -90.991  6.406   1.00 129.47 ? 59  PRO   C CG  1 
ATOM   4271  C  CD  . PRO   C  3  61  ? 48.009  -90.435  5.631   1.00 132.63 ? 59  PRO   C CD  1 
ATOM   4272  N  N   . SER   C  3  62  ? 44.902  -91.109  2.025   1.00 132.26 ? 60  SER   C N   1 
ATOM   4273  C  CA  . SER   C  3  62  ? 44.023  -90.568  0.954   1.00 127.19 ? 60  SER   C CA  1 
ATOM   4274  C  C   . SER   C  3  62  ? 42.684  -90.147  1.569   1.00 118.78 ? 60  SER   C C   1 
ATOM   4275  O  O   . SER   C  3  62  ? 42.294  -90.737  2.593   1.00 122.72 ? 60  SER   C O   1 
ATOM   4276  C  CB  . SER   C  3  62  ? 43.825  -91.561  -0.160  1.00 129.93 ? 60  SER   C CB  1 
ATOM   4277  O  OG  . SER   C  3  62  ? 43.095  -90.972  -1.226  1.00 130.43 ? 60  SER   C OG  1 
ATOM   4278  N  N   . LYS   C  3  63  ? 42.007  -89.170  0.961   1.00 118.61 ? 61  LYS   C N   1 
ATOM   4279  C  CA  . LYS   C  3  63  ? 40.770  -88.558  1.517   1.00 119.72 ? 61  LYS   C CA  1 
ATOM   4280  C  C   . LYS   C  3  63  ? 39.570  -89.467  1.222   1.00 110.31 ? 61  LYS   C C   1 
ATOM   4281  O  O   . LYS   C  3  63  ? 38.629  -89.473  2.040   1.00 109.10 ? 61  LYS   C O   1 
ATOM   4282  C  CB  . LYS   C  3  63  ? 40.561  -87.146  0.958   1.00 125.72 ? 61  LYS   C CB  1 
ATOM   4283  C  CG  . LYS   C  3  63  ? 39.930  -86.162  1.936   1.00 131.10 ? 61  LYS   C CG  1 
ATOM   4284  C  CD  . LYS   C  3  63  ? 40.939  -85.443  2.814   1.00 130.33 ? 61  LYS   C CD  1 
ATOM   4285  C  CE  . LYS   C  3  63  ? 40.390  -85.034  4.166   1.00 130.69 ? 61  LYS   C CE  1 
ATOM   4286  N  NZ  . LYS   C  3  63  ? 39.116  -84.284  4.053   1.00 130.29 ? 61  LYS   C NZ  1 
ATOM   4287  N  N   . VAL   C  3  64  ? 39.603  -90.195  0.099   1.00 105.97 ? 62  VAL   C N   1 
ATOM   4288  C  CA  . VAL   C  3  64  ? 38.561  -91.190  -0.298  1.00 104.52 ? 62  VAL   C CA  1 
ATOM   4289  C  C   . VAL   C  3  64  ? 39.073  -92.591  0.049   1.00 100.98 ? 62  VAL   C C   1 
ATOM   4290  O  O   . VAL   C  3  64  ? 40.164  -92.952  -0.431  1.00 102.27 ? 62  VAL   C O   1 
ATOM   4291  C  CB  . VAL   C  3  64  ? 38.209  -91.077  -1.795  1.00 105.42 ? 62  VAL   C CB  1 
ATOM   4292  C  CG1 . VAL   C  3  64  ? 37.177  -92.114  -2.216  1.00 105.23 ? 62  VAL   C CG1 1 
ATOM   4293  C  CG2 . VAL   C  3  64  ? 37.734  -89.678  -2.156  1.00 105.45 ? 62  VAL   C CG2 1 
ATOM   4294  N  N   . SER   C  3  65  ? 38.306  -93.347  0.841   1.00 99.20  ? 63  SER   C N   1 
ATOM   4295  C  CA  . SER   C  3  65  ? 38.640  -94.722  1.297   1.00 100.37 ? 63  SER   C CA  1 
ATOM   4296  C  C   . SER   C  3  65  ? 37.692  -95.735  0.650   1.00 98.38  ? 63  SER   C C   1 
ATOM   4297  O  O   . SER   C  3  65  ? 36.494  -95.417  0.509   1.00 98.35  ? 63  SER   C O   1 
ATOM   4298  C  CB  . SER   C  3  65  ? 38.586  -94.829  2.797   1.00 100.98 ? 63  SER   C CB  1 
ATOM   4299  O  OG  . SER   C  3  65  ? 39.405  -93.843  3.406   1.00 103.14 ? 63  SER   C OG  1 
ATOM   4300  N  N   . LYS   C  3  66  ? 38.219  -96.907  0.280   1.00 97.72  ? 64  LYS   C N   1 
ATOM   4301  C  CA  . LYS   C  3  66  ? 37.422  -98.086  -0.144  1.00 95.91  ? 64  LYS   C CA  1 
ATOM   4302  C  C   . LYS   C  3  66  ? 36.913  -98.786  1.120   1.00 92.09  ? 64  LYS   C C   1 
ATOM   4303  O  O   . LYS   C  3  66  ? 37.739  -99.046  2.012   1.00 90.11  ? 64  LYS   C O   1 
ATOM   4304  C  CB  . LYS   C  3  66  ? 38.265  -99.027  -1.012  1.00 99.08  ? 64  LYS   C CB  1 
ATOM   4305  C  CG  . LYS   C  3  66  ? 38.510  -98.547  -2.437  1.00 101.47 ? 64  LYS   C CG  1 
ATOM   4306  C  CD  . LYS   C  3  66  ? 39.426  -99.451  -3.238  1.00 105.49 ? 64  LYS   C CD  1 
ATOM   4307  C  CE  . LYS   C  3  66  ? 38.773  -100.754 -3.648  1.00 107.00 ? 64  LYS   C CE  1 
ATOM   4308  N  NZ  . LYS   C  3  66  ? 39.747  -101.672 -4.282  1.00 110.89 ? 64  LYS   C NZ  1 
ATOM   4309  N  N   . ILE   C  3  67  ? 35.602  -99.029  1.206   1.00 91.97  ? 65  ILE   C N   1 
ATOM   4310  C  CA  . ILE   C  3  67  ? 34.951  -99.823  2.294   1.00 94.89  ? 65  ILE   C CA  1 
ATOM   4311  C  C   . ILE   C  3  67  ? 34.844  -101.285 1.841   1.00 98.75  ? 65  ILE   C C   1 
ATOM   4312  O  O   . ILE   C  3  67  ? 35.059  -102.190 2.673   1.00 101.21 ? 65  ILE   C O   1 
ATOM   4313  C  CB  . ILE   C  3  67  ? 33.574  -99.233  2.655   1.00 91.09  ? 65  ILE   C CB  1 
ATOM   4314  C  CG1 . ILE   C  3  67  ? 33.672  -97.756  3.045   1.00 89.46  ? 65  ILE   C CG1 1 
ATOM   4315  C  CG2 . ILE   C  3  67  ? 32.903  -100.057 3.742   1.00 91.68  ? 65  ILE   C CG2 1 
ATOM   4316  C  CD1 . ILE   C  3  67  ? 34.686  -97.465  4.130   1.00 88.88  ? 65  ILE   C CD1 1 
ATOM   4317  N  N   . ASP   C  3  68  ? 34.474  -101.491 0.576   1.00 103.94 ? 66  ASP   C N   1 
ATOM   4318  C  CA  . ASP   C  3  68  ? 34.561  -102.787 -0.148  1.00 108.12 ? 66  ASP   C CA  1 
ATOM   4319  C  C   . ASP   C  3  68  ? 35.048  -102.462 -1.568  1.00 109.80 ? 66  ASP   C C   1 
ATOM   4320  O  O   . ASP   C  3  68  ? 35.354  -101.278 -1.828  1.00 114.88 ? 66  ASP   C O   1 
ATOM   4321  C  CB  . ASP   C  3  68  ? 33.218  -103.528 -0.097  1.00 108.22 ? 66  ASP   C CB  1 
ATOM   4322  C  CG  . ASP   C  3  68  ? 33.308  -105.049 -0.038  1.00 107.40 ? 66  ASP   C CG  1 
ATOM   4323  O  OD1 . ASP   C  3  68  ? 34.338  -105.604 -0.479  1.00 108.25 ? 66  ASP   C OD1 1 
ATOM   4324  O  OD2 . ASP   C  3  68  ? 32.336  -105.675 0.448   1.00 95.49  ? 66  ASP   C OD2 1 
ATOM   4325  N  N   . SER   C  3  69  ? 35.126  -103.456 -2.456  1.00 106.66 ? 67  SER   C N   1 
ATOM   4326  C  CA  . SER   C  3  69  ? 35.612  -103.285 -3.850  1.00 104.49 ? 67  SER   C CA  1 
ATOM   4327  C  C   . SER   C  3  69  ? 34.618  -102.455 -4.678  1.00 101.49 ? 67  SER   C C   1 
ATOM   4328  O  O   . SER   C  3  69  ? 35.017  -102.001 -5.769  1.00 99.38  ? 67  SER   C O   1 
ATOM   4329  C  CB  . SER   C  3  69  ? 35.885  -104.619 -4.493  1.00 106.09 ? 67  SER   C CB  1 
ATOM   4330  O  OG  . SER   C  3  69  ? 34.705  -105.406 -4.550  1.00 107.11 ? 67  SER   C OG  1 
ATOM   4331  N  N   . HIS   C  3  70  ? 33.387  -102.252 -4.183  1.00 97.93  ? 68  HIS   C N   1 
ATOM   4332  C  CA  . HIS   C  3  70  ? 32.264  -101.616 -4.932  1.00 97.11  ? 68  HIS   C CA  1 
ATOM   4333  C  C   . HIS   C  3  70  ? 31.756  -100.327 -4.263  1.00 95.58  ? 68  HIS   C C   1 
ATOM   4334  O  O   . HIS   C  3  70  ? 30.980  -99.618  -4.932  1.00 94.52  ? 68  HIS   C O   1 
ATOM   4335  C  CB  . HIS   C  3  70  ? 31.117  -102.617 -5.135  1.00 95.45  ? 68  HIS   C CB  1 
ATOM   4336  C  CG  . HIS   C  3  70  ? 30.375  -102.967 -3.889  1.00 93.87  ? 68  HIS   C CG  1 
ATOM   4337  N  ND1 . HIS   C  3  70  ? 30.961  -103.673 -2.858  1.00 98.61  ? 68  HIS   C ND1 1 
ATOM   4338  C  CD2 . HIS   C  3  70  ? 29.098  -102.740 -3.514  1.00 89.97  ? 68  HIS   C CD2 1 
ATOM   4339  C  CE1 . HIS   C  3  70  ? 30.080  -103.853 -1.895  1.00 98.12  ? 68  HIS   C CE1 1 
ATOM   4340  N  NE2 . HIS   C  3  70  ? 28.929  -103.286 -2.273  1.00 92.45  ? 68  HIS   C NE2 1 
ATOM   4341  N  N   . VAL   C  3  71  ? 32.144  -100.029 -3.015  1.00 95.56  ? 69  VAL   C N   1 
ATOM   4342  C  CA  . VAL   C  3  71  ? 31.675  -98.823  -2.260  1.00 95.41  ? 69  VAL   C CA  1 
ATOM   4343  C  C   . VAL   C  3  71  ? 32.888  -98.022  -1.771  1.00 94.43  ? 69  VAL   C C   1 
ATOM   4344  O  O   . VAL   C  3  71  ? 33.893  -98.645  -1.379  1.00 94.27  ? 69  VAL   C O   1 
ATOM   4345  C  CB  . VAL   C  3  71  ? 30.760  -99.196  -1.075  1.00 96.76  ? 69  VAL   C CB  1 
ATOM   4346  C  CG1 . VAL   C  3  71  ? 30.038  -97.981  -0.513  1.00 95.12  ? 69  VAL   C CG1 1 
ATOM   4347  C  CG2 . VAL   C  3  71  ? 29.758  -100.276 -1.445  1.00 100.77 ? 69  VAL   C CG2 1 
ATOM   4348  N  N   . VAL   C  3  72  ? 32.773  -96.690  -1.772  1.00 92.79  ? 70  VAL   C N   1 
ATOM   4349  C  CA  . VAL   C  3  72  ? 33.826  -95.744  -1.290  1.00 93.24  ? 70  VAL   C CA  1 
ATOM   4350  C  C   . VAL   C  3  72  ? 33.209  -94.760  -0.291  1.00 91.30  ? 70  VAL   C C   1 
ATOM   4351  O  O   . VAL   C  3  72  ? 31.990  -94.504  -0.368  1.00 85.85  ? 70  VAL   C O   1 
ATOM   4352  C  CB  . VAL   C  3  72  ? 34.512  -94.992  -2.447  1.00 94.15  ? 70  VAL   C CB  1 
ATOM   4353  C  CG1 . VAL   C  3  72  ? 35.576  -95.848  -3.112  1.00 96.85  ? 70  VAL   C CG1 1 
ATOM   4354  C  CG2 . VAL   C  3  72  ? 33.517  -94.467  -3.472  1.00 94.27  ? 70  VAL   C CG2 1 
ATOM   4355  N  N   . LEU   C  3  73  ? 34.047  -94.225  0.600   1.00 91.46  ? 71  LEU   C N   1 
ATOM   4356  C  CA  . LEU   C  3  73  ? 33.663  -93.253  1.655   1.00 93.89  ? 71  LEU   C CA  1 
ATOM   4357  C  C   . LEU   C  3  73  ? 34.666  -92.094  1.671   1.00 93.29  ? 71  LEU   C C   1 
ATOM   4358  O  O   . LEU   C  3  73  ? 35.861  -92.349  1.922   1.00 96.00  ? 71  LEU   C O   1 
ATOM   4359  C  CB  . LEU   C  3  73  ? 33.635  -93.977  3.004   1.00 91.95  ? 71  LEU   C CB  1 
ATOM   4360  C  CG  . LEU   C  3  73  ? 33.084  -93.168  4.179   1.00 92.36  ? 71  LEU   C CG  1 
ATOM   4361  C  CD1 . LEU   C  3  73  ? 32.338  -94.064  5.155   1.00 91.54  ? 71  LEU   C CD1 1 
ATOM   4362  C  CD2 . LEU   C  3  73  ? 34.191  -92.412  4.899   1.00 92.22  ? 71  LEU   C CD2 1 
ATOM   4363  N  N   . SER   C  3  74  ? 34.191  -90.874  1.404   1.00 95.70  ? 72  SER   C N   1 
ATOM   4364  C  CA  . SER   C  3  74  ? 34.915  -89.602  1.661   1.00 94.59  ? 72  SER   C CA  1 
ATOM   4365  C  C   . SER   C  3  74  ? 34.229  -88.885  2.825   1.00 90.24  ? 72  SER   C C   1 
ATOM   4366  O  O   . SER   C  3  74  ? 33.062  -89.215  3.114   1.00 85.53  ? 72  SER   C O   1 
ATOM   4367  C  CB  . SER   C  3  74  ? 34.981  -88.728  0.435   1.00 98.06  ? 72  SER   C CB  1 
ATOM   4368  O  OG  . SER   C  3  74  ? 33.709  -88.187  0.115   1.00 102.72 ? 72  SER   C OG  1 
ATOM   4369  N  N   . PHE   C  3  75  ? 34.927  -87.946  3.463   1.00 90.59  ? 73  PHE   C N   1 
ATOM   4370  C  CA  . PHE   C  3  75  ? 34.457  -87.268  4.696   1.00 92.19  ? 73  PHE   C CA  1 
ATOM   4371  C  C   . PHE   C  3  75  ? 34.969  -85.824  4.759   1.00 92.33  ? 73  PHE   C C   1 
ATOM   4372  O  O   . PHE   C  3  75  ? 35.896  -85.450  4.009   1.00 88.60  ? 73  PHE   C O   1 
ATOM   4373  C  CB  . PHE   C  3  75  ? 34.922  -88.046  5.929   1.00 91.34  ? 73  PHE   C CB  1 
ATOM   4374  C  CG  . PHE   C  3  75  ? 36.403  -87.950  6.191   1.00 92.17  ? 73  PHE   C CG  1 
ATOM   4375  C  CD1 . PHE   C  3  75  ? 37.294  -88.804  5.560   1.00 94.18  ? 73  PHE   C CD1 1 
ATOM   4376  C  CD2 . PHE   C  3  75  ? 36.910  -86.988  7.050   1.00 94.15  ? 73  PHE   C CD2 1 
ATOM   4377  C  CE1 . PHE   C  3  75  ? 38.657  -88.707  5.794   1.00 95.50  ? 73  PHE   C CE1 1 
ATOM   4378  C  CE2 . PHE   C  3  75  ? 38.274  -86.892  7.281   1.00 93.84  ? 73  PHE   C CE2 1 
ATOM   4379  C  CZ  . PHE   C  3  75  ? 39.146  -87.750  6.653   1.00 94.63  ? 73  PHE   C CZ  1 
ATOM   4380  N  N   . SER   C  3  76  ? 34.360  -85.047  5.657   1.00 94.31  ? 74  SER   C N   1 
ATOM   4381  C  CA  . SER   C  3  76  ? 34.815  -83.706  6.102   1.00 98.48  ? 74  SER   C CA  1 
ATOM   4382  C  C   . SER   C  3  76  ? 34.826  -83.678  7.633   1.00 95.29  ? 74  SER   C C   1 
ATOM   4383  O  O   . SER   C  3  76  ? 33.837  -84.139  8.237   1.00 95.50  ? 74  SER   C O   1 
ATOM   4384  C  CB  . SER   C  3  76  ? 33.943  -82.611  5.537   1.00 103.00 ? 74  SER   C CB  1 
ATOM   4385  O  OG  . SER   C  3  76  ? 34.263  -82.351  4.177   1.00 110.44 ? 74  SER   C OG  1 
ATOM   4386  N  N   . GLY   C  3  77  ? 35.910  -83.176  8.229   1.00 94.28  ? 75  GLY   C N   1 
ATOM   4387  C  CA  . GLY   C  3  77  ? 36.022  -82.955  9.682   1.00 93.76  ? 75  GLY   C CA  1 
ATOM   4388  C  C   . GLY   C  3  77  ? 37.311  -83.522  10.241  1.00 94.45  ? 75  GLY   C C   1 
ATOM   4389  O  O   . GLY   C  3  77  ? 38.344  -83.427  9.547   1.00 95.05  ? 75  GLY   C O   1 
ATOM   4390  N  N   . LEU   C  3  78  ? 37.248  -84.089  11.451  1.00 96.27  ? 76  LEU   C N   1 
ATOM   4391  C  CA  . LEU   C  3  78  ? 38.417  -84.635  12.195  1.00 97.39  ? 76  LEU   C CA  1 
ATOM   4392  C  C   . LEU   C  3  78  ? 38.891  -85.927  11.521  1.00 95.61  ? 76  LEU   C C   1 
ATOM   4393  O  O   . LEU   C  3  78  ? 38.094  -86.881  11.442  1.00 92.83  ? 76  LEU   C O   1 
ATOM   4394  C  CB  . LEU   C  3  78  ? 38.024  -84.889  13.654  1.00 99.07  ? 76  LEU   C CB  1 
ATOM   4395  C  CG  . LEU   C  3  78  ? 37.633  -83.652  14.460  1.00 100.12 ? 76  LEU   C CG  1 
ATOM   4396  C  CD1 . LEU   C  3  78  ? 37.022  -84.049  15.794  1.00 99.98  ? 76  LEU   C CD1 1 
ATOM   4397  C  CD2 . LEU   C  3  78  ? 38.831  -82.739  14.677  1.00 102.60 ? 76  LEU   C CD2 1 
ATOM   4398  N  N   . ASN   C  3  79  ? 40.148  -85.945  11.070  1.00 96.25  ? 77  ASN   C N   1 
ATOM   4399  C  CA  . ASN   C  3  79  ? 40.760  -87.055  10.292  1.00 97.16  ? 77  ASN   C CA  1 
ATOM   4400  C  C   . ASN   C  3  79  ? 40.846  -88.310  11.169  1.00 97.01  ? 77  ASN   C C   1 
ATOM   4401  O  O   . ASN   C  3  79  ? 40.474  -89.396  10.680  1.00 93.48  ? 77  ASN   C O   1 
ATOM   4402  C  CB  . ASN   C  3  79  ? 42.138  -86.667  9.748   1.00 101.33 ? 77  ASN   C CB  1 
ATOM   4403  C  CG  . ASN   C  3  79  ? 42.091  -85.750  8.542   1.00 104.41 ? 77  ASN   C CG  1 
ATOM   4404  O  OD1 . ASN   C  3  79  ? 43.049  -85.698  7.776   1.00 111.24 ? 77  ASN   C OD1 1 
ATOM   4405  N  ND2 . ASN   C  3  79  ? 41.001  -85.020  8.353   1.00 109.08 ? 77  ASN   C ND2 1 
ATOM   4406  N  N   . ALA   C  3  80  ? 41.318  -88.162  12.411  1.00 94.98  ? 78  ALA   C N   1 
ATOM   4407  C  CA  . ALA   C  3  80  ? 41.497  -89.259  13.391  1.00 94.22  ? 78  ALA   C CA  1 
ATOM   4408  C  C   . ALA   C  3  80  ? 40.157  -89.956  13.660  1.00 95.93  ? 78  ALA   C C   1 
ATOM   4409  O  O   . ALA   C  3  80  ? 40.151  -91.201  13.762  1.00 95.66  ? 78  ALA   C O   1 
ATOM   4410  C  CB  . ALA   C  3  80  ? 42.105  -88.723  14.662  1.00 93.35  ? 78  ALA   C CB  1 
ATOM   4411  N  N   . ASP   C  3  81  ? 39.070  -89.183  13.772  1.00 97.16  ? 79  ASP   C N   1 
ATOM   4412  C  CA  . ASP   C  3  81  ? 37.688  -89.691  14.000  1.00 96.47  ? 79  ASP   C CA  1 
ATOM   4413  C  C   . ASP   C  3  81  ? 37.239  -90.558  12.818  1.00 95.93  ? 79  ASP   C C   1 
ATOM   4414  O  O   . ASP   C  3  81  ? 36.595  -91.592  13.071  1.00 100.80 ? 79  ASP   C O   1 
ATOM   4415  C  CB  . ASP   C  3  81  ? 36.680  -88.554  14.202  1.00 96.45  ? 79  ASP   C CB  1 
ATOM   4416  C  CG  . ASP   C  3  81  ? 36.584  -88.043  15.629  1.00 95.78  ? 79  ASP   C CG  1 
ATOM   4417  O  OD1 . ASP   C  3  81  ? 37.435  -88.431  16.456  1.00 97.36  ? 79  ASP   C OD1 1 
ATOM   4418  O  OD2 . ASP   C  3  81  ? 35.650  -87.262  15.906  1.00 93.13  ? 79  ASP   C OD2 1 
ATOM   4419  N  N   . SER   C  3  82  ? 37.543  -90.144  11.583  1.00 93.14  ? 80  SER   C N   1 
ATOM   4420  C  CA  . SER   C  3  82  ? 37.064  -90.800  10.336  1.00 94.40  ? 80  SER   C CA  1 
ATOM   4421  C  C   . SER   C  3  82  ? 37.604  -92.234  10.235  1.00 93.34  ? 80  SER   C C   1 
ATOM   4422  O  O   . SER   C  3  82  ? 36.870  -93.093  9.712   1.00 88.50  ? 80  SER   C O   1 
ATOM   4423  C  CB  . SER   C  3  82  ? 37.417  -89.992  9.113   1.00 97.13  ? 80  SER   C CB  1 
ATOM   4424  O  OG  . SER   C  3  82  ? 38.817  -90.009  8.873   1.00 99.32  ? 80  SER   C OG  1 
ATOM   4425  N  N   . ARG   C  3  83  ? 38.827  -92.479  10.722  1.00 95.43  ? 81  ARG   C N   1 
ATOM   4426  C  CA  . ARG   C  3  83  ? 39.497  -93.808  10.671  1.00 95.55  ? 81  ARG   C CA  1 
ATOM   4427  C  C   . ARG   C  3  83  ? 38.672  -94.835  11.455  1.00 95.02  ? 81  ARG   C C   1 
ATOM   4428  O  O   . ARG   C  3  83  ? 38.601  -95.996  11.001  1.00 96.46  ? 81  ARG   C O   1 
ATOM   4429  C  CB  . ARG   C  3  83  ? 40.924  -93.744  11.226  1.00 98.35  ? 81  ARG   C CB  1 
ATOM   4430  C  CG  . ARG   C  3  83  ? 41.919  -93.041  10.313  1.00 99.97  ? 81  ARG   C CG  1 
ATOM   4431  C  CD  . ARG   C  3  83  ? 43.346  -93.482  10.582  1.00 101.92 ? 81  ARG   C CD  1 
ATOM   4432  N  NE  . ARG   C  3  83  ? 43.687  -93.405  11.998  1.00 102.96 ? 81  ARG   C NE  1 
ATOM   4433  C  CZ  . ARG   C  3  83  ? 44.060  -92.302  12.644  1.00 103.89 ? 81  ARG   C CZ  1 
ATOM   4434  N  NH1 . ARG   C  3  83  ? 44.153  -91.144  12.009  1.00 106.28 ? 81  ARG   C NH1 1 
ATOM   4435  N  NH2 . ARG   C  3  83  ? 44.341  -92.363  13.934  1.00 102.06 ? 81  ARG   C NH2 1 
ATOM   4436  N  N   . ILE   C  3  84  ? 38.085  -94.429  12.585  1.00 90.03  ? 82  ILE   C N   1 
ATOM   4437  C  CA  . ILE   C  3  84  ? 37.253  -95.314  13.454  1.00 90.73  ? 82  ILE   C CA  1 
ATOM   4438  C  C   . ILE   C  3  84  ? 35.975  -95.697  12.694  1.00 93.50  ? 82  ILE   C C   1 
ATOM   4439  O  O   . ILE   C  3  84  ? 35.590  -96.882  12.767  1.00 99.72  ? 82  ILE   C O   1 
ATOM   4440  C  CB  . ILE   C  3  84  ? 36.962  -94.664  14.825  1.00 88.87  ? 82  ILE   C CB  1 
ATOM   4441  C  CG1 . ILE   C  3  84  ? 38.119  -94.875  15.807  1.00 89.70  ? 82  ILE   C CG1 1 
ATOM   4442  C  CG2 . ILE   C  3  84  ? 35.655  -95.175  15.414  1.00 87.94  ? 82  ILE   C CG2 1 
ATOM   4443  C  CD1 . ILE   C  3  84  ? 39.432  -94.261  15.378  1.00 90.88  ? 82  ILE   C CD1 1 
ATOM   4444  N  N   . LEU   C  3  85  ? 35.345  -94.751  11.988  1.00 91.43  ? 83  LEU   C N   1 
ATOM   4445  C  CA  . LEU   C  3  85  ? 34.108  -95.008  11.195  1.00 91.75  ? 83  LEU   C CA  1 
ATOM   4446  C  C   . LEU   C  3  85  ? 34.427  -95.920  10.001  1.00 91.13  ? 83  LEU   C C   1 
ATOM   4447  O  O   . LEU   C  3  85  ? 33.628  -96.838  9.738   1.00 90.11  ? 83  LEU   C O   1 
ATOM   4448  C  CB  . LEU   C  3  85  ? 33.494  -93.687  10.719  1.00 93.13  ? 83  LEU   C CB  1 
ATOM   4449  C  CG  . LEU   C  3  85  ? 32.660  -92.915  11.743  1.00 91.68  ? 83  LEU   C CG  1 
ATOM   4450  C  CD1 . LEU   C  3  85  ? 32.074  -91.666  11.109  1.00 93.70  ? 83  LEU   C CD1 1 
ATOM   4451  C  CD2 . LEU   C  3  85  ? 31.542  -93.769  12.328  1.00 90.57  ? 83  LEU   C CD2 1 
ATOM   4452  N  N   . ILE   C  3  86  ? 35.539  -95.665  9.302   1.00 92.12  ? 84  ILE   C N   1 
ATOM   4453  C  CA  . ILE   C  3  86  ? 35.982  -96.443  8.105   1.00 91.80  ? 84  ILE   C CA  1 
ATOM   4454  C  C   . ILE   C  3  86  ? 36.277  -97.887  8.525   1.00 93.62  ? 84  ILE   C C   1 
ATOM   4455  O  O   . ILE   C  3  86  ? 35.847  -98.803  7.797   1.00 93.34  ? 84  ILE   C O   1 
ATOM   4456  C  CB  . ILE   C  3  86  ? 37.204  -95.788  7.430   1.00 92.62  ? 84  ILE   C CB  1 
ATOM   4457  C  CG1 . ILE   C  3  86  ? 36.836  -94.450  6.787   1.00 95.31  ? 84  ILE   C CG1 1 
ATOM   4458  C  CG2 . ILE   C  3  86  ? 37.839  -96.732  6.418   1.00 91.56  ? 84  ILE   C CG2 1 
ATOM   4459  C  CD1 . ILE   C  3  86  ? 38.018  -93.543  6.536   1.00 99.80  ? 84  ILE   C CD1 1 
ATOM   4460  N  N   . GLU   C  3  87  ? 37.001  -98.076  9.633   1.00 92.51  ? 85  GLU   C N   1 
ATOM   4461  C  CA  . GLU   C  3  87  ? 37.395  -99.416  10.146  1.00 94.89  ? 85  GLU   C CA  1 
ATOM   4462  C  C   . GLU   C  3  87  ? 36.132  -100.244 10.407  1.00 90.93  ? 85  GLU   C C   1 
ATOM   4463  O  O   . GLU   C  3  87  ? 36.042  -101.351 9.854   1.00 92.11  ? 85  GLU   C O   1 
ATOM   4464  C  CB  . GLU   C  3  87  ? 38.244  -99.297  11.412  1.00 97.60  ? 85  GLU   C CB  1 
ATOM   4465  C  CG  . GLU   C  3  87  ? 38.631  -100.641 12.007  1.00 100.33 ? 85  GLU   C CG  1 
ATOM   4466  C  CD  . GLU   C  3  87  ? 39.358  -101.579 11.057  1.00 106.21 ? 85  GLU   C CD  1 
ATOM   4467  O  OE1 . GLU   C  3  87  ? 39.221  -102.809 11.227  1.00 107.83 ? 85  GLU   C OE1 1 
ATOM   4468  O  OE2 . GLU   C  3  87  ? 40.061  -101.079 10.149  1.00 106.53 ? 85  GLU   C OE2 1 
ATOM   4469  N  N   . LYS   C  3  88  ? 35.198  -99.717  11.203  1.00 86.83  ? 86  LYS   C N   1 
ATOM   4470  C  CA  . LYS   C  3  88  ? 33.912  -100.382 11.550  1.00 87.23  ? 86  LYS   C CA  1 
ATOM   4471  C  C   . LYS   C  3  88  ? 33.120  -100.720 10.281  1.00 90.42  ? 86  LYS   C C   1 
ATOM   4472  O  O   . LYS   C  3  88  ? 32.543  -101.825 10.230  1.00 95.21  ? 86  LYS   C O   1 
ATOM   4473  C  CB  . LYS   C  3  88  ? 33.067  -99.491  12.463  1.00 84.21  ? 86  LYS   C CB  1 
ATOM   4474  C  CG  . LYS   C  3  88  ? 33.564  -99.396  13.895  1.00 84.14  ? 86  LYS   C CG  1 
ATOM   4475  C  CD  . LYS   C  3  88  ? 32.701  -98.515  14.759  1.00 83.36  ? 86  LYS   C CD  1 
ATOM   4476  C  CE  . LYS   C  3  88  ? 33.330  -98.226  16.103  1.00 85.34  ? 86  LYS   C CE  1 
ATOM   4477  N  NZ  . LYS   C  3  88  ? 33.497  -99.461  16.904  1.00 87.69  ? 86  LYS   C NZ  1 
ATOM   4478  N  N   . ALA   C  3  89  ? 33.077  -99.800  9.312   1.00 89.24  ? 87  ALA   C N   1 
ATOM   4479  C  CA  . ALA   C  3  89  ? 32.362  -99.955  8.022   1.00 90.59  ? 87  ALA   C CA  1 
ATOM   4480  C  C   . ALA   C  3  89  ? 32.960  -101.129 7.235   1.00 88.50  ? 87  ALA   C C   1 
ATOM   4481  O  O   . ALA   C  3  89  ? 32.181  -101.950 6.713   1.00 89.12  ? 87  ALA   C O   1 
ATOM   4482  C  CB  . ALA   C  3  89  ? 32.422  -98.668  7.231   1.00 91.47  ? 87  ALA   C CB  1 
ATOM   4483  N  N   . ARG   C  3  90  ? 34.293  -101.205 7.166   1.00 86.84  ? 88  ARG   C N   1 
ATOM   4484  C  CA  . ARG   C  3  90  ? 35.046  -102.253 6.423   1.00 87.16  ? 88  ARG   C CA  1 
ATOM   4485  C  C   . ARG   C  3  90  ? 34.823  -103.630 7.061   1.00 87.06  ? 88  ARG   C C   1 
ATOM   4486  O  O   . ARG   C  3  90  ? 34.772  -104.618 6.301   1.00 86.62  ? 88  ARG   C O   1 
ATOM   4487  C  CB  . ARG   C  3  90  ? 36.538  -101.913 6.386   1.00 89.23  ? 88  ARG   C CB  1 
ATOM   4488  C  CG  . ARG   C  3  90  ? 36.891  -100.807 5.404   1.00 89.33  ? 88  ARG   C CG  1 
ATOM   4489  C  CD  . ARG   C  3  90  ? 38.311  -100.318 5.592   1.00 89.35  ? 88  ARG   C CD  1 
ATOM   4490  N  NE  . ARG   C  3  90  ? 38.788  -99.571  4.438   1.00 89.74  ? 88  ARG   C NE  1 
ATOM   4491  C  CZ  . ARG   C  3  90  ? 39.915  -98.869  4.397   1.00 90.98  ? 88  ARG   C CZ  1 
ATOM   4492  N  NH1 . ARG   C  3  90  ? 40.699  -98.794  5.461   1.00 90.59  ? 88  ARG   C NH1 1 
ATOM   4493  N  NH2 . ARG   C  3  90  ? 40.253  -98.233  3.287   1.00 93.15  ? 88  ARG   C NH2 1 
ATOM   4494  N  N   . VAL   C  3  91  ? 34.716  -103.692 8.393   1.00 85.43  ? 89  VAL   C N   1 
ATOM   4495  C  CA  . VAL   C  3  91  ? 34.493  -104.952 9.166   1.00 85.67  ? 89  VAL   C CA  1 
ATOM   4496  C  C   . VAL   C  3  91  ? 33.049  -105.416 8.945   1.00 85.60  ? 89  VAL   C C   1 
ATOM   4497  O  O   . VAL   C  3  91  ? 32.846  -106.631 8.804   1.00 87.65  ? 89  VAL   C O   1 
ATOM   4498  C  CB  . VAL   C  3  91  ? 34.804  -104.780 10.667  1.00 85.27  ? 89  VAL   C CB  1 
ATOM   4499  C  CG1 . VAL   C  3  91  ? 34.388  -105.998 11.477  1.00 84.69  ? 89  VAL   C CG1 1 
ATOM   4500  C  CG2 . VAL   C  3  91  ? 36.275  -104.474 10.906  1.00 85.78  ? 89  VAL   C CG2 1 
ATOM   4501  N  N   . GLU   C  3  92  ? 32.086  -104.492 8.934   1.00 82.41  ? 90  GLU   C N   1 
ATOM   4502  C  CA  . GLU   C  3  92  ? 30.656  -104.801 8.667   1.00 82.79  ? 90  GLU   C CA  1 
ATOM   4503  C  C   . GLU   C  3  92  ? 30.498  -105.275 7.216   1.00 83.41  ? 90  GLU   C C   1 
ATOM   4504  O  O   . GLU   C  3  92  ? 29.630  -106.136 6.968   1.00 81.14  ? 90  GLU   C O   1 
ATOM   4505  C  CB  . GLU   C  3  92  ? 29.779  -103.578 8.941   1.00 82.64  ? 90  GLU   C CB  1 
ATOM   4506  C  CG  . GLU   C  3  92  ? 28.299  -103.823 8.699   1.00 84.29  ? 90  GLU   C CG  1 
ATOM   4507  C  CD  . GLU   C  3  92  ? 27.688  -104.931 9.536   1.00 85.37  ? 90  GLU   C CD  1 
ATOM   4508  O  OE1 . GLU   C  3  92  ? 26.692  -105.525 9.082   1.00 88.70  ? 90  GLU   C OE1 1 
ATOM   4509  O  OE2 . GLU   C  3  92  ? 28.210  -105.196 10.639  1.00 87.15  ? 90  GLU   C OE2 1 
ATOM   4510  N  N   . ALA   C  3  93  ? 31.298  -104.723 6.298   1.00 85.29  ? 91  ALA   C N   1 
ATOM   4511  C  CA  . ALA   C  3  93  ? 31.299  -105.069 4.856   1.00 89.04  ? 91  ALA   C CA  1 
ATOM   4512  C  C   . ALA   C  3  93  ? 31.606  -106.561 4.682   1.00 87.50  ? 91  ALA   C C   1 
ATOM   4513  O  O   . ALA   C  3  93  ? 30.890  -107.221 3.908   1.00 88.73  ? 91  ALA   C O   1 
ATOM   4514  C  CB  . ALA   C  3  93  ? 32.293  -104.210 4.109   1.00 91.34  ? 91  ALA   C CB  1 
ATOM   4515  N  N   . GLN   C  3  94  ? 32.627  -107.061 5.384   1.00 88.39  ? 92  GLN   C N   1 
ATOM   4516  C  CA  . GLN   C  3  94  ? 33.084  -108.476 5.325   1.00 88.42  ? 92  GLN   C CA  1 
ATOM   4517  C  C   . GLN   C  3  94  ? 32.090  -109.373 6.072   1.00 90.61  ? 92  GLN   C C   1 
ATOM   4518  O  O   . GLN   C  3  94  ? 31.839  -110.492 5.584   1.00 93.24  ? 92  GLN   C O   1 
ATOM   4519  C  CB  . GLN   C  3  94  ? 34.492  -108.616 5.909   1.00 89.32  ? 92  GLN   C CB  1 
ATOM   4520  C  CG  . GLN   C  3  94  ? 35.569  -107.930 5.079   1.00 90.69  ? 92  GLN   C CG  1 
ATOM   4521  C  CD  . GLN   C  3  94  ? 35.536  -108.310 3.619   1.00 92.83  ? 92  GLN   C CD  1 
ATOM   4522  O  OE1 . GLN   C  3  94  ? 35.630  -107.458 2.737   1.00 94.20  ? 92  GLN   C OE1 1 
ATOM   4523  N  NE2 . GLN   C  3  94  ? 35.398  -109.599 3.348   1.00 93.62  ? 92  GLN   C NE2 1 
ATOM   4524  N  N   . SER   C  3  95  ? 31.559  -108.905 7.207   1.00 88.74  ? 93  SER   C N   1 
ATOM   4525  C  CA  . SER   C  3  95  ? 30.579  -109.630 8.059   1.00 90.08  ? 93  SER   C CA  1 
ATOM   4526  C  C   . SER   C  3  95  ? 29.272  -109.858 7.294   1.00 91.10  ? 93  SER   C C   1 
ATOM   4527  O  O   . SER   C  3  95  ? 28.669  -110.931 7.475   1.00 91.49  ? 93  SER   C O   1 
ATOM   4528  C  CB  . SER   C  3  95  ? 30.313  -108.889 9.338   1.00 89.73  ? 93  SER   C CB  1 
ATOM   4529  O  OG  . SER   C  3  95  ? 29.390  -109.596 10.148  1.00 95.12  ? 93  SER   C OG  1 
ATOM   4530  N  N   . HIS   C  3  96  ? 28.842  -108.877 6.495   1.00 91.63  ? 94  HIS   C N   1 
ATOM   4531  C  CA  . HIS   C  3  96  ? 27.624  -108.963 5.646   1.00 90.57  ? 94  HIS   C CA  1 
ATOM   4532  C  C   . HIS   C  3  96  ? 27.817  -110.040 4.570   1.00 91.74  ? 94  HIS   C C   1 
ATOM   4533  O  O   . HIS   C  3  96  ? 26.904  -110.873 4.404   1.00 89.55  ? 94  HIS   C O   1 
ATOM   4534  C  CB  . HIS   C  3  96  ? 27.278  -107.604 5.027   1.00 90.76  ? 94  HIS   C CB  1 
ATOM   4535  C  CG  . HIS   C  3  96  ? 25.918  -107.576 4.415   1.00 89.41  ? 94  HIS   C CG  1 
ATOM   4536  N  ND1 . HIS   C  3  96  ? 25.682  -108.000 3.123   1.00 91.20  ? 94  HIS   C ND1 1 
ATOM   4537  C  CD2 . HIS   C  3  96  ? 24.721  -107.205 4.917   1.00 88.93  ? 94  HIS   C CD2 1 
ATOM   4538  C  CE1 . HIS   C  3  96  ? 24.398  -107.879 2.850   1.00 91.66  ? 94  HIS   C CE1 1 
ATOM   4539  N  NE2 . HIS   C  3  96  ? 23.786  -107.392 3.935   1.00 90.03  ? 94  HIS   C NE2 1 
ATOM   4540  N  N   . ARG   C  3  97  ? 28.961  -110.022 3.875   1.00 93.82  ? 95  ARG   C N   1 
ATOM   4541  C  CA  . ARG   C  3  97  ? 29.323  -111.005 2.815   1.00 98.17  ? 95  ARG   C CA  1 
ATOM   4542  C  C   . ARG   C  3  97  ? 29.311  -112.424 3.395   1.00 99.18  ? 95  ARG   C C   1 
ATOM   4543  O  O   . ARG   C  3  97  ? 28.982  -113.360 2.644   1.00 102.10 ? 95  ARG   C O   1 
ATOM   4544  C  CB  . ARG   C  3  97  ? 30.710  -110.708 2.237   1.00 100.60 ? 95  ARG   C CB  1 
ATOM   4545  C  CG  . ARG   C  3  97  ? 30.807  -109.410 1.448   1.00 102.11 ? 95  ARG   C CG  1 
ATOM   4546  C  CD  . ARG   C  3  97  ? 32.246  -109.081 1.094   1.00 104.66 ? 95  ARG   C CD  1 
ATOM   4547  N  NE  . ARG   C  3  97  ? 32.659  -109.694 -0.162  1.00 107.69 ? 95  ARG   C NE  1 
ATOM   4548  C  CZ  . ARG   C  3  97  ? 32.682  -109.089 -1.347  1.00 110.22 ? 95  ARG   C CZ  1 
ATOM   4549  N  NH1 . ARG   C  3  97  ? 32.315  -107.824 -1.472  1.00 110.41 ? 95  ARG   C NH1 1 
ATOM   4550  N  NH2 . ARG   C  3  97  ? 33.080  -109.760 -2.414  1.00 115.45 ? 95  ARG   C NH2 1 
ATOM   4551  N  N   . LEU   C  3  98  ? 29.664  -112.564 4.678   1.00 97.48  ? 96  LEU   C N   1 
ATOM   4552  C  CA  . LEU   C  3  98  ? 29.845  -113.862 5.381   1.00 96.67  ? 96  LEU   C CA  1 
ATOM   4553  C  C   . LEU   C  3  98  ? 28.483  -114.485 5.711   1.00 95.74  ? 96  LEU   C C   1 
ATOM   4554  O  O   . LEU   C  3  98  ? 28.338  -115.693 5.479   1.00 100.59 ? 96  LEU   C O   1 
ATOM   4555  C  CB  . LEU   C  3  98  ? 30.675  -113.626 6.647   1.00 97.00  ? 96  LEU   C CB  1 
ATOM   4556  C  CG  . LEU   C  3  98  ? 31.359  -114.853 7.248   1.00 99.47  ? 96  LEU   C CG  1 
ATOM   4557  C  CD1 . LEU   C  3  98  ? 32.307  -115.511 6.252   1.00 103.91 ? 96  LEU   C CD1 1 
ATOM   4558  C  CD2 . LEU   C  3  98  ? 32.113  -114.472 8.512   1.00 99.74  ? 96  LEU   C CD2 1 
ATOM   4559  N  N   . THR   C  3  99  ? 27.523  -113.705 6.219   1.00 90.06  ? 97  THR   C N   1 
ATOM   4560  C  CA  . THR   C  3  99  ? 26.201  -114.208 6.690   1.00 89.90  ? 97  THR   C CA  1 
ATOM   4561  C  C   . THR   C  3  99  ? 25.153  -114.162 5.568   1.00 91.64  ? 97  THR   C C   1 
ATOM   4562  O  O   . THR   C  3  99  ? 24.401  -115.146 5.456   1.00 90.23  ? 97  THR   C O   1 
ATOM   4563  C  CB  . THR   C  3  99  ? 25.731  -113.457 7.942   1.00 87.94  ? 97  THR   C CB  1 
ATOM   4564  O  OG1 . THR   C  3  99  ? 25.714  -112.055 7.679   1.00 87.37  ? 97  THR   C OG1 1 
ATOM   4565  C  CG2 . THR   C  3  99  ? 26.614  -113.728 9.139   1.00 90.04  ? 97  THR   C CG2 1 
ATOM   4566  N  N   . LEU   C  3  100 ? 25.088  -113.079 4.782   1.00 92.06  ? 98  LEU   C N   1 
ATOM   4567  C  CA  . LEU   C  3  100 ? 24.064  -112.890 3.711   1.00 95.02  ? 98  LEU   C CA  1 
ATOM   4568  C  C   . LEU   C  3  100 ? 24.548  -113.482 2.377   1.00 96.13  ? 98  LEU   C C   1 
ATOM   4569  O  O   . LEU   C  3  100 ? 23.703  -113.614 1.467   1.00 93.48  ? 98  LEU   C O   1 
ATOM   4570  C  CB  . LEU   C  3  100 ? 23.739  -111.400 3.538   1.00 96.19  ? 98  LEU   C CB  1 
ATOM   4571  C  CG  . LEU   C  3  100 ? 22.832  -110.747 4.586   1.00 96.23  ? 98  LEU   C CG  1 
ATOM   4572  C  CD1 . LEU   C  3  100 ? 21.568  -111.557 4.839   1.00 97.70  ? 98  LEU   C CD1 1 
ATOM   4573  C  CD2 . LEU   C  3  100 ? 23.575  -110.503 5.887   1.00 96.36  ? 98  LEU   C CD2 1 
ATOM   4574  N  N   . GLU   C  3  101 ? 25.842  -113.810 2.255   1.00 97.41  ? 99  GLU   C N   1 
ATOM   4575  C  CA  . GLU   C  3  101 ? 26.485  -114.313 1.006   1.00 99.59  ? 99  GLU   C CA  1 
ATOM   4576  C  C   . GLU   C  3  101 ? 26.226  -113.326 -0.139  1.00 100.16 ? 99  GLU   C C   1 
ATOM   4577  O  O   . GLU   C  3  101 ? 25.925  -113.778 -1.256  1.00 98.40  ? 99  GLU   C O   1 
ATOM   4578  C  CB  . GLU   C  3  101 ? 25.982  -115.716 0.652   1.00 99.40  ? 99  GLU   C CB  1 
ATOM   4579  C  CG  . GLU   C  3  101 ? 26.462  -116.796 1.605   1.00 100.62 ? 99  GLU   C CG  1 
ATOM   4580  C  CD  . GLU   C  3  101 ? 26.415  -118.211 1.044   1.00 102.32 ? 99  GLU   C CD  1 
ATOM   4581  O  OE1 . GLU   C  3  101 ? 27.083  -119.098 1.616   1.00 101.43 ? 99  GLU   C OE1 1 
ATOM   4582  O  OE2 . GLU   C  3  101 ? 25.702  -118.435 0.043   1.00 104.51 ? 99  GLU   C OE2 1 
ATOM   4583  N  N   . ASP   C  3  102 ? 26.338  -112.024 0.141   1.00 102.88 ? 100 ASP   C N   1 
ATOM   4584  C  CA  . ASP   C  3  102 ? 26.157  -110.923 -0.845  1.00 106.06 ? 100 ASP   C CA  1 
ATOM   4585  C  C   . ASP   C  3  102 ? 26.797  -109.659 -0.272  1.00 102.56 ? 100 ASP   C C   1 
ATOM   4586  O  O   . ASP   C  3  102 ? 26.612  -109.365 0.906   1.00 98.11  ? 100 ASP   C O   1 
ATOM   4587  C  CB  . ASP   C  3  102 ? 24.672  -110.705 -1.166  1.00 111.77 ? 100 ASP   C CB  1 
ATOM   4588  C  CG  . ASP   C  3  102 ? 24.371  -110.303 -2.605  1.00 114.38 ? 100 ASP   C CG  1 
ATOM   4589  O  OD1 . ASP   C  3  102 ? 25.274  -110.424 -3.458  1.00 119.53 ? 100 ASP   C OD1 1 
ATOM   4590  O  OD2 . ASP   C  3  102 ? 23.223  -109.886 -2.867  1.00 119.51 ? 100 ASP   C OD2 1 
ATOM   4591  N  N   . PRO   C  3  103 ? 27.585  -108.883 -1.057  1.00 100.07 ? 101 PRO   C N   1 
ATOM   4592  C  CA  . PRO   C  3  103 ? 28.121  -107.611 -0.573  1.00 99.18  ? 101 PRO   C CA  1 
ATOM   4593  C  C   . PRO   C  3  103 ? 27.002  -106.636 -0.173  1.00 96.49  ? 101 PRO   C C   1 
ATOM   4594  O  O   . PRO   C  3  103 ? 25.893  -106.773 -0.667  1.00 96.10  ? 101 PRO   C O   1 
ATOM   4595  C  CB  . PRO   C  3  103 ? 28.925  -107.052 -1.758  1.00 97.96  ? 101 PRO   C CB  1 
ATOM   4596  C  CG  . PRO   C  3  103 ? 29.208  -108.259 -2.628  1.00 99.93  ? 101 PRO   C CG  1 
ATOM   4597  C  CD  . PRO   C  3  103 ? 28.032  -109.191 -2.424  1.00 100.68 ? 101 PRO   C CD  1 
ATOM   4598  N  N   . VAL   C  3  104 ? 27.317  -105.690 0.716   1.00 95.93  ? 102 VAL   C N   1 
ATOM   4599  C  CA  . VAL   C  3  104 ? 26.361  -104.660 1.224   1.00 94.79  ? 102 VAL   C CA  1 
ATOM   4600  C  C   . VAL   C  3  104 ? 25.822  -103.841 0.046   1.00 93.37  ? 102 VAL   C C   1 
ATOM   4601  O  O   . VAL   C  3  104 ? 26.562  -103.649 -0.940  1.00 91.69  ? 102 VAL   C O   1 
ATOM   4602  C  CB  . VAL   C  3  104 ? 27.001  -103.731 2.278   1.00 93.02  ? 102 VAL   C CB  1 
ATOM   4603  C  CG1 . VAL   C  3  104 ? 27.225  -104.447 3.598   1.00 95.65  ? 102 VAL   C CG1 1 
ATOM   4604  C  CG2 . VAL   C  3  104 ? 28.292  -103.087 1.790   1.00 92.12  ? 102 VAL   C CG2 1 
ATOM   4605  N  N   . THR   C  3  105 ? 24.574  -103.378 0.158   1.00 91.13  ? 103 THR   C N   1 
ATOM   4606  C  CA  . THR   C  3  105 ? 24.025  -102.252 -0.641  1.00 89.70  ? 103 THR   C CA  1 
ATOM   4607  C  C   . THR   C  3  105 ? 24.631  -100.963 -0.084  1.00 88.33  ? 103 THR   C C   1 
ATOM   4608  O  O   . THR   C  3  105 ? 25.035  -100.972 1.095   1.00 88.18  ? 103 THR   C O   1 
ATOM   4609  C  CB  . THR   C  3  105 ? 22.493  -102.211 -0.602  1.00 86.73  ? 103 THR   C CB  1 
ATOM   4610  O  OG1 . THR   C  3  105 ? 22.068  -101.993 0.743   1.00 83.68  ? 103 THR   C OG1 1 
ATOM   4611  C  CG2 . THR   C  3  105 ? 21.861  -103.479 -1.128  1.00 89.24  ? 103 THR   C CG2 1 
ATOM   4612  N  N   . VAL   C  3  106 ? 24.692  -99.902  -0.888  1.00 89.97  ? 104 VAL   C N   1 
ATOM   4613  C  CA  . VAL   C  3  106 ? 25.269  -98.593  -0.464  1.00 90.32  ? 104 VAL   C CA  1 
ATOM   4614  C  C   . VAL   C  3  106 ? 24.367  -98.017  0.631   1.00 86.02  ? 104 VAL   C C   1 
ATOM   4615  O  O   . VAL   C  3  106 ? 24.905  -97.432  1.589   1.00 83.82  ? 104 VAL   C O   1 
ATOM   4616  C  CB  . VAL   C  3  106 ? 25.426  -97.612  -1.641  1.00 93.10  ? 104 VAL   C CB  1 
ATOM   4617  C  CG1 . VAL   C  3  106 ? 26.139  -96.338  -1.211  1.00 94.07  ? 104 VAL   C CG1 1 
ATOM   4618  C  CG2 . VAL   C  3  106 ? 26.147  -98.249  -2.820  1.00 95.36  ? 104 VAL   C CG2 1 
ATOM   4619  N  N   . GLU   C  3  107 ? 23.050  -98.196  0.489   1.00 86.69  ? 105 GLU   C N   1 
ATOM   4620  C  CA  . GLU   C  3  107 ? 22.030  -97.763  1.479   1.00 88.37  ? 105 GLU   C CA  1 
ATOM   4621  C  C   . GLU   C  3  107 ? 22.320  -98.439  2.825   1.00 90.24  ? 105 GLU   C C   1 
ATOM   4622  O  O   . GLU   C  3  107 ? 22.344  -97.721  3.844   1.00 93.07  ? 105 GLU   C O   1 
ATOM   4623  C  CB  . GLU   C  3  107 ? 20.621  -98.080  0.971   1.00 90.04  ? 105 GLU   C CB  1 
ATOM   4624  C  CG  . GLU   C  3  107 ? 19.515  -97.438  1.791   1.00 92.72  ? 105 GLU   C CG  1 
ATOM   4625  C  CD  . GLU   C  3  107 ? 19.133  -98.175  3.064   1.00 96.88  ? 105 GLU   C CD  1 
ATOM   4626  O  OE1 . GLU   C  3  107 ? 18.835  -97.492  4.066   1.00 97.99  ? 105 GLU   C OE1 1 
ATOM   4627  O  OE2 . GLU   C  3  107 ? 19.128  -99.429  3.051   1.00 103.90 ? 105 GLU   C OE2 1 
ATOM   4628  N  N   . TYR   C  3  108 ? 22.545  -99.759  2.830   1.00 90.94  ? 106 TYR   C N   1 
ATOM   4629  C  CA  . TYR   C  3  108 ? 22.780  -100.565 4.059   1.00 91.32  ? 106 TYR   C CA  1 
ATOM   4630  C  C   . TYR   C  3  108 ? 24.074  -100.114 4.745   1.00 88.45  ? 106 TYR   C C   1 
ATOM   4631  O  O   . TYR   C  3  108 ? 24.042  -99.881  5.967   1.00 88.09  ? 106 TYR   C O   1 
ATOM   4632  C  CB  . TYR   C  3  108 ? 22.861  -102.065 3.766   1.00 92.32  ? 106 TYR   C CB  1 
ATOM   4633  C  CG  . TYR   C  3  108 ? 23.176  -102.890 4.988   1.00 94.22  ? 106 TYR   C CG  1 
ATOM   4634  C  CD1 . TYR   C  3  108 ? 24.485  -103.098 5.394   1.00 95.14  ? 106 TYR   C CD1 1 
ATOM   4635  C  CD2 . TYR   C  3  108 ? 22.164  -103.425 5.770   1.00 94.46  ? 106 TYR   C CD2 1 
ATOM   4636  C  CE1 . TYR   C  3  108 ? 24.782  -103.834 6.529   1.00 97.18  ? 106 TYR   C CE1 1 
ATOM   4637  C  CE2 . TYR   C  3  108 ? 22.444  -104.166 6.907   1.00 97.38  ? 106 TYR   C CE2 1 
ATOM   4638  C  CZ  . TYR   C  3  108 ? 23.759  -104.371 7.288   1.00 98.34  ? 106 TYR   C CZ  1 
ATOM   4639  O  OH  . TYR   C  3  108 ? 24.052  -105.099 8.405   1.00 106.42 ? 106 TYR   C OH  1 
ATOM   4640  N  N   . LEU   C  3  109 ? 25.176  -100.038 3.992   1.00 88.41  ? 107 LEU   C N   1 
ATOM   4641  C  CA  . LEU   C  3  109 ? 26.512  -99.632  4.510   1.00 88.82  ? 107 LEU   C CA  1 
ATOM   4642  C  C   . LEU   C  3  109 ? 26.386  -98.241  5.142   1.00 89.95  ? 107 LEU   C C   1 
ATOM   4643  O  O   . LEU   C  3  109 ? 26.930  -98.048  6.248   1.00 90.34  ? 107 LEU   C O   1 
ATOM   4644  C  CB  . LEU   C  3  109 ? 27.537  -99.651  3.367   1.00 87.29  ? 107 LEU   C CB  1 
ATOM   4645  C  CG  . LEU   C  3  109 ? 29.017  -99.553  3.754   1.00 87.17  ? 107 LEU   C CG  1 
ATOM   4646  C  CD1 . LEU   C  3  109 ? 29.451  -98.112  3.964   1.00 87.40  ? 107 LEU   C CD1 1 
ATOM   4647  C  CD2 . LEU   C  3  109 ? 29.341  -100.387 4.984   1.00 87.89  ? 107 LEU   C CD2 1 
ATOM   4648  N  N   . THR   C  3  110 ? 25.674  -97.327  4.473   1.00 91.73  ? 108 THR   C N   1 
ATOM   4649  C  CA  . THR   C  3  110 ? 25.385  -95.949  4.958   1.00 92.25  ? 108 THR   C CA  1 
ATOM   4650  C  C   . THR   C  3  110 ? 24.557  -96.027  6.247   1.00 93.90  ? 108 THR   C C   1 
ATOM   4651  O  O   . THR   C  3  110 ? 24.940  -95.353  7.225   1.00 94.93  ? 108 THR   C O   1 
ATOM   4652  C  CB  . THR   C  3  110 ? 24.675  -95.106  3.890   1.00 90.80  ? 108 THR   C CB  1 
ATOM   4653  O  OG1 . THR   C  3  110 ? 25.542  -94.962  2.765   1.00 87.65  ? 108 THR   C OG1 1 
ATOM   4654  C  CG2 . THR   C  3  110 ? 24.280  -93.737  4.398   1.00 89.56  ? 108 THR   C CG2 1 
ATOM   4655  N  N   . ARG   C  3  111 ? 23.472  -96.813  6.243   1.00 95.85  ? 109 ARG   C N   1 
ATOM   4656  C  CA  . ARG   C  3  111 ? 22.540  -96.963  7.397   1.00 95.06  ? 109 ARG   C CA  1 
ATOM   4657  C  C   . ARG   C  3  111 ? 23.328  -97.430  8.627   1.00 90.94  ? 109 ARG   C C   1 
ATOM   4658  O  O   . ARG   C  3  111 ? 23.017  -96.955  9.738   1.00 87.36  ? 109 ARG   C O   1 
ATOM   4659  C  CB  . ARG   C  3  111 ? 21.390  -97.921  7.059   1.00 96.47  ? 109 ARG   C CB  1 
ATOM   4660  C  CG  . ARG   C  3  111 ? 20.583  -98.389  8.264   1.00 97.32  ? 109 ARG   C CG  1 
ATOM   4661  C  CD  . ARG   C  3  111 ? 19.174  -98.823  7.902   1.00 98.81  ? 109 ARG   C CD  1 
ATOM   4662  N  NE  . ARG   C  3  111 ? 19.121  -99.549  6.639   1.00 101.67 ? 109 ARG   C NE  1 
ATOM   4663  C  CZ  . ARG   C  3  111 ? 19.150  -100.874 6.504   1.00 104.54 ? 109 ARG   C CZ  1 
ATOM   4664  N  NH1 . ARG   C  3  111 ? 19.098  -101.405 5.293   1.00 106.90 ? 109 ARG   C NH1 1 
ATOM   4665  N  NH2 . ARG   C  3  111 ? 19.228  -101.669 7.560   1.00 111.16 ? 109 ARG   C NH2 1 
ATOM   4666  N  N   . TYR   C  3  112 ? 24.309  -98.317  8.437   1.00 91.24  ? 110 TYR   C N   1 
ATOM   4667  C  CA  . TYR   C  3  112 ? 25.171  -98.844  9.526   1.00 91.79  ? 110 TYR   C CA  1 
ATOM   4668  C  C   . TYR   C  3  112 ? 26.049  -97.712  10.072  1.00 91.58  ? 110 TYR   C C   1 
ATOM   4669  O  O   . TYR   C  3  112 ? 26.050  -97.512  11.301  1.00 92.67  ? 110 TYR   C O   1 
ATOM   4670  C  CB  . TYR   C  3  112 ? 26.034  -100.020 9.059   1.00 91.12  ? 110 TYR   C CB  1 
ATOM   4671  C  CG  . TYR   C  3  112 ? 27.062  -100.436 10.079  1.00 87.34  ? 110 TYR   C CG  1 
ATOM   4672  C  CD1 . TYR   C  3  112 ? 26.705  -101.181 11.191  1.00 85.97  ? 110 TYR   C CD1 1 
ATOM   4673  C  CD2 . TYR   C  3  112 ? 28.384  -100.040 9.960   1.00 86.92  ? 110 TYR   C CD2 1 
ATOM   4674  C  CE1 . TYR   C  3  112 ? 27.640  -101.545 12.145  1.00 85.29  ? 110 TYR   C CE1 1 
ATOM   4675  C  CE2 . TYR   C  3  112 ? 29.332  -100.395 10.905  1.00 85.45  ? 110 TYR   C CE2 1 
ATOM   4676  C  CZ  . TYR   C  3  112 ? 28.959  -101.148 12.003  1.00 84.67  ? 110 TYR   C CZ  1 
ATOM   4677  O  OH  . TYR   C  3  112 ? 29.895  -101.492 12.935  1.00 83.27  ? 110 TYR   C OH  1 
ATOM   4678  N  N   . VAL   C  3  113 ? 26.760  -97.004  9.186   1.00 94.28  ? 111 VAL   C N   1 
ATOM   4679  C  CA  . VAL   C  3  113 ? 27.719  -95.911  9.544   1.00 93.47  ? 111 VAL   C CA  1 
ATOM   4680  C  C   . VAL   C  3  113 ? 26.960  -94.823  10.316  1.00 91.75  ? 111 VAL   C C   1 
ATOM   4681  O  O   . VAL   C  3  113 ? 27.502  -94.333  11.327  1.00 89.53  ? 111 VAL   C O   1 
ATOM   4682  C  CB  . VAL   C  3  113 ? 28.435  -95.336  8.303   1.00 96.45  ? 111 VAL   C CB  1 
ATOM   4683  C  CG1 . VAL   C  3  113 ? 29.228  -94.078  8.630   1.00 97.45  ? 111 VAL   C CG1 1 
ATOM   4684  C  CG2 . VAL   C  3  113 ? 29.342  -96.364  7.643   1.00 97.69  ? 111 VAL   C CG2 1 
ATOM   4685  N  N   . ALA   C  3  114 ? 25.756  -94.466  9.856   1.00 88.84  ? 112 ALA   C N   1 
ATOM   4686  C  CA  . ALA   C  3  114 ? 24.865  -93.463  10.485  1.00 85.09  ? 112 ALA   C CA  1 
ATOM   4687  C  C   . ALA   C  3  114 ? 24.415  -93.961  11.864  1.00 84.68  ? 112 ALA   C C   1 
ATOM   4688  O  O   . ALA   C  3  114 ? 24.365  -93.142  12.801  1.00 78.57  ? 112 ALA   C O   1 
ATOM   4689  C  CB  . ALA   C  3  114 ? 23.687  -93.185  9.586   1.00 86.78  ? 112 ALA   C CB  1 
ATOM   4690  N  N   . GLY   C  3  115 ? 24.102  -95.255  11.977  1.00 82.95  ? 113 GLY   C N   1 
ATOM   4691  C  CA  . GLY   C  3  115 ? 23.706  -95.899  13.245  1.00 82.42  ? 113 GLY   C CA  1 
ATOM   4692  C  C   . GLY   C  3  115 ? 24.804  -95.795  14.292  1.00 81.86  ? 113 GLY   C C   1 
ATOM   4693  O  O   . GLY   C  3  115 ? 24.480  -95.502  15.464  1.00 77.48  ? 113 GLY   C O   1 
ATOM   4694  N  N   . VAL   C  3  116 ? 26.056  -96.027  13.885  1.00 82.92  ? 114 VAL   C N   1 
ATOM   4695  C  CA  . VAL   C  3  116 ? 27.265  -95.904  14.754  1.00 83.39  ? 114 VAL   C CA  1 
ATOM   4696  C  C   . VAL   C  3  116 ? 27.335  -94.462  15.266  1.00 83.26  ? 114 VAL   C C   1 
ATOM   4697  O  O   . VAL   C  3  116 ? 27.440  -94.280  16.491  1.00 85.90  ? 114 VAL   C O   1 
ATOM   4698  C  CB  . VAL   C  3  116 ? 28.554  -96.297  14.006  1.00 83.31  ? 114 VAL   C CB  1 
ATOM   4699  C  CG1 . VAL   C  3  116 ? 29.803  -95.945  14.800  1.00 84.02  ? 114 VAL   C CG1 1 
ATOM   4700  C  CG2 . VAL   C  3  116 ? 28.566  -97.770  13.631  1.00 83.72  ? 114 VAL   C CG2 1 
ATOM   4701  N  N   . GLN   C  3  117 ? 27.272  -93.485  14.354  1.00 82.87  ? 115 GLN   C N   1 
ATOM   4702  C  CA  . GLN   C  3  117 ? 27.360  -92.034  14.672  1.00 83.81  ? 115 GLN   C CA  1 
ATOM   4703  C  C   . GLN   C  3  117 ? 26.287  -91.671  15.705  1.00 80.37  ? 115 GLN   C C   1 
ATOM   4704  O  O   . GLN   C  3  117 ? 26.638  -91.017  16.704  1.00 80.48  ? 115 GLN   C O   1 
ATOM   4705  C  CB  . GLN   C  3  117 ? 27.226  -91.191  13.402  1.00 83.73  ? 115 GLN   C CB  1 
ATOM   4706  C  CG  . GLN   C  3  117 ? 28.508  -91.120  12.584  1.00 86.76  ? 115 GLN   C CG  1 
ATOM   4707  C  CD  . GLN   C  3  117 ? 28.348  -90.281  11.337  1.00 90.37  ? 115 GLN   C CD  1 
ATOM   4708  O  OE1 . GLN   C  3  117 ? 27.775  -90.717  10.340  1.00 95.19  ? 115 GLN   C OE1 1 
ATOM   4709  N  NE2 . GLN   C  3  117 ? 28.863  -89.063  11.375  1.00 89.54  ? 115 GLN   C NE2 1 
ATOM   4710  N  N   . GLN   C  3  118 ? 25.038  -92.090  15.474  1.00 79.39  ? 116 GLN   C N   1 
ATOM   4711  C  CA  . GLN   C  3  118 ? 23.876  -91.813  16.362  1.00 81.31  ? 116 GLN   C CA  1 
ATOM   4712  C  C   . GLN   C  3  118 ? 24.152  -92.373  17.761  1.00 81.27  ? 116 GLN   C C   1 
ATOM   4713  O  O   . GLN   C  3  118 ? 23.845  -91.674  18.737  1.00 81.43  ? 116 GLN   C O   1 
ATOM   4714  C  CB  . GLN   C  3  118 ? 22.594  -92.424  15.792  1.00 81.75  ? 116 GLN   C CB  1 
ATOM   4715  C  CG  . GLN   C  3  118 ? 21.321  -91.961  16.494  1.00 81.72  ? 116 GLN   C CG  1 
ATOM   4716  C  CD  . GLN   C  3  118 ? 21.106  -92.547  17.870  1.00 81.21  ? 116 GLN   C CD  1 
ATOM   4717  O  OE1 . GLN   C  3  118 ? 20.785  -91.838  18.820  1.00 78.10  ? 116 GLN   C OE1 1 
ATOM   4718  N  NE2 . GLN   C  3  118 ? 21.268  -93.855  17.995  1.00 82.09  ? 116 GLN   C NE2 1 
ATOM   4719  N  N   . ARG   C  3  119 ? 24.697  -93.590  17.852  1.00 84.92  ? 117 ARG   C N   1 
ATOM   4720  C  CA  . ARG   C  3  119 ? 24.962  -94.285  19.144  1.00 88.12  ? 117 ARG   C CA  1 
ATOM   4721  C  C   . ARG   C  3  119 ? 25.842  -93.389  20.028  1.00 84.85  ? 117 ARG   C C   1 
ATOM   4722  O  O   . ARG   C  3  119 ? 25.587  -93.328  21.244  1.00 83.68  ? 117 ARG   C O   1 
ATOM   4723  C  CB  . ARG   C  3  119 ? 25.591  -95.667  18.915  1.00 91.89  ? 117 ARG   C CB  1 
ATOM   4724  C  CG  . ARG   C  3  119 ? 25.179  -96.705  19.951  1.00 95.74  ? 117 ARG   C CG  1 
ATOM   4725  C  CD  . ARG   C  3  119 ? 25.864  -98.054  19.807  1.00 100.02 ? 117 ARG   C CD  1 
ATOM   4726  N  NE  . ARG   C  3  119 ? 25.786  -98.598  18.452  1.00 107.37 ? 117 ARG   C NE  1 
ATOM   4727  C  CZ  . ARG   C  3  119 ? 26.825  -98.913  17.671  1.00 113.16 ? 117 ARG   C CZ  1 
ATOM   4728  N  NH1 . ARG   C  3  119 ? 28.072  -98.756  18.088  1.00 113.36 ? 117 ARG   C NH1 1 
ATOM   4729  N  NH2 . ARG   C  3  119 ? 26.604  -99.398  16.459  1.00 112.79 ? 117 ARG   C NH2 1 
ATOM   4730  N  N   . TYR   C  3  120 ? 26.804  -92.681  19.428  1.00 86.01  ? 118 TYR   C N   1 
ATOM   4731  C  CA  . TYR   C  3  120 ? 27.795  -91.827  20.134  1.00 87.64  ? 118 TYR   C CA  1 
ATOM   4732  C  C   . TYR   C  3  120 ? 27.147  -90.511  20.598  1.00 90.00  ? 118 TYR   C C   1 
ATOM   4733  O  O   . TYR   C  3  120 ? 27.820  -89.743  21.321  1.00 88.47  ? 118 TYR   C O   1 
ATOM   4734  C  CB  . TYR   C  3  120 ? 29.022  -91.600  19.243  1.00 89.41  ? 118 TYR   C CB  1 
ATOM   4735  C  CG  . TYR   C  3  120 ? 30.033  -92.719  19.275  1.00 90.15  ? 118 TYR   C CG  1 
ATOM   4736  C  CD1 . TYR   C  3  120 ? 29.704  -93.997  18.851  1.00 89.05  ? 118 TYR   C CD1 1 
ATOM   4737  C  CD2 . TYR   C  3  120 ? 31.325  -92.504  19.731  1.00 91.95  ? 118 TYR   C CD2 1 
ATOM   4738  C  CE1 . TYR   C  3  120 ? 30.628  -95.031  18.881  1.00 88.89  ? 118 TYR   C CE1 1 
ATOM   4739  C  CE2 . TYR   C  3  120 ? 32.261  -93.525  19.766  1.00 90.21  ? 118 TYR   C CE2 1 
ATOM   4740  C  CZ  . TYR   C  3  120 ? 31.912  -94.793  19.340  1.00 87.28  ? 118 TYR   C CZ  1 
ATOM   4741  O  OH  . TYR   C  3  120 ? 32.847  -95.784  19.381  1.00 87.90  ? 118 TYR   C OH  1 
ATOM   4742  N  N   . THR   C  3  121 ? 25.887  -90.252  20.223  1.00 88.79  ? 119 THR   C N   1 
ATOM   4743  C  CA  . THR   C  3  121 ? 25.146  -89.017  20.603  1.00 88.35  ? 119 THR   C CA  1 
ATOM   4744  C  C   . THR   C  3  121 ? 24.250  -89.270  21.824  1.00 93.98  ? 119 THR   C C   1 
ATOM   4745  O  O   . THR   C  3  121 ? 23.837  -88.264  22.432  1.00 98.02  ? 119 THR   C O   1 
ATOM   4746  C  CB  . THR   C  3  121 ? 24.323  -88.440  19.443  1.00 84.63  ? 119 THR   C CB  1 
ATOM   4747  O  OG1 . THR   C  3  121 ? 23.236  -89.318  19.156  1.00 80.08  ? 119 THR   C OG1 1 
ATOM   4748  C  CG2 . THR   C  3  121 ? 25.146  -88.206  18.196  1.00 84.36  ? 119 THR   C CG2 1 
ATOM   4749  N  N   . GLN   C  3  122 ? 23.934  -90.528  22.170  1.00 93.96  ? 120 GLN   C N   1 
ATOM   4750  C  CA  . GLN   C  3  122 ? 23.202  -90.839  23.433  1.00 92.71  ? 120 GLN   C CA  1 
ATOM   4751  C  C   . GLN   C  3  122 ? 23.816  -92.061  24.127  1.00 89.00  ? 120 GLN   C C   1 
ATOM   4752  O  O   . GLN   C  3  122 ? 23.057  -92.839  24.731  1.00 90.56  ? 120 GLN   C O   1 
ATOM   4753  C  CB  . GLN   C  3  122 ? 21.688  -90.955  23.210  1.00 96.07  ? 120 GLN   C CB  1 
ATOM   4754  C  CG  . GLN   C  3  122 ? 21.222  -92.121  22.347  1.00 97.34  ? 120 GLN   C CG  1 
ATOM   4755  C  CD  . GLN   C  3  122 ? 19.713  -92.164  22.261  1.00 100.16 ? 120 GLN   C CD  1 
ATOM   4756  O  OE1 . GLN   C  3  122 ? 19.006  -91.772  23.190  1.00 98.46  ? 120 GLN   C OE1 1 
ATOM   4757  N  NE2 . GLN   C  3  122 ? 19.198  -92.641  21.137  1.00 102.19 ? 120 GLN   C NE2 1 
ATOM   4758  N  N   . SER   C  3  123 ? 25.147  -92.175  24.096  1.00 85.70  ? 121 SER   C N   1 
ATOM   4759  C  CA  . SER   C  3  123 ? 25.948  -93.058  24.984  1.00 84.97  ? 121 SER   C CA  1 
ATOM   4760  C  C   . SER   C  3  123 ? 26.695  -92.207  26.015  1.00 89.03  ? 121 SER   C C   1 
ATOM   4761  O  O   . SER   C  3  123 ? 27.123  -91.085  25.669  1.00 90.70  ? 121 SER   C O   1 
ATOM   4762  C  CB  . SER   C  3  123 ? 26.904  -93.907  24.200  1.00 82.42  ? 121 SER   C CB  1 
ATOM   4763  O  OG  . SER   C  3  123 ? 26.202  -94.803  23.354  1.00 81.33  ? 121 SER   C OG  1 
ATOM   4764  N  N   . GLY   C  3  124 ? 26.836  -92.729  27.236  1.00 84.66  ? 122 GLY   C N   1 
ATOM   4765  C  CA  . GLY   C  3  124 ? 27.592  -92.097  28.332  1.00 84.96  ? 122 GLY   C CA  1 
ATOM   4766  C  C   . GLY   C  3  124 ? 29.089  -92.232  28.115  1.00 83.63  ? 122 GLY   C C   1 
ATOM   4767  O  O   . GLY   C  3  124 ? 29.524  -93.298  27.664  1.00 81.27  ? 122 GLY   C O   1 
ATOM   4768  N  N   . GLY   C  3  125 ? 29.846  -91.172  28.395  1.00 85.94  ? 123 GLY   C N   1 
ATOM   4769  C  CA  . GLY   C  3  125 ? 31.320  -91.191  28.428  1.00 86.17  ? 123 GLY   C CA  1 
ATOM   4770  C  C   . GLY   C  3  125 ? 31.959  -91.059  27.054  1.00 86.14  ? 123 GLY   C C   1 
ATOM   4771  O  O   . GLY   C  3  125 ? 33.191  -91.216  26.981  1.00 83.67  ? 123 GLY   C O   1 
ATOM   4772  N  N   . VAL   C  3  126 ? 31.175  -90.766  26.008  1.00 88.50  ? 124 VAL   C N   1 
ATOM   4773  C  CA  . VAL   C  3  126 ? 31.681  -90.551  24.618  1.00 89.92  ? 124 VAL   C CA  1 
ATOM   4774  C  C   . VAL   C  3  126 ? 31.163  -89.208  24.088  1.00 91.83  ? 124 VAL   C C   1 
ATOM   4775  O  O   . VAL   C  3  126 ? 30.044  -88.799  24.491  1.00 88.03  ? 124 VAL   C O   1 
ATOM   4776  C  CB  . VAL   C  3  126 ? 31.282  -91.703  23.677  1.00 90.93  ? 124 VAL   C CB  1 
ATOM   4777  C  CG1 . VAL   C  3  126 ? 31.723  -93.051  24.220  1.00 92.55  ? 124 VAL   C CG1 1 
ATOM   4778  C  CG2 . VAL   C  3  126 ? 29.791  -91.716  23.382  1.00 92.11  ? 124 VAL   C CG2 1 
ATOM   4779  N  N   . ARG   C  3  127 ? 31.949  -88.567  23.210  1.00 93.95  ? 125 ARG   C N   1 
ATOM   4780  C  CA  . ARG   C  3  127 ? 31.540  -87.376  22.415  1.00 91.88  ? 125 ARG   C CA  1 
ATOM   4781  C  C   . ARG   C  3  127 ? 31.156  -87.828  21.009  1.00 90.25  ? 125 ARG   C C   1 
ATOM   4782  O  O   . ARG   C  3  127 ? 31.667  -88.829  20.511  1.00 85.79  ? 125 ARG   C O   1 
ATOM   4783  C  CB  . ARG   C  3  127 ? 32.643  -86.312  22.357  1.00 94.16  ? 125 ARG   C CB  1 
ATOM   4784  C  CG  . ARG   C  3  127 ? 33.940  -86.759  21.694  1.00 94.42  ? 125 ARG   C CG  1 
ATOM   4785  C  CD  . ARG   C  3  127 ? 34.764  -85.598  21.166  1.00 95.30  ? 125 ARG   C CD  1 
ATOM   4786  N  NE  . ARG   C  3  127 ? 36.001  -86.049  20.533  1.00 94.88  ? 125 ARG   C NE  1 
ATOM   4787  C  CZ  . ARG   C  3  127 ? 36.102  -86.550  19.302  1.00 93.86  ? 125 ARG   C CZ  1 
ATOM   4788  N  NH1 . ARG   C  3  127 ? 35.031  -86.680  18.533  1.00 92.72  ? 125 ARG   C NH1 1 
ATOM   4789  N  NH2 . ARG   C  3  127 ? 37.285  -86.924  18.844  1.00 92.16  ? 125 ARG   C NH2 1 
ATOM   4790  N  N   . PRO   C  3  128 ? 30.243  -87.105  20.325  1.00 90.87  ? 126 PRO   C N   1 
ATOM   4791  C  CA  . PRO   C  3  128 ? 29.890  -87.426  18.943  1.00 91.04  ? 126 PRO   C CA  1 
ATOM   4792  C  C   . PRO   C  3  128 ? 31.108  -87.368  18.009  1.00 89.24  ? 126 PRO   C C   1 
ATOM   4793  O  O   . PRO   C  3  128 ? 32.097  -86.752  18.367  1.00 87.22  ? 126 PRO   C O   1 
ATOM   4794  C  CB  . PRO   C  3  128 ? 28.872  -86.342  18.557  1.00 93.09  ? 126 PRO   C CB  1 
ATOM   4795  C  CG  . PRO   C  3  128 ? 28.331  -85.843  19.881  1.00 93.69  ? 126 PRO   C CG  1 
ATOM   4796  C  CD  . PRO   C  3  128 ? 29.494  -85.952  20.844  1.00 92.25  ? 126 PRO   C CD  1 
ATOM   4797  N  N   . PHE   C  3  129 ? 31.005  -88.017  16.847  1.00 91.14  ? 127 PHE   C N   1 
ATOM   4798  C  CA  . PHE   C  3  129 ? 32.029  -87.975  15.772  1.00 94.34  ? 127 PHE   C CA  1 
ATOM   4799  C  C   . PHE   C  3  129 ? 32.023  -86.581  15.138  1.00 94.70  ? 127 PHE   C C   1 
ATOM   4800  O  O   . PHE   C  3  129 ? 30.940  -86.106  14.736  1.00 99.58  ? 127 PHE   C O   1 
ATOM   4801  C  CB  . PHE   C  3  129 ? 31.770  -89.058  14.724  1.00 94.63  ? 127 PHE   C CB  1 
ATOM   4802  C  CG  . PHE   C  3  129 ? 32.124  -90.451  15.174  1.00 93.67  ? 127 PHE   C CG  1 
ATOM   4803  C  CD1 . PHE   C  3  129 ? 33.438  -90.893  15.138  1.00 93.21  ? 127 PHE   C CD1 1 
ATOM   4804  C  CD2 . PHE   C  3  129 ? 31.146  -91.318  15.636  1.00 93.97  ? 127 PHE   C CD2 1 
ATOM   4805  C  CE1 . PHE   C  3  129 ? 33.765  -92.175  15.552  1.00 93.07  ? 127 PHE   C CE1 1 
ATOM   4806  C  CE2 . PHE   C  3  129 ? 31.475  -92.600  16.050  1.00 93.26  ? 127 PHE   C CE2 1 
ATOM   4807  C  CZ  . PHE   C  3  129 ? 32.783  -93.025  16.007  1.00 93.95  ? 127 PHE   C CZ  1 
ATOM   4808  N  N   . GLY   C  3  130 ? 33.197  -85.949  15.058  1.00 95.42  ? 128 GLY   C N   1 
ATOM   4809  C  CA  . GLY   C  3  130 ? 33.395  -84.669  14.353  1.00 95.80  ? 128 GLY   C CA  1 
ATOM   4810  C  C   . GLY   C  3  130 ? 33.594  -84.912  12.871  1.00 92.27  ? 128 GLY   C C   1 
ATOM   4811  O  O   . GLY   C  3  130 ? 34.634  -84.482  12.335  1.00 92.11  ? 128 GLY   C O   1 
ATOM   4812  N  N   . VAL   C  3  131 ? 32.641  -85.608  12.242  1.00 91.14  ? 129 VAL   C N   1 
ATOM   4813  C  CA  . VAL   C  3  131 ? 32.742  -86.110  10.841  1.00 91.14  ? 129 VAL   C CA  1 
ATOM   4814  C  C   . VAL   C  3  131 ? 31.344  -86.142  10.217  1.00 90.51  ? 129 VAL   C C   1 
ATOM   4815  O  O   . VAL   C  3  131 ? 30.398  -86.592  10.893  1.00 91.73  ? 129 VAL   C O   1 
ATOM   4816  C  CB  . VAL   C  3  131 ? 33.394  -87.506  10.787  1.00 90.62  ? 129 VAL   C CB  1 
ATOM   4817  C  CG1 . VAL   C  3  131 ? 33.414  -88.062  9.373   1.00 90.92  ? 129 VAL   C CG1 1 
ATOM   4818  C  CG2 . VAL   C  3  131 ? 34.799  -87.505  11.368  1.00 92.54  ? 129 VAL   C CG2 1 
ATOM   4819  N  N   . SER   C  3  132 ? 31.243  -85.666  8.975   1.00 92.30  ? 130 SER   C N   1 
ATOM   4820  C  CA  . SER   C  3  132 ? 30.155  -85.970  8.011   1.00 93.45  ? 130 SER   C CA  1 
ATOM   4821  C  C   . SER   C  3  132 ? 30.771  -86.775  6.867   1.00 91.36  ? 130 SER   C C   1 
ATOM   4822  O  O   . SER   C  3  132 ? 31.941  -86.510  6.532   1.00 89.96  ? 130 SER   C O   1 
ATOM   4823  C  CB  . SER   C  3  132 ? 29.491  -84.717  7.507   1.00 95.48  ? 130 SER   C CB  1 
ATOM   4824  O  OG  . SER   C  3  132 ? 28.750  -84.086  8.540   1.00 100.65 ? 130 SER   C OG  1 
ATOM   4825  N  N   . THR   C  3  133 ? 30.033  -87.735  6.310   1.00 91.22  ? 131 THR   C N   1 
ATOM   4826  C  CA  . THR   C  3  133 ? 30.544  -88.652  5.260   1.00 94.19  ? 131 THR   C CA  1 
ATOM   4827  C  C   . THR   C  3  133 ? 29.702  -88.521  3.990   1.00 93.75  ? 131 THR   C C   1 
ATOM   4828  O  O   . THR   C  3  133 ? 28.482  -88.277  4.099   1.00 90.46  ? 131 THR   C O   1 
ATOM   4829  C  CB  . THR   C  3  133 ? 30.578  -90.108  5.744   1.00 94.16  ? 131 THR   C CB  1 
ATOM   4830  O  OG1 . THR   C  3  133 ? 29.245  -90.538  6.024   1.00 94.78  ? 131 THR   C OG1 1 
ATOM   4831  C  CG2 . THR   C  3  133 ? 31.442  -90.294  6.971   1.00 95.28  ? 131 THR   C CG2 1 
ATOM   4832  N  N   . LEU   C  3  134 ? 30.364  -88.654  2.839   1.00 96.03  ? 132 LEU   C N   1 
ATOM   4833  C  CA  . LEU   C  3  134 ? 29.745  -88.990  1.533   1.00 97.11  ? 132 LEU   C CA  1 
ATOM   4834  C  C   . LEU   C  3  134 ? 30.085  -90.449  1.228   1.00 96.12  ? 132 LEU   C C   1 
ATOM   4835  O  O   . LEU   C  3  134 ? 31.288  -90.771  1.181   1.00 93.80  ? 132 LEU   C O   1 
ATOM   4836  C  CB  . LEU   C  3  134 ? 30.297  -88.065  0.446   1.00 98.60  ? 132 LEU   C CB  1 
ATOM   4837  C  CG  . LEU   C  3  134 ? 30.015  -86.576  0.627   1.00 99.13  ? 132 LEU   C CG  1 
ATOM   4838  C  CD1 . LEU   C  3  134 ? 30.821  -85.760  -0.372  1.00 100.47 ? 132 LEU   C CD1 1 
ATOM   4839  C  CD2 . LEU   C  3  134 ? 28.529  -86.281  0.489   1.00 99.58  ? 132 LEU   C CD2 1 
ATOM   4840  N  N   . ILE   C  3  135 ? 29.067  -91.293  1.061   1.00 96.68  ? 133 ILE   C N   1 
ATOM   4841  C  CA  . ILE   C  3  135 ? 29.226  -92.741  0.740   1.00 96.90  ? 133 ILE   C CA  1 
ATOM   4842  C  C   . ILE   C  3  135 ? 28.612  -92.988  -0.639  1.00 96.33  ? 133 ILE   C C   1 
ATOM   4843  O  O   . ILE   C  3  135 ? 27.408  -92.714  -0.810  1.00 94.30  ? 133 ILE   C O   1 
ATOM   4844  C  CB  . ILE   C  3  135 ? 28.599  -93.621  1.838   1.00 95.52  ? 133 ILE   C CB  1 
ATOM   4845  C  CG1 . ILE   C  3  135 ? 29.271  -93.372  3.190   1.00 97.28  ? 133 ILE   C CG1 1 
ATOM   4846  C  CG2 . ILE   C  3  135 ? 28.649  -95.090  1.443   1.00 94.92  ? 133 ILE   C CG2 1 
ATOM   4847  C  CD1 . ILE   C  3  135 ? 28.514  -93.923  4.376   1.00 97.40  ? 133 ILE   C CD1 1 
ATOM   4848  N  N   . ALA   C  3  136 ? 29.424  -93.474  -1.581  1.00 97.65  ? 134 ALA   C N   1 
ATOM   4849  C  CA  . ALA   C  3  136 ? 29.056  -93.653  -3.003  1.00 100.77 ? 134 ALA   C CA  1 
ATOM   4850  C  C   . ALA   C  3  136 ? 29.465  -95.049  -3.480  1.00 103.03 ? 134 ALA   C C   1 
ATOM   4851  O  O   . ALA   C  3  136 ? 30.462  -95.589  -2.959  1.00 105.92 ? 134 ALA   C O   1 
ATOM   4852  C  CB  . ALA   C  3  136 ? 29.707  -92.576  -3.832  1.00 101.13 ? 134 ALA   C CB  1 
ATOM   4853  N  N   . GLY   C  3  137 ? 28.716  -95.603  -4.437  1.00 104.83 ? 135 GLY   C N   1 
ATOM   4854  C  CA  . GLY   C  3  137 ? 28.997  -96.917  -5.045  1.00 107.12 ? 135 GLY   C CA  1 
ATOM   4855  C  C   . GLY   C  3  137 ? 27.822  -97.453  -5.844  1.00 106.83 ? 135 GLY   C C   1 
ATOM   4856  O  O   . GLY   C  3  137 ? 26.947  -96.652  -6.232  1.00 105.82 ? 135 GLY   C O   1 
ATOM   4857  N  N   . PHE   C  3  138 ? 27.811  -98.769  -6.076  1.00 107.95 ? 136 PHE   C N   1 
ATOM   4858  C  CA  . PHE   C  3  138 ? 26.772  -99.505  -6.843  1.00 108.99 ? 136 PHE   C CA  1 
ATOM   4859  C  C   . PHE   C  3  138 ? 26.417  -100.805 -6.118  1.00 109.60 ? 136 PHE   C C   1 
ATOM   4860  O  O   . PHE   C  3  138 ? 27.341  -101.563 -5.772  1.00 111.51 ? 136 PHE   C O   1 
ATOM   4861  C  CB  . PHE   C  3  138 ? 27.274  -99.813  -8.254  1.00 110.07 ? 136 PHE   C CB  1 
ATOM   4862  C  CG  . PHE   C  3  138 ? 27.397  -98.606  -9.145  1.00 110.59 ? 136 PHE   C CG  1 
ATOM   4863  C  CD1 . PHE   C  3  138 ? 28.550  -97.837  -9.145  1.00 111.51 ? 136 PHE   C CD1 1 
ATOM   4864  C  CD2 . PHE   C  3  138 ? 26.355  -98.237  -9.981  1.00 110.66 ? 136 PHE   C CD2 1 
ATOM   4865  C  CE1 . PHE   C  3  138 ? 28.660  -96.725  -9.964  1.00 112.64 ? 136 PHE   C CE1 1 
ATOM   4866  C  CE2 . PHE   C  3  138 ? 26.467  -97.125  -10.800 1.00 111.79 ? 136 PHE   C CE2 1 
ATOM   4867  C  CZ  . PHE   C  3  138 ? 27.617  -96.372  -10.790 1.00 112.33 ? 136 PHE   C CZ  1 
ATOM   4868  N  N   . ASP   C  3  139 ? 25.121  -101.062 -5.922  1.00 107.60 ? 137 ASP   C N   1 
ATOM   4869  C  CA  . ASP   C  3  139 ? 24.610  -102.314 -5.303  1.00 107.95 ? 137 ASP   C CA  1 
ATOM   4870  C  C   . ASP   C  3  139 ? 25.065  -103.496 -6.157  1.00 109.70 ? 137 ASP   C C   1 
ATOM   4871  O  O   . ASP   C  3  139 ? 25.211  -103.359 -7.369  1.00 107.42 ? 137 ASP   C O   1 
ATOM   4872  C  CB  . ASP   C  3  139 ? 23.087  -102.279 -5.152  1.00 110.59 ? 137 ASP   C CB  1 
ATOM   4873  C  CG  . ASP   C  3  139 ? 22.582  -101.192 -4.217  1.00 110.04 ? 137 ASP   C CG  1 
ATOM   4874  O  OD1 . ASP   C  3  139 ? 23.418  -100.572 -3.526  1.00 111.69 ? 137 ASP   C OD1 1 
ATOM   4875  O  OD2 . ASP   C  3  139 ? 21.355  -100.974 -4.187  1.00 112.09 ? 137 ASP   C OD2 1 
ATOM   4876  N  N   . PRO   C  3  140 ? 25.338  -104.678 -5.553  1.00 111.59 ? 138 PRO   C N   1 
ATOM   4877  C  CA  . PRO   C  3  140 ? 25.675  -105.878 -6.319  1.00 113.51 ? 138 PRO   C CA  1 
ATOM   4878  C  C   . PRO   C  3  140 ? 24.710  -106.122 -7.491  1.00 115.77 ? 138 PRO   C C   1 
ATOM   4879  O  O   . PRO   C  3  140 ? 23.510  -106.044 -7.282  1.00 117.09 ? 138 PRO   C O   1 
ATOM   4880  C  CB  . PRO   C  3  140 ? 25.560  -107.000 -5.276  1.00 111.57 ? 138 PRO   C CB  1 
ATOM   4881  C  CG  . PRO   C  3  140 ? 25.918  -106.324 -3.974  1.00 110.90 ? 138 PRO   C CG  1 
ATOM   4882  C  CD  . PRO   C  3  140 ? 25.370  -104.917 -4.101  1.00 110.56 ? 138 PRO   C CD  1 
ATOM   4883  N  N   . ARG   C  3  141 ? 25.259  -106.384 -8.683  1.00 116.39 ? 139 ARG   C N   1 
ATOM   4884  C  CA  . ARG   C  3  141 ? 24.501  -106.714 -9.922  1.00 121.10 ? 139 ARG   C CA  1 
ATOM   4885  C  C   . ARG   C  3  141 ? 23.512  -105.587 -10.252 1.00 122.98 ? 139 ARG   C C   1 
ATOM   4886  O  O   . ARG   C  3  141 ? 22.399  -105.897 -10.723 1.00 125.28 ? 139 ARG   C O   1 
ATOM   4887  C  CB  . ARG   C  3  141 ? 23.760  -108.046 -9.755  1.00 123.48 ? 139 ARG   C CB  1 
ATOM   4888  C  CG  . ARG   C  3  141 ? 24.648  -109.226 -9.386  1.00 122.79 ? 139 ARG   C CG  1 
ATOM   4889  C  CD  . ARG   C  3  141 ? 23.831  -110.458 -9.054  1.00 125.70 ? 139 ARG   C CD  1 
ATOM   4890  N  NE  . ARG   C  3  141 ? 22.907  -110.215 -7.952  1.00 127.34 ? 139 ARG   C NE  1 
ATOM   4891  C  CZ  . ARG   C  3  141 ? 23.245  -110.147 -6.663  1.00 126.71 ? 139 ARG   C CZ  1 
ATOM   4892  N  NH1 . ARG   C  3  141 ? 24.504  -110.301 -6.285  1.00 130.24 ? 139 ARG   C NH1 1 
ATOM   4893  N  NH2 . ARG   C  3  141 ? 22.315  -109.919 -5.751  1.00 124.99 ? 139 ARG   C NH2 1 
ATOM   4894  N  N   . ASP   C  3  142 ? 23.901  -104.329 -10.014 1.00 122.22 ? 140 ASP   C N   1 
ATOM   4895  C  CA  . ASP   C  3  142 ? 23.061  -103.124 -10.256 1.00 119.80 ? 140 ASP   C CA  1 
ATOM   4896  C  C   . ASP   C  3  142 ? 23.934  -102.027 -10.871 1.00 120.44 ? 140 ASP   C C   1 
ATOM   4897  O  O   . ASP   C  3  142 ? 25.096  -101.891 -10.442 1.00 117.60 ? 140 ASP   C O   1 
ATOM   4898  C  CB  . ASP   C  3  142 ? 22.393  -102.644 -8.964  1.00 117.16 ? 140 ASP   C CB  1 
ATOM   4899  C  CG  . ASP   C  3  142 ? 21.339  -101.570 -9.170  1.00 115.19 ? 140 ASP   C CG  1 
ATOM   4900  O  OD1 . ASP   C  3  142 ? 20.477  -101.757 -10.048 1.00 115.97 ? 140 ASP   C OD1 1 
ATOM   4901  O  OD2 . ASP   C  3  142 ? 21.391  -100.552 -8.450  1.00 111.57 ? 140 ASP   C OD2 1 
ATOM   4902  N  N   . ASP   C  3  143 ? 23.384  -101.276 -11.830 1.00 121.51 ? 141 ASP   C N   1 
ATOM   4903  C  CA  . ASP   C  3  143 ? 24.110  -100.235 -12.610 1.00 124.85 ? 141 ASP   C CA  1 
ATOM   4904  C  C   . ASP   C  3  143 ? 23.578  -98.834  -12.271 1.00 126.22 ? 141 ASP   C C   1 
ATOM   4905  O  O   . ASP   C  3  143 ? 24.064  -97.868  -12.891 1.00 127.62 ? 141 ASP   C O   1 
ATOM   4906  C  CB  . ASP   C  3  143 ? 24.030  -100.510 -14.116 1.00 126.72 ? 141 ASP   C CB  1 
ATOM   4907  C  CG  . ASP   C  3  143 ? 22.625  -100.732 -14.657 1.00 127.05 ? 141 ASP   C CG  1 
ATOM   4908  O  OD1 . ASP   C  3  143 ? 21.658  -100.500 -13.904 1.00 129.92 ? 141 ASP   C OD1 1 
ATOM   4909  O  OD2 . ASP   C  3  143 ? 22.510  -101.140 -15.829 1.00 128.63 ? 141 ASP   C OD2 1 
ATOM   4910  N  N   . GLU   C  3  144 ? 22.631  -98.718  -11.332 1.00 125.77 ? 142 GLU   C N   1 
ATOM   4911  C  CA  . GLU   C  3  144 ? 22.075  -97.414  -10.877 1.00 123.27 ? 142 GLU   C CA  1 
ATOM   4912  C  C   . GLU   C  3  144 ? 23.045  -96.785  -9.877  1.00 121.86 ? 142 GLU   C C   1 
ATOM   4913  O  O   . GLU   C  3  144 ? 23.375  -97.407  -8.867  1.00 118.80 ? 142 GLU   C O   1 
ATOM   4914  C  CB  . GLU   C  3  144 ? 20.690  -97.590  -10.253 1.00 127.16 ? 142 GLU   C CB  1 
ATOM   4915  C  CG  . GLU   C  3  144 ? 19.961  -96.276  -10.041 1.00 128.73 ? 142 GLU   C CG  1 
ATOM   4916  C  CD  . GLU   C  3  144 ? 18.779  -96.352  -9.092  1.00 131.21 ? 142 GLU   C CD  1 
ATOM   4917  O  OE1 . GLU   C  3  144 ? 18.647  -95.446  -8.247  1.00 134.37 ? 142 GLU   C OE1 1 
ATOM   4918  O  OE2 . GLU   C  3  144 ? 17.993  -97.316  -9.203  1.00 135.18 ? 142 GLU   C OE2 1 
ATOM   4919  N  N   . PRO   C  3  145 ? 23.530  -95.541  -10.118 1.00 114.91 ? 143 PRO   C N   1 
ATOM   4920  C  CA  . PRO   C  3  145 ? 24.468  -94.889  -9.205  1.00 109.91 ? 143 PRO   C CA  1 
ATOM   4921  C  C   . PRO   C  3  145 ? 23.804  -94.560  -7.861  1.00 105.53 ? 143 PRO   C C   1 
ATOM   4922  O  O   . PRO   C  3  145 ? 22.616  -94.288  -7.846  1.00 107.72 ? 143 PRO   C O   1 
ATOM   4923  C  CB  . PRO   C  3  145 ? 24.892  -93.599  -9.929  1.00 109.92 ? 143 PRO   C CB  1 
ATOM   4924  C  CG  . PRO   C  3  145 ? 24.412  -93.772  -11.358 1.00 112.37 ? 143 PRO   C CG  1 
ATOM   4925  C  CD  . PRO   C  3  145 ? 23.210  -94.689  -11.272 1.00 114.61 ? 143 PRO   C CD  1 
ATOM   4926  N  N   . LYS   C  3  146 ? 24.586  -94.603  -6.780  1.00 103.35 ? 144 LYS   C N   1 
ATOM   4927  C  CA  . LYS   C  3  146 ? 24.129  -94.338  -5.391  1.00 100.97 ? 144 LYS   C CA  1 
ATOM   4928  C  C   . LYS   C  3  146 ? 25.096  -93.357  -4.722  1.00 99.10  ? 144 LYS   C C   1 
ATOM   4929  O  O   . LYS   C  3  146 ? 26.306  -93.651  -4.694  1.00 97.19  ? 144 LYS   C O   1 
ATOM   4930  C  CB  . LYS   C  3  146 ? 24.064  -95.643  -4.593  1.00 102.70 ? 144 LYS   C CB  1 
ATOM   4931  C  CG  . LYS   C  3  146 ? 23.226  -96.751  -5.215  1.00 103.22 ? 144 LYS   C CG  1 
ATOM   4932  C  CD  . LYS   C  3  146 ? 21.742  -96.552  -5.035  1.00 104.84 ? 144 LYS   C CD  1 
ATOM   4933  C  CE  . LYS   C  3  146 ? 20.930  -97.665  -5.659  1.00 107.06 ? 144 LYS   C CE  1 
ATOM   4934  N  NZ  . LYS   C  3  146 ? 19.533  -97.656  -5.166  1.00 109.24 ? 144 LYS   C NZ  1 
ATOM   4935  N  N   . LEU   C  3  147 ? 24.574  -92.237  -4.217  1.00 97.81  ? 145 LEU   C N   1 
ATOM   4936  C  CA  . LEU   C  3  147 ? 25.313  -91.260  -3.373  1.00 95.85  ? 145 LEU   C CA  1 
ATOM   4937  C  C   . LEU   C  3  147 ? 24.490  -90.984  -2.113  1.00 92.15  ? 145 LEU   C C   1 
ATOM   4938  O  O   . LEU   C  3  147 ? 23.306  -90.619  -2.249  1.00 90.87  ? 145 LEU   C O   1 
ATOM   4939  C  CB  . LEU   C  3  147 ? 25.553  -89.973  -4.168  1.00 95.48  ? 145 LEU   C CB  1 
ATOM   4940  C  CG  . LEU   C  3  147 ? 26.266  -88.853  -3.411  1.00 96.52  ? 145 LEU   C CG  1 
ATOM   4941  C  CD1 . LEU   C  3  147 ? 27.745  -89.168  -3.234  1.00 95.05  ? 145 LEU   C CD1 1 
ATOM   4942  C  CD2 . LEU   C  3  147 ? 26.086  -87.520  -4.119  1.00 97.96  ? 145 LEU   C CD2 1 
ATOM   4943  N  N   . TYR   C  3  148 ? 25.103  -91.164  -0.940  1.00 90.65  ? 146 TYR   C N   1 
ATOM   4944  C  CA  . TYR   C  3  148 ? 24.488  -90.915  0.388   1.00 90.78  ? 146 TYR   C CA  1 
ATOM   4945  C  C   . TYR   C  3  148 ? 25.399  -89.999  1.211   1.00 89.23  ? 146 TYR   C C   1 
ATOM   4946  O  O   . TYR   C  3  148 ? 26.630  -90.004  1.002   1.00 87.26  ? 146 TYR   C O   1 
ATOM   4947  C  CB  . TYR   C  3  148 ? 24.229  -92.233  1.123   1.00 89.70  ? 146 TYR   C CB  1 
ATOM   4948  C  CG  . TYR   C  3  148 ? 22.983  -92.964  0.690   1.00 90.91  ? 146 TYR   C CG  1 
ATOM   4949  C  CD1 . TYR   C  3  148 ? 23.010  -93.871  -0.357  1.00 90.04  ? 146 TYR   C CD1 1 
ATOM   4950  C  CD2 . TYR   C  3  148 ? 21.772  -92.751  1.331   1.00 89.95  ? 146 TYR   C CD2 1 
ATOM   4951  C  CE1 . TYR   C  3  148 ? 21.867  -94.543  -0.761  1.00 89.85  ? 146 TYR   C CE1 1 
ATOM   4952  C  CE2 . TYR   C  3  148 ? 20.620  -93.414  0.941   1.00 89.36  ? 146 TYR   C CE2 1 
ATOM   4953  C  CZ  . TYR   C  3  148 ? 20.667  -94.313  -0.109  1.00 89.11  ? 146 TYR   C CZ  1 
ATOM   4954  O  OH  . TYR   C  3  148 ? 19.530  -94.962  -0.492  1.00 91.73  ? 146 TYR   C OH  1 
ATOM   4955  N  N   . GLN   C  3  149 ? 24.790  -89.237  2.121   1.00 91.34  ? 147 GLN   C N   1 
ATOM   4956  C  CA  . GLN   C  3  149 ? 25.477  -88.322  3.067   1.00 93.96  ? 147 GLN   C CA  1 
ATOM   4957  C  C   . GLN   C  3  149 ? 25.024  -88.669  4.487   1.00 91.44  ? 147 GLN   C C   1 
ATOM   4958  O  O   . GLN   C  3  149 ? 23.817  -88.908  4.670   1.00 89.66  ? 147 GLN   C O   1 
ATOM   4959  C  CB  . GLN   C  3  149 ? 25.135  -86.867  2.742   1.00 95.12  ? 147 GLN   C CB  1 
ATOM   4960  C  CG  . GLN   C  3  149 ? 26.021  -85.858  3.460   1.00 97.87  ? 147 GLN   C CG  1 
ATOM   4961  C  CD  . GLN   C  3  149 ? 25.240  -84.813  4.221   1.00 98.25  ? 147 GLN   C CD  1 
ATOM   4962  O  OE1 . GLN   C  3  149 ? 25.513  -84.547  5.388   1.00 106.79 ? 147 GLN   C OE1 1 
ATOM   4963  N  NE2 . GLN   C  3  149 ? 24.257  -84.209  3.572   1.00 96.16  ? 147 GLN   C NE2 1 
ATOM   4964  N  N   . THR   C  3  150 ? 25.956  -88.711  5.442   1.00 91.59  ? 148 THR   C N   1 
ATOM   4965  C  CA  . THR   C  3  150 ? 25.667  -88.840  6.896   1.00 94.53  ? 148 THR   C CA  1 
ATOM   4966  C  C   . THR   C  3  150 ? 26.245  -87.620  7.617   1.00 97.03  ? 148 THR   C C   1 
ATOM   4967  O  O   . THR   C  3  150 ? 27.059  -86.902  7.001   1.00 99.52  ? 148 THR   C O   1 
ATOM   4968  C  CB  . THR   C  3  150 ? 26.221  -90.143  7.485   1.00 90.99  ? 148 THR   C CB  1 
ATOM   4969  O  OG1 . THR   C  3  150 ? 27.624  -89.989  7.704   1.00 87.10  ? 148 THR   C OG1 1 
ATOM   4970  C  CG2 . THR   C  3  150 ? 25.965  -91.344  6.602   1.00 92.62  ? 148 THR   C CG2 1 
ATOM   4971  N  N   . GLU   C  3  151 ? 25.836  -87.402  8.868   1.00 102.51 ? 149 GLU   C N   1 
ATOM   4972  C  CA  . GLU   C  3  151 ? 26.332  -86.281  9.707   1.00 105.21 ? 149 GLU   C CA  1 
ATOM   4973  C  C   . GLU   C  3  151 ? 26.282  -86.685  11.181  1.00 104.09 ? 149 GLU   C C   1 
ATOM   4974  O  O   . GLU   C  3  151 ? 25.589  -87.634  11.547  1.00 107.02 ? 149 GLU   C O   1 
ATOM   4975  C  CB  . GLU   C  3  151 ? 25.546  -85.008  9.377   1.00 109.59 ? 149 GLU   C CB  1 
ATOM   4976  C  CG  . GLU   C  3  151 ? 24.116  -84.993  9.888   1.00 114.22 ? 149 GLU   C CG  1 
ATOM   4977  C  CD  . GLU   C  3  151 ? 23.334  -83.753  9.481   1.00 118.59 ? 149 GLU   C CD  1 
ATOM   4978  O  OE1 . GLU   C  3  151 ? 22.794  -83.072  10.380  1.00 114.77 ? 149 GLU   C OE1 1 
ATOM   4979  O  OE2 . GLU   C  3  151 ? 23.267  -83.468  8.266   1.00 127.24 ? 149 GLU   C OE2 1 
ATOM   4980  N  N   . PRO   C  3  152 ? 27.026  -85.975  12.063  1.00 102.18 ? 150 PRO   C N   1 
ATOM   4981  C  CA  . PRO   C  3  152 ? 27.220  -86.394  13.455  1.00 99.79  ? 150 PRO   C CA  1 
ATOM   4982  C  C   . PRO   C  3  152 ? 25.960  -86.801  14.237  1.00 98.21  ? 150 PRO   C C   1 
ATOM   4983  O  O   . PRO   C  3  152 ? 26.069  -87.688  15.071  1.00 96.32  ? 150 PRO   C O   1 
ATOM   4984  C  CB  . PRO   C  3  152 ? 27.820  -85.138  14.103  1.00 101.45 ? 150 PRO   C CB  1 
ATOM   4985  C  CG  . PRO   C  3  152 ? 28.590  -84.484  12.982  1.00 102.36 ? 150 PRO   C CG  1 
ATOM   4986  C  CD  . PRO   C  3  152 ? 27.737  -84.723  11.757  1.00 102.69 ? 150 PRO   C CD  1 
ATOM   4987  N  N   . SER   C  3  153 ? 24.825  -86.140  13.978  1.00 97.27  ? 151 SER   C N   1 
ATOM   4988  C  CA  . SER   C  3  153 ? 23.516  -86.408  14.635  1.00 96.03  ? 151 SER   C CA  1 
ATOM   4989  C  C   . SER   C  3  153 ? 23.126  -87.873  14.422  1.00 93.60  ? 151 SER   C C   1 
ATOM   4990  O  O   . SER   C  3  153 ? 22.623  -88.493  15.378  1.00 93.89  ? 151 SER   C O   1 
ATOM   4991  C  CB  . SER   C  3  153 ? 22.440  -85.489  14.126  1.00 96.82  ? 151 SER   C CB  1 
ATOM   4992  O  OG  . SER   C  3  153 ? 22.128  -85.783  12.774  1.00 97.85  ? 151 SER   C OG  1 
ATOM   4993  N  N   . GLY   C  3  154 ? 23.357  -88.390  13.211  1.00 92.68  ? 152 GLY   C N   1 
ATOM   4994  C  CA  . GLY   C  3  154 ? 23.032  -89.773  12.816  1.00 91.42  ? 152 GLY   C CA  1 
ATOM   4995  C  C   . GLY   C  3  154 ? 22.041  -89.830  11.665  1.00 92.93  ? 152 GLY   C C   1 
ATOM   4996  O  O   . GLY   C  3  154 ? 21.738  -90.950  11.217  1.00 89.47  ? 152 GLY   C O   1 
ATOM   4997  N  N   . ILE   C  3  155 ? 21.530  -88.684  11.205  1.00 93.68  ? 153 ILE   C N   1 
ATOM   4998  C  CA  . ILE   C  3  155 ? 20.622  -88.627  10.021  1.00 93.90  ? 153 ILE   C CA  1 
ATOM   4999  C  C   . ILE   C  3  155 ? 21.462  -88.895  8.770   1.00 91.81  ? 153 ILE   C C   1 
ATOM   5000  O  O   . ILE   C  3  155 ? 22.644  -88.490  8.739   1.00 88.83  ? 153 ILE   C O   1 
ATOM   5001  C  CB  . ILE   C  3  155 ? 19.829  -87.304  9.931   1.00 98.25  ? 153 ILE   C CB  1 
ATOM   5002  C  CG1 . ILE   C  3  155 ? 20.732  -86.080  9.735   1.00 104.74 ? 153 ILE   C CG1 1 
ATOM   5003  C  CG2 . ILE   C  3  155 ? 18.913  -87.155  11.138  1.00 96.00  ? 153 ILE   C CG2 1 
ATOM   5004  C  CD1 . ILE   C  3  155 ? 19.980  -84.791  9.457   1.00 110.14 ? 153 ILE   C CD1 1 
ATOM   5005  N  N   . TYR   C  3  156 ? 20.873  -89.601  7.806   1.00 91.63  ? 154 TYR   C N   1 
ATOM   5006  C  CA  . TYR   C  3  156 ? 21.466  -89.899  6.481   1.00 92.48  ? 154 TYR   C CA  1 
ATOM   5007  C  C   . TYR   C  3  156 ? 20.369  -89.744  5.430   1.00 91.90  ? 154 TYR   C C   1 
ATOM   5008  O  O   . TYR   C  3  156 ? 19.182  -89.883  5.784   1.00 93.43  ? 154 TYR   C O   1 
ATOM   5009  C  CB  . TYR   C  3  156 ? 22.088  -91.298  6.466   1.00 91.31  ? 154 TYR   C CB  1 
ATOM   5010  C  CG  . TYR   C  3  156 ? 21.098  -92.437  6.507   1.00 93.08  ? 154 TYR   C CG  1 
ATOM   5011  C  CD1 . TYR   C  3  156 ? 20.470  -92.797  7.688   1.00 94.28  ? 154 TYR   C CD1 1 
ATOM   5012  C  CD2 . TYR   C  3  156 ? 20.792  -93.161  5.365   1.00 93.18  ? 154 TYR   C CD2 1 
ATOM   5013  C  CE1 . TYR   C  3  156 ? 19.561  -93.842  7.735   1.00 96.02  ? 154 TYR   C CE1 1 
ATOM   5014  C  CE2 . TYR   C  3  156 ? 19.885  -94.207  5.394   1.00 94.83  ? 154 TYR   C CE2 1 
ATOM   5015  C  CZ  . TYR   C  3  156 ? 19.268  -94.549  6.584   1.00 95.39  ? 154 TYR   C CZ  1 
ATOM   5016  O  OH  . TYR   C  3  156 ? 18.377  -95.581  6.621   1.00 100.67 ? 154 TYR   C OH  1 
ATOM   5017  N  N   . SER   C  3  157 ? 20.760  -89.459  4.188   1.00 92.81  ? 155 SER   C N   1 
ATOM   5018  C  CA  . SER   C  3  157 ? 19.830  -89.264  3.047   1.00 95.45  ? 155 SER   C CA  1 
ATOM   5019  C  C   . SER   C  3  157 ? 20.575  -89.426  1.719   1.00 97.48  ? 155 SER   C C   1 
ATOM   5020  O  O   . SER   C  3  157 ? 21.821  -89.354  1.723   1.00 97.66  ? 155 SER   C O   1 
ATOM   5021  C  CB  . SER   C  3  157 ? 19.153  -87.928  3.142   1.00 96.70  ? 155 SER   C CB  1 
ATOM   5022  O  OG  . SER   C  3  157 ? 20.099  -86.900  3.390   1.00 98.27  ? 155 SER   C OG  1 
ATOM   5023  N  N   . SER   C  3  158 ? 19.821  -89.639  0.635   1.00 99.50  ? 156 SER   C N   1 
ATOM   5024  C  CA  . SER   C  3  158 ? 20.330  -89.827  -0.748  1.00 101.33 ? 156 SER   C CA  1 
ATOM   5025  C  C   . SER   C  3  158 ? 20.360  -88.476  -1.468  1.00 99.73  ? 156 SER   C C   1 
ATOM   5026  O  O   . SER   C  3  158 ? 19.387  -87.716  -1.330  1.00 101.96 ? 156 SER   C O   1 
ATOM   5027  C  CB  . SER   C  3  158 ? 19.491  -90.826  -1.500  1.00 102.14 ? 156 SER   C CB  1 
ATOM   5028  O  OG  . SER   C  3  158 ? 20.085  -91.152  -2.748  1.00 105.72 ? 156 SER   C OG  1 
ATOM   5029  N  N   . TRP   C  3  159 ? 21.435  -88.202  -2.211  1.00 99.22  ? 157 TRP   C N   1 
ATOM   5030  C  CA  . TRP   C  3  159 ? 21.656  -86.923  -2.937  1.00 100.63 ? 157 TRP   C CA  1 
ATOM   5031  C  C   . TRP   C  3  159 ? 21.994  -87.204  -4.403  1.00 100.68 ? 157 TRP   C C   1 
ATOM   5032  O  O   . TRP   C  3  159 ? 22.745  -88.158  -4.658  1.00 104.93 ? 157 TRP   C O   1 
ATOM   5033  C  CB  . TRP   C  3  159 ? 22.765  -86.114  -2.258  1.00 102.25 ? 157 TRP   C CB  1 
ATOM   5034  C  CG  . TRP   C  3  159 ? 22.406  -85.634  -0.887  1.00 103.14 ? 157 TRP   C CG  1 
ATOM   5035  C  CD1 . TRP   C  3  159 ? 22.401  -86.363  0.266   1.00 102.69 ? 157 TRP   C CD1 1 
ATOM   5036  C  CD2 . TRP   C  3  159 ? 21.994  -84.305  -0.523  1.00 103.66 ? 157 TRP   C CD2 1 
ATOM   5037  N  NE1 . TRP   C  3  159 ? 22.014  -85.582  1.321   1.00 103.58 ? 157 TRP   C NE1 1 
ATOM   5038  C  CE2 . TRP   C  3  159 ? 21.760  -84.314  0.869   1.00 104.30 ? 157 TRP   C CE2 1 
ATOM   5039  C  CE3 . TRP   C  3  159 ? 21.804  -83.113  -1.232  1.00 105.27 ? 157 TRP   C CE3 1 
ATOM   5040  C  CZ2 . TRP   C  3  159 ? 21.344  -83.177  1.560   1.00 105.03 ? 157 TRP   C CZ2 1 
ATOM   5041  C  CZ3 . TRP   C  3  159 ? 21.393  -81.990  -0.548  1.00 105.81 ? 157 TRP   C CZ3 1 
ATOM   5042  C  CH2 . TRP   C  3  159 ? 21.168  -82.024  0.829   1.00 106.21 ? 157 TRP   C CH2 1 
ATOM   5043  N  N   . SER   C  3  160 ? 21.456  -86.394  -5.320  1.00 100.79 ? 158 SER   C N   1 
ATOM   5044  C  CA  . SER   C  3  160 ? 21.831  -86.371  -6.758  1.00 102.38 ? 158 SER   C CA  1 
ATOM   5045  C  C   . SER   C  3  160 ? 23.258  -85.829  -6.874  1.00 100.37 ? 158 SER   C C   1 
ATOM   5046  O  O   . SER   C  3  160 ? 24.054  -86.372  -7.662  1.00 94.13  ? 158 SER   C O   1 
ATOM   5047  C  CB  . SER   C  3  160 ? 20.860  -85.545  -7.556  1.00 104.48 ? 158 SER   C CB  1 
ATOM   5048  O  OG  . SER   C  3  160 ? 19.532  -86.008  -7.370  1.00 108.90 ? 158 SER   C OG  1 
ATOM   5049  N  N   . ALA   C  3  161 ? 23.544  -84.782  -6.099  1.00 100.26 ? 159 ALA   C N   1 
ATOM   5050  C  CA  . ALA   C  3  161 ? 24.892  -84.216  -5.864  1.00 101.11 ? 159 ALA   C CA  1 
ATOM   5051  C  C   . ALA   C  3  161 ? 24.885  -83.496  -4.514  1.00 100.02 ? 159 ALA   C C   1 
ATOM   5052  O  O   . ALA   C  3  161 ? 23.857  -82.873  -4.180  1.00 99.22  ? 159 ALA   C O   1 
ATOM   5053  C  CB  . ALA   C  3  161 ? 25.271  -83.284  -6.985  1.00 102.78 ? 159 ALA   C CB  1 
ATOM   5054  N  N   . GLN   C  3  162 ? 25.977  -83.597  -3.757  1.00 100.39 ? 160 GLN   C N   1 
ATOM   5055  C  CA  . GLN   C  3  162 ? 26.094  -82.948  -2.428  1.00 100.84 ? 160 GLN   C CA  1 
ATOM   5056  C  C   . GLN   C  3  162 ? 27.562  -82.621  -2.148  1.00 99.27  ? 160 GLN   C C   1 
ATOM   5057  O  O   . GLN   C  3  162 ? 28.450  -83.255  -2.747  1.00 97.97  ? 160 GLN   C O   1 
ATOM   5058  C  CB  . GLN   C  3  162 ? 25.456  -83.839  -1.357  1.00 102.21 ? 160 GLN   C CB  1 
ATOM   5059  C  CG  . GLN   C  3  162 ? 25.655  -83.371  0.082   1.00 104.22 ? 160 GLN   C CG  1 
ATOM   5060  C  CD  . GLN   C  3  162 ? 24.777  -82.216  0.506   1.00 104.81 ? 160 GLN   C CD  1 
ATOM   5061  O  OE1 . GLN   C  3  162 ? 24.301  -82.172  1.636   1.00 109.95 ? 160 GLN   C OE1 1 
ATOM   5062  N  NE2 . GLN   C  3  162 ? 24.553  -81.261  -0.382  1.00 106.86 ? 160 GLN   C NE2 1 
ATOM   5063  N  N   . THR   C  3  163 ? 27.780  -81.637  -1.279  1.00 99.42  ? 161 THR   C N   1 
ATOM   5064  C  CA  . THR   C  3  163 ? 29.105  -81.204  -0.776  1.00 102.61 ? 161 THR   C CA  1 
ATOM   5065  C  C   . THR   C  3  163 ? 29.022  -81.084  0.750   1.00 101.94 ? 161 THR   C C   1 
ATOM   5066  O  O   . THR   C  3  163 ? 27.899  -80.925  1.271   1.00 105.13 ? 161 THR   C O   1 
ATOM   5067  C  CB  . THR   C  3  163 ? 29.544  -79.906  -1.466  1.00 104.82 ? 161 THR   C CB  1 
ATOM   5068  O  OG1 . THR   C  3  163 ? 30.739  -79.435  -0.841  1.00 103.02 ? 161 THR   C OG1 1 
ATOM   5069  C  CG2 . THR   C  3  163 ? 28.482  -78.828  -1.422  1.00 106.29 ? 161 THR   C CG2 1 
ATOM   5070  N  N   . ILE   C  3  164 ? 30.168  -81.193  1.424   1.00 102.44 ? 162 ILE   C N   1 
ATOM   5071  C  CA  . ILE   C  3  164 ? 30.328  -80.998  2.896   1.00 101.28 ? 162 ILE   C CA  1 
ATOM   5072  C  C   . ILE   C  3  164 ? 31.713  -80.392  3.146   1.00 100.52 ? 162 ILE   C C   1 
ATOM   5073  O  O   . ILE   C  3  164 ? 32.582  -80.522  2.260   1.00 98.66  ? 162 ILE   C O   1 
ATOM   5074  C  CB  . ILE   C  3  164 ? 30.141  -82.328  3.654   1.00 100.78 ? 162 ILE   C CB  1 
ATOM   5075  C  CG1 . ILE   C  3  164 ? 30.940  -83.462  3.004   1.00 103.04 ? 162 ILE   C CG1 1 
ATOM   5076  C  CG2 . ILE   C  3  164 ? 28.666  -82.677  3.787   1.00 99.89  ? 162 ILE   C CG2 1 
ATOM   5077  C  CD1 . ILE   C  3  164 ? 31.112  -84.681  3.880   1.00 102.70 ? 162 ILE   C CD1 1 
ATOM   5078  N  N   . GLY   C  3  165 ? 31.903  -79.761  4.307   1.00 100.31 ? 163 GLY   C N   1 
ATOM   5079  C  CA  . GLY   C  3  165 ? 33.179  -79.136  4.706   1.00 104.89 ? 163 GLY   C CA  1 
ATOM   5080  C  C   . GLY   C  3  165 ? 33.114  -77.622  4.612   1.00 105.77 ? 163 GLY   C C   1 
ATOM   5081  O  O   . GLY   C  3  165 ? 31.993  -77.081  4.546   1.00 110.77 ? 163 GLY   C O   1 
ATOM   5082  N  N   . ARG   C  3  166 ? 34.275  -76.959  4.601   1.00 108.79 ? 164 ARG   C N   1 
ATOM   5083  C  CA  . ARG   C  3  166 ? 34.386  -75.475  4.583   1.00 110.96 ? 164 ARG   C CA  1 
ATOM   5084  C  C   . ARG   C  3  166 ? 34.002  -74.949  3.197   1.00 109.99 ? 164 ARG   C C   1 
ATOM   5085  O  O   . ARG   C  3  166 ? 34.409  -75.564  2.191   1.00 106.42 ? 164 ARG   C O   1 
ATOM   5086  C  CB  . ARG   C  3  166 ? 35.793  -75.016  4.984   1.00 113.85 ? 164 ARG   C CB  1 
ATOM   5087  C  CG  . ARG   C  3  166 ? 36.901  -75.386  4.009   1.00 117.03 ? 164 ARG   C CG  1 
ATOM   5088  C  CD  . ARG   C  3  166 ? 38.260  -75.181  4.650   1.00 120.37 ? 164 ARG   C CD  1 
ATOM   5089  N  NE  . ARG   C  3  166 ? 39.366  -75.341  3.715   1.00 126.34 ? 164 ARG   C NE  1 
ATOM   5090  C  CZ  . ARG   C  3  166 ? 40.654  -75.216  4.032   1.00 130.69 ? 164 ARG   C CZ  1 
ATOM   5091  N  NH1 . ARG   C  3  166 ? 41.580  -75.378  3.102   1.00 135.19 ? 164 ARG   C NH1 1 
ATOM   5092  N  NH2 . ARG   C  3  166 ? 41.018  -74.931  5.271   1.00 134.80 ? 164 ARG   C NH2 1 
ATOM   5093  N  N   . ASN   C  3  167 ? 33.237  -73.853  3.168   1.00 110.06 ? 165 ASN   C N   1 
ATOM   5094  C  CA  . ASN   C  3  167 ? 32.749  -73.176  1.937   1.00 112.00 ? 165 ASN   C CA  1 
ATOM   5095  C  C   . ASN   C  3  167 ? 31.851  -74.128  1.137   1.00 112.27 ? 165 ASN   C C   1 
ATOM   5096  O  O   . ASN   C  3  167 ? 31.690  -73.898  -0.075  1.00 112.50 ? 165 ASN   C O   1 
ATOM   5097  C  CB  . ASN   C  3  167 ? 33.913  -72.659  1.087   1.00 113.17 ? 165 ASN   C CB  1 
ATOM   5098  C  CG  . ASN   C  3  167 ? 34.773  -71.648  1.814   1.00 114.38 ? 165 ASN   C CG  1 
ATOM   5099  O  OD1 . ASN   C  3  167 ? 35.958  -71.885  2.043   1.00 110.21 ? 165 ASN   C OD1 1 
ATOM   5100  N  ND2 . ASN   C  3  167 ? 34.186  -70.519  2.181   1.00 115.57 ? 165 ASN   C ND2 1 
ATOM   5101  N  N   . SER   C  3  168 ? 31.273  -75.145  1.785   1.00 111.86 ? 166 SER   C N   1 
ATOM   5102  C  CA  . SER   C  3  168 ? 30.368  -76.135  1.143   1.00 112.59 ? 166 SER   C CA  1 
ATOM   5103  C  C   . SER   C  3  168 ? 29.093  -75.429  0.665   1.00 116.09 ? 166 SER   C C   1 
ATOM   5104  O  O   . SER   C  3  168 ? 28.503  -75.893  -0.327  1.00 120.08 ? 166 SER   C O   1 
ATOM   5105  C  CB  . SER   C  3  168 ? 30.045  -77.282  2.063   1.00 111.04 ? 166 SER   C CB  1 
ATOM   5106  O  OG  . SER   C  3  168 ? 29.467  -76.816  3.271   1.00 110.80 ? 166 SER   C OG  1 
ATOM   5107  N  N   . LYS   C  3  169 ? 28.693  -74.348  1.341   1.00 116.57 ? 167 LYS   C N   1 
ATOM   5108  C  CA  . LYS   C  3  169 ? 27.475  -73.564  1.004   1.00 117.12 ? 167 LYS   C CA  1 
ATOM   5109  C  C   . LYS   C  3  169 ? 27.676  -72.883  -0.356  1.00 113.88 ? 167 LYS   C C   1 
ATOM   5110  O  O   . LYS   C  3  169 ? 26.692  -72.798  -1.114  1.00 110.28 ? 167 LYS   C O   1 
ATOM   5111  C  CB  . LYS   C  3  169 ? 27.154  -72.559  2.115   1.00 121.27 ? 167 LYS   C CB  1 
ATOM   5112  C  CG  . LYS   C  3  169 ? 25.678  -72.209  2.256   1.00 126.43 ? 167 LYS   C CG  1 
ATOM   5113  C  CD  . LYS   C  3  169 ? 25.268  -71.882  3.676   1.00 131.96 ? 167 LYS   C CD  1 
ATOM   5114  C  CE  . LYS   C  3  169 ? 25.837  -70.569  4.172   1.00 136.12 ? 167 LYS   C CE  1 
ATOM   5115  N  NZ  . LYS   C  3  169 ? 25.598  -70.385  5.623   1.00 139.36 ? 167 LYS   C NZ  1 
ATOM   5116  N  N   . THR   C  3  170 ? 28.903  -72.435  -0.651  1.00 115.12 ? 168 THR   C N   1 
ATOM   5117  C  CA  . THR   C  3  170 ? 29.292  -71.787  -1.936  1.00 118.57 ? 168 THR   C CA  1 
ATOM   5118  C  C   . THR   C  3  170 ? 29.200  -72.801  -3.083  1.00 119.15 ? 168 THR   C C   1 
ATOM   5119  O  O   . THR   C  3  170 ? 28.643  -72.439  -4.138  1.00 122.45 ? 168 THR   C O   1 
ATOM   5120  C  CB  . THR   C  3  170 ? 30.702  -71.184  -1.871  1.00 119.76 ? 168 THR   C CB  1 
ATOM   5121  O  OG1 . THR   C  3  170 ? 30.761  -70.282  -0.765  1.00 120.29 ? 168 THR   C OG1 1 
ATOM   5122  C  CG2 . THR   C  3  170 ? 31.092  -70.456  -3.140  1.00 120.68 ? 168 THR   C CG2 1 
ATOM   5123  N  N   . VAL   C  3  171 ? 29.741  -74.010  -2.892  1.00 116.49 ? 169 VAL   C N   1 
ATOM   5124  C  CA  . VAL   C  3  171 ? 29.795  -75.074  -3.944  1.00 115.22 ? 169 VAL   C CA  1 
ATOM   5125  C  C   . VAL   C  3  171 ? 28.408  -75.720  -4.075  1.00 111.00 ? 169 VAL   C C   1 
ATOM   5126  O  O   . VAL   C  3  171 ? 28.059  -76.110  -5.203  1.00 113.23 ? 169 VAL   C O   1 
ATOM   5127  C  CB  . VAL   C  3  171 ? 30.917  -76.115  -3.715  1.00 114.79 ? 169 VAL   C CB  1 
ATOM   5128  C  CG1 . VAL   C  3  171 ? 31.322  -76.266  -2.260  1.00 115.29 ? 169 VAL   C CG1 1 
ATOM   5129  C  CG2 . VAL   C  3  171 ? 30.573  -77.476  -4.305  1.00 114.23 ? 169 VAL   C CG2 1 
ATOM   5130  N  N   . ARG   C  3  172 ? 27.639  -75.821  -2.984  1.00 108.52 ? 170 ARG   C N   1 
ATOM   5131  C  CA  . ARG   C  3  172 ? 26.231  -76.304  -3.028  1.00 109.24 ? 170 ARG   C CA  1 
ATOM   5132  C  C   . ARG   C  3  172 ? 25.414  -75.348  -3.907  1.00 112.02 ? 170 ARG   C C   1 
ATOM   5133  O  O   . ARG   C  3  172 ? 24.662  -75.845  -4.767  1.00 110.21 ? 170 ARG   C O   1 
ATOM   5134  C  CB  . ARG   C  3  172 ? 25.620  -76.415  -1.628  1.00 109.56 ? 170 ARG   C CB  1 
ATOM   5135  C  CG  . ARG   C  3  172 ? 24.338  -77.237  -1.580  1.00 109.13 ? 170 ARG   C CG  1 
ATOM   5136  C  CD  . ARG   C  3  172 ? 23.765  -77.376  -0.181  1.00 110.15 ? 170 ARG   C CD  1 
ATOM   5137  N  NE  . ARG   C  3  172 ? 24.642  -78.143  0.697   1.00 110.08 ? 170 ARG   C NE  1 
ATOM   5138  C  CZ  . ARG   C  3  172 ? 25.478  -77.637  1.603   1.00 111.26 ? 170 ARG   C CZ  1 
ATOM   5139  N  NH1 . ARG   C  3  172 ? 25.573  -76.331  1.795   1.00 114.21 ? 170 ARG   C NH1 1 
ATOM   5140  N  NH2 . ARG   C  3  172 ? 26.223  -78.453  2.327   1.00 113.84 ? 170 ARG   C NH2 1 
ATOM   5141  N  N   . GLU   C  3  173 ? 25.577  -74.035  -3.698  1.00 114.76 ? 171 GLU   C N   1 
ATOM   5142  C  CA  . GLU   C  3  173 ? 24.963  -72.955  -4.520  1.00 118.56 ? 171 GLU   C CA  1 
ATOM   5143  C  C   . GLU   C  3  173 ? 25.236  -73.240  -6.002  1.00 115.62 ? 171 GLU   C C   1 
ATOM   5144  O  O   . GLU   C  3  173 ? 24.270  -73.229  -6.790  1.00 114.77 ? 171 GLU   C O   1 
ATOM   5145  C  CB  . GLU   C  3  173 ? 25.526  -71.586  -4.127  1.00 122.89 ? 171 GLU   C CB  1 
ATOM   5146  C  CG  . GLU   C  3  173 ? 24.747  -70.408  -4.693  1.00 129.25 ? 171 GLU   C CG  1 
ATOM   5147  C  CD  . GLU   C  3  173 ? 23.610  -69.887  -3.827  1.00 134.74 ? 171 GLU   C CD  1 
ATOM   5148  O  OE1 . GLU   C  3  173 ? 22.643  -69.337  -4.393  1.00 140.05 ? 171 GLU   C OE1 1 
ATOM   5149  O  OE2 . GLU   C  3  173 ? 23.701  -70.013  -2.589  1.00 140.88 ? 171 GLU   C OE2 1 
ATOM   5150  N  N   . PHE   C  3  174 ? 26.504  -73.491  -6.352  1.00 114.25 ? 172 PHE   C N   1 
ATOM   5151  C  CA  . PHE   C  3  174 ? 26.973  -73.769  -7.737  1.00 115.71 ? 172 PHE   C CA  1 
ATOM   5152  C  C   . PHE   C  3  174 ? 26.243  -74.994  -8.300  1.00 115.38 ? 172 PHE   C C   1 
ATOM   5153  O  O   . PHE   C  3  174 ? 25.659  -74.892  -9.396  1.00 113.65 ? 172 PHE   C O   1 
ATOM   5154  C  CB  . PHE   C  3  174 ? 28.490  -73.978  -7.776  1.00 115.42 ? 172 PHE   C CB  1 
ATOM   5155  C  CG  . PHE   C  3  174 ? 29.016  -74.423  -9.117  1.00 118.96 ? 172 PHE   C CG  1 
ATOM   5156  C  CD1 . PHE   C  3  174 ? 29.137  -75.771  -9.419  1.00 119.16 ? 172 PHE   C CD1 1 
ATOM   5157  C  CD2 . PHE   C  3  174 ? 29.373  -73.496  -10.084 1.00 120.58 ? 172 PHE   C CD2 1 
ATOM   5158  C  CE1 . PHE   C  3  174 ? 29.612  -76.180  -10.656 1.00 122.33 ? 172 PHE   C CE1 1 
ATOM   5159  C  CE2 . PHE   C  3  174 ? 29.848  -73.906  -11.320 1.00 122.50 ? 172 PHE   C CE2 1 
ATOM   5160  C  CZ  . PHE   C  3  174 ? 29.965  -75.247  -11.604 1.00 123.46 ? 172 PHE   C CZ  1 
ATOM   5161  N  N   . LEU   C  3  175 ? 26.286  -76.113  -7.570  1.00 113.86 ? 173 LEU   C N   1 
ATOM   5162  C  CA  . LEU   C  3  175 ? 25.679  -77.410  -7.977  1.00 114.58 ? 173 LEU   C CA  1 
ATOM   5163  C  C   . LEU   C  3  175 ? 24.163  -77.253  -8.139  1.00 114.82 ? 173 LEU   C C   1 
ATOM   5164  O  O   . LEU   C  3  175 ? 23.610  -77.899  -9.043  1.00 118.92 ? 173 LEU   C O   1 
ATOM   5165  C  CB  . LEU   C  3  175 ? 25.995  -78.481  -6.928  1.00 113.35 ? 173 LEU   C CB  1 
ATOM   5166  C  CG  . LEU   C  3  175 ? 27.453  -78.931  -6.847  1.00 113.90 ? 173 LEU   C CG  1 
ATOM   5167  C  CD1 . LEU   C  3  175 ? 27.684  -79.764  -5.595  1.00 112.95 ? 173 LEU   C CD1 1 
ATOM   5168  C  CD2 . LEU   C  3  175 ? 27.859  -79.712  -8.088  1.00 114.38 ? 173 LEU   C CD2 1 
ATOM   5169  N  N   . GLU   C  3  176 ? 23.521  -76.436  -7.298  1.00 116.68 ? 174 GLU   C N   1 
ATOM   5170  C  CA  . GLU   C  3  176 ? 22.041  -76.270  -7.267  1.00 121.64 ? 174 GLU   C CA  1 
ATOM   5171  C  C   . GLU   C  3  176 ? 21.543  -75.652  -8.583  1.00 122.87 ? 174 GLU   C C   1 
ATOM   5172  O  O   . GLU   C  3  176 ? 20.399  -75.967  -8.968  1.00 121.97 ? 174 GLU   C O   1 
ATOM   5173  C  CB  . GLU   C  3  176 ? 21.600  -75.446  -6.053  1.00 123.11 ? 174 GLU   C CB  1 
ATOM   5174  C  CG  . GLU   C  3  176 ? 21.442  -76.276  -4.788  1.00 124.02 ? 174 GLU   C CG  1 
ATOM   5175  C  CD  . GLU   C  3  176 ? 20.921  -75.526  -3.572  1.00 126.28 ? 174 GLU   C CD  1 
ATOM   5176  O  OE1 . GLU   C  3  176 ? 20.496  -74.362  -3.727  1.00 129.51 ? 174 GLU   C OE1 1 
ATOM   5177  O  OE2 . GLU   C  3  176 ? 20.942  -76.111  -2.469  1.00 125.47 ? 174 GLU   C OE2 1 
ATOM   5178  N  N   . LYS   C  3  177 ? 22.351  -74.818  -9.251  1.00 125.94 ? 175 LYS   C N   1 
ATOM   5179  C  CA  . LYS   C  3  177 ? 21.969  -74.170  -10.540 1.00 130.39 ? 175 LYS   C CA  1 
ATOM   5180  C  C   . LYS   C  3  177 ? 22.616  -74.897  -11.730 1.00 127.50 ? 175 LYS   C C   1 
ATOM   5181  O  O   . LYS   C  3  177 ? 22.117  -74.703  -12.855 1.00 128.20 ? 175 LYS   C O   1 
ATOM   5182  C  CB  . LYS   C  3  177 ? 22.306  -72.673  -10.542 1.00 136.16 ? 175 LYS   C CB  1 
ATOM   5183  C  CG  . LYS   C  3  177 ? 23.783  -72.302  -10.489 1.00 141.66 ? 175 LYS   C CG  1 
ATOM   5184  C  CD  . LYS   C  3  177 ? 24.133  -71.063  -11.304 1.00 145.17 ? 175 LYS   C CD  1 
ATOM   5185  C  CE  . LYS   C  3  177 ? 23.500  -69.785  -10.792 1.00 149.07 ? 175 LYS   C CE  1 
ATOM   5186  N  NZ  . LYS   C  3  177 ? 24.167  -69.294  -9.563  1.00 151.38 ? 175 LYS   C NZ  1 
ATOM   5187  N  N   . ASN   C  3  178 ? 23.661  -75.705  -11.510 1.00 123.53 ? 176 ASN   C N   1 
ATOM   5188  C  CA  . ASN   C  3  178 ? 24.443  -76.353  -12.602 1.00 123.86 ? 176 ASN   C CA  1 
ATOM   5189  C  C   . ASN   C  3  178 ? 24.118  -77.850  -12.741 1.00 119.00 ? 176 ASN   C C   1 
ATOM   5190  O  O   . ASN   C  3  178 ? 24.620  -78.452  -13.709 1.00 117.91 ? 176 ASN   C O   1 
ATOM   5191  C  CB  . ASN   C  3  178 ? 25.951  -76.151  -12.420 1.00 123.37 ? 176 ASN   C CB  1 
ATOM   5192  C  CG  . ASN   C  3  178 ? 26.437  -74.835  -12.988 1.00 126.65 ? 176 ASN   C CG  1 
ATOM   5193  O  OD1 . ASN   C  3  178 ? 26.817  -74.763  -14.154 1.00 125.57 ? 176 ASN   C OD1 1 
ATOM   5194  N  ND2 . ASN   C  3  178 ? 26.417  -73.787  -12.180 1.00 128.26 ? 176 ASN   C ND2 1 
ATOM   5195  N  N   . TYR   C  3  179 ? 23.325  -78.443  -11.838 1.00 117.87 ? 177 TYR   C N   1 
ATOM   5196  C  CA  . TYR   C  3  179 ? 22.927  -79.877  -11.902 1.00 117.85 ? 177 TYR   C CA  1 
ATOM   5197  C  C   . TYR   C  3  179 ? 21.454  -79.988  -12.309 1.00 116.74 ? 177 TYR   C C   1 
ATOM   5198  O  O   . TYR   C  3  179 ? 20.580  -79.550  -11.536 1.00 116.06 ? 177 TYR   C O   1 
ATOM   5199  C  CB  . TYR   C  3  179 ? 23.161  -80.596  -10.571 1.00 115.44 ? 177 TYR   C CB  1 
ATOM   5200  C  CG  . TYR   C  3  179 ? 23.022  -82.098  -10.648 1.00 114.19 ? 177 TYR   C CG  1 
ATOM   5201  C  CD1 . TYR   C  3  179 ? 21.781  -82.713  -10.568 1.00 113.49 ? 177 TYR   C CD1 1 
ATOM   5202  C  CD2 . TYR   C  3  179 ? 24.134  -82.911  -10.811 1.00 111.97 ? 177 TYR   C CD2 1 
ATOM   5203  C  CE1 . TYR   C  3  179 ? 21.648  -84.091  -10.645 1.00 110.32 ? 177 TYR   C CE1 1 
ATOM   5204  C  CE2 . TYR   C  3  179 ? 24.019  -84.290  -10.887 1.00 109.64 ? 177 TYR   C CE2 1 
ATOM   5205  C  CZ  . TYR   C  3  179 ? 22.772  -84.883  -10.804 1.00 106.88 ? 177 TYR   C CZ  1 
ATOM   5206  O  OH  . TYR   C  3  179 ? 22.660  -86.239  -10.877 1.00 104.50 ? 177 TYR   C OH  1 
ATOM   5207  N  N   . ASP   C  3  180 ? 21.198  -80.578  -13.479 1.00 118.42 ? 178 ASP   C N   1 
ATOM   5208  C  CA  . ASP   C  3  180 ? 19.833  -80.862  -13.992 1.00 125.46 ? 178 ASP   C CA  1 
ATOM   5209  C  C   . ASP   C  3  180 ? 19.442  -82.281  -13.570 1.00 127.17 ? 178 ASP   C C   1 
ATOM   5210  O  O   . ASP   C  3  180 ? 20.143  -83.228  -13.974 1.00 132.32 ? 178 ASP   C O   1 
ATOM   5211  C  CB  . ASP   C  3  180 ? 19.762  -80.695  -15.511 1.00 126.52 ? 178 ASP   C CB  1 
ATOM   5212  C  CG  . ASP   C  3  180 ? 18.355  -80.789  -16.078 1.00 130.79 ? 178 ASP   C CG  1 
ATOM   5213  O  OD1 . ASP   C  3  180 ? 17.394  -80.553  -15.315 1.00 132.29 ? 178 ASP   C OD1 1 
ATOM   5214  O  OD2 . ASP   C  3  180 ? 18.230  -81.097  -17.280 1.00 135.17 ? 178 ASP   C OD2 1 
ATOM   5215  N  N   . ARG   C  3  181 ? 18.372  -82.409  -12.778 1.00 132.91 ? 179 ARG   C N   1 
ATOM   5216  C  CA  . ARG   C  3  181 ? 17.806  -83.709  -12.324 1.00 134.29 ? 179 ARG   C CA  1 
ATOM   5217  C  C   . ARG   C  3  181 ? 17.281  -84.494  -13.532 1.00 136.42 ? 179 ARG   C C   1 
ATOM   5218  O  O   . ARG   C  3  181 ? 17.426  -85.732  -13.535 1.00 132.25 ? 179 ARG   C O   1 
ATOM   5219  C  CB  . ARG   C  3  181 ? 16.693  -83.475  -11.298 1.00 136.22 ? 179 ARG   C CB  1 
ATOM   5220  C  CG  . ARG   C  3  181 ? 17.195  -83.195  -9.888  1.00 133.60 ? 179 ARG   C CG  1 
ATOM   5221  C  CD  . ARG   C  3  181 ? 17.062  -84.398  -8.973  1.00 130.90 ? 179 ARG   C CD  1 
ATOM   5222  N  NE  . ARG   C  3  181 ? 16.794  -83.988  -7.602  1.00 128.21 ? 179 ARG   C NE  1 
ATOM   5223  C  CZ  . ARG   C  3  181 ? 16.103  -84.691  -6.709  1.00 129.80 ? 179 ARG   C CZ  1 
ATOM   5224  N  NH1 . ARG   C  3  181 ? 15.586  -85.869  -7.024  1.00 131.59 ? 179 ARG   C NH1 1 
ATOM   5225  N  NH2 . ARG   C  3  181 ? 15.924  -84.206  -5.492  1.00 131.68 ? 179 ARG   C NH2 1 
ATOM   5226  N  N   . LYS   C  3  182 ? 16.697  -83.798  -14.513 1.00 138.37 ? 180 LYS   C N   1 
ATOM   5227  C  CA  . LYS   C  3  182 ? 16.132  -84.401  -15.753 1.00 141.69 ? 180 LYS   C CA  1 
ATOM   5228  C  C   . LYS   C  3  182 ? 17.254  -84.988  -16.625 1.00 140.40 ? 180 LYS   C C   1 
ATOM   5229  O  O   . LYS   C  3  182 ? 16.962  -85.944  -17.372 1.00 136.48 ? 180 LYS   C O   1 
ATOM   5230  C  CB  . LYS   C  3  182 ? 15.302  -83.378  -16.539 1.00 146.84 ? 180 LYS   C CB  1 
ATOM   5231  C  CG  . LYS   C  3  182 ? 13.793  -83.591  -16.485 1.00 150.73 ? 180 LYS   C CG  1 
ATOM   5232  C  CD  . LYS   C  3  182 ? 13.153  -83.246  -15.152 1.00 150.29 ? 180 LYS   C CD  1 
ATOM   5233  C  CE  . LYS   C  3  182 ? 12.568  -81.849  -15.103 1.00 153.35 ? 180 LYS   C CE  1 
ATOM   5234  N  NZ  . LYS   C  3  182 ? 13.617  -80.809  -14.979 1.00 153.49 ? 180 LYS   C NZ  1 
ATOM   5235  N  N   . GLU   C  3  183 ? 18.478  -84.450  -16.543 1.00 140.04 ? 181 GLU   C N   1 
ATOM   5236  C  CA  . GLU   C  3  183 ? 19.636  -84.909  -17.362 1.00 140.46 ? 181 GLU   C CA  1 
ATOM   5237  C  C   . GLU   C  3  183 ? 20.931  -84.829  -16.556 1.00 134.04 ? 181 GLU   C C   1 
ATOM   5238  O  O   . GLU   C  3  183 ? 21.671  -83.852  -16.655 1.00 126.38 ? 181 GLU   C O   1 
ATOM   5239  C  CB  . GLU   C  3  183 ? 19.740  -84.084  -18.645 1.00 146.79 ? 181 GLU   C CB  1 
ATOM   5240  C  CG  . GLU   C  3  183 ? 20.788  -84.611  -19.609 1.00 151.97 ? 181 GLU   C CG  1 
ATOM   5241  C  CD  . GLU   C  3  183 ? 20.598  -84.168  -21.049 1.00 156.04 ? 181 GLU   C CD  1 
ATOM   5242  O  OE1 . GLU   C  3  183 ? 21.498  -83.489  -21.581 1.00 160.92 ? 181 GLU   C OE1 1 
ATOM   5243  O  OE2 . GLU   C  3  183 ? 19.553  -84.510  -21.637 1.00 168.09 ? 181 GLU   C OE2 1 
ATOM   5244  N  N   . PRO   C  3  184 ? 21.249  -85.858  -15.736 1.00 132.66 ? 182 PRO   C N   1 
ATOM   5245  C  CA  . PRO   C  3  184 ? 22.555  -85.948  -15.081 1.00 131.37 ? 182 PRO   C CA  1 
ATOM   5246  C  C   . PRO   C  3  184 ? 23.707  -86.115  -16.072 1.00 130.09 ? 182 PRO   C C   1 
ATOM   5247  O  O   . PRO   C  3  184 ? 23.508  -86.630  -17.171 1.00 132.51 ? 182 PRO   C O   1 
ATOM   5248  C  CB  . PRO   C  3  184 ? 22.430  -87.187  -14.176 1.00 131.67 ? 182 PRO   C CB  1 
ATOM   5249  C  CG  . PRO   C  3  184 ? 21.304  -87.995  -14.788 1.00 134.15 ? 182 PRO   C CG  1 
ATOM   5250  C  CD  . PRO   C  3  184 ? 20.354  -86.964  -15.359 1.00 134.16 ? 182 PRO   C CD  1 
ATOM   5251  N  N   . PRO   C  3  185 ? 24.937  -85.671  -15.715 1.00 125.21 ? 183 PRO   C N   1 
ATOM   5252  C  CA  . PRO   C  3  185 ? 26.123  -85.869  -16.551 1.00 126.79 ? 183 PRO   C CA  1 
ATOM   5253  C  C   . PRO   C  3  185 ? 26.144  -87.252  -17.222 1.00 127.81 ? 183 PRO   C C   1 
ATOM   5254  O  O   . PRO   C  3  185 ? 26.356  -88.236  -16.534 1.00 128.79 ? 183 PRO   C O   1 
ATOM   5255  C  CB  . PRO   C  3  185 ? 27.282  -85.713  -15.552 1.00 122.62 ? 183 PRO   C CB  1 
ATOM   5256  C  CG  . PRO   C  3  185 ? 26.753  -84.769  -14.488 1.00 122.39 ? 183 PRO   C CG  1 
ATOM   5257  C  CD  . PRO   C  3  185 ? 25.245  -84.927  -14.485 1.00 123.98 ? 183 PRO   C CD  1 
ATOM   5258  N  N   . ALA   C  3  186 ? 25.917  -87.291  -18.539 1.00 131.27 ? 184 ALA   C N   1 
ATOM   5259  C  CA  . ALA   C  3  186 ? 25.650  -88.523  -19.322 1.00 133.46 ? 184 ALA   C CA  1 
ATOM   5260  C  C   . ALA   C  3  186 ? 26.888  -89.432  -19.389 1.00 136.24 ? 184 ALA   C C   1 
ATOM   5261  O  O   . ALA   C  3  186 ? 26.694  -90.643  -19.610 1.00 142.00 ? 184 ALA   C O   1 
ATOM   5262  C  CB  . ALA   C  3  186 ? 25.155  -88.167  -20.703 1.00 134.08 ? 184 ALA   C CB  1 
ATOM   5263  N  N   . THR   C  3  187 ? 28.102  -88.894  -19.215 1.00 137.92 ? 185 THR   C N   1 
ATOM   5264  C  CA  . THR   C  3  187 ? 29.371  -89.674  -19.288 1.00 140.22 ? 185 THR   C CA  1 
ATOM   5265  C  C   . THR   C  3  187 ? 30.249  -89.423  -18.058 1.00 139.91 ? 185 THR   C C   1 
ATOM   5266  O  O   . THR   C  3  187 ? 29.905  -88.548  -17.236 1.00 139.35 ? 185 THR   C O   1 
ATOM   5267  C  CB  . THR   C  3  187 ? 30.152  -89.364  -20.572 1.00 143.00 ? 185 THR   C CB  1 
ATOM   5268  O  OG1 . THR   C  3  187 ? 30.361  -87.953  -20.650 1.00 143.83 ? 185 THR   C OG1 1 
ATOM   5269  C  CG2 . THR   C  3  187 ? 29.441  -89.851  -21.814 1.00 142.33 ? 185 THR   C CG2 1 
ATOM   5270  N  N   . VAL   C  3  188 ? 31.343  -90.185  -17.958 1.00 140.23 ? 186 VAL   C N   1 
ATOM   5271  C  CA  . VAL   C  3  188 ? 32.395  -90.059  -16.905 1.00 140.54 ? 186 VAL   C CA  1 
ATOM   5272  C  C   . VAL   C  3  188 ? 33.027  -88.667  -17.027 1.00 138.06 ? 186 VAL   C C   1 
ATOM   5273  O  O   . VAL   C  3  188 ? 33.130  -87.982  -15.993 1.00 141.21 ? 186 VAL   C O   1 
ATOM   5274  C  CB  . VAL   C  3  188 ? 33.462  -91.167  -17.020 1.00 142.43 ? 186 VAL   C CB  1 
ATOM   5275  C  CG1 . VAL   C  3  188 ? 34.460  -91.105  -15.873 1.00 142.02 ? 186 VAL   C CG1 1 
ATOM   5276  C  CG2 . VAL   C  3  188 ? 32.852  -92.560  -17.109 1.00 143.68 ? 186 VAL   C CG2 1 
ATOM   5277  N  N   . GLU   C  3  189 ? 33.422  -88.270  -18.243 1.00 136.94 ? 187 GLU   C N   1 
ATOM   5278  C  CA  . GLU   C  3  189 ? 34.101  -86.975  -18.527 1.00 136.18 ? 187 GLU   C CA  1 
ATOM   5279  C  C   . GLU   C  3  189 ? 33.237  -85.814  -18.022 1.00 133.98 ? 187 GLU   C C   1 
ATOM   5280  O  O   . GLU   C  3  189 ? 33.783  -84.955  -17.305 1.00 137.03 ? 187 GLU   C O   1 
ATOM   5281  C  CB  . GLU   C  3  189 ? 34.400  -86.804  -20.020 1.00 139.45 ? 187 GLU   C CB  1 
ATOM   5282  C  CG  . GLU   C  3  189 ? 35.786  -87.281  -20.426 1.00 144.13 ? 187 GLU   C CG  1 
ATOM   5283  C  CD  . GLU   C  3  189 ? 36.438  -86.486  -21.546 1.00 147.72 ? 187 GLU   C CD  1 
ATOM   5284  O  OE1 . GLU   C  3  189 ? 37.679  -86.359  -21.533 1.00 151.14 ? 187 GLU   C OE1 1 
ATOM   5285  O  OE2 . GLU   C  3  189 ? 35.707  -85.996  -22.431 1.00 151.80 ? 187 GLU   C OE2 1 
ATOM   5286  N  N   . GLU   C  3  190 ? 31.948  -85.794  -18.380 1.00 131.46 ? 188 GLU   C N   1 
ATOM   5287  C  CA  . GLU   C  3  190 ? 30.983  -84.734  -17.972 1.00 134.60 ? 188 GLU   C CA  1 
ATOM   5288  C  C   . GLU   C  3  190 ? 30.917  -84.646  -16.442 1.00 132.50 ? 188 GLU   C C   1 
ATOM   5289  O  O   . GLU   C  3  190 ? 30.977  -83.516  -15.913 1.00 131.71 ? 188 GLU   C O   1 
ATOM   5290  C  CB  . GLU   C  3  190 ? 29.588  -85.006  -18.537 1.00 134.57 ? 188 GLU   C CB  1 
ATOM   5291  C  CG  . GLU   C  3  190 ? 29.374  -84.448  -19.930 1.00 137.83 ? 188 GLU   C CG  1 
ATOM   5292  C  CD  . GLU   C  3  190 ? 28.030  -84.817  -20.532 1.00 135.87 ? 188 GLU   C CD  1 
ATOM   5293  O  OE1 . GLU   C  3  190 ? 27.236  -83.901  -20.812 1.00 139.18 ? 188 GLU   C OE1 1 
ATOM   5294  O  OE2 . GLU   C  3  190 ? 27.781  -86.023  -20.714 1.00 138.15 ? 188 GLU   C OE2 1 
ATOM   5295  N  N   . CYS   C  3  191 ? 30.797  -85.793  -15.766 1.00 131.61 ? 189 CYS   C N   1 
ATOM   5296  C  CA  . CYS   C  3  191 ? 30.599  -85.897  -14.295 1.00 130.86 ? 189 CYS   C CA  1 
ATOM   5297  C  C   . CYS   C  3  191 ? 31.848  -85.400  -13.556 1.00 124.84 ? 189 CYS   C C   1 
ATOM   5298  O  O   . CYS   C  3  191 ? 31.683  -84.666  -12.563 1.00 121.05 ? 189 CYS   C O   1 
ATOM   5299  C  CB  . CYS   C  3  191 ? 30.266  -87.327  -13.879 1.00 135.63 ? 189 CYS   C CB  1 
ATOM   5300  S  SG  . CYS   C  3  191 ? 29.546  -87.449  -12.220 1.00 143.56 ? 189 CYS   C SG  1 
ATOM   5301  N  N   . VAL   C  3  192 ? 33.044  -85.779  -14.022 1.00 123.92 ? 190 VAL   C N   1 
ATOM   5302  C  CA  . VAL   C  3  192 ? 34.346  -85.349  -13.425 1.00 125.74 ? 190 VAL   C CA  1 
ATOM   5303  C  C   . VAL   C  3  192 ? 34.463  -83.827  -13.572 1.00 126.48 ? 190 VAL   C C   1 
ATOM   5304  O  O   . VAL   C  3  192 ? 34.844  -83.168  -12.585 1.00 127.23 ? 190 VAL   C O   1 
ATOM   5305  C  CB  . VAL   C  3  192 ? 35.551  -86.079  -14.057 1.00 130.03 ? 190 VAL   C CB  1 
ATOM   5306  C  CG1 . VAL   C  3  192 ? 36.880  -85.477  -13.620 1.00 129.91 ? 190 VAL   C CG1 1 
ATOM   5307  C  CG2 . VAL   C  3  192 ? 35.530  -87.571  -13.753 1.00 129.57 ? 190 VAL   C CG2 1 
ATOM   5308  N  N   . LYS   C  3  193 ? 34.130  -83.294  -14.753 1.00 125.40 ? 191 LYS   C N   1 
ATOM   5309  C  CA  . LYS   C  3  193 ? 34.269  -81.851  -15.085 1.00 123.07 ? 191 LYS   C CA  1 
ATOM   5310  C  C   . LYS   C  3  193 ? 33.380  -81.025  -14.150 1.00 116.84 ? 191 LYS   C C   1 
ATOM   5311  O  O   . LYS   C  3  193 ? 33.907  -80.079  -13.535 1.00 114.64 ? 191 LYS   C O   1 
ATOM   5312  C  CB  . LYS   C  3  193 ? 33.911  -81.582  -16.549 1.00 123.97 ? 191 LYS   C CB  1 
ATOM   5313  C  CG  . LYS   C  3  193 ? 34.322  -80.207  -17.054 1.00 126.44 ? 191 LYS   C CG  1 
ATOM   5314  C  CD  . LYS   C  3  193 ? 33.802  -79.880  -18.433 1.00 130.77 ? 191 LYS   C CD  1 
ATOM   5315  C  CE  . LYS   C  3  193 ? 34.050  -78.437  -18.815 1.00 132.31 ? 191 LYS   C CE  1 
ATOM   5316  N  NZ  . LYS   C  3  193 ? 33.433  -78.101  -20.120 1.00 135.51 ? 191 LYS   C NZ  1 
ATOM   5317  N  N   . LEU   C  3  194 ? 32.093  -81.375  -14.046 1.00 114.19 ? 192 LEU   C N   1 
ATOM   5318  C  CA  . LEU   C  3  194 ? 31.108  -80.668  -13.180 1.00 114.58 ? 192 LEU   C CA  1 
ATOM   5319  C  C   . LEU   C  3  194 ? 31.590  -80.705  -11.725 1.00 116.21 ? 192 LEU   C C   1 
ATOM   5320  O  O   . LEU   C  3  194 ? 31.363  -79.711  -11.007 1.00 121.86 ? 192 LEU   C O   1 
ATOM   5321  C  CB  . LEU   C  3  194 ? 29.723  -81.310  -13.319 1.00 112.28 ? 192 LEU   C CB  1 
ATOM   5322  C  CG  . LEU   C  3  194 ? 28.615  -80.669  -12.481 1.00 112.17 ? 192 LEU   C CG  1 
ATOM   5323  C  CD1 . LEU   C  3  194 ? 28.440  -79.196  -12.827 1.00 113.88 ? 192 LEU   C CD1 1 
ATOM   5324  C  CD2 . LEU   C  3  194 ? 27.300  -81.410  -12.658 1.00 111.22 ? 192 LEU   C CD2 1 
ATOM   5325  N  N   . THR   C  3  195 ? 32.228  -81.804  -11.309 1.00 114.42 ? 193 THR   C N   1 
ATOM   5326  C  CA  . THR   C  3  195 ? 32.817  -81.967  -9.952  1.00 112.95 ? 193 THR   C CA  1 
ATOM   5327  C  C   . THR   C  3  195 ? 34.017  -81.023  -9.806  1.00 117.52 ? 193 THR   C C   1 
ATOM   5328  O  O   . THR   C  3  195 ? 34.066  -80.295  -8.796  1.00 118.96 ? 193 THR   C O   1 
ATOM   5329  C  CB  . THR   C  3  195 ? 33.208  -83.423  -9.666  1.00 111.59 ? 193 THR   C CB  1 
ATOM   5330  O  OG1 . THR   C  3  195 ? 32.070  -84.255  -9.893  1.00 109.41 ? 193 THR   C OG1 1 
ATOM   5331  C  CG2 . THR   C  3  195 ? 33.701  -83.627  -8.250  1.00 108.31 ? 193 THR   C CG2 1 
ATOM   5332  N  N   . VAL   C  3  196 ? 34.942  -81.033  -10.772 1.00 119.97 ? 194 VAL   C N   1 
ATOM   5333  C  CA  . VAL   C  3  196 ? 36.176  -80.189  -10.746 1.00 123.39 ? 194 VAL   C CA  1 
ATOM   5334  C  C   . VAL   C  3  196 ? 35.767  -78.709  -10.777 1.00 124.66 ? 194 VAL   C C   1 
ATOM   5335  O  O   . VAL   C  3  196 ? 36.362  -77.924  -10.013 1.00 123.57 ? 194 VAL   C O   1 
ATOM   5336  C  CB  . VAL   C  3  196 ? 37.148  -80.544  -11.891 1.00 127.54 ? 194 VAL   C CB  1 
ATOM   5337  C  CG1 . VAL   C  3  196 ? 38.262  -79.515  -12.033 1.00 129.63 ? 194 VAL   C CG1 1 
ATOM   5338  C  CG2 . VAL   C  3  196 ? 37.739  -81.934  -11.711 1.00 126.76 ? 194 VAL   C CG2 1 
ATOM   5339  N  N   . ARG   C  3  197 ? 34.789  -78.347  -11.615 1.00 124.13 ? 195 ARG   C N   1 
ATOM   5340  C  CA  . ARG   C  3  197 ? 34.257  -76.959  -11.720 1.00 126.07 ? 195 ARG   C CA  1 
ATOM   5341  C  C   . ARG   C  3  197 ? 33.783  -76.489  -10.339 1.00 126.04 ? 195 ARG   C C   1 
ATOM   5342  O  O   . ARG   C  3  197 ? 34.159  -75.370  -9.936  1.00 127.62 ? 195 ARG   C O   1 
ATOM   5343  C  CB  . ARG   C  3  197 ? 33.102  -76.864  -12.724 1.00 128.82 ? 195 ARG   C CB  1 
ATOM   5344  C  CG  . ARG   C  3  197 ? 33.530  -76.641  -14.168 1.00 128.93 ? 195 ARG   C CG  1 
ATOM   5345  C  CD  . ARG   C  3  197 ? 32.347  -76.665  -15.119 1.00 128.85 ? 195 ARG   C CD  1 
ATOM   5346  N  NE  . ARG   C  3  197 ? 31.415  -75.567  -14.884 1.00 129.14 ? 195 ARG   C NE  1 
ATOM   5347  C  CZ  . ARG   C  3  197 ? 30.151  -75.527  -15.305 1.00 129.37 ? 195 ARG   C CZ  1 
ATOM   5348  N  NH1 . ARG   C  3  197 ? 29.632  -76.533  -15.992 1.00 129.76 ? 195 ARG   C NH1 1 
ATOM   5349  N  NH2 . ARG   C  3  197 ? 29.401  -74.474  -15.028 1.00 129.99 ? 195 ARG   C NH2 1 
ATOM   5350  N  N   . SER   C  3  198 ? 32.990  -77.316  -9.650  1.00 122.79 ? 196 SER   C N   1 
ATOM   5351  C  CA  . SER   C  3  198 ? 32.340  -76.988  -8.353  1.00 120.61 ? 196 SER   C CA  1 
ATOM   5352  C  C   . SER   C  3  198 ? 33.399  -76.748  -7.268  1.00 120.91 ? 196 SER   C C   1 
ATOM   5353  O  O   . SER   C  3  198 ? 33.158  -75.888  -6.400  1.00 122.33 ? 196 SER   C O   1 
ATOM   5354  C  CB  . SER   C  3  198 ? 31.360  -78.059  -7.945  1.00 118.48 ? 196 SER   C CB  1 
ATOM   5355  O  OG  . SER   C  3  198 ? 32.030  -79.261  -7.599  1.00 118.13 ? 196 SER   C OG  1 
ATOM   5356  N  N   . LEU   C  3  199 ? 34.522  -77.473  -7.314  1.00 120.86 ? 197 LEU   C N   1 
ATOM   5357  C  CA  . LEU   C  3  199 ? 35.644  -77.319  -6.346  1.00 124.23 ? 197 LEU   C CA  1 
ATOM   5358  C  C   . LEU   C  3  199 ? 36.440  -76.046  -6.664  1.00 127.05 ? 197 LEU   C C   1 
ATOM   5359  O  O   . LEU   C  3  199 ? 36.918  -75.405  -5.703  1.00 129.83 ? 197 LEU   C O   1 
ATOM   5360  C  CB  . LEU   C  3  199 ? 36.549  -78.557  -6.383  1.00 124.48 ? 197 LEU   C CB  1 
ATOM   5361  C  CG  . LEU   C  3  199 ? 36.115  -79.726  -5.497  1.00 123.09 ? 197 LEU   C CG  1 
ATOM   5362  C  CD1 . LEU   C  3  199 ? 36.932  -80.970  -5.811  1.00 123.16 ? 197 LEU   C CD1 1 
ATOM   5363  C  CD2 . LEU   C  3  199 ? 36.235  -79.378  -4.019  1.00 123.72 ? 197 LEU   C CD2 1 
ATOM   5364  N  N   . LEU   C  3  200 ? 36.570  -75.690  -7.949  1.00 127.27 ? 198 LEU   C N   1 
ATOM   5365  C  CA  . LEU   C  3  200 ? 37.355  -74.511  -8.416  1.00 124.74 ? 198 LEU   C CA  1 
ATOM   5366  C  C   . LEU   C  3  200 ? 36.682  -73.204  -7.974  1.00 123.51 ? 198 LEU   C C   1 
ATOM   5367  O  O   . LEU   C  3  200 ? 37.377  -72.170  -7.977  1.00 121.96 ? 198 LEU   C O   1 
ATOM   5368  C  CB  . LEU   C  3  200 ? 37.522  -74.558  -9.939  1.00 126.09 ? 198 LEU   C CB  1 
ATOM   5369  C  CG  . LEU   C  3  200 ? 38.553  -75.560  -10.457 1.00 125.76 ? 198 LEU   C CG  1 
ATOM   5370  C  CD1 . LEU   C  3  200 ? 38.425  -75.735  -11.962 1.00 127.92 ? 198 LEU   C CD1 1 
ATOM   5371  C  CD2 . LEU   C  3  200 ? 39.969  -75.137  -10.090 1.00 126.48 ? 198 LEU   C CD2 1 
ATOM   5372  N  N   . GLU   C  3  201 ? 35.396  -73.244  -7.606  1.00 120.67 ? 199 GLU   C N   1 
ATOM   5373  C  CA  . GLU   C  3  201 ? 34.663  -72.092  -7.012  1.00 122.56 ? 199 GLU   C CA  1 
ATOM   5374  C  C   . GLU   C  3  201 ? 35.271  -71.741  -5.646  1.00 122.85 ? 199 GLU   C C   1 
ATOM   5375  O  O   . GLU   C  3  201 ? 35.157  -70.570  -5.241  1.00 123.61 ? 199 GLU   C O   1 
ATOM   5376  C  CB  . GLU   C  3  201 ? 33.171  -72.401  -6.850  1.00 125.55 ? 199 GLU   C CB  1 
ATOM   5377  C  CG  . GLU   C  3  201 ? 32.434  -72.618  -8.162  1.00 128.98 ? 199 GLU   C CG  1 
ATOM   5378  C  CD  . GLU   C  3  201 ? 32.290  -71.387  -9.045  1.00 130.83 ? 199 GLU   C CD  1 
ATOM   5379  O  OE1 . GLU   C  3  201 ? 31.724  -70.381  -8.573  1.00 135.84 ? 199 GLU   C OE1 1 
ATOM   5380  O  OE2 . GLU   C  3  201 ? 32.743  -71.438  -10.206 1.00 137.65 ? 199 GLU   C OE2 1 
ATOM   5381  N  N   . VAL   C  3  202 ? 35.890  -72.716  -4.969  1.00 119.91 ? 200 VAL   C N   1 
ATOM   5382  C  CA  . VAL   C  3  202 ? 36.305  -72.617  -3.537  1.00 119.78 ? 200 VAL   C CA  1 
ATOM   5383  C  C   . VAL   C  3  202 ? 37.818  -72.832  -3.371  1.00 119.59 ? 200 VAL   C C   1 
ATOM   5384  O  O   . VAL   C  3  202 ? 38.375  -72.229  -2.437  1.00 116.37 ? 200 VAL   C O   1 
ATOM   5385  C  CB  . VAL   C  3  202 ? 35.495  -73.615  -2.685  1.00 119.13 ? 200 VAL   C CB  1 
ATOM   5386  C  CG1 . VAL   C  3  202 ? 36.099  -73.831  -1.305  1.00 117.54 ? 200 VAL   C CG1 1 
ATOM   5387  C  CG2 . VAL   C  3  202 ? 34.040  -73.185  -2.567  1.00 120.77 ? 200 VAL   C CG2 1 
ATOM   5388  N  N   . VAL   C  3  203 ? 38.465  -73.650  -4.210  1.00 124.70 ? 201 VAL   C N   1 
ATOM   5389  C  CA  . VAL   C  3  203 ? 39.783  -74.277  -3.875  1.00 131.29 ? 201 VAL   C CA  1 
ATOM   5390  C  C   . VAL   C  3  203 ? 40.903  -73.218  -3.828  1.00 137.88 ? 201 VAL   C C   1 
ATOM   5391  O  O   . VAL   C  3  203 ? 41.341  -72.920  -2.701  1.00 141.80 ? 201 VAL   C O   1 
ATOM   5392  C  CB  . VAL   C  3  203 ? 40.112  -75.483  -4.783  1.00 133.12 ? 201 VAL   C CB  1 
ATOM   5393  C  CG1 . VAL   C  3  203 ? 40.392  -75.107  -6.230  1.00 136.22 ? 201 VAL   C CG1 1 
ATOM   5394  C  CG2 . VAL   C  3  203 ? 41.262  -76.302  -4.217  1.00 132.48 ? 201 VAL   C CG2 1 
ATOM   5395  N  N   . GLN   C  3  204 ? 41.329  -72.653  -4.969  1.00 140.99 ? 202 GLN   C N   1 
ATOM   5396  C  CA  . GLN   C  3  204 ? 42.564  -71.822  -5.132  1.00 152.80 ? 202 GLN   C CA  1 
ATOM   5397  C  C   . GLN   C  3  204 ? 43.216  -72.189  -6.475  1.00 150.97 ? 202 GLN   C C   1 
ATOM   5398  O  O   . GLN   C  3  204 ? 42.711  -71.716  -7.513  1.00 151.57 ? 202 GLN   C O   1 
ATOM   5399  C  CB  . GLN   C  3  204 ? 43.514  -71.983  -3.934  1.00 155.77 ? 202 GLN   C CB  1 
ATOM   5400  C  CG  . GLN   C  3  204 ? 44.868  -71.291  -4.071  1.00 167.26 ? 202 GLN   C CG  1 
ATOM   5401  C  CD  . GLN   C  3  204 ? 44.772  -69.802  -4.301  1.00 176.85 ? 202 GLN   C CD  1 
ATOM   5402  O  OE1 . GLN   C  3  204 ? 43.830  -69.145  -3.862  1.00 184.62 ? 202 GLN   C OE1 1 
ATOM   5403  N  NE2 . GLN   C  3  204 ? 45.764  -69.254  -4.985  1.00 185.63 ? 202 GLN   C NE2 1 
ATOM   5404  N  N   . THR   C  3  205 ? 44.278  -73.006  -6.460  1.00 154.50 ? 203 THR   C N   1 
ATOM   5405  C  CA  . THR   C  3  205 ? 44.981  -73.529  -7.663  1.00 158.11 ? 203 THR   C CA  1 
ATOM   5406  C  C   . THR   C  3  205 ? 44.472  -74.952  -7.907  1.00 159.69 ? 203 THR   C C   1 
ATOM   5407  O  O   . THR   C  3  205 ? 44.283  -75.680  -6.913  1.00 165.27 ? 203 THR   C O   1 
ATOM   5408  C  CB  . THR   C  3  205 ? 46.508  -73.524  -7.488  1.00 156.29 ? 203 THR   C CB  1 
ATOM   5409  O  OG1 . THR   C  3  205 ? 46.843  -72.812  -6.298  1.00 150.22 ? 203 THR   C OG1 1 
ATOM   5410  C  CG2 . THR   C  3  205 ? 47.243  -72.909  -8.661  1.00 154.14 ? 203 THR   C CG2 1 
ATOM   5411  N  N   . GLY   C  3  206 ? 44.265  -75.336  -9.168  1.00 162.22 ? 204 GLY   C N   1 
ATOM   5412  C  CA  . GLY   C  3  206 ? 43.853  -76.703  -9.543  1.00 161.24 ? 204 GLY   C CA  1 
ATOM   5413  C  C   . GLY   C  3  206 ? 45.040  -77.652  -9.620  1.00 160.43 ? 204 GLY   C C   1 
ATOM   5414  O  O   . GLY   C  3  206 ? 44.945  -78.652  -10.356 1.00 155.60 ? 204 GLY   C O   1 
ATOM   5415  N  N   . ALA   C  3  207 ? 46.115  -77.361  -8.877  1.00 162.27 ? 205 ALA   C N   1 
ATOM   5416  C  CA  . ALA   C  3  207 ? 47.368  -78.149  -8.839  1.00 161.47 ? 205 ALA   C CA  1 
ATOM   5417  C  C   . ALA   C  3  207 ? 47.149  -79.383  -7.951  1.00 161.97 ? 205 ALA   C C   1 
ATOM   5418  O  O   . ALA   C  3  207 ? 46.174  -80.118  -8.211  1.00 155.14 ? 205 ALA   C O   1 
ATOM   5419  C  CB  . ALA   C  3  207 ? 48.505  -77.269  -8.367  1.00 159.28 ? 205 ALA   C CB  1 
ATOM   5420  N  N   . LYS   C  3  208 ? 47.995  -79.599  -6.935  1.00 165.64 ? 206 LYS   C N   1 
ATOM   5421  C  CA  . LYS   C  3  208 ? 47.889  -80.740  -5.984  1.00 168.81 ? 206 LYS   C CA  1 
ATOM   5422  C  C   . LYS   C  3  208 ? 46.941  -80.359  -4.838  1.00 163.28 ? 206 LYS   C C   1 
ATOM   5423  O  O   . LYS   C  3  208 ? 47.257  -80.685  -3.675  1.00 167.08 ? 206 LYS   C O   1 
ATOM   5424  C  CB  . LYS   C  3  208 ? 49.281  -81.137  -5.476  1.00 172.03 ? 206 LYS   C CB  1 
ATOM   5425  C  CG  . LYS   C  3  208 ? 50.181  -81.785  -6.519  1.00 176.34 ? 206 LYS   C CG  1 
ATOM   5426  C  CD  . LYS   C  3  208 ? 51.640  -81.859  -6.117  1.00 177.51 ? 206 LYS   C CD  1 
ATOM   5427  C  CE  . LYS   C  3  208 ? 52.524  -82.448  -7.198  1.00 177.96 ? 206 LYS   C CE  1 
ATOM   5428  N  NZ  . LYS   C  3  208 ? 52.656  -81.541  -8.364  1.00 182.32 ? 206 LYS   C NZ  1 
ATOM   5429  N  N   . ASN   C  3  209 ? 45.819  -79.703  -5.161  1.00 161.45 ? 207 ASN   C N   1 
ATOM   5430  C  CA  . ASN   C  3  209 ? 44.779  -79.266  -4.191  1.00 155.76 ? 207 ASN   C CA  1 
ATOM   5431  C  C   . ASN   C  3  209 ? 43.497  -80.089  -4.371  1.00 146.67 ? 207 ASN   C C   1 
ATOM   5432  O  O   . ASN   C  3  209 ? 42.708  -80.138  -3.409  1.00 138.43 ? 207 ASN   C O   1 
ATOM   5433  C  CB  . ASN   C  3  209 ? 44.465  -77.773  -4.325  1.00 161.72 ? 207 ASN   C CB  1 
ATOM   5434  C  CG  . ASN   C  3  209 ? 45.577  -76.876  -3.824  1.00 165.88 ? 207 ASN   C CG  1 
ATOM   5435  O  OD1 . ASN   C  3  209 ? 46.606  -77.356  -3.352  1.00 168.12 ? 207 ASN   C OD1 1 
ATOM   5436  N  ND2 . ASN   C  3  209 ? 45.379  -75.571  -3.917  1.00 168.69 ? 207 ASN   C ND2 1 
ATOM   5437  N  N   . ILE   C  3  210 ? 43.288  -80.696  -5.546  1.00 145.71 ? 208 ILE   C N   1 
ATOM   5438  C  CA  . ILE   C  3  210 ? 42.052  -81.467  -5.880  1.00 142.74 ? 208 ILE   C CA  1 
ATOM   5439  C  C   . ILE   C  3  210 ? 42.405  -82.950  -6.061  1.00 138.19 ? 208 ILE   C C   1 
ATOM   5440  O  O   . ILE   C  3  210 ? 43.346  -83.248  -6.822  1.00 142.02 ? 208 ILE   C O   1 
ATOM   5441  C  CB  . ILE   C  3  210 ? 41.350  -80.878  -7.122  1.00 143.78 ? 208 ILE   C CB  1 
ATOM   5442  C  CG1 . ILE   C  3  210 ? 40.820  -79.469  -6.838  1.00 148.88 ? 208 ILE   C CG1 1 
ATOM   5443  C  CG2 . ILE   C  3  210 ? 40.247  -81.806  -7.613  1.00 141.65 ? 208 ILE   C CG2 1 
ATOM   5444  C  CD1 . ILE   C  3  210 ? 40.249  -78.757  -8.045  1.00 153.63 ? 208 ILE   C CD1 1 
ATOM   5445  N  N   . GLU   C  3  211 ? 41.667  -83.827  -5.370  1.00 136.83 ? 209 GLU   C N   1 
ATOM   5446  C  CA  . GLU   C  3  211 ? 41.630  -85.300  -5.587  1.00 135.01 ? 209 GLU   C CA  1 
ATOM   5447  C  C   . GLU   C  3  211 ? 40.294  -85.665  -6.242  1.00 127.01 ? 209 GLU   C C   1 
ATOM   5448  O  O   . GLU   C  3  211 ? 39.260  -85.141  -5.783  1.00 121.64 ? 209 GLU   C O   1 
ATOM   5449  C  CB  . GLU   C  3  211 ? 41.755  -86.057  -4.264  1.00 138.73 ? 209 GLU   C CB  1 
ATOM   5450  C  CG  . GLU   C  3  211 ? 43.179  -86.189  -3.757  1.00 148.26 ? 209 GLU   C CG  1 
ATOM   5451  C  CD  . GLU   C  3  211 ? 43.311  -86.934  -2.438  1.00 153.71 ? 209 GLU   C CD  1 
ATOM   5452  O  OE1 . GLU   C  3  211 ? 42.285  -87.440  -1.935  1.00 159.48 ? 209 GLU   C OE1 1 
ATOM   5453  O  OE2 . GLU   C  3  211 ? 44.442  -87.010  -1.915  1.00 164.44 ? 209 GLU   C OE2 1 
ATOM   5454  N  N   . ILE   C  3  212 ? 40.316  -86.529  -7.261  1.00 123.72 ? 210 ILE   C N   1 
ATOM   5455  C  CA  . ILE   C  3  212 ? 39.097  -87.063  -7.940  1.00 127.68 ? 210 ILE   C CA  1 
ATOM   5456  C  C   . ILE   C  3  212 ? 39.175  -88.592  -7.954  1.00 126.27 ? 210 ILE   C C   1 
ATOM   5457  O  O   . ILE   C  3  212 ? 40.187  -89.127  -8.449  1.00 127.58 ? 210 ILE   C O   1 
ATOM   5458  C  CB  . ILE   C  3  212 ? 38.948  -86.500  -9.369  1.00 131.68 ? 210 ILE   C CB  1 
ATOM   5459  C  CG1 . ILE   C  3  212 ? 38.834  -84.972  -9.385  1.00 134.96 ? 210 ILE   C CG1 1 
ATOM   5460  C  CG2 . ILE   C  3  212 ? 37.779  -87.161  -10.088 1.00 130.54 ? 210 ILE   C CG2 1 
ATOM   5461  C  CD1 . ILE   C  3  212 ? 37.562  -84.425  -8.769  1.00 137.23 ? 210 ILE   C CD1 1 
ATOM   5462  N  N   . THR   C  3  213 ? 38.137  -89.255  -7.438  1.00 125.39 ? 211 THR   C N   1 
ATOM   5463  C  CA  . THR   C  3  213 ? 37.935  -90.725  -7.534  1.00 127.36 ? 211 THR   C CA  1 
ATOM   5464  C  C   . THR   C  3  213 ? 36.650  -90.991  -8.323  1.00 124.32 ? 211 THR   C C   1 
ATOM   5465  O  O   . THR   C  3  213 ? 35.625  -90.352  -8.011  1.00 121.63 ? 211 THR   C O   1 
ATOM   5466  C  CB  . THR   C  3  213 ? 37.884  -91.390  -6.153  1.00 124.47 ? 211 THR   C CB  1 
ATOM   5467  O  OG1 . THR   C  3  213 ? 39.005  -90.938  -5.392  1.00 128.31 ? 211 THR   C OG1 1 
ATOM   5468  C  CG2 . THR   C  3  213 ? 37.908  -92.901  -6.235  1.00 125.06 ? 211 THR   C CG2 1 
ATOM   5469  N  N   . VAL   C  3  214 ? 36.719  -91.897  -9.302  1.00 127.72 ? 212 VAL   C N   1 
ATOM   5470  C  CA  . VAL   C  3  214 ? 35.572  -92.310  -10.164 1.00 126.99 ? 212 VAL   C CA  1 
ATOM   5471  C  C   . VAL   C  3  214 ? 35.199  -93.753  -9.812  1.00 126.86 ? 212 VAL   C C   1 
ATOM   5472  O  O   . VAL   C  3  214 ? 36.058  -94.640  -9.982  1.00 129.96 ? 212 VAL   C O   1 
ATOM   5473  C  CB  . VAL   C  3  214 ? 35.909  -92.179  -11.662 1.00 126.11 ? 212 VAL   C CB  1 
ATOM   5474  C  CG1 . VAL   C  3  214 ? 34.716  -92.535  -12.536 1.00 124.52 ? 212 VAL   C CG1 1 
ATOM   5475  C  CG2 . VAL   C  3  214 ? 36.430  -90.794  -12.008 1.00 127.06 ? 212 VAL   C CG2 1 
ATOM   5476  N  N   . VAL   C  3  215 ? 33.964  -93.968  -9.349  1.00 125.84 ? 213 VAL   C N   1 
ATOM   5477  C  CA  . VAL   C  3  215 ? 33.380  -95.324  -9.123  1.00 122.94 ? 213 VAL   C CA  1 
ATOM   5478  C  C   . VAL   C  3  215 ? 32.383  -95.601  -10.257 1.00 124.79 ? 213 VAL   C C   1 
ATOM   5479  O  O   . VAL   C  3  215 ? 31.515  -94.742  -10.508 1.00 126.31 ? 213 VAL   C O   1 
ATOM   5480  C  CB  . VAL   C  3  215 ? 32.744  -95.473  -7.724  1.00 122.23 ? 213 VAL   C CB  1 
ATOM   5481  C  CG1 . VAL   C  3  215 ? 31.838  -94.310  -7.349  1.00 121.07 ? 213 VAL   C CG1 1 
ATOM   5482  C  CG2 . VAL   C  3  215 ? 31.996  -96.791  -7.585  1.00 124.14 ? 213 VAL   C CG2 1 
ATOM   5483  N  N   . LYS   C  3  216 ? 32.548  -96.744  -10.932 1.00 124.10 ? 214 LYS   C N   1 
ATOM   5484  C  CA  . LYS   C  3  216 ? 31.651  -97.263  -12.000 1.00 123.34 ? 214 LYS   C CA  1 
ATOM   5485  C  C   . LYS   C  3  216 ? 31.084  -98.606  -11.547 1.00 124.79 ? 214 LYS   C C   1 
ATOM   5486  O  O   . LYS   C  3  216 ? 31.591  -99.197  -10.595 1.00 120.67 ? 214 LYS   C O   1 
ATOM   5487  C  CB  . LYS   C  3  216 ? 32.423  -97.399  -13.316 1.00 127.52 ? 214 LYS   C CB  1 
ATOM   5488  C  CG  . LYS   C  3  216 ? 32.493  -96.136  -14.163 1.00 127.76 ? 214 LYS   C CG  1 
ATOM   5489  C  CD  . LYS   C  3  216 ? 33.422  -96.266  -15.350 1.00 132.04 ? 214 LYS   C CD  1 
ATOM   5490  C  CE  . LYS   C  3  216 ? 34.880  -96.116  -14.974 1.00 133.86 ? 214 LYS   C CE  1 
ATOM   5491  N  NZ  . LYS   C  3  216 ? 35.761  -96.217  -16.161 1.00 139.29 ? 214 LYS   C NZ  1 
ATOM   5492  N  N   . PRO   C  3  217 ? 30.019  -99.131  -12.201 1.00 124.18 ? 215 PRO   C N   1 
ATOM   5493  C  CA  . PRO   C  3  217 ? 29.417  -100.405 -11.802 1.00 126.03 ? 215 PRO   C CA  1 
ATOM   5494  C  C   . PRO   C  3  217 ? 30.384  -101.602 -11.804 1.00 131.25 ? 215 PRO   C C   1 
ATOM   5495  O  O   . PRO   C  3  217 ? 31.379  -101.557 -12.512 1.00 132.45 ? 215 PRO   C O   1 
ATOM   5496  C  CB  . PRO   C  3  217 ? 28.319  -100.641 -12.851 1.00 124.68 ? 215 PRO   C CB  1 
ATOM   5497  C  CG  . PRO   C  3  217 ? 27.996  -99.263  -13.378 1.00 123.75 ? 215 PRO   C CG  1 
ATOM   5498  C  CD  . PRO   C  3  217 ? 29.308  -98.509  -13.329 1.00 124.54 ? 215 PRO   C CD  1 
ATOM   5499  N  N   . ASP   C  3  218 ? 30.050  -102.631 -11.013 1.00 133.23 ? 216 ASP   C N   1 
ATOM   5500  C  CA  . ASP   C  3  218 ? 30.780  -103.924 -10.887 1.00 133.90 ? 216 ASP   C CA  1 
ATOM   5501  C  C   . ASP   C  3  218 ? 32.221  -103.667 -10.423 1.00 131.31 ? 216 ASP   C C   1 
ATOM   5502  O  O   . ASP   C  3  218 ? 33.157  -104.057 -11.152 1.00 134.83 ? 216 ASP   C O   1 
ATOM   5503  C  CB  . ASP   C  3  218 ? 30.725  -104.725 -12.194 1.00 138.76 ? 216 ASP   C CB  1 
ATOM   5504  C  CG  . ASP   C  3  218 ? 29.359  -105.310 -12.517 1.00 142.98 ? 216 ASP   C CG  1 
ATOM   5505  O  OD1 . ASP   C  3  218 ? 28.613  -105.630 -11.567 1.00 143.69 ? 216 ASP   C OD1 1 
ATOM   5506  O  OD2 . ASP   C  3  218 ? 29.054  -105.453 -13.719 1.00 144.89 ? 216 ASP   C OD2 1 
ATOM   5507  N  N   . SER   C  3  219 ? 32.378  -103.036 -9.254  1.00 127.44 ? 217 SER   C N   1 
ATOM   5508  C  CA  . SER   C  3  219 ? 33.663  -102.859 -8.524  1.00 123.94 ? 217 SER   C CA  1 
ATOM   5509  C  C   . SER   C  3  219 ? 34.728  -102.228 -9.432  1.00 124.45 ? 217 SER   C C   1 
ATOM   5510  O  O   . SER   C  3  219 ? 35.864  -102.742 -9.459  1.00 120.99 ? 217 SER   C O   1 
ATOM   5511  C  CB  . SER   C  3  219 ? 34.133  -104.177 -7.970  1.00 123.37 ? 217 SER   C CB  1 
ATOM   5512  O  OG  . SER   C  3  219 ? 33.135  -104.765 -7.150  1.00 123.20 ? 217 SER   C OG  1 
ATOM   5513  N  N   . ASP   C  3  220 ? 34.373  -101.151 -10.138 1.00 124.88 ? 218 ASP   C N   1 
ATOM   5514  C  CA  . ASP   C  3  220 ? 35.272  -100.432 -11.080 1.00 126.19 ? 218 ASP   C CA  1 
ATOM   5515  C  C   . ASP   C  3  220 ? 35.594  -99.051  -10.495 1.00 126.45 ? 218 ASP   C C   1 
ATOM   5516  O  O   . ASP   C  3  220 ? 34.948  -98.066  -10.908 1.00 130.72 ? 218 ASP   C O   1 
ATOM   5517  C  CB  . ASP   C  3  220 ? 34.641  -100.360 -12.474 1.00 127.70 ? 218 ASP   C CB  1 
ATOM   5518  C  CG  . ASP   C  3  220 ? 35.589  -99.884  -13.561 1.00 128.72 ? 218 ASP   C CG  1 
ATOM   5519  O  OD1 . ASP   C  3  220 ? 36.817  -99.941  -13.339 1.00 126.17 ? 218 ASP   C OD1 1 
ATOM   5520  O  OD2 . ASP   C  3  220 ? 35.091  -99.466  -14.625 1.00 130.54 ? 218 ASP   C OD2 1 
ATOM   5521  N  N   . ILE   C  3  221 ? 36.556  -98.992  -9.566  1.00 123.99 ? 219 ILE   C N   1 
ATOM   5522  C  CA  . ILE   C  3  221 ? 36.992  -97.747  -8.862  1.00 122.08 ? 219 ILE   C CA  1 
ATOM   5523  C  C   . ILE   C  3  221 ? 38.450  -97.447  -9.228  1.00 121.19 ? 219 ILE   C C   1 
ATOM   5524  O  O   . ILE   C  3  221 ? 39.295  -98.345  -9.058  1.00 124.26 ? 219 ILE   C O   1 
ATOM   5525  C  CB  . ILE   C  3  221 ? 36.813  -97.882  -7.336  1.00 120.42 ? 219 ILE   C CB  1 
ATOM   5526  C  CG1 . ILE   C  3  221 ? 35.370  -98.233  -6.962  1.00 119.68 ? 219 ILE   C CG1 1 
ATOM   5527  C  CG2 . ILE   C  3  221 ? 37.285  -96.621  -6.624  1.00 121.19 ? 219 ILE   C CG2 1 
ATOM   5528  C  CD1 . ILE   C  3  221 ? 35.214  -98.783  -5.565  1.00 118.63 ? 219 ILE   C CD1 1 
ATOM   5529  N  N   . VAL   C  3  222 ? 38.728  -96.222  -9.690  1.00 122.14 ? 220 VAL   C N   1 
ATOM   5530  C  CA  . VAL   C  3  222 ? 40.104  -95.726  -9.993  1.00 123.43 ? 220 VAL   C CA  1 
ATOM   5531  C  C   . VAL   C  3  222 ? 40.228  -94.270  -9.524  1.00 121.89 ? 220 VAL   C C   1 
ATOM   5532  O  O   . VAL   C  3  222 ? 39.243  -93.513  -9.653  1.00 119.39 ? 220 VAL   C O   1 
ATOM   5533  C  CB  . VAL   C  3  222 ? 40.449  -95.875  -11.489 1.00 126.14 ? 220 VAL   C CB  1 
ATOM   5534  C  CG1 . VAL   C  3  222 ? 39.607  -94.968  -12.376 1.00 126.08 ? 220 VAL   C CG1 1 
ATOM   5535  C  CG2 . VAL   C  3  222 ? 41.932  -95.653  -11.746 1.00 126.11 ? 220 VAL   C CG2 1 
ATOM   5536  N  N   . ALA   C  3  223 ? 41.401  -93.908  -8.996  1.00 122.72 ? 221 ALA   C N   1 
ATOM   5537  C  CA  . ALA   C  3  223 ? 41.775  -92.533  -8.593  1.00 123.02 ? 221 ALA   C CA  1 
ATOM   5538  C  C   . ALA   C  3  223 ? 42.562  -91.876  -9.733  1.00 125.04 ? 221 ALA   C C   1 
ATOM   5539  O  O   . ALA   C  3  223 ? 43.506  -92.515  -10.240 1.00 130.53 ? 221 ALA   C O   1 
ATOM   5540  C  CB  . ALA   C  3  223 ? 42.576  -92.574  -7.316  1.00 123.43 ? 221 ALA   C CB  1 
ATOM   5541  N  N   . LEU   C  3  224 ? 42.178  -90.655  -10.122 1.00 125.45 ? 222 LEU   C N   1 
ATOM   5542  C  CA  . LEU   C  3  224 ? 42.866  -89.849  -11.169 1.00 125.80 ? 222 LEU   C CA  1 
ATOM   5543  C  C   . LEU   C  3  224 ? 44.192  -89.318  -10.610 1.00 124.37 ? 222 LEU   C C   1 
ATOM   5544  O  O   . LEU   C  3  224 ? 44.250  -89.040  -9.397  1.00 118.89 ? 222 LEU   C O   1 
ATOM   5545  C  CB  . LEU   C  3  224 ? 41.965  -88.688  -11.606 1.00 126.54 ? 222 LEU   C CB  1 
ATOM   5546  C  CG  . LEU   C  3  224 ? 40.997  -88.977  -12.753 1.00 127.47 ? 222 LEU   C CG  1 
ATOM   5547  C  CD1 . LEU   C  3  224 ? 40.139  -90.200  -12.469 1.00 126.62 ? 222 LEU   C CD1 1 
ATOM   5548  C  CD2 . LEU   C  3  224 ? 40.120  -87.764  -13.023 1.00 126.61 ? 222 LEU   C CD2 1 
ATOM   5549  N  N   . SER   C  3  225 ? 45.205  -89.177  -11.472 1.00 129.92 ? 223 SER   C N   1 
ATOM   5550  C  CA  . SER   C  3  225 ? 46.537  -88.602  -11.144 1.00 134.46 ? 223 SER   C CA  1 
ATOM   5551  C  C   . SER   C  3  225 ? 46.490  -87.081  -11.327 1.00 136.15 ? 223 SER   C C   1 
ATOM   5552  O  O   . SER   C  3  225 ? 45.458  -86.580  -11.817 1.00 142.80 ? 223 SER   C O   1 
ATOM   5553  C  CB  . SER   C  3  225 ? 47.626  -89.225  -11.984 1.00 135.77 ? 223 SER   C CB  1 
ATOM   5554  O  OG  . SER   C  3  225 ? 47.520  -88.823  -13.342 1.00 136.42 ? 223 SER   C OG  1 
ATOM   5555  N  N   . SER   C  3  226 ? 47.568  -86.384  -10.952 1.00 137.44 ? 224 SER   C N   1 
ATOM   5556  C  CA  . SER   C  3  226 ? 47.702  -84.904  -11.033 1.00 136.90 ? 224 SER   C CA  1 
ATOM   5557  C  C   . SER   C  3  226 ? 47.409  -84.428  -12.461 1.00 141.18 ? 224 SER   C C   1 
ATOM   5558  O  O   . SER   C  3  226 ? 46.486  -83.606  -12.626 1.00 140.50 ? 224 SER   C O   1 
ATOM   5559  C  CB  . SER   C  3  226 ? 49.067  -84.452  -10.580 1.00 132.91 ? 224 SER   C CB  1 
ATOM   5560  O  OG  . SER   C  3  226 ? 49.256  -84.714  -9.199  1.00 128.10 ? 224 SER   C OG  1 
ATOM   5561  N  N   . GLU   C  3  227 ? 48.158  -84.942  -13.445 1.00 148.13 ? 225 GLU   C N   1 
ATOM   5562  C  CA  . GLU   C  3  227 ? 48.086  -84.532  -14.877 1.00 152.59 ? 225 GLU   C CA  1 
ATOM   5563  C  C   . GLU   C  3  227 ? 46.654  -84.695  -15.402 1.00 152.76 ? 225 GLU   C C   1 
ATOM   5564  O  O   . GLU   C  3  227 ? 46.161  -83.753  -16.058 1.00 149.92 ? 225 GLU   C O   1 
ATOM   5565  C  CB  . GLU   C  3  227 ? 49.057  -85.343  -15.739 1.00 159.32 ? 225 GLU   C CB  1 
ATOM   5566  C  CG  . GLU   C  3  227 ? 50.462  -84.767  -15.788 1.00 164.16 ? 225 GLU   C CG  1 
ATOM   5567  C  CD  . GLU   C  3  227 ? 51.317  -85.013  -14.556 1.00 166.72 ? 225 GLU   C CD  1 
ATOM   5568  O  OE1 . GLU   C  3  227 ? 50.805  -85.603  -13.583 1.00 168.82 ? 225 GLU   C OE1 1 
ATOM   5569  O  OE2 . GLU   C  3  227 ? 52.498  -84.612  -14.573 1.00 170.63 ? 225 GLU   C OE2 1 
ATOM   5570  N  N   . GLU   C  3  228 ? 46.026  -85.846  -15.132 1.00 151.30 ? 226 GLU   C N   1 
ATOM   5571  C  CA  . GLU   C  3  228 ? 44.642  -86.177  -15.576 1.00 147.89 ? 226 GLU   C CA  1 
ATOM   5572  C  C   . GLU   C  3  228 ? 43.675  -85.096  -15.075 1.00 145.49 ? 226 GLU   C C   1 
ATOM   5573  O  O   . GLU   C  3  228 ? 42.857  -84.620  -15.885 1.00 147.26 ? 226 GLU   C O   1 
ATOM   5574  C  CB  . GLU   C  3  228 ? 44.212  -87.556  -15.068 1.00 145.31 ? 226 GLU   C CB  1 
ATOM   5575  C  CG  . GLU   C  3  228 ? 44.987  -88.710  -15.683 1.00 144.24 ? 226 GLU   C CG  1 
ATOM   5576  C  CD  . GLU   C  3  228 ? 44.538  -90.093  -15.237 1.00 141.26 ? 226 GLU   C CD  1 
ATOM   5577  O  OE1 . GLU   C  3  228 ? 43.314  -90.323  -15.156 1.00 132.44 ? 226 GLU   C OE1 1 
ATOM   5578  O  OE2 . GLU   C  3  228 ? 45.414  -90.940  -14.970 1.00 138.85 ? 226 GLU   C OE2 1 
ATOM   5579  N  N   . ILE   C  3  229 ? 43.780  -84.721  -13.795 1.00 144.03 ? 227 ILE   C N   1 
ATOM   5580  C  CA  . ILE   C  3  229 ? 42.933  -83.673  -13.148 1.00 144.04 ? 227 ILE   C CA  1 
ATOM   5581  C  C   . ILE   C  3  229 ? 43.328  -82.307  -13.722 1.00 143.49 ? 227 ILE   C C   1 
ATOM   5582  O  O   . ILE   C  3  229 ? 42.419  -81.503  -13.994 1.00 145.40 ? 227 ILE   C O   1 
ATOM   5583  C  CB  . ILE   C  3  229 ? 43.061  -83.706  -11.608 1.00 144.86 ? 227 ILE   C CB  1 
ATOM   5584  C  CG1 . ILE   C  3  229 ? 42.690  -85.073  -11.027 1.00 145.24 ? 227 ILE   C CG1 1 
ATOM   5585  C  CG2 . ILE   C  3  229 ? 42.232  -82.598  -10.972 1.00 141.22 ? 227 ILE   C CG2 1 
ATOM   5586  C  CD1 . ILE   C  3  229 ? 43.261  -85.333  -9.651  1.00 147.75 ? 227 ILE   C CD1 1 
ATOM   5587  N  N   . ASN   C  3  230 ? 44.633  -82.065  -13.898 1.00 145.98 ? 228 ASN   C N   1 
ATOM   5588  C  CA  . ASN   C  3  230 ? 45.198  -80.770  -14.369 1.00 147.02 ? 228 ASN   C CA  1 
ATOM   5589  C  C   . ASN   C  3  230 ? 44.634  -80.436  -15.757 1.00 148.15 ? 228 ASN   C C   1 
ATOM   5590  O  O   . ASN   C  3  230 ? 44.473  -79.235  -16.049 1.00 149.44 ? 228 ASN   C O   1 
ATOM   5591  C  CB  . ASN   C  3  230 ? 46.731  -80.784  -14.386 1.00 149.54 ? 228 ASN   C CB  1 
ATOM   5592  C  CG  . ASN   C  3  230 ? 47.351  -79.409  -14.237 1.00 149.35 ? 228 ASN   C CG  1 
ATOM   5593  O  OD1 . ASN   C  3  230 ? 46.670  -78.391  -14.349 1.00 151.13 ? 228 ASN   C OD1 1 
ATOM   5594  N  ND2 . ASN   C  3  230 ? 48.648  -79.365  -13.980 1.00 149.84 ? 228 ASN   C ND2 1 
ATOM   5595  N  N   . GLN   C  3  231 ? 44.352  -81.454  -16.578 1.00 147.19 ? 229 GLN   C N   1 
ATOM   5596  C  CA  . GLN   C  3  231 ? 43.774  -81.291  -17.941 1.00 149.58 ? 229 GLN   C CA  1 
ATOM   5597  C  C   . GLN   C  3  231 ? 42.354  -80.721  -17.840 1.00 151.56 ? 229 GLN   C C   1 
ATOM   5598  O  O   . GLN   C  3  231 ? 42.006  -79.878  -18.691 1.00 156.95 ? 229 GLN   C O   1 
ATOM   5599  C  CB  . GLN   C  3  231 ? 43.789  -82.618  -18.700 1.00 147.86 ? 229 GLN   C CB  1 
ATOM   5600  C  CG  . GLN   C  3  231 ? 45.167  -82.988  -19.225 1.00 150.22 ? 229 GLN   C CG  1 
ATOM   5601  C  CD  . GLN   C  3  231 ? 45.267  -84.446  -19.598 1.00 150.24 ? 229 GLN   C CD  1 
ATOM   5602  O  OE1 . GLN   C  3  231 ? 44.330  -85.036  -20.133 1.00 149.55 ? 229 GLN   C OE1 1 
ATOM   5603  N  NE2 . GLN   C  3  231 ? 46.414  -85.044  -19.319 1.00 153.23 ? 229 GLN   C NE2 1 
ATOM   5604  N  N   . TYR   C  3  232 ? 41.569  -81.162  -16.850 1.00 154.12 ? 230 TYR   C N   1 
ATOM   5605  C  CA  . TYR   C  3  232 ? 40.208  -80.636  -16.555 1.00 155.14 ? 230 TYR   C CA  1 
ATOM   5606  C  C   . TYR   C  3  232 ? 40.313  -79.171  -16.112 1.00 158.00 ? 230 TYR   C C   1 
ATOM   5607  O  O   . TYR   C  3  232 ? 39.523  -78.345  -16.609 1.00 164.70 ? 230 TYR   C O   1 
ATOM   5608  C  CB  . TYR   C  3  232 ? 39.493  -81.486  -15.500 1.00 152.64 ? 230 TYR   C CB  1 
ATOM   5609  C  CG  . TYR   C  3  232 ? 38.924  -82.779  -16.026 1.00 148.01 ? 230 TYR   C CG  1 
ATOM   5610  C  CD1 . TYR   C  3  232 ? 37.660  -82.825  -16.591 1.00 147.52 ? 230 TYR   C CD1 1 
ATOM   5611  C  CD2 . TYR   C  3  232 ? 39.651  -83.957  -15.967 1.00 146.72 ? 230 TYR   C CD2 1 
ATOM   5612  C  CE1 . TYR   C  3  232 ? 37.131  -84.008  -17.080 1.00 145.06 ? 230 TYR   C CE1 1 
ATOM   5613  C  CE2 . TYR   C  3  232 ? 39.137  -85.148  -16.451 1.00 144.47 ? 230 TYR   C CE2 1 
ATOM   5614  C  CZ  . TYR   C  3  232 ? 37.871  -85.174  -17.009 1.00 146.47 ? 230 TYR   C CZ  1 
ATOM   5615  O  OH  . TYR   C  3  232 ? 37.357  -86.343  -17.488 1.00 144.64 ? 230 TYR   C OH  1 
ATOM   5616  N  N   . VAL   C  3  233 ? 41.267  -78.864  -15.225 1.00 156.08 ? 231 VAL   C N   1 
ATOM   5617  C  CA  . VAL   C  3  233 ? 41.513  -77.488  -14.695 1.00 157.72 ? 231 VAL   C CA  1 
ATOM   5618  C  C   . VAL   C  3  233 ? 41.843  -76.569  -15.878 1.00 155.84 ? 231 VAL   C C   1 
ATOM   5619  O  O   . VAL   C  3  233 ? 41.194  -75.511  -15.996 1.00 162.99 ? 231 VAL   C O   1 
ATOM   5620  C  CB  . VAL   C  3  233 ? 42.631  -77.461  -13.632 1.00 157.16 ? 231 VAL   C CB  1 
ATOM   5621  C  CG1 . VAL   C  3  233 ? 42.914  -76.048  -13.139 1.00 156.53 ? 231 VAL   C CG1 1 
ATOM   5622  C  CG2 . VAL   C  3  233 ? 42.325  -78.375  -12.455 1.00 158.42 ? 231 VAL   C CG2 1 
ATOM   5623  N  N   . THR   C  3  234 ? 42.805  -76.970  -16.720 1.00 149.87 ? 232 THR   C N   1 
ATOM   5624  C  CA  . THR   C  3  234 ? 43.299  -76.190  -17.889 1.00 147.62 ? 232 THR   C CA  1 
ATOM   5625  C  C   . THR   C  3  234 ? 42.146  -75.911  -18.859 1.00 149.48 ? 232 THR   C C   1 
ATOM   5626  O  O   . THR   C  3  234 ? 42.031  -74.756  -19.315 1.00 153.37 ? 232 THR   C O   1 
ATOM   5627  C  CB  . THR   C  3  234 ? 44.427  -76.915  -18.634 1.00 148.37 ? 232 THR   C CB  1 
ATOM   5628  O  OG1 . THR   C  3  234 ? 45.415  -77.328  -17.689 1.00 144.64 ? 232 THR   C OG1 1 
ATOM   5629  C  CG2 . THR   C  3  234 ? 45.068  -76.046  -19.695 1.00 149.00 ? 232 THR   C CG2 1 
ATOM   5630  N  N   . GLN   C  3  235 ? 41.343  -76.933  -19.166 1.00 144.18 ? 233 GLN   C N   1 
ATOM   5631  C  CA  . GLN   C  3  235 ? 40.236  -76.863  -20.157 1.00 147.98 ? 233 GLN   C CA  1 
ATOM   5632  C  C   . GLN   C  3  235 ? 39.141  -75.909  -19.658 1.00 150.67 ? 233 GLN   C C   1 
ATOM   5633  O  O   . GLN   C  3  235 ? 38.629  -75.129  -20.486 1.00 157.24 ? 233 GLN   C O   1 
ATOM   5634  C  CB  . GLN   C  3  235 ? 39.664  -78.257  -20.421 1.00 146.71 ? 233 GLN   C CB  1 
ATOM   5635  C  CG  . GLN   C  3  235 ? 38.699  -78.302  -21.598 1.00 149.89 ? 233 GLN   C CG  1 
ATOM   5636  C  CD  . GLN   C  3  235 ? 37.786  -79.501  -21.545 1.00 151.13 ? 233 GLN   C CD  1 
ATOM   5637  O  OE1 . GLN   C  3  235 ? 36.576  -79.375  -21.371 1.00 154.12 ? 233 GLN   C OE1 1 
ATOM   5638  N  NE2 . GLN   C  3  235 ? 38.363  -80.683  -21.687 1.00 152.76 ? 233 GLN   C NE2 1 
ATOM   5639  N  N   . ILE   C  3  236 ? 38.800  -75.966  -18.365 1.00 148.55 ? 234 ILE   C N   1 
ATOM   5640  C  CA  . ILE   C  3  236 ? 37.691  -75.172  -17.748 1.00 151.74 ? 234 ILE   C CA  1 
ATOM   5641  C  C   . ILE   C  3  236 ? 38.037  -73.676  -17.785 1.00 154.80 ? 234 ILE   C C   1 
ATOM   5642  O  O   . ILE   C  3  236 ? 37.123  -72.878  -18.072 1.00 150.87 ? 234 ILE   C O   1 
ATOM   5643  C  CB  . ILE   C  3  236 ? 37.384  -75.664  -16.316 1.00 151.22 ? 234 ILE   C CB  1 
ATOM   5644  C  CG1 . ILE   C  3  236 ? 36.714  -77.041  -16.330 1.00 150.27 ? 234 ILE   C CG1 1 
ATOM   5645  C  CG2 . ILE   C  3  236 ? 36.542  -74.649  -15.553 1.00 152.98 ? 234 ILE   C CG2 1 
ATOM   5646  C  CD1 . ILE   C  3  236 ? 36.825  -77.794  -15.024 1.00 149.74 ? 234 ILE   C CD1 1 
ATOM   5647  N  N   . GLU   C  3  237 ? 39.295  -73.314  -17.498 1.00 161.41 ? 235 GLU   C N   1 
ATOM   5648  C  CA  . GLU   C  3  237 ? 39.771  -71.904  -17.405 1.00 164.39 ? 235 GLU   C CA  1 
ATOM   5649  C  C   . GLU   C  3  237 ? 39.747  -71.234  -18.786 1.00 168.50 ? 235 GLU   C C   1 
ATOM   5650  O  O   . GLU   C  3  237 ? 39.460  -70.022  -18.842 1.00 171.62 ? 235 GLU   C O   1 
ATOM   5651  C  CB  . GLU   C  3  237 ? 41.178  -71.839  -16.804 1.00 166.22 ? 235 GLU   C CB  1 
ATOM   5652  C  CG  . GLU   C  3  237 ? 41.194  -71.953  -15.291 1.00 164.36 ? 235 GLU   C CG  1 
ATOM   5653  C  CD  . GLU   C  3  237 ? 42.576  -71.917  -14.661 1.00 167.49 ? 235 GLU   C CD  1 
ATOM   5654  O  OE1 . GLU   C  3  237 ? 42.673  -71.516  -13.485 1.00 173.82 ? 235 GLU   C OE1 1 
ATOM   5655  O  OE2 . GLU   C  3  237 ? 43.548  -72.293  -15.344 1.00 169.40 ? 235 GLU   C OE2 1 
ATOM   5656  N  N   . GLN   C  3  238 ? 40.043  -71.984  -19.853 1.00 166.60 ? 236 GLN   C N   1 
ATOM   5657  C  CA  . GLN   C  3  238 ? 40.117  -71.458  -21.244 1.00 169.95 ? 236 GLN   C CA  1 
ATOM   5658  C  C   . GLN   C  3  238 ? 38.706  -71.147  -21.760 1.00 169.07 ? 236 GLN   C C   1 
ATOM   5659  O  O   . GLN   C  3  238 ? 38.560  -70.151  -22.495 1.00 173.00 ? 236 GLN   C O   1 
ATOM   5660  C  CB  . GLN   C  3  238 ? 40.854  -72.445  -22.151 1.00 172.50 ? 236 GLN   C CB  1 
ATOM   5661  C  CG  . GLN   C  3  238 ? 42.345  -72.521  -21.855 1.00 174.04 ? 236 GLN   C CG  1 
ATOM   5662  C  CD  . GLN   C  3  238 ? 43.076  -73.493  -22.748 1.00 176.31 ? 236 GLN   C CD  1 
ATOM   5663  O  OE1 . GLN   C  3  238 ? 42.478  -74.366  -23.373 1.00 177.28 ? 236 GLN   C OE1 1 
ATOM   5664  N  NE2 . GLN   C  3  238 ? 44.390  -73.347  -22.811 1.00 180.59 ? 236 GLN   C NE2 1 
ATOM   5665  N  N   . GLU   C  3  239 ? 37.713  -71.959  -21.386 1.00 163.76 ? 237 GLU   C N   1 
ATOM   5666  C  CA  . GLU   C  3  239 ? 36.280  -71.739  -21.728 1.00 165.76 ? 237 GLU   C CA  1 
ATOM   5667  C  C   . GLU   C  3  239 ? 35.737  -70.548  -20.927 1.00 169.81 ? 237 GLU   C C   1 
ATOM   5668  O  O   . GLU   C  3  239 ? 34.819  -69.871  -21.435 1.00 168.25 ? 237 GLU   C O   1 
ATOM   5669  C  CB  . GLU   C  3  239 ? 35.458  -73.000  -21.451 1.00 162.62 ? 237 GLU   C CB  1 
ATOM   5670  C  CG  . GLU   C  3  239 ? 35.843  -74.179  -22.326 1.00 161.44 ? 237 GLU   C CG  1 
ATOM   5671  C  CD  . GLU   C  3  239 ? 35.125  -75.478  -21.997 1.00 158.98 ? 237 GLU   C CD  1 
ATOM   5672  O  OE1 . GLU   C  3  239 ? 33.898  -75.437  -21.784 1.00 158.77 ? 237 GLU   C OE1 1 
ATOM   5673  O  OE2 . GLU   C  3  239 ? 35.797  -76.527  -21.949 1.00 153.14 ? 237 GLU   C OE2 1 
ATOM   5674  N  N   . LYS   C  3  240 ? 36.286  -70.304  -19.729 1.00 168.96 ? 238 LYS   C N   1 
ATOM   5675  C  CA  . LYS   C  3  240 ? 35.832  -69.245  -18.785 1.00 168.58 ? 238 LYS   C CA  1 
ATOM   5676  C  C   . LYS   C  3  240 ? 36.132  -67.862  -19.375 1.00 171.41 ? 238 LYS   C C   1 
ATOM   5677  O  O   . LYS   C  3  240 ? 35.229  -67.004  -19.329 1.00 177.99 ? 238 LYS   C O   1 
ATOM   5678  C  CB  . LYS   C  3  240 ? 36.497  -69.411  -17.414 1.00 165.06 ? 238 LYS   C CB  1 
ATOM   5679  C  CG  . LYS   C  3  240 ? 35.904  -68.550  -16.307 1.00 163.75 ? 238 LYS   C CG  1 
ATOM   5680  C  CD  . LYS   C  3  240 ? 36.570  -68.740  -14.964 1.00 164.65 ? 238 LYS   C CD  1 
ATOM   5681  C  CE  . LYS   C  3  240 ? 36.006  -67.823  -13.900 1.00 165.73 ? 238 LYS   C CE  1 
ATOM   5682  N  NZ  . LYS   C  3  240 ? 36.647  -68.052  -12.585 1.00 167.29 ? 238 LYS   C NZ  1 
ATOM   5683  N  N   . GLN   C  3  241 ? 37.346  -67.655  -19.901 1.00 172.52 ? 239 GLN   C N   1 
ATOM   5684  C  CA  . GLN   C  3  241 ? 37.769  -66.375  -20.535 1.00 173.92 ? 239 GLN   C CA  1 
ATOM   5685  C  C   . GLN   C  3  241 ? 36.940  -66.163  -21.807 1.00 171.95 ? 239 GLN   C C   1 
ATOM   5686  O  O   . GLN   C  3  241 ? 37.433  -66.496  -22.905 1.00 167.03 ? 239 GLN   C O   1 
ATOM   5687  C  CB  . GLN   C  3  241 ? 39.274  -66.370  -20.818 1.00 173.26 ? 239 GLN   C CB  1 
ATOM   5688  C  CG  . GLN   C  3  241 ? 40.117  -66.110  -19.579 1.00 173.53 ? 239 GLN   C CG  1 
ATOM   5689  C  CD  . GLN   C  3  241 ? 41.574  -66.444  -19.788 1.00 175.65 ? 239 GLN   C CD  1 
ATOM   5690  O  OE1 . GLN   C  3  241 ? 42.129  -66.243  -20.867 1.00 173.95 ? 239 GLN   C OE1 1 
ATOM   5691  N  NE2 . GLN   C  3  241 ? 42.212  -66.954  -18.746 1.00 177.01 ? 239 GLN   C NE2 1 
ATOM   5692  N  N   . GLU   C  3  242 ? 35.721  -65.638  -21.645 1.00 176.41 ? 240 GLU   C N   1 
ATOM   5693  C  CA  . GLU   C  3  242 ? 34.731  -65.442  -22.737 1.00 177.90 ? 240 GLU   C CA  1 
ATOM   5694  C  C   . GLU   C  3  242 ? 33.860  -64.222  -22.415 1.00 182.02 ? 240 GLU   C C   1 
ATOM   5695  O  O   . GLU   C  3  242 ? 33.014  -64.260  -21.521 1.00 186.07 ? 240 GLU   C O   1 
ATOM   5696  C  CB  . GLU   C  3  242 ? 33.892  -66.711  -22.909 1.00 174.57 ? 240 GLU   C CB  1 
ATOM   5697  C  CG  . GLU   C  3  242 ? 33.593  -67.042  -24.358 1.00 175.51 ? 240 GLU   C CG  1 
ATOM   5698  C  CD  . GLU   C  3  242 ? 34.751  -67.664  -25.122 1.00 174.79 ? 240 GLU   C CD  1 
ATOM   5699  O  OE1 . GLU   C  3  242 ? 34.741  -67.588  -26.364 1.00 180.61 ? 240 GLU   C OE1 1 
ATOM   5700  O  OE2 . GLU   C  3  242 ? 35.658  -68.225  -24.475 1.00 173.50 ? 240 GLU   C OE2 1 
ATOM   5701  N  N   . ASP   D  4  9   ? 27.640  -78.103  36.159  1.00 153.13 ? 1   ASP   D N   1 
ATOM   5702  C  CA  . ASP   D  4  9   ? 26.408  -78.585  35.458  1.00 150.89 ? 1   ASP   D CA  1 
ATOM   5703  C  C   . ASP   D  4  9   ? 25.444  -79.149  36.515  1.00 149.33 ? 1   ASP   D C   1 
ATOM   5704  O  O   . ASP   D  4  9   ? 25.319  -78.513  37.582  1.00 158.61 ? 1   ASP   D O   1 
ATOM   5705  C  CB  . ASP   D  4  9   ? 26.769  -79.561  34.330  1.00 148.48 ? 1   ASP   D CB  1 
ATOM   5706  C  CG  . ASP   D  4  9   ? 25.750  -79.626  33.200  1.00 141.29 ? 1   ASP   D CG  1 
ATOM   5707  O  OD1 . ASP   D  4  9   ? 24.592  -79.218  33.422  1.00 146.25 ? 1   ASP   D OD1 1 
ATOM   5708  O  OD2 . ASP   D  4  9   ? 26.124  -80.084  32.101  1.00 134.99 ? 1   ASP   D OD2 1 
ATOM   5709  N  N   . ARG   D  4  10  ? 24.790  -80.284  36.241  1.00 145.94 ? 2   ARG   D N   1 
ATOM   5710  C  CA  . ARG   D  4  10  ? 23.694  -80.850  37.076  1.00 141.89 ? 2   ARG   D CA  1 
ATOM   5711  C  C   . ARG   D  4  10  ? 23.351  -82.260  36.571  1.00 134.86 ? 2   ARG   D C   1 
ATOM   5712  O  O   . ARG   D  4  10  ? 23.648  -82.553  35.394  1.00 138.45 ? 2   ARG   D O   1 
ATOM   5713  C  CB  . ARG   D  4  10  ? 22.485  -79.911  37.001  1.00 137.84 ? 2   ARG   D CB  1 
ATOM   5714  C  CG  . ARG   D  4  10  ? 21.370  -80.187  37.999  1.00 138.00 ? 2   ARG   D CG  1 
ATOM   5715  C  CD  . ARG   D  4  10  ? 20.236  -79.206  37.763  1.00 139.93 ? 2   ARG   D CD  1 
ATOM   5716  N  NE  . ARG   D  4  10  ? 19.810  -79.231  36.366  1.00 143.40 ? 2   ARG   D NE  1 
ATOM   5717  C  CZ  . ARG   D  4  10  ? 19.381  -78.184  35.658  1.00 148.13 ? 2   ARG   D CZ  1 
ATOM   5718  N  NH1 . ARG   D  4  10  ? 19.305  -76.978  36.198  1.00 149.75 ? 2   ARG   D NH1 1 
ATOM   5719  N  NH2 . ARG   D  4  10  ? 19.033  -78.352  34.393  1.00 152.22 ? 2   ARG   D NH2 1 
ATOM   5720  N  N   . GLY   D  4  11  ? 22.748  -83.092  37.429  1.00 128.56 ? 3   GLY   D N   1 
ATOM   5721  C  CA  . GLY   D  4  11  ? 22.328  -84.470  37.104  1.00 122.07 ? 3   GLY   D CA  1 
ATOM   5722  C  C   . GLY   D  4  11  ? 21.388  -84.510  35.909  1.00 117.62 ? 3   GLY   D C   1 
ATOM   5723  O  O   . GLY   D  4  11  ? 20.615  -83.546  35.731  1.00 115.01 ? 3   GLY   D O   1 
ATOM   5724  N  N   . VAL   D  4  12  ? 21.452  -85.584  35.118  1.00 111.53 ? 4   VAL   D N   1 
ATOM   5725  C  CA  . VAL   D  4  12  ? 20.615  -85.784  33.898  1.00 109.78 ? 4   VAL   D CA  1 
ATOM   5726  C  C   . VAL   D  4  12  ? 19.179  -86.128  34.317  1.00 106.64 ? 4   VAL   D C   1 
ATOM   5727  O  O   . VAL   D  4  12  ? 18.251  -85.746  33.577  1.00 106.60 ? 4   VAL   D O   1 
ATOM   5728  C  CB  . VAL   D  4  12  ? 21.225  -86.859  32.977  1.00 111.78 ? 4   VAL   D CB  1 
ATOM   5729  C  CG1 . VAL   D  4  12  ? 20.230  -87.376  31.947  1.00 115.45 ? 4   VAL   D CG1 1 
ATOM   5730  C  CG2 . VAL   D  4  12  ? 22.479  -86.343  32.292  1.00 111.49 ? 4   VAL   D CG2 1 
ATOM   5731  N  N   . SER   D  4  13  ? 19.003  -86.813  35.453  1.00 104.32 ? 5   SER   D N   1 
ATOM   5732  C  CA  . SER   D  4  13  ? 17.684  -87.232  36.001  1.00 107.13 ? 5   SER   D CA  1 
ATOM   5733  C  C   . SER   D  4  13  ? 17.243  -86.296  37.135  1.00 107.29 ? 5   SER   D C   1 
ATOM   5734  O  O   . SER   D  4  13  ? 16.657  -86.798  38.116  1.00 115.41 ? 5   SER   D O   1 
ATOM   5735  C  CB  . SER   D  4  13  ? 17.728  -88.666  36.471  1.00 104.04 ? 5   SER   D CB  1 
ATOM   5736  O  OG  . SER   D  4  13  ? 18.078  -89.542  35.410  1.00 102.60 ? 5   SER   D OG  1 
ATOM   5737  N  N   . THR   D  4  14  ? 17.485  -84.987  37.008  1.00 107.05 ? 6   THR   D N   1 
ATOM   5738  C  CA  . THR   D  4  14  ? 17.147  -83.978  38.048  1.00 105.28 ? 6   THR   D CA  1 
ATOM   5739  C  C   . THR   D  4  14  ? 15.710  -83.496  37.833  1.00 104.50 ? 6   THR   D C   1 
ATOM   5740  O  O   . THR   D  4  14  ? 15.299  -83.360  36.664  1.00 105.62 ? 6   THR   D O   1 
ATOM   5741  C  CB  . THR   D  4  14  ? 18.139  -82.808  38.051  1.00 103.95 ? 6   THR   D CB  1 
ATOM   5742  O  OG1 . THR   D  4  14  ? 19.460  -83.345  38.030  1.00 100.44 ? 6   THR   D OG1 1 
ATOM   5743  C  CG2 . THR   D  4  14  ? 17.984  -81.916  39.263  1.00 108.11 ? 6   THR   D CG2 1 
ATOM   5744  N  N   . PHE   D  4  15  ? 14.982  -83.263  38.928  1.00 103.12 ? 7   PHE   D N   1 
ATOM   5745  C  CA  . PHE   D  4  15  ? 13.646  -82.613  38.939  1.00 108.62 ? 7   PHE   D CA  1 
ATOM   5746  C  C   . PHE   D  4  15  ? 13.812  -81.093  39.024  1.00 111.52 ? 7   PHE   D C   1 
ATOM   5747  O  O   . PHE   D  4  15  ? 14.670  -80.618  39.799  1.00 114.44 ? 7   PHE   D O   1 
ATOM   5748  C  CB  . PHE   D  4  15  ? 12.802  -83.097  40.120  1.00 109.80 ? 7   PHE   D CB  1 
ATOM   5749  C  CG  . PHE   D  4  15  ? 12.087  -84.402  39.890  1.00 110.79 ? 7   PHE   D CG  1 
ATOM   5750  C  CD1 . PHE   D  4  15  ? 11.015  -84.474  39.013  1.00 114.07 ? 7   PHE   D CD1 1 
ATOM   5751  C  CD2 . PHE   D  4  15  ? 12.475  -85.554  40.556  1.00 110.58 ? 7   PHE   D CD2 1 
ATOM   5752  C  CE1 . PHE   D  4  15  ? 10.353  -85.673  38.801  1.00 113.43 ? 7   PHE   D CE1 1 
ATOM   5753  C  CE2 . PHE   D  4  15  ? 11.812  -86.752  40.342  1.00 110.24 ? 7   PHE   D CE2 1 
ATOM   5754  C  CZ  . PHE   D  4  15  ? 10.752  -86.810  39.466  1.00 112.06 ? 7   PHE   D CZ  1 
ATOM   5755  N  N   . SER   D  4  16  ? 13.001  -80.354  38.260  1.00 111.16 ? 8   SER   D N   1 
ATOM   5756  C  CA  . SER   D  4  16  ? 12.814  -78.889  38.411  1.00 112.14 ? 8   SER   D CA  1 
ATOM   5757  C  C   . SER   D  4  16  ? 12.032  -78.639  39.697  1.00 110.01 ? 8   SER   D C   1 
ATOM   5758  O  O   . SER   D  4  16  ? 11.422  -79.556  40.241  1.00 103.41 ? 8   SER   D O   1 
ATOM   5759  C  CB  . SER   D  4  16  ? 12.112  -78.294  37.215  1.00 112.79 ? 8   SER   D CB  1 
ATOM   5760  O  OG  . SER   D  4  16  ? 10.708  -78.505  37.290  1.00 114.33 ? 8   SER   D OG  1 
ATOM   5761  N  N   . PRO   D  4  17  ? 12.017  -77.397  40.227  1.00 112.63 ? 9   PRO   D N   1 
ATOM   5762  C  CA  . PRO   D  4  17  ? 11.183  -77.079  41.387  1.00 115.02 ? 9   PRO   D CA  1 
ATOM   5763  C  C   . PRO   D  4  17  ? 9.679   -77.305  41.144  1.00 113.28 ? 9   PRO   D C   1 
ATOM   5764  O  O   . PRO   D  4  17  ? 8.973   -77.500  42.113  1.00 111.50 ? 9   PRO   D O   1 
ATOM   5765  C  CB  . PRO   D  4  17  ? 11.488  -75.595  41.645  1.00 117.43 ? 9   PRO   D CB  1 
ATOM   5766  C  CG  . PRO   D  4  17  ? 12.839  -75.369  40.997  1.00 117.31 ? 9   PRO   D CG  1 
ATOM   5767  C  CD  . PRO   D  4  17  ? 12.819  -76.252  39.770  1.00 113.82 ? 9   PRO   D CD  1 
ATOM   5768  N  N   . GLU   D  4  18  ? 9.233   -77.292  39.880  1.00 116.61 ? 10  GLU   D N   1 
ATOM   5769  C  CA  . GLU   D  4  18  ? 7.808   -77.477  39.480  1.00 121.36 ? 10  GLU   D CA  1 
ATOM   5770  C  C   . GLU   D  4  18  ? 7.479   -78.974  39.380  1.00 119.35 ? 10  GLU   D C   1 
ATOM   5771  O  O   . GLU   D  4  18  ? 6.314   -79.297  39.066  1.00 120.80 ? 10  GLU   D O   1 
ATOM   5772  C  CB  . GLU   D  4  18  ? 7.510   -76.763  38.156  1.00 124.27 ? 10  GLU   D CB  1 
ATOM   5773  C  CG  . GLU   D  4  18  ? 7.589   -75.249  38.245  1.00 128.40 ? 10  GLU   D CG  1 
ATOM   5774  C  CD  . GLU   D  4  18  ? 8.995   -74.679  38.173  1.00 130.78 ? 10  GLU   D CD  1 
ATOM   5775  O  OE1 . GLU   D  4  18  ? 9.319   -73.813  39.009  1.00 138.01 ? 10  GLU   D OE1 1 
ATOM   5776  O  OE2 . GLU   D  4  18  ? 9.762   -75.101  37.283  1.00 127.10 ? 10  GLU   D OE2 1 
ATOM   5777  N  N   . GLY   D  4  19  ? 8.457   -79.852  39.634  1.00 118.98 ? 11  GLY   D N   1 
ATOM   5778  C  CA  . GLY   D  4  19  ? 8.270   -81.316  39.689  1.00 116.38 ? 11  GLY   D CA  1 
ATOM   5779  C  C   . GLY   D  4  19  ? 8.330   -81.975  38.319  1.00 113.10 ? 11  GLY   D C   1 
ATOM   5780  O  O   . GLY   D  4  19  ? 7.652   -83.004  38.140  1.00 111.93 ? 11  GLY   D O   1 
ATOM   5781  N  N   . ARG   D  4  20  ? 9.114   -81.419  37.388  1.00 112.75 ? 12  ARG   D N   1 
ATOM   5782  C  CA  . ARG   D  4  20  ? 9.307   -81.969  36.018  1.00 111.39 ? 12  ARG   D CA  1 
ATOM   5783  C  C   . ARG   D  4  20  ? 10.790  -82.283  35.798  1.00 105.41 ? 12  ARG   D C   1 
ATOM   5784  O  O   . ARG   D  4  20  ? 11.639  -81.593  36.391  1.00 103.76 ? 12  ARG   D O   1 
ATOM   5785  C  CB  . ARG   D  4  20  ? 8.797   -80.985  34.961  1.00 113.77 ? 12  ARG   D CB  1 
ATOM   5786  C  CG  . ARG   D  4  20  ? 7.315   -80.660  35.079  1.00 118.12 ? 12  ARG   D CG  1 
ATOM   5787  C  CD  . ARG   D  4  20  ? 6.721   -80.216  33.757  1.00 119.11 ? 12  ARG   D CD  1 
ATOM   5788  N  NE  . ARG   D  4  20  ? 5.701   -79.191  33.925  1.00 125.86 ? 12  ARG   D NE  1 
ATOM   5789  C  CZ  . ARG   D  4  20  ? 5.933   -77.880  34.001  1.00 133.09 ? 12  ARG   D CZ  1 
ATOM   5790  N  NH1 . ARG   D  4  20  ? 7.165   -77.401  33.929  1.00 136.52 ? 12  ARG   D NH1 1 
ATOM   5791  N  NH2 . ARG   D  4  20  ? 4.919   -77.044  34.151  1.00 137.83 ? 12  ARG   D NH2 1 
ATOM   5792  N  N   . LEU   D  4  21  ? 11.079  -83.290  34.969  1.00 102.83 ? 13  LEU   D N   1 
ATOM   5793  C  CA  . LEU   D  4  21  ? 12.461  -83.703  34.612  1.00 100.98 ? 13  LEU   D CA  1 
ATOM   5794  C  C   . LEU   D  4  21  ? 12.983  -82.785  33.503  1.00 99.40  ? 13  LEU   D C   1 
ATOM   5795  O  O   . LEU   D  4  21  ? 12.392  -82.786  32.407  1.00 98.04  ? 13  LEU   D O   1 
ATOM   5796  C  CB  . LEU   D  4  21  ? 12.457  -85.169  34.170  1.00 100.62 ? 13  LEU   D CB  1 
ATOM   5797  C  CG  . LEU   D  4  21  ? 12.033  -86.174  35.240  1.00 102.10 ? 13  LEU   D CG  1 
ATOM   5798  C  CD1 . LEU   D  4  21  ? 11.838  -87.557  34.639  1.00 101.58 ? 13  LEU   D CD1 1 
ATOM   5799  C  CD2 . LEU   D  4  21  ? 13.046  -86.226  36.376  1.00 103.03 ? 13  LEU   D CD2 1 
ATOM   5800  N  N   . PHE   D  4  22  ? 14.043  -82.030  33.801  1.00 99.47  ? 14  PHE   D N   1 
ATOM   5801  C  CA  . PHE   D  4  22  ? 14.668  -81.022  32.905  1.00 100.97 ? 14  PHE   D CA  1 
ATOM   5802  C  C   . PHE   D  4  22  ? 14.864  -81.613  31.506  1.00 99.78  ? 14  PHE   D C   1 
ATOM   5803  O  O   . PHE   D  4  22  ? 14.375  -81.018  30.527  1.00 100.91 ? 14  PHE   D O   1 
ATOM   5804  C  CB  . PHE   D  4  22  ? 16.002  -80.544  33.484  1.00 102.78 ? 14  PHE   D CB  1 
ATOM   5805  C  CG  . PHE   D  4  22  ? 15.877  -79.538  34.601  1.00 103.77 ? 14  PHE   D CG  1 
ATOM   5806  C  CD1 . PHE   D  4  22  ? 15.451  -78.244  34.341  1.00 105.99 ? 14  PHE   D CD1 1 
ATOM   5807  C  CD2 . PHE   D  4  22  ? 16.192  -79.877  35.909  1.00 103.05 ? 14  PHE   D CD2 1 
ATOM   5808  C  CE1 . PHE   D  4  22  ? 15.336  -77.315  35.363  1.00 106.62 ? 14  PHE   D CE1 1 
ATOM   5809  C  CE2 . PHE   D  4  22  ? 16.077  -78.946  36.930  1.00 104.78 ? 14  PHE   D CE2 1 
ATOM   5810  C  CZ  . PHE   D  4  22  ? 15.650  -77.667  36.656  1.00 106.68 ? 14  PHE   D CZ  1 
ATOM   5811  N  N   . GLN   D  4  23  ? 15.547  -82.757  31.428  1.00 97.26  ? 15  GLN   D N   1 
ATOM   5812  C  CA  . GLN   D  4  23  ? 15.999  -83.376  30.153  1.00 96.86  ? 15  GLN   D CA  1 
ATOM   5813  C  C   . GLN   D  4  23  ? 14.799  -83.842  29.321  1.00 98.34  ? 15  GLN   D C   1 
ATOM   5814  O  O   . GLN   D  4  23  ? 14.894  -83.772  28.081  1.00 100.79 ? 15  GLN   D O   1 
ATOM   5815  C  CB  . GLN   D  4  23  ? 16.962  -84.525  30.442  1.00 95.97  ? 15  GLN   D CB  1 
ATOM   5816  C  CG  . GLN   D  4  23  ? 18.349  -84.045  30.836  1.00 97.04  ? 15  GLN   D CG  1 
ATOM   5817  C  CD  . GLN   D  4  23  ? 19.097  -83.463  29.662  1.00 96.85  ? 15  GLN   D CD  1 
ATOM   5818  O  OE1 . GLN   D  4  23  ? 19.436  -82.283  29.639  1.00 97.84  ? 15  GLN   D OE1 1 
ATOM   5819  N  NE2 . GLN   D  4  23  ? 19.350  -84.295  28.666  1.00 97.86  ? 15  GLN   D NE2 1 
ATOM   5820  N  N   . VAL   D  4  24  ? 13.719  -84.297  29.964  1.00 100.01 ? 16  VAL   D N   1 
ATOM   5821  C  CA  . VAL   D  4  24  ? 12.458  -84.710  29.275  1.00 101.89 ? 16  VAL   D CA  1 
ATOM   5822  C  C   . VAL   D  4  24  ? 11.781  -83.458  28.700  1.00 104.71 ? 16  VAL   D C   1 
ATOM   5823  O  O   . VAL   D  4  24  ? 11.313  -83.517  27.545  1.00 105.62 ? 16  VAL   D O   1 
ATOM   5824  C  CB  . VAL   D  4  24  ? 11.508  -85.480  30.213  1.00 102.49 ? 16  VAL   D CB  1 
ATOM   5825  C  CG1 . VAL   D  4  24  ? 10.161  -85.754  29.555  1.00 102.92 ? 16  VAL   D CG1 1 
ATOM   5826  C  CG2 . VAL   D  4  24  ? 12.130  -86.778  30.701  1.00 102.02 ? 16  VAL   D CG2 1 
ATOM   5827  N  N   . GLU   D  4  25  ? 11.723  -82.375  29.480  1.00 104.61 ? 17  GLU   D N   1 
ATOM   5828  C  CA  . GLU   D  4  25  ? 11.090  -81.091  29.076  1.00 106.18 ? 17  GLU   D CA  1 
ATOM   5829  C  C   . GLU   D  4  25  ? 11.870  -80.470  27.912  1.00 102.95 ? 17  GLU   D C   1 
ATOM   5830  O  O   . GLU   D  4  25  ? 11.221  -79.907  27.007  1.00 101.30 ? 17  GLU   D O   1 
ATOM   5831  C  CB  . GLU   D  4  25  ? 11.020  -80.130  30.262  1.00 110.91 ? 17  GLU   D CB  1 
ATOM   5832  C  CG  . GLU   D  4  25  ? 10.025  -80.561  31.324  1.00 117.63 ? 17  GLU   D CG  1 
ATOM   5833  C  CD  . GLU   D  4  25  ? 8.586   -80.644  30.843  1.00 121.56 ? 17  GLU   D CD  1 
ATOM   5834  O  OE1 . GLU   D  4  25  ? 8.055   -81.770  30.756  1.00 125.29 ? 17  GLU   D OE1 1 
ATOM   5835  O  OE2 . GLU   D  4  25  ? 7.996   -79.580  30.559  1.00 131.78 ? 17  GLU   D OE2 1 
ATOM   5836  N  N   . TYR   D  4  26  ? 13.202  -80.559  27.936  1.00 98.05  ? 18  TYR   D N   1 
ATOM   5837  C  CA  . TYR   D  4  26  ? 14.089  -79.981  26.893  1.00 99.23  ? 18  TYR   D CA  1 
ATOM   5838  C  C   . TYR   D  4  26  ? 13.969  -80.791  25.596  1.00 99.52  ? 18  TYR   D C   1 
ATOM   5839  O  O   . TYR   D  4  26  ? 14.018  -80.177  24.516  1.00 102.20 ? 18  TYR   D O   1 
ATOM   5840  C  CB  . TYR   D  4  26  ? 15.542  -79.903  27.370  1.00 98.73  ? 18  TYR   D CB  1 
ATOM   5841  C  CG  . TYR   D  4  26  ? 15.805  -79.025  28.570  1.00 100.78 ? 18  TYR   D CG  1 
ATOM   5842  C  CD1 . TYR   D  4  26  ? 14.877  -78.098  29.024  1.00 102.67 ? 18  TYR   D CD1 1 
ATOM   5843  C  CD2 . TYR   D  4  26  ? 17.014  -79.103  29.241  1.00 101.09 ? 18  TYR   D CD2 1 
ATOM   5844  C  CE1 . TYR   D  4  26  ? 15.135  -77.293  30.123  1.00 105.05 ? 18  TYR   D CE1 1 
ATOM   5845  C  CE2 . TYR   D  4  26  ? 17.290  -78.304  30.339  1.00 102.64 ? 18  TYR   D CE2 1 
ATOM   5846  C  CZ  . TYR   D  4  26  ? 16.348  -77.394  30.782  1.00 103.96 ? 18  TYR   D CZ  1 
ATOM   5847  O  OH  . TYR   D  4  26  ? 16.617  -76.603  31.861  1.00 106.58 ? 18  TYR   D OH  1 
ATOM   5848  N  N   . SER   D  4  27  ? 13.811  -82.116  25.684  1.00 98.82  ? 19  SER   D N   1 
ATOM   5849  C  CA  . SER   D  4  27  ? 13.648  -83.013  24.506  1.00 98.90  ? 19  SER   D CA  1 
ATOM   5850  C  C   . SER   D  4  27  ? 12.316  -82.718  23.800  1.00 97.85  ? 19  SER   D C   1 
ATOM   5851  O  O   . SER   D  4  27  ? 12.250  -82.897  22.569  1.00 93.24  ? 19  SER   D O   1 
ATOM   5852  C  CB  . SER   D  4  27  ? 13.765  -84.469  24.884  1.00 98.08  ? 19  SER   D CB  1 
ATOM   5853  O  OG  . SER   D  4  27  ? 12.689  -84.870  25.717  1.00 100.80 ? 19  SER   D OG  1 
ATOM   5854  N  N   . LEU   D  4  28  ? 11.299  -82.280  24.552  1.00 99.37  ? 20  LEU   D N   1 
ATOM   5855  C  CA  . LEU   D  4  28  ? 9.978   -81.847  24.014  1.00 101.73 ? 20  LEU   D CA  1 
ATOM   5856  C  C   . LEU   D  4  28  ? 10.153  -80.601  23.131  1.00 105.56 ? 20  LEU   D C   1 
ATOM   5857  O  O   . LEU   D  4  28  ? 9.358   -80.449  22.182  1.00 104.81 ? 20  LEU   D O   1 
ATOM   5858  C  CB  . LEU   D  4  28  ? 9.015   -81.569  25.175  1.00 103.09 ? 20  LEU   D CB  1 
ATOM   5859  C  CG  . LEU   D  4  28  ? 8.081   -82.707  25.594  1.00 103.01 ? 20  LEU   D CG  1 
ATOM   5860  C  CD1 . LEU   D  4  28  ? 8.686   -84.081  25.343  1.00 104.84 ? 20  LEU   D CD1 1 
ATOM   5861  C  CD2 . LEU   D  4  28  ? 7.694   -82.567  27.058  1.00 102.59 ? 20  LEU   D CD2 1 
ATOM   5862  N  N   . GLU   D  4  29  ? 11.142  -79.747  23.429  1.00 107.02 ? 21  GLU   D N   1 
ATOM   5863  C  CA  . GLU   D  4  29  ? 11.474  -78.541  22.620  1.00 109.78 ? 21  GLU   D CA  1 
ATOM   5864  C  C   . GLU   D  4  29  ? 12.109  -78.973  21.293  1.00 109.46 ? 21  GLU   D C   1 
ATOM   5865  O  O   . GLU   D  4  29  ? 11.787  -78.352  20.262  1.00 114.08 ? 21  GLU   D O   1 
ATOM   5866  C  CB  . GLU   D  4  29  ? 12.410  -77.590  23.371  1.00 108.87 ? 21  GLU   D CB  1 
ATOM   5867  C  CG  . GLU   D  4  29  ? 11.760  -76.890  24.552  1.00 112.77 ? 21  GLU   D CG  1 
ATOM   5868  C  CD  . GLU   D  4  29  ? 10.528  -76.066  24.216  1.00 115.53 ? 21  GLU   D CD  1 
ATOM   5869  O  OE1 . GLU   D  4  29  ? 9.648   -75.944  25.089  1.00 122.31 ? 21  GLU   D OE1 1 
ATOM   5870  O  OE2 . GLU   D  4  29  ? 10.452  -75.543  23.085  1.00 118.54 ? 21  GLU   D OE2 1 
ATOM   5871  N  N   . ALA   D  4  30  ? 12.979  -79.988  21.321  1.00 108.90 ? 22  ALA   D N   1 
ATOM   5872  C  CA  . ALA   D  4  30  ? 13.629  -80.578  20.126  1.00 108.60 ? 22  ALA   D CA  1 
ATOM   5873  C  C   . ALA   D  4  30  ? 12.560  -81.085  19.149  1.00 108.01 ? 22  ALA   D C   1 
ATOM   5874  O  O   . ALA   D  4  30  ? 12.745  -80.907  17.928  1.00 100.95 ? 22  ALA   D O   1 
ATOM   5875  C  CB  . ALA   D  4  30  ? 14.567  -81.690  20.533  1.00 108.92 ? 22  ALA   D CB  1 
ATOM   5876  N  N   . ILE   D  4  31  ? 11.485  -81.685  19.675  1.00 108.91 ? 23  ILE   D N   1 
ATOM   5877  C  CA  . ILE   D  4  31  ? 10.381  -82.305  18.879  1.00 109.13 ? 23  ILE   D CA  1 
ATOM   5878  C  C   . ILE   D  4  31  ? 9.561   -81.204  18.195  1.00 110.12 ? 23  ILE   D C   1 
ATOM   5879  O  O   . ILE   D  4  31  ? 9.102   -81.441  17.058  1.00 113.21 ? 23  ILE   D O   1 
ATOM   5880  C  CB  . ILE   D  4  31  ? 9.505   -83.223  19.759  1.00 110.49 ? 23  ILE   D CB  1 
ATOM   5881  C  CG1 . ILE   D  4  31  ? 10.310  -84.416  20.281  1.00 107.88 ? 23  ILE   D CG1 1 
ATOM   5882  C  CG2 . ILE   D  4  31  ? 8.261   -83.677  19.005  1.00 109.36 ? 23  ILE   D CG2 1 
ATOM   5883  C  CD1 . ILE   D  4  31  ? 9.674   -85.136  21.444  1.00 107.73 ? 23  ILE   D CD1 1 
ATOM   5884  N  N   . LYS   D  4  32  ? 9.387   -80.053  18.853  1.00 109.49 ? 24  LYS   D N   1 
ATOM   5885  C  CA  . LYS   D  4  32  ? 8.665   -78.881  18.288  1.00 107.99 ? 24  LYS   D CA  1 
ATOM   5886  C  C   . LYS   D  4  32  ? 9.404   -78.372  17.042  1.00 103.28 ? 24  LYS   D C   1 
ATOM   5887  O  O   . LYS   D  4  32  ? 8.724   -77.843  16.156  1.00 104.58 ? 24  LYS   D O   1 
ATOM   5888  C  CB  . LYS   D  4  32  ? 8.509   -77.775  19.336  1.00 111.56 ? 24  LYS   D CB  1 
ATOM   5889  C  CG  . LYS   D  4  32  ? 7.486   -78.059  20.428  1.00 115.56 ? 24  LYS   D CG  1 
ATOM   5890  C  CD  . LYS   D  4  32  ? 7.318   -76.915  21.408  1.00 118.71 ? 24  LYS   D CD  1 
ATOM   5891  C  CE  . LYS   D  4  32  ? 6.645   -77.329  22.700  1.00 117.94 ? 24  LYS   D CE  1 
ATOM   5892  N  NZ  . LYS   D  4  32  ? 6.638   -76.226  23.689  1.00 121.12 ? 24  LYS   D NZ  1 
ATOM   5893  N  N   . LEU   D  4  33  ? 10.731  -78.532  16.971  1.00 104.28 ? 25  LEU   D N   1 
ATOM   5894  C  CA  . LEU   D  4  33  ? 11.556  -78.120  15.798  1.00 107.67 ? 25  LEU   D CA  1 
ATOM   5895  C  C   . LEU   D  4  33  ? 11.392  -79.133  14.653  1.00 107.37 ? 25  LEU   D C   1 
ATOM   5896  O  O   . LEU   D  4  33  ? 11.672  -78.759  13.498  1.00 106.03 ? 25  LEU   D O   1 
ATOM   5897  C  CB  . LEU   D  4  33  ? 13.028  -77.992  16.212  1.00 107.56 ? 25  LEU   D CB  1 
ATOM   5898  C  CG  . LEU   D  4  33  ? 13.352  -76.869  17.198  1.00 110.14 ? 25  LEU   D CG  1 
ATOM   5899  C  CD1 . LEU   D  4  33  ? 14.765  -77.019  17.745  1.00 108.55 ? 25  LEU   D CD1 1 
ATOM   5900  C  CD2 . LEU   D  4  33  ? 13.179  -75.501  16.551  1.00 110.44 ? 25  LEU   D CD2 1 
ATOM   5901  N  N   . GLY   D  4  34  ? 10.953  -80.360  14.955  1.00 108.42 ? 26  GLY   D N   1 
ATOM   5902  C  CA  . GLY   D  4  34  ? 10.776  -81.449  13.973  1.00 105.56 ? 26  GLY   D CA  1 
ATOM   5903  C  C   . GLY   D  4  34  ? 9.737   -81.114  12.913  1.00 105.11 ? 26  GLY   D C   1 
ATOM   5904  O  O   . GLY   D  4  34  ? 8.974   -80.145  13.115  1.00 100.27 ? 26  GLY   D O   1 
ATOM   5905  N  N   . SER   D  4  35  ? 9.707   -81.892  11.825  1.00 102.82 ? 27  SER   D N   1 
ATOM   5906  C  CA  . SER   D  4  35  ? 8.746   -81.758  10.697  1.00 100.01 ? 27  SER   D CA  1 
ATOM   5907  C  C   . SER   D  4  35  ? 7.388   -82.324  11.122  1.00 99.75  ? 27  SER   D C   1 
ATOM   5908  O  O   . SER   D  4  35  ? 7.371   -83.246  11.959  1.00 99.86  ? 27  SER   D O   1 
ATOM   5909  C  CB  . SER   D  4  35  ? 9.265   -82.429  9.449   1.00 102.05 ? 27  SER   D CB  1 
ATOM   5910  O  OG  . SER   D  4  35  ? 9.399   -83.831  9.638   1.00 102.26 ? 27  SER   D OG  1 
ATOM   5911  N  N   . THR   D  4  36  ? 6.293   -81.788  10.575  1.00 96.55  ? 28  THR   D N   1 
ATOM   5912  C  CA  . THR   D  4  36  ? 4.908   -82.141  10.983  1.00 100.87 ? 28  THR   D CA  1 
ATOM   5913  C  C   . THR   D  4  36  ? 4.607   -83.592  10.589  1.00 101.03 ? 28  THR   D C   1 
ATOM   5914  O  O   . THR   D  4  36  ? 4.984   -84.003  9.472   1.00 107.05 ? 28  THR   D O   1 
ATOM   5915  C  CB  . THR   D  4  36  ? 3.864   -81.185  10.395  1.00 101.16 ? 28  THR   D CB  1 
ATOM   5916  O  OG1 . THR   D  4  36  ? 4.253   -79.850  10.718  1.00 101.60 ? 28  THR   D OG1 1 
ATOM   5917  C  CG2 . THR   D  4  36  ? 2.472   -81.451  10.927  1.00 101.07 ? 28  THR   D CG2 1 
ATOM   5918  N  N   . ALA   D  4  37  ? 3.959   -84.330  11.493  1.00 99.01  ? 29  ALA   D N   1 
ATOM   5919  C  CA  . ALA   D  4  37  ? 3.390   -85.675  11.258  1.00 98.98  ? 29  ALA   D CA  1 
ATOM   5920  C  C   . ALA   D  4  37  ? 1.960   -85.696  11.805  1.00 100.36 ? 29  ALA   D C   1 
ATOM   5921  O  O   . ALA   D  4  37  ? 1.769   -85.283  12.963  1.00 98.48  ? 29  ALA   D O   1 
ATOM   5922  C  CB  . ALA   D  4  37  ? 4.255   -86.720  11.911  1.00 98.03  ? 29  ALA   D CB  1 
ATOM   5923  N  N   . ILE   D  4  38  ? 0.999   -86.139  10.990  1.00 103.82 ? 30  ILE   D N   1 
ATOM   5924  C  CA  . ILE   D  4  38  ? -0.452  -86.185  11.341  1.00 106.45 ? 30  ILE   D CA  1 
ATOM   5925  C  C   . ILE   D  4  38  ? -0.951  -87.627  11.200  1.00 104.95 ? 30  ILE   D C   1 
ATOM   5926  O  O   . ILE   D  4  38  ? -0.566  -88.298  10.220  1.00 102.27 ? 30  ILE   D O   1 
ATOM   5927  C  CB  . ILE   D  4  38  ? -1.257  -85.196  10.473  1.00 108.02 ? 30  ILE   D CB  1 
ATOM   5928  C  CG1 . ILE   D  4  38  ? -0.824  -83.751  10.738  1.00 110.58 ? 30  ILE   D CG1 1 
ATOM   5929  C  CG2 . ILE   D  4  38  ? -2.754  -85.380  10.681  1.00 109.51 ? 30  ILE   D CG2 1 
ATOM   5930  C  CD1 . ILE   D  4  38  ? -1.354  -82.747  9.741   1.00 112.76 ? 30  ILE   D CD1 1 
ATOM   5931  N  N   . GLY   D  4  39  ? -1.768  -88.070  12.160  1.00 105.56 ? 31  GLY   D N   1 
ATOM   5932  C  CA  . GLY   D  4  39  ? -2.482  -89.360  12.138  1.00 105.95 ? 31  GLY   D CA  1 
ATOM   5933  C  C   . GLY   D  4  39  ? -3.958  -89.168  12.439  1.00 107.48 ? 31  GLY   D C   1 
ATOM   5934  O  O   . GLY   D  4  39  ? -4.267  -88.415  13.382  1.00 107.66 ? 31  GLY   D O   1 
ATOM   5935  N  N   . ILE   D  4  40  ? -4.837  -89.797  11.651  1.00 108.88 ? 32  ILE   D N   1 
ATOM   5936  C  CA  . ILE   D  4  40  ? -6.315  -89.811  11.869  1.00 114.00 ? 32  ILE   D CA  1 
ATOM   5937  C  C   . ILE   D  4  40  ? -6.786  -91.270  11.885  1.00 112.93 ? 32  ILE   D C   1 
ATOM   5938  O  O   . ILE   D  4  40  ? -6.402  -92.024  10.969  1.00 114.87 ? 32  ILE   D O   1 
ATOM   5939  C  CB  . ILE   D  4  40  ? -7.052  -88.982  10.796  1.00 114.94 ? 32  ILE   D CB  1 
ATOM   5940  C  CG1 . ILE   D  4  40  ? -6.593  -87.521  10.795  1.00 115.90 ? 32  ILE   D CG1 1 
ATOM   5941  C  CG2 . ILE   D  4  40  ? -8.562  -89.098  10.970  1.00 118.41 ? 32  ILE   D CG2 1 
ATOM   5942  C  CD1 . ILE   D  4  40  ? -7.165  -86.690  9.668   1.00 116.50 ? 32  ILE   D CD1 1 
ATOM   5943  N  N   . ALA   D  4  41  ? -7.591  -91.635  12.888  1.00 115.50 ? 33  ALA   D N   1 
ATOM   5944  C  CA  . ALA   D  4  41  ? -8.180  -92.982  13.073  1.00 115.16 ? 33  ALA   D CA  1 
ATOM   5945  C  C   . ALA   D  4  41  ? -9.638  -92.968  12.603  1.00 116.91 ? 33  ALA   D C   1 
ATOM   5946  O  O   . ALA   D  4  41  ? -10.380 -92.073  13.039  1.00 120.88 ? 33  ALA   D O   1 
ATOM   5947  C  CB  . ALA   D  4  41  ? -8.084  -93.389  14.522  1.00 115.25 ? 33  ALA   D CB  1 
ATOM   5948  N  N   . THR   D  4  42  ? -10.022 -93.920  11.747  1.00 116.30 ? 34  THR   D N   1 
ATOM   5949  C  CA  . THR   D  4  42  ? -11.425 -94.163  11.312  1.00 113.81 ? 34  THR   D CA  1 
ATOM   5950  C  C   . THR   D  4  42  ? -11.798 -95.616  11.619  1.00 114.27 ? 34  THR   D C   1 
ATOM   5951  O  O   . THR   D  4  42  ? -10.920 -96.363  12.090  1.00 110.58 ? 34  THR   D O   1 
ATOM   5952  C  CB  . THR   D  4  42  ? -11.631 -93.860  9.821   1.00 114.98 ? 34  THR   D CB  1 
ATOM   5953  O  OG1 . THR   D  4  42  ? -10.982 -94.873  9.052   1.00 113.88 ? 34  THR   D OG1 1 
ATOM   5954  C  CG2 . THR   D  4  42  ? -11.116 -92.497  9.415   1.00 113.91 ? 34  THR   D CG2 1 
ATOM   5955  N  N   . LYS   D  4  43  ? -13.051 -95.990  11.353  1.00 113.09 ? 35  LYS   D N   1 
ATOM   5956  C  CA  . LYS   D  4  43  ? -13.552 -97.382  11.486  1.00 115.76 ? 35  LYS   D CA  1 
ATOM   5957  C  C   . LYS   D  4  43  ? -13.183 -98.185  10.230  1.00 117.92 ? 35  LYS   D C   1 
ATOM   5958  O  O   . LYS   D  4  43  ? -13.305 -99.425  10.278  1.00 122.19 ? 35  LYS   D O   1 
ATOM   5959  C  CB  . LYS   D  4  43  ? -15.060 -97.379  11.757  1.00 117.86 ? 35  LYS   D CB  1 
ATOM   5960  C  CG  . LYS   D  4  43  ? -15.448 -96.954  13.167  1.00 122.93 ? 35  LYS   D CG  1 
ATOM   5961  C  CD  . LYS   D  4  43  ? -16.849 -97.367  13.569  1.00 128.72 ? 35  LYS   D CD  1 
ATOM   5962  C  CE  . LYS   D  4  43  ? -17.067 -97.340  15.068  1.00 132.91 ? 35  LYS   D CE  1 
ATOM   5963  N  NZ  . LYS   D  4  43  ? -17.059 -95.957  15.599  1.00 134.10 ? 35  LYS   D NZ  1 
ATOM   5964  N  N   . GLU   D  4  44  ? -12.739 -97.512  9.161   1.00 115.07 ? 36  GLU   D N   1 
ATOM   5965  C  CA  . GLU   D  4  44  ? -12.289 -98.148  7.892   1.00 114.17 ? 36  GLU   D CA  1 
ATOM   5966  C  C   . GLU   D  4  44  ? -10.760 -98.266  7.859   1.00 110.43 ? 36  GLU   D C   1 
ATOM   5967  O  O   . GLU   D  4  44  ? -10.255 -98.936  6.939   1.00 112.25 ? 36  GLU   D O   1 
ATOM   5968  C  CB  . GLU   D  4  44  ? -12.763 -97.346  6.679   1.00 114.76 ? 36  GLU   D CB  1 
ATOM   5969  C  CG  . GLU   D  4  44  ? -14.257 -97.436  6.434   1.00 117.93 ? 36  GLU   D CG  1 
ATOM   5970  C  CD  . GLU   D  4  44  ? -14.751 -96.613  5.257   1.00 117.59 ? 36  GLU   D CD  1 
ATOM   5971  O  OE1 . GLU   D  4  44  ? -13.906 -96.094  4.501   1.00 119.35 ? 36  GLU   D OE1 1 
ATOM   5972  O  OE2 . GLU   D  4  44  ? -15.979 -96.489  5.101   1.00 122.23 ? 36  GLU   D OE2 1 
ATOM   5973  N  N   . GLY   D  4  45  ? -10.053 -97.632  8.801   1.00 109.00 ? 37  GLY   D N   1 
ATOM   5974  C  CA  . GLY   D  4  45  ? -8.580  -97.695  8.892   1.00 109.56 ? 37  GLY   D CA  1 
ATOM   5975  C  C   . GLY   D  4  45  ? -7.987  -96.465  9.554   1.00 108.96 ? 37  GLY   D C   1 
ATOM   5976  O  O   . GLY   D  4  45  ? -8.744  -95.517  9.833   1.00 112.30 ? 37  GLY   D O   1 
ATOM   5977  N  N   . VAL   D  4  46  ? -6.676  -96.488  9.807   1.00 109.08 ? 38  VAL   D N   1 
ATOM   5978  C  CA  . VAL   D  4  46  ? -5.893  -95.333  10.337  1.00 109.67 ? 38  VAL   D CA  1 
ATOM   5979  C  C   . VAL   D  4  46  ? -5.014  -94.810  9.198   1.00 107.29 ? 38  VAL   D C   1 
ATOM   5980  O  O   . VAL   D  4  46  ? -4.447  -95.645  8.468   1.00 104.25 ? 38  VAL   D O   1 
ATOM   5981  C  CB  . VAL   D  4  46  ? -5.046  -95.716  11.567  1.00 111.67 ? 38  VAL   D CB  1 
ATOM   5982  C  CG1 . VAL   D  4  46  ? -4.487  -94.483  12.263  1.00 111.64 ? 38  VAL   D CG1 1 
ATOM   5983  C  CG2 . VAL   D  4  46  ? -5.820  -96.576  12.556  1.00 114.03 ? 38  VAL   D CG2 1 
ATOM   5984  N  N   . VAL   D  4  47  ? -4.922  -93.484  9.054   1.00 106.94 ? 39  VAL   D N   1 
ATOM   5985  C  CA  . VAL   D  4  47  ? -4.062  -92.795  8.045   1.00 104.05 ? 39  VAL   D CA  1 
ATOM   5986  C  C   . VAL   D  4  47  ? -2.922  -92.078  8.775   1.00 101.50 ? 39  VAL   D C   1 
ATOM   5987  O  O   . VAL   D  4  47  ? -3.204  -91.369  9.758   1.00 100.25 ? 39  VAL   D O   1 
ATOM   5988  C  CB  . VAL   D  4  47  ? -4.867  -91.805  7.183   1.00 103.40 ? 39  VAL   D CB  1 
ATOM   5989  C  CG1 . VAL   D  4  47  ? -3.973  -91.061  6.202   1.00 101.23 ? 39  VAL   D CG1 1 
ATOM   5990  C  CG2 . VAL   D  4  47  ? -6.004  -92.498  6.450   1.00 106.09 ? 39  VAL   D CG2 1 
ATOM   5991  N  N   . LEU   D  4  48  ? -1.692  -92.256  8.283   1.00 99.48  ? 40  LEU   D N   1 
ATOM   5992  C  CA  . LEU   D  4  48  ? -0.458  -91.587  8.770   1.00 96.69  ? 40  LEU   D CA  1 
ATOM   5993  C  C   . LEU   D  4  48  ? 0.144   -90.782  7.614   1.00 96.49  ? 40  LEU   D C   1 
ATOM   5994  O  O   . LEU   D  4  48  ? 0.438   -91.391  6.565   1.00 93.17  ? 40  LEU   D O   1 
ATOM   5995  C  CB  . LEU   D  4  48  ? 0.524   -92.649  9.281   1.00 98.12  ? 40  LEU   D CB  1 
ATOM   5996  C  CG  . LEU   D  4  48  ? 0.730   -92.729  10.795  1.00 98.88  ? 40  LEU   D CG  1 
ATOM   5997  C  CD1 . LEU   D  4  48  ? -0.587  -92.692  11.558  1.00 101.14 ? 40  LEU   D CD1 1 
ATOM   5998  C  CD2 . LEU   D  4  48  ? 1.506   -93.986  11.156  1.00 98.97  ? 40  LEU   D CD2 1 
ATOM   5999  N  N   . GLY   D  4  49  ? 0.293   -89.466  7.804   1.00 96.76  ? 41  GLY   D N   1 
ATOM   6000  C  CA  . GLY   D  4  49  ? 0.910   -88.539  6.834   1.00 95.51  ? 41  GLY   D CA  1 
ATOM   6001  C  C   . GLY   D  4  49  ? 2.002   -87.717  7.488   1.00 94.12  ? 41  GLY   D C   1 
ATOM   6002  O  O   . GLY   D  4  49  ? 1.843   -87.384  8.675   1.00 92.43  ? 41  GLY   D O   1 
ATOM   6003  N  N   . VAL   D  4  50  ? 3.078   -87.419  6.751   1.00 96.09  ? 42  VAL   D N   1 
ATOM   6004  C  CA  . VAL   D  4  50  ? 4.244   -86.629  7.251   1.00 99.22  ? 42  VAL   D CA  1 
ATOM   6005  C  C   . VAL   D  4  50  ? 4.669   -85.604  6.198   1.00 101.74 ? 42  VAL   D C   1 
ATOM   6006  O  O   . VAL   D  4  50  ? 4.501   -85.873  4.993   1.00 106.37 ? 42  VAL   D O   1 
ATOM   6007  C  CB  . VAL   D  4  50  ? 5.435   -87.529  7.634   1.00 99.24  ? 42  VAL   D CB  1 
ATOM   6008  C  CG1 . VAL   D  4  50  ? 5.080   -88.479  8.765   1.00 100.31 ? 42  VAL   D CG1 1 
ATOM   6009  C  CG2 . VAL   D  4  50  ? 5.993   -88.296  6.443   1.00 98.49  ? 42  VAL   D CG2 1 
ATOM   6010  N  N   . GLU   D  4  51  ? 5.207   -84.477  6.665   1.00 102.85 ? 43  GLU   D N   1 
ATOM   6011  C  CA  . GLU   D  4  51  ? 5.992   -83.506  5.862   1.00 105.20 ? 43  GLU   D CA  1 
ATOM   6012  C  C   . GLU   D  4  51  ? 7.422   -84.050  5.763   1.00 103.56 ? 43  GLU   D C   1 
ATOM   6013  O  O   . GLU   D  4  51  ? 8.008   -84.350  6.820   1.00 104.08 ? 43  GLU   D O   1 
ATOM   6014  C  CB  . GLU   D  4  51  ? 5.928   -82.126  6.526   1.00 108.18 ? 43  GLU   D CB  1 
ATOM   6015  C  CG  . GLU   D  4  51  ? 6.933   -81.118  5.989   1.00 110.67 ? 43  GLU   D CG  1 
ATOM   6016  C  CD  . GLU   D  4  51  ? 7.154   -79.899  6.871   1.00 111.03 ? 43  GLU   D CD  1 
ATOM   6017  O  OE1 . GLU   D  4  51  ? 7.858   -78.974  6.426   1.00 116.48 ? 43  GLU   D OE1 1 
ATOM   6018  O  OE2 . GLU   D  4  51  ? 6.625   -79.875  8.002   1.00 112.51 ? 43  GLU   D OE2 1 
ATOM   6019  N  N   . LYS   D  4  52  ? 7.950   -84.195  4.546   1.00 101.65 ? 44  LYS   D N   1 
ATOM   6020  C  CA  . LYS   D  4  52  ? 9.328   -84.700  4.303   1.00 103.06 ? 44  LYS   D CA  1 
ATOM   6021  C  C   . LYS   D  4  52  ? 10.339  -83.600  4.644   1.00 104.96 ? 44  LYS   D C   1 
ATOM   6022  O  O   . LYS   D  4  52  ? 11.293  -83.892  5.393   1.00 101.63 ? 44  LYS   D O   1 
ATOM   6023  C  CB  . LYS   D  4  52  ? 9.478   -85.182  2.859   1.00 104.89 ? 44  LYS   D CB  1 
ATOM   6024  C  CG  . LYS   D  4  52  ? 8.751   -86.483  2.549   1.00 106.08 ? 44  LYS   D CG  1 
ATOM   6025  C  CD  . LYS   D  4  52  ? 9.269   -87.179  1.314   1.00 107.01 ? 44  LYS   D CD  1 
ATOM   6026  C  CE  . LYS   D  4  52  ? 8.520   -88.453  0.995   1.00 106.72 ? 44  LYS   D CE  1 
ATOM   6027  N  NZ  . LYS   D  4  52  ? 9.104   -89.134  -0.181  1.00 107.98 ? 44  LYS   D NZ  1 
ATOM   6028  N  N   . ARG   D  4  53  ? 10.130  -82.389  4.118   1.00 109.72 ? 45  ARG   D N   1 
ATOM   6029  C  CA  . ARG   D  4  53  ? 10.969  -81.186  4.382   1.00 112.19 ? 45  ARG   D CA  1 
ATOM   6030  C  C   . ARG   D  4  53  ? 12.434  -81.490  4.033   1.00 111.96 ? 45  ARG   D C   1 
ATOM   6031  O  O   . ARG   D  4  53  ? 13.241  -81.697  4.960   1.00 109.77 ? 45  ARG   D O   1 
ATOM   6032  C  CB  . ARG   D  4  53  ? 10.819  -80.743  5.843   1.00 111.58 ? 45  ARG   D CB  1 
ATOM   6033  C  CG  . ARG   D  4  53  ? 11.491  -79.416  6.166   1.00 112.33 ? 45  ARG   D CG  1 
ATOM   6034  C  CD  . ARG   D  4  53  ? 11.728  -79.226  7.653   1.00 111.92 ? 45  ARG   D CD  1 
ATOM   6035  N  NE  . ARG   D  4  53  ? 10.533  -78.783  8.360   1.00 111.24 ? 45  ARG   D NE  1 
ATOM   6036  C  CZ  . ARG   D  4  53  ? 10.409  -78.719  9.685   1.00 111.10 ? 45  ARG   D CZ  1 
ATOM   6037  N  NH1 . ARG   D  4  53  ? 11.406  -79.088  10.475  1.00 113.80 ? 45  ARG   D NH1 1 
ATOM   6038  N  NH2 . ARG   D  4  53  ? 9.276   -78.293  10.218  1.00 107.65 ? 45  ARG   D NH2 1 
ATOM   6039  N  N   . ALA   D  4  54  ? 12.760  -81.510  2.737   1.00 115.28 ? 46  ALA   D N   1 
ATOM   6040  C  CA  . ALA   D  4  54  ? 14.140  -81.632  2.212   1.00 118.39 ? 46  ALA   D CA  1 
ATOM   6041  C  C   . ALA   D  4  54  ? 14.873  -80.306  2.440   1.00 121.27 ? 46  ALA   D C   1 
ATOM   6042  O  O   . ALA   D  4  54  ? 14.340  -79.260  2.017   1.00 120.52 ? 46  ALA   D O   1 
ATOM   6043  C  CB  . ALA   D  4  54  ? 14.112  -81.995  0.748   1.00 122.18 ? 46  ALA   D CB  1 
ATOM   6044  N  N   . THR   D  4  55  ? 16.052  -80.355  3.068   1.00 121.69 ? 47  THR   D N   1 
ATOM   6045  C  CA  . THR   D  4  55  ? 16.873  -79.167  3.435   1.00 122.92 ? 47  THR   D CA  1 
ATOM   6046  C  C   . THR   D  4  55  ? 17.405  -78.474  2.172   1.00 121.52 ? 47  THR   D C   1 
ATOM   6047  O  O   . THR   D  4  55  ? 17.703  -77.267  2.254   1.00 117.58 ? 47  THR   D O   1 
ATOM   6048  C  CB  . THR   D  4  55  ? 18.018  -79.553  4.380   1.00 126.60 ? 47  THR   D CB  1 
ATOM   6049  O  OG1 . THR   D  4  55  ? 18.741  -80.632  3.786   1.00 130.13 ? 47  THR   D OG1 1 
ATOM   6050  C  CG2 . THR   D  4  55  ? 17.531  -79.955  5.755   1.00 127.45 ? 47  THR   D CG2 1 
ATOM   6051  N  N   . SER   D  4  56  ? 17.522  -79.202  1.056   1.00 119.04 ? 48  SER   D N   1 
ATOM   6052  C  CA  . SER   D  4  56  ? 18.057  -78.697  -0.236  1.00 118.35 ? 48  SER   D CA  1 
ATOM   6053  C  C   . SER   D  4  56  ? 17.348  -79.385  -1.402  1.00 113.66 ? 48  SER   D C   1 
ATOM   6054  O  O   . SER   D  4  56  ? 16.884  -80.513  -1.267  1.00 118.08 ? 48  SER   D O   1 
ATOM   6055  C  CB  . SER   D  4  56  ? 19.552  -78.894  -0.285  1.00 119.32 ? 48  SER   D CB  1 
ATOM   6056  O  OG  . SER   D  4  56  ? 20.064  -78.697  -1.596  1.00 122.49 ? 48  SER   D OG  1 
ATOM   6057  N  N   . PRO   D  4  57  ? 17.217  -78.722  -2.574  1.00 111.60 ? 49  PRO   D N   1 
ATOM   6058  C  CA  . PRO   D  4  57  ? 16.604  -79.342  -3.752  1.00 109.38 ? 49  PRO   D CA  1 
ATOM   6059  C  C   . PRO   D  4  57  ? 17.382  -80.501  -4.401  1.00 104.22 ? 49  PRO   D C   1 
ATOM   6060  O  O   . PRO   D  4  57  ? 16.770  -81.238  -5.146  1.00 103.49 ? 49  PRO   D O   1 
ATOM   6061  C  CB  . PRO   D  4  57  ? 16.508  -78.187  -4.763  1.00 111.10 ? 49  PRO   D CB  1 
ATOM   6062  C  CG  . PRO   D  4  57  ? 17.574  -77.209  -4.317  1.00 113.41 ? 49  PRO   D CG  1 
ATOM   6063  C  CD  . PRO   D  4  57  ? 17.589  -77.319  -2.808  1.00 112.85 ? 49  PRO   D CD  1 
ATOM   6064  N  N   . LEU   D  4  58  ? 18.688  -80.628  -4.135  1.00 103.03 ? 50  LEU   D N   1 
ATOM   6065  C  CA  . LEU   D  4  58  ? 19.551  -81.706  -4.701  1.00 104.88 ? 50  LEU   D CA  1 
ATOM   6066  C  C   . LEU   D  4  58  ? 19.315  -83.036  -3.964  1.00 104.47 ? 50  LEU   D C   1 
ATOM   6067  O  O   . LEU   D  4  58  ? 19.606  -84.093  -4.562  1.00 100.98 ? 50  LEU   D O   1 
ATOM   6068  C  CB  . LEU   D  4  58  ? 21.023  -81.285  -4.618  1.00 104.38 ? 50  LEU   D CB  1 
ATOM   6069  C  CG  . LEU   D  4  58  ? 21.516  -80.371  -5.739  1.00 104.71 ? 50  LEU   D CG  1 
ATOM   6070  C  CD1 . LEU   D  4  58  ? 22.897  -79.819  -5.422  1.00 106.37 ? 50  LEU   D CD1 1 
ATOM   6071  C  CD2 . LEU   D  4  58  ? 21.536  -81.102  -7.073  1.00 104.47 ? 50  LEU   D CD2 1 
ATOM   6072  N  N   . LEU   D  4  59  ? 18.824  -82.988  -2.720  1.00 106.13 ? 51  LEU   D N   1 
ATOM   6073  C  CA  . LEU   D  4  59  ? 18.532  -84.181  -1.872  1.00 104.35 ? 51  LEU   D CA  1 
ATOM   6074  C  C   . LEU   D  4  59  ? 17.324  -84.930  -2.453  1.00 105.11 ? 51  LEU   D C   1 
ATOM   6075  O  O   . LEU   D  4  59  ? 16.252  -84.312  -2.583  1.00 104.87 ? 51  LEU   D O   1 
ATOM   6076  C  CB  . LEU   D  4  59  ? 18.315  -83.718  -0.422  1.00 104.91 ? 51  LEU   D CB  1 
ATOM   6077  C  CG  . LEU   D  4  59  ? 17.334  -84.501  0.453   1.00 105.10 ? 51  LEU   D CG  1 
ATOM   6078  C  CD1 . LEU   D  4  59  ? 17.652  -85.988  0.493   1.00 104.32 ? 51  LEU   D CD1 1 
ATOM   6079  C  CD2 . LEU   D  4  59  ? 17.343  -83.938  1.866   1.00 105.80 ? 51  LEU   D CD2 1 
ATOM   6080  N  N   . GLU   D  4  60  ? 17.513  -86.214  -2.781  1.00 105.13 ? 52  GLU   D N   1 
ATOM   6081  C  CA  . GLU   D  4  60  ? 16.489  -87.117  -3.379  1.00 105.79 ? 52  GLU   D CA  1 
ATOM   6082  C  C   . GLU   D  4  60  ? 15.442  -87.460  -2.312  1.00 107.05 ? 52  GLU   D C   1 
ATOM   6083  O  O   . GLU   D  4  60  ? 15.739  -88.295  -1.432  1.00 104.22 ? 52  GLU   D O   1 
ATOM   6084  C  CB  . GLU   D  4  60  ? 17.151  -88.377  -3.938  1.00 107.50 ? 52  GLU   D CB  1 
ATOM   6085  C  CG  . GLU   D  4  60  ? 18.233  -88.086  -4.963  1.00 109.11 ? 52  GLU   D CG  1 
ATOM   6086  C  CD  . GLU   D  4  60  ? 18.824  -89.311  -5.634  1.00 111.58 ? 52  GLU   D CD  1 
ATOM   6087  O  OE1 . GLU   D  4  60  ? 19.569  -89.137  -6.617  1.00 112.01 ? 52  GLU   D OE1 1 
ATOM   6088  O  OE2 . GLU   D  4  60  ? 18.547  -90.434  -5.168  1.00 114.42 ? 52  GLU   D OE2 1 
ATOM   6089  N  N   . SER   D  4  61  ? 14.258  -86.849  -2.411  1.00 108.05 ? 53  SER   D N   1 
ATOM   6090  C  CA  . SER   D  4  61  ? 13.234  -86.768  -1.335  1.00 109.91 ? 53  SER   D CA  1 
ATOM   6091  C  C   . SER   D  4  61  ? 12.723  -88.160  -0.944  1.00 107.08 ? 53  SER   D C   1 
ATOM   6092  O  O   . SER   D  4  61  ? 12.361  -88.332  0.233   1.00 106.66 ? 53  SER   D O   1 
ATOM   6093  C  CB  . SER   D  4  61  ? 12.095  -85.867  -1.736  1.00 112.31 ? 53  SER   D CB  1 
ATOM   6094  O  OG  . SER   D  4  61  ? 11.357  -86.428  -2.812  1.00 118.45 ? 53  SER   D OG  1 
ATOM   6095  N  N   . ASP   D  4  62  ? 12.693  -89.110  -1.883  1.00 107.27 ? 54  ASP   D N   1 
ATOM   6096  C  CA  . ASP   D  4  62  ? 12.151  -90.479  -1.647  1.00 105.36 ? 54  ASP   D CA  1 
ATOM   6097  C  C   . ASP   D  4  62  ? 13.039  -91.237  -0.650  1.00 97.72  ? 54  ASP   D C   1 
ATOM   6098  O  O   . ASP   D  4  62  ? 12.533  -92.203  -0.065  1.00 93.29  ? 54  ASP   D O   1 
ATOM   6099  C  CB  . ASP   D  4  62  ? 11.942  -91.257  -2.951  1.00 112.88 ? 54  ASP   D CB  1 
ATOM   6100  C  CG  . ASP   D  4  62  ? 13.019  -91.048  -4.002  1.00 119.95 ? 54  ASP   D CG  1 
ATOM   6101  O  OD1 . ASP   D  4  62  ? 14.167  -90.748  -3.616  1.00 125.51 ? 54  ASP   D OD1 1 
ATOM   6102  O  OD2 . ASP   D  4  62  ? 12.694  -91.175  -5.199  1.00 126.62 ? 54  ASP   D OD2 1 
ATOM   6103  N  N   . SER   D  4  63  ? 14.290  -90.808  -0.445  1.00 95.83  ? 55  SER   D N   1 
ATOM   6104  C  CA  . SER   D  4  63  ? 15.229  -91.396  0.549   1.00 94.94  ? 55  SER   D CA  1 
ATOM   6105  C  C   . SER   D  4  63  ? 14.898  -90.912  1.968   1.00 93.94  ? 55  SER   D C   1 
ATOM   6106  O  O   . SER   D  4  63  ? 15.443  -91.496  2.921   1.00 96.98  ? 55  SER   D O   1 
ATOM   6107  C  CB  . SER   D  4  63  ? 16.665  -91.105  0.195   1.00 94.48  ? 55  SER   D CB  1 
ATOM   6108  O  OG  . SER   D  4  63  ? 17.000  -89.749  0.457   1.00 93.12  ? 55  SER   D OG  1 
ATOM   6109  N  N   . ILE   D  4  64  ? 14.050  -89.888  2.112   1.00 94.99  ? 56  ILE   D N   1 
ATOM   6110  C  CA  . ILE   D  4  64  ? 13.547  -89.417  3.438   1.00 95.21  ? 56  ILE   D CA  1 
ATOM   6111  C  C   . ILE   D  4  64  ? 12.470  -90.405  3.898   1.00 95.20  ? 56  ILE   D C   1 
ATOM   6112  O  O   . ILE   D  4  64  ? 11.416  -90.481  3.234   1.00 91.44  ? 56  ILE   D O   1 
ATOM   6113  C  CB  . ILE   D  4  64  ? 13.019  -87.967  3.387   1.00 95.98  ? 56  ILE   D CB  1 
ATOM   6114  C  CG1 . ILE   D  4  64  ? 14.052  -86.996  2.803   1.00 96.65  ? 56  ILE   D CG1 1 
ATOM   6115  C  CG2 . ILE   D  4  64  ? 12.557  -87.526  4.770   1.00 94.74  ? 56  ILE   D CG2 1 
ATOM   6116  C  CD1 . ILE   D  4  64  ? 13.502  -85.626  2.468   1.00 96.89  ? 56  ILE   D CD1 1 
ATOM   6117  N  N   . GLU   D  4  65  ? 12.738  -91.123  4.992   1.00 95.05  ? 57  GLU   D N   1 
ATOM   6118  C  CA  . GLU   D  4  65  ? 11.916  -92.257  5.492   1.00 98.25  ? 57  GLU   D CA  1 
ATOM   6119  C  C   . GLU   D  4  65  ? 11.417  -91.924  6.904   1.00 97.84  ? 57  GLU   D C   1 
ATOM   6120  O  O   . GLU   D  4  65  ? 12.093  -92.308  7.878   1.00 95.55  ? 57  GLU   D O   1 
ATOM   6121  C  CB  . GLU   D  4  65  ? 12.763  -93.532  5.459   1.00 101.87 ? 57  GLU   D CB  1 
ATOM   6122  C  CG  . GLU   D  4  65  ? 11.983  -94.800  5.752   1.00 106.10 ? 57  GLU   D CG  1 
ATOM   6123  C  CD  . GLU   D  4  65  ? 12.831  -96.049  5.935   1.00 108.89 ? 57  GLU   D CD  1 
ATOM   6124  O  OE1 . GLU   D  4  65  ? 12.265  -97.090  6.327   1.00 109.80 ? 57  GLU   D OE1 1 
ATOM   6125  O  OE2 . GLU   D  4  65  ? 14.053  -95.981  5.687   1.00 110.31 ? 57  GLU   D OE2 1 
ATOM   6126  N  N   . LYS   D  4  66  ? 10.285  -91.222  7.006   1.00 98.50  ? 58  LYS   D N   1 
ATOM   6127  C  CA  . LYS   D  4  66  ? 9.698   -90.766  8.297   1.00 101.40 ? 58  LYS   D CA  1 
ATOM   6128  C  C   . LYS   D  4  66  ? 8.391   -91.514  8.591   1.00 100.13 ? 58  LYS   D C   1 
ATOM   6129  O  O   . LYS   D  4  66  ? 7.827   -91.287  9.678   1.00 96.50  ? 58  LYS   D O   1 
ATOM   6130  C  CB  . LYS   D  4  66  ? 9.500   -89.247  8.275   1.00 104.39 ? 58  LYS   D CB  1 
ATOM   6131  C  CG  . LYS   D  4  66  ? 10.788  -88.444  8.414   1.00 107.00 ? 58  LYS   D CG  1 
ATOM   6132  C  CD  . LYS   D  4  66  ? 10.618  -86.946  8.272   1.00 107.29 ? 58  LYS   D CD  1 
ATOM   6133  C  CE  . LYS   D  4  66  ? 11.945  -86.219  8.251   1.00 108.00 ? 58  LYS   D CE  1 
ATOM   6134  N  NZ  . LYS   D  4  66  ? 11.777  -84.759  8.063   1.00 109.77 ? 58  LYS   D NZ  1 
ATOM   6135  N  N   . ILE   D  4  67  ? 7.927   -92.363  7.668   1.00 101.75 ? 59  ILE   D N   1 
ATOM   6136  C  CA  . ILE   D  4  67  ? 6.850   -93.369  7.918   1.00 101.56 ? 59  ILE   D CA  1 
ATOM   6137  C  C   . ILE   D  4  67  ? 7.469   -94.759  7.745   1.00 100.19 ? 59  ILE   D C   1 
ATOM   6138  O  O   . ILE   D  4  67  ? 8.183   -94.963  6.744   1.00 108.02 ? 59  ILE   D O   1 
ATOM   6139  C  CB  . ILE   D  4  67  ? 5.632   -93.163  6.995   1.00 104.01 ? 59  ILE   D CB  1 
ATOM   6140  C  CG1 . ILE   D  4  67  ? 5.132   -91.714  7.005   1.00 104.64 ? 59  ILE   D CG1 1 
ATOM   6141  C  CG2 . ILE   D  4  67  ? 4.530   -94.145  7.369   1.00 104.82 ? 59  ILE   D CG2 1 
ATOM   6142  C  CD1 . ILE   D  4  67  ? 4.008   -91.435  6.026   1.00 103.86 ? 59  ILE   D CD1 1 
ATOM   6143  N  N   . VAL   D  4  68  ? 7.190   -95.677  8.675   1.00 97.10  ? 60  VAL   D N   1 
ATOM   6144  C  CA  . VAL   D  4  68  ? 7.937   -96.960  8.827   1.00 96.32  ? 60  VAL   D CA  1 
ATOM   6145  C  C   . VAL   D  4  68  ? 6.984   -98.078  9.276   1.00 93.59  ? 60  VAL   D C   1 
ATOM   6146  O  O   . VAL   D  4  68  ? 6.091   -97.802  10.103  1.00 90.58  ? 60  VAL   D O   1 
ATOM   6147  C  CB  . VAL   D  4  68  ? 9.109   -96.764  9.809   1.00 94.24  ? 60  VAL   D CB  1 
ATOM   6148  C  CG1 . VAL   D  4  68  ? 9.424   -98.019  10.605  1.00 94.97  ? 60  VAL   D CG1 1 
ATOM   6149  C  CG2 . VAL   D  4  68  ? 10.352  -96.260  9.093   1.00 93.13  ? 60  VAL   D CG2 1 
ATOM   6150  N  N   . GLU   D  4  69  ? 7.196   -99.294  8.756   1.00 94.14  ? 61  GLU   D N   1 
ATOM   6151  C  CA  . GLU   D  4  69  ? 6.449   -100.528 9.127   1.00 94.94  ? 61  GLU   D CA  1 
ATOM   6152  C  C   . GLU   D  4  69  ? 7.106   -101.175 10.352  1.00 90.70  ? 61  GLU   D C   1 
ATOM   6153  O  O   . GLU   D  4  69  ? 8.339   -101.359 10.340  1.00 86.24  ? 61  GLU   D O   1 
ATOM   6154  C  CB  . GLU   D  4  69  ? 6.425   -101.520 7.961   1.00 98.57  ? 61  GLU   D CB  1 
ATOM   6155  C  CG  . GLU   D  4  69  ? 5.564   -102.748 8.222   1.00 102.48 ? 61  GLU   D CG  1 
ATOM   6156  C  CD  . GLU   D  4  69  ? 5.553   -103.798 7.117   1.00 105.88 ? 61  GLU   D CD  1 
ATOM   6157  O  OE1 . GLU   D  4  69  ? 5.217   -104.968 7.413   1.00 105.98 ? 61  GLU   D OE1 1 
ATOM   6158  O  OE2 . GLU   D  4  69  ? 5.870   -103.450 5.962   1.00 107.85 ? 61  GLU   D OE2 1 
ATOM   6159  N  N   . ILE   D  4  70  ? 6.301   -101.518 11.361  1.00 91.15  ? 62  ILE   D N   1 
ATOM   6160  C  CA  . ILE   D  4  70  ? 6.739   -102.258 12.582  1.00 97.38  ? 62  ILE   D CA  1 
ATOM   6161  C  C   . ILE   D  4  70  ? 6.376   -103.737 12.402  1.00 100.00 ? 62  ILE   D C   1 
ATOM   6162  O  O   . ILE   D  4  70  ? 7.252   -104.593 12.641  1.00 102.38 ? 62  ILE   D O   1 
ATOM   6163  C  CB  . ILE   D  4  70  ? 6.111   -101.636 13.845  1.00 98.67  ? 62  ILE   D CB  1 
ATOM   6164  C  CG1 . ILE   D  4  70  ? 6.600   -100.197 14.042  1.00 98.11  ? 62  ILE   D CG1 1 
ATOM   6165  C  CG2 . ILE   D  4  70  ? 6.366   -102.507 15.070  1.00 99.87  ? 62  ILE   D CG2 1 
ATOM   6166  C  CD1 . ILE   D  4  70  ? 6.099   -99.524  15.300  1.00 99.08  ? 62  ILE   D CD1 1 
ATOM   6167  N  N   . ASP   D  4  71  ? 5.128   -104.014 12.010  1.00 103.19 ? 63  ASP   D N   1 
ATOM   6168  C  CA  . ASP   D  4  71  ? 4.644   -105.352 11.568  1.00 104.01 ? 63  ASP   D CA  1 
ATOM   6169  C  C   . ASP   D  4  71  ? 3.569   -105.131 10.496  1.00 103.68 ? 63  ASP   D C   1 
ATOM   6170  O  O   . ASP   D  4  71  ? 3.340   -103.964 10.128  1.00 107.23 ? 63  ASP   D O   1 
ATOM   6171  C  CB  . ASP   D  4  71  ? 4.144   -106.183 12.756  1.00 106.84 ? 63  ASP   D CB  1 
ATOM   6172  C  CG  . ASP   D  4  71  ? 4.320   -107.687 12.596  1.00 110.13 ? 63  ASP   D CG  1 
ATOM   6173  O  OD1 . ASP   D  4  71  ? 4.451   -108.151 11.444  1.00 112.85 ? 63  ASP   D OD1 1 
ATOM   6174  O  OD2 . ASP   D  4  71  ? 4.327   -108.389 13.627  1.00 114.24 ? 63  ASP   D OD2 1 
ATOM   6175  N  N   . ARG   D  4  72  ? 2.937   -106.200 10.007  1.00 102.37 ? 64  ARG   D N   1 
ATOM   6176  C  CA  . ARG   D  4  72  ? 1.912   -106.131 8.929   1.00 102.52 ? 64  ARG   D CA  1 
ATOM   6177  C  C   . ARG   D  4  72  ? 0.681   -105.362 9.425   1.00 99.03  ? 64  ARG   D C   1 
ATOM   6178  O  O   . ARG   D  4  72  ? -0.011  -104.771 8.578   1.00 98.03  ? 64  ARG   D O   1 
ATOM   6179  C  CB  . ARG   D  4  72  ? 1.504   -107.532 8.467   1.00 103.79 ? 64  ARG   D CB  1 
ATOM   6180  C  CG  . ARG   D  4  72  ? 1.142   -107.610 6.991   1.00 107.59 ? 64  ARG   D CG  1 
ATOM   6181  C  CD  . ARG   D  4  72  ? 0.389   -108.881 6.658   1.00 109.21 ? 64  ARG   D CD  1 
ATOM   6182  N  NE  . ARG   D  4  72  ? -1.057  -108.684 6.701   1.00 113.56 ? 64  ARG   D NE  1 
ATOM   6183  C  CZ  . ARG   D  4  72  ? -1.846  -108.469 5.645   1.00 112.96 ? 64  ARG   D CZ  1 
ATOM   6184  N  NH1 . ARG   D  4  72  ? -3.147  -108.306 5.826   1.00 114.42 ? 64  ARG   D NH1 1 
ATOM   6185  N  NH2 . ARG   D  4  72  ? -1.353  -108.419 4.418   1.00 112.12 ? 64  ARG   D NH2 1 
ATOM   6186  N  N   . HIS   D  4  73  ? 0.419   -105.377 10.738  1.00 97.91  ? 65  HIS   D N   1 
ATOM   6187  C  CA  . HIS   D  4  73  ? -0.786  -104.773 11.371  1.00 100.66 ? 65  HIS   D CA  1 
ATOM   6188  C  C   . HIS   D  4  73  ? -0.451  -103.463 12.106  1.00 97.57  ? 65  HIS   D C   1 
ATOM   6189  O  O   . HIS   D  4  73  ? -1.403  -102.834 12.604  1.00 99.26  ? 65  HIS   D O   1 
ATOM   6190  C  CB  . HIS   D  4  73  ? -1.471  -105.795 12.294  1.00 99.17  ? 65  HIS   D CB  1 
ATOM   6191  C  CG  . HIS   D  4  73  ? -0.689  -106.155 13.512  1.00 97.89  ? 65  HIS   D CG  1 
ATOM   6192  N  ND1 . HIS   D  4  73  ? 0.486   -106.877 13.448  1.00 99.27  ? 65  HIS   D ND1 1 
ATOM   6193  C  CD2 . HIS   D  4  73  ? -0.917  -105.917 14.822  1.00 97.83  ? 65  HIS   D CD2 1 
ATOM   6194  C  CE1 . HIS   D  4  73  ? 0.955   -107.056 14.665  1.00 99.96  ? 65  HIS   D CE1 1 
ATOM   6195  N  NE2 . HIS   D  4  73  ? 0.114   -106.475 15.525  1.00 98.74  ? 65  HIS   D NE2 1 
ATOM   6196  N  N   . ILE   D  4  74  ? 0.826   -103.056 12.173  1.00 95.58  ? 66  ILE   D N   1 
ATOM   6197  C  CA  . ILE   D  4  74  ? 1.278   -101.835 12.914  1.00 93.99  ? 66  ILE   D CA  1 
ATOM   6198  C  C   . ILE   D  4  74  ? 2.258   -101.030 12.053  1.00 93.68  ? 66  ILE   D C   1 
ATOM   6199  O  O   . ILE   D  4  74  ? 3.270   -101.604 11.607  1.00 91.05  ? 66  ILE   D O   1 
ATOM   6200  C  CB  . ILE   D  4  74  ? 1.907   -102.192 14.278  1.00 94.69  ? 66  ILE   D CB  1 
ATOM   6201  C  CG1 . ILE   D  4  74  ? 0.874   -102.792 15.236  1.00 95.65  ? 66  ILE   D CG1 1 
ATOM   6202  C  CG2 . ILE   D  4  74  ? 2.592   -100.975 14.889  1.00 94.46  ? 66  ILE   D CG2 1 
ATOM   6203  C  CD1 . ILE   D  4  74  ? 1.455   -103.341 16.519  1.00 95.03  ? 66  ILE   D CD1 1 
ATOM   6204  N  N   . GLY   D  4  75  ? 1.975   -99.733  11.890  1.00 94.81  ? 67  GLY   D N   1 
ATOM   6205  C  CA  . GLY   D  4  75  ? 2.840   -98.736  11.227  1.00 95.73  ? 67  GLY   D CA  1 
ATOM   6206  C  C   . GLY   D  4  75  ? 3.149   -97.573  12.156  1.00 93.95  ? 67  GLY   D C   1 
ATOM   6207  O  O   . GLY   D  4  75  ? 2.455   -97.431  13.184  1.00 95.11  ? 67  GLY   D O   1 
ATOM   6208  N  N   . CYS   D  4  76  ? 4.142   -96.752  11.805  1.00 96.05  ? 68  CYS   D N   1 
ATOM   6209  C  CA  . CYS   D  4  76  ? 4.708   -95.706  12.697  1.00 102.15 ? 68  CYS   D CA  1 
ATOM   6210  C  C   . CYS   D  4  76  ? 5.198   -94.494  11.891  1.00 104.22 ? 68  CYS   D C   1 
ATOM   6211  O  O   . CYS   D  4  76  ? 5.852   -94.696  10.847  1.00 107.92 ? 68  CYS   D O   1 
ATOM   6212  C  CB  . CYS   D  4  76  ? 5.841   -96.298  13.524  1.00 100.71 ? 68  CYS   D CB  1 
ATOM   6213  S  SG  . CYS   D  4  76  ? 6.676   -95.099  14.592  1.00 106.41 ? 68  CYS   D SG  1 
ATOM   6214  N  N   . ALA   D  4  77  ? 4.877   -93.286  12.370  1.00 105.31 ? 69  ALA   D N   1 
ATOM   6215  C  CA  . ALA   D  4  77  ? 5.372   -91.983  11.865  1.00 102.09 ? 69  ALA   D CA  1 
ATOM   6216  C  C   . ALA   D  4  77  ? 6.139   -91.279  12.990  1.00 102.39 ? 69  ALA   D C   1 
ATOM   6217  O  O   . ALA   D  4  77  ? 5.825   -91.543  14.167  1.00 99.10  ? 69  ALA   D O   1 
ATOM   6218  C  CB  . ALA   D  4  77  ? 4.222   -91.142  11.371  1.00 103.68 ? 69  ALA   D CB  1 
ATOM   6219  N  N   . MET   D  4  78  ? 7.096   -90.416  12.640  1.00 100.66 ? 70  MET   D N   1 
ATOM   6220  C  CA  . MET   D  4  78  ? 8.068   -89.823  13.599  1.00 101.38 ? 70  MET   D CA  1 
ATOM   6221  C  C   . MET   D  4  78  ? 8.200   -88.316  13.353  1.00 99.98  ? 70  MET   D C   1 
ATOM   6222  O  O   . MET   D  4  78  ? 7.880   -87.867  12.239  1.00 99.96  ? 70  MET   D O   1 
ATOM   6223  C  CB  . MET   D  4  78  ? 9.440   -90.493  13.463  1.00 102.15 ? 70  MET   D CB  1 
ATOM   6224  C  CG  . MET   D  4  78  ? 10.084  -90.315  12.099  1.00 105.74 ? 70  MET   D CG  1 
ATOM   6225  S  SD  . MET   D  4  78  ? 11.506  -91.408  11.863  1.00 112.01 ? 70  MET   D SD  1 
ATOM   6226  C  CE  . MET   D  4  78  ? 10.672  -92.959  11.518  1.00 116.91 ? 70  MET   D CE  1 
ATOM   6227  N  N   . SER   D  4  79  ? 8.652   -87.576  14.371  1.00 100.62 ? 71  SER   D N   1 
ATOM   6228  C  CA  . SER   D  4  79  ? 8.914   -86.113  14.325  1.00 102.28 ? 71  SER   D CA  1 
ATOM   6229  C  C   . SER   D  4  79  ? 9.942   -85.729  15.396  1.00 99.66  ? 71  SER   D C   1 
ATOM   6230  O  O   . SER   D  4  79  ? 9.762   -86.132  16.560  1.00 99.33  ? 71  SER   D O   1 
ATOM   6231  C  CB  . SER   D  4  79  ? 7.640   -85.332  14.492  1.00 102.27 ? 71  SER   D CB  1 
ATOM   6232  O  OG  . SER   D  4  79  ? 7.887   -83.938  14.394  1.00 104.81 ? 71  SER   D OG  1 
ATOM   6233  N  N   . GLY   D  4  80  ? 10.968  -84.965  15.007  1.00 101.67 ? 72  GLY   D N   1 
ATOM   6234  C  CA  . GLY   D  4  80  ? 12.061  -84.514  15.889  1.00 101.23 ? 72  GLY   D CA  1 
ATOM   6235  C  C   . GLY   D  4  80  ? 13.404  -85.001  15.382  1.00 98.04  ? 72  GLY   D C   1 
ATOM   6236  O  O   . GLY   D  4  80  ? 13.576  -85.066  14.151  1.00 99.03  ? 72  GLY   D O   1 
ATOM   6237  N  N   . LEU   D  4  81  ? 14.327  -85.325  16.292  1.00 98.56  ? 73  LEU   D N   1 
ATOM   6238  C  CA  . LEU   D  4  81  ? 15.653  -85.908  15.952  1.00 100.09 ? 73  LEU   D CA  1 
ATOM   6239  C  C   . LEU   D  4  81  ? 15.427  -87.334  15.436  1.00 100.60 ? 73  LEU   D C   1 
ATOM   6240  O  O   . LEU   D  4  81  ? 15.498  -88.276  16.245  1.00 101.52 ? 73  LEU   D O   1 
ATOM   6241  C  CB  . LEU   D  4  81  ? 16.557  -85.887  17.191  1.00 101.15 ? 73  LEU   D CB  1 
ATOM   6242  C  CG  . LEU   D  4  81  ? 16.932  -84.504  17.726  1.00 100.88 ? 73  LEU   D CG  1 
ATOM   6243  C  CD1 . LEU   D  4  81  ? 17.625  -84.618  19.074  1.00 101.77 ? 73  LEU   D CD1 1 
ATOM   6244  C  CD2 . LEU   D  4  81  ? 17.817  -83.751  16.744  1.00 102.04 ? 73  LEU   D CD2 1 
ATOM   6245  N  N   . THR   D  4  82  ? 15.146  -87.479  14.137  1.00 99.61  ? 74  THR   D N   1 
ATOM   6246  C  CA  . THR   D  4  82  ? 14.653  -88.736  13.505  1.00 100.21 ? 74  THR   D CA  1 
ATOM   6247  C  C   . THR   D  4  82  ? 15.703  -89.852  13.580  1.00 100.03 ? 74  THR   D C   1 
ATOM   6248  O  O   . THR   D  4  82  ? 15.299  -91.028  13.503  1.00 102.94 ? 74  THR   D O   1 
ATOM   6249  C  CB  . THR   D  4  82  ? 14.229  -88.515  12.048  1.00 99.10  ? 74  THR   D CB  1 
ATOM   6250  O  OG1 . THR   D  4  82  ? 15.323  -87.924  11.348  1.00 99.85  ? 74  THR   D OG1 1 
ATOM   6251  C  CG2 . THR   D  4  82  ? 12.995  -87.648  11.929  1.00 99.90  ? 74  THR   D CG2 1 
ATOM   6252  N  N   . ALA   D  4  83  ? 16.989  -89.511  13.707  1.00 100.21 ? 75  ALA   D N   1 
ATOM   6253  C  CA  . ALA   D  4  83  ? 18.099  -90.482  13.867  1.00 97.66  ? 75  ALA   D CA  1 
ATOM   6254  C  C   . ALA   D  4  83  ? 17.897  -91.294  15.155  1.00 96.01  ? 75  ALA   D C   1 
ATOM   6255  O  O   . ALA   D  4  83  ? 18.270  -92.484  15.159  1.00 92.20  ? 75  ALA   D O   1 
ATOM   6256  C  CB  . ALA   D  4  83  ? 19.429  -89.767  13.859  1.00 97.17  ? 75  ALA   D CB  1 
ATOM   6257  N  N   . ASP   D  4  84  ? 17.311  -90.678  16.190  1.00 96.13  ? 76  ASP   D N   1 
ATOM   6258  C  CA  . ASP   D  4  84  ? 17.040  -91.298  17.519  1.00 97.89  ? 76  ASP   D CA  1 
ATOM   6259  C  C   . ASP   D  4  84  ? 15.998  -92.423  17.397  1.00 98.33  ? 76  ASP   D C   1 
ATOM   6260  O  O   . ASP   D  4  84  ? 15.992  -93.313  18.276  1.00 97.88  ? 76  ASP   D O   1 
ATOM   6261  C  CB  . ASP   D  4  84  ? 16.572  -90.256  18.543  1.00 97.87  ? 76  ASP   D CB  1 
ATOM   6262  C  CG  . ASP   D  4  84  ? 17.669  -89.344  19.073  1.00 97.98  ? 76  ASP   D CG  1 
ATOM   6263  O  OD1 . ASP   D  4  84  ? 18.759  -89.315  18.466  1.00 96.34  ? 76  ASP   D OD1 1 
ATOM   6264  O  OD2 . ASP   D  4  84  ? 17.424  -88.668  20.095  1.00 98.62  ? 76  ASP   D OD2 1 
ATOM   6265  N  N   . ALA   D  4  85  ? 15.149  -92.391  16.362  1.00 99.64  ? 77  ALA   D N   1 
ATOM   6266  C  CA  . ALA   D  4  85  ? 13.998  -93.310  16.188  1.00 100.22 ? 77  ALA   D CA  1 
ATOM   6267  C  C   . ALA   D  4  85  ? 14.456  -94.699  15.721  1.00 101.23 ? 77  ALA   D C   1 
ATOM   6268  O  O   . ALA   D  4  85  ? 13.669  -95.644  15.892  1.00 100.90 ? 77  ALA   D O   1 
ATOM   6269  C  CB  . ALA   D  4  85  ? 13.000  -92.720  15.221  1.00 100.16 ? 77  ALA   D CB  1 
ATOM   6270  N  N   . ARG   D  4  86  ? 15.664  -94.831  15.160  1.00 101.87 ? 78  ARG   D N   1 
ATOM   6271  C  CA  . ARG   D  4  86  ? 16.133  -96.095  14.523  1.00 103.99 ? 78  ARG   D CA  1 
ATOM   6272  C  C   . ARG   D  4  86  ? 16.094  -97.237  15.546  1.00 101.33 ? 78  ARG   D C   1 
ATOM   6273  O  O   . ARG   D  4  86  ? 15.510  -98.291  15.221  1.00 101.49 ? 78  ARG   D O   1 
ATOM   6274  C  CB  . ARG   D  4  86  ? 17.531  -95.941  13.911  1.00 108.68 ? 78  ARG   D CB  1 
ATOM   6275  C  CG  . ARG   D  4  86  ? 17.614  -94.925  12.778  1.00 116.31 ? 78  ARG   D CG  1 
ATOM   6276  C  CD  . ARG   D  4  86  ? 16.682  -95.227  11.613  1.00 121.76 ? 78  ARG   D CD  1 
ATOM   6277  N  NE  . ARG   D  4  86  ? 16.220  -94.016  10.942  1.00 128.74 ? 78  ARG   D NE  1 
ATOM   6278  C  CZ  . ARG   D  4  86  ? 15.046  -93.872  10.321  1.00 131.44 ? 78  ARG   D CZ  1 
ATOM   6279  N  NH1 . ARG   D  4  86  ? 14.169  -94.864  10.276  1.00 130.69 ? 78  ARG   D NH1 1 
ATOM   6280  N  NH2 . ARG   D  4  86  ? 14.746  -92.717  9.749   1.00 131.41 ? 78  ARG   D NH2 1 
ATOM   6281  N  N   . SER   D  4  87  ? 16.672  -97.032  16.733  1.00 96.43  ? 79  SER   D N   1 
ATOM   6282  C  CA  . SER   D  4  87  ? 16.730  -98.042  17.823  1.00 95.66  ? 79  SER   D CA  1 
ATOM   6283  C  C   . SER   D  4  87  ? 15.336  -98.262  18.426  1.00 96.70  ? 79  SER   D C   1 
ATOM   6284  O  O   . SER   D  4  87  ? 15.094  -99.368  18.936  1.00 102.86 ? 79  SER   D O   1 
ATOM   6285  C  CB  . SER   D  4  87  ? 17.725  -97.654  18.880  1.00 95.03  ? 79  SER   D CB  1 
ATOM   6286  O  OG  . SER   D  4  87  ? 17.370  -96.412  19.465  1.00 95.07  ? 79  SER   D OG  1 
ATOM   6287  N  N   . MET   D  4  88  ? 14.458  -97.256  18.379  1.00 96.09  ? 80  MET   D N   1 
ATOM   6288  C  CA  . MET   D  4  88  ? 13.051  -97.371  18.850  1.00 97.97  ? 80  MET   D CA  1 
ATOM   6289  C  C   . MET   D  4  88  ? 12.272  -98.283  17.893  1.00 95.69  ? 80  MET   D C   1 
ATOM   6290  O  O   . MET   D  4  88  ? 11.470  -99.092  18.389  1.00 97.20  ? 80  MET   D O   1 
ATOM   6291  C  CB  . MET   D  4  88  ? 12.353  -96.008  18.921  1.00 100.94 ? 80  MET   D CB  1 
ATOM   6292  C  CG  . MET   D  4  88  ? 13.008  -95.026  19.880  1.00 104.01 ? 80  MET   D CG  1 
ATOM   6293  S  SD  . MET   D  4  88  ? 12.144  -93.430  19.976  1.00 106.35 ? 80  MET   D SD  1 
ATOM   6294  C  CE  . MET   D  4  88  ? 10.791  -93.854  21.073  1.00 111.73 ? 80  MET   D CE  1 
ATOM   6295  N  N   . ILE   D  4  89  ? 12.497  -98.147  16.580  1.00 96.33  ? 81  ILE   D N   1 
ATOM   6296  C  CA  . ILE   D  4  89  ? 11.861  -98.988  15.518  1.00 97.33  ? 81  ILE   D CA  1 
ATOM   6297  C  C   . ILE   D  4  89  ? 12.412  -100.416 15.622  1.00 96.38  ? 81  ILE   D C   1 
ATOM   6298  O  O   . ILE   D  4  89  ? 11.603  -101.369 15.572  1.00 94.98  ? 81  ILE   D O   1 
ATOM   6299  C  CB  . ILE   D  4  89  ? 12.094  -98.396  14.111  1.00 98.31  ? 81  ILE   D CB  1 
ATOM   6300  C  CG1 . ILE   D  4  89  ? 11.492  -96.994  13.964  1.00 100.90 ? 81  ILE   D CG1 1 
ATOM   6301  C  CG2 . ILE   D  4  89  ? 11.583  -99.338  13.031  1.00 94.91  ? 81  ILE   D CG2 1 
ATOM   6302  C  CD1 . ILE   D  4  89  ? 10.009  -96.906  14.258  1.00 106.19 ? 81  ILE   D CD1 1 
ATOM   6303  N  N   . GLU   D  4  90  ? 13.737  -100.553 15.739  1.00 94.77  ? 82  GLU   D N   1 
ATOM   6304  C  CA  . GLU   D  4  90  ? 14.438  -101.860 15.847  1.00 93.50  ? 82  GLU   D CA  1 
ATOM   6305  C  C   . GLU   D  4  90  ? 13.834  -102.647 17.017  1.00 91.59  ? 82  GLU   D C   1 
ATOM   6306  O  O   . GLU   D  4  90  ? 13.517  -103.835 16.821  1.00 88.49  ? 82  GLU   D O   1 
ATOM   6307  C  CB  . GLU   D  4  90  ? 15.948  -101.641 15.985  1.00 96.40  ? 82  GLU   D CB  1 
ATOM   6308  C  CG  . GLU   D  4  90  ? 16.736  -102.903 16.303  1.00 99.32  ? 82  GLU   D CG  1 
ATOM   6309  C  CD  . GLU   D  4  90  ? 16.559  -104.064 15.333  1.00 101.09 ? 82  GLU   D CD  1 
ATOM   6310  O  OE1 . GLU   D  4  90  ? 16.143  -103.821 14.181  1.00 102.52 ? 82  GLU   D OE1 1 
ATOM   6311  O  OE2 . GLU   D  4  90  ? 16.850  -105.214 15.729  1.00 103.13 ? 82  GLU   D OE2 1 
ATOM   6312  N  N   . HIS   D  4  91  ? 13.656  -101.999 18.174  1.00 88.76  ? 83  HIS   D N   1 
ATOM   6313  C  CA  . HIS   D  4  91  ? 13.046  -102.591 19.394  1.00 89.33  ? 83  HIS   D CA  1 
ATOM   6314  C  C   . HIS   D  4  91  ? 11.596  -102.995 19.113  1.00 89.02  ? 83  HIS   D C   1 
ATOM   6315  O  O   . HIS   D  4  91  ? 11.234  -104.133 19.445  1.00 91.78  ? 83  HIS   D O   1 
ATOM   6316  C  CB  . HIS   D  4  91  ? 13.107  -101.621 20.579  1.00 91.63  ? 83  HIS   D CB  1 
ATOM   6317  C  CG  . HIS   D  4  91  ? 12.447  -102.153 21.806  1.00 94.88  ? 83  HIS   D CG  1 
ATOM   6318  N  ND1 . HIS   D  4  91  ? 13.155  -102.789 22.808  1.00 96.48  ? 83  HIS   D ND1 1 
ATOM   6319  C  CD2 . HIS   D  4  91  ? 11.151  -102.161 22.191  1.00 97.92  ? 83  HIS   D CD2 1 
ATOM   6320  C  CE1 . HIS   D  4  91  ? 12.323  -103.160 23.762  1.00 100.03 ? 83  HIS   D CE1 1 
ATOM   6321  N  NE2 . HIS   D  4  91  ? 11.087  -102.786 23.407  1.00 98.91  ? 83  HIS   D NE2 1 
ATOM   6322  N  N   . ALA   D  4  92  ? 10.804  -102.083 18.546  1.00 88.29  ? 84  ALA   D N   1 
ATOM   6323  C  CA  . ALA   D  4  92  ? 9.367   -102.275 18.239  1.00 90.76  ? 84  ALA   D CA  1 
ATOM   6324  C  C   . ALA   D  4  92  ? 9.183   -103.504 17.344  1.00 88.66  ? 84  ALA   D C   1 
ATOM   6325  O  O   . ALA   D  4  92  ? 8.273   -104.298 17.628  1.00 92.12  ? 84  ALA   D O   1 
ATOM   6326  C  CB  . ALA   D  4  92  ? 8.808   -101.040 17.579  1.00 92.57  ? 84  ALA   D CB  1 
ATOM   6327  N  N   . ARG   D  4  93  ? 10.013  -103.645 16.304  1.00 89.87  ? 85  ARG   D N   1 
ATOM   6328  C  CA  . ARG   D  4  93  ? 9.950   -104.763 15.320  1.00 89.86  ? 85  ARG   D CA  1 
ATOM   6329  C  C   . ARG   D  4  93  ? 10.275  -106.092 16.011  1.00 87.24  ? 85  ARG   D C   1 
ATOM   6330  O  O   . ARG   D  4  93  ? 9.558   -107.080 15.752  1.00 84.64  ? 85  ARG   D O   1 
ATOM   6331  C  CB  . ARG   D  4  93  ? 10.912  -104.516 14.155  1.00 90.40  ? 85  ARG   D CB  1 
ATOM   6332  C  CG  . ARG   D  4  93  ? 10.414  -103.467 13.174  1.00 90.41  ? 85  ARG   D CG  1 
ATOM   6333  C  CD  . ARG   D  4  93  ? 11.490  -103.009 12.213  1.00 88.40  ? 85  ARG   D CD  1 
ATOM   6334  N  NE  . ARG   D  4  93  ? 10.939  -102.196 11.136  1.00 86.80  ? 85  ARG   D NE  1 
ATOM   6335  C  CZ  . ARG   D  4  93  ? 11.660  -101.590 10.198  1.00 85.11  ? 85  ARG   D CZ  1 
ATOM   6336  N  NH1 . ARG   D  4  93  ? 12.980  -101.690 10.195  1.00 84.25  ? 85  ARG   D NH1 1 
ATOM   6337  N  NH2 . ARG   D  4  93  ? 11.057  -100.877 9.265   1.00 86.53  ? 85  ARG   D NH2 1 
ATOM   6338  N  N   . THR   D  4  94  ? 11.319  -106.112 16.844  1.00 85.19  ? 86  THR   D N   1 
ATOM   6339  C  CA  . THR   D  4  94  ? 11.760  -107.306 17.611  1.00 83.91  ? 86  THR   D CA  1 
ATOM   6340  C  C   . THR   D  4  94  ? 10.674  -107.689 18.621  1.00 87.13  ? 86  THR   D C   1 
ATOM   6341  O  O   . THR   D  4  94  ? 10.382  -108.891 18.731  1.00 88.91  ? 86  THR   D O   1 
ATOM   6342  C  CB  . THR   D  4  94  ? 13.105  -107.077 18.307  1.00 82.54  ? 86  THR   D CB  1 
ATOM   6343  O  OG1 . THR   D  4  94  ? 14.038  -106.601 17.337  1.00 80.41  ? 86  THR   D OG1 1 
ATOM   6344  C  CG2 . THR   D  4  94  ? 13.644  -108.337 18.946  1.00 82.11  ? 86  THR   D CG2 1 
ATOM   6345  N  N   . ALA   D  4  95  ? 10.105  -106.706 19.326  1.00 86.87  ? 87  ALA   D N   1 
ATOM   6346  C  CA  . ALA   D  4  95  ? 9.002   -106.891 20.300  1.00 88.49  ? 87  ALA   D CA  1 
ATOM   6347  C  C   . ALA   D  4  95  ? 7.800   -107.546 19.609  1.00 89.11  ? 87  ALA   D C   1 
ATOM   6348  O  O   . ALA   D  4  95  ? 7.212   -108.469 20.203  1.00 92.60  ? 87  ALA   D O   1 
ATOM   6349  C  CB  . ALA   D  4  95  ? 8.621   -105.569 20.918  1.00 88.81  ? 87  ALA   D CB  1 
ATOM   6350  N  N   . ALA   D  4  96  ? 7.465   -107.092 18.397  1.00 88.11  ? 88  ALA   D N   1 
ATOM   6351  C  CA  . ALA   D  4  96  ? 6.306   -107.560 17.600  1.00 89.71  ? 88  ALA   D CA  1 
ATOM   6352  C  C   . ALA   D  4  96  ? 6.532   -109.000 17.122  1.00 89.11  ? 88  ALA   D C   1 
ATOM   6353  O  O   . ALA   D  4  96  ? 5.623   -109.833 17.298  1.00 90.61  ? 88  ALA   D O   1 
ATOM   6354  C  CB  . ALA   D  4  96  ? 6.070   -106.636 16.433  1.00 90.40  ? 88  ALA   D CB  1 
ATOM   6355  N  N   . VAL   D  4  97  ? 7.696   -109.268 16.522  1.00 89.09  ? 89  VAL   D N   1 
ATOM   6356  C  CA  . VAL   D  4  97  ? 8.076   -110.602 15.967  1.00 88.88  ? 89  VAL   D CA  1 
ATOM   6357  C  C   . VAL   D  4  97  ? 8.267   -111.596 17.121  1.00 87.95  ? 89  VAL   D C   1 
ATOM   6358  O  O   . VAL   D  4  97  ? 7.803   -112.748 16.985  1.00 86.73  ? 89  VAL   D O   1 
ATOM   6359  C  CB  . VAL   D  4  97  ? 9.331   -110.502 15.076  1.00 90.90  ? 89  VAL   D CB  1 
ATOM   6360  C  CG1 . VAL   D  4  97  ? 9.906   -111.869 14.740  1.00 91.06  ? 89  VAL   D CG1 1 
ATOM   6361  C  CG2 . VAL   D  4  97  ? 9.047   -109.724 13.800  1.00 93.20  ? 89  VAL   D CG2 1 
ATOM   6362  N  N   . THR   D  4  98  ? 8.926   -111.178 18.208  1.00 84.34  ? 90  THR   D N   1 
ATOM   6363  C  CA  . THR   D  4  98  ? 9.216   -112.038 19.386  1.00 84.09  ? 90  THR   D CA  1 
ATOM   6364  C  C   . THR   D  4  98  ? 7.899   -112.526 19.993  1.00 86.74  ? 90  THR   D C   1 
ATOM   6365  O  O   . THR   D  4  98  ? 7.817   -113.721 20.329  1.00 87.93  ? 90  THR   D O   1 
ATOM   6366  C  CB  . THR   D  4  98  ? 10.047  -111.323 20.457  1.00 81.82  ? 90  THR   D CB  1 
ATOM   6367  O  OG1 . THR   D  4  98  ? 11.307  -110.968 19.890  1.00 81.18  ? 90  THR   D OG1 1 
ATOM   6368  C  CG2 . THR   D  4  98  ? 10.291  -112.182 21.678  1.00 81.77  ? 90  THR   D CG2 1 
ATOM   6369  N  N   . HIS   D  4  99  ? 6.920   -111.634 20.151  1.00 86.61  ? 91  HIS   D N   1 
ATOM   6370  C  CA  . HIS   D  4  99  ? 5.586   -111.973 20.709  1.00 86.90  ? 91  HIS   D CA  1 
ATOM   6371  C  C   . HIS   D  4  99  ? 4.911   -113.022 19.818  1.00 89.56  ? 91  HIS   D C   1 
ATOM   6372  O  O   . HIS   D  4  99  ? 4.248   -113.922 20.368  1.00 93.77  ? 91  HIS   D O   1 
ATOM   6373  C  CB  . HIS   D  4  99  ? 4.726   -110.720 20.873  1.00 87.08  ? 91  HIS   D CB  1 
ATOM   6374  C  CG  . HIS   D  4  99  ? 3.353   -111.013 21.372  1.00 87.10  ? 91  HIS   D CG  1 
ATOM   6375  N  ND1 . HIS   D  4  99  ? 3.018   -110.904 22.705  1.00 91.78  ? 91  HIS   D ND1 1 
ATOM   6376  C  CD2 . HIS   D  4  99  ? 2.239   -111.428 20.732  1.00 89.61  ? 91  HIS   D CD2 1 
ATOM   6377  C  CE1 . HIS   D  4  99  ? 1.750   -111.230 22.864  1.00 95.21  ? 91  HIS   D CE1 1 
ATOM   6378  N  NE2 . HIS   D  4  99  ? 1.250   -111.555 21.668  1.00 94.51  ? 91  HIS   D NE2 1 
ATOM   6379  N  N   . ASN   D  4  100 ? 5.078   -112.914 18.498  1.00 87.69  ? 92  ASN   D N   1 
ATOM   6380  C  CA  . ASN   D  4  100 ? 4.499   -113.868 17.515  1.00 90.31  ? 92  ASN   D CA  1 
ATOM   6381  C  C   . ASN   D  4  100 ? 5.169   -115.237 17.685  1.00 88.99  ? 92  ASN   D C   1 
ATOM   6382  O  O   . ASN   D  4  100 ? 4.456   -116.254 17.591  1.00 91.10  ? 92  ASN   D O   1 
ATOM   6383  C  CB  . ASN   D  4  100 ? 4.615   -113.345 16.083  1.00 91.37  ? 92  ASN   D CB  1 
ATOM   6384  C  CG  . ASN   D  4  100 ? 4.099   -114.332 15.060  1.00 94.15  ? 92  ASN   D CG  1 
ATOM   6385  O  OD1 . ASN   D  4  100 ? 4.866   -114.842 14.249  1.00 99.14  ? 92  ASN   D OD1 1 
ATOM   6386  N  ND2 . ASN   D  4  100 ? 2.808   -114.621 15.106  1.00 96.84  ? 92  ASN   D ND2 1 
ATOM   6387  N  N   . LEU   D  4  101 ? 6.480   -115.261 17.941  1.00 88.97  ? 93  LEU   D N   1 
ATOM   6388  C  CA  . LEU   D  4  101 ? 7.261   -116.512 18.144  1.00 88.34  ? 93  LEU   D CA  1 
ATOM   6389  C  C   . LEU   D  4  101 ? 6.814   -117.191 19.447  1.00 92.37  ? 93  LEU   D C   1 
ATOM   6390  O  O   . LEU   D  4  101 ? 6.662   -118.424 19.431  1.00 94.08  ? 93  LEU   D O   1 
ATOM   6391  C  CB  . LEU   D  4  101 ? 8.759   -116.185 18.158  1.00 84.25  ? 93  LEU   D CB  1 
ATOM   6392  C  CG  . LEU   D  4  101 ? 9.701   -117.374 18.346  1.00 83.37  ? 93  LEU   D CG  1 
ATOM   6393  C  CD1 . LEU   D  4  101 ? 9.625   -118.328 17.165  1.00 83.84  ? 93  LEU   D CD1 1 
ATOM   6394  C  CD2 . LEU   D  4  101 ? 11.132  -116.907 18.552  1.00 81.28  ? 93  LEU   D CD2 1 
ATOM   6395  N  N   . TYR   D  4  102 ? 6.597   -116.424 20.522  1.00 93.54  ? 94  TYR   D N   1 
ATOM   6396  C  CA  . TYR   D  4  102 ? 6.267   -116.951 21.875  1.00 95.73  ? 94  TYR   D CA  1 
ATOM   6397  C  C   . TYR   D  4  102 ? 4.787   -117.345 21.974  1.00 95.84  ? 94  TYR   D C   1 
ATOM   6398  O  O   . TYR   D  4  102 ? 4.491   -118.216 22.813  1.00 99.31  ? 94  TYR   D O   1 
ATOM   6399  C  CB  . TYR   D  4  102 ? 6.611   -115.949 22.985  1.00 98.81  ? 94  TYR   D CB  1 
ATOM   6400  C  CG  . TYR   D  4  102 ? 8.080   -115.753 23.276  1.00 102.79 ? 94  TYR   D CG  1 
ATOM   6401  C  CD1 . TYR   D  4  102 ? 9.031   -116.698 22.918  1.00 105.72 ? 94  TYR   D CD1 1 
ATOM   6402  C  CD2 . TYR   D  4  102 ? 8.522   -114.624 23.950  1.00 101.77 ? 94  TYR   D CD2 1 
ATOM   6403  C  CE1 . TYR   D  4  102 ? 10.376  -116.515 23.194  1.00 108.83 ? 94  TYR   D CE1 1 
ATOM   6404  C  CE2 . TYR   D  4  102 ? 9.863   -114.426 24.236  1.00 103.35 ? 94  TYR   D CE2 1 
ATOM   6405  C  CZ  . TYR   D  4  102 ? 10.795  -115.375 23.856  1.00 105.45 ? 94  TYR   D CZ  1 
ATOM   6406  O  OH  . TYR   D  4  102 ? 12.118  -115.191 24.132  1.00 113.70 ? 94  TYR   D OH  1 
ATOM   6407  N  N   . TYR   D  4  103 ? 3.890   -116.739 21.182  1.00 92.24  ? 95  TYR   D N   1 
ATOM   6408  C  CA  . TYR   D  4  103 ? 2.417   -116.869 21.371  1.00 92.15  ? 95  TYR   D CA  1 
ATOM   6409  C  C   . TYR   D  4  103 ? 1.658   -117.171 20.070  1.00 91.93  ? 95  TYR   D C   1 
ATOM   6410  O  O   . TYR   D  4  103 ? 0.417   -117.263 20.148  1.00 88.10  ? 95  TYR   D O   1 
ATOM   6411  C  CB  . TYR   D  4  103 ? 1.855   -115.600 22.018  1.00 91.08  ? 95  TYR   D CB  1 
ATOM   6412  C  CG  . TYR   D  4  103 ? 2.371   -115.332 23.408  1.00 89.34  ? 95  TYR   D CG  1 
ATOM   6413  C  CD1 . TYR   D  4  103 ? 1.933   -116.079 24.489  1.00 90.05  ? 95  TYR   D CD1 1 
ATOM   6414  C  CD2 . TYR   D  4  103 ? 3.304   -114.338 23.645  1.00 88.19  ? 95  TYR   D CD2 1 
ATOM   6415  C  CE1 . TYR   D  4  103 ? 2.406   -115.845 25.769  1.00 90.68  ? 95  TYR   D CE1 1 
ATOM   6416  C  CE2 . TYR   D  4  103 ? 3.786   -114.089 24.918  1.00 89.36  ? 95  TYR   D CE2 1 
ATOM   6417  C  CZ  . TYR   D  4  103 ? 3.335   -114.844 25.985  1.00 89.64  ? 95  TYR   D CZ  1 
ATOM   6418  O  OH  . TYR   D  4  103 ? 3.806   -114.603 27.241  1.00 93.26  ? 95  TYR   D OH  1 
ATOM   6419  N  N   . ASP   D  4  104 ? 2.335   -117.328 18.927  1.00 93.06  ? 96  ASP   D N   1 
ATOM   6420  C  CA  . ASP   D  4  104 ? 1.690   -117.722 17.644  1.00 96.88  ? 96  ASP   D CA  1 
ATOM   6421  C  C   . ASP   D  4  104 ? 0.458   -116.837 17.401  1.00 96.01  ? 96  ASP   D C   1 
ATOM   6422  O  O   . ASP   D  4  104 ? -0.620  -117.384 17.096  1.00 95.96  ? 96  ASP   D O   1 
ATOM   6423  C  CB  . ASP   D  4  104 ? 1.323   -119.211 17.664  1.00 100.75 ? 96  ASP   D CB  1 
ATOM   6424  C  CG  . ASP   D  4  104 ? 0.688   -119.722 16.382  1.00 105.73 ? 96  ASP   D CG  1 
ATOM   6425  O  OD1 . ASP   D  4  104 ? 0.959   -119.132 15.313  1.00 105.43 ? 96  ASP   D OD1 1 
ATOM   6426  O  OD2 . ASP   D  4  104 ? -0.080  -120.703 16.465  1.00 115.11 ? 96  ASP   D OD2 1 
ATOM   6427  N  N   . GLU   D  4  105 ? 0.609   -115.519 17.550  1.00 93.95  ? 97  GLU   D N   1 
ATOM   6428  C  CA  . GLU   D  4  105 ? -0.486  -114.527 17.369  1.00 95.43  ? 97  GLU   D CA  1 
ATOM   6429  C  C   . GLU   D  4  105 ? 0.118   -113.141 17.117  1.00 94.26  ? 97  GLU   D C   1 
ATOM   6430  O  O   . GLU   D  4  105 ? 1.321   -112.968 17.375  1.00 91.38  ? 97  GLU   D O   1 
ATOM   6431  C  CB  . GLU   D  4  105 ? -1.414  -114.520 18.588  1.00 96.73  ? 97  GLU   D CB  1 
ATOM   6432  C  CG  . GLU   D  4  105 ? -0.790  -113.936 19.845  1.00 96.13  ? 97  GLU   D CG  1 
ATOM   6433  C  CD  . GLU   D  4  105 ? -1.720  -113.840 21.043  1.00 99.61  ? 97  GLU   D CD  1 
ATOM   6434  O  OE1 . GLU   D  4  105 ? -1.353  -113.142 22.009  1.00 96.36  ? 97  GLU   D OE1 1 
ATOM   6435  O  OE2 . GLU   D  4  105 ? -2.807  -114.461 21.012  1.00 102.51 ? 97  GLU   D OE2 1 
ATOM   6436  N  N   . ASP   D  4  106 ? -0.692  -112.202 16.623  1.00 98.88  ? 98  ASP   D N   1 
ATOM   6437  C  CA  . ASP   D  4  106 ? -0.317  -110.770 16.474  1.00 100.05 ? 98  ASP   D CA  1 
ATOM   6438  C  C   . ASP   D  4  106 ? -0.344  -110.109 17.854  1.00 98.05  ? 98  ASP   D C   1 
ATOM   6439  O  O   . ASP   D  4  106 ? -1.237  -110.445 18.653  1.00 98.97  ? 98  ASP   D O   1 
ATOM   6440  C  CB  . ASP   D  4  106 ? -1.252  -110.034 15.511  1.00 103.02 ? 98  ASP   D CB  1 
ATOM   6441  C  CG  . ASP   D  4  106 ? -1.053  -110.404 14.052  1.00 105.42 ? 98  ASP   D CG  1 
ATOM   6442  O  OD1 . ASP   D  4  106 ? -0.241  -111.310 13.782  1.00 109.32 ? 98  ASP   D OD1 1 
ATOM   6443  O  OD2 . ASP   D  4  106 ? -1.708  -109.776 13.197  1.00 107.75 ? 98  ASP   D OD2 1 
ATOM   6444  N  N   . ILE   D  4  107 ? 0.587   -109.191 18.110  1.00 99.44  ? 99  ILE   D N   1 
ATOM   6445  C  CA  . ILE   D  4  107 ? 0.713   -108.485 19.421  1.00 100.80 ? 99  ILE   D CA  1 
ATOM   6446  C  C   . ILE   D  4  107 ? -0.206  -107.261 19.360  1.00 98.64  ? 99  ILE   D C   1 
ATOM   6447  O  O   . ILE   D  4  107 ? -0.269  -106.627 18.291  1.00 95.26  ? 99  ILE   D O   1 
ATOM   6448  C  CB  . ILE   D  4  107 ? 2.184   -108.143 19.763  1.00 99.82  ? 99  ILE   D CB  1 
ATOM   6449  C  CG1 . ILE   D  4  107 ? 2.449   -106.646 19.926  1.00 101.26 ? 99  ILE   D CG1 1 
ATOM   6450  C  CG2 . ILE   D  4  107 ? 3.145   -108.755 18.754  1.00 102.34 ? 99  ILE   D CG2 1 
ATOM   6451  C  CD1 . ILE   D  4  107 ? 2.800   -105.951 18.634  1.00 103.59 ? 99  ILE   D CD1 1 
ATOM   6452  N  N   . ASN   D  4  108 ? -0.918  -106.972 20.453  1.00 101.57 ? 100 ASN   D N   1 
ATOM   6453  C  CA  . ASN   D  4  108 ? -1.867  -105.831 20.548  1.00 102.93 ? 100 ASN   D CA  1 
ATOM   6454  C  C   . ASN   D  4  108 ? -1.100  -104.519 20.345  1.00 103.33 ? 100 ASN   D C   1 
ATOM   6455  O  O   . ASN   D  4  108 ? 0.034   -104.407 20.848  1.00 104.34 ? 100 ASN   D O   1 
ATOM   6456  C  CB  . ASN   D  4  108 ? -2.631  -105.823 21.876  1.00 104.31 ? 100 ASN   D CB  1 
ATOM   6457  C  CG  . ASN   D  4  108 ? -3.613  -106.968 22.030  1.00 104.18 ? 100 ASN   D CG  1 
ATOM   6458  O  OD1 . ASN   D  4  108 ? -3.809  -107.465 23.137  1.00 106.71 ? 100 ASN   D OD1 1 
ATOM   6459  N  ND2 . ASN   D  4  108 ? -4.245  -107.395 20.946  1.00 103.67 ? 100 ASN   D ND2 1 
ATOM   6460  N  N   . VAL   D  4  109 ? -1.713  -103.565 19.639  1.00 104.39 ? 101 VAL   D N   1 
ATOM   6461  C  CA  . VAL   D  4  109 ? -1.109  -102.244 19.290  1.00 105.36 ? 101 VAL   D CA  1 
ATOM   6462  C  C   . VAL   D  4  109 ? -0.701  -101.538 20.589  1.00 103.14 ? 101 VAL   D C   1 
ATOM   6463  O  O   . VAL   D  4  109 ? 0.395   -100.948 20.617  1.00 103.70 ? 101 VAL   D O   1 
ATOM   6464  C  CB  . VAL   D  4  109 ? -2.074  -101.377 18.455  1.00 108.45 ? 101 VAL   D CB  1 
ATOM   6465  C  CG1 . VAL   D  4  109 ? -1.482  -100.013 18.131  1.00 108.35 ? 101 VAL   D CG1 1 
ATOM   6466  C  CG2 . VAL   D  4  109 ? -2.510  -102.078 17.175  1.00 110.80 ? 101 VAL   D CG2 1 
ATOM   6467  N  N   . GLU   D  4  110 ? -1.548  -101.611 21.621  1.00 101.71 ? 102 GLU   D N   1 
ATOM   6468  C  CA  . GLU   D  4  110 ? -1.324  -100.944 22.932  1.00 103.55 ? 102 GLU   D CA  1 
ATOM   6469  C  C   . GLU   D  4  110 ? -0.113  -101.582 23.625  1.00 101.98 ? 102 GLU   D C   1 
ATOM   6470  O  O   . GLU   D  4  110 ? 0.700   -100.829 24.197  1.00 96.36  ? 102 GLU   D O   1 
ATOM   6471  C  CB  . GLU   D  4  110 ? -2.572  -101.036 23.812  1.00 110.43 ? 102 GLU   D CB  1 
ATOM   6472  C  CG  . GLU   D  4  110 ? -2.623  -99.974  24.898  1.00 115.50 ? 102 GLU   D CG  1 
ATOM   6473  C  CD  . GLU   D  4  110 ? -2.972  -100.488 26.284  1.00 122.74 ? 102 GLU   D CD  1 
ATOM   6474  O  OE1 . GLU   D  4  110 ? -4.086  -100.187 26.762  1.00 127.25 ? 102 GLU   D OE1 1 
ATOM   6475  O  OE2 . GLU   D  4  110 ? -2.123  -101.180 26.887  1.00 131.42 ? 102 GLU   D OE2 1 
ATOM   6476  N  N   . SER   D  4  111 ? -0.005  -102.915 23.571  1.00 102.11 ? 103 SER   D N   1 
ATOM   6477  C  CA  . SER   D  4  111 ? 1.118   -103.709 24.140  1.00 100.95 ? 103 SER   D CA  1 
ATOM   6478  C  C   . SER   D  4  111 ? 2.430   -103.328 23.445  1.00 96.81  ? 103 SER   D C   1 
ATOM   6479  O  O   . SER   D  4  111 ? 3.447   -103.177 24.153  1.00 95.50  ? 103 SER   D O   1 
ATOM   6480  C  CB  . SER   D  4  111 ? 0.850   -105.186 24.033  1.00 101.09 ? 103 SER   D CB  1 
ATOM   6481  O  OG  . SER   D  4  111 ? -0.322  -105.534 24.756  1.00 107.69 ? 103 SER   D OG  1 
ATOM   6482  N  N   . LEU   D  4  112 ? 2.404   -103.177 22.116  1.00 93.05  ? 104 LEU   D N   1 
ATOM   6483  C  CA  . LEU   D  4  112 ? 3.561   -102.705 21.308  1.00 92.61  ? 104 LEU   D CA  1 
ATOM   6484  C  C   . LEU   D  4  112 ? 3.982   -101.326 21.819  1.00 94.08  ? 104 LEU   D C   1 
ATOM   6485  O  O   . LEU   D  4  112 ? 5.179   -101.147 22.116  1.00 98.47  ? 104 LEU   D O   1 
ATOM   6486  C  CB  . LEU   D  4  112 ? 3.169   -102.629 19.829  1.00 88.63  ? 104 LEU   D CB  1 
ATOM   6487  C  CG  . LEU   D  4  112 ? 4.308   -102.426 18.823  1.00 88.27  ? 104 LEU   D CG  1 
ATOM   6488  C  CD1 . LEU   D  4  112 ? 4.623   -100.952 18.631  1.00 89.98  ? 104 LEU   D CD1 1 
ATOM   6489  C  CD2 . LEU   D  4  112 ? 5.567   -103.180 19.216  1.00 86.28  ? 104 LEU   D CD2 1 
ATOM   6490  N  N   . THR   D  4  113 ? 3.023   -100.399 21.907  1.00 97.36  ? 105 THR   D N   1 
ATOM   6491  C  CA  . THR   D  4  113 ? 3.250   -98.979  22.283  1.00 98.96  ? 105 THR   D CA  1 
ATOM   6492  C  C   . THR   D  4  113 ? 3.852   -98.924  23.692  1.00 99.29  ? 105 THR   D C   1 
ATOM   6493  O  O   . THR   D  4  113 ? 4.814   -98.155  23.885  1.00 101.47 ? 105 THR   D O   1 
ATOM   6494  C  CB  . THR   D  4  113 ? 1.963   -98.153  22.157  1.00 101.13 ? 105 THR   D CB  1 
ATOM   6495  O  OG1 . THR   D  4  113 ? 1.392   -98.405  20.872  1.00 103.56 ? 105 THR   D OG1 1 
ATOM   6496  C  CG2 . THR   D  4  113 ? 2.204   -96.668  22.314  1.00 101.48 ? 105 THR   D CG2 1 
ATOM   6497  N  N   . GLN   D  4  114 ? 3.323   -99.725  24.625  1.00 99.41  ? 106 GLN   D N   1 
ATOM   6498  C  CA  . GLN   D  4  114 ? 3.790   -99.787  26.038  1.00 99.25  ? 106 GLN   D CA  1 
ATOM   6499  C  C   . GLN   D  4  114 ? 5.237   -100.297 26.075  1.00 96.00  ? 106 GLN   D C   1 
ATOM   6500  O  O   . GLN   D  4  114 ? 6.003   -99.819  26.934  1.00 89.85  ? 106 GLN   D O   1 
ATOM   6501  C  CB  . GLN   D  4  114 ? 2.857   -100.668 26.876  1.00 101.29 ? 106 GLN   D CB  1 
ATOM   6502  C  CG  . GLN   D  4  114 ? 3.301   -100.841 28.323  1.00 101.43 ? 106 GLN   D CG  1 
ATOM   6503  C  CD  . GLN   D  4  114 ? 3.326   -99.537  29.080  1.00 100.44 ? 106 GLN   D CD  1 
ATOM   6504  O  OE1 . GLN   D  4  114 ? 4.361   -98.887  29.197  1.00 101.80 ? 106 GLN   D OE1 1 
ATOM   6505  N  NE2 . GLN   D  4  114 ? 2.174   -99.139  29.593  1.00 103.00 ? 106 GLN   D NE2 1 
ATOM   6506  N  N   . SER   D  4  115 ? 5.591   -101.226 25.180  1.00 98.70  ? 107 SER   D N   1 
ATOM   6507  C  CA  . SER   D  4  115 ? 6.952   -101.817 25.052  1.00 99.06  ? 107 SER   D CA  1 
ATOM   6508  C  C   . SER   D  4  115 ? 7.956   -100.747 24.602  1.00 99.12  ? 107 SER   D C   1 
ATOM   6509  O  O   . SER   D  4  115 ? 9.076   -100.718 25.147  1.00 95.52  ? 107 SER   D O   1 
ATOM   6510  C  CB  . SER   D  4  115 ? 6.956   -102.991 24.104  1.00 102.73 ? 107 SER   D CB  1 
ATOM   6511  O  OG  . SER   D  4  115 ? 8.190   -103.691 24.172  1.00 105.05 ? 107 SER   D OG  1 
ATOM   6512  N  N   . VAL   D  4  116 ? 7.576   -99.916  23.627  1.00 100.59 ? 108 VAL   D N   1 
ATOM   6513  C  CA  . VAL   D  4  116 ? 8.430   -98.819  23.079  1.00 100.36 ? 108 VAL   D CA  1 
ATOM   6514  C  C   . VAL   D  4  116 ? 8.625   -97.758  24.170  1.00 103.14 ? 108 VAL   D C   1 
ATOM   6515  O  O   . VAL   D  4  116 ? 9.770   -97.290  24.344  1.00 100.12 ? 108 VAL   D O   1 
ATOM   6516  C  CB  . VAL   D  4  116 ? 7.826   -98.214  21.794  1.00 100.71 ? 108 VAL   D CB  1 
ATOM   6517  C  CG1 . VAL   D  4  116 ? 8.581   -96.972  21.341  1.00 99.34  ? 108 VAL   D CG1 1 
ATOM   6518  C  CG2 . VAL   D  4  116 ? 7.763   -99.233  20.665  1.00 99.20  ? 108 VAL   D CG2 1 
ATOM   6519  N  N   . CYS   D  4  117 ? 7.547   -97.404  24.878  1.00 104.62 ? 109 CYS   D N   1 
ATOM   6520  C  CA  . CYS   D  4  117 ? 7.529   -96.367  25.947  1.00 104.34 ? 109 CYS   D CA  1 
ATOM   6521  C  C   . CYS   D  4  117 ? 8.384   -96.802  27.146  1.00 102.94 ? 109 CYS   D C   1 
ATOM   6522  O  O   . CYS   D  4  117 ? 8.798   -95.919  27.916  1.00 99.19  ? 109 CYS   D O   1 
ATOM   6523  C  CB  . CYS   D  4  117 ? 6.105   -96.058  26.395  1.00 106.32 ? 109 CYS   D CB  1 
ATOM   6524  S  SG  . CYS   D  4  117 ? 5.178   -95.076  25.188  1.00 109.99 ? 109 CYS   D SG  1 
ATOM   6525  N  N   . ASP   D  4  118 ? 8.637   -98.106  27.303  1.00 103.56 ? 110 ASP   D N   1 
ATOM   6526  C  CA  . ASP   D  4  118 ? 9.484   -98.655  28.397  1.00 104.56 ? 110 ASP   D CA  1 
ATOM   6527  C  C   . ASP   D  4  118 ? 10.945  -98.232  28.184  1.00 103.41 ? 110 ASP   D C   1 
ATOM   6528  O  O   . ASP   D  4  118 ? 11.633  -98.014  29.198  1.00 102.85 ? 110 ASP   D O   1 
ATOM   6529  C  CB  . ASP   D  4  118 ? 9.330   -100.175 28.524  1.00 106.24 ? 110 ASP   D CB  1 
ATOM   6530  C  CG  . ASP   D  4  118 ? 8.055   -100.623 29.221  1.00 107.98 ? 110 ASP   D CG  1 
ATOM   6531  O  OD1 . ASP   D  4  118 ? 7.323   -99.755  29.737  1.00 112.49 ? 110 ASP   D OD1 1 
ATOM   6532  O  OD2 . ASP   D  4  118 ? 7.802   -101.845 29.247  1.00 108.54 ? 110 ASP   D OD2 1 
ATOM   6533  N  N   . LEU   D  4  119 ? 11.401  -98.108  26.931  1.00 102.61 ? 111 LEU   D N   1 
ATOM   6534  C  CA  . LEU   D  4  119 ? 12.772  -97.622  26.597  1.00 105.83 ? 111 LEU   D CA  1 
ATOM   6535  C  C   . LEU   D  4  119 ? 12.956  -96.183  27.097  1.00 107.82 ? 111 LEU   D C   1 
ATOM   6536  O  O   . LEU   D  4  119 ? 14.085  -95.841  27.498  1.00 108.05 ? 111 LEU   D O   1 
ATOM   6537  C  CB  . LEU   D  4  119 ? 13.000  -97.650  25.082  1.00 104.54 ? 111 LEU   D CB  1 
ATOM   6538  C  CG  . LEU   D  4  119 ? 13.267  -99.006  24.434  1.00 104.36 ? 111 LEU   D CG  1 
ATOM   6539  C  CD1 . LEU   D  4  119 ? 13.402  -98.838  22.928  1.00 104.94 ? 111 LEU   D CD1 1 
ATOM   6540  C  CD2 . LEU   D  4  119 ? 14.517  -99.661  25.001  1.00 104.07 ? 111 LEU   D CD2 1 
ATOM   6541  N  N   . ALA   D  4  120 ? 11.893  -95.372  27.033  1.00 117.55 ? 112 ALA   D N   1 
ATOM   6542  C  CA  . ALA   D  4  120 ? 11.934  -93.891  27.106  1.00 119.75 ? 112 ALA   D CA  1 
ATOM   6543  C  C   . ALA   D  4  120 ? 12.737  -93.415  28.325  1.00 119.17 ? 112 ALA   D C   1 
ATOM   6544  O  O   . ALA   D  4  120 ? 13.745  -92.710  28.111  1.00 125.76 ? 112 ALA   D O   1 
ATOM   6545  C  CB  . ALA   D  4  120 ? 10.530  -93.335  27.109  1.00 125.25 ? 112 ALA   D CB  1 
ATOM   6546  N  N   . LEU   D  4  121 ? 12.320  -93.773  29.547  1.00 116.33 ? 113 LEU   D N   1 
ATOM   6547  C  CA  . LEU   D  4  121 ? 12.943  -93.270  30.807  1.00 115.11 ? 113 LEU   D CA  1 
ATOM   6548  C  C   . LEU   D  4  121 ? 14.184  -94.099  31.178  1.00 110.90 ? 113 LEU   D C   1 
ATOM   6549  O  O   . LEU   D  4  121 ? 14.753  -93.828  32.254  1.00 104.73 ? 113 LEU   D O   1 
ATOM   6550  C  CB  . LEU   D  4  121 ? 11.927  -93.290  31.959  1.00 116.71 ? 113 LEU   D CB  1 
ATOM   6551  C  CG  . LEU   D  4  121 ? 10.859  -92.192  31.983  1.00 116.94 ? 113 LEU   D CG  1 
ATOM   6552  C  CD1 . LEU   D  4  121 ? 10.123  -92.208  33.315  1.00 119.50 ? 113 LEU   D CD1 1 
ATOM   6553  C  CD2 . LEU   D  4  121 ? 11.442  -90.807  31.741  1.00 114.34 ? 113 LEU   D CD2 1 
ATOM   6554  N  N   . ARG   D  4  122 ? 14.614  -95.048  30.336  1.00 114.31 ? 114 ARG   D N   1 
ATOM   6555  C  CA  . ARG   D  4  122 ? 15.858  -95.840  30.566  1.00 113.73 ? 114 ARG   D CA  1 
ATOM   6556  C  C   . ARG   D  4  122 ? 17.085  -94.992  30.196  1.00 108.77 ? 114 ARG   D C   1 
ATOM   6557  O  O   . ARG   D  4  122 ? 17.933  -95.476  29.425  1.00 107.74 ? 114 ARG   D O   1 
ATOM   6558  C  CB  . ARG   D  4  122 ? 15.834  -97.172  29.802  1.00 118.83 ? 114 ARG   D CB  1 
ATOM   6559  C  CG  . ARG   D  4  122 ? 15.417  -98.364  30.653  1.00 124.23 ? 114 ARG   D CG  1 
ATOM   6560  C  CD  . ARG   D  4  122 ? 15.872  -99.702  30.095  1.00 129.99 ? 114 ARG   D CD  1 
ATOM   6561  N  NE  . ARG   D  4  122 ? 14.889  -100.306 29.204  1.00 136.61 ? 114 ARG   D NE  1 
ATOM   6562  C  CZ  . ARG   D  4  122 ? 13.750  -100.880 29.592  1.00 142.73 ? 114 ARG   D CZ  1 
ATOM   6563  N  NH1 . ARG   D  4  122 ? 13.419  -100.928 30.873  1.00 141.91 ? 114 ARG   D NH1 1 
ATOM   6564  N  NH2 . ARG   D  4  122 ? 12.934  -101.398 28.689  1.00 150.21 ? 114 ARG   D NH2 1 
ATOM   6565  N  N   . PHE   D  4  123 ? 17.178  -93.778  30.744  1.00 108.26 ? 115 PHE   D N   1 
ATOM   6566  C  CA  . PHE   D  4  123 ? 18.348  -92.869  30.618  1.00 112.05 ? 115 PHE   D CA  1 
ATOM   6567  C  C   . PHE   D  4  123 ? 18.805  -92.471  32.024  1.00 112.49 ? 115 PHE   D C   1 
ATOM   6568  O  O   . PHE   D  4  123 ? 18.095  -92.785  32.999  1.00 112.93 ? 115 PHE   D O   1 
ATOM   6569  C  CB  . PHE   D  4  123 ? 18.007  -91.642  29.765  1.00 113.38 ? 115 PHE   D CB  1 
ATOM   6570  C  CG  . PHE   D  4  123 ? 17.085  -90.645  30.422  1.00 115.14 ? 115 PHE   D CG  1 
ATOM   6571  C  CD1 . PHE   D  4  123 ? 15.710  -90.816  30.379  1.00 115.82 ? 115 PHE   D CD1 1 
ATOM   6572  C  CD2 . PHE   D  4  123 ? 17.590  -89.534  31.083  1.00 112.53 ? 115 PHE   D CD2 1 
ATOM   6573  C  CE1 . PHE   D  4  123 ? 14.861  -89.903  30.986  1.00 114.87 ? 115 PHE   D CE1 1 
ATOM   6574  C  CE2 . PHE   D  4  123 ? 16.740  -88.622  31.691  1.00 111.75 ? 115 PHE   D CE2 1 
ATOM   6575  C  CZ  . PHE   D  4  123 ? 15.377  -88.808  31.642  1.00 113.45 ? 115 PHE   D CZ  1 
ATOM   6576  N  N   . GLY   D  4  124 ? 19.951  -91.793  32.116  1.00 117.73 ? 116 GLY   D N   1 
ATOM   6577  C  CA  . GLY   D  4  124 ? 20.520  -91.299  33.384  1.00 121.64 ? 116 GLY   D CA  1 
ATOM   6578  C  C   . GLY   D  4  124 ? 22.003  -91.601  33.495  1.00 122.43 ? 116 GLY   D C   1 
ATOM   6579  O  O   . GLY   D  4  124 ? 22.655  -91.773  32.443  1.00 118.29 ? 116 GLY   D O   1 
ATOM   6580  N  N   . GLU   D  4  125 ? 22.508  -91.669  34.730  1.00 127.94 ? 117 GLU   D N   1 
ATOM   6581  C  CA  . GLU   D  4  125 ? 23.950  -91.822  35.059  1.00 132.65 ? 117 GLU   D CA  1 
ATOM   6582  C  C   . GLU   D  4  125 ? 24.114  -92.982  36.050  1.00 135.56 ? 117 GLU   D C   1 
ATOM   6583  O  O   . GLU   D  4  125 ? 25.191  -93.060  36.675  1.00 137.97 ? 117 GLU   D O   1 
ATOM   6584  C  CB  . GLU   D  4  125 ? 24.482  -90.498  35.618  1.00 139.46 ? 117 GLU   D CB  1 
ATOM   6585  C  CG  . GLU   D  4  125 ? 25.914  -90.186  35.214  1.00 142.53 ? 117 GLU   D CG  1 
ATOM   6586  C  CD  . GLU   D  4  125 ? 26.109  -88.831  34.553  1.00 144.45 ? 117 GLU   D CD  1 
ATOM   6587  O  OE1 . GLU   D  4  125 ? 27.140  -88.186  34.824  1.00 144.83 ? 117 GLU   D OE1 1 
ATOM   6588  O  OE2 . GLU   D  4  125 ? 25.234  -88.425  33.758  1.00 145.50 ? 117 GLU   D OE2 1 
ATOM   6589  N  N   . LEU   D  4  133 ? 21.853  -98.314  30.655  1.00 116.02 ? 125 LEU   D N   1 
ATOM   6590  C  CA  . LEU   D  4  133 ? 20.936  -97.221  30.220  1.00 119.69 ? 125 LEU   D CA  1 
ATOM   6591  C  C   . LEU   D  4  133 ? 21.705  -96.173  29.399  1.00 116.42 ? 125 LEU   D C   1 
ATOM   6592  O  O   . LEU   D  4  133 ? 22.931  -96.032  29.598  1.00 115.50 ? 125 LEU   D O   1 
ATOM   6593  C  CB  . LEU   D  4  133 ? 20.221  -96.588  31.426  1.00 120.85 ? 125 LEU   D CB  1 
ATOM   6594  C  CG  . LEU   D  4  133 ? 21.026  -96.349  32.709  1.00 119.03 ? 125 LEU   D CG  1 
ATOM   6595  C  CD1 . LEU   D  4  133 ? 21.964  -95.158  32.574  1.00 120.60 ? 125 LEU   D CD1 1 
ATOM   6596  C  CD2 . LEU   D  4  133 ? 20.085  -96.133  33.887  1.00 115.25 ? 125 LEU   D CD2 1 
ATOM   6597  N  N   . MET   D  4  134 ? 20.996  -95.481  28.499  1.00 112.41 ? 126 MET   D N   1 
ATOM   6598  C  CA  . MET   D  4  134 ? 21.546  -94.446  27.579  1.00 108.76 ? 126 MET   D CA  1 
ATOM   6599  C  C   . MET   D  4  134 ? 21.743  -93.128  28.346  1.00 109.00 ? 126 MET   D C   1 
ATOM   6600  O  O   . MET   D  4  134 ? 21.303  -93.051  29.512  1.00 111.95 ? 126 MET   D O   1 
ATOM   6601  C  CB  . MET   D  4  134 ? 20.626  -94.238  26.367  1.00 104.31 ? 126 MET   D CB  1 
ATOM   6602  C  CG  . MET   D  4  134 ? 19.217  -93.780  26.706  1.00 102.72 ? 126 MET   D CG  1 
ATOM   6603  S  SD  . MET   D  4  134 ? 18.016  -94.272  25.442  1.00 99.64  ? 126 MET   D SD  1 
ATOM   6604  C  CE  . MET   D  4  134 ? 16.489  -93.728  26.206  1.00 102.21 ? 126 MET   D CE  1 
ATOM   6605  N  N   . SER   D  4  135 ? 22.397  -92.139  27.723  1.00 103.85 ? 127 SER   D N   1 
ATOM   6606  C  CA  . SER   D  4  135 ? 22.912  -90.909  28.385  1.00 101.34 ? 127 SER   D CA  1 
ATOM   6607  C  C   . SER   D  4  135 ? 21.831  -89.825  28.470  1.00 100.37 ? 127 SER   D C   1 
ATOM   6608  O  O   . SER   D  4  135 ? 21.911  -89.002  29.402  1.00 98.07  ? 127 SER   D O   1 
ATOM   6609  C  CB  . SER   D  4  135 ? 24.148  -90.394  27.688  1.00 100.20 ? 127 SER   D CB  1 
ATOM   6610  O  OG  . SER   D  4  135 ? 23.817  -89.613  26.550  1.00 101.60 ? 127 SER   D OG  1 
ATOM   6611  N  N   . ARG   D  4  136 ? 20.874  -89.814  27.534  1.00 100.11 ? 128 ARG   D N   1 
ATOM   6612  C  CA  . ARG   D  4  136 ? 19.831  -88.756  27.409  1.00 101.00 ? 128 ARG   D CA  1 
ATOM   6613  C  C   . ARG   D  4  136 ? 18.526  -89.366  26.905  1.00 100.39 ? 128 ARG   D C   1 
ATOM   6614  O  O   . ARG   D  4  136 ? 18.538  -90.426  26.283  1.00 102.63 ? 128 ARG   D O   1 
ATOM   6615  C  CB  . ARG   D  4  136 ? 20.298  -87.658  26.446  1.00 102.13 ? 128 ARG   D CB  1 
ATOM   6616  C  CG  . ARG   D  4  136 ? 20.730  -88.169  25.078  1.00 102.58 ? 128 ARG   D CG  1 
ATOM   6617  C  CD  . ARG   D  4  136 ? 20.979  -87.045  24.093  1.00 102.73 ? 128 ARG   D CD  1 
ATOM   6618  N  NE  . ARG   D  4  136 ? 21.250  -87.540  22.749  1.00 103.00 ? 128 ARG   D NE  1 
ATOM   6619  C  CZ  . ARG   D  4  136 ? 20.329  -87.937  21.870  1.00 102.92 ? 128 ARG   D CZ  1 
ATOM   6620  N  NH1 . ARG   D  4  136 ? 19.041  -87.916  22.180  1.00 103.82 ? 128 ARG   D NH1 1 
ATOM   6621  N  NH2 . ARG   D  4  136 ? 20.708  -88.368  20.677  1.00 103.16 ? 128 ARG   D NH2 1 
ATOM   6622  N  N   . PRO   D  4  137 ? 17.365  -88.707  27.124  1.00 97.24  ? 129 PRO   D N   1 
ATOM   6623  C  CA  . PRO   D  4  137 ? 16.105  -89.169  26.543  1.00 96.90  ? 129 PRO   D CA  1 
ATOM   6624  C  C   . PRO   D  4  137 ? 16.177  -89.119  25.012  1.00 94.78  ? 129 PRO   D C   1 
ATOM   6625  O  O   . PRO   D  4  137 ? 17.097  -88.511  24.490  1.00 94.83  ? 129 PRO   D O   1 
ATOM   6626  C  CB  . PRO   D  4  137 ? 15.044  -88.182  27.056  1.00 97.26  ? 129 PRO   D CB  1 
ATOM   6627  C  CG  . PRO   D  4  137 ? 15.709  -87.466  28.217  1.00 98.04  ? 129 PRO   D CG  1 
ATOM   6628  C  CD  . PRO   D  4  137 ? 17.195  -87.486  27.922  1.00 97.42  ? 129 PRO   D CD  1 
ATOM   6629  N  N   . PHE   D  4  138 ? 15.219  -89.755  24.335  1.00 97.74  ? 130 PHE   D N   1 
ATOM   6630  C  CA  . PHE   D  4  138 ? 15.044  -89.658  22.863  1.00 97.13  ? 130 PHE   D CA  1 
ATOM   6631  C  C   . PHE   D  4  138 ? 14.577  -88.239  22.522  1.00 93.94  ? 130 PHE   D C   1 
ATOM   6632  O  O   . PHE   D  4  138 ? 13.796  -87.659  23.301  1.00 94.07  ? 130 PHE   D O   1 
ATOM   6633  C  CB  . PHE   D  4  138 ? 14.048  -90.701  22.352  1.00 97.48  ? 130 PHE   D CB  1 
ATOM   6634  C  CG  . PHE   D  4  138 ? 14.460  -92.134  22.571  1.00 97.44  ? 130 PHE   D CG  1 
ATOM   6635  C  CD1 . PHE   D  4  138 ? 15.603  -92.643  21.974  1.00 96.14  ? 130 PHE   D CD1 1 
ATOM   6636  C  CD2 . PHE   D  4  138 ? 13.696  -92.976  23.365  1.00 97.80  ? 130 PHE   D CD2 1 
ATOM   6637  C  CE1 . PHE   D  4  138 ? 15.980  -93.962  22.175  1.00 96.01  ? 130 PHE   D CE1 1 
ATOM   6638  C  CE2 . PHE   D  4  138 ? 14.071  -94.295  23.561  1.00 97.96  ? 130 PHE   D CE2 1 
ATOM   6639  C  CZ  . PHE   D  4  138 ? 15.212  -94.785  22.966  1.00 97.29  ? 130 PHE   D CZ  1 
ATOM   6640  N  N   . GLY   D  4  139 ? 15.051  -87.698  21.397  1.00 92.54  ? 131 GLY   D N   1 
ATOM   6641  C  CA  . GLY   D  4  139 ? 14.634  -86.380  20.885  1.00 94.06  ? 131 GLY   D CA  1 
ATOM   6642  C  C   . GLY   D  4  139 ? 13.607  -86.508  19.776  1.00 95.55  ? 131 GLY   D C   1 
ATOM   6643  O  O   . GLY   D  4  139 ? 13.604  -85.641  18.874  1.00 95.57  ? 131 GLY   D O   1 
ATOM   6644  N  N   . VAL   D  4  140 ? 12.758  -87.541  19.839  1.00 94.33  ? 132 VAL   D N   1 
ATOM   6645  C  CA  . VAL   D  4  140 ? 11.747  -87.853  18.785  1.00 94.43  ? 132 VAL   D CA  1 
ATOM   6646  C  C   . VAL   D  4  140 ? 10.461  -88.372  19.443  1.00 93.49  ? 132 VAL   D C   1 
ATOM   6647  O  O   . VAL   D  4  140 ? 10.549  -89.168  20.399  1.00 91.68  ? 132 VAL   D O   1 
ATOM   6648  C  CB  . VAL   D  4  140 ? 12.312  -88.847  17.749  1.00 93.17  ? 132 VAL   D CB  1 
ATOM   6649  C  CG1 . VAL   D  4  140 ? 12.695  -90.178  18.376  1.00 93.03  ? 132 VAL   D CG1 1 
ATOM   6650  C  CG2 . VAL   D  4  140 ? 11.360  -89.056  16.581  1.00 92.44  ? 132 VAL   D CG2 1 
ATOM   6651  N  N   . ALA   D  4  141 ? 9.312   -87.910  18.941  1.00 95.10  ? 133 ALA   D N   1 
ATOM   6652  C  CA  . ALA   D  4  141 ? 7.956   -88.403  19.272  1.00 95.92  ? 133 ALA   D CA  1 
ATOM   6653  C  C   . ALA   D  4  141 ? 7.491   -89.331  18.147  1.00 95.81  ? 133 ALA   D C   1 
ATOM   6654  O  O   . ALA   D  4  141 ? 7.829   -89.052  16.980  1.00 93.47  ? 133 ALA   D O   1 
ATOM   6655  C  CB  . ALA   D  4  141 ? 7.006   -87.245  19.444  1.00 97.55  ? 133 ALA   D CB  1 
ATOM   6656  N  N   . LEU   D  4  142 ? 6.752   -90.390  18.488  1.00 97.67  ? 134 LEU   D N   1 
ATOM   6657  C  CA  . LEU   D  4  142 ? 6.236   -91.389  17.514  1.00 100.32 ? 134 LEU   D CA  1 
ATOM   6658  C  C   . LEU   D  4  142 ? 4.704   -91.383  17.525  1.00 100.66 ? 134 LEU   D C   1 
ATOM   6659  O  O   . LEU   D  4  142 ? 4.115   -91.361  18.625  1.00 103.26 ? 134 LEU   D O   1 
ATOM   6660  C  CB  . LEU   D  4  142 ? 6.761   -92.783  17.872  1.00 98.93  ? 134 LEU   D CB  1 
ATOM   6661  C  CG  . LEU   D  4  142 ? 8.277   -92.980  17.827  1.00 97.56  ? 134 LEU   D CG  1 
ATOM   6662  C  CD1 . LEU   D  4  142 ? 8.624   -94.432  18.113  1.00 97.05  ? 134 LEU   D CD1 1 
ATOM   6663  C  CD2 . LEU   D  4  142 ? 8.863   -92.553  16.488  1.00 98.77  ? 134 LEU   D CD2 1 
ATOM   6664  N  N   . LEU   D  4  143 ? 4.097   -91.398  16.335  1.00 102.15 ? 135 LEU   D N   1 
ATOM   6665  C  CA  . LEU   D  4  143 ? 2.672   -91.756  16.122  1.00 103.11 ? 135 LEU   D CA  1 
ATOM   6666  C  C   . LEU   D  4  143 ? 2.629   -93.230  15.715  1.00 100.18 ? 135 LEU   D C   1 
ATOM   6667  O  O   . LEU   D  4  143 ? 3.150   -93.547  14.631  1.00 104.02 ? 135 LEU   D O   1 
ATOM   6668  C  CB  . LEU   D  4  143 ? 2.063   -90.872  15.029  1.00 105.35 ? 135 LEU   D CB  1 
ATOM   6669  C  CG  . LEU   D  4  143 ? 1.926   -89.385  15.356  1.00 106.97 ? 135 LEU   D CG  1 
ATOM   6670  C  CD1 . LEU   D  4  143 ? 1.420   -88.617  14.144  1.00 108.62 ? 135 LEU   D CD1 1 
ATOM   6671  C  CD2 . LEU   D  4  143 ? 1.005   -89.158  16.546  1.00 107.20 ? 135 LEU   D CD2 1 
ATOM   6672  N  N   . ILE   D  4  144 ? 2.064   -94.092  16.564  1.00 98.36  ? 136 ILE   D N   1 
ATOM   6673  C  CA  . ILE   D  4  144 ? 1.946   -95.560  16.313  1.00 96.81  ? 136 ILE   D CA  1 
ATOM   6674  C  C   . ILE   D  4  144 ? 0.486   -95.878  15.975  1.00 93.84  ? 136 ILE   D C   1 
ATOM   6675  O  O   . ILE   D  4  144 ? -0.381  -95.686  16.848  1.00 95.09  ? 136 ILE   D O   1 
ATOM   6676  C  CB  . ILE   D  4  144 ? 2.461   -96.368  17.519  1.00 94.98  ? 136 ILE   D CB  1 
ATOM   6677  C  CG1 . ILE   D  4  144 ? 3.967   -96.170  17.711  1.00 93.62  ? 136 ILE   D CG1 1 
ATOM   6678  C  CG2 . ILE   D  4  144 ? 2.099   -97.839  17.374  1.00 96.19  ? 136 ILE   D CG2 1 
ATOM   6679  C  CD1 . ILE   D  4  144 ? 4.490   -96.627  19.052  1.00 92.99  ? 136 ILE   D CD1 1 
ATOM   6680  N  N   . ALA   D  4  145 ? 0.244   -96.355  14.752  1.00 92.69  ? 137 ALA   D N   1 
ATOM   6681  C  CA  . ALA   D  4  145 ? -1.095  -96.648  14.195  1.00 97.81  ? 137 ALA   D CA  1 
ATOM   6682  C  C   . ALA   D  4  145 ? -1.162  -98.125  13.800  1.00 97.63  ? 137 ALA   D C   1 
ATOM   6683  O  O   . ALA   D  4  145 ? -0.228  -98.588  13.119  1.00 101.35 ? 137 ALA   D O   1 
ATOM   6684  C  CB  . ALA   D  4  145 ? -1.351  -95.752  13.011  1.00 97.87  ? 137 ALA   D CB  1 
ATOM   6685  N  N   . GLY   D  4  146 ? -2.220  -98.833  14.208  1.00 100.94 ? 138 GLY   D N   1 
ATOM   6686  C  CA  . GLY   D  4  146 ? -2.370  -100.275 13.933  1.00 101.03 ? 138 GLY   D CA  1 
ATOM   6687  C  C   . GLY   D  4  146 ? -3.797  -100.769 14.088  1.00 101.17 ? 138 GLY   D C   1 
ATOM   6688  O  O   . GLY   D  4  146 ? -4.702  -99.937  14.306  1.00 100.24 ? 138 GLY   D O   1 
ATOM   6689  N  N   . HIS   D  4  147 ? -3.978  -102.087 13.964  1.00 101.06 ? 139 HIS   D N   1 
ATOM   6690  C  CA  . HIS   D  4  147 ? -5.258  -102.816 14.167  1.00 103.31 ? 139 HIS   D CA  1 
ATOM   6691  C  C   . HIS   D  4  147 ? -4.992  -104.135 14.902  1.00 102.73 ? 139 HIS   D C   1 
ATOM   6692  O  O   . HIS   D  4  147 ? -4.000  -104.808 14.567  1.00 103.39 ? 139 HIS   D O   1 
ATOM   6693  C  CB  . HIS   D  4  147 ? -5.955  -103.077 12.826  1.00 101.99 ? 139 HIS   D CB  1 
ATOM   6694  C  CG  . HIS   D  4  147 ? -7.249  -103.803 12.970  1.00 103.26 ? 139 HIS   D CG  1 
ATOM   6695  N  ND1 . HIS   D  4  147 ? -7.326  -105.181 12.959  1.00 101.47 ? 139 HIS   D ND1 1 
ATOM   6696  C  CD2 . HIS   D  4  147 ? -8.507  -103.351 13.154  1.00 104.26 ? 139 HIS   D CD2 1 
ATOM   6697  C  CE1 . HIS   D  4  147 ? -8.581  -105.547 13.117  1.00 104.39 ? 139 HIS   D CE1 1 
ATOM   6698  N  NE2 . HIS   D  4  147 ? -9.326  -104.442 13.239  1.00 105.33 ? 139 HIS   D NE2 1 
ATOM   6699  N  N   . ASP   D  4  148 ? -5.847  -104.477 15.869  1.00 103.74 ? 140 ASP   D N   1 
ATOM   6700  C  CA  . ASP   D  4  148 ? -5.923  -105.831 16.479  1.00 104.99 ? 140 ASP   D CA  1 
ATOM   6701  C  C   . ASP   D  4  148 ? -7.401  -106.199 16.649  1.00 108.36 ? 140 ASP   D C   1 
ATOM   6702  O  O   . ASP   D  4  148 ? -8.252  -105.292 16.564  1.00 107.73 ? 140 ASP   D O   1 
ATOM   6703  C  CB  . ASP   D  4  148 ? -5.128  -105.913 17.786  1.00 103.73 ? 140 ASP   D CB  1 
ATOM   6704  C  CG  . ASP   D  4  148 ? -5.634  -105.011 18.899  1.00 102.55 ? 140 ASP   D CG  1 
ATOM   6705  O  OD1 . ASP   D  4  148 ? -6.827  -105.115 19.247  1.00 102.68 ? 140 ASP   D OD1 1 
ATOM   6706  O  OD2 . ASP   D  4  148 ? -4.823  -104.222 19.423  1.00 100.72 ? 140 ASP   D OD2 1 
ATOM   6707  N  N   . ALA   D  4  149 ? -7.682  -107.483 16.884  1.00 112.37 ? 141 ALA   D N   1 
ATOM   6708  C  CA  . ALA   D  4  149 ? -9.042  -108.072 16.927  1.00 116.17 ? 141 ALA   D CA  1 
ATOM   6709  C  C   . ALA   D  4  149 ? -9.816  -107.562 18.151  1.00 117.29 ? 141 ALA   D C   1 
ATOM   6710  O  O   . ALA   D  4  149 ? -11.059 -107.527 18.077  1.00 118.28 ? 141 ALA   D O   1 
ATOM   6711  C  CB  . ALA   D  4  149 ? -8.948  -109.581 16.923  1.00 116.38 ? 141 ALA   D CB  1 
ATOM   6712  N  N   . ASP   D  4  150 ? -9.115  -107.175 19.223  1.00 117.68 ? 142 ASP   D N   1 
ATOM   6713  C  CA  . ASP   D  4  150 ? -9.718  -106.822 20.538  1.00 120.39 ? 142 ASP   D CA  1 
ATOM   6714  C  C   . ASP   D  4  150 ? -10.268 -105.389 20.504  1.00 121.50 ? 142 ASP   D C   1 
ATOM   6715  O  O   . ASP   D  4  150 ? -11.456 -105.215 20.847  1.00 125.49 ? 142 ASP   D O   1 
ATOM   6716  C  CB  . ASP   D  4  150 ? -8.709  -107.003 21.677  1.00 122.22 ? 142 ASP   D CB  1 
ATOM   6717  C  CG  . ASP   D  4  150 ? -8.242  -108.438 21.864  1.00 121.81 ? 142 ASP   D CG  1 
ATOM   6718  O  OD1 . ASP   D  4  150 ? -7.019  -108.667 21.800  1.00 119.71 ? 142 ASP   D OD1 1 
ATOM   6719  O  OD2 . ASP   D  4  150 ? -9.105  -109.313 22.080  1.00 128.84 ? 142 ASP   D OD2 1 
ATOM   6720  N  N   . ASP   D  4  151 ? -9.443  -104.405 20.121  1.00 119.54 ? 143 ASP   D N   1 
ATOM   6721  C  CA  . ASP   D  4  151 ? -9.755  -102.953 20.248  1.00 117.64 ? 143 ASP   D CA  1 
ATOM   6722  C  C   . ASP   D  4  151 ? -9.798  -102.266 18.872  1.00 115.19 ? 143 ASP   D C   1 
ATOM   6723  O  O   . ASP   D  4  151 ? -9.894  -101.019 18.849  1.00 114.62 ? 143 ASP   D O   1 
ATOM   6724  C  CB  . ASP   D  4  151 ? -8.754  -102.270 21.185  1.00 117.33 ? 143 ASP   D CB  1 
ATOM   6725  C  CG  . ASP   D  4  151 ? -8.961  -102.614 22.650  1.00 117.90 ? 143 ASP   D CG  1 
ATOM   6726  O  OD1 . ASP   D  4  151 ? -9.282  -103.783 22.940  1.00 118.19 ? 143 ASP   D OD1 1 
ATOM   6727  O  OD2 . ASP   D  4  151 ? -8.805  -101.707 23.489  1.00 121.97 ? 143 ASP   D OD2 1 
ATOM   6728  N  N   . GLY   D  4  152 ? -9.751  -103.031 17.775  1.00 110.41 ? 144 GLY   D N   1 
ATOM   6729  C  CA  . GLY   D  4  152 ? -9.869  -102.513 16.397  1.00 108.29 ? 144 GLY   D CA  1 
ATOM   6730  C  C   . GLY   D  4  152 ? -8.764  -101.527 16.050  1.00 106.17 ? 144 GLY   D C   1 
ATOM   6731  O  O   . GLY   D  4  152 ? -7.627  -101.723 16.520  1.00 99.36  ? 144 GLY   D O   1 
ATOM   6732  N  N   . TYR   D  4  153 ? -9.091  -100.502 15.253  1.00 109.30 ? 145 TYR   D N   1 
ATOM   6733  C  CA  . TYR   D  4  153 ? -8.146  -99.474  14.738  1.00 107.16 ? 145 TYR   D CA  1 
ATOM   6734  C  C   . TYR   D  4  153 ? -7.791  -98.490  15.853  1.00 106.44 ? 145 TYR   D C   1 
ATOM   6735  O  O   . TYR   D  4  153 ? -8.714  -97.967  16.507  1.00 106.78 ? 145 TYR   D O   1 
ATOM   6736  C  CB  . TYR   D  4  153 ? -8.743  -98.731  13.543  1.00 109.68 ? 145 TYR   D CB  1 
ATOM   6737  C  CG  . TYR   D  4  153 ? -8.938  -99.595  12.325  1.00 110.20 ? 145 TYR   D CG  1 
ATOM   6738  C  CD1 . TYR   D  4  153 ? -7.849  -100.070 11.613  1.00 111.63 ? 145 TYR   D CD1 1 
ATOM   6739  C  CD2 . TYR   D  4  153 ? -10.206 -99.949  11.892  1.00 109.52 ? 145 TYR   D CD2 1 
ATOM   6740  C  CE1 . TYR   D  4  153 ? -8.013  -100.871 10.495  1.00 113.32 ? 145 TYR   D CE1 1 
ATOM   6741  C  CE2 . TYR   D  4  153 ? -10.387 -100.745 10.774  1.00 110.95 ? 145 TYR   D CE2 1 
ATOM   6742  C  CZ  . TYR   D  4  153 ? -9.287  -101.207 10.071  1.00 114.96 ? 145 TYR   D CZ  1 
ATOM   6743  O  OH  . TYR   D  4  153 ? -9.463  -101.993 8.968   1.00 116.59 ? 145 TYR   D OH  1 
ATOM   6744  N  N   . GLN   D  4  154 ? -6.491  -98.244  16.039  1.00 106.24 ? 146 GLN   D N   1 
ATOM   6745  C  CA  . GLN   D  4  154 ? -5.936  -97.440  17.159  1.00 107.27 ? 146 GLN   D CA  1 
ATOM   6746  C  C   . GLN   D  4  154 ? -4.807  -96.542  16.643  1.00 106.89 ? 146 GLN   D C   1 
ATOM   6747  O  O   . GLN   D  4  154 ? -4.025  -97.001  15.783  1.00 102.17 ? 146 GLN   D O   1 
ATOM   6748  C  CB  . GLN   D  4  154 ? -5.413  -98.357  18.267  1.00 106.85 ? 146 GLN   D CB  1 
ATOM   6749  C  CG  . GLN   D  4  154 ? -6.497  -99.192  18.935  1.00 108.47 ? 146 GLN   D CG  1 
ATOM   6750  C  CD  . GLN   D  4  154 ? -5.952  -100.445 19.576  1.00 109.16 ? 146 GLN   D CD  1 
ATOM   6751  O  OE1 . GLN   D  4  154 ? -6.052  -101.539 19.025  1.00 107.83 ? 146 GLN   D OE1 1 
ATOM   6752  N  NE2 . GLN   D  4  154 ? -5.361  -100.293 20.750  1.00 110.58 ? 146 GLN   D NE2 1 
ATOM   6753  N  N   . LEU   D  4  155 ? -4.744  -95.314  17.165  1.00 108.47 ? 147 LEU   D N   1 
ATOM   6754  C  CA  . LEU   D  4  155 ? -3.628  -94.352  16.972  1.00 107.18 ? 147 LEU   D CA  1 
ATOM   6755  C  C   . LEU   D  4  155 ? -3.088  -93.988  18.357  1.00 105.29 ? 147 LEU   D C   1 
ATOM   6756  O  O   . LEU   D  4  155 ? -3.909  -93.699  19.249  1.00 106.79 ? 147 LEU   D O   1 
ATOM   6757  C  CB  . LEU   D  4  155 ? -4.151  -93.124  16.216  1.00 107.85 ? 147 LEU   D CB  1 
ATOM   6758  C  CG  . LEU   D  4  155 ? -3.161  -91.975  16.021  1.00 107.14 ? 147 LEU   D CG  1 
ATOM   6759  C  CD1 . LEU   D  4  155 ? -2.081  -92.343  15.015  1.00 105.83 ? 147 LEU   D CD1 1 
ATOM   6760  C  CD2 . LEU   D  4  155 ? -3.887  -90.714  15.582  1.00 108.12 ? 147 LEU   D CD2 1 
ATOM   6761  N  N   . PHE   D  4  156 ? -1.765  -94.041  18.533  1.00 106.44 ? 148 PHE   D N   1 
ATOM   6762  C  CA  . PHE   D  4  156 ? -1.066  -93.729  19.806  1.00 108.24 ? 148 PHE   D CA  1 
ATOM   6763  C  C   . PHE   D  4  156 ? 0.015   -92.672  19.557  1.00 108.45 ? 148 PHE   D C   1 
ATOM   6764  O  O   . PHE   D  4  156 ? 0.730   -92.762  18.537  1.00 105.83 ? 148 PHE   D O   1 
ATOM   6765  C  CB  . PHE   D  4  156 ? -0.453  -94.993  20.413  1.00 106.36 ? 148 PHE   D CB  1 
ATOM   6766  C  CG  . PHE   D  4  156 ? -1.443  -95.941  21.039  1.00 107.51 ? 148 PHE   D CG  1 
ATOM   6767  C  CD1 . PHE   D  4  156 ? -1.969  -95.692  22.298  1.00 107.34 ? 148 PHE   D CD1 1 
ATOM   6768  C  CD2 . PHE   D  4  156 ? -1.843  -97.089  20.374  1.00 107.60 ? 148 PHE   D CD2 1 
ATOM   6769  C  CE1 . PHE   D  4  156 ? -2.877  -96.567  22.875  1.00 106.56 ? 148 PHE   D CE1 1 
ATOM   6770  C  CE2 . PHE   D  4  156 ? -2.752  -97.963  20.951  1.00 107.12 ? 148 PHE   D CE2 1 
ATOM   6771  C  CZ  . PHE   D  4  156 ? -3.269  -97.700  22.200  1.00 105.37 ? 148 PHE   D CZ  1 
ATOM   6772  N  N   . HIS   D  4  157 ? 0.114   -91.699  20.468  1.00 108.29 ? 149 HIS   D N   1 
ATOM   6773  C  CA  . HIS   D  4  157 ? 1.222   -90.712  20.556  1.00 108.33 ? 149 HIS   D CA  1 
ATOM   6774  C  C   . HIS   D  4  157 ? 2.179   -91.168  21.662  1.00 107.30 ? 149 HIS   D C   1 
ATOM   6775  O  O   . HIS   D  4  157 ? 1.754   -91.173  22.830  1.00 108.22 ? 149 HIS   D O   1 
ATOM   6776  C  CB  . HIS   D  4  157 ? 0.663   -89.301  20.786  1.00 106.59 ? 149 HIS   D CB  1 
ATOM   6777  C  CG  . HIS   D  4  157 ? 1.712   -88.250  20.937  1.00 108.34 ? 149 HIS   D CG  1 
ATOM   6778  N  ND1 . HIS   D  4  157 ? 1.595   -87.216  21.845  1.00 110.39 ? 149 HIS   D ND1 1 
ATOM   6779  C  CD2 . HIS   D  4  157 ? 2.900   -88.079  20.318  1.00 108.02 ? 149 HIS   D CD2 1 
ATOM   6780  C  CE1 . HIS   D  4  157 ? 2.662   -86.447  21.771  1.00 111.70 ? 149 HIS   D CE1 1 
ATOM   6781  N  NE2 . HIS   D  4  157 ? 3.479   -86.957  20.842  1.00 109.54 ? 149 HIS   D NE2 1 
ATOM   6782  N  N   . ALA   D  4  158 ? 3.403   -91.567  21.295  1.00 107.61 ? 150 ALA   D N   1 
ATOM   6783  C  CA  . ALA   D  4  158 ? 4.462   -92.046  22.216  1.00 109.44 ? 150 ALA   D CA  1 
ATOM   6784  C  C   . ALA   D  4  158 ? 5.527   -90.958  22.397  1.00 108.52 ? 150 ALA   D C   1 
ATOM   6785  O  O   . ALA   D  4  158 ? 6.203   -90.616  21.404  1.00 105.86 ? 150 ALA   D O   1 
ATOM   6786  C  CB  . ALA   D  4  158 ? 5.071   -93.320  21.685  1.00 110.84 ? 150 ALA   D CB  1 
ATOM   6787  N  N   . GLU   D  4  159 ? 5.682   -90.458  23.627  1.00 109.39 ? 151 GLU   D N   1 
ATOM   6788  C  CA  . GLU   D  4  159 ? 6.596   -89.336  23.971  1.00 108.66 ? 151 GLU   D CA  1 
ATOM   6789  C  C   . GLU   D  4  159 ? 7.849   -89.876  24.658  1.00 108.66 ? 151 GLU   D C   1 
ATOM   6790  O  O   . GLU   D  4  159 ? 7.838   -90.977  25.207  1.00 103.10 ? 151 GLU   D O   1 
ATOM   6791  C  CB  . GLU   D  4  159 ? 5.885   -88.323  24.869  1.00 110.95 ? 151 GLU   D CB  1 
ATOM   6792  C  CG  . GLU   D  4  159 ? 4.932   -87.411  24.120  1.00 112.06 ? 151 GLU   D CG  1 
ATOM   6793  C  CD  . GLU   D  4  159 ? 4.206   -86.421  25.014  1.00 115.89 ? 151 GLU   D CD  1 
ATOM   6794  O  OE1 . GLU   D  4  159 ? 4.173   -85.221  24.666  1.00 118.96 ? 151 GLU   D OE1 1 
ATOM   6795  O  OE2 . GLU   D  4  159 ? 3.677   -86.853  26.057  1.00 115.75 ? 151 GLU   D OE2 1 
ATOM   6796  N  N   . PRO   D  4  160 ? 8.969   -89.113  24.628  1.00 107.34 ? 152 PRO   D N   1 
ATOM   6797  C  CA  . PRO   D  4  160 ? 10.171  -89.443  25.400  1.00 106.11 ? 152 PRO   D CA  1 
ATOM   6798  C  C   . PRO   D  4  160 ? 10.031  -89.394  26.931  1.00 106.06 ? 152 PRO   D C   1 
ATOM   6799  O  O   . PRO   D  4  160 ? 11.003  -89.708  27.597  1.00 105.30 ? 152 PRO   D O   1 
ATOM   6800  C  CB  . PRO   D  4  160 ? 11.183  -88.358  24.996  1.00 105.87 ? 152 PRO   D CB  1 
ATOM   6801  C  CG  . PRO   D  4  160 ? 10.671  -87.833  23.675  1.00 105.29 ? 152 PRO   D CG  1 
ATOM   6802  C  CD  . PRO   D  4  160 ? 9.165   -87.929  23.778  1.00 106.35 ? 152 PRO   D CD  1 
ATOM   6803  N  N   . SER   D  4  161 ? 8.869   -88.968  27.442  1.00 110.37 ? 153 SER   D N   1 
ATOM   6804  C  CA  . SER   D  4  161 ? 8.501   -88.985  28.885  1.00 111.72 ? 153 SER   D CA  1 
ATOM   6805  C  C   . SER   D  4  161 ? 8.208   -90.417  29.348  1.00 112.61 ? 153 SER   D C   1 
ATOM   6806  O  O   . SER   D  4  161 ? 8.262   -90.660  30.570  1.00 114.76 ? 153 SER   D O   1 
ATOM   6807  C  CB  . SER   D  4  161 ? 7.315   -88.098  29.151  1.00 113.80 ? 153 SER   D CB  1 
ATOM   6808  O  OG  . SER   D  4  161 ? 6.194   -88.510  28.381  1.00 115.54 ? 153 SER   D OG  1 
ATOM   6809  N  N   . GLY   D  4  162 ? 7.889   -91.315  28.409  1.00 111.56 ? 154 GLY   D N   1 
ATOM   6810  C  CA  . GLY   D  4  162 ? 7.451   -92.697  28.686  1.00 111.13 ? 154 GLY   D CA  1 
ATOM   6811  C  C   . GLY   D  4  162 ? 5.937   -92.794  28.761  1.00 109.34 ? 154 GLY   D C   1 
ATOM   6812  O  O   . GLY   D  4  162 ? 5.433   -93.877  29.114  1.00 106.55 ? 154 GLY   D O   1 
ATOM   6813  N  N   . THR   D  4  163 ? 5.240   -91.698  28.442  1.00 112.19 ? 155 THR   D N   1 
ATOM   6814  C  CA  . THR   D  4  163 ? 3.757   -91.609  28.412  1.00 109.31 ? 155 THR   D CA  1 
ATOM   6815  C  C   . THR   D  4  163 ? 3.278   -91.808  26.972  1.00 107.20 ? 155 THR   D C   1 
ATOM   6816  O  O   . THR   D  4  163 ? 3.971   -91.341  26.046  1.00 107.76 ? 155 THR   D O   1 
ATOM   6817  C  CB  . THR   D  4  163 ? 3.258   -90.272  28.975  1.00 109.75 ? 155 THR   D CB  1 
ATOM   6818  O  OG1 . THR   D  4  163 ? 3.920   -90.028  30.217  1.00 108.57 ? 155 THR   D OG1 1 
ATOM   6819  C  CG2 . THR   D  4  163 ? 1.760   -90.256  29.183  1.00 111.71 ? 155 THR   D CG2 1 
ATOM   6820  N  N   . PHE   D  4  164 ? 2.144   -92.488  26.805  1.00 106.33 ? 156 PHE   D N   1 
ATOM   6821  C  CA  . PHE   D  4  164 ? 1.423   -92.628  25.514  1.00 108.10 ? 156 PHE   D CA  1 
ATOM   6822  C  C   . PHE   D  4  164 ? -0.073  -92.424  25.761  1.00 107.67 ? 156 PHE   D C   1 
ATOM   6823  O  O   . PHE   D  4  164 ? -0.620  -92.975  26.738  1.00 109.92 ? 156 PHE   D O   1 
ATOM   6824  C  CB  . PHE   D  4  164 ? 1.713   -93.980  24.855  1.00 107.10 ? 156 PHE   D CB  1 
ATOM   6825  C  CG  . PHE   D  4  164 ? 1.298   -95.181  25.667  1.00 106.47 ? 156 PHE   D CG  1 
ATOM   6826  C  CD1 . PHE   D  4  164 ? 2.057   -95.599  26.747  1.00 105.74 ? 156 PHE   D CD1 1 
ATOM   6827  C  CD2 . PHE   D  4  164 ? 0.147   -95.890  25.355  1.00 104.96 ? 156 PHE   D CD2 1 
ATOM   6828  C  CE1 . PHE   D  4  164 ? 1.675   -96.696  27.500  1.00 107.48 ? 156 PHE   D CE1 1 
ATOM   6829  C  CE2 . PHE   D  4  164 ? -0.233  -96.990  26.107  1.00 105.41 ? 156 PHE   D CE2 1 
ATOM   6830  C  CZ  . PHE   D  4  164 ? 0.532   -97.392  27.177  1.00 107.74 ? 156 PHE   D CZ  1 
ATOM   6831  N  N   . TYR   D  4  165 ? -0.699  -91.623  24.901  1.00 108.50 ? 157 TYR   D N   1 
ATOM   6832  C  CA  . TYR   D  4  165 ? -2.164  -91.397  24.851  1.00 110.54 ? 157 TYR   D CA  1 
ATOM   6833  C  C   . TYR   D  4  165 ? -2.703  -92.056  23.582  1.00 107.91 ? 157 TYR   D C   1 
ATOM   6834  O  O   . TYR   D  4  165 ? -2.000  -92.023  22.553  1.00 102.86 ? 157 TYR   D O   1 
ATOM   6835  C  CB  . TYR   D  4  165 ? -2.475  -89.899  24.857  1.00 112.11 ? 157 TYR   D CB  1 
ATOM   6836  C  CG  . TYR   D  4  165 ? -2.520  -89.260  26.221  1.00 115.12 ? 157 TYR   D CG  1 
ATOM   6837  C  CD1 . TYR   D  4  165 ? -3.675  -89.299  26.984  1.00 116.97 ? 157 TYR   D CD1 1 
ATOM   6838  C  CD2 . TYR   D  4  165 ? -1.419  -88.600  26.744  1.00 115.56 ? 157 TYR   D CD2 1 
ATOM   6839  C  CE1 . TYR   D  4  165 ? -3.735  -88.708  28.235  1.00 119.01 ? 157 TYR   D CE1 1 
ATOM   6840  C  CE2 . TYR   D  4  165 ? -1.462  -88.003  27.993  1.00 117.84 ? 157 TYR   D CE2 1 
ATOM   6841  C  CZ  . TYR   D  4  165 ? -2.625  -88.057  28.742  1.00 120.58 ? 157 TYR   D CZ  1 
ATOM   6842  O  OH  . TYR   D  4  165 ? -2.682  -87.473  29.975  1.00 123.25 ? 157 TYR   D OH  1 
ATOM   6843  N  N   . ARG   D  4  166 ? -3.898  -92.646  23.656  1.00 110.25 ? 158 ARG   D N   1 
ATOM   6844  C  CA  . ARG   D  4  166 ? -4.678  -93.024  22.450  1.00 112.57 ? 158 ARG   D CA  1 
ATOM   6845  C  C   . ARG   D  4  166 ? -5.342  -91.749  21.922  1.00 112.80 ? 158 ARG   D C   1 
ATOM   6846  O  O   . ARG   D  4  166 ? -5.795  -90.946  22.755  1.00 110.94 ? 158 ARG   D O   1 
ATOM   6847  C  CB  . ARG   D  4  166 ? -5.720  -94.106  22.749  1.00 113.81 ? 158 ARG   D CB  1 
ATOM   6848  C  CG  . ARG   D  4  166 ? -6.265  -94.772  21.495  1.00 115.00 ? 158 ARG   D CG  1 
ATOM   6849  C  CD  . ARG   D  4  166 ? -7.318  -95.825  21.774  1.00 116.34 ? 158 ARG   D CD  1 
ATOM   6850  N  NE  . ARG   D  4  166 ? -8.120  -96.095  20.586  1.00 117.87 ? 158 ARG   D NE  1 
ATOM   6851  C  CZ  . ARG   D  4  166 ? -9.060  -97.032  20.491  1.00 120.05 ? 158 ARG   D CZ  1 
ATOM   6852  N  NH1 . ARG   D  4  166 ? -9.330  -97.823  21.517  1.00 122.14 ? 158 ARG   D NH1 1 
ATOM   6853  N  NH2 . ARG   D  4  166 ? -9.725  -97.181  19.358  1.00 123.57 ? 158 ARG   D NH2 1 
ATOM   6854  N  N   . TYR   D  4  167 ? -5.371  -91.568  20.599  1.00 112.70 ? 159 TYR   D N   1 
ATOM   6855  C  CA  . TYR   D  4  167 ? -5.948  -90.383  19.913  1.00 110.00 ? 159 TYR   D CA  1 
ATOM   6856  C  C   . TYR   D  4  167 ? -6.895  -90.846  18.803  1.00 112.46 ? 159 TYR   D C   1 
ATOM   6857  O  O   . TYR   D  4  167 ? -6.612  -91.873  18.160  1.00 112.26 ? 159 TYR   D O   1 
ATOM   6858  C  CB  . TYR   D  4  167 ? -4.841  -89.498  19.335  1.00 108.53 ? 159 TYR   D CB  1 
ATOM   6859  C  CG  . TYR   D  4  167 ? -4.234  -88.518  20.307  1.00 107.44 ? 159 TYR   D CG  1 
ATOM   6860  C  CD1 . TYR   D  4  167 ? -3.058  -88.810  20.976  1.00 108.32 ? 159 TYR   D CD1 1 
ATOM   6861  C  CD2 . TYR   D  4  167 ? -4.822  -87.287  20.545  1.00 109.00 ? 159 TYR   D CD2 1 
ATOM   6862  C  CE1 . TYR   D  4  167 ? -2.486  -87.912  21.863  1.00 106.65 ? 159 TYR   D CE1 1 
ATOM   6863  C  CE2 . TYR   D  4  167 ? -4.265  -86.377  21.429  1.00 109.57 ? 159 TYR   D CE2 1 
ATOM   6864  C  CZ  . TYR   D  4  167 ? -3.093  -86.693  22.094  1.00 106.47 ? 159 TYR   D CZ  1 
ATOM   6865  O  OH  . TYR   D  4  167 ? -2.519  -85.821  22.970  1.00 108.49 ? 159 TYR   D OH  1 
ATOM   6866  N  N   . ASN   D  4  168 ? -7.989  -90.109  18.598  1.00 109.40 ? 160 ASN   D N   1 
ATOM   6867  C  CA  . ASN   D  4  168 ? -8.854  -90.227  17.395  1.00 110.08 ? 160 ASN   D CA  1 
ATOM   6868  C  C   . ASN   D  4  168 ? -8.119  -89.579  16.219  1.00 110.59 ? 160 ASN   D C   1 
ATOM   6869  O  O   . ASN   D  4  168 ? -8.253  -90.073  15.084  1.00 114.27 ? 160 ASN   D O   1 
ATOM   6870  C  CB  . ASN   D  4  168 ? -10.225 -89.584  17.608  1.00 110.11 ? 160 ASN   D CB  1 
ATOM   6871  C  CG  . ASN   D  4  168 ? -11.114 -90.346  18.568  1.00 111.11 ? 160 ASN   D CG  1 
ATOM   6872  O  OD1 . ASN   D  4  168 ? -11.749 -89.744  19.430  1.00 114.04 ? 160 ASN   D OD1 1 
ATOM   6873  N  ND2 . ASN   D  4  168 ? -11.184 -91.661  18.427  1.00 110.22 ? 160 ASN   D ND2 1 
ATOM   6874  N  N   . ALA   D  4  169 ? -7.376  -88.507  16.504  1.00 109.75 ? 161 ALA   D N   1 
ATOM   6875  C  CA  . ALA   D  4  169 ? -6.482  -87.796  15.563  1.00 109.48 ? 161 ALA   D CA  1 
ATOM   6876  C  C   . ALA   D  4  169 ? -5.418  -87.042  16.367  1.00 108.04 ? 161 ALA   D C   1 
ATOM   6877  O  O   . ALA   D  4  169 ? -5.714  -86.655  17.515  1.00 109.25 ? 161 ALA   D O   1 
ATOM   6878  C  CB  . ALA   D  4  169 ? -7.290  -86.867  14.693  1.00 111.39 ? 161 ALA   D CB  1 
ATOM   6879  N  N   . LYS   D  4  170 ? -4.224  -86.850  15.801  1.00 106.16 ? 162 LYS   D N   1 
ATOM   6880  C  CA  . LYS   D  4  170 ? -3.094  -86.189  16.506  1.00 107.20 ? 162 LYS   D CA  1 
ATOM   6881  C  C   . LYS   D  4  170 ? -2.048  -85.696  15.501  1.00 105.72 ? 162 LYS   D C   1 
ATOM   6882  O  O   . LYS   D  4  170 ? -1.670  -86.473  14.602  1.00 104.36 ? 162 LYS   D O   1 
ATOM   6883  C  CB  . LYS   D  4  170 ? -2.469  -87.158  17.514  1.00 106.68 ? 162 LYS   D CB  1 
ATOM   6884  C  CG  . LYS   D  4  170 ? -1.276  -86.616  18.289  1.00 107.87 ? 162 LYS   D CG  1 
ATOM   6885  C  CD  . LYS   D  4  170 ? -1.580  -85.377  19.099  1.00 112.27 ? 162 LYS   D CD  1 
ATOM   6886  C  CE  . LYS   D  4  170 ? -0.456  -85.016  20.046  1.00 116.26 ? 162 LYS   D CE  1 
ATOM   6887  N  NZ  . LYS   D  4  170 ? -0.677  -83.700  20.694  1.00 119.88 ? 162 LYS   D NZ  1 
ATOM   6888  N  N   . ALA   D  4  171 ? -1.607  -84.447  15.674  1.00 106.92 ? 163 ALA   D N   1 
ATOM   6889  C  CA  . ALA   D  4  171 ? -0.481  -83.815  14.950  1.00 106.13 ? 163 ALA   D CA  1 
ATOM   6890  C  C   . ALA   D  4  171 ? 0.688   -83.614  15.921  1.00 102.34 ? 163 ALA   D C   1 
ATOM   6891  O  O   . ALA   D  4  171 ? 0.433   -83.230  17.080  1.00 96.44  ? 163 ALA   D O   1 
ATOM   6892  C  CB  . ALA   D  4  171 ? -0.927  -82.504  14.350  1.00 108.76 ? 163 ALA   D CB  1 
ATOM   6893  N  N   . ILE   D  4  172 ? 1.915   -83.869  15.458  1.00 102.38 ? 164 ILE   D N   1 
ATOM   6894  C  CA  . ILE   D  4  172 ? 3.179   -83.636  16.219  1.00 103.82 ? 164 ILE   D CA  1 
ATOM   6895  C  C   . ILE   D  4  172 ? 4.168   -82.893  15.316  1.00 106.20 ? 164 ILE   D C   1 
ATOM   6896  O  O   . ILE   D  4  172 ? 4.154   -83.144  14.094  1.00 101.19 ? 164 ILE   D O   1 
ATOM   6897  C  CB  . ILE   D  4  172 ? 3.779   -84.956  16.745  1.00 103.82 ? 164 ILE   D CB  1 
ATOM   6898  C  CG1 . ILE   D  4  172 ? 3.883   -86.018  15.647  1.00 103.84 ? 164 ILE   D CG1 1 
ATOM   6899  C  CG2 . ILE   D  4  172 ? 2.994   -85.460  17.944  1.00 103.26 ? 164 ILE   D CG2 1 
ATOM   6900  C  CD1 . ILE   D  4  172 ? 4.811   -87.164  15.981  1.00 104.26 ? 164 ILE   D CD1 1 
ATOM   6901  N  N   . GLY   D  4  173 ? 4.990   -82.022  15.910  1.00 110.87 ? 165 GLY   D N   1 
ATOM   6902  C  CA  . GLY   D  4  173 ? 6.036   -81.246  15.213  1.00 113.09 ? 165 GLY   D CA  1 
ATOM   6903  C  C   . GLY   D  4  173 ? 5.764   -79.751  15.242  1.00 113.64 ? 165 GLY   D C   1 
ATOM   6904  O  O   . GLY   D  4  173 ? 4.944   -79.303  16.067  1.00 110.97 ? 165 GLY   D O   1 
ATOM   6905  N  N   . SER   D  4  174 ? 6.435   -79.003  14.365  1.00 114.02 ? 166 SER   D N   1 
ATOM   6906  C  CA  . SER   D  4  174 ? 6.427   -77.518  14.318  1.00 115.00 ? 166 SER   D CA  1 
ATOM   6907  C  C   . SER   D  4  174 ? 5.002   -76.981  14.130  1.00 117.83 ? 166 SER   D C   1 
ATOM   6908  O  O   . SER   D  4  174 ? 4.660   -75.983  14.801  1.00 125.79 ? 166 SER   D O   1 
ATOM   6909  C  CB  . SER   D  4  174 ? 7.352   -77.017  13.241  1.00 115.36 ? 166 SER   D CB  1 
ATOM   6910  O  OG  . SER   D  4  174 ? 7.138   -77.724  12.028  1.00 112.87 ? 166 SER   D OG  1 
ATOM   6911  N  N   . GLY   D  4  175 ? 4.204   -77.611  13.264  1.00 113.20 ? 167 GLY   D N   1 
ATOM   6912  C  CA  . GLY   D  4  175 ? 2.859   -77.126  12.901  1.00 114.33 ? 167 GLY   D CA  1 
ATOM   6913  C  C   . GLY   D  4  175 ? 1.758   -77.738  13.753  1.00 114.33 ? 167 GLY   D C   1 
ATOM   6914  O  O   . GLY   D  4  175 ? 0.589   -77.614  13.351  1.00 117.64 ? 167 GLY   D O   1 
ATOM   6915  N  N   . SER   D  4  176 ? 2.095   -78.345  14.896  1.00 113.68 ? 168 SER   D N   1 
ATOM   6916  C  CA  . SER   D  4  176 ? 1.198   -79.252  15.665  1.00 113.47 ? 168 SER   D CA  1 
ATOM   6917  C  C   . SER   D  4  176 ? 0.019   -78.496  16.293  1.00 118.81 ? 168 SER   D C   1 
ATOM   6918  O  O   . SER   D  4  176 ? -1.126  -78.927  16.065  1.00 118.44 ? 168 SER   D O   1 
ATOM   6919  C  CB  . SER   D  4  176 ? 1.958   -80.025  16.712  1.00 113.26 ? 168 SER   D CB  1 
ATOM   6920  O  OG  . SER   D  4  176 ? 2.475   -79.157  17.709  1.00 111.30 ? 168 SER   D OG  1 
ATOM   6921  N  N   . GLU   D  4  177 ? 0.273   -77.433  17.065  1.00 120.17 ? 169 GLU   D N   1 
ATOM   6922  C  CA  . GLU   D  4  177 ? -0.770  -76.753  17.886  1.00 124.51 ? 169 GLU   D CA  1 
ATOM   6923  C  C   . GLU   D  4  177 ? -1.835  -76.148  16.958  1.00 123.65 ? 169 GLU   D C   1 
ATOM   6924  O  O   . GLU   D  4  177 ? -3.022  -76.170  17.342  1.00 124.08 ? 169 GLU   D O   1 
ATOM   6925  C  CB  . GLU   D  4  177 ? -0.152  -75.718  18.832  1.00 126.83 ? 169 GLU   D CB  1 
ATOM   6926  C  CG  . GLU   D  4  177 ? -0.109  -74.302  18.281  1.00 129.45 ? 169 GLU   D CG  1 
ATOM   6927  C  CD  . GLU   D  4  177 ? 0.521   -73.281  19.213  1.00 132.13 ? 169 GLU   D CD  1 
ATOM   6928  O  OE1 . GLU   D  4  177 ? 1.590   -73.583  19.780  1.00 138.73 ? 169 GLU   D OE1 1 
ATOM   6929  O  OE2 . GLU   D  4  177 ? -0.062  -72.187  19.374  1.00 131.77 ? 169 GLU   D OE2 1 
ATOM   6930  N  N   . GLY   D  4  178 ? -1.425  -75.639  15.790  1.00 121.72 ? 170 GLY   D N   1 
ATOM   6931  C  CA  . GLY   D  4  178 ? -2.324  -75.113  14.743  1.00 120.74 ? 170 GLY   D CA  1 
ATOM   6932  C  C   . GLY   D  4  178 ? -3.095  -76.224  14.047  1.00 118.94 ? 170 GLY   D C   1 
ATOM   6933  O  O   . GLY   D  4  178 ? -4.311  -76.053  13.834  1.00 114.31 ? 170 GLY   D O   1 
ATOM   6934  N  N   . ALA   D  4  179 ? -2.410  -77.322  13.704  1.00 117.90 ? 171 ALA   D N   1 
ATOM   6935  C  CA  . ALA   D  4  179 ? -2.976  -78.514  13.026  1.00 117.49 ? 171 ALA   D CA  1 
ATOM   6936  C  C   . ALA   D  4  179 ? -3.927  -79.262  13.970  1.00 118.42 ? 171 ALA   D C   1 
ATOM   6937  O  O   . ALA   D  4  179 ? -4.955  -79.770  13.478  1.00 122.69 ? 171 ALA   D O   1 
ATOM   6938  C  CB  . ALA   D  4  179 ? -1.866  -79.417  12.541  1.00 115.33 ? 171 ALA   D CB  1 
ATOM   6939  N  N   . GLN   D  4  180 ? -3.598  -79.332  15.266  1.00 118.58 ? 172 GLN   D N   1 
ATOM   6940  C  CA  . GLN   D  4  180 ? -4.397  -80.050  16.299  1.00 122.00 ? 172 GLN   D CA  1 
ATOM   6941  C  C   . GLN   D  4  180 ? -5.737  -79.330  16.494  1.00 122.00 ? 172 GLN   D C   1 
ATOM   6942  O  O   . GLN   D  4  180 ? -6.762  -80.029  16.629  1.00 118.39 ? 172 GLN   D O   1 
ATOM   6943  C  CB  . GLN   D  4  180 ? -3.629  -80.145  17.621  1.00 123.34 ? 172 GLN   D CB  1 
ATOM   6944  C  CG  . GLN   D  4  180 ? -4.302  -81.025  18.671  1.00 124.61 ? 172 GLN   D CG  1 
ATOM   6945  C  CD  . GLN   D  4  180 ? -4.269  -82.497  18.331  1.00 122.08 ? 172 GLN   D CD  1 
ATOM   6946  O  OE1 . GLN   D  4  180 ? -3.572  -82.934  17.417  1.00 114.62 ? 172 GLN   D OE1 1 
ATOM   6947  N  NE2 . GLN   D  4  180 ? -5.026  -83.283  19.081  1.00 121.96 ? 172 GLN   D NE2 1 
ATOM   6948  N  N   . ALA   D  4  181 ? -5.715  -77.992  16.514  1.00 125.90 ? 173 ALA   D N   1 
ATOM   6949  C  CA  . ALA   D  4  181 ? -6.907  -77.114  16.603  1.00 127.42 ? 173 ALA   D CA  1 
ATOM   6950  C  C   . ALA   D  4  181 ? -7.821  -77.354  15.395  1.00 127.37 ? 173 ALA   D C   1 
ATOM   6951  O  O   . ALA   D  4  181 ? -9.056  -77.285  15.567  1.00 124.35 ? 173 ALA   D O   1 
ATOM   6952  C  CB  . ALA   D  4  181 ? -6.484  -75.668  16.688  1.00 130.74 ? 173 ALA   D CB  1 
ATOM   6953  N  N   . GLU   D  4  182 ? -7.228  -77.615  14.223  1.00 127.21 ? 174 GLU   D N   1 
ATOM   6954  C  CA  . GLU   D  4  182 ? -7.951  -77.922  12.959  1.00 127.62 ? 174 GLU   D CA  1 
ATOM   6955  C  C   . GLU   D  4  182 ? -8.571  -79.322  13.064  1.00 122.79 ? 174 GLU   D C   1 
ATOM   6956  O  O   . GLU   D  4  182 ? -9.744  -79.476  12.682  1.00 121.33 ? 174 GLU   D O   1 
ATOM   6957  C  CB  . GLU   D  4  182 ? -7.012  -77.820  11.753  1.00 133.22 ? 174 GLU   D CB  1 
ATOM   6958  C  CG  . GLU   D  4  182 ? -7.723  -77.460  10.458  1.00 139.45 ? 174 GLU   D CG  1 
ATOM   6959  C  CD  . GLU   D  4  182 ? -8.217  -76.024  10.377  1.00 145.26 ? 174 GLU   D CD  1 
ATOM   6960  O  OE1 . GLU   D  4  182 ? -9.351  -75.818  9.897   1.00 157.16 ? 174 GLU   D OE1 1 
ATOM   6961  O  OE2 . GLU   D  4  182 ? -7.461  -75.114  10.779  1.00 149.54 ? 174 GLU   D OE2 1 
ATOM   6962  N  N   . LEU   D  4  183 ? -7.813  -80.298  13.574  1.00 117.31 ? 175 LEU   D N   1 
ATOM   6963  C  CA  . LEU   D  4  183 ? -8.265  -81.707  13.748  1.00 115.52 ? 175 LEU   D CA  1 
ATOM   6964  C  C   . LEU   D  4  183 ? -9.403  -81.780  14.775  1.00 119.08 ? 175 LEU   D C   1 
ATOM   6965  O  O   . LEU   D  4  183 ? -10.220 -82.716  14.667  1.00 120.46 ? 175 LEU   D O   1 
ATOM   6966  C  CB  . LEU   D  4  183 ? -7.081  -82.578  14.181  1.00 111.56 ? 175 LEU   D CB  1 
ATOM   6967  C  CG  . LEU   D  4  183 ? -6.106  -82.968  13.071  1.00 106.47 ? 175 LEU   D CG  1 
ATOM   6968  C  CD1 . LEU   D  4  183 ? -4.849  -83.590  13.657  1.00 104.84 ? 175 LEU   D CD1 1 
ATOM   6969  C  CD2 . LEU   D  4  183 ? -6.760  -83.917  12.077  1.00 104.18 ? 175 LEU   D CD2 1 
ATOM   6970  N  N   . LEU   D  4  184 ? -9.451  -80.842  15.730  1.00 120.86 ? 176 LEU   D N   1 
ATOM   6971  C  CA  . LEU   D  4  184 ? -10.519 -80.762  16.767  1.00 121.65 ? 176 LEU   D CA  1 
ATOM   6972  C  C   . LEU   D  4  184 ? -11.864 -80.501  16.074  1.00 119.15 ? 176 LEU   D C   1 
ATOM   6973  O  O   . LEU   D  4  184 ? -12.867 -81.124  16.470  1.00 114.80 ? 176 LEU   D O   1 
ATOM   6974  C  CB  . LEU   D  4  184 ? -10.189 -79.648  17.772  1.00 123.41 ? 176 LEU   D CB  1 
ATOM   6975  C  CG  . LEU   D  4  184 ? -10.437 -79.964  19.251  1.00 124.20 ? 176 LEU   D CG  1 
ATOM   6976  C  CD1 . LEU   D  4  184 ? -11.771 -80.666  19.470  1.00 122.90 ? 176 LEU   D CD1 1 
ATOM   6977  C  CD2 . LEU   D  4  184 ? -9.298  -80.792  19.827  1.00 123.30 ? 176 LEU   D CD2 1 
ATOM   6978  N  N   . ASN   D  4  185 ? -11.869 -79.618  15.070  1.00 120.82 ? 177 ASN   D N   1 
ATOM   6979  C  CA  . ASN   D  4  185 ? -13.082 -79.182  14.328  1.00 124.97 ? 177 ASN   D CA  1 
ATOM   6980  C  C   . ASN   D  4  185 ? -13.505 -80.266  13.329  1.00 125.55 ? 177 ASN   D C   1 
ATOM   6981  O  O   . ASN   D  4  185 ? -14.717 -80.526  13.235  1.00 133.07 ? 177 ASN   D O   1 
ATOM   6982  C  CB  . ASN   D  4  185 ? -12.857 -77.848  13.608  1.00 125.35 ? 177 ASN   D CB  1 
ATOM   6983  C  CG  . ASN   D  4  185 ? -12.784 -76.668  14.556  1.00 126.65 ? 177 ASN   D CG  1 
ATOM   6984  O  OD1 . ASN   D  4  185 ? -13.492 -76.628  15.559  1.00 128.18 ? 177 ASN   D OD1 1 
ATOM   6985  N  ND2 . ASN   D  4  185 ? -11.937 -75.699  14.246  1.00 129.02 ? 177 ASN   D ND2 1 
ATOM   6986  N  N   . GLU   D  4  186 ? -12.546 -80.879  12.626  1.00 124.61 ? 178 GLU   D N   1 
ATOM   6987  C  CA  . GLU   D  4  186 ? -12.800 -81.682  11.398  1.00 125.06 ? 178 GLU   D CA  1 
ATOM   6988  C  C   . GLU   D  4  186 ? -13.204 -83.123  11.744  1.00 126.47 ? 178 GLU   D C   1 
ATOM   6989  O  O   . GLU   D  4  186 ? -14.050 -83.672  11.008  1.00 124.31 ? 178 GLU   D O   1 
ATOM   6990  C  CB  . GLU   D  4  186 ? -11.571 -81.673  10.487  1.00 126.32 ? 178 GLU   D CB  1 
ATOM   6991  C  CG  . GLU   D  4  186 ? -11.162 -80.287  10.014  1.00 129.13 ? 178 GLU   D CG  1 
ATOM   6992  C  CD  . GLU   D  4  186 ? -11.955 -79.731  8.841   1.00 130.57 ? 178 GLU   D CD  1 
ATOM   6993  O  OE1 . GLU   D  4  186 ? -11.353 -79.026  8.006   1.00 131.39 ? 178 GLU   D OE1 1 
ATOM   6994  O  OE2 . GLU   D  4  186 ? -13.172 -79.990  8.766   1.00 135.95 ? 178 GLU   D OE2 1 
ATOM   6995  N  N   . TRP   D  4  187 ? -12.629 -83.720  12.797  1.00 126.39 ? 179 TRP   D N   1 
ATOM   6996  C  CA  . TRP   D  4  187 ? -12.818 -85.161  13.128  1.00 123.93 ? 179 TRP   D CA  1 
ATOM   6997  C  C   . TRP   D  4  187 ? -14.244 -85.419  13.629  1.00 123.80 ? 179 TRP   D C   1 
ATOM   6998  O  O   . TRP   D  4  187 ? -14.724 -84.653  14.485  1.00 131.00 ? 179 TRP   D O   1 
ATOM   6999  C  CB  . TRP   D  4  187 ? -11.791 -85.668  14.151  1.00 122.60 ? 179 TRP   D CB  1 
ATOM   7000  C  CG  . TRP   D  4  187 ? -11.885 -87.151  14.352  1.00 121.51 ? 179 TRP   D CG  1 
ATOM   7001  C  CD1 . TRP   D  4  187 ? -11.238 -88.114  13.633  1.00 119.21 ? 179 TRP   D CD1 1 
ATOM   7002  C  CD2 . TRP   D  4  187 ? -12.716 -87.852  15.299  1.00 120.92 ? 179 TRP   D CD2 1 
ATOM   7003  N  NE1 . TRP   D  4  187 ? -11.592 -89.359  14.075  1.00 116.98 ? 179 TRP   D NE1 1 
ATOM   7004  C  CE2 . TRP   D  4  187 ? -12.501 -89.232  15.092  1.00 119.33 ? 179 TRP   D CE2 1 
ATOM   7005  C  CE3 . TRP   D  4  187 ? -13.611 -87.455  16.301  1.00 122.81 ? 179 TRP   D CE3 1 
ATOM   7006  C  CZ2 . TRP   D  4  187 ? -13.141 -90.208  15.856  1.00 118.78 ? 179 TRP   D CZ2 1 
ATOM   7007  C  CZ3 . TRP   D  4  187 ? -14.245 -88.421  17.052  1.00 120.82 ? 179 TRP   D CZ3 1 
ATOM   7008  C  CH2 . TRP   D  4  187 ? -14.012 -89.779  16.831  1.00 120.06 ? 179 TRP   D CH2 1 
ATOM   7009  N  N   . HIS   D  4  188 ? -14.876 -86.478  13.113  1.00 121.88 ? 180 HIS   D N   1 
ATOM   7010  C  CA  . HIS   D  4  188 ? -16.112 -87.101  13.659  1.00 125.55 ? 180 HIS   D CA  1 
ATOM   7011  C  C   . HIS   D  4  188 ? -15.981 -88.628  13.567  1.00 126.34 ? 180 HIS   D C   1 
ATOM   7012  O  O   . HIS   D  4  188 ? -15.085 -89.105  12.840  1.00 128.31 ? 180 HIS   D O   1 
ATOM   7013  C  CB  . HIS   D  4  188 ? -17.364 -86.549  12.958  1.00 126.52 ? 180 HIS   D CB  1 
ATOM   7014  C  CG  . HIS   D  4  188 ? -17.407 -86.777  11.482  1.00 126.39 ? 180 HIS   D CG  1 
ATOM   7015  N  ND1 . HIS   D  4  188 ? -18.119 -87.817  10.915  1.00 126.68 ? 180 HIS   D ND1 1 
ATOM   7016  C  CD2 . HIS   D  4  188 ? -16.854 -86.095  10.455  1.00 123.50 ? 180 HIS   D CD2 1 
ATOM   7017  C  CE1 . HIS   D  4  188 ? -17.993 -87.773  9.605   1.00 124.09 ? 180 HIS   D CE1 1 
ATOM   7018  N  NE2 . HIS   D  4  188 ? -17.220 -86.726  9.296   1.00 121.37 ? 180 HIS   D NE2 1 
ATOM   7019  N  N   . SER   D  4  189 ? -16.845 -89.360  14.274  1.00 127.69 ? 181 SER   D N   1 
ATOM   7020  C  CA  . SER   D  4  189 ? -16.751 -90.831  14.477  1.00 124.36 ? 181 SER   D CA  1 
ATOM   7021  C  C   . SER   D  4  189 ? -17.167 -91.604  13.216  1.00 124.64 ? 181 SER   D C   1 
ATOM   7022  O  O   . SER   D  4  189 ? -17.110 -92.850  13.258  1.00 122.59 ? 181 SER   D O   1 
ATOM   7023  C  CB  . SER   D  4  189 ? -17.569 -91.247  15.672  1.00 124.67 ? 181 SER   D CB  1 
ATOM   7024  O  OG  . SER   D  4  189 ? -18.936 -90.911  15.489  1.00 126.26 ? 181 SER   D OG  1 
ATOM   7025  N  N   . SER   D  4  190 ? -17.548 -90.910  12.135  1.00 123.74 ? 182 SER   D N   1 
ATOM   7026  C  CA  . SER   D  4  190 ? -18.107 -91.511  10.893  1.00 122.94 ? 182 SER   D CA  1 
ATOM   7027  C  C   . SER   D  4  190 ? -17.281 -91.128  9.655   1.00 118.29 ? 182 SER   D C   1 
ATOM   7028  O  O   . SER   D  4  190 ? -17.803 -91.298  8.535   1.00 116.31 ? 182 SER   D O   1 
ATOM   7029  C  CB  . SER   D  4  190 ? -19.549 -91.112  10.723  1.00 124.82 ? 182 SER   D CB  1 
ATOM   7030  O  OG  . SER   D  4  190 ? -20.282 -91.360  11.913  1.00 128.09 ? 182 SER   D OG  1 
ATOM   7031  N  N   . LEU   D  4  191 ? -16.045 -90.646  9.831   1.00 117.44 ? 183 LEU   D N   1 
ATOM   7032  C  CA  . LEU   D  4  191 ? -15.121 -90.334  8.704   1.00 117.16 ? 183 LEU   D CA  1 
ATOM   7033  C  C   . LEU   D  4  191 ? -14.825 -91.625  7.939   1.00 115.88 ? 183 LEU   D C   1 
ATOM   7034  O  O   . LEU   D  4  191 ? -14.519 -92.633  8.599   1.00 115.89 ? 183 LEU   D O   1 
ATOM   7035  C  CB  . LEU   D  4  191 ? -13.811 -89.737  9.230   1.00 117.93 ? 183 LEU   D CB  1 
ATOM   7036  C  CG  . LEU   D  4  191 ? -13.831 -88.255  9.595   1.00 119.63 ? 183 LEU   D CG  1 
ATOM   7037  C  CD1 . LEU   D  4  191 ? -12.559 -87.883  10.339  1.00 119.16 ? 183 LEU   D CD1 1 
ATOM   7038  C  CD2 . LEU   D  4  191 ? -13.993 -87.380  8.359   1.00 120.73 ? 183 LEU   D CD2 1 
ATOM   7039  N  N   . THR   D  4  192 ? -14.895 -91.584  6.606   1.00 113.98 ? 184 THR   D N   1 
ATOM   7040  C  CA  . THR   D  4  192 ? -14.442 -92.681  5.711   1.00 113.87 ? 184 THR   D CA  1 
ATOM   7041  C  C   . THR   D  4  192 ? -12.918 -92.574  5.575   1.00 114.07 ? 184 THR   D C   1 
ATOM   7042  O  O   . THR   D  4  192 ? -12.374 -91.511  5.932   1.00 107.16 ? 184 THR   D O   1 
ATOM   7043  C  CB  . THR   D  4  192 ? -15.177 -92.641  4.365   1.00 115.34 ? 184 THR   D CB  1 
ATOM   7044  O  OG1 . THR   D  4  192 ? -14.798 -91.447  3.680   1.00 115.81 ? 184 THR   D OG1 1 
ATOM   7045  C  CG2 . THR   D  4  192 ? -16.682 -92.686  4.514   1.00 116.24 ? 184 THR   D CG2 1 
ATOM   7046  N  N   . LEU   D  4  193 ? -12.256 -93.639  5.110   1.00 119.78 ? 185 LEU   D N   1 
ATOM   7047  C  CA  . LEU   D  4  193 ? -10.780 -93.668  4.914   1.00 124.31 ? 185 LEU   D CA  1 
ATOM   7048  C  C   . LEU   D  4  193 ? -10.387 -92.557  3.932   1.00 126.93 ? 185 LEU   D C   1 
ATOM   7049  O  O   . LEU   D  4  193 ? -9.413  -91.840  4.221   1.00 129.35 ? 185 LEU   D O   1 
ATOM   7050  C  CB  . LEU   D  4  193 ? -10.340 -95.044  4.400   1.00 124.94 ? 185 LEU   D CB  1 
ATOM   7051  C  CG  . LEU   D  4  193 ? -8.827  -95.266  4.346   1.00 126.15 ? 185 LEU   D CG  1 
ATOM   7052  C  CD1 . LEU   D  4  193 ? -8.260  -95.502  5.739   1.00 126.24 ? 185 LEU   D CD1 1 
ATOM   7053  C  CD2 . LEU   D  4  193 ? -8.474  -96.424  3.426   1.00 126.74 ? 185 LEU   D CD2 1 
ATOM   7054  N  N   . LYS   D  4  194 ? -11.130 -92.422  2.827   1.00 129.70 ? 186 LYS   D N   1 
ATOM   7055  C  CA  . LYS   D  4  194 ? -10.909 -91.396  1.768   1.00 130.51 ? 186 LYS   D CA  1 
ATOM   7056  C  C   . LYS   D  4  194 ? -11.050 -89.984  2.351   1.00 129.79 ? 186 LYS   D C   1 
ATOM   7057  O  O   . LYS   D  4  194 ? -10.258 -89.103  1.955   1.00 126.10 ? 186 LYS   D O   1 
ATOM   7058  C  CB  . LYS   D  4  194 ? -11.896 -91.590  0.612   1.00 134.54 ? 186 LYS   D CB  1 
ATOM   7059  C  CG  . LYS   D  4  194 ? -11.541 -92.716  -0.349  1.00 135.47 ? 186 LYS   D CG  1 
ATOM   7060  C  CD  . LYS   D  4  194 ? -12.529 -92.868  -1.484  1.00 137.08 ? 186 LYS   D CD  1 
ATOM   7061  C  CE  . LYS   D  4  194 ? -11.940 -93.576  -2.685  1.00 138.18 ? 186 LYS   D CE  1 
ATOM   7062  N  NZ  . LYS   D  4  194 ? -10.996 -92.705  -3.426  1.00 141.03 ? 186 LYS   D NZ  1 
ATOM   7063  N  N   . GLU   D  4  195 ? -12.031 -89.772  3.235   1.00 125.74 ? 187 GLU   D N   1 
ATOM   7064  C  CA  . GLU   D  4  195 ? -12.258 -88.475  3.929   1.00 126.32 ? 187 GLU   D CA  1 
ATOM   7065  C  C   . GLU   D  4  195 ? -11.034 -88.145  4.793   1.00 126.16 ? 187 GLU   D C   1 
ATOM   7066  O  O   . GLU   D  4  195 ? -10.596 -86.981  4.758   1.00 126.92 ? 187 GLU   D O   1 
ATOM   7067  C  CB  . GLU   D  4  195 ? -13.542 -88.510  4.762   1.00 128.34 ? 187 GLU   D CB  1 
ATOM   7068  C  CG  . GLU   D  4  195 ? -14.799 -88.293  3.938   1.00 132.59 ? 187 GLU   D CG  1 
ATOM   7069  C  CD  . GLU   D  4  195 ? -16.102 -88.471  4.702   1.00 138.79 ? 187 GLU   D CD  1 
ATOM   7070  O  OE1 . GLU   D  4  195 ? -16.263 -87.823  5.754   1.00 138.06 ? 187 GLU   D OE1 1 
ATOM   7071  O  OE2 . GLU   D  4  195 ? -16.952 -89.262  4.243   1.00 143.24 ? 187 GLU   D OE2 1 
ATOM   7072  N  N   . ALA   D  4  196 ? -10.499 -89.133  5.519   1.00 124.31 ? 188 ALA   D N   1 
ATOM   7073  C  CA  . ALA   D  4  196 ? -9.315  -88.991  6.401   1.00 122.64 ? 188 ALA   D CA  1 
ATOM   7074  C  C   . ALA   D  4  196 ? -8.082  -88.637  5.559   1.00 120.98 ? 188 ALA   D C   1 
ATOM   7075  O  O   . ALA   D  4  196 ? -7.371  -87.687  5.939   1.00 121.23 ? 188 ALA   D O   1 
ATOM   7076  C  CB  . ALA   D  4  196 ? -9.097  -90.252  7.202   1.00 123.70 ? 188 ALA   D CB  1 
ATOM   7077  N  N   . GLU   D  4  197 ? -7.853  -89.363  4.457   1.00 119.59 ? 189 GLU   D N   1 
ATOM   7078  C  CA  . GLU   D  4  197 ? -6.700  -89.165  3.532   1.00 119.58 ? 189 GLU   D CA  1 
ATOM   7079  C  C   . GLU   D  4  197 ? -6.630  -87.694  3.103   1.00 119.58 ? 189 GLU   D C   1 
ATOM   7080  O  O   . GLU   D  4  197 ? -5.546  -87.091  3.234   1.00 119.74 ? 189 GLU   D O   1 
ATOM   7081  C  CB  . GLU   D  4  197 ? -6.830  -90.052  2.291   1.00 122.93 ? 189 GLU   D CB  1 
ATOM   7082  C  CG  . GLU   D  4  197 ? -6.628  -91.534  2.559   1.00 123.57 ? 189 GLU   D CG  1 
ATOM   7083  C  CD  . GLU   D  4  197 ? -7.047  -92.455  1.422   1.00 126.80 ? 189 GLU   D CD  1 
ATOM   7084  O  OE1 . GLU   D  4  197 ? -6.837  -93.678  1.550   1.00 125.66 ? 189 GLU   D OE1 1 
ATOM   7085  O  OE2 . GLU   D  4  197 ? -7.583  -91.952  0.410   1.00 127.19 ? 189 GLU   D OE2 1 
ATOM   7086  N  N   . LEU   D  4  198 ? -7.748  -87.155  2.607   1.00 118.30 ? 190 LEU   D N   1 
ATOM   7087  C  CA  . LEU   D  4  198 ? -7.887  -85.748  2.134   1.00 118.93 ? 190 LEU   D CA  1 
ATOM   7088  C  C   . LEU   D  4  198 ? -7.639  -84.768  3.289   1.00 117.31 ? 190 LEU   D C   1 
ATOM   7089  O  O   . LEU   D  4  198 ? -7.042  -83.702  3.038   1.00 116.57 ? 190 LEU   D O   1 
ATOM   7090  C  CB  . LEU   D  4  198 ? -9.291  -85.554  1.548   1.00 120.24 ? 190 LEU   D CB  1 
ATOM   7091  C  CG  . LEU   D  4  198 ? -9.424  -85.721  0.033   1.00 121.80 ? 190 LEU   D CG  1 
ATOM   7092  C  CD1 . LEU   D  4  198 ? -8.596  -86.886  -0.491  1.00 122.01 ? 190 LEU   D CD1 1 
ATOM   7093  C  CD2 . LEU   D  4  198 ? -10.884 -85.896  -0.355  1.00 123.77 ? 190 LEU   D CD2 1 
ATOM   7094  N  N   . LEU   D  4  199 ? -8.089  -85.114  4.499   1.00 117.03 ? 191 LEU   D N   1 
ATOM   7095  C  CA  . LEU   D  4  199 ? -8.031  -84.241  5.705   1.00 114.15 ? 191 LEU   D CA  1 
ATOM   7096  C  C   . LEU   D  4  199 ? -6.574  -84.071  6.149   1.00 110.60 ? 191 LEU   D C   1 
ATOM   7097  O  O   . LEU   D  4  199 ? -6.222  -82.958  6.569   1.00 113.59 ? 191 LEU   D O   1 
ATOM   7098  C  CB  . LEU   D  4  199 ? -8.880  -84.862  6.820   1.00 114.00 ? 191 LEU   D CB  1 
ATOM   7099  C  CG  . LEU   D  4  199 ? -9.622  -83.884  7.728   1.00 116.90 ? 191 LEU   D CG  1 
ATOM   7100  C  CD1 . LEU   D  4  199 ? -10.628 -83.053  6.940   1.00 120.41 ? 191 LEU   D CD1 1 
ATOM   7101  C  CD2 . LEU   D  4  199 ? -10.323 -84.639  8.847   1.00 114.53 ? 191 LEU   D CD2 1 
ATOM   7102  N  N   . VAL   D  4  200 ? -5.771  -85.136  6.066   1.00 106.50 ? 192 VAL   D N   1 
ATOM   7103  C  CA  . VAL   D  4  200 ? -4.319  -85.126  6.417   1.00 103.57 ? 192 VAL   D CA  1 
ATOM   7104  C  C   . VAL   D  4  200 ? -3.572  -84.243  5.410   1.00 101.95 ? 192 VAL   D C   1 
ATOM   7105  O  O   . VAL   D  4  200 ? -2.721  -83.453  5.850   1.00 100.52 ? 192 VAL   D O   1 
ATOM   7106  C  CB  . VAL   D  4  200 ? -3.734  -86.552  6.461   1.00 100.56 ? 192 VAL   D CB  1 
ATOM   7107  C  CG1 . VAL   D  4  200 ? -2.219  -86.547  6.588   1.00 100.51 ? 192 VAL   D CG1 1 
ATOM   7108  C  CG2 . VAL   D  4  200 ? -4.351  -87.376  7.578   1.00 99.24  ? 192 VAL   D CG2 1 
ATOM   7109  N  N   . LEU   D  4  201 ? -3.868  -84.397  4.114   1.00 103.93 ? 193 LEU   D N   1 
ATOM   7110  C  CA  . LEU   D  4  201 ? -3.292  -83.590  3.000   1.00 108.66 ? 193 LEU   D CA  1 
ATOM   7111  C  C   . LEU   D  4  201 ? -3.644  -82.110  3.191   1.00 111.51 ? 193 LEU   D C   1 
ATOM   7112  O  O   . LEU   D  4  201 ? -2.731  -81.267  3.066   1.00 113.06 ? 193 LEU   D O   1 
ATOM   7113  C  CB  . LEU   D  4  201 ? -3.843  -84.100  1.661   1.00 108.92 ? 193 LEU   D CB  1 
ATOM   7114  C  CG  . LEU   D  4  201 ? -2.910  -84.942  0.785   1.00 107.79 ? 193 LEU   D CG  1 
ATOM   7115  C  CD1 . LEU   D  4  201 ? -1.824  -85.651  1.585   1.00 107.82 ? 193 LEU   D CD1 1 
ATOM   7116  C  CD2 . LEU   D  4  201 ? -3.713  -85.949  -0.026  1.00 107.02 ? 193 LEU   D CD2 1 
ATOM   7117  N  N   . LYS   D  4  202 ? -4.921  -81.817  3.460   1.00 117.08 ? 194 LYS   D N   1 
ATOM   7118  C  CA  . LYS   D  4  202 ? -5.462  -80.442  3.649   1.00 118.27 ? 194 LYS   D CA  1 
ATOM   7119  C  C   . LYS   D  4  202 ? -4.715  -79.749  4.795   1.00 118.90 ? 194 LYS   D C   1 
ATOM   7120  O  O   . LYS   D  4  202 ? -4.248  -78.611  4.582   1.00 125.91 ? 194 LYS   D O   1 
ATOM   7121  C  CB  . LYS   D  4  202 ? -6.967  -80.487  3.933   1.00 119.25 ? 194 LYS   D CB  1 
ATOM   7122  C  CG  . LYS   D  4  202 ? -7.617  -79.147  4.256   1.00 121.17 ? 194 LYS   D CG  1 
ATOM   7123  C  CD  . LYS   D  4  202 ? -9.125  -79.224  4.382   1.00 122.47 ? 194 LYS   D CD  1 
ATOM   7124  C  CE  . LYS   D  4  202 ? -9.757  -77.923  4.827   1.00 125.44 ? 194 LYS   D CE  1 
ATOM   7125  N  NZ  . LYS   D  4  202 ? -9.615  -77.712  6.288   1.00 126.77 ? 194 LYS   D NZ  1 
ATOM   7126  N  N   . ILE   D  4  203 ? -4.613  -80.407  5.956   1.00 111.90 ? 195 ILE   D N   1 
ATOM   7127  C  CA  . ILE   D  4  203 ? -4.039  -79.819  7.204   1.00 110.19 ? 195 ILE   D CA  1 
ATOM   7128  C  C   . ILE   D  4  203 ? -2.513  -79.742  7.074   1.00 108.56 ? 195 ILE   D C   1 
ATOM   7129  O  O   . ILE   D  4  203 ? -1.943  -78.772  7.602   1.00 112.24 ? 195 ILE   D O   1 
ATOM   7130  C  CB  . ILE   D  4  203 ? -4.498  -80.586  8.462   1.00 109.68 ? 195 ILE   D CB  1 
ATOM   7131  C  CG1 . ILE   D  4  203 ? -6.020  -80.522  8.621   1.00 113.69 ? 195 ILE   D CG1 1 
ATOM   7132  C  CG2 . ILE   D  4  203 ? -3.790  -80.067  9.706   1.00 108.36 ? 195 ILE   D CG2 1 
ATOM   7133  C  CD1 . ILE   D  4  203 ? -6.575  -81.391  9.728   1.00 116.25 ? 195 ILE   D CD1 1 
ATOM   7134  N  N   . LEU   D  4  204 ? -1.872  -80.701  6.396   1.00 106.80 ? 196 LEU   D N   1 
ATOM   7135  C  CA  . LEU   D  4  204 ? -0.407  -80.651  6.124   1.00 107.74 ? 196 LEU   D CA  1 
ATOM   7136  C  C   . LEU   D  4  204 ? -0.099  -79.433  5.246   1.00 108.95 ? 196 LEU   D C   1 
ATOM   7137  O  O   . LEU   D  4  204 ? 0.862   -78.710  5.567   1.00 104.61 ? 196 LEU   D O   1 
ATOM   7138  C  CB  . LEU   D  4  204 ? 0.073   -81.941  5.448   1.00 108.82 ? 196 LEU   D CB  1 
ATOM   7139  C  CG  . LEU   D  4  204 ? 0.474   -83.084  6.381   1.00 108.78 ? 196 LEU   D CG  1 
ATOM   7140  C  CD1 . LEU   D  4  204 ? 0.819   -84.329  5.580   1.00 110.67 ? 196 LEU   D CD1 1 
ATOM   7141  C  CD2 . LEU   D  4  204 ? 1.644   -82.696  7.277   1.00 109.50 ? 196 LEU   D CD2 1 
ATOM   7142  N  N   . LYS   D  4  205 ? -0.889  -79.214  4.190   1.00 111.55 ? 197 LYS   D N   1 
ATOM   7143  C  CA  . LYS   D  4  205 ? -0.719  -78.082  3.235   1.00 115.04 ? 197 LYS   D CA  1 
ATOM   7144  C  C   . LYS   D  4  205 ? -0.814  -76.747  3.986   1.00 114.67 ? 197 LYS   D C   1 
ATOM   7145  O  O   . LYS   D  4  205 ? -0.082  -75.812  3.603   1.00 112.35 ? 197 LYS   D O   1 
ATOM   7146  C  CB  . LYS   D  4  205 ? -1.760  -78.136  2.111   1.00 115.89 ? 197 LYS   D CB  1 
ATOM   7147  C  CG  . LYS   D  4  205 ? -1.483  -77.188  0.951   1.00 117.87 ? 197 LYS   D CG  1 
ATOM   7148  C  CD  . LYS   D  4  205 ? -2.244  -77.511  -0.324  1.00 121.88 ? 197 LYS   D CD  1 
ATOM   7149  C  CE  . LYS   D  4  205 ? -3.511  -76.700  -0.507  1.00 123.81 ? 197 LYS   D CE  1 
ATOM   7150  N  NZ  . LYS   D  4  205 ? -4.617  -77.190  0.349   1.00 126.01 ? 197 LYS   D NZ  1 
ATOM   7151  N  N   . GLN   D  4  206 ? -1.672  -76.678  5.013   1.00 117.02 ? 198 GLN   D N   1 
ATOM   7152  C  CA  . GLN   D  4  206 ? -1.923  -75.463  5.836   1.00 118.04 ? 198 GLN   D CA  1 
ATOM   7153  C  C   . GLN   D  4  206 ? -0.691  -75.103  6.674   1.00 121.52 ? 198 GLN   D C   1 
ATOM   7154  O  O   . GLN   D  4  206 ? -0.375  -73.899  6.733   1.00 132.10 ? 198 GLN   D O   1 
ATOM   7155  C  CB  . GLN   D  4  206 ? -3.116  -75.658  6.773   1.00 120.21 ? 198 GLN   D CB  1 
ATOM   7156  C  CG  . GLN   D  4  206 ? -4.460  -75.405  6.108   1.00 124.35 ? 198 GLN   D CG  1 
ATOM   7157  C  CD  . GLN   D  4  206 ? -5.627  -75.667  7.029   1.00 129.68 ? 198 GLN   D CD  1 
ATOM   7158  O  OE1 . GLN   D  4  206 ? -6.660  -76.185  6.611   1.00 134.14 ? 198 GLN   D OE1 1 
ATOM   7159  N  NE2 . GLN   D  4  206 ? -5.480  -75.308  8.295   1.00 130.06 ? 198 GLN   D NE2 1 
ATOM   7160  N  N   . VAL   D  4  207 ? -0.040  -76.084  7.311   1.00 115.14 ? 199 VAL   D N   1 
ATOM   7161  C  CA  . VAL   D  4  207 ? 1.039   -75.843  8.322   1.00 115.44 ? 199 VAL   D CA  1 
ATOM   7162  C  C   . VAL   D  4  207 ? 2.433   -75.961  7.688   1.00 116.48 ? 199 VAL   D C   1 
ATOM   7163  O  O   . VAL   D  4  207 ? 3.399   -75.541  8.354   1.00 119.89 ? 199 VAL   D O   1 
ATOM   7164  C  CB  . VAL   D  4  207 ? 0.916   -76.779  9.540   1.00 112.74 ? 199 VAL   D CB  1 
ATOM   7165  C  CG1 . VAL   D  4  207 ? -0.424  -76.619  10.239  1.00 113.39 ? 199 VAL   D CG1 1 
ATOM   7166  C  CG2 . VAL   D  4  207 ? 1.172   -78.236  9.185   1.00 111.27 ? 199 VAL   D CG2 1 
ATOM   7167  N  N   . MET   D  4  208 ? 2.552   -76.526  6.482   1.00 117.57 ? 200 MET   D N   1 
ATOM   7168  C  CA  . MET   D  4  208 ? 3.854   -76.696  5.777   1.00 122.30 ? 200 MET   D CA  1 
ATOM   7169  C  C   . MET   D  4  208 ? 4.354   -75.340  5.268   1.00 124.74 ? 200 MET   D C   1 
ATOM   7170  O  O   . MET   D  4  208 ? 3.513   -74.517  4.865   1.00 130.50 ? 200 MET   D O   1 
ATOM   7171  C  CB  . MET   D  4  208 ? 3.731   -77.646  4.584   1.00 122.60 ? 200 MET   D CB  1 
ATOM   7172  C  CG  . MET   D  4  208 ? 3.938   -79.098  4.944   1.00 122.47 ? 200 MET   D CG  1 
ATOM   7173  S  SD  . MET   D  4  208 ? 3.762   -80.175  3.503   1.00 123.73 ? 200 MET   D SD  1 
ATOM   7174  C  CE  . MET   D  4  208 ? 5.218   -79.720  2.564   1.00 122.22 ? 200 MET   D CE  1 
ATOM   7175  N  N   . GLU   D  4  209 ? 5.676   -75.139  5.263   1.00 131.00 ? 201 GLU   D N   1 
ATOM   7176  C  CA  . GLU   D  4  209 ? 6.333   -73.903  4.753   1.00 131.54 ? 201 GLU   D CA  1 
ATOM   7177  C  C   . GLU   D  4  209 ? 6.219   -73.886  3.224   1.00 127.92 ? 201 GLU   D C   1 
ATOM   7178  O  O   . GLU   D  4  209 ? 5.444   -73.065  2.698   1.00 122.44 ? 201 GLU   D O   1 
ATOM   7179  C  CB  . GLU   D  4  209 ? 7.794   -73.828  5.206   1.00 136.68 ? 201 GLU   D CB  1 
ATOM   7180  C  CG  . GLU   D  4  209 ? 7.974   -73.255  6.602   1.00 138.28 ? 201 GLU   D CG  1 
ATOM   7181  C  CD  . GLU   D  4  209 ? 7.623   -71.782  6.730   1.00 140.68 ? 201 GLU   D CD  1 
ATOM   7182  O  OE1 . GLU   D  4  209 ? 8.102   -70.987  5.896   1.00 140.40 ? 201 GLU   D OE1 1 
ATOM   7183  O  OE2 . GLU   D  4  209 ? 6.866   -71.434  7.658   1.00 141.14 ? 201 GLU   D OE2 1 
ATOM   7184  N  N   . GLU   D  4  210 ? 6.949   -74.778  2.549   1.00 126.22 ? 202 GLU   D N   1 
ATOM   7185  C  CA  . GLU   D  4  210 ? 6.927   -74.928  1.068   1.00 128.13 ? 202 GLU   D CA  1 
ATOM   7186  C  C   . GLU   D  4  210 ? 5.583   -75.537  0.643   1.00 122.29 ? 202 GLU   D C   1 
ATOM   7187  O  O   . GLU   D  4  210 ? 4.941   -76.219  1.471   1.00 114.60 ? 202 GLU   D O   1 
ATOM   7188  C  CB  . GLU   D  4  210 ? 8.110   -75.763  0.565   1.00 134.45 ? 202 GLU   D CB  1 
ATOM   7189  C  CG  . GLU   D  4  210 ? 8.450   -76.963  1.437   1.00 137.18 ? 202 GLU   D CG  1 
ATOM   7190  C  CD  . GLU   D  4  210 ? 9.287   -78.048  0.777   1.00 142.75 ? 202 GLU   D CD  1 
ATOM   7191  O  OE1 . GLU   D  4  210 ? 9.567   -79.067  1.450   1.00 136.18 ? 202 GLU   D OE1 1 
ATOM   7192  O  OE2 . GLU   D  4  210 ? 9.658   -77.879  -0.404  1.00 156.33 ? 202 GLU   D OE2 1 
ATOM   7193  N  N   . LYS   D  4  211 ? 5.179   -75.281  -0.606  1.00 124.07 ? 203 LYS   D N   1 
ATOM   7194  C  CA  . LYS   D  4  211 ? 3.871   -75.699  -1.177  1.00 123.72 ? 203 LYS   D CA  1 
ATOM   7195  C  C   . LYS   D  4  211 ? 3.827   -77.224  -1.272  1.00 121.33 ? 203 LYS   D C   1 
ATOM   7196  O  O   . LYS   D  4  211 ? 4.755   -77.797  -1.871  1.00 121.87 ? 203 LYS   D O   1 
ATOM   7197  C  CB  . LYS   D  4  211 ? 3.659   -75.093  -2.566  1.00 123.14 ? 203 LYS   D CB  1 
ATOM   7198  C  CG  . LYS   D  4  211 ? 2.278   -75.341  -3.158  1.00 123.29 ? 203 LYS   D CG  1 
ATOM   7199  C  CD  . LYS   D  4  211 ? 2.218   -75.210  -4.661  1.00 123.54 ? 203 LYS   D CD  1 
ATOM   7200  C  CE  . LYS   D  4  211 ? 0.978   -75.855  -5.239  1.00 122.23 ? 203 LYS   D CE  1 
ATOM   7201  N  NZ  . LYS   D  4  211 ? 0.933   -75.736  -6.715  1.00 122.96 ? 203 LYS   D NZ  1 
ATOM   7202  N  N   . LEU   D  4  212 ? 2.776   -77.841  -0.724  1.00 124.18 ? 204 LEU   D N   1 
ATOM   7203  C  CA  . LEU   D  4  212 ? 2.621   -79.320  -0.634  1.00 123.06 ? 204 LEU   D CA  1 
ATOM   7204  C  C   . LEU   D  4  212 ? 2.481   -79.922  -2.038  1.00 121.00 ? 204 LEU   D C   1 
ATOM   7205  O  O   . LEU   D  4  212 ? 1.706   -79.371  -2.841  1.00 125.48 ? 204 LEU   D O   1 
ATOM   7206  C  CB  . LEU   D  4  212 ? 1.399   -79.654  0.230   1.00 124.92 ? 204 LEU   D CB  1 
ATOM   7207  C  CG  . LEU   D  4  212 ? 1.108   -81.145  0.416   1.00 122.40 ? 204 LEU   D CG  1 
ATOM   7208  C  CD1 . LEU   D  4  212 ? 0.645   -81.444  1.834   1.00 121.68 ? 204 LEU   D CD1 1 
ATOM   7209  C  CD2 . LEU   D  4  212 ? 0.078   -81.639  -0.590  1.00 121.12 ? 204 LEU   D CD2 1 
ATOM   7210  N  N   . ASP   D  4  213 ? 3.205   -81.015  -2.300  1.00 117.76 ? 205 ASP   D N   1 
ATOM   7211  C  CA  . ASP   D  4  213 ? 3.067   -81.875  -3.508  1.00 117.81 ? 205 ASP   D CA  1 
ATOM   7212  C  C   . ASP   D  4  213 ? 3.391   -83.327  -3.116  1.00 116.87 ? 205 ASP   D C   1 
ATOM   7213  O  O   . ASP   D  4  213 ? 3.555   -83.594  -1.905  1.00 112.06 ? 205 ASP   D O   1 
ATOM   7214  C  CB  . ASP   D  4  213 ? 3.918   -81.348  -4.670  1.00 117.04 ? 205 ASP   D CB  1 
ATOM   7215  C  CG  . ASP   D  4  213 ? 5.424   -81.375  -4.451  1.00 114.59 ? 205 ASP   D CG  1 
ATOM   7216  O  OD1 . ASP   D  4  213 ? 5.881   -82.099  -3.551  1.00 117.37 ? 205 ASP   D OD1 1 
ATOM   7217  O  OD2 . ASP   D  4  213 ? 6.133   -80.675  -5.197  1.00 116.57 ? 205 ASP   D OD2 1 
ATOM   7218  N  N   . GLU   D  4  214 ? 3.481   -84.229  -4.100  1.00 118.90 ? 206 GLU   D N   1 
ATOM   7219  C  CA  . GLU   D  4  214 ? 3.686   -85.688  -3.884  1.00 119.45 ? 206 GLU   D CA  1 
ATOM   7220  C  C   . GLU   D  4  214 ? 5.142   -85.990  -3.494  1.00 118.45 ? 206 GLU   D C   1 
ATOM   7221  O  O   . GLU   D  4  214 ? 5.399   -87.136  -3.079  1.00 118.21 ? 206 GLU   D O   1 
ATOM   7222  C  CB  . GLU   D  4  214 ? 3.282   -86.491  -5.126  1.00 123.15 ? 206 GLU   D CB  1 
ATOM   7223  C  CG  . GLU   D  4  214 ? 4.166   -86.274  -6.347  1.00 125.91 ? 206 GLU   D CG  1 
ATOM   7224  C  CD  . GLU   D  4  214 ? 3.648   -85.273  -7.365  1.00 128.18 ? 206 GLU   D CD  1 
ATOM   7225  O  OE1 . GLU   D  4  214 ? 3.969   -85.432  -8.559  1.00 132.34 ? 206 GLU   D OE1 1 
ATOM   7226  O  OE2 . GLU   D  4  214 ? 2.930   -84.333  -6.964  1.00 130.21 ? 206 GLU   D OE2 1 
ATOM   7227  N  N   . ASN   D  4  215 ? 6.054   -85.020  -3.622  1.00 118.13 ? 207 ASN   D N   1 
ATOM   7228  C  CA  . ASN   D  4  215 ? 7.517   -85.212  -3.414  1.00 117.52 ? 207 ASN   D CA  1 
ATOM   7229  C  C   . ASN   D  4  215 ? 7.958   -84.749  -2.018  1.00 114.52 ? 207 ASN   D C   1 
ATOM   7230  O  O   . ASN   D  4  215 ? 9.005   -85.240  -1.563  1.00 115.33 ? 207 ASN   D O   1 
ATOM   7231  C  CB  . ASN   D  4  215 ? 8.339   -84.487  -4.483  1.00 122.53 ? 207 ASN   D CB  1 
ATOM   7232  C  CG  . ASN   D  4  215 ? 8.391   -85.232  -5.799  1.00 125.79 ? 207 ASN   D CG  1 
ATOM   7233  O  OD1 . ASN   D  4  215 ? 7.713   -86.242  -5.979  1.00 124.26 ? 207 ASN   D OD1 1 
ATOM   7234  N  ND2 . ASN   D  4  215 ? 9.198   -84.741  -6.725  1.00 131.76 ? 207 ASN   D ND2 1 
ATOM   7235  N  N   . ASN   D  4  216 ? 7.228   -83.828  -1.377  1.00 113.91 ? 208 ASN   D N   1 
ATOM   7236  C  CA  . ASN   D  4  216 ? 7.619   -83.239  -0.064  1.00 117.10 ? 208 ASN   D CA  1 
ATOM   7237  C  C   . ASN   D  4  216 ? 6.613   -83.625  1.030   1.00 114.11 ? 208 ASN   D C   1 
ATOM   7238  O  O   . ASN   D  4  216 ? 6.785   -83.145  2.171   1.00 117.61 ? 208 ASN   D O   1 
ATOM   7239  C  CB  . ASN   D  4  216 ? 7.782   -81.718  -0.145  1.00 120.98 ? 208 ASN   D CB  1 
ATOM   7240  C  CG  . ASN   D  4  216 ? 6.516   -80.998  -0.562  1.00 126.46 ? 208 ASN   D CG  1 
ATOM   7241  O  OD1 . ASN   D  4  216 ? 5.431   -81.574  -0.549  1.00 131.38 ? 208 ASN   D OD1 1 
ATOM   7242  N  ND2 . ASN   D  4  216 ? 6.646   -79.734  -0.931  1.00 130.13 ? 208 ASN   D ND2 1 
ATOM   7243  N  N   . ALA   D  4  217 ? 5.605   -84.442  0.701   1.00 111.88 ? 209 ALA   D N   1 
ATOM   7244  C  CA  . ALA   D  4  217 ? 4.663   -85.055  1.668   1.00 108.03 ? 209 ALA   D CA  1 
ATOM   7245  C  C   . ALA   D  4  217 ? 4.444   -86.523  1.293   1.00 107.74 ? 209 ALA   D C   1 
ATOM   7246  O  O   . ALA   D  4  217 ? 4.525   -86.845  0.092   1.00 113.37 ? 209 ALA   D O   1 
ATOM   7247  C  CB  . ALA   D  4  217 ? 3.364   -84.290  1.698   1.00 108.15 ? 209 ALA   D CB  1 
ATOM   7248  N  N   . GLN   D  4  218 ? 4.186   -87.371  2.292   1.00 103.11 ? 210 GLN   D N   1 
ATOM   7249  C  CA  . GLN   D  4  218 ? 3.959   -88.829  2.121   1.00 102.25 ? 210 GLN   D CA  1 
ATOM   7250  C  C   . GLN   D  4  218 ? 2.717   -89.241  2.914   1.00 102.28 ? 210 GLN   D C   1 
ATOM   7251  O  O   . GLN   D  4  218 ? 2.568   -88.768  4.055   1.00 98.52  ? 210 GLN   D O   1 
ATOM   7252  C  CB  . GLN   D  4  218 ? 5.185   -89.612  2.590   1.00 99.28  ? 210 GLN   D CB  1 
ATOM   7253  C  CG  . GLN   D  4  218 ? 5.144   -91.085  2.211   1.00 98.65  ? 210 GLN   D CG  1 
ATOM   7254  C  CD  . GLN   D  4  218 ? 6.488   -91.744  2.385   1.00 94.91  ? 210 GLN   D CD  1 
ATOM   7255  O  OE1 . GLN   D  4  218 ? 7.162   -92.073  1.413   1.00 93.24  ? 210 GLN   D OE1 1 
ATOM   7256  N  NE2 . GLN   D  4  218 ? 6.901   -91.918  3.631   1.00 94.72  ? 210 GLN   D NE2 1 
ATOM   7257  N  N   . LEU   D  4  219 ? 1.866   -90.083  2.320   1.00 107.60 ? 211 LEU   D N   1 
ATOM   7258  C  CA  . LEU   D  4  219 ? 0.692   -90.701  2.990   1.00 111.59 ? 211 LEU   D CA  1 
ATOM   7259  C  C   . LEU   D  4  219 ? 0.946   -92.195  3.192   1.00 111.02 ? 211 LEU   D C   1 
ATOM   7260  O  O   . LEU   D  4  219 ? 1.739   -92.782  2.428   1.00 113.57 ? 211 LEU   D O   1 
ATOM   7261  C  CB  . LEU   D  4  219 ? -0.569  -90.490  2.147   1.00 114.08 ? 211 LEU   D CB  1 
ATOM   7262  C  CG  . LEU   D  4  219 ? -1.291  -89.157  2.328   1.00 116.73 ? 211 LEU   D CG  1 
ATOM   7263  C  CD1 . LEU   D  4  219 ? -2.537  -89.117  1.456   1.00 119.56 ? 211 LEU   D CD1 1 
ATOM   7264  C  CD2 . LEU   D  4  219 ? -1.657  -88.910  3.787   1.00 116.44 ? 211 LEU   D CD2 1 
ATOM   7265  N  N   . SER   D  4  220 ? 0.274   -92.767  4.190   1.00 112.50 ? 212 SER   D N   1 
ATOM   7266  C  CA  . SER   D  4  220 ? 0.236   -94.220  4.489   1.00 112.31 ? 212 SER   D CA  1 
ATOM   7267  C  C   . SER   D  4  220 ? -1.066  -94.529  5.231   1.00 113.77 ? 212 SER   D C   1 
ATOM   7268  O  O   . SER   D  4  220 ? -1.706  -93.578  5.725   1.00 113.45 ? 212 SER   D O   1 
ATOM   7269  C  CB  . SER   D  4  220 ? 1.432   -94.644  5.294   1.00 111.55 ? 212 SER   D CB  1 
ATOM   7270  O  OG  . SER   D  4  220 ? 1.263   -94.303  6.661   1.00 114.02 ? 212 SER   D OG  1 
ATOM   7271  N  N   . CYS   D  4  221 ? -1.437  -95.806  5.302   1.00 116.59 ? 213 CYS   D N   1 
ATOM   7272  C  CA  . CYS   D  4  221 ? -2.617  -96.288  6.061   1.00 116.16 ? 213 CYS   D CA  1 
ATOM   7273  C  C   . CYS   D  4  221 ? -2.410  -97.742  6.485   1.00 115.57 ? 213 CYS   D C   1 
ATOM   7274  O  O   . CYS   D  4  221 ? -1.615  -98.447  5.833   1.00 116.65 ? 213 CYS   D O   1 
ATOM   7275  C  CB  . CYS   D  4  221 ? -3.893  -96.183  5.235   1.00 116.30 ? 213 CYS   D CB  1 
ATOM   7276  S  SG  . CYS   D  4  221 ? -4.052  -97.491  3.990   1.00 117.13 ? 213 CYS   D SG  1 
ATOM   7277  N  N   . ILE   D  4  222 ? -3.120  -98.153  7.535   1.00 115.53 ? 214 ILE   D N   1 
ATOM   7278  C  CA  . ILE   D  4  222 ? -3.210  -99.566  8.004   1.00 115.60 ? 214 ILE   D CA  1 
ATOM   7279  C  C   . ILE   D  4  222 ? -4.695  -99.944  8.012   1.00 114.93 ? 214 ILE   D C   1 
ATOM   7280  O  O   . ILE   D  4  222 ? -5.492  -99.219  8.644   1.00 112.30 ? 214 ILE   D O   1 
ATOM   7281  C  CB  . ILE   D  4  222 ? -2.506  -99.773  9.366   1.00 118.27 ? 214 ILE   D CB  1 
ATOM   7282  C  CG1 . ILE   D  4  222 ? -3.290  -100.695 10.307  1.00 121.77 ? 214 ILE   D CG1 1 
ATOM   7283  C  CG2 . ILE   D  4  222 ? -2.179  -98.447  10.041  1.00 119.26 ? 214 ILE   D CG2 1 
ATOM   7284  C  CD1 . ILE   D  4  222 ? -3.192  -102.163 9.963   1.00 124.48 ? 214 ILE   D CD1 1 
ATOM   7285  N  N   . THR   D  4  223 ? -5.041  -101.009 7.284   1.00 113.70 ? 215 THR   D N   1 
ATOM   7286  C  CA  . THR   D  4  223 ? -6.397  -101.614 7.214   1.00 114.13 ? 215 THR   D CA  1 
ATOM   7287  C  C   . THR   D  4  223 ? -6.293  -103.091 7.606   1.00 114.95 ? 215 THR   D C   1 
ATOM   7288  O  O   . THR   D  4  223 ? -5.269  -103.720 7.261   1.00 110.91 ? 215 THR   D O   1 
ATOM   7289  C  CB  . THR   D  4  223 ? -7.014  -101.452 5.819   1.00 113.32 ? 215 THR   D CB  1 
ATOM   7290  O  OG1 . THR   D  4  223 ? -6.250  -102.212 4.881   1.00 108.21 ? 215 THR   D OG1 1 
ATOM   7291  C  CG2 . THR   D  4  223 ? -7.069  -100.010 5.367   1.00 113.41 ? 215 THR   D CG2 1 
ATOM   7292  N  N   . LYS   D  4  224 ? -7.311  -103.617 8.293   1.00 116.67 ? 216 LYS   D N   1 
ATOM   7293  C  CA  . LYS   D  4  224 ? -7.378  -105.038 8.728   1.00 113.13 ? 216 LYS   D CA  1 
ATOM   7294  C  C   . LYS   D  4  224 ? -7.037  -105.940 7.536   1.00 113.73 ? 216 LYS   D C   1 
ATOM   7295  O  O   . LYS   D  4  224 ? -6.207  -106.852 7.709   1.00 108.48 ? 216 LYS   D O   1 
ATOM   7296  C  CB  . LYS   D  4  224 ? -8.762  -105.383 9.289   1.00 114.28 ? 216 LYS   D CB  1 
ATOM   7297  C  CG  . LYS   D  4  224 ? -9.064  -106.874 9.347   1.00 113.84 ? 216 LYS   D CG  1 
ATOM   7298  C  CD  . LYS   D  4  224 ? -10.228 -107.251 10.229  1.00 119.42 ? 216 LYS   D CD  1 
ATOM   7299  C  CE  . LYS   D  4  224 ? -10.341 -108.752 10.395  1.00 121.19 ? 216 LYS   D CE  1 
ATOM   7300  N  NZ  . LYS   D  4  224 ? -11.318 -109.122 11.445  1.00 125.41 ? 216 LYS   D NZ  1 
ATOM   7301  N  N   . GLN   D  4  225 ? -7.640  -105.667 6.374   1.00 115.11 ? 217 GLN   D N   1 
ATOM   7302  C  CA  . GLN   D  4  225 ? -7.614  -106.555 5.180   1.00 115.88 ? 217 GLN   D CA  1 
ATOM   7303  C  C   . GLN   D  4  225 ? -6.212  -106.575 4.556   1.00 112.94 ? 217 GLN   D C   1 
ATOM   7304  O  O   . GLN   D  4  225 ? -5.667  -107.677 4.385   1.00 115.05 ? 217 GLN   D O   1 
ATOM   7305  C  CB  . GLN   D  4  225 ? -8.659  -106.113 4.154   1.00 121.32 ? 217 GLN   D CB  1 
ATOM   7306  C  CG  . GLN   D  4  225 ? -9.129  -107.246 3.251   1.00 125.85 ? 217 GLN   D CG  1 
ATOM   7307  C  CD  . GLN   D  4  225 ? -9.671  -106.744 1.934   1.00 128.89 ? 217 GLN   D CD  1 
ATOM   7308  O  OE1 . GLN   D  4  225 ? -8.935  -106.219 1.100   1.00 130.63 ? 217 GLN   D OE1 1 
ATOM   7309  N  NE2 . GLN   D  4  225 ? -10.968 -106.908 1.730   1.00 132.46 ? 217 GLN   D NE2 1 
ATOM   7310  N  N   . ASP   D  4  226 ? -5.649  -105.410 4.227   1.00 113.23 ? 218 ASP   D N   1 
ATOM   7311  C  CA  . ASP   D  4  226 ? -4.408  -105.290 3.412   1.00 114.82 ? 218 ASP   D CA  1 
ATOM   7312  C  C   . ASP   D  4  226 ? -3.199  -104.929 4.286   1.00 109.79 ? 218 ASP   D C   1 
ATOM   7313  O  O   . ASP   D  4  226 ? -2.080  -104.890 3.737   1.00 109.08 ? 218 ASP   D O   1 
ATOM   7314  C  CB  . ASP   D  4  226 ? -4.597  -104.262 2.297   1.00 118.11 ? 218 ASP   D CB  1 
ATOM   7315  C  CG  . ASP   D  4  226 ? -5.778  -104.575 1.395   1.00 122.99 ? 218 ASP   D CG  1 
ATOM   7316  O  OD1 . ASP   D  4  226 ? -5.916  -105.752 1.003   1.00 125.22 ? 218 ASP   D OD1 1 
ATOM   7317  O  OD2 . ASP   D  4  226 ? -6.558  -103.643 1.108   1.00 126.36 ? 218 ASP   D OD2 1 
ATOM   7318  N  N   . GLY   D  4  227 ? -3.405  -104.675 5.583   1.00 108.26 ? 219 GLY   D N   1 
ATOM   7319  C  CA  . GLY   D  4  227 ? -2.328  -104.315 6.525   1.00 110.02 ? 219 GLY   D CA  1 
ATOM   7320  C  C   . GLY   D  4  227 ? -1.785  -102.919 6.259   1.00 109.34 ? 219 GLY   D C   1 
ATOM   7321  O  O   . GLY   D  4  227 ? -2.501  -102.110 5.633   1.00 113.71 ? 219 GLY   D O   1 
ATOM   7322  N  N   . PHE   D  4  228 ? -0.556  -102.651 6.711   1.00 108.17 ? 220 PHE   D N   1 
ATOM   7323  C  CA  . PHE   D  4  228 ? 0.131   -101.336 6.613   1.00 106.76 ? 220 PHE   D CA  1 
ATOM   7324  C  C   . PHE   D  4  228 ? 0.738   -101.169 5.216   1.00 104.73 ? 220 PHE   D C   1 
ATOM   7325  O  O   . PHE   D  4  228 ? 1.490   -102.053 4.774   1.00 99.26  ? 220 PHE   D O   1 
ATOM   7326  C  CB  . PHE   D  4  228 ? 1.212   -101.211 7.687   1.00 107.18 ? 220 PHE   D CB  1 
ATOM   7327  C  CG  . PHE   D  4  228 ? 2.072   -99.981  7.555   1.00 109.65 ? 220 PHE   D CG  1 
ATOM   7328  C  CD1 . PHE   D  4  228 ? 1.600   -98.741  7.958   1.00 109.90 ? 220 PHE   D CD1 1 
ATOM   7329  C  CD2 . PHE   D  4  228 ? 3.346   -100.062 7.014   1.00 111.82 ? 220 PHE   D CD2 1 
ATOM   7330  C  CE1 . PHE   D  4  228 ? 2.390   -97.609  7.830   1.00 110.95 ? 220 PHE   D CE1 1 
ATOM   7331  C  CE2 . PHE   D  4  228 ? 4.135   -98.929  6.887   1.00 112.64 ? 220 PHE   D CE2 1 
ATOM   7332  C  CZ  . PHE   D  4  228 ? 3.655   -97.706  7.295   1.00 112.24 ? 220 PHE   D CZ  1 
ATOM   7333  N  N   . LYS   D  4  229 ? 0.444   -100.041 4.565   1.00 107.59 ? 221 LYS   D N   1 
ATOM   7334  C  CA  . LYS   D  4  229 ? 0.881   -99.713  3.181   1.00 112.42 ? 221 LYS   D CA  1 
ATOM   7335  C  C   . LYS   D  4  229 ? 1.299   -98.240  3.112   1.00 108.21 ? 221 LYS   D C   1 
ATOM   7336  O  O   . LYS   D  4  229 ? 0.465   -97.380  3.457   1.00 108.55 ? 221 LYS   D O   1 
ATOM   7337  C  CB  . LYS   D  4  229 ? -0.262  -99.970  2.192   1.00 118.25 ? 221 LYS   D CB  1 
ATOM   7338  C  CG  . LYS   D  4  229 ? -0.450  -101.419 1.762   1.00 121.56 ? 221 LYS   D CG  1 
ATOM   7339  C  CD  . LYS   D  4  229 ? 0.486   -101.847 0.649   1.00 125.23 ? 221 LYS   D CD  1 
ATOM   7340  C  CE  . LYS   D  4  229 ? 0.001   -103.067 -0.107  1.00 127.72 ? 221 LYS   D CE  1 
ATOM   7341  N  NZ  . LYS   D  4  229 ? 0.103   -104.302 0.706   1.00 129.91 ? 221 LYS   D NZ  1 
ATOM   7342  N  N   . ILE   D  4  230 ? 2.536   -97.966  2.681   1.00 105.54 ? 222 ILE   D N   1 
ATOM   7343  C  CA  . ILE   D  4  230 ? 3.003   -96.599  2.295   1.00 104.39 ? 222 ILE   D CA  1 
ATOM   7344  C  C   . ILE   D  4  230 ? 2.563   -96.356  0.850   1.00 101.52 ? 222 ILE   D C   1 
ATOM   7345  O  O   . ILE   D  4  230 ? 2.866   -97.210  -0.000  1.00 104.03 ? 222 ILE   D O   1 
ATOM   7346  C  CB  . ILE   D  4  230 ? 4.530   -96.445  2.454   1.00 103.08 ? 222 ILE   D CB  1 
ATOM   7347  C  CG1 . ILE   D  4  230 ? 4.985   -96.698  3.894   1.00 103.24 ? 222 ILE   D CG1 1 
ATOM   7348  C  CG2 . ILE   D  4  230 ? 4.983   -95.082  1.953   1.00 105.20 ? 222 ILE   D CG2 1 
ATOM   7349  C  CD1 . ILE   D  4  230 ? 6.488   -96.740  4.073   1.00 102.13 ? 222 ILE   D CD1 1 
ATOM   7350  N  N   . TYR   D  4  231 ? 1.888   -95.234  0.584   1.00 101.74 ? 223 TYR   D N   1 
ATOM   7351  C  CA  . TYR   D  4  231 ? 1.316   -94.896  -0.746  1.00 103.58 ? 223 TYR   D CA  1 
ATOM   7352  C  C   . TYR   D  4  231 ? 2.437   -94.499  -1.708  1.00 106.38 ? 223 TYR   D C   1 
ATOM   7353  O  O   . TYR   D  4  231 ? 3.443   -93.911  -1.265  1.00 105.11 ? 223 TYR   D O   1 
ATOM   7354  C  CB  . TYR   D  4  231 ? 0.292   -93.763  -0.646  1.00 103.98 ? 223 TYR   D CB  1 
ATOM   7355  C  CG  . TYR   D  4  231 ? -0.969  -94.073  0.120   1.00 104.81 ? 223 TYR   D CG  1 
ATOM   7356  C  CD1 . TYR   D  4  231 ? -1.266  -95.352  0.566   1.00 106.23 ? 223 TYR   D CD1 1 
ATOM   7357  C  CD2 . TYR   D  4  231 ? -1.896  -93.076  0.374   1.00 106.93 ? 223 TYR   D CD2 1 
ATOM   7358  C  CE1 . TYR   D  4  231 ? -2.431  -95.622  1.267   1.00 109.00 ? 223 TYR   D CE1 1 
ATOM   7359  C  CE2 . TYR   D  4  231 ? -3.069  -93.330  1.064   1.00 107.62 ? 223 TYR   D CE2 1 
ATOM   7360  C  CZ  . TYR   D  4  231 ? -3.340  -94.609  1.512   1.00 107.69 ? 223 TYR   D CZ  1 
ATOM   7361  O  OH  . TYR   D  4  231 ? -4.497  -94.857  2.193   1.00 106.91 ? 223 TYR   D OH  1 
ATOM   7362  N  N   . ASP   D  4  232 ? 2.247   -94.805  -2.995  1.00 112.36 ? 224 ASP   D N   1 
ATOM   7363  C  CA  . ASP   D  4  232 ? 3.134   -94.371  -4.107  1.00 119.58 ? 224 ASP   D CA  1 
ATOM   7364  C  C   . ASP   D  4  232 ? 3.011   -92.850  -4.245  1.00 119.40 ? 224 ASP   D C   1 
ATOM   7365  O  O   . ASP   D  4  232 ? 2.001   -92.296  -3.765  1.00 120.08 ? 224 ASP   D O   1 
ATOM   7366  C  CB  . ASP   D  4  232 ? 2.772   -95.055  -5.430  1.00 128.53 ? 224 ASP   D CB  1 
ATOM   7367  C  CG  . ASP   D  4  232 ? 2.490   -96.546  -5.323  1.00 132.61 ? 224 ASP   D CG  1 
ATOM   7368  O  OD1 . ASP   D  4  232 ? 3.217   -97.330  -5.966  1.00 141.80 ? 224 ASP   D OD1 1 
ATOM   7369  O  OD2 . ASP   D  4  232 ? 1.531   -96.912  -4.612  1.00 139.35 ? 224 ASP   D OD2 1 
ATOM   7370  N  N   . ASN   D  4  233 ? 3.993   -92.205  -4.881  1.00 119.43 ? 225 ASN   D N   1 
ATOM   7371  C  CA  . ASN   D  4  233 ? 3.950   -90.751  -5.194  1.00 121.48 ? 225 ASN   D CA  1 
ATOM   7372  C  C   . ASN   D  4  233 ? 2.848   -90.501  -6.231  1.00 124.17 ? 225 ASN   D C   1 
ATOM   7373  O  O   . ASN   D  4  233 ? 2.278   -89.392  -6.224  1.00 129.40 ? 225 ASN   D O   1 
ATOM   7374  C  CB  . ASN   D  4  233 ? 5.309   -90.221  -5.662  1.00 119.34 ? 225 ASN   D CB  1 
ATOM   7375  C  CG  . ASN   D  4  233 ? 6.399   -90.286  -4.610  1.00 116.02 ? 225 ASN   D CG  1 
ATOM   7376  O  OD1 . ASN   D  4  233 ? 7.578   -90.200  -4.943  1.00 118.81 ? 225 ASN   D OD1 1 
ATOM   7377  N  ND2 . ASN   D  4  233 ? 6.038   -90.431  -3.344  1.00 115.14 ? 225 ASN   D ND2 1 
ATOM   7378  N  N   . GLU   D  4  234 ? 2.546   -91.497  -7.072  1.00 124.75 ? 226 GLU   D N   1 
ATOM   7379  C  CA  . GLU   D  4  234 ? 1.478   -91.424  -8.108  1.00 126.65 ? 226 GLU   D CA  1 
ATOM   7380  C  C   . GLU   D  4  234 ? 0.103   -91.426  -7.431  1.00 122.11 ? 226 GLU   D C   1 
ATOM   7381  O  O   . GLU   D  4  234 ? -0.768  -90.661  -7.880  1.00 123.11 ? 226 GLU   D O   1 
ATOM   7382  C  CB  . GLU   D  4  234 ? 1.582   -92.583  -9.102  1.00 131.49 ? 226 GLU   D CB  1 
ATOM   7383  C  CG  . GLU   D  4  234 ? 2.678   -92.406  -10.140 1.00 138.53 ? 226 GLU   D CG  1 
ATOM   7384  C  CD  . GLU   D  4  234 ? 4.092   -92.624  -9.629  1.00 144.20 ? 226 GLU   D CD  1 
ATOM   7385  O  OE1 . GLU   D  4  234 ? 4.942   -91.738  -9.854  1.00 150.15 ? 226 GLU   D OE1 1 
ATOM   7386  O  OE2 . GLU   D  4  234 ? 4.343   -93.683  -9.016  1.00 148.06 ? 226 GLU   D OE2 1 
ATOM   7387  N  N   . LYS   D  4  235 ? -0.084  -92.255  -6.399  1.00 119.90 ? 227 LYS   D N   1 
ATOM   7388  C  CA  . LYS   D  4  235 ? -1.382  -92.410  -5.687  1.00 120.34 ? 227 LYS   D CA  1 
ATOM   7389  C  C   . LYS   D  4  235 ? -1.688  -91.143  -4.879  1.00 118.53 ? 227 LYS   D C   1 
ATOM   7390  O  O   . LYS   D  4  235 ? -2.851  -90.694  -4.919  1.00 118.88 ? 227 LYS   D O   1 
ATOM   7391  C  CB  . LYS   D  4  235 ? -1.372  -93.636  -4.768  1.00 119.78 ? 227 LYS   D CB  1 
ATOM   7392  C  CG  . LYS   D  4  235 ? -2.737  -94.000  -4.197  1.00 123.65 ? 227 LYS   D CG  1 
ATOM   7393  C  CD  . LYS   D  4  235 ? -2.706  -95.124  -3.189  1.00 127.29 ? 227 LYS   D CD  1 
ATOM   7394  C  CE  . LYS   D  4  235 ? -4.084  -95.474  -2.669  1.00 132.55 ? 227 LYS   D CE  1 
ATOM   7395  N  NZ  . LYS   D  4  235 ? -4.036  -96.562  -1.662  1.00 132.09 ? 227 LYS   D NZ  1 
ATOM   7396  N  N   . THR   D  4  236 ? -0.694  -90.603  -4.165  1.00 116.24 ? 228 THR   D N   1 
ATOM   7397  C  CA  . THR   D  4  236 ? -0.835  -89.395  -3.307  1.00 116.10 ? 228 THR   D CA  1 
ATOM   7398  C  C   . THR   D  4  236 ? -1.073  -88.165  -4.193  1.00 118.69 ? 228 THR   D C   1 
ATOM   7399  O  O   . THR   D  4  236 ? -1.838  -87.282  -3.762  1.00 125.49 ? 228 THR   D O   1 
ATOM   7400  C  CB  . THR   D  4  236 ? 0.375   -89.209  -2.380  1.00 113.78 ? 228 THR   D CB  1 
ATOM   7401  O  OG1 . THR   D  4  236 ? 0.474   -90.354  -1.532  1.00 111.52 ? 228 THR   D OG1 1 
ATOM   7402  C  CG2 . THR   D  4  236 ? 0.278   -87.965  -1.524  1.00 113.69 ? 228 THR   D CG2 1 
ATOM   7403  N  N   . ALA   D  4  237 ? -0.449  -88.108  -5.377  1.00 115.23 ? 229 ALA   D N   1 
ATOM   7404  C  CA  . ALA   D  4  237 ? -0.570  -86.988  -6.344  1.00 115.91 ? 229 ALA   D CA  1 
ATOM   7405  C  C   . ALA   D  4  237 ? -2.030  -86.826  -6.786  1.00 118.54 ? 229 ALA   D C   1 
ATOM   7406  O  O   . ALA   D  4  237 ? -2.477  -85.670  -6.924  1.00 123.05 ? 229 ALA   D O   1 
ATOM   7407  C  CB  . ALA   D  4  237 ? 0.339   -87.208  -7.528  1.00 111.27 ? 229 ALA   D CB  1 
ATOM   7408  N  N   . GLU   D  4  238 ? -2.742  -87.938  -6.994  1.00 116.06 ? 230 GLU   D N   1 
ATOM   7409  C  CA  . GLU   D  4  238 ? -4.168  -87.957  -7.420  1.00 118.97 ? 230 GLU   D CA  1 
ATOM   7410  C  C   . GLU   D  4  238 ? -5.078  -87.526  -6.263  1.00 116.91 ? 230 GLU   D C   1 
ATOM   7411  O  O   . GLU   D  4  238 ? -6.122  -86.911  -6.548  1.00 120.64 ? 230 GLU   D O   1 
ATOM   7412  C  CB  . GLU   D  4  238 ? -4.570  -89.346  -7.910  1.00 121.39 ? 230 GLU   D CB  1 
ATOM   7413  C  CG  . GLU   D  4  238 ? -3.869  -89.763  -9.187  1.00 129.20 ? 230 GLU   D CG  1 
ATOM   7414  C  CD  . GLU   D  4  238 ? -4.317  -91.111  -9.725  1.00 135.05 ? 230 GLU   D CD  1 
ATOM   7415  O  OE1 . GLU   D  4  238 ? -3.442  -91.944  -10.040 1.00 142.78 ? 230 GLU   D OE1 1 
ATOM   7416  O  OE2 . GLU   D  4  238 ? -5.542  -91.327  -9.827  1.00 139.89 ? 230 GLU   D OE2 1 
ATOM   7417  N  N   . LEU   D  4  239 ? -4.714  -87.855  -5.017  1.00 114.82 ? 231 LEU   D N   1 
ATOM   7418  C  CA  . LEU   D  4  239 ? -5.454  -87.434  -3.793  1.00 116.66 ? 231 LEU   D CA  1 
ATOM   7419  C  C   . LEU   D  4  239 ? -5.245  -85.931  -3.552  1.00 118.60 ? 231 LEU   D C   1 
ATOM   7420  O  O   . LEU   D  4  239 ? -6.193  -85.282  -3.063  1.00 120.11 ? 231 LEU   D O   1 
ATOM   7421  C  CB  . LEU   D  4  239 ? -4.984  -88.259  -2.589  1.00 112.89 ? 231 LEU   D CB  1 
ATOM   7422  C  CG  . LEU   D  4  239 ? -5.409  -89.727  -2.579  1.00 111.54 ? 231 LEU   D CG  1 
ATOM   7423  C  CD1 . LEU   D  4  239 ? -4.594  -90.512  -1.562  1.00 110.97 ? 231 LEU   D CD1 1 
ATOM   7424  C  CD2 . LEU   D  4  239 ? -6.897  -89.866  -2.289  1.00 109.89 ? 231 LEU   D CD2 1 
ATOM   7425  N  N   . ILE   D  4  240 ? -4.056  -85.404  -3.871  1.00 119.88 ? 232 ILE   D N   1 
ATOM   7426  C  CA  . ILE   D  4  240 ? -3.728  -83.946  -3.803  1.00 119.85 ? 232 ILE   D CA  1 
ATOM   7427  C  C   . ILE   D  4  240 ? -4.594  -83.200  -4.825  1.00 121.83 ? 232 ILE   D C   1 
ATOM   7428  O  O   . ILE   D  4  240 ? -5.116  -82.125  -4.474  1.00 119.48 ? 232 ILE   D O   1 
ATOM   7429  C  CB  . ILE   D  4  240 ? -2.222  -83.690  -4.030  1.00 120.83 ? 232 ILE   D CB  1 
ATOM   7430  C  CG1 . ILE   D  4  240 ? -1.386  -84.179  -2.844  1.00 121.74 ? 232 ILE   D CG1 1 
ATOM   7431  C  CG2 . ILE   D  4  240 ? -1.955  -82.221  -4.325  1.00 120.05 ? 232 ILE   D CG2 1 
ATOM   7432  C  CD1 . ILE   D  4  240 ? 0.083   -84.359  -3.153  1.00 123.17 ? 232 ILE   D CD1 1 
ATOM   7433  N  N   . LYS   D  4  241 ? -4.728  -83.750  -6.036  1.00 123.66 ? 233 LYS   D N   1 
ATOM   7434  C  CA  . LYS   D  4  241 ? -5.525  -83.158  -7.145  1.00 129.26 ? 233 LYS   D CA  1 
ATOM   7435  C  C   . LYS   D  4  241 ? -7.017  -83.198  -6.789  1.00 130.83 ? 233 LYS   D C   1 
ATOM   7436  O  O   . LYS   D  4  241 ? -7.712  -82.198  -7.057  1.00 134.87 ? 233 LYS   D O   1 
ATOM   7437  C  CB  . LYS   D  4  241 ? -5.253  -83.894  -8.460  1.00 133.73 ? 233 LYS   D CB  1 
ATOM   7438  C  CG  . LYS   D  4  241 ? -5.861  -83.233  -9.690  1.00 138.33 ? 233 LYS   D CG  1 
ATOM   7439  C  CD  . LYS   D  4  241 ? -5.068  -83.447  -10.963 1.00 144.76 ? 233 LYS   D CD  1 
ATOM   7440  C  CE  . LYS   D  4  241 ? -5.227  -84.837  -11.543 1.00 146.31 ? 233 LYS   D CE  1 
ATOM   7441  N  NZ  . LYS   D  4  241 ? -6.531  -85.001  -12.229 1.00 148.47 ? 233 LYS   D NZ  1 
ATOM   7442  N  N   . GLU   D  4  242 ? -7.484  -84.309  -6.210  1.00 128.88 ? 234 GLU   D N   1 
ATOM   7443  C  CA  . GLU   D  4  242 ? -8.889  -84.507  -5.758  1.00 132.16 ? 234 GLU   D CA  1 
ATOM   7444  C  C   . GLU   D  4  242 ? -9.226  -83.498  -4.651  1.00 133.25 ? 234 GLU   D C   1 
ATOM   7445  O  O   . GLU   D  4  242 ? -10.386 -83.039  -4.606  1.00 130.94 ? 234 GLU   D O   1 
ATOM   7446  C  CB  . GLU   D  4  242 ? -9.083  -85.946  -5.270  1.00 131.84 ? 234 GLU   D CB  1 
ATOM   7447  C  CG  . GLU   D  4  242 ? -10.528 -86.304  -4.971  1.00 135.90 ? 234 GLU   D CG  1 
ATOM   7448  C  CD  . GLU   D  4  242 ? -10.755 -87.756  -4.582  1.00 137.91 ? 234 GLU   D CD  1 
ATOM   7449  O  OE1 . GLU   D  4  242 ? -10.059 -88.634  -5.133  1.00 138.85 ? 234 GLU   D OE1 1 
ATOM   7450  O  OE2 . GLU   D  4  242 ? -11.628 -88.006  -3.726  1.00 145.41 ? 234 GLU   D OE2 1 
ATOM   7451  N  N   . LEU   D  4  243 ? -8.250  -83.171  -3.797  1.00 131.63 ? 235 LEU   D N   1 
ATOM   7452  C  CA  . LEU   D  4  243 ? -8.398  -82.236  -2.647  1.00 133.63 ? 235 LEU   D CA  1 
ATOM   7453  C  C   . LEU   D  4  243 ? -8.578  -80.806  -3.177  1.00 137.70 ? 235 LEU   D C   1 
ATOM   7454  O  O   . LEU   D  4  243 ? -9.546  -80.144  -2.749  1.00 138.51 ? 235 LEU   D O   1 
ATOM   7455  C  CB  . LEU   D  4  243 ? -7.167  -82.381  -1.741  1.00 128.39 ? 235 LEU   D CB  1 
ATOM   7456  C  CG  . LEU   D  4  243 ? -7.151  -81.608  -0.419  1.00 126.06 ? 235 LEU   D CG  1 
ATOM   7457  C  CD1 . LEU   D  4  243 ? -6.421  -80.282  -0.566  1.00 126.57 ? 235 LEU   D CD1 1 
ATOM   7458  C  CD2 . LEU   D  4  243 ? -8.547  -81.397  0.155   1.00 126.38 ? 235 LEU   D CD2 1 
ATOM   7459  N  N   . LYS   D  4  244 ? -7.710  -80.364  -4.096  1.00 143.60 ? 236 LYS   D N   1 
ATOM   7460  C  CA  . LYS   D  4  244 ? -7.706  -78.978  -4.646  1.00 144.14 ? 236 LYS   D CA  1 
ATOM   7461  C  C   . LYS   D  4  244 ? -9.020  -78.710  -5.393  1.00 144.86 ? 236 LYS   D C   1 
ATOM   7462  O  O   . LYS   D  4  244 ? -9.550  -77.586  -5.269  1.00 143.79 ? 236 LYS   D O   1 
ATOM   7463  C  CB  . LYS   D  4  244 ? -6.514  -78.740  -5.580  1.00 151.51 ? 236 LYS   D CB  1 
ATOM   7464  C  CG  . LYS   D  4  244 ? -5.974  -77.314  -5.562  1.00 153.00 ? 236 LYS   D CG  1 
ATOM   7465  C  CD  . LYS   D  4  244 ? -5.633  -76.749  -6.925  1.00 157.42 ? 236 LYS   D CD  1 
ATOM   7466  C  CE  . LYS   D  4  244 ? -4.413  -77.380  -7.565  1.00 158.26 ? 236 LYS   D CE  1 
ATOM   7467  N  NZ  . LYS   D  4  244 ? -4.776  -78.476  -8.495  1.00 155.74 ? 236 LYS   D NZ  1 
ATOM   7468  N  N   . GLU   D  4  245 ? -9.511  -79.701  -6.145  1.00 141.14 ? 237 GLU   D N   1 
ATOM   7469  C  CA  . GLU   D  4  245 ? -10.775 -79.623  -6.928  1.00 140.39 ? 237 GLU   D CA  1 
ATOM   7470  C  C   . GLU   D  4  245 ? -11.968 -79.469  -5.977  1.00 139.00 ? 237 GLU   D C   1 
ATOM   7471  O  O   . GLU   D  4  245 ? -12.903 -78.728  -6.330  1.00 142.31 ? 237 GLU   D O   1 
ATOM   7472  C  CB  . GLU   D  4  245 ? -10.944 -80.864  -7.807  1.00 139.58 ? 237 GLU   D CB  1 
ATOM   7473  C  CG  . GLU   D  4  245 ? -10.039 -80.873  -9.026  1.00 140.40 ? 237 GLU   D CG  1 
ATOM   7474  C  CD  . GLU   D  4  245 ? -9.973  -82.203  -9.757  1.00 138.94 ? 237 GLU   D CD  1 
ATOM   7475  O  OE1 . GLU   D  4  245 ? -10.839 -83.065  -9.502  1.00 137.38 ? 237 GLU   D OE1 1 
ATOM   7476  O  OE2 . GLU   D  4  245 ? -9.052  -82.378  -10.578 1.00 139.96 ? 237 GLU   D OE2 1 
ATOM   7477  N  N   . LYS   D  4  246 ? -11.936 -80.140  -4.821  1.00 138.07 ? 238 LYS   D N   1 
ATOM   7478  C  CA  . LYS   D  4  246 ? -13.067 -80.182  -3.853  1.00 140.53 ? 238 LYS   D CA  1 
ATOM   7479  C  C   . LYS   D  4  246 ? -13.164 -78.849  -3.098  1.00 136.85 ? 238 LYS   D C   1 
ATOM   7480  O  O   . LYS   D  4  246 ? -14.303 -78.417  -2.841  1.00 139.66 ? 238 LYS   D O   1 
ATOM   7481  C  CB  . LYS   D  4  246 ? -12.935 -81.382  -2.907  1.00 140.48 ? 238 LYS   D CB  1 
ATOM   7482  C  CG  . LYS   D  4  246 ? -13.512 -82.679  -3.460  1.00 140.96 ? 238 LYS   D CG  1 
ATOM   7483  C  CD  . LYS   D  4  246 ? -13.488 -83.844  -2.497  1.00 140.58 ? 238 LYS   D CD  1 
ATOM   7484  C  CE  . LYS   D  4  246 ? -14.189 -85.063  -3.058  1.00 144.53 ? 238 LYS   D CE  1 
ATOM   7485  N  NZ  . LYS   D  4  246 ? -14.019 -86.251  -2.188  1.00 144.43 ? 238 LYS   D NZ  1 
ATOM   7486  N  N   . GLU   D  4  247 ? -12.030 -78.217  -2.768  1.00 134.83 ? 239 GLU   D N   1 
ATOM   7487  C  CA  . GLU   D  4  247 ? -11.985 -76.917  -2.036  1.00 134.40 ? 239 GLU   D CA  1 
ATOM   7488  C  C   . GLU   D  4  247 ? -12.496 -75.793  -2.946  1.00 134.23 ? 239 GLU   D C   1 
ATOM   7489  O  O   . GLU   D  4  247 ? -13.203 -74.895  -2.443  1.00 132.91 ? 239 GLU   D O   1 
ATOM   7490  C  CB  . GLU   D  4  247 ? -10.571 -76.612  -1.538  1.00 137.38 ? 239 GLU   D CB  1 
ATOM   7491  C  CG  . GLU   D  4  247 ? -10.101 -77.555  -0.444  1.00 136.88 ? 239 GLU   D CG  1 
ATOM   7492  C  CD  . GLU   D  4  247 ? -9.106  -76.957  0.539   1.00 140.39 ? 239 GLU   D CD  1 
ATOM   7493  O  OE1 . GLU   D  4  247 ? -9.479  -76.780  1.717   1.00 141.10 ? 239 GLU   D OE1 1 
ATOM   7494  O  OE2 . GLU   D  4  247 ? -7.959  -76.681  0.131   1.00 134.19 ? 239 GLU   D OE2 1 
ATOM   7495  N  N   . ALA   D  4  248 ? -12.153 -75.850  -4.236  1.00 126.48 ? 240 ALA   D N   1 
ATOM   7496  C  CA  . ALA   D  4  248 ? -12.600 -74.894  -5.272  1.00 128.61 ? 240 ALA   D CA  1 
ATOM   7497  C  C   . ALA   D  4  248 ? -14.105 -75.055  -5.532  1.00 137.27 ? 240 ALA   D C   1 
ATOM   7498  O  O   . ALA   D  4  248 ? -14.730 -74.061  -5.960  1.00 146.53 ? 240 ALA   D O   1 
ATOM   7499  C  CB  . ALA   D  4  248 ? -11.793 -75.094  -6.531  1.00 122.94 ? 240 ALA   D CB  1 
ATOM   7500  N  N   . ALA   D  4  249 ? -14.671 -76.239  -5.260  1.00 135.94 ? 241 ALA   D N   1 
ATOM   7501  C  CA  . ALA   D  4  249 ? -16.053 -76.635  -5.634  1.00 144.15 ? 241 ALA   D CA  1 
ATOM   7502  C  C   . ALA   D  4  249 ? -17.088 -76.130  -4.615  1.00 151.10 ? 241 ALA   D C   1 
ATOM   7503  O  O   . ALA   D  4  249 ? -18.209 -76.679  -4.611  1.00 156.79 ? 241 ALA   D O   1 
ATOM   7504  C  CB  . ALA   D  4  249 ? -16.132 -78.136  -5.796  1.00 144.06 ? 241 ALA   D CB  1 
ATOM   7505  N  N   . GLU   D  4  250 ? -16.745 -75.131  -3.791  1.00 156.98 ? 242 GLU   D N   1 
ATOM   7506  C  CA  . GLU   D  4  250 ? -17.713 -74.358  -2.961  1.00 162.53 ? 242 GLU   D CA  1 
ATOM   7507  C  C   . GLU   D  4  250 ? -16.987 -73.162  -2.330  1.00 163.64 ? 242 GLU   D C   1 
ATOM   7508  O  O   . GLU   D  4  250 ? -17.311 -72.005  -2.610  1.00 170.58 ? 242 GLU   D O   1 
ATOM   7509  C  CB  . GLU   D  4  250 ? -18.362 -75.247  -1.894  1.00 159.81 ? 242 GLU   D CB  1 
ATOM   7510  C  CG  . GLU   D  4  250 ? -19.854 -75.007  -1.722  1.00 162.61 ? 242 GLU   D CG  1 
ATOM   7511  C  CD  . GLU   D  4  250 ? -20.226 -73.695  -1.051  1.00 163.49 ? 242 GLU   D CD  1 
ATOM   7512  O  OE1 . GLU   D  4  250 ? -20.701 -73.739  0.100   1.00 162.85 ? 242 GLU   D OE1 1 
ATOM   7513  O  OE2 . GLU   D  4  250 ? -20.056 -72.634  -1.685  1.00 165.95 ? 242 GLU   D OE2 1 
ATOM   7514  N  N   . ASN   E  5  4   ? 18.273  -74.721  46.751  1.00 113.97 ? 3   ASN   E N   1 
ATOM   7515  C  CA  . ASN   E  5  4   ? 19.010  -73.609  46.074  1.00 119.32 ? 3   ASN   E CA  1 
ATOM   7516  C  C   . ASN   E  5  4   ? 20.356  -74.139  45.556  1.00 117.31 ? 3   ASN   E C   1 
ATOM   7517  O  O   . ASN   E  5  4   ? 20.441  -74.430  44.346  1.00 116.78 ? 3   ASN   E O   1 
ATOM   7518  C  CB  . ASN   E  5  4   ? 19.157  -72.398  47.001  1.00 124.44 ? 3   ASN   E CB  1 
ATOM   7519  C  CG  . ASN   E  5  4   ? 19.990  -71.281  46.405  1.00 131.70 ? 3   ASN   E CG  1 
ATOM   7520  O  OD1 . ASN   E  5  4   ? 19.682  -70.778  45.326  1.00 137.68 ? 3   ASN   E OD1 1 
ATOM   7521  N  ND2 . ASN   E  5  4   ? 21.040  -70.877  47.104  1.00 134.94 ? 3   ASN   E ND2 1 
ATOM   7522  N  N   . ASN   E  5  5   ? 21.359  -74.257  46.436  1.00 117.31 ? 4   ASN   E N   1 
ATOM   7523  C  CA  . ASN   E  5  5   ? 22.696  -74.846  46.140  1.00 119.12 ? 4   ASN   E CA  1 
ATOM   7524  C  C   . ASN   E  5  5   ? 22.697  -76.337  46.508  1.00 115.79 ? 4   ASN   E C   1 
ATOM   7525  O  O   . ASN   E  5  5   ? 23.695  -77.017  46.199  1.00 116.95 ? 4   ASN   E O   1 
ATOM   7526  C  CB  . ASN   E  5  5   ? 23.823  -74.122  46.888  1.00 118.64 ? 4   ASN   E CB  1 
ATOM   7527  C  CG  . ASN   E  5  5   ? 24.473  -73.014  46.088  1.00 121.62 ? 4   ASN   E CG  1 
ATOM   7528  O  OD1 . ASN   E  5  5   ? 24.453  -71.856  46.499  1.00 127.12 ? 4   ASN   E OD1 1 
ATOM   7529  N  ND2 . ASN   E  5  5   ? 25.063  -73.356  44.954  1.00 125.06 ? 4   ASN   E ND2 1 
ATOM   7530  N  N   . TYR   E  5  6   ? 21.623  -76.824  47.140  1.00 113.05 ? 5   TYR   E N   1 
ATOM   7531  C  CA  . TYR   E  5  6   ? 21.550  -78.159  47.789  1.00 113.54 ? 5   TYR   E CA  1 
ATOM   7532  C  C   . TYR   E  5  6   ? 20.472  -79.034  47.132  1.00 114.60 ? 5   TYR   E C   1 
ATOM   7533  O  O   . TYR   E  5  6   ? 20.052  -80.032  47.760  1.00 111.33 ? 5   TYR   E O   1 
ATOM   7534  C  CB  . TYR   E  5  6   ? 21.270  -77.981  49.282  1.00 113.46 ? 5   TYR   E CB  1 
ATOM   7535  C  CG  . TYR   E  5  6   ? 22.196  -77.016  49.979  1.00 113.80 ? 5   TYR   E CG  1 
ATOM   7536  C  CD1 . TYR   E  5  6   ? 21.902  -75.665  50.050  1.00 116.08 ? 5   TYR   E CD1 1 
ATOM   7537  C  CD2 . TYR   E  5  6   ? 23.373  -77.453  50.565  1.00 115.00 ? 5   TYR   E CD2 1 
ATOM   7538  C  CE1 . TYR   E  5  6   ? 22.749  -74.772  50.687  1.00 118.21 ? 5   TYR   E CE1 1 
ATOM   7539  C  CE2 . TYR   E  5  6   ? 24.230  -76.575  51.209  1.00 115.07 ? 5   TYR   E CE2 1 
ATOM   7540  C  CZ  . TYR   E  5  6   ? 23.918  -75.229  51.270  1.00 115.04 ? 5   TYR   E CZ  1 
ATOM   7541  O  OH  . TYR   E  5  6   ? 24.757  -74.355  51.899  1.00 114.96 ? 5   TYR   E OH  1 
ATOM   7542  N  N   . ASP   E  5  7   ? 20.054  -78.692  45.909  1.00 112.69 ? 6   ASP   E N   1 
ATOM   7543  C  CA  . ASP   E  5  7   ? 18.967  -79.394  45.173  1.00 112.82 ? 6   ASP   E CA  1 
ATOM   7544  C  C   . ASP   E  5  7   ? 19.510  -80.007  43.874  1.00 112.55 ? 6   ASP   E C   1 
ATOM   7545  O  O   . ASP   E  5  7   ? 18.684  -80.374  43.014  1.00 115.48 ? 6   ASP   E O   1 
ATOM   7546  C  CB  . ASP   E  5  7   ? 17.795  -78.446  44.901  1.00 116.05 ? 6   ASP   E CB  1 
ATOM   7547  C  CG  . ASP   E  5  7   ? 18.113  -77.304  43.948  1.00 118.59 ? 6   ASP   E CG  1 
ATOM   7548  O  OD1 . ASP   E  5  7   ? 19.311  -77.062  43.689  1.00 120.07 ? 6   ASP   E OD1 1 
ATOM   7549  O  OD2 . ASP   E  5  7   ? 17.155  -76.665  43.470  1.00 121.85 ? 6   ASP   E OD2 1 
ATOM   7550  N  N   . GLY   E  5  8   ? 20.836  -80.118  43.734  1.00 111.34 ? 7   GLY   E N   1 
ATOM   7551  C  CA  . GLY   E  5  8   ? 21.502  -80.671  42.537  1.00 111.44 ? 7   GLY   E CA  1 
ATOM   7552  C  C   . GLY   E  5  8   ? 21.265  -82.165  42.384  1.00 107.85 ? 7   GLY   E C   1 
ATOM   7553  O  O   . GLY   E  5  8   ? 21.170  -82.629  41.230  1.00 104.16 ? 7   GLY   E O   1 
ATOM   7554  N  N   . ASP   E  5  9   ? 21.175  -82.890  43.504  1.00 109.56 ? 8   ASP   E N   1 
ATOM   7555  C  CA  . ASP   E  5  9   ? 20.994  -84.367  43.545  1.00 109.59 ? 8   ASP   E CA  1 
ATOM   7556  C  C   . ASP   E  5  9   ? 20.406  -84.788  44.900  1.00 108.11 ? 8   ASP   E C   1 
ATOM   7557  O  O   . ASP   E  5  9   ? 20.351  -83.948  45.824  1.00 97.40  ? 8   ASP   E O   1 
ATOM   7558  C  CB  . ASP   E  5  9   ? 22.317  -85.079  43.256  1.00 114.05 ? 8   ASP   E CB  1 
ATOM   7559  C  CG  . ASP   E  5  9   ? 23.515  -84.416  43.912  1.00 116.44 ? 8   ASP   E CG  1 
ATOM   7560  O  OD1 . ASP   E  5  9   ? 23.484  -84.243  45.144  1.00 120.39 ? 8   ASP   E OD1 1 
ATOM   7561  O  OD2 . ASP   E  5  9   ? 24.460  -84.061  43.180  1.00 124.73 ? 8   ASP   E OD2 1 
ATOM   7562  N  N   . THR   E  5  10  ? 19.988  -86.052  45.008  1.00 107.05 ? 9   THR   E N   1 
ATOM   7563  C  CA  . THR   E  5  10  ? 19.291  -86.622  46.193  1.00 108.42 ? 9   THR   E CA  1 
ATOM   7564  C  C   . THR   E  5  10  ? 20.279  -86.880  47.334  1.00 103.87 ? 9   THR   E C   1 
ATOM   7565  O  O   . THR   E  5  10  ? 19.815  -87.014  48.483  1.00 105.21 ? 9   THR   E O   1 
ATOM   7566  C  CB  . THR   E  5  10  ? 18.589  -87.946  45.874  1.00 110.48 ? 9   THR   E CB  1 
ATOM   7567  O  OG1 . THR   E  5  10  ? 18.356  -88.029  44.468  1.00 112.85 ? 9   THR   E OG1 1 
ATOM   7568  C  CG2 . THR   E  5  10  ? 17.289  -88.086  46.634  1.00 110.55 ? 9   THR   E CG2 1 
ATOM   7569  N  N   . VAL   E  5  11  ? 21.576  -86.965  47.026  1.00 100.48 ? 10  VAL   E N   1 
ATOM   7570  C  CA  . VAL   E  5  11  ? 22.637  -87.373  47.994  1.00 98.76  ? 10  VAL   E CA  1 
ATOM   7571  C  C   . VAL   E  5  11  ? 23.026  -86.185  48.890  1.00 100.31 ? 10  VAL   E C   1 
ATOM   7572  O  O   . VAL   E  5  11  ? 23.801  -86.412  49.845  1.00 95.74  ? 10  VAL   E O   1 
ATOM   7573  C  CB  . VAL   E  5  11  ? 23.853  -87.974  47.260  1.00 99.17  ? 10  VAL   E CB  1 
ATOM   7574  C  CG1 . VAL   E  5  11  ? 24.866  -86.922  46.829  1.00 97.89  ? 10  VAL   E CG1 1 
ATOM   7575  C  CG2 . VAL   E  5  11  ? 24.525  -89.050  48.097  1.00 101.77 ? 10  VAL   E CG2 1 
ATOM   7576  N  N   . THR   E  5  12  ? 22.513  -84.977  48.614  1.00 99.29  ? 11  THR   E N   1 
ATOM   7577  C  CA  . THR   E  5  12  ? 22.852  -83.731  49.357  1.00 96.85  ? 11  THR   E CA  1 
ATOM   7578  C  C   . THR   E  5  12  ? 21.719  -83.326  50.307  1.00 94.26  ? 11  THR   E C   1 
ATOM   7579  O  O   . THR   E  5  12  ? 20.562  -83.188  49.851  1.00 93.16  ? 11  THR   E O   1 
ATOM   7580  C  CB  . THR   E  5  12  ? 23.169  -82.559  48.421  1.00 96.87  ? 11  THR   E CB  1 
ATOM   7581  O  OG1 . THR   E  5  12  ? 24.029  -83.011  47.375  1.00 96.35  ? 11  THR   E OG1 1 
ATOM   7582  C  CG2 . THR   E  5  12  ? 23.839  -81.416  49.150  1.00 98.15  ? 11  THR   E CG2 1 
ATOM   7583  N  N   . PHE   E  5  13  ? 22.079  -83.107  51.574  1.00 90.10  ? 12  PHE   E N   1 
ATOM   7584  C  CA  . PHE   E  5  13  ? 21.241  -82.496  52.635  1.00 92.50  ? 12  PHE   E CA  1 
ATOM   7585  C  C   . PHE   E  5  13  ? 21.381  -80.975  52.554  1.00 97.10  ? 12  PHE   E C   1 
ATOM   7586  O  O   . PHE   E  5  13  ? 22.506  -80.494  52.309  1.00 102.02 ? 12  PHE   E O   1 
ATOM   7587  C  CB  . PHE   E  5  13  ? 21.682  -82.950  54.029  1.00 90.65  ? 12  PHE   E CB  1 
ATOM   7588  C  CG  . PHE   E  5  13  ? 20.988  -84.178  54.559  1.00 86.68  ? 12  PHE   E CG  1 
ATOM   7589  C  CD1 . PHE   E  5  13  ? 19.630  -84.154  54.834  1.00 89.26  ? 12  PHE   E CD1 1 
ATOM   7590  C  CD2 . PHE   E  5  13  ? 21.692  -85.344  54.814  1.00 83.99  ? 12  PHE   E CD2 1 
ATOM   7591  C  CE1 . PHE   E  5  13  ? 18.986  -85.278  55.330  1.00 87.58  ? 12  PHE   E CE1 1 
ATOM   7592  C  CE2 . PHE   E  5  13  ? 21.047  -86.466  55.312  1.00 83.24  ? 12  PHE   E CE2 1 
ATOM   7593  C  CZ  . PHE   E  5  13  ? 19.695  -86.431  55.569  1.00 84.31  ? 12  PHE   E CZ  1 
ATOM   7594  N  N   . SER   E  5  14  ? 20.282  -80.247  52.771  1.00 101.35 ? 13  SER   E N   1 
ATOM   7595  C  CA  . SER   E  5  14  ? 20.276  -78.771  52.947  1.00 102.79 ? 13  SER   E CA  1 
ATOM   7596  C  C   . SER   E  5  14  ? 20.716  -78.443  54.373  1.00 101.80 ? 13  SER   E C   1 
ATOM   7597  O  O   . SER   E  5  14  ? 20.718  -79.319  55.236  1.00 101.71 ? 13  SER   E O   1 
ATOM   7598  C  CB  . SER   E  5  14  ? 18.924  -78.181  52.621  1.00 104.54 ? 13  SER   E CB  1 
ATOM   7599  O  OG  . SER   E  5  14  ? 17.990  -78.427  53.663  1.00 100.54 ? 13  SER   E OG  1 
ATOM   7600  N  N   . PRO   E  5  15  ? 21.126  -77.187  54.666  1.00 103.72 ? 14  PRO   E N   1 
ATOM   7601  C  CA  . PRO   E  5  15  ? 21.533  -76.804  56.021  1.00 102.65 ? 14  PRO   E CA  1 
ATOM   7602  C  C   . PRO   E  5  15  ? 20.479  -76.987  57.128  1.00 100.68 ? 14  PRO   E C   1 
ATOM   7603  O  O   . PRO   E  5  15  ? 20.878  -77.040  58.276  1.00 101.83 ? 14  PRO   E O   1 
ATOM   7604  C  CB  . PRO   E  5  15  ? 21.877  -75.315  55.877  1.00 105.96 ? 14  PRO   E CB  1 
ATOM   7605  C  CG  . PRO   E  5  15  ? 22.249  -75.160  54.419  1.00 106.33 ? 14  PRO   E CG  1 
ATOM   7606  C  CD  . PRO   E  5  15  ? 21.303  -76.093  53.697  1.00 103.96 ? 14  PRO   E CD  1 
ATOM   7607  N  N   . THR   E  5  16  ? 19.188  -77.068  56.783  1.00 98.85  ? 15  THR   E N   1 
ATOM   7608  C  CA  . THR   E  5  16  ? 18.079  -77.332  57.745  1.00 100.37 ? 15  THR   E CA  1 
ATOM   7609  C  C   . THR   E  5  16  ? 17.668  -78.813  57.703  1.00 99.74  ? 15  THR   E C   1 
ATOM   7610  O  O   . THR   E  5  16  ? 16.650  -79.151  58.337  1.00 102.96 ? 15  THR   E O   1 
ATOM   7611  C  CB  . THR   E  5  16  ? 16.883  -76.405  57.492  1.00 98.43  ? 15  THR   E CB  1 
ATOM   7612  O  OG1 . THR   E  5  16  ? 16.374  -76.628  56.178  1.00 95.59  ? 15  THR   E OG1 1 
ATOM   7613  C  CG2 . THR   E  5  16  ? 17.241  -74.944  57.638  1.00 100.79 ? 15  THR   E CG2 1 
ATOM   7614  N  N   . GLY   E  5  17  ? 18.425  -79.659  56.994  1.00 101.14 ? 16  GLY   E N   1 
ATOM   7615  C  CA  . GLY   E  5  17  ? 18.254  -81.127  56.979  1.00 99.44  ? 16  GLY   E CA  1 
ATOM   7616  C  C   . GLY   E  5  17  ? 17.150  -81.592  56.040  1.00 99.10  ? 16  GLY   E C   1 
ATOM   7617  O  O   . GLY   E  5  17  ? 16.507  -82.617  56.355  1.00 89.76  ? 16  GLY   E O   1 
ATOM   7618  N  N   . ARG   E  5  18  ? 16.943  -80.887  54.922  1.00 101.15 ? 17  ARG   E N   1 
ATOM   7619  C  CA  . ARG   E  5  18  ? 15.929  -81.234  53.891  1.00 102.62 ? 17  ARG   E CA  1 
ATOM   7620  C  C   . ARG   E  5  18  ? 16.614  -81.910  52.696  1.00 101.36 ? 17  ARG   E C   1 
ATOM   7621  O  O   . ARG   E  5  18  ? 17.806  -81.625  52.449  1.00 105.45 ? 17  ARG   E O   1 
ATOM   7622  C  CB  . ARG   E  5  18  ? 15.172  -79.984  53.430  1.00 106.65 ? 17  ARG   E CB  1 
ATOM   7623  C  CG  . ARG   E  5  18  ? 14.565  -79.161  54.557  1.00 110.17 ? 17  ARG   E CG  1 
ATOM   7624  C  CD  . ARG   E  5  18  ? 14.164  -77.774  54.093  1.00 115.99 ? 17  ARG   E CD  1 
ATOM   7625  N  NE  . ARG   E  5  18  ? 12.993  -77.783  53.226  1.00 120.13 ? 17  ARG   E NE  1 
ATOM   7626  C  CZ  . ARG   E  5  18  ? 12.504  -76.715  52.602  1.00 124.67 ? 17  ARG   E CZ  1 
ATOM   7627  N  NH1 . ARG   E  5  18  ? 13.082  -75.532  52.739  1.00 131.02 ? 17  ARG   E NH1 1 
ATOM   7628  N  NH2 . ARG   E  5  18  ? 11.433  -76.832  51.836  1.00 129.99 ? 17  ARG   E NH2 1 
ATOM   7629  N  N   . LEU   E  5  19  ? 15.877  -82.773  51.991  1.00 97.96  ? 18  LEU   E N   1 
ATOM   7630  C  CA  . LEU   E  5  19  ? 16.272  -83.363  50.685  1.00 99.21  ? 18  LEU   E CA  1 
ATOM   7631  C  C   . LEU   E  5  19  ? 15.369  -82.767  49.603  1.00 100.22 ? 18  LEU   E C   1 
ATOM   7632  O  O   . LEU   E  5  19  ? 14.212  -83.220  49.488  1.00 100.29 ? 18  LEU   E O   1 
ATOM   7633  C  CB  . LEU   E  5  19  ? 16.120  -84.885  50.748  1.00 96.12  ? 18  LEU   E CB  1 
ATOM   7634  C  CG  . LEU   E  5  19  ? 16.842  -85.575  51.902  1.00 93.55  ? 18  LEU   E CG  1 
ATOM   7635  C  CD1 . LEU   E  5  19  ? 16.446  -87.041  51.973  1.00 94.66  ? 18  LEU   E CD1 1 
ATOM   7636  C  CD2 . LEU   E  5  19  ? 18.349  -85.433  51.765  1.00 90.89  ? 18  LEU   E CD2 1 
ATOM   7637  N  N   . PHE   E  5  20  ? 15.869  -81.777  48.860  1.00 103.47 ? 19  PHE   E N   1 
ATOM   7638  C  CA  . PHE   E  5  20  ? 15.061  -80.969  47.908  1.00 104.31 ? 19  PHE   E CA  1 
ATOM   7639  C  C   . PHE   E  5  20  ? 14.605  -81.845  46.733  1.00 101.95 ? 19  PHE   E C   1 
ATOM   7640  O  O   . PHE   E  5  20  ? 13.440  -81.708  46.316  1.00 102.94 ? 19  PHE   E O   1 
ATOM   7641  C  CB  . PHE   E  5  20  ? 15.824  -79.718  47.463  1.00 103.42 ? 19  PHE   E CB  1 
ATOM   7642  C  CG  . PHE   E  5  20  ? 15.721  -78.570  48.434  1.00 102.88 ? 19  PHE   E CG  1 
ATOM   7643  C  CD1 . PHE   E  5  20  ? 14.537  -77.861  48.563  1.00 104.92 ? 19  PHE   E CD1 1 
ATOM   7644  C  CD2 . PHE   E  5  20  ? 16.797  -78.207  49.229  1.00 102.68 ? 19  PHE   E CD2 1 
ATOM   7645  C  CE1 . PHE   E  5  20  ? 14.435  -76.807  49.458  1.00 106.88 ? 19  PHE   E CE1 1 
ATOM   7646  C  CE2 . PHE   E  5  20  ? 16.693  -77.154  50.125  1.00 103.90 ? 19  PHE   E CE2 1 
ATOM   7647  C  CZ  . PHE   E  5  20  ? 15.513  -76.456  50.237  1.00 105.94 ? 19  PHE   E CZ  1 
ATOM   7648  N  N   . GLN   E  5  21  ? 15.473  -82.725  46.227  1.00 100.76 ? 20  GLN   E N   1 
ATOM   7649  C  CA  . GLN   E  5  21  ? 15.130  -83.640  45.104  1.00 99.99  ? 20  GLN   E CA  1 
ATOM   7650  C  C   . GLN   E  5  21  ? 13.905  -84.479  45.488  1.00 97.26  ? 20  GLN   E C   1 
ATOM   7651  O  O   . GLN   E  5  21  ? 13.032  -84.668  44.617  1.00 98.01  ? 20  GLN   E O   1 
ATOM   7652  C  CB  . GLN   E  5  21  ? 16.322  -84.519  44.718  1.00 101.21 ? 20  GLN   E CB  1 
ATOM   7653  C  CG  . GLN   E  5  21  ? 17.284  -83.844  43.749  1.00 103.28 ? 20  GLN   E CG  1 
ATOM   7654  C  CD  . GLN   E  5  21  ? 16.615  -83.434  42.458  1.00 105.15 ? 20  GLN   E CD  1 
ATOM   7655  O  OE1 . GLN   E  5  21  ? 16.092  -84.262  41.716  1.00 107.46 ? 20  GLN   E OE1 1 
ATOM   7656  N  NE2 . GLN   E  5  21  ? 16.622  -82.142  42.179  1.00 107.46 ? 20  GLN   E NE2 1 
ATOM   7657  N  N   . VAL   E  5  22  ? 13.834  -84.941  46.741  1.00 96.17  ? 21  VAL   E N   1 
ATOM   7658  C  CA  . VAL   E  5  22  ? 12.687  -85.736  47.278  1.00 96.10  ? 21  VAL   E CA  1 
ATOM   7659  C  C   . VAL   E  5  22  ? 11.451  -84.831  47.346  1.00 93.45  ? 21  VAL   E C   1 
ATOM   7660  O  O   . VAL   E  5  22  ? 10.353  -85.313  47.010  1.00 87.54  ? 21  VAL   E O   1 
ATOM   7661  C  CB  . VAL   E  5  22  ? 13.010  -86.358  48.652  1.00 98.51  ? 21  VAL   E CB  1 
ATOM   7662  C  CG1 . VAL   E  5  22  ? 11.798  -87.045  49.267  1.00 100.13 ? 21  VAL   E CG1 1 
ATOM   7663  C  CG2 . VAL   E  5  22  ? 14.183  -87.325  48.573  1.00 98.64  ? 21  VAL   E CG2 1 
ATOM   7664  N  N   . GLU   E  5  23  ? 11.627  -83.576  47.774  1.00 95.40  ? 22  GLU   E N   1 
ATOM   7665  C  CA  . GLU   E  5  23  ? 10.538  -82.564  47.876  1.00 98.12  ? 22  GLU   E CA  1 
ATOM   7666  C  C   . GLU   E  5  23  ? 10.036  -82.190  46.475  1.00 96.31  ? 22  GLU   E C   1 
ATOM   7667  O  O   . GLU   E  5  23  ? 8.819   -81.956  46.336  1.00 95.38  ? 22  GLU   E O   1 
ATOM   7668  C  CB  . GLU   E  5  23  ? 11.013  -81.316  48.622  1.00 100.93 ? 22  GLU   E CB  1 
ATOM   7669  C  CG  . GLU   E  5  23  ? 11.112  -81.508  50.124  1.00 104.56 ? 22  GLU   E CG  1 
ATOM   7670  C  CD  . GLU   E  5  23  ? 11.452  -80.251  50.909  1.00 108.27 ? 22  GLU   E CD  1 
ATOM   7671  O  OE1 . GLU   E  5  23  ? 11.288  -79.141  50.359  1.00 109.03 ? 22  GLU   E OE1 1 
ATOM   7672  O  OE2 . GLU   E  5  23  ? 11.880  -80.384  52.073  1.00 113.95 ? 22  GLU   E OE2 1 
ATOM   7673  N  N   . TYR   E  5  24  ? 10.933  -82.119  45.484  1.00 96.45  ? 23  TYR   E N   1 
ATOM   7674  C  CA  . TYR   E  5  24  ? 10.596  -81.813  44.067  1.00 99.04  ? 23  TYR   E CA  1 
ATOM   7675  C  C   . TYR   E  5  24  ? 9.822   -82.990  43.459  1.00 99.81  ? 23  TYR   E C   1 
ATOM   7676  O  O   . TYR   E  5  24  ? 8.893   -82.740  42.669  1.00 103.72 ? 23  TYR   E O   1 
ATOM   7677  C  CB  . TYR   E  5  24  ? 11.846  -81.494  43.242  1.00 98.42  ? 23  TYR   E CB  1 
ATOM   7678  C  CG  . TYR   E  5  24  ? 12.589  -80.235  43.621  1.00 96.98  ? 23  TYR   E CG  1 
ATOM   7679  C  CD1 . TYR   E  5  24  ? 12.062  -79.306  44.510  1.00 95.83  ? 23  TYR   E CD1 1 
ATOM   7680  C  CD2 . TYR   E  5  24  ? 13.825  -79.959  43.059  1.00 95.13  ? 23  TYR   E CD2 1 
ATOM   7681  C  CE1 . TYR   E  5  24  ? 12.755  -78.155  44.849  1.00 96.29  ? 23  TYR   E CE1 1 
ATOM   7682  C  CE2 . TYR   E  5  24  ? 14.529  -78.811  43.383  1.00 96.02  ? 23  TYR   E CE2 1 
ATOM   7683  C  CZ  . TYR   E  5  24  ? 13.992  -77.906  44.281  1.00 97.76  ? 23  TYR   E CZ  1 
ATOM   7684  O  OH  . TYR   E  5  24  ? 14.686  -76.777  44.597  1.00 99.84  ? 23  TYR   E OH  1 
ATOM   7685  N  N   . ALA   E  5  25  ? 10.188  -84.226  43.813  1.00 99.35  ? 24  ALA   E N   1 
ATOM   7686  C  CA  . ALA   E  5  25  ? 9.445   -85.452  43.438  1.00 100.07 ? 24  ALA   E CA  1 
ATOM   7687  C  C   . ALA   E  5  25  ? 8.026   -85.366  44.013  1.00 98.84  ? 24  ALA   E C   1 
ATOM   7688  O  O   . ALA   E  5  25  ? 7.066   -85.565  43.246  1.00 97.83  ? 24  ALA   E O   1 
ATOM   7689  C  CB  . ALA   E  5  25  ? 10.172  -86.680  43.927  1.00 101.55 ? 24  ALA   E CB  1 
ATOM   7690  N  N   . LEU   E  5  26  ? 7.913   -85.057  45.311  1.00 102.15 ? 25  LEU   E N   1 
ATOM   7691  C  CA  . LEU   E  5  26  ? 6.627   -84.846  46.036  1.00 105.70 ? 25  LEU   E CA  1 
ATOM   7692  C  C   . LEU   E  5  26  ? 5.754   -83.842  45.270  1.00 106.48 ? 25  LEU   E C   1 
ATOM   7693  O  O   . LEU   E  5  26  ? 4.521   -84.019  45.280  1.00 102.07 ? 25  LEU   E O   1 
ATOM   7694  C  CB  . LEU   E  5  26  ? 6.913   -84.351  47.462  1.00 111.45 ? 25  LEU   E CB  1 
ATOM   7695  C  CG  . LEU   E  5  26  ? 6.656   -85.331  48.612  1.00 112.66 ? 25  LEU   E CG  1 
ATOM   7696  C  CD1 . LEU   E  5  26  ? 7.064   -86.756  48.267  1.00 113.91 ? 25  LEU   E CD1 1 
ATOM   7697  C  CD2 . LEU   E  5  26  ? 7.378   -84.875  49.871  1.00 115.81 ? 25  LEU   E CD2 1 
ATOM   7698  N  N   . GLU   E  5  27  ? 6.369   -82.838  44.635  1.00 111.67 ? 26  GLU   E N   1 
ATOM   7699  C  CA  . GLU   E  5  27  ? 5.669   -81.737  43.915  1.00 117.46 ? 26  GLU   E CA  1 
ATOM   7700  C  C   . GLU   E  5  27  ? 4.976   -82.286  42.659  1.00 115.12 ? 26  GLU   E C   1 
ATOM   7701  O  O   . GLU   E  5  27  ? 3.884   -81.788  42.334  1.00 114.49 ? 26  GLU   E O   1 
ATOM   7702  C  CB  . GLU   E  5  27  ? 6.645   -80.609  43.564  1.00 122.34 ? 26  GLU   E CB  1 
ATOM   7703  C  CG  . GLU   E  5  27  ? 5.964   -79.297  43.208  1.00 126.68 ? 26  GLU   E CG  1 
ATOM   7704  C  CD  . GLU   E  5  27  ? 5.091   -78.703  44.302  1.00 130.63 ? 26  GLU   E CD  1 
ATOM   7705  O  OE1 . GLU   E  5  27  ? 4.025   -78.143  43.971  1.00 135.00 ? 26  GLU   E OE1 1 
ATOM   7706  O  OE2 . GLU   E  5  27  ? 5.480   -78.798  45.484  1.00 136.34 ? 26  GLU   E OE2 1 
ATOM   7707  N  N   . ALA   E  5  28  ? 5.582   -83.269  41.983  1.00 114.01 ? 27  ALA   E N   1 
ATOM   7708  C  CA  . ALA   E  5  28  ? 5.027   -83.936  40.779  1.00 112.56 ? 27  ALA   E CA  1 
ATOM   7709  C  C   . ALA   E  5  28  ? 3.682   -84.595  41.115  1.00 112.00 ? 27  ALA   E C   1 
ATOM   7710  O  O   . ALA   E  5  28  ? 2.804   -84.628  40.226  1.00 108.88 ? 27  ALA   E O   1 
ATOM   7711  C  CB  . ALA   E  5  28  ? 6.009   -84.945  40.236  1.00 110.08 ? 27  ALA   E CB  1 
ATOM   7712  N  N   . ILE   E  5  29  ? 3.532   -85.096  42.347  1.00 111.43 ? 28  ILE   E N   1 
ATOM   7713  C  CA  . ILE   E  5  29  ? 2.288   -85.761  42.847  1.00 112.14 ? 28  ILE   E CA  1 
ATOM   7714  C  C   . ILE   E  5  29  ? 1.177   -84.712  42.932  1.00 115.17 ? 28  ILE   E C   1 
ATOM   7715  O  O   . ILE   E  5  29  ? 0.054   -85.008  42.482  1.00 110.85 ? 28  ILE   E O   1 
ATOM   7716  C  CB  . ILE   E  5  29  ? 2.507   -86.446  44.212  1.00 113.49 ? 28  ILE   E CB  1 
ATOM   7717  C  CG1 . ILE   E  5  29  ? 3.647   -87.467  44.166  1.00 114.13 ? 28  ILE   E CG1 1 
ATOM   7718  C  CG2 . ILE   E  5  29  ? 1.213   -87.078  44.708  1.00 112.13 ? 28  ILE   E CG2 1 
ATOM   7719  C  CD1 . ILE   E  5  29  ? 4.094   -87.948  45.522  1.00 113.22 ? 28  ILE   E CD1 1 
ATOM   7720  N  N   . LYS   E  5  30  ? 1.495   -83.544  43.500  1.00 119.62 ? 29  LYS   E N   1 
ATOM   7721  C  CA  . LYS   E  5  30  ? 0.552   -82.409  43.701  1.00 122.14 ? 29  LYS   E CA  1 
ATOM   7722  C  C   . LYS   E  5  30  ? -0.045  -81.975  42.354  1.00 121.17 ? 29  LYS   E C   1 
ATOM   7723  O  O   . LYS   E  5  30  ? -1.237  -81.614  42.341  1.00 118.58 ? 29  LYS   E O   1 
ATOM   7724  C  CB  . LYS   E  5  30  ? 1.245   -81.242  44.416  1.00 124.73 ? 29  LYS   E CB  1 
ATOM   7725  C  CG  . LYS   E  5  30  ? 0.840   -81.045  45.872  1.00 127.54 ? 29  LYS   E CG  1 
ATOM   7726  C  CD  . LYS   E  5  30  ? 1.348   -82.123  46.812  1.00 125.92 ? 29  LYS   E CD  1 
ATOM   7727  C  CE  . LYS   E  5  30  ? 2.803   -81.955  47.198  1.00 122.61 ? 29  LYS   E CE  1 
ATOM   7728  N  NZ  . LYS   E  5  30  ? 3.019   -80.759  48.045  1.00 124.63 ? 29  LYS   E NZ  1 
ATOM   7729  N  N   . GLN   E  5  31  ? 0.738   -82.022  41.267  1.00 120.12 ? 30  GLN   E N   1 
ATOM   7730  C  CA  . GLN   E  5  31  ? 0.282   -81.634  39.901  1.00 121.61 ? 30  GLN   E CA  1 
ATOM   7731  C  C   . GLN   E  5  31  ? -0.606  -82.742  39.320  1.00 118.18 ? 30  GLN   E C   1 
ATOM   7732  O  O   . GLN   E  5  31  ? -1.385  -82.444  38.395  1.00 114.92 ? 30  GLN   E O   1 
ATOM   7733  C  CB  . GLN   E  5  31  ? 1.445   -81.375  38.935  1.00 124.14 ? 30  GLN   E CB  1 
ATOM   7734  C  CG  . GLN   E  5  31  ? 2.616   -80.582  39.506  1.00 126.27 ? 30  GLN   E CG  1 
ATOM   7735  C  CD  . GLN   E  5  31  ? 2.263   -79.204  40.013  1.00 127.78 ? 30  GLN   E CD  1 
ATOM   7736  O  OE1 . GLN   E  5  31  ? 1.159   -78.701  39.813  1.00 125.34 ? 30  GLN   E OE1 1 
ATOM   7737  N  NE2 . GLN   E  5  31  ? 3.223   -78.570  40.669  1.00 128.63 ? 30  GLN   E NE2 1 
ATOM   7738  N  N   . GLY   E  5  32  ? -0.480  -83.973  39.827  1.00 116.35 ? 31  GLY   E N   1 
ATOM   7739  C  CA  . GLY   E  5  32  ? -1.228  -85.154  39.350  1.00 114.20 ? 31  GLY   E CA  1 
ATOM   7740  C  C   . GLY   E  5  32  ? -2.721  -85.038  39.610  1.00 115.17 ? 31  GLY   E C   1 
ATOM   7741  O  O   . GLY   E  5  32  ? -3.109  -84.291  40.533  1.00 114.47 ? 31  GLY   E O   1 
ATOM   7742  N  N   . SER   E  5  33  ? -3.530  -85.757  38.823  1.00 112.87 ? 32  SER   E N   1 
ATOM   7743  C  CA  . SER   E  5  33  ? -5.013  -85.798  38.925  1.00 114.21 ? 32  SER   E CA  1 
ATOM   7744  C  C   . SER   E  5  33  ? -5.413  -86.470  40.242  1.00 113.63 ? 32  SER   E C   1 
ATOM   7745  O  O   . SER   E  5  33  ? -4.738  -87.440  40.641  1.00 112.36 ? 32  SER   E O   1 
ATOM   7746  C  CB  . SER   E  5  33  ? -5.625  -86.500  37.739  1.00 113.39 ? 32  SER   E CB  1 
ATOM   7747  O  OG  . SER   E  5  33  ? -7.041  -86.491  37.823  1.00 114.77 ? 32  SER   E OG  1 
ATOM   7748  N  N   . VAL   E  5  34  ? -6.467  -85.965  40.889  1.00 117.17 ? 33  VAL   E N   1 
ATOM   7749  C  CA  . VAL   E  5  34  ? -6.927  -86.430  42.232  1.00 119.51 ? 33  VAL   E CA  1 
ATOM   7750  C  C   . VAL   E  5  34  ? -7.326  -87.905  42.135  1.00 118.55 ? 33  VAL   E C   1 
ATOM   7751  O  O   . VAL   E  5  34  ? -7.969  -88.287  41.138  1.00 117.51 ? 33  VAL   E O   1 
ATOM   7752  C  CB  . VAL   E  5  34  ? -8.077  -85.567  42.792  1.00 125.42 ? 33  VAL   E CB  1 
ATOM   7753  C  CG1 . VAL   E  5  34  ? -9.341  -85.640  41.945  1.00 129.03 ? 33  VAL   E CG1 1 
ATOM   7754  C  CG2 . VAL   E  5  34  ? -8.387  -85.922  44.240  1.00 127.06 ? 33  VAL   E CG2 1 
ATOM   7755  N  N   . THR   E  5  35  ? -6.922  -88.696  43.131  1.00 116.31 ? 34  THR   E N   1 
ATOM   7756  C  CA  . THR   E  5  35  ? -7.398  -90.084  43.371  1.00 116.96 ? 34  THR   E CA  1 
ATOM   7757  C  C   . THR   E  5  35  ? -7.718  -90.233  44.862  1.00 114.76 ? 34  THR   E C   1 
ATOM   7758  O  O   . THR   E  5  35  ? -7.011  -89.620  45.685  1.00 113.72 ? 34  THR   E O   1 
ATOM   7759  C  CB  . THR   E  5  35  ? -6.380  -91.122  42.878  1.00 116.19 ? 34  THR   E CB  1 
ATOM   7760  O  OG1 . THR   E  5  35  ? -6.940  -92.423  43.062  1.00 115.63 ? 34  THR   E OG1 1 
ATOM   7761  C  CG2 . THR   E  5  35  ? -5.047  -91.033  43.588  1.00 115.59 ? 34  THR   E CG2 1 
ATOM   7762  N  N   . VAL   E  5  36  ? -8.751  -91.016  45.177  1.00 114.04 ? 35  VAL   E N   1 
ATOM   7763  C  CA  . VAL   E  5  36  ? -9.279  -91.218  46.556  1.00 116.30 ? 35  VAL   E CA  1 
ATOM   7764  C  C   . VAL   E  5  36  ? -9.187  -92.708  46.903  1.00 116.83 ? 35  VAL   E C   1 
ATOM   7765  O  O   . VAL   E  5  36  ? -9.353  -93.545  45.993  1.00 119.47 ? 35  VAL   E O   1 
ATOM   7766  C  CB  . VAL   E  5  36  ? -10.725 -90.699  46.672  1.00 118.81 ? 35  VAL   E CB  1 
ATOM   7767  C  CG1 . VAL   E  5  36  ? -11.350 -91.039  48.016  1.00 117.66 ? 35  VAL   E CG1 1 
ATOM   7768  C  CG2 . VAL   E  5  36  ? -10.801 -89.201  46.412  1.00 120.94 ? 35  VAL   E CG2 1 
ATOM   7769  N  N   . GLY   E  5  37  ? -8.923  -93.006  48.177  1.00 117.38 ? 36  GLY   E N   1 
ATOM   7770  C  CA  . GLY   E  5  37  ? -8.983  -94.359  48.761  1.00 114.43 ? 36  GLY   E CA  1 
ATOM   7771  C  C   . GLY   E  5  37  ? -9.762  -94.339  50.063  1.00 113.12 ? 36  GLY   E C   1 
ATOM   7772  O  O   . GLY   E  5  37  ? -9.541  -93.409  50.860  1.00 117.57 ? 36  GLY   E O   1 
ATOM   7773  N  N   . LEU   E  5  38  ? -10.659 -95.305  50.267  1.00 110.28 ? 37  LEU   E N   1 
ATOM   7774  C  CA  . LEU   E  5  38  ? -11.411 -95.478  51.540  1.00 112.86 ? 37  LEU   E CA  1 
ATOM   7775  C  C   . LEU   E  5  38  ? -11.806 -96.950  51.694  1.00 114.13 ? 37  LEU   E C   1 
ATOM   7776  O  O   . LEU   E  5  38  ? -11.805 -97.675  50.676  1.00 118.22 ? 37  LEU   E O   1 
ATOM   7777  C  CB  . LEU   E  5  38  ? -12.625 -94.542  51.557  1.00 111.59 ? 37  LEU   E CB  1 
ATOM   7778  C  CG  . LEU   E  5  38  ? -13.892 -95.028  50.851  1.00 112.40 ? 37  LEU   E CG  1 
ATOM   7779  C  CD1 . LEU   E  5  38  ? -15.074 -94.139  51.212  1.00 113.94 ? 37  LEU   E CD1 1 
ATOM   7780  C  CD2 . LEU   E  5  38  ? -13.706 -95.074  49.342  1.00 111.49 ? 37  LEU   E CD2 1 
ATOM   7781  N  N   . ARG   E  5  39  ? -12.111 -97.376  52.924  1.00 115.85 ? 38  ARG   E N   1 
ATOM   7782  C  CA  . ARG   E  5  39  ? -12.436 -98.792  53.235  1.00 115.16 ? 38  ARG   E CA  1 
ATOM   7783  C  C   . ARG   E  5  39  ? -13.430 -98.886  54.396  1.00 115.62 ? 38  ARG   E C   1 
ATOM   7784  O  O   . ARG   E  5  39  ? -13.509 -97.941  55.208  1.00 113.33 ? 38  ARG   E O   1 
ATOM   7785  C  CB  . ARG   E  5  39  ? -11.163 -99.581  53.557  1.00 110.58 ? 38  ARG   E CB  1 
ATOM   7786  C  CG  . ARG   E  5  39  ? -10.575 -99.342  54.943  1.00 112.20 ? 38  ARG   E CG  1 
ATOM   7787  C  CD  . ARG   E  5  39  ? -9.758  -100.541 55.393  1.00 110.45 ? 38  ARG   E CD  1 
ATOM   7788  N  NE  . ARG   E  5  39  ? -9.207  -100.414 56.739  1.00 110.13 ? 38  ARG   E NE  1 
ATOM   7789  C  CZ  . ARG   E  5  39  ? -9.750  -100.910 57.854  1.00 110.71 ? 38  ARG   E CZ  1 
ATOM   7790  N  NH1 . ARG   E  5  39  ? -10.890 -101.582 57.822  1.00 110.95 ? 38  ARG   E NH1 1 
ATOM   7791  N  NH2 . ARG   E  5  39  ? -9.140  -100.728 59.012  1.00 111.16 ? 38  ARG   E NH2 1 
ATOM   7792  N  N   . SER   E  5  40  ? -14.144 -100.012 54.448  1.00 115.90 ? 39  SER   E N   1 
ATOM   7793  C  CA  . SER   E  5  40  ? -14.969 -100.474 55.592  1.00 119.26 ? 39  SER   E CA  1 
ATOM   7794  C  C   . SER   E  5  40  ? -14.203 -101.601 56.298  1.00 115.20 ? 39  SER   E C   1 
ATOM   7795  O  O   . SER   E  5  40  ? -12.957 -101.562 56.271  1.00 112.14 ? 39  SER   E O   1 
ATOM   7796  C  CB  . SER   E  5  40  ? -16.342 -100.896 55.121  1.00 119.03 ? 39  SER   E CB  1 
ATOM   7797  O  OG  . SER   E  5  40  ? -16.301 -102.151 54.456  1.00 119.99 ? 39  SER   E OG  1 
ATOM   7798  N  N   . ASN   E  5  41  ? -14.905 -102.563 56.902  1.00 117.47 ? 40  ASN   E N   1 
ATOM   7799  C  CA  . ASN   E  5  41  ? -14.293 -103.769 57.521  1.00 116.50 ? 40  ASN   E CA  1 
ATOM   7800  C  C   . ASN   E  5  41  ? -14.348 -104.942 56.535  1.00 115.85 ? 40  ASN   E C   1 
ATOM   7801  O  O   . ASN   E  5  41  ? -13.627 -105.927 56.779  1.00 114.91 ? 40  ASN   E O   1 
ATOM   7802  C  CB  . ASN   E  5  41  ? -14.953 -104.106 58.859  1.00 119.66 ? 40  ASN   E CB  1 
ATOM   7803  C  CG  . ASN   E  5  41  ? -14.499 -103.179 59.966  1.00 123.34 ? 40  ASN   E CG  1 
ATOM   7804  O  OD1 . ASN   E  5  41  ? -13.374 -103.296 60.447  1.00 126.83 ? 40  ASN   E OD1 1 
ATOM   7805  N  ND2 . ASN   E  5  41  ? -15.353 -102.250 60.368  1.00 128.77 ? 40  ASN   E ND2 1 
ATOM   7806  N  N   . THR   E  5  42  ? -15.141 -104.830 55.459  1.00 117.15 ? 41  THR   E N   1 
ATOM   7807  C  CA  . THR   E  5  42  ? -15.393 -105.920 54.474  1.00 119.19 ? 41  THR   E CA  1 
ATOM   7808  C  C   . THR   E  5  42  ? -14.776 -105.598 53.105  1.00 119.31 ? 41  THR   E C   1 
ATOM   7809  O  O   . THR   E  5  42  ? -14.309 -106.547 52.451  1.00 121.63 ? 41  THR   E O   1 
ATOM   7810  C  CB  . THR   E  5  42  ? -16.893 -106.220 54.338  1.00 123.97 ? 41  THR   E CB  1 
ATOM   7811  O  OG1 . THR   E  5  42  ? -17.561 -105.035 53.903  1.00 121.72 ? 41  THR   E OG1 1 
ATOM   7812  C  CG2 . THR   E  5  42  ? -17.508 -106.721 55.627  1.00 124.55 ? 41  THR   E CG2 1 
ATOM   7813  N  N   . HIS   E  5  43  ? -14.784 -104.332 52.675  1.00 116.01 ? 42  HIS   E N   1 
ATOM   7814  C  CA  . HIS   E  5  43  ? -14.318 -103.907 51.326  1.00 116.93 ? 42  HIS   E CA  1 
ATOM   7815  C  C   . HIS   E  5  43  ? -13.380 -102.700 51.431  1.00 114.17 ? 42  HIS   E C   1 
ATOM   7816  O  O   . HIS   E  5  43  ? -13.519 -101.918 52.394  1.00 117.43 ? 42  HIS   E O   1 
ATOM   7817  C  CB  . HIS   E  5  43  ? -15.515 -103.593 50.418  1.00 120.19 ? 42  HIS   E CB  1 
ATOM   7818  C  CG  . HIS   E  5  43  ? -16.395 -104.763 50.135  1.00 120.88 ? 42  HIS   E CG  1 
ATOM   7819  N  ND1 . HIS   E  5  43  ? -17.332 -105.220 51.041  1.00 122.24 ? 42  HIS   E ND1 1 
ATOM   7820  C  CD2 . HIS   E  5  43  ? -16.501 -105.557 49.047  1.00 121.40 ? 42  HIS   E CD2 1 
ATOM   7821  C  CE1 . HIS   E  5  43  ? -17.969 -106.253 50.529  1.00 120.12 ? 42  HIS   E CE1 1 
ATOM   7822  N  NE2 . HIS   E  5  43  ? -17.479 -106.479 49.306  1.00 119.63 ? 42  HIS   E NE2 1 
ATOM   7823  N  N   . ALA   E  5  44  ? -12.467 -102.568 50.463  1.00 109.91 ? 43  ALA   E N   1 
ATOM   7824  C  CA  . ALA   E  5  44  ? -11.599 -101.388 50.237  1.00 108.48 ? 43  ALA   E CA  1 
ATOM   7825  C  C   . ALA   E  5  44  ? -11.825 -100.883 48.808  1.00 107.79 ? 43  ALA   E C   1 
ATOM   7826  O  O   . ALA   E  5  44  ? -11.844 -101.726 47.887  1.00 105.95 ? 43  ALA   E O   1 
ATOM   7827  C  CB  . ALA   E  5  44  ? -10.155 -101.749 50.470  1.00 106.03 ? 43  ALA   E CB  1 
ATOM   7828  N  N   . VAL   E  5  45  ? -11.988 -99.566  48.637  1.00 108.37 ? 44  VAL   E N   1 
ATOM   7829  C  CA  . VAL   E  5  45  ? -12.406 -98.934  47.348  1.00 105.39 ? 44  VAL   E CA  1 
ATOM   7830  C  C   . VAL   E  5  45  ? -11.402 -97.842  46.966  1.00 107.01 ? 44  VAL   E C   1 
ATOM   7831  O  O   . VAL   E  5  45  ? -11.091 -96.996  47.826  1.00 109.80 ? 44  VAL   E O   1 
ATOM   7832  C  CB  . VAL   E  5  45  ? -13.842 -98.378  47.439  1.00 104.09 ? 44  VAL   E CB  1 
ATOM   7833  C  CG1 . VAL   E  5  45  ? -14.195 -97.489  46.256  1.00 101.66 ? 44  VAL   E CG1 1 
ATOM   7834  C  CG2 . VAL   E  5  45  ? -14.860 -99.499  47.577  1.00 107.37 ? 44  VAL   E CG2 1 
ATOM   7835  N  N   . LEU   E  5  46  ? -10.921 -97.881  45.719  1.00 104.32 ? 45  LEU   E N   1 
ATOM   7836  C  CA  . LEU   E  5  46  ? -10.217 -96.757  45.047  1.00 104.70 ? 45  LEU   E CA  1 
ATOM   7837  C  C   . LEU   E  5  46  ? -11.207 -96.038  44.126  1.00 111.36 ? 45  LEU   E C   1 
ATOM   7838  O  O   . LEU   E  5  46  ? -12.017 -96.732  43.476  1.00 111.86 ? 45  LEU   E O   1 
ATOM   7839  C  CB  . LEU   E  5  46  ? -9.036  -97.290  44.231  1.00 100.66 ? 45  LEU   E CB  1 
ATOM   7840  C  CG  . LEU   E  5  46  ? -7.867  -97.859  45.029  1.00 99.20  ? 45  LEU   E CG  1 
ATOM   7841  C  CD1 . LEU   E  5  46  ? -6.917  -98.609  44.109  1.00 99.12  ? 45  LEU   E CD1 1 
ATOM   7842  C  CD2 . LEU   E  5  46  ? -7.129  -96.763  45.779  1.00 99.01  ? 45  LEU   E CD2 1 
ATOM   7843  N  N   . VAL   E  5  47  ? -11.136 -94.704  44.086  1.00 114.53 ? 46  VAL   E N   1 
ATOM   7844  C  CA  . VAL   E  5  47  ? -11.826 -93.837  43.084  1.00 114.81 ? 46  VAL   E CA  1 
ATOM   7845  C  C   . VAL   E  5  47  ? -10.787 -92.858  42.531  1.00 112.18 ? 46  VAL   E C   1 
ATOM   7846  O  O   . VAL   E  5  47  ? -10.102 -92.209  43.345  1.00 110.31 ? 46  VAL   E O   1 
ATOM   7847  C  CB  . VAL   E  5  47  ? -13.032 -93.093  43.690  1.00 118.83 ? 46  VAL   E CB  1 
ATOM   7848  C  CG1 . VAL   E  5  47  ? -13.807 -92.324  42.629  1.00 121.57 ? 46  VAL   E CG1 1 
ATOM   7849  C  CG2 . VAL   E  5  47  ? -13.958 -94.032  44.447  1.00 120.29 ? 46  VAL   E CG2 1 
ATOM   7850  N  N   . ALA   E  5  48  ? -10.674 -92.764  41.204  1.00 110.78 ? 47  ALA   E N   1 
ATOM   7851  C  CA  . ALA   E  5  48  ? -9.662  -91.936  40.508  1.00 112.66 ? 47  ALA   E CA  1 
ATOM   7852  C  C   . ALA   E  5  48  ? -10.328 -91.082  39.424  1.00 116.08 ? 47  ALA   E C   1 
ATOM   7853  O  O   . ALA   E  5  48  ? -11.117 -91.632  38.628  1.00 114.34 ? 47  ALA   E O   1 
ATOM   7854  C  CB  . ALA   E  5  48  ? -8.584  -92.820  39.931  1.00 110.64 ? 47  ALA   E CB  1 
ATOM   7855  N  N   . LEU   E  5  49  ? -10.015 -89.782  39.416  1.00 117.32 ? 48  LEU   E N   1 
ATOM   7856  C  CA  . LEU   E  5  49  ? -10.329 -88.843  38.308  1.00 121.33 ? 48  LEU   E CA  1 
ATOM   7857  C  C   . LEU   E  5  49  ? -9.234  -88.988  37.248  1.00 119.07 ? 48  LEU   E C   1 
ATOM   7858  O  O   . LEU   E  5  49  ? -8.064  -88.709  37.574  1.00 110.24 ? 48  LEU   E O   1 
ATOM   7859  C  CB  . LEU   E  5  49  ? -10.388 -87.411  38.850  1.00 123.83 ? 48  LEU   E CB  1 
ATOM   7860  C  CG  . LEU   E  5  49  ? -10.725 -86.330  37.823  1.00 129.44 ? 48  LEU   E CG  1 
ATOM   7861  C  CD1 . LEU   E  5  49  ? -12.185 -86.413  37.406  1.00 133.70 ? 48  LEU   E CD1 1 
ATOM   7862  C  CD2 . LEU   E  5  49  ? -10.405 -84.943  38.362  1.00 132.11 ? 48  LEU   E CD2 1 
ATOM   7863  N  N   . LYS   E  5  50  ? -9.597  -89.430  36.042  1.00 121.70 ? 49  LYS   E N   1 
ATOM   7864  C  CA  . LYS   E  5  50  ? -8.646  -89.636  34.918  1.00 122.41 ? 49  LYS   E CA  1 
ATOM   7865  C  C   . LYS   E  5  50  ? -8.506  -88.329  34.135  1.00 123.41 ? 49  LYS   E C   1 
ATOM   7866  O  O   . LYS   E  5  50  ? -9.481  -87.557  34.092  1.00 131.20 ? 49  LYS   E O   1 
ATOM   7867  C  CB  . LYS   E  5  50  ? -9.111  -90.776  34.010  1.00 118.93 ? 49  LYS   E CB  1 
ATOM   7868  C  CG  . LYS   E  5  50  ? -8.932  -92.169  34.592  1.00 116.93 ? 49  LYS   E CG  1 
ATOM   7869  C  CD  . LYS   E  5  50  ? -9.268  -93.267  33.611  1.00 115.84 ? 49  LYS   E CD  1 
ATOM   7870  C  CE  . LYS   E  5  50  ? -10.757 -93.424  33.389  1.00 116.73 ? 49  LYS   E CE  1 
ATOM   7871  N  NZ  . LYS   E  5  50  ? -11.058 -94.554  32.480  1.00 116.87 ? 49  LYS   E NZ  1 
ATOM   7872  N  N   . ARG   E  5  51  ? -7.336  -88.116  33.529  1.00 125.97 ? 50  ARG   E N   1 
ATOM   7873  C  CA  . ARG   E  5  51  ? -6.948  -86.853  32.849  1.00 126.43 ? 50  ARG   E CA  1 
ATOM   7874  C  C   . ARG   E  5  51  ? -6.561  -87.158  31.400  1.00 126.26 ? 50  ARG   E C   1 
ATOM   7875  O  O   . ARG   E  5  51  ? -5.807  -88.127  31.182  1.00 125.63 ? 50  ARG   E O   1 
ATOM   7876  C  CB  . ARG   E  5  51  ? -5.791  -86.195  33.605  1.00 129.85 ? 50  ARG   E CB  1 
ATOM   7877  C  CG  . ARG   E  5  51  ? -5.361  -84.844  33.051  1.00 133.18 ? 50  ARG   E CG  1 
ATOM   7878  C  CD  . ARG   E  5  51  ? -4.230  -84.253  33.868  1.00 135.02 ? 50  ARG   E CD  1 
ATOM   7879  N  NE  . ARG   E  5  51  ? -4.688  -83.725  35.147  1.00 137.66 ? 50  ARG   E NE  1 
ATOM   7880  C  CZ  . ARG   E  5  51  ? -3.897  -83.385  36.164  1.00 137.15 ? 50  ARG   E CZ  1 
ATOM   7881  N  NH1 . ARG   E  5  51  ? -2.583  -83.519  36.075  1.00 135.18 ? 50  ARG   E NH1 1 
ATOM   7882  N  NH2 . ARG   E  5  51  ? -4.430  -82.914  37.279  1.00 135.74 ? 50  ARG   E NH2 1 
ATOM   7883  N  N   . ASN   E  5  52  ? -7.055  -86.345  30.460  1.00 126.71 ? 51  ASN   E N   1 
ATOM   7884  C  CA  . ASN   E  5  52  ? -6.779  -86.456  29.002  1.00 126.09 ? 51  ASN   E CA  1 
ATOM   7885  C  C   . ASN   E  5  52  ? -5.806  -85.345  28.589  1.00 129.52 ? 51  ASN   E C   1 
ATOM   7886  O  O   . ASN   E  5  52  ? -5.630  -84.388  29.372  1.00 131.58 ? 51  ASN   E O   1 
ATOM   7887  C  CB  . ASN   E  5  52  ? -8.072  -86.413  28.180  1.00 126.94 ? 51  ASN   E CB  1 
ATOM   7888  C  CG  . ASN   E  5  52  ? -8.852  -85.122  28.327  1.00 128.11 ? 51  ASN   E CG  1 
ATOM   7889  O  OD1 . ASN   E  5  52  ? -8.599  -84.329  29.231  1.00 130.75 ? 51  ASN   E OD1 1 
ATOM   7890  N  ND2 . ASN   E  5  52  ? -9.817  -84.908  27.447  1.00 125.09 ? 51  ASN   E ND2 1 
ATOM   7891  N  N   . ALA   E  5  53  ? -5.196  -85.479  27.407  1.00 128.96 ? 52  ALA   E N   1 
ATOM   7892  C  CA  . ALA   E  5  53  ? -4.325  -84.457  26.779  1.00 127.71 ? 52  ALA   E CA  1 
ATOM   7893  C  C   . ALA   E  5  53  ? -5.206  -83.399  26.105  1.00 127.41 ? 52  ALA   E C   1 
ATOM   7894  O  O   . ALA   E  5  53  ? -4.916  -82.199  26.268  1.00 129.83 ? 52  ALA   E O   1 
ATOM   7895  C  CB  . ALA   E  5  53  ? -3.379  -85.108  25.801  1.00 127.13 ? 52  ALA   E CB  1 
ATOM   7896  N  N   . ASP   E  5  54  ? -6.239  -83.841  25.378  1.00 126.22 ? 53  ASP   E N   1 
ATOM   7897  C  CA  . ASP   E  5  54  ? -7.307  -82.983  24.794  1.00 129.02 ? 53  ASP   E CA  1 
ATOM   7898  C  C   . ASP   E  5  54  ? -8.539  -83.860  24.518  1.00 132.35 ? 53  ASP   E C   1 
ATOM   7899  O  O   . ASP   E  5  54  ? -8.574  -84.992  25.041  1.00 134.69 ? 53  ASP   E O   1 
ATOM   7900  C  CB  . ASP   E  5  54  ? -6.787  -82.223  23.568  1.00 130.40 ? 53  ASP   E CB  1 
ATOM   7901  C  CG  . ASP   E  5  54  ? -6.251  -83.101  22.450  1.00 129.01 ? 53  ASP   E CG  1 
ATOM   7902  O  OD1 . ASP   E  5  54  ? -6.707  -84.251  22.335  1.00 133.45 ? 53  ASP   E OD1 1 
ATOM   7903  O  OD2 . ASP   E  5  54  ? -5.382  -82.621  21.698  1.00 127.25 ? 53  ASP   E OD2 1 
ATOM   7904  N  N   . GLU   E  5  55  ? -9.507  -83.361  23.737  1.00 136.38 ? 54  GLU   E N   1 
ATOM   7905  C  CA  . GLU   E  5  55  ? -10.799 -84.051  23.446  1.00 139.65 ? 54  GLU   E CA  1 
ATOM   7906  C  C   . GLU   E  5  55  ? -10.617 -85.160  22.399  1.00 138.31 ? 54  GLU   E C   1 
ATOM   7907  O  O   . GLU   E  5  55  ? -11.580 -85.928  22.199  1.00 140.33 ? 54  GLU   E O   1 
ATOM   7908  C  CB  . GLU   E  5  55  ? -11.864 -83.055  22.975  1.00 144.32 ? 54  GLU   E CB  1 
ATOM   7909  C  CG  . GLU   E  5  55  ? -13.091 -83.005  23.871  1.00 149.94 ? 54  GLU   E CG  1 
ATOM   7910  C  CD  . GLU   E  5  55  ? -12.810 -82.756  25.343  1.00 152.03 ? 54  GLU   E CD  1 
ATOM   7911  O  OE1 . GLU   E  5  55  ? -13.269 -83.564  26.175  1.00 153.43 ? 54  GLU   E OE1 1 
ATOM   7912  O  OE2 . GLU   E  5  55  ? -12.134 -81.754  25.655  1.00 154.41 ? 54  GLU   E OE2 1 
ATOM   7913  N  N   . LEU   E  5  56  ? -9.448  -85.243  21.756  1.00 138.60 ? 55  LEU   E N   1 
ATOM   7914  C  CA  . LEU   E  5  56  ? -9.115  -86.310  20.772  1.00 133.26 ? 55  LEU   E CA  1 
ATOM   7915  C  C   . LEU   E  5  56  ? -8.418  -87.488  21.470  1.00 132.16 ? 55  LEU   E C   1 
ATOM   7916  O  O   . LEU   E  5  56  ? -8.419  -88.585  20.878  1.00 127.41 ? 55  LEU   E O   1 
ATOM   7917  C  CB  . LEU   E  5  56  ? -8.236  -85.722  19.661  1.00 133.96 ? 55  LEU   E CB  1 
ATOM   7918  C  CG  . LEU   E  5  56  ? -8.944  -85.356  18.354  1.00 133.80 ? 55  LEU   E CG  1 
ATOM   7919  C  CD1 . LEU   E  5  56  ? -10.335 -84.785  18.594  1.00 133.66 ? 55  LEU   E CD1 1 
ATOM   7920  C  CD2 . LEU   E  5  56  ? -8.107  -84.375  17.548  1.00 135.29 ? 55  LEU   E CD2 1 
ATOM   7921  N  N   . SER   E  5  57  ? -7.866  -87.285  22.674  1.00 126.01 ? 56  SER   E N   1 
ATOM   7922  C  CA  . SER   E  5  57  ? -7.007  -88.272  23.384  1.00 124.30 ? 56  SER   E CA  1 
ATOM   7923  C  C   . SER   E  5  57  ? -7.839  -89.161  24.318  1.00 126.07 ? 56  SER   E C   1 
ATOM   7924  O  O   . SER   E  5  57  ? -8.966  -88.762  24.680  1.00 127.25 ? 56  SER   E O   1 
ATOM   7925  C  CB  . SER   E  5  57  ? -5.892  -87.591  24.141  1.00 119.26 ? 56  SER   E CB  1 
ATOM   7926  O  OG  . SER   E  5  57  ? -6.348  -87.081  25.386  1.00 121.34 ? 56  SER   E OG  1 
ATOM   7927  N  N   . SER   E  5  58  ? -7.276  -90.318  24.692  1.00 123.26 ? 57  SER   E N   1 
ATOM   7928  C  CA  . SER   E  5  58  ? -7.778  -91.229  25.754  1.00 121.07 ? 57  SER   E CA  1 
ATOM   7929  C  C   . SER   E  5  58  ? -7.570  -90.571  27.120  1.00 120.94 ? 57  SER   E C   1 
ATOM   7930  O  O   . SER   E  5  58  ? -6.933  -89.500  27.176  1.00 116.05 ? 57  SER   E O   1 
ATOM   7931  C  CB  . SER   E  5  58  ? -7.083  -92.563  25.703  1.00 120.76 ? 57  SER   E CB  1 
ATOM   7932  O  OG  . SER   E  5  58  ? -5.674  -92.395  25.775  1.00 118.49 ? 57  SER   E OG  1 
ATOM   7933  N  N   . TYR   E  5  59  ? -8.072  -91.208  28.178  1.00 121.93 ? 58  TYR   E N   1 
ATOM   7934  C  CA  . TYR   E  5  59  ? -7.937  -90.752  29.584  1.00 120.56 ? 58  TYR   E CA  1 
ATOM   7935  C  C   . TYR   E  5  59  ? -6.936  -91.658  30.309  1.00 119.16 ? 58  TYR   E C   1 
ATOM   7936  O  O   . TYR   E  5  59  ? -7.235  -92.848  30.508  1.00 118.88 ? 58  TYR   E O   1 
ATOM   7937  C  CB  . TYR   E  5  59  ? -9.313  -90.705  30.251  1.00 121.87 ? 58  TYR   E CB  1 
ATOM   7938  C  CG  . TYR   E  5  59  ? -10.125 -89.490  29.881  1.00 121.16 ? 58  TYR   E CG  1 
ATOM   7939  C  CD1 . TYR   E  5  59  ? -10.829 -89.436  28.689  1.00 120.02 ? 58  TYR   E CD1 1 
ATOM   7940  C  CD2 . TYR   E  5  59  ? -10.175 -88.385  30.715  1.00 121.42 ? 58  TYR   E CD2 1 
ATOM   7941  C  CE1 . TYR   E  5  59  ? -11.571 -88.321  28.339  1.00 121.72 ? 58  TYR   E CE1 1 
ATOM   7942  C  CE2 . TYR   E  5  59  ? -10.910 -87.260  30.379  1.00 123.37 ? 58  TYR   E CE2 1 
ATOM   7943  C  CZ  . TYR   E  5  59  ? -11.611 -87.228  29.186  1.00 124.21 ? 58  TYR   E CZ  1 
ATOM   7944  O  OH  . TYR   E  5  59  ? -12.337 -86.123  28.847  1.00 128.78 ? 58  TYR   E OH  1 
ATOM   7945  N  N   . GLN   E  5  60  ? -5.780  -91.093  30.673  1.00 119.54 ? 59  GLN   E N   1 
ATOM   7946  C  CA  . GLN   E  5  60  ? -4.662  -91.784  31.370  1.00 121.12 ? 59  GLN   E CA  1 
ATOM   7947  C  C   . GLN   E  5  60  ? -5.228  -92.665  32.491  1.00 119.93 ? 59  GLN   E C   1 
ATOM   7948  O  O   . GLN   E  5  60  ? -5.835  -92.105  33.424  1.00 120.11 ? 59  GLN   E O   1 
ATOM   7949  C  CB  . GLN   E  5  60  ? -3.680  -90.753  31.931  1.00 124.32 ? 59  GLN   E CB  1 
ATOM   7950  C  CG  . GLN   E  5  60  ? -2.390  -91.358  32.465  1.00 127.43 ? 59  GLN   E CG  1 
ATOM   7951  C  CD  . GLN   E  5  60  ? -1.358  -91.593  31.388  1.00 130.98 ? 59  GLN   E CD  1 
ATOM   7952  O  OE1 . GLN   E  5  60  ? -1.674  -91.711  30.204  1.00 133.26 ? 59  GLN   E OE1 1 
ATOM   7953  N  NE2 . GLN   E  5  60  ? -0.102  -91.667  31.798  1.00 131.93 ? 59  GLN   E NE2 1 
ATOM   7954  N  N   . LYS   E  5  61  ? -5.044  -93.987  32.386  1.00 118.09 ? 60  LYS   E N   1 
ATOM   7955  C  CA  . LYS   E  5  61  ? -5.509  -94.987  33.389  1.00 117.90 ? 60  LYS   E CA  1 
ATOM   7956  C  C   . LYS   E  5  61  ? -4.687  -94.832  34.674  1.00 116.94 ? 60  LYS   E C   1 
ATOM   7957  O  O   . LYS   E  5  61  ? -3.443  -94.815  34.586  1.00 120.18 ? 60  LYS   E O   1 
ATOM   7958  C  CB  . LYS   E  5  61  ? -5.440  -96.420  32.844  1.00 118.86 ? 60  LYS   E CB  1 
ATOM   7959  C  CG  . LYS   E  5  61  ? -4.158  -96.816  32.120  1.00 122.13 ? 60  LYS   E CG  1 
ATOM   7960  C  CD  . LYS   E  5  61  ? -4.245  -98.185  31.475  1.00 125.70 ? 60  LYS   E CD  1 
ATOM   7961  C  CE  . LYS   E  5  61  ? -3.938  -99.322  32.427  1.00 126.70 ? 60  LYS   E CE  1 
ATOM   7962  N  NZ  . LYS   E  5  61  ? -2.480  -99.495  32.628  1.00 126.66 ? 60  LYS   E NZ  1 
ATOM   7963  N  N   . LYS   E  5  62  ? -5.376  -94.729  35.816  1.00 115.66 ? 61  LYS   E N   1 
ATOM   7964  C  CA  . LYS   E  5  62  ? -4.802  -94.363  37.140  1.00 115.58 ? 61  LYS   E CA  1 
ATOM   7965  C  C   . LYS   E  5  62  ? -4.675  -95.602  38.037  1.00 107.66 ? 61  LYS   E C   1 
ATOM   7966  O  O   . LYS   E  5  62  ? -3.890  -95.541  39.002  1.00 104.72 ? 61  LYS   E O   1 
ATOM   7967  C  CB  . LYS   E  5  62  ? -5.692  -93.319  37.827  1.00 119.73 ? 61  LYS   E CB  1 
ATOM   7968  C  CG  . LYS   E  5  62  ? -5.928  -92.036  37.039  1.00 122.67 ? 61  LYS   E CG  1 
ATOM   7969  C  CD  . LYS   E  5  62  ? -4.900  -90.956  37.303  1.00 125.16 ? 61  LYS   E CD  1 
ATOM   7970  C  CE  . LYS   E  5  62  ? -5.143  -90.213  38.600  1.00 125.91 ? 61  LYS   E CE  1 
ATOM   7971  N  NZ  . LYS   E  5  62  ? -3.949  -89.444  39.021  1.00 123.06 ? 61  LYS   E NZ  1 
ATOM   7972  N  N   . ILE   E  5  63  ? -5.420  -96.674  37.746  1.00 102.74 ? 62  ILE   E N   1 
ATOM   7973  C  CA  . ILE   E  5  63  ? -5.551  -97.868  38.635  1.00 100.65 ? 62  ILE   E CA  1 
ATOM   7974  C  C   . ILE   E  5  63  ? -4.874  -99.072  37.974  1.00 99.74  ? 62  ILE   E C   1 
ATOM   7975  O  O   . ILE   E  5  63  ? -5.072  -99.276  36.760  1.00 100.21 ? 62  ILE   E O   1 
ATOM   7976  C  CB  . ILE   E  5  63  ? -7.029  -98.148  38.967  1.00 99.82  ? 62  ILE   E CB  1 
ATOM   7977  C  CG1 . ILE   E  5  63  ? -7.665  -96.971  39.713  1.00 101.04 ? 62  ILE   E CG1 1 
ATOM   7978  C  CG2 . ILE   E  5  63  ? -7.166  -99.448  39.746  1.00 98.53  ? 62  ILE   E CG2 1 
ATOM   7979  C  CD1 . ILE   E  5  63  ? -9.170  -97.044  39.826  1.00 102.15 ? 62  ILE   E CD1 1 
ATOM   7980  N  N   . ILE   E  5  64  ? -4.118  -99.842  38.763  1.00 97.00  ? 63  ILE   E N   1 
ATOM   7981  C  CA  . ILE   E  5  64  ? -3.374  -101.055 38.312  1.00 98.99  ? 63  ILE   E CA  1 
ATOM   7982  C  C   . ILE   E  5  64  ? -3.645  -102.192 39.303  1.00 100.47 ? 63  ILE   E C   1 
ATOM   7983  O  O   . ILE   E  5  64  ? -3.626  -101.931 40.523  1.00 101.39 ? 63  ILE   E O   1 
ATOM   7984  C  CB  . ILE   E  5  64  ? -1.865  -100.766 38.176  1.00 97.62  ? 63  ILE   E CB  1 
ATOM   7985  C  CG1 . ILE   E  5  64  ? -1.597  -99.527  37.316  1.00 98.45  ? 63  ILE   E CG1 1 
ATOM   7986  C  CG2 . ILE   E  5  64  ? -1.133  -101.988 37.640  1.00 97.20  ? 63  ILE   E CG2 1 
ATOM   7987  C  CD1 . ILE   E  5  64  ? -0.192  -98.987  37.433  1.00 100.43 ? 63  ILE   E CD1 1 
ATOM   7988  N  N   . LYS   E  5  65  ? -3.885  -103.399 38.783  1.00 103.07 ? 64  LYS   E N   1 
ATOM   7989  C  CA  . LYS   E  5  65  ? -4.048  -104.650 39.570  1.00 104.99 ? 64  LYS   E CA  1 
ATOM   7990  C  C   . LYS   E  5  65  ? -2.664  -105.253 39.839  1.00 106.81 ? 64  LYS   E C   1 
ATOM   7991  O  O   . LYS   E  5  65  ? -1.857  -105.315 38.889  1.00 108.43 ? 64  LYS   E O   1 
ATOM   7992  C  CB  . LYS   E  5  65  ? -4.933  -105.634 38.802  1.00 105.77 ? 64  LYS   E CB  1 
ATOM   7993  C  CG  . LYS   E  5  65  ? -5.228  -106.940 39.523  1.00 107.60 ? 64  LYS   E CG  1 
ATOM   7994  C  CD  . LYS   E  5  65  ? -6.216  -107.810 38.778  1.00 108.35 ? 64  LYS   E CD  1 
ATOM   7995  C  CE  . LYS   E  5  65  ? -6.374  -109.190 39.377  1.00 104.80 ? 64  LYS   E CE  1 
ATOM   7996  N  NZ  . LYS   E  5  65  ? -7.324  -110.008 38.589  1.00 104.65 ? 64  LYS   E NZ  1 
ATOM   7997  N  N   . CYS   E  5  66  ? -2.409  -105.685 41.079  1.00 110.84 ? 65  CYS   E N   1 
ATOM   7998  C  CA  . CYS   E  5  66  ? -1.115  -106.266 41.538  1.00 115.39 ? 65  CYS   E CA  1 
ATOM   7999  C  C   . CYS   E  5  66  ? -1.239  -107.785 41.720  1.00 117.63 ? 65  CYS   E C   1 
ATOM   8000  O  O   . CYS   E  5  66  ? -0.315  -108.513 41.294  1.00 120.57 ? 65  CYS   E O   1 
ATOM   8001  C  CB  . CYS   E  5  66  ? -0.661  -105.618 42.838  1.00 111.70 ? 65  CYS   E CB  1 
ATOM   8002  S  SG  . CYS   E  5  66  ? -0.079  -103.918 42.611  1.00 111.58 ? 65  CYS   E SG  1 
ATOM   8003  N  N   . ASP   E  5  67  ? -2.323  -108.234 42.359  1.00 117.12 ? 66  ASP   E N   1 
ATOM   8004  C  CA  . ASP   E  5  67  ? -2.683  -109.668 42.516  1.00 116.71 ? 66  ASP   E CA  1 
ATOM   8005  C  C   . ASP   E  5  67  ? -4.213  -109.774 42.528  1.00 111.24 ? 66  ASP   E C   1 
ATOM   8006  O  O   . ASP   E  5  67  ? -4.873  -108.755 42.264  1.00 108.74 ? 66  ASP   E O   1 
ATOM   8007  C  CB  . ASP   E  5  67  ? -2.027  -110.255 43.771  1.00 120.62 ? 66  ASP   E CB  1 
ATOM   8008  C  CG  . ASP   E  5  67  ? -1.776  -111.754 43.707  1.00 127.40 ? 66  ASP   E CG  1 
ATOM   8009  O  OD1 . ASP   E  5  67  ? -2.361  -112.413 42.825  1.00 132.25 ? 66  ASP   E OD1 1 
ATOM   8010  O  OD2 . ASP   E  5  67  ? -0.998  -112.254 44.544  1.00 136.89 ? 66  ASP   E OD2 1 
ATOM   8011  N  N   . GLU   E  5  68  ? -4.753  -110.959 42.816  1.00 113.13 ? 67  GLU   E N   1 
ATOM   8012  C  CA  . GLU   E  5  68  ? -6.217  -111.211 42.900  1.00 115.22 ? 67  GLU   E CA  1 
ATOM   8013  C  C   . GLU   E  5  68  ? -6.804  -110.463 44.105  1.00 110.55 ? 67  GLU   E C   1 
ATOM   8014  O  O   . GLU   E  5  68  ? -8.021  -110.189 44.080  1.00 105.29 ? 67  GLU   E O   1 
ATOM   8015  C  CB  . GLU   E  5  68  ? -6.493  -112.714 42.999  1.00 120.84 ? 67  GLU   E CB  1 
ATOM   8016  C  CG  . GLU   E  5  68  ? -6.089  -113.492 41.758  1.00 123.26 ? 67  GLU   E CG  1 
ATOM   8017  C  CD  . GLU   E  5  68  ? -6.739  -113.014 40.471  1.00 128.87 ? 67  GLU   E CD  1 
ATOM   8018  O  OE1 . GLU   E  5  68  ? -7.956  -112.733 40.493  1.00 130.28 ? 67  GLU   E OE1 1 
ATOM   8019  O  OE2 . GLU   E  5  68  ? -6.024  -112.910 39.453  1.00 132.62 ? 67  GLU   E OE2 1 
ATOM   8020  N  N   . HIS   E  5  69  ? -5.969  -110.144 45.104  1.00 108.66 ? 68  HIS   E N   1 
ATOM   8021  C  CA  . HIS   E  5  69  ? -6.374  -109.593 46.427  1.00 108.10 ? 68  HIS   E CA  1 
ATOM   8022  C  C   . HIS   E  5  69  ? -5.768  -108.205 46.682  1.00 106.33 ? 68  HIS   E C   1 
ATOM   8023  O  O   . HIS   E  5  69  ? -5.997  -107.682 47.792  1.00 104.91 ? 68  HIS   E O   1 
ATOM   8024  C  CB  . HIS   E  5  69  ? -5.957  -110.559 47.545  1.00 108.56 ? 68  HIS   E CB  1 
ATOM   8025  C  CG  . HIS   E  5  69  ? -4.482  -110.607 47.759  1.00 107.34 ? 68  HIS   E CG  1 
ATOM   8026  N  ND1 . HIS   E  5  69  ? -3.868  -109.963 48.814  1.00 104.08 ? 68  HIS   E ND1 1 
ATOM   8027  C  CD2 . HIS   E  5  69  ? -3.496  -111.191 47.043  1.00 108.59 ? 68  HIS   E CD2 1 
ATOM   8028  C  CE1 . HIS   E  5  69  ? -2.569  -110.162 48.746  1.00 101.53 ? 68  HIS   E CE1 1 
ATOM   8029  N  NE2 . HIS   E  5  69  ? -2.313  -110.908 47.668  1.00 105.18 ? 68  HIS   E NE2 1 
ATOM   8030  N  N   . MET   E  5  70  ? -5.020  -107.634 45.727  1.00 105.32 ? 69  MET   E N   1 
ATOM   8031  C  CA  . MET   E  5  70  ? -4.289  -106.348 45.917  1.00 100.86 ? 69  MET   E CA  1 
ATOM   8032  C  C   . MET   E  5  70  ? -4.220  -105.553 44.604  1.00 98.36  ? 69  MET   E C   1 
ATOM   8033  O  O   . MET   E  5  70  ? -4.288  -106.162 43.521  1.00 97.45  ? 69  MET   E O   1 
ATOM   8034  C  CB  . MET   E  5  70  ? -2.866  -106.607 46.423  1.00 100.30 ? 69  MET   E CB  1 
ATOM   8035  C  CG  . MET   E  5  70  ? -2.284  -105.450 47.220  1.00 99.69  ? 69  MET   E CG  1 
ATOM   8036  S  SD  . MET   E  5  70  ? -0.529  -105.674 47.632  1.00 98.85  ? 69  MET   E SD  1 
ATOM   8037  C  CE  . MET   E  5  70  ? -0.622  -107.121 48.686  1.00 99.37  ? 69  MET   E CE  1 
ATOM   8038  N  N   . GLY   E  5  71  ? -4.089  -104.230 44.721  1.00 96.12  ? 70  GLY   E N   1 
ATOM   8039  C  CA  . GLY   E  5  71  ? -3.880  -103.287 43.604  1.00 98.79  ? 70  GLY   E CA  1 
ATOM   8040  C  C   . GLY   E  5  71  ? -3.742  -101.863 44.120  1.00 97.23  ? 70  GLY   E C   1 
ATOM   8041  O  O   . GLY   E  5  71  ? -3.998  -101.651 45.325  1.00 97.33  ? 70  GLY   E O   1 
ATOM   8042  N  N   . LEU   E  5  72  ? -3.357  -100.909 43.265  1.00 95.48  ? 71  LEU   E N   1 
ATOM   8043  C  CA  . LEU   E  5  72  ? -3.190  -99.493  43.692  1.00 95.42  ? 71  LEU   E CA  1 
ATOM   8044  C  C   . LEU   E  5  72  ? -3.735  -98.514  42.644  1.00 94.25  ? 71  LEU   E C   1 
ATOM   8045  O  O   . LEU   E  5  72  ? -4.082  -98.951  41.526  1.00 92.94  ? 71  LEU   E O   1 
ATOM   8046  C  CB  . LEU   E  5  72  ? -1.721  -99.221  44.055  1.00 94.58  ? 71  LEU   E CB  1 
ATOM   8047  C  CG  . LEU   E  5  72  ? -0.631  -99.249  42.972  1.00 92.49  ? 71  LEU   E CG  1 
ATOM   8048  C  CD1 . LEU   E  5  72  ? 0.116   -100.567 42.973  1.00 92.96  ? 71  LEU   E CD1 1 
ATOM   8049  C  CD2 . LEU   E  5  72  ? -1.130  -98.933  41.570  1.00 93.65  ? 71  LEU   E CD2 1 
ATOM   8050  N  N   . SER   E  5  73  ? -3.853  -97.242  43.041  1.00 94.13  ? 72  SER   E N   1 
ATOM   8051  C  CA  . SER   E  5  73  ? -4.082  -96.070  42.158  1.00 95.36  ? 72  SER   E CA  1 
ATOM   8052  C  C   . SER   E  5  73  ? -2.849  -95.163  42.230  1.00 95.30  ? 72  SER   E C   1 
ATOM   8053  O  O   . SER   E  5  73  ? -2.130  -95.227  43.250  1.00 93.29  ? 72  SER   E O   1 
ATOM   8054  C  CB  . SER   E  5  73  ? -5.349  -95.332  42.522  1.00 94.77  ? 72  SER   E CB  1 
ATOM   8055  O  OG  . SER   E  5  73  ? -5.167  -94.527  43.677  1.00 94.54  ? 72  SER   E OG  1 
ATOM   8056  N  N   . LEU   E  5  74  ? -2.615  -94.361  41.189  1.00 97.98  ? 73  LEU   E N   1 
ATOM   8057  C  CA  . LEU   E  5  74  ? -1.385  -93.538  41.029  1.00 96.60  ? 73  LEU   E CA  1 
ATOM   8058  C  C   . LEU   E  5  74  ? -1.757  -92.064  40.835  1.00 97.65  ? 73  LEU   E C   1 
ATOM   8059  O  O   . LEU   E  5  74  ? -2.853  -91.786  40.310  1.00 92.51  ? 73  LEU   E O   1 
ATOM   8060  C  CB  . LEU   E  5  74  ? -0.573  -94.078  39.845  1.00 96.88  ? 73  LEU   E CB  1 
ATOM   8061  C  CG  . LEU   E  5  74  ? -1.188  -93.883  38.458  1.00 97.75  ? 73  LEU   E CG  1 
ATOM   8062  C  CD1 . LEU   E  5  74  ? -0.574  -92.688  37.744  1.00 97.71  ? 73  LEU   E CD1 1 
ATOM   8063  C  CD2 . LEU   E  5  74  ? -1.025  -95.137  37.612  1.00 97.10  ? 73  LEU   E CD2 1 
ATOM   8064  N  N   . ALA   E  5  75  ? -0.863  -91.171  41.268  1.00 98.46  ? 74  ALA   E N   1 
ATOM   8065  C  CA  . ALA   E  5  75  ? -0.887  -89.712  41.010  1.00 102.27 ? 74  ALA   E CA  1 
ATOM   8066  C  C   . ALA   E  5  75  ? 0.557   -89.222  40.864  1.00 99.91  ? 74  ALA   E C   1 
ATOM   8067  O  O   . ALA   E  5  75  ? 1.316   -89.330  41.848  1.00 96.27  ? 74  ALA   E O   1 
ATOM   8068  C  CB  . ALA   E  5  75  ? -1.611  -88.996  42.124  1.00 103.68 ? 74  ALA   E CB  1 
ATOM   8069  N  N   . GLY   E  5  76  ? 0.923   -88.737  39.673  1.00 102.39 ? 75  GLY   E N   1 
ATOM   8070  C  CA  . GLY   E  5  76  ? 2.280   -88.257  39.344  1.00 103.91 ? 75  GLY   E CA  1 
ATOM   8071  C  C   . GLY   E  5  76  ? 2.814   -88.913  38.082  1.00 103.08 ? 75  GLY   E C   1 
ATOM   8072  O  O   . GLY   E  5  76  ? 2.000   -89.179  37.172  1.00 102.90 ? 75  GLY   E O   1 
ATOM   8073  N  N   . LEU   E  5  77  ? 4.128   -89.164  38.023  1.00 103.67 ? 76  LEU   E N   1 
ATOM   8074  C  CA  . LEU   E  5  77  ? 4.801   -89.832  36.873  1.00 106.61 ? 76  LEU   E CA  1 
ATOM   8075  C  C   . LEU   E  5  77  ? 4.262   -91.262  36.735  1.00 106.91 ? 76  LEU   E C   1 
ATOM   8076  O  O   . LEU   E  5  77  ? 4.539   -92.089  37.625  1.00 106.38 ? 76  LEU   E O   1 
ATOM   8077  C  CB  . LEU   E  5  77  ? 6.322   -89.844  37.075  1.00 108.05 ? 76  LEU   E CB  1 
ATOM   8078  C  CG  . LEU   E  5  77  ? 7.096   -88.664  36.488  1.00 111.14 ? 76  LEU   E CG  1 
ATOM   8079  C  CD1 . LEU   E  5  77  ? 8.574   -88.777  36.834  1.00 112.80 ? 76  LEU   E CD1 1 
ATOM   8080  C  CD2 . LEU   E  5  77  ? 6.916   -88.573  34.979  1.00 110.68 ? 76  LEU   E CD2 1 
ATOM   8081  N  N   . ALA   E  5  78  ? 3.529   -91.536  35.652  1.00 108.61 ? 77  ALA   E N   1 
ATOM   8082  C  CA  . ALA   E  5  78  ? 2.858   -92.829  35.381  1.00 107.49 ? 77  ALA   E CA  1 
ATOM   8083  C  C   . ALA   E  5  78  ? 3.879   -93.933  35.100  1.00 104.78 ? 77  ALA   E C   1 
ATOM   8084  O  O   . ALA   E  5  78  ? 3.676   -95.066  35.529  1.00 105.09 ? 77  ALA   E O   1 
ATOM   8085  C  CB  . ALA   E  5  78  ? 1.877   -92.675  34.245  1.00 108.83 ? 77  ALA   E CB  1 
ATOM   8086  N  N   . PRO   E  5  79  ? 4.990   -93.676  34.366  1.00 104.20 ? 78  PRO   E N   1 
ATOM   8087  C  CA  . PRO   E  5  79  ? 6.015   -94.701  34.156  1.00 102.66 ? 78  PRO   E CA  1 
ATOM   8088  C  C   . PRO   E  5  79  ? 6.636   -95.214  35.465  1.00 103.25 ? 78  PRO   E C   1 
ATOM   8089  O  O   . PRO   E  5  79  ? 6.952   -96.383  35.531  1.00 106.49 ? 78  PRO   E O   1 
ATOM   8090  C  CB  . PRO   E  5  79  ? 7.089   -93.995  33.317  1.00 101.64 ? 78  PRO   E CB  1 
ATOM   8091  C  CG  . PRO   E  5  79  ? 6.351   -92.858  32.648  1.00 103.03 ? 78  PRO   E CG  1 
ATOM   8092  C  CD  . PRO   E  5  79  ? 5.313   -92.424  33.662  1.00 104.66 ? 78  PRO   E CD  1 
ATOM   8093  N  N   . ASP   E  5  80  ? 6.808   -94.332  36.455  1.00 104.01 ? 79  ASP   E N   1 
ATOM   8094  C  CA  . ASP   E  5  80  ? 7.347   -94.674  37.800  1.00 103.53 ? 79  ASP   E CA  1 
ATOM   8095  C  C   . ASP   E  5  80  ? 6.357   -95.598  38.522  1.00 100.43 ? 79  ASP   E C   1 
ATOM   8096  O  O   . ASP   E  5  80  ? 6.824   -96.502  39.244  1.00 97.12  ? 79  ASP   E O   1 
ATOM   8097  C  CB  . ASP   E  5  80  ? 7.656   -93.415  38.619  1.00 102.53 ? 79  ASP   E CB  1 
ATOM   8098  C  CG  . ASP   E  5  80  ? 8.886   -92.653  38.151  1.00 102.08 ? 79  ASP   E CG  1 
ATOM   8099  O  OD1 . ASP   E  5  80  ? 9.481   -93.057  37.128  1.00 104.60 ? 79  ASP   E OD1 1 
ATOM   8100  O  OD2 . ASP   E  5  80  ? 9.244   -91.660  38.815  1.00 99.60  ? 79  ASP   E OD2 1 
ATOM   8101  N  N   . ALA   E  5  81  ? 5.050   -95.384  38.333  1.00 101.28 ? 80  ALA   E N   1 
ATOM   8102  C  CA  . ALA   E  5  81  ? 3.966   -96.218  38.908  1.00 102.57 ? 80  ALA   E CA  1 
ATOM   8103  C  C   . ALA   E  5  81  ? 3.998   -97.610  38.268  1.00 100.86 ? 80  ALA   E C   1 
ATOM   8104  O  O   . ALA   E  5  81  ? 3.716   -98.598  38.978  1.00 101.24 ? 80  ALA   E O   1 
ATOM   8105  C  CB  . ALA   E  5  81  ? 2.623   -95.556  38.709  1.00 104.34 ? 80  ALA   E CB  1 
ATOM   8106  N  N   . ARG   E  5  82  ? 4.325   -97.675  36.973  1.00 98.90  ? 81  ARG   E N   1 
ATOM   8107  C  CA  . ARG   E  5  82  ? 4.448   -98.942  36.205  1.00 94.79  ? 81  ARG   E CA  1 
ATOM   8108  C  C   . ARG   E  5  82  ? 5.623   -99.762  36.759  1.00 93.90  ? 81  ARG   E C   1 
ATOM   8109  O  O   . ARG   E  5  82  ? 5.466   -100.994 36.875  1.00 95.24  ? 81  ARG   E O   1 
ATOM   8110  C  CB  . ARG   E  5  82  ? 4.600   -98.659  34.708  1.00 95.24  ? 81  ARG   E CB  1 
ATOM   8111  C  CG  . ARG   E  5  82  ? 4.917   -99.895  33.882  1.00 93.15  ? 81  ARG   E CG  1 
ATOM   8112  C  CD  . ARG   E  5  82  ? 4.634   -99.697  32.408  1.00 95.62  ? 81  ARG   E CD  1 
ATOM   8113  N  NE  . ARG   E  5  82  ? 5.296   -100.712 31.602  1.00 95.68  ? 81  ARG   E NE  1 
ATOM   8114  C  CZ  . ARG   E  5  82  ? 4.932   -101.988 31.526  1.00 97.55  ? 81  ARG   E CZ  1 
ATOM   8115  N  NH1 . ARG   E  5  82  ? 3.893   -102.438 32.212  1.00 99.03  ? 81  ARG   E NH1 1 
ATOM   8116  N  NH2 . ARG   E  5  82  ? 5.617   -102.820 30.760  1.00 101.53 ? 81  ARG   E NH2 1 
ATOM   8117  N  N   . VAL   E  5  83  ? 6.745   -99.111  37.091  1.00 87.36  ? 82  VAL   E N   1 
ATOM   8118  C  CA  . VAL   E  5  83  ? 7.947   -99.768  37.692  1.00 84.16  ? 82  VAL   E CA  1 
ATOM   8119  C  C   . VAL   E  5  83  ? 7.572   -100.323 39.072  1.00 86.46  ? 82  VAL   E C   1 
ATOM   8120  O  O   . VAL   E  5  83  ? 7.861   -101.508 39.325  1.00 85.60  ? 82  VAL   E O   1 
ATOM   8121  C  CB  . VAL   E  5  83  ? 9.149   -98.808  37.792  1.00 82.03  ? 82  VAL   E CB  1 
ATOM   8122  C  CG1 . VAL   E  5  83  ? 10.282  -99.398  38.618  1.00 80.45  ? 82  VAL   E CG1 1 
ATOM   8123  C  CG2 . VAL   E  5  83  ? 9.659   -98.399  36.421  1.00 84.35  ? 82  VAL   E CG2 1 
ATOM   8124  N  N   . LEU   E  5  84  ? 6.965   -99.493  39.925  1.00 87.00  ? 83  LEU   E N   1 
ATOM   8125  C  CA  . LEU   E  5  84  ? 6.642   -99.832  41.339  1.00 88.82  ? 83  LEU   E CA  1 
ATOM   8126  C  C   . LEU   E  5  84  ? 5.524   -100.882 41.401  1.00 90.93  ? 83  LEU   E C   1 
ATOM   8127  O  O   . LEU   E  5  84  ? 5.592   -101.741 42.303  1.00 88.36  ? 83  LEU   E O   1 
ATOM   8128  C  CB  . LEU   E  5  84  ? 6.248   -98.562  42.103  1.00 89.62  ? 83  LEU   E CB  1 
ATOM   8129  C  CG  . LEU   E  5  84  ? 7.398   -97.615  42.443  1.00 90.79  ? 83  LEU   E CG  1 
ATOM   8130  C  CD1 . LEU   E  5  84  ? 6.872   -96.296  42.985  1.00 91.81  ? 83  LEU   E CD1 1 
ATOM   8131  C  CD2 . LEU   E  5  84  ? 8.361   -98.251  43.437  1.00 91.53  ? 83  LEU   E CD2 1 
ATOM   8132  N  N   . SER   E  5  85  ? 4.533   -100.816 40.502  1.00 92.99  ? 84  SER   E N   1 
ATOM   8133  C  CA  . SER   E  5  85  ? 3.431   -101.812 40.406  1.00 94.51  ? 84  SER   E CA  1 
ATOM   8134  C  C   . SER   E  5  85  ? 4.003   -103.166 39.965  1.00 94.75  ? 84  SER   E C   1 
ATOM   8135  O  O   . SER   E  5  85  ? 3.634   -104.192 40.576  1.00 93.98  ? 84  SER   E O   1 
ATOM   8136  C  CB  . SER   E  5  85  ? 2.330   -101.359 39.479  1.00 95.25  ? 84  SER   E CB  1 
ATOM   8137  O  OG  . SER   E  5  85  ? 2.831   -101.119 38.174  1.00 97.15  ? 84  SER   E OG  1 
ATOM   8138  N  N   . ASN   E  5  86  ? 4.871   -103.157 38.947  1.00 93.44  ? 85  ASN   E N   1 
ATOM   8139  C  CA  . ASN   E  5  86  ? 5.549   -104.364 38.402  1.00 94.32  ? 85  ASN   E CA  1 
ATOM   8140  C  C   . ASN   E  5  86  ? 6.372   -105.045 39.502  1.00 94.13  ? 85  ASN   E C   1 
ATOM   8141  O  O   . ASN   E  5  86  ? 6.395   -106.290 39.530  1.00 94.98  ? 85  ASN   E O   1 
ATOM   8142  C  CB  . ASN   E  5  86  ? 6.448   -104.033 37.210  1.00 94.64  ? 85  ASN   E CB  1 
ATOM   8143  C  CG  . ASN   E  5  86  ? 6.927   -105.279 36.498  1.00 96.44  ? 85  ASN   E CG  1 
ATOM   8144  O  OD1 . ASN   E  5  86  ? 8.007   -105.786 36.790  1.00 97.18  ? 85  ASN   E OD1 1 
ATOM   8145  N  ND2 . ASN   E  5  86  ? 6.116   -105.799 35.589  1.00 97.16  ? 85  ASN   E ND2 1 
ATOM   8146  N  N   . TYR   E  5  87  ? 7.038   -104.259 40.356  1.00 92.99  ? 86  TYR   E N   1 
ATOM   8147  C  CA  . TYR   E  5  87  ? 7.807   -104.753 41.529  1.00 92.93  ? 86  TYR   E CA  1 
ATOM   8148  C  C   . TYR   E  5  87  ? 6.851   -105.446 42.506  1.00 89.86  ? 86  TYR   E C   1 
ATOM   8149  O  O   . TYR   E  5  87  ? 7.176   -106.554 42.950  1.00 91.90  ? 86  TYR   E O   1 
ATOM   8150  C  CB  . TYR   E  5  87  ? 8.564   -103.619 42.224  1.00 92.21  ? 86  TYR   E CB  1 
ATOM   8151  C  CG  . TYR   E  5  87  ? 9.287   -104.044 43.477  1.00 90.06  ? 86  TYR   E CG  1 
ATOM   8152  C  CD1 . TYR   E  5  87  ? 10.417  -104.842 43.411  1.00 89.34  ? 86  TYR   E CD1 1 
ATOM   8153  C  CD2 . TYR   E  5  87  ? 8.834   -103.664 44.731  1.00 90.35  ? 86  TYR   E CD2 1 
ATOM   8154  C  CE1 . TYR   E  5  87  ? 11.085  -105.244 44.556  1.00 89.84  ? 86  TYR   E CE1 1 
ATOM   8155  C  CE2 . TYR   E  5  87  ? 9.490   -104.057 45.886  1.00 90.15  ? 86  TYR   E CE2 1 
ATOM   8156  C  CZ  . TYR   E  5  87  ? 10.619  -104.852 45.798  1.00 91.09  ? 86  TYR   E CZ  1 
ATOM   8157  O  OH  . TYR   E  5  87  ? 11.268  -105.243 46.933  1.00 95.02  ? 86  TYR   E OH  1 
ATOM   8158  N  N   . LEU   E  5  88  ? 5.717   -104.811 42.824  1.00 91.54  ? 87  LEU   E N   1 
ATOM   8159  C  CA  . LEU   E  5  88  ? 4.680   -105.370 43.736  1.00 92.47  ? 87  LEU   E CA  1 
ATOM   8160  C  C   . LEU   E  5  88  ? 4.125   -106.676 43.162  1.00 94.41  ? 87  LEU   E C   1 
ATOM   8161  O  O   . LEU   E  5  88  ? 3.932   -107.623 43.948  1.00 94.28  ? 87  LEU   E O   1 
ATOM   8162  C  CB  . LEU   E  5  88  ? 3.545   -104.363 43.949  1.00 96.50  ? 87  LEU   E CB  1 
ATOM   8163  C  CG  . LEU   E  5  88  ? 3.409   -103.813 45.367  1.00 99.64  ? 87  LEU   E CG  1 
ATOM   8164  C  CD1 . LEU   E  5  88  ? 2.218   -102.871 45.465  1.00 103.29 ? 87  LEU   E CD1 1 
ATOM   8165  C  CD2 . LEU   E  5  88  ? 3.278   -104.935 46.387  1.00 99.22  ? 87  LEU   E CD2 1 
ATOM   8166  N  N   . ARG   E  5  89  ? 3.855   -106.712 41.854  1.00 92.44  ? 88  ARG   E N   1 
ATOM   8167  C  CA  . ARG   E  5  89  ? 3.323   -107.915 41.157  1.00 95.11  ? 88  ARG   E CA  1 
ATOM   8168  C  C   . ARG   E  5  89  ? 4.268   -109.101 41.398  1.00 91.95  ? 88  ARG   E C   1 
ATOM   8169  O  O   . ARG   E  5  89  ? 3.761   -110.188 41.728  1.00 91.79  ? 88  ARG   E O   1 
ATOM   8170  C  CB  . ARG   E  5  89  ? 3.123   -107.638 39.665  1.00 94.31  ? 88  ARG   E CB  1 
ATOM   8171  C  CG  . ARG   E  5  89  ? 1.865   -106.841 39.352  1.00 94.36  ? 88  ARG   E CG  1 
ATOM   8172  C  CD  . ARG   E  5  89  ? 1.814   -106.437 37.894  1.00 94.65  ? 88  ARG   E CD  1 
ATOM   8173  N  NE  . ARG   E  5  89  ? 0.516   -105.903 37.506  1.00 94.64  ? 88  ARG   E NE  1 
ATOM   8174  C  CZ  . ARG   E  5  89  ? 0.216   -105.466 36.288  1.00 97.16  ? 88  ARG   E CZ  1 
ATOM   8175  N  NH1 . ARG   E  5  89  ? 1.125   -105.492 35.327  1.00 95.91  ? 88  ARG   E NH1 1 
ATOM   8176  N  NH2 . ARG   E  5  89  ? -0.996  -104.999 36.035  1.00 101.58 ? 88  ARG   E NH2 1 
ATOM   8177  N  N   . GLN   E  5  90  ? 5.582   -108.882 41.261  1.00 90.95  ? 89  GLN   E N   1 
ATOM   8178  C  CA  . GLN   E  5  90  ? 6.643   -109.906 41.471  1.00 89.01  ? 89  GLN   E CA  1 
ATOM   8179  C  C   . GLN   E  5  90  ? 6.674   -110.338 42.943  1.00 91.83  ? 89  GLN   E C   1 
ATOM   8180  O  O   . GLN   E  5  90  ? 6.767   -111.555 43.191  1.00 95.53  ? 89  GLN   E O   1 
ATOM   8181  C  CB  . GLN   E  5  90  ? 8.010   -109.370 41.042  1.00 88.69  ? 89  GLN   E CB  1 
ATOM   8182  C  CG  . GLN   E  5  90  ? 8.200   -109.339 39.533  1.00 91.09  ? 89  GLN   E CG  1 
ATOM   8183  C  CD  . GLN   E  5  90  ? 9.409   -108.537 39.120  1.00 94.94  ? 89  GLN   E CD  1 
ATOM   8184  O  OE1 . GLN   E  5  90  ? 10.155  -108.023 39.951  1.00 97.08  ? 89  GLN   E OE1 1 
ATOM   8185  N  NE2 . GLN   E  5  90  ? 9.609   -108.420 37.817  1.00 99.44  ? 89  GLN   E NE2 1 
ATOM   8186  N  N   . GLN   E  5  91  ? 6.610   -109.386 43.879  1.00 88.85  ? 90  GLN   E N   1 
ATOM   8187  C  CA  . GLN   E  5  91  ? 6.677   -109.654 45.343  1.00 87.63  ? 90  GLN   E CA  1 
ATOM   8188  C  C   . GLN   E  5  91  ? 5.455   -110.476 45.768  1.00 89.96  ? 90  GLN   E C   1 
ATOM   8189  O  O   . GLN   E  5  91  ? 5.650   -111.460 46.509  1.00 89.49  ? 90  GLN   E O   1 
ATOM   8190  C  CB  . GLN   E  5  91  ? 6.786   -108.351 46.141  1.00 85.46  ? 90  GLN   E CB  1 
ATOM   8191  C  CG  . GLN   E  5  91  ? 8.148   -107.680 46.028  1.00 84.15  ? 90  GLN   E CG  1 
ATOM   8192  C  CD  . GLN   E  5  91  ? 9.277   -108.633 46.337  1.00 84.87  ? 90  GLN   E CD  1 
ATOM   8193  O  OE1 . GLN   E  5  91  ? 9.283   -109.296 47.372  1.00 85.31  ? 90  GLN   E OE1 1 
ATOM   8194  N  NE2 . GLN   E  5  91  ? 10.236  -108.722 45.428  1.00 83.48  ? 90  GLN   E NE2 1 
ATOM   8195  N  N   . CYS   E  5  92  ? 4.255   -110.090 45.317  1.00 89.10  ? 91  CYS   E N   1 
ATOM   8196  C  CA  . CYS   E  5  92  ? 2.987   -110.848 45.516  1.00 91.95  ? 91  CYS   E CA  1 
ATOM   8197  C  C   . CYS   E  5  92  ? 3.124   -112.258 44.933  1.00 90.77  ? 91  CYS   E C   1 
ATOM   8198  O  O   . CYS   E  5  92  ? 2.630   -113.218 45.559  1.00 91.49  ? 91  CYS   E O   1 
ATOM   8199  C  CB  . CYS   E  5  92  ? 1.803   -110.177 44.833  1.00 96.48  ? 91  CYS   E CB  1 
ATOM   8200  S  SG  . CYS   E  5  92  ? 1.139   -108.761 45.745  1.00 104.55 ? 91  CYS   E SG  1 
ATOM   8201  N  N   . ASN   E  5  93  ? 3.755   -112.354 43.762  1.00 89.85  ? 92  ASN   E N   1 
ATOM   8202  C  CA  . ASN   E  5  93  ? 3.910   -113.607 42.981  1.00 88.82  ? 92  ASN   E CA  1 
ATOM   8203  C  C   . ASN   E  5  93  ? 4.905   -114.530 43.695  1.00 91.11  ? 92  ASN   E C   1 
ATOM   8204  O  O   . ASN   E  5  93  ? 4.577   -115.717 43.867  1.00 92.76  ? 92  ASN   E O   1 
ATOM   8205  C  CB  . ASN   E  5  93  ? 4.331   -113.302 41.541  1.00 86.62  ? 92  ASN   E CB  1 
ATOM   8206  C  CG  . ASN   E  5  93  ? 4.032   -114.421 40.570  1.00 85.79  ? 92  ASN   E CG  1 
ATOM   8207  O  OD1 . ASN   E  5  93  ? 4.750   -114.589 39.591  1.00 88.32  ? 92  ASN   E OD1 1 
ATOM   8208  N  ND2 . ASN   E  5  93  ? 2.979   -115.181 40.824  1.00 89.49  ? 92  ASN   E ND2 1 
ATOM   8209  N  N   . TYR   E  5  94  ? 6.065   -114.002 44.102  1.00 89.18  ? 93  TYR   E N   1 
ATOM   8210  C  CA  . TYR   E  5  94  ? 7.116   -114.739 44.856  1.00 89.41  ? 93  TYR   E CA  1 
ATOM   8211  C  C   . TYR   E  5  94  ? 6.486   -115.412 46.080  1.00 89.26  ? 93  TYR   E C   1 
ATOM   8212  O  O   . TYR   E  5  94  ? 6.735   -116.610 46.295  1.00 89.93  ? 93  TYR   E O   1 
ATOM   8213  C  CB  . TYR   E  5  94  ? 8.251   -113.805 45.281  1.00 90.38  ? 93  TYR   E CB  1 
ATOM   8214  C  CG  . TYR   E  5  94  ? 9.389   -114.482 46.005  1.00 92.47  ? 93  TYR   E CG  1 
ATOM   8215  C  CD1 . TYR   E  5  94  ? 10.423  -115.083 45.304  1.00 91.64  ? 93  TYR   E CD1 1 
ATOM   8216  C  CD2 . TYR   E  5  94  ? 9.440   -114.518 47.390  1.00 92.69  ? 93  TYR   E CD2 1 
ATOM   8217  C  CE1 . TYR   E  5  94  ? 11.477  -115.704 45.957  1.00 91.47  ? 93  TYR   E CE1 1 
ATOM   8218  C  CE2 . TYR   E  5  94  ? 10.486  -115.136 48.059  1.00 93.59  ? 93  TYR   E CE2 1 
ATOM   8219  C  CZ  . TYR   E  5  94  ? 11.509  -115.734 47.340  1.00 93.97  ? 93  TYR   E CZ  1 
ATOM   8220  O  OH  . TYR   E  5  94  ? 12.548  -116.352 47.980  1.00 93.37  ? 93  TYR   E OH  1 
ATOM   8221  N  N   . SER   E  5  95  ? 5.696   -114.658 46.851  1.00 86.49  ? 94  SER   E N   1 
ATOM   8222  C  CA  . SER   E  5  95  ? 4.986   -115.127 48.071  1.00 88.23  ? 94  SER   E CA  1 
ATOM   8223  C  C   . SER   E  5  95  ? 4.107   -116.340 47.738  1.00 91.30  ? 94  SER   E C   1 
ATOM   8224  O  O   . SER   E  5  95  ? 4.124   -117.313 48.520  1.00 93.73  ? 94  SER   E O   1 
ATOM   8225  C  CB  . SER   E  5  95  ? 4.176   -114.013 48.686  1.00 85.86  ? 94  SER   E CB  1 
ATOM   8226  O  OG  . SER   E  5  95  ? 3.628   -114.406 49.935  1.00 87.04  ? 94  SER   E OG  1 
ATOM   8227  N  N   . SER   E  5  96  ? 3.373   -116.285 46.621  1.00 92.46  ? 95  SER   E N   1 
ATOM   8228  C  CA  . SER   E  5  96  ? 2.434   -117.346 46.163  1.00 94.50  ? 95  SER   E CA  1 
ATOM   8229  C  C   . SER   E  5  96  ? 3.199   -118.605 45.741  1.00 93.80  ? 95  SER   E C   1 
ATOM   8230  O  O   . SER   E  5  96  ? 2.818   -119.699 46.190  1.00 93.84  ? 95  SER   E O   1 
ATOM   8231  C  CB  . SER   E  5  96  ? 1.555   -116.859 45.043  1.00 96.74  ? 95  SER   E CB  1 
ATOM   8232  O  OG  . SER   E  5  96  ? 0.626   -115.898 45.518  1.00 100.27 ? 95  SER   E OG  1 
ATOM   8233  N  N   . LEU   E  5  97  ? 4.218   -118.464 44.891  1.00 93.06  ? 96  LEU   E N   1 
ATOM   8234  C  CA  . LEU   E  5  97  ? 4.959   -119.619 44.320  1.00 93.84  ? 96  LEU   E CA  1 
ATOM   8235  C  C   . LEU   E  5  97  ? 5.756   -120.321 45.426  1.00 93.89  ? 96  LEU   E C   1 
ATOM   8236  O  O   . LEU   E  5  97  ? 5.666   -121.565 45.503  1.00 95.27  ? 96  LEU   E O   1 
ATOM   8237  C  CB  . LEU   E  5  97  ? 5.870   -119.149 43.179  1.00 95.24  ? 96  LEU   E CB  1 
ATOM   8238  C  CG  . LEU   E  5  97  ? 5.157   -118.582 41.950  1.00 98.89  ? 96  LEU   E CG  1 
ATOM   8239  C  CD1 . LEU   E  5  97  ? 6.162   -118.182 40.880  1.00 100.45 ? 96  LEU   E CD1 1 
ATOM   8240  C  CD2 . LEU   E  5  97  ? 4.144   -119.569 41.381  1.00 100.30 ? 96  LEU   E CD2 1 
ATOM   8241  N  N   . VAL   E  5  98  ? 6.474   -119.565 46.265  1.00 88.59  ? 97  VAL   E N   1 
ATOM   8242  C  CA  . VAL   E  5  98  ? 7.475   -120.121 47.227  1.00 88.10  ? 97  VAL   E CA  1 
ATOM   8243  C  C   . VAL   E  5  98  ? 6.781   -120.576 48.515  1.00 88.45  ? 97  VAL   E C   1 
ATOM   8244  O  O   . VAL   E  5  98  ? 7.166   -121.645 49.018  1.00 92.17  ? 97  VAL   E O   1 
ATOM   8245  C  CB  . VAL   E  5  98  ? 8.606   -119.122 47.530  1.00 86.67  ? 97  VAL   E CB  1 
ATOM   8246  C  CG1 . VAL   E  5  98  ? 9.590   -119.674 48.552  1.00 87.62  ? 97  VAL   E CG1 1 
ATOM   8247  C  CG2 . VAL   E  5  98  ? 9.338   -118.714 46.262  1.00 87.84  ? 97  VAL   E CG2 1 
ATOM   8248  N  N   . PHE   E  5  99  ? 5.826   -119.802 49.040  1.00 87.12  ? 98  PHE   E N   1 
ATOM   8249  C  CA  . PHE   E  5  99  ? 5.192   -120.057 50.363  1.00 89.39  ? 98  PHE   E CA  1 
ATOM   8250  C  C   . PHE   E  5  99  ? 3.703   -120.406 50.230  1.00 90.67  ? 98  PHE   E C   1 
ATOM   8251  O  O   . PHE   E  5  99  ? 3.074   -120.647 51.276  1.00 93.30  ? 98  PHE   E O   1 
ATOM   8252  C  CB  . PHE   E  5  99  ? 5.375   -118.846 51.280  1.00 88.20  ? 98  PHE   E CB  1 
ATOM   8253  C  CG  . PHE   E  5  99  ? 6.810   -118.542 51.619  1.00 87.94  ? 98  PHE   E CG  1 
ATOM   8254  C  CD1 . PHE   E  5  99  ? 7.478   -119.267 52.596  1.00 85.40  ? 98  PHE   E CD1 1 
ATOM   8255  C  CD2 . PHE   E  5  99  ? 7.496   -117.536 50.958  1.00 87.34  ? 98  PHE   E CD2 1 
ATOM   8256  C  CE1 . PHE   E  5  99  ? 8.801   -118.990 52.904  1.00 82.84  ? 98  PHE   E CE1 1 
ATOM   8257  C  CE2 . PHE   E  5  99  ? 8.819   -117.260 51.268  1.00 85.75  ? 98  PHE   E CE2 1 
ATOM   8258  C  CZ  . PHE   E  5  99  ? 9.469   -117.988 52.238  1.00 83.26  ? 98  PHE   E CZ  1 
ATOM   8259  N  N   . ASN   E  5  100 ? 3.150   -120.443 49.014  1.00 93.79  ? 99  ASN   E N   1 
ATOM   8260  C  CA  . ASN   E  5  100 ? 1.698   -120.679 48.784  1.00 97.11  ? 99  ASN   E CA  1 
ATOM   8261  C  C   . ASN   E  5  100 ? 0.911   -119.756 49.721  1.00 96.93  ? 99  ASN   E C   1 
ATOM   8262  O  O   . ASN   E  5  100 ? -0.034  -120.234 50.381  1.00 98.59  ? 99  ASN   E O   1 
ATOM   8263  C  CB  . ASN   E  5  100 ? 1.330   -122.152 48.984  1.00 98.97  ? 99  ASN   E CB  1 
ATOM   8264  C  CG  . ASN   E  5  100 ? -0.049  -122.529 48.480  1.00 104.06 ? 99  ASN   E CG  1 
ATOM   8265  O  OD1 . ASN   E  5  100 ? -0.571  -123.577 48.854  1.00 111.07 ? 99  ASN   E OD1 1 
ATOM   8266  N  ND2 . ASN   E  5  100 ? -0.655  -121.706 47.636  1.00 104.24 ? 99  ASN   E ND2 1 
ATOM   8267  N  N   . ARG   E  5  101 ? 1.314   -118.484 49.773  1.00 98.73  ? 100 ARG   E N   1 
ATOM   8268  C  CA  . ARG   E  5  101 ? 0.841   -117.467 50.748  1.00 97.82  ? 100 ARG   E CA  1 
ATOM   8269  C  C   . ARG   E  5  101 ? 0.521   -116.174 49.994  1.00 96.50  ? 100 ARG   E C   1 
ATOM   8270  O  O   . ARG   E  5  101 ? 1.344   -115.762 49.155  1.00 91.77  ? 100 ARG   E O   1 
ATOM   8271  C  CB  . ARG   E  5  101 ? 1.924   -117.229 51.805  1.00 96.80  ? 100 ARG   E CB  1 
ATOM   8272  C  CG  . ARG   E  5  101 ? 1.516   -116.319 52.954  1.00 94.00  ? 100 ARG   E CG  1 
ATOM   8273  C  CD  . ARG   E  5  101 ? 2.661   -116.186 53.938  1.00 93.56  ? 100 ARG   E CD  1 
ATOM   8274  N  NE  . ARG   E  5  101 ? 2.279   -115.538 55.185  1.00 92.73  ? 100 ARG   E NE  1 
ATOM   8275  C  CZ  . ARG   E  5  101 ? 3.062   -115.433 56.256  1.00 94.12  ? 100 ARG   E CZ  1 
ATOM   8276  N  NH1 . ARG   E  5  101 ? 4.284   -115.941 56.245  1.00 91.04  ? 100 ARG   E NH1 1 
ATOM   8277  N  NH2 . ARG   E  5  101 ? 2.618   -114.820 57.341  1.00 96.79  ? 100 ARG   E NH2 1 
ATOM   8278  N  N   . LYS   E  5  102 ? -0.630  -115.566 50.282  1.00 98.58  ? 101 LYS   E N   1 
ATOM   8279  C  CA  . LYS   E  5  102 ? -1.012  -114.238 49.737  1.00 99.50  ? 101 LYS   E CA  1 
ATOM   8280  C  C   . LYS   E  5  102 ? -0.252  -113.165 50.525  1.00 99.02  ? 101 LYS   E C   1 
ATOM   8281  O  O   . LYS   E  5  102 ? -0.330  -113.188 51.769  1.00 103.36 ? 101 LYS   E O   1 
ATOM   8282  C  CB  . LYS   E  5  102 ? -2.529  -114.049 49.805  1.00 102.31 ? 101 LYS   E CB  1 
ATOM   8283  C  CG  . LYS   E  5  102 ? -3.316  -114.903 48.823  1.00 105.49 ? 101 LYS   E CG  1 
ATOM   8284  C  CD  . LYS   E  5  102 ? -4.777  -115.010 49.175  1.00 110.26 ? 101 LYS   E CD  1 
ATOM   8285  C  CE  . LYS   E  5  102 ? -5.632  -115.439 48.004  1.00 117.34 ? 101 LYS   E CE  1 
ATOM   8286  N  NZ  . LYS   E  5  102 ? -7.003  -115.791 48.440  1.00 123.44 ? 101 LYS   E NZ  1 
ATOM   8287  N  N   . LEU   E  5  103 ? 0.473   -112.286 49.825  1.00 96.66  ? 102 LEU   E N   1 
ATOM   8288  C  CA  . LEU   E  5  103 ? 1.317   -111.220 50.430  1.00 94.46  ? 102 LEU   E CA  1 
ATOM   8289  C  C   . LEU   E  5  103 ? 0.430   -110.285 51.259  1.00 96.64  ? 102 LEU   E C   1 
ATOM   8290  O  O   . LEU   E  5  103 ? -0.527  -109.729 50.696  1.00 96.80  ? 102 LEU   E O   1 
ATOM   8291  C  CB  . LEU   E  5  103 ? 2.038   -110.453 49.316  1.00 91.46  ? 102 LEU   E CB  1 
ATOM   8292  C  CG  . LEU   E  5  103 ? 3.053   -109.404 49.772  1.00 87.68  ? 102 LEU   E CG  1 
ATOM   8293  C  CD1 . LEU   E  5  103 ? 4.221   -110.045 50.505  1.00 85.29  ? 102 LEU   E CD1 1 
ATOM   8294  C  CD2 . LEU   E  5  103 ? 3.556   -108.595 48.587  1.00 86.62  ? 102 LEU   E CD2 1 
ATOM   8295  N  N   . ALA   E  5  104 ? 0.737   -110.126 52.550  1.00 101.18 ? 103 ALA   E N   1 
ATOM   8296  C  CA  . ALA   E  5  104 ? 0.039   -109.201 53.475  1.00 102.09 ? 103 ALA   E CA  1 
ATOM   8297  C  C   . ALA   E  5  104 ? 0.213   -107.762 52.975  1.00 101.48 ? 103 ALA   E C   1 
ATOM   8298  O  O   . ALA   E  5  104 ? 1.365   -107.369 52.695  1.00 93.62  ? 103 ALA   E O   1 
ATOM   8299  C  CB  . ALA   E  5  104 ? 0.570   -109.364 54.878  1.00 105.42 ? 103 ALA   E CB  1 
ATOM   8300  N  N   . VAL   E  5  105 ? -0.891  -107.011 52.879  1.00 102.17 ? 104 VAL   E N   1 
ATOM   8301  C  CA  . VAL   E  5  105 ? -0.929  -105.609 52.357  1.00 101.56 ? 104 VAL   E CA  1 
ATOM   8302  C  C   . VAL   E  5  105 ? 0.100   -104.770 53.126  1.00 99.87  ? 104 VAL   E C   1 
ATOM   8303  O  O   . VAL   E  5  105 ? 0.663   -103.837 52.525  1.00 97.99  ? 104 VAL   E O   1 
ATOM   8304  C  CB  . VAL   E  5  105 ? -2.343  -104.996 52.448  1.00 102.34 ? 104 VAL   E CB  1 
ATOM   8305  C  CG1 . VAL   E  5  105 ? -2.365  -103.548 51.979  1.00 104.50 ? 104 VAL   E CG1 1 
ATOM   8306  C  CG2 . VAL   E  5  105 ? -3.371  -105.804 51.671  1.00 102.81 ? 104 VAL   E CG2 1 
ATOM   8307  N  N   . GLU   E  5  106 ? 0.339   -105.098 54.400  1.00 101.26 ? 105 GLU   E N   1 
ATOM   8308  C  CA  . GLU   E  5  106 ? 1.313   -104.394 55.277  1.00 102.15 ? 105 GLU   E CA  1 
ATOM   8309  C  C   . GLU   E  5  106 ? 2.740   -104.621 54.760  1.00 102.06 ? 105 GLU   E C   1 
ATOM   8310  O  O   . GLU   E  5  106 ? 3.484   -103.628 54.662  1.00 97.08  ? 105 GLU   E O   1 
ATOM   8311  C  CB  . GLU   E  5  106 ? 1.172   -104.858 56.727  1.00 108.74 ? 105 GLU   E CB  1 
ATOM   8312  C  CG  . GLU   E  5  106 ? 1.705   -103.849 57.725  1.00 115.92 ? 105 GLU   E CG  1 
ATOM   8313  C  CD  . GLU   E  5  106 ? 1.513   -104.228 59.184  1.00 124.94 ? 105 GLU   E CD  1 
ATOM   8314  O  OE1 . GLU   E  5  106 ? 2.504   -104.173 59.941  1.00 127.76 ? 105 GLU   E OE1 1 
ATOM   8315  O  OE2 . GLU   E  5  106 ? 0.371   -104.563 59.563  1.00 137.23 ? 105 GLU   E OE2 1 
ATOM   8316  N  N   . ARG   E  5  107 ? 3.107   -105.871 54.447  1.00 101.24 ? 106 ARG   E N   1 
ATOM   8317  C  CA  . ARG   E  5  107 ? 4.439   -106.231 53.880  1.00 101.25 ? 106 ARG   E CA  1 
ATOM   8318  C  C   . ARG   E  5  107 ? 4.622   -105.523 52.531  1.00 96.54  ? 106 ARG   E C   1 
ATOM   8319  O  O   . ARG   E  5  107 ? 5.736   -105.021 52.280  1.00 92.55  ? 106 ARG   E O   1 
ATOM   8320  C  CB  . ARG   E  5  107 ? 4.609   -107.749 53.735  1.00 102.41 ? 106 ARG   E CB  1 
ATOM   8321  C  CG  . ARG   E  5  107 ? 5.106   -108.445 54.995  1.00 103.99 ? 106 ARG   E CG  1 
ATOM   8322  C  CD  . ARG   E  5  107 ? 5.808   -109.757 54.703  1.00 104.67 ? 106 ARG   E CD  1 
ATOM   8323  N  NE  . ARG   E  5  107 ? 7.232   -109.576 54.425  1.00 107.81 ? 106 ARG   E NE  1 
ATOM   8324  C  CZ  . ARG   E  5  107 ? 7.866   -109.935 53.305  1.00 107.75 ? 106 ARG   E CZ  1 
ATOM   8325  N  NH1 . ARG   E  5  107 ? 7.222   -110.520 52.307  1.00 110.38 ? 106 ARG   E NH1 1 
ATOM   8326  N  NH2 . ARG   E  5  107 ? 9.164   -109.713 53.191  1.00 106.33 ? 106 ARG   E NH2 1 
ATOM   8327  N  N   . ALA   E  5  108 ? 3.571   -105.481 51.705  1.00 94.08  ? 107 ALA   E N   1 
ATOM   8328  C  CA  . ALA   E  5  108 ? 3.543   -104.777 50.400  1.00 95.99  ? 107 ALA   E CA  1 
ATOM   8329  C  C   . ALA   E  5  108 ? 4.016   -103.331 50.596  1.00 96.75  ? 107 ALA   E C   1 
ATOM   8330  O  O   . ALA   E  5  108 ? 4.839   -102.858 49.785  1.00 96.31  ? 107 ALA   E O   1 
ATOM   8331  C  CB  . ALA   E  5  108 ? 2.156   -104.831 49.809  1.00 96.25  ? 107 ALA   E CB  1 
ATOM   8332  N  N   . GLY   E  5  109 ? 3.522   -102.674 51.650  1.00 96.30  ? 108 GLY   E N   1 
ATOM   8333  C  CA  . GLY   E  5  109 ? 3.919   -101.311 52.049  1.00 96.06  ? 108 GLY   E CA  1 
ATOM   8334  C  C   . GLY   E  5  109 ? 5.397   -101.245 52.390  1.00 95.38  ? 108 GLY   E C   1 
ATOM   8335  O  O   . GLY   E  5  109 ? 6.095   -100.394 51.807  1.00 94.60  ? 108 GLY   E O   1 
ATOM   8336  N  N   . HIS   E  5  110 ? 5.860   -102.133 53.277  1.00 95.42  ? 109 HIS   E N   1 
ATOM   8337  C  CA  . HIS   E  5  110 ? 7.257   -102.188 53.790  1.00 95.60  ? 109 HIS   E CA  1 
ATOM   8338  C  C   . HIS   E  5  110 ? 8.238   -102.356 52.624  1.00 93.27  ? 109 HIS   E C   1 
ATOM   8339  O  O   . HIS   E  5  110 ? 9.326   -101.753 52.682  1.00 94.70  ? 109 HIS   E O   1 
ATOM   8340  C  CB  . HIS   E  5  110 ? 7.428   -103.317 54.817  1.00 98.11  ? 109 HIS   E CB  1 
ATOM   8341  C  CG  . HIS   E  5  110 ? 6.613   -103.157 56.058  1.00 103.61 ? 109 HIS   E CG  1 
ATOM   8342  N  ND1 . HIS   E  5  110 ? 6.675   -102.024 56.847  1.00 102.00 ? 109 HIS   E ND1 1 
ATOM   8343  C  CD2 . HIS   E  5  110 ? 5.736   -103.991 56.661  1.00 107.02 ? 109 HIS   E CD2 1 
ATOM   8344  C  CE1 . HIS   E  5  110 ? 5.858   -102.162 57.873  1.00 106.62 ? 109 HIS   E CE1 1 
ATOM   8345  N  NE2 . HIS   E  5  110 ? 5.272   -103.360 57.783  1.00 106.76 ? 109 HIS   E NE2 1 
ATOM   8346  N  N   . LEU   E  5  111 ? 7.867   -103.150 51.615  1.00 94.67  ? 110 LEU   E N   1 
ATOM   8347  C  CA  . LEU   E  5  111 ? 8.718   -103.464 50.434  1.00 96.19  ? 110 LEU   E CA  1 
ATOM   8348  C  C   . LEU   E  5  111 ? 8.836   -102.234 49.529  1.00 94.17  ? 110 LEU   E C   1 
ATOM   8349  O  O   . LEU   E  5  111 ? 9.944   -102.000 49.007  1.00 94.56  ? 110 LEU   E O   1 
ATOM   8350  C  CB  . LEU   E  5  111 ? 8.119   -104.651 49.675  1.00 99.04  ? 110 LEU   E CB  1 
ATOM   8351  C  CG  . LEU   E  5  111 ? 8.261   -106.005 50.368  1.00 99.33  ? 110 LEU   E CG  1 
ATOM   8352  C  CD1 . LEU   E  5  111 ? 7.309   -107.025 49.765  1.00 102.12 ? 110 LEU   E CD1 1 
ATOM   8353  C  CD2 . LEU   E  5  111 ? 9.696   -106.505 50.298  1.00 99.98  ? 110 LEU   E CD2 1 
ATOM   8354  N  N   . LEU   E  5  112 ? 7.740   -101.491 49.343  1.00 96.13  ? 111 LEU   E N   1 
ATOM   8355  C  CA  . LEU   E  5  112 ? 7.719   -100.247 48.526  1.00 98.34  ? 111 LEU   E CA  1 
ATOM   8356  C  C   . LEU   E  5  112 ? 8.577   -99.181  49.214  1.00 99.37  ? 111 LEU   E C   1 
ATOM   8357  O  O   . LEU   E  5  112 ? 9.412   -98.568  48.518  1.00 102.50 ? 111 LEU   E O   1 
ATOM   8358  C  CB  . LEU   E  5  112 ? 6.276   -99.768  48.332  1.00 99.36  ? 111 LEU   E CB  1 
ATOM   8359  C  CG  . LEU   E  5  112 ? 5.433   -100.589 47.356  1.00 98.29  ? 111 LEU   E CG  1 
ATOM   8360  C  CD1 . LEU   E  5  112 ? 3.995   -100.095 47.336  1.00 99.37  ? 111 LEU   E CD1 1 
ATOM   8361  C  CD2 . LEU   E  5  112 ? 6.021   -100.555 45.952  1.00 99.68  ? 111 LEU   E CD2 1 
ATOM   8362  N  N   . CYS   E  5  113 ? 8.384   -98.986  50.524  1.00 100.99 ? 112 CYS   E N   1 
ATOM   8363  C  CA  . CYS   E  5  113 ? 9.156   -98.035  51.374  1.00 101.36 ? 112 CYS   E CA  1 
ATOM   8364  C  C   . CYS   E  5  113 ? 10.660  -98.234  51.146  1.00 101.87 ? 112 CYS   E C   1 
ATOM   8365  O  O   . CYS   E  5  113 ? 11.355  -97.233  50.880  1.00 99.67  ? 112 CYS   E O   1 
ATOM   8366  C  CB  . CYS   E  5  113 ? 8.823   -98.215  52.852  1.00 103.01 ? 112 CYS   E CB  1 
ATOM   8367  S  SG  . CYS   E  5  113 ? 9.949   -97.340  53.972  1.00 102.86 ? 112 CYS   E SG  1 
ATOM   8368  N  N   . ASP   E  5  114 ? 11.132  -99.482  51.232  1.00 100.77 ? 113 ASP   E N   1 
ATOM   8369  C  CA  . ASP   E  5  114 ? 12.576  -99.836  51.183  1.00 102.61 ? 113 ASP   E CA  1 
ATOM   8370  C  C   . ASP   E  5  114 ? 13.108  -99.655  49.755  1.00 94.83  ? 113 ASP   E C   1 
ATOM   8371  O  O   . ASP   E  5  114 ? 14.311  -99.350  49.617  1.00 91.94  ? 113 ASP   E O   1 
ATOM   8372  C  CB  . ASP   E  5  114 ? 12.815  -101.257 51.703  1.00 106.69 ? 113 ASP   E CB  1 
ATOM   8373  C  CG  . ASP   E  5  114 ? 12.511  -101.436 53.182  1.00 111.40 ? 113 ASP   E CG  1 
ATOM   8374  O  OD1 . ASP   E  5  114 ? 12.445  -100.414 53.900  1.00 118.74 ? 113 ASP   E OD1 1 
ATOM   8375  O  OD2 . ASP   E  5  114 ? 12.344  -102.601 53.609  1.00 110.62 ? 113 ASP   E OD2 1 
ATOM   8376  N  N   . LYS   E  5  115 ? 12.257  -99.831  48.738  1.00 92.95  ? 114 LYS   E N   1 
ATOM   8377  C  CA  . LYS   E  5  115 ? 12.656  -99.711  47.310  1.00 95.73  ? 114 LYS   E CA  1 
ATOM   8378  C  C   . LYS   E  5  115 ? 12.835  -98.232  46.963  1.00 94.81  ? 114 LYS   E C   1 
ATOM   8379  O  O   . LYS   E  5  115 ? 13.812  -97.905  46.260  1.00 93.91  ? 114 LYS   E O   1 
ATOM   8380  C  CB  . LYS   E  5  115 ? 11.631  -100.352 46.370  1.00 98.98  ? 114 LYS   E CB  1 
ATOM   8381  C  CG  . LYS   E  5  115 ? 12.231  -100.895 45.080  1.00 101.69 ? 114 LYS   E CG  1 
ATOM   8382  C  CD  . LYS   E  5  115 ? 11.321  -100.809 43.876  1.00 105.60 ? 114 LYS   E CD  1 
ATOM   8383  C  CE  . LYS   E  5  115 ? 11.822  -101.626 42.701  1.00 108.58 ? 114 LYS   E CE  1 
ATOM   8384  N  NZ  . LYS   E  5  115 ? 13.139  -101.154 42.208  1.00 111.15 ? 114 LYS   E NZ  1 
ATOM   8385  N  N   . ALA   E  5  116 ? 11.916  -97.386  47.437  1.00 96.27  ? 115 ALA   E N   1 
ATOM   8386  C  CA  . ALA   E  5  116 ? 11.927  -95.917  47.242  1.00 97.39  ? 115 ALA   E CA  1 
ATOM   8387  C  C   . ALA   E  5  116 ? 13.117  -95.303  47.992  1.00 97.41  ? 115 ALA   E C   1 
ATOM   8388  O  O   . ALA   E  5  116 ? 13.745  -94.382  47.434  1.00 102.58 ? 115 ALA   E O   1 
ATOM   8389  C  CB  . ALA   E  5  116 ? 10.613  -95.325  47.695  1.00 98.66  ? 115 ALA   E CB  1 
ATOM   8390  N  N   . GLN   E  5  117 ? 13.418  -95.810  49.193  1.00 94.88  ? 116 GLN   E N   1 
ATOM   8391  C  CA  . GLN   E  5  117 ? 14.456  -95.264  50.112  1.00 97.52  ? 116 GLN   E CA  1 
ATOM   8392  C  C   . GLN   E  5  117 ? 15.835  -95.318  49.444  1.00 98.02  ? 116 GLN   E C   1 
ATOM   8393  O  O   . GLN   E  5  117 ? 16.569  -94.318  49.538  1.00 97.92  ? 116 GLN   E O   1 
ATOM   8394  C  CB  . GLN   E  5  117 ? 14.466  -96.040  51.432  1.00 100.35 ? 116 GLN   E CB  1 
ATOM   8395  C  CG  . GLN   E  5  117 ? 15.373  -95.437  52.502  1.00 103.78 ? 116 GLN   E CG  1 
ATOM   8396  C  CD  . GLN   E  5  117 ? 16.850  -95.708  52.318  1.00 103.31 ? 116 GLN   E CD  1 
ATOM   8397  O  OE1 . GLN   E  5  117 ? 17.686  -94.834  52.540  1.00 106.68 ? 116 GLN   E OE1 1 
ATOM   8398  N  NE2 . GLN   E  5  117 ? 17.195  -96.923  51.921  1.00 103.82 ? 116 GLN   E NE2 1 
ATOM   8399  N  N   . LYS   E  5  118 ? 16.174  -96.442  48.807  1.00 101.82 ? 117 LYS   E N   1 
ATOM   8400  C  CA  . LYS   E  5  118 ? 17.514  -96.697  48.207  1.00 103.73 ? 117 LYS   E CA  1 
ATOM   8401  C  C   . LYS   E  5  118 ? 17.820  -95.647  47.130  1.00 100.86 ? 117 LYS   E C   1 
ATOM   8402  O  O   . LYS   E  5  118 ? 19.011  -95.326  46.938  1.00 103.82 ? 117 LYS   E O   1 
ATOM   8403  C  CB  . LYS   E  5  118 ? 17.580  -98.119  47.640  1.00 106.48 ? 117 LYS   E CB  1 
ATOM   8404  C  CG  . LYS   E  5  118 ? 17.677  -99.211  48.697  1.00 108.63 ? 117 LYS   E CG  1 
ATOM   8405  C  CD  . LYS   E  5  118 ? 17.468  -100.607 48.159  1.00 111.29 ? 117 LYS   E CD  1 
ATOM   8406  C  CE  . LYS   E  5  118 ? 17.652  -101.674 49.217  1.00 113.13 ? 117 LYS   E CE  1 
ATOM   8407  N  NZ  . LYS   E  5  118 ? 17.605  -103.036 48.636  1.00 112.80 ? 117 LYS   E NZ  1 
ATOM   8408  N  N   . ASN   E  5  119 ? 16.783  -95.117  46.478  1.00 95.84  ? 118 ASN   E N   1 
ATOM   8409  C  CA  . ASN   E  5  119 ? 16.901  -94.114  45.386  1.00 97.56  ? 118 ASN   E CA  1 
ATOM   8410  C  C   . ASN   E  5  119 ? 17.154  -92.713  45.965  1.00 98.53  ? 118 ASN   E C   1 
ATOM   8411  O  O   . ASN   E  5  119 ? 17.371  -91.789  45.157  1.00 98.74  ? 118 ASN   E O   1 
ATOM   8412  C  CB  . ASN   E  5  119 ? 15.662  -94.136  44.486  1.00 94.71  ? 118 ASN   E CB  1 
ATOM   8413  C  CG  . ASN   E  5  119 ? 15.710  -95.225  43.435  1.00 94.50  ? 118 ASN   E CG  1 
ATOM   8414  O  OD1 . ASN   E  5  119 ? 15.559  -94.946  42.249  1.00 88.03  ? 118 ASN   E OD1 1 
ATOM   8415  N  ND2 . ASN   E  5  119 ? 15.926  -96.463  43.851  1.00 95.01  ? 118 ASN   E ND2 1 
ATOM   8416  N  N   . THR   E  5  120 ? 17.142  -92.554  47.297  1.00 100.96 ? 119 THR   E N   1 
ATOM   8417  C  CA  . THR   E  5  120 ? 17.269  -91.240  47.991  1.00 100.12 ? 119 THR   E CA  1 
ATOM   8418  C  C   . THR   E  5  120 ? 18.599  -91.121  48.753  1.00 100.02 ? 119 THR   E C   1 
ATOM   8419  O  O   . THR   E  5  120 ? 18.802  -90.062  49.384  1.00 96.01  ? 119 THR   E O   1 
ATOM   8420  C  CB  . THR   E  5  120 ? 16.096  -90.981  48.950  1.00 98.71  ? 119 THR   E CB  1 
ATOM   8421  O  OG1 . THR   E  5  120 ? 16.176  -91.889  50.049  1.00 97.97  ? 119 THR   E OG1 1 
ATOM   8422  C  CG2 . THR   E  5  120 ? 14.743  -91.105  48.285  1.00 97.37  ? 119 THR   E CG2 1 
ATOM   8423  N  N   . GLN   E  5  121 ? 19.467  -92.140  48.708  1.00 100.55 ? 120 GLN   E N   1 
ATOM   8424  C  CA  . GLN   E  5  121 ? 20.737  -92.166  49.489  1.00 102.01 ? 120 GLN   E CA  1 
ATOM   8425  C  C   . GLN   E  5  121 ? 21.961  -92.360  48.577  1.00 104.09 ? 120 GLN   E C   1 
ATOM   8426  O  O   . GLN   E  5  121 ? 23.086  -92.171  49.085  1.00 94.96  ? 120 GLN   E O   1 
ATOM   8427  C  CB  . GLN   E  5  121 ? 20.655  -93.252  50.568  1.00 103.03 ? 120 GLN   E CB  1 
ATOM   8428  C  CG  . GLN   E  5  121 ? 21.702  -93.105  51.669  1.00 102.16 ? 120 GLN   E CG  1 
ATOM   8429  C  CD  . GLN   E  5  121 ? 21.439  -93.899  52.928  1.00 99.94  ? 120 GLN   E CD  1 
ATOM   8430  O  OE1 . GLN   E  5  121 ? 22.085  -93.682  53.951  1.00 95.01  ? 120 GLN   E OE1 1 
ATOM   8431  N  NE2 . GLN   E  5  121 ? 20.499  -94.832  52.881  1.00 99.81  ? 120 GLN   E NE2 1 
ATOM   8432  N  N   . SER   E  5  122 ? 21.775  -92.693  47.291  1.00 108.03 ? 121 SER   E N   1 
ATOM   8433  C  CA  . SER   E  5  122 ? 22.873  -93.026  46.341  1.00 109.12 ? 121 SER   E CA  1 
ATOM   8434  C  C   . SER   E  5  122 ? 22.989  -91.965  45.240  1.00 112.52 ? 121 SER   E C   1 
ATOM   8435  O  O   . SER   E  5  122 ? 21.945  -91.426  44.819  1.00 111.79 ? 121 SER   E O   1 
ATOM   8436  C  CB  . SER   E  5  122 ? 22.685  -94.394  45.739  1.00 109.86 ? 121 SER   E CB  1 
ATOM   8437  O  OG  . SER   E  5  122 ? 22.690  -95.392  46.747  1.00 103.92 ? 121 SER   E OG  1 
ATOM   8438  N  N   . TYR   E  5  123 ? 24.220  -91.709  44.785  1.00 115.40 ? 122 TYR   E N   1 
ATOM   8439  C  CA  . TYR   E  5  123 ? 24.554  -90.779  43.673  1.00 120.74 ? 122 TYR   E CA  1 
ATOM   8440  C  C   . TYR   E  5  123 ? 24.109  -91.405  42.349  1.00 120.07 ? 122 TYR   E C   1 
ATOM   8441  O  O   . TYR   E  5  123 ? 24.183  -92.642  42.224  1.00 122.50 ? 122 TYR   E O   1 
ATOM   8442  C  CB  . TYR   E  5  123 ? 26.053  -90.467  43.639  1.00 128.24 ? 122 TYR   E CB  1 
ATOM   8443  C  CG  . TYR   E  5  123 ? 26.501  -89.709  42.413  1.00 142.22 ? 122 TYR   E CG  1 
ATOM   8444  C  CD1 . TYR   E  5  123 ? 26.125  -88.390  42.208  1.00 147.98 ? 122 TYR   E CD1 1 
ATOM   8445  C  CD2 . TYR   E  5  123 ? 27.288  -90.314  41.446  1.00 146.43 ? 122 TYR   E CD2 1 
ATOM   8446  C  CE1 . TYR   E  5  123 ? 26.528  -87.691  41.081  1.00 150.78 ? 122 TYR   E CE1 1 
ATOM   8447  C  CE2 . TYR   E  5  123 ? 27.699  -89.631  40.312  1.00 151.46 ? 122 TYR   E CE2 1 
ATOM   8448  C  CZ  . TYR   E  5  123 ? 27.318  -88.313  40.129  1.00 155.70 ? 122 TYR   E CZ  1 
ATOM   8449  O  OH  . TYR   E  5  123 ? 27.720  -87.635  39.014  1.00 158.39 ? 122 TYR   E OH  1 
ATOM   8450  N  N   . GLY   E  5  124 ? 23.654  -90.572  41.408  1.00 119.33 ? 123 GLY   E N   1 
ATOM   8451  C  CA  . GLY   E  5  124 ? 23.267  -90.981  40.043  1.00 117.55 ? 123 GLY   E CA  1 
ATOM   8452  C  C   . GLY   E  5  124 ? 21.774  -91.237  39.924  1.00 116.06 ? 123 GLY   E C   1 
ATOM   8453  O  O   . GLY   E  5  124 ? 21.198  -90.883  38.874  1.00 122.50 ? 123 GLY   E O   1 
ATOM   8454  N  N   . GLY   E  5  125 ? 21.166  -91.829  40.957  1.00 108.92 ? 124 GLY   E N   1 
ATOM   8455  C  CA  . GLY   E  5  125 ? 19.729  -92.154  40.993  1.00 103.53 ? 124 GLY   E CA  1 
ATOM   8456  C  C   . GLY   E  5  125 ? 18.876  -90.911  41.174  1.00 99.87  ? 124 GLY   E C   1 
ATOM   8457  O  O   . GLY   E  5  125 ? 19.445  -89.817  41.368  1.00 100.33 ? 124 GLY   E O   1 
ATOM   8458  N  N   . ARG   E  5  126 ? 17.553  -91.074  41.102  1.00 91.85  ? 125 ARG   E N   1 
ATOM   8459  C  CA  . ARG   E  5  126 ? 16.560  -90.018  41.424  1.00 90.94  ? 125 ARG   E CA  1 
ATOM   8460  C  C   . ARG   E  5  126 ? 15.412  -90.640  42.210  1.00 89.73  ? 125 ARG   E C   1 
ATOM   8461  O  O   . ARG   E  5  126 ? 15.132  -91.825  42.058  1.00 89.34  ? 125 ARG   E O   1 
ATOM   8462  C  CB  . ARG   E  5  126 ? 16.032  -89.358  40.149  1.00 90.78  ? 125 ARG   E CB  1 
ATOM   8463  C  CG  . ARG   E  5  126 ? 15.178  -90.262  39.271  1.00 90.87  ? 125 ARG   E CG  1 
ATOM   8464  C  CD  . ARG   E  5  126 ? 14.333  -89.458  38.303  1.00 93.29  ? 125 ARG   E CD  1 
ATOM   8465  N  NE  . ARG   E  5  126 ? 13.638  -90.301  37.337  1.00 92.33  ? 125 ARG   E NE  1 
ATOM   8466  C  CZ  . ARG   E  5  126 ? 12.487  -90.931  37.555  1.00 91.55  ? 125 ARG   E CZ  1 
ATOM   8467  N  NH1 . ARG   E  5  126 ? 11.874  -90.835  38.725  1.00 92.11  ? 125 ARG   E NH1 1 
ATOM   8468  N  NH2 . ARG   E  5  126 ? 11.951  -91.661  36.592  1.00 92.16  ? 125 ARG   E NH2 1 
ATOM   8469  N  N   . PRO   E  5  127 ? 14.700  -89.866  43.057  1.00 89.76  ? 126 PRO   E N   1 
ATOM   8470  C  CA  . PRO   E  5  127 ? 13.505  -90.371  43.726  1.00 89.14  ? 126 PRO   E CA  1 
ATOM   8471  C  C   . PRO   E  5  127 ? 12.429  -90.707  42.689  1.00 87.38  ? 126 PRO   E C   1 
ATOM   8472  O  O   . PRO   E  5  127 ? 12.416  -90.090  41.639  1.00 83.79  ? 126 PRO   E O   1 
ATOM   8473  C  CB  . PRO   E  5  127 ? 13.029  -89.215  44.619  1.00 89.93  ? 126 PRO   E CB  1 
ATOM   8474  C  CG  . PRO   E  5  127 ? 14.218  -88.278  44.704  1.00 91.56  ? 126 PRO   E CG  1 
ATOM   8475  C  CD  . PRO   E  5  127 ? 14.987  -88.470  43.413  1.00 91.09  ? 126 PRO   E CD  1 
ATOM   8476  N  N   . TYR   E  5  128 ? 11.567  -91.674  43.006  1.00 89.05  ? 127 TYR   E N   1 
ATOM   8477  C  CA  . TYR   E  5  128 ? 10.340  -91.970  42.226  1.00 91.81  ? 127 TYR   E CA  1 
ATOM   8478  C  C   . TYR   E  5  128 ? 9.446   -90.726  42.296  1.00 92.28  ? 127 TYR   E C   1 
ATOM   8479  O  O   . TYR   E  5  128 ? 9.362   -90.110  43.373  1.00 90.04  ? 127 TYR   E O   1 
ATOM   8480  C  CB  . TYR   E  5  128 ? 9.666   -93.244  42.742  1.00 93.35  ? 127 TYR   E CB  1 
ATOM   8481  C  CG  . TYR   E  5  128 ? 10.461  -94.506  42.512  1.00 94.58  ? 127 TYR   E CG  1 
ATOM   8482  C  CD1 . TYR   E  5  128 ? 10.317  -95.243  41.347  1.00 94.63  ? 127 TYR   E CD1 1 
ATOM   8483  C  CD2 . TYR   E  5  128 ? 11.367  -94.964  43.456  1.00 96.02  ? 127 TYR   E CD2 1 
ATOM   8484  C  CE1 . TYR   E  5  128 ? 11.047  -96.401  41.127  1.00 93.70  ? 127 TYR   E CE1 1 
ATOM   8485  C  CE2 . TYR   E  5  128 ? 12.103  -96.121  43.253  1.00 94.90  ? 127 TYR   E CE2 1 
ATOM   8486  C  CZ  . TYR   E  5  128 ? 11.942  -96.842  42.084  1.00 92.15  ? 127 TYR   E CZ  1 
ATOM   8487  O  OH  . TYR   E  5  128 ? 12.663  -97.982  41.878  1.00 92.98  ? 127 TYR   E OH  1 
ATOM   8488  N  N   . GLY   E  5  129 ? 8.850   -90.332  41.168  1.00 92.36  ? 128 GLY   E N   1 
ATOM   8489  C  CA  . GLY   E  5  129 ? 8.038   -89.106  41.062  1.00 92.56  ? 128 GLY   E CA  1 
ATOM   8490  C  C   . GLY   E  5  129 ? 6.553   -89.410  41.041  1.00 94.22  ? 128 GLY   E C   1 
ATOM   8491  O  O   . GLY   E  5  129 ? 5.844   -88.789  40.228  1.00 95.91  ? 128 GLY   E O   1 
ATOM   8492  N  N   . VAL   E  5  130 ? 6.087   -90.318  41.905  1.00 94.33  ? 129 VAL   E N   1 
ATOM   8493  C  CA  . VAL   E  5  130 ? 4.654   -90.737  41.948  1.00 95.15  ? 129 VAL   E CA  1 
ATOM   8494  C  C   . VAL   E  5  130 ? 4.247   -91.085  43.384  1.00 95.61  ? 129 VAL   E C   1 
ATOM   8495  O  O   . VAL   E  5  130 ? 5.103   -91.566  44.155  1.00 91.47  ? 129 VAL   E O   1 
ATOM   8496  C  CB  . VAL   E  5  130 ? 4.383   -91.907  40.982  1.00 94.56  ? 129 VAL   E CB  1 
ATOM   8497  C  CG1 . VAL   E  5  130 ? 4.962   -93.223  41.479  1.00 92.76  ? 129 VAL   E CG1 1 
ATOM   8498  C  CG2 . VAL   E  5  130 ? 2.899   -92.051  40.688  1.00 97.11  ? 129 VAL   E CG2 1 
ATOM   8499  N  N   . GLY   E  5  131 ? 2.975   -90.830  43.708  1.00 98.50  ? 130 GLY   E N   1 
ATOM   8500  C  CA  . GLY   E  5  131 ? 2.295   -91.270  44.941  1.00 99.19  ? 130 GLY   E CA  1 
ATOM   8501  C  C   . GLY   E  5  131 ? 1.278   -92.352  44.626  1.00 98.54  ? 130 GLY   E C   1 
ATOM   8502  O  O   . GLY   E  5  131 ? 0.612   -92.244  43.576  1.00 96.64  ? 130 GLY   E O   1 
ATOM   8503  N  N   . LEU   E  5  132 ? 1.164   -93.362  45.494  1.00 98.30  ? 131 LEU   E N   1 
ATOM   8504  C  CA  . LEU   E  5  132 ? 0.296   -94.551  45.280  1.00 98.36  ? 131 LEU   E CA  1 
ATOM   8505  C  C   . LEU   E  5  132 ? -0.667  -94.711  46.459  1.00 99.07  ? 131 LEU   E C   1 
ATOM   8506  O  O   . LEU   E  5  132 ? -0.242  -94.471  47.606  1.00 98.24  ? 131 LEU   E O   1 
ATOM   8507  C  CB  . LEU   E  5  132 ? 1.171   -95.799  45.131  1.00 95.92  ? 131 LEU   E CB  1 
ATOM   8508  C  CG  . LEU   E  5  132 ? 2.199   -95.763  44.002  1.00 97.57  ? 131 LEU   E CG  1 
ATOM   8509  C  CD1 . LEU   E  5  132 ? 3.172   -96.925  44.127  1.00 96.86  ? 131 LEU   E CD1 1 
ATOM   8510  C  CD2 . LEU   E  5  132 ? 1.513   -95.785  42.644  1.00 100.21 ? 131 LEU   E CD2 1 
ATOM   8511  N  N   . LEU   E  5  133 ? -1.912  -95.099  46.170  1.00 102.38 ? 132 LEU   E N   1 
ATOM   8512  C  CA  . LEU   E  5  133 ? -2.904  -95.579  47.169  1.00 105.04 ? 132 LEU   E CA  1 
ATOM   8513  C  C   . LEU   E  5  133 ? -3.125  -97.077  46.939  1.00 105.69 ? 132 LEU   E C   1 
ATOM   8514  O  O   . LEU   E  5  133 ? -3.756  -97.418  45.924  1.00 102.31 ? 132 LEU   E O   1 
ATOM   8515  C  CB  . LEU   E  5  133 ? -4.223  -94.814  47.015  1.00 107.62 ? 132 LEU   E CB  1 
ATOM   8516  C  CG  . LEU   E  5  133 ? -4.149  -93.292  47.126  1.00 109.24 ? 132 LEU   E CG  1 
ATOM   8517  C  CD1 . LEU   E  5  133 ? -5.540  -92.686  47.006  1.00 110.38 ? 132 LEU   E CD1 1 
ATOM   8518  C  CD2 . LEU   E  5  133 ? -3.492  -92.863  48.429  1.00 109.89 ? 132 LEU   E CD2 1 
ATOM   8519  N  N   . ILE   E  5  134 ? -2.618  -97.927  47.838  1.00 106.22 ? 133 ILE   E N   1 
ATOM   8520  C  CA  . ILE   E  5  134 ? -2.726  -99.414  47.740  1.00 106.89 ? 133 ILE   E CA  1 
ATOM   8521  C  C   . ILE   E  5  134 ? -3.919  -99.869  48.586  1.00 106.48 ? 133 ILE   E C   1 
ATOM   8522  O  O   . ILE   E  5  134 ? -3.954  -99.536  49.786  1.00 112.32 ? 133 ILE   E O   1 
ATOM   8523  C  CB  . ILE   E  5  134 ? -1.423  -100.116 48.179  1.00 106.38 ? 133 ILE   E CB  1 
ATOM   8524  C  CG1 . ILE   E  5  134 ? -0.203  -99.614  47.401  1.00 108.05 ? 133 ILE   E CG1 1 
ATOM   8525  C  CG2 . ILE   E  5  134 ? -1.567  -101.626 48.070  1.00 107.53 ? 133 ILE   E CG2 1 
ATOM   8526  C  CD1 . ILE   E  5  134 ? 0.563   -98.512  48.091  1.00 111.76 ? 133 ILE   E CD1 1 
ATOM   8527  N  N   . ILE   E  5  135 ? -4.851  -100.605 47.975  1.00 102.17 ? 134 ILE   E N   1 
ATOM   8528  C  CA  . ILE   E  5  135 ? -5.969  -101.299 48.679  1.00 104.33 ? 134 ILE   E CA  1 
ATOM   8529  C  C   . ILE   E  5  135 ? -5.754  -102.809 48.543  1.00 103.75 ? 134 ILE   E C   1 
ATOM   8530  O  O   . ILE   E  5  135 ? -5.113  -103.235 47.562  1.00 105.43 ? 134 ILE   E O   1 
ATOM   8531  C  CB  . ILE   E  5  135 ? -7.344  -100.854 48.139  1.00 103.04 ? 134 ILE   E CB  1 
ATOM   8532  C  CG1 . ILE   E  5  135 ? -7.524  -101.177 46.653  1.00 100.78 ? 134 ILE   E CG1 1 
ATOM   8533  C  CG2 . ILE   E  5  135 ? -7.570  -99.377  48.429  1.00 104.55 ? 134 ILE   E CG2 1 
ATOM   8534  C  CD1 . ILE   E  5  135 ? -8.968  -101.198 46.202  1.00 101.10 ? 134 ILE   E CD1 1 
ATOM   8535  N  N   . GLY   E  5  136 ? -6.259  -103.581 49.506  1.00 105.36 ? 135 GLY   E N   1 
ATOM   8536  C  CA  . GLY   E  5  136 ? -6.163  -105.052 49.500  1.00 107.74 ? 135 GLY   E CA  1 
ATOM   8537  C  C   . GLY   E  5  136 ? -7.020  -105.683 50.580  1.00 110.18 ? 135 GLY   E C   1 
ATOM   8538  O  O   . GLY   E  5  136 ? -7.376  -104.976 51.547  1.00 113.32 ? 135 GLY   E O   1 
ATOM   8539  N  N   . TYR   E  5  137 ? -7.348  -106.967 50.410  1.00 110.67 ? 136 TYR   E N   1 
ATOM   8540  C  CA  . TYR   E  5  137 ? -8.031  -107.816 51.418  1.00 109.21 ? 136 TYR   E CA  1 
ATOM   8541  C  C   . TYR   E  5  137 ? -7.175  -109.061 51.655  1.00 107.54 ? 136 TYR   E C   1 
ATOM   8542  O  O   . TYR   E  5  137 ? -6.960  -109.823 50.697  1.00 106.59 ? 136 TYR   E O   1 
ATOM   8543  C  CB  . TYR   E  5  137 ? -9.448  -108.180 50.967  1.00 110.83 ? 136 TYR   E CB  1 
ATOM   8544  C  CG  . TYR   E  5  137 ? -10.317 -108.716 52.075  1.00 111.95 ? 136 TYR   E CG  1 
ATOM   8545  C  CD1 . TYR   E  5  137 ? -10.309 -110.061 52.405  1.00 110.92 ? 136 TYR   E CD1 1 
ATOM   8546  C  CD2 . TYR   E  5  137 ? -11.133 -107.873 52.813  1.00 115.02 ? 136 TYR   E CD2 1 
ATOM   8547  C  CE1 . TYR   E  5  137 ? -11.096 -110.556 53.433  1.00 112.62 ? 136 TYR   E CE1 1 
ATOM   8548  C  CE2 . TYR   E  5  137 ? -11.928 -108.353 53.842  1.00 113.77 ? 136 TYR   E CE2 1 
ATOM   8549  C  CZ  . TYR   E  5  137 ? -11.911 -109.700 54.152  1.00 112.00 ? 136 TYR   E CZ  1 
ATOM   8550  O  OH  . TYR   E  5  137 ? -12.692 -110.175 55.165  1.00 114.51 ? 136 TYR   E OH  1 
ATOM   8551  N  N   . ASP   E  5  138 ? -6.692  -109.240 52.887  1.00 107.59 ? 137 ASP   E N   1 
ATOM   8552  C  CA  . ASP   E  5  138 ? -5.777  -110.345 53.281  1.00 109.22 ? 137 ASP   E CA  1 
ATOM   8553  C  C   . ASP   E  5  138 ? -6.345  -111.031 54.532  1.00 110.96 ? 137 ASP   E C   1 
ATOM   8554  O  O   . ASP   E  5  138 ? -7.557  -110.877 54.789  1.00 111.42 ? 137 ASP   E O   1 
ATOM   8555  C  CB  . ASP   E  5  138 ? -4.344  -109.823 53.439  1.00 110.98 ? 137 ASP   E CB  1 
ATOM   8556  C  CG  . ASP   E  5  138 ? -4.169  -108.763 54.515  1.00 111.99 ? 137 ASP   E CG  1 
ATOM   8557  O  OD1 . ASP   E  5  138 ? -5.060  -108.646 55.379  1.00 116.81 ? 137 ASP   E OD1 1 
ATOM   8558  O  OD2 . ASP   E  5  138 ? -3.139  -108.061 54.478  1.00 115.32 ? 137 ASP   E OD2 1 
ATOM   8559  N  N   . LYS   E  5  139 ? -5.505  -111.758 55.275  1.00 111.24 ? 138 LYS   E N   1 
ATOM   8560  C  CA  . LYS   E  5  139 ? -5.920  -112.594 56.434  1.00 113.56 ? 138 LYS   E CA  1 
ATOM   8561  C  C   . LYS   E  5  139 ? -6.335  -111.722 57.630  1.00 112.87 ? 138 LYS   E C   1 
ATOM   8562  O  O   . LYS   E  5  139 ? -6.930  -112.286 58.566  1.00 114.50 ? 138 LYS   E O   1 
ATOM   8563  C  CB  . LYS   E  5  139 ? -4.802  -113.568 56.823  1.00 114.77 ? 138 LYS   E CB  1 
ATOM   8564  C  CG  . LYS   E  5  139 ? -4.756  -114.852 56.005  1.00 116.56 ? 138 LYS   E CG  1 
ATOM   8565  C  CD  . LYS   E  5  139 ? -4.249  -116.052 56.779  1.00 117.82 ? 138 LYS   E CD  1 
ATOM   8566  C  CE  . LYS   E  5  139 ? -4.632  -117.368 56.138  1.00 118.52 ? 138 LYS   E CE  1 
ATOM   8567  N  NZ  . LYS   E  5  139 ? -4.356  -118.512 57.038  1.00 120.99 ? 138 LYS   E NZ  1 
ATOM   8568  N  N   . SER   E  5  140 ? -6.042  -110.416 57.618  1.00 113.02 ? 139 SER   E N   1 
ATOM   8569  C  CA  . SER   E  5  140 ? -6.467  -109.461 58.679  1.00 114.36 ? 139 SER   E CA  1 
ATOM   8570  C  C   . SER   E  5  140 ? -7.486  -108.450 58.131  1.00 117.83 ? 139 SER   E C   1 
ATOM   8571  O  O   . SER   E  5  140 ? -7.551  -107.329 58.675  1.00 119.70 ? 139 SER   E O   1 
ATOM   8572  C  CB  . SER   E  5  140 ? -5.273  -108.779 59.302  1.00 113.43 ? 139 SER   E CB  1 
ATOM   8573  O  OG  . SER   E  5  140 ? -4.639  -107.908 58.379  1.00 114.44 ? 139 SER   E OG  1 
ATOM   8574  N  N   . GLY   E  5  141 ? -8.262  -108.835 57.109  1.00 120.76 ? 140 GLY   E N   1 
ATOM   8575  C  CA  . GLY   E  5  141 ? -9.405  -108.057 56.585  1.00 120.98 ? 140 GLY   E CA  1 
ATOM   8576  C  C   . GLY   E  5  141 ? -8.995  -107.054 55.517  1.00 119.90 ? 140 GLY   E C   1 
ATOM   8577  O  O   . GLY   E  5  141 ? -7.991  -107.305 54.821  1.00 118.62 ? 140 GLY   E O   1 
ATOM   8578  N  N   . ALA   E  5  142 ? -9.754  -105.958 55.390  1.00 118.48 ? 141 ALA   E N   1 
ATOM   8579  C  CA  . ALA   E  5  142 ? -9.573  -104.897 54.369  1.00 116.22 ? 141 ALA   E CA  1 
ATOM   8580  C  C   . ALA   E  5  142 ? -8.512  -103.895 54.841  1.00 112.06 ? 141 ALA   E C   1 
ATOM   8581  O  O   . ALA   E  5  142 ? -8.411  -103.669 56.064  1.00 104.30 ? 141 ALA   E O   1 
ATOM   8582  C  CB  . ALA   E  5  142 ? -10.893 -104.217 54.093  1.00 118.88 ? 141 ALA   E CB  1 
ATOM   8583  N  N   . HIS   E  5  143 ? -7.755  -103.320 53.899  1.00 111.51 ? 142 HIS   E N   1 
ATOM   8584  C  CA  . HIS   E  5  143 ? -6.650  -102.357 54.161  1.00 114.02 ? 142 HIS   E CA  1 
ATOM   8585  C  C   . HIS   E  5  143 ? -6.607  -101.258 53.096  1.00 113.90 ? 142 HIS   E C   1 
ATOM   8586  O  O   . HIS   E  5  143 ? -6.970  -101.532 51.935  1.00 119.47 ? 142 HIS   E O   1 
ATOM   8587  C  CB  . HIS   E  5  143 ? -5.296  -103.072 54.196  1.00 112.40 ? 142 HIS   E CB  1 
ATOM   8588  C  CG  . HIS   E  5  143 ? -5.201  -104.126 55.242  1.00 115.72 ? 142 HIS   E CG  1 
ATOM   8589  N  ND1 . HIS   E  5  143 ? -4.817  -103.847 56.537  1.00 117.93 ? 142 HIS   E ND1 1 
ATOM   8590  C  CD2 . HIS   E  5  143 ? -5.442  -105.452 55.192  1.00 117.87 ? 142 HIS   E CD2 1 
ATOM   8591  C  CE1 . HIS   E  5  143 ? -4.822  -104.958 57.242  1.00 118.23 ? 142 HIS   E CE1 1 
ATOM   8592  N  NE2 . HIS   E  5  143 ? -5.203  -105.957 56.440  1.00 118.20 ? 142 HIS   E NE2 1 
ATOM   8593  N  N   . LEU   E  5  144 ? -6.152  -100.069 53.495  1.00 110.04 ? 143 LEU   E N   1 
ATOM   8594  C  CA  . LEU   E  5  144 ? -5.757  -98.964  52.586  1.00 107.58 ? 143 LEU   E CA  1 
ATOM   8595  C  C   . LEU   E  5  144 ? -4.409  -98.415  53.061  1.00 102.70 ? 143 LEU   E C   1 
ATOM   8596  O  O   . LEU   E  5  144 ? -4.276  -98.145  54.269  1.00 98.13  ? 143 LEU   E O   1 
ATOM   8597  C  CB  . LEU   E  5  144 ? -6.843  -97.883  52.591  1.00 109.16 ? 143 LEU   E CB  1 
ATOM   8598  C  CG  . LEU   E  5  144 ? -6.432  -96.518  52.037  1.00 110.17 ? 143 LEU   E CG  1 
ATOM   8599  C  CD1 . LEU   E  5  144 ? -6.195  -96.579  50.535  1.00 107.76 ? 143 LEU   E CD1 1 
ATOM   8600  C  CD2 . LEU   E  5  144 ? -7.484  -95.473  52.371  1.00 110.98 ? 143 LEU   E CD2 1 
ATOM   8601  N  N   . LEU   E  5  145 ? -3.458  -98.278  52.134  1.00 104.07 ? 144 LEU   E N   1 
ATOM   8602  C  CA  . LEU   E  5  145 ? -2.114  -97.685  52.360  1.00 104.15 ? 144 LEU   E CA  1 
ATOM   8603  C  C   . LEU   E  5  145 ? -1.981  -96.423  51.502  1.00 104.28 ? 144 LEU   E C   1 
ATOM   8604  O  O   . LEU   E  5  145 ? -2.627  -96.366  50.437  1.00 101.76 ? 144 LEU   E O   1 
ATOM   8605  C  CB  . LEU   E  5  145 ? -1.043  -98.715  51.981  1.00 104.96 ? 144 LEU   E CB  1 
ATOM   8606  C  CG  . LEU   E  5  145 ? -0.458  -99.545  53.124  1.00 104.77 ? 144 LEU   E CG  1 
ATOM   8607  C  CD1 . LEU   E  5  145 ? -1.547  -100.126 54.016  1.00 109.15 ? 144 LEU   E CD1 1 
ATOM   8608  C  CD2 . LEU   E  5  145 ? 0.424   -100.654 52.571  1.00 103.71 ? 144 LEU   E CD2 1 
ATOM   8609  N  N   . GLU   E  5  146 ? -1.186  -95.453  51.962  1.00 104.94 ? 145 GLU   E N   1 
ATOM   8610  C  CA  . GLU   E  5  146 ? -0.726  -94.290  51.158  1.00 106.39 ? 145 GLU   E CA  1 
ATOM   8611  C  C   . GLU   E  5  146 ? 0.799   -94.358  51.039  1.00 103.09 ? 145 GLU   E C   1 
ATOM   8612  O  O   . GLU   E  5  146 ? 1.471   -94.303  52.084  1.00 102.38 ? 145 GLU   E O   1 
ATOM   8613  C  CB  . GLU   E  5  146 ? -1.146  -92.961  51.788  1.00 111.52 ? 145 GLU   E CB  1 
ATOM   8614  C  CG  . GLU   E  5  146 ? -0.788  -91.762  50.923  1.00 115.48 ? 145 GLU   E CG  1 
ATOM   8615  C  CD  . GLU   E  5  146 ? -1.034  -90.400  51.547  1.00 121.00 ? 145 GLU   E CD  1 
ATOM   8616  O  OE1 . GLU   E  5  146 ? -2.019  -90.262  52.300  1.00 123.02 ? 145 GLU   E OE1 1 
ATOM   8617  O  OE2 . GLU   E  5  146 ? -0.237  -89.479  51.272  1.00 125.96 ? 145 GLU   E OE2 1 
ATOM   8618  N  N   . PHE   E  5  147 ? 1.311   -94.473  49.811  1.00 101.24 ? 146 PHE   E N   1 
ATOM   8619  C  CA  . PHE   E  5  147 ? 2.762   -94.479  49.490  1.00 103.67 ? 146 PHE   E CA  1 
ATOM   8620  C  C   . PHE   E  5  147 ? 3.181   -93.084  49.016  1.00 103.40 ? 146 PHE   E C   1 
ATOM   8621  O  O   . PHE   E  5  147 ? 2.550   -92.555  48.081  1.00 104.79 ? 146 PHE   E O   1 
ATOM   8622  C  CB  . PHE   E  5  147 ? 3.082   -95.521  48.416  1.00 100.24 ? 146 PHE   E CB  1 
ATOM   8623  C  CG  . PHE   E  5  147 ? 4.451   -95.382  47.797  1.00 97.76  ? 146 PHE   E CG  1 
ATOM   8624  C  CD1 . PHE   E  5  147 ? 5.563   -95.941  48.403  1.00 95.95  ? 146 PHE   E CD1 1 
ATOM   8625  C  CD2 . PHE   E  5  147 ? 4.628   -94.681  46.613  1.00 99.72  ? 146 PHE   E CD2 1 
ATOM   8626  C  CE1 . PHE   E  5  147 ? 6.822   -95.809  47.837  1.00 95.09  ? 146 PHE   E CE1 1 
ATOM   8627  C  CE2 . PHE   E  5  147 ? 5.888   -94.546  46.049  1.00 97.84  ? 146 PHE   E CE2 1 
ATOM   8628  C  CZ  . PHE   E  5  147 ? 6.983   -95.111  46.662  1.00 95.43  ? 146 PHE   E CZ  1 
ATOM   8629  N  N   . GLN   E  5  148 ? 4.217   -92.519  49.644  1.00 106.93 ? 147 GLN   E N   1 
ATOM   8630  C  CA  . GLN   E  5  148 ? 4.918   -91.293  49.181  1.00 107.76 ? 147 GLN   E CA  1 
ATOM   8631  C  C   . GLN   E  5  148 ? 6.347   -91.662  48.795  1.00 105.19 ? 147 GLN   E C   1 
ATOM   8632  O  O   . GLN   E  5  148 ? 6.997   -92.440  49.488  1.00 110.15 ? 147 GLN   E O   1 
ATOM   8633  C  CB  . GLN   E  5  148 ? 4.904   -90.214  50.261  1.00 109.62 ? 147 GLN   E CB  1 
ATOM   8634  C  CG  . GLN   E  5  148 ? 3.661   -89.337  50.214  1.00 116.81 ? 147 GLN   E CG  1 
ATOM   8635  C  CD  . GLN   E  5  148 ? 3.600   -88.317  51.325  1.00 126.87 ? 147 GLN   E CD  1 
ATOM   8636  O  OE1 . GLN   E  5  148 ? 2.518   -87.918  51.751  1.00 137.90 ? 147 GLN   E OE1 1 
ATOM   8637  N  NE2 . GLN   E  5  148 ? 4.754   -87.872  51.803  1.00 130.37 ? 147 GLN   E NE2 1 
ATOM   8638  N  N   . PRO   E  5  149 ? 6.879   -91.095  47.690  1.00 103.26 ? 148 PRO   E N   1 
ATOM   8639  C  CA  . PRO   E  5  149 ? 8.192   -91.476  47.164  1.00 101.83 ? 148 PRO   E CA  1 
ATOM   8640  C  C   . PRO   E  5  149 ? 9.388   -91.019  48.013  1.00 99.55  ? 148 PRO   E C   1 
ATOM   8641  O  O   . PRO   E  5  149 ? 10.515  -91.301  47.636  1.00 98.82  ? 148 PRO   E O   1 
ATOM   8642  C  CB  . PRO   E  5  149 ? 8.238   -90.773  45.803  1.00 101.85 ? 148 PRO   E CB  1 
ATOM   8643  C  CG  . PRO   E  5  149 ? 7.357   -89.562  45.989  1.00 104.44 ? 148 PRO   E CG  1 
ATOM   8644  C  CD  . PRO   E  5  149 ? 6.239   -90.045  46.888  1.00 105.02 ? 148 PRO   E CD  1 
ATOM   8645  N  N   . SER   E  5  150 ? 9.119   -90.318  49.117  1.00 96.88  ? 149 SER   E N   1 
ATOM   8646  C  CA  . SER   E  5  150 ? 10.084  -90.076  50.218  1.00 100.63 ? 149 SER   E CA  1 
ATOM   8647  C  C   . SER   E  5  150 ? 10.455  -91.410  50.876  1.00 101.09 ? 149 SER   E C   1 
ATOM   8648  O  O   . SER   E  5  150 ? 11.539  -91.483  51.487  1.00 110.72 ? 149 SER   E O   1 
ATOM   8649  C  CB  . SER   E  5  150 ? 9.511   -89.116  51.222  1.00 100.42 ? 149 SER   E CB  1 
ATOM   8650  O  OG  . SER   E  5  150 ? 8.374   -89.679  51.860  1.00 98.89  ? 149 SER   E OG  1 
ATOM   8651  N  N   . GLY   E  5  151 ? 9.583   -92.418  50.743  1.00 101.09 ? 150 GLY   E N   1 
ATOM   8652  C  CA  . GLY   E  5  151 ? 9.708   -93.748  51.372  1.00 101.02 ? 150 GLY   E CA  1 
ATOM   8653  C  C   . GLY   E  5  151 ? 8.616   -93.986  52.403  1.00 103.08 ? 150 GLY   E C   1 
ATOM   8654  O  O   . GLY   E  5  151 ? 8.414   -95.154  52.791  1.00 103.53 ? 150 GLY   E O   1 
ATOM   8655  N  N   . ASN   E  5  152 ? 7.923   -92.923  52.825  1.00 100.19 ? 151 ASN   E N   1 
ATOM   8656  C  CA  . ASN   E  5  152 ? 6.906   -92.957  53.909  1.00 98.25  ? 151 ASN   E CA  1 
ATOM   8657  C  C   . ASN   E  5  152 ? 5.630   -93.634  53.402  1.00 97.91  ? 151 ASN   E C   1 
ATOM   8658  O  O   . ASN   E  5  152 ? 4.998   -93.087  52.481  1.00 96.64  ? 151 ASN   E O   1 
ATOM   8659  C  CB  . ASN   E  5  152 ? 6.611   -91.557  54.446  1.00 101.04 ? 151 ASN   E CB  1 
ATOM   8660  C  CG  . ASN   E  5  152 ? 7.771   -90.990  55.237  1.00 101.32 ? 151 ASN   E CG  1 
ATOM   8661  O  OD1 . ASN   E  5  152 ? 8.124   -91.521  56.288  1.00 101.58 ? 151 ASN   E OD1 1 
ATOM   8662  N  ND2 . ASN   E  5  152 ? 8.373   -89.920  54.742  1.00 105.80 ? 151 ASN   E ND2 1 
ATOM   8663  N  N   . VAL   E  5  153 ? 5.285   -94.783  53.991  1.00 98.82  ? 152 VAL   E N   1 
ATOM   8664  C  CA  . VAL   E  5  153 ? 4.023   -95.538  53.736  1.00 101.54 ? 152 VAL   E CA  1 
ATOM   8665  C  C   . VAL   E  5  153 ? 3.173   -95.484  55.008  1.00 98.71  ? 152 VAL   E C   1 
ATOM   8666  O  O   . VAL   E  5  153 ? 3.738   -95.689  56.098  1.00 99.64  ? 152 VAL   E O   1 
ATOM   8667  C  CB  . VAL   E  5  153 ? 4.307   -96.990  53.312  1.00 103.16 ? 152 VAL   E CB  1 
ATOM   8668  C  CG1 . VAL   E  5  153 ? 3.022   -97.780  53.105  1.00 106.02 ? 152 VAL   E CG1 1 
ATOM   8669  C  CG2 . VAL   E  5  153 ? 5.174   -97.043  52.063  1.00 105.20 ? 152 VAL   E CG2 1 
ATOM   8670  N  N   . THR   E  5  154 ? 1.870   -95.230  54.865  1.00 99.91  ? 153 THR   E N   1 
ATOM   8671  C  CA  . THR   E  5  154 ? 0.930   -94.969  55.987  1.00 100.98 ? 153 THR   E CA  1 
ATOM   8672  C  C   . THR   E  5  154 ? -0.375  -95.743  55.772  1.00 103.17 ? 153 THR   E C   1 
ATOM   8673  O  O   . THR   E  5  154 ? -0.953  -95.619  54.675  1.00 109.16 ? 153 THR   E O   1 
ATOM   8674  C  CB  . THR   E  5  154 ? 0.655   -93.467  56.120  1.00 101.23 ? 153 THR   E CB  1 
ATOM   8675  O  OG1 . THR   E  5  154 ? 1.901   -92.807  56.346  1.00 103.14 ? 153 THR   E OG1 1 
ATOM   8676  C  CG2 . THR   E  5  154 ? -0.304  -93.141  57.242  1.00 102.86 ? 153 THR   E CG2 1 
ATOM   8677  N  N   . GLU   E  5  155 ? -0.825  -96.484  56.792  1.00 103.89 ? 154 GLU   E N   1 
ATOM   8678  C  CA  . GLU   E  5  155 ? -2.116  -97.228  56.788  1.00 108.35 ? 154 GLU   E CA  1 
ATOM   8679  C  C   . GLU   E  5  155 ? -3.222  -96.313  57.324  1.00 105.10 ? 154 GLU   E C   1 
ATOM   8680  O  O   . GLU   E  5  155 ? -3.050  -95.765  58.427  1.00 103.48 ? 154 GLU   E O   1 
ATOM   8681  C  CB  . GLU   E  5  155 ? -2.028  -98.507  57.623  1.00 115.27 ? 154 GLU   E CB  1 
ATOM   8682  C  CG  . GLU   E  5  155 ? -3.272  -99.378  57.515  1.00 121.67 ? 154 GLU   E CG  1 
ATOM   8683  C  CD  . GLU   E  5  155 ? -3.129  -100.821 57.976  1.00 123.38 ? 154 GLU   E CD  1 
ATOM   8684  O  OE1 . GLU   E  5  155 ? -4.039  -101.621 57.681  1.00 121.34 ? 154 GLU   E OE1 1 
ATOM   8685  O  OE2 . GLU   E  5  155 ? -2.116  -101.146 58.630  1.00 132.46 ? 154 GLU   E OE2 1 
ATOM   8686  N  N   . LEU   E  5  156 ? -4.319  -96.186  56.572  1.00 106.56 ? 155 LEU   E N   1 
ATOM   8687  C  CA  . LEU   E  5  156 ? -5.417  -95.216  56.825  1.00 111.62 ? 155 LEU   E CA  1 
ATOM   8688  C  C   . LEU   E  5  156 ? -6.768  -95.906  56.613  1.00 112.19 ? 155 LEU   E C   1 
ATOM   8689  O  O   . LEU   E  5  156 ? -6.802  -96.932  55.909  1.00 112.09 ? 155 LEU   E O   1 
ATOM   8690  C  CB  . LEU   E  5  156 ? -5.250  -94.033  55.864  1.00 117.57 ? 155 LEU   E CB  1 
ATOM   8691  C  CG  . LEU   E  5  156 ? -3.982  -93.198  56.052  1.00 119.31 ? 155 LEU   E CG  1 
ATOM   8692  C  CD1 . LEU   E  5  156 ? -3.374  -92.805  54.712  1.00 120.78 ? 155 LEU   E CD1 1 
ATOM   8693  C  CD2 . LEU   E  5  156 ? -4.257  -91.965  56.900  1.00 120.06 ? 155 LEU   E CD2 1 
ATOM   8694  N  N   . TYR   E  5  157 ? -7.833  -95.360  57.207  1.00 115.99 ? 156 TYR   E N   1 
ATOM   8695  C  CA  . TYR   E  5  157 ? -9.246  -95.725  56.920  1.00 117.58 ? 156 TYR   E CA  1 
ATOM   8696  C  C   . TYR   E  5  157 ? -9.622  -95.176  55.541  1.00 118.47 ? 156 TYR   E C   1 
ATOM   8697  O  O   . TYR   E  5  157 ? -10.264 -95.901  54.753  1.00 119.55 ? 156 TYR   E O   1 
ATOM   8698  C  CB  . TYR   E  5  157 ? -10.191 -95.168  57.988  1.00 118.13 ? 156 TYR   E CB  1 
ATOM   8699  C  CG  . TYR   E  5  157 ? -10.028 -95.782  59.354  1.00 117.32 ? 156 TYR   E CG  1 
ATOM   8700  C  CD1 . TYR   E  5  157 ? -10.338 -97.113  59.580  1.00 113.65 ? 156 TYR   E CD1 1 
ATOM   8701  C  CD2 . TYR   E  5  157 ? -9.573  -95.030  60.426  1.00 117.49 ? 156 TYR   E CD2 1 
ATOM   8702  C  CE1 . TYR   E  5  157 ? -10.194 -97.684  60.833  1.00 112.64 ? 156 TYR   E CE1 1 
ATOM   8703  C  CE2 . TYR   E  5  157 ? -9.423  -95.586  61.686  1.00 115.32 ? 156 TYR   E CE2 1 
ATOM   8704  C  CZ  . TYR   E  5  157 ? -9.735  -96.917  61.890  1.00 113.42 ? 156 TYR   E CZ  1 
ATOM   8705  O  OH  . TYR   E  5  157 ? -9.588  -97.463  63.130  1.00 118.15 ? 156 TYR   E OH  1 
ATOM   8706  N  N   . GLY   E  5  158 ? -9.232  -93.924  55.279  1.00 119.54 ? 157 GLY   E N   1 
ATOM   8707  C  CA  . GLY   E  5  158 ? -9.447  -93.220  54.001  1.00 119.28 ? 157 GLY   E CA  1 
ATOM   8708  C  C   . GLY   E  5  158 ? -8.379  -92.167  53.763  1.00 116.32 ? 157 GLY   E C   1 
ATOM   8709  O  O   . GLY   E  5  158 ? -7.723  -91.765  54.746  1.00 116.23 ? 157 GLY   E O   1 
ATOM   8710  N  N   . THR   E  5  159 ? -8.199  -91.742  52.507  1.00 112.53 ? 158 THR   E N   1 
ATOM   8711  C  CA  . THR   E  5  159 ? -7.268  -90.648  52.115  1.00 110.71 ? 158 THR   E CA  1 
ATOM   8712  C  C   . THR   E  5  159 ? -7.474  -90.256  50.648  1.00 108.06 ? 158 THR   E C   1 
ATOM   8713  O  O   . THR   E  5  159 ? -8.316  -90.876  49.971  1.00 109.96 ? 158 THR   E O   1 
ATOM   8714  C  CB  . THR   E  5  159 ? -5.804  -91.045  52.347  1.00 108.21 ? 158 THR   E CB  1 
ATOM   8715  O  OG1 . THR   E  5  159 ? -4.989  -89.895  52.124  1.00 107.21 ? 158 THR   E OG1 1 
ATOM   8716  C  CG2 . THR   E  5  159 ? -5.344  -92.173  51.449  1.00 108.53 ? 158 THR   E CG2 1 
ATOM   8717  N  N   . ALA   E  5  160 ? -6.710  -89.262  50.191  1.00 105.10 ? 159 ALA   E N   1 
ATOM   8718  C  CA  . ALA   E  5  160 ? -6.674  -88.780  48.793  1.00 106.99 ? 159 ALA   E CA  1 
ATOM   8719  C  C   . ALA   E  5  160 ? -5.324  -88.107  48.518  1.00 104.97 ? 159 ALA   E C   1 
ATOM   8720  O  O   . ALA   E  5  160 ? -4.789  -87.457  49.436  1.00 104.56 ? 159 ALA   E O   1 
ATOM   8721  C  CB  . ALA   E  5  160 ? -7.824  -87.835  48.551  1.00 109.79 ? 159 ALA   E CB  1 
ATOM   8722  N  N   . ILE   E  5  161 ? -4.799  -88.273  47.302  1.00 105.71 ? 160 ILE   E N   1 
ATOM   8723  C  CA  . ILE   E  5  161 ? -3.550  -87.614  46.814  1.00 107.61 ? 160 ILE   E CA  1 
ATOM   8724  C  C   . ILE   E  5  161 ? -3.822  -87.005  45.435  1.00 111.87 ? 160 ILE   E C   1 
ATOM   8725  O  O   . ILE   E  5  161 ? -4.723  -87.508  44.731  1.00 110.63 ? 160 ILE   E O   1 
ATOM   8726  C  CB  . ILE   E  5  161 ? -2.368  -88.603  46.771  1.00 107.11 ? 160 ILE   E CB  1 
ATOM   8727  C  CG1 . ILE   E  5  161 ? -2.734  -89.895  46.034  1.00 107.93 ? 160 ILE   E CG1 1 
ATOM   8728  C  CG2 . ILE   E  5  161 ? -1.848  -88.876  48.174  1.00 106.53 ? 160 ILE   E CG2 1 
ATOM   8729  C  CD1 . ILE   E  5  161 ? -1.545  -90.728  45.613  1.00 107.84 ? 160 ILE   E CD1 1 
ATOM   8730  N  N   . GLY   E  5  162 ? -3.061  -85.966  45.077  1.00 114.80 ? 161 GLY   E N   1 
ATOM   8731  C  CA  . GLY   E  5  162 ? -3.179  -85.238  43.799  1.00 118.07 ? 161 GLY   E CA  1 
ATOM   8732  C  C   . GLY   E  5  162 ? -3.613  -83.800  44.014  1.00 120.28 ? 161 GLY   E C   1 
ATOM   8733  O  O   . GLY   E  5  162 ? -3.654  -83.363  45.181  1.00 121.43 ? 161 GLY   E O   1 
ATOM   8734  N  N   . ALA   E  5  163 ? -3.930  -83.093  42.924  1.00 124.67 ? 162 ALA   E N   1 
ATOM   8735  C  CA  . ALA   E  5  163 ? -4.383  -81.681  42.921  1.00 126.04 ? 162 ALA   E CA  1 
ATOM   8736  C  C   . ALA   E  5  163 ? -5.760  -81.583  43.588  1.00 126.73 ? 162 ALA   E C   1 
ATOM   8737  O  O   . ALA   E  5  163 ? -6.670  -82.326  43.169  1.00 126.56 ? 162 ALA   E O   1 
ATOM   8738  C  CB  . ALA   E  5  163 ? -4.417  -81.153  41.507  1.00 127.30 ? 162 ALA   E CB  1 
ATOM   8739  N  N   . ARG   E  5  164 ? -5.892  -80.704  44.588  1.00 128.83 ? 163 ARG   E N   1 
ATOM   8740  C  CA  . ARG   E  5  164 ? -7.149  -80.425  45.340  1.00 135.07 ? 163 ARG   E CA  1 
ATOM   8741  C  C   . ARG   E  5  164 ? -7.604  -81.678  46.102  1.00 132.06 ? 163 ARG   E C   1 
ATOM   8742  O  O   . ARG   E  5  164 ? -8.823  -81.819  46.327  1.00 136.79 ? 163 ARG   E O   1 
ATOM   8743  C  CB  . ARG   E  5  164 ? -8.247  -79.928  44.393  1.00 141.33 ? 163 ARG   E CB  1 
ATOM   8744  C  CG  . ARG   E  5  164 ? -8.121  -78.460  44.012  1.00 147.15 ? 163 ARG   E CG  1 
ATOM   8745  C  CD  . ARG   E  5  164 ? -8.935  -78.138  42.775  1.00 155.25 ? 163 ARG   E CD  1 
ATOM   8746  N  NE  . ARG   E  5  164 ? -8.167  -78.324  41.549  1.00 159.67 ? 163 ARG   E NE  1 
ATOM   8747  C  CZ  . ARG   E  5  164 ? -8.644  -78.787  40.392  1.00 161.21 ? 163 ARG   E CZ  1 
ATOM   8748  N  NH1 . ARG   E  5  164 ? -9.911  -79.152  40.272  1.00 163.30 ? 163 ARG   E NH1 1 
ATOM   8749  N  NH2 . ARG   E  5  164 ? -7.836  -78.899  39.353  1.00 160.55 ? 163 ARG   E NH2 1 
ATOM   8750  N  N   . SER   E  5  165 ? -6.664  -82.533  46.516  1.00 130.07 ? 164 SER   E N   1 
ATOM   8751  C  CA  . SER   E  5  165 ? -6.932  -83.757  47.318  1.00 122.34 ? 164 SER   E CA  1 
ATOM   8752  C  C   . SER   E  5  165 ? -7.441  -83.368  48.713  1.00 125.56 ? 164 SER   E C   1 
ATOM   8753  O  O   . SER   E  5  165 ? -8.111  -84.210  49.348  1.00 124.67 ? 164 SER   E O   1 
ATOM   8754  C  CB  . SER   E  5  165 ? -5.708  -84.632  47.409  1.00 119.88 ? 164 SER   E CB  1 
ATOM   8755  O  OG  . SER   E  5  165 ? -4.651  -83.963  48.080  1.00 111.24 ? 164 SER   E OG  1 
ATOM   8756  N  N   . GLN   E  5  166 ? -7.132  -82.143  49.161  1.00 121.82 ? 165 GLN   E N   1 
ATOM   8757  C  CA  . GLN   E  5  166 ? -7.471  -81.617  50.512  1.00 121.43 ? 165 GLN   E CA  1 
ATOM   8758  C  C   . GLN   E  5  166 ? -8.994  -81.597  50.705  1.00 118.31 ? 165 GLN   E C   1 
ATOM   8759  O  O   . GLN   E  5  166 ? -9.438  -81.798  51.853  1.00 120.06 ? 165 GLN   E O   1 
ATOM   8760  C  CB  . GLN   E  5  166 ? -6.864  -80.225  50.703  1.00 124.04 ? 165 GLN   E CB  1 
ATOM   8761  C  CG  . GLN   E  5  166 ? -6.994  -79.680  52.120  1.00 130.58 ? 165 GLN   E CG  1 
ATOM   8762  C  CD  . GLN   E  5  166 ? -6.399  -80.603  53.158  1.00 131.01 ? 165 GLN   E CD  1 
ATOM   8763  O  OE1 . GLN   E  5  166 ? -7.064  -81.496  53.678  1.00 130.26 ? 165 GLN   E OE1 1 
ATOM   8764  N  NE2 . GLN   E  5  166 ? -5.132  -80.390  53.474  1.00 131.80 ? 165 GLN   E NE2 1 
ATOM   8765  N  N   . GLY   E  5  167 ? -9.760  -81.363  49.634  1.00 115.92 ? 166 GLY   E N   1 
ATOM   8766  C  CA  . GLY   E  5  167 ? -11.236 -81.335  49.660  1.00 121.00 ? 166 GLY   E CA  1 
ATOM   8767  C  C   . GLY   E  5  167 ? -11.815 -82.682  50.056  1.00 120.89 ? 166 GLY   E C   1 
ATOM   8768  O  O   . GLY   E  5  167 ? -12.614 -82.724  51.014  1.00 128.94 ? 166 GLY   E O   1 
ATOM   8769  N  N   . ALA   E  5  168 ? -11.423 -83.743  49.345  1.00 118.49 ? 167 ALA   E N   1 
ATOM   8770  C  CA  . ALA   E  5  168 ? -11.836 -85.142  49.602  1.00 116.64 ? 167 ALA   E CA  1 
ATOM   8771  C  C   . ALA   E  5  168 ? -11.331 -85.581  50.980  1.00 115.40 ? 167 ALA   E C   1 
ATOM   8772  O  O   . ALA   E  5  168 ? -12.101 -86.234  51.708  1.00 116.60 ? 167 ALA   E O   1 
ATOM   8773  C  CB  . ALA   E  5  168 ? -11.317 -86.044  48.508  1.00 113.68 ? 167 ALA   E CB  1 
ATOM   8774  N  N   . LYS   E  5  169 ? -10.090 -85.219  51.323  1.00 118.33 ? 168 LYS   E N   1 
ATOM   8775  C  CA  . LYS   E  5  169 ? -9.403  -85.649  52.572  1.00 124.21 ? 168 LYS   E CA  1 
ATOM   8776  C  C   . LYS   E  5  169 ? -10.135 -85.069  53.789  1.00 127.05 ? 168 LYS   E C   1 
ATOM   8777  O  O   . LYS   E  5  169 ? -10.221 -85.779  54.810  1.00 128.25 ? 168 LYS   E O   1 
ATOM   8778  C  CB  . LYS   E  5  169 ? -7.927  -85.236  52.559  1.00 127.45 ? 168 LYS   E CB  1 
ATOM   8779  C  CG  . LYS   E  5  169 ? -7.055  -85.951  53.583  1.00 129.34 ? 168 LYS   E CG  1 
ATOM   8780  C  CD  . LYS   E  5  169 ? -5.571  -85.787  53.344  1.00 131.26 ? 168 LYS   E CD  1 
ATOM   8781  C  CE  . LYS   E  5  169 ? -4.730  -86.552  54.343  1.00 131.44 ? 168 LYS   E CE  1 
ATOM   8782  N  NZ  . LYS   E  5  169 ? -3.285  -86.455  54.031  1.00 132.36 ? 168 LYS   E NZ  1 
ATOM   8783  N  N   . THR   E  5  170 ? -10.639 -83.835  53.684  1.00 129.65 ? 169 THR   E N   1 
ATOM   8784  C  CA  . THR   E  5  170 ? -11.469 -83.176  54.729  1.00 133.05 ? 169 THR   E CA  1 
ATOM   8785  C  C   . THR   E  5  170 ? -12.815 -83.902  54.835  1.00 137.77 ? 169 THR   E C   1 
ATOM   8786  O  O   . THR   E  5  170 ? -13.237 -84.190  55.974  1.00 139.82 ? 169 THR   E O   1 
ATOM   8787  C  CB  . THR   E  5  170 ? -11.680 -81.684  54.444  1.00 133.16 ? 169 THR   E CB  1 
ATOM   8788  O  OG1 . THR   E  5  170 ? -10.398 -81.062  54.371  1.00 133.90 ? 169 THR   E OG1 1 
ATOM   8789  C  CG2 . THR   E  5  170 ? -12.520 -80.998  55.500  1.00 133.04 ? 169 THR   E CG2 1 
ATOM   8790  N  N   . TYR   E  5  171 ? -13.460 -84.169  53.693  1.00 139.90 ? 170 TYR   E N   1 
ATOM   8791  C  CA  . TYR   E  5  171 ? -14.786 -84.837  53.599  1.00 137.02 ? 170 TYR   E CA  1 
ATOM   8792  C  C   . TYR   E  5  171 ? -14.729 -86.195  54.307  1.00 138.19 ? 170 TYR   E C   1 
ATOM   8793  O  O   . TYR   E  5  171 ? -15.582 -86.451  55.179  1.00 138.03 ? 170 TYR   E O   1 
ATOM   8794  C  CB  . TYR   E  5  171 ? -15.227 -85.005  52.142  1.00 136.26 ? 170 TYR   E CB  1 
ATOM   8795  C  CG  . TYR   E  5  171 ? -16.380 -85.959  51.951  1.00 135.30 ? 170 TYR   E CG  1 
ATOM   8796  C  CD1 . TYR   E  5  171 ? -16.164 -87.318  51.779  1.00 135.28 ? 170 TYR   E CD1 1 
ATOM   8797  C  CD2 . TYR   E  5  171 ? -17.691 -85.512  51.964  1.00 137.08 ? 170 TYR   E CD2 1 
ATOM   8798  C  CE1 . TYR   E  5  171 ? -17.216 -88.204  51.614  1.00 135.08 ? 170 TYR   E CE1 1 
ATOM   8799  C  CE2 . TYR   E  5  171 ? -18.755 -86.384  51.800  1.00 134.18 ? 170 TYR   E CE2 1 
ATOM   8800  C  CZ  . TYR   E  5  171 ? -18.518 -87.736  51.625  1.00 134.06 ? 170 TYR   E CZ  1 
ATOM   8801  O  OH  . TYR   E  5  171 ? -19.564 -88.597  51.462  1.00 132.50 ? 170 TYR   E OH  1 
ATOM   8802  N  N   . LEU   E  5  172 ? -13.759 -87.036  53.932  1.00 137.19 ? 171 LEU   E N   1 
ATOM   8803  C  CA  . LEU   E  5  172 ? -13.566 -88.398  54.502  1.00 136.06 ? 171 LEU   E CA  1 
ATOM   8804  C  C   . LEU   E  5  172 ? -13.326 -88.290  56.013  1.00 133.93 ? 171 LEU   E C   1 
ATOM   8805  O  O   . LEU   E  5  172 ? -13.803 -89.175  56.745  1.00 136.05 ? 171 LEU   E O   1 
ATOM   8806  C  CB  . LEU   E  5  172 ? -12.391 -89.094  53.806  1.00 131.43 ? 171 LEU   E CB  1 
ATOM   8807  C  CG  . LEU   E  5  172 ? -12.649 -89.562  52.375  1.00 133.15 ? 171 LEU   E CG  1 
ATOM   8808  C  CD1 . LEU   E  5  172 ? -11.355 -90.005  51.714  1.00 128.83 ? 171 LEU   E CD1 1 
ATOM   8809  C  CD2 . LEU   E  5  172 ? -13.675 -90.688  52.339  1.00 136.31 ? 171 LEU   E CD2 1 
ATOM   8810  N  N   . GLU   E  5  173 ? -12.626 -87.242  56.457  1.00 132.66 ? 172 GLU   E N   1 
ATOM   8811  C  CA  . GLU   E  5  173 ? -12.334 -86.989  57.893  1.00 134.02 ? 172 GLU   E CA  1 
ATOM   8812  C  C   . GLU   E  5  173 ? -13.655 -86.744  58.636  1.00 137.69 ? 172 GLU   E C   1 
ATOM   8813  O  O   . GLU   E  5  173 ? -13.777 -87.220  59.782  1.00 137.69 ? 172 GLU   E O   1 
ATOM   8814  C  CB  . GLU   E  5  173 ? -11.365 -85.815  58.046  1.00 136.99 ? 172 GLU   E CB  1 
ATOM   8815  C  CG  . GLU   E  5  173 ? -10.515 -85.890  59.302  1.00 140.33 ? 172 GLU   E CG  1 
ATOM   8816  C  CD  . GLU   E  5  173 ? -9.251  -85.048  59.270  1.00 145.32 ? 172 GLU   E CD  1 
ATOM   8817  O  OE1 . GLU   E  5  173 ? -8.409  -85.219  60.174  1.00 145.62 ? 172 GLU   E OE1 1 
ATOM   8818  O  OE2 . GLU   E  5  173 ? -9.107  -84.224  58.342  1.00 152.57 ? 172 GLU   E OE2 1 
ATOM   8819  N  N   . ARG   E  5  174 ? -14.604 -86.046  57.998  1.00 140.57 ? 173 ARG   E N   1 
ATOM   8820  C  CA  . ARG   E  5  174 ? -15.968 -85.785  58.536  1.00 143.38 ? 173 ARG   E CA  1 
ATOM   8821  C  C   . ARG   E  5  174 ? -16.816 -87.062  58.470  1.00 141.45 ? 173 ARG   E C   1 
ATOM   8822  O  O   . ARG   E  5  174 ? -17.564 -87.312  59.432  1.00 143.17 ? 173 ARG   E O   1 
ATOM   8823  C  CB  . ARG   E  5  174 ? -16.675 -84.672  57.755  1.00 147.55 ? 173 ARG   E CB  1 
ATOM   8824  C  CG  . ARG   E  5  174 ? -16.136 -83.271  58.008  1.00 152.22 ? 173 ARG   E CG  1 
ATOM   8825  C  CD  . ARG   E  5  174 ? -16.833 -82.220  57.157  1.00 156.00 ? 173 ARG   E CD  1 
ATOM   8826  N  NE  . ARG   E  5  174 ? -18.286 -82.385  57.133  1.00 161.66 ? 173 ARG   E NE  1 
ATOM   8827  C  CZ  . ARG   E  5  174 ? -19.001 -82.902  56.129  1.00 161.14 ? 173 ARG   E CZ  1 
ATOM   8828  N  NH1 . ARG   E  5  174 ? -18.419 -83.319  55.016  1.00 157.23 ? 173 ARG   E NH1 1 
ATOM   8829  N  NH2 . ARG   E  5  174 ? -20.316 -82.997  56.245  1.00 161.59 ? 173 ARG   E NH2 1 
ATOM   8830  N  N   . THR   E  5  175 ? -16.707 -87.828  57.376  1.00 140.86 ? 174 THR   E N   1 
ATOM   8831  C  CA  . THR   E  5  175 ? -17.564 -89.009  57.066  1.00 142.89 ? 174 THR   E CA  1 
ATOM   8832  C  C   . THR   E  5  175 ? -17.026 -90.285  57.739  1.00 139.44 ? 174 THR   E C   1 
ATOM   8833  O  O   . THR   E  5  175 ? -17.693 -91.332  57.604  1.00 138.19 ? 174 THR   E O   1 
ATOM   8834  C  CB  . THR   E  5  175 ? -17.684 -89.219  55.548  1.00 140.00 ? 174 THR   E CB  1 
ATOM   8835  O  OG1 . THR   E  5  175 ? -17.676 -87.946  54.904  1.00 141.10 ? 174 THR   E OG1 1 
ATOM   8836  C  CG2 . THR   E  5  175 ? -18.939 -89.964  55.148  1.00 143.56 ? 174 THR   E CG2 1 
ATOM   8837  N  N   . LEU   E  5  176 ? -15.890 -90.210  58.446  1.00 138.33 ? 175 LEU   E N   1 
ATOM   8838  C  CA  . LEU   E  5  176 ? -15.136 -91.389  58.965  1.00 132.84 ? 175 LEU   E CA  1 
ATOM   8839  C  C   . LEU   E  5  176 ? -16.092 -92.389  59.628  1.00 133.74 ? 175 LEU   E C   1 
ATOM   8840  O  O   . LEU   E  5  176 ? -16.042 -93.578  59.260  1.00 138.10 ? 175 LEU   E O   1 
ATOM   8841  C  CB  . LEU   E  5  176 ? -14.058 -90.927  59.954  1.00 130.05 ? 175 LEU   E CB  1 
ATOM   8842  C  CG  . LEU   E  5  176 ? -13.233 -92.038  60.607  1.00 126.37 ? 175 LEU   E CG  1 
ATOM   8843  C  CD1 . LEU   E  5  176 ? -12.691 -93.014  59.571  1.00 126.07 ? 175 LEU   E CD1 1 
ATOM   8844  C  CD2 . LEU   E  5  176 ? -12.092 -91.458  61.427  1.00 123.23 ? 175 LEU   E CD2 1 
ATOM   8845  N  N   . ASP   E  5  177 ? -16.927 -91.924  60.561  1.00 133.74 ? 176 ASP   E N   1 
ATOM   8846  C  CA  . ASP   E  5  177 ? -17.787 -92.786  61.415  1.00 132.20 ? 176 ASP   E CA  1 
ATOM   8847  C  C   . ASP   E  5  177 ? -18.854 -93.486  60.564  1.00 131.91 ? 176 ASP   E C   1 
ATOM   8848  O  O   . ASP   E  5  177 ? -19.257 -94.596  60.953  1.00 132.26 ? 176 ASP   E O   1 
ATOM   8849  C  CB  . ASP   E  5  177 ? -18.412 -91.985  62.560  1.00 132.28 ? 176 ASP   E CB  1 
ATOM   8850  C  CG  . ASP   E  5  177 ? -17.390 -91.448  63.547  1.00 133.40 ? 176 ASP   E CG  1 
ATOM   8851  O  OD1 . ASP   E  5  177 ? -16.559 -92.248  64.021  1.00 135.12 ? 176 ASP   E OD1 1 
ATOM   8852  O  OD2 . ASP   E  5  177 ? -17.426 -90.231  63.824  1.00 129.72 ? 176 ASP   E OD2 1 
ATOM   8853  N  N   . THR   E  5  178 ? -19.290 -92.876  59.454  1.00 129.97 ? 177 THR   E N   1 
ATOM   8854  C  CA  . THR   E  5  178 ? -20.338 -93.428  58.550  1.00 130.83 ? 177 THR   E CA  1 
ATOM   8855  C  C   . THR   E  5  178 ? -19.757 -94.552  57.683  1.00 133.97 ? 177 THR   E C   1 
ATOM   8856  O  O   . THR   E  5  178 ? -20.276 -95.685  57.775  1.00 132.52 ? 177 THR   E O   1 
ATOM   8857  C  CB  . THR   E  5  178 ? -20.968 -92.349  57.659  1.00 127.01 ? 177 THR   E CB  1 
ATOM   8858  O  OG1 . THR   E  5  178 ? -21.441 -91.294  58.496  1.00 129.62 ? 177 THR   E OG1 1 
ATOM   8859  C  CG2 . THR   E  5  178 ? -22.111 -92.876  56.817  1.00 125.58 ? 177 THR   E CG2 1 
ATOM   8860  N  N   . PHE   E  5  179 ? -18.741 -94.252  56.864  1.00 135.49 ? 178 PHE   E N   1 
ATOM   8861  C  CA  . PHE   E  5  179 ? -18.286 -95.129  55.750  1.00 134.82 ? 178 PHE   E CA  1 
ATOM   8862  C  C   . PHE   E  5  179 ? -17.531 -96.356  56.285  1.00 134.65 ? 178 PHE   E C   1 
ATOM   8863  O  O   . PHE   E  5  179 ? -17.514 -97.376  55.567  1.00 132.56 ? 178 PHE   E O   1 
ATOM   8864  C  CB  . PHE   E  5  179 ? -17.475 -94.352  54.706  1.00 134.14 ? 178 PHE   E CB  1 
ATOM   8865  C  CG  . PHE   E  5  179 ? -16.057 -93.998  55.080  1.00 131.53 ? 178 PHE   E CG  1 
ATOM   8866  C  CD1 . PHE   E  5  179 ? -15.047 -94.949  55.042  1.00 130.23 ? 178 PHE   E CD1 1 
ATOM   8867  C  CD2 . PHE   E  5  179 ? -15.722 -92.698  55.423  1.00 132.80 ? 178 PHE   E CD2 1 
ATOM   8868  C  CE1 . PHE   E  5  179 ? -13.742 -94.614  55.371  1.00 129.29 ? 178 PHE   E CE1 1 
ATOM   8869  C  CE2 . PHE   E  5  179 ? -14.416 -92.364  55.746  1.00 132.87 ? 178 PHE   E CE2 1 
ATOM   8870  C  CZ  . PHE   E  5  179 ? -13.429 -93.322  55.721  1.00 130.37 ? 178 PHE   E CZ  1 
ATOM   8871  N  N   . ILE   E  5  180 ? -16.935 -96.276  57.481  1.00 132.81 ? 179 ILE   E N   1 
ATOM   8872  C  CA  . ILE   E  5  180 ? -16.155 -97.399  58.089  1.00 134.44 ? 179 ILE   E CA  1 
ATOM   8873  C  C   . ILE   E  5  180 ? -17.097 -98.575  58.392  1.00 138.07 ? 179 ILE   E C   1 
ATOM   8874  O  O   . ILE   E  5  180 ? -16.610 -99.724  58.394  1.00 139.52 ? 179 ILE   E O   1 
ATOM   8875  C  CB  . ILE   E  5  180 ? -15.360 -96.954  59.339  1.00 134.86 ? 179 ILE   E CB  1 
ATOM   8876  C  CG1 . ILE   E  5  180 ? -14.364 -98.024  59.800  1.00 135.04 ? 179 ILE   E CG1 1 
ATOM   8877  C  CG2 . ILE   E  5  180 ? -16.287 -96.550  60.478  1.00 133.37 ? 179 ILE   E CG2 1 
ATOM   8878  C  CD1 . ILE   E  5  180 ? -13.374 -98.469  58.745  1.00 137.05 ? 179 ILE   E CD1 1 
ATOM   8879  N  N   . LYS   E  5  181 ? -18.388 -98.309  58.628  1.00 138.09 ? 180 LYS   E N   1 
ATOM   8880  C  CA  . LYS   E  5  181 ? -19.402 -99.342  58.983  1.00 139.91 ? 180 LYS   E CA  1 
ATOM   8881  C  C   . LYS   E  5  181 ? -20.310 -99.660  57.783  1.00 138.25 ? 180 LYS   E C   1 
ATOM   8882  O  O   . LYS   E  5  181 ? -21.410 -100.200 58.018  1.00 136.86 ? 180 LYS   E O   1 
ATOM   8883  C  CB  . LYS   E  5  181 ? -20.220 -98.880  60.193  1.00 140.01 ? 180 LYS   E CB  1 
ATOM   8884  C  CG  . LYS   E  5  181 ? -19.515 -99.031  61.536  1.00 139.95 ? 180 LYS   E CG  1 
ATOM   8885  C  CD  . LYS   E  5  181 ? -20.293 -98.487  62.718  1.00 141.06 ? 180 LYS   E CD  1 
ATOM   8886  C  CE  . LYS   E  5  181 ? -20.994 -97.178  62.423  1.00 145.13 ? 180 LYS   E CE  1 
ATOM   8887  N  NZ  . LYS   E  5  181 ? -21.340 -96.445  63.663  1.00 150.26 ? 180 LYS   E NZ  1 
ATOM   8888  N  N   . ILE   E  5  182 ? -19.877 -99.367  56.550  1.00 137.70 ? 181 ILE   E N   1 
ATOM   8889  C  CA  . ILE   E  5  182 ? -20.548 -99.868  55.310  1.00 139.53 ? 181 ILE   E CA  1 
ATOM   8890  C  C   . ILE   E  5  182 ? -19.965 -101.254 55.007  1.00 136.02 ? 181 ILE   E C   1 
ATOM   8891  O  O   . ILE   E  5  182 ? -19.125 -101.378 54.089  1.00 132.03 ? 181 ILE   E O   1 
ATOM   8892  C  CB  . ILE   E  5  182 ? -20.422 -98.887  54.124  1.00 139.71 ? 181 ILE   E CB  1 
ATOM   8893  C  CG1 . ILE   E  5  182 ? -20.893 -97.480  54.504  1.00 141.72 ? 181 ILE   E CG1 1 
ATOM   8894  C  CG2 . ILE   E  5  182 ? -21.177 -99.419  52.911  1.00 141.72 ? 181 ILE   E CG2 1 
ATOM   8895  C  CD1 . ILE   E  5  182 ? -20.700 -96.439  53.420  1.00 140.81 ? 181 ILE   E CD1 1 
ATOM   8896  N  N   . ASP   E  5  183 ? -20.395 -102.251 55.784  1.00 134.17 ? 182 ASP   E N   1 
ATOM   8897  C  CA  . ASP   E  5  183 ? -19.955 -103.667 55.684  1.00 132.37 ? 182 ASP   E CA  1 
ATOM   8898  C  C   . ASP   E  5  183 ? -20.978 -104.442 54.849  1.00 129.67 ? 182 ASP   E C   1 
ATOM   8899  O  O   . ASP   E  5  183 ? -22.187 -104.206 55.031  1.00 127.63 ? 182 ASP   E O   1 
ATOM   8900  C  CB  . ASP   E  5  183 ? -19.780 -104.279 57.076  1.00 132.94 ? 182 ASP   E CB  1 
ATOM   8901  C  CG  . ASP   E  5  183 ? -18.760 -103.551 57.936  1.00 132.47 ? 182 ASP   E CG  1 
ATOM   8902  O  OD1 . ASP   E  5  183 ? -17.795 -103.006 57.365  1.00 132.56 ? 182 ASP   E OD1 1 
ATOM   8903  O  OD2 . ASP   E  5  183 ? -18.944 -103.526 59.168  1.00 136.54 ? 182 ASP   E OD2 1 
ATOM   8904  N  N   . GLY   E  5  184 ? -20.502 -105.324 53.965  1.00 132.60 ? 183 GLY   E N   1 
ATOM   8905  C  CA  . GLY   E  5  184 ? -21.343 -106.192 53.118  1.00 135.95 ? 183 GLY   E CA  1 
ATOM   8906  C  C   . GLY   E  5  184 ? -22.229 -105.392 52.177  1.00 136.41 ? 183 GLY   E C   1 
ATOM   8907  O  O   . GLY   E  5  184 ? -23.348 -105.859 51.890  1.00 143.37 ? 183 GLY   E O   1 
ATOM   8908  N  N   . ASN   E  5  185 ? -21.756 -104.228 51.718  1.00 138.12 ? 184 ASN   E N   1 
ATOM   8909  C  CA  . ASN   E  5  185 ? -22.473 -103.360 50.744  1.00 138.32 ? 184 ASN   E CA  1 
ATOM   8910  C  C   . ASN   E  5  185 ? -21.435 -102.641 49.886  1.00 138.34 ? 184 ASN   E C   1 
ATOM   8911  O  O   . ASN   E  5  185 ? -20.986 -101.550 50.230  1.00 137.09 ? 184 ASN   E O   1 
ATOM   8912  C  CB  . ASN   E  5  185 ? -23.434 -102.393 51.446  1.00 138.86 ? 184 ASN   E CB  1 
ATOM   8913  C  CG  . ASN   E  5  185 ? -24.544 -101.849 50.565  1.00 138.78 ? 184 ASN   E CG  1 
ATOM   8914  O  OD1 . ASN   E  5  185 ? -25.437 -101.167 51.061  1.00 134.23 ? 184 ASN   E OD1 1 
ATOM   8915  N  ND2 . ASN   E  5  185 ? -24.521 -102.133 49.270  1.00 140.88 ? 184 ASN   E ND2 1 
ATOM   8916  N  N   . PRO   E  5  186 ? -21.005 -103.251 48.758  1.00 138.47 ? 185 PRO   E N   1 
ATOM   8917  C  CA  . PRO   E  5  186 ? -20.055 -102.620 47.840  1.00 137.61 ? 185 PRO   E CA  1 
ATOM   8918  C  C   . PRO   E  5  186 ? -20.524 -101.271 47.265  1.00 141.35 ? 185 PRO   E C   1 
ATOM   8919  O  O   . PRO   E  5  186 ? -19.779 -100.311 47.369  1.00 139.61 ? 185 PRO   E O   1 
ATOM   8920  C  CB  . PRO   E  5  186 ? -19.913 -103.652 46.708  1.00 135.33 ? 185 PRO   E CB  1 
ATOM   8921  C  CG  . PRO   E  5  186 ? -20.269 -104.967 47.359  1.00 135.47 ? 185 PRO   E CG  1 
ATOM   8922  C  CD  . PRO   E  5  186 ? -21.370 -104.612 48.335  1.00 137.49 ? 185 PRO   E CD  1 
ATOM   8923  N  N   . ASP   E  5  187 ? -21.730 -101.231 46.686  1.00 144.96 ? 186 ASP   E N   1 
ATOM   8924  C  CA  . ASP   E  5  187 ? -22.267 -100.068 45.922  1.00 145.80 ? 186 ASP   E CA  1 
ATOM   8925  C  C   . ASP   E  5  187 ? -22.338 -98.820  46.813  1.00 149.42 ? 186 ASP   E C   1 
ATOM   8926  O  O   . ASP   E  5  187 ? -22.176 -97.709  46.267  1.00 159.06 ? 186 ASP   E O   1 
ATOM   8927  C  CB  . ASP   E  5  187 ? -23.631 -100.385 45.301  1.00 142.78 ? 186 ASP   E CB  1 
ATOM   8928  C  CG  . ASP   E  5  187 ? -23.546 -101.263 44.065  1.00 142.14 ? 186 ASP   E CG  1 
ATOM   8929  O  OD1 . ASP   E  5  187 ? -22.547 -101.996 43.934  1.00 140.07 ? 186 ASP   E OD1 1 
ATOM   8930  O  OD2 . ASP   E  5  187 ? -24.477 -101.198 43.240  1.00 143.13 ? 186 ASP   E OD2 1 
ATOM   8931  N  N   . GLU   E  5  188 ? -22.575 -98.984  48.120  1.00 148.84 ? 187 GLU   E N   1 
ATOM   8932  C  CA  . GLU   E  5  188 ? -22.681 -97.857  49.091  1.00 146.53 ? 187 GLU   E CA  1 
ATOM   8933  C  C   . GLU   E  5  188 ? -21.286 -97.323  49.440  1.00 139.76 ? 187 GLU   E C   1 
ATOM   8934  O  O   . GLU   E  5  188 ? -21.164 -96.096  49.615  1.00 141.48 ? 187 GLU   E O   1 
ATOM   8935  C  CB  . GLU   E  5  188 ? -23.433 -98.279  50.357  1.00 145.26 ? 187 GLU   E CB  1 
ATOM   8936  C  CG  . GLU   E  5  188 ? -24.943 -98.192  50.221  1.00 145.47 ? 187 GLU   E CG  1 
ATOM   8937  C  CD  . GLU   E  5  188 ? -25.466 -96.817  49.837  1.00 142.90 ? 187 GLU   E CD  1 
ATOM   8938  O  OE1 . GLU   E  5  188 ? -26.338 -96.745  48.950  1.00 148.59 ? 187 GLU   E OE1 1 
ATOM   8939  O  OE2 . GLU   E  5  188 ? -24.996 -95.823  50.421  1.00 139.50 ? 187 GLU   E OE2 1 
ATOM   8940  N  N   . LEU   E  5  189 ? -20.283 -98.201  49.547  1.00 138.71 ? 188 LEU   E N   1 
ATOM   8941  C  CA  . LEU   E  5  189 ? -18.877 -97.812  49.851  1.00 134.36 ? 188 LEU   E CA  1 
ATOM   8942  C  C   . LEU   E  5  189 ? -18.301 -97.032  48.661  1.00 134.15 ? 188 LEU   E C   1 
ATOM   8943  O  O   . LEU   E  5  189 ? -17.498 -96.110  48.897  1.00 138.30 ? 188 LEU   E O   1 
ATOM   8944  C  CB  . LEU   E  5  189 ? -18.030 -99.057  50.143  1.00 132.89 ? 188 LEU   E CB  1 
ATOM   8945  C  CG  . LEU   E  5  189 ? -17.110 -98.984  51.364  1.00 129.93 ? 188 LEU   E CG  1 
ATOM   8946  C  CD1 . LEU   E  5  189 ? -16.058 -100.077 51.298  1.00 130.03 ? 188 LEU   E CD1 1 
ATOM   8947  C  CD2 . LEU   E  5  189 ? -16.437 -97.626  51.505  1.00 128.64 ? 188 LEU   E CD2 1 
ATOM   8948  N  N   . ILE   E  5  190 ? -18.692 -97.401  47.435  1.00 132.41 ? 189 ILE   E N   1 
ATOM   8949  C  CA  . ILE   E  5  190 ? -18.284 -96.714  46.172  1.00 131.54 ? 189 ILE   E CA  1 
ATOM   8950  C  C   . ILE   E  5  190 ? -18.931 -95.322  46.145  1.00 131.40 ? 189 ILE   E C   1 
ATOM   8951  O  O   . ILE   E  5  190 ? -18.199 -94.344  45.899  1.00 128.34 ? 189 ILE   E O   1 
ATOM   8952  C  CB  . ILE   E  5  190 ? -18.645 -97.554  44.928  1.00 129.90 ? 189 ILE   E CB  1 
ATOM   8953  C  CG1 . ILE   E  5  190 ? -17.881 -98.883  44.900  1.00 127.09 ? 189 ILE   E CG1 1 
ATOM   8954  C  CG2 . ILE   E  5  190 ? -18.416 -96.757  43.651  1.00 131.21 ? 189 ILE   E CG2 1 
ATOM   8955  C  CD1 . ILE   E  5  190 ? -18.449 -99.905  43.942  1.00 127.24 ? 189 ILE   E CD1 1 
ATOM   8956  N  N   . LYS   E  5  191 ? -20.244 -95.243  46.397  1.00 135.05 ? 190 LYS   E N   1 
ATOM   8957  C  CA  . LYS   E  5  191 ? -21.028 -93.975  46.441  1.00 137.00 ? 190 LYS   E CA  1 
ATOM   8958  C  C   . LYS   E  5  191 ? -20.337 -92.965  47.368  1.00 137.53 ? 190 LYS   E C   1 
ATOM   8959  O  O   . LYS   E  5  191 ? -20.258 -91.781  46.984  1.00 138.03 ? 190 LYS   E O   1 
ATOM   8960  C  CB  . LYS   E  5  191 ? -22.470 -94.235  46.892  1.00 138.51 ? 190 LYS   E CB  1 
ATOM   8961  C  CG  . LYS   E  5  191 ? -23.453 -94.530  45.767  1.00 139.83 ? 190 LYS   E CG  1 
ATOM   8962  C  CD  . LYS   E  5  191 ? -24.873 -94.754  46.241  1.00 142.96 ? 190 LYS   E CD  1 
ATOM   8963  C  CE  . LYS   E  5  191 ? -25.893 -94.600  45.133  1.00 145.01 ? 190 LYS   E CE  1 
ATOM   8964  N  NZ  . LYS   E  5  191 ? -27.266 -94.897  45.605  1.00 145.57 ? 190 LYS   E NZ  1 
ATOM   8965  N  N   . ALA   E  5  192 ? -19.857 -93.418  48.533  1.00 138.30 ? 191 ALA   E N   1 
ATOM   8966  C  CA  . ALA   E  5  192 ? -19.140 -92.601  49.544  1.00 136.14 ? 191 ALA   E CA  1 
ATOM   8967  C  C   . ALA   E  5  192 ? -17.803 -92.110  48.972  1.00 131.42 ? 191 ALA   E C   1 
ATOM   8968  O  O   . ALA   E  5  192 ? -17.428 -90.957  49.263  1.00 133.73 ? 191 ALA   E O   1 
ATOM   8969  C  CB  . ALA   E  5  192 ? -18.932 -93.398  50.810  1.00 136.85 ? 191 ALA   E CB  1 
ATOM   8970  N  N   . GLY   E  5  193 ? -17.111 -92.964  48.208  1.00 128.44 ? 192 GLY   E N   1 
ATOM   8971  C  CA  . GLY   E  5  193 ? -15.835 -92.651  47.534  1.00 121.13 ? 192 GLY   E CA  1 
ATOM   8972  C  C   . GLY   E  5  193 ? -16.022 -91.710  46.354  1.00 118.97 ? 192 GLY   E C   1 
ATOM   8973  O  O   . GLY   E  5  193 ? -15.105 -90.905  46.098  1.00 114.03 ? 192 GLY   E O   1 
ATOM   8974  N  N   . VAL   E  5  194 ? -17.152 -91.819  45.644  1.00 119.71 ? 193 VAL   E N   1 
ATOM   8975  C  CA  . VAL   E  5  194 ? -17.506 -90.953  44.478  1.00 120.39 ? 193 VAL   E CA  1 
ATOM   8976  C  C   . VAL   E  5  194 ? -17.926 -89.570  44.996  1.00 122.63 ? 193 VAL   E C   1 
ATOM   8977  O  O   . VAL   E  5  194 ? -17.611 -88.570  44.322  1.00 124.48 ? 193 VAL   E O   1 
ATOM   8978  C  CB  . VAL   E  5  194 ? -18.595 -91.600  43.597  1.00 119.32 ? 193 VAL   E CB  1 
ATOM   8979  C  CG1 . VAL   E  5  194 ? -19.112 -90.650  42.528  1.00 120.18 ? 193 VAL   E CG1 1 
ATOM   8980  C  CG2 . VAL   E  5  194 ? -18.099 -92.886  42.956  1.00 117.08 ? 193 VAL   E CG2 1 
ATOM   8981  N  N   . GLU   E  5  195 ? -18.613 -89.513  46.142  1.00 123.27 ? 194 GLU   E N   1 
ATOM   8982  C  CA  . GLU   E  5  195 ? -19.002 -88.243  46.813  1.00 125.83 ? 194 GLU   E CA  1 
ATOM   8983  C  C   . GLU   E  5  195 ? -17.748 -87.562  47.376  1.00 123.62 ? 194 GLU   E C   1 
ATOM   8984  O  O   . GLU   E  5  195 ? -17.698 -86.320  47.358  1.00 125.86 ? 194 GLU   E O   1 
ATOM   8985  C  CB  . GLU   E  5  195 ? -20.027 -88.498  47.919  1.00 129.90 ? 194 GLU   E CB  1 
ATOM   8986  C  CG  . GLU   E  5  195 ? -20.521 -87.226  48.581  1.00 135.42 ? 194 GLU   E CG  1 
ATOM   8987  C  CD  . GLU   E  5  195 ? -21.821 -87.381  49.350  1.00 144.18 ? 194 GLU   E CD  1 
ATOM   8988  O  OE1 . GLU   E  5  195 ? -21.817 -87.128  50.570  1.00 153.81 ? 194 GLU   E OE1 1 
ATOM   8989  O  OE2 . GLU   E  5  195 ? -22.835 -87.748  48.724  1.00 151.42 ? 194 GLU   E OE2 1 
ATOM   8990  N  N   . ALA   E  5  196 ? -16.781 -88.346  47.860  1.00 121.29 ? 195 ALA   E N   1 
ATOM   8991  C  CA  . ALA   E  5  196 ? -15.492 -87.862  48.409  1.00 118.82 ? 195 ALA   E CA  1 
ATOM   8992  C  C   . ALA   E  5  196 ? -14.712 -87.123  47.316  1.00 119.19 ? 195 ALA   E C   1 
ATOM   8993  O  O   . ALA   E  5  196 ? -14.301 -85.975  47.566  1.00 117.08 ? 195 ALA   E O   1 
ATOM   8994  C  CB  . ALA   E  5  196 ? -14.698 -89.013  48.980  1.00 116.96 ? 195 ALA   E CB  1 
ATOM   8995  N  N   . ILE   E  5  197 ? -14.540 -87.748  46.145  1.00 121.65 ? 196 ILE   E N   1 
ATOM   8996  C  CA  . ILE   E  5  197 ? -13.735 -87.197  45.011  1.00 124.62 ? 196 ILE   E CA  1 
ATOM   8997  C  C   . ILE   E  5  197 ? -14.452 -85.978  44.414  1.00 127.23 ? 196 ILE   E C   1 
ATOM   8998  O  O   . ILE   E  5  197 ? -13.764 -85.149  43.785  1.00 128.74 ? 196 ILE   E O   1 
ATOM   8999  C  CB  . ILE   E  5  197 ? -13.437 -88.270  43.940  1.00 125.79 ? 196 ILE   E CB  1 
ATOM   9000  C  CG1 . ILE   E  5  197 ? -12.236 -87.875  43.076  1.00 127.38 ? 196 ILE   E CG1 1 
ATOM   9001  C  CG2 . ILE   E  5  197 ? -14.665 -88.572  43.091  1.00 125.74 ? 196 ILE   E CG2 1 
ATOM   9002  C  CD1 . ILE   E  5  197 ? -11.610 -89.025  42.323  1.00 127.64 ? 196 ILE   E CD1 1 
ATOM   9003  N  N   . SER   E  5  198 ? -15.773 -85.872  44.598  1.00 129.85 ? 197 SER   E N   1 
ATOM   9004  C  CA  . SER   E  5  198 ? -16.606 -84.749  44.090  1.00 132.39 ? 197 SER   E CA  1 
ATOM   9005  C  C   . SER   E  5  198 ? -16.263 -83.443  44.819  1.00 132.20 ? 197 SER   E C   1 
ATOM   9006  O  O   . SER   E  5  198 ? -16.606 -82.374  44.281  1.00 134.00 ? 197 SER   E O   1 
ATOM   9007  C  CB  . SER   E  5  198 ? -18.077 -85.060  44.193  1.00 135.54 ? 197 SER   E CB  1 
ATOM   9008  O  OG  . SER   E  5  198 ? -18.421 -86.155  43.358  1.00 137.88 ? 197 SER   E OG  1 
ATOM   9009  N  N   . GLN   E  5  199 ? -15.607 -83.525  45.985  1.00 130.39 ? 198 GLN   E N   1 
ATOM   9010  C  CA  . GLN   E  5  199 ? -15.180 -82.351  46.798  1.00 129.89 ? 198 GLN   E CA  1 
ATOM   9011  C  C   . GLN   E  5  199 ? -13.841 -81.803  46.282  1.00 129.02 ? 198 GLN   E C   1 
ATOM   9012  O  O   . GLN   E  5  199 ? -13.356 -80.820  46.872  1.00 131.82 ? 198 GLN   E O   1 
ATOM   9013  C  CB  . GLN   E  5  199 ? -15.048 -82.723  48.278  1.00 131.53 ? 198 GLN   E CB  1 
ATOM   9014  C  CG  . GLN   E  5  199 ? -16.259 -83.446  48.855  1.00 134.46 ? 198 GLN   E CG  1 
ATOM   9015  C  CD  . GLN   E  5  199 ? -17.562 -82.732  48.588  1.00 135.59 ? 198 GLN   E CD  1 
ATOM   9016  O  OE1 . GLN   E  5  199 ? -17.696 -81.535  48.832  1.00 135.01 ? 198 GLN   E OE1 1 
ATOM   9017  N  NE2 . GLN   E  5  199 ? -18.544 -83.469  48.091  1.00 138.87 ? 198 GLN   E NE2 1 
ATOM   9018  N  N   . SER   E  5  200 ? -13.266 -82.412  45.237  1.00 129.40 ? 199 SER   E N   1 
ATOM   9019  C  CA  . SER   E  5  200 ? -11.956 -82.033  44.641  1.00 129.26 ? 199 SER   E CA  1 
ATOM   9020  C  C   . SER   E  5  200 ? -12.117 -81.555  43.190  1.00 131.96 ? 199 SER   E C   1 
ATOM   9021  O  O   . SER   E  5  200 ? -11.082 -81.270  42.554  1.00 128.55 ? 199 SER   E O   1 
ATOM   9022  C  CB  . SER   E  5  200 ? -10.993 -83.187  44.720  1.00 126.16 ? 199 SER   E CB  1 
ATOM   9023  O  OG  . SER   E  5  200 ? -10.842 -83.629  46.061  1.00 125.24 ? 199 SER   E OG  1 
ATOM   9024  N  N   . LEU   E  5  201 ? -13.354 -81.461  42.689  1.00 137.95 ? 200 LEU   E N   1 
ATOM   9025  C  CA  . LEU   E  5  201 ? -13.662 -81.056  41.289  1.00 144.01 ? 200 LEU   E CA  1 
ATOM   9026  C  C   . LEU   E  5  201 ? -13.797 -79.531  41.207  1.00 145.04 ? 200 LEU   E C   1 
ATOM   9027  O  O   . LEU   E  5  201 ? -14.333 -78.933  42.161  1.00 147.76 ? 200 LEU   E O   1 
ATOM   9028  C  CB  . LEU   E  5  201 ? -14.964 -81.726  40.841  1.00 143.70 ? 200 LEU   E CB  1 
ATOM   9029  C  CG  . LEU   E  5  201 ? -14.962 -83.253  40.812  1.00 143.70 ? 200 LEU   E CG  1 
ATOM   9030  C  CD1 . LEU   E  5  201 ? -16.372 -83.779  40.590  1.00 141.02 ? 200 LEU   E CD1 1 
ATOM   9031  C  CD2 . LEU   E  5  201 ? -14.020 -83.781  39.740  1.00 141.12 ? 200 LEU   E CD2 1 
ATOM   9032  N  N   . ARG   E  5  202 ? -13.342 -78.941  40.096  1.00 152.73 ? 201 ARG   E N   1 
ATOM   9033  C  CA  . ARG   E  5  202 ? -13.470 -77.491  39.781  1.00 154.24 ? 201 ARG   E CA  1 
ATOM   9034  C  C   . ARG   E  5  202 ? -13.758 -77.321  38.285  1.00 155.30 ? 201 ARG   E C   1 
ATOM   9035  O  O   . ARG   E  5  202 ? -12.896 -77.709  37.473  1.00 147.75 ? 201 ARG   E O   1 
ATOM   9036  C  CB  . ARG   E  5  202 ? -12.192 -76.740  40.164  1.00 157.20 ? 201 ARG   E CB  1 
ATOM   9037  C  CG  . ARG   E  5  202 ? -12.029 -76.507  41.658  1.00 163.37 ? 201 ARG   E CG  1 
ATOM   9038  C  CD  . ARG   E  5  202 ? -12.342 -75.082  42.069  1.00 168.48 ? 201 ARG   E CD  1 
ATOM   9039  N  NE  . ARG   E  5  202 ? -11.178 -74.213  41.933  1.00 175.84 ? 201 ARG   E NE  1 
ATOM   9040  C  CZ  . ARG   E  5  202 ? -10.174 -74.130  42.807  1.00 176.16 ? 201 ARG   E CZ  1 
ATOM   9041  N  NH1 . ARG   E  5  202 ? -10.169 -74.869  43.906  1.00 172.89 ? 201 ARG   E NH1 1 
ATOM   9042  N  NH2 . ARG   E  5  202 ? -9.169  -73.304  42.573  1.00 177.44 ? 201 ARG   E NH2 1 
ATOM   9043  N  N   . ASP   E  5  203 ? -14.936 -76.785  37.947  1.00 157.64 ? 202 ASP   E N   1 
ATOM   9044  C  CA  . ASP   E  5  203 ? -15.387 -76.470  36.561  1.00 164.54 ? 202 ASP   E CA  1 
ATOM   9045  C  C   . ASP   E  5  203 ? -15.684 -77.759  35.776  1.00 163.54 ? 202 ASP   E C   1 
ATOM   9046  O  O   . ASP   E  5  203 ? -16.480 -77.679  34.820  1.00 167.80 ? 202 ASP   E O   1 
ATOM   9047  C  CB  . ASP   E  5  203 ? -14.377 -75.580  35.828  1.00 166.30 ? 202 ASP   E CB  1 
ATOM   9048  C  CG  . ASP   E  5  203 ? -14.247 -74.188  36.424  1.00 167.84 ? 202 ASP   E CG  1 
ATOM   9049  O  OD1 . ASP   E  5  203 ? -13.865 -74.090  37.607  1.00 167.95 ? 202 ASP   E OD1 1 
ATOM   9050  O  OD2 . ASP   E  5  203 ? -14.540 -73.211  35.704  1.00 168.15 ? 202 ASP   E OD2 1 
ATOM   9051  N  N   . GLU   E  5  204 ? -15.080 -78.892  36.153  1.00 162.40 ? 203 GLU   E N   1 
ATOM   9052  C  CA  . GLU   E  5  204 ? -15.301 -80.221  35.523  1.00 161.07 ? 203 GLU   E CA  1 
ATOM   9053  C  C   . GLU   E  5  204 ? -16.153 -81.080  36.465  1.00 154.88 ? 203 GLU   E C   1 
ATOM   9054  O  O   . GLU   E  5  204 ? -16.018 -80.908  37.692  1.00 152.69 ? 203 GLU   E O   1 
ATOM   9055  C  CB  . GLU   E  5  204 ? -13.956 -80.888  35.229  1.00 165.35 ? 203 GLU   E CB  1 
ATOM   9056  C  CG  . GLU   E  5  204 ? -14.054 -82.073  34.285  1.00 167.52 ? 203 GLU   E CG  1 
ATOM   9057  C  CD  . GLU   E  5  204 ? -12.751 -82.821  34.056  1.00 169.12 ? 203 GLU   E CD  1 
ATOM   9058  O  OE1 . GLU   E  5  204 ? -12.648 -83.520  33.028  1.00 164.66 ? 203 GLU   E OE1 1 
ATOM   9059  O  OE2 . GLU   E  5  204 ? -11.846 -82.711  34.908  1.00 172.33 ? 203 GLU   E OE2 1 
ATOM   9060  N  N   . SER   E  5  205 ? -17.000 -81.956  35.912  1.00 154.89 ? 204 SER   E N   1 
ATOM   9061  C  CA  . SER   E  5  205 ? -17.824 -82.941  36.664  1.00 153.57 ? 204 SER   E CA  1 
ATOM   9062  C  C   . SER   E  5  205 ? -17.525 -84.362  36.166  1.00 151.16 ? 204 SER   E C   1 
ATOM   9063  O  O   . SER   E  5  205 ? -16.942 -84.495  35.071  1.00 154.58 ? 204 SER   E O   1 
ATOM   9064  C  CB  . SER   E  5  205 ? -19.293 -82.614  36.573  1.00 153.22 ? 204 SER   E CB  1 
ATOM   9065  O  OG  . SER   E  5  205 ? -19.706 -82.488  35.220  1.00 153.56 ? 204 SER   E OG  1 
ATOM   9066  N  N   . LEU   E  5  206 ? -17.908 -85.377  36.949  1.00 149.11 ? 205 LEU   E N   1 
ATOM   9067  C  CA  . LEU   E  5  206 ? -17.597 -86.810  36.685  1.00 147.54 ? 205 LEU   E CA  1 
ATOM   9068  C  C   . LEU   E  5  206 ? -18.441 -87.301  35.501  1.00 147.62 ? 205 LEU   E C   1 
ATOM   9069  O  O   . LEU   E  5  206 ? -19.682 -87.337  35.638  1.00 153.26 ? 205 LEU   E O   1 
ATOM   9070  C  CB  . LEU   E  5  206 ? -17.880 -87.647  37.939  1.00 147.39 ? 205 LEU   E CB  1 
ATOM   9071  C  CG  . LEU   E  5  206 ? -17.122 -87.256  39.210  1.00 142.54 ? 205 LEU   E CG  1 
ATOM   9072  C  CD1 . LEU   E  5  206 ? -17.606 -88.076  40.396  1.00 139.92 ? 205 LEU   E CD1 1 
ATOM   9073  C  CD2 . LEU   E  5  206 ? -15.617 -87.415  39.037  1.00 140.75 ? 205 LEU   E CD2 1 
ATOM   9074  N  N   . THR   E  5  207 ? -17.787 -87.659  34.390  1.00 141.20 ? 206 THR   E N   1 
ATOM   9075  C  CA  . THR   E  5  207 ? -18.409 -88.240  33.167  1.00 138.62 ? 206 THR   E CA  1 
ATOM   9076  C  C   . THR   E  5  207 ? -18.077 -89.739  33.100  1.00 137.52 ? 206 THR   E C   1 
ATOM   9077  O  O   . THR   E  5  207 ? -17.439 -90.247  34.046  1.00 133.21 ? 206 THR   E O   1 
ATOM   9078  C  CB  . THR   E  5  207 ? -17.973 -87.487  31.901  1.00 134.66 ? 206 THR   E CB  1 
ATOM   9079  O  OG1 . THR   E  5  207 ? -16.704 -87.981  31.472  1.00 128.84 ? 206 THR   E OG1 1 
ATOM   9080  C  CG2 . THR   E  5  207 ? -17.884 -85.990  32.097  1.00 134.96 ? 206 THR   E CG2 1 
ATOM   9081  N  N   . VAL   E  5  208 ? -18.489 -90.411  32.019  1.00 138.51 ? 207 VAL   E N   1 
ATOM   9082  C  CA  . VAL   E  5  208 ? -18.490 -91.901  31.891  1.00 135.85 ? 207 VAL   E CA  1 
ATOM   9083  C  C   . VAL   E  5  208 ? -17.099 -92.401  31.482  1.00 132.75 ? 207 VAL   E C   1 
ATOM   9084  O  O   . VAL   E  5  208 ? -16.782 -93.557  31.815  1.00 132.26 ? 207 VAL   E O   1 
ATOM   9085  C  CB  . VAL   E  5  208 ? -19.574 -92.377  30.903  1.00 139.62 ? 207 VAL   E CB  1 
ATOM   9086  C  CG1 . VAL   E  5  208 ? -19.097 -92.347  29.457  1.00 141.01 ? 207 VAL   E CG1 1 
ATOM   9087  C  CG2 . VAL   E  5  208 ? -20.087 -93.760  31.267  1.00 139.58 ? 207 VAL   E CG2 1 
ATOM   9088  N  N   . ASP   E  5  209 ? -16.314 -91.580  30.775  1.00 132.12 ? 208 ASP   E N   1 
ATOM   9089  C  CA  . ASP   E  5  209 ? -14.929 -91.910  30.333  1.00 130.82 ? 208 ASP   E CA  1 
ATOM   9090  C  C   . ASP   E  5  209 ? -13.928 -91.088  31.160  1.00 131.97 ? 208 ASP   E C   1 
ATOM   9091  O  O   . ASP   E  5  209 ? -12.752 -90.998  30.753  1.00 136.33 ? 208 ASP   E O   1 
ATOM   9092  C  CB  . ASP   E  5  209 ? -14.763 -91.709  28.821  1.00 127.35 ? 208 ASP   E CB  1 
ATOM   9093  C  CG  . ASP   E  5  209 ? -15.578 -90.563  28.248  1.00 127.81 ? 208 ASP   E CG  1 
ATOM   9094  O  OD1 . ASP   E  5  209 ? -15.541 -89.470  28.840  1.00 129.76 ? 208 ASP   E OD1 1 
ATOM   9095  O  OD2 . ASP   E  5  209 ? -16.251 -90.780  27.222  1.00 121.42 ? 208 ASP   E OD2 1 
ATOM   9096  N  N   . ASN   E  5  210 ? -14.383 -90.545  32.294  1.00 132.74 ? 209 ASN   E N   1 
ATOM   9097  C  CA  . ASN   E  5  210 ? -13.620 -89.640  33.196  1.00 134.01 ? 209 ASN   E CA  1 
ATOM   9098  C  C   . ASN   E  5  210 ? -13.369 -90.335  34.542  1.00 126.62 ? 209 ASN   E C   1 
ATOM   9099  O  O   . ASN   E  5  210 ? -12.303 -90.092  35.143  1.00 121.03 ? 209 ASN   E O   1 
ATOM   9100  C  CB  . ASN   E  5  210 ? -14.385 -88.327  33.380  1.00 135.28 ? 209 ASN   E CB  1 
ATOM   9101  C  CG  . ASN   E  5  210 ? -13.661 -87.292  34.214  1.00 139.04 ? 209 ASN   E CG  1 
ATOM   9102  O  OD1 . ASN   E  5  210 ? -12.437 -87.313  34.320  1.00 146.46 ? 209 ASN   E OD1 1 
ATOM   9103  N  ND2 . ASN   E  5  210 ? -14.409 -86.363  34.791  1.00 138.83 ? 209 ASN   E ND2 1 
ATOM   9104  N  N   . LEU   E  5  211 ? -14.316 -91.170  34.985  1.00 126.14 ? 210 LEU   E N   1 
ATOM   9105  C  CA  . LEU   E  5  211 ? -14.350 -91.789  36.337  1.00 126.06 ? 210 LEU   E CA  1 
ATOM   9106  C  C   . LEU   E  5  211 ? -13.775 -93.209  36.268  1.00 120.63 ? 210 LEU   E C   1 
ATOM   9107  O  O   . LEU   E  5  211 ? -14.135 -93.957  35.335  1.00 115.93 ? 210 LEU   E O   1 
ATOM   9108  C  CB  . LEU   E  5  211 ? -15.803 -91.792  36.824  1.00 126.72 ? 210 LEU   E CB  1 
ATOM   9109  C  CG  . LEU   E  5  211 ? -16.053 -92.348  38.226  1.00 127.37 ? 210 LEU   E CG  1 
ATOM   9110  C  CD1 . LEU   E  5  211 ? -15.284 -91.568  39.283  1.00 125.78 ? 210 LEU   E CD1 1 
ATOM   9111  C  CD2 . LEU   E  5  211 ? -17.542 -92.338  38.540  1.00 130.52 ? 210 LEU   E CD2 1 
ATOM   9112  N  N   . SER   E  5  212 ? -12.908 -93.551  37.224  1.00 120.85 ? 211 SER   E N   1 
ATOM   9113  C  CA  . SER   E  5  212 ? -12.294 -94.893  37.392  1.00 118.25 ? 211 SER   E CA  1 
ATOM   9114  C  C   . SER   E  5  212 ? -12.495 -95.348  38.839  1.00 118.98 ? 211 SER   E C   1 
ATOM   9115  O  O   . SER   E  5  212 ? -12.089 -94.601  39.751  1.00 116.60 ? 211 SER   E O   1 
ATOM   9116  C  CB  . SER   E  5  212 ? -10.836 -94.878  37.024  1.00 116.00 ? 211 SER   E CB  1 
ATOM   9117  O  OG  . SER   E  5  212 ? -10.396 -96.178  36.658  1.00 112.59 ? 211 SER   E OG  1 
ATOM   9118  N  N   . ILE   E  5  213 ? -13.115 -96.515  39.028  1.00 120.00 ? 212 ILE   E N   1 
ATOM   9119  C  CA  . ILE   E  5  213 ? -13.397 -97.118  40.364  1.00 120.64 ? 212 ILE   E CA  1 
ATOM   9120  C  C   . ILE   E  5  213 ? -12.793 -98.524  40.394  1.00 116.37 ? 212 ILE   E C   1 
ATOM   9121  O  O   . ILE   E  5  213 ? -12.925 -99.247  39.388  1.00 120.65 ? 212 ILE   E O   1 
ATOM   9122  C  CB  . ILE   E  5  213 ? -14.912 -97.135  40.656  1.00 125.93 ? 212 ILE   E CB  1 
ATOM   9123  C  CG1 . ILE   E  5  213 ? -15.518 -95.730  40.591  1.00 130.24 ? 212 ILE   E CG1 1 
ATOM   9124  C  CG2 . ILE   E  5  213 ? -15.203 -97.806  41.993  1.00 126.38 ? 212 ILE   E CG2 1 
ATOM   9125  C  CD1 . ILE   E  5  213 ? -17.014 -95.716  40.385  1.00 132.78 ? 212 ILE   E CD1 1 
ATOM   9126  N  N   . ALA   E  5  214 ? -12.151 -98.883  41.508  1.00 111.87 ? 213 ALA   E N   1 
ATOM   9127  C  CA  . ALA   E  5  214 ? -11.653 -100.246 41.801  1.00 110.98 ? 213 ALA   E CA  1 
ATOM   9128  C  C   . ALA   E  5  214 ? -12.189 -100.682 43.165  1.00 113.18 ? 213 ALA   E C   1 
ATOM   9129  O  O   . ALA   E  5  214 ? -12.407 -99.802  44.021  1.00 115.51 ? 213 ALA   E O   1 
ATOM   9130  C  CB  . ALA   E  5  214 ? -10.148 -100.273 41.767  1.00 107.37 ? 213 ALA   E CB  1 
ATOM   9131  N  N   . ILE   E  5  215 ? -12.404 -101.987 43.346  1.00 116.17 ? 214 ILE   E N   1 
ATOM   9132  C  CA  . ILE   E  5  215 ? -12.894 -102.579 44.625  1.00 116.32 ? 214 ILE   E CA  1 
ATOM   9133  C  C   . ILE   E  5  215 ? -12.241 -103.948 44.843  1.00 116.21 ? 214 ILE   E C   1 
ATOM   9134  O  O   . ILE   E  5  215 ? -12.056 -104.694 43.860  1.00 115.52 ? 214 ILE   E O   1 
ATOM   9135  C  CB  . ILE   E  5  215 ? -14.433 -102.670 44.653  1.00 118.06 ? 214 ILE   E CB  1 
ATOM   9136  C  CG1 . ILE   E  5  215 ? -14.927 -103.170 46.014  1.00 119.41 ? 214 ILE   E CG1 1 
ATOM   9137  C  CG2 . ILE   E  5  215 ? -14.958 -103.529 43.510  1.00 117.34 ? 214 ILE   E CG2 1 
ATOM   9138  C  CD1 . ILE   E  5  215 ? -16.381 -102.879 46.288  1.00 120.00 ? 214 ILE   E CD1 1 
ATOM   9139  N  N   . VAL   E  5  216 ? -11.911 -104.241 46.102  1.00 114.46 ? 215 VAL   E N   1 
ATOM   9140  C  CA  . VAL   E  5  216 ? -11.475 -105.578 46.596  1.00 111.83 ? 215 VAL   E CA  1 
ATOM   9141  C  C   . VAL   E  5  216 ? -12.131 -105.788 47.964  1.00 114.06 ? 215 VAL   E C   1 
ATOM   9142  O  O   . VAL   E  5  216 ? -12.408 -104.779 48.642  1.00 111.45 ? 215 VAL   E O   1 
ATOM   9143  C  CB  . VAL   E  5  216 ? -9.938  -105.677 46.664  1.00 109.12 ? 215 VAL   E CB  1 
ATOM   9144  C  CG1 . VAL   E  5  216 ? -9.351  -104.784 47.747  1.00 107.23 ? 215 VAL   E CG1 1 
ATOM   9145  C  CG2 . VAL   E  5  216 ? -9.473  -107.113 46.841  1.00 108.34 ? 215 VAL   E CG2 1 
ATOM   9146  N  N   . GLY   E  5  217 ? -12.394 -107.040 48.344  1.00 115.97 ? 216 GLY   E N   1 
ATOM   9147  C  CA  . GLY   E  5  217 ? -13.020 -107.359 49.640  1.00 119.65 ? 216 GLY   E CA  1 
ATOM   9148  C  C   . GLY   E  5  217 ? -13.197 -108.850 49.868  1.00 122.20 ? 216 GLY   E C   1 
ATOM   9149  O  O   . GLY   E  5  217 ? -12.604 -109.651 49.115  1.00 121.39 ? 216 GLY   E O   1 
ATOM   9150  N  N   . LYS   E  5  218 ? -14.010 -109.193 50.871  1.00 124.86 ? 217 LYS   E N   1 
ATOM   9151  C  CA  . LYS   E  5  218 ? -14.146 -110.555 51.452  1.00 128.28 ? 217 LYS   E CA  1 
ATOM   9152  C  C   . LYS   E  5  218 ? -14.458 -111.574 50.350  1.00 131.64 ? 217 LYS   E C   1 
ATOM   9153  O  O   . LYS   E  5  218 ? -13.735 -112.586 50.264  1.00 136.31 ? 217 LYS   E O   1 
ATOM   9154  C  CB  . LYS   E  5  218 ? -15.230 -110.566 52.533  1.00 131.50 ? 217 LYS   E CB  1 
ATOM   9155  C  CG  . LYS   E  5  218 ? -15.182 -111.777 53.451  1.00 132.34 ? 217 LYS   E CG  1 
ATOM   9156  C  CD  . LYS   E  5  218 ? -16.394 -111.933 54.331  1.00 136.22 ? 217 LYS   E CD  1 
ATOM   9157  C  CE  . LYS   E  5  218 ? -16.237 -113.079 55.306  1.00 137.89 ? 217 LYS   E CE  1 
ATOM   9158  N  NZ  . LYS   E  5  218 ? -17.523 -113.428 55.950  1.00 143.34 ? 217 LYS   E NZ  1 
ATOM   9159  N  N   . ASP   E  5  219 ? -15.498 -111.322 49.552  1.00 134.18 ? 218 ASP   E N   1 
ATOM   9160  C  CA  . ASP   E  5  219 ? -15.931 -112.209 48.439  1.00 139.69 ? 218 ASP   E CA  1 
ATOM   9161  C  C   . ASP   E  5  219 ? -15.935 -111.400 47.139  1.00 136.90 ? 218 ASP   E C   1 
ATOM   9162  O  O   . ASP   E  5  219 ? -16.955 -111.431 46.419  1.00 143.38 ? 218 ASP   E O   1 
ATOM   9163  C  CB  . ASP   E  5  219 ? -17.291 -112.845 48.743  1.00 146.04 ? 218 ASP   E CB  1 
ATOM   9164  C  CG  . ASP   E  5  219 ? -17.243 -113.911 49.827  1.00 150.90 ? 218 ASP   E CG  1 
ATOM   9165  O  OD1 . ASP   E  5  219 ? -16.207 -114.602 49.931  1.00 148.26 ? 218 ASP   E OD1 1 
ATOM   9166  O  OD2 . ASP   E  5  219 ? -18.244 -114.043 50.559  1.00 157.07 ? 218 ASP   E OD2 1 
ATOM   9167  N  N   . THR   E  5  220 ? -14.831 -110.700 46.857  1.00 126.74 ? 219 THR   E N   1 
ATOM   9168  C  CA  . THR   E  5  220 ? -14.645 -109.875 45.634  1.00 125.60 ? 219 THR   E CA  1 
ATOM   9169  C  C   . THR   E  5  220 ? -13.158 -109.784 45.302  1.00 116.85 ? 219 THR   E C   1 
ATOM   9170  O  O   . THR   E  5  220 ? -12.396 -109.177 46.050  1.00 118.64 ? 219 THR   E O   1 
ATOM   9171  C  CB  . THR   E  5  220 ? -15.252 -108.475 45.799  1.00 131.07 ? 219 THR   E CB  1 
ATOM   9172  O  OG1 . THR   E  5  220 ? -16.442 -108.571 46.583  1.00 138.91 ? 219 THR   E OG1 1 
ATOM   9173  C  CG2 . THR   E  5  220 ? -15.576 -107.827 44.471  1.00 133.14 ? 219 THR   E CG2 1 
ATOM   9174  N  N   . PRO   E  5  221 ? -12.695 -110.392 44.185  1.00 112.37 ? 220 PRO   E N   1 
ATOM   9175  C  CA  . PRO   E  5  221 ? -11.334 -110.167 43.694  1.00 113.10 ? 220 PRO   E CA  1 
ATOM   9176  C  C   . PRO   E  5  221 ? -11.140 -108.710 43.249  1.00 112.81 ? 220 PRO   E C   1 
ATOM   9177  O  O   . PRO   E  5  221 ? -12.110 -108.102 42.821  1.00 115.73 ? 220 PRO   E O   1 
ATOM   9178  C  CB  . PRO   E  5  221 ? -11.200 -111.110 42.487  1.00 110.09 ? 220 PRO   E CB  1 
ATOM   9179  C  CG  . PRO   E  5  221 ? -12.332 -112.105 42.647  1.00 112.41 ? 220 PRO   E CG  1 
ATOM   9180  C  CD  . PRO   E  5  221 ? -13.438 -111.344 43.348  1.00 112.60 ? 220 PRO   E CD  1 
ATOM   9181  N  N   . PHE   E  5  222 ? -9.914  -108.186 43.353  1.00 114.75 ? 221 PHE   E N   1 
ATOM   9182  C  CA  . PHE   E  5  222 ? -9.560  -106.819 42.887  1.00 115.16 ? 221 PHE   E CA  1 
ATOM   9183  C  C   . PHE   E  5  222 ? -9.998  -106.682 41.426  1.00 113.50 ? 221 PHE   E C   1 
ATOM   9184  O  O   . PHE   E  5  222 ? -9.415  -107.353 40.554  1.00 111.70 ? 221 PHE   E O   1 
ATOM   9185  C  CB  . PHE   E  5  222 ? -8.066  -106.519 43.040  1.00 115.03 ? 221 PHE   E CB  1 
ATOM   9186  C  CG  . PHE   E  5  222 ? -7.689  -105.102 42.681  1.00 116.41 ? 221 PHE   E CG  1 
ATOM   9187  C  CD1 . PHE   E  5  222 ? -7.456  -104.739 41.361  1.00 115.31 ? 221 PHE   E CD1 1 
ATOM   9188  C  CD2 . PHE   E  5  222 ? -7.589  -104.124 43.659  1.00 115.36 ? 221 PHE   E CD2 1 
ATOM   9189  C  CE1 . PHE   E  5  222 ? -7.121  -103.434 41.031  1.00 114.53 ? 221 PHE   E CE1 1 
ATOM   9190  C  CE2 . PHE   E  5  222 ? -7.254  -102.819 43.328  1.00 114.70 ? 221 PHE   E CE2 1 
ATOM   9191  C  CZ  . PHE   E  5  222 ? -7.021  -102.477 42.015  1.00 115.42 ? 221 PHE   E CZ  1 
ATOM   9192  N  N   . THR   E  5  223 ? -11.011 -105.852 41.176  1.00 114.85 ? 222 THR   E N   1 
ATOM   9193  C  CA  . THR   E  5  223 ? -11.584 -105.608 39.826  1.00 116.88 ? 222 THR   E CA  1 
ATOM   9194  C  C   . THR   E  5  223 ? -11.740 -104.100 39.599  1.00 115.29 ? 222 THR   E C   1 
ATOM   9195  O  O   . THR   E  5  223 ? -12.058 -103.380 40.569  1.00 113.39 ? 222 THR   E O   1 
ATOM   9196  C  CB  . THR   E  5  223 ? -12.903 -106.367 39.646  1.00 121.60 ? 222 THR   E CB  1 
ATOM   9197  O  OG1 . THR   E  5  223 ? -13.693 -106.193 40.823  1.00 126.58 ? 222 THR   E OG1 1 
ATOM   9198  C  CG2 . THR   E  5  223 ? -12.692 -107.843 39.391  1.00 121.18 ? 222 THR   E CG2 1 
ATOM   9199  N  N   . ILE   E  5  224 ? -11.518 -103.658 38.358  1.00 111.86 ? 223 ILE   E N   1 
ATOM   9200  C  CA  . ILE   E  5  224 ? -11.553 -102.226 37.937  1.00 112.48 ? 223 ILE   E CA  1 
ATOM   9201  C  C   . ILE   E  5  224 ? -12.789 -102.000 37.062  1.00 111.70 ? 223 ILE   E C   1 
ATOM   9202  O  O   . ILE   E  5  224 ? -13.078 -102.860 36.210  1.00 113.16 ? 223 ILE   E O   1 
ATOM   9203  C  CB  . ILE   E  5  224 ? -10.257 -101.841 37.196  1.00 110.67 ? 223 ILE   E CB  1 
ATOM   9204  C  CG1 . ILE   E  5  224 ? -9.007  -102.250 37.980  1.00 107.38 ? 223 ILE   E CG1 1 
ATOM   9205  C  CG2 . ILE   E  5  224 ? -10.259 -100.354 36.870  1.00 115.06 ? 223 ILE   E CG2 1 
ATOM   9206  C  CD1 . ILE   E  5  224 ? -7.727  -102.196 37.177  1.00 105.79 ? 223 ILE   E CD1 1 
ATOM   9207  N  N   . TYR   E  5  225 ? -13.471 -100.871 37.262  1.00 113.11 ? 224 TYR   E N   1 
ATOM   9208  C  CA  . TYR   E  5  225 ? -14.663 -100.444 36.485  1.00 121.69 ? 224 TYR   E CA  1 
ATOM   9209  C  C   . TYR   E  5  225 ? -14.350 -99.144  35.738  1.00 125.45 ? 224 TYR   E C   1 
ATOM   9210  O  O   . TYR   E  5  225 ? -13.994 -98.138  36.389  1.00 123.37 ? 224 TYR   E O   1 
ATOM   9211  C  CB  . TYR   E  5  225 ? -15.871 -100.272 37.405  1.00 122.14 ? 224 TYR   E CB  1 
ATOM   9212  C  CG  . TYR   E  5  225 ? -16.277 -101.528 38.130  1.00 123.68 ? 224 TYR   E CG  1 
ATOM   9213  C  CD1 . TYR   E  5  225 ? -16.654 -102.663 37.431  1.00 124.39 ? 224 TYR   E CD1 1 
ATOM   9214  C  CD2 . TYR   E  5  225 ? -16.285 -101.584 39.514  1.00 125.72 ? 224 TYR   E CD2 1 
ATOM   9215  C  CE1 . TYR   E  5  225 ? -17.027 -103.824 38.087  1.00 126.37 ? 224 TYR   E CE1 1 
ATOM   9216  C  CE2 . TYR   E  5  225 ? -16.656 -102.737 40.186  1.00 127.82 ? 224 TYR   E CE2 1 
ATOM   9217  C  CZ  . TYR   E  5  225 ? -17.028 -103.861 39.470  1.00 128.00 ? 224 TYR   E CZ  1 
ATOM   9218  O  OH  . TYR   E  5  225 ? -17.395 -105.002 40.121  1.00 131.25 ? 224 TYR   E OH  1 
ATOM   9219  N  N   . ASP   E  5  226 ? -14.479 -99.184  34.408  1.00 128.31 ? 225 ASP   E N   1 
ATOM   9220  C  CA  . ASP   E  5  226 ? -14.343 -98.022  33.491  1.00 128.97 ? 225 ASP   E CA  1 
ATOM   9221  C  C   . ASP   E  5  226 ? -15.577 -97.970  32.586  1.00 127.40 ? 225 ASP   E C   1 
ATOM   9222  O  O   . ASP   E  5  226 ? -16.406 -98.900  32.663  1.00 127.14 ? 225 ASP   E O   1 
ATOM   9223  C  CB  . ASP   E  5  226 ? -13.064 -98.121  32.657  1.00 133.04 ? 225 ASP   E CB  1 
ATOM   9224  C  CG  . ASP   E  5  226 ? -11.788 -98.008  33.476  1.00 133.59 ? 225 ASP   E CG  1 
ATOM   9225  O  OD1 . ASP   E  5  226 ? -11.672 -97.038  34.253  1.00 130.40 ? 225 ASP   E OD1 1 
ATOM   9226  O  OD2 . ASP   E  5  226 ? -10.924 -98.895  33.335  1.00 142.45 ? 225 ASP   E OD2 1 
ATOM   9227  N  N   . GLY   E  5  227 ? -15.684 -96.920  31.768  1.00 126.36 ? 226 GLY   E N   1 
ATOM   9228  C  CA  . GLY   E  5  227 ? -16.743 -96.755  30.755  1.00 125.27 ? 226 GLY   E CA  1 
ATOM   9229  C  C   . GLY   E  5  227 ? -18.133 -96.934  31.343  1.00 123.40 ? 226 GLY   E C   1 
ATOM   9230  O  O   . GLY   E  5  227 ? -18.386 -96.405  32.438  1.00 116.37 ? 226 GLY   E O   1 
ATOM   9231  N  N   . GLU   E  5  228 ? -18.993 -97.692  30.659  1.00 126.44 ? 227 GLU   E N   1 
ATOM   9232  C  CA  . GLU   E  5  228 ? -20.453 -97.767  30.943  1.00 132.41 ? 227 GLU   E CA  1 
ATOM   9233  C  C   . GLU   E  5  228 ? -20.713 -98.428  32.305  1.00 133.63 ? 227 GLU   E C   1 
ATOM   9234  O  O   . GLU   E  5  228 ? -21.844 -98.285  32.810  1.00 133.58 ? 227 GLU   E O   1 
ATOM   9235  C  CB  . GLU   E  5  228 ? -21.176 -98.522  29.824  1.00 137.83 ? 227 GLU   E CB  1 
ATOM   9236  C  CG  . GLU   E  5  228 ? -22.586 -98.018  29.576  1.00 141.23 ? 227 GLU   E CG  1 
ATOM   9237  C  CD  . GLU   E  5  228 ? -22.669 -96.560  29.158  1.00 144.39 ? 227 GLU   E CD  1 
ATOM   9238  O  OE1 . GLU   E  5  228 ? -21.823 -96.128  28.347  1.00 142.43 ? 227 GLU   E OE1 1 
ATOM   9239  O  OE2 . GLU   E  5  228 ? -23.570 -95.855  29.655  1.00 148.37 ? 227 GLU   E OE2 1 
ATOM   9240  N  N   . ALA   E  5  229 ? -19.720 -99.115  32.879  1.00 131.52 ? 228 ALA   E N   1 
ATOM   9241  C  CA  . ALA   E  5  229 ? -19.834 -99.832  34.171  1.00 131.84 ? 228 ALA   E CA  1 
ATOM   9242  C  C   . ALA   E  5  229 ? -19.819 -98.849  35.353  1.00 136.50 ? 228 ALA   E C   1 
ATOM   9243  O  O   . ALA   E  5  229 ? -20.189 -99.290  36.460  1.00 145.61 ? 228 ALA   E O   1 
ATOM   9244  C  CB  . ALA   E  5  229 ? -18.735 -100.859 34.298  1.00 125.76 ? 228 ALA   E CB  1 
ATOM   9245  N  N   . VAL   E  5  230 ? -19.412 -97.586  35.149  1.00 138.22 ? 229 VAL   E N   1 
ATOM   9246  C  CA  . VAL   E  5  230 ? -19.385 -96.541  36.222  1.00 134.67 ? 229 VAL   E CA  1 
ATOM   9247  C  C   . VAL   E  5  230 ? -20.550 -95.557  36.044  1.00 132.28 ? 229 VAL   E C   1 
ATOM   9248  O  O   . VAL   E  5  230 ? -20.722 -94.707  36.940  1.00 128.19 ? 229 VAL   E O   1 
ATOM   9249  C  CB  . VAL   E  5  230 ? -18.034 -95.798  36.296  1.00 135.96 ? 229 VAL   E CB  1 
ATOM   9250  C  CG1 . VAL   E  5  230 ? -16.872 -96.755  36.512  1.00 136.85 ? 229 VAL   E CG1 1 
ATOM   9251  C  CG2 . VAL   E  5  230 ? -17.778 -94.907  35.089  1.00 136.96 ? 229 VAL   E CG2 1 
ATOM   9252  N  N   . ALA   E  5  231 ? -21.320 -95.664  34.953  1.00 133.34 ? 230 ALA   E N   1 
ATOM   9253  C  CA  . ALA   E  5  231 ? -22.499 -94.810  34.661  1.00 136.41 ? 230 ALA   E CA  1 
ATOM   9254  C  C   . ALA   E  5  231 ? -23.481 -94.867  35.838  1.00 138.95 ? 230 ALA   E C   1 
ATOM   9255  O  O   . ALA   E  5  231 ? -24.120 -93.837  36.128  1.00 142.81 ? 230 ALA   E O   1 
ATOM   9256  C  CB  . ALA   E  5  231 ? -23.158 -95.246  33.376  1.00 135.13 ? 230 ALA   E CB  1 
ATOM   9257  N  N   . LYS   E  5  232 ? -23.576 -96.034  36.485  1.00 140.32 ? 231 LYS   E N   1 
ATOM   9258  C  CA  . LYS   E  5  232 ? -24.404 -96.308  37.692  1.00 144.62 ? 231 LYS   E CA  1 
ATOM   9259  C  C   . LYS   E  5  232 ? -24.155 -95.257  38.788  1.00 145.60 ? 231 LYS   E C   1 
ATOM   9260  O  O   . LYS   E  5  232 ? -25.107 -94.974  39.542  1.00 152.30 ? 231 LYS   E O   1 
ATOM   9261  C  CB  . LYS   E  5  232 ? -24.085 -97.718  38.205  1.00 144.01 ? 231 LYS   E CB  1 
ATOM   9262  C  CG  . LYS   E  5  232 ? -25.003 -98.262  39.293  1.00 145.12 ? 231 LYS   E CG  1 
ATOM   9263  C  CD  . LYS   E  5  232 ? -24.358 -99.334  40.158  1.00 144.06 ? 231 LYS   E CD  1 
ATOM   9264  C  CE  . LYS   E  5  232 ? -24.284 -100.700 39.504  1.00 142.88 ? 231 LYS   E CE  1 
ATOM   9265  N  NZ  . LYS   E  5  232 ? -23.113 -100.838 38.604  1.00 141.26 ? 231 LYS   E NZ  1 
ATOM   9266  N  N   . TYR   E  5  233 ? -22.940 -94.698  38.874  1.00 145.62 ? 232 TYR   E N   1 
ATOM   9267  C  CA  . TYR   E  5  233 ? -22.456 -93.890  40.029  1.00 144.34 ? 232 TYR   E CA  1 
ATOM   9268  C  C   . TYR   E  5  233 ? -22.368 -92.388  39.708  1.00 142.91 ? 232 TYR   E C   1 
ATOM   9269  O  O   . TYR   E  5  233 ? -21.772 -91.664  40.529  1.00 136.21 ? 232 TYR   E O   1 
ATOM   9270  C  CB  . TYR   E  5  233 ? -21.090 -94.409  40.486  1.00 142.62 ? 232 TYR   E CB  1 
ATOM   9271  C  CG  . TYR   E  5  233 ? -21.088 -95.852  40.922  1.00 142.02 ? 232 TYR   E CG  1 
ATOM   9272  C  CD1 . TYR   E  5  233 ? -21.574 -96.222  42.166  1.00 142.54 ? 232 TYR   E CD1 1 
ATOM   9273  C  CD2 . TYR   E  5  233 ? -20.601 -96.850  40.093  1.00 143.30 ? 232 TYR   E CD2 1 
ATOM   9274  C  CE1 . TYR   E  5  233 ? -21.575 -97.545  42.576  1.00 143.29 ? 232 TYR   E CE1 1 
ATOM   9275  C  CE2 . TYR   E  5  233 ? -20.596 -98.178  40.487  1.00 144.24 ? 232 TYR   E CE2 1 
ATOM   9276  C  CZ  . TYR   E  5  233 ? -21.084 -98.528  41.735  1.00 144.64 ? 232 TYR   E CZ  1 
ATOM   9277  O  OH  . TYR   E  5  233 ? -21.085 -99.835  42.131  1.00 144.41 ? 232 TYR   E OH  1 
ATOM   9278  N  N   . ILE   E  5  234 ? -22.936 -91.923  38.588  1.00 145.17 ? 233 ILE   E N   1 
ATOM   9279  C  CA  . ILE   E  5  234 ? -22.975 -90.471  38.220  1.00 149.33 ? 233 ILE   E CA  1 
ATOM   9280  C  C   . ILE   E  5  234 ? -24.402 -89.946  38.430  1.00 154.22 ? 233 ILE   E C   1 
ATOM   9281  O  O   . ILE   E  5  234 ? -25.373 -90.518  37.935  1.00 164.89 ? 233 ILE   E O   1 
ATOM   9282  C  CB  . ILE   E  5  234 ? -22.485 -90.230  36.776  1.00 147.90 ? 233 ILE   E CB  1 
ATOM   9283  C  CG1 . ILE   E  5  234 ? -21.112 -90.857  36.520  1.00 144.81 ? 233 ILE   E CG1 1 
ATOM   9284  C  CG2 . ILE   E  5  234 ? -22.485 -88.741  36.451  1.00 147.41 ? 233 ILE   E CG2 1 
ATOM   9285  C  CD1 . ILE   E  5  234 ? -20.806 -91.077  35.057  1.00 144.80 ? 233 ILE   E CD1 1 
ATOM   9286  O  OXT . ILE   E  5  234 ? -24.612 -88.932  39.098  1.00 151.53 ? 233 ILE   E OXT 1 
ATOM   9287  N  N   . THR   F  6  6   ? 34.361  -71.044  50.445  1.00 137.15 ? 2   THR   F N   1 
ATOM   9288  C  CA  . THR   F  6  6   ? 33.649  -72.148  51.169  1.00 135.83 ? 2   THR   F CA  1 
ATOM   9289  C  C   . THR   F  6  6   ? 33.121  -73.167  50.145  1.00 130.63 ? 2   THR   F C   1 
ATOM   9290  O  O   . THR   F  6  6   ? 33.830  -73.408  49.146  1.00 128.25 ? 2   THR   F O   1 
ATOM   9291  C  CB  . THR   F  6  6   ? 32.581  -71.573  52.112  1.00 141.22 ? 2   THR   F CB  1 
ATOM   9292  O  OG1 . THR   F  6  6   ? 31.780  -70.643  51.380  1.00 138.01 ? 2   THR   F OG1 1 
ATOM   9293  C  CG2 . THR   F  6  6   ? 33.180  -70.891  53.323  1.00 140.65 ? 2   THR   F CG2 1 
ATOM   9294  N  N   . GLY   F  6  7   ? 31.938  -73.745  50.384  1.00 127.25 ? 3   GLY   F N   1 
ATOM   9295  C  CA  . GLY   F  6  7   ? 31.387  -74.878  49.614  1.00 124.29 ? 3   GLY   F CA  1 
ATOM   9296  C  C   . GLY   F  6  7   ? 31.713  -76.215  50.264  1.00 124.22 ? 3   GLY   F C   1 
ATOM   9297  O  O   . GLY   F  6  7   ? 31.370  -77.260  49.667  1.00 126.57 ? 3   GLY   F O   1 
ATOM   9298  N  N   . TYR   F  6  8   ? 32.346  -76.187  51.445  1.00 117.42 ? 4   TYR   F N   1 
ATOM   9299  C  CA  . TYR   F  6  8   ? 32.787  -77.377  52.225  1.00 112.01 ? 4   TYR   F CA  1 
ATOM   9300  C  C   . TYR   F  6  8   ? 31.582  -78.220  52.666  1.00 111.61 ? 4   TYR   F C   1 
ATOM   9301  O  O   . TYR   F  6  8   ? 31.777  -79.416  52.981  1.00 106.51 ? 4   TYR   F O   1 
ATOM   9302  C  CB  . TYR   F  6  8   ? 33.597  -76.949  53.454  1.00 108.44 ? 4   TYR   F CB  1 
ATOM   9303  C  CG  . TYR   F  6  8   ? 34.935  -76.322  53.154  1.00 104.18 ? 4   TYR   F CG  1 
ATOM   9304  C  CD1 . TYR   F  6  8   ? 36.033  -77.105  52.836  1.00 104.25 ? 4   TYR   F CD1 1 
ATOM   9305  C  CD2 . TYR   F  6  8   ? 35.111  -74.948  53.196  1.00 103.68 ? 4   TYR   F CD2 1 
ATOM   9306  C  CE1 . TYR   F  6  8   ? 37.269  -76.541  52.561  1.00 101.27 ? 4   TYR   F CE1 1 
ATOM   9307  C  CE2 . TYR   F  6  8   ? 36.341  -74.368  52.925  1.00 102.42 ? 4   TYR   F CE2 1 
ATOM   9308  C  CZ  . TYR   F  6  8   ? 37.425  -75.168  52.607  1.00 101.33 ? 4   TYR   F CZ  1 
ATOM   9309  O  OH  . TYR   F  6  8   ? 38.648  -74.628  52.337  1.00 95.42  ? 4   TYR   F OH  1 
ATOM   9310  N  N   . ASP   F  6  9   ? 30.386  -77.618  52.703  1.00 102.88 ? 5   ASP   F N   1 
ATOM   9311  C  CA  . ASP   F  6  9   ? 29.136  -78.247  53.211  1.00 99.82  ? 5   ASP   F CA  1 
ATOM   9312  C  C   . ASP   F  6  9   ? 28.320  -78.868  52.066  1.00 101.14 ? 5   ASP   F C   1 
ATOM   9313  O  O   . ASP   F  6  9   ? 27.245  -79.424  52.364  1.00 107.12 ? 5   ASP   F O   1 
ATOM   9314  C  CB  . ASP   F  6  9   ? 28.282  -77.234  53.980  1.00 102.32 ? 5   ASP   F CB  1 
ATOM   9315  C  CG  . ASP   F  6  9   ? 27.618  -76.186  53.102  1.00 103.33 ? 5   ASP   F CG  1 
ATOM   9316  O  OD1 . ASP   F  6  9   ? 28.251  -75.756  52.118  1.00 111.13 ? 5   ASP   F OD1 1 
ATOM   9317  O  OD2 . ASP   F  6  9   ? 26.470  -75.810  53.409  1.00 104.11 ? 5   ASP   F OD2 1 
ATOM   9318  N  N   . LEU   F  6  10  ? 28.788  -78.783  50.816  1.00 96.16  ? 6   LEU   F N   1 
ATOM   9319  C  CA  . LEU   F  6  10  ? 28.018  -79.225  49.619  1.00 102.11 ? 6   LEU   F CA  1 
ATOM   9320  C  C   . LEU   F  6  10  ? 28.257  -80.713  49.332  1.00 102.09 ? 6   LEU   F C   1 
ATOM   9321  O  O   . LEU   F  6  10  ? 27.468  -81.294  48.555  1.00 106.75 ? 6   LEU   F O   1 
ATOM   9322  C  CB  . LEU   F  6  10  ? 28.421  -78.377  48.408  1.00 101.48 ? 6   LEU   F CB  1 
ATOM   9323  C  CG  . LEU   F  6  10  ? 28.057  -76.896  48.482  1.00 101.56 ? 6   LEU   F CG  1 
ATOM   9324  C  CD1 . LEU   F  6  10  ? 28.700  -76.135  47.334  1.00 102.84 ? 6   LEU   F CD1 1 
ATOM   9325  C  CD2 . LEU   F  6  10  ? 26.546  -76.698  48.475  1.00 103.92 ? 6   LEU   F CD2 1 
ATOM   9326  N  N   . SER   F  6  11  ? 29.299  -81.308  49.921  1.00 101.56 ? 7   SER   F N   1 
ATOM   9327  C  CA  . SER   F  6  11  ? 29.762  -82.686  49.614  1.00 97.94  ? 7   SER   F CA  1 
ATOM   9328  C  C   . SER   F  6  11  ? 30.045  -83.450  50.912  1.00 96.79  ? 7   SER   F C   1 
ATOM   9329  O  O   . SER   F  6  11  ? 30.743  -82.900  51.790  1.00 94.65  ? 7   SER   F O   1 
ATOM   9330  C  CB  . SER   F  6  11  ? 30.969  -82.640  48.713  1.00 97.13  ? 7   SER   F CB  1 
ATOM   9331  O  OG  . SER   F  6  11  ? 31.420  -83.946  48.393  1.00 95.70  ? 7   SER   F OG  1 
ATOM   9332  N  N   . ASN   F  6  12  ? 29.505  -84.667  51.023  1.00 92.07  ? 8   ASN   F N   1 
ATOM   9333  C  CA  . ASN   F  6  12  ? 29.742  -85.600  52.156  1.00 91.90  ? 8   ASN   F CA  1 
ATOM   9334  C  C   . ASN   F  6  12  ? 31.192  -86.095  52.094  1.00 90.82  ? 8   ASN   F C   1 
ATOM   9335  O  O   . ASN   F  6  12  ? 31.697  -86.298  50.973  1.00 89.81  ? 8   ASN   F O   1 
ATOM   9336  C  CB  . ASN   F  6  12  ? 28.749  -86.766  52.136  1.00 92.60  ? 8   ASN   F CB  1 
ATOM   9337  C  CG  . ASN   F  6  12  ? 28.884  -87.691  53.328  1.00 92.90  ? 8   ASN   F CG  1 
ATOM   9338  O  OD1 . ASN   F  6  12  ? 29.388  -87.296  54.376  1.00 94.02  ? 8   ASN   F OD1 1 
ATOM   9339  N  ND2 . ASN   F  6  12  ? 28.430  -88.926  53.182  1.00 94.86  ? 8   ASN   F ND2 1 
ATOM   9340  N  N   . SER   F  6  13  ? 31.830  -86.256  53.260  1.00 89.55  ? 9   SER   F N   1 
ATOM   9341  C  CA  . SER   F  6  13  ? 33.197  -86.818  53.449  1.00 91.03  ? 9   SER   F CA  1 
ATOM   9342  C  C   . SER   F  6  13  ? 34.271  -85.729  53.311  1.00 96.34  ? 9   SER   F C   1 
ATOM   9343  O  O   . SER   F  6  13  ? 35.459  -86.060  53.511  1.00 95.83  ? 9   SER   F O   1 
ATOM   9344  C  CB  . SER   F  6  13  ? 33.465  -87.964  52.500  1.00 93.22  ? 9   SER   F CB  1 
ATOM   9345  O  OG  . SER   F  6  13  ? 33.909  -87.486  51.236  1.00 87.28  ? 9   SER   F OG  1 
ATOM   9346  N  N   . VAL   F  6  14  ? 33.885  -84.491  52.978  1.00 97.26  ? 10  VAL   F N   1 
ATOM   9347  C  CA  . VAL   F  6  14  ? 34.818  -83.329  52.863  1.00 95.95  ? 10  VAL   F CA  1 
ATOM   9348  C  C   . VAL   F  6  14  ? 34.975  -82.694  54.248  1.00 94.96  ? 10  VAL   F C   1 
ATOM   9349  O  O   . VAL   F  6  14  ? 33.946  -82.288  54.837  1.00 91.66  ? 10  VAL   F O   1 
ATOM   9350  C  CB  . VAL   F  6  14  ? 34.336  -82.291  51.829  1.00 97.20  ? 10  VAL   F CB  1 
ATOM   9351  C  CG1 . VAL   F  6  14  ? 35.173  -81.021  51.874  1.00 99.70  ? 10  VAL   F CG1 1 
ATOM   9352  C  CG2 . VAL   F  6  14  ? 34.316  -82.860  50.418  1.00 97.07  ? 10  VAL   F CG2 1 
ATOM   9353  N  N   . PHE   F  6  15  ? 36.217  -82.605  54.732  1.00 91.55  ? 11  PHE   F N   1 
ATOM   9354  C  CA  . PHE   F  6  15  ? 36.595  -81.884  55.975  1.00 94.59  ? 11  PHE   F CA  1 
ATOM   9355  C  C   . PHE   F  6  15  ? 36.532  -80.378  55.720  1.00 96.19  ? 11  PHE   F C   1 
ATOM   9356  O  O   . PHE   F  6  15  ? 37.125  -79.908  54.729  1.00 104.15 ? 11  PHE   F O   1 
ATOM   9357  C  CB  . PHE   F  6  15  ? 38.003  -82.259  56.444  1.00 92.67  ? 11  PHE   F CB  1 
ATOM   9358  C  CG  . PHE   F  6  15  ? 38.115  -83.622  57.077  1.00 91.86  ? 11  PHE   F CG  1 
ATOM   9359  C  CD1 . PHE   F  6  15  ? 37.509  -83.888  58.295  1.00 91.83  ? 11  PHE   F CD1 1 
ATOM   9360  C  CD2 . PHE   F  6  15  ? 38.832  -84.637  56.460  1.00 91.51  ? 11  PHE   F CD2 1 
ATOM   9361  C  CE1 . PHE   F  6  15  ? 37.612  -85.142  58.879  1.00 90.91  ? 11  PHE   F CE1 1 
ATOM   9362  C  CE2 . PHE   F  6  15  ? 38.934  -85.889  57.046  1.00 90.85  ? 11  PHE   F CE2 1 
ATOM   9363  C  CZ  . PHE   F  6  15  ? 38.324  -86.139  58.253  1.00 89.73  ? 11  PHE   F CZ  1 
ATOM   9364  N  N   . SER   F  6  16  ? 35.840  -79.646  56.593  1.00 97.30  ? 12  SER   F N   1 
ATOM   9365  C  CA  . SER   F  6  16  ? 35.919  -78.167  56.689  1.00 96.42  ? 12  SER   F CA  1 
ATOM   9366  C  C   . SER   F  6  16  ? 37.270  -77.799  57.295  1.00 95.25  ? 12  SER   F C   1 
ATOM   9367  O  O   . SER   F  6  16  ? 37.950  -78.665  57.840  1.00 93.68  ? 12  SER   F O   1 
ATOM   9368  C  CB  . SER   F  6  16  ? 34.786  -77.623  57.509  1.00 97.17  ? 12  SER   F CB  1 
ATOM   9369  O  OG  . SER   F  6  16  ? 34.950  -77.971  58.875  1.00 95.94  ? 12  SER   F OG  1 
ATOM   9370  N  N   . PRO   F  6  17  ? 37.717  -76.525  57.217  1.00 96.55  ? 13  PRO   F N   1 
ATOM   9371  C  CA  . PRO   F  6  17  ? 38.933  -76.096  57.912  1.00 94.68  ? 13  PRO   F CA  1 
ATOM   9372  C  C   . PRO   F  6  17  ? 38.914  -76.326  59.433  1.00 92.21  ? 13  PRO   F C   1 
ATOM   9373  O  O   . PRO   F  6  17  ? 39.982  -76.400  60.006  1.00 86.52  ? 13  PRO   F O   1 
ATOM   9374  C  CB  . PRO   F  6  17  ? 39.016  -74.597  57.593  1.00 96.70  ? 13  PRO   F CB  1 
ATOM   9375  C  CG  . PRO   F  6  17  ? 38.288  -74.470  56.276  1.00 99.10  ? 13  PRO   F CG  1 
ATOM   9376  C  CD  . PRO   F  6  17  ? 37.142  -75.455  56.387  1.00 98.96  ? 13  PRO   F CD  1 
ATOM   9377  N  N   . ASP   F  6  18  ? 37.725  -76.432  60.037  1.00 97.08  ? 14  ASP   F N   1 
ATOM   9378  C  CA  . ASP   F  6  18  ? 37.540  -76.776  61.476  1.00 105.01 ? 14  ASP   F CA  1 
ATOM   9379  C  C   . ASP   F  6  18  ? 38.010  -78.216  61.730  1.00 104.11 ? 14  ASP   F C   1 
ATOM   9380  O  O   . ASP   F  6  18  ? 38.571  -78.476  62.815  1.00 104.45 ? 14  ASP   F O   1 
ATOM   9381  C  CB  . ASP   F  6  18  ? 36.077  -76.684  61.917  1.00 108.35 ? 14  ASP   F CB  1 
ATOM   9382  C  CG  . ASP   F  6  18  ? 35.320  -75.485  61.377  1.00 111.11 ? 14  ASP   F CG  1 
ATOM   9383  O  OD1 . ASP   F  6  18  ? 35.185  -74.499  62.124  1.00 119.24 ? 14  ASP   F OD1 1 
ATOM   9384  O  OD2 . ASP   F  6  18  ? 34.854  -75.558  60.222  1.00 119.36 ? 14  ASP   F OD2 1 
ATOM   9385  N  N   . GLY   F  6  19  ? 37.770  -79.108  60.763  1.00 104.49 ? 15  GLY   F N   1 
ATOM   9386  C  CA  . GLY   F  6  19  ? 37.920  -80.569  60.902  1.00 101.54 ? 15  GLY   F CA  1 
ATOM   9387  C  C   . GLY   F  6  19  ? 36.569  -81.243  61.065  1.00 103.35 ? 15  GLY   F C   1 
ATOM   9388  O  O   . GLY   F  6  19  ? 36.529  -82.325  61.680  1.00 105.98 ? 15  GLY   F O   1 
ATOM   9389  N  N   . ARG   F  6  20  ? 35.507  -80.633  60.525  1.00 99.99  ? 16  ARG   F N   1 
ATOM   9390  C  CA  . ARG   F  6  20  ? 34.100  -81.100  60.652  1.00 101.43 ? 16  ARG   F CA  1 
ATOM   9391  C  C   . ARG   F  6  20  ? 33.556  -81.553  59.293  1.00 104.09 ? 16  ARG   F C   1 
ATOM   9392  O  O   . ARG   F  6  20  ? 34.024  -81.040  58.251  1.00 103.67 ? 16  ARG   F O   1 
ATOM   9393  C  CB  . ARG   F  6  20  ? 33.211  -79.980  61.195  1.00 100.93 ? 16  ARG   F CB  1 
ATOM   9394  C  CG  . ARG   F  6  20  ? 33.423  -79.678  62.671  1.00 103.17 ? 16  ARG   F CG  1 
ATOM   9395  C  CD  . ARG   F  6  20  ? 33.104  -78.234  63.010  1.00 101.97 ? 16  ARG   F CD  1 
ATOM   9396  N  NE  . ARG   F  6  20  ? 31.708  -77.890  62.782  1.00 102.32 ? 16  ARG   F NE  1 
ATOM   9397  C  CZ  . ARG   F  6  20  ? 31.232  -76.650  62.699  1.00 103.38 ? 16  ARG   F CZ  1 
ATOM   9398  N  NH1 . ARG   F  6  20  ? 32.039  -75.607  62.823  1.00 107.22 ? 16  ARG   F NH1 1 
ATOM   9399  N  NH2 . ARG   F  6  20  ? 29.943  -76.454  62.486  1.00 107.49 ? 16  ARG   F NH2 1 
ATOM   9400  N  N   . ASN   F  6  21  ? 32.579  -82.462  59.327  1.00 104.78 ? 17  ASN   F N   1 
ATOM   9401  C  CA  . ASN   F  6  21  ? 31.839  -82.978  58.145  1.00 106.23 ? 17  ASN   F CA  1 
ATOM   9402  C  C   . ASN   F  6  21  ? 30.426  -82.391  58.192  1.00 99.29  ? 17  ASN   F C   1 
ATOM   9403  O  O   . ASN   F  6  21  ? 29.534  -83.031  58.783  1.00 100.02 ? 17  ASN   F O   1 
ATOM   9404  C  CB  . ASN   F  6  21  ? 31.844  -84.509  58.114  1.00 105.61 ? 17  ASN   F CB  1 
ATOM   9405  C  CG  . ASN   F  6  21  ? 31.222  -85.087  56.861  1.00 111.18 ? 17  ASN   F CG  1 
ATOM   9406  O  OD1 . ASN   F  6  21  ? 30.816  -84.354  55.960  1.00 111.88 ? 17  ASN   F OD1 1 
ATOM   9407  N  ND2 . ASN   F  6  21  ? 31.148  -86.406  56.797  1.00 114.56 ? 17  ASN   F ND2 1 
ATOM   9408  N  N   . PHE   F  6  22  ? 30.241  -81.210  57.601  1.00 96.94  ? 18  PHE   F N   1 
ATOM   9409  C  CA  . PHE   F  6  22  ? 28.998  -80.403  57.719  1.00 97.32  ? 18  PHE   F CA  1 
ATOM   9410  C  C   . PHE   F  6  22  ? 27.782  -81.248  57.321  1.00 94.46  ? 18  PHE   F C   1 
ATOM   9411  O  O   . PHE   F  6  22  ? 26.721  -81.102  57.960  1.00 94.66  ? 18  PHE   F O   1 
ATOM   9412  C  CB  . PHE   F  6  22  ? 29.111  -79.108  56.908  1.00 99.46  ? 18  PHE   F CB  1 
ATOM   9413  C  CG  . PHE   F  6  22  ? 29.669  -77.945  57.691  1.00 96.57  ? 18  PHE   F CG  1 
ATOM   9414  C  CD1 . PHE   F  6  22  ? 28.835  -76.954  58.185  1.00 95.77  ? 18  PHE   F CD1 1 
ATOM   9415  C  CD2 . PHE   F  6  22  ? 31.026  -77.860  57.965  1.00 97.71  ? 18  PHE   F CD2 1 
ATOM   9416  C  CE1 . PHE   F  6  22  ? 29.348  -75.895  58.916  1.00 95.94  ? 18  PHE   F CE1 1 
ATOM   9417  C  CE2 . PHE   F  6  22  ? 31.537  -76.801  58.698  1.00 94.50  ? 18  PHE   F CE2 1 
ATOM   9418  C  CZ  . PHE   F  6  22  ? 30.698  -75.821  59.172  1.00 95.89  ? 18  PHE   F CZ  1 
ATOM   9419  N  N   . GLN   F  6  23  ? 27.931  -82.116  56.316  1.00 93.63  ? 19  GLN   F N   1 
ATOM   9420  C  CA  . GLN   F  6  23  ? 26.820  -82.943  55.773  1.00 93.07  ? 19  GLN   F CA  1 
ATOM   9421  C  C   . GLN   F  6  23  ? 26.232  -83.836  56.875  1.00 92.25  ? 19  GLN   F C   1 
ATOM   9422  O  O   . GLN   F  6  23  ? 24.997  -84.028  56.876  1.00 87.83  ? 19  GLN   F O   1 
ATOM   9423  C  CB  . GLN   F  6  23  ? 27.308  -83.750  54.570  1.00 97.27  ? 19  GLN   F CB  1 
ATOM   9424  C  CG  . GLN   F  6  23  ? 27.093  -83.028  53.246  1.00 98.03  ? 19  GLN   F CG  1 
ATOM   9425  C  CD  . GLN   F  6  23  ? 25.632  -82.975  52.865  1.00 94.82  ? 19  GLN   F CD  1 
ATOM   9426  O  OE1 . GLN   F  6  23  ? 25.081  -81.916  52.572  1.00 90.78  ? 19  GLN   F OE1 1 
ATOM   9427  N  NE2 . GLN   F  6  23  ? 24.989  -84.132  52.877  1.00 98.71  ? 19  GLN   F NE2 1 
ATOM   9428  N  N   . VAL   F  6  24  ? 27.073  -84.358  57.774  1.00 89.56  ? 20  VAL   F N   1 
ATOM   9429  C  CA  . VAL   F  6  24  ? 26.638  -85.170  58.952  1.00 90.92  ? 20  VAL   F CA  1 
ATOM   9430  C  C   . VAL   F  6  24  ? 25.866  -84.255  59.910  1.00 91.46  ? 20  VAL   F C   1 
ATOM   9431  O  O   . VAL   F  6  24  ? 24.750  -84.624  60.320  1.00 93.53  ? 20  VAL   F O   1 
ATOM   9432  C  CB  . VAL   F  6  24  ? 27.832  -85.842  59.658  1.00 92.43  ? 20  VAL   F CB  1 
ATOM   9433  C  CG1 . VAL   F  6  24  ? 27.425  -86.481  60.977  1.00 95.32  ? 20  VAL   F CG1 1 
ATOM   9434  C  CG2 . VAL   F  6  24  ? 28.511  -86.866  58.762  1.00 92.23  ? 20  VAL   F CG2 1 
ATOM   9435  N  N   . GLU   F  6  25  ? 26.448  -83.101  60.243  1.00 94.95  ? 21  GLU   F N   1 
ATOM   9436  C  CA  . GLU   F  6  25  ? 25.831  -82.068  61.118  1.00 95.17  ? 21  GLU   F CA  1 
ATOM   9437  C  C   . GLU   F  6  25  ? 24.463  -81.662  60.552  1.00 92.00  ? 21  GLU   F C   1 
ATOM   9438  O  O   . GLU   F  6  25  ? 23.558  -81.373  61.353  1.00 92.61  ? 21  GLU   F O   1 
ATOM   9439  C  CB  . GLU   F  6  25  ? 26.760  -80.861  61.255  1.00 95.74  ? 21  GLU   F CB  1 
ATOM   9440  C  CG  . GLU   F  6  25  ? 27.986  -81.135  62.107  1.00 103.74 ? 21  GLU   F CG  1 
ATOM   9441  C  CD  . GLU   F  6  25  ? 28.909  -79.945  62.319  1.00 109.52 ? 21  GLU   F CD  1 
ATOM   9442  O  OE1 . GLU   F  6  25  ? 28.430  -78.792  62.242  1.00 112.77 ? 21  GLU   F OE1 1 
ATOM   9443  O  OE2 . GLU   F  6  25  ? 30.110  -80.172  62.566  1.00 121.69 ? 21  GLU   F OE2 1 
ATOM   9444  N  N   . TYR   F  6  26  ? 24.320  -81.650  59.223  1.00 94.34  ? 22  TYR   F N   1 
ATOM   9445  C  CA  . TYR   F  6  26  ? 23.056  -81.322  58.512  1.00 97.99  ? 22  TYR   F CA  1 
ATOM   9446  C  C   . TYR   F  6  26  ? 22.058  -82.474  58.680  1.00 95.62  ? 22  TYR   F C   1 
ATOM   9447  O  O   . TYR   F  6  26  ? 20.860  -82.195  58.866  1.00 100.87 ? 22  TYR   F O   1 
ATOM   9448  C  CB  . TYR   F  6  26  ? 23.332  -81.011  57.037  1.00 101.73 ? 22  TYR   F CB  1 
ATOM   9449  C  CG  . TYR   F  6  26  ? 23.978  -79.674  56.759  1.00 103.80 ? 22  TYR   F CG  1 
ATOM   9450  C  CD1 . TYR   F  6  26  ? 24.416  -78.843  57.781  1.00 102.86 ? 22  TYR   F CD1 1 
ATOM   9451  C  CD2 . TYR   F  6  26  ? 24.178  -79.249  55.455  1.00 106.72 ? 22  TYR   F CD2 1 
ATOM   9452  C  CE1 . TYR   F  6  26  ? 25.013  -77.621  57.516  1.00 104.20 ? 22  TYR   F CE1 1 
ATOM   9453  C  CE2 . TYR   F  6  26  ? 24.776  -78.031  55.172  1.00 105.50 ? 22  TYR   F CE2 1 
ATOM   9454  C  CZ  . TYR   F  6  26  ? 25.196  -77.214  56.206  1.00 105.11 ? 22  TYR   F CZ  1 
ATOM   9455  O  OH  . TYR   F  6  26  ? 25.785  -76.014  55.936  1.00 106.57 ? 22  TYR   F OH  1 
ATOM   9456  N  N   . ALA   F  6  27  ? 22.527  -83.725  58.620  1.00 94.30  ? 23  ALA   F N   1 
ATOM   9457  C  CA  . ALA   F  6  27  ? 21.700  -84.926  58.882  1.00 92.90  ? 23  ALA   F CA  1 
ATOM   9458  C  C   . ALA   F  6  27  ? 21.154  -84.854  60.313  1.00 90.58  ? 23  ALA   F C   1 
ATOM   9459  O  O   . ALA   F  6  27  ? 19.977  -85.206  60.514  1.00 87.53  ? 23  ALA   F O   1 
ATOM   9460  C  CB  . ALA   F  6  27  ? 22.499  -86.186  58.650  1.00 95.32  ? 23  ALA   F CB  1 
ATOM   9461  N  N   . VAL   F  6  28  ? 21.973  -84.391  61.263  1.00 88.09  ? 24  VAL   F N   1 
ATOM   9462  C  CA  . VAL   F  6  28  ? 21.592  -84.250  62.700  1.00 90.28  ? 24  VAL   F CA  1 
ATOM   9463  C  C   . VAL   F  6  28  ? 20.373  -83.323  62.798  1.00 93.17  ? 24  VAL   F C   1 
ATOM   9464  O  O   . VAL   F  6  28  ? 19.509  -83.587  63.654  1.00 93.43  ? 24  VAL   F O   1 
ATOM   9465  C  CB  . VAL   F  6  28  ? 22.773  -83.753  63.558  1.00 90.32  ? 24  VAL   F CB  1 
ATOM   9466  C  CG1 . VAL   F  6  28  ? 22.337  -83.339  64.956  1.00 92.42  ? 24  VAL   F CG1 1 
ATOM   9467  C  CG2 . VAL   F  6  28  ? 23.882  -84.791  63.639  1.00 88.04  ? 24  VAL   F CG2 1 
ATOM   9468  N  N   . LYS   F  6  29  ? 20.299  -82.290  61.952  1.00 98.65  ? 25  LYS   F N   1 
ATOM   9469  C  CA  . LYS   F  6  29  ? 19.163  -81.327  61.920  1.00 103.74 ? 25  LYS   F CA  1 
ATOM   9470  C  C   . LYS   F  6  29  ? 17.872  -82.083  61.574  1.00 100.86 ? 25  LYS   F C   1 
ATOM   9471  O  O   . LYS   F  6  29  ? 16.831  -81.771  62.181  1.00 102.07 ? 25  LYS   F O   1 
ATOM   9472  C  CB  . LYS   F  6  29  ? 19.427  -80.183  60.933  1.00 107.76 ? 25  LYS   F CB  1 
ATOM   9473  C  CG  . LYS   F  6  29  ? 20.544  -79.223  61.324  1.00 109.86 ? 25  LYS   F CG  1 
ATOM   9474  C  CD  . LYS   F  6  29  ? 20.205  -78.334  62.501  1.00 114.61 ? 25  LYS   F CD  1 
ATOM   9475  C  CE  . LYS   F  6  29  ? 21.199  -77.209  62.691  1.00 117.56 ? 25  LYS   F CE  1 
ATOM   9476  N  NZ  . LYS   F  6  29  ? 20.910  -76.422  63.914  1.00 123.59 ? 25  LYS   F NZ  1 
ATOM   9477  N  N   . ALA   F  6  30  ? 17.943  -83.046  60.648  1.00 101.08 ? 26  ALA   F N   1 
ATOM   9478  C  CA  . ALA   F  6  30  ? 16.801  -83.896  60.232  1.00 103.66 ? 26  ALA   F CA  1 
ATOM   9479  C  C   . ALA   F  6  30  ? 16.319  -84.736  61.422  1.00 103.33 ? 26  ALA   F C   1 
ATOM   9480  O  O   . ALA   F  6  30  ? 15.098  -84.969  61.526  1.00 103.00 ? 26  ALA   F O   1 
ATOM   9481  C  CB  . ALA   F  6  30  ? 17.188  -84.770  59.062  1.00 103.93 ? 26  ALA   F CB  1 
ATOM   9482  N  N   . VAL   F  6  31  ? 17.244  -85.169  62.285  1.00 103.42 ? 27  VAL   F N   1 
ATOM   9483  C  CA  . VAL   F  6  31  ? 16.944  -85.994  63.493  1.00 104.62 ? 27  VAL   F CA  1 
ATOM   9484  C  C   . VAL   F  6  31  ? 16.212  -85.115  64.510  1.00 106.61 ? 27  VAL   F C   1 
ATOM   9485  O  O   . VAL   F  6  31  ? 15.151  -85.545  65.006  1.00 111.40 ? 27  VAL   F O   1 
ATOM   9486  C  CB  . VAL   F  6  31  ? 18.215  -86.606  64.114  1.00 106.61 ? 27  VAL   F CB  1 
ATOM   9487  C  CG1 . VAL   F  6  31  ? 17.886  -87.454  65.333  1.00 108.10 ? 27  VAL   F CG1 1 
ATOM   9488  C  CG2 . VAL   F  6  31  ? 19.017  -87.416  63.106  1.00 107.70 ? 27  VAL   F CG2 1 
ATOM   9489  N  N   . GLU   F  6  32  ? 16.766  -83.934  64.802  1.00 106.38 ? 28  GLU   F N   1 
ATOM   9490  C  CA  . GLU   F  6  32  ? 16.199  -82.957  65.769  1.00 104.76 ? 28  GLU   F CA  1 
ATOM   9491  C  C   . GLU   F  6  32  ? 14.745  -82.667  65.376  1.00 99.46  ? 28  GLU   F C   1 
ATOM   9492  O  O   . GLU   F  6  32  ? 13.919  -82.484  66.287  1.00 98.81  ? 28  GLU   F O   1 
ATOM   9493  C  CB  . GLU   F  6  32  ? 17.068  -81.696  65.818  1.00 109.82 ? 28  GLU   F CB  1 
ATOM   9494  C  CG  . GLU   F  6  32  ? 18.423  -81.922  66.474  1.00 113.89 ? 28  GLU   F CG  1 
ATOM   9495  C  CD  . GLU   F  6  32  ? 19.416  -80.773  66.377  1.00 124.15 ? 28  GLU   F CD  1 
ATOM   9496  O  OE1 . GLU   F  6  32  ? 19.058  -79.717  65.810  1.00 134.30 ? 28  GLU   F OE1 1 
ATOM   9497  O  OE2 . GLU   F  6  32  ? 20.551  -80.940  66.872  1.00 120.59 ? 28  GLU   F OE2 1 
ATOM   9498  N  N   . ASN   F  6  33  ? 14.444  -82.671  64.072  1.00 102.41 ? 29  ASN   F N   1 
ATOM   9499  C  CA  . ASN   F  6  33  ? 13.104  -82.356  63.507  1.00 109.51 ? 29  ASN   F CA  1 
ATOM   9500  C  C   . ASN   F  6  33  ? 12.112  -83.484  63.828  1.00 109.85 ? 29  ASN   F C   1 
ATOM   9501  O  O   . ASN   F  6  33  ? 10.911  -83.182  63.970  1.00 117.24 ? 29  ASN   F O   1 
ATOM   9502  C  CB  . ASN   F  6  33  ? 13.179  -82.107  61.998  1.00 111.27 ? 29  ASN   F CB  1 
ATOM   9503  C  CG  . ASN   F  6  33  ? 11.909  -81.510  61.431  1.00 115.84 ? 29  ASN   F CG  1 
ATOM   9504  O  OD1 . ASN   F  6  33  ? 11.216  -82.153  60.646  1.00 115.34 ? 29  ASN   F OD1 1 
ATOM   9505  N  ND2 . ASN   F  6  33  ? 11.594  -80.286  61.827  1.00 120.24 ? 29  ASN   F ND2 1 
ATOM   9506  N  N   . GLY   F  6  34  ? 12.590  -84.728  63.938  1.00 108.06 ? 30  GLY   F N   1 
ATOM   9507  C  CA  . GLY   F  6  34  ? 11.748  -85.927  64.123  1.00 109.65 ? 30  GLY   F CA  1 
ATOM   9508  C  C   . GLY   F  6  34  ? 11.063  -85.956  65.480  1.00 113.19 ? 30  GLY   F C   1 
ATOM   9509  O  O   . GLY   F  6  34  ? 11.383  -85.095  66.323  1.00 111.69 ? 30  GLY   F O   1 
ATOM   9510  N  N   . THR   F  6  35  ? 10.159  -86.923  65.685  1.00 114.66 ? 31  THR   F N   1 
ATOM   9511  C  CA  . THR   F  6  35  ? 9.380   -87.115  66.942  1.00 114.64 ? 31  THR   F CA  1 
ATOM   9512  C  C   . THR   F  6  35  ? 10.312  -87.671  68.023  1.00 113.74 ? 31  THR   F C   1 
ATOM   9513  O  O   . THR   F  6  35  ? 11.404  -88.155  67.666  1.00 107.48 ? 31  THR   F O   1 
ATOM   9514  C  CB  . THR   F  6  35  ? 8.170   -88.043  66.748  1.00 113.71 ? 31  THR   F CB  1 
ATOM   9515  O  OG1 . THR   F  6  35  ? 8.636   -89.380  66.562  1.00 110.33 ? 31  THR   F OG1 1 
ATOM   9516  C  CG2 . THR   F  6  35  ? 7.292   -87.648  65.580  1.00 116.51 ? 31  THR   F CG2 1 
ATOM   9517  N  N   . THR   F  6  36  ? 9.890   -87.613  69.289  1.00 114.58 ? 32  THR   F N   1 
ATOM   9518  C  CA  . THR   F  6  36  ? 10.704  -88.047  70.454  1.00 117.63 ? 32  THR   F CA  1 
ATOM   9519  C  C   . THR   F  6  36  ? 10.666  -89.576  70.568  1.00 115.92 ? 32  THR   F C   1 
ATOM   9520  O  O   . THR   F  6  36  ? 9.570   -90.159  70.443  1.00 116.72 ? 32  THR   F O   1 
ATOM   9521  C  CB  . THR   F  6  36  ? 10.250  -87.389  71.763  1.00 122.57 ? 32  THR   F CB  1 
ATOM   9522  O  OG1 . THR   F  6  36  ? 10.007  -86.000  71.532  1.00 126.38 ? 32  THR   F OG1 1 
ATOM   9523  C  CG2 . THR   F  6  36  ? 11.275  -87.553  72.864  1.00 119.52 ? 32  THR   F CG2 1 
ATOM   9524  N  N   . SER   F  6  37  ? 11.833  -90.188  70.784  1.00 112.17 ? 33  SER   F N   1 
ATOM   9525  C  CA  . SER   F  6  37  ? 12.011  -91.622  71.131  1.00 110.29 ? 33  SER   F CA  1 
ATOM   9526  C  C   . SER   F  6  37  ? 13.025  -91.731  72.275  1.00 112.32 ? 33  SER   F C   1 
ATOM   9527  O  O   . SER   F  6  37  ? 13.969  -90.914  72.306  1.00 112.57 ? 33  SER   F O   1 
ATOM   9528  C  CB  . SER   F  6  37  ? 12.438  -92.428  69.934  1.00 105.62 ? 33  SER   F CB  1 
ATOM   9529  O  OG  . SER   F  6  37  ? 13.656  -91.936  69.397  1.00 99.54  ? 33  SER   F OG  1 
ATOM   9530  N  N   . ILE   F  6  38  ? 12.834  -92.699  73.176  1.00 109.85 ? 34  ILE   F N   1 
ATOM   9531  C  CA  . ILE   F  6  38  ? 13.661  -92.865  74.409  1.00 109.69 ? 34  ILE   F CA  1 
ATOM   9532  C  C   . ILE   F  6  38  ? 14.002  -94.343  74.613  1.00 109.60 ? 34  ILE   F C   1 
ATOM   9533  O  O   . ILE   F  6  38  ? 13.339  -95.207  73.998  1.00 108.84 ? 34  ILE   F O   1 
ATOM   9534  C  CB  . ILE   F  6  38  ? 12.942  -92.292  75.646  1.00 108.61 ? 34  ILE   F CB  1 
ATOM   9535  C  CG1 . ILE   F  6  38  ? 11.553  -92.910  75.832  1.00 107.09 ? 34  ILE   F CG1 1 
ATOM   9536  C  CG2 . ILE   F  6  38  ? 12.883  -90.775  75.576  1.00 110.98 ? 34  ILE   F CG2 1 
ATOM   9537  C  CD1 . ILE   F  6  38  ? 10.987  -92.748  77.221  1.00 106.45 ? 34  ILE   F CD1 1 
ATOM   9538  N  N   . GLY   F  6  39  ? 14.996  -94.592  75.468  1.00 109.55 ? 35  GLY   F N   1 
ATOM   9539  C  CA  . GLY   F  6  39  ? 15.379  -95.926  75.964  1.00 106.42 ? 35  GLY   F CA  1 
ATOM   9540  C  C   . GLY   F  6  39  ? 15.774  -95.858  77.427  1.00 104.66 ? 35  GLY   F C   1 
ATOM   9541  O  O   . GLY   F  6  39  ? 16.641  -95.027  77.757  1.00 101.61 ? 35  GLY   F O   1 
ATOM   9542  N  N   . ILE   F  6  40  ? 15.140  -96.674  78.276  1.00 105.85 ? 36  ILE   F N   1 
ATOM   9543  C  CA  . ILE   F  6  40  ? 15.453  -96.777  79.733  1.00 106.10 ? 36  ILE   F CA  1 
ATOM   9544  C  C   . ILE   F  6  40  ? 16.033  -98.168  80.006  1.00 104.50 ? 36  ILE   F C   1 
ATOM   9545  O  O   . ILE   F  6  40  ? 15.312  -99.165  79.799  1.00 102.40 ? 36  ILE   F O   1 
ATOM   9546  C  CB  . ILE   F  6  40  ? 14.218  -96.495  80.613  1.00 107.82 ? 36  ILE   F CB  1 
ATOM   9547  C  CG1 . ILE   F  6  40  ? 13.496  -95.210  80.199  1.00 112.26 ? 36  ILE   F CG1 1 
ATOM   9548  C  CG2 . ILE   F  6  40  ? 14.615  -96.465  82.083  1.00 106.26 ? 36  ILE   F CG2 1 
ATOM   9549  C  CD1 . ILE   F  6  40  ? 12.150  -95.015  80.862  1.00 117.24 ? 36  ILE   F CD1 1 
ATOM   9550  N  N   . LYS   F  6  41  ? 17.289  -98.215  80.453  1.00 105.12 ? 37  LYS   F N   1 
ATOM   9551  C  CA  . LYS   F  6  41  ? 17.963  -99.439  80.958  1.00 105.01 ? 37  LYS   F CA  1 
ATOM   9552  C  C   . LYS   F  6  41  ? 17.453  -99.708  82.374  1.00 107.61 ? 37  LYS   F C   1 
ATOM   9553  O  O   . LYS   F  6  41  ? 17.299  -98.732  83.133  1.00 109.90 ? 37  LYS   F O   1 
ATOM   9554  C  CB  . LYS   F  6  41  ? 19.480  -99.242  80.957  1.00 104.45 ? 37  LYS   F CB  1 
ATOM   9555  C  CG  . LYS   F  6  41  ? 20.306  -100.489 81.225  1.00 104.89 ? 37  LYS   F CG  1 
ATOM   9556  C  CD  . LYS   F  6  41  ? 21.761  -100.163 81.453  1.00 109.06 ? 37  LYS   F CD  1 
ATOM   9557  C  CE  . LYS   F  6  41  ? 22.616  -101.385 81.706  1.00 111.24 ? 37  LYS   F CE  1 
ATOM   9558  N  NZ  . LYS   F  6  41  ? 24.051  -101.025 81.790  1.00 115.38 ? 37  LYS   F NZ  1 
ATOM   9559  N  N   . CYS   F  6  42  ? 17.205  -100.975 82.714  1.00 107.20 ? 38  CYS   F N   1 
ATOM   9560  C  CA  . CYS   F  6  42  ? 16.610  -101.389 84.013  1.00 111.93 ? 38  CYS   F CA  1 
ATOM   9561  C  C   . CYS   F  6  42  ? 17.417  -102.544 84.620  1.00 112.06 ? 38  CYS   F C   1 
ATOM   9562  O  O   . CYS   F  6  42  ? 18.476  -102.888 84.055  1.00 106.12 ? 38  CYS   F O   1 
ATOM   9563  C  CB  . CYS   F  6  42  ? 15.134  -101.737 83.840  1.00 116.32 ? 38  CYS   F CB  1 
ATOM   9564  S  SG  . CYS   F  6  42  ? 14.818  -103.286 82.955  1.00 117.44 ? 38  CYS   F SG  1 
ATOM   9565  N  N   . ASN   F  6  43  ? 16.939  -103.082 85.747  1.00 118.23 ? 39  ASN   F N   1 
ATOM   9566  C  CA  . ASN   F  6  43  ? 17.583  -104.160 86.548  1.00 121.84 ? 39  ASN   F CA  1 
ATOM   9567  C  C   . ASN   F  6  43  ? 18.140  -105.263 85.643  1.00 118.61 ? 39  ASN   F C   1 
ATOM   9568  O  O   . ASN   F  6  43  ? 19.355  -105.529 85.726  1.00 114.96 ? 39  ASN   F O   1 
ATOM   9569  C  CB  . ASN   F  6  43  ? 16.601  -104.768 87.553  1.00 125.98 ? 39  ASN   F CB  1 
ATOM   9570  C  CG  . ASN   F  6  43  ? 16.406  -103.900 88.777  1.00 131.79 ? 39  ASN   F CG  1 
ATOM   9571  O  OD1 . ASN   F  6  43  ? 17.312  -103.172 89.179  1.00 128.96 ? 39  ASN   F OD1 1 
ATOM   9572  N  ND2 . ASN   F  6  43  ? 15.228  -103.972 89.378  1.00 138.77 ? 39  ASN   F ND2 1 
ATOM   9573  N  N   . ASP   F  6  44  ? 17.283  -105.885 84.828  1.00 119.77 ? 40  ASP   F N   1 
ATOM   9574  C  CA  . ASP   F  6  44  ? 17.615  -107.110 84.052  1.00 120.88 ? 40  ASP   F CA  1 
ATOM   9575  C  C   . ASP   F  6  44  ? 17.214  -106.945 82.581  1.00 120.23 ? 40  ASP   F C   1 
ATOM   9576  O  O   . ASP   F  6  44  ? 16.987  -107.981 81.923  1.00 123.73 ? 40  ASP   F O   1 
ATOM   9577  C  CB  . ASP   F  6  44  ? 16.941  -108.340 84.671  1.00 122.72 ? 40  ASP   F CB  1 
ATOM   9578  C  CG  . ASP   F  6  44  ? 15.420  -108.310 84.637  1.00 125.32 ? 40  ASP   F CG  1 
ATOM   9579  O  OD1 . ASP   F  6  44  ? 14.855  -107.222 84.393  1.00 131.30 ? 40  ASP   F OD1 1 
ATOM   9580  O  OD2 . ASP   F  6  44  ? 14.811  -109.377 84.856  1.00 122.30 ? 40  ASP   F OD2 1 
ATOM   9581  N  N   . GLY   F  6  45  ? 17.139  -105.712 82.068  1.00 117.78 ? 41  GLY   F N   1 
ATOM   9582  C  CA  . GLY   F  6  45  ? 16.727  -105.478 80.671  1.00 115.22 ? 41  GLY   F CA  1 
ATOM   9583  C  C   . GLY   F  6  45  ? 16.699  -104.013 80.272  1.00 112.67 ? 41  GLY   F C   1 
ATOM   9584  O  O   . GLY   F  6  45  ? 17.378  -103.196 80.926  1.00 111.66 ? 41  GLY   F O   1 
ATOM   9585  N  N   . VAL   F  6  46  ? 15.935  -103.712 79.218  1.00 107.61 ? 42  VAL   F N   1 
ATOM   9586  C  CA  . VAL   F  6  46  ? 15.800  -102.362 78.595  1.00 107.05 ? 42  VAL   F CA  1 
ATOM   9587  C  C   . VAL   F  6  46  ? 14.331  -102.140 78.223  1.00 109.58 ? 42  VAL   F C   1 
ATOM   9588  O  O   . VAL   F  6  46  ? 13.627  -103.139 77.976  1.00 111.95 ? 42  VAL   F O   1 
ATOM   9589  C  CB  . VAL   F  6  46  ? 16.715  -102.216 77.363  1.00 107.47 ? 42  VAL   F CB  1 
ATOM   9590  C  CG1 . VAL   F  6  46  ? 18.169  -102.033 77.763  1.00 107.35 ? 42  VAL   F CG1 1 
ATOM   9591  C  CG2 . VAL   F  6  46  ? 16.569  -103.383 76.396  1.00 107.98 ? 42  VAL   F CG2 1 
ATOM   9592  N  N   . VAL   F  6  47  ? 13.900  -100.876 78.187  1.00 111.62 ? 43  VAL   F N   1 
ATOM   9593  C  CA  . VAL   F  6  47  ? 12.529  -100.455 77.773  1.00 112.30 ? 43  VAL   F CA  1 
ATOM   9594  C  C   . VAL   F  6  47  ? 12.659  -99.356  76.714  1.00 113.65 ? 43  VAL   F C   1 
ATOM   9595  O  O   . VAL   F  6  47  ? 13.431  -98.402  76.944  1.00 115.20 ? 43  VAL   F O   1 
ATOM   9596  C  CB  . VAL   F  6  47  ? 11.695  -99.975  78.977  1.00 112.57 ? 43  VAL   F CB  1 
ATOM   9597  C  CG1 . VAL   F  6  47  ? 10.327  -99.462  78.551  1.00 113.57 ? 43  VAL   F CG1 1 
ATOM   9598  C  CG2 . VAL   F  6  47  ? 11.553  -101.064 80.028  1.00 111.67 ? 43  VAL   F CG2 1 
ATOM   9599  N  N   . PHE   F  6  48  ? 11.920  -99.494  75.608  1.00 111.22 ? 44  PHE   F N   1 
ATOM   9600  C  CA  . PHE   F  6  48  ? 11.857  -98.521  74.487  1.00 105.02 ? 44  PHE   F CA  1 
ATOM   9601  C  C   . PHE   F  6  48  ? 10.439  -97.957  74.397  1.00 102.15 ? 44  PHE   F C   1 
ATOM   9602  O  O   . PHE   F  6  48  ? 9.470   -98.718  74.576  1.00 99.77  ? 44  PHE   F O   1 
ATOM   9603  C  CB  . PHE   F  6  48  ? 12.269  -99.182  73.170  1.00 101.04 ? 44  PHE   F CB  1 
ATOM   9604  C  CG  . PHE   F  6  48  ? 13.547  -99.972  73.259  1.00 98.96  ? 44  PHE   F CG  1 
ATOM   9605  C  CD1 . PHE   F  6  48  ? 14.779  -99.340  73.196  1.00 101.28 ? 44  PHE   F CD1 1 
ATOM   9606  C  CD2 . PHE   F  6  48  ? 13.516  -101.345 73.440  1.00 95.66  ? 44  PHE   F CD2 1 
ATOM   9607  C  CE1 . PHE   F  6  48  ? 15.955  -100.067 73.295  1.00 99.21  ? 44  PHE   F CE1 1 
ATOM   9608  C  CE2 . PHE   F  6  48  ? 14.692  -102.071 73.536  1.00 97.03  ? 44  PHE   F CE2 1 
ATOM   9609  C  CZ  . PHE   F  6  48  ? 15.908  -101.431 73.463  1.00 97.14  ? 44  PHE   F CZ  1 
ATOM   9610  N  N   . ALA   F  6  49  ? 10.334  -96.654  74.139  1.00 102.31 ? 45  ALA   F N   1 
ATOM   9611  C  CA  . ALA   F  6  49  ? 9.063   -95.938  73.902  1.00 102.68 ? 45  ALA   F CA  1 
ATOM   9612  C  C   . ALA   F  6  49  ? 9.290   -94.898  72.805  1.00 103.07 ? 45  ALA   F C   1 
ATOM   9613  O  O   . ALA   F  6  49  ? 10.459  -94.509  72.600  1.00 98.10  ? 45  ALA   F O   1 
ATOM   9614  C  CB  . ALA   F  6  49  ? 8.572   -95.317  75.186  1.00 104.51 ? 45  ALA   F CB  1 
ATOM   9615  N  N   . VAL   F  6  50  ? 8.222   -94.498  72.109  1.00 107.51 ? 46  VAL   F N   1 
ATOM   9616  C  CA  . VAL   F  6  50  ? 8.281   -93.483  71.017  1.00 108.61 ? 46  VAL   F CA  1 
ATOM   9617  C  C   . VAL   F  6  50  ? 6.948   -92.734  70.930  1.00 111.60 ? 46  VAL   F C   1 
ATOM   9618  O  O   . VAL   F  6  50  ? 5.895   -93.337  71.230  1.00 104.88 ? 46  VAL   F O   1 
ATOM   9619  C  CB  . VAL   F  6  50  ? 8.660   -94.129  69.669  1.00 110.96 ? 46  VAL   F CB  1 
ATOM   9620  C  CG1 . VAL   F  6  50  ? 7.628   -95.145  69.205  1.00 112.71 ? 46  VAL   F CG1 1 
ATOM   9621  C  CG2 . VAL   F  6  50  ? 8.911   -93.084  68.592  1.00 113.71 ? 46  VAL   F CG2 1 
ATOM   9622  N  N   . GLU   F  6  51  ? 7.028   -91.462  70.528  1.00 114.26 ? 47  GLU   F N   1 
ATOM   9623  C  CA  . GLU   F  6  51  ? 5.886   -90.554  70.242  1.00 115.61 ? 47  GLU   F CA  1 
ATOM   9624  C  C   . GLU   F  6  51  ? 5.464   -90.750  68.781  1.00 108.80 ? 47  GLU   F C   1 
ATOM   9625  O  O   . GLU   F  6  51  ? 6.318   -90.557  67.890  1.00 99.82  ? 47  GLU   F O   1 
ATOM   9626  C  CB  . GLU   F  6  51  ? 6.311   -89.111  70.535  1.00 116.39 ? 47  GLU   F CB  1 
ATOM   9627  C  CG  . GLU   F  6  51  ? 5.381   -88.045  69.984  1.00 121.04 ? 47  GLU   F CG  1 
ATOM   9628  C  CD  . GLU   F  6  51  ? 5.866   -86.624  70.217  1.00 121.06 ? 47  GLU   F CD  1 
ATOM   9629  O  OE1 . GLU   F  6  51  ? 5.019   -85.715  70.253  1.00 130.50 ? 47  GLU   F OE1 1 
ATOM   9630  O  OE2 . GLU   F  6  51  ? 7.092   -86.429  70.355  1.00 119.31 ? 47  GLU   F OE2 1 
ATOM   9631  N  N   . LYS   F  6  52  ? 4.205   -91.136  68.553  1.00 109.19 ? 48  LYS   F N   1 
ATOM   9632  C  CA  . LYS   F  6  52  ? 3.587   -91.256  67.205  1.00 112.61 ? 48  LYS   F CA  1 
ATOM   9633  C  C   . LYS   F  6  52  ? 2.557   -90.136  67.040  1.00 110.92 ? 48  LYS   F C   1 
ATOM   9634  O  O   . LYS   F  6  52  ? 1.434   -90.300  67.551  1.00 110.22 ? 48  LYS   F O   1 
ATOM   9635  C  CB  . LYS   F  6  52  ? 2.913   -92.620  67.034  1.00 115.95 ? 48  LYS   F CB  1 
ATOM   9636  C  CG  . LYS   F  6  52  ? 3.840   -93.825  67.098  1.00 120.30 ? 48  LYS   F CG  1 
ATOM   9637  C  CD  . LYS   F  6  52  ? 3.109   -95.131  67.337  1.00 123.23 ? 48  LYS   F CD  1 
ATOM   9638  C  CE  . LYS   F  6  52  ? 2.165   -95.504  66.213  1.00 123.80 ? 48  LYS   F CE  1 
ATOM   9639  N  NZ  . LYS   F  6  52  ? 1.634   -96.878  66.374  1.00 124.39 ? 48  LYS   F NZ  1 
ATOM   9640  N  N   . LEU   F  6  53  ? 2.930   -89.040  66.371  1.00 113.35 ? 49  LEU   F N   1 
ATOM   9641  C  CA  . LEU   F  6  53  ? 2.014   -87.899  66.097  1.00 113.96 ? 49  LEU   F CA  1 
ATOM   9642  C  C   . LEU   F  6  53  ? 0.822   -88.417  65.289  1.00 110.59 ? 49  LEU   F C   1 
ATOM   9643  O  O   . LEU   F  6  53  ? 1.056   -88.993  64.207  1.00 101.81 ? 49  LEU   F O   1 
ATOM   9644  C  CB  . LEU   F  6  53  ? 2.742   -86.804  65.310  1.00 112.45 ? 49  LEU   F CB  1 
ATOM   9645  C  CG  . LEU   F  6  53  ? 3.903   -86.104  66.013  1.00 110.71 ? 49  LEU   F CG  1 
ATOM   9646  C  CD1 . LEU   F  6  53  ? 4.487   -85.031  65.107  1.00 111.08 ? 49  LEU   F CD1 1 
ATOM   9647  C  CD2 . LEU   F  6  53  ? 3.470   -85.498  67.340  1.00 113.57 ? 49  LEU   F CD2 1 
ATOM   9648  N  N   . ILE   F  6  54  ? -0.399  -88.225  65.799  1.00 115.28 ? 50  ILE   F N   1 
ATOM   9649  C  CA  . ILE   F  6  54  ? -1.660  -88.535  65.063  1.00 118.02 ? 50  ILE   F CA  1 
ATOM   9650  C  C   . ILE   F  6  54  ? -1.951  -87.341  64.146  1.00 120.49 ? 50  ILE   F C   1 
ATOM   9651  O  O   . ILE   F  6  54  ? -2.591  -86.373  64.610  1.00 122.24 ? 50  ILE   F O   1 
ATOM   9652  C  CB  . ILE   F  6  54  ? -2.833  -88.851  66.016  1.00 116.25 ? 50  ILE   F CB  1 
ATOM   9653  C  CG1 . ILE   F  6  54  ? -2.468  -89.932  67.039  1.00 114.04 ? 50  ILE   F CG1 1 
ATOM   9654  C  CG2 . ILE   F  6  54  ? -4.073  -89.233  65.218  1.00 115.97 ? 50  ILE   F CG2 1 
ATOM   9655  C  CD1 . ILE   F  6  54  ? -3.503  -90.138  68.124  1.00 115.12 ? 50  ILE   F CD1 1 
ATOM   9656  N  N   . THR   F  6  55  ? -1.457  -87.400  62.905  1.00 123.90 ? 51  THR   F N   1 
ATOM   9657  C  CA  . THR   F  6  55  ? -1.644  -86.359  61.858  1.00 123.45 ? 51  THR   F CA  1 
ATOM   9658  C  C   . THR   F  6  55  ? -3.139  -86.137  61.608  1.00 122.48 ? 51  THR   F C   1 
ATOM   9659  O  O   . THR   F  6  55  ? -3.542  -84.967  61.483  1.00 124.94 ? 51  THR   F O   1 
ATOM   9660  C  CB  . THR   F  6  55  ? -0.958  -86.742  60.540  1.00 123.01 ? 51  THR   F CB  1 
ATOM   9661  O  OG1 . THR   F  6  55  ? 0.346   -87.245  60.828  1.00 126.57 ? 51  THR   F OG1 1 
ATOM   9662  C  CG2 . THR   F  6  55  ? -0.852  -85.575  59.583  1.00 120.58 ? 51  THR   F CG2 1 
ATOM   9663  N  N   . SER   F  6  56  ? -3.919  -87.221  61.533  1.00 122.07 ? 52  SER   F N   1 
ATOM   9664  C  CA  . SER   F  6  56  ? -5.357  -87.202  61.159  1.00 123.16 ? 52  SER   F CA  1 
ATOM   9665  C  C   . SER   F  6  56  ? -6.135  -88.295  61.904  1.00 122.02 ? 52  SER   F C   1 
ATOM   9666  O  O   . SER   F  6  56  ? -5.515  -89.286  62.341  1.00 120.42 ? 52  SER   F O   1 
ATOM   9667  C  CB  . SER   F  6  56  ? -5.505  -87.340  59.665  1.00 123.13 ? 52  SER   F CB  1 
ATOM   9668  O  OG  . SER   F  6  56  ? -6.860  -87.550  59.300  1.00 128.10 ? 52  SER   F OG  1 
ATOM   9669  N  N   . LYS   F  6  57  ? -7.453  -88.101  62.027  1.00 121.36 ? 53  LYS   F N   1 
ATOM   9670  C  CA  . LYS   F  6  57  ? -8.441  -89.100  62.526  1.00 124.40 ? 53  LYS   F CA  1 
ATOM   9671  C  C   . LYS   F  6  57  ? -8.347  -90.393  61.701  1.00 126.90 ? 53  LYS   F C   1 
ATOM   9672  O  O   . LYS   F  6  57  ? -8.689  -91.467  62.245  1.00 120.01 ? 53  LYS   F O   1 
ATOM   9673  C  CB  . LYS   F  6  57  ? -9.860  -88.523  62.445  1.00 125.31 ? 53  LYS   F CB  1 
ATOM   9674  C  CG  . LYS   F  6  57  ? -10.338 -87.765  63.677  1.00 126.53 ? 53  LYS   F CG  1 
ATOM   9675  C  CD  . LYS   F  6  57  ? -10.944 -88.661  64.735  1.00 130.72 ? 53  LYS   F CD  1 
ATOM   9676  C  CE  . LYS   F  6  57  ? -11.573 -87.894  65.879  1.00 131.88 ? 53  LYS   F CE  1 
ATOM   9677  N  NZ  . LYS   F  6  57  ? -12.058 -88.806  66.941  1.00 136.05 ? 53  LYS   F NZ  1 
ATOM   9678  N  N   . LEU   F  6  58  ? -7.905  -90.290  60.441  1.00 124.76 ? 54  LEU   F N   1 
ATOM   9679  C  CA  . LEU   F  6  58  ? -7.947  -91.382  59.429  1.00 126.14 ? 54  LEU   F CA  1 
ATOM   9680  C  C   . LEU   F  6  58  ? -6.816  -92.398  59.646  1.00 124.15 ? 54  LEU   F C   1 
ATOM   9681  O  O   . LEU   F  6  58  ? -6.897  -93.477  59.028  1.00 123.56 ? 54  LEU   F O   1 
ATOM   9682  C  CB  . LEU   F  6  58  ? -7.862  -90.767  58.029  1.00 124.88 ? 54  LEU   F CB  1 
ATOM   9683  C  CG  . LEU   F  6  58  ? -9.034  -89.866  57.640  1.00 126.33 ? 54  LEU   F CG  1 
ATOM   9684  C  CD1 . LEU   F  6  58  ? -8.662  -88.955  56.480  1.00 126.14 ? 54  LEU   F CD1 1 
ATOM   9685  C  CD2 . LEU   F  6  58  ? -10.265 -90.692  57.301  1.00 127.11 ? 54  LEU   F CD2 1 
ATOM   9686  N  N   . LEU   F  6  59  ? -5.802  -92.081  60.461  1.00 124.79 ? 55  LEU   F N   1 
ATOM   9687  C  CA  . LEU   F  6  59  ? -4.756  -93.058  60.878  1.00 122.32 ? 55  LEU   F CA  1 
ATOM   9688  C  C   . LEU   F  6  59  ? -5.427  -94.169  61.690  1.00 124.12 ? 55  LEU   F C   1 
ATOM   9689  O  O   . LEU   F  6  59  ? -6.137  -93.833  62.658  1.00 131.23 ? 55  LEU   F O   1 
ATOM   9690  C  CB  . LEU   F  6  59  ? -3.685  -92.373  61.732  1.00 120.02 ? 55  LEU   F CB  1 
ATOM   9691  C  CG  . LEU   F  6  59  ? -2.725  -91.432  61.007  1.00 120.09 ? 55  LEU   F CG  1 
ATOM   9692  C  CD1 . LEU   F  6  59  ? -1.853  -90.697  62.012  1.00 121.12 ? 55  LEU   F CD1 1 
ATOM   9693  C  CD2 . LEU   F  6  59  ? -1.856  -92.184  60.012  1.00 117.56 ? 55  LEU   F CD2 1 
ATOM   9694  N  N   . VAL   F  6  60  ? -5.204  -95.434  61.322  1.00 123.59 ? 56  VAL   F N   1 
ATOM   9695  C  CA  . VAL   F  6  60  ? -5.712  -96.613  62.086  1.00 120.36 ? 56  VAL   F CA  1 
ATOM   9696  C  C   . VAL   F  6  60  ? -4.872  -96.737  63.354  1.00 118.61 ? 56  VAL   F C   1 
ATOM   9697  O  O   . VAL   F  6  60  ? -3.653  -96.881  63.272  1.00 116.46 ? 56  VAL   F O   1 
ATOM   9698  C  CB  . VAL   F  6  60  ? -5.679  -97.908  61.253  1.00 120.22 ? 56  VAL   F CB  1 
ATOM   9699  C  CG1 . VAL   F  6  60  ? -6.196  -99.097  62.050  1.00 120.05 ? 56  VAL   F CG1 1 
ATOM   9700  C  CG2 . VAL   F  6  60  ? -6.456  -97.762  59.953  1.00 119.06 ? 56  VAL   F CG2 1 
ATOM   9701  N  N   . PRO   F  6  61  ? -5.481  -96.659  64.561  1.00 117.50 ? 57  PRO   F N   1 
ATOM   9702  C  CA  . PRO   F  6  61  ? -4.728  -96.801  65.808  1.00 119.46 ? 57  PRO   F CA  1 
ATOM   9703  C  C   . PRO   F  6  61  ? -4.051  -98.175  65.936  1.00 119.94 ? 57  PRO   F C   1 
ATOM   9704  O  O   . PRO   F  6  61  ? -4.619  -99.151  65.480  1.00 119.43 ? 57  PRO   F O   1 
ATOM   9705  C  CB  . PRO   F  6  61  ? -5.786  -96.608  66.908  1.00 119.71 ? 57  PRO   F CB  1 
ATOM   9706  C  CG  . PRO   F  6  61  ? -6.917  -95.872  66.221  1.00 119.24 ? 57  PRO   F CG  1 
ATOM   9707  C  CD  . PRO   F  6  61  ? -6.908  -96.393  64.800  1.00 118.06 ? 57  PRO   F CD  1 
ATOM   9708  N  N   . GLN   F  6  62  ? -2.853  -98.195  66.532  1.00 124.65 ? 58  GLN   F N   1 
ATOM   9709  C  CA  . GLN   F  6  62  ? -2.035  -99.403  66.842  1.00 128.24 ? 58  GLN   F CA  1 
ATOM   9710  C  C   . GLN   F  6  62  ? -1.465  -100.042 65.565  1.00 126.84 ? 58  GLN   F C   1 
ATOM   9711  O  O   . GLN   F  6  62  ? -0.812  -101.092 65.706  1.00 131.02 ? 58  GLN   F O   1 
ATOM   9712  C  CB  . GLN   F  6  62  ? -2.853  -100.434 67.632  1.00 130.14 ? 58  GLN   F CB  1 
ATOM   9713  C  CG  . GLN   F  6  62  ? -2.616  -100.391 69.135  1.00 135.25 ? 58  GLN   F CG  1 
ATOM   9714  C  CD  . GLN   F  6  62  ? -3.079  -99.097  69.761  1.00 137.67 ? 58  GLN   F CD  1 
ATOM   9715  O  OE1 . GLN   F  6  62  ? -4.102  -98.533  69.381  1.00 144.63 ? 58  GLN   F OE1 1 
ATOM   9716  N  NE2 . GLN   F  6  62  ? -2.328  -98.619  70.741  1.00 140.41 ? 58  GLN   F NE2 1 
ATOM   9717  N  N   . LYS   F  6  63  ? -1.653  -99.444  64.380  1.00 127.28 ? 59  LYS   F N   1 
ATOM   9718  C  CA  . LYS   F  6  63  ? -1.400  -100.136 63.083  1.00 126.57 ? 59  LYS   F CA  1 
ATOM   9719  C  C   . LYS   F  6  63  ? -0.365  -99.402  62.216  1.00 123.70 ? 59  LYS   F C   1 
ATOM   9720  O  O   . LYS   F  6  63  ? -0.286  -99.726  61.012  1.00 133.79 ? 59  LYS   F O   1 
ATOM   9721  C  CB  . LYS   F  6  63  ? -2.719  -100.343 62.327  1.00 132.22 ? 59  LYS   F CB  1 
ATOM   9722  C  CG  . LYS   F  6  63  ? -3.469  -101.622 62.681  1.00 138.59 ? 59  LYS   F CG  1 
ATOM   9723  C  CD  . LYS   F  6  63  ? -2.629  -102.890 62.563  1.00 141.24 ? 59  LYS   F CD  1 
ATOM   9724  C  CE  . LYS   F  6  63  ? -2.986  -103.767 61.381  1.00 146.86 ? 59  LYS   F CE  1 
ATOM   9725  N  NZ  . LYS   F  6  63  ? -4.039  -104.750 61.732  1.00 150.91 ? 59  LYS   F NZ  1 
ATOM   9726  N  N   . ASN   F  6  64  ? 0.426   -98.490  62.790  1.00 116.72 ? 60  ASN   F N   1 
ATOM   9727  C  CA  . ASN   F  6  64  ? 1.626   -97.911  62.127  1.00 110.62 ? 60  ASN   F CA  1 
ATOM   9728  C  C   . ASN   F  6  64  ? 2.815   -98.074  63.076  1.00 110.09 ? 60  ASN   F C   1 
ATOM   9729  O  O   . ASN   F  6  64  ? 3.324   -97.058  63.576  1.00 114.41 ? 60  ASN   F O   1 
ATOM   9730  C  CB  . ASN   F  6  64  ? 1.399   -96.460  61.696  1.00 111.45 ? 60  ASN   F CB  1 
ATOM   9731  C  CG  . ASN   F  6  64  ? 0.449   -96.344  60.523  1.00 107.14 ? 60  ASN   F CG  1 
ATOM   9732  O  OD1 . ASN   F  6  64  ? 0.730   -96.855  59.441  1.00 107.90 ? 60  ASN   F OD1 1 
ATOM   9733  N  ND2 . ASN   F  6  64  ? -0.671  -95.667  60.718  1.00 110.35 ? 60  ASN   F ND2 1 
ATOM   9734  N  N   . VAL   F  6  65  ? 3.234   -99.322  63.294  1.00 109.42 ? 61  VAL   F N   1 
ATOM   9735  C  CA  . VAL   F  6  65  ? 4.237   -99.713  64.330  1.00 112.11 ? 61  VAL   F CA  1 
ATOM   9736  C  C   . VAL   F  6  65  ? 5.599   -99.141  63.914  1.00 109.89 ? 61  VAL   F C   1 
ATOM   9737  O  O   . VAL   F  6  65  ? 5.950   -99.264  62.723  1.00 111.85 ? 61  VAL   F O   1 
ATOM   9738  C  CB  . VAL   F  6  65  ? 4.284   -101.243 64.529  1.00 111.43 ? 61  VAL   F CB  1 
ATOM   9739  C  CG1 . VAL   F  6  65  ? 5.213   -101.635 65.668  1.00 111.96 ? 61  VAL   F CG1 1 
ATOM   9740  C  CG2 . VAL   F  6  65  ? 2.899   -101.836 64.759  1.00 111.85 ? 61  VAL   F CG2 1 
ATOM   9741  N  N   . LYS   F  6  66  ? 6.317   -98.516  64.854  1.00 110.00 ? 62  LYS   F N   1 
ATOM   9742  C  CA  . LYS   F  6  66  ? 7.596   -97.797  64.598  1.00 114.17 ? 62  LYS   F CA  1 
ATOM   9743  C  C   . LYS   F  6  66  ? 8.773   -98.521  65.261  1.00 110.86 ? 62  LYS   F C   1 
ATOM   9744  O  O   . LYS   F  6  66  ? 9.862   -98.513  64.652  1.00 114.55 ? 62  LYS   F O   1 
ATOM   9745  C  CB  . LYS   F  6  66  ? 7.504   -96.350  65.086  1.00 119.86 ? 62  LYS   F CB  1 
ATOM   9746  C  CG  . LYS   F  6  66  ? 6.603   -95.459  64.244  1.00 124.14 ? 62  LYS   F CG  1 
ATOM   9747  C  CD  . LYS   F  6  66  ? 6.602   -94.016  64.681  1.00 128.25 ? 62  LYS   F CD  1 
ATOM   9748  C  CE  . LYS   F  6  66  ? 7.791   -93.236  64.161  1.00 135.85 ? 62  LYS   F CE  1 
ATOM   9749  N  NZ  . LYS   F  6  66  ? 7.696   -91.799  64.512  1.00 139.28 ? 62  LYS   F NZ  1 
ATOM   9750  N  N   . ILE   F  6  67  ? 8.583   -99.096  66.456  1.00 108.52 ? 63  ILE   F N   1 
ATOM   9751  C  CA  . ILE   F  6  67  ? 9.623   -99.931  67.132  1.00 105.89 ? 63  ILE   F CA  1 
ATOM   9752  C  C   . ILE   F  6  67  ? 9.783   -101.213 66.306  1.00 102.76 ? 63  ILE   F C   1 
ATOM   9753  O  O   . ILE   F  6  67  ? 8.755   -101.775 65.880  1.00 104.52 ? 63  ILE   F O   1 
ATOM   9754  C  CB  . ILE   F  6  67  ? 9.283   -100.235 68.608  1.00 107.24 ? 63  ILE   F CB  1 
ATOM   9755  C  CG1 . ILE   F  6  67  ? 9.085   -98.964  69.440  1.00 105.91 ? 63  ILE   F CG1 1 
ATOM   9756  C  CG2 . ILE   F  6  67  ? 10.348  -101.134 69.222  1.00 109.90 ? 63  ILE   F CG2 1 
ATOM   9757  C  CD1 . ILE   F  6  67  ? 8.500   -99.213  70.814  1.00 108.54 ? 63  ILE   F CD1 1 
ATOM   9758  N  N   . GLN   F  6  68  ? 11.026  -101.641 66.078  1.00 99.57  ? 64  GLN   F N   1 
ATOM   9759  C  CA  . GLN   F  6  68  ? 11.367  -102.840 65.269  1.00 99.46  ? 64  GLN   F CA  1 
ATOM   9760  C  C   . GLN   F  6  68  ? 12.197  -103.804 66.118  1.00 99.86  ? 64  GLN   F C   1 
ATOM   9761  O  O   . GLN   F  6  68  ? 12.928  -103.331 67.010  1.00 100.47 ? 64  GLN   F O   1 
ATOM   9762  C  CB  . GLN   F  6  68  ? 12.131  -102.431 64.010  1.00 98.28  ? 64  GLN   F CB  1 
ATOM   9763  C  CG  . GLN   F  6  68  ? 11.236  -101.856 62.923  1.00 96.52  ? 64  GLN   F CG  1 
ATOM   9764  C  CD  . GLN   F  6  68  ? 12.000  -101.589 61.650  1.00 96.53  ? 64  GLN   F CD  1 
ATOM   9765  O  OE1 . GLN   F  6  68  ? 12.617  -100.541 61.482  1.00 97.86  ? 64  GLN   F OE1 1 
ATOM   9766  N  NE2 . GLN   F  6  68  ? 11.967  -102.544 60.735  1.00 97.69  ? 64  GLN   F NE2 1 
ATOM   9767  N  N   . VAL   F  6  69  ? 12.076  -105.105 65.841  1.00 98.33  ? 65  VAL   F N   1 
ATOM   9768  C  CA  . VAL   F  6  69  ? 12.872  -106.187 66.494  1.00 96.64  ? 65  VAL   F CA  1 
ATOM   9769  C  C   . VAL   F  6  69  ? 13.982  -106.618 65.529  1.00 96.15  ? 65  VAL   F C   1 
ATOM   9770  O  O   . VAL   F  6  69  ? 13.708  -106.721 64.316  1.00 99.36  ? 65  VAL   F O   1 
ATOM   9771  C  CB  . VAL   F  6  69  ? 11.989  -107.379 66.918  1.00 97.56  ? 65  VAL   F CB  1 
ATOM   9772  C  CG1 . VAL   F  6  69  ? 11.284  -108.033 65.737  1.00 95.53  ? 65  VAL   F CG1 1 
ATOM   9773  C  CG2 . VAL   F  6  69  ? 12.785  -108.414 67.698  1.00 97.34  ? 65  VAL   F CG2 1 
ATOM   9774  N  N   . VAL   F  6  70  ? 15.190  -106.843 66.055  1.00 93.53  ? 66  VAL   F N   1 
ATOM   9775  C  CA  . VAL   F  6  70  ? 16.319  -107.506 65.338  1.00 91.99  ? 66  VAL   F CA  1 
ATOM   9776  C  C   . VAL   F  6  70  ? 16.591  -108.842 66.039  1.00 94.03  ? 66  VAL   F C   1 
ATOM   9777  O  O   . VAL   F  6  70  ? 16.629  -108.859 67.287  1.00 99.17  ? 66  VAL   F O   1 
ATOM   9778  C  CB  . VAL   F  6  70  ? 17.571  -106.609 65.287  1.00 89.19  ? 66  VAL   F CB  1 
ATOM   9779  C  CG1 . VAL   F  6  70  ? 18.779  -107.347 64.728  1.00 86.30  ? 66  VAL   F CG1 1 
ATOM   9780  C  CG2 . VAL   F  6  70  ? 17.315  -105.339 64.492  1.00 89.23  ? 66  VAL   F CG2 1 
ATOM   9781  N  N   . ASP   F  6  71  ? 16.762  -109.915 65.262  1.00 92.52  ? 67  ASP   F N   1 
ATOM   9782  C  CA  . ASP   F  6  71  ? 16.869  -111.310 65.764  1.00 96.17  ? 67  ASP   F CA  1 
ATOM   9783  C  C   . ASP   F  6  71  ? 15.605  -111.597 66.591  1.00 96.63  ? 67  ASP   F C   1 
ATOM   9784  O  O   . ASP   F  6  71  ? 14.501  -111.371 66.051  1.00 95.09  ? 67  ASP   F O   1 
ATOM   9785  C  CB  . ASP   F  6  71  ? 18.205  -111.512 66.486  1.00 97.26  ? 67  ASP   F CB  1 
ATOM   9786  C  CG  . ASP   F  6  71  ? 18.649  -112.963 66.553  1.00 102.40 ? 67  ASP   F CG  1 
ATOM   9787  O  OD1 . ASP   F  6  71  ? 17.917  -113.770 67.162  1.00 109.47 ? 67  ASP   F OD1 1 
ATOM   9788  O  OD2 . ASP   F  6  71  ? 19.720  -113.276 65.985  1.00 98.83  ? 67  ASP   F OD2 1 
ATOM   9789  N  N   . ARG   F  6  72  ? 15.739  -112.069 67.836  1.00 95.51  ? 68  ARG   F N   1 
ATOM   9790  C  CA  . ARG   F  6  72  ? 14.587  -112.329 68.742  1.00 97.91  ? 68  ARG   F CA  1 
ATOM   9791  C  C   . ARG   F  6  72  ? 14.785  -111.624 70.092  1.00 97.79  ? 68  ARG   F C   1 
ATOM   9792  O  O   . ARG   F  6  72  ? 13.829  -111.643 70.894  1.00 101.49 ? 68  ARG   F O   1 
ATOM   9793  C  CB  . ARG   F  6  72  ? 14.381  -113.844 68.881  1.00 98.83  ? 68  ARG   F CB  1 
ATOM   9794  C  CG  . ARG   F  6  72  ? 13.288  -114.402 67.975  1.00 100.21 ? 68  ARG   F CG  1 
ATOM   9795  C  CD  . ARG   F  6  72  ? 13.696  -115.564 67.083  1.00 102.20 ? 68  ARG   F CD  1 
ATOM   9796  N  NE  . ARG   F  6  72  ? 13.417  -116.876 67.659  1.00 105.06 ? 68  ARG   F NE  1 
ATOM   9797  C  CZ  . ARG   F  6  72  ? 13.240  -118.002 66.964  1.00 104.98 ? 68  ARG   F CZ  1 
ATOM   9798  N  NH1 . ARG   F  6  72  ? 13.297  -118.002 65.642  1.00 102.75 ? 68  ARG   F NH1 1 
ATOM   9799  N  NH2 . ARG   F  6  72  ? 12.994  -119.135 67.600  1.00 107.80 ? 68  ARG   F NH2 1 
ATOM   9800  N  N   . HIS   F  6  73  ? 15.942  -110.985 70.319  1.00 97.22  ? 69  HIS   F N   1 
ATOM   9801  C  CA  . HIS   F  6  73  ? 16.380  -110.488 71.654  1.00 98.38  ? 69  HIS   F CA  1 
ATOM   9802  C  C   . HIS   F  6  73  ? 16.734  -108.994 71.641  1.00 97.92  ? 69  HIS   F C   1 
ATOM   9803  O  O   . HIS   F  6  73  ? 17.017  -108.479 72.740  1.00 103.09 ? 69  HIS   F O   1 
ATOM   9804  C  CB  . HIS   F  6  73  ? 17.564  -111.319 72.173  1.00 95.75  ? 69  HIS   F CB  1 
ATOM   9805  C  CG  . HIS   F  6  73  ? 18.827  -111.134 71.401  1.00 91.89  ? 69  HIS   F CG  1 
ATOM   9806  N  ND1 . HIS   F  6  73  ? 18.937  -111.483 70.069  1.00 90.82  ? 69  HIS   F ND1 1 
ATOM   9807  C  CD2 . HIS   F  6  73  ? 20.035  -110.657 71.769  1.00 90.90  ? 69  HIS   F CD2 1 
ATOM   9808  C  CE1 . HIS   F  6  73  ? 20.157  -111.221 69.647  1.00 90.43  ? 69  HIS   F CE1 1 
ATOM   9809  N  NE2 . HIS   F  6  73  ? 20.850  -110.713 70.672  1.00 90.83  ? 69  HIS   F NE2 1 
ATOM   9810  N  N   . ILE   F  6  74  ? 16.727  -108.327 70.477  1.00 96.06  ? 70  ILE   F N   1 
ATOM   9811  C  CA  . ILE   F  6  74  ? 17.108  -106.886 70.334  1.00 93.06  ? 70  ILE   F CA  1 
ATOM   9812  C  C   . ILE   F  6  74  ? 15.894  -106.081 69.854  1.00 93.33  ? 70  ILE   F C   1 
ATOM   9813  O  O   . ILE   F  6  74  ? 15.180  -106.563 68.957  1.00 95.01  ? 70  ILE   F O   1 
ATOM   9814  C  CB  . ILE   F  6  74  ? 18.304  -106.705 69.377  1.00 89.62  ? 70  ILE   F CB  1 
ATOM   9815  C  CG1 . ILE   F  6  74  ? 19.494  -107.586 69.768  1.00 87.63  ? 70  ILE   F CG1 1 
ATOM   9816  C  CG2 . ILE   F  6  74  ? 18.703  -105.239 69.289  1.00 90.39  ? 70  ILE   F CG2 1 
ATOM   9817  C  CD1 . ILE   F  6  74  ? 20.531  -107.732 68.679  1.00 86.28  ? 70  ILE   F CD1 1 
ATOM   9818  N  N   . GLY   F  6  75  ? 15.704  -104.886 70.420  1.00 93.59  ? 71  GLY   F N   1 
ATOM   9819  C  CA  . GLY   F  6  75  ? 14.699  -103.895 69.989  1.00 96.74  ? 71  GLY   F CA  1 
ATOM   9820  C  C   . GLY   F  6  75  ? 15.366  -102.614 69.517  1.00 96.77  ? 71  GLY   F C   1 
ATOM   9821  O  O   . GLY   F  6  75  ? 16.372  -102.214 70.139  1.00 94.94  ? 71  GLY   F O   1 
ATOM   9822  N  N   . CYS   F  6  76  ? 14.833  -101.994 68.458  1.00 98.50  ? 72  CYS   F N   1 
ATOM   9823  C  CA  . CYS   F  6  76  ? 15.357  -100.740 67.851  1.00 97.19  ? 72  CYS   F CA  1 
ATOM   9824  C  C   . CYS   F  6  76  ? 14.232  -99.715  67.702  1.00 97.01  ? 72  CYS   F C   1 
ATOM   9825  O  O   . CYS   F  6  76  ? 13.133  -100.092 67.251  1.00 97.73  ? 72  CYS   F O   1 
ATOM   9826  C  CB  . CYS   F  6  76  ? 15.974  -100.983 66.479  1.00 97.98  ? 72  CYS   F CB  1 
ATOM   9827  S  SG  . CYS   F  6  76  ? 17.331  -102.182 66.491  1.00 100.35 ? 72  CYS   F SG  1 
ATOM   9828  N  N   . VAL   F  6  77  ? 14.518  -98.464  68.065  1.00 95.13  ? 73  VAL   F N   1 
ATOM   9829  C  CA  . VAL   F  6  77  ? 13.631  -97.290  67.829  1.00 93.84  ? 73  VAL   F CA  1 
ATOM   9830  C  C   . VAL   F  6  77  ? 14.516  -96.116  67.400  1.00 91.90  ? 73  VAL   F C   1 
ATOM   9831  O  O   . VAL   F  6  77  ? 15.673  -96.043  67.861  1.00 83.68  ? 73  VAL   F O   1 
ATOM   9832  C  CB  . VAL   F  6  77  ? 12.789  -96.963  69.076  1.00 94.33  ? 73  VAL   F CB  1 
ATOM   9833  C  CG1 . VAL   F  6  77  ? 13.621  -96.332  70.182  1.00 93.49  ? 73  VAL   F CG1 1 
ATOM   9834  C  CG2 . VAL   F  6  77  ? 11.601  -96.085  68.726  1.00 95.03  ? 73  VAL   F CG2 1 
ATOM   9835  N  N   . TYR   F  6  78  ? 13.999  -95.240  66.537  1.00 94.21  ? 74  TYR   F N   1 
ATOM   9836  C  CA  . TYR   F  6  78  ? 14.773  -94.124  65.937  1.00 96.65  ? 74  TYR   F CA  1 
ATOM   9837  C  C   . TYR   F  6  78  ? 13.870  -92.911  65.696  1.00 98.72  ? 74  TYR   F C   1 
ATOM   9838  O  O   . TYR   F  6  78  ? 12.638  -93.068  65.569  1.00 107.95 ? 74  TYR   F O   1 
ATOM   9839  C  CB  . TYR   F  6  78  ? 15.449  -94.582  64.644  1.00 96.33  ? 74  TYR   F CB  1 
ATOM   9840  C  CG  . TYR   F  6  78  ? 14.608  -95.487  63.779  1.00 95.65  ? 74  TYR   F CG  1 
ATOM   9841  C  CD1 . TYR   F  6  78  ? 13.599  -94.978  62.978  1.00 97.51  ? 74  TYR   F CD1 1 
ATOM   9842  C  CD2 . TYR   F  6  78  ? 14.820  -96.856  63.759  1.00 95.61  ? 74  TYR   F CD2 1 
ATOM   9843  C  CE1 . TYR   F  6  78  ? 12.823  -95.803  62.180  1.00 95.53  ? 74  TYR   F CE1 1 
ATOM   9844  C  CE2 . TYR   F  6  78  ? 14.054  -97.695  62.967  1.00 95.27  ? 74  TYR   F CE2 1 
ATOM   9845  C  CZ  . TYR   F  6  78  ? 13.051  -97.167  62.173  1.00 95.46  ? 74  TYR   F CZ  1 
ATOM   9846  O  OH  . TYR   F  6  78  ? 12.289  -97.980  61.386  1.00 95.62  ? 74  TYR   F OH  1 
ATOM   9847  N  N   . SER   F  6  79  ? 14.497  -91.733  65.646  1.00 97.20  ? 75  SER   F N   1 
ATOM   9848  C  CA  . SER   F  6  79  ? 13.876  -90.424  65.324  1.00 95.03  ? 75  SER   F CA  1 
ATOM   9849  C  C   . SER   F  6  79  ? 14.533  -89.869  64.060  1.00 91.56  ? 75  SER   F C   1 
ATOM   9850  O  O   . SER   F  6  79  ? 15.747  -90.094  63.883  1.00 86.17  ? 75  SER   F O   1 
ATOM   9851  C  CB  . SER   F  6  79  ? 14.011  -89.464  66.474  1.00 93.85  ? 75  SER   F CB  1 
ATOM   9852  O  OG  . SER   F  6  79  ? 13.346  -89.959  67.625  1.00 95.44  ? 75  SER   F OG  1 
ATOM   9853  N  N   . GLY   F  6  80  ? 13.754  -89.178  63.224  1.00 91.01  ? 76  GLY   F N   1 
ATOM   9854  C  CA  . GLY   F  6  80  ? 14.221  -88.547  61.975  1.00 93.03  ? 76  GLY   F CA  1 
ATOM   9855  C  C   . GLY   F  6  80  ? 13.533  -89.144  60.761  1.00 92.94  ? 76  GLY   F C   1 
ATOM   9856  O  O   . GLY   F  6  80  ? 12.317  -89.422  60.851  1.00 93.23  ? 76  GLY   F O   1 
ATOM   9857  N  N   . LEU   F  6  81  ? 14.279  -89.340  59.668  1.00 92.27  ? 77  LEU   F N   1 
ATOM   9858  C  CA  . LEU   F  6  81  ? 13.766  -89.943  58.408  1.00 93.64  ? 77  LEU   F CA  1 
ATOM   9859  C  C   . LEU   F  6  81  ? 13.478  -91.427  58.665  1.00 92.55  ? 77  LEU   F C   1 
ATOM   9860  O  O   . LEU   F  6  81  ? 14.441  -92.203  58.782  1.00 92.48  ? 77  LEU   F O   1 
ATOM   9861  C  CB  . LEU   F  6  81  ? 14.793  -89.772  57.283  1.00 93.19  ? 77  LEU   F CB  1 
ATOM   9862  C  CG  . LEU   F  6  81  ? 15.284  -88.352  57.010  1.00 93.34  ? 77  LEU   F CG  1 
ATOM   9863  C  CD1 . LEU   F  6  81  ? 16.151  -88.328  55.762  1.00 94.54  ? 77  LEU   F CD1 1 
ATOM   9864  C  CD2 . LEU   F  6  81  ? 14.125  -87.376  56.869  1.00 95.42  ? 77  LEU   F CD2 1 
ATOM   9865  N  N   . ILE   F  6  82  ? 12.201  -91.803  58.746  1.00 95.20  ? 78  ILE   F N   1 
ATOM   9866  C  CA  . ILE   F  6  82  ? 11.760  -93.175  59.141  1.00 96.92  ? 78  ILE   F CA  1 
ATOM   9867  C  C   . ILE   F  6  82  ? 12.316  -94.202  58.153  1.00 98.22  ? 78  ILE   F C   1 
ATOM   9868  O  O   . ILE   F  6  82  ? 12.852  -95.221  58.583  1.00 101.28 ? 78  ILE   F O   1 
ATOM   9869  C  CB  . ILE   F  6  82  ? 10.224  -93.243  59.292  1.00 99.70  ? 78  ILE   F CB  1 
ATOM   9870  C  CG1 . ILE   F  6  82  ? 9.721   -92.319  60.406  1.00 104.52 ? 78  ILE   F CG1 1 
ATOM   9871  C  CG2 . ILE   F  6  82  ? 9.752   -94.673  59.501  1.00 99.81  ? 78  ILE   F CG2 1 
ATOM   9872  C  CD1 . ILE   F  6  82  ? 10.385  -92.535  61.752  1.00 105.03 ? 78  ILE   F CD1 1 
ATOM   9873  N  N   . PRO   F  6  83  ? 12.214  -93.999  56.817  1.00 94.55  ? 79  PRO   F N   1 
ATOM   9874  C  CA  . PRO   F  6  83  ? 12.812  -94.926  55.853  1.00 94.69  ? 79  PRO   F CA  1 
ATOM   9875  C  C   . PRO   F  6  83  ? 14.301  -95.220  56.095  1.00 97.92  ? 79  PRO   F C   1 
ATOM   9876  O  O   . PRO   F  6  83  ? 14.681  -96.365  55.961  1.00 104.44 ? 79  PRO   F O   1 
ATOM   9877  C  CB  . PRO   F  6  83  ? 12.618  -94.217  54.505  1.00 91.69  ? 79  PRO   F CB  1 
ATOM   9878  C  CG  . PRO   F  6  83  ? 11.369  -93.396  54.716  1.00 93.39  ? 79  PRO   F CG  1 
ATOM   9879  C  CD  . PRO   F  6  83  ? 11.472  -92.917  56.150  1.00 96.01  ? 79  PRO   F CD  1 
ATOM   9880  N  N   . ASP   F  6  84  ? 15.096  -94.202  56.445  1.00 96.54  ? 80  ASP   F N   1 
ATOM   9881  C  CA  . ASP   F  6  84  ? 16.549  -94.342  56.750  1.00 99.44  ? 80  ASP   F CA  1 
ATOM   9882  C  C   . ASP   F  6  84  ? 16.748  -95.283  57.944  1.00 93.74  ? 80  ASP   F C   1 
ATOM   9883  O  O   . ASP   F  6  84  ? 17.747  -96.027  57.942  1.00 97.53  ? 80  ASP   F O   1 
ATOM   9884  C  CB  . ASP   F  6  84  ? 17.212  -92.993  57.040  1.00 100.55 ? 80  ASP   F CB  1 
ATOM   9885  C  CG  . ASP   F  6  84  ? 17.713  -92.270  55.804  1.00 106.39 ? 80  ASP   F CG  1 
ATOM   9886  O  OD1 . ASP   F  6  84  ? 17.142  -92.497  54.717  1.00 111.14 ? 80  ASP   F OD1 1 
ATOM   9887  O  OD2 . ASP   F  6  84  ? 18.674  -91.485  55.938  1.00 105.77 ? 80  ASP   F OD2 1 
ATOM   9888  N  N   . GLY   F  6  85  ? 15.850  -95.227  58.933  1.00 91.61  ? 81  GLY   F N   1 
ATOM   9889  C  CA  . GLY   F  6  85  ? 15.860  -96.116  60.110  1.00 91.54  ? 81  GLY   F CA  1 
ATOM   9890  C  C   . GLY   F  6  85  ? 15.599  -97.560  59.718  1.00 91.23  ? 81  GLY   F C   1 
ATOM   9891  O  O   . GLY   F  6  85  ? 16.326  -98.443  60.209  1.00 90.36  ? 81  GLY   F O   1 
ATOM   9892  N  N   . ARG   F  6  86  ? 14.605  -97.794  58.855  1.00 87.94  ? 82  ARG   F N   1 
ATOM   9893  C  CA  . ARG   F  6  86  ? 14.236  -99.148  58.360  1.00 91.08  ? 82  ARG   F CA  1 
ATOM   9894  C  C   . ARG   F  6  86  ? 15.425  -99.767  57.613  1.00 93.91  ? 82  ARG   F C   1 
ATOM   9895  O  O   . ARG   F  6  86  ? 15.679  -100.975 57.822  1.00 94.62  ? 82  ARG   F O   1 
ATOM   9896  C  CB  . ARG   F  6  86  ? 12.992  -99.093  57.468  1.00 90.36  ? 82  ARG   F CB  1 
ATOM   9897  C  CG  . ARG   F  6  86  ? 11.680  -99.091  58.240  1.00 93.20  ? 82  ARG   F CG  1 
ATOM   9898  C  CD  . ARG   F  6  86  ? 10.480  -99.345  57.347  1.00 96.22  ? 82  ARG   F CD  1 
ATOM   9899  N  NE  . ARG   F  6  86  ? 10.641  -100.552 56.546  1.00 97.12  ? 82  ARG   F NE  1 
ATOM   9900  C  CZ  . ARG   F  6  86  ? 10.479  -101.796 56.990  1.00 101.31 ? 82  ARG   F CZ  1 
ATOM   9901  N  NH1 . ARG   F  6  86  ? 10.136  -102.026 58.247  1.00 103.86 ? 82  ARG   F NH1 1 
ATOM   9902  N  NH2 . ARG   F  6  86  ? 10.663  -102.814 56.166  1.00 100.47 ? 82  ARG   F NH2 1 
ATOM   9903  N  N   . HIS   F  6  87  ? 16.121  -98.977  56.785  1.00 91.52  ? 83  HIS   F N   1 
ATOM   9904  C  CA  . HIS   F  6  87  ? 17.344  -99.398  56.048  1.00 93.44  ? 83  HIS   F CA  1 
ATOM   9905  C  C   . HIS   F  6  87  ? 18.397  -99.905  57.040  1.00 95.16  ? 83  HIS   F C   1 
ATOM   9906  O  O   . HIS   F  6  87  ? 19.020  -100.945 56.753  1.00 101.28 ? 83  HIS   F O   1 
ATOM   9907  C  CB  . HIS   F  6  87  ? 17.906  -98.257  55.188  1.00 91.86  ? 83  HIS   F CB  1 
ATOM   9908  C  CG  . HIS   F  6  87  ? 19.142  -98.628  54.440  1.00 95.82  ? 83  HIS   F CG  1 
ATOM   9909  N  ND1 . HIS   F  6  87  ? 19.117  -99.005  53.110  1.00 100.68 ? 83  HIS   F ND1 1 
ATOM   9910  C  CD2 . HIS   F  6  87  ? 20.434  -98.698  54.828  1.00 97.50  ? 83  HIS   F CD2 1 
ATOM   9911  C  CE1 . HIS   F  6  87  ? 20.343  -99.286  52.712  1.00 102.78 ? 83  HIS   F CE1 1 
ATOM   9912  N  NE2 . HIS   F  6  87  ? 21.169  -99.103  53.747  1.00 101.96 ? 83  HIS   F NE2 1 
ATOM   9913  N  N   . LEU   F  6  88  ? 18.585  -99.196  58.156  1.00 93.81  ? 84  LEU   F N   1 
ATOM   9914  C  CA  . LEU   F  6  88  ? 19.608  -99.525  59.186  1.00 97.80  ? 84  LEU   F CA  1 
ATOM   9915  C  C   . LEU   F  6  88  ? 19.229  -100.835 59.896  1.00 94.82  ? 84  LEU   F C   1 
ATOM   9916  O  O   . LEU   F  6  88  ? 20.143  -101.646 60.149  1.00 92.25  ? 84  LEU   F O   1 
ATOM   9917  C  CB  . LEU   F  6  88  ? 19.734  -98.353  60.168  1.00 100.51 ? 84  LEU   F CB  1 
ATOM   9918  C  CG  . LEU   F  6  88  ? 20.920  -98.409  61.132  1.00 103.14 ? 84  LEU   F CG  1 
ATOM   9919  C  CD1 . LEU   F  6  88  ? 22.237  -98.601  60.392  1.00 102.87 ? 84  LEU   F CD1 1 
ATOM   9920  C  CD2 . LEU   F  6  88  ? 20.977  -97.152  61.987  1.00 105.41 ? 84  LEU   F CD2 1 
ATOM   9921  N  N   . VAL   F  6  89  ? 17.938  -101.046 60.185  1.00 91.96  ? 85  VAL   F N   1 
ATOM   9922  C  CA  . VAL   F  6  89  ? 17.415  -102.273 60.862  1.00 91.11  ? 85  VAL   F CA  1 
ATOM   9923  C  C   . VAL   F  6  89  ? 17.557  -103.470 59.912  1.00 93.74  ? 85  VAL   F C   1 
ATOM   9924  O  O   . VAL   F  6  89  ? 17.958  -104.552 60.387  1.00 93.03  ? 85  VAL   F O   1 
ATOM   9925  C  CB  . VAL   F  6  89  ? 15.956  -102.097 61.330  1.00 90.34  ? 85  VAL   F CB  1 
ATOM   9926  C  CG1 . VAL   F  6  89  ? 15.339  -103.416 61.772  1.00 92.05  ? 85  VAL   F CG1 1 
ATOM   9927  C  CG2 . VAL   F  6  89  ? 15.847  -101.068 62.443  1.00 88.94  ? 85  VAL   F CG2 1 
ATOM   9928  N  N   . ASN   F  6  90  ? 17.223  -103.291 58.629  1.00 92.46  ? 86  ASN   F N   1 
ATOM   9929  C  CA  . ASN   F  6  90  ? 17.366  -104.337 57.578  1.00 92.46  ? 86  ASN   F CA  1 
ATOM   9930  C  C   . ASN   F  6  90  ? 18.811  -104.841 57.556  1.00 93.18  ? 86  ASN   F C   1 
ATOM   9931  O  O   . ASN   F  6  90  ? 19.004  -106.068 57.488  1.00 96.80  ? 86  ASN   F O   1 
ATOM   9932  C  CB  . ASN   F  6  90  ? 16.951  -103.832 56.193  1.00 91.65  ? 86  ASN   F CB  1 
ATOM   9933  C  CG  . ASN   F  6  90  ? 15.451  -103.737 56.014  1.00 93.96  ? 86  ASN   F CG  1 
ATOM   9934  O  OD1 . ASN   F  6  90  ? 14.952  -102.777 55.433  1.00 96.30  ? 86  ASN   F OD1 1 
ATOM   9935  N  ND2 . ASN   F  6  90  ? 14.718  -104.729 56.496  1.00 100.42 ? 86  ASN   F ND2 1 
ATOM   9936  N  N   . ARG   F  6  91  ? 19.782  -103.926 57.616  1.00 89.28  ? 87  ARG   F N   1 
ATOM   9937  C  CA  . ARG   F  6  91  ? 21.226  -104.258 57.710  1.00 88.42  ? 87  ARG   F CA  1 
ATOM   9938  C  C   . ARG   F  6  91  ? 21.488  -104.972 59.038  1.00 87.93  ? 87  ARG   F C   1 
ATOM   9939  O  O   . ARG   F  6  91  ? 22.160  -106.020 59.020  1.00 86.73  ? 87  ARG   F O   1 
ATOM   9940  C  CB  . ARG   F  6  91  ? 22.080  -102.992 57.605  1.00 86.03  ? 87  ARG   F CB  1 
ATOM   9941  C  CG  . ARG   F  6  91  ? 23.573  -103.250 57.732  1.00 84.94  ? 87  ARG   F CG  1 
ATOM   9942  C  CD  . ARG   F  6  91  ? 24.126  -103.990 56.534  1.00 86.98  ? 87  ARG   F CD  1 
ATOM   9943  N  NE  . ARG   F  6  91  ? 25.539  -104.270 56.723  1.00 85.37  ? 87  ARG   F NE  1 
ATOM   9944  C  CZ  . ARG   F  6  91  ? 26.402  -104.533 55.749  1.00 86.22  ? 87  ARG   F CZ  1 
ATOM   9945  N  NH1 . ARG   F  6  91  ? 26.008  -104.546 54.486  1.00 87.84  ? 87  ARG   F NH1 1 
ATOM   9946  N  NH2 . ARG   F  6  91  ? 27.667  -104.778 56.046  1.00 88.06  ? 87  ARG   F NH2 1 
ATOM   9947  N  N   . GLY   F  6  92  ? 20.986  -104.406 60.141  1.00 91.75  ? 88  GLY   F N   1 
ATOM   9948  C  CA  . GLY   F  6  92  ? 21.092  -104.974 61.499  1.00 91.75  ? 88  GLY   F CA  1 
ATOM   9949  C  C   . GLY   F  6  92  ? 20.663  -106.430 61.539  1.00 92.26  ? 88  GLY   F C   1 
ATOM   9950  O  O   . GLY   F  6  92  ? 21.334  -107.220 62.232  1.00 91.65  ? 88  GLY   F O   1 
ATOM   9951  N  N   . ARG   F  6  93  ? 19.590  -106.771 60.817  1.00 91.39  ? 89  ARG   F N   1 
ATOM   9952  C  CA  . ARG   F  6  93  ? 19.028  -108.147 60.733  1.00 89.41  ? 89  ARG   F CA  1 
ATOM   9953  C  C   . ARG   F  6  93  ? 19.964  -109.049 59.919  1.00 86.23  ? 89  ARG   F C   1 
ATOM   9954  O  O   . ARG   F  6  93  ? 20.144  -110.214 60.319  1.00 87.11  ? 89  ARG   F O   1 
ATOM   9955  C  CB  . ARG   F  6  93  ? 17.616  -108.105 60.144  1.00 93.45  ? 89  ARG   F CB  1 
ATOM   9956  C  CG  . ARG   F  6  93  ? 16.588  -107.516 61.098  1.00 97.29  ? 89  ARG   F CG  1 
ATOM   9957  C  CD  . ARG   F  6  93  ? 15.303  -107.077 60.425  1.00 98.02  ? 89  ARG   F CD  1 
ATOM   9958  N  NE  . ARG   F  6  93  ? 14.308  -106.664 61.408  1.00 96.84  ? 89  ARG   F NE  1 
ATOM   9959  C  CZ  . ARG   F  6  93  ? 13.104  -106.178 61.121  1.00 94.89  ? 89  ARG   F CZ  1 
ATOM   9960  N  NH1 . ARG   F  6  93  ? 12.723  -106.031 59.862  1.00 93.47  ? 89  ARG   F NH1 1 
ATOM   9961  N  NH2 . ARG   F  6  93  ? 12.282  -105.837 62.099  1.00 96.02  ? 89  ARG   F NH2 1 
ATOM   9962  N  N   . GLU   F  6  94  ? 20.533  -108.534 58.825  1.00 84.31  ? 90  GLU   F N   1 
ATOM   9963  C  CA  . GLU   F  6  94  ? 21.517  -109.261 57.978  1.00 86.57  ? 90  GLU   F CA  1 
ATOM   9964  C  C   . GLU   F  6  94  ? 22.788  -109.546 58.788  1.00 88.55  ? 90  GLU   F C   1 
ATOM   9965  O  O   . GLU   F  6  94  ? 23.313  -110.671 58.670  1.00 89.15  ? 90  GLU   F O   1 
ATOM   9966  C  CB  . GLU   F  6  94  ? 21.851  -108.464 56.716  1.00 88.84  ? 90  GLU   F CB  1 
ATOM   9967  C  CG  . GLU   F  6  94  ? 20.757  -108.506 55.666  1.00 94.63  ? 90  GLU   F CG  1 
ATOM   9968  C  CD  . GLU   F  6  94  ? 20.961  -107.552 54.502  1.00 100.00 ? 90  GLU   F CD  1 
ATOM   9969  O  OE1 . GLU   F  6  94  ? 22.129  -107.247 54.187  1.00 110.79 ? 90  GLU   F OE1 1 
ATOM   9970  O  OE2 . GLU   F  6  94  ? 19.950  -107.114 53.915  1.00 107.53 ? 90  GLU   F OE2 1 
ATOM   9971  N  N   . GLU   F  6  95  ? 23.264  -108.567 59.567  1.00 88.16  ? 91  GLU   F N   1 
ATOM   9972  C  CA  . GLU   F  6  95  ? 24.484  -108.686 60.416  1.00 89.94  ? 91  GLU   F CA  1 
ATOM   9973  C  C   . GLU   F  6  95  ? 24.257  -109.765 61.486  1.00 86.78  ? 91  GLU   F C   1 
ATOM   9974  O  O   . GLU   F  6  95  ? 25.142  -110.633 61.651  1.00 81.20  ? 91  GLU   F O   1 
ATOM   9975  C  CB  . GLU   F  6  95  ? 24.837  -107.346 61.073  1.00 90.77  ? 91  GLU   F CB  1 
ATOM   9976  C  CG  . GLU   F  6  95  ? 25.275  -106.261 60.097  1.00 92.98  ? 91  GLU   F CG  1 
ATOM   9977  C  CD  . GLU   F  6  95  ? 26.688  -106.369 59.541  1.00 92.78  ? 91  GLU   F CD  1 
ATOM   9978  O  OE1 . GLU   F  6  95  ? 27.307  -107.444 59.675  1.00 96.65  ? 91  GLU   F OE1 1 
ATOM   9979  O  OE2 . GLU   F  6  95  ? 27.170  -105.368 58.971  1.00 92.17  ? 91  GLU   F OE2 1 
ATOM   9980  N  N   . ALA   F  6  96  ? 23.113  -109.706 62.178  1.00 86.88  ? 92  ALA   F N   1 
ATOM   9981  C  CA  . ALA   F  6  96  ? 22.732  -110.597 63.301  1.00 84.30  ? 92  ALA   F CA  1 
ATOM   9982  C  C   . ALA   F  6  96  ? 22.564  -112.039 62.810  1.00 87.26  ? 92  ALA   F C   1 
ATOM   9983  O  O   . ALA   F  6  96  ? 22.913  -112.964 63.577  1.00 84.60  ? 92  ALA   F O   1 
ATOM   9984  C  CB  . ALA   F  6  96  ? 21.463  -110.099 63.946  1.00 83.18  ? 92  ALA   F CB  1 
ATOM   9985  N  N   . ALA   F  6  97  ? 22.026  -112.214 61.597  1.00 86.03  ? 93  ALA   F N   1 
ATOM   9986  C  CA  . ALA   F  6  97  ? 21.776  -113.525 60.953  1.00 85.77  ? 93  ALA   F CA  1 
ATOM   9987  C  C   . ALA   F  6  97  ? 23.110  -114.209 60.623  1.00 88.66  ? 93  ALA   F C   1 
ATOM   9988  O  O   . ALA   F  6  97  ? 23.247  -115.408 60.945  1.00 89.42  ? 93  ALA   F O   1 
ATOM   9989  C  CB  . ALA   F  6  97  ? 20.919  -113.352 59.722  1.00 82.56  ? 93  ALA   F CB  1 
ATOM   9990  N  N   . SER   F  6  98  ? 24.059  -113.482 60.021  1.00 89.16  ? 94  SER   F N   1 
ATOM   9991  C  CA  . SER   F  6  98  ? 25.388  -114.017 59.615  1.00 88.94  ? 94  SER   F CA  1 
ATOM   9992  C  C   . SER   F  6  98  ? 26.212  -114.365 60.861  1.00 92.20  ? 94  SER   F C   1 
ATOM   9993  O  O   . SER   F  6  98  ? 27.001  -115.324 60.781  1.00 93.51  ? 94  SER   F O   1 
ATOM   9994  C  CB  . SER   F  6  98  ? 26.137  -113.068 58.714  1.00 90.17  ? 94  SER   F CB  1 
ATOM   9995  O  OG  . SER   F  6  98  ? 27.019  -112.246 59.464  1.00 90.92  ? 94  SER   F OG  1 
ATOM   9996  N  N   . PHE   F  6  99  ? 26.044  -113.612 61.957  1.00 93.99  ? 95  PHE   F N   1 
ATOM   9997  C  CA  . PHE   F  6  99  ? 26.706  -113.865 63.266  1.00 93.63  ? 95  PHE   F CA  1 
ATOM   9998  C  C   . PHE   F  6  99  ? 26.187  -115.186 63.845  1.00 94.46  ? 95  PHE   F C   1 
ATOM   9999  O  O   . PHE   F  6  99  ? 27.019  -116.039 64.216  1.00 97.42  ? 95  PHE   F O   1 
ATOM   10000 C  CB  . PHE   F  6  99  ? 26.487  -112.708 64.248  1.00 93.76  ? 95  PHE   F CB  1 
ATOM   10001 C  CG  . PHE   F  6  99  ? 27.339  -112.785 65.492  1.00 93.29  ? 95  PHE   F CG  1 
ATOM   10002 C  CD1 . PHE   F  6  99  ? 26.944  -113.548 66.580  1.00 92.38  ? 95  PHE   F CD1 1 
ATOM   10003 C  CD2 . PHE   F  6  99  ? 28.546  -112.106 65.567  1.00 91.46  ? 95  PHE   F CD2 1 
ATOM   10004 C  CE1 . PHE   F  6  99  ? 27.735  -113.628 67.716  1.00 93.84  ? 95  PHE   F CE1 1 
ATOM   10005 C  CE2 . PHE   F  6  99  ? 29.335  -112.186 66.704  1.00 93.45  ? 95  PHE   F CE2 1 
ATOM   10006 C  CZ  . PHE   F  6  99  ? 28.928  -112.946 67.777  1.00 94.82  ? 95  PHE   F CZ  1 
ATOM   10007 N  N   . LYS   F  6  100 ? 24.860  -115.348 63.910  1.00 90.57  ? 96  LYS   F N   1 
ATOM   10008 C  CA  . LYS   F  6  100 ? 24.189  -116.569 64.442  1.00 89.55  ? 96  LYS   F CA  1 
ATOM   10009 C  C   . LYS   F  6  100 ? 24.527  -117.770 63.544  1.00 88.84  ? 96  LYS   F C   1 
ATOM   10010 O  O   . LYS   F  6  100 ? 24.684  -118.878 64.086  1.00 83.85  ? 96  LYS   F O   1 
ATOM   10011 C  CB  . LYS   F  6  100 ? 22.679  -116.336 64.583  1.00 90.60  ? 96  LYS   F CB  1 
ATOM   10012 C  CG  . LYS   F  6  100 ? 21.832  -117.577 64.847  1.00 91.78  ? 96  LYS   F CG  1 
ATOM   10013 C  CD  . LYS   F  6  100 ? 21.040  -117.538 66.144  1.00 96.44  ? 96  LYS   F CD  1 
ATOM   10014 C  CE  . LYS   F  6  100 ? 19.940  -116.495 66.172  1.00 99.75  ? 96  LYS   F CE  1 
ATOM   10015 N  NZ  . LYS   F  6  100 ? 18.724  -116.943 65.453  1.00 103.24 ? 96  LYS   F NZ  1 
ATOM   10016 N  N   . LYS   F  6  101 ? 24.662  -117.554 62.232  1.00 90.05  ? 97  LYS   F N   1 
ATOM   10017 C  CA  . LYS   F  6  101 ? 24.988  -118.615 61.240  1.00 89.41  ? 97  LYS   F CA  1 
ATOM   10018 C  C   . LYS   F  6  101 ? 26.369  -119.209 61.548  1.00 90.31  ? 97  LYS   F C   1 
ATOM   10019 O  O   . LYS   F  6  101 ? 26.468  -120.445 61.637  1.00 87.06  ? 97  LYS   F O   1 
ATOM   10020 C  CB  . LYS   F  6  101 ? 24.959  -118.052 59.816  1.00 92.48  ? 97  LYS   F CB  1 
ATOM   10021 C  CG  . LYS   F  6  101 ? 25.046  -119.093 58.709  1.00 96.33  ? 97  LYS   F CG  1 
ATOM   10022 C  CD  . LYS   F  6  101 ? 25.019  -118.495 57.317  1.00 102.41 ? 97  LYS   F CD  1 
ATOM   10023 C  CE  . LYS   F  6  101 ? 24.919  -119.532 56.216  1.00 104.65 ? 97  LYS   F CE  1 
ATOM   10024 N  NZ  . LYS   F  6  101 ? 26.137  -120.373 56.125  1.00 105.60 ? 97  LYS   F NZ  1 
ATOM   10025 N  N   . LEU   F  6  102 ? 27.388  -118.360 61.700  1.00 90.13  ? 98  LEU   F N   1 
ATOM   10026 C  CA  . LEU   F  6  102 ? 28.811  -118.775 61.833  1.00 91.92  ? 98  LEU   F CA  1 
ATOM   10027 C  C   . LEU   F  6  102 ? 29.107  -119.204 63.278  1.00 94.34  ? 98  LEU   F C   1 
ATOM   10028 O  O   . LEU   F  6  102 ? 29.802  -120.226 63.448  1.00 96.13  ? 98  LEU   F O   1 
ATOM   10029 C  CB  . LEU   F  6  102 ? 29.715  -117.618 61.388  1.00 94.60  ? 98  LEU   F CB  1 
ATOM   10030 C  CG  . LEU   F  6  102 ? 31.223  -117.854 61.495  1.00 96.84  ? 98  LEU   F CG  1 
ATOM   10031 C  CD1 . LEU   F  6  102 ? 31.655  -119.095 60.724  1.00 97.44  ? 98  LEU   F CD1 1 
ATOM   10032 C  CD2 . LEU   F  6  102 ? 31.997  -116.639 61.007  1.00 98.01  ? 98  LEU   F CD2 1 
ATOM   10033 N  N   . TYR   F  6  103 ? 28.603  -118.464 64.274  1.00 92.06  ? 99  TYR   F N   1 
ATOM   10034 C  CA  . TYR   F  6  103 ? 28.999  -118.596 65.704  1.00 91.39  ? 99  TYR   F CA  1 
ATOM   10035 C  C   . TYR   F  6  103 ? 27.908  -119.272 66.549  1.00 87.32  ? 99  TYR   F C   1 
ATOM   10036 O  O   . TYR   F  6  103 ? 28.174  -119.500 67.742  1.00 85.97  ? 99  TYR   F O   1 
ATOM   10037 C  CB  . TYR   F  6  103 ? 29.365  -117.223 66.276  1.00 91.26  ? 99  TYR   F CB  1 
ATOM   10038 C  CG  . TYR   F  6  103 ? 30.461  -116.511 65.523  1.00 90.47  ? 99  TYR   F CG  1 
ATOM   10039 C  CD1 . TYR   F  6  103 ? 31.682  -117.123 65.288  1.00 90.31  ? 99  TYR   F CD1 1 
ATOM   10040 C  CD2 . TYR   F  6  103 ? 30.283  -115.223 65.045  1.00 92.15  ? 99  TYR   F CD2 1 
ATOM   10041 C  CE1 . TYR   F  6  103 ? 32.695  -116.479 64.595  1.00 89.46  ? 99  TYR   F CE1 1 
ATOM   10042 C  CE2 . TYR   F  6  103 ? 31.286  -114.563 64.351  1.00 93.21  ? 99  TYR   F CE2 1 
ATOM   10043 C  CZ  . TYR   F  6  103 ? 32.499  -115.193 64.126  1.00 88.32  ? 99  TYR   F CZ  1 
ATOM   10044 O  OH  . TYR   F  6  103 ? 33.503  -114.572 63.442  1.00 85.06  ? 99  TYR   F OH  1 
ATOM   10045 N  N   . LYS   F  6  104 ? 26.735  -119.565 65.975  1.00 87.59  ? 100 LYS   F N   1 
ATOM   10046 C  CA  . LYS   F  6  104 ? 25.623  -120.326 66.617  1.00 90.53  ? 100 LYS   F CA  1 
ATOM   10047 C  C   . LYS   F  6  104 ? 24.871  -119.446 67.627  1.00 93.39  ? 100 LYS   F C   1 
ATOM   10048 O  O   . LYS   F  6  104 ? 23.633  -119.359 67.513  1.00 97.27  ? 100 LYS   F O   1 
ATOM   10049 C  CB  . LYS   F  6  104 ? 26.134  -121.598 67.304  1.00 91.47  ? 100 LYS   F CB  1 
ATOM   10050 C  CG  . LYS   F  6  104 ? 25.049  -122.553 67.786  1.00 97.31  ? 100 LYS   F CG  1 
ATOM   10051 C  CD  . LYS   F  6  104 ? 24.288  -123.230 66.661  1.00 100.63 ? 100 LYS   F CD  1 
ATOM   10052 C  CE  . LYS   F  6  104 ? 23.453  -124.407 67.123  1.00 105.82 ? 100 LYS   F CE  1 
ATOM   10053 N  NZ  . LYS   F  6  104 ? 22.269  -123.972 67.902  1.00 106.24 ? 100 LYS   F NZ  1 
ATOM   10054 N  N   . THR   F  6  105 ? 25.577  -118.862 68.600  1.00 93.09  ? 101 THR   F N   1 
ATOM   10055 C  CA  . THR   F  6  105 ? 24.998  -117.995 69.667  1.00 94.11  ? 101 THR   F CA  1 
ATOM   10056 C  C   . THR   F  6  105 ? 24.381  -116.745 69.037  1.00 92.09  ? 101 THR   F C   1 
ATOM   10057 O  O   . THR   F  6  105 ? 24.921  -116.214 68.068  1.00 88.80  ? 101 THR   F O   1 
ATOM   10058 C  CB  . THR   F  6  105 ? 26.040  -117.656 70.745  1.00 96.44  ? 101 THR   F CB  1 
ATOM   10059 O  OG1 . THR   F  6  105 ? 25.416  -116.788 71.692  1.00 103.03 ? 101 THR   F OG1 1 
ATOM   10060 C  CG2 . THR   F  6  105 ? 27.293  -116.997 70.208  1.00 97.02  ? 101 THR   F CG2 1 
ATOM   10061 N  N   . PRO   F  6  106 ? 23.224  -116.249 69.542  1.00 91.71  ? 102 PRO   F N   1 
ATOM   10062 C  CA  . PRO   F  6  106 ? 22.675  -114.961 69.111  1.00 94.02  ? 102 PRO   F CA  1 
ATOM   10063 C  C   . PRO   F  6  106 ? 23.651  -113.807 69.387  1.00 96.48  ? 102 PRO   F C   1 
ATOM   10064 O  O   . PRO   F  6  106 ? 24.349  -113.875 70.383  1.00 101.32 ? 102 PRO   F O   1 
ATOM   10065 C  CB  . PRO   F  6  106 ? 21.400  -114.790 69.952  1.00 93.66  ? 102 PRO   F CB  1 
ATOM   10066 C  CG  . PRO   F  6  106 ? 21.032  -116.198 70.360  1.00 93.46  ? 102 PRO   F CG  1 
ATOM   10067 C  CD  . PRO   F  6  106 ? 22.357  -116.911 70.530  1.00 93.03  ? 102 PRO   F CD  1 
ATOM   10068 N  N   . ILE   F  6  107 ? 23.667  -112.789 68.518  1.00 97.64  ? 103 ILE   F N   1 
ATOM   10069 C  CA  . ILE   F  6  107 ? 24.678  -111.687 68.536  1.00 93.46  ? 103 ILE   F CA  1 
ATOM   10070 C  C   . ILE   F  6  107 ? 24.578  -110.912 69.850  1.00 90.06  ? 103 ILE   F C   1 
ATOM   10071 O  O   . ILE   F  6  107 ? 23.505  -110.432 70.207  1.00 89.53  ? 103 ILE   F O   1 
ATOM   10072 C  CB  . ILE   F  6  107 ? 24.540  -110.765 67.306  1.00 93.61  ? 103 ILE   F CB  1 
ATOM   10073 C  CG1 . ILE   F  6  107 ? 25.675  -109.738 67.267  1.00 93.69  ? 103 ILE   F CG1 1 
ATOM   10074 C  CG2 . ILE   F  6  107 ? 23.173  -110.092 67.246  1.00 97.07  ? 103 ILE   F CG2 1 
ATOM   10075 C  CD1 . ILE   F  6  107 ? 25.948  -109.172 65.896  1.00 93.77  ? 103 ILE   F CD1 1 
ATOM   10076 N  N   . PRO   F  6  108 ? 25.683  -110.791 70.625  1.00 88.99  ? 104 PRO   F N   1 
ATOM   10077 C  CA  . PRO   F  6  108 ? 25.731  -109.893 71.783  1.00 91.40  ? 104 PRO   F CA  1 
ATOM   10078 C  C   . PRO   F  6  108 ? 25.460  -108.430 71.399  1.00 88.50  ? 104 PRO   F C   1 
ATOM   10079 O  O   . PRO   F  6  108 ? 25.764  -108.054 70.283  1.00 89.38  ? 104 PRO   F O   1 
ATOM   10080 C  CB  . PRO   F  6  108 ? 27.166  -110.052 72.312  1.00 92.18  ? 104 PRO   F CB  1 
ATOM   10081 C  CG  . PRO   F  6  108 ? 27.585  -111.418 71.829  1.00 92.57  ? 104 PRO   F CG  1 
ATOM   10082 C  CD  . PRO   F  6  108 ? 26.927  -111.559 70.472  1.00 91.52  ? 104 PRO   F CD  1 
ATOM   10083 N  N   . ILE   F  6  109 ? 24.921  -107.643 72.334  1.00 86.58  ? 105 ILE   F N   1 
ATOM   10084 C  CA  . ILE   F  6  109 ? 24.433  -106.257 72.066  1.00 86.21  ? 105 ILE   F CA  1 
ATOM   10085 C  C   . ILE   F  6  109 ? 25.623  -105.367 71.700  1.00 84.72  ? 105 ILE   F C   1 
ATOM   10086 O  O   . ILE   F  6  109 ? 25.533  -104.609 70.737  1.00 79.26  ? 105 ILE   F O   1 
ATOM   10087 C  CB  . ILE   F  6  109 ? 23.606  -105.684 73.239  1.00 87.15  ? 105 ILE   F CB  1 
ATOM   10088 C  CG1 . ILE   F  6  109 ? 22.622  -106.700 73.829  1.00 89.47  ? 105 ILE   F CG1 1 
ATOM   10089 C  CG2 . ILE   F  6  109 ? 22.887  -104.418 72.803  1.00 87.22  ? 105 ILE   F CG2 1 
ATOM   10090 C  CD1 . ILE   F  6  109 ? 21.632  -107.263 72.833  1.00 90.87  ? 105 ILE   F CD1 1 
ATOM   10091 N  N   . PRO   F  6  110 ? 26.769  -105.418 72.425  1.00 86.36  ? 106 PRO   F N   1 
ATOM   10092 C  CA  . PRO   F  6  110 ? 27.945  -104.627 72.051  1.00 86.24  ? 106 PRO   F CA  1 
ATOM   10093 C  C   . PRO   F  6  110 ? 28.456  -104.956 70.641  1.00 84.59  ? 106 PRO   F C   1 
ATOM   10094 O  O   . PRO   F  6  110 ? 28.778  -104.046 69.911  1.00 88.62  ? 106 PRO   F O   1 
ATOM   10095 C  CB  . PRO   F  6  110 ? 29.004  -104.998 73.102  1.00 87.23  ? 106 PRO   F CB  1 
ATOM   10096 C  CG  . PRO   F  6  110 ? 28.194  -105.493 74.280  1.00 88.97  ? 106 PRO   F CG  1 
ATOM   10097 C  CD  . PRO   F  6  110 ? 27.000  -106.190 73.658  1.00 89.04  ? 106 PRO   F CD  1 
ATOM   10098 N  N   . ALA   F  6  111 ? 28.520  -106.243 70.301  1.00 82.39  ? 107 ALA   F N   1 
ATOM   10099 C  CA  . ALA   F  6  111 ? 28.889  -106.740 68.956  1.00 83.26  ? 107 ALA   F CA  1 
ATOM   10100 C  C   . ALA   F  6  111 ? 27.929  -106.150 67.918  1.00 80.60  ? 107 ALA   F C   1 
ATOM   10101 O  O   . ALA   F  6  111 ? 28.417  -105.647 66.888  1.00 78.71  ? 107 ALA   F O   1 
ATOM   10102 C  CB  . ALA   F  6  111 ? 28.860  -108.247 68.932  1.00 82.83  ? 107 ALA   F CB  1 
ATOM   10103 N  N   . PHE   F  6  112 ? 26.621  -106.210 68.194  1.00 81.16  ? 108 PHE   F N   1 
ATOM   10104 C  CA  . PHE   F  6  112 ? 25.542  -105.700 67.307  1.00 82.86  ? 108 PHE   F CA  1 
ATOM   10105 C  C   . PHE   F  6  112 ? 25.665  -104.180 67.166  1.00 84.47  ? 108 PHE   F C   1 
ATOM   10106 O  O   . PHE   F  6  112 ? 25.454  -103.670 66.049  1.00 90.51  ? 108 PHE   F O   1 
ATOM   10107 C  CB  . PHE   F  6  112 ? 24.151  -106.065 67.831  1.00 81.65  ? 108 PHE   F CB  1 
ATOM   10108 C  CG  . PHE   F  6  112 ? 23.031  -105.436 67.041  1.00 81.32  ? 108 PHE   F CG  1 
ATOM   10109 C  CD1 . PHE   F  6  112 ? 22.768  -105.851 65.745  1.00 84.55  ? 108 PHE   F CD1 1 
ATOM   10110 C  CD2 . PHE   F  6  112 ? 22.265  -104.409 67.571  1.00 80.64  ? 108 PHE   F CD2 1 
ATOM   10111 C  CE1 . PHE   F  6  112 ? 21.753  -105.263 65.006  1.00 84.94  ? 108 PHE   F CE1 1 
ATOM   10112 C  CE2 . PHE   F  6  112 ? 21.247  -103.826 66.831  1.00 79.40  ? 108 PHE   F CE2 1 
ATOM   10113 C  CZ  . PHE   F  6  112 ? 20.993  -104.253 65.549  1.00 81.80  ? 108 PHE   F CZ  1 
ATOM   10114 N  N   . ALA   F  6  113 ? 25.984  -103.484 68.262  1.00 84.81  ? 109 ALA   F N   1 
ATOM   10115 C  CA  . ALA   F  6  113 ? 26.124  -102.010 68.301  1.00 85.21  ? 109 ALA   F CA  1 
ATOM   10116 C  C   . ALA   F  6  113 ? 27.209  -101.581 67.308  1.00 84.84  ? 109 ALA   F C   1 
ATOM   10117 O  O   . ALA   F  6  113 ? 26.951  -100.643 66.532  1.00 88.45  ? 109 ALA   F O   1 
ATOM   10118 C  CB  . ALA   F  6  113 ? 26.427  -101.534 69.702  1.00 83.29  ? 109 ALA   F CB  1 
ATOM   10119 N  N   . ASP   F  6  114 ? 28.360  -102.261 67.307  1.00 84.29  ? 110 ASP   F N   1 
ATOM   10120 C  CA  . ASP   F  6  114 ? 29.510  -101.903 66.436  1.00 85.59  ? 110 ASP   F CA  1 
ATOM   10121 C  C   . ASP   F  6  114 ? 29.165  -102.224 64.978  1.00 90.36  ? 110 ASP   F C   1 
ATOM   10122 O  O   . ASP   F  6  114 ? 29.633  -101.478 64.098  1.00 93.29  ? 110 ASP   F O   1 
ATOM   10123 C  CB  . ASP   F  6  114 ? 30.808  -102.593 66.859  1.00 86.08  ? 110 ASP   F CB  1 
ATOM   10124 C  CG  . ASP   F  6  114 ? 32.044  -101.906 66.303  1.00 87.62  ? 110 ASP   F CG  1 
ATOM   10125 O  OD1 . ASP   F  6  114 ? 32.130  -100.666 66.420  1.00 89.90  ? 110 ASP   F OD1 1 
ATOM   10126 O  OD2 . ASP   F  6  114 ? 32.901  -102.609 65.740  1.00 91.57  ? 110 ASP   F OD2 1 
ATOM   10127 N  N   . ARG   F  6  115 ? 28.376  -103.276 64.731  1.00 91.56  ? 111 ARG   F N   1 
ATOM   10128 C  CA  . ARG   F  6  115 ? 27.926  -103.662 63.364  1.00 94.18  ? 111 ARG   F CA  1 
ATOM   10129 C  C   . ARG   F  6  115 ? 27.149  -102.499 62.734  1.00 90.68  ? 111 ARG   F C   1 
ATOM   10130 O  O   . ARG   F  6  115 ? 27.445  -102.160 61.570  1.00 92.21  ? 111 ARG   F O   1 
ATOM   10131 C  CB  . ARG   F  6  115 ? 27.055  -104.924 63.384  1.00 96.33  ? 111 ARG   F CB  1 
ATOM   10132 C  CG  . ARG   F  6  115 ? 27.796  -106.205 63.737  1.00 96.28  ? 111 ARG   F CG  1 
ATOM   10133 C  CD  . ARG   F  6  115 ? 28.907  -106.548 62.762  1.00 98.53  ? 111 ARG   F CD  1 
ATOM   10134 N  NE  . ARG   F  6  115 ? 29.609  -107.765 63.157  1.00 100.89 ? 111 ARG   F NE  1 
ATOM   10135 C  CZ  . ARG   F  6  115 ? 29.359  -108.994 62.704  1.00 102.57 ? 111 ARG   F CZ  1 
ATOM   10136 N  NH1 . ARG   F  6  115 ? 28.411  -109.213 61.805  1.00 105.21 ? 111 ARG   F NH1 1 
ATOM   10137 N  NH2 . ARG   F  6  115 ? 30.072  -110.013 63.155  1.00 100.86 ? 111 ARG   F NH2 1 
ATOM   10138 N  N   . LEU   F  6  116 ? 26.189  -101.924 63.467  1.00 88.54  ? 112 LEU   F N   1 
ATOM   10139 C  CA  . LEU   F  6  116 ? 25.442  -100.713 63.032  1.00 87.03  ? 112 LEU   F CA  1 
ATOM   10140 C  C   . LEU   F  6  116 ? 26.421  -99.536  62.940  1.00 86.45  ? 112 LEU   F C   1 
ATOM   10141 O  O   . LEU   F  6  116 ? 26.359  -98.799  61.940  1.00 88.93  ? 112 LEU   F O   1 
ATOM   10142 C  CB  . LEU   F  6  116 ? 24.312  -100.399 64.019  1.00 88.83  ? 112 LEU   F CB  1 
ATOM   10143 C  CG  . LEU   F  6  116 ? 23.169  -101.412 64.110  1.00 91.01  ? 112 LEU   F CG  1 
ATOM   10144 C  CD1 . LEU   F  6  116 ? 22.060  -100.871 65.001  1.00 93.79  ? 112 LEU   F CD1 1 
ATOM   10145 C  CD2 . LEU   F  6  116 ? 22.610  -101.758 62.738  1.00 92.08  ? 112 LEU   F CD2 1 
ATOM   10146 N  N   . GLY   F  6  117 ? 27.294  -99.385  63.942  1.00 82.54  ? 113 GLY   F N   1 
ATOM   10147 C  CA  . GLY   F  6  117 ? 28.248  -98.264  64.060  1.00 84.70  ? 113 GLY   F CA  1 
ATOM   10148 C  C   . GLY   F  6  117 ? 29.174  -98.175  62.861  1.00 84.98  ? 113 GLY   F C   1 
ATOM   10149 O  O   . GLY   F  6  117 ? 29.290  -97.079  62.281  1.00 85.44  ? 113 GLY   F O   1 
ATOM   10150 N  N   . GLN   F  6  118 ? 29.806  -99.291  62.496  1.00 83.90  ? 114 GLN   F N   1 
ATOM   10151 C  CA  . GLN   F  6  118 ? 30.747  -99.378  61.348  1.00 84.00  ? 114 GLN   F CA  1 
ATOM   10152 C  C   . GLN   F  6  118 ? 30.004  -99.073  60.043  1.00 82.43  ? 114 GLN   F C   1 
ATOM   10153 O  O   . GLN   F  6  118 ? 30.604  -98.409  59.172  1.00 81.11  ? 114 GLN   F O   1 
ATOM   10154 C  CB  . GLN   F  6  118 ? 31.382  -100.765 61.278  1.00 84.66  ? 114 GLN   F CB  1 
ATOM   10155 C  CG  . GLN   F  6  118 ? 32.270  -101.091 62.469  1.00 87.56  ? 114 GLN   F CG  1 
ATOM   10156 C  CD  . GLN   F  6  118 ? 33.549  -100.293 62.483  1.00 89.57  ? 114 GLN   F CD  1 
ATOM   10157 O  OE1 . GLN   F  6  118 ? 33.906  -99.624  61.514  1.00 97.39  ? 114 GLN   F OE1 1 
ATOM   10158 N  NE2 . GLN   F  6  118 ? 34.259  -100.366 63.596  1.00 91.06  ? 114 GLN   F NE2 1 
ATOM   10159 N  N   . TYR   F  6  119 ? 28.760  -99.549  59.915  1.00 82.01  ? 115 TYR   F N   1 
ATOM   10160 C  CA  . TYR   F  6  119 ? 27.907  -99.380  58.708  1.00 83.17  ? 115 TYR   F CA  1 
ATOM   10161 C  C   . TYR   F  6  119 ? 27.575  -97.895  58.510  1.00 82.35  ? 115 TYR   F C   1 
ATOM   10162 O  O   . TYR   F  6  119 ? 27.750  -97.385  57.387  1.00 84.55  ? 115 TYR   F O   1 
ATOM   10163 C  CB  . TYR   F  6  119 ? 26.630  -100.216 58.814  1.00 81.70  ? 115 TYR   F CB  1 
ATOM   10164 C  CG  . TYR   F  6  119 ? 25.823  -100.274 57.542  1.00 82.08  ? 115 TYR   F CG  1 
ATOM   10165 C  CD1 . TYR   F  6  119 ? 26.301  -100.944 56.427  1.00 82.41  ? 115 TYR   F CD1 1 
ATOM   10166 C  CD2 . TYR   F  6  119 ? 24.581  -99.663  57.449  1.00 81.07  ? 115 TYR   F CD2 1 
ATOM   10167 C  CE1 . TYR   F  6  119 ? 25.570  -101.005 55.252  1.00 83.18  ? 115 TYR   F CE1 1 
ATOM   10168 C  CE2 . TYR   F  6  119 ? 23.837  -99.716  56.282  1.00 81.05  ? 115 TYR   F CE2 1 
ATOM   10169 C  CZ  . TYR   F  6  119 ? 24.333  -100.388 55.180  1.00 82.95  ? 115 TYR   F CZ  1 
ATOM   10170 O  OH  . TYR   F  6  119 ? 23.602  -100.439 54.030  1.00 82.72  ? 115 TYR   F OH  1 
ATOM   10171 N  N   . VAL   F  6  120 ? 27.108  -97.227  59.570  1.00 81.52  ? 116 VAL   F N   1 
ATOM   10172 C  CA  . VAL   F  6  120 ? 26.732  -95.781  59.551  1.00 81.13  ? 116 VAL   F CA  1 
ATOM   10173 C  C   . VAL   F  6  120 ? 27.997  -94.944  59.316  1.00 79.79  ? 116 VAL   F C   1 
ATOM   10174 O  O   . VAL   F  6  120 ? 27.926  -93.994  58.515  1.00 80.64  ? 116 VAL   F O   1 
ATOM   10175 C  CB  . VAL   F  6  120 ? 25.994  -95.372  60.841  1.00 81.32  ? 116 VAL   F CB  1 
ATOM   10176 C  CG1 . VAL   F  6  120 ? 25.868  -93.862  60.981  1.00 82.01  ? 116 VAL   F CG1 1 
ATOM   10177 C  CG2 . VAL   F  6  120 ? 24.623  -96.024  60.923  1.00 83.37  ? 116 VAL   F CG2 1 
ATOM   10178 N  N   . GLN   F  6  121 ? 29.107  -95.290  59.978  1.00 78.30  ? 117 GLN   F N   1 
ATOM   10179 C  CA  . GLN   F  6  121 ? 30.422  -94.605  59.825  1.00 78.80  ? 117 GLN   F CA  1 
ATOM   10180 C  C   . GLN   F  6  121 ? 30.873  -94.693  58.363  1.00 77.57  ? 117 GLN   F C   1 
ATOM   10181 O  O   . GLN   F  6  121 ? 31.492  -93.737  57.881  1.00 74.55  ? 117 GLN   F O   1 
ATOM   10182 C  CB  . GLN   F  6  121 ? 31.473  -95.225  60.747  1.00 81.39  ? 117 GLN   F CB  1 
ATOM   10183 C  CG  . GLN   F  6  121 ? 32.778  -94.434  60.824  1.00 81.87  ? 117 GLN   F CG  1 
ATOM   10184 C  CD  . GLN   F  6  121 ? 33.787  -94.700  59.728  1.00 80.82  ? 117 GLN   F CD  1 
ATOM   10185 O  OE1 . GLN   F  6  121 ? 34.613  -93.849  59.412  1.00 84.91  ? 117 GLN   F OE1 1 
ATOM   10186 N  NE2 . GLN   F  6  121 ? 33.765  -95.890  59.151  1.00 85.94  ? 117 GLN   F NE2 1 
ATOM   10187 N  N   . ALA   F  6  122 ? 30.577  -95.810  57.692  1.00 84.16  ? 118 ALA   F N   1 
ATOM   10188 C  CA  . ALA   F  6  122 ? 30.955  -96.070  56.283  1.00 87.88  ? 118 ALA   F CA  1 
ATOM   10189 C  C   . ALA   F  6  122 ? 30.247  -95.075  55.354  1.00 93.49  ? 118 ALA   F C   1 
ATOM   10190 O  O   . ALA   F  6  122 ? 30.798  -94.797  54.269  1.00 102.96 ? 118 ALA   F O   1 
ATOM   10191 C  CB  . ALA   F  6  122 ? 30.638  -97.497  55.911  1.00 88.32  ? 118 ALA   F CB  1 
ATOM   10192 N  N   . HIS   F  6  123 ? 29.083  -94.557  55.764  1.00 91.70  ? 119 HIS   F N   1 
ATOM   10193 C  CA  . HIS   F  6  123 ? 28.267  -93.577  54.994  1.00 92.66  ? 119 HIS   F CA  1 
ATOM   10194 C  C   . HIS   F  6  123 ? 28.723  -92.135  55.266  1.00 93.05  ? 119 HIS   F C   1 
ATOM   10195 O  O   . HIS   F  6  123 ? 27.986  -91.206  54.868  1.00 92.89  ? 119 HIS   F O   1 
ATOM   10196 C  CB  . HIS   F  6  123 ? 26.774  -93.775  55.293  1.00 94.17  ? 119 HIS   F CB  1 
ATOM   10197 C  CG  . HIS   F  6  123 ? 26.193  -94.978  54.634  1.00 93.01  ? 119 HIS   F CG  1 
ATOM   10198 N  ND1 . HIS   F  6  123 ? 26.449  -96.256  55.081  1.00 92.48  ? 119 HIS   F ND1 1 
ATOM   10199 C  CD2 . HIS   F  6  123 ? 25.384  -95.104  53.561  1.00 95.18  ? 119 HIS   F CD2 1 
ATOM   10200 C  CE1 . HIS   F  6  123 ? 25.817  -97.121  54.316  1.00 96.49  ? 119 HIS   F CE1 1 
ATOM   10201 N  NE2 . HIS   F  6  123 ? 25.156  -96.439  53.375  1.00 94.76  ? 119 HIS   F NE2 1 
ATOM   10202 N  N   . THR   F  6  124 ? 29.880  -91.946  55.913  1.00 88.50  ? 120 THR   F N   1 
ATOM   10203 C  CA  . THR   F  6  124 ? 30.552  -90.627  56.076  1.00 86.57  ? 120 THR   F CA  1 
ATOM   10204 C  C   . THR   F  6  124 ? 31.901  -90.625  55.341  1.00 83.23  ? 120 THR   F C   1 
ATOM   10205 O  O   . THR   F  6  124 ? 32.582  -89.590  55.403  1.00 79.89  ? 120 THR   F O   1 
ATOM   10206 C  CB  . THR   F  6  124 ? 30.750  -90.265  57.556  1.00 83.76  ? 120 THR   F CB  1 
ATOM   10207 O  OG1 . THR   F  6  124 ? 31.816  -91.053  58.084  1.00 84.10  ? 120 THR   F OG1 1 
ATOM   10208 C  CG2 . THR   F  6  124 ? 29.504  -90.456  58.395  1.00 84.92  ? 120 THR   F CG2 1 
ATOM   10209 N  N   . LEU   F  6  125 ? 32.270  -91.724  54.670  1.00 86.30  ? 121 LEU   F N   1 
ATOM   10210 C  CA  . LEU   F  6  125 ? 33.622  -91.925  54.069  1.00 89.95  ? 121 LEU   F CA  1 
ATOM   10211 C  C   . LEU   F  6  125 ? 33.653  -91.458  52.607  1.00 93.17  ? 121 LEU   F C   1 
ATOM   10212 O  O   . LEU   F  6  125 ? 34.765  -91.159  52.124  1.00 98.22  ? 121 LEU   F O   1 
ATOM   10213 C  CB  . LEU   F  6  125 ? 34.019  -93.405  54.148  1.00 91.70  ? 121 LEU   F CB  1 
ATOM   10214 C  CG  . LEU   F  6  125 ? 34.383  -93.952  55.529  1.00 88.03  ? 121 LEU   F CG  1 
ATOM   10215 C  CD1 . LEU   F  6  125 ? 34.630  -95.448  55.447  1.00 88.16  ? 121 LEU   F CD1 1 
ATOM   10216 C  CD2 . LEU   F  6  125 ? 35.606  -93.252  56.106  1.00 88.13  ? 121 LEU   F CD2 1 
ATOM   10217 N  N   . TYR   F  6  126 ? 32.504  -91.428  51.920  1.00 93.08  ? 122 TYR   F N   1 
ATOM   10218 C  CA  . TYR   F  6  126 ? 32.406  -91.191  50.453  1.00 90.72  ? 122 TYR   F CA  1 
ATOM   10219 C  C   . TYR   F  6  126 ? 31.406  -90.068  50.158  1.00 88.52  ? 122 TYR   F C   1 
ATOM   10220 O  O   . TYR   F  6  126 ? 30.445  -89.890  50.933  1.00 83.95  ? 122 TYR   F O   1 
ATOM   10221 C  CB  . TYR   F  6  126 ? 31.995  -92.476  49.726  1.00 90.40  ? 122 TYR   F CB  1 
ATOM   10222 C  CG  . TYR   F  6  126 ? 32.672  -93.726  50.228  1.00 91.43  ? 122 TYR   F CG  1 
ATOM   10223 C  CD1 . TYR   F  6  126 ? 33.925  -94.096  49.767  1.00 90.61  ? 122 TYR   F CD1 1 
ATOM   10224 C  CD2 . TYR   F  6  126 ? 32.063  -94.536  51.173  1.00 90.85  ? 122 TYR   F CD2 1 
ATOM   10225 C  CE1 . TYR   F  6  126 ? 34.555  -95.241  50.228  1.00 92.58  ? 122 TYR   F CE1 1 
ATOM   10226 C  CE2 . TYR   F  6  126 ? 32.678  -95.684  51.645  1.00 93.47  ? 122 TYR   F CE2 1 
ATOM   10227 C  CZ  . TYR   F  6  126 ? 33.930  -96.038  51.172  1.00 94.82  ? 122 TYR   F CZ  1 
ATOM   10228 O  OH  . TYR   F  6  126 ? 34.541  -97.169  51.631  1.00 95.98  ? 122 TYR   F OH  1 
ATOM   10229 N  N   . ASN   F  6  127 ? 31.630  -89.349  49.053  1.00 89.22  ? 123 ASN   F N   1 
ATOM   10230 C  CA  . ASN   F  6  127 ? 30.751  -88.251  48.559  1.00 89.89  ? 123 ASN   F CA  1 
ATOM   10231 C  C   . ASN   F  6  127 ? 29.624  -88.809  47.679  1.00 88.45  ? 123 ASN   F C   1 
ATOM   10232 O  O   . ASN   F  6  127 ? 28.800  -88.000  47.215  1.00 87.83  ? 123 ASN   F O   1 
ATOM   10233 C  CB  . ASN   F  6  127 ? 31.538  -87.155  47.829  1.00 93.89  ? 123 ASN   F CB  1 
ATOM   10234 C  CG  . ASN   F  6  127 ? 32.228  -87.564  46.539  1.00 98.15  ? 123 ASN   F CG  1 
ATOM   10235 O  OD1 . ASN   F  6  127 ? 32.893  -86.734  45.926  1.00 102.65 ? 123 ASN   F OD1 1 
ATOM   10236 N  ND2 . ASN   F  6  127 ? 32.097  -88.807  46.098  1.00 101.12 ? 123 ASN   F ND2 1 
ATOM   10237 N  N   . SER   F  6  128 ? 29.590  -90.128  47.453  1.00 86.93  ? 124 SER   F N   1 
ATOM   10238 C  CA  . SER   F  6  128 ? 28.607  -90.814  46.573  1.00 87.35  ? 124 SER   F CA  1 
ATOM   10239 C  C   . SER   F  6  128 ? 27.457  -91.404  47.398  1.00 86.80  ? 124 SER   F C   1 
ATOM   10240 O  O   . SER   F  6  128 ? 26.507  -91.920  46.787  1.00 88.73  ? 124 SER   F O   1 
ATOM   10241 C  CB  . SER   F  6  128 ? 29.281  -91.869  45.736  1.00 84.49  ? 124 SER   F CB  1 
ATOM   10242 O  OG  . SER   F  6  128 ? 30.010  -92.768  46.553  1.00 84.51  ? 124 SER   F OG  1 
ATOM   10243 N  N   . VAL   F  6  129 ? 27.532  -91.330  48.730  1.00 88.78  ? 125 VAL   F N   1 
ATOM   10244 C  CA  . VAL   F  6  129 ? 26.423  -91.735  49.645  1.00 93.51  ? 125 VAL   F CA  1 
ATOM   10245 C  C   . VAL   F  6  129 ? 26.091  -90.571  50.582  1.00 91.50  ? 125 VAL   F C   1 
ATOM   10246 O  O   . VAL   F  6  129 ? 26.965  -89.706  50.808  1.00 91.34  ? 125 VAL   F O   1 
ATOM   10247 C  CB  . VAL   F  6  129 ? 26.744  -93.011  50.448  1.00 95.60  ? 125 VAL   F CB  1 
ATOM   10248 C  CG1 . VAL   F  6  129 ? 26.658  -94.254  49.579  1.00 97.65  ? 125 VAL   F CG1 1 
ATOM   10249 C  CG2 . VAL   F  6  129 ? 28.089  -92.933  51.157  1.00 96.96  ? 125 VAL   F CG2 1 
ATOM   10250 N  N   . ARG   F  6  130 ? 24.860  -90.579  51.097  1.00 91.93  ? 126 ARG   F N   1 
ATOM   10251 C  CA  . ARG   F  6  130 ? 24.316  -89.591  52.062  1.00 90.78  ? 126 ARG   F CA  1 
ATOM   10252 C  C   . ARG   F  6  130 ? 24.404  -90.189  53.463  1.00 94.65  ? 126 ARG   F C   1 
ATOM   10253 O  O   . ARG   F  6  130 ? 24.131  -91.373  53.641  1.00 100.83 ? 126 ARG   F O   1 
ATOM   10254 C  CB  . ARG   F  6  130 ? 22.871  -89.264  51.682  1.00 85.35  ? 126 ARG   F CB  1 
ATOM   10255 C  CG  . ARG   F  6  130 ? 22.142  -88.371  52.673  1.00 85.86  ? 126 ARG   F CG  1 
ATOM   10256 C  CD  . ARG   F  6  130 ? 20.735  -88.064  52.204  1.00 84.80  ? 126 ARG   F CD  1 
ATOM   10257 N  NE  . ARG   F  6  130 ? 19.928  -89.257  51.972  1.00 83.59  ? 126 ARG   F NE  1 
ATOM   10258 C  CZ  . ARG   F  6  130 ? 19.289  -89.947  52.912  1.00 83.24  ? 126 ARG   F CZ  1 
ATOM   10259 N  NH1 . ARG   F  6  130 ? 19.364  -89.589  54.183  1.00 84.09  ? 126 ARG   F NH1 1 
ATOM   10260 N  NH2 . ARG   F  6  130 ? 18.578  -91.006  52.576  1.00 86.74  ? 126 ARG   F NH2 1 
ATOM   10261 N  N   . PRO   F  6  131 ? 24.793  -89.409  54.499  1.00 95.31  ? 127 PRO   F N   1 
ATOM   10262 C  CA  . PRO   F  6  131 ? 24.715  -89.879  55.882  1.00 93.42  ? 127 PRO   F CA  1 
ATOM   10263 C  C   . PRO   F  6  131 ? 23.281  -90.263  56.267  1.00 93.15  ? 127 PRO   F C   1 
ATOM   10264 O  O   . PRO   F  6  131 ? 22.361  -89.803  55.619  1.00 89.94  ? 127 PRO   F O   1 
ATOM   10265 C  CB  . PRO   F  6  131 ? 25.171  -88.670  56.710  1.00 93.01  ? 127 PRO   F CB  1 
ATOM   10266 C  CG  . PRO   F  6  131 ? 26.025  -87.871  55.752  1.00 94.26  ? 127 PRO   F CG  1 
ATOM   10267 C  CD  . PRO   F  6  131 ? 25.359  -88.055  54.404  1.00 94.95  ? 127 PRO   F CD  1 
ATOM   10268 N  N   . PHE   F  6  132 ? 23.127  -91.089  57.304  1.00 95.14  ? 128 PHE   F N   1 
ATOM   10269 C  CA  . PHE   F  6  132 ? 21.802  -91.526  57.815  1.00 93.34  ? 128 PHE   F CA  1 
ATOM   10270 C  C   . PHE   F  6  132 ? 21.130  -90.345  58.520  1.00 94.60  ? 128 PHE   F C   1 
ATOM   10271 O  O   . PHE   F  6  132 ? 21.785  -89.693  59.351  1.00 94.98  ? 128 PHE   F O   1 
ATOM   10272 C  CB  . PHE   F  6  132 ? 21.939  -92.753  58.717  1.00 95.06  ? 128 PHE   F CB  1 
ATOM   10273 C  CG  . PHE   F  6  132 ? 22.145  -94.032  57.949  1.00 93.92  ? 128 PHE   F CG  1 
ATOM   10274 C  CD1 . PHE   F  6  132 ? 23.420  -94.469  57.631  1.00 94.99  ? 128 PHE   F CD1 1 
ATOM   10275 C  CD2 . PHE   F  6  132 ? 21.060  -94.773  57.507  1.00 94.19  ? 128 PHE   F CD2 1 
ATOM   10276 C  CE1 . PHE   F  6  132 ? 23.607  -95.636  56.908  1.00 96.81  ? 128 PHE   F CE1 1 
ATOM   10277 C  CE2 . PHE   F  6  132 ? 21.248  -95.939  56.784  1.00 96.07  ? 128 PHE   F CE2 1 
ATOM   10278 C  CZ  . PHE   F  6  132 ? 22.522  -96.370  56.487  1.00 98.13  ? 128 PHE   F CZ  1 
ATOM   10279 N  N   . GLY   F  6  133 ? 19.868  -90.082  58.171  1.00 93.41  ? 129 GLY   F N   1 
ATOM   10280 C  CA  . GLY   F  6  133 ? 19.032  -89.034  58.785  1.00 93.44  ? 129 GLY   F CA  1 
ATOM   10281 C  C   . GLY   F  6  133 ? 18.254  -89.573  59.973  1.00 93.04  ? 129 GLY   F C   1 
ATOM   10282 O  O   . GLY   F  6  133 ? 17.042  -89.290  60.058  1.00 90.39  ? 129 GLY   F O   1 
ATOM   10283 N  N   . VAL   F  6  134 ? 18.922  -90.331  60.851  1.00 94.80  ? 130 VAL   F N   1 
ATOM   10284 C  CA  . VAL   F  6  134 ? 18.322  -90.920  62.085  1.00 97.56  ? 130 VAL   F CA  1 
ATOM   10285 C  C   . VAL   F  6  134 ? 19.391  -91.031  63.177  1.00 100.01 ? 130 VAL   F C   1 
ATOM   10286 O  O   . VAL   F  6  134 ? 20.558  -91.339  62.853  1.00 102.45 ? 130 VAL   F O   1 
ATOM   10287 C  CB  . VAL   F  6  134 ? 17.677  -92.296  61.822  1.00 95.36  ? 130 VAL   F CB  1 
ATOM   10288 C  CG1 . VAL   F  6  134 ? 16.292  -92.171  61.212  1.00 96.47  ? 130 VAL   F CG1 1 
ATOM   10289 C  CG2 . VAL   F  6  134 ? 18.561  -93.196  60.970  1.00 95.06  ? 130 VAL   F CG2 1 
ATOM   10290 N  N   . SER   F  6  135 ? 18.985  -90.769  64.421  1.00 103.48 ? 131 SER   F N   1 
ATOM   10291 C  CA  . SER   F  6  135 ? 19.615  -91.292  65.660  1.00 104.55 ? 131 SER   F CA  1 
ATOM   10292 C  C   . SER   F  6  135 ? 18.800  -92.508  66.101  1.00 100.17 ? 131 SER   F C   1 
ATOM   10293 O  O   . SER   F  6  135 ? 17.561  -92.386  66.153  1.00 99.97  ? 131 SER   F O   1 
ATOM   10294 C  CB  . SER   F  6  135 ? 19.678  -90.249  66.748  1.00 103.42 ? 131 SER   F CB  1 
ATOM   10295 O  OG  . SER   F  6  135 ? 20.679  -89.281  66.474  1.00 108.61 ? 131 SER   F OG  1 
ATOM   10296 N  N   . THR   F  6  136 ? 19.455  -93.639  66.370  1.00 99.40  ? 132 THR   F N   1 
ATOM   10297 C  CA  . THR   F  6  136 ? 18.786  -94.922  66.716  1.00 96.50  ? 132 THR   F CA  1 
ATOM   10298 C  C   . THR   F  6  136 ? 19.122  -95.314  68.157  1.00 90.41  ? 132 THR   F C   1 
ATOM   10299 O  O   . THR   F  6  136 ? 20.318  -95.481  68.460  1.00 82.35  ? 132 THR   F O   1 
ATOM   10300 C  CB  . THR   F  6  136 ? 19.182  -96.050  65.756  1.00 97.35  ? 132 THR   F CB  1 
ATOM   10301 O  OG1 . THR   F  6  136 ? 19.006  -95.598  64.413  1.00 100.83 ? 132 THR   F OG1 1 
ATOM   10302 C  CG2 . THR   F  6  136 ? 18.373  -97.307  65.989  1.00 99.95  ? 132 THR   F CG2 1 
ATOM   10303 N  N   . ILE   F  6  137 ? 18.091  -95.453  68.996  1.00 93.36  ? 133 ILE   F N   1 
ATOM   10304 C  CA  . ILE   F  6  137 ? 18.176  -96.034  70.368  1.00 95.51  ? 133 ILE   F CA  1 
ATOM   10305 C  C   . ILE   F  6  137 ? 17.796  -97.514  70.268  1.00 96.05  ? 133 ILE   F C   1 
ATOM   10306 O  O   . ILE   F  6  137 ? 16.700  -97.814  69.757  1.00 95.46  ? 133 ILE   F O   1 
ATOM   10307 C  CB  . ILE   F  6  137 ? 17.273  -95.272  71.360  1.00 98.24  ? 133 ILE   F CB  1 
ATOM   10308 C  CG1 . ILE   F  6  137 ? 17.691  -93.805  71.499  1.00 100.46 ? 133 ILE   F CG1 1 
ATOM   10309 C  CG2 . ILE   F  6  137 ? 17.244  -95.977  72.709  1.00 98.78  ? 133 ILE   F CG2 1 
ATOM   10310 C  CD1 . ILE   F  6  137 ? 16.609  -92.907  72.054  1.00 102.98 ? 133 ILE   F CD1 1 
ATOM   10311 N  N   . PHE   F  6  138 ? 18.669  -98.400  70.744  1.00 93.60  ? 134 PHE   F N   1 
ATOM   10312 C  CA  . PHE   F  6  138 ? 18.508  -99.871  70.619  1.00 94.43  ? 134 PHE   F CA  1 
ATOM   10313 C  C   . PHE   F  6  138 ? 19.264  -100.579 71.746  1.00 94.68  ? 134 PHE   F C   1 
ATOM   10314 O  O   . PHE   F  6  138 ? 20.171  -99.981  72.362  1.00 91.01  ? 134 PHE   F O   1 
ATOM   10315 C  CB  . PHE   F  6  138 ? 19.015  -100.348 69.257  1.00 91.99  ? 134 PHE   F CB  1 
ATOM   10316 C  CG  . PHE   F  6  138 ? 20.499  -100.170 69.065  1.00 90.41  ? 134 PHE   F CG  1 
ATOM   10317 C  CD1 . PHE   F  6  138 ? 21.011  -98.965  68.613  1.00 91.57  ? 134 PHE   F CD1 1 
ATOM   10318 C  CD2 . PHE   F  6  138 ? 21.385  -101.196 69.362  1.00 85.18  ? 134 PHE   F CD2 1 
ATOM   10319 C  CE1 . PHE   F  6  138 ? 22.376  -98.795  68.446  1.00 91.31  ? 134 PHE   F CE1 1 
ATOM   10320 C  CE2 . PHE   F  6  138 ? 22.750  -101.025 69.193  1.00 83.50  ? 134 PHE   F CE2 1 
ATOM   10321 C  CZ  . PHE   F  6  138 ? 23.242  -99.826  68.735  1.00 86.30  ? 134 PHE   F CZ  1 
ATOM   10322 N  N   . GLY   F  6  139 ? 18.903  -101.840 71.977  1.00 95.18  ? 135 GLY   F N   1 
ATOM   10323 C  CA  . GLY   F  6  139 ? 19.495  -102.682 73.029  1.00 98.17  ? 135 GLY   F CA  1 
ATOM   10324 C  C   . GLY   F  6  139 ? 18.714  -103.968 73.226  1.00 100.96 ? 135 GLY   F C   1 
ATOM   10325 O  O   . GLY   F  6  139 ? 17.769  -104.223 72.452  1.00 101.83 ? 135 GLY   F O   1 
ATOM   10326 N  N   . GLY   F  6  140 ? 19.097  -104.743 74.240  1.00 102.51 ? 136 GLY   F N   1 
ATOM   10327 C  CA  . GLY   F  6  140 ? 18.467  -106.029 74.582  1.00 104.32 ? 136 GLY   F CA  1 
ATOM   10328 C  C   . GLY   F  6  140 ? 19.219  -106.720 75.700  1.00 106.04 ? 136 GLY   F C   1 
ATOM   10329 O  O   . GLY   F  6  140 ? 19.982  -106.032 76.408  1.00 111.45 ? 136 GLY   F O   1 
ATOM   10330 N  N   . VAL   F  6  141 ? 19.021  -108.032 75.843  1.00 106.39 ? 137 VAL   F N   1 
ATOM   10331 C  CA  . VAL   F  6  141 ? 19.654  -108.875 76.900  1.00 102.58 ? 137 VAL   F CA  1 
ATOM   10332 C  C   . VAL   F  6  141 ? 20.507  -109.950 76.221  1.00 99.76  ? 137 VAL   F C   1 
ATOM   10333 O  O   . VAL   F  6  141 ? 19.987  -110.633 75.318  1.00 102.27 ? 137 VAL   F O   1 
ATOM   10334 C  CB  . VAL   F  6  141 ? 18.597  -109.506 77.825  1.00 103.42 ? 137 VAL   F CB  1 
ATOM   10335 C  CG1 . VAL   F  6  141 ? 19.229  -110.421 78.862  1.00 102.26 ? 137 VAL   F CG1 1 
ATOM   10336 C  CG2 . VAL   F  6  141 ? 17.740  -108.446 78.498  1.00 106.11 ? 137 VAL   F CG2 1 
ATOM   10337 N  N   . ASP   F  6  142 ? 21.762  -110.087 76.653  1.00 96.34  ? 138 ASP   F N   1 
ATOM   10338 C  CA  . ASP   F  6  142 ? 22.681  -111.169 76.212  1.00 97.94  ? 138 ASP   F CA  1 
ATOM   10339 C  C   . ASP   F  6  142 ? 23.216  -111.886 77.458  1.00 97.90  ? 138 ASP   F C   1 
ATOM   10340 O  O   . ASP   F  6  142 ? 22.674  -111.654 78.558  1.00 92.53  ? 138 ASP   F O   1 
ATOM   10341 C  CB  . ASP   F  6  142 ? 23.764  -110.623 75.271  1.00 97.65  ? 138 ASP   F CB  1 
ATOM   10342 C  CG  . ASP   F  6  142 ? 24.803  -109.718 75.914  1.00 97.12  ? 138 ASP   F CG  1 
ATOM   10343 O  OD1 . ASP   F  6  142 ? 24.977  -109.797 77.145  1.00 97.24  ? 138 ASP   F OD1 1 
ATOM   10344 O  OD2 . ASP   F  6  142 ? 25.445  -108.947 75.171  1.00 99.86  ? 138 ASP   F OD2 1 
ATOM   10345 N  N   . LYS   F  6  143 ? 24.235  -112.731 77.271  1.00 103.14 ? 139 LYS   F N   1 
ATOM   10346 C  CA  . LYS   F  6  143 ? 24.872  -113.587 78.310  1.00 104.86 ? 139 LYS   F CA  1 
ATOM   10347 C  C   . LYS   F  6  143 ? 25.474  -112.723 79.432  1.00 101.15 ? 139 LYS   F C   1 
ATOM   10348 O  O   . LYS   F  6  143 ? 25.632  -113.260 80.548  1.00 99.55  ? 139 LYS   F O   1 
ATOM   10349 C  CB  . LYS   F  6  143 ? 25.878  -114.516 77.615  1.00 110.64 ? 139 LYS   F CB  1 
ATOM   10350 C  CG  . LYS   F  6  143 ? 27.014  -115.072 78.466  1.00 115.80 ? 139 LYS   F CG  1 
ATOM   10351 C  CD  . LYS   F  6  143 ? 28.366  -114.479 78.123  1.00 116.54 ? 139 LYS   F CD  1 
ATOM   10352 C  CE  . LYS   F  6  143 ? 28.958  -115.072 76.862  1.00 115.06 ? 139 LYS   F CE  1 
ATOM   10353 N  NZ  . LYS   F  6  143 ? 30.311  -114.537 76.582  1.00 112.29 ? 139 LYS   F NZ  1 
ATOM   10354 N  N   . ASN   F  6  144 ? 25.769  -111.440 79.172  1.00 98.65  ? 140 ASN   F N   1 
ATOM   10355 C  CA  . ASN   F  6  144 ? 26.384  -110.503 80.155  1.00 94.84  ? 140 ASN   F CA  1 
ATOM   10356 C  C   . ASN   F  6  144 ? 25.337  -109.539 80.734  1.00 93.91  ? 140 ASN   F C   1 
ATOM   10357 O  O   . ASN   F  6  144 ? 25.754  -108.559 81.376  1.00 100.42 ? 140 ASN   F O   1 
ATOM   10358 C  CB  . ASN   F  6  144 ? 27.545  -109.723 79.533  1.00 92.80  ? 140 ASN   F CB  1 
ATOM   10359 C  CG  . ASN   F  6  144 ? 28.727  -110.602 79.190  1.00 94.23  ? 140 ASN   F CG  1 
ATOM   10360 O  OD1 . ASN   F  6  144 ? 29.126  -110.687 78.032  1.00 94.17  ? 140 ASN   F OD1 1 
ATOM   10361 N  ND2 . ASN   F  6  144 ? 29.290  -111.264 80.187  1.00 97.45  ? 140 ASN   F ND2 1 
ATOM   10362 N  N   . GLY   F  6  145 ? 24.040  -109.811 80.551  1.00 94.52  ? 141 GLY   F N   1 
ATOM   10363 C  CA  . GLY   F  6  145 ? 22.941  -108.978 81.082  1.00 94.36  ? 141 GLY   F CA  1 
ATOM   10364 C  C   . GLY   F  6  145 ? 22.432  -107.972 80.062  1.00 94.04  ? 141 GLY   F C   1 
ATOM   10365 O  O   . GLY   F  6  145 ? 22.531  -108.254 78.850  1.00 90.64  ? 141 GLY   F O   1 
ATOM   10366 N  N   . ALA   F  6  146 ? 21.913  -106.834 80.537  1.00 95.23  ? 142 ALA   F N   1 
ATOM   10367 C  CA  . ALA   F  6  146 ? 21.212  -105.808 79.727  1.00 94.60  ? 142 ALA   F CA  1 
ATOM   10368 C  C   . ALA   F  6  146 ? 22.206  -104.762 79.210  1.00 95.65  ? 142 ALA   F C   1 
ATOM   10369 O  O   . ALA   F  6  146 ? 23.173  -104.444 79.930  1.00 97.69  ? 142 ALA   F O   1 
ATOM   10370 C  CB  . ALA   F  6  146 ? 20.123  -105.163 80.547  1.00 97.49  ? 142 ALA   F CB  1 
ATOM   10371 N  N   . HIS   F  6  147 ? 21.963  -104.256 77.998  1.00 93.50  ? 143 HIS   F N   1 
ATOM   10372 C  CA  . HIS   F  6  147 ? 22.719  -103.144 77.362  1.00 95.80  ? 143 HIS   F CA  1 
ATOM   10373 C  C   . HIS   F  6  147 ? 21.746  -102.228 76.616  1.00 97.48  ? 143 HIS   F C   1 
ATOM   10374 O  O   . HIS   F  6  147 ? 20.882  -102.763 75.891  1.00 92.25  ? 143 HIS   F O   1 
ATOM   10375 C  CB  . HIS   F  6  147 ? 23.790  -103.679 76.404  1.00 95.98  ? 143 HIS   F CB  1 
ATOM   10376 C  CG  . HIS   F  6  147 ? 24.705  -104.685 77.013  1.00 96.31  ? 143 HIS   F CG  1 
ATOM   10377 N  ND1 . HIS   F  6  147 ? 24.352  -106.012 77.154  1.00 98.02  ? 143 HIS   F ND1 1 
ATOM   10378 C  CD2 . HIS   F  6  147 ? 25.955  -104.567 77.511  1.00 98.60  ? 143 HIS   F CD2 1 
ATOM   10379 C  CE1 . HIS   F  6  147 ? 25.344  -106.669 77.718  1.00 96.18  ? 143 HIS   F CE1 1 
ATOM   10380 N  NE2 . HIS   F  6  147 ? 26.340  -105.807 77.947  1.00 97.63  ? 143 HIS   F NE2 1 
ATOM   10381 N  N   . LEU   F  6  148 ? 21.894  -100.910 76.797  1.00 100.59 ? 144 LEU   F N   1 
ATOM   10382 C  CA  . LEU   F  6  148 ? 21.194  -99.860  76.009  1.00 96.94  ? 144 LEU   F CA  1 
ATOM   10383 C  C   . LEU   F  6  148 ? 22.245  -99.058  75.239  1.00 94.28  ? 144 LEU   F C   1 
ATOM   10384 O  O   . LEU   F  6  148 ? 23.308  -98.773  75.820  1.00 99.37  ? 144 LEU   F O   1 
ATOM   10385 C  CB  . LEU   F  6  148 ? 20.391  -98.964  76.955  1.00 96.54  ? 144 LEU   F CB  1 
ATOM   10386 C  CG  . LEU   F  6  148 ? 19.694  -97.775  76.293  1.00 99.96  ? 144 LEU   F CG  1 
ATOM   10387 C  CD1 . LEU   F  6  148 ? 18.489  -98.235  75.487  1.00 99.20  ? 144 LEU   F CD1 1 
ATOM   10388 C  CD2 . LEU   F  6  148 ? 19.288  -96.736  77.326  1.00 101.09 ? 144 LEU   F CD2 1 
ATOM   10389 N  N   . TYR   F  6  149 ? 21.955  -98.722  73.980  1.00 95.22  ? 145 TYR   F N   1 
ATOM   10390 C  CA  . TYR   F  6  149 ? 22.849  -97.940  73.088  1.00 95.39  ? 145 TYR   F CA  1 
ATOM   10391 C  C   . TYR   F  6  149 ? 22.051  -96.860  72.356  1.00 99.19  ? 145 TYR   F C   1 
ATOM   10392 O  O   . TYR   F  6  149 ? 20.831  -97.034  72.153  1.00 97.28  ? 145 TYR   F O   1 
ATOM   10393 C  CB  . TYR   F  6  149 ? 23.550  -98.861  72.088  1.00 94.93  ? 145 TYR   F CB  1 
ATOM   10394 C  CG  . TYR   F  6  149 ? 24.657  -99.685  72.691  1.00 93.17  ? 145 TYR   F CG  1 
ATOM   10395 C  CD1 . TYR   F  6  149 ? 25.944  -99.185  72.792  1.00 93.37  ? 145 TYR   F CD1 1 
ATOM   10396 C  CD2 . TYR   F  6  149 ? 24.417  -100.959 73.175  1.00 94.29  ? 145 TYR   F CD2 1 
ATOM   10397 C  CE1 . TYR   F  6  149 ? 26.969  -99.932  73.349  1.00 92.47  ? 145 TYR   F CE1 1 
ATOM   10398 C  CE2 . TYR   F  6  149 ? 25.431  -101.721 73.734  1.00 93.96  ? 145 TYR   F CE2 1 
ATOM   10399 C  CZ  . TYR   F  6  149 ? 26.712  -101.205 73.822  1.00 91.56  ? 145 TYR   F CZ  1 
ATOM   10400 O  OH  . TYR   F  6  149 ? 27.723  -101.938 74.373  1.00 92.92  ? 145 TYR   F OH  1 
ATOM   10401 N  N   . MET   F  6  150 ? 22.740  -95.778  71.984  1.00 98.41  ? 146 MET   F N   1 
ATOM   10402 C  CA  . MET   F  6  150 ? 22.234  -94.718  71.075  1.00 98.82  ? 146 MET   F CA  1 
ATOM   10403 C  C   . MET   F  6  150 ? 23.294  -94.450  70.003  1.00 93.89  ? 146 MET   F C   1 
ATOM   10404 O  O   . MET   F  6  150 ? 24.462  -94.227  70.373  1.00 85.71  ? 146 MET   F O   1 
ATOM   10405 C  CB  . MET   F  6  150 ? 21.931  -93.426  71.837  1.00 101.97 ? 146 MET   F CB  1 
ATOM   10406 C  CG  . MET   F  6  150 ? 21.313  -92.356  70.968  1.00 106.70 ? 146 MET   F CG  1 
ATOM   10407 S  SD  . MET   F  6  150 ? 20.651  -90.998  71.946  1.00 111.92 ? 146 MET   F SD  1 
ATOM   10408 C  CE  . MET   F  6  150 ? 20.680  -89.690  70.721  1.00 115.92 ? 146 MET   F CE  1 
ATOM   10409 N  N   . LEU   F  6  151 ? 22.890  -94.485  68.730  1.00 94.25  ? 147 LEU   F N   1 
ATOM   10410 C  CA  . LEU   F  6  151 ? 23.779  -94.360  67.545  1.00 97.48  ? 147 LEU   F CA  1 
ATOM   10411 C  C   . LEU   F  6  151 ? 23.359  -93.129  66.738  1.00 99.88  ? 147 LEU   F C   1 
ATOM   10412 O  O   . LEU   F  6  151 ? 22.147  -92.986  66.481  1.00 108.40 ? 147 LEU   F O   1 
ATOM   10413 C  CB  . LEU   F  6  151 ? 23.663  -95.639  66.710  1.00 94.91  ? 147 LEU   F CB  1 
ATOM   10414 C  CG  . LEU   F  6  151 ? 24.373  -95.623  65.358  1.00 94.58  ? 147 LEU   F CG  1 
ATOM   10415 C  CD1 . LEU   F  6  151 ? 25.885  -95.597  65.529  1.00 94.01  ? 147 LEU   F CD1 1 
ATOM   10416 C  CD2 . LEU   F  6  151 ? 23.953  -96.822  64.529  1.00 94.00  ? 147 LEU   F CD2 1 
ATOM   10417 N  N   . GLU   F  6  152 ? 24.326  -92.294  66.346  1.00 98.63  ? 148 GLU   F N   1 
ATOM   10418 C  CA  . GLU   F  6  152 ? 24.082  -90.984  65.685  1.00 97.69  ? 148 GLU   F CA  1 
ATOM   10419 C  C   . GLU   F  6  152 ? 24.627  -91.004  64.259  1.00 90.09  ? 148 GLU   F C   1 
ATOM   10420 O  O   . GLU   F  6  152 ? 25.527  -91.777  63.939  1.00 82.81  ? 148 GLU   F O   1 
ATOM   10421 C  CB  . GLU   F  6  152 ? 24.694  -89.860  66.521  1.00 102.99 ? 148 GLU   F CB  1 
ATOM   10422 C  CG  . GLU   F  6  152 ? 23.793  -89.417  67.660  1.00 108.95 ? 148 GLU   F CG  1 
ATOM   10423 C  CD  . GLU   F  6  152 ? 24.457  -88.555  68.719  1.00 119.31 ? 148 GLU   F CD  1 
ATOM   10424 O  OE1 . GLU   F  6  152 ? 25.703  -88.559  68.789  1.00 130.33 ? 148 GLU   F OE1 1 
ATOM   10425 O  OE2 . GLU   F  6  152 ? 23.723  -87.879  69.472  1.00 124.12 ? 148 GLU   F OE2 1 
ATOM   10426 N  N   . PRO   F  6  153 ? 24.085  -90.141  63.369  1.00 90.16  ? 149 PRO   F N   1 
ATOM   10427 C  CA  . PRO   F  6  153 ? 24.475  -90.095  61.956  1.00 90.02  ? 149 PRO   F CA  1 
ATOM   10428 C  C   . PRO   F  6  153 ? 25.978  -90.145  61.628  1.00 90.84  ? 149 PRO   F C   1 
ATOM   10429 O  O   . PRO   F  6  153 ? 26.310  -90.600  60.543  1.00 88.43  ? 149 PRO   F O   1 
ATOM   10430 C  CB  . PRO   F  6  153 ? 23.933  -88.728  61.520  1.00 90.91  ? 149 PRO   F CB  1 
ATOM   10431 C  CG  . PRO   F  6  153 ? 22.684  -88.549  62.351  1.00 91.21  ? 149 PRO   F CG  1 
ATOM   10432 C  CD  . PRO   F  6  153 ? 23.024  -89.171  63.687  1.00 90.57  ? 149 PRO   F CD  1 
ATOM   10433 N  N   . SER   F  6  154 ? 26.834  -89.656  62.535  1.00 90.83  ? 150 SER   F N   1 
ATOM   10434 C  CA  . SER   F  6  154 ? 28.317  -89.657  62.407  1.00 90.62  ? 150 SER   F CA  1 
ATOM   10435 C  C   . SER   F  6  154 ? 28.874  -91.083  62.500  1.00 88.61  ? 150 SER   F C   1 
ATOM   10436 O  O   . SER   F  6  154 ? 30.000  -91.303  62.011  1.00 86.02  ? 150 SER   F O   1 
ATOM   10437 C  CB  . SER   F  6  154 ? 28.955  -88.776  63.453  1.00 89.56  ? 150 SER   F CB  1 
ATOM   10438 O  OG  . SER   F  6  154 ? 28.714  -89.283  64.758  1.00 89.54  ? 150 SER   F OG  1 
ATOM   10439 N  N   . GLY   F  6  155 ? 28.124  -91.999  63.122  1.00 89.96  ? 151 GLY   F N   1 
ATOM   10440 C  CA  . GLY   F  6  155 ? 28.562  -93.373  63.436  1.00 91.66  ? 151 GLY   F CA  1 
ATOM   10441 C  C   . GLY   F  6  155 ? 28.974  -93.499  64.893  1.00 93.34  ? 151 GLY   F C   1 
ATOM   10442 O  O   . GLY   F  6  155 ? 29.315  -94.624  65.323  1.00 90.96  ? 151 GLY   F O   1 
ATOM   10443 N  N   . SER   F  6  156 ? 28.948  -92.384  65.630  1.00 92.22  ? 152 SER   F N   1 
ATOM   10444 C  CA  . SER   F  6  156 ? 29.217  -92.328  67.089  1.00 92.21  ? 152 SER   F CA  1 
ATOM   10445 C  C   . SER   F  6  156 ? 28.095  -93.067  67.821  1.00 91.11  ? 152 SER   F C   1 
ATOM   10446 O  O   . SER   F  6  156 ? 26.918  -92.874  67.455  1.00 90.98  ? 152 SER   F O   1 
ATOM   10447 C  CB  . SER   F  6  156 ? 29.357  -90.903  67.573  1.00 91.15  ? 152 SER   F CB  1 
ATOM   10448 O  OG  . SER   F  6  156 ? 29.682  -90.857  68.958  1.00 88.89  ? 152 SER   F OG  1 
ATOM   10449 N  N   . TYR   F  6  157 ? 28.461  -93.911  68.785  1.00 89.49  ? 153 TYR   F N   1 
ATOM   10450 C  CA  . TYR   F  6  157 ? 27.528  -94.592  69.717  1.00 89.94  ? 153 TYR   F CA  1 
ATOM   10451 C  C   . TYR   F  6  157 ? 28.236  -94.801  71.059  1.00 87.65  ? 153 TYR   F C   1 
ATOM   10452 O  O   . TYR   F  6  157 ? 29.476  -94.932  71.080  1.00 83.72  ? 153 TYR   F O   1 
ATOM   10453 C  CB  . TYR   F  6  157 ? 27.026  -95.910  69.116  1.00 89.12  ? 153 TYR   F CB  1 
ATOM   10454 C  CG  . TYR   F  6  157 ? 28.052  -97.013  69.063  1.00 88.71  ? 153 TYR   F CG  1 
ATOM   10455 C  CD1 . TYR   F  6  157 ? 28.324  -97.786  70.181  1.00 89.49  ? 153 TYR   F CD1 1 
ATOM   10456 C  CD2 . TYR   F  6  157 ? 28.757  -97.286  67.901  1.00 87.46  ? 153 TYR   F CD2 1 
ATOM   10457 C  CE1 . TYR   F  6  157 ? 29.268  -98.799  70.149  1.00 90.05  ? 153 TYR   F CE1 1 
ATOM   10458 C  CE2 . TYR   F  6  157 ? 29.702  -98.299  67.850  1.00 88.94  ? 153 TYR   F CE2 1 
ATOM   10459 C  CZ  . TYR   F  6  157 ? 29.959  -99.060  68.978  1.00 87.65  ? 153 TYR   F CZ  1 
ATOM   10460 O  OH  . TYR   F  6  157 ? 30.888  -100.059 68.946  1.00 86.03  ? 153 TYR   F OH  1 
ATOM   10461 N  N   . TRP   F  6  158 ? 27.461  -94.819  72.144  1.00 90.67  ? 154 TRP   F N   1 
ATOM   10462 C  CA  . TRP   F  6  158 ? 27.932  -95.140  73.517  1.00 94.35  ? 154 TRP   F CA  1 
ATOM   10463 C  C   . TRP   F  6  158 ? 26.905  -96.045  74.200  1.00 96.35  ? 154 TRP   F C   1 
ATOM   10464 O  O   . TRP   F  6  158 ? 25.755  -96.101  73.723  1.00 99.97  ? 154 TRP   F O   1 
ATOM   10465 C  CB  . TRP   F  6  158 ? 28.158  -93.867  74.342  1.00 96.28  ? 154 TRP   F CB  1 
ATOM   10466 C  CG  . TRP   F  6  158 ? 29.102  -92.878  73.733  1.00 96.31  ? 154 TRP   F CG  1 
ATOM   10467 C  CD1 . TRP   F  6  158 ? 28.796  -91.630  73.274  1.00 99.03  ? 154 TRP   F CD1 1 
ATOM   10468 C  CD2 . TRP   F  6  158 ? 30.516  -93.046  73.525  1.00 97.25  ? 154 TRP   F CD2 1 
ATOM   10469 N  NE1 . TRP   F  6  158 ? 29.918  -91.012  72.792  1.00 100.25 ? 154 TRP   F NE1 1 
ATOM   10470 C  CE2 . TRP   F  6  158 ? 30.988  -91.855  72.933  1.00 97.09  ? 154 TRP   F CE2 1 
ATOM   10471 C  CE3 . TRP   F  6  158 ? 31.424  -94.082  73.775  1.00 96.25  ? 154 TRP   F CE3 1 
ATOM   10472 C  CZ2 . TRP   F  6  158 ? 32.328  -91.675  72.590  1.00 97.55  ? 154 TRP   F CZ2 1 
ATOM   10473 C  CZ3 . TRP   F  6  158 ? 32.748  -93.903  73.435  1.00 96.69  ? 154 TRP   F CZ3 1 
ATOM   10474 C  CH2 . TRP   F  6  158 ? 33.192  -92.714  72.853  1.00 96.58  ? 154 TRP   F CH2 1 
ATOM   10475 N  N   . GLY   F  6  159 ? 27.317  -96.723  75.273  1.00 96.23  ? 155 GLY   F N   1 
ATOM   10476 C  CA  . GLY   F  6  159 ? 26.397  -97.352  76.237  1.00 95.68  ? 155 GLY   F CA  1 
ATOM   10477 C  C   . GLY   F  6  159 ? 25.740  -96.284  77.091  1.00 92.94  ? 155 GLY   F C   1 
ATOM   10478 O  O   . GLY   F  6  159 ? 26.432  -95.307  77.432  1.00 91.38  ? 155 GLY   F O   1 
ATOM   10479 N  N   . TYR   F  6  160 ? 24.452  -96.444  77.410  1.00 94.82  ? 156 TYR   F N   1 
ATOM   10480 C  CA  . TYR   F  6  160 ? 23.642  -95.445  78.155  1.00 98.38  ? 156 TYR   F CA  1 
ATOM   10481 C  C   . TYR   F  6  160 ? 22.896  -96.119  79.311  1.00 101.23 ? 156 TYR   F C   1 
ATOM   10482 O  O   . TYR   F  6  160 ? 22.534  -97.305  79.199  1.00 102.32 ? 156 TYR   F O   1 
ATOM   10483 C  CB  . TYR   F  6  160 ? 22.669  -94.733  77.211  1.00 100.70 ? 156 TYR   F CB  1 
ATOM   10484 C  CG  . TYR   F  6  160 ? 23.308  -93.687  76.334  1.00 98.32  ? 156 TYR   F CG  1 
ATOM   10485 C  CD1 . TYR   F  6  160 ? 23.879  -94.034  75.121  1.00 98.79  ? 156 TYR   F CD1 1 
ATOM   10486 C  CD2 . TYR   F  6  160 ? 23.356  -92.356  76.715  1.00 95.98  ? 156 TYR   F CD2 1 
ATOM   10487 C  CE1 . TYR   F  6  160 ? 24.480  -93.089  74.307  1.00 95.02  ? 156 TYR   F CE1 1 
ATOM   10488 C  CE2 . TYR   F  6  160 ? 23.951  -91.398  75.911  1.00 94.69  ? 156 TYR   F CE2 1 
ATOM   10489 C  CZ  . TYR   F  6  160 ? 24.514  -91.767  74.703  1.00 94.01  ? 156 TYR   F CZ  1 
ATOM   10490 O  OH  . TYR   F  6  160 ? 25.106  -90.849  73.888  1.00 98.14  ? 156 TYR   F OH  1 
ATOM   10491 N  N   . LYS   F  6  161 ? 22.705  -95.368  80.399  1.00 102.00 ? 157 LYS   F N   1 
ATOM   10492 C  CA  . LYS   F  6  161 ? 21.740  -95.672  81.490  1.00 102.57 ? 157 LYS   F CA  1 
ATOM   10493 C  C   . LYS   F  6  161 ? 20.339  -95.302  80.996  1.00 102.71 ? 157 LYS   F C   1 
ATOM   10494 O  O   . LYS   F  6  161 ? 19.407  -96.111  81.159  1.00 98.56  ? 157 LYS   F O   1 
ATOM   10495 C  CB  . LYS   F  6  161 ? 22.100  -94.891  82.758  1.00 104.71 ? 157 LYS   F CB  1 
ATOM   10496 C  CG  . LYS   F  6  161 ? 23.332  -95.401  83.489  1.00 105.67 ? 157 LYS   F CG  1 
ATOM   10497 C  CD  . LYS   F  6  161 ? 23.958  -94.391  84.421  1.00 109.78 ? 157 LYS   F CD  1 
ATOM   10498 C  CE  . LYS   F  6  161 ? 25.185  -94.938  85.118  1.00 111.28 ? 157 LYS   F CE  1 
ATOM   10499 N  NZ  . LYS   F  6  161 ? 25.893  -93.889  85.888  1.00 114.74 ? 157 LYS   F NZ  1 
ATOM   10500 N  N   . GLY   F  6  162 ? 20.219  -94.107  80.414  1.00 103.38 ? 158 GLY   F N   1 
ATOM   10501 C  CA  . GLY   F  6  162 ? 19.025  -93.628  79.694  1.00 103.07 ? 158 GLY   F CA  1 
ATOM   10502 C  C   . GLY   F  6  162 ? 19.431  -92.899  78.427  1.00 101.31 ? 158 GLY   F C   1 
ATOM   10503 O  O   . GLY   F  6  162 ? 20.544  -92.342  78.396  1.00 99.19  ? 158 GLY   F O   1 
ATOM   10504 N  N   . ALA   F  6  163 ? 18.573  -92.914  77.407  1.00 100.76 ? 159 ALA   F N   1 
ATOM   10505 C  CA  . ALA   F  6  163 ? 18.832  -92.282  76.094  1.00 101.21 ? 159 ALA   F CA  1 
ATOM   10506 C  C   . ALA   F  6  163 ? 17.543  -91.660  75.555  1.00 101.29 ? 159 ALA   F C   1 
ATOM   10507 O  O   . ALA   F  6  163 ? 16.461  -92.242  75.766  1.00 105.55 ? 159 ALA   F O   1 
ATOM   10508 C  CB  . ALA   F  6  163 ? 19.401  -93.295  75.134  1.00 100.78 ? 159 ALA   F CB  1 
ATOM   10509 N  N   . ALA   F  6  164 ? 17.678  -90.515  74.885  1.00 97.26  ? 160 ALA   F N   1 
ATOM   10510 C  CA  . ALA   F  6  164 ? 16.573  -89.738  74.285  1.00 96.72  ? 160 ALA   F CA  1 
ATOM   10511 C  C   . ALA   F  6  164 ? 17.076  -89.076  73.001  1.00 94.11  ? 160 ALA   F C   1 
ATOM   10512 O  O   . ALA   F  6  164 ? 18.271  -88.726  72.943  1.00 91.29  ? 160 ALA   F O   1 
ATOM   10513 C  CB  . ALA   F  6  164 ? 16.071  -88.719  75.277  1.00 97.95  ? 160 ALA   F CB  1 
ATOM   10514 N  N   . THR   F  6  165 ? 16.196  -88.932  72.009  1.00 95.04  ? 161 THR   F N   1 
ATOM   10515 C  CA  . THR   F  6  165 ? 16.465  -88.201  70.743  1.00 96.64  ? 161 THR   F CA  1 
ATOM   10516 C  C   . THR   F  6  165 ? 15.139  -87.752  70.120  1.00 97.26  ? 161 THR   F C   1 
ATOM   10517 O  O   . THR   F  6  165 ? 14.104  -88.377  70.417  1.00 96.82  ? 161 THR   F O   1 
ATOM   10518 C  CB  . THR   F  6  165 ? 17.284  -89.066  69.779  1.00 94.18  ? 161 THR   F CB  1 
ATOM   10519 O  OG1 . THR   F  6  165 ? 17.697  -88.252  68.680  1.00 97.38  ? 161 THR   F OG1 1 
ATOM   10520 C  CG2 . THR   F  6  165 ? 16.519  -90.271  69.279  1.00 93.52  ? 161 THR   F CG2 1 
ATOM   10521 N  N   . GLY   F  6  166 ? 15.191  -86.718  69.279  1.00 102.22 ? 162 GLY   F N   1 
ATOM   10522 C  CA  . GLY   F  6  166 ? 14.018  -86.120  68.614  1.00 106.21 ? 162 GLY   F CA  1 
ATOM   10523 C  C   . GLY   F  6  166 ? 13.785  -84.696  69.083  1.00 108.51 ? 162 GLY   F C   1 
ATOM   10524 O  O   . GLY   F  6  166 ? 14.719  -84.100  69.653  1.00 106.39 ? 162 GLY   F O   1 
ATOM   10525 N  N   . LYS   F  6  167 ? 12.575  -84.174  68.866  1.00 110.38 ? 163 LYS   F N   1 
ATOM   10526 C  CA  . LYS   F  6  167 ? 12.232  -82.750  69.119  1.00 112.72 ? 163 LYS   F CA  1 
ATOM   10527 C  C   . LYS   F  6  167 ? 12.193  -82.475  70.628  1.00 110.58 ? 163 LYS   F C   1 
ATOM   10528 O  O   . LYS   F  6  167 ? 12.484  -81.327  71.013  1.00 111.77 ? 163 LYS   F O   1 
ATOM   10529 C  CB  . LYS   F  6  167 ? 10.908  -82.381  68.442  1.00 122.43 ? 163 LYS   F CB  1 
ATOM   10530 C  CG  . LYS   F  6  167 ? 10.711  -80.885  68.220  1.00 126.09 ? 163 LYS   F CG  1 
ATOM   10531 C  CD  . LYS   F  6  167 ? 10.347  -80.515  66.797  1.00 131.18 ? 163 LYS   F CD  1 
ATOM   10532 C  CE  . LYS   F  6  167 ? 8.913   -80.849  66.450  1.00 136.51 ? 163 LYS   F CE  1 
ATOM   10533 N  NZ  . LYS   F  6  167 ? 8.679   -80.802  64.988  1.00 137.38 ? 163 LYS   F NZ  1 
ATOM   10534 N  N   . GLY   F  6  168 ? 11.860  -83.479  71.446  1.00 108.60 ? 164 GLY   F N   1 
ATOM   10535 C  CA  . GLY   F  6  168 ? 11.740  -83.336  72.911  1.00 108.70 ? 164 GLY   F CA  1 
ATOM   10536 C  C   . GLY   F  6  168 ? 12.871  -84.016  73.667  1.00 105.36 ? 164 GLY   F C   1 
ATOM   10537 O  O   . GLY   F  6  168 ? 12.601  -84.517  74.775  1.00 104.33 ? 164 GLY   F O   1 
ATOM   10538 N  N   . ARG   F  6  169 ? 14.095  -84.011  73.119  1.00 105.52 ? 165 ARG   F N   1 
ATOM   10539 C  CA  . ARG   F  6  169 ? 15.257  -84.767  73.670  1.00 105.53 ? 165 ARG   F CA  1 
ATOM   10540 C  C   . ARG   F  6  169 ? 15.720  -84.137  74.992  1.00 107.81 ? 165 ARG   F C   1 
ATOM   10541 O  O   . ARG   F  6  169 ? 16.049  -84.906  75.915  1.00 104.36 ? 165 ARG   F O   1 
ATOM   10542 C  CB  . ARG   F  6  169 ? 16.395  -84.869  72.643  1.00 104.04 ? 165 ARG   F CB  1 
ATOM   10543 C  CG  . ARG   F  6  169 ? 17.366  -83.695  72.614  1.00 102.74 ? 165 ARG   F CG  1 
ATOM   10544 C  CD  . ARG   F  6  169 ? 18.039  -83.545  71.264  1.00 104.46 ? 165 ARG   F CD  1 
ATOM   10545 N  NE  . ARG   F  6  169 ? 17.111  -82.976  70.293  1.00 109.30 ? 165 ARG   F NE  1 
ATOM   10546 C  CZ  . ARG   F  6  169 ? 17.071  -81.701  69.899  1.00 112.35 ? 165 ARG   F CZ  1 
ATOM   10547 N  NH1 . ARG   F  6  169 ? 17.930  -80.811  70.371  1.00 116.42 ? 165 ARG   F NH1 1 
ATOM   10548 N  NH2 . ARG   F  6  169 ? 16.165  -81.321  69.013  1.00 114.13 ? 165 ARG   F NH2 1 
ATOM   10549 N  N   . GLN   F  6  170 ? 15.730  -82.803  75.087  1.00 109.65 ? 166 GLN   F N   1 
ATOM   10550 C  CA  . GLN   F  6  170 ? 16.240  -82.052  76.267  1.00 112.27 ? 166 GLN   F CA  1 
ATOM   10551 C  C   . GLN   F  6  170 ? 15.284  -82.252  77.447  1.00 109.04 ? 166 GLN   F C   1 
ATOM   10552 O  O   . GLN   F  6  170 ? 15.776  -82.523  78.561  1.00 104.08 ? 166 GLN   F O   1 
ATOM   10553 C  CB  . GLN   F  6  170 ? 16.401  -80.567  75.940  1.00 119.90 ? 166 GLN   F CB  1 
ATOM   10554 C  CG  . GLN   F  6  170 ? 17.494  -80.285  74.919  1.00 127.99 ? 166 GLN   F CG  1 
ATOM   10555 C  CD  . GLN   F  6  170 ? 17.568  -78.822  74.549  1.00 136.63 ? 166 GLN   F CD  1 
ATOM   10556 O  OE1 . GLN   F  6  170 ? 16.636  -78.260  73.977  1.00 147.13 ? 166 GLN   F OE1 1 
ATOM   10557 N  NE2 . GLN   F  6  170 ? 18.684  -78.187  74.871  1.00 141.29 ? 166 GLN   F NE2 1 
ATOM   10558 N  N   . SER   F  6  171 ? 13.977  -82.111  77.205  1.00 108.10 ? 167 SER   F N   1 
ATOM   10559 C  CA  . SER   F  6  171 ? 12.888  -82.394  78.177  1.00 110.35 ? 167 SER   F CA  1 
ATOM   10560 C  C   . SER   F  6  171 ? 13.044  -83.821  78.715  1.00 108.12 ? 167 SER   F C   1 
ATOM   10561 O  O   . SER   F  6  171 ? 13.078  -83.995  79.948  1.00 105.40 ? 167 SER   F O   1 
ATOM   10562 C  CB  . SER   F  6  171 ? 11.534  -82.192  77.544  1.00 112.78 ? 167 SER   F CB  1 
ATOM   10563 O  OG  . SER   F  6  171 ? 10.501  -82.681  78.385  1.00 118.46 ? 167 SER   F OG  1 
ATOM   10564 N  N   . ALA   F  6  172 ? 13.151  -84.795  77.809  1.00 107.85 ? 168 ALA   F N   1 
ATOM   10565 C  CA  . ALA   F  6  172 ? 13.271  -86.240  78.113  1.00 110.43 ? 168 ALA   F CA  1 
ATOM   10566 C  C   . ALA   F  6  172 ? 14.571  -86.517  78.879  1.00 110.24 ? 168 ALA   F C   1 
ATOM   10567 O  O   . ALA   F  6  172 ? 14.518  -87.299  79.847  1.00 114.70 ? 168 ALA   F O   1 
ATOM   10568 C  CB  . ALA   F  6  172 ? 13.197  -87.044  76.837  1.00 109.47 ? 168 ALA   F CB  1 
ATOM   10569 N  N   . LYS   F  6  173 ? 15.687  -85.905  78.464  1.00 107.45 ? 169 LYS   F N   1 
ATOM   10570 C  CA  . LYS   F  6  173 ? 17.024  -86.088  79.097  1.00 107.27 ? 169 LYS   F CA  1 
ATOM   10571 C  C   . LYS   F  6  173 ? 16.970  -85.644  80.563  1.00 111.55 ? 169 LYS   F C   1 
ATOM   10572 O  O   . LYS   F  6  173 ? 17.447  -86.409  81.422  1.00 109.27 ? 169 LYS   F O   1 
ATOM   10573 C  CB  . LYS   F  6  173 ? 18.114  -85.308  78.357  1.00 107.69 ? 169 LYS   F CB  1 
ATOM   10574 C  CG  . LYS   F  6  173 ? 18.764  -86.046  77.197  1.00 110.22 ? 169 LYS   F CG  1 
ATOM   10575 C  CD  . LYS   F  6  173 ? 20.145  -85.528  76.860  1.00 114.86 ? 169 LYS   F CD  1 
ATOM   10576 C  CE  . LYS   F  6  173 ? 20.699  -86.114  75.580  1.00 118.45 ? 169 LYS   F CE  1 
ATOM   10577 N  NZ  . LYS   F  6  173 ? 20.044  -85.534  74.384  1.00 122.27 ? 169 LYS   F NZ  1 
ATOM   10578 N  N   . ALA   F  6  174 ? 16.425  -84.451  80.829  1.00 113.03 ? 170 ALA   F N   1 
ATOM   10579 C  CA  . ALA   F  6  174 ? 16.246  -83.882  82.187  1.00 114.96 ? 170 ALA   F CA  1 
ATOM   10580 C  C   . ALA   F  6  174 ? 15.463  -84.866  83.063  1.00 118.64 ? 170 ALA   F C   1 
ATOM   10581 O  O   . ALA   F  6  174 ? 15.818  -85.012  84.248  1.00 124.42 ? 170 ALA   F O   1 
ATOM   10582 C  CB  . ALA   F  6  174 ? 15.544  -82.549  82.110  1.00 113.80 ? 170 ALA   F CB  1 
ATOM   10583 N  N   . GLU   F  6  175 ? 14.442  -85.515  82.492  1.00 119.49 ? 171 GLU   F N   1 
ATOM   10584 C  CA  . GLU   F  6  175 ? 13.543  -86.462  83.206  1.00 122.04 ? 171 GLU   F CA  1 
ATOM   10585 C  C   . GLU   F  6  175 ? 14.284  -87.782  83.463  1.00 119.62 ? 171 GLU   F C   1 
ATOM   10586 O  O   . GLU   F  6  175 ? 14.086  -88.365  84.550  1.00 115.42 ? 171 GLU   F O   1 
ATOM   10587 C  CB  . GLU   F  6  175 ? 12.255  -86.680  82.408  1.00 122.99 ? 171 GLU   F CB  1 
ATOM   10588 C  CG  . GLU   F  6  175 ? 11.029  -86.856  83.285  1.00 127.55 ? 171 GLU   F CG  1 
ATOM   10589 C  CD  . GLU   F  6  175 ? 10.746  -85.679  84.204  1.00 127.32 ? 171 GLU   F CD  1 
ATOM   10590 O  OE1 . GLU   F  6  175 ? 11.081  -84.540  83.826  1.00 128.91 ? 171 GLU   F OE1 1 
ATOM   10591 O  OE2 . GLU   F  6  175 ? 10.200  -85.904  85.300  1.00 134.75 ? 171 GLU   F OE2 1 
ATOM   10592 N  N   . LEU   F  6  176 ? 15.098  -88.229  82.498  1.00 119.40 ? 172 LEU   F N   1 
ATOM   10593 C  CA  . LEU   F  6  176 ? 15.959  -89.442  82.598  1.00 116.22 ? 172 LEU   F CA  1 
ATOM   10594 C  C   . LEU   F  6  176 ? 16.985  -89.259  83.726  1.00 115.21 ? 172 LEU   F C   1 
ATOM   10595 O  O   . LEU   F  6  176 ? 17.136  -90.196  84.534  1.00 113.27 ? 172 LEU   F O   1 
ATOM   10596 C  CB  . LEU   F  6  176 ? 16.659  -89.690  81.254  1.00 115.02 ? 172 LEU   F CB  1 
ATOM   10597 C  CG  . LEU   F  6  176 ? 16.181  -90.885  80.421  1.00 114.63 ? 172 LEU   F CG  1 
ATOM   10598 C  CD1 . LEU   F  6  176 ? 14.707  -91.195  80.635  1.00 115.50 ? 172 LEU   F CD1 1 
ATOM   10599 C  CD2 . LEU   F  6  176 ? 16.454  -90.651  78.942  1.00 113.96 ? 172 LEU   F CD2 1 
ATOM   10600 N  N   . GLU   F  6  177 ? 17.658  -88.103  83.776  1.00 114.70 ? 173 GLU   F N   1 
ATOM   10601 C  CA  . GLU   F  6  177 ? 18.733  -87.795  84.762  1.00 114.76 ? 173 GLU   F CA  1 
ATOM   10602 C  C   . GLU   F  6  177 ? 18.184  -87.908  86.190  1.00 108.92 ? 173 GLU   F C   1 
ATOM   10603 O  O   . GLU   F  6  177 ? 18.936  -88.380  87.063  1.00 100.48 ? 173 GLU   F O   1 
ATOM   10604 C  CB  . GLU   F  6  177 ? 19.325  -86.404  84.520  1.00 116.58 ? 173 GLU   F CB  1 
ATOM   10605 C  CG  . GLU   F  6  177 ? 20.274  -86.343  83.337  1.00 119.76 ? 173 GLU   F CG  1 
ATOM   10606 C  CD  . GLU   F  6  177 ? 20.939  -84.993  83.126  1.00 123.38 ? 173 GLU   F CD  1 
ATOM   10607 O  OE1 . GLU   F  6  177 ? 20.985  -84.535  81.966  1.00 130.43 ? 173 GLU   F OE1 1 
ATOM   10608 O  OE2 . GLU   F  6  177 ? 21.413  -84.405  84.119  1.00 132.04 ? 173 GLU   F OE2 1 
ATOM   10609 N  N   . LYS   F  6  178 ? 16.933  -87.486  86.415  1.00 114.30 ? 174 LYS   F N   1 
ATOM   10610 C  CA  . LYS   F  6  178 ? 16.252  -87.531  87.740  1.00 120.38 ? 174 LYS   F CA  1 
ATOM   10611 C  C   . LYS   F  6  178 ? 16.106  -88.989  88.189  1.00 120.18 ? 174 LYS   F C   1 
ATOM   10612 O  O   . LYS   F  6  178 ? 16.383  -89.265  89.372  1.00 123.02 ? 174 LYS   F O   1 
ATOM   10613 C  CB  . LYS   F  6  178 ? 14.895  -86.818  87.690  1.00 126.02 ? 174 LYS   F CB  1 
ATOM   10614 C  CG  . LYS   F  6  178 ? 14.955  -85.322  87.970  1.00 128.42 ? 174 LYS   F CG  1 
ATOM   10615 C  CD  . LYS   F  6  178 ? 13.947  -84.494  87.198  1.00 132.87 ? 174 LYS   F CD  1 
ATOM   10616 C  CE  . LYS   F  6  178 ? 14.290  -83.018  87.202  1.00 133.49 ? 174 LYS   F CE  1 
ATOM   10617 N  NZ  . LYS   F  6  178 ? 13.439  -82.246  86.265  1.00 134.59 ? 174 LYS   F NZ  1 
ATOM   10618 N  N   . LEU   F  6  179 ? 15.694  -89.880  87.280  1.00 120.57 ? 175 LEU   F N   1 
ATOM   10619 C  CA  . LEU   F  6  179 ? 15.549  -91.338  87.552  1.00 119.87 ? 175 LEU   F CA  1 
ATOM   10620 C  C   . LEU   F  6  179 ? 16.906  -91.928  87.952  1.00 116.27 ? 175 LEU   F C   1 
ATOM   10621 O  O   . LEU   F  6  179 ? 16.944  -92.686  88.939  1.00 114.03 ? 175 LEU   F O   1 
ATOM   10622 C  CB  . LEU   F  6  179 ? 14.988  -92.051  86.317  1.00 118.07 ? 175 LEU   F CB  1 
ATOM   10623 C  CG  . LEU   F  6  179 ? 13.489  -91.880  86.079  1.00 119.86 ? 175 LEU   F CG  1 
ATOM   10624 C  CD1 . LEU   F  6  179 ? 13.087  -92.473  84.739  1.00 119.05 ? 175 LEU   F CD1 1 
ATOM   10625 C  CD2 . LEU   F  6  179 ? 12.680  -92.508  87.205  1.00 120.79 ? 175 LEU   F CD2 1 
ATOM   10626 N  N   . VAL   F  6  180 ? 17.971  -91.591  87.218  1.00 114.70 ? 176 VAL   F N   1 
ATOM   10627 C  CA  . VAL   F  6  180 ? 19.349  -92.112  87.470  1.00 116.47 ? 176 VAL   F CA  1 
ATOM   10628 C  C   . VAL   F  6  180 ? 19.786  -91.681  88.876  1.00 123.50 ? 176 VAL   F C   1 
ATOM   10629 O  O   . VAL   F  6  180 ? 20.363  -92.523  89.591  1.00 123.22 ? 176 VAL   F O   1 
ATOM   10630 C  CB  . VAL   F  6  180 ? 20.348  -91.650  86.390  1.00 115.95 ? 176 VAL   F CB  1 
ATOM   10631 C  CG1 . VAL   F  6  180 ? 21.783  -92.021  86.740  1.00 113.68 ? 176 VAL   F CG1 1 
ATOM   10632 C  CG2 . VAL   F  6  180 ? 19.983  -92.203  85.020  1.00 115.34 ? 176 VAL   F CG2 1 
ATOM   10633 N  N   . ASP   F  6  181 ? 19.506  -90.428  89.256  1.00 128.47 ? 177 ASP   F N   1 
ATOM   10634 C  CA  . ASP   F  6  181 ? 19.875  -89.847  90.576  1.00 133.51 ? 177 ASP   F CA  1 
ATOM   10635 C  C   . ASP   F  6  181 ? 19.030  -90.487  91.686  1.00 133.78 ? 177 ASP   F C   1 
ATOM   10636 O  O   . ASP   F  6  181 ? 19.613  -90.836  92.728  1.00 138.93 ? 177 ASP   F O   1 
ATOM   10637 C  CB  . ASP   F  6  181 ? 19.725  -88.322  90.584  1.00 137.95 ? 177 ASP   F CB  1 
ATOM   10638 C  CG  . ASP   F  6  181 ? 20.747  -87.596  89.726  1.00 143.29 ? 177 ASP   F CG  1 
ATOM   10639 O  OD1 . ASP   F  6  181 ? 21.867  -88.125  89.563  1.00 139.43 ? 177 ASP   F OD1 1 
ATOM   10640 O  OD2 . ASP   F  6  181 ? 20.413  -86.502  89.229  1.00 152.96 ? 177 ASP   F OD2 1 
ATOM   10641 N  N   . HIS   F  6  182 ? 17.719  -90.643  91.470  1.00 134.44 ? 178 HIS   F N   1 
ATOM   10642 C  CA  . HIS   F  6  182 ? 16.741  -91.094  92.501  1.00 135.93 ? 178 HIS   F CA  1 
ATOM   10643 C  C   . HIS   F  6  182 ? 16.757  -92.621  92.671  1.00 128.95 ? 178 HIS   F C   1 
ATOM   10644 O  O   . HIS   F  6  182 ? 16.174  -93.092  93.665  1.00 126.12 ? 178 HIS   F O   1 
ATOM   10645 C  CB  . HIS   F  6  182 ? 15.326  -90.591  92.175  1.00 142.60 ? 178 HIS   F CB  1 
ATOM   10646 C  CG  . HIS   F  6  182 ? 15.143  -89.121  92.361  1.00 148.69 ? 178 HIS   F CG  1 
ATOM   10647 N  ND1 . HIS   F  6  182 ? 14.201  -88.400  91.651  1.00 152.96 ? 178 HIS   F ND1 1 
ATOM   10648 C  CD2 . HIS   F  6  182 ? 15.773  -88.233  93.162  1.00 149.05 ? 178 HIS   F CD2 1 
ATOM   10649 C  CE1 . HIS   F  6  182 ? 14.254  -87.135  92.013  1.00 154.37 ? 178 HIS   F CE1 1 
ATOM   10650 N  NE2 . HIS   F  6  182 ? 15.212  -87.005  92.938  1.00 150.88 ? 178 HIS   F NE2 1 
ATOM   10651 N  N   . HIS   F  6  183 ? 17.378  -93.365  91.748  1.00 127.52 ? 179 HIS   F N   1 
ATOM   10652 C  CA  . HIS   F  6  183 ? 17.432  -94.853  91.761  1.00 127.72 ? 179 HIS   F CA  1 
ATOM   10653 C  C   . HIS   F  6  183 ? 18.856  -95.326  91.470  1.00 129.14 ? 179 HIS   F C   1 
ATOM   10654 O  O   . HIS   F  6  183 ? 19.132  -95.829  90.384  1.00 132.11 ? 179 HIS   F O   1 
ATOM   10655 C  CB  . HIS   F  6  183 ? 16.411  -95.435  90.769  1.00 124.82 ? 179 HIS   F CB  1 
ATOM   10656 C  CG  . HIS   F  6  183 ? 15.009  -94.960  90.973  1.00 123.66 ? 179 HIS   F CG  1 
ATOM   10657 N  ND1 . HIS   F  6  183 ? 14.148  -95.547  91.883  1.00 123.71 ? 179 HIS   F ND1 1 
ATOM   10658 C  CD2 . HIS   F  6  183 ? 14.306  -93.970  90.378  1.00 125.01 ? 179 HIS   F CD2 1 
ATOM   10659 C  CE1 . HIS   F  6  183 ? 12.981  -94.934  91.844  1.00 122.85 ? 179 HIS   F CE1 1 
ATOM   10660 N  NE2 . HIS   F  6  183 ? 13.053  -93.963  90.930  1.00 123.02 ? 179 HIS   F NE2 1 
ATOM   10661 N  N   . PRO   F  6  184 ? 19.806  -95.182  92.426  1.00 131.67 ? 180 PRO   F N   1 
ATOM   10662 C  CA  . PRO   F  6  184 ? 21.181  -95.647  92.223  1.00 129.71 ? 180 PRO   F CA  1 
ATOM   10663 C  C   . PRO   F  6  184 ? 21.323  -97.177  92.238  1.00 125.16 ? 180 PRO   F C   1 
ATOM   10664 O  O   . PRO   F  6  184 ? 22.235  -97.676  91.602  1.00 114.53 ? 180 PRO   F O   1 
ATOM   10665 C  CB  . PRO   F  6  184 ? 21.946  -95.032  93.405  1.00 132.23 ? 180 PRO   F CB  1 
ATOM   10666 C  CG  . PRO   F  6  184 ? 20.897  -94.874  94.486  1.00 134.18 ? 180 PRO   F CG  1 
ATOM   10667 C  CD  . PRO   F  6  184 ? 19.615  -94.555  93.744  1.00 132.55 ? 180 PRO   F CD  1 
ATOM   10668 N  N   . GLU   F  6  185 ? 20.434  -97.874  92.955  1.00 129.03 ? 181 GLU   F N   1 
ATOM   10669 C  CA  . GLU   F  6  185 ? 20.432  -99.361  93.069  1.00 130.37 ? 181 GLU   F CA  1 
ATOM   10670 C  C   . GLU   F  6  185 ? 19.888  -99.970  91.768  1.00 126.57 ? 181 GLU   F C   1 
ATOM   10671 O  O   . GLU   F  6  185 ? 20.491  -100.953 91.296  1.00 125.39 ? 181 GLU   F O   1 
ATOM   10672 C  CB  . GLU   F  6  185 ? 19.669  -99.880  94.298  1.00 134.88 ? 181 GLU   F CB  1 
ATOM   10673 C  CG  . GLU   F  6  185 ? 18.815  -98.860  95.039  1.00 138.38 ? 181 GLU   F CG  1 
ATOM   10674 C  CD  . GLU   F  6  185 ? 17.603  -98.337  94.287  1.00 138.96 ? 181 GLU   F CD  1 
ATOM   10675 O  OE1 . GLU   F  6  185 ? 17.270  -97.147  94.464  1.00 141.29 ? 181 GLU   F OE1 1 
ATOM   10676 O  OE2 . GLU   F  6  185 ? 16.993  -99.118  93.532  1.00 138.28 ? 181 GLU   F OE2 1 
ATOM   10677 N  N   . GLY   F  6  186 ? 18.807  -99.412  91.208  1.00 126.60 ? 182 GLY   F N   1 
ATOM   10678 C  CA  . GLY   F  6  186 ? 18.250  -99.839  89.908  1.00 125.21 ? 182 GLY   F CA  1 
ATOM   10679 C  C   . GLY   F  6  186 ? 16.742  -99.677  89.824  1.00 124.33 ? 182 GLY   F C   1 
ATOM   10680 O  O   . GLY   F  6  186 ? 16.083  -99.634  90.880  1.00 126.53 ? 182 GLY   F O   1 
ATOM   10681 N  N   . LEU   F  6  187 ? 16.223  -99.605  88.594  1.00 125.30 ? 183 LEU   F N   1 
ATOM   10682 C  CA  . LEU   F  6  187 ? 14.776  -99.508  88.263  1.00 125.42 ? 183 LEU   F CA  1 
ATOM   10683 C  C   . LEU   F  6  187 ? 14.297  -100.884 87.781  1.00 120.56 ? 183 LEU   F C   1 
ATOM   10684 O  O   . LEU   F  6  187 ? 15.065  -101.546 87.052  1.00 111.05 ? 183 LEU   F O   1 
ATOM   10685 C  CB  . LEU   F  6  187 ? 14.608  -98.436  87.180  1.00 126.76 ? 183 LEU   F CB  1 
ATOM   10686 C  CG  . LEU   F  6  187 ? 13.223  -97.804  87.045  1.00 132.30 ? 183 LEU   F CG  1 
ATOM   10687 C  CD1 . LEU   F  6  187 ? 12.824  -97.060  88.314  1.00 135.87 ? 183 LEU   F CD1 1 
ATOM   10688 C  CD2 . LEU   F  6  187 ? 13.185  -96.860  85.851  1.00 131.54 ? 183 LEU   F CD2 1 
ATOM   10689 N  N   . SER   F  6  188 ? 13.096  -101.312 88.190  1.00 122.05 ? 184 SER   F N   1 
ATOM   10690 C  CA  . SER   F  6  188 ? 12.475  -102.599 87.772  1.00 120.21 ? 184 SER   F CA  1 
ATOM   10691 C  C   . SER   F  6  188 ? 11.855  -102.435 86.380  1.00 121.68 ? 184 SER   F C   1 
ATOM   10692 O  O   . SER   F  6  188 ? 11.459  -101.303 86.038  1.00 117.64 ? 184 SER   F O   1 
ATOM   10693 C  CB  . SER   F  6  188 ? 11.464  -103.102 88.779  1.00 117.40 ? 184 SER   F CB  1 
ATOM   10694 O  OG  . SER   F  6  188 ? 10.246  -102.377 88.706  1.00 115.17 ? 184 SER   F OG  1 
ATOM   10695 N  N   . ALA   F  6  189 ? 11.788  -103.528 85.614  1.00 124.59 ? 185 ALA   F N   1 
ATOM   10696 C  CA  . ALA   F  6  189 ? 11.290  -103.566 84.218  1.00 125.77 ? 185 ALA   F CA  1 
ATOM   10697 C  C   . ALA   F  6  189 ? 9.886   -102.954 84.145  1.00 131.30 ? 185 ALA   F C   1 
ATOM   10698 O  O   . ALA   F  6  189 ? 9.663   -102.103 83.264  1.00 136.04 ? 185 ALA   F O   1 
ATOM   10699 C  CB  . ALA   F  6  189 ? 11.299  -104.984 83.703  1.00 124.43 ? 185 ALA   F CB  1 
ATOM   10700 N  N   . ARG   F  6  190 ? 8.986   -103.364 85.046  1.00 136.63 ? 186 ARG   F N   1 
ATOM   10701 C  CA  . ARG   F  6  190 ? 7.570   -102.902 85.090  1.00 137.35 ? 186 ARG   F CA  1 
ATOM   10702 C  C   . ARG   F  6  190 ? 7.505   -101.415 85.471  1.00 138.66 ? 186 ARG   F C   1 
ATOM   10703 O  O   . ARG   F  6  190 ? 6.617   -100.720 84.938  1.00 140.73 ? 186 ARG   F O   1 
ATOM   10704 C  CB  . ARG   F  6  190 ? 6.756   -103.758 86.066  1.00 139.34 ? 186 ARG   F CB  1 
ATOM   10705 C  CG  . ARG   F  6  190 ? 6.530   -105.186 85.593  1.00 138.06 ? 186 ARG   F CG  1 
ATOM   10706 C  CD  . ARG   F  6  190 ? 5.740   -106.004 86.597  1.00 141.92 ? 186 ARG   F CD  1 
ATOM   10707 N  NE  . ARG   F  6  190 ? 4.959   -107.061 85.965  1.00 141.50 ? 186 ARG   F NE  1 
ATOM   10708 C  CZ  . ARG   F  6  190 ? 3.749   -106.910 85.424  1.00 141.90 ? 186 ARG   F CZ  1 
ATOM   10709 N  NH1 . ARG   F  6  190 ? 3.150   -105.729 85.422  1.00 138.71 ? 186 ARG   F NH1 1 
ATOM   10710 N  NH2 . ARG   F  6  190 ? 3.141   -107.951 84.881  1.00 140.56 ? 186 ARG   F NH2 1 
ATOM   10711 N  N   . GLU   F  6  191 ? 8.391   -100.953 86.362  1.00 137.02 ? 187 GLU   F N   1 
ATOM   10712 C  CA  . GLU   F  6  191 ? 8.523   -99.518  86.749  1.00 137.85 ? 187 GLU   F CA  1 
ATOM   10713 C  C   . GLU   F  6  191 ? 8.984   -98.700  85.535  1.00 132.19 ? 187 GLU   F C   1 
ATOM   10714 O  O   . GLU   F  6  191 ? 8.375   -97.645  85.274  1.00 134.83 ? 187 GLU   F O   1 
ATOM   10715 C  CB  . GLU   F  6  191 ? 9.506   -99.328  87.910  1.00 138.65 ? 187 GLU   F CB  1 
ATOM   10716 C  CG  . GLU   F  6  191 ? 8.834   -99.143  89.261  1.00 144.92 ? 187 GLU   F CG  1 
ATOM   10717 C  CD  . GLU   F  6  191 ? 8.339   -97.733  89.542  1.00 146.97 ? 187 GLU   F CD  1 
ATOM   10718 O  OE1 . GLU   F  6  191 ? 9.172   -96.803  89.555  1.00 149.27 ? 187 GLU   F OE1 1 
ATOM   10719 O  OE2 . GLU   F  6  191 ? 7.120   -97.565  89.746  1.00 151.03 ? 187 GLU   F OE2 1 
ATOM   10720 N  N   . ALA   F  6  192 ? 10.021  -99.169  84.833  1.00 121.24 ? 188 ALA   F N   1 
ATOM   10721 C  CA  . ALA   F  6  192 ? 10.649  -98.485  83.676  1.00 118.37 ? 188 ALA   F CA  1 
ATOM   10722 C  C   . ALA   F  6  192 ? 9.630   -98.296  82.544  1.00 120.79 ? 188 ALA   F C   1 
ATOM   10723 O  O   . ALA   F  6  192 ? 9.700   -97.251  81.869  1.00 122.02 ? 188 ALA   F O   1 
ATOM   10724 C  CB  . ALA   F  6  192 ? 11.855  -99.259  83.206  1.00 114.06 ? 188 ALA   F CB  1 
ATOM   10725 N  N   . VAL   F  6  193 ? 8.730   -99.268  82.339  1.00 119.17 ? 189 VAL   F N   1 
ATOM   10726 C  CA  . VAL   F  6  193 ? 7.617   -99.192  81.342  1.00 118.66 ? 189 VAL   F CA  1 
ATOM   10727 C  C   . VAL   F  6  193 ? 6.727   -97.990  81.686  1.00 123.41 ? 189 VAL   F C   1 
ATOM   10728 O  O   . VAL   F  6  193 ? 6.384   -97.229  80.758  1.00 126.80 ? 189 VAL   F O   1 
ATOM   10729 C  CB  . VAL   F  6  193 ? 6.802   -100.500 81.281  1.00 114.47 ? 189 VAL   F CB  1 
ATOM   10730 C  CG1 . VAL   F  6  193 ? 5.501   -100.332 80.505  1.00 111.09 ? 189 VAL   F CG1 1 
ATOM   10731 C  CG2 . VAL   F  6  193 ? 7.618   -101.640 80.694  1.00 112.89 ? 189 VAL   F CG2 1 
ATOM   10732 N  N   . LYS   F  6  194 ? 6.369   -97.833  82.965  1.00 125.99 ? 190 LYS   F N   1 
ATOM   10733 C  CA  . LYS   F  6  194 ? 5.507   -96.730  83.473  1.00 128.17 ? 190 LYS   F CA  1 
ATOM   10734 C  C   . LYS   F  6  194 ? 6.235   -95.392  83.302  1.00 128.13 ? 190 LYS   F C   1 
ATOM   10735 O  O   . LYS   F  6  194 ? 5.599   -94.435  82.819  1.00 133.38 ? 190 LYS   F O   1 
ATOM   10736 C  CB  . LYS   F  6  194 ? 5.139   -96.953  84.944  1.00 132.28 ? 190 LYS   F CB  1 
ATOM   10737 C  CG  . LYS   F  6  194 ? 4.298   -98.193  85.219  1.00 131.92 ? 190 LYS   F CG  1 
ATOM   10738 C  CD  . LYS   F  6  194 ? 4.293   -98.621  86.673  1.00 135.17 ? 190 LYS   F CD  1 
ATOM   10739 C  CE  . LYS   F  6  194 ? 2.990   -98.326  87.384  1.00 137.99 ? 190 LYS   F CE  1 
ATOM   10740 N  NZ  . LYS   F  6  194 ? 2.922   -99.016  88.693  1.00 140.22 ? 190 LYS   F NZ  1 
ATOM   10741 N  N   . GLN   F  6  195 ? 7.513   -95.333  83.692  1.00 122.67 ? 191 GLN   F N   1 
ATOM   10742 C  CA  . GLN   F  6  195 ? 8.371   -94.121  83.589  1.00 121.15 ? 191 GLN   F CA  1 
ATOM   10743 C  C   . GLN   F  6  195 ? 8.492   -93.692  82.121  1.00 122.44 ? 191 GLN   F C   1 
ATOM   10744 O  O   . GLN   F  6  195 ? 8.394   -92.477  81.856  1.00 123.20 ? 191 GLN   F O   1 
ATOM   10745 C  CB  . GLN   F  6  195 ? 9.750   -94.381  84.199  1.00 120.98 ? 191 GLN   F CB  1 
ATOM   10746 C  CG  . GLN   F  6  195 ? 9.735   -94.522  85.717  1.00 123.37 ? 191 GLN   F CG  1 
ATOM   10747 C  CD  . GLN   F  6  195 ? 9.088   -93.358  86.429  1.00 123.23 ? 191 GLN   F CD  1 
ATOM   10748 O  OE1 . GLN   F  6  195 ? 8.190   -93.533  87.250  1.00 126.50 ? 191 GLN   F OE1 1 
ATOM   10749 N  NE2 . GLN   F  6  195 ? 9.541   -92.153  86.125  1.00 123.63 ? 191 GLN   F NE2 1 
ATOM   10750 N  N   . ALA   F  6  196 ? 8.694   -94.649  81.209  1.00 116.77 ? 192 ALA   F N   1 
ATOM   10751 C  CA  . ALA   F  6  196 ? 8.782   -94.424  79.746  1.00 113.90 ? 192 ALA   F CA  1 
ATOM   10752 C  C   . ALA   F  6  196 ? 7.525   -93.693  79.259  1.00 114.54 ? 192 ALA   F C   1 
ATOM   10753 O  O   . ALA   F  6  196 ? 7.670   -92.718  78.497  1.00 114.03 ? 192 ALA   F O   1 
ATOM   10754 C  CB  . ALA   F  6  196 ? 8.963   -95.733  79.019  1.00 110.47 ? 192 ALA   F CB  1 
ATOM   10755 N  N   . ALA   F  6  197 ? 6.344   -94.151  79.688  1.00 112.87 ? 193 ALA   F N   1 
ATOM   10756 C  CA  . ALA   F  6  197 ? 5.034   -93.542  79.361  1.00 115.13 ? 193 ALA   F CA  1 
ATOM   10757 C  C   . ALA   F  6  197 ? 4.989   -92.101  79.888  1.00 119.03 ? 193 ALA   F C   1 
ATOM   10758 O  O   . ALA   F  6  197 ? 4.544   -91.220  79.133  1.00 118.07 ? 193 ALA   F O   1 
ATOM   10759 C  CB  . ALA   F  6  197 ? 3.905   -94.378  79.916  1.00 113.98 ? 193 ALA   F CB  1 
ATOM   10760 N  N   . LYS   F  6  198 ? 5.452   -91.865  81.122  1.00 120.71 ? 194 LYS   F N   1 
ATOM   10761 C  CA  . LYS   F  6  198 ? 5.455   -90.517  81.756  1.00 125.12 ? 194 LYS   F CA  1 
ATOM   10762 C  C   . LYS   F  6  198 ? 6.345   -89.567  80.944  1.00 122.89 ? 194 LYS   F C   1 
ATOM   10763 O  O   . LYS   F  6  198 ? 5.914   -88.423  80.702  1.00 126.66 ? 194 LYS   F O   1 
ATOM   10764 C  CB  . LYS   F  6  198 ? 5.936   -90.566  83.211  1.00 129.16 ? 194 LYS   F CB  1 
ATOM   10765 C  CG  . LYS   F  6  198 ? 6.010   -89.205  83.896  1.00 132.85 ? 194 LYS   F CG  1 
ATOM   10766 C  CD  . LYS   F  6  198 ? 6.236   -89.270  85.390  1.00 133.09 ? 194 LYS   F CD  1 
ATOM   10767 C  CE  . LYS   F  6  198 ? 7.678   -89.535  85.764  1.00 131.84 ? 194 LYS   F CE  1 
ATOM   10768 N  NZ  . LYS   F  6  198 ? 8.528   -88.333  85.596  1.00 132.37 ? 194 LYS   F NZ  1 
ATOM   10769 N  N   . ILE   F  6  199 ? 7.536   -90.026  80.550  1.00 118.19 ? 195 ILE   F N   1 
ATOM   10770 C  CA  . ILE   F  6  199 ? 8.590   -89.191  79.896  1.00 114.81 ? 195 ILE   F CA  1 
ATOM   10771 C  C   . ILE   F  6  199 ? 8.147   -88.817  78.476  1.00 113.60 ? 195 ILE   F C   1 
ATOM   10772 O  O   . ILE   F  6  199 ? 8.404   -87.669  78.073  1.00 117.47 ? 195 ILE   F O   1 
ATOM   10773 C  CB  . ILE   F  6  199 ? 9.952   -89.914  79.923  1.00 112.59 ? 195 ILE   F CB  1 
ATOM   10774 C  CG1 . ILE   F  6  199 ? 10.461  -90.067  81.358  1.00 116.70 ? 195 ILE   F CG1 1 
ATOM   10775 C  CG2 . ILE   F  6  199 ? 10.972  -89.206  79.044  1.00 110.17 ? 195 ILE   F CG2 1 
ATOM   10776 C  CD1 . ILE   F  6  199 ? 11.410  -91.221  81.550  1.00 118.85 ? 195 ILE   F CD1 1 
ATOM   10777 N  N   . ILE   F  6  200 ? 7.519   -89.740  77.741  1.00 112.17 ? 196 ILE   F N   1 
ATOM   10778 C  CA  . ILE   F  6  200 ? 6.995   -89.477  76.366  1.00 112.24 ? 196 ILE   F CA  1 
ATOM   10779 C  C   . ILE   F  6  200 ? 5.905   -88.400  76.451  1.00 116.21 ? 196 ILE   F C   1 
ATOM   10780 O  O   . ILE   F  6  200 ? 5.903   -87.507  75.580  1.00 118.33 ? 196 ILE   F O   1 
ATOM   10781 C  CB  . ILE   F  6  200 ? 6.493   -90.773  75.693  1.00 110.49 ? 196 ILE   F CB  1 
ATOM   10782 C  CG1 . ILE   F  6  200 ? 7.653   -91.697  75.309  1.00 108.60 ? 196 ILE   F CG1 1 
ATOM   10783 C  CG2 . ILE   F  6  200 ? 5.602   -90.462  74.497  1.00 109.18 ? 196 ILE   F CG2 1 
ATOM   10784 C  CD1 . ILE   F  6  200 ? 8.536   -91.174  74.191  1.00 106.74 ? 196 ILE   F CD1 1 
ATOM   10785 N  N   . TYR   F  6  201 ? 5.025   -88.479  77.457  1.00 119.19 ? 197 TYR   F N   1 
ATOM   10786 C  CA  . TYR   F  6  201 ? 3.934   -87.497  77.714  1.00 124.34 ? 197 TYR   F CA  1 
ATOM   10787 C  C   . TYR   F  6  201 ? 4.533   -86.129  78.076  1.00 125.19 ? 197 TYR   F C   1 
ATOM   10788 O  O   . TYR   F  6  201 ? 4.009   -85.106  77.597  1.00 129.88 ? 197 TYR   F O   1 
ATOM   10789 C  CB  . TYR   F  6  201 ? 2.975   -88.000  78.800  1.00 127.95 ? 197 TYR   F CB  1 
ATOM   10790 C  CG  . TYR   F  6  201 ? 1.785   -88.773  78.287  1.00 128.87 ? 197 TYR   F CG  1 
ATOM   10791 C  CD1 . TYR   F  6  201 ? 1.853   -90.140  78.071  1.00 127.12 ? 197 TYR   F CD1 1 
ATOM   10792 C  CD2 . TYR   F  6  201 ? 0.583   -88.139  78.013  1.00 132.06 ? 197 TYR   F CD2 1 
ATOM   10793 C  CE1 . TYR   F  6  201 ? 0.766   -90.856  77.597  1.00 127.05 ? 197 TYR   F CE1 1 
ATOM   10794 C  CE2 . TYR   F  6  201 ? -0.514  -88.839  77.538  1.00 131.99 ? 197 TYR   F CE2 1 
ATOM   10795 C  CZ  . TYR   F  6  201 ? -0.424  -90.204  77.330  1.00 129.30 ? 197 TYR   F CZ  1 
ATOM   10796 O  OH  . TYR   F  6  201 ? -1.498  -90.903  76.862  1.00 131.54 ? 197 TYR   F OH  1 
ATOM   10797 N  N   . LEU   F  6  202 ? 5.593   -86.108  78.892  1.00 121.76 ? 198 LEU   F N   1 
ATOM   10798 C  CA  . LEU   F  6  202 ? 6.293   -84.862  79.315  1.00 122.68 ? 198 LEU   F CA  1 
ATOM   10799 C  C   . LEU   F  6  202 ? 7.061   -84.267  78.128  1.00 126.02 ? 198 LEU   F C   1 
ATOM   10800 O  O   . LEU   F  6  202 ? 7.093   -83.027  78.021  1.00 132.64 ? 198 LEU   F O   1 
ATOM   10801 C  CB  . LEU   F  6  202 ? 7.227   -85.158  80.496  1.00 119.66 ? 198 LEU   F CB  1 
ATOM   10802 C  CG  . LEU   F  6  202 ? 6.716   -84.722  81.870  1.00 123.29 ? 198 LEU   F CG  1 
ATOM   10803 C  CD1 . LEU   F  6  202 ? 5.323   -85.266  82.152  1.00 124.85 ? 198 LEU   F CD1 1 
ATOM   10804 C  CD2 . LEU   F  6  202 ? 7.681   -85.150  82.962  1.00 122.82 ? 198 LEU   F CD2 1 
ATOM   10805 N  N   . ALA   F  6  203 ? 7.642   -85.113  77.270  1.00 123.95 ? 199 ALA   F N   1 
ATOM   10806 C  CA  . ALA   F  6  203 ? 8.421   -84.706  76.075  1.00 126.03 ? 199 ALA   F CA  1 
ATOM   10807 C  C   . ALA   F  6  203 ? 7.484   -84.300  74.929  1.00 126.91 ? 199 ALA   F C   1 
ATOM   10808 O  O   . ALA   F  6  203 ? 7.991   -83.746  73.931  1.00 123.73 ? 199 ALA   F O   1 
ATOM   10809 C  CB  . ALA   F  6  203 ? 9.341   -85.822  75.647  1.00 126.50 ? 199 ALA   F CB  1 
ATOM   10810 N  N   . HIS   F  6  204 ? 6.180   -84.575  75.056  1.00 128.95 ? 200 HIS   F N   1 
ATOM   10811 C  CA  . HIS   F  6  204 ? 5.136   -84.225  74.054  1.00 133.11 ? 200 HIS   F CA  1 
ATOM   10812 C  C   . HIS   F  6  204 ? 4.800   -82.727  74.116  1.00 136.25 ? 200 HIS   F C   1 
ATOM   10813 O  O   . HIS   F  6  204 ? 4.201   -82.228  73.144  1.00 143.70 ? 200 HIS   F O   1 
ATOM   10814 C  CB  . HIS   F  6  204 ? 3.881   -85.087  74.247  1.00 130.00 ? 200 HIS   F CB  1 
ATOM   10815 C  CG  . HIS   F  6  204 ? 2.813   -84.801  73.247  1.00 130.75 ? 200 HIS   F CG  1 
ATOM   10816 N  ND1 . HIS   F  6  204 ? 2.977   -85.069  71.905  1.00 130.89 ? 200 HIS   F ND1 1 
ATOM   10817 C  CD2 . HIS   F  6  204 ? 1.585   -84.255  73.380  1.00 133.18 ? 200 HIS   F CD2 1 
ATOM   10818 C  CE1 . HIS   F  6  204 ? 1.894   -84.708  71.251  1.00 132.84 ? 200 HIS   F CE1 1 
ATOM   10819 N  NE2 . HIS   F  6  204 ? 1.022   -84.206  72.133  1.00 134.95 ? 200 HIS   F NE2 1 
ATOM   10820 N  N   . GLU   F  6  205 ? 5.167   -82.040  75.206  1.00 143.37 ? 201 GLU   F N   1 
ATOM   10821 C  CA  . GLU   F  6  205 ? 4.953   -80.576  75.397  1.00 148.97 ? 201 GLU   F CA  1 
ATOM   10822 C  C   . GLU   F  6  205 ? 5.643   -79.784  74.278  1.00 151.53 ? 201 GLU   F C   1 
ATOM   10823 O  O   . GLU   F  6  205 ? 5.160   -78.684  73.950  1.00 145.55 ? 201 GLU   F O   1 
ATOM   10824 C  CB  . GLU   F  6  205 ? 5.487   -80.118  76.756  1.00 148.91 ? 201 GLU   F CB  1 
ATOM   10825 C  CG  . GLU   F  6  205 ? 4.692   -80.645  77.937  1.00 151.71 ? 201 GLU   F CG  1 
ATOM   10826 C  CD  . GLU   F  6  205 ? 3.203   -80.355  77.875  1.00 154.23 ? 201 GLU   F CD  1 
ATOM   10827 O  OE1 . GLU   F  6  205 ? 2.411   -81.303  78.040  1.00 158.01 ? 201 GLU   F OE1 1 
ATOM   10828 O  OE2 . GLU   F  6  205 ? 2.839   -79.182  77.660  1.00 159.40 ? 201 GLU   F OE2 1 
ATOM   10829 N  N   . ASP   F  6  206 ? 6.730   -80.326  73.719  1.00 155.72 ? 202 ASP   F N   1 
ATOM   10830 C  CA  . ASP   F  6  206 ? 7.552   -79.686  72.657  1.00 164.92 ? 202 ASP   F CA  1 
ATOM   10831 C  C   . ASP   F  6  206 ? 6.988   -80.016  71.266  1.00 172.11 ? 202 ASP   F C   1 
ATOM   10832 O  O   . ASP   F  6  206 ? 7.670   -79.691  70.271  1.00 182.14 ? 202 ASP   F O   1 
ATOM   10833 C  CB  . ASP   F  6  206 ? 9.010   -80.138  72.782  1.00 161.92 ? 202 ASP   F CB  1 
ATOM   10834 C  CG  . ASP   F  6  206 ? 9.644   -79.830  74.129  1.00 164.71 ? 202 ASP   F CG  1 
ATOM   10835 O  OD1 . ASP   F  6  206 ? 9.048   -79.045  74.897  1.00 172.28 ? 202 ASP   F OD1 1 
ATOM   10836 O  OD2 . ASP   F  6  206 ? 10.731  -80.380  74.402  1.00 143.92 ? 202 ASP   F OD2 1 
ATOM   10837 N  N   . ASN   F  6  207 ? 5.794   -80.620  71.194  1.00 173.05 ? 203 ASN   F N   1 
ATOM   10838 C  CA  . ASN   F  6  207 ? 5.177   -81.126  69.935  1.00 167.77 ? 203 ASN   F CA  1 
ATOM   10839 C  C   . ASN   F  6  207 ? 3.648   -81.180  70.100  1.00 162.19 ? 203 ASN   F C   1 
ATOM   10840 O  O   . ASN   F  6  207 ? 3.028   -82.120  69.562  1.00 156.14 ? 203 ASN   F O   1 
ATOM   10841 C  CB  . ASN   F  6  207 ? 5.753   -82.505  69.586  1.00 168.82 ? 203 ASN   F CB  1 
ATOM   10842 C  CG  . ASN   F  6  207 ? 6.242   -82.640  68.158  1.00 170.19 ? 203 ASN   F CG  1 
ATOM   10843 O  OD1 . ASN   F  6  207 ? 7.243   -83.311  67.912  1.00 161.26 ? 203 ASN   F OD1 1 
ATOM   10844 N  ND2 . ASN   F  6  207 ? 5.547   -82.028  67.211  1.00 174.87 ? 203 ASN   F ND2 1 
ATOM   10845 N  N   . LYS   F  6  208 ? 3.062   -80.192  70.787  1.00 160.66 ? 204 LYS   F N   1 
ATOM   10846 C  CA  . LYS   F  6  208 ? 1.723   -80.298  71.436  1.00 156.02 ? 204 LYS   F CA  1 
ATOM   10847 C  C   . LYS   F  6  208 ? 0.582   -79.832  70.517  1.00 151.58 ? 204 LYS   F C   1 
ATOM   10848 O  O   . LYS   F  6  208 ? -0.571  -79.856  70.995  1.00 145.99 ? 204 LYS   F O   1 
ATOM   10849 C  CB  . LYS   F  6  208 ? 1.708   -79.503  72.747  1.00 157.98 ? 204 LYS   F CB  1 
ATOM   10850 C  CG  . LYS   F  6  208 ? 1.739   -77.987  72.599  1.00 158.34 ? 204 LYS   F CG  1 
ATOM   10851 C  CD  . LYS   F  6  208 ? 2.210   -77.263  73.841  1.00 158.46 ? 204 LYS   F CD  1 
ATOM   10852 C  CE  . LYS   F  6  208 ? 1.246   -77.377  75.002  1.00 156.19 ? 204 LYS   F CE  1 
ATOM   10853 N  NZ  . LYS   F  6  208 ? 1.653   -76.502  76.127  1.00 155.29 ? 204 LYS   F NZ  1 
ATOM   10854 N  N   . GLU   F  6  209 ? 0.857   -79.436  69.266  1.00 155.72 ? 205 GLU   F N   1 
ATOM   10855 C  CA  . GLU   F  6  209 ? -0.198  -79.045  68.286  1.00 157.19 ? 205 GLU   F CA  1 
ATOM   10856 C  C   . GLU   F  6  209 ? -1.076  -80.267  68.001  1.00 153.69 ? 205 GLU   F C   1 
ATOM   10857 O  O   . GLU   F  6  209 ? -2.271  -80.235  68.352  1.00 151.16 ? 205 GLU   F O   1 
ATOM   10858 C  CB  . GLU   F  6  209 ? 0.386   -78.512  66.974  1.00 162.49 ? 205 GLU   F CB  1 
ATOM   10859 C  CG  . GLU   F  6  209 ? 0.971   -77.115  67.077  1.00 165.02 ? 205 GLU   F CG  1 
ATOM   10860 C  CD  . GLU   F  6  209 ? 2.466   -77.059  67.340  1.00 171.01 ? 205 GLU   F CD  1 
ATOM   10861 O  OE1 . GLU   F  6  209 ? 3.081   -76.029  67.001  1.00 174.10 ? 205 GLU   F OE1 1 
ATOM   10862 O  OE2 . GLU   F  6  209 ? 3.011   -78.043  67.882  1.00 172.77 ? 205 GLU   F OE2 1 
ATOM   10863 N  N   . LYS   F  6  210 ? -0.487  -81.296  67.385  1.00 152.58 ? 206 LYS   F N   1 
ATOM   10864 C  CA  . LYS   F  6  210 ? -1.111  -82.626  67.164  1.00 150.45 ? 206 LYS   F CA  1 
ATOM   10865 C  C   . LYS   F  6  210 ? -1.001  -83.432  68.461  1.00 146.09 ? 206 LYS   F C   1 
ATOM   10866 O  O   . LYS   F  6  210 ? 0.087   -83.406  69.067  1.00 146.55 ? 206 LYS   F O   1 
ATOM   10867 C  CB  . LYS   F  6  210 ? -0.395  -83.372  66.032  1.00 150.68 ? 206 LYS   F CB  1 
ATOM   10868 C  CG  . LYS   F  6  210 ? -0.378  -82.672  64.679  1.00 152.22 ? 206 LYS   F CG  1 
ATOM   10869 C  CD  . LYS   F  6  210 ? -1.593  -82.963  63.820  1.00 151.64 ? 206 LYS   F CD  1 
ATOM   10870 C  CE  . LYS   F  6  210 ? -2.697  -81.937  63.968  1.00 154.26 ? 206 LYS   F CE  1 
ATOM   10871 N  NZ  . LYS   F  6  210 ? -2.412  -80.714  63.180  1.00 153.64 ? 206 LYS   F NZ  1 
ATOM   10872 N  N   . ASP   F  6  211 ? -2.077  -84.110  68.874  1.00 143.68 ? 207 ASP   F N   1 
ATOM   10873 C  CA  . ASP   F  6  211 ? -2.030  -85.137  69.951  1.00 142.50 ? 207 ASP   F CA  1 
ATOM   10874 C  C   . ASP   F  6  211 ? -1.436  -86.411  69.336  1.00 138.67 ? 207 ASP   F C   1 
ATOM   10875 O  O   . ASP   F  6  211 ? -1.349  -86.477  68.091  1.00 136.64 ? 207 ASP   F O   1 
ATOM   10876 C  CB  . ASP   F  6  211 ? -3.394  -85.337  70.620  1.00 148.10 ? 207 ASP   F CB  1 
ATOM   10877 C  CG  . ASP   F  6  211 ? -4.493  -85.851  69.706  1.00 149.07 ? 207 ASP   F CG  1 
ATOM   10878 O  OD1 . ASP   F  6  211 ? -4.382  -85.651  68.480  1.00 155.62 ? 207 ASP   F OD1 1 
ATOM   10879 O  OD2 . ASP   F  6  211 ? -5.458  -86.440  70.232  1.00 154.52 ? 207 ASP   F OD2 1 
ATOM   10880 N  N   . PHE   F  6  212 ? -1.035  -87.375  70.168  1.00 136.72 ? 208 PHE   F N   1 
ATOM   10881 C  CA  . PHE   F  6  212 ? -0.123  -88.484  69.778  1.00 133.20 ? 208 PHE   F CA  1 
ATOM   10882 C  C   . PHE   F  6  212 ? -0.659  -89.838  70.254  1.00 127.62 ? 208 PHE   F C   1 
ATOM   10883 O  O   . PHE   F  6  212 ? -1.661  -89.888  70.994  1.00 130.82 ? 208 PHE   F O   1 
ATOM   10884 C  CB  . PHE   F  6  212 ? 1.277   -88.235  70.345  1.00 130.91 ? 208 PHE   F CB  1 
ATOM   10885 C  CG  . PHE   F  6  212 ? 1.399   -88.446  71.834  1.00 132.71 ? 208 PHE   F CG  1 
ATOM   10886 C  CD1 . PHE   F  6  212 ? 0.858   -87.535  72.730  1.00 132.24 ? 208 PHE   F CD1 1 
ATOM   10887 C  CD2 . PHE   F  6  212 ? 2.055   -89.557  72.340  1.00 133.23 ? 208 PHE   F CD2 1 
ATOM   10888 C  CE1 . PHE   F  6  212 ? 0.970   -87.733  74.098  1.00 131.29 ? 208 PHE   F CE1 1 
ATOM   10889 C  CE2 . PHE   F  6  212 ? 2.168   -89.752  73.708  1.00 132.20 ? 208 PHE   F CE2 1 
ATOM   10890 C  CZ  . PHE   F  6  212 ? 1.625   -88.840  74.584  1.00 131.35 ? 208 PHE   F CZ  1 
ATOM   10891 N  N   . GLU   F  6  213 ? 0.016   -90.905  69.819  1.00 125.31 ? 209 GLU   F N   1 
ATOM   10892 C  CA  . GLU   F  6  213 ? -0.223  -92.311  70.238  1.00 125.85 ? 209 GLU   F CA  1 
ATOM   10893 C  C   . GLU   F  6  213 ? 1.069   -92.856  70.854  1.00 119.53 ? 209 GLU   F C   1 
ATOM   10894 O  O   . GLU   F  6  213 ? 2.131   -92.721  70.216  1.00 117.74 ? 209 GLU   F O   1 
ATOM   10895 C  CB  . GLU   F  6  213 ? -0.660  -93.154  69.041  1.00 126.84 ? 209 GLU   F CB  1 
ATOM   10896 C  CG  . GLU   F  6  213 ? -1.104  -94.555  69.416  1.00 130.46 ? 209 GLU   F CG  1 
ATOM   10897 C  CD  . GLU   F  6  213 ? -1.737  -95.327  68.272  1.00 136.86 ? 209 GLU   F CD  1 
ATOM   10898 O  OE1 . GLU   F  6  213 ? -2.581  -94.742  67.563  1.00 139.07 ? 209 GLU   F OE1 1 
ATOM   10899 O  OE2 . GLU   F  6  213 ? -1.378  -96.509  68.088  1.00 141.55 ? 209 GLU   F OE2 1 
ATOM   10900 N  N   . LEU   F  6  214 ? 0.975   -93.441  72.050  1.00 115.71 ? 210 LEU   F N   1 
ATOM   10901 C  CA  . LEU   F  6  214 ? 2.135   -93.991  72.797  1.00 113.92 ? 210 LEU   F CA  1 
ATOM   10902 C  C   . LEU   F  6  214 ? 2.385   -95.429  72.332  1.00 111.62 ? 210 LEU   F C   1 
ATOM   10903 O  O   . LEU   F  6  214 ? 1.400   -96.170  72.151  1.00 114.89 ? 210 LEU   F O   1 
ATOM   10904 C  CB  . LEU   F  6  214 ? 1.839   -93.924  74.299  1.00 114.13 ? 210 LEU   F CB  1 
ATOM   10905 C  CG  . LEU   F  6  214 ? 2.874   -94.573  75.216  1.00 114.09 ? 210 LEU   F CG  1 
ATOM   10906 C  CD1 . LEU   F  6  214 ? 4.227   -93.886  75.100  1.00 113.57 ? 210 LEU   F CD1 1 
ATOM   10907 C  CD2 . LEU   F  6  214 ? 2.390   -94.555  76.657  1.00 116.79 ? 210 LEU   F CD2 1 
ATOM   10908 N  N   . GLU   F  6  215 ? 3.657   -95.788  72.134  1.00 112.48 ? 211 GLU   F N   1 
ATOM   10909 C  CA  . GLU   F  6  215 ? 4.107   -97.157  71.767  1.00 112.28 ? 211 GLU   F CA  1 
ATOM   10910 C  C   . GLU   F  6  215 ? 5.302   -97.535  72.649  1.00 108.71 ? 211 GLU   F C   1 
ATOM   10911 O  O   . GLU   F  6  215 ? 6.299   -96.790  72.629  1.00 110.04 ? 211 GLU   F O   1 
ATOM   10912 C  CB  . GLU   F  6  215 ? 4.469   -97.212  70.283  1.00 115.41 ? 211 GLU   F CB  1 
ATOM   10913 C  CG  . GLU   F  6  215 ? 4.713   -98.619  69.768  1.00 118.18 ? 211 GLU   F CG  1 
ATOM   10914 C  CD  . GLU   F  6  215 ? 4.885   -98.716  68.261  1.00 120.64 ? 211 GLU   F CD  1 
ATOM   10915 O  OE1 . GLU   F  6  215 ? 5.980   -99.115  67.815  1.00 123.46 ? 211 GLU   F OE1 1 
ATOM   10916 O  OE2 . GLU   F  6  215 ? 3.922   -98.398  67.535  1.00 121.52 ? 211 GLU   F OE2 1 
ATOM   10917 N  N   . ILE   F  6  216 ? 5.194   -98.642  73.392  1.00 108.08 ? 212 ILE   F N   1 
ATOM   10918 C  CA  . ILE   F  6  216 ? 6.252   -99.153  74.315  1.00 108.16 ? 212 ILE   F CA  1 
ATOM   10919 C  C   . ILE   F  6  216 ? 6.576   -100.607 73.948  1.00 108.31 ? 212 ILE   F C   1 
ATOM   10920 O  O   . ILE   F  6  216 ? 5.649   -101.344 73.552  1.00 110.21 ? 212 ILE   F O   1 
ATOM   10921 C  CB  . ILE   F  6  216 ? 5.822   -99.032  75.792  1.00 105.73 ? 212 ILE   F CB  1 
ATOM   10922 C  CG1 . ILE   F  6  216 ? 5.240   -97.655  76.121  1.00 106.37 ? 212 ILE   F CG1 1 
ATOM   10923 C  CG2 . ILE   F  6  216 ? 6.980   -99.383  76.716  1.00 104.40 ? 212 ILE   F CG2 1 
ATOM   10924 C  CD1 . ILE   F  6  216 ? 4.556   -97.586  77.466  1.00 108.91 ? 212 ILE   F CD1 1 
ATOM   10925 N  N   . SER   F  6  217 ? 7.851   -100.987 74.081  1.00 110.18 ? 213 SER   F N   1 
ATOM   10926 C  CA  . SER   F  6  217 ? 8.353   -102.386 74.030  1.00 109.95 ? 213 SER   F CA  1 
ATOM   10927 C  C   . SER   F  6  217 ? 9.371   -102.594 75.158  1.00 110.49 ? 213 SER   F C   1 
ATOM   10928 O  O   . SER   F  6  217 ? 9.761   -101.594 75.792  1.00 113.93 ? 213 SER   F O   1 
ATOM   10929 C  CB  . SER   F  6  217 ? 8.945   -102.704 72.681  1.00 109.05 ? 213 SER   F CB  1 
ATOM   10930 O  OG  . SER   F  6  217 ? 10.185  -102.035 72.499  1.00 105.56 ? 213 SER   F OG  1 
ATOM   10931 N  N   . TRP   F  6  218 ? 9.793   -103.840 75.395  1.00 110.35 ? 214 TRP   F N   1 
ATOM   10932 C  CA  . TRP   F  6  218 ? 10.752  -104.188 76.479  1.00 108.12 ? 214 TRP   F CA  1 
ATOM   10933 C  C   . TRP   F  6  218 ? 11.380  -105.567 76.252  1.00 106.71 ? 214 TRP   F C   1 
ATOM   10934 O  O   . TRP   F  6  218 ? 10.718  -106.443 75.660  1.00 100.48 ? 214 TRP   F O   1 
ATOM   10935 C  CB  . TRP   F  6  218 ? 10.085  -104.087 77.861  1.00 106.89 ? 214 TRP   F CB  1 
ATOM   10936 C  CG  . TRP   F  6  218 ? 8.927   -105.007 78.104  1.00 105.94 ? 214 TRP   F CG  1 
ATOM   10937 C  CD1 . TRP   F  6  218 ? 8.128   -105.616 77.179  1.00 106.33 ? 214 TRP   F CD1 1 
ATOM   10938 C  CD2 . TRP   F  6  218 ? 8.397   -105.381 79.388  1.00 105.79 ? 214 TRP   F CD2 1 
ATOM   10939 N  NE1 . TRP   F  6  218 ? 7.159   -106.361 77.796  1.00 106.18 ? 214 TRP   F NE1 1 
ATOM   10940 C  CE2 . TRP   F  6  218 ? 7.296   -106.233 79.152  1.00 107.59 ? 214 TRP   F CE2 1 
ATOM   10941 C  CE3 . TRP   F  6  218 ? 8.750   -105.088 80.710  1.00 105.48 ? 214 TRP   F CE3 1 
ATOM   10942 C  CZ2 . TRP   F  6  218 ? 6.550   -106.792 80.189  1.00 110.05 ? 214 TRP   F CZ2 1 
ATOM   10943 C  CZ3 . TRP   F  6  218 ? 8.012   -105.640 81.735  1.00 110.42 ? 214 TRP   F CZ3 1 
ATOM   10944 C  CH2 . TRP   F  6  218 ? 6.927   -106.480 81.475  1.00 112.26 ? 214 TRP   F CH2 1 
ATOM   10945 N  N   . CYS   F  6  219 ? 12.635  -105.709 76.685  1.00 110.98 ? 215 CYS   F N   1 
ATOM   10946 C  CA  . CYS   F  6  219 ? 13.348  -106.992 76.913  1.00 114.26 ? 215 CYS   F CA  1 
ATOM   10947 C  C   . CYS   F  6  219 ? 13.708  -107.072 78.396  1.00 114.39 ? 215 CYS   F C   1 
ATOM   10948 O  O   . CYS   F  6  219 ? 14.296  -106.101 78.899  1.00 112.71 ? 215 CYS   F O   1 
ATOM   10949 C  CB  . CYS   F  6  219 ? 14.627  -107.091 76.092  1.00 124.53 ? 215 CYS   F CB  1 
ATOM   10950 S  SG  . CYS   F  6  219 ? 14.406  -106.660 74.348  1.00 142.88 ? 215 CYS   F SG  1 
ATOM   10951 N  N   . SER   F  6  220 ? 13.349  -108.171 79.064  1.00 113.50 ? 216 SER   F N   1 
ATOM   10952 C  CA  . SER   F  6  220 ? 13.639  -108.418 80.500  1.00 112.12 ? 216 SER   F CA  1 
ATOM   10953 C  C   . SER   F  6  220 ? 13.891  -109.912 80.729  1.00 109.62 ? 216 SER   F C   1 
ATOM   10954 O  O   . SER   F  6  220 ? 13.091  -110.733 80.236  1.00 108.66 ? 216 SER   F O   1 
ATOM   10955 C  CB  . SER   F  6  220 ? 12.523  -107.904 81.367  1.00 113.06 ? 216 SER   F CB  1 
ATOM   10956 O  OG  . SER   F  6  220 ? 12.726  -108.260 82.727  1.00 113.85 ? 216 SER   F OG  1 
ATOM   10957 N  N   . LEU   F  6  221 ? 14.965  -110.233 81.457  1.00 109.53 ? 217 LEU   F N   1 
ATOM   10958 C  CA  . LEU   F  6  221 ? 15.409  -111.620 81.758  1.00 108.07 ? 217 LEU   F CA  1 
ATOM   10959 C  C   . LEU   F  6  221 ? 14.318  -112.352 82.549  1.00 108.06 ? 217 LEU   F C   1 
ATOM   10960 O  O   . LEU   F  6  221 ? 14.189  -113.572 82.359  1.00 111.52 ? 217 LEU   F O   1 
ATOM   10961 C  CB  . LEU   F  6  221 ? 16.724  -111.560 82.542  1.00 110.33 ? 217 LEU   F CB  1 
ATOM   10962 C  CG  . LEU   F  6  221 ? 17.373  -112.901 82.882  1.00 112.58 ? 217 LEU   F CG  1 
ATOM   10963 C  CD1 . LEU   F  6  221 ? 17.748  -113.672 81.624  1.00 108.68 ? 217 LEU   F CD1 1 
ATOM   10964 C  CD2 . LEU   F  6  221 ? 18.598  -112.691 83.761  1.00 115.55 ? 217 LEU   F CD2 1 
ATOM   10965 N  N   . SER   F  6  222 ? 13.564  -111.637 83.393  1.00 104.39 ? 218 SER   F N   1 
ATOM   10966 C  CA  . SER   F  6  222 ? 12.498  -112.206 84.261  1.00 108.97 ? 218 SER   F CA  1 
ATOM   10967 C  C   . SER   F  6  222 ? 11.113  -112.023 83.626  1.00 112.90 ? 218 SER   F C   1 
ATOM   10968 O  O   . SER   F  6  222 ? 10.334  -112.996 83.644  1.00 122.56 ? 218 SER   F O   1 
ATOM   10969 C  CB  . SER   F  6  222 ? 12.543  -111.605 85.638  1.00 108.47 ? 218 SER   F CB  1 
ATOM   10970 O  OG  . SER   F  6  222 ? 12.313  -110.205 85.586  1.00 108.25 ? 218 SER   F OG  1 
ATOM   10971 N  N   . GLU   F  6  223 ? 10.810  -110.832 83.097  1.00 113.38 ? 219 GLU   F N   1 
ATOM   10972 C  CA  . GLU   F  6  223 ? 9.439   -110.447 82.658  1.00 116.11 ? 219 GLU   F CA  1 
ATOM   10973 C  C   . GLU   F  6  223 ? 9.128   -111.003 81.260  1.00 112.44 ? 219 GLU   F C   1 
ATOM   10974 O  O   . GLU   F  6  223 ? 7.980   -111.445 81.067  1.00 118.31 ? 219 GLU   F O   1 
ATOM   10975 C  CB  . GLU   F  6  223 ? 9.259   -108.928 82.698  1.00 118.17 ? 219 GLU   F CB  1 
ATOM   10976 C  CG  . GLU   F  6  223 ? 9.236   -108.358 84.105  1.00 121.73 ? 219 GLU   F CG  1 
ATOM   10977 C  CD  . GLU   F  6  223 ? 8.001   -108.710 84.918  1.00 123.71 ? 219 GLU   F CD  1 
ATOM   10978 O  OE1 . GLU   F  6  223 ? 8.114   -108.779 86.157  1.00 129.76 ? 219 GLU   F OE1 1 
ATOM   10979 O  OE2 . GLU   F  6  223 ? 6.927   -108.912 84.311  1.00 117.81 ? 219 GLU   F OE2 1 
ATOM   10980 N  N   . THR   F  6  224 ? 10.078  -110.970 80.317  1.00 110.82 ? 220 THR   F N   1 
ATOM   10981 C  CA  . THR   F  6  224 ? 9.867   -111.419 78.909  1.00 113.23 ? 220 THR   F CA  1 
ATOM   10982 C  C   . THR   F  6  224 ? 10.805  -112.575 78.536  1.00 111.64 ? 220 THR   F C   1 
ATOM   10983 O  O   . THR   F  6  224 ? 10.809  -112.956 77.347  1.00 112.07 ? 220 THR   F O   1 
ATOM   10984 C  CB  . THR   F  6  224 ? 10.038  -110.266 77.912  1.00 112.00 ? 220 THR   F CB  1 
ATOM   10985 O  OG1 . THR   F  6  224 ? 11.388  -109.802 77.974  1.00 109.47 ? 220 THR   F OG1 1 
ATOM   10986 C  CG2 . THR   F  6  224 ? 9.085   -109.122 78.176  1.00 114.31 ? 220 THR   F CG2 1 
ATOM   10987 N  N   . ASN   F  6  225 ? 11.560  -113.115 79.498  1.00 114.30 ? 221 ASN   F N   1 
ATOM   10988 C  CA  . ASN   F  6  225 ? 12.418  -114.318 79.315  1.00 113.70 ? 221 ASN   F CA  1 
ATOM   10989 C  C   . ASN   F  6  225 ? 13.589  -113.991 78.375  1.00 107.81 ? 221 ASN   F C   1 
ATOM   10990 O  O   . ASN   F  6  225 ? 14.098  -114.923 77.722  1.00 102.64 ? 221 ASN   F O   1 
ATOM   10991 C  CB  . ASN   F  6  225 ? 11.584  -115.503 78.816  1.00 116.51 ? 221 ASN   F CB  1 
ATOM   10992 C  CG  . ASN   F  6  225 ? 11.928  -116.797 79.520  1.00 118.78 ? 221 ASN   F CG  1 
ATOM   10993 O  OD1 . ASN   F  6  225 ? 11.189  -117.240 80.396  1.00 123.31 ? 221 ASN   F OD1 1 
ATOM   10994 N  ND2 . ASN   F  6  225 ? 13.051  -117.396 79.158  1.00 122.92 ? 221 ASN   F ND2 1 
ATOM   10995 N  N   . GLY   F  6  226 ? 14.007  -112.720 78.319  1.00 108.69 ? 222 GLY   F N   1 
ATOM   10996 C  CA  . GLY   F  6  226 ? 15.175  -112.253 77.545  1.00 107.23 ? 222 GLY   F CA  1 
ATOM   10997 C  C   . GLY   F  6  226 ? 14.836  -111.906 76.103  1.00 106.65 ? 222 GLY   F C   1 
ATOM   10998 O  O   . GLY   F  6  226 ? 15.749  -111.445 75.386  1.00 107.42 ? 222 GLY   F O   1 
ATOM   10999 N  N   . LEU   F  6  227 ? 13.581  -112.104 75.686  1.00 105.69 ? 223 LEU   F N   1 
ATOM   11000 C  CA  . LEU   F  6  227 ? 13.113  -111.866 74.294  1.00 107.39 ? 223 LEU   F CA  1 
ATOM   11001 C  C   . LEU   F  6  227 ? 12.439  -110.494 74.210  1.00 108.59 ? 223 LEU   F C   1 
ATOM   11002 O  O   . LEU   F  6  227 ? 11.897  -110.036 75.238  1.00 108.92 ? 223 LEU   F O   1 
ATOM   11003 C  CB  . LEU   F  6  227 ? 12.137  -112.973 73.885  1.00 109.32 ? 223 LEU   F CB  1 
ATOM   11004 C  CG  . LEU   F  6  227 ? 12.675  -114.401 73.966  1.00 110.61 ? 223 LEU   F CG  1 
ATOM   11005 C  CD1 . LEU   F  6  227 ? 11.580  -115.404 73.640  1.00 111.25 ? 223 LEU   F CD1 1 
ATOM   11006 C  CD2 . LEU   F  6  227 ? 13.868  -114.595 73.039  1.00 110.29 ? 223 LEU   F CD2 1 
ATOM   11007 N  N   . HIS   F  6  228 ? 12.475  -109.878 73.024  1.00 107.56 ? 224 HIS   F N   1 
ATOM   11008 C  CA  . HIS   F  6  228 ? 11.807  -108.584 72.719  1.00 106.64 ? 224 HIS   F CA  1 
ATOM   11009 C  C   . HIS   F  6  228 ? 10.302  -108.814 72.566  1.00 105.89 ? 224 HIS   F C   1 
ATOM   11010 O  O   . HIS   F  6  228 ? 9.917   -109.714 71.798  1.00 105.69 ? 224 HIS   F O   1 
ATOM   11011 C  CB  . HIS   F  6  228 ? 12.398  -107.937 71.461  1.00 106.05 ? 224 HIS   F CB  1 
ATOM   11012 C  CG  . HIS   F  6  228 ? 11.861  -106.571 71.198  1.00 110.32 ? 224 HIS   F CG  1 
ATOM   11013 N  ND1 . HIS   F  6  228 ? 10.824  -106.340 70.314  1.00 113.16 ? 224 HIS   F ND1 1 
ATOM   11014 C  CD2 . HIS   F  6  228 ? 12.196  -105.368 71.714  1.00 109.83 ? 224 HIS   F CD2 1 
ATOM   11015 C  CE1 . HIS   F  6  228 ? 10.553  -105.051 70.289  1.00 114.11 ? 224 HIS   F CE1 1 
ATOM   11016 N  NE2 . HIS   F  6  228 ? 11.382  -104.432 71.138  1.00 113.75 ? 224 HIS   F NE2 1 
ATOM   11017 N  N   . LYS   F  6  229 ? 9.493   -108.022 73.273  1.00 109.55 ? 225 LYS   F N   1 
ATOM   11018 C  CA  . LYS   F  6  229 ? 8.010   -108.078 73.221  1.00 113.68 ? 225 LYS   F CA  1 
ATOM   11019 C  C   . LYS   F  6  229 ? 7.460   -106.649 73.244  1.00 109.92 ? 225 LYS   F C   1 
ATOM   11020 O  O   . LYS   F  6  229 ? 8.063   -105.793 73.918  1.00 103.13 ? 225 LYS   F O   1 
ATOM   11021 C  CB  . LYS   F  6  229 ? 7.463   -108.896 74.396  1.00 117.47 ? 225 LYS   F CB  1 
ATOM   11022 C  CG  . LYS   F  6  229 ? 7.806   -110.380 74.377  1.00 124.64 ? 225 LYS   F CG  1 
ATOM   11023 C  CD  . LYS   F  6  229 ? 7.007   -111.190 75.381  1.00 129.11 ? 225 LYS   F CD  1 
ATOM   11024 C  CE  . LYS   F  6  229 ? 7.632   -112.527 75.720  1.00 131.22 ? 225 LYS   F CE  1 
ATOM   11025 N  NZ  . LYS   F  6  229 ? 7.603   -113.462 74.570  1.00 135.21 ? 225 LYS   F NZ  1 
ATOM   11026 N  N   . PHE   F  6  230 ? 6.371   -106.407 72.513  1.00 111.96 ? 226 PHE   F N   1 
ATOM   11027 C  CA  . PHE   F  6  230 ? 5.594   -105.141 72.550  1.00 114.04 ? 226 PHE   F CA  1 
ATOM   11028 C  C   . PHE   F  6  230 ? 4.682   -105.152 73.778  1.00 115.39 ? 226 PHE   F C   1 
ATOM   11029 O  O   . PHE   F  6  230 ? 4.073   -106.201 74.064  1.00 117.51 ? 226 PHE   F O   1 
ATOM   11030 C  CB  . PHE   F  6  230 ? 4.774   -104.963 71.271  1.00 112.60 ? 226 PHE   F CB  1 
ATOM   11031 C  CG  . PHE   F  6  230 ? 5.595   -104.601 70.063  1.00 111.68 ? 226 PHE   F CG  1 
ATOM   11032 C  CD1 . PHE   F  6  230 ? 6.132   -105.586 69.250  1.00 112.85 ? 226 PHE   F CD1 1 
ATOM   11033 C  CD2 . PHE   F  6  230 ? 5.842   -103.275 69.749  1.00 108.64 ? 226 PHE   F CD2 1 
ATOM   11034 C  CE1 . PHE   F  6  230 ? 6.892   -105.252 68.140  1.00 110.58 ? 226 PHE   F CE1 1 
ATOM   11035 C  CE2 . PHE   F  6  230 ? 6.600   -102.943 68.638  1.00 108.43 ? 226 PHE   F CE2 1 
ATOM   11036 C  CZ  . PHE   F  6  230 ? 7.124   -103.931 67.837  1.00 109.96 ? 226 PHE   F CZ  1 
ATOM   11037 N  N   . VAL   F  6  231 ? 4.597   -104.015 74.473  1.00 117.67 ? 227 VAL   F N   1 
ATOM   11038 C  CA  . VAL   F  6  231 ? 3.662   -103.792 75.615  1.00 119.08 ? 227 VAL   F CA  1 
ATOM   11039 C  C   . VAL   F  6  231 ? 2.287   -103.448 75.034  1.00 119.12 ? 227 VAL   F C   1 
ATOM   11040 O  O   . VAL   F  6  231 ? 2.176   -102.397 74.375  1.00 114.73 ? 227 VAL   F O   1 
ATOM   11041 C  CB  . VAL   F  6  231 ? 4.172   -102.684 76.555  1.00 122.09 ? 227 VAL   F CB  1 
ATOM   11042 C  CG1 . VAL   F  6  231 ? 3.191   -102.406 77.685  1.00 124.82 ? 227 VAL   F CG1 1 
ATOM   11043 C  CG2 . VAL   F  6  231 ? 5.552   -103.008 77.110  1.00 121.67 ? 227 VAL   F CG2 1 
ATOM   11044 N  N   . LYS   F  6  232 ? 1.288   -104.307 75.264  1.00 123.68 ? 228 LYS   F N   1 
ATOM   11045 C  CA  . LYS   F  6  232 ? -0.083  -104.169 74.700  1.00 129.28 ? 228 LYS   F CA  1 
ATOM   11046 C  C   . LYS   F  6  232 ? -1.128  -104.395 75.797  1.00 129.09 ? 228 LYS   F C   1 
ATOM   11047 O  O   . LYS   F  6  232 ? -0.766  -104.916 76.874  1.00 126.27 ? 228 LYS   F O   1 
ATOM   11048 C  CB  . LYS   F  6  232 ? -0.309  -105.177 73.569  1.00 134.02 ? 228 LYS   F CB  1 
ATOM   11049 C  CG  . LYS   F  6  232 ? 0.778   -105.224 72.499  1.00 136.53 ? 228 LYS   F CG  1 
ATOM   11050 C  CD  . LYS   F  6  232 ? 1.009   -106.591 71.867  1.00 140.50 ? 228 LYS   F CD  1 
ATOM   11051 C  CE  . LYS   F  6  232 ? 1.131   -107.740 72.851  1.00 144.55 ? 228 LYS   F CE  1 
ATOM   11052 N  NZ  . LYS   F  6  232 ? 0.523   -108.982 72.318  1.00 146.63 ? 228 LYS   F NZ  1 
ATOM   11053 N  N   . GLY   F  6  233 ? -2.376  -104.015 75.508  1.00 130.81 ? 229 GLY   F N   1 
ATOM   11054 C  CA  . GLY   F  6  233 ? -3.566  -104.286 76.338  1.00 131.93 ? 229 GLY   F CA  1 
ATOM   11055 C  C   . GLY   F  6  233 ? -3.452  -103.696 77.734  1.00 131.87 ? 229 GLY   F C   1 
ATOM   11056 O  O   . GLY   F  6  233 ? -3.202  -102.480 77.841  1.00 129.68 ? 229 GLY   F O   1 
ATOM   11057 N  N   . ASP   F  6  234 ? -3.627  -104.536 78.760  1.00 132.42 ? 230 ASP   F N   1 
ATOM   11058 C  CA  . ASP   F  6  234 ? -3.764  -104.138 80.188  1.00 133.08 ? 230 ASP   F CA  1 
ATOM   11059 C  C   . ASP   F  6  234 ? -2.504  -103.411 80.670  1.00 133.81 ? 230 ASP   F C   1 
ATOM   11060 O  O   . ASP   F  6  234 ? -2.657  -102.393 81.374  1.00 137.32 ? 230 ASP   F O   1 
ATOM   11061 C  CB  . ASP   F  6  234 ? -4.064  -105.350 81.074  1.00 132.87 ? 230 ASP   F CB  1 
ATOM   11062 C  CG  . ASP   F  6  234 ? -5.496  -105.846 80.971  1.00 136.44 ? 230 ASP   F CG  1 
ATOM   11063 O  OD1 . ASP   F  6  234 ? -6.241  -105.320 80.118  1.00 137.83 ? 230 ASP   F OD1 1 
ATOM   11064 O  OD2 . ASP   F  6  234 ? -5.854  -106.754 81.745  1.00 140.28 ? 230 ASP   F OD2 1 
ATOM   11065 N  N   . LEU   F  6  235 ? -1.314  -103.913 80.321  1.00 130.03 ? 231 LEU   F N   1 
ATOM   11066 C  CA  . LEU   F  6  235 ? -0.015  -103.344 80.777  1.00 131.50 ? 231 LEU   F CA  1 
ATOM   11067 C  C   . LEU   F  6  235 ? 0.211   -101.969 80.133  1.00 131.28 ? 231 LEU   F C   1 
ATOM   11068 O  O   . LEU   F  6  235 ? 0.803   -101.101 80.805  1.00 137.75 ? 231 LEU   F O   1 
ATOM   11069 C  CB  . LEU   F  6  235 ? 1.125   -104.309 80.435  1.00 128.70 ? 231 LEU   F CB  1 
ATOM   11070 C  CG  . LEU   F  6  235 ? 2.465   -104.004 81.107  1.00 130.51 ? 231 LEU   F CG  1 
ATOM   11071 C  CD1 . LEU   F  6  235 ? 2.359   -104.109 82.622  1.00 130.77 ? 231 LEU   F CD1 1 
ATOM   11072 C  CD2 . LEU   F  6  235 ? 3.557   -104.928 80.590  1.00 127.85 ? 231 LEU   F CD2 1 
ATOM   11073 N  N   . LEU   F  6  236 ? -0.236  -101.781 78.884  1.00 132.23 ? 232 LEU   F N   1 
ATOM   11074 C  CA  . LEU   F  6  236 ? -0.116  -100.498 78.137  1.00 129.11 ? 232 LEU   F CA  1 
ATOM   11075 C  C   . LEU   F  6  236 ? -1.069  -99.457  78.740  1.00 125.08 ? 232 LEU   F C   1 
ATOM   11076 O  O   . LEU   F  6  236 ? -0.602  -98.339  79.014  1.00 132.92 ? 232 LEU   F O   1 
ATOM   11077 C  CB  . LEU   F  6  236 ? -0.422  -100.727 76.653  1.00 124.97 ? 232 LEU   F CB  1 
ATOM   11078 C  CG  . LEU   F  6  236 ? -0.250  -99.506  75.748  1.00 121.76 ? 232 LEU   F CG  1 
ATOM   11079 C  CD1 . LEU   F  6  236 ? 1.217   -99.123  75.615  1.00 118.47 ? 232 LEU   F CD1 1 
ATOM   11080 C  CD2 . LEU   F  6  236 ? -0.862  -99.756  74.378  1.00 120.59 ? 232 LEU   F CD2 1 
ATOM   11081 N  N   . GLN   F  6  237 ? -2.348  -99.804  78.927  1.00 125.10 ? 233 GLN   F N   1 
ATOM   11082 C  CA  . GLN   F  6  237 ? -3.390  -98.878  79.454  1.00 125.34 ? 233 GLN   F CA  1 
ATOM   11083 C  C   . GLN   F  6  237 ? -3.034  -98.465  80.888  1.00 124.09 ? 233 GLN   F C   1 
ATOM   11084 O  O   . GLN   F  6  237 ? -3.332  -97.315  81.254  1.00 122.17 ? 233 GLN   F O   1 
ATOM   11085 C  CB  . GLN   F  6  237 ? -4.782  -99.514  79.407  1.00 127.70 ? 233 GLN   F CB  1 
ATOM   11086 C  CG  . GLN   F  6  237 ? -5.909  -98.532  79.707  1.00 133.43 ? 233 GLN   F CG  1 
ATOM   11087 C  CD  . GLN   F  6  237 ? -5.934  -97.378  78.733  1.00 134.79 ? 233 GLN   F CD  1 
ATOM   11088 O  OE1 . GLN   F  6  237 ? -5.864  -97.568  77.521  1.00 141.35 ? 233 GLN   F OE1 1 
ATOM   11089 N  NE2 . GLN   F  6  237 ? -6.030  -96.164  79.254  1.00 137.89 ? 233 GLN   F NE2 1 
ATOM   11090 N  N   . GLU   F  6  238 ? -2.431  -99.375  81.662  1.00 127.01 ? 234 GLU   F N   1 
ATOM   11091 C  CA  . GLU   F  6  238 ? -1.934  -99.128  83.044  1.00 131.65 ? 234 GLU   F CA  1 
ATOM   11092 C  C   . GLU   F  6  238 ? -0.811  -98.083  83.013  1.00 126.71 ? 234 GLU   F C   1 
ATOM   11093 O  O   . GLU   F  6  238 ? -0.793  -97.216  83.910  1.00 129.77 ? 234 GLU   F O   1 
ATOM   11094 C  CB  . GLU   F  6  238 ? -1.440  -100.436 83.667  1.00 133.74 ? 234 GLU   F CB  1 
ATOM   11095 C  CG  . GLU   F  6  238 ? -0.951  -100.292 85.097  1.00 138.31 ? 234 GLU   F CG  1 
ATOM   11096 C  CD  . GLU   F  6  238 ? -0.237  -101.520 85.634  1.00 136.29 ? 234 GLU   F CD  1 
ATOM   11097 O  OE1 . GLU   F  6  238 ? 0.753   -101.349 86.371  1.00 139.76 ? 234 GLU   F OE1 1 
ATOM   11098 O  OE2 . GLU   F  6  238 ? -0.671  -102.643 85.311  1.00 136.45 ? 234 GLU   F OE2 1 
ATOM   11099 N  N   . ALA   F  6  239 ? 0.092   -98.179  82.030  1.00 122.78 ? 235 ALA   F N   1 
ATOM   11100 C  CA  . ALA   F  6  239 ? 1.249   -97.270  81.835  1.00 121.76 ? 235 ALA   F CA  1 
ATOM   11101 C  C   . ALA   F  6  239 ? 0.770   -95.894  81.347  1.00 119.99 ? 235 ALA   F C   1 
ATOM   11102 O  O   . ALA   F  6  239 ? 1.349   -94.882  81.792  1.00 118.09 ? 235 ALA   F O   1 
ATOM   11103 C  CB  . ALA   F  6  239 ? 2.236   -97.885  80.871  1.00 119.58 ? 235 ALA   F CB  1 
ATOM   11104 N  N   . ILE   F  6  240 ? -0.236  -95.859  80.463  1.00 121.43 ? 236 ILE   F N   1 
ATOM   11105 C  CA  . ILE   F  6  240 ? -0.867  -94.604  79.949  1.00 123.97 ? 236 ILE   F CA  1 
ATOM   11106 C  C   . ILE   F  6  240 ? -1.507  -93.860  81.126  1.00 131.88 ? 236 ILE   F C   1 
ATOM   11107 O  O   . ILE   F  6  240 ? -1.288  -92.638  81.238  1.00 138.48 ? 236 ILE   F O   1 
ATOM   11108 C  CB  . ILE   F  6  240 ? -1.898  -94.892  78.836  1.00 124.16 ? 236 ILE   F CB  1 
ATOM   11109 C  CG1 . ILE   F  6  240 ? -1.221  -95.348  77.540  1.00 124.07 ? 236 ILE   F CG1 1 
ATOM   11110 C  CG2 . ILE   F  6  240 ? -2.793  -93.682  78.601  1.00 123.81 ? 236 ILE   F CG2 1 
ATOM   11111 C  CD1 . ILE   F  6  240 ? -2.172  -95.909  76.504  1.00 126.31 ? 236 ILE   F CD1 1 
ATOM   11112 N  N   . ASP   F  6  241 ? -2.282  -94.571  81.952  1.00 133.87 ? 237 ASP   F N   1 
ATOM   11113 C  CA  . ASP   F  6  241 ? -3.020  -94.005  83.114  1.00 139.43 ? 237 ASP   F CA  1 
ATOM   11114 C  C   . ASP   F  6  241 ? -2.021  -93.371  84.088  1.00 141.73 ? 237 ASP   F C   1 
ATOM   11115 O  O   . ASP   F  6  241 ? -2.275  -92.228  84.525  1.00 147.39 ? 237 ASP   F O   1 
ATOM   11116 C  CB  . ASP   F  6  241 ? -3.877  -95.068  83.807  1.00 142.60 ? 237 ASP   F CB  1 
ATOM   11117 C  CG  . ASP   F  6  241 ? -5.038  -95.576  82.967  1.00 143.57 ? 237 ASP   F CG  1 
ATOM   11118 O  OD1 . ASP   F  6  241 ? -5.531  -94.807  82.116  1.00 151.50 ? 237 ASP   F OD1 1 
ATOM   11119 O  OD2 . ASP   F  6  241 ? -5.434  -96.743  83.163  1.00 141.95 ? 237 ASP   F OD2 1 
ATOM   11120 N  N   . PHE   F  6  242 ? -0.935  -94.083  84.411  1.00 137.19 ? 238 PHE   F N   1 
ATOM   11121 C  CA  . PHE   F  6  242 ? 0.163   -93.603  85.291  1.00 138.67 ? 238 PHE   F CA  1 
ATOM   11122 C  C   . PHE   F  6  242 ? 0.705   -92.270  84.759  1.00 140.12 ? 238 PHE   F C   1 
ATOM   11123 O  O   . PHE   F  6  242 ? 0.912   -91.351  85.572  1.00 144.57 ? 238 PHE   F O   1 
ATOM   11124 C  CB  . PHE   F  6  242 ? 1.283   -94.642  85.398  1.00 132.86 ? 238 PHE   F CB  1 
ATOM   11125 C  CG  . PHE   F  6  242 ? 2.472   -94.190  86.208  1.00 130.67 ? 238 PHE   F CG  1 
ATOM   11126 C  CD1 . PHE   F  6  242 ? 2.498   -94.354  87.584  1.00 133.38 ? 238 PHE   F CD1 1 
ATOM   11127 C  CD2 . PHE   F  6  242 ? 3.560   -93.587  85.595  1.00 127.26 ? 238 PHE   F CD2 1 
ATOM   11128 C  CE1 . PHE   F  6  242 ? 3.590   -93.931  88.328  1.00 135.14 ? 238 PHE   F CE1 1 
ATOM   11129 C  CE2 . PHE   F  6  242 ? 4.651   -93.165  86.340  1.00 130.22 ? 238 PHE   F CE2 1 
ATOM   11130 C  CZ  . PHE   F  6  242 ? 4.663   -93.337  87.705  1.00 134.09 ? 238 PHE   F CZ  1 
ATOM   11131 N  N   . ALA   F  6  243 ? 0.923   -92.175  83.442  1.00 142.39 ? 239 ALA   F N   1 
ATOM   11132 C  CA  . ALA   F  6  243 ? 1.470   -90.983  82.750  1.00 142.35 ? 239 ALA   F CA  1 
ATOM   11133 C  C   . ALA   F  6  243 ? 0.467   -89.824  82.811  1.00 145.77 ? 239 ALA   F C   1 
ATOM   11134 O  O   . ALA   F  6  243 ? 0.904   -88.689  83.087  1.00 147.47 ? 239 ALA   F O   1 
ATOM   11135 C  CB  . ALA   F  6  243 ? 1.824   -91.322  81.322  1.00 142.55 ? 239 ALA   F CB  1 
ATOM   11136 N  N   . GLN   F  6  244 ? -0.817  -90.101  82.554  1.00 147.48 ? 240 GLN   F N   1 
ATOM   11137 C  CA  . GLN   F  6  244 ? -1.921  -89.098  82.562  1.00 150.45 ? 240 GLN   F CA  1 
ATOM   11138 C  C   . GLN   F  6  244 ? -2.039  -88.451  83.948  1.00 150.85 ? 240 GLN   F C   1 
ATOM   11139 O  O   . GLN   F  6  244 ? -2.321  -87.239  84.006  1.00 152.33 ? 240 GLN   F O   1 
ATOM   11140 C  CB  . GLN   F  6  244 ? -3.255  -89.741  82.171  1.00 151.74 ? 240 GLN   F CB  1 
ATOM   11141 C  CG  . GLN   F  6  244 ? -3.482  -89.835  80.666  1.00 155.63 ? 240 GLN   F CG  1 
ATOM   11142 C  CD  . GLN   F  6  244 ? -3.628  -88.514  79.943  1.00 156.26 ? 240 GLN   F CD  1 
ATOM   11143 O  OE1 . GLN   F  6  244 ? -3.548  -88.459  78.719  1.00 160.30 ? 240 GLN   F OE1 1 
ATOM   11144 N  NE2 . GLN   F  6  244 ? -3.853  -87.431  80.675  1.00 161.02 ? 240 GLN   F NE2 1 
ATOM   11145 N  N   . LYS   F  6  245 ? -1.843  -89.230  85.017  1.00 147.83 ? 241 LYS   F N   1 
ATOM   11146 C  CA  . LYS   F  6  245 ? -1.973  -88.770  86.426  1.00 150.97 ? 241 LYS   F CA  1 
ATOM   11147 C  C   . LYS   F  6  245 ? -0.864  -87.761  86.758  1.00 153.78 ? 241 LYS   F C   1 
ATOM   11148 O  O   . LYS   F  6  245 ? -1.125  -86.857  87.576  1.00 155.66 ? 241 LYS   F O   1 
ATOM   11149 C  CB  . LYS   F  6  245 ? -1.925  -89.960  87.389  1.00 150.58 ? 241 LYS   F CB  1 
ATOM   11150 C  CG  . LYS   F  6  245 ? -2.474  -89.680  88.781  1.00 153.92 ? 241 LYS   F CG  1 
ATOM   11151 C  CD  . LYS   F  6  245 ? -2.553  -90.908  89.662  1.00 155.92 ? 241 LYS   F CD  1 
ATOM   11152 C  CE  . LYS   F  6  245 ? -3.200  -90.634  91.004  1.00 160.94 ? 241 LYS   F CE  1 
ATOM   11153 N  NZ  . LYS   F  6  245 ? -2.277  -90.913  92.129  1.00 163.07 ? 241 LYS   F NZ  1 
ATOM   11154 N  N   . GLU   F  6  246 ? 0.315   -87.904  86.141  1.00 153.21 ? 242 GLU   F N   1 
ATOM   11155 C  CA  . GLU   F  6  246 ? 1.548   -87.139  86.481  1.00 156.25 ? 242 GLU   F CA  1 
ATOM   11156 C  C   . GLU   F  6  246 ? 1.561   -85.767  85.790  1.00 160.52 ? 242 GLU   F C   1 
ATOM   11157 O  O   . GLU   F  6  246 ? 2.149   -84.835  86.376  1.00 160.35 ? 242 GLU   F O   1 
ATOM   11158 C  CB  . GLU   F  6  246 ? 2.794   -87.945  86.107  1.00 153.54 ? 242 GLU   F CB  1 
ATOM   11159 C  CG  . GLU   F  6  246 ? 2.909   -89.256  86.863  1.00 152.37 ? 242 GLU   F CG  1 
ATOM   11160 C  CD  . GLU   F  6  246 ? 3.263   -89.118  88.333  1.00 154.79 ? 242 GLU   F CD  1 
ATOM   11161 O  OE1 . GLU   F  6  246 ? 2.433   -89.508  89.177  1.00 157.93 ? 242 GLU   F OE1 1 
ATOM   11162 O  OE2 . GLU   F  6  246 ? 4.370   -88.628  88.628  1.00 161.23 ? 242 GLU   F OE2 1 
ATOM   11163 N  N   . ILE   F  6  247 ? 0.960   -85.635  84.600  1.00 160.27 ? 243 ILE   F N   1 
ATOM   11164 C  CA  . ILE   F  6  247 ? 0.913   -84.341  83.848  1.00 162.51 ? 243 ILE   F CA  1 
ATOM   11165 C  C   . ILE   F  6  247 ? -0.078  -83.392  84.541  1.00 170.56 ? 243 ILE   F C   1 
ATOM   11166 O  O   . ILE   F  6  247 ? 0.107   -82.165  84.412  1.00 179.45 ? 243 ILE   F O   1 
ATOM   11167 C  CB  . ILE   F  6  247 ? 0.595   -84.531  82.345  1.00 156.78 ? 243 ILE   F CB  1 
ATOM   11168 C  CG1 . ILE   F  6  247 ? -0.839  -85.000  82.081  1.00 159.75 ? 243 ILE   F CG1 1 
ATOM   11169 C  CG2 . ILE   F  6  247 ? 1.612   -85.454  81.690  1.00 149.06 ? 243 ILE   F CG2 1 
ATOM   11170 C  CD1 . ILE   F  6  247 ? -1.358  -84.630  80.708  1.00 159.59 ? 243 ILE   F CD1 1 
ATOM   11171 N  N   . ASN   F  6  248 ? -1.080  -83.934  85.248  1.00 168.17 ? 244 ASN   F N   1 
ATOM   11172 C  CA  . ASN   F  6  248 ? -2.084  -83.160  86.032  1.00 169.19 ? 244 ASN   F CA  1 
ATOM   11173 C  C   . ASN   F  6  248 ? -1.744  -83.256  87.524  1.00 168.36 ? 244 ASN   F C   1 
ATOM   11174 O  O   . ASN   F  6  248 ? -0.595  -83.472  87.911  1.00 165.95 ? 244 ASN   F O   1 
ATOM   11175 C  CB  . ASN   F  6  248 ? -3.515  -83.644  85.775  1.00 169.01 ? 244 ASN   F CB  1 
ATOM   11176 C  CG  . ASN   F  6  248 ? -3.836  -83.814  84.305  1.00 164.57 ? 244 ASN   F CG  1 
ATOM   11177 O  OD1 . ASN   F  6  248 ? -3.518  -82.949  83.492  1.00 161.23 ? 244 ASN   F OD1 1 
ATOM   11178 N  ND2 . ASN   F  6  248 ? -4.472  -84.921  83.955  1.00 160.89 ? 244 ASN   F ND2 1 
ATOM   11179 N  N   . GLY   G  7  11  ? 37.736  -73.043  44.680  1.00 121.69 ? 2   GLY   G N   1 
ATOM   11180 C  CA  . GLY   G  7  11  ? 38.938  -73.699  45.272  1.00 121.66 ? 2   GLY   G CA  1 
ATOM   11181 C  C   . GLY   G  7  11  ? 38.638  -75.113  45.743  1.00 122.60 ? 2   GLY   G C   1 
ATOM   11182 O  O   . GLY   G  7  11  ? 38.643  -75.340  46.969  1.00 123.61 ? 2   GLY   G O   1 
ATOM   11183 N  N   . TYR   G  7  12  ? 38.393  -76.036  44.805  1.00 124.01 ? 3   TYR   G N   1 
ATOM   11184 C  CA  . TYR   G  7  12  ? 38.028  -77.453  45.081  1.00 127.75 ? 3   TYR   G CA  1 
ATOM   11185 C  C   . TYR   G  7  12  ? 39.258  -78.259  45.521  1.00 118.10 ? 3   TYR   G C   1 
ATOM   11186 O  O   . TYR   G  7  12  ? 39.065  -79.383  46.012  1.00 116.12 ? 3   TYR   G O   1 
ATOM   11187 C  CB  . TYR   G  7  12  ? 37.367  -78.109  43.864  1.00 131.59 ? 3   TYR   G CB  1 
ATOM   11188 C  CG  . TYR   G  7  12  ? 35.937  -77.700  43.606  1.00 144.63 ? 3   TYR   G CG  1 
ATOM   11189 C  CD1 . TYR   G  7  12  ? 35.018  -77.593  44.641  1.00 150.12 ? 3   TYR   G CD1 1 
ATOM   11190 C  CD2 . TYR   G  7  12  ? 35.488  -77.445  42.318  1.00 149.66 ? 3   TYR   G CD2 1 
ATOM   11191 C  CE1 . TYR   G  7  12  ? 33.703  -77.220  44.408  1.00 158.65 ? 3   TYR   G CE1 1 
ATOM   11192 C  CE2 . TYR   G  7  12  ? 34.175  -77.074  42.068  1.00 156.03 ? 3   TYR   G CE2 1 
ATOM   11193 C  CZ  . TYR   G  7  12  ? 33.279  -76.961  43.117  1.00 157.67 ? 3   TYR   G CZ  1 
ATOM   11194 O  OH  . TYR   G  7  12  ? 31.985  -76.596  42.880  1.00 163.60 ? 3   TYR   G OH  1 
ATOM   11195 N  N   . ASP   G  7  13  ? 40.469  -77.711  45.368  1.00 117.25 ? 4   ASP   G N   1 
ATOM   11196 C  CA  . ASP   G  7  13  ? 41.738  -78.345  45.825  1.00 114.64 ? 4   ASP   G CA  1 
ATOM   11197 C  C   . ASP   G  7  13  ? 41.771  -78.440  47.358  1.00 118.10 ? 4   ASP   G C   1 
ATOM   11198 O  O   . ASP   G  7  13  ? 42.694  -79.106  47.881  1.00 115.37 ? 4   ASP   G O   1 
ATOM   11199 C  CB  . ASP   G  7  13  ? 42.967  -77.584  45.321  1.00 116.42 ? 4   ASP   G CB  1 
ATOM   11200 C  CG  . ASP   G  7  13  ? 43.035  -76.144  45.797  1.00 117.90 ? 4   ASP   G CG  1 
ATOM   11201 O  OD1 . ASP   G  7  13  ? 41.981  -75.477  45.795  1.00 121.05 ? 4   ASP   G OD1 1 
ATOM   11202 O  OD2 . ASP   G  7  13  ? 44.138  -75.705  46.172  1.00 122.49 ? 4   ASP   G OD2 1 
ATOM   11203 N  N   . ARG   G  7  14  ? 40.827  -77.787  48.050  1.00 113.73 ? 5   ARG   G N   1 
ATOM   11204 C  CA  . ARG   G  7  14  ? 40.688  -77.832  49.532  1.00 112.81 ? 5   ARG   G CA  1 
ATOM   11205 C  C   . ARG   G  7  14  ? 39.618  -78.848  49.953  1.00 107.84 ? 5   ARG   G C   1 
ATOM   11206 O  O   . ARG   G  7  14  ? 39.498  -79.081  51.170  1.00 108.38 ? 5   ARG   G O   1 
ATOM   11207 C  CB  . ARG   G  7  14  ? 40.329  -76.448  50.079  1.00 115.65 ? 5   ARG   G CB  1 
ATOM   11208 C  CG  . ARG   G  7  14  ? 41.227  -75.330  49.571  1.00 119.43 ? 5   ARG   G CG  1 
ATOM   11209 C  CD  . ARG   G  7  14  ? 41.478  -74.258  50.614  1.00 121.55 ? 5   ARG   G CD  1 
ATOM   11210 N  NE  . ARG   G  7  14  ? 42.594  -73.400  50.240  1.00 124.67 ? 5   ARG   G NE  1 
ATOM   11211 C  CZ  . ARG   G  7  14  ? 43.279  -72.622  51.076  1.00 128.87 ? 5   ARG   G CZ  1 
ATOM   11212 N  NH1 . ARG   G  7  14  ? 42.976  -72.578  52.364  1.00 131.25 ? 5   ARG   G NH1 1 
ATOM   11213 N  NH2 . ARG   G  7  14  ? 44.278  -71.889  50.616  1.00 134.99 ? 5   ARG   G NH2 1 
ATOM   11214 N  N   . HIS   G  7  15  ? 38.873  -79.425  49.002  1.00 104.71 ? 6   HIS   G N   1 
ATOM   11215 C  CA  . HIS   G  7  15  ? 37.741  -80.360  49.261  1.00 101.52 ? 6   HIS   G CA  1 
ATOM   11216 C  C   . HIS   G  7  15  ? 38.191  -81.821  49.140  1.00 95.39  ? 6   HIS   G C   1 
ATOM   11217 O  O   . HIS   G  7  15  ? 37.672  -82.645  49.909  1.00 91.35  ? 6   HIS   G O   1 
ATOM   11218 C  CB  . HIS   G  7  15  ? 36.566  -80.069  48.321  1.00 106.01 ? 6   HIS   G CB  1 
ATOM   11219 C  CG  . HIS   G  7  15  ? 35.946  -78.732  48.536  1.00 110.28 ? 6   HIS   G CG  1 
ATOM   11220 N  ND1 . HIS   G  7  15  ? 34.581  -78.541  48.499  1.00 114.17 ? 6   HIS   G ND1 1 
ATOM   11221 C  CD2 . HIS   G  7  15  ? 36.494  -77.526  48.802  1.00 113.52 ? 6   HIS   G CD2 1 
ATOM   11222 C  CE1 . HIS   G  7  15  ? 34.317  -77.270  48.722  1.00 115.83 ? 6   HIS   G CE1 1 
ATOM   11223 N  NE2 . HIS   G  7  15  ? 35.471  -76.627  48.914  1.00 116.46 ? 6   HIS   G NE2 1 
ATOM   11224 N  N   . ILE   G  7  16  ? 39.098  -82.128  48.207  1.00 92.07  ? 7   ILE   G N   1 
ATOM   11225 C  CA  . ILE   G  7  16  ? 39.628  -83.506  47.973  1.00 92.34  ? 7   ILE   G CA  1 
ATOM   11226 C  C   . ILE   G  7  16  ? 41.151  -83.498  48.134  1.00 94.99  ? 7   ILE   G C   1 
ATOM   11227 O  O   . ILE   G  7  16  ? 41.743  -82.397  48.192  1.00 95.37  ? 7   ILE   G O   1 
ATOM   11228 C  CB  . ILE   G  7  16  ? 39.193  -84.047  46.596  1.00 92.19  ? 7   ILE   G CB  1 
ATOM   11229 C  CG1 . ILE   G  7  16  ? 39.569  -83.099  45.455  1.00 90.94  ? 7   ILE   G CG1 1 
ATOM   11230 C  CG2 . ILE   G  7  16  ? 37.705  -84.360  46.600  1.00 95.19  ? 7   ILE   G CG2 1 
ATOM   11231 C  CD1 . ILE   G  7  16  ? 39.597  -83.758  44.097  1.00 89.67  ? 7   ILE   G CD1 1 
ATOM   11232 N  N   . THR   G  7  17  ? 41.752  -84.690  48.206  1.00 93.75  ? 8   THR   G N   1 
ATOM   11233 C  CA  . THR   G  7  17  ? 43.201  -84.895  48.464  1.00 93.59  ? 8   THR   G CA  1 
ATOM   11234 C  C   . THR   G  7  17  ? 43.968  -84.779  47.141  1.00 92.93  ? 8   THR   G C   1 
ATOM   11235 O  O   . THR   G  7  17  ? 44.502  -85.807  46.670  1.00 88.40  ? 8   THR   G O   1 
ATOM   11236 C  CB  . THR   G  7  17  ? 43.442  -86.215  49.209  1.00 93.67  ? 8   THR   G CB  1 
ATOM   11237 O  OG1 . THR   G  7  17  ? 42.811  -87.274  48.489  1.00 97.31  ? 8   THR   G OG1 1 
ATOM   11238 C  CG2 . THR   G  7  17  ? 42.921  -86.177  50.629  1.00 95.83  ? 8   THR   G CG2 1 
ATOM   11239 N  N   . ILE   G  7  18  ? 43.991  -83.568  46.570  1.00 90.47  ? 9   ILE   G N   1 
ATOM   11240 C  CA  . ILE   G  7  18  ? 44.911  -83.144  45.471  1.00 90.85  ? 9   ILE   G CA  1 
ATOM   11241 C  C   . ILE   G  7  18  ? 45.755  -81.969  45.978  1.00 92.77  ? 9   ILE   G C   1 
ATOM   11242 O  O   . ILE   G  7  18  ? 45.339  -81.313  46.960  1.00 92.96  ? 9   ILE   G O   1 
ATOM   11243 C  CB  . ILE   G  7  18  ? 44.146  -82.775  44.182  1.00 90.57  ? 9   ILE   G CB  1 
ATOM   11244 C  CG1 . ILE   G  7  18  ? 43.179  -81.609  44.394  1.00 90.14  ? 9   ILE   G CG1 1 
ATOM   11245 C  CG2 . ILE   G  7  18  ? 43.437  -83.990  43.610  1.00 92.04  ? 9   ILE   G CG2 1 
ATOM   11246 C  CD1 . ILE   G  7  18  ? 42.749  -80.938  43.113  1.00 91.79  ? 9   ILE   G CD1 1 
ATOM   11247 N  N   . PHE   G  7  19  ? 46.885  -81.707  45.317  1.00 92.09  ? 10  PHE   G N   1 
ATOM   11248 C  CA  . PHE   G  7  19  ? 47.873  -80.672  45.714  1.00 95.44  ? 10  PHE   G CA  1 
ATOM   11249 C  C   . PHE   G  7  19  ? 47.291  -79.274  45.490  1.00 96.38  ? 10  PHE   G C   1 
ATOM   11250 O  O   . PHE   G  7  19  ? 46.691  -79.017  44.427  1.00 97.20  ? 10  PHE   G O   1 
ATOM   11251 C  CB  . PHE   G  7  19  ? 49.181  -80.829  44.934  1.00 94.27  ? 10  PHE   G CB  1 
ATOM   11252 C  CG  . PHE   G  7  19  ? 49.987  -82.044  45.306  1.00 94.37  ? 10  PHE   G CG  1 
ATOM   11253 C  CD1 . PHE   G  7  19  ? 50.499  -82.185  46.585  1.00 94.73  ? 10  PHE   G CD1 1 
ATOM   11254 C  CD2 . PHE   G  7  19  ? 50.240  -83.041  44.377  1.00 94.38  ? 10  PHE   G CD2 1 
ATOM   11255 C  CE1 . PHE   G  7  19  ? 51.243  -83.301  46.930  1.00 95.78  ? 10  PHE   G CE1 1 
ATOM   11256 C  CE2 . PHE   G  7  19  ? 50.984  -84.157  44.724  1.00 95.46  ? 10  PHE   G CE2 1 
ATOM   11257 C  CZ  . PHE   G  7  19  ? 51.485  -84.285  45.999  1.00 95.87  ? 10  PHE   G CZ  1 
ATOM   11258 N  N   . SER   G  7  20  ? 47.475  -78.393  46.474  1.00 97.95  ? 11  SER   G N   1 
ATOM   11259 C  CA  . SER   G  7  20  ? 47.287  -76.927  46.337  1.00 100.28 ? 11  SER   G CA  1 
ATOM   11260 C  C   . SER   G  7  20  ? 48.490  -76.352  45.593  1.00 99.26  ? 11  SER   G C   1 
ATOM   11261 O  O   . SER   G  7  20  ? 49.528  -77.006  45.505  1.00 100.05 ? 11  SER   G O   1 
ATOM   11262 C  CB  . SER   G  7  20  ? 47.097  -76.277  47.683  1.00 102.69 ? 11  SER   G CB  1 
ATOM   11263 O  OG  . SER   G  7  20  ? 48.324  -76.216  48.397  1.00 103.74 ? 11  SER   G OG  1 
ATOM   11264 N  N   . PRO   G  7  21  ? 48.388  -75.131  45.019  1.00 96.47  ? 12  PRO   G N   1 
ATOM   11265 C  CA  . PRO   G  7  21  ? 49.521  -74.491  44.348  1.00 95.57  ? 12  PRO   G CA  1 
ATOM   11266 C  C   . PRO   G  7  21  ? 50.845  -74.466  45.131  1.00 96.35  ? 12  PRO   G C   1 
ATOM   11267 O  O   . PRO   G  7  21  ? 51.880  -74.467  44.488  1.00 99.13  ? 12  PRO   G O   1 
ATOM   11268 C  CB  . PRO   G  7  21  ? 49.018  -73.060  44.136  1.00 96.55  ? 12  PRO   G CB  1 
ATOM   11269 C  CG  . PRO   G  7  21  ? 47.524  -73.216  43.976  1.00 96.09  ? 12  PRO   G CG  1 
ATOM   11270 C  CD  . PRO   G  7  21  ? 47.155  -74.336  44.922  1.00 93.60  ? 12  PRO   G CD  1 
ATOM   11271 N  N   . GLU   G  7  22  ? 50.787  -74.460  46.470  1.00 99.33  ? 13  GLU   G N   1 
ATOM   11272 C  CA  . GLU   G  7  22  ? 51.980  -74.428  47.366  1.00 105.51 ? 13  GLU   G CA  1 
ATOM   11273 C  C   . GLU   G  7  22  ? 52.362  -75.856  47.789  1.00 104.49 ? 13  GLU   G C   1 
ATOM   11274 O  O   . GLU   G  7  22  ? 53.216  -75.989  48.686  1.00 107.24 ? 13  GLU   G O   1 
ATOM   11275 C  CB  . GLU   G  7  22  ? 51.758  -73.506  48.574  1.00 111.05 ? 13  GLU   G CB  1 
ATOM   11276 C  CG  . GLU   G  7  22  ? 50.402  -73.635  49.256  1.00 112.86 ? 13  GLU   G CG  1 
ATOM   11277 C  CD  . GLU   G  7  22  ? 49.271  -72.808  48.663  1.00 112.56 ? 13  GLU   G CD  1 
ATOM   11278 O  OE1 . GLU   G  7  22  ? 49.562  -71.843  47.927  1.00 109.00 ? 13  GLU   G OE1 1 
ATOM   11279 O  OE2 . GLU   G  7  22  ? 48.097  -73.132  48.944  1.00 108.53 ? 13  GLU   G OE2 1 
ATOM   11280 N  N   . GLY   G  7  23  ? 51.774  -76.877  47.152  1.00 102.65 ? 14  GLY   G N   1 
ATOM   11281 C  CA  . GLY   G  7  23  ? 52.149  -78.298  47.307  1.00 99.84  ? 14  GLY   G CA  1 
ATOM   11282 C  C   . GLY   G  7  23  ? 51.644  -78.897  48.609  1.00 97.29  ? 14  GLY   G C   1 
ATOM   11283 O  O   . GLY   G  7  23  ? 52.334  -79.782  49.144  1.00 99.64  ? 14  GLY   G O   1 
ATOM   11284 N  N   . ARG   G  7  24  ? 50.479  -78.449  49.090  1.00 96.42  ? 15  ARG   G N   1 
ATOM   11285 C  CA  . ARG   G  7  24  ? 49.873  -78.880  50.379  1.00 96.85  ? 15  ARG   G CA  1 
ATOM   11286 C  C   . ARG   G  7  24  ? 48.588  -79.674  50.113  1.00 91.18  ? 15  ARG   G C   1 
ATOM   11287 O  O   . ARG   G  7  24  ? 47.950  -79.445  49.065  1.00 87.16  ? 15  ARG   G O   1 
ATOM   11288 C  CB  . ARG   G  7  24  ? 49.572  -77.662  51.257  1.00 101.50 ? 15  ARG   G CB  1 
ATOM   11289 C  CG  . ARG   G  7  24  ? 50.799  -77.019  51.888  1.00 105.28 ? 15  ARG   G CG  1 
ATOM   11290 C  CD  . ARG   G  7  24  ? 50.514  -75.633  52.439  1.00 108.48 ? 15  ARG   G CD  1 
ATOM   11291 N  NE  . ARG   G  7  24  ? 49.504  -75.621  53.490  1.00 110.87 ? 15  ARG   G NE  1 
ATOM   11292 C  CZ  . ARG   G  7  24  ? 49.099  -74.536  54.150  1.00 114.51 ? 15  ARG   G CZ  1 
ATOM   11293 N  NH1 . ARG   G  7  24  ? 49.615  -73.347  53.877  1.00 115.95 ? 15  ARG   G NH1 1 
ATOM   11294 N  NH2 . ARG   G  7  24  ? 48.175  -74.645  55.090  1.00 117.23 ? 15  ARG   G NH2 1 
ATOM   11295 N  N   . LEU   G  7  25  ? 48.230  -80.564  51.043  1.00 89.71  ? 16  LEU   G N   1 
ATOM   11296 C  CA  . LEU   G  7  25  ? 46.958  -81.338  51.051  1.00 91.39  ? 16  LEU   G CA  1 
ATOM   11297 C  C   . LEU   G  7  25  ? 46.108  -80.855  52.228  1.00 93.86  ? 16  LEU   G C   1 
ATOM   11298 O  O   . LEU   G  7  25  ? 46.344  -81.330  53.355  1.00 95.52  ? 16  LEU   G O   1 
ATOM   11299 C  CB  . LEU   G  7  25  ? 47.265  -82.833  51.193  1.00 89.16  ? 16  LEU   G CB  1 
ATOM   11300 C  CG  . LEU   G  7  25  ? 48.094  -83.468  50.079  1.00 86.59  ? 16  LEU   G CG  1 
ATOM   11301 C  CD1 . LEU   G  7  25  ? 48.436  -84.905  50.432  1.00 86.50  ? 16  LEU   G CD1 1 
ATOM   11302 C  CD2 . LEU   G  7  25  ? 47.368  -83.411  48.746  1.00 87.67  ? 16  LEU   G CD2 1 
ATOM   11303 N  N   . TYR   G  7  26  ? 45.166  -79.942  51.984  1.00 92.60  ? 17  TYR   G N   1 
ATOM   11304 C  CA  . TYR   G  7  26  ? 44.376  -79.271  53.050  1.00 92.71  ? 17  TYR   G CA  1 
ATOM   11305 C  C   . TYR   G  7  26  ? 43.493  -80.287  53.779  1.00 91.58  ? 17  TYR   G C   1 
ATOM   11306 O  O   . TYR   G  7  26  ? 43.353  -80.172  55.013  1.00 94.08  ? 17  TYR   G O   1 
ATOM   11307 C  CB  . TYR   G  7  26  ? 43.570  -78.103  52.481  1.00 95.32  ? 17  TYR   G CB  1 
ATOM   11308 C  CG  . TYR   G  7  26  ? 44.406  -76.870  52.258  1.00 100.01 ? 17  TYR   G CG  1 
ATOM   11309 C  CD1 . TYR   G  7  26  ? 44.800  -76.071  53.320  1.00 100.52 ? 17  TYR   G CD1 1 
ATOM   11310 C  CD2 . TYR   G  7  26  ? 44.840  -76.522  50.989  1.00 104.58 ? 17  TYR   G CD2 1 
ATOM   11311 C  CE1 . TYR   G  7  26  ? 45.585  -74.945  53.125  1.00 101.74 ? 17  TYR   G CE1 1 
ATOM   11312 C  CE2 . TYR   G  7  26  ? 45.623  -75.399  50.776  1.00 103.67 ? 17  TYR   G CE2 1 
ATOM   11313 C  CZ  . TYR   G  7  26  ? 45.999  -74.609  51.847  1.00 101.94 ? 17  TYR   G CZ  1 
ATOM   11314 O  OH  . TYR   G  7  26  ? 46.772  -73.509  51.619  1.00 100.35 ? 17  TYR   G OH  1 
ATOM   11315 N  N   . GLN   G  7  27  ? 42.930  -81.256  53.055  1.00 87.76  ? 18  GLN   G N   1 
ATOM   11316 C  CA  . GLN   G  7  27  ? 42.036  -82.283  53.647  1.00 82.84  ? 18  GLN   G CA  1 
ATOM   11317 C  C   . GLN   G  7  27  ? 42.814  -83.091  54.690  1.00 83.09  ? 18  GLN   G C   1 
ATOM   11318 O  O   . GLN   G  7  27  ? 42.212  -83.425  55.728  1.00 83.60  ? 18  GLN   G O   1 
ATOM   11319 C  CB  . GLN   G  7  27  ? 41.435  -83.159  52.553  1.00 81.67  ? 18  GLN   G CB  1 
ATOM   11320 C  CG  . GLN   G  7  27  ? 40.253  -82.505  51.858  1.00 81.15  ? 18  GLN   G CG  1 
ATOM   11321 C  CD  . GLN   G  7  27  ? 39.101  -82.301  52.811  1.00 81.18  ? 18  GLN   G CD  1 
ATOM   11322 O  OE1 . GLN   G  7  27  ? 38.557  -83.243  53.374  1.00 84.16  ? 18  GLN   G OE1 1 
ATOM   11323 N  NE2 . GLN   G  7  27  ? 38.715  -81.058  53.014  1.00 80.01  ? 18  GLN   G NE2 1 
ATOM   11324 N  N   . VAL   G  7  28  ? 44.099  -83.364  54.438  1.00 84.71  ? 19  VAL   G N   1 
ATOM   11325 C  CA  . VAL   G  7  28  ? 45.010  -84.053  55.403  1.00 86.66  ? 19  VAL   G CA  1 
ATOM   11326 C  C   . VAL   G  7  28  ? 45.213  -83.133  56.613  1.00 87.85  ? 19  VAL   G C   1 
ATOM   11327 O  O   . VAL   G  7  28  ? 45.116  -83.627  57.753  1.00 82.87  ? 19  VAL   G O   1 
ATOM   11328 C  CB  . VAL   G  7  28  ? 46.355  -84.445  54.758  1.00 88.65  ? 19  VAL   G CB  1 
ATOM   11329 C  CG1 . VAL   G  7  28  ? 47.316  -85.055  55.771  1.00 88.68  ? 19  VAL   G CG1 1 
ATOM   11330 C  CG2 . VAL   G  7  28  ? 46.156  -85.390  53.582  1.00 88.40  ? 19  VAL   G CG2 1 
ATOM   11331 N  N   . GLU   G  7  29  ? 45.471  -81.846  56.366  1.00 86.75  ? 20  GLU   G N   1 
ATOM   11332 C  CA  . GLU   G  7  29  ? 45.718  -80.820  57.416  1.00 86.24  ? 20  GLU   G CA  1 
ATOM   11333 C  C   . GLU   G  7  29  ? 44.478  -80.658  58.298  1.00 85.86  ? 20  GLU   G C   1 
ATOM   11334 O  O   . GLU   G  7  29  ? 44.650  -80.489  59.517  1.00 89.36  ? 20  GLU   G O   1 
ATOM   11335 C  CB  . GLU   G  7  29  ? 46.075  -79.472  56.795  1.00 87.19  ? 20  GLU   G CB  1 
ATOM   11336 C  CG  . GLU   G  7  29  ? 47.417  -79.470  56.093  1.00 90.38  ? 20  GLU   G CG  1 
ATOM   11337 C  CD  . GLU   G  7  29  ? 47.885  -78.096  55.649  1.00 94.65  ? 20  GLU   G CD  1 
ATOM   11338 O  OE1 . GLU   G  7  29  ? 48.888  -78.032  54.914  1.00 99.60  ? 20  GLU   G OE1 1 
ATOM   11339 O  OE2 . GLU   G  7  29  ? 47.248  -77.092  56.040  1.00 99.80  ? 20  GLU   G OE2 1 
ATOM   11340 N  N   . TYR   G  7  30  ? 43.283  -80.685  57.705  1.00 84.43  ? 21  TYR   G N   1 
ATOM   11341 C  CA  . TYR   G  7  30  ? 41.994  -80.499  58.423  1.00 87.83  ? 21  TYR   G CA  1 
ATOM   11342 C  C   . TYR   G  7  30  ? 41.657  -81.763  59.218  1.00 87.29  ? 21  TYR   G C   1 
ATOM   11343 O  O   . TYR   G  7  30  ? 41.061  -81.636  60.308  1.00 88.69  ? 21  TYR   G O   1 
ATOM   11344 C  CB  . TYR   G  7  30  ? 40.869  -80.131  57.454  1.00 90.58  ? 21  TYR   G CB  1 
ATOM   11345 C  CG  . TYR   G  7  30  ? 41.077  -78.860  56.667  1.00 94.95  ? 21  TYR   G CG  1 
ATOM   11346 C  CD1 . TYR   G  7  30  ? 42.007  -77.902  57.053  1.00 97.20  ? 21  TYR   G CD1 1 
ATOM   11347 C  CD2 . TYR   G  7  30  ? 40.316  -78.599  55.539  1.00 96.64  ? 21  TYR   G CD2 1 
ATOM   11348 C  CE1 . TYR   G  7  30  ? 42.188  -76.734  56.328  1.00 99.88  ? 21  TYR   G CE1 1 
ATOM   11349 C  CE2 . TYR   G  7  30  ? 40.482  -77.435  54.806  1.00 99.34  ? 21  TYR   G CE2 1 
ATOM   11350 C  CZ  . TYR   G  7  30  ? 41.421  -76.497  55.201  1.00 101.82 ? 21  TYR   G CZ  1 
ATOM   11351 O  OH  . TYR   G  7  30  ? 41.586  -75.349  54.480  1.00 104.55 ? 21  TYR   G OH  1 
ATOM   11352 N  N   . ALA   G  7  31  ? 42.024  -82.939  58.698  1.00 86.24  ? 22  ALA   G N   1 
ATOM   11353 C  CA  . ALA   G  7  31  ? 41.878  -84.237  59.396  1.00 87.15  ? 22  ALA   G CA  1 
ATOM   11354 C  C   . ALA   G  7  31  ? 42.716  -84.216  60.681  1.00 85.70  ? 22  ALA   G C   1 
ATOM   11355 O  O   . ALA   G  7  31  ? 42.260  -84.788  61.690  1.00 87.62  ? 22  ALA   G O   1 
ATOM   11356 C  CB  . ALA   G  7  31  ? 42.269  -85.375  58.483  1.00 88.32  ? 22  ALA   G CB  1 
ATOM   11357 N  N   . PHE   G  7  32  ? 43.888  -83.572  60.650  1.00 83.46  ? 23  PHE   G N   1 
ATOM   11358 C  CA  . PHE   G  7  32  ? 44.766  -83.383  61.834  1.00 86.42  ? 23  PHE   G CA  1 
ATOM   11359 C  C   . PHE   G  7  32  ? 44.020  -82.576  62.901  1.00 90.85  ? 23  PHE   G C   1 
ATOM   11360 O  O   . PHE   G  7  32  ? 44.183  -82.887  64.089  1.00 93.99  ? 23  PHE   G O   1 
ATOM   11361 C  CB  . PHE   G  7  32  ? 46.082  -82.692  61.467  1.00 85.97  ? 23  PHE   G CB  1 
ATOM   11362 C  CG  . PHE   G  7  32  ? 47.225  -83.628  61.176  1.00 85.72  ? 23  PHE   G CG  1 
ATOM   11363 C  CD1 . PHE   G  7  32  ? 47.959  -84.195  62.208  1.00 85.84  ? 23  PHE   G CD1 1 
ATOM   11364 C  CD2 . PHE   G  7  32  ? 47.574  -83.933  59.870  1.00 85.53  ? 23  PHE   G CD2 1 
ATOM   11365 C  CE1 . PHE   G  7  32  ? 49.016  -85.050  61.937  1.00 86.04  ? 23  PHE   G CE1 1 
ATOM   11366 C  CE2 . PHE   G  7  32  ? 48.632  -84.787  59.601  1.00 87.22  ? 23  PHE   G CE2 1 
ATOM   11367 C  CZ  . PHE   G  7  32  ? 49.351  -85.345  60.634  1.00 87.77  ? 23  PHE   G CZ  1 
ATOM   11368 N  N   . LYS   G  7  33  ? 43.240  -81.570  62.493  1.00 93.37  ? 24  LYS   G N   1 
ATOM   11369 C  CA  . LYS   G  7  33  ? 42.478  -80.698  63.429  1.00 97.01  ? 24  LYS   G CA  1 
ATOM   11370 C  C   . LYS   G  7  33  ? 41.304  -81.489  64.023  1.00 97.21  ? 24  LYS   G C   1 
ATOM   11371 O  O   . LYS   G  7  33  ? 40.979  -81.247  65.202  1.00 102.86 ? 24  LYS   G O   1 
ATOM   11372 C  CB  . LYS   G  7  33  ? 42.042  -79.393  62.749  1.00 101.39 ? 24  LYS   G CB  1 
ATOM   11373 C  CG  . LYS   G  7  33  ? 42.920  -78.192  63.085  1.00 104.79 ? 24  LYS   G CG  1 
ATOM   11374 C  CD  . LYS   G  7  33  ? 42.539  -76.912  62.371  1.00 109.85 ? 24  LYS   G CD  1 
ATOM   11375 C  CE  . LYS   G  7  33  ? 43.202  -76.768  61.016  1.00 109.67 ? 24  LYS   G CE  1 
ATOM   11376 N  NZ  . LYS   G  7  33  ? 42.754  -75.544  60.311  1.00 110.86 ? 24  LYS   G NZ  1 
ATOM   11377 N  N   . ALA   G  7  34  ? 40.714  -82.420  63.264  1.00 96.03  ? 25  ALA   G N   1 
ATOM   11378 C  CA  . ALA   G  7  34  ? 39.650  -83.335  63.747  1.00 92.69  ? 25  ALA   G CA  1 
ATOM   11379 C  C   . ALA   G  7  34  ? 40.185  -84.176  64.913  1.00 88.90  ? 25  ALA   G C   1 
ATOM   11380 O  O   . ALA   G  7  34  ? 39.381  -84.533  65.788  1.00 82.71  ? 25  ALA   G O   1 
ATOM   11381 C  CB  . ALA   G  7  34  ? 39.145  -84.207  62.624  1.00 93.42  ? 25  ALA   G CB  1 
ATOM   11382 N  N   . THR   G  7  35  ? 41.491  -84.471  64.909  1.00 90.75  ? 26  THR   G N   1 
ATOM   11383 C  CA  . THR   G  7  35  ? 42.225  -85.236  65.956  1.00 94.20  ? 26  THR   G CA  1 
ATOM   11384 C  C   . THR   G  7  35  ? 41.872  -84.728  67.361  1.00 97.52  ? 26  THR   G C   1 
ATOM   11385 O  O   . THR   G  7  35  ? 41.654  -85.576  68.257  1.00 100.79 ? 26  THR   G O   1 
ATOM   11386 C  CB  . THR   G  7  35  ? 43.741  -85.158  65.729  1.00 97.72  ? 26  THR   G CB  1 
ATOM   11387 O  OG1 . THR   G  7  35  ? 44.085  -86.160  64.770  1.00 96.35  ? 26  THR   G OG1 1 
ATOM   11388 C  CG2 . THR   G  7  35  ? 44.557  -85.339  66.991  1.00 99.20  ? 26  THR   G CG2 1 
ATOM   11389 N  N   . ASN   G  7  36  ? 41.847  -83.406  67.555  1.00 93.92  ? 27  ASN   G N   1 
ATOM   11390 C  CA  . ASN   G  7  36  ? 41.712  -82.775  68.894  1.00 92.10  ? 27  ASN   G CA  1 
ATOM   11391 C  C   . ASN   G  7  36  ? 40.233  -82.565  69.244  1.00 90.53  ? 27  ASN   G C   1 
ATOM   11392 O  O   . ASN   G  7  36  ? 39.974  -82.054  70.342  1.00 96.16  ? 27  ASN   G O   1 
ATOM   11393 C  CB  . ASN   G  7  36  ? 42.499  -81.466  68.967  1.00 93.11  ? 27  ASN   G CB  1 
ATOM   11394 C  CG  . ASN   G  7  36  ? 43.996  -81.677  68.871  1.00 94.75  ? 27  ASN   G CG  1 
ATOM   11395 O  OD1 . ASN   G  7  36  ? 44.525  -82.653  69.397  1.00 91.13  ? 27  ASN   G OD1 1 
ATOM   11396 N  ND2 . ASN   G  7  36  ? 44.689  -80.764  68.209  1.00 99.18  ? 27  ASN   G ND2 1 
ATOM   11397 N  N   . GLN   G  7  37  ? 39.303  -82.976  68.376  1.00 93.54  ? 28  GLN   G N   1 
ATOM   11398 C  CA  . GLN   G  7  37  ? 37.845  -82.700  68.518  1.00 102.05 ? 28  GLN   G CA  1 
ATOM   11399 C  C   . GLN   G  7  37  ? 37.325  -83.234  69.863  1.00 100.74 ? 28  GLN   G C   1 
ATOM   11400 O  O   . GLN   G  7  37  ? 36.373  -82.632  70.395  1.00 97.89  ? 28  GLN   G O   1 
ATOM   11401 C  CB  . GLN   G  7  37  ? 37.074  -83.292  67.332  1.00 110.75 ? 28  GLN   G CB  1 
ATOM   11402 C  CG  . GLN   G  7  37  ? 35.704  -82.665  67.101  1.00 121.89 ? 28  GLN   G CG  1 
ATOM   11403 C  CD  . GLN   G  7  37  ? 34.571  -83.500  67.649  1.00 127.06 ? 28  GLN   G CD  1 
ATOM   11404 O  OE1 . GLN   G  7  37  ? 34.406  -84.666  67.294  1.00 126.26 ? 28  GLN   G OE1 1 
ATOM   11405 N  NE2 . GLN   G  7  37  ? 33.762  -82.899  68.510  1.00 136.66 ? 28  GLN   G NE2 1 
ATOM   11406 N  N   . THR   G  7  38  ? 37.930  -84.301  70.401  1.00 99.04  ? 29  THR   G N   1 
ATOM   11407 C  CA  . THR   G  7  38  ? 37.507  -84.978  71.660  1.00 100.90 ? 29  THR   G CA  1 
ATOM   11408 C  C   . THR   G  7  38  ? 38.050  -84.252  72.898  1.00 97.06  ? 29  THR   G C   1 
ATOM   11409 O  O   . THR   G  7  38  ? 37.552  -84.544  74.003  1.00 92.51  ? 29  THR   G O   1 
ATOM   11410 C  CB  . THR   G  7  38  ? 37.966  -86.440  71.687  1.00 102.25 ? 29  THR   G CB  1 
ATOM   11411 O  OG1 . THR   G  7  38  ? 39.388  -86.471  71.549  1.00 103.95 ? 29  THR   G OG1 1 
ATOM   11412 C  CG2 . THR   G  7  38  ? 37.325  -87.267  70.595  1.00 104.60 ? 29  THR   G CG2 1 
ATOM   11413 N  N   . ASN   G  7  39  ? 39.039  -83.371  72.727  1.00 99.39  ? 30  ASN   G N   1 
ATOM   11414 C  CA  . ASN   G  7  39  ? 39.672  -82.583  73.821  1.00 103.22 ? 30  ASN   G CA  1 
ATOM   11415 C  C   . ASN   G  7  39  ? 40.221  -83.544  74.884  1.00 104.52 ? 30  ASN   G C   1 
ATOM   11416 O  O   . ASN   G  7  39  ? 40.001  -83.292  76.086  1.00 102.01 ? 30  ASN   G O   1 
ATOM   11417 C  CB  . ASN   G  7  39  ? 38.694  -81.565  74.418  1.00 107.37 ? 30  ASN   G CB  1 
ATOM   11418 C  CG  . ASN   G  7  39  ? 39.357  -80.579  75.357  1.00 109.10 ? 30  ASN   G CG  1 
ATOM   11419 O  OD1 . ASN   G  7  39  ? 38.924  -80.420  76.497  1.00 109.62 ? 30  ASN   G OD1 1 
ATOM   11420 N  ND2 . ASN   G  7  39  ? 40.409  -79.921  74.897  1.00 110.39 ? 30  ASN   G ND2 1 
ATOM   11421 N  N   . ILE   G  7  40  ? 40.903  -84.606  74.442  1.00 107.59 ? 31  ILE   G N   1 
ATOM   11422 C  CA  . ILE   G  7  40  ? 41.519  -85.659  75.304  1.00 112.05 ? 31  ILE   G CA  1 
ATOM   11423 C  C   . ILE   G  7  40  ? 43.019  -85.728  74.997  1.00 105.34 ? 31  ILE   G C   1 
ATOM   11424 O  O   . ILE   G  7  40  ? 43.372  -85.738  73.799  1.00 104.65 ? 31  ILE   G O   1 
ATOM   11425 C  CB  . ILE   G  7  40  ? 40.830  -87.021  75.073  1.00 114.09 ? 31  ILE   G CB  1 
ATOM   11426 C  CG1 . ILE   G  7  40  ? 39.400  -87.046  75.623  1.00 118.46 ? 31  ILE   G CG1 1 
ATOM   11427 C  CG2 . ILE   G  7  40  ? 41.670  -88.164  75.629  1.00 120.51 ? 31  ILE   G CG2 1 
ATOM   11428 C  CD1 . ILE   G  7  40  ? 39.296  -86.873  77.125  1.00 119.45 ? 31  ILE   G CD1 1 
ATOM   11429 N  N   . ASN   G  7  41  ? 43.856  -85.791  76.039  1.00 104.10 ? 32  ASN   G N   1 
ATOM   11430 C  CA  . ASN   G  7  41  ? 45.333  -85.940  75.923  1.00 104.85 ? 32  ASN   G CA  1 
ATOM   11431 C  C   . ASN   G  7  41  ? 45.728  -87.372  76.301  1.00 100.93 ? 32  ASN   G C   1 
ATOM   11432 O  O   . ASN   G  7  41  ? 45.224  -87.878  77.326  1.00 99.42  ? 32  ASN   G O   1 
ATOM   11433 C  CB  . ASN   G  7  41  ? 46.092  -84.928  76.785  1.00 105.66 ? 32  ASN   G CB  1 
ATOM   11434 C  CG  . ASN   G  7  41  ? 45.936  -83.504  76.294  1.00 107.52 ? 32  ASN   G CG  1 
ATOM   11435 O  OD1 . ASN   G  7  41  ? 46.589  -83.101  75.334  1.00 114.98 ? 32  ASN   G OD1 1 
ATOM   11436 N  ND2 . ASN   G  7  41  ? 45.079  -82.734  76.944  1.00 111.93 ? 32  ASN   G ND2 1 
ATOM   11437 N  N   . SER   G  7  42  ? 46.601  -87.988  75.497  1.00 99.92  ? 33  SER   G N   1 
ATOM   11438 C  CA  . SER   G  7  42  ? 47.166  -89.345  75.720  1.00 99.72  ? 33  SER   G CA  1 
ATOM   11439 C  C   . SER   G  7  42  ? 48.684  -89.238  75.904  1.00 95.76  ? 33  SER   G C   1 
ATOM   11440 O  O   . SER   G  7  42  ? 49.269  -88.211  75.507  1.00 90.76  ? 33  SER   G O   1 
ATOM   11441 C  CB  . SER   G  7  42  ? 46.791  -90.302  74.604  1.00 100.98 ? 33  SER   G CB  1 
ATOM   11442 O  OG  . SER   G  7  42  ? 47.667  -90.187  73.490  1.00 100.44 ? 33  SER   G OG  1 
ATOM   11443 N  N   . LEU   G  7  43  ? 49.283  -90.268  76.499  1.00 94.78  ? 34  LEU   G N   1 
ATOM   11444 C  CA  . LEU   G  7  43  ? 50.721  -90.325  76.864  1.00 94.70  ? 34  LEU   G CA  1 
ATOM   11445 C  C   . LEU   G  7  43  ? 51.155  -91.793  76.872  1.00 92.79  ? 34  LEU   G C   1 
ATOM   11446 O  O   . LEU   G  7  43  ? 50.399  -92.619  77.420  1.00 92.59  ? 34  LEU   G O   1 
ATOM   11447 C  CB  . LEU   G  7  43  ? 50.881  -89.674  78.242  1.00 94.02  ? 34  LEU   G CB  1 
ATOM   11448 C  CG  . LEU   G  7  43  ? 52.252  -89.784  78.913  1.00 96.52  ? 34  LEU   G CG  1 
ATOM   11449 C  CD1 . LEU   G  7  43  ? 52.413  -88.698  79.966  1.00 98.29  ? 34  LEU   G CD1 1 
ATOM   11450 C  CD2 . LEU   G  7  43  ? 52.466  -91.146  79.553  1.00 96.55  ? 34  LEU   G CD2 1 
ATOM   11451 N  N   . ALA   G  7  44  ? 52.313  -92.101  76.281  1.00 94.46  ? 35  ALA   G N   1 
ATOM   11452 C  CA  . ALA   G  7  44  ? 52.926  -93.451  76.282  1.00 93.19  ? 35  ALA   G CA  1 
ATOM   11453 C  C   . ALA   G  7  44  ? 54.385  -93.354  76.742  1.00 92.09  ? 35  ALA   G C   1 
ATOM   11454 O  O   . ALA   G  7  44  ? 55.093  -92.427  76.299  1.00 90.19  ? 35  ALA   G O   1 
ATOM   11455 C  CB  . ALA   G  7  44  ? 52.820  -94.082  74.915  1.00 90.47  ? 35  ALA   G CB  1 
ATOM   11456 N  N   . VAL   G  7  45  ? 54.801  -94.279  77.608  1.00 93.74  ? 36  VAL   G N   1 
ATOM   11457 C  CA  . VAL   G  7  45  ? 56.209  -94.429  78.086  1.00 96.53  ? 36  VAL   G CA  1 
ATOM   11458 C  C   . VAL   G  7  45  ? 56.574  -95.917  78.114  1.00 96.09  ? 36  VAL   G C   1 
ATOM   11459 O  O   . VAL   G  7  45  ? 55.659  -96.771  78.125  1.00 91.16  ? 36  VAL   G O   1 
ATOM   11460 C  CB  . VAL   G  7  45  ? 56.421  -93.789  79.471  1.00 97.90  ? 36  VAL   G CB  1 
ATOM   11461 C  CG1 . VAL   G  7  45  ? 56.423  -92.273  79.392  1.00 101.22 ? 36  VAL   G CG1 1 
ATOM   11462 C  CG2 . VAL   G  7  45  ? 55.398  -94.277  80.485  1.00 98.51  ? 36  VAL   G CG2 1 
ATOM   11463 N  N   . ARG   G  7  46  ? 57.876  -96.200  78.150  1.00 96.71  ? 37  ARG   G N   1 
ATOM   11464 C  CA  . ARG   G  7  46  ? 58.434  -97.573  78.162  1.00 98.17  ? 37  ARG   G CA  1 
ATOM   11465 C  C   . ARG   G  7  46  ? 59.202  -97.807  79.465  1.00 103.59 ? 37  ARG   G C   1 
ATOM   11466 O  O   . ARG   G  7  46  ? 60.006  -96.935  79.848  1.00 98.51  ? 37  ARG   G O   1 
ATOM   11467 C  CB  . ARG   G  7  46  ? 59.379  -97.776  76.979  1.00 98.26  ? 37  ARG   G CB  1 
ATOM   11468 C  CG  . ARG   G  7  46  ? 58.775  -97.433  75.626  1.00 95.70  ? 37  ARG   G CG  1 
ATOM   11469 C  CD  . ARG   G  7  46  ? 59.749  -97.756  74.512  1.00 96.96  ? 37  ARG   G CD  1 
ATOM   11470 N  NE  . ARG   G  7  46  ? 61.027  -97.079  74.691  1.00 95.30  ? 37  ARG   G NE  1 
ATOM   11471 C  CZ  . ARG   G  7  46  ? 62.126  -97.322  73.984  1.00 97.74  ? 37  ARG   G CZ  1 
ATOM   11472 N  NH1 . ARG   G  7  46  ? 62.127  -98.237  73.030  1.00 97.73  ? 37  ARG   G NH1 1 
ATOM   11473 N  NH2 . ARG   G  7  46  ? 63.229  -96.643  74.240  1.00 98.76  ? 37  ARG   G NH2 1 
ATOM   11474 N  N   . GLY   G  7  47  ? 58.962  -98.955  80.102  1.00 107.01 ? 38  GLY   G N   1 
ATOM   11475 C  CA  . GLY   G  7  47  ? 59.790  -99.482  81.200  1.00 112.45 ? 38  GLY   G CA  1 
ATOM   11476 C  C   . GLY   G  7  47  ? 60.850  -100.426 80.662  1.00 114.40 ? 38  GLY   G C   1 
ATOM   11477 O  O   . GLY   G  7  47  ? 61.099  -100.402 79.438  1.00 111.69 ? 38  GLY   G O   1 
ATOM   11478 N  N   . LYS   G  7  48  ? 61.456  -101.228 81.539  1.00 115.60 ? 39  LYS   G N   1 
ATOM   11479 C  CA  . LYS   G  7  48  ? 62.415  -102.296 81.155  1.00 116.12 ? 39  LYS   G CA  1 
ATOM   11480 C  C   . LYS   G  7  48  ? 61.634  -103.461 80.538  1.00 113.32 ? 39  LYS   G C   1 
ATOM   11481 O  O   . LYS   G  7  48  ? 62.030  -103.930 79.453  1.00 112.55 ? 39  LYS   G O   1 
ATOM   11482 C  CB  . LYS   G  7  48  ? 63.216  -102.766 82.373  1.00 118.11 ? 39  LYS   G CB  1 
ATOM   11483 C  CG  . LYS   G  7  48  ? 64.318  -101.817 82.823  1.00 124.43 ? 39  LYS   G CG  1 
ATOM   11484 C  CD  . LYS   G  7  48  ? 64.708  -101.985 84.278  1.00 126.88 ? 39  LYS   G CD  1 
ATOM   11485 C  CE  . LYS   G  7  48  ? 65.266  -103.355 84.602  1.00 129.64 ? 39  LYS   G CE  1 
ATOM   11486 N  NZ  . LYS   G  7  48  ? 66.623  -103.543 84.039  1.00 134.17 ? 39  LYS   G NZ  1 
ATOM   11487 N  N   . ASP   G  7  49  ? 60.559  -103.885 81.210  1.00 114.81 ? 40  ASP   G N   1 
ATOM   11488 C  CA  . ASP   G  7  49  ? 59.789  -105.118 80.894  1.00 114.14 ? 40  ASP   G CA  1 
ATOM   11489 C  C   . ASP   G  7  49  ? 58.469  -104.783 80.191  1.00 108.11 ? 40  ASP   G C   1 
ATOM   11490 O  O   . ASP   G  7  49  ? 57.875  -105.714 79.624  1.00 106.05 ? 40  ASP   G O   1 
ATOM   11491 C  CB  . ASP   G  7  49  ? 59.502  -105.925 82.165  1.00 118.33 ? 40  ASP   G CB  1 
ATOM   11492 C  CG  . ASP   G  7  49  ? 60.630  -106.852 82.585  1.00 125.02 ? 40  ASP   G CG  1 
ATOM   11493 O  OD1 . ASP   G  7  49  ? 61.759  -106.675 82.082  1.00 128.14 ? 40  ASP   G OD1 1 
ATOM   11494 O  OD2 . ASP   G  7  49  ? 60.369  -107.749 83.412  1.00 136.00 ? 40  ASP   G OD2 1 
ATOM   11495 N  N   . CYS   G  7  50  ? 58.017  -103.525 80.225  1.00 106.35 ? 41  CYS   G N   1 
ATOM   11496 C  CA  . CYS   G  7  50  ? 56.629  -103.147 79.847  1.00 99.22  ? 41  CYS   G CA  1 
ATOM   11497 C  C   . CYS   G  7  50  ? 56.594  -101.846 79.038  1.00 98.22  ? 41  CYS   G C   1 
ATOM   11498 O  O   . CYS   G  7  50  ? 57.617  -101.132 78.987  1.00 101.20 ? 41  CYS   G O   1 
ATOM   11499 C  CB  . CYS   G  7  50  ? 55.757  -102.997 81.089  1.00 99.49  ? 41  CYS   G CB  1 
ATOM   11500 S  SG  . CYS   G  7  50  ? 56.351  -101.722 82.234  1.00 97.49  ? 41  CYS   G SG  1 
ATOM   11501 N  N   . THR   G  7  51  ? 55.439  -101.583 78.424  1.00 92.04  ? 42  THR   G N   1 
ATOM   11502 C  CA  . THR   G  7  51  ? 55.062  -100.306 77.773  1.00 91.24  ? 42  THR   G CA  1 
ATOM   11503 C  C   . THR   G  7  51  ? 53.707  -99.876  78.338  1.00 90.47  ? 42  THR   G C   1 
ATOM   11504 O  O   . THR   G  7  51  ? 52.737  -100.647 78.179  1.00 83.88  ? 42  THR   G O   1 
ATOM   11505 C  CB  . THR   G  7  51  ? 55.024  -100.450 76.247  1.00 92.02  ? 42  THR   G CB  1 
ATOM   11506 O  OG1 . THR   G  7  51  ? 56.245  -101.070 75.840  1.00 90.02  ? 42  THR   G OG1 1 
ATOM   11507 C  CG2 . THR   G  7  51  ? 54.848  -99.123  75.539  1.00 94.14  ? 42  THR   G CG2 1 
ATOM   11508 N  N   . VAL   G  7  52  ? 53.660  -98.712  78.993  1.00 91.92  ? 43  VAL   G N   1 
ATOM   11509 C  CA  . VAL   G  7  52  ? 52.422  -98.135  79.595  1.00 93.23  ? 43  VAL   G CA  1 
ATOM   11510 C  C   . VAL   G  7  52  ? 51.907  -97.020  78.687  1.00 93.29  ? 43  VAL   G C   1 
ATOM   11511 O  O   . VAL   G  7  52  ? 52.712  -96.155  78.294  1.00 96.58  ? 43  VAL   G O   1 
ATOM   11512 C  CB  . VAL   G  7  52  ? 52.666  -97.604  81.018  1.00 94.80  ? 43  VAL   G CB  1 
ATOM   11513 C  CG1 . VAL   G  7  52  ? 51.425  -96.919  81.572  1.00 94.86  ? 43  VAL   G CG1 1 
ATOM   11514 C  CG2 . VAL   G  7  52  ? 53.139  -98.705  81.953  1.00 96.71  ? 43  VAL   G CG2 1 
ATOM   11515 N  N   . VAL   G  7  53  ? 50.607  -97.048  78.388  1.00 93.39  ? 44  VAL   G N   1 
ATOM   11516 C  CA  . VAL   G  7  53  ? 49.871  -95.935  77.723  1.00 93.97  ? 44  VAL   G CA  1 
ATOM   11517 C  C   . VAL   G  7  53  ? 48.762  -95.477  78.679  1.00 94.99  ? 44  VAL   G C   1 
ATOM   11518 O  O   . VAL   G  7  53  ? 48.068  -96.352  79.239  1.00 90.61  ? 44  VAL   G O   1 
ATOM   11519 C  CB  . VAL   G  7  53  ? 49.337  -96.353  76.337  1.00 92.13  ? 44  VAL   G CB  1 
ATOM   11520 C  CG1 . VAL   G  7  53  ? 48.164  -97.319  76.415  1.00 89.67  ? 44  VAL   G CG1 1 
ATOM   11521 C  CG2 . VAL   G  7  53  ? 48.970  -95.144  75.495  1.00 94.46  ? 44  VAL   G CG2 1 
ATOM   11522 N  N   . ILE   G  7  54  ? 48.640  -94.161  78.894  1.00 97.04  ? 45  ILE   G N   1 
ATOM   11523 C  CA  . ILE   G  7  54  ? 47.532  -93.536  79.679  1.00 96.81  ? 45  ILE   G CA  1 
ATOM   11524 C  C   . ILE   G  7  54  ? 46.863  -92.460  78.823  1.00 95.95  ? 45  ILE   G C   1 
ATOM   11525 O  O   . ILE   G  7  54  ? 47.554  -91.838  77.990  1.00 99.07  ? 45  ILE   G O   1 
ATOM   11526 C  CB  . ILE   G  7  54  ? 48.019  -92.968  81.027  1.00 99.73  ? 45  ILE   G CB  1 
ATOM   11527 C  CG1 . ILE   G  7  54  ? 48.973  -91.786  80.849  1.00 101.72 ? 45  ILE   G CG1 1 
ATOM   11528 C  CG2 . ILE   G  7  54  ? 48.643  -94.063  81.873  1.00 101.82 ? 45  ILE   G CG2 1 
ATOM   11529 C  CD1 . ILE   G  7  54  ? 49.154  -90.961  82.099  1.00 106.45 ? 45  ILE   G CD1 1 
ATOM   11530 N  N   . SER   G  7  55  ? 45.564  -92.261  79.041  1.00 95.42  ? 46  SER   G N   1 
ATOM   11531 C  CA  . SER   G  7  55  ? 44.705  -91.291  78.318  1.00 97.73  ? 46  SER   G CA  1 
ATOM   11532 C  C   . SER   G  7  55  ? 43.674  -90.724  79.296  1.00 95.21  ? 46  SER   G C   1 
ATOM   11533 O  O   . SER   G  7  55  ? 43.258  -91.462  80.207  1.00 100.47 ? 46  SER   G O   1 
ATOM   11534 C  CB  . SER   G  7  55  ? 44.049  -91.940  77.123  1.00 98.45  ? 46  SER   G CB  1 
ATOM   11535 O  OG  . SER   G  7  55  ? 43.145  -91.049  76.483  1.00 101.93 ? 46  SER   G OG  1 
ATOM   11536 N  N   . GLN   G  7  56  ? 43.303  -89.455  79.129  1.00 95.20  ? 47  GLN   G N   1 
ATOM   11537 C  CA  . GLN   G  7  56  ? 42.226  -88.819  79.929  1.00 97.30  ? 47  GLN   G CA  1 
ATOM   11538 C  C   . GLN   G  7  56  ? 40.909  -89.521  79.591  1.00 94.05  ? 47  GLN   G C   1 
ATOM   11539 O  O   . GLN   G  7  56  ? 40.759  -89.986  78.444  1.00 91.70  ? 47  GLN   G O   1 
ATOM   11540 C  CB  . GLN   G  7  56  ? 42.144  -87.317  79.651  1.00 97.60  ? 47  GLN   G CB  1 
ATOM   11541 C  CG  . GLN   G  7  56  ? 43.371  -86.544  80.107  1.00 97.46  ? 47  GLN   G CG  1 
ATOM   11542 C  CD  . GLN   G  7  56  ? 43.211  -85.066  79.859  1.00 97.76  ? 47  GLN   G CD  1 
ATOM   11543 O  OE1 . GLN   G  7  56  ? 43.758  -84.518  78.906  1.00 97.91  ? 47  GLN   G OE1 1 
ATOM   11544 N  NE2 . GLN   G  7  56  ? 42.436  -84.412  80.709  1.00 102.07 ? 47  GLN   G NE2 1 
ATOM   11545 N  N   . LYS   G  7  57  ? 40.008  -89.613  80.568  1.00 95.57  ? 48  LYS   G N   1 
ATOM   11546 C  CA  . LYS   G  7  57  ? 38.637  -90.156  80.398  1.00 98.53  ? 48  LYS   G CA  1 
ATOM   11547 C  C   . LYS   G  7  57  ? 37.637  -89.106  80.884  1.00 98.51  ? 48  LYS   G C   1 
ATOM   11548 O  O   . LYS   G  7  57  ? 37.464  -88.975  82.110  1.00 98.46  ? 48  LYS   G O   1 
ATOM   11549 C  CB  . LYS   G  7  57  ? 38.481  -91.470  81.165  1.00 100.03 ? 48  LYS   G CB  1 
ATOM   11550 C  CG  . LYS   G  7  57  ? 37.106  -92.111  81.052  1.00 104.00 ? 48  LYS   G CG  1 
ATOM   11551 C  CD  . LYS   G  7  57  ? 37.036  -93.482  81.671  1.00 108.00 ? 48  LYS   G CD  1 
ATOM   11552 C  CE  . LYS   G  7  57  ? 35.680  -94.132  81.497  1.00 110.88 ? 48  LYS   G CE  1 
ATOM   11553 N  NZ  . LYS   G  7  57  ? 35.716  -95.568  81.858  1.00 112.44 ? 48  LYS   G NZ  1 
ATOM   11554 N  N   . LYS   G  7  58  ? 37.025  -88.376  79.950  1.00 101.47 ? 49  LYS   G N   1 
ATOM   11555 C  CA  . LYS   G  7  58  ? 36.001  -87.343  80.244  1.00 103.99 ? 49  LYS   G CA  1 
ATOM   11556 C  C   . LYS   G  7  58  ? 34.629  -87.921  79.881  1.00 105.29 ? 49  LYS   G C   1 
ATOM   11557 O  O   . LYS   G  7  58  ? 34.382  -88.164  78.685  1.00 105.56 ? 49  LYS   G O   1 
ATOM   11558 C  CB  . LYS   G  7  58  ? 36.331  -86.044  79.502  1.00 105.77 ? 49  LYS   G CB  1 
ATOM   11559 C  CG  . LYS   G  7  58  ? 37.610  -85.361  79.970  1.00 106.99 ? 49  LYS   G CG  1 
ATOM   11560 C  CD  . LYS   G  7  58  ? 37.939  -84.079  79.235  1.00 109.18 ? 49  LYS   G CD  1 
ATOM   11561 C  CE  . LYS   G  7  58  ? 39.266  -83.489  79.663  1.00 109.53 ? 49  LYS   G CE  1 
ATOM   11562 N  NZ  . LYS   G  7  58  ? 39.594  -82.265  78.896  1.00 111.91 ? 49  LYS   G NZ  1 
ATOM   11563 N  N   . VAL   G  7  59  ? 33.803  -88.179  80.896  1.00 104.25 ? 50  VAL   G N   1 
ATOM   11564 C  CA  . VAL   G  7  59  ? 32.379  -88.602  80.753  1.00 107.36 ? 50  VAL   G CA  1 
ATOM   11565 C  C   . VAL   G  7  59  ? 31.506  -87.444  81.230  1.00 109.52 ? 50  VAL   G C   1 
ATOM   11566 O  O   . VAL   G  7  59  ? 31.189  -87.351  82.414  1.00 114.82 ? 50  VAL   G O   1 
ATOM   11567 C  CB  . VAL   G  7  59  ? 32.095  -89.901  81.532  1.00 107.45 ? 50  VAL   G CB  1 
ATOM   11568 C  CG1 . VAL   G  7  59  ? 30.731  -90.474  81.183  1.00 108.81 ? 50  VAL   G CG1 1 
ATOM   11569 C  CG2 . VAL   G  7  59  ? 33.183  -90.943  81.311  1.00 107.65 ? 50  VAL   G CG2 1 
ATOM   11570 N  N   . PRO   G  7  60  ? 31.111  -86.512  80.331  1.00 108.12 ? 51  PRO   G N   1 
ATOM   11571 C  CA  . PRO   G  7  60  ? 30.347  -85.332  80.735  1.00 107.84 ? 51  PRO   G CA  1 
ATOM   11572 C  C   . PRO   G  7  60  ? 28.887  -85.653  81.090  1.00 108.66 ? 51  PRO   G C   1 
ATOM   11573 O  O   . PRO   G  7  60  ? 28.396  -85.110  82.063  1.00 110.41 ? 51  PRO   G O   1 
ATOM   11574 C  CB  . PRO   G  7  60  ? 30.420  -84.421  79.502  1.00 107.91 ? 51  PRO   G CB  1 
ATOM   11575 C  CG  . PRO   G  7  60  ? 30.589  -85.374  78.335  1.00 106.77 ? 51  PRO   G CG  1 
ATOM   11576 C  CD  . PRO   G  7  60  ? 31.373  -86.547  78.884  1.00 105.77 ? 51  PRO   G CD  1 
ATOM   11577 N  N   . ASP   G  7  61  ? 28.240  -86.517  80.302  1.00 108.76 ? 52  ASP   G N   1 
ATOM   11578 C  CA  . ASP   G  7  61  ? 26.809  -86.893  80.464  1.00 110.94 ? 52  ASP   G CA  1 
ATOM   11579 C  C   . ASP   G  7  61  ? 26.687  -87.876  81.636  1.00 110.24 ? 52  ASP   G C   1 
ATOM   11580 O  O   . ASP   G  7  61  ? 27.497  -88.824  81.710  1.00 104.99 ? 52  ASP   G O   1 
ATOM   11581 C  CB  . ASP   G  7  61  ? 26.243  -87.458  79.156  1.00 110.51 ? 52  ASP   G CB  1 
ATOM   11582 C  CG  . ASP   G  7  61  ? 24.725  -87.509  79.085  1.00 113.21 ? 52  ASP   G CG  1 
ATOM   11583 O  OD1 . ASP   G  7  61  ? 24.083  -87.513  80.153  1.00 122.75 ? 52  ASP   G OD1 1 
ATOM   11584 O  OD2 . ASP   G  7  61  ? 24.196  -87.549  77.956  1.00 108.95 ? 52  ASP   G OD2 1 
ATOM   11585 N  N   . LYS   G  7  62  ? 25.708  -87.645  82.516  1.00 112.16 ? 53  LYS   G N   1 
ATOM   11586 C  CA  . LYS   G  7  62  ? 25.414  -88.489  83.706  1.00 113.35 ? 53  LYS   G CA  1 
ATOM   11587 C  C   . LYS   G  7  62  ? 24.648  -89.744  83.263  1.00 115.29 ? 53  LYS   G C   1 
ATOM   11588 O  O   . LYS   G  7  62  ? 24.640  -90.723  84.038  1.00 116.51 ? 53  LYS   G O   1 
ATOM   11589 C  CB  . LYS   G  7  62  ? 24.614  -87.691  84.743  1.00 117.61 ? 53  LYS   G CB  1 
ATOM   11590 C  CG  . LYS   G  7  62  ? 25.136  -87.776  86.171  1.00 120.46 ? 53  LYS   G CG  1 
ATOM   11591 C  CD  . LYS   G  7  62  ? 24.127  -87.335  87.211  1.00 127.01 ? 53  LYS   G CD  1 
ATOM   11592 C  CE  . LYS   G  7  62  ? 23.756  -85.870  87.106  1.00 130.46 ? 53  LYS   G CE  1 
ATOM   11593 N  NZ  . LYS   G  7  62  ? 22.542  -85.557  87.895  1.00 134.24 ? 53  LYS   G NZ  1 
ATOM   11594 N  N   . LEU   G  7  63  ? 24.031  -89.713  82.073  1.00 108.92 ? 54  LEU   G N   1 
ATOM   11595 C  CA  . LEU   G  7  63  ? 23.204  -90.820  81.512  1.00 107.53 ? 54  LEU   G CA  1 
ATOM   11596 C  C   . LEU   G  7  63  ? 24.083  -91.862  80.806  1.00 107.23 ? 54  LEU   G C   1 
ATOM   11597 O  O   . LEU   G  7  63  ? 23.579  -92.977  80.567  1.00 102.79 ? 54  LEU   G O   1 
ATOM   11598 C  CB  . LEU   G  7  63  ? 22.174  -90.251  80.530  1.00 105.01 ? 54  LEU   G CB  1 
ATOM   11599 C  CG  . LEU   G  7  63  ? 21.106  -89.334  81.123  1.00 104.89 ? 54  LEU   G CG  1 
ATOM   11600 C  CD1 . LEU   G  7  63  ? 20.121  -88.905  80.048  1.00 105.79 ? 54  LEU   G CD1 1 
ATOM   11601 C  CD2 . LEU   G  7  63  ? 20.371  -90.003  82.274  1.00 105.67 ? 54  LEU   G CD2 1 
ATOM   11602 N  N   . LEU   G  7  64  ? 25.328  -91.519  80.458  1.00 108.00 ? 55  LEU   G N   1 
ATOM   11603 C  CA  . LEU   G  7  64  ? 26.285  -92.466  79.823  1.00 107.33 ? 55  LEU   G CA  1 
ATOM   11604 C  C   . LEU   G  7  64  ? 26.607  -93.598  80.806  1.00 108.32 ? 55  LEU   G C   1 
ATOM   11605 O  O   . LEU   G  7  64  ? 26.652  -93.339  82.028  1.00 108.10 ? 55  LEU   G O   1 
ATOM   11606 C  CB  . LEU   G  7  64  ? 27.573  -91.738  79.419  1.00 105.68 ? 55  LEU   G CB  1 
ATOM   11607 C  CG  . LEU   G  7  64  ? 27.496  -90.881  78.156  1.00 106.25 ? 55  LEU   G CG  1 
ATOM   11608 C  CD1 . LEU   G  7  64  ? 28.679  -89.924  78.081  1.00 104.32 ? 55  LEU   G CD1 1 
ATOM   11609 C  CD2 . LEU   G  7  64  ? 27.434  -91.747  76.907  1.00 105.74 ? 55  LEU   G CD2 1 
ATOM   11610 N  N   . ASP   G  7  65  ? 26.806  -94.807  80.277  1.00 106.79 ? 56  ASP   G N   1 
ATOM   11611 C  CA  . ASP   G  7  65  ? 27.452  -95.937  80.990  1.00 104.87 ? 56  ASP   G CA  1 
ATOM   11612 C  C   . ASP   G  7  65  ? 28.959  -95.729  80.881  1.00 101.31 ? 56  ASP   G C   1 
ATOM   11613 O  O   . ASP   G  7  65  ? 29.528  -95.915  79.808  1.00 95.85  ? 56  ASP   G O   1 
ATOM   11614 C  CB  . ASP   G  7  65  ? 27.010  -97.286  80.418  1.00 106.18 ? 56  ASP   G CB  1 
ATOM   11615 C  CG  . ASP   G  7  65  ? 27.618  -98.488  81.121  1.00 109.71 ? 56  ASP   G CG  1 
ATOM   11616 O  OD1 . ASP   G  7  65  ? 28.396  -98.286  82.081  1.00 104.63 ? 56  ASP   G OD1 1 
ATOM   11617 O  OD2 . ASP   G  7  65  ? 27.306  -99.620  80.704  1.00 113.23 ? 56  ASP   G OD2 1 
ATOM   11618 N  N   . PRO   G  7  66  ? 29.648  -95.328  81.975  1.00 102.83 ? 57  PRO   G N   1 
ATOM   11619 C  CA  . PRO   G  7  66  ? 31.062  -94.951  81.896  1.00 101.19 ? 57  PRO   G CA  1 
ATOM   11620 C  C   . PRO   G  7  66  ? 31.993  -96.085  81.431  1.00 100.68 ? 57  PRO   G C   1 
ATOM   11621 O  O   . PRO   G  7  66  ? 33.033  -95.781  80.872  1.00 92.18  ? 57  PRO   G O   1 
ATOM   11622 C  CB  . PRO   G  7  66  ? 31.406  -94.520  83.333  1.00 102.53 ? 57  PRO   G CB  1 
ATOM   11623 C  CG  . PRO   G  7  66  ? 30.371  -95.209  84.195  1.00 104.55 ? 57  PRO   G CG  1 
ATOM   11624 C  CD  . PRO   G  7  66  ? 29.119  -95.234  83.345  1.00 105.51 ? 57  PRO   G CD  1 
ATOM   11625 N  N   . THR   G  7  67  ? 31.600  -97.345  81.651  1.00 101.16 ? 58  THR   G N   1 
ATOM   11626 C  CA  . THR   G  7  67  ? 32.408  -98.553  81.323  1.00 98.90  ? 58  THR   G CA  1 
ATOM   11627 C  C   . THR   G  7  67  ? 32.522  -98.739  79.805  1.00 97.95  ? 58  THR   G C   1 
ATOM   11628 O  O   . THR   G  7  67  ? 33.472  -99.430  79.384  1.00 96.43  ? 58  THR   G O   1 
ATOM   11629 C  CB  . THR   G  7  67  ? 31.820  -99.808  81.974  1.00 100.12 ? 58  THR   G CB  1 
ATOM   11630 O  OG1 . THR   G  7  67  ? 30.437  -99.871  81.629  1.00 101.43 ? 58  THR   G OG1 1 
ATOM   11631 C  CG2 . THR   G  7  67  ? 31.975  -99.813  83.478  1.00 103.61 ? 58  THR   G CG2 1 
ATOM   11632 N  N   . THR   G  7  68  ? 31.602  -98.157  79.022  1.00 99.93  ? 59  THR   G N   1 
ATOM   11633 C  CA  . THR   G  7  68  ? 31.543  -98.276  77.537  1.00 99.39  ? 59  THR   G CA  1 
ATOM   11634 C  C   . THR   G  7  68  ? 32.281  -97.112  76.859  1.00 98.42  ? 59  THR   G C   1 
ATOM   11635 O  O   . THR   G  7  68  ? 32.467  -97.187  75.630  1.00 98.80  ? 59  THR   G O   1 
ATOM   11636 C  CB  . THR   G  7  68  ? 30.096  -98.352  77.035  1.00 98.91  ? 59  THR   G CB  1 
ATOM   11637 O  OG1 . THR   G  7  68  ? 29.451  -97.110  77.318  1.00 99.15  ? 59  THR   G OG1 1 
ATOM   11638 C  CG2 . THR   G  7  68  ? 29.322  -99.492  77.659  1.00 99.33  ? 59  THR   G CG2 1 
ATOM   11639 N  N   . VAL   G  7  69  ? 32.672  -96.076  77.608  1.00 99.62  ? 60  VAL   G N   1 
ATOM   11640 C  CA  . VAL   G  7  69  ? 33.458  -94.918  77.081  1.00 99.14  ? 60  VAL   G CA  1 
ATOM   11641 C  C   . VAL   G  7  69  ? 34.949  -95.262  77.167  1.00 97.70  ? 60  VAL   G C   1 
ATOM   11642 O  O   . VAL   G  7  69  ? 35.495  -95.240  78.287  1.00 98.50  ? 60  VAL   G O   1 
ATOM   11643 C  CB  . VAL   G  7  69  ? 33.142  -93.617  77.841  1.00 99.21  ? 60  VAL   G CB  1 
ATOM   11644 C  CG1 . VAL   G  7  69  ? 33.954  -92.450  77.301  1.00 101.38 ? 60  VAL   G CG1 1 
ATOM   11645 C  CG2 . VAL   G  7  69  ? 31.656  -93.295  77.813  1.00 100.67 ? 60  VAL   G CG2 1 
ATOM   11646 N  N   . SER   G  7  70  ? 35.579  -95.555  76.026  1.00 94.74  ? 61  SER   G N   1 
ATOM   11647 C  CA  . SER   G  7  70  ? 36.998  -95.988  75.944  1.00 96.37  ? 61  SER   G CA  1 
ATOM   11648 C  C   . SER   G  7  70  ? 37.609  -95.585  74.600  1.00 92.85  ? 61  SER   G C   1 
ATOM   11649 O  O   . SER   G  7  70  ? 36.933  -95.762  73.567  1.00 92.68  ? 61  SER   G O   1 
ATOM   11650 C  CB  . SER   G  7  70  ? 37.114  -97.476  76.160  1.00 96.98  ? 61  SER   G CB  1 
ATOM   11651 O  OG  . SER   G  7  70  ? 38.473  -97.892  76.150  1.00 99.15  ? 61  SER   G OG  1 
ATOM   11652 N  N   . TYR   G  7  71  ? 38.847  -95.081  74.627  1.00 91.22  ? 62  TYR   G N   1 
ATOM   11653 C  CA  . TYR   G  7  71  ? 39.670  -94.774  73.427  1.00 92.09  ? 62  TYR   G CA  1 
ATOM   11654 C  C   . TYR   G  7  71  ? 40.933  -95.644  73.413  1.00 89.34  ? 62  TYR   G C   1 
ATOM   11655 O  O   . TYR   G  7  71  ? 41.815  -95.371  72.574  1.00 82.73  ? 62  TYR   G O   1 
ATOM   11656 C  CB  . TYR   G  7  71  ? 40.000  -93.281  73.384  1.00 93.51  ? 62  TYR   G CB  1 
ATOM   11657 C  CG  . TYR   G  7  71  ? 38.822  -92.405  73.040  1.00 95.78  ? 62  TYR   G CG  1 
ATOM   11658 C  CD1 . TYR   G  7  71  ? 37.955  -91.957  74.022  1.00 101.21 ? 62  TYR   G CD1 1 
ATOM   11659 C  CD2 . TYR   G  7  71  ? 38.559  -92.038  71.730  1.00 95.48  ? 62  TYR   G CD2 1 
ATOM   11660 C  CE1 . TYR   G  7  71  ? 36.865  -91.157  73.717  1.00 102.09 ? 62  TYR   G CE1 1 
ATOM   11661 C  CE2 . TYR   G  7  71  ? 37.473  -91.241  71.407  1.00 96.19  ? 62  TYR   G CE2 1 
ATOM   11662 C  CZ  . TYR   G  7  71  ? 36.621  -90.798  72.403  1.00 97.29  ? 62  TYR   G CZ  1 
ATOM   11663 O  OH  . TYR   G  7  71  ? 35.548  -90.012  72.092  1.00 95.77  ? 62  TYR   G OH  1 
ATOM   11664 N  N   . ILE   G  7  72  ? 41.010  -96.651  74.297  1.00 92.07  ? 63  ILE   G N   1 
ATOM   11665 C  CA  . ILE   G  7  72  ? 42.069  -97.708  74.301  1.00 91.55  ? 63  ILE   G CA  1 
ATOM   11666 C  C   . ILE   G  7  72  ? 41.440  -99.021  73.817  1.00 90.80  ? 63  ILE   G C   1 
ATOM   11667 O  O   . ILE   G  7  72  ? 40.341  -99.368  74.297  1.00 87.85  ? 63  ILE   G O   1 
ATOM   11668 C  CB  . ILE   G  7  72  ? 42.730  -97.848  75.690  1.00 93.59  ? 63  ILE   G CB  1 
ATOM   11669 C  CG1 . ILE   G  7  72  ? 43.396  -96.533  76.110  1.00 93.21  ? 63  ILE   G CG1 1 
ATOM   11670 C  CG2 . ILE   G  7  72  ? 43.707  -99.018  75.709  1.00 91.65  ? 63  ILE   G CG2 1 
ATOM   11671 C  CD1 . ILE   G  7  72  ? 44.284  -96.625  77.330  1.00 95.24  ? 63  ILE   G CD1 1 
ATOM   11672 N  N   . PHE   G  7  73  ? 42.119  -99.710  72.896  1.00 91.03  ? 64  PHE   G N   1 
ATOM   11673 C  CA  . PHE   G  7  73  ? 41.643  -100.952 72.231  1.00 91.35  ? 64  PHE   G CA  1 
ATOM   11674 C  C   . PHE   G  7  73  ? 42.702  -102.050 72.354  1.00 90.60  ? 64  PHE   G C   1 
ATOM   11675 O  O   . PHE   G  7  73  ? 43.906  -101.756 72.209  1.00 89.12  ? 64  PHE   G O   1 
ATOM   11676 C  CB  . PHE   G  7  73  ? 41.328  -100.686 70.758  1.00 89.88  ? 64  PHE   G CB  1 
ATOM   11677 C  CG  . PHE   G  7  73  ? 40.268  -99.640  70.531  1.00 89.28  ? 64  PHE   G CG  1 
ATOM   11678 C  CD1 . PHE   G  7  73  ? 38.938  -99.999  70.381  1.00 91.37  ? 64  PHE   G CD1 1 
ATOM   11679 C  CD2 . PHE   G  7  73  ? 40.601  -98.296  70.476  1.00 88.57  ? 64  PHE   G CD2 1 
ATOM   11680 C  CE1 . PHE   G  7  73  ? 37.963  -99.035  70.173  1.00 91.05  ? 64  PHE   G CE1 1 
ATOM   11681 C  CE2 . PHE   G  7  73  ? 39.625  -97.333  70.268  1.00 90.36  ? 64  PHE   G CE2 1 
ATOM   11682 C  CZ  . PHE   G  7  73  ? 38.308  -97.704  70.116  1.00 90.62  ? 64  PHE   G CZ  1 
ATOM   11683 N  N   . CYS   G  7  74  ? 42.254  -103.282 72.606  1.00 92.19  ? 65  CYS   G N   1 
ATOM   11684 C  CA  . CYS   G  7  74  ? 43.093  -104.506 72.565  1.00 90.20  ? 65  CYS   G CA  1 
ATOM   11685 C  C   . CYS   G  7  74  ? 43.022  -105.082 71.148  1.00 88.80  ? 65  CYS   G C   1 
ATOM   11686 O  O   . CYS   G  7  74  ? 42.033  -105.774 70.838  1.00 92.26  ? 65  CYS   G O   1 
ATOM   11687 C  CB  . CYS   G  7  74  ? 42.636  -105.509 73.616  1.00 94.43  ? 65  CYS   G CB  1 
ATOM   11688 S  SG  . CYS   G  7  74  ? 42.485  -104.770 75.264  1.00 95.22  ? 65  CYS   G SG  1 
ATOM   11689 N  N   . ILE   G  7  75  ? 44.020  -104.773 70.315  1.00 83.01  ? 66  ILE   G N   1 
ATOM   11690 C  CA  . ILE   G  7  75  ? 44.072  -105.176 68.877  1.00 87.17  ? 66  ILE   G CA  1 
ATOM   11691 C  C   . ILE   G  7  75  ? 44.298  -106.692 68.807  1.00 87.05  ? 66  ILE   G C   1 
ATOM   11692 O  O   . ILE   G  7  75  ? 43.512  -107.389 68.134  1.00 88.25  ? 66  ILE   G O   1 
ATOM   11693 C  CB  . ILE   G  7  75  ? 45.162  -104.386 68.124  1.00 85.60  ? 66  ILE   G CB  1 
ATOM   11694 C  CG1 . ILE   G  7  75  ? 44.929  -102.875 68.205  1.00 86.10  ? 66  ILE   G CG1 1 
ATOM   11695 C  CG2 . ILE   G  7  75  ? 45.280  -104.854 66.682  1.00 83.30  ? 66  ILE   G CG2 1 
ATOM   11696 C  CD1 . ILE   G  7  75  ? 43.551  -102.432 67.766  1.00 88.98  ? 66  ILE   G CD1 1 
ATOM   11697 N  N   . SER   G  7  76  ? 45.337  -107.174 69.489  1.00 86.82  ? 67  SER   G N   1 
ATOM   11698 C  CA  . SER   G  7  76  ? 45.691  -108.610 69.599  1.00 88.49  ? 67  SER   G CA  1 
ATOM   11699 C  C   . SER   G  7  76  ? 46.007  -108.928 71.061  1.00 90.65  ? 67  SER   G C   1 
ATOM   11700 O  O   . SER   G  7  76  ? 45.834  -108.035 71.910  1.00 95.76  ? 67  SER   G O   1 
ATOM   11701 C  CB  . SER   G  7  76  ? 46.839  -108.953 68.681  1.00 84.92  ? 67  SER   G CB  1 
ATOM   11702 O  OG  . SER   G  7  76  ? 48.077  -108.476 69.187  1.00 85.39  ? 67  SER   G OG  1 
ATOM   11703 N  N   . ARG   G  7  77  ? 46.445  -110.154 71.347  1.00 92.82  ? 68  ARG   G N   1 
ATOM   11704 C  CA  . ARG   G  7  77  ? 46.854  -110.557 72.714  1.00 94.30  ? 68  ARG   G CA  1 
ATOM   11705 C  C   . ARG   G  7  77  ? 48.062  -109.717 73.141  1.00 90.87  ? 68  ARG   G C   1 
ATOM   11706 O  O   . ARG   G  7  77  ? 48.135  -109.407 74.337  1.00 91.39  ? 68  ARG   G O   1 
ATOM   11707 C  CB  . ARG   G  7  77  ? 47.162  -112.053 72.782  1.00 99.15  ? 68  ARG   G CB  1 
ATOM   11708 C  CG  . ARG   G  7  77  ? 47.234  -112.592 74.204  1.00 106.01 ? 68  ARG   G CG  1 
ATOM   11709 C  CD  . ARG   G  7  77  ? 47.265  -114.106 74.243  1.00 112.94 ? 68  ARG   G CD  1 
ATOM   11710 N  NE  . ARG   G  7  77  ? 46.002  -114.676 73.792  1.00 119.44 ? 68  ARG   G NE  1 
ATOM   11711 C  CZ  . ARG   G  7  77  ? 45.852  -115.897 73.283  1.00 128.43 ? 68  ARG   G CZ  1 
ATOM   11712 N  NH1 . ARG   G  7  77  ? 46.893  -116.706 73.151  1.00 135.30 ? 68  ARG   G NH1 1 
ATOM   11713 N  NH2 . ARG   G  7  77  ? 44.654  -116.307 72.900  1.00 134.85 ? 68  ARG   G NH2 1 
ATOM   11714 N  N   . THR   G  7  78  ? 48.942  -109.339 72.202  1.00 91.16  ? 69  THR   G N   1 
ATOM   11715 C  CA  . THR   G  7  78  ? 50.233  -108.644 72.479  1.00 90.82  ? 69  THR   G CA  1 
ATOM   11716 C  C   . THR   G  7  78  ? 50.159  -107.136 72.180  1.00 91.29  ? 69  THR   G C   1 
ATOM   11717 O  O   . THR   G  7  78  ? 50.930  -106.390 72.825  1.00 91.50  ? 69  THR   G O   1 
ATOM   11718 C  CB  . THR   G  7  78  ? 51.389  -109.299 71.712  1.00 90.15  ? 69  THR   G CB  1 
ATOM   11719 O  OG1 . THR   G  7  78  ? 51.078  -109.326 70.319  1.00 89.72  ? 69  THR   G OG1 1 
ATOM   11720 C  CG2 . THR   G  7  78  ? 51.669  -110.705 72.191  1.00 92.45  ? 69  THR   G CG2 1 
ATOM   11721 N  N   . ILE   G  7  79  ? 49.292  -106.691 71.261  1.00 89.05  ? 70  ILE   G N   1 
ATOM   11722 C  CA  . ILE   G  7  79  ? 49.243  -105.268 70.803  1.00 88.25  ? 70  ILE   G CA  1 
ATOM   11723 C  C   . ILE   G  7  79  ? 48.023  -104.558 71.400  1.00 87.09  ? 70  ILE   G C   1 
ATOM   11724 O  O   . ILE   G  7  79  ? 46.901  -105.097 71.306  1.00 82.28  ? 70  ILE   G O   1 
ATOM   11725 C  CB  . ILE   G  7  79  ? 49.258  -105.154 69.265  1.00 88.66  ? 70  ILE   G CB  1 
ATOM   11726 C  CG1 . ILE   G  7  79  ? 50.603  -105.604 68.690  1.00 91.34  ? 70  ILE   G CG1 1 
ATOM   11727 C  CG2 . ILE   G  7  79  ? 48.914  -103.736 68.830  1.00 88.45  ? 70  ILE   G CG2 1 
ATOM   11728 C  CD1 . ILE   G  7  79  ? 50.639  -105.692 67.182  1.00 91.36  ? 70  ILE   G CD1 1 
ATOM   11729 N  N   . GLY   G  7  80  ? 48.264  -103.368 71.958  1.00 88.77  ? 71  GLY   G N   1 
ATOM   11730 C  CA  . GLY   G  7  80  ? 47.241  -102.385 72.357  1.00 89.23  ? 71  GLY   G CA  1 
ATOM   11731 C  C   . GLY   G  7  80  ? 47.379  -101.107 71.549  1.00 88.14  ? 71  GLY   G C   1 
ATOM   11732 O  O   . GLY   G  7  80  ? 48.494  -100.828 71.058  1.00 85.77  ? 71  GLY   G O   1 
ATOM   11733 N  N   . MET   G  7  81  ? 46.287  -100.355 71.412  1.00 87.80  ? 72  MET   G N   1 
ATOM   11734 C  CA  . MET   G  7  81  ? 46.227  -99.122  70.588  1.00 87.65  ? 72  MET   G CA  1 
ATOM   11735 C  C   . MET   G  7  81  ? 45.298  -98.112  71.268  1.00 89.15  ? 72  MET   G C   1 
ATOM   11736 O  O   . MET   G  7  81  ? 44.144  -98.482  71.564  1.00 91.26  ? 72  MET   G O   1 
ATOM   11737 C  CB  . MET   G  7  81  ? 45.711  -99.456  69.184  1.00 85.52  ? 72  MET   G CB  1 
ATOM   11738 C  CG  . MET   G  7  81  ? 45.656  -98.274  68.233  1.00 85.91  ? 72  MET   G CG  1 
ATOM   11739 S  SD  . MET   G  7  81  ? 44.622  -98.621  66.787  1.00 83.89  ? 72  MET   G SD  1 
ATOM   11740 C  CE  . MET   G  7  81  ? 42.995  -98.590  67.541  1.00 86.88  ? 72  MET   G CE  1 
ATOM   11741 N  N   . VAL   G  7  82  ? 45.801  -96.901  71.529  1.00 90.03  ? 73  VAL   G N   1 
ATOM   11742 C  CA  . VAL   G  7  82  ? 44.996  -95.730  71.992  1.00 87.72  ? 73  VAL   G CA  1 
ATOM   11743 C  C   . VAL   G  7  82  ? 44.809  -94.789  70.801  1.00 89.79  ? 73  VAL   G C   1 
ATOM   11744 O  O   . VAL   G  7  82  ? 45.757  -94.665  69.996  1.00 93.42  ? 73  VAL   G O   1 
ATOM   11745 C  CB  . VAL   G  7  82  ? 45.635  -95.003  73.192  1.00 86.26  ? 73  VAL   G CB  1 
ATOM   11746 C  CG1 . VAL   G  7  82  ? 46.978  -94.378  72.851  1.00 84.21  ? 73  VAL   G CG1 1 
ATOM   11747 C  CG2 . VAL   G  7  82  ? 44.692  -93.957  73.767  1.00 88.40  ? 73  VAL   G CG2 1 
ATOM   11748 N  N   . VAL   G  7  83  ? 43.632  -94.163  70.704  1.00 90.79  ? 74  VAL   G N   1 
ATOM   11749 C  CA  . VAL   G  7  83  ? 43.247  -93.259  69.580  1.00 94.13  ? 74  VAL   G CA  1 
ATOM   11750 C  C   . VAL   G  7  83  ? 43.019  -91.845  70.122  1.00 93.52  ? 74  VAL   G C   1 
ATOM   11751 O  O   . VAL   G  7  83  ? 42.336  -91.704  71.155  1.00 101.92 ? 74  VAL   G O   1 
ATOM   11752 C  CB  . VAL   G  7  83  ? 41.987  -93.751  68.844  1.00 91.94  ? 74  VAL   G CB  1 
ATOM   11753 C  CG1 . VAL   G  7  83  ? 41.723  -92.920  67.599  1.00 93.22  ? 74  VAL   G CG1 1 
ATOM   11754 C  CG2 . VAL   G  7  83  ? 42.058  -95.228  68.492  1.00 90.09  ? 74  VAL   G CG2 1 
ATOM   11755 N  N   . ASN   G  7  84  ? 43.548  -90.846  69.415  1.00 95.47  ? 75  ASN   G N   1 
ATOM   11756 C  CA  . ASN   G  7  84  ? 43.201  -89.411  69.583  1.00 98.61  ? 75  ASN   G CA  1 
ATOM   11757 C  C   . ASN   G  7  84  ? 42.349  -88.983  68.387  1.00 94.44  ? 75  ASN   G C   1 
ATOM   11758 O  O   . ASN   G  7  84  ? 42.923  -88.802  67.293  1.00 92.14  ? 75  ASN   G O   1 
ATOM   11759 C  CB  . ASN   G  7  84  ? 44.450  -88.541  69.714  1.00 99.21  ? 75  ASN   G CB  1 
ATOM   11760 C  CG  . ASN   G  7  84  ? 45.071  -88.640  71.089  1.00 102.39 ? 75  ASN   G CG  1 
ATOM   11761 O  OD1 . ASN   G  7  84  ? 45.581  -89.693  71.467  1.00 99.02  ? 75  ASN   G OD1 1 
ATOM   11762 N  ND2 . ASN   G  7  84  ? 45.023  -87.555  71.843  1.00 106.51 ? 75  ASN   G ND2 1 
ATOM   11763 N  N   . GLY   G  7  85  ? 41.033  -88.857  68.587  1.00 97.15  ? 76  GLY   G N   1 
ATOM   11764 C  CA  . GLY   G  7  85  ? 40.084  -88.415  67.547  1.00 92.97  ? 76  GLY   G CA  1 
ATOM   11765 C  C   . GLY   G  7  85  ? 38.677  -88.957  67.778  1.00 89.45  ? 76  GLY   G C   1 
ATOM   11766 O  O   . GLY   G  7  85  ? 38.455  -89.736  68.705  1.00 86.25  ? 76  GLY   G O   1 
ATOM   11767 N  N   . PRO   G  7  86  ? 37.695  -88.569  66.927  1.00 84.81  ? 77  PRO   G N   1 
ATOM   11768 C  CA  . PRO   G  7  86  ? 36.302  -88.981  67.097  1.00 86.89  ? 77  PRO   G CA  1 
ATOM   11769 C  C   . PRO   G  7  86  ? 36.176  -90.511  67.146  1.00 86.67  ? 77  PRO   G C   1 
ATOM   11770 O  O   . PRO   G  7  86  ? 36.935  -91.189  66.473  1.00 86.13  ? 77  PRO   G O   1 
ATOM   11771 C  CB  . PRO   G  7  86  ? 35.589  -88.407  65.862  1.00 83.49  ? 77  PRO   G CB  1 
ATOM   11772 C  CG  . PRO   G  7  86  ? 36.474  -87.265  65.424  1.00 84.12  ? 77  PRO   G CG  1 
ATOM   11773 C  CD  . PRO   G  7  86  ? 37.879  -87.732  65.734  1.00 83.38  ? 77  PRO   G CD  1 
ATOM   11774 N  N   . ILE   G  7  87  ? 35.223  -91.010  67.935  1.00 90.98  ? 78  ILE   G N   1 
ATOM   11775 C  CA  . ILE   G  7  87  ? 35.082  -92.463  68.245  1.00 91.32  ? 78  ILE   G CA  1 
ATOM   11776 C  C   . ILE   G  7  87  ? 34.661  -93.245  66.999  1.00 91.09  ? 78  ILE   G C   1 
ATOM   11777 O  O   . ILE   G  7  87  ? 35.096  -94.384  66.846  1.00 96.62  ? 78  ILE   G O   1 
ATOM   11778 C  CB  . ILE   G  7  87  ? 34.155  -92.704  69.457  1.00 94.79  ? 78  ILE   G CB  1 
ATOM   11779 C  CG1 . ILE   G  7  87  ? 34.278  -94.138  69.984  1.00 94.92  ? 78  ILE   G CG1 1 
ATOM   11780 C  CG2 . ILE   G  7  87  ? 32.706  -92.337  69.161  1.00 96.91  ? 78  ILE   G CG2 1 
ATOM   11781 C  CD1 . ILE   G  7  87  ? 35.601  -94.443  70.655  1.00 95.43  ? 78  ILE   G CD1 1 
ATOM   11782 N  N   . PRO   G  7  88  ? 33.839  -92.715  66.058  1.00 89.39  ? 79  PRO   G N   1 
ATOM   11783 C  CA  . PRO   G  7  88  ? 33.451  -93.498  64.882  1.00 89.56  ? 79  PRO   G CA  1 
ATOM   11784 C  C   . PRO   G  7  88  ? 34.673  -93.901  64.043  1.00 88.58  ? 79  PRO   G C   1 
ATOM   11785 O  O   . PRO   G  7  88  ? 34.805  -95.070  63.733  1.00 88.23  ? 79  PRO   G O   1 
ATOM   11786 C  CB  . PRO   G  7  88  ? 32.521  -92.575  64.082  1.00 89.14  ? 79  PRO   G CB  1 
ATOM   11787 C  CG  . PRO   G  7  88  ? 32.075  -91.535  65.087  1.00 91.37  ? 79  PRO   G CG  1 
ATOM   11788 C  CD  . PRO   G  7  88  ? 33.242  -91.371  66.037  1.00 89.61  ? 79  PRO   G CD  1 
ATOM   11789 N  N   . ASP   G  7  89  ? 35.529  -92.927  63.714  1.00 88.32  ? 80  ASP   G N   1 
ATOM   11790 C  CA  . ASP   G  7  89  ? 36.817  -93.133  62.996  1.00 89.04  ? 80  ASP   G CA  1 
ATOM   11791 C  C   . ASP   G  7  89  ? 37.745  -94.006  63.847  1.00 87.66  ? 80  ASP   G C   1 
ATOM   11792 O  O   . ASP   G  7  89  ? 38.440  -94.861  63.264  1.00 85.79  ? 80  ASP   G O   1 
ATOM   11793 C  CB  . ASP   G  7  89  ? 37.494  -91.801  62.659  1.00 89.45  ? 80  ASP   G CB  1 
ATOM   11794 C  CG  . ASP   G  7  89  ? 36.856  -91.057  61.499  1.00 91.91  ? 80  ASP   G CG  1 
ATOM   11795 O  OD1 . ASP   G  7  89  ? 35.762  -91.472  61.064  1.00 93.08  ? 80  ASP   G OD1 1 
ATOM   11796 O  OD2 . ASP   G  7  89  ? 37.460  -90.068  61.032  1.00 95.50  ? 80  ASP   G OD2 1 
ATOM   11797 N  N   . ALA   G  7  90  ? 37.760  -93.790  65.168  1.00 87.48  ? 81  ALA   G N   1 
ATOM   11798 C  CA  . ALA   G  7  90  ? 38.613  -94.520  66.135  1.00 87.44  ? 81  ALA   G CA  1 
ATOM   11799 C  C   . ALA   G  7  90  ? 38.313  -96.022  66.058  1.00 86.87  ? 81  ALA   G C   1 
ATOM   11800 O  O   . ALA   G  7  90  ? 39.273  -96.813  65.980  1.00 84.48  ? 81  ALA   G O   1 
ATOM   11801 C  CB  . ALA   G  7  90  ? 38.401  -93.985  67.533  1.00 88.69  ? 81  ALA   G CB  1 
ATOM   11802 N  N   . ARG   G  7  91  ? 37.028  -96.392  66.068  1.00 86.05  ? 82  ARG   G N   1 
ATOM   11803 C  CA  . ARG   G  7  91  ? 36.561  -97.804  66.042  1.00 86.92  ? 82  ARG   G CA  1 
ATOM   11804 C  C   . ARG   G  7  91  ? 36.773  -98.393  64.643  1.00 89.37  ? 82  ARG   G C   1 
ATOM   11805 O  O   . ARG   G  7  91  ? 37.102  -99.593  64.559  1.00 88.05  ? 82  ARG   G O   1 
ATOM   11806 C  CB  . ARG   G  7  91  ? 35.095  -97.902  66.476  1.00 87.53  ? 82  ARG   G CB  1 
ATOM   11807 C  CG  . ARG   G  7  91  ? 34.900  -97.762  67.978  1.00 87.81  ? 82  ARG   G CG  1 
ATOM   11808 C  CD  . ARG   G  7  91  ? 33.459  -97.501  68.359  1.00 89.36  ? 82  ARG   G CD  1 
ATOM   11809 N  NE  . ARG   G  7  91  ? 33.308  -97.444  69.805  1.00 91.81  ? 82  ARG   G NE  1 
ATOM   11810 C  CZ  . ARG   G  7  91  ? 32.294  -96.873  70.448  1.00 93.92  ? 82  ARG   G CZ  1 
ATOM   11811 N  NH1 . ARG   G  7  91  ? 31.318  -96.281  69.779  1.00 93.10  ? 82  ARG   G NH1 1 
ATOM   11812 N  NH2 . ARG   G  7  91  ? 32.268  -96.884  71.770  1.00 99.28  ? 82  ARG   G NH2 1 
ATOM   11813 N  N   . ASN   G  7  92  ? 36.575  -97.588  63.593  1.00 87.88  ? 83  ASN   G N   1 
ATOM   11814 C  CA  . ASN   G  7  92  ? 36.863  -97.965  62.183  1.00 87.80  ? 83  ASN   G CA  1 
ATOM   11815 C  C   . ASN   G  7  92  ? 38.307  -98.475  62.089  1.00 88.63  ? 83  ASN   G C   1 
ATOM   11816 O  O   . ASN   G  7  92  ? 38.513  -99.555  61.503  1.00 88.79  ? 83  ASN   G O   1 
ATOM   11817 C  CB  . ASN   G  7  92  ? 36.611  -96.797  61.224  1.00 87.16  ? 83  ASN   G CB  1 
ATOM   11818 C  CG  . ASN   G  7  92  ? 36.983  -97.096  59.785  1.00 86.40  ? 83  ASN   G CG  1 
ATOM   11819 O  OD1 . ASN   G  7  92  ? 36.110  -97.207  58.928  1.00 92.00  ? 83  ASN   G OD1 1 
ATOM   11820 N  ND2 . ASN   G  7  92  ? 38.271  -97.218  59.500  1.00 83.73  ? 83  ASN   G ND2 1 
ATOM   11821 N  N   . ALA   G  7  93  ? 39.260  -97.716  62.640  1.00 88.23  ? 84  ALA   G N   1 
ATOM   11822 C  CA  . ALA   G  7  93  ? 40.711  -98.024  62.640  1.00 88.24  ? 84  ALA   G CA  1 
ATOM   11823 C  C   . ALA   G  7  93  ? 40.986  -99.298  63.452  1.00 87.50  ? 84  ALA   G C   1 
ATOM   11824 O  O   . ALA   G  7  93  ? 41.808  -100.119 62.997  1.00 85.63  ? 84  ALA   G O   1 
ATOM   11825 C  CB  . ALA   G  7  93  ? 41.487  -96.851  63.188  1.00 87.74  ? 84  ALA   G CB  1 
ATOM   11826 N  N   . ALA   G  7  94  ? 40.327  -99.445  64.607  1.00 86.25  ? 85  ALA   G N   1 
ATOM   11827 C  CA  . ALA   G  7  94  ? 40.519  -100.557 65.569  1.00 86.68  ? 85  ALA   G CA  1 
ATOM   11828 C  C   . ALA   G  7  94  ? 40.093  -101.890 64.936  1.00 87.10  ? 85  ALA   G C   1 
ATOM   11829 O  O   . ALA   G  7  94  ? 40.856  -102.873 65.067  1.00 85.62  ? 85  ALA   G O   1 
ATOM   11830 C  CB  . ALA   G  7  94  ? 39.762  -100.278 66.846  1.00 86.04  ? 85  ALA   G CB  1 
ATOM   11831 N  N   . LEU   G  7  95  ? 38.932  -101.931 64.271  1.00 85.34  ? 86  LEU   G N   1 
ATOM   11832 C  CA  . LEU   G  7  95  ? 38.401  -103.172 63.640  1.00 83.37  ? 86  LEU   G CA  1 
ATOM   11833 C  C   . LEU   G  7  95  ? 39.353  -103.614 62.526  1.00 85.83  ? 86  LEU   G C   1 
ATOM   11834 O  O   . LEU   G  7  95  ? 39.643  -104.825 62.446  1.00 91.16  ? 86  LEU   G O   1 
ATOM   11835 C  CB  . LEU   G  7  95  ? 36.986  -102.943 63.096  1.00 81.37  ? 86  LEU   G CB  1 
ATOM   11836 C  CG  . LEU   G  7  95  ? 36.361  -104.135 62.368  1.00 81.92  ? 86  LEU   G CG  1 
ATOM   11837 C  CD1 . LEU   G  7  95  ? 36.333  -105.375 63.251  1.00 82.07  ? 86  LEU   G CD1 1 
ATOM   11838 C  CD2 . LEU   G  7  95  ? 34.958  -103.808 61.880  1.00 81.11  ? 86  LEU   G CD2 1 
ATOM   11839 N  N   . ARG   G  7  96  ? 39.819  -102.674 61.700  1.00 81.72  ? 87  ARG   G N   1 
ATOM   11840 C  CA  . ARG   G  7  96  ? 40.759  -102.962 60.586  1.00 81.30  ? 87  ARG   G CA  1 
ATOM   11841 C  C   . ARG   G  7  96  ? 42.071  -103.507 61.160  1.00 79.67  ? 87  ARG   G C   1 
ATOM   11842 O  O   . ARG   G  7  96  ? 42.570  -104.507 60.625  1.00 79.65  ? 87  ARG   G O   1 
ATOM   11843 C  CB  . ARG   G  7  96  ? 41.014  -101.714 59.737  1.00 82.01  ? 87  ARG   G CB  1 
ATOM   11844 C  CG  . ARG   G  7  96  ? 41.882  -101.965 58.512  1.00 83.66  ? 87  ARG   G CG  1 
ATOM   11845 C  CD  . ARG   G  7  96  ? 41.421  -103.169 57.713  1.00 85.06  ? 87  ARG   G CD  1 
ATOM   11846 N  NE  . ARG   G  7  96  ? 42.144  -103.307 56.457  1.00 85.79  ? 87  ARG   G NE  1 
ATOM   11847 C  CZ  . ARG   G  7  96  ? 41.843  -102.682 55.322  1.00 84.90  ? 87  ARG   G CZ  1 
ATOM   11848 N  NH1 . ARG   G  7  96  ? 40.816  -101.850 55.260  1.00 86.06  ? 87  ARG   G NH1 1 
ATOM   11849 N  NH2 . ARG   G  7  96  ? 42.579  -102.893 54.246  1.00 86.47  ? 87  ARG   G NH2 1 
ATOM   11850 N  N   . ALA   G  7  97  ? 42.593  -102.874 62.214  1.00 80.22  ? 88  ALA   G N   1 
ATOM   11851 C  CA  . ALA   G  7  97  ? 43.860  -103.246 62.888  1.00 83.01  ? 88  ALA   G CA  1 
ATOM   11852 C  C   . ALA   G  7  97  ? 43.754  -104.672 63.438  1.00 84.36  ? 88  ALA   G C   1 
ATOM   11853 O  O   . ALA   G  7  97  ? 44.717  -105.445 63.267  1.00 88.68  ? 88  ALA   G O   1 
ATOM   11854 C  CB  . ALA   G  7  97  ? 44.177  -102.261 63.985  1.00 83.73  ? 88  ALA   G CB  1 
ATOM   11855 N  N   . LYS   G  7  98  ? 42.630  -104.995 64.084  1.00 86.14  ? 89  LYS   G N   1 
ATOM   11856 C  CA  . LYS   G  7  98  ? 42.333  -106.352 64.617  1.00 87.84  ? 89  LYS   G CA  1 
ATOM   11857 C  C   . LYS   G  7  98  ? 42.353  -107.362 63.462  1.00 89.23  ? 89  LYS   G C   1 
ATOM   11858 O  O   . LYS   G  7  98  ? 43.086  -108.368 63.566  1.00 91.38  ? 89  LYS   G O   1 
ATOM   11859 C  CB  . LYS   G  7  98  ? 40.985  -106.355 65.346  1.00 89.68  ? 89  LYS   G CB  1 
ATOM   11860 C  CG  . LYS   G  7  98  ? 40.980  -105.645 66.694  1.00 88.54  ? 89  LYS   G CG  1 
ATOM   11861 C  CD  . LYS   G  7  98  ? 39.597  -105.433 67.262  1.00 88.57  ? 89  LYS   G CD  1 
ATOM   11862 C  CE  . LYS   G  7  98  ? 39.618  -104.723 68.596  1.00 88.81  ? 89  LYS   G CE  1 
ATOM   11863 N  NZ  . LYS   G  7  98  ? 38.250  -104.534 69.131  1.00 92.26  ? 89  LYS   G NZ  1 
ATOM   11864 N  N   . ALA   G  7  99  ? 41.588  -107.092 62.400  1.00 85.10  ? 90  ALA   G N   1 
ATOM   11865 C  CA  . ALA   G  7  99  ? 41.459  -107.958 61.205  1.00 85.42  ? 90  ALA   G CA  1 
ATOM   11866 C  C   . ALA   G  7  99  ? 42.827  -108.160 60.541  1.00 86.72  ? 90  ALA   G C   1 
ATOM   11867 O  O   . ALA   G  7  99  ? 43.118  -109.301 60.134  1.00 92.22  ? 90  ALA   G O   1 
ATOM   11868 C  CB  . ALA   G  7  99  ? 40.464  -107.366 60.243  1.00 85.83  ? 90  ALA   G CB  1 
ATOM   11869 N  N   . GLU   G  7  100 ? 43.628  -107.097 60.433  1.00 83.99  ? 91  GLU   G N   1 
ATOM   11870 C  CA  . GLU   G  7  100 ? 44.980  -107.131 59.811  1.00 87.43  ? 91  GLU   G CA  1 
ATOM   11871 C  C   . GLU   G  7  100 ? 45.928  -107.996 60.648  1.00 88.17  ? 91  GLU   G C   1 
ATOM   11872 O  O   . GLU   G  7  100 ? 46.697  -108.766 60.043  1.00 92.00  ? 91  GLU   G O   1 
ATOM   11873 C  CB  . GLU   G  7  100 ? 45.556  -105.721 59.673  1.00 89.69  ? 91  GLU   G CB  1 
ATOM   11874 C  CG  . GLU   G  7  100 ? 44.900  -104.903 58.575  1.00 92.25  ? 91  GLU   G CG  1 
ATOM   11875 C  CD  . GLU   G  7  100 ? 45.141  -105.412 57.163  1.00 93.69  ? 91  GLU   G CD  1 
ATOM   11876 O  OE1 . GLU   G  7  100 ? 46.061  -106.237 56.975  1.00 99.76  ? 91  GLU   G OE1 1 
ATOM   11877 O  OE2 . GLU   G  7  100 ? 44.408  -104.979 56.252  1.00 93.74  ? 91  GLU   G OE2 1 
ATOM   11878 N  N   . ALA   G  7  101 ? 45.886  -107.857 61.979  1.00 87.67  ? 92  ALA   G N   1 
ATOM   11879 C  CA  . ALA   G  7  101 ? 46.747  -108.592 62.939  1.00 88.17  ? 92  ALA   G CA  1 
ATOM   11880 C  C   . ALA   G  7  101 ? 46.378  -110.082 62.956  1.00 87.70  ? 92  ALA   G C   1 
ATOM   11881 O  O   . ALA   G  7  101 ? 47.298  -110.909 63.096  1.00 86.20  ? 92  ALA   G O   1 
ATOM   11882 C  CB  . ALA   G  7  101 ? 46.641  -107.977 64.314  1.00 90.28  ? 92  ALA   G CB  1 
ATOM   11883 N  N   . ALA   G  7  102 ? 45.087  -110.405 62.818  1.00 86.15  ? 93  ALA   G N   1 
ATOM   11884 C  CA  . ALA   G  7  102 ? 44.552  -111.787 62.787  1.00 85.57  ? 93  ALA   G CA  1 
ATOM   11885 C  C   . ALA   G  7  102 ? 45.020  -112.491 61.508  1.00 86.50  ? 93  ALA   G C   1 
ATOM   11886 O  O   . ALA   G  7  102 ? 45.523  -113.628 61.606  1.00 83.51  ? 93  ALA   G O   1 
ATOM   11887 C  CB  . ALA   G  7  102 ? 43.045  -111.767 62.889  1.00 86.15  ? 93  ALA   G CB  1 
ATOM   11888 N  N   . GLU   G  7  103 ? 44.870  -111.826 60.359  1.00 85.40  ? 94  GLU   G N   1 
ATOM   11889 C  CA  . GLU   G  7  103 ? 45.252  -112.357 59.023  1.00 87.70  ? 94  GLU   G CA  1 
ATOM   11890 C  C   . GLU   G  7  103 ? 46.765  -112.603 58.980  1.00 89.53  ? 94  GLU   G C   1 
ATOM   11891 O  O   . GLU   G  7  103 ? 47.164  -113.677 58.499  1.00 93.43  ? 94  GLU   G O   1 
ATOM   11892 C  CB  . GLU   G  7  103 ? 44.824  -111.392 57.917  1.00 89.98  ? 94  GLU   G CB  1 
ATOM   11893 C  CG  . GLU   G  7  103 ? 45.158  -111.884 56.521  1.00 94.93  ? 94  GLU   G CG  1 
ATOM   11894 C  CD  . GLU   G  7  103 ? 45.030  -110.826 55.439  1.00 101.32 ? 94  GLU   G CD  1 
ATOM   11895 O  OE1 . GLU   G  7  103 ? 43.956  -110.194 55.351  1.00 111.10 ? 94  GLU   G OE1 1 
ATOM   11896 O  OE2 . GLU   G  7  103 ? 46.012  -110.624 54.694  1.00 104.77 ? 94  GLU   G OE2 1 
ATOM   11897 N  N   . PHE   G  7  104 ? 47.572  -111.646 59.449  1.00 86.86  ? 95  PHE   G N   1 
ATOM   11898 C  CA  . PHE   G  7  104 ? 49.056  -111.746 59.485  1.00 86.37  ? 95  PHE   G CA  1 
ATOM   11899 C  C   . PHE   G  7  104 ? 49.454  -113.068 60.152  1.00 86.18  ? 95  PHE   G C   1 
ATOM   11900 O  O   . PHE   G  7  104 ? 50.296  -113.793 59.588  1.00 88.18  ? 95  PHE   G O   1 
ATOM   11901 C  CB  . PHE   G  7  104 ? 49.685  -110.558 60.220  1.00 84.27  ? 95  PHE   G CB  1 
ATOM   11902 C  CG  . PHE   G  7  104 ? 51.193  -110.530 60.171  1.00 83.71  ? 95  PHE   G CG  1 
ATOM   11903 C  CD1 . PHE   G  7  104 ? 51.949  -111.271 61.069  1.00 85.49  ? 95  PHE   G CD1 1 
ATOM   11904 C  CD2 . PHE   G  7  104 ? 51.858  -109.777 59.217  1.00 82.55  ? 95  PHE   G CD2 1 
ATOM   11905 C  CE1 . PHE   G  7  104 ? 53.336  -111.253 61.016  1.00 86.26  ? 95  PHE   G CE1 1 
ATOM   11906 C  CE2 . PHE   G  7  104 ? 53.244  -109.758 59.166  1.00 83.38  ? 95  PHE   G CE2 1 
ATOM   11907 C  CZ  . PHE   G  7  104 ? 53.980  -110.495 60.065  1.00 85.15  ? 95  PHE   G CZ  1 
ATOM   11908 N  N   . ARG   G  7  105 ? 48.863  -113.362 61.315  1.00 86.61  ? 96  ARG   G N   1 
ATOM   11909 C  CA  . ARG   G  7  105 ? 49.169  -114.567 62.133  1.00 88.96  ? 96  ARG   G CA  1 
ATOM   11910 C  C   . ARG   G  7  105 ? 48.818  -115.827 61.332  1.00 87.03  ? 96  ARG   G C   1 
ATOM   11911 O  O   . ARG   G  7  105 ? 49.632  -116.775 61.338  1.00 86.49  ? 96  ARG   G O   1 
ATOM   11912 C  CB  . ARG   G  7  105 ? 48.425  -114.516 63.472  1.00 91.07  ? 96  ARG   G CB  1 
ATOM   11913 C  CG  . ARG   G  7  105 ? 48.579  -115.767 64.327  1.00 95.10  ? 96  ARG   G CG  1 
ATOM   11914 C  CD  . ARG   G  7  105 ? 50.020  -116.087 64.689  1.00 98.31  ? 96  ARG   G CD  1 
ATOM   11915 N  NE  . ARG   G  7  105 ? 50.148  -117.395 65.323  1.00 101.59 ? 96  ARG   G NE  1 
ATOM   11916 C  CZ  . ARG   G  7  105 ? 50.113  -118.563 64.681  1.00 102.13 ? 96  ARG   G CZ  1 
ATOM   11917 N  NH1 . ARG   G  7  105 ? 49.943  -118.609 63.370  1.00 103.39 ? 96  ARG   G NH1 1 
ATOM   11918 N  NH2 . ARG   G  7  105 ? 50.243  -119.691 65.357  1.00 103.66 ? 96  ARG   G NH2 1 
ATOM   11919 N  N   . TYR   G  7  106 ? 47.658  -115.837 60.666  1.00 87.55  ? 97  TYR   G N   1 
ATOM   11920 C  CA  . TYR   G  7  106 ? 47.171  -116.980 59.849  1.00 86.40  ? 97  TYR   G CA  1 
ATOM   11921 C  C   . TYR   G  7  106 ? 48.114  -117.203 58.662  1.00 88.10  ? 97  TYR   G C   1 
ATOM   11922 O  O   . TYR   G  7  106 ? 48.456  -118.365 58.386  1.00 90.84  ? 97  TYR   G O   1 
ATOM   11923 C  CB  . TYR   G  7  106 ? 45.736  -116.761 59.363  1.00 86.28  ? 97  TYR   G CB  1 
ATOM   11924 C  CG  . TYR   G  7  106 ? 45.264  -117.809 58.388  1.00 86.82  ? 97  TYR   G CG  1 
ATOM   11925 C  CD1 . TYR   G  7  106 ? 45.053  -119.119 58.792  1.00 88.54  ? 97  TYR   G CD1 1 
ATOM   11926 C  CD2 . TYR   G  7  106 ? 45.062  -117.506 57.051  1.00 87.37  ? 97  TYR   G CD2 1 
ATOM   11927 C  CE1 . TYR   G  7  106 ? 44.635  -120.094 57.900  1.00 89.50  ? 97  TYR   G CE1 1 
ATOM   11928 C  CE2 . TYR   G  7  106 ? 44.644  -118.469 56.146  1.00 88.16  ? 97  TYR   G CE2 1 
ATOM   11929 C  CZ  . TYR   G  7  106 ? 44.429  -119.768 56.572  1.00 88.20  ? 97  TYR   G CZ  1 
ATOM   11930 O  OH  . TYR   G  7  106 ? 44.019  -120.721 55.688  1.00 92.37  ? 97  TYR   G OH  1 
ATOM   11931 N  N   . LYS   G  7  107 ? 48.521  -116.126 57.987  1.00 84.77  ? 98  LYS   G N   1 
ATOM   11932 C  CA  . LYS   G  7  107 ? 49.329  -116.184 56.740  1.00 85.16  ? 98  LYS   G CA  1 
ATOM   11933 C  C   . LYS   G  7  107 ? 50.791  -116.547 57.032  1.00 85.98  ? 98  LYS   G C   1 
ATOM   11934 O  O   . LYS   G  7  107 ? 51.350  -117.333 56.241  1.00 85.86  ? 98  LYS   G O   1 
ATOM   11935 C  CB  . LYS   G  7  107 ? 49.281  -114.853 55.987  1.00 84.14  ? 98  LYS   G CB  1 
ATOM   11936 C  CG  . LYS   G  7  107 ? 48.167  -114.736 54.957  1.00 87.10  ? 98  LYS   G CG  1 
ATOM   11937 C  CD  . LYS   G  7  107 ? 48.406  -113.631 53.956  1.00 89.35  ? 98  LYS   G CD  1 
ATOM   11938 C  CE  . LYS   G  7  107 ? 47.502  -113.710 52.744  1.00 96.51  ? 98  LYS   G CE  1 
ATOM   11939 N  NZ  . LYS   G  7  107 ? 46.578  -112.552 52.675  1.00 100.93 ? 98  LYS   G NZ  1 
ATOM   11940 N  N   . TYR   G  7  108 ? 51.395  -115.984 58.088  1.00 85.34  ? 99  TYR   G N   1 
ATOM   11941 C  CA  . TYR   G  7  108 ? 52.871  -115.975 58.298  1.00 88.53  ? 99  TYR   G CA  1 
ATOM   11942 C  C   . TYR   G  7  108 ? 53.296  -116.745 59.554  1.00 86.94  ? 99  TYR   G C   1 
ATOM   11943 O  O   . TYR   G  7  108 ? 54.516  -116.830 59.784  1.00 86.03  ? 99  TYR   G O   1 
ATOM   11944 C  CB  . TYR   G  7  108 ? 53.389  -114.536 58.343  1.00 89.40  ? 99  TYR   G CB  1 
ATOM   11945 C  CG  . TYR   G  7  108 ? 53.055  -113.745 57.105  1.00 91.62  ? 99  TYR   G CG  1 
ATOM   11946 C  CD1 . TYR   G  7  108 ? 53.603  -114.086 55.879  1.00 92.24  ? 99  TYR   G CD1 1 
ATOM   11947 C  CD2 . TYR   G  7  108 ? 52.168  -112.683 57.148  1.00 89.93  ? 99  TYR   G CD2 1 
ATOM   11948 C  CE1 . TYR   G  7  108 ? 53.290  -113.383 54.728  1.00 91.69  ? 99  TYR   G CE1 1 
ATOM   11949 C  CE2 . TYR   G  7  108 ? 51.844  -111.970 56.007  1.00 90.38  ? 99  TYR   G CE2 1 
ATOM   11950 C  CZ  . TYR   G  7  108 ? 52.406  -112.321 54.792  1.00 92.79  ? 99  TYR   G CZ  1 
ATOM   11951 O  OH  . TYR   G  7  108 ? 52.096  -111.626 53.658  1.00 97.38  ? 99  TYR   G OH  1 
ATOM   11952 N  N   . GLY   G  7  109 ? 52.352  -117.277 60.337  1.00 89.27  ? 100 GLY   G N   1 
ATOM   11953 C  CA  . GLY   G  7  109 ? 52.629  -118.294 61.373  1.00 89.79  ? 100 GLY   G CA  1 
ATOM   11954 C  C   . GLY   G  7  109 ? 53.262  -117.722 62.633  1.00 87.93  ? 100 GLY   G C   1 
ATOM   11955 O  O   . GLY   G  7  109 ? 53.736  -118.525 63.460  1.00 84.07  ? 100 GLY   G O   1 
ATOM   11956 N  N   . TYR   G  7  110 ? 53.278  -116.395 62.788  1.00 88.05  ? 101 TYR   G N   1 
ATOM   11957 C  CA  . TYR   G  7  110 ? 53.763  -115.712 64.015  1.00 89.21  ? 101 TYR   G CA  1 
ATOM   11958 C  C   . TYR   G  7  110 ? 53.002  -114.398 64.202  1.00 88.53  ? 101 TYR   G C   1 
ATOM   11959 O  O   . TYR   G  7  110 ? 52.455  -113.878 63.214  1.00 85.60  ? 101 TYR   G O   1 
ATOM   11960 C  CB  . TYR   G  7  110 ? 55.283  -115.529 63.971  1.00 90.64  ? 101 TYR   G CB  1 
ATOM   11961 C  CG  . TYR   G  7  110 ? 55.792  -114.431 63.072  1.00 89.33  ? 101 TYR   G CG  1 
ATOM   11962 C  CD1 . TYR   G  7  110 ? 56.015  -114.655 61.723  1.00 89.72  ? 101 TYR   G CD1 1 
ATOM   11963 C  CD2 . TYR   G  7  110 ? 56.089  -113.176 63.576  1.00 88.09  ? 101 TYR   G CD2 1 
ATOM   11964 C  CE1 . TYR   G  7  110 ? 56.502  -113.656 60.895  1.00 89.86  ? 101 TYR   G CE1 1 
ATOM   11965 C  CE2 . TYR   G  7  110 ? 56.578  -112.166 62.763  1.00 89.09  ? 101 TYR   G CE2 1 
ATOM   11966 C  CZ  . TYR   G  7  110 ? 56.785  -112.406 61.417  1.00 88.81  ? 101 TYR   G CZ  1 
ATOM   11967 O  OH  . TYR   G  7  110 ? 57.266  -111.416 60.610  1.00 88.45  ? 101 TYR   G OH  1 
ATOM   11968 N  N   . ASP   G  7  111 ? 52.977  -113.901 65.443  1.00 90.25  ? 102 ASP   G N   1 
ATOM   11969 C  CA  . ASP   G  7  111 ? 52.177  -112.727 65.886  1.00 92.59  ? 102 ASP   G CA  1 
ATOM   11970 C  C   . ASP   G  7  111 ? 52.709  -111.459 65.208  1.00 91.35  ? 102 ASP   G C   1 
ATOM   11971 O  O   . ASP   G  7  111 ? 53.942  -111.257 65.207  1.00 92.34  ? 102 ASP   G O   1 
ATOM   11972 C  CB  . ASP   G  7  111 ? 52.208  -112.570 67.409  1.00 95.68  ? 102 ASP   G CB  1 
ATOM   11973 C  CG  . ASP   G  7  111 ? 51.678  -113.774 68.169  1.00 101.19 ? 102 ASP   G CG  1 
ATOM   11974 O  OD1 . ASP   G  7  111 ? 50.765  -114.443 67.645  1.00 106.94 ? 102 ASP   G OD1 1 
ATOM   11975 O  OD2 . ASP   G  7  111 ? 52.187  -114.034 69.280  1.00 106.32 ? 102 ASP   G OD2 1 
ATOM   11976 N  N   . MET   G  7  112 ? 51.806  -110.637 64.667  1.00 89.98  ? 103 MET   G N   1 
ATOM   11977 C  CA  . MET   G  7  112 ? 52.148  -109.369 63.973  1.00 89.71  ? 103 MET   G CA  1 
ATOM   11978 C  C   . MET   G  7  112 ? 52.878  -108.463 64.958  1.00 86.73  ? 103 MET   G C   1 
ATOM   11979 O  O   . MET   G  7  112 ? 52.339  -108.169 66.024  1.00 78.30  ? 103 MET   G O   1 
ATOM   11980 C  CB  . MET   G  7  112 ? 50.892  -108.660 63.457  1.00 91.44  ? 103 MET   G CB  1 
ATOM   11981 C  CG  . MET   G  7  112 ? 51.197  -107.525 62.496  1.00 93.23  ? 103 MET   G CG  1 
ATOM   11982 S  SD  . MET   G  7  112 ? 49.745  -106.940 61.574  1.00 92.69  ? 103 MET   G SD  1 
ATOM   11983 C  CE  . MET   G  7  112 ? 50.540  -106.292 60.105  1.00 91.54  ? 103 MET   G CE  1 
ATOM   11984 N  N   . PRO   G  7  113 ? 54.134  -108.045 64.662  1.00 90.93  ? 104 PRO   G N   1 
ATOM   11985 C  CA  . PRO   G  7  113 ? 54.827  -107.039 65.469  1.00 91.99  ? 104 PRO   G CA  1 
ATOM   11986 C  C   . PRO   G  7  113 ? 54.104  -105.683 65.459  1.00 91.35  ? 104 PRO   G C   1 
ATOM   11987 O  O   . PRO   G  7  113 ? 53.455  -105.364 64.478  1.00 92.05  ? 104 PRO   G O   1 
ATOM   11988 C  CB  . PRO   G  7  113 ? 56.211  -106.900 64.812  1.00 92.31  ? 104 PRO   G CB  1 
ATOM   11989 C  CG  . PRO   G  7  113 ? 56.383  -108.180 64.022  1.00 92.96  ? 104 PRO   G CG  1 
ATOM   11990 C  CD  . PRO   G  7  113 ? 54.984  -108.546 63.568  1.00 92.46  ? 104 PRO   G CD  1 
ATOM   11991 N  N   . CYS   G  7  114 ? 54.248  -104.928 66.550  1.00 91.64  ? 105 CYS   G N   1 
ATOM   11992 C  CA  . CYS   G  7  114 ? 53.645  -103.587 66.763  1.00 90.53  ? 105 CYS   G CA  1 
ATOM   11993 C  C   . CYS   G  7  114 ? 54.036  -102.653 65.608  1.00 84.31  ? 105 CYS   G C   1 
ATOM   11994 O  O   . CYS   G  7  114 ? 53.124  -102.030 65.030  1.00 81.04  ? 105 CYS   G O   1 
ATOM   11995 C  CB  . CYS   G  7  114 ? 54.080  -103.040 68.117  1.00 94.46  ? 105 CYS   G CB  1 
ATOM   11996 S  SG  . CYS   G  7  114 ? 53.523  -101.352 68.454  1.00 100.73 ? 105 CYS   G SG  1 
ATOM   11997 N  N   . ASP   G  7  115 ? 55.326  -102.603 65.255  1.00 82.51  ? 106 ASP   G N   1 
ATOM   11998 C  CA  . ASP   G  7  115 ? 55.883  -101.665 64.239  1.00 84.56  ? 106 ASP   G CA  1 
ATOM   11999 C  C   . ASP   G  7  115 ? 55.423  -102.046 62.824  1.00 87.36  ? 106 ASP   G C   1 
ATOM   12000 O  O   . ASP   G  7  115 ? 55.321  -101.132 61.978  1.00 86.27  ? 106 ASP   G O   1 
ATOM   12001 C  CB  . ASP   G  7  115 ? 57.410  -101.597 64.299  1.00 84.69  ? 106 ASP   G CB  1 
ATOM   12002 C  CG  . ASP   G  7  115 ? 58.096  -102.938 64.164  1.00 85.54  ? 106 ASP   G CG  1 
ATOM   12003 O  OD1 . ASP   G  7  115 ? 57.830  -103.809 65.013  1.00 89.02  ? 106 ASP   G OD1 1 
ATOM   12004 O  OD2 . ASP   G  7  115 ? 58.890  -103.093 63.217  1.00 85.05  ? 106 ASP   G OD2 1 
ATOM   12005 N  N   . VAL   G  7  116 ? 55.173  -103.332 62.562  1.00 83.95  ? 107 VAL   G N   1 
ATOM   12006 C  CA  . VAL   G  7  116 ? 54.699  -103.818 61.232  1.00 84.31  ? 107 VAL   G CA  1 
ATOM   12007 C  C   . VAL   G  7  116 ? 53.227  -103.417 61.072  1.00 83.29  ? 107 VAL   G C   1 
ATOM   12008 O  O   . VAL   G  7  116 ? 52.883  -102.890 59.997  1.00 84.31  ? 107 VAL   G O   1 
ATOM   12009 C  CB  . VAL   G  7  116 ? 54.917  -105.335 61.057  1.00 84.31  ? 107 VAL   G CB  1 
ATOM   12010 C  CG1 . VAL   G  7  116 ? 54.342  -105.845 59.742  1.00 84.96  ? 107 VAL   G CG1 1 
ATOM   12011 C  CG2 . VAL   G  7  116 ? 56.390  -105.703 61.161  1.00 84.51  ? 107 VAL   G CG2 1 
ATOM   12012 N  N   . LEU   G  7  117 ? 52.402  -103.641 62.102  1.00 82.58  ? 108 LEU   G N   1 
ATOM   12013 C  CA  . LEU   G  7  117 ? 50.965  -103.248 62.121  1.00 82.75  ? 108 LEU   G CA  1 
ATOM   12014 C  C   . LEU   G  7  117 ? 50.855  -101.731 61.937  1.00 86.11  ? 108 LEU   G C   1 
ATOM   12015 O  O   . LEU   G  7  117 ? 49.955  -101.292 61.192  1.00 85.92  ? 108 LEU   G O   1 
ATOM   12016 C  CB  . LEU   G  7  117 ? 50.318  -103.684 63.439  1.00 80.83  ? 108 LEU   G CB  1 
ATOM   12017 C  CG  . LEU   G  7  117 ? 48.893  -103.180 63.672  1.00 80.83  ? 108 LEU   G CG  1 
ATOM   12018 C  CD1 . LEU   G  7  117 ? 47.953  -103.636 62.567  1.00 81.22  ? 108 LEU   G CD1 1 
ATOM   12019 C  CD2 . LEU   G  7  117 ? 48.377  -103.636 65.025  1.00 80.70  ? 108 LEU   G CD2 1 
ATOM   12020 N  N   . ALA   G  7  118 ? 51.732  -100.971 62.601  1.00 87.99  ? 109 ALA   G N   1 
ATOM   12021 C  CA  . ALA   G  7  118 ? 51.835  -99.498  62.474  1.00 90.05  ? 109 ALA   G CA  1 
ATOM   12022 C  C   . ALA   G  7  118 ? 52.067  -99.138  61.002  1.00 87.27  ? 109 ALA   G C   1 
ATOM   12023 O  O   . ALA   G  7  118 ? 51.267  -98.353  60.455  1.00 89.17  ? 109 ALA   G O   1 
ATOM   12024 C  CB  . ALA   G  7  118 ? 52.936  -98.965  63.361  1.00 91.67  ? 109 ALA   G CB  1 
ATOM   12025 N  N   . LYS   G  7  119 ? 53.101  -99.721  60.382  1.00 86.20  ? 110 LYS   G N   1 
ATOM   12026 C  CA  . LYS   G  7  119 ? 53.478  -99.467  58.964  1.00 83.32  ? 110 LYS   G CA  1 
ATOM   12027 C  C   . LYS   G  7  119 ? 52.298  -99.800  58.044  1.00 81.56  ? 110 LYS   G C   1 
ATOM   12028 O  O   . LYS   G  7  119 ? 52.075  -99.054  57.076  1.00 77.82  ? 110 LYS   G O   1 
ATOM   12029 C  CB  . LYS   G  7  119 ? 54.697  -100.292 58.544  1.00 86.00  ? 110 LYS   G CB  1 
ATOM   12030 C  CG  . LYS   G  7  119 ? 55.224  -99.951  57.157  1.00 88.03  ? 110 LYS   G CG  1 
ATOM   12031 C  CD  . LYS   G  7  119 ? 56.140  -100.984 56.553  1.00 91.47  ? 110 LYS   G CD  1 
ATOM   12032 C  CE  . LYS   G  7  119 ? 56.436  -100.687 55.098  1.00 94.42  ? 110 LYS   G CE  1 
ATOM   12033 N  NZ  . LYS   G  7  119 ? 57.506  -101.558 54.562  1.00 97.19  ? 110 LYS   G NZ  1 
ATOM   12034 N  N   . ARG   G  7  120 ? 51.593  -100.899 58.317  1.00 81.47  ? 111 ARG   G N   1 
ATOM   12035 C  CA  . ARG   G  7  120 ? 50.441  -101.368 57.500  1.00 82.71  ? 111 ARG   G CA  1 
ATOM   12036 C  C   . ARG   G  7  120 ? 49.300  -100.347 57.606  1.00 82.67  ? 111 ARG   G C   1 
ATOM   12037 O  O   . ARG   G  7  120 ? 48.760  -99.954  56.553  1.00 82.85  ? 111 ARG   G O   1 
ATOM   12038 C  CB  . ARG   G  7  120 ? 50.009  -102.770 57.943  1.00 82.65  ? 111 ARG   G CB  1 
ATOM   12039 C  CG  . ARG   G  7  120 ? 48.715  -103.261 57.311  1.00 82.41  ? 111 ARG   G CG  1 
ATOM   12040 C  CD  . ARG   G  7  120 ? 48.742  -103.274 55.795  1.00 85.24  ? 111 ARG   G CD  1 
ATOM   12041 N  NE  . ARG   G  7  120 ? 47.501  -103.829 55.276  1.00 88.47  ? 111 ARG   G NE  1 
ATOM   12042 C  CZ  . ARG   G  7  120 ? 47.034  -103.657 54.043  1.00 91.02  ? 111 ARG   G CZ  1 
ATOM   12043 N  NH1 . ARG   G  7  120 ? 47.696  -102.922 53.163  1.00 87.43  ? 111 ARG   G NH1 1 
ATOM   12044 N  NH2 . ARG   G  7  120 ? 45.888  -104.221 53.699  1.00 98.94  ? 111 ARG   G NH2 1 
ATOM   12045 N  N   . MET   G  7  121 ? 48.952  -99.931  58.827  1.00 81.83  ? 112 MET   G N   1 
ATOM   12046 C  CA  . MET   G  7  121 ? 47.859  -98.955  59.092  1.00 80.68  ? 112 MET   G CA  1 
ATOM   12047 C  C   . MET   G  7  121 ? 48.228  -97.583  58.515  1.00 79.85  ? 112 MET   G C   1 
ATOM   12048 O  O   . MET   G  7  121 ? 47.312  -96.874  58.047  1.00 74.93  ? 112 MET   G O   1 
ATOM   12049 C  CB  . MET   G  7  121 ? 47.591  -98.828  60.594  1.00 81.56  ? 112 MET   G CB  1 
ATOM   12050 C  CG  . MET   G  7  121 ? 46.957  -100.065 61.193  1.00 82.69  ? 112 MET   G CG  1 
ATOM   12051 S  SD  . MET   G  7  121 ? 45.428  -100.530 60.345  1.00 84.65  ? 112 MET   G SD  1 
ATOM   12052 C  CE  . MET   G  7  121 ? 44.361  -99.166  60.797  1.00 83.03  ? 112 MET   G CE  1 
ATOM   12053 N  N   . ALA   G  7  122 ? 49.518  -97.229  58.555  1.00 83.33  ? 113 ALA   G N   1 
ATOM   12054 C  CA  . ALA   G  7  122 ? 50.087  -95.987  57.978  1.00 84.18  ? 113 ALA   G CA  1 
ATOM   12055 C  C   . ALA   G  7  122 ? 49.975  -96.025  56.450  1.00 82.87  ? 113 ALA   G C   1 
ATOM   12056 O  O   . ALA   G  7  122 ? 49.667  -94.978  55.860  1.00 81.31  ? 113 ALA   G O   1 
ATOM   12057 C  CB  . ALA   G  7  122 ? 51.522  -95.823  58.417  1.00 86.27  ? 113 ALA   G CB  1 
ATOM   12058 N  N   . ASN   G  7  123 ? 50.228  -97.188  55.840  1.00 85.03  ? 114 ASN   G N   1 
ATOM   12059 C  CA  . ASN   G  7  123 ? 50.139  -97.410  54.369  1.00 82.65  ? 114 ASN   G CA  1 
ATOM   12060 C  C   . ASN   G  7  123 ? 48.686  -97.225  53.911  1.00 80.86  ? 114 ASN   G C   1 
ATOM   12061 O  O   . ASN   G  7  123 ? 48.484  -96.604  52.851  1.00 74.20  ? 114 ASN   G O   1 
ATOM   12062 C  CB  . ASN   G  7  123 ? 50.668  -98.790  53.957  1.00 83.28  ? 114 ASN   G CB  1 
ATOM   12063 C  CG  . ASN   G  7  123 ? 52.168  -98.868  53.743  1.00 83.75  ? 114 ASN   G CG  1 
ATOM   12064 O  OD1 . ASN   G  7  123 ? 52.738  -99.955  53.774  1.00 91.10  ? 114 ASN   G OD1 1 
ATOM   12065 N  ND2 . ASN   G  7  123 ? 52.825  -97.751  53.487  1.00 82.58  ? 114 ASN   G ND2 1 
ATOM   12066 N  N   . LEU   G  7  124 ? 47.725  -97.768  54.668  1.00 85.16  ? 115 LEU   G N   1 
ATOM   12067 C  CA  . LEU   G  7  124 ? 46.264  -97.586  54.432  1.00 89.24  ? 115 LEU   G CA  1 
ATOM   12068 C  C   . LEU   G  7  124 ? 45.934  -96.090  54.504  1.00 91.62  ? 115 LEU   G C   1 
ATOM   12069 O  O   . LEU   G  7  124 ? 45.255  -95.592  53.583  1.00 96.50  ? 115 LEU   G O   1 
ATOM   12070 C  CB  . LEU   G  7  124 ? 45.459  -98.382  55.471  1.00 90.14  ? 115 LEU   G CB  1 
ATOM   12071 C  CG  . LEU   G  7  124 ? 44.984  -99.784  55.071  1.00 89.16  ? 115 LEU   G CG  1 
ATOM   12072 C  CD1 . LEU   G  7  124 ? 45.862  -100.418 54.001  1.00 90.91  ? 115 LEU   G CD1 1 
ATOM   12073 C  CD2 . LEU   G  7  124 ? 44.907  -100.693 56.289  1.00 87.71  ? 115 LEU   G CD2 1 
ATOM   12074 N  N   . SER   G  7  125 ? 46.401  -95.402  55.553  1.00 92.56  ? 116 SER   G N   1 
ATOM   12075 C  CA  . SER   G  7  125 ? 46.200  -93.943  55.766  1.00 89.42  ? 116 SER   G CA  1 
ATOM   12076 C  C   . SER   G  7  125 ? 46.758  -93.162  54.568  1.00 83.68  ? 116 SER   G C   1 
ATOM   12077 O  O   . SER   G  7  125 ? 46.066  -92.246  54.092  1.00 88.06  ? 116 SER   G O   1 
ATOM   12078 C  CB  . SER   G  7  125 ? 46.820  -93.481  57.063  1.00 89.88  ? 116 SER   G CB  1 
ATOM   12079 O  OG  . SER   G  7  125 ? 46.127  -94.015  58.181  1.00 95.35  ? 116 SER   G OG  1 
ATOM   12080 N  N   . GLN   G  7  126 ? 47.957  -93.526  54.099  1.00 77.69  ? 117 GLN   G N   1 
ATOM   12081 C  CA  . GLN   G  7  126 ? 48.637  -92.903  52.930  1.00 75.59  ? 117 GLN   G CA  1 
ATOM   12082 C  C   . GLN   G  7  126 ? 47.729  -92.995  51.699  1.00 75.99  ? 117 GLN   G C   1 
ATOM   12083 O  O   . GLN   G  7  126 ? 47.619  -91.992  50.984  1.00 74.56  ? 117 GLN   G O   1 
ATOM   12084 C  CB  . GLN   G  7  126 ? 49.981  -93.587  52.670  1.00 75.56  ? 117 GLN   G CB  1 
ATOM   12085 C  CG  . GLN   G  7  126 ? 50.812  -92.947  51.562  1.00 73.85  ? 117 GLN   G CG  1 
ATOM   12086 C  CD  . GLN   G  7  126 ? 50.300  -93.168  50.157  1.00 73.72  ? 117 GLN   G CD  1 
ATOM   12087 O  OE1 . GLN   G  7  126 ? 50.376  -92.277  49.315  1.00 71.29  ? 117 GLN   G OE1 1 
ATOM   12088 N  NE2 . GLN   G  7  126 ? 49.788  -94.356  49.872  1.00 73.75  ? 117 GLN   G NE2 1 
ATOM   12089 N  N   . ILE   G  7  127 ? 47.113  -94.155  51.454  1.00 79.96  ? 118 ILE   G N   1 
ATOM   12090 C  CA  . ILE   G  7  127 ? 46.239  -94.396  50.265  1.00 81.58  ? 118 ILE   G CA  1 
ATOM   12091 C  C   . ILE   G  7  127 ? 45.130  -93.338  50.239  1.00 81.12  ? 118 ILE   G C   1 
ATOM   12092 O  O   . ILE   G  7  127 ? 44.849  -92.829  49.145  1.00 84.36  ? 118 ILE   G O   1 
ATOM   12093 C  CB  . ILE   G  7  127 ? 45.670  -95.830  50.244  1.00 82.34  ? 118 ILE   G CB  1 
ATOM   12094 C  CG1 . ILE   G  7  127 ? 46.760  -96.857  49.927  1.00 83.59  ? 118 ILE   G CG1 1 
ATOM   12095 C  CG2 . ILE   G  7  127 ? 44.501  -95.935  49.273  1.00 82.87  ? 118 ILE   G CG2 1 
ATOM   12096 C  CD1 . ILE   G  7  127 ? 46.350  -98.292  50.167  1.00 85.06  ? 118 ILE   G CD1 1 
ATOM   12097 N  N   . TYR   G  7  128 ? 44.532  -93.008  51.388  1.00 80.62  ? 119 TYR   G N   1 
ATOM   12098 C  CA  . TYR   G  7  128 ? 43.397  -92.051  51.482  1.00 83.92  ? 119 TYR   G CA  1 
ATOM   12099 C  C   . TYR   G  7  128 ? 43.880  -90.630  51.132  1.00 85.77  ? 119 TYR   G C   1 
ATOM   12100 O  O   . TYR   G  7  128 ? 43.046  -89.810  50.679  1.00 85.91  ? 119 TYR   G O   1 
ATOM   12101 C  CB  . TYR   G  7  128 ? 42.728  -92.094  52.861  1.00 85.36  ? 119 TYR   G CB  1 
ATOM   12102 C  CG  . TYR   G  7  128 ? 42.468  -93.464  53.441  1.00 87.94  ? 119 TYR   G CG  1 
ATOM   12103 C  CD1 . TYR   G  7  128 ? 42.045  -94.524  52.655  1.00 89.69  ? 119 TYR   G CD1 1 
ATOM   12104 C  CD2 . TYR   G  7  128 ? 42.617  -93.692  54.800  1.00 88.82  ? 119 TYR   G CD2 1 
ATOM   12105 C  CE1 . TYR   G  7  128 ? 41.802  -95.777  53.199  1.00 93.57  ? 119 TYR   G CE1 1 
ATOM   12106 C  CE2 . TYR   G  7  128 ? 42.376  -94.935  55.361  1.00 92.12  ? 119 TYR   G CE2 1 
ATOM   12107 C  CZ  . TYR   G  7  128 ? 41.966  -95.985  54.559  1.00 94.24  ? 119 TYR   G CZ  1 
ATOM   12108 O  OH  . TYR   G  7  128 ? 41.732  -97.212  55.113  1.00 100.77 ? 119 TYR   G OH  1 
ATOM   12109 N  N   . THR   G  7  129 ? 45.177  -90.341  51.325  1.00 84.71  ? 120 THR   G N   1 
ATOM   12110 C  CA  . THR   G  7  129 ? 45.811  -89.027  51.008  1.00 83.15  ? 120 THR   G CA  1 
ATOM   12111 C  C   . THR   G  7  129 ? 46.087  -88.921  49.501  1.00 83.65  ? 120 THR   G C   1 
ATOM   12112 O  O   . THR   G  7  129 ? 46.313  -87.786  49.037  1.00 80.34  ? 120 THR   G O   1 
ATOM   12113 C  CB  . THR   G  7  129 ? 47.111  -88.777  51.789  1.00 80.12  ? 120 THR   G CB  1 
ATOM   12114 O  OG1 . THR   G  7  129 ? 48.157  -89.592  51.258  1.00 79.11  ? 120 THR   G OG1 1 
ATOM   12115 C  CG2 . THR   G  7  129 ? 46.973  -89.007  53.280  1.00 79.65  ? 120 THR   G CG2 1 
ATOM   12116 N  N   . GLN   G  7  130 ? 46.091  -90.048  48.775  1.00 82.93  ? 121 GLN   G N   1 
ATOM   12117 C  CA  . GLN   G  7  130 ? 46.395  -90.109  47.316  1.00 83.38  ? 121 GLN   G CA  1 
ATOM   12118 C  C   . GLN   G  7  130 ? 45.131  -90.441  46.509  1.00 85.42  ? 121 GLN   G C   1 
ATOM   12119 O  O   . GLN   G  7  130 ? 44.983  -89.878  45.407  1.00 85.13  ? 121 GLN   G O   1 
ATOM   12120 C  CB  . GLN   G  7  130 ? 47.501  -91.128  47.040  1.00 82.61  ? 121 GLN   G CB  1 
ATOM   12121 C  CG  . GLN   G  7  130 ? 48.005  -91.099  45.601  1.00 82.64  ? 121 GLN   G CG  1 
ATOM   12122 C  CD  . GLN   G  7  130 ? 49.402  -91.647  45.418  1.00 83.69  ? 121 GLN   G CD  1 
ATOM   12123 O  OE1 . GLN   G  7  130 ? 50.108  -91.276  44.481  1.00 78.10  ? 121 GLN   G OE1 1 
ATOM   12124 N  NE2 . GLN   G  7  130 ? 49.816  -92.544  46.304  1.00 85.76  ? 121 GLN   G NE2 1 
ATOM   12125 N  N   . ARG   G  7  131 ? 44.266  -91.324  47.020  1.00 89.36  ? 122 ARG   G N   1 
ATOM   12126 C  CA  . ARG   G  7  131 ? 42.985  -91.711  46.364  1.00 96.92  ? 122 ARG   G CA  1 
ATOM   12127 C  C   . ARG   G  7  131 ? 41.909  -90.697  46.773  1.00 94.67  ? 122 ARG   G C   1 
ATOM   12128 O  O   . ARG   G  7  131 ? 41.886  -90.306  47.956  1.00 95.92  ? 122 ARG   G O   1 
ATOM   12129 C  CB  . ARG   G  7  131 ? 42.586  -93.147  46.732  1.00 105.17 ? 122 ARG   G CB  1 
ATOM   12130 C  CG  . ARG   G  7  131 ? 42.063  -93.970  45.561  1.00 110.78 ? 122 ARG   G CG  1 
ATOM   12131 C  CD  . ARG   G  7  131 ? 43.111  -94.896  44.963  1.00 118.75 ? 122 ARG   G CD  1 
ATOM   12132 N  NE  . ARG   G  7  131 ? 43.166  -96.184  45.646  1.00 124.89 ? 122 ARG   G NE  1 
ATOM   12133 C  CZ  . ARG   G  7  131 ? 44.130  -97.095  45.500  1.00 128.43 ? 122 ARG   G CZ  1 
ATOM   12134 N  NH1 . ARG   G  7  131 ? 45.153  -96.874  44.690  1.00 138.31 ? 122 ARG   G NH1 1 
ATOM   12135 N  NH2 . ARG   G  7  131 ? 44.069  -98.230  46.175  1.00 128.91 ? 122 ARG   G NH2 1 
ATOM   12136 N  N   . ALA   G  7  132 ? 41.054  -90.294  45.829  1.00 94.72  ? 123 ALA   G N   1 
ATOM   12137 C  CA  . ALA   G  7  132 ? 40.127  -89.145  45.965  1.00 94.49  ? 123 ALA   G CA  1 
ATOM   12138 C  C   . ALA   G  7  132 ? 38.812  -89.561  46.635  1.00 96.94  ? 123 ALA   G C   1 
ATOM   12139 O  O   . ALA   G  7  132 ? 38.277  -88.739  47.403  1.00 98.32  ? 123 ALA   G O   1 
ATOM   12140 C  CB  . ALA   G  7  132 ? 39.870  -88.530  44.614  1.00 95.49  ? 123 ALA   G CB  1 
ATOM   12141 N  N   . TYR   G  7  133 ? 38.299  -90.765  46.348  1.00 99.69  ? 124 TYR   G N   1 
ATOM   12142 C  CA  . TYR   G  7  133 ? 36.947  -91.218  46.781  1.00 100.83 ? 124 TYR   G CA  1 
ATOM   12143 C  C   . TYR   G  7  133 ? 36.944  -91.474  48.293  1.00 95.02  ? 124 TYR   G C   1 
ATOM   12144 O  O   . TYR   G  7  133 ? 35.858  -91.381  48.898  1.00 93.52  ? 124 TYR   G O   1 
ATOM   12145 C  CB  . TYR   G  7  133 ? 36.467  -92.422  45.958  1.00 102.39 ? 124 TYR   G CB  1 
ATOM   12146 C  CG  . TYR   G  7  133 ? 36.884  -93.796  46.430  1.00 106.10 ? 124 TYR   G CG  1 
ATOM   12147 C  CD1 . TYR   G  7  133 ? 38.175  -94.263  46.235  1.00 108.96 ? 124 TYR   G CD1 1 
ATOM   12148 C  CD2 . TYR   G  7  133 ? 35.969  -94.659  47.017  1.00 106.83 ? 124 TYR   G CD2 1 
ATOM   12149 C  CE1 . TYR   G  7  133 ? 38.557  -95.533  46.642  1.00 112.92 ? 124 TYR   G CE1 1 
ATOM   12150 C  CE2 . TYR   G  7  133 ? 36.334  -95.933  47.427  1.00 111.64 ? 124 TYR   G CE2 1 
ATOM   12151 C  CZ  . TYR   G  7  133 ? 37.634  -96.370  47.241  1.00 112.55 ? 124 TYR   G CZ  1 
ATOM   12152 O  OH  . TYR   G  7  133 ? 38.012  -97.619  47.640  1.00 118.09 ? 124 TYR   G OH  1 
ATOM   12153 N  N   . MET   G  7  134 ? 38.116  -91.747  48.876  1.00 95.84  ? 125 MET   G N   1 
ATOM   12154 C  CA  . MET   G  7  134 ? 38.295  -92.060  50.320  1.00 99.18  ? 125 MET   G CA  1 
ATOM   12155 C  C   . MET   G  7  134 ? 38.809  -90.809  51.047  1.00 92.86  ? 125 MET   G C   1 
ATOM   12156 O  O   . MET   G  7  134 ? 39.811  -90.226  50.582  1.00 93.21  ? 125 MET   G O   1 
ATOM   12157 C  CB  . MET   G  7  134 ? 39.284  -93.220  50.492  1.00 104.10 ? 125 MET   G CB  1 
ATOM   12158 C  CG  . MET   G  7  134 ? 38.749  -94.556  49.988  1.00 108.37 ? 125 MET   G CG  1 
ATOM   12159 S  SD  . MET   G  7  134 ? 38.411  -95.751  51.307  1.00 113.60 ? 125 MET   G SD  1 
ATOM   12160 C  CE  . MET   G  7  134 ? 37.353  -94.795  52.396  1.00 120.74 ? 125 MET   G CE  1 
ATOM   12161 N  N   . ARG   G  7  135 ? 38.127  -90.394  52.121  1.00 90.37  ? 126 ARG   G N   1 
ATOM   12162 C  CA  . ARG   G  7  135 ? 38.608  -89.336  53.049  1.00 88.58  ? 126 ARG   G CA  1 
ATOM   12163 C  C   . ARG   G  7  135 ? 39.625  -89.954  54.004  1.00 90.08  ? 126 ARG   G C   1 
ATOM   12164 O  O   . ARG   G  7  135 ? 39.555  -91.148  54.291  1.00 91.93  ? 126 ARG   G O   1 
ATOM   12165 C  CB  . ARG   G  7  135 ? 37.450  -88.681  53.814  1.00 88.14  ? 126 ARG   G CB  1 
ATOM   12166 C  CG  . ARG   G  7  135 ? 36.788  -89.534  54.889  1.00 86.60  ? 126 ARG   G CG  1 
ATOM   12167 C  CD  . ARG   G  7  135 ? 35.937  -88.671  55.805  1.00 87.73  ? 126 ARG   G CD  1 
ATOM   12168 N  NE  . ARG   G  7  135 ? 35.151  -89.417  56.783  1.00 88.43  ? 126 ARG   G NE  1 
ATOM   12169 C  CZ  . ARG   G  7  135 ? 35.564  -89.786  57.997  1.00 87.83  ? 126 ARG   G CZ  1 
ATOM   12170 N  NH1 . ARG   G  7  135 ? 36.788  -89.500  58.414  1.00 87.72  ? 126 ARG   G NH1 1 
ATOM   12171 N  NH2 . ARG   G  7  135 ? 34.742  -90.452  58.791  1.00 87.12  ? 126 ARG   G NH2 1 
ATOM   12172 N  N   . PRO   G  7  136 ? 40.611  -89.180  54.514  1.00 88.63  ? 127 PRO   G N   1 
ATOM   12173 C  CA  . PRO   G  7  136 ? 41.432  -89.635  55.634  1.00 85.94  ? 127 PRO   G CA  1 
ATOM   12174 C  C   . PRO   G  7  136 ? 40.543  -89.840  56.869  1.00 82.17  ? 127 PRO   G C   1 
ATOM   12175 O  O   . PRO   G  7  136 ? 39.489  -89.235  56.931  1.00 85.21  ? 127 PRO   G O   1 
ATOM   12176 C  CB  . PRO   G  7  136 ? 42.438  -88.497  55.870  1.00 87.03  ? 127 PRO   G CB  1 
ATOM   12177 C  CG  . PRO   G  7  136 ? 42.401  -87.672  54.596  1.00 88.74  ? 127 PRO   G CG  1 
ATOM   12178 C  CD  . PRO   G  7  136 ? 41.002  -87.844  54.040  1.00 87.84  ? 127 PRO   G CD  1 
ATOM   12179 N  N   . LEU   G  7  137 ? 40.962  -90.700  57.797  1.00 84.63  ? 128 LEU   G N   1 
ATOM   12180 C  CA  . LEU   G  7  137 ? 40.330  -90.808  59.137  1.00 87.11  ? 128 LEU   G CA  1 
ATOM   12181 C  C   . LEU   G  7  137 ? 40.915  -89.694  60.008  1.00 85.56  ? 128 LEU   G C   1 
ATOM   12182 O  O   . LEU   G  7  137 ? 42.149  -89.519  59.981  1.00 89.04  ? 128 LEU   G O   1 
ATOM   12183 C  CB  . LEU   G  7  137 ? 40.599  -92.191  59.741  1.00 88.86  ? 128 LEU   G CB  1 
ATOM   12184 C  CG  . LEU   G  7  137 ? 40.115  -93.389  58.926  1.00 90.10  ? 128 LEU   G CG  1 
ATOM   12185 C  CD1 . LEU   G  7  137 ? 40.563  -94.687  59.583  1.00 92.31  ? 128 LEU   G CD1 1 
ATOM   12186 C  CD2 . LEU   G  7  137 ? 38.601  -93.375  58.757  1.00 89.81  ? 128 LEU   G CD2 1 
ATOM   12187 N  N   . GLY   G  7  138 ? 40.063  -88.952  60.719  1.00 85.28  ? 129 GLY   G N   1 
ATOM   12188 C  CA  . GLY   G  7  138 ? 40.484  -87.872  61.632  1.00 86.38  ? 129 GLY   G CA  1 
ATOM   12189 C  C   . GLY   G  7  138 ? 40.978  -88.432  62.954  1.00 83.58  ? 129 GLY   G C   1 
ATOM   12190 O  O   . GLY   G  7  138 ? 40.363  -88.125  63.987  1.00 81.89  ? 129 GLY   G O   1 
ATOM   12191 N  N   . VAL   G  7  139 ? 42.043  -89.238  62.925  1.00 84.72  ? 130 VAL   G N   1 
ATOM   12192 C  CA  . VAL   G  7  139 ? 42.553  -89.981  64.115  1.00 86.77  ? 130 VAL   G CA  1 
ATOM   12193 C  C   . VAL   G  7  139 ? 44.079  -90.067  64.056  1.00 86.54  ? 130 VAL   G C   1 
ATOM   12194 O  O   . VAL   G  7  139 ? 44.636  -90.123  62.940  1.00 83.99  ? 130 VAL   G O   1 
ATOM   12195 C  CB  . VAL   G  7  139 ? 41.938  -91.390  64.217  1.00 88.33  ? 130 VAL   G CB  1 
ATOM   12196 C  CG1 . VAL   G  7  139 ? 40.454  -91.337  64.544  1.00 91.24  ? 130 VAL   G CG1 1 
ATOM   12197 C  CG2 . VAL   G  7  139 ? 42.186  -92.217  62.963  1.00 88.53  ? 130 VAL   G CG2 1 
ATOM   12198 N  N   . ILE   G  7  140 ? 44.707  -90.081  65.234  1.00 87.77  ? 131 ILE   G N   1 
ATOM   12199 C  CA  . ILE   G  7  140 ? 46.139  -90.442  65.446  1.00 88.39  ? 131 ILE   G CA  1 
ATOM   12200 C  C   . ILE   G  7  140 ? 46.165  -91.724  66.290  1.00 88.91  ? 131 ILE   G C   1 
ATOM   12201 O  O   . ILE   G  7  140 ? 45.624  -91.715  67.417  1.00 85.40  ? 131 ILE   G O   1 
ATOM   12202 C  CB  . ILE   G  7  140 ? 46.914  -89.270  66.086  1.00 88.93  ? 131 ILE   G CB  1 
ATOM   12203 C  CG1 . ILE   G  7  140 ? 47.109  -88.128  65.083  1.00 88.24  ? 131 ILE   G CG1 1 
ATOM   12204 C  CG2 . ILE   G  7  140 ? 48.242  -89.737  66.670  1.00 89.86  ? 131 ILE   G CG2 1 
ATOM   12205 C  CD1 . ILE   G  7  140 ? 47.684  -86.861  65.676  1.00 88.50  ? 131 ILE   G CD1 1 
ATOM   12206 N  N   . LEU   G  7  141 ? 46.750  -92.793  65.748  1.00 88.03  ? 132 LEU   G N   1 
ATOM   12207 C  CA  . LEU   G  7  141 ? 46.786  -94.134  66.386  1.00 88.72  ? 132 LEU   G CA  1 
ATOM   12208 C  C   . LEU   G  7  141 ? 48.158  -94.343  67.031  1.00 90.23  ? 132 LEU   G C   1 
ATOM   12209 O  O   . LEU   G  7  141 ? 49.166  -94.283  66.298  1.00 91.53  ? 132 LEU   G O   1 
ATOM   12210 C  CB  . LEU   G  7  141 ? 46.513  -95.206  65.328  1.00 85.60  ? 132 LEU   G CB  1 
ATOM   12211 C  CG  . LEU   G  7  141 ? 45.330  -94.937  64.403  1.00 84.57  ? 132 LEU   G CG  1 
ATOM   12212 C  CD1 . LEU   G  7  141 ? 45.243  -96.011  63.334  1.00 85.48  ? 132 LEU   G CD1 1 
ATOM   12213 C  CD2 . LEU   G  7  141 ? 44.030  -94.854  65.189  1.00 85.97  ? 132 LEU   G CD2 1 
ATOM   12214 N  N   . THR   G  7  142 ? 48.187  -94.574  68.346  1.00 91.53  ? 133 THR   G N   1 
ATOM   12215 C  CA  . THR   G  7  142 ? 49.407  -94.957  69.100  1.00 94.33  ? 133 THR   G CA  1 
ATOM   12216 C  C   . THR   G  7  142 ? 49.343  -96.454  69.404  1.00 91.24  ? 133 THR   G C   1 
ATOM   12217 O  O   . THR   G  7  142 ? 48.442  -96.852  70.165  1.00 98.96  ? 133 THR   G O   1 
ATOM   12218 C  CB  . THR   G  7  142 ? 49.557  -94.158  70.397  1.00 96.46  ? 133 THR   G CB  1 
ATOM   12219 O  OG1 . THR   G  7  142 ? 49.188  -92.800  70.148  1.00 101.40 ? 133 THR   G OG1 1 
ATOM   12220 C  CG2 . THR   G  7  142 ? 50.966  -94.240  70.942  1.00 96.18  ? 133 THR   G CG2 1 
ATOM   12221 N  N   . PHE   G  7  143 ? 50.255  -97.239  68.823  1.00 90.01  ? 134 PHE   G N   1 
ATOM   12222 C  CA  . PHE   G  7  143 ? 50.367  -98.707  69.022  1.00 87.68  ? 134 PHE   G CA  1 
ATOM   12223 C  C   . PHE   G  7  143 ? 51.450  -98.988  70.065  1.00 88.04  ? 134 PHE   G C   1 
ATOM   12224 O  O   . PHE   G  7  143 ? 52.532  -98.375  69.976  1.00 91.44  ? 134 PHE   G O   1 
ATOM   12225 C  CB  . PHE   G  7  143 ? 50.673  -99.407  67.697  1.00 84.19  ? 134 PHE   G CB  1 
ATOM   12226 C  CG  . PHE   G  7  143 ? 49.579  -99.283  66.668  1.00 80.97  ? 134 PHE   G CG  1 
ATOM   12227 C  CD1 . PHE   G  7  143 ? 48.481  -100.129 66.695  1.00 80.05  ? 134 PHE   G CD1 1 
ATOM   12228 C  CD2 . PHE   G  7  143 ? 49.645  -98.317  65.677  1.00 77.85  ? 134 PHE   G CD2 1 
ATOM   12229 C  CE1 . PHE   G  7  143 ? 47.471  -100.010 65.754  1.00 77.80  ? 134 PHE   G CE1 1 
ATOM   12230 C  CE2 . PHE   G  7  143 ? 48.635  -98.202  64.736  1.00 77.85  ? 134 PHE   G CE2 1 
ATOM   12231 C  CZ  . PHE   G  7  143 ? 47.550  -99.047  64.777  1.00 77.29  ? 134 PHE   G CZ  1 
ATOM   12232 N  N   . VAL   G  7  144 ? 51.158  -99.882  71.016  1.00 90.25  ? 135 VAL   G N   1 
ATOM   12233 C  CA  . VAL   G  7  144 ? 52.077  -100.261 72.131  1.00 91.61  ? 135 VAL   G CA  1 
ATOM   12234 C  C   . VAL   G  7  144 ? 52.131  -101.787 72.249  1.00 92.42  ? 135 VAL   G C   1 
ATOM   12235 O  O   . VAL   G  7  144 ? 51.096  -102.445 72.020  1.00 94.37  ? 135 VAL   G O   1 
ATOM   12236 C  CB  . VAL   G  7  144 ? 51.655  -99.613  73.462  1.00 90.99  ? 135 VAL   G CB  1 
ATOM   12237 C  CG1 . VAL   G  7  144 ? 51.857  -98.106  73.428  1.00 92.01  ? 135 VAL   G CG1 1 
ATOM   12238 C  CG2 . VAL   G  7  144 ? 50.223  -99.959  73.844  1.00 87.38  ? 135 VAL   G CG2 1 
ATOM   12239 N  N   . SER   G  7  145 ? 53.305  -102.316 72.599  1.00 94.80  ? 136 SER   G N   1 
ATOM   12240 C  CA  . SER   G  7  145 ? 53.556  -103.761 72.835  1.00 93.26  ? 136 SER   G CA  1 
ATOM   12241 C  C   . SER   G  7  145 ? 54.887  -103.946 73.567  1.00 91.41  ? 136 SER   G C   1 
ATOM   12242 O  O   . SER   G  7  145 ? 55.595  -102.942 73.798  1.00 88.85  ? 136 SER   G O   1 
ATOM   12243 C  CB  . SER   G  7  145 ? 53.543  -104.537 71.540  1.00 93.33  ? 136 SER   G CB  1 
ATOM   12244 O  OG  . SER   G  7  145 ? 54.798  -104.458 70.879  1.00 95.92  ? 136 SER   G OG  1 
ATOM   12245 N  N   . VAL   G  7  146 ? 55.192  -105.196 73.921  1.00 90.60  ? 137 VAL   G N   1 
ATOM   12246 C  CA  . VAL   G  7  146 ? 56.563  -105.675 74.261  1.00 86.21  ? 137 VAL   G CA  1 
ATOM   12247 C  C   . VAL   G  7  146 ? 56.932  -106.708 73.191  1.00 85.04  ? 137 VAL   G C   1 
ATOM   12248 O  O   . VAL   G  7  146 ? 56.660  -107.905 73.393  1.00 81.20  ? 137 VAL   G O   1 
ATOM   12249 C  CB  . VAL   G  7  146 ? 56.636  -106.235 75.694  1.00 83.57  ? 137 VAL   G CB  1 
ATOM   12250 C  CG1 . VAL   G  7  146 ? 58.040  -106.696 76.056  1.00 82.98  ? 137 VAL   G CG1 1 
ATOM   12251 C  CG2 . VAL   G  7  146 ? 56.134  -105.221 76.709  1.00 83.56  ? 137 VAL   G CG2 1 
ATOM   12252 N  N   . ASP   G  7  147 ? 57.475  -106.234 72.068  1.00 87.63  ? 138 ASP   G N   1 
ATOM   12253 C  CA  . ASP   G  7  147 ? 57.815  -107.062 70.881  1.00 91.91  ? 138 ASP   G CA  1 
ATOM   12254 C  C   . ASP   G  7  147 ? 58.841  -108.118 71.299  1.00 94.89  ? 138 ASP   G C   1 
ATOM   12255 O  O   . ASP   G  7  147 ? 59.759  -107.775 72.065  1.00 94.69  ? 138 ASP   G O   1 
ATOM   12256 C  CB  . ASP   G  7  147 ? 58.355  -106.206 69.733  1.00 95.58  ? 138 ASP   G CB  1 
ATOM   12257 C  CG  . ASP   G  7  147 ? 58.407  -106.953 68.411  1.00 96.55  ? 138 ASP   G CG  1 
ATOM   12258 O  OD1 . ASP   G  7  147 ? 57.328  -107.335 67.916  1.00 96.61  ? 138 ASP   G OD1 1 
ATOM   12259 O  OD2 . ASP   G  7  147 ? 59.526  -107.164 67.898  1.00 100.18 ? 138 ASP   G OD2 1 
ATOM   12260 N  N   . GLU   G  7  148 ? 58.693  -109.349 70.802  1.00 99.12  ? 139 GLU   G N   1 
ATOM   12261 C  CA  . GLU   G  7  148 ? 59.560  -110.496 71.187  1.00 103.99 ? 139 GLU   G CA  1 
ATOM   12262 C  C   . GLU   G  7  148 ? 60.981  -110.286 70.641  1.00 106.37 ? 139 GLU   G C   1 
ATOM   12263 O  O   . GLU   G  7  148 ? 61.899  -110.955 71.159  1.00 109.04 ? 139 GLU   G O   1 
ATOM   12264 C  CB  . GLU   G  7  148 ? 58.944  -111.830 70.747  1.00 107.15 ? 139 GLU   G CB  1 
ATOM   12265 C  CG  . GLU   G  7  148 ? 58.820  -112.023 69.242  1.00 107.39 ? 139 GLU   G CG  1 
ATOM   12266 C  CD  . GLU   G  7  148 ? 58.301  -113.396 68.837  1.00 105.67 ? 139 GLU   G CD  1 
ATOM   12267 O  OE1 . GLU   G  7  148 ? 57.487  -113.474 67.893  1.00 101.99 ? 139 GLU   G OE1 1 
ATOM   12268 O  OE2 . GLU   G  7  148 ? 58.716  -114.391 69.463  1.00 108.81 ? 139 GLU   G OE2 1 
ATOM   12269 N  N   . GLU   G  7  149 ? 61.164  -109.392 69.659  1.00 103.82 ? 140 GLU   G N   1 
ATOM   12270 C  CA  . GLU   G  7  149 ? 62.491  -109.061 69.068  1.00 102.82 ? 140 GLU   G CA  1 
ATOM   12271 C  C   . GLU   G  7  149 ? 62.977  -107.693 69.560  1.00 100.16 ? 140 GLU   G C   1 
ATOM   12272 O  O   . GLU   G  7  149 ? 64.109  -107.632 70.065  1.00 106.57 ? 140 GLU   G O   1 
ATOM   12273 C  CB  . GLU   G  7  149 ? 62.438  -109.083 67.539  1.00 105.00 ? 140 GLU   G CB  1 
ATOM   12274 C  CG  . GLU   G  7  149 ? 62.379  -110.482 66.955  1.00 106.94 ? 140 GLU   G CG  1 
ATOM   12275 C  CD  . GLU   G  7  149 ? 62.639  -110.541 65.460  1.00 106.52 ? 140 GLU   G CD  1 
ATOM   12276 O  OE1 . GLU   G  7  149 ? 63.710  -110.065 65.028  1.00 103.91 ? 140 GLU   G OE1 1 
ATOM   12277 O  OE2 . GLU   G  7  149 ? 61.769  -111.056 64.732  1.00 110.34 ? 140 GLU   G OE2 1 
ATOM   12278 N  N   . LEU   G  7  150 ? 62.171  -106.637 69.405  1.00 97.92  ? 141 LEU   G N   1 
ATOM   12279 C  CA  . LEU   G  7  150 ? 62.595  -105.230 69.663  1.00 99.64  ? 141 LEU   G CA  1 
ATOM   12280 C  C   . LEU   G  7  150 ? 62.372  -104.836 71.130  1.00 95.62  ? 141 LEU   G C   1 
ATOM   12281 O  O   . LEU   G  7  150 ? 62.995  -103.848 71.556  1.00 96.35  ? 141 LEU   G O   1 
ATOM   12282 C  CB  . LEU   G  7  150 ? 61.827  -104.280 68.738  1.00 98.40  ? 141 LEU   G CB  1 
ATOM   12283 C  CG  . LEU   G  7  150 ? 62.104  -104.413 67.241  1.00 101.57 ? 141 LEU   G CG  1 
ATOM   12284 C  CD1 . LEU   G  7  150 ? 61.298  -103.383 66.461  1.00 100.27 ? 141 LEU   G CD1 1 
ATOM   12285 C  CD2 . LEU   G  7  150 ? 63.589  -104.271 66.926  1.00 101.57 ? 141 LEU   G CD2 1 
ATOM   12286 N  N   . GLY   G  7  151 ? 61.516  -105.551 71.867  1.00 94.08  ? 142 GLY   G N   1 
ATOM   12287 C  CA  . GLY   G  7  151 ? 61.209  -105.250 73.280  1.00 93.04  ? 142 GLY   G CA  1 
ATOM   12288 C  C   . GLY   G  7  151 ? 60.122  -104.185 73.402  1.00 92.60  ? 142 GLY   G C   1 
ATOM   12289 O  O   . GLY   G  7  151 ? 59.325  -104.018 72.480  1.00 90.02  ? 142 GLY   G O   1 
ATOM   12290 N  N   . PRO   G  7  152 ? 60.055  -103.431 74.528  1.00 91.40  ? 143 PRO   G N   1 
ATOM   12291 C  CA  . PRO   G  7  152 ? 59.043  -102.388 74.704  1.00 90.71  ? 143 PRO   G CA  1 
ATOM   12292 C  C   . PRO   G  7  152 ? 59.040  -101.432 73.503  1.00 91.68  ? 143 PRO   G C   1 
ATOM   12293 O  O   . PRO   G  7  152 ? 60.098  -100.923 73.169  1.00 92.02  ? 143 PRO   G O   1 
ATOM   12294 C  CB  . PRO   G  7  152 ? 59.473  -101.670 75.991  1.00 90.33  ? 143 PRO   G CB  1 
ATOM   12295 C  CG  . PRO   G  7  152 ? 60.248  -102.717 76.756  1.00 91.52  ? 143 PRO   G CG  1 
ATOM   12296 C  CD  . PRO   G  7  152 ? 60.951  -103.531 75.689  1.00 92.21  ? 143 PRO   G CD  1 
ATOM   12297 N  N   . SER   G  7  153 ? 57.873  -101.236 72.880  1.00 91.39  ? 144 SER   G N   1 
ATOM   12298 C  CA  . SER   G  7  153 ? 57.718  -100.526 71.583  1.00 91.54  ? 144 SER   G CA  1 
ATOM   12299 C  C   . SER   G  7  153 ? 56.533  -99.558  71.629  1.00 86.68  ? 144 SER   G C   1 
ATOM   12300 O  O   . SER   G  7  153 ? 55.435  -99.982  72.033  1.00 85.01  ? 144 SER   G O   1 
ATOM   12301 C  CB  . SER   G  7  153 ? 57.561  -101.510 70.453  1.00 90.81  ? 144 SER   G CB  1 
ATOM   12302 O  OG  . SER   G  7  153 ? 58.706  -102.339 70.334  1.00 95.64  ? 144 SER   G OG  1 
ATOM   12303 N  N   . ILE   G  7  154 ? 56.763  -98.308  71.219  1.00 85.30  ? 145 ILE   G N   1 
ATOM   12304 C  CA  . ILE   G  7  154 ? 55.700  -97.303  70.921  1.00 83.81  ? 145 ILE   G CA  1 
ATOM   12305 C  C   . ILE   G  7  154 ? 55.879  -96.856  69.468  1.00 82.88  ? 145 ILE   G C   1 
ATOM   12306 O  O   . ILE   G  7  154 ? 56.972  -96.364  69.139  1.00 81.74  ? 145 ILE   G O   1 
ATOM   12307 C  CB  . ILE   G  7  154 ? 55.751  -96.100  71.883  1.00 83.47  ? 145 ILE   G CB  1 
ATOM   12308 C  CG1 . ILE   G  7  154 ? 55.824  -96.531  73.350  1.00 84.66  ? 145 ILE   G CG1 1 
ATOM   12309 C  CG2 . ILE   G  7  154 ? 54.569  -95.177  71.632  1.00 83.06  ? 145 ILE   G CG2 1 
ATOM   12310 C  CD1 . ILE   G  7  154 ? 56.312  -95.446  74.275  1.00 85.71  ? 145 ILE   G CD1 1 
ATOM   12311 N  N   . TYR   G  7  155 ? 54.847  -97.048  68.644  1.00 83.79  ? 146 TYR   G N   1 
ATOM   12312 C  CA  . TYR   G  7  155 ? 54.786  -96.618  67.223  1.00 85.26  ? 146 TYR   G CA  1 
ATOM   12313 C  C   . TYR   G  7  155 ? 53.466  -95.868  67.023  1.00 86.36  ? 146 TYR   G C   1 
ATOM   12314 O  O   . TYR   G  7  155 ? 52.436  -96.336  67.551  1.00 87.86  ? 146 TYR   G O   1 
ATOM   12315 C  CB  . TYR   G  7  155 ? 54.966  -97.828  66.298  1.00 84.33  ? 146 TYR   G CB  1 
ATOM   12316 C  CG  . TYR   G  7  155 ? 56.384  -98.340  66.227  1.00 86.30  ? 146 TYR   G CG  1 
ATOM   12317 C  CD1 . TYR   G  7  155 ? 56.919  -99.121  67.241  1.00 85.06  ? 146 TYR   G CD1 1 
ATOM   12318 C  CD2 . TYR   G  7  155 ? 57.207  -98.023  65.157  1.00 87.88  ? 146 TYR   G CD2 1 
ATOM   12319 C  CE1 . TYR   G  7  155 ? 58.227  -99.578  67.190  1.00 87.17  ? 146 TYR   G CE1 1 
ATOM   12320 C  CE2 . TYR   G  7  155 ? 58.516  -98.474  65.089  1.00 88.60  ? 146 TYR   G CE2 1 
ATOM   12321 C  CZ  . TYR   G  7  155 ? 59.030  -99.254  66.110  1.00 87.51  ? 146 TYR   G CZ  1 
ATOM   12322 O  OH  . TYR   G  7  155 ? 60.315  -99.707  66.040  1.00 90.87  ? 146 TYR   G OH  1 
ATOM   12323 N  N   . LYS   G  7  156 ? 53.505  -94.729  66.322  1.00 86.87  ? 147 LYS   G N   1 
ATOM   12324 C  CA  . LYS   G  7  156 ? 52.346  -93.805  66.182  1.00 89.19  ? 147 LYS   G CA  1 
ATOM   12325 C  C   . LYS   G  7  156 ? 52.083  -93.484  64.705  1.00 87.80  ? 147 LYS   G C   1 
ATOM   12326 O  O   . LYS   G  7  156 ? 53.058  -93.273  63.956  1.00 86.27  ? 147 LYS   G O   1 
ATOM   12327 C  CB  . LYS   G  7  156 ? 52.589  -92.521  66.977  1.00 89.95  ? 147 LYS   G CB  1 
ATOM   12328 C  CG  . LYS   G  7  156 ? 51.344  -91.678  67.215  1.00 90.97  ? 147 LYS   G CG  1 
ATOM   12329 C  CD  . LYS   G  7  156 ? 51.469  -90.716  68.375  1.00 92.07  ? 147 LYS   G CD  1 
ATOM   12330 C  CE  . LYS   G  7  156 ? 52.214  -89.450  68.017  1.00 93.27  ? 147 LYS   G CE  1 
ATOM   12331 N  NZ  . LYS   G  7  156 ? 52.182  -88.477  69.132  1.00 95.77  ? 147 LYS   G NZ  1 
ATOM   12332 N  N   . THR   G  7  157 ? 50.799  -93.428  64.334  1.00 87.33  ? 148 THR   G N   1 
ATOM   12333 C  CA  . THR   G  7  157 ? 50.280  -93.175  62.962  1.00 89.16  ? 148 THR   G CA  1 
ATOM   12334 C  C   . THR   G  7  157 ? 49.422  -91.905  62.973  1.00 87.12  ? 148 THR   G C   1 
ATOM   12335 O  O   . THR   G  7  157 ? 48.787  -91.647  64.010  1.00 86.04  ? 148 THR   G O   1 
ATOM   12336 C  CB  . THR   G  7  157 ? 49.452  -94.369  62.471  1.00 89.12  ? 148 THR   G CB  1 
ATOM   12337 O  OG1 . THR   G  7  157 ? 50.335  -95.476  62.292  1.00 87.76  ? 148 THR   G OG1 1 
ATOM   12338 C  CG2 . THR   G  7  157 ? 48.711  -94.094  61.180  1.00 90.50  ? 148 THR   G CG2 1 
ATOM   12339 N  N   . ASP   G  7  158 ? 49.385  -91.166  61.858  1.00 89.99  ? 149 ASP   G N   1 
ATOM   12340 C  CA  . ASP   G  7  158 ? 48.578  -89.921  61.697  1.00 93.90  ? 149 ASP   G CA  1 
ATOM   12341 C  C   . ASP   G  7  158 ? 47.859  -89.946  60.348  1.00 91.36  ? 149 ASP   G C   1 
ATOM   12342 O  O   . ASP   G  7  158 ? 48.113  -90.827  59.529  1.00 97.09  ? 149 ASP   G O   1 
ATOM   12343 C  CB  . ASP   G  7  158 ? 49.449  -88.672  61.884  1.00 97.71  ? 149 ASP   G CB  1 
ATOM   12344 C  CG  . ASP   G  7  158 ? 50.647  -88.570  60.953  1.00 102.68 ? 149 ASP   G CG  1 
ATOM   12345 O  OD1 . ASP   G  7  158 ? 50.578  -89.123  59.833  1.00 101.74 ? 149 ASP   G OD1 1 
ATOM   12346 O  OD2 . ASP   G  7  158 ? 51.639  -87.921  61.353  1.00 106.81 ? 149 ASP   G OD2 1 
ATOM   12347 N  N   . PRO   G  7  159 ? 46.919  -89.005  60.082  1.00 85.65  ? 150 PRO   G N   1 
ATOM   12348 C  CA  . PRO   G  7  159 ? 46.194  -88.963  58.807  1.00 84.05  ? 150 PRO   G CA  1 
ATOM   12349 C  C   . PRO   G  7  159 ? 47.045  -88.743  57.543  1.00 85.46  ? 150 PRO   G C   1 
ATOM   12350 O  O   . PRO   G  7  159 ? 46.547  -89.043  56.465  1.00 82.53  ? 150 PRO   G O   1 
ATOM   12351 C  CB  . PRO   G  7  159 ? 45.222  -87.783  58.985  1.00 81.01  ? 150 PRO   G CB  1 
ATOM   12352 C  CG  . PRO   G  7  159 ? 45.052  -87.670  60.480  1.00 80.98  ? 150 PRO   G CG  1 
ATOM   12353 C  CD  . PRO   G  7  159 ? 46.427  -87.988  61.026  1.00 83.61  ? 150 PRO   G CD  1 
ATOM   12354 N  N   . ALA   G  7  160 ? 48.282  -88.250  57.686  1.00 84.52  ? 151 ALA   G N   1 
ATOM   12355 C  CA  . ALA   G  7  160 ? 49.239  -88.033  56.571  1.00 85.53  ? 151 ALA   G CA  1 
ATOM   12356 C  C   . ALA   G  7  160 ? 49.804  -89.373  56.082  1.00 86.29  ? 151 ALA   G C   1 
ATOM   12357 O  O   . ALA   G  7  160 ? 50.297  -89.421  54.936  1.00 83.97  ? 151 ALA   G O   1 
ATOM   12358 C  CB  . ALA   G  7  160 ? 50.349  -87.106  57.003  1.00 85.41  ? 151 ALA   G CB  1 
ATOM   12359 N  N   . GLY   G  7  161 ? 49.738  -90.412  56.921  1.00 86.45  ? 152 GLY   G N   1 
ATOM   12360 C  CA  . GLY   G  7  161 ? 50.329  -91.737  56.659  1.00 88.61  ? 152 GLY   G CA  1 
ATOM   12361 C  C   . GLY   G  7  161 ? 51.750  -91.824  57.184  1.00 91.97  ? 152 GLY   G C   1 
ATOM   12362 O  O   . GLY   G  7  161 ? 52.437  -92.795  56.842  1.00 95.80  ? 152 GLY   G O   1 
ATOM   12363 N  N   . TYR   G  7  162 ? 52.182  -90.844  57.983  1.00 92.99  ? 153 TYR   G N   1 
ATOM   12364 C  CA  . TYR   G  7  162 ? 53.500  -90.826  58.672  1.00 93.89  ? 153 TYR   G CA  1 
ATOM   12365 C  C   . TYR   G  7  162 ? 53.439  -91.805  59.850  1.00 90.48  ? 153 TYR   G C   1 
ATOM   12366 O  O   . TYR   G  7  162 ? 52.354  -91.972  60.447  1.00 87.81  ? 153 TYR   G O   1 
ATOM   12367 C  CB  . TYR   G  7  162 ? 53.850  -89.399  59.104  1.00 93.77  ? 153 TYR   G CB  1 
ATOM   12368 C  CG  . TYR   G  7  162 ? 55.099  -89.243  59.936  1.00 95.93  ? 153 TYR   G CG  1 
ATOM   12369 C  CD1 . TYR   G  7  162 ? 55.045  -89.275  61.322  1.00 97.79  ? 153 TYR   G CD1 1 
ATOM   12370 C  CD2 . TYR   G  7  162 ? 56.331  -89.017  59.344  1.00 100.80 ? 153 TYR   G CD2 1 
ATOM   12371 C  CE1 . TYR   G  7  162 ? 56.184  -89.111  62.097  1.00 102.29 ? 153 TYR   G CE1 1 
ATOM   12372 C  CE2 . TYR   G  7  162 ? 57.478  -88.848  60.104  1.00 103.76 ? 153 TYR   G CE2 1 
ATOM   12373 C  CZ  . TYR   G  7  162 ? 57.407  -88.897  61.486  1.00 103.30 ? 153 TYR   G CZ  1 
ATOM   12374 O  OH  . TYR   G  7  162 ? 58.539  -88.734  62.234  1.00 104.28 ? 153 TYR   G OH  1 
ATOM   12375 N  N   . TYR   G  7  163 ? 54.562  -92.457  60.155  1.00 86.84  ? 154 TYR   G N   1 
ATOM   12376 C  CA  . TYR   G  7  163 ? 54.724  -93.308  61.362  1.00 88.39  ? 154 TYR   G CA  1 
ATOM   12377 C  C   . TYR   G  7  163 ? 56.201  -93.334  61.759  1.00 85.14  ? 154 TYR   G C   1 
ATOM   12378 O  O   . TYR   G  7  163 ? 57.076  -93.257  60.872  1.00 88.34  ? 154 TYR   G O   1 
ATOM   12379 C  CB  . TYR   G  7  163 ? 54.145  -94.706  61.124  1.00 87.57  ? 154 TYR   G CB  1 
ATOM   12380 C  CG  . TYR   G  7  163 ? 55.140  -95.777  60.747  1.00 90.12  ? 154 TYR   G CG  1 
ATOM   12381 C  CD1 . TYR   G  7  163 ? 55.549  -95.953  59.434  1.00 90.81  ? 154 TYR   G CD1 1 
ATOM   12382 C  CD2 . TYR   G  7  163 ? 55.662  -96.635  61.703  1.00 91.88  ? 154 TYR   G CD2 1 
ATOM   12383 C  CE1 . TYR   G  7  163 ? 56.456  -96.941  59.084  1.00 92.68  ? 154 TYR   G CE1 1 
ATOM   12384 C  CE2 . TYR   G  7  163 ? 56.571  -97.628  61.371  1.00 93.08  ? 154 TYR   G CE2 1 
ATOM   12385 C  CZ  . TYR   G  7  163 ? 56.969  -97.783  60.055  1.00 91.43  ? 154 TYR   G CZ  1 
ATOM   12386 O  OH  . TYR   G  7  163 ? 57.861  -98.758  59.716  1.00 94.91  ? 154 TYR   G OH  1 
ATOM   12387 N  N   . VAL   G  7  164 ? 56.463  -93.422  63.062  1.00 84.98  ? 155 VAL   G N   1 
ATOM   12388 C  CA  . VAL   G  7  164 ? 57.841  -93.537  63.623  1.00 86.78  ? 155 VAL   G CA  1 
ATOM   12389 C  C   . VAL   G  7  164 ? 57.759  -94.162  65.021  1.00 86.07  ? 155 VAL   G C   1 
ATOM   12390 O  O   . VAL   G  7  164 ? 56.709  -94.016  65.683  1.00 83.41  ? 155 VAL   G O   1 
ATOM   12391 C  CB  . VAL   G  7  164 ? 58.553  -92.169  63.639  1.00 87.49  ? 155 VAL   G CB  1 
ATOM   12392 C  CG1 . VAL   G  7  164 ? 57.971  -91.229  64.685  1.00 86.75  ? 155 VAL   G CG1 1 
ATOM   12393 C  CG2 . VAL   G  7  164 ? 60.055  -92.319  63.825  1.00 89.33  ? 155 VAL   G CG2 1 
ATOM   12394 N  N   . GLY   G  7  165 ? 58.828  -94.846  65.432  1.00 87.50  ? 156 GLY   G N   1 
ATOM   12395 C  CA  . GLY   G  7  165 ? 59.006  -95.362  66.802  1.00 89.15  ? 156 GLY   G CA  1 
ATOM   12396 C  C   . GLY   G  7  165 ? 59.381  -94.243  67.761  1.00 88.67  ? 156 GLY   G C   1 
ATOM   12397 O  O   . GLY   G  7  165 ? 59.987  -93.255  67.304  1.00 85.32  ? 156 GLY   G O   1 
ATOM   12398 N  N   . TYR   G  7  166 ? 59.049  -94.400  69.046  1.00 91.35  ? 157 TYR   G N   1 
ATOM   12399 C  CA  . TYR   G  7  166 ? 59.259  -93.386  70.113  1.00 91.57  ? 157 TYR   G CA  1 
ATOM   12400 C  C   . TYR   G  7  166 ? 59.898  -94.013  71.358  1.00 95.73  ? 157 TYR   G C   1 
ATOM   12401 O  O   . TYR   G  7  166 ? 59.596  -95.182  71.673  1.00 98.91  ? 157 TYR   G O   1 
ATOM   12402 C  CB  . TYR   G  7  166 ? 57.925  -92.748  70.500  1.00 92.46  ? 157 TYR   G CB  1 
ATOM   12403 C  CG  . TYR   G  7  166 ? 57.342  -91.830  69.457  1.00 92.97  ? 157 TYR   G CG  1 
ATOM   12404 C  CD1 . TYR   G  7  166 ? 56.490  -92.313  68.479  1.00 93.17  ? 157 TYR   G CD1 1 
ATOM   12405 C  CD2 . TYR   G  7  166 ? 57.642  -90.476  69.447  1.00 92.66  ? 157 TYR   G CD2 1 
ATOM   12406 C  CE1 . TYR   G  7  166 ? 55.948  -91.475  67.518  1.00 93.11  ? 157 TYR   G CE1 1 
ATOM   12407 C  CE2 . TYR   G  7  166 ? 57.108  -89.625  68.493  1.00 90.31  ? 157 TYR   G CE2 1 
ATOM   12408 C  CZ  . TYR   G  7  166 ? 56.256  -90.126  67.526  1.00 90.16  ? 157 TYR   G CZ  1 
ATOM   12409 O  OH  . TYR   G  7  166 ? 55.728  -89.298  66.580  1.00 89.02  ? 157 TYR   G OH  1 
ATOM   12410 N  N   . LYS   G  7  167 ? 60.748  -93.238  72.044  1.00 94.56  ? 158 LYS   G N   1 
ATOM   12411 C  CA  . LYS   G  7  167 ? 61.250  -93.517  73.418  1.00 94.35  ? 158 LYS   G CA  1 
ATOM   12412 C  C   . LYS   G  7  167 ? 60.082  -93.336  74.393  1.00 90.71  ? 158 LYS   G C   1 
ATOM   12413 O  O   . LYS   G  7  167 ? 59.932  -94.152  75.322  1.00 89.38  ? 158 LYS   G O   1 
ATOM   12414 C  CB  . LYS   G  7  167 ? 62.388  -92.561  73.789  1.00 99.20  ? 158 LYS   G CB  1 
ATOM   12415 C  CG  . LYS   G  7  167 ? 63.635  -92.650  72.919  1.00 106.53 ? 158 LYS   G CG  1 
ATOM   12416 C  CD  . LYS   G  7  167 ? 64.543  -91.440  73.041  1.00 113.27 ? 158 LYS   G CD  1 
ATOM   12417 C  CE  . LYS   G  7  167 ? 65.735  -91.494  72.108  1.00 116.89 ? 158 LYS   G CE  1 
ATOM   12418 N  NZ  . LYS   G  7  167 ? 66.505  -90.227  72.127  1.00 116.98 ? 158 LYS   G NZ  1 
ATOM   12419 N  N   . ALA   G  7  168 ? 59.317  -92.266  74.179  1.00 87.37  ? 159 ALA   G N   1 
ATOM   12420 C  CA  . ALA   G  7  168 ? 58.008  -91.961  74.798  1.00 87.44  ? 159 ALA   G CA  1 
ATOM   12421 C  C   . ALA   G  7  168 ? 57.276  -90.974  73.882  1.00 88.08  ? 159 ALA   G C   1 
ATOM   12422 O  O   . ALA   G  7  168 ? 57.943  -90.393  73.001  1.00 88.38  ? 159 ALA   G O   1 
ATOM   12423 C  CB  . ALA   G  7  168 ? 58.210  -91.381  76.171  1.00 87.95  ? 159 ALA   G CB  1 
ATOM   12424 N  N   . THR   G  7  169 ? 55.970  -90.775  74.066  1.00 86.23  ? 160 THR   G N   1 
ATOM   12425 C  CA  . THR   G  7  169 ? 55.176  -89.847  73.217  1.00 88.42  ? 160 THR   G CA  1 
ATOM   12426 C  C   . THR   G  7  169 ? 53.926  -89.363  73.957  1.00 87.77  ? 160 THR   G C   1 
ATOM   12427 O  O   . THR   G  7  169 ? 53.511  -90.010  74.942  1.00 84.45  ? 160 THR   G O   1 
ATOM   12428 C  CB  . THR   G  7  169 ? 54.818  -90.483  71.865  1.00 88.81  ? 160 THR   G CB  1 
ATOM   12429 O  OG1 . THR   G  7  169 ? 54.316  -89.471  70.991  1.00 94.97  ? 160 THR   G OG1 1 
ATOM   12430 C  CG2 . THR   G  7  169 ? 53.782  -91.579  71.968  1.00 89.37  ? 160 THR   G CG2 1 
ATOM   12431 N  N   . ALA   G  7  170 ? 53.374  -88.248  73.472  1.00 88.74  ? 161 ALA   G N   1 
ATOM   12432 C  CA  . ALA   G  7  170 ? 52.101  -87.636  73.914  1.00 88.64  ? 161 ALA   G CA  1 
ATOM   12433 C  C   . ALA   G  7  170 ? 51.339  -87.122  72.690  1.00 86.54  ? 161 ALA   G C   1 
ATOM   12434 O  O   . ALA   G  7  170 ? 51.991  -86.743  71.697  1.00 81.99  ? 161 ALA   G O   1 
ATOM   12435 C  CB  . ALA   G  7  170 ? 52.376  -86.522  74.890  1.00 90.43  ? 161 ALA   G CB  1 
ATOM   12436 N  N   . THR   G  7  171 ? 50.007  -87.119  72.775  1.00 87.72  ? 162 THR   G N   1 
ATOM   12437 C  CA  . THR   G  7  171 ? 49.080  -86.664  71.707  1.00 91.20  ? 162 THR   G CA  1 
ATOM   12438 C  C   . THR   G  7  171 ? 47.883  -85.961  72.353  1.00 92.38  ? 162 THR   G C   1 
ATOM   12439 O  O   . THR   G  7  171 ? 47.486  -86.381  73.461  1.00 90.94  ? 162 THR   G O   1 
ATOM   12440 C  CB  . THR   G  7  171 ? 48.595  -87.829  70.834  1.00 93.63  ? 162 THR   G CB  1 
ATOM   12441 O  OG1 . THR   G  7  171 ? 49.676  -88.728  70.574  1.00 94.32  ? 162 THR   G OG1 1 
ATOM   12442 C  CG2 . THR   G  7  171 ? 47.995  -87.346  69.530  1.00 95.88  ? 162 THR   G CG2 1 
ATOM   12443 N  N   . GLY   G  7  172 ? 47.337  -84.940  71.679  1.00 95.25  ? 163 GLY   G N   1 
ATOM   12444 C  CA  . GLY   G  7  172 ? 46.139  -84.198  72.118  1.00 93.95  ? 163 GLY   G CA  1 
ATOM   12445 C  C   . GLY   G  7  172 ? 46.363  -82.689  72.120  1.00 92.88  ? 163 GLY   G C   1 
ATOM   12446 O  O   . GLY   G  7  172 ? 47.425  -82.211  71.725  1.00 91.77  ? 163 GLY   G O   1 
ATOM   12447 N  N   . PRO   G  7  173 ? 45.361  -81.900  72.569  1.00 92.50  ? 164 PRO   G N   1 
ATOM   12448 C  CA  . PRO   G  7  173 ? 45.444  -80.439  72.540  1.00 93.18  ? 164 PRO   G CA  1 
ATOM   12449 C  C   . PRO   G  7  173 ? 46.656  -79.884  73.303  1.00 94.55  ? 164 PRO   G C   1 
ATOM   12450 O  O   . PRO   G  7  173 ? 47.309  -79.000  72.781  1.00 96.29  ? 164 PRO   G O   1 
ATOM   12451 C  CB  . PRO   G  7  173 ? 44.135  -79.981  73.203  1.00 92.78  ? 164 PRO   G CB  1 
ATOM   12452 C  CG  . PRO   G  7  173 ? 43.195  -81.157  73.041  1.00 91.23  ? 164 PRO   G CG  1 
ATOM   12453 C  CD  . PRO   G  7  173 ? 44.084  -82.379  73.119  1.00 90.62  ? 164 PRO   G CD  1 
ATOM   12454 N  N   . LYS   G  7  174 ? 46.928  -80.414  74.500  1.00 96.42  ? 165 LYS   G N   1 
ATOM   12455 C  CA  . LYS   G  7  174 ? 48.050  -79.975  75.374  1.00 100.87 ? 165 LYS   G CA  1 
ATOM   12456 C  C   . LYS   G  7  174 ? 49.184  -81.004  75.303  1.00 96.47  ? 165 LYS   G C   1 
ATOM   12457 O  O   . LYS   G  7  174 ? 49.709  -81.384  76.361  1.00 97.27  ? 165 LYS   G O   1 
ATOM   12458 C  CB  . LYS   G  7  174 ? 47.548  -79.756  76.805  1.00 106.39 ? 165 LYS   G CB  1 
ATOM   12459 C  CG  . LYS   G  7  174 ? 46.700  -78.504  76.994  1.00 113.65 ? 165 LYS   G CG  1 
ATOM   12460 C  CD  . LYS   G  7  174 ? 46.716  -77.952  78.407  1.00 119.82 ? 165 LYS   G CD  1 
ATOM   12461 C  CE  . LYS   G  7  174 ? 45.626  -78.525  79.287  1.00 123.79 ? 165 LYS   G CE  1 
ATOM   12462 N  NZ  . LYS   G  7  174 ? 44.324  -77.860  79.042  1.00 126.53 ? 165 LYS   G NZ  1 
ATOM   12463 N  N   . GLN   G  7  175 ? 49.562  -81.408  74.087  1.00 97.35  ? 166 GLN   G N   1 
ATOM   12464 C  CA  . GLN   G  7  175 ? 50.606  -82.435  73.828  1.00 97.56  ? 166 GLN   G CA  1 
ATOM   12465 C  C   . GLN   G  7  175 ? 51.995  -81.820  74.040  1.00 100.93 ? 166 GLN   G C   1 
ATOM   12466 O  O   . GLN   G  7  175 ? 52.850  -82.507  74.628  1.00 95.25  ? 166 GLN   G O   1 
ATOM   12467 C  CB  . GLN   G  7  175 ? 50.410  -83.031  72.430  1.00 99.06  ? 166 GLN   G CB  1 
ATOM   12468 C  CG  . GLN   G  7  175 ? 51.695  -83.398  71.697  1.00 101.52 ? 166 GLN   G CG  1 
ATOM   12469 C  CD  . GLN   G  7  175 ? 52.012  -82.427  70.587  1.00 103.44 ? 166 GLN   G CD  1 
ATOM   12470 O  OE1 . GLN   G  7  175 ? 53.054  -81.776  70.587  1.00 102.59 ? 166 GLN   G OE1 1 
ATOM   12471 N  NE2 . GLN   G  7  175 ? 51.103  -82.327  69.629  1.00 107.27 ? 166 GLN   G NE2 1 
ATOM   12472 N  N   . GLN   G  7  176 ? 52.206  -80.577  73.595  1.00 104.66 ? 167 GLN   G N   1 
ATOM   12473 C  CA  . GLN   G  7  176 ? 53.532  -79.900  73.627  1.00 107.24 ? 167 GLN   G CA  1 
ATOM   12474 C  C   . GLN   G  7  176 ? 54.032  -79.792  75.075  1.00 110.00 ? 167 GLN   G C   1 
ATOM   12475 O  O   . GLN   G  7  176 ? 55.244  -80.015  75.290  1.00 109.45 ? 167 GLN   G O   1 
ATOM   12476 C  CB  . GLN   G  7  176 ? 53.466  -78.523  72.960  1.00 107.92 ? 167 GLN   G CB  1 
ATOM   12477 C  CG  . GLN   G  7  176 ? 54.833  -77.879  72.766  1.00 109.67 ? 167 GLN   G CG  1 
ATOM   12478 C  CD  . GLN   G  7  176 ? 55.815  -78.805  72.086  1.00 110.87 ? 167 GLN   G CD  1 
ATOM   12479 O  OE1 . GLN   G  7  176 ? 55.580  -79.284  70.978  1.00 115.22 ? 167 GLN   G OE1 1 
ATOM   12480 N  NE2 . GLN   G  7  176 ? 56.928  -79.072  72.749  1.00 109.11 ? 167 GLN   G NE2 1 
ATOM   12481 N  N   . GLU   G  7  177 ? 53.144  -79.464  76.022  1.00 109.79 ? 168 GLU   G N   1 
ATOM   12482 C  CA  . GLU   G  7  177 ? 53.474  -79.340  77.471  1.00 113.46 ? 168 GLU   G CA  1 
ATOM   12483 C  C   . GLU   G  7  177 ? 53.974  -80.690  77.999  1.00 109.56 ? 168 GLU   G C   1 
ATOM   12484 O  O   . GLU   G  7  177 ? 55.010  -80.704  78.695  1.00 112.89 ? 168 GLU   G O   1 
ATOM   12485 C  CB  . GLU   G  7  177 ? 52.269  -78.861  78.287  1.00 122.98 ? 168 GLU   G CB  1 
ATOM   12486 C  CG  . GLU   G  7  177 ? 51.995  -77.368  78.173  1.00 131.25 ? 168 GLU   G CG  1 
ATOM   12487 C  CD  . GLU   G  7  177 ? 50.942  -76.971  77.151  1.00 141.45 ? 168 GLU   G CD  1 
ATOM   12488 O  OE1 . GLU   G  7  177 ? 50.060  -76.156  77.496  1.00 148.89 ? 168 GLU   G OE1 1 
ATOM   12489 O  OE2 . GLU   G  7  177 ? 51.013  -77.468  76.007  1.00 153.99 ? 168 GLU   G OE2 1 
ATOM   12490 N  N   . ILE   G  7  178 ? 53.270  -81.777  77.664  1.00 102.33 ? 169 ILE   G N   1 
ATOM   12491 C  CA  . ILE   G  7  178 ? 53.597  -83.164  78.113  1.00 97.16  ? 169 ILE   G CA  1 
ATOM   12492 C  C   . ILE   G  7  178 ? 54.921  -83.570  77.456  1.00 96.29  ? 169 ILE   G C   1 
ATOM   12493 O  O   . ILE   G  7  178 ? 55.773  -84.133  78.164  1.00 99.56  ? 169 ILE   G O   1 
ATOM   12494 C  CB  . ILE   G  7  178 ? 52.462  -84.161  77.789  1.00 92.17  ? 169 ILE   G CB  1 
ATOM   12495 C  CG1 . ILE   G  7  178 ? 51.093  -83.686  78.286  1.00 90.97  ? 169 ILE   G CG1 1 
ATOM   12496 C  CG2 . ILE   G  7  178 ? 52.789  -85.540  78.340  1.00 89.83  ? 169 ILE   G CG2 1 
ATOM   12497 C  CD1 . ILE   G  7  178 ? 49.927  -84.381  77.617  1.00 89.96  ? 169 ILE   G CD1 1 
ATOM   12498 N  N   . THR   G  7  179 ? 55.083  -83.277  76.160  1.00 96.06  ? 170 THR   G N   1 
ATOM   12499 C  CA  . THR   G  7  179 ? 56.263  -83.661  75.335  1.00 100.05 ? 170 THR   G CA  1 
ATOM   12500 C  C   . THR   G  7  179 ? 57.542  -83.094  75.961  1.00 100.67 ? 170 THR   G C   1 
ATOM   12501 O  O   . THR   G  7  179 ? 58.481  -83.877  76.181  1.00 95.82  ? 170 THR   G O   1 
ATOM   12502 C  CB  . THR   G  7  179 ? 56.120  -83.191  73.881  1.00 103.14 ? 170 THR   G CB  1 
ATOM   12503 O  OG1 . THR   G  7  179 ? 54.864  -83.642  73.374  1.00 105.93 ? 170 THR   G OG1 1 
ATOM   12504 C  CG2 . THR   G  7  179 ? 57.239  -83.693  72.993  1.00 105.98 ? 170 THR   G CG2 1 
ATOM   12505 N  N   . THR   G  7  180 ? 57.578  -81.784  76.224  1.00 104.33 ? 171 THR   G N   1 
ATOM   12506 C  CA  . THR   G  7  180 ? 58.745  -81.085  76.830  1.00 106.17 ? 171 THR   G CA  1 
ATOM   12507 C  C   . THR   G  7  180 ? 58.990  -81.634  78.240  1.00 108.61 ? 171 THR   G C   1 
ATOM   12508 O  O   . THR   G  7  180 ? 60.166  -81.846  78.590  1.00 113.00 ? 171 THR   G O   1 
ATOM   12509 C  CB  . THR   G  7  180 ? 58.568  -79.560  76.843  1.00 107.65 ? 171 THR   G CB  1 
ATOM   12510 O  OG1 . THR   G  7  180 ? 57.190  -79.264  77.075  1.00 104.63 ? 171 THR   G OG1 1 
ATOM   12511 C  CG2 . THR   G  7  180 ? 59.028  -78.913  75.555  1.00 109.78 ? 171 THR   G CG2 1 
ATOM   12512 N  N   . ASN   G  7  181 ? 57.921  -81.864  79.008  1.00 102.26 ? 172 ASN   G N   1 
ATOM   12513 C  CA  . ASN   G  7  181 ? 57.992  -82.448  80.375  1.00 101.92 ? 172 ASN   G CA  1 
ATOM   12514 C  C   . ASN   G  7  181 ? 58.781  -83.762  80.319  1.00 101.72 ? 172 ASN   G C   1 
ATOM   12515 O  O   . ASN   G  7  181 ? 59.672  -83.948  81.172  1.00 97.83  ? 172 ASN   G O   1 
ATOM   12516 C  CB  . ASN   G  7  181 ? 56.601  -82.648  80.981  1.00 99.05  ? 172 ASN   G CB  1 
ATOM   12517 C  CG  . ASN   G  7  181 ? 56.650  -83.266  82.362  1.00 100.73 ? 172 ASN   G CG  1 
ATOM   12518 O  OD1 . ASN   G  7  181 ? 56.862  -84.467  82.500  1.00 97.11  ? 172 ASN   G OD1 1 
ATOM   12519 N  ND2 . ASN   G  7  181 ? 56.464  -82.457  83.392  1.00 102.42 ? 172 ASN   G ND2 1 
ATOM   12520 N  N   . LEU   G  7  182 ? 58.464  -84.623  79.344  1.00 102.92 ? 173 LEU   G N   1 
ATOM   12521 C  CA  . LEU   G  7  182 ? 59.114  -85.945  79.129  1.00 103.27 ? 173 LEU   G CA  1 
ATOM   12522 C  C   . LEU   G  7  182 ? 60.548  -85.743  78.617  1.00 105.98 ? 173 LEU   G C   1 
ATOM   12523 O  O   . LEU   G  7  182 ? 61.448  -86.431  79.137  1.00 104.90 ? 173 LEU   G O   1 
ATOM   12524 C  CB  . LEU   G  7  182 ? 58.275  -86.774  78.149  1.00 101.03 ? 173 LEU   G CB  1 
ATOM   12525 C  CG  . LEU   G  7  182 ? 56.960  -87.319  78.709  1.00 101.28 ? 173 LEU   G CG  1 
ATOM   12526 C  CD1 . LEU   G  7  182 ? 56.014  -87.726  77.587  1.00 101.56 ? 173 LEU   G CD1 1 
ATOM   12527 C  CD2 . LEU   G  7  182 ? 57.212  -88.494  79.643  1.00 100.12 ? 173 LEU   G CD2 1 
ATOM   12528 N  N   . GLU   G  7  183 ? 60.751  -84.840  77.646  1.00 109.02 ? 174 GLU   G N   1 
ATOM   12529 C  CA  . GLU   G  7  183 ? 62.088  -84.478  77.090  1.00 111.49 ? 174 GLU   G CA  1 
ATOM   12530 C  C   . GLU   G  7  183 ? 63.035  -84.095  78.230  1.00 112.38 ? 174 GLU   G C   1 
ATOM   12531 O  O   . GLU   G  7  183 ? 64.194  -84.555  78.220  1.00 113.00 ? 174 GLU   G O   1 
ATOM   12532 C  CB  . GLU   G  7  183 ? 62.011  -83.279  76.142  1.00 113.58 ? 174 GLU   G CB  1 
ATOM   12533 C  CG  . GLU   G  7  183 ? 61.438  -83.588  74.774  1.00 116.50 ? 174 GLU   G CG  1 
ATOM   12534 C  CD  . GLU   G  7  183 ? 61.192  -82.352  73.922  1.00 120.08 ? 174 GLU   G CD  1 
ATOM   12535 O  OE1 . GLU   G  7  183 ? 61.848  -81.316  74.173  1.00 122.04 ? 174 GLU   G OE1 1 
ATOM   12536 O  OE2 . GLU   G  7  183 ? 60.350  -82.427  73.005  1.00 121.43 ? 174 GLU   G OE2 1 
ATOM   12537 N  N   . ASN   G  7  184 ? 62.554  -83.258  79.153  1.00 112.02 ? 175 ASN   G N   1 
ATOM   12538 C  CA  . ASN   G  7  184 ? 63.349  -82.711  80.281  1.00 119.20 ? 175 ASN   G CA  1 
ATOM   12539 C  C   . ASN   G  7  184 ? 63.734  -83.852  81.230  1.00 121.13 ? 175 ASN   G C   1 
ATOM   12540 O  O   . ASN   G  7  184 ? 64.870  -83.823  81.742  1.00 130.00 ? 175 ASN   G O   1 
ATOM   12541 C  CB  . ASN   G  7  184 ? 62.610  -81.581  81.007  1.00 121.71 ? 175 ASN   G CB  1 
ATOM   12542 C  CG  . ASN   G  7  184 ? 62.379  -80.354  80.149  1.00 121.65 ? 175 ASN   G CG  1 
ATOM   12543 O  OD1 . ASN   G  7  184 ? 61.308  -79.753  80.205  1.00 122.14 ? 175 ASN   G OD1 1 
ATOM   12544 N  ND2 . ASN   G  7  184 ? 63.367  -79.965  79.356  1.00 126.30 ? 175 ASN   G ND2 1 
ATOM   12545 N  N   . HIS   G  7  185 ? 62.840  -84.822  81.447  1.00 120.84 ? 176 HIS   G N   1 
ATOM   12546 C  CA  . HIS   G  7  185 ? 63.103  -86.009  82.305  1.00 121.67 ? 176 HIS   G CA  1 
ATOM   12547 C  C   . HIS   G  7  185 ? 64.222  -86.860  81.692  1.00 123.46 ? 176 HIS   G C   1 
ATOM   12548 O  O   . HIS   G  7  185 ? 65.137  -87.250  82.444  1.00 126.42 ? 176 HIS   G O   1 
ATOM   12549 C  CB  . HIS   G  7  185 ? 61.837  -86.847  82.534  1.00 119.60 ? 176 HIS   G CB  1 
ATOM   12550 C  CG  . HIS   G  7  185 ? 62.116  -88.106  83.284  1.00 118.98 ? 176 HIS   G CG  1 
ATOM   12551 N  ND1 . HIS   G  7  185 ? 62.378  -89.302  82.646  1.00 117.08 ? 176 HIS   G ND1 1 
ATOM   12552 C  CD2 . HIS   G  7  185 ? 62.224  -88.351  84.608  1.00 118.94 ? 176 HIS   G CD2 1 
ATOM   12553 C  CE1 . HIS   G  7  185 ? 62.613  -90.236  83.544  1.00 119.03 ? 176 HIS   G CE1 1 
ATOM   12554 N  NE2 . HIS   G  7  185 ? 62.527  -89.677  84.756  1.00 116.37 ? 176 HIS   G NE2 1 
ATOM   12555 N  N   . PHE   G  7  186 ? 64.147  -87.140  80.386  1.00 123.44 ? 177 PHE   G N   1 
ATOM   12556 C  CA  . PHE   G  7  186 ? 65.087  -88.038  79.661  1.00 127.17 ? 177 PHE   G CA  1 
ATOM   12557 C  C   . PHE   G  7  186 ? 66.434  -87.336  79.442  1.00 128.07 ? 177 PHE   G C   1 
ATOM   12558 O  O   . PHE   G  7  186 ? 67.447  -88.051  79.309  1.00 132.38 ? 177 PHE   G O   1 
ATOM   12559 C  CB  . PHE   G  7  186 ? 64.474  -88.539  78.349  1.00 128.52 ? 177 PHE   G CB  1 
ATOM   12560 C  CG  . PHE   G  7  186 ? 63.374  -89.558  78.523  1.00 127.98 ? 177 PHE   G CG  1 
ATOM   12561 C  CD1 . PHE   G  7  186 ? 63.605  -90.744  79.204  1.00 128.02 ? 177 PHE   G CD1 1 
ATOM   12562 C  CD2 . PHE   G  7  186 ? 62.106  -89.335  78.006  1.00 125.74 ? 177 PHE   G CD2 1 
ATOM   12563 C  CE1 . PHE   G  7  186 ? 62.594  -91.678  79.370  1.00 124.26 ? 177 PHE   G CE1 1 
ATOM   12564 C  CE2 . PHE   G  7  186 ? 61.097  -90.271  78.173  1.00 123.45 ? 177 PHE   G CE2 1 
ATOM   12565 C  CZ  . PHE   G  7  186 ? 61.342  -91.441  78.854  1.00 123.09 ? 177 PHE   G CZ  1 
ATOM   12566 N  N   . LYS   G  7  187 ? 66.450  -85.997  79.400  1.00 127.95 ? 178 LYS   G N   1 
ATOM   12567 C  CA  . LYS   G  7  187 ? 67.699  -85.190  79.479  1.00 126.85 ? 178 LYS   G CA  1 
ATOM   12568 C  C   . LYS   G  7  187 ? 68.401  -85.521  80.802  1.00 122.77 ? 178 LYS   G C   1 
ATOM   12569 O  O   . LYS   G  7  187 ? 69.626  -85.745  80.781  1.00 111.05 ? 178 LYS   G O   1 
ATOM   12570 C  CB  . LYS   G  7  187 ? 67.413  -83.685  79.394  1.00 128.12 ? 178 LYS   G CB  1 
ATOM   12571 C  CG  . LYS   G  7  187 ? 67.612  -83.046  78.026  1.00 132.88 ? 178 LYS   G CG  1 
ATOM   12572 C  CD  . LYS   G  7  187 ? 67.904  -81.559  78.110  1.00 137.60 ? 178 LYS   G CD  1 
ATOM   12573 C  CE  . LYS   G  7  187 ? 67.846  -80.851  76.773  1.00 142.82 ? 178 LYS   G CE  1 
ATOM   12574 N  NZ  . LYS   G  7  187 ? 66.451  -80.590  76.347  1.00 144.39 ? 178 LYS   G NZ  1 
ATOM   12575 N  N   . LYS   G  7  188 ? 67.628  -85.575  81.892  1.00 126.19 ? 179 LYS   G N   1 
ATOM   12576 C  CA  . LYS   G  7  188 ? 68.106  -85.752  83.291  1.00 133.35 ? 179 LYS   G CA  1 
ATOM   12577 C  C   . LYS   G  7  188 ? 68.559  -87.203  83.504  1.00 134.89 ? 179 LYS   G C   1 
ATOM   12578 O  O   . LYS   G  7  188 ? 69.705  -87.400  83.952  1.00 139.62 ? 179 LYS   G O   1 
ATOM   12579 C  CB  . LYS   G  7  188 ? 66.993  -85.371  84.274  1.00 135.34 ? 179 LYS   G CB  1 
ATOM   12580 C  CG  . LYS   G  7  188 ? 67.451  -84.692  85.557  1.00 137.34 ? 179 LYS   G CG  1 
ATOM   12581 C  CD  . LYS   G  7  188 ? 66.295  -84.298  86.450  1.00 140.92 ? 179 LYS   G CD  1 
ATOM   12582 C  CE  . LYS   G  7  188 ? 66.619  -83.154  87.386  1.00 143.37 ? 179 LYS   G CE  1 
ATOM   12583 N  NZ  . LYS   G  7  188 ? 65.403  -82.667  88.080  1.00 146.04 ? 179 LYS   G NZ  1 
ATOM   12584 N  N   . SER   G  7  189 ? 67.690  -88.174  83.195  1.00 133.95 ? 180 SER   G N   1 
ATOM   12585 C  CA  . SER   G  7  189 ? 67.903  -89.627  83.441  1.00 132.59 ? 180 SER   G CA  1 
ATOM   12586 C  C   . SER   G  7  189 ? 69.012  -90.177  82.531  1.00 129.48 ? 180 SER   G C   1 
ATOM   12587 O  O   . SER   G  7  189 ? 69.683  -91.138  82.952  1.00 130.68 ? 180 SER   G O   1 
ATOM   12588 C  CB  . SER   G  7  189 ? 66.620  -90.406  83.274  1.00 132.92 ? 180 SER   G CB  1 
ATOM   12589 O  OG  . SER   G  7  189 ? 66.261  -90.522  81.904  1.00 132.49 ? 180 SER   G OG  1 
ATOM   12590 N  N   . LYS   G  7  190 ? 69.176  -89.606  81.331  1.00 128.08 ? 181 LYS   G N   1 
ATOM   12591 C  CA  . LYS   G  7  190 ? 70.265  -89.929  80.365  1.00 130.84 ? 181 LYS   G CA  1 
ATOM   12592 C  C   . LYS   G  7  190 ? 70.016  -91.295  79.704  1.00 128.19 ? 181 LYS   G C   1 
ATOM   12593 O  O   . LYS   G  7  190 ? 70.975  -91.838  79.116  1.00 125.02 ? 181 LYS   G O   1 
ATOM   12594 C  CB  . LYS   G  7  190 ? 71.623  -89.924  81.079  1.00 133.54 ? 181 LYS   G CB  1 
ATOM   12595 C  CG  . LYS   G  7  190 ? 72.815  -89.480  80.239  1.00 138.24 ? 181 LYS   G CG  1 
ATOM   12596 C  CD  . LYS   G  7  190 ? 73.354  -88.111  80.614  1.00 142.30 ? 181 LYS   G CD  1 
ATOM   12597 C  CE  . LYS   G  7  190 ? 72.534  -86.969  80.052  1.00 140.27 ? 181 LYS   G CE  1 
ATOM   12598 N  NZ  . LYS   G  7  190 ? 72.958  -85.663  80.611  1.00 140.13 ? 181 LYS   G NZ  1 
ATOM   12599 N  N   . ILE   G  7  191 ? 68.787  -91.826  79.777  1.00 127.96 ? 182 ILE   G N   1 
ATOM   12600 C  CA  . ILE   G  7  191 ? 68.418  -93.178  79.250  1.00 126.05 ? 182 ILE   G CA  1 
ATOM   12601 C  C   . ILE   G  7  191 ? 67.154  -93.076  78.387  1.00 127.72 ? 182 ILE   G C   1 
ATOM   12602 O  O   . ILE   G  7  191 ? 66.516  -92.005  78.382  1.00 123.76 ? 182 ILE   G O   1 
ATOM   12603 C  CB  . ILE   G  7  191 ? 68.253  -94.205  80.392  1.00 125.78 ? 182 ILE   G CB  1 
ATOM   12604 C  CG1 . ILE   G  7  191 ? 67.373  -93.674  81.529  1.00 124.11 ? 182 ILE   G CG1 1 
ATOM   12605 C  CG2 . ILE   G  7  191 ? 69.615  -94.662  80.892  1.00 124.66 ? 182 ILE   G CG2 1 
ATOM   12606 C  CD1 . ILE   G  7  191 ? 66.904  -94.739  82.492  1.00 125.26 ? 182 ILE   G CD1 1 
ATOM   12607 N  N   . ASP   G  7  192 ? 66.817  -94.171  77.697  1.00 128.39 ? 183 ASP   G N   1 
ATOM   12608 C  CA  . ASP   G  7  192 ? 65.763  -94.242  76.647  1.00 128.39 ? 183 ASP   G CA  1 
ATOM   12609 C  C   . ASP   G  7  192 ? 64.406  -94.645  77.241  1.00 127.30 ? 183 ASP   G C   1 
ATOM   12610 O  O   . ASP   G  7  192 ? 63.422  -94.641  76.475  1.00 128.42 ? 183 ASP   G O   1 
ATOM   12611 C  CB  . ASP   G  7  192 ? 66.159  -95.236  75.550  1.00 129.43 ? 183 ASP   G CB  1 
ATOM   12612 C  CG  . ASP   G  7  192 ? 67.045  -94.658  74.460  1.00 130.74 ? 183 ASP   G CG  1 
ATOM   12613 O  OD1 . ASP   G  7  192 ? 67.365  -93.454  74.529  1.00 133.51 ? 183 ASP   G OD1 1 
ATOM   12614 O  OD2 . ASP   G  7  192 ? 67.404  -95.421  73.543  1.00 135.29 ? 183 ASP   G OD2 1 
ATOM   12615 N  N   . HIS   G  7  193 ? 64.340  -94.974  78.537  1.00 125.84 ? 184 HIS   G N   1 
ATOM   12616 C  CA  . HIS   G  7  193 ? 63.152  -95.611  79.169  1.00 122.44 ? 184 HIS   G CA  1 
ATOM   12617 C  C   . HIS   G  7  193 ? 63.074  -95.286  80.664  1.00 121.47 ? 184 HIS   G C   1 
ATOM   12618 O  O   . HIS   G  7  193 ? 64.006  -94.639  81.184  1.00 121.67 ? 184 HIS   G O   1 
ATOM   12619 C  CB  . HIS   G  7  193 ? 63.204  -97.127  78.942  1.00 123.56 ? 184 HIS   G CB  1 
ATOM   12620 C  CG  . HIS   G  7  193 ? 64.424  -97.765  79.515  1.00 124.72 ? 184 HIS   G CG  1 
ATOM   12621 N  ND1 . HIS   G  7  193 ? 64.424  -98.377  80.752  1.00 126.89 ? 184 HIS   G ND1 1 
ATOM   12622 C  CD2 . HIS   G  7  193 ? 65.683  -97.872  79.037  1.00 127.00 ? 184 HIS   G CD2 1 
ATOM   12623 C  CE1 . HIS   G  7  193 ? 65.629  -98.843  81.009  1.00 125.99 ? 184 HIS   G CE1 1 
ATOM   12624 N  NE2 . HIS   G  7  193 ? 66.420  -98.547  79.972  1.00 125.45 ? 184 HIS   G NE2 1 
ATOM   12625 N  N   . ILE   G  7  194 ? 61.997  -95.736  81.316  1.00 115.16 ? 185 ILE   G N   1 
ATOM   12626 C  CA  . ILE   G  7  194 ? 61.787  -95.640  82.792  1.00 117.26 ? 185 ILE   G CA  1 
ATOM   12627 C  C   . ILE   G  7  194 ? 62.497  -96.834  83.438  1.00 121.82 ? 185 ILE   G C   1 
ATOM   12628 O  O   . ILE   G  7  194 ? 62.010  -97.970  83.272  1.00 124.77 ? 185 ILE   G O   1 
ATOM   12629 C  CB  . ILE   G  7  194 ? 60.288  -95.607  83.159  1.00 114.59 ? 185 ILE   G CB  1 
ATOM   12630 C  CG1 . ILE   G  7  194 ? 59.479  -94.657  82.268  1.00 115.62 ? 185 ILE   G CG1 1 
ATOM   12631 C  CG2 . ILE   G  7  194 ? 60.105  -95.279  84.633  1.00 113.89 ? 185 ILE   G CG2 1 
ATOM   12632 C  CD1 . ILE   G  7  194 ? 60.088  -93.284  82.094  1.00 118.91 ? 185 ILE   G CD1 1 
ATOM   12633 N  N   . ASN   G  7  195 ? 63.604  -96.585  84.144  1.00 124.32 ? 186 ASN   G N   1 
ATOM   12634 C  CA  . ASN   G  7  195 ? 64.444  -97.637  84.778  1.00 125.30 ? 186 ASN   G CA  1 
ATOM   12635 C  C   . ASN   G  7  195 ? 63.695  -98.199  85.992  1.00 122.89 ? 186 ASN   G C   1 
ATOM   12636 O  O   . ASN   G  7  195 ? 64.088  -97.885  87.130  1.00 122.75 ? 186 ASN   G O   1 
ATOM   12637 C  CB  . ASN   G  7  195 ? 65.830  -97.102  85.150  1.00 128.21 ? 186 ASN   G CB  1 
ATOM   12638 C  CG  . ASN   G  7  195 ? 66.800  -98.192  85.556  1.00 130.01 ? 186 ASN   G CG  1 
ATOM   12639 O  OD1 . ASN   G  7  195 ? 67.391  -98.130  86.632  1.00 139.49 ? 186 ASN   G OD1 1 
ATOM   12640 N  ND2 . ASN   G  7  195 ? 66.974  -99.191  84.707  1.00 127.27 ? 186 ASN   G ND2 1 
ATOM   12641 N  N   . GLU   G  7  196 ? 62.654  -98.998  85.746  1.00 120.89 ? 187 GLU   G N   1 
ATOM   12642 C  CA  . GLU   G  7  196 ? 61.751  -99.540  86.795  1.00 125.70 ? 187 GLU   G CA  1 
ATOM   12643 C  C   . GLU   G  7  196 ? 61.453  -101.017 86.509  1.00 127.39 ? 187 GLU   G C   1 
ATOM   12644 O  O   . GLU   G  7  196 ? 61.305  -101.378 85.322  1.00 127.57 ? 187 GLU   G O   1 
ATOM   12645 C  CB  . GLU   G  7  196 ? 60.466  -98.714  86.851  1.00 124.68 ? 187 GLU   G CB  1 
ATOM   12646 C  CG  . GLU   G  7  196 ? 59.775  -98.773  88.198  1.00 126.59 ? 187 GLU   G CG  1 
ATOM   12647 C  CD  . GLU   G  7  196 ? 60.476  -98.004  89.305  1.00 129.35 ? 187 GLU   G CD  1 
ATOM   12648 O  OE1 . GLU   G  7  196 ? 60.815  -96.826  89.083  1.00 131.15 ? 187 GLU   G OE1 1 
ATOM   12649 O  OE2 . GLU   G  7  196 ? 60.690  -98.588  90.385  1.00 135.38 ? 187 GLU   G OE2 1 
ATOM   12650 N  N   . GLU   G  7  197 ? 61.356  -101.825 87.570  1.00 130.87 ? 188 GLU   G N   1 
ATOM   12651 C  CA  . GLU   G  7  197 ? 61.165  -103.299 87.507  1.00 130.24 ? 188 GLU   G CA  1 
ATOM   12652 C  C   . GLU   G  7  197 ? 59.697  -103.612 87.201  1.00 120.43 ? 188 GLU   G C   1 
ATOM   12653 O  O   . GLU   G  7  197 ? 59.436  -104.272 86.179  1.00 120.23 ? 188 GLU   G O   1 
ATOM   12654 C  CB  . GLU   G  7  197 ? 61.579  -103.950 88.828  1.00 136.65 ? 188 GLU   G CB  1 
ATOM   12655 C  CG  . GLU   G  7  197 ? 63.040  -103.745 89.187  1.00 146.28 ? 188 GLU   G CG  1 
ATOM   12656 C  CD  . GLU   G  7  197 ? 64.003  -104.696 88.498  1.00 151.89 ? 188 GLU   G CD  1 
ATOM   12657 O  OE1 . GLU   G  7  197 ? 64.931  -105.183 89.175  1.00 158.02 ? 188 GLU   G OE1 1 
ATOM   12658 O  OE2 . GLU   G  7  197 ? 63.826  -104.947 87.288  1.00 157.34 ? 188 GLU   G OE2 1 
ATOM   12659 N  N   . SER   G  7  198 ? 58.784  -103.153 88.062  1.00 114.91 ? 189 SER   G N   1 
ATOM   12660 C  CA  . SER   G  7  198 ? 57.326  -103.435 87.994  1.00 116.95 ? 189 SER   G CA  1 
ATOM   12661 C  C   . SER   G  7  198 ? 56.648  -102.451 87.034  1.00 115.71 ? 189 SER   G C   1 
ATOM   12662 O  O   . SER   G  7  198 ? 57.090  -101.286 86.976  1.00 122.54 ? 189 SER   G O   1 
ATOM   12663 C  CB  . SER   G  7  198 ? 56.700  -103.382 89.366  1.00 116.15 ? 189 SER   G CB  1 
ATOM   12664 O  OG  . SER   G  7  198 ? 56.615  -102.046 89.843  1.00 115.85 ? 189 SER   G OG  1 
ATOM   12665 N  N   . TRP   G  7  199 ? 55.619  -102.907 86.311  1.00 112.95 ? 190 TRP   G N   1 
ATOM   12666 C  CA  . TRP   G  7  199 ? 54.760  -102.047 85.451  1.00 109.07 ? 190 TRP   G CA  1 
ATOM   12667 C  C   . TRP   G  7  199 ? 53.953  -101.084 86.330  1.00 112.56 ? 190 TRP   G C   1 
ATOM   12668 O  O   . TRP   G  7  199 ? 53.680  -99.960  85.861  1.00 116.39 ? 190 TRP   G O   1 
ATOM   12669 C  CB  . TRP   G  7  199 ? 53.852  -102.878 84.530  1.00 105.11 ? 190 TRP   G CB  1 
ATOM   12670 C  CG  . TRP   G  7  199 ? 52.897  -103.806 85.219  1.00 101.66 ? 190 TRP   G CG  1 
ATOM   12671 C  CD1 . TRP   G  7  199 ? 53.071  -105.142 85.433  1.00 101.04 ? 190 TRP   G CD1 1 
ATOM   12672 C  CD2 . TRP   G  7  199 ? 51.599  -103.484 85.756  1.00 102.16 ? 190 TRP   G CD2 1 
ATOM   12673 N  NE1 . TRP   G  7  199 ? 51.984  -105.669 86.076  1.00 100.30 ? 190 TRP   G NE1 1 
ATOM   12674 C  CE2 . TRP   G  7  199 ? 51.063  -104.678 86.286  1.00 101.31 ? 190 TRP   G CE2 1 
ATOM   12675 C  CE3 . TRP   G  7  199 ? 50.840  -102.310 85.851  1.00 103.86 ? 190 TRP   G CE3 1 
ATOM   12676 C  CZ2 . TRP   G  7  199 ? 49.810  -104.729 86.897  1.00 102.56 ? 190 TRP   G CZ2 1 
ATOM   12677 C  CZ3 . TRP   G  7  199 ? 49.602  -102.361 86.455  1.00 103.34 ? 190 TRP   G CZ3 1 
ATOM   12678 C  CH2 . TRP   G  7  199 ? 49.096  -103.555 86.972  1.00 102.69 ? 190 TRP   G CH2 1 
ATOM   12679 N  N   . GLU   G  7  200 ? 53.608  -101.502 87.555  1.00 112.39 ? 191 GLU   G N   1 
ATOM   12680 C  CA  . GLU   G  7  200 ? 52.802  -100.712 88.529  1.00 111.55 ? 191 GLU   G CA  1 
ATOM   12681 C  C   . GLU   G  7  200 ? 53.434  -99.330  88.739  1.00 111.24 ? 191 GLU   G C   1 
ATOM   12682 O  O   . GLU   G  7  200 ? 52.675  -98.344  88.769  1.00 108.96 ? 191 GLU   G O   1 
ATOM   12683 C  CB  . GLU   G  7  200 ? 52.676  -101.440 89.871  1.00 115.36 ? 191 GLU   G CB  1 
ATOM   12684 C  CG  . GLU   G  7  200 ? 51.682  -102.591 89.863  1.00 117.50 ? 191 GLU   G CG  1 
ATOM   12685 C  CD  . GLU   G  7  200 ? 52.263  -103.958 89.538  1.00 116.93 ? 191 GLU   G CD  1 
ATOM   12686 O  OE1 . GLU   G  7  200 ? 51.693  -104.966 90.002  1.00 115.19 ? 191 GLU   G OE1 1 
ATOM   12687 O  OE2 . GLU   G  7  200 ? 53.279  -104.016 88.818  1.00 126.77 ? 191 GLU   G OE2 1 
ATOM   12688 N  N   . LYS   G  7  201 ? 54.763  -99.265  88.877  1.00 107.69 ? 192 LYS   G N   1 
ATOM   12689 C  CA  . LYS   G  7  201 ? 55.511  -98.003  89.128  1.00 110.88 ? 192 LYS   G CA  1 
ATOM   12690 C  C   . LYS   G  7  201 ? 55.706  -97.220  87.821  1.00 109.68 ? 192 LYS   G C   1 
ATOM   12691 O  O   . LYS   G  7  201 ? 55.796  -95.979  87.902  1.00 115.77 ? 192 LYS   G O   1 
ATOM   12692 C  CB  . LYS   G  7  201 ? 56.854  -98.289  89.803  1.00 115.75 ? 192 LYS   G CB  1 
ATOM   12693 C  CG  . LYS   G  7  201 ? 56.768  -98.736  91.257  1.00 122.00 ? 192 LYS   G CG  1 
ATOM   12694 C  CD  . LYS   G  7  201 ? 57.838  -98.137  92.152  1.00 125.77 ? 192 LYS   G CD  1 
ATOM   12695 C  CE  . LYS   G  7  201 ? 57.312  -97.063  93.082  1.00 127.99 ? 192 LYS   G CE  1 
ATOM   12696 N  NZ  . LYS   G  7  201 ? 56.503  -97.645  94.179  1.00 131.87 ? 192 LYS   G NZ  1 
ATOM   12697 N  N   . VAL   G  7  202 ? 55.773  -97.893  86.667  1.00 102.69 ? 193 VAL   G N   1 
ATOM   12698 C  CA  . VAL   G  7  202 ? 55.859  -97.217  85.335  1.00 98.96  ? 193 VAL   G CA  1 
ATOM   12699 C  C   . VAL   G  7  202 ? 54.515  -96.536  85.053  1.00 98.94  ? 193 VAL   G C   1 
ATOM   12700 O  O   . VAL   G  7  202 ? 54.536  -95.438  84.466  1.00 99.64  ? 193 VAL   G O   1 
ATOM   12701 C  CB  . VAL   G  7  202 ? 56.248  -98.174  84.193  1.00 95.86  ? 193 VAL   G CB  1 
ATOM   12702 C  CG1 . VAL   G  7  202 ? 56.348  -97.447  82.860  1.00 93.71  ? 193 VAL   G CG1 1 
ATOM   12703 C  CG2 . VAL   G  7  202 ? 57.549  -98.903  84.487  1.00 98.59  ? 193 VAL   G CG2 1 
ATOM   12704 N  N   . VAL   G  7  203 ? 53.400  -97.157  85.456  1.00 96.40  ? 194 VAL   G N   1 
ATOM   12705 C  CA  . VAL   G  7  203 ? 52.036  -96.548  85.383  1.00 99.31  ? 194 VAL   G CA  1 
ATOM   12706 C  C   . VAL   G  7  203 ? 52.001  -95.317  86.299  1.00 101.90 ? 194 VAL   G C   1 
ATOM   12707 O  O   . VAL   G  7  203 ? 51.420  -94.291  85.886  1.00 99.65  ? 194 VAL   G O   1 
ATOM   12708 C  CB  . VAL   G  7  203 ? 50.922  -97.551  85.748  1.00 102.10 ? 194 VAL   G CB  1 
ATOM   12709 C  CG1 . VAL   G  7  203 ? 49.563  -96.870  85.842  1.00 105.16 ? 194 VAL   G CG1 1 
ATOM   12710 C  CG2 . VAL   G  7  203 ? 50.852  -98.714  84.770  1.00 99.79  ? 194 VAL   G CG2 1 
ATOM   12711 N  N   . GLU   G  7  204 ? 52.589  -95.421  87.495  1.00 101.62 ? 195 GLU   G N   1 
ATOM   12712 C  CA  . GLU   G  7  204 ? 52.649  -94.325  88.501  1.00 103.69 ? 195 GLU   G CA  1 
ATOM   12713 C  C   . GLU   G  7  204 ? 53.464  -93.151  87.945  1.00 103.55 ? 195 GLU   G C   1 
ATOM   12714 O  O   . GLU   G  7  204 ? 53.033  -91.996  88.147  1.00 103.63 ? 195 GLU   G O   1 
ATOM   12715 C  CB  . GLU   G  7  204 ? 53.239  -94.829  89.819  1.00 107.58 ? 195 GLU   G CB  1 
ATOM   12716 C  CG  . GLU   G  7  204 ? 52.271  -95.682  90.617  1.00 110.58 ? 195 GLU   G CG  1 
ATOM   12717 C  CD  . GLU   G  7  204 ? 52.878  -96.490  91.754  1.00 114.98 ? 195 GLU   G CD  1 
ATOM   12718 O  OE1 . GLU   G  7  204 ? 52.266  -97.508  92.142  1.00 115.17 ? 195 GLU   G OE1 1 
ATOM   12719 O  OE2 . GLU   G  7  204 ? 53.958  -96.101  92.250  1.00 117.78 ? 195 GLU   G OE2 1 
ATOM   12720 N  N   . PHE   G  7  205 ? 54.590  -93.435  87.280  1.00 99.87  ? 196 PHE   G N   1 
ATOM   12721 C  CA  . PHE   G  7  205 ? 55.447  -92.426  86.601  1.00 100.17 ? 196 PHE   G CA  1 
ATOM   12722 C  C   . PHE   G  7  205 ? 54.620  -91.688  85.540  1.00 101.20 ? 196 PHE   G C   1 
ATOM   12723 O  O   . PHE   G  7  205 ? 54.648  -90.438  85.520  1.00 102.90 ? 196 PHE   G O   1 
ATOM   12724 C  CB  . PHE   G  7  205 ? 56.680  -93.073  85.965  1.00 100.01 ? 196 PHE   G CB  1 
ATOM   12725 C  CG  . PHE   G  7  205 ? 57.510  -92.124  85.137  1.00 101.47 ? 196 PHE   G CG  1 
ATOM   12726 C  CD1 . PHE   G  7  205 ? 57.170  -91.844  83.821  1.00 103.13 ? 196 PHE   G CD1 1 
ATOM   12727 C  CD2 . PHE   G  7  205 ? 58.616  -91.491  85.680  1.00 104.31 ? 196 PHE   G CD2 1 
ATOM   12728 C  CE1 . PHE   G  7  205 ? 57.923  -90.957  83.066  1.00 104.27 ? 196 PHE   G CE1 1 
ATOM   12729 C  CE2 . PHE   G  7  205 ? 59.370  -90.607  84.923  1.00 108.11 ? 196 PHE   G CE2 1 
ATOM   12730 C  CZ  . PHE   G  7  205 ? 59.023  -90.341  83.618  1.00 107.15 ? 196 PHE   G CZ  1 
ATOM   12731 N  N   . ALA   G  7  206 ? 53.922  -92.441  84.683  1.00 98.39  ? 197 ALA   G N   1 
ATOM   12732 C  CA  . ALA   G  7  206 ? 53.100  -91.918  83.566  1.00 98.05  ? 197 ALA   G CA  1 
ATOM   12733 C  C   . ALA   G  7  206 ? 52.070  -90.917  84.104  1.00 99.33  ? 197 ALA   G C   1 
ATOM   12734 O  O   . ALA   G  7  206 ? 51.955  -89.827  83.513  1.00 102.91 ? 197 ALA   G O   1 
ATOM   12735 C  CB  . ALA   G  7  206 ? 52.430  -93.050  82.827  1.00 95.73  ? 197 ALA   G CB  1 
ATOM   12736 N  N   . ILE   G  7  207 ? 51.363  -91.270  85.184  1.00 96.69  ? 198 ILE   G N   1 
ATOM   12737 C  CA  . ILE   G  7  207 ? 50.282  -90.431  85.786  1.00 98.76  ? 198 ILE   G CA  1 
ATOM   12738 C  C   . ILE   G  7  207 ? 50.918  -89.204  86.449  1.00 105.84 ? 198 ILE   G C   1 
ATOM   12739 O  O   . ILE   G  7  207 ? 50.370  -88.093  86.274  1.00 113.62 ? 198 ILE   G O   1 
ATOM   12740 C  CB  . ILE   G  7  207 ? 49.414  -91.242  86.771  1.00 97.85  ? 198 ILE   G CB  1 
ATOM   12741 C  CG1 . ILE   G  7  207 ? 48.703  -92.402  86.067  1.00 99.50  ? 198 ILE   G CG1 1 
ATOM   12742 C  CG2 . ILE   G  7  207 ? 48.419  -90.337  87.485  1.00 95.40  ? 198 ILE   G CG2 1 
ATOM   12743 C  CD1 . ILE   G  7  207 ? 48.138  -93.447  87.003  1.00 101.17 ? 198 ILE   G CD1 1 
ATOM   12744 N  N   . THR   G  7  208 ? 52.021  -89.398  87.180  1.00 104.73 ? 199 THR   G N   1 
ATOM   12745 C  CA  . THR   G  7  208 ? 52.773  -88.320  87.882  1.00 105.56 ? 199 THR   G CA  1 
ATOM   12746 C  C   . THR   G  7  208 ? 53.175  -87.228  86.882  1.00 106.07 ? 199 THR   G C   1 
ATOM   12747 O  O   . THR   G  7  208 ? 52.899  -86.048  87.162  1.00 109.94 ? 199 THR   G O   1 
ATOM   12748 C  CB  . THR   G  7  208 ? 54.000  -88.876  88.616  1.00 100.48 ? 199 THR   G CB  1 
ATOM   12749 O  OG1 . THR   G  7  208 ? 53.527  -89.654  89.715  1.00 93.21  ? 199 THR   G OG1 1 
ATOM   12750 C  CG2 . THR   G  7  208 ? 54.924  -87.797  89.135  1.00 103.65 ? 199 THR   G CG2 1 
ATOM   12751 N  N   . HIS   G  7  209 ? 53.804  -87.609  85.767  1.00 108.11 ? 200 HIS   G N   1 
ATOM   12752 C  CA  . HIS   G  7  209 ? 54.368  -86.674  84.756  1.00 107.78 ? 200 HIS   G CA  1 
ATOM   12753 C  C   . HIS   G  7  209 ? 53.252  -86.062  83.899  1.00 111.78 ? 200 HIS   G C   1 
ATOM   12754 O  O   . HIS   G  7  209 ? 53.498  -84.984  83.322  1.00 112.83 ? 200 HIS   G O   1 
ATOM   12755 C  CB  . HIS   G  7  209 ? 55.454  -87.368  83.920  1.00 107.82 ? 200 HIS   G CB  1 
ATOM   12756 C  CG  . HIS   G  7  209 ? 56.772  -87.443  84.615  1.00 106.71 ? 200 HIS   G CG  1 
ATOM   12757 N  ND1 . HIS   G  7  209 ? 57.868  -86.717  84.194  1.00 110.36 ? 200 HIS   G ND1 1 
ATOM   12758 C  CD2 . HIS   G  7  209 ? 57.170  -88.131  85.708  1.00 103.27 ? 200 HIS   G CD2 1 
ATOM   12759 C  CE1 . HIS   G  7  209 ? 58.888  -86.962  84.990  1.00 110.92 ? 200 HIS   G CE1 1 
ATOM   12760 N  NE2 . HIS   G  7  209 ? 58.486  -87.828  85.927  1.00 105.91 ? 200 HIS   G NE2 1 
ATOM   12761 N  N   . MET   G  7  210 ? 52.081  -86.705  83.817  1.00 109.37 ? 201 MET   G N   1 
ATOM   12762 C  CA  . MET   G  7  210 ? 50.874  -86.132  83.158  1.00 112.91 ? 201 MET   G CA  1 
ATOM   12763 C  C   . MET   G  7  210 ? 50.273  -85.051  84.068  1.00 115.73 ? 201 MET   G C   1 
ATOM   12764 O  O   . MET   G  7  210 ? 49.903  -83.979  83.546  1.00 121.24 ? 201 MET   G O   1 
ATOM   12765 C  CB  . MET   G  7  210 ? 49.817  -87.199  82.851  1.00 112.95 ? 201 MET   G CB  1 
ATOM   12766 C  CG  . MET   G  7  210 ? 48.499  -86.616  82.364  1.00 116.50 ? 201 MET   G CG  1 
ATOM   12767 S  SD  . MET   G  7  210 ? 47.671  -87.650  81.138  1.00 116.49 ? 201 MET   G SD  1 
ATOM   12768 C  CE  . MET   G  7  210 ? 48.621  -87.222  79.679  1.00 124.35 ? 201 MET   G CE  1 
ATOM   12769 N  N   . ILE   G  7  211 ? 50.180  -85.323  85.373  1.00 109.41 ? 202 ILE   G N   1 
ATOM   12770 C  CA  . ILE   G  7  211 ? 49.661  -84.368  86.400  1.00 111.34 ? 202 ILE   G CA  1 
ATOM   12771 C  C   . ILE   G  7  211 ? 50.491  -83.077  86.362  1.00 115.66 ? 202 ILE   G C   1 
ATOM   12772 O  O   . ILE   G  7  211 ? 49.880  -81.990  86.355  1.00 114.86 ? 202 ILE   G O   1 
ATOM   12773 C  CB  . ILE   G  7  211 ? 49.657  -85.014  87.801  1.00 109.06 ? 202 ILE   G CB  1 
ATOM   12774 C  CG1 . ILE   G  7  211 ? 48.495  -85.999  87.955  1.00 106.46 ? 202 ILE   G CG1 1 
ATOM   12775 C  CG2 . ILE   G  7  211 ? 49.648  -83.953  88.894  1.00 110.38 ? 202 ILE   G CG2 1 
ATOM   12776 C  CD1 . ILE   G  7  211 ? 48.647  -86.963  89.109  1.00 103.34 ? 202 ILE   G CD1 1 
ATOM   12777 N  N   . ASP   G  7  212 ? 51.823  -83.198  86.347  1.00 116.83 ? 203 ASP   G N   1 
ATOM   12778 C  CA  . ASP   G  7  212 ? 52.777  -82.055  86.374  1.00 121.06 ? 203 ASP   G CA  1 
ATOM   12779 C  C   . ASP   G  7  212 ? 52.607  -81.207  85.108  1.00 125.11 ? 203 ASP   G C   1 
ATOM   12780 O  O   . ASP   G  7  212 ? 52.540  -79.965  85.238  1.00 132.11 ? 203 ASP   G O   1 
ATOM   12781 C  CB  . ASP   G  7  212 ? 54.226  -82.533  86.512  1.00 127.04 ? 203 ASP   G CB  1 
ATOM   12782 C  CG  . ASP   G  7  212 ? 54.512  -83.302  87.793  1.00 128.47 ? 203 ASP   G CG  1 
ATOM   12783 O  OD1 . ASP   G  7  212 ? 53.652  -83.284  88.698  1.00 134.30 ? 203 ASP   G OD1 1 
ATOM   12784 O  OD2 . ASP   G  7  212 ? 55.591  -83.922  87.873  1.00 136.46 ? 203 ASP   G OD2 1 
ATOM   12785 N  N   . ALA   G  7  213 ? 52.539  -81.850  83.937  1.00 115.86 ? 204 ALA   G N   1 
ATOM   12786 C  CA  . ALA   G  7  213 ? 52.493  -81.188  82.611  1.00 116.01 ? 204 ALA   G CA  1 
ATOM   12787 C  C   . ALA   G  7  213 ? 51.135  -80.506  82.396  1.00 116.75 ? 204 ALA   G C   1 
ATOM   12788 O  O   . ALA   G  7  213 ? 51.135  -79.351  81.921  1.00 128.95 ? 204 ALA   G O   1 
ATOM   12789 C  CB  . ALA   G  7  213 ? 52.795  -82.180  81.516  1.00 113.43 ? 204 ALA   G CB  1 
ATOM   12790 N  N   . LEU   G  7  214 ? 50.027  -81.184  82.723  1.00 104.25 ? 205 LEU   G N   1 
ATOM   12791 C  CA  . LEU   G  7  214 ? 48.647  -80.653  82.537  1.00 103.79 ? 205 LEU   G CA  1 
ATOM   12792 C  C   . LEU   G  7  214 ? 48.264  -79.736  83.704  1.00 109.01 ? 205 LEU   G C   1 
ATOM   12793 O  O   . LEU   G  7  214 ? 47.396  -78.865  83.492  1.00 110.18 ? 205 LEU   G O   1 
ATOM   12794 C  CB  . LEU   G  7  214 ? 47.645  -81.806  82.418  1.00 102.12 ? 205 LEU   G CB  1 
ATOM   12795 C  CG  . LEU   G  7  214 ? 47.723  -82.660  81.151  1.00 100.75 ? 205 LEU   G CG  1 
ATOM   12796 C  CD1 . LEU   G  7  214 ? 46.526  -83.592  81.074  1.00 99.07  ? 205 LEU   G CD1 1 
ATOM   12797 C  CD2 . LEU   G  7  214 ? 47.795  -81.809  79.890  1.00 102.97 ? 205 LEU   G CD2 1 
ATOM   12798 N  N   . GLY   G  7  215 ? 48.868  -79.937  84.882  1.00 111.17 ? 206 GLY   G N   1 
ATOM   12799 C  CA  . GLY   G  7  215 ? 48.629  -79.128  86.095  1.00 115.75 ? 206 GLY   G CA  1 
ATOM   12800 C  C   . GLY   G  7  215 ? 47.279  -79.419  86.733  1.00 116.84 ? 206 GLY   G C   1 
ATOM   12801 O  O   . GLY   G  7  215 ? 46.775  -78.541  87.465  1.00 115.07 ? 206 GLY   G O   1 
ATOM   12802 N  N   . THR   G  7  216 ? 46.708  -80.601  86.476  1.00 117.12 ? 207 THR   G N   1 
ATOM   12803 C  CA  . THR   G  7  216 ? 45.396  -81.042  87.026  1.00 119.12 ? 207 THR   G CA  1 
ATOM   12804 C  C   . THR   G  7  216 ? 45.580  -82.300  87.879  1.00 118.59 ? 207 THR   G C   1 
ATOM   12805 O  O   . THR   G  7  216 ? 46.533  -83.066  87.627  1.00 114.78 ? 207 THR   G O   1 
ATOM   12806 C  CB  . THR   G  7  216 ? 44.358  -81.301  85.925  1.00 119.32 ? 207 THR   G CB  1 
ATOM   12807 O  OG1 . THR   G  7  216 ? 45.023  -81.825  84.775  1.00 119.17 ? 207 THR   G OG1 1 
ATOM   12808 C  CG2 . THR   G  7  216 ? 43.584  -80.058  85.545  1.00 118.54 ? 207 THR   G CG2 1 
ATOM   12809 N  N   . GLU   G  7  217 ? 44.681  -82.485  88.848  1.00 123.87 ? 208 GLU   G N   1 
ATOM   12810 C  CA  . GLU   G  7  217 ? 44.571  -83.695  89.702  1.00 127.24 ? 208 GLU   G CA  1 
ATOM   12811 C  C   . GLU   G  7  217 ? 43.541  -84.634  89.067  1.00 122.23 ? 208 GLU   G C   1 
ATOM   12812 O  O   . GLU   G  7  217 ? 42.599  -84.120  88.434  1.00 128.09 ? 208 GLU   G O   1 
ATOM   12813 C  CB  . GLU   G  7  217 ? 44.148  -83.300  91.117  1.00 129.86 ? 208 GLU   G CB  1 
ATOM   12814 C  CG  . GLU   G  7  217 ? 44.762  -84.171  92.194  1.00 131.93 ? 208 GLU   G CG  1 
ATOM   12815 C  CD  . GLU   G  7  217 ? 46.151  -83.728  92.615  1.00 133.32 ? 208 GLU   G CD  1 
ATOM   12816 O  OE1 . GLU   G  7  217 ? 46.267  -82.627  93.187  1.00 134.56 ? 208 GLU   G OE1 1 
ATOM   12817 O  OE2 . GLU   G  7  217 ? 47.114  -84.475  92.355  1.00 133.74 ? 208 GLU   G OE2 1 
ATOM   12818 N  N   . PHE   G  7  218 ? 43.709  -85.948  89.230  1.00 118.88 ? 209 PHE   G N   1 
ATOM   12819 C  CA  . PHE   G  7  218 ? 42.828  -86.982  88.624  1.00 115.18 ? 209 PHE   G CA  1 
ATOM   12820 C  C   . PHE   G  7  218 ? 42.217  -87.869  89.710  1.00 111.79 ? 209 PHE   G C   1 
ATOM   12821 O  O   . PHE   G  7  218 ? 42.960  -88.347  90.591  1.00 105.71 ? 209 PHE   G O   1 
ATOM   12822 C  CB  . PHE   G  7  218 ? 43.599  -87.851  87.630  1.00 113.24 ? 209 PHE   G CB  1 
ATOM   12823 C  CG  . PHE   G  7  218 ? 44.170  -87.100  86.456  1.00 116.25 ? 209 PHE   G CG  1 
ATOM   12824 C  CD1 . PHE   G  7  218 ? 43.335  -86.474  85.542  1.00 120.24 ? 209 PHE   G CD1 1 
ATOM   12825 C  CD2 . PHE   G  7  218 ? 45.540  -87.022  86.265  1.00 115.58 ? 209 PHE   G CD2 1 
ATOM   12826 C  CE1 . PHE   G  7  218 ? 43.861  -85.781  84.462  1.00 124.72 ? 209 PHE   G CE1 1 
ATOM   12827 C  CE2 . PHE   G  7  218 ? 46.064  -86.330  85.185  1.00 121.13 ? 209 PHE   G CE2 1 
ATOM   12828 C  CZ  . PHE   G  7  218 ? 45.225  -85.711  84.285  1.00 124.31 ? 209 PHE   G CZ  1 
ATOM   12829 N  N   . SER   G  7  219 ? 40.899  -88.077  89.630  1.00 115.65 ? 210 SER   G N   1 
ATOM   12830 C  CA  . SER   G  7  219 ? 40.163  -89.164  90.324  1.00 117.19 ? 210 SER   G CA  1 
ATOM   12831 C  C   . SER   G  7  219 ? 40.298  -90.443  89.490  1.00 114.86 ? 210 SER   G C   1 
ATOM   12832 O  O   . SER   G  7  219 ? 40.818  -90.360  88.358  1.00 121.61 ? 210 SER   G O   1 
ATOM   12833 C  CB  . SER   G  7  219 ? 38.718  -88.792  90.565  1.00 120.06 ? 210 SER   G CB  1 
ATOM   12834 O  OG  . SER   G  7  219 ? 37.963  -88.856  89.366  1.00 122.89 ? 210 SER   G OG  1 
ATOM   12835 N  N   . LYS   G  7  220 ? 39.851  -91.580  90.027  1.00 114.36 ? 211 LYS   G N   1 
ATOM   12836 C  CA  . LYS   G  7  220 ? 39.981  -92.917  89.381  1.00 112.34 ? 211 LYS   G CA  1 
ATOM   12837 C  C   . LYS   G  7  220 ? 39.202  -92.968  88.058  1.00 110.62 ? 211 LYS   G C   1 
ATOM   12838 O  O   . LYS   G  7  220 ? 39.529  -93.839  87.232  1.00 109.09 ? 211 LYS   G O   1 
ATOM   12839 C  CB  . LYS   G  7  220 ? 39.497  -94.025  90.323  1.00 112.00 ? 211 LYS   G CB  1 
ATOM   12840 C  CG  . LYS   G  7  220 ? 38.046  -93.918  90.776  1.00 113.72 ? 211 LYS   G CG  1 
ATOM   12841 C  CD  . LYS   G  7  220 ? 37.629  -95.002  91.748  1.00 116.17 ? 211 LYS   G CD  1 
ATOM   12842 C  CE  . LYS   G  7  220 ? 36.191  -94.857  92.200  1.00 114.35 ? 211 LYS   G CE  1 
ATOM   12843 N  NZ  . LYS   G  7  220 ? 35.791  -95.941  93.127  1.00 113.75 ? 211 LYS   G NZ  1 
ATOM   12844 N  N   . ASN   G  7  221 ? 38.215  -92.085  87.865  1.00 106.64 ? 212 ASN   G N   1 
ATOM   12845 C  CA  . ASN   G  7  221 ? 37.301  -92.095  86.690  1.00 106.15 ? 212 ASN   G CA  1 
ATOM   12846 C  C   . ASN   G  7  221 ? 37.742  -91.054  85.654  1.00 105.63 ? 212 ASN   G C   1 
ATOM   12847 O  O   . ASN   G  7  221 ? 37.096  -90.997  84.590  1.00 105.37 ? 212 ASN   G O   1 
ATOM   12848 C  CB  . ASN   G  7  221 ? 35.850  -91.857  87.112  1.00 108.34 ? 212 ASN   G CB  1 
ATOM   12849 C  CG  . ASN   G  7  221 ? 35.434  -92.734  88.275  1.00 106.98 ? 212 ASN   G CG  1 
ATOM   12850 O  OD1 . ASN   G  7  221 ? 35.339  -93.952  88.138  1.00 102.63 ? 212 ASN   G OD1 1 
ATOM   12851 N  ND2 . ASN   G  7  221 ? 35.194  -92.126  89.425  1.00 111.02 ? 212 ASN   G ND2 1 
ATOM   12852 N  N   . ASP   G  7  222 ? 38.789  -90.273  85.947  1.00 109.13 ? 213 ASP   G N   1 
ATOM   12853 C  CA  . ASP   G  7  222 ? 39.328  -89.220  85.042  1.00 111.59 ? 213 ASP   G CA  1 
ATOM   12854 C  C   . ASP   G  7  222 ? 40.402  -89.820  84.128  1.00 105.82 ? 213 ASP   G C   1 
ATOM   12855 O  O   . ASP   G  7  222 ? 40.810  -89.119  83.180  1.00 110.30 ? 213 ASP   G O   1 
ATOM   12856 C  CB  . ASP   G  7  222 ? 39.912  -88.033  85.817  1.00 115.78 ? 213 ASP   G CB  1 
ATOM   12857 C  CG  . ASP   G  7  222 ? 38.925  -87.321  86.728  1.00 116.95 ? 213 ASP   G CG  1 
ATOM   12858 O  OD1 . ASP   G  7  222 ? 37.707  -87.416  86.471  1.00 120.24 ? 213 ASP   G OD1 1 
ATOM   12859 O  OD2 . ASP   G  7  222 ? 39.384  -86.674  87.691  1.00 117.76 ? 213 ASP   G OD2 1 
ATOM   12860 N  N   . LEU   G  7  223 ? 40.843  -91.055  84.396  1.00 100.80 ? 214 LEU   G N   1 
ATOM   12861 C  CA  . LEU   G  7  223 ? 41.967  -91.696  83.663  1.00 100.73 ? 214 LEU   G CA  1 
ATOM   12862 C  C   . LEU   G  7  223 ? 41.551  -93.032  83.042  1.00 98.41  ? 214 LEU   G C   1 
ATOM   12863 O  O   . LEU   G  7  223 ? 40.519  -93.610  83.440  1.00 97.96  ? 214 LEU   G O   1 
ATOM   12864 C  CB  . LEU   G  7  223 ? 43.148  -91.913  84.612  1.00 101.49 ? 214 LEU   G CB  1 
ATOM   12865 C  CG  . LEU   G  7  223 ? 44.073  -90.717  84.823  1.00 103.61 ? 214 LEU   G CG  1 
ATOM   12866 C  CD1 . LEU   G  7  223 ? 45.204  -91.099  85.759  1.00 103.64 ? 214 LEU   G CD1 1 
ATOM   12867 C  CD2 . LEU   G  7  223 ? 44.632  -90.190  83.506  1.00 107.33 ? 214 LEU   G CD2 1 
ATOM   12868 N  N   . GLU   G  7  224 ? 42.389  -93.486  82.111  1.00 96.39  ? 215 GLU   G N   1 
ATOM   12869 C  CA  . GLU   G  7  224 ? 42.277  -94.746  81.341  1.00 97.48  ? 215 GLU   G CA  1 
ATOM   12870 C  C   . GLU   G  7  224 ? 43.703  -95.263  81.132  1.00 95.52  ? 215 GLU   G C   1 
ATOM   12871 O  O   . GLU   G  7  224 ? 44.533  -94.476  80.638  1.00 98.78  ? 215 GLU   G O   1 
ATOM   12872 C  CB  . GLU   G  7  224 ? 41.573  -94.458  80.015  1.00 98.04  ? 215 GLU   G CB  1 
ATOM   12873 C  CG  . GLU   G  7  224 ? 41.142  -95.701  79.267  1.00 103.42 ? 215 GLU   G CG  1 
ATOM   12874 C  CD  . GLU   G  7  224 ? 40.246  -95.434  78.071  1.00 104.75 ? 215 GLU   G CD  1 
ATOM   12875 O  OE1 . GLU   G  7  224 ? 40.215  -94.282  77.588  1.00 108.17 ? 215 GLU   G OE1 1 
ATOM   12876 O  OE2 . GLU   G  7  224 ? 39.582  -96.382  77.625  1.00 114.50 ? 215 GLU   G OE2 1 
ATOM   12877 N  N   . VAL   G  7  225 ? 43.996  -96.505  81.527  1.00 92.55  ? 216 VAL   G N   1 
ATOM   12878 C  CA  . VAL   G  7  225 ? 45.385  -97.054  81.512  1.00 92.64  ? 216 VAL   G CA  1 
ATOM   12879 C  C   . VAL   G  7  225 ? 45.400  -98.385  80.758  1.00 90.82  ? 216 VAL   G C   1 
ATOM   12880 O  O   . VAL   G  7  225 ? 44.619  -99.281  81.120  1.00 90.70  ? 216 VAL   G O   1 
ATOM   12881 C  CB  . VAL   G  7  225 ? 45.957  -97.224  82.932  1.00 92.38  ? 216 VAL   G CB  1 
ATOM   12882 C  CG1 . VAL   G  7  225 ? 47.417  -97.656  82.899  1.00 92.33  ? 216 VAL   G CG1 1 
ATOM   12883 C  CG2 . VAL   G  7  225 ? 45.793  -95.961  83.763  1.00 93.93  ? 216 VAL   G CG2 1 
ATOM   12884 N  N   . GLY   G  7  226 ? 46.270  -98.478  79.751  1.00 93.35  ? 217 GLY   G N   1 
ATOM   12885 C  CA  . GLY   G  7  226 ? 46.666  -99.730  79.084  1.00 94.29  ? 217 GLY   G CA  1 
ATOM   12886 C  C   . GLY   G  7  226 ? 48.092  -100.092 79.456  1.00 97.19  ? 217 GLY   G C   1 
ATOM   12887 O  O   . GLY   G  7  226 ? 48.919  -99.163  79.588  1.00 93.64  ? 217 GLY   G O   1 
ATOM   12888 N  N   . VAL   G  7  227 ? 48.365  -101.387 79.646  1.00 97.39  ? 218 VAL   G N   1 
ATOM   12889 C  CA  . VAL   G  7  227 ? 49.720  -101.921 79.973  1.00 94.16  ? 218 VAL   G CA  1 
ATOM   12890 C  C   . VAL   G  7  227 ? 50.012  -103.108 79.052  1.00 93.54  ? 218 VAL   G C   1 
ATOM   12891 O  O   . VAL   G  7  227 ? 49.212  -104.063 79.051  1.00 94.45  ? 218 VAL   G O   1 
ATOM   12892 C  CB  . VAL   G  7  227 ? 49.832  -102.327 81.454  1.00 94.57  ? 218 VAL   G CB  1 
ATOM   12893 C  CG1 . VAL   G  7  227 ? 51.264  -102.683 81.824  1.00 93.92  ? 218 VAL   G CG1 1 
ATOM   12894 C  CG2 . VAL   G  7  227 ? 49.295  -101.243 82.379  1.00 96.63  ? 218 VAL   G CG2 1 
ATOM   12895 N  N   . ALA   G  7  228 ? 51.111  -103.027 78.297  1.00 93.39  ? 219 ALA   G N   1 
ATOM   12896 C  CA  . ALA   G  7  228 ? 51.670  -104.125 77.476  1.00 92.26  ? 219 ALA   G CA  1 
ATOM   12897 C  C   . ALA   G  7  228 ? 52.844  -104.759 78.225  1.00 92.04  ? 219 ALA   G C   1 
ATOM   12898 O  O   . ALA   G  7  228 ? 53.801  -104.030 78.528  1.00 91.97  ? 219 ALA   G O   1 
ATOM   12899 C  CB  . ALA   G  7  228 ? 52.107  -103.600 76.132  1.00 92.10  ? 219 ALA   G CB  1 
ATOM   12900 N  N   . THR   G  7  229 ? 52.751  -106.057 78.525  1.00 95.00  ? 220 THR   G N   1 
ATOM   12901 C  CA  . THR   G  7  229 ? 53.865  -106.905 79.032  1.00 98.18  ? 220 THR   G CA  1 
ATOM   12902 C  C   . THR   G  7  229 ? 54.139  -108.008 78.007  1.00 99.72  ? 220 THR   G C   1 
ATOM   12903 O  O   . THR   G  7  229 ? 53.405  -108.066 76.997  1.00 100.56 ? 220 THR   G O   1 
ATOM   12904 C  CB  . THR   G  7  229 ? 53.551  -107.492 80.413  1.00 100.33 ? 220 THR   G CB  1 
ATOM   12905 O  OG1 . THR   G  7  229 ? 52.344  -108.250 80.315  1.00 100.16 ? 220 THR   G OG1 1 
ATOM   12906 C  CG2 . THR   G  7  229 ? 53.420  -106.425 81.478  1.00 102.72 ? 220 THR   G CG2 1 
ATOM   12907 N  N   . LYS   G  7  230 ? 55.154  -108.840 78.251  1.00 102.87 ? 221 LYS   G N   1 
ATOM   12908 C  CA  . LYS   G  7  230 ? 55.475  -109.998 77.376  1.00 106.76 ? 221 LYS   G CA  1 
ATOM   12909 C  C   . LYS   G  7  230 ? 54.250  -110.919 77.312  1.00 107.27 ? 221 LYS   G C   1 
ATOM   12910 O  O   . LYS   G  7  230 ? 53.787  -111.366 78.381  1.00 108.40 ? 221 LYS   G O   1 
ATOM   12911 C  CB  . LYS   G  7  230 ? 56.707  -110.759 77.874  1.00 110.02 ? 221 LYS   G CB  1 
ATOM   12912 C  CG  . LYS   G  7  230 ? 57.359  -111.640 76.817  1.00 112.19 ? 221 LYS   G CG  1 
ATOM   12913 C  CD  . LYS   G  7  230 ? 58.134  -112.819 77.364  1.00 115.47 ? 221 LYS   G CD  1 
ATOM   12914 C  CE  . LYS   G  7  230 ? 58.541  -113.786 76.272  1.00 114.81 ? 221 LYS   G CE  1 
ATOM   12915 N  NZ  . LYS   G  7  230 ? 59.235  -114.978 76.810  1.00 117.55 ? 221 LYS   G NZ  1 
ATOM   12916 N  N   . ASP   G  7  231 ? 53.727  -111.142 76.103  1.00 109.36 ? 222 ASP   G N   1 
ATOM   12917 C  CA  . ASP   G  7  231 ? 52.685  -112.154 75.773  1.00 116.94 ? 222 ASP   G CA  1 
ATOM   12918 C  C   . ASP   G  7  231 ? 51.277  -111.693 76.183  1.00 114.77 ? 222 ASP   G C   1 
ATOM   12919 O  O   . ASP   G  7  231 ? 50.352  -112.512 76.011  1.00 120.47 ? 222 ASP   G O   1 
ATOM   12920 C  CB  . ASP   G  7  231 ? 53.005  -113.521 76.390  1.00 123.59 ? 222 ASP   G CB  1 
ATOM   12921 C  CG  . ASP   G  7  231 ? 54.169  -114.233 75.722  1.00 132.91 ? 222 ASP   G CG  1 
ATOM   12922 O  OD1 . ASP   G  7  231 ? 54.212  -114.243 74.475  1.00 139.32 ? 222 ASP   G OD1 1 
ATOM   12923 O  OD2 . ASP   G  7  231 ? 55.023  -114.775 76.455  1.00 142.95 ? 222 ASP   G OD2 1 
ATOM   12924 N  N   . LYS   G  7  232 ? 51.084  -110.459 76.671  1.00 112.35 ? 223 LYS   G N   1 
ATOM   12925 C  CA  . LYS   G  7  232 ? 49.714  -109.890 76.831  1.00 109.74 ? 223 LYS   G CA  1 
ATOM   12926 C  C   . LYS   G  7  232 ? 49.730  -108.368 77.037  1.00 105.30 ? 223 LYS   G C   1 
ATOM   12927 O  O   . LYS   G  7  232 ? 50.607  -107.866 77.769  1.00 106.57 ? 223 LYS   G O   1 
ATOM   12928 C  CB  . LYS   G  7  232 ? 48.946  -110.566 77.972  1.00 115.24 ? 223 LYS   G CB  1 
ATOM   12929 C  CG  . LYS   G  7  232 ? 49.553  -110.446 79.363  1.00 118.81 ? 223 LYS   G CG  1 
ATOM   12930 C  CD  . LYS   G  7  232 ? 48.794  -111.249 80.400  1.00 125.01 ? 223 LYS   G CD  1 
ATOM   12931 C  CE  . LYS   G  7  232 ? 47.398  -110.722 80.663  1.00 131.31 ? 223 LYS   G CE  1 
ATOM   12932 N  NZ  . LYS   G  7  232 ? 46.566  -111.714 81.384  1.00 136.33 ? 223 LYS   G NZ  1 
ATOM   12933 N  N   . PHE   G  7  233 ? 48.767  -107.685 76.402  1.00 100.30 ? 224 PHE   G N   1 
ATOM   12934 C  CA  . PHE   G  7  233 ? 48.360  -106.277 76.651  1.00 95.41  ? 224 PHE   G CA  1 
ATOM   12935 C  C   . PHE   G  7  233 ? 46.975  -106.263 77.310  1.00 89.82  ? 224 PHE   G C   1 
ATOM   12936 O  O   . PHE   G  7  233 ? 46.047  -106.864 76.746  1.00 89.33  ? 224 PHE   G O   1 
ATOM   12937 C  CB  . PHE   G  7  233 ? 48.304  -105.471 75.350  1.00 94.90  ? 224 PHE   G CB  1 
ATOM   12938 C  CG  . PHE   G  7  233 ? 47.609  -104.139 75.491  1.00 94.09  ? 224 PHE   G CG  1 
ATOM   12939 C  CD1 . PHE   G  7  233 ? 48.310  -103.013 75.895  1.00 93.67  ? 224 PHE   G CD1 1 
ATOM   12940 C  CD2 . PHE   G  7  233 ? 46.246  -104.017 75.258  1.00 95.84  ? 224 PHE   G CD2 1 
ATOM   12941 C  CE1 . PHE   G  7  233 ? 47.670  -101.792 76.042  1.00 92.98  ? 224 PHE   G CE1 1 
ATOM   12942 C  CE2 . PHE   G  7  233 ? 45.605  -102.796 75.411  1.00 94.92  ? 224 PHE   G CE2 1 
ATOM   12943 C  CZ  . PHE   G  7  233 ? 46.319  -101.685 75.801  1.00 94.53  ? 224 PHE   G CZ  1 
ATOM   12944 N  N   . PHE   G  7  234 ? 46.833  -105.559 78.437  1.00 90.85  ? 225 PHE   G N   1 
ATOM   12945 C  CA  . PHE   G  7  234 ? 45.575  -105.455 79.225  1.00 93.40  ? 225 PHE   G CA  1 
ATOM   12946 C  C   . PHE   G  7  234 ? 45.330  -103.998 79.637  1.00 93.58  ? 225 PHE   G C   1 
ATOM   12947 O  O   . PHE   G  7  234 ? 46.311  -103.232 79.782  1.00 91.12  ? 225 PHE   G O   1 
ATOM   12948 C  CB  . PHE   G  7  234 ? 45.641  -106.359 80.459  1.00 92.34  ? 225 PHE   G CB  1 
ATOM   12949 C  CG  . PHE   G  7  234 ? 46.837  -106.129 81.350  1.00 91.76  ? 225 PHE   G CG  1 
ATOM   12950 C  CD1 . PHE   G  7  234 ? 48.046  -106.759 81.096  1.00 90.46  ? 225 PHE   G CD1 1 
ATOM   12951 C  CD2 . PHE   G  7  234 ? 46.755  -105.277 82.442  1.00 94.18  ? 225 PHE   G CD2 1 
ATOM   12952 C  CE1 . PHE   G  7  234 ? 49.145  -106.543 81.914  1.00 90.41  ? 225 PHE   G CE1 1 
ATOM   12953 C  CE2 . PHE   G  7  234 ? 47.855  -105.063 83.261  1.00 94.00  ? 225 PHE   G CE2 1 
ATOM   12954 C  CZ  . PHE   G  7  234 ? 49.048  -105.696 82.995  1.00 91.93  ? 225 PHE   G CZ  1 
ATOM   12955 N  N   . THR   G  7  235 ? 44.053  -103.639 79.816  1.00 96.64  ? 226 THR   G N   1 
ATOM   12956 C  CA  . THR   G  7  235 ? 43.591  -102.337 80.373  1.00 92.80  ? 226 THR   G CA  1 
ATOM   12957 C  C   . THR   G  7  235 ? 43.310  -102.512 81.870  1.00 94.30  ? 226 THR   G C   1 
ATOM   12958 O  O   . THR   G  7  235 ? 42.955  -103.634 82.274  1.00 89.19  ? 226 THR   G O   1 
ATOM   12959 C  CB  . THR   G  7  235 ? 42.351  -101.805 79.642  1.00 93.35  ? 226 THR   G CB  1 
ATOM   12960 O  OG1 . THR   G  7  235 ? 41.265  -102.703 79.872  1.00 95.90  ? 226 THR   G OG1 1 
ATOM   12961 C  CG2 . THR   G  7  235 ? 42.564  -101.626 78.154  1.00 93.93  ? 226 THR   G CG2 1 
ATOM   12962 N  N   . LEU   G  7  236 ? 43.461  -101.439 82.652  1.00 92.87  ? 227 LEU   G N   1 
ATOM   12963 C  CA  . LEU   G  7  236 ? 43.236  -101.429 84.122  1.00 93.89  ? 227 LEU   G CA  1 
ATOM   12964 C  C   . LEU   G  7  236 ? 41.787  -101.035 84.419  1.00 95.52  ? 227 LEU   G C   1 
ATOM   12965 O  O   . LEU   G  7  236 ? 41.237  -100.192 83.689  1.00 96.56  ? 227 LEU   G O   1 
ATOM   12966 C  CB  . LEU   G  7  236 ? 44.194  -100.434 84.782  1.00 94.28  ? 227 LEU   G CB  1 
ATOM   12967 C  CG  . LEU   G  7  236 ? 45.687  -100.733 84.657  1.00 95.68  ? 227 LEU   G CG  1 
ATOM   12968 C  CD1 . LEU   G  7  236 ? 46.488  -99.788  85.539  1.00 97.89  ? 227 LEU   G CD1 1 
ATOM   12969 C  CD2 . LEU   G  7  236 ? 46.006  -102.175 85.017  1.00 95.91  ? 227 LEU   G CD2 1 
ATOM   12970 N  N   . SER   G  7  237 ? 41.212  -101.606 85.477  1.00 98.49  ? 228 SER   G N   1 
ATOM   12971 C  CA  . SER   G  7  237 ? 39.886  -101.228 86.027  1.00 101.78 ? 228 SER   G CA  1 
ATOM   12972 C  C   . SER   G  7  237 ? 40.031  -99.908  86.786  1.00 103.57 ? 228 SER   G C   1 
ATOM   12973 O  O   . SER   G  7  237 ? 41.182  -99.477  87.005  1.00 101.17 ? 228 SER   G O   1 
ATOM   12974 C  CB  . SER   G  7  237 ? 39.333  -102.305 86.920  1.00 104.26 ? 228 SER   G CB  1 
ATOM   12975 O  OG  . SER   G  7  237 ? 40.089  -102.408 88.119  1.00 106.83 ? 228 SER   G OG  1 
ATOM   12976 N  N   . ALA   G  7  238 ? 38.908  -99.305  87.184  1.00 109.13 ? 229 ALA   G N   1 
ATOM   12977 C  CA  . ALA   G  7  238 ? 38.866  -98.068  87.998  1.00 115.24 ? 229 ALA   G CA  1 
ATOM   12978 C  C   . ALA   G  7  238 ? 39.623  -98.305  89.312  1.00 117.86 ? 229 ALA   G C   1 
ATOM   12979 O  O   . ALA   G  7  238 ? 40.359  -97.399  89.745  1.00 123.38 ? 229 ALA   G O   1 
ATOM   12980 C  CB  . ALA   G  7  238 ? 37.435  -97.649  88.240  1.00 116.43 ? 229 ALA   G CB  1 
ATOM   12981 N  N   . GLU   G  7  239 ? 39.469  -99.493  89.904  1.00 116.20 ? 230 GLU   G N   1 
ATOM   12982 C  CA  . GLU   G  7  239 ? 40.071  -99.853  91.218  1.00 118.81 ? 230 GLU   G CA  1 
ATOM   12983 C  C   . GLU   G  7  239 ? 41.571  -100.132 91.062  1.00 112.73 ? 230 GLU   G C   1 
ATOM   12984 O  O   . GLU   G  7  239 ? 42.306  -99.904  92.041  1.00 115.20 ? 230 GLU   G O   1 
ATOM   12985 C  CB  . GLU   G  7  239 ? 39.338  -101.039 91.848  1.00 124.03 ? 230 GLU   G CB  1 
ATOM   12986 C  CG  . GLU   G  7  239 ? 38.270  -100.616 92.840  1.00 132.11 ? 230 GLU   G CG  1 
ATOM   12987 C  CD  . GLU   G  7  239 ? 37.248  -99.639  92.284  1.00 135.60 ? 230 GLU   G CD  1 
ATOM   12988 O  OE1 . GLU   G  7  239 ? 36.630  -99.960  91.249  1.00 144.50 ? 230 GLU   G OE1 1 
ATOM   12989 O  OE2 . GLU   G  7  239 ? 37.088  -98.552  92.876  1.00 141.79 ? 230 GLU   G OE2 1 
ATOM   12990 N  N   . ASN   G  7  240 ? 42.009  -100.615 89.897  1.00 110.12 ? 231 ASN   G N   1 
ATOM   12991 C  CA  . ASN   G  7  240 ? 43.450  -100.809 89.581  1.00 111.40 ? 231 ASN   G CA  1 
ATOM   12992 C  C   . ASN   G  7  240 ? 44.131  -99.439  89.510  1.00 110.47 ? 231 ASN   G C   1 
ATOM   12993 O  O   . ASN   G  7  240 ? 45.260  -99.316  90.020  1.00 114.40 ? 231 ASN   G O   1 
ATOM   12994 C  CB  . ASN   G  7  240 ? 43.665  -101.576 88.274  1.00 111.29 ? 231 ASN   G CB  1 
ATOM   12995 C  CG  . ASN   G  7  240 ? 43.190  -103.014 88.326  1.00 111.27 ? 231 ASN   G CG  1 
ATOM   12996 O  OD1 . ASN   G  7  240 ? 42.506  -103.475 87.414  1.00 105.10 ? 231 ASN   G OD1 1 
ATOM   12997 N  ND2 . ASN   G  7  240 ? 43.547  -103.735 89.377  1.00 112.96 ? 231 ASN   G ND2 1 
ATOM   12998 N  N   . ILE   G  7  241 ? 43.464  -98.457  88.896  1.00 110.28 ? 232 ILE   G N   1 
ATOM   12999 C  CA  . ILE   G  7  241 ? 43.952  -97.050  88.772  1.00 112.29 ? 232 ILE   G CA  1 
ATOM   13000 C  C   . ILE   G  7  241 ? 43.901  -96.396  90.159  1.00 112.84 ? 232 ILE   G C   1 
ATOM   13001 O  O   . ILE   G  7  241 ? 44.871  -95.698  90.505  1.00 114.04 ? 232 ILE   G O   1 
ATOM   13002 C  CB  . ILE   G  7  241 ? 43.143  -96.264  87.716  1.00 110.05 ? 232 ILE   G CB  1 
ATOM   13003 C  CG1 . ILE   G  7  241 ? 43.314  -96.859  86.315  1.00 108.65 ? 232 ILE   G CG1 1 
ATOM   13004 C  CG2 . ILE   G  7  241 ? 43.507  -94.785  87.738  1.00 111.97 ? 232 ILE   G CG2 1 
ATOM   13005 C  CD1 . ILE   G  7  241 ? 42.316  -96.350  85.297  1.00 106.96 ? 232 ILE   G CD1 1 
ATOM   13006 N  N   . GLU   G  7  242 ? 42.818  -96.619  90.915  1.00 115.38 ? 233 GLU   G N   1 
ATOM   13007 C  CA  . GLU   G  7  242 ? 42.596  -96.046  92.274  1.00 117.86 ? 233 GLU   G CA  1 
ATOM   13008 C  C   . GLU   G  7  242 ? 43.716  -96.511  93.213  1.00 117.07 ? 233 GLU   G C   1 
ATOM   13009 O  O   . GLU   G  7  242 ? 44.231  -95.676  93.982  1.00 115.52 ? 233 GLU   G O   1 
ATOM   13010 C  CB  . GLU   G  7  242 ? 41.224  -96.456  92.817  1.00 120.32 ? 233 GLU   G CB  1 
ATOM   13011 C  CG  . GLU   G  7  242 ? 40.963  -96.009  94.247  1.00 125.04 ? 233 GLU   G CG  1 
ATOM   13012 C  CD  . GLU   G  7  242 ? 41.075  -94.514  94.485  1.00 127.08 ? 233 GLU   G CD  1 
ATOM   13013 O  OE1 . GLU   G  7  242 ? 41.658  -94.127  95.516  1.00 131.05 ? 233 GLU   G OE1 1 
ATOM   13014 O  OE2 . GLU   G  7  242 ? 40.575  -93.744  93.642  1.00 129.99 ? 233 GLU   G OE2 1 
ATOM   13015 N  N   . GLU   G  7  243 ? 44.058  -97.800  93.153  1.00 117.39 ? 234 GLU   G N   1 
ATOM   13016 C  CA  . GLU   G  7  243 ? 45.191  -98.417  93.894  1.00 120.27 ? 234 GLU   G CA  1 
ATOM   13017 C  C   . GLU   G  7  243 ? 46.482  -97.674  93.528  1.00 111.94 ? 234 GLU   G C   1 
ATOM   13018 O  O   . GLU   G  7  243 ? 47.315  -97.460  94.426  1.00 114.59 ? 234 GLU   G O   1 
ATOM   13019 C  CB  . GLU   G  7  243 ? 45.284  -99.906  93.549  1.00 120.67 ? 234 GLU   G CB  1 
ATOM   13020 C  CG  . GLU   G  7  243 ? 46.163  -100.710 94.491  1.00 127.39 ? 234 GLU   G CG  1 
ATOM   13021 C  CD  . GLU   G  7  243 ? 46.300  -102.184 94.134  1.00 125.38 ? 234 GLU   G CD  1 
ATOM   13022 O  OE1 . GLU   G  7  243 ? 47.350  -102.774 94.455  1.00 129.47 ? 234 GLU   G OE1 1 
ATOM   13023 O  OE2 . GLU   G  7  243 ? 45.356  -102.744 93.539  1.00 129.98 ? 234 GLU   G OE2 1 
ATOM   13024 N  N   . ARG   G  7  244 ? 46.619  -97.291  92.255  1.00 111.31 ? 235 ARG   G N   1 
ATOM   13025 C  CA  . ARG   G  7  244 ? 47.811  -96.607  91.682  1.00 114.48 ? 235 ARG   G CA  1 
ATOM   13026 C  C   . ARG   G  7  244 ? 47.851  -95.148  92.156  1.00 115.04 ? 235 ARG   G C   1 
ATOM   13027 O  O   . ARG   G  7  244 ? 48.950  -94.676  92.502  1.00 115.41 ? 235 ARG   G O   1 
ATOM   13028 C  CB  . ARG   G  7  244 ? 47.772  -96.686  90.152  1.00 115.45 ? 235 ARG   G CB  1 
ATOM   13029 C  CG  . ARG   G  7  244 ? 49.120  -96.964  89.504  1.00 117.63 ? 235 ARG   G CG  1 
ATOM   13030 C  CD  . ARG   G  7  244 ? 49.453  -98.440  89.385  1.00 115.49 ? 235 ARG   G CD  1 
ATOM   13031 N  NE  . ARG   G  7  244 ? 50.196  -98.941  90.536  1.00 118.03 ? 235 ARG   G NE  1 
ATOM   13032 C  CZ  . ARG   G  7  244 ? 49.676  -99.612  91.562  1.00 120.90 ? 235 ARG   G CZ  1 
ATOM   13033 N  NH1 . ARG   G  7  244 ? 48.382  -99.884  91.616  1.00 124.66 ? 235 ARG   G NH1 1 
ATOM   13034 N  NH2 . ARG   G  7  244 ? 50.465  -100.013 92.544  1.00 126.29 ? 235 ARG   G NH2 1 
ATOM   13035 N  N   . LEU   G  7  245 ? 46.699  -94.466  92.151  1.00 117.07 ? 236 LEU   G N   1 
ATOM   13036 C  CA  . LEU   G  7  245 ? 46.535  -93.049  92.586  1.00 120.24 ? 236 LEU   G CA  1 
ATOM   13037 C  C   . LEU   G  7  245 ? 46.877  -92.913  94.077  1.00 124.26 ? 236 LEU   G C   1 
ATOM   13038 O  O   . LEU   G  7  245 ? 47.494  -91.890  94.447  1.00 130.17 ? 236 LEU   G O   1 
ATOM   13039 C  CB  . LEU   G  7  245 ? 45.095  -92.594  92.310  1.00 114.29 ? 236 LEU   G CB  1 
ATOM   13040 C  CG  . LEU   G  7  245 ? 44.874  -91.665  91.113  1.00 113.37 ? 236 LEU   G CG  1 
ATOM   13041 C  CD1 . LEU   G  7  245 ? 45.876  -91.901  89.989  1.00 111.51 ? 236 LEU   G CD1 1 
ATOM   13042 C  CD2 . LEU   G  7  245 ? 43.450  -91.798  90.590  1.00 115.70 ? 236 LEU   G CD2 1 
ATOM   13043 N  N   . VAL   G  7  246 ? 46.480  -93.892  94.897  1.00 124.73 ? 237 VAL   G N   1 
ATOM   13044 C  CA  . VAL   G  7  246 ? 46.758  -93.930  96.365  1.00 122.85 ? 237 VAL   G CA  1 
ATOM   13045 C  C   . VAL   G  7  246 ? 48.274  -93.999  96.588  1.00 121.18 ? 237 VAL   G C   1 
ATOM   13046 O  O   . VAL   G  7  246 ? 48.769  -93.283  97.482  1.00 120.63 ? 237 VAL   G O   1 
ATOM   13047 C  CB  . VAL   G  7  246 ? 46.031  -95.104  97.049  1.00 124.63 ? 237 VAL   G CB  1 
ATOM   13048 C  CG1 . VAL   G  7  246 ? 46.594  -95.400  98.433  1.00 124.51 ? 237 VAL   G CG1 1 
ATOM   13049 C  CG2 . VAL   G  7  246 ? 44.532  -94.860  97.128  1.00 127.38 ? 237 VAL   G CG2 1 
ATOM   13050 N  N   . ALA   G  7  247 ? 48.973  -94.831  95.809  1.00 118.35 ? 238 ALA   G N   1 
ATOM   13051 C  CA  . ALA   G  7  247 ? 50.435  -95.062  95.901  1.00 120.61 ? 238 ALA   G CA  1 
ATOM   13052 C  C   . ALA   G  7  247 ? 51.197  -93.754  95.646  1.00 121.75 ? 238 ALA   G C   1 
ATOM   13053 O  O   . ALA   G  7  247 ? 52.145  -93.471  96.408  1.00 117.95 ? 238 ALA   G O   1 
ATOM   13054 C  CB  . ALA   G  7  247 ? 50.850  -96.144  94.933  1.00 120.96 ? 238 ALA   G CB  1 
ATOM   13055 N  N   . ILE   G  7  248 ? 50.796  -92.987  94.625  1.00 119.22 ? 239 ILE   G N   1 
ATOM   13056 C  CA  . ILE   G  7  248 ? 51.423  -91.680  94.254  1.00 124.35 ? 239 ILE   G CA  1 
ATOM   13057 C  C   . ILE   G  7  248 ? 51.230  -90.694  95.414  1.00 128.90 ? 239 ILE   G C   1 
ATOM   13058 O  O   . ILE   G  7  248 ? 52.225  -90.057  95.812  1.00 133.39 ? 239 ILE   G O   1 
ATOM   13059 C  CB  . ILE   G  7  248 ? 50.851  -91.128  92.928  1.00 118.97 ? 239 ILE   G CB  1 
ATOM   13060 C  CG1 . ILE   G  7  248 ? 51.244  -92.002  91.732  1.00 117.32 ? 239 ILE   G CG1 1 
ATOM   13061 C  CG2 . ILE   G  7  248 ? 51.269  -89.677  92.718  1.00 120.25 ? 239 ILE   G CG2 1 
ATOM   13062 C  CD1 . ILE   G  7  248 ? 50.463  -91.714  90.467  1.00 113.42 ? 239 ILE   G CD1 1 
ATOM   13063 N  N   . ALA   G  7  249 ? 49.999  -90.581  95.927  1.00 136.20 ? 240 ALA   G N   1 
ATOM   13064 C  CA  . ALA   G  7  249 ? 49.589  -89.623  96.983  1.00 139.15 ? 240 ALA   G CA  1 
ATOM   13065 C  C   . ALA   G  7  249 ? 50.385  -89.869  98.272  1.00 143.76 ? 240 ALA   G C   1 
ATOM   13066 O  O   . ALA   G  7  249 ? 50.723  -88.878  98.946  1.00 146.02 ? 240 ALA   G O   1 
ATOM   13067 C  CB  . ALA   G  7  249 ? 48.103  -89.727  97.233  1.00 140.91 ? 240 ALA   G CB  1 
ATOM   13068 N  N   . GLU   G  7  250 ? 50.678  -91.134  98.593  1.00 149.91 ? 241 GLU   G N   1 
ATOM   13069 C  CA  . GLU   G  7  250 ? 51.413  -91.543  99.824  1.00 155.08 ? 241 GLU   G CA  1 
ATOM   13070 C  C   . GLU   G  7  250 ? 52.929  -91.487  99.581  1.00 153.39 ? 241 GLU   G C   1 
ATOM   13071 O  O   . GLU   G  7  250 ? 53.646  -92.343  100.136 1.00 148.03 ? 241 GLU   G O   1 
ATOM   13072 C  CB  . GLU   G  7  250 ? 50.981  -92.947  100.261 1.00 160.15 ? 241 GLU   G CB  1 
ATOM   13073 C  CG  . GLU   G  7  250 ? 49.577  -93.006  100.839 1.00 166.01 ? 241 GLU   G CG  1 
ATOM   13074 C  CD  . GLU   G  7  250 ? 49.077  -94.408  101.152 1.00 167.17 ? 241 GLU   G CD  1 
ATOM   13075 O  OE1 . GLU   G  7  250 ? 47.858  -94.566  101.361 1.00 166.97 ? 241 GLU   G OE1 1 
ATOM   13076 O  OE2 . GLU   G  7  250 ? 49.907  -95.340  101.187 1.00 168.49 ? 241 GLU   G OE2 1 
ATOM   13077 N  N   . GLN   G  7  251 ? 53.404  -90.512  98.797  1.00 154.83 ? 242 GLN   G N   1 
ATOM   13078 C  CA  . GLN   G  7  251 ? 54.850  -90.280  98.531  1.00 161.98 ? 242 GLN   G CA  1 
ATOM   13079 C  C   . GLN   G  7  251 ? 55.057  -88.831  98.074  1.00 165.01 ? 242 GLN   G C   1 
ATOM   13080 O  O   . GLN   G  7  251 ? 55.739  -88.052  98.740  1.00 175.27 ? 242 GLN   G O   1 
ATOM   13081 C  CB  . GLN   G  7  251 ? 55.365  -91.277  97.489  1.00 160.95 ? 242 GLN   G CB  1 
ATOM   13082 C  CG  . GLN   G  7  251 ? 56.807  -91.038  97.054  1.00 163.28 ? 242 GLN   G CG  1 
ATOM   13083 C  CD  . GLN   G  7  251 ? 57.817  -91.314  98.142  1.00 164.82 ? 242 GLN   G CD  1 
ATOM   13084 O  OE1 . GLN   G  7  251 ? 57.475  -91.617  99.283  1.00 163.17 ? 242 GLN   G OE1 1 
ATOM   13085 N  NE2 . GLN   G  7  251 ? 59.089  -91.213  97.790  1.00 170.52 ? 242 GLN   G NE2 1 
ATOM   13086 N  N   . THR   H  8  1   ? 66.581  -139.081 47.531  1.00 109.34 ? 2   THR   H N   1 
ATOM   13087 C  CA  . THR   H  8  1   ? 66.683  -139.386 48.980  1.00 94.48  ? 2   THR   H CA  1 
ATOM   13088 C  C   . THR   H  8  1   ? 66.945  -138.072 49.713  1.00 91.87  ? 2   THR   H C   1 
ATOM   13089 O  O   . THR   H  8  1   ? 67.894  -137.386 49.328  1.00 90.10  ? 2   THR   H O   1 
ATOM   13090 C  CB  . THR   H  8  1   ? 67.760  -140.446 49.216  1.00 93.52  ? 2   THR   H CB  1 
ATOM   13091 O  OG1 . THR   H  8  1   ? 67.247  -141.678 48.714  1.00 94.59  ? 2   THR   H OG1 1 
ATOM   13092 C  CG2 . THR   H  8  1   ? 68.106  -140.601 50.676  1.00 94.46  ? 2   THR   H CG2 1 
ATOM   13093 N  N   . ILE   H  8  2   ? 66.149  -137.762 50.738  1.00 90.53  ? 3   ILE   H N   1 
ATOM   13094 C  CA  . ILE   H  8  2   ? 66.267  -136.448 51.431  1.00 93.61  ? 3   ILE   H CA  1 
ATOM   13095 C  C   . ILE   H  8  2   ? 66.086  -136.618 52.939  1.00 91.35  ? 3   ILE   H C   1 
ATOM   13096 O  O   . ILE   H  8  2   ? 65.061  -137.185 53.335  1.00 95.08  ? 3   ILE   H O   1 
ATOM   13097 C  CB  . ILE   H  8  2   ? 65.178  -135.531 50.856  1.00 94.12  ? 3   ILE   H CB  1 
ATOM   13098 C  CG1 . ILE   H  8  2   ? 65.753  -134.521 49.868  1.00 95.27  ? 3   ILE   H CG1 1 
ATOM   13099 C  CG2 . ILE   H  8  2   ? 64.368  -134.873 51.955  1.00 98.59  ? 3   ILE   H CG2 1 
ATOM   13100 C  CD1 . ILE   H  8  2   ? 65.092  -134.574 48.526  1.00 97.76  ? 3   ILE   H CD1 1 
ATOM   13101 N  N   . VAL   H  8  3   ? 67.027  -136.095 53.732  1.00 89.37  ? 4   VAL   H N   1 
ATOM   13102 C  CA  . VAL   H  8  3   ? 66.976  -136.182 55.222  1.00 88.55  ? 4   VAL   H CA  1 
ATOM   13103 C  C   . VAL   H  8  3   ? 67.229  -134.796 55.826  1.00 89.03  ? 4   VAL   H C   1 
ATOM   13104 O  O   . VAL   H  8  3   ? 67.899  -133.964 55.179  1.00 86.46  ? 4   VAL   H O   1 
ATOM   13105 C  CB  . VAL   H  8  3   ? 67.975  -137.216 55.777  1.00 88.87  ? 4   VAL   H CB  1 
ATOM   13106 C  CG1 . VAL   H  8  3   ? 67.848  -138.557 55.072  1.00 89.28  ? 4   VAL   H CG1 1 
ATOM   13107 C  CG2 . VAL   H  8  3   ? 69.410  -136.719 55.720  1.00 88.47  ? 4   VAL   H CG2 1 
ATOM   13108 N  N   . GLY   H  8  4   ? 66.704  -134.586 57.035  1.00 89.20  ? 5   GLY   H N   1 
ATOM   13109 C  CA  . GLY   H  8  4   ? 66.973  -133.422 57.898  1.00 88.04  ? 5   GLY   H CA  1 
ATOM   13110 C  C   . GLY   H  8  4   ? 67.212  -133.878 59.324  1.00 88.14  ? 5   GLY   H C   1 
ATOM   13111 O  O   . GLY   H  8  4   ? 66.429  -134.716 59.801  1.00 88.14  ? 5   GLY   H O   1 
ATOM   13112 N  N   . VAL   H  8  5   ? 68.266  -133.373 59.969  1.00 88.35  ? 6   VAL   H N   1 
ATOM   13113 C  CA  . VAL   H  8  5   ? 68.679  -133.774 61.348  1.00 91.75  ? 6   VAL   H CA  1 
ATOM   13114 C  C   . VAL   H  8  5   ? 68.948  -132.512 62.176  1.00 91.64  ? 6   VAL   H C   1 
ATOM   13115 O  O   . VAL   H  8  5   ? 69.674  -131.621 61.691  1.00 92.44  ? 6   VAL   H O   1 
ATOM   13116 C  CB  . VAL   H  8  5   ? 69.908  -134.702 61.316  1.00 91.52  ? 6   VAL   H CB  1 
ATOM   13117 C  CG1 . VAL   H  8  5   ? 70.442  -134.992 62.711  1.00 94.39  ? 6   VAL   H CG1 1 
ATOM   13118 C  CG2 . VAL   H  8  5   ? 69.614  -136.001 60.586  1.00 91.83  ? 6   VAL   H CG2 1 
ATOM   13119 N  N   . LYS   H  8  6   ? 68.393  -132.463 63.390  1.00 92.78  ? 7   LYS   H N   1 
ATOM   13120 C  CA  . LYS   H  8  6   ? 68.577  -131.369 64.378  1.00 95.08  ? 7   LYS   H CA  1 
ATOM   13121 C  C   . LYS   H  8  6   ? 69.763  -131.730 65.278  1.00 96.72  ? 7   LYS   H C   1 
ATOM   13122 O  O   . LYS   H  8  6   ? 69.850  -132.909 65.681  1.00 93.32  ? 7   LYS   H O   1 
ATOM   13123 C  CB  . LYS   H  8  6   ? 67.294  -131.183 65.195  1.00 95.09  ? 7   LYS   H CB  1 
ATOM   13124 C  CG  . LYS   H  8  6   ? 66.202  -130.368 64.515  1.00 95.79  ? 7   LYS   H CG  1 
ATOM   13125 C  CD  . LYS   H  8  6   ? 65.980  -129.012 65.149  1.00 100.11 ? 7   LYS   H CD  1 
ATOM   13126 C  CE  . LYS   H  8  6   ? 65.215  -129.094 66.453  1.00 102.38 ? 7   LYS   H CE  1 
ATOM   13127 N  NZ  . LYS   H  8  6   ? 64.823  -127.752 66.943  1.00 104.79 ? 7   LYS   H NZ  1 
ATOM   13128 N  N   . PHE   H  8  7   ? 70.649  -130.767 65.556  1.00 97.93  ? 8   PHE   H N   1 
ATOM   13129 C  CA  . PHE   H  8  7   ? 71.760  -130.894 66.540  1.00 99.38  ? 8   PHE   H CA  1 
ATOM   13130 C  C   . PHE   H  8  7   ? 71.573  -129.810 67.612  1.00 100.78 ? 8   PHE   H C   1 
ATOM   13131 O  O   . PHE   H  8  7   ? 70.519  -129.147 67.571  1.00 101.26 ? 8   PHE   H O   1 
ATOM   13132 C  CB  . PHE   H  8  7   ? 73.110  -130.929 65.814  1.00 101.24 ? 8   PHE   H CB  1 
ATOM   13133 C  CG  . PHE   H  8  7   ? 73.545  -129.679 65.089  1.00 101.67 ? 8   PHE   H CG  1 
ATOM   13134 C  CD1 . PHE   H  8  7   ? 74.280  -128.704 65.744  1.00 106.99 ? 8   PHE   H CD1 1 
ATOM   13135 C  CD2 . PHE   H  8  7   ? 73.284  -129.507 63.737  1.00 101.30 ? 8   PHE   H CD2 1 
ATOM   13136 C  CE1 . PHE   H  8  7   ? 74.705  -127.563 65.077  1.00 108.95 ? 8   PHE   H CE1 1 
ATOM   13137 C  CE2 . PHE   H  8  7   ? 73.711  -128.367 63.070  1.00 103.98 ? 8   PHE   H CE2 1 
ATOM   13138 C  CZ  . PHE   H  8  7   ? 74.421  -127.398 63.741  1.00 107.23 ? 8   PHE   H CZ  1 
ATOM   13139 N  N   . ASN   H  8  8   ? 72.507  -129.671 68.564  1.00 105.08 ? 9   ASN   H N   1 
ATOM   13140 C  CA  . ASN   H  8  8   ? 72.341  -128.764 69.738  1.00 108.54 ? 9   ASN   H CA  1 
ATOM   13141 C  C   . ASN   H  8  8   ? 72.155  -127.320 69.259  1.00 110.03 ? 9   ASN   H C   1 
ATOM   13142 O  O   . ASN   H  8  8   ? 71.185  -126.668 69.697  1.00 110.53 ? 9   ASN   H O   1 
ATOM   13143 C  CB  . ASN   H  8  8   ? 73.520  -128.711 70.718  1.00 110.95 ? 9   ASN   H CB  1 
ATOM   13144 C  CG  . ASN   H  8  8   ? 74.336  -129.981 70.824  1.00 113.32 ? 9   ASN   H CG  1 
ATOM   13145 O  OD1 . ASN   H  8  8   ? 73.813  -131.036 71.177  1.00 117.51 ? 9   ASN   H OD1 1 
ATOM   13146 N  ND2 . ASN   H  8  8   ? 75.630  -129.870 70.561  1.00 112.83 ? 9   ASN   H ND2 1 
ATOM   13147 N  N   . ASN   H  8  9   ? 73.078  -126.841 68.418  1.00 110.38 ? 10  ASN   H N   1 
ATOM   13148 C  CA  . ASN   H  8  9   ? 73.230  -125.404 68.074  1.00 114.04 ? 10  ASN   H CA  1 
ATOM   13149 C  C   . ASN   H  8  9   ? 72.588  -125.086 66.716  1.00 113.30 ? 10  ASN   H C   1 
ATOM   13150 O  O   . ASN   H  8  9   ? 72.725  -123.927 66.273  1.00 119.84 ? 10  ASN   H O   1 
ATOM   13151 C  CB  . ASN   H  8  9   ? 74.703  -124.984 68.073  1.00 116.65 ? 10  ASN   H CB  1 
ATOM   13152 C  CG  . ASN   H  8  9   ? 74.895  -123.520 68.408  1.00 119.06 ? 10  ASN   H CG  1 
ATOM   13153 O  OD1 . ASN   H  8  9   ? 74.128  -122.950 69.182  1.00 122.08 ? 10  ASN   H OD1 1 
ATOM   13154 N  ND2 . ASN   H  8  9   ? 75.911  -122.899 67.831  1.00 121.28 ? 10  ASN   H ND2 1 
ATOM   13155 N  N   . GLY   H  8  10  ? 71.915  -126.045 66.072  1.00 104.06 ? 11  GLY   H N   1 
ATOM   13156 C  CA  . GLY   H  8  10  ? 71.256  -125.787 64.777  1.00 102.70 ? 11  GLY   H CA  1 
ATOM   13157 C  C   . GLY   H  8  10  ? 70.672  -127.029 64.131  1.00 98.73  ? 11  GLY   H C   1 
ATOM   13158 O  O   . GLY   H  8  10  ? 70.446  -128.031 64.836  1.00 100.32 ? 11  GLY   H O   1 
ATOM   13159 N  N   . VAL   H  8  11  ? 70.426  -126.940 62.822  1.00 96.56  ? 12  VAL   H N   1 
ATOM   13160 C  CA  . VAL   H  8  11  ? 69.819  -128.010 61.978  1.00 93.22  ? 12  VAL   H CA  1 
ATOM   13161 C  C   . VAL   H  8  11  ? 70.710  -128.207 60.748  1.00 93.20  ? 12  VAL   H C   1 
ATOM   13162 O  O   . VAL   H  8  11  ? 71.339  -127.229 60.299  1.00 93.79  ? 12  VAL   H O   1 
ATOM   13163 C  CB  . VAL   H  8  11  ? 68.368  -127.657 61.592  1.00 92.62  ? 12  VAL   H CB  1 
ATOM   13164 C  CG1 . VAL   H  8  11  ? 68.284  -126.365 60.795  1.00 92.81  ? 12  VAL   H CG1 1 
ATOM   13165 C  CG2 . VAL   H  8  11  ? 67.686  -128.789 60.841  1.00 91.05  ? 12  VAL   H CG2 1 
ATOM   13166 N  N   . VAL   H  8  12  ? 70.765  -129.439 60.245  1.00 92.06  ? 13  VAL   H N   1 
ATOM   13167 C  CA  . VAL   H  8  12  ? 71.527  -129.833 59.025  1.00 93.62  ? 13  VAL   H CA  1 
ATOM   13168 C  C   . VAL   H  8  12  ? 70.578  -130.632 58.131  1.00 92.43  ? 13  VAL   H C   1 
ATOM   13169 O  O   . VAL   H  8  12  ? 69.853  -131.492 58.661  1.00 92.67  ? 13  VAL   H O   1 
ATOM   13170 C  CB  . VAL   H  8  12  ? 72.795  -130.637 59.375  1.00 95.58  ? 13  VAL   H CB  1 
ATOM   13171 C  CG1 . VAL   H  8  12  ? 72.529  -131.707 60.424  1.00 95.33  ? 13  VAL   H CG1 1 
ATOM   13172 C  CG2 . VAL   H  8  12  ? 73.442  -131.252 58.141  1.00 97.09  ? 13  VAL   H CG2 1 
ATOM   13173 N  N   . ILE   H  8  13  ? 70.572  -130.334 56.832  1.00 90.74  ? 14  ILE   H N   1 
ATOM   13174 C  CA  . ILE   H  8  13  ? 69.807  -131.099 55.806  1.00 90.88  ? 14  ILE   H CA  1 
ATOM   13175 C  C   . ILE   H  8  13  ? 70.803  -131.604 54.766  1.00 90.65  ? 14  ILE   H C   1 
ATOM   13176 O  O   . ILE   H  8  13  ? 71.819  -130.918 54.524  1.00 88.66  ? 14  ILE   H O   1 
ATOM   13177 C  CB  . ILE   H  8  13  ? 68.694  -130.247 55.169  1.00 90.26  ? 14  ILE   H CB  1 
ATOM   13178 C  CG1 . ILE   H  8  13  ? 69.273  -129.168 54.249  1.00 95.23  ? 14  ILE   H CG1 1 
ATOM   13179 C  CG2 . ILE   H  8  13  ? 67.789  -129.670 56.247  1.00 89.37  ? 14  ILE   H CG2 1 
ATOM   13180 C  CD1 . ILE   H  8  13  ? 68.238  -128.337 53.527  1.00 98.28  ? 14  ILE   H CD1 1 
ATOM   13181 N  N   . ALA   H  8  14  ? 70.517  -132.773 54.198  1.00 90.47  ? 15  ALA   H N   1 
ATOM   13182 C  CA  . ALA   H  8  14  ? 71.313  -133.402 53.124  1.00 88.71  ? 15  ALA   H CA  1 
ATOM   13183 C  C   . ALA   H  8  14  ? 70.362  -134.067 52.128  1.00 84.32  ? 15  ALA   H C   1 
ATOM   13184 O  O   . ALA   H  8  14  ? 69.206  -134.360 52.495  1.00 81.62  ? 15  ALA   H O   1 
ATOM   13185 C  CB  . ALA   H  8  14  ? 72.295  -134.385 53.711  1.00 90.09  ? 15  ALA   H CB  1 
ATOM   13186 N  N   . ALA   H  8  15  ? 70.842  -134.259 50.902  1.00 83.50  ? 16  ALA   H N   1 
ATOM   13187 C  CA  . ALA   H  8  15  ? 70.112  -134.904 49.792  1.00 85.12  ? 16  ALA   H CA  1 
ATOM   13188 C  C   . ALA   H  8  15  ? 71.137  -135.533 48.846  1.00 86.62  ? 16  ALA   H C   1 
ATOM   13189 O  O   . ALA   H  8  15  ? 72.330  -135.182 48.945  1.00 88.05  ? 16  ALA   H O   1 
ATOM   13190 C  CB  . ALA   H  8  15  ? 69.240  -133.888 49.096  1.00 83.84  ? 16  ALA   H CB  1 
ATOM   13191 N  N   . ASP   H  8  16  ? 70.694  -136.442 47.978  1.00 87.77  ? 17  ASP   H N   1 
ATOM   13192 C  CA  . ASP   H  8  16  ? 71.563  -137.076 46.955  1.00 91.92  ? 17  ASP   H CA  1 
ATOM   13193 C  C   . ASP   H  8  16  ? 71.587  -136.161 45.721  1.00 94.21  ? 17  ASP   H C   1 
ATOM   13194 O  O   . ASP   H  8  16  ? 71.066  -135.031 45.815  1.00 95.48  ? 17  ASP   H O   1 
ATOM   13195 C  CB  . ASP   H  8  16  ? 71.094  -138.500 46.661  1.00 92.87  ? 17  ASP   H CB  1 
ATOM   13196 C  CG  . ASP   H  8  16  ? 69.947  -138.548 45.674  1.00 94.33  ? 17  ASP   H CG  1 
ATOM   13197 O  OD1 . ASP   H  8  16  ? 69.084  -137.651 45.745  1.00 93.66  ? 17  ASP   H OD1 1 
ATOM   13198 O  OD2 . ASP   H  8  16  ? 69.939  -139.464 44.832  1.00 96.94  ? 17  ASP   H OD2 1 
ATOM   13199 N  N   . THR   H  8  17  ? 72.158  -136.626 44.605  1.00 96.58  ? 18  THR   H N   1 
ATOM   13200 C  CA  . THR   H  8  17  ? 72.447  -135.792 43.405  1.00 98.14  ? 18  THR   H CA  1 
ATOM   13201 C  C   . THR   H  8  17  ? 71.828  -136.368 42.126  1.00 100.43 ? 18  THR   H C   1 
ATOM   13202 O  O   . THR   H  8  17  ? 72.115  -135.802 41.052  1.00 96.12  ? 18  THR   H O   1 
ATOM   13203 C  CB  . THR   H  8  17  ? 73.958  -135.635 43.200  1.00 100.64 ? 18  THR   H CB  1 
ATOM   13204 O  OG1 . THR   H  8  17  ? 74.596  -136.454 44.175  1.00 103.55 ? 18  THR   H OG1 1 
ATOM   13205 C  CG2 . THR   H  8  17  ? 74.433  -134.207 43.344  1.00 99.54  ? 18  THR   H CG2 1 
ATOM   13206 N  N   . ARG   H  8  18  ? 71.011  -137.421 42.211  1.00 101.80 ? 19  ARG   H N   1 
ATOM   13207 C  CA  . ARG   H  8  18  ? 70.480  -138.115 41.006  1.00 103.38 ? 19  ARG   H CA  1 
ATOM   13208 C  C   . ARG   H  8  18  ? 69.019  -137.727 40.753  1.00 99.17  ? 19  ARG   H C   1 
ATOM   13209 O  O   . ARG   H  8  18  ? 68.192  -137.896 41.666  1.00 98.78  ? 19  ARG   H O   1 
ATOM   13210 C  CB  . ARG   H  8  18  ? 70.578  -139.635 41.133  1.00 105.15 ? 19  ARG   H CB  1 
ATOM   13211 C  CG  . ARG   H  8  18  ? 69.810  -140.370 40.042  1.00 107.27 ? 19  ARG   H CG  1 
ATOM   13212 C  CD  . ARG   H  8  18  ? 69.566  -141.821 40.382  1.00 105.96 ? 19  ARG   H CD  1 
ATOM   13213 N  NE  . ARG   H  8  18  ? 70.722  -142.628 40.019  1.00 108.87 ? 19  ARG   H NE  1 
ATOM   13214 C  CZ  . ARG   H  8  18  ? 71.088  -143.744 40.637  1.00 112.12 ? 19  ARG   H CZ  1 
ATOM   13215 N  NH1 . ARG   H  8  18  ? 70.392  -144.195 41.668  1.00 115.72 ? 19  ARG   H NH1 1 
ATOM   13216 N  NH2 . ARG   H  8  18  ? 72.162  -144.400 40.235  1.00 114.17 ? 19  ARG   H NH2 1 
ATOM   13217 N  N   . SER   H  8  19  ? 68.724  -137.288 39.527  1.00 95.59  ? 20  SER   H N   1 
ATOM   13218 C  CA  . SER   H  8  19  ? 67.363  -136.981 39.018  1.00 93.59  ? 20  SER   H CA  1 
ATOM   13219 C  C   . SER   H  8  19  ? 67.057  -137.916 37.846  1.00 90.17  ? 20  SER   H C   1 
ATOM   13220 O  O   . SER   H  8  19  ? 67.919  -138.029 36.956  1.00 92.75  ? 20  SER   H O   1 
ATOM   13221 C  CB  . SER   H  8  19  ? 67.260  -135.544 38.600  1.00 92.39  ? 20  SER   H CB  1 
ATOM   13222 O  OG  . SER   H  8  19  ? 67.122  -135.422 37.192  1.00 94.33  ? 20  SER   H OG  1 
ATOM   13223 N  N   . THR   H  8  20  ? 65.881  -138.547 37.842  1.00 89.85  ? 21  THR   H N   1 
ATOM   13224 C  CA  . THR   H  8  20  ? 65.508  -139.585 36.846  1.00 91.87  ? 21  THR   H CA  1 
ATOM   13225 C  C   . THR   H  8  20  ? 64.187  -139.238 36.161  1.00 92.36  ? 21  THR   H C   1 
ATOM   13226 O  O   . THR   H  8  20  ? 63.344  -138.562 36.781  1.00 87.25  ? 21  THR   H O   1 
ATOM   13227 C  CB  . THR   H  8  20  ? 65.396  -140.975 37.482  1.00 94.29  ? 21  THR   H CB  1 
ATOM   13228 O  OG1 . THR   H  8  20  ? 64.358  -140.929 38.464  1.00 89.91  ? 21  THR   H OG1 1 
ATOM   13229 C  CG2 . THR   H  8  20  ? 66.696  -141.438 38.105  1.00 95.60  ? 21  THR   H CG2 1 
ATOM   13230 N  N   . GLN   H  8  21  ? 64.043  -139.722 34.926  1.00 96.72  ? 22  GLN   H N   1 
ATOM   13231 C  CA  . GLN   H  8  21  ? 62.797  -139.717 34.118  1.00 99.73  ? 22  GLN   H CA  1 
ATOM   13232 C  C   . GLN   H  8  21  ? 62.464  -141.168 33.749  1.00 97.49  ? 22  GLN   H C   1 
ATOM   13233 O  O   . GLN   H  8  21  ? 63.149  -141.728 32.867  1.00 94.84  ? 22  GLN   H O   1 
ATOM   13234 C  CB  . GLN   H  8  21  ? 63.008  -138.844 32.883  1.00 103.81 ? 22  GLN   H CB  1 
ATOM   13235 C  CG  . GLN   H  8  21  ? 61.715  -138.349 32.260  1.00 108.65 ? 22  GLN   H CG  1 
ATOM   13236 C  CD  . GLN   H  8  21  ? 61.964  -137.237 31.272  1.00 115.27 ? 22  GLN   H CD  1 
ATOM   13237 O  OE1 . GLN   H  8  21  ? 63.025  -136.613 31.261  1.00 114.21 ? 22  GLN   H OE1 1 
ATOM   13238 N  NE2 . GLN   H  8  21  ? 60.976  -136.978 30.429  1.00 121.90 ? 22  GLN   H NE2 1 
ATOM   13239 N  N   . GLY   H  8  22  ? 61.463  -141.759 34.410  1.00 96.54  ? 23  GLY   H N   1 
ATOM   13240 C  CA  . GLY   H  8  22  ? 61.199  -143.209 34.356  1.00 96.24  ? 23  GLY   H CA  1 
ATOM   13241 C  C   . GLY   H  8  22  ? 62.372  -143.989 34.949  1.00 94.94  ? 23  GLY   H C   1 
ATOM   13242 O  O   . GLY   H  8  22  ? 62.768  -143.728 36.084  1.00 89.19  ? 23  GLY   H O   1 
ATOM   13243 N  N   . PRO   H  8  23  ? 62.972  -144.950 34.204  1.00 95.39  ? 24  PRO   H N   1 
ATOM   13244 C  CA  . PRO   H  8  23  ? 64.164  -145.665 34.663  1.00 95.70  ? 24  PRO   H CA  1 
ATOM   13245 C  C   . PRO   H  8  23  ? 65.494  -145.086 34.151  1.00 95.87  ? 24  PRO   H C   1 
ATOM   13246 O  O   . PRO   H  8  23  ? 66.524  -145.700 34.370  1.00 91.67  ? 24  PRO   H O   1 
ATOM   13247 C  CB  . PRO   H  8  23  ? 63.906  -147.047 34.050  1.00 97.11  ? 24  PRO   H CB  1 
ATOM   13248 C  CG  . PRO   H  8  23  ? 63.295  -146.730 32.697  1.00 96.66  ? 24  PRO   H CG  1 
ATOM   13249 C  CD  . PRO   H  8  23  ? 62.520  -145.440 32.892  1.00 96.29  ? 24  PRO   H CD  1 
ATOM   13250 N  N   . ILE   H  8  24  ? 65.440  -143.929 33.482  1.00 96.29  ? 25  ILE   H N   1 
ATOM   13251 C  CA  . ILE   H  8  24  ? 66.612  -143.236 32.866  1.00 96.13  ? 25  ILE   H CA  1 
ATOM   13252 C  C   . ILE   H  8  24  ? 67.065  -142.104 33.796  1.00 95.88  ? 25  ILE   H C   1 
ATOM   13253 O  O   . ILE   H  8  24  ? 66.192  -141.374 34.298  1.00 93.81  ? 25  ILE   H O   1 
ATOM   13254 C  CB  . ILE   H  8  24  ? 66.245  -142.717 31.460  1.00 98.74  ? 25  ILE   H CB  1 
ATOM   13255 C  CG1 . ILE   H  8  24  ? 66.219  -143.848 30.426  1.00 98.57  ? 25  ILE   H CG1 1 
ATOM   13256 C  CG2 . ILE   H  8  24  ? 67.159  -141.575 31.033  1.00 98.80  ? 25  ILE   H CG2 1 
ATOM   13257 C  CD1 . ILE   H  8  24  ? 67.581  -144.405 30.067  1.00 99.86  ? 25  ILE   H CD1 1 
ATOM   13258 N  N   . VAL   H  8  25  ? 68.379  -141.963 33.999  1.00 97.37  ? 26  VAL   H N   1 
ATOM   13259 C  CA  . VAL   H  8  25  ? 68.990  -140.872 34.815  1.00 99.22  ? 26  VAL   H CA  1 
ATOM   13260 C  C   . VAL   H  8  25  ? 69.161  -139.642 33.917  1.00 102.66 ? 26  VAL   H C   1 
ATOM   13261 O  O   . VAL   H  8  25  ? 70.095  -139.642 33.090  1.00 102.94 ? 26  VAL   H O   1 
ATOM   13262 C  CB  . VAL   H  8  25  ? 70.332  -141.303 35.438  1.00 101.33 ? 26  VAL   H CB  1 
ATOM   13263 C  CG1 . VAL   H  8  25  ? 70.999  -140.160 36.190  1.00 100.71 ? 26  VAL   H CG1 1 
ATOM   13264 C  CG2 . VAL   H  8  25  ? 70.171  -142.514 36.344  1.00 102.34 ? 26  VAL   H CG2 1 
ATOM   13265 N  N   . ALA   H  8  26  ? 68.288  -138.641 34.081  1.00 104.15 ? 27  ALA   H N   1 
ATOM   13266 C  CA  . ALA   H  8  26  ? 68.301  -137.364 33.328  1.00 103.94 ? 27  ALA   H CA  1 
ATOM   13267 C  C   . ALA   H  8  26  ? 69.522  -136.531 33.736  1.00 104.65 ? 27  ALA   H C   1 
ATOM   13268 O  O   . ALA   H  8  26  ? 70.221  -136.038 32.830  1.00 105.36 ? 27  ALA   H O   1 
ATOM   13269 C  CB  . ALA   H  8  26  ? 67.015  -136.608 33.556  1.00 104.86 ? 27  ALA   H CB  1 
ATOM   13270 N  N   . ASP   H  8  27  ? 69.768  -136.381 35.043  1.00 104.54 ? 28  ASP   H N   1 
ATOM   13271 C  CA  . ASP   H  8  27  ? 70.910  -135.598 35.588  1.00 106.94 ? 28  ASP   H CA  1 
ATOM   13272 C  C   . ASP   H  8  27  ? 71.675  -136.441 36.614  1.00 103.35 ? 28  ASP   H C   1 
ATOM   13273 O  O   . ASP   H  8  27  ? 71.069  -136.828 37.632  1.00 99.96  ? 28  ASP   H O   1 
ATOM   13274 C  CB  . ASP   H  8  27  ? 70.440  -134.278 36.204  1.00 111.56 ? 28  ASP   H CB  1 
ATOM   13275 C  CG  . ASP   H  8  27  ? 71.513  -133.198 36.228  1.00 118.41 ? 28  ASP   H CG  1 
ATOM   13276 O  OD1 . ASP   H  8  27  ? 71.141  -132.005 36.302  1.00 119.59 ? 28  ASP   H OD1 1 
ATOM   13277 O  OD2 . ASP   H  8  27  ? 72.711  -133.554 36.173  1.00 116.91 ? 28  ASP   H OD2 1 
ATOM   13278 N  N   . LYS   H  8  28  ? 72.962  -136.690 36.347  1.00 104.21 ? 29  LYS   H N   1 
ATOM   13279 C  CA  . LYS   H  8  28  ? 73.883  -137.463 37.224  1.00 102.35 ? 29  LYS   H CA  1 
ATOM   13280 C  C   . LYS   H  8  28  ? 74.258  -136.627 38.450  1.00 103.28 ? 29  LYS   H C   1 
ATOM   13281 O  O   . LYS   H  8  28  ? 74.535  -137.227 39.508  1.00 101.76 ? 29  LYS   H O   1 
ATOM   13282 C  CB  . LYS   H  8  28  ? 75.142  -137.874 36.457  1.00 103.26 ? 29  LYS   H CB  1 
ATOM   13283 C  CG  . LYS   H  8  28  ? 74.945  -139.048 35.512  1.00 102.45 ? 29  LYS   H CG  1 
ATOM   13284 C  CD  . LYS   H  8  28  ? 76.231  -139.587 34.948  1.00 104.40 ? 29  LYS   H CD  1 
ATOM   13285 C  CE  . LYS   H  8  28  ? 76.725  -138.813 33.747  1.00 105.96 ? 29  LYS   H CE  1 
ATOM   13286 N  NZ  . LYS   H  8  28  ? 77.568  -139.668 32.886  1.00 109.24 ? 29  LYS   H NZ  1 
ATOM   13287 N  N   . ASN   H  8  29  ? 74.283  -135.299 38.301  1.00 102.02 ? 30  ASN   H N   1 
ATOM   13288 C  CA  . ASN   H  8  29  ? 74.650  -134.343 39.379  1.00 98.97  ? 30  ASN   H CA  1 
ATOM   13289 C  C   . ASN   H  8  29  ? 73.725  -133.121 39.303  1.00 99.13  ? 30  ASN   H C   1 
ATOM   13290 O  O   . ASN   H  8  29  ? 74.053  -132.172 38.563  1.00 101.34 ? 30  ASN   H O   1 
ATOM   13291 C  CB  . ASN   H  8  29  ? 76.136  -133.977 39.293  1.00 95.30  ? 30  ASN   H CB  1 
ATOM   13292 C  CG  . ASN   H  8  29  ? 76.656  -133.267 40.522  1.00 92.16  ? 30  ASN   H CG  1 
ATOM   13293 O  OD1 . ASN   H  8  29  ? 77.778  -133.508 40.954  1.00 88.60  ? 30  ASN   H OD1 1 
ATOM   13294 N  ND2 . ASN   H  8  29  ? 75.854  -132.394 41.099  1.00 92.04  ? 30  ASN   H ND2 1 
ATOM   13295 N  N   . CYS   H  8  30  ? 72.624  -133.144 40.059  1.00 95.28  ? 31  CYS   H N   1 
ATOM   13296 C  CA  . CYS   H  8  30  ? 71.656  -132.024 40.203  1.00 98.16  ? 31  CYS   H CA  1 
ATOM   13297 C  C   . CYS   H  8  30  ? 71.463  -131.726 41.690  1.00 99.24  ? 31  CYS   H C   1 
ATOM   13298 O  O   . CYS   H  8  30  ? 71.448  -132.682 42.480  1.00 101.92 ? 31  CYS   H O   1 
ATOM   13299 C  CB  . CYS   H  8  30  ? 70.308  -132.359 39.577  1.00 103.23 ? 31  CYS   H CB  1 
ATOM   13300 S  SG  . CYS   H  8  30  ? 69.254  -133.382 40.639  1.00 107.13 ? 31  CYS   H SG  1 
ATOM   13301 N  N   . ALA   H  8  31  ? 71.320  -130.453 42.057  1.00 103.01 ? 32  ALA   H N   1 
ATOM   13302 C  CA  . ALA   H  8  31  ? 71.131  -130.011 43.458  1.00 104.35 ? 32  ALA   H CA  1 
ATOM   13303 C  C   . ALA   H  8  31  ? 69.639  -130.044 43.797  1.00 100.71 ? 32  ALA   H C   1 
ATOM   13304 O  O   . ALA   H  8  31  ? 68.846  -129.437 43.050  1.00 103.09 ? 32  ALA   H O   1 
ATOM   13305 C  CB  . ALA   H  8  31  ? 71.719  -128.639 43.664  1.00 106.23 ? 32  ALA   H CB  1 
ATOM   13306 N  N   . LYS   H  8  32  ? 69.283  -130.747 44.873  1.00 98.89  ? 33  LYS   H N   1 
ATOM   13307 C  CA  . LYS   H  8  32  ? 67.894  -130.856 45.389  1.00 97.11  ? 33  LYS   H CA  1 
ATOM   13308 C  C   . LYS   H  8  32  ? 67.743  -129.966 46.625  1.00 96.07  ? 33  LYS   H C   1 
ATOM   13309 O  O   . LYS   H  8  32  ? 66.647  -129.971 47.218  1.00 91.96  ? 33  LYS   H O   1 
ATOM   13310 C  CB  . LYS   H  8  32  ? 67.580  -132.320 45.700  1.00 97.63  ? 33  LYS   H CB  1 
ATOM   13311 C  CG  . LYS   H  8  32  ? 67.859  -133.264 44.543  1.00 98.68  ? 33  LYS   H CG  1 
ATOM   13312 C  CD  . LYS   H  8  32  ? 67.486  -134.689 44.810  1.00 98.91  ? 33  LYS   H CD  1 
ATOM   13313 C  CE  . LYS   H  8  32  ? 67.778  -135.564 43.614  1.00 100.26 ? 33  LYS   H CE  1 
ATOM   13314 N  NZ  . LYS   H  8  32  ? 67.598  -136.990 43.947  1.00 102.21 ? 33  LYS   H NZ  1 
ATOM   13315 N  N   . LEU   H  8  33  ? 68.808  -129.237 46.982  1.00 98.41  ? 34  LEU   H N   1 
ATOM   13316 C  CA  . LEU   H  8  33  ? 68.845  -128.259 48.102  1.00 99.70  ? 34  LEU   H CA  1 
ATOM   13317 C  C   . LEU   H  8  33  ? 68.626  -126.856 47.540  1.00 99.46  ? 34  LEU   H C   1 
ATOM   13318 O  O   . LEU   H  8  33  ? 69.474  -126.397 46.748  1.00 96.20  ? 34  LEU   H O   1 
ATOM   13319 C  CB  . LEU   H  8  33  ? 70.198  -128.342 48.814  1.00 101.26 ? 34  LEU   H CB  1 
ATOM   13320 C  CG  . LEU   H  8  33  ? 70.269  -129.293 50.008  1.00 98.28  ? 34  LEU   H CG  1 
ATOM   13321 C  CD1 . LEU   H  8  33  ? 69.444  -130.549 49.776  1.00 97.54  ? 34  LEU   H CD1 1 
ATOM   13322 C  CD2 . LEU   H  8  33  ? 71.713  -129.654 50.307  1.00 98.60  ? 34  LEU   H CD2 1 
ATOM   13323 N  N   . HIS   H  8  34  ? 67.537  -126.209 47.950  1.00 101.98 ? 35  HIS   H N   1 
ATOM   13324 C  CA  . HIS   H  8  34  ? 67.155  -124.849 47.499  1.00 103.69 ? 35  HIS   H CA  1 
ATOM   13325 C  C   . HIS   H  8  34  ? 67.228  -123.880 48.678  1.00 99.23  ? 35  HIS   H C   1 
ATOM   13326 O  O   . HIS   H  8  34  ? 66.905  -124.284 49.813  1.00 99.33  ? 35  HIS   H O   1 
ATOM   13327 C  CB  . HIS   H  8  34  ? 65.757  -124.853 46.882  1.00 108.54 ? 35  HIS   H CB  1 
ATOM   13328 C  CG  . HIS   H  8  34  ? 65.469  -126.028 46.012  1.00 110.55 ? 35  HIS   H CG  1 
ATOM   13329 N  ND1 . HIS   H  8  34  ? 65.696  -126.013 44.651  1.00 113.72 ? 35  HIS   H ND1 1 
ATOM   13330 C  CD2 . HIS   H  8  34  ? 64.963  -127.245 46.303  1.00 112.40 ? 35  HIS   H CD2 1 
ATOM   13331 C  CE1 . HIS   H  8  34  ? 65.345  -127.176 44.140  1.00 113.19 ? 35  HIS   H CE1 1 
ATOM   13332 N  NE2 . HIS   H  8  34  ? 64.893  -127.950 45.132  1.00 114.46 ? 35  HIS   H NE2 1 
ATOM   13333 N  N   . ARG   H  8  35  ? 67.564  -122.625 48.375  1.00 98.81  ? 36  ARG   H N   1 
ATOM   13334 C  CA  . ARG   H  8  35  ? 67.656  -121.544 49.384  1.00 94.48  ? 36  ARG   H CA  1 
ATOM   13335 C  C   . ARG   H  8  35  ? 66.389  -120.699 49.336  1.00 89.54  ? 36  ARG   H C   1 
ATOM   13336 O  O   . ARG   H  8  35  ? 66.160  -120.045 48.322  1.00 87.22  ? 36  ARG   H O   1 
ATOM   13337 C  CB  . ARG   H  8  35  ? 68.843  -120.628 49.077  1.00 97.91  ? 36  ARG   H CB  1 
ATOM   13338 C  CG  . ARG   H  8  35  ? 68.892  -119.355 49.910  1.00 98.27  ? 36  ARG   H CG  1 
ATOM   13339 C  CD  . ARG   H  8  35  ? 70.010  -118.424 49.474  1.00 101.72 ? 36  ARG   H CD  1 
ATOM   13340 N  NE  . ARG   H  8  35  ? 69.744  -117.864 48.159  1.00 102.68 ? 36  ARG   H NE  1 
ATOM   13341 C  CZ  . ARG   H  8  35  ? 70.567  -117.880 47.116  1.00 106.42 ? 36  ARG   H CZ  1 
ATOM   13342 N  NH1 . ARG   H  8  35  ? 71.765  -118.437 47.182  1.00 110.12 ? 36  ARG   H NH1 1 
ATOM   13343 N  NH2 . ARG   H  8  35  ? 70.177  -117.335 45.984  1.00 110.04 ? 36  ARG   H NH2 1 
ATOM   13344 N  N   . ILE   H  8  36  ? 65.564  -120.800 50.368  1.00 85.69  ? 37  ILE   H N   1 
ATOM   13345 C  CA  . ILE   H  8  36  ? 64.368  -119.922 50.529  1.00 87.85  ? 37  ILE   H CA  1 
ATOM   13346 C  C   . ILE   H  8  36  ? 64.852  -118.535 50.975  1.00 90.50  ? 37  ILE   H C   1 
ATOM   13347 O  O   . ILE   H  8  36  ? 64.329  -117.521 50.458  1.00 89.63  ? 37  ILE   H O   1 
ATOM   13348 C  CB  . ILE   H  8  36  ? 63.355  -120.541 51.513  1.00 86.85  ? 37  ILE   H CB  1 
ATOM   13349 C  CG1 . ILE   H  8  36  ? 62.686  -121.771 50.895  1.00 86.44  ? 37  ILE   H CG1 1 
ATOM   13350 C  CG2 . ILE   H  8  36  ? 62.337  -119.503 51.968  1.00 87.69  ? 37  ILE   H CG2 1 
ATOM   13351 C  CD1 . ILE   H  8  36  ? 61.678  -122.456 51.789  1.00 87.34  ? 37  ILE   H CD1 1 
ATOM   13352 N  N   . SER   H  8  37  ? 65.814  -118.511 51.901  1.00 90.22  ? 38  SER   H N   1 
ATOM   13353 C  CA  . SER   H  8  37  ? 66.485  -117.293 52.425  1.00 91.55  ? 38  SER   H CA  1 
ATOM   13354 C  C   . SER   H  8  37  ? 67.911  -117.653 52.831  1.00 92.22  ? 38  SER   H C   1 
ATOM   13355 O  O   . SER   H  8  37  ? 68.261  -118.828 52.873  1.00 94.05  ? 38  SER   H O   1 
ATOM   13356 C  CB  . SER   H  8  37  ? 65.711  -116.711 53.578  1.00 90.82  ? 38  SER   H CB  1 
ATOM   13357 O  OG  . SER   H  8  37  ? 66.219  -117.163 54.824  1.00 90.99  ? 38  SER   H OG  1 
ATOM   13358 N  N   . PRO   H  8  38  ? 68.775  -116.672 53.167  1.00 93.06  ? 39  PRO   H N   1 
ATOM   13359 C  CA  . PRO   H  8  38  ? 70.163  -116.971 53.516  1.00 94.22  ? 39  PRO   H CA  1 
ATOM   13360 C  C   . PRO   H  8  38  ? 70.281  -118.055 54.599  1.00 93.49  ? 39  PRO   H C   1 
ATOM   13361 O  O   . PRO   H  8  38  ? 71.104  -118.934 54.444  1.00 90.51  ? 39  PRO   H O   1 
ATOM   13362 C  CB  . PRO   H  8  38  ? 70.692  -115.616 54.013  1.00 94.66  ? 39  PRO   H CB  1 
ATOM   13363 C  CG  . PRO   H  8  38  ? 69.853  -114.609 53.264  1.00 95.64  ? 39  PRO   H CG  1 
ATOM   13364 C  CD  . PRO   H  8  38  ? 68.475  -115.235 53.245  1.00 94.97  ? 39  PRO   H CD  1 
ATOM   13365 N  N   . LYS   H  8  39  ? 69.453  -117.974 55.645  1.00 94.63  ? 40  LYS   H N   1 
ATOM   13366 C  CA  . LYS   H  8  39  ? 69.514  -118.878 56.827  1.00 96.24  ? 40  LYS   H CA  1 
ATOM   13367 C  C   . LYS   H  8  39  ? 68.281  -119.791 56.889  1.00 92.92  ? 40  LYS   H C   1 
ATOM   13368 O  O   . LYS   H  8  39  ? 68.067  -120.408 57.950  1.00 91.81  ? 40  LYS   H O   1 
ATOM   13369 C  CB  . LYS   H  8  39  ? 69.659  -118.050 58.105  1.00 97.45  ? 40  LYS   H CB  1 
ATOM   13370 C  CG  . LYS   H  8  39  ? 70.977  -117.302 58.222  1.00 99.95  ? 40  LYS   H CG  1 
ATOM   13371 C  CD  . LYS   H  8  39  ? 71.667  -117.566 59.524  1.00 103.55 ? 40  LYS   H CD  1 
ATOM   13372 C  CE  . LYS   H  8  39  ? 72.939  -116.770 59.681  1.00 108.10 ? 40  LYS   H CE  1 
ATOM   13373 N  NZ  . LYS   H  8  39  ? 73.359  -116.771 61.094  1.00 108.91 ? 40  LYS   H NZ  1 
ATOM   13374 N  N   . ILE   H  8  40  ? 67.508  -119.888 55.802  1.00 92.55  ? 41  ILE   H N   1 
ATOM   13375 C  CA  . ILE   H  8  40  ? 66.407  -120.888 55.651  1.00 93.71  ? 41  ILE   H CA  1 
ATOM   13376 C  C   . ILE   H  8  40  ? 66.606  -121.660 54.345  1.00 93.16  ? 41  ILE   H C   1 
ATOM   13377 O  O   . ILE   H  8  40  ? 66.439  -121.056 53.268  1.00 100.19 ? 41  ILE   H O   1 
ATOM   13378 C  CB  . ILE   H  8  40  ? 65.016  -120.229 55.681  1.00 93.18  ? 41  ILE   H CB  1 
ATOM   13379 C  CG1 . ILE   H  8  40  ? 64.775  -119.470 56.989  1.00 96.96  ? 41  ILE   H CG1 1 
ATOM   13380 C  CG2 . ILE   H  8  40  ? 63.942  -121.275 55.409  1.00 91.43  ? 41  ILE   H CG2 1 
ATOM   13381 C  CD1 . ILE   H  8  40  ? 63.333  -119.093 57.227  1.00 97.05  ? 41  ILE   H CD1 1 
ATOM   13382 N  N   . TRP   H  8  41  ? 66.892  -122.958 54.443  1.00 90.79  ? 42  TRP   H N   1 
ATOM   13383 C  CA  . TRP   H  8  41  ? 67.062  -123.860 53.275  1.00 90.96  ? 42  TRP   H CA  1 
ATOM   13384 C  C   . TRP   H  8  41  ? 66.027  -124.985 53.321  1.00 89.02  ? 42  TRP   H C   1 
ATOM   13385 O  O   . TRP   H  8  41  ? 65.588  -125.370 54.420  1.00 88.73  ? 42  TRP   H O   1 
ATOM   13386 C  CB  . TRP   H  8  41  ? 68.484  -124.419 53.224  1.00 90.38  ? 42  TRP   H CB  1 
ATOM   13387 C  CG  . TRP   H  8  41  ? 69.521  -123.395 52.891  1.00 90.51  ? 42  TRP   H CG  1 
ATOM   13388 C  CD1 . TRP   H  8  41  ? 69.915  -122.335 53.655  1.00 90.49  ? 42  TRP   H CD1 1 
ATOM   13389 C  CD2 . TRP   H  8  41  ? 70.319  -123.349 51.698  1.00 90.04  ? 42  TRP   H CD2 1 
ATOM   13390 N  NE1 . TRP   H  8  41  ? 70.897  -121.630 53.015  1.00 90.99  ? 42  TRP   H NE1 1 
ATOM   13391 C  CE2 . TRP   H  8  41  ? 71.168  -122.229 51.814  1.00 90.94  ? 42  TRP   H CE2 1 
ATOM   13392 C  CE3 . TRP   H  8  41  ? 70.398  -124.142 50.550  1.00 91.12  ? 42  TRP   H CE3 1 
ATOM   13393 C  CZ2 . TRP   H  8  41  ? 72.081  -121.884 50.820  1.00 92.18  ? 42  TRP   H CZ2 1 
ATOM   13394 C  CZ3 . TRP   H  8  41  ? 71.301  -123.801 49.568  1.00 92.80  ? 42  TRP   H CZ3 1 
ATOM   13395 C  CH2 . TRP   H  8  41  ? 72.130  -122.686 49.704  1.00 93.13  ? 42  TRP   H CH2 1 
ATOM   13396 N  N   . CYS   H  8  42  ? 65.676  -125.499 52.146  1.00 88.91  ? 43  CYS   H N   1 
ATOM   13397 C  CA  . CYS   H  8  42  ? 64.636  -126.535 51.948  1.00 92.08  ? 43  CYS   H CA  1 
ATOM   13398 C  C   . CYS   H  8  42  ? 65.160  -127.589 50.965  1.00 90.17  ? 43  CYS   H C   1 
ATOM   13399 O  O   . CYS   H  8  42  ? 65.799  -127.204 49.965  1.00 87.07  ? 43  CYS   H O   1 
ATOM   13400 C  CB  . CYS   H  8  42  ? 63.351  -125.871 51.468  1.00 94.86  ? 43  CYS   H CB  1 
ATOM   13401 S  SG  . CYS   H  8  42  ? 62.303  -126.925 50.434  1.00 103.51 ? 43  CYS   H SG  1 
ATOM   13402 N  N   . ALA   H  8  43  ? 64.923  -128.869 51.265  1.00 90.86  ? 44  ALA   H N   1 
ATOM   13403 C  CA  . ALA   H  8  43  ? 65.266  -130.026 50.405  1.00 91.30  ? 44  ALA   H CA  1 
ATOM   13404 C  C   . ALA   H  8  43  ? 63.970  -130.661 49.887  1.00 87.31  ? 44  ALA   H C   1 
ATOM   13405 O  O   . ALA   H  8  43  ? 63.081  -130.934 50.717  1.00 85.56  ? 44  ALA   H O   1 
ATOM   13406 C  CB  . ALA   H  8  43  ? 66.104  -131.015 51.176  1.00 94.14  ? 44  ALA   H CB  1 
ATOM   13407 N  N   . GLY   H  8  44  ? 63.875  -130.888 48.571  1.00 85.23  ? 45  GLY   H N   1 
ATOM   13408 C  CA  . GLY   H  8  44  ? 62.612  -131.246 47.897  1.00 85.76  ? 45  GLY   H CA  1 
ATOM   13409 C  C   . GLY   H  8  44  ? 62.705  -132.512 47.060  1.00 83.67  ? 45  GLY   H C   1 
ATOM   13410 O  O   . GLY   H  8  44  ? 63.692  -132.678 46.317  1.00 82.60  ? 45  GLY   H O   1 
ATOM   13411 N  N   . ALA   H  8  45  ? 61.690  -133.371 47.185  1.00 84.73  ? 46  ALA   H N   1 
ATOM   13412 C  CA  . ALA   H  8  45  ? 61.486  -134.620 46.418  1.00 87.15  ? 46  ALA   H CA  1 
ATOM   13413 C  C   . ALA   H  8  45  ? 60.171  -134.508 45.642  1.00 88.56  ? 46  ALA   H C   1 
ATOM   13414 O  O   . ALA   H  8  45  ? 59.377  -133.597 45.956  1.00 90.00  ? 46  ALA   H O   1 
ATOM   13415 C  CB  . ALA   H  8  45  ? 61.462  -135.791 47.366  1.00 86.49  ? 46  ALA   H CB  1 
ATOM   13416 N  N   . GLY   H  8  46  ? 59.942  -135.410 44.685  1.00 88.76  ? 47  GLY   H N   1 
ATOM   13417 C  CA  . GLY   H  8  46  ? 58.773  -135.379 43.784  1.00 88.59  ? 47  GLY   H CA  1 
ATOM   13418 C  C   . GLY   H  8  46  ? 59.133  -134.730 42.461  1.00 88.43  ? 47  GLY   H C   1 
ATOM   13419 O  O   . GLY   H  8  46  ? 60.335  -134.720 42.129  1.00 88.98  ? 47  GLY   H O   1 
ATOM   13420 N  N   . THR   H  8  47  ? 58.149  -134.200 41.726  1.00 89.92  ? 48  THR   H N   1 
ATOM   13421 C  CA  . THR   H  8  47  ? 58.371  -133.531 40.414  1.00 91.12  ? 48  THR   H CA  1 
ATOM   13422 C  C   . THR   H  8  47  ? 59.386  -132.397 40.595  1.00 90.09  ? 48  THR   H C   1 
ATOM   13423 O  O   . THR   H  8  47  ? 59.102  -131.485 41.389  1.00 86.29  ? 48  THR   H O   1 
ATOM   13424 C  CB  . THR   H  8  47  ? 57.080  -132.974 39.804  1.00 91.57  ? 48  THR   H CB  1 
ATOM   13425 O  OG1 . THR   H  8  47  ? 56.077  -133.989 39.834  1.00 97.12  ? 48  THR   H OG1 1 
ATOM   13426 C  CG2 . THR   H  8  47  ? 57.294  -132.487 38.386  1.00 90.27  ? 48  THR   H CG2 1 
ATOM   13427 N  N   . ALA   H  8  48  ? 60.508  -132.457 39.870  1.00 93.96  ? 49  ALA   H N   1 
ATOM   13428 C  CA  . ALA   H  8  48  ? 61.682  -131.563 40.020  1.00 95.83  ? 49  ALA   H CA  1 
ATOM   13429 C  C   . ALA   H  8  48  ? 61.290  -130.104 39.748  1.00 95.53  ? 49  ALA   H C   1 
ATOM   13430 O  O   . ALA   H  8  48  ? 61.706  -129.221 40.530  1.00 96.66  ? 49  ALA   H O   1 
ATOM   13431 C  CB  . ALA   H  8  48  ? 62.785  -132.014 39.096  1.00 94.60  ? 49  ALA   H CB  1 
ATOM   13432 N  N   . ALA   H  8  49  ? 60.537  -129.858 38.670  1.00 97.65  ? 50  ALA   H N   1 
ATOM   13433 C  CA  . ALA   H  8  49  ? 60.068  -128.512 38.264  1.00 93.27  ? 50  ALA   H CA  1 
ATOM   13434 C  C   . ALA   H  8  49  ? 59.197  -127.914 39.373  1.00 93.09  ? 50  ALA   H C   1 
ATOM   13435 O  O   . ALA   H  8  49  ? 59.361  -126.720 39.657  1.00 96.03  ? 50  ALA   H O   1 
ATOM   13436 C  CB  . ALA   H  8  49  ? 59.308  -128.584 36.966  1.00 94.37  ? 50  ALA   H CB  1 
ATOM   13437 N  N   . ASP   H  8  50  ? 58.313  -128.719 39.971  1.00 89.46  ? 51  ASP   H N   1 
ATOM   13438 C  CA  . ASP   H  8  50  ? 57.365  -128.278 41.030  1.00 87.51  ? 51  ASP   H CA  1 
ATOM   13439 C  C   . ASP   H  8  50  ? 58.126  -127.872 42.297  1.00 87.18  ? 51  ASP   H C   1 
ATOM   13440 O  O   . ASP   H  8  50  ? 57.766  -126.832 42.866  1.00 87.89  ? 51  ASP   H O   1 
ATOM   13441 C  CB  . ASP   H  8  50  ? 56.324  -129.352 41.353  1.00 87.61  ? 51  ASP   H CB  1 
ATOM   13442 C  CG  . ASP   H  8  50  ? 55.220  -129.454 40.320  1.00 89.52  ? 51  ASP   H CG  1 
ATOM   13443 O  OD1 . ASP   H  8  50  ? 54.983  -128.457 39.615  1.00 91.34  ? 51  ASP   H OD1 1 
ATOM   13444 O  OD2 . ASP   H  8  50  ? 54.607  -130.531 40.230  1.00 94.07  ? 51  ASP   H OD2 1 
ATOM   13445 N  N   . THR   H  8  51  ? 59.115  -128.658 42.737  1.00 87.23  ? 52  THR   H N   1 
ATOM   13446 C  CA  . THR   H  8  51  ? 59.892  -128.373 43.977  1.00 88.99  ? 52  THR   H CA  1 
ATOM   13447 C  C   . THR   H  8  51  ? 60.699  -127.084 43.789  1.00 88.33  ? 52  THR   H C   1 
ATOM   13448 O  O   . THR   H  8  51  ? 60.683  -126.255 44.716  1.00 89.88  ? 52  THR   H O   1 
ATOM   13449 C  CB  . THR   H  8  51  ? 60.815  -129.526 44.403  1.00 88.15  ? 52  THR   H CB  1 
ATOM   13450 O  OG1 . THR   H  8  51  ? 61.842  -129.726 43.430  1.00 90.97  ? 52  THR   H OG1 1 
ATOM   13451 C  CG2 . THR   H  8  51  ? 60.071  -130.823 44.623  1.00 86.97  ? 52  THR   H CG2 1 
ATOM   13452 N  N   . GLU   H  8  52  ? 61.376  -126.928 42.646  1.00 88.10  ? 53  GLU   H N   1 
ATOM   13453 C  CA  . GLU   H  8  52  ? 62.169  -125.710 42.326  1.00 90.60  ? 53  GLU   H CA  1 
ATOM   13454 C  C   . GLU   H  8  52  ? 61.219  -124.508 42.266  1.00 88.22  ? 53  GLU   H C   1 
ATOM   13455 O  O   . GLU   H  8  52  ? 61.511  -123.501 42.935  1.00 88.23  ? 53  GLU   H O   1 
ATOM   13456 C  CB  . GLU   H  8  52  ? 62.947  -125.873 41.016  1.00 96.43  ? 53  GLU   H CB  1 
ATOM   13457 C  CG  . GLU   H  8  52  ? 63.830  -124.676 40.676  1.00 102.83 ? 53  GLU   H CG  1 
ATOM   13458 C  CD  . GLU   H  8  52  ? 65.225  -124.656 41.288  1.00 108.63 ? 53  GLU   H CD  1 
ATOM   13459 O  OE1 . GLU   H  8  52  ? 65.798  -125.745 41.503  1.00 115.67 ? 53  GLU   H OE1 1 
ATOM   13460 O  OE2 . GLU   H  8  52  ? 65.745  -123.544 41.535  1.00 109.70 ? 53  GLU   H OE2 1 
ATOM   13461 N  N   . ALA   H  8  53  ? 60.116  -124.626 41.517  1.00 85.18  ? 54  ALA   H N   1 
ATOM   13462 C  CA  . ALA   H  8  53  ? 59.155  -123.532 41.231  1.00 85.68  ? 54  ALA   H CA  1 
ATOM   13463 C  C   . ALA   H  8  53  ? 58.528  -123.004 42.528  1.00 86.31  ? 54  ALA   H C   1 
ATOM   13464 O  O   . ALA   H  8  53  ? 58.562  -121.774 42.728  1.00 85.62  ? 54  ALA   H O   1 
ATOM   13465 C  CB  . ALA   H  8  53  ? 58.095  -124.001 40.263  1.00 84.49  ? 54  ALA   H CB  1 
ATOM   13466 N  N   . VAL   H  8  54  ? 57.969  -123.885 43.365  1.00 84.12  ? 55  VAL   H N   1 
ATOM   13467 C  CA  . VAL   H  8  54  ? 57.269  -123.501 44.631  1.00 84.73  ? 55  VAL   H CA  1 
ATOM   13468 C  C   . VAL   H  8  54  ? 58.286  -122.895 45.607  1.00 84.71  ? 55  VAL   H C   1 
ATOM   13469 O  O   . VAL   H  8  54  ? 57.915  -121.951 46.325  1.00 83.15  ? 55  VAL   H O   1 
ATOM   13470 C  CB  . VAL   H  8  54  ? 56.498  -124.672 45.277  1.00 85.55  ? 55  VAL   H CB  1 
ATOM   13471 C  CG1 . VAL   H  8  54  ? 57.406  -125.808 45.732  1.00 87.03  ? 55  VAL   H CG1 1 
ATOM   13472 C  CG2 . VAL   H  8  54  ? 55.653  -124.189 46.444  1.00 87.60  ? 55  VAL   H CG2 1 
ATOM   13473 N  N   . THR   H  8  55  ? 59.512  -123.422 45.649  1.00 85.51  ? 56  THR   H N   1 
ATOM   13474 C  CA  . THR   H  8  55  ? 60.611  -122.904 46.507  1.00 89.82  ? 56  THR   H CA  1 
ATOM   13475 C  C   . THR   H  8  55  ? 60.935  -121.455 46.122  1.00 91.12  ? 56  THR   H C   1 
ATOM   13476 O  O   . THR   H  8  55  ? 61.035  -120.609 47.036  1.00 95.80  ? 56  THR   H O   1 
ATOM   13477 C  CB  . THR   H  8  55  ? 61.872  -123.767 46.399  1.00 88.74  ? 56  THR   H CB  1 
ATOM   13478 O  OG1 . THR   H  8  55  ? 61.701  -124.922 47.222  1.00 85.00  ? 56  THR   H OG1 1 
ATOM   13479 C  CG2 . THR   H  8  55  ? 63.112  -123.017 46.827  1.00 91.73  ? 56  THR   H CG2 1 
ATOM   13480 N  N   . GLN   H  8  56  ? 61.124  -121.194 44.825  1.00 91.55  ? 57  GLN   H N   1 
ATOM   13481 C  CA  . GLN   H  8  56  ? 61.495  -119.858 44.290  1.00 91.52  ? 57  GLN   H CA  1 
ATOM   13482 C  C   . GLN   H  8  56  ? 60.372  -118.855 44.580  1.00 85.45  ? 57  GLN   H C   1 
ATOM   13483 O  O   . GLN   H  8  56  ? 60.696  -117.728 44.986  1.00 87.13  ? 57  GLN   H O   1 
ATOM   13484 C  CB  . GLN   H  8  56  ? 61.780  -119.924 42.790  1.00 94.81  ? 57  GLN   H CB  1 
ATOM   13485 C  CG  . GLN   H  8  56  ? 63.137  -120.528 42.453  1.00 99.19  ? 57  GLN   H CG  1 
ATOM   13486 C  CD  . GLN   H  8  56  ? 63.524  -120.422 40.994  1.00 103.57 ? 57  GLN   H CD  1 
ATOM   13487 O  OE1 . GLN   H  8  56  ? 64.561  -120.937 40.581  1.00 104.52 ? 57  GLN   H OE1 1 
ATOM   13488 N  NE2 . GLN   H  8  56  ? 62.708  -119.751 40.192  1.00 108.60 ? 57  GLN   H NE2 1 
ATOM   13489 N  N   . LEU   H  8  57  ? 59.110  -119.247 44.374  1.00 82.43  ? 58  LEU   H N   1 
ATOM   13490 C  CA  . LEU   H  8  57  ? 57.929  -118.360 44.564  1.00 82.37  ? 58  LEU   H CA  1 
ATOM   13491 C  C   . LEU   H  8  57  ? 57.847  -117.917 46.027  1.00 84.88  ? 58  LEU   H C   1 
ATOM   13492 O  O   . LEU   H  8  57  ? 57.695  -116.705 46.258  1.00 88.66  ? 58  LEU   H O   1 
ATOM   13493 C  CB  . LEU   H  8  57  ? 56.643  -119.080 44.149  1.00 79.89  ? 58  LEU   H CB  1 
ATOM   13494 C  CG  . LEU   H  8  57  ? 55.352  -118.318 44.452  1.00 79.99  ? 58  LEU   H CG  1 
ATOM   13495 C  CD1 . LEU   H  8  57  ? 55.254  -117.059 43.605  1.00 80.42  ? 58  LEU   H CD1 1 
ATOM   13496 C  CD2 . LEU   H  8  57  ? 54.131  -119.198 44.239  1.00 79.55  ? 58  LEU   H CD2 1 
ATOM   13497 N  N   . ILE   H  8  58  ? 57.918  -118.857 46.973  1.00 82.19  ? 59  ILE   H N   1 
ATOM   13498 C  CA  . ILE   H  8  58  ? 57.858  -118.548 48.434  1.00 83.48  ? 59  ILE   H CA  1 
ATOM   13499 C  C   . ILE   H  8  58  ? 59.141  -117.797 48.821  1.00 86.01  ? 59  ILE   H C   1 
ATOM   13500 O  O   . ILE   H  8  58  ? 59.042  -116.858 49.632  1.00 87.74  ? 59  ILE   H O   1 
ATOM   13501 C  CB  . ILE   H  8  58  ? 57.621  -119.810 49.292  1.00 82.11  ? 59  ILE   H CB  1 
ATOM   13502 C  CG1 . ILE   H  8  58  ? 56.144  -120.217 49.323  1.00 82.91  ? 59  ILE   H CG1 1 
ATOM   13503 C  CG2 . ILE   H  8  58  ? 58.145  -119.612 50.707  1.00 82.05  ? 59  ILE   H CG2 1 
ATOM   13504 C  CD1 . ILE   H  8  58  ? 55.504  -120.403 47.966  1.00 84.74  ? 59  ILE   H CD1 1 
ATOM   13505 N  N   . GLY   H  8  59  ? 60.291  -118.186 48.255  1.00 88.12  ? 60  GLY   H N   1 
ATOM   13506 C  CA  . GLY   H  8  59  ? 61.582  -117.492 48.440  1.00 89.97  ? 60  GLY   H CA  1 
ATOM   13507 C  C   . GLY   H  8  59  ? 61.502  -116.025 48.038  1.00 88.77  ? 60  GLY   H C   1 
ATOM   13508 O  O   . GLY   H  8  59  ? 62.015  -115.175 48.794  1.00 90.37  ? 60  GLY   H O   1 
ATOM   13509 N  N   . SER   H  8  60  ? 60.886  -115.743 46.884  1.00 87.24  ? 61  SER   H N   1 
ATOM   13510 C  CA  . SER   H  8  60  ? 60.618  -114.380 46.353  1.00 87.11  ? 61  SER   H CA  1 
ATOM   13511 C  C   . SER   H  8  60  ? 59.724  -113.616 47.338  1.00 86.58  ? 61  SER   H C   1 
ATOM   13512 O  O   . SER   H  8  60  ? 60.109  -112.500 47.737  1.00 87.90  ? 61  SER   H O   1 
ATOM   13513 C  CB  . SER   H  8  60  ? 60.001  -114.451 44.974  1.00 85.78  ? 61  SER   H CB  1 
ATOM   13514 O  OG  . SER   H  8  60  ? 59.561  -113.176 44.536  1.00 86.27  ? 61  SER   H OG  1 
ATOM   13515 N  N   . ASN   H  8  61  ? 58.590  -114.208 47.728  1.00 85.24  ? 62  ASN   H N   1 
ATOM   13516 C  CA  . ASN   H  8  61  ? 57.586  -113.591 48.637  1.00 86.19  ? 62  ASN   H CA  1 
ATOM   13517 C  C   . ASN   H  8  61  ? 58.176  -113.405 50.040  1.00 86.45  ? 62  ASN   H C   1 
ATOM   13518 O  O   . ASN   H  8  61  ? 57.762  -112.452 50.719  1.00 89.81  ? 62  ASN   H O   1 
ATOM   13519 C  CB  . ASN   H  8  61  ? 56.293  -114.407 48.709  1.00 87.18  ? 62  ASN   H CB  1 
ATOM   13520 C  CG  . ASN   H  8  61  ? 55.412  -114.226 47.493  1.00 89.89  ? 62  ASN   H CG  1 
ATOM   13521 O  OD1 . ASN   H  8  61  ? 55.352  -113.138 46.926  1.00 91.74  ? 62  ASN   H OD1 1 
ATOM   13522 N  ND2 . ASN   H  8  61  ? 54.713  -115.276 47.095  1.00 92.90  ? 62  ASN   H ND2 1 
ATOM   13523 N  N   . ILE   H  8  62  ? 59.084  -114.286 50.467  1.00 88.02  ? 63  ILE   H N   1 
ATOM   13524 C  CA  . ILE   H  8  62  ? 59.765  -114.204 51.796  1.00 88.63  ? 63  ILE   H CA  1 
ATOM   13525 C  C   . ILE   H  8  62  ? 60.719  -113.006 51.784  1.00 86.28  ? 63  ILE   H C   1 
ATOM   13526 O  O   . ILE   H  8  62  ? 60.786  -112.310 52.812  1.00 86.60  ? 63  ILE   H O   1 
ATOM   13527 C  CB  . ILE   H  8  62  ? 60.485  -115.526 52.153  1.00 88.75  ? 63  ILE   H CB  1 
ATOM   13528 C  CG1 . ILE   H  8  62  ? 59.525  -116.550 52.769  1.00 88.93  ? 63  ILE   H CG1 1 
ATOM   13529 C  CG2 . ILE   H  8  62  ? 61.690  -115.281 53.052  1.00 89.15  ? 63  ILE   H CG2 1 
ATOM   13530 C  CD1 . ILE   H  8  62  ? 58.963  -116.163 54.124  1.00 88.82  ? 63  ILE   H CD1 1 
ATOM   13531 N  N   . GLU   H  8  63  ? 61.432  -112.788 50.674  1.00 85.66  ? 64  GLU   H N   1 
ATOM   13532 C  CA  . GLU   H  8  63  ? 62.395  -111.665 50.511  1.00 88.40  ? 64  GLU   H CA  1 
ATOM   13533 C  C   . GLU   H  8  63  ? 61.644  -110.332 50.618  1.00 86.23  ? 64  GLU   H C   1 
ATOM   13534 O  O   . GLU   H  8  63  ? 62.122  -109.449 51.356  1.00 84.91  ? 64  GLU   H O   1 
ATOM   13535 C  CB  . GLU   H  8  63  ? 63.137  -111.773 49.178  1.00 91.29  ? 64  GLU   H CB  1 
ATOM   13536 C  CG  . GLU   H  8  63  ? 64.212  -110.717 49.003  1.00 97.50  ? 64  GLU   H CG  1 
ATOM   13537 C  CD  . GLU   H  8  63  ? 65.042  -110.864 47.741  1.00 104.26 ? 64  GLU   H CD  1 
ATOM   13538 O  OE1 . GLU   H  8  63  ? 65.331  -109.829 47.105  1.00 112.98 ? 64  GLU   H OE1 1 
ATOM   13539 O  OE2 . GLU   H  8  63  ? 65.407  -112.008 47.399  1.00 105.44 ? 64  GLU   H OE2 1 
ATOM   13540 N  N   . LEU   H  8  64  ? 60.520  -110.197 49.904  1.00 86.53  ? 65  LEU   H N   1 
ATOM   13541 C  CA  . LEU   H  8  64  ? 59.643  -108.993 49.937  1.00 86.80  ? 65  LEU   H CA  1 
ATOM   13542 C  C   . LEU   H  8  64  ? 59.141  -108.768 51.368  1.00 87.72  ? 65  LEU   H C   1 
ATOM   13543 O  O   . LEU   H  8  64  ? 59.180  -107.611 51.835  1.00 89.96  ? 65  LEU   H O   1 
ATOM   13544 C  CB  . LEU   H  8  64  ? 58.459  -109.175 48.979  1.00 85.36  ? 65  LEU   H CB  1 
ATOM   13545 C  CG  . LEU   H  8  64  ? 58.777  -109.209 47.484  1.00 86.03  ? 65  LEU   H CG  1 
ATOM   13546 C  CD1 . LEU   H  8  64  ? 57.495  -109.362 46.682  1.00 87.28  ? 65  LEU   H CD1 1 
ATOM   13547 C  CD2 . LEU   H  8  64  ? 59.527  -107.964 47.034  1.00 86.46  ? 65  LEU   H CD2 1 
ATOM   13548 N  N   . HIS   H  8  65  ? 58.673  -109.830 52.026  1.00 86.26  ? 66  HIS   H N   1 
ATOM   13549 C  CA  . HIS   H  8  65  ? 58.149  -109.806 53.419  1.00 87.85  ? 66  HIS   H CA  1 
ATOM   13550 C  C   . HIS   H  8  65  ? 59.240  -109.311 54.375  1.00 86.15  ? 66  HIS   H C   1 
ATOM   13551 O  O   . HIS   H  8  65  ? 58.933  -108.460 55.224  1.00 85.86  ? 66  HIS   H O   1 
ATOM   13552 C  CB  . HIS   H  8  65  ? 57.633  -111.192 53.824  1.00 88.33  ? 66  HIS   H CB  1 
ATOM   13553 C  CG  . HIS   H  8  65  ? 56.903  -111.205 55.125  1.00 89.41  ? 66  HIS   H CG  1 
ATOM   13554 N  ND1 . HIS   H  8  65  ? 57.509  -111.577 56.309  1.00 88.40  ? 66  HIS   H ND1 1 
ATOM   13555 C  CD2 . HIS   H  8  65  ? 55.625  -110.895 55.433  1.00 91.68  ? 66  HIS   H CD2 1 
ATOM   13556 C  CE1 . HIS   H  8  65  ? 56.634  -111.499 57.291  1.00 88.56  ? 66  HIS   H CE1 1 
ATOM   13557 N  NE2 . HIS   H  8  65  ? 55.470  -111.084 56.780  1.00 90.00  ? 66  HIS   H NE2 1 
ATOM   13558 N  N   . SER   H  8  66  ? 60.459  -109.843 54.239  1.00 86.00  ? 67  SER   H N   1 
ATOM   13559 C  CA  . SER   H  8  66  ? 61.660  -109.471 55.033  1.00 88.92  ? 67  SER   H CA  1 
ATOM   13560 C  C   . SER   H  8  66  ? 61.932  -107.965 54.906  1.00 89.23  ? 67  SER   H C   1 
ATOM   13561 O  O   . SER   H  8  66  ? 62.120  -107.304 55.948  1.00 90.82  ? 67  SER   H O   1 
ATOM   13562 C  CB  . SER   H  8  66  ? 62.855  -110.284 54.600  1.00 87.59  ? 67  SER   H CB  1 
ATOM   13563 O  OG  . SER   H  8  66  ? 63.973  -110.035 55.435  1.00 90.66  ? 67  SER   H OG  1 
ATOM   13564 N  N   . LEU   H  8  67  ? 61.955  -107.457 53.669  1.00 89.21  ? 68  LEU   H N   1 
ATOM   13565 C  CA  . LEU   H  8  67  ? 62.155  -106.020 53.334  1.00 88.80  ? 68  LEU   H CA  1 
ATOM   13566 C  C   . LEU   H  8  67  ? 61.024  -105.176 53.942  1.00 86.26  ? 68  LEU   H C   1 
ATOM   13567 O  O   . LEU   H  8  67  ? 61.335  -104.101 54.483  1.00 86.30  ? 68  LEU   H O   1 
ATOM   13568 C  CB  . LEU   H  8  67  ? 62.217  -105.863 51.808  1.00 89.17  ? 68  LEU   H CB  1 
ATOM   13569 C  CG  . LEU   H  8  67  ? 63.608  -105.773 51.173  1.00 91.25  ? 68  LEU   H CG  1 
ATOM   13570 C  CD1 . LEU   H  8  67  ? 64.637  -106.631 51.896  1.00 90.82  ? 68  LEU   H CD1 1 
ATOM   13571 C  CD2 . LEU   H  8  67  ? 63.549  -106.156 49.700  1.00 91.62  ? 68  LEU   H CD2 1 
ATOM   13572 N  N   . TYR   H  8  68  ? 59.770  -105.641 53.865  1.00 85.12  ? 69  TYR   H N   1 
ATOM   13573 C  CA  . TYR   H  8  68  ? 58.562  -104.907 54.337  1.00 83.99  ? 69  TYR   H CA  1 
ATOM   13574 C  C   . TYR   H  8  68  ? 58.580  -104.776 55.861  1.00 84.94  ? 69  TYR   H C   1 
ATOM   13575 O  O   . TYR   H  8  68  ? 58.240  -103.695 56.365  1.00 84.51  ? 69  TYR   H O   1 
ATOM   13576 C  CB  . TYR   H  8  68  ? 57.268  -105.612 53.922  1.00 84.63  ? 69  TYR   H CB  1 
ATOM   13577 C  CG  . TYR   H  8  68  ? 55.994  -104.849 54.202  1.00 86.77  ? 69  TYR   H CG  1 
ATOM   13578 C  CD1 . TYR   H  8  68  ? 55.368  -104.907 55.439  1.00 88.05  ? 69  TYR   H CD1 1 
ATOM   13579 C  CD2 . TYR   H  8  68  ? 55.392  -104.083 53.216  1.00 88.05  ? 69  TYR   H CD2 1 
ATOM   13580 C  CE1 . TYR   H  8  68  ? 54.187  -104.223 55.689  1.00 89.63  ? 69  TYR   H CE1 1 
ATOM   13581 C  CE2 . TYR   H  8  68  ? 54.213  -103.394 53.448  1.00 90.28  ? 69  TYR   H CE2 1 
ATOM   13582 C  CZ  . TYR   H  8  68  ? 53.605  -103.465 54.689  1.00 90.86  ? 69  TYR   H CZ  1 
ATOM   13583 O  OH  . TYR   H  8  68  ? 52.439  -102.792 54.915  1.00 98.95  ? 69  TYR   H OH  1 
ATOM   13584 N  N   . THR   H  8  69  ? 58.931  -105.855 56.565  1.00 83.28  ? 70  THR   H N   1 
ATOM   13585 C  CA  . THR   H  8  69  ? 58.874  -105.957 58.050  1.00 84.48  ? 70  THR   H CA  1 
ATOM   13586 C  C   . THR   H  8  69  ? 60.210  -105.547 58.687  1.00 85.23  ? 70  THR   H C   1 
ATOM   13587 O  O   . THR   H  8  69  ? 60.260  -105.493 59.931  1.00 85.10  ? 70  THR   H O   1 
ATOM   13588 C  CB  . THR   H  8  69  ? 58.512  -107.379 58.492  1.00 84.35  ? 70  THR   H CB  1 
ATOM   13589 O  OG1 . THR   H  8  69  ? 59.542  -108.246 58.019  1.00 84.30  ? 70  THR   H OG1 1 
ATOM   13590 C  CG2 . THR   H  8  69  ? 57.168  -107.839 57.970  1.00 83.68  ? 70  THR   H CG2 1 
ATOM   13591 N  N   . SER   H  8  70  ? 61.246  -105.282 57.881  1.00 87.27  ? 71  SER   H N   1 
ATOM   13592 C  CA  . SER   H  8  70  ? 62.615  -104.932 58.345  1.00 89.37  ? 71  SER   H CA  1 
ATOM   13593 C  C   . SER   H  8  70  ? 63.102  -105.986 59.349  1.00 88.14  ? 71  SER   H C   1 
ATOM   13594 O  O   . SER   H  8  70  ? 63.715  -105.616 60.366  1.00 84.40  ? 71  SER   H O   1 
ATOM   13595 C  CB  . SER   H  8  70  ? 62.635  -103.548 58.932  1.00 90.14  ? 71  SER   H CB  1 
ATOM   13596 O  OG  . SER   H  8  70  ? 62.135  -102.603 57.998  1.00 92.44  ? 71  SER   H OG  1 
ATOM   13597 N  N   . ARG   H  8  71  ? 62.832  -107.258 59.055  1.00 89.79  ? 72  ARG   H N   1 
ATOM   13598 C  CA  . ARG   H  8  71  ? 63.089  -108.410 59.960  1.00 92.53  ? 72  ARG   H CA  1 
ATOM   13599 C  C   . ARG   H  8  71  ? 63.631  -109.592 59.156  1.00 94.88  ? 72  ARG   H C   1 
ATOM   13600 O  O   . ARG   H  8  71  ? 63.235  -109.748 57.980  1.00 92.35  ? 72  ARG   H O   1 
ATOM   13601 C  CB  . ARG   H  8  71  ? 61.804  -108.846 60.668  1.00 91.05  ? 72  ARG   H CB  1 
ATOM   13602 C  CG  . ARG   H  8  71  ? 61.542  -108.124 61.979  1.00 89.92  ? 72  ARG   H CG  1 
ATOM   13603 C  CD  . ARG   H  8  71  ? 60.185  -108.482 62.544  1.00 90.16  ? 72  ARG   H CD  1 
ATOM   13604 N  NE  . ARG   H  8  71  ? 59.976  -107.823 63.821  1.00 92.89  ? 72  ARG   H NE  1 
ATOM   13605 C  CZ  . ARG   H  8  71  ? 59.685  -106.535 63.972  1.00 96.62  ? 72  ARG   H CZ  1 
ATOM   13606 N  NH1 . ARG   H  8  71  ? 59.557  -105.743 62.918  1.00 98.89  ? 72  ARG   H NH1 1 
ATOM   13607 N  NH2 . ARG   H  8  71  ? 59.525  -106.040 65.187  1.00 99.68  ? 72  ARG   H NH2 1 
ATOM   13608 N  N   . GLU   H  8  72  ? 64.476  -110.408 59.788  1.00 95.79  ? 73  GLU   H N   1 
ATOM   13609 C  CA  . GLU   H  8  72  ? 64.968  -111.683 59.212  1.00 94.61  ? 73  GLU   H CA  1 
ATOM   13610 C  C   . GLU   H  8  72  ? 63.799  -112.657 59.152  1.00 92.38  ? 73  GLU   H C   1 
ATOM   13611 O  O   . GLU   H  8  72  ? 63.038  -112.772 60.113  1.00 91.31  ? 73  GLU   H O   1 
ATOM   13612 C  CB  . GLU   H  8  72  ? 66.129  -112.236 60.034  1.00 99.66  ? 73  GLU   H CB  1 
ATOM   13613 C  CG  . GLU   H  8  72  ? 67.330  -111.311 60.049  1.00 107.64 ? 73  GLU   H CG  1 
ATOM   13614 C  CD  . GLU   H  8  72  ? 68.653  -111.987 59.730  1.00 117.30 ? 73  GLU   H CD  1 
ATOM   13615 O  OE1 . GLU   H  8  72  ? 68.927  -113.061 60.308  1.00 125.00 ? 73  GLU   H OE1 1 
ATOM   13616 O  OE2 . GLU   H  8  72  ? 69.403  -111.442 58.892  1.00 129.04 ? 73  GLU   H OE2 1 
ATOM   13617 N  N   . PRO   H  8  73  ? 63.613  -113.369 58.018  1.00 90.91  ? 74  PRO   H N   1 
ATOM   13618 C  CA  . PRO   H  8  73  ? 62.458  -114.246 57.840  1.00 91.50  ? 74  PRO   H CA  1 
ATOM   13619 C  C   . PRO   H  8  73  ? 62.506  -115.452 58.787  1.00 88.36  ? 74  PRO   H C   1 
ATOM   13620 O  O   . PRO   H  8  73  ? 63.593  -115.861 59.171  1.00 86.57  ? 74  PRO   H O   1 
ATOM   13621 C  CB  . PRO   H  8  73  ? 62.565  -114.691 56.375  1.00 91.90  ? 74  PRO   H CB  1 
ATOM   13622 C  CG  . PRO   H  8  73  ? 64.044  -114.584 56.066  1.00 92.67  ? 74  PRO   H CG  1 
ATOM   13623 C  CD  . PRO   H  8  73  ? 64.512  -113.379 56.853  1.00 91.50  ? 74  PRO   H CD  1 
ATOM   13624 N  N   . ARG   H  8  74  ? 61.330  -115.983 59.131  1.00 89.57  ? 75  ARG   H N   1 
ATOM   13625 C  CA  . ARG   H  8  74  ? 61.167  -117.135 60.056  1.00 91.27  ? 75  ARG   H CA  1 
ATOM   13626 C  C   . ARG   H  8  74  ? 60.797  -118.389 59.257  1.00 91.33  ? 75  ARG   H C   1 
ATOM   13627 O  O   . ARG   H  8  74  ? 60.153  -118.261 58.194  1.00 89.64  ? 75  ARG   H O   1 
ATOM   13628 C  CB  . ARG   H  8  74  ? 60.110  -116.808 61.111  1.00 88.55  ? 75  ARG   H CB  1 
ATOM   13629 C  CG  . ARG   H  8  74  ? 60.443  -115.573 61.930  1.00 88.91  ? 75  ARG   H CG  1 
ATOM   13630 C  CD  . ARG   H  8  74  ? 59.485  -115.370 63.082  1.00 89.65  ? 75  ARG   H CD  1 
ATOM   13631 N  NE  . ARG   H  8  74  ? 59.847  -114.202 63.871  1.00 91.72  ? 75  ARG   H NE  1 
ATOM   13632 C  CZ  . ARG   H  8  74  ? 59.231  -113.817 64.983  1.00 91.23  ? 75  ARG   H CZ  1 
ATOM   13633 N  NH1 . ARG   H  8  74  ? 58.211  -114.511 65.459  1.00 91.10  ? 75  ARG   H NH1 1 
ATOM   13634 N  NH2 . ARG   H  8  74  ? 59.640  -112.733 65.616  1.00 94.18  ? 75  ARG   H NH2 1 
ATOM   13635 N  N   . VAL   H  8  75  ? 61.199  -119.558 59.759  1.00 91.25  ? 76  VAL   H N   1 
ATOM   13636 C  CA  . VAL   H  8  75  ? 60.994  -120.870 59.079  1.00 88.84  ? 76  VAL   H CA  1 
ATOM   13637 C  C   . VAL   H  8  75  ? 59.491  -121.162 59.040  1.00 88.15  ? 76  VAL   H C   1 
ATOM   13638 O  O   . VAL   H  8  75  ? 59.029  -121.695 58.012  1.00 89.79  ? 76  VAL   H O   1 
ATOM   13639 C  CB  . VAL   H  8  75  ? 61.796  -121.997 59.758  1.00 89.48  ? 76  VAL   H CB  1 
ATOM   13640 C  CG1 . VAL   H  8  75  ? 61.564  -123.339 59.081  1.00 89.03  ? 76  VAL   H CG1 1 
ATOM   13641 C  CG2 . VAL   H  8  75  ? 63.286  -121.685 59.798  1.00 90.09  ? 76  VAL   H CG2 1 
ATOM   13642 N  N   . VAL   H  8  76  ? 58.759  -120.792 60.098  1.00 85.56  ? 77  VAL   H N   1 
ATOM   13643 C  CA  . VAL   H  8  76  ? 57.286  -121.023 60.218  1.00 82.92  ? 77  VAL   H CA  1 
ATOM   13644 C  C   . VAL   H  8  76  ? 56.526  -120.213 59.158  1.00 83.35  ? 77  VAL   H C   1 
ATOM   13645 O  O   . VAL   H  8  76  ? 55.434  -120.665 58.764  1.00 83.71  ? 77  VAL   H O   1 
ATOM   13646 C  CB  . VAL   H  8  76  ? 56.757  -120.709 61.629  1.00 81.91  ? 77  VAL   H CB  1 
ATOM   13647 C  CG1 . VAL   H  8  76  ? 57.255  -121.723 62.643  1.00 84.87  ? 77  VAL   H CG1 1 
ATOM   13648 C  CG2 . VAL   H  8  76  ? 57.077  -119.294 62.073  1.00 80.50  ? 77  VAL   H CG2 1 
ATOM   13649 N  N   . SER   H  8  77  ? 57.052  -119.060 58.730  1.00 82.69  ? 78  SER   H N   1 
ATOM   13650 C  CA  . SER   H  8  77  ? 56.443  -118.226 57.658  1.00 82.90  ? 78  SER   H CA  1 
ATOM   13651 C  C   . SER   H  8  77  ? 56.553  -118.970 56.322  1.00 81.05  ? 78  SER   H C   1 
ATOM   13652 O  O   . SER   H  8  77  ? 55.518  -119.117 55.643  1.00 79.51  ? 78  SER   H O   1 
ATOM   13653 C  CB  . SER   H  8  77  ? 57.060  -116.847 57.583  1.00 83.05  ? 78  SER   H CB  1 
ATOM   13654 O  OG  . SER   H  8  77  ? 56.805  -116.101 58.766  1.00 82.44  ? 78  SER   H OG  1 
ATOM   13655 N  N   . ALA   H  8  78  ? 57.756  -119.437 55.975  1.00 79.26  ? 79  ALA   H N   1 
ATOM   13656 C  CA  . ALA   H  8  78  ? 58.030  -120.252 54.768  1.00 78.99  ? 79  ALA   H CA  1 
ATOM   13657 C  C   . ALA   H  8  78  ? 57.186  -121.531 54.818  1.00 80.14  ? 79  ALA   H C   1 
ATOM   13658 O  O   . ALA   H  8  78  ? 56.641  -121.921 53.768  1.00 80.08  ? 79  ALA   H O   1 
ATOM   13659 C  CB  . ALA   H  8  78  ? 59.503  -120.564 54.667  1.00 77.95  ? 79  ALA   H CB  1 
ATOM   13660 N  N   . LEU   H  8  79  ? 57.070  -122.143 56.001  1.00 80.68  ? 80  LEU   H N   1 
ATOM   13661 C  CA  . LEU   H  8  79  ? 56.280  -123.383 56.233  1.00 81.51  ? 80  LEU   H CA  1 
ATOM   13662 C  C   . LEU   H  8  79  ? 54.796  -123.105 55.956  1.00 83.84  ? 80  LEU   H C   1 
ATOM   13663 O  O   . LEU   H  8  79  ? 54.168  -123.910 55.240  1.00 85.13  ? 80  LEU   H O   1 
ATOM   13664 C  CB  . LEU   H  8  79  ? 56.493  -123.864 57.672  1.00 82.50  ? 80  LEU   H CB  1 
ATOM   13665 C  CG  . LEU   H  8  79  ? 55.865  -125.215 58.019  1.00 82.57  ? 80  LEU   H CG  1 
ATOM   13666 C  CD1 . LEU   H  8  79  ? 56.644  -126.351 57.379  1.00 84.05  ? 80  LEU   H CD1 1 
ATOM   13667 C  CD2 . LEU   H  8  79  ? 55.788  -125.415 59.523  1.00 84.60  ? 80  LEU   H CD2 1 
ATOM   13668 N  N   . GLN   H  8  80  ? 54.263  -122.007 56.498  1.00 84.48  ? 81  GLN   H N   1 
ATOM   13669 C  CA  . GLN   H  8  80  ? 52.828  -121.634 56.377  1.00 85.13  ? 81  GLN   H CA  1 
ATOM   13670 C  C   . GLN   H  8  80  ? 52.510  -121.318 54.911  1.00 84.23  ? 81  GLN   H C   1 
ATOM   13671 O  O   . GLN   H  8  80  ? 51.467  -121.787 54.424  1.00 83.61  ? 81  GLN   H O   1 
ATOM   13672 C  CB  . GLN   H  8  80  ? 52.504  -120.437 57.272  1.00 86.07  ? 81  GLN   H CB  1 
ATOM   13673 C  CG  . GLN   H  8  80  ? 51.013  -120.225 57.487  1.00 87.13  ? 81  GLN   H CG  1 
ATOM   13674 C  CD  . GLN   H  8  80  ? 50.443  -121.134 58.548  1.00 87.98  ? 81  GLN   H CD  1 
ATOM   13675 O  OE1 . GLN   H  8  80  ? 50.997  -122.186 58.859  1.00 89.30  ? 81  GLN   H OE1 1 
ATOM   13676 N  NE2 . GLN   H  8  80  ? 49.321  -120.727 59.120  1.00 86.42  ? 81  GLN   H NE2 1 
ATOM   13677 N  N   . MET   H  8  81  ? 53.384  -120.556 54.246  1.00 86.86  ? 82  MET   H N   1 
ATOM   13678 C  CA  . MET   H  8  81  ? 53.193  -120.073 52.851  1.00 89.17  ? 82  MET   H CA  1 
ATOM   13679 C  C   . MET   H  8  81  ? 53.273  -121.254 51.874  1.00 88.11  ? 82  MET   H C   1 
ATOM   13680 O  O   . MET   H  8  81  ? 52.444  -121.295 50.942  1.00 91.86  ? 82  MET   H O   1 
ATOM   13681 C  CB  . MET   H  8  81  ? 54.240  -119.014 52.487  1.00 90.74  ? 82  MET   H CB  1 
ATOM   13682 C  CG  . MET   H  8  81  ? 54.016  -117.686 53.198  1.00 91.86  ? 82  MET   H CG  1 
ATOM   13683 S  SD  . MET   H  8  81  ? 55.461  -116.592 53.180  1.00 92.75  ? 82  MET   H SD  1 
ATOM   13684 C  CE  . MET   H  8  81  ? 55.473  -116.077 51.464  1.00 91.88  ? 82  MET   H CE  1 
ATOM   13685 N  N   . LEU   H  8  82  ? 54.222  -122.177 52.080  1.00 86.26  ? 83  LEU   H N   1 
ATOM   13686 C  CA  . LEU   H  8  82  ? 54.376  -123.409 51.254  1.00 81.69  ? 83  LEU   H CA  1 
ATOM   13687 C  C   . LEU   H  8  82  ? 53.125  -124.283 51.408  1.00 78.87  ? 83  LEU   H C   1 
ATOM   13688 O  O   . LEU   H  8  82  ? 52.558  -124.671 50.374  1.00 80.00  ? 83  LEU   H O   1 
ATOM   13689 C  CB  . LEU   H  8  82  ? 55.637  -124.179 51.668  1.00 79.55  ? 83  LEU   H CB  1 
ATOM   13690 C  CG  . LEU   H  8  82  ? 56.962  -123.614 51.155  1.00 78.94  ? 83  LEU   H CG  1 
ATOM   13691 C  CD1 . LEU   H  8  82  ? 58.140  -124.236 51.884  1.00 78.03  ? 83  LEU   H CD1 1 
ATOM   13692 C  CD2 . LEU   H  8  82  ? 57.103  -123.815 49.655  1.00 79.48  ? 83  LEU   H CD2 1 
ATOM   13693 N  N   . LYS   H  8  83  ? 52.704  -124.562 52.646  1.00 77.43  ? 84  LYS   H N   1 
ATOM   13694 C  CA  . LYS   H  8  83  ? 51.625  -125.543 52.945  1.00 79.25  ? 84  LYS   H CA  1 
ATOM   13695 C  C   . LYS   H  8  83  ? 50.279  -125.028 52.418  1.00 79.26  ? 84  LYS   H C   1 
ATOM   13696 O  O   . LYS   H  8  83  ? 49.478  -125.855 51.959  1.00 79.19  ? 84  LYS   H O   1 
ATOM   13697 C  CB  . LYS   H  8  83  ? 51.551  -125.864 54.442  1.00 80.96  ? 84  LYS   H CB  1 
ATOM   13698 C  CG  . LYS   H  8  83  ? 50.877  -124.820 55.321  1.00 83.01  ? 84  LYS   H CG  1 
ATOM   13699 C  CD  . LYS   H  8  83  ? 49.968  -125.412 56.372  1.00 85.52  ? 84  LYS   H CD  1 
ATOM   13700 C  CE  . LYS   H  8  83  ? 50.715  -126.282 57.356  1.00 88.38  ? 84  LYS   H CE  1 
ATOM   13701 N  NZ  . LYS   H  8  83  ? 49.812  -126.893 58.357  1.00 90.63  ? 84  LYS   H NZ  1 
ATOM   13702 N  N   . GLN   H  8  84  ? 50.037  -123.717 52.476  1.00 77.54  ? 85  GLN   H N   1 
ATOM   13703 C  CA  . GLN   H  8  84  ? 48.745  -123.108 52.057  1.00 78.90  ? 85  GLN   H CA  1 
ATOM   13704 C  C   . GLN   H  8  84  ? 48.678  -123.069 50.527  1.00 78.09  ? 85  GLN   H C   1 
ATOM   13705 O  O   . GLN   H  8  84  ? 47.557  -123.180 49.993  1.00 76.45  ? 85  GLN   H O   1 
ATOM   13706 C  CB  . GLN   H  8  84  ? 48.572  -121.721 52.675  1.00 78.36  ? 85  GLN   H CB  1 
ATOM   13707 C  CG  . GLN   H  8  84  ? 48.190  -121.774 54.148  1.00 81.37  ? 85  GLN   H CG  1 
ATOM   13708 C  CD  . GLN   H  8  84  ? 48.003  -120.415 54.778  1.00 81.65  ? 85  GLN   H CD  1 
ATOM   13709 O  OE1 . GLN   H  8  84  ? 48.109  -119.376 54.129  1.00 82.84  ? 85  GLN   H OE1 1 
ATOM   13710 N  NE2 . GLN   H  8  84  ? 47.721  -120.413 56.070  1.00 83.33  ? 85  GLN   H NE2 1 
ATOM   13711 N  N   . HIS   H  8  85  ? 49.831  -122.920 49.862  1.00 80.26  ? 86  HIS   H N   1 
ATOM   13712 C  CA  . HIS   H  8  85  ? 49.981  -122.962 48.382  1.00 82.18  ? 86  HIS   H CA  1 
ATOM   13713 C  C   . HIS   H  8  85  ? 49.755  -124.393 47.884  1.00 81.06  ? 86  HIS   H C   1 
ATOM   13714 O  O   . HIS   H  8  85  ? 48.976  -124.574 46.931  1.00 84.71  ? 86  HIS   H O   1 
ATOM   13715 C  CB  . HIS   H  8  85  ? 51.359  -122.435 47.954  1.00 82.65  ? 86  HIS   H CB  1 
ATOM   13716 C  CG  . HIS   H  8  85  ? 51.542  -122.368 46.474  1.00 85.13  ? 86  HIS   H CG  1 
ATOM   13717 N  ND1 . HIS   H  8  85  ? 50.978  -121.367 45.705  1.00 84.69  ? 86  HIS   H ND1 1 
ATOM   13718 C  CD2 . HIS   H  8  85  ? 52.213  -123.171 45.620  1.00 87.58  ? 86  HIS   H CD2 1 
ATOM   13719 C  CE1 . HIS   H  8  85  ? 51.296  -121.558 44.440  1.00 85.70  ? 86  HIS   H CE1 1 
ATOM   13720 N  NE2 . HIS   H  8  85  ? 52.054  -122.658 44.361  1.00 88.45  ? 86  HIS   H NE2 1 
ATOM   13721 N  N   . LEU   H  8  86  ? 50.421  -125.368 48.508  1.00 77.28  ? 87  LEU   H N   1 
ATOM   13722 C  CA  . LEU   H  8  86  ? 50.340  -126.796 48.115  1.00 75.02  ? 87  LEU   H CA  1 
ATOM   13723 C  C   . LEU   H  8  86  ? 48.919  -127.309 48.366  1.00 75.12  ? 87  LEU   H C   1 
ATOM   13724 O  O   . LEU   H  8  86  ? 48.400  -128.007 47.473  1.00 75.53  ? 87  LEU   H O   1 
ATOM   13725 C  CB  . LEU   H  8  86  ? 51.391  -127.595 48.887  1.00 73.76  ? 87  LEU   H CB  1 
ATOM   13726 C  CG  . LEU   H  8  86  ? 52.831  -127.398 48.415  1.00 75.38  ? 87  LEU   H CG  1 
ATOM   13727 C  CD1 . LEU   H  8  86  ? 53.799  -128.175 49.292  1.00 77.22  ? 87  LEU   H CD1 1 
ATOM   13728 C  CD2 . LEU   H  8  86  ? 52.993  -127.814 46.963  1.00 76.51  ? 87  LEU   H CD2 1 
ATOM   13729 N  N   . PHE   H  8  87  ? 48.306  -126.957 49.504  1.00 73.59  ? 88  PHE   H N   1 
ATOM   13730 C  CA  . PHE   H  8  87  ? 46.938  -127.400 49.890  1.00 76.90  ? 88  PHE   H CA  1 
ATOM   13731 C  C   . PHE   H  8  87  ? 45.913  -126.896 48.874  1.00 79.36  ? 88  PHE   H C   1 
ATOM   13732 O  O   . PHE   H  8  87  ? 44.966  -127.632 48.546  1.00 85.55  ? 88  PHE   H O   1 
ATOM   13733 C  CB  . PHE   H  8  87  ? 46.513  -126.891 51.268  1.00 75.47  ? 88  PHE   H CB  1 
ATOM   13734 C  CG  . PHE   H  8  87  ? 45.135  -127.356 51.666  1.00 74.16  ? 88  PHE   H CG  1 
ATOM   13735 C  CD1 . PHE   H  8  87  ? 44.950  -128.618 52.207  1.00 76.22  ? 88  PHE   H CD1 1 
ATOM   13736 C  CD2 . PHE   H  8  87  ? 44.020  -126.560 51.457  1.00 71.76  ? 88  PHE   H CD2 1 
ATOM   13737 C  CE1 . PHE   H  8  87  ? 43.684  -129.060 52.556  1.00 76.03  ? 88  PHE   H CE1 1 
ATOM   13738 C  CE2 . PHE   H  8  87  ? 42.755  -127.004 51.808  1.00 70.96  ? 88  PHE   H CE2 1 
ATOM   13739 C  CZ  . PHE   H  8  87  ? 42.589  -128.252 52.358  1.00 72.51  ? 88  PHE   H CZ  1 
ATOM   13740 N  N   . LYS   H  8  88  ? 46.091  -125.655 48.426  1.00 83.34  ? 89  LYS   H N   1 
ATOM   13741 C  CA  . LYS   H  8  88  ? 45.216  -124.973 47.437  1.00 86.30  ? 89  LYS   H CA  1 
ATOM   13742 C  C   . LYS   H  8  88  ? 45.175  -125.767 46.124  1.00 82.94  ? 89  LYS   H C   1 
ATOM   13743 O  O   . LYS   H  8  88  ? 44.140  -125.692 45.440  1.00 78.71  ? 89  LYS   H O   1 
ATOM   13744 C  CB  . LYS   H  8  88  ? 45.735  -123.555 47.194  1.00 92.05  ? 89  LYS   H CB  1 
ATOM   13745 C  CG  . LYS   H  8  88  ? 44.864  -122.681 46.304  1.00 96.53  ? 89  LYS   H CG  1 
ATOM   13746 C  CD  . LYS   H  8  88  ? 45.325  -121.240 46.267  1.00 105.18 ? 89  LYS   H CD  1 
ATOM   13747 C  CE  . LYS   H  8  88  ? 46.632  -121.053 45.522  1.00 112.69 ? 89  LYS   H CE  1 
ATOM   13748 N  NZ  . LYS   H  8  88  ? 47.224  -119.718 45.773  1.00 119.77 ? 89  LYS   H NZ  1 
ATOM   13749 N  N   . TYR   H  8  89  ? 46.257  -126.483 45.790  1.00 85.33  ? 90  TYR   H N   1 
ATOM   13750 C  CA  . TYR   H  8  89  ? 46.420  -127.253 44.525  1.00 88.94  ? 90  TYR   H CA  1 
ATOM   13751 C  C   . TYR   H  8  89  ? 46.162  -128.753 44.741  1.00 91.25  ? 90  TYR   H C   1 
ATOM   13752 O  O   . TYR   H  8  89  ? 46.475  -129.547 43.829  1.00 93.28  ? 90  TYR   H O   1 
ATOM   13753 C  CB  . TYR   H  8  89  ? 47.805  -126.988 43.929  1.00 87.44  ? 90  TYR   H CB  1 
ATOM   13754 C  CG  . TYR   H  8  89  ? 47.876  -125.700 43.153  1.00 84.87  ? 90  TYR   H CG  1 
ATOM   13755 C  CD1 . TYR   H  8  89  ? 47.632  -125.680 41.791  1.00 86.77  ? 90  TYR   H CD1 1 
ATOM   13756 C  CD2 . TYR   H  8  89  ? 48.146  -124.498 43.780  1.00 85.32  ? 90  TYR   H CD2 1 
ATOM   13757 C  CE1 . TYR   H  8  89  ? 47.673  -124.501 41.065  1.00 86.90  ? 90  TYR   H CE1 1 
ATOM   13758 C  CE2 . TYR   H  8  89  ? 48.192  -123.309 43.071  1.00 87.46  ? 90  TYR   H CE2 1 
ATOM   13759 C  CZ  . TYR   H  8  89  ? 47.954  -123.311 41.708  1.00 86.52  ? 90  TYR   H CZ  1 
ATOM   13760 O  OH  . TYR   H  8  89  ? 47.996  -122.155 40.988  1.00 92.51  ? 90  TYR   H OH  1 
ATOM   13761 N  N   . GLN   H  8  90  ? 45.607  -129.130 45.898  1.00 92.27  ? 91  GLN   H N   1 
ATOM   13762 C  CA  . GLN   H  8  90  ? 45.070  -130.489 46.178  1.00 90.70  ? 91  GLN   H CA  1 
ATOM   13763 C  C   . GLN   H  8  90  ? 46.033  -131.568 45.658  1.00 91.04  ? 91  GLN   H C   1 
ATOM   13764 O  O   . GLN   H  8  90  ? 45.549  -132.555 45.068  1.00 90.13  ? 91  GLN   H O   1 
ATOM   13765 C  CB  . GLN   H  8  90  ? 43.684  -130.624 45.541  1.00 93.76  ? 91  GLN   H CB  1 
ATOM   13766 C  CG  . GLN   H  8  90  ? 42.615  -129.772 46.213  1.00 96.21  ? 91  GLN   H CG  1 
ATOM   13767 C  CD  . GLN   H  8  90  ? 42.237  -130.284 47.583  1.00 99.55  ? 91  GLN   H CD  1 
ATOM   13768 O  OE1 . GLN   H  8  90  ? 42.000  -131.475 47.785  1.00 105.43 ? 91  GLN   H OE1 1 
ATOM   13769 N  NE2 . GLN   H  8  90  ? 42.167  -129.380 48.547  1.00 98.26  ? 91  GLN   H NE2 1 
ATOM   13770 N  N   . GLY   H  8  91  ? 47.342  -131.385 45.865  1.00 90.45  ? 92  GLY   H N   1 
ATOM   13771 C  CA  . GLY   H  8  91  ? 48.372  -132.409 45.595  1.00 88.96  ? 92  GLY   H CA  1 
ATOM   13772 C  C   . GLY   H  8  91  ? 48.867  -132.406 44.157  1.00 86.61  ? 92  GLY   H C   1 
ATOM   13773 O  O   . GLY   H  8  91  ? 49.843  -133.131 43.881  1.00 82.04  ? 92  GLY   H O   1 
ATOM   13774 N  N   . HIS   H  8  92  ? 48.242  -131.630 43.265  1.00 84.15  ? 93  HIS   H N   1 
ATOM   13775 C  CA  . HIS   H  8  92  ? 48.581  -131.597 41.815  1.00 86.41  ? 93  HIS   H CA  1 
ATOM   13776 C  C   . HIS   H  8  92  ? 49.983  -131.011 41.611  1.00 89.88  ? 93  HIS   H C   1 
ATOM   13777 O  O   . HIS   H  8  92  ? 50.634  -131.392 40.621  1.00 96.31  ? 93  HIS   H O   1 
ATOM   13778 C  CB  . HIS   H  8  92  ? 47.517  -130.845 41.008  1.00 85.34  ? 93  HIS   H CB  1 
ATOM   13779 C  CG  . HIS   H  8  92  ? 46.228  -131.585 40.893  1.00 87.22  ? 93  HIS   H CG  1 
ATOM   13780 N  ND1 . HIS   H  8  92  ? 46.082  -132.695 40.081  1.00 90.62  ? 93  HIS   H ND1 1 
ATOM   13781 C  CD2 . HIS   H  8  92  ? 45.031  -131.387 41.485  1.00 88.55  ? 93  HIS   H CD2 1 
ATOM   13782 C  CE1 . HIS   H  8  92  ? 44.849  -133.149 40.180  1.00 90.09  ? 93  HIS   H CE1 1 
ATOM   13783 N  NE2 . HIS   H  8  92  ? 44.183  -132.362 41.032  1.00 90.38  ? 93  HIS   H NE2 1 
ATOM   13784 N  N   . ILE   H  8  93  ? 50.424  -130.117 42.501  1.00 89.57  ? 94  ILE   H N   1 
ATOM   13785 C  CA  . ILE   H  8  93  ? 51.853  -129.698 42.608  1.00 89.64  ? 94  ILE   H CA  1 
ATOM   13786 C  C   . ILE   H  8  93  ? 52.566  -130.720 43.500  1.00 89.96  ? 94  ILE   H C   1 
ATOM   13787 O  O   . ILE   H  8  93  ? 52.440  -130.620 44.740  1.00 93.67  ? 94  ILE   H O   1 
ATOM   13788 C  CB  . ILE   H  8  93  ? 51.982  -128.254 43.128  1.00 88.20  ? 94  ILE   H CB  1 
ATOM   13789 C  CG1 . ILE   H  8  93  ? 51.355  -127.267 42.141  1.00 89.74  ? 94  ILE   H CG1 1 
ATOM   13790 C  CG2 . ILE   H  8  93  ? 53.436  -127.910 43.421  1.00 86.87  ? 94  ILE   H CG2 1 
ATOM   13791 C  CD1 . ILE   H  8  93  ? 51.317  -125.834 42.620  1.00 90.73  ? 94  ILE   H CD1 1 
ATOM   13792 N  N   . GLY   H  8  94  ? 53.269  -131.672 42.873  1.00 90.59  ? 95  GLY   H N   1 
ATOM   13793 C  CA  . GLY   H  8  94  ? 53.917  -132.819 43.536  1.00 88.28  ? 95  GLY   H CA  1 
ATOM   13794 C  C   . GLY   H  8  94  ? 55.256  -132.438 44.134  1.00 84.62  ? 95  GLY   H C   1 
ATOM   13795 O  O   . GLY   H  8  94  ? 56.280  -133.003 43.699  1.00 84.08  ? 95  GLY   H O   1 
ATOM   13796 N  N   . ALA   H  8  95  ? 55.242  -131.512 45.094  1.00 83.41  ? 96  ALA   H N   1 
ATOM   13797 C  CA  . ALA   H  8  95  ? 56.417  -131.105 45.893  1.00 83.08  ? 96  ALA   H CA  1 
ATOM   13798 C  C   . ALA   H  8  95  ? 56.330  -131.784 47.261  1.00 81.26  ? 96  ALA   H C   1 
ATOM   13799 O  O   . ALA   H  8  95  ? 55.298  -131.625 47.936  1.00 81.90  ? 96  ALA   H O   1 
ATOM   13800 C  CB  . ALA   H  8  95  ? 56.469  -129.604 46.015  1.00 83.71  ? 96  ALA   H CB  1 
ATOM   13801 N  N   . TYR   H  8  96  ? 57.356  -132.555 47.617  1.00 83.09  ? 97  TYR   H N   1 
ATOM   13802 C  CA  . TYR   H  8  96  ? 57.577  -133.098 48.981  1.00 85.30  ? 97  TYR   H CA  1 
ATOM   13803 C  C   . TYR   H  8  96  ? 58.864  -132.458 49.504  1.00 86.70  ? 97  TYR   H C   1 
ATOM   13804 O  O   . TYR   H  8  96  ? 59.928  -132.703 48.911  1.00 92.79  ? 97  TYR   H O   1 
ATOM   13805 C  CB  . TYR   H  8  96  ? 57.608  -134.629 48.952  1.00 85.75  ? 97  TYR   H CB  1 
ATOM   13806 C  CG  . TYR   H  8  96  ? 56.342  -135.241 48.408  1.00 83.30  ? 97  TYR   H CG  1 
ATOM   13807 C  CD1 . TYR   H  8  96  ? 56.157  -135.398 47.044  1.00 84.71  ? 97  TYR   H CD1 1 
ATOM   13808 C  CD2 . TYR   H  8  96  ? 55.313  -135.631 49.251  1.00 82.32  ? 97  TYR   H CD2 1 
ATOM   13809 C  CE1 . TYR   H  8  96  ? 54.990  -135.940 46.531  1.00 85.72  ? 97  TYR   H CE1 1 
ATOM   13810 C  CE2 . TYR   H  8  96  ? 54.141  -136.182 48.755  1.00 83.51  ? 97  TYR   H CE2 1 
ATOM   13811 C  CZ  . TYR   H  8  96  ? 53.977  -136.332 47.389  1.00 84.34  ? 97  TYR   H CZ  1 
ATOM   13812 O  OH  . TYR   H  8  96  ? 52.822  -136.859 46.893  1.00 86.89  ? 97  TYR   H OH  1 
ATOM   13813 N  N   . LEU   H  8  97  ? 58.755  -131.632 50.547  1.00 85.48  ? 98  LEU   H N   1 
ATOM   13814 C  CA  . LEU   H  8  97  ? 59.852  -130.745 51.008  1.00 87.61  ? 98  LEU   H CA  1 
ATOM   13815 C  C   . LEU   H  8  97  ? 60.212  -131.063 52.461  1.00 82.96  ? 98  LEU   H C   1 
ATOM   13816 O  O   . LEU   H  8  97  ? 59.300  -131.388 53.243  1.00 83.83  ? 98  LEU   H O   1 
ATOM   13817 C  CB  . LEU   H  8  97  ? 59.397  -129.289 50.868  1.00 88.71  ? 98  LEU   H CB  1 
ATOM   13818 C  CG  . LEU   H  8  97  ? 58.885  -128.877 49.487  1.00 91.15  ? 98  LEU   H CG  1 
ATOM   13819 C  CD1 . LEU   H  8  97  ? 58.152  -127.548 49.561  1.00 91.48  ? 98  LEU   H CD1 1 
ATOM   13820 C  CD2 . LEU   H  8  97  ? 60.021  -128.803 48.479  1.00 91.44  ? 98  LEU   H CD2 1 
ATOM   13821 N  N   . ILE   H  8  98  ? 61.503  -130.973 52.787  1.00 84.88  ? 99  ILE   H N   1 
ATOM   13822 C  CA  . ILE   H  8  98  ? 62.026  -130.829 54.177  1.00 90.95  ? 99  ILE   H CA  1 
ATOM   13823 C  C   . ILE   H  8  98  ? 62.513  -129.384 54.330  1.00 91.47  ? 99  ILE   H C   1 
ATOM   13824 O  O   . ILE   H  8  98  ? 63.514  -129.030 53.675  1.00 94.97  ? 99  ILE   H O   1 
ATOM   13825 C  CB  . ILE   H  8  98  ? 63.130  -131.865 54.471  1.00 92.10  ? 99  ILE   H CB  1 
ATOM   13826 C  CG1 . ILE   H  8  98  ? 62.532  -133.271 54.585  1.00 93.04  ? 99  ILE   H CG1 1 
ATOM   13827 C  CG2 . ILE   H  8  98  ? 63.930  -131.476 55.709  1.00 94.08  ? 99  ILE   H CG2 1 
ATOM   13828 C  CD1 . ILE   H  8  98  ? 63.505  -134.346 55.022  1.00 94.75  ? 99  ILE   H CD1 1 
ATOM   13829 N  N   . VAL   H  8  99  ? 61.807  -128.589 55.140  1.00 90.87  ? 100 VAL   H N   1 
ATOM   13830 C  CA  . VAL   H  8  99  ? 62.097  -127.146 55.388  1.00 89.99  ? 100 VAL   H CA  1 
ATOM   13831 C  C   . VAL   H  8  99  ? 62.863  -127.043 56.707  1.00 87.97  ? 100 VAL   H C   1 
ATOM   13832 O  O   . VAL   H  8  99  ? 62.367  -127.586 57.711  1.00 84.81  ? 100 VAL   H O   1 
ATOM   13833 C  CB  . VAL   H  8  99  ? 60.806  -126.308 55.426  1.00 90.79  ? 100 VAL   H CB  1 
ATOM   13834 C  CG1 . VAL   H  8  99  ? 61.104  -124.818 55.415  1.00 91.43  ? 100 VAL   H CG1 1 
ATOM   13835 C  CG2 . VAL   H  8  99  ? 59.866  -126.666 54.287  1.00 91.24  ? 100 VAL   H CG2 1 
ATOM   13836 N  N   . ALA   H  8  100 ? 64.022  -126.379 56.695  1.00 90.14  ? 101 ALA   H N   1 
ATOM   13837 C  CA  . ALA   H  8  100 ? 64.889  -126.175 57.880  1.00 91.41  ? 101 ALA   H CA  1 
ATOM   13838 C  C   . ALA   H  8  100 ? 65.565  -124.802 57.821  1.00 90.37  ? 101 ALA   H C   1 
ATOM   13839 O  O   . ALA   H  8  100 ? 65.609  -124.200 56.734  1.00 90.96  ? 101 ALA   H O   1 
ATOM   13840 C  CB  . ALA   H  8  100 ? 65.908  -127.281 57.957  1.00 94.40  ? 101 ALA   H CB  1 
ATOM   13841 N  N   . GLY   H  8  101 ? 66.061  -124.325 58.963  1.00 87.95  ? 102 GLY   H N   1 
ATOM   13842 C  CA  . GLY   H  8  101 ? 66.833  -123.072 59.053  1.00 89.28  ? 102 GLY   H CA  1 
ATOM   13843 C  C   . GLY   H  8  101 ? 66.835  -122.489 60.451  1.00 89.62  ? 102 GLY   H C   1 
ATOM   13844 O  O   . GLY   H  8  101 ? 66.198  -123.072 61.351  1.00 86.76  ? 102 GLY   H O   1 
ATOM   13845 N  N   . VAL   H  8  102 ? 67.531  -121.363 60.613  1.00 92.68  ? 103 VAL   H N   1 
ATOM   13846 C  CA  . VAL   H  8  102 ? 67.642  -120.603 61.891  1.00 93.15  ? 103 VAL   H CA  1 
ATOM   13847 C  C   . VAL   H  8  102 ? 67.057  -119.205 61.668  1.00 94.54  ? 103 VAL   H C   1 
ATOM   13848 O  O   . VAL   H  8  102 ? 67.196  -118.673 60.547  1.00 90.28  ? 103 VAL   H O   1 
ATOM   13849 C  CB  . VAL   H  8  102 ? 69.097  -120.553 62.396  1.00 93.71  ? 103 VAL   H CB  1 
ATOM   13850 C  CG1 . VAL   H  8  102 ? 69.602  -121.938 62.762  1.00 93.73  ? 103 VAL   H CG1 1 
ATOM   13851 C  CG2 . VAL   H  8  102 ? 70.042  -119.890 61.403  1.00 94.29  ? 103 VAL   H CG2 1 
ATOM   13852 N  N   . ASP   H  8  103 ? 66.410  -118.658 62.698  1.00 94.27  ? 104 ASP   H N   1 
ATOM   13853 C  CA  . ASP   H  8  103 ? 65.782  -117.311 62.688  1.00 99.33  ? 104 ASP   H CA  1 
ATOM   13854 C  C   . ASP   H  8  103 ? 65.854  -116.750 64.106  1.00 101.42 ? 104 ASP   H C   1 
ATOM   13855 O  O   . ASP   H  8  103 ? 66.265  -117.457 65.024  1.00 97.37  ? 104 ASP   H O   1 
ATOM   13856 C  CB  . ASP   H  8  103 ? 64.360  -117.401 62.123  1.00 98.61  ? 104 ASP   H CB  1 
ATOM   13857 C  CG  . ASP   H  8  103 ? 63.469  -118.389 62.858  1.00 97.48  ? 104 ASP   H CG  1 
ATOM   13858 O  OD1 . ASP   H  8  103 ? 63.488  -118.380 64.103  1.00 88.53  ? 104 ASP   H OD1 1 
ATOM   13859 O  OD2 . ASP   H  8  103 ? 62.770  -119.168 62.178  1.00 101.27 ? 104 ASP   H OD2 1 
ATOM   13860 N  N   . PRO   H  8  104 ? 65.473  -115.470 64.335  1.00 107.06 ? 105 PRO   H N   1 
ATOM   13861 C  CA  . PRO   H  8  104 ? 65.445  -114.908 65.688  1.00 109.22 ? 105 PRO   H CA  1 
ATOM   13862 C  C   . PRO   H  8  104 ? 64.794  -115.811 66.753  1.00 107.28 ? 105 PRO   H C   1 
ATOM   13863 O  O   . PRO   H  8  104 ? 65.171  -115.700 67.904  1.00 110.73 ? 105 PRO   H O   1 
ATOM   13864 C  CB  . PRO   H  8  104 ? 64.640  -113.610 65.498  1.00 112.23 ? 105 PRO   H CB  1 
ATOM   13865 C  CG  . PRO   H  8  104 ? 64.955  -113.185 64.078  1.00 111.66 ? 105 PRO   H CG  1 
ATOM   13866 C  CD  . PRO   H  8  104 ? 65.093  -114.482 63.308  1.00 109.54 ? 105 PRO   H CD  1 
ATOM   13867 N  N   . THR   H  8  105 ? 63.859  -116.684 66.358  1.00 105.32 ? 106 THR   H N   1 
ATOM   13868 C  CA  . THR   H  8  105 ? 63.072  -117.562 67.270  1.00 106.57 ? 106 THR   H CA  1 
ATOM   13869 C  C   . THR   H  8  105 ? 63.907  -118.779 67.696  1.00 103.66 ? 106 THR   H C   1 
ATOM   13870 O  O   . THR   H  8  105 ? 63.649  -119.305 68.797  1.00 101.92 ? 106 THR   H O   1 
ATOM   13871 C  CB  . THR   H  8  105 ? 61.743  -117.972 66.620  1.00 110.16 ? 106 THR   H CB  1 
ATOM   13872 O  OG1 . THR   H  8  105 ? 60.941  -116.798 66.482  1.00 114.59 ? 106 THR   H OG1 1 
ATOM   13873 C  CG2 . THR   H  8  105 ? 60.979  -119.011 67.410  1.00 110.36 ? 106 THR   H CG2 1 
ATOM   13874 N  N   . GLY   H  8  106 ? 64.856  -119.213 66.860  1.00 106.32 ? 107 GLY   H N   1 
ATOM   13875 C  CA  . GLY   H  8  106 ? 65.713  -120.392 67.106  1.00 108.09 ? 107 GLY   H CA  1 
ATOM   13876 C  C   . GLY   H  8  106 ? 65.936  -121.196 65.836  1.00 108.62 ? 107 GLY   H C   1 
ATOM   13877 O  O   . GLY   H  8  106 ? 65.772  -120.621 64.739  1.00 109.71 ? 107 GLY   H O   1 
ATOM   13878 N  N   . SER   H  8  107 ? 66.298  -122.477 65.973  1.00 109.53 ? 108 SER   H N   1 
ATOM   13879 C  CA  . SER   H  8  107 ? 66.527  -123.429 64.851  1.00 107.79 ? 108 SER   H CA  1 
ATOM   13880 C  C   . SER   H  8  107 ? 65.321  -124.368 64.715  1.00 102.26 ? 108 SER   H C   1 
ATOM   13881 O  O   . SER   H  8  107 ? 64.757  -124.760 65.756  1.00 95.93  ? 108 SER   H O   1 
ATOM   13882 C  CB  . SER   H  8  107 ? 67.810  -124.200 65.038  1.00 110.74 ? 108 SER   H CB  1 
ATOM   13883 O  OG  . SER   H  8  107 ? 67.607  -125.337 65.865  1.00 116.42 ? 108 SER   H OG  1 
ATOM   13884 N  N   . HIS   H  8  108 ? 64.950  -124.719 63.478  1.00 101.73 ? 109 HIS   H N   1 
ATOM   13885 C  CA  . HIS   H  8  108 ? 63.682  -125.424 63.144  1.00 99.79  ? 109 HIS   H CA  1 
ATOM   13886 C  C   . HIS   H  8  108 ? 63.905  -126.495 62.072  1.00 98.52  ? 109 HIS   H C   1 
ATOM   13887 O  O   . HIS   H  8  108 ? 64.762  -126.291 61.190  1.00 98.06  ? 109 HIS   H O   1 
ATOM   13888 C  CB  . HIS   H  8  108 ? 62.625  -124.422 62.674  1.00 102.40 ? 109 HIS   H CB  1 
ATOM   13889 C  CG  . HIS   H  8  108 ? 62.378  -123.317 63.641  1.00 107.22 ? 109 HIS   H CG  1 
ATOM   13890 N  ND1 . HIS   H  8  108 ? 61.566  -123.473 64.747  1.00 109.78 ? 109 HIS   H ND1 1 
ATOM   13891 C  CD2 . HIS   H  8  108 ? 62.836  -122.047 63.675  1.00 116.24 ? 109 HIS   H CD2 1 
ATOM   13892 C  CE1 . HIS   H  8  108 ? 61.532  -122.341 65.422  1.00 118.79 ? 109 HIS   H CE1 1 
ATOM   13893 N  NE2 . HIS   H  8  108 ? 62.303  -121.450 64.784  1.00 122.69 ? 109 HIS   H NE2 1 
ATOM   13894 N  N   . LEU   H  8  109 ? 63.132  -127.582 62.150  1.00 95.18  ? 110 LEU   H N   1 
ATOM   13895 C  CA  . LEU   H  8  109 ? 63.097  -128.679 61.146  1.00 95.23  ? 110 LEU   H CA  1 
ATOM   13896 C  C   . LEU   H  8  109 ? 61.648  -129.136 60.942  1.00 89.32  ? 110 LEU   H C   1 
ATOM   13897 O  O   . LEU   H  8  109 ? 61.007  -129.568 61.923  1.00 84.77  ? 110 LEU   H O   1 
ATOM   13898 C  CB  . LEU   H  8  109 ? 63.974  -129.843 61.620  1.00 95.86  ? 110 LEU   H CB  1 
ATOM   13899 C  CG  . LEU   H  8  109 ? 64.034  -131.049 60.680  1.00 95.61  ? 110 LEU   H CG  1 
ATOM   13900 C  CD1 . LEU   H  8  109 ? 64.595  -130.659 59.319  1.00 95.75  ? 110 LEU   H CD1 1 
ATOM   13901 C  CD2 . LEU   H  8  109 ? 64.859  -132.172 61.287  1.00 94.16  ? 110 LEU   H CD2 1 
ATOM   13902 N  N   . PHE   H  8  110 ? 61.166  -129.052 59.702  1.00 85.68  ? 111 PHE   H N   1 
ATOM   13903 C  CA  . PHE   H  8  110 ? 59.793  -129.439 59.297  1.00 86.14  ? 111 PHE   H CA  1 
ATOM   13904 C  C   . PHE   H  8  110 ? 59.851  -130.278 58.020  1.00 84.79  ? 111 PHE   H C   1 
ATOM   13905 O  O   . PHE   H  8  110 ? 60.896  -130.306 57.345  1.00 87.11  ? 111 PHE   H O   1 
ATOM   13906 C  CB  . PHE   H  8  110 ? 58.927  -128.204 59.051  1.00 85.00  ? 111 PHE   H CB  1 
ATOM   13907 C  CG  . PHE   H  8  110 ? 58.823  -127.260 60.219  1.00 87.66  ? 111 PHE   H CG  1 
ATOM   13908 C  CD1 . PHE   H  8  110 ? 58.122  -127.617 61.360  1.00 90.07  ? 111 PHE   H CD1 1 
ATOM   13909 C  CD2 . PHE   H  8  110 ? 59.419  -126.009 60.175  1.00 90.67  ? 111 PHE   H CD2 1 
ATOM   13910 C  CE1 . PHE   H  8  110 ? 58.025  -126.745 62.434  1.00 92.36  ? 111 PHE   H CE1 1 
ATOM   13911 C  CE2 . PHE   H  8  110 ? 59.320  -125.137 61.248  1.00 92.93  ? 111 PHE   H CE2 1 
ATOM   13912 C  CZ  . PHE   H  8  110 ? 58.623  -125.506 62.376  1.00 94.10  ? 111 PHE   H CZ  1 
ATOM   13913 N  N   . SER   H  8  111 ? 58.735  -130.930 57.705  1.00 85.71  ? 112 SER   H N   1 
ATOM   13914 C  CA  . SER   H  8  111 ? 58.503  -131.677 56.444  1.00 88.92  ? 112 SER   H CA  1 
ATOM   13915 C  C   . SER   H  8  111 ? 57.146  -131.248 55.877  1.00 85.03  ? 112 SER   H C   1 
ATOM   13916 O  O   . SER   H  8  111 ? 56.227  -131.003 56.683  1.00 80.94  ? 112 SER   H O   1 
ATOM   13917 C  CB  . SER   H  8  111 ? 58.578  -133.169 56.676  1.00 91.99  ? 112 SER   H CB  1 
ATOM   13918 O  OG  . SER   H  8  111 ? 57.312  -133.702 57.041  1.00 93.04  ? 112 SER   H OG  1 
ATOM   13919 N  N   . ILE   H  8  112 ? 57.034  -131.129 54.552  1.00 85.82  ? 113 ILE   H N   1 
ATOM   13920 C  CA  . ILE   H  8  112 ? 55.761  -130.755 53.865  1.00 90.23  ? 113 ILE   H CA  1 
ATOM   13921 C  C   . ILE   H  8  112 ? 55.465  -131.772 52.762  1.00 89.92  ? 113 ILE   H C   1 
ATOM   13922 O  O   . ILE   H  8  112 ? 56.358  -132.021 51.931  1.00 87.67  ? 113 ILE   H O   1 
ATOM   13923 C  CB  . ILE   H  8  112 ? 55.806  -129.327 53.291  1.00 91.99  ? 113 ILE   H CB  1 
ATOM   13924 C  CG1 . ILE   H  8  112 ? 56.441  -128.333 54.269  1.00 96.10  ? 113 ILE   H CG1 1 
ATOM   13925 C  CG2 . ILE   H  8  112 ? 54.406  -128.902 52.865  1.00 88.92  ? 113 ILE   H CG2 1 
ATOM   13926 C  CD1 . ILE   H  8  112 ? 56.493  -126.912 53.755  1.00 97.12  ? 113 ILE   H CD1 1 
ATOM   13927 N  N   . HIS   H  8  113 ? 54.233  -132.288 52.751  1.00 94.63  ? 114 HIS   H N   1 
ATOM   13928 C  CA  . HIS   H  8  113 ? 53.694  -133.223 51.728  1.00 98.77  ? 114 HIS   H CA  1 
ATOM   13929 C  C   . HIS   H  8  113 ? 52.915  -132.418 50.678  1.00 92.25  ? 114 HIS   H C   1 
ATOM   13930 O  O   . HIS   H  8  113 ? 52.396  -131.335 51.021  1.00 90.75  ? 114 HIS   H O   1 
ATOM   13931 C  CB  . HIS   H  8  113 ? 52.847  -134.319 52.398  1.00 105.66 ? 114 HIS   H CB  1 
ATOM   13932 C  CG  . HIS   H  8  113 ? 53.648  -135.432 52.995  1.00 114.27 ? 114 HIS   H CG  1 
ATOM   13933 N  ND1 . HIS   H  8  113 ? 54.541  -135.232 54.034  1.00 118.93 ? 114 HIS   H ND1 1 
ATOM   13934 C  CD2 . HIS   H  8  113 ? 53.683  -136.755 52.717  1.00 118.94 ? 114 HIS   H CD2 1 
ATOM   13935 C  CE1 . HIS   H  8  113 ? 55.098  -136.383 54.362  1.00 123.17 ? 114 HIS   H CE1 1 
ATOM   13936 N  NE2 . HIS   H  8  113 ? 54.586  -137.334 53.569  1.00 119.39 ? 114 HIS   H NE2 1 
ATOM   13937 N  N   . ALA   H  8  114 ? 52.838  -132.945 49.451  1.00 90.28  ? 115 ALA   H N   1 
ATOM   13938 C  CA  . ALA   H  8  114 ? 52.230  -132.309 48.258  1.00 85.40  ? 115 ALA   H CA  1 
ATOM   13939 C  C   . ALA   H  8  114 ? 50.782  -131.884 48.537  1.00 82.24  ? 115 ALA   H C   1 
ATOM   13940 O  O   . ALA   H  8  114 ? 50.360  -130.857 47.980  1.00 79.46  ? 115 ALA   H O   1 
ATOM   13941 C  CB  . ALA   H  8  114 ? 52.300  -133.260 47.088  1.00 86.66  ? 115 ALA   H CB  1 
ATOM   13942 N  N   . HIS   H  8  115 ? 50.045  -132.650 49.347  1.00 82.10  ? 116 HIS   H N   1 
ATOM   13943 C  CA  . HIS   H  8  115 ? 48.614  -132.388 49.670  1.00 80.69  ? 116 HIS   H CA  1 
ATOM   13944 C  C   . HIS   H  8  115 ? 48.489  -131.230 50.671  1.00 80.78  ? 116 HIS   H C   1 
ATOM   13945 O  O   . HIS   H  8  115 ? 47.403  -130.620 50.713  1.00 81.66  ? 116 HIS   H O   1 
ATOM   13946 C  CB  . HIS   H  8  115 ? 47.910  -133.677 50.121  1.00 80.09  ? 116 HIS   H CB  1 
ATOM   13947 C  CG  . HIS   H  8  115 ? 47.447  -134.499 48.966  1.00 77.23  ? 116 HIS   H CG  1 
ATOM   13948 N  ND1 . HIS   H  8  115 ? 46.461  -134.062 48.104  1.00 75.66  ? 116 HIS   H ND1 1 
ATOM   13949 C  CD2 . HIS   H  8  115 ? 47.838  -135.708 48.512  1.00 80.28  ? 116 HIS   H CD2 1 
ATOM   13950 C  CE1 . HIS   H  8  115 ? 46.260  -134.969 47.173  1.00 75.59  ? 116 HIS   H CE1 1 
ATOM   13951 N  NE2 . HIS   H  8  115 ? 47.090  -135.987 47.402  1.00 77.23  ? 116 HIS   H NE2 1 
ATOM   13952 N  N   . GLY   H  8  116 ? 49.547  -130.938 51.438  1.00 81.73  ? 117 GLY   H N   1 
ATOM   13953 C  CA  . GLY   H  8  116 ? 49.639  -129.729 52.280  1.00 80.79  ? 117 GLY   H CA  1 
ATOM   13954 C  C   . GLY   H  8  116 ? 49.798  -130.019 53.764  1.00 83.70  ? 117 GLY   H C   1 
ATOM   13955 O  O   . GLY   H  8  116 ? 49.815  -129.038 54.533  1.00 82.79  ? 117 GLY   H O   1 
ATOM   13956 N  N   . SER   H  8  117 ? 49.906  -131.291 54.173  1.00 82.51  ? 118 SER   H N   1 
ATOM   13957 C  CA  . SER   H  8  117 ? 50.168  -131.690 55.583  1.00 82.11  ? 118 SER   H CA  1 
ATOM   13958 C  C   . SER   H  8  117 ? 51.626  -131.361 55.936  1.00 81.01  ? 118 SER   H C   1 
ATOM   13959 O  O   . SER   H  8  117 ? 52.474  -131.396 55.021  1.00 79.46  ? 118 SER   H O   1 
ATOM   13960 C  CB  . SER   H  8  117 ? 49.844  -133.146 55.817  1.00 82.71  ? 118 SER   H CB  1 
ATOM   13961 O  OG  . SER   H  8  117 ? 50.579  -133.984 54.936  1.00 84.68  ? 118 SER   H OG  1 
ATOM   13962 N  N   . THR   H  8  118 ? 51.894  -131.023 57.202  1.00 81.92  ? 119 THR   H N   1 
ATOM   13963 C  CA  . THR   H  8  118 ? 53.247  -130.711 57.740  1.00 88.43  ? 119 THR   H CA  1 
ATOM   13964 C  C   . THR   H  8  118 ? 53.544  -131.544 58.994  1.00 86.93  ? 119 THR   H C   1 
ATOM   13965 O  O   . THR   H  8  118 ? 52.593  -131.882 59.728  1.00 84.07  ? 119 THR   H O   1 
ATOM   13966 C  CB  . THR   H  8  118 ? 53.384  -129.217 58.050  1.00 89.16  ? 119 THR   H CB  1 
ATOM   13967 O  OG1 . THR   H  8  118 ? 52.416  -128.865 59.041  1.00 90.60  ? 119 THR   H OG1 1 
ATOM   13968 C  CG2 . THR   H  8  118 ? 53.194  -128.360 56.820  1.00 91.85  ? 119 THR   H CG2 1 
ATOM   13969 N  N   . ASP   H  8  119 ? 54.828  -131.834 59.225  1.00 91.70  ? 120 ASP   H N   1 
ATOM   13970 C  CA  . ASP   H  8  119 ? 55.345  -132.604 60.388  1.00 97.58  ? 120 ASP   H CA  1 
ATOM   13971 C  C   . ASP   H  8  119 ? 56.407  -131.776 61.114  1.00 96.00  ? 120 ASP   H C   1 
ATOM   13972 O  O   . ASP   H  8  119 ? 57.044  -130.929 60.461  1.00 97.14  ? 120 ASP   H O   1 
ATOM   13973 C  CB  . ASP   H  8  119 ? 55.977  -133.930 59.957  1.00 106.12 ? 120 ASP   H CB  1 
ATOM   13974 C  CG  . ASP   H  8  119 ? 55.028  -134.913 59.288  1.00 113.43 ? 120 ASP   H CG  1 
ATOM   13975 O  OD1 . ASP   H  8  119 ? 53.799  -134.699 59.367  1.00 122.95 ? 120 ASP   H OD1 1 
ATOM   13976 O  OD2 . ASP   H  8  119 ? 55.527  -135.896 58.697  1.00 122.15 ? 120 ASP   H OD2 1 
ATOM   13977 N  N   . VAL   H  8  120 ? 56.590  -132.037 62.411  1.00 96.41  ? 121 VAL   H N   1 
ATOM   13978 C  CA  . VAL   H  8  120 ? 57.717  -131.522 63.246  1.00 98.25  ? 121 VAL   H CA  1 
ATOM   13979 C  C   . VAL   H  8  120 ? 58.515  -132.736 63.735  1.00 98.43  ? 121 VAL   H C   1 
ATOM   13980 O  O   . VAL   H  8  120 ? 57.883  -133.766 64.055  1.00 104.51 ? 121 VAL   H O   1 
ATOM   13981 C  CB  . VAL   H  8  120 ? 57.216  -130.672 64.429  1.00 96.91  ? 121 VAL   H CB  1 
ATOM   13982 C  CG1 . VAL   H  8  120 ? 58.358  -129.924 65.100  1.00 97.63  ? 121 VAL   H CG1 1 
ATOM   13983 C  CG2 . VAL   H  8  120 ? 56.120  -129.701 64.016  1.00 96.57  ? 121 VAL   H CG2 1 
ATOM   13984 N  N   . GLY   H  8  121 ? 59.846  -132.628 63.781  1.00 93.53  ? 122 GLY   H N   1 
ATOM   13985 C  CA  . GLY   H  8  121 ? 60.724  -133.720 64.243  1.00 94.06  ? 122 GLY   H CA  1 
ATOM   13986 C  C   . GLY   H  8  121 ? 62.182  -133.306 64.310  1.00 94.39  ? 122 GLY   H C   1 
ATOM   13987 O  O   . GLY   H  8  121 ? 62.534  -132.288 63.684  1.00 96.72  ? 122 GLY   H O   1 
ATOM   13988 N  N   . TYR   H  8  122 ? 62.994  -134.076 65.041  1.00 95.27  ? 123 TYR   H N   1 
ATOM   13989 C  CA  . TYR   H  8  122 ? 64.458  -133.872 65.207  1.00 97.74  ? 123 TYR   H CA  1 
ATOM   13990 C  C   . TYR   H  8  122 ? 65.205  -134.514 64.036  1.00 94.34  ? 123 TYR   H C   1 
ATOM   13991 O  O   . TYR   H  8  122 ? 66.322  -134.070 63.712  1.00 97.87  ? 123 TYR   H O   1 
ATOM   13992 C  CB  . TYR   H  8  122 ? 64.946  -134.457 66.534  1.00 100.12 ? 123 TYR   H CB  1 
ATOM   13993 C  CG  . TYR   H  8  122 ? 64.460  -133.708 67.746  1.00 104.54 ? 123 TYR   H CG  1 
ATOM   13994 C  CD1 . TYR   H  8  122 ? 65.166  -132.625 68.243  1.00 107.39 ? 123 TYR   H CD1 1 
ATOM   13995 C  CD2 . TYR   H  8  122 ? 63.284  -134.068 68.383  1.00 106.38 ? 123 TYR   H CD2 1 
ATOM   13996 C  CE1 . TYR   H  8  122 ? 64.723  -131.924 69.351  1.00 111.93 ? 123 TYR   H CE1 1 
ATOM   13997 C  CE2 . TYR   H  8  122 ? 62.826  -133.377 69.493  1.00 108.80 ? 123 TYR   H CE2 1 
ATOM   13998 C  CZ  . TYR   H  8  122 ? 63.549  -132.303 69.977  1.00 113.57 ? 123 TYR   H CZ  1 
ATOM   13999 O  OH  . TYR   H  8  122 ? 63.111  -131.617 71.069  1.00 121.83 ? 123 TYR   H OH  1 
ATOM   14000 N  N   . TYR   H  8  123 ? 64.611  -135.549 63.441  1.00 90.64  ? 124 TYR   H N   1 
ATOM   14001 C  CA  . TYR   H  8  123 ? 65.135  -136.251 62.243  1.00 91.19  ? 124 TYR   H CA  1 
ATOM   14002 C  C   . TYR   H  8  123 ? 63.958  -136.638 61.344  1.00 86.99  ? 124 TYR   H C   1 
ATOM   14003 O  O   . TYR   H  8  123 ? 62.968  -137.204 61.849  1.00 87.21  ? 124 TYR   H O   1 
ATOM   14004 C  CB  . TYR   H  8  123 ? 65.973  -137.466 62.649  1.00 92.03  ? 124 TYR   H CB  1 
ATOM   14005 C  CG  . TYR   H  8  123 ? 65.218  -138.510 63.431  1.00 91.37  ? 124 TYR   H CG  1 
ATOM   14006 C  CD1 . TYR   H  8  123 ? 64.967  -138.344 64.783  1.00 93.10  ? 124 TYR   H CD1 1 
ATOM   14007 C  CD2 . TYR   H  8  123 ? 64.741  -139.656 62.819  1.00 90.69  ? 124 TYR   H CD2 1 
ATOM   14008 C  CE1 . TYR   H  8  123 ? 64.266  -139.291 65.511  1.00 92.94  ? 124 TYR   H CE1 1 
ATOM   14009 C  CE2 . TYR   H  8  123 ? 64.039  -140.614 63.532  1.00 92.09  ? 124 TYR   H CE2 1 
ATOM   14010 C  CZ  . TYR   H  8  123 ? 63.801  -140.431 64.883  1.00 92.62  ? 124 TYR   H CZ  1 
ATOM   14011 O  OH  . TYR   H  8  123 ? 63.113  -141.367 65.595  1.00 94.07  ? 124 TYR   H OH  1 
ATOM   14012 N  N   . LEU   H  8  124 ? 64.062  -136.309 60.056  1.00 84.80  ? 125 LEU   H N   1 
ATOM   14013 C  CA  . LEU   H  8  124 ? 63.038  -136.604 59.021  1.00 86.37  ? 125 LEU   H CA  1 
ATOM   14014 C  C   . LEU   H  8  124 ? 63.753  -137.096 57.763  1.00 83.96  ? 125 LEU   H C   1 
ATOM   14015 O  O   . LEU   H  8  124 ? 64.939  -136.755 57.591  1.00 85.59  ? 125 LEU   H O   1 
ATOM   14016 C  CB  . LEU   H  8  124 ? 62.234  -135.336 58.717  1.00 87.65  ? 125 LEU   H CB  1 
ATOM   14017 C  CG  . LEU   H  8  124 ? 61.530  -134.685 59.906  1.00 92.71  ? 125 LEU   H CG  1 
ATOM   14018 C  CD1 . LEU   H  8  124 ? 61.098  -133.267 59.558  1.00 93.84  ? 125 LEU   H CD1 1 
ATOM   14019 C  CD2 . LEU   H  8  124 ? 60.341  -135.518 60.365  1.00 93.01  ? 125 LEU   H CD2 1 
ATOM   14020 N  N   . SER   H  8  125 ? 63.062  -137.885 56.940  1.00 83.84  ? 126 SER   H N   1 
ATOM   14021 C  CA  . SER   H  8  125 ? 63.495  -138.240 55.565  1.00 84.44  ? 126 SER   H CA  1 
ATOM   14022 C  C   . SER   H  8  125 ? 62.274  -138.370 54.653  1.00 85.87  ? 126 SER   H C   1 
ATOM   14023 O  O   . SER   H  8  125 ? 61.235  -138.871 55.120  1.00 93.37  ? 126 SER   H O   1 
ATOM   14024 C  CB  . SER   H  8  125 ? 64.317  -139.499 55.546  1.00 84.46  ? 126 SER   H CB  1 
ATOM   14025 O  OG  . SER   H  8  125 ? 63.508  -140.623 55.841  1.00 84.16  ? 126 SER   H OG  1 
ATOM   14026 N  N   . LEU   H  8  126 ? 62.422  -137.931 53.403  1.00 85.12  ? 127 LEU   H N   1 
ATOM   14027 C  CA  . LEU   H  8  126 ? 61.379  -137.961 52.345  1.00 85.48  ? 127 LEU   H CA  1 
ATOM   14028 C  C   . LEU   H  8  126 ? 61.996  -138.549 51.074  1.00 83.02  ? 127 LEU   H C   1 
ATOM   14029 O  O   . LEU   H  8  126 ? 63.239  -138.629 51.002  1.00 81.74  ? 127 LEU   H O   1 
ATOM   14030 C  CB  . LEU   H  8  126 ? 60.875  -136.532 52.106  1.00 86.21  ? 127 LEU   H CB  1 
ATOM   14031 C  CG  . LEU   H  8  126 ? 59.516  -136.161 52.705  1.00 87.98  ? 127 LEU   H CG  1 
ATOM   14032 C  CD1 . LEU   H  8  126 ? 59.287  -136.784 54.077  1.00 86.61  ? 127 LEU   H CD1 1 
ATOM   14033 C  CD2 . LEU   H  8  126 ? 59.384  -134.647 52.790  1.00 90.59  ? 127 LEU   H CD2 1 
ATOM   14034 N  N   . GLY   H  8  127 ? 61.149  -138.952 50.124  1.00 83.40  ? 128 GLY   H N   1 
ATOM   14035 C  CA  . GLY   H  8  127 ? 61.562  -139.469 48.805  1.00 86.94  ? 128 GLY   H CA  1 
ATOM   14036 C  C   . GLY   H  8  127 ? 61.493  -140.984 48.743  1.00 86.78  ? 128 GLY   H C   1 
ATOM   14037 O  O   . GLY   H  8  127 ? 61.176  -141.610 49.775  1.00 86.76  ? 128 GLY   H O   1 
ATOM   14038 N  N   . SER   H  8  128 ? 61.787  -141.554 47.572  1.00 89.49  ? 129 SER   H N   1 
ATOM   14039 C  CA  . SER   H  8  128 ? 61.703  -143.011 47.293  1.00 89.88  ? 129 SER   H CA  1 
ATOM   14040 C  C   . SER   H  8  128 ? 62.747  -143.776 48.117  1.00 89.37  ? 129 SER   H C   1 
ATOM   14041 O  O   . SER   H  8  128 ? 62.542  -144.981 48.338  1.00 91.74  ? 129 SER   H O   1 
ATOM   14042 C  CB  . SER   H  8  128 ? 61.844  -143.293 45.817  1.00 90.81  ? 129 SER   H CB  1 
ATOM   14043 O  OG  . SER   H  8  128 ? 63.074  -142.791 45.317  1.00 94.20  ? 129 SER   H OG  1 
ATOM   14044 N  N   . GLY   H  8  129 ? 63.819  -143.110 48.558  1.00 88.87  ? 130 GLY   H N   1 
ATOM   14045 C  CA  . GLY   H  8  129 ? 64.883  -143.719 49.381  1.00 89.45  ? 130 GLY   H CA  1 
ATOM   14046 C  C   . GLY   H  8  129 ? 64.740  -143.395 50.860  1.00 87.94  ? 130 GLY   H C   1 
ATOM   14047 O  O   . GLY   H  8  129 ? 65.704  -143.657 51.607  1.00 85.48  ? 130 GLY   H O   1 
ATOM   14048 N  N   . SER   H  8  130 ? 63.584  -142.861 51.277  1.00 88.50  ? 131 SER   H N   1 
ATOM   14049 C  CA  . SER   H  8  130 ? 63.319  -142.399 52.666  1.00 88.23  ? 131 SER   H CA  1 
ATOM   14050 C  C   . SER   H  8  130 ? 63.339  -143.588 53.634  1.00 87.63  ? 131 SER   H C   1 
ATOM   14051 O  O   . SER   H  8  130 ? 63.736  -143.394 54.795  1.00 85.36  ? 131 SER   H O   1 
ATOM   14052 C  CB  . SER   H  8  130 ? 62.019  -141.627 52.764  1.00 88.03  ? 131 SER   H CB  1 
ATOM   14053 O  OG  . SER   H  8  130 ? 60.897  -142.486 52.630  1.00 89.95  ? 131 SER   H OG  1 
ATOM   14054 N  N   . LEU   H  8  131 ? 62.933  -144.775 53.179  1.00 85.31  ? 132 LEU   H N   1 
ATOM   14055 C  CA  . LEU   H  8  131 ? 62.861  -145.985 54.042  1.00 88.11  ? 132 LEU   H CA  1 
ATOM   14056 C  C   . LEU   H  8  131 ? 64.273  -146.505 54.340  1.00 86.43  ? 132 LEU   H C   1 
ATOM   14057 O  O   . LEU   H  8  131 ? 64.505  -146.922 55.488  1.00 88.60  ? 132 LEU   H O   1 
ATOM   14058 C  CB  . LEU   H  8  131 ? 61.988  -147.052 53.379  1.00 88.19  ? 132 LEU   H CB  1 
ATOM   14059 C  CG  . LEU   H  8  131 ? 60.502  -146.962 53.717  1.00 90.60  ? 132 LEU   H CG  1 
ATOM   14060 C  CD1 . LEU   H  8  131 ? 59.828  -145.851 52.926  1.00 91.48  ? 132 LEU   H CD1 1 
ATOM   14061 C  CD2 . LEU   H  8  131 ? 59.807  -148.290 53.469  1.00 90.59  ? 132 LEU   H CD2 1 
ATOM   14062 N  N   . ALA   H  8  132 ? 65.182  -146.478 53.363  1.00 85.28  ? 133 ALA   H N   1 
ATOM   14063 C  CA  . ALA   H  8  132 ? 66.609  -146.828 53.558  1.00 87.02  ? 133 ALA   H CA  1 
ATOM   14064 C  C   . ALA   H  8  132 ? 67.252  -145.817 54.515  1.00 89.63  ? 133 ALA   H C   1 
ATOM   14065 O  O   . ALA   H  8  132 ? 67.999  -146.251 55.416  1.00 90.48  ? 133 ALA   H O   1 
ATOM   14066 C  CB  . ALA   H  8  132 ? 67.332  -146.870 52.236  1.00 86.25  ? 133 ALA   H CB  1 
ATOM   14067 N  N   . ALA   H  8  133 ? 66.960  -144.523 54.323  1.00 90.53  ? 134 ALA   H N   1 
ATOM   14068 C  CA  . ALA   H  8  133 ? 67.467  -143.397 55.144  1.00 90.19  ? 134 ALA   H CA  1 
ATOM   14069 C  C   . ALA   H  8  133 ? 66.916  -143.512 56.571  1.00 90.17  ? 134 ALA   H C   1 
ATOM   14070 O  O   . ALA   H  8  133 ? 67.729  -143.531 57.515  1.00 92.17  ? 134 ALA   H O   1 
ATOM   14071 C  CB  . ALA   H  8  133 ? 67.095  -142.077 54.511  1.00 89.51  ? 134 ALA   H CB  1 
ATOM   14072 N  N   . MET   H  8  134 ? 65.589  -143.602 56.714  1.00 87.35  ? 135 MET   H N   1 
ATOM   14073 C  CA  . MET   H  8  134 ? 64.886  -143.603 58.026  1.00 88.71  ? 135 MET   H CA  1 
ATOM   14074 C  C   . MET   H  8  134 ? 65.381  -144.782 58.869  1.00 88.66  ? 135 MET   H C   1 
ATOM   14075 O  O   . MET   H  8  134 ? 65.483  -144.621 60.098  1.00 92.77  ? 135 MET   H O   1 
ATOM   14076 C  CB  . MET   H  8  134 ? 63.366  -143.696 57.853  1.00 85.32  ? 135 MET   H CB  1 
ATOM   14077 C  CG  . MET   H  8  134 ? 62.597  -143.670 59.165  1.00 87.39  ? 135 MET   H CG  1 
ATOM   14078 S  SD  . MET   H  8  134 ? 63.014  -142.248 60.215  1.00 90.47  ? 135 MET   H SD  1 
ATOM   14079 C  CE  . MET   H  8  134 ? 62.389  -140.893 59.221  1.00 89.43  ? 135 MET   H CE  1 
ATOM   14080 N  N   . ALA   H  8  135 ? 65.677  -145.917 58.232  1.00 90.67  ? 136 ALA   H N   1 
ATOM   14081 C  CA  . ALA   H  8  135 ? 66.225  -147.125 58.890  1.00 93.80  ? 136 ALA   H CA  1 
ATOM   14082 C  C   . ALA   H  8  135 ? 67.534  -146.763 59.601  1.00 93.05  ? 136 ALA   H C   1 
ATOM   14083 O  O   . ALA   H  8  135 ? 67.697  -147.157 60.771  1.00 97.14  ? 136 ALA   H O   1 
ATOM   14084 C  CB  . ALA   H  8  135 ? 66.425  -148.229 57.880  1.00 95.24  ? 136 ALA   H CB  1 
ATOM   14085 N  N   . VAL   H  8  136 ? 68.415  -146.019 58.923  1.00 93.01  ? 137 VAL   H N   1 
ATOM   14086 C  CA  . VAL   H  8  136 ? 69.732  -145.569 59.468  1.00 92.69  ? 137 VAL   H CA  1 
ATOM   14087 C  C   . VAL   H  8  136 ? 69.488  -144.553 60.589  1.00 90.95  ? 137 VAL   H C   1 
ATOM   14088 O  O   . VAL   H  8  136 ? 70.130  -144.690 61.645  1.00 91.30  ? 137 VAL   H O   1 
ATOM   14089 C  CB  . VAL   H  8  136 ? 70.641  -144.988 58.367  1.00 91.71  ? 137 VAL   H CB  1 
ATOM   14090 C  CG1 . VAL   H  8  136 ? 71.803  -144.193 58.943  1.00 92.77  ? 137 VAL   H CG1 1 
ATOM   14091 C  CG2 . VAL   H  8  136 ? 71.152  -146.075 57.439  1.00 92.26  ? 137 VAL   H CG2 1 
ATOM   14092 N  N   . LEU   H  8  137 ? 68.608  -143.570 60.359  1.00 93.69  ? 138 LEU   H N   1 
ATOM   14093 C  CA  . LEU   H  8  137 ? 68.272  -142.507 61.348  1.00 93.62  ? 138 LEU   H CA  1 
ATOM   14094 C  C   . LEU   H  8  137 ? 67.728  -143.168 62.621  1.00 94.18  ? 138 LEU   H C   1 
ATOM   14095 O  O   . LEU   H  8  137 ? 68.223  -142.830 63.711  1.00 93.62  ? 138 LEU   H O   1 
ATOM   14096 C  CB  . LEU   H  8  137 ? 67.253  -141.523 60.755  1.00 93.34  ? 138 LEU   H CB  1 
ATOM   14097 C  CG  . LEU   H  8  137 ? 67.747  -140.639 59.608  1.00 90.97  ? 138 LEU   H CG  1 
ATOM   14098 C  CD1 . LEU   H  8  137 ? 66.597  -139.834 59.020  1.00 91.66  ? 138 LEU   H CD1 1 
ATOM   14099 C  CD2 . LEU   H  8  137 ? 68.865  -139.710 60.061  1.00 89.02  ? 138 LEU   H CD2 1 
ATOM   14100 N  N   . GLU   H  8  138 ? 66.774  -144.094 62.481  1.00 94.48  ? 139 GLU   H N   1 
ATOM   14101 C  CA  . GLU   H  8  138 ? 66.120  -144.792 63.622  1.00 95.87  ? 139 GLU   H CA  1 
ATOM   14102 C  C   . GLU   H  8  138 ? 67.150  -145.646 64.368  1.00 96.72  ? 139 GLU   H C   1 
ATOM   14103 O  O   . GLU   H  8  138 ? 66.934  -145.898 65.568  1.00 100.36 ? 139 GLU   H O   1 
ATOM   14104 C  CB  . GLU   H  8  138 ? 64.947  -145.650 63.144  1.00 97.93  ? 139 GLU   H CB  1 
ATOM   14105 C  CG  . GLU   H  8  138 ? 63.718  -144.838 62.783  1.00 99.64  ? 139 GLU   H CG  1 
ATOM   14106 C  CD  . GLU   H  8  138 ? 62.890  -144.386 63.974  1.00 100.78 ? 139 GLU   H CD  1 
ATOM   14107 O  OE1 . GLU   H  8  138 ? 61.649  -144.405 63.864  1.00 105.44 ? 139 GLU   H OE1 1 
ATOM   14108 O  OE2 . GLU   H  8  138 ? 63.482  -144.011 65.006  1.00 101.53 ? 139 GLU   H OE2 1 
ATOM   14109 N  N   . SER   H  8  139 ? 68.223  -146.062 63.686  1.00 97.21  ? 140 SER   H N   1 
ATOM   14110 C  CA  . SER   H  8  139 ? 69.301  -146.927 64.237  1.00 98.73  ? 140 SER   H CA  1 
ATOM   14111 C  C   . SER   H  8  139 ? 70.344  -146.104 65.005  1.00 99.52  ? 140 SER   H C   1 
ATOM   14112 O  O   . SER   H  8  139 ? 70.813  -146.606 66.041  1.00 99.58  ? 140 SER   H O   1 
ATOM   14113 C  CB  . SER   H  8  139 ? 69.960  -147.738 63.151  1.00 98.61  ? 140 SER   H CB  1 
ATOM   14114 O  OG  . SER   H  8  139 ? 69.059  -148.691 62.614  1.00 99.69  ? 140 SER   H OG  1 
ATOM   14115 N  N   . HIS   H  8  140 ? 70.709  -144.910 64.517  1.00 100.73 ? 141 HIS   H N   1 
ATOM   14116 C  CA  . HIS   H  8  140 ? 71.899  -144.143 64.986  1.00 101.99 ? 141 HIS   H CA  1 
ATOM   14117 C  C   . HIS   H  8  140 ? 71.553  -142.746 65.528  1.00 100.03 ? 141 HIS   H C   1 
ATOM   14118 O  O   . HIS   H  8  140 ? 72.488  -142.095 66.036  1.00 100.93 ? 141 HIS   H O   1 
ATOM   14119 C  CB  . HIS   H  8  140 ? 72.943  -144.028 63.866  1.00 102.45 ? 141 HIS   H CB  1 
ATOM   14120 C  CG  . HIS   H  8  140 ? 73.472  -145.339 63.395  1.00 105.04 ? 141 HIS   H CG  1 
ATOM   14121 N  ND1 . HIS   H  8  140 ? 73.761  -146.374 64.261  1.00 106.60 ? 141 HIS   H ND1 1 
ATOM   14122 C  CD2 . HIS   H  8  140 ? 73.782  -145.780 62.157  1.00 106.51 ? 141 HIS   H CD2 1 
ATOM   14123 C  CE1 . HIS   H  8  140 ? 74.215  -147.403 63.575  1.00 108.85 ? 141 HIS   H CE1 1 
ATOM   14124 N  NE2 . HIS   H  8  140 ? 74.239  -147.063 62.280  1.00 108.75 ? 141 HIS   H NE2 1 
ATOM   14125 N  N   . TRP   H  8  141 ? 70.303  -142.275 65.439  1.00 99.45  ? 142 TRP   H N   1 
ATOM   14126 C  CA  . TRP   H  8  141 ? 69.921  -140.949 65.998  1.00 100.80 ? 142 TRP   H CA  1 
ATOM   14127 C  C   . TRP   H  8  141 ? 69.929  -141.019 67.527  1.00 101.99 ? 142 TRP   H C   1 
ATOM   14128 O  O   . TRP   H  8  141 ? 69.585  -142.080 68.073  1.00 103.75 ? 142 TRP   H O   1 
ATOM   14129 C  CB  . TRP   H  8  141 ? 68.561  -140.451 65.494  1.00 101.20 ? 142 TRP   H CB  1 
ATOM   14130 C  CG  . TRP   H  8  141 ? 68.206  -139.102 66.046  1.00 101.79 ? 142 TRP   H CG  1 
ATOM   14131 C  CD1 . TRP   H  8  141 ? 68.534  -137.886 65.518  1.00 101.76 ? 142 TRP   H CD1 1 
ATOM   14132 C  CD2 . TRP   H  8  141 ? 67.493  -138.826 67.266  1.00 103.50 ? 142 TRP   H CD2 1 
ATOM   14133 N  NE1 . TRP   H  8  141 ? 68.061  -136.876 66.312  1.00 101.15 ? 142 TRP   H NE1 1 
ATOM   14134 C  CE2 . TRP   H  8  141 ? 67.419  -137.421 67.392  1.00 101.36 ? 142 TRP   H CE2 1 
ATOM   14135 C  CE3 . TRP   H  8  141 ? 66.907  -139.624 68.257  1.00 104.11 ? 142 TRP   H CE3 1 
ATOM   14136 C  CZ2 . TRP   H  8  141 ? 66.777  -136.803 68.464  1.00 102.45 ? 142 TRP   H CZ2 1 
ATOM   14137 C  CZ3 . TRP   H  8  141 ? 66.275  -139.012 69.318  1.00 104.99 ? 142 TRP   H CZ3 1 
ATOM   14138 C  CH2 . TRP   H  8  141 ? 66.213  -137.621 69.418  1.00 104.92 ? 142 TRP   H CH2 1 
ATOM   14139 N  N   . LYS   H  8  142 ? 70.297  -139.912 68.177  1.00 107.16 ? 143 LYS   H N   1 
ATOM   14140 C  CA  . LYS   H  8  142 ? 70.165  -139.712 69.645  1.00 108.95 ? 143 LYS   H CA  1 
ATOM   14141 C  C   . LYS   H  8  142 ? 69.953  -138.223 69.933  1.00 112.74 ? 143 LYS   H C   1 
ATOM   14142 O  O   . LYS   H  8  142 ? 70.263  -137.397 69.052  1.00 107.95 ? 143 LYS   H O   1 
ATOM   14143 C  CB  . LYS   H  8  142 ? 71.393  -140.253 70.386  1.00 108.77 ? 143 LYS   H CB  1 
ATOM   14144 C  CG  . LYS   H  8  142 ? 72.744  -139.716 69.928  1.00 110.35 ? 143 LYS   H CG  1 
ATOM   14145 C  CD  . LYS   H  8  142 ? 73.880  -140.149 70.837  1.00 112.28 ? 143 LYS   H CD  1 
ATOM   14146 C  CE  . LYS   H  8  142 ? 75.243  -140.122 70.177  1.00 115.55 ? 143 LYS   H CE  1 
ATOM   14147 N  NZ  . LYS   H  8  142 ? 75.751  -138.740 70.011  1.00 116.85 ? 143 LYS   H NZ  1 
ATOM   14148 N  N   . GLN   H  8  143 ? 69.425  -137.910 71.118  1.00 117.47 ? 144 GLN   H N   1 
ATOM   14149 C  CA  . GLN   H  8  143 ? 69.273  -136.522 71.632  1.00 123.22 ? 144 GLN   H CA  1 
ATOM   14150 C  C   . GLN   H  8  143 ? 70.673  -135.948 71.898  1.00 124.68 ? 144 GLN   H C   1 
ATOM   14151 O  O   . GLN   H  8  143 ? 71.573  -136.732 72.267  1.00 130.08 ? 144 GLN   H O   1 
ATOM   14152 C  CB  . GLN   H  8  143 ? 68.395  -136.528 72.887  1.00 129.93 ? 144 GLN   H CB  1 
ATOM   14153 C  CG  . GLN   H  8  143 ? 67.949  -135.146 73.351  1.00 133.24 ? 144 GLN   H CG  1 
ATOM   14154 C  CD  . GLN   H  8  143 ? 66.818  -134.578 72.527  1.00 134.21 ? 144 GLN   H CD  1 
ATOM   14155 O  OE1 . GLN   H  8  143 ? 65.645  -134.725 72.865  1.00 139.18 ? 144 GLN   H OE1 1 
ATOM   14156 N  NE2 . GLN   H  8  143 ? 67.159  -133.915 71.432  1.00 132.29 ? 144 GLN   H NE2 1 
ATOM   14157 N  N   . ASP   H  8  144 ? 70.847  -134.637 71.694  1.00 124.01 ? 145 ASP   H N   1 
ATOM   14158 C  CA  . ASP   H  8  144 ? 72.102  -133.882 71.964  1.00 121.76 ? 145 ASP   H CA  1 
ATOM   14159 C  C   . ASP   H  8  144 ? 73.206  -134.364 71.015  1.00 113.72 ? 145 ASP   H C   1 
ATOM   14160 O  O   . ASP   H  8  144 ? 74.273  -134.777 71.505  1.00 113.14 ? 145 ASP   H O   1 
ATOM   14161 C  CB  . ASP   H  8  144 ? 72.527  -134.001 73.431  1.00 130.95 ? 145 ASP   H CB  1 
ATOM   14162 C  CG  . ASP   H  8  144 ? 71.544  -133.373 74.403  1.00 134.45 ? 145 ASP   H CG  1 
ATOM   14163 O  OD1 . ASP   H  8  144 ? 71.199  -132.190 74.207  1.00 130.35 ? 145 ASP   H OD1 1 
ATOM   14164 O  OD2 . ASP   H  8  144 ? 71.126  -134.074 75.346  1.00 151.63 ? 145 ASP   H OD2 1 
ATOM   14165 N  N   . LEU   H  8  145 ? 72.950  -134.308 69.706  1.00 108.56 ? 146 LEU   H N   1 
ATOM   14166 C  CA  . LEU   H  8  145 ? 73.979  -134.499 68.649  1.00 109.01 ? 146 LEU   H CA  1 
ATOM   14167 C  C   . LEU   H  8  145 ? 74.827  -133.225 68.552  1.00 106.06 ? 146 LEU   H C   1 
ATOM   14168 O  O   . LEU   H  8  145 ? 74.262  -132.133 68.740  1.00 108.29 ? 146 LEU   H O   1 
ATOM   14169 C  CB  . LEU   H  8  145 ? 73.294  -134.785 67.308  1.00 109.39 ? 146 LEU   H CB  1 
ATOM   14170 C  CG  . LEU   H  8  145 ? 72.755  -136.202 67.122  1.00 108.71 ? 146 LEU   H CG  1 
ATOM   14171 C  CD1 . LEU   H  8  145 ? 71.630  -136.226 66.099  1.00 109.49 ? 146 LEU   H CD1 1 
ATOM   14172 C  CD2 . LEU   H  8  145 ? 73.869  -137.151 66.714  1.00 109.35 ? 146 LEU   H CD2 1 
ATOM   14173 N  N   . THR   H  8  146 ? 76.122  -133.362 68.253  1.00 102.47 ? 147 THR   H N   1 
ATOM   14174 C  CA  . THR   H  8  146 ? 77.015  -132.236 67.872  1.00 102.93 ? 147 THR   H CA  1 
ATOM   14175 C  C   . THR   H  8  146 ? 76.876  -131.981 66.368  1.00 103.95 ? 147 THR   H C   1 
ATOM   14176 O  O   . THR   H  8  146 ? 76.281  -132.833 65.676  1.00 96.86  ? 147 THR   H O   1 
ATOM   14177 C  CB  . THR   H  8  146 ? 78.480  -132.509 68.236  1.00 102.16 ? 147 THR   H CB  1 
ATOM   14178 O  OG1 . THR   H  8  146 ? 78.960  -133.588 67.435  1.00 102.87 ? 147 THR   H OG1 1 
ATOM   14179 C  CG2 . THR   H  8  146 ? 78.670  -132.834 69.699  1.00 104.42 ? 147 THR   H CG2 1 
ATOM   14180 N  N   . LYS   H  8  147 ? 77.411  -130.852 65.895  1.00 108.24 ? 148 LYS   H N   1 
ATOM   14181 C  CA  . LYS   H  8  147 ? 77.421  -130.453 64.462  1.00 110.58 ? 148 LYS   H CA  1 
ATOM   14182 C  C   . LYS   H  8  147 ? 78.028  -131.593 63.630  1.00 112.55 ? 148 LYS   H C   1 
ATOM   14183 O  O   . LYS   H  8  147 ? 77.358  -132.046 62.682  1.00 115.20 ? 148 LYS   H O   1 
ATOM   14184 C  CB  . LYS   H  8  147 ? 78.185  -129.134 64.291  1.00 109.09 ? 148 LYS   H CB  1 
ATOM   14185 C  CG  . LYS   H  8  147 ? 78.224  -128.574 62.876  1.00 109.48 ? 148 LYS   H CG  1 
ATOM   14186 C  CD  . LYS   H  8  147 ? 79.250  -127.477 62.694  1.00 113.20 ? 148 LYS   H CD  1 
ATOM   14187 C  CE  . LYS   H  8  147 ? 79.536  -127.183 61.238  1.00 115.47 ? 148 LYS   H CE  1 
ATOM   14188 N  NZ  . LYS   H  8  147 ? 80.567  -126.131 61.083  1.00 119.13 ? 148 LYS   H NZ  1 
ATOM   14189 N  N   . GLU   H  8  148 ? 79.229  -132.063 63.991  1.00 112.50 ? 149 GLU   H N   1 
ATOM   14190 C  CA  . GLU   H  8  148 ? 80.020  -133.043 63.193  1.00 110.29 ? 149 GLU   H CA  1 
ATOM   14191 C  C   . GLU   H  8  148 ? 79.394  -134.441 63.286  1.00 106.31 ? 149 GLU   H C   1 
ATOM   14192 O  O   . GLU   H  8  148 ? 79.622  -135.239 62.357  1.00 101.79 ? 149 GLU   H O   1 
ATOM   14193 C  CB  . GLU   H  8  148 ? 81.482  -133.081 63.643  1.00 116.31 ? 149 GLU   H CB  1 
ATOM   14194 C  CG  . GLU   H  8  148 ? 82.309  -131.913 63.129  1.00 122.77 ? 149 GLU   H CG  1 
ATOM   14195 C  CD  . GLU   H  8  148 ? 82.108  -130.592 63.857  1.00 127.92 ? 149 GLU   H CD  1 
ATOM   14196 O  OE1 . GLU   H  8  148 ? 82.462  -129.544 63.279  1.00 135.46 ? 149 GLU   H OE1 1 
ATOM   14197 O  OE2 . GLU   H  8  148 ? 81.605  -130.611 65.001  1.00 127.57 ? 149 GLU   H OE2 1 
ATOM   14198 N  N   . GLU   H  8  149 ? 78.658  -134.731 64.363  1.00 104.74 ? 150 GLU   H N   1 
ATOM   14199 C  CA  . GLU   H  8  149 ? 77.886  -135.993 64.529  1.00 103.23 ? 150 GLU   H CA  1 
ATOM   14200 C  C   . GLU   H  8  149 ? 76.656  -135.957 63.615  1.00 103.18 ? 150 GLU   H C   1 
ATOM   14201 O  O   . GLU   H  8  149 ? 76.393  -136.967 62.936  1.00 101.17 ? 150 GLU   H O   1 
ATOM   14202 C  CB  . GLU   H  8  149 ? 77.450  -136.190 65.981  1.00 104.06 ? 150 GLU   H CB  1 
ATOM   14203 C  CG  . GLU   H  8  149 ? 78.555  -136.701 66.886  1.00 108.20 ? 150 GLU   H CG  1 
ATOM   14204 C  CD  . GLU   H  8  149 ? 78.165  -136.824 68.350  1.00 113.69 ? 150 GLU   H CD  1 
ATOM   14205 O  OE1 . GLU   H  8  149 ? 77.452  -135.930 68.853  1.00 113.83 ? 150 GLU   H OE1 1 
ATOM   14206 O  OE2 . GLU   H  8  149 ? 78.568  -137.821 68.985  1.00 116.02 ? 150 GLU   H OE2 1 
ATOM   14207 N  N   . ALA   H  8  150 ? 75.934  -134.833 63.608  1.00 102.31 ? 151 ALA   H N   1 
ATOM   14208 C  CA  . ALA   H  8  150 ? 74.679  -134.634 62.846  1.00 101.71 ? 151 ALA   H CA  1 
ATOM   14209 C  C   . ALA   H  8  150 ? 74.957  -134.692 61.338  1.00 98.59  ? 151 ALA   H C   1 
ATOM   14210 O  O   . ALA   H  8  150 ? 74.122  -135.271 60.619  1.00 96.48  ? 151 ALA   H O   1 
ATOM   14211 C  CB  . ALA   H  8  150 ? 74.038  -133.327 63.239  1.00 102.17 ? 151 ALA   H CB  1 
ATOM   14212 N  N   . ILE   H  8  151 ? 76.071  -134.108 60.880  1.00 98.85  ? 152 ILE   H N   1 
ATOM   14213 C  CA  . ILE   H  8  151 ? 76.512  -134.155 59.452  1.00 97.44  ? 152 ILE   H CA  1 
ATOM   14214 C  C   . ILE   H  8  151 ? 76.776  -135.619 59.082  1.00 97.75  ? 152 ILE   H C   1 
ATOM   14215 O  O   . ILE   H  8  151 ? 76.327  -136.050 58.000  1.00 95.49  ? 152 ILE   H O   1 
ATOM   14216 C  CB  . ILE   H  8  151 ? 77.758  -133.277 59.198  1.00 98.11  ? 152 ILE   H CB  1 
ATOM   14217 C  CG1 . ILE   H  8  151 ? 77.482  -131.790 59.433  1.00 98.68  ? 152 ILE   H CG1 1 
ATOM   14218 C  CG2 . ILE   H  8  151 ? 78.307  -133.517 57.797  1.00 97.95  ? 152 ILE   H CG2 1 
ATOM   14219 C  CD1 . ILE   H  8  151 ? 78.733  -130.950 59.595  1.00 99.75  ? 152 ILE   H CD1 1 
ATOM   14220 N  N   . LYS   H  8  152 ? 77.486  -136.348 59.948  1.00 96.17  ? 153 LYS   H N   1 
ATOM   14221 C  CA  . LYS   H  8  152 ? 77.856  -137.774 59.733  1.00 96.18  ? 153 LYS   H CA  1 
ATOM   14222 C  C   . LYS   H  8  152 ? 76.575  -138.605 59.600  1.00 93.37  ? 153 LYS   H C   1 
ATOM   14223 O  O   . LYS   H  8  152 ? 76.470  -139.361 58.619  1.00 92.93  ? 153 LYS   H O   1 
ATOM   14224 C  CB  . LYS   H  8  152 ? 78.742  -138.287 60.872  1.00 97.31  ? 153 LYS   H CB  1 
ATOM   14225 C  CG  . LYS   H  8  152 ? 79.895  -139.178 60.434  1.00 100.07 ? 153 LYS   H CG  1 
ATOM   14226 C  CD  . LYS   H  8  152 ? 79.509  -140.620 60.200  1.00 102.84 ? 153 LYS   H CD  1 
ATOM   14227 C  CE  . LYS   H  8  152 ? 80.607  -141.406 59.516  1.00 105.63 ? 153 LYS   H CE  1 
ATOM   14228 N  NZ  . LYS   H  8  152 ? 80.259  -142.840 59.386  1.00 107.32 ? 153 LYS   H NZ  1 
ATOM   14229 N  N   . LEU   H  8  153 ? 75.636  -138.439 60.537  1.00 91.91  ? 154 LEU   H N   1 
ATOM   14230 C  CA  . LEU   H  8  153 ? 74.332  -139.157 60.567  1.00 91.26  ? 154 LEU   H CA  1 
ATOM   14231 C  C   . LEU   H  8  153 ? 73.532  -138.844 59.298  1.00 90.36  ? 154 LEU   H C   1 
ATOM   14232 O  O   . LEU   H  8  153 ? 73.025  -139.794 58.674  1.00 90.06  ? 154 LEU   H O   1 
ATOM   14233 C  CB  . LEU   H  8  153 ? 73.553  -138.736 61.817  1.00 92.50  ? 154 LEU   H CB  1 
ATOM   14234 C  CG  . LEU   H  8  153 ? 72.188  -139.399 62.002  1.00 93.85  ? 154 LEU   H CG  1 
ATOM   14235 C  CD1 . LEU   H  8  153 ? 72.308  -140.914 62.038  1.00 95.20  ? 154 LEU   H CD1 1 
ATOM   14236 C  CD2 . LEU   H  8  153 ? 71.511  -138.894 63.266  1.00 95.67  ? 154 LEU   H CD2 1 
ATOM   14237 N  N   . ALA   H  8  154 ? 73.407  -137.562 58.948  1.00 89.09  ? 155 ALA   H N   1 
ATOM   14238 C  CA  . ALA   H  8  154 ? 72.645  -137.076 57.774  1.00 88.29  ? 155 ALA   H CA  1 
ATOM   14239 C  C   . ALA   H  8  154 ? 73.214  -137.709 56.499  1.00 87.01  ? 155 ALA   H C   1 
ATOM   14240 O  O   . ALA   H  8  154 ? 72.429  -138.305 55.743  1.00 85.90  ? 155 ALA   H O   1 
ATOM   14241 C  CB  . ALA   H  8  154 ? 72.678  -135.568 57.712  1.00 87.90  ? 155 ALA   H CB  1 
ATOM   14242 N  N   . SER   H  8  155 ? 74.529  -137.604 56.280  1.00 86.39  ? 156 SER   H N   1 
ATOM   14243 C  CA  . SER   H  8  155 ? 75.205  -138.065 55.038  1.00 89.76  ? 156 SER   H CA  1 
ATOM   14244 C  C   . SER   H  8  155 ? 75.190  -139.597 54.972  1.00 92.09  ? 156 SER   H C   1 
ATOM   14245 O  O   . SER   H  8  155 ? 75.097  -140.130 53.853  1.00 98.70  ? 156 SER   H O   1 
ATOM   14246 C  CB  . SER   H  8  155 ? 76.602  -137.514 54.923  1.00 88.35  ? 156 SER   H CB  1 
ATOM   14247 O  OG  . SER   H  8  155 ? 77.467  -138.130 55.860  1.00 91.57  ? 156 SER   H OG  1 
ATOM   14248 N  N   . ASP   H  8  156 ? 75.265  -140.272 56.124  1.00 95.89  ? 157 ASP   H N   1 
ATOM   14249 C  CA  . ASP   H  8  156 ? 75.142  -141.751 56.238  1.00 97.61  ? 157 ASP   H CA  1 
ATOM   14250 C  C   . ASP   H  8  156 ? 73.736  -142.176 55.806  1.00 95.26  ? 157 ASP   H C   1 
ATOM   14251 O  O   . ASP   H  8  156 ? 73.628  -143.174 55.071  1.00 97.37  ? 157 ASP   H O   1 
ATOM   14252 C  CB  . ASP   H  8  156 ? 75.437  -142.244 57.659  1.00 101.36 ? 157 ASP   H CB  1 
ATOM   14253 C  CG  . ASP   H  8  156 ? 76.917  -142.376 57.984  1.00 107.30 ? 157 ASP   H CG  1 
ATOM   14254 O  OD1 . ASP   H  8  156 ? 77.745  -141.943 57.154  1.00 112.00 ? 157 ASP   H OD1 1 
ATOM   14255 O  OD2 . ASP   H  8  156 ? 77.231  -142.909 59.070  1.00 109.28 ? 157 ASP   H OD2 1 
ATOM   14256 N  N   . ALA   H  8  157 ? 72.707  -141.451 56.254  1.00 91.67  ? 158 ALA   H N   1 
ATOM   14257 C  CA  . ALA   H  8  157 ? 71.285  -141.697 55.916  1.00 91.46  ? 158 ALA   H CA  1 
ATOM   14258 C  C   . ALA   H  8  157 ? 71.076  -141.531 54.405  1.00 92.45  ? 158 ALA   H C   1 
ATOM   14259 O  O   . ALA   H  8  157 ? 70.326  -142.340 53.818  1.00 86.23  ? 158 ALA   H O   1 
ATOM   14260 C  CB  . ALA   H  8  157 ? 70.392  -140.773 56.707  1.00 91.81  ? 158 ALA   H CB  1 
ATOM   14261 N  N   . ILE   H  8  158 ? 71.716  -140.524 53.799  1.00 93.20  ? 159 ILE   H N   1 
ATOM   14262 C  CA  . ILE   H  8  158 ? 71.657  -140.269 52.328  1.00 94.63  ? 159 ILE   H CA  1 
ATOM   14263 C  C   . ILE   H  8  158 ? 72.345  -141.431 51.601  1.00 95.09  ? 159 ILE   H C   1 
ATOM   14264 O  O   . ILE   H  8  158 ? 71.771  -141.919 50.607  1.00 97.18  ? 159 ILE   H O   1 
ATOM   14265 C  CB  . ILE   H  8  158 ? 72.275  -138.903 51.959  1.00 95.08  ? 159 ILE   H CB  1 
ATOM   14266 C  CG1 . ILE   H  8  158 ? 71.495  -137.737 52.574  1.00 95.87  ? 159 ILE   H CG1 1 
ATOM   14267 C  CG2 . ILE   H  8  158 ? 72.398  -138.752 50.449  1.00 94.75  ? 159 ILE   H CG2 1 
ATOM   14268 C  CD1 . ILE   H  8  158 ? 70.044  -137.658 52.142  1.00 96.27  ? 159 ILE   H CD1 1 
ATOM   14269 N  N   . GLN   H  8  159 ? 73.518  -141.858 52.080  1.00 95.63  ? 160 GLN   H N   1 
ATOM   14270 C  CA  . GLN   H  8  159 ? 74.311  -142.967 51.478  1.00 95.52  ? 160 GLN   H CA  1 
ATOM   14271 C  C   . GLN   H  8  159 ? 73.466  -144.246 51.438  1.00 94.48  ? 160 GLN   H C   1 
ATOM   14272 O  O   . GLN   H  8  159 ? 73.517  -144.943 50.408  1.00 95.49  ? 160 GLN   H O   1 
ATOM   14273 C  CB  . GLN   H  8  159 ? 75.623  -143.189 52.234  1.00 96.16  ? 160 GLN   H CB  1 
ATOM   14274 C  CG  . GLN   H  8  159 ? 76.721  -142.217 51.827  1.00 97.29  ? 160 GLN   H CG  1 
ATOM   14275 C  CD  . GLN   H  8  159 ? 78.093  -142.686 52.243  1.00 97.23  ? 160 GLN   H CD  1 
ATOM   14276 O  OE1 . GLN   H  8  159 ? 78.616  -143.664 51.715  1.00 98.35  ? 160 GLN   H OE1 1 
ATOM   14277 N  NE2 . GLN   H  8  159 ? 78.697  -141.977 53.185  1.00 96.83  ? 160 GLN   H NE2 1 
ATOM   14278 N  N   . ALA   H  8  160 ? 72.712  -144.537 52.503  1.00 94.50  ? 161 ALA   H N   1 
ATOM   14279 C  CA  . ALA   H  8  160 ? 71.783  -145.691 52.583  1.00 94.43  ? 161 ALA   H CA  1 
ATOM   14280 C  C   . ALA   H  8  160 ? 70.896  -145.716 51.335  1.00 93.21  ? 161 ALA   H C   1 
ATOM   14281 O  O   . ALA   H  8  160 ? 70.781  -146.786 50.718  1.00 93.99  ? 161 ALA   H O   1 
ATOM   14282 C  CB  . ALA   H  8  160 ? 70.946  -145.617 53.835  1.00 94.47  ? 161 ALA   H CB  1 
ATOM   14283 N  N   . GLY   H  8  161 ? 70.305  -144.567 50.986  1.00 95.91  ? 162 GLY   H N   1 
ATOM   14284 C  CA  . GLY   H  8  161 ? 69.447  -144.396 49.797  1.00 92.46  ? 162 GLY   H CA  1 
ATOM   14285 C  C   . GLY   H  8  161 ? 70.231  -144.579 48.509  1.00 89.19  ? 162 GLY   H C   1 
ATOM   14286 O  O   . GLY   H  8  161 ? 69.751  -145.320 47.630  1.00 87.06  ? 162 GLY   H O   1 
ATOM   14287 N  N   . ILE   H  8  162 ? 71.398  -143.934 48.404  1.00 89.19  ? 163 ILE   H N   1 
ATOM   14288 C  CA  . ILE   H  8  162 ? 72.269  -143.960 47.189  1.00 89.25  ? 163 ILE   H CA  1 
ATOM   14289 C  C   . ILE   H  8  162 ? 72.518  -145.423 46.795  1.00 90.68  ? 163 ILE   H C   1 
ATOM   14290 O  O   . ILE   H  8  162 ? 72.310  -145.756 45.608  1.00 84.58  ? 163 ILE   H O   1 
ATOM   14291 C  CB  . ILE   H  8  162 ? 73.572  -143.165 47.424  1.00 92.18  ? 163 ILE   H CB  1 
ATOM   14292 C  CG1 . ILE   H  8  162 ? 73.296  -141.658 47.461  1.00 94.91  ? 163 ILE   H CG1 1 
ATOM   14293 C  CG2 . ILE   H  8  162 ? 74.632  -143.512 46.386  1.00 91.83  ? 163 ILE   H CG2 1 
ATOM   14294 C  CD1 . ILE   H  8  162 ? 74.435  -140.817 48.004  1.00 97.42  ? 163 ILE   H CD1 1 
ATOM   14295 N  N   . TRP   H  8  163 ? 72.895  -146.266 47.762  1.00 89.38  ? 164 TRP   H N   1 
ATOM   14296 C  CA  . TRP   H  8  163 ? 73.313  -147.677 47.537  1.00 90.35  ? 164 TRP   H CA  1 
ATOM   14297 C  C   . TRP   H  8  163 ? 72.092  -148.591 47.348  1.00 91.53  ? 164 TRP   H C   1 
ATOM   14298 O  O   . TRP   H  8  163 ? 72.148  -149.461 46.454  1.00 89.71  ? 164 TRP   H O   1 
ATOM   14299 C  CB  . TRP   H  8  163 ? 74.219  -148.162 48.678  1.00 90.75  ? 164 TRP   H CB  1 
ATOM   14300 C  CG  . TRP   H  8  163 ? 75.415  -147.291 48.917  1.00 90.17  ? 164 TRP   H CG  1 
ATOM   14301 C  CD1 . TRP   H  8  163 ? 75.806  -146.738 50.102  1.00 90.53  ? 164 TRP   H CD1 1 
ATOM   14302 C  CD2 . TRP   H  8  163 ? 76.378  -146.860 47.938  1.00 90.25  ? 164 TRP   H CD2 1 
ATOM   14303 N  NE1 . TRP   H  8  163 ? 76.942  -145.996 49.928  1.00 91.59  ? 164 TRP   H NE1 1 
ATOM   14304 C  CE2 . TRP   H  8  163 ? 77.318  -146.052 48.613  1.00 90.93  ? 164 TRP   H CE2 1 
ATOM   14305 C  CE3 . TRP   H  8  163 ? 76.540  -147.077 46.564  1.00 90.21  ? 164 TRP   H CE3 1 
ATOM   14306 C  CZ2 . TRP   H  8  163 ? 78.399  -145.464 47.958  1.00 92.14  ? 164 TRP   H CZ2 1 
ATOM   14307 C  CZ3 . TRP   H  8  163 ? 77.609  -146.497 45.919  1.00 90.71  ? 164 TRP   H CZ3 1 
ATOM   14308 C  CH2 . TRP   H  8  163 ? 78.525  -145.702 46.608  1.00 91.50  ? 164 TRP   H CH2 1 
ATOM   14309 N  N   . ASN   H  8  164 ? 71.024  -148.392 48.130  1.00 91.45  ? 165 ASN   H N   1 
ATOM   14310 C  CA  . ASN   H  8  164 ? 69.903  -149.364 48.271  1.00 91.80  ? 165 ASN   H CA  1 
ATOM   14311 C  C   . ASN   H  8  164 ? 68.699  -148.965 47.402  1.00 93.04  ? 165 ASN   H C   1 
ATOM   14312 O  O   . ASN   H  8  164 ? 68.009  -149.877 46.916  1.00 89.95  ? 165 ASN   H O   1 
ATOM   14313 C  CB  . ASN   H  8  164 ? 69.521  -149.548 49.743  1.00 93.71  ? 165 ASN   H CB  1 
ATOM   14314 C  CG  . ASN   H  8  164 ? 70.683  -150.019 50.594  1.00 94.39  ? 165 ASN   H CG  1 
ATOM   14315 O  OD1 . ASN   H  8  164 ? 71.066  -149.358 51.554  1.00 101.39 ? 165 ASN   H OD1 1 
ATOM   14316 N  ND2 . ASN   H  8  164 ? 71.268  -151.152 50.246  1.00 92.84  ? 165 ASN   H ND2 1 
ATOM   14317 N  N   . ASP   H  8  165 ? 68.445  -147.670 47.206  1.00 93.74  ? 166 ASP   H N   1 
ATOM   14318 C  CA  . ASP   H  8  165 ? 67.314  -147.172 46.375  1.00 96.46  ? 166 ASP   H CA  1 
ATOM   14319 C  C   . ASP   H  8  165 ? 67.822  -146.914 44.951  1.00 95.24  ? 166 ASP   H C   1 
ATOM   14320 O  O   . ASP   H  8  165 ? 68.871  -146.248 44.806  1.00 87.98  ? 166 ASP   H O   1 
ATOM   14321 C  CB  . ASP   H  8  165 ? 66.675  -145.921 46.987  1.00 97.75  ? 166 ASP   H CB  1 
ATOM   14322 C  CG  . ASP   H  8  165 ? 65.453  -145.418 46.234  1.00 98.93  ? 166 ASP   H CG  1 
ATOM   14323 O  OD1 . ASP   H  8  165 ? 64.736  -146.255 45.645  1.00 101.49 ? 166 ASP   H OD1 1 
ATOM   14324 O  OD2 . ASP   H  8  165 ? 65.229  -144.191 46.240  1.00 97.86  ? 166 ASP   H OD2 1 
ATOM   14325 N  N   . LEU   H  8  166 ? 67.105  -147.431 43.946  1.00 95.45  ? 167 LEU   H N   1 
ATOM   14326 C  CA  . LEU   H  8  166 ? 67.416  -147.238 42.502  1.00 94.88  ? 167 LEU   H CA  1 
ATOM   14327 C  C   . LEU   H  8  166 ? 67.052  -145.810 42.080  1.00 94.60  ? 167 LEU   H C   1 
ATOM   14328 O  O   . LEU   H  8  166 ? 67.641  -145.323 41.093  1.00 90.19  ? 167 LEU   H O   1 
ATOM   14329 C  CB  . LEU   H  8  166 ? 66.641  -148.260 41.663  1.00 93.99  ? 167 LEU   H CB  1 
ATOM   14330 C  CG  . LEU   H  8  166 ? 66.951  -149.731 41.930  1.00 94.39  ? 167 LEU   H CG  1 
ATOM   14331 C  CD1 . LEU   H  8  166 ? 66.206  -150.615 40.941  1.00 93.55  ? 167 LEU   H CD1 1 
ATOM   14332 C  CD2 . LEU   H  8  166 ? 68.446  -150.006 41.865  1.00 94.58  ? 167 LEU   H CD2 1 
ATOM   14333 N  N   . GLY   H  8  167 ? 66.108  -145.180 42.789  1.00 95.23  ? 168 GLY   H N   1 
ATOM   14334 C  CA  . GLY   H  8  167 ? 65.695  -143.779 42.575  1.00 94.29  ? 168 GLY   H CA  1 
ATOM   14335 C  C   . GLY   H  8  167 ? 66.798  -142.794 42.932  1.00 93.77  ? 168 GLY   H C   1 
ATOM   14336 O  O   . GLY   H  8  167 ? 66.787  -141.682 42.364  1.00 90.08  ? 168 GLY   H O   1 
ATOM   14337 N  N   . SER   H  8  168 ? 67.707  -143.179 43.839  1.00 94.44  ? 169 SER   H N   1 
ATOM   14338 C  CA  . SER   H  8  168 ? 68.749  -142.312 44.454  1.00 92.36  ? 169 SER   H CA  1 
ATOM   14339 C  C   . SER   H  8  168 ? 70.152  -142.800 44.086  1.00 98.19  ? 169 SER   H C   1 
ATOM   14340 O  O   . SER   H  8  168 ? 70.361  -144.030 44.083  1.00 97.95  ? 169 SER   H O   1 
ATOM   14341 C  CB  . SER   H  8  168 ? 68.597  -142.287 45.943  1.00 92.56  ? 169 SER   H CB  1 
ATOM   14342 O  OG  . SER   H  8  168 ? 67.457  -141.529 46.313  1.00 92.84  ? 169 SER   H OG  1 
ATOM   14343 N  N   . GLY   H  8  169 ? 71.081  -141.873 43.830  1.00 96.06  ? 170 GLY   H N   1 
ATOM   14344 C  CA  . GLY   H  8  169 ? 72.464  -142.203 43.430  1.00 98.54  ? 170 GLY   H CA  1 
ATOM   14345 C  C   . GLY   H  8  169 ? 73.402  -141.005 43.424  1.00 97.83  ? 170 GLY   H C   1 
ATOM   14346 O  O   . GLY   H  8  169 ? 73.009  -139.925 43.913  1.00 92.53  ? 170 GLY   H O   1 
ATOM   14347 N  N   . SER   H  8  170 ? 74.612  -141.216 42.894  1.00 99.86  ? 171 SER   H N   1 
ATOM   14348 C  CA  . SER   H  8  170 ? 75.678  -140.205 42.666  1.00 100.48 ? 171 SER   H CA  1 
ATOM   14349 C  C   . SER   H  8  170 ? 76.216  -139.677 44.005  1.00 102.09 ? 171 SER   H C   1 
ATOM   14350 O  O   . SER   H  8  170 ? 76.811  -140.484 44.748  1.00 108.49 ? 171 SER   H O   1 
ATOM   14351 C  CB  . SER   H  8  170 ? 75.196  -139.102 41.754  1.00 100.61 ? 171 SER   H CB  1 
ATOM   14352 O  OG  . SER   H  8  170 ? 74.924  -139.605 40.456  1.00 102.98 ? 171 SER   H OG  1 
ATOM   14353 N  N   . ASN   H  8  171 ? 76.005  -138.390 44.310  1.00 98.37  ? 172 ASN   H N   1 
ATOM   14354 C  CA  . ASN   H  8  171 ? 76.769  -137.627 45.336  1.00 95.23  ? 172 ASN   H CA  1 
ATOM   14355 C  C   . ASN   H  8  171 ? 75.855  -137.243 46.506  1.00 93.44  ? 172 ASN   H C   1 
ATOM   14356 O  O   . ASN   H  8  171 ? 74.630  -137.439 46.398  1.00 89.90  ? 172 ASN   H O   1 
ATOM   14357 C  CB  . ASN   H  8  171 ? 77.417  -136.382 44.721  1.00 94.69  ? 172 ASN   H CB  1 
ATOM   14358 C  CG  . ASN   H  8  171 ? 78.133  -136.663 43.416  1.00 94.89  ? 172 ASN   H CG  1 
ATOM   14359 O  OD1 . ASN   H  8  171 ? 77.961  -135.935 42.443  1.00 96.47  ? 172 ASN   H OD1 1 
ATOM   14360 N  ND2 . ASN   H  8  171 ? 78.936  -137.713 43.379  1.00 93.95  ? 172 ASN   H ND2 1 
ATOM   14361 N  N   . VAL   H  8  172 ? 76.447  -136.715 47.582  1.00 95.08  ? 173 VAL   H N   1 
ATOM   14362 C  CA  . VAL   H  8  172 ? 75.734  -136.176 48.779  1.00 98.42  ? 173 VAL   H CA  1 
ATOM   14363 C  C   . VAL   H  8  172 ? 75.963  -134.662 48.847  1.00 99.96  ? 173 VAL   H C   1 
ATOM   14364 O  O   . VAL   H  8  172 ? 77.135  -134.245 48.974  1.00 103.59 ? 173 VAL   H O   1 
ATOM   14365 C  CB  . VAL   H  8  172 ? 76.207  -136.855 50.078  1.00 98.03  ? 173 VAL   H CB  1 
ATOM   14366 C  CG1 . VAL   H  8  172 ? 75.438  -136.349 51.291  1.00 97.78  ? 173 VAL   H CG1 1 
ATOM   14367 C  CG2 . VAL   H  8  172 ? 76.127  -138.372 49.990  1.00 98.07  ? 173 VAL   H CG2 1 
ATOM   14368 N  N   . ASP   H  8  173 ? 74.882  -133.880 48.769  1.00 101.43 ? 174 ASP   H N   1 
ATOM   14369 C  CA  . ASP   H  8  173 ? 74.871  -132.426 49.079  1.00 100.25 ? 174 ASP   H CA  1 
ATOM   14370 C  C   . ASP   H  8  173 ? 74.452  -132.257 50.542  1.00 96.99  ? 174 ASP   H C   1 
ATOM   14371 O  O   . ASP   H  8  173 ? 73.623  -133.052 51.018  1.00 91.15  ? 174 ASP   H O   1 
ATOM   14372 C  CB  . ASP   H  8  173 ? 73.938  -131.647 48.149  1.00 101.09 ? 174 ASP   H CB  1 
ATOM   14373 C  CG  . ASP   H  8  173 ? 74.376  -131.617 46.695  1.00 104.35 ? 174 ASP   H CG  1 
ATOM   14374 O  OD1 . ASP   H  8  173 ? 75.531  -132.007 46.419  1.00 102.76 ? 174 ASP   H OD1 1 
ATOM   14375 O  OD2 . ASP   H  8  173 ? 73.558  -131.197 45.848  1.00 106.91 ? 174 ASP   H OD2 1 
ATOM   14376 N  N   . VAL   H  8  174 ? 75.023  -131.261 51.218  1.00 99.21  ? 175 VAL   H N   1 
ATOM   14377 C  CA  . VAL   H  8  174 ? 74.755  -130.934 52.649  1.00 102.44 ? 175 VAL   H CA  1 
ATOM   14378 C  C   . VAL   H  8  174 ? 74.615  -129.412 52.766  1.00 103.18 ? 175 VAL   H C   1 
ATOM   14379 O  O   . VAL   H  8  174 ? 75.293  -128.695 52.000  1.00 103.61 ? 175 VAL   H O   1 
ATOM   14380 C  CB  . VAL   H  8  174 ? 75.877  -131.471 53.562  1.00 102.91 ? 175 VAL   H CB  1 
ATOM   14381 C  CG1 . VAL   H  8  174 ? 75.731  -130.997 55.001  1.00 106.30 ? 175 VAL   H CG1 1 
ATOM   14382 C  CG2 . VAL   H  8  174 ? 75.975  -132.989 53.511  1.00 102.11 ? 175 VAL   H CG2 1 
ATOM   14383 N  N   . CYS   H  8  175 ? 73.757  -128.945 53.675  1.00 101.85 ? 176 CYS   H N   1 
ATOM   14384 C  CA  . CYS   H  8  175 ? 73.699  -127.531 54.127  1.00 101.71 ? 176 CYS   H CA  1 
ATOM   14385 C  C   . CYS   H  8  175 ? 73.566  -127.501 55.650  1.00 98.71  ? 176 CYS   H C   1 
ATOM   14386 O  O   . CYS   H  8  175 ? 72.605  -128.103 56.173  1.00 92.96  ? 176 CYS   H O   1 
ATOM   14387 C  CB  . CYS   H  8  175 ? 72.548  -126.768 53.484  1.00 101.46 ? 176 CYS   H CB  1 
ATOM   14388 S  SG  . CYS   H  8  175 ? 72.634  -124.980 53.775  1.00 104.62 ? 176 CYS   H SG  1 
ATOM   14389 N  N   . VAL   H  8  176 ? 74.511  -126.834 56.318  1.00 102.82 ? 177 VAL   H N   1 
ATOM   14390 C  CA  . VAL   H  8  176 ? 74.556  -126.679 57.800  1.00 102.66 ? 177 VAL   H CA  1 
ATOM   14391 C  C   . VAL   H  8  176 ? 74.075  -125.267 58.144  1.00 103.54 ? 177 VAL   H C   1 
ATOM   14392 O  O   . VAL   H  8  176 ? 74.724  -124.293 57.704  1.00 105.36 ? 177 VAL   H O   1 
ATOM   14393 C  CB  . VAL   H  8  176 ? 75.965  -126.942 58.364  1.00 99.16  ? 177 VAL   H CB  1 
ATOM   14394 C  CG1 . VAL   H  8  176 ? 75.941  -127.016 59.882  1.00 99.51  ? 177 VAL   H CG1 1 
ATOM   14395 C  CG2 . VAL   H  8  176 ? 76.594  -128.195 57.775  1.00 97.40  ? 177 VAL   H CG2 1 
ATOM   14396 N  N   . MET   H  8  177 ? 72.970  -125.177 58.885  1.00 103.36 ? 178 MET   H N   1 
ATOM   14397 C  CA  . MET   H  8  177 ? 72.409  -123.909 59.417  1.00 104.74 ? 178 MET   H CA  1 
ATOM   14398 C  C   . MET   H  8  177 ? 72.583  -123.908 60.937  1.00 105.75 ? 178 MET   H C   1 
ATOM   14399 O  O   . MET   H  8  177 ? 71.812  -124.608 61.621  1.00 106.31 ? 178 MET   H O   1 
ATOM   14400 C  CB  . MET   H  8  177 ? 70.929  -123.777 59.054  1.00 102.15 ? 178 MET   H CB  1 
ATOM   14401 C  CG  . MET   H  8  177 ? 70.710  -123.414 57.602  1.00 105.40 ? 178 MET   H CG  1 
ATOM   14402 S  SD  . MET   H  8  177 ? 69.253  -124.226 56.907  1.00 106.71 ? 178 MET   H SD  1 
ATOM   14403 C  CE  . MET   H  8  177 ? 69.880  -125.888 56.683  1.00 106.82 ? 178 MET   H CE  1 
ATOM   14404 N  N   . GLU   H  8  178 ? 73.583  -123.169 61.424  1.00 107.29 ? 179 GLU   H N   1 
ATOM   14405 C  CA  . GLU   H  8  178 ? 73.926  -123.040 62.865  1.00 108.43 ? 179 GLU   H CA  1 
ATOM   14406 C  C   . GLU   H  8  178 ? 73.474  -121.658 63.350  1.00 108.79 ? 179 GLU   H C   1 
ATOM   14407 O  O   . GLU   H  8  178 ? 73.527  -120.712 62.541  1.00 114.01 ? 179 GLU   H O   1 
ATOM   14408 C  CB  . GLU   H  8  178 ? 75.428  -123.258 63.044  1.00 112.66 ? 179 GLU   H CB  1 
ATOM   14409 C  CG  . GLU   H  8  178 ? 75.873  -123.316 64.493  1.00 117.14 ? 179 GLU   H CG  1 
ATOM   14410 C  CD  . GLU   H  8  178 ? 77.207  -124.013 64.717  1.00 119.66 ? 179 GLU   H CD  1 
ATOM   14411 O  OE1 . GLU   H  8  178 ? 77.446  -124.476 65.850  1.00 122.63 ? 179 GLU   H OE1 1 
ATOM   14412 O  OE2 . GLU   H  8  178 ? 78.005  -124.097 63.759  1.00 124.83 ? 179 GLU   H OE2 1 
ATOM   14413 N  N   . ILE   H  8  179 ? 73.036  -121.552 64.610  1.00 105.05 ? 180 ILE   H N   1 
ATOM   14414 C  CA  . ILE   H  8  179 ? 72.565  -120.273 65.226  1.00 104.28 ? 180 ILE   H CA  1 
ATOM   14415 C  C   . ILE   H  8  179 ? 73.779  -119.356 65.425  1.00 103.16 ? 180 ILE   H C   1 
ATOM   14416 O  O   . ILE   H  8  179 ? 74.786  -119.821 65.988  1.00 104.98 ? 180 ILE   H O   1 
ATOM   14417 C  CB  . ILE   H  8  179 ? 71.811  -120.512 66.554  1.00 103.19 ? 180 ILE   H CB  1 
ATOM   14418 C  CG1 . ILE   H  8  179 ? 70.594  -121.426 66.380  1.00 102.39 ? 180 ILE   H CG1 1 
ATOM   14419 C  CG2 . ILE   H  8  179 ? 71.410  -119.188 67.190  1.00 103.40 ? 180 ILE   H CG2 1 
ATOM   14420 C  CD1 . ILE   H  8  179 ? 70.137  -122.086 67.662  1.00 102.23 ? 180 ILE   H CD1 1 
ATOM   14421 N  N   . GLY   H  8  180 ? 73.681  -118.103 64.974  1.00 104.20 ? 181 GLY   H N   1 
ATOM   14422 C  CA  . GLY   H  8  180 ? 74.712  -117.067 65.175  1.00 108.51 ? 181 GLY   H CA  1 
ATOM   14423 C  C   . GLY   H  8  180 ? 75.815  -117.111 64.127  1.00 111.05 ? 181 GLY   H C   1 
ATOM   14424 O  O   . GLY   H  8  180 ? 76.749  -116.292 64.242  1.00 117.03 ? 181 GLY   H O   1 
ATOM   14425 N  N   . LYS   H  8  181 ? 75.727  -118.015 63.143  1.00 107.45 ? 182 LYS   H N   1 
ATOM   14426 C  CA  . LYS   H  8  181 ? 76.756  -118.202 62.080  1.00 107.76 ? 182 LYS   H CA  1 
ATOM   14427 C  C   . LYS   H  8  181 ? 76.111  -118.349 60.706  1.00 102.20 ? 182 LYS   H C   1 
ATOM   14428 O  O   . LYS   H  8  181 ? 75.025  -118.946 60.645  1.00 98.80  ? 182 LYS   H O   1 
ATOM   14429 C  CB  . LYS   H  8  181 ? 77.527  -119.503 62.277  1.00 109.89 ? 182 LYS   H CB  1 
ATOM   14430 C  CG  . LYS   H  8  181 ? 78.430  -119.539 63.492  1.00 115.42 ? 182 LYS   H CG  1 
ATOM   14431 C  CD  . LYS   H  8  181 ? 79.495  -120.585 63.351  1.00 118.75 ? 182 LYS   H CD  1 
ATOM   14432 C  CE  . LYS   H  8  181 ? 80.515  -120.515 64.460  1.00 125.39 ? 182 LYS   H CE  1 
ATOM   14433 N  NZ  . LYS   H  8  181 ? 81.688  -121.364 64.154  1.00 131.56 ? 182 LYS   H NZ  1 
ATOM   14434 N  N   . ASP   H  8  182 ? 76.779  -117.879 59.649  1.00 104.43 ? 183 ASP   H N   1 
ATOM   14435 C  CA  . ASP   H  8  182 ? 76.284  -117.970 58.249  1.00 107.48 ? 183 ASP   H CA  1 
ATOM   14436 C  C   . ASP   H  8  182 ? 76.029  -119.445 57.916  1.00 104.20 ? 183 ASP   H C   1 
ATOM   14437 O  O   . ASP   H  8  182 ? 76.876  -120.284 58.279  1.00 108.33 ? 183 ASP   H O   1 
ATOM   14438 C  CB  . ASP   H  8  182 ? 77.271  -117.342 57.259  1.00 111.17 ? 183 ASP   H CB  1 
ATOM   14439 C  CG  . ASP   H  8  182 ? 77.385  -115.827 57.353  1.00 114.50 ? 183 ASP   H CG  1 
ATOM   14440 O  OD1 . ASP   H  8  182 ? 76.533  -115.207 58.026  1.00 115.16 ? 183 ASP   H OD1 1 
ATOM   14441 O  OD2 . ASP   H  8  182 ? 78.326  -115.276 56.746  1.00 119.80 ? 183 ASP   H OD2 1 
ATOM   14442 N  N   . ALA   H  8  183 ? 74.896  -119.748 57.275  1.00 104.14 ? 184 ALA   H N   1 
ATOM   14443 C  CA  . ALA   H  8  183 ? 74.571  -121.086 56.727  1.00 104.14 ? 184 ALA   H CA  1 
ATOM   14444 C  C   . ALA   H  8  183 ? 75.677  -121.486 55.745  1.00 100.59 ? 184 ALA   H C   1 
ATOM   14445 O  O   . ALA   H  8  183 ? 76.009  -120.651 54.890  1.00 103.77 ? 184 ALA   H O   1 
ATOM   14446 C  CB  . ALA   H  8  183 ? 73.225  -121.048 56.044  1.00 104.30 ? 184 ALA   H CB  1 
ATOM   14447 N  N   . GLU   H  8  184 ? 76.245  -122.691 55.855  1.00 99.01  ? 185 GLU   H N   1 
ATOM   14448 C  CA  . GLU   H  8  184 ? 77.278  -123.154 54.885  1.00 98.37  ? 185 GLU   H CA  1 
ATOM   14449 C  C   . GLU   H  8  184 ? 76.700  -124.284 54.024  1.00 96.63  ? 185 GLU   H C   1 
ATOM   14450 O  O   . GLU   H  8  184 ? 76.395  -125.362 54.562  1.00 96.53  ? 185 GLU   H O   1 
ATOM   14451 C  CB  . GLU   H  8  184 ? 78.606  -123.498 55.566  1.00 99.51  ? 185 GLU   H CB  1 
ATOM   14452 C  CG  . GLU   H  8  184 ? 78.548  -124.577 56.628  1.00 99.50  ? 185 GLU   H CG  1 
ATOM   14453 C  CD  . GLU   H  8  184 ? 79.921  -124.953 57.165  1.00 102.49 ? 185 GLU   H CD  1 
ATOM   14454 O  OE1 . GLU   H  8  184 ? 80.026  -125.231 58.376  1.00 104.70 ? 185 GLU   H OE1 1 
ATOM   14455 O  OE2 . GLU   H  8  184 ? 80.888  -124.967 56.371  1.00 101.64 ? 185 GLU   H OE2 1 
ATOM   14456 N  N   . TYR   H  8  185 ? 76.530  -123.996 52.729  1.00 96.38  ? 186 TYR   H N   1 
ATOM   14457 C  CA  . TYR   H  8  185 ? 76.091  -124.927 51.658  1.00 94.42  ? 186 TYR   H CA  1 
ATOM   14458 C  C   . TYR   H  8  185 ? 77.302  -125.725 51.166  1.00 95.64  ? 186 TYR   H C   1 
ATOM   14459 O  O   . TYR   H  8  185 ? 78.218  -125.136 50.567  1.00 93.37  ? 186 TYR   H O   1 
ATOM   14460 C  CB  . TYR   H  8  185 ? 75.449  -124.140 50.512  1.00 94.89  ? 186 TYR   H CB  1 
ATOM   14461 C  CG  . TYR   H  8  185 ? 75.011  -124.955 49.321  1.00 94.31  ? 186 TYR   H CG  1 
ATOM   14462 C  CD1 . TYR   H  8  185 ? 74.237  -126.094 49.469  1.00 93.30  ? 186 TYR   H CD1 1 
ATOM   14463 C  CD2 . TYR   H  8  185 ? 75.338  -124.561 48.033  1.00 95.54  ? 186 TYR   H CD2 1 
ATOM   14464 C  CE1 . TYR   H  8  185 ? 73.819  -126.832 48.373  1.00 94.41  ? 186 TYR   H CE1 1 
ATOM   14465 C  CE2 . TYR   H  8  185 ? 74.925  -125.284 46.926  1.00 93.63  ? 186 TYR   H CE2 1 
ATOM   14466 C  CZ  . TYR   H  8  185 ? 74.162  -126.424 47.095  1.00 92.59  ? 186 TYR   H CZ  1 
ATOM   14467 O  OH  . TYR   H  8  185 ? 73.758  -127.133 46.002  1.00 94.52  ? 186 TYR   H OH  1 
ATOM   14468 N  N   . LEU   H  8  186 ? 77.297  -127.035 51.410  1.00 95.66  ? 187 LEU   H N   1 
ATOM   14469 C  CA  . LEU   H  8  186 ? 78.398  -127.956 51.029  1.00 96.30  ? 187 LEU   H CA  1 
ATOM   14470 C  C   . LEU   H  8  186 ? 77.964  -128.776 49.810  1.00 95.87  ? 187 LEU   H C   1 
ATOM   14471 O  O   . LEU   H  8  186 ? 77.505  -129.916 49.989  1.00 98.08  ? 187 LEU   H O   1 
ATOM   14472 C  CB  . LEU   H  8  186 ? 78.735  -128.842 52.230  1.00 95.21  ? 187 LEU   H CB  1 
ATOM   14473 C  CG  . LEU   H  8  186 ? 79.345  -128.110 53.424  1.00 96.22  ? 187 LEU   H CG  1 
ATOM   14474 C  CD1 . LEU   H  8  186 ? 79.370  -129.007 54.651  1.00 96.40  ? 187 LEU   H CD1 1 
ATOM   14475 C  CD2 . LEU   H  8  186 ? 80.743  -127.606 53.099  1.00 97.74  ? 187 LEU   H CD2 1 
ATOM   14476 N  N   . ARG   H  8  187 ? 78.097  -128.186 48.619  1.00 97.55  ? 188 ARG   H N   1 
ATOM   14477 C  CA  . ARG   H  8  187 ? 77.759  -128.805 47.310  1.00 96.01  ? 188 ARG   H CA  1 
ATOM   14478 C  C   . ARG   H  8  187 ? 78.759  -129.929 47.014  1.00 93.95  ? 188 ARG   H C   1 
ATOM   14479 O  O   . ARG   H  8  187 ? 79.968  -129.643 46.994  1.00 91.01  ? 188 ARG   H O   1 
ATOM   14480 C  CB  . ARG   H  8  187 ? 77.768  -127.725 46.222  1.00 98.74  ? 188 ARG   H CB  1 
ATOM   14481 C  CG  . ARG   H  8  187 ? 77.725  -128.255 44.798  1.00 100.43 ? 188 ARG   H CG  1 
ATOM   14482 C  CD  . ARG   H  8  187 ? 76.471  -129.054 44.517  1.00 99.94  ? 188 ARG   H CD  1 
ATOM   14483 N  NE  . ARG   H  8  187 ? 76.223  -129.128 43.087  1.00 101.65 ? 188 ARG   H NE  1 
ATOM   14484 C  CZ  . ARG   H  8  187 ? 75.264  -129.845 42.516  1.00 100.37 ? 188 ARG   H CZ  1 
ATOM   14485 N  NH1 . ARG   H  8  187 ? 74.450  -130.590 43.247  1.00 96.62  ? 188 ARG   H NH1 1 
ATOM   14486 N  NH2 . ARG   H  8  187 ? 75.136  -129.824 41.200  1.00 104.97 ? 188 ARG   H NH2 1 
ATOM   14487 N  N   . ASN   H  8  188 ? 78.260  -131.151 46.791  1.00 93.20  ? 189 ASN   H N   1 
ATOM   14488 C  CA  . ASN   H  8  188 ? 79.063  -132.381 46.541  1.00 93.63  ? 189 ASN   H CA  1 
ATOM   14489 C  C   . ASN   H  8  188 ? 80.013  -132.617 47.720  1.00 94.08  ? 189 ASN   H C   1 
ATOM   14490 O  O   . ASN   H  8  188 ? 81.232  -132.760 47.485  1.00 92.11  ? 189 ASN   H O   1 
ATOM   14491 C  CB  . ASN   H  8  188 ? 79.808  -132.310 45.205  1.00 94.50  ? 189 ASN   H CB  1 
ATOM   14492 C  CG  . ASN   H  8  188 ? 78.879  -132.389 44.013  1.00 94.63  ? 189 ASN   H CG  1 
ATOM   14493 O  OD1 . ASN   H  8  188 ? 77.658  -132.412 44.167  1.00 93.97  ? 189 ASN   H OD1 1 
ATOM   14494 N  ND2 . ASN   H  8  188 ? 79.447  -132.436 42.820  1.00 97.29  ? 189 ASN   H ND2 1 
ATOM   14495 N  N   . TYR   H  8  189 ? 79.455  -132.658 48.935  1.00 95.52  ? 190 TYR   H N   1 
ATOM   14496 C  CA  . TYR   H  8  189 ? 80.172  -132.904 50.215  1.00 99.27  ? 190 TYR   H CA  1 
ATOM   14497 C  C   . TYR   H  8  189 ? 80.855  -134.274 50.164  1.00 99.86  ? 190 TYR   H C   1 
ATOM   14498 O  O   . TYR   H  8  189 ? 82.003  -134.387 50.638  1.00 102.18 ? 190 TYR   H O   1 
ATOM   14499 C  CB  . TYR   H  8  189 ? 79.202  -132.807 51.395  1.00 99.96  ? 190 TYR   H CB  1 
ATOM   14500 C  CG  . TYR   H  8  189 ? 79.783  -133.222 52.723  1.00 100.93 ? 190 TYR   H CG  1 
ATOM   14501 C  CD1 . TYR   H  8  189 ? 80.681  -132.410 53.399  1.00 100.60 ? 190 TYR   H CD1 1 
ATOM   14502 C  CD2 . TYR   H  8  189 ? 79.433  -134.428 53.308  1.00 100.14 ? 190 TYR   H CD2 1 
ATOM   14503 C  CE1 . TYR   H  8  189 ? 81.217  -132.786 54.620  1.00 99.05  ? 190 TYR   H CE1 1 
ATOM   14504 C  CE2 . TYR   H  8  189 ? 79.959  -134.819 54.529  1.00 99.71  ? 190 TYR   H CE2 1 
ATOM   14505 C  CZ  . TYR   H  8  189 ? 80.855  -133.995 55.187  1.00 98.89  ? 190 TYR   H CZ  1 
ATOM   14506 O  OH  . TYR   H  8  189 ? 81.375  -134.374 56.389  1.00 100.50 ? 190 TYR   H OH  1 
ATOM   14507 N  N   . LEU   H  8  190 ? 80.155  -135.275 49.617  1.00 101.62 ? 191 LEU   H N   1 
ATOM   14508 C  CA  . LEU   H  8  190 ? 80.694  -136.627 49.301  1.00 102.40 ? 191 LEU   H CA  1 
ATOM   14509 C  C   . LEU   H  8  190 ? 80.450  -136.937 47.820  1.00 98.67  ? 191 LEU   H C   1 
ATOM   14510 O  O   . LEU   H  8  190 ? 79.335  -136.664 47.337  1.00 94.41  ? 191 LEU   H O   1 
ATOM   14511 C  CB  . LEU   H  8  190 ? 80.004  -137.674 50.180  1.00 102.47 ? 191 LEU   H CB  1 
ATOM   14512 C  CG  . LEU   H  8  190 ? 80.455  -137.725 51.637  1.00 104.86 ? 191 LEU   H CG  1 
ATOM   14513 C  CD1 . LEU   H  8  190 ? 79.502  -138.578 52.461  1.00 103.48 ? 191 LEU   H CD1 1 
ATOM   14514 C  CD2 . LEU   H  8  190 ? 81.877  -138.252 51.746  1.00 107.45 ? 191 LEU   H CD2 1 
ATOM   14515 N  N   . THR   H  8  191 ? 81.451  -137.509 47.144  1.00 100.10 ? 192 THR   H N   1 
ATOM   14516 C  CA  . THR   H  8  191 ? 81.364  -137.988 45.739  1.00 103.33 ? 192 THR   H CA  1 
ATOM   14517 C  C   . THR   H  8  191 ? 81.850  -139.434 45.675  1.00 105.40 ? 192 THR   H C   1 
ATOM   14518 O  O   . THR   H  8  191 ? 82.935  -139.710 45.165  1.00 111.07 ? 192 THR   H O   1 
ATOM   14519 C  CB  . THR   H  8  191 ? 82.130  -137.061 44.786  1.00 101.98 ? 192 THR   H CB  1 
ATOM   14520 O  OG1 . THR   H  8  191 ? 83.494  -136.994 45.202  1.00 102.49 ? 192 THR   H OG1 1 
ATOM   14521 C  CG2 . THR   H  8  191 ? 81.536  -135.671 44.733  1.00 101.55 ? 192 THR   H CG2 1 
ATOM   14522 N  N   . PRO   H  8  192 ? 81.052  -140.401 46.185  1.00 102.20 ? 193 PRO   H N   1 
ATOM   14523 C  CA  . PRO   H  8  192 ? 81.472  -141.799 46.256  1.00 103.11 ? 193 PRO   H CA  1 
ATOM   14524 C  C   . PRO   H  8  192 ? 81.137  -142.631 45.005  1.00 102.13 ? 193 PRO   H C   1 
ATOM   14525 O  O   . PRO   H  8  192 ? 81.178  -143.843 45.099  1.00 102.36 ? 193 PRO   H O   1 
ATOM   14526 C  CB  . PRO   H  8  192 ? 80.689  -142.301 47.482  1.00 101.81 ? 193 PRO   H CB  1 
ATOM   14527 C  CG  . PRO   H  8  192 ? 79.416  -141.465 47.518  1.00 101.11 ? 193 PRO   H CG  1 
ATOM   14528 C  CD  . PRO   H  8  192 ? 79.701  -140.201 46.731  1.00 102.32 ? 193 PRO   H CD  1 
ATOM   14529 N  N   . ASN   H  8  193 ? 80.839  -141.981 43.873  1.00 102.32 ? 194 ASN   H N   1 
ATOM   14530 C  CA  . ASN   H  8  193 ? 80.379  -142.652 42.626  1.00 101.29 ? 194 ASN   H CA  1 
ATOM   14531 C  C   . ASN   H  8  193 ? 81.083  -142.039 41.412  1.00 101.57 ? 194 ASN   H C   1 
ATOM   14532 O  O   . ASN   H  8  193 ? 80.407  -141.790 40.397  1.00 101.97 ? 194 ASN   H O   1 
ATOM   14533 C  CB  . ASN   H  8  193 ? 78.855  -142.593 42.499  1.00 101.33 ? 194 ASN   H CB  1 
ATOM   14534 C  CG  . ASN   H  8  193 ? 78.166  -143.607 43.387  1.00 101.94 ? 194 ASN   H CG  1 
ATOM   14535 O  OD1 . ASN   H  8  193 ? 78.262  -144.809 43.149  1.00 102.34 ? 194 ASN   H OD1 1 
ATOM   14536 N  ND2 . ASN   H  8  193 ? 77.478  -143.139 44.414  1.00 103.12 ? 194 ASN   H ND2 1 
ATOM   14537 N  N   . VAL   H  8  194 ? 82.400  -141.839 41.501  1.00 103.34 ? 195 VAL   H N   1 
ATOM   14538 C  CA  . VAL   H  8  194 ? 83.241  -141.363 40.364  1.00 106.20 ? 195 VAL   H CA  1 
ATOM   14539 C  C   . VAL   H  8  194 ? 83.324  -142.501 39.341  1.00 107.39 ? 195 VAL   H C   1 
ATOM   14540 O  O   . VAL   H  8  194 ? 83.561  -143.651 39.755  1.00 110.12 ? 195 VAL   H O   1 
ATOM   14541 C  CB  . VAL   H  8  194 ? 84.638  -140.904 40.828  1.00 108.31 ? 195 VAL   H CB  1 
ATOM   14542 C  CG1 . VAL   H  8  194 ? 85.507  -140.466 39.657  1.00 106.82 ? 195 VAL   H CG1 1 
ATOM   14543 C  CG2 . VAL   H  8  194 ? 84.546  -139.792 41.862  1.00 110.06 ? 195 VAL   H CG2 1 
ATOM   14544 N  N   . ARG   H  8  195 ? 83.120  -142.182 38.060  1.00 106.74 ? 196 ARG   H N   1 
ATOM   14545 C  CA  . ARG   H  8  195 ? 83.192  -143.138 36.922  1.00 106.29 ? 196 ARG   H CA  1 
ATOM   14546 C  C   . ARG   H  8  195 ? 84.644  -143.593 36.748  1.00 109.96 ? 196 ARG   H C   1 
ATOM   14547 O  O   . ARG   H  8  195 ? 85.534  -142.722 36.745  1.00 108.89 ? 196 ARG   H O   1 
ATOM   14548 C  CB  . ARG   H  8  195 ? 82.692  -142.471 35.636  1.00 105.94 ? 196 ARG   H CB  1 
ATOM   14549 C  CG  . ARG   H  8  195 ? 81.786  -143.342 34.777  1.00 106.44 ? 196 ARG   H CG  1 
ATOM   14550 C  CD  . ARG   H  8  195 ? 82.434  -143.920 33.531  1.00 110.91 ? 196 ARG   H CD  1 
ATOM   14551 N  NE  . ARG   H  8  195 ? 81.642  -143.601 32.345  1.00 111.80 ? 196 ARG   H NE  1 
ATOM   14552 C  CZ  . ARG   H  8  195 ? 81.520  -144.360 31.254  1.00 115.62 ? 196 ARG   H CZ  1 
ATOM   14553 N  NH1 . ARG   H  8  195 ? 82.126  -145.533 31.166  1.00 119.23 ? 196 ARG   H NH1 1 
ATOM   14554 N  NH2 . ARG   H  8  195 ? 80.770  -143.938 30.249  1.00 113.00 ? 196 ARG   H NH2 1 
ATOM   14555 N  N   . GLU   H  8  196 ? 84.872  -144.901 36.605  1.00 111.04 ? 197 GLU   H N   1 
ATOM   14556 C  CA  . GLU   H  8  196 ? 86.225  -145.483 36.399  1.00 116.42 ? 197 GLU   H CA  1 
ATOM   14557 C  C   . GLU   H  8  196 ? 86.715  -145.103 34.999  1.00 118.61 ? 197 GLU   H C   1 
ATOM   14558 O  O   . GLU   H  8  196 ? 85.861  -144.872 34.117  1.00 121.42 ? 197 GLU   H O   1 
ATOM   14559 C  CB  . GLU   H  8  196 ? 86.208  -147.002 36.586  1.00 117.07 ? 197 GLU   H CB  1 
ATOM   14560 C  CG  . GLU   H  8  196 ? 85.576  -147.765 35.434  1.00 119.67 ? 197 GLU   H CG  1 
ATOM   14561 C  CD  . GLU   H  8  196 ? 85.683  -149.276 35.549  1.00 120.86 ? 197 GLU   H CD  1 
ATOM   14562 O  OE1 . GLU   H  8  196 ? 85.947  -149.927 34.520  1.00 123.54 ? 197 GLU   H OE1 1 
ATOM   14563 O  OE2 . GLU   H  8  196 ? 85.502  -149.797 36.667  1.00 125.54 ? 197 GLU   H OE2 1 
ATOM   14564 N  N   . GLU   H  8  197 ? 88.037  -145.045 34.812  1.00 122.82 ? 198 GLU   H N   1 
ATOM   14565 C  CA  . GLU   H  8  197 ? 88.680  -144.793 33.495  1.00 125.85 ? 198 GLU   H CA  1 
ATOM   14566 C  C   . GLU   H  8  197 ? 88.074  -145.743 32.458  1.00 124.75 ? 198 GLU   H C   1 
ATOM   14567 O  O   . GLU   H  8  197 ? 87.969  -146.950 32.755  1.00 125.96 ? 198 GLU   H O   1 
ATOM   14568 C  CB  . GLU   H  8  197 ? 90.195  -145.005 33.558  1.00 133.39 ? 198 GLU   H CB  1 
ATOM   14569 C  CG  . GLU   H  8  197 ? 90.992  -143.722 33.701  1.00 139.79 ? 198 GLU   H CG  1 
ATOM   14570 C  CD  . GLU   H  8  197 ? 92.375  -143.796 33.078  1.00 146.89 ? 198 GLU   H CD  1 
ATOM   14571 O  OE1 . GLU   H  8  197 ? 92.456  -143.948 31.841  1.00 151.90 ? 198 GLU   H OE1 1 
ATOM   14572 O  OE2 . GLU   H  8  197 ? 93.366  -143.721 33.829  1.00 157.39 ? 198 GLU   H OE2 1 
ATOM   14573 N  N   . LYS   H  8  198 ? 87.690  -145.213 31.295  1.00 119.95 ? 199 LYS   H N   1 
ATOM   14574 C  CA  . LYS   H  8  198 ? 87.185  -146.017 30.151  1.00 119.14 ? 199 LYS   H CA  1 
ATOM   14575 C  C   . LYS   H  8  198 ? 88.342  -146.844 29.579  1.00 116.34 ? 199 LYS   H C   1 
ATOM   14576 O  O   . LYS   H  8  198 ? 89.498  -146.383 29.655  1.00 114.44 ? 199 LYS   H O   1 
ATOM   14577 C  CB  . LYS   H  8  198 ? 86.545  -145.120 29.087  1.00 119.94 ? 199 LYS   H CB  1 
ATOM   14578 C  CG  . LYS   H  8  198 ? 85.117  -144.686 29.393  1.00 119.31 ? 199 LYS   H CG  1 
ATOM   14579 C  CD  . LYS   H  8  198 ? 84.292  -144.391 28.158  1.00 118.18 ? 199 LYS   H CD  1 
ATOM   14580 C  CE  . LYS   H  8  198 ? 84.494  -142.988 27.630  1.00 116.01 ? 199 LYS   H CE  1 
ATOM   14581 N  NZ  . LYS   H  8  198 ? 83.496  -142.051 28.196  1.00 116.53 ? 199 LYS   H NZ  1 
ATOM   14582 N  N   . GLN   H  8  199 ? 88.030  -148.023 29.035  1.00 116.35 ? 200 GLN   H N   1 
ATOM   14583 C  CA  . GLN   H  8  199 ? 89.016  -148.991 28.486  1.00 117.90 ? 200 GLN   H CA  1 
ATOM   14584 C  C   . GLN   H  8  199 ? 89.658  -148.433 27.212  1.00 119.92 ? 200 GLN   H C   1 
ATOM   14585 O  O   . GLN   H  8  199 ? 90.758  -148.902 26.856  1.00 126.36 ? 200 GLN   H O   1 
ATOM   14586 C  CB  . GLN   H  8  199 ? 88.338  -150.322 28.155  1.00 115.99 ? 200 GLN   H CB  1 
ATOM   14587 C  CG  . GLN   H  8  199 ? 87.840  -151.083 29.374  1.00 113.56 ? 200 GLN   H CG  1 
ATOM   14588 C  CD  . GLN   H  8  199 ? 88.969  -151.632 30.212  1.00 113.28 ? 200 GLN   H CD  1 
ATOM   14589 O  OE1 . GLN   H  8  199 ? 89.084  -151.333 31.396  1.00 112.29 ? 200 GLN   H OE1 1 
ATOM   14590 N  NE2 . GLN   H  8  199 ? 89.817  -152.445 29.602  1.00 116.26 ? 200 GLN   H NE2 1 
ATOM   14591 N  N   . LYS   H  8  200 ? 88.992  -147.483 26.548  1.00 119.34 ? 201 LYS   H N   1 
ATOM   14592 C  CA  . LYS   H  8  200 ? 89.307  -147.072 25.156  1.00 121.11 ? 201 LYS   H CA  1 
ATOM   14593 C  C   . LYS   H  8  200 ? 88.916  -145.604 24.938  1.00 119.16 ? 201 LYS   H C   1 
ATOM   14594 O  O   . LYS   H  8  200 ? 87.903  -145.165 25.520  1.00 120.50 ? 201 LYS   H O   1 
ATOM   14595 C  CB  . LYS   H  8  200 ? 88.553  -148.004 24.204  1.00 119.28 ? 201 LYS   H CB  1 
ATOM   14596 C  CG  . LYS   H  8  200 ? 89.049  -148.030 22.768  1.00 121.44 ? 201 LYS   H CG  1 
ATOM   14597 C  CD  . LYS   H  8  200 ? 88.299  -149.032 21.919  1.00 124.90 ? 201 LYS   H CD  1 
ATOM   14598 C  CE  . LYS   H  8  200 ? 88.771  -149.075 20.482  1.00 127.86 ? 201 LYS   H CE  1 
ATOM   14599 N  NZ  . LYS   H  8  200 ? 88.404  -147.844 19.744  1.00 127.57 ? 201 LYS   H NZ  1 
ATOM   14600 N  N   . SER   H  8  201 ? 89.703  -144.877 24.139  1.00 119.44 ? 202 SER   H N   1 
ATOM   14601 C  CA  . SER   H  8  201 ? 89.342  -143.556 23.562  1.00 118.28 ? 202 SER   H CA  1 
ATOM   14602 C  C   . SER   H  8  201 ? 88.577  -143.786 22.254  1.00 116.95 ? 202 SER   H C   1 
ATOM   14603 O  O   . SER   H  8  201 ? 89.125  -144.475 21.373  1.00 118.20 ? 202 SER   H O   1 
ATOM   14604 C  CB  . SER   H  8  201 ? 90.560  -142.703 23.329  1.00 118.62 ? 202 SER   H CB  1 
ATOM   14605 O  OG  . SER   H  8  201 ? 90.192  -141.430 22.817  1.00 117.59 ? 202 SER   H OG  1 
ATOM   14606 N  N   . TYR   H  8  202 ? 87.368  -143.229 22.134  1.00 119.35 ? 203 TYR   H N   1 
ATOM   14607 C  CA  . TYR   H  8  202 ? 86.484  -143.371 20.945  1.00 120.86 ? 203 TYR   H CA  1 
ATOM   14608 C  C   . TYR   H  8  202 ? 86.561  -142.097 20.094  1.00 117.94 ? 203 TYR   H C   1 
ATOM   14609 O  O   . TYR   H  8  202 ? 85.603  -141.798 19.354  1.00 116.25 ? 203 TYR   H O   1 
ATOM   14610 C  CB  . TYR   H  8  202 ? 85.063  -143.726 21.390  1.00 121.27 ? 203 TYR   H CB  1 
ATOM   14611 C  CG  . TYR   H  8  202 ? 84.977  -145.068 22.068  1.00 125.80 ? 203 TYR   H CG  1 
ATOM   14612 C  CD1 . TYR   H  8  202 ? 84.923  -146.238 21.328  1.00 128.57 ? 203 TYR   H CD1 1 
ATOM   14613 C  CD2 . TYR   H  8  202 ? 84.995  -145.173 23.449  1.00 127.79 ? 203 TYR   H CD2 1 
ATOM   14614 C  CE1 . TYR   H  8  202 ? 84.865  -147.479 21.941  1.00 133.03 ? 203 TYR   H CE1 1 
ATOM   14615 C  CE2 . TYR   H  8  202 ? 84.937  -146.406 24.079  1.00 132.84 ? 203 TYR   H CE2 1 
ATOM   14616 C  CZ  . TYR   H  8  202 ? 84.872  -147.564 23.321  1.00 135.04 ? 203 TYR   H CZ  1 
ATOM   14617 O  OH  . TYR   H  8  202 ? 84.812  -148.789 23.918  1.00 141.75 ? 203 TYR   H OH  1 
ATOM   14618 N  N   . LYS   H  8  203 ? 87.687  -141.384 20.195  1.00 119.70 ? 204 LYS   H N   1 
ATOM   14619 C  CA  . LYS   H  8  203 ? 88.073  -140.252 19.312  1.00 120.24 ? 204 LYS   H CA  1 
ATOM   14620 C  C   . LYS   H  8  203 ? 88.213  -140.767 17.876  1.00 123.44 ? 204 LYS   H C   1 
ATOM   14621 O  O   . LYS   H  8  203 ? 89.060  -141.654 17.654  1.00 127.06 ? 204 LYS   H O   1 
ATOM   14622 C  CB  . LYS   H  8  203 ? 89.395  -139.657 19.799  1.00 124.50 ? 204 LYS   H CB  1 
ATOM   14623 C  CG  . LYS   H  8  203 ? 89.763  -138.301 19.216  1.00 126.56 ? 204 LYS   H CG  1 
ATOM   14624 C  CD  . LYS   H  8  203 ? 90.724  -137.542 20.104  1.00 125.80 ? 204 LYS   H CD  1 
ATOM   14625 C  CE  . LYS   H  8  203 ? 91.749  -136.732 19.344  1.00 125.10 ? 204 LYS   H CE  1 
ATOM   14626 N  NZ  . LYS   H  8  203 ? 92.849  -136.305 20.239  1.00 125.75 ? 204 LYS   H NZ  1 
ATOM   14627 N  N   . PHE   H  8  204 ? 87.421  -140.229 16.944  1.00 121.03 ? 205 PHE   H N   1 
ATOM   14628 C  CA  . PHE   H  8  204 ? 87.339  -140.705 15.538  1.00 124.15 ? 205 PHE   H CA  1 
ATOM   14629 C  C   . PHE   H  8  204 ? 88.424  -140.036 14.700  1.00 127.56 ? 205 PHE   H C   1 
ATOM   14630 O  O   . PHE   H  8  204 ? 88.729  -138.862 14.907  1.00 122.21 ? 205 PHE   H O   1 
ATOM   14631 C  CB  . PHE   H  8  204 ? 85.954  -140.432 14.945  1.00 122.14 ? 205 PHE   H CB  1 
ATOM   14632 C  CG  . PHE   H  8  204 ? 84.840  -141.226 15.574  1.00 122.07 ? 205 PHE   H CG  1 
ATOM   14633 C  CD1 . PHE   H  8  204 ? 84.504  -142.484 15.095  1.00 122.78 ? 205 PHE   H CD1 1 
ATOM   14634 C  CD2 . PHE   H  8  204 ? 84.133  -140.720 16.652  1.00 118.72 ? 205 PHE   H CD2 1 
ATOM   14635 C  CE1 . PHE   H  8  204 ? 83.481  -143.216 15.679  1.00 123.55 ? 205 PHE   H CE1 1 
ATOM   14636 C  CE2 . PHE   H  8  204 ? 83.111  -141.453 17.235  1.00 119.96 ? 205 PHE   H CE2 1 
ATOM   14637 C  CZ  . PHE   H  8  204 ? 82.787  -142.699 16.748  1.00 121.65 ? 205 PHE   H CZ  1 
ATOM   14638 N  N   . PRO   H  8  205 ? 89.048  -140.768 13.744  1.00 134.18 ? 206 PRO   H N   1 
ATOM   14639 C  CA  . PRO   H  8  205 ? 89.856  -140.141 12.697  1.00 136.96 ? 206 PRO   H CA  1 
ATOM   14640 C  C   . PRO   H  8  205 ? 89.046  -139.049 11.980  1.00 136.82 ? 206 PRO   H C   1 
ATOM   14641 O  O   . PRO   H  8  205 ? 87.935  -139.334 11.569  1.00 134.83 ? 206 PRO   H O   1 
ATOM   14642 C  CB  . PRO   H  8  205 ? 90.190  -141.301 11.743  1.00 139.35 ? 206 PRO   H CB  1 
ATOM   14643 C  CG  . PRO   H  8  205 ? 90.105  -142.541 12.610  1.00 138.00 ? 206 PRO   H CG  1 
ATOM   14644 C  CD  . PRO   H  8  205 ? 89.030  -142.236 13.634  1.00 135.62 ? 206 PRO   H CD  1 
ATOM   14645 N  N   . ARG   H  8  206 ? 89.600  -137.837 11.866  1.00 134.40 ? 207 ARG   H N   1 
ATOM   14646 C  CA  . ARG   H  8  206 ? 88.909  -136.669 11.252  1.00 131.69 ? 207 ARG   H CA  1 
ATOM   14647 C  C   . ARG   H  8  206 ? 88.605  -136.980 9.783   1.00 128.35 ? 207 ARG   H C   1 
ATOM   14648 O  O   . ARG   H  8  206 ? 89.549  -137.326 9.047   1.00 129.55 ? 207 ARG   H O   1 
ATOM   14649 C  CB  . ARG   H  8  206 ? 89.755  -135.399 11.361  1.00 135.90 ? 207 ARG   H CB  1 
ATOM   14650 C  CG  . ARG   H  8  206 ? 89.956  -134.905 12.786  1.00 137.93 ? 207 ARG   H CG  1 
ATOM   14651 C  CD  . ARG   H  8  206 ? 90.573  -133.519 12.824  1.00 138.80 ? 207 ARG   H CD  1 
ATOM   14652 N  NE  . ARG   H  8  206 ? 91.091  -133.168 14.141  1.00 137.50 ? 207 ARG   H NE  1 
ATOM   14653 C  CZ  . ARG   H  8  206 ? 91.581  -131.977 14.479  1.00 135.57 ? 207 ARG   H CZ  1 
ATOM   14654 N  NH1 . ARG   H  8  206 ? 91.625  -130.992 13.596  1.00 132.85 ? 207 ARG   H NH1 1 
ATOM   14655 N  NH2 . ARG   H  8  206 ? 92.025  -131.773 15.707  1.00 134.91 ? 207 ARG   H NH2 1 
ATOM   14656 N  N   . GLY   H  8  207 ? 87.334  -136.851 9.389   1.00 127.17 ? 208 GLY   H N   1 
ATOM   14657 C  CA  . GLY   H  8  207 ? 86.824  -137.217 8.054   1.00 129.92 ? 208 GLY   H CA  1 
ATOM   14658 C  C   . GLY   H  8  207 ? 85.907  -138.429 8.100   1.00 130.96 ? 208 GLY   H C   1 
ATOM   14659 O  O   . GLY   H  8  207 ? 85.321  -138.743 7.049   1.00 136.77 ? 208 GLY   H O   1 
ATOM   14660 N  N   . THR   H  8  208 ? 85.781  -139.087 9.261   1.00 131.32 ? 209 THR   H N   1 
ATOM   14661 C  CA  . THR   H  8  208 ? 84.983  -140.332 9.446   1.00 133.80 ? 209 THR   H CA  1 
ATOM   14662 C  C   . THR   H  8  208 ? 83.538  -140.084 8.998   1.00 135.73 ? 209 THR   H C   1 
ATOM   14663 O  O   . THR   H  8  208 ? 82.985  -140.959 8.297   1.00 138.40 ? 209 THR   H O   1 
ATOM   14664 C  CB  . THR   H  8  208 ? 85.033  -140.838 10.895  1.00 135.44 ? 209 THR   H CB  1 
ATOM   14665 O  OG1 . THR   H  8  208 ? 86.398  -141.102 11.217  1.00 134.22 ? 209 THR   H OG1 1 
ATOM   14666 C  CG2 . THR   H  8  208 ? 84.205  -142.087 11.118  1.00 138.24 ? 209 THR   H CG2 1 
ATOM   14667 N  N   . THR   H  8  209 ? 82.961  -138.940 9.380   1.00 133.35 ? 210 THR   H N   1 
ATOM   14668 C  CA  . THR   H  8  209 ? 81.544  -138.582 9.106   1.00 132.14 ? 210 THR   H CA  1 
ATOM   14669 C  C   . THR   H  8  209 ? 81.417  -137.989 7.699   1.00 132.45 ? 210 THR   H C   1 
ATOM   14670 O  O   . THR   H  8  209 ? 82.133  -137.010 7.405   1.00 127.57 ? 210 THR   H O   1 
ATOM   14671 C  CB  . THR   H  8  209 ? 80.986  -137.585 10.129  1.00 129.63 ? 210 THR   H CB  1 
ATOM   14672 O  OG1 . THR   H  8  209 ? 81.279  -138.041 11.450  1.00 129.61 ? 210 THR   H OG1 1 
ATOM   14673 C  CG2 . THR   H  8  209 ? 79.493  -137.392 9.973   1.00 128.37 ? 210 THR   H CG2 1 
ATOM   14674 N  N   . ALA   H  8  210 ? 80.526  -138.561 6.883   1.00 137.68 ? 211 ALA   H N   1 
ATOM   14675 C  CA  . ALA   H  8  210 ? 80.174  -138.086 5.523   1.00 138.82 ? 211 ALA   H CA  1 
ATOM   14676 C  C   . ALA   H  8  210 ? 79.351  -136.798 5.637   1.00 135.95 ? 211 ALA   H C   1 
ATOM   14677 O  O   . ALA   H  8  210 ? 78.385  -136.781 6.428   1.00 130.77 ? 211 ALA   H O   1 
ATOM   14678 C  CB  . ALA   H  8  210 ? 79.425  -139.162 4.771   1.00 141.02 ? 211 ALA   H CB  1 
ATOM   14679 N  N   . VAL   H  8  211 ? 79.728  -135.765 4.875   1.00 136.07 ? 212 VAL   H N   1 
ATOM   14680 C  CA  . VAL   H  8  211 ? 79.124  -134.398 4.917   1.00 134.54 ? 212 VAL   H CA  1 
ATOM   14681 C  C   . VAL   H  8  211 ? 78.589  -134.038 3.525   1.00 137.51 ? 212 VAL   H C   1 
ATOM   14682 O  O   . VAL   H  8  211 ? 79.326  -134.253 2.542   1.00 138.80 ? 212 VAL   H O   1 
ATOM   14683 C  CB  . VAL   H  8  211 ? 80.155  -133.360 5.396   1.00 130.83 ? 212 VAL   H CB  1 
ATOM   14684 C  CG1 . VAL   H  8  211 ? 79.645  -131.937 5.236   1.00 128.26 ? 212 VAL   H CG1 1 
ATOM   14685 C  CG2 . VAL   H  8  211 ? 80.581  -133.619 6.832   1.00 132.59 ? 212 VAL   H CG2 1 
ATOM   14686 N  N   . LEU   H  8  212 ? 77.371  -133.484 3.458   1.00 139.92 ? 213 LEU   H N   1 
ATOM   14687 C  CA  . LEU   H  8  212 ? 76.697  -133.071 2.194   1.00 142.22 ? 213 LEU   H CA  1 
ATOM   14688 C  C   . LEU   H  8  212 ? 76.968  -131.584 1.923   1.00 139.78 ? 213 LEU   H C   1 
ATOM   14689 O  O   . LEU   H  8  212 ? 77.316  -131.255 0.773   1.00 136.51 ? 213 LEU   H O   1 
ATOM   14690 C  CB  . LEU   H  8  212 ? 75.189  -133.341 2.289   1.00 147.76 ? 213 LEU   H CB  1 
ATOM   14691 C  CG  . LEU   H  8  212 ? 74.763  -134.804 2.426   1.00 152.60 ? 213 LEU   H CG  1 
ATOM   14692 C  CD1 . LEU   H  8  212 ? 73.260  -134.911 2.647   1.00 154.60 ? 213 LEU   H CD1 1 
ATOM   14693 C  CD2 . LEU   H  8  212 ? 75.176  -135.629 1.212   1.00 153.97 ? 213 LEU   H CD2 1 
ATOM   14694 N  N   . LYS   H  8  213 ? 76.807  -130.723 2.934   1.00 138.24 ? 214 LYS   H N   1 
ATOM   14695 C  CA  . LYS   H  8  213 ? 76.912  -129.241 2.799   1.00 140.84 ? 214 LYS   H CA  1 
ATOM   14696 C  C   . LYS   H  8  213 ? 77.658  -128.623 3.986   1.00 138.66 ? 214 LYS   H C   1 
ATOM   14697 O  O   . LYS   H  8  213 ? 77.607  -129.194 5.093   1.00 140.33 ? 214 LYS   H O   1 
ATOM   14698 C  CB  . LYS   H  8  213 ? 75.528  -128.592 2.751   1.00 139.44 ? 214 LYS   H CB  1 
ATOM   14699 C  CG  . LYS   H  8  213 ? 74.725  -128.838 1.485   1.00 144.35 ? 214 LYS   H CG  1 
ATOM   14700 C  CD  . LYS   H  8  213 ? 73.337  -128.246 1.569   1.00 147.32 ? 214 LYS   H CD  1 
ATOM   14701 C  CE  . LYS   H  8  213 ? 72.602  -128.254 0.248   1.00 151.24 ? 214 LYS   H CE  1 
ATOM   14702 N  NZ  . LYS   H  8  213 ? 71.382  -127.414 0.302   1.00 151.87 ? 214 LYS   H NZ  1 
ATOM   14703 N  N   . GLU   H  8  214 ? 78.292  -127.471 3.743   1.00 137.18 ? 215 GLU   H N   1 
ATOM   14704 C  CA  . GLU   H  8  214 ? 78.901  -126.576 4.763   1.00 135.74 ? 215 GLU   H CA  1 
ATOM   14705 C  C   . GLU   H  8  214 ? 78.397  -125.150 4.522   1.00 133.15 ? 215 GLU   H C   1 
ATOM   14706 O  O   . GLU   H  8  214 ? 78.103  -124.824 3.357   1.00 136.23 ? 215 GLU   H O   1 
ATOM   14707 C  CB  . GLU   H  8  214 ? 80.428  -126.580 4.666   1.00 137.52 ? 215 GLU   H CB  1 
ATOM   14708 C  CG  . GLU   H  8  214 ? 81.090  -127.794 5.289   1.00 138.57 ? 215 GLU   H CG  1 
ATOM   14709 C  CD  . GLU   H  8  214 ? 82.582  -127.636 5.538   1.00 139.77 ? 215 GLU   H CD  1 
ATOM   14710 O  OE1 . GLU   H  8  214 ? 83.011  -126.514 5.870   1.00 139.05 ? 215 GLU   H OE1 1 
ATOM   14711 O  OE2 . GLU   H  8  214 ? 83.313  -128.639 5.406   1.00 143.88 ? 215 GLU   H OE2 1 
ATOM   14712 N  N   . SER   H  8  215 ? 78.312  -124.333 5.574   1.00 132.14 ? 216 SER   H N   1 
ATOM   14713 C  CA  . SER   H  8  215 ? 77.960  -122.890 5.482   1.00 133.11 ? 216 SER   H CA  1 
ATOM   14714 C  C   . SER   H  8  215 ? 78.295  -122.164 6.789   1.00 132.16 ? 216 SER   H C   1 
ATOM   14715 O  O   . SER   H  8  215 ? 78.204  -122.794 7.864   1.00 129.92 ? 216 SER   H O   1 
ATOM   14716 C  CB  . SER   H  8  215 ? 76.511  -122.699 5.105   1.00 131.95 ? 216 SER   H CB  1 
ATOM   14717 O  OG  . SER   H  8  215 ? 75.657  -123.488 5.919   1.00 129.79 ? 216 SER   H OG  1 
ATOM   14718 N  N   . ILE   H  8  216 ? 78.670  -120.885 6.682   1.00 132.80 ? 217 ILE   H N   1 
ATOM   14719 C  CA  . ILE   H  8  216 ? 78.922  -119.966 7.833   1.00 128.68 ? 217 ILE   H CA  1 
ATOM   14720 C  C   . ILE   H  8  216 ? 77.572  -119.410 8.296   1.00 127.26 ? 217 ILE   H C   1 
ATOM   14721 O  O   . ILE   H  8  216 ? 76.810  -118.927 7.437   1.00 124.46 ? 217 ILE   H O   1 
ATOM   14722 C  CB  . ILE   H  8  216 ? 79.898  -118.834 7.448   1.00 128.88 ? 217 ILE   H CB  1 
ATOM   14723 C  CG1 . ILE   H  8  216 ? 81.236  -119.370 6.925   1.00 129.92 ? 217 ILE   H CG1 1 
ATOM   14724 C  CG2 . ILE   H  8  216 ? 80.090  -117.868 8.609   1.00 124.78 ? 217 ILE   H CG2 1 
ATOM   14725 C  CD1 . ILE   H  8  216 ? 82.072  -120.102 7.955   1.00 129.12 ? 217 ILE   H CD1 1 
ATOM   14726 N  N   . VAL   H  8  217 ? 77.296  -119.478 9.601   1.00 128.40 ? 218 VAL   H N   1 
ATOM   14727 C  CA  . VAL   H  8  217 ? 76.044  -118.956 10.223  1.00 131.95 ? 218 VAL   H CA  1 
ATOM   14728 C  C   . VAL   H  8  217 ? 76.331  -117.542 10.735  1.00 135.93 ? 218 VAL   H C   1 
ATOM   14729 O  O   . VAL   H  8  217 ? 77.347  -117.364 11.437  1.00 140.11 ? 218 VAL   H O   1 
ATOM   14730 C  CB  . VAL   H  8  217 ? 75.532  -119.869 11.353  1.00 131.98 ? 218 VAL   H CB  1 
ATOM   14731 C  CG1 . VAL   H  8  217 ? 74.128  -119.488 11.798  1.00 128.60 ? 218 VAL   H CG1 1 
ATOM   14732 C  CG2 . VAL   H  8  217 ? 75.572  -121.333 10.958  1.00 135.13 ? 218 VAL   H CG2 1 
ATOM   14733 N  N   . ASN   H  8  218 ? 75.471  -116.583 10.382  1.00 137.25 ? 219 ASN   H N   1 
ATOM   14734 C  CA  . ASN   H  8  218 ? 75.589  -115.154 10.776  1.00 138.42 ? 219 ASN   H CA  1 
ATOM   14735 C  C   . ASN   H  8  218 ? 74.842  -114.920 12.095  1.00 140.32 ? 219 ASN   H C   1 
ATOM   14736 O  O   . ASN   H  8  218 ? 73.595  -114.958 12.082  1.00 136.26 ? 219 ASN   H O   1 
ATOM   14737 C  CB  . ASN   H  8  218 ? 75.061  -114.225 9.683   1.00 140.19 ? 219 ASN   H CB  1 
ATOM   14738 C  CG  . ASN   H  8  218 ? 75.373  -112.771 9.963   1.00 141.42 ? 219 ASN   H CG  1 
ATOM   14739 O  OD1 . ASN   H  8  218 ? 76.537  -112.376 9.973   1.00 139.87 ? 219 ASN   H OD1 1 
ATOM   14740 N  ND2 . ASN   H  8  218 ? 74.346  -111.971 10.198  1.00 143.10 ? 219 ASN   H ND2 1 
ATOM   14741 N  N   . ILE   H  8  219 ? 75.583  -114.672 13.182  1.00 142.74 ? 220 ILE   H N   1 
ATOM   14742 C  CA  . ILE   H  8  219 ? 75.033  -114.420 14.551  1.00 146.92 ? 220 ILE   H CA  1 
ATOM   14743 C  C   . ILE   H  8  219 ? 74.994  -112.908 14.821  1.00 148.95 ? 220 ILE   H C   1 
ATOM   14744 O  O   . ILE   H  8  219 ? 74.220  -112.497 15.706  1.00 149.89 ? 220 ILE   H O   1 
ATOM   14745 C  CB  . ILE   H  8  219 ? 75.824  -115.186 15.638  1.00 142.67 ? 220 ILE   H CB  1 
ATOM   14746 C  CG1 . ILE   H  8  219 ? 77.338  -114.960 15.545  1.00 137.90 ? 220 ILE   H CG1 1 
ATOM   14747 C  CG2 . ILE   H  8  219 ? 75.473  -116.666 15.601  1.00 142.79 ? 220 ILE   H CG2 1 
ATOM   14748 C  CD1 . ILE   H  8  219 ? 78.103  -115.362 16.789  1.00 133.15 ? 220 ILE   H CD1 1 
ATOM   14749 N  N   . CYS   H  8  220 ? 75.778  -112.114 14.082  1.00 158.00 ? 221 CYS   H N   1 
ATOM   14750 C  CA  . CYS   H  8  220 ? 75.879  -110.635 14.235  1.00 162.15 ? 221 CYS   H CA  1 
ATOM   14751 C  C   . CYS   H  8  220 ? 74.616  -109.960 13.679  1.00 169.48 ? 221 CYS   H C   1 
ATOM   14752 O  O   . CYS   H  8  220 ? 73.751  -110.676 13.132  1.00 175.03 ? 221 CYS   H O   1 
ATOM   14753 C  CB  . CYS   H  8  220 ? 77.116  -110.089 13.530  1.00 165.13 ? 221 CYS   H CB  1 
ATOM   14754 S  SG  . CYS   H  8  220 ? 78.676  -110.687 14.232  1.00 165.32 ? 221 CYS   H SG  1 
ATOM   14755 N  N   . ASP   H  8  221 ? 74.523  -108.632 13.824  1.00 172.67 ? 222 ASP   H N   1 
ATOM   14756 C  CA  . ASP   H  8  221 ? 73.398  -107.790 13.330  1.00 169.46 ? 222 ASP   H CA  1 
ATOM   14757 C  C   . ASP   H  8  221 ? 73.699  -107.338 11.896  1.00 164.70 ? 222 ASP   H C   1 
ATOM   14758 O  O   . ASP   H  8  221 ? 74.042  -106.182 11.643  1.00 153.42 ? 222 ASP   H O   1 
ATOM   14759 C  CB  . ASP   H  8  221 ? 73.157  -106.592 14.253  1.00 174.88 ? 222 ASP   H CB  1 
ATOM   14760 C  CG  . ASP   H  8  221 ? 72.593  -106.969 15.611  1.00 177.66 ? 222 ASP   H CG  1 
ATOM   14761 O  OD1 . ASP   H  8  221 ? 71.590  -107.710 15.644  1.00 178.73 ? 222 ASP   H OD1 1 
ATOM   14762 O  OD2 . ASP   H  8  221 ? 73.160  -106.518 16.628  1.00 183.39 ? 222 ASP   H OD2 1 
ATOM   14763 N  N   . SER   I  9  2   ? 48.531  -141.595 19.785  1.00 139.62 ? 1   SER   I N   1 
ATOM   14764 C  CA  . SER   I  9  2   ? 48.061  -140.291 20.355  1.00 136.26 ? 1   SER   I CA  1 
ATOM   14765 C  C   . SER   I  9  2   ? 48.866  -139.926 21.612  1.00 134.71 ? 1   SER   I C   1 
ATOM   14766 O  O   . SER   I  9  2   ? 48.241  -139.544 22.625  1.00 142.78 ? 1   SER   I O   1 
ATOM   14767 C  CB  . SER   I  9  2   ? 46.578  -140.329 20.638  1.00 132.61 ? 1   SER   I CB  1 
ATOM   14768 O  OG  . SER   I  9  2   ? 45.833  -140.312 19.431  1.00 133.64 ? 1   SER   I OG  1 
ATOM   14769 N  N   . ASP   I  9  3   ? 50.200  -140.036 21.544  1.00 131.23 ? 2   ASP   I N   1 
ATOM   14770 C  CA  . ASP   I  9  3   ? 51.145  -139.473 22.547  1.00 121.93 ? 2   ASP   I CA  1 
ATOM   14771 C  C   . ASP   I  9  3   ? 51.795  -138.240 21.929  1.00 117.45 ? 2   ASP   I C   1 
ATOM   14772 O  O   . ASP   I  9  3   ? 52.624  -138.370 21.031  1.00 116.24 ? 2   ASP   I O   1 
ATOM   14773 C  CB  . ASP   I  9  3   ? 52.218  -140.476 22.978  1.00 120.52 ? 2   ASP   I CB  1 
ATOM   14774 C  CG  . ASP   I  9  3   ? 53.273  -139.859 23.884  1.00 116.52 ? 2   ASP   I CG  1 
ATOM   14775 O  OD1 . ASP   I  9  3   ? 52.889  -139.101 24.796  1.00 116.49 ? 2   ASP   I OD1 1 
ATOM   14776 O  OD2 . ASP   I  9  3   ? 54.470  -140.124 23.659  1.00 117.57 ? 2   ASP   I OD2 1 
ATOM   14777 N  N   . PRO   I  9  4   ? 51.463  -137.016 22.402  1.00 110.56 ? 3   PRO   I N   1 
ATOM   14778 C  CA  . PRO   I  9  4   ? 51.818  -135.795 21.679  1.00 106.13 ? 3   PRO   I CA  1 
ATOM   14779 C  C   . PRO   I  9  4   ? 53.318  -135.681 21.361  1.00 100.47 ? 3   PRO   I C   1 
ATOM   14780 O  O   . PRO   I  9  4   ? 53.646  -135.145 20.318  1.00 93.45  ? 3   PRO   I O   1 
ATOM   14781 C  CB  . PRO   I  9  4   ? 51.382  -134.662 22.622  1.00 108.03 ? 3   PRO   I CB  1 
ATOM   14782 C  CG  . PRO   I  9  4   ? 50.353  -135.293 23.538  1.00 109.86 ? 3   PRO   I CG  1 
ATOM   14783 C  CD  . PRO   I  9  4   ? 50.771  -136.741 23.671  1.00 110.78 ? 3   PRO   I CD  1 
ATOM   14784 N  N   . SER   I  9  5   ? 54.181  -136.204 22.240  1.00 102.77 ? 4   SER   I N   1 
ATOM   14785 C  CA  . SER   I  9  5   ? 55.661  -136.075 22.152  1.00 102.44 ? 4   SER   I CA  1 
ATOM   14786 C  C   . SER   I  9  5   ? 56.256  -137.054 21.128  1.00 99.85  ? 4   SER   I C   1 
ATOM   14787 O  O   . SER   I  9  5   ? 57.476  -136.953 20.889  1.00 96.99  ? 4   SER   I O   1 
ATOM   14788 C  CB  . SER   I  9  5   ? 56.298  -136.250 23.508  1.00 105.83 ? 4   SER   I CB  1 
ATOM   14789 O  OG  . SER   I  9  5   ? 55.964  -137.513 24.062  1.00 108.30 ? 4   SER   I OG  1 
ATOM   14790 N  N   . SER   I  9  6   ? 55.454  -137.953 20.537  1.00 98.99  ? 5   SER   I N   1 
ATOM   14791 C  CA  . SER   I  9  6   ? 55.929  -138.983 19.570  1.00 101.54 ? 5   SER   I CA  1 
ATOM   14792 C  C   . SER   I  9  6   ? 54.975  -139.132 18.375  1.00 100.59 ? 5   SER   I C   1 
ATOM   14793 O  O   . SER   I  9  6   ? 54.881  -140.260 17.844  1.00 103.94 ? 5   SER   I O   1 
ATOM   14794 C  CB  . SER   I  9  6   ? 56.141  -140.307 20.263  1.00 106.15 ? 5   SER   I CB  1 
ATOM   14795 O  OG  . SER   I  9  6   ? 54.913  -140.835 20.743  1.00 115.23 ? 5   SER   I OG  1 
ATOM   14796 N  N   . ILE   I  9  7   ? 54.313  -138.051 17.947  1.00 92.25  ? 6   ILE   I N   1 
ATOM   14797 C  CA  . ILE   I  9  7   ? 53.484  -138.022 16.702  1.00 90.68  ? 6   ILE   I CA  1 
ATOM   14798 C  C   . ILE   I  9  7   ? 54.392  -137.653 15.522  1.00 88.32  ? 6   ILE   I C   1 
ATOM   14799 O  O   . ILE   I  9  7   ? 54.317  -138.339 14.487  1.00 84.91  ? 6   ILE   I O   1 
ATOM   14800 C  CB  . ILE   I  9  7   ? 52.278  -137.066 16.836  1.00 90.07  ? 6   ILE   I CB  1 
ATOM   14801 C  CG1 . ILE   I  9  7   ? 51.308  -137.531 17.926  1.00 91.80  ? 6   ILE   I CG1 1 
ATOM   14802 C  CG2 . ILE   I  9  7   ? 51.568  -136.900 15.500  1.00 91.91  ? 6   ILE   I CG2 1 
ATOM   14803 C  CD1 . ILE   I  9  7   ? 50.214  -136.537 18.256  1.00 92.85  ? 6   ILE   I CD1 1 
ATOM   14804 N  N   . ASN   I  9  8   ? 55.226  -136.619 15.681  1.00 87.26  ? 7   ASN   I N   1 
ATOM   14805 C  CA  . ASN   I  9  8   ? 56.056  -136.028 14.594  1.00 90.04  ? 7   ASN   I CA  1 
ATOM   14806 C  C   . ASN   I  9  8   ? 57.473  -136.611 14.608  1.00 90.16  ? 7   ASN   I C   1 
ATOM   14807 O  O   . ASN   I  9  8   ? 58.077  -136.706 13.520  1.00 90.35  ? 7   ASN   I O   1 
ATOM   14808 C  CB  . ASN   I  9  8   ? 56.127  -134.503 14.695  1.00 90.56  ? 7   ASN   I CB  1 
ATOM   14809 C  CG  . ASN   I  9  8   ? 54.765  -133.846 14.759  1.00 91.42  ? 7   ASN   I CG  1 
ATOM   14810 O  OD1 . ASN   I  9  8   ? 54.516  -133.022 15.635  1.00 90.40  ? 7   ASN   I OD1 1 
ATOM   14811 N  ND2 . ASN   I  9  8   ? 53.878  -134.202 13.842  1.00 92.89  ? 7   ASN   I ND2 1 
ATOM   14812 N  N   . GLY   I  9  9   ? 57.993  -136.958 15.788  1.00 90.24  ? 8   GLY   I N   1 
ATOM   14813 C  CA  . GLY   I  9  9   ? 59.351  -137.509 15.953  1.00 90.84  ? 8   GLY   I CA  1 
ATOM   14814 C  C   . GLY   I  9  9   ? 60.400  -136.421 15.841  1.00 90.55  ? 8   GLY   I C   1 
ATOM   14815 O  O   . GLY   I  9  9   ? 60.018  -135.261 15.620  1.00 95.17  ? 8   GLY   I O   1 
ATOM   14816 N  N   . GLY   I  9  10  ? 61.677  -136.782 15.987  1.00 90.05  ? 9   GLY   I N   1 
ATOM   14817 C  CA  . GLY   I  9  10  ? 62.811  -135.845 15.878  1.00 90.34  ? 9   GLY   I CA  1 
ATOM   14818 C  C   . GLY   I  9  10  ? 63.687  -135.854 17.116  1.00 88.97  ? 9   GLY   I C   1 
ATOM   14819 O  O   . GLY   I  9  10  ? 63.174  -136.198 18.199  1.00 86.94  ? 9   GLY   I O   1 
ATOM   14820 N  N   . ILE   I  9  11  ? 64.957  -135.465 16.963  1.00 89.77  ? 10  ILE   I N   1 
ATOM   14821 C  CA  . ILE   I  9  11  ? 65.967  -135.428 18.063  1.00 91.22  ? 10  ILE   I CA  1 
ATOM   14822 C  C   . ILE   I  9  11  ? 66.825  -134.163 17.968  1.00 91.92  ? 10  ILE   I C   1 
ATOM   14823 O  O   . ILE   I  9  11  ? 66.950  -133.580 16.870  1.00 88.59  ? 10  ILE   I O   1 
ATOM   14824 C  CB  . ILE   I  9  11  ? 66.855  -136.686 18.062  1.00 90.30  ? 10  ILE   I CB  1 
ATOM   14825 C  CG1 . ILE   I  9  11  ? 67.325  -137.068 16.657  1.00 91.57  ? 10  ILE   I CG1 1 
ATOM   14826 C  CG2 . ILE   I  9  11  ? 66.145  -137.833 18.755  1.00 91.89  ? 10  ILE   I CG2 1 
ATOM   14827 C  CD1 . ILE   I  9  11  ? 68.469  -138.053 16.648  1.00 93.44  ? 10  ILE   I CD1 1 
ATOM   14828 N  N   . VAL   I  9  12  ? 67.398  -133.785 19.110  1.00 92.48  ? 11  VAL   I N   1 
ATOM   14829 C  CA  . VAL   I  9  12  ? 68.392  -132.688 19.275  1.00 96.99  ? 11  VAL   I CA  1 
ATOM   14830 C  C   . VAL   I  9  12  ? 69.431  -133.167 20.291  1.00 94.43  ? 11  VAL   I C   1 
ATOM   14831 O  O   . VAL   I  9  12  ? 69.038  -133.859 21.251  1.00 94.82  ? 11  VAL   I O   1 
ATOM   14832 C  CB  . VAL   I  9  12  ? 67.714  -131.382 19.733  1.00 100.62 ? 11  VAL   I CB  1 
ATOM   14833 C  CG1 . VAL   I  9  12  ? 68.722  -130.337 20.191  1.00 102.03 ? 11  VAL   I CG1 1 
ATOM   14834 C  CG2 . VAL   I  9  12  ? 66.810  -130.810 18.652  1.00 105.30 ? 11  VAL   I CG2 1 
ATOM   14835 N  N   . VAL   I  9  13  ? 70.699  -132.814 20.083  1.00 95.36  ? 12  VAL   I N   1 
ATOM   14836 C  CA  . VAL   I  9  13  ? 71.811  -133.092 21.038  1.00 95.92  ? 12  VAL   I CA  1 
ATOM   14837 C  C   . VAL   I  9  13  ? 72.756  -131.886 21.042  1.00 96.82  ? 12  VAL   I C   1 
ATOM   14838 O  O   . VAL   I  9  13  ? 72.993  -131.316 19.959  1.00 96.38  ? 12  VAL   I O   1 
ATOM   14839 C  CB  . VAL   I  9  13  ? 72.545  -134.402 20.690  1.00 96.17  ? 12  VAL   I CB  1 
ATOM   14840 C  CG1 . VAL   I  9  13  ? 73.179  -134.364 19.308  1.00 97.92  ? 12  VAL   I CG1 1 
ATOM   14841 C  CG2 . VAL   I  9  13  ? 73.582  -134.763 21.742  1.00 97.54  ? 12  VAL   I CG2 1 
ATOM   14842 N  N   . ALA   I  9  14  ? 73.254  -131.514 22.225  1.00 98.26  ? 13  ALA   I N   1 
ATOM   14843 C  CA  . ALA   I  9  14  ? 74.239  -130.429 22.436  1.00 96.94  ? 13  ALA   I CA  1 
ATOM   14844 C  C   . ALA   I  9  14  ? 75.442  -130.983 23.206  1.00 98.59  ? 13  ALA   I C   1 
ATOM   14845 O  O   . ALA   I  9  14  ? 75.234  -131.825 24.099  1.00 94.46  ? 13  ALA   I O   1 
ATOM   14846 C  CB  . ALA   I  9  14  ? 73.596  -129.282 23.170  1.00 94.81  ? 13  ALA   I CB  1 
ATOM   14847 N  N   . MET   I  9  15  ? 76.647  -130.527 22.856  1.00 102.64 ? 14  MET   I N   1 
ATOM   14848 C  CA  . MET   I  9  15  ? 77.921  -130.923 23.512  1.00 108.22 ? 14  MET   I CA  1 
ATOM   14849 C  C   . MET   I  9  15  ? 78.798  -129.682 23.706  1.00 109.04 ? 14  MET   I C   1 
ATOM   14850 O  O   . MET   I  9  15  ? 78.686  -128.739 22.894  1.00 110.96 ? 14  MET   I O   1 
ATOM   14851 C  CB  . MET   I  9  15  ? 78.688  -131.947 22.671  1.00 110.96 ? 14  MET   I CB  1 
ATOM   14852 C  CG  . MET   I  9  15  ? 78.285  -133.380 22.928  1.00 112.48 ? 14  MET   I CG  1 
ATOM   14853 S  SD  . MET   I  9  15  ? 79.212  -134.512 21.872  1.00 117.10 ? 14  MET   I SD  1 
ATOM   14854 C  CE  . MET   I  9  15  ? 78.573  -136.090 22.436  1.00 119.71 ? 14  MET   I CE  1 
ATOM   14855 N  N   . THR   I  9  16  ? 79.640  -129.704 24.743  1.00 109.18 ? 15  THR   I N   1 
ATOM   14856 C  CA  . THR   I  9  16  ? 80.669  -128.674 25.034  1.00 107.14 ? 15  THR   I CA  1 
ATOM   14857 C  C   . THR   I  9  16  ? 82.047  -129.218 24.644  1.00 109.56 ? 15  THR   I C   1 
ATOM   14858 O  O   . THR   I  9  16  ? 82.303  -130.413 24.891  1.00 110.00 ? 15  THR   I O   1 
ATOM   14859 C  CB  . THR   I  9  16  ? 80.645  -128.268 26.512  1.00 106.44 ? 15  THR   I CB  1 
ATOM   14860 O  OG1 . THR   I  9  16  ? 81.030  -129.407 27.281  1.00 110.24 ? 15  THR   I OG1 1 
ATOM   14861 C  CG2 . THR   I  9  16  ? 79.291  -127.770 26.964  1.00 103.27 ? 15  THR   I CG2 1 
ATOM   14862 N  N   . GLY   I  9  17  ? 82.885  -128.365 24.052  1.00 111.29 ? 16  GLY   I N   1 
ATOM   14863 C  CA  . GLY   I  9  17  ? 84.306  -128.644 23.771  1.00 115.70 ? 16  GLY   I CA  1 
ATOM   14864 C  C   . GLY   I  9  17  ? 85.197  -127.591 24.404  1.00 116.85 ? 16  GLY   I C   1 
ATOM   14865 O  O   . GLY   I  9  17  ? 84.720  -126.875 25.311  1.00 109.77 ? 16  GLY   I O   1 
ATOM   14866 N  N   . LYS   I  9  18  ? 86.447  -127.494 23.943  1.00 122.45 ? 17  LYS   I N   1 
ATOM   14867 C  CA  . LYS   I  9  18  ? 87.433  -126.495 24.429  1.00 126.45 ? 17  LYS   I CA  1 
ATOM   14868 C  C   . LYS   I  9  18  ? 87.134  -125.148 23.761  1.00 124.35 ? 17  LYS   I C   1 
ATOM   14869 O  O   . LYS   I  9  18  ? 87.421  -125.010 22.555  1.00 121.20 ? 17  LYS   I O   1 
ATOM   14870 C  CB  . LYS   I  9  18  ? 88.864  -126.966 24.151  1.00 133.00 ? 17  LYS   I CB  1 
ATOM   14871 C  CG  . LYS   I  9  18  ? 89.947  -126.045 24.697  1.00 139.90 ? 17  LYS   I CG  1 
ATOM   14872 C  CD  . LYS   I  9  18  ? 91.219  -126.759 25.104  1.00 144.20 ? 17  LYS   I CD  1 
ATOM   14873 C  CE  . LYS   I  9  18  ? 92.107  -125.915 25.994  1.00 149.72 ? 17  LYS   I CE  1 
ATOM   14874 N  NZ  . LYS   I  9  18  ? 91.558  -125.798 27.366  1.00 152.93 ? 17  LYS   I NZ  1 
ATOM   14875 N  N   . ASP   I  9  19  ? 86.560  -124.209 24.522  1.00 123.43 ? 18  ASP   I N   1 
ATOM   14876 C  CA  . ASP   I  9  19  ? 86.212  -122.830 24.079  1.00 124.46 ? 18  ASP   I CA  1 
ATOM   14877 C  C   . ASP   I  9  19  ? 85.231  -122.890 22.900  1.00 121.10 ? 18  ASP   I C   1 
ATOM   14878 O  O   . ASP   I  9  19  ? 85.315  -122.007 22.022  1.00 124.69 ? 18  ASP   I O   1 
ATOM   14879 C  CB  . ASP   I  9  19  ? 87.465  -122.033 23.700  1.00 125.10 ? 18  ASP   I CB  1 
ATOM   14880 C  CG  . ASP   I  9  19  ? 88.436  -121.813 24.845  1.00 127.18 ? 18  ASP   I CG  1 
ATOM   14881 O  OD1 . ASP   I  9  19  ? 87.967  -121.528 25.965  1.00 129.05 ? 18  ASP   I OD1 1 
ATOM   14882 O  OD2 . ASP   I  9  19  ? 89.653  -121.923 24.604  1.00 131.05 ? 18  ASP   I OD2 1 
ATOM   14883 N  N   . CYS   I  9  20  ? 84.329  -123.877 22.882  1.00 119.36 ? 19  CYS   I N   1 
ATOM   14884 C  CA  . CYS   I  9  20  ? 83.343  -124.088 21.785  1.00 115.73 ? 19  CYS   I CA  1 
ATOM   14885 C  C   . CYS   I  9  20  ? 82.165  -124.938 22.274  1.00 110.11 ? 19  CYS   I C   1 
ATOM   14886 O  O   . CYS   I  9  20  ? 82.332  -125.669 23.271  1.00 106.80 ? 19  CYS   I O   1 
ATOM   14887 C  CB  . CYS   I  9  20  ? 84.001  -124.744 20.575  1.00 117.35 ? 19  CYS   I CB  1 
ATOM   14888 S  SG  . CYS   I  9  20  ? 84.527  -126.454 20.862  1.00 121.38 ? 19  CYS   I SG  1 
ATOM   14889 N  N   . VAL   I  9  21  ? 81.020  -124.831 21.592  1.00 106.75 ? 20  VAL   I N   1 
ATOM   14890 C  CA  . VAL   I  9  21  ? 79.816  -125.694 21.799  1.00 103.15 ? 20  VAL   I CA  1 
ATOM   14891 C  C   . VAL   I  9  21  ? 79.295  -126.154 20.439  1.00 102.42 ? 20  VAL   I C   1 
ATOM   14892 O  O   . VAL   I  9  21  ? 79.438  -125.402 19.454  1.00 101.01 ? 20  VAL   I O   1 
ATOM   14893 C  CB  . VAL   I  9  21  ? 78.691  -124.992 22.583  1.00 103.10 ? 20  VAL   I CB  1 
ATOM   14894 C  CG1 . VAL   I  9  21  ? 78.911  -125.084 24.079  1.00 103.29 ? 20  VAL   I CG1 1 
ATOM   14895 C  CG2 . VAL   I  9  21  ? 78.494  -123.549 22.149  1.00 104.46 ? 20  VAL   I CG2 1 
ATOM   14896 N  N   . ALA   I  9  22  ? 78.695  -127.345 20.416  1.00 100.20 ? 21  ALA   I N   1 
ATOM   14897 C  CA  . ALA   I  9  22  ? 78.037  -127.951 19.240  1.00 98.03  ? 21  ALA   I CA  1 
ATOM   14898 C  C   . ALA   I  9  22  ? 76.591  -128.292 19.607  1.00 93.38  ? 21  ALA   I C   1 
ATOM   14899 O  O   . ALA   I  9  22  ? 76.379  -128.826 20.711  1.00 90.03  ? 21  ALA   I O   1 
ATOM   14900 C  CB  . ALA   I  9  22  ? 78.801  -129.173 18.796  1.00 99.91  ? 21  ALA   I CB  1 
ATOM   14901 N  N   . ILE   I  9  23  ? 75.645  -127.968 18.723  1.00 91.72  ? 22  ILE   I N   1 
ATOM   14902 C  CA  . ILE   I  9  23  ? 74.223  -128.412 18.817  1.00 89.73  ? 22  ILE   I CA  1 
ATOM   14903 C  C   . ILE   I  9  23  ? 73.804  -128.966 17.451  1.00 89.80  ? 22  ILE   I C   1 
ATOM   14904 O  O   . ILE   I  9  23  ? 74.058  -128.296 16.431  1.00 89.03  ? 22  ILE   I O   1 
ATOM   14905 C  CB  . ILE   I  9  23  ? 73.297  -127.283 19.314  1.00 87.49  ? 22  ILE   I CB  1 
ATOM   14906 C  CG1 . ILE   I  9  23  ? 71.876  -127.797 19.562  1.00 85.59  ? 22  ILE   I CG1 1 
ATOM   14907 C  CG2 . ILE   I  9  23  ? 73.310  -126.091 18.369  1.00 89.60  ? 22  ILE   I CG2 1 
ATOM   14908 C  CD1 . ILE   I  9  23  ? 71.044  -126.904 20.452  1.00 85.01  ? 22  ILE   I CD1 1 
ATOM   14909 N  N   . ALA   I  9  24  ? 73.216  -130.165 17.445  1.00 91.54  ? 23  ALA   I N   1 
ATOM   14910 C  CA  . ALA   I  9  24  ? 72.828  -130.920 16.232  1.00 91.58  ? 23  ALA   I CA  1 
ATOM   14911 C  C   . ALA   I  9  24  ? 71.368  -131.363 16.353  1.00 88.89  ? 23  ALA   I C   1 
ATOM   14912 O  O   . ALA   I  9  24  ? 70.875  -131.491 17.492  1.00 84.08  ? 23  ALA   I O   1 
ATOM   14913 C  CB  . ALA   I  9  24  ? 73.754  -132.097 16.045  1.00 92.79  ? 23  ALA   I CB  1 
ATOM   14914 N  N   . CYS   I  9  25  ? 70.706  -131.570 15.213  1.00 90.57  ? 24  CYS   I N   1 
ATOM   14915 C  CA  . CYS   I  9  25  ? 69.304  -132.055 15.124  1.00 93.91  ? 24  CYS   I CA  1 
ATOM   14916 C  C   . CYS   I  9  25  ? 69.093  -132.804 13.806  1.00 96.80  ? 24  CYS   I C   1 
ATOM   14917 O  O   . CYS   I  9  25  ? 69.841  -132.535 12.845  1.00 100.36 ? 24  CYS   I O   1 
ATOM   14918 C  CB  . CYS   I  9  25  ? 68.313  -130.902 15.207  1.00 94.23  ? 24  CYS   I CB  1 
ATOM   14919 S  SG  . CYS   I  9  25  ? 68.157  -129.976 13.656  1.00 97.78  ? 24  CYS   I SG  1 
ATOM   14920 N  N   . ASP   I  9  26  ? 68.105  -133.702 13.778  1.00 100.73 ? 25  ASP   I N   1 
ATOM   14921 C  CA  . ASP   I  9  26  ? 67.638  -134.402 12.552  1.00 103.79 ? 25  ASP   I CA  1 
ATOM   14922 C  C   . ASP   I  9  26  ? 66.717  -133.449 11.783  1.00 103.30 ? 25  ASP   I C   1 
ATOM   14923 O  O   . ASP   I  9  26  ? 66.479  -132.330 12.286  1.00 106.59 ? 25  ASP   I O   1 
ATOM   14924 C  CB  . ASP   I  9  26  ? 66.947  -135.723 12.900  1.00 104.17 ? 25  ASP   I CB  1 
ATOM   14925 C  CG  . ASP   I  9  26  ? 65.546  -135.551 13.460  1.00 104.11 ? 25  ASP   I CG  1 
ATOM   14926 O  OD1 . ASP   I  9  26  ? 65.333  -134.589 14.227  1.00 103.48 ? 25  ASP   I OD1 1 
ATOM   14927 O  OD2 . ASP   I  9  26  ? 64.677  -136.376 13.120  1.00 107.96 ? 25  ASP   I OD2 1 
ATOM   14928 N  N   . LEU   I  9  27  ? 66.212  -133.874 10.621  1.00 101.69 ? 26  LEU   I N   1 
ATOM   14929 C  CA  . LEU   I  9  27  ? 65.371  -133.029 9.730   1.00 100.50 ? 26  LEU   I CA  1 
ATOM   14930 C  C   . LEU   I  9  27  ? 63.965  -133.618 9.557   1.00 97.05  ? 26  LEU   I C   1 
ATOM   14931 O  O   . LEU   I  9  27  ? 63.146  -132.956 8.888   1.00 93.11  ? 26  LEU   I O   1 
ATOM   14932 C  CB  . LEU   I  9  27  ? 66.068  -132.899 8.372   1.00 106.08 ? 26  LEU   I CB  1 
ATOM   14933 C  CG  . LEU   I  9  27  ? 67.358  -132.080 8.352   1.00 107.33 ? 26  LEU   I CG  1 
ATOM   14934 C  CD1 . LEU   I  9  27  ? 67.898  -131.983 6.933   1.00 114.16 ? 26  LEU   I CD1 1 
ATOM   14935 C  CD2 . LEU   I  9  27  ? 67.144  -130.690 8.928   1.00 102.26 ? 26  LEU   I CD2 1 
ATOM   14936 N  N   . ARG   I  9  28  ? 63.680  -134.796 10.124  1.00 97.41  ? 27  ARG   I N   1 
ATOM   14937 C  CA  . ARG   I  9  28  ? 62.390  -135.500 9.889   1.00 95.67  ? 27  ARG   I CA  1 
ATOM   14938 C  C   . ARG   I  9  28  ? 61.254  -134.707 10.542  1.00 90.06  ? 27  ARG   I C   1 
ATOM   14939 O  O   . ARG   I  9  28  ? 61.444  -134.193 11.659  1.00 87.19  ? 27  ARG   I O   1 
ATOM   14940 C  CB  . ARG   I  9  28  ? 62.403  -136.940 10.417  1.00 97.67  ? 27  ARG   I CB  1 
ATOM   14941 C  CG  . ARG   I  9  28  ? 61.211  -137.767 9.950   1.00 101.06 ? 27  ARG   I CG  1 
ATOM   14942 C  CD  . ARG   I  9  28  ? 61.322  -139.244 10.273  1.00 105.03 ? 27  ARG   I CD  1 
ATOM   14943 N  NE  . ARG   I  9  28  ? 60.117  -139.984 9.909   1.00 110.74 ? 27  ARG   I NE  1 
ATOM   14944 C  CZ  . ARG   I  9  28  ? 58.998  -140.047 10.635  1.00 110.55 ? 27  ARG   I CZ  1 
ATOM   14945 N  NH1 . ARG   I  9  28  ? 58.897  -139.404 11.788  1.00 111.85 ? 27  ARG   I NH1 1 
ATOM   14946 N  NH2 . ARG   I  9  28  ? 57.973  -140.759 10.199  1.00 113.64 ? 27  ARG   I NH2 1 
ATOM   14947 N  N   . LEU   I  9  29  ? 60.136  -134.581 9.829   1.00 87.51  ? 28  LEU   I N   1 
ATOM   14948 C  CA  . LEU   I  9  29  ? 58.788  -134.354 10.407  1.00 88.40  ? 28  LEU   I CA  1 
ATOM   14949 C  C   . LEU   I  9  29  ? 57.832  -135.360 9.764   1.00 89.07  ? 28  LEU   I C   1 
ATOM   14950 O  O   . LEU   I  9  29  ? 57.719  -135.355 8.522   1.00 89.92  ? 28  LEU   I O   1 
ATOM   14951 C  CB  . LEU   I  9  29  ? 58.328  -132.918 10.146  1.00 88.24  ? 28  LEU   I CB  1 
ATOM   14952 C  CG  . LEU   I  9  29  ? 56.951  -132.565 10.712  1.00 88.33  ? 28  LEU   I CG  1 
ATOM   14953 C  CD1 . LEU   I  9  29  ? 56.931  -131.143 11.247  1.00 87.43  ? 28  LEU   I CD1 1 
ATOM   14954 C  CD2 . LEU   I  9  29  ? 55.852  -132.754 9.674   1.00 88.87  ? 28  LEU   I CD2 1 
ATOM   14955 N  N   . GLY   I  9  30  ? 57.194  -136.199 10.583  1.00 88.86  ? 29  GLY   I N   1 
ATOM   14956 C  CA  . GLY   I  9  30  ? 56.251  -137.234 10.128  1.00 89.83  ? 29  GLY   I CA  1 
ATOM   14957 C  C   . GLY   I  9  30  ? 54.892  -137.065 10.771  1.00 89.28  ? 29  GLY   I C   1 
ATOM   14958 O  O   . GLY   I  9  30  ? 54.730  -136.142 11.586  1.00 87.08  ? 29  GLY   I O   1 
ATOM   14959 N  N   . SER   I  9  31  ? 53.943  -137.913 10.379  1.00 91.51  ? 30  SER   I N   1 
ATOM   14960 C  CA  . SER   I  9  31  ? 52.661  -138.159 11.081  1.00 92.45  ? 30  SER   I CA  1 
ATOM   14961 C  C   . SER   I  9  31  ? 52.586  -139.656 11.406  1.00 95.55  ? 30  SER   I C   1 
ATOM   14962 O  O   . SER   I  9  31  ? 52.187  -140.445 10.520  1.00 97.50  ? 30  SER   I O   1 
ATOM   14963 C  CB  . SER   I  9  31  ? 51.499  -137.677 10.258  1.00 93.27  ? 30  SER   I CB  1 
ATOM   14964 O  OG  . SER   I  9  31  ? 50.313  -137.651 11.034  1.00 93.36  ? 30  SER   I OG  1 
ATOM   14965 N  N   . GLN   I  9  32  ? 53.007  -140.021 12.622  1.00 98.16  ? 31  GLN   I N   1 
ATOM   14966 C  CA  . GLN   I  9  32  ? 53.248  -141.420 13.062  1.00 100.40 ? 31  GLN   I CA  1 
ATOM   14967 C  C   . GLN   I  9  32  ? 54.145  -142.093 12.012  1.00 100.40 ? 31  GLN   I C   1 
ATOM   14968 O  O   . GLN   I  9  32  ? 55.312  -141.661 11.897  1.00 98.83  ? 31  GLN   I O   1 
ATOM   14969 C  CB  . GLN   I  9  32  ? 51.911  -142.111 13.346  1.00 102.27 ? 31  GLN   I CB  1 
ATOM   14970 C  CG  . GLN   I  9  32  ? 51.315  -141.708 14.690  1.00 102.79 ? 31  GLN   I CG  1 
ATOM   14971 C  CD  . GLN   I  9  32  ? 49.894  -142.176 14.885  1.00 107.15 ? 31  GLN   I CD  1 
ATOM   14972 O  OE1 . GLN   I  9  32  ? 49.589  -142.903 15.828  1.00 114.97 ? 31  GLN   I OE1 1 
ATOM   14973 N  NE2 . GLN   I  9  32  ? 49.006  -141.761 13.996  1.00 109.38 ? 31  GLN   I NE2 1 
ATOM   14974 N  N   . SER   I  9  33  ? 53.622  -143.059 11.246  1.00 104.32 ? 32  SER   I N   1 
ATOM   14975 C  CA  . SER   I  9  33  ? 54.411  -143.926 10.328  1.00 101.20 ? 32  SER   I CA  1 
ATOM   14976 C  C   . SER   I  9  33  ? 54.830  -143.141 9.078   1.00 101.85 ? 32  SER   I C   1 
ATOM   14977 O  O   . SER   I  9  33  ? 55.959  -143.366 8.589   1.00 100.21 ? 32  SER   I O   1 
ATOM   14978 C  CB  . SER   I  9  33  ? 53.644  -145.173 9.962   1.00 102.93 ? 32  SER   I CB  1 
ATOM   14979 O  OG  . SER   I  9  33  ? 52.613  -144.877 9.033   1.00 99.29  ? 32  SER   I OG  1 
ATOM   14980 N  N   . LEU   I  9  34  ? 53.952  -142.260 8.587   1.00 101.66 ? 33  LEU   I N   1 
ATOM   14981 C  CA  . LEU   I  9  34  ? 54.147  -141.463 7.345   1.00 100.34 ? 33  LEU   I CA  1 
ATOM   14982 C  C   . LEU   I  9  34  ? 55.188  -140.369 7.594   1.00 97.70  ? 33  LEU   I C   1 
ATOM   14983 O  O   . LEU   I  9  34  ? 54.936  -139.520 8.463   1.00 96.79  ? 33  LEU   I O   1 
ATOM   14984 C  CB  . LEU   I  9  34  ? 52.806  -140.844 6.931   1.00 100.67 ? 33  LEU   I CB  1 
ATOM   14985 C  CG  . LEU   I  9  34  ? 52.855  -139.829 5.788   1.00 99.32  ? 33  LEU   I CG  1 
ATOM   14986 C  CD1 . LEU   I  9  34  ? 53.280  -140.484 4.484   1.00 100.52 ? 33  LEU   I CD1 1 
ATOM   14987 C  CD2 . LEU   I  9  34  ? 51.507  -139.149 5.620   1.00 99.65  ? 33  LEU   I CD2 1 
ATOM   14988 N  N   . GLY   I  9  35  ? 56.301  -140.394 6.853   1.00 99.82  ? 34  GLY   I N   1 
ATOM   14989 C  CA  . GLY   I  9  35  ? 57.224  -139.249 6.713   1.00 98.38  ? 34  GLY   I CA  1 
ATOM   14990 C  C   . GLY   I  9  35  ? 56.609  -138.178 5.822   1.00 99.98  ? 34  GLY   I C   1 
ATOM   14991 O  O   . GLY   I  9  35  ? 56.073  -138.547 4.759   1.00 98.21  ? 34  GLY   I O   1 
ATOM   14992 N  N   . VAL   I  9  36  ? 56.656  -136.905 6.238   1.00 98.35  ? 35  VAL   I N   1 
ATOM   14993 C  CA  . VAL   I  9  36  ? 55.964  -135.769 5.548   1.00 99.97  ? 35  VAL   I CA  1 
ATOM   14994 C  C   . VAL   I  9  36  ? 56.988  -134.750 5.025   1.00 100.17 ? 35  VAL   I C   1 
ATOM   14995 O  O   . VAL   I  9  36  ? 56.834  -134.317 3.859   1.00 96.69  ? 35  VAL   I O   1 
ATOM   14996 C  CB  . VAL   I  9  36  ? 54.929  -135.085 6.464   1.00 96.27  ? 35  VAL   I CB  1 
ATOM   14997 C  CG1 . VAL   I  9  36  ? 54.319  -133.864 5.797   1.00 96.77  ? 35  VAL   I CG1 1 
ATOM   14998 C  CG2 . VAL   I  9  36  ? 53.834  -136.047 6.901   1.00 97.14  ? 35  VAL   I CG2 1 
ATOM   14999 N  N   . SER   I  9  37  ? 57.952  -134.342 5.860   1.00 99.59  ? 36  SER   I N   1 
ATOM   15000 C  CA  . SER   I  9  37  ? 58.998  -133.343 5.513   1.00 99.90  ? 36  SER   I CA  1 
ATOM   15001 C  C   . SER   I  9  37  ? 60.391  -133.811 5.947   1.00 101.49 ? 36  SER   I C   1 
ATOM   15002 O  O   . SER   I  9  37  ? 60.533  -134.277 7.096   1.00 96.31  ? 36  SER   I O   1 
ATOM   15003 C  CB  . SER   I  9  37  ? 58.691  -132.011 6.119   1.00 97.20  ? 36  SER   I CB  1 
ATOM   15004 O  OG  . SER   I  9  37  ? 59.720  -131.080 5.819   1.00 97.90  ? 36  SER   I OG  1 
ATOM   15005 N  N   . ASN   I  9  38  ? 61.378  -133.617 5.065   1.00 107.55 ? 37  ASN   I N   1 
ATOM   15006 C  CA  . ASN   I  9  38  ? 62.822  -133.911 5.287   1.00 113.42 ? 37  ASN   I CA  1 
ATOM   15007 C  C   . ASN   I  9  38  ? 63.603  -132.590 5.254   1.00 114.15 ? 37  ASN   I C   1 
ATOM   15008 O  O   . ASN   I  9  38  ? 64.788  -132.606 4.859   1.00 118.94 ? 37  ASN   I O   1 
ATOM   15009 C  CB  . ASN   I  9  38  ? 63.377  -134.937 4.287   1.00 124.95 ? 37  ASN   I CB  1 
ATOM   15010 C  CG  . ASN   I  9  38  ? 62.632  -134.995 2.967   1.00 129.79 ? 37  ASN   I CG  1 
ATOM   15011 O  OD1 . ASN   I  9  38  ? 62.239  -136.073 2.522   1.00 142.93 ? 37  ASN   I OD1 1 
ATOM   15012 N  ND2 . ASN   I  9  38  ? 62.437  -133.853 2.328   1.00 126.74 ? 37  ASN   I ND2 1 
ATOM   15013 N  N   . LYS   I  9  39  ? 62.957  -131.491 5.657   1.00 108.57 ? 38  LYS   I N   1 
ATOM   15014 C  CA  . LYS   I  9  39  ? 63.539  -130.123 5.669   1.00 109.34 ? 38  LYS   I CA  1 
ATOM   15015 C  C   . LYS   I  9  39  ? 63.217  -129.400 6.984   1.00 104.23 ? 38  LYS   I C   1 
ATOM   15016 O  O   . LYS   I  9  39  ? 63.531  -128.199 7.077   1.00 104.47 ? 38  LYS   I O   1 
ATOM   15017 C  CB  . LYS   I  9  39  ? 62.982  -129.319 4.491   1.00 111.16 ? 38  LYS   I CB  1 
ATOM   15018 C  CG  . LYS   I  9  39  ? 63.548  -129.686 3.127   1.00 116.79 ? 38  LYS   I CG  1 
ATOM   15019 C  CD  . LYS   I  9  39  ? 62.572  -129.438 1.997   1.00 118.19 ? 38  LYS   I CD  1 
ATOM   15020 C  CE  . LYS   I  9  39  ? 63.246  -129.185 0.666   1.00 122.86 ? 38  LYS   I CE  1 
ATOM   15021 N  NZ  . LYS   I  9  39  ? 64.191  -130.270 0.311   1.00 125.90 ? 38  LYS   I NZ  1 
ATOM   15022 N  N   . PHE   I  9  40  ? 62.636  -130.092 7.969   1.00 101.67 ? 39  PHE   I N   1 
ATOM   15023 C  CA  . PHE   I  9  40  ? 62.133  -129.481 9.227   1.00 98.48  ? 39  PHE   I CA  1 
ATOM   15024 C  C   . PHE   I  9  40  ? 63.278  -129.356 10.238  1.00 99.47  ? 39  PHE   I C   1 
ATOM   15025 O  O   . PHE   I  9  40  ? 63.528  -130.308 11.003  1.00 99.20  ? 39  PHE   I O   1 
ATOM   15026 C  CB  . PHE   I  9  40  ? 60.969  -130.294 9.793   1.00 96.78  ? 39  PHE   I CB  1 
ATOM   15027 C  CG  . PHE   I  9  40  ? 60.195  -129.577 10.869  1.00 93.16  ? 39  PHE   I CG  1 
ATOM   15028 C  CD1 . PHE   I  9  40  ? 59.261  -128.609 10.538  1.00 92.26  ? 39  PHE   I CD1 1 
ATOM   15029 C  CD2 . PHE   I  9  40  ? 60.406  -129.862 12.210  1.00 92.99  ? 39  PHE   I CD2 1 
ATOM   15030 C  CE1 . PHE   I  9  40  ? 58.548  -127.945 11.524  1.00 91.13  ? 39  PHE   I CE1 1 
ATOM   15031 C  CE2 . PHE   I  9  40  ? 59.691  -129.198 13.195  1.00 90.72  ? 39  PHE   I CE2 1 
ATOM   15032 C  CZ  . PHE   I  9  40  ? 58.763  -128.241 12.850  1.00 89.94  ? 39  PHE   I CZ  1 
ATOM   15033 N  N   . GLU   I  9  41  ? 63.948  -128.201 10.245  1.00 99.84  ? 40  GLU   I N   1 
ATOM   15034 C  CA  . GLU   I  9  41  ? 65.059  -127.890 11.184  1.00 100.44 ? 40  GLU   I CA  1 
ATOM   15035 C  C   . GLU   I  9  41  ? 64.473  -127.559 12.560  1.00 99.87  ? 40  GLU   I C   1 
ATOM   15036 O  O   . GLU   I  9  41  ? 63.441  -126.858 12.614  1.00 97.16  ? 40  GLU   I O   1 
ATOM   15037 C  CB  . GLU   I  9  41  ? 65.916  -126.740 10.656  1.00 102.63 ? 40  GLU   I CB  1 
ATOM   15038 C  CG  . GLU   I  9  41  ? 66.613  -127.070 9.349   1.00 105.59 ? 40  GLU   I CG  1 
ATOM   15039 C  CD  . GLU   I  9  41  ? 67.756  -126.146 8.965   1.00 107.08 ? 40  GLU   I CD  1 
ATOM   15040 O  OE1 . GLU   I  9  41  ? 68.231  -126.250 7.816   1.00 107.42 ? 40  GLU   I OE1 1 
ATOM   15041 O  OE2 . GLU   I  9  41  ? 68.179  -125.334 9.815   1.00 108.72 ? 40  GLU   I OE2 1 
ATOM   15042 N  N   . LYS   I  9  42  ? 65.119  -128.054 13.620  1.00 99.96  ? 41  LYS   I N   1 
ATOM   15043 C  CA  . LYS   I  9  42  ? 64.639  -127.972 15.024  1.00 96.07  ? 41  LYS   I CA  1 
ATOM   15044 C  C   . LYS   I  9  42  ? 65.559  -127.065 15.847  1.00 94.23  ? 41  LYS   I C   1 
ATOM   15045 O  O   . LYS   I  9  42  ? 65.307  -126.939 17.060  1.00 89.87  ? 41  LYS   I O   1 
ATOM   15046 C  CB  . LYS   I  9  42  ? 64.560  -129.383 15.615  1.00 97.59  ? 41  LYS   I CB  1 
ATOM   15047 C  CG  . LYS   I  9  42  ? 63.460  -130.245 15.013  1.00 99.23  ? 41  LYS   I CG  1 
ATOM   15048 C  CD  . LYS   I  9  42  ? 63.599  -131.723 15.281  1.00 100.30 ? 41  LYS   I CD  1 
ATOM   15049 C  CE  . LYS   I  9  42  ? 62.720  -132.546 14.365  1.00 100.96 ? 41  LYS   I CE  1 
ATOM   15050 N  NZ  . LYS   I  9  42  ? 63.309  -132.679 13.012  1.00 103.64 ? 41  LYS   I NZ  1 
ATOM   15051 N  N   . ILE   I  9  43  ? 66.567  -126.452 15.217  1.00 91.77  ? 42  ILE   I N   1 
ATOM   15052 C  CA  . ILE   I  9  43  ? 67.509  -125.502 15.881  1.00 92.01  ? 42  ILE   I CA  1 
ATOM   15053 C  C   . ILE   I  9  43  ? 67.253  -124.088 15.351  1.00 91.45  ? 42  ILE   I C   1 
ATOM   15054 O  O   . ILE   I  9  43  ? 67.212  -123.902 14.119  1.00 84.49  ? 42  ILE   I O   1 
ATOM   15055 C  CB  . ILE   I  9  43  ? 68.976  -125.936 15.697  1.00 94.07  ? 42  ILE   I CB  1 
ATOM   15056 C  CG1 . ILE   I  9  43  ? 69.241  -127.280 16.379  1.00 94.60  ? 42  ILE   I CG1 1 
ATOM   15057 C  CG2 . ILE   I  9  43  ? 69.925  -124.856 16.200  1.00 94.26  ? 42  ILE   I CG2 1 
ATOM   15058 C  CD1 . ILE   I  9  43  ? 70.549  -127.923 15.988  1.00 96.32  ? 42  ILE   I CD1 1 
ATOM   15059 N  N   . PHE   I  9  44  ? 67.100  -123.140 16.279  1.00 91.16  ? 43  PHE   I N   1 
ATOM   15060 C  CA  . PHE   I  9  44  ? 66.879  -121.692 16.037  1.00 93.55  ? 43  PHE   I CA  1 
ATOM   15061 C  C   . PHE   I  9  44  ? 67.909  -120.916 16.863  1.00 94.99  ? 43  PHE   I C   1 
ATOM   15062 O  O   . PHE   I  9  44  ? 68.475  -121.512 17.801  1.00 92.53  ? 43  PHE   I O   1 
ATOM   15063 C  CB  . PHE   I  9  44  ? 65.443  -121.317 16.411  1.00 93.27  ? 43  PHE   I CB  1 
ATOM   15064 C  CG  . PHE   I  9  44  ? 64.399  -122.298 15.935  1.00 93.21  ? 43  PHE   I CG  1 
ATOM   15065 C  CD1 . PHE   I  9  44  ? 63.803  -122.154 14.691  1.00 92.16  ? 43  PHE   I CD1 1 
ATOM   15066 C  CD2 . PHE   I  9  44  ? 64.021  -123.373 16.725  1.00 92.27  ? 43  PHE   I CD2 1 
ATOM   15067 C  CE1 . PHE   I  9  44  ? 62.844  -123.053 14.252  1.00 91.57  ? 43  PHE   I CE1 1 
ATOM   15068 C  CE2 . PHE   I  9  44  ? 63.065  -124.275 16.283  1.00 93.97  ? 43  PHE   I CE2 1 
ATOM   15069 C  CZ  . PHE   I  9  44  ? 62.476  -124.112 15.049  1.00 91.96  ? 43  PHE   I CZ  1 
ATOM   15070 N  N   . HIS   I  9  45  ? 68.160  -119.647 16.529  1.00 96.28  ? 44  HIS   I N   1 
ATOM   15071 C  CA  . HIS   I  9  45  ? 69.061  -118.765 17.318  1.00 96.52  ? 44  HIS   I CA  1 
ATOM   15072 C  C   . HIS   I  9  45  ? 68.487  -117.349 17.430  1.00 96.84  ? 44  HIS   I C   1 
ATOM   15073 O  O   . HIS   I  9  45  ? 67.821  -116.885 16.481  1.00 95.20  ? 44  HIS   I O   1 
ATOM   15074 C  CB  . HIS   I  9  45  ? 70.488  -118.785 16.754  1.00 100.99 ? 44  HIS   I CB  1 
ATOM   15075 C  CG  . HIS   I  9  45  ? 70.608  -118.267 15.362  1.00 105.96 ? 44  HIS   I CG  1 
ATOM   15076 N  ND1 . HIS   I  9  45  ? 70.881  -116.941 15.093  1.00 107.83 ? 44  HIS   I ND1 1 
ATOM   15077 C  CD2 . HIS   I  9  45  ? 70.514  -118.890 14.167  1.00 107.42 ? 44  HIS   I CD2 1 
ATOM   15078 C  CE1 . HIS   I  9  45  ? 70.941  -116.765 13.789  1.00 112.34 ? 44  HIS   I CE1 1 
ATOM   15079 N  NE2 . HIS   I  9  45  ? 70.721  -117.947 13.199  1.00 111.45 ? 44  HIS   I NE2 1 
ATOM   15080 N  N   . TYR   I  9  46  ? 68.754  -116.714 18.575  1.00 93.69  ? 45  TYR   I N   1 
ATOM   15081 C  CA  . TYR   I  9  46  ? 68.356  -115.331 18.941  1.00 93.15  ? 45  TYR   I CA  1 
ATOM   15082 C  C   . TYR   I  9  46  ? 69.624  -114.586 19.368  1.00 92.06  ? 45  TYR   I C   1 
ATOM   15083 O  O   . TYR   I  9  46  ? 70.065  -114.721 20.531  1.00 88.20  ? 45  TYR   I O   1 
ATOM   15084 C  CB  . TYR   I  9  46  ? 67.280  -115.379 20.027  1.00 90.91  ? 45  TYR   I CB  1 
ATOM   15085 C  CG  . TYR   I  9  46  ? 66.272  -116.481 19.824  1.00 91.05  ? 45  TYR   I CG  1 
ATOM   15086 C  CD1 . TYR   I  9  46  ? 65.227  -116.336 18.927  1.00 90.64  ? 45  TYR   I CD1 1 
ATOM   15087 C  CD2 . TYR   I  9  46  ? 66.385  -117.685 20.500  1.00 91.35  ? 45  TYR   I CD2 1 
ATOM   15088 C  CE1 . TYR   I  9  46  ? 64.305  -117.349 18.723  1.00 91.10  ? 45  TYR   I CE1 1 
ATOM   15089 C  CE2 . TYR   I  9  46  ? 65.470  -118.708 20.310  1.00 92.28  ? 45  TYR   I CE2 1 
ATOM   15090 C  CZ  . TYR   I  9  46  ? 64.426  -118.539 19.418  1.00 91.12  ? 45  TYR   I CZ  1 
ATOM   15091 O  OH  . TYR   I  9  46  ? 63.523  -119.542 19.227  1.00 91.66  ? 45  TYR   I OH  1 
ATOM   15092 N  N   . GLY   I  9  47  ? 70.213  -113.842 18.431  1.00 94.77  ? 46  GLY   I N   1 
ATOM   15093 C  CA  . GLY   I  9  47  ? 71.608  -113.378 18.528  1.00 98.77  ? 46  GLY   I CA  1 
ATOM   15094 C  C   . GLY   I  9  47  ? 72.553  -114.566 18.511  1.00 97.83  ? 46  GLY   I C   1 
ATOM   15095 O  O   . GLY   I  9  47  ? 72.474  -115.363 17.556  1.00 97.34  ? 46  GLY   I O   1 
ATOM   15096 N  N   . HIS   I  9  48  ? 73.382  -114.708 19.550  1.00 99.05  ? 47  HIS   I N   1 
ATOM   15097 C  CA  . HIS   I  9  48  ? 74.434  -115.756 19.668  1.00 100.33 ? 47  HIS   I CA  1 
ATOM   15098 C  C   . HIS   I  9  48  ? 73.962  -116.914 20.556  1.00 99.15  ? 47  HIS   I C   1 
ATOM   15099 O  O   . HIS   I  9  48  ? 74.784  -117.818 20.816  1.00 98.85  ? 47  HIS   I O   1 
ATOM   15100 C  CB  . HIS   I  9  48  ? 75.730  -115.155 20.223  1.00 101.52 ? 47  HIS   I CB  1 
ATOM   15101 C  CG  . HIS   I  9  48  ? 75.597  -114.663 21.624  1.00 103.69 ? 47  HIS   I CG  1 
ATOM   15102 N  ND1 . HIS   I  9  48  ? 75.205  -113.371 21.917  1.00 103.48 ? 47  HIS   I ND1 1 
ATOM   15103 C  CD2 . HIS   I  9  48  ? 75.778  -115.284 22.809  1.00 104.17 ? 47  HIS   I CD2 1 
ATOM   15104 C  CE1 . HIS   I  9  48  ? 75.162  -113.215 23.224  1.00 103.76 ? 47  HIS   I CE1 1 
ATOM   15105 N  NE2 . HIS   I  9  48  ? 75.509  -114.374 23.794  1.00 103.62 ? 47  HIS   I NE2 1 
ATOM   15106 N  N   . VAL   I  9  49  ? 72.709  -116.878 21.023  1.00 101.10 ? 48  VAL   I N   1 
ATOM   15107 C  CA  . VAL   I  9  49  ? 72.095  -117.947 21.867  1.00 101.12 ? 48  VAL   I CA  1 
ATOM   15108 C  C   . VAL   I  9  49  ? 71.270  -118.870 20.964  1.00 102.12 ? 48  VAL   I C   1 
ATOM   15109 O  O   . VAL   I  9  49  ? 70.297  -118.377 20.356  1.00 107.63 ? 48  VAL   I O   1 
ATOM   15110 C  CB  . VAL   I  9  49  ? 71.231  -117.349 22.993  1.00 101.65 ? 48  VAL   I CB  1 
ATOM   15111 C  CG1 . VAL   I  9  49  ? 70.598  -118.431 23.857  1.00 100.55 ? 48  VAL   I CG1 1 
ATOM   15112 C  CG2 . VAL   I  9  49  ? 72.028  -116.378 23.849  1.00 103.77 ? 48  VAL   I CG2 1 
ATOM   15113 N  N   . PHE   I  9  50  ? 71.641  -120.155 20.899  1.00 99.63  ? 49  PHE   I N   1 
ATOM   15114 C  CA  . PHE   I  9  50  ? 70.983  -121.199 20.069  1.00 95.57  ? 49  PHE   I CA  1 
ATOM   15115 C  C   . PHE   I  9  50  ? 70.013  -122.013 20.931  1.00 92.45  ? 49  PHE   I C   1 
ATOM   15116 O  O   . PHE   I  9  50  ? 70.364  -122.367 22.075  1.00 91.55  ? 49  PHE   I O   1 
ATOM   15117 C  CB  . PHE   I  9  50  ? 72.027  -122.099 19.404  1.00 96.52  ? 49  PHE   I CB  1 
ATOM   15118 C  CG  . PHE   I  9  50  ? 72.725  -121.464 18.231  1.00 99.49  ? 49  PHE   I CG  1 
ATOM   15119 C  CD1 . PHE   I  9  50  ? 73.715  -120.512 18.424  1.00 100.40 ? 49  PHE   I CD1 1 
ATOM   15120 C  CD2 . PHE   I  9  50  ? 72.384  -121.809 16.932  1.00 100.86 ? 49  PHE   I CD2 1 
ATOM   15121 C  CE1 . PHE   I  9  50  ? 74.354  -119.923 17.343  1.00 101.54 ? 49  PHE   I CE1 1 
ATOM   15122 C  CE2 . PHE   I  9  50  ? 73.023  -121.219 15.852  1.00 103.62 ? 49  PHE   I CE2 1 
ATOM   15123 C  CZ  . PHE   I  9  50  ? 74.007  -120.277 16.059  1.00 103.38 ? 49  PHE   I CZ  1 
ATOM   15124 N  N   . LEU   I  9  51  ? 68.826  -122.291 20.384  1.00 89.34  ? 50  LEU   I N   1 
ATOM   15125 C  CA  . LEU   I  9  51  ? 67.768  -123.122 21.015  1.00 89.59  ? 50  LEU   I CA  1 
ATOM   15126 C  C   . LEU   I  9  51  ? 67.345  -124.219 20.036  1.00 89.63  ? 50  LEU   I C   1 
ATOM   15127 O  O   . LEU   I  9  51  ? 66.925  -123.874 18.915  1.00 88.77  ? 50  LEU   I O   1 
ATOM   15128 C  CB  . LEU   I  9  51  ? 66.575  -122.232 21.379  1.00 89.31  ? 50  LEU   I CB  1 
ATOM   15129 C  CG  . LEU   I  9  51  ? 65.362  -122.959 21.960  1.00 89.64  ? 50  LEU   I CG  1 
ATOM   15130 C  CD1 . LEU   I  9  51  ? 65.681  -123.543 23.328  1.00 91.01  ? 50  LEU   I CD1 1 
ATOM   15131 C  CD2 . LEU   I  9  51  ? 64.159  -122.032 22.045  1.00 89.63  ? 50  LEU   I CD2 1 
ATOM   15132 N  N   . GLY   I  9  52  ? 67.459  -125.484 20.454  1.00 90.92  ? 51  GLY   I N   1 
ATOM   15133 C  CA  . GLY   I  9  52  ? 66.889  -126.654 19.758  1.00 90.82  ? 51  GLY   I CA  1 
ATOM   15134 C  C   . GLY   I  9  52  ? 65.648  -127.145 20.482  1.00 89.53  ? 51  GLY   I C   1 
ATOM   15135 O  O   . GLY   I  9  52  ? 65.679  -127.163 21.723  1.00 93.15  ? 51  GLY   I O   1 
ATOM   15136 N  N   . ILE   I  9  53  ? 64.587  -127.500 19.751  1.00 89.37  ? 52  ILE   I N   1 
ATOM   15137 C  CA  . ILE   I  9  53  ? 63.289  -127.951 20.340  1.00 90.30  ? 52  ILE   I CA  1 
ATOM   15138 C  C   . ILE   I  9  53  ? 62.832  -129.233 19.632  1.00 89.41  ? 52  ILE   I C   1 
ATOM   15139 O  O   . ILE   I  9  53  ? 62.643  -129.192 18.399  1.00 93.16  ? 52  ILE   I O   1 
ATOM   15140 C  CB  . ILE   I  9  53  ? 62.212  -126.847 20.261  1.00 91.26  ? 52  ILE   I CB  1 
ATOM   15141 C  CG1 . ILE   I  9  53  ? 62.764  -125.458 20.595  1.00 93.32  ? 52  ILE   I CG1 1 
ATOM   15142 C  CG2 . ILE   I  9  53  ? 61.027  -127.204 21.148  1.00 90.41  ? 52  ILE   I CG2 1 
ATOM   15143 C  CD1 . ILE   I  9  53  ? 61.802  -124.324 20.303  1.00 95.77  ? 52  ILE   I CD1 1 
ATOM   15144 N  N   . THR   I  9  54  ? 62.656  -130.318 20.396  1.00 86.37  ? 53  THR   I N   1 
ATOM   15145 C  CA  . THR   I  9  54  ? 62.021  -131.591 19.959  1.00 84.35  ? 53  THR   I CA  1 
ATOM   15146 C  C   . THR   I  9  54  ? 60.598  -131.666 20.519  1.00 80.81  ? 53  THR   I C   1 
ATOM   15147 O  O   . THR   I  9  54  ? 60.272  -130.868 21.412  1.00 78.62  ? 53  THR   I O   1 
ATOM   15148 C  CB  . THR   I  9  54  ? 62.814  -132.811 20.434  1.00 82.89  ? 53  THR   I CB  1 
ATOM   15149 O  OG1 . THR   I  9  54  ? 62.854  -132.767 21.861  1.00 82.75  ? 53  THR   I OG1 1 
ATOM   15150 C  CG2 . THR   I  9  54  ? 64.217  -132.859 19.872  1.00 83.99  ? 53  THR   I CG2 1 
ATOM   15151 N  N   . GLY   I  9  55  ? 59.802  -132.613 20.026  1.00 81.42  ? 54  GLY   I N   1 
ATOM   15152 C  CA  . GLY   I  9  55  ? 58.412  -132.837 20.462  1.00 83.44  ? 54  GLY   I CA  1 
ATOM   15153 C  C   . GLY   I  9  55  ? 57.425  -132.421 19.388  1.00 85.19  ? 54  GLY   I C   1 
ATOM   15154 O  O   . GLY   I  9  55  ? 57.817  -132.399 18.200  1.00 85.91  ? 54  GLY   I O   1 
ATOM   15155 N  N   . LEU   I  9  56  ? 56.197  -132.089 19.798  1.00 83.57  ? 55  LEU   I N   1 
ATOM   15156 C  CA  . LEU   I  9  56  ? 55.054  -131.777 18.898  1.00 84.33  ? 55  LEU   I CA  1 
ATOM   15157 C  C   . LEU   I  9  56  ? 55.416  -130.552 18.050  1.00 86.58  ? 55  LEU   I C   1 
ATOM   15158 O  O   . LEU   I  9  56  ? 55.699  -129.492 18.637  1.00 89.98  ? 55  LEU   I O   1 
ATOM   15159 C  CB  . LEU   I  9  56  ? 53.805  -131.542 19.755  1.00 80.70  ? 55  LEU   I CB  1 
ATOM   15160 C  CG  . LEU   I  9  56  ? 52.475  -131.492 19.006  1.00 82.09  ? 55  LEU   I CG  1 
ATOM   15161 C  CD1 . LEU   I  9  56  ? 52.158  -132.819 18.338  1.00 84.63  ? 55  LEU   I CD1 1 
ATOM   15162 C  CD2 . LEU   I  9  56  ? 51.347  -131.098 19.946  1.00 82.29  ? 55  LEU   I CD2 1 
ATOM   15163 N  N   . ALA   I  9  57  ? 55.417  -130.706 16.720  1.00 91.55  ? 56  ALA   I N   1 
ATOM   15164 C  CA  . ALA   I  9  57  ? 56.008  -129.760 15.740  1.00 89.58  ? 56  ALA   I CA  1 
ATOM   15165 C  C   . ALA   I  9  57  ? 55.309  -128.395 15.789  1.00 85.10  ? 56  ALA   I C   1 
ATOM   15166 O  O   . ALA   I  9  57  ? 55.998  -127.386 15.551  1.00 85.85  ? 56  ALA   I O   1 
ATOM   15167 C  CB  . ALA   I  9  57  ? 55.957  -130.352 14.352  1.00 90.73  ? 56  ALA   I CB  1 
ATOM   15168 N  N   . THR   I  9  58  ? 54.000  -128.355 16.059  1.00 82.12  ? 57  THR   I N   1 
ATOM   15169 C  CA  . THR   I  9  58  ? 53.209  -127.094 16.163  1.00 82.66  ? 57  THR   I CA  1 
ATOM   15170 C  C   . THR   I  9  58  ? 53.699  -126.266 17.361  1.00 82.39  ? 57  THR   I C   1 
ATOM   15171 O  O   . THR   I  9  58  ? 53.686  -125.022 17.260  1.00 80.40  ? 57  THR   I O   1 
ATOM   15172 C  CB  . THR   I  9  58  ? 51.699  -127.360 16.246  1.00 81.95  ? 57  THR   I CB  1 
ATOM   15173 O  OG1 . THR   I  9  58  ? 51.034  -126.102 16.354  1.00 84.27  ? 57  THR   I OG1 1 
ATOM   15174 C  CG2 . THR   I  9  58  ? 51.296  -128.232 17.415  1.00 80.61  ? 57  THR   I CG2 1 
ATOM   15175 N  N   . ASP   I  9  59  ? 54.102  -126.929 18.451  1.00 81.42  ? 58  ASP   I N   1 
ATOM   15176 C  CA  . ASP   I  9  59  ? 54.646  -126.280 19.674  1.00 80.92  ? 58  ASP   I CA  1 
ATOM   15177 C  C   . ASP   I  9  59  ? 56.105  -125.872 19.442  1.00 81.50  ? 58  ASP   I C   1 
ATOM   15178 O  O   . ASP   I  9  59  ? 56.510  -124.835 19.998  1.00 85.16  ? 58  ASP   I O   1 
ATOM   15179 C  CB  . ASP   I  9  59  ? 54.511  -127.186 20.898  1.00 78.40  ? 58  ASP   I CB  1 
ATOM   15180 C  CG  . ASP   I  9  59  ? 53.076  -127.340 21.366  1.00 79.60  ? 58  ASP   I CG  1 
ATOM   15181 O  OD1 . ASP   I  9  59  ? 52.200  -126.661 20.794  1.00 79.49  ? 58  ASP   I OD1 1 
ATOM   15182 O  OD2 . ASP   I  9  59  ? 52.847  -128.128 22.302  1.00 80.01  ? 58  ASP   I OD2 1 
ATOM   15183 N  N   . VAL   I  9  60  ? 56.865  -126.653 18.668  1.00 78.89  ? 59  VAL   I N   1 
ATOM   15184 C  CA  . VAL   I  9  60  ? 58.252  -126.295 18.244  1.00 81.31  ? 59  VAL   I CA  1 
ATOM   15185 C  C   . VAL   I  9  60  ? 58.196  -124.947 17.517  1.00 82.35  ? 59  VAL   I C   1 
ATOM   15186 O  O   . VAL   I  9  60  ? 58.966  -124.041 17.893  1.00 84.50  ? 59  VAL   I O   1 
ATOM   15187 C  CB  . VAL   I  9  60  ? 58.890  -127.379 17.353  1.00 82.57  ? 59  VAL   I CB  1 
ATOM   15188 C  CG1 . VAL   I  9  60  ? 60.168  -126.886 16.686  1.00 84.16  ? 59  VAL   I CG1 1 
ATOM   15189 C  CG2 . VAL   I  9  60  ? 59.155  -128.661 18.125  1.00 82.74  ? 59  VAL   I CG2 1 
ATOM   15190 N  N   . THR   I  9  61  ? 57.317  -124.836 16.515  1.00 82.36  ? 60  THR   I N   1 
ATOM   15191 C  CA  . THR   I  9  61  ? 57.100  -123.609 15.703  1.00 81.83  ? 60  THR   I CA  1 
ATOM   15192 C  C   . THR   I  9  61  ? 56.663  -122.465 16.623  1.00 81.83  ? 60  THR   I C   1 
ATOM   15193 O  O   . THR   I  9  61  ? 57.312  -121.409 16.577  1.00 82.68  ? 60  THR   I O   1 
ATOM   15194 C  CB  . THR   I  9  61  ? 56.067  -123.830 14.590  1.00 83.47  ? 60  THR   I CB  1 
ATOM   15195 O  OG1 . THR   I  9  61  ? 56.486  -124.946 13.803  1.00 82.13  ? 60  THR   I OG1 1 
ATOM   15196 C  CG2 . THR   I  9  61  ? 55.902  -122.614 13.704  1.00 84.72  ? 60  THR   I CG2 1 
ATOM   15197 N  N   . THR   I  9  62  ? 55.608  -122.676 17.415  1.00 78.97  ? 61  THR   I N   1 
ATOM   15198 C  CA  . THR   I  9  62  ? 55.013  -121.658 18.323  1.00 79.26  ? 61  THR   I CA  1 
ATOM   15199 C  C   . THR   I  9  62  ? 56.096  -121.094 19.250  1.00 81.02  ? 61  THR   I C   1 
ATOM   15200 O  O   . THR   I  9  62  ? 56.221  -119.855 19.321  1.00 82.10  ? 61  THR   I O   1 
ATOM   15201 C  CB  . THR   I  9  62  ? 53.843  -122.231 19.134  1.00 78.48  ? 61  THR   I CB  1 
ATOM   15202 O  OG1 . THR   I  9  62  ? 52.788  -122.548 18.227  1.00 81.80  ? 61  THR   I OG1 1 
ATOM   15203 C  CG2 . THR   I  9  62  ? 53.337  -121.274 20.190  1.00 77.30  ? 61  THR   I CG2 1 
ATOM   15204 N  N   . LEU   I  9  63  ? 56.847  -121.962 19.931  1.00 80.46  ? 62  LEU   I N   1 
ATOM   15205 C  CA  . LEU   I  9  63  ? 57.844  -121.545 20.954  1.00 81.88  ? 62  LEU   I CA  1 
ATOM   15206 C  C   . LEU   I  9  63  ? 58.981  -120.758 20.293  1.00 81.68  ? 62  LEU   I C   1 
ATOM   15207 O  O   . LEU   I  9  63  ? 59.453  -119.789 20.913  1.00 82.14  ? 62  LEU   I O   1 
ATOM   15208 C  CB  . LEU   I  9  63  ? 58.378  -122.767 21.708  1.00 83.24  ? 62  LEU   I CB  1 
ATOM   15209 C  CG  . LEU   I  9  63  ? 57.490  -123.295 22.836  1.00 83.38  ? 62  LEU   I CG  1 
ATOM   15210 C  CD1 . LEU   I  9  63  ? 58.225  -124.359 23.626  1.00 84.88  ? 62  LEU   I CD1 1 
ATOM   15211 C  CD2 . LEU   I  9  63  ? 57.035  -122.182 23.770  1.00 85.25  ? 62  LEU   I CD2 1 
ATOM   15212 N  N   . ASN   I  9  64  ? 59.405  -121.149 19.089  1.00 81.16  ? 63  ASN   I N   1 
ATOM   15213 C  CA  . ASN   I  9  64  ? 60.423  -120.396 18.309  1.00 84.73  ? 63  ASN   I CA  1 
ATOM   15214 C  C   . ASN   I  9  64  ? 59.923  -118.963 18.103  1.00 85.62  ? 63  ASN   I C   1 
ATOM   15215 O  O   . ASN   I  9  64  ? 60.668  -118.022 18.441  1.00 85.58  ? 63  ASN   I O   1 
ATOM   15216 C  CB  . ASN   I  9  64  ? 60.733  -121.051 16.962  1.00 86.22  ? 63  ASN   I CB  1 
ATOM   15217 C  CG  . ASN   I  9  64  ? 61.547  -120.149 16.060  1.00 87.63  ? 63  ASN   I CG  1 
ATOM   15218 O  OD1 . ASN   I  9  64  ? 62.489  -119.498 16.509  1.00 90.04  ? 63  ASN   I OD1 1 
ATOM   15219 N  ND2 . ASN   I  9  64  ? 61.191  -120.098 14.787  1.00 91.06  ? 63  ASN   I ND2 1 
ATOM   15220 N  N   . GLU   I  9  65  ? 58.704  -118.824 17.575  1.00 86.78  ? 64  GLU   I N   1 
ATOM   15221 C  CA  . GLU   I  9  65  ? 58.037  -117.521 17.310  1.00 90.77  ? 64  GLU   I CA  1 
ATOM   15222 C  C   . GLU   I  9  65  ? 57.912  -116.730 18.618  1.00 94.53  ? 64  GLU   I C   1 
ATOM   15223 O  O   . GLU   I  9  65  ? 58.063  -115.489 18.574  1.00 99.32  ? 64  GLU   I O   1 
ATOM   15224 C  CB  . GLU   I  9  65  ? 56.655  -117.739 16.687  1.00 93.42  ? 64  GLU   I CB  1 
ATOM   15225 C  CG  . GLU   I  9  65  ? 56.694  -118.326 15.286  1.00 94.85  ? 64  GLU   I CG  1 
ATOM   15226 C  CD  . GLU   I  9  65  ? 55.333  -118.671 14.699  1.00 98.14  ? 64  GLU   I CD  1 
ATOM   15227 O  OE1 . GLU   I  9  65  ? 55.285  -119.065 13.511  1.00 99.62  ? 64  GLU   I OE1 1 
ATOM   15228 O  OE2 . GLU   I  9  65  ? 54.321  -118.547 15.428  1.00 93.98  ? 64  GLU   I OE2 1 
ATOM   15229 N  N   . MET   I  9  66  ? 57.639  -117.425 19.728  1.00 92.71  ? 65  MET   I N   1 
ATOM   15230 C  CA  . MET   I  9  66  ? 57.402  -116.826 21.070  1.00 92.83  ? 65  MET   I CA  1 
ATOM   15231 C  C   . MET   I  9  66  ? 58.717  -116.300 21.657  1.00 91.67  ? 65  MET   I C   1 
ATOM   15232 O  O   . MET   I  9  66  ? 58.693  -115.204 22.238  1.00 93.23  ? 65  MET   I O   1 
ATOM   15233 C  CB  . MET   I  9  66  ? 56.799  -117.856 22.029  1.00 93.19  ? 65  MET   I CB  1 
ATOM   15234 C  CG  . MET   I  9  66  ? 56.259  -117.257 23.311  1.00 98.37  ? 65  MET   I CG  1 
ATOM   15235 S  SD  . MET   I  9  66  ? 55.887  -118.539 24.535  1.00 98.28  ? 65  MET   I SD  1 
ATOM   15236 C  CE  . MET   I  9  66  ? 57.539  -118.883 25.137  1.00 98.84  ? 65  MET   I CE  1 
ATOM   15237 N  N   . PHE   I  9  67  ? 59.814  -117.054 21.539  1.00 87.33  ? 66  PHE   I N   1 
ATOM   15238 C  CA  . PHE   I  9  67  ? 61.139  -116.675 22.102  1.00 89.45  ? 66  PHE   I CA  1 
ATOM   15239 C  C   . PHE   I  9  67  ? 61.805  -115.610 21.220  1.00 91.93  ? 66  PHE   I C   1 
ATOM   15240 O  O   . PHE   I  9  67  ? 62.589  -114.806 21.765  1.00 94.43  ? 66  PHE   I O   1 
ATOM   15241 C  CB  . PHE   I  9  67  ? 62.025  -117.906 22.316  1.00 88.11  ? 66  PHE   I CB  1 
ATOM   15242 C  CG  . PHE   I  9  67  ? 61.572  -118.795 23.448  1.00 88.46  ? 66  PHE   I CG  1 
ATOM   15243 C  CD1 . PHE   I  9  67  ? 61.332  -118.270 24.710  1.00 89.24  ? 66  PHE   I CD1 1 
ATOM   15244 C  CD2 . PHE   I  9  67  ? 61.382  -120.154 23.257  1.00 87.38  ? 66  PHE   I CD2 1 
ATOM   15245 C  CE1 . PHE   I  9  67  ? 60.904  -119.083 25.748  1.00 88.88  ? 66  PHE   I CE1 1 
ATOM   15246 C  CE2 . PHE   I  9  67  ? 60.956  -120.967 24.297  1.00 87.10  ? 66  PHE   I CE2 1 
ATOM   15247 C  CZ  . PHE   I  9  67  ? 60.716  -120.430 25.540  1.00 86.87  ? 66  PHE   I CZ  1 
ATOM   15248 N  N   . ARG   I  9  68  ? 61.503  -115.587 19.917  1.00 89.42  ? 67  ARG   I N   1 
ATOM   15249 C  CA  . ARG   I  9  68  ? 61.921  -114.491 19.000  1.00 88.60  ? 67  ARG   I CA  1 
ATOM   15250 C  C   . ARG   I  9  68  ? 61.267  -113.191 19.479  1.00 85.38  ? 67  ARG   I C   1 
ATOM   15251 O  O   . ARG   I  9  68  ? 61.992  -112.204 19.676  1.00 86.56  ? 67  ARG   I O   1 
ATOM   15252 C  CB  . ARG   I  9  68  ? 61.527  -114.798 17.553  1.00 87.60  ? 67  ARG   I CB  1 
ATOM   15253 C  CG  . ARG   I  9  68  ? 61.971  -113.737 16.557  1.00 88.46  ? 67  ARG   I CG  1 
ATOM   15254 C  CD  . ARG   I  9  68  ? 61.651  -114.114 15.128  1.00 90.16  ? 67  ARG   I CD  1 
ATOM   15255 N  NE  . ARG   I  9  68  ? 60.222  -114.294 14.908  1.00 91.75  ? 67  ARG   I NE  1 
ATOM   15256 C  CZ  . ARG   I  9  68  ? 59.667  -114.564 13.730  1.00 95.43  ? 67  ARG   I CZ  1 
ATOM   15257 N  NH1 . ARG   I  9  68  ? 60.419  -114.683 12.646  1.00 100.13 ? 67  ARG   I NH1 1 
ATOM   15258 N  NH2 . ARG   I  9  68  ? 58.357  -114.710 13.638  1.00 96.33  ? 67  ARG   I NH2 1 
ATOM   15259 N  N   . TYR   I  9  69  ? 59.944  -113.225 19.665  1.00 84.09  ? 68  TYR   I N   1 
ATOM   15260 C  CA  . TYR   I  9  69  ? 59.094  -112.138 20.222  1.00 83.75  ? 68  TYR   I CA  1 
ATOM   15261 C  C   . TYR   I  9  69  ? 59.720  -111.585 21.508  1.00 85.60  ? 68  TYR   I C   1 
ATOM   15262 O  O   . TYR   I  9  69  ? 59.857  -110.356 21.625  1.00 86.31  ? 68  TYR   I O   1 
ATOM   15263 C  CB  . TYR   I  9  69  ? 57.680  -112.674 20.469  1.00 82.91  ? 68  TYR   I CB  1 
ATOM   15264 C  CG  . TYR   I  9  69  ? 56.676  -111.704 21.041  1.00 80.92  ? 68  TYR   I CG  1 
ATOM   15265 C  CD1 . TYR   I  9  69  ? 56.804  -111.198 22.324  1.00 79.14  ? 68  TYR   I CD1 1 
ATOM   15266 C  CD2 . TYR   I  9  69  ? 55.554  -111.339 20.314  1.00 82.27  ? 68  TYR   I CD2 1 
ATOM   15267 C  CE1 . TYR   I  9  69  ? 55.869  -110.324 22.854  1.00 79.99  ? 68  TYR   I CE1 1 
ATOM   15268 C  CE2 . TYR   I  9  69  ? 54.609  -110.467 20.829  1.00 82.90  ? 68  TYR   I CE2 1 
ATOM   15269 C  CZ  . TYR   I  9  69  ? 54.766  -109.959 22.106  1.00 82.08  ? 68  TYR   I CZ  1 
ATOM   15270 O  OH  . TYR   I  9  69  ? 53.846  -109.102 22.636  1.00 84.65  ? 68  TYR   I OH  1 
ATOM   15271 N  N   . LYS   I  9  70  ? 60.078  -112.469 22.444  1.00 83.63  ? 69  LYS   I N   1 
ATOM   15272 C  CA  . LYS   I  9  70  ? 60.490  -112.101 23.827  1.00 84.37  ? 69  LYS   I CA  1 
ATOM   15273 C  C   . LYS   I  9  70  ? 61.934  -111.588 23.841  1.00 84.96  ? 69  LYS   I C   1 
ATOM   15274 O  O   . LYS   I  9  70  ? 62.204  -110.657 24.621  1.00 86.79  ? 69  LYS   I O   1 
ATOM   15275 C  CB  . LYS   I  9  70  ? 60.293  -113.283 24.779  1.00 82.57  ? 69  LYS   I CB  1 
ATOM   15276 C  CG  . LYS   I  9  70  ? 58.840  -113.521 25.166  1.00 84.03  ? 69  LYS   I CG  1 
ATOM   15277 C  CD  . LYS   I  9  70  ? 58.631  -114.597 26.205  1.00 85.03  ? 69  LYS   I CD  1 
ATOM   15278 C  CE  . LYS   I  9  70  ? 57.178  -114.715 26.615  1.00 86.03  ? 69  LYS   I CE  1 
ATOM   15279 N  NZ  . LYS   I  9  70  ? 57.008  -115.569 27.812  1.00 86.86  ? 69  LYS   I NZ  1 
ATOM   15280 N  N   . THR   I  9  71  ? 62.824  -112.159 23.024  1.00 83.85  ? 70  THR   I N   1 
ATOM   15281 C  CA  . THR   I  9  71  ? 64.249  -111.738 22.927  1.00 85.61  ? 70  THR   I CA  1 
ATOM   15282 C  C   . THR   I  9  71  ? 64.370  -110.411 22.165  1.00 89.17  ? 70  THR   I C   1 
ATOM   15283 O  O   . THR   I  9  71  ? 65.315  -109.647 22.466  1.00 91.49  ? 70  THR   I O   1 
ATOM   15284 C  CB  . THR   I  9  71  ? 65.117  -112.822 22.280  1.00 85.43  ? 70  THR   I CB  1 
ATOM   15285 O  OG1 . THR   I  9  71  ? 64.469  -113.259 21.084  1.00 84.66  ? 70  THR   I OG1 1 
ATOM   15286 C  CG2 . THR   I  9  71  ? 65.360  -113.989 23.211  1.00 84.01  ? 70  THR   I CG2 1 
ATOM   15287 N  N   . ASN   I  9  72  ? 63.466  -110.156 21.213  1.00 87.80  ? 71  ASN   I N   1 
ATOM   15288 C  CA  . ASN   I  9  72  ? 63.422  -108.895 20.423  1.00 86.82  ? 71  ASN   I CA  1 
ATOM   15289 C  C   . ASN   I  9  72  ? 63.100  -107.731 21.366  1.00 85.78  ? 71  ASN   I C   1 
ATOM   15290 O  O   . ASN   I  9  72  ? 63.815  -106.713 21.288  1.00 83.95  ? 71  ASN   I O   1 
ATOM   15291 C  CB  . ASN   I  9  72  ? 62.439  -108.982 19.251  1.00 84.89  ? 71  ASN   I CB  1 
ATOM   15292 C  CG  . ASN   I  9  72  ? 63.014  -109.710 18.054  1.00 83.84  ? 71  ASN   I CG  1 
ATOM   15293 O  OD1 . ASN   I  9  72  ? 64.028  -110.394 18.169  1.00 83.45  ? 71  ASN   I OD1 1 
ATOM   15294 N  ND2 . ASN   I  9  72  ? 62.386  -109.561 16.900  1.00 85.32  ? 71  ASN   I ND2 1 
ATOM   15295 N  N   . LEU   I  9  73  ? 62.081  -107.889 22.221  1.00 84.26  ? 72  LEU   I N   1 
ATOM   15296 C  CA  . LEU   I  9  73  ? 61.660  -106.870 23.224  1.00 86.76  ? 72  LEU   I CA  1 
ATOM   15297 C  C   . LEU   I  9  73  ? 62.744  -106.724 24.297  1.00 88.69  ? 72  LEU   I C   1 
ATOM   15298 O  O   . LEU   I  9  73  ? 62.954  -105.590 24.772  1.00 88.35  ? 72  LEU   I O   1 
ATOM   15299 C  CB  . LEU   I  9  73  ? 60.324  -107.265 23.865  1.00 87.54  ? 72  LEU   I CB  1 
ATOM   15300 C  CG  . LEU   I  9  73  ? 59.076  -107.113 22.994  1.00 89.85  ? 72  LEU   I CG  1 
ATOM   15301 C  CD1 . LEU   I  9  73  ? 57.829  -107.511 23.770  1.00 88.95  ? 72  LEU   I CD1 1 
ATOM   15302 C  CD2 . LEU   I  9  73  ? 58.927  -105.693 22.457  1.00 92.17  ? 72  LEU   I CD2 1 
ATOM   15303 N  N   . TYR   I  9  74  ? 63.388  -107.832 24.677  1.00 89.23  ? 73  TYR   I N   1 
ATOM   15304 C  CA  . TYR   I  9  74  ? 64.516  -107.860 25.645  1.00 90.54  ? 73  TYR   I CA  1 
ATOM   15305 C  C   . TYR   I  9  74  ? 65.623  -106.925 25.148  1.00 93.34  ? 73  TYR   I C   1 
ATOM   15306 O  O   . TYR   I  9  74  ? 66.080  -106.076 25.929  1.00 98.85  ? 73  TYR   I O   1 
ATOM   15307 C  CB  . TYR   I  9  74  ? 65.046  -109.285 25.834  1.00 88.83  ? 73  TYR   I CB  1 
ATOM   15308 C  CG  . TYR   I  9  74  ? 66.176  -109.416 26.824  1.00 87.54  ? 73  TYR   I CG  1 
ATOM   15309 C  CD1 . TYR   I  9  74  ? 67.498  -109.290 26.425  1.00 88.53  ? 73  TYR   I CD1 1 
ATOM   15310 C  CD2 . TYR   I  9  74  ? 65.930  -109.671 28.164  1.00 86.15  ? 73  TYR   I CD2 1 
ATOM   15311 C  CE1 . TYR   I  9  74  ? 68.543  -109.408 27.328  1.00 87.73  ? 73  TYR   I CE1 1 
ATOM   15312 C  CE2 . TYR   I  9  74  ? 66.963  -109.792 29.081  1.00 86.18  ? 73  TYR   I CE2 1 
ATOM   15313 C  CZ  . TYR   I  9  74  ? 68.275  -109.661 28.661  1.00 86.57  ? 73  TYR   I CZ  1 
ATOM   15314 O  OH  . TYR   I  9  74  ? 69.302  -109.782 29.553  1.00 86.36  ? 73  TYR   I OH  1 
ATOM   15315 N  N   . LYS   I  9  75  ? 66.018  -107.077 23.880  1.00 96.27  ? 74  LYS   I N   1 
ATOM   15316 C  CA  . LYS   I  9  75  ? 67.152  -106.345 23.255  1.00 98.06  ? 74  LYS   I CA  1 
ATOM   15317 C  C   . LYS   I  9  75  ? 66.827  -104.850 23.133  1.00 97.56  ? 74  LYS   I C   1 
ATOM   15318 O  O   . LYS   I  9  75  ? 67.749  -104.037 23.332  1.00 97.65  ? 74  LYS   I O   1 
ATOM   15319 C  CB  . LYS   I  9  75  ? 67.478  -106.934 21.881  1.00 99.57  ? 74  LYS   I CB  1 
ATOM   15320 C  CG  . LYS   I  9  75  ? 68.791  -106.448 21.292  1.00 101.18 ? 74  LYS   I CG  1 
ATOM   15321 C  CD  . LYS   I  9  75  ? 69.071  -106.984 19.917  1.00 103.93 ? 74  LYS   I CD  1 
ATOM   15322 C  CE  . LYS   I  9  75  ? 70.431  -106.563 19.411  1.00 108.66 ? 74  LYS   I CE  1 
ATOM   15323 N  NZ  . LYS   I  9  75  ? 70.837  -107.356 18.229  1.00 112.56 ? 74  LYS   I NZ  1 
ATOM   15324 N  N   . LEU   I  9  76  ? 65.580  -104.504 22.796  1.00 97.25  ? 75  LEU   I N   1 
ATOM   15325 C  CA  . LEU   I  9  76  ? 65.121  -103.097 22.632  1.00 98.45  ? 75  LEU   I CA  1 
ATOM   15326 C  C   . LEU   I  9  76  ? 65.216  -102.362 23.978  1.00 101.16 ? 75  LEU   I C   1 
ATOM   15327 O  O   . LEU   I  9  76  ? 65.634  -101.185 23.975  1.00 104.83 ? 75  LEU   I O   1 
ATOM   15328 C  CB  . LEU   I  9  76  ? 63.689  -103.085 22.083  1.00 94.83  ? 75  LEU   I CB  1 
ATOM   15329 C  CG  . LEU   I  9  76  ? 63.562  -103.284 20.573  1.00 93.84  ? 75  LEU   I CG  1 
ATOM   15330 C  CD1 . LEU   I  9  76  ? 62.195  -103.841 20.207  1.00 92.41  ? 75  LEU   I CD1 1 
ATOM   15331 C  CD2 . LEU   I  9  76  ? 63.819  -101.982 19.834  1.00 94.76  ? 75  LEU   I CD2 1 
ATOM   15332 N  N   . LYS   I  9  77  ? 64.858  -103.035 25.079  1.00 98.43  ? 76  LYS   I N   1 
ATOM   15333 C  CA  . LYS   I  9  77  ? 64.768  -102.446 26.445  1.00 98.91  ? 76  LYS   I CA  1 
ATOM   15334 C  C   . LYS   I  9  77  ? 66.129  -102.512 27.150  1.00 99.20  ? 76  LYS   I C   1 
ATOM   15335 O  O   . LYS   I  9  77  ? 66.478  -101.541 27.842  1.00 101.28 ? 76  LYS   I O   1 
ATOM   15336 C  CB  . LYS   I  9  77  ? 63.700  -103.174 27.266  1.00 99.84  ? 76  LYS   I CB  1 
ATOM   15337 C  CG  . LYS   I  9  77  ? 62.287  -103.073 26.706  1.00 102.60 ? 76  LYS   I CG  1 
ATOM   15338 C  CD  . LYS   I  9  77  ? 61.321  -104.086 27.277  1.00 105.22 ? 76  LYS   I CD  1 
ATOM   15339 C  CE  . LYS   I  9  77  ? 60.668  -103.623 28.561  1.00 108.67 ? 76  LYS   I CE  1 
ATOM   15340 N  NZ  . LYS   I  9  77  ? 59.686  -104.617 29.054  1.00 111.25 ? 76  LYS   I NZ  1 
ATOM   15341 N  N   . GLU   I  9  78  ? 66.857  -103.619 26.993  1.00 98.58  ? 77  GLU   I N   1 
ATOM   15342 C  CA  . GLU   I  9  78  ? 68.167  -103.867 27.658  1.00 102.94 ? 77  GLU   I CA  1 
ATOM   15343 C  C   . GLU   I  9  78  ? 69.309  -103.232 26.852  1.00 102.94 ? 77  GLU   I C   1 
ATOM   15344 O  O   . GLU   I  9  78  ? 70.373  -102.996 27.454  1.00 102.43 ? 77  GLU   I O   1 
ATOM   15345 C  CB  . GLU   I  9  78  ? 68.414  -105.370 27.816  1.00 103.19 ? 77  GLU   I CB  1 
ATOM   15346 C  CG  . GLU   I  9  78  ? 67.435  -106.065 28.752  1.00 103.74 ? 77  GLU   I CG  1 
ATOM   15347 C  CD  . GLU   I  9  78  ? 67.872  -106.207 30.203  1.00 104.00 ? 77  GLU   I CD  1 
ATOM   15348 O  OE1 . GLU   I  9  78  ? 68.994  -105.772 30.540  1.00 107.73 ? 77  GLU   I OE1 1 
ATOM   15349 O  OE2 . GLU   I  9  78  ? 67.084  -106.761 31.000  1.00 100.41 ? 77  GLU   I OE2 1 
ATOM   15350 N  N   . GLU   I  9  79  ? 69.105  -102.992 25.549  1.00 105.09 ? 78  GLU   I N   1 
ATOM   15351 C  CA  . GLU   I  9  79  ? 70.124  -102.463 24.595  1.00 109.44 ? 78  GLU   I CA  1 
ATOM   15352 C  C   . GLU   I  9  79  ? 71.339  -103.401 24.546  1.00 106.45 ? 78  GLU   I C   1 
ATOM   15353 O  O   . GLU   I  9  79  ? 72.473  -102.902 24.424  1.00 104.43 ? 78  GLU   I O   1 
ATOM   15354 C  CB  . GLU   I  9  79  ? 70.527  -101.034 24.969  1.00 113.87 ? 78  GLU   I CB  1 
ATOM   15355 C  CG  . GLU   I  9  79  ? 69.533  -99.987  24.506  1.00 118.59 ? 78  GLU   I CG  1 
ATOM   15356 C  CD  . GLU   I  9  79  ? 69.886  -98.566  24.907  1.00 123.85 ? 78  GLU   I CD  1 
ATOM   15357 O  OE1 . GLU   I  9  79  ? 70.292  -98.362  26.068  1.00 126.86 ? 78  GLU   I OE1 1 
ATOM   15358 O  OE2 . GLU   I  9  79  ? 69.759  -97.667  24.053  1.00 132.51 ? 78  GLU   I OE2 1 
ATOM   15359 N  N   . ARG   I  9  80  ? 71.109  -104.714 24.625  1.00 105.32 ? 79  ARG   I N   1 
ATOM   15360 C  CA  . ARG   I  9  80  ? 72.166  -105.752 24.485  1.00 106.44 ? 79  ARG   I CA  1 
ATOM   15361 C  C   . ARG   I  9  80  ? 71.516  -107.099 24.159  1.00 105.96 ? 79  ARG   I C   1 
ATOM   15362 O  O   . ARG   I  9  80  ? 70.323  -107.277 24.486  1.00 108.20 ? 79  ARG   I O   1 
ATOM   15363 C  CB  . ARG   I  9  80  ? 73.021  -105.847 25.755  1.00 108.10 ? 79  ARG   I CB  1 
ATOM   15364 C  CG  . ARG   I  9  80  ? 72.302  -106.401 26.978  1.00 107.84 ? 79  ARG   I CG  1 
ATOM   15365 C  CD  . ARG   I  9  80  ? 73.191  -106.319 28.205  1.00 109.76 ? 79  ARG   I CD  1 
ATOM   15366 N  NE  . ARG   I  9  80  ? 72.520  -106.766 29.418  1.00 109.81 ? 79  ARG   I NE  1 
ATOM   15367 C  CZ  . ARG   I  9  80  ? 72.435  -108.028 29.833  1.00 107.88 ? 79  ARG   I CZ  1 
ATOM   15368 N  NH1 . ARG   I  9  80  ? 72.977  -109.012 29.134  1.00 107.81 ? 79  ARG   I NH1 1 
ATOM   15369 N  NH2 . ARG   I  9  80  ? 71.798  -108.300 30.959  1.00 110.93 ? 79  ARG   I NH2 1 
ATOM   15370 N  N   . ALA   I  9  81  ? 72.282  -108.002 23.540  1.00 107.07 ? 80  ALA   I N   1 
ATOM   15371 C  CA  . ALA   I  9  81  ? 71.865  -109.385 23.216  1.00 104.38 ? 80  ALA   I CA  1 
ATOM   15372 C  C   . ALA   I  9  81  ? 71.749  -110.186 24.518  1.00 100.50 ? 80  ALA   I C   1 
ATOM   15373 O  O   . ALA   I  9  81  ? 72.606  -110.002 25.408  1.00 96.84  ? 80  ALA   I O   1 
ATOM   15374 C  CB  . ALA   I  9  81  ? 72.850  -110.014 22.258  1.00 106.12 ? 80  ALA   I CB  1 
ATOM   15375 N  N   . ILE   I  9  82  ? 70.717  -111.025 24.628  1.00 97.45  ? 81  ILE   I N   1 
ATOM   15376 C  CA  . ILE   I  9  82  ? 70.491  -111.927 25.798  1.00 97.67  ? 81  ILE   I CA  1 
ATOM   15377 C  C   . ILE   I  9  82  ? 71.615  -112.971 25.842  1.00 99.58  ? 81  ILE   I C   1 
ATOM   15378 O  O   . ILE   I  9  82  ? 72.061  -113.402 24.757  1.00 97.44  ? 81  ILE   I O   1 
ATOM   15379 C  CB  . ILE   I  9  82  ? 69.093  -112.578 25.739  1.00 96.16  ? 81  ILE   I CB  1 
ATOM   15380 C  CG1 . ILE   I  9  82  ? 68.709  -113.198 27.086  1.00 94.87  ? 81  ILE   I CG1 1 
ATOM   15381 C  CG2 . ILE   I  9  82  ? 68.993  -113.590 24.603  1.00 95.74  ? 81  ILE   I CG2 1 
ATOM   15382 C  CD1 . ILE   I  9  82  ? 67.224  -113.423 27.258  1.00 92.05  ? 81  ILE   I CD1 1 
ATOM   15383 N  N   . GLU   I  9  83  ? 72.056  -113.345 27.050  1.00 100.05 ? 82  GLU   I N   1 
ATOM   15384 C  CA  . GLU   I  9  83  ? 73.113  -114.369 27.284  1.00 100.01 ? 82  GLU   I CA  1 
ATOM   15385 C  C   . GLU   I  9  83  ? 72.454  -115.727 27.526  1.00 99.26  ? 82  GLU   I C   1 
ATOM   15386 O  O   . GLU   I  9  83  ? 71.300  -115.790 27.948  1.00 98.48  ? 82  GLU   I O   1 
ATOM   15387 C  CB  . GLU   I  9  83  ? 74.003  -113.981 28.468  1.00 101.08 ? 82  GLU   I CB  1 
ATOM   15388 C  CG  . GLU   I  9  83  ? 74.768  -112.679 28.274  1.00 102.07 ? 82  GLU   I CG  1 
ATOM   15389 C  CD  . GLU   I  9  83  ? 75.771  -112.657 27.132  1.00 101.59 ? 82  GLU   I CD  1 
ATOM   15390 O  OE1 . GLU   I  9  83  ? 76.162  -113.741 26.658  1.00 102.50 ? 82  GLU   I OE1 1 
ATOM   15391 O  OE2 . GLU   I  9  83  ? 76.164  -111.550 26.723  1.00 103.09 ? 82  GLU   I OE2 1 
ATOM   15392 N  N   . PRO   I  9  84  ? 73.164  -116.852 27.262  1.00 98.70  ? 83  PRO   I N   1 
ATOM   15393 C  CA  . PRO   I  9  84  ? 72.583  -118.190 27.401  1.00 96.85  ? 83  PRO   I CA  1 
ATOM   15394 C  C   . PRO   I  9  84  ? 71.952  -118.471 28.775  1.00 95.78  ? 83  PRO   I C   1 
ATOM   15395 O  O   . PRO   I  9  84  ? 70.889  -119.068 28.809  1.00 96.95  ? 83  PRO   I O   1 
ATOM   15396 C  CB  . PRO   I  9  84  ? 73.783  -119.123 27.171  1.00 95.70  ? 83  PRO   I CB  1 
ATOM   15397 C  CG  . PRO   I  9  84  ? 74.711  -118.322 26.290  1.00 96.95  ? 83  PRO   I CG  1 
ATOM   15398 C  CD  . PRO   I  9  84  ? 74.556  -116.899 26.782  1.00 98.64  ? 83  PRO   I CD  1 
ATOM   15399 N  N   . GLU   I  9  85  ? 72.607  -118.035 29.857  1.00 97.91  ? 84  GLU   I N   1 
ATOM   15400 C  CA  . GLU   I  9  85  ? 72.164  -118.272 31.259  1.00 97.70  ? 84  GLU   I CA  1 
ATOM   15401 C  C   . GLU   I  9  85  ? 70.821  -117.572 31.492  1.00 96.60  ? 84  GLU   I C   1 
ATOM   15402 O  O   . GLU   I  9  85  ? 69.930  -118.205 32.094  1.00 92.76  ? 84  GLU   I O   1 
ATOM   15403 C  CB  . GLU   I  9  85  ? 73.199  -117.773 32.268  1.00 99.44  ? 84  GLU   I CB  1 
ATOM   15404 C  CG  . GLU   I  9  85  ? 74.476  -118.591 32.293  1.00 102.81 ? 84  GLU   I CG  1 
ATOM   15405 C  CD  . GLU   I  9  85  ? 75.568  -118.123 31.345  1.00 106.60 ? 84  GLU   I CD  1 
ATOM   15406 O  OE1 . GLU   I  9  85  ? 75.235  -117.490 30.320  1.00 109.29 ? 84  GLU   I OE1 1 
ATOM   15407 O  OE2 . GLU   I  9  85  ? 76.752  -118.387 31.637  1.00 109.51 ? 84  GLU   I OE2 1 
ATOM   15408 N  N   . THR   I  9  86  ? 70.691  -116.320 31.039  1.00 98.87  ? 85  THR   I N   1 
ATOM   15409 C  CA  . THR   I  9  86  ? 69.446  -115.512 31.149  1.00 99.35  ? 85  THR   I CA  1 
ATOM   15410 C  C   . THR   I  9  86  ? 68.359  -116.168 30.291  1.00 95.03  ? 85  THR   I C   1 
ATOM   15411 O  O   . THR   I  9  86  ? 67.246  -116.373 30.813  1.00 94.39  ? 85  THR   I O   1 
ATOM   15412 C  CB  . THR   I  9  86  ? 69.680  -114.043 30.769  1.00 99.19  ? 85  THR   I CB  1 
ATOM   15413 O  OG1 . THR   I  9  86  ? 70.720  -113.547 31.611  1.00 103.67 ? 85  THR   I OG1 1 
ATOM   15414 C  CG2 . THR   I  9  86  ? 68.445  -113.182 30.927  1.00 99.41  ? 85  THR   I CG2 1 
ATOM   15415 N  N   . PHE   I  9  87  ? 68.672  -116.496 29.033  1.00 93.71  ? 86  PHE   I N   1 
ATOM   15416 C  CA  . PHE   I  9  87  ? 67.702  -117.077 28.069  1.00 92.34  ? 86  PHE   I CA  1 
ATOM   15417 C  C   . PHE   I  9  87  ? 67.143  -118.380 28.645  1.00 91.32  ? 86  PHE   I C   1 
ATOM   15418 O  O   . PHE   I  9  87  ? 65.919  -118.589 28.563  1.00 91.52  ? 86  PHE   I O   1 
ATOM   15419 C  CB  . PHE   I  9  87  ? 68.324  -117.320 26.693  1.00 91.90  ? 86  PHE   I CB  1 
ATOM   15420 C  CG  . PHE   I  9  87  ? 67.326  -117.824 25.681  1.00 90.71  ? 86  PHE   I CG  1 
ATOM   15421 C  CD1 . PHE   I  9  87  ? 66.339  -116.985 25.189  1.00 92.48  ? 86  PHE   I CD1 1 
ATOM   15422 C  CD2 . PHE   I  9  87  ? 67.342  -119.143 25.258  1.00 91.45  ? 86  PHE   I CD2 1 
ATOM   15423 C  CE1 . PHE   I  9  87  ? 65.405  -117.448 24.275  1.00 91.64  ? 86  PHE   I CE1 1 
ATOM   15424 C  CE2 . PHE   I  9  87  ? 66.407  -119.603 24.342  1.00 91.87  ? 86  PHE   I CE2 1 
ATOM   15425 C  CZ  . PHE   I  9  87  ? 65.442  -118.755 23.851  1.00 92.04  ? 86  PHE   I CZ  1 
ATOM   15426 N  N   . THR   I  9  88  ? 68.018  -119.217 29.211  1.00 89.92  ? 87  THR   I N   1 
ATOM   15427 C  CA  . THR   I  9  88  ? 67.660  -120.502 29.872  1.00 88.32  ? 87  THR   I CA  1 
ATOM   15428 C  C   . THR   I  9  88  ? 66.572  -120.254 30.924  1.00 88.29  ? 87  THR   I C   1 
ATOM   15429 O  O   . THR   I  9  88  ? 65.606  -121.041 30.976  1.00 86.65  ? 87  THR   I O   1 
ATOM   15430 C  CB  . THR   I  9  88  ? 68.883  -121.164 30.518  1.00 87.21  ? 87  THR   I CB  1 
ATOM   15431 O  OG1 . THR   I  9  88  ? 69.759  -121.598 29.478  1.00 87.65  ? 87  THR   I OG1 1 
ATOM   15432 C  CG2 . THR   I  9  88  ? 68.516  -122.338 31.399  1.00 86.90  ? 87  THR   I CG2 1 
ATOM   15433 N  N   . GLN   I  9  89  ? 66.740  -119.207 31.735  1.00 88.92  ? 88  GLN   I N   1 
ATOM   15434 C  CA  . GLN   I  9  89  ? 65.776  -118.815 32.794  1.00 87.49  ? 88  GLN   I CA  1 
ATOM   15435 C  C   . GLN   I  9  89  ? 64.445  -118.411 32.149  1.00 84.80  ? 88  GLN   I C   1 
ATOM   15436 O  O   . GLN   I  9  89  ? 63.397  -118.811 32.690  1.00 79.99  ? 88  GLN   I O   1 
ATOM   15437 C  CB  . GLN   I  9  89  ? 66.361  -117.695 33.655  1.00 89.57  ? 88  GLN   I CB  1 
ATOM   15438 C  CG  . GLN   I  9  89  ? 67.398  -118.182 34.659  1.00 91.33  ? 88  GLN   I CG  1 
ATOM   15439 C  CD  . GLN   I  9  89  ? 66.856  -119.235 35.595  1.00 91.24  ? 88  GLN   I CD  1 
ATOM   15440 O  OE1 . GLN   I  9  89  ? 67.466  -120.283 35.787  1.00 91.09  ? 88  GLN   I OE1 1 
ATOM   15441 N  NE2 . GLN   I  9  89  ? 65.700  -118.967 36.183  1.00 94.47  ? 88  GLN   I NE2 1 
ATOM   15442 N  N   . LEU   I  9  90  ? 64.486  -117.662 31.039  1.00 87.99  ? 89  LEU   I N   1 
ATOM   15443 C  CA  . LEU   I  9  90  ? 63.275  -117.186 30.309  1.00 88.25  ? 89  LEU   I CA  1 
ATOM   15444 C  C   . LEU   I  9  90  ? 62.493  -118.396 29.783  1.00 84.55  ? 89  LEU   I C   1 
ATOM   15445 O  O   . LEU   I  9  90  ? 61.253  -118.390 29.896  1.00 82.32  ? 89  LEU   I O   1 
ATOM   15446 C  CB  . LEU   I  9  90  ? 63.677  -116.242 29.166  1.00 89.65  ? 89  LEU   I CB  1 
ATOM   15447 C  CG  . LEU   I  9  90  ? 62.530  -115.742 28.286  1.00 88.52  ? 89  LEU   I CG  1 
ATOM   15448 C  CD1 . LEU   I  9  90  ? 61.588  -114.839 29.069  1.00 88.94  ? 89  LEU   I CD1 1 
ATOM   15449 C  CD2 . LEU   I  9  90  ? 63.061  -115.019 27.057  1.00 89.73  ? 89  LEU   I CD2 1 
ATOM   15450 N  N   . VAL   I  9  91  ? 63.193  -119.390 29.229  1.00 83.83  ? 90  VAL   I N   1 
ATOM   15451 C  CA  . VAL   I  9  91  ? 62.579  -120.638 28.682  1.00 83.97  ? 90  VAL   I CA  1 
ATOM   15452 C  C   . VAL   I  9  91  ? 61.870  -121.378 29.823  1.00 83.70  ? 90  VAL   I C   1 
ATOM   15453 O  O   . VAL   I  9  91  ? 60.714  -121.806 29.622  1.00 80.79  ? 90  VAL   I O   1 
ATOM   15454 C  CB  . VAL   I  9  91  ? 63.622  -121.537 27.989  1.00 85.13  ? 90  VAL   I CB  1 
ATOM   15455 C  CG1 . VAL   I  9  91  ? 63.059  -122.917 27.683  1.00 83.74  ? 90  VAL   I CG1 1 
ATOM   15456 C  CG2 . VAL   I  9  91  ? 64.168  -120.896 26.722  1.00 86.19  ? 90  VAL   I CG2 1 
ATOM   15457 N  N   . SER   I  9  92  ? 62.542  -121.518 30.970  1.00 83.83  ? 91  SER   I N   1 
ATOM   15458 C  CA  . SER   I  9  92  ? 62.016  -122.188 32.186  1.00 83.06  ? 91  SER   I CA  1 
ATOM   15459 C  C   . SER   I  9  92  ? 60.723  -121.504 32.645  1.00 84.22  ? 91  SER   I C   1 
ATOM   15460 O  O   . SER   I  9  92  ? 59.713  -122.216 32.813  1.00 82.65  ? 91  SER   I O   1 
ATOM   15461 C  CB  . SER   I  9  92  ? 63.040  -122.203 33.284  1.00 85.31  ? 91  SER   I CB  1 
ATOM   15462 O  OG  . SER   I  9  92  ? 62.629  -123.058 34.340  1.00 85.97  ? 91  SER   I OG  1 
ATOM   15463 N  N   . SER   I  9  93  ? 60.764  -120.180 32.835  1.00 86.00  ? 92  SER   I N   1 
ATOM   15464 C  CA  . SER   I  9  93  ? 59.611  -119.330 33.234  1.00 87.24  ? 92  SER   I CA  1 
ATOM   15465 C  C   . SER   I  9  93  ? 58.437  -119.579 32.285  1.00 82.03  ? 92  SER   I C   1 
ATOM   15466 O  O   . SER   I  9  93  ? 57.334  -119.889 32.774  1.00 81.88  ? 92  SER   I O   1 
ATOM   15467 C  CB  . SER   I  9  93  ? 59.986  -117.869 33.239  1.00 89.68  ? 92  SER   I CB  1 
ATOM   15468 O  OG  . SER   I  9  93  ? 61.254  -117.680 33.847  1.00 95.13  ? 92  SER   I OG  1 
ATOM   15469 N  N   . SER   I  9  94  ? 58.693  -119.447 30.980  1.00 85.20  ? 93  SER   I N   1 
ATOM   15470 C  CA  . SER   I  9  94  ? 57.682  -119.476 29.892  1.00 89.14  ? 93  SER   I CA  1 
ATOM   15471 C  C   . SER   I  9  94  ? 56.963  -120.831 29.875  1.00 88.34  ? 93  SER   I C   1 
ATOM   15472 O  O   . SER   I  9  94  ? 55.729  -120.844 29.682  1.00 91.18  ? 93  SER   I O   1 
ATOM   15473 C  CB  . SER   I  9  94  ? 58.321  -119.166 28.559  1.00 91.78  ? 93  SER   I CB  1 
ATOM   15474 O  OG  . SER   I  9  94  ? 58.950  -117.892 28.577  1.00 93.55  ? 93  SER   I OG  1 
ATOM   15475 N  N   . LEU   I  9  95  ? 57.702  -121.926 30.080  1.00 86.81  ? 94  LEU   I N   1 
ATOM   15476 C  CA  . LEU   I  9  95  ? 57.154  -123.309 30.044  1.00 86.10  ? 94  LEU   I CA  1 
ATOM   15477 C  C   . LEU   I  9  95  ? 56.290  -123.559 31.285  1.00 83.29  ? 94  LEU   I C   1 
ATOM   15478 O  O   . LEU   I  9  95  ? 55.178  -124.104 31.122  1.00 85.47  ? 94  LEU   I O   1 
ATOM   15479 C  CB  . LEU   I  9  95  ? 58.299  -124.325 29.954  1.00 87.17  ? 94  LEU   I CB  1 
ATOM   15480 C  CG  . LEU   I  9  95  ? 59.023  -124.399 28.608  1.00 87.03  ? 94  LEU   I CG  1 
ATOM   15481 C  CD1 . LEU   I  9  95  ? 60.222  -125.329 28.694  1.00 83.93  ? 94  LEU   I CD1 1 
ATOM   15482 C  CD2 . LEU   I  9  95  ? 58.084  -124.846 27.494  1.00 88.07  ? 94  LEU   I CD2 1 
ATOM   15483 N  N   . TYR   I  9  96  ? 56.773  -123.181 32.473  1.00 79.62  ? 95  TYR   I N   1 
ATOM   15484 C  CA  . TYR   I  9  96  ? 56.072  -123.422 33.761  1.00 80.22  ? 95  TYR   I CA  1 
ATOM   15485 C  C   . TYR   I  9  96  ? 54.787  -122.586 33.820  1.00 82.29  ? 95  TYR   I C   1 
ATOM   15486 O  O   . TYR   I  9  96  ? 53.855  -122.978 34.547  1.00 83.84  ? 95  TYR   I O   1 
ATOM   15487 C  CB  . TYR   I  9  96  ? 56.977  -123.149 34.966  1.00 80.42  ? 95  TYR   I CB  1 
ATOM   15488 C  CG  . TYR   I  9  96  ? 56.446  -123.767 36.232  1.00 81.78  ? 95  TYR   I CG  1 
ATOM   15489 C  CD1 . TYR   I  9  96  ? 56.708  -125.092 36.536  1.00 82.21  ? 95  TYR   I CD1 1 
ATOM   15490 C  CD2 . TYR   I  9  96  ? 55.624  -123.056 37.090  1.00 83.22  ? 95  TYR   I CD2 1 
ATOM   15491 C  CE1 . TYR   I  9  96  ? 56.198  -125.688 37.678  1.00 84.78  ? 95  TYR   I CE1 1 
ATOM   15492 C  CE2 . TYR   I  9  96  ? 55.105  -123.635 38.237  1.00 86.86  ? 95  TYR   I CE2 1 
ATOM   15493 C  CZ  . TYR   I  9  96  ? 55.392  -124.958 38.531  1.00 87.01  ? 95  TYR   I CZ  1 
ATOM   15494 O  OH  . TYR   I  9  96  ? 54.889  -125.550 39.654  1.00 87.72  ? 95  TYR   I OH  1 
ATOM   15495 N  N   . GLU   I  9  97  ? 54.737  -121.475 33.077  1.00 86.34  ? 96  GLU   I N   1 
ATOM   15496 C  CA  . GLU   I  9  97  ? 53.536  -120.603 32.954  1.00 91.67  ? 96  GLU   I CA  1 
ATOM   15497 C  C   . GLU   I  9  97  ? 52.358  -121.436 32.437  1.00 91.06  ? 96  GLU   I C   1 
ATOM   15498 O  O   . GLU   I  9  97  ? 51.208  -121.094 32.768  1.00 94.38  ? 96  GLU   I O   1 
ATOM   15499 C  CB  . GLU   I  9  97  ? 53.830  -119.420 32.030  1.00 95.84  ? 96  GLU   I CB  1 
ATOM   15500 C  CG  . GLU   I  9  97  ? 52.717  -118.390 31.980  1.00 99.02  ? 96  GLU   I CG  1 
ATOM   15501 C  CD  . GLU   I  9  97  ? 53.123  -117.074 31.343  1.00 101.84 ? 96  GLU   I CD  1 
ATOM   15502 O  OE1 . GLU   I  9  97  ? 52.613  -116.028 31.785  1.00 106.89 ? 96  GLU   I OE1 1 
ATOM   15503 O  OE2 . GLU   I  9  97  ? 53.951  -117.100 30.409  1.00 103.29 ? 96  GLU   I OE2 1 
ATOM   15504 N  N   . ARG   I  9  98  ? 52.643  -122.481 31.653  1.00 93.14  ? 97  ARG   I N   1 
ATOM   15505 C  CA  . ARG   I  9  98  ? 51.643  -123.445 31.120  1.00 94.44  ? 97  ARG   I CA  1 
ATOM   15506 C  C   . ARG   I  9  98  ? 51.776  -124.769 31.883  1.00 91.96  ? 97  ARG   I C   1 
ATOM   15507 O  O   . ARG   I  9  98  ? 51.845  -125.824 31.229  1.00 93.55  ? 97  ARG   I O   1 
ATOM   15508 C  CB  . ARG   I  9  98  ? 51.855  -123.630 29.613  1.00 96.66  ? 97  ARG   I CB  1 
ATOM   15509 C  CG  . ARG   I  9  98  ? 51.441  -122.432 28.771  1.00 102.81 ? 97  ARG   I CG  1 
ATOM   15510 C  CD  . ARG   I  9  98  ? 49.959  -122.451 28.447  1.00 110.00 ? 97  ARG   I CD  1 
ATOM   15511 N  NE  . ARG   I  9  98  ? 49.473  -121.153 27.991  1.00 118.53 ? 97  ARG   I NE  1 
ATOM   15512 C  CZ  . ARG   I  9  98  ? 48.996  -120.180 28.774  1.00 125.52 ? 97  ARG   I CZ  1 
ATOM   15513 N  NH1 . ARG   I  9  98  ? 48.926  -120.333 30.088  1.00 121.79 ? 97  ARG   I NH1 1 
ATOM   15514 N  NH2 . ARG   I  9  98  ? 48.586  -119.045 28.230  1.00 126.83 ? 97  ARG   I NH2 1 
ATOM   15515 N  N   . ARG   I  9  99  ? 51.804  -124.717 33.218  1.00 92.41  ? 98  ARG   I N   1 
ATOM   15516 C  CA  . ARG   I  9  99  ? 52.079  -125.894 34.090  1.00 89.87  ? 98  ARG   I CA  1 
ATOM   15517 C  C   . ARG   I  9  99  ? 50.999  -126.970 33.904  1.00 86.26  ? 98  ARG   I C   1 
ATOM   15518 O  O   . ARG   I  9  99  ? 51.366  -128.146 33.859  1.00 85.35  ? 98  ARG   I O   1 
ATOM   15519 C  CB  . ARG   I  9  99  ? 52.180  -125.479 35.562  1.00 92.87  ? 98  ARG   I CB  1 
ATOM   15520 C  CG  . ARG   I  9  99  ? 52.197  -126.640 36.548  1.00 95.13  ? 98  ARG   I CG  1 
ATOM   15521 C  CD  . ARG   I  9  99  ? 53.348  -127.603 36.310  1.00 93.79  ? 98  ARG   I CD  1 
ATOM   15522 N  NE  . ARG   I  9  99  ? 53.365  -128.709 37.263  1.00 95.60  ? 98  ARG   I NE  1 
ATOM   15523 C  CZ  . ARG   I  9  99  ? 52.813  -129.907 37.075  1.00 93.57  ? 98  ARG   I CZ  1 
ATOM   15524 N  NH1 . ARG   I  9  99  ? 52.893  -130.821 38.027  1.00 95.71  ? 98  ARG   I NH1 1 
ATOM   15525 N  NH2 . ARG   I  9  99  ? 52.184  -130.200 35.950  1.00 91.64  ? 98  ARG   I NH2 1 
ATOM   15526 N  N   . PHE   I  9  100 ? 49.718  -126.601 33.824  1.00 84.27  ? 99  PHE   I N   1 
ATOM   15527 C  CA  . PHE   I  9  100 ? 48.588  -127.567 33.749  1.00 87.18  ? 99  PHE   I CA  1 
ATOM   15528 C  C   . PHE   I  9  100 ? 47.933  -127.520 32.362  1.00 87.85  ? 99  PHE   I C   1 
ATOM   15529 O  O   . PHE   I  9  100 ? 46.719  -127.782 32.255  1.00 92.93  ? 99  PHE   I O   1 
ATOM   15530 C  CB  . PHE   I  9  100 ? 47.601  -127.309 34.889  1.00 89.06  ? 99  PHE   I CB  1 
ATOM   15531 C  CG  . PHE   I  9  100 ? 48.217  -127.422 36.260  1.00 93.67  ? 99  PHE   I CG  1 
ATOM   15532 C  CD1 . PHE   I  9  100 ? 48.649  -128.648 36.745  1.00 95.48  ? 99  PHE   I CD1 1 
ATOM   15533 C  CD2 . PHE   I  9  100 ? 48.377  -126.303 37.063  1.00 94.78  ? 99  PHE   I CD2 1 
ATOM   15534 C  CE1 . PHE   I  9  100 ? 49.224  -128.752 38.002  1.00 98.08  ? 99  PHE   I CE1 1 
ATOM   15535 C  CE2 . PHE   I  9  100 ? 48.951  -126.409 38.320  1.00 97.62  ? 99  PHE   I CE2 1 
ATOM   15536 C  CZ  . PHE   I  9  100 ? 49.374  -127.632 38.788  1.00 98.03  ? 99  PHE   I CZ  1 
ATOM   15537 N  N   . GLY   I  9  101 ? 48.726  -127.213 31.332  1.00 89.21  ? 100 GLY   I N   1 
ATOM   15538 C  CA  . GLY   I  9  101 ? 48.332  -127.271 29.910  1.00 90.96  ? 100 GLY   I CA  1 
ATOM   15539 C  C   . GLY   I  9  101 ? 49.549  -127.075 29.010  1.00 89.58  ? 100 GLY   I C   1 
ATOM   15540 O  O   . GLY   I  9  101 ? 49.573  -126.180 28.165  1.00 90.33  ? 100 GLY   I O   1 
ATOM   15541 N  N   . PRO   I  9  102 ? 50.593  -127.920 29.169  1.00 88.09  ? 101 PRO   I N   1 
ATOM   15542 C  CA  . PRO   I  9  102 ? 51.934  -127.588 28.692  1.00 85.77  ? 101 PRO   I CA  1 
ATOM   15543 C  C   . PRO   I  9  102 ? 52.150  -127.741 27.183  1.00 85.56  ? 101 PRO   I C   1 
ATOM   15544 O  O   . PRO   I  9  102 ? 51.387  -128.438 26.535  1.00 80.95  ? 101 PRO   I O   1 
ATOM   15545 C  CB  . PRO   I  9  102 ? 52.821  -128.602 29.427  1.00 84.96  ? 101 PRO   I CB  1 
ATOM   15546 C  CG  . PRO   I  9  102 ? 51.927  -129.807 29.622  1.00 85.69  ? 101 PRO   I CG  1 
ATOM   15547 C  CD  . PRO   I  9  102 ? 50.532  -129.245 29.805  1.00 87.26  ? 101 PRO   I CD  1 
ATOM   15548 N  N   . TYR   I  9  103 ? 53.192  -127.072 26.684  1.00 86.08  ? 102 TYR   I N   1 
ATOM   15549 C  CA  . TYR   I  9  103 ? 53.795  -127.315 25.351  1.00 87.16  ? 102 TYR   I CA  1 
ATOM   15550 C  C   . TYR   I  9  103 ? 54.521  -128.661 25.423  1.00 81.88  ? 102 TYR   I C   1 
ATOM   15551 O  O   . TYR   I  9  103 ? 55.308  -128.850 26.365  1.00 80.76  ? 102 TYR   I O   1 
ATOM   15552 C  CB  . TYR   I  9  103 ? 54.742  -126.175 24.957  1.00 90.64  ? 102 TYR   I CB  1 
ATOM   15553 C  CG  . TYR   I  9  103 ? 54.104  -124.810 24.861  1.00 95.19  ? 102 TYR   I CG  1 
ATOM   15554 C  CD1 . TYR   I  9  103 ? 53.226  -124.501 23.834  1.00 99.40  ? 102 TYR   I CD1 1 
ATOM   15555 C  CD2 . TYR   I  9  103 ? 54.388  -123.819 25.787  1.00 95.11  ? 102 TYR   I CD2 1 
ATOM   15556 C  CE1 . TYR   I  9  103 ? 52.639  -123.250 23.735  1.00 102.78 ? 102 TYR   I CE1 1 
ATOM   15557 C  CE2 . TYR   I  9  103 ? 53.809  -122.563 25.704  1.00 99.18  ? 102 TYR   I CE2 1 
ATOM   15558 C  CZ  . TYR   I  9  103 ? 52.932  -122.276 24.673  1.00 101.90 ? 102 TYR   I CZ  1 
ATOM   15559 O  OH  . TYR   I  9  103 ? 52.359  -121.040 24.583  1.00 107.70 ? 102 TYR   I OH  1 
ATOM   15560 N  N   . PHE   I  9  104 ? 54.234  -129.568 24.485  1.00 82.01  ? 103 PHE   I N   1 
ATOM   15561 C  CA  . PHE   I  9  104 ? 54.778  -130.953 24.445  1.00 80.50  ? 103 PHE   I CA  1 
ATOM   15562 C  C   . PHE   I  9  104 ? 56.117  -130.933 23.706  1.00 79.78  ? 103 PHE   I C   1 
ATOM   15563 O  O   . PHE   I  9  104 ? 56.191  -131.376 22.543  1.00 79.00  ? 103 PHE   I O   1 
ATOM   15564 C  CB  . PHE   I  9  104 ? 53.756  -131.903 23.819  1.00 80.56  ? 103 PHE   I CB  1 
ATOM   15565 C  CG  . PHE   I  9  104 ? 52.484  -132.022 24.617  1.00 80.12  ? 103 PHE   I CG  1 
ATOM   15566 C  CD1 . PHE   I  9  104 ? 52.461  -132.743 25.801  1.00 80.20  ? 103 PHE   I CD1 1 
ATOM   15567 C  CD2 . PHE   I  9  104 ? 51.316  -131.401 24.200  1.00 82.13  ? 103 PHE   I CD2 1 
ATOM   15568 C  CE1 . PHE   I  9  104 ? 51.295  -132.852 26.543  1.00 81.64  ? 103 PHE   I CE1 1 
ATOM   15569 C  CE2 . PHE   I  9  104 ? 50.151  -131.508 24.946  1.00 83.80  ? 103 PHE   I CE2 1 
ATOM   15570 C  CZ  . PHE   I  9  104 ? 50.143  -132.233 26.116  1.00 82.89  ? 103 PHE   I CZ  1 
ATOM   15571 N  N   . VAL   I  9  105 ? 57.148  -130.428 24.388  1.00 78.49  ? 104 VAL   I N   1 
ATOM   15572 C  CA  . VAL   I  9  105 ? 58.460  -130.057 23.784  1.00 81.34  ? 104 VAL   I CA  1 
ATOM   15573 C  C   . VAL   I  9  105 ? 59.598  -130.557 24.680  1.00 78.39  ? 104 VAL   I C   1 
ATOM   15574 O  O   . VAL   I  9  105 ? 59.354  -130.819 25.876  1.00 75.28  ? 104 VAL   I O   1 
ATOM   15575 C  CB  . VAL   I  9  105 ? 58.544  -128.534 23.560  1.00 82.69  ? 104 VAL   I CB  1 
ATOM   15576 C  CG1 . VAL   I  9  105 ? 57.548  -128.072 22.505  1.00 84.01  ? 104 VAL   I CG1 1 
ATOM   15577 C  CG2 . VAL   I  9  105 ? 58.350  -127.756 24.855  1.00 82.25  ? 104 VAL   I CG2 1 
ATOM   15578 N  N   . GLY   I  9  106 ? 60.794  -130.683 24.099  1.00 81.36  ? 105 GLY   I N   1 
ATOM   15579 C  CA  . GLY   I  9  106 ? 62.053  -130.997 24.801  1.00 83.30  ? 105 GLY   I CA  1 
ATOM   15580 C  C   . GLY   I  9  106 ? 63.157  -130.029 24.386  1.00 83.84  ? 105 GLY   I C   1 
ATOM   15581 O  O   . GLY   I  9  106 ? 64.052  -130.393 23.626  1.00 85.24  ? 105 GLY   I O   1 
ATOM   15582 N  N   . PRO   I  9  107 ? 63.118  -128.763 24.860  1.00 82.84  ? 106 PRO   I N   1 
ATOM   15583 C  CA  . PRO   I  9  107 ? 64.048  -127.742 24.385  1.00 83.37  ? 106 PRO   I CA  1 
ATOM   15584 C  C   . PRO   I  9  107 ? 65.469  -127.934 24.937  1.00 82.75  ? 106 PRO   I C   1 
ATOM   15585 O  O   . PRO   I  9  107 ? 65.623  -128.523 25.991  1.00 78.71  ? 106 PRO   I O   1 
ATOM   15586 C  CB  . PRO   I  9  107 ? 63.426  -126.415 24.849  1.00 83.55  ? 106 PRO   I CB  1 
ATOM   15587 C  CG  . PRO   I  9  107 ? 62.508  -126.777 26.002  1.00 83.04  ? 106 PRO   I CG  1 
ATOM   15588 C  CD  . PRO   I  9  107 ? 62.183  -128.252 25.872  1.00 82.76  ? 106 PRO   I CD  1 
ATOM   15589 N  N   . VAL   I  9  108 ? 66.460  -127.445 24.184  1.00 85.10  ? 107 VAL   I N   1 
ATOM   15590 C  CA  . VAL   I  9  108 ? 67.915  -127.489 24.515  1.00 89.21  ? 107 VAL   I CA  1 
ATOM   15591 C  C   . VAL   I  9  108 ? 68.522  -126.123 24.180  1.00 90.50  ? 107 VAL   I C   1 
ATOM   15592 O  O   . VAL   I  9  108 ? 68.494  -125.748 22.992  1.00 93.97  ? 107 VAL   I O   1 
ATOM   15593 C  CB  . VAL   I  9  108 ? 68.635  -128.610 23.740  1.00 88.47  ? 107 VAL   I CB  1 
ATOM   15594 C  CG1 . VAL   I  9  108 ? 70.133  -128.619 24.009  1.00 88.51  ? 107 VAL   I CG1 1 
ATOM   15595 C  CG2 . VAL   I  9  108 ? 68.033  -129.972 24.037  1.00 90.74  ? 107 VAL   I CG2 1 
ATOM   15596 N  N   . VAL   I  9  109 ? 69.051  -125.421 25.186  1.00 92.70  ? 108 VAL   I N   1 
ATOM   15597 C  CA  . VAL   I  9  109 ? 69.820  -124.154 25.010  1.00 92.12  ? 108 VAL   I CA  1 
ATOM   15598 C  C   . VAL   I  9  109 ? 71.299  -124.507 24.842  1.00 91.44  ? 108 VAL   I C   1 
ATOM   15599 O  O   . VAL   I  9  109 ? 71.776  -125.415 25.546  1.00 87.75  ? 108 VAL   I O   1 
ATOM   15600 C  CB  . VAL   I  9  109 ? 69.601  -123.183 26.184  1.00 95.59  ? 108 VAL   I CB  1 
ATOM   15601 C  CG1 . VAL   I  9  109 ? 70.621  -122.052 26.186  1.00 98.72  ? 108 VAL   I CG1 1 
ATOM   15602 C  CG2 . VAL   I  9  109 ? 68.186  -122.627 26.177  1.00 98.81  ? 108 VAL   I CG2 1 
ATOM   15603 N  N   . ALA   I  9  110 ? 71.979  -123.809 23.933  1.00 91.97  ? 109 ALA   I N   1 
ATOM   15604 C  CA  . ALA   I  9  110 ? 73.429  -123.934 23.668  1.00 95.62  ? 109 ALA   I CA  1 
ATOM   15605 C  C   . ALA   I  9  110 ? 73.965  -122.571 23.221  1.00 96.09  ? 109 ALA   I C   1 
ATOM   15606 O  O   . ALA   I  9  110 ? 73.253  -121.873 22.475  1.00 95.19  ? 109 ALA   I O   1 
ATOM   15607 C  CB  . ALA   I  9  110 ? 73.673  -124.998 22.626  1.00 97.46  ? 109 ALA   I CB  1 
ATOM   15608 N  N   . GLY   I  9  111 ? 75.164  -122.203 23.674  1.00 98.83  ? 110 GLY   I N   1 
ATOM   15609 C  CA  . GLY   I  9  111 ? 75.822  -120.941 23.285  1.00 100.71 ? 110 GLY   I CA  1 
ATOM   15610 C  C   . GLY   I  9  111 ? 76.999  -120.609 24.182  1.00 101.72 ? 110 GLY   I C   1 
ATOM   15611 O  O   . GLY   I  9  111 ? 77.230  -121.348 25.160  1.00 104.72 ? 110 GLY   I O   1 
ATOM   15612 N  N   . ILE   I  9  112 ? 77.715  -119.529 23.857  1.00 102.95 ? 111 ILE   I N   1 
ATOM   15613 C  CA  . ILE   I  9  112 ? 78.906  -119.042 24.615  1.00 103.67 ? 111 ILE   I CA  1 
ATOM   15614 C  C   . ILE   I  9  112 ? 78.586  -117.652 25.168  1.00 108.25 ? 111 ILE   I C   1 
ATOM   15615 O  O   . ILE   I  9  112 ? 78.298  -116.747 24.356  1.00 110.43 ? 111 ILE   I O   1 
ATOM   15616 C  CB  . ILE   I  9  112 ? 80.163  -119.018 23.725  1.00 100.93 ? 111 ILE   I CB  1 
ATOM   15617 C  CG1 . ILE   I  9  112 ? 80.512  -120.411 23.199  1.00 100.08 ? 111 ILE   I CG1 1 
ATOM   15618 C  CG2 . ILE   I  9  112 ? 81.336  -118.395 24.463  1.00 99.87  ? 111 ILE   I CG2 1 
ATOM   15619 C  CD1 . ILE   I  9  112 ? 81.206  -120.396 21.862  1.00 102.49 ? 111 ILE   I CD1 1 
ATOM   15620 N  N   . ASN   I  9  113 ? 78.643  -117.502 26.495  1.00 111.82 ? 112 ASN   I N   1 
ATOM   15621 C  CA  . ASN   I  9  113 ? 78.522  -116.199 27.200  1.00 112.26 ? 112 ASN   I CA  1 
ATOM   15622 C  C   . ASN   I  9  113 ? 79.585  -115.249 26.636  1.00 114.44 ? 112 ASN   I C   1 
ATOM   15623 O  O   . ASN   I  9  113 ? 80.785  -115.559 26.767  1.00 113.26 ? 112 ASN   I O   1 
ATOM   15624 C  CB  . ASN   I  9  113 ? 78.658  -116.359 28.716  1.00 111.59 ? 112 ASN   I CB  1 
ATOM   15625 C  CG  . ASN   I  9  113 ? 78.290  -115.106 29.483  1.00 110.96 ? 112 ASN   I CG  1 
ATOM   15626 O  OD1 . ASN   I  9  113 ? 78.967  -114.084 29.379  1.00 106.12 ? 112 ASN   I OD1 1 
ATOM   15627 N  ND2 . ASN   I  9  113 ? 77.225  -115.176 30.264  1.00 112.63 ? 112 ASN   I ND2 1 
ATOM   15628 N  N   . SER   I  9  114 ? 79.153  -114.145 26.022  1.00 114.45 ? 113 SER   I N   1 
ATOM   15629 C  CA  . SER   I  9  114 ? 80.025  -113.185 25.295  1.00 111.39 ? 113 SER   I CA  1 
ATOM   15630 C  C   . SER   I  9  114 ? 80.930  -112.429 26.277  1.00 114.89 ? 113 SER   I C   1 
ATOM   15631 O  O   . SER   I  9  114 ? 82.015  -111.992 25.846  1.00 114.90 ? 113 SER   I O   1 
ATOM   15632 C  CB  . SER   I  9  114 ? 79.201  -112.243 24.460  1.00 107.54 ? 113 SER   I CB  1 
ATOM   15633 O  OG  . SER   I  9  114 ? 78.394  -111.418 25.283  1.00 106.03 ? 113 SER   I OG  1 
ATOM   15634 N  N   . LYS   I  9  115 ? 80.514  -112.291 27.542  1.00 115.91 ? 114 LYS   I N   1 
ATOM   15635 C  CA  . LYS   I  9  115 ? 81.270  -111.546 28.587  1.00 119.99 ? 114 LYS   I CA  1 
ATOM   15636 C  C   . LYS   I  9  115 ? 82.365  -112.448 29.172  1.00 119.93 ? 114 LYS   I C   1 
ATOM   15637 O  O   . LYS   I  9  115 ? 83.529  -112.001 29.215  1.00 119.83 ? 114 LYS   I O   1 
ATOM   15638 C  CB  . LYS   I  9  115 ? 80.334  -111.031 29.687  1.00 120.28 ? 114 LYS   I CB  1 
ATOM   15639 C  CG  . LYS   I  9  115 ? 80.781  -109.736 30.354  1.00 121.43 ? 114 LYS   I CG  1 
ATOM   15640 C  CD  . LYS   I  9  115 ? 80.445  -108.502 29.542  1.00 121.77 ? 114 LYS   I CD  1 
ATOM   15641 C  CE  . LYS   I  9  115 ? 81.142  -107.249 30.027  1.00 125.82 ? 114 LYS   I CE  1 
ATOM   15642 N  NZ  . LYS   I  9  115 ? 80.638  -106.812 31.350  1.00 126.64 ? 114 LYS   I NZ  1 
ATOM   15643 N  N   . SER   I  9  116 ? 82.009  -113.666 29.599  1.00 119.67 ? 115 SER   I N   1 
ATOM   15644 C  CA  . SER   I  9  116 ? 82.907  -114.610 30.320  1.00 119.90 ? 115 SER   I CA  1 
ATOM   15645 C  C   . SER   I  9  116 ? 83.684  -115.500 29.336  1.00 118.83 ? 115 SER   I C   1 
ATOM   15646 O  O   . SER   I  9  116 ? 84.813  -115.901 29.681  1.00 121.34 ? 115 SER   I O   1 
ATOM   15647 C  CB  . SER   I  9  116 ? 82.134  -115.433 31.323  1.00 119.48 ? 115 SER   I CB  1 
ATOM   15648 O  OG  . SER   I  9  116 ? 81.299  -116.383 30.681  1.00 119.49 ? 115 SER   I OG  1 
ATOM   15649 N  N   . GLY   I  9  117 ? 83.107  -115.802 28.166  1.00 115.39 ? 116 GLY   I N   1 
ATOM   15650 C  CA  . GLY   I  9  117 ? 83.700  -116.700 27.154  1.00 114.82 ? 116 GLY   I CA  1 
ATOM   15651 C  C   . GLY   I  9  117 ? 83.477  -118.170 27.481  1.00 112.52 ? 116 GLY   I C   1 
ATOM   15652 O  O   . GLY   I  9  117 ? 84.089  -119.020 26.803  1.00 106.73 ? 116 GLY   I O   1 
ATOM   15653 N  N   . LYS   I  9  118 ? 82.624  -118.463 28.470  1.00 113.05 ? 117 LYS   I N   1 
ATOM   15654 C  CA  . LYS   I  9  118 ? 82.338  -119.838 28.962  1.00 114.44 ? 117 LYS   I CA  1 
ATOM   15655 C  C   . LYS   I  9  118 ? 81.309  -120.506 28.056  1.00 111.38 ? 117 LYS   I C   1 
ATOM   15656 O  O   . LYS   I  9  118 ? 80.281  -119.909 27.740  1.00 111.00 ? 117 LYS   I O   1 
ATOM   15657 C  CB  . LYS   I  9  118 ? 81.820  -119.811 30.403  1.00 119.59 ? 117 LYS   I CB  1 
ATOM   15658 C  CG  . LYS   I  9  118 ? 82.895  -119.628 31.464  1.00 125.97 ? 117 LYS   I CG  1 
ATOM   15659 C  CD  . LYS   I  9  118 ? 82.351  -119.226 32.817  1.00 128.36 ? 117 LYS   I CD  1 
ATOM   15660 C  CE  . LYS   I  9  118 ? 83.443  -118.926 33.822  1.00 131.58 ? 117 LYS   I CE  1 
ATOM   15661 N  NZ  . LYS   I  9  118 ? 84.109  -120.162 34.295  1.00 132.29 ? 117 LYS   I NZ  1 
ATOM   15662 N  N   . PRO   I  9  119 ? 81.562  -121.757 27.604  1.00 108.50 ? 118 PRO   I N   1 
ATOM   15663 C  CA  . PRO   I  9  119 ? 80.544  -122.557 26.925  1.00 103.48 ? 118 PRO   I CA  1 
ATOM   15664 C  C   . PRO   I  9  119 ? 79.429  -122.974 27.897  1.00 99.91  ? 118 PRO   I C   1 
ATOM   15665 O  O   . PRO   I  9  119 ? 79.749  -123.343 29.012  1.00 97.40  ? 118 PRO   I O   1 
ATOM   15666 C  CB  . PRO   I  9  119 ? 81.306  -123.792 26.417  1.00 106.87 ? 118 PRO   I CB  1 
ATOM   15667 C  CG  . PRO   I  9  119 ? 82.772  -123.426 26.525  1.00 109.64 ? 118 PRO   I CG  1 
ATOM   15668 C  CD  . PRO   I  9  119 ? 82.853  -122.455 27.681  1.00 109.49 ? 118 PRO   I CD  1 
ATOM   15669 N  N   . PHE   I  9  120 ? 78.169  -122.910 27.451  1.00 98.26  ? 119 PHE   I N   1 
ATOM   15670 C  CA  . PHE   I  9  120 ? 76.960  -123.190 28.272  1.00 98.30  ? 119 PHE   I CA  1 
ATOM   15671 C  C   . PHE   I  9  120 ? 75.924  -123.987 27.469  1.00 99.91  ? 119 PHE   I C   1 
ATOM   15672 O  O   . PHE   I  9  120 ? 75.499  -123.516 26.392  1.00 97.61  ? 119 PHE   I O   1 
ATOM   15673 C  CB  . PHE   I  9  120 ? 76.328  -121.887 28.764  1.00 97.13  ? 119 PHE   I CB  1 
ATOM   15674 C  CG  . PHE   I  9  120 ? 75.146  -122.089 29.677  1.00 94.98  ? 119 PHE   I CG  1 
ATOM   15675 C  CD1 . PHE   I  9  120 ? 73.864  -122.228 29.166  1.00 93.74  ? 119 PHE   I CD1 1 
ATOM   15676 C  CD2 . PHE   I  9  120 ? 75.320  -122.159 31.051  1.00 96.45  ? 119 PHE   I CD2 1 
ATOM   15677 C  CE1 . PHE   I  9  120 ? 72.781  -122.420 30.011  1.00 93.20  ? 119 PHE   I CE1 1 
ATOM   15678 C  CE2 . PHE   I  9  120 ? 74.237  -122.352 31.894  1.00 96.36  ? 119 PHE   I CE2 1 
ATOM   15679 C  CZ  . PHE   I  9  120 ? 72.969  -122.481 31.373  1.00 94.37  ? 119 PHE   I CZ  1 
ATOM   15680 N  N   . ILE   I  9  121 ? 75.510  -125.140 28.007  1.00 95.94  ? 120 ILE   I N   1 
ATOM   15681 C  CA  . ILE   I  9  121 ? 74.372  -125.964 27.498  1.00 94.92  ? 120 ILE   I CA  1 
ATOM   15682 C  C   . ILE   I  9  121 ? 73.403  -126.232 28.653  1.00 91.98  ? 120 ILE   I C   1 
ATOM   15683 O  O   . ILE   I  9  121 ? 73.855  -126.257 29.815  1.00 91.46  ? 120 ILE   I O   1 
ATOM   15684 C  CB  . ILE   I  9  121 ? 74.860  -127.279 26.857  1.00 94.27  ? 120 ILE   I CB  1 
ATOM   15685 C  CG1 . ILE   I  9  121 ? 75.732  -128.096 27.814  1.00 95.60  ? 120 ILE   I CG1 1 
ATOM   15686 C  CG2 . ILE   I  9  121 ? 75.572  -126.996 25.544  1.00 97.81  ? 120 ILE   I CG2 1 
ATOM   15687 C  CD1 . ILE   I  9  121 ? 75.936  -129.527 27.386  1.00 97.38  ? 120 ILE   I CD1 1 
ATOM   15688 N  N   . ALA   I  9  122 ? 72.121  -126.424 28.332  1.00 89.54  ? 121 ALA   I N   1 
ATOM   15689 C  CA  . ALA   I  9  122 ? 71.045  -126.736 29.299  1.00 92.83  ? 121 ALA   I CA  1 
ATOM   15690 C  C   . ALA   I  9  122 ? 69.897  -127.456 28.584  1.00 92.43  ? 121 ALA   I C   1 
ATOM   15691 O  O   . ALA   I  9  122 ? 69.687  -127.199 27.382  1.00 95.70  ? 121 ALA   I O   1 
ATOM   15692 C  CB  . ALA   I  9  122 ? 70.568  -125.470 29.969  1.00 95.12  ? 121 ALA   I CB  1 
ATOM   15693 N  N   . GLY   I  9  123 ? 69.199  -128.331 29.311  1.00 92.61  ? 122 GLY   I N   1 
ATOM   15694 C  CA  . GLY   I  9  123 ? 68.004  -129.058 28.842  1.00 92.74  ? 122 GLY   I CA  1 
ATOM   15695 C  C   . GLY   I  9  123 ? 66.827  -128.825 29.770  1.00 90.90  ? 122 GLY   I C   1 
ATOM   15696 O  O   . GLY   I  9  123 ? 67.061  -128.514 30.949  1.00 93.46  ? 122 GLY   I O   1 
ATOM   15697 N  N   . PHE   I  9  124 ? 65.605  -128.959 29.255  1.00 90.29  ? 123 PHE   I N   1 
ATOM   15698 C  CA  . PHE   I  9  124 ? 64.344  -128.767 30.015  1.00 92.23  ? 123 PHE   I CA  1 
ATOM   15699 C  C   . PHE   I  9  124 ? 63.407  -129.942 29.743  1.00 91.03  ? 123 PHE   I C   1 
ATOM   15700 O  O   . PHE   I  9  124 ? 63.471  -130.506 28.635  1.00 91.34  ? 123 PHE   I O   1 
ATOM   15701 C  CB  . PHE   I  9  124 ? 63.647  -127.464 29.614  1.00 94.33  ? 123 PHE   I CB  1 
ATOM   15702 C  CG  . PHE   I  9  124 ? 64.558  -126.277 29.434  1.00 97.52  ? 123 PHE   I CG  1 
ATOM   15703 C  CD1 . PHE   I  9  124 ? 65.329  -126.141 28.290  1.00 98.07  ? 123 PHE   I CD1 1 
ATOM   15704 C  CD2 . PHE   I  9  124 ? 64.631  -125.288 30.401  1.00 101.01 ? 123 PHE   I CD2 1 
ATOM   15705 C  CE1 . PHE   I  9  124 ? 66.161  -125.047 28.120  1.00 100.60 ? 123 PHE   I CE1 1 
ATOM   15706 C  CE2 . PHE   I  9  124 ? 65.461  -124.191 30.228  1.00 105.60 ? 123 PHE   I CE2 1 
ATOM   15707 C  CZ  . PHE   I  9  124 ? 66.224  -124.072 29.089  1.00 104.20 ? 123 PHE   I CZ  1 
ATOM   15708 N  N   . ASP   I  9  125 ? 62.563  -130.283 30.720  1.00 92.12  ? 124 ASP   I N   1 
ATOM   15709 C  CA  . ASP   I  9  125 ? 61.361  -131.134 30.513  1.00 96.08  ? 124 ASP   I CA  1 
ATOM   15710 C  C   . ASP   I  9  125 ? 60.245  -130.228 29.981  1.00 93.28  ? 124 ASP   I C   1 
ATOM   15711 O  O   . ASP   I  9  125 ? 60.424  -128.995 30.016  1.00 90.99  ? 124 ASP   I O   1 
ATOM   15712 C  CB  . ASP   I  9  125 ? 60.970  -131.898 31.785  1.00 99.14  ? 124 ASP   I CB  1 
ATOM   15713 C  CG  . ASP   I  9  125 ? 60.655  -131.029 32.993  1.00 103.11 ? 124 ASP   I CG  1 
ATOM   15714 O  OD1 . ASP   I  9  125 ? 60.605  -129.793 32.831  1.00 109.00 ? 124 ASP   I OD1 1 
ATOM   15715 O  OD2 . ASP   I  9  125 ? 60.465  -131.597 34.094  1.00 96.99  ? 124 ASP   I OD2 1 
ATOM   15716 N  N   . LEU   I  9  126 ? 59.137  -130.812 29.519  1.00 96.75  ? 125 LEU   I N   1 
ATOM   15717 C  CA  . LEU   I  9  126 ? 58.008  -130.073 28.887  1.00 95.03  ? 125 LEU   I CA  1 
ATOM   15718 C  C   . LEU   I  9  126 ? 57.437  -129.031 29.863  1.00 96.64  ? 125 LEU   I C   1 
ATOM   15719 O  O   . LEU   I  9  126 ? 56.675  -128.151 29.403  1.00 98.88  ? 125 LEU   I O   1 
ATOM   15720 C  CB  . LEU   I  9  126 ? 56.934  -131.068 28.424  1.00 93.59  ? 125 LEU   I CB  1 
ATOM   15721 C  CG  . LEU   I  9  126 ? 55.925  -131.538 29.473  1.00 91.91  ? 125 LEU   I CG  1 
ATOM   15722 C  CD1 . LEU   I  9  126 ? 54.716  -132.172 28.800  1.00 93.54  ? 125 LEU   I CD1 1 
ATOM   15723 C  CD2 . LEU   I  9  126 ? 56.559  -132.511 30.454  1.00 89.47  ? 125 LEU   I CD2 1 
ATOM   15724 N  N   . ILE   I  9  127 ? 57.800  -129.111 31.149  1.00 92.35  ? 126 ILE   I N   1 
ATOM   15725 C  CA  . ILE   I  9  127 ? 57.170  -128.319 32.246  1.00 94.38  ? 126 ILE   I CA  1 
ATOM   15726 C  C   . ILE   I  9  127 ? 58.178  -127.335 32.863  1.00 91.47  ? 126 ILE   I C   1 
ATOM   15727 O  O   . ILE   I  9  127 ? 57.785  -126.632 33.813  1.00 92.48  ? 126 ILE   I O   1 
ATOM   15728 C  CB  . ILE   I  9  127 ? 56.530  -129.278 33.274  1.00 94.11  ? 126 ILE   I CB  1 
ATOM   15729 C  CG1 . ILE   I  9  127 ? 55.188  -128.743 33.769  1.00 100.43 ? 126 ILE   I CG1 1 
ATOM   15730 C  CG2 . ILE   I  9  127 ? 57.466  -129.627 34.421  1.00 93.91  ? 126 ILE   I CG2 1 
ATOM   15731 C  CD1 . ILE   I  9  127 ? 54.070  -128.957 32.778  1.00 101.93 ? 126 ILE   I CD1 1 
ATOM   15732 N  N   . GLY   I  9  128 ? 59.411  -127.264 32.342  1.00 90.58  ? 127 GLY   I N   1 
ATOM   15733 C  CA  . GLY   I  9  128 ? 60.325  -126.122 32.558  1.00 91.72  ? 127 GLY   I CA  1 
ATOM   15734 C  C   . GLY   I  9  128 ? 61.559  -126.450 33.386  1.00 91.74  ? 127 GLY   I C   1 
ATOM   15735 O  O   . GLY   I  9  128 ? 62.426  -125.564 33.494  1.00 91.53  ? 127 GLY   I O   1 
ATOM   15736 N  N   . CYS   I  9  129 ? 61.659  -127.656 33.952  1.00 91.08  ? 128 CYS   I N   1 
ATOM   15737 C  CA  . CYS   I  9  129 ? 62.759  -128.054 34.876  1.00 92.59  ? 128 CYS   I CA  1 
ATOM   15738 C  C   . CYS   I  9  129 ? 64.112  -127.980 34.162  1.00 93.42  ? 128 CYS   I C   1 
ATOM   15739 O  O   . CYS   I  9  129 ? 64.352  -128.812 33.267  1.00 88.43  ? 128 CYS   I O   1 
ATOM   15740 C  CB  . CYS   I  9  129 ? 62.576  -129.467 35.415  1.00 94.20  ? 128 CYS   I CB  1 
ATOM   15741 S  SG  . CYS   I  9  129 ? 63.825  -129.918 36.648  1.00 96.43  ? 128 CYS   I SG  1 
ATOM   15742 N  N   . ILE   I  9  130 ? 64.969  -127.039 34.573  1.00 94.68  ? 129 ILE   I N   1 
ATOM   15743 C  CA  . ILE   I  9  130 ? 66.313  -126.806 33.963  1.00 95.44  ? 129 ILE   I CA  1 
ATOM   15744 C  C   . ILE   I  9  130 ? 67.226  -127.982 34.333  1.00 97.87  ? 129 ILE   I C   1 
ATOM   15745 O  O   . ILE   I  9  130 ? 67.281  -128.341 35.525  1.00 97.02  ? 129 ILE   I O   1 
ATOM   15746 C  CB  . ILE   I  9  130 ? 66.907  -125.447 34.393  1.00 96.26  ? 129 ILE   I CB  1 
ATOM   15747 C  CG1 . ILE   I  9  130 ? 65.990  -124.279 34.021  1.00 96.54  ? 129 ILE   I CG1 1 
ATOM   15748 C  CG2 . ILE   I  9  130 ? 68.301  -125.260 33.808  1.00 94.57  ? 129 ILE   I CG2 1 
ATOM   15749 C  CD1 . ILE   I  9  130 ? 66.243  -123.018 34.815  1.00 98.89  ? 129 ILE   I CD1 1 
ATOM   15750 N  N   . ASP   I  9  131 ? 67.894  -128.558 33.329  1.00 101.73 ? 130 ASP   I N   1 
ATOM   15751 C  CA  . ASP   I  9  131 ? 68.921  -129.627 33.458  1.00 108.32 ? 130 ASP   I CA  1 
ATOM   15752 C  C   . ASP   I  9  131 ? 70.228  -129.082 32.870  1.00 103.52 ? 130 ASP   I C   1 
ATOM   15753 O  O   . ASP   I  9  131 ? 70.367  -129.080 31.629  1.00 96.88  ? 130 ASP   I O   1 
ATOM   15754 C  CB  . ASP   I  9  131 ? 68.445  -130.924 32.791  1.00 113.11 ? 130 ASP   I CB  1 
ATOM   15755 C  CG  . ASP   I  9  131 ? 69.523  -131.969 32.529  1.00 116.17 ? 130 ASP   I CG  1 
ATOM   15756 O  OD1 . ASP   I  9  131 ? 70.511  -132.011 33.295  1.00 115.75 ? 130 ASP   I OD1 1 
ATOM   15757 O  OD2 . ASP   I  9  131 ? 69.359  -132.745 31.561  1.00 118.45 ? 130 ASP   I OD2 1 
ATOM   15758 N  N   . GLU   I  9  132 ? 71.133  -128.612 33.732  1.00 107.51 ? 131 GLU   I N   1 
ATOM   15759 C  CA  . GLU   I  9  132 ? 72.443  -128.029 33.340  1.00 112.82 ? 131 GLU   I CA  1 
ATOM   15760 C  C   . GLU   I  9  132 ? 73.481  -129.154 33.326  1.00 109.85 ? 131 GLU   I C   1 
ATOM   15761 O  O   . GLU   I  9  132 ? 73.409  -130.025 34.216  1.00 117.29 ? 131 GLU   I O   1 
ATOM   15762 C  CB  . GLU   I  9  132 ? 72.843  -126.917 34.310  1.00 117.05 ? 131 GLU   I CB  1 
ATOM   15763 C  CG  . GLU   I  9  132 ? 73.532  -125.745 33.637  1.00 125.11 ? 131 GLU   I CG  1 
ATOM   15764 C  CD  . GLU   I  9  132 ? 74.001  -124.659 34.593  1.00 133.12 ? 131 GLU   I CD  1 
ATOM   15765 O  OE1 . GLU   I  9  132 ? 73.204  -123.743 34.885  1.00 136.51 ? 131 GLU   I OE1 1 
ATOM   15766 O  OE2 . GLU   I  9  132 ? 75.159  -124.737 35.052  1.00 151.98 ? 131 GLU   I OE2 1 
ATOM   15767 N  N   . ALA   I  9  133 ? 74.398  -129.141 32.355  1.00 107.49 ? 132 ALA   I N   1 
ATOM   15768 C  CA  . ALA   I  9  133 ? 75.411  -130.203 32.154  1.00 106.49 ? 132 ALA   I CA  1 
ATOM   15769 C  C   . ALA   I  9  133 ? 76.738  -129.594 31.702  1.00 108.17 ? 132 ALA   I C   1 
ATOM   15770 O  O   . ALA   I  9  133 ? 76.715  -128.637 30.907  1.00 110.65 ? 132 ALA   I O   1 
ATOM   15771 C  CB  . ALA   I  9  133 ? 74.911  -131.210 31.150  1.00 106.29 ? 132 ALA   I CB  1 
ATOM   15772 N  N   . LYS   I  9  134 ? 77.845  -130.154 32.196  1.00 111.42 ? 133 LYS   I N   1 
ATOM   15773 C  CA  . LYS   I  9  134 ? 79.227  -129.834 31.757  1.00 115.84 ? 133 LYS   I CA  1 
ATOM   15774 C  C   . LYS   I  9  134 ? 79.460  -130.400 30.352  1.00 113.45 ? 133 LYS   I C   1 
ATOM   15775 O  O   . LYS   I  9  134 ? 80.138  -129.725 29.557  1.00 114.77 ? 133 LYS   I O   1 
ATOM   15776 C  CB  . LYS   I  9  134 ? 80.250  -130.432 32.727  1.00 123.65 ? 133 LYS   I CB  1 
ATOM   15777 C  CG  . LYS   I  9  134 ? 80.233  -129.854 34.134  1.00 131.05 ? 133 LYS   I CG  1 
ATOM   15778 C  CD  . LYS   I  9  134 ? 81.325  -130.425 35.013  1.00 136.50 ? 133 LYS   I CD  1 
ATOM   15779 C  CE  . LYS   I  9  134 ? 81.397  -129.770 36.376  1.00 137.67 ? 133 LYS   I CE  1 
ATOM   15780 N  NZ  . LYS   I  9  134 ? 82.796  -129.473 36.760  1.00 141.53 ? 133 LYS   I NZ  1 
ATOM   15781 N  N   . ASP   I  9  135 ? 78.904  -131.584 30.066  1.00 110.85 ? 134 ASP   I N   1 
ATOM   15782 C  CA  . ASP   I  9  135 ? 79.292  -132.438 28.909  1.00 110.62 ? 134 ASP   I CA  1 
ATOM   15783 C  C   . ASP   I  9  135 ? 78.251  -132.318 27.788  1.00 102.65 ? 134 ASP   I C   1 
ATOM   15784 O  O   . ASP   I  9  135 ? 78.570  -131.657 26.779  1.00 98.59  ? 134 ASP   I O   1 
ATOM   15785 C  CB  . ASP   I  9  135 ? 79.552  -133.886 29.344  1.00 112.62 ? 134 ASP   I CB  1 
ATOM   15786 C  CG  . ASP   I  9  135 ? 78.568  -134.459 30.355  1.00 113.40 ? 134 ASP   I CG  1 
ATOM   15787 O  OD1 . ASP   I  9  135 ? 77.428  -133.953 30.426  1.00 111.23 ? 134 ASP   I OD1 1 
ATOM   15788 O  OD2 . ASP   I  9  135 ? 78.952  -135.411 31.068  1.00 115.19 ? 134 ASP   I OD2 1 
ATOM   15789 N  N   . PHE   I  9  136 ? 77.069  -132.932 27.939  1.00 100.24 ? 135 PHE   I N   1 
ATOM   15790 C  CA  . PHE   I  9  136 ? 76.059  -133.064 26.853  1.00 97.65  ? 135 PHE   I CA  1 
ATOM   15791 C  C   . PHE   I  9  136 ? 74.628  -133.049 27.402  1.00 96.27  ? 135 PHE   I C   1 
ATOM   15792 O  O   . PHE   I  9  136 ? 74.393  -133.519 28.535  1.00 94.71  ? 135 PHE   I O   1 
ATOM   15793 C  CB  . PHE   I  9  136 ? 76.286  -134.349 26.053  1.00 98.21  ? 135 PHE   I CB  1 
ATOM   15794 C  CG  . PHE   I  9  136 ? 76.360  -135.602 26.886  1.00 98.10  ? 135 PHE   I CG  1 
ATOM   15795 C  CD1 . PHE   I  9  136 ? 75.215  -136.322 27.194  1.00 97.10  ? 135 PHE   I CD1 1 
ATOM   15796 C  CD2 . PHE   I  9  136 ? 77.578  -136.060 27.364  1.00 98.51  ? 135 PHE   I CD2 1 
ATOM   15797 C  CE1 . PHE   I  9  136 ? 75.288  -137.473 27.963  1.00 98.07  ? 135 PHE   I CE1 1 
ATOM   15798 C  CE2 . PHE   I  9  136 ? 77.649  -137.209 28.135  1.00 100.50 ? 135 PHE   I CE2 1 
ATOM   15799 C  CZ  . PHE   I  9  136 ? 76.505  -137.914 28.431  1.00 101.09 ? 135 PHE   I CZ  1 
ATOM   15800 N  N   . ILE   I  9  137 ? 73.708  -132.526 26.584  1.00 96.50  ? 136 ILE   I N   1 
ATOM   15801 C  CA  . ILE   I  9  137 ? 72.227  -132.592 26.762  1.00 96.25  ? 136 ILE   I CA  1 
ATOM   15802 C  C   . ILE   I  9  137 ? 71.655  -133.348 25.558  1.00 92.10  ? 136 ILE   I C   1 
ATOM   15803 O  O   . ILE   I  9  137 ? 72.186  -133.164 24.444  1.00 93.06  ? 136 ILE   I O   1 
ATOM   15804 C  CB  . ILE   I  9  137 ? 71.626  -131.175 26.900  1.00 95.56  ? 136 ILE   I CB  1 
ATOM   15805 C  CG1 . ILE   I  9  137 ? 72.169  -130.439 28.128  1.00 97.72  ? 136 ILE   I CG1 1 
ATOM   15806 C  CG2 . ILE   I  9  137 ? 70.104  -131.211 26.903  1.00 97.24  ? 136 ILE   I CG2 1 
ATOM   15807 C  CD1 . ILE   I  9  137 ? 71.879  -131.120 29.447  1.00 99.69  ? 136 ILE   I CD1 1 
ATOM   15808 N  N   . VAL   I  9  138 ? 70.624  -134.168 25.781  1.00 91.38  ? 137 VAL   I N   1 
ATOM   15809 C  CA  . VAL   I  9  138 ? 69.932  -134.959 24.720  1.00 91.43  ? 137 VAL   I CA  1 
ATOM   15810 C  C   . VAL   I  9  138 ? 68.425  -134.718 24.831  1.00 89.02  ? 137 VAL   I C   1 
ATOM   15811 O  O   . VAL   I  9  138 ? 67.951  -134.422 25.946  1.00 91.53  ? 137 VAL   I O   1 
ATOM   15812 C  CB  . VAL   I  9  138 ? 70.263  -136.460 24.823  1.00 92.55  ? 137 VAL   I CB  1 
ATOM   15813 C  CG1 . VAL   I  9  138 ? 71.762  -136.708 24.750  1.00 93.92  ? 137 VAL   I CG1 1 
ATOM   15814 C  CG2 . VAL   I  9  138 ? 69.677  -137.087 26.080  1.00 94.29  ? 137 VAL   I CG2 1 
ATOM   15815 N  N   . SER   I  9  139 ? 67.709  -134.858 23.714  1.00 88.50  ? 138 SER   I N   1 
ATOM   15816 C  CA  . SER   I  9  139 ? 66.246  -134.626 23.617  1.00 89.51  ? 138 SER   I CA  1 
ATOM   15817 C  C   . SER   I  9  139 ? 65.670  -135.395 22.425  1.00 88.99  ? 138 SER   I C   1 
ATOM   15818 O  O   . SER   I  9  139 ? 66.407  -135.595 21.439  1.00 88.88  ? 138 SER   I O   1 
ATOM   15819 C  CB  . SER   I  9  139 ? 65.950  -133.155 23.510  1.00 87.78  ? 138 SER   I CB  1 
ATOM   15820 O  OG  . SER   I  9  139 ? 64.591  -132.894 23.819  1.00 89.33  ? 138 SER   I OG  1 
ATOM   15821 N  N   . GLY   I  9  140 ? 64.405  -135.817 22.532  1.00 90.37  ? 139 GLY   I N   1 
ATOM   15822 C  CA  . GLY   I  9  140 ? 63.614  -136.363 21.412  1.00 92.09  ? 139 GLY   I CA  1 
ATOM   15823 C  C   . GLY   I  9  140 ? 63.281  -137.835 21.587  1.00 92.02  ? 139 GLY   I C   1 
ATOM   15824 O  O   . GLY   I  9  140 ? 63.472  -138.372 22.700  1.00 91.47  ? 139 GLY   I O   1 
ATOM   15825 N  N   . THR   I  9  141 ? 62.802  -138.461 20.507  1.00 90.73  ? 140 THR   I N   1 
ATOM   15826 C  CA  . THR   I  9  141 ? 62.237  -139.836 20.482  1.00 90.42  ? 140 THR   I CA  1 
ATOM   15827 C  C   . THR   I  9  141 ? 63.357  -140.881 20.566  1.00 90.77  ? 140 THR   I C   1 
ATOM   15828 O  O   . THR   I  9  141 ? 63.039  -142.033 20.925  1.00 94.44  ? 140 THR   I O   1 
ATOM   15829 C  CB  . THR   I  9  141 ? 61.350  -140.035 19.246  1.00 89.67  ? 140 THR   I CB  1 
ATOM   15830 O  OG1 . THR   I  9  141 ? 62.029  -139.490 18.114  1.00 86.76  ? 140 THR   I OG1 1 
ATOM   15831 C  CG2 . THR   I  9  141 ? 59.992  -139.381 19.395  1.00 89.04  ? 140 THR   I CG2 1 
ATOM   15832 N  N   . ALA   I  9  142 ? 64.602  -140.499 20.255  1.00 89.15  ? 141 ALA   I N   1 
ATOM   15833 C  CA  . ALA   I  9  142 ? 65.806  -141.360 20.348  1.00 90.18  ? 141 ALA   I CA  1 
ATOM   15834 C  C   . ALA   I  9  142 ? 66.738  -140.844 21.451  1.00 89.33  ? 141 ALA   I C   1 
ATOM   15835 O  O   . ALA   I  9  142 ? 67.968  -140.856 21.237  1.00 87.28  ? 141 ALA   I O   1 
ATOM   15836 C  CB  . ALA   I  9  142 ? 66.514  -141.411 19.015  1.00 92.00  ? 141 ALA   I CB  1 
ATOM   15837 N  N   . SER   I  9  143 ? 66.179  -140.416 22.589  1.00 89.49  ? 142 SER   I N   1 
ATOM   15838 C  CA  . SER   I  9  143 ? 66.942  -139.866 23.741  1.00 88.30  ? 142 SER   I CA  1 
ATOM   15839 C  C   . SER   I  9  143 ? 67.746  -140.987 24.413  1.00 91.78  ? 142 SER   I C   1 
ATOM   15840 O  O   . SER   I  9  143 ? 68.928  -140.746 24.734  1.00 87.95  ? 142 SER   I O   1 
ATOM   15841 C  CB  . SER   I  9  143 ? 66.043  -139.148 24.720  1.00 84.69  ? 142 SER   I CB  1 
ATOM   15842 O  OG  . SER   I  9  143 ? 65.196  -140.049 25.413  1.00 87.92  ? 142 SER   I OG  1 
ATOM   15843 N  N   . ASP   I  9  144 ? 67.130  -142.162 24.598  1.00 93.35  ? 143 ASP   I N   1 
ATOM   15844 C  CA  . ASP   I  9  144 ? 67.783  -143.382 25.149  1.00 97.39  ? 143 ASP   I CA  1 
ATOM   15845 C  C   . ASP   I  9  144 ? 69.039  -143.705 24.329  1.00 97.06  ? 143 ASP   I C   1 
ATOM   15846 O  O   . ASP   I  9  144 ? 70.104  -143.920 24.943  1.00 99.90  ? 143 ASP   I O   1 
ATOM   15847 C  CB  . ASP   I  9  144 ? 66.825  -144.577 25.160  1.00 101.99 ? 143 ASP   I CB  1 
ATOM   15848 C  CG  . ASP   I  9  144 ? 65.786  -144.525 26.267  1.00 105.32 ? 143 ASP   I CG  1 
ATOM   15849 O  OD1 . ASP   I  9  144 ? 65.487  -143.408 26.743  1.00 103.09 ? 143 ASP   I OD1 1 
ATOM   15850 O  OD2 . ASP   I  9  144 ? 65.285  -145.605 26.644  1.00 114.59 ? 143 ASP   I OD2 1 
ATOM   15851 N  N   . GLN   I  9  145 ? 68.911  -143.735 22.999  1.00 95.37  ? 144 GLN   I N   1 
ATOM   15852 C  CA  . GLN   I  9  145 ? 70.022  -144.027 22.053  1.00 94.60  ? 144 GLN   I CA  1 
ATOM   15853 C  C   . GLN   I  9  145 ? 71.092  -142.938 22.180  1.00 94.08  ? 144 GLN   I C   1 
ATOM   15854 O  O   . GLN   I  9  145 ? 72.281  -143.299 22.260  1.00 95.85  ? 144 GLN   I O   1 
ATOM   15855 C  CB  . GLN   I  9  145 ? 69.521  -144.104 20.610  1.00 91.80  ? 144 GLN   I CB  1 
ATOM   15856 C  CG  . GLN   I  9  145 ? 68.604  -145.287 20.333  1.00 91.77  ? 144 GLN   I CG  1 
ATOM   15857 C  CD  . GLN   I  9  145 ? 67.142  -144.963 20.531  1.00 87.57  ? 144 GLN   I CD  1 
ATOM   15858 O  OE1 . GLN   I  9  145 ? 66.764  -144.235 21.445  1.00 83.94  ? 144 GLN   I OE1 1 
ATOM   15859 N  NE2 . GLN   I  9  145 ? 66.298  -145.518 19.678  1.00 88.13  ? 144 GLN   I NE2 1 
ATOM   15860 N  N   . LEU   I  9  146 ? 70.680  -141.664 22.197  1.00 95.67  ? 145 LEU   I N   1 
ATOM   15861 C  CA  . LEU   I  9  146 ? 71.592  -140.494 22.332  1.00 96.11  ? 145 LEU   I CA  1 
ATOM   15862 C  C   . LEU   I  9  146 ? 72.339  -140.581 23.669  1.00 93.49  ? 145 LEU   I C   1 
ATOM   15863 O  O   . LEU   I  9  146 ? 73.563  -140.335 23.667  1.00 94.27  ? 145 LEU   I O   1 
ATOM   15864 C  CB  . LEU   I  9  146 ? 70.797  -139.186 22.218  1.00 96.56  ? 145 LEU   I CB  1 
ATOM   15865 C  CG  . LEU   I  9  146 ? 70.439  -138.740 20.799  1.00 97.59  ? 145 LEU   I CG  1 
ATOM   15866 C  CD1 . LEU   I  9  146 ? 69.442  -137.591 20.831  1.00 98.39  ? 145 LEU   I CD1 1 
ATOM   15867 C  CD2 . LEU   I  9  146 ? 71.677  -138.336 20.013  1.00 96.70  ? 145 LEU   I CD2 1 
ATOM   15868 N  N   . PHE   I  9  147 ? 71.638  -140.932 24.757  1.00 91.67  ? 146 PHE   I N   1 
ATOM   15869 C  CA  . PHE   I  9  147 ? 72.221  -141.099 26.117  1.00 91.59  ? 146 PHE   I CA  1 
ATOM   15870 C  C   . PHE   I  9  147 ? 73.342  -142.139 26.061  1.00 94.23  ? 146 PHE   I C   1 
ATOM   15871 O  O   . PHE   I  9  147 ? 74.413  -141.885 26.637  1.00 92.49  ? 146 PHE   I O   1 
ATOM   15872 C  CB  . PHE   I  9  147 ? 71.163  -141.498 27.151  1.00 89.72  ? 146 PHE   I CB  1 
ATOM   15873 C  CG  . PHE   I  9  147 ? 70.548  -140.346 27.904  1.00 88.27  ? 146 PHE   I CG  1 
ATOM   15874 C  CD1 . PHE   I  9  147 ? 71.346  -139.422 28.561  1.00 88.29  ? 146 PHE   I CD1 1 
ATOM   15875 C  CD2 . PHE   I  9  147 ? 69.171  -140.194 27.974  1.00 88.48  ? 146 PHE   I CD2 1 
ATOM   15876 C  CE1 . PHE   I  9  147 ? 70.780  -138.364 29.255  1.00 88.55  ? 146 PHE   I CE1 1 
ATOM   15877 C  CE2 . PHE   I  9  147 ? 68.607  -139.136 28.672  1.00 86.99  ? 146 PHE   I CE2 1 
ATOM   15878 C  CZ  . PHE   I  9  147 ? 69.413  -138.224 29.311  1.00 88.18  ? 146 PHE   I CZ  1 
ATOM   15879 N  N   . GLY   I  9  148 ? 73.096  -143.263 25.380  1.00 96.79  ? 147 GLY   I N   1 
ATOM   15880 C  CA  . GLY   I  9  148 ? 74.061  -144.366 25.210  1.00 100.75 ? 147 GLY   I CA  1 
ATOM   15881 C  C   . GLY   I  9  148 ? 75.230  -143.968 24.322  1.00 103.54 ? 147 GLY   I C   1 
ATOM   15882 O  O   . GLY   I  9  148 ? 76.379  -144.299 24.679  1.00 103.86 ? 147 GLY   I O   1 
ATOM   15883 N  N   . MET   I  9  149 ? 74.951  -143.284 23.206  1.00 105.96 ? 148 MET   I N   1 
ATOM   15884 C  CA  . MET   I  9  149 ? 75.974  -142.822 22.228  1.00 108.69 ? 148 MET   I CA  1 
ATOM   15885 C  C   . MET   I  9  149 ? 76.884  -141.783 22.894  1.00 109.87 ? 148 MET   I C   1 
ATOM   15886 O  O   . MET   I  9  149 ? 78.116  -141.947 22.817  1.00 110.92 ? 148 MET   I O   1 
ATOM   15887 C  CB  . MET   I  9  149 ? 75.331  -142.200 20.983  1.00 111.28 ? 148 MET   I CB  1 
ATOM   15888 C  CG  . MET   I  9  149 ? 74.736  -143.213 20.013  1.00 113.37 ? 148 MET   I CG  1 
ATOM   15889 S  SD  . MET   I  9  149 ? 75.854  -144.570 19.565  1.00 118.01 ? 148 MET   I SD  1 
ATOM   15890 C  CE  . MET   I  9  149 ? 77.262  -143.672 18.916  1.00 117.56 ? 148 MET   I CE  1 
ATOM   15891 N  N   . CYS   I  9  150 ? 76.296  -140.763 23.529  1.00 110.06 ? 149 CYS   I N   1 
ATOM   15892 C  CA  . CYS   I  9  150 ? 77.026  -139.635 24.172  1.00 109.24 ? 149 CYS   I CA  1 
ATOM   15893 C  C   . CYS   I  9  150 ? 77.859  -140.155 25.351  1.00 110.58 ? 149 CYS   I C   1 
ATOM   15894 O  O   . CYS   I  9  150 ? 79.054  -139.809 25.421  1.00 112.27 ? 149 CYS   I O   1 
ATOM   15895 C  CB  . CYS   I  9  150 ? 76.073  -138.540 24.640  1.00 107.16 ? 149 CYS   I CB  1 
ATOM   15896 S  SG  . CYS   I  9  150 ? 75.287  -137.632 23.282  1.00 106.28 ? 149 CYS   I SG  1 
ATOM   15897 N  N   . GLU   I  9  151 ? 77.256  -140.976 26.218  1.00 108.87 ? 150 GLU   I N   1 
ATOM   15898 C  CA  . GLU   I  9  151 ? 77.864  -141.451 27.491  1.00 108.18 ? 150 GLU   I CA  1 
ATOM   15899 C  C   . GLU   I  9  151 ? 79.146  -142.246 27.204  1.00 108.85 ? 150 GLU   I C   1 
ATOM   15900 O  O   . GLU   I  9  151 ? 80.053  -142.225 28.057  1.00 111.45 ? 150 GLU   I O   1 
ATOM   15901 C  CB  . GLU   I  9  151 ? 76.859  -142.290 28.283  1.00 108.09 ? 150 GLU   I CB  1 
ATOM   15902 C  CG  . GLU   I  9  151 ? 77.264  -142.517 29.722  1.00 109.41 ? 150 GLU   I CG  1 
ATOM   15903 C  CD  . GLU   I  9  151 ? 77.401  -141.238 30.524  1.00 111.35 ? 150 GLU   I CD  1 
ATOM   15904 O  OE1 . GLU   I  9  151 ? 76.405  -140.488 30.616  1.00 109.29 ? 150 GLU   I OE1 1 
ATOM   15905 O  OE2 . GLU   I  9  151 ? 78.504  -140.992 31.054  1.00 114.70 ? 150 GLU   I OE2 1 
ATOM   15906 N  N   . SER   I  9  152 ? 79.221  -142.917 26.053  1.00 110.32 ? 151 SER   I N   1 
ATOM   15907 C  CA  . SER   I  9  152 ? 80.386  -143.739 25.635  1.00 112.50 ? 151 SER   I CA  1 
ATOM   15908 C  C   . SER   I  9  152 ? 81.369  -142.896 24.811  1.00 112.17 ? 151 SER   I C   1 
ATOM   15909 O  O   . SER   I  9  152 ? 82.566  -142.917 25.149  1.00 113.93 ? 151 SER   I O   1 
ATOM   15910 C  CB  . SER   I  9  152 ? 79.941  -144.973 24.890  1.00 114.09 ? 151 SER   I CB  1 
ATOM   15911 O  OG  . SER   I  9  152 ? 79.028  -144.643 23.855  1.00 115.19 ? 151 SER   I OG  1 
ATOM   15912 N  N   . LEU   I  9  153 ? 80.890  -142.178 23.786  1.00 109.92 ? 152 LEU   I N   1 
ATOM   15913 C  CA  . LEU   I  9  153 ? 81.752  -141.481 22.786  1.00 110.94 ? 152 LEU   I CA  1 
ATOM   15914 C  C   . LEU   I  9  153 ? 82.439  -140.258 23.409  1.00 112.56 ? 152 LEU   I C   1 
ATOM   15915 O  O   . LEU   I  9  153 ? 83.615  -140.020 23.068  1.00 115.20 ? 152 LEU   I O   1 
ATOM   15916 C  CB  . LEU   I  9  153 ? 80.925  -141.051 21.567  1.00 110.38 ? 152 LEU   I CB  1 
ATOM   15917 C  CG  . LEU   I  9  153 ? 80.420  -142.155 20.635  1.00 110.59 ? 152 LEU   I CG  1 
ATOM   15918 C  CD1 . LEU   I  9  153 ? 79.922  -141.550 19.330  1.00 111.26 ? 152 LEU   I CD1 1 
ATOM   15919 C  CD2 . LEU   I  9  153 ? 81.488  -143.200 20.347  1.00 114.65 ? 152 LEU   I CD2 1 
ATOM   15920 N  N   . TYR   I  9  154 ? 81.741  -139.507 24.270  1.00 111.23 ? 153 TYR   I N   1 
ATOM   15921 C  CA  . TYR   I  9  154 ? 82.157  -138.154 24.732  1.00 111.80 ? 153 TYR   I CA  1 
ATOM   15922 C  C   . TYR   I  9  154 ? 83.442  -138.227 25.565  1.00 112.84 ? 153 TYR   I C   1 
ATOM   15923 O  O   . TYR   I  9  154 ? 83.596  -139.168 26.367  1.00 115.26 ? 153 TYR   I O   1 
ATOM   15924 C  CB  . TYR   I  9  154 ? 81.058  -137.475 25.554  1.00 110.38 ? 153 TYR   I CB  1 
ATOM   15925 C  CG  . TYR   I  9  154 ? 81.419  -136.085 26.012  1.00 114.38 ? 153 TYR   I CG  1 
ATOM   15926 C  CD1 . TYR   I  9  154 ? 81.223  -134.990 25.185  1.00 115.01 ? 153 TYR   I CD1 1 
ATOM   15927 C  CD2 . TYR   I  9  154 ? 81.994  -135.863 27.254  1.00 114.85 ? 153 TYR   I CD2 1 
ATOM   15928 C  CE1 . TYR   I  9  154 ? 81.570  -133.710 25.584  1.00 117.37 ? 153 TYR   I CE1 1 
ATOM   15929 C  CE2 . TYR   I  9  154 ? 82.350  -134.590 27.668  1.00 118.19 ? 153 TYR   I CE2 1 
ATOM   15930 C  CZ  . TYR   I  9  154 ? 82.136  -133.507 26.831  1.00 119.16 ? 153 TYR   I CZ  1 
ATOM   15931 O  OH  . TYR   I  9  154 ? 82.479  -132.247 27.228  1.00 120.06 ? 153 TYR   I OH  1 
ATOM   15932 N  N   . GLU   I  9  155 ? 84.328  -137.243 25.372  1.00 113.93 ? 154 GLU   I N   1 
ATOM   15933 C  CA  . GLU   I  9  155 ? 85.470  -136.927 26.274  1.00 118.18 ? 154 GLU   I CA  1 
ATOM   15934 C  C   . GLU   I  9  155 ? 85.604  -135.408 26.387  1.00 119.81 ? 154 GLU   I C   1 
ATOM   15935 O  O   . GLU   I  9  155 ? 85.288  -134.685 25.443  1.00 119.46 ? 154 GLU   I O   1 
ATOM   15936 C  CB  . GLU   I  9  155 ? 86.765  -137.587 25.787  1.00 120.41 ? 154 GLU   I CB  1 
ATOM   15937 C  CG  . GLU   I  9  155 ? 87.057  -137.398 24.309  1.00 120.77 ? 154 GLU   I CG  1 
ATOM   15938 C  CD  . GLU   I  9  155 ? 88.372  -138.019 23.865  1.00 124.92 ? 154 GLU   I CD  1 
ATOM   15939 O  OE1 . GLU   I  9  155 ? 89.432  -137.538 24.313  1.00 124.46 ? 154 GLU   I OE1 1 
ATOM   15940 O  OE2 . GLU   I  9  155 ? 88.333  -138.995 23.089  1.00 126.63 ? 154 GLU   I OE2 1 
ATOM   15941 N  N   . PRO   I  9  156 ? 86.062  -134.869 27.542  1.00 121.01 ? 155 PRO   I N   1 
ATOM   15942 C  CA  . PRO   I  9  156 ? 86.123  -133.421 27.747  1.00 120.26 ? 155 PRO   I CA  1 
ATOM   15943 C  C   . PRO   I  9  156 ? 87.170  -132.711 26.873  1.00 123.71 ? 155 PRO   I C   1 
ATOM   15944 O  O   . PRO   I  9  156 ? 88.101  -133.362 26.431  1.00 128.98 ? 155 PRO   I O   1 
ATOM   15945 C  CB  . PRO   I  9  156 ? 86.522  -133.258 29.225  1.00 121.01 ? 155 PRO   I CB  1 
ATOM   15946 C  CG  . PRO   I  9  156 ? 86.320  -134.627 29.845  1.00 121.22 ? 155 PRO   I CG  1 
ATOM   15947 C  CD  . PRO   I  9  156 ? 86.536  -135.613 28.718  1.00 121.18 ? 155 PRO   I CD  1 
ATOM   15948 N  N   . ASN   I  9  157 ? 86.982  -131.403 26.660  1.00 121.27 ? 156 ASN   I N   1 
ATOM   15949 C  CA  . ASN   I  9  157 ? 87.963  -130.470 26.039  1.00 122.04 ? 156 ASN   I CA  1 
ATOM   15950 C  C   . ASN   I  9  157 ? 88.356  -130.947 24.635  1.00 122.25 ? 156 ASN   I C   1 
ATOM   15951 O  O   . ASN   I  9  157 ? 89.564  -130.935 24.325  1.00 125.04 ? 156 ASN   I O   1 
ATOM   15952 C  CB  . ASN   I  9  157 ? 89.202  -130.298 26.921  1.00 125.23 ? 156 ASN   I CB  1 
ATOM   15953 C  CG  . ASN   I  9  157 ? 88.882  -129.647 28.248  1.00 125.43 ? 156 ASN   I CG  1 
ATOM   15954 O  OD1 . ASN   I  9  157 ? 89.059  -130.256 29.300  1.00 126.47 ? 156 ASN   I OD1 1 
ATOM   15955 N  ND2 . ASN   I  9  157 ? 88.399  -128.416 28.206  1.00 125.40 ? 156 ASN   I ND2 1 
ATOM   15956 N  N   . LEU   I  9  158 ? 87.376  -131.336 23.815  1.00 122.68 ? 157 LEU   I N   1 
ATOM   15957 C  CA  . LEU   I  9  158 ? 87.592  -131.663 22.380  1.00 123.50 ? 157 LEU   I CA  1 
ATOM   15958 C  C   . LEU   I  9  158 ? 87.769  -130.357 21.598  1.00 123.63 ? 157 LEU   I C   1 
ATOM   15959 O  O   . LEU   I  9  158 ? 87.110  -129.359 21.950  1.00 124.24 ? 157 LEU   I O   1 
ATOM   15960 C  CB  . LEU   I  9  158 ? 86.405  -132.468 21.843  1.00 120.59 ? 157 LEU   I CB  1 
ATOM   15961 C  CG  . LEU   I  9  158 ? 86.364  -133.939 22.251  1.00 119.68 ? 157 LEU   I CG  1 
ATOM   15962 C  CD1 . LEU   I  9  158 ? 84.976  -134.518 22.032  1.00 117.87 ? 157 LEU   I CD1 1 
ATOM   15963 C  CD2 . LEU   I  9  158 ? 87.405  -134.745 21.488  1.00 120.86 ? 157 LEU   I CD2 1 
ATOM   15964 N  N   . GLU   I  9  159 ? 88.632  -130.369 20.580  1.00 126.58 ? 158 GLU   I N   1 
ATOM   15965 C  CA  . GLU   I  9  159 ? 88.804  -129.242 19.626  1.00 129.83 ? 158 GLU   I CA  1 
ATOM   15966 C  C   . GLU   I  9  159 ? 87.575  -129.192 18.724  1.00 126.59 ? 158 GLU   I C   1 
ATOM   15967 O  O   . GLU   I  9  159 ? 86.972  -130.223 18.440  1.00 131.33 ? 158 GLU   I O   1 
ATOM   15968 C  CB  . GLU   I  9  159 ? 90.095  -129.404 18.820  1.00 133.58 ? 158 GLU   I CB  1 
ATOM   15969 C  CG  . GLU   I  9  159 ? 91.356  -129.207 19.646  1.00 136.89 ? 158 GLU   I CG  1 
ATOM   15970 C  CD  . GLU   I  9  159 ? 91.531  -127.813 20.231  1.00 137.53 ? 158 GLU   I CD  1 
ATOM   15971 O  OE1 . GLU   I  9  159 ? 91.180  -126.834 19.543  1.00 136.99 ? 158 GLU   I OE1 1 
ATOM   15972 O  OE2 . GLU   I  9  159 ? 92.014  -127.710 21.377  1.00 138.51 ? 158 GLU   I OE2 1 
ATOM   15973 N  N   . PRO   I  9  160 ? 87.154  -127.990 18.268  1.00 123.77 ? 159 PRO   I N   1 
ATOM   15974 C  CA  . PRO   I  9  160 ? 85.974  -127.843 17.413  1.00 121.34 ? 159 PRO   I CA  1 
ATOM   15975 C  C   . PRO   I  9  160 ? 85.816  -128.908 16.312  1.00 118.04 ? 159 PRO   I C   1 
ATOM   15976 O  O   . PRO   I  9  160 ? 84.711  -129.394 16.142  1.00 111.96 ? 159 PRO   I O   1 
ATOM   15977 C  CB  . PRO   I  9  160 ? 86.196  -126.457 16.790  1.00 121.27 ? 159 PRO   I CB  1 
ATOM   15978 C  CG  . PRO   I  9  160 ? 86.914  -125.679 17.873  1.00 122.74 ? 159 PRO   I CG  1 
ATOM   15979 C  CD  . PRO   I  9  160 ? 87.778  -126.697 18.589  1.00 124.62 ? 159 PRO   I CD  1 
ATOM   15980 N  N   . GLU   I  9  161 ? 86.904  -129.248 15.611  1.00 119.19 ? 160 GLU   I N   1 
ATOM   15981 C  CA  . GLU   I  9  161 ? 86.901  -130.194 14.458  1.00 122.95 ? 160 GLU   I CA  1 
ATOM   15982 C  C   . GLU   I  9  161 ? 86.680  -131.626 14.962  1.00 120.28 ? 160 GLU   I C   1 
ATOM   15983 O  O   . GLU   I  9  161 ? 86.028  -132.410 14.245  1.00 119.90 ? 160 GLU   I O   1 
ATOM   15984 C  CB  . GLU   I  9  161 ? 88.204  -130.101 13.660  1.00 129.64 ? 160 GLU   I CB  1 
ATOM   15985 C  CG  . GLU   I  9  161 ? 88.415  -128.756 12.984  1.00 134.32 ? 160 GLU   I CG  1 
ATOM   15986 C  CD  . GLU   I  9  161 ? 89.117  -127.700 13.824  1.00 138.54 ? 160 GLU   I CD  1 
ATOM   15987 O  OE1 . GLU   I  9  161 ? 89.226  -127.891 15.054  1.00 141.88 ? 160 GLU   I OE1 1 
ATOM   15988 O  OE2 . GLU   I  9  161 ? 89.552  -126.685 13.244  1.00 143.83 ? 160 GLU   I OE2 1 
ATOM   15989 N  N   . ASP   I  9  162 ? 87.213  -131.950 16.144  1.00 116.62 ? 161 ASP   I N   1 
ATOM   15990 C  CA  . ASP   I  9  162 ? 87.045  -133.270 16.807  1.00 115.08 ? 161 ASP   I CA  1 
ATOM   15991 C  C   . ASP   I  9  162 ? 85.624  -133.362 17.376  1.00 111.05 ? 161 ASP   I C   1 
ATOM   15992 O  O   . ASP   I  9  162 ? 84.967  -134.392 17.141  1.00 111.26 ? 161 ASP   I O   1 
ATOM   15993 C  CB  . ASP   I  9  162 ? 88.105  -133.485 17.891  1.00 114.85 ? 161 ASP   I CB  1 
ATOM   15994 C  CG  . ASP   I  9  162 ? 89.531  -133.485 17.363  1.00 118.44 ? 161 ASP   I CG  1 
ATOM   15995 O  OD1 . ASP   I  9  162 ? 89.764  -134.100 16.305  1.00 122.82 ? 161 ASP   I OD1 1 
ATOM   15996 O  OD2 . ASP   I  9  162 ? 90.397  -132.867 18.012  1.00 118.77 ? 161 ASP   I OD2 1 
ATOM   15997 N  N   . LEU   I  9  163 ? 85.173  -132.320 18.083  1.00 109.23 ? 162 LEU   I N   1 
ATOM   15998 C  CA  . LEU   I  9  163 ? 83.820  -132.235 18.704  1.00 108.82 ? 162 LEU   I CA  1 
ATOM   15999 C  C   . LEU   I  9  163 ? 82.741  -132.450 17.636  1.00 107.49 ? 162 LEU   I C   1 
ATOM   16000 O  O   . LEU   I  9  163 ? 81.704  -133.055 17.967  1.00 105.63 ? 162 LEU   I O   1 
ATOM   16001 C  CB  . LEU   I  9  163 ? 83.648  -130.869 19.378  1.00 109.33 ? 162 LEU   I CB  1 
ATOM   16002 C  CG  . LEU   I  9  163 ? 82.285  -130.623 20.026  1.00 108.33 ? 162 LEU   I CG  1 
ATOM   16003 C  CD1 . LEU   I  9  163 ? 82.068  -131.555 21.207  1.00 106.98 ? 162 LEU   I CD1 1 
ATOM   16004 C  CD2 . LEU   I  9  163 ? 82.141  -129.173 20.461  1.00 108.55 ? 162 LEU   I CD2 1 
ATOM   16005 N  N   . PHE   I  9  164 ? 82.971  -131.953 16.416  1.00 109.19 ? 163 PHE   I N   1 
ATOM   16006 C  CA  . PHE   I  9  164 ? 82.063  -132.122 15.250  1.00 109.24 ? 163 PHE   I CA  1 
ATOM   16007 C  C   . PHE   I  9  164 ? 81.896  -133.612 14.932  1.00 109.54 ? 163 PHE   I C   1 
ATOM   16008 O  O   . PHE   I  9  164 ? 80.754  -134.044 14.696  1.00 108.89 ? 163 PHE   I O   1 
ATOM   16009 C  CB  . PHE   I  9  164 ? 82.588  -131.389 14.013  1.00 108.88 ? 163 PHE   I CB  1 
ATOM   16010 C  CG  . PHE   I  9  164 ? 81.879  -131.787 12.744  1.00 110.51 ? 163 PHE   I CG  1 
ATOM   16011 C  CD1 . PHE   I  9  164 ? 80.583  -131.362 12.497  1.00 107.74 ? 163 PHE   I CD1 1 
ATOM   16012 C  CD2 . PHE   I  9  164 ? 82.487  -132.623 11.821  1.00 114.30 ? 163 PHE   I CD2 1 
ATOM   16013 C  CE1 . PHE   I  9  164 ? 79.920  -131.743 11.342  1.00 109.61 ? 163 PHE   I CE1 1 
ATOM   16014 C  CE2 . PHE   I  9  164 ? 81.823  -133.004 10.666  1.00 116.67 ? 163 PHE   I CE2 1 
ATOM   16015 C  CZ  . PHE   I  9  164 ? 80.541  -132.563 10.428  1.00 113.92 ? 163 PHE   I CZ  1 
ATOM   16016 N  N   . GLU   I  9  165 ? 83.004  -134.360 14.905  1.00 112.48 ? 164 GLU   I N   1 
ATOM   16017 C  CA  . GLU   I  9  165 ? 83.023  -135.810 14.569  1.00 115.56 ? 164 GLU   I CA  1 
ATOM   16018 C  C   . GLU   I  9  165 ? 82.248  -136.586 15.640  1.00 111.97 ? 164 GLU   I C   1 
ATOM   16019 O  O   . GLU   I  9  165 ? 81.451  -137.466 15.262  1.00 114.69 ? 164 GLU   I O   1 
ATOM   16020 C  CB  . GLU   I  9  165 ? 84.457  -136.333 14.447  1.00 118.36 ? 164 GLU   I CB  1 
ATOM   16021 C  CG  . GLU   I  9  165 ? 85.257  -135.688 13.328  1.00 122.27 ? 164 GLU   I CG  1 
ATOM   16022 C  CD  . GLU   I  9  165 ? 84.729  -135.929 11.923  1.00 124.69 ? 164 GLU   I CD  1 
ATOM   16023 O  OE1 . GLU   I  9  165 ? 85.161  -135.206 11.003  1.00 126.04 ? 164 GLU   I OE1 1 
ATOM   16024 O  OE2 . GLU   I  9  165 ? 83.890  -136.839 11.748  1.00 129.93 ? 164 GLU   I OE2 1 
ATOM   16025 N  N   . THR   I  9  166 ? 82.462  -136.257 16.920  1.00 108.69 ? 165 THR   I N   1 
ATOM   16026 C  CA  . THR   I  9  166 ? 81.853  -136.950 18.088  1.00 103.87 ? 165 THR   I CA  1 
ATOM   16027 C  C   . THR   I  9  166 ? 80.338  -136.713 18.102  1.00 103.32 ? 165 THR   I C   1 
ATOM   16028 O  O   . THR   I  9  166 ? 79.597  -137.707 18.209  1.00 103.64 ? 165 THR   I O   1 
ATOM   16029 C  CB  . THR   I  9  166 ? 82.503  -136.518 19.409  1.00 101.54 ? 165 THR   I CB  1 
ATOM   16030 O  OG1 . THR   I  9  166 ? 83.912  -136.712 19.286  1.00 100.22 ? 165 THR   I OG1 1 
ATOM   16031 C  CG2 . THR   I  9  166 ? 81.990  -137.296 20.601  1.00 99.77  ? 165 THR   I CG2 1 
ATOM   16032 N  N   . ILE   I  9  167 ? 79.892  -135.457 18.002  1.00 102.40 ? 166 ILE   I N   1 
ATOM   16033 C  CA  . ILE   I  9  167 ? 78.442  -135.098 18.086  1.00 100.08 ? 166 ILE   I CA  1 
ATOM   16034 C  C   . ILE   I  9  167 ? 77.701  -135.679 16.873  1.00 100.89 ? 166 ILE   I C   1 
ATOM   16035 O  O   . ILE   I  9  167 ? 76.545  -136.112 17.044  1.00 98.09  ? 166 ILE   I O   1 
ATOM   16036 C  CB  . ILE   I  9  167 ? 78.216  -133.577 18.236  1.00 97.60  ? 166 ILE   I CB  1 
ATOM   16037 C  CG1 . ILE   I  9  167 ? 76.766  -133.281 18.630  1.00 93.97  ? 166 ILE   I CG1 1 
ATOM   16038 C  CG2 . ILE   I  9  167 ? 78.623  -132.817 16.981  1.00 97.49  ? 166 ILE   I CG2 1 
ATOM   16039 C  CD1 . ILE   I  9  167 ? 76.547  -131.907 19.207  1.00 93.99  ? 166 ILE   I CD1 1 
ATOM   16040 N  N   . SER   I  9  168 ? 78.339  -135.697 15.698  1.00 104.26 ? 167 SER   I N   1 
ATOM   16041 C  CA  . SER   I  9  168 ? 77.751  -136.210 14.432  1.00 108.23 ? 167 SER   I CA  1 
ATOM   16042 C  C   . SER   I  9  168 ? 77.518  -137.720 14.538  1.00 111.58 ? 167 SER   I C   1 
ATOM   16043 O  O   . SER   I  9  168 ? 76.412  -138.172 14.180  1.00 117.02 ? 167 SER   I O   1 
ATOM   16044 C  CB  . SER   I  9  168 ? 78.622  -135.890 13.250  1.00 110.54 ? 167 SER   I CB  1 
ATOM   16045 O  OG  . SER   I  9  168 ? 78.789  -134.488 13.099  1.00 108.47 ? 167 SER   I OG  1 
ATOM   16046 N  N   . GLN   I  9  169 ? 78.527  -138.459 15.009  1.00 113.14 ? 168 GLN   I N   1 
ATOM   16047 C  CA  . GLN   I  9  169 ? 78.475  -139.935 15.188  1.00 115.27 ? 168 GLN   I CA  1 
ATOM   16048 C  C   . GLN   I  9  169 ? 77.477  -140.279 16.302  1.00 108.70 ? 168 GLN   I C   1 
ATOM   16049 O  O   . GLN   I  9  169 ? 76.890  -141.375 16.235  1.00 109.01 ? 168 GLN   I O   1 
ATOM   16050 C  CB  . GLN   I  9  169 ? 79.877  -140.491 15.462  1.00 117.30 ? 168 GLN   I CB  1 
ATOM   16051 C  CG  . GLN   I  9  169 ? 80.794  -140.459 14.246  1.00 122.18 ? 168 GLN   I CG  1 
ATOM   16052 C  CD  . GLN   I  9  169 ? 80.307  -141.359 13.135  1.00 124.07 ? 168 GLN   I CD  1 
ATOM   16053 O  OE1 . GLN   I  9  169 ? 79.937  -142.509 13.362  1.00 130.02 ? 168 GLN   I OE1 1 
ATOM   16054 N  NE2 . GLN   I  9  169 ? 80.299  -140.842 11.917  1.00 123.70 ? 168 GLN   I NE2 1 
ATOM   16055 N  N   . ALA   I  9  170 ? 77.271  -139.380 17.271  1.00 105.39 ? 169 ALA   I N   1 
ATOM   16056 C  CA  . ALA   I  9  170 ? 76.290  -139.546 18.370  1.00 104.09 ? 169 ALA   I CA  1 
ATOM   16057 C  C   . ALA   I  9  170 ? 74.872  -139.510 17.794  1.00 104.20 ? 169 ALA   I C   1 
ATOM   16058 O  O   . ALA   I  9  170 ? 74.086  -140.419 18.113  1.00 104.11 ? 169 ALA   I O   1 
ATOM   16059 C  CB  . ALA   I  9  170 ? 76.481  -138.488 19.429  1.00 102.64 ? 169 ALA   I CB  1 
ATOM   16060 N  N   . LEU   I  9  171 ? 74.571  -138.501 16.970  1.00 104.75 ? 170 LEU   I N   1 
ATOM   16061 C  CA  . LEU   I  9  171 ? 73.222  -138.265 16.383  1.00 106.39 ? 170 LEU   I CA  1 
ATOM   16062 C  C   . LEU   I  9  171 ? 72.895  -139.356 15.355  1.00 106.04 ? 170 LEU   I C   1 
ATOM   16063 O  O   . LEU   I  9  171 ? 71.819  -139.975 15.479  1.00 103.63 ? 170 LEU   I O   1 
ATOM   16064 C  CB  . LEU   I  9  171 ? 73.182  -136.873 15.740  1.00 107.44 ? 170 LEU   I CB  1 
ATOM   16065 C  CG  . LEU   I  9  171 ? 71.810  -136.426 15.230  1.00 107.14 ? 170 LEU   I CG  1 
ATOM   16066 C  CD1 . LEU   I  9  171 ? 71.608  -134.933 15.429  1.00 107.81 ? 170 LEU   I CD1 1 
ATOM   16067 C  CD2 . LEU   I  9  171 ? 71.612  -136.792 13.767  1.00 109.16 ? 170 LEU   I CD2 1 
ATOM   16068 N  N   . LEU   I  9  172 ? 73.778  -139.559 14.372  1.00 108.41 ? 171 LEU   I N   1 
ATOM   16069 C  CA  . LEU   I  9  172 ? 73.573  -140.475 13.214  1.00 110.30 ? 171 LEU   I CA  1 
ATOM   16070 C  C   . LEU   I  9  172 ? 73.211  -141.885 13.700  1.00 111.23 ? 171 LEU   I C   1 
ATOM   16071 O  O   . LEU   I  9  172 ? 72.188  -142.422 13.231  1.00 110.08 ? 171 LEU   I O   1 
ATOM   16072 C  CB  . LEU   I  9  172 ? 74.844  -140.505 12.355  1.00 114.05 ? 171 LEU   I CB  1 
ATOM   16073 C  CG  . LEU   I  9  172 ? 74.823  -139.694 11.055  1.00 112.33 ? 171 LEU   I CG  1 
ATOM   16074 C  CD1 . LEU   I  9  172 ? 73.920  -138.471 11.138  1.00 110.42 ? 171 LEU   I CD1 1 
ATOM   16075 C  CD2 . LEU   I  9  172 ? 76.233  -139.277 10.666  1.00 113.96 ? 171 LEU   I CD2 1 
ATOM   16076 N  N   . ASN   I  9  173 ? 74.019  -142.459 14.597  1.00 112.74 ? 172 ASN   I N   1 
ATOM   16077 C  CA  . ASN   I  9  173 ? 73.885  -143.868 15.060  1.00 110.68 ? 172 ASN   I CA  1 
ATOM   16078 C  C   . ASN   I  9  173 ? 72.672  -144.005 15.988  1.00 110.90 ? 172 ASN   I C   1 
ATOM   16079 O  O   . ASN   I  9  173 ? 72.096  -145.111 16.029  1.00 113.08 ? 172 ASN   I O   1 
ATOM   16080 C  CB  . ASN   I  9  173 ? 75.177  -144.366 15.711  1.00 109.85 ? 172 ASN   I CB  1 
ATOM   16081 C  CG  . ASN   I  9  173 ? 76.294  -144.503 14.700  1.00 109.63 ? 172 ASN   I CG  1 
ATOM   16082 O  OD1 . ASN   I  9  173 ? 76.352  -145.489 13.970  1.00 111.83 ? 172 ASN   I OD1 1 
ATOM   16083 N  ND2 . ASN   I  9  173 ? 77.168  -143.513 14.631  1.00 109.95 ? 172 ASN   I ND2 1 
ATOM   16084 N  N   . ALA   I  9  174 ? 72.297  -142.934 16.697  1.00 109.16 ? 173 ALA   I N   1 
ATOM   16085 C  CA  . ALA   I  9  174 ? 71.088  -142.877 17.552  1.00 107.61 ? 173 ALA   I CA  1 
ATOM   16086 C  C   . ALA   I  9  174 ? 69.839  -142.836 16.664  1.00 107.98 ? 173 ALA   I C   1 
ATOM   16087 O  O   . ALA   I  9  174 ? 68.885  -143.591 16.948  1.00 103.15 ? 173 ALA   I O   1 
ATOM   16088 C  CB  . ALA   I  9  174 ? 71.149  -141.684 18.477  1.00 106.15 ? 173 ALA   I CB  1 
ATOM   16089 N  N   . ALA   I  9  175 ? 69.861  -141.991 15.626  1.00 108.75 ? 174 ALA   I N   1 
ATOM   16090 C  CA  . ALA   I  9  175 ? 68.746  -141.738 14.680  1.00 108.28 ? 174 ALA   I CA  1 
ATOM   16091 C  C   . ALA   I  9  175 ? 68.407  -142.999 13.873  1.00 112.11 ? 174 ALA   I C   1 
ATOM   16092 O  O   . ALA   I  9  175 ? 67.235  -143.143 13.466  1.00 110.30 ? 174 ALA   I O   1 
ATOM   16093 C  CB  . ALA   I  9  175 ? 69.108  -140.599 13.758  1.00 107.75 ? 174 ALA   I CB  1 
ATOM   16094 N  N   . ASP   I  9  176 ? 69.395  -143.864 13.628  1.00 111.21 ? 175 ASP   I N   1 
ATOM   16095 C  CA  . ASP   I  9  176 ? 69.239  -145.081 12.790  1.00 114.91 ? 175 ASP   I CA  1 
ATOM   16096 C  C   . ASP   I  9  176 ? 68.626  -146.220 13.614  1.00 114.03 ? 175 ASP   I C   1 
ATOM   16097 O  O   . ASP   I  9  176 ? 68.163  -147.194 12.989  1.00 121.53 ? 175 ASP   I O   1 
ATOM   16098 C  CB  . ASP   I  9  176 ? 70.572  -145.463 12.144  1.00 117.63 ? 175 ASP   I CB  1 
ATOM   16099 C  CG  . ASP   I  9  176 ? 71.012  -144.476 11.074  1.00 118.66 ? 175 ASP   I CG  1 
ATOM   16100 O  OD1 . ASP   I  9  176 ? 70.223  -143.558 10.756  1.00 112.35 ? 175 ASP   I OD1 1 
ATOM   16101 O  OD2 . ASP   I  9  176 ? 72.138  -144.629 10.565  1.00 124.15 ? 175 ASP   I OD2 1 
ATOM   16102 N  N   . ARG   I  9  177 ? 68.600  -146.102 14.948  1.00 110.86 ? 176 ARG   I N   1 
ATOM   16103 C  CA  . ARG   I  9  177 ? 67.940  -147.084 15.852  1.00 110.01 ? 176 ARG   I CA  1 
ATOM   16104 C  C   . ARG   I  9  177 ? 66.552  -146.569 16.259  1.00 111.22 ? 176 ARG   I C   1 
ATOM   16105 O  O   . ARG   I  9  177 ? 65.899  -147.250 17.077  1.00 117.01 ? 176 ARG   I O   1 
ATOM   16106 C  CB  . ARG   I  9  177 ? 68.822  -147.385 17.071  1.00 110.00 ? 176 ARG   I CB  1 
ATOM   16107 C  CG  . ARG   I  9  177 ? 69.878  -148.452 16.821  1.00 111.48 ? 176 ARG   I CG  1 
ATOM   16108 C  CD  . ARG   I  9  177 ? 69.282  -149.841 16.663  1.00 111.68 ? 176 ARG   I CD  1 
ATOM   16109 N  NE  . ARG   I  9  177 ? 70.241  -150.797 16.128  1.00 112.37 ? 176 ARG   I NE  1 
ATOM   16110 C  CZ  . ARG   I  9  177 ? 69.980  -152.076 15.873  1.00 112.37 ? 176 ARG   I CZ  1 
ATOM   16111 N  NH1 . ARG   I  9  177 ? 68.777  -152.577 16.103  1.00 113.22 ? 176 ARG   I NH1 1 
ATOM   16112 N  NH2 . ARG   I  9  177 ? 70.928  -152.860 15.391  1.00 115.43 ? 176 ARG   I NH2 1 
ATOM   16113 N  N   . ASP   I  9  178 ? 66.110  -145.436 15.699  1.00 110.14 ? 177 ASP   I N   1 
ATOM   16114 C  CA  . ASP   I  9  178 ? 64.761  -144.853 15.943  1.00 107.85 ? 177 ASP   I CA  1 
ATOM   16115 C  C   . ASP   I  9  178 ? 64.016  -144.714 14.611  1.00 105.51 ? 177 ASP   I C   1 
ATOM   16116 O  O   . ASP   I  9  178 ? 64.569  -144.101 13.672  1.00 98.72  ? 177 ASP   I O   1 
ATOM   16117 C  CB  . ASP   I  9  178 ? 64.846  -143.509 16.670  1.00 106.83 ? 177 ASP   I CB  1 
ATOM   16118 C  CG  . ASP   I  9  178 ? 63.498  -142.960 17.117  1.00 106.71 ? 177 ASP   I CG  1 
ATOM   16119 O  OD1 . ASP   I  9  178 ? 62.549  -143.761 17.256  1.00 112.58 ? 177 ASP   I OD1 1 
ATOM   16120 O  OD2 . ASP   I  9  178 ? 63.405  -141.735 17.326  1.00 101.09 ? 177 ASP   I OD2 1 
ATOM   16121 N  N   . ALA   I  9  179 ? 62.796  -145.256 14.552  1.00 104.68 ? 178 ALA   I N   1 
ATOM   16122 C  CA  . ALA   I  9  179 ? 61.903  -145.241 13.371  1.00 106.92 ? 178 ALA   I CA  1 
ATOM   16123 C  C   . ALA   I  9  179 ? 61.485  -143.801 13.045  1.00 104.60 ? 178 ALA   I C   1 
ATOM   16124 O  O   . ALA   I  9  179 ? 61.382  -143.476 11.841  1.00 102.98 ? 178 ALA   I O   1 
ATOM   16125 C  CB  . ALA   I  9  179 ? 60.701  -146.121 13.627  1.00 108.28 ? 178 ALA   I CB  1 
ATOM   16126 N  N   . LEU   I  9  180 ? 61.273  -142.972 14.076  1.00 100.23 ? 179 LEU   I N   1 
ATOM   16127 C  CA  . LEU   I  9  180 ? 60.667  -141.616 13.954  1.00 96.63  ? 179 LEU   I CA  1 
ATOM   16128 C  C   . LEU   I  9  180 ? 61.738  -140.530 13.783  1.00 92.92  ? 179 LEU   I C   1 
ATOM   16129 O  O   . LEU   I  9  180 ? 61.346  -139.394 13.487  1.00 90.76  ? 179 LEU   I O   1 
ATOM   16130 C  CB  . LEU   I  9  180 ? 59.811  -141.329 15.192  1.00 95.12  ? 179 LEU   I CB  1 
ATOM   16131 C  CG  . LEU   I  9  180 ? 58.639  -142.277 15.440  1.00 98.45  ? 179 LEU   I CG  1 
ATOM   16132 C  CD1 . LEU   I  9  180 ? 57.763  -141.759 16.571  1.00 99.51  ? 179 LEU   I CD1 1 
ATOM   16133 C  CD2 . LEU   I  9  180 ? 57.806  -142.483 14.184  1.00 100.30 ? 179 LEU   I CD2 1 
ATOM   16134 N  N   . SER   I  9  181 ? 63.024  -140.839 13.976  1.00 96.40  ? 180 SER   I N   1 
ATOM   16135 C  CA  . SER   I  9  181 ? 64.142  -139.869 13.815  1.00 96.46  ? 180 SER   I CA  1 
ATOM   16136 C  C   . SER   I  9  181 ? 64.896  -140.144 12.510  1.00 100.87 ? 180 SER   I C   1 
ATOM   16137 O  O   . SER   I  9  181 ? 64.783  -141.271 11.977  1.00 100.21 ? 180 SER   I O   1 
ATOM   16138 C  CB  . SER   I  9  181 ? 65.070  -139.888 15.005  1.00 97.33  ? 180 SER   I CB  1 
ATOM   16139 O  OG  . SER   I  9  181 ? 64.392  -139.452 16.174  1.00 97.14  ? 180 SER   I OG  1 
ATOM   16140 N  N   . GLY   I  9  182 ? 65.616  -139.130 12.016  1.00 102.00 ? 181 GLY   I N   1 
ATOM   16141 C  CA  . GLY   I  9  182 ? 66.548  -139.226 10.874  1.00 108.04 ? 181 GLY   I CA  1 
ATOM   16142 C  C   . GLY   I  9  182 ? 66.122  -138.351 9.705   1.00 109.46 ? 181 GLY   I C   1 
ATOM   16143 O  O   . GLY   I  9  182 ? 65.767  -137.178 9.940   1.00 106.47 ? 181 GLY   I O   1 
ATOM   16144 N  N   . TRP   I  9  183 ? 66.173  -138.900 8.484   1.00 114.60 ? 182 TRP   I N   1 
ATOM   16145 C  CA  . TRP   I  9  183 ? 65.758  -138.241 7.212   1.00 114.45 ? 182 TRP   I CA  1 
ATOM   16146 C  C   . TRP   I  9  183 ? 66.602  -136.989 6.930   1.00 113.23 ? 182 TRP   I C   1 
ATOM   16147 O  O   . TRP   I  9  183 ? 66.086  -136.058 6.279   1.00 111.06 ? 182 TRP   I O   1 
ATOM   16148 C  CB  . TRP   I  9  183 ? 64.255  -137.927 7.244   1.00 111.36 ? 182 TRP   I CB  1 
ATOM   16149 C  CG  . TRP   I  9  183 ? 63.436  -138.799 6.346   1.00 115.15 ? 182 TRP   I CG  1 
ATOM   16150 C  CD1 . TRP   I  9  183 ? 63.716  -140.078 5.960   1.00 118.35 ? 182 TRP   I CD1 1 
ATOM   16151 C  CD2 . TRP   I  9  183 ? 62.179  -138.463 5.734   1.00 110.44 ? 182 TRP   I CD2 1 
ATOM   16152 N  NE1 . TRP   I  9  183 ? 62.730  -140.553 5.141   1.00 120.66 ? 182 TRP   I NE1 1 
ATOM   16153 C  CE2 . TRP   I  9  183 ? 61.772  -139.586 4.985   1.00 115.38 ? 182 TRP   I CE2 1 
ATOM   16154 C  CE3 . TRP   I  9  183 ? 61.358  -137.330 5.748   1.00 107.17 ? 182 TRP   I CE3 1 
ATOM   16155 C  CZ2 . TRP   I  9  183 ? 60.583  -139.602 4.256   1.00 115.88 ? 182 TRP   I CZ2 1 
ATOM   16156 C  CZ3 . TRP   I  9  183 ? 60.187  -137.344 5.023   1.00 108.30 ? 182 TRP   I CZ3 1 
ATOM   16157 C  CH2 . TRP   I  9  183 ? 59.806  -138.467 4.289   1.00 111.49 ? 182 TRP   I CH2 1 
ATOM   16158 N  N   . GLY   I  9  184 ? 67.869  -136.995 7.354   1.00 113.58 ? 183 GLY   I N   1 
ATOM   16159 C  CA  . GLY   I  9  184 ? 68.794  -135.852 7.235   1.00 114.89 ? 183 GLY   I CA  1 
ATOM   16160 C  C   . GLY   I  9  184 ? 69.162  -135.310 8.603   1.00 112.54 ? 183 GLY   I C   1 
ATOM   16161 O  O   . GLY   I  9  184 ? 68.459  -135.645 9.577   1.00 116.95 ? 183 GLY   I O   1 
ATOM   16162 N  N   . ALA   I  9  185 ? 70.218  -134.498 8.678   1.00 111.55 ? 184 ALA   I N   1 
ATOM   16163 C  CA  . ALA   I  9  185 ? 70.763  -133.952 9.942   1.00 110.16 ? 184 ALA   I CA  1 
ATOM   16164 C  C   . ALA   I  9  185 ? 71.487  -132.629 9.676   1.00 108.34 ? 184 ALA   I C   1 
ATOM   16165 O  O   . ALA   I  9  185 ? 71.959  -132.420 8.540   1.00 108.29 ? 184 ALA   I O   1 
ATOM   16166 C  CB  . ALA   I  9  185 ? 71.682  -134.964 10.585  1.00 109.78 ? 184 ALA   I CB  1 
ATOM   16167 N  N   . VAL   I  9  186 ? 71.548  -131.776 10.702  1.00 107.72 ? 185 VAL   I N   1 
ATOM   16168 C  CA  . VAL   I  9  186 ? 72.302  -130.489 10.711  1.00 106.80 ? 185 VAL   I CA  1 
ATOM   16169 C  C   . VAL   I  9  186 ? 73.109  -130.412 12.009  1.00 103.87 ? 185 VAL   I C   1 
ATOM   16170 O  O   . VAL   I  9  186 ? 72.533  -130.683 13.081  1.00 99.38  ? 185 VAL   I O   1 
ATOM   16171 C  CB  . VAL   I  9  186 ? 71.359  -129.280 10.576  1.00 105.36 ? 185 VAL   I CB  1 
ATOM   16172 C  CG1 . VAL   I  9  186 ? 72.103  -127.964 10.736  1.00 104.26 ? 185 VAL   I CG1 1 
ATOM   16173 C  CG2 . VAL   I  9  186 ? 70.602  -129.308 9.260   1.00 108.90 ? 185 VAL   I CG2 1 
ATOM   16174 N  N   . VAL   I  9  187 ? 74.387  -130.044 11.904  1.00 104.56 ? 186 VAL   I N   1 
ATOM   16175 C  CA  . VAL   I  9  187 ? 75.290  -129.804 13.067  1.00 104.27 ? 186 VAL   I CA  1 
ATOM   16176 C  C   . VAL   I  9  187 ? 75.750  -128.346 13.034  1.00 103.38 ? 186 VAL   I C   1 
ATOM   16177 O  O   . VAL   I  9  187 ? 76.212  -127.894 11.969  1.00 105.10 ? 186 VAL   I O   1 
ATOM   16178 C  CB  . VAL   I  9  187 ? 76.495  -130.761 13.062  1.00 105.64 ? 186 VAL   I CB  1 
ATOM   16179 C  CG1 . VAL   I  9  187 ? 77.406  -130.518 14.256  1.00 106.43 ? 186 VAL   I CG1 1 
ATOM   16180 C  CG2 . VAL   I  9  187 ? 76.051  -132.213 13.014  1.00 106.64 ? 186 VAL   I CG2 1 
ATOM   16181 N  N   . TYR   I  9  188 ? 75.626  -127.656 14.170  1.00 102.47 ? 187 TYR   I N   1 
ATOM   16182 C  CA  . TYR   I  9  188 ? 76.152  -126.288 14.408  1.00 102.51 ? 187 TYR   I CA  1 
ATOM   16183 C  C   . TYR   I  9  188 ? 77.399  -126.391 15.291  1.00 102.38 ? 187 TYR   I C   1 
ATOM   16184 O  O   . TYR   I  9  188 ? 77.275  -126.881 16.426  1.00 99.19  ? 187 TYR   I O   1 
ATOM   16185 C  CB  . TYR   I  9  188 ? 75.105  -125.405 15.092  1.00 100.21 ? 187 TYR   I CB  1 
ATOM   16186 C  CG  . TYR   I  9  188 ? 73.955  -124.962 14.222  1.00 98.07  ? 187 TYR   I CG  1 
ATOM   16187 C  CD1 . TYR   I  9  188 ? 72.836  -125.762 14.051  1.00 97.56  ? 187 TYR   I CD1 1 
ATOM   16188 C  CD2 . TYR   I  9  188 ? 73.967  -123.726 13.594  1.00 97.10  ? 187 TYR   I CD2 1 
ATOM   16189 C  CE1 . TYR   I  9  188 ? 71.770  -125.356 13.265  1.00 95.86  ? 187 TYR   I CE1 1 
ATOM   16190 C  CE2 . TYR   I  9  188 ? 72.909  -123.305 12.805  1.00 95.77  ? 187 TYR   I CE2 1 
ATOM   16191 C  CZ  . TYR   I  9  188 ? 71.807  -124.124 12.639  1.00 95.01  ? 187 TYR   I CZ  1 
ATOM   16192 O  OH  . TYR   I  9  188 ? 70.758  -123.728 11.863  1.00 96.30  ? 187 TYR   I OH  1 
ATOM   16193 N  N   . ILE   I  9  189 ? 78.554  -125.967 14.772  1.00 106.84 ? 188 ILE   I N   1 
ATOM   16194 C  CA  . ILE   I  9  189 ? 79.800  -125.742 15.563  1.00 107.28 ? 188 ILE   I CA  1 
ATOM   16195 C  C   . ILE   I  9  189 ? 79.877  -124.249 15.887  1.00 108.06 ? 188 ILE   I C   1 
ATOM   16196 O  O   . ILE   I  9  189 ? 79.851  -123.439 14.939  1.00 107.18 ? 188 ILE   I O   1 
ATOM   16197 C  CB  . ILE   I  9  189 ? 81.049  -126.239 14.808  1.00 112.28 ? 188 ILE   I CB  1 
ATOM   16198 C  CG1 . ILE   I  9  189 ? 80.931  -127.718 14.430  1.00 113.55 ? 188 ILE   I CG1 1 
ATOM   16199 C  CG2 . ILE   I  9  189 ? 82.314  -125.961 15.610  1.00 114.30 ? 188 ILE   I CG2 1 
ATOM   16200 C  CD1 . ILE   I  9  189 ? 80.749  -128.652 15.608  1.00 113.83 ? 188 ILE   I CD1 1 
ATOM   16201 N  N   . ILE   I  9  190 ? 79.962  -123.913 17.178  1.00 105.48 ? 189 ILE   I N   1 
ATOM   16202 C  CA  . ILE   I  9  190 ? 79.882  -122.516 17.699  1.00 106.70 ? 189 ILE   I CA  1 
ATOM   16203 C  C   . ILE   I  9  190 ? 81.185  -122.184 18.430  1.00 108.96 ? 189 ILE   I C   1 
ATOM   16204 O  O   . ILE   I  9  190 ? 81.487  -122.863 19.432  1.00 105.20 ? 189 ILE   I O   1 
ATOM   16205 C  CB  . ILE   I  9  190 ? 78.657  -122.344 18.618  1.00 103.36 ? 189 ILE   I CB  1 
ATOM   16206 C  CG1 . ILE   I  9  190 ? 77.362  -122.803 17.942  1.00 100.33 ? 189 ILE   I CG1 1 
ATOM   16207 C  CG2 . ILE   I  9  190 ? 78.549  -120.909 19.108  1.00 104.24 ? 189 ILE   I CG2 1 
ATOM   16208 C  CD1 . ILE   I  9  190 ? 76.240  -123.101 18.907  1.00 97.40  ? 189 ILE   I CD1 1 
ATOM   16209 N  N   . LYS   I  9  191 ? 81.910  -121.176 17.933  1.00 116.90 ? 190 LYS   I N   1 
ATOM   16210 C  CA  . LYS   I  9  191 ? 83.105  -120.571 18.581  1.00 118.97 ? 190 LYS   I CA  1 
ATOM   16211 C  C   . LYS   I  9  191 ? 82.734  -119.147 19.015  1.00 120.45 ? 190 LYS   I C   1 
ATOM   16212 O  O   . LYS   I  9  191 ? 81.603  -118.717 18.707  1.00 115.66 ? 190 LYS   I O   1 
ATOM   16213 C  CB  . LYS   I  9  191 ? 84.298  -120.615 17.621  1.00 123.20 ? 190 LYS   I CB  1 
ATOM   16214 C  CG  . LYS   I  9  191 ? 84.660  -122.006 17.115  1.00 122.57 ? 190 LYS   I CG  1 
ATOM   16215 C  CD  . LYS   I  9  191 ? 85.704  -122.004 16.025  1.00 126.29 ? 190 LYS   I CD  1 
ATOM   16216 C  CE  . LYS   I  9  191 ? 87.095  -121.710 16.544  1.00 129.10 ? 190 LYS   I CE  1 
ATOM   16217 N  NZ  . LYS   I  9  191 ? 88.098  -121.735 15.454  1.00 134.94 ? 190 LYS   I NZ  1 
ATOM   16218 N  N   . LYS   I  9  192 ? 83.642  -118.449 19.705  1.00 128.78 ? 191 LYS   I N   1 
ATOM   16219 C  CA  . LYS   I  9  192 ? 83.350  -117.159 20.389  1.00 134.36 ? 191 LYS   I CA  1 
ATOM   16220 C  C   . LYS   I  9  192 ? 82.758  -116.150 19.392  1.00 132.31 ? 191 LYS   I C   1 
ATOM   16221 O  O   . LYS   I  9  192 ? 81.824  -115.424 19.789  1.00 131.02 ? 191 LYS   I O   1 
ATOM   16222 C  CB  . LYS   I  9  192 ? 84.598  -116.591 21.075  1.00 140.33 ? 191 LYS   I CB  1 
ATOM   16223 C  CG  . LYS   I  9  192 ? 84.303  -115.553 22.153  1.00 144.19 ? 191 LYS   I CG  1 
ATOM   16224 C  CD  . LYS   I  9  192 ? 85.064  -114.250 21.981  1.00 146.94 ? 191 LYS   I CD  1 
ATOM   16225 C  CE  . LYS   I  9  192 ? 84.730  -113.181 23.006  1.00 149.85 ? 191 LYS   I CE  1 
ATOM   16226 N  NZ  . LYS   I  9  192 ? 83.355  -113.298 23.551  1.00 150.43 ? 191 LYS   I NZ  1 
ATOM   16227 N  N   . ASP   I  9  193 ? 83.267  -116.102 18.154  1.00 135.91 ? 192 ASP   I N   1 
ATOM   16228 C  CA  . ASP   I  9  193 ? 82.782  -115.156 17.110  1.00 138.50 ? 192 ASP   I CA  1 
ATOM   16229 C  C   . ASP   I  9  193 ? 82.936  -115.765 15.707  1.00 138.01 ? 192 ASP   I C   1 
ATOM   16230 O  O   . ASP   I  9  193 ? 83.332  -115.026 14.782  1.00 141.54 ? 192 ASP   I O   1 
ATOM   16231 C  CB  . ASP   I  9  193 ? 83.468  -113.791 17.244  1.00 142.13 ? 192 ASP   I CB  1 
ATOM   16232 C  CG  . ASP   I  9  193 ? 84.877  -113.851 17.808  1.00 143.39 ? 192 ASP   I CG  1 
ATOM   16233 O  OD1 . ASP   I  9  193 ? 85.597  -114.820 17.491  1.00 155.96 ? 192 ASP   I OD1 1 
ATOM   16234 O  OD2 . ASP   I  9  193 ? 85.240  -112.932 18.571  1.00 137.80 ? 192 ASP   I OD2 1 
ATOM   16235 N  N   . GLU   I  9  194 ? 82.616  -117.054 15.551  1.00 132.79 ? 193 GLU   I N   1 
ATOM   16236 C  CA  . GLU   I  9  194 ? 82.257  -117.668 14.242  1.00 126.70 ? 193 GLU   I CA  1 
ATOM   16237 C  C   . GLU   I  9  194 ? 81.429  -118.930 14.507  1.00 121.23 ? 193 GLU   I C   1 
ATOM   16238 O  O   . GLU   I  9  194 ? 81.734  -119.651 15.481  1.00 117.33 ? 193 GLU   I O   1 
ATOM   16239 C  CB  . GLU   I  9  194 ? 83.491  -117.921 13.366  1.00 130.71 ? 193 GLU   I CB  1 
ATOM   16240 C  CG  . GLU   I  9  194 ? 84.112  -119.305 13.492  1.00 132.06 ? 193 GLU   I CG  1 
ATOM   16241 C  CD  . GLU   I  9  194 ? 84.951  -119.729 12.296  1.00 134.56 ? 193 GLU   I CD  1 
ATOM   16242 O  OE1 . GLU   I  9  194 ? 84.536  -119.453 11.151  1.00 133.30 ? 193 GLU   I OE1 1 
ATOM   16243 O  OE2 . GLU   I  9  194 ? 86.016  -120.339 12.512  1.00 140.48 ? 193 GLU   I OE2 1 
ATOM   16244 N  N   . VAL   I  9  195 ? 80.402  -119.156 13.684  1.00 118.17 ? 194 VAL   I N   1 
ATOM   16245 C  CA  . VAL   I  9  195 ? 79.509  -120.350 13.739  1.00 112.64 ? 194 VAL   I CA  1 
ATOM   16246 C  C   . VAL   I  9  195 ? 79.507  -121.009 12.357  1.00 110.95 ? 194 VAL   I C   1 
ATOM   16247 O  O   . VAL   I  9  195 ? 79.263  -120.297 11.362  1.00 106.45 ? 194 VAL   I O   1 
ATOM   16248 C  CB  . VAL   I  9  195 ? 78.084  -119.973 14.187  1.00 109.94 ? 194 VAL   I CB  1 
ATOM   16249 C  CG1 . VAL   I  9  195 ? 77.164  -121.186 14.216  1.00 108.82 ? 194 VAL   I CG1 1 
ATOM   16250 C  CG2 . VAL   I  9  195 ? 78.084  -119.273 15.536  1.00 107.51 ? 194 VAL   I CG2 1 
ATOM   16251 N  N   . VAL   I  9  196 ? 79.771  -122.317 12.311  1.00 112.40 ? 195 VAL   I N   1 
ATOM   16252 C  CA  . VAL   I  9  196 ? 79.761  -123.140 11.066  1.00 116.19 ? 195 VAL   I CA  1 
ATOM   16253 C  C   . VAL   I  9  196 ? 78.600  -124.134 11.167  1.00 112.06 ? 195 VAL   I C   1 
ATOM   16254 O  O   . VAL   I  9  196 ? 78.517  -124.844 12.188  1.00 114.84 ? 195 VAL   I O   1 
ATOM   16255 C  CB  . VAL   I  9  196 ? 81.107  -123.857 10.844  1.00 120.85 ? 195 VAL   I CB  1 
ATOM   16256 C  CG1 . VAL   I  9  196 ? 81.140  -124.584 9.507   1.00 124.24 ? 195 VAL   I CG1 1 
ATOM   16257 C  CG2 . VAL   I  9  196 ? 82.285  -122.898 10.956  1.00 123.62 ? 195 VAL   I CG2 1 
ATOM   16258 N  N   . LYS   I  9  197 ? 77.742  -124.162 10.144  1.00 110.63 ? 196 LYS   I N   1 
ATOM   16259 C  CA  . LYS   I  9  197 ? 76.558  -125.054 10.035  1.00 110.69 ? 196 LYS   I CA  1 
ATOM   16260 C  C   . LYS   I  9  197 ? 76.819  -126.082 8.932   1.00 113.61 ? 196 LYS   I C   1 
ATOM   16261 O  O   . LYS   I  9  197 ? 77.023  -125.660 7.777   1.00 118.72 ? 196 LYS   I O   1 
ATOM   16262 C  CB  . LYS   I  9  197 ? 75.316  -124.217 9.724   1.00 108.72 ? 196 LYS   I CB  1 
ATOM   16263 C  CG  . LYS   I  9  197 ? 74.014  -124.980 9.539   1.00 107.98 ? 196 LYS   I CG  1 
ATOM   16264 C  CD  . LYS   I  9  197 ? 72.881  -124.076 9.117   1.00 109.34 ? 196 LYS   I CD  1 
ATOM   16265 C  CE  . LYS   I  9  197 ? 71.579  -124.812 8.889   1.00 109.92 ? 196 LYS   I CE  1 
ATOM   16266 N  NZ  . LYS   I  9  197 ? 70.522  -123.894 8.406   1.00 111.93 ? 196 LYS   I NZ  1 
ATOM   16267 N  N   . ARG   I  9  198 ? 76.812  -127.372 9.277   1.00 113.55 ? 197 ARG   I N   1 
ATOM   16268 C  CA  . ARG   I  9  198 ? 77.059  -128.483 8.322   1.00 114.26 ? 197 ARG   I CA  1 
ATOM   16269 C  C   . ARG   I  9  198 ? 75.828  -129.395 8.258   1.00 111.07 ? 197 ARG   I C   1 
ATOM   16270 O  O   . ARG   I  9  198 ? 75.256  -129.699 9.324   1.00 107.80 ? 197 ARG   I O   1 
ATOM   16271 C  CB  . ARG   I  9  198 ? 78.315  -129.258 8.730   1.00 114.84 ? 197 ARG   I CB  1 
ATOM   16272 C  CG  . ARG   I  9  198 ? 79.585  -128.419 8.736   1.00 117.97 ? 197 ARG   I CG  1 
ATOM   16273 C  CD  . ARG   I  9  198 ? 80.828  -129.282 8.632   1.00 119.38 ? 197 ARG   I CD  1 
ATOM   16274 N  NE  . ARG   I  9  198 ? 82.066  -128.526 8.771   1.00 122.10 ? 197 ARG   I NE  1 
ATOM   16275 C  CZ  . ARG   I  9  198 ? 82.603  -128.135 9.925   1.00 121.63 ? 197 ARG   I CZ  1 
ATOM   16276 N  NH1 . ARG   I  9  198 ? 82.007  -128.411 11.074  1.00 121.81 ? 197 ARG   I NH1 1 
ATOM   16277 N  NH2 . ARG   I  9  198 ? 83.738  -127.459 9.926   1.00 123.24 ? 197 ARG   I NH2 1 
ATOM   16278 N  N   . TYR   I  9  199 ? 75.441  -129.793 7.043   1.00 111.68 ? 198 TYR   I N   1 
ATOM   16279 C  CA  . TYR   I  9  199 ? 74.422  -130.837 6.762   1.00 117.52 ? 198 TYR   I CA  1 
ATOM   16280 C  C   . TYR   I  9  199 ? 75.136  -132.179 6.579   1.00 118.08 ? 198 TYR   I C   1 
ATOM   16281 O  O   . TYR   I  9  199 ? 76.072  -132.248 5.758   1.00 119.67 ? 198 TYR   I O   1 
ATOM   16282 C  CB  . TYR   I  9  199 ? 73.614  -130.497 5.509   1.00 119.42 ? 198 TYR   I CB  1 
ATOM   16283 C  CG  . TYR   I  9  199 ? 72.697  -129.311 5.655   1.00 120.53 ? 198 TYR   I CG  1 
ATOM   16284 C  CD1 . TYR   I  9  199 ? 73.198  -128.020 5.698   1.00 121.62 ? 198 TYR   I CD1 1 
ATOM   16285 C  CD2 . TYR   I  9  199 ? 71.325  -129.477 5.748   1.00 121.72 ? 198 TYR   I CD2 1 
ATOM   16286 C  CE1 . TYR   I  9  199 ? 72.361  -126.925 5.835   1.00 120.80 ? 198 TYR   I CE1 1 
ATOM   16287 C  CE2 . TYR   I  9  199 ? 70.474  -128.393 5.884   1.00 119.20 ? 198 TYR   I CE2 1 
ATOM   16288 C  CZ  . TYR   I  9  199 ? 70.993  -127.112 5.928   1.00 117.52 ? 198 TYR   I CZ  1 
ATOM   16289 O  OH  . TYR   I  9  199 ? 70.161  -126.040 6.062   1.00 115.94 ? 198 TYR   I OH  1 
ATOM   16290 N  N   . LEU   I  9  200 ? 74.707  -133.206 7.316   1.00 121.53 ? 199 LEU   I N   1 
ATOM   16291 C  CA  . LEU   I  9  200 ? 75.331  -134.554 7.284   1.00 123.63 ? 199 LEU   I CA  1 
ATOM   16292 C  C   . LEU   I  9  200 ? 74.637  -135.405 6.215   1.00 121.46 ? 199 LEU   I C   1 
ATOM   16293 O  O   . LEU   I  9  200 ? 73.437  -135.168 5.949   1.00 123.28 ? 199 LEU   I O   1 
ATOM   16294 C  CB  . LEU   I  9  200 ? 75.223  -135.203 8.669   1.00 122.97 ? 199 LEU   I CB  1 
ATOM   16295 C  CG  . LEU   I  9  200 ? 75.773  -134.392 9.844   1.00 124.16 ? 199 LEU   I CG  1 
ATOM   16296 C  CD1 . LEU   I  9  200 ? 75.698  -135.201 11.131  1.00 121.37 ? 199 LEU   I CD1 1 
ATOM   16297 C  CD2 . LEU   I  9  200 ? 77.205  -133.942 9.587   1.00 127.60 ? 199 LEU   I CD2 1 
ATOM   16298 N  N   . LYS   I  9  201 ? 75.385  -136.334 5.611   1.00 123.11 ? 200 LYS   I N   1 
ATOM   16299 C  CA  . LYS   I  9  201 ? 74.853  -137.431 4.760   1.00 126.02 ? 200 LYS   I CA  1 
ATOM   16300 C  C   . LYS   I  9  201 ? 74.503  -138.618 5.660   1.00 122.28 ? 200 LYS   I C   1 
ATOM   16301 O  O   . LYS   I  9  201 ? 75.421  -139.142 6.321   1.00 124.42 ? 200 LYS   I O   1 
ATOM   16302 C  CB  . LYS   I  9  201 ? 75.884  -137.872 3.718   1.00 130.85 ? 200 LYS   I CB  1 
ATOM   16303 C  CG  . LYS   I  9  201 ? 75.426  -139.009 2.814   1.00 136.98 ? 200 LYS   I CG  1 
ATOM   16304 C  CD  . LYS   I  9  201 ? 76.516  -139.552 1.924   1.00 141.36 ? 200 LYS   I CD  1 
ATOM   16305 C  CE  . LYS   I  9  201 ? 76.195  -140.932 1.395   1.00 144.01 ? 200 LYS   I CE  1 
ATOM   16306 N  NZ  . LYS   I  9  201 ? 77.231  -141.402 0.447   1.00 148.09 ? 200 LYS   I NZ  1 
ATOM   16307 N  N   . MET   I  9  202 ? 73.235  -139.031 5.678   1.00 119.34 ? 201 MET   I N   1 
ATOM   16308 C  CA  . MET   I  9  202 ? 72.769  -140.183 6.493   1.00 116.97 ? 201 MET   I CA  1 
ATOM   16309 C  C   . MET   I  9  202 ? 71.747  -140.992 5.687   1.00 119.10 ? 201 MET   I C   1 
ATOM   16310 O  O   . MET   I  9  202 ? 71.172  -140.428 4.735   1.00 120.49 ? 201 MET   I O   1 
ATOM   16311 C  CB  . MET   I  9  202 ? 72.170  -139.707 7.822   1.00 112.41 ? 201 MET   I CB  1 
ATOM   16312 C  CG  . MET   I  9  202 ? 70.786  -139.088 7.719   1.00 111.59 ? 201 MET   I CG  1 
ATOM   16313 S  SD  . MET   I  9  202 ? 70.071  -138.770 9.353   1.00 108.46 ? 201 MET   I SD  1 
ATOM   16314 C  CE  . MET   I  9  202 ? 69.905  -140.440 9.986   1.00 110.28 ? 201 MET   I CE  1 
ATOM   16315 N  N   . ARG   I  9  203 ? 71.555  -142.267 6.047   1.00 119.18 ? 202 ARG   I N   1 
ATOM   16316 C  CA  . ARG   I  9  203 ? 70.591  -143.189 5.384   1.00 121.29 ? 202 ARG   I CA  1 
ATOM   16317 C  C   . ARG   I  9  203 ? 69.187  -142.568 5.453   1.00 118.63 ? 202 ARG   I C   1 
ATOM   16318 O  O   . ARG   I  9  203 ? 68.851  -141.969 6.498   1.00 116.77 ? 202 ARG   I O   1 
ATOM   16319 C  CB  . ARG   I  9  203 ? 70.655  -144.594 5.998   1.00 120.30 ? 202 ARG   I CB  1 
ATOM   16320 C  CG  . ARG   I  9  203 ? 70.225  -144.694 7.456   1.00 117.97 ? 202 ARG   I CG  1 
ATOM   16321 C  CD  . ARG   I  9  203 ? 70.420  -146.095 8.010   1.00 118.15 ? 202 ARG   I CD  1 
ATOM   16322 N  NE  . ARG   I  9  203 ? 69.742  -147.111 7.210   1.00 118.94 ? 202 ARG   I NE  1 
ATOM   16323 C  CZ  . ARG   I  9  203 ? 70.333  -148.052 6.471   1.00 120.49 ? 202 ARG   I CZ  1 
ATOM   16324 N  NH1 . ARG   I  9  203 ? 71.652  -148.150 6.409   1.00 119.22 ? 202 ARG   I NH1 1 
ATOM   16325 N  NH2 . ARG   I  9  203 ? 69.588  -148.911 5.795   1.00 122.54 ? 202 ARG   I NH2 1 
ATOM   16326 N  N   . GLN   I  9  204 ? 68.406  -142.697 4.375   1.00 118.05 ? 203 GLN   I N   1 
ATOM   16327 C  CA  . GLN   I  9  204 ? 67.109  -141.990 4.189   1.00 119.25 ? 203 GLN   I CA  1 
ATOM   16328 C  C   . GLN   I  9  204 ? 65.940  -142.978 4.304   1.00 122.63 ? 203 GLN   I C   1 
ATOM   16329 O  O   . GLN   I  9  204 ? 65.015  -142.885 3.476   1.00 124.13 ? 203 GLN   I O   1 
ATOM   16330 C  CB  . GLN   I  9  204 ? 67.091  -141.285 2.831   1.00 121.17 ? 203 GLN   I CB  1 
ATOM   16331 C  CG  . GLN   I  9  204 ? 68.189  -140.244 2.666   1.00 120.05 ? 203 GLN   I CG  1 
ATOM   16332 C  CD  . GLN   I  9  204 ? 67.954  -139.017 3.515   1.00 118.74 ? 203 GLN   I CD  1 
ATOM   16333 O  OE1 . GLN   I  9  204 ? 66.942  -138.333 3.381   1.00 115.28 ? 203 GLN   I OE1 1 
ATOM   16334 N  NE2 . GLN   I  9  204 ? 68.897  -138.723 4.398   1.00 121.38 ? 203 GLN   I NE2 1 
ATOM   16335 N  N   . ASP   I  9  205 ? 65.971  -143.873 5.297   1.00 127.79 ? 204 ASP   I N   1 
ATOM   16336 C  CA  . ASP   I  9  205 ? 64.884  -144.851 5.579   1.00 132.66 ? 204 ASP   I CA  1 
ATOM   16337 C  C   . ASP   I  9  205 ? 64.430  -144.678 7.035   1.00 136.79 ? 204 ASP   I C   1 
ATOM   16338 O  O   . ASP   I  9  205 ? 63.863  -145.587 7.637   1.00 145.75 ? 204 ASP   I O   1 
ATOM   16339 C  CB  . ASP   I  9  205 ? 65.324  -146.279 5.234   1.00 135.82 ? 204 ASP   I CB  1 
ATOM   16340 C  CG  . ASP   I  9  205 ? 66.534  -146.790 6.000   1.00 134.72 ? 204 ASP   I CG  1 
ATOM   16341 O  OD1 . ASP   I  9  205 ? 67.211  -145.973 6.660   1.00 128.35 ? 204 ASP   I OD1 1 
ATOM   16342 O  OD2 . ASP   I  9  205 ? 66.796  -148.008 5.926   1.00 140.22 ? 204 ASP   I OD2 1 
ATOM   16343 O  OXT . ASP   I  9  205 ? 64.604  -143.621 7.651   1.00 136.08 ? 204 ASP   I OXT 1 
ATOM   16344 N  N   . MET   J  10 1   ? 34.130  -134.711 2.472   1.00 135.90 ? 1   MET   J N   1 
ATOM   16345 C  CA  . MET   J  10 1   ? 35.584  -134.335 2.454   1.00 133.39 ? 1   MET   J CA  1 
ATOM   16346 C  C   . MET   J  10 1   ? 36.407  -135.558 2.019   1.00 129.71 ? 1   MET   J C   1 
ATOM   16347 O  O   . MET   J  10 1   ? 35.830  -136.411 1.317   1.00 140.82 ? 1   MET   J O   1 
ATOM   16348 C  CB  . MET   J  10 1   ? 36.021  -133.810 3.828   1.00 138.55 ? 1   MET   J CB  1 
ATOM   16349 C  CG  . MET   J  10 1   ? 35.310  -132.516 4.224   1.00 146.45 ? 1   MET   J CG  1 
ATOM   16350 S  SD  . MET   J  10 1   ? 35.713  -131.103 3.150   1.00 158.34 ? 1   MET   J SD  1 
ATOM   16351 C  CE  . MET   J  10 1   ? 34.154  -130.218 3.149   1.00 153.74 ? 1   MET   J CE  1 
ATOM   16352 N  N   . ASP   J  10 2   ? 37.705  -135.599 2.345   1.00 119.54 ? 2   ASP   J N   1 
ATOM   16353 C  CA  . ASP   J  10 2   ? 38.597  -136.791 2.258   1.00 117.73 ? 2   ASP   J CA  1 
ATOM   16354 C  C   . ASP   J  10 2   ? 39.862  -136.415 1.471   1.00 109.80 ? 2   ASP   J C   1 
ATOM   16355 O  O   . ASP   J  10 2   ? 40.878  -136.127 2.130   1.00 108.43 ? 2   ASP   J O   1 
ATOM   16356 C  CB  . ASP   J  10 2   ? 37.891  -138.037 1.704   1.00 118.75 ? 2   ASP   J CB  1 
ATOM   16357 C  CG  . ASP   J  10 2   ? 38.424  -139.338 2.281   1.00 120.24 ? 2   ASP   J CG  1 
ATOM   16358 O  OD1 . ASP   J  10 2   ? 39.658  -139.502 2.318   1.00 117.81 ? 2   ASP   J OD1 1 
ATOM   16359 O  OD2 . ASP   J  10 2   ? 37.597  -140.172 2.706   1.00 124.57 ? 2   ASP   J OD2 1 
ATOM   16360 N  N   . ILE   J  10 3   ? 39.810  -136.393 0.133   1.00 107.60 ? 3   ILE   J N   1 
ATOM   16361 C  CA  . ILE   J  10 3   ? 41.021  -136.271 -0.739  1.00 106.40 ? 3   ILE   J CA  1 
ATOM   16362 C  C   . ILE   J  10 3   ? 41.254  -134.806 -1.115  1.00 103.33 ? 3   ILE   J C   1 
ATOM   16363 O  O   . ILE   J  10 3   ? 40.394  -134.227 -1.803  1.00 100.07 ? 3   ILE   J O   1 
ATOM   16364 C  CB  . ILE   J  10 3   ? 40.914  -137.149 -2.002  1.00 109.87 ? 3   ILE   J CB  1 
ATOM   16365 C  CG1 . ILE   J  10 3   ? 40.793  -138.631 -1.633  1.00 113.90 ? 3   ILE   J CG1 1 
ATOM   16366 C  CG2 . ILE   J  10 3   ? 42.084  -136.879 -2.944  1.00 107.33 ? 3   ILE   J CG2 1 
ATOM   16367 C  CD1 . ILE   J  10 3   ? 40.752  -139.575 -2.813  1.00 117.28 ? 3   ILE   J CD1 1 
ATOM   16368 N  N   . ILE   J  10 4   ? 42.401  -134.257 -0.702  1.00 102.18 ? 4   ILE   J N   1 
ATOM   16369 C  CA  . ILE   J  10 4   ? 42.956  -132.970 -1.215  1.00 100.74 ? 4   ILE   J CA  1 
ATOM   16370 C  C   . ILE   J  10 4   ? 44.447  -133.168 -1.519  1.00 98.03  ? 4   ILE   J C   1 
ATOM   16371 O  O   . ILE   J  10 4   ? 45.181  -133.672 -0.642  1.00 92.11  ? 4   ILE   J O   1 
ATOM   16372 C  CB  . ILE   J  10 4   ? 42.689  -131.805 -0.239  1.00 99.48  ? 4   ILE   J CB  1 
ATOM   16373 C  CG1 . ILE   J  10 4   ? 43.219  -132.074 1.171   1.00 99.80  ? 4   ILE   J CG1 1 
ATOM   16374 C  CG2 . ILE   J  10 4   ? 41.206  -131.464 -0.213  1.00 102.82 ? 4   ILE   J CG2 1 
ATOM   16375 C  CD1 . ILE   J  10 4   ? 43.385  -130.823 2.003   1.00 99.09  ? 4   ILE   J CD1 1 
ATOM   16376 N  N   . LEU   J  10 5   ? 44.857  -132.809 -2.740  1.00 100.58 ? 5   LEU   J N   1 
ATOM   16377 C  CA  . LEU   J  10 5   ? 46.253  -132.897 -3.242  1.00 100.59 ? 5   LEU   J CA  1 
ATOM   16378 C  C   . LEU   J  10 5   ? 46.723  -131.501 -3.658  1.00 99.82  ? 5   LEU   J C   1 
ATOM   16379 O  O   . LEU   J  10 5   ? 45.863  -130.618 -3.878  1.00 98.27  ? 5   LEU   J O   1 
ATOM   16380 C  CB  . LEU   J  10 5   ? 46.311  -133.854 -4.437  1.00 103.94 ? 5   LEU   J CB  1 
ATOM   16381 C  CG  . LEU   J  10 5   ? 45.764  -135.258 -4.196  1.00 105.18 ? 5   LEU   J CG  1 
ATOM   16382 C  CD1 . LEU   J  10 5   ? 45.638  -136.016 -5.508  1.00 108.82 ? 5   LEU   J CD1 1 
ATOM   16383 C  CD2 . LEU   J  10 5   ? 46.640  -136.025 -3.220  1.00 107.63 ? 5   LEU   J CD2 1 
ATOM   16384 N  N   . GLY   J  10 6   ? 48.041  -131.327 -3.767  1.00 97.50  ? 6   GLY   J N   1 
ATOM   16385 C  CA  . GLY   J  10 6   ? 48.687  -130.085 -4.229  1.00 96.65  ? 6   GLY   J CA  1 
ATOM   16386 C  C   . GLY   J  10 6   ? 50.033  -130.375 -4.861  1.00 97.55  ? 6   GLY   J C   1 
ATOM   16387 O  O   . GLY   J  10 6   ? 50.810  -131.130 -4.251  1.00 100.44 ? 6   GLY   J O   1 
ATOM   16388 N  N   . ILE   J  10 7   ? 50.291  -129.820 -6.049  1.00 99.20  ? 7   ILE   J N   1 
ATOM   16389 C  CA  . ILE   J  10 7   ? 51.600  -129.924 -6.761  1.00 101.72 ? 7   ILE   J CA  1 
ATOM   16390 C  C   . ILE   J  10 7   ? 52.050  -128.512 -7.154  1.00 100.99 ? 7   ILE   J C   1 
ATOM   16391 O  O   . ILE   J  10 7   ? 51.311  -127.828 -7.891  1.00 100.18 ? 7   ILE   J O   1 
ATOM   16392 C  CB  . ILE   J  10 7   ? 51.518  -130.868 -7.979  1.00 103.81 ? 7   ILE   J CB  1 
ATOM   16393 C  CG1 . ILE   J  10 7   ? 51.204  -132.306 -7.556  1.00 106.71 ? 7   ILE   J CG1 1 
ATOM   16394 C  CG2 . ILE   J  10 7   ? 52.796  -130.793 -8.806  1.00 102.43 ? 7   ILE   J CG2 1 
ATOM   16395 C  CD1 . ILE   J  10 7   ? 50.955  -133.262 -8.706  1.00 111.44 ? 7   ILE   J CD1 1 
ATOM   16396 N  N   . ARG   J  10 8   ? 53.219  -128.105 -6.654  1.00 101.21 ? 8   ARG   J N   1 
ATOM   16397 C  CA  . ARG   J  10 8   ? 53.953  -126.891 -7.089  1.00 102.14 ? 8   ARG   J CA  1 
ATOM   16398 C  C   . ARG   J  10 8   ? 54.907  -127.281 -8.219  1.00 104.74 ? 8   ARG   J C   1 
ATOM   16399 O  O   . ARG   J  10 8   ? 55.703  -128.212 -8.013  1.00 106.74 ? 8   ARG   J O   1 
ATOM   16400 C  CB  . ARG   J  10 8   ? 54.742  -126.292 -5.922  1.00 101.70 ? 8   ARG   J CB  1 
ATOM   16401 C  CG  . ARG   J  10 8   ? 55.750  -125.232 -6.340  1.00 105.13 ? 8   ARG   J CG  1 
ATOM   16402 C  CD  . ARG   J  10 8   ? 56.371  -124.522 -5.152  1.00 104.79 ? 8   ARG   J CD  1 
ATOM   16403 N  NE  . ARG   J  10 8   ? 57.101  -125.407 -4.248  1.00 103.46 ? 8   ARG   J NE  1 
ATOM   16404 C  CZ  . ARG   J  10 8   ? 58.307  -125.926 -4.482  1.00 102.97 ? 8   ARG   J CZ  1 
ATOM   16405 N  NH1 . ARG   J  10 8   ? 58.944  -125.682 -5.616  1.00 104.42 ? 8   ARG   J NH1 1 
ATOM   16406 N  NH2 . ARG   J  10 8   ? 58.871  -126.706 -3.577  1.00 103.90 ? 8   ARG   J NH2 1 
ATOM   16407 N  N   . VAL   J  10 9   ? 54.840  -126.580 -9.352  1.00 104.53 ? 9   VAL   J N   1 
ATOM   16408 C  CA  . VAL   J  10 9   ? 55.752  -126.775 -10.519 1.00 109.29 ? 9   VAL   J CA  1 
ATOM   16409 C  C   . VAL   J  10 9   ? 56.515  -125.464 -10.763 1.00 107.74 ? 9   VAL   J C   1 
ATOM   16410 O  O   . VAL   J  10 9   ? 56.484  -124.595 -9.873  1.00 104.39 ? 9   VAL   J O   1 
ATOM   16411 C  CB  . VAL   J  10 9   ? 54.980  -127.261 -11.764 1.00 112.04 ? 9   VAL   J CB  1 
ATOM   16412 C  CG1 . VAL   J  10 9   ? 54.524  -128.702 -11.608 1.00 115.86 ? 9   VAL   J CG1 1 
ATOM   16413 C  CG2 . VAL   J  10 9   ? 53.804  -126.362 -12.111 1.00 111.89 ? 9   VAL   J CG2 1 
ATOM   16414 N  N   . GLN   J  10 10  ? 57.202  -125.352 -11.904 1.00 111.48 ? 10  GLN   J N   1 
ATOM   16415 C  CA  . GLN   J  10 10  ? 58.064  -124.200 -12.284 1.00 114.31 ? 10  GLN   J CA  1 
ATOM   16416 C  C   . GLN   J  10 10  ? 57.328  -122.882 -12.012 1.00 114.25 ? 10  GLN   J C   1 
ATOM   16417 O  O   . GLN   J  10 10  ? 57.889  -122.039 -11.284 1.00 113.28 ? 10  GLN   J O   1 
ATOM   16418 C  CB  . GLN   J  10 10  ? 58.469  -124.324 -13.757 1.00 120.49 ? 10  GLN   J CB  1 
ATOM   16419 C  CG  . GLN   J  10 10  ? 59.333  -123.181 -14.282 1.00 123.20 ? 10  GLN   J CG  1 
ATOM   16420 C  CD  . GLN   J  10 10  ? 60.800  -123.343 -13.959 1.00 125.68 ? 10  GLN   J CD  1 
ATOM   16421 O  OE1 . GLN   J  10 10  ? 61.202  -123.347 -12.798 1.00 129.24 ? 10  GLN   J OE1 1 
ATOM   16422 N  NE2 . GLN   J  10 10  ? 61.621  -123.464 -14.991 1.00 128.75 ? 10  GLN   J NE2 1 
ATOM   16423 N  N   . ASP   J  10 11  ? 56.119  -122.719 -12.562 1.00 114.59 ? 11  ASP   J N   1 
ATOM   16424 C  CA  . ASP   J  10 11  ? 55.445  -121.399 -12.700 1.00 116.58 ? 11  ASP   J CA  1 
ATOM   16425 C  C   . ASP   J  10 11  ? 54.064  -121.370 -12.035 1.00 109.32 ? 11  ASP   J C   1 
ATOM   16426 O  O   . ASP   J  10 11  ? 53.435  -120.299 -12.085 1.00 107.08 ? 11  ASP   J O   1 
ATOM   16427 C  CB  . ASP   J  10 11  ? 55.287  -121.024 -14.176 1.00 121.35 ? 11  ASP   J CB  1 
ATOM   16428 C  CG  . ASP   J  10 11  ? 56.606  -120.911 -14.919 1.00 130.24 ? 11  ASP   J CG  1 
ATOM   16429 O  OD1 . ASP   J  10 11  ? 57.497  -120.194 -14.421 1.00 133.26 ? 11  ASP   J OD1 1 
ATOM   16430 O  OD2 . ASP   J  10 11  ? 56.733  -121.545 -15.986 1.00 142.66 ? 11  ASP   J OD2 1 
ATOM   16431 N  N   . SER   J  10 12  ? 53.587  -122.469 -11.445 1.00 107.31 ? 12  SER   J N   1 
ATOM   16432 C  CA  . SER   J  10 12  ? 52.205  -122.540 -10.904 1.00 105.61 ? 12  SER   J CA  1 
ATOM   16433 C  C   . SER   J  10 12  ? 52.086  -123.560 -9.771  1.00 103.39 ? 12  SER   J C   1 
ATOM   16434 O  O   . SER   J  10 12  ? 52.976  -124.421 -9.636  1.00 105.64 ? 12  SER   J O   1 
ATOM   16435 C  CB  . SER   J  10 12  ? 51.216  -122.833 -12.001 1.00 108.26 ? 12  SER   J CB  1 
ATOM   16436 O  OG  . SER   J  10 12  ? 51.477  -124.093 -12.598 1.00 112.68 ? 12  SER   J OG  1 
ATOM   16437 N  N   . VAL   J  10 13  ? 51.013  -123.424 -8.987  1.00 101.66 ? 13  VAL   J N   1 
ATOM   16438 C  CA  . VAL   J  10 13  ? 50.543  -124.406 -7.968  1.00 104.47 ? 13  VAL   J CA  1 
ATOM   16439 C  C   . VAL   J  10 13  ? 49.212  -124.982 -8.462  1.00 102.35 ? 13  VAL   J C   1 
ATOM   16440 O  O   . VAL   J  10 13  ? 48.326  -124.186 -8.830  1.00 101.97 ? 13  VAL   J O   1 
ATOM   16441 C  CB  . VAL   J  10 13  ? 50.378  -123.762 -6.579  1.00 104.27 ? 13  VAL   J CB  1 
ATOM   16442 C  CG1 . VAL   J  10 13  ? 50.158  -124.818 -5.507  1.00 107.07 ? 13  VAL   J CG1 1 
ATOM   16443 C  CG2 . VAL   J  10 13  ? 51.552  -122.867 -6.216  1.00 104.39 ? 13  VAL   J CG2 1 
ATOM   16444 N  N   . ILE   J  10 14  ? 49.088  -126.311 -8.472  1.00 104.97 ? 14  ILE   J N   1 
ATOM   16445 C  CA  . ILE   J  10 14  ? 47.859  -127.039 -8.905  1.00 103.75 ? 14  ILE   J CA  1 
ATOM   16446 C  C   . ILE   J  10 14  ? 47.269  -127.731 -7.672  1.00 101.39 ? 14  ILE   J C   1 
ATOM   16447 O  O   . ILE   J  10 14  ? 48.017  -128.467 -7.004  1.00 99.61  ? 14  ILE   J O   1 
ATOM   16448 C  CB  . ILE   J  10 14  ? 48.177  -128.030 -10.046 1.00 106.28 ? 14  ILE   J CB  1 
ATOM   16449 C  CG1 . ILE   J  10 14  ? 49.071  -127.403 -11.121 1.00 107.76 ? 14  ILE   J CG1 1 
ATOM   16450 C  CG2 . ILE   J  10 14  ? 46.892  -128.585 -10.644 1.00 106.78 ? 14  ILE   J CG2 1 
ATOM   16451 C  CD1 . ILE   J  10 14  ? 49.776  -128.406 -12.006 1.00 110.13 ? 14  ILE   J CD1 1 
ATOM   16452 N  N   . LEU   J  10 15  ? 45.993  -127.467 -7.368  1.00 99.84  ? 15  LEU   J N   1 
ATOM   16453 C  CA  . LEU   J  10 15  ? 45.232  -128.127 -6.272  1.00 100.10 ? 15  LEU   J CA  1 
ATOM   16454 C  C   . LEU   J  10 15  ? 44.126  -128.999 -6.871  1.00 100.91 ? 15  LEU   J C   1 
ATOM   16455 O  O   . LEU   J  10 15  ? 43.293  -128.453 -7.618  1.00 101.16 ? 15  LEU   J O   1 
ATOM   16456 C  CB  . LEU   J  10 15  ? 44.609  -127.073 -5.352  1.00 102.03 ? 15  LEU   J CB  1 
ATOM   16457 C  CG  . LEU   J  10 15  ? 45.566  -126.119 -4.638  1.00 104.53 ? 15  LEU   J CG  1 
ATOM   16458 C  CD1 . LEU   J  10 15  ? 44.813  -125.336 -3.573  1.00 104.89 ? 15  LEU   J CD1 1 
ATOM   16459 C  CD2 . LEU   J  10 15  ? 46.745  -126.853 -4.013  1.00 106.04 ? 15  LEU   J CD2 1 
ATOM   16460 N  N   . ALA   J  10 16  ? 44.119  -130.291 -6.527  1.00 100.72 ? 16  ALA   J N   1 
ATOM   16461 C  CA  . ALA   J  10 16  ? 43.044  -131.263 -6.837  1.00 98.93  ? 16  ALA   J CA  1 
ATOM   16462 C  C   . ALA   J  10 16  ? 42.321  -131.622 -5.537  1.00 96.48  ? 16  ALA   J C   1 
ATOM   16463 O  O   . ALA   J  10 16  ? 43.012  -131.888 -4.535  1.00 97.36  ? 16  ALA   J O   1 
ATOM   16464 C  CB  . ALA   J  10 16  ? 43.620  -132.489 -7.494  1.00 99.73  ? 16  ALA   J CB  1 
ATOM   16465 N  N   . SER   J  10 17  ? 40.986  -131.619 -5.558  1.00 95.11  ? 17  SER   J N   1 
ATOM   16466 C  CA  . SER   J  10 17  ? 40.123  -131.806 -4.363  1.00 96.24  ? 17  SER   J CA  1 
ATOM   16467 C  C   . SER   J  10 17  ? 38.893  -132.636 -4.746  1.00 94.08  ? 17  SER   J C   1 
ATOM   16468 O  O   . SER   J  10 17  ? 38.199  -132.240 -5.697  1.00 97.48  ? 17  SER   J O   1 
ATOM   16469 C  CB  . SER   J  10 17  ? 39.737  -130.469 -3.770  1.00 100.89 ? 17  SER   J CB  1 
ATOM   16470 O  OG  . SER   J  10 17  ? 40.860  -129.600 -3.690  1.00 105.24 ? 17  SER   J OG  1 
ATOM   16471 N  N   . SER   J  10 18  ? 38.645  -133.741 -4.032  1.00 92.31  ? 18  SER   J N   1 
ATOM   16472 C  CA  . SER   J  10 18  ? 37.551  -134.712 -4.309  1.00 92.69  ? 18  SER   J CA  1 
ATOM   16473 C  C   . SER   J  10 18  ? 36.191  -134.007 -4.263  1.00 92.56  ? 18  SER   J C   1 
ATOM   16474 O  O   . SER   J  10 18  ? 36.055  -133.030 -3.506  1.00 92.51  ? 18  SER   J O   1 
ATOM   16475 C  CB  . SER   J  10 18  ? 37.593  -135.888 -3.362  1.00 90.73  ? 18  SER   J CB  1 
ATOM   16476 O  OG  . SER   J  10 18  ? 37.582  -135.467 -2.007  1.00 89.66  ? 18  SER   J OG  1 
ATOM   16477 N  N   . LYS   J  10 19  ? 35.224  -134.497 -5.044  1.00 93.13  ? 19  LYS   J N   1 
ATOM   16478 C  CA  . LYS   J  10 19  ? 33.914  -133.831 -5.282  1.00 93.81  ? 19  LYS   J CA  1 
ATOM   16479 C  C   . LYS   J  10 19  ? 32.802  -134.464 -4.435  1.00 93.59  ? 19  LYS   J C   1 
ATOM   16480 O  O   . LYS   J  10 19  ? 31.694  -133.896 -4.414  1.00 93.51  ? 19  LYS   J O   1 
ATOM   16481 C  CB  . LYS   J  10 19  ? 33.546  -133.910 -6.766  1.00 96.45  ? 19  LYS   J CB  1 
ATOM   16482 C  CG  . LYS   J  10 19  ? 34.442  -133.109 -7.699  1.00 97.77  ? 19  LYS   J CG  1 
ATOM   16483 C  CD  . LYS   J  10 19  ? 33.807  -132.835 -9.045  1.00 100.90 ? 19  LYS   J CD  1 
ATOM   16484 C  CE  . LYS   J  10 19  ? 33.903  -134.004 -9.998  1.00 103.88 ? 19  LYS   J CE  1 
ATOM   16485 N  NZ  . LYS   J  10 19  ? 33.014  -133.819 -11.169 1.00 108.38 ? 19  LYS   J NZ  1 
ATOM   16486 N  N   . ALA   J  10 20  ? 33.066  -135.590 -3.769  1.00 93.80  ? 20  ALA   J N   1 
ATOM   16487 C  CA  . ALA   J  10 20  ? 32.045  -136.356 -3.016  1.00 94.33  ? 20  ALA   J CA  1 
ATOM   16488 C  C   . ALA   J  10 20  ? 31.825  -135.724 -1.640  1.00 91.55  ? 20  ALA   J C   1 
ATOM   16489 O  O   . ALA   J  10 20  ? 32.824  -135.360 -0.989  1.00 91.25  ? 20  ALA   J O   1 
ATOM   16490 C  CB  . ALA   J  10 20  ? 32.459  -137.798 -2.882  1.00 95.70  ? 20  ALA   J CB  1 
ATOM   16491 N  N   . VAL   J  10 21  ? 30.560  -135.599 -1.230  1.00 90.86  ? 21  VAL   J N   1 
ATOM   16492 C  CA  . VAL   J  10 21  ? 30.154  -135.351 0.184   1.00 89.22  ? 21  VAL   J CA  1 
ATOM   16493 C  C   . VAL   J  10 21  ? 29.280  -136.527 0.615   1.00 93.53  ? 21  VAL   J C   1 
ATOM   16494 O  O   . VAL   J  10 21  ? 28.098  -136.568 0.210   1.00 94.51  ? 21  VAL   J O   1 
ATOM   16495 C  CB  . VAL   J  10 21  ? 29.424  -134.009 0.370   1.00 88.30  ? 21  VAL   J CB  1 
ATOM   16496 C  CG1 . VAL   J  10 21  ? 28.957  -133.827 1.808   1.00 85.88  ? 21  VAL   J CG1 1 
ATOM   16497 C  CG2 . VAL   J  10 21  ? 30.294  -132.841 -0.063  1.00 86.95  ? 21  VAL   J CG2 1 
ATOM   16498 N  N   . THR   J  10 22  ? 29.862  -137.448 1.388   1.00 94.67  ? 22  THR   J N   1 
ATOM   16499 C  CA  . THR   J  10 22  ? 29.197  -138.671 1.900   1.00 98.02  ? 22  THR   J CA  1 
ATOM   16500 C  C   . THR   J  10 22  ? 28.806  -138.442 3.361   1.00 96.77  ? 22  THR   J C   1 
ATOM   16501 O  O   . THR   J  10 22  ? 29.633  -137.893 4.112   1.00 92.79  ? 22  THR   J O   1 
ATOM   16502 C  CB  . THR   J  10 22  ? 30.099  -139.901 1.740   1.00 99.98  ? 22  THR   J CB  1 
ATOM   16503 O  OG1 . THR   J  10 22  ? 30.497  -139.997 0.371   1.00 97.61  ? 22  THR   J OG1 1 
ATOM   16504 C  CG2 . THR   J  10 22  ? 29.413  -141.182 2.163   1.00 103.28 ? 22  THR   J CG2 1 
ATOM   16505 N  N   . ARG   J  10 23  ? 27.582  -138.835 3.722   1.00 103.03 ? 23  ARG   J N   1 
ATOM   16506 C  CA  . ARG   J  10 23  ? 27.084  -138.892 5.121   1.00 107.99 ? 23  ARG   J CA  1 
ATOM   16507 C  C   . ARG   J  10 23  ? 26.361  -140.230 5.318   1.00 111.61 ? 23  ARG   J C   1 
ATOM   16508 O  O   . ARG   J  10 23  ? 25.311  -140.432 4.672   1.00 116.00 ? 23  ARG   J O   1 
ATOM   16509 C  CB  . ARG   J  10 23  ? 26.151  -137.710 5.402   1.00 109.63 ? 23  ARG   J CB  1 
ATOM   16510 C  CG  . ARG   J  10 23  ? 26.553  -136.851 6.593   1.00 110.53 ? 23  ARG   J CG  1 
ATOM   16511 C  CD  . ARG   J  10 23  ? 27.258  -135.566 6.198   1.00 112.24 ? 23  ARG   J CD  1 
ATOM   16512 N  NE  . ARG   J  10 23  ? 28.653  -135.774 5.833   1.00 112.63 ? 23  ARG   J NE  1 
ATOM   16513 C  CZ  . ARG   J  10 23  ? 29.516  -134.801 5.552   1.00 114.34 ? 23  ARG   J CZ  1 
ATOM   16514 N  NH1 . ARG   J  10 23  ? 30.766  -135.099 5.234   1.00 116.55 ? 23  ARG   J NH1 1 
ATOM   16515 N  NH2 . ARG   J  10 23  ? 29.134  -133.535 5.589   1.00 115.72 ? 23  ARG   J NH2 1 
ATOM   16516 N  N   . GLY   J  10 24  ? 26.909  -141.110 6.163   1.00 112.08 ? 24  GLY   J N   1 
ATOM   16517 C  CA  . GLY   J  10 24  ? 26.399  -142.478 6.380   1.00 111.94 ? 24  GLY   J CA  1 
ATOM   16518 C  C   . GLY   J  10 24  ? 26.593  -143.336 5.143   1.00 112.04 ? 24  GLY   J C   1 
ATOM   16519 O  O   . GLY   J  10 24  ? 27.717  -143.333 4.600   1.00 110.73 ? 24  GLY   J O   1 
ATOM   16520 N  N   . ILE   J  10 25  ? 25.536  -144.025 4.697   1.00 112.63 ? 25  ILE   J N   1 
ATOM   16521 C  CA  . ILE   J  10 25  ? 25.565  -144.947 3.518   1.00 112.50 ? 25  ILE   J CA  1 
ATOM   16522 C  C   . ILE   J  10 25  ? 24.999  -144.238 2.278   1.00 110.71 ? 25  ILE   J C   1 
ATOM   16523 O  O   . ILE   J  10 25  ? 24.553  -144.953 1.357   1.00 111.71 ? 25  ILE   J O   1 
ATOM   16524 C  CB  . ILE   J  10 25  ? 24.816  -146.264 3.819   1.00 114.39 ? 25  ILE   J CB  1 
ATOM   16525 C  CG1 . ILE   J  10 25  ? 23.335  -146.045 4.147   1.00 114.10 ? 25  ILE   J CG1 1 
ATOM   16526 C  CG2 . ILE   J  10 25  ? 25.525  -147.042 4.917   1.00 113.78 ? 25  ILE   J CG2 1 
ATOM   16527 C  CD1 . ILE   J  10 25  ? 22.476  -147.270 3.941   1.00 117.04 ? 25  ILE   J CD1 1 
ATOM   16528 N  N   . SER   J  10 26  ? 25.028  -142.900 2.238   1.00 107.08 ? 26  SER   J N   1 
ATOM   16529 C  CA  . SER   J  10 26  ? 24.537  -142.080 1.096   1.00 103.79 ? 26  SER   J CA  1 
ATOM   16530 C  C   . SER   J  10 26  ? 25.592  -141.056 0.673   1.00 101.68 ? 26  SER   J C   1 
ATOM   16531 O  O   . SER   J  10 26  ? 26.059  -140.294 1.544   1.00 99.60  ? 26  SER   J O   1 
ATOM   16532 C  CB  . SER   J  10 26  ? 23.246  -141.383 1.428   1.00 102.32 ? 26  SER   J CB  1 
ATOM   16533 O  OG  . SER   J  10 26  ? 22.168  -142.304 1.507   1.00 100.42 ? 26  SER   J OG  1 
ATOM   16534 N  N   . VAL   J  10 27  ? 25.928  -141.033 -0.620  1.00 100.91 ? 27  VAL   J N   1 
ATOM   16535 C  CA  . VAL   J  10 27  ? 26.700  -139.931 -1.265  1.00 100.38 ? 27  VAL   J CA  1 
ATOM   16536 C  C   . VAL   J  10 27  ? 25.698  -138.814 -1.577  1.00 103.04 ? 27  VAL   J C   1 
ATOM   16537 O  O   . VAL   J  10 27  ? 24.943  -138.963 -2.557  1.00 105.19 ? 27  VAL   J O   1 
ATOM   16538 C  CB  . VAL   J  10 27  ? 27.446  -140.402 -2.529  1.00 100.59 ? 27  VAL   J CB  1 
ATOM   16539 C  CG1 . VAL   J  10 27  ? 28.263  -139.279 -3.150  1.00 100.02 ? 27  VAL   J CG1 1 
ATOM   16540 C  CG2 . VAL   J  10 27  ? 28.337  -141.603 -2.251  1.00 100.46 ? 27  VAL   J CG2 1 
ATOM   16541 N  N   . LEU   J  10 28  ? 25.678  -137.758 -0.757  1.00 102.87 ? 28  LEU   J N   1 
ATOM   16542 C  CA  . LEU   J  10 28  ? 24.669  -136.666 -0.829  1.00 104.59 ? 28  LEU   J CA  1 
ATOM   16543 C  C   . LEU   J  10 28  ? 24.947  -135.767 -2.039  1.00 102.69 ? 28  LEU   J C   1 
ATOM   16544 O  O   . LEU   J  10 28  ? 23.973  -135.223 -2.593  1.00 104.36 ? 28  LEU   J O   1 
ATOM   16545 C  CB  . LEU   J  10 28  ? 24.691  -135.854 0.472   1.00 104.45 ? 28  LEU   J CB  1 
ATOM   16546 C  CG  . LEU   J  10 28  ? 24.253  -136.600 1.732   1.00 109.45 ? 28  LEU   J CG  1 
ATOM   16547 C  CD1 . LEU   J  10 28  ? 24.373  -135.698 2.952   1.00 109.70 ? 28  LEU   J CD1 1 
ATOM   16548 C  CD2 . LEU   J  10 28  ? 22.830  -137.131 1.601   1.00 112.33 ? 28  LEU   J CD2 1 
ATOM   16549 N  N   . LYS   J  10 29  ? 26.215  -135.618 -2.435  1.00 101.99 ? 29  LYS   J N   1 
ATOM   16550 C  CA  . LYS   J  10 29  ? 26.631  -134.681 -3.511  1.00 103.71 ? 29  LYS   J CA  1 
ATOM   16551 C  C   . LYS   J  10 29  ? 27.922  -135.179 -4.169  1.00 100.48 ? 29  LYS   J C   1 
ATOM   16552 O  O   . LYS   J  10 29  ? 28.769  -135.741 -3.453  1.00 98.39  ? 29  LYS   J O   1 
ATOM   16553 C  CB  . LYS   J  10 29  ? 26.817  -133.276 -2.932  1.00 106.06 ? 29  LYS   J CB  1 
ATOM   16554 C  CG  . LYS   J  10 29  ? 26.757  -132.157 -3.960  1.00 110.11 ? 29  LYS   J CG  1 
ATOM   16555 C  CD  . LYS   J  10 29  ? 26.775  -130.768 -3.369  1.00 112.20 ? 29  LYS   J CD  1 
ATOM   16556 C  CE  . LYS   J  10 29  ? 26.925  -129.705 -4.435  1.00 115.48 ? 29  LYS   J CE  1 
ATOM   16557 N  NZ  . LYS   J  10 29  ? 26.949  -128.345 -3.850  1.00 118.89 ? 29  LYS   J NZ  1 
ATOM   16558 N  N   . ASP   J  10 30  ? 28.061  -134.946 -5.478  1.00 101.16 ? 30  ASP   J N   1 
ATOM   16559 C  CA  . ASP   J  10 30  ? 29.189  -135.437 -6.316  1.00 104.14 ? 30  ASP   J CA  1 
ATOM   16560 C  C   . ASP   J  10 30  ? 29.822  -134.281 -7.107  1.00 104.46 ? 30  ASP   J C   1 
ATOM   16561 O  O   . ASP   J  10 30  ? 30.505  -134.569 -8.110  1.00 106.18 ? 30  ASP   J O   1 
ATOM   16562 C  CB  . ASP   J  10 30  ? 28.707  -136.544 -7.259  1.00 110.22 ? 30  ASP   J CB  1 
ATOM   16563 C  CG  . ASP   J  10 30  ? 27.628  -136.109 -8.242  1.00 112.69 ? 30  ASP   J CG  1 
ATOM   16564 O  OD1 . ASP   J  10 30  ? 27.186  -134.945 -8.161  1.00 113.95 ? 30  ASP   J OD1 1 
ATOM   16565 O  OD2 . ASP   J  10 30  ? 27.231  -136.943 -9.079  1.00 119.89 ? 30  ASP   J OD2 1 
ATOM   16566 N  N   . SER   J  10 31  ? 29.613  -133.030 -6.677  1.00 102.05 ? 31  SER   J N   1 
ATOM   16567 C  CA  . SER   J  10 31  ? 30.080  -131.803 -7.375  1.00 102.68 ? 31  SER   J CA  1 
ATOM   16568 C  C   . SER   J  10 31  ? 30.548  -130.737 -6.376  1.00 101.64 ? 31  SER   J C   1 
ATOM   16569 O  O   . SER   J  10 31  ? 30.572  -129.552 -6.759  1.00 101.91 ? 31  SER   J O   1 
ATOM   16570 C  CB  . SER   J  10 31  ? 28.985  -131.266 -8.254  1.00 104.78 ? 31  SER   J CB  1 
ATOM   16571 O  OG  . SER   J  10 31  ? 27.872  -130.865 -7.468  1.00 105.52 ? 31  SER   J OG  1 
ATOM   16572 N  N   . ASP   J  10 32  ? 30.927  -131.133 -5.157  1.00 100.40 ? 32  ASP   J N   1 
ATOM   16573 C  CA  . ASP   J  10 32  ? 31.290  -130.196 -4.060  1.00 101.07 ? 32  ASP   J CA  1 
ATOM   16574 C  C   . ASP   J  10 32  ? 32.677  -129.605 -4.339  1.00 99.66  ? 32  ASP   J C   1 
ATOM   16575 O  O   . ASP   J  10 32  ? 33.605  -130.375 -4.651  1.00 95.64  ? 32  ASP   J O   1 
ATOM   16576 C  CB  . ASP   J  10 32  ? 31.243  -130.882 -2.692  1.00 102.16 ? 32  ASP   J CB  1 
ATOM   16577 C  CG  . ASP   J  10 32  ? 31.496  -129.940 -1.524  1.00 103.34 ? 32  ASP   J CG  1 
ATOM   16578 O  OD1 . ASP   J  10 32  ? 30.851  -128.875 -1.485  1.00 108.65 ? 32  ASP   J OD1 1 
ATOM   16579 O  OD2 . ASP   J  10 32  ? 32.340  -130.275 -0.664  1.00 100.54 ? 32  ASP   J OD2 1 
ATOM   16580 N  N   . ASP   J  10 33  ? 32.801  -128.280 -4.223  1.00 101.71 ? 33  ASP   J N   1 
ATOM   16581 C  CA  . ASP   J  10 33  ? 34.075  -127.537 -4.413  1.00 107.47 ? 33  ASP   J CA  1 
ATOM   16582 C  C   . ASP   J  10 33  ? 34.687  -127.250 -3.037  1.00 103.40 ? 33  ASP   J C   1 
ATOM   16583 O  O   . ASP   J  10 33  ? 34.233  -126.299 -2.370  1.00 99.92  ? 33  ASP   J O   1 
ATOM   16584 C  CB  . ASP   J  10 33  ? 33.856  -126.254 -5.218  1.00 109.50 ? 33  ASP   J CB  1 
ATOM   16585 C  CG  . ASP   J  10 33  ? 35.147  -125.606 -5.695  1.00 116.59 ? 33  ASP   J CG  1 
ATOM   16586 O  OD1 . ASP   J  10 33  ? 36.215  -126.252 -5.571  1.00 115.56 ? 33  ASP   J OD1 1 
ATOM   16587 O  OD2 . ASP   J  10 33  ? 35.079  -124.459 -6.188  1.00 121.44 ? 33  ASP   J OD2 1 
ATOM   16588 N  N   . LYS   J  10 34  ? 35.683  -128.044 -2.635  1.00 107.56 ? 34  LYS   J N   1 
ATOM   16589 C  CA  . LYS   J  10 34  ? 36.325  -127.975 -1.294  1.00 101.85 ? 34  LYS   J CA  1 
ATOM   16590 C  C   . LYS   J  10 34  ? 37.474  -126.964 -1.331  1.00 97.52  ? 34  LYS   J C   1 
ATOM   16591 O  O   . LYS   J  10 34  ? 38.600  -127.331 -0.936  1.00 91.04  ? 34  LYS   J O   1 
ATOM   16592 C  CB  . LYS   J  10 34  ? 36.818  -129.363 -0.876  1.00 102.40 ? 34  LYS   J CB  1 
ATOM   16593 C  CG  . LYS   J  10 34  ? 35.711  -130.376 -0.637  1.00 104.33 ? 34  LYS   J CG  1 
ATOM   16594 C  CD  . LYS   J  10 34  ? 36.197  -131.804 -0.607  1.00 105.05 ? 34  LYS   J CD  1 
ATOM   16595 C  CE  . LYS   J  10 34  ? 35.081  -132.799 -0.367  1.00 107.75 ? 34  LYS   J CE  1 
ATOM   16596 N  NZ  . LYS   J  10 34  ? 33.987  -132.686 -1.359  1.00 110.65 ? 34  LYS   J NZ  1 
ATOM   16597 N  N   . THR   J  10 35  ? 37.194  -125.735 -1.773  1.00 96.51  ? 35  THR   J N   1 
ATOM   16598 C  CA  . THR   J  10 35  ? 38.207  -124.658 -1.921  1.00 93.99  ? 35  THR   J CA  1 
ATOM   16599 C  C   . THR   J  10 35  ? 37.556  -123.283 -1.711  1.00 91.22  ? 35  THR   J C   1 
ATOM   16600 O  O   . THR   J  10 35  ? 36.350  -123.134 -1.998  1.00 85.60  ? 35  THR   J O   1 
ATOM   16601 C  CB  . THR   J  10 35  ? 38.920  -124.772 -3.276  1.00 99.40  ? 35  THR   J CB  1 
ATOM   16602 O  OG1 . THR   J  10 35  ? 40.267  -124.323 -3.121  1.00 99.60  ? 35  THR   J OG1 1 
ATOM   16603 C  CG2 . THR   J  10 35  ? 38.244  -123.982 -4.376  1.00 99.54  ? 35  THR   J CG2 1 
ATOM   16604 N  N   . ARG   J  10 36  ? 38.340  -122.327 -1.210  1.00 87.16  ? 36  ARG   J N   1 
ATOM   16605 C  CA  . ARG   J  10 36  ? 37.989  -120.885 -1.165  1.00 86.00  ? 36  ARG   J CA  1 
ATOM   16606 C  C   . ARG   J  10 36  ? 39.164  -120.072 -1.707  1.00 85.03  ? 36  ARG   J C   1 
ATOM   16607 O  O   . ARG   J  10 36  ? 40.325  -120.447 -1.429  1.00 83.69  ? 36  ARG   J O   1 
ATOM   16608 C  CB  . ARG   J  10 36  ? 37.654  -120.431 0.259   1.00 84.16  ? 36  ARG   J CB  1 
ATOM   16609 C  CG  . ARG   J  10 36  ? 36.363  -121.008 0.822   1.00 84.48  ? 36  ARG   J CG  1 
ATOM   16610 C  CD  . ARG   J  10 36  ? 35.145  -120.759 -0.046  1.00 87.61  ? 36  ARG   J CD  1 
ATOM   16611 N  NE  . ARG   J  10 36  ? 34.262  -121.921 -0.030  1.00 87.84  ? 36  ARG   J NE  1 
ATOM   16612 C  CZ  . ARG   J  10 36  ? 33.040  -121.961 0.498   1.00 88.92  ? 36  ARG   J CZ  1 
ATOM   16613 N  NH1 . ARG   J  10 36  ? 32.506  -120.888 1.059   1.00 90.99  ? 36  ARG   J NH1 1 
ATOM   16614 N  NH2 . ARG   J  10 36  ? 32.344  -123.084 0.448   1.00 87.61  ? 36  ARG   J NH2 1 
ATOM   16615 N  N   . GLN   J  10 37  ? 38.861  -119.009 -2.455  1.00 84.33  ? 37  GLN   J N   1 
ATOM   16616 C  CA  . GLN   J  10 37  ? 39.848  -117.986 -2.879  1.00 85.26  ? 37  GLN   J CA  1 
ATOM   16617 C  C   . GLN   J  10 37  ? 40.005  -116.983 -1.733  1.00 83.89  ? 37  GLN   J C   1 
ATOM   16618 O  O   . GLN   J  10 37  ? 39.005  -116.331 -1.386  1.00 84.52  ? 37  GLN   J O   1 
ATOM   16619 C  CB  . GLN   J  10 37  ? 39.387  -117.313 -4.171  1.00 86.88  ? 37  GLN   J CB  1 
ATOM   16620 C  CG  . GLN   J  10 37  ? 40.370  -116.273 -4.685  1.00 90.62  ? 37  GLN   J CG  1 
ATOM   16621 C  CD  . GLN   J  10 37  ? 39.920  -115.599 -5.957  1.00 95.48  ? 37  GLN   J CD  1 
ATOM   16622 O  OE1 . GLN   J  10 37  ? 40.014  -114.381 -6.091  1.00 103.02 ? 37  GLN   J OE1 1 
ATOM   16623 N  NE2 . GLN   J  10 37  ? 39.426  -116.380 -6.905  1.00 96.44  ? 37  GLN   J NE2 1 
ATOM   16624 N  N   . LEU   J  10 38  ? 41.201  -116.886 -1.150  1.00 84.97  ? 38  LEU   J N   1 
ATOM   16625 C  CA  . LEU   J  10 38  ? 41.500  -115.946 -0.036  1.00 91.55  ? 38  LEU   J CA  1 
ATOM   16626 C  C   . LEU   J  10 38  ? 41.866  -114.574 -0.616  1.00 96.71  ? 38  LEU   J C   1 
ATOM   16627 O  O   . LEU   J  10 38  ? 41.456  -113.551 -0.025  1.00 105.62 ? 38  LEU   J O   1 
ATOM   16628 C  CB  . LEU   J  10 38  ? 42.634  -116.517 0.821   1.00 90.31  ? 38  LEU   J CB  1 
ATOM   16629 C  CG  . LEU   J  10 38  ? 42.428  -117.943 1.339   1.00 88.96  ? 38  LEU   J CG  1 
ATOM   16630 C  CD1 . LEU   J  10 38  ? 43.544  -118.330 2.299   1.00 88.39  ? 38  LEU   J CD1 1 
ATOM   16631 C  CD2 . LEU   J  10 38  ? 41.073  -118.103 2.015   1.00 87.55  ? 38  LEU   J CD2 1 
ATOM   16632 N  N   . SER   J  10 39  ? 42.604  -114.557 -1.730  1.00 99.42  ? 39  SER   J N   1 
ATOM   16633 C  CA  . SER   J  10 39  ? 42.984  -113.334 -2.484  1.00 98.82  ? 39  SER   J CA  1 
ATOM   16634 C  C   . SER   J  10 39  ? 43.157  -113.687 -3.961  1.00 101.98 ? 39  SER   J C   1 
ATOM   16635 O  O   . SER   J  10 39  ? 43.166  -114.866 -4.312  1.00 104.59 ? 39  SER   J O   1 
ATOM   16636 C  CB  . SER   J  10 39  ? 44.223  -112.715 -1.884  1.00 96.83  ? 39  SER   J CB  1 
ATOM   16637 O  OG  . SER   J  10 39  ? 45.379  -113.488 -2.168  1.00 96.20  ? 39  SER   J OG  1 
ATOM   16638 N  N   . PRO   J  10 40  ? 43.283  -112.696 -4.876  1.00 101.48 ? 40  PRO   J N   1 
ATOM   16639 C  CA  . PRO   J  10 40  ? 43.426  -112.973 -6.308  1.00 101.43 ? 40  PRO   J CA  1 
ATOM   16640 C  C   . PRO   J  10 40  ? 44.466  -114.041 -6.685  1.00 101.00 ? 40  PRO   J C   1 
ATOM   16641 O  O   . PRO   J  10 40  ? 44.227  -114.740 -7.653  1.00 97.97  ? 40  PRO   J O   1 
ATOM   16642 C  CB  . PRO   J  10 40  ? 43.868  -111.619 -6.879  1.00 102.23 ? 40  PRO   J CB  1 
ATOM   16643 C  CG  . PRO   J  10 40  ? 43.214  -110.612 -5.962  1.00 103.02 ? 40  PRO   J CG  1 
ATOM   16644 C  CD  . PRO   J  10 40  ? 43.272  -111.252 -4.591  1.00 101.53 ? 40  PRO   J CD  1 
ATOM   16645 N  N   . HIS   J  10 41  ? 45.576  -114.131 -5.938  1.00 99.71  ? 41  HIS   J N   1 
ATOM   16646 C  CA  . HIS   J  10 41  ? 46.714  -115.057 -6.199  1.00 98.58  ? 41  HIS   J CA  1 
ATOM   16647 C  C   . HIS   J  10 41  ? 46.929  -116.029 -5.028  1.00 98.09  ? 41  HIS   J C   1 
ATOM   16648 O  O   . HIS   J  10 41  ? 48.060  -116.543 -4.906  1.00 102.01 ? 41  HIS   J O   1 
ATOM   16649 C  CB  . HIS   J  10 41  ? 47.996  -114.261 -6.488  1.00 99.62  ? 41  HIS   J CB  1 
ATOM   16650 C  CG  . HIS   J  10 41  ? 47.877  -113.314 -7.634  1.00 100.14 ? 41  HIS   J CG  1 
ATOM   16651 N  ND1 . HIS   J  10 41  ? 47.670  -111.962 -7.458  1.00 98.92  ? 41  HIS   J ND1 1 
ATOM   16652 C  CD2 . HIS   J  10 41  ? 47.941  -113.517 -8.968  1.00 102.21 ? 41  HIS   J CD2 1 
ATOM   16653 C  CE1 . HIS   J  10 41  ? 47.610  -111.371 -8.633  1.00 100.09 ? 41  HIS   J CE1 1 
ATOM   16654 N  NE2 . HIS   J  10 41  ? 47.774  -112.303 -9.576  1.00 102.14 ? 41  HIS   J NE2 1 
ATOM   16655 N  N   . THR   J  10 42  ? 45.904  -116.286 -4.207  1.00 95.09  ? 42  THR   J N   1 
ATOM   16656 C  CA  . THR   J  10 42  ? 45.956  -117.289 -3.106  1.00 94.30  ? 42  THR   J CA  1 
ATOM   16657 C  C   . THR   J  10 42  ? 44.657  -118.100 -3.045  1.00 93.88  ? 42  THR   J C   1 
ATOM   16658 O  O   . THR   J  10 42  ? 43.573  -117.487 -2.919  1.00 94.18  ? 42  THR   J O   1 
ATOM   16659 C  CB  . THR   J  10 42  ? 46.249  -116.634 -1.753  1.00 92.28  ? 42  THR   J CB  1 
ATOM   16660 O  OG1 . THR   J  10 42  ? 47.576  -116.112 -1.820  1.00 92.12  ? 42  THR   J OG1 1 
ATOM   16661 C  CG2 . THR   J  10 42  ? 46.135  -117.603 -0.597  1.00 91.98  ? 42  THR   J CG2 1 
ATOM   16662 N  N   . LEU   J  10 43  ? 44.794  -119.432 -3.089  1.00 92.47  ? 43  LEU   J N   1 
ATOM   16663 C  CA  . LEU   J  10 43  ? 43.694  -120.430 -3.018  1.00 88.49  ? 43  LEU   J CA  1 
ATOM   16664 C  C   . LEU   J  10 43  ? 43.980  -121.385 -1.856  1.00 86.34  ? 43  LEU   J C   1 
ATOM   16665 O  O   . LEU   J  10 43  ? 45.160  -121.748 -1.674  1.00 85.38  ? 43  LEU   J O   1 
ATOM   16666 C  CB  . LEU   J  10 43  ? 43.630  -121.186 -4.350  1.00 87.21  ? 43  LEU   J CB  1 
ATOM   16667 C  CG  . LEU   J  10 43  ? 42.468  -122.166 -4.514  1.00 86.46  ? 43  LEU   J CG  1 
ATOM   16668 C  CD1 . LEU   J  10 43  ? 41.141  -121.431 -4.614  1.00 87.08  ? 43  LEU   J CD1 1 
ATOM   16669 C  CD2 . LEU   J  10 43  ? 42.674  -123.041 -5.740  1.00 87.36  ? 43  LEU   J CD2 1 
ATOM   16670 N  N   . MET   J  10 44  ? 42.943  -121.767 -1.107  1.00 86.27  ? 44  MET   J N   1 
ATOM   16671 C  CA  . MET   J  10 44  ? 43.040  -122.719 0.033   1.00 85.71  ? 44  MET   J CA  1 
ATOM   16672 C  C   . MET   J  10 44  ? 42.014  -123.843 -0.145  1.00 85.07  ? 44  MET   J C   1 
ATOM   16673 O  O   . MET   J  10 44  ? 40.809  -123.540 -0.215  1.00 79.65  ? 44  MET   J O   1 
ATOM   16674 C  CB  . MET   J  10 44  ? 42.784  -122.016 1.371   1.00 85.64  ? 44  MET   J CB  1 
ATOM   16675 C  CG  . MET   J  10 44  ? 43.010  -122.915 2.574   1.00 85.95  ? 44  MET   J CG  1 
ATOM   16676 S  SD  . MET   J  10 44  ? 43.026  -122.024 4.158   1.00 85.26  ? 44  MET   J SD  1 
ATOM   16677 C  CE  . MET   J  10 44  ? 41.267  -121.858 4.458   1.00 84.79  ? 44  MET   J CE  1 
ATOM   16678 N  N   . SER   J  10 45  ? 42.487  -125.090 -0.209  1.00 85.90  ? 45  SER   J N   1 
ATOM   16679 C  CA  . SER   J  10 45  ? 41.657  -126.321 -0.146  1.00 90.05  ? 45  SER   J CA  1 
ATOM   16680 C  C   . SER   J  10 45  ? 41.619  -126.813 1.303   1.00 88.44  ? 45  SER   J C   1 
ATOM   16681 O  O   . SER   J  10 45  ? 42.570  -126.506 2.056   1.00 86.86  ? 45  SER   J O   1 
ATOM   16682 C  CB  . SER   J  10 45  ? 42.172  -127.387 -1.078  1.00 91.30  ? 45  SER   J CB  1 
ATOM   16683 O  OG  . SER   J  10 45  ? 43.460  -127.833 -0.683  1.00 94.45  ? 45  SER   J OG  1 
ATOM   16684 N  N   . PHE   J  10 46  ? 40.568  -127.548 1.674   1.00 88.51  ? 46  PHE   J N   1 
ATOM   16685 C  CA  . PHE   J  10 46  ? 40.310  -127.979 3.072   1.00 86.02  ? 46  PHE   J CA  1 
ATOM   16686 C  C   . PHE   J  10 46  ? 39.596  -129.335 3.096   1.00 85.33  ? 46  PHE   J C   1 
ATOM   16687 O  O   . PHE   J  10 46  ? 38.770  -129.621 2.207   1.00 84.85  ? 46  PHE   J O   1 
ATOM   16688 C  CB  . PHE   J  10 46  ? 39.504  -126.909 3.814   1.00 85.09  ? 46  PHE   J CB  1 
ATOM   16689 C  CG  . PHE   J  10 46  ? 38.316  -126.373 3.058   1.00 84.86  ? 46  PHE   J CG  1 
ATOM   16690 C  CD1 . PHE   J  10 46  ? 37.093  -127.024 3.100   1.00 86.47  ? 46  PHE   J CD1 1 
ATOM   16691 C  CD2 . PHE   J  10 46  ? 38.420  -125.216 2.305   1.00 85.10  ? 46  PHE   J CD2 1 
ATOM   16692 C  CE1 . PHE   J  10 46  ? 36.000  -126.529 2.406   1.00 87.50  ? 46  PHE   J CE1 1 
ATOM   16693 C  CE2 . PHE   J  10 46  ? 37.327  -124.722 1.611   1.00 86.69  ? 46  PHE   J CE2 1 
ATOM   16694 C  CZ  . PHE   J  10 46  ? 36.119  -125.379 1.661   1.00 87.72  ? 46  PHE   J CZ  1 
ATOM   16695 N  N   . ALA   J  10 47  ? 39.919  -130.141 4.109   1.00 82.60  ? 47  ALA   J N   1 
ATOM   16696 C  CA  . ALA   J  10 47  ? 39.304  -131.458 4.389   1.00 83.30  ? 47  ALA   J CA  1 
ATOM   16697 C  C   . ALA   J  10 47  ? 39.318  -131.707 5.900   1.00 79.70  ? 47  ALA   J C   1 
ATOM   16698 O  O   . ALA   J  10 47  ? 40.306  -131.317 6.554   1.00 80.91  ? 47  ALA   J O   1 
ATOM   16699 C  CB  . ALA   J  10 47  ? 40.043  -132.539 3.642   1.00 84.54  ? 47  ALA   J CB  1 
ATOM   16700 N  N   . GLY   J  10 48  ? 38.259  -132.329 6.424   1.00 77.93  ? 48  GLY   J N   1 
ATOM   16701 C  CA  . GLY   J  10 48  ? 38.113  -132.645 7.857   1.00 77.82  ? 48  GLY   J CA  1 
ATOM   16702 C  C   . GLY   J  10 48  ? 36.660  -132.689 8.293   1.00 79.58  ? 48  GLY   J C   1 
ATOM   16703 O  O   . GLY   J  10 48  ? 35.790  -132.932 7.439   1.00 80.80  ? 48  GLY   J O   1 
ATOM   16704 N  N   . GLU   J  10 49  ? 36.419  -132.434 9.582   1.00 81.05  ? 49  GLU   J N   1 
ATOM   16705 C  CA  . GLU   J  10 49  ? 35.108  -132.577 10.272  1.00 86.74  ? 49  GLU   J CA  1 
ATOM   16706 C  C   . GLU   J  10 49  ? 34.042  -131.765 9.527   1.00 86.66  ? 49  GLU   J C   1 
ATOM   16707 O  O   . GLU   J  10 49  ? 34.343  -130.628 9.113   1.00 85.72  ? 49  GLU   J O   1 
ATOM   16708 C  CB  . GLU   J  10 49  ? 35.261  -132.131 11.730  1.00 90.55  ? 49  GLU   J CB  1 
ATOM   16709 C  CG  . GLU   J  10 49  ? 33.970  -132.125 12.532  1.00 97.76  ? 49  GLU   J CG  1 
ATOM   16710 C  CD  . GLU   J  10 49  ? 33.326  -133.486 12.742  1.00 105.20 ? 49  GLU   J CD  1 
ATOM   16711 O  OE1 . GLU   J  10 49  ? 34.068  -134.491 12.831  1.00 112.07 ? 49  GLU   J OE1 1 
ATOM   16712 O  OE2 . GLU   J  10 49  ? 32.079  -133.540 12.821  1.00 111.04 ? 49  GLU   J OE2 1 
ATOM   16713 N  N   . ALA   J  10 50  ? 32.844  -132.338 9.366   1.00 87.09  ? 50  ALA   J N   1 
ATOM   16714 C  CA  . ALA   J  10 50  ? 31.673  -131.708 8.712   1.00 89.98  ? 50  ALA   J CA  1 
ATOM   16715 C  C   . ALA   J  10 50  ? 31.301  -130.427 9.465   1.00 91.04  ? 50  ALA   J C   1 
ATOM   16716 O  O   . ALA   J  10 50  ? 31.336  -130.447 10.710  1.00 92.65  ? 50  ALA   J O   1 
ATOM   16717 C  CB  . ALA   J  10 50  ? 30.514  -132.672 8.678   1.00 90.98  ? 50  ALA   J CB  1 
ATOM   16718 N  N   . GLY   J  10 51  ? 30.965  -129.360 8.732   1.00 92.43  ? 51  GLY   J N   1 
ATOM   16719 C  CA  . GLY   J  10 51  ? 30.647  -128.031 9.289   1.00 91.42  ? 51  GLY   J CA  1 
ATOM   16720 C  C   . GLY   J  10 51  ? 31.906  -127.224 9.553   1.00 90.77  ? 51  GLY   J C   1 
ATOM   16721 O  O   . GLY   J  10 51  ? 32.022  -126.121 8.985   1.00 89.07  ? 51  GLY   J O   1 
ATOM   16722 N  N   . ASP   J  10 52  ? 32.814  -127.765 10.376  1.00 92.04  ? 52  ASP   J N   1 
ATOM   16723 C  CA  . ASP   J  10 52  ? 34.104  -127.139 10.783  1.00 91.99  ? 52  ASP   J CA  1 
ATOM   16724 C  C   . ASP   J  10 52  ? 34.864  -126.631 9.550   1.00 91.21  ? 52  ASP   J C   1 
ATOM   16725 O  O   . ASP   J  10 52  ? 35.382  -125.500 9.609   1.00 89.61  ? 52  ASP   J O   1 
ATOM   16726 C  CB  . ASP   J  10 52  ? 34.983  -128.120 11.568  1.00 93.03  ? 52  ASP   J CB  1 
ATOM   16727 C  CG  . ASP   J  10 52  ? 34.594  -128.305 13.027  1.00 96.43  ? 52  ASP   J CG  1 
ATOM   16728 O  OD1 . ASP   J  10 52  ? 33.616  -127.664 13.465  1.00 95.81  ? 52  ASP   J OD1 1 
ATOM   16729 O  OD2 . ASP   J  10 52  ? 35.278  -129.092 13.719  1.00 97.13  ? 52  ASP   J OD2 1 
ATOM   16730 N  N   . THR   J  10 53  ? 34.940  -127.446 8.492   1.00 91.29  ? 53  THR   J N   1 
ATOM   16731 C  CA  . THR   J  10 53  ? 35.739  -127.190 7.261   1.00 89.32  ? 53  THR   J CA  1 
ATOM   16732 C  C   . THR   J  10 53  ? 35.333  -125.859 6.619   1.00 87.61  ? 53  THR   J C   1 
ATOM   16733 O  O   . THR   J  10 53  ? 36.190  -124.959 6.541   1.00 86.79  ? 53  THR   J O   1 
ATOM   16734 C  CB  . THR   J  10 53  ? 35.585  -128.335 6.253   1.00 91.21  ? 53  THR   J CB  1 
ATOM   16735 O  OG1 . THR   J  10 53  ? 34.194  -128.631 6.126   1.00 95.03  ? 53  THR   J OG1 1 
ATOM   16736 C  CG2 . THR   J  10 53  ? 36.340  -129.579 6.662   1.00 90.52  ? 53  THR   J CG2 1 
ATOM   16737 N  N   . VAL   J  10 54  ? 34.082  -125.751 6.166   1.00 87.27  ? 54  VAL   J N   1 
ATOM   16738 C  CA  . VAL   J  10 54  ? 33.565  -124.562 5.425   1.00 87.97  ? 54  VAL   J CA  1 
ATOM   16739 C  C   . VAL   J  10 54  ? 33.583  -123.352 6.370   1.00 86.47  ? 54  VAL   J C   1 
ATOM   16740 O  O   . VAL   J  10 54  ? 33.983  -122.267 5.915   1.00 90.91  ? 54  VAL   J O   1 
ATOM   16741 C  CB  . VAL   J  10 54  ? 32.163  -124.816 4.836   1.00 90.27  ? 54  VAL   J CB  1 
ATOM   16742 C  CG1 . VAL   J  10 54  ? 31.606  -123.582 4.139   1.00 89.59  ? 54  VAL   J CG1 1 
ATOM   16743 C  CG2 . VAL   J  10 54  ? 32.160  -126.001 3.881   1.00 91.64  ? 54  VAL   J CG2 1 
ATOM   16744 N  N   . GLN   J  10 55  ? 33.181  -123.535 7.633   1.00 83.41  ? 55  GLN   J N   1 
ATOM   16745 C  CA  . GLN   J  10 55  ? 33.125  -122.457 8.661   1.00 81.81  ? 55  GLN   J CA  1 
ATOM   16746 C  C   . GLN   J  10 55  ? 34.509  -121.817 8.825   1.00 81.94  ? 55  GLN   J C   1 
ATOM   16747 O  O   . GLN   J  10 55  ? 34.575  -120.576 8.871   1.00 82.86  ? 55  GLN   J O   1 
ATOM   16748 C  CB  . GLN   J  10 55  ? 32.627  -122.995 10.004  1.00 80.51  ? 55  GLN   J CB  1 
ATOM   16749 C  CG  . GLN   J  10 55  ? 31.111  -123.129 10.088  1.00 81.60  ? 55  GLN   J CG  1 
ATOM   16750 C  CD  . GLN   J  10 55  ? 30.339  -121.832 10.169  1.00 80.25  ? 55  GLN   J CD  1 
ATOM   16751 O  OE1 . GLN   J  10 55  ? 29.128  -121.811 9.966   1.00 82.41  ? 55  GLN   J OE1 1 
ATOM   16752 N  NE2 . GLN   J  10 55  ? 31.011  -120.734 10.473  1.00 79.90  ? 55  GLN   J NE2 1 
ATOM   16753 N  N   . PHE   J  10 56  ? 35.566  -122.629 8.916   1.00 80.45  ? 56  PHE   J N   1 
ATOM   16754 C  CA  . PHE   J  10 56  ? 36.971  -122.162 9.068   1.00 79.13  ? 56  PHE   J CA  1 
ATOM   16755 C  C   . PHE   J  10 56  ? 37.447  -121.498 7.769   1.00 80.23  ? 56  PHE   J C   1 
ATOM   16756 O  O   . PHE   J  10 56  ? 38.071  -120.424 7.848   1.00 82.23  ? 56  PHE   J O   1 
ATOM   16757 C  CB  . PHE   J  10 56  ? 37.903  -123.309 9.466   1.00 77.34  ? 56  PHE   J CB  1 
ATOM   16758 C  CG  . PHE   J  10 56  ? 39.352  -122.906 9.585   1.00 75.09  ? 56  PHE   J CG  1 
ATOM   16759 C  CD1 . PHE   J  10 56  ? 39.812  -122.221 10.698  1.00 73.91  ? 56  PHE   J CD1 1 
ATOM   16760 C  CD2 . PHE   J  10 56  ? 40.253  -123.187 8.569   1.00 76.40  ? 56  PHE   J CD2 1 
ATOM   16761 C  CE1 . PHE   J  10 56  ? 41.142  -121.841 10.800  1.00 72.79  ? 56  PHE   J CE1 1 
ATOM   16762 C  CE2 . PHE   J  10 56  ? 41.583  -122.806 8.672   1.00 74.75  ? 56  PHE   J CE2 1 
ATOM   16763 C  CZ  . PHE   J  10 56  ? 42.026  -122.135 9.788   1.00 72.79  ? 56  PHE   J CZ  1 
ATOM   16764 N  N   . ALA   J  10 57  ? 37.177  -122.121 6.618   1.00 80.58  ? 57  ALA   J N   1 
ATOM   16765 C  CA  . ALA   J  10 57  ? 37.571  -121.632 5.274   1.00 83.18  ? 57  ALA   J CA  1 
ATOM   16766 C  C   . ALA   J  10 57  ? 37.038  -120.211 5.055   1.00 84.71  ? 57  ALA   J C   1 
ATOM   16767 O  O   . ALA   J  10 57  ? 37.842  -119.326 4.694   1.00 86.81  ? 57  ALA   J O   1 
ATOM   16768 C  CB  . ALA   J  10 57  ? 37.059  -122.572 4.213   1.00 84.53  ? 57  ALA   J CB  1 
ATOM   16769 N  N   . GLU   J  10 58  ? 35.734  -120.008 5.269   1.00 84.76  ? 58  GLU   J N   1 
ATOM   16770 C  CA  . GLU   J  10 58  ? 35.029  -118.717 5.039   1.00 88.37  ? 58  GLU   J CA  1 
ATOM   16771 C  C   . GLU   J  10 58  ? 35.507  -117.666 6.048   1.00 87.28  ? 58  GLU   J C   1 
ATOM   16772 O  O   . GLU   J  10 58  ? 35.605  -116.487 5.663   1.00 89.58  ? 58  GLU   J O   1 
ATOM   16773 C  CB  . GLU   J  10 58  ? 33.515  -118.903 5.139   1.00 90.32  ? 58  GLU   J CB  1 
ATOM   16774 C  CG  . GLU   J  10 58  ? 32.928  -119.669 3.971   1.00 92.68  ? 58  GLU   J CG  1 
ATOM   16775 C  CD  . GLU   J  10 58  ? 31.417  -119.812 4.020   1.00 95.60  ? 58  GLU   J CD  1 
ATOM   16776 O  OE1 . GLU   J  10 58  ? 30.791  -119.165 4.888   1.00 91.57  ? 58  GLU   J OE1 1 
ATOM   16777 O  OE2 . GLU   J  10 58  ? 30.867  -120.569 3.192   1.00 100.46 ? 58  GLU   J OE2 1 
ATOM   16778 N  N   . TYR   J  10 59  ? 35.777  -118.075 7.291   1.00 86.97  ? 59  TYR   J N   1 
ATOM   16779 C  CA  . TYR   J  10 59  ? 36.291  -117.192 8.370   1.00 84.85  ? 59  TYR   J CA  1 
ATOM   16780 C  C   . TYR   J  10 59  ? 37.656  -116.629 7.957   1.00 85.23  ? 59  TYR   J C   1 
ATOM   16781 O  O   . TYR   J  10 59  ? 37.856  -115.412 8.108   1.00 86.31  ? 59  TYR   J O   1 
ATOM   16782 C  CB  . TYR   J  10 59  ? 36.373  -117.932 9.706   1.00 86.00  ? 59  TYR   J CB  1 
ATOM   16783 C  CG  . TYR   J  10 59  ? 37.218  -117.233 10.739  1.00 87.07  ? 59  TYR   J CG  1 
ATOM   16784 C  CD1 . TYR   J  10 59  ? 36.833  -116.014 11.271  1.00 87.61  ? 59  TYR   J CD1 1 
ATOM   16785 C  CD2 . TYR   J  10 59  ? 38.411  -117.783 11.177  1.00 89.45  ? 59  TYR   J CD2 1 
ATOM   16786 C  CE1 . TYR   J  10 59  ? 37.608  -115.362 12.216  1.00 90.77  ? 59  TYR   J CE1 1 
ATOM   16787 C  CE2 . TYR   J  10 59  ? 39.197  -117.147 12.123  1.00 89.78  ? 59  TYR   J CE2 1 
ATOM   16788 C  CZ  . TYR   J  10 59  ? 38.794  -115.932 12.646  1.00 90.21  ? 59  TYR   J CZ  1 
ATOM   16789 O  OH  . TYR   J  10 59  ? 39.567  -115.306 13.580  1.00 95.94  ? 59  TYR   J OH  1 
ATOM   16790 N  N   . ILE   J  10 60  ? 38.558  -117.480 7.453   1.00 81.09  ? 60  ILE   J N   1 
ATOM   16791 C  CA  . ILE   J  10 60  ? 39.901  -117.063 6.944   1.00 82.24  ? 60  ILE   J CA  1 
ATOM   16792 C  C   . ILE   J  10 60  ? 39.704  -116.137 5.739   1.00 83.35  ? 60  ILE   J C   1 
ATOM   16793 O  O   . ILE   J  10 60  ? 40.388  -115.096 5.677   1.00 81.98  ? 60  ILE   J O   1 
ATOM   16794 C  CB  . ILE   J  10 60  ? 40.782  -118.278 6.581   1.00 80.46  ? 60  ILE   J CB  1 
ATOM   16795 C  CG1 . ILE   J  10 60  ? 41.141  -119.120 7.807   1.00 81.27  ? 60  ILE   J CG1 1 
ATOM   16796 C  CG2 . ILE   J  10 60  ? 42.032  -117.844 5.826   1.00 81.50  ? 60  ILE   J CG2 1 
ATOM   16797 C  CD1 . ILE   J  10 60  ? 41.842  -118.356 8.910   1.00 80.36  ? 60  ILE   J CD1 1 
ATOM   16798 N  N   . GLN   J  10 61  ? 38.815  -116.518 4.817   1.00 85.22  ? 61  GLN   J N   1 
ATOM   16799 C  CA  . GLN   J  10 61  ? 38.522  -115.759 3.572   1.00 87.56  ? 61  GLN   J CA  1 
ATOM   16800 C  C   . GLN   J  10 61  ? 38.125  -114.324 3.935   1.00 88.56  ? 61  GLN   J C   1 
ATOM   16801 O  O   . GLN   J  10 61  ? 38.663  -113.394 3.307   1.00 92.34  ? 61  GLN   J O   1 
ATOM   16802 C  CB  . GLN   J  10 61  ? 37.416  -116.444 2.771   1.00 87.29  ? 61  GLN   J CB  1 
ATOM   16803 C  CG  . GLN   J  10 61  ? 37.126  -115.767 1.443   1.00 90.12  ? 61  GLN   J CG  1 
ATOM   16804 C  CD  . GLN   J  10 61  ? 36.063  -116.506 0.671   1.00 91.59  ? 61  GLN   J CD  1 
ATOM   16805 O  OE1 . GLN   J  10 61  ? 35.011  -116.849 1.208   1.00 91.03  ? 61  GLN   J OE1 1 
ATOM   16806 N  NE2 . GLN   J  10 61  ? 36.334  -116.760 -0.599  1.00 95.06  ? 61  GLN   J NE2 1 
ATOM   16807 N  N   . ALA   J  10 62  ? 37.224  -114.160 4.910   1.00 86.70  ? 62  ALA   J N   1 
ATOM   16808 C  CA  . ALA   J  10 62  ? 36.709  -112.852 5.378   1.00 88.01  ? 62  ALA   J CA  1 
ATOM   16809 C  C   . ALA   J  10 62  ? 37.870  -112.004 5.911   1.00 89.62  ? 62  ALA   J C   1 
ATOM   16810 O  O   . ALA   J  10 62  ? 37.930  -110.810 5.566   1.00 96.00  ? 62  ALA   J O   1 
ATOM   16811 C  CB  . ALA   J  10 62  ? 35.640  -113.048 6.427   1.00 85.94  ? 62  ALA   J CB  1 
ATOM   16812 N  N   . ASN   J  10 63  ? 38.762  -112.606 6.704   1.00 88.70  ? 63  ASN   J N   1 
ATOM   16813 C  CA  . ASN   J  10 63  ? 39.903  -111.910 7.361   1.00 89.59  ? 63  ASN   J CA  1 
ATOM   16814 C  C   . ASN   J  10 63  ? 40.902  -111.406 6.311   1.00 89.78  ? 63  ASN   J C   1 
ATOM   16815 O  O   . ASN   J  10 63  ? 41.375  -110.264 6.464   1.00 90.70  ? 63  ASN   J O   1 
ATOM   16816 C  CB  . ASN   J  10 63  ? 40.598  -112.797 8.398   1.00 89.90  ? 63  ASN   J CB  1 
ATOM   16817 C  CG  . ASN   J  10 63  ? 40.003  -112.661 9.784   1.00 91.06  ? 63  ASN   J CG  1 
ATOM   16818 O  OD1 . ASN   J  10 63  ? 39.454  -113.614 10.328  1.00 93.34  ? 63  ASN   J OD1 1 
ATOM   16819 N  ND2 . ASN   J  10 63  ? 40.101  -111.476 10.364  1.00 94.93  ? 63  ASN   J ND2 1 
ATOM   16820 N  N   . ILE   J  10 64  ? 41.226  -112.215 5.298   1.00 88.21  ? 64  ILE   J N   1 
ATOM   16821 C  CA  . ILE   J  10 64  ? 42.206  -111.843 4.232   1.00 89.57  ? 64  ILE   J CA  1 
ATOM   16822 C  C   . ILE   J  10 64  ? 41.589  -110.750 3.350   1.00 89.61  ? 64  ILE   J C   1 
ATOM   16823 O  O   . ILE   J  10 64  ? 42.324  -109.814 2.980   1.00 92.65  ? 64  ILE   J O   1 
ATOM   16824 C  CB  . ILE   J  10 64  ? 42.650  -113.073 3.412   1.00 88.93  ? 64  ILE   J CB  1 
ATOM   16825 C  CG1 . ILE   J  10 64  ? 43.301  -114.144 4.292   1.00 88.54  ? 64  ILE   J CG1 1 
ATOM   16826 C  CG2 . ILE   J  10 64  ? 43.567  -112.664 2.268   1.00 90.92  ? 64  ILE   J CG2 1 
ATOM   16827 C  CD1 . ILE   J  10 64  ? 44.484  -113.656 5.098   1.00 89.06  ? 64  ILE   J CD1 1 
ATOM   16828 N  N   . GLN   J  10 65  ? 40.297  -110.866 3.027   1.00 89.21  ? 65  GLN   J N   1 
ATOM   16829 C  CA  . GLN   J  10 65  ? 39.543  -109.861 2.228   1.00 90.75  ? 65  GLN   J CA  1 
ATOM   16830 C  C   . GLN   J  10 65  ? 39.460  -108.539 3.007   1.00 90.58  ? 65  GLN   J C   1 
ATOM   16831 O  O   . GLN   J  10 65  ? 39.568  -107.475 2.361   1.00 93.64  ? 65  GLN   J O   1 
ATOM   16832 C  CB  . GLN   J  10 65  ? 38.154  -110.391 1.866   1.00 89.86  ? 65  GLN   J CB  1 
ATOM   16833 C  CG  . GLN   J  10 65  ? 38.172  -111.439 0.762   1.00 89.29  ? 65  GLN   J CG  1 
ATOM   16834 C  CD  . GLN   J  10 65  ? 36.809  -112.038 0.519   1.00 90.52  ? 65  GLN   J CD  1 
ATOM   16835 O  OE1 . GLN   J  10 65  ? 35.807  -111.603 1.083   1.00 90.76  ? 65  GLN   J OE1 1 
ATOM   16836 N  NE2 . GLN   J  10 65  ? 36.759  -113.048 -0.335  1.00 90.95  ? 65  GLN   J NE2 1 
ATOM   16837 N  N   . LEU   J  10 66  ? 39.272  -108.597 4.333   1.00 87.22  ? 66  LEU   J N   1 
ATOM   16838 C  CA  . LEU   J  10 66  ? 39.238  -107.400 5.221   1.00 85.47  ? 66  LEU   J CA  1 
ATOM   16839 C  C   . LEU   J  10 66  ? 40.599  -106.704 5.183   1.00 86.45  ? 66  LEU   J C   1 
ATOM   16840 O  O   . LEU   J  10 66  ? 40.616  -105.466 5.098   1.00 90.00  ? 66  LEU   J O   1 
ATOM   16841 C  CB  . LEU   J  10 66  ? 38.893  -107.798 6.659   1.00 83.61  ? 66  LEU   J CB  1 
ATOM   16842 C  CG  . LEU   J  10 66  ? 38.905  -106.655 7.675   1.00 83.23  ? 66  LEU   J CG  1 
ATOM   16843 C  CD1 . LEU   J  10 66  ? 37.901  -105.575 7.305   1.00 84.18  ? 66  LEU   J CD1 1 
ATOM   16844 C  CD2 . LEU   J  10 66  ? 38.622  -107.176 9.073   1.00 83.53  ? 66  LEU   J CD2 1 
ATOM   16845 N  N   . TYR   J  10 67  ? 41.688  -107.475 5.265   1.00 85.07  ? 67  TYR   J N   1 
ATOM   16846 C  CA  . TYR   J  10 67  ? 43.084  -106.969 5.194   1.00 84.06  ? 67  TYR   J CA  1 
ATOM   16847 C  C   . TYR   J  10 67  ? 43.312  -106.283 3.840   1.00 86.03  ? 67  TYR   J C   1 
ATOM   16848 O  O   . TYR   J  10 67  ? 43.876  -105.171 3.822   1.00 85.79  ? 67  TYR   J O   1 
ATOM   16849 C  CB  . TYR   J  10 67  ? 44.100  -108.096 5.395   1.00 81.62  ? 67  TYR   J CB  1 
ATOM   16850 C  CG  . TYR   J  10 67  ? 45.510  -107.613 5.615   1.00 80.65  ? 67  TYR   J CG  1 
ATOM   16851 C  CD1 . TYR   J  10 67  ? 46.266  -107.107 4.570   1.00 83.03  ? 67  TYR   J CD1 1 
ATOM   16852 C  CD2 . TYR   J  10 67  ? 46.087  -107.649 6.873   1.00 78.46  ? 67  TYR   J CD2 1 
ATOM   16853 C  CE1 . TYR   J  10 67  ? 47.559  -106.650 4.767   1.00 85.69  ? 67  TYR   J CE1 1 
ATOM   16854 C  CE2 . TYR   J  10 67  ? 47.380  -107.200 7.088   1.00 81.02  ? 67  TYR   J CE2 1 
ATOM   16855 C  CZ  . TYR   J  10 67  ? 48.119  -106.699 6.032   1.00 84.40  ? 67  TYR   J CZ  1 
ATOM   16856 O  OH  . TYR   J  10 67  ? 49.393  -106.258 6.244   1.00 88.80  ? 67  TYR   J OH  1 
ATOM   16857 N  N   . SER   J  10 68  ? 42.911  -106.943 2.747   1.00 87.63  ? 68  SER   J N   1 
ATOM   16858 C  CA  . SER   J  10 68  ? 43.030  -106.439 1.353   1.00 92.31  ? 68  SER   J CA  1 
ATOM   16859 C  C   . SER   J  10 68  ? 42.410  -105.041 1.246   1.00 93.77  ? 68  SER   J C   1 
ATOM   16860 O  O   . SER   J  10 68  ? 43.101  -104.123 0.761   1.00 92.83  ? 68  SER   J O   1 
ATOM   16861 C  CB  . SER   J  10 68  ? 42.408  -107.397 0.371   1.00 94.34  ? 68  SER   J CB  1 
ATOM   16862 O  OG  . SER   J  10 68  ? 43.201  -108.570 0.244   1.00 95.81  ? 68  SER   J OG  1 
ATOM   16863 N  N   . ILE   J  10 69  ? 41.166  -104.889 1.709   1.00 96.79  ? 69  ILE   J N   1 
ATOM   16864 C  CA  . ILE   J  10 69  ? 40.379  -103.623 1.617   1.00 100.50 ? 69  ILE   J CA  1 
ATOM   16865 C  C   . ILE   J  10 69  ? 41.033  -102.551 2.499   1.00 99.75  ? 69  ILE   J C   1 
ATOM   16866 O  O   . ILE   J  10 69  ? 41.011  -101.377 2.089   1.00 106.42 ? 69  ILE   J O   1 
ATOM   16867 C  CB  . ILE   J  10 69  ? 38.892  -103.870 1.963   1.00 105.00 ? 69  ILE   J CB  1 
ATOM   16868 C  CG1 . ILE   J  10 69  ? 38.131  -104.469 0.774   1.00 111.78 ? 69  ILE   J CG1 1 
ATOM   16869 C  CG2 . ILE   J  10 69  ? 38.211  -102.609 2.471   1.00 107.16 ? 69  ILE   J CG2 1 
ATOM   16870 C  CD1 . ILE   J  10 69  ? 38.045  -103.565 -0.445  1.00 113.66 ? 69  ILE   J CD1 1 
ATOM   16871 N  N   . ARG   J  10 70  ? 41.607  -102.927 3.646   1.00 93.57  ? 70  ARG   J N   1 
ATOM   16872 C  CA  . ARG   J  10 70  ? 42.190  -101.959 4.615   1.00 94.90  ? 70  ARG   J CA  1 
ATOM   16873 C  C   . ARG   J  10 70  ? 43.472  -101.345 4.040   1.00 98.10  ? 70  ARG   J C   1 
ATOM   16874 O  O   . ARG   J  10 70  ? 43.580  -100.107 4.063   1.00 103.14 ? 70  ARG   J O   1 
ATOM   16875 C  CB  . ARG   J  10 70  ? 42.491  -102.617 5.964   1.00 91.36  ? 70  ARG   J CB  1 
ATOM   16876 C  CG  . ARG   J  10 70  ? 42.994  -101.640 7.017   1.00 94.15  ? 70  ARG   J CG  1 
ATOM   16877 C  CD  . ARG   J  10 70  ? 43.316  -102.303 8.340   1.00 94.29  ? 70  ARG   J CD  1 
ATOM   16878 N  NE  . ARG   J  10 70  ? 42.134  -102.887 8.963   1.00 92.52  ? 70  ARG   J NE  1 
ATOM   16879 C  CZ  . ARG   J  10 70  ? 41.947  -104.182 9.215   1.00 89.69  ? 70  ARG   J CZ  1 
ATOM   16880 N  NH1 . ARG   J  10 70  ? 42.876  -105.075 8.912   1.00 89.47  ? 70  ARG   J NH1 1 
ATOM   16881 N  NH2 . ARG   J  10 70  ? 40.823  -104.582 9.783   1.00 88.72  ? 70  ARG   J NH2 1 
ATOM   16882 N  N   . GLU   J  10 71  ? 44.402  -102.176 3.557   1.00 98.33  ? 71  GLU   J N   1 
ATOM   16883 C  CA  . GLU   J  10 71  ? 45.774  -101.757 3.152   1.00 100.86 ? 71  GLU   J CA  1 
ATOM   16884 C  C   . GLU   J  10 71  ? 45.863  -101.526 1.637   1.00 97.21  ? 71  GLU   J C   1 
ATOM   16885 O  O   . GLU   J  10 71  ? 46.946  -101.105 1.186   1.00 93.57  ? 71  GLU   J O   1 
ATOM   16886 C  CB  . GLU   J  10 71  ? 46.805  -102.816 3.555   1.00 99.77  ? 71  GLU   J CB  1 
ATOM   16887 C  CG  . GLU   J  10 71  ? 46.720  -103.246 5.008   1.00 102.11 ? 71  GLU   J CG  1 
ATOM   16888 C  CD  . GLU   J  10 71  ? 46.907  -102.138 6.030   1.00 105.39 ? 71  GLU   J CD  1 
ATOM   16889 O  OE1 . GLU   J  10 71  ? 46.448  -102.318 7.175   1.00 109.25 ? 71  GLU   J OE1 1 
ATOM   16890 O  OE2 . GLU   J  10 71  ? 47.512  -101.102 5.684   1.00 108.99 ? 71  GLU   J OE2 1 
ATOM   16891 N  N   . ASP   J  10 72  ? 44.785  -101.793 0.887   1.00 101.14 ? 72  ASP   J N   1 
ATOM   16892 C  CA  . ASP   J  10 72  ? 44.757  -101.741 -0.601  1.00 102.94 ? 72  ASP   J CA  1 
ATOM   16893 C  C   . ASP   J  10 72  ? 45.963  -102.523 -1.138  1.00 106.29 ? 72  ASP   J C   1 
ATOM   16894 O  O   . ASP   J  10 72  ? 46.719  -101.960 -1.960  1.00 104.04 ? 72  ASP   J O   1 
ATOM   16895 C  CB  . ASP   J  10 72  ? 44.748  -100.297 -1.111  1.00 105.17 ? 72  ASP   J CB  1 
ATOM   16896 C  CG  . ASP   J  10 72  ? 44.464  -100.176 -2.599  1.00 106.86 ? 72  ASP   J CG  1 
ATOM   16897 O  OD1 . ASP   J  10 72  ? 43.604  -100.932 -3.094  1.00 103.53 ? 72  ASP   J OD1 1 
ATOM   16898 O  OD2 . ASP   J  10 72  ? 45.111  -99.333  -3.252  1.00 112.30 ? 72  ASP   J OD2 1 
ATOM   16899 N  N   . TYR   J  10 73  ? 46.136  -103.767 -0.677  1.00 105.96 ? 73  TYR   J N   1 
ATOM   16900 C  CA  . TYR   J  10 73  ? 47.354  -104.590 -0.903  1.00 106.47 ? 73  TYR   J CA  1 
ATOM   16901 C  C   . TYR   J  10 73  ? 47.065  -106.072 -0.643  1.00 105.98 ? 73  TYR   J C   1 
ATOM   16902 O  O   . TYR   J  10 73  ? 46.291  -106.382 0.284   1.00 107.15 ? 73  TYR   J O   1 
ATOM   16903 C  CB  . TYR   J  10 73  ? 48.480  -104.119 0.019   1.00 104.93 ? 73  TYR   J CB  1 
ATOM   16904 C  CG  . TYR   J  10 73  ? 49.868  -104.486 -0.439  1.00 107.06 ? 73  TYR   J CG  1 
ATOM   16905 C  CD1 . TYR   J  10 73  ? 50.413  -103.916 -1.579  1.00 109.85 ? 73  TYR   J CD1 1 
ATOM   16906 C  CD2 . TYR   J  10 73  ? 50.646  -105.382 0.275   1.00 104.02 ? 73  TYR   J CD2 1 
ATOM   16907 C  CE1 . TYR   J  10 73  ? 51.692  -104.236 -2.005  1.00 113.54 ? 73  TYR   J CE1 1 
ATOM   16908 C  CE2 . TYR   J  10 73  ? 51.926  -105.712 -0.136  1.00 107.35 ? 73  TYR   J CE2 1 
ATOM   16909 C  CZ  . TYR   J  10 73  ? 52.451  -105.138 -1.281  1.00 110.53 ? 73  TYR   J CZ  1 
ATOM   16910 O  OH  . TYR   J  10 73  ? 53.711  -105.460 -1.691  1.00 117.56 ? 73  TYR   J OH  1 
ATOM   16911 N  N   . GLU   J  10 74  ? 47.701  -106.950 -1.427  1.00 107.19 ? 74  GLU   J N   1 
ATOM   16912 C  CA  . GLU   J  10 74  ? 47.570  -108.430 -1.331  1.00 104.04 ? 74  GLU   J CA  1 
ATOM   16913 C  C   . GLU   J  10 74  ? 48.720  -108.990 -0.485  1.00 98.34  ? 74  GLU   J C   1 
ATOM   16914 O  O   . GLU   J  10 74  ? 49.887  -108.812 -0.882  1.00 97.98  ? 74  GLU   J O   1 
ATOM   16915 C  CB  . GLU   J  10 74  ? 47.573  -109.051 -2.729  1.00 107.18 ? 74  GLU   J CB  1 
ATOM   16916 C  CG  . GLU   J  10 74  ? 47.408  -110.561 -2.726  1.00 108.43 ? 74  GLU   J CG  1 
ATOM   16917 C  CD  . GLU   J  10 74  ? 47.235  -111.189 -4.100  1.00 112.96 ? 74  GLU   J CD  1 
ATOM   16918 O  OE1 . GLU   J  10 74  ? 46.674  -112.302 -4.173  1.00 109.69 ? 74  GLU   J OE1 1 
ATOM   16919 O  OE2 . GLU   J  10 74  ? 47.668  -110.568 -5.092  1.00 118.29 ? 74  GLU   J OE2 1 
ATOM   16920 N  N   . LEU   J  10 75  ? 48.391  -109.641 0.635   1.00 95.49  ? 75  LEU   J N   1 
ATOM   16921 C  CA  . LEU   J  10 75  ? 49.348  -110.380 1.506   1.00 93.69  ? 75  LEU   J CA  1 
ATOM   16922 C  C   . LEU   J  10 75  ? 50.055  -111.455 0.678   1.00 92.71  ? 75  LEU   J C   1 
ATOM   16923 O  O   . LEU   J  10 75  ? 49.383  -112.080 -0.164  1.00 91.54  ? 75  LEU   J O   1 
ATOM   16924 C  CB  . LEU   J  10 75  ? 48.584  -111.026 2.669   1.00 93.44  ? 75  LEU   J CB  1 
ATOM   16925 C  CG  . LEU   J  10 75  ? 48.939  -110.582 4.090   1.00 94.41  ? 75  LEU   J CG  1 
ATOM   16926 C  CD1 . LEU   J  10 75  ? 49.521  -109.175 4.146   1.00 94.95  ? 75  LEU   J CD1 1 
ATOM   16927 C  CD2 . LEU   J  10 75  ? 47.715  -110.686 4.989   1.00 95.47  ? 75  LEU   J CD2 1 
ATOM   16928 N  N   . SER   J  10 76  ? 51.347  -111.677 0.934   1.00 93.90  ? 76  SER   J N   1 
ATOM   16929 C  CA  . SER   J  10 76  ? 52.158  -112.750 0.298   1.00 97.50  ? 76  SER   J CA  1 
ATOM   16930 C  C   . SER   J  10 76  ? 51.592  -114.109 0.704   1.00 97.30  ? 76  SER   J C   1 
ATOM   16931 O  O   . SER   J  10 76  ? 51.013  -114.241 1.781   1.00 100.18 ? 76  SER   J O   1 
ATOM   16932 C  CB  . SER   J  10 76  ? 53.617  -112.632 0.664   1.00 97.96  ? 76  SER   J CB  1 
ATOM   16933 O  OG  . SER   J  10 76  ? 53.848  -113.082 1.992   1.00 95.90  ? 76  SER   J OG  1 
ATOM   16934 N  N   . PRO   J  10 77  ? 51.714  -115.156 -0.146  1.00 99.47  ? 77  PRO   J N   1 
ATOM   16935 C  CA  . PRO   J  10 77  ? 51.316  -116.509 0.247   1.00 97.48  ? 77  PRO   J CA  1 
ATOM   16936 C  C   . PRO   J  10 77  ? 51.921  -116.935 1.595   1.00 91.51  ? 77  PRO   J C   1 
ATOM   16937 O  O   . PRO   J  10 77  ? 51.211  -117.531 2.384   1.00 90.03  ? 77  PRO   J O   1 
ATOM   16938 C  CB  . PRO   J  10 77  ? 51.839  -117.379 -0.906  1.00 100.56 ? 77  PRO   J CB  1 
ATOM   16939 C  CG  . PRO   J  10 77  ? 51.828  -116.448 -2.101  1.00 101.40 ? 77  PRO   J CG  1 
ATOM   16940 C  CD  . PRO   J  10 77  ? 52.192  -115.090 -1.537  1.00 102.28 ? 77  PRO   J CD  1 
ATOM   16941 N  N   . GLN   J  10 78  ? 53.196  -116.602 1.831   1.00 90.71  ? 78  GLN   J N   1 
ATOM   16942 C  CA  . GLN   J  10 78  ? 53.927  -116.914 3.090   1.00 89.28  ? 78  GLN   J CA  1 
ATOM   16943 C  C   . GLN   J  10 78  ? 53.179  -116.283 4.270   1.00 87.69  ? 78  GLN   J C   1 
ATOM   16944 O  O   . GLN   J  10 78  ? 52.926  -116.992 5.258   1.00 82.83  ? 78  GLN   J O   1 
ATOM   16945 C  CB  . GLN   J  10 78  ? 55.373  -116.414 3.019   1.00 93.08  ? 78  GLN   J CB  1 
ATOM   16946 C  CG  . GLN   J  10 78  ? 56.299  -117.059 4.046   1.00 93.97  ? 78  GLN   J CG  1 
ATOM   16947 C  CD  . GLN   J  10 78  ? 56.011  -116.649 5.471   1.00 92.97  ? 78  GLN   J CD  1 
ATOM   16948 O  OE1 . GLN   J  10 78  ? 55.798  -117.482 6.348   1.00 93.59  ? 78  GLN   J OE1 1 
ATOM   16949 N  NE2 . GLN   J  10 78  ? 56.002  -115.351 5.720   1.00 94.50  ? 78  GLN   J NE2 1 
ATOM   16950 N  N   . ALA   J  10 79  ? 52.838  -114.997 4.162   1.00 87.75  ? 79  ALA   J N   1 
ATOM   16951 C  CA  . ALA   J  10 79  ? 52.151  -114.211 5.213   1.00 88.12  ? 79  ALA   J CA  1 
ATOM   16952 C  C   . ALA   J  10 79  ? 50.783  -114.834 5.522   1.00 86.03  ? 79  ALA   J C   1 
ATOM   16953 O  O   . ALA   J  10 79  ? 50.476  -114.997 6.718   1.00 84.45  ? 79  ALA   J O   1 
ATOM   16954 C  CB  . ALA   J  10 79  ? 52.021  -112.771 4.784   1.00 88.87  ? 79  ALA   J CB  1 
ATOM   16955 N  N   . VAL   J  10 80  ? 49.999  -115.163 4.486   1.00 89.27  ? 80  VAL   J N   1 
ATOM   16956 C  CA  . VAL   J  10 80  ? 48.635  -115.766 4.617   1.00 87.99  ? 80  VAL   J CA  1 
ATOM   16957 C  C   . VAL   J  10 80  ? 48.758  -117.119 5.326   1.00 87.44  ? 80  VAL   J C   1 
ATOM   16958 O  O   . VAL   J  10 80  ? 47.950  -117.386 6.237   1.00 86.12  ? 80  VAL   J O   1 
ATOM   16959 C  CB  . VAL   J  10 80  ? 47.926  -115.918 3.255   1.00 89.11  ? 80  VAL   J CB  1 
ATOM   16960 C  CG1 . VAL   J  10 80  ? 46.701  -116.817 3.354   1.00 85.90  ? 80  VAL   J CG1 1 
ATOM   16961 C  CG2 . VAL   J  10 80  ? 47.543  -114.572 2.661   1.00 90.42  ? 80  VAL   J CG2 1 
ATOM   16962 N  N   . SER   J  10 81  ? 49.721  -117.944 4.906   1.00 89.30  ? 81  SER   J N   1 
ATOM   16963 C  CA  . SER   J  10 81  ? 49.973  -119.295 5.474   1.00 89.38  ? 81  SER   J CA  1 
ATOM   16964 C  C   . SER   J  10 81  ? 50.281  -119.170 6.971   1.00 85.52  ? 81  SER   J C   1 
ATOM   16965 O  O   . SER   J  10 81  ? 49.747  -119.978 7.746   1.00 88.27  ? 81  SER   J O   1 
ATOM   16966 C  CB  . SER   J  10 81  ? 51.075  -120.017 4.736   1.00 92.17  ? 81  SER   J CB  1 
ATOM   16967 O  OG  . SER   J  10 81  ? 52.352  -119.545 5.137   1.00 97.50  ? 81  SER   J OG  1 
ATOM   16968 N  N   . SER   J  10 82  ? 51.087  -118.175 7.359   1.00 82.33  ? 82  SER   J N   1 
ATOM   16969 C  CA  . SER   J  10 82  ? 51.516  -117.930 8.762   1.00 81.39  ? 82  SER   J CA  1 
ATOM   16970 C  C   . SER   J  10 82  ? 50.316  -117.495 9.610   1.00 78.05  ? 82  SER   J C   1 
ATOM   16971 O  O   . SER   J  10 82  ? 50.238  -117.916 10.776  1.00 74.55  ? 82  SER   J O   1 
ATOM   16972 C  CB  . SER   J  10 82  ? 52.627  -116.915 8.834   1.00 80.73  ? 82  SER   J CB  1 
ATOM   16973 O  OG  . SER   J  10 82  ? 53.810  -117.408 8.226   1.00 81.94  ? 82  SER   J OG  1 
ATOM   16974 N  N   . PHE   J  10 83  ? 49.426  -116.675 9.046   1.00 79.24  ? 83  PHE   J N   1 
ATOM   16975 C  CA  . PHE   J  10 83  ? 48.154  -116.255 9.691   1.00 80.41  ? 83  PHE   J CA  1 
ATOM   16976 C  C   . PHE   J  10 83  ? 47.312  -117.504 9.961   1.00 81.70  ? 83  PHE   J C   1 
ATOM   16977 O  O   . PHE   J  10 83  ? 46.904  -117.712 11.120  1.00 78.57  ? 83  PHE   J O   1 
ATOM   16978 C  CB  . PHE   J  10 83  ? 47.384  -115.249 8.829   1.00 80.33  ? 83  PHE   J CB  1 
ATOM   16979 C  CG  . PHE   J  10 83  ? 45.999  -114.932 9.337   1.00 78.46  ? 83  PHE   J CG  1 
ATOM   16980 C  CD1 . PHE   J  10 83  ? 45.820  -114.182 10.489  1.00 79.75  ? 83  PHE   J CD1 1 
ATOM   16981 C  CD2 . PHE   J  10 83  ? 44.872  -115.388 8.670   1.00 79.53  ? 83  PHE   J CD2 1 
ATOM   16982 C  CE1 . PHE   J  10 83  ? 44.548  -113.891 10.959  1.00 78.94  ? 83  PHE   J CE1 1 
ATOM   16983 C  CE2 . PHE   J  10 83  ? 43.601  -115.095 9.141   1.00 79.68  ? 83  PHE   J CE2 1 
ATOM   16984 C  CZ  . PHE   J  10 83  ? 43.440  -114.349 10.285  1.00 78.99  ? 83  PHE   J CZ  1 
ATOM   16985 N  N   . VAL   J  10 84  ? 47.086  -118.311 8.919   1.00 83.85  ? 84  VAL   J N   1 
ATOM   16986 C  CA  . VAL   J  10 84  ? 46.204  -119.516 8.960   1.00 85.10  ? 84  VAL   J CA  1 
ATOM   16987 C  C   . VAL   J  10 84  ? 46.772  -120.513 9.976   1.00 85.59  ? 84  VAL   J C   1 
ATOM   16988 O  O   . VAL   J  10 84  ? 45.966  -121.077 10.743  1.00 87.36  ? 84  VAL   J O   1 
ATOM   16989 C  CB  . VAL   J  10 84  ? 46.029  -120.155 7.568   1.00 87.21  ? 84  VAL   J CB  1 
ATOM   16990 C  CG1 . VAL   J  10 84  ? 45.388  -121.534 7.652   1.00 85.37  ? 84  VAL   J CG1 1 
ATOM   16991 C  CG2 . VAL   J  10 84  ? 45.225  -119.251 6.643   1.00 88.94  ? 84  VAL   J CG2 1 
ATOM   16992 N  N   . ARG   J  10 85  ? 48.095  -120.719 9.984   1.00 86.71  ? 85  ARG   J N   1 
ATOM   16993 C  CA  . ARG   J  10 85  ? 48.772  -121.635 10.942  1.00 85.70  ? 85  ARG   J CA  1 
ATOM   16994 C  C   . ARG   J  10 85  ? 48.452  -121.191 12.372  1.00 83.40  ? 85  ARG   J C   1 
ATOM   16995 O  O   . ARG   J  10 85  ? 48.051  -122.052 13.172  1.00 81.53  ? 85  ARG   J O   1 
ATOM   16996 C  CB  . ARG   J  10 85  ? 50.292  -121.671 10.750  1.00 87.74  ? 85  ARG   J CB  1 
ATOM   16997 C  CG  . ARG   J  10 85  ? 50.959  -122.844 11.458  1.00 88.32  ? 85  ARG   J CG  1 
ATOM   16998 C  CD  . ARG   J  10 85  ? 52.406  -122.586 11.836  1.00 89.03  ? 85  ARG   J CD  1 
ATOM   16999 N  NE  . ARG   J  10 85  ? 52.529  -121.817 13.069  1.00 89.87  ? 85  ARG   J NE  1 
ATOM   17000 C  CZ  . ARG   J  10 85  ? 52.475  -122.321 14.301  1.00 88.52  ? 85  ARG   J CZ  1 
ATOM   17001 N  NH1 . ARG   J  10 85  ? 52.293  -123.616 14.493  1.00 88.96  ? 85  ARG   J NH1 1 
ATOM   17002 N  NH2 . ARG   J  10 85  ? 52.603  -121.523 15.347  1.00 88.21  ? 85  ARG   J NH2 1 
ATOM   17003 N  N   . GLN   J  10 86  ? 48.622  -119.898 12.666  1.00 85.05  ? 86  GLN   J N   1 
ATOM   17004 C  CA  . GLN   J  10 86  ? 48.463  -119.328 14.030  1.00 84.96  ? 86  GLN   J CA  1 
ATOM   17005 C  C   . GLN   J  10 86  ? 47.013  -119.490 14.494  1.00 80.59  ? 86  GLN   J C   1 
ATOM   17006 O  O   . GLN   J  10 86  ? 46.814  -119.735 15.693  1.00 76.69  ? 86  GLN   J O   1 
ATOM   17007 C  CB  . GLN   J  10 86  ? 48.859  -117.853 14.081  1.00 89.32  ? 86  GLN   J CB  1 
ATOM   17008 C  CG  . GLN   J  10 86  ? 49.011  -117.346 15.508  1.00 92.51  ? 86  GLN   J CG  1 
ATOM   17009 C  CD  . GLN   J  10 86  ? 49.294  -115.868 15.583  1.00 95.23  ? 86  GLN   J CD  1 
ATOM   17010 O  OE1 . GLN   J  10 86  ? 48.620  -115.058 14.951  1.00 95.48  ? 86  GLN   J OE1 1 
ATOM   17011 N  NE2 . GLN   J  10 86  ? 50.290  -115.504 16.376  1.00 98.08  ? 86  GLN   J NE2 1 
ATOM   17012 N  N   . GLU   J  10 87  ? 46.044  -119.336 13.585  1.00 83.35  ? 87  GLU   J N   1 
ATOM   17013 C  CA  . GLU   J  10 87  ? 44.594  -119.478 13.889  1.00 85.24  ? 87  GLU   J CA  1 
ATOM   17014 C  C   . GLU   J  10 87  ? 44.304  -120.919 14.316  1.00 82.85  ? 87  GLU   J C   1 
ATOM   17015 O  O   . GLU   J  10 87  ? 43.558  -121.096 15.299  1.00 78.77  ? 87  GLU   J O   1 
ATOM   17016 C  CB  . GLU   J  10 87  ? 43.735  -119.075 12.688  1.00 88.80  ? 87  GLU   J CB  1 
ATOM   17017 C  CG  . GLU   J  10 87  ? 43.628  -117.573 12.513  1.00 93.76  ? 87  GLU   J CG  1 
ATOM   17018 C  CD  . GLU   J  10 87  ? 42.998  -116.860 13.699  1.00 96.62  ? 87  GLU   J CD  1 
ATOM   17019 O  OE1 . GLU   J  10 87  ? 41.851  -117.201 14.052  1.00 99.10  ? 87  GLU   J OE1 1 
ATOM   17020 O  OE2 . GLU   J  10 87  ? 43.668  -115.985 14.284  1.00 104.25 ? 87  GLU   J OE2 1 
ATOM   17021 N  N   . LEU   J  10 88  ? 44.874  -121.898 13.605  1.00 83.42  ? 88  LEU   J N   1 
ATOM   17022 C  CA  . LEU   J  10 88  ? 44.735  -123.346 13.921  1.00 83.67  ? 88  LEU   J CA  1 
ATOM   17023 C  C   . LEU   J  10 88  ? 45.498  -123.662 15.214  1.00 83.62  ? 88  LEU   J C   1 
ATOM   17024 O  O   . LEU   J  10 88  ? 44.952  -124.408 16.045  1.00 84.50  ? 88  LEU   J O   1 
ATOM   17025 C  CB  . LEU   J  10 88  ? 45.236  -124.190 12.741  1.00 82.61  ? 88  LEU   J CB  1 
ATOM   17026 C  CG  . LEU   J  10 88  ? 44.306  -124.243 11.528  1.00 81.21  ? 88  LEU   J CG  1 
ATOM   17027 C  CD1 . LEU   J  10 88  ? 45.006  -124.860 10.326  1.00 79.25  ? 88  LEU   J CD1 1 
ATOM   17028 C  CD2 . LEU   J  10 88  ? 43.028  -125.006 11.847  1.00 81.36  ? 88  LEU   J CD2 1 
ATOM   17029 N  N   . ALA   J  10 89  ? 46.696  -123.094 15.391  1.00 84.55  ? 89  ALA   J N   1 
ATOM   17030 C  CA  . ALA   J  10 89  ? 47.555  -123.289 16.585  1.00 87.20  ? 89  ALA   J CA  1 
ATOM   17031 C  C   . ALA   J  10 89  ? 46.835  -122.772 17.841  1.00 88.98  ? 89  ALA   J C   1 
ATOM   17032 O  O   . ALA   J  10 89  ? 46.964  -123.418 18.896  1.00 87.26  ? 89  ALA   J O   1 
ATOM   17033 C  CB  . ALA   J  10 89  ? 48.892  -122.611 16.389  1.00 86.60  ? 89  ALA   J CB  1 
ATOM   17034 N  N   . LYS   J  10 90  ? 46.120  -121.645 17.733  1.00 92.56  ? 90  LYS   J N   1 
ATOM   17035 C  CA  . LYS   J  10 90  ? 45.176  -121.145 18.773  1.00 93.59  ? 90  LYS   J CA  1 
ATOM   17036 C  C   . LYS   J  10 90  ? 44.089  -122.199 19.002  1.00 93.44  ? 90  LYS   J C   1 
ATOM   17037 O  O   . LYS   J  10 90  ? 43.862  -122.576 20.164  1.00 90.69  ? 90  LYS   J O   1 
ATOM   17038 C  CB  . LYS   J  10 90  ? 44.476  -119.853 18.341  1.00 97.40  ? 90  LYS   J CB  1 
ATOM   17039 C  CG  . LYS   J  10 90  ? 45.254  -118.558 18.522  1.00 99.40  ? 90  LYS   J CG  1 
ATOM   17040 C  CD  . LYS   J  10 90  ? 44.399  -117.347 18.198  1.00 101.21 ? 90  LYS   J CD  1 
ATOM   17041 C  CE  . LYS   J  10 90  ? 45.191  -116.122 17.798  1.00 101.75 ? 90  LYS   J CE  1 
ATOM   17042 N  NZ  . LYS   J  10 90  ? 44.342  -115.161 17.057  1.00 103.87 ? 90  LYS   J NZ  1 
ATOM   17043 N  N   . SER   J  10 91  ? 43.450  -122.633 17.910  1.00 96.84  ? 91  SER   J N   1 
ATOM   17044 C  CA  . SER   J  10 91  ? 42.242  -123.502 17.885  1.00 96.16  ? 91  SER   J CA  1 
ATOM   17045 C  C   . SER   J  10 91  ? 42.482  -124.803 18.661  1.00 95.61  ? 91  SER   J C   1 
ATOM   17046 O  O   . SER   J  10 91  ? 41.554  -125.231 19.376  1.00 93.47  ? 91  SER   J O   1 
ATOM   17047 C  CB  . SER   J  10 91  ? 41.801  -123.777 16.463  1.00 97.86  ? 91  SER   J CB  1 
ATOM   17048 O  OG  . SER   J  10 91  ? 40.806  -124.791 16.420  1.00 100.29 ? 91  SER   J OG  1 
ATOM   17049 N  N   . ILE   J  10 92  ? 43.673  -125.399 18.547  1.00 92.65  ? 92  ILE   J N   1 
ATOM   17050 C  CA  . ILE   J  10 92  ? 43.939  -126.788 19.033  1.00 92.49  ? 92  ILE   J CA  1 
ATOM   17051 C  C   . ILE   J  10 92  ? 43.825  -126.853 20.563  1.00 90.47  ? 92  ILE   J C   1 
ATOM   17052 O  O   . ILE   J  10 92  ? 43.568  -127.958 21.068  1.00 88.55  ? 92  ILE   J O   1 
ATOM   17053 C  CB  . ILE   J  10 92  ? 45.285  -127.343 18.513  1.00 92.00  ? 92  ILE   J CB  1 
ATOM   17054 C  CG1 . ILE   J  10 92  ? 45.335  -128.872 18.601  1.00 93.75  ? 92  ILE   J CG1 1 
ATOM   17055 C  CG2 . ILE   J  10 92  ? 46.475  -126.713 19.219  1.00 89.89  ? 92  ILE   J CG2 1 
ATOM   17056 C  CD1 . ILE   J  10 92  ? 44.203  -129.584 17.882  1.00 96.08  ? 92  ILE   J CD1 1 
ATOM   17057 N  N   . ARG   J  10 93  ? 43.972  -125.728 21.271  1.00 90.29  ? 93  ARG   J N   1 
ATOM   17058 C  CA  . ARG   J  10 93  ? 43.873  -125.672 22.757  1.00 91.38  ? 93  ARG   J CA  1 
ATOM   17059 C  C   . ARG   J  10 93  ? 42.580  -124.966 23.185  1.00 92.98  ? 93  ARG   J C   1 
ATOM   17060 O  O   . ARG   J  10 93  ? 42.455  -124.666 24.386  1.00 93.56  ? 93  ARG   J O   1 
ATOM   17061 C  CB  . ARG   J  10 93  ? 45.122  -125.003 23.334  1.00 92.55  ? 93  ARG   J CB  1 
ATOM   17062 C  CG  . ARG   J  10 93  ? 46.369  -125.863 23.203  1.00 93.65  ? 93  ARG   J CG  1 
ATOM   17063 C  CD  . ARG   J  10 93  ? 47.649  -125.174 23.632  1.00 97.45  ? 93  ARG   J CD  1 
ATOM   17064 N  NE  . ARG   J  10 93  ? 48.818  -125.922 23.182  1.00 98.62  ? 93  ARG   J NE  1 
ATOM   17065 C  CZ  . ARG   J  10 93  ? 49.287  -127.038 23.745  1.00 96.35  ? 93  ARG   J CZ  1 
ATOM   17066 N  NH1 . ARG   J  10 93  ? 48.699  -127.563 24.808  1.00 98.67  ? 93  ARG   J NH1 1 
ATOM   17067 N  NH2 . ARG   J  10 93  ? 50.354  -127.628 23.236  1.00 94.64  ? 93  ARG   J NH2 1 
ATOM   17068 N  N   . SER   J  10 94  ? 41.643  -124.746 22.254  1.00 97.40  ? 94  SER   J N   1 
ATOM   17069 C  CA  . SER   J  10 94  ? 40.298  -124.170 22.522  1.00 102.53 ? 94  SER   J CA  1 
ATOM   17070 C  C   . SER   J  10 94  ? 39.414  -125.225 23.192  1.00 100.98 ? 94  SER   J C   1 
ATOM   17071 O  O   . SER   J  10 94  ? 39.837  -126.397 23.263  1.00 99.16  ? 94  SER   J O   1 
ATOM   17072 C  CB  . SER   J  10 94  ? 39.647  -123.659 21.263  1.00 107.42 ? 94  SER   J CB  1 
ATOM   17073 O  OG  . SER   J  10 94  ? 40.528  -122.810 20.545  1.00 115.30 ? 94  SER   J OG  1 
ATOM   17074 N  N   . ARG   J  10 95  ? 38.228  -124.819 23.652  1.00 103.00 ? 95  ARG   J N   1 
ATOM   17075 C  CA  . ARG   J  10 95  ? 37.221  -125.736 24.249  1.00 105.84 ? 95  ARG   J CA  1 
ATOM   17076 C  C   . ARG   J  10 95  ? 36.777  -126.739 23.180  1.00 103.34 ? 95  ARG   J C   1 
ATOM   17077 O  O   . ARG   J  10 95  ? 36.650  -127.929 23.520  1.00 100.97 ? 95  ARG   J O   1 
ATOM   17078 C  CB  . ARG   J  10 95  ? 36.027  -124.964 24.818  1.00 111.21 ? 95  ARG   J CB  1 
ATOM   17079 C  CG  . ARG   J  10 95  ? 35.096  -125.821 25.664  1.00 116.95 ? 95  ARG   J CG  1 
ATOM   17080 C  CD  . ARG   J  10 95  ? 33.829  -125.098 26.082  1.00 122.46 ? 95  ARG   J CD  1 
ATOM   17081 N  NE  . ARG   J  10 95  ? 33.169  -124.436 24.962  1.00 126.89 ? 95  ARG   J NE  1 
ATOM   17082 C  CZ  . ARG   J  10 95  ? 32.424  -125.040 24.037  1.00 127.21 ? 95  ARG   J CZ  1 
ATOM   17083 N  NH1 . ARG   J  10 95  ? 32.221  -126.347 24.076  1.00 131.39 ? 95  ARG   J NH1 1 
ATOM   17084 N  NH2 . ARG   J  10 95  ? 31.880  -124.326 23.066  1.00 129.67 ? 95  ARG   J NH2 1 
ATOM   17085 N  N   . ARG   J  10 96  ? 36.556  -126.273 21.945  1.00 105.91 ? 96  ARG   J N   1 
ATOM   17086 C  CA  . ARG   J  10 96  ? 36.263  -127.138 20.770  1.00 103.96 ? 96  ARG   J CA  1 
ATOM   17087 C  C   . ARG   J  10 96  ? 37.169  -126.735 19.607  1.00 101.13 ? 96  ARG   J C   1 
ATOM   17088 O  O   . ARG   J  10 96  ? 36.898  -125.758 18.913  1.00 101.55 ? 96  ARG   J O   1 
ATOM   17089 C  CB  . ARG   J  10 96  ? 34.781  -127.079 20.390  1.00 106.82 ? 96  ARG   J CB  1 
ATOM   17090 C  CG  . ARG   J  10 96  ? 34.339  -128.274 19.556  1.00 109.39 ? 96  ARG   J CG  1 
ATOM   17091 C  CD  . ARG   J  10 96  ? 32.862  -128.285 19.220  1.00 112.47 ? 96  ARG   J CD  1 
ATOM   17092 N  NE  . ARG   J  10 96  ? 32.461  -127.105 18.465  1.00 112.20 ? 96  ARG   J NE  1 
ATOM   17093 C  CZ  . ARG   J  10 96  ? 32.698  -126.904 17.170  1.00 111.03 ? 96  ARG   J CZ  1 
ATOM   17094 N  NH1 . ARG   J  10 96  ? 33.352  -127.803 16.451  1.00 110.34 ? 96  ARG   J NH1 1 
ATOM   17095 N  NH2 . ARG   J  10 96  ? 32.281  -125.790 16.594  1.00 110.87 ? 96  ARG   J NH2 1 
ATOM   17096 N  N   . PRO   J  10 97  ? 38.284  -127.466 19.376  1.00 98.12  ? 97  PRO   J N   1 
ATOM   17097 C  CA  . PRO   J  10 97  ? 39.186  -127.178 18.261  1.00 96.98  ? 97  PRO   J CA  1 
ATOM   17098 C  C   . PRO   J  10 97  ? 38.582  -127.454 16.878  1.00 98.39  ? 97  PRO   J C   1 
ATOM   17099 O  O   . PRO   J  10 97  ? 37.894  -128.447 16.726  1.00 102.12 ? 97  PRO   J O   1 
ATOM   17100 C  CB  . PRO   J  10 97  ? 40.368  -128.138 18.470  1.00 96.35  ? 97  PRO   J CB  1 
ATOM   17101 C  CG  . PRO   J  10 97  ? 40.257  -128.570 19.915  1.00 98.45  ? 97  PRO   J CG  1 
ATOM   17102 C  CD  . PRO   J  10 97  ? 38.772  -128.577 20.205  1.00 99.27  ? 97  PRO   J CD  1 
ATOM   17103 N  N   . TYR   J  10 98  ? 38.863  -126.570 15.916  1.00 99.80  ? 98  TYR   J N   1 
ATOM   17104 C  CA  . TYR   J  10 98  ? 38.653  -126.805 14.465  1.00 98.84  ? 98  TYR   J CA  1 
ATOM   17105 C  C   . TYR   J  10 98  ? 39.400  -128.085 14.085  1.00 96.94  ? 98  TYR   J C   1 
ATOM   17106 O  O   . TYR   J  10 98  ? 40.630  -128.137 14.302  1.00 90.90  ? 98  TYR   J O   1 
ATOM   17107 C  CB  . TYR   J  10 98  ? 39.167  -125.633 13.623  1.00 99.38  ? 98  TYR   J CB  1 
ATOM   17108 C  CG  . TYR   J  10 98  ? 38.314  -124.390 13.642  1.00 100.94 ? 98  TYR   J CG  1 
ATOM   17109 C  CD1 . TYR   J  10 98  ? 37.048  -124.378 13.077  1.00 104.02 ? 98  TYR   J CD1 1 
ATOM   17110 C  CD2 . TYR   J  10 98  ? 38.786  -123.209 14.194  1.00 102.61 ? 98  TYR   J CD2 1 
ATOM   17111 C  CE1 . TYR   J  10 98  ? 36.266  -123.233 13.080  1.00 105.90 ? 98  TYR   J CE1 1 
ATOM   17112 C  CE2 . TYR   J  10 98  ? 38.019  -122.055 14.203  1.00 104.58 ? 98  TYR   J CE2 1 
ATOM   17113 C  CZ  . TYR   J  10 98  ? 36.752  -122.066 13.644  1.00 104.54 ? 98  TYR   J CZ  1 
ATOM   17114 O  OH  . TYR   J  10 98  ? 35.994  -120.930 13.651  1.00 100.15 ? 98  TYR   J OH  1 
ATOM   17115 N  N   . GLN   J  10 99  ? 38.670  -129.082 13.579  1.00 95.32  ? 99  GLN   J N   1 
ATOM   17116 C  CA  . GLN   J  10 99  ? 39.232  -130.325 12.991  1.00 93.64  ? 99  GLN   J CA  1 
ATOM   17117 C  C   . GLN   J  10 99  ? 39.240  -130.156 11.468  1.00 87.27  ? 99  GLN   J C   1 
ATOM   17118 O  O   . GLN   J  10 99  ? 38.389  -130.768 10.796  1.00 86.13  ? 99  GLN   J O   1 
ATOM   17119 C  CB  . GLN   J  10 99  ? 38.430  -131.541 13.453  1.00 96.40  ? 99  GLN   J CB  1 
ATOM   17120 C  CG  . GLN   J  10 99  ? 38.620  -131.857 14.928  1.00 101.16 ? 99  GLN   J CG  1 
ATOM   17121 C  CD  . GLN   J  10 99  ? 37.844  -133.080 15.346  1.00 106.18 ? 99  GLN   J CD  1 
ATOM   17122 O  OE1 . GLN   J  10 99  ? 38.026  -134.168 14.801  1.00 112.04 ? 99  GLN   J OE1 1 
ATOM   17123 N  NE2 . GLN   J  10 99  ? 36.971  -132.913 16.327  1.00 110.43 ? 99  GLN   J NE2 1 
ATOM   17124 N  N   . VAL   J  10 100 ? 40.151  -129.318 10.967  1.00 86.33  ? 100 VAL   J N   1 
ATOM   17125 C  CA  . VAL   J  10 100 ? 40.281  -128.965 9.522   1.00 85.43  ? 100 VAL   J CA  1 
ATOM   17126 C  C   . VAL   J  10 100 ? 41.756  -129.057 9.121   1.00 82.65  ? 100 VAL   J C   1 
ATOM   17127 O  O   . VAL   J  10 100 ? 42.611  -128.516 9.850   1.00 81.60  ? 100 VAL   J O   1 
ATOM   17128 C  CB  . VAL   J  10 100 ? 39.717  -127.562 9.230   1.00 84.07  ? 100 VAL   J CB  1 
ATOM   17129 C  CG1 . VAL   J  10 100 ? 39.778  -127.231 7.747   1.00 86.61  ? 100 VAL   J CG1 1 
ATOM   17130 C  CG2 . VAL   J  10 100 ? 38.299  -127.399 9.754   1.00 84.94  ? 100 VAL   J CG2 1 
ATOM   17131 N  N   . ASN   J  10 101 ? 42.022  -129.714 7.994   1.00 83.35  ? 101 ASN   J N   1 
ATOM   17132 C  CA  . ASN   J  10 101 ? 43.356  -129.794 7.347   1.00 86.94  ? 101 ASN   J CA  1 
ATOM   17133 C  C   . ASN   J  10 101 ? 43.277  -129.007 6.037   1.00 85.65  ? 101 ASN   J C   1 
ATOM   17134 O  O   . ASN   J  10 101 ? 42.289  -129.195 5.304   1.00 86.98  ? 101 ASN   J O   1 
ATOM   17135 C  CB  . ASN   J  10 101 ? 43.771  -131.251 7.135   1.00 89.63  ? 101 ASN   J CB  1 
ATOM   17136 C  CG  . ASN   J  10 101 ? 43.868  -132.015 8.438   1.00 91.23  ? 101 ASN   J CG  1 
ATOM   17137 O  OD1 . ASN   J  10 101 ? 44.452  -131.526 9.403   1.00 87.79  ? 101 ASN   J OD1 1 
ATOM   17138 N  ND2 . ASN   J  10 101 ? 43.295  -133.208 8.481   1.00 97.15  ? 101 ASN   J ND2 1 
ATOM   17139 N  N   . VAL   J  10 102 ? 44.258  -128.142 5.769   1.00 84.25  ? 102 VAL   J N   1 
ATOM   17140 C  CA  . VAL   J  10 102 ? 44.239  -127.220 4.595   1.00 86.90  ? 102 VAL   J CA  1 
ATOM   17141 C  C   . VAL   J  10 102 ? 45.545  -127.348 3.807   1.00 88.39  ? 102 VAL   J C   1 
ATOM   17142 O  O   . VAL   J  10 102 ? 46.597  -127.617 4.422   1.00 89.49  ? 102 VAL   J O   1 
ATOM   17143 C  CB  . VAL   J  10 102 ? 44.008  -125.760 5.025   1.00 85.23  ? 102 VAL   J CB  1 
ATOM   17144 C  CG1 . VAL   J  10 102 ? 42.731  -125.608 5.836   1.00 85.82  ? 102 VAL   J CG1 1 
ATOM   17145 C  CG2 . VAL   J  10 102 ? 45.196  -125.192 5.790   1.00 86.76  ? 102 VAL   J CG2 1 
ATOM   17146 N  N   . LEU   J  10 103 ? 45.458  -127.151 2.490   1.00 90.18  ? 103 LEU   J N   1 
ATOM   17147 C  CA  . LEU   J  10 103 ? 46.604  -126.827 1.603   1.00 92.41  ? 103 LEU   J CA  1 
ATOM   17148 C  C   . LEU   J  10 103 ? 46.409  -125.395 1.110   1.00 92.97  ? 103 LEU   J C   1 
ATOM   17149 O  O   . LEU   J  10 103 ? 45.265  -125.066 0.741   1.00 98.30  ? 103 LEU   J O   1 
ATOM   17150 C  CB  . LEU   J  10 103 ? 46.647  -127.792 0.415   1.00 92.20  ? 103 LEU   J CB  1 
ATOM   17151 C  CG  . LEU   J  10 103 ? 46.843  -129.267 0.753   1.00 93.21  ? 103 LEU   J CG  1 
ATOM   17152 C  CD1 . LEU   J  10 103 ? 46.640  -130.127 -0.485  1.00 95.39  ? 103 LEU   J CD1 1 
ATOM   17153 C  CD2 . LEU   J  10 103 ? 48.216  -129.510 1.357   1.00 92.30  ? 103 LEU   J CD2 1 
ATOM   17154 N  N   . ILE   J  10 104 ? 47.470  -124.584 1.109   1.00 91.45  ? 104 ILE   J N   1 
ATOM   17155 C  CA  . ILE   J  10 104 ? 47.442  -123.192 0.571   1.00 90.49  ? 104 ILE   J CA  1 
ATOM   17156 C  C   . ILE   J  10 104 ? 48.380  -123.109 -0.633  1.00 88.27  ? 104 ILE   J C   1 
ATOM   17157 O  O   . ILE   J  10 104 ? 49.610  -123.180 -0.439  1.00 86.25  ? 104 ILE   J O   1 
ATOM   17158 C  CB  . ILE   J  10 104 ? 47.799  -122.154 1.650   1.00 88.42  ? 104 ILE   J CB  1 
ATOM   17159 C  CG1 . ILE   J  10 104 ? 46.702  -122.078 2.715   1.00 88.87  ? 104 ILE   J CG1 1 
ATOM   17160 C  CG2 . ILE   J  10 104 ? 48.062  -120.795 1.017   1.00 90.42  ? 104 ILE   J CG2 1 
ATOM   17161 C  CD1 . ILE   J  10 104 ? 47.088  -121.295 3.944   1.00 88.52  ? 104 ILE   J CD1 1 
ATOM   17162 N  N   . GLY   J  10 105 ? 47.793  -122.960 -1.822  1.00 90.20  ? 105 GLY   J N   1 
ATOM   17163 C  CA  . GLY   J  10 105 ? 48.505  -122.698 -3.084  1.00 90.50  ? 105 GLY   J CA  1 
ATOM   17164 C  C   . GLY   J  10 105 ? 48.454  -121.222 -3.409  1.00 89.49  ? 105 GLY   J C   1 
ATOM   17165 O  O   . GLY   J  10 105 ? 47.339  -120.664 -3.433  1.00 86.74  ? 105 GLY   J O   1 
ATOM   17166 N  N   . GLY   J  10 106 ? 49.618  -120.606 -3.611  1.00 90.93  ? 106 GLY   J N   1 
ATOM   17167 C  CA  . GLY   J  10 106 ? 49.742  -119.165 -3.893  1.00 92.58  ? 106 GLY   J CA  1 
ATOM   17168 C  C   . GLY   J  10 106 ? 50.839  -118.881 -4.899  1.00 94.81  ? 106 GLY   J C   1 
ATOM   17169 O  O   . GLY   J  10 106 ? 51.763  -119.714 -5.023  1.00 94.43  ? 106 GLY   J O   1 
ATOM   17170 N  N   . TYR   J  10 107 ? 50.727  -117.747 -5.597  1.00 96.42  ? 107 TYR   J N   1 
ATOM   17171 C  CA  . TYR   J  10 107 ? 51.784  -117.168 -6.465  1.00 95.74  ? 107 TYR   J CA  1 
ATOM   17172 C  C   . TYR   J  10 107 ? 52.219  -115.828 -5.865  1.00 94.47  ? 107 TYR   J C   1 
ATOM   17173 O  O   . TYR   J  10 107 ? 51.424  -114.873 -5.896  1.00 94.19  ? 107 TYR   J O   1 
ATOM   17174 C  CB  . TYR   J  10 107 ? 51.299  -117.017 -7.909  1.00 96.20  ? 107 TYR   J CB  1 
ATOM   17175 C  CG  . TYR   J  10 107 ? 52.408  -116.734 -8.890  1.00 97.27  ? 107 TYR   J CG  1 
ATOM   17176 C  CD1 . TYR   J  10 107 ? 52.825  -115.439 -9.144  1.00 97.07  ? 107 TYR   J CD1 1 
ATOM   17177 C  CD2 . TYR   J  10 107 ? 53.064  -117.763 -9.546  1.00 100.52 ? 107 TYR   J CD2 1 
ATOM   17178 C  CE1 . TYR   J  10 107 ? 53.851  -115.171 -10.035 1.00 100.70 ? 107 TYR   J CE1 1 
ATOM   17179 C  CE2 . TYR   J  10 107 ? 54.092  -117.514 -10.441 1.00 102.62 ? 107 TYR   J CE2 1 
ATOM   17180 C  CZ  . TYR   J  10 107 ? 54.489  -116.211 -10.685 1.00 102.19 ? 107 TYR   J CZ  1 
ATOM   17181 O  OH  . TYR   J  10 107 ? 55.499  -115.952 -11.564 1.00 107.45 ? 107 TYR   J OH  1 
ATOM   17182 N  N   . ASP   J  10 108 ? 53.432  -115.784 -5.306  1.00 96.60  ? 108 ASP   J N   1 
ATOM   17183 C  CA  . ASP   J  10 108 ? 54.078  -114.552 -4.781  1.00 99.56  ? 108 ASP   J CA  1 
ATOM   17184 C  C   . ASP   J  10 108 ? 54.475  -113.674 -5.973  1.00 103.18 ? 108 ASP   J C   1 
ATOM   17185 O  O   . ASP   J  10 108 ? 55.389  -114.072 -6.722  1.00 104.85 ? 108 ASP   J O   1 
ATOM   17186 C  CB  . ASP   J  10 108 ? 55.284  -114.891 -3.900  1.00 98.83  ? 108 ASP   J CB  1 
ATOM   17187 C  CG  . ASP   J  10 108 ? 55.825  -113.712 -3.109  1.00 100.50 ? 108 ASP   J CG  1 
ATOM   17188 O  OD1 . ASP   J  10 108 ? 55.669  -112.563 -3.575  1.00 101.44 ? 108 ASP   J OD1 1 
ATOM   17189 O  OD2 . ASP   J  10 108 ? 56.393  -113.953 -2.027  1.00 100.01 ? 108 ASP   J OD2 1 
ATOM   17190 N  N   . LYS   J  10 109 ? 53.803  -112.531 -6.141  1.00 103.68 ? 109 LYS   J N   1 
ATOM   17191 C  CA  . LYS   J  10 109 ? 53.998  -111.608 -7.292  1.00 106.15 ? 109 LYS   J CA  1 
ATOM   17192 C  C   . LYS   J  10 109 ? 55.305  -110.827 -7.111  1.00 109.76 ? 109 LYS   J C   1 
ATOM   17193 O  O   . LYS   J  10 109 ? 55.907  -110.452 -8.139  1.00 113.42 ? 109 LYS   J O   1 
ATOM   17194 C  CB  . LYS   J  10 109 ? 52.787  -110.681 -7.440  1.00 106.99 ? 109 LYS   J CB  1 
ATOM   17195 C  CG  . LYS   J  10 109 ? 51.493  -111.380 -7.835  1.00 106.36 ? 109 LYS   J CG  1 
ATOM   17196 C  CD  . LYS   J  10 109 ? 51.410  -111.717 -9.311  1.00 109.10 ? 109 LYS   J CD  1 
ATOM   17197 C  CE  . LYS   J  10 109 ? 50.998  -110.534 -10.162 1.00 109.77 ? 109 LYS   J CE  1 
ATOM   17198 N  NZ  . LYS   J  10 109 ? 51.015  -110.863 -11.606 1.00 112.00 ? 109 LYS   J NZ  1 
ATOM   17199 N  N   . LYS   J  10 110 ? 55.731  -110.600 -5.863  1.00 108.43 ? 110 LYS   J N   1 
ATOM   17200 C  CA  . LYS   J  10 110 ? 56.997  -109.887 -5.537  1.00 111.04 ? 110 LYS   J CA  1 
ATOM   17201 C  C   . LYS   J  10 110 ? 58.195  -110.780 -5.880  1.00 111.92 ? 110 LYS   J C   1 
ATOM   17202 O  O   . LYS   J  10 110 ? 59.229  -110.229 -6.297  1.00 114.27 ? 110 LYS   J O   1 
ATOM   17203 C  CB  . LYS   J  10 110 ? 57.041  -109.470 -4.063  1.00 111.44 ? 110 LYS   J CB  1 
ATOM   17204 C  CG  . LYS   J  10 110 ? 55.861  -108.633 -3.587  1.00 115.48 ? 110 LYS   J CG  1 
ATOM   17205 C  CD  . LYS   J  10 110 ? 56.240  -107.554 -2.590  1.00 120.39 ? 110 LYS   J CD  1 
ATOM   17206 C  CE  . LYS   J  10 110 ? 56.755  -106.291 -3.251  1.00 124.99 ? 110 LYS   J CE  1 
ATOM   17207 N  NZ  . LYS   J  10 110 ? 56.776  -105.143 -2.314  1.00 129.86 ? 110 LYS   J NZ  1 
ATOM   17208 N  N   . LYS   J  10 111 ? 58.058  -112.101 -5.714  1.00 110.90 ? 111 LYS   J N   1 
ATOM   17209 C  CA  . LYS   J  10 111 ? 59.136  -113.098 -5.966  1.00 112.73 ? 111 LYS   J CA  1 
ATOM   17210 C  C   . LYS   J  10 111 ? 58.975  -113.754 -7.344  1.00 112.53 ? 111 LYS   J C   1 
ATOM   17211 O  O   . LYS   J  10 111 ? 59.971  -114.330 -7.823  1.00 115.87 ? 111 LYS   J O   1 
ATOM   17212 C  CB  . LYS   J  10 111 ? 59.129  -114.182 -4.885  1.00 112.40 ? 111 LYS   J CB  1 
ATOM   17213 C  CG  . LYS   J  10 111 ? 59.651  -113.740 -3.527  1.00 113.26 ? 111 LYS   J CG  1 
ATOM   17214 C  CD  . LYS   J  10 111 ? 59.639  -114.851 -2.508  1.00 114.86 ? 111 LYS   J CD  1 
ATOM   17215 C  CE  . LYS   J  10 111 ? 60.421  -114.515 -1.257  1.00 119.02 ? 111 LYS   J CE  1 
ATOM   17216 N  NZ  . LYS   J  10 111 ? 60.537  -115.693 -0.364  1.00 121.58 ? 111 LYS   J NZ  1 
ATOM   17217 N  N   . ASN   J  10 112 ? 57.781  -113.681 -7.947  1.00 113.51 ? 112 ASN   J N   1 
ATOM   17218 C  CA  . ASN   J  10 112 ? 57.428  -114.369 -9.220  1.00 114.32 ? 112 ASN   J CA  1 
ATOM   17219 C  C   . ASN   J  10 112 ? 57.686  -115.872 -9.060  1.00 111.94 ? 112 ASN   J C   1 
ATOM   17220 O  O   . ASN   J  10 112 ? 58.382  -116.448 -9.919  1.00 112.05 ? 112 ASN   J O   1 
ATOM   17221 C  CB  . ASN   J  10 112 ? 58.193  -113.786 -10.413 1.00 116.99 ? 112 ASN   J CB  1 
ATOM   17222 C  CG  . ASN   J  10 112 ? 57.687  -112.416 -10.814 1.00 119.99 ? 112 ASN   J CG  1 
ATOM   17223 O  OD1 . ASN   J  10 112 ? 56.555  -112.283 -11.273 1.00 119.82 ? 112 ASN   J OD1 1 
ATOM   17224 N  ND2 . ASN   J  10 112 ? 58.513  -111.396 -10.645 1.00 121.88 ? 112 ASN   J ND2 1 
ATOM   17225 N  N   . LYS   J  10 113 ? 57.149  -116.472 -7.992  1.00 109.30 ? 113 LYS   J N   1 
ATOM   17226 C  CA  . LYS   J  10 113 ? 57.370  -117.897 -7.625  1.00 108.70 ? 113 LYS   J CA  1 
ATOM   17227 C  C   . LYS   J  10 113 ? 56.077  -118.522 -7.109  1.00 102.82 ? 113 LYS   J C   1 
ATOM   17228 O  O   . LYS   J  10 113 ? 55.363  -117.913 -6.316  1.00 97.77  ? 113 LYS   J O   1 
ATOM   17229 C  CB  . LYS   J  10 113 ? 58.458  -118.015 -6.552  1.00 111.75 ? 113 LYS   J CB  1 
ATOM   17230 C  CG  . LYS   J  10 113 ? 59.865  -118.263 -7.077  1.00 118.30 ? 113 LYS   J CG  1 
ATOM   17231 C  CD  . LYS   J  10 113 ? 60.896  -118.401 -5.976  1.00 121.57 ? 113 LYS   J CD  1 
ATOM   17232 C  CE  . LYS   J  10 113 ? 62.154  -119.115 -6.422  1.00 126.98 ? 113 LYS   J CE  1 
ATOM   17233 N  NZ  . LYS   J  10 113 ? 62.873  -118.358 -7.474  1.00 133.22 ? 113 LYS   J NZ  1 
ATOM   17234 N  N   . PRO   J  10 114 ? 55.749  -119.767 -7.525  1.00 103.23 ? 114 PRO   J N   1 
ATOM   17235 C  CA  . PRO   J  10 114 ? 54.655  -120.516 -6.911  1.00 102.30 ? 114 PRO   J CA  1 
ATOM   17236 C  C   . PRO   J  10 114 ? 55.080  -121.030 -5.527  1.00 98.99  ? 114 PRO   J C   1 
ATOM   17237 O  O   . PRO   J  10 114 ? 56.257  -121.285 -5.335  1.00 96.81  ? 114 PRO   J O   1 
ATOM   17238 C  CB  . PRO   J  10 114 ? 54.405  -121.660 -7.906  1.00 104.23 ? 114 PRO   J CB  1 
ATOM   17239 C  CG  . PRO   J  10 114 ? 55.754  -121.885 -8.560  1.00 106.05 ? 114 PRO   J CG  1 
ATOM   17240 C  CD  . PRO   J  10 114 ? 56.414  -120.522 -8.600  1.00 105.71 ? 114 PRO   J CD  1 
ATOM   17241 N  N   . GLU   J  10 115 ? 54.125  -121.155 -4.602  1.00 96.79  ? 115 GLU   J N   1 
ATOM   17242 C  CA  . GLU   J  10 115 ? 54.366  -121.642 -3.218  1.00 96.53  ? 115 GLU   J CA  1 
ATOM   17243 C  C   . GLU   J  10 115 ? 53.181  -122.502 -2.764  1.00 93.37  ? 115 GLU   J C   1 
ATOM   17244 O  O   . GLU   J  10 115 ? 52.025  -122.073 -2.955  1.00 89.33  ? 115 GLU   J O   1 
ATOM   17245 C  CB  . GLU   J  10 115 ? 54.592  -120.461 -2.273  1.00 97.14  ? 115 GLU   J CB  1 
ATOM   17246 C  CG  . GLU   J  10 115 ? 55.994  -119.878 -2.355  1.00 100.91 ? 115 GLU   J CG  1 
ATOM   17247 C  CD  . GLU   J  10 115 ? 56.245  -118.649 -1.493  1.00 99.10  ? 115 GLU   J CD  1 
ATOM   17248 O  OE1 . GLU   J  10 115 ? 57.425  -118.284 -1.325  1.00 99.58  ? 115 GLU   J OE1 1 
ATOM   17249 O  OE2 . GLU   J  10 115 ? 55.266  -118.052 -0.998  1.00 96.30  ? 115 GLU   J OE2 1 
ATOM   17250 N  N   . LEU   J  10 116 ? 53.475  -123.672 -2.188  1.00 92.87  ? 116 LEU   J N   1 
ATOM   17251 C  CA  . LEU   J  10 116 ? 52.476  -124.638 -1.657  1.00 92.32  ? 116 LEU   J CA  1 
ATOM   17252 C  C   . LEU   J  10 116 ? 52.788  -124.907 -0.182  1.00 89.27  ? 116 LEU   J C   1 
ATOM   17253 O  O   . LEU   J  10 116 ? 53.914  -125.346 0.108   1.00 88.79  ? 116 LEU   J O   1 
ATOM   17254 C  CB  . LEU   J  10 116 ? 52.540  -125.927 -2.480  1.00 92.88  ? 116 LEU   J CB  1 
ATOM   17255 C  CG  . LEU   J  10 116 ? 51.663  -127.075 -1.981  1.00 93.74  ? 116 LEU   J CG  1 
ATOM   17256 C  CD1 . LEU   J  10 116 ? 50.190  -126.770 -2.204  1.00 91.08  ? 116 LEU   J CD1 1 
ATOM   17257 C  CD2 . LEU   J  10 116 ? 52.050  -128.382 -2.659  1.00 96.06  ? 116 LEU   J CD2 1 
ATOM   17258 N  N   . TYR   J  10 117 ? 51.823  -124.648 0.705   1.00 88.88  ? 117 TYR   J N   1 
ATOM   17259 C  CA  . TYR   J  10 117 ? 51.940  -124.857 2.172   1.00 90.10  ? 117 TYR   J CA  1 
ATOM   17260 C  C   . TYR   J  10 117 ? 50.912  -125.892 2.635   1.00 87.69  ? 117 TYR   J C   1 
ATOM   17261 O  O   . TYR   J  10 117 ? 49.707  -125.704 2.373   1.00 84.61  ? 117 TYR   J O   1 
ATOM   17262 C  CB  . TYR   J  10 117 ? 51.728  -123.548 2.933   1.00 90.46  ? 117 TYR   J CB  1 
ATOM   17263 C  CG  . TYR   J  10 117 ? 52.742  -122.477 2.629   1.00 92.21  ? 117 TYR   J CG  1 
ATOM   17264 C  CD1 . TYR   J  10 117 ? 53.956  -122.433 3.295   1.00 91.15  ? 117 TYR   J CD1 1 
ATOM   17265 C  CD2 . TYR   J  10 117 ? 52.492  -121.512 1.668   1.00 92.91  ? 117 TYR   J CD2 1 
ATOM   17266 C  CE1 . TYR   J  10 117 ? 54.897  -121.456 3.018   1.00 90.84  ? 117 TYR   J CE1 1 
ATOM   17267 C  CE2 . TYR   J  10 117 ? 53.423  -120.529 1.376   1.00 93.66  ? 117 TYR   J CE2 1 
ATOM   17268 C  CZ  . TYR   J  10 117 ? 54.630  -120.502 2.054   1.00 92.24  ? 117 TYR   J CZ  1 
ATOM   17269 O  OH  . TYR   J  10 117 ? 55.562  -119.543 1.783   1.00 96.04  ? 117 TYR   J OH  1 
ATOM   17270 N  N   . GLN   J  10 118 ? 51.388  -126.940 3.312   1.00 90.42  ? 118 GLN   J N   1 
ATOM   17271 C  CA  . GLN   J  10 118 ? 50.551  -127.979 3.967   1.00 90.77  ? 118 GLN   J CA  1 
ATOM   17272 C  C   . GLN   J  10 118 ? 50.439  -127.622 5.451   1.00 86.90  ? 118 GLN   J C   1 
ATOM   17273 O  O   . GLN   J  10 118 ? 51.493  -127.494 6.106   1.00 82.53  ? 118 GLN   J O   1 
ATOM   17274 C  CB  . GLN   J  10 118 ? 51.163  -129.366 3.753   1.00 91.15  ? 118 GLN   J CB  1 
ATOM   17275 C  CG  . GLN   J  10 118 ? 50.275  -130.507 4.237   1.00 92.78  ? 118 GLN   J CG  1 
ATOM   17276 C  CD  . GLN   J  10 118 ? 50.834  -131.879 3.945   1.00 94.27  ? 118 GLN   J CD  1 
ATOM   17277 O  OE1 . GLN   J  10 118 ? 50.761  -132.780 4.773   1.00 99.80  ? 118 GLN   J OE1 1 
ATOM   17278 N  NE2 . GLN   J  10 118 ? 51.387  -132.062 2.756   1.00 99.75  ? 118 GLN   J NE2 1 
ATOM   17279 N  N   . ILE   J  10 119 ? 49.211  -127.429 5.944   1.00 86.04  ? 119 ILE   J N   1 
ATOM   17280 C  CA  . ILE   J  10 119 ? 48.916  -127.119 7.375   1.00 88.58  ? 119 ILE   J CA  1 
ATOM   17281 C  C   . ILE   J  10 119 ? 47.817  -128.066 7.868   1.00 89.82  ? 119 ILE   J C   1 
ATOM   17282 O  O   . ILE   J  10 119 ? 46.724  -128.060 7.266   1.00 91.85  ? 119 ILE   J O   1 
ATOM   17283 C  CB  . ILE   J  10 119 ? 48.502  -125.647 7.570   1.00 87.75  ? 119 ILE   J CB  1 
ATOM   17284 C  CG1 . ILE   J  10 119 ? 49.385  -124.681 6.777   1.00 90.49  ? 119 ILE   J CG1 1 
ATOM   17285 C  CG2 . ILE   J  10 119 ? 48.483  -125.303 9.051   1.00 88.59  ? 119 ILE   J CG2 1 
ATOM   17286 C  CD1 . ILE   J  10 119 ? 48.856  -123.264 6.719   1.00 89.87  ? 119 ILE   J CD1 1 
ATOM   17287 N  N   . ASP   J  10 120 ? 48.093  -128.823 8.935   1.00 91.33  ? 120 ASP   J N   1 
ATOM   17288 C  CA  . ASP   J  10 120 ? 47.120  -129.750 9.575   1.00 90.87  ? 120 ASP   J CA  1 
ATOM   17289 C  C   . ASP   J  10 120 ? 46.389  -128.998 10.696  1.00 87.63  ? 120 ASP   J C   1 
ATOM   17290 O  O   . ASP   J  10 120 ? 46.757  -127.841 10.967  1.00 88.04  ? 120 ASP   J O   1 
ATOM   17291 C  CB  . ASP   J  10 120 ? 47.809  -131.038 10.042  1.00 94.32  ? 120 ASP   J CB  1 
ATOM   17292 C  CG  . ASP   J  10 120 ? 48.629  -130.918 11.318  1.00 96.73  ? 120 ASP   J CG  1 
ATOM   17293 O  OD1 . ASP   J  10 120 ? 48.778  -129.790 11.824  1.00 97.19  ? 120 ASP   J OD1 1 
ATOM   17294 O  OD2 . ASP   J  10 120 ? 49.111  -131.963 11.800  1.00 102.55 ? 120 ASP   J OD2 1 
ATOM   17295 N  N   . TYR   J  10 121 ? 45.400  -129.642 11.321  1.00 84.27  ? 121 TYR   J N   1 
ATOM   17296 C  CA  . TYR   J  10 121 ? 44.484  -129.061 12.342  1.00 82.68  ? 121 TYR   J CA  1 
ATOM   17297 C  C   . TYR   J  10 121 ? 45.229  -128.694 13.636  1.00 79.14  ? 121 TYR   J C   1 
ATOM   17298 O  O   . TYR   J  10 121 ? 44.683  -127.885 14.421  1.00 76.63  ? 121 TYR   J O   1 
ATOM   17299 C  CB  . TYR   J  10 121 ? 43.327  -130.022 12.633  1.00 83.67  ? 121 TYR   J CB  1 
ATOM   17300 C  CG  . TYR   J  10 121 ? 43.679  -131.266 13.415  1.00 85.63  ? 121 TYR   J CG  1 
ATOM   17301 C  CD1 . TYR   J  10 121 ? 44.319  -132.339 12.814  1.00 87.34  ? 121 TYR   J CD1 1 
ATOM   17302 C  CD2 . TYR   J  10 121 ? 43.339  -131.387 14.753  1.00 87.01  ? 121 TYR   J CD2 1 
ATOM   17303 C  CE1 . TYR   J  10 121 ? 44.629  -133.487 13.524  1.00 89.38  ? 121 TYR   J CE1 1 
ATOM   17304 C  CE2 . TYR   J  10 121 ? 43.644  -132.527 15.478  1.00 88.12  ? 121 TYR   J CE2 1 
ATOM   17305 C  CZ  . TYR   J  10 121 ? 44.290  -133.583 14.861  1.00 91.01  ? 121 TYR   J CZ  1 
ATOM   17306 O  OH  . TYR   J  10 121 ? 44.587  -134.710 15.573  1.00 92.57  ? 121 TYR   J OH  1 
ATOM   17307 N  N   . LEU   J  10 122 ? 46.407  -129.284 13.878  1.00 80.06  ? 122 LEU   J N   1 
ATOM   17308 C  CA  . LEU   J  10 122 ? 47.280  -128.954 15.039  1.00 80.76  ? 122 LEU   J CA  1 
ATOM   17309 C  C   . LEU   J  10 122 ? 47.968  -127.605 14.808  1.00 80.70  ? 122 LEU   J C   1 
ATOM   17310 O  O   . LEU   J  10 122 ? 48.425  -127.001 15.800  1.00 82.38  ? 122 LEU   J O   1 
ATOM   17311 C  CB  . LEU   J  10 122 ? 48.339  -130.045 15.228  1.00 80.76  ? 122 LEU   J CB  1 
ATOM   17312 C  CG  . LEU   J  10 122 ? 47.823  -131.452 15.516  1.00 81.10  ? 122 LEU   J CG  1 
ATOM   17313 C  CD1 . LEU   J  10 122 ? 48.979  -132.437 15.533  1.00 83.18  ? 122 LEU   J CD1 1 
ATOM   17314 C  CD2 . LEU   J  10 122 ? 47.068  -131.503 16.832  1.00 80.81  ? 122 LEU   J CD2 1 
ATOM   17315 N  N   . GLY   J  10 123 ? 48.063  -127.171 13.548  1.00 80.99  ? 123 GLY   J N   1 
ATOM   17316 C  CA  . GLY   J  10 123 ? 48.852  -125.997 13.135  1.00 82.89  ? 123 GLY   J CA  1 
ATOM   17317 C  C   . GLY   J  10 123 ? 50.289  -126.393 12.850  1.00 84.10  ? 123 GLY   J C   1 
ATOM   17318 O  O   . GLY   J  10 123 ? 51.203  -125.711 13.347  1.00 90.06  ? 123 GLY   J O   1 
ATOM   17319 N  N   . THR   J  10 124 ? 50.477  -127.477 12.095  1.00 84.28  ? 124 THR   J N   1 
ATOM   17320 C  CA  . THR   J  10 124 ? 51.796  -127.971 11.625  1.00 86.34  ? 124 THR   J CA  1 
ATOM   17321 C  C   . THR   J  10 124 ? 51.987  -127.497 10.183  1.00 86.64  ? 124 THR   J C   1 
ATOM   17322 O  O   . THR   J  10 124 ? 51.364  -128.088 9.286   1.00 90.31  ? 124 THR   J O   1 
ATOM   17323 C  CB  . THR   J  10 124 ? 51.894  -129.498 11.749  1.00 87.29  ? 124 THR   J CB  1 
ATOM   17324 O  OG1 . THR   J  10 124 ? 51.338  -129.896 13.004  1.00 84.67  ? 124 THR   J OG1 1 
ATOM   17325 C  CG2 . THR   J  10 124 ? 53.316  -130.001 11.644  1.00 89.43  ? 124 THR   J CG2 1 
ATOM   17326 N  N   . LYS   J  10 125 ? 52.790  -126.454 9.974   1.00 86.14  ? 125 LYS   J N   1 
ATOM   17327 C  CA  . LYS   J  10 125 ? 53.023  -125.874 8.627   1.00 90.21  ? 125 LYS   J CA  1 
ATOM   17328 C  C   . LYS   J  10 125 ? 54.329  -126.429 8.053   1.00 90.08  ? 125 LYS   J C   1 
ATOM   17329 O  O   . LYS   J  10 125 ? 55.312  -126.555 8.815   1.00 87.02  ? 125 LYS   J O   1 
ATOM   17330 C  CB  . LYS   J  10 125 ? 53.057  -124.344 8.673   1.00 90.42  ? 125 LYS   J CB  1 
ATOM   17331 C  CG  . LYS   J  10 125 ? 52.944  -123.674 7.310   1.00 92.43  ? 125 LYS   J CG  1 
ATOM   17332 C  CD  . LYS   J  10 125 ? 53.043  -122.169 7.352   1.00 93.51  ? 125 LYS   J CD  1 
ATOM   17333 C  CE  . LYS   J  10 125 ? 54.455  -121.669 7.142   1.00 95.51  ? 125 LYS   J CE  1 
ATOM   17334 N  NZ  . LYS   J  10 125 ? 54.496  -120.193 7.043   1.00 96.72  ? 125 LYS   J NZ  1 
ATOM   17335 N  N   . VAL   J  10 126 ? 54.313  -126.759 6.757   1.00 92.72  ? 126 VAL   J N   1 
ATOM   17336 C  CA  . VAL   J  10 126 ? 55.516  -127.085 5.937   1.00 95.57  ? 126 VAL   J CA  1 
ATOM   17337 C  C   . VAL   J  10 126 ? 55.296  -126.537 4.522   1.00 95.55  ? 126 VAL   J C   1 
ATOM   17338 O  O   . VAL   J  10 126 ? 54.153  -126.626 4.028   1.00 98.10  ? 126 VAL   J O   1 
ATOM   17339 C  CB  . VAL   J  10 126 ? 55.792  -128.600 5.909   1.00 94.44  ? 126 VAL   J CB  1 
ATOM   17340 C  CG1 . VAL   J  10 126 ? 57.026  -128.926 5.084   1.00 97.28  ? 126 VAL   J CG1 1 
ATOM   17341 C  CG2 . VAL   J  10 126 ? 55.922  -129.181 7.308   1.00 94.42  ? 126 VAL   J CG2 1 
ATOM   17342 N  N   . GLU   J  10 127 ? 56.347  -125.979 3.910   1.00 99.66  ? 127 GLU   J N   1 
ATOM   17343 C  CA  . GLU   J  10 127 ? 56.394  -125.643 2.461   1.00 100.66 ? 127 GLU   J CA  1 
ATOM   17344 C  C   . GLU   J  10 127 ? 56.902  -126.881 1.714   1.00 97.55  ? 127 GLU   J C   1 
ATOM   17345 O  O   . GLU   J  10 127 ? 57.959  -127.413 2.112   1.00 93.73  ? 127 GLU   J O   1 
ATOM   17346 C  CB  . GLU   J  10 127 ? 57.285  -124.424 2.212   1.00 103.40 ? 127 GLU   J CB  1 
ATOM   17347 C  CG  . GLU   J  10 127 ? 56.970  -123.693 0.916   1.00 108.68 ? 127 GLU   J CG  1 
ATOM   17348 C  CD  . GLU   J  10 127 ? 57.483  -124.361 -0.351  1.00 113.86 ? 127 GLU   J CD  1 
ATOM   17349 O  OE1 . GLU   J  10 127 ? 58.664  -124.768 -0.370  1.00 116.56 ? 127 GLU   J OE1 1 
ATOM   17350 O  OE2 . GLU   J  10 127 ? 56.699  -124.478 -1.319  1.00 114.62 ? 127 GLU   J OE2 1 
ATOM   17351 N  N   . LEU   J  10 128 ? 56.173  -127.325 0.684   1.00 96.64  ? 128 LEU   J N   1 
ATOM   17352 C  CA  . LEU   J  10 128 ? 56.434  -128.598 -0.038  1.00 96.67  ? 128 LEU   J CA  1 
ATOM   17353 C  C   . LEU   J  10 128 ? 56.338  -128.388 -1.545  1.00 93.33  ? 128 LEU   J C   1 
ATOM   17354 O  O   . LEU   J  10 128 ? 55.551  -127.568 -2.011  1.00 93.15  ? 128 LEU   J O   1 
ATOM   17355 C  CB  . LEU   J  10 128 ? 55.410  -129.645 0.410   1.00 98.15  ? 128 LEU   J CB  1 
ATOM   17356 C  CG  . LEU   J  10 128 ? 55.569  -130.174 1.833   1.00 101.76 ? 128 LEU   J CG  1 
ATOM   17357 C  CD1 . LEU   J  10 128 ? 54.383  -131.049 2.208   1.00 103.45 ? 128 LEU   J CD1 1 
ATOM   17358 C  CD2 . LEU   J  10 128 ? 56.872  -130.946 1.991   1.00 105.48 ? 128 LEU   J CD2 1 
ATOM   17359 N  N   . PRO   J  10 129 ? 57.137  -129.123 -2.351  1.00 92.02  ? 129 PRO   J N   1 
ATOM   17360 C  CA  . PRO   J  10 129 ? 56.904  -129.210 -3.792  1.00 93.91  ? 129 PRO   J CA  1 
ATOM   17361 C  C   . PRO   J  10 129 ? 55.569  -129.900 -4.121  1.00 93.21  ? 129 PRO   J C   1 
ATOM   17362 O  O   . PRO   J  10 129 ? 54.935  -129.495 -5.075  1.00 95.50  ? 129 PRO   J O   1 
ATOM   17363 C  CB  . PRO   J  10 129 ? 58.108  -130.009 -4.317  1.00 96.70  ? 129 PRO   J CB  1 
ATOM   17364 C  CG  . PRO   J  10 129 ? 58.621  -130.766 -3.109  1.00 97.90  ? 129 PRO   J CG  1 
ATOM   17365 C  CD  . PRO   J  10 129 ? 58.336  -129.864 -1.928  1.00 94.07  ? 129 PRO   J CD  1 
ATOM   17366 N  N   . TYR   J  10 130 ? 55.180  -130.914 -3.340  1.00 90.49  ? 130 TYR   J N   1 
ATOM   17367 C  CA  . TYR   J  10 130 ? 53.876  -131.623 -3.460  1.00 91.46  ? 130 TYR   J CA  1 
ATOM   17368 C  C   . TYR   J  10 130 ? 53.370  -132.008 -2.066  1.00 88.24  ? 130 TYR   J C   1 
ATOM   17369 O  O   . TYR   J  10 130 ? 54.187  -132.401 -1.205  1.00 84.59  ? 130 TYR   J O   1 
ATOM   17370 C  CB  . TYR   J  10 130 ? 53.979  -132.842 -4.385  1.00 93.01  ? 130 TYR   J CB  1 
ATOM   17371 C  CG  . TYR   J  10 130 ? 55.251  -133.642 -4.263  1.00 93.80  ? 130 TYR   J CG  1 
ATOM   17372 C  CD1 . TYR   J  10 130 ? 55.347  -134.716 -3.394  1.00 92.98  ? 130 TYR   J CD1 1 
ATOM   17373 C  CD2 . TYR   J  10 130 ? 56.361  -133.328 -5.030  1.00 96.22  ? 130 TYR   J CD2 1 
ATOM   17374 C  CE1 . TYR   J  10 130 ? 56.516  -135.451 -3.285  1.00 96.17  ? 130 TYR   J CE1 1 
ATOM   17375 C  CE2 . TYR   J  10 130 ? 57.538  -134.052 -4.932  1.00 98.08  ? 130 TYR   J CE2 1 
ATOM   17376 C  CZ  . TYR   J  10 130 ? 57.616  -135.119 -4.058  1.00 98.42  ? 130 TYR   J CZ  1 
ATOM   17377 O  OH  . TYR   J  10 130 ? 58.778  -135.829 -3.973  1.00 104.19 ? 130 TYR   J OH  1 
ATOM   17378 N  N   . GLY   J  10 131 ? 52.051  -131.904 -1.868  1.00 87.36  ? 131 GLY   J N   1 
ATOM   17379 C  CA  . GLY   J  10 131 ? 51.382  -132.103 -0.569  1.00 88.64  ? 131 GLY   J CA  1 
ATOM   17380 C  C   . GLY   J  10 131 ? 50.064  -132.845 -0.703  1.00 90.35  ? 131 GLY   J C   1 
ATOM   17381 O  O   . GLY   J  10 131 ? 49.419  -132.741 -1.768  1.00 94.42  ? 131 GLY   J O   1 
ATOM   17382 N  N   . ALA   J  10 132 ? 49.681  -133.567 0.351   1.00 90.98  ? 132 ALA   J N   1 
ATOM   17383 C  CA  . ALA   J  10 132 ? 48.421  -134.335 0.463   1.00 94.20  ? 132 ALA   J CA  1 
ATOM   17384 C  C   . ALA   J  10 132 ? 47.988  -134.359 1.931   1.00 94.64  ? 132 ALA   J C   1 
ATOM   17385 O  O   . ALA   J  10 132 ? 48.869  -134.242 2.803   1.00 96.49  ? 132 ALA   J O   1 
ATOM   17386 C  CB  . ALA   J  10 132 ? 48.628  -135.730 -0.073  1.00 98.55  ? 132 ALA   J CB  1 
ATOM   17387 N  N   . HIS   J  10 133 ? 46.685  -134.495 2.187   1.00 95.73  ? 133 HIS   J N   1 
ATOM   17388 C  CA  . HIS   J  10 133 ? 46.103  -134.648 3.548   1.00 96.10  ? 133 HIS   J CA  1 
ATOM   17389 C  C   . HIS   J  10 133 ? 45.277  -135.932 3.614   1.00 99.15  ? 133 HIS   J C   1 
ATOM   17390 O  O   . HIS   J  10 133 ? 44.605  -136.250 2.613   1.00 102.34 ? 133 HIS   J O   1 
ATOM   17391 C  CB  . HIS   J  10 133 ? 45.266  -133.422 3.931   1.00 94.94  ? 133 HIS   J CB  1 
ATOM   17392 C  CG  . HIS   J  10 133 ? 46.052  -132.335 4.585   1.00 93.10  ? 133 HIS   J CG  1 
ATOM   17393 N  ND1 . HIS   J  10 133 ? 46.805  -132.551 5.722   1.00 93.15  ? 133 HIS   J ND1 1 
ATOM   17394 C  CD2 . HIS   J  10 133 ? 46.192  -131.027 4.284   1.00 92.10  ? 133 HIS   J CD2 1 
ATOM   17395 C  CE1 . HIS   J  10 133 ? 47.384  -131.426 6.085   1.00 91.99  ? 133 HIS   J CE1 1 
ATOM   17396 N  NE2 . HIS   J  10 133 ? 47.022  -130.476 5.222   1.00 90.90  ? 133 HIS   J NE2 1 
ATOM   17397 N  N   . GLY   J  10 134 ? 45.330  -136.624 4.757   1.00 98.34  ? 134 GLY   J N   1 
ATOM   17398 C  CA  . GLY   J  10 134 ? 44.608  -137.887 4.999   1.00 96.54  ? 134 GLY   J CA  1 
ATOM   17399 C  C   . GLY   J  10 134 ? 45.324  -139.069 4.371   1.00 99.75  ? 134 GLY   J C   1 
ATOM   17400 O  O   . GLY   J  10 134 ? 46.562  -139.001 4.226   1.00 99.22  ? 134 GLY   J O   1 
ATOM   17401 N  N   . TYR   J  10 135 ? 44.569  -140.105 3.993   1.00 101.94 ? 135 TYR   J N   1 
ATOM   17402 C  CA  . TYR   J  10 135 ? 45.090  -141.406 3.492   1.00 104.45 ? 135 TYR   J CA  1 
ATOM   17403 C  C   . TYR   J  10 135 ? 45.691  -141.245 2.087   1.00 103.17 ? 135 TYR   J C   1 
ATOM   17404 O  O   . TYR   J  10 135 ? 46.471  -142.126 1.681   1.00 106.59 ? 135 TYR   J O   1 
ATOM   17405 C  CB  . TYR   J  10 135 ? 43.992  -142.475 3.513   1.00 103.31 ? 135 TYR   J CB  1 
ATOM   17406 C  CG  . TYR   J  10 135 ? 43.547  -142.896 4.892   1.00 102.27 ? 135 TYR   J CG  1 
ATOM   17407 C  CD1 . TYR   J  10 135 ? 44.448  -143.425 5.804   1.00 100.67 ? 135 TYR   J CD1 1 
ATOM   17408 C  CD2 . TYR   J  10 135 ? 42.223  -142.779 5.284   1.00 102.64 ? 135 TYR   J CD2 1 
ATOM   17409 C  CE1 . TYR   J  10 135 ? 44.049  -143.817 7.071   1.00 101.26 ? 135 TYR   J CE1 1 
ATOM   17410 C  CE2 . TYR   J  10 135 ? 41.807  -143.167 6.547   1.00 102.60 ? 135 TYR   J CE2 1 
ATOM   17411 C  CZ  . TYR   J  10 135 ? 42.723  -143.686 7.444   1.00 102.29 ? 135 TYR   J CZ  1 
ATOM   17412 O  OH  . TYR   J  10 135 ? 42.319  -144.067 8.690   1.00 105.26 ? 135 TYR   J OH  1 
ATOM   17413 N  N   . SER   J  10 136 ? 45.341  -140.172 1.369   1.00 100.90 ? 136 SER   J N   1 
ATOM   17414 C  CA  . SER   J  10 136 ? 45.805  -139.880 -0.016  1.00 102.61 ? 136 SER   J CA  1 
ATOM   17415 C  C   . SER   J  10 136 ? 47.334  -139.893 -0.092  1.00 100.19 ? 136 SER   J C   1 
ATOM   17416 O  O   . SER   J  10 136 ? 47.867  -140.462 -1.060  1.00 106.74 ? 136 SER   J O   1 
ATOM   17417 C  CB  . SER   J  10 136 ? 45.279  -138.561 -0.504  1.00 104.53 ? 136 SER   J CB  1 
ATOM   17418 O  OG  . SER   J  10 136 ? 43.887  -138.442 -0.263  1.00 112.75 ? 136 SER   J OG  1 
ATOM   17419 N  N   . GLY   J  10 137 ? 48.004  -139.259 0.873   1.00 95.83  ? 137 GLY   J N   1 
ATOM   17420 C  CA  . GLY   J  10 137 ? 49.477  -139.217 0.966   1.00 98.03  ? 137 GLY   J CA  1 
ATOM   17421 C  C   . GLY   J  10 137 ? 50.102  -140.592 0.770   1.00 98.86  ? 137 GLY   J C   1 
ATOM   17422 O  O   . GLY   J  10 137 ? 51.089  -140.693 0.009   1.00 94.00  ? 137 GLY   J O   1 
ATOM   17423 N  N   . PHE   J  10 138 ? 49.528  -141.619 1.409   1.00 99.36  ? 138 PHE   J N   1 
ATOM   17424 C  CA  . PHE   J  10 138 ? 50.079  -142.997 1.506   1.00 102.38 ? 138 PHE   J CA  1 
ATOM   17425 C  C   . PHE   J  10 138 ? 50.270  -143.616 0.113   1.00 106.82 ? 138 PHE   J C   1 
ATOM   17426 O  O   . PHE   J  10 138 ? 51.102  -144.540 -0.002  1.00 113.38 ? 138 PHE   J O   1 
ATOM   17427 C  CB  . PHE   J  10 138 ? 49.188  -143.868 2.397   1.00 101.50 ? 138 PHE   J CB  1 
ATOM   17428 C  CG  . PHE   J  10 138 ? 49.368  -143.626 3.874   1.00 100.36 ? 138 PHE   J CG  1 
ATOM   17429 C  CD1 . PHE   J  10 138 ? 48.612  -142.673 4.539   1.00 98.19  ? 138 PHE   J CD1 1 
ATOM   17430 C  CD2 . PHE   J  10 138 ? 50.300  -144.351 4.599   1.00 102.69 ? 138 PHE   J CD2 1 
ATOM   17431 C  CE1 . PHE   J  10 138 ? 48.783  -142.455 5.898   1.00 99.11  ? 138 PHE   J CE1 1 
ATOM   17432 C  CE2 . PHE   J  10 138 ? 50.469  -144.134 5.958   1.00 104.16 ? 138 PHE   J CE2 1 
ATOM   17433 C  CZ  . PHE   J  10 138 ? 49.711  -143.185 6.604   1.00 101.13 ? 138 PHE   J CZ  1 
ATOM   17434 N  N   . TYR   J  10 139 ? 49.535  -143.143 -0.901  1.00 104.39 ? 139 TYR   J N   1 
ATOM   17435 C  CA  . TYR   J  10 139 ? 49.654  -143.608 -2.311  1.00 108.05 ? 139 TYR   J CA  1 
ATOM   17436 C  C   . TYR   J  10 139 ? 50.417  -142.599 -3.172  1.00 109.15 ? 139 TYR   J C   1 
ATOM   17437 O  O   . TYR   J  10 139 ? 51.204  -143.039 -4.033  1.00 109.22 ? 139 TYR   J O   1 
ATOM   17438 C  CB  . TYR   J  10 139 ? 48.276  -143.869 -2.919  1.00 111.62 ? 139 TYR   J CB  1 
ATOM   17439 C  CG  . TYR   J  10 139 ? 47.639  -145.138 -2.422  1.00 118.40 ? 139 TYR   J CG  1 
ATOM   17440 C  CD1 . TYR   J  10 139 ? 48.115  -146.377 -2.824  1.00 123.68 ? 139 TYR   J CD1 1 
ATOM   17441 C  CD2 . TYR   J  10 139 ? 46.583  -145.104 -1.529  1.00 120.68 ? 139 TYR   J CD2 1 
ATOM   17442 C  CE1 . TYR   J  10 139 ? 47.546  -147.551 -2.361  1.00 127.83 ? 139 TYR   J CE1 1 
ATOM   17443 C  CE2 . TYR   J  10 139 ? 46.000  -146.269 -1.057  1.00 125.16 ? 139 TYR   J CE2 1 
ATOM   17444 C  CZ  . TYR   J  10 139 ? 46.484  -147.497 -1.475  1.00 128.94 ? 139 TYR   J CZ  1 
ATOM   17445 O  OH  . TYR   J  10 139 ? 45.921  -148.653 -1.020  1.00 133.02 ? 139 TYR   J OH  1 
ATOM   17446 N  N   . THR   J  10 140 ? 50.177  -141.302 -2.965  1.00 108.46 ? 140 THR   J N   1 
ATOM   17447 C  CA  . THR   J  10 140 ? 50.649  -140.216 -3.863  1.00 106.66 ? 140 THR   J CA  1 
ATOM   17448 C  C   . THR   J  10 140 ? 52.134  -139.929 -3.606  1.00 104.09 ? 140 THR   J C   1 
ATOM   17449 O  O   . THR   J  10 140 ? 52.880  -139.885 -4.598  1.00 102.34 ? 140 THR   J O   1 
ATOM   17450 C  CB  . THR   J  10 140 ? 49.734  -138.993 -3.743  1.00 106.62 ? 140 THR   J CB  1 
ATOM   17451 O  OG1 . THR   J  10 140 ? 49.644  -138.634 -2.364  1.00 107.83 ? 140 THR   J OG1 1 
ATOM   17452 C  CG2 . THR   J  10 140 ? 48.352  -139.263 -4.296  1.00 107.21 ? 140 THR   J CG2 1 
ATOM   17453 N  N   . PHE   J  10 141 ? 52.555  -139.767 -2.344  1.00 106.50 ? 141 PHE   J N   1 
ATOM   17454 C  CA  . PHE   J  10 141 ? 53.916  -139.283 -1.972  1.00 108.75 ? 141 PHE   J CA  1 
ATOM   17455 C  C   . PHE   J  10 141 ? 54.988  -140.141 -2.663  1.00 107.46 ? 141 PHE   J C   1 
ATOM   17456 O  O   . PHE   J  10 141 ? 55.880  -139.567 -3.315  1.00 99.90  ? 141 PHE   J O   1 
ATOM   17457 C  CB  . PHE   J  10 141 ? 54.111  -139.235 -0.452  1.00 110.02 ? 141 PHE   J CB  1 
ATOM   17458 C  CG  . PHE   J  10 141 ? 53.701  -137.937 0.200   1.00 111.82 ? 141 PHE   J CG  1 
ATOM   17459 C  CD1 . PHE   J  10 141 ? 54.328  -136.744 -0.133  1.00 116.49 ? 141 PHE   J CD1 1 
ATOM   17460 C  CD2 . PHE   J  10 141 ? 52.702  -137.906 1.162   1.00 113.68 ? 141 PHE   J CD2 1 
ATOM   17461 C  CE1 . PHE   J  10 141 ? 53.956  -135.551 0.471   1.00 119.48 ? 141 PHE   J CE1 1 
ATOM   17462 C  CE2 . PHE   J  10 141 ? 52.332  -136.714 1.766   1.00 115.87 ? 141 PHE   J CE2 1 
ATOM   17463 C  CZ  . PHE   J  10 141 ? 52.960  -135.538 1.421   1.00 119.30 ? 141 PHE   J CZ  1 
ATOM   17464 N  N   . SER   J  10 142 ? 54.898  -141.467 -2.535  1.00 111.71 ? 142 SER   J N   1 
ATOM   17465 C  CA  . SER   J  10 142 ? 55.827  -142.451 -3.160  1.00 114.60 ? 142 SER   J CA  1 
ATOM   17466 C  C   . SER   J  10 142 ? 55.797  -142.332 -4.690  1.00 113.44 ? 142 SER   J C   1 
ATOM   17467 O  O   . SER   J  10 142 ? 56.863  -142.512 -5.322  1.00 108.06 ? 142 SER   J O   1 
ATOM   17468 C  CB  . SER   J  10 142 ? 55.490  -143.855 -2.734  1.00 119.27 ? 142 SER   J CB  1 
ATOM   17469 O  OG  . SER   J  10 142 ? 54.232  -144.255 -3.263  1.00 119.58 ? 142 SER   J OG  1 
ATOM   17470 N  N   . LEU   J  10 143 ? 54.611  -142.080 -5.255  1.00 113.09 ? 143 LEU   J N   1 
ATOM   17471 C  CA  . LEU   J  10 143 ? 54.378  -141.903 -6.716  1.00 113.89 ? 143 LEU   J CA  1 
ATOM   17472 C  C   . LEU   J  10 143 ? 55.080  -140.624 -7.190  1.00 110.54 ? 143 LEU   J C   1 
ATOM   17473 O  O   . LEU   J  10 143 ? 55.814  -140.689 -8.195  1.00 109.74 ? 143 LEU   J O   1 
ATOM   17474 C  CB  . LEU   J  10 143 ? 52.867  -141.841 -6.974  1.00 112.54 ? 143 LEU   J CB  1 
ATOM   17475 C  CG  . LEU   J  10 143 ? 52.426  -141.969 -8.432  1.00 113.59 ? 143 LEU   J CG  1 
ATOM   17476 C  CD1 . LEU   J  10 143 ? 51.003  -142.500 -8.521  1.00 110.69 ? 143 LEU   J CD1 1 
ATOM   17477 C  CD2 . LEU   J  10 143 ? 52.533  -140.637 -9.160  1.00 114.42 ? 143 LEU   J CD2 1 
ATOM   17478 N  N   . LEU   J  10 144 ? 54.851  -139.507 -6.491  1.00 111.78 ? 144 LEU   J N   1 
ATOM   17479 C  CA  . LEU   J  10 144 ? 55.430  -138.172 -6.810  1.00 111.59 ? 144 LEU   J CA  1 
ATOM   17480 C  C   . LEU   J  10 144 ? 56.936  -138.172 -6.520  1.00 109.09 ? 144 LEU   J C   1 
ATOM   17481 O  O   . LEU   J  10 144 ? 57.676  -137.571 -7.313  1.00 109.63 ? 144 LEU   J O   1 
ATOM   17482 C  CB  . LEU   J  10 144 ? 54.700  -137.088 -6.004  1.00 110.99 ? 144 LEU   J CB  1 
ATOM   17483 C  CG  . LEU   J  10 144 ? 53.586  -136.318 -6.722  1.00 113.34 ? 144 LEU   J CG  1 
ATOM   17484 C  CD1 . LEU   J  10 144 ? 53.088  -137.034 -7.971  1.00 115.67 ? 144 LEU   J CD1 1 
ATOM   17485 C  CD2 . LEU   J  10 144 ? 52.425  -136.038 -5.776  1.00 111.43 ? 144 LEU   J CD2 1 
ATOM   17486 N  N   . ASP   J  10 145 ? 57.379  -138.829 -5.442  1.00 108.96 ? 145 ASP   J N   1 
ATOM   17487 C  CA  . ASP   J  10 145 ? 58.824  -139.005 -5.126  1.00 113.71 ? 145 ASP   J CA  1 
ATOM   17488 C  C   . ASP   J  10 145 ? 59.544  -139.487 -6.391  1.00 115.64 ? 145 ASP   J C   1 
ATOM   17489 O  O   . ASP   J  10 145 ? 60.667  -139.013 -6.649  1.00 116.07 ? 145 ASP   J O   1 
ATOM   17490 C  CB  . ASP   J  10 145 ? 59.044  -139.977 -3.961  1.00 116.99 ? 145 ASP   J CB  1 
ATOM   17491 C  CG  . ASP   J  10 145 ? 58.889  -139.363 -2.578  1.00 116.91 ? 145 ASP   J CG  1 
ATOM   17492 O  OD1 . ASP   J  10 145 ? 58.796  -138.121 -2.487  1.00 112.90 ? 145 ASP   J OD1 1 
ATOM   17493 O  OD2 . ASP   J  10 145 ? 58.867  -140.138 -1.598  1.00 122.82 ? 145 ASP   J OD2 1 
ATOM   17494 N  N   . HIS   J  10 146 ? 58.898  -140.373 -7.156  1.00 121.24 ? 146 HIS   J N   1 
ATOM   17495 C  CA  . HIS   J  10 146 ? 59.448  -141.030 -8.371  1.00 125.89 ? 146 HIS   J CA  1 
ATOM   17496 C  C   . HIS   J  10 146 ? 59.371  -140.072 -9.568  1.00 127.67 ? 146 HIS   J C   1 
ATOM   17497 O  O   . HIS   J  10 146 ? 60.439  -139.744 -10.121 1.00 127.98 ? 146 HIS   J O   1 
ATOM   17498 C  CB  . HIS   J  10 146 ? 58.719  -142.364 -8.610  1.00 129.11 ? 146 HIS   J CB  1 
ATOM   17499 C  CG  . HIS   J  10 146 ? 59.266  -143.185 -9.731  1.00 132.94 ? 146 HIS   J CG  1 
ATOM   17500 N  ND1 . HIS   J  10 146 ? 60.612  -143.469 -9.860  1.00 134.08 ? 146 HIS   J ND1 1 
ATOM   17501 C  CD2 . HIS   J  10 146 ? 58.649  -143.809 -10.758 1.00 133.47 ? 146 HIS   J CD2 1 
ATOM   17502 C  CE1 . HIS   J  10 146 ? 60.799  -144.217 -10.928 1.00 135.34 ? 146 HIS   J CE1 1 
ATOM   17503 N  NE2 . HIS   J  10 146 ? 59.612  -144.439 -11.495 1.00 134.59 ? 146 HIS   J NE2 1 
ATOM   17504 N  N   . HIS   J  10 147 ? 58.163  -139.620 -9.927  1.00 128.47 ? 147 HIS   J N   1 
ATOM   17505 C  CA  . HIS   J  10 147 ? 57.845  -139.000 -11.245 1.00 130.78 ? 147 HIS   J CA  1 
ATOM   17506 C  C   . HIS   J  10 147 ? 58.059  -137.477 -11.245 1.00 126.49 ? 147 HIS   J C   1 
ATOM   17507 O  O   . HIS   J  10 147 ? 58.272  -136.933 -12.344 1.00 122.49 ? 147 HIS   J O   1 
ATOM   17508 C  CB  . HIS   J  10 147 ? 56.414  -139.353 -11.679 1.00 133.57 ? 147 HIS   J CB  1 
ATOM   17509 C  CG  . HIS   J  10 147 ? 56.228  -140.781 -12.067 1.00 138.18 ? 147 HIS   J CG  1 
ATOM   17510 N  ND1 . HIS   J  10 147 ? 55.370  -141.624 -11.384 1.00 144.42 ? 147 HIS   J ND1 1 
ATOM   17511 C  CD2 . HIS   J  10 147 ? 56.776  -141.518 -13.057 1.00 144.77 ? 147 HIS   J CD2 1 
ATOM   17512 C  CE1 . HIS   J  10 147 ? 55.398  -142.819 -11.937 1.00 146.00 ? 147 HIS   J CE1 1 
ATOM   17513 N  NE2 . HIS   J  10 147 ? 56.254  -142.781 -12.966 1.00 146.52 ? 147 HIS   J NE2 1 
ATOM   17514 N  N   . TYR   J  10 148 ? 57.996  -136.806 -10.088 1.00 126.37 ? 148 TYR   J N   1 
ATOM   17515 C  CA  . TYR   J  10 148 ? 58.044  -135.319 -9.982  1.00 125.53 ? 148 TYR   J CA  1 
ATOM   17516 C  C   . TYR   J  10 148 ? 59.452  -134.796 -10.291 1.00 128.16 ? 148 TYR   J C   1 
ATOM   17517 O  O   . TYR   J  10 148 ? 60.437  -135.370 -9.784  1.00 127.31 ? 148 TYR   J O   1 
ATOM   17518 C  CB  . TYR   J  10 148 ? 57.634  -134.825 -8.592  1.00 120.49 ? 148 TYR   J CB  1 
ATOM   17519 C  CG  . TYR   J  10 148 ? 57.814  -133.342 -8.381  1.00 117.54 ? 148 TYR   J CG  1 
ATOM   17520 C  CD1 . TYR   J  10 148 ? 56.829  -132.442 -8.753  1.00 116.41 ? 148 TYR   J CD1 1 
ATOM   17521 C  CD2 . TYR   J  10 148 ? 58.974  -132.833 -7.816  1.00 115.37 ? 148 TYR   J CD2 1 
ATOM   17522 C  CE1 . TYR   J  10 148 ? 56.988  -131.079 -8.564  1.00 116.60 ? 148 TYR   J CE1 1 
ATOM   17523 C  CE2 . TYR   J  10 148 ? 59.149  -131.473 -7.618  1.00 113.95 ? 148 TYR   J CE2 1 
ATOM   17524 C  CZ  . TYR   J  10 148 ? 58.152  -130.591 -7.995  1.00 116.16 ? 148 TYR   J CZ  1 
ATOM   17525 O  OH  . TYR   J  10 148 ? 58.321  -129.250 -7.806  1.00 120.78 ? 148 TYR   J OH  1 
ATOM   17526 N  N   . ARG   J  10 149 ? 59.523  -133.715 -11.075 1.00 129.11 ? 149 ARG   J N   1 
ATOM   17527 C  CA  . ARG   J  10 149 ? 60.750  -132.908 -11.320 1.00 133.51 ? 149 ARG   J CA  1 
ATOM   17528 C  C   . ARG   J  10 149 ? 60.434  -131.441 -11.031 1.00 133.00 ? 149 ARG   J C   1 
ATOM   17529 O  O   . ARG   J  10 149 ? 59.338  -130.968 -11.330 1.00 126.36 ? 149 ARG   J O   1 
ATOM   17530 C  CB  . ARG   J  10 149 ? 61.252  -133.099 -12.757 1.00 136.46 ? 149 ARG   J CB  1 
ATOM   17531 C  CG  . ARG   J  10 149 ? 61.570  -134.540 -13.135 1.00 140.33 ? 149 ARG   J CG  1 
ATOM   17532 C  CD  . ARG   J  10 149 ? 62.777  -135.113 -12.411 1.00 139.91 ? 149 ARG   J CD  1 
ATOM   17533 N  NE  . ARG   J  10 149 ? 63.105  -136.470 -12.844 1.00 142.19 ? 149 ARG   J NE  1 
ATOM   17534 C  CZ  . ARG   J  10 149 ? 62.561  -137.591 -12.366 1.00 141.12 ? 149 ARG   J CZ  1 
ATOM   17535 N  NH1 . ARG   J  10 149 ? 61.636  -137.549 -11.420 1.00 141.53 ? 149 ARG   J NH1 1 
ATOM   17536 N  NH2 . ARG   J  10 149 ? 62.948  -138.761 -12.842 1.00 141.32 ? 149 ARG   J NH2 1 
ATOM   17537 N  N   . PRO   J  10 150 ? 61.382  -130.671 -10.447 1.00 134.02 ? 150 PRO   J N   1 
ATOM   17538 C  CA  . PRO   J  10 150 ? 61.102  -129.306 -9.989  1.00 130.83 ? 150 PRO   J CA  1 
ATOM   17539 C  C   . PRO   J  10 150 ? 60.865  -128.268 -11.100 1.00 127.28 ? 150 PRO   J C   1 
ATOM   17540 O  O   . PRO   J  10 150 ? 60.374  -127.200 -10.782 1.00 124.08 ? 150 PRO   J O   1 
ATOM   17541 C  CB  . PRO   J  10 150 ? 62.370  -128.932 -9.202  1.00 133.08 ? 150 PRO   J CB  1 
ATOM   17542 C  CG  . PRO   J  10 150 ? 63.459  -129.771 -9.835  1.00 138.64 ? 150 PRO   J CG  1 
ATOM   17543 C  CD  . PRO   J  10 150 ? 62.775  -131.074 -10.195 1.00 139.67 ? 150 PRO   J CD  1 
ATOM   17544 N  N   . ASP   J  10 151 ? 61.207  -128.599 -12.352 1.00 126.68 ? 151 ASP   J N   1 
ATOM   17545 C  CA  . ASP   J  10 151 ? 61.189  -127.667 -13.514 1.00 121.77 ? 151 ASP   J CA  1 
ATOM   17546 C  C   . ASP   J  10 151 ? 60.036  -128.015 -14.466 1.00 115.06 ? 151 ASP   J C   1 
ATOM   17547 O  O   . ASP   J  10 151 ? 60.111  -127.609 -15.638 1.00 114.68 ? 151 ASP   J O   1 
ATOM   17548 C  CB  . ASP   J  10 151 ? 62.530  -127.701 -14.255 1.00 124.52 ? 151 ASP   J CB  1 
ATOM   17549 C  CG  . ASP   J  10 151 ? 62.864  -129.046 -14.885 1.00 126.79 ? 151 ASP   J CG  1 
ATOM   17550 O  OD1 . ASP   J  10 151 ? 62.416  -130.079 -14.345 1.00 125.71 ? 151 ASP   J OD1 1 
ATOM   17551 O  OD2 . ASP   J  10 151 ? 63.570  -129.050 -15.912 1.00 126.81 ? 151 ASP   J OD2 1 
ATOM   17552 N  N   . MET   J  10 152 ? 59.009  -128.728 -13.991 1.00 114.26 ? 152 MET   J N   1 
ATOM   17553 C  CA  . MET   J  10 152 ? 57.885  -129.219 -14.835 1.00 115.98 ? 152 MET   J CA  1 
ATOM   17554 C  C   . MET   J  10 152 ? 56.994  -128.040 -15.237 1.00 111.36 ? 152 MET   J C   1 
ATOM   17555 O  O   . MET   J  10 152 ? 56.937  -127.064 -14.476 1.00 109.16 ? 152 MET   J O   1 
ATOM   17556 C  CB  . MET   J  10 152 ? 57.043  -130.262 -14.095 1.00 120.22 ? 152 MET   J CB  1 
ATOM   17557 C  CG  . MET   J  10 152 ? 57.724  -131.607 -13.979 1.00 123.18 ? 152 MET   J CG  1 
ATOM   17558 S  SD  . MET   J  10 152 ? 56.807  -132.731 -12.896 1.00 127.16 ? 152 MET   J SD  1 
ATOM   17559 C  CE  . MET   J  10 152 ? 55.774  -133.562 -14.102 1.00 127.11 ? 152 MET   J CE  1 
ATOM   17560 N  N   . THR   J  10 153 ? 56.342  -128.136 -16.399 1.00 110.12 ? 153 THR   J N   1 
ATOM   17561 C  CA  . THR   J  10 153 ? 55.332  -127.159 -16.888 1.00 111.57 ? 153 THR   J CA  1 
ATOM   17562 C  C   . THR   J  10 153 ? 53.991  -127.457 -16.216 1.00 110.24 ? 153 THR   J C   1 
ATOM   17563 O  O   . THR   J  10 153 ? 53.862  -128.544 -15.629 1.00 110.39 ? 153 THR   J O   1 
ATOM   17564 C  CB  . THR   J  10 153 ? 55.201  -127.195 -18.415 1.00 114.49 ? 153 THR   J CB  1 
ATOM   17565 O  OG1 . THR   J  10 153 ? 54.894  -128.530 -18.815 1.00 117.61 ? 153 THR   J OG1 1 
ATOM   17566 C  CG2 . THR   J  10 153 ? 56.456  -126.725 -19.115 1.00 116.05 ? 153 THR   J CG2 1 
ATOM   17567 N  N   . THR   J  10 154 ? 53.041  -126.521 -16.291 1.00 113.46 ? 154 THR   J N   1 
ATOM   17568 C  CA  . THR   J  10 154 ? 51.653  -126.689 -15.782 1.00 113.10 ? 154 THR   J CA  1 
ATOM   17569 C  C   . THR   J  10 154 ? 51.038  -127.942 -16.422 1.00 115.44 ? 154 THR   J C   1 
ATOM   17570 O  O   . THR   J  10 154 ? 50.350  -128.691 -15.702 1.00 111.22 ? 154 THR   J O   1 
ATOM   17571 C  CB  . THR   J  10 154 ? 50.804  -125.435 -16.033 1.00 111.87 ? 154 THR   J CB  1 
ATOM   17572 O  OG1 . THR   J  10 154 ? 51.421  -124.336 -15.361 1.00 111.50 ? 154 THR   J OG1 1 
ATOM   17573 C  CG2 . THR   J  10 154 ? 49.376  -125.582 -15.553 1.00 108.23 ? 154 THR   J CG2 1 
ATOM   17574 N  N   . GLU   J  10 155 ? 51.295  -128.165 -17.715 1.00 120.94 ? 155 GLU   J N   1 
ATOM   17575 C  CA  . GLU   J  10 155 ? 50.755  -129.316 -18.491 1.00 125.43 ? 155 GLU   J CA  1 
ATOM   17576 C  C   . GLU   J  10 155 ? 51.335  -130.631 -17.955 1.00 123.47 ? 155 GLU   J C   1 
ATOM   17577 O  O   . GLU   J  10 155 ? 50.556  -131.596 -17.805 1.00 120.82 ? 155 GLU   J O   1 
ATOM   17578 C  CB  . GLU   J  10 155 ? 51.050  -129.159 -19.985 1.00 133.28 ? 155 GLU   J CB  1 
ATOM   17579 C  CG  . GLU   J  10 155 ? 49.915  -128.508 -20.754 1.00 139.25 ? 155 GLU   J CG  1 
ATOM   17580 C  CD  . GLU   J  10 155 ? 48.611  -129.290 -20.719 1.00 145.70 ? 155 GLU   J CD  1 
ATOM   17581 O  OE1 . GLU   J  10 155 ? 48.654  -130.522 -20.923 1.00 150.98 ? 155 GLU   J OE1 1 
ATOM   17582 O  OE2 . GLU   J  10 155 ? 47.559  -128.669 -20.468 1.00 148.53 ? 155 GLU   J OE2 1 
ATOM   17583 N  N   . GLU   J  10 156 ? 52.648  -130.669 -17.701 1.00 122.08 ? 156 GLU   J N   1 
ATOM   17584 C  CA  . GLU   J  10 156 ? 53.350  -131.831 -17.090 1.00 119.45 ? 156 GLU   J CA  1 
ATOM   17585 C  C   . GLU   J  10 156 ? 52.768  -132.082 -15.694 1.00 118.91 ? 156 GLU   J C   1 
ATOM   17586 O  O   . GLU   J  10 156 ? 52.505  -133.256 -15.370 1.00 121.63 ? 156 GLU   J O   1 
ATOM   17587 C  CB  . GLU   J  10 156 ? 54.860  -131.584 -17.033 1.00 119.52 ? 156 GLU   J CB  1 
ATOM   17588 C  CG  . GLU   J  10 156 ? 55.553  -131.750 -18.372 1.00 121.80 ? 156 GLU   J CG  1 
ATOM   17589 C  CD  . GLU   J  10 156 ? 57.019  -131.352 -18.378 1.00 123.42 ? 156 GLU   J CD  1 
ATOM   17590 O  OE1 . GLU   J  10 156 ? 57.869  -132.235 -18.601 1.00 127.81 ? 156 GLU   J OE1 1 
ATOM   17591 O  OE2 . GLU   J  10 156 ? 57.307  -130.159 -18.166 1.00 119.72 ? 156 GLU   J OE2 1 
ATOM   17592 N  N   . GLY   J  10 157 ? 52.572  -131.015 -14.912 1.00 115.83 ? 157 GLY   J N   1 
ATOM   17593 C  CA  . GLY   J  10 157 ? 51.957  -131.055 -13.571 1.00 113.32 ? 157 GLY   J CA  1 
ATOM   17594 C  C   . GLY   J  10 157 ? 50.584  -131.705 -13.593 1.00 111.45 ? 157 GLY   J C   1 
ATOM   17595 O  O   . GLY   J  10 157 ? 50.300  -132.501 -12.680 1.00 111.09 ? 157 GLY   J O   1 
ATOM   17596 N  N   . LEU   J  10 158 ? 49.763  -131.385 -14.599 1.00 113.16 ? 158 LEU   J N   1 
ATOM   17597 C  CA  . LEU   J  10 158 ? 48.379  -131.914 -14.750 1.00 113.25 ? 158 LEU   J CA  1 
ATOM   17598 C  C   . LEU   J  10 158 ? 48.422  -133.406 -15.107 1.00 114.77 ? 158 LEU   J C   1 
ATOM   17599 O  O   . LEU   J  10 158 ? 47.550  -134.141 -14.612 1.00 116.98 ? 158 LEU   J O   1 
ATOM   17600 C  CB  . LEU   J  10 158 ? 47.630  -131.112 -15.820 1.00 114.96 ? 158 LEU   J CB  1 
ATOM   17601 C  CG  . LEU   J  10 158 ? 47.235  -129.688 -15.426 1.00 112.36 ? 158 LEU   J CG  1 
ATOM   17602 C  CD1 . LEU   J  10 158 ? 46.817  -128.890 -16.652 1.00 113.67 ? 158 LEU   J CD1 1 
ATOM   17603 C  CD2 . LEU   J  10 158 ? 46.122  -129.689 -14.388 1.00 108.66 ? 158 LEU   J CD2 1 
ATOM   17604 N  N   . ASP   J  10 159 ? 49.384  -133.830 -15.936 1.00 117.59 ? 159 ASP   J N   1 
ATOM   17605 C  CA  . ASP   J  10 159 ? 49.592  -135.255 -16.324 1.00 119.56 ? 159 ASP   J CA  1 
ATOM   17606 C  C   . ASP   J  10 159 ? 50.071  -136.054 -15.104 1.00 114.58 ? 159 ASP   J C   1 
ATOM   17607 O  O   . ASP   J  10 159 ? 49.604  -137.196 -14.925 1.00 115.48 ? 159 ASP   J O   1 
ATOM   17608 C  CB  . ASP   J  10 159 ? 50.587  -135.388 -17.481 1.00 124.82 ? 159 ASP   J CB  1 
ATOM   17609 C  CG  . ASP   J  10 159 ? 50.078  -134.863 -18.814 1.00 126.74 ? 159 ASP   J CG  1 
ATOM   17610 O  OD1 . ASP   J  10 159 ? 48.844  -134.765 -18.980 1.00 130.10 ? 159 ASP   J OD1 1 
ATOM   17611 O  OD2 . ASP   J  10 159 ? 50.920  -134.559 -19.681 1.00 130.28 ? 159 ASP   J OD2 1 
ATOM   17612 N  N   . LEU   J  10 160 ? 50.976  -135.471 -14.311 1.00 110.24 ? 160 LEU   J N   1 
ATOM   17613 C  CA  . LEU   J  10 160 ? 51.510  -136.049 -13.048 1.00 108.20 ? 160 LEU   J CA  1 
ATOM   17614 C  C   . LEU   J  10 160 ? 50.368  -136.207 -12.038 1.00 106.51 ? 160 LEU   J C   1 
ATOM   17615 O  O   . LEU   J  10 160 ? 50.400  -137.177 -11.259 1.00 103.12 ? 160 LEU   J O   1 
ATOM   17616 C  CB  . LEU   J  10 160 ? 52.594  -135.114 -12.505 1.00 108.88 ? 160 LEU   J CB  1 
ATOM   17617 C  CG  . LEU   J  10 160 ? 53.494  -135.684 -11.409 1.00 108.88 ? 160 LEU   J CG  1 
ATOM   17618 C  CD1 . LEU   J  10 160 ? 54.420  -136.749 -11.968 1.00 109.07 ? 160 LEU   J CD1 1 
ATOM   17619 C  CD2 . LEU   J  10 160 ? 54.305  -134.576 -10.752 1.00 110.19 ? 160 LEU   J CD2 1 
ATOM   17620 N  N   . LEU   J  10 161 ? 49.413  -135.270 -12.053 1.00 108.32 ? 161 LEU   J N   1 
ATOM   17621 C  CA  . LEU   J  10 161 ? 48.217  -135.241 -11.167 1.00 108.61 ? 161 LEU   J CA  1 
ATOM   17622 C  C   . LEU   J  10 161 ? 47.214  -136.309 -11.623 1.00 113.51 ? 161 LEU   J C   1 
ATOM   17623 O  O   . LEU   J  10 161 ? 46.615  -136.960 -10.744 1.00 114.28 ? 161 LEU   J O   1 
ATOM   17624 C  CB  . LEU   J  10 161 ? 47.603  -133.838 -11.217 1.00 109.15 ? 161 LEU   J CB  1 
ATOM   17625 C  CG  . LEU   J  10 161 ? 46.585  -133.502 -10.129 1.00 107.01 ? 161 LEU   J CG  1 
ATOM   17626 C  CD1 . LEU   J  10 161 ? 47.253  -133.377 -8.767  1.00 102.82 ? 161 LEU   J CD1 1 
ATOM   17627 C  CD2 . LEU   J  10 161 ? 45.859  -132.213 -10.481 1.00 109.97 ? 161 LEU   J CD2 1 
ATOM   17628 N  N   . LYS   J  10 162 ? 47.034  -136.479 -12.939 1.00 116.07 ? 162 LYS   J N   1 
ATOM   17629 C  CA  . LYS   J  10 162 ? 46.164  -137.532 -13.538 1.00 118.60 ? 162 LYS   J CA  1 
ATOM   17630 C  C   . LYS   J  10 162 ? 46.622  -138.912 -13.055 1.00 118.95 ? 162 LYS   J C   1 
ATOM   17631 O  O   . LYS   J  10 162 ? 45.753  -139.761 -12.773 1.00 118.99 ? 162 LYS   J O   1 
ATOM   17632 C  CB  . LYS   J  10 162 ? 46.210  -137.499 -15.068 1.00 124.15 ? 162 LYS   J CB  1 
ATOM   17633 C  CG  . LYS   J  10 162 ? 45.322  -136.454 -15.725 1.00 124.44 ? 162 LYS   J CG  1 
ATOM   17634 C  CD  . LYS   J  10 162 ? 45.297  -136.572 -17.229 1.00 130.86 ? 162 LYS   J CD  1 
ATOM   17635 C  CE  . LYS   J  10 162 ? 44.432  -137.717 -17.712 1.00 134.67 ? 162 LYS   J CE  1 
ATOM   17636 N  NZ  . LYS   J  10 162 ? 44.584  -137.938 -19.170 1.00 140.52 ? 162 LYS   J NZ  1 
ATOM   17637 N  N   . LEU   J  10 163 ? 47.940  -139.113 -12.982 1.00 118.28 ? 163 LEU   J N   1 
ATOM   17638 C  CA  . LEU   J  10 163 ? 48.580  -140.374 -12.523 1.00 117.87 ? 163 LEU   J CA  1 
ATOM   17639 C  C   . LEU   J  10 163 ? 48.183  -140.637 -11.065 1.00 116.02 ? 163 LEU   J C   1 
ATOM   17640 O  O   . LEU   J  10 163 ? 47.924  -141.809 -10.730 1.00 120.22 ? 163 LEU   J O   1 
ATOM   17641 C  CB  . LEU   J  10 163 ? 50.101  -140.249 -12.680 1.00 117.25 ? 163 LEU   J CB  1 
ATOM   17642 C  CG  . LEU   J  10 163 ? 50.817  -141.452 -13.293 1.00 119.11 ? 163 LEU   J CG  1 
ATOM   17643 C  CD1 . LEU   J  10 163 ? 50.225  -141.823 -14.645 1.00 120.55 ? 163 LEU   J CD1 1 
ATOM   17644 C  CD2 . LEU   J  10 163 ? 52.305  -141.165 -13.433 1.00 119.05 ? 163 LEU   J CD2 1 
ATOM   17645 N  N   . CYS   J  10 164 ? 48.118  -139.587 -10.240 1.00 112.85 ? 164 CYS   J N   1 
ATOM   17646 C  CA  . CYS   J  10 164 ? 47.775  -139.668 -8.795  1.00 110.30 ? 164 CYS   J CA  1 
ATOM   17647 C  C   . CYS   J  10 164 ? 46.296  -140.038 -8.627  1.00 108.14 ? 164 CYS   J C   1 
ATOM   17648 O  O   . CYS   J  10 164 ? 46.016  -140.943 -7.822  1.00 107.54 ? 164 CYS   J O   1 
ATOM   17649 C  CB  . CYS   J  10 164 ? 48.103  -138.367 -8.072  1.00 109.70 ? 164 CYS   J CB  1 
ATOM   17650 S  SG  . CYS   J  10 164 ? 49.885  -138.047 -7.994  1.00 111.28 ? 164 CYS   J SG  1 
ATOM   17651 N  N   . VAL   J  10 165 ? 45.395  -139.377 -9.364  1.00 107.42 ? 165 VAL   J N   1 
ATOM   17652 C  CA  . VAL   J  10 165 ? 43.923  -139.640 -9.318  1.00 106.86 ? 165 VAL   J CA  1 
ATOM   17653 C  C   . VAL   J  10 165 ? 43.661  -141.084 -9.765  1.00 106.35 ? 165 VAL   J C   1 
ATOM   17654 O  O   . VAL   J  10 165 ? 42.808  -141.744 -9.141  1.00 106.32 ? 165 VAL   J O   1 
ATOM   17655 C  CB  . VAL   J  10 165 ? 43.126  -138.634 -10.172 1.00 106.73 ? 165 VAL   J CB  1 
ATOM   17656 C  CG1 . VAL   J  10 165 ? 41.664  -139.036 -10.307 1.00 109.08 ? 165 VAL   J CG1 1 
ATOM   17657 C  CG2 . VAL   J  10 165 ? 43.230  -137.222 -9.619  1.00 104.16 ? 165 VAL   J CG2 1 
ATOM   17658 N  N   . GLN   J  10 166 ? 44.360  -141.547 -10.806 1.00 108.82 ? 166 GLN   J N   1 
ATOM   17659 C  CA  . GLN   J  10 166 ? 44.230  -142.921 -11.366 1.00 112.30 ? 166 GLN   J CA  1 
ATOM   17660 C  C   . GLN   J  10 166 ? 44.582  -143.956 -10.291 1.00 109.40 ? 166 GLN   J C   1 
ATOM   17661 O  O   . GLN   J  10 166 ? 43.797  -144.909 -10.117 1.00 108.89 ? 166 GLN   J O   1 
ATOM   17662 C  CB  . GLN   J  10 166 ? 45.123  -143.093 -12.596 1.00 116.39 ? 166 GLN   J CB  1 
ATOM   17663 C  CG  . GLN   J  10 166 ? 44.460  -142.632 -13.886 1.00 120.87 ? 166 GLN   J CG  1 
ATOM   17664 C  CD  . GLN   J  10 166 ? 45.440  -142.442 -15.018 1.00 125.03 ? 166 GLN   J CD  1 
ATOM   17665 O  OE1 . GLN   J  10 166 ? 46.528  -143.015 -15.032 1.00 130.81 ? 166 GLN   J OE1 1 
ATOM   17666 N  NE2 . GLN   J  10 166 ? 45.057  -141.629 -15.990 1.00 127.20 ? 166 GLN   J NE2 1 
ATOM   17667 N  N   . GLU   J  10 167 ? 45.717  -143.768 -9.607  1.00 108.07 ? 167 GLU   J N   1 
ATOM   17668 C  CA  . GLU   J  10 167 ? 46.217  -144.666 -8.530  1.00 107.98 ? 167 GLU   J CA  1 
ATOM   17669 C  C   . GLU   J  10 167 ? 45.202  -144.711 -7.383  1.00 107.07 ? 167 GLU   J C   1 
ATOM   17670 O  O   . GLU   J  10 167 ? 44.944  -145.818 -6.876  1.00 107.51 ? 167 GLU   J O   1 
ATOM   17671 C  CB  . GLU   J  10 167 ? 47.583  -144.199 -8.021  1.00 107.64 ? 167 GLU   J CB  1 
ATOM   17672 C  CG  . GLU   J  10 167 ? 48.146  -145.052 -6.895  1.00 109.83 ? 167 GLU   J CG  1 
ATOM   17673 C  CD  . GLU   J  10 167 ? 48.350  -146.519 -7.237  1.00 112.85 ? 167 GLU   J CD  1 
ATOM   17674 O  OE1 . GLU   J  10 167 ? 48.540  -147.318 -6.301  1.00 117.67 ? 167 GLU   J OE1 1 
ATOM   17675 O  OE2 . GLU   J  10 167 ? 48.325  -146.860 -8.436  1.00 115.91 ? 167 GLU   J OE2 1 
ATOM   17676 N  N   . LEU   J  10 168 ? 44.663  -143.553 -6.986  1.00 105.61 ? 168 LEU   J N   1 
ATOM   17677 C  CA  . LEU   J  10 168 ? 43.660  -143.432 -5.893  1.00 105.98 ? 168 LEU   J CA  1 
ATOM   17678 C  C   . LEU   J  10 168 ? 42.360  -144.131 -6.314  1.00 105.41 ? 168 LEU   J C   1 
ATOM   17679 O  O   . LEU   J  10 168 ? 41.780  -144.839 -5.475  1.00 105.33 ? 168 LEU   J O   1 
ATOM   17680 C  CB  . LEU   J  10 168 ? 43.427  -141.951 -5.562  1.00 104.85 ? 168 LEU   J CB  1 
ATOM   17681 C  CG  . LEU   J  10 168 ? 44.614  -141.212 -4.940  1.00 104.78 ? 168 LEU   J CG  1 
ATOM   17682 C  CD1 . LEU   J  10 168 ? 44.370  -139.711 -4.923  1.00 103.99 ? 168 LEU   J CD1 1 
ATOM   17683 C  CD2 . LEU   J  10 168 ? 44.906  -141.712 -3.534  1.00 105.54 ? 168 LEU   J CD2 1 
ATOM   17684 N  N   . GLU   J  10 169 ? 41.937  -143.975 -7.572  1.00 106.11 ? 169 GLU   J N   1 
ATOM   17685 C  CA  . GLU   J  10 169 ? 40.683  -144.579 -8.101  1.00 110.19 ? 169 GLU   J CA  1 
ATOM   17686 C  C   . GLU   J  10 169 ? 40.826  -146.102 -8.208  1.00 109.01 ? 169 GLU   J C   1 
ATOM   17687 O  O   . GLU   J  10 169 ? 39.781  -146.770 -8.303  1.00 110.10 ? 169 GLU   J O   1 
ATOM   17688 C  CB  . GLU   J  10 169 ? 40.312  -143.979 -9.458  1.00 114.99 ? 169 GLU   J CB  1 
ATOM   17689 C  CG  . GLU   J  10 169 ? 39.588  -142.650 -9.342  1.00 116.74 ? 169 GLU   J CG  1 
ATOM   17690 C  CD  . GLU   J  10 169 ? 39.232  -141.987 -10.662 1.00 121.33 ? 169 GLU   J CD  1 
ATOM   17691 O  OE1 . GLU   J  10 169 ? 38.475  -140.994 -10.635 1.00 122.28 ? 169 GLU   J OE1 1 
ATOM   17692 O  OE2 . GLU   J  10 169 ? 39.713  -142.462 -11.713 1.00 126.00 ? 169 GLU   J OE2 1 
ATOM   17693 N  N   . LYS   J  10 170 ? 42.056  -146.628 -8.191  1.00 109.17 ? 170 LYS   J N   1 
ATOM   17694 C  CA  . LYS   J  10 170 ? 42.346  -148.084 -8.309  1.00 111.82 ? 170 LYS   J CA  1 
ATOM   17695 C  C   . LYS   J  10 170 ? 42.378  -148.736 -6.919  1.00 109.93 ? 170 LYS   J C   1 
ATOM   17696 O  O   . LYS   J  10 170 ? 41.782  -149.823 -6.775  1.00 111.44 ? 170 LYS   J O   1 
ATOM   17697 C  CB  . LYS   J  10 170 ? 43.665  -148.312 -9.056  1.00 113.25 ? 170 LYS   J CB  1 
ATOM   17698 C  CG  . LYS   J  10 170 ? 44.071  -149.773 -9.205  1.00 116.93 ? 170 LYS   J CG  1 
ATOM   17699 C  CD  . LYS   J  10 170 ? 45.128  -150.023 -10.261 1.00 118.65 ? 170 LYS   J CD  1 
ATOM   17700 C  CE  . LYS   J  10 170 ? 45.572  -151.470 -10.327 1.00 121.18 ? 170 LYS   J CE  1 
ATOM   17701 N  NZ  . LYS   J  10 170 ? 44.452  -152.379 -10.666 1.00 122.88 ? 170 LYS   J NZ  1 
ATOM   17702 N  N   . ARG   J  10 171 ? 43.036  -148.105 -5.939  1.00 109.49 ? 171 ARG   J N   1 
ATOM   17703 C  CA  . ARG   J  10 171 ? 43.446  -148.760 -4.665  1.00 109.43 ? 171 ARG   J CA  1 
ATOM   17704 C  C   . ARG   J  10 171 ? 42.668  -148.226 -3.454  1.00 109.81 ? 171 ARG   J C   1 
ATOM   17705 O  O   . ARG   J  10 171 ? 42.675  -148.927 -2.426  1.00 114.26 ? 171 ARG   J O   1 
ATOM   17706 C  CB  . ARG   J  10 171 ? 44.954  -148.587 -4.451  1.00 108.15 ? 171 ARG   J CB  1 
ATOM   17707 C  CG  . ARG   J  10 171 ? 45.813  -149.285 -5.495  1.00 108.31 ? 171 ARG   J CG  1 
ATOM   17708 C  CD  . ARG   J  10 171 ? 45.619  -150.789 -5.473  1.00 109.82 ? 171 ARG   J CD  1 
ATOM   17709 N  NE  . ARG   J  10 171 ? 46.504  -151.485 -6.393  1.00 111.55 ? 171 ARG   J NE  1 
ATOM   17710 C  CZ  . ARG   J  10 171 ? 46.515  -152.801 -6.587  1.00 114.40 ? 171 ARG   J CZ  1 
ATOM   17711 N  NH1 . ARG   J  10 171 ? 45.682  -153.582 -5.920  1.00 114.76 ? 171 ARG   J NH1 1 
ATOM   17712 N  NH2 . ARG   J  10 171 ? 47.364  -153.333 -7.449  1.00 115.87 ? 171 ARG   J NH2 1 
ATOM   17713 N  N   . MET   J  10 172 ? 42.037  -147.049 -3.541  1.00 109.82 ? 172 MET   J N   1 
ATOM   17714 C  CA  . MET   J  10 172 ? 41.280  -146.456 -2.403  1.00 110.12 ? 172 MET   J CA  1 
ATOM   17715 C  C   . MET   J  10 172 ? 39.955  -147.196 -2.231  1.00 105.73 ? 172 MET   J C   1 
ATOM   17716 O  O   . MET   J  10 172 ? 39.291  -147.508 -3.215  1.00 100.63 ? 172 MET   J O   1 
ATOM   17717 C  CB  . MET   J  10 172 ? 41.011  -144.964 -2.613  1.00 110.26 ? 172 MET   J CB  1 
ATOM   17718 C  CG  . MET   J  10 172 ? 42.198  -144.097 -2.266  1.00 114.80 ? 172 MET   J CG  1 
ATOM   17719 S  SD  . MET   J  10 172 ? 42.177  -143.666 -0.513  1.00 122.61 ? 172 MET   J SD  1 
ATOM   17720 C  CE  . MET   J  10 172 ? 43.900  -143.257 -0.239  1.00 124.12 ? 172 MET   J CE  1 
ATOM   17721 N  N   . PRO   J  10 173 ? 39.530  -147.495 -0.981  1.00 108.81 ? 173 PRO   J N   1 
ATOM   17722 C  CA  . PRO   J  10 173 ? 38.284  -148.225 -0.738  1.00 111.47 ? 173 PRO   J CA  1 
ATOM   17723 C  C   . PRO   J  10 173 ? 37.012  -147.472 -1.161  1.00 113.55 ? 173 PRO   J C   1 
ATOM   17724 O  O   . PRO   J  10 173 ? 36.086  -148.124 -1.599  1.00 111.92 ? 173 PRO   J O   1 
ATOM   17725 C  CB  . PRO   J  10 173 ? 38.256  -148.428 0.788   1.00 113.21 ? 173 PRO   J CB  1 
ATOM   17726 C  CG  . PRO   J  10 173 ? 39.684  -148.194 1.237   1.00 113.32 ? 173 PRO   J CG  1 
ATOM   17727 C  CD  . PRO   J  10 173 ? 40.227  -147.161 0.272   1.00 111.21 ? 173 PRO   J CD  1 
ATOM   17728 N  N   . MET   J  10 174 ? 36.990  -146.140 -1.013  1.00 115.80 ? 174 MET   J N   1 
ATOM   17729 C  CA  . MET   J  10 174 ? 35.764  -145.304 -1.157  1.00 118.06 ? 174 MET   J CA  1 
ATOM   17730 C  C   . MET   J  10 174 ? 35.731  -144.615 -2.531  1.00 113.10 ? 174 MET   J C   1 
ATOM   17731 O  O   . MET   J  10 174 ? 36.813  -144.310 -3.080  1.00 106.06 ? 174 MET   J O   1 
ATOM   17732 C  CB  . MET   J  10 174 ? 35.662  -144.262 -0.034  1.00 121.09 ? 174 MET   J CB  1 
ATOM   17733 C  CG  . MET   J  10 174 ? 36.528  -143.024 -0.222  1.00 126.90 ? 174 MET   J CG  1 
ATOM   17734 S  SD  . MET   J  10 174 ? 38.307  -143.367 -0.291  1.00 136.87 ? 174 MET   J SD  1 
ATOM   17735 C  CE  . MET   J  10 174 ? 38.943  -141.710 -0.539  1.00 135.01 ? 174 MET   J CE  1 
ATOM   17736 N  N   . ASP   J  10 175 ? 34.521  -144.397 -3.059  1.00 108.60 ? 175 ASP   J N   1 
ATOM   17737 C  CA  . ASP   J  10 175 ? 34.253  -143.641 -4.312  1.00 106.67 ? 175 ASP   J CA  1 
ATOM   17738 C  C   . ASP   J  10 175 ? 34.169  -142.148 -3.973  1.00 102.01 ? 175 ASP   J C   1 
ATOM   17739 O  O   . ASP   J  10 175 ? 33.186  -141.740 -3.320  1.00 96.76  ? 175 ASP   J O   1 
ATOM   17740 C  CB  . ASP   J  10 175 ? 32.970  -144.129 -4.992  1.00 108.60 ? 175 ASP   J CB  1 
ATOM   17741 C  CG  . ASP   J  10 175 ? 32.820  -143.670 -6.434  1.00 108.97 ? 175 ASP   J CG  1 
ATOM   17742 O  OD1 . ASP   J  10 175 ? 33.383  -142.612 -6.781  1.00 105.47 ? 175 ASP   J OD1 1 
ATOM   17743 O  OD2 . ASP   J  10 175 ? 32.140  -144.378 -7.201  1.00 112.74 ? 175 ASP   J OD2 1 
ATOM   17744 N  N   . PHE   J  10 176 ? 35.161  -141.369 -4.410  1.00 99.09  ? 176 PHE   J N   1 
ATOM   17745 C  CA  . PHE   J  10 176 ? 35.305  -139.924 -4.093  1.00 97.90  ? 176 PHE   J CA  1 
ATOM   17746 C  C   . PHE   J  10 176 ? 34.840  -139.069 -5.282  1.00 97.67  ? 176 PHE   J C   1 
ATOM   17747 O  O   . PHE   J  10 176 ? 35.013  -137.836 -5.232  1.00 97.08  ? 176 PHE   J O   1 
ATOM   17748 C  CB  . PHE   J  10 176 ? 36.742  -139.618 -3.664  1.00 97.44  ? 176 PHE   J CB  1 
ATOM   17749 C  CG  . PHE   J  10 176 ? 37.792  -139.859 -4.718  1.00 99.21  ? 176 PHE   J CG  1 
ATOM   17750 C  CD1 . PHE   J  10 176 ? 38.139  -138.861 -5.614  1.00 99.08  ? 176 PHE   J CD1 1 
ATOM   17751 C  CD2 . PHE   J  10 176 ? 38.448  -141.077 -4.802  1.00 102.03 ? 176 PHE   J CD2 1 
ATOM   17752 C  CE1 . PHE   J  10 176 ? 39.111  -139.081 -6.577  1.00 100.16 ? 176 PHE   J CE1 1 
ATOM   17753 C  CE2 . PHE   J  10 176 ? 39.421  -141.295 -5.766  1.00 103.28 ? 176 PHE   J CE2 1 
ATOM   17754 C  CZ  . PHE   J  10 176 ? 39.751  -140.296 -6.651  1.00 101.81 ? 176 PHE   J CZ  1 
ATOM   17755 N  N   . LYS   J  10 177 ? 34.266  -139.704 -6.311  1.00 99.44  ? 177 LYS   J N   1 
ATOM   17756 C  CA  . LYS   J  10 177 ? 33.510  -139.055 -7.420  1.00 99.59  ? 177 LYS   J CA  1 
ATOM   17757 C  C   . LYS   J  10 177 ? 34.392  -138.062 -8.193  1.00 98.43  ? 177 LYS   J C   1 
ATOM   17758 O  O   . LYS   J  10 177 ? 33.847  -137.053 -8.677  1.00 97.17  ? 177 LYS   J O   1 
ATOM   17759 C  CB  . LYS   J  10 177 ? 32.265  -138.352 -6.867  1.00 98.81  ? 177 LYS   J CB  1 
ATOM   17760 C  CG  . LYS   J  10 177 ? 31.279  -139.246 -6.126  1.00 101.21 ? 177 LYS   J CG  1 
ATOM   17761 C  CD  . LYS   J  10 177 ? 30.674  -140.335 -6.987  1.00 105.62 ? 177 LYS   J CD  1 
ATOM   17762 C  CE  . LYS   J  10 177 ? 29.707  -141.219 -6.228  1.00 108.35 ? 177 LYS   J CE  1 
ATOM   17763 N  NZ  . LYS   J  10 177 ? 29.444  -142.490 -6.945  1.00 111.10 ? 177 LYS   J NZ  1 
ATOM   17764 N  N   . GLY   J  10 178 ? 35.691  -138.346 -8.337  1.00 99.73  ? 178 GLY   J N   1 
ATOM   17765 C  CA  . GLY   J  10 178 ? 36.634  -137.506 -9.105  1.00 100.85 ? 178 GLY   J CA  1 
ATOM   17766 C  C   . GLY   J  10 178 ? 37.004  -136.231 -8.362  1.00 98.19  ? 178 GLY   J C   1 
ATOM   17767 O  O   . GLY   J  10 178 ? 36.574  -136.081 -7.204  1.00 99.57  ? 178 GLY   J O   1 
ATOM   17768 N  N   . VAL   J  10 179 ? 37.758  -135.334 -9.009  1.00 99.32  ? 179 VAL   J N   1 
ATOM   17769 C  CA  . VAL   J  10 179 ? 38.359  -134.120 -8.372  1.00 97.73  ? 179 VAL   J CA  1 
ATOM   17770 C  C   . VAL   J  10 179 ? 38.030  -132.863 -9.190  1.00 96.50  ? 179 VAL   J C   1 
ATOM   17771 O  O   . VAL   J  10 179 ? 37.818  -132.981 -10.413 1.00 93.92  ? 179 VAL   J O   1 
ATOM   17772 C  CB  . VAL   J  10 179 ? 39.884  -134.273 -8.196  1.00 99.08  ? 179 VAL   J CB  1 
ATOM   17773 C  CG1 . VAL   J  10 179 ? 40.226  -135.350 -7.179  1.00 98.77  ? 179 VAL   J CG1 1 
ATOM   17774 C  CG2 . VAL   J  10 179 ? 40.599  -134.535 -9.515  1.00 100.32 ? 179 VAL   J CG2 1 
ATOM   17775 N  N   . ILE   J  10 180 ? 37.998  -131.706 -8.519  1.00 92.94  ? 180 ILE   J N   1 
ATOM   17776 C  CA  . ILE   J  10 180 ? 38.013  -130.347 -9.138  1.00 93.65  ? 180 ILE   J CA  1 
ATOM   17777 C  C   . ILE   J  10 180 ? 39.451  -129.829 -9.071  1.00 94.43  ? 180 ILE   J C   1 
ATOM   17778 O  O   . ILE   J  10 180 ? 39.976  -129.697 -7.946  1.00 96.60  ? 180 ILE   J O   1 
ATOM   17779 C  CB  . ILE   J  10 180 ? 37.024  -129.391 -8.439  1.00 93.67  ? 180 ILE   J CB  1 
ATOM   17780 C  CG1 . ILE   J  10 180 ? 35.583  -129.685 -8.860  1.00 92.71  ? 180 ILE   J CG1 1 
ATOM   17781 C  CG2 . ILE   J  10 180 ? 37.397  -127.938 -8.700  1.00 95.01  ? 180 ILE   J CG2 1 
ATOM   17782 C  CD1 . ILE   J  10 180 ? 34.529  -129.019 -8.008  1.00 91.60  ? 180 ILE   J CD1 1 
ATOM   17783 N  N   . VAL   J  10 181 ? 40.049  -129.543 -10.231 1.00 95.26  ? 181 VAL   J N   1 
ATOM   17784 C  CA  . VAL   J  10 181 ? 41.464  -129.087 -10.363 1.00 99.32  ? 181 VAL   J CA  1 
ATOM   17785 C  C   . VAL   J  10 181 ? 41.466  -127.578 -10.625 1.00 99.36  ? 181 VAL   J C   1 
ATOM   17786 O  O   . VAL   J  10 181 ? 40.709  -127.130 -11.507 1.00 103.61 ? 181 VAL   J O   1 
ATOM   17787 C  CB  . VAL   J  10 181 ? 42.201  -129.855 -11.476 1.00 102.52 ? 181 VAL   J CB  1 
ATOM   17788 C  CG1 . VAL   J  10 181 ? 43.628  -129.359 -11.664 1.00 102.41 ? 181 VAL   J CG1 1 
ATOM   17789 C  CG2 . VAL   J  10 181 ? 42.186  -131.352 -11.216 1.00 104.74 ? 181 VAL   J CG2 1 
ATOM   17790 N  N   . LYS   J  10 182 ? 42.295  -126.838 -9.884  1.00 100.57 ? 182 LYS   J N   1 
ATOM   17791 C  CA  . LYS   J  10 182 ? 42.459  -125.366 -10.018 1.00 101.17 ? 182 LYS   J CA  1 
ATOM   17792 C  C   . LYS   J  10 182 ? 43.952  -125.035 -10.076 1.00 103.70 ? 182 LYS   J C   1 
ATOM   17793 O  O   . LYS   J  10 182 ? 44.733  -125.694 -9.358  1.00 104.59 ? 182 LYS   J O   1 
ATOM   17794 C  CB  . LYS   J  10 182 ? 41.767  -124.647 -8.857  1.00 98.79  ? 182 LYS   J CB  1 
ATOM   17795 C  CG  . LYS   J  10 182 ? 40.302  -125.011 -8.676  1.00 98.45  ? 182 LYS   J CG  1 
ATOM   17796 C  CD  . LYS   J  10 182 ? 39.508  -123.969 -7.931  1.00 97.29  ? 182 LYS   J CD  1 
ATOM   17797 C  CE  . LYS   J  10 182 ? 38.027  -124.280 -7.914  1.00 99.49  ? 182 LYS   J CE  1 
ATOM   17798 N  NZ  . LYS   J  10 182 ? 37.227  -123.117 -7.464  1.00 101.23 ? 182 LYS   J NZ  1 
ATOM   17799 N  N   . ILE   J  10 183 ? 44.317  -124.050 -10.904 1.00 103.73 ? 183 ILE   J N   1 
ATOM   17800 C  CA  . ILE   J  10 183 ? 45.725  -123.616 -11.145 1.00 104.30 ? 183 ILE   J CA  1 
ATOM   17801 C  C   . ILE   J  10 183 ? 45.896  -122.194 -10.601 1.00 106.63 ? 183 ILE   J C   1 
ATOM   17802 O  O   . ILE   J  10 183 ? 45.060  -121.328 -10.930 1.00 111.14 ? 183 ILE   J O   1 
ATOM   17803 C  CB  . ILE   J  10 183 ? 46.086  -123.699 -12.641 1.00 103.84 ? 183 ILE   J CB  1 
ATOM   17804 C  CG1 . ILE   J  10 183 ? 45.729  -125.063 -13.237 1.00 104.53 ? 183 ILE   J CG1 1 
ATOM   17805 C  CG2 . ILE   J  10 183 ? 47.554  -123.357 -12.858 1.00 102.83 ? 183 ILE   J CG2 1 
ATOM   17806 C  CD1 . ILE   J  10 183 ? 45.657  -125.074 -14.743 1.00 106.76 ? 183 ILE   J CD1 1 
ATOM   17807 N  N   . VAL   J  10 184 ? 46.948  -121.982 -9.805  1.00 108.35 ? 184 VAL   J N   1 
ATOM   17808 C  CA  . VAL   J  10 184 ? 47.364  -120.658 -9.258  1.00 109.08 ? 184 VAL   J CA  1 
ATOM   17809 C  C   . VAL   J  10 184 ? 48.693  -120.280 -9.923  1.00 107.67 ? 184 VAL   J C   1 
ATOM   17810 O  O   . VAL   J  10 184 ? 49.659  -121.053 -9.784  1.00 106.94 ? 184 VAL   J O   1 
ATOM   17811 C  CB  . VAL   J  10 184 ? 47.494  -120.702 -7.722  1.00 106.99 ? 184 VAL   J CB  1 
ATOM   17812 C  CG1 . VAL   J  10 184 ? 47.713  -119.314 -7.136  1.00 106.56 ? 184 VAL   J CG1 1 
ATOM   17813 C  CG2 . VAL   J  10 184 ? 46.298  -121.379 -7.066  1.00 105.93 ? 184 VAL   J CG2 1 
ATOM   17814 N  N   . ASP   J  10 185 ? 48.732  -119.147 -10.630 1.00 109.84 ? 185 ASP   J N   1 
ATOM   17815 C  CA  . ASP   J  10 185 ? 49.944  -118.650 -11.337 1.00 113.10 ? 185 ASP   J CA  1 
ATOM   17816 C  C   . ASP   J  10 185 ? 49.961  -117.115 -11.306 1.00 115.80 ? 185 ASP   J C   1 
ATOM   17817 O  O   . ASP   J  10 185 ? 49.186  -116.524 -10.522 1.00 116.04 ? 185 ASP   J O   1 
ATOM   17818 C  CB  . ASP   J  10 185 ? 50.014  -119.219 -12.758 1.00 114.63 ? 185 ASP   J CB  1 
ATOM   17819 C  CG  . ASP   J  10 185 ? 48.840  -118.842 -13.648 1.00 114.41 ? 185 ASP   J CG  1 
ATOM   17820 O  OD1 . ASP   J  10 185 ? 48.190  -117.816 -13.371 1.00 109.80 ? 185 ASP   J OD1 1 
ATOM   17821 O  OD2 . ASP   J  10 185 ? 48.584  -119.585 -14.614 1.00 116.58 ? 185 ASP   J OD2 1 
ATOM   17822 N  N   . LYS   J  10 186 ? 50.824  -116.502 -12.125 1.00 116.86 ? 186 LYS   J N   1 
ATOM   17823 C  CA  . LYS   J  10 186 ? 51.020  -115.030 -12.216 1.00 113.21 ? 186 LYS   J CA  1 
ATOM   17824 C  C   . LYS   J  10 186 ? 49.709  -114.330 -12.601 1.00 109.82 ? 186 LYS   J C   1 
ATOM   17825 O  O   . LYS   J  10 186 ? 49.539  -113.165 -12.197 1.00 108.36 ? 186 LYS   J O   1 
ATOM   17826 C  CB  . LYS   J  10 186 ? 52.138  -114.700 -13.211 1.00 117.43 ? 186 LYS   J CB  1 
ATOM   17827 C  CG  . LYS   J  10 186 ? 51.915  -115.170 -14.643 1.00 122.81 ? 186 LYS   J CG  1 
ATOM   17828 C  CD  . LYS   J  10 186 ? 53.085  -114.860 -15.551 1.00 128.10 ? 186 LYS   J CD  1 
ATOM   17829 C  CE  . LYS   J  10 186 ? 52.987  -115.531 -16.904 1.00 133.63 ? 186 LYS   J CE  1 
ATOM   17830 N  NZ  . LYS   J  10 186 ? 51.907  -114.944 -17.731 1.00 138.27 ? 186 LYS   J NZ  1 
ATOM   17831 N  N   . ASP   J  10 187 ? 48.820  -115.007 -13.337 1.00 105.74 ? 187 ASP   J N   1 
ATOM   17832 C  CA  . ASP   J  10 187 ? 47.548  -114.432 -13.854 1.00 103.58 ? 187 ASP   J CA  1 
ATOM   17833 C  C   . ASP   J  10 187 ? 46.377  -114.753 -12.914 1.00 97.45  ? 187 ASP   J C   1 
ATOM   17834 O  O   . ASP   J  10 187 ? 45.235  -114.425 -13.285 1.00 95.91  ? 187 ASP   J O   1 
ATOM   17835 C  CB  . ASP   J  10 187 ? 47.256  -114.934 -15.268 1.00 106.87 ? 187 ASP   J CB  1 
ATOM   17836 C  CG  . ASP   J  10 187 ? 48.347  -114.582 -16.263 1.00 111.38 ? 187 ASP   J CG  1 
ATOM   17837 O  OD1 . ASP   J  10 187 ? 48.721  -113.395 -16.327 1.00 112.00 ? 187 ASP   J OD1 1 
ATOM   17838 O  OD2 . ASP   J  10 187 ? 48.824  -115.500 -16.951 1.00 118.50 ? 187 ASP   J OD2 1 
ATOM   17839 N  N   . GLY   J  10 188 ? 46.640  -115.367 -11.756 1.00 94.94  ? 188 GLY   J N   1 
ATOM   17840 C  CA  . GLY   J  10 188 ? 45.628  -115.616 -10.711 1.00 95.51  ? 188 GLY   J CA  1 
ATOM   17841 C  C   . GLY   J  10 188 ? 45.147  -117.056 -10.705 1.00 97.43  ? 188 GLY   J C   1 
ATOM   17842 O  O   . GLY   J  10 188 ? 45.969  -117.955 -10.978 1.00 100.56 ? 188 GLY   J O   1 
ATOM   17843 N  N   . ILE   J  10 189 ? 43.858  -117.263 -10.411 1.00 98.29  ? 189 ILE   J N   1 
ATOM   17844 C  CA  . ILE   J  10 189 ? 43.231  -118.597 -10.163 1.00 100.48 ? 189 ILE   J CA  1 
ATOM   17845 C  C   . ILE   J  10 189 ? 42.225  -118.894 -11.280 1.00 103.14 ? 189 ILE   J C   1 
ATOM   17846 O  O   . ILE   J  10 189 ? 41.365  -118.032 -11.541 1.00 106.18 ? 189 ILE   J O   1 
ATOM   17847 C  CB  . ILE   J  10 189 ? 42.563  -118.626 -8.772  1.00 98.44  ? 189 ILE   J CB  1 
ATOM   17848 C  CG1 . ILE   J  10 189 ? 43.595  -118.461 -7.654  1.00 97.24  ? 189 ILE   J CG1 1 
ATOM   17849 C  CG2 . ILE   J  10 189 ? 41.732  -119.887 -8.582  1.00 97.33  ? 189 ILE   J CG2 1 
ATOM   17850 C  CD1 . ILE   J  10 189 ? 43.043  -117.839 -6.396  1.00 95.24  ? 189 ILE   J CD1 1 
ATOM   17851 N  N   . ARG   J  10 190 ? 42.326  -120.076 -11.897 1.00 105.35 ? 190 ARG   J N   1 
ATOM   17852 C  CA  . ARG   J  10 190 ? 41.366  -120.569 -12.921 1.00 106.12 ? 190 ARG   J CA  1 
ATOM   17853 C  C   . ARG   J  10 190 ? 41.125  -122.066 -12.706 1.00 107.30 ? 190 ARG   J C   1 
ATOM   17854 O  O   . ARG   J  10 190 ? 42.047  -122.747 -12.214 1.00 108.68 ? 190 ARG   J O   1 
ATOM   17855 C  CB  . ARG   J  10 190 ? 41.887  -120.279 -14.331 1.00 107.04 ? 190 ARG   J CB  1 
ATOM   17856 C  CG  . ARG   J  10 190 ? 43.076  -121.129 -14.754 1.00 108.39 ? 190 ARG   J CG  1 
ATOM   17857 C  CD  . ARG   J  10 190 ? 43.490  -120.807 -16.174 1.00 113.05 ? 190 ARG   J CD  1 
ATOM   17858 N  NE  . ARG   J  10 190 ? 44.525  -121.709 -16.660 1.00 116.29 ? 190 ARG   J NE  1 
ATOM   17859 C  CZ  . ARG   J  10 190 ? 45.822  -121.623 -16.366 1.00 116.17 ? 190 ARG   J CZ  1 
ATOM   17860 N  NH1 . ARG   J  10 190 ? 46.275  -120.669 -15.569 1.00 116.25 ? 190 ARG   J NH1 1 
ATOM   17861 N  NH2 . ARG   J  10 190 ? 46.667  -122.504 -16.873 1.00 119.02 ? 190 ARG   J NH2 1 
ATOM   17862 N  N   . GLN   J  10 191 ? 39.931  -122.542 -13.073 1.00 109.41 ? 191 GLN   J N   1 
ATOM   17863 C  CA  . GLN   J  10 191 ? 39.468  -123.940 -12.857 1.00 109.73 ? 191 GLN   J CA  1 
ATOM   17864 C  C   . GLN   J  10 191 ? 39.524  -124.715 -14.177 1.00 112.60 ? 191 GLN   J C   1 
ATOM   17865 O  O   . GLN   J  10 191 ? 39.007  -124.202 -15.187 1.00 115.78 ? 191 GLN   J O   1 
ATOM   17866 C  CB  . GLN   J  10 191 ? 38.041  -123.943 -12.305 1.00 107.35 ? 191 GLN   J CB  1 
ATOM   17867 C  CG  . GLN   J  10 191 ? 37.535  -125.331 -11.939 1.00 105.32 ? 191 GLN   J CG  1 
ATOM   17868 C  CD  . GLN   J  10 191 ? 36.088  -125.351 -11.505 1.00 105.58 ? 191 GLN   J CD  1 
ATOM   17869 O  OE1 . GLN   J  10 191 ? 35.334  -126.250 -11.866 1.00 105.95 ? 191 GLN   J OE1 1 
ATOM   17870 N  NE2 . GLN   J  10 191 ? 35.684  -124.368 -10.715 1.00 105.75 ? 191 GLN   J NE2 1 
ATOM   17871 N  N   . VAL   J  10 192 ? 40.114  -125.914 -14.153 1.00 112.72 ? 192 VAL   J N   1 
ATOM   17872 C  CA  . VAL   J  10 192 ? 40.064  -126.905 -15.270 1.00 116.13 ? 192 VAL   J CA  1 
ATOM   17873 C  C   . VAL   J  10 192 ? 38.697  -127.598 -15.213 1.00 122.25 ? 192 VAL   J C   1 
ATOM   17874 O  O   . VAL   J  10 192 ? 38.408  -128.240 -14.181 1.00 118.13 ? 192 VAL   J O   1 
ATOM   17875 C  CB  . VAL   J  10 192 ? 41.212  -127.928 -15.182 1.00 112.55 ? 192 VAL   J CB  1 
ATOM   17876 C  CG1 . VAL   J  10 192 ? 41.144  -128.946 -16.310 1.00 113.97 ? 192 VAL   J CG1 1 
ATOM   17877 C  CG2 . VAL   J  10 192 ? 42.575  -127.254 -15.155 1.00 110.86 ? 192 VAL   J CG2 1 
ATOM   17878 N  N   . ASP   J  10 193 ? 37.900  -127.479 -16.281 1.00 132.52 ? 193 ASP   J N   1 
ATOM   17879 C  CA  . ASP   J  10 193 ? 36.483  -127.938 -16.330 1.00 137.90 ? 193 ASP   J CA  1 
ATOM   17880 C  C   . ASP   J  10 193 ? 36.405  -129.400 -16.797 1.00 138.14 ? 193 ASP   J C   1 
ATOM   17881 O  O   . ASP   J  10 193 ? 35.417  -130.070 -16.436 1.00 145.23 ? 193 ASP   J O   1 
ATOM   17882 C  CB  . ASP   J  10 193 ? 35.615  -127.017 -17.198 1.00 142.10 ? 193 ASP   J CB  1 
ATOM   17883 C  CG  . ASP   J  10 193 ? 36.207  -126.641 -18.548 1.00 141.60 ? 193 ASP   J CG  1 
ATOM   17884 O  OD1 . ASP   J  10 193 ? 37.216  -127.258 -18.945 1.00 150.06 ? 193 ASP   J OD1 1 
ATOM   17885 O  OD2 . ASP   J  10 193 ? 35.656  -125.726 -19.193 1.00 141.20 ? 193 ASP   J OD2 1 
ATOM   17886 N  N   . ASP   J  10 194 ? 37.397  -129.879 -17.556 1.00 138.25 ? 194 ASP   J N   1 
ATOM   17887 C  CA  . ASP   J  10 194 ? 37.416  -131.254 -18.128 1.00 140.28 ? 194 ASP   J CA  1 
ATOM   17888 C  C   . ASP   J  10 194 ? 38.560  -132.052 -17.491 1.00 136.75 ? 194 ASP   J C   1 
ATOM   17889 O  O   . ASP   J  10 194 ? 39.685  -132.013 -18.028 1.00 144.17 ? 194 ASP   J O   1 
ATOM   17890 C  CB  . ASP   J  10 194 ? 37.500  -131.225 -19.659 1.00 142.79 ? 194 ASP   J CB  1 
ATOM   17891 C  CG  . ASP   J  10 194 ? 38.434  -130.167 -20.226 1.00 146.01 ? 194 ASP   J CG  1 
ATOM   17892 O  OD1 . ASP   J  10 194 ? 39.456  -129.870 -19.573 1.00 136.20 ? 194 ASP   J OD1 1 
ATOM   17893 O  OD2 . ASP   J  10 194 ? 38.125  -129.641 -21.313 1.00 151.83 ? 194 ASP   J OD2 1 
ATOM   17894 N  N   . PHE   J  10 195 ? 38.279  -132.748 -16.385 1.00 128.93 ? 195 PHE   J N   1 
ATOM   17895 C  CA  . PHE   J  10 195 ? 39.229  -133.669 -15.706 1.00 126.42 ? 195 PHE   J CA  1 
ATOM   17896 C  C   . PHE   J  10 195 ? 38.519  -134.986 -15.364 1.00 125.86 ? 195 PHE   J C   1 
ATOM   17897 O  O   . PHE   J  10 195 ? 38.750  -136.016 -16.004 1.00 119.12 ? 195 PHE   J O   1 
ATOM   17898 C  CB  . PHE   J  10 195 ? 39.829  -133.003 -14.465 1.00 125.96 ? 195 PHE   J CB  1 
ATOM   17899 C  CG  . PHE   J  10 195 ? 41.205  -133.507 -14.109 1.00 126.05 ? 195 PHE   J CG  1 
ATOM   17900 C  CD1 . PHE   J  10 195 ? 41.369  -134.613 -13.287 1.00 124.49 ? 195 PHE   J CD1 1 
ATOM   17901 C  CD2 . PHE   J  10 195 ? 42.338  -132.888 -14.616 1.00 123.62 ? 195 PHE   J CD2 1 
ATOM   17902 C  CE1 . PHE   J  10 195 ? 42.636  -135.078 -12.970 1.00 121.80 ? 195 PHE   J CE1 1 
ATOM   17903 C  CE2 . PHE   J  10 195 ? 43.604  -133.355 -14.298 1.00 122.38 ? 195 PHE   J CE2 1 
ATOM   17904 C  CZ  . PHE   J  10 195 ? 43.751  -134.448 -13.475 1.00 122.03 ? 195 PHE   J CZ  1 
ATOM   17905 N  N   . THR   K  11 1   ? 11.159  -140.071 6.202   1.00 96.28  ? 2   THR   K N   1 
ATOM   17906 C  CA  . THR   K  11 1   ? 11.614  -139.928 4.799   1.00 95.78  ? 2   THR   K CA  1 
ATOM   17907 C  C   . THR   K  11 1   ? 11.134  -138.582 4.252   1.00 95.46  ? 2   THR   K C   1 
ATOM   17908 O  O   . THR   K  11 1   ? 9.916   -138.331 4.286   1.00 91.60  ? 2   THR   K O   1 
ATOM   17909 C  CB  . THR   K  11 1   ? 11.183  -141.112 3.929   1.00 95.61  ? 2   THR   K CB  1 
ATOM   17910 O  OG1 . THR   K  11 1   ? 11.546  -142.317 4.600   1.00 94.25  ? 2   THR   K OG1 1 
ATOM   17911 C  CG2 . THR   K  11 1   ? 11.844  -141.092 2.571   1.00 94.52  ? 2   THR   K CG2 1 
ATOM   17912 N  N   . THR   K  11 2   ? 12.091  -137.756 3.820   1.00 95.79  ? 3   THR   K N   1 
ATOM   17913 C  CA  . THR   K  11 2   ? 11.862  -136.410 3.216   1.00 96.18  ? 3   THR   K CA  1 
ATOM   17914 C  C   . THR   K  11 2   ? 12.748  -136.250 1.977   1.00 94.42  ? 3   THR   K C   1 
ATOM   17915 O  O   . THR   K  11 2   ? 13.905  -136.711 2.020   1.00 95.14  ? 3   THR   K O   1 
ATOM   17916 C  CB  . THR   K  11 2   ? 12.180  -135.261 4.185   1.00 92.63  ? 3   THR   K CB  1 
ATOM   17917 O  OG1 . THR   K  11 2   ? 13.595  -135.169 4.367   1.00 93.04  ? 3   THR   K OG1 1 
ATOM   17918 C  CG2 . THR   K  11 2   ? 11.513  -135.414 5.533   1.00 92.03  ? 3   THR   K CG2 1 
ATOM   17919 N  N   . LEU   K  11 3   ? 12.239  -135.599 0.929   1.00 94.07  ? 4   LEU   K N   1 
ATOM   17920 C  CA  . LEU   K  11 3   ? 13.050  -135.227 -0.260  1.00 99.02  ? 4   LEU   K CA  1 
ATOM   17921 C  C   . LEU   K  11 3   ? 12.505  -133.947 -0.896  1.00 96.71  ? 4   LEU   K C   1 
ATOM   17922 O  O   . LEU   K  11 3   ? 11.347  -133.574 -0.627  1.00 95.96  ? 4   LEU   K O   1 
ATOM   17923 C  CB  . LEU   K  11 3   ? 13.125  -136.386 -1.266  1.00 102.79 ? 4   LEU   K CB  1 
ATOM   17924 C  CG  . LEU   K  11 3   ? 11.845  -136.852 -1.971  1.00 107.03 ? 4   LEU   K CG  1 
ATOM   17925 C  CD1 . LEU   K  11 3   ? 10.864  -137.471 -0.998  1.00 108.84 ? 4   LEU   K CD1 1 
ATOM   17926 C  CD2 . LEU   K  11 3   ? 11.168  -135.755 -2.781  1.00 107.98 ? 4   LEU   K CD2 1 
ATOM   17927 N  N   . ALA   K  11 4   ? 13.359  -133.295 -1.681  1.00 96.05  ? 5   ALA   K N   1 
ATOM   17928 C  CA  . ALA   K  11 4   ? 13.046  -132.119 -2.519  1.00 97.67  ? 5   ALA   K CA  1 
ATOM   17929 C  C   . ALA   K  11 4   ? 13.986  -132.143 -3.722  1.00 98.06  ? 5   ALA   K C   1 
ATOM   17930 O  O   . ALA   K  11 4   ? 15.153  -132.553 -3.554  1.00 98.84  ? 5   ALA   K O   1 
ATOM   17931 C  CB  . ALA   K  11 4   ? 13.199  -130.852 -1.719  1.00 97.69  ? 5   ALA   K CB  1 
ATOM   17932 N  N   . PHE   K  11 5   ? 13.493  -131.746 -4.893  1.00 99.39  ? 6   PHE   K N   1 
ATOM   17933 C  CA  . PHE   K  11 5   ? 14.298  -131.713 -6.137  1.00 103.57 ? 6   PHE   K CA  1 
ATOM   17934 C  C   . PHE   K  11 5   ? 13.870  -130.529 -7.006  1.00 104.67 ? 6   PHE   K C   1 
ATOM   17935 O  O   . PHE   K  11 5   ? 12.738  -130.025 -6.861  1.00 104.45 ? 6   PHE   K O   1 
ATOM   17936 C  CB  . PHE   K  11 5   ? 14.201  -133.047 -6.883  1.00 103.30 ? 6   PHE   K CB  1 
ATOM   17937 C  CG  . PHE   K  11 5   ? 12.833  -133.383 -7.421  1.00 105.96 ? 6   PHE   K CG  1 
ATOM   17938 C  CD1 . PHE   K  11 5   ? 12.310  -132.701 -8.509  1.00 110.63 ? 6   PHE   K CD1 1 
ATOM   17939 C  CD2 . PHE   K  11 5   ? 12.075  -134.394 -6.851  1.00 104.02 ? 6   PHE   K CD2 1 
ATOM   17940 C  CE1 . PHE   K  11 5   ? 11.055  -133.013 -9.007  1.00 113.08 ? 6   PHE   K CE1 1 
ATOM   17941 C  CE2 . PHE   K  11 5   ? 10.821  -134.708 -7.352  1.00 106.27 ? 6   PHE   K CE2 1 
ATOM   17942 C  CZ  . PHE   K  11 5   ? 10.315  -134.018 -8.429  1.00 110.49 ? 6   PHE   K CZ  1 
ATOM   17943 N  N   . ARG   K  11 6   ? 14.776  -130.131 -7.900  1.00 108.93 ? 7   ARG   K N   1 
ATOM   17944 C  CA  . ARG   K  11 6   ? 14.640  -128.986 -8.833  1.00 113.23 ? 7   ARG   K CA  1 
ATOM   17945 C  C   . ARG   K  11 6   ? 14.399  -129.516 -10.247 1.00 116.31 ? 7   ARG   K C   1 
ATOM   17946 O  O   . ARG   K  11 6   ? 14.965  -130.577 -10.587 1.00 113.99 ? 7   ARG   K O   1 
ATOM   17947 C  CB  . ARG   K  11 6   ? 15.926  -128.160 -8.827  1.00 112.59 ? 7   ARG   K CB  1 
ATOM   17948 C  CG  . ARG   K  11 6   ? 15.802  -126.770 -8.223  1.00 113.39 ? 7   ARG   K CG  1 
ATOM   17949 C  CD  . ARG   K  11 6   ? 17.191  -126.174 -8.094  1.00 112.45 ? 7   ARG   K CD  1 
ATOM   17950 N  NE  . ARG   K  11 6   ? 17.926  -126.261 -9.354  1.00 115.45 ? 7   ARG   K NE  1 
ATOM   17951 C  CZ  . ARG   K  11 6   ? 18.299  -125.233 -10.113 1.00 117.19 ? 7   ARG   K CZ  1 
ATOM   17952 N  NH1 . ARG   K  11 6   ? 18.038  -123.988 -9.749  1.00 117.52 ? 7   ARG   K NH1 1 
ATOM   17953 N  NH2 . ARG   K  11 6   ? 18.953  -125.454 -11.239 1.00 120.93 ? 7   ARG   K NH2 1 
ATOM   17954 N  N   . PHE   K  11 7   ? 13.613  -128.787 -11.041 1.00 120.10 ? 8   PHE   K N   1 
ATOM   17955 C  CA  . PHE   K  11 7   ? 13.349  -129.096 -12.469 1.00 122.32 ? 8   PHE   K CA  1 
ATOM   17956 C  C   . PHE   K  11 7   ? 12.881  -127.819 -13.177 1.00 123.03 ? 8   PHE   K C   1 
ATOM   17957 O  O   . PHE   K  11 7   ? 12.882  -126.745 -12.548 1.00 120.31 ? 8   PHE   K O   1 
ATOM   17958 C  CB  . PHE   K  11 7   ? 12.367  -130.267 -12.580 1.00 125.33 ? 8   PHE   K CB  1 
ATOM   17959 C  CG  . PHE   K  11 7   ? 10.928  -129.956 -12.249 1.00 124.17 ? 8   PHE   K CG  1 
ATOM   17960 C  CD1 . PHE   K  11 7   ? 10.554  -129.546 -10.977 1.00 119.94 ? 8   PHE   K CD1 1 
ATOM   17961 C  CD2 . PHE   K  11 7   ? 9.936   -130.114 -13.205 1.00 126.64 ? 8   PHE   K CD2 1 
ATOM   17962 C  CE1 . PHE   K  11 7   ? 9.226   -129.275 -10.680 1.00 117.85 ? 8   PHE   K CE1 1 
ATOM   17963 C  CE2 . PHE   K  11 7   ? 8.609   -129.843 -12.907 1.00 125.24 ? 8   PHE   K CE2 1 
ATOM   17964 C  CZ  . PHE   K  11 7   ? 8.256   -129.424 -11.645 1.00 120.55 ? 8   PHE   K CZ  1 
ATOM   17965 N  N   . GLN   K  11 8   ? 12.529  -127.944 -14.459 1.00 128.75 ? 9   GLN   K N   1 
ATOM   17966 C  CA  . GLN   K  11 8   ? 12.018  -126.839 -15.316 1.00 131.69 ? 9   GLN   K CA  1 
ATOM   17967 C  C   . GLN   K  11 8   ? 10.849  -126.140 -14.607 1.00 130.02 ? 9   GLN   K C   1 
ATOM   17968 O  O   . GLN   K  11 8   ? 10.883  -124.901 -14.501 1.00 128.83 ? 9   GLN   K O   1 
ATOM   17969 C  CB  . GLN   K  11 8   ? 11.630  -127.394 -16.691 1.00 138.12 ? 9   GLN   K CB  1 
ATOM   17970 C  CG  . GLN   K  11 8   ? 10.425  -126.719 -17.335 1.00 143.47 ? 9   GLN   K CG  1 
ATOM   17971 C  CD  . GLN   K  11 8   ? 9.148   -127.491 -17.107 1.00 145.05 ? 9   GLN   K CD  1 
ATOM   17972 O  OE1 . GLN   K  11 8   ? 8.207   -126.999 -16.487 1.00 142.52 ? 9   GLN   K OE1 1 
ATOM   17973 N  NE2 . GLN   K  11 8   ? 9.110   -128.718 -17.602 1.00 150.14 ? 9   GLN   K NE2 1 
ATOM   17974 N  N   . GLY   K  11 9   ? 9.860   -126.913 -14.147 1.00 128.73 ? 10  GLY   K N   1 
ATOM   17975 C  CA  . GLY   K  11 9   ? 8.632   -126.422 -13.489 1.00 125.13 ? 10  GLY   K CA  1 
ATOM   17976 C  C   . GLY   K  11 9   ? 8.915   -125.680 -12.193 1.00 119.97 ? 10  GLY   K C   1 
ATOM   17977 O  O   . GLY   K  11 9   ? 8.091   -124.826 -11.825 1.00 121.20 ? 10  GLY   K O   1 
ATOM   17978 N  N   . GLY   K  11 10  ? 10.018  -126.005 -11.511 1.00 117.91 ? 11  GLY   K N   1 
ATOM   17979 C  CA  . GLY   K  11 10  ? 10.458  -125.324 -10.277 1.00 117.30 ? 11  GLY   K CA  1 
ATOM   17980 C  C   . GLY   K  11 10  ? 11.069  -126.294 -9.280  1.00 114.56 ? 11  GLY   K C   1 
ATOM   17981 O  O   . GLY   K  11 10  ? 12.033  -126.993 -9.651  1.00 117.26 ? 11  GLY   K O   1 
ATOM   17982 N  N   . ILE   K  11 11  ? 10.535  -126.327 -8.055  1.00 111.26 ? 12  ILE   K N   1 
ATOM   17983 C  CA  . ILE   K  11 11  ? 10.970  -127.254 -6.970  1.00 109.22 ? 12  ILE   K CA  1 
ATOM   17984 C  C   . ILE   K  11 11  ? 9.749   -128.045 -6.494  1.00 106.59 ? 12  ILE   K C   1 
ATOM   17985 O  O   . ILE   K  11 11  ? 8.677   -127.438 -6.320  1.00 100.36 ? 12  ILE   K O   1 
ATOM   17986 C  CB  . ILE   K  11 11  ? 11.643  -126.490 -5.812  1.00 110.14 ? 12  ILE   K CB  1 
ATOM   17987 C  CG1 . ILE   K  11 11  ? 12.692  -125.499 -6.324  1.00 114.04 ? 12  ILE   K CG1 1 
ATOM   17988 C  CG2 . ILE   K  11 11  ? 12.231  -127.455 -4.791  1.00 108.36 ? 12  ILE   K CG2 1 
ATOM   17989 C  CD1 . ILE   K  11 11  ? 13.122  -124.474 -5.303  1.00 113.46 ? 12  ILE   K CD1 1 
ATOM   17990 N  N   . ILE   K  11 12  ? 9.922   -129.355 -6.307  1.00 106.51 ? 13  ILE   K N   1 
ATOM   17991 C  CA  . ILE   K  11 12  ? 8.900   -130.277 -5.734  1.00 106.92 ? 13  ILE   K CA  1 
ATOM   17992 C  C   . ILE   K  11 12  ? 9.405   -130.739 -4.366  1.00 101.24 ? 13  ILE   K C   1 
ATOM   17993 O  O   . ILE   K  11 12  ? 10.597  -131.091 -4.271  1.00 98.53  ? 13  ILE   K O   1 
ATOM   17994 C  CB  . ILE   K  11 12  ? 8.624   -131.453 -6.695  1.00 109.21 ? 13  ILE   K CB  1 
ATOM   17995 C  CG1 . ILE   K  11 12  ? 7.567   -131.084 -7.740  1.00 114.65 ? 13  ILE   K CG1 1 
ATOM   17996 C  CG2 . ILE   K  11 12  ? 8.246   -132.719 -5.938  1.00 108.87 ? 13  ILE   K CG2 1 
ATOM   17997 C  CD1 . ILE   K  11 12  ? 6.162   -131.015 -7.196  1.00 116.02 ? 13  ILE   K CD1 1 
ATOM   17998 N  N   . VAL   K  11 13  ? 8.531   -130.724 -3.357  1.00 99.61  ? 14  VAL   K N   1 
ATOM   17999 C  CA  . VAL   K  11 13  ? 8.851   -131.145 -1.962  1.00 99.19  ? 14  VAL   K CA  1 
ATOM   18000 C  C   . VAL   K  11 13  ? 7.831   -132.199 -1.523  1.00 99.38  ? 14  VAL   K C   1 
ATOM   18001 O  O   . VAL   K  11 13  ? 6.620   -131.897 -1.528  1.00 104.14 ? 14  VAL   K O   1 
ATOM   18002 C  CB  . VAL   K  11 13  ? 8.877   -129.944 -0.999  1.00 96.25  ? 14  VAL   K CB  1 
ATOM   18003 C  CG1 . VAL   K  11 13  ? 9.176   -130.369 0.430   1.00 94.98  ? 14  VAL   K CG1 1 
ATOM   18004 C  CG2 . VAL   K  11 13  ? 9.864   -128.883 -1.456  1.00 96.82  ? 14  VAL   K CG2 1 
ATOM   18005 N  N   . ALA   K  11 14  ? 8.320   -133.388 -1.163  1.00 97.22  ? 15  ALA   K N   1 
ATOM   18006 C  CA  . ALA   K  11 14  ? 7.525   -134.530 -0.660  1.00 97.06  ? 15  ALA   K CA  1 
ATOM   18007 C  C   . ALA   K  11 14  ? 8.140   -135.015 0.655   1.00 93.20  ? 15  ALA   K C   1 
ATOM   18008 O  O   . ALA   K  11 14  ? 9.374   -135.189 0.706   1.00 90.59  ? 15  ALA   K O   1 
ATOM   18009 C  CB  . ALA   K  11 14  ? 7.486   -135.627 -1.695  1.00 97.58  ? 15  ALA   K CB  1 
ATOM   18010 N  N   . VAL   K  11 15  ? 7.308   -135.190 1.682   1.00 93.13  ? 16  VAL   K N   1 
ATOM   18011 C  CA  . VAL   K  11 15  ? 7.706   -135.738 3.012   1.00 92.34  ? 16  VAL   K CA  1 
ATOM   18012 C  C   . VAL   K  11 15  ? 6.706   -136.837 3.374   1.00 91.76  ? 16  VAL   K C   1 
ATOM   18013 O  O   . VAL   K  11 15  ? 5.608   -136.843 2.787   1.00 93.53  ? 16  VAL   K O   1 
ATOM   18014 C  CB  . VAL   K  11 15  ? 7.756   -134.635 4.089   1.00 90.54  ? 16  VAL   K CB  1 
ATOM   18015 C  CG1 . VAL   K  11 15  ? 8.583   -133.443 3.633   1.00 91.23  ? 16  VAL   K CG1 1 
ATOM   18016 C  CG2 . VAL   K  11 15  ? 6.365   -134.186 4.516   1.00 89.68  ? 16  VAL   K CG2 1 
ATOM   18017 N  N   . ASP   K  11 16  ? 7.076   -137.732 4.293   1.00 90.72  ? 17  ASP   K N   1 
ATOM   18018 C  CA  . ASP   K  11 16  ? 6.133   -138.700 4.914   1.00 93.64  ? 17  ASP   K CA  1 
ATOM   18019 C  C   . ASP   K  11 16  ? 5.552   -138.025 6.160   1.00 94.99  ? 17  ASP   K C   1 
ATOM   18020 O  O   . ASP   K  11 16  ? 5.901   -136.849 6.398   1.00 95.38  ? 17  ASP   K O   1 
ATOM   18021 C  CB  . ASP   K  11 16  ? 6.816   -140.034 5.216   1.00 94.11  ? 17  ASP   K CB  1 
ATOM   18022 C  CG  . ASP   K  11 16  ? 7.578   -140.021 6.525   1.00 92.88  ? 17  ASP   K CG  1 
ATOM   18023 O  OD1 . ASP   K  11 16  ? 8.443   -139.146 6.679   1.00 93.64  ? 17  ASP   K OD1 1 
ATOM   18024 O  OD2 . ASP   K  11 16  ? 7.278   -140.862 7.391   1.00 95.78  ? 17  ASP   K OD2 1 
ATOM   18025 N  N   . SER   K  11 17  ? 4.701   -138.719 6.924   1.00 94.26  ? 18  SER   K N   1 
ATOM   18026 C  CA  . SER   K  11 17  ? 4.002   -138.136 8.099   1.00 96.11  ? 18  SER   K CA  1 
ATOM   18027 C  C   . SER   K  11 17  ? 4.055   -139.072 9.310   1.00 97.46  ? 18  SER   K C   1 
ATOM   18028 O  O   . SER   K  11 17  ? 3.061   -139.091 10.058  1.00 101.16 ? 18  SER   K O   1 
ATOM   18029 C  CB  . SER   K  11 17  ? 2.574   -137.798 7.759   1.00 96.49  ? 18  SER   K CB  1 
ATOM   18030 O  OG  . SER   K  11 17  ? 1.777   -138.972 7.713   1.00 94.15  ? 18  SER   K OG  1 
ATOM   18031 N  N   . ARG   K  11 18  ? 5.160   -139.792 9.526   1.00 96.73  ? 19  ARG   K N   1 
ATOM   18032 C  CA  . ARG   K  11 18  ? 5.263   -140.750 10.659  1.00 97.27  ? 19  ARG   K CA  1 
ATOM   18033 C  C   . ARG   K  11 18  ? 6.360   -140.334 11.639  1.00 94.42  ? 19  ARG   K C   1 
ATOM   18034 O  O   . ARG   K  11 18  ? 7.512   -140.148 11.202  1.00 91.51  ? 19  ARG   K O   1 
ATOM   18035 C  CB  . ARG   K  11 18  ? 5.542   -142.175 10.183  1.00 98.06  ? 19  ARG   K CB  1 
ATOM   18036 C  CG  . ARG   K  11 18  ? 5.608   -143.171 11.331  1.00 100.18 ? 19  ARG   K CG  1 
ATOM   18037 C  CD  . ARG   K  11 18  ? 5.921   -144.573 10.866  1.00 101.88 ? 19  ARG   K CD  1 
ATOM   18038 N  NE  . ARG   K  11 18  ? 4.712   -145.345 10.619  1.00 105.43 ? 19  ARG   K NE  1 
ATOM   18039 C  CZ  . ARG   K  11 18  ? 4.675   -146.514 9.986   1.00 108.93 ? 19  ARG   K CZ  1 
ATOM   18040 N  NH1 . ARG   K  11 18  ? 5.786   -147.061 9.518   1.00 111.30 ? 19  ARG   K NH1 1 
ATOM   18041 N  NH2 . ARG   K  11 18  ? 3.520   -147.136 9.820   1.00 111.02 ? 19  ARG   K NH2 1 
ATOM   18042 N  N   . ALA   K  11 19  ? 5.996   -140.260 12.923  1.00 96.10  ? 20  ALA   K N   1 
ATOM   18043 C  CA  . ALA   K  11 19  ? 6.893   -140.021 14.076  1.00 98.30  ? 20  ALA   K CA  1 
ATOM   18044 C  C   . ALA   K  11 19  ? 6.981   -141.300 14.908  1.00 96.06  ? 20  ALA   K C   1 
ATOM   18045 O  O   . ALA   K  11 19  ? 5.927   -141.919 15.146  1.00 91.82  ? 20  ALA   K O   1 
ATOM   18046 C  CB  . ALA   K  11 19  ? 6.370   -138.877 14.905  1.00 100.27 ? 20  ALA   K CB  1 
ATOM   18047 N  N   . THR   K  11 20  ? 8.190   -141.661 15.346  1.00 100.61 ? 21  THR   K N   1 
ATOM   18048 C  CA  . THR   K  11 20  ? 8.468   -142.888 16.137  1.00 105.81 ? 21  THR   K CA  1 
ATOM   18049 C  C   . THR   K  11 20  ? 9.297   -142.546 17.380  1.00 111.35 ? 21  THR   K C   1 
ATOM   18050 O  O   . THR   K  11 20  ? 10.229  -141.719 17.271  1.00 108.97 ? 21  THR   K O   1 
ATOM   18051 C  CB  . THR   K  11 20  ? 9.206   -143.937 15.297  1.00 107.65 ? 21  THR   K CB  1 
ATOM   18052 O  OG1 . THR   K  11 20  ? 10.460  -143.380 14.899  1.00 106.48 ? 21  THR   K OG1 1 
ATOM   18053 C  CG2 . THR   K  11 20  ? 8.424   -144.373 14.077  1.00 107.43 ? 21  THR   K CG2 1 
ATOM   18054 N  N   . ALA   K  11 21  ? 8.957   -143.171 18.511  1.00 118.27 ? 22  ALA   K N   1 
ATOM   18055 C  CA  . ALA   K  11 21  ? 9.753   -143.192 19.759  1.00 121.14 ? 22  ALA   K CA  1 
ATOM   18056 C  C   . ALA   K  11 21  ? 10.208  -144.635 20.001  1.00 125.62 ? 22  ALA   K C   1 
ATOM   18057 O  O   . ALA   K  11 21  ? 9.388   -145.447 20.478  1.00 125.86 ? 22  ALA   K O   1 
ATOM   18058 C  CB  . ALA   K  11 21  ? 8.942   -142.649 20.911  1.00 124.09 ? 22  ALA   K CB  1 
ATOM   18059 N  N   . GLY   K  11 22  ? 11.460  -144.943 19.652  1.00 126.98 ? 23  GLY   K N   1 
ATOM   18060 C  CA  . GLY   K  11 22  ? 11.975  -146.324 19.563  1.00 127.19 ? 23  GLY   K CA  1 
ATOM   18061 C  C   . GLY   K  11 22  ? 11.312  -147.077 18.420  1.00 124.72 ? 23  GLY   K C   1 
ATOM   18062 O  O   . GLY   K  11 22  ? 11.412  -146.603 17.270  1.00 127.18 ? 23  GLY   K O   1 
ATOM   18063 N  N   . ASN   K  11 23  ? 10.644  -148.196 18.722  1.00 123.04 ? 24  ASN   K N   1 
ATOM   18064 C  CA  . ASN   K  11 23  ? 9.903   -149.035 17.739  1.00 122.99 ? 24  ASN   K CA  1 
ATOM   18065 C  C   . ASN   K  11 23  ? 8.394   -148.821 17.907  1.00 116.09 ? 24  ASN   K C   1 
ATOM   18066 O  O   . ASN   K  11 23  ? 7.616   -149.587 17.304  1.00 115.25 ? 24  ASN   K O   1 
ATOM   18067 C  CB  . ASN   K  11 23  ? 10.266  -150.515 17.882  1.00 128.10 ? 24  ASN   K CB  1 
ATOM   18068 C  CG  . ASN   K  11 23  ? 11.696  -150.804 17.479  1.00 131.90 ? 24  ASN   K CG  1 
ATOM   18069 O  OD1 . ASN   K  11 23  ? 12.117  -150.443 16.382  1.00 133.16 ? 24  ASN   K OD1 1 
ATOM   18070 N  ND2 . ASN   K  11 23  ? 12.450  -151.452 18.353  1.00 135.91 ? 24  ASN   K ND2 1 
ATOM   18071 N  N   . TRP   K  11 24  ? 8.005   -147.816 18.696  1.00 112.96 ? 25  TRP   K N   1 
ATOM   18072 C  CA  . TRP   K  11 24  ? 6.596   -147.408 18.931  1.00 110.96 ? 25  TRP   K CA  1 
ATOM   18073 C  C   . TRP   K  11 24  ? 6.251   -146.258 17.977  1.00 109.42 ? 25  TRP   K C   1 
ATOM   18074 O  O   . TRP   K  11 24  ? 7.023   -145.277 17.938  1.00 111.34 ? 25  TRP   K O   1 
ATOM   18075 C  CB  . TRP   K  11 24  ? 6.402   -147.031 20.406  1.00 110.26 ? 25  TRP   K CB  1 
ATOM   18076 C  CG  . TRP   K  11 24  ? 5.330   -146.021 20.661  1.00 109.85 ? 25  TRP   K CG  1 
ATOM   18077 C  CD1 . TRP   K  11 24  ? 5.476   -144.667 20.753  1.00 109.98 ? 25  TRP   K CD1 1 
ATOM   18078 C  CD2 . TRP   K  11 24  ? 3.935   -146.289 20.874  1.00 109.55 ? 25  TRP   K CD2 1 
ATOM   18079 N  NE1 . TRP   K  11 24  ? 4.268   -144.074 20.999  1.00 111.05 ? 25  TRP   K NE1 1 
ATOM   18080 C  CE2 . TRP   K  11 24  ? 3.304   -145.044 21.080  1.00 110.99 ? 25  TRP   K CE2 1 
ATOM   18081 C  CE3 . TRP   K  11 24  ? 3.163   -147.454 20.903  1.00 109.22 ? 25  TRP   K CE3 1 
ATOM   18082 C  CZ2 . TRP   K  11 24  ? 1.935   -144.936 21.315  1.00 112.01 ? 25  TRP   K CZ2 1 
ATOM   18083 C  CZ3 . TRP   K  11 24  ? 1.810   -147.346 21.133  1.00 111.27 ? 25  TRP   K CZ3 1 
ATOM   18084 C  CH2 . TRP   K  11 24  ? 1.208   -146.104 21.336  1.00 112.59 ? 25  TRP   K CH2 1 
ATOM   18085 N  N   . VAL   K  11 25  ? 5.154   -146.393 17.223  1.00 105.80 ? 26  VAL   K N   1 
ATOM   18086 C  CA  . VAL   K  11 25  ? 4.624   -145.344 16.300  1.00 102.41 ? 26  VAL   K CA  1 
ATOM   18087 C  C   . VAL   K  11 25  ? 3.831   -144.337 17.137  1.00 101.16 ? 26  VAL   K C   1 
ATOM   18088 O  O   . VAL   K  11 25  ? 2.682   -144.651 17.514  1.00 100.80 ? 26  VAL   K O   1 
ATOM   18089 C  CB  . VAL   K  11 25  ? 3.759   -145.946 15.177  1.00 101.32 ? 26  VAL   K CB  1 
ATOM   18090 C  CG1 . VAL   K  11 25  ? 3.138   -144.871 14.298  1.00 99.60  ? 26  VAL   K CG1 1 
ATOM   18091 C  CG2 . VAL   K  11 25  ? 4.546   -146.932 14.331  1.00 101.77 ? 26  VAL   K CG2 1 
ATOM   18092 N  N   . ALA   K  11 26  ? 4.434   -143.178 17.419  1.00 100.53 ? 27  ALA   K N   1 
ATOM   18093 C  CA  . ALA   K  11 26  ? 3.841   -142.093 18.231  1.00 101.68 ? 27  ALA   K CA  1 
ATOM   18094 C  C   . ALA   K  11 26  ? 2.695   -141.445 17.449  1.00 98.54  ? 27  ALA   K C   1 
ATOM   18095 O  O   . ALA   K  11 26  ? 1.585   -141.353 18.007  1.00 97.81  ? 27  ALA   K O   1 
ATOM   18096 C  CB  . ALA   K  11 26  ? 4.900   -141.087 18.610  1.00 102.27 ? 27  ALA   K CB  1 
ATOM   18097 N  N   . SER   K  11 27  ? 2.949   -141.043 16.200  1.00 98.59  ? 28  SER   K N   1 
ATOM   18098 C  CA  . SER   K  11 27  ? 1.984   -140.307 15.342  1.00 99.72  ? 28  SER   K CA  1 
ATOM   18099 C  C   . SER   K  11 27  ? 2.114   -140.740 13.877  1.00 95.16  ? 28  SER   K C   1 
ATOM   18100 O  O   . SER   K  11 27  ? 3.202   -141.202 13.476  1.00 88.58  ? 28  SER   K O   1 
ATOM   18101 C  CB  . SER   K  11 27  ? 2.169   -138.817 15.500  1.00 99.42  ? 28  SER   K CB  1 
ATOM   18102 O  OG  . SER   K  11 27  ? 1.368   -138.100 14.572  1.00 103.23 ? 28  SER   K OG  1 
ATOM   18103 N  N   . GLN   K  11 28  ? 1.022   -140.593 13.121  1.00 96.12  ? 29  GLN   K N   1 
ATOM   18104 C  CA  . GLN   K  11 28  ? 0.949   -140.829 11.654  1.00 99.69  ? 29  GLN   K CA  1 
ATOM   18105 C  C   . GLN   K  11 28  ? 0.454   -139.567 10.934  1.00 98.49  ? 29  GLN   K C   1 
ATOM   18106 O  O   . GLN   K  11 28  ? 0.185   -139.663 9.720   1.00 96.65  ? 29  GLN   K O   1 
ATOM   18107 C  CB  . GLN   K  11 28  ? -0.008  -141.983 11.356  1.00 102.50 ? 29  GLN   K CB  1 
ATOM   18108 C  CG  . GLN   K  11 28  ? 0.428   -143.320 11.938  1.00 105.14 ? 29  GLN   K CG  1 
ATOM   18109 C  CD  . GLN   K  11 28  ? 1.095   -144.207 10.914  1.00 105.19 ? 29  GLN   K CD  1 
ATOM   18110 O  OE1 . GLN   K  11 28  ? 2.066   -143.826 10.265  1.00 109.73 ? 29  GLN   K OE1 1 
ATOM   18111 N  NE2 . GLN   K  11 28  ? 0.577   -145.414 10.765  1.00 106.54 ? 29  GLN   K NE2 1 
ATOM   18112 N  N   . THR   K  11 29  ? 0.342   -138.435 11.640  1.00 98.65  ? 30  THR   K N   1 
ATOM   18113 C  CA  . THR   K  11 29  ? -0.277  -137.186 11.120  1.00 98.42  ? 30  THR   K CA  1 
ATOM   18114 C  C   . THR   K  11 29  ? 0.677   -135.997 11.275  1.00 99.65  ? 30  THR   K C   1 
ATOM   18115 O  O   . THR   K  11 29  ? 0.189   -134.850 11.195  1.00 101.33 ? 30  THR   K O   1 
ATOM   18116 C  CB  . THR   K  11 29  ? -1.613  -136.911 11.821  1.00 99.54  ? 30  THR   K CB  1 
ATOM   18117 O  OG1 . THR   K  11 29  ? -1.369  -136.407 13.134  1.00 101.32 ? 30  THR   K OG1 1 
ATOM   18118 C  CG2 . THR   K  11 29  ? -2.476  -138.147 11.935  1.00 99.44  ? 30  THR   K CG2 1 
ATOM   18119 N  N   . VAL   K  11 30  ? 1.976   -136.246 11.461  1.00 97.96  ? 31  VAL   K N   1 
ATOM   18120 C  CA  . VAL   K  11 30  ? 2.976   -135.171 11.728  1.00 99.20  ? 31  VAL   K CA  1 
ATOM   18121 C  C   . VAL   K  11 30  ? 3.197   -134.364 10.445  1.00 97.08  ? 31  VAL   K C   1 
ATOM   18122 O  O   . VAL   K  11 30  ? 3.315   -134.977 9.360   1.00 88.37  ? 31  VAL   K O   1 
ATOM   18123 C  CB  . VAL   K  11 30  ? 4.310   -135.721 12.263  1.00 102.09 ? 31  VAL   K CB  1 
ATOM   18124 C  CG1 . VAL   K  11 30  ? 5.308   -134.598 12.502  1.00 105.32 ? 31  VAL   K CG1 1 
ATOM   18125 C  CG2 . VAL   K  11 30  ? 4.119   -136.536 13.530  1.00 100.84 ? 31  VAL   K CG2 1 
ATOM   18126 N  N   . LYS   K  11 31  ? 3.259   -133.038 10.594  1.00 99.42  ? 32  LYS   K N   1 
ATOM   18127 C  CA  . LYS   K  11 31  ? 3.664   -132.079 9.538   1.00 99.42  ? 32  LYS   K CA  1 
ATOM   18128 C  C   . LYS   K  11 31  ? 5.190   -131.941 9.581   1.00 99.11  ? 32  LYS   K C   1 
ATOM   18129 O  O   . LYS   K  11 31  ? 5.697   -131.390 10.575  1.00 100.67 ? 32  LYS   K O   1 
ATOM   18130 C  CB  . LYS   K  11 31  ? 2.986   -130.727 9.769   1.00 104.00 ? 32  LYS   K CB  1 
ATOM   18131 C  CG  . LYS   K  11 31  ? 1.540   -130.622 9.303   1.00 110.64 ? 32  LYS   K CG  1 
ATOM   18132 C  CD  . LYS   K  11 31  ? 1.107   -129.187 9.044   1.00 118.28 ? 32  LYS   K CD  1 
ATOM   18133 C  CE  . LYS   K  11 31  ? 1.976   -128.483 8.020   1.00 122.13 ? 32  LYS   K CE  1 
ATOM   18134 N  NZ  . LYS   K  11 31  ? 1.637   -127.047 7.891   1.00 125.86 ? 32  LYS   K NZ  1 
ATOM   18135 N  N   . LYS   K  11 32  ? 5.891   -132.449 8.563   1.00 96.58  ? 33  LYS   K N   1 
ATOM   18136 C  CA  . LYS   K  11 32  ? 7.378   -132.440 8.480   1.00 95.96  ? 33  LYS   K CA  1 
ATOM   18137 C  C   . LYS   K  11 32  ? 7.853   -131.361 7.502   1.00 94.29  ? 33  LYS   K C   1 
ATOM   18138 O  O   . LYS   K  11 32  ? 9.074   -131.277 7.260   1.00 92.30  ? 33  LYS   K O   1 
ATOM   18139 C  CB  . LYS   K  11 32  ? 7.887   -133.817 8.054   1.00 96.61  ? 33  LYS   K CB  1 
ATOM   18140 C  CG  . LYS   K  11 32  ? 7.610   -134.922 9.058   1.00 98.89  ? 33  LYS   K CG  1 
ATOM   18141 C  CD  . LYS   K  11 32  ? 8.141   -136.255 8.620   1.00 100.14 ? 33  LYS   K CD  1 
ATOM   18142 C  CE  . LYS   K  11 32  ? 7.887   -137.336 9.645   1.00 102.12 ? 33  LYS   K CE  1 
ATOM   18143 N  NZ  . LYS   K  11 32  ? 8.482   -138.620 9.218   1.00 103.48 ? 33  LYS   K NZ  1 
ATOM   18144 N  N   . VAL   K  11 33  ? 6.922   -130.582 6.949   1.00 95.11  ? 34  VAL   K N   1 
ATOM   18145 C  CA  . VAL   K  11 33  ? 7.221   -129.337 6.186   1.00 97.20  ? 34  VAL   K CA  1 
ATOM   18146 C  C   . VAL   K  11 33  ? 6.706   -128.162 7.020   1.00 96.27  ? 34  VAL   K C   1 
ATOM   18147 O  O   . VAL   K  11 33  ? 5.542   -128.213 7.459   1.00 93.46  ? 34  VAL   K O   1 
ATOM   18148 C  CB  . VAL   K  11 33  ? 6.594   -129.358 4.779   1.00 96.86  ? 34  VAL   K CB  1 
ATOM   18149 C  CG1 . VAL   K  11 33  ? 6.805   -128.045 4.046   1.00 98.34  ? 34  VAL   K CG1 1 
ATOM   18150 C  CG2 . VAL   K  11 33  ? 7.124   -130.513 3.950   1.00 97.27  ? 34  VAL   K CG2 1 
ATOM   18151 N  N   . ILE   K  11 34  ? 7.550   -127.154 7.236   1.00 99.21  ? 35  ILE   K N   1 
ATOM   18152 C  CA  . ILE   K  11 34  ? 7.183   -125.903 7.961   1.00 106.70 ? 35  ILE   K CA  1 
ATOM   18153 C  C   . ILE   K  11 34  ? 7.107   -124.774 6.927   1.00 110.18 ? 35  ILE   K C   1 
ATOM   18154 O  O   . ILE   K  11 34  ? 8.087   -124.581 6.173   1.00 106.59 ? 35  ILE   K O   1 
ATOM   18155 C  CB  . ILE   K  11 34  ? 8.158   -125.619 9.126   1.00 107.38 ? 35  ILE   K CB  1 
ATOM   18156 C  CG1 . ILE   K  11 34  ? 7.833   -124.322 9.876   1.00 111.90 ? 35  ILE   K CG1 1 
ATOM   18157 C  CG2 . ILE   K  11 34  ? 9.605   -125.662 8.666   1.00 106.89 ? 35  ILE   K CG2 1 
ATOM   18158 C  CD1 . ILE   K  11 34  ? 8.294   -123.051 9.192   1.00 114.54 ? 35  ILE   K CD1 1 
ATOM   18159 N  N   . GLU   K  11 35  ? 5.964   -124.085 6.874   1.00 115.16 ? 36  GLU   K N   1 
ATOM   18160 C  CA  . GLU   K  11 35  ? 5.734   -122.924 5.977   1.00 116.71 ? 36  GLU   K CA  1 
ATOM   18161 C  C   . GLU   K  11 35  ? 6.371   -121.691 6.625   1.00 116.14 ? 36  GLU   K C   1 
ATOM   18162 O  O   . GLU   K  11 35  ? 5.685   -121.014 7.416   1.00 118.02 ? 36  GLU   K O   1 
ATOM   18163 C  CB  . GLU   K  11 35  ? 4.239   -122.730 5.711   1.00 122.27 ? 36  GLU   K CB  1 
ATOM   18164 C  CG  . GLU   K  11 35  ? 3.538   -123.985 5.215   1.00 122.74 ? 36  GLU   K CG  1 
ATOM   18165 C  CD  . GLU   K  11 35  ? 2.237   -123.734 4.471   1.00 124.44 ? 36  GLU   K CD  1 
ATOM   18166 O  OE1 . GLU   K  11 35  ? 1.645   -122.644 4.666   1.00 129.06 ? 36  GLU   K OE1 1 
ATOM   18167 O  OE2 . GLU   K  11 35  ? 1.821   -124.625 3.690   1.00 128.53 ? 36  GLU   K OE2 1 
ATOM   18168 N  N   . ILE   K  11 36  ? 7.652   -121.448 6.331   1.00 111.99 ? 37  ILE   K N   1 
ATOM   18169 C  CA  . ILE   K  11 36  ? 8.430   -120.280 6.839   1.00 111.42 ? 37  ILE   K CA  1 
ATOM   18170 C  C   . ILE   K  11 36  ? 7.766   -118.995 6.325   1.00 114.68 ? 37  ILE   K C   1 
ATOM   18171 O  O   . ILE   K  11 36  ? 7.576   -118.059 7.129   1.00 116.44 ? 37  ILE   K O   1 
ATOM   18172 C  CB  . ILE   K  11 36  ? 9.912   -120.389 6.420   1.00 108.72 ? 37  ILE   K CB  1 
ATOM   18173 C  CG1 . ILE   K  11 36  ? 10.627  -121.508 7.185   1.00 104.20 ? 37  ILE   K CG1 1 
ATOM   18174 C  CG2 . ILE   K  11 36  ? 10.614  -119.049 6.582   1.00 109.56 ? 37  ILE   K CG2 1 
ATOM   18175 C  CD1 . ILE   K  11 36  ? 11.974  -121.896 6.618   1.00 101.70 ? 37  ILE   K CD1 1 
ATOM   18176 N  N   . ASN   K  11 37  ? 7.424   -118.960 5.034   1.00 117.85 ? 38  ASN   K N   1 
ATOM   18177 C  CA  . ASN   K  11 37  ? 6.726   -117.822 4.378   1.00 121.63 ? 38  ASN   K CA  1 
ATOM   18178 C  C   . ASN   K  11 37  ? 6.131   -118.324 3.062   1.00 120.71 ? 38  ASN   K C   1 
ATOM   18179 O  O   . ASN   K  11 37  ? 6.338   -119.480 2.702   1.00 123.75 ? 38  ASN   K O   1 
ATOM   18180 C  CB  . ASN   K  11 37  ? 7.668   -116.618 4.248   1.00 122.53 ? 38  ASN   K CB  1 
ATOM   18181 C  CG  . ASN   K  11 37  ? 8.619   -116.692 3.070   1.00 125.90 ? 38  ASN   K CG  1 
ATOM   18182 O  OD1 . ASN   K  11 37  ? 8.274   -117.212 2.011   1.00 127.47 ? 38  ASN   K OD1 1 
ATOM   18183 N  ND2 . ASN   K  11 37  ? 9.816   -116.151 3.235   1.00 126.99 ? 38  ASN   K ND2 1 
ATOM   18184 N  N   . PRO   K  11 38  ? 5.375   -117.488 2.312   1.00 121.83 ? 39  PRO   K N   1 
ATOM   18185 C  CA  . PRO   K  11 38  ? 4.761   -117.900 1.046   1.00 122.81 ? 39  PRO   K CA  1 
ATOM   18186 C  C   . PRO   K  11 38  ? 5.701   -118.371 -0.076  1.00 118.64 ? 39  PRO   K C   1 
ATOM   18187 O  O   . PRO   K  11 38  ? 5.215   -119.027 -0.983  1.00 119.84 ? 39  PRO   K O   1 
ATOM   18188 C  CB  . PRO   K  11 38  ? 4.090   -116.619 0.532   1.00 126.67 ? 39  PRO   K CB  1 
ATOM   18189 C  CG  . PRO   K  11 38  ? 3.844   -115.803 1.777   1.00 129.31 ? 39  PRO   K CG  1 
ATOM   18190 C  CD  . PRO   K  11 38  ? 5.032   -116.104 2.666   1.00 123.56 ? 39  PRO   K CD  1 
ATOM   18191 N  N   . PHE   K  11 39  ? 6.980   -117.981 -0.031  1.00 116.82 ? 40  PHE   K N   1 
ATOM   18192 C  CA  . PHE   K  11 39  ? 8.023   -118.372 -1.019  1.00 119.57 ? 40  PHE   K CA  1 
ATOM   18193 C  C   . PHE   K  11 39  ? 9.043   -119.342 -0.409  1.00 114.93 ? 40  PHE   K C   1 
ATOM   18194 O  O   . PHE   K  11 39  ? 9.879   -119.839 -1.189  1.00 117.96 ? 40  PHE   K O   1 
ATOM   18195 C  CB  . PHE   K  11 39  ? 8.754   -117.141 -1.561  1.00 122.40 ? 40  PHE   K CB  1 
ATOM   18196 C  CG  . PHE   K  11 39  ? 8.067   -116.475 -2.725  1.00 129.69 ? 40  PHE   K CG  1 
ATOM   18197 C  CD1 . PHE   K  11 39  ? 8.354   -116.858 -4.027  1.00 135.42 ? 40  PHE   K CD1 1 
ATOM   18198 C  CD2 . PHE   K  11 39  ? 7.126   -115.476 -2.522  1.00 129.92 ? 40  PHE   K CD2 1 
ATOM   18199 C  CE1 . PHE   K  11 39  ? 7.717   -116.255 -5.101  1.00 136.35 ? 40  PHE   K CE1 1 
ATOM   18200 C  CE2 . PHE   K  11 39  ? 6.492   -114.873 -3.598  1.00 132.42 ? 40  PHE   K CE2 1 
ATOM   18201 C  CZ  . PHE   K  11 39  ? 6.787   -115.264 -4.885  1.00 134.54 ? 40  PHE   K CZ  1 
ATOM   18202 N  N   . LEU   K  11 40  ? 8.993   -119.603 0.906   1.00 113.16 ? 41  LEU   K N   1 
ATOM   18203 C  CA  . LEU   K  11 40  ? 10.018  -120.426 1.610   1.00 107.93 ? 41  LEU   K CA  1 
ATOM   18204 C  C   . LEU   K  11 40  ? 9.391   -121.617 2.345   1.00 107.69 ? 41  LEU   K C   1 
ATOM   18205 O  O   . LEU   K  11 40  ? 8.455   -121.411 3.148   1.00 101.64 ? 41  LEU   K O   1 
ATOM   18206 C  CB  . LEU   K  11 40  ? 10.821  -119.550 2.578   1.00 107.24 ? 41  LEU   K CB  1 
ATOM   18207 C  CG  . LEU   K  11 40  ? 12.253  -119.217 2.153   1.00 104.89 ? 41  LEU   K CG  1 
ATOM   18208 C  CD1 . LEU   K  11 40  ? 13.142  -119.040 3.372   1.00 100.80 ? 41  LEU   K CD1 1 
ATOM   18209 C  CD2 . LEU   K  11 40  ? 12.843  -120.286 1.241   1.00 105.05 ? 41  LEU   K CD2 1 
ATOM   18210 N  N   . LEU   K  11 41  ? 9.953   -122.807 2.095   1.00 105.96 ? 42  LEU   K N   1 
ATOM   18211 C  CA  . LEU   K  11 41  ? 9.561   -124.109 2.695   1.00 103.20 ? 42  LEU   K CA  1 
ATOM   18212 C  C   . LEU   K  11 41  ? 10.771  -124.729 3.401   1.00 98.14  ? 42  LEU   K C   1 
ATOM   18213 O  O   . LEU   K  11 41  ? 11.899  -124.584 2.886   1.00 94.47  ? 42  LEU   K O   1 
ATOM   18214 C  CB  . LEU   K  11 41  ? 9.046   -125.036 1.589   1.00 105.62 ? 42  LEU   K CB  1 
ATOM   18215 C  CG  . LEU   K  11 41  ? 7.540   -124.998 1.327   1.00 109.67 ? 42  LEU   K CG  1 
ATOM   18216 C  CD1 . LEU   K  11 41  ? 7.123   -126.181 0.469   1.00 111.55 ? 42  LEU   K CD1 1 
ATOM   18217 C  CD2 . LEU   K  11 41  ? 6.747   -124.982 2.627   1.00 110.38 ? 42  LEU   K CD2 1 
ATOM   18218 N  N   . GLY   K  11 42  ? 10.524  -125.405 4.526   1.00 97.78  ? 43  GLY   K N   1 
ATOM   18219 C  CA  . GLY   K  11 42  ? 11.546  -126.100 5.333   1.00 97.67  ? 43  GLY   K CA  1 
ATOM   18220 C  C   . GLY   K  11 42  ? 11.161  -127.546 5.598   1.00 96.78  ? 43  GLY   K C   1 
ATOM   18221 O  O   . GLY   K  11 42  ? 10.044  -127.777 6.101   1.00 93.36  ? 43  GLY   K O   1 
ATOM   18222 N  N   . THR   K  11 43  ? 12.054  -128.481 5.265   1.00 99.80  ? 44  THR   K N   1 
ATOM   18223 C  CA  . THR   K  11 43  ? 11.917  -129.946 5.496   1.00 103.11 ? 44  THR   K CA  1 
ATOM   18224 C  C   . THR   K  11 43  ? 12.451  -130.294 6.888   1.00 98.93  ? 44  THR   K C   1 
ATOM   18225 O  O   . THR   K  11 43  ? 13.468  -129.704 7.265   1.00 99.16  ? 44  THR   K O   1 
ATOM   18226 C  CB  . THR   K  11 43  ? 12.743  -130.739 4.481   1.00 106.57 ? 44  THR   K CB  1 
ATOM   18227 O  OG1 . THR   K  11 43  ? 13.962  -130.006 4.379   1.00 112.72 ? 44  THR   K OG1 1 
ATOM   18228 C  CG2 . THR   K  11 43  ? 12.088  -130.896 3.127   1.00 108.77 ? 44  THR   K CG2 1 
ATOM   18229 N  N   . MET   K  11 44  ? 11.823  -131.238 7.595   1.00 99.78  ? 45  MET   K N   1 
ATOM   18230 C  CA  . MET   K  11 44  ? 12.232  -131.654 8.967   1.00 97.17  ? 45  MET   K CA  1 
ATOM   18231 C  C   . MET   K  11 44  ? 12.663  -133.127 8.980   1.00 99.25  ? 45  MET   K C   1 
ATOM   18232 O  O   . MET   K  11 44  ? 11.887  -133.988 8.516   1.00 98.87  ? 45  MET   K O   1 
ATOM   18233 C  CB  . MET   K  11 44  ? 11.088  -131.466 9.965   1.00 96.73  ? 45  MET   K CB  1 
ATOM   18234 C  CG  . MET   K  11 44  ? 10.609  -130.044 10.064  1.00 96.83  ? 45  MET   K CG  1 
ATOM   18235 S  SD  . MET   K  11 44  ? 9.454   -129.841 11.432  1.00 101.93 ? 45  MET   K SD  1 
ATOM   18236 C  CE  . MET   K  11 44  ? 8.923   -128.159 11.126  1.00 104.35 ? 45  MET   K CE  1 
ATOM   18237 N  N   . ALA   K  11 45  ? 13.852  -133.394 9.527   1.00 95.59  ? 46  ALA   K N   1 
ATOM   18238 C  CA  . ALA   K  11 45  ? 14.415  -134.744 9.767   1.00 93.59  ? 46  ALA   K CA  1 
ATOM   18239 C  C   . ALA   K  11 45  ? 15.168  -134.734 11.100  1.00 91.63  ? 46  ALA   K C   1 
ATOM   18240 O  O   . ALA   K  11 45  ? 15.600  -133.652 11.524  1.00 94.84  ? 46  ALA   K O   1 
ATOM   18241 C  CB  . ALA   K  11 45  ? 15.327  -135.137 8.635   1.00 93.38  ? 46  ALA   K CB  1 
ATOM   18242 N  N   . GLY   K  11 46  ? 15.332  -135.898 11.725  1.00 90.94  ? 47  GLY   K N   1 
ATOM   18243 C  CA  . GLY   K  11 46  ? 15.980  -136.026 13.043  1.00 91.63  ? 47  GLY   K CA  1 
ATOM   18244 C  C   . GLY   K  11 46  ? 15.035  -135.611 14.156  1.00 89.75  ? 47  GLY   K C   1 
ATOM   18245 O  O   . GLY   K  11 46  ? 13.819  -135.848 14.015  1.00 94.10  ? 47  GLY   K O   1 
ATOM   18246 N  N   . GLY   K  11 47  ? 15.569  -135.009 15.222  1.00 88.63  ? 48  GLY   K N   1 
ATOM   18247 C  CA  . GLY   K  11 47  ? 14.789  -134.559 16.390  1.00 86.99  ? 48  GLY   K CA  1 
ATOM   18248 C  C   . GLY   K  11 47  ? 13.675  -133.621 15.969  1.00 85.38  ? 48  GLY   K C   1 
ATOM   18249 O  O   . GLY   K  11 47  ? 13.988  -132.588 15.348  1.00 83.70  ? 48  GLY   K O   1 
ATOM   18250 N  N   . ALA   K  11 48  ? 12.424  -133.983 16.271  1.00 86.32  ? 49  ALA   K N   1 
ATOM   18251 C  CA  . ALA   K  11 48  ? 11.204  -133.225 15.905  1.00 87.99  ? 49  ALA   K CA  1 
ATOM   18252 C  C   . ALA   K  11 48  ? 11.226  -131.847 16.576  1.00 86.96  ? 49  ALA   K C   1 
ATOM   18253 O  O   . ALA   K  11 48  ? 10.989  -130.847 15.876  1.00 89.21  ? 49  ALA   K O   1 
ATOM   18254 C  CB  . ALA   K  11 48  ? 9.973   -134.001 16.301  1.00 90.20  ? 49  ALA   K CB  1 
ATOM   18255 N  N   . ALA   K  11 49  ? 11.505  -131.809 17.883  1.00 87.31  ? 50  ALA   K N   1 
ATOM   18256 C  CA  . ALA   K  11 49  ? 11.540  -130.581 18.712  1.00 85.72  ? 50  ALA   K CA  1 
ATOM   18257 C  C   . ALA   K  11 49  ? 12.584  -129.615 18.153  1.00 82.50  ? 50  ALA   K C   1 
ATOM   18258 O  O   . ALA   K  11 49  ? 12.253  -128.440 17.998  1.00 85.71  ? 50  ALA   K O   1 
ATOM   18259 C  CB  . ALA   K  11 49  ? 11.839  -130.918 20.150  1.00 88.05  ? 50  ALA   K CB  1 
ATOM   18260 N  N   . ASP   K  11 50  ? 13.791  -130.102 17.857  1.00 80.31  ? 51  ASP   K N   1 
ATOM   18261 C  CA  . ASP   K  11 50  ? 14.917  -129.270 17.359  1.00 81.41  ? 51  ASP   K CA  1 
ATOM   18262 C  C   . ASP   K  11 50  ? 14.492  -128.588 16.053  1.00 84.98  ? 51  ASP   K C   1 
ATOM   18263 O  O   . ASP   K  11 50  ? 14.485  -127.342 16.027  1.00 87.30  ? 51  ASP   K O   1 
ATOM   18264 C  CB  . ASP   K  11 50  ? 16.199  -130.093 17.212  1.00 80.08  ? 51  ASP   K CB  1 
ATOM   18265 C  CG  . ASP   K  11 50  ? 16.713  -130.662 18.523  1.00 81.74  ? 51  ASP   K CG  1 
ATOM   18266 O  OD1 . ASP   K  11 50  ? 16.202  -130.247 19.580  1.00 82.25  ? 51  ASP   K OD1 1 
ATOM   18267 O  OD2 . ASP   K  11 50  ? 17.627  -131.510 18.476  1.00 82.88  ? 51  ASP   K OD2 1 
ATOM   18268 N  N   . CYS   K  11 51  ? 14.137  -129.358 15.017  1.00 85.76  ? 52  CYS   K N   1 
ATOM   18269 C  CA  . CYS   K  11 51  ? 13.733  -128.830 13.684  1.00 86.90  ? 52  CYS   K CA  1 
ATOM   18270 C  C   . CYS   K  11 51  ? 12.594  -127.822 13.845  1.00 87.02  ? 52  CYS   K C   1 
ATOM   18271 O  O   . CYS   K  11 51  ? 12.756  -126.673 13.397  1.00 90.46  ? 52  CYS   K O   1 
ATOM   18272 C  CB  . CYS   K  11 51  ? 13.268  -129.939 12.751  1.00 87.54  ? 52  CYS   K CB  1 
ATOM   18273 S  SG  . CYS   K  11 51  ? 14.535  -131.202 12.489  1.00 91.69  ? 52  CYS   K SG  1 
ATOM   18274 N  N   . GLN   K  11 52  ? 11.501  -128.255 14.476  1.00 84.82  ? 53  GLN   K N   1 
ATOM   18275 C  CA  . GLN   K  11 52  ? 10.245  -127.483 14.662  1.00 86.27  ? 53  GLN   K CA  1 
ATOM   18276 C  C   . GLN   K  11 52  ? 10.539  -126.148 15.360  1.00 85.54  ? 53  GLN   K C   1 
ATOM   18277 O  O   . GLN   K  11 52  ? 10.046  -125.114 14.875  1.00 90.34  ? 53  GLN   K O   1 
ATOM   18278 C  CB  . GLN   K  11 52  ? 9.257   -128.328 15.463  1.00 87.86  ? 53  GLN   K CB  1 
ATOM   18279 C  CG  . GLN   K  11 52  ? 7.905   -127.668 15.686  1.00 90.41  ? 53  GLN   K CG  1 
ATOM   18280 C  CD  . GLN   K  11 52  ? 6.916   -128.632 16.298  1.00 91.44  ? 53  GLN   K CD  1 
ATOM   18281 O  OE1 . GLN   K  11 52  ? 6.240   -128.321 17.277  1.00 96.05  ? 53  GLN   K OE1 1 
ATOM   18282 N  NE2 . GLN   K  11 52  ? 6.825   -129.823 15.727  1.00 90.17  ? 53  GLN   K NE2 1 
ATOM   18283 N  N   . PHE   K  11 53  ? 11.304  -126.166 16.455  1.00 81.27  ? 54  PHE   K N   1 
ATOM   18284 C  CA  . PHE   K  11 53  ? 11.646  -124.959 17.251  1.00 80.37  ? 54  PHE   K CA  1 
ATOM   18285 C  C   . PHE   K  11 53  ? 12.475  -123.989 16.401  1.00 80.38  ? 54  PHE   K C   1 
ATOM   18286 O  O   . PHE   K  11 53  ? 12.096  -122.807 16.305  1.00 81.85  ? 54  PHE   K O   1 
ATOM   18287 C  CB  . PHE   K  11 53  ? 12.407  -125.324 18.528  1.00 78.75  ? 54  PHE   K CB  1 
ATOM   18288 C  CG  . PHE   K  11 53  ? 12.763  -124.135 19.383  1.00 78.86  ? 54  PHE   K CG  1 
ATOM   18289 C  CD1 . PHE   K  11 53  ? 11.975  -123.776 20.466  1.00 78.90  ? 54  PHE   K CD1 1 
ATOM   18290 C  CD2 . PHE   K  11 53  ? 13.869  -123.354 19.083  1.00 78.61  ? 54  PHE   K CD2 1 
ATOM   18291 C  CE1 . PHE   K  11 53  ? 12.295  -122.672 21.240  1.00 78.09  ? 54  PHE   K CE1 1 
ATOM   18292 C  CE2 . PHE   K  11 53  ? 14.185  -122.249 19.856  1.00 78.46  ? 54  PHE   K CE2 1 
ATOM   18293 C  CZ  . PHE   K  11 53  ? 13.399  -121.912 20.934  1.00 77.99  ? 54  PHE   K CZ  1 
ATOM   18294 N  N   . TRP   K  11 54  ? 13.582  -124.464 15.825  1.00 79.57  ? 55  TRP   K N   1 
ATOM   18295 C  CA  . TRP   K  11 54  ? 14.600  -123.606 15.161  1.00 80.10  ? 55  TRP   K CA  1 
ATOM   18296 C  C   . TRP   K  11 54  ? 14.144  -123.171 13.765  1.00 80.51  ? 55  TRP   K C   1 
ATOM   18297 O  O   . TRP   K  11 54  ? 14.619  -122.125 13.309  1.00 83.27  ? 55  TRP   K O   1 
ATOM   18298 C  CB  . TRP   K  11 54  ? 15.963  -124.300 15.113  1.00 79.53  ? 55  TRP   K CB  1 
ATOM   18299 C  CG  . TRP   K  11 54  ? 16.623  -124.371 16.455  1.00 80.60  ? 55  TRP   K CG  1 
ATOM   18300 C  CD1 . TRP   K  11 54  ? 16.875  -125.488 17.195  1.00 80.29  ? 55  TRP   K CD1 1 
ATOM   18301 C  CD2 . TRP   K  11 54  ? 17.086  -123.261 17.245  1.00 80.43  ? 55  TRP   K CD2 1 
ATOM   18302 N  NE1 . TRP   K  11 54  ? 17.481  -125.156 18.374  1.00 80.70  ? 55  TRP   K NE1 1 
ATOM   18303 C  CE2 . TRP   K  11 54  ? 17.622  -123.798 18.435  1.00 79.66  ? 55  TRP   K CE2 1 
ATOM   18304 C  CE3 . TRP   K  11 54  ? 17.109  -121.874 17.063  1.00 79.12  ? 55  TRP   K CE3 1 
ATOM   18305 C  CZ2 . TRP   K  11 54  ? 18.174  -122.999 19.433  1.00 78.36  ? 55  TRP   K CZ2 1 
ATOM   18306 C  CZ3 . TRP   K  11 54  ? 17.655  -121.084 18.049  1.00 78.50  ? 55  TRP   K CZ3 1 
ATOM   18307 C  CH2 . TRP   K  11 54  ? 18.180  -121.641 19.217  1.00 77.76  ? 55  TRP   K CH2 1 
ATOM   18308 N  N   . GLU   K  11 55  ? 13.284  -123.935 13.091  1.00 81.35  ? 56  GLU   K N   1 
ATOM   18309 C  CA  . GLU   K  11 55  ? 12.788  -123.541 11.745  1.00 84.10  ? 56  GLU   K CA  1 
ATOM   18310 C  C   . GLU   K  11 55  ? 11.659  -122.512 11.878  1.00 83.46  ? 56  GLU   K C   1 
ATOM   18311 O  O   . GLU   K  11 55  ? 11.613  -121.626 11.015  1.00 87.07  ? 56  GLU   K O   1 
ATOM   18312 C  CB  . GLU   K  11 55  ? 12.350  -124.745 10.916  1.00 84.35  ? 56  GLU   K CB  1 
ATOM   18313 C  CG  . GLU   K  11 55  ? 13.514  -125.590 10.439  1.00 85.34  ? 56  GLU   K CG  1 
ATOM   18314 C  CD  . GLU   K  11 55  ? 13.199  -126.507 9.271   1.00 86.06  ? 56  GLU   K CD  1 
ATOM   18315 O  OE1 . GLU   K  11 55  ? 12.139  -126.351 8.655   1.00 88.77  ? 56  GLU   K OE1 1 
ATOM   18316 O  OE2 . GLU   K  11 55  ? 14.021  -127.366 8.973   1.00 88.66  ? 56  GLU   K OE2 1 
ATOM   18317 N  N   . THR   K  11 56  ? 10.777  -122.612 12.881  1.00 83.86  ? 57  THR   K N   1 
ATOM   18318 C  CA  . THR   K  11 56  ? 9.751   -121.559 13.144  1.00 87.13  ? 57  THR   K CA  1 
ATOM   18319 C  C   . THR   K  11 56  ? 10.472  -120.297 13.647  1.00 87.79  ? 57  THR   K C   1 
ATOM   18320 O  O   . THR   K  11 56  ? 9.978   -119.185 13.355  1.00 89.34  ? 57  THR   K O   1 
ATOM   18321 C  CB  . THR   K  11 56  ? 8.631   -121.981 14.108  1.00 88.14  ? 57  THR   K CB  1 
ATOM   18322 O  OG1 . THR   K  11 56  ? 9.175   -122.020 15.427  1.00 90.24  ? 57  THR   K OG1 1 
ATOM   18323 C  CG2 . THR   K  11 56  ? 7.973   -123.300 13.758  1.00 90.34  ? 57  THR   K CG2 1 
ATOM   18324 N  N   . TRP   K  11 57  ? 11.597  -120.461 14.358  1.00 86.71  ? 58  TRP   K N   1 
ATOM   18325 C  CA  . TRP   K  11 57  ? 12.525  -119.359 14.744  1.00 87.02  ? 58  TRP   K CA  1 
ATOM   18326 C  C   . TRP   K  11 57  ? 13.146  -118.744 13.486  1.00 87.14  ? 58  TRP   K C   1 
ATOM   18327 O  O   . TRP   K  11 57  ? 13.145  -117.507 13.378  1.00 90.94  ? 58  TRP   K O   1 
ATOM   18328 C  CB  . TRP   K  11 57  ? 13.617  -119.841 15.709  1.00 83.61  ? 58  TRP   K CB  1 
ATOM   18329 C  CG  . TRP   K  11 57  ? 14.723  -118.849 15.926  1.00 81.60  ? 58  TRP   K CG  1 
ATOM   18330 C  CD1 . TRP   K  11 57  ? 14.749  -117.837 16.841  1.00 81.31  ? 58  TRP   K CD1 1 
ATOM   18331 C  CD2 . TRP   K  11 57  ? 15.973  -118.770 15.214  1.00 79.74  ? 58  TRP   K CD2 1 
ATOM   18332 N  NE1 . TRP   K  11 57  ? 15.923  -117.138 16.751  1.00 79.96  ? 58  TRP   K NE1 1 
ATOM   18333 C  CE2 . TRP   K  11 57  ? 16.695  -117.686 15.762  1.00 78.65  ? 58  TRP   K CE2 1 
ATOM   18334 C  CE3 . TRP   K  11 57  ? 16.552  -119.501 14.169  1.00 79.63  ? 58  TRP   K CE3 1 
ATOM   18335 C  CZ2 . TRP   K  11 57  ? 17.962  -117.324 15.303  1.00 77.51  ? 58  TRP   K CZ2 1 
ATOM   18336 C  CZ3 . TRP   K  11 57  ? 17.804  -119.144 13.716  1.00 78.83  ? 58  TRP   K CZ3 1 
ATOM   18337 C  CH2 . TRP   K  11 57  ? 18.498  -118.069 14.277  1.00 77.33  ? 58  TRP   K CH2 1 
ATOM   18338 N  N   . LEU   K  11 58  ? 13.675  -119.580 12.586  1.00 85.20  ? 59  LEU   K N   1 
ATOM   18339 C  CA  . LEU   K  11 58  ? 14.234  -119.150 11.276  1.00 85.16  ? 59  LEU   K CA  1 
ATOM   18340 C  C   . LEU   K  11 58  ? 13.206  -118.262 10.566  1.00 86.29  ? 59  LEU   K C   1 
ATOM   18341 O  O   . LEU   K  11 58  ? 13.610  -117.223 10.009  1.00 83.56  ? 59  LEU   K O   1 
ATOM   18342 C  CB  . LEU   K  11 58  ? 14.572  -120.382 10.428  1.00 85.24  ? 59  LEU   K CB  1 
ATOM   18343 C  CG  . LEU   K  11 58  ? 14.961  -120.098 8.977   1.00 85.61  ? 59  LEU   K CG  1 
ATOM   18344 C  CD1 . LEU   K  11 58  ? 16.201  -119.223 8.911   1.00 86.10  ? 59  LEU   K CD1 1 
ATOM   18345 C  CD2 . LEU   K  11 58  ? 15.183  -121.389 8.206   1.00 87.53  ? 59  LEU   K CD2 1 
ATOM   18346 N  N   . GLY   K  11 59  ? 11.932  -118.670 10.587  1.00 88.48  ? 60  GLY   K N   1 
ATOM   18347 C  CA  . GLY   K  11 59  ? 10.807  -117.953 9.956   1.00 92.66  ? 60  GLY   K CA  1 
ATOM   18348 C  C   . GLY   K  11 59  ? 10.664  -116.539 10.486  1.00 95.04  ? 60  GLY   K C   1 
ATOM   18349 O  O   . GLY   K  11 59  ? 10.345  -115.634 9.685   1.00 97.39  ? 60  GLY   K O   1 
ATOM   18350 N  N   . SER   K  11 60  ? 10.893  -116.354 11.789  1.00 94.56  ? 61  SER   K N   1 
ATOM   18351 C  CA  . SER   K  11 60  ? 10.872  -115.035 12.473  1.00 95.92  ? 61  SER   K CA  1 
ATOM   18352 C  C   . SER   K  11 60  ? 12.060  -114.184 12.007  1.00 93.22  ? 61  SER   K C   1 
ATOM   18353 O  O   . SER   K  11 60  ? 11.868  -112.973 11.821  1.00 94.96  ? 61  SER   K O   1 
ATOM   18354 C  CB  . SER   K  11 60  ? 10.870  -115.189 13.970  1.00 94.93  ? 61  SER   K CB  1 
ATOM   18355 O  OG  . SER   K  11 60  ? 9.728   -115.905 14.409  1.00 101.37 ? 61  SER   K OG  1 
ATOM   18356 N  N   . GLN   K  11 61  ? 13.236  -114.795 11.825  1.00 92.45  ? 62  GLN   K N   1 
ATOM   18357 C  CA  . GLN   K  11 61  ? 14.468  -114.099 11.360  1.00 94.17  ? 62  GLN   K CA  1 
ATOM   18358 C  C   . GLN   K  11 61  ? 14.272  -113.616 9.919   1.00 94.60  ? 62  GLN   K C   1 
ATOM   18359 O  O   . GLN   K  11 61  ? 14.710  -112.491 9.619   1.00 94.82  ? 62  GLN   K O   1 
ATOM   18360 C  CB  . GLN   K  11 61  ? 15.693  -115.011 11.447  1.00 91.86  ? 62  GLN   K CB  1 
ATOM   18361 C  CG  . GLN   K  11 61  ? 16.029  -115.454 12.863  1.00 94.12  ? 62  GLN   K CG  1 
ATOM   18362 C  CD  . GLN   K  11 61  ? 16.223  -114.286 13.801  1.00 94.69  ? 62  GLN   K CD  1 
ATOM   18363 O  OE1 . GLN   K  11 61  ? 17.070  -113.422 13.581  1.00 96.25  ? 62  GLN   K OE1 1 
ATOM   18364 N  NE2 . GLN   K  11 61  ? 15.432  -114.247 14.861  1.00 98.70  ? 62  GLN   K NE2 1 
ATOM   18365 N  N   . CYS   K  11 62  ? 13.661  -114.447 9.066   1.00 98.92  ? 63  CYS   K N   1 
ATOM   18366 C  CA  . CYS   K  11 62  ? 13.341  -114.131 7.647   1.00 101.55 ? 63  CYS   K CA  1 
ATOM   18367 C  C   . CYS   K  11 62  ? 12.372  -112.945 7.584   1.00 101.73 ? 63  CYS   K C   1 
ATOM   18368 O  O   . CYS   K  11 62  ? 12.554  -112.092 6.692   1.00 107.15 ? 63  CYS   K O   1 
ATOM   18369 C  CB  . CYS   K  11 62  ? 12.766  -115.347 6.931   1.00 102.42 ? 63  CYS   K CB  1 
ATOM   18370 S  SG  . CYS   K  11 62  ? 13.955  -116.711 6.820   1.00 103.29 ? 63  CYS   K SG  1 
ATOM   18371 N  N   . ARG   K  11 63  ? 11.395  -112.886 8.496   1.00 98.95  ? 64  ARG   K N   1 
ATOM   18372 C  CA  . ARG   K  11 63  ? 10.416  -111.766 8.593   1.00 100.08 ? 64  ARG   K CA  1 
ATOM   18373 C  C   . ARG   K  11 63  ? 11.138  -110.474 8.996   1.00 97.09  ? 64  ARG   K C   1 
ATOM   18374 O  O   . ARG   K  11 63  ? 10.789  -109.423 8.449   1.00 100.07 ? 64  ARG   K O   1 
ATOM   18375 C  CB  . ARG   K  11 63  ? 9.302   -112.086 9.596   1.00 102.06 ? 64  ARG   K CB  1 
ATOM   18376 C  CG  . ARG   K  11 63  ? 8.298   -110.959 9.799   1.00 106.00 ? 64  ARG   K CG  1 
ATOM   18377 C  CD  . ARG   K  11 63  ? 7.424   -110.718 8.581   1.00 109.91 ? 64  ARG   K CD  1 
ATOM   18378 N  NE  . ARG   K  11 63  ? 6.493   -109.612 8.790   1.00 115.32 ? 64  ARG   K NE  1 
ATOM   18379 C  CZ  . ARG   K  11 63  ? 6.457   -108.475 8.091   1.00 117.46 ? 64  ARG   K CZ  1 
ATOM   18380 N  NH1 . ARG   K  11 63  ? 7.300   -108.261 7.094   1.00 119.23 ? 64  ARG   K NH1 1 
ATOM   18381 N  NH2 . ARG   K  11 63  ? 5.559   -107.551 8.387   1.00 120.90 ? 64  ARG   K NH2 1 
ATOM   18382 N  N   . LEU   K  11 64  ? 12.088  -110.548 9.932   1.00 93.49  ? 65  LEU   K N   1 
ATOM   18383 C  CA  . LEU   K  11 64  ? 12.859  -109.375 10.428  1.00 93.69  ? 65  LEU   K CA  1 
ATOM   18384 C  C   . LEU   K  11 64  ? 13.786  -108.851 9.326   1.00 95.76  ? 65  LEU   K C   1 
ATOM   18385 O  O   . LEU   K  11 64  ? 14.035  -107.634 9.318   1.00 99.95  ? 65  LEU   K O   1 
ATOM   18386 C  CB  . LEU   K  11 64  ? 13.669  -109.754 11.672  1.00 91.04  ? 65  LEU   K CB  1 
ATOM   18387 C  CG  . LEU   K  11 64  ? 12.909  -109.748 12.997  1.00 91.12  ? 65  LEU   K CG  1 
ATOM   18388 C  CD1 . LEU   K  11 64  ? 13.758  -110.355 14.100  1.00 89.67  ? 65  LEU   K CD1 1 
ATOM   18389 C  CD2 . LEU   K  11 64  ? 12.477  -108.341 13.380  1.00 92.33  ? 65  LEU   K CD2 1 
ATOM   18390 N  N   . HIS   K  11 65  ? 14.297  -109.724 8.452   1.00 96.14  ? 66  HIS   K N   1 
ATOM   18391 C  CA  . HIS   K  11 65  ? 15.148  -109.325 7.298   1.00 98.95  ? 66  HIS   K CA  1 
ATOM   18392 C  C   . HIS   K  11 65  ? 14.329  -108.439 6.351   1.00 100.99 ? 66  HIS   K C   1 
ATOM   18393 O  O   . HIS   K  11 65  ? 14.840  -107.368 5.971   1.00 102.50 ? 66  HIS   K O   1 
ATOM   18394 C  CB  . HIS   K  11 65  ? 15.739  -110.540 6.566   1.00 98.78  ? 66  HIS   K CB  1 
ATOM   18395 C  CG  . HIS   K  11 65  ? 16.449  -110.178 5.301   1.00 100.00 ? 66  HIS   K CG  1 
ATOM   18396 N  ND1 . HIS   K  11 65  ? 17.816  -109.976 5.245   1.00 97.98  ? 66  HIS   K ND1 1 
ATOM   18397 C  CD2 . HIS   K  11 65  ? 15.985  -109.967 4.049   1.00 103.46 ? 66  HIS   K CD2 1 
ATOM   18398 C  CE1 . HIS   K  11 65  ? 18.160  -109.663 4.009   1.00 100.38 ? 66  HIS   K CE1 1 
ATOM   18399 N  NE2 . HIS   K  11 65  ? 17.055  -109.649 3.257   1.00 103.84 ? 66  HIS   K NE2 1 
ATOM   18400 N  N   . GLU   K  11 66  ? 13.111  -108.861 5.992   1.00 102.97 ? 67  GLU   K N   1 
ATOM   18401 C  CA  . GLU   K  11 66  ? 12.277  -108.163 4.975   1.00 106.65 ? 67  GLU   K CA  1 
ATOM   18402 C  C   . GLU   K  11 66  ? 11.693  -106.872 5.572   1.00 107.27 ? 67  GLU   K C   1 
ATOM   18403 O  O   . GLU   K  11 66  ? 11.388  -105.963 4.777   1.00 111.68 ? 67  GLU   K O   1 
ATOM   18404 C  CB  . GLU   K  11 66  ? 11.219  -109.096 4.370   1.00 111.69 ? 67  GLU   K CB  1 
ATOM   18405 C  CG  . GLU   K  11 66  ? 10.091  -109.499 5.303   1.00 112.78 ? 67  GLU   K CG  1 
ATOM   18406 C  CD  . GLU   K  11 66  ? 9.110   -110.487 4.692   1.00 114.76 ? 67  GLU   K CD  1 
ATOM   18407 O  OE1 . GLU   K  11 66  ? 9.552   -111.587 4.296   1.00 109.01 ? 67  GLU   K OE1 1 
ATOM   18408 O  OE2 . GLU   K  11 66  ? 7.909   -110.150 4.600   1.00 118.00 ? 67  GLU   K OE2 1 
ATOM   18409 N  N   . LEU   K  11 67  ? 11.564  -106.772 6.902   1.00 100.27 ? 68  LEU   K N   1 
ATOM   18410 C  CA  . LEU   K  11 67  ? 11.177  -105.508 7.591   1.00 100.88 ? 68  LEU   K CA  1 
ATOM   18411 C  C   . LEU   K  11 67  ? 12.348  -104.523 7.526   1.00 100.72 ? 68  LEU   K C   1 
ATOM   18412 O  O   . LEU   K  11 67  ? 12.106  -103.346 7.213   1.00 102.84 ? 68  LEU   K O   1 
ATOM   18413 C  CB  . LEU   K  11 67  ? 10.781  -105.780 9.048   1.00 97.71  ? 68  LEU   K CB  1 
ATOM   18414 C  CG  . LEU   K  11 67  ? 9.334   -106.214 9.279   1.00 98.71  ? 68  LEU   K CG  1 
ATOM   18415 C  CD1 . LEU   K  11 67  ? 9.155   -106.765 10.685  1.00 97.21  ? 68  LEU   K CD1 1 
ATOM   18416 C  CD2 . LEU   K  11 67  ? 8.366   -105.066 9.036   1.00 101.87 ? 68  LEU   K CD2 1 
ATOM   18417 N  N   . ARG   K  11 68  ? 13.566  -104.995 7.811   1.00 99.65  ? 69  ARG   K N   1 
ATOM   18418 C  CA  . ARG   K  11 68  ? 14.786  -104.148 7.917   1.00 101.42 ? 69  ARG   K CA  1 
ATOM   18419 C  C   . ARG   K  11 68  ? 15.314  -103.785 6.522   1.00 103.17 ? 69  ARG   K C   1 
ATOM   18420 O  O   . ARG   K  11 68  ? 15.761  -102.636 6.361   1.00 105.38 ? 69  ARG   K O   1 
ATOM   18421 C  CB  . ARG   K  11 68  ? 15.873  -104.847 8.742   1.00 100.45 ? 69  ARG   K CB  1 
ATOM   18422 C  CG  . ARG   K  11 68  ? 15.633  -104.813 10.246  1.00 101.87 ? 69  ARG   K CG  1 
ATOM   18423 C  CD  . ARG   K  11 68  ? 16.842  -105.280 11.039  1.00 102.90 ? 69  ARG   K CD  1 
ATOM   18424 N  NE  . ARG   K  11 68  ? 16.937  -106.734 11.148  1.00 103.32 ? 69  ARG   K NE  1 
ATOM   18425 C  CZ  . ARG   K  11 68  ? 16.716  -107.448 12.254  1.00 103.86 ? 69  ARG   K CZ  1 
ATOM   18426 N  NH1 . ARG   K  11 68  ? 16.382  -106.860 13.391  1.00 105.41 ? 69  ARG   K NH1 1 
ATOM   18427 N  NH2 . ARG   K  11 68  ? 16.836  -108.764 12.218  1.00 104.28 ? 69  ARG   K NH2 1 
ATOM   18428 N  N   . GLU   K  11 69  ? 15.274  -104.717 5.562   1.00 102.83 ? 70  GLU   K N   1 
ATOM   18429 C  CA  . GLU   K  11 69  ? 15.906  -104.556 4.222   1.00 105.18 ? 70  GLU   K CA  1 
ATOM   18430 C  C   . GLU   K  11 69  ? 14.859  -104.279 3.133   1.00 105.09 ? 70  GLU   K C   1 
ATOM   18431 O  O   . GLU   K  11 69  ? 15.276  -104.059 1.979   1.00 103.18 ? 70  GLU   K O   1 
ATOM   18432 C  CB  . GLU   K  11 69  ? 16.723  -105.801 3.867   1.00 104.00 ? 70  GLU   K CB  1 
ATOM   18433 C  CG  . GLU   K  11 69  ? 17.783  -106.152 4.895   1.00 104.55 ? 70  GLU   K CG  1 
ATOM   18434 C  CD  . GLU   K  11 69  ? 18.664  -104.990 5.318   1.00 108.58 ? 70  GLU   K CD  1 
ATOM   18435 O  OE1 . GLU   K  11 69  ? 19.002  -104.160 4.448   1.00 110.31 ? 70  GLU   K OE1 1 
ATOM   18436 O  OE2 . GLU   K  11 69  ? 18.999  -104.910 6.519   1.00 112.53 ? 70  GLU   K OE2 1 
ATOM   18437 N  N   . LYS   K  11 70  ? 13.564  -104.278 3.472   1.00 107.26 ? 71  LYS   K N   1 
ATOM   18438 C  CA  . LYS   K  11 70  ? 12.455  -103.986 2.523   1.00 114.10 ? 71  LYS   K CA  1 
ATOM   18439 C  C   . LYS   K  11 70  ? 12.627  -104.850 1.267   1.00 114.88 ? 71  LYS   K C   1 
ATOM   18440 O  O   . LYS   K  11 70  ? 12.607  -104.292 0.157   1.00 116.80 ? 71  LYS   K O   1 
ATOM   18441 C  CB  . LYS   K  11 70  ? 12.444  -102.495 2.166   1.00 118.67 ? 71  LYS   K CB  1 
ATOM   18442 C  CG  . LYS   K  11 70  ? 12.003  -101.555 3.279   1.00 121.89 ? 71  LYS   K CG  1 
ATOM   18443 C  CD  . LYS   K  11 70  ? 12.122  -100.093 2.906   1.00 127.42 ? 71  LYS   K CD  1 
ATOM   18444 C  CE  . LYS   K  11 70  ? 11.382  -99.176  3.858   1.00 131.94 ? 71  LYS   K CE  1 
ATOM   18445 N  NZ  . LYS   K  11 70  ? 11.310  -97.786  3.345   1.00 136.14 ? 71  LYS   K NZ  1 
ATOM   18446 N  N   . GLU   K  11 71  ? 12.807  -106.160 1.446   1.00 114.08 ? 72  GLU   K N   1 
ATOM   18447 C  CA  . GLU   K  11 71  ? 13.126  -107.129 0.361   1.00 119.21 ? 72  GLU   K CA  1 
ATOM   18448 C  C   . GLU   K  11 71  ? 13.126  -108.548 0.940   1.00 117.51 ? 72  GLU   K C   1 
ATOM   18449 O  O   . GLU   K  11 71  ? 13.706  -108.732 2.026   1.00 119.47 ? 72  GLU   K O   1 
ATOM   18450 C  CB  . GLU   K  11 71  ? 14.491  -106.801 -0.251  1.00 122.69 ? 72  GLU   K CB  1 
ATOM   18451 C  CG  . GLU   K  11 71  ? 14.875  -107.691 -1.420  1.00 127.14 ? 72  GLU   K CG  1 
ATOM   18452 C  CD  . GLU   K  11 71  ? 16.220  -107.358 -2.044  1.00 131.16 ? 72  GLU   K CD  1 
ATOM   18453 O  OE1 . GLU   K  11 71  ? 16.394  -106.207 -2.487  1.00 136.48 ? 72  GLU   K OE1 1 
ATOM   18454 O  OE2 . GLU   K  11 71  ? 17.093  -108.248 -2.077  1.00 135.78 ? 72  GLU   K OE2 1 
ATOM   18455 N  N   . ARG   K  11 72  ? 12.528  -109.514 0.236   1.00 117.48 ? 73  ARG   K N   1 
ATOM   18456 C  CA  . ARG   K  11 72  ? 12.439  -110.926 0.699   1.00 114.33 ? 73  ARG   K CA  1 
ATOM   18457 C  C   . ARG   K  11 72  ? 13.849  -111.526 0.753   1.00 105.73 ? 73  ARG   K C   1 
ATOM   18458 O  O   . ARG   K  11 72  ? 14.648  -111.259 -0.168  1.00 102.32 ? 73  ARG   K O   1 
ATOM   18459 C  CB  . ARG   K  11 72  ? 11.503  -111.757 -0.185  1.00 118.00 ? 73  ARG   K CB  1 
ATOM   18460 C  CG  . ARG   K  11 72  ? 10.123  -111.964 0.424   1.00 122.70 ? 73  ARG   K CG  1 
ATOM   18461 C  CD  . ARG   K  11 72  ? 9.107   -112.520 -0.554  1.00 127.78 ? 73  ARG   K CD  1 
ATOM   18462 N  NE  . ARG   K  11 72  ? 9.693   -113.486 -1.479  1.00 132.50 ? 73  ARG   K NE  1 
ATOM   18463 C  CZ  . ARG   K  11 72  ? 9.966   -113.265 -2.766  1.00 141.77 ? 73  ARG   K CZ  1 
ATOM   18464 N  NH1 . ARG   K  11 72  ? 9.704   -112.096 -3.331  1.00 148.22 ? 73  ARG   K NH1 1 
ATOM   18465 N  NH2 . ARG   K  11 72  ? 10.501  -114.232 -3.494  1.00 140.74 ? 73  ARG   K NH2 1 
ATOM   18466 N  N   . ILE   K  11 73  ? 14.134  -112.292 1.809   1.00 98.05  ? 74  ILE   K N   1 
ATOM   18467 C  CA  . ILE   K  11 73  ? 15.469  -112.911 2.058   1.00 95.81  ? 74  ILE   K CA  1 
ATOM   18468 C  C   . ILE   K  11 73  ? 15.757  -113.941 0.958   1.00 93.29  ? 74  ILE   K C   1 
ATOM   18469 O  O   . ILE   K  11 73  ? 14.809  -114.626 0.515   1.00 91.73  ? 74  ILE   K O   1 
ATOM   18470 C  CB  . ILE   K  11 73  ? 15.546  -113.534 3.468   1.00 92.67  ? 74  ILE   K CB  1 
ATOM   18471 C  CG1 . ILE   K  11 73  ? 16.980  -113.951 3.805   1.00 92.40  ? 74  ILE   K CG1 1 
ATOM   18472 C  CG2 . ILE   K  11 73  ? 14.571  -114.694 3.621   1.00 93.06  ? 74  ILE   K CG2 1 
ATOM   18473 C  CD1 . ILE   K  11 73  ? 17.251  -114.125 5.281   1.00 91.01  ? 74  ILE   K CD1 1 
ATOM   18474 N  N   . SER   K  11 74  ? 17.023  -114.031 0.536   1.00 92.89  ? 75  SER   K N   1 
ATOM   18475 C  CA  . SER   K  11 74  ? 17.529  -115.033 -0.439  1.00 93.35  ? 75  SER   K CA  1 
ATOM   18476 C  C   . SER   K  11 74  ? 17.557  -116.406 0.233   1.00 91.87  ? 75  SER   K C   1 
ATOM   18477 O  O   . SER   K  11 74  ? 17.786  -116.460 1.459   1.00 87.06  ? 75  SER   K O   1 
ATOM   18478 C  CB  . SER   K  11 74  ? 18.892  -114.665 -0.974  1.00 89.89  ? 75  SER   K CB  1 
ATOM   18479 O  OG  . SER   K  11 74  ? 19.870  -114.686 0.053   1.00 85.24  ? 75  SER   K OG  1 
ATOM   18480 N  N   . VAL   K  11 75  ? 17.342  -117.466 -0.549  1.00 95.15  ? 76  VAL   K N   1 
ATOM   18481 C  CA  . VAL   K  11 75  ? 17.342  -118.878 -0.063  1.00 93.87  ? 76  VAL   K CA  1 
ATOM   18482 C  C   . VAL   K  11 75  ? 18.714  -119.158 0.562   1.00 90.03  ? 76  VAL   K C   1 
ATOM   18483 O  O   . VAL   K  11 75  ? 18.758  -119.861 1.588   1.00 87.92  ? 76  VAL   K O   1 
ATOM   18484 C  CB  . VAL   K  11 75  ? 17.003  -119.877 -1.188  1.00 97.99  ? 76  VAL   K CB  1 
ATOM   18485 C  CG1 . VAL   K  11 75  ? 16.932  -121.305 -0.669  1.00 98.63  ? 76  VAL   K CG1 1 
ATOM   18486 C  CG2 . VAL   K  11 75  ? 15.707  -119.519 -1.906  1.00 101.86 ? 76  VAL   K CG2 1 
ATOM   18487 N  N   . ALA   K  11 76  ? 19.781  -118.600 -0.019  1.00 91.28  ? 77  ALA   K N   1 
ATOM   18488 C  CA  . ALA   K  11 76  ? 21.180  -118.753 0.448   1.00 92.36  ? 77  ALA   K CA  1 
ATOM   18489 C  C   . ALA   K  11 76  ? 21.326  -118.171 1.859   1.00 91.61  ? 77  ALA   K C   1 
ATOM   18490 O  O   . ALA   K  11 76  ? 21.883  -118.870 2.728   1.00 91.42  ? 77  ALA   K O   1 
ATOM   18491 C  CB  . ALA   K  11 76  ? 22.132  -118.094 -0.521  1.00 93.43  ? 77  ALA   K CB  1 
ATOM   18492 N  N   . ALA   K  11 77  ? 20.844  -116.942 2.074   1.00 92.33  ? 78  ALA   K N   1 
ATOM   18493 C  CA  . ALA   K  11 77  ? 20.969  -116.195 3.348   1.00 89.73  ? 78  ALA   K CA  1 
ATOM   18494 C  C   . ALA   K  11 77  ? 20.116  -116.868 4.430   1.00 87.02  ? 78  ALA   K C   1 
ATOM   18495 O  O   . ALA   K  11 77  ? 20.612  -117.004 5.565   1.00 86.42  ? 78  ALA   K O   1 
ATOM   18496 C  CB  . ALA   K  11 77  ? 20.586  -114.748 3.147   1.00 91.21  ? 78  ALA   K CB  1 
ATOM   18497 N  N   . ALA   K  11 78  ? 18.894  -117.290 4.089   1.00 86.07  ? 79  ALA   K N   1 
ATOM   18498 C  CA  . ALA   K  11 78  ? 17.955  -117.969 5.012   1.00 85.76  ? 79  ALA   K CA  1 
ATOM   18499 C  C   . ALA   K  11 78  ? 18.596  -119.266 5.524   1.00 85.86  ? 79  ALA   K C   1 
ATOM   18500 O  O   . ALA   K  11 78  ? 18.660  -119.460 6.756   1.00 81.79  ? 79  ALA   K O   1 
ATOM   18501 C  CB  . ALA   K  11 78  ? 16.642  -118.234 4.319   1.00 86.49  ? 79  ALA   K CB  1 
ATOM   18502 N  N   . SER   K  11 79  ? 19.075  -120.112 4.607   1.00 86.50  ? 80  SER   K N   1 
ATOM   18503 C  CA  . SER   K  11 79  ? 19.739  -121.406 4.914   1.00 86.71  ? 80  SER   K CA  1 
ATOM   18504 C  C   . SER   K  11 79  ? 20.959  -121.166 5.808   1.00 86.65  ? 80  SER   K C   1 
ATOM   18505 O  O   . SER   K  11 79  ? 21.214  -122.008 6.689   1.00 88.25  ? 80  SER   K O   1 
ATOM   18506 C  CB  . SER   K  11 79  ? 20.130  -122.139 3.658   1.00 88.05  ? 80  SER   K CB  1 
ATOM   18507 O  OG  . SER   K  11 79  ? 21.103  -121.406 2.927   1.00 90.79  ? 80  SER   K OG  1 
ATOM   18508 N  N   . LYS   K  11 80  ? 21.687  -120.068 5.587   1.00 85.79  ? 81  LYS   K N   1 
ATOM   18509 C  CA  . LYS   K  11 80  ? 22.958  -119.780 6.302   1.00 83.19  ? 81  LYS   K CA  1 
ATOM   18510 C  C   . LYS   K  11 80  ? 22.666  -119.237 7.703   1.00 82.13  ? 81  LYS   K C   1 
ATOM   18511 O  O   . LYS   K  11 80  ? 23.535  -119.412 8.577   1.00 79.23  ? 81  LYS   K O   1 
ATOM   18512 C  CB  . LYS   K  11 80  ? 23.844  -118.805 5.528   1.00 84.57  ? 81  LYS   K CB  1 
ATOM   18513 C  CG  . LYS   K  11 80  ? 25.319  -118.902 5.888   1.00 84.03  ? 81  LYS   K CG  1 
ATOM   18514 C  CD  . LYS   K  11 80  ? 26.227  -118.312 4.846   1.00 86.54  ? 81  LYS   K CD  1 
ATOM   18515 C  CE  . LYS   K  11 80  ? 27.669  -118.737 5.009   1.00 87.81  ? 81  LYS   K CE  1 
ATOM   18516 N  NZ  . LYS   K  11 80  ? 28.527  -118.120 3.971   1.00 90.99  ? 81  LYS   K NZ  1 
ATOM   18517 N  N   . ILE   K  11 81  ? 21.514  -118.590 7.911   1.00 82.82  ? 82  ILE   K N   1 
ATOM   18518 C  CA  . ILE   K  11 81  ? 21.049  -118.199 9.275   1.00 83.76  ? 82  ILE   K CA  1 
ATOM   18519 C  C   . ILE   K  11 81  ? 20.925  -119.481 10.103  1.00 83.24  ? 82  ILE   K C   1 
ATOM   18520 O  O   . ILE   K  11 81  ? 21.495  -119.514 11.211  1.00 85.18  ? 82  ILE   K O   1 
ATOM   18521 C  CB  . ILE   K  11 81  ? 19.732  -117.394 9.243   1.00 84.23  ? 82  ILE   K CB  1 
ATOM   18522 C  CG1 . ILE   K  11 81  ? 19.977  -115.940 8.831   1.00 84.52  ? 82  ILE   K CG1 1 
ATOM   18523 C  CG2 . ILE   K  11 81  ? 19.005  -117.482 10.580  1.00 85.52  ? 82  ILE   K CG2 1 
ATOM   18524 C  CD1 . ILE   K  11 81  ? 18.714  -115.138 8.609   1.00 87.07  ? 82  ILE   K CD1 1 
ATOM   18525 N  N   . LEU   K  11 82  ? 20.231  -120.493 9.566   1.00 83.42  ? 83  LEU   K N   1 
ATOM   18526 C  CA  . LEU   K  11 82  ? 19.972  -121.793 10.246  1.00 81.93  ? 83  LEU   K CA  1 
ATOM   18527 C  C   . LEU   K  11 82  ? 21.297  -122.538 10.456  1.00 76.93  ? 83  LEU   K C   1 
ATOM   18528 O  O   . LEU   K  11 82  ? 21.518  -123.005 11.582  1.00 76.49  ? 83  LEU   K O   1 
ATOM   18529 C  CB  . LEU   K  11 82  ? 18.984  -122.624 9.420   1.00 81.90  ? 83  LEU   K CB  1 
ATOM   18530 C  CG  . LEU   K  11 82  ? 18.569  -123.964 10.028  1.00 84.24  ? 83  LEU   K CG  1 
ATOM   18531 C  CD1 . LEU   K  11 82  ? 17.821  -123.771 11.339  1.00 84.39  ? 83  LEU   K CD1 1 
ATOM   18532 C  CD2 . LEU   K  11 82  ? 17.723  -124.768 9.049   1.00 85.57  ? 83  LEU   K CD2 1 
ATOM   18533 N  N   . SER   K  11 83  ? 22.144  -122.634 9.424   1.00 77.22  ? 84  SER   K N   1 
ATOM   18534 C  CA  . SER   K  11 83  ? 23.426  -123.393 9.462   1.00 77.33  ? 84  SER   K CA  1 
ATOM   18535 C  C   . SER   K  11 83  ? 24.397  -122.754 10.464  1.00 78.08  ? 84  SER   K C   1 
ATOM   18536 O  O   . SER   K  11 83  ? 25.115  -123.508 11.144  1.00 77.52  ? 84  SER   K O   1 
ATOM   18537 C  CB  . SER   K  11 83  ? 24.057  -123.505 8.099   1.00 78.17  ? 84  SER   K CB  1 
ATOM   18538 O  OG  . SER   K  11 83  ? 24.686  -122.288 7.731   1.00 77.52  ? 84  SER   K OG  1 
ATOM   18539 N  N   . ASN   K  11 84  ? 24.438  -121.419 10.531  1.00 79.40  ? 85  ASN   K N   1 
ATOM   18540 C  CA  . ASN   K  11 84  ? 25.300  -120.661 11.480  1.00 79.86  ? 85  ASN   K CA  1 
ATOM   18541 C  C   . ASN   K  11 84  ? 24.762  -120.835 12.905  1.00 78.30  ? 85  ASN   K C   1 
ATOM   18542 O  O   . ASN   K  11 84  ? 25.589  -120.859 13.835  1.00 78.72  ? 85  ASN   K O   1 
ATOM   18543 C  CB  . ASN   K  11 84  ? 25.418  -119.177 11.112  1.00 81.01  ? 85  ASN   K CB  1 
ATOM   18544 C  CG  . ASN   K  11 84  ? 26.347  -118.885 9.949   1.00 82.61  ? 85  ASN   K CG  1 
ATOM   18545 O  OD1 . ASN   K  11 84  ? 26.453  -117.739 9.520   1.00 84.71  ? 85  ASN   K OD1 1 
ATOM   18546 N  ND2 . ASN   K  11 84  ? 27.033  -119.891 9.425   1.00 85.75  ? 85  ASN   K ND2 1 
ATOM   18547 N  N   . LEU   K  11 85  ? 23.438  -120.948 13.067  1.00 78.14  ? 86  LEU   K N   1 
ATOM   18548 C  CA  . LEU   K  11 85  ? 22.775  -121.143 14.386  1.00 79.42  ? 86  LEU   K CA  1 
ATOM   18549 C  C   . LEU   K  11 85  ? 23.177  -122.510 14.950  1.00 79.60  ? 86  LEU   K C   1 
ATOM   18550 O  O   . LEU   K  11 85  ? 23.655  -122.550 16.094  1.00 81.95  ? 86  LEU   K O   1 
ATOM   18551 C  CB  . LEU   K  11 85  ? 21.254  -121.024 14.221  1.00 78.65  ? 86  LEU   K CB  1 
ATOM   18552 C  CG  . LEU   K  11 85  ? 20.405  -121.194 15.486  1.00 79.38  ? 86  LEU   K CG  1 
ATOM   18553 C  CD1 . LEU   K  11 85  ? 20.240  -122.661 15.863  1.00 79.14  ? 86  LEU   K CD1 1 
ATOM   18554 C  CD2 . LEU   K  11 85  ? 20.965  -120.398 16.654  1.00 77.65  ? 86  LEU   K CD2 1 
ATOM   18555 N  N   . VAL   K  11 86  ? 22.989  -123.584 14.175  1.00 82.28  ? 87  VAL   K N   1 
ATOM   18556 C  CA  . VAL   K  11 86  ? 23.246  -124.991 14.615  1.00 83.09  ? 87  VAL   K CA  1 
ATOM   18557 C  C   . VAL   K  11 86  ? 24.753  -125.204 14.811  1.00 82.67  ? 87  VAL   K C   1 
ATOM   18558 O  O   . VAL   K  11 86  ? 25.107  -126.021 15.682  1.00 83.39  ? 87  VAL   K O   1 
ATOM   18559 C  CB  . VAL   K  11 86  ? 22.650  -126.038 13.650  1.00 83.44  ? 87  VAL   K CB  1 
ATOM   18560 C  CG1 . VAL   K  11 86  ? 21.133  -125.940 13.581  1.00 84.19  ? 87  VAL   K CG1 1 
ATOM   18561 C  CG2 . VAL   K  11 86  ? 23.257  -125.977 12.255  1.00 84.33  ? 87  VAL   K CG2 1 
ATOM   18562 N  N   . TYR   K  11 87  ? 25.608  -124.512 14.047  1.00 80.58  ? 88  TYR   K N   1 
ATOM   18563 C  CA  . TYR   K  11 87  ? 27.087  -124.614 14.172  1.00 80.04  ? 88  TYR   K CA  1 
ATOM   18564 C  C   . TYR   K  11 87  ? 27.532  -124.065 15.531  1.00 79.50  ? 88  TYR   K C   1 
ATOM   18565 O  O   . TYR   K  11 87  ? 28.540  -124.553 16.074  1.00 79.57  ? 88  TYR   K O   1 
ATOM   18566 C  CB  . TYR   K  11 87  ? 27.833  -123.876 13.059  1.00 79.36  ? 88  TYR   K CB  1 
ATOM   18567 C  CG  . TYR   K  11 87  ? 29.322  -124.092 13.135  1.00 79.75  ? 88  TYR   K CG  1 
ATOM   18568 C  CD1 . TYR   K  11 87  ? 29.879  -125.307 12.774  1.00 80.62  ? 88  TYR   K CD1 1 
ATOM   18569 C  CD2 . TYR   K  11 87  ? 30.170  -123.113 13.627  1.00 79.74  ? 88  TYR   K CD2 1 
ATOM   18570 C  CE1 . TYR   K  11 87  ? 31.243  -125.532 12.862  1.00 82.86  ? 88  TYR   K CE1 1 
ATOM   18571 C  CE2 . TYR   K  11 87  ? 31.536  -123.320 13.721  1.00 81.73  ? 88  TYR   K CE2 1 
ATOM   18572 C  CZ  . TYR   K  11 87  ? 32.076  -124.534 13.335  1.00 83.57  ? 88  TYR   K CZ  1 
ATOM   18573 O  OH  . TYR   K  11 87  ? 33.422  -124.740 13.432  1.00 88.56  ? 88  TYR   K OH  1 
ATOM   18574 N  N   . GLN   K  11 88  ? 26.813  -123.068 16.052  1.00 81.25  ? 89  GLN   K N   1 
ATOM   18575 C  CA  . GLN   K  11 88  ? 27.065  -122.490 17.398  1.00 84.46  ? 89  GLN   K CA  1 
ATOM   18576 C  C   . GLN   K  11 88  ? 26.813  -123.559 18.464  1.00 83.53  ? 89  GLN   K C   1 
ATOM   18577 O  O   . GLN   K  11 88  ? 27.515  -123.538 19.484  1.00 87.55  ? 89  GLN   K O   1 
ATOM   18578 C  CB  . GLN   K  11 88  ? 26.195  -121.256 17.646  1.00 88.47  ? 89  GLN   K CB  1 
ATOM   18579 C  CG  . GLN   K  11 88  ? 26.748  -119.988 17.016  1.00 94.02  ? 89  GLN   K CG  1 
ATOM   18580 C  CD  . GLN   K  11 88  ? 26.468  -118.783 17.878  1.00 102.33 ? 89  GLN   K CD  1 
ATOM   18581 O  OE1 . GLN   K  11 88  ? 25.320  -118.377 18.052  1.00 109.41 ? 89  GLN   K OE1 1 
ATOM   18582 N  NE2 . GLN   K  11 88  ? 27.522  -118.206 18.434  1.00 109.37 ? 89  GLN   K NE2 1 
ATOM   18583 N  N   . TYR   K  11 89  ? 25.857  -124.460 18.228  1.00 81.93  ? 90  TYR   K N   1 
ATOM   18584 C  CA  . TYR   K  11 89  ? 25.459  -125.541 19.168  1.00 83.55  ? 90  TYR   K CA  1 
ATOM   18585 C  C   . TYR   K  11 89  ? 26.224  -126.840 18.872  1.00 83.22  ? 90  TYR   K C   1 
ATOM   18586 O  O   . TYR   K  11 89  ? 25.965  -127.837 19.573  1.00 79.64  ? 90  TYR   K O   1 
ATOM   18587 C  CB  . TYR   K  11 89  ? 23.951  -125.786 19.080  1.00 82.57  ? 90  TYR   K CB  1 
ATOM   18588 C  CG  . TYR   K  11 89  ? 23.097  -124.757 19.774  1.00 79.69  ? 90  TYR   K CG  1 
ATOM   18589 C  CD1 . TYR   K  11 89  ? 22.674  -124.947 21.078  1.00 78.51  ? 90  TYR   K CD1 1 
ATOM   18590 C  CD2 . TYR   K  11 89  ? 22.695  -123.604 19.125  1.00 79.39  ? 90  TYR   K CD2 1 
ATOM   18591 C  CE1 . TYR   K  11 89  ? 21.880  -124.016 21.724  1.00 77.44  ? 90  TYR   K CE1 1 
ATOM   18592 C  CE2 . TYR   K  11 89  ? 21.899  -122.662 19.755  1.00 79.31  ? 90  TYR   K CE2 1 
ATOM   18593 C  CZ  . TYR   K  11 89  ? 21.491  -122.870 21.061  1.00 78.02  ? 90  TYR   K CZ  1 
ATOM   18594 O  OH  . TYR   K  11 89  ? 20.708  -121.964 21.713  1.00 81.47  ? 90  TYR   K OH  1 
ATOM   18595 N  N   . LYS   K  11 90  ? 27.131  -126.841 17.886  1.00 86.49  ? 91  LYS   K N   1 
ATOM   18596 C  CA  . LYS   K  11 90  ? 27.812  -128.074 17.399  1.00 86.94  ? 91  LYS   K CA  1 
ATOM   18597 C  C   . LYS   K  11 90  ? 28.476  -128.785 18.585  1.00 87.87  ? 91  LYS   K C   1 
ATOM   18598 O  O   . LYS   K  11 90  ? 29.286  -128.145 19.277  1.00 87.34  ? 91  LYS   K O   1 
ATOM   18599 C  CB  . LYS   K  11 90  ? 28.848  -127.769 16.313  1.00 88.93  ? 91  LYS   K CB  1 
ATOM   18600 C  CG  . LYS   K  11 90  ? 29.418  -129.007 15.630  1.00 89.33  ? 91  LYS   K CG  1 
ATOM   18601 C  CD  . LYS   K  11 90  ? 30.468  -128.712 14.583  1.00 90.71  ? 91  LYS   K CD  1 
ATOM   18602 C  CE  . LYS   K  11 90  ? 31.240  -129.943 14.158  1.00 90.60  ? 91  LYS   K CE  1 
ATOM   18603 N  NZ  . LYS   K  11 90  ? 30.383  -130.900 13.420  1.00 93.28  ? 91  LYS   K NZ  1 
ATOM   18604 N  N   . GLY   K  11 91  ? 28.127  -130.058 18.799  1.00 89.43  ? 92  GLY   K N   1 
ATOM   18605 C  CA  . GLY   K  11 91  ? 28.631  -130.897 19.905  1.00 90.66  ? 92  GLY   K CA  1 
ATOM   18606 C  C   . GLY   K  11 91  ? 27.634  -131.015 21.049  1.00 87.92  ? 92  GLY   K C   1 
ATOM   18607 O  O   . GLY   K  11 91  ? 27.732  -131.995 21.805  1.00 89.68  ? 92  GLY   K O   1 
ATOM   18608 N  N   . ALA   K  11 92  ? 26.703  -130.062 21.176  1.00 86.86  ? 93  ALA   K N   1 
ATOM   18609 C  CA  . ALA   K  11 92  ? 25.697  -129.986 22.265  1.00 85.15  ? 93  ALA   K CA  1 
ATOM   18610 C  C   . ALA   K  11 92  ? 24.699  -131.148 22.167  1.00 84.48  ? 93  ALA   K C   1 
ATOM   18611 O  O   . ALA   K  11 92  ? 24.100  -131.487 23.202  1.00 82.85  ? 93  ALA   K O   1 
ATOM   18612 C  CB  . ALA   K  11 92  ? 24.977  -128.662 22.219  1.00 83.58  ? 93  ALA   K CB  1 
ATOM   18613 N  N   . GLY   K  11 93  ? 24.498  -131.707 20.969  1.00 86.11  ? 94  GLY   K N   1 
ATOM   18614 C  CA  . GLY   K  11 93  ? 23.655  -132.898 20.755  1.00 90.60  ? 94  GLY   K CA  1 
ATOM   18615 C  C   . GLY   K  11 93  ? 22.375  -132.599 19.993  1.00 91.89  ? 94  GLY   K C   1 
ATOM   18616 O  O   . GLY   K  11 93  ? 21.498  -133.483 19.980  1.00 97.35  ? 94  GLY   K O   1 
ATOM   18617 N  N   . LEU   K  11 94  ? 22.251  -131.416 19.380  1.00 90.75  ? 95  LEU   K N   1 
ATOM   18618 C  CA  . LEU   K  11 94  ? 21.138  -131.111 18.439  1.00 90.02  ? 95  LEU   K CA  1 
ATOM   18619 C  C   . LEU   K  11 94  ? 21.186  -132.130 17.298  1.00 89.08  ? 95  LEU   K C   1 
ATOM   18620 O  O   . LEU   K  11 94  ? 22.290  -132.349 16.760  1.00 85.35  ? 95  LEU   K O   1 
ATOM   18621 C  CB  . LEU   K  11 94  ? 21.275  -129.691 17.880  1.00 90.63  ? 95  LEU   K CB  1 
ATOM   18622 C  CG  . LEU   K  11 94  ? 20.791  -128.552 18.775  1.00 89.90  ? 95  LEU   K CG  1 
ATOM   18623 C  CD1 . LEU   K  11 94  ? 21.029  -127.214 18.096  1.00 87.44  ? 95  LEU   K CD1 1 
ATOM   18624 C  CD2 . LEU   K  11 94  ? 19.319  -128.704 19.126  1.00 92.16  ? 95  LEU   K CD2 1 
ATOM   18625 N  N   . SER   K  11 95  ? 20.042  -132.729 16.959  1.00 89.57  ? 96  SER   K N   1 
ATOM   18626 C  CA  . SER   K  11 95  ? 19.895  -133.691 15.836  1.00 91.04  ? 96  SER   K CA  1 
ATOM   18627 C  C   . SER   K  11 95  ? 18.832  -133.170 14.859  1.00 89.46  ? 96  SER   K C   1 
ATOM   18628 O  O   . SER   K  11 95  ? 17.629  -133.252 15.190  1.00 89.01  ? 96  SER   K O   1 
ATOM   18629 C  CB  . SER   K  11 95  ? 19.581  -135.079 16.349  1.00 92.93  ? 96  SER   K CB  1 
ATOM   18630 O  OG  . SER   K  11 95  ? 19.115  -135.923 15.304  1.00 94.12  ? 96  SER   K OG  1 
ATOM   18631 N  N   . MET   K  11 96  ? 19.267  -132.626 13.717  1.00 87.30  ? 97  MET   K N   1 
ATOM   18632 C  CA  . MET   K  11 96  ? 18.375  -132.205 12.602  1.00 89.68  ? 97  MET   K CA  1 
ATOM   18633 C  C   . MET   K  11 96  ? 19.069  -132.414 11.256  1.00 90.93  ? 97  MET   K C   1 
ATOM   18634 O  O   . MET   K  11 96  ? 20.283  -132.138 11.157  1.00 87.25  ? 97  MET   K O   1 
ATOM   18635 C  CB  . MET   K  11 96  ? 17.986  -130.726 12.642  1.00 89.92  ? 97  MET   K CB  1 
ATOM   18636 C  CG  . MET   K  11 96  ? 18.250  -130.015 13.930  1.00 92.16  ? 97  MET   K CG  1 
ATOM   18637 S  SD  . MET   K  11 96  ? 18.202  -128.247 13.583  1.00 95.43  ? 97  MET   K SD  1 
ATOM   18638 C  CE  . MET   K  11 96  ? 17.495  -127.665 15.116  1.00 90.65  ? 97  MET   K CE  1 
ATOM   18639 N  N   . GLY   K  11 97  ? 18.281  -132.820 10.257  1.00 92.38  ? 98  GLY   K N   1 
ATOM   18640 C  CA  . GLY   K  11 97  ? 18.621  -132.773 8.824   1.00 92.15  ? 98  GLY   K CA  1 
ATOM   18641 C  C   . GLY   K  11 97  ? 17.495  -132.114 8.052   1.00 92.54  ? 98  GLY   K C   1 
ATOM   18642 O  O   . GLY   K  11 97  ? 16.398  -132.689 8.000   1.00 96.07  ? 98  GLY   K O   1 
ATOM   18643 N  N   . THR   K  11 98  ? 17.728  -130.924 7.504   1.00 92.35  ? 99  THR   K N   1 
ATOM   18644 C  CA  . THR   K  11 98  ? 16.678  -130.139 6.808   1.00 93.97  ? 99  THR   K CA  1 
ATOM   18645 C  C   . THR   K  11 98  ? 17.154  -129.722 5.421   1.00 92.11  ? 99  THR   K C   1 
ATOM   18646 O  O   . THR   K  11 98  ? 18.373  -129.756 5.148   1.00 88.58  ? 99  THR   K O   1 
ATOM   18647 C  CB  . THR   K  11 98  ? 16.268  -128.892 7.599   1.00 94.73  ? 99  THR   K CB  1 
ATOM   18648 O  OG1 . THR   K  11 98  ? 17.437  -128.098 7.810   1.00 92.25  ? 99  THR   K OG1 1 
ATOM   18649 C  CG2 . THR   K  11 98  ? 15.614  -129.226 8.924   1.00 96.20  ? 99  THR   K CG2 1 
ATOM   18650 N  N   . MET   K  11 99  ? 16.183  -129.334 4.601   1.00 93.81  ? 100 MET   K N   1 
ATOM   18651 C  CA  . MET   K  11 99  ? 16.370  -128.772 3.246   1.00 96.01  ? 100 MET   K CA  1 
ATOM   18652 C  C   . MET   K  11 99  ? 15.593  -127.458 3.183   1.00 92.95  ? 100 MET   K C   1 
ATOM   18653 O  O   . MET   K  11 99  ? 14.377  -127.480 3.474   1.00 86.39  ? 100 MET   K O   1 
ATOM   18654 C  CB  . MET   K  11 99  ? 15.832  -129.729 2.182   1.00 100.76 ? 100 MET   K CB  1 
ATOM   18655 C  CG  . MET   K  11 99  ? 15.713  -131.172 2.661   1.00 103.01 ? 100 MET   K CG  1 
ATOM   18656 S  SD  . MET   K  11 99  ? 15.837  -132.326 1.301   1.00 109.24 ? 100 MET   K SD  1 
ATOM   18657 C  CE  . MET   K  11 99  ? 17.284  -131.623 0.519   1.00 108.30 ? 100 MET   K CE  1 
ATOM   18658 N  N   . ILE   K  11 100 ? 16.275  -126.360 2.860   1.00 93.44  ? 101 ILE   K N   1 
ATOM   18659 C  CA  . ILE   K  11 100 ? 15.637  -125.028 2.662   1.00 94.74  ? 101 ILE   K CA  1 
ATOM   18660 C  C   . ILE   K  11 100 ? 15.386  -124.851 1.165   1.00 95.04  ? 101 ILE   K C   1 
ATOM   18661 O  O   . ILE   K  11 100 ? 16.369  -124.798 0.401   1.00 92.42  ? 101 ILE   K O   1 
ATOM   18662 C  CB  . ILE   K  11 100 ? 16.497  -123.897 3.254   1.00 95.13  ? 101 ILE   K CB  1 
ATOM   18663 C  CG1 . ILE   K  11 100 ? 16.798  -124.118 4.741   1.00 92.76  ? 101 ILE   K CG1 1 
ATOM   18664 C  CG2 . ILE   K  11 100 ? 15.841  -122.550 2.997   1.00 98.26  ? 101 ILE   K CG2 1 
ATOM   18665 C  CD1 . ILE   K  11 100 ? 15.658  -124.725 5.535   1.00 92.92  ? 101 ILE   K CD1 1 
ATOM   18666 N  N   . CYS   K  11 101 ? 14.110  -124.779 0.781   1.00 97.71  ? 102 CYS   K N   1 
ATOM   18667 C  CA  . CYS   K  11 101 ? 13.636  -124.747 -0.626  1.00 103.15 ? 102 CYS   K CA  1 
ATOM   18668 C  C   . CYS   K  11 101 ? 12.871  -123.443 -0.866  1.00 104.84 ? 102 CYS   K C   1 
ATOM   18669 O  O   . CYS   K  11 101 ? 12.070  -123.068 0.014   1.00 104.63 ? 102 CYS   K O   1 
ATOM   18670 C  CB  . CYS   K  11 101 ? 12.727  -125.935 -0.918  1.00 106.33 ? 102 CYS   K CB  1 
ATOM   18671 S  SG  . CYS   K  11 101 ? 13.236  -127.463 -0.086  1.00 106.62 ? 102 CYS   K SG  1 
ATOM   18672 N  N   . GLY   K  11 102 ? 13.103  -122.788 -2.006  1.00 107.93 ? 103 GLY   K N   1 
ATOM   18673 C  CA  . GLY   K  11 102 ? 12.370  -121.566 -2.388  1.00 109.19 ? 103 GLY   K CA  1 
ATOM   18674 C  C   . GLY   K  11 102 ? 12.813  -120.995 -3.720  1.00 112.48 ? 103 GLY   K C   1 
ATOM   18675 O  O   . GLY   K  11 102 ? 13.837  -121.457 -4.264  1.00 107.85 ? 103 GLY   K O   1 
ATOM   18676 N  N   . TYR   K  11 103 ? 12.053  -120.015 -4.216  1.00 118.03 ? 104 TYR   K N   1 
ATOM   18677 C  CA  . TYR   K  11 103 ? 12.347  -119.233 -5.443  1.00 124.24 ? 104 TYR   K CA  1 
ATOM   18678 C  C   . TYR   K  11 103 ? 12.553  -117.761 -5.075  1.00 122.61 ? 104 TYR   K C   1 
ATOM   18679 O  O   . TYR   K  11 103 ? 11.741  -117.204 -4.305  1.00 118.81 ? 104 TYR   K O   1 
ATOM   18680 C  CB  . TYR   K  11 103 ? 11.214  -119.353 -6.465  1.00 132.10 ? 104 TYR   K CB  1 
ATOM   18681 C  CG  . TYR   K  11 103 ? 11.391  -118.458 -7.666  1.00 145.82 ? 104 TYR   K CG  1 
ATOM   18682 C  CD1 . TYR   K  11 103 ? 11.029  -117.118 -7.622  1.00 153.89 ? 104 TYR   K CD1 1 
ATOM   18683 C  CD2 . TYR   K  11 103 ? 11.944  -118.940 -8.842  1.00 151.21 ? 104 TYR   K CD2 1 
ATOM   18684 C  CE1 . TYR   K  11 103 ? 11.199  -116.285 -8.717  1.00 161.21 ? 104 TYR   K CE1 1 
ATOM   18685 C  CE2 . TYR   K  11 103 ? 12.118  -118.121 -9.948  1.00 161.53 ? 104 TYR   K CE2 1 
ATOM   18686 C  CZ  . TYR   K  11 103 ? 11.745  -116.787 -9.886  1.00 161.75 ? 104 TYR   K CZ  1 
ATOM   18687 O  OH  . TYR   K  11 103 ? 11.910  -115.965 -10.963 1.00 163.97 ? 104 TYR   K OH  1 
ATOM   18688 N  N   . THR   K  11 104 ? 13.607  -117.156 -5.628  1.00 121.70 ? 105 THR   K N   1 
ATOM   18689 C  CA  . THR   K  11 104 ? 13.826  -115.688 -5.669  1.00 122.08 ? 105 THR   K CA  1 
ATOM   18690 C  C   . THR   K  11 104 ? 14.214  -115.294 -7.096  1.00 121.80 ? 105 THR   K C   1 
ATOM   18691 O  O   . THR   K  11 104 ? 14.560  -116.193 -7.884  1.00 120.87 ? 105 THR   K O   1 
ATOM   18692 C  CB  . THR   K  11 104 ? 14.881  -115.249 -4.647  1.00 122.73 ? 105 THR   K CB  1 
ATOM   18693 O  OG1 . THR   K  11 104 ? 16.073  -116.000 -4.881  1.00 120.36 ? 105 THR   K OG1 1 
ATOM   18694 C  CG2 . THR   K  11 104 ? 14.429  -115.454 -3.218  1.00 121.93 ? 105 THR   K CG2 1 
ATOM   18695 N  N   . ARG   K  11 105 ? 14.153  -113.998 -7.404  1.00 124.93 ? 106 ARG   K N   1 
ATOM   18696 C  CA  . ARG   K  11 105 ? 14.512  -113.448 -8.735  1.00 128.55 ? 106 ARG   K CA  1 
ATOM   18697 C  C   . ARG   K  11 105 ? 16.008  -113.671 -8.989  1.00 123.95 ? 106 ARG   K C   1 
ATOM   18698 O  O   . ARG   K  11 105 ? 16.335  -114.199 -10.066 1.00 128.64 ? 106 ARG   K O   1 
ATOM   18699 C  CB  . ARG   K  11 105 ? 14.125  -111.969 -8.828  1.00 133.42 ? 106 ARG   K CB  1 
ATOM   18700 C  CG  . ARG   K  11 105 ? 12.903  -111.705 -9.694  1.00 140.10 ? 106 ARG   K CG  1 
ATOM   18701 C  CD  . ARG   K  11 105 ? 13.210  -111.880 -11.170 1.00 147.53 ? 106 ARG   K CD  1 
ATOM   18702 N  NE  . ARG   K  11 105 ? 12.680  -110.782 -11.970 1.00 155.87 ? 106 ARG   K NE  1 
ATOM   18703 C  CZ  . ARG   K  11 105 ? 13.215  -109.562 -12.055 1.00 161.00 ? 106 ARG   K CZ  1 
ATOM   18704 N  NH1 . ARG   K  11 105 ? 14.311  -109.253 -11.378 1.00 161.12 ? 106 ARG   K NH1 1 
ATOM   18705 N  NH2 . ARG   K  11 105 ? 12.644  -108.645 -12.818 1.00 164.89 ? 106 ARG   K NH2 1 
ATOM   18706 N  N   . LYS   K  11 106 ? 16.876  -113.310 -8.035  1.00 120.37 ? 107 LYS   K N   1 
ATOM   18707 C  CA  . LYS   K  11 106 ? 18.353  -113.294 -8.231  1.00 121.59 ? 107 LYS   K CA  1 
ATOM   18708 C  C   . LYS   K  11 106 ? 18.904  -114.726 -8.299  1.00 117.79 ? 107 LYS   K C   1 
ATOM   18709 O  O   . LYS   K  11 106 ? 19.938  -114.907 -8.967  1.00 119.02 ? 107 LYS   K O   1 
ATOM   18710 C  CB  . LYS   K  11 106 ? 19.062  -112.464 -7.151  1.00 124.99 ? 107 LYS   K CB  1 
ATOM   18711 C  CG  . LYS   K  11 106 ? 19.061  -113.031 -5.734  1.00 124.96 ? 107 LYS   K CG  1 
ATOM   18712 C  CD  . LYS   K  11 106 ? 20.385  -112.859 -4.999  1.00 128.88 ? 107 LYS   K CD  1 
ATOM   18713 C  CE  . LYS   K  11 106 ? 21.473  -113.794 -5.493  1.00 131.61 ? 107 LYS   K CE  1 
ATOM   18714 N  NZ  . LYS   K  11 106 ? 22.711  -113.691 -4.683  1.00 130.79 ? 107 LYS   K NZ  1 
ATOM   18715 N  N   . GLU   K  11 107 ? 18.248  -115.696 -7.649  1.00 115.60 ? 108 GLU   K N   1 
ATOM   18716 C  CA  . GLU   K  11 107 ? 18.733  -117.100 -7.516  1.00 114.03 ? 108 GLU   K CA  1 
ATOM   18717 C  C   . GLU   K  11 107 ? 17.992  -118.041 -8.473  1.00 112.87 ? 108 GLU   K C   1 
ATOM   18718 O  O   . GLU   K  11 107 ? 18.640  -118.970 -8.990  1.00 112.87 ? 108 GLU   K O   1 
ATOM   18719 C  CB  . GLU   K  11 107 ? 18.527  -117.621 -6.094  1.00 112.30 ? 108 GLU   K CB  1 
ATOM   18720 C  CG  . GLU   K  11 107 ? 19.364  -116.919 -5.043  1.00 112.43 ? 108 GLU   K CG  1 
ATOM   18721 C  CD  . GLU   K  11 107 ? 19.020  -117.330 -3.621  1.00 111.03 ? 108 GLU   K CD  1 
ATOM   18722 O  OE1 . GLU   K  11 107 ? 19.928  -117.793 -2.901  1.00 111.15 ? 108 GLU   K OE1 1 
ATOM   18723 O  OE2 . GLU   K  11 107 ? 17.841  -117.189 -3.238  1.00 111.74 ? 108 GLU   K OE2 1 
ATOM   18724 N  N   . GLY   K  11 108 ? 16.686  -117.829 -8.673  1.00 115.74 ? 109 GLY   K N   1 
ATOM   18725 C  CA  . GLY   K  11 108 ? 15.779  -118.806 -9.306  1.00 116.46 ? 109 GLY   K CA  1 
ATOM   18726 C  C   . GLY   K  11 108 ? 15.382  -119.884 -8.302  1.00 112.56 ? 109 GLY   K C   1 
ATOM   18727 O  O   . GLY   K  11 108 ? 15.580  -119.701 -7.103  1.00 113.81 ? 109 GLY   K O   1 
ATOM   18728 N  N   . PRO   K  11 109 ? 14.810  -121.032 -8.737  1.00 112.34 ? 110 PRO   K N   1 
ATOM   18729 C  CA  . PRO   K  11 109 ? 14.541  -122.142 -7.821  1.00 108.88 ? 110 PRO   K CA  1 
ATOM   18730 C  C   . PRO   K  11 109 ? 15.849  -122.641 -7.186  1.00 102.79 ? 110 PRO   K C   1 
ATOM   18731 O  O   . PRO   K  11 109 ? 16.767  -122.915 -7.924  1.00 105.04 ? 110 PRO   K O   1 
ATOM   18732 C  CB  . PRO   K  11 109 ? 13.887  -123.221 -8.700  1.00 109.21 ? 110 PRO   K CB  1 
ATOM   18733 C  CG  . PRO   K  11 109 ? 14.235  -122.832 -10.126 1.00 113.65 ? 110 PRO   K CG  1 
ATOM   18734 C  CD  . PRO   K  11 109 ? 14.393  -121.325 -10.116 1.00 115.58 ? 110 PRO   K CD  1 
ATOM   18735 N  N   . THR   K  11 110 ? 15.914  -122.708 -5.852  1.00 99.37  ? 111 THR   K N   1 
ATOM   18736 C  CA  . THR   K  11 110 ? 17.132  -123.095 -5.087  1.00 98.64  ? 111 THR   K CA  1 
ATOM   18737 C  C   . THR   K  11 110 ? 16.778  -124.024 -3.921  1.00 97.33  ? 111 THR   K C   1 
ATOM   18738 O  O   . THR   K  11 110 ? 15.774  -123.751 -3.232  1.00 95.89  ? 111 THR   K O   1 
ATOM   18739 C  CB  . THR   K  11 110 ? 17.854  -121.857 -4.546  1.00 96.59  ? 111 THR   K CB  1 
ATOM   18740 O  OG1 . THR   K  11 110 ? 18.060  -120.969 -5.644  1.00 98.80  ? 111 THR   K OG1 1 
ATOM   18741 C  CG2 . THR   K  11 110 ? 19.180  -122.182 -3.896  1.00 95.09  ? 111 THR   K CG2 1 
ATOM   18742 N  N   . ILE   K  11 111 ? 17.603  -125.056 -3.704  1.00 97.56  ? 112 ILE   K N   1 
ATOM   18743 C  CA  . ILE   K  11 111 ? 17.518  -126.007 -2.554  1.00 96.84  ? 112 ILE   K CA  1 
ATOM   18744 C  C   . ILE   K  11 111 ? 18.868  -126.010 -1.827  1.00 91.07  ? 112 ILE   K C   1 
ATOM   18745 O  O   . ILE   K  11 111 ? 19.905  -126.150 -2.503  1.00 91.81  ? 112 ILE   K O   1 
ATOM   18746 C  CB  . ILE   K  11 111 ? 17.140  -127.430 -3.014  1.00 98.68  ? 112 ILE   K CB  1 
ATOM   18747 C  CG1 . ILE   K  11 111 ? 15.938  -127.439 -3.962  1.00 102.87 ? 112 ILE   K CG1 1 
ATOM   18748 C  CG2 . ILE   K  11 111 ? 16.910  -128.334 -1.810  1.00 98.23  ? 112 ILE   K CG2 1 
ATOM   18749 C  CD1 . ILE   K  11 111 ? 15.746  -128.749 -4.690  1.00 105.15 ? 112 ILE   K CD1 1 
ATOM   18750 N  N   . TYR   K  11 112 ? 18.847  -125.879 -0.499  1.00 88.77  ? 113 TYR   K N   1 
ATOM   18751 C  CA  . TYR   K  11 112 ? 20.039  -125.991 0.380   1.00 90.26  ? 113 TYR   K CA  1 
ATOM   18752 C  C   . TYR   K  11 112 ? 19.806  -127.089 1.418   1.00 87.80  ? 113 TYR   K C   1 
ATOM   18753 O  O   . TYR   K  11 112 ? 18.777  -127.039 2.114   1.00 85.21  ? 113 TYR   K O   1 
ATOM   18754 C  CB  . TYR   K  11 112 ? 20.337  -124.665 1.083   1.00 90.89  ? 113 TYR   K CB  1 
ATOM   18755 C  CG  . TYR   K  11 112 ? 21.196  -123.714 0.289   1.00 94.75  ? 113 TYR   K CG  1 
ATOM   18756 C  CD1 . TYR   K  11 112 ? 22.579  -123.817 0.304   1.00 94.28  ? 113 TYR   K CD1 1 
ATOM   18757 C  CD2 . TYR   K  11 112 ? 20.628  -122.710 -0.479  1.00 95.06  ? 113 TYR   K CD2 1 
ATOM   18758 C  CE1 . TYR   K  11 112 ? 23.375  -122.948 -0.426  1.00 95.12  ? 113 TYR   K CE1 1 
ATOM   18759 C  CE2 . TYR   K  11 112 ? 21.409  -121.834 -1.216  1.00 95.14  ? 113 TYR   K CE2 1 
ATOM   18760 C  CZ  . TYR   K  11 112 ? 22.788  -121.951 -1.187  1.00 96.19  ? 113 TYR   K CZ  1 
ATOM   18761 O  OH  . TYR   K  11 112 ? 23.563  -121.087 -1.905  1.00 95.89  ? 113 TYR   K OH  1 
ATOM   18762 N  N   . TYR   K  11 113 ? 20.743  -128.034 1.515   1.00 89.51  ? 114 TYR   K N   1 
ATOM   18763 C  CA  . TYR   K  11 113 ? 20.804  -129.064 2.584   1.00 92.49  ? 114 TYR   K CA  1 
ATOM   18764 C  C   . TYR   K  11 113 ? 21.511  -128.449 3.796   1.00 88.94  ? 114 TYR   K C   1 
ATOM   18765 O  O   . TYR   K  11 113 ? 22.620  -127.906 3.621   1.00 88.30  ? 114 TYR   K O   1 
ATOM   18766 C  CB  . TYR   K  11 113 ? 21.528  -130.322 2.092   1.00 91.98  ? 114 TYR   K CB  1 
ATOM   18767 C  CG  . TYR   K  11 113 ? 21.825  -131.336 3.168   1.00 92.34  ? 114 TYR   K CG  1 
ATOM   18768 C  CD1 . TYR   K  11 113 ? 20.887  -132.286 3.540   1.00 94.65  ? 114 TYR   K CD1 1 
ATOM   18769 C  CD2 . TYR   K  11 113 ? 23.048  -131.349 3.820   1.00 93.40  ? 114 TYR   K CD2 1 
ATOM   18770 C  CE1 . TYR   K  11 113 ? 21.153  -133.221 4.528   1.00 93.69  ? 114 TYR   K CE1 1 
ATOM   18771 C  CE2 . TYR   K  11 113 ? 23.331  -132.275 4.811   1.00 92.39  ? 114 TYR   K CE2 1 
ATOM   18772 C  CZ  . TYR   K  11 113 ? 22.381  -133.216 5.167   1.00 92.24  ? 114 TYR   K CZ  1 
ATOM   18773 O  OH  . TYR   K  11 113 ? 22.662  -134.127 6.144   1.00 89.84  ? 114 TYR   K OH  1 
ATOM   18774 N  N   . VAL   K  11 114 ? 20.882  -128.514 4.973   1.00 88.71  ? 115 VAL   K N   1 
ATOM   18775 C  CA  . VAL   K  11 114 ? 21.442  -127.992 6.257   1.00 88.77  ? 115 VAL   K CA  1 
ATOM   18776 C  C   . VAL   K  11 114 ? 21.202  -129.028 7.358   1.00 85.87  ? 115 VAL   K C   1 
ATOM   18777 O  O   . VAL   K  11 114 ? 20.020  -129.303 7.644   1.00 86.07  ? 115 VAL   K O   1 
ATOM   18778 C  CB  . VAL   K  11 114 ? 20.815  -126.640 6.642   1.00 89.78  ? 115 VAL   K CB  1 
ATOM   18779 C  CG1 . VAL   K  11 114 ? 21.304  -126.164 8.003   1.00 91.85  ? 115 VAL   K CG1 1 
ATOM   18780 C  CG2 . VAL   K  11 114 ? 21.061  -125.575 5.586   1.00 90.39  ? 115 VAL   K CG2 1 
ATOM   18781 N  N   . ASP   K  11 115 ? 22.274  -129.546 7.971   1.00 85.09  ? 116 ASP   K N   1 
ATOM   18782 C  CA  . ASP   K  11 115 ? 22.198  -130.553 9.066   1.00 87.34  ? 116 ASP   K CA  1 
ATOM   18783 C  C   . ASP   K  11 115 ? 22.891  -130.001 10.317  1.00 83.88  ? 116 ASP   K C   1 
ATOM   18784 O  O   . ASP   K  11 115 ? 23.528  -128.934 10.230  1.00 83.20  ? 116 ASP   K O   1 
ATOM   18785 C  CB  . ASP   K  11 115 ? 22.746  -131.915 8.622   1.00 87.39  ? 116 ASP   K CB  1 
ATOM   18786 C  CG  . ASP   K  11 115 ? 24.261  -132.019 8.521   1.00 91.81  ? 116 ASP   K CG  1 
ATOM   18787 O  OD1 . ASP   K  11 115 ? 24.951  -131.084 8.981   1.00 92.92  ? 116 ASP   K OD1 1 
ATOM   18788 O  OD2 . ASP   K  11 115 ? 24.742  -133.045 7.981   1.00 88.41  ? 116 ASP   K OD2 1 
ATOM   18789 N  N   . SER   K  11 116 ? 22.772  -130.724 11.432  1.00 84.45  ? 117 SER   K N   1 
ATOM   18790 C  CA  . SER   K  11 116 ? 23.105  -130.244 12.798  1.00 85.06  ? 117 SER   K CA  1 
ATOM   18791 C  C   . SER   K  11 116 ? 24.619  -130.223 13.042  1.00 86.00  ? 117 SER   K C   1 
ATOM   18792 O  O   . SER   K  11 116 ? 25.029  -129.504 13.967  1.00 86.28  ? 117 SER   K O   1 
ATOM   18793 C  CB  . SER   K  11 116 ? 22.390  -131.045 13.855  1.00 84.28  ? 117 SER   K CB  1 
ATOM   18794 O  OG  . SER   K  11 116 ? 22.529  -132.438 13.633  1.00 85.39  ? 117 SER   K OG  1 
ATOM   18795 N  N   . ASP   K  11 117 ? 25.426  -130.957 12.266  1.00 85.58  ? 118 ASP   K N   1 
ATOM   18796 C  CA  . ASP   K  11 117 ? 26.910  -130.881 12.387  1.00 91.51  ? 118 ASP   K CA  1 
ATOM   18797 C  C   . ASP   K  11 117 ? 27.429  -129.740 11.503  1.00 89.43  ? 118 ASP   K C   1 
ATOM   18798 O  O   . ASP   K  11 117 ? 28.657  -129.591 11.411  1.00 88.67  ? 118 ASP   K O   1 
ATOM   18799 C  CB  . ASP   K  11 117 ? 27.637  -132.217 12.156  1.00 99.12  ? 118 ASP   K CB  1 
ATOM   18800 C  CG  . ASP   K  11 117 ? 26.932  -133.259 11.305  1.00 104.72 ? 118 ASP   K CG  1 
ATOM   18801 O  OD1 . ASP   K  11 117 ? 26.826  -133.044 10.081  1.00 113.39 ? 118 ASP   K OD1 1 
ATOM   18802 O  OD2 . ASP   K  11 117 ? 26.529  -134.298 11.873  1.00 114.42 ? 118 ASP   K OD2 1 
ATOM   18803 N  N   . GLY   K  11 118 ? 26.531  -128.946 10.910  1.00 88.84  ? 119 GLY   K N   1 
ATOM   18804 C  CA  . GLY   K  11 118 ? 26.856  -127.642 10.299  1.00 89.31  ? 119 GLY   K CA  1 
ATOM   18805 C  C   . GLY   K  11 118 ? 27.135  -127.735 8.810   1.00 90.33  ? 119 GLY   K C   1 
ATOM   18806 O  O   . GLY   K  11 118 ? 27.622  -126.733 8.253   1.00 96.49  ? 119 GLY   K O   1 
ATOM   18807 N  N   . THR   K  11 119 ? 26.841  -128.875 8.178   1.00 87.09  ? 120 THR   K N   1 
ATOM   18808 C  CA  . THR   K  11 119 ? 26.960  -129.060 6.708   1.00 88.38  ? 120 THR   K CA  1 
ATOM   18809 C  C   . THR   K  11 119 ? 25.907  -128.191 6.015   1.00 88.10  ? 120 THR   K C   1 
ATOM   18810 O  O   . THR   K  11 119 ? 24.729  -128.265 6.420   1.00 88.77  ? 120 THR   K O   1 
ATOM   18811 C  CB  . THR   K  11 119 ? 26.789  -130.526 6.299   1.00 88.40  ? 120 THR   K CB  1 
ATOM   18812 O  OG1 . THR   K  11 119 ? 27.661  -131.315 7.107   1.00 91.57  ? 120 THR   K OG1 1 
ATOM   18813 C  CG2 . THR   K  11 119 ? 27.091  -130.762 4.835   1.00 90.58  ? 120 THR   K CG2 1 
ATOM   18814 N  N   . ARG   K  11 120 ? 26.329  -127.399 5.023   1.00 85.84  ? 121 ARG   K N   1 
ATOM   18815 C  CA  . ARG   K  11 120 ? 25.444  -126.584 4.149   1.00 86.19  ? 121 ARG   K CA  1 
ATOM   18816 C  C   . ARG   K  11 120 ? 25.845  -126.835 2.695   1.00 84.21  ? 121 ARG   K C   1 
ATOM   18817 O  O   . ARG   K  11 120 ? 27.003  -126.529 2.351   1.00 80.57  ? 121 ARG   K O   1 
ATOM   18818 C  CB  . ARG   K  11 120 ? 25.552  -125.101 4.511   1.00 87.69  ? 121 ARG   K CB  1 
ATOM   18819 C  CG  . ARG   K  11 120 ? 24.594  -124.192 3.753   1.00 90.28  ? 121 ARG   K CG  1 
ATOM   18820 C  CD  . ARG   K  11 120 ? 24.519  -122.808 4.379   1.00 90.94  ? 121 ARG   K CD  1 
ATOM   18821 N  NE  . ARG   K  11 120 ? 23.979  -121.810 3.464   1.00 90.97  ? 121 ARG   K NE  1 
ATOM   18822 C  CZ  . ARG   K  11 120 ? 24.684  -121.149 2.548   1.00 91.09  ? 121 ARG   K CZ  1 
ATOM   18823 N  NH1 . ARG   K  11 120 ? 24.079  -120.273 1.764   1.00 88.79  ? 121 ARG   K NH1 1 
ATOM   18824 N  NH2 . ARG   K  11 120 ? 25.982  -121.364 2.410   1.00 94.92  ? 121 ARG   K NH2 1 
ATOM   18825 N  N   . LEU   K  11 121 ? 24.927  -127.386 1.892   1.00 84.19  ? 122 LEU   K N   1 
ATOM   18826 C  CA  . LEU   K  11 121 ? 25.169  -127.779 0.478   1.00 87.12  ? 122 LEU   K CA  1 
ATOM   18827 C  C   . LEU   K  11 121 ? 24.035  -127.252 -0.404  1.00 89.19  ? 122 LEU   K C   1 
ATOM   18828 O  O   . LEU   K  11 121 ? 22.863  -127.501 -0.065  1.00 87.70  ? 122 LEU   K O   1 
ATOM   18829 C  CB  . LEU   K  11 121 ? 25.243  -129.306 0.375   1.00 86.56  ? 122 LEU   K CB  1 
ATOM   18830 C  CG  . LEU   K  11 121 ? 26.320  -129.992 1.212   1.00 85.19  ? 122 LEU   K CG  1 
ATOM   18831 C  CD1 . LEU   K  11 121 ? 26.119  -131.497 1.188   1.00 85.24  ? 122 LEU   K CD1 1 
ATOM   18832 C  CD2 . LEU   K  11 121 ? 27.716  -129.633 0.725   1.00 84.37  ? 122 LEU   K CD2 1 
ATOM   18833 N  N   . LYS   K  11 122 ? 24.383  -126.561 -1.493  1.00 93.42  ? 123 LYS   K N   1 
ATOM   18834 C  CA  . LYS   K  11 122 ? 23.462  -126.281 -2.625  1.00 97.94  ? 123 LYS   K CA  1 
ATOM   18835 C  C   . LYS   K  11 122 ? 23.414  -127.536 -3.502  1.00 98.97  ? 123 LYS   K C   1 
ATOM   18836 O  O   . LYS   K  11 122 ? 24.469  -128.170 -3.674  1.00 102.87 ? 123 LYS   K O   1 
ATOM   18837 C  CB  . LYS   K  11 122 ? 23.926  -125.053 -3.414  1.00 100.50 ? 123 LYS   K CB  1 
ATOM   18838 C  CG  . LYS   K  11 122 ? 22.913  -124.532 -4.424  1.00 103.52 ? 123 LYS   K CG  1 
ATOM   18839 C  CD  . LYS   K  11 122 ? 23.149  -123.098 -4.843  1.00 106.67 ? 123 LYS   K CD  1 
ATOM   18840 C  CE  . LYS   K  11 122 ? 24.334  -122.934 -5.770  1.00 109.85 ? 123 LYS   K CE  1 
ATOM   18841 N  NZ  . LYS   K  11 122 ? 24.575  -121.509 -6.095  1.00 110.98 ? 123 LYS   K NZ  1 
ATOM   18842 N  N   . GLY   K  11 123 ? 22.236  -127.904 -4.008  1.00 100.00 ? 124 GLY   K N   1 
ATOM   18843 C  CA  . GLY   K  11 123 ? 22.074  -129.083 -4.880  1.00 102.27 ? 124 GLY   K CA  1 
ATOM   18844 C  C   . GLY   K  11 123 ? 20.729  -129.102 -5.580  1.00 103.88 ? 124 GLY   K C   1 
ATOM   18845 O  O   . GLY   K  11 123 ? 19.861  -128.279 -5.224  1.00 102.89 ? 124 GLY   K O   1 
ATOM   18846 N  N   . ASP   K  11 124 ? 20.570  -130.014 -6.542  1.00 105.94 ? 125 ASP   K N   1 
ATOM   18847 C  CA  . ASP   K  11 124 ? 19.341  -130.177 -7.363  1.00 106.89 ? 125 ASP   K CA  1 
ATOM   18848 C  C   . ASP   K  11 124 ? 18.437  -131.241 -6.729  1.00 104.14 ? 125 ASP   K C   1 
ATOM   18849 O  O   . ASP   K  11 124 ? 17.212  -131.031 -6.709  1.00 97.94  ? 125 ASP   K O   1 
ATOM   18850 C  CB  . ASP   K  11 124 ? 19.701  -130.514 -8.812  1.00 113.12 ? 125 ASP   K CB  1 
ATOM   18851 C  CG  . ASP   K  11 124 ? 20.465  -129.409 -9.527  1.00 116.40 ? 125 ASP   K CG  1 
ATOM   18852 O  OD1 . ASP   K  11 124 ? 20.367  -128.242 -9.091  1.00 113.04 ? 125 ASP   K OD1 1 
ATOM   18853 O  OD2 . ASP   K  11 124 ? 21.156  -129.723 -10.516 1.00 121.65 ? 125 ASP   K OD2 1 
ATOM   18854 N  N   . ILE   K  11 125 ? 19.020  -132.341 -6.243  1.00 103.30 ? 126 ILE   K N   1 
ATOM   18855 C  CA  . ILE   K  11 125 ? 18.291  -133.471 -5.595  1.00 101.62 ? 126 ILE   K CA  1 
ATOM   18856 C  C   . ILE   K  11 125 ? 18.926  -133.741 -4.233  1.00 97.93  ? 126 ILE   K C   1 
ATOM   18857 O  O   . ILE   K  11 125 ? 20.167  -133.785 -4.159  1.00 99.72  ? 126 ILE   K O   1 
ATOM   18858 C  CB  . ILE   K  11 125 ? 18.328  -134.744 -6.462  1.00 104.29 ? 126 ILE   K CB  1 
ATOM   18859 C  CG1 . ILE   K  11 125 ? 18.018  -134.458 -7.934  1.00 109.03 ? 126 ILE   K CG1 1 
ATOM   18860 C  CG2 . ILE   K  11 125 ? 17.399  -135.801 -5.882  1.00 102.84 ? 126 ILE   K CG2 1 
ATOM   18861 C  CD1 . ILE   K  11 125 ? 18.511  -135.528 -8.881  1.00 113.49 ? 126 ILE   K CD1 1 
ATOM   18862 N  N   . PHE   K  11 126 ? 18.096  -133.932 -3.209  1.00 94.75  ? 127 PHE   K N   1 
ATOM   18863 C  CA  . PHE   K  11 126 ? 18.504  -134.490 -1.896  1.00 93.77  ? 127 PHE   K CA  1 
ATOM   18864 C  C   . PHE   K  11 126 ? 17.354  -135.306 -1.302  1.00 90.62  ? 127 PHE   K C   1 
ATOM   18865 O  O   . PHE   K  11 126 ? 16.174  -134.950 -1.508  1.00 89.31  ? 127 PHE   K O   1 
ATOM   18866 C  CB  . PHE   K  11 126 ? 18.849  -133.391 -0.894  1.00 90.84  ? 127 PHE   K CB  1 
ATOM   18867 C  CG  . PHE   K  11 126 ? 20.060  -132.542 -1.180  1.00 89.77  ? 127 PHE   K CG  1 
ATOM   18868 C  CD1 . PHE   K  11 126 ? 21.337  -133.027 -0.954  1.00 90.37  ? 127 PHE   K CD1 1 
ATOM   18869 C  CD2 . PHE   K  11 126 ? 19.917  -131.232 -1.604  1.00 89.10  ? 127 PHE   K CD2 1 
ATOM   18870 C  CE1 . PHE   K  11 126 ? 22.449  -132.236 -1.192  1.00 89.88  ? 127 PHE   K CE1 1 
ATOM   18871 C  CE2 . PHE   K  11 126 ? 21.029  -130.441 -1.840  1.00 90.93  ? 127 PHE   K CE2 1 
ATOM   18872 C  CZ  . PHE   K  11 126 ? 22.293  -130.945 -1.634  1.00 90.16  ? 127 PHE   K CZ  1 
ATOM   18873 N  N   . CYS   K  11 127 ? 17.713  -136.351 -0.558  1.00 90.25  ? 128 CYS   K N   1 
ATOM   18874 C  CA  . CYS   K  11 127 ? 16.802  -137.174 0.273   1.00 91.06  ? 128 CYS   K CA  1 
ATOM   18875 C  C   . CYS   K  11 127 ? 17.409  -137.282 1.673   1.00 89.66  ? 128 CYS   K C   1 
ATOM   18876 O  O   . CYS   K  11 127 ? 18.621  -137.577 1.776   1.00 88.33  ? 128 CYS   K O   1 
ATOM   18877 C  CB  . CYS   K  11 127 ? 16.587  -138.548 -0.345  1.00 93.23  ? 128 CYS   K CB  1 
ATOM   18878 S  SG  . CYS   K  11 127 ? 16.051  -138.457 -2.073  1.00 94.34  ? 128 CYS   K SG  1 
ATOM   18879 N  N   . VAL   K  11 128 ? 16.606  -137.005 2.700   1.00 88.98  ? 129 VAL   K N   1 
ATOM   18880 C  CA  . VAL   K  11 128 ? 17.055  -136.966 4.121   1.00 89.47  ? 129 VAL   K CA  1 
ATOM   18881 C  C   . VAL   K  11 128 ? 16.084  -137.803 4.955   1.00 88.32  ? 129 VAL   K C   1 
ATOM   18882 O  O   . VAL   K  11 128 ? 14.891  -137.863 4.602   1.00 87.43  ? 129 VAL   K O   1 
ATOM   18883 C  CB  . VAL   K  11 128 ? 17.144  -135.524 4.652   1.00 88.88  ? 129 VAL   K CB  1 
ATOM   18884 C  CG1 . VAL   K  11 128 ? 18.004  -135.445 5.903   1.00 87.40  ? 129 VAL   K CG1 1 
ATOM   18885 C  CG2 . VAL   K  11 128 ? 17.654  -134.556 3.596   1.00 91.59  ? 129 VAL   K CG2 1 
ATOM   18886 N  N   . GLY   K  11 129 ? 16.598  -138.412 6.024   1.00 91.05  ? 130 GLY   K N   1 
ATOM   18887 C  CA  . GLY   K  11 129 ? 15.828  -139.255 6.955   1.00 93.64  ? 130 GLY   K CA  1 
ATOM   18888 C  C   . GLY   K  11 129 ? 16.219  -140.715 6.829   1.00 94.26  ? 130 GLY   K C   1 
ATOM   18889 O  O   . GLY   K  11 129 ? 17.004  -141.043 5.917   1.00 93.11  ? 130 GLY   K O   1 
ATOM   18890 N  N   . SER   K  11 130 ? 15.683  -141.564 7.710   1.00 96.20  ? 131 SER   K N   1 
ATOM   18891 C  CA  . SER   K  11 130 ? 16.031  -143.006 7.829   1.00 97.25  ? 131 SER   K CA  1 
ATOM   18892 C  C   . SER   K  11 130 ? 15.686  -143.756 6.535   1.00 94.88  ? 131 SER   K C   1 
ATOM   18893 O  O   . SER   K  11 130 ? 16.342  -144.773 6.259   1.00 95.51  ? 131 SER   K O   1 
ATOM   18894 C  CB  . SER   K  11 130 ? 15.363  -143.627 9.032   1.00 100.44 ? 131 SER   K CB  1 
ATOM   18895 O  OG  . SER   K  11 130 ? 13.969  -143.356 9.045   1.00 103.29 ? 131 SER   K OG  1 
ATOM   18896 N  N   . GLY   K  11 131 ? 14.708  -143.269 5.767   1.00 93.89  ? 132 GLY   K N   1 
ATOM   18897 C  CA  . GLY   K  11 131 ? 14.273  -143.889 4.499   1.00 94.23  ? 132 GLY   K CA  1 
ATOM   18898 C  C   . GLY   K  11 131 ? 14.849  -143.200 3.270   1.00 91.64  ? 132 GLY   K C   1 
ATOM   18899 O  O   . GLY   K  11 131 ? 14.349  -143.481 2.168   1.00 85.19  ? 132 GLY   K O   1 
ATOM   18900 N  N   . GLN   K  11 132 ? 15.859  -142.336 3.436   1.00 95.01  ? 133 GLN   K N   1 
ATOM   18901 C  CA  . GLN   K  11 132 ? 16.438  -141.505 2.343   1.00 96.51  ? 133 GLN   K CA  1 
ATOM   18902 C  C   . GLN   K  11 132 ? 16.917  -142.403 1.197   1.00 96.60  ? 133 GLN   K C   1 
ATOM   18903 O  O   . GLN   K  11 132 ? 16.707  -142.019 0.034   1.00 95.42  ? 133 GLN   K O   1 
ATOM   18904 C  CB  . GLN   K  11 132 ? 17.581  -140.617 2.845   1.00 96.74  ? 133 GLN   K CB  1 
ATOM   18905 C  CG  . GLN   K  11 132 ? 18.807  -141.368 3.342   1.00 99.52  ? 133 GLN   K CG  1 
ATOM   18906 C  CD  . GLN   K  11 132 ? 19.824  -140.402 3.897   1.00 101.52 ? 133 GLN   K CD  1 
ATOM   18907 O  OE1 . GLN   K  11 132 ? 19.573  -139.705 4.877   1.00 105.15 ? 133 GLN   K OE1 1 
ATOM   18908 N  NE2 . GLN   K  11 132 ? 20.981  -140.343 3.260   1.00 105.14 ? 133 GLN   K NE2 1 
ATOM   18909 N  N   . THR   K  11 133 ? 17.528  -143.549 1.518   1.00 99.46  ? 134 THR   K N   1 
ATOM   18910 C  CA  . THR   K  11 133 ? 18.140  -144.493 0.539   1.00 99.54  ? 134 THR   K CA  1 
ATOM   18911 C  C   . THR   K  11 133 ? 17.054  -145.115 -0.351  1.00 94.82  ? 134 THR   K C   1 
ATOM   18912 O  O   . THR   K  11 133 ? 17.318  -145.296 -1.558  1.00 92.59  ? 134 THR   K O   1 
ATOM   18913 C  CB  . THR   K  11 133 ? 18.960  -145.581 1.246   1.00 101.77 ? 134 THR   K CB  1 
ATOM   18914 O  OG1 . THR   K  11 133 ? 18.098  -146.274 2.149   1.00 101.70 ? 134 THR   K OG1 1 
ATOM   18915 C  CG2 . THR   K  11 133 ? 20.154  -145.028 1.995   1.00 105.43 ? 134 THR   K CG2 1 
ATOM   18916 N  N   . PHE   K  11 134 ? 15.889  -145.430 0.225   1.00 96.79  ? 135 PHE   K N   1 
ATOM   18917 C  CA  . PHE   K  11 134 ? 14.723  -146.041 -0.470  1.00 99.06  ? 135 PHE   K CA  1 
ATOM   18918 C  C   . PHE   K  11 134 ? 14.135  -145.025 -1.458  1.00 96.78  ? 135 PHE   K C   1 
ATOM   18919 O  O   . PHE   K  11 134 ? 13.802  -145.419 -2.587  1.00 94.53  ? 135 PHE   K O   1 
ATOM   18920 C  CB  . PHE   K  11 134 ? 13.667  -146.517 0.534   1.00 101.96 ? 135 PHE   K CB  1 
ATOM   18921 C  CG  . PHE   K  11 134 ? 14.146  -147.539 1.537   1.00 105.14 ? 135 PHE   K CG  1 
ATOM   18922 C  CD1 . PHE   K  11 134 ? 14.396  -148.849 1.159   1.00 106.74 ? 135 PHE   K CD1 1 
ATOM   18923 C  CD2 . PHE   K  11 134 ? 14.341  -147.191 2.866   1.00 105.82 ? 135 PHE   K CD2 1 
ATOM   18924 C  CE1 . PHE   K  11 134 ? 14.838  -149.782 2.085   1.00 109.76 ? 135 PHE   K CE1 1 
ATOM   18925 C  CE2 . PHE   K  11 134 ? 14.781  -148.124 3.792   1.00 107.18 ? 135 PHE   K CE2 1 
ATOM   18926 C  CZ  . PHE   K  11 134 ? 15.029  -149.419 3.400   1.00 109.06 ? 135 PHE   K CZ  1 
ATOM   18927 N  N   . ALA   K  11 135 ? 14.019  -143.760 -1.037  1.00 96.82  ? 136 ALA   K N   1 
ATOM   18928 C  CA  . ALA   K  11 135 ? 13.527  -142.612 -1.843  1.00 97.79  ? 136 ALA   K CA  1 
ATOM   18929 C  C   . ALA   K  11 135 ? 14.475  -142.338 -3.018  1.00 94.43  ? 136 ALA   K C   1 
ATOM   18930 O  O   . ALA   K  11 135 ? 13.978  -142.195 -4.144  1.00 91.67  ? 136 ALA   K O   1 
ATOM   18931 C  CB  . ALA   K  11 135 ? 13.384  -141.385 -0.975  1.00 96.94  ? 136 ALA   K CB  1 
ATOM   18932 N  N   . TYR   K  11 136 ? 15.783  -142.243 -2.749  1.00 99.17  ? 137 TYR   K N   1 
ATOM   18933 C  CA  . TYR   K  11 136 ? 16.860  -142.104 -3.767  1.00 103.43 ? 137 TYR   K CA  1 
ATOM   18934 C  C   . TYR   K  11 136 ? 16.698  -143.195 -4.831  1.00 106.15 ? 137 TYR   K C   1 
ATOM   18935 O  O   . TYR   K  11 136 ? 16.646  -142.855 -6.025  1.00 108.64 ? 137 TYR   K O   1 
ATOM   18936 C  CB  . TYR   K  11 136 ? 18.255  -142.209 -3.140  1.00 105.76 ? 137 TYR   K CB  1 
ATOM   18937 C  CG  . TYR   K  11 136 ? 18.843  -140.917 -2.626  1.00 106.81 ? 137 TYR   K CG  1 
ATOM   18938 C  CD1 . TYR   K  11 136 ? 18.862  -139.775 -3.409  1.00 105.55 ? 137 TYR   K CD1 1 
ATOM   18939 C  CD2 . TYR   K  11 136 ? 19.422  -140.846 -1.367  1.00 106.45 ? 137 TYR   K CD2 1 
ATOM   18940 C  CE1 . TYR   K  11 136 ? 19.408  -138.588 -2.947  1.00 106.17 ? 137 TYR   K CE1 1 
ATOM   18941 C  CE2 . TYR   K  11 136 ? 19.979  -139.669 -0.891  1.00 106.54 ? 137 TYR   K CE2 1 
ATOM   18942 C  CZ  . TYR   K  11 136 ? 19.972  -138.534 -1.685  1.00 105.57 ? 137 TYR   K CZ  1 
ATOM   18943 O  OH  . TYR   K  11 136 ? 20.514  -137.365 -1.231  1.00 106.31 ? 137 TYR   K OH  1 
ATOM   18944 N  N   . GLY   K  11 137 ? 16.623  -144.460 -4.399  1.00 109.26 ? 138 GLY   K N   1 
ATOM   18945 C  CA  . GLY   K  11 137 ? 16.519  -145.644 -5.275  1.00 112.78 ? 138 GLY   K CA  1 
ATOM   18946 C  C   . GLY   K  11 137 ? 15.532  -145.428 -6.411  1.00 114.29 ? 138 GLY   K C   1 
ATOM   18947 O  O   . GLY   K  11 137 ? 15.907  -145.669 -7.576  1.00 114.73 ? 138 GLY   K O   1 
ATOM   18948 N  N   . VAL   K  11 138 ? 14.318  -144.975 -6.080  1.00 113.20 ? 139 VAL   K N   1 
ATOM   18949 C  CA  . VAL   K  11 138 ? 13.197  -144.738 -7.040  1.00 111.61 ? 139 VAL   K CA  1 
ATOM   18950 C  C   . VAL   K  11 138 ? 13.426  -143.410 -7.772  1.00 110.45 ? 139 VAL   K C   1 
ATOM   18951 O  O   . VAL   K  11 138 ? 13.255  -143.377 -9.004  1.00 109.36 ? 139 VAL   K O   1 
ATOM   18952 C  CB  . VAL   K  11 138 ? 11.833  -144.749 -6.319  1.00 112.21 ? 139 VAL   K CB  1 
ATOM   18953 C  CG1 . VAL   K  11 138 ? 10.715  -144.193 -7.190  1.00 112.14 ? 139 VAL   K CG1 1 
ATOM   18954 C  CG2 . VAL   K  11 138 ? 11.478  -146.139 -5.815  1.00 114.85 ? 139 VAL   K CG2 1 
ATOM   18955 N  N   . LEU   K  11 139 ? 13.774  -142.352 -7.035  1.00 108.36 ? 140 LEU   K N   1 
ATOM   18956 C  CA  . LEU   K  11 139 ? 13.886  -140.963 -7.561  1.00 109.55 ? 140 LEU   K CA  1 
ATOM   18957 C  C   . LEU   K  11 139 ? 14.989  -140.892 -8.629  1.00 104.85 ? 140 LEU   K C   1 
ATOM   18958 O  O   . LEU   K  11 139 ? 14.683  -140.464 -9.753  1.00 101.51 ? 140 LEU   K O   1 
ATOM   18959 C  CB  . LEU   K  11 139 ? 14.156  -140.011 -6.388  1.00 106.31 ? 140 LEU   K CB  1 
ATOM   18960 C  CG  . LEU   K  11 139 ? 14.290  -138.529 -6.738  1.00 106.84 ? 140 LEU   K CG  1 
ATOM   18961 C  CD1 . LEU   K  11 139 ? 13.154  -138.068 -7.637  1.00 108.14 ? 140 LEU   K CD1 1 
ATOM   18962 C  CD2 . LEU   K  11 139 ? 14.344  -137.680 -5.477  1.00 104.14 ? 140 LEU   K CD2 1 
ATOM   18963 N  N   . ASP   K  11 140 ? 16.211  -141.316 -8.292  1.00 108.53 ? 141 ASP   K N   1 
ATOM   18964 C  CA  . ASP   K  11 140 ? 17.383  -141.352 -9.212  1.00 112.24 ? 141 ASP   K CA  1 
ATOM   18965 C  C   . ASP   K  11 140 ? 17.027  -142.116 -10.491 1.00 114.76 ? 141 ASP   K C   1 
ATOM   18966 O  O   . ASP   K  11 140 ? 17.329  -141.597 -11.581 1.00 110.93 ? 141 ASP   K O   1 
ATOM   18967 C  CB  . ASP   K  11 140 ? 18.595  -142.027 -8.564  1.00 112.69 ? 141 ASP   K CB  1 
ATOM   18968 C  CG  . ASP   K  11 140 ? 19.339  -141.150 -7.579  1.00 113.83 ? 141 ASP   K CG  1 
ATOM   18969 O  OD1 . ASP   K  11 140 ? 19.532  -139.959 -7.888  1.00 115.71 ? 141 ASP   K OD1 1 
ATOM   18970 O  OD2 . ASP   K  11 140 ? 19.726  -141.669 -6.514  1.00 112.64 ? 141 ASP   K OD2 1 
ATOM   18971 N  N   . SER   K  11 141 ? 16.418  -143.302 -10.349 1.00 121.39 ? 142 SER   K N   1 
ATOM   18972 C  CA  . SER   K  11 141 ? 16.176  -144.287 -11.440 1.00 129.12 ? 142 SER   K CA  1 
ATOM   18973 C  C   . SER   K  11 141 ? 14.993  -143.871 -12.328 1.00 130.19 ? 142 SER   K C   1 
ATOM   18974 O  O   . SER   K  11 141 ? 14.706  -144.612 -13.285 1.00 134.28 ? 142 SER   K O   1 
ATOM   18975 C  CB  . SER   K  11 141 ? 15.982  -145.686 -10.884 1.00 132.64 ? 142 SER   K CB  1 
ATOM   18976 O  OG  . SER   K  11 141 ? 14.828  -145.760 -10.058 1.00 136.32 ? 142 SER   K OG  1 
ATOM   18977 N  N   . ASN   K  11 142 ? 14.329  -142.747 -12.031 1.00 131.36 ? 143 ASN   K N   1 
ATOM   18978 C  CA  . ASN   K  11 142 ? 13.203  -142.202 -12.840 1.00 133.82 ? 143 ASN   K CA  1 
ATOM   18979 C  C   . ASN   K  11 142 ? 13.410  -140.713 -13.150 1.00 134.37 ? 143 ASN   K C   1 
ATOM   18980 O  O   . ASN   K  11 142 ? 12.634  -140.185 -13.968 1.00 130.04 ? 143 ASN   K O   1 
ATOM   18981 C  CB  . ASN   K  11 142 ? 11.859  -142.404 -12.133 1.00 136.60 ? 143 ASN   K CB  1 
ATOM   18982 C  CG  . ASN   K  11 142 ? 11.385  -143.842 -12.156 1.00 141.68 ? 143 ASN   K CG  1 
ATOM   18983 O  OD1 . ASN   K  11 142 ? 11.311  -144.494 -11.116 1.00 144.78 ? 143 ASN   K OD1 1 
ATOM   18984 N  ND2 . ASN   K  11 142 ? 11.067  -144.347 -13.337 1.00 144.99 ? 143 ASN   K ND2 1 
ATOM   18985 N  N   . TYR   K  11 143 ? 14.403  -140.057 -12.536 1.00 136.77 ? 144 TYR   K N   1 
ATOM   18986 C  CA  . TYR   K  11 143 ? 14.612  -138.588 -12.640 1.00 139.74 ? 144 TYR   K CA  1 
ATOM   18987 C  C   . TYR   K  11 143 ? 15.170  -138.232 -14.021 1.00 145.15 ? 144 TYR   K C   1 
ATOM   18988 O  O   . TYR   K  11 143 ? 16.149  -138.855 -14.476 1.00 150.90 ? 144 TYR   K O   1 
ATOM   18989 C  CB  . TYR   K  11 143 ? 15.555  -138.053 -11.558 1.00 135.89 ? 144 TYR   K CB  1 
ATOM   18990 C  CG  . TYR   K  11 143 ? 15.850  -136.577 -11.677 1.00 135.51 ? 144 TYR   K CG  1 
ATOM   18991 C  CD1 . TYR   K  11 143 ? 14.989  -135.628 -11.146 1.00 130.45 ? 144 TYR   K CD1 1 
ATOM   18992 C  CD2 . TYR   K  11 143 ? 16.982  -136.122 -12.338 1.00 134.84 ? 144 TYR   K CD2 1 
ATOM   18993 C  CE1 . TYR   K  11 143 ? 15.249  -134.271 -11.257 1.00 128.44 ? 144 TYR   K CE1 1 
ATOM   18994 C  CE2 . TYR   K  11 143 ? 17.256  -134.769 -12.459 1.00 132.23 ? 144 TYR   K CE2 1 
ATOM   18995 C  CZ  . TYR   K  11 143 ? 16.387  -133.839 -11.916 1.00 127.63 ? 144 TYR   K CZ  1 
ATOM   18996 O  OH  . TYR   K  11 143 ? 16.649  -132.505 -12.030 1.00 122.29 ? 144 TYR   K OH  1 
ATOM   18997 N  N   . LYS   K  11 144 ? 14.534  -137.249 -14.659 1.00 147.22 ? 145 LYS   K N   1 
ATOM   18998 C  CA  . LYS   K  11 144 ? 15.073  -136.454 -15.793 1.00 147.76 ? 145 LYS   K CA  1 
ATOM   18999 C  C   . LYS   K  11 144 ? 14.742  -134.986 -15.503 1.00 144.55 ? 145 LYS   K C   1 
ATOM   19000 O  O   . LYS   K  11 144 ? 13.744  -134.739 -14.795 1.00 131.99 ? 145 LYS   K O   1 
ATOM   19001 C  CB  . LYS   K  11 144 ? 14.473  -136.923 -17.124 1.00 153.45 ? 145 LYS   K CB  1 
ATOM   19002 C  CG  . LYS   K  11 144 ? 14.858  -138.329 -17.568 1.00 156.44 ? 145 LYS   K CG  1 
ATOM   19003 C  CD  . LYS   K  11 144 ? 13.993  -138.852 -18.697 1.00 159.82 ? 145 LYS   K CD  1 
ATOM   19004 C  CE  . LYS   K  11 144 ? 14.440  -140.199 -19.224 1.00 160.68 ? 145 LYS   K CE  1 
ATOM   19005 N  NZ  . LYS   K  11 144 ? 13.468  -140.753 -20.195 1.00 162.69 ? 145 LYS   K NZ  1 
ATOM   19006 N  N   . TRP   K  11 145 ? 15.551  -134.048 -16.004 1.00 144.75 ? 146 TRP   K N   1 
ATOM   19007 C  CA  . TRP   K  11 145 ? 15.327  -132.587 -15.824 1.00 145.17 ? 146 TRP   K CA  1 
ATOM   19008 C  C   . TRP   K  11 145 ? 14.000  -132.170 -16.472 1.00 147.15 ? 146 TRP   K C   1 
ATOM   19009 O  O   . TRP   K  11 145 ? 13.351  -131.241 -15.943 1.00 140.37 ? 146 TRP   K O   1 
ATOM   19010 C  CB  . TRP   K  11 145 ? 16.492  -131.769 -16.394 1.00 146.54 ? 146 TRP   K CB  1 
ATOM   19011 C  CG  . TRP   K  11 145 ? 16.247  -130.293 -16.327 1.00 147.45 ? 146 TRP   K CG  1 
ATOM   19012 C  CD1 . TRP   K  11 145 ? 15.723  -129.498 -17.306 1.00 150.44 ? 146 TRP   K CD1 1 
ATOM   19013 C  CD2 . TRP   K  11 145 ? 16.473  -129.435 -15.195 1.00 147.65 ? 146 TRP   K CD2 1 
ATOM   19014 N  NE1 . TRP   K  11 145 ? 15.626  -128.204 -16.869 1.00 147.74 ? 146 TRP   K NE1 1 
ATOM   19015 C  CE2 . TRP   K  11 145 ? 16.078  -128.133 -15.578 1.00 146.47 ? 146 TRP   K CE2 1 
ATOM   19016 C  CE3 . TRP   K  11 145 ? 16.979  -129.635 -13.905 1.00 146.82 ? 146 TRP   K CE3 1 
ATOM   19017 C  CZ2 . TRP   K  11 145 ? 16.176  -127.043 -14.713 1.00 144.48 ? 146 TRP   K CZ2 1 
ATOM   19018 C  CZ3 . TRP   K  11 145 ? 17.076  -128.557 -13.051 1.00 144.24 ? 146 TRP   K CZ3 1 
ATOM   19019 C  CH2 . TRP   K  11 145 ? 16.679  -127.279 -13.452 1.00 142.95 ? 146 TRP   K CH2 1 
ATOM   19020 N  N   . ASP   K  11 146 ? 13.619  -132.839 -17.566 1.00 150.80 ? 147 ASP   K N   1 
ATOM   19021 C  CA  . ASP   K  11 146 ? 12.530  -132.419 -18.491 1.00 151.23 ? 147 ASP   K CA  1 
ATOM   19022 C  C   . ASP   K  11 146 ? 11.175  -132.994 -18.055 1.00 147.15 ? 147 ASP   K C   1 
ATOM   19023 O  O   . ASP   K  11 146 ? 10.215  -132.848 -18.836 1.00 147.33 ? 147 ASP   K O   1 
ATOM   19024 C  CB  . ASP   K  11 146 ? 12.868  -132.833 -19.925 1.00 154.70 ? 147 ASP   K CB  1 
ATOM   19025 C  CG  . ASP   K  11 146 ? 14.219  -132.318 -20.387 1.00 157.28 ? 147 ASP   K CG  1 
ATOM   19026 O  OD1 . ASP   K  11 146 ? 14.398  -131.084 -20.403 1.00 159.06 ? 147 ASP   K OD1 1 
ATOM   19027 O  OD2 . ASP   K  11 146 ? 15.089  -133.153 -20.702 1.00 160.29 ? 147 ASP   K OD2 1 
ATOM   19028 N  N   . LEU   K  11 147 ? 11.087  -133.610 -16.867 1.00 146.42 ? 148 LEU   K N   1 
ATOM   19029 C  CA  . LEU   K  11 147 ? 9.807   -134.101 -16.279 1.00 141.22 ? 148 LEU   K CA  1 
ATOM   19030 C  C   . LEU   K  11 147 ? 8.763   -132.978 -16.350 1.00 134.69 ? 148 LEU   K C   1 
ATOM   19031 O  O   . LEU   K  11 147 ? 9.125   -131.809 -16.102 1.00 124.63 ? 148 LEU   K O   1 
ATOM   19032 C  CB  . LEU   K  11 147 ? 10.027  -134.557 -14.828 1.00 142.11 ? 148 LEU   K CB  1 
ATOM   19033 C  CG  . LEU   K  11 147 ? 10.182  -136.062 -14.589 1.00 146.42 ? 148 LEU   K CG  1 
ATOM   19034 C  CD1 . LEU   K  11 147 ? 11.088  -136.720 -15.620 1.00 152.31 ? 148 LEU   K CD1 1 
ATOM   19035 C  CD2 . LEU   K  11 147 ? 10.706  -136.328 -13.184 1.00 145.26 ? 148 LEU   K CD2 1 
ATOM   19036 N  N   . SER   K  11 148 ? 7.520   -133.322 -16.697 1.00 134.07 ? 149 SER   K N   1 
ATOM   19037 C  CA  . SER   K  11 148 ? 6.347   -132.415 -16.620 1.00 135.79 ? 149 SER   K CA  1 
ATOM   19038 C  C   . SER   K  11 148 ? 6.022   -132.166 -15.144 1.00 133.55 ? 149 SER   K C   1 
ATOM   19039 O  O   . SER   K  11 148 ? 6.433   -132.992 -14.306 1.00 133.59 ? 149 SER   K O   1 
ATOM   19040 C  CB  . SER   K  11 148 ? 5.158   -132.974 -17.363 1.00 140.03 ? 149 SER   K CB  1 
ATOM   19041 O  OG  . SER   K  11 148 ? 4.722   -134.195 -16.784 1.00 138.10 ? 149 SER   K OG  1 
ATOM   19042 N  N   . VAL   K  11 149 ? 5.325   -131.070 -14.840 1.00 131.43 ? 150 VAL   K N   1 
ATOM   19043 C  CA  . VAL   K  11 149 ? 4.848   -130.737 -13.464 1.00 131.45 ? 150 VAL   K CA  1 
ATOM   19044 C  C   . VAL   K  11 149 ? 4.034   -131.916 -12.917 1.00 133.92 ? 150 VAL   K C   1 
ATOM   19045 O  O   . VAL   K  11 149 ? 4.214   -132.257 -11.729 1.00 135.98 ? 150 VAL   K O   1 
ATOM   19046 C  CB  . VAL   K  11 149 ? 4.023   -129.436 -13.454 1.00 134.73 ? 150 VAL   K CB  1 
ATOM   19047 C  CG1 . VAL   K  11 149 ? 3.134   -129.331 -12.223 1.00 133.38 ? 150 VAL   K CG1 1 
ATOM   19048 C  CG2 . VAL   K  11 149 ? 4.919   -128.214 -13.577 1.00 135.89 ? 150 VAL   K CG2 1 
ATOM   19049 N  N   . GLU   K  11 150 ? 3.174   -132.504 -13.755 1.00 136.72 ? 151 GLU   K N   1 
ATOM   19050 C  CA  . GLU   K  11 150 ? 2.295   -133.651 -13.398 1.00 136.38 ? 151 GLU   K CA  1 
ATOM   19051 C  C   . GLU   K  11 150 ? 3.162   -134.859 -13.022 1.00 131.58 ? 151 GLU   K C   1 
ATOM   19052 O  O   . GLU   K  11 150 ? 2.903   -135.455 -11.960 1.00 125.99 ? 151 GLU   K O   1 
ATOM   19053 C  CB  . GLU   K  11 150 ? 1.360   -133.982 -14.562 1.00 139.08 ? 151 GLU   K CB  1 
ATOM   19054 C  CG  . GLU   K  11 150 ? 0.187   -134.862 -14.172 1.00 139.98 ? 151 GLU   K CG  1 
ATOM   19055 C  CD  . GLU   K  11 150 ? -0.629  -135.383 -15.344 1.00 144.00 ? 151 GLU   K CD  1 
ATOM   19056 O  OE1 . GLU   K  11 150 ? -1.835  -135.632 -15.157 1.00 146.13 ? 151 GLU   K OE1 1 
ATOM   19057 O  OE2 . GLU   K  11 150 ? -0.057  -135.543 -16.442 1.00 146.46 ? 151 GLU   K OE2 1 
ATOM   19058 N  N   . ASP   K  11 151 ? 4.157   -135.187 -13.857 1.00 132.96 ? 152 ASP   K N   1 
ATOM   19059 C  CA  . ASP   K  11 151 ? 5.050   -136.368 -13.695 1.00 131.67 ? 152 ASP   K CA  1 
ATOM   19060 C  C   . ASP   K  11 151 ? 5.962   -136.163 -12.478 1.00 129.54 ? 152 ASP   K C   1 
ATOM   19061 O  O   . ASP   K  11 151 ? 6.117   -137.126 -11.695 1.00 130.29 ? 152 ASP   K O   1 
ATOM   19062 C  CB  . ASP   K  11 151 ? 5.863   -136.637 -14.967 1.00 135.97 ? 152 ASP   K CB  1 
ATOM   19063 C  CG  . ASP   K  11 151 ? 5.046   -137.167 -16.138 1.00 138.61 ? 152 ASP   K CG  1 
ATOM   19064 O  OD1 . ASP   K  11 151 ? 3.961   -137.733 -15.895 1.00 141.30 ? 152 ASP   K OD1 1 
ATOM   19065 O  OD2 . ASP   K  11 151 ? 5.502   -137.008 -17.288 1.00 137.52 ? 152 ASP   K OD2 1 
ATOM   19066 N  N   . ALA   K  11 152 ? 6.540   -134.966 -12.327 1.00 123.24 ? 153 ALA   K N   1 
ATOM   19067 C  CA  . ALA   K  11 152 ? 7.443   -134.595 -11.210 1.00 118.59 ? 153 ALA   K CA  1 
ATOM   19068 C  C   . ALA   K  11 152 ? 6.712   -134.756 -9.870  1.00 117.55 ? 153 ALA   K C   1 
ATOM   19069 O  O   . ALA   K  11 152 ? 7.321   -135.303 -8.926  1.00 117.31 ? 153 ALA   K O   1 
ATOM   19070 C  CB  . ALA   K  11 152 ? 7.954   -133.189 -11.393 1.00 116.80 ? 153 ALA   K CB  1 
ATOM   19071 N  N   . LEU   K  11 153 ? 5.456   -134.307 -9.795  1.00 114.98 ? 154 LEU   K N   1 
ATOM   19072 C  CA  . LEU   K  11 153 ? 4.598   -134.441 -8.585  1.00 114.03 ? 154 LEU   K CA  1 
ATOM   19073 C  C   . LEU   K  11 153 ? 4.426   -135.922 -8.229  1.00 112.88 ? 154 LEU   K C   1 
ATOM   19074 O  O   . LEU   K  11 153 ? 4.612   -136.260 -7.044  1.00 112.46 ? 154 LEU   K O   1 
ATOM   19075 C  CB  . LEU   K  11 153 ? 3.241   -133.775 -8.835  1.00 117.50 ? 154 LEU   K CB  1 
ATOM   19076 C  CG  . LEU   K  11 153 ? 3.200   -132.268 -8.589  1.00 118.87 ? 154 LEU   K CG  1 
ATOM   19077 C  CD1 . LEU   K  11 153 ? 1.994   -131.636 -9.265  1.00 122.58 ? 154 LEU   K CD1 1 
ATOM   19078 C  CD2 . LEU   K  11 153 ? 3.191   -131.965 -7.098  1.00 115.00 ? 154 LEU   K CD2 1 
ATOM   19079 N  N   . TYR   K  11 154 ? 4.090   -136.767 -9.211  1.00 112.13 ? 155 TYR   K N   1 
ATOM   19080 C  CA  . TYR   K  11 154 ? 3.909   -138.231 -9.025  1.00 112.43 ? 155 TYR   K CA  1 
ATOM   19081 C  C   . TYR   K  11 154 ? 5.217   -138.832 -8.493  1.00 110.07 ? 155 TYR   K C   1 
ATOM   19082 O  O   . TYR   K  11 154 ? 5.161   -139.519 -7.455  1.00 108.92 ? 155 TYR   K O   1 
ATOM   19083 C  CB  . TYR   K  11 154 ? 3.448   -138.914 -10.318 1.00 113.56 ? 155 TYR   K CB  1 
ATOM   19084 C  CG  . TYR   K  11 154 ? 3.165   -140.390 -10.179 1.00 113.99 ? 155 TYR   K CG  1 
ATOM   19085 C  CD1 . TYR   K  11 154 ? 2.017   -140.841 -9.547  1.00 114.38 ? 155 TYR   K CD1 1 
ATOM   19086 C  CD2 . TYR   K  11 154 ? 4.048   -141.340 -10.671 1.00 113.81 ? 155 TYR   K CD2 1 
ATOM   19087 C  CE1 . TYR   K  11 154 ? 1.751   -142.194 -9.408  1.00 116.63 ? 155 TYR   K CE1 1 
ATOM   19088 C  CE2 . TYR   K  11 154 ? 3.799   -142.697 -10.539 1.00 116.51 ? 155 TYR   K CE2 1 
ATOM   19089 C  CZ  . TYR   K  11 154 ? 2.646   -143.125 -9.905  1.00 119.26 ? 155 TYR   K CZ  1 
ATOM   19090 O  OH  . TYR   K  11 154 ? 2.386   -144.458 -9.771  1.00 123.61 ? 155 TYR   K OH  1 
ATOM   19091 N  N   . LEU   K  11 155 ? 6.349   -138.562 -9.157  1.00 109.27 ? 156 LEU   K N   1 
ATOM   19092 C  CA  . LEU   K  11 155 ? 7.663   -139.181 -8.824  1.00 110.34 ? 156 LEU   K CA  1 
ATOM   19093 C  C   . LEU   K  11 155 ? 8.018   -138.871 -7.366  1.00 108.58 ? 156 LEU   K C   1 
ATOM   19094 O  O   . LEU   K  11 155 ? 8.400   -139.807 -6.637  1.00 110.77 ? 156 LEU   K O   1 
ATOM   19095 C  CB  . LEU   K  11 155 ? 8.756   -138.680 -9.774  1.00 114.09 ? 156 LEU   K CB  1 
ATOM   19096 C  CG  . LEU   K  11 155 ? 10.151  -139.262 -9.529  1.00 118.09 ? 156 LEU   K CG  1 
ATOM   19097 C  CD1 . LEU   K  11 155 ? 10.120  -140.786 -9.449  1.00 121.93 ? 156 LEU   K CD1 1 
ATOM   19098 C  CD2 . LEU   K  11 155 ? 11.127  -138.816 -10.606 1.00 119.17 ? 156 LEU   K CD2 1 
ATOM   19099 N  N   . GLY   K  11 156 ? 7.899   -137.606 -6.963  1.00 105.23 ? 157 GLY   K N   1 
ATOM   19100 C  CA  . GLY   K  11 156 ? 8.103   -137.179 -5.567  1.00 103.68 ? 157 GLY   K CA  1 
ATOM   19101 C  C   . GLY   K  11 156 ? 7.202   -137.954 -4.621  1.00 101.97 ? 157 GLY   K C   1 
ATOM   19102 O  O   . GLY   K  11 156 ? 7.703   -138.419 -3.579  1.00 102.57 ? 157 GLY   K O   1 
ATOM   19103 N  N   . LYS   K  11 157 ? 5.922   -138.096 -4.979  1.00 101.68 ? 158 LYS   K N   1 
ATOM   19104 C  CA  . LYS   K  11 157 ? 4.905   -138.848 -4.197  1.00 104.22 ? 158 LYS   K CA  1 
ATOM   19105 C  C   . LYS   K  11 157 ? 5.286   -140.332 -4.156  1.00 103.40 ? 158 LYS   K C   1 
ATOM   19106 O  O   . LYS   K  11 157 ? 5.222   -140.927 -3.065  1.00 107.36 ? 158 LYS   K O   1 
ATOM   19107 C  CB  . LYS   K  11 157 ? 3.513   -138.675 -4.813  1.00 105.78 ? 158 LYS   K CB  1 
ATOM   19108 C  CG  . LYS   K  11 157 ? 2.358   -139.203 -3.973  1.00 105.49 ? 158 LYS   K CG  1 
ATOM   19109 C  CD  . LYS   K  11 157 ? 1.153   -139.601 -4.793  1.00 110.56 ? 158 LYS   K CD  1 
ATOM   19110 C  CE  . LYS   K  11 157 ? 0.432   -138.419 -5.404  1.00 114.20 ? 158 LYS   K CE  1 
ATOM   19111 N  NZ  . LYS   K  11 157 ? -0.686  -138.855 -6.273  1.00 119.78 ? 158 LYS   K NZ  1 
ATOM   19112 N  N   . ARG   K  11 158 ? 5.665   -140.901 -5.304  1.00 105.84 ? 159 ARG   K N   1 
ATOM   19113 C  CA  . ARG   K  11 158 ? 5.972   -142.347 -5.464  1.00 106.44 ? 159 ARG   K CA  1 
ATOM   19114 C  C   . ARG   K  11 158 ? 7.248   -142.697 -4.686  1.00 104.86 ? 159 ARG   K C   1 
ATOM   19115 O  O   . ARG   K  11 158 ? 7.317   -143.825 -4.159  1.00 105.71 ? 159 ARG   K O   1 
ATOM   19116 C  CB  . ARG   K  11 158 ? 6.104   -142.708 -6.948  1.00 110.44 ? 159 ARG   K CB  1 
ATOM   19117 C  CG  . ARG   K  11 158 ? 6.358   -144.186 -7.219  1.00 114.42 ? 159 ARG   K CG  1 
ATOM   19118 C  CD  . ARG   K  11 158 ? 5.239   -145.093 -6.733  1.00 117.41 ? 159 ARG   K CD  1 
ATOM   19119 N  NE  . ARG   K  11 158 ? 5.509   -146.510 -6.952  1.00 119.67 ? 159 ARG   K NE  1 
ATOM   19120 C  CZ  . ARG   K  11 158 ? 6.337   -147.259 -6.225  1.00 120.34 ? 159 ARG   K CZ  1 
ATOM   19121 N  NH1 . ARG   K  11 158 ? 7.016   -146.735 -5.216  1.00 119.83 ? 159 ARG   K NH1 1 
ATOM   19122 N  NH2 . ARG   K  11 158 ? 6.490   -148.540 -6.513  1.00 122.49 ? 159 ARG   K NH2 1 
ATOM   19123 N  N   . SER   K  11 159 ? 8.215   -141.777 -4.616  1.00 98.71  ? 160 SER   K N   1 
ATOM   19124 C  CA  . SER   K  11 159 ? 9.521   -141.980 -3.933  1.00 96.36  ? 160 SER   K CA  1 
ATOM   19125 C  C   . SER   K  11 159 ? 9.327   -142.033 -2.412  1.00 94.46  ? 160 SER   K C   1 
ATOM   19126 O  O   . SER   K  11 159 ? 10.058  -142.803 -1.757  1.00 89.79  ? 160 SER   K O   1 
ATOM   19127 C  CB  . SER   K  11 159 ? 10.516  -140.919 -4.321  1.00 95.58  ? 160 SER   K CB  1 
ATOM   19128 O  OG  . SER   K  11 159 ? 10.742  -140.924 -5.723  1.00 95.94  ? 160 SER   K OG  1 
ATOM   19129 N  N   . ILE   K  11 160 ? 8.398   -141.238 -1.869  1.00 93.68  ? 161 ILE   K N   1 
ATOM   19130 C  CA  . ILE   K  11 160 ? 8.008   -141.284 -0.427  1.00 93.80  ? 161 ILE   K CA  1 
ATOM   19131 C  C   . ILE   K  11 160 ? 7.326   -142.630 -0.160  1.00 96.09  ? 161 ILE   K C   1 
ATOM   19132 O  O   . ILE   K  11 160 ? 7.719   -143.298 0.814   1.00 97.06  ? 161 ILE   K O   1 
ATOM   19133 C  CB  . ILE   K  11 160 ? 7.113   -140.090 -0.030  1.00 93.29  ? 161 ILE   K CB  1 
ATOM   19134 C  CG1 . ILE   K  11 160 ? 7.887   -138.770 -0.043  1.00 93.28  ? 161 ILE   K CG1 1 
ATOM   19135 C  CG2 . ILE   K  11 160 ? 6.452   -140.329 1.321   1.00 93.04  ? 161 ILE   K CG2 1 
ATOM   19136 C  CD1 . ILE   K  11 160 ? 8.949   -138.659 1.034   1.00 92.72  ? 161 ILE   K CD1 1 
ATOM   19137 N  N   . LEU   K  11 161 ? 6.357   -143.010 -1.000  1.00 96.89  ? 162 LEU   K N   1 
ATOM   19138 C  CA  . LEU   K  11 161 ? 5.591   -144.283 -0.881  1.00 99.57  ? 162 LEU   K CA  1 
ATOM   19139 C  C   . LEU   K  11 161 ? 6.557   -145.476 -0.846  1.00 99.64  ? 162 LEU   K C   1 
ATOM   19140 O  O   . LEU   K  11 161 ? 6.338   -146.383 -0.017  1.00 100.67 ? 162 LEU   K O   1 
ATOM   19141 C  CB  . LEU   K  11 161 ? 4.614   -144.409 -2.056  1.00 102.70 ? 162 LEU   K CB  1 
ATOM   19142 C  CG  . LEU   K  11 161 ? 3.761   -145.680 -2.074  1.00 102.99 ? 162 LEU   K CG  1 
ATOM   19143 C  CD1 . LEU   K  11 161 ? 2.920   -145.798 -0.810  1.00 102.46 ? 162 LEU   K CD1 1 
ATOM   19144 C  CD2 . LEU   K  11 161 ? 2.870   -145.715 -3.306  1.00 103.89 ? 162 LEU   K CD2 1 
ATOM   19145 N  N   . ALA   K  11 162 ? 7.571   -145.472 -1.718  1.00 95.19  ? 163 ALA   K N   1 
ATOM   19146 C  CA  . ALA   K  11 162 ? 8.636   -146.500 -1.799  1.00 95.28  ? 163 ALA   K CA  1 
ATOM   19147 C  C   . ALA   K  11 162 ? 9.298   -146.680 -0.429  1.00 96.07  ? 163 ALA   K C   1 
ATOM   19148 O  O   . ALA   K  11 162 ? 9.409   -147.833 0.028   1.00 96.93  ? 163 ALA   K O   1 
ATOM   19149 C  CB  . ALA   K  11 162 ? 9.652   -146.106 -2.838  1.00 93.99  ? 163 ALA   K CB  1 
ATOM   19150 N  N   . ALA   K  11 163 ? 9.719   -145.575 0.189   1.00 95.30  ? 164 ALA   K N   1 
ATOM   19151 C  CA  . ALA   K  11 163 ? 10.389  -145.545 1.508   1.00 95.52  ? 164 ALA   K CA  1 
ATOM   19152 C  C   . ALA   K  11 163 ? 9.384   -145.925 2.600   1.00 98.11  ? 164 ALA   K C   1 
ATOM   19153 O  O   . ALA   K  11 163 ? 9.714   -146.815 3.407   1.00 100.48 ? 164 ALA   K O   1 
ATOM   19154 C  CB  . ALA   K  11 163 ? 10.987  -144.185 1.751   1.00 95.29  ? 164 ALA   K CB  1 
ATOM   19155 N  N   . ALA   K  11 164 ? 8.207   -145.285 2.610   1.00 98.47  ? 165 ALA   K N   1 
ATOM   19156 C  CA  . ALA   K  11 164 ? 7.113   -145.516 3.588   1.00 99.84  ? 165 ALA   K CA  1 
ATOM   19157 C  C   . ALA   K  11 164 ? 6.868   -147.019 3.727   1.00 100.17 ? 165 ALA   K C   1 
ATOM   19158 O  O   . ALA   K  11 164 ? 6.672   -147.495 4.861   1.00 101.91 ? 165 ALA   K O   1 
ATOM   19159 C  CB  . ALA   K  11 164 ? 5.852   -144.809 3.157   1.00 100.01 ? 165 ALA   K CB  1 
ATOM   19160 N  N   . HIS   K  11 165 ? 6.897   -147.729 2.600   1.00 98.47  ? 166 HIS   K N   1 
ATOM   19161 C  CA  . HIS   K  11 165 ? 6.680   -149.194 2.511   1.00 101.17 ? 166 HIS   K CA  1 
ATOM   19162 C  C   . HIS   K  11 165 ? 7.859   -149.954 3.137   1.00 100.55 ? 166 HIS   K C   1 
ATOM   19163 O  O   . HIS   K  11 165 ? 7.600   -150.832 3.980   1.00 101.50 ? 166 HIS   K O   1 
ATOM   19164 C  CB  . HIS   K  11 165 ? 6.419   -149.586 1.052   1.00 102.99 ? 166 HIS   K CB  1 
ATOM   19165 C  CG  . HIS   K  11 165 ? 6.222   -151.048 0.837   1.00 106.57 ? 166 HIS   K CG  1 
ATOM   19166 N  ND1 . HIS   K  11 165 ? 5.301   -151.781 1.558   1.00 109.90 ? 166 HIS   K ND1 1 
ATOM   19167 C  CD2 . HIS   K  11 165 ? 6.803   -151.911 -0.024  1.00 108.96 ? 166 HIS   K CD2 1 
ATOM   19168 C  CE1 . HIS   K  11 165 ? 5.331   -153.035 1.160   1.00 110.74 ? 166 HIS   K CE1 1 
ATOM   19169 N  NE2 . HIS   K  11 165 ? 6.243   -153.141 0.185   1.00 110.44 ? 166 HIS   K NE2 1 
ATOM   19170 N  N   . ARG   K  11 166 ? 9.101   -149.630 2.759   1.00 100.42 ? 167 ARG   K N   1 
ATOM   19171 C  CA  . ARG   K  11 166 ? 10.302  -150.432 3.127   1.00 99.82  ? 167 ARG   K CA  1 
ATOM   19172 C  C   . ARG   K  11 166 ? 10.841  -150.025 4.505   1.00 101.42 ? 167 ARG   K C   1 
ATOM   19173 O  O   . ARG   K  11 166 ? 11.081  -150.943 5.321   1.00 100.81 ? 167 ARG   K O   1 
ATOM   19174 C  CB  . ARG   K  11 166 ? 11.383  -150.329 2.047   1.00 98.52  ? 167 ARG   K CB  1 
ATOM   19175 C  CG  . ARG   K  11 166 ? 11.147  -151.260 0.867   1.00 98.94  ? 167 ARG   K CG  1 
ATOM   19176 C  CD  . ARG   K  11 166 ? 11.399  -152.716 1.214   1.00 98.91  ? 167 ARG   K CD  1 
ATOM   19177 N  NE  . ARG   K  11 166 ? 11.090  -153.619 0.110   1.00 100.22 ? 167 ARG   K NE  1 
ATOM   19178 C  CZ  . ARG   K  11 166 ? 11.248  -154.942 0.133   1.00 101.40 ? 167 ARG   K CZ  1 
ATOM   19179 N  NH1 . ARG   K  11 166 ? 11.718  -155.551 1.210   1.00 99.08  ? 167 ARG   K NH1 1 
ATOM   19180 N  NH2 . ARG   K  11 166 ? 10.934  -155.657 -0.933  1.00 101.28 ? 167 ARG   K NH2 1 
ATOM   19181 N  N   . ASP   K  11 167 ? 11.037  -148.725 4.754   1.00 100.30 ? 168 ASP   K N   1 
ATOM   19182 C  CA  . ASP   K  11 167 ? 11.529  -148.200 6.058   1.00 101.48 ? 168 ASP   K CA  1 
ATOM   19183 C  C   . ASP   K  11 167 ? 10.393  -148.332 7.078   1.00 98.99  ? 168 ASP   K C   1 
ATOM   19184 O  O   . ASP   K  11 167 ? 9.272   -147.879 6.776   1.00 97.21  ? 168 ASP   K O   1 
ATOM   19185 C  CB  . ASP   K  11 167 ? 12.052  -146.764 5.933   1.00 102.79 ? 168 ASP   K CB  1 
ATOM   19186 C  CG  . ASP   K  11 167 ? 12.608  -146.170 7.221   1.00 103.35 ? 168 ASP   K CG  1 
ATOM   19187 O  OD1 . ASP   K  11 167 ? 12.896  -146.948 8.156   1.00 110.24 ? 168 ASP   K OD1 1 
ATOM   19188 O  OD2 . ASP   K  11 167 ? 12.763  -144.932 7.276   1.00 102.36 ? 168 ASP   K OD2 1 
ATOM   19189 N  N   . ALA   K  11 168 ? 10.673  -148.960 8.223   1.00 100.13 ? 169 ALA   K N   1 
ATOM   19190 C  CA  . ALA   K  11 168 ? 9.710   -149.208 9.322   1.00 101.74 ? 169 ALA   K CA  1 
ATOM   19191 C  C   . ALA   K  11 168 ? 9.344   -147.887 10.013  1.00 102.00 ? 169 ALA   K C   1 
ATOM   19192 O  O   . ALA   K  11 168 ? 8.203   -147.785 10.507  1.00 104.07 ? 169 ALA   K O   1 
ATOM   19193 C  CB  . ALA   K  11 168 ? 10.293  -150.204 10.297  1.00 103.07 ? 169 ALA   K CB  1 
ATOM   19194 N  N   . TYR   K  11 169 ? 10.269  -146.918 10.032  1.00 100.19 ? 170 TYR   K N   1 
ATOM   19195 C  CA  . TYR   K  11 169 ? 10.149  -145.624 10.757  1.00 100.38 ? 170 TYR   K CA  1 
ATOM   19196 C  C   . TYR   K  11 169 ? 9.579   -144.548 9.820   1.00 96.53  ? 170 TYR   K C   1 
ATOM   19197 O  O   . TYR   K  11 169 ? 9.375   -143.405 10.277  1.00 98.07  ? 170 TYR   K O   1 
ATOM   19198 C  CB  . TYR   K  11 169 ? 11.507  -145.256 11.365  1.00 99.60  ? 170 TYR   K CB  1 
ATOM   19199 C  CG  . TYR   K  11 169 ? 12.095  -146.346 12.224  1.00 100.90 ? 170 TYR   K CG  1 
ATOM   19200 C  CD1 . TYR   K  11 169 ? 11.361  -146.901 13.260  1.00 104.40 ? 170 TYR   K CD1 1 
ATOM   19201 C  CD2 . TYR   K  11 169 ? 13.369  -146.842 11.992  1.00 102.14 ? 170 TYR   K CD2 1 
ATOM   19202 C  CE1 . TYR   K  11 169 ? 11.878  -147.914 14.052  1.00 106.36 ? 170 TYR   K CE1 1 
ATOM   19203 C  CE2 . TYR   K  11 169 ? 13.902  -147.854 12.775  1.00 103.98 ? 170 TYR   K CE2 1 
ATOM   19204 C  CZ  . TYR   K  11 169 ? 13.154  -148.390 13.808  1.00 106.65 ? 170 TYR   K CZ  1 
ATOM   19205 O  OH  . TYR   K  11 169 ? 13.673  -149.385 14.583  1.00 108.21 ? 170 TYR   K OH  1 
ATOM   19206 N  N   . SER   K  11 170 ? 9.315   -144.909 8.559   1.00 92.12  ? 171 SER   K N   1 
ATOM   19207 C  CA  . SER   K  11 170 ? 8.647   -144.068 7.529   1.00 89.58  ? 171 SER   K CA  1 
ATOM   19208 C  C   . SER   K  11 170 ? 7.211   -144.556 7.319   1.00 90.61  ? 171 SER   K C   1 
ATOM   19209 O  O   . SER   K  11 170 ? 6.989   -145.773 7.430   1.00 89.91  ? 171 SER   K O   1 
ATOM   19210 C  CB  . SER   K  11 170 ? 9.404   -144.114 6.234   1.00 89.29  ? 171 SER   K CB  1 
ATOM   19211 O  OG  . SER   K  11 170 ? 10.723  -143.621 6.397   1.00 88.67  ? 171 SER   K OG  1 
ATOM   19212 N  N   . GLY   K  11 171 ? 6.278   -143.651 7.012   1.00 90.39  ? 172 GLY   K N   1 
ATOM   19213 C  CA  . GLY   K  11 171 ? 4.879   -144.015 6.712   1.00 94.70  ? 172 GLY   K CA  1 
ATOM   19214 C  C   . GLY   K  11 171 ? 3.894   -142.890 6.978   1.00 98.44  ? 172 GLY   K C   1 
ATOM   19215 O  O   . GLY   K  11 171 ? 4.294   -141.709 6.898   1.00 102.10 ? 172 GLY   K O   1 
ATOM   19216 N  N   . GLY   K  11 172 ? 2.642   -143.257 7.276   1.00 98.92  ? 173 GLY   K N   1 
ATOM   19217 C  CA  . GLY   K  11 172 ? 1.530   -142.327 7.548   1.00 97.37  ? 173 GLY   K CA  1 
ATOM   19218 C  C   . GLY   K  11 172 ? 0.877   -141.856 6.263   1.00 96.20  ? 173 GLY   K C   1 
ATOM   19219 O  O   . GLY   K  11 172 ? 0.017   -142.585 5.736   1.00 92.17  ? 173 GLY   K O   1 
ATOM   19220 N  N   . SER   K  11 173 ? 1.280   -140.680 5.778   1.00 97.32  ? 174 SER   K N   1 
ATOM   19221 C  CA  . SER   K  11 173 ? 0.759   -140.041 4.544   1.00 99.09  ? 174 SER   K CA  1 
ATOM   19222 C  C   . SER   K  11 173 ? 1.897   -139.311 3.826   1.00 99.99  ? 174 SER   K C   1 
ATOM   19223 O  O   . SER   K  11 173 ? 2.985   -139.180 4.419   1.00 97.87  ? 174 SER   K O   1 
ATOM   19224 C  CB  . SER   K  11 173 ? -0.387  -139.117 4.868   1.00 101.14 ? 174 SER   K CB  1 
ATOM   19225 O  OG  . SER   K  11 173 ? 0.017   -138.108 5.779   1.00 102.72 ? 174 SER   K OG  1 
ATOM   19226 N  N   . VAL   K  11 174 ? 1.647   -138.877 2.589   1.00 102.37 ? 175 VAL   K N   1 
ATOM   19227 C  CA  . VAL   K  11 174 ? 2.574   -138.036 1.779   1.00 103.29 ? 175 VAL   K CA  1 
ATOM   19228 C  C   . VAL   K  11 174 ? 2.003   -136.616 1.738   1.00 104.64 ? 175 VAL   K C   1 
ATOM   19229 O  O   . VAL   K  11 174 ? 0.786   -136.477 1.505   1.00 109.10 ? 175 VAL   K O   1 
ATOM   19230 C  CB  . VAL   K  11 174 ? 2.767   -138.603 0.360   1.00 104.57 ? 175 VAL   K CB  1 
ATOM   19231 C  CG1 . VAL   K  11 174 ? 3.909   -137.911 -0.370  1.00 105.01 ? 175 VAL   K CG1 1 
ATOM   19232 C  CG2 . VAL   K  11 174 ? 2.980   -140.107 0.379   1.00 104.50 ? 175 VAL   K CG2 1 
ATOM   19233 N  N   . ASN   K  11 175 ? 2.853   -135.616 1.982   1.00 103.33 ? 176 ASN   K N   1 
ATOM   19234 C  CA  . ASN   K  11 175 ? 2.532   -134.177 1.807   1.00 103.03 ? 176 ASN   K CA  1 
ATOM   19235 C  C   . ASN   K  11 175 ? 3.347   -133.652 0.623   1.00 103.01 ? 176 ASN   K C   1 
ATOM   19236 O  O   . ASN   K  11 175 ? 4.591   -133.650 0.717   1.00 98.32  ? 176 ASN   K O   1 
ATOM   19237 C  CB  . ASN   K  11 175 ? 2.775   -133.392 3.097   1.00 100.88 ? 176 ASN   K CB  1 
ATOM   19238 C  CG  . ASN   K  11 175 ? 1.673   -133.612 4.112   1.00 100.22 ? 176 ASN   K CG  1 
ATOM   19239 O  OD1 . ASN   K  11 175 ? 1.872   -134.292 5.117   1.00 92.38  ? 176 ASN   K OD1 1 
ATOM   19240 N  ND2 . ASN   K  11 175 ? 0.501   -133.059 3.841   1.00 102.84 ? 176 ASN   K ND2 1 
ATOM   19241 N  N   . LEU   K  11 176 ? 2.660   -133.255 -0.452  1.00 105.57 ? 177 LEU   K N   1 
ATOM   19242 C  CA  . LEU   K  11 176 ? 3.288   -132.728 -1.690  1.00 107.10 ? 177 LEU   K CA  1 
ATOM   19243 C  C   . LEU   K  11 176 ? 3.290   -131.199 -1.648  1.00 106.17 ? 177 LEU   K C   1 
ATOM   19244 O  O   . LEU   K  11 176 ? 2.381   -130.614 -1.025  1.00 103.08 ? 177 LEU   K O   1 
ATOM   19245 C  CB  . LEU   K  11 176 ? 2.534   -133.240 -2.922  1.00 110.79 ? 177 LEU   K CB  1 
ATOM   19246 C  CG  . LEU   K  11 176 ? 3.079   -134.522 -3.548  1.00 112.94 ? 177 LEU   K CG  1 
ATOM   19247 C  CD1 . LEU   K  11 176 ? 2.141   -135.020 -4.639  1.00 116.40 ? 177 LEU   K CD1 1 
ATOM   19248 C  CD2 . LEU   K  11 176 ? 4.480   -134.309 -4.108  1.00 112.23 ? 177 LEU   K CD2 1 
ATOM   19249 N  N   . TYR   K  11 177 ? 4.298   -130.603 -2.286  1.00 108.43 ? 178 TYR   K N   1 
ATOM   19250 C  CA  . TYR   K  11 177 ? 4.439   -129.145 -2.525  1.00 111.18 ? 178 TYR   K CA  1 
ATOM   19251 C  C   . TYR   K  11 177 ? 5.137   -128.923 -3.868  1.00 111.98 ? 178 TYR   K C   1 
ATOM   19252 O  O   . TYR   K  11 177 ? 6.083   -129.674 -4.176  1.00 111.85 ? 178 TYR   K O   1 
ATOM   19253 C  CB  . TYR   K  11 177 ? 5.257   -128.489 -1.412  1.00 108.76 ? 178 TYR   K CB  1 
ATOM   19254 C  CG  . TYR   K  11 177 ? 4.538   -128.322 -0.098  1.00 109.85 ? 178 TYR   K CG  1 
ATOM   19255 C  CD1 . TYR   K  11 177 ? 4.609   -129.295 0.886   1.00 106.50 ? 178 TYR   K CD1 1 
ATOM   19256 C  CD2 . TYR   K  11 177 ? 3.805   -127.177 0.171   1.00 112.31 ? 178 TYR   K CD2 1 
ATOM   19257 C  CE1 . TYR   K  11 177 ? 3.961   -129.140 2.101   1.00 106.52 ? 178 TYR   K CE1 1 
ATOM   19258 C  CE2 . TYR   K  11 177 ? 3.154   -127.004 1.381   1.00 111.95 ? 178 TYR   K CE2 1 
ATOM   19259 C  CZ  . TYR   K  11 177 ? 3.233   -127.990 2.350   1.00 107.76 ? 178 TYR   K CZ  1 
ATOM   19260 O  OH  . TYR   K  11 177 ? 2.595   -127.837 3.546   1.00 109.10 ? 178 TYR   K OH  1 
ATOM   19261 N  N   . HIS   K  11 178 ? 4.685   -127.920 -4.624  1.00 115.64 ? 179 HIS   K N   1 
ATOM   19262 C  CA  . HIS   K  11 178 ? 5.331   -127.428 -5.868  1.00 117.08 ? 179 HIS   K CA  1 
ATOM   19263 C  C   . HIS   K  11 178 ? 5.730   -125.971 -5.644  1.00 115.62 ? 179 HIS   K C   1 
ATOM   19264 O  O   . HIS   K  11 178 ? 4.866   -125.200 -5.207  1.00 115.67 ? 179 HIS   K O   1 
ATOM   19265 C  CB  . HIS   K  11 178 ? 4.397   -127.600 -7.074  1.00 122.76 ? 179 HIS   K CB  1 
ATOM   19266 C  CG  . HIS   K  11 178 ? 4.990   -127.163 -8.373  1.00 125.83 ? 179 HIS   K CG  1 
ATOM   19267 N  ND1 . HIS   K  11 178 ? 4.238   -126.562 -9.366  1.00 127.67 ? 179 HIS   K ND1 1 
ATOM   19268 C  CD2 . HIS   K  11 178 ? 6.254   -127.237 -8.848  1.00 128.32 ? 179 HIS   K CD2 1 
ATOM   19269 C  CE1 . HIS   K  11 178 ? 5.012   -126.298 -10.400 1.00 128.47 ? 179 HIS   K CE1 1 
ATOM   19270 N  NE2 . HIS   K  11 178 ? 6.255   -126.693 -10.104 1.00 129.16 ? 179 HIS   K NE2 1 
ATOM   19271 N  N   . VAL   K  11 179 ? 6.994   -125.632 -5.901  1.00 118.14 ? 180 VAL   K N   1 
ATOM   19272 C  CA  . VAL   K  11 179 ? 7.534   -124.245 -5.798  1.00 122.94 ? 180 VAL   K CA  1 
ATOM   19273 C  C   . VAL   K  11 179 ? 7.801   -123.730 -7.215  1.00 128.22 ? 180 VAL   K C   1 
ATOM   19274 O  O   . VAL   K  11 179 ? 8.605   -124.362 -7.926  1.00 127.65 ? 180 VAL   K O   1 
ATOM   19275 C  CB  . VAL   K  11 179 ? 8.809   -124.185 -4.937  1.00 118.70 ? 180 VAL   K CB  1 
ATOM   19276 C  CG1 . VAL   K  11 179 ? 9.214   -122.751 -4.641  1.00 120.74 ? 180 VAL   K CG1 1 
ATOM   19277 C  CG2 . VAL   K  11 179 ? 8.667   -124.977 -3.646  1.00 116.78 ? 180 VAL   K CG2 1 
ATOM   19278 N  N   . THR   K  11 180 ? 7.145   -122.631 -7.598  1.00 134.12 ? 181 THR   K N   1 
ATOM   19279 C  CA  . THR   K  11 180 ? 7.305   -121.950 -8.911  1.00 137.93 ? 181 THR   K CA  1 
ATOM   19280 C  C   . THR   K  11 180 ? 7.902   -120.559 -8.679  1.00 140.07 ? 181 THR   K C   1 
ATOM   19281 O  O   . THR   K  11 180 ? 8.229   -120.234 -7.514  1.00 133.22 ? 181 THR   K O   1 
ATOM   19282 C  CB  . THR   K  11 180 ? 5.972   -121.895 -9.672  1.00 141.94 ? 181 THR   K CB  1 
ATOM   19283 O  OG1 . THR   K  11 180 ? 5.033   -121.138 -8.907  1.00 136.74 ? 181 THR   K OG1 1 
ATOM   19284 C  CG2 . THR   K  11 180 ? 5.408   -123.270 -9.954  1.00 143.97 ? 181 THR   K CG2 1 
ATOM   19285 N  N   . GLU   K  11 181 ? 8.054   -119.789 -9.761  1.00 147.70 ? 182 GLU   K N   1 
ATOM   19286 C  CA  . GLU   K  11 181 ? 8.441   -118.353 -9.737  1.00 147.07 ? 182 GLU   K CA  1 
ATOM   19287 C  C   . GLU   K  11 181 ? 7.408   -117.541 -8.935  1.00 151.49 ? 182 GLU   K C   1 
ATOM   19288 O  O   . GLU   K  11 181 ? 7.795   -116.481 -8.401  1.00 154.26 ? 182 GLU   K O   1 
ATOM   19289 C  CB  . GLU   K  11 181 ? 8.629   -117.822 -11.163 1.00 152.39 ? 182 GLU   K CB  1 
ATOM   19290 C  CG  . GLU   K  11 181 ? 7.388   -117.892 -12.042 1.00 154.06 ? 182 GLU   K CG  1 
ATOM   19291 C  CD  . GLU   K  11 181 ? 7.606   -117.456 -13.483 1.00 156.40 ? 182 GLU   K CD  1 
ATOM   19292 O  OE1 . GLU   K  11 181 ? 6.634   -117.500 -14.263 1.00 159.95 ? 182 GLU   K OE1 1 
ATOM   19293 O  OE2 . GLU   K  11 181 ? 8.744   -117.073 -13.823 1.00 152.92 ? 182 GLU   K OE2 1 
ATOM   19294 N  N   . ASP   K  11 182 ? 6.162   -118.025 -8.836  1.00 154.30 ? 183 ASP   K N   1 
ATOM   19295 C  CA  . ASP   K  11 182 ? 5.021   -117.325 -8.180  1.00 150.72 ? 183 ASP   K CA  1 
ATOM   19296 C  C   . ASP   K  11 182 ? 4.949   -117.673 -6.682  1.00 140.47 ? 183 ASP   K C   1 
ATOM   19297 O  O   . ASP   K  11 182 ? 4.199   -116.981 -5.965  1.00 136.04 ? 183 ASP   K O   1 
ATOM   19298 C  CB  . ASP   K  11 182 ? 3.703   -117.652 -8.893  1.00 155.57 ? 183 ASP   K CB  1 
ATOM   19299 C  CG  . ASP   K  11 182 ? 3.697   -117.294 -10.369 1.00 158.53 ? 183 ASP   K CG  1 
ATOM   19300 O  OD1 . ASP   K  11 182 ? 4.115   -116.166 -10.701 1.00 160.87 ? 183 ASP   K OD1 1 
ATOM   19301 O  OD2 . ASP   K  11 182 ? 3.275   -118.148 -11.176 1.00 163.49 ? 183 ASP   K OD2 1 
ATOM   19302 N  N   . GLY   K  11 183 ? 5.696   -118.688 -6.224  1.00 134.77 ? 184 GLY   K N   1 
ATOM   19303 C  CA  . GLY   K  11 183 ? 5.689   -119.176 -4.827  1.00 129.17 ? 184 GLY   K CA  1 
ATOM   19304 C  C   . GLY   K  11 183 ? 5.417   -120.670 -4.752  1.00 127.91 ? 184 GLY   K C   1 
ATOM   19305 O  O   . GLY   K  11 183 ? 5.453   -121.319 -5.819  1.00 124.06 ? 184 GLY   K O   1 
ATOM   19306 N  N   . TRP   K  11 184 ? 5.155   -121.203 -3.548  1.00 124.59 ? 185 TRP   K N   1 
ATOM   19307 C  CA  . TRP   K  11 184 ? 4.823   -122.642 -3.328  1.00 125.58 ? 185 TRP   K CA  1 
ATOM   19308 C  C   . TRP   K  11 184 ? 3.313   -122.863 -3.465  1.00 126.79 ? 185 TRP   K C   1 
ATOM   19309 O  O   . TRP   K  11 184 ? 2.533   -121.954 -3.109  1.00 126.55 ? 185 TRP   K O   1 
ATOM   19310 C  CB  . TRP   K  11 184 ? 5.342   -123.198 -1.989  1.00 117.75 ? 185 TRP   K CB  1 
ATOM   19311 C  CG  . TRP   K  11 184 ? 4.816   -122.521 -0.760  1.00 116.45 ? 185 TRP   K CG  1 
ATOM   19312 C  CD1 . TRP   K  11 184 ? 5.500   -121.635 0.016   1.00 117.12 ? 185 TRP   K CD1 1 
ATOM   19313 C  CD2 . TRP   K  11 184 ? 3.523   -122.680 -0.142  1.00 115.93 ? 185 TRP   K CD2 1 
ATOM   19314 N  NE1 . TRP   K  11 184 ? 4.722   -121.215 1.059   1.00 119.61 ? 185 TRP   K NE1 1 
ATOM   19315 C  CE2 . TRP   K  11 184 ? 3.505   -121.836 0.989   1.00 118.28 ? 185 TRP   K CE2 1 
ATOM   19316 C  CE3 . TRP   K  11 184 ? 2.375   -123.432 -0.428  1.00 116.59 ? 185 TRP   K CE3 1 
ATOM   19317 C  CZ2 . TRP   K  11 184 ? 2.395   -121.721 1.824   1.00 120.87 ? 185 TRP   K CZ2 1 
ATOM   19318 C  CZ3 . TRP   K  11 184 ? 1.278   -123.322 0.399   1.00 117.97 ? 185 TRP   K CZ3 1 
ATOM   19319 C  CH2 . TRP   K  11 184 ? 1.290   -122.477 1.510   1.00 119.64 ? 185 TRP   K CH2 1 
ATOM   19320 N  N   . ILE   K  11 185 ? 2.943   -124.047 -3.958  1.00 126.76 ? 186 ILE   K N   1 
ATOM   19321 C  CA  . ILE   K  11 185 ? 1.542   -124.539 -4.108  1.00 127.21 ? 186 ILE   K CA  1 
ATOM   19322 C  C   . ILE   K  11 185 ? 1.469   -125.897 -3.403  1.00 121.17 ? 186 ILE   K C   1 
ATOM   19323 O  O   . ILE   K  11 185 ? 2.308   -126.768 -3.712  1.00 113.81 ? 186 ILE   K O   1 
ATOM   19324 C  CB  . ILE   K  11 185 ? 1.144   -124.631 -5.598  1.00 130.71 ? 186 ILE   K CB  1 
ATOM   19325 C  CG1 . ILE   K  11 185 ? 1.403   -123.320 -6.349  1.00 134.41 ? 186 ILE   K CG1 1 
ATOM   19326 C  CG2 . ILE   K  11 185 ? -0.303  -125.082 -5.748  1.00 130.08 ? 186 ILE   K CG2 1 
ATOM   19327 C  CD1 . ILE   K  11 185 ? 1.870   -123.508 -7.777  1.00 139.92 ? 186 ILE   K CD1 1 
ATOM   19328 N  N   . TYR   K  11 186 ? 0.530   -126.050 -2.467  1.00 119.71 ? 187 TYR   K N   1 
ATOM   19329 C  CA  . TYR   K  11 186 ? 0.246   -127.321 -1.753  1.00 117.48 ? 187 TYR   K CA  1 
ATOM   19330 C  C   . TYR   K  11 186 ? -0.522  -128.253 -2.698  1.00 119.17 ? 187 TYR   K C   1 
ATOM   19331 O  O   . TYR   K  11 186 ? -1.475  -127.783 -3.351  1.00 123.91 ? 187 TYR   K O   1 
ATOM   19332 C  CB  . TYR   K  11 186 ? -0.537  -127.034 -0.469  1.00 115.81 ? 187 TYR   K CB  1 
ATOM   19333 C  CG  . TYR   K  11 186 ? -0.808  -128.235 0.400   1.00 113.42 ? 187 TYR   K CG  1 
ATOM   19334 C  CD1 . TYR   K  11 186 ? 0.225   -129.039 0.857   1.00 111.28 ? 187 TYR   K CD1 1 
ATOM   19335 C  CD2 . TYR   K  11 186 ? -2.099  -128.559 0.788   1.00 114.72 ? 187 TYR   K CD2 1 
ATOM   19336 C  CE1 . TYR   K  11 186 ? -0.017  -130.141 1.662   1.00 109.63 ? 187 TYR   K CE1 1 
ATOM   19337 C  CE2 . TYR   K  11 186 ? -2.359  -129.655 1.596   1.00 112.89 ? 187 TYR   K CE2 1 
ATOM   19338 C  CZ  . TYR   K  11 186 ? -1.314  -130.450 2.035   1.00 110.44 ? 187 TYR   K CZ  1 
ATOM   19339 O  OH  . TYR   K  11 186 ? -1.560  -131.531 2.830   1.00 106.88 ? 187 TYR   K OH  1 
ATOM   19340 N  N   . HIS   K  11 187 ? -0.109  -129.523 -2.779  1.00 120.60 ? 188 HIS   K N   1 
ATOM   19341 C  CA  . HIS   K  11 187 ? -0.741  -130.567 -3.632  1.00 121.39 ? 188 HIS   K CA  1 
ATOM   19342 C  C   . HIS   K  11 187 ? -1.214  -131.739 -2.761  1.00 116.96 ? 188 HIS   K C   1 
ATOM   19343 O  O   . HIS   K  11 187 ? -1.043  -132.896 -3.182  1.00 117.58 ? 188 HIS   K O   1 
ATOM   19344 C  CB  . HIS   K  11 187 ? 0.211   -130.981 -4.764  1.00 123.45 ? 188 HIS   K CB  1 
ATOM   19345 C  CG  . HIS   K  11 187 ? 0.273   -129.987 -5.875  1.00 126.84 ? 188 HIS   K CG  1 
ATOM   19346 N  ND1 . HIS   K  11 187 ? -0.575  -130.044 -6.966  1.00 129.50 ? 188 HIS   K ND1 1 
ATOM   19347 C  CD2 . HIS   K  11 187 ? 1.064   -128.909 -6.065  1.00 126.34 ? 188 HIS   K CD2 1 
ATOM   19348 C  CE1 . HIS   K  11 187 ? -0.301  -129.047 -7.783  1.00 130.13 ? 188 HIS   K CE1 1 
ATOM   19349 N  NE2 . HIS   K  11 187 ? 0.699   -128.335 -7.253  1.00 129.44 ? 188 HIS   K NE2 1 
ATOM   19350 N  N   . GLY   K  11 188 ? -1.787  -131.434 -1.593  1.00 111.47 ? 189 GLY   K N   1 
ATOM   19351 C  CA  . GLY   K  11 188 ? -2.654  -132.348 -0.826  1.00 111.06 ? 189 GLY   K CA  1 
ATOM   19352 C  C   . GLY   K  11 188 ? -1.891  -133.259 0.121   1.00 110.18 ? 189 GLY   K C   1 
ATOM   19353 O  O   . GLY   K  11 188 ? -0.657  -133.393 -0.028  1.00 109.77 ? 189 GLY   K O   1 
ATOM   19354 N  N   . ASN   K  11 189 ? -2.626  -133.849 1.070   1.00 111.60 ? 190 ASN   K N   1 
ATOM   19355 C  CA  . ASN   K  11 189 ? -2.190  -134.950 1.970   1.00 110.42 ? 190 ASN   K CA  1 
ATOM   19356 C  C   . ASN   K  11 189 ? -2.699  -136.277 1.393   1.00 110.76 ? 190 ASN   K C   1 
ATOM   19357 O  O   . ASN   K  11 189 ? -3.908  -136.361 1.096   1.00 110.79 ? 190 ASN   K O   1 
ATOM   19358 C  CB  . ASN   K  11 189 ? -2.720  -134.737 3.390   1.00 109.72 ? 190 ASN   K CB  1 
ATOM   19359 C  CG  . ASN   K  11 189 ? -2.364  -135.866 4.331   1.00 108.93 ? 190 ASN   K CG  1 
ATOM   19360 O  OD1 . ASN   K  11 189 ? -3.152  -136.788 4.522   1.00 110.62 ? 190 ASN   K OD1 1 
ATOM   19361 N  ND2 . ASN   K  11 189 ? -1.179  -135.807 4.915   1.00 108.56 ? 190 ASN   K ND2 1 
ATOM   19362 N  N   . HIS   K  11 190 ? -1.821  -137.274 1.247   1.00 107.33 ? 191 HIS   K N   1 
ATOM   19363 C  CA  . HIS   K  11 190 ? -2.126  -138.578 0.597   1.00 108.70 ? 191 HIS   K CA  1 
ATOM   19364 C  C   . HIS   K  11 190 ? -1.801  -139.732 1.551   1.00 108.98 ? 191 HIS   K C   1 
ATOM   19365 O  O   . HIS   K  11 190 ? -0.613  -140.104 1.646   1.00 109.43 ? 191 HIS   K O   1 
ATOM   19366 C  CB  . HIS   K  11 190 ? -1.377  -138.693 -0.738  1.00 106.47 ? 191 HIS   K CB  1 
ATOM   19367 C  CG  . HIS   K  11 190 ? -1.589  -137.521 -1.636  1.00 105.90 ? 191 HIS   K CG  1 
ATOM   19368 N  ND1 . HIS   K  11 190 ? -2.619  -137.468 -2.555  1.00 107.06 ? 191 HIS   K ND1 1 
ATOM   19369 C  CD2 . HIS   K  11 190 ? -0.920  -136.354 -1.747  1.00 103.50 ? 191 HIS   K CD2 1 
ATOM   19370 C  CE1 . HIS   K  11 190 ? -2.568  -136.322 -3.201  1.00 106.24 ? 191 HIS   K CE1 1 
ATOM   19371 N  NE2 . HIS   K  11 190 ? -1.534  -135.623 -2.726  1.00 103.44 ? 191 HIS   K NE2 1 
ATOM   19372 N  N   . ASP   K  11 191 ? -2.826  -140.272 2.221   1.00 111.00 ? 192 ASP   K N   1 
ATOM   19373 C  CA  . ASP   K  11 191 ? -2.729  -141.433 3.148   1.00 110.71 ? 192 ASP   K CA  1 
ATOM   19374 C  C   . ASP   K  11 191 ? -2.132  -142.621 2.388   1.00 107.05 ? 192 ASP   K C   1 
ATOM   19375 O  O   . ASP   K  11 191 ? -2.628  -142.917 1.289   1.00 107.76 ? 192 ASP   K O   1 
ATOM   19376 C  CB  . ASP   K  11 191 ? -4.096  -141.805 3.730   1.00 114.03 ? 192 ASP   K CB  1 
ATOM   19377 C  CG  . ASP   K  11 191 ? -4.032  -142.717 4.945   1.00 114.85 ? 192 ASP   K CG  1 
ATOM   19378 O  OD1 . ASP   K  11 191 ? -4.774  -142.454 5.912   1.00 123.67 ? 192 ASP   K OD1 1 
ATOM   19379 O  OD2 . ASP   K  11 191 ? -3.252  -143.687 4.913   1.00 117.38 ? 192 ASP   K OD2 1 
ATOM   19380 N  N   . VAL   K  11 192 ? -1.116  -143.271 2.962   1.00 105.34 ? 193 VAL   K N   1 
ATOM   19381 C  CA  . VAL   K  11 192 ? -0.440  -144.467 2.374   1.00 104.55 ? 193 VAL   K CA  1 
ATOM   19382 C  C   . VAL   K  11 192 ? -1.418  -145.648 2.410   1.00 103.35 ? 193 VAL   K C   1 
ATOM   19383 O  O   . VAL   K  11 192 ? -1.344  -146.498 1.502   1.00 100.95 ? 193 VAL   K O   1 
ATOM   19384 C  CB  . VAL   K  11 192 ? 0.876   -144.791 3.108   1.00 104.70 ? 193 VAL   K CB  1 
ATOM   19385 C  CG1 . VAL   K  11 192 ? 1.506   -146.081 2.605   1.00 107.34 ? 193 VAL   K CG1 1 
ATOM   19386 C  CG2 . VAL   K  11 192 ? 1.868   -143.642 3.012   1.00 104.08 ? 193 VAL   K CG2 1 
ATOM   19387 N  N   . GLY   K  11 193 ? -2.294  -145.687 3.422   1.00 104.55 ? 194 GLY   K N   1 
ATOM   19388 C  CA  . GLY   K  11 193 ? -3.366  -146.690 3.578   1.00 107.13 ? 194 GLY   K CA  1 
ATOM   19389 C  C   . GLY   K  11 193 ? -4.083  -146.962 2.266   1.00 108.41 ? 194 GLY   K C   1 
ATOM   19390 O  O   . GLY   K  11 193 ? -4.195  -148.147 1.893   1.00 108.94 ? 194 GLY   K O   1 
ATOM   19391 N  N   . GLU   K  11 194 ? -4.537  -145.903 1.583   1.00 109.34 ? 195 GLU   K N   1 
ATOM   19392 C  CA  . GLU   K  11 194 ? -5.282  -145.979 0.295   1.00 109.03 ? 195 GLU   K CA  1 
ATOM   19393 C  C   . GLU   K  11 194 ? -4.318  -145.868 -0.893  1.00 103.15 ? 195 GLU   K C   1 
ATOM   19394 O  O   . GLU   K  11 194 ? -4.550  -146.566 -1.897  1.00 100.31 ? 195 GLU   K O   1 
ATOM   19395 C  CB  . GLU   K  11 194 ? -6.334  -144.872 0.195   1.00 111.11 ? 195 GLU   K CB  1 
ATOM   19396 C  CG  . GLU   K  11 194 ? -7.506  -145.047 1.142   1.00 116.87 ? 195 GLU   K CG  1 
ATOM   19397 C  CD  . GLU   K  11 194 ? -7.454  -144.152 2.366   1.00 122.70 ? 195 GLU   K CD  1 
ATOM   19398 O  OE1 . GLU   K  11 194 ? -7.221  -144.679 3.472   1.00 128.74 ? 195 GLU   K OE1 1 
ATOM   19399 O  OE2 . GLU   K  11 194 ? -7.651  -142.928 2.209   1.00 126.38 ? 195 GLU   K OE2 1 
ATOM   19400 N  N   . LEU   K  11 195 ? -3.295  -145.011 -0.793  1.00 103.95 ? 196 LEU   K N   1 
ATOM   19401 C  CA  . LEU   K  11 195 ? -2.377  -144.670 -1.916  1.00 104.62 ? 196 LEU   K CA  1 
ATOM   19402 C  C   . LEU   K  11 195 ? -1.639  -145.925 -2.396  1.00 105.24 ? 196 LEU   K C   1 
ATOM   19403 O  O   . LEU   K  11 195 ? -1.528  -146.094 -3.622  1.00 103.51 ? 196 LEU   K O   1 
ATOM   19404 C  CB  . LEU   K  11 195 ? -1.387  -143.584 -1.473  1.00 104.13 ? 196 LEU   K CB  1 
ATOM   19405 C  CG  . LEU   K  11 195 ? -0.340  -143.170 -2.510  1.00 101.73 ? 196 LEU   K CG  1 
ATOM   19406 C  CD1 . LEU   K  11 195 ? -0.994  -142.651 -3.781  1.00 102.57 ? 196 LEU   K CD1 1 
ATOM   19407 C  CD2 . LEU   K  11 195 ? 0.605   -142.127 -1.935  1.00 100.42 ? 196 LEU   K CD2 1 
ATOM   19408 N  N   . PHE   K  11 196 ? -1.148  -146.763 -1.475  1.00 106.40 ? 197 PHE   K N   1 
ATOM   19409 C  CA  . PHE   K  11 196 ? -0.349  -147.978 -1.793  1.00 109.53 ? 197 PHE   K CA  1 
ATOM   19410 C  C   . PHE   K  11 196 ? -1.142  -148.903 -2.725  1.00 111.30 ? 197 PHE   K C   1 
ATOM   19411 O  O   . PHE   K  11 196 ? -0.611  -149.281 -3.789  1.00 107.47 ? 197 PHE   K O   1 
ATOM   19412 C  CB  . PHE   K  11 196 ? 0.055   -148.746 -0.532  1.00 109.85 ? 197 PHE   K CB  1 
ATOM   19413 C  CG  . PHE   K  11 196 ? 0.870   -149.982 -0.823  1.00 111.20 ? 197 PHE   K CG  1 
ATOM   19414 C  CD1 . PHE   K  11 196 ? 2.252   -149.912 -0.906  1.00 114.38 ? 197 PHE   K CD1 1 
ATOM   19415 C  CD2 . PHE   K  11 196 ? 0.256   -151.204 -1.055  1.00 110.61 ? 197 PHE   K CD2 1 
ATOM   19416 C  CE1 . PHE   K  11 196 ? 3.004   -151.043 -1.189  1.00 115.10 ? 197 PHE   K CE1 1 
ATOM   19417 C  CE2 . PHE   K  11 196 ? 1.010   -152.331 -1.345  1.00 112.62 ? 197 PHE   K CE2 1 
ATOM   19418 C  CZ  . PHE   K  11 196 ? 2.382   -152.249 -1.408  1.00 114.20 ? 197 PHE   K CZ  1 
ATOM   19419 N  N   . TRP   K  11 197 ? -2.365  -149.269 -2.321  1.00 115.71 ? 198 TRP   K N   1 
ATOM   19420 C  CA  . TRP   K  11 197 ? -3.267  -150.199 -3.058  1.00 117.74 ? 198 TRP   K CA  1 
ATOM   19421 C  C   . TRP   K  11 197 ? -3.659  -149.582 -4.408  1.00 117.12 ? 198 TRP   K C   1 
ATOM   19422 O  O   . TRP   K  11 197 ? -3.736  -150.331 -5.402  1.00 116.62 ? 198 TRP   K O   1 
ATOM   19423 C  CB  . TRP   K  11 197 ? -4.507  -150.545 -2.219  1.00 121.04 ? 198 TRP   K CB  1 
ATOM   19424 C  CG  . TRP   K  11 197 ? -4.209  -151.263 -0.939  1.00 121.62 ? 198 TRP   K CG  1 
ATOM   19425 C  CD1 . TRP   K  11 197 ? -4.433  -150.811 0.329   1.00 123.50 ? 198 TRP   K CD1 1 
ATOM   19426 C  CD2 . TRP   K  11 197 ? -3.621  -152.567 -0.799  1.00 121.02 ? 198 TRP   K CD2 1 
ATOM   19427 N  NE1 . TRP   K  11 197 ? -4.030  -151.742 1.248   1.00 124.18 ? 198 TRP   K NE1 1 
ATOM   19428 C  CE2 . TRP   K  11 197 ? -3.527  -152.830 0.585   1.00 123.70 ? 198 TRP   K CE2 1 
ATOM   19429 C  CE3 . TRP   K  11 197 ? -3.163  -153.531 -1.703  1.00 120.80 ? 198 TRP   K CE3 1 
ATOM   19430 C  CZ2 . TRP   K  11 197 ? -2.996  -154.020 1.080   1.00 122.55 ? 198 TRP   K CZ2 1 
ATOM   19431 C  CZ3 . TRP   K  11 197 ? -2.640  -154.706 -1.212  1.00 122.66 ? 198 TRP   K CZ3 1 
ATOM   19432 C  CH2 . TRP   K  11 197 ? -2.558  -154.945 0.161   1.00 123.87 ? 198 TRP   K CH2 1 
ATOM   19433 N  N   . LYS   K  11 198 ? -3.903  -148.268 -4.431  1.00 114.45 ? 199 LYS   K N   1 
ATOM   19434 C  CA  . LYS   K  11 198 ? -4.261  -147.494 -5.650  1.00 114.29 ? 199 LYS   K CA  1 
ATOM   19435 C  C   . LYS   K  11 198 ? -3.085  -147.519 -6.634  1.00 107.94 ? 199 LYS   K C   1 
ATOM   19436 O  O   . LYS   K  11 198 ? -3.322  -147.779 -7.823  1.00 106.39 ? 199 LYS   K O   1 
ATOM   19437 C  CB  . LYS   K  11 198 ? -4.639  -146.061 -5.264  1.00 115.81 ? 199 LYS   K CB  1 
ATOM   19438 C  CG  . LYS   K  11 198 ? -4.962  -145.124 -6.422  1.00 120.28 ? 199 LYS   K CG  1 
ATOM   19439 C  CD  . LYS   K  11 198 ? -5.381  -143.738 -5.962  1.00 120.68 ? 199 LYS   K CD  1 
ATOM   19440 C  CE  . LYS   K  11 198 ? -4.963  -142.630 -6.906  1.00 121.40 ? 199 LYS   K CE  1 
ATOM   19441 N  NZ  . LYS   K  11 198 ? -5.756  -142.642 -8.158  1.00 124.56 ? 199 LYS   K NZ  1 
ATOM   19442 N  N   . VAL   K  11 199 ? -1.867  -147.254 -6.153  1.00 107.39 ? 200 VAL   K N   1 
ATOM   19443 C  CA  . VAL   K  11 199 ? -0.620  -147.281 -6.975  1.00 110.39 ? 200 VAL   K CA  1 
ATOM   19444 C  C   . VAL   K  11 199 ? -0.384  -148.719 -7.452  1.00 114.69 ? 200 VAL   K C   1 
ATOM   19445 O  O   . VAL   K  11 199 ? -0.163  -148.891 -8.663  1.00 116.74 ? 200 VAL   K O   1 
ATOM   19446 C  CB  . VAL   K  11 199 ? 0.591   -146.717 -6.205  1.00 107.94 ? 200 VAL   K CB  1 
ATOM   19447 C  CG1 . VAL   K  11 199 ? 1.918   -147.113 -6.838  1.00 108.29 ? 200 VAL   K CG1 1 
ATOM   19448 C  CG2 . VAL   K  11 199 ? 0.505   -145.205 -6.070  1.00 107.71 ? 200 VAL   K CG2 1 
ATOM   19449 N  N   . LYS   K  11 200 ? -0.446  -149.703 -6.542  1.00 118.58 ? 201 LYS   K N   1 
ATOM   19450 C  CA  . LYS   K  11 200 ? -0.198  -151.142 -6.842  1.00 121.74 ? 201 LYS   K CA  1 
ATOM   19451 C  C   . LYS   K  11 200 ? -1.089  -151.570 -8.014  1.00 124.22 ? 201 LYS   K C   1 
ATOM   19452 O  O   . LYS   K  11 200 ? -0.546  -152.115 -8.996  1.00 125.71 ? 201 LYS   K O   1 
ATOM   19453 C  CB  . LYS   K  11 200 ? -0.458  -152.034 -5.621  1.00 122.75 ? 201 LYS   K CB  1 
ATOM   19454 C  CG  . LYS   K  11 200 ? -0.265  -153.529 -5.865  1.00 125.28 ? 201 LYS   K CG  1 
ATOM   19455 C  CD  . LYS   K  11 200 ? -0.405  -154.391 -4.627  1.00 123.68 ? 201 LYS   K CD  1 
ATOM   19456 C  CE  . LYS   K  11 200 ? -0.545  -155.870 -4.934  1.00 126.11 ? 201 LYS   K CE  1 
ATOM   19457 N  NZ  . LYS   K  11 200 ? 0.519   -156.366 -5.840  1.00 125.50 ? 201 LYS   K NZ  1 
ATOM   19458 N  N   . GLU   K  11 201 ? -2.399  -151.322 -7.907  1.00 123.42 ? 202 GLU   K N   1 
ATOM   19459 C  CA  . GLU   K  11 201 ? -3.421  -151.723 -8.913  1.00 125.19 ? 202 GLU   K CA  1 
ATOM   19460 C  C   . GLU   K  11 201 ? -3.128  -151.032 -10.251 1.00 125.48 ? 202 GLU   K C   1 
ATOM   19461 O  O   . GLU   K  11 201 ? -2.969  -151.743 -11.260 1.00 121.01 ? 202 GLU   K O   1 
ATOM   19462 C  CB  . GLU   K  11 201 ? -4.829  -151.389 -8.412  1.00 126.81 ? 202 GLU   K CB  1 
ATOM   19463 C  CG  . GLU   K  11 201 ? -5.918  -151.648 -9.440  1.00 129.82 ? 202 GLU   K CG  1 
ATOM   19464 C  CD  . GLU   K  11 201 ? -7.331  -151.629 -8.886  1.00 130.43 ? 202 GLU   K CD  1 
ATOM   19465 O  OE1 . GLU   K  11 201 ? -7.692  -152.575 -8.160  1.00 132.07 ? 202 GLU   K OE1 1 
ATOM   19466 O  OE2 . GLU   K  11 201 ? -8.064  -150.664 -9.177  1.00 130.79 ? 202 GLU   K OE2 1 
ATOM   19467 N  N   . GLU   K  11 202 ? -3.047  -149.698 -10.246 1.00 126.63 ? 203 GLU   K N   1 
ATOM   19468 C  CA  . GLU   K  11 202 ? -2.958  -148.847 -11.467 1.00 127.74 ? 203 GLU   K CA  1 
ATOM   19469 C  C   . GLU   K  11 202 ? -1.580  -148.977 -12.131 1.00 124.91 ? 203 GLU   K C   1 
ATOM   19470 O  O   . GLU   K  11 202 ? -1.532  -148.971 -13.374 1.00 120.38 ? 203 GLU   K O   1 
ATOM   19471 C  CB  . GLU   K  11 202 ? -3.239  -147.384 -11.119 1.00 129.87 ? 203 GLU   K CB  1 
ATOM   19472 C  CG  . GLU   K  11 202 ? -4.680  -147.123 -10.716 1.00 133.95 ? 203 GLU   K CG  1 
ATOM   19473 C  CD  . GLU   K  11 202 ? -4.999  -145.675 -10.379 1.00 135.22 ? 203 GLU   K CD  1 
ATOM   19474 O  OE1 . GLU   K  11 202 ? -4.123  -144.809 -10.587 1.00 135.19 ? 203 GLU   K OE1 1 
ATOM   19475 O  OE2 . GLU   K  11 202 ? -6.126  -145.415 -9.909  1.00 139.92 ? 203 GLU   K OE2 1 
ATOM   19476 N  N   . GLU   K  11 203 ? -0.506  -149.069 -11.340 1.00 124.59 ? 204 GLU   K N   1 
ATOM   19477 C  CA  . GLU   K  11 203 ? 0.898   -149.090 -11.838 1.00 126.36 ? 204 GLU   K CA  1 
ATOM   19478 C  C   . GLU   K  11 203 ? 1.321   -150.529 -12.170 1.00 124.95 ? 204 GLU   K C   1 
ATOM   19479 O  O   . GLU   K  11 203 ? 2.043   -150.707 -13.171 1.00 123.22 ? 204 GLU   K O   1 
ATOM   19480 C  CB  . GLU   K  11 203 ? 1.837   -148.460 -10.806 1.00 123.31 ? 204 GLU   K CB  1 
ATOM   19481 C  CG  . GLU   K  11 203 ? 3.167   -148.024 -11.388 1.00 125.30 ? 204 GLU   K CG  1 
ATOM   19482 C  CD  . GLU   K  11 203 ? 3.985   -147.131 -10.473 1.00 125.09 ? 204 GLU   K CD  1 
ATOM   19483 O  OE1 . GLU   K  11 203 ? 4.265   -145.983 -10.870 1.00 124.91 ? 204 GLU   K OE1 1 
ATOM   19484 O  OE2 . GLU   K  11 203 ? 4.345   -147.586 -9.370  1.00 128.16 ? 204 GLU   K OE2 1 
ATOM   19485 N  N   . GLY   K  11 204 ? 0.897   -151.508 -11.360 1.00 126.72 ? 205 GLY   K N   1 
ATOM   19486 C  CA  . GLY   K  11 204 ? 1.259   -152.933 -11.505 1.00 128.59 ? 205 GLY   K CA  1 
ATOM   19487 C  C   . GLY   K  11 204 ? 2.551   -153.280 -10.779 1.00 129.17 ? 205 GLY   K C   1 
ATOM   19488 O  O   . GLY   K  11 204 ? 3.062   -154.397 -11.000 1.00 131.18 ? 205 GLY   K O   1 
ATOM   19489 N  N   . SER   K  11 205 ? 3.054   -152.368 -9.938  1.00 125.51 ? 206 SER   K N   1 
ATOM   19490 C  CA  . SER   K  11 205 ? 4.276   -152.538 -9.107  1.00 124.59 ? 206 SER   K CA  1 
ATOM   19491 C  C   . SER   K  11 205 ? 3.892   -153.178 -7.769  1.00 124.30 ? 206 SER   K C   1 
ATOM   19492 O  O   . SER   K  11 205 ? 2.708   -153.533 -7.612  1.00 124.46 ? 206 SER   K O   1 
ATOM   19493 C  CB  . SER   K  11 205 ? 4.972   -151.216 -8.919  1.00 123.69 ? 206 SER   K CB  1 
ATOM   19494 O  OG  . SER   K  11 205 ? 4.073   -150.246 -8.403  1.00 124.52 ? 206 SER   K OG  1 
ATOM   19495 N  N   . PHE   K  11 206 ? 4.855   -153.326 -6.851  1.00 125.44 ? 207 PHE   K N   1 
ATOM   19496 C  CA  . PHE   K  11 206 ? 4.675   -153.933 -5.505  1.00 124.65 ? 207 PHE   K CA  1 
ATOM   19497 C  C   . PHE   K  11 206 ? 4.127   -155.359 -5.671  1.00 130.35 ? 207 PHE   K C   1 
ATOM   19498 O  O   . PHE   K  11 206 ? 3.039   -155.677 -5.144  1.00 133.49 ? 207 PHE   K O   1 
ATOM   19499 C  CB  . PHE   K  11 206 ? 3.792   -153.043 -4.623  1.00 120.26 ? 207 PHE   K CB  1 
ATOM   19500 C  CG  . PHE   K  11 206 ? 4.430   -151.741 -4.211  1.00 117.83 ? 207 PHE   K CG  1 
ATOM   19501 C  CD1 . PHE   K  11 206 ? 5.597   -151.732 -3.461  1.00 116.52 ? 207 PHE   K CD1 1 
ATOM   19502 C  CD2 . PHE   K  11 206 ? 3.863   -150.526 -4.562  1.00 115.18 ? 207 PHE   K CD2 1 
ATOM   19503 C  CE1 . PHE   K  11 206 ? 6.187   -150.538 -3.080  1.00 116.08 ? 207 PHE   K CE1 1 
ATOM   19504 C  CE2 . PHE   K  11 206 ? 4.453   -149.332 -4.178  1.00 115.38 ? 207 PHE   K CE2 1 
ATOM   19505 C  CZ  . PHE   K  11 206 ? 5.613   -149.340 -3.438  1.00 114.55 ? 207 PHE   K CZ  1 
ATOM   19506 N  N   . ASN   K  11 207 ? 4.877   -156.196 -6.394  1.00 131.00 ? 208 ASN   K N   1 
ATOM   19507 C  CA  . ASN   K  11 207 ? 4.547   -157.622 -6.652  1.00 133.29 ? 208 ASN   K CA  1 
ATOM   19508 C  C   . ASN   K  11 207 ? 5.028   -158.490 -5.482  1.00 130.17 ? 208 ASN   K C   1 
ATOM   19509 O  O   . ASN   K  11 207 ? 4.473   -159.588 -5.305  1.00 131.59 ? 208 ASN   K O   1 
ATOM   19510 C  CB  . ASN   K  11 207 ? 5.131   -158.080 -7.989  1.00 136.03 ? 208 ASN   K CB  1 
ATOM   19511 C  CG  . ASN   K  11 207 ? 4.516   -157.346 -9.161  1.00 135.36 ? 208 ASN   K CG  1 
ATOM   19512 O  OD1 . ASN   K  11 207 ? 5.124   -156.432 -9.713  1.00 133.74 ? 208 ASN   K OD1 1 
ATOM   19513 N  ND2 . ASN   K  11 207 ? 3.302   -157.723 -9.529  1.00 137.46 ? 208 ASN   K ND2 1 
ATOM   19514 N  N   . ASN   K  11 208 ? 6.017   -158.014 -4.715  1.00 131.91 ? 209 ASN   K N   1 
ATOM   19515 C  CA  . ASN   K  11 208 ? 6.490   -158.651 -3.454  1.00 134.04 ? 209 ASN   K CA  1 
ATOM   19516 C  C   . ASN   K  11 208 ? 5.297   -158.869 -2.510  1.00 137.48 ? 209 ASN   K C   1 
ATOM   19517 O  O   . ASN   K  11 208 ? 5.283   -159.906 -1.818  1.00 139.84 ? 209 ASN   K O   1 
ATOM   19518 C  CB  . ASN   K  11 208 ? 7.600   -157.836 -2.775  1.00 135.67 ? 209 ASN   K CB  1 
ATOM   19519 C  CG  . ASN   K  11 208 ? 7.199   -156.416 -2.422  1.00 131.99 ? 209 ASN   K CG  1 
ATOM   19520 O  OD1 . ASN   K  11 208 ? 6.379   -155.806 -3.103  1.00 130.13 ? 209 ASN   K OD1 1 
ATOM   19521 N  ND2 . ASN   K  11 208 ? 7.783   -155.871 -1.365  1.00 131.85 ? 209 ASN   K ND2 1 
ATOM   19522 N  N   . VAL   K  11 209 ? 4.334   -157.937 -2.495  1.00 137.81 ? 210 VAL   K N   1 
ATOM   19523 C  CA  . VAL   K  11 209 ? 3.193   -157.897 -1.529  1.00 132.07 ? 210 VAL   K CA  1 
ATOM   19524 C  C   . VAL   K  11 209 ? 2.061   -158.800 -2.027  1.00 132.87 ? 210 VAL   K C   1 
ATOM   19525 O  O   . VAL   K  11 209 ? 1.765   -158.765 -3.239  1.00 129.10 ? 210 VAL   K O   1 
ATOM   19526 C  CB  . VAL   K  11 209 ? 2.695   -156.455 -1.305  1.00 130.75 ? 210 VAL   K CB  1 
ATOM   19527 C  CG1 . VAL   K  11 209 ? 1.359   -156.416 -0.575  1.00 129.66 ? 210 VAL   K CG1 1 
ATOM   19528 C  CG2 . VAL   K  11 209 ? 3.732   -155.622 -0.567  1.00 128.03 ? 210 VAL   K CG2 1 
ATOM   19529 N  N   . ILE   K  11 210 ? 1.444   -159.547 -1.104  1.00 137.83 ? 211 ILE   K N   1 
ATOM   19530 C  CA  . ILE   K  11 210 ? 0.247   -160.404 -1.361  1.00 139.13 ? 211 ILE   K CA  1 
ATOM   19531 C  C   . ILE   K  11 210 ? -0.901  -159.475 -1.774  1.00 137.69 ? 211 ILE   K C   1 
ATOM   19532 O  O   . ILE   K  11 210 ? -1.311  -158.632 -0.945  1.00 132.33 ? 211 ILE   K O   1 
ATOM   19533 C  CB  . ILE   K  11 210 ? -0.092  -161.288 -0.138  1.00 145.13 ? 211 ILE   K CB  1 
ATOM   19534 C  CG1 . ILE   K  11 210 ? 1.001   -162.336 0.110   1.00 142.58 ? 211 ILE   K CG1 1 
ATOM   19535 C  CG2 . ILE   K  11 210 ? -1.466  -161.934 -0.287  1.00 145.29 ? 211 ILE   K CG2 1 
ATOM   19536 C  CD1 . ILE   K  11 210 ? 0.805   -163.174 1.355   1.00 142.76 ? 211 ILE   K CD1 1 
ATOM   19537 N  N   . GLY   K  11 211 ? -1.366  -159.615 -3.020  1.00 141.28 ? 212 GLY   K N   1 
ATOM   19538 C  CA  . GLY   K  11 211 ? -2.386  -158.752 -3.648  1.00 142.01 ? 212 GLY   K CA  1 
ATOM   19539 C  C   . GLY   K  11 211 ? -3.755  -158.942 -3.022  1.00 146.02 ? 212 GLY   K C   1 
ATOM   19540 O  O   . GLY   K  11 211 ? -4.040  -159.967 -2.399  1.00 150.54 ? 212 GLY   K O   1 
ATOM   19541 O  OXT . GLY   K  11 211 ? -4.610  -158.062 -3.131  1.00 141.87 ? 212 GLY   K OXT 1 
ATOM   19542 N  N   . GLN   L  12 1   ? 26.160  -142.508 42.068  1.00 98.98  ? 1   GLN   L N   1 
ATOM   19543 C  CA  . GLN   L  12 1   ? 25.995  -141.136 41.492  1.00 100.12 ? 1   GLN   L CA  1 
ATOM   19544 C  C   . GLN   L  12 1   ? 24.521  -140.726 41.621  1.00 98.77  ? 1   GLN   L C   1 
ATOM   19545 O  O   . GLN   L  12 1   ? 23.646  -141.593 41.414  1.00 99.16  ? 1   GLN   L O   1 
ATOM   19546 C  CB  . GLN   L  12 1   ? 26.477  -141.106 40.035  1.00 106.45 ? 1   GLN   L CB  1 
ATOM   19547 C  CG  . GLN   L  12 1   ? 27.247  -139.847 39.647  1.00 112.33 ? 1   GLN   L CG  1 
ATOM   19548 C  CD  . GLN   L  12 1   ? 26.403  -138.812 38.942  1.00 117.77 ? 1   GLN   L CD  1 
ATOM   19549 O  OE1 . GLN   L  12 1   ? 26.365  -138.749 37.715  1.00 126.78 ? 1   GLN   L OE1 1 
ATOM   19550 N  NE2 . GLN   L  12 1   ? 25.720  -137.980 39.713  1.00 120.53 ? 1   GLN   L NE2 1 
ATOM   19551 N  N   . PHE   L  12 2   ? 24.262  -139.465 41.980  1.00 95.70  ? 2   PHE   L N   1 
ATOM   19552 C  CA  . PHE   L  12 2   ? 22.902  -138.876 42.113  1.00 90.67  ? 2   PHE   L CA  1 
ATOM   19553 C  C   . PHE   L  12 2   ? 22.204  -138.850 40.747  1.00 85.74  ? 2   PHE   L C   1 
ATOM   19554 O  O   . PHE   L  12 2   ? 22.744  -138.248 39.799  1.00 82.26  ? 2   PHE   L O   1 
ATOM   19555 C  CB  . PHE   L  12 2   ? 22.964  -137.467 42.707  1.00 88.69  ? 2   PHE   L CB  1 
ATOM   19556 C  CG  . PHE   L  12 2   ? 21.637  -136.752 42.733  1.00 86.89  ? 2   PHE   L CG  1 
ATOM   19557 C  CD1 . PHE   L  12 2   ? 20.563  -137.282 43.433  1.00 87.80  ? 2   PHE   L CD1 1 
ATOM   19558 C  CD2 . PHE   L  12 2   ? 21.456  -135.556 42.054  1.00 85.69  ? 2   PHE   L CD2 1 
ATOM   19559 C  CE1 . PHE   L  12 2   ? 19.339  -136.631 43.457  1.00 87.25  ? 2   PHE   L CE1 1 
ATOM   19560 C  CE2 . PHE   L  12 2   ? 20.232  -134.906 42.080  1.00 86.04  ? 2   PHE   L CE2 1 
ATOM   19561 C  CZ  . PHE   L  12 2   ? 19.176  -135.444 42.781  1.00 86.17  ? 2   PHE   L CZ  1 
ATOM   19562 N  N   . ASN   L  12 3   ? 21.034  -139.490 40.667  1.00 85.71  ? 3   ASN   L N   1 
ATOM   19563 C  CA  . ASN   L  12 3   ? 20.140  -139.514 39.478  1.00 87.28  ? 3   ASN   L CA  1 
ATOM   19564 C  C   . ASN   L  12 3   ? 19.032  -138.495 39.723  1.00 84.03  ? 3   ASN   L C   1 
ATOM   19565 O  O   . ASN   L  12 3   ? 18.188  -138.708 40.591  1.00 83.99  ? 3   ASN   L O   1 
ATOM   19566 C  CB  . ASN   L  12 3   ? 19.604  -140.930 39.232  1.00 90.66  ? 3   ASN   L CB  1 
ATOM   19567 C  CG  . ASN   L  12 3   ? 18.634  -141.068 38.074  1.00 93.29  ? 3   ASN   L CG  1 
ATOM   19568 O  OD1 . ASN   L  12 3   ? 17.933  -142.074 37.985  1.00 102.91 ? 3   ASN   L OD1 1 
ATOM   19569 N  ND2 . ASN   L  12 3   ? 18.582  -140.096 37.174  1.00 87.25  ? 3   ASN   L ND2 1 
ATOM   19570 N  N   . PRO   L  12 4   ? 19.008  -137.352 38.995  1.00 81.52  ? 4   PRO   L N   1 
ATOM   19571 C  CA  . PRO   L  12 4   ? 18.023  -136.303 39.258  1.00 79.85  ? 4   PRO   L CA  1 
ATOM   19572 C  C   . PRO   L  12 4   ? 16.584  -136.646 38.837  1.00 80.97  ? 4   PRO   L C   1 
ATOM   19573 O  O   . PRO   L  12 4   ? 15.690  -135.931 39.242  1.00 81.14  ? 4   PRO   L O   1 
ATOM   19574 C  CB  . PRO   L  12 4   ? 18.556  -135.117 38.441  1.00 78.46  ? 4   PRO   L CB  1 
ATOM   19575 C  CG  . PRO   L  12 4   ? 19.298  -135.762 37.296  1.00 78.82  ? 4   PRO   L CG  1 
ATOM   19576 C  CD  . PRO   L  12 4   ? 19.936  -136.990 37.908  1.00 79.34  ? 4   PRO   L CD  1 
ATOM   19577 N  N   . TYR   L  12 5   ? 16.390  -137.714 38.058  1.00 82.19  ? 5   TYR   L N   1 
ATOM   19578 C  CA  . TYR   L  12 5   ? 15.071  -138.128 37.512  1.00 83.70  ? 5   TYR   L CA  1 
ATOM   19579 C  C   . TYR   L  12 5   ? 14.507  -139.320 38.294  1.00 86.36  ? 5   TYR   L C   1 
ATOM   19580 O  O   . TYR   L  12 5   ? 15.284  -140.107 38.872  1.00 88.94  ? 5   TYR   L O   1 
ATOM   19581 C  CB  . TYR   L  12 5   ? 15.195  -138.476 36.028  1.00 84.64  ? 5   TYR   L CB  1 
ATOM   19582 C  CG  . TYR   L  12 5   ? 15.553  -137.310 35.145  1.00 81.89  ? 5   TYR   L CG  1 
ATOM   19583 C  CD1 . TYR   L  12 5   ? 14.672  -136.258 34.968  1.00 79.17  ? 5   TYR   L CD1 1 
ATOM   19584 C  CD2 . TYR   L  12 5   ? 16.769  -137.258 34.482  1.00 81.34  ? 5   TYR   L CD2 1 
ATOM   19585 C  CE1 . TYR   L  12 5   ? 14.988  -135.183 34.155  1.00 79.40  ? 5   TYR   L CE1 1 
ATOM   19586 C  CE2 . TYR   L  12 5   ? 17.102  -136.192 33.664  1.00 79.31  ? 5   TYR   L CE2 1 
ATOM   19587 C  CZ  . TYR   L  12 5   ? 16.207  -135.151 33.500  1.00 79.71  ? 5   TYR   L CZ  1 
ATOM   19588 O  OH  . TYR   L  12 5   ? 16.528  -134.097 32.696  1.00 81.75  ? 5   TYR   L OH  1 
ATOM   19589 N  N   . GLY   L  12 6   ? 13.175  -139.427 38.297  1.00 86.89  ? 6   GLY   L N   1 
ATOM   19590 C  CA  . GLY   L  12 6   ? 12.396  -140.574 38.802  1.00 87.36  ? 6   GLY   L CA  1 
ATOM   19591 C  C   . GLY   L  12 6   ? 11.188  -140.816 37.916  1.00 87.39  ? 6   GLY   L C   1 
ATOM   19592 O  O   . GLY   L  12 6   ? 10.915  -139.957 37.066  1.00 90.43  ? 6   GLY   L O   1 
ATOM   19593 N  N   . ASP   L  12 7   ? 10.495  -141.943 38.092  1.00 88.26  ? 7   ASP   L N   1 
ATOM   19594 C  CA  . ASP   L  12 7   ? 9.257   -142.289 37.343  1.00 88.44  ? 7   ASP   L CA  1 
ATOM   19595 C  C   . ASP   L  12 7   ? 8.116   -142.455 38.351  1.00 88.07  ? 7   ASP   L C   1 
ATOM   19596 O  O   . ASP   L  12 7   ? 8.201   -143.370 39.198  1.00 88.86  ? 7   ASP   L O   1 
ATOM   19597 C  CB  . ASP   L  12 7   ? 9.453   -143.543 36.485  1.00 91.15  ? 7   ASP   L CB  1 
ATOM   19598 C  CG  . ASP   L  12 7   ? 8.280   -143.880 35.575  1.00 94.53  ? 7   ASP   L CG  1 
ATOM   19599 O  OD1 . ASP   L  12 7   ? 7.320   -143.077 35.525  1.00 98.79  ? 7   ASP   L OD1 1 
ATOM   19600 O  OD2 . ASP   L  12 7   ? 8.337   -144.945 34.918  1.00 93.15  ? 7   ASP   L OD2 1 
ATOM   19601 N  N   . ASN   L  12 8   ? 7.097   -141.597 38.255  1.00 84.98  ? 8   ASN   L N   1 
ATOM   19602 C  CA  . ASN   L  12 8   ? 5.928   -141.566 39.173  1.00 86.98  ? 8   ASN   L CA  1 
ATOM   19603 C  C   . ASN   L  12 8   ? 4.725   -142.256 38.517  1.00 85.64  ? 8   ASN   L C   1 
ATOM   19604 O  O   . ASN   L  12 8   ? 3.619   -142.174 39.090  1.00 85.45  ? 8   ASN   L O   1 
ATOM   19605 C  CB  . ASN   L  12 8   ? 5.615   -140.134 39.612  1.00 87.77  ? 8   ASN   L CB  1 
ATOM   19606 C  CG  . ASN   L  12 8   ? 6.696   -139.565 40.505  1.00 89.77  ? 8   ASN   L CG  1 
ATOM   19607 O  OD1 . ASN   L  12 8   ? 7.395   -138.629 40.121  1.00 90.03  ? 8   ASN   L OD1 1 
ATOM   19608 N  ND2 . ASN   L  12 8   ? 6.861   -140.145 41.684  1.00 89.93  ? 8   ASN   L ND2 1 
ATOM   19609 N  N   . GLY   L  12 9   ? 4.938   -142.917 37.372  1.00 88.40  ? 9   GLY   L N   1 
ATOM   19610 C  CA  . GLY   L  12 9   ? 3.952   -143.806 36.727  1.00 90.84  ? 9   GLY   L CA  1 
ATOM   19611 C  C   . GLY   L  12 9   ? 2.700   -143.056 36.311  1.00 92.60  ? 9   GLY   L C   1 
ATOM   19612 O  O   . GLY   L  12 9   ? 2.817   -141.869 35.936  1.00 92.99  ? 9   GLY   L O   1 
ATOM   19613 N  N   . GLY   L  12 10  ? 1.545   -143.725 36.375  1.00 93.02  ? 10  GLY   L N   1 
ATOM   19614 C  CA  . GLY   L  12 10  ? 0.245   -143.170 35.954  1.00 92.71  ? 10  GLY   L CA  1 
ATOM   19615 C  C   . GLY   L  12 10  ? 0.178   -142.966 34.449  1.00 92.26  ? 10  GLY   L C   1 
ATOM   19616 O  O   . GLY   L  12 10  ? 1.227   -143.080 33.783  1.00 89.06  ? 10  GLY   L O   1 
ATOM   19617 N  N   . THR   L  12 11  ? -1.013  -142.664 33.928  1.00 91.95  ? 11  THR   L N   1 
ATOM   19618 C  CA  . THR   L  12 11  ? -1.275  -142.456 32.479  1.00 94.32  ? 11  THR   L CA  1 
ATOM   19619 C  C   . THR   L  12 11  ? -2.368  -141.393 32.310  1.00 95.68  ? 11  THR   L C   1 
ATOM   19620 O  O   . THR   L  12 11  ? -3.167  -141.209 33.252  1.00 93.29  ? 11  THR   L O   1 
ATOM   19621 C  CB  . THR   L  12 11  ? -1.611  -143.792 31.800  1.00 96.98  ? 11  THR   L CB  1 
ATOM   19622 O  OG1 . THR   L  12 11  ? -1.366  -143.667 30.399  1.00 98.89  ? 11  THR   L OG1 1 
ATOM   19623 C  CG2 . THR   L  12 11  ? -3.037  -144.242 32.035  1.00 99.00  ? 11  THR   L CG2 1 
ATOM   19624 N  N   . ILE   L  12 12  ? -2.392  -140.722 31.153  1.00 94.78  ? 12  ILE   L N   1 
ATOM   19625 C  CA  . ILE   L  12 12  ? -3.348  -139.621 30.822  1.00 93.98  ? 12  ILE   L CA  1 
ATOM   19626 C  C   . ILE   L  12 12  ? -3.846  -139.789 29.383  1.00 94.00  ? 12  ILE   L C   1 
ATOM   19627 O  O   . ILE   L  12 12  ? -3.183  -140.495 28.601  1.00 90.45  ? 12  ILE   L O   1 
ATOM   19628 C  CB  . ILE   L  12 12  ? -2.696  -138.243 31.035  1.00 94.21  ? 12  ILE   L CB  1 
ATOM   19629 C  CG1 . ILE   L  12 12  ? -1.357  -138.131 30.301  1.00 92.50  ? 12  ILE   L CG1 1 
ATOM   19630 C  CG2 . ILE   L  12 12  ? -2.556  -137.950 32.521  1.00 94.02  ? 12  ILE   L CG2 1 
ATOM   19631 C  CD1 . ILE   L  12 12  ? -0.868  -136.716 30.129  1.00 92.47  ? 12  ILE   L CD1 1 
ATOM   19632 N  N   . LEU   L  12 13  ? -4.958  -139.128 29.054  1.00 95.98  ? 13  LEU   L N   1 
ATOM   19633 C  CA  . LEU   L  12 13  ? -5.725  -139.350 27.799  1.00 98.80  ? 13  LEU   L CA  1 
ATOM   19634 C  C   . LEU   L  12 13  ? -6.576  -138.104 27.503  1.00 98.56  ? 13  LEU   L C   1 
ATOM   19635 O  O   . LEU   L  12 13  ? -7.320  -137.670 28.404  1.00 101.28 ? 13  LEU   L O   1 
ATOM   19636 C  CB  . LEU   L  12 13  ? -6.545  -140.636 27.989  1.00 99.46  ? 13  LEU   L CB  1 
ATOM   19637 C  CG  . LEU   L  12 13  ? -7.925  -140.711 27.333  1.00 99.56  ? 13  LEU   L CG  1 
ATOM   19638 C  CD1 . LEU   L  12 13  ? -7.818  -140.640 25.822  1.00 98.80  ? 13  LEU   L CD1 1 
ATOM   19639 C  CD2 . LEU   L  12 13  ? -8.643  -141.989 27.743  1.00 100.80 ? 13  LEU   L CD2 1 
ATOM   19640 N  N   . GLY   L  12 14  ? -6.440  -137.540 26.295  1.00 96.09  ? 14  GLY   L N   1 
ATOM   19641 C  CA  . GLY   L  12 14  ? -7.177  -136.345 25.837  1.00 94.35  ? 14  GLY   L CA  1 
ATOM   19642 C  C   . GLY   L  12 14  ? -7.914  -136.593 24.529  1.00 93.30  ? 14  GLY   L C   1 
ATOM   19643 O  O   . GLY   L  12 14  ? -7.239  -136.901 23.527  1.00 91.41  ? 14  GLY   L O   1 
ATOM   19644 N  N   . ILE   L  12 15  ? -9.247  -136.460 24.538  1.00 95.60  ? 15  ILE   L N   1 
ATOM   19645 C  CA  . ILE   L  12 15  ? -10.135 -136.604 23.343  1.00 99.16  ? 15  ILE   L CA  1 
ATOM   19646 C  C   . ILE   L  12 15  ? -10.842 -135.263 23.106  1.00 98.79  ? 15  ILE   L C   1 
ATOM   19647 O  O   . ILE   L  12 15  ? -11.128 -134.562 24.101  1.00 97.35  ? 15  ILE   L O   1 
ATOM   19648 C  CB  . ILE   L  12 15  ? -11.133 -137.770 23.523  1.00 99.23  ? 15  ILE   L CB  1 
ATOM   19649 C  CG1 . ILE   L  12 15  ? -10.415 -139.086 23.837  1.00 101.17 ? 15  ILE   L CG1 1 
ATOM   19650 C  CG2 . ILE   L  12 15  ? -12.038 -137.907 22.306  1.00 99.47  ? 15  ILE   L CG2 1 
ATOM   19651 C  CD1 . ILE   L  12 15  ? -11.326 -140.202 24.313  1.00 104.23 ? 15  ILE   L CD1 1 
ATOM   19652 N  N   . ALA   L  12 16  ? -11.107 -134.925 21.838  1.00 97.32  ? 16  ALA   L N   1 
ATOM   19653 C  CA  . ALA   L  12 16  ? -11.744 -133.660 21.404  1.00 97.47  ? 16  ALA   L CA  1 
ATOM   19654 C  C   . ALA   L  12 16  ? -13.032 -133.950 20.625  1.00 101.22 ? 16  ALA   L C   1 
ATOM   19655 O  O   . ALA   L  12 16  ? -12.952 -134.654 19.604  1.00 103.28 ? 16  ALA   L O   1 
ATOM   19656 C  CB  . ALA   L  12 16  ? -10.776 -132.871 20.562  1.00 97.11  ? 16  ALA   L CB  1 
ATOM   19657 N  N   . GLY   L  12 17  ? -14.164 -133.403 21.085  1.00 104.52 ? 17  GLY   L N   1 
ATOM   19658 C  CA  . GLY   L  12 17  ? -15.458 -133.434 20.375  1.00 110.60 ? 17  GLY   L CA  1 
ATOM   19659 C  C   . GLY   L  12 17  ? -15.628 -132.222 19.472  1.00 115.00 ? 17  GLY   L C   1 
ATOM   19660 O  O   . GLY   L  12 17  ? -14.621 -131.529 19.214  1.00 120.52 ? 17  GLY   L O   1 
ATOM   19661 N  N   . GLU   L  12 18  ? -16.857 -131.971 19.008  1.00 119.36 ? 18  GLU   L N   1 
ATOM   19662 C  CA  . GLU   L  12 18  ? -17.192 -130.854 18.084  1.00 122.85 ? 18  GLU   L CA  1 
ATOM   19663 C  C   . GLU   L  12 18  ? -17.207 -129.526 18.850  1.00 119.19 ? 18  GLU   L C   1 
ATOM   19664 O  O   . GLU   L  12 18  ? -16.719 -128.537 18.282  1.00 124.47 ? 18  GLU   L O   1 
ATOM   19665 C  CB  . GLU   L  12 18  ? -18.540 -131.090 17.400  1.00 125.00 ? 18  GLU   L CB  1 
ATOM   19666 C  CG  . GLU   L  12 18  ? -18.817 -130.118 16.265  1.00 130.34 ? 18  GLU   L CG  1 
ATOM   19667 C  CD  . GLU   L  12 18  ? -20.118 -130.360 15.519  1.00 134.84 ? 18  GLU   L CD  1 
ATOM   19668 O  OE1 . GLU   L  12 18  ? -20.700 -131.452 15.682  1.00 138.94 ? 18  GLU   L OE1 1 
ATOM   19669 O  OE2 . GLU   L  12 18  ? -20.546 -129.454 14.776  1.00 140.09 ? 18  GLU   L OE2 1 
ATOM   19670 N  N   . ASP   L  12 19  ? -17.764 -129.501 20.068  1.00 116.81 ? 19  ASP   L N   1 
ATOM   19671 C  CA  . ASP   L  12 19  ? -17.907 -128.269 20.894  1.00 116.83 ? 19  ASP   L CA  1 
ATOM   19672 C  C   . ASP   L  12 19  ? -17.406 -128.507 22.328  1.00 113.57 ? 19  ASP   L C   1 
ATOM   19673 O  O   . ASP   L  12 19  ? -17.729 -127.678 23.205  1.00 115.10 ? 19  ASP   L O   1 
ATOM   19674 C  CB  . ASP   L  12 19  ? -19.357 -127.771 20.891  1.00 121.64 ? 19  ASP   L CB  1 
ATOM   19675 C  CG  . ASP   L  12 19  ? -20.339 -128.709 21.573  1.00 120.28 ? 19  ASP   L CG  1 
ATOM   19676 O  OD1 . ASP   L  12 19  ? -20.169 -129.934 21.436  1.00 121.64 ? 19  ASP   L OD1 1 
ATOM   19677 O  OD2 . ASP   L  12 19  ? -21.264 -128.205 22.237  1.00 126.95 ? 19  ASP   L OD2 1 
ATOM   19678 N  N   . PHE   L  12 20  ? -16.631 -129.570 22.561  1.00 108.43 ? 20  PHE   L N   1 
ATOM   19679 C  CA  . PHE   L  12 20  ? -16.063 -129.915 23.892  1.00 107.11 ? 20  PHE   L CA  1 
ATOM   19680 C  C   . PHE   L  12 20  ? -14.738 -130.666 23.723  1.00 101.92 ? 20  PHE   L C   1 
ATOM   19681 O  O   . PHE   L  12 20  ? -14.426 -131.123 22.606  1.00 95.14  ? 20  PHE   L O   1 
ATOM   19682 C  CB  . PHE   L  12 20  ? -17.051 -130.764 24.696  1.00 110.38 ? 20  PHE   L CB  1 
ATOM   19683 C  CG  . PHE   L  12 20  ? -17.164 -132.191 24.223  1.00 110.80 ? 20  PHE   L CG  1 
ATOM   19684 C  CD1 . PHE   L  12 20  ? -17.953 -132.516 23.130  1.00 110.00 ? 20  PHE   L CD1 1 
ATOM   19685 C  CD2 . PHE   L  12 20  ? -16.469 -133.206 24.862  1.00 111.80 ? 20  PHE   L CD2 1 
ATOM   19686 C  CE1 . PHE   L  12 20  ? -18.054 -133.826 22.691  1.00 111.43 ? 20  PHE   L CE1 1 
ATOM   19687 C  CE2 . PHE   L  12 20  ? -16.568 -134.516 24.419  1.00 113.96 ? 20  PHE   L CE2 1 
ATOM   19688 C  CZ  . PHE   L  12 20  ? -17.356 -134.822 23.333  1.00 113.81 ? 20  PHE   L CZ  1 
ATOM   19689 N  N   . ALA   L  12 21  ? -13.994 -130.798 24.824  1.00 100.42 ? 21  ALA   L N   1 
ATOM   19690 C  CA  . ALA   L  12 21  ? -12.750 -131.595 24.926  1.00 98.34  ? 21  ALA   L CA  1 
ATOM   19691 C  C   . ALA   L  12 21  ? -12.615 -132.139 26.352  1.00 97.86  ? 21  ALA   L C   1 
ATOM   19692 O  O   . ALA   L  12 21  ? -12.910 -131.387 27.302  1.00 101.29 ? 21  ALA   L O   1 
ATOM   19693 C  CB  . ALA   L  12 21  ? -11.560 -130.751 24.542  1.00 97.74  ? 21  ALA   L CB  1 
ATOM   19694 N  N   . VAL   L  12 22  ? -12.197 -133.400 26.485  1.00 96.81  ? 22  VAL   L N   1 
ATOM   19695 C  CA  . VAL   L  12 22  ? -11.935 -134.062 27.798  1.00 97.09  ? 22  VAL   L CA  1 
ATOM   19696 C  C   . VAL   L  12 22  ? -10.433 -134.327 27.922  1.00 95.34  ? 22  VAL   L C   1 
ATOM   19697 O  O   . VAL   L  12 22  ? -9.801  -134.677 26.903  1.00 92.41  ? 22  VAL   L O   1 
ATOM   19698 C  CB  . VAL   L  12 22  ? -12.744 -135.361 27.975  1.00 97.30  ? 22  VAL   L CB  1 
ATOM   19699 C  CG1 . VAL   L  12 22  ? -14.238 -135.088 28.019  1.00 99.16  ? 22  VAL   L CG1 1 
ATOM   19700 C  CG2 . VAL   L  12 22  ? -12.418 -136.399 26.911  1.00 98.57  ? 22  VAL   L CG2 1 
ATOM   19701 N  N   . LEU   L  12 23  ? -9.897  -134.144 29.131  1.00 94.53  ? 23  LEU   L N   1 
ATOM   19702 C  CA  . LEU   L  12 23  ? -8.516  -134.527 29.516  1.00 91.96  ? 23  LEU   L CA  1 
ATOM   19703 C  C   . LEU   L  12 23  ? -8.619  -135.362 30.794  1.00 91.58  ? 23  LEU   L C   1 
ATOM   19704 O  O   . LEU   L  12 23  ? -8.933  -134.786 31.854  1.00 90.07  ? 23  LEU   L O   1 
ATOM   19705 C  CB  . LEU   L  12 23  ? -7.672  -133.268 29.732  1.00 91.44  ? 23  LEU   L CB  1 
ATOM   19706 C  CG  . LEU   L  12 23  ? -6.198  -133.356 29.328  1.00 92.48  ? 23  LEU   L CG  1 
ATOM   19707 C  CD1 . LEU   L  12 23  ? -5.391  -132.262 30.012  1.00 94.56  ? 23  LEU   L CD1 1 
ATOM   19708 C  CD2 . LEU   L  12 23  ? -5.594  -134.715 29.643  1.00 91.10  ? 23  LEU   L CD2 1 
ATOM   19709 N  N   . ALA   L  12 24  ? -8.414  -136.674 30.674  1.00 91.98  ? 24  ALA   L N   1 
ATOM   19710 C  CA  . ALA   L  12 24  ? -8.548  -137.657 31.773  1.00 91.72  ? 24  ALA   L CA  1 
ATOM   19711 C  C   . ALA   L  12 24  ? -7.162  -138.142 32.205  1.00 85.38  ? 24  ALA   L C   1 
ATOM   19712 O  O   . ALA   L  12 24  ? -6.245  -138.174 31.361  1.00 80.88  ? 24  ALA   L O   1 
ATOM   19713 C  CB  . ALA   L  12 24  ? -9.419  -138.807 31.332  1.00 93.29  ? 24  ALA   L CB  1 
ATOM   19714 N  N   . GLY   L  12 25  ? -7.036  -138.500 33.484  1.00 87.83  ? 25  GLY   L N   1 
ATOM   19715 C  CA  . GLY   L  12 25  ? -5.825  -139.099 34.072  1.00 90.56  ? 25  GLY   L CA  1 
ATOM   19716 C  C   . GLY   L  12 25  ? -6.159  -139.855 35.345  1.00 93.92  ? 25  GLY   L C   1 
ATOM   19717 O  O   . GLY   L  12 25  ? -6.979  -139.342 36.132  1.00 98.47  ? 25  GLY   L O   1 
ATOM   19718 N  N   . ASP   L  12 26  ? -5.556  -141.031 35.541  1.00 94.42  ? 26  ASP   L N   1 
ATOM   19719 C  CA  . ASP   L  12 26  ? -5.684  -141.823 36.792  1.00 97.38  ? 26  ASP   L CA  1 
ATOM   19720 C  C   . ASP   L  12 26  ? -5.014  -141.044 37.926  1.00 94.48  ? 26  ASP   L C   1 
ATOM   19721 O  O   . ASP   L  12 26  ? -4.135  -140.215 37.632  1.00 98.19  ? 26  ASP   L O   1 
ATOM   19722 C  CB  . ASP   L  12 26  ? -5.068  -143.217 36.658  1.00 99.97  ? 26  ASP   L CB  1 
ATOM   19723 C  CG  . ASP   L  12 26  ? -3.554  -143.212 36.507  1.00 104.94 ? 26  ASP   L CG  1 
ATOM   19724 O  OD1 . ASP   L  12 26  ? -3.027  -142.247 35.912  1.00 107.38 ? 26  ASP   L OD1 1 
ATOM   19725 O  OD2 . ASP   L  12 26  ? -2.911  -144.169 36.991  1.00 104.85 ? 26  ASP   L OD2 1 
ATOM   19726 N  N   . THR   L  12 27  ? -5.397  -141.319 39.173  1.00 92.70  ? 27  THR   L N   1 
ATOM   19727 C  CA  . THR   L  12 27  ? -4.992  -140.525 40.363  1.00 93.65  ? 27  THR   L CA  1 
ATOM   19728 C  C   . THR   L  12 27  ? -3.908  -141.265 41.159  1.00 93.76  ? 27  THR   L C   1 
ATOM   19729 O  O   . THR   L  12 27  ? -3.525  -140.759 42.232  1.00 92.77  ? 27  THR   L O   1 
ATOM   19730 C  CB  . THR   L  12 27  ? -6.220  -140.196 41.217  1.00 95.84  ? 27  THR   L CB  1 
ATOM   19731 O  OG1 . THR   L  12 27  ? -6.797  -141.436 41.631  1.00 95.17  ? 27  THR   L OG1 1 
ATOM   19732 C  CG2 . THR   L  12 27  ? -7.236  -139.356 40.475  1.00 95.42  ? 27  THR   L CG2 1 
ATOM   19733 N  N   . ARG   L  12 28  ? -3.426  -142.402 40.653  1.00 92.63  ? 28  ARG   L N   1 
ATOM   19734 C  CA  . ARG   L  12 28  ? -2.368  -143.211 41.314  1.00 94.26  ? 28  ARG   L CA  1 
ATOM   19735 C  C   . ARG   L  12 28  ? -1.002  -142.563 41.062  1.00 90.10  ? 28  ARG   L C   1 
ATOM   19736 O  O   . ARG   L  12 28  ? -0.716  -142.217 39.897  1.00 86.36  ? 28  ARG   L O   1 
ATOM   19737 C  CB  . ARG   L  12 28  ? -2.389  -144.657 40.812  1.00 97.66  ? 28  ARG   L CB  1 
ATOM   19738 C  CG  . ARG   L  12 28  ? -1.285  -145.532 41.392  1.00 100.96 ? 28  ARG   L CG  1 
ATOM   19739 C  CD  . ARG   L  12 28  ? -1.375  -146.976 40.934  1.00 100.93 ? 28  ARG   L CD  1 
ATOM   19740 N  NE  . ARG   L  12 28  ? -2.264  -147.779 41.760  1.00 102.34 ? 28  ARG   L NE  1 
ATOM   19741 C  CZ  . ARG   L  12 28  ? -2.575  -149.049 41.527  1.00 106.96 ? 28  ARG   L CZ  1 
ATOM   19742 N  NH1 . ARG   L  12 28  ? -3.397  -149.689 42.343  1.00 111.45 ? 28  ARG   L NH1 1 
ATOM   19743 N  NH2 . ARG   L  12 28  ? -2.068  -149.681 40.482  1.00 111.64 ? 28  ARG   L NH2 1 
ATOM   19744 N  N   . ASN   L  12 29  ? -0.200  -142.434 42.125  1.00 90.48  ? 29  ASN   L N   1 
ATOM   19745 C  CA  . ASN   L  12 29  ? 1.201   -141.936 42.108  1.00 88.62  ? 29  ASN   L CA  1 
ATOM   19746 C  C   . ASN   L  12 29  ? 2.088   -143.003 42.761  1.00 85.15  ? 29  ASN   L C   1 
ATOM   19747 O  O   . ASN   L  12 29  ? 1.741   -143.440 43.877  1.00 80.68  ? 29  ASN   L O   1 
ATOM   19748 C  CB  . ASN   L  12 29  ? 1.312   -140.582 42.814  1.00 91.32  ? 29  ASN   L CB  1 
ATOM   19749 C  CG  . ASN   L  12 29  ? 2.691   -139.959 42.722  1.00 92.44  ? 29  ASN   L CG  1 
ATOM   19750 O  OD1 . ASN   L  12 29  ? 3.661   -140.502 43.248  1.00 90.61  ? 29  ASN   L OD1 1 
ATOM   19751 N  ND2 . ASN   L  12 29  ? 2.786   -138.806 42.078  1.00 96.41  ? 29  ASN   L ND2 1 
ATOM   19752 N  N   . ILE   L  12 30  ? 3.174   -143.404 42.089  1.00 85.91  ? 30  ILE   L N   1 
ATOM   19753 C  CA  . ILE   L  12 30  ? 4.024   -144.573 42.475  1.00 86.85  ? 30  ILE   L CA  1 
ATOM   19754 C  C   . ILE   L  12 30  ? 5.507   -144.198 42.408  1.00 88.38  ? 30  ILE   L C   1 
ATOM   19755 O  O   . ILE   L  12 30  ? 5.844   -143.241 41.696  1.00 87.00  ? 30  ILE   L O   1 
ATOM   19756 C  CB  . ILE   L  12 30  ? 3.719   -145.792 41.577  1.00 87.68  ? 30  ILE   L CB  1 
ATOM   19757 C  CG1 . ILE   L  12 30  ? 4.164   -145.590 40.123  1.00 88.20  ? 30  ILE   L CG1 1 
ATOM   19758 C  CG2 . ILE   L  12 30  ? 2.248   -146.167 41.661  1.00 89.17  ? 30  ILE   L CG2 1 
ATOM   19759 C  CD1 . ILE   L  12 30  ? 5.548   -146.126 39.810  1.00 88.21  ? 30  ILE   L CD1 1 
ATOM   19760 N  N   . THR   L  12 31  ? 6.346   -144.944 43.134  1.00 89.54  ? 31  THR   L N   1 
ATOM   19761 C  CA  . THR   L  12 31  ? 7.814   -145.065 42.915  1.00 91.59  ? 31  THR   L CA  1 
ATOM   19762 C  C   . THR   L  12 31  ? 8.190   -146.547 43.055  1.00 93.52  ? 31  THR   L C   1 
ATOM   19763 O  O   . THR   L  12 31  ? 7.818   -147.154 44.081  1.00 89.55  ? 31  THR   L O   1 
ATOM   19764 C  CB  . THR   L  12 31  ? 8.631   -144.171 43.861  1.00 92.72  ? 31  THR   L CB  1 
ATOM   19765 O  OG1 . THR   L  12 31  ? 8.162   -144.373 45.194  1.00 94.36  ? 31  THR   L OG1 1 
ATOM   19766 C  CG2 . THR   L  12 31  ? 8.548   -142.697 43.523  1.00 90.10  ? 31  THR   L CG2 1 
ATOM   19767 N  N   . ASP   L  12 32  ? 8.875   -147.104 42.050  1.00 94.96  ? 32  ASP   L N   1 
ATOM   19768 C  CA  . ASP   L  12 32  ? 9.248   -148.542 41.976  1.00 94.78  ? 32  ASP   L CA  1 
ATOM   19769 C  C   . ASP   L  12 32  ? 7.970   -149.378 42.135  1.00 96.46  ? 32  ASP   L C   1 
ATOM   19770 O  O   . ASP   L  12 32  ? 7.058   -149.194 41.302  1.00 93.13  ? 32  ASP   L O   1 
ATOM   19771 C  CB  . ASP   L  12 32  ? 10.351  -148.863 42.989  1.00 98.39  ? 32  ASP   L CB  1 
ATOM   19772 C  CG  . ASP   L  12 32  ? 11.632  -148.079 42.756  1.00 98.34  ? 32  ASP   L CG  1 
ATOM   19773 O  OD1 . ASP   L  12 32  ? 11.968  -147.837 41.578  1.00 94.27  ? 32  ASP   L OD1 1 
ATOM   19774 O  OD2 . ASP   L  12 32  ? 12.281  -147.709 43.755  1.00 104.82 ? 32  ASP   L OD2 1 
ATOM   19775 N  N   . TYR   L  12 33  ? 7.887   -150.226 43.169  1.00 95.39  ? 33  TYR   L N   1 
ATOM   19776 C  CA  . TYR   L  12 33  ? 6.778   -151.195 43.387  1.00 95.42  ? 33  TYR   L CA  1 
ATOM   19777 C  C   . TYR   L  12 33  ? 5.876   -150.750 44.546  1.00 91.60  ? 33  TYR   L C   1 
ATOM   19778 O  O   . TYR   L  12 33  ? 5.104   -151.591 45.046  1.00 95.36  ? 33  TYR   L O   1 
ATOM   19779 C  CB  . TYR   L  12 33  ? 7.345   -152.599 43.623  1.00 97.55  ? 33  TYR   L CB  1 
ATOM   19780 C  CG  . TYR   L  12 33  ? 7.772   -153.307 42.363  1.00 100.08 ? 33  TYR   L CG  1 
ATOM   19781 C  CD1 . TYR   L  12 33  ? 6.844   -153.947 41.557  1.00 98.21  ? 33  TYR   L CD1 1 
ATOM   19782 C  CD2 . TYR   L  12 33  ? 9.099   -153.322 41.963  1.00 102.98 ? 33  TYR   L CD2 1 
ATOM   19783 C  CE1 . TYR   L  12 33  ? 7.222   -154.590 40.390  1.00 99.41  ? 33  TYR   L CE1 1 
ATOM   19784 C  CE2 . TYR   L  12 33  ? 9.495   -153.963 40.800  1.00 102.66 ? 33  TYR   L CE2 1 
ATOM   19785 C  CZ  . TYR   L  12 33  ? 8.553   -154.599 40.012  1.00 101.83 ? 33  TYR   L CZ  1 
ATOM   19786 O  OH  . TYR   L  12 33  ? 8.942   -155.228 38.867  1.00 105.91 ? 33  TYR   L OH  1 
ATOM   19787 N  N   . SER   L  12 34  ? 5.938   -149.473 44.939  1.00 88.96  ? 34  SER   L N   1 
ATOM   19788 C  CA  . SER   L  12 34  ? 5.150   -148.896 46.060  1.00 86.11  ? 34  SER   L CA  1 
ATOM   19789 C  C   . SER   L  12 34  ? 4.165   -147.850 45.533  1.00 86.39  ? 34  SER   L C   1 
ATOM   19790 O  O   . SER   L  12 34  ? 4.482   -147.197 44.517  1.00 84.63  ? 34  SER   L O   1 
ATOM   19791 C  CB  . SER   L  12 34  ? 6.049   -148.295 47.102  1.00 84.19  ? 34  SER   L CB  1 
ATOM   19792 O  OG  . SER   L  12 34  ? 6.584   -149.297 47.950  1.00 84.02  ? 34  SER   L OG  1 
ATOM   19793 N  N   . ILE   L  12 35  ? 3.027   -147.698 46.219  1.00 88.52  ? 35  ILE   L N   1 
ATOM   19794 C  CA  . ILE   L  12 35  ? 2.027   -146.617 45.971  1.00 89.84  ? 35  ILE   L CA  1 
ATOM   19795 C  C   . ILE   L  12 35  ? 2.297   -145.480 46.961  1.00 87.46  ? 35  ILE   L C   1 
ATOM   19796 O  O   . ILE   L  12 35  ? 2.326   -145.741 48.179  1.00 84.94  ? 35  ILE   L O   1 
ATOM   19797 C  CB  . ILE   L  12 35  ? 0.581   -147.141 46.083  1.00 93.96  ? 35  ILE   L CB  1 
ATOM   19798 C  CG1 . ILE   L  12 35  ? 0.307   -148.258 45.073  1.00 94.15  ? 35  ILE   L CG1 1 
ATOM   19799 C  CG2 . ILE   L  12 35  ? -0.417  -145.998 45.936  1.00 97.02  ? 35  ILE   L CG2 1 
ATOM   19800 C  CD1 . ILE   L  12 35  ? -0.933  -149.067 45.374  1.00 97.17  ? 35  ILE   L CD1 1 
ATOM   19801 N  N   . ASN   L  12 36  ? 2.481   -144.267 46.438  1.00 87.94  ? 36  ASN   L N   1 
ATOM   19802 C  CA  . ASN   L  12 36  ? 2.682   -143.026 47.228  1.00 87.07  ? 36  ASN   L CA  1 
ATOM   19803 C  C   . ASN   L  12 36  ? 1.309   -142.509 47.665  1.00 85.42  ? 36  ASN   L C   1 
ATOM   19804 O  O   . ASN   L  12 36  ? 1.115   -142.277 48.876  1.00 83.66  ? 36  ASN   L O   1 
ATOM   19805 C  CB  . ASN   L  12 36  ? 3.458   -141.990 46.414  1.00 86.75  ? 36  ASN   L CB  1 
ATOM   19806 C  CG  . ASN   L  12 36  ? 4.813   -142.493 45.962  1.00 85.07  ? 36  ASN   L CG  1 
ATOM   19807 O  OD1 . ASN   L  12 36  ? 5.457   -143.270 46.660  1.00 86.17  ? 36  ASN   L OD1 1 
ATOM   19808 N  ND2 . ASN   L  12 36  ? 5.259   -142.052 44.799  1.00 87.71  ? 36  ASN   L ND2 1 
ATOM   19809 N  N   . SER   L  12 37  ? 0.393   -142.370 46.703  1.00 86.48  ? 37  SER   L N   1 
ATOM   19810 C  CA  . SER   L  12 37  ? -0.968  -141.806 46.886  1.00 88.72  ? 37  SER   L CA  1 
ATOM   19811 C  C   . SER   L  12 37  ? -1.942  -142.517 45.945  1.00 87.32  ? 37  SER   L C   1 
ATOM   19812 O  O   . SER   L  12 37  ? -1.547  -142.813 44.798  1.00 85.33  ? 37  SER   L O   1 
ATOM   19813 C  CB  . SER   L  12 37  ? -0.962  -140.314 46.657  1.00 90.50  ? 37  SER   L CB  1 
ATOM   19814 O  OG  . SER   L  12 37  ? -2.248  -139.758 46.893  1.00 93.57  ? 37  SER   L OG  1 
ATOM   19815 N  N   . ARG   L  12 38  ? -3.155  -142.797 46.430  1.00 86.47  ? 38  ARG   L N   1 
ATOM   19816 C  CA  . ARG   L  12 38  ? -4.270  -143.359 45.623  1.00 89.96  ? 38  ARG   L CA  1 
ATOM   19817 C  C   . ARG   L  12 38  ? -5.051  -142.216 44.961  1.00 90.72  ? 38  ARG   L C   1 
ATOM   19818 O  O   . ARG   L  12 38  ? -5.698  -142.476 43.925  1.00 86.31  ? 38  ARG   L O   1 
ATOM   19819 C  CB  . ARG   L  12 38  ? -5.181  -144.228 46.494  1.00 91.76  ? 38  ARG   L CB  1 
ATOM   19820 C  CG  . ARG   L  12 38  ? -4.496  -145.467 47.054  1.00 92.24  ? 38  ARG   L CG  1 
ATOM   19821 C  CD  . ARG   L  12 38  ? -5.484  -146.533 47.484  1.00 94.45  ? 38  ARG   L CD  1 
ATOM   19822 N  NE  . ARG   L  12 38  ? -4.844  -147.658 48.161  1.00 96.87  ? 38  ARG   L NE  1 
ATOM   19823 C  CZ  . ARG   L  12 38  ? -4.365  -148.755 47.570  1.00 97.67  ? 38  ARG   L CZ  1 
ATOM   19824 N  NH1 . ARG   L  12 38  ? -4.431  -148.911 46.257  1.00 97.97  ? 38  ARG   L NH1 1 
ATOM   19825 N  NH2 . ARG   L  12 38  ? -3.813  -149.705 48.305  1.00 96.80  ? 38  ARG   L NH2 1 
ATOM   19826 N  N   . TYR   L  12 39  ? -5.000  -141.007 45.533  1.00 92.54  ? 39  TYR   L N   1 
ATOM   19827 C  CA  . TYR   L  12 39  ? -5.616  -139.782 44.957  1.00 93.30  ? 39  TYR   L CA  1 
ATOM   19828 C  C   . TYR   L  12 39  ? -4.633  -138.605 45.017  1.00 93.25  ? 39  TYR   L C   1 
ATOM   19829 O  O   . TYR   L  12 39  ? -4.633  -137.854 46.012  1.00 96.98  ? 39  TYR   L O   1 
ATOM   19830 C  CB  . TYR   L  12 39  ? -6.933  -139.438 45.657  1.00 94.69  ? 39  TYR   L CB  1 
ATOM   19831 C  CG  . TYR   L  12 39  ? -7.650  -138.267 45.035  1.00 96.20  ? 39  TYR   L CG  1 
ATOM   19832 C  CD1 . TYR   L  12 39  ? -8.320  -138.401 43.829  1.00 98.22  ? 39  TYR   L CD1 1 
ATOM   19833 C  CD2 . TYR   L  12 39  ? -7.632  -137.016 45.629  1.00 95.39  ? 39  TYR   L CD2 1 
ATOM   19834 C  CE1 . TYR   L  12 39  ? -8.969  -137.330 43.238  1.00 97.54  ? 39  TYR   L CE1 1 
ATOM   19835 C  CE2 . TYR   L  12 39  ? -8.277  -135.934 45.052  1.00 95.47  ? 39  TYR   L CE2 1 
ATOM   19836 C  CZ  . TYR   L  12 39  ? -8.949  -136.092 43.852  1.00 96.62  ? 39  TYR   L CZ  1 
ATOM   19837 O  OH  . TYR   L  12 39  ? -9.586  -135.037 43.270  1.00 98.59  ? 39  TYR   L OH  1 
ATOM   19838 N  N   . GLU   L  12 40  ? -3.825  -138.458 43.964  1.00 92.52  ? 40  GLU   L N   1 
ATOM   19839 C  CA  . GLU   L  12 40  ? -2.958  -137.278 43.704  1.00 93.79  ? 40  GLU   L CA  1 
ATOM   19840 C  C   . GLU   L  12 40  ? -3.272  -136.775 42.300  1.00 92.53  ? 40  GLU   L C   1 
ATOM   19841 O  O   . GLU   L  12 40  ? -2.764  -137.323 41.325  1.00 93.63  ? 40  GLU   L O   1 
ATOM   19842 C  CB  . GLU   L  12 40  ? -1.480  -137.649 43.846  1.00 94.58  ? 40  GLU   L CB  1 
ATOM   19843 C  CG  . GLU   L  12 40  ? -0.535  -136.462 43.745  1.00 98.97  ? 40  GLU   L CG  1 
ATOM   19844 C  CD  . GLU   L  12 40  ? -0.629  -135.455 44.881  1.00 105.13 ? 40  GLU   L CD  1 
ATOM   19845 O  OE1 . GLU   L  12 40  ? -0.958  -135.867 46.015  1.00 105.93 ? 40  GLU   L OE1 1 
ATOM   19846 O  OE2 . GLU   L  12 40  ? -0.371  -134.256 44.630  1.00 110.85 ? 40  GLU   L OE2 1 
ATOM   19847 N  N   . PRO   L  12 41  ? -4.129  -135.738 42.143  1.00 95.55  ? 41  PRO   L N   1 
ATOM   19848 C  CA  . PRO   L  12 41  ? -4.537  -135.275 40.817  1.00 94.31  ? 41  PRO   L CA  1 
ATOM   19849 C  C   . PRO   L  12 41  ? -3.341  -134.709 40.038  1.00 92.11  ? 41  PRO   L C   1 
ATOM   19850 O  O   . PRO   L  12 41  ? -2.498  -134.079 40.654  1.00 93.81  ? 41  PRO   L O   1 
ATOM   19851 C  CB  . PRO   L  12 41  ? -5.577  -134.177 41.094  1.00 95.89  ? 41  PRO   L CB  1 
ATOM   19852 C  CG  . PRO   L  12 41  ? -5.971  -134.371 42.546  1.00 98.73  ? 41  PRO   L CG  1 
ATOM   19853 C  CD  . PRO   L  12 41  ? -4.743  -134.946 43.220  1.00 98.37  ? 41  PRO   L CD  1 
ATOM   19854 N  N   . LYS   L  12 42  ? -3.289  -134.967 38.726  1.00 90.86  ? 42  LYS   L N   1 
ATOM   19855 C  CA  . LYS   L  12 42  ? -2.242  -134.437 37.808  1.00 90.17  ? 42  LYS   L CA  1 
ATOM   19856 C  C   . LYS   L  12 42  ? -2.870  -133.810 36.551  1.00 90.40  ? 42  LYS   L C   1 
ATOM   19857 O  O   . LYS   L  12 42  ? -2.108  -133.503 35.606  1.00 86.84  ? 42  LYS   L O   1 
ATOM   19858 C  CB  . LYS   L  12 42  ? -1.263  -135.554 37.444  1.00 89.09  ? 42  LYS   L CB  1 
ATOM   19859 C  CG  . LYS   L  12 42  ? -1.850  -136.701 36.634  1.00 91.37  ? 42  LYS   L CG  1 
ATOM   19860 C  CD  . LYS   L  12 42  ? -1.025  -137.955 36.757  1.00 92.90  ? 42  LYS   L CD  1 
ATOM   19861 C  CE  . LYS   L  12 42  ? -1.672  -139.177 36.144  1.00 95.78  ? 42  LYS   L CE  1 
ATOM   19862 N  NZ  . LYS   L  12 42  ? -1.468  -140.367 37.003  1.00 96.73  ? 42  LYS   L NZ  1 
ATOM   19863 N  N   . VAL   L  12 43  ? -4.195  -133.615 36.542  1.00 90.12  ? 43  VAL   L N   1 
ATOM   19864 C  CA  . VAL   L  12 43  ? -4.934  -132.835 35.505  1.00 90.62  ? 43  VAL   L CA  1 
ATOM   19865 C  C   . VAL   L  12 43  ? -5.453  -131.560 36.175  1.00 89.79  ? 43  VAL   L C   1 
ATOM   19866 O  O   . VAL   L  12 43  ? -6.176  -131.677 37.182  1.00 92.62  ? 43  VAL   L O   1 
ATOM   19867 C  CB  . VAL   L  12 43  ? -6.087  -133.643 34.884  1.00 89.63  ? 43  VAL   L CB  1 
ATOM   19868 C  CG1 . VAL   L  12 43  ? -6.694  -132.909 33.702  1.00 91.60  ? 43  VAL   L CG1 1 
ATOM   19869 C  CG2 . VAL   L  12 43  ? -5.655  -135.041 34.475  1.00 90.52  ? 43  VAL   L CG2 1 
ATOM   19870 N  N   . PHE   L  12 44  ? -5.104  -130.391 35.632  1.00 90.00  ? 44  PHE   L N   1 
ATOM   19871 C  CA  . PHE   L  12 44  ? -5.330  -129.073 36.278  1.00 91.06  ? 44  PHE   L CA  1 
ATOM   19872 C  C   . PHE   L  12 44  ? -6.035  -128.116 35.314  1.00 87.86  ? 44  PHE   L C   1 
ATOM   19873 O  O   . PHE   L  12 44  ? -5.724  -128.129 34.107  1.00 80.69  ? 44  PHE   L O   1 
ATOM   19874 C  CB  . PHE   L  12 44  ? -4.001  -128.483 36.750  1.00 89.53  ? 44  PHE   L CB  1 
ATOM   19875 C  CG  . PHE   L  12 44  ? -3.262  -129.351 37.735  1.00 89.50  ? 44  PHE   L CG  1 
ATOM   19876 C  CD1 . PHE   L  12 44  ? -3.644  -129.390 39.067  1.00 92.08  ? 44  PHE   L CD1 1 
ATOM   19877 C  CD2 . PHE   L  12 44  ? -2.198  -130.143 37.330  1.00 88.93  ? 44  PHE   L CD2 1 
ATOM   19878 C  CE1 . PHE   L  12 44  ? -2.972  -130.194 39.975  1.00 89.98  ? 44  PHE   L CE1 1 
ATOM   19879 C  CE2 . PHE   L  12 44  ? -1.526  -130.946 38.240  1.00 87.46  ? 44  PHE   L CE2 1 
ATOM   19880 C  CZ  . PHE   L  12 44  ? -1.914  -130.971 39.560  1.00 87.20  ? 44  PHE   L CZ  1 
ATOM   19881 N  N   . ASP   L  12 45  ? -6.961  -127.323 35.862  1.00 92.52  ? 45  ASP   L N   1 
ATOM   19882 C  CA  . ASP   L  12 45  ? -7.559  -126.120 35.227  1.00 91.78  ? 45  ASP   L CA  1 
ATOM   19883 C  C   . ASP   L  12 45  ? -6.541  -124.984 35.373  1.00 88.36  ? 45  ASP   L C   1 
ATOM   19884 O  O   . ASP   L  12 45  ? -6.196  -124.668 36.522  1.00 85.99  ? 45  ASP   L O   1 
ATOM   19885 C  CB  . ASP   L  12 45  ? -8.909  -125.795 35.877  1.00 97.46  ? 45  ASP   L CB  1 
ATOM   19886 C  CG  . ASP   L  12 45  ? -9.725  -124.732 35.165  1.00 102.08 ? 45  ASP   L CG  1 
ATOM   19887 O  OD1 . ASP   L  12 45  ? -9.178  -124.070 34.260  1.00 111.39 ? 45  ASP   L OD1 1 
ATOM   19888 O  OD2 . ASP   L  12 45  ? -10.908 -124.576 35.524  1.00 111.70 ? 45  ASP   L OD2 1 
ATOM   19889 N  N   . CYS   L  12 46  ? -6.055  -124.428 34.258  1.00 88.11  ? 46  CYS   L N   1 
ATOM   19890 C  CA  . CYS   L  12 46  ? -4.995  -123.381 34.219  1.00 91.62  ? 46  CYS   L CA  1 
ATOM   19891 C  C   . CYS   L  12 46  ? -5.586  -122.000 33.893  1.00 93.57  ? 46  CYS   L C   1 
ATOM   19892 O  O   . CYS   L  12 46  ? -4.792  -121.070 33.645  1.00 92.49  ? 46  CYS   L O   1 
ATOM   19893 C  CB  . CYS   L  12 46  ? -3.926  -123.741 33.195  1.00 91.42  ? 46  CYS   L CB  1 
ATOM   19894 S  SG  . CYS   L  12 46  ? -3.134  -125.331 33.534  1.00 91.93  ? 46  CYS   L SG  1 
ATOM   19895 N  N   . GLY   L  12 47  ? -6.917  -121.864 33.909  1.00 95.66  ? 47  GLY   L N   1 
ATOM   19896 C  CA  . GLY   L  12 47  ? -7.627  -120.630 33.521  1.00 98.13  ? 47  GLY   L CA  1 
ATOM   19897 C  C   . GLY   L  12 47  ? -7.776  -120.524 32.013  1.00 101.71 ? 47  GLY   L C   1 
ATOM   19898 O  O   . GLY   L  12 47  ? -7.137  -121.324 31.300  1.00 103.34 ? 47  GLY   L O   1 
ATOM   19899 N  N   . ASP   L  12 48  ? -8.595  -119.575 31.547  1.00 104.38 ? 48  ASP   L N   1 
ATOM   19900 C  CA  . ASP   L  12 48  ? -8.877  -119.303 30.109  1.00 106.35 ? 48  ASP   L CA  1 
ATOM   19901 C  C   . ASP   L  12 48  ? -9.343  -120.582 29.396  1.00 107.22 ? 48  ASP   L C   1 
ATOM   19902 O  O   . ASP   L  12 48  ? -9.044  -120.723 28.192  1.00 105.28 ? 48  ASP   L O   1 
ATOM   19903 C  CB  . ASP   L  12 48  ? -7.650  -118.712 29.409  1.00 108.46 ? 48  ASP   L CB  1 
ATOM   19904 C  CG  . ASP   L  12 48  ? -7.316  -117.296 29.837  1.00 110.23 ? 48  ASP   L CG  1 
ATOM   19905 O  OD1 . ASP   L  12 48  ? -7.863  -116.844 30.863  1.00 111.97 ? 48  ASP   L OD1 1 
ATOM   19906 O  OD2 . ASP   L  12 48  ? -6.511  -116.659 29.134  1.00 117.86 ? 48  ASP   L OD2 1 
ATOM   19907 N  N   . ASN   L  12 49  ? -10.062 -121.465 30.100  1.00 104.94 ? 49  ASN   L N   1 
ATOM   19908 C  CA  . ASN   L  12 49  ? -10.612 -122.738 29.557  1.00 105.07 ? 49  ASN   L CA  1 
ATOM   19909 C  C   . ASN   L  12 49  ? -9.492  -123.579 28.937  1.00 101.66 ? 49  ASN   L C   1 
ATOM   19910 O  O   . ASN   L  12 49  ? -9.718  -124.166 27.857  1.00 100.20 ? 49  ASN   L O   1 
ATOM   19911 C  CB  . ASN   L  12 49  ? -11.727 -122.481 28.541  1.00 106.36 ? 49  ASN   L CB  1 
ATOM   19912 C  CG  . ASN   L  12 49  ? -13.106 -122.619 29.145  1.00 110.18 ? 49  ASN   L CG  1 
ATOM   19913 O  OD1 . ASN   L  12 49  ? -14.006 -123.158 28.508  1.00 116.66 ? 49  ASN   L OD1 1 
ATOM   19914 N  ND2 . ASN   L  12 49  ? -13.281 -122.145 30.369  1.00 110.79 ? 49  ASN   L ND2 1 
ATOM   19915 N  N   . ILE   L  12 50  ? -8.334  -123.632 29.600  1.00 100.95 ? 50  ILE   L N   1 
ATOM   19916 C  CA  . ILE   L  12 50  ? -7.217  -124.560 29.258  1.00 96.41  ? 50  ILE   L CA  1 
ATOM   19917 C  C   . ILE   L  12 50  ? -7.032  -125.521 30.433  1.00 96.45  ? 50  ILE   L C   1 
ATOM   19918 O  O   . ILE   L  12 50  ? -6.803  -125.040 31.561  1.00 92.25  ? 50  ILE   L O   1 
ATOM   19919 C  CB  . ILE   L  12 50  ? -5.915  -123.800 28.935  1.00 96.21  ? 50  ILE   L CB  1 
ATOM   19920 C  CG1 . ILE   L  12 50  ? -6.115  -122.780 27.811  1.00 97.93  ? 50  ILE   L CG1 1 
ATOM   19921 C  CG2 . ILE   L  12 50  ? -4.791  -124.776 28.611  1.00 94.10  ? 50  ILE   L CG2 1 
ATOM   19922 C  CD1 . ILE   L  12 50  ? -5.083  -121.677 27.802  1.00 97.85  ? 50  ILE   L CD1 1 
ATOM   19923 N  N   . VAL   L  12 51  ? -7.143  -126.824 30.165  1.00 95.52  ? 51  VAL   L N   1 
ATOM   19924 C  CA  . VAL   L  12 51  ? -6.767  -127.910 31.115  1.00 93.56  ? 51  VAL   L CA  1 
ATOM   19925 C  C   . VAL   L  12 51  ? -5.456  -128.524 30.619  1.00 91.30  ? 51  VAL   L C   1 
ATOM   19926 O  O   . VAL   L  12 51  ? -5.262  -128.591 29.389  1.00 90.45  ? 51  VAL   L O   1 
ATOM   19927 C  CB  . VAL   L  12 51  ? -7.882  -128.961 31.280  1.00 95.84  ? 51  VAL   L CB  1 
ATOM   19928 C  CG1 . VAL   L  12 51  ? -9.061  -128.395 32.054  1.00 97.74  ? 51  VAL   L CG1 1 
ATOM   19929 C  CG2 . VAL   L  12 51  ? -8.339  -129.542 29.951  1.00 97.49  ? 51  VAL   L CG2 1 
ATOM   19930 N  N   . MET   L  12 52  ? -4.589  -128.924 31.551  1.00 92.34  ? 52  MET   L N   1 
ATOM   19931 C  CA  . MET   L  12 52  ? -3.189  -129.335 31.272  1.00 93.11  ? 52  MET   L CA  1 
ATOM   19932 C  C   . MET   L  12 52  ? -2.806  -130.511 32.175  1.00 91.63  ? 52  MET   L C   1 
ATOM   19933 O  O   . MET   L  12 52  ? -3.224  -130.527 33.350  1.00 93.35  ? 52  MET   L O   1 
ATOM   19934 C  CB  . MET   L  12 52  ? -2.233  -128.167 31.526  1.00 91.65  ? 52  MET   L CB  1 
ATOM   19935 C  CG  . MET   L  12 52  ? -0.765  -128.510 31.350  1.00 93.67  ? 52  MET   L CG  1 
ATOM   19936 S  SD  . MET   L  12 52  ? 0.270   -127.032 31.458  1.00 98.09  ? 52  MET   L SD  1 
ATOM   19937 C  CE  . MET   L  12 52  ? 1.910   -127.746 31.545  1.00 93.25  ? 52  MET   L CE  1 
ATOM   19938 N  N   . SER   L  12 53  ? -2.041  -131.457 31.628  1.00 92.44  ? 53  SER   L N   1 
ATOM   19939 C  CA  . SER   L  12 53  ? -1.378  -132.547 32.386  1.00 91.60  ? 53  SER   L CA  1 
ATOM   19940 C  C   . SER   L  12 53  ? 0.033   -132.767 31.835  1.00 93.28  ? 53  SER   L C   1 
ATOM   19941 O  O   . SER   L  12 53  ? 0.186   -132.827 30.597  1.00 90.75  ? 53  SER   L O   1 
ATOM   19942 C  CB  . SER   L  12 53  ? -2.183  -133.817 32.352  1.00 91.59  ? 53  SER   L CB  1 
ATOM   19943 O  OG  . SER   L  12 53  ? -1.680  -134.741 33.304  1.00 88.54  ? 53  SER   L OG  1 
ATOM   19944 N  N   . ALA   L  12 54  ? 1.015   -132.863 32.733  1.00 91.80  ? 54  ALA   L N   1 
ATOM   19945 C  CA  . ALA   L  12 54  ? 2.427   -133.191 32.432  1.00 90.77  ? 54  ALA   L CA  1 
ATOM   19946 C  C   . ALA   L  12 54  ? 2.794   -134.477 33.176  1.00 90.46  ? 54  ALA   L C   1 
ATOM   19947 O  O   . ALA   L  12 54  ? 3.132   -134.394 34.372  1.00 88.68  ? 54  ALA   L O   1 
ATOM   19948 C  CB  . ALA   L  12 54  ? 3.318   -132.038 32.819  1.00 89.70  ? 54  ALA   L CB  1 
ATOM   19949 N  N   . ASN   L  12 55  ? 2.709   -135.619 32.488  1.00 90.44  ? 55  ASN   L N   1 
ATOM   19950 C  CA  . ASN   L  12 55  ? 2.789   -136.971 33.101  1.00 90.80  ? 55  ASN   L CA  1 
ATOM   19951 C  C   . ASN   L  12 55  ? 4.181   -137.565 32.878  1.00 87.07  ? 55  ASN   L C   1 
ATOM   19952 O  O   . ASN   L  12 55  ? 4.689   -137.477 31.747  1.00 91.13  ? 55  ASN   L O   1 
ATOM   19953 C  CB  . ASN   L  12 55  ? 1.720   -137.914 32.546  1.00 96.74  ? 55  ASN   L CB  1 
ATOM   19954 C  CG  . ASN   L  12 55  ? 1.626   -139.206 33.329  1.00 99.55  ? 55  ASN   L CG  1 
ATOM   19955 O  OD1 . ASN   L  12 55  ? 1.781   -140.288 32.769  1.00 105.08 ? 55  ASN   L OD1 1 
ATOM   19956 N  ND2 . ASN   L  12 55  ? 1.392   -139.104 34.627  1.00 102.26 ? 55  ASN   L ND2 1 
ATOM   19957 N  N   . GLY   L  12 56  ? 4.743   -138.174 33.924  1.00 81.95  ? 56  GLY   L N   1 
ATOM   19958 C  CA  . GLY   L  12 56  ? 6.061   -138.834 33.904  1.00 82.43  ? 56  GLY   L CA  1 
ATOM   19959 C  C   . GLY   L  12 56  ? 6.746   -138.687 35.246  1.00 81.00  ? 56  GLY   L C   1 
ATOM   19960 O  O   . GLY   L  12 56  ? 6.367   -139.416 36.177  1.00 85.08  ? 56  GLY   L O   1 
ATOM   19961 N  N   . PHE   L  12 57  ? 7.691   -137.749 35.347  1.00 81.40  ? 57  PHE   L N   1 
ATOM   19962 C  CA  . PHE   L  12 57  ? 8.399   -137.378 36.599  1.00 82.98  ? 57  PHE   L CA  1 
ATOM   19963 C  C   . PHE   L  12 57  ? 7.642   -136.216 37.251  1.00 84.18  ? 57  PHE   L C   1 
ATOM   19964 O  O   . PHE   L  12 57  ? 7.755   -135.088 36.748  1.00 88.77  ? 57  PHE   L O   1 
ATOM   19965 C  CB  . PHE   L  12 57  ? 9.859   -137.029 36.295  1.00 82.93  ? 57  PHE   L CB  1 
ATOM   19966 C  CG  . PHE   L  12 57  ? 10.670  -136.597 37.491  1.00 84.72  ? 57  PHE   L CG  1 
ATOM   19967 C  CD1 . PHE   L  12 57  ? 10.571  -137.269 38.700  1.00 88.56  ? 57  PHE   L CD1 1 
ATOM   19968 C  CD2 . PHE   L  12 57  ? 11.546  -135.527 37.405  1.00 84.47  ? 57  PHE   L CD2 1 
ATOM   19969 C  CE1 . PHE   L  12 57  ? 11.322  -136.872 39.797  1.00 88.85  ? 57  PHE   L CE1 1 
ATOM   19970 C  CE2 . PHE   L  12 57  ? 12.295  -135.131 38.503  1.00 84.38  ? 57  PHE   L CE2 1 
ATOM   19971 C  CZ  . PHE   L  12 57  ? 12.183  -135.804 39.696  1.00 85.66  ? 57  PHE   L CZ  1 
ATOM   19972 N  N   . ALA   L  12 58  ? 6.892   -136.493 38.323  1.00 85.68  ? 58  ALA   L N   1 
ATOM   19973 C  CA  . ALA   L  12 58  ? 5.888   -135.585 38.934  1.00 89.17  ? 58  ALA   L CA  1 
ATOM   19974 C  C   . ALA   L  12 58  ? 6.516   -134.245 39.339  1.00 89.46  ? 58  ALA   L C   1 
ATOM   19975 O  O   . ALA   L  12 58  ? 5.810   -133.222 39.230  1.00 95.30  ? 58  ALA   L O   1 
ATOM   19976 C  CB  . ALA   L  12 58  ? 5.236   -136.250 40.121  1.00 90.12  ? 58  ALA   L CB  1 
ATOM   19977 N  N   . ALA   L  12 59  ? 7.772   -134.244 39.800  1.00 87.40  ? 59  ALA   L N   1 
ATOM   19978 C  CA  . ALA   L  12 59  ? 8.513   -133.023 40.200  1.00 86.43  ? 59  ALA   L CA  1 
ATOM   19979 C  C   . ALA   L  12 59  ? 8.641   -132.077 38.998  1.00 85.13  ? 59  ALA   L C   1 
ATOM   19980 O  O   . ALA   L  12 59  ? 8.414   -130.867 39.182  1.00 87.87  ? 59  ALA   L O   1 
ATOM   19981 C  CB  . ALA   L  12 59  ? 9.863   -133.383 40.768  1.00 86.13  ? 59  ALA   L CB  1 
ATOM   19982 N  N   . ASP   L  12 60  ? 8.983   -132.611 37.818  1.00 82.01  ? 60  ASP   L N   1 
ATOM   19983 C  CA  . ASP   L  12 60  ? 9.091   -131.847 36.546  1.00 80.15  ? 60  ASP   L CA  1 
ATOM   19984 C  C   . ASP   L  12 60  ? 7.682   -131.514 36.043  1.00 81.55  ? 60  ASP   L C   1 
ATOM   19985 O  O   . ASP   L  12 60  ? 7.506   -130.418 35.481  1.00 82.20  ? 60  ASP   L O   1 
ATOM   19986 C  CB  . ASP   L  12 60  ? 9.911   -132.603 35.493  1.00 80.73  ? 60  ASP   L CB  1 
ATOM   19987 C  CG  . ASP   L  12 60  ? 11.421  -132.517 35.689  1.00 78.02  ? 60  ASP   L CG  1 
ATOM   19988 O  OD1 . ASP   L  12 60  ? 11.858  -131.881 36.667  1.00 76.34  ? 60  ASP   L OD1 1 
ATOM   19989 O  OD2 . ASP   L  12 60  ? 12.154  -133.095 34.862  1.00 80.79  ? 60  ASP   L OD2 1 
ATOM   19990 N  N   . GLY   L  12 61  ? 6.722   -132.422 36.238  1.00 81.71  ? 61  GLY   L N   1 
ATOM   19991 C  CA  . GLY   L  12 61  ? 5.306   -132.218 35.876  1.00 86.54  ? 61  GLY   L CA  1 
ATOM   19992 C  C   . GLY   L  12 61  ? 4.702   -131.041 36.620  1.00 88.61  ? 61  GLY   L C   1 
ATOM   19993 O  O   . GLY   L  12 61  ? 4.061   -130.192 35.967  1.00 94.61  ? 61  GLY   L O   1 
ATOM   19994 N  N   . ASP   L  12 62  ? 4.910   -130.984 37.938  1.00 88.60  ? 62  ASP   L N   1 
ATOM   19995 C  CA  . ASP   L  12 62  ? 4.383   -129.910 38.822  1.00 89.97  ? 62  ASP   L CA  1 
ATOM   19996 C  C   . ASP   L  12 62  ? 5.075   -128.582 38.491  1.00 86.83  ? 62  ASP   L C   1 
ATOM   19997 O  O   . ASP   L  12 62  ? 4.366   -127.563 38.420  1.00 85.00  ? 62  ASP   L O   1 
ATOM   19998 C  CB  . ASP   L  12 62  ? 4.539   -130.290 40.296  1.00 95.41  ? 62  ASP   L CB  1 
ATOM   19999 C  CG  . ASP   L  12 62  ? 3.554   -131.354 40.757  1.00 99.60  ? 62  ASP   L CG  1 
ATOM   20000 O  OD1 . ASP   L  12 62  ? 2.607   -131.654 39.997  1.00 104.22 ? 62  ASP   L OD1 1 
ATOM   20001 O  OD2 . ASP   L  12 62  ? 3.742   -131.880 41.871  1.00 108.57 ? 62  ASP   L OD2 1 
ATOM   20002 N  N   . ALA   L  12 63  ? 6.396   -128.604 38.283  1.00 85.99  ? 63  ALA   L N   1 
ATOM   20003 C  CA  . ALA   L  12 63  ? 7.226   -127.426 37.933  1.00 86.89  ? 63  ALA   L CA  1 
ATOM   20004 C  C   . ALA   L  12 63  ? 6.703   -126.780 36.645  1.00 87.96  ? 63  ALA   L C   1 
ATOM   20005 O  O   . ALA   L  12 63  ? 6.580   -125.545 36.622  1.00 92.85  ? 63  ALA   L O   1 
ATOM   20006 C  CB  . ALA   L  12 63  ? 8.676   -127.826 37.794  1.00 85.58  ? 63  ALA   L CB  1 
ATOM   20007 N  N   . LEU   L  12 64  ? 6.406   -127.582 35.618  1.00 86.39  ? 64  LEU   L N   1 
ATOM   20008 C  CA  . LEU   L  12 64  ? 5.948   -127.091 34.291  1.00 86.84  ? 64  LEU   L CA  1 
ATOM   20009 C  C   . LEU   L  12 64  ? 4.546   -126.491 34.426  1.00 87.71  ? 64  LEU   L C   1 
ATOM   20010 O  O   . LEU   L  12 64  ? 4.356   -125.361 33.949  1.00 91.35  ? 64  LEU   L O   1 
ATOM   20011 C  CB  . LEU   L  12 64  ? 5.953   -128.235 33.275  1.00 87.40  ? 64  LEU   L CB  1 
ATOM   20012 C  CG  . LEU   L  12 64  ? 5.639   -127.824 31.837  1.00 89.99  ? 64  LEU   L CG  1 
ATOM   20013 C  CD1 . LEU   L  12 64  ? 6.761   -126.978 31.256  1.00 92.11  ? 64  LEU   L CD1 1 
ATOM   20014 C  CD2 . LEU   L  12 64  ? 5.383   -129.043 30.964  1.00 92.02  ? 64  LEU   L CD2 1 
ATOM   20015 N  N   . VAL   L  12 65  ? 3.605   -127.220 35.036  1.00 85.72  ? 65  VAL   L N   1 
ATOM   20016 C  CA  . VAL   L  12 65  ? 2.204   -126.751 35.270  1.00 89.94  ? 65  VAL   L CA  1 
ATOM   20017 C  C   . VAL   L  12 65  ? 2.252   -125.420 36.031  1.00 90.41  ? 65  VAL   L C   1 
ATOM   20018 O  O   . VAL   L  12 65  ? 1.471   -124.509 35.687  1.00 95.80  ? 65  VAL   L O   1 
ATOM   20019 C  CB  . VAL   L  12 65  ? 1.362   -127.797 36.029  1.00 90.23  ? 65  VAL   L CB  1 
ATOM   20020 C  CG1 . VAL   L  12 65  ? 0.064   -127.208 36.569  1.00 92.53  ? 65  VAL   L CG1 1 
ATOM   20021 C  CG2 . VAL   L  12 65  ? 1.067   -129.011 35.166  1.00 91.29  ? 65  VAL   L CG2 1 
ATOM   20022 N  N   . LYS   L  12 66  ? 3.133   -125.327 37.030  1.00 87.84  ? 66  LYS   L N   1 
ATOM   20023 C  CA  . LYS   L  12 66  ? 3.324   -124.129 37.888  1.00 88.21  ? 66  LYS   L CA  1 
ATOM   20024 C  C   . LYS   L  12 66  ? 3.776   -122.943 37.026  1.00 87.22  ? 66  LYS   L C   1 
ATOM   20025 O  O   . LYS   L  12 66  ? 3.216   -121.843 37.205  1.00 88.94  ? 66  LYS   L O   1 
ATOM   20026 C  CB  . LYS   L  12 66  ? 4.342   -124.439 38.988  1.00 88.99  ? 66  LYS   L CB  1 
ATOM   20027 C  CG  . LYS   L  12 66  ? 4.354   -123.462 40.151  1.00 91.86  ? 66  LYS   L CG  1 
ATOM   20028 C  CD  . LYS   L  12 66  ? 4.832   -124.087 41.440  1.00 94.88  ? 66  LYS   L CD  1 
ATOM   20029 C  CE  . LYS   L  12 66  ? 4.753   -123.140 42.617  1.00 97.28  ? 66  LYS   L CE  1 
ATOM   20030 N  NZ  . LYS   L  12 66  ? 5.153   -123.805 43.879  1.00 98.65  ? 66  LYS   L NZ  1 
ATOM   20031 N  N   . ARG   L  12 67  ? 4.740   -123.163 36.125  1.00 83.37  ? 67  ARG   L N   1 
ATOM   20032 C  CA  . ARG   L  12 67  ? 5.322   -122.109 35.250  1.00 83.97  ? 67  ARG   L CA  1 
ATOM   20033 C  C   . ARG   L  12 67  ? 4.287   -121.660 34.212  1.00 87.97  ? 67  ARG   L C   1 
ATOM   20034 O  O   . ARG   L  12 67  ? 4.188   -120.437 33.985  1.00 87.97  ? 67  ARG   L O   1 
ATOM   20035 C  CB  . ARG   L  12 67  ? 6.602   -122.589 34.559  1.00 82.97  ? 67  ARG   L CB  1 
ATOM   20036 C  CG  . ARG   L  12 67  ? 7.818   -122.634 35.472  1.00 83.71  ? 67  ARG   L CG  1 
ATOM   20037 C  CD  . ARG   L  12 67  ? 9.039   -122.022 34.812  1.00 88.80  ? 67  ARG   L CD  1 
ATOM   20038 N  NE  . ARG   L  12 67  ? 9.557   -122.839 33.721  1.00 90.98  ? 67  ARG   L NE  1 
ATOM   20039 C  CZ  . ARG   L  12 67  ? 10.339  -122.400 32.734  1.00 95.54  ? 67  ARG   L CZ  1 
ATOM   20040 N  NH1 . ARG   L  12 67  ? 10.697  -121.126 32.667  1.00 97.74  ? 67  ARG   L NH1 1 
ATOM   20041 N  NH2 . ARG   L  12 67  ? 10.756  -123.241 31.804  1.00 96.20  ? 67  ARG   L NH2 1 
ATOM   20042 N  N   . PHE   L  12 68  ? 3.554   -122.596 33.598  1.00 87.35  ? 68  PHE   L N   1 
ATOM   20043 C  CA  . PHE   L  12 68  ? 2.522   -122.283 32.575  1.00 89.23  ? 68  PHE   L CA  1 
ATOM   20044 C  C   . PHE   L  12 68  ? 1.367   -121.509 33.222  1.00 92.14  ? 68  PHE   L C   1 
ATOM   20045 O  O   . PHE   L  12 68  ? 0.898   -120.539 32.603  1.00 98.97  ? 68  PHE   L O   1 
ATOM   20046 C  CB  . PHE   L  12 68  ? 1.980   -123.528 31.873  1.00 89.21  ? 68  PHE   L CB  1 
ATOM   20047 C  CG  . PHE   L  12 68  ? 0.837   -123.211 30.941  1.00 90.87  ? 68  PHE   L CG  1 
ATOM   20048 C  CD1 . PHE   L  12 68  ? 1.063   -122.527 29.755  1.00 91.42  ? 68  PHE   L CD1 1 
ATOM   20049 C  CD2 . PHE   L  12 68  ? -0.468  -123.538 31.276  1.00 91.79  ? 68  PHE   L CD2 1 
ATOM   20050 C  CE1 . PHE   L  12 68  ? 0.011   -122.208 28.908  1.00 93.14  ? 68  PHE   L CE1 1 
ATOM   20051 C  CE2 . PHE   L  12 68  ? -1.518  -123.220 30.428  1.00 94.78  ? 68  PHE   L CE2 1 
ATOM   20052 C  CZ  . PHE   L  12 68  ? -1.276  -122.555 29.247  1.00 95.21  ? 68  PHE   L CZ  1 
ATOM   20053 N  N   . LYS   L  12 69  ? 0.913   -121.929 34.408  1.00 91.05  ? 69  LYS   L N   1 
ATOM   20054 C  CA  . LYS   L  12 69  ? -0.154  -121.226 35.175  1.00 93.30  ? 69  LYS   L CA  1 
ATOM   20055 C  C   . LYS   L  12 69  ? 0.279   -119.780 35.432  1.00 93.57  ? 69  LYS   L C   1 
ATOM   20056 O  O   . LYS   L  12 69  ? -0.575  -118.871 35.350  1.00 95.63  ? 69  LYS   L O   1 
ATOM   20057 C  CB  . LYS   L  12 69  ? -0.437  -121.924 36.507  1.00 95.05  ? 69  LYS   L CB  1 
ATOM   20058 C  CG  . LYS   L  12 69  ? -1.472  -123.035 36.441  1.00 99.30  ? 69  LYS   L CG  1 
ATOM   20059 C  CD  . LYS   L  12 69  ? -1.945  -123.491 37.802  1.00 104.99 ? 69  LYS   L CD  1 
ATOM   20060 C  CE  . LYS   L  12 69  ? -3.093  -124.473 37.719  1.00 106.39 ? 69  LYS   L CE  1 
ATOM   20061 N  NZ  . LYS   L  12 69  ? -3.478  -124.989 39.054  1.00 108.08 ? 69  LYS   L NZ  1 
ATOM   20062 N  N   . ASN   L  12 70  ? 1.564   -119.594 35.741  1.00 93.22  ? 70  ASN   L N   1 
ATOM   20063 C  CA  . ASN   L  12 70  ? 2.190   -118.273 36.002  1.00 92.99  ? 70  ASN   L CA  1 
ATOM   20064 C  C   . ASN   L  12 70  ? 2.280   -117.483 34.691  1.00 94.31  ? 70  ASN   L C   1 
ATOM   20065 O  O   . ASN   L  12 70  ? 2.114   -116.253 34.741  1.00 97.08  ? 70  ASN   L O   1 
ATOM   20066 C  CB  . ASN   L  12 70  ? 3.557   -118.449 36.665  1.00 91.02  ? 70  ASN   L CB  1 
ATOM   20067 C  CG  . ASN   L  12 70  ? 4.078   -117.183 37.303  1.00 90.71  ? 70  ASN   L CG  1 
ATOM   20068 O  OD1 . ASN   L  12 70  ? 5.260   -116.877 37.185  1.00 94.00  ? 70  ASN   L OD1 1 
ATOM   20069 N  ND2 . ASN   L  12 70  ? 3.210   -116.448 37.976  1.00 93.30  ? 70  ASN   L ND2 1 
ATOM   20070 N  N   . SER   L  12 71  ? 2.529   -118.167 33.567  1.00 93.99  ? 71  SER   L N   1 
ATOM   20071 C  CA  . SER   L  12 71  ? 2.605   -117.576 32.203  1.00 92.09  ? 71  SER   L CA  1 
ATOM   20072 C  C   . SER   L  12 71  ? 1.245   -116.991 31.796  1.00 91.69  ? 71  SER   L C   1 
ATOM   20073 O  O   . SER   L  12 71  ? 1.239   -115.901 31.192  1.00 87.43  ? 71  SER   L O   1 
ATOM   20074 C  CB  . SER   L  12 71  ? 3.084   -118.585 31.193  1.00 93.95  ? 71  SER   L CB  1 
ATOM   20075 O  OG  . SER   L  12 71  ? 3.354   -117.959 29.947  1.00 97.90  ? 71  SER   L OG  1 
ATOM   20076 N  N   . VAL   L  12 72  ? 0.148   -117.695 32.106  1.00 90.47  ? 72  VAL   L N   1 
ATOM   20077 C  CA  . VAL   L  12 72  ? -1.256  -117.254 31.837  1.00 93.92  ? 72  VAL   L CA  1 
ATOM   20078 C  C   . VAL   L  12 72  ? -1.525  -115.961 32.619  1.00 95.92  ? 72  VAL   L C   1 
ATOM   20079 O  O   . VAL   L  12 72  ? -2.176  -115.054 32.061  1.00 97.42  ? 72  VAL   L O   1 
ATOM   20080 C  CB  . VAL   L  12 72  ? -2.286  -118.344 32.201  1.00 93.95  ? 72  VAL   L CB  1 
ATOM   20081 C  CG1 . VAL   L  12 72  ? -3.716  -117.824 32.135  1.00 94.29  ? 72  VAL   L CG1 1 
ATOM   20082 C  CG2 . VAL   L  12 72  ? -2.139  -119.581 31.327  1.00 95.05  ? 72  VAL   L CG2 1 
ATOM   20083 N  N   . LYS   L  12 73  ? -1.053  -115.894 33.868  1.00 94.66  ? 73  LYS   L N   1 
ATOM   20084 C  CA  . LYS   L  12 73  ? -1.245  -114.735 34.781  1.00 96.42  ? 73  LYS   L CA  1 
ATOM   20085 C  C   . LYS   L  12 73  ? -0.597  -113.483 34.178  1.00 95.15  ? 73  LYS   L C   1 
ATOM   20086 O  O   . LYS   L  12 73  ? -1.262  -112.427 34.148  1.00 96.30  ? 73  LYS   L O   1 
ATOM   20087 C  CB  . LYS   L  12 73  ? -0.643  -115.029 36.158  1.00 96.31  ? 73  LYS   L CB  1 
ATOM   20088 C  CG  . LYS   L  12 73  ? -1.101  -114.089 37.263  1.00 100.21 ? 73  LYS   L CG  1 
ATOM   20089 C  CD  . LYS   L  12 73  ? -0.367  -114.279 38.567  1.00 103.03 ? 73  LYS   L CD  1 
ATOM   20090 C  CE  . LYS   L  12 73  ? -0.887  -113.364 39.654  1.00 108.40 ? 73  LYS   L CE  1 
ATOM   20091 N  NZ  . LYS   L  12 73  ? 0.028   -113.320 40.818  1.00 111.33 ? 73  LYS   L NZ  1 
ATOM   20092 N  N   . TRP   L  12 74  ? 0.656   -113.599 33.729  1.00 93.20  ? 74  TRP   L N   1 
ATOM   20093 C  CA  . TRP   L  12 74  ? 1.465   -112.468 33.201  1.00 94.25  ? 74  TRP   L CA  1 
ATOM   20094 C  C   . TRP   L  12 74  ? 0.987   -112.072 31.802  1.00 96.47  ? 74  TRP   L C   1 
ATOM   20095 O  O   . TRP   L  12 74  ? 1.087   -110.879 31.473  1.00 101.32 ? 74  TRP   L O   1 
ATOM   20096 C  CB  . TRP   L  12 74  ? 2.961   -112.801 33.225  1.00 95.44  ? 74  TRP   L CB  1 
ATOM   20097 C  CG  . TRP   L  12 74  ? 3.565   -112.598 34.579  1.00 98.09  ? 74  TRP   L CG  1 
ATOM   20098 C  CD1 . TRP   L  12 74  ? 3.838   -113.550 35.518  1.00 99.19  ? 74  TRP   L CD1 1 
ATOM   20099 C  CD2 . TRP   L  12 74  ? 3.924   -111.339 35.173  1.00 99.48  ? 74  TRP   L CD2 1 
ATOM   20100 N  NE1 . TRP   L  12 74  ? 4.360   -112.974 36.644  1.00 100.81 ? 74  TRP   L NE1 1 
ATOM   20101 C  CE2 . TRP   L  12 74  ? 4.425   -111.618 36.462  1.00 99.83  ? 74  TRP   L CE2 1 
ATOM   20102 C  CE3 . TRP   L  12 74  ? 3.878   -110.011 34.739  1.00 102.44 ? 74  TRP   L CE3 1 
ATOM   20103 C  CZ2 . TRP   L  12 74  ? 4.878   -110.616 37.317  1.00 101.12 ? 74  TRP   L CZ2 1 
ATOM   20104 C  CZ3 . TRP   L  12 74  ? 4.326   -109.021 35.584  1.00 105.35 ? 74  TRP   L CZ3 1 
ATOM   20105 C  CH2 . TRP   L  12 74  ? 4.820   -109.322 36.855  1.00 104.78 ? 74  TRP   L CH2 1 
ATOM   20106 N  N   . TYR   L  12 75  ? 0.490   -113.025 31.011  1.00 93.72  ? 75  TYR   L N   1 
ATOM   20107 C  CA  . TYR   L  12 75  ? -0.127  -112.755 29.686  1.00 92.57  ? 75  TYR   L CA  1 
ATOM   20108 C  C   . TYR   L  12 75  ? -1.257  -111.737 29.863  1.00 95.87  ? 75  TYR   L C   1 
ATOM   20109 O  O   . TYR   L  12 75  ? -1.341  -110.807 29.041  1.00 97.92  ? 75  TYR   L O   1 
ATOM   20110 C  CB  . TYR   L  12 75  ? -0.638  -114.039 29.030  1.00 91.40  ? 75  TYR   L CB  1 
ATOM   20111 C  CG  . TYR   L  12 75  ? -1.190  -113.844 27.642  1.00 92.53  ? 75  TYR   L CG  1 
ATOM   20112 C  CD1 . TYR   L  12 75  ? -0.349  -113.746 26.544  1.00 92.98  ? 75  TYR   L CD1 1 
ATOM   20113 C  CD2 . TYR   L  12 75  ? -2.555  -113.751 27.424  1.00 94.46  ? 75  TYR   L CD2 1 
ATOM   20114 C  CE1 . TYR   L  12 75  ? -0.849  -113.564 25.265  1.00 95.75  ? 75  TYR   L CE1 1 
ATOM   20115 C  CE2 . TYR   L  12 75  ? -3.072  -113.575 26.152  1.00 96.28  ? 75  TYR   L CE2 1 
ATOM   20116 C  CZ  . TYR   L  12 75  ? -2.217  -113.480 25.069  1.00 97.44  ? 75  TYR   L CZ  1 
ATOM   20117 O  OH  . TYR   L  12 75  ? -2.732  -113.304 23.819  1.00 102.09 ? 75  TYR   L OH  1 
ATOM   20118 N  N   . HIS   L  12 76  ? -2.079  -111.902 30.907  1.00 98.49  ? 76  HIS   L N   1 
ATOM   20119 C  CA  . HIS   L  12 76  ? -3.186  -110.973 31.272  1.00 102.29 ? 76  HIS   L CA  1 
ATOM   20120 C  C   . HIS   L  12 76  ? -2.622  -109.599 31.650  1.00 104.20 ? 76  HIS   L C   1 
ATOM   20121 O  O   . HIS   L  12 76  ? -3.155  -108.590 31.147  1.00 106.90 ? 76  HIS   L O   1 
ATOM   20122 C  CB  . HIS   L  12 76  ? -4.043  -111.533 32.416  1.00 104.55 ? 76  HIS   L CB  1 
ATOM   20123 C  CG  . HIS   L  12 76  ? -4.810  -112.763 32.066  1.00 107.68 ? 76  HIS   L CG  1 
ATOM   20124 N  ND1 . HIS   L  12 76  ? -5.380  -112.948 30.822  1.00 109.63 ? 76  HIS   L ND1 1 
ATOM   20125 C  CD2 . HIS   L  12 76  ? -5.127  -113.852 32.798  1.00 107.44 ? 76  HIS   L CD2 1 
ATOM   20126 C  CE1 . HIS   L  12 76  ? -6.001  -114.108 30.796  1.00 108.96 ? 76  HIS   L CE1 1 
ATOM   20127 N  NE2 . HIS   L  12 76  ? -5.862  -114.684 31.998  1.00 108.49 ? 76  HIS   L NE2 1 
ATOM   20128 N  N   . PHE   L  12 77  ? -1.598  -109.569 32.511  1.00 104.15 ? 77  PHE   L N   1 
ATOM   20129 C  CA  . PHE   L  12 77  ? -0.941  -108.331 33.016  1.00 104.91 ? 77  PHE   L CA  1 
ATOM   20130 C  C   . PHE   L  12 77  ? -0.343  -107.525 31.854  1.00 104.81 ? 77  PHE   L C   1 
ATOM   20131 O  O   . PHE   L  12 77  ? -0.418  -106.281 31.911  1.00 106.16 ? 77  PHE   L O   1 
ATOM   20132 C  CB  . PHE   L  12 77  ? 0.150   -108.650 34.046  1.00 104.07 ? 77  PHE   L CB  1 
ATOM   20133 C  CG  . PHE   L  12 77  ? -0.327  -108.999 35.436  1.00 105.74 ? 77  PHE   L CG  1 
ATOM   20134 C  CD1 . PHE   L  12 77  ? -1.503  -108.471 35.952  1.00 107.14 ? 77  PHE   L CD1 1 
ATOM   20135 C  CD2 . PHE   L  12 77  ? 0.429   -109.832 36.250  1.00 104.27 ? 77  PHE   L CD2 1 
ATOM   20136 C  CE1 . PHE   L  12 77  ? -1.924  -108.793 37.234  1.00 108.83 ? 77  PHE   L CE1 1 
ATOM   20137 C  CE2 . PHE   L  12 77  ? 0.008   -110.150 37.533  1.00 105.06 ? 77  PHE   L CE2 1 
ATOM   20138 C  CZ  . PHE   L  12 77  ? -1.169  -109.631 38.022  1.00 107.67 ? 77  PHE   L CZ  1 
ATOM   20139 N  N   . ASP   L  12 78  ? 0.218   -108.201 30.842  1.00 99.95  ? 78  ASP   L N   1 
ATOM   20140 C  CA  . ASP   L  12 78  ? 1.032   -107.571 29.764  1.00 101.31 ? 78  ASP   L CA  1 
ATOM   20141 C  C   . ASP   L  12 78  ? 0.190   -107.267 28.516  1.00 102.84 ? 78  ASP   L C   1 
ATOM   20142 O  O   . ASP   L  12 78  ? 0.674   -106.475 27.680  1.00 106.66 ? 78  ASP   L O   1 
ATOM   20143 C  CB  . ASP   L  12 78  ? 2.226   -108.450 29.383  1.00 101.88 ? 78  ASP   L CB  1 
ATOM   20144 C  CG  . ASP   L  12 78  ? 3.266   -108.585 30.481  1.00 105.60 ? 78  ASP   L CG  1 
ATOM   20145 O  OD1 . ASP   L  12 78  ? 3.586   -107.558 31.111  1.00 106.22 ? 78  ASP   L OD1 1 
ATOM   20146 O  OD2 . ASP   L  12 78  ? 3.750   -109.717 30.696  1.00 105.39 ? 78  ASP   L OD2 1 
ATOM   20147 N  N   . HIS   L  12 79  ? -0.999  -107.863 28.369  1.00 98.92  ? 79  HIS   L N   1 
ATOM   20148 C  CA  . HIS   L  12 79  ? -1.847  -107.726 27.152  1.00 101.72 ? 79  HIS   L CA  1 
ATOM   20149 C  C   . HIS   L  12 79  ? -3.316  -107.518 27.537  1.00 100.64 ? 79  HIS   L C   1 
ATOM   20150 O  O   . HIS   L  12 79  ? -4.176  -108.228 26.992  1.00 103.04 ? 79  HIS   L O   1 
ATOM   20151 C  CB  . HIS   L  12 79  ? -1.621  -108.923 26.220  1.00 104.08 ? 79  HIS   L CB  1 
ATOM   20152 C  CG  . HIS   L  12 79  ? -0.181  -109.143 25.903  1.00 108.38 ? 79  HIS   L CG  1 
ATOM   20153 N  ND1 . HIS   L  12 79  ? 0.622   -109.961 26.674  1.00 110.75 ? 79  HIS   L ND1 1 
ATOM   20154 C  CD2 . HIS   L  12 79  ? 0.613   -108.634 24.934  1.00 108.51 ? 79  HIS   L CD2 1 
ATOM   20155 C  CE1 . HIS   L  12 79  ? 1.845   -109.962 26.185  1.00 111.74 ? 79  HIS   L CE1 1 
ATOM   20156 N  NE2 . HIS   L  12 79  ? 1.867   -109.151 25.118  1.00 108.91 ? 79  HIS   L NE2 1 
ATOM   20157 N  N   . ASN   L  12 80  ? -3.572  -106.565 28.438  1.00 103.62 ? 80  ASN   L N   1 
ATOM   20158 C  CA  . ASN   L  12 80  ? -4.909  -105.983 28.741  1.00 107.51 ? 80  ASN   L CA  1 
ATOM   20159 C  C   . ASN   L  12 80  ? -5.945  -107.096 28.946  1.00 107.73 ? 80  ASN   L C   1 
ATOM   20160 O  O   . ASN   L  12 80  ? -7.026  -107.015 28.327  1.00 105.78 ? 80  ASN   L O   1 
ATOM   20161 C  CB  . ASN   L  12 80  ? -5.331  -104.993 27.648  1.00 111.63 ? 80  ASN   L CB  1 
ATOM   20162 C  CG  . ASN   L  12 80  ? -6.446  -104.057 28.069  1.00 113.96 ? 80  ASN   L CG  1 
ATOM   20163 O  OD1 . ASN   L  12 80  ? -7.402  -103.853 27.325  1.00 114.01 ? 80  ASN   L OD1 1 
ATOM   20164 N  ND2 . ASN   L  12 80  ? -6.336  -103.476 29.254  1.00 113.44 ? 80  ASN   L ND2 1 
ATOM   20165 N  N   . ASP   L  12 81  ? -5.619  -108.087 29.786  1.00 108.42 ? 81  ASP   L N   1 
ATOM   20166 C  CA  . ASP   L  12 81  ? -6.521  -109.187 30.235  1.00 110.31 ? 81  ASP   L CA  1 
ATOM   20167 C  C   . ASP   L  12 81  ? -6.999  -110.042 29.051  1.00 109.20 ? 81  ASP   L C   1 
ATOM   20168 O  O   . ASP   L  12 81  ? -7.995  -110.774 29.234  1.00 108.79 ? 81  ASP   L O   1 
ATOM   20169 C  CB  . ASP   L  12 81  ? -7.723  -108.637 31.014  1.00 114.33 ? 81  ASP   L CB  1 
ATOM   20170 C  CG  . ASP   L  12 81  ? -7.536  -108.605 32.522  1.00 117.10 ? 81  ASP   L CG  1 
ATOM   20171 O  OD1 . ASP   L  12 81  ? -6.870  -109.515 33.052  1.00 114.38 ? 81  ASP   L OD1 1 
ATOM   20172 O  OD2 . ASP   L  12 81  ? -8.072  -107.675 33.156  1.00 124.18 ? 81  ASP   L OD2 1 
ATOM   20173 N  N   . LYS   L  12 82  ? -6.318  -109.985 27.900  1.00 110.72 ? 82  LYS   L N   1 
ATOM   20174 C  CA  . LYS   L  12 82  ? -6.690  -110.762 26.685  1.00 110.81 ? 82  LYS   L CA  1 
ATOM   20175 C  C   . LYS   L  12 82  ? -6.712  -112.255 27.033  1.00 108.07 ? 82  LYS   L C   1 
ATOM   20176 O  O   . LYS   L  12 82  ? -5.834  -112.699 27.805  1.00 106.31 ? 82  LYS   L O   1 
ATOM   20177 C  CB  . LYS   L  12 82  ? -5.716  -110.502 25.530  1.00 112.20 ? 82  LYS   L CB  1 
ATOM   20178 C  CG  . LYS   L  12 82  ? -5.938  -111.375 24.300  1.00 111.99 ? 82  LYS   L CG  1 
ATOM   20179 C  CD  . LYS   L  12 82  ? -5.070  -111.012 23.117  1.00 113.03 ? 82  LYS   L CD  1 
ATOM   20180 C  CE  . LYS   L  12 82  ? -5.282  -111.940 21.940  1.00 112.72 ? 82  LYS   L CE  1 
ATOM   20181 N  NZ  . LYS   L  12 82  ? -4.617  -111.436 20.716  1.00 114.02 ? 82  LYS   L NZ  1 
ATOM   20182 N  N   . LYS   L  12 83  ? -7.677  -112.996 26.482  1.00 108.86 ? 83  LYS   L N   1 
ATOM   20183 C  CA  . LYS   L  12 83  ? -7.793  -114.465 26.676  1.00 104.95 ? 83  LYS   L CA  1 
ATOM   20184 C  C   . LYS   L  12 83  ? -6.669  -115.155 25.896  1.00 102.15 ? 83  LYS   L C   1 
ATOM   20185 O  O   . LYS   L  12 83  ? -6.478  -114.821 24.709  1.00 102.78 ? 83  LYS   L O   1 
ATOM   20186 C  CB  . LYS   L  12 83  ? -9.159  -114.985 26.221  1.00 107.97 ? 83  LYS   L CB  1 
ATOM   20187 C  CG  . LYS   L  12 83  ? -9.489  -116.384 26.723  1.00 108.28 ? 83  LYS   L CG  1 
ATOM   20188 C  CD  . LYS   L  12 83  ? -10.576 -117.089 25.945  1.00 112.14 ? 83  LYS   L CD  1 
ATOM   20189 C  CE  . LYS   L  12 83  ? -10.881 -118.461 26.507  1.00 110.95 ? 83  LYS   L CE  1 
ATOM   20190 N  NZ  . LYS   L  12 83  ? -11.865 -119.192 25.677  1.00 114.20 ? 83  LYS   L NZ  1 
ATOM   20191 N  N   . LEU   L  12 84  ? -5.954  -116.075 26.549  1.00 98.93  ? 84  LEU   L N   1 
ATOM   20192 C  CA  . LEU   L  12 84  ? -4.899  -116.910 25.920  1.00 96.84  ? 84  LEU   L CA  1 
ATOM   20193 C  C   . LEU   L  12 84  ? -5.572  -118.066 25.174  1.00 94.95  ? 84  LEU   L C   1 
ATOM   20194 O  O   . LEU   L  12 84  ? -6.085  -118.984 25.844  1.00 92.52  ? 84  LEU   L O   1 
ATOM   20195 C  CB  . LEU   L  12 84  ? -3.935  -117.419 26.997  1.00 93.76  ? 84  LEU   L CB  1 
ATOM   20196 C  CG  . LEU   L  12 84  ? -2.745  -118.231 26.487  1.00 93.68  ? 84  LEU   L CG  1 
ATOM   20197 C  CD1 . LEU   L  12 84  ? -1.829  -117.391 25.610  1.00 93.86  ? 84  LEU   L CD1 1 
ATOM   20198 C  CD2 . LEU   L  12 84  ? -1.961  -118.820 27.646  1.00 95.41  ? 84  LEU   L CD2 1 
ATOM   20199 N  N   . SER   L  12 85  ? -5.586  -117.998 23.839  1.00 97.02  ? 85  SER   L N   1 
ATOM   20200 C  CA  . SER   L  12 85  ? -6.130  -119.045 22.937  1.00 98.91  ? 85  SER   L CA  1 
ATOM   20201 C  C   . SER   L  12 85  ? -5.277  -120.313 23.065  1.00 97.25  ? 85  SER   L C   1 
ATOM   20202 O  O   . SER   L  12 85  ? -4.069  -120.182 23.350  1.00 96.43  ? 85  SER   L O   1 
ATOM   20203 C  CB  . SER   L  12 85  ? -6.186  -118.553 21.514  1.00 100.23 ? 85  SER   L CB  1 
ATOM   20204 O  OG  . SER   L  12 85  ? -4.927  -118.034 21.107  1.00 101.83 ? 85  SER   L OG  1 
ATOM   20205 N  N   . ILE   L  12 86  ? -5.890  -121.485 22.865  1.00 97.72  ? 86  ILE   L N   1 
ATOM   20206 C  CA  . ILE   L  12 86  ? -5.251  -122.824 23.050  1.00 95.93  ? 86  ILE   L CA  1 
ATOM   20207 C  C   . ILE   L  12 86  ? -4.001  -122.922 22.164  1.00 93.35  ? 86  ILE   L C   1 
ATOM   20208 O  O   . ILE   L  12 86  ? -2.990  -123.473 22.638  1.00 89.27  ? 86  ILE   L O   1 
ATOM   20209 C  CB  . ILE   L  12 86  ? -6.258  -123.964 22.777  1.00 98.38  ? 86  ILE   L CB  1 
ATOM   20210 C  CG1 . ILE   L  12 86  ? -5.758  -125.305 23.322  1.00 98.04  ? 86  ILE   L CG1 1 
ATOM   20211 C  CG2 . ILE   L  12 86  ? -6.622  -124.055 21.300  1.00 99.47  ? 86  ILE   L CG2 1 
ATOM   20212 C  CD1 . ILE   L  12 86  ? -5.923  -125.461 24.816  1.00 99.26  ? 86  ILE   L CD1 1 
ATOM   20213 N  N   . ASN   L  12 87  ? -4.066  -122.400 20.933  1.00 96.10  ? 87  ASN   L N   1 
ATOM   20214 C  CA  . ASN   L  12 87  ? -2.956  -122.441 19.942  1.00 95.70  ? 87  ASN   L CA  1 
ATOM   20215 C  C   . ASN   L  12 87  ? -1.770  -121.619 20.462  1.00 95.91  ? 87  ASN   L C   1 
ATOM   20216 O  O   . ASN   L  12 87  ? -0.618  -122.040 20.227  1.00 88.93  ? 87  ASN   L O   1 
ATOM   20217 C  CB  . ASN   L  12 87  ? -3.399  -121.936 18.567  1.00 97.43  ? 87  ASN   L CB  1 
ATOM   20218 C  CG  . ASN   L  12 87  ? -3.646  -120.442 18.547  1.00 98.31  ? 87  ASN   L CG  1 
ATOM   20219 O  OD1 . ASN   L  12 87  ? -4.606  -119.962 19.145  1.00 95.75  ? 87  ASN   L OD1 1 
ATOM   20220 N  ND2 . ASN   L  12 87  ? -2.777  -119.698 17.882  1.00 98.48  ? 87  ASN   L ND2 1 
ATOM   20221 N  N   . SER   L  12 88  ? -2.047  -120.490 21.128  1.00 95.84  ? 88  SER   L N   1 
ATOM   20222 C  CA  . SER   L  12 88  ? -1.036  -119.581 21.732  1.00 94.24  ? 88  SER   L CA  1 
ATOM   20223 C  C   . SER   L  12 88  ? -0.442  -120.231 22.986  1.00 91.36  ? 88  SER   L C   1 
ATOM   20224 O  O   . SER   L  12 88  ? 0.787   -120.130 23.176  1.00 89.26  ? 88  SER   L O   1 
ATOM   20225 C  CB  . SER   L  12 88  ? -1.619  -118.223 22.047  1.00 94.09  ? 88  SER   L CB  1 
ATOM   20226 O  OG  . SER   L  12 88  ? -2.060  -117.565 20.868  1.00 94.93  ? 88  SER   L OG  1 
ATOM   20227 N  N   . ALA   L  12 89  ? -1.286  -120.868 23.804  1.00 90.44  ? 89  ALA   L N   1 
ATOM   20228 C  CA  . ALA   L  12 89  ? -0.878  -121.667 24.982  1.00 89.91  ? 89  ALA   L CA  1 
ATOM   20229 C  C   . ALA   L  12 89  ? 0.115   -122.747 24.538  1.00 90.03  ? 89  ALA   L C   1 
ATOM   20230 O  O   . ALA   L  12 89  ? 1.180   -122.854 25.169  1.00 91.63  ? 89  ALA   L O   1 
ATOM   20231 C  CB  . ALA   L  12 89  ? -2.085  -122.275 25.652  1.00 89.22  ? 89  ALA   L CB  1 
ATOM   20232 N  N   . ALA   L  12 90  ? -0.221  -123.495 23.480  1.00 92.55  ? 90  ALA   L N   1 
ATOM   20233 C  CA  . ALA   L  12 90  ? 0.611   -124.579 22.906  1.00 93.47  ? 90  ALA   L CA  1 
ATOM   20234 C  C   . ALA   L  12 90  ? 2.000   -124.034 22.555  1.00 91.86  ? 90  ALA   L C   1 
ATOM   20235 O  O   . ALA   L  12 90  ? 3.001   -124.609 23.017  1.00 88.36  ? 90  ALA   L O   1 
ATOM   20236 C  CB  . ALA   L  12 90  ? -0.062  -125.184 21.696  1.00 97.70  ? 90  ALA   L CB  1 
ATOM   20237 N  N   . ARG   L  12 91  ? 2.053   -122.952 21.776  1.00 93.04  ? 91  ARG   L N   1 
ATOM   20238 C  CA  . ARG   L  12 91  ? 3.321   -122.329 21.312  1.00 91.72  ? 91  ARG   L CA  1 
ATOM   20239 C  C   . ARG   L  12 91  ? 4.144   -121.858 22.518  1.00 92.58  ? 91  ARG   L C   1 
ATOM   20240 O  O   . ARG   L  12 91  ? 5.385   -121.946 22.453  1.00 92.60  ? 91  ARG   L O   1 
ATOM   20241 C  CB  . ARG   L  12 91  ? 3.039   -121.159 20.366  1.00 92.49  ? 91  ARG   L CB  1 
ATOM   20242 C  CG  . ARG   L  12 91  ? 4.293   -120.454 19.868  1.00 91.32  ? 91  ARG   L CG  1 
ATOM   20243 C  CD  . ARG   L  12 91  ? 5.239   -121.381 19.129  1.00 92.04  ? 91  ARG   L CD  1 
ATOM   20244 N  NE  . ARG   L  12 91  ? 4.741   -121.708 17.801  1.00 94.59  ? 91  ARG   L NE  1 
ATOM   20245 C  CZ  . ARG   L  12 91  ? 4.900   -120.951 16.721  1.00 98.34  ? 91  ARG   L CZ  1 
ATOM   20246 N  NH1 . ARG   L  12 91  ? 5.550   -119.800 16.795  1.00 100.89 ? 91  ARG   L NH1 1 
ATOM   20247 N  NH2 . ARG   L  12 91  ? 4.405   -121.347 15.561  1.00 102.32 ? 91  ARG   L NH2 1 
ATOM   20248 N  N   . ASN   L  12 92  ? 3.478   -121.363 23.565  1.00 92.54  ? 92  ASN   L N   1 
ATOM   20249 C  CA  . ASN   L  12 92  ? 4.128   -120.876 24.812  1.00 94.14  ? 92  ASN   L CA  1 
ATOM   20250 C  C   . ASN   L  12 92  ? 4.784   -122.060 25.534  1.00 93.67  ? 92  ASN   L C   1 
ATOM   20251 O  O   . ASN   L  12 92  ? 5.960   -121.922 25.933  1.00 92.98  ? 92  ASN   L O   1 
ATOM   20252 C  CB  . ASN   L  12 92  ? 3.138   -120.128 25.711  1.00 95.34  ? 92  ASN   L CB  1 
ATOM   20253 C  CG  . ASN   L  12 92  ? 3.725   -119.723 27.047  1.00 97.31  ? 92  ASN   L CG  1 
ATOM   20254 O  OD1 . ASN   L  12 92  ? 3.112   -119.951 28.087  1.00 100.52 ? 92  ASN   L OD1 1 
ATOM   20255 N  ND2 . ASN   L  12 92  ? 4.908   -119.129 27.034  1.00 99.85  ? 92  ASN   L ND2 1 
ATOM   20256 N  N   . ILE   L  12 93  ? 4.058   -123.177 25.677  1.00 91.47  ? 93  ILE   L N   1 
ATOM   20257 C  CA  . ILE   L  12 93  ? 4.525   -124.407 26.389  1.00 86.18  ? 93  ILE   L CA  1 
ATOM   20258 C  C   . ILE   L  12 93  ? 5.739   -124.981 25.646  1.00 84.22  ? 93  ILE   L C   1 
ATOM   20259 O  O   . ILE   L  12 93  ? 6.641   -125.492 26.333  1.00 85.64  ? 93  ILE   L O   1 
ATOM   20260 C  CB  . ILE   L  12 93  ? 3.380   -125.431 26.564  1.00 84.83  ? 93  ILE   L CB  1 
ATOM   20261 C  CG1 . ILE   L  12 93  ? 2.308   -124.904 27.524  1.00 84.07  ? 93  ILE   L CG1 1 
ATOM   20262 C  CG2 . ILE   L  12 93  ? 3.915   -126.785 27.020  1.00 84.06  ? 93  ILE   L CG2 1 
ATOM   20263 C  CD1 . ILE   L  12 93  ? 1.042   -125.732 27.572  1.00 84.19  ? 93  ILE   L CD1 1 
ATOM   20264 N  N   . GLN   L  12 94  ? 5.782   -124.887 24.310  1.00 83.49  ? 94  GLN   L N   1 
ATOM   20265 C  CA  . GLN   L  12 94  ? 6.947   -125.344 23.502  1.00 83.83  ? 94  GLN   L CA  1 
ATOM   20266 C  C   . GLN   L  12 94  ? 8.210   -124.648 24.013  1.00 82.11  ? 94  GLN   L C   1 
ATOM   20267 O  O   . GLN   L  12 94  ? 9.229   -125.335 24.206  1.00 77.02  ? 94  GLN   L O   1 
ATOM   20268 C  CB  . GLN   L  12 94  ? 6.782   -125.054 22.008  1.00 88.39  ? 94  GLN   L CB  1 
ATOM   20269 C  CG  . GLN   L  12 94  ? 8.062   -125.297 21.216  1.00 90.70  ? 94  GLN   L CG  1 
ATOM   20270 C  CD  . GLN   L  12 94  ? 7.850   -125.261 19.723  1.00 96.62  ? 94  GLN   L CD  1 
ATOM   20271 O  OE1 . GLN   L  12 94  ? 7.738   -124.195 19.122  1.00 100.65 ? 94  GLN   L OE1 1 
ATOM   20272 N  NE2 . GLN   L  12 94  ? 7.808   -126.433 19.108  1.00 97.62  ? 94  GLN   L NE2 1 
ATOM   20273 N  N   . HIS   L  12 95  ? 8.137   -123.331 24.211  1.00 80.92  ? 95  HIS   L N   1 
ATOM   20274 C  CA  . HIS   L  12 95  ? 9.272   -122.481 24.659  1.00 80.24  ? 95  HIS   L CA  1 
ATOM   20275 C  C   . HIS   L  12 95  ? 9.622   -122.780 26.123  1.00 81.28  ? 95  HIS   L C   1 
ATOM   20276 O  O   . HIS   L  12 95  ? 10.820  -122.681 26.466  1.00 78.09  ? 95  HIS   L O   1 
ATOM   20277 C  CB  . HIS   L  12 95  ? 8.966   -120.999 24.419  1.00 80.88  ? 95  HIS   L CB  1 
ATOM   20278 C  CG  . HIS   L  12 95  ? 9.207   -120.576 23.011  1.00 82.55  ? 95  HIS   L CG  1 
ATOM   20279 N  ND1 . HIS   L  12 95  ? 8.254   -120.727 22.022  1.00 84.21  ? 95  HIS   L ND1 1 
ATOM   20280 C  CD2 . HIS   L  12 95  ? 10.289  -120.027 22.420  1.00 83.46  ? 95  HIS   L CD2 1 
ATOM   20281 C  CE1 . HIS   L  12 95  ? 8.737   -120.284 20.879  1.00 86.44  ? 95  HIS   L CE1 1 
ATOM   20282 N  NE2 . HIS   L  12 95  ? 9.984   -119.846 21.098  1.00 85.33  ? 95  HIS   L NE2 1 
ATOM   20283 N  N   . LEU   L  12 96  ? 8.632   -123.129 26.952  1.00 81.62  ? 96  LEU   L N   1 
ATOM   20284 C  CA  . LEU   L  12 96  ? 8.864   -123.577 28.353  1.00 83.47  ? 96  LEU   L CA  1 
ATOM   20285 C  C   . LEU   L  12 96  ? 9.707   -124.857 28.333  1.00 84.49  ? 96  LEU   L C   1 
ATOM   20286 O  O   . LEU   L  12 96  ? 10.727  -124.905 29.052  1.00 86.42  ? 96  LEU   L O   1 
ATOM   20287 C  CB  . LEU   L  12 96  ? 7.527   -123.818 29.064  1.00 81.79  ? 96  LEU   L CB  1 
ATOM   20288 C  CG  . LEU   L  12 96  ? 6.706   -122.573 29.396  1.00 82.38  ? 96  LEU   L CG  1 
ATOM   20289 C  CD1 . LEU   L  12 96  ? 5.403   -122.956 30.084  1.00 84.37  ? 96  LEU   L CD1 1 
ATOM   20290 C  CD2 . LEU   L  12 96  ? 7.495   -121.610 30.266  1.00 80.90  ? 96  LEU   L CD2 1 
ATOM   20291 N  N   . LEU   L  12 97  ? 9.300   -125.845 27.529  1.00 87.05  ? 97  LEU   L N   1 
ATOM   20292 C  CA  . LEU   L  12 97  ? 9.956   -127.175 27.442  1.00 85.34  ? 97  LEU   L CA  1 
ATOM   20293 C  C   . LEU   L  12 97  ? 11.343  -127.021 26.807  1.00 82.44  ? 97  LEU   L C   1 
ATOM   20294 O  O   . LEU   L  12 97  ? 12.322  -127.458 27.447  1.00 79.86  ? 97  LEU   L O   1 
ATOM   20295 C  CB  . LEU   L  12 97  ? 9.065   -128.136 26.646  1.00 87.60  ? 97  LEU   L CB  1 
ATOM   20296 C  CG  . LEU   L  12 97  ? 7.822   -128.641 27.382  1.00 92.00  ? 97  LEU   L CG  1 
ATOM   20297 C  CD1 . LEU   L  12 97  ? 6.836   -129.272 26.411  1.00 94.19  ? 97  LEU   L CD1 1 
ATOM   20298 C  CD2 . LEU   L  12 97  ? 8.195   -129.636 28.473  1.00 94.41  ? 97  LEU   L CD2 1 
ATOM   20299 N  N   . TYR   L  12 98  ? 11.431  -126.409 25.617  1.00 82.65  ? 98  TYR   L N   1 
ATOM   20300 C  CA  . TYR   L  12 98  ? 12.684  -126.331 24.816  1.00 82.07  ? 98  TYR   L CA  1 
ATOM   20301 C  C   . TYR   L  12 98  ? 13.717  -125.448 25.525  1.00 83.58  ? 98  TYR   L C   1 
ATOM   20302 O  O   . TYR   L  12 98  ? 14.922  -125.607 25.246  1.00 83.96  ? 98  TYR   L O   1 
ATOM   20303 C  CB  . TYR   L  12 98  ? 12.459  -125.828 23.387  1.00 81.89  ? 98  TYR   L CB  1 
ATOM   20304 C  CG  . TYR   L  12 98  ? 13.594  -126.217 22.474  1.00 80.77  ? 98  TYR   L CG  1 
ATOM   20305 C  CD1 . TYR   L  12 98  ? 13.590  -127.442 21.826  1.00 82.31  ? 98  TYR   L CD1 1 
ATOM   20306 C  CD2 . TYR   L  12 98  ? 14.714  -125.413 22.326  1.00 78.96  ? 98  TYR   L CD2 1 
ATOM   20307 C  CE1 . TYR   L  12 98  ? 14.642  -127.840 21.018  1.00 82.35  ? 98  TYR   L CE1 1 
ATOM   20308 C  CE2 . TYR   L  12 98  ? 15.776  -125.795 21.522  1.00 79.87  ? 98  TYR   L CE2 1 
ATOM   20309 C  CZ  . TYR   L  12 98  ? 15.740  -127.014 20.865  1.00 80.39  ? 98  TYR   L CZ  1 
ATOM   20310 O  OH  . TYR   L  12 98  ? 16.770  -127.415 20.069  1.00 78.48  ? 98  TYR   L OH  1 
ATOM   20311 N  N   . GLY   L  12 99  ? 13.263  -124.548 26.403  1.00 84.38  ? 99  GLY   L N   1 
ATOM   20312 C  CA  . GLY   L  12 99  ? 14.137  -123.736 27.274  1.00 84.10  ? 99  GLY   L CA  1 
ATOM   20313 C  C   . GLY   L  12 99  ? 15.039  -124.604 28.136  1.00 82.84  ? 99  GLY   L C   1 
ATOM   20314 O  O   . GLY   L  12 99  ? 16.128  -124.133 28.509  1.00 82.13  ? 99  GLY   L O   1 
ATOM   20315 N  N   . LYS   L  12 100 ? 14.602  -125.829 28.443  1.00 84.45  ? 100 LYS   L N   1 
ATOM   20316 C  CA  . LYS   L  12 100 ? 15.395  -126.853 29.174  1.00 85.10  ? 100 LYS   L CA  1 
ATOM   20317 C  C   . LYS   L  12 100 ? 15.722  -128.013 28.225  1.00 85.84  ? 100 LYS   L C   1 
ATOM   20318 O  O   . LYS   L  12 100 ? 15.600  -129.174 28.649  1.00 88.06  ? 100 LYS   L O   1 
ATOM   20319 C  CB  . LYS   L  12 100 ? 14.618  -127.312 30.412  1.00 85.44  ? 100 LYS   L CB  1 
ATOM   20320 C  CG  . LYS   L  12 100 ? 14.764  -126.404 31.625  1.00 85.01  ? 100 LYS   L CG  1 
ATOM   20321 C  CD  . LYS   L  12 100 ? 13.897  -126.805 32.801  1.00 87.60  ? 100 LYS   L CD  1 
ATOM   20322 C  CE  . LYS   L  12 100 ? 14.186  -128.189 33.350  1.00 87.13  ? 100 LYS   L CE  1 
ATOM   20323 N  NZ  . LYS   L  12 100 ? 15.584  -128.332 33.824  1.00 88.15  ? 100 LYS   L NZ  1 
ATOM   20324 N  N   . ARG   L  12 101 ? 16.141  -127.710 26.992  1.00 83.04  ? 101 ARG   L N   1 
ATOM   20325 C  CA  . ARG   L  12 101 ? 16.496  -128.726 25.966  1.00 81.52  ? 101 ARG   L CA  1 
ATOM   20326 C  C   . ARG   L  12 101 ? 17.618  -129.621 26.499  1.00 83.53  ? 101 ARG   L C   1 
ATOM   20327 O  O   . ARG   L  12 101 ? 17.541  -130.837 26.271  1.00 83.62  ? 101 ARG   L O   1 
ATOM   20328 C  CB  . ARG   L  12 101 ? 16.915  -128.064 24.650  1.00 83.78  ? 101 ARG   L CB  1 
ATOM   20329 C  CG  . ARG   L  12 101 ? 17.594  -129.001 23.660  1.00 85.06  ? 101 ARG   L CG  1 
ATOM   20330 C  CD  . ARG   L  12 101 ? 16.718  -130.172 23.253  1.00 84.75  ? 101 ARG   L CD  1 
ATOM   20331 N  NE  . ARG   L  12 101 ? 17.295  -130.885 22.122  1.00 84.83  ? 101 ARG   L NE  1 
ATOM   20332 C  CZ  . ARG   L  12 101 ? 18.309  -131.743 22.192  1.00 84.24  ? 101 ARG   L CZ  1 
ATOM   20333 N  NH1 . ARG   L  12 101 ? 18.879  -132.021 23.353  1.00 85.97  ? 101 ARG   L NH1 1 
ATOM   20334 N  NH2 . ARG   L  12 101 ? 18.756  -132.324 21.092  1.00 84.38  ? 101 ARG   L NH2 1 
ATOM   20335 N  N   . PHE   L  12 102 ? 18.611  -129.046 27.184  1.00 80.83  ? 102 PHE   L N   1 
ATOM   20336 C  CA  . PHE   L  12 102 ? 19.841  -129.757 27.626  1.00 82.73  ? 102 PHE   L CA  1 
ATOM   20337 C  C   . PHE   L  12 102 ? 19.757  -130.153 29.110  1.00 85.31  ? 102 PHE   L C   1 
ATOM   20338 O  O   . PHE   L  12 102 ? 20.787  -130.598 29.661  1.00 87.94  ? 102 PHE   L O   1 
ATOM   20339 C  CB  . PHE   L  12 102 ? 21.069  -128.910 27.294  1.00 81.00  ? 102 PHE   L CB  1 
ATOM   20340 C  CG  . PHE   L  12 102 ? 21.171  -128.587 25.827  1.00 81.90  ? 102 PHE   L CG  1 
ATOM   20341 C  CD1 . PHE   L  12 102 ? 21.440  -129.583 24.902  1.00 82.70  ? 102 PHE   L CD1 1 
ATOM   20342 C  CD2 . PHE   L  12 102 ? 20.959  -127.300 25.366  1.00 82.72  ? 102 PHE   L CD2 1 
ATOM   20343 C  CE1 . PHE   L  12 102 ? 21.519  -129.294 23.548  1.00 83.90  ? 102 PHE   L CE1 1 
ATOM   20344 C  CE2 . PHE   L  12 102 ? 21.039  -127.012 24.012  1.00 84.24  ? 102 PHE   L CE2 1 
ATOM   20345 C  CZ  . PHE   L  12 102 ? 21.319  -128.009 23.106  1.00 83.87  ? 102 PHE   L CZ  1 
ATOM   20346 N  N   . PHE   L  12 103 ? 18.579  -130.020 29.729  1.00 84.74  ? 103 PHE   L N   1 
ATOM   20347 C  CA  . PHE   L  12 103 ? 18.234  -130.644 31.035  1.00 82.69  ? 103 PHE   L CA  1 
ATOM   20348 C  C   . PHE   L  12 103 ? 16.722  -130.847 31.089  1.00 81.27  ? 103 PHE   L C   1 
ATOM   20349 O  O   . PHE   L  12 103 ? 16.038  -130.251 31.918  1.00 81.07  ? 103 PHE   L O   1 
ATOM   20350 C  CB  . PHE   L  12 103 ? 18.771  -129.804 32.198  1.00 82.37  ? 103 PHE   L CB  1 
ATOM   20351 C  CG  . PHE   L  12 103 ? 18.705  -130.457 33.559  1.00 82.47  ? 103 PHE   L CG  1 
ATOM   20352 C  CD1 . PHE   L  12 103 ? 18.517  -131.825 33.702  1.00 83.17  ? 103 PHE   L CD1 1 
ATOM   20353 C  CD2 . PHE   L  12 103 ? 18.864  -129.700 34.709  1.00 81.90  ? 103 PHE   L CD2 1 
ATOM   20354 C  CE1 . PHE   L  12 103 ? 18.467  -132.412 34.959  1.00 82.07  ? 103 PHE   L CE1 1 
ATOM   20355 C  CE2 . PHE   L  12 103 ? 18.817  -130.289 35.964  1.00 79.98  ? 103 PHE   L CE2 1 
ATOM   20356 C  CZ  . PHE   L  12 103 ? 18.620  -131.643 36.088  1.00 79.21  ? 103 PHE   L CZ  1 
ATOM   20357 N  N   . PRO   L  12 104 ? 16.169  -131.720 30.216  1.00 81.06  ? 104 PRO   L N   1 
ATOM   20358 C  CA  . PRO   L  12 104 ? 14.737  -131.721 29.911  1.00 82.76  ? 104 PRO   L CA  1 
ATOM   20359 C  C   . PRO   L  12 104 ? 13.825  -131.974 31.118  1.00 80.75  ? 104 PRO   L C   1 
ATOM   20360 O  O   . PRO   L  12 104 ? 14.261  -132.601 32.063  1.00 82.03  ? 104 PRO   L O   1 
ATOM   20361 C  CB  . PRO   L  12 104 ? 14.572  -132.873 28.905  1.00 83.31  ? 104 PRO   L CB  1 
ATOM   20362 C  CG  . PRO   L  12 104 ? 15.962  -133.092 28.343  1.00 83.20  ? 104 PRO   L CG  1 
ATOM   20363 C  CD  . PRO   L  12 104 ? 16.897  -132.771 29.488  1.00 80.43  ? 104 PRO   L CD  1 
ATOM   20364 N  N   . TYR   L  12 105 ? 12.593  -131.464 31.055  1.00 82.44  ? 105 TYR   L N   1 
ATOM   20365 C  CA  . TYR   L  12 105 ? 11.459  -131.926 31.892  1.00 85.88  ? 105 TYR   L CA  1 
ATOM   20366 C  C   . TYR   L  12 105 ? 11.074  -133.327 31.414  1.00 89.12  ? 105 TYR   L C   1 
ATOM   20367 O  O   . TYR   L  12 105 ? 10.624  -133.438 30.256  1.00 94.17  ? 105 TYR   L O   1 
ATOM   20368 C  CB  . TYR   L  12 105 ? 10.236  -131.017 31.760  1.00 88.99  ? 105 TYR   L CB  1 
ATOM   20369 C  CG  . TYR   L  12 105 ? 10.361  -129.623 32.325  1.00 90.17  ? 105 TYR   L CG  1 
ATOM   20370 C  CD1 . TYR   L  12 105 ? 10.482  -129.404 33.688  1.00 89.26  ? 105 TYR   L CD1 1 
ATOM   20371 C  CD2 . TYR   L  12 105 ? 10.292  -128.513 31.497  1.00 93.56  ? 105 TYR   L CD2 1 
ATOM   20372 C  CE1 . TYR   L  12 105 ? 10.568  -128.123 34.210  1.00 90.08  ? 105 TYR   L CE1 1 
ATOM   20373 C  CE2 . TYR   L  12 105 ? 10.376  -127.226 32.003  1.00 92.64  ? 105 TYR   L CE2 1 
ATOM   20374 C  CZ  . TYR   L  12 105 ? 10.512  -127.029 33.365  1.00 90.55  ? 105 TYR   L CZ  1 
ATOM   20375 O  OH  . TYR   L  12 105 ? 10.601  -125.764 33.870  1.00 90.76  ? 105 TYR   L OH  1 
ATOM   20376 N  N   . TYR   L  12 106 ? 11.253  -134.355 32.250  1.00 89.81  ? 106 TYR   L N   1 
ATOM   20377 C  CA  . TYR   L  12 106 ? 10.886  -135.762 31.932  1.00 90.43  ? 106 TYR   L CA  1 
ATOM   20378 C  C   . TYR   L  12 106 ? 9.373   -135.916 32.095  1.00 85.18  ? 106 TYR   L C   1 
ATOM   20379 O  O   . TYR   L  12 106 ? 8.924   -136.591 33.040  1.00 85.64  ? 106 TYR   L O   1 
ATOM   20380 C  CB  . TYR   L  12 106 ? 11.658  -136.762 32.798  1.00 93.01  ? 106 TYR   L CB  1 
ATOM   20381 C  CG  . TYR   L  12 106 ? 12.740  -137.510 32.062  1.00 102.15 ? 106 TYR   L CG  1 
ATOM   20382 C  CD1 . TYR   L  12 106 ? 13.792  -136.834 31.464  1.00 104.11 ? 106 TYR   L CD1 1 
ATOM   20383 C  CD2 . TYR   L  12 106 ? 12.712  -138.892 31.959  1.00 105.25 ? 106 TYR   L CD2 1 
ATOM   20384 C  CE1 . TYR   L  12 106 ? 14.792  -137.510 30.784  1.00 110.83 ? 106 TYR   L CE1 1 
ATOM   20385 C  CE2 . TYR   L  12 106 ? 13.704  -139.583 31.283  1.00 113.86 ? 106 TYR   L CE2 1 
ATOM   20386 C  CZ  . TYR   L  12 106 ? 14.748  -138.890 30.694  1.00 114.08 ? 106 TYR   L CZ  1 
ATOM   20387 O  OH  . TYR   L  12 106 ? 15.731  -139.560 30.024  1.00 126.37 ? 106 TYR   L OH  1 
ATOM   20388 N  N   . VAL   L  12 107 ? 8.610   -135.284 31.202  1.00 83.17  ? 107 VAL   L N   1 
ATOM   20389 C  CA  . VAL   L  12 107 ? 7.121   -135.340 31.209  1.00 85.49  ? 107 VAL   L CA  1 
ATOM   20390 C  C   . VAL   L  12 107 ? 6.599   -135.378 29.774  1.00 86.47  ? 107 VAL   L C   1 
ATOM   20391 O  O   . VAL   L  12 107 ? 7.236   -134.799 28.870  1.00 82.56  ? 107 VAL   L O   1 
ATOM   20392 C  CB  . VAL   L  12 107 ? 6.502   -134.160 31.977  1.00 85.73  ? 107 VAL   L CB  1 
ATOM   20393 C  CG1 . VAL   L  12 107 ? 6.877   -134.193 33.446  1.00 86.20  ? 107 VAL   L CG1 1 
ATOM   20394 C  CG2 . VAL   L  12 107 ? 6.867   -132.822 31.350  1.00 87.34  ? 107 VAL   L CG2 1 
ATOM   20395 N  N   . HIS   L  12 108 ? 5.460   -136.046 29.614  1.00 91.30  ? 108 HIS   L N   1 
ATOM   20396 C  CA  . HIS   L  12 108 ? 4.602   -136.041 28.407  1.00 97.29  ? 108 HIS   L CA  1 
ATOM   20397 C  C   . HIS   L  12 108 ? 3.475   -135.046 28.675  1.00 92.36  ? 108 HIS   L C   1 
ATOM   20398 O  O   . HIS   L  12 108 ? 2.668   -135.316 29.586  1.00 89.25  ? 108 HIS   L O   1 
ATOM   20399 C  CB  . HIS   L  12 108 ? 4.063   -137.454 28.150  1.00 107.53 ? 108 HIS   L CB  1 
ATOM   20400 C  CG  . HIS   L  12 108 ? 4.425   -138.035 26.827  1.00 124.96 ? 108 HIS   L CG  1 
ATOM   20401 N  ND1 . HIS   L  12 108 ? 4.088   -139.333 26.494  1.00 136.01 ? 108 HIS   L ND1 1 
ATOM   20402 C  CD2 . HIS   L  12 108 ? 5.101   -137.531 25.770  1.00 129.32 ? 108 HIS   L CD2 1 
ATOM   20403 C  CE1 . HIS   L  12 108 ? 4.522   -139.599 25.280  1.00 140.49 ? 108 HIS   L CE1 1 
ATOM   20404 N  NE2 . HIS   L  12 108 ? 5.151   -138.510 24.813  1.00 140.67 ? 108 HIS   L NE2 1 
ATOM   20405 N  N   . THR   L  12 109 ? 3.436   -133.929 27.949  1.00 90.59  ? 109 THR   L N   1 
ATOM   20406 C  CA  . THR   L  12 109 ? 2.469   -132.836 28.214  1.00 88.89  ? 109 THR   L CA  1 
ATOM   20407 C  C   . THR   L  12 109 ? 1.325   -132.916 27.201  1.00 88.20  ? 109 THR   L C   1 
ATOM   20408 O  O   . THR   L  12 109 ? 1.606   -133.008 25.990  1.00 86.84  ? 109 THR   L O   1 
ATOM   20409 C  CB  . THR   L  12 109 ? 3.158   -131.470 28.228  1.00 88.11  ? 109 THR   L CB  1 
ATOM   20410 O  OG1 . THR   L  12 109 ? 4.433   -131.631 28.854  1.00 83.52  ? 109 THR   L OG1 1 
ATOM   20411 C  CG2 . THR   L  12 109 ? 2.328   -130.433 28.951  1.00 88.30  ? 109 THR   L CG2 1 
ATOM   20412 N  N   . ILE   L  12 110 ? 0.087   -132.920 27.701  1.00 89.45  ? 110 ILE   L N   1 
ATOM   20413 C  CA  . ILE   L  12 110 ? -1.158  -132.790 26.892  1.00 93.93  ? 110 ILE   L CA  1 
ATOM   20414 C  C   . ILE   L  12 110 ? -1.976  -131.637 27.479  1.00 93.84  ? 110 ILE   L C   1 
ATOM   20415 O  O   . ILE   L  12 110 ? -2.116  -131.590 28.718  1.00 95.34  ? 110 ILE   L O   1 
ATOM   20416 C  CB  . ILE   L  12 110 ? -1.962  -134.106 26.870  1.00 94.68  ? 110 ILE   L CB  1 
ATOM   20417 C  CG1 . ILE   L  12 110 ? -1.098  -135.300 26.452  1.00 97.41  ? 110 ILE   L CG1 1 
ATOM   20418 C  CG2 . ILE   L  12 110 ? -3.191  -133.963 25.983  1.00 97.03  ? 110 ILE   L CG2 1 
ATOM   20419 C  CD1 . ILE   L  12 110 ? -1.754  -136.650 26.660  1.00 99.06  ? 110 ILE   L CD1 1 
ATOM   20420 N  N   . ILE   L  12 111 ? -2.474  -130.743 26.621  1.00 94.59  ? 111 ILE   L N   1 
ATOM   20421 C  CA  . ILE   L  12 111 ? -3.453  -129.678 26.992  1.00 94.40  ? 111 ILE   L CA  1 
ATOM   20422 C  C   . ILE   L  12 111 ? -4.711  -129.867 26.141  1.00 93.59  ? 111 ILE   L C   1 
ATOM   20423 O  O   . ILE   L  12 111 ? -4.587  -130.338 24.991  1.00 91.93  ? 111 ILE   L O   1 
ATOM   20424 C  CB  . ILE   L  12 111 ? -2.857  -128.264 26.831  1.00 94.22  ? 111 ILE   L CB  1 
ATOM   20425 C  CG1 . ILE   L  12 111 ? -2.480  -127.954 25.380  1.00 95.98  ? 111 ILE   L CG1 1 
ATOM   20426 C  CG2 . ILE   L  12 111 ? -1.680  -128.078 27.772  1.00 93.81  ? 111 ILE   L CG2 1 
ATOM   20427 C  CD1 . ILE   L  12 111 ? -2.269  -126.488 25.098  1.00 96.86  ? 111 ILE   L CD1 1 
ATOM   20428 N  N   . ALA   L  12 112 ? -5.869  -129.512 26.699  1.00 92.29  ? 112 ALA   L N   1 
ATOM   20429 C  CA  . ALA   L  12 112 ? -7.187  -129.590 26.032  1.00 93.39  ? 112 ALA   L CA  1 
ATOM   20430 C  C   . ALA   L  12 112 ? -7.962  -128.296 26.284  1.00 93.63  ? 112 ALA   L C   1 
ATOM   20431 O  O   . ALA   L  12 112 ? -7.707  -127.633 27.308  1.00 89.67  ? 112 ALA   L O   1 
ATOM   20432 C  CB  . ALA   L  12 112 ? -7.949  -130.797 26.518  1.00 95.04  ? 112 ALA   L CB  1 
ATOM   20433 N  N   . GLY   L  12 113 ? -8.869  -127.965 25.363  1.00 96.00  ? 113 GLY   L N   1 
ATOM   20434 C  CA  . GLY   L  12 113 ? -9.725  -126.769 25.422  1.00 98.17  ? 113 GLY   L CA  1 
ATOM   20435 C  C   . GLY   L  12 113 ? -10.489 -126.580 24.126  1.00 100.99 ? 113 GLY   L C   1 
ATOM   20436 O  O   . GLY   L  12 113 ? -10.737 -127.587 23.435  1.00 100.75 ? 113 GLY   L O   1 
ATOM   20437 N  N   . LEU   L  12 114 ? -10.844 -125.333 23.811  1.00 101.76 ? 114 LEU   L N   1 
ATOM   20438 C  CA  . LEU   L  12 114 ? -11.547 -124.952 22.560  1.00 103.08 ? 114 LEU   L CA  1 
ATOM   20439 C  C   . LEU   L  12 114 ? -10.647 -124.009 21.757  1.00 104.36 ? 114 LEU   L C   1 
ATOM   20440 O  O   . LEU   L  12 114 ? -10.007 -123.132 22.375  1.00 101.67 ? 114 LEU   L O   1 
ATOM   20441 C  CB  . LEU   L  12 114 ? -12.878 -124.281 22.911  1.00 103.69 ? 114 LEU   L CB  1 
ATOM   20442 C  CG  . LEU   L  12 114 ? -13.794 -125.070 23.846  1.00 104.82 ? 114 LEU   L CG  1 
ATOM   20443 C  CD1 . LEU   L  12 114 ? -14.985 -124.224 24.264  1.00 104.63 ? 114 LEU   L CD1 1 
ATOM   20444 C  CD2 . LEU   L  12 114 ? -14.260 -126.365 23.196  1.00 106.41 ? 114 LEU   L CD2 1 
ATOM   20445 N  N   . ASP   L  12 115 ? -10.599 -124.193 20.434  1.00 107.38 ? 115 ASP   L N   1 
ATOM   20446 C  CA  . ASP   L  12 115 ? -9.923  -123.266 19.488  1.00 109.41 ? 115 ASP   L CA  1 
ATOM   20447 C  C   . ASP   L  12 115 ? -10.773 -121.992 19.387  1.00 110.94 ? 115 ASP   L C   1 
ATOM   20448 O  O   . ASP   L  12 115 ? -11.831 -121.925 20.051  1.00 111.67 ? 115 ASP   L O   1 
ATOM   20449 C  CB  . ASP   L  12 115 ? -9.656  -123.936 18.133  1.00 109.83 ? 115 ASP   L CB  1 
ATOM   20450 C  CG  . ASP   L  12 115 ? -10.891 -124.266 17.309  1.00 108.78 ? 115 ASP   L CG  1 
ATOM   20451 O  OD1 . ASP   L  12 115 ? -12.013 -124.018 17.791  1.00 112.08 ? 115 ASP   L OD1 1 
ATOM   20452 O  OD2 . ASP   L  12 115 ? -10.719 -124.771 16.186  1.00 110.30 ? 115 ASP   L OD2 1 
ATOM   20453 N  N   . GLU   L  12 116 ? -10.335 -121.021 18.584  1.00 111.53 ? 116 GLU   L N   1 
ATOM   20454 C  CA  . GLU   L  12 116 ? -10.984 -119.687 18.482  1.00 113.30 ? 116 GLU   L CA  1 
ATOM   20455 C  C   . GLU   L  12 116 ? -12.303 -119.787 17.702  1.00 111.52 ? 116 GLU   L C   1 
ATOM   20456 O  O   . GLU   L  12 116 ? -13.056 -118.802 17.733  1.00 113.38 ? 116 GLU   L O   1 
ATOM   20457 C  CB  . GLU   L  12 116 ? -10.005 -118.678 17.878  1.00 118.20 ? 116 GLU   L CB  1 
ATOM   20458 C  CG  . GLU   L  12 116 ? -9.045  -118.104 18.908  1.00 120.43 ? 116 GLU   L CG  1 
ATOM   20459 C  CD  . GLU   L  12 116 ? -7.771  -117.483 18.359  1.00 125.87 ? 116 GLU   L CD  1 
ATOM   20460 O  OE1 . GLU   L  12 116 ? -7.469  -116.328 18.731  1.00 127.28 ? 116 GLU   L OE1 1 
ATOM   20461 O  OE2 . GLU   L  12 116 ? -7.072  -118.162 17.580  1.00 127.04 ? 116 GLU   L OE2 1 
ATOM   20462 N  N   . ASP   L  12 117 ? -12.588 -120.925 17.055  1.00 113.71 ? 117 ASP   L N   1 
ATOM   20463 C  CA  . ASP   L  12 117 ? -13.864 -121.185 16.329  1.00 116.01 ? 117 ASP   L CA  1 
ATOM   20464 C  C   . ASP   L  12 117 ? -14.856 -121.935 17.232  1.00 111.37 ? 117 ASP   L C   1 
ATOM   20465 O  O   . ASP   L  12 117 ? -15.969 -122.232 16.752  1.00 106.85 ? 117 ASP   L O   1 
ATOM   20466 C  CB  . ASP   L  12 117 ? -13.615 -121.956 15.027  1.00 120.88 ? 117 ASP   L CB  1 
ATOM   20467 C  CG  . ASP   L  12 117 ? -12.922 -121.142 13.947  1.00 125.64 ? 117 ASP   L CG  1 
ATOM   20468 O  OD1 . ASP   L  12 117 ? -12.996 -119.897 14.007  1.00 129.45 ? 117 ASP   L OD1 1 
ATOM   20469 O  OD2 . ASP   L  12 117 ? -12.316 -121.760 13.050  1.00 131.49 ? 117 ASP   L OD2 1 
ATOM   20470 N  N   . GLY   L  12 118 ? -14.476 -122.230 18.482  1.00 111.39 ? 118 GLY   L N   1 
ATOM   20471 C  CA  . GLY   L  12 118 ? -15.346 -122.868 19.492  1.00 112.18 ? 118 GLY   L CA  1 
ATOM   20472 C  C   . GLY   L  12 118 ? -15.284 -124.389 19.463  1.00 110.09 ? 118 GLY   L C   1 
ATOM   20473 O  O   . GLY   L  12 118 ? -15.955 -125.012 20.313  1.00 107.03 ? 118 GLY   L O   1 
ATOM   20474 N  N   . LYS   L  12 119 ? -14.517 -124.976 18.534  1.00 110.15 ? 119 LYS   L N   1 
ATOM   20475 C  CA  . LYS   L  12 119 ? -14.412 -126.450 18.350  1.00 110.40 ? 119 LYS   L CA  1 
ATOM   20476 C  C   . LYS   L  12 119 ? -13.393 -127.026 19.337  1.00 107.09 ? 119 LYS   L C   1 
ATOM   20477 O  O   . LYS   L  12 119 ? -12.420 -126.322 19.664  1.00 109.44 ? 119 LYS   L O   1 
ATOM   20478 C  CB  . LYS   L  12 119 ? -14.033 -126.798 16.907  1.00 115.43 ? 119 LYS   L CB  1 
ATOM   20479 C  CG  . LYS   L  12 119 ? -15.146 -126.580 15.894  1.00 120.62 ? 119 LYS   L CG  1 
ATOM   20480 C  CD  . LYS   L  12 119 ? -14.875 -127.183 14.536  1.00 126.89 ? 119 LYS   L CD  1 
ATOM   20481 C  CE  . LYS   L  12 119 ? -16.081 -127.105 13.624  1.00 130.41 ? 119 LYS   L CE  1 
ATOM   20482 N  NZ  . LYS   L  12 119 ? -15.713 -126.641 12.267  1.00 134.62 ? 119 LYS   L NZ  1 
ATOM   20483 N  N   . GLY   L  12 120 ? -13.617 -128.269 19.779  1.00 106.30 ? 120 GLY   L N   1 
ATOM   20484 C  CA  . GLY   L  12 120 ? -12.746 -128.999 20.720  1.00 102.68 ? 120 GLY   L CA  1 
ATOM   20485 C  C   . GLY   L  12 120 ? -11.332 -129.139 20.185  1.00 97.91  ? 120 GLY   L C   1 
ATOM   20486 O  O   . GLY   L  12 120 ? -11.186 -129.397 18.975  1.00 95.36  ? 120 GLY   L O   1 
ATOM   20487 N  N   . ALA   L  12 121 ? -10.329 -128.985 21.056  1.00 96.30  ? 121 ALA   L N   1 
ATOM   20488 C  CA  . ALA   L  12 121 ? -8.889  -129.000 20.706  1.00 95.96  ? 121 ALA   L CA  1 
ATOM   20489 C  C   . ALA   L  12 121 ? -8.084  -129.784 21.750  1.00 94.87  ? 121 ALA   L C   1 
ATOM   20490 O  O   . ALA   L  12 121 ? -8.326  -129.603 22.958  1.00 93.44  ? 121 ALA   L O   1 
ATOM   20491 C  CB  . ALA   L  12 121 ? -8.382  -127.588 20.585  1.00 95.92  ? 121 ALA   L CB  1 
ATOM   20492 N  N   . VAL   L  12 122 ? -7.155  -130.618 21.275  1.00 96.60  ? 122 VAL   L N   1 
ATOM   20493 C  CA  . VAL   L  12 122 ? -6.155  -131.364 22.092  1.00 96.38  ? 122 VAL   L CA  1 
ATOM   20494 C  C   . VAL   L  12 122 ? -4.782  -131.147 21.443  1.00 93.45  ? 122 VAL   L C   1 
ATOM   20495 O  O   . VAL   L  12 122 ? -4.665  -131.366 20.222  1.00 92.45  ? 122 VAL   L O   1 
ATOM   20496 C  CB  . VAL   L  12 122 ? -6.524  -132.859 22.201  1.00 98.93  ? 122 VAL   L CB  1 
ATOM   20497 C  CG1 . VAL   L  12 122 ? -5.375  -133.711 22.722  1.00 98.69  ? 122 VAL   L CG1 1 
ATOM   20498 C  CG2 . VAL   L  12 122 ? -7.768  -133.069 23.054  1.00 103.07 ? 122 VAL   L CG2 1 
ATOM   20499 N  N   . TYR   L  12 123 ? -3.800  -130.697 22.228  1.00 92.78  ? 123 TYR   L N   1 
ATOM   20500 C  CA  . TYR   L  12 123 ? -2.384  -130.518 21.813  1.00 94.93  ? 123 TYR   L CA  1 
ATOM   20501 C  C   . TYR   L  12 123 ? -1.486  -131.402 22.683  1.00 90.06  ? 123 TYR   L C   1 
ATOM   20502 O  O   . TYR   L  12 123 ? -1.647  -131.375 23.917  1.00 84.70  ? 123 TYR   L O   1 
ATOM   20503 C  CB  . TYR   L  12 123 ? -1.947  -129.062 21.967  1.00 96.65  ? 123 TYR   L CB  1 
ATOM   20504 C  CG  . TYR   L  12 123 ? -2.451  -128.112 20.911  1.00 101.44 ? 123 TYR   L CG  1 
ATOM   20505 C  CD1 . TYR   L  12 123 ? -3.725  -127.570 20.979  1.00 102.32 ? 123 TYR   L CD1 1 
ATOM   20506 C  CD2 . TYR   L  12 123 ? -1.639  -127.724 19.857  1.00 102.76 ? 123 TYR   L CD2 1 
ATOM   20507 C  CE1 . TYR   L  12 123 ? -4.186  -126.686 20.017  1.00 102.74 ? 123 TYR   L CE1 1 
ATOM   20508 C  CE2 . TYR   L  12 123 ? -2.083  -126.839 18.887  1.00 102.29 ? 123 TYR   L CE2 1 
ATOM   20509 C  CZ  . TYR   L  12 123 ? -3.363  -126.318 18.966  1.00 103.29 ? 123 TYR   L CZ  1 
ATOM   20510 O  OH  . TYR   L  12 123 ? -3.803  -125.445 18.014  1.00 106.94 ? 123 TYR   L OH  1 
ATOM   20511 N  N   . SER   L  12 124 ? -0.559  -132.132 22.058  1.00 91.29  ? 124 SER   L N   1 
ATOM   20512 C  CA  . SER   L  12 124 ? 0.358   -133.090 22.728  1.00 91.17  ? 124 SER   L CA  1 
ATOM   20513 C  C   . SER   L  12 124 ? 1.810   -132.695 22.450  1.00 87.84  ? 124 SER   L C   1 
ATOM   20514 O  O   . SER   L  12 124 ? 2.113   -132.327 21.299  1.00 83.03  ? 124 SER   L O   1 
ATOM   20515 C  CB  . SER   L  12 124 ? 0.073   -134.509 22.307  1.00 95.62  ? 124 SER   L CB  1 
ATOM   20516 O  OG  . SER   L  12 124 ? 0.180   -134.657 20.898  1.00 102.25 ? 124 SER   L OG  1 
ATOM   20517 N  N   . PHE   L  12 125 ? 2.656   -132.775 23.481  1.00 86.26  ? 125 PHE   L N   1 
ATOM   20518 C  CA  . PHE   L  12 125 ? 4.087   -132.372 23.470  1.00 86.54  ? 125 PHE   L CA  1 
ATOM   20519 C  C   . PHE   L  12 125 ? 4.971   -133.543 23.896  1.00 87.42  ? 125 PHE   L C   1 
ATOM   20520 O  O   . PHE   L  12 125 ? 4.583   -134.288 24.817  1.00 89.64  ? 125 PHE   L O   1 
ATOM   20521 C  CB  . PHE   L  12 125 ? 4.352   -131.234 24.455  1.00 86.61  ? 125 PHE   L CB  1 
ATOM   20522 C  CG  . PHE   L  12 125 ? 3.433   -130.049 24.313  1.00 88.32  ? 125 PHE   L CG  1 
ATOM   20523 C  CD1 . PHE   L  12 125 ? 2.126   -130.104 24.773  1.00 89.61  ? 125 PHE   L CD1 1 
ATOM   20524 C  CD2 . PHE   L  12 125 ? 3.878   -128.877 23.726  1.00 88.49  ? 125 PHE   L CD2 1 
ATOM   20525 C  CE1 . PHE   L  12 125 ? 1.280   -129.015 24.641  1.00 88.05  ? 125 PHE   L CE1 1 
ATOM   20526 C  CE2 . PHE   L  12 125 ? 3.031   -127.788 23.594  1.00 88.45  ? 125 PHE   L CE2 1 
ATOM   20527 C  CZ  . PHE   L  12 125 ? 1.735   -127.859 24.054  1.00 88.04  ? 125 PHE   L CZ  1 
ATOM   20528 N  N   . ASP   L  12 126 ? 6.145   -133.663 23.271  1.00 86.37  ? 126 ASP   L N   1 
ATOM   20529 C  CA  . ASP   L  12 126 ? 7.236   -134.559 23.736  1.00 88.31  ? 126 ASP   L CA  1 
ATOM   20530 C  C   . ASP   L  12 126 ? 7.939   -133.845 24.892  1.00 84.84  ? 126 ASP   L C   1 
ATOM   20531 O  O   . ASP   L  12 126 ? 7.572   -132.729 25.256  1.00 85.18  ? 126 ASP   L O   1 
ATOM   20532 C  CB  . ASP   L  12 126 ? 8.128   -134.992 22.562  1.00 89.51  ? 126 ASP   L CB  1 
ATOM   20533 C  CG  . ASP   L  12 126 ? 9.147   -133.967 22.088  1.00 91.28  ? 126 ASP   L CG  1 
ATOM   20534 O  OD1 . ASP   L  12 126 ? 8.990   -132.777 22.425  1.00 95.02  ? 126 ASP   L OD1 1 
ATOM   20535 O  OD2 . ASP   L  12 126 ? 10.089  -134.368 21.369  1.00 87.86  ? 126 ASP   L OD2 1 
ATOM   20536 N  N   . PRO   L  12 127 ? 8.932   -134.479 25.550  1.00 84.64  ? 127 PRO   L N   1 
ATOM   20537 C  CA  . PRO   L  12 127 ? 9.654   -133.837 26.652  1.00 83.41  ? 127 PRO   L CA  1 
ATOM   20538 C  C   . PRO   L  12 127 ? 10.407  -132.535 26.314  1.00 87.09  ? 127 PRO   L C   1 
ATOM   20539 O  O   . PRO   L  12 127 ? 10.645  -131.761 27.233  1.00 87.28  ? 127 PRO   L O   1 
ATOM   20540 C  CB  . PRO   L  12 127 ? 10.648  -134.928 27.079  1.00 82.37  ? 127 PRO   L CB  1 
ATOM   20541 C  CG  . PRO   L  12 127 ? 9.967   -136.213 26.673  1.00 82.97  ? 127 PRO   L CG  1 
ATOM   20542 C  CD  . PRO   L  12 127 ? 9.338   -135.876 25.342  1.00 83.78  ? 127 PRO   L CD  1 
ATOM   20543 N  N   . VAL   L  12 128 ? 10.753  -132.306 25.040  1.00 85.16  ? 128 VAL   L N   1 
ATOM   20544 C  CA  . VAL   L  12 128 ? 11.603  -131.150 24.610  1.00 85.85  ? 128 VAL   L CA  1 
ATOM   20545 C  C   . VAL   L  12 128 ? 10.804  -130.167 23.741  1.00 86.37  ? 128 VAL   L C   1 
ATOM   20546 O  O   . VAL   L  12 128 ? 11.427  -129.219 23.228  1.00 89.41  ? 128 VAL   L O   1 
ATOM   20547 C  CB  . VAL   L  12 128 ? 12.896  -131.606 23.902  1.00 85.19  ? 128 VAL   L CB  1 
ATOM   20548 C  CG1 . VAL   L  12 128 ? 14.023  -131.820 24.899  1.00 82.04  ? 128 VAL   L CG1 1 
ATOM   20549 C  CG2 . VAL   L  12 128 ? 12.694  -132.844 23.042  1.00 85.90  ? 128 VAL   L CG2 1 
ATOM   20550 N  N   . GLY   L  12 129 ? 9.490   -130.360 23.584  1.00 89.21  ? 129 GLY   L N   1 
ATOM   20551 C  CA  . GLY   L  12 129 ? 8.567   -129.306 23.116  1.00 88.27  ? 129 GLY   L CA  1 
ATOM   20552 C  C   . GLY   L  12 129 ? 8.159   -129.438 21.658  1.00 89.48  ? 129 GLY   L C   1 
ATOM   20553 O  O   . GLY   L  12 129 ? 7.616   -128.456 21.122  1.00 89.68  ? 129 GLY   L O   1 
ATOM   20554 N  N   . SER   L  12 130 ? 8.377   -130.595 21.030  1.00 87.23  ? 130 SER   L N   1 
ATOM   20555 C  CA  . SER   L  12 130 ? 7.753   -130.937 19.727  1.00 89.25  ? 130 SER   L CA  1 
ATOM   20556 C  C   . SER   L  12 130 ? 6.251   -131.102 19.976  1.00 86.99  ? 130 SER   L C   1 
ATOM   20557 O  O   . SER   L  12 130 ? 5.905   -131.922 20.844  1.00 89.88  ? 130 SER   L O   1 
ATOM   20558 C  CB  . SER   L  12 130 ? 8.358   -132.179 19.127  1.00 90.47  ? 130 SER   L CB  1 
ATOM   20559 O  OG  . SER   L  12 130 ? 7.935   -132.346 17.785  1.00 96.33  ? 130 SER   L OG  1 
ATOM   20560 N  N   . TYR   L  12 131 ? 5.398   -130.329 19.297  1.00 85.44  ? 131 TYR   L N   1 
ATOM   20561 C  CA  . TYR   L  12 131 ? 3.930   -130.351 19.530  1.00 88.11  ? 131 TYR   L CA  1 
ATOM   20562 C  C   . TYR   L  12 131 ? 3.162   -130.417 18.208  1.00 87.82  ? 131 TYR   L C   1 
ATOM   20563 O  O   . TYR   L  12 131 ? 3.714   -130.095 17.138  1.00 84.68  ? 131 TYR   L O   1 
ATOM   20564 C  CB  . TYR   L  12 131 ? 3.490   -129.173 20.403  1.00 89.94  ? 131 TYR   L CB  1 
ATOM   20565 C  CG  . TYR   L  12 131 ? 3.349   -127.841 19.709  1.00 92.35  ? 131 TYR   L CG  1 
ATOM   20566 C  CD1 . TYR   L  12 131 ? 4.394   -126.931 19.694  1.00 94.33  ? 131 TYR   L CD1 1 
ATOM   20567 C  CD2 . TYR   L  12 131 ? 2.159   -127.466 19.107  1.00 95.23  ? 131 TYR   L CD2 1 
ATOM   20568 C  CE1 . TYR   L  12 131 ? 4.272   -125.698 19.077  1.00 96.96  ? 131 TYR   L CE1 1 
ATOM   20569 C  CE2 . TYR   L  12 131 ? 2.020   -126.238 18.482  1.00 98.63  ? 131 TYR   L CE2 1 
ATOM   20570 C  CZ  . TYR   L  12 131 ? 3.081   -125.349 18.467  1.00 101.03 ? 131 TYR   L CZ  1 
ATOM   20571 O  OH  . TYR   L  12 131 ? 2.956   -124.133 17.858  1.00 108.55 ? 131 TYR   L OH  1 
ATOM   20572 N  N   . GLU   L  12 132 ? 1.900   -130.831 18.328  1.00 92.29  ? 132 GLU   L N   1 
ATOM   20573 C  CA  . GLU   L  12 132 ? 0.990   -131.228 17.223  1.00 99.31  ? 132 GLU   L CA  1 
ATOM   20574 C  C   . GLU   L  12 132 ? -0.436  -131.221 17.781  1.00 99.10  ? 132 GLU   L C   1 
ATOM   20575 O  O   . GLU   L  12 132 ? -0.620  -131.684 18.924  1.00 102.29 ? 132 GLU   L O   1 
ATOM   20576 C  CB  . GLU   L  12 132 ? 1.389   -132.615 16.711  1.00 102.42 ? 132 GLU   L CB  1 
ATOM   20577 C  CG  . GLU   L  12 132 ? 0.567   -133.118 15.537  1.00 109.66 ? 132 GLU   L CG  1 
ATOM   20578 C  CD  . GLU   L  12 132 ? 0.701   -134.609 15.271  1.00 114.81 ? 132 GLU   L CD  1 
ATOM   20579 O  OE1 . GLU   L  12 132 ? 0.978   -135.370 16.227  1.00 116.93 ? 132 GLU   L OE1 1 
ATOM   20580 O  OE2 . GLU   L  12 132 ? 0.528   -135.008 14.106  1.00 121.44 ? 132 GLU   L OE2 1 
ATOM   20581 N  N   . ARG   L  12 133 ? -1.401  -130.693 17.030  1.00 99.25  ? 133 ARG   L N   1 
ATOM   20582 C  CA  . ARG   L  12 133 ? -2.836  -130.777 17.402  1.00 102.44 ? 133 ARG   L CA  1 
ATOM   20583 C  C   . ARG   L  12 133 ? -3.387  -132.103 16.868  1.00 103.67 ? 133 ARG   L C   1 
ATOM   20584 O  O   . ARG   L  12 133 ? -3.025  -132.479 15.736  1.00 104.41 ? 133 ARG   L O   1 
ATOM   20585 C  CB  . ARG   L  12 133 ? -3.624  -129.582 16.863  1.00 101.39 ? 133 ARG   L CB  1 
ATOM   20586 C  CG  . ARG   L  12 133 ? -5.027  -129.479 17.443  1.00 103.61 ? 133 ARG   L CG  1 
ATOM   20587 C  CD  . ARG   L  12 133 ? -5.866  -128.396 16.794  1.00 105.10 ? 133 ARG   L CD  1 
ATOM   20588 N  NE  . ARG   L  12 133 ? -7.250  -128.445 17.248  1.00 107.04 ? 133 ARG   L NE  1 
ATOM   20589 C  CZ  . ARG   L  12 133 ? -8.212  -127.608 16.864  1.00 108.62 ? 133 ARG   L CZ  1 
ATOM   20590 N  NH1 . ARG   L  12 133 ? -7.951  -126.631 16.011  1.00 109.25 ? 133 ARG   L NH1 1 
ATOM   20591 N  NH2 . ARG   L  12 133 ? -9.437  -127.752 17.340  1.00 110.78 ? 133 ARG   L NH2 1 
ATOM   20592 N  N   . GLU   L  12 134 ? -4.207  -132.788 17.669  1.00 109.56 ? 134 GLU   L N   1 
ATOM   20593 C  CA  . GLU   L  12 134 ? -4.857  -134.075 17.305  1.00 113.39 ? 134 GLU   L CA  1 
ATOM   20594 C  C   . GLU   L  12 134 ? -6.284  -134.107 17.865  1.00 115.09 ? 134 GLU   L C   1 
ATOM   20595 O  O   . GLU   L  12 134 ? -6.594  -133.286 18.748  1.00 118.70 ? 134 GLU   L O   1 
ATOM   20596 C  CB  . GLU   L  12 134 ? -4.045  -135.252 17.851  1.00 120.16 ? 134 GLU   L CB  1 
ATOM   20597 C  CG  . GLU   L  12 134 ? -2.720  -135.472 17.143  1.00 125.25 ? 134 GLU   L CG  1 
ATOM   20598 C  CD  . GLU   L  12 134 ? -1.746  -136.362 17.899  1.00 123.35 ? 134 GLU   L CD  1 
ATOM   20599 O  OE1 . GLU   L  12 134 ? -1.526  -137.510 17.458  1.00 134.46 ? 134 GLU   L OE1 1 
ATOM   20600 O  OE2 . GLU   L  12 134 ? -1.202  -135.902 18.924  1.00 118.77 ? 134 GLU   L OE2 1 
ATOM   20601 N  N   . GLN   L  12 135 ? -7.111  -135.025 17.358  1.00 114.46 ? 135 GLN   L N   1 
ATOM   20602 C  CA  . GLN   L  12 135 ? -8.442  -135.368 17.928  1.00 117.57 ? 135 GLN   L CA  1 
ATOM   20603 C  C   . GLN   L  12 135 ? -8.247  -136.178 19.215  1.00 112.79 ? 135 GLN   L C   1 
ATOM   20604 O  O   . GLN   L  12 135 ? -9.180  -136.207 20.043  1.00 113.29 ? 135 GLN   L O   1 
ATOM   20605 C  CB  . GLN   L  12 135 ? -9.267  -136.191 16.933  1.00 121.13 ? 135 GLN   L CB  1 
ATOM   20606 C  CG  . GLN   L  12 135 ? -9.956  -135.367 15.851  1.00 127.04 ? 135 GLN   L CG  1 
ATOM   20607 C  CD  . GLN   L  12 135 ? -11.109 -134.529 16.355  1.00 130.10 ? 135 GLN   L CD  1 
ATOM   20608 O  OE1 . GLN   L  12 135 ? -11.205 -133.338 16.064  1.00 131.31 ? 135 GLN   L OE1 1 
ATOM   20609 N  NE2 . GLN   L  12 135 ? -12.008 -135.145 17.108  1.00 136.49 ? 135 GLN   L NE2 1 
ATOM   20610 N  N   . CYS   L  12 136 ? -7.070  -136.792 19.376  1.00 109.86 ? 136 CYS   L N   1 
ATOM   20611 C  CA  . CYS   L  12 136 ? -6.863  -138.021 20.184  1.00 110.57 ? 136 CYS   L CA  1 
ATOM   20612 C  C   . CYS   L  12 136 ? -5.401  -138.168 20.614  1.00 101.12 ? 136 CYS   L C   1 
ATOM   20613 O  O   . CYS   L  12 136 ? -4.521  -138.162 19.727  1.00 98.92  ? 136 CYS   L O   1 
ATOM   20614 C  CB  . CYS   L  12 136 ? -7.234  -139.243 19.355  1.00 113.70 ? 136 CYS   L CB  1 
ATOM   20615 S  SG  . CYS   L  12 136 ? -8.228  -140.440 20.275  1.00 122.20 ? 136 CYS   L SG  1 
ATOM   20616 N  N   . ARG   L  12 137 ? -5.154  -138.344 21.914  1.00 96.41  ? 137 ARG   L N   1 
ATOM   20617 C  CA  . ARG   L  12 137 ? -3.800  -138.673 22.427  1.00 92.38  ? 137 ARG   L CA  1 
ATOM   20618 C  C   . ARG   L  12 137 ? -3.878  -139.231 23.847  1.00 93.48  ? 137 ARG   L C   1 
ATOM   20619 O  O   . ARG   L  12 137 ? -4.491  -138.580 24.712  1.00 95.64  ? 137 ARG   L O   1 
ATOM   20620 C  CB  . ARG   L  12 137 ? -2.881  -137.450 22.416  1.00 90.82  ? 137 ARG   L CB  1 
ATOM   20621 C  CG  . ARG   L  12 137 ? -1.484  -137.729 22.952  1.00 91.02  ? 137 ARG   L CG  1 
ATOM   20622 C  CD  . ARG   L  12 137 ? -0.763  -138.820 22.187  1.00 92.74  ? 137 ARG   L CD  1 
ATOM   20623 N  NE  . ARG   L  12 137 ? -0.317  -138.373 20.875  1.00 97.86  ? 137 ARG   L NE  1 
ATOM   20624 C  CZ  . ARG   L  12 137 ? 0.151   -139.172 19.919  1.00 102.91 ? 137 ARG   L CZ  1 
ATOM   20625 N  NH1 . ARG   L  12 137 ? 0.235   -140.480 20.108  1.00 103.47 ? 137 ARG   L NH1 1 
ATOM   20626 N  NH2 . ARG   L  12 137 ? 0.529   -138.657 18.763  1.00 109.17 ? 137 ARG   L NH2 1 
ATOM   20627 N  N   . ALA   L  12 138 ? -3.243  -140.386 24.051  1.00 92.97  ? 138 ALA   L N   1 
ATOM   20628 C  CA  . ALA   L  12 138 ? -2.901  -140.966 25.367  1.00 91.61  ? 138 ALA   L CA  1 
ATOM   20629 C  C   . ALA   L  12 138 ? -1.422  -140.682 25.646  1.00 87.61  ? 138 ALA   L C   1 
ATOM   20630 O  O   . ALA   L  12 138 ? -0.625  -140.682 24.686  1.00 83.17  ? 138 ALA   L O   1 
ATOM   20631 C  CB  . ALA   L  12 138 ? -3.199  -142.446 25.374  1.00 94.22  ? 138 ALA   L CB  1 
ATOM   20632 N  N   . GLY   L  12 139 ? -1.082  -140.432 26.910  1.00 85.69  ? 139 GLY   L N   1 
ATOM   20633 C  CA  . GLY   L  12 139 ? 0.299   -140.192 27.367  1.00 86.66  ? 139 GLY   L CA  1 
ATOM   20634 C  C   . GLY   L  12 139 ? 0.577   -140.913 28.671  1.00 86.53  ? 139 GLY   L C   1 
ATOM   20635 O  O   . GLY   L  12 139 ? -0.389  -141.192 29.408  1.00 87.21  ? 139 GLY   L O   1 
ATOM   20636 N  N   . GLY   L  12 140 ? 1.848   -141.219 28.941  1.00 88.16  ? 140 GLY   L N   1 
ATOM   20637 C  CA  . GLY   L  12 140 ? 2.285   -141.852 30.199  1.00 91.04  ? 140 GLY   L CA  1 
ATOM   20638 C  C   . GLY   L  12 140 ? 2.489   -143.352 30.060  1.00 90.84  ? 140 GLY   L C   1 
ATOM   20639 O  O   . GLY   L  12 140 ? 2.597   -143.840 28.918  1.00 89.71  ? 140 GLY   L O   1 
ATOM   20640 N  N   . ALA   L  12 141 ? 2.513   -144.054 31.197  1.00 94.23  ? 141 ALA   L N   1 
ATOM   20641 C  CA  . ALA   L  12 141 ? 2.961   -145.460 31.352  1.00 95.20  ? 141 ALA   L CA  1 
ATOM   20642 C  C   . ALA   L  12 141 ? 2.198   -146.399 30.405  1.00 93.73  ? 141 ALA   L C   1 
ATOM   20643 O  O   . ALA   L  12 141 ? 2.853   -147.248 29.768  1.00 91.35  ? 141 ALA   L O   1 
ATOM   20644 C  CB  . ALA   L  12 141 ? 2.801   -145.883 32.793  1.00 97.03  ? 141 ALA   L CB  1 
ATOM   20645 N  N   . ALA   L  12 142 ? 0.872   -146.257 30.313  1.00 94.12  ? 142 ALA   L N   1 
ATOM   20646 C  CA  . ALA   L  12 142 ? -0.024  -147.185 29.583  1.00 95.12  ? 142 ALA   L CA  1 
ATOM   20647 C  C   . ALA   L  12 142 ? -0.446  -146.596 28.231  1.00 92.97  ? 142 ALA   L C   1 
ATOM   20648 O  O   . ALA   L  12 142 ? -1.414  -147.114 27.645  1.00 90.94  ? 142 ALA   L O   1 
ATOM   20649 C  CB  . ALA   L  12 142 ? -1.226  -147.503 30.439  1.00 98.75  ? 142 ALA   L CB  1 
ATOM   20650 N  N   . ALA   L  12 143 ? 0.249   -145.565 27.742  1.00 95.43  ? 143 ALA   L N   1 
ATOM   20651 C  CA  . ALA   L  12 143 ? -0.038  -144.911 26.442  1.00 95.81  ? 143 ALA   L CA  1 
ATOM   20652 C  C   . ALA   L  12 143 ? -0.054  -145.971 25.335  1.00 92.13  ? 143 ALA   L C   1 
ATOM   20653 O  O   . ALA   L  12 143 ? -0.960  -145.929 24.481  1.00 85.88  ? 143 ALA   L O   1 
ATOM   20654 C  CB  . ALA   L  12 143 ? 0.975   -143.825 26.165  1.00 98.29  ? 143 ALA   L CB  1 
ATOM   20655 N  N   . SER   L  12 144 ? 0.895   -146.910 25.379  1.00 93.08  ? 144 SER   L N   1 
ATOM   20656 C  CA  . SER   L  12 144 ? 1.083   -147.968 24.352  1.00 93.85  ? 144 SER   L CA  1 
ATOM   20657 C  C   . SER   L  12 144 ? -0.112  -148.931 24.338  1.00 90.58  ? 144 SER   L C   1 
ATOM   20658 O  O   . SER   L  12 144 ? -0.368  -149.515 23.272  1.00 87.11  ? 144 SER   L O   1 
ATOM   20659 C  CB  . SER   L  12 144 ? 2.391   -148.698 24.544  1.00 96.91  ? 144 SER   L CB  1 
ATOM   20660 O  OG  . SER   L  12 144 ? 2.385   -149.455 25.745  1.00 99.96  ? 144 SER   L OG  1 
ATOM   20661 N  N   . LEU   L  12 145 ? -0.813  -149.080 25.470  1.00 93.37  ? 145 LEU   L N   1 
ATOM   20662 C  CA  . LEU   L  12 145 ? -2.022  -149.943 25.610  1.00 93.44  ? 145 LEU   L CA  1 
ATOM   20663 C  C   . LEU   L  12 145 ? -3.260  -149.208 25.078  1.00 92.73  ? 145 LEU   L C   1 
ATOM   20664 O  O   . LEU   L  12 145 ? -4.070  -149.848 24.390  1.00 89.89  ? 145 LEU   L O   1 
ATOM   20665 C  CB  . LEU   L  12 145 ? -2.231  -150.326 27.080  1.00 96.48  ? 145 LEU   L CB  1 
ATOM   20666 C  CG  . LEU   L  12 145 ? -1.350  -151.452 27.622  1.00 97.09  ? 145 LEU   L CG  1 
ATOM   20667 C  CD1 . LEU   L  12 145 ? 0.022   -150.931 28.027  1.00 97.62  ? 145 LEU   L CD1 1 
ATOM   20668 C  CD2 . LEU   L  12 145 ? -2.021  -152.134 28.804  1.00 98.16  ? 145 LEU   L CD2 1 
ATOM   20669 N  N   . ILE   L  12 146 ? -3.415  -147.923 25.409  1.00 92.32  ? 146 ILE   L N   1 
ATOM   20670 C  CA  . ILE   L  12 146 ? -4.679  -147.158 25.188  1.00 93.20  ? 146 ILE   L CA  1 
ATOM   20671 C  C   . ILE   L  12 146 ? -4.721  -146.622 23.751  1.00 90.79  ? 146 ILE   L C   1 
ATOM   20672 O  O   . ILE   L  12 146 ? -5.801  -146.691 23.139  1.00 89.73  ? 146 ILE   L O   1 
ATOM   20673 C  CB  . ILE   L  12 146 ? -4.841  -146.034 26.232  1.00 92.33  ? 146 ILE   L CB  1 
ATOM   20674 C  CG1 . ILE   L  12 146 ? -4.864  -146.594 27.658  1.00 93.91  ? 146 ILE   L CG1 1 
ATOM   20675 C  CG2 . ILE   L  12 146 ? -6.083  -145.204 25.937  1.00 92.17  ? 146 ILE   L CG2 1 
ATOM   20676 C  CD1 . ILE   L  12 146 ? -4.767  -145.545 28.745  1.00 93.83  ? 146 ILE   L CD1 1 
ATOM   20677 N  N   . MET   L  12 147 ? -3.604  -146.100 23.235  1.00 94.16  ? 147 MET   L N   1 
ATOM   20678 C  CA  . MET   L  12 147 ? -3.567  -145.322 21.964  1.00 96.37  ? 147 MET   L CA  1 
ATOM   20679 C  C   . MET   L  12 147 ? -4.085  -146.156 20.790  1.00 95.42  ? 147 MET   L C   1 
ATOM   20680 O  O   . MET   L  12 147 ? -4.877  -145.657 19.997  1.00 96.34  ? 147 MET   L O   1 
ATOM   20681 C  CB  . MET   L  12 147 ? -2.157  -144.806 21.653  1.00 98.00  ? 147 MET   L CB  1 
ATOM   20682 C  CG  . MET   L  12 147 ? -2.130  -143.702 20.605  1.00 96.82  ? 147 MET   L CG  1 
ATOM   20683 S  SD  . MET   L  12 147 ? -3.111  -142.258 21.082  1.00 97.47  ? 147 MET   L SD  1 
ATOM   20684 C  CE  . MET   L  12 147 ? -3.256  -141.420 19.503  1.00 101.05 ? 147 MET   L CE  1 
ATOM   20685 N  N   . PRO   L  12 148 ? -3.671  -147.432 20.605  1.00 98.74  ? 148 PRO   L N   1 
ATOM   20686 C  CA  . PRO   L  12 148 ? -4.173  -148.233 19.484  1.00 98.34  ? 148 PRO   L CA  1 
ATOM   20687 C  C   . PRO   L  12 148 ? -5.695  -148.451 19.512  1.00 95.30  ? 148 PRO   L C   1 
ATOM   20688 O  O   . PRO   L  12 148 ? -6.287  -148.542 18.451  1.00 92.17  ? 148 PRO   L O   1 
ATOM   20689 C  CB  . PRO   L  12 148 ? -3.441  -149.578 19.617  1.00 99.31  ? 148 PRO   L CB  1 
ATOM   20690 C  CG  . PRO   L  12 148 ? -2.954  -149.611 21.052  1.00 101.40 ? 148 PRO   L CG  1 
ATOM   20691 C  CD  . PRO   L  12 148 ? -2.689  -148.166 21.419  1.00 100.71 ? 148 PRO   L CD  1 
ATOM   20692 N  N   . PHE   L  12 149 ? -6.279  -148.539 20.713  1.00 97.69  ? 149 PHE   L N   1 
ATOM   20693 C  CA  . PHE   L  12 149 ? -7.743  -148.653 20.951  1.00 100.64 ? 149 PHE   L CA  1 
ATOM   20694 C  C   . PHE   L  12 149 ? -8.442  -147.371 20.482  1.00 99.71  ? 149 PHE   L C   1 
ATOM   20695 O  O   . PHE   L  12 149 ? -9.504  -147.482 19.841  1.00 101.92 ? 149 PHE   L O   1 
ATOM   20696 C  CB  . PHE   L  12 149 ? -8.032  -148.930 22.430  1.00 100.20 ? 149 PHE   L CB  1 
ATOM   20697 C  CG  . PHE   L  12 149 ? -9.489  -148.876 22.812  1.00 102.73 ? 149 PHE   L CG  1 
ATOM   20698 C  CD1 . PHE   L  12 149 ? -10.377 -149.844 22.369  1.00 100.79 ? 149 PHE   L CD1 1 
ATOM   20699 C  CD2 . PHE   L  12 149 ? -9.973  -147.858 23.622  1.00 104.45 ? 149 PHE   L CD2 1 
ATOM   20700 C  CE1 . PHE   L  12 149 ? -11.715 -149.795 22.727  1.00 101.31 ? 149 PHE   L CE1 1 
ATOM   20701 C  CE2 . PHE   L  12 149 ? -11.313 -147.810 23.976  1.00 105.36 ? 149 PHE   L CE2 1 
ATOM   20702 C  CZ  . PHE   L  12 149 ? -12.181 -148.778 23.528  1.00 103.24 ? 149 PHE   L CZ  1 
ATOM   20703 N  N   . LEU   L  12 150 ? -7.863  -146.208 20.806  1.00 103.41 ? 150 LEU   L N   1 
ATOM   20704 C  CA  . LEU   L  12 150 ? -8.368  -144.859 20.422  1.00 102.96 ? 150 LEU   L CA  1 
ATOM   20705 C  C   . LEU   L  12 150 ? -8.365  -144.729 18.894  1.00 101.21 ? 150 LEU   L C   1 
ATOM   20706 O  O   . LEU   L  12 150 ? -9.393  -144.287 18.350  1.00 101.78 ? 150 LEU   L O   1 
ATOM   20707 C  CB  . LEU   L  12 150 ? -7.496  -143.777 21.074  1.00 101.48 ? 150 LEU   L CB  1 
ATOM   20708 C  CG  . LEU   L  12 150 ? -8.007  -143.165 22.380  1.00 102.14 ? 150 LEU   L CG  1 
ATOM   20709 C  CD1 . LEU   L  12 150 ? -8.833  -144.141 23.206  1.00 101.87 ? 150 LEU   L CD1 1 
ATOM   20710 C  CD2 . LEU   L  12 150 ? -6.838  -142.641 23.196  1.00 105.03 ? 150 LEU   L CD2 1 
ATOM   20711 N  N   . ASP   L  12 151 ? -7.263  -145.110 18.233  1.00 102.77 ? 151 ASP   L N   1 
ATOM   20712 C  CA  . ASP   L  12 151 ? -7.142  -145.116 16.748  1.00 106.01 ? 151 ASP   L CA  1 
ATOM   20713 C  C   . ASP   L  12 151 ? -8.348  -145.846 16.151  1.00 105.41 ? 151 ASP   L C   1 
ATOM   20714 O  O   . ASP   L  12 151 ? -8.871  -145.383 15.124  1.00 107.65 ? 151 ASP   L O   1 
ATOM   20715 C  CB  . ASP   L  12 151 ? -5.867  -145.812 16.267  1.00 109.84 ? 151 ASP   L CB  1 
ATOM   20716 C  CG  . ASP   L  12 151 ? -4.588  -145.082 16.625  1.00 111.66 ? 151 ASP   L CG  1 
ATOM   20717 O  OD1 . ASP   L  12 151 ? -4.549  -143.847 16.455  1.00 114.15 ? 151 ASP   L OD1 1 
ATOM   20718 O  OD2 . ASP   L  12 151 ? -3.640  -145.759 17.068  1.00 117.91 ? 151 ASP   L OD2 1 
ATOM   20719 N  N   . ASN   L  12 152 ? -8.762  -146.946 16.784  1.00 105.67 ? 152 ASN   L N   1 
ATOM   20720 C  CA  . ASN   L  12 152 ? -9.813  -147.864 16.274  1.00 106.16 ? 152 ASN   L CA  1 
ATOM   20721 C  C   . ASN   L  12 152 ? -11.213 -147.301 16.550  1.00 106.71 ? 152 ASN   L C   1 
ATOM   20722 O  O   . ASN   L  12 152 ? -12.078 -147.475 15.680  1.00 105.12 ? 152 ASN   L O   1 
ATOM   20723 C  CB  . ASN   L  12 152 ? -9.668  -149.265 16.876  1.00 106.87 ? 152 ASN   L CB  1 
ATOM   20724 C  CG  . ASN   L  12 152 ? -10.594 -150.290 16.251  1.00 107.95 ? 152 ASN   L CG  1 
ATOM   20725 O  OD1 . ASN   L  12 152 ? -11.244 -151.059 16.956  1.00 107.31 ? 152 ASN   L OD1 1 
ATOM   20726 N  ND2 . ASN   L  12 152 ? -10.661 -150.324 14.930  1.00 107.22 ? 152 ASN   L ND2 1 
ATOM   20727 N  N   . GLN   L  12 153 ? -11.435 -146.674 17.711  1.00 109.23 ? 153 GLN   L N   1 
ATOM   20728 C  CA  . GLN   L  12 153 ? -12.796 -146.324 18.212  1.00 114.05 ? 153 GLN   L CA  1 
ATOM   20729 C  C   . GLN   L  12 153 ? -13.106 -144.831 18.032  1.00 114.70 ? 153 GLN   L C   1 
ATOM   20730 O  O   . GLN   L  12 153 ? -14.310 -144.505 17.979  1.00 116.90 ? 153 GLN   L O   1 
ATOM   20731 C  CB  . GLN   L  12 153 ? -12.945 -146.750 19.675  1.00 115.57 ? 153 GLN   L CB  1 
ATOM   20732 C  CG  . GLN   L  12 153 ? -12.921 -148.260 19.866  1.00 116.19 ? 153 GLN   L CG  1 
ATOM   20733 C  CD  . GLN   L  12 153 ? -14.030 -148.952 19.109  1.00 117.56 ? 153 GLN   L CD  1 
ATOM   20734 O  OE1 . GLN   L  12 153 ? -15.200 -148.587 19.216  1.00 115.23 ? 153 GLN   L OE1 1 
ATOM   20735 N  NE2 . GLN   L  12 153 ? -13.672 -149.962 18.330  1.00 118.12 ? 153 GLN   L NE2 1 
ATOM   20736 N  N   . VAL   L  12 154 ? -12.092 -143.960 17.948  1.00 115.35 ? 154 VAL   L N   1 
ATOM   20737 C  CA  . VAL   L  12 154 ? -12.281 -142.490 17.749  1.00 114.98 ? 154 VAL   L CA  1 
ATOM   20738 C  C   . VAL   L  12 154 ? -12.128 -142.175 16.254  1.00 112.70 ? 154 VAL   L C   1 
ATOM   20739 O  O   . VAL   L  12 154 ? -13.076 -141.605 15.680  1.00 113.73 ? 154 VAL   L O   1 
ATOM   20740 C  CB  . VAL   L  12 154 ? -11.327 -141.662 18.635  1.00 116.36 ? 154 VAL   L CB  1 
ATOM   20741 C  CG1 . VAL   L  12 154 ? -11.511 -140.164 18.434  1.00 118.87 ? 154 VAL   L CG1 1 
ATOM   20742 C  CG2 . VAL   L  12 154 ? -11.488 -142.012 20.109  1.00 117.60 ? 154 VAL   L CG2 1 
ATOM   20743 N  N   . ASN   L  12 155 ? -11.003 -142.564 15.642  1.00 114.05 ? 155 ASN   L N   1 
ATOM   20744 C  CA  . ASN   L  12 155 ? -10.644 -142.219 14.237  1.00 117.55 ? 155 ASN   L CA  1 
ATOM   20745 C  C   . ASN   L  12 155 ? -11.064 -143.343 13.273  1.00 115.72 ? 155 ASN   L C   1 
ATOM   20746 O  O   . ASN   L  12 155 ? -10.812 -143.192 12.060  1.00 115.22 ? 155 ASN   L O   1 
ATOM   20747 C  CB  . ASN   L  12 155 ? -9.151  -141.890 14.116  1.00 121.83 ? 155 ASN   L CB  1 
ATOM   20748 C  CG  . ASN   L  12 155 ? -8.760  -140.618 14.841  1.00 124.71 ? 155 ASN   L CG  1 
ATOM   20749 O  OD1 . ASN   L  12 155 ? -9.529  -139.659 14.882  1.00 129.12 ? 155 ASN   L OD1 1 
ATOM   20750 N  ND2 . ASN   L  12 155 ? -7.561  -140.590 15.406  1.00 124.77 ? 155 ASN   L ND2 1 
ATOM   20751 N  N   . PHE   L  12 156 ? -11.684 -144.416 13.783  1.00 117.10 ? 156 PHE   L N   1 
ATOM   20752 C  CA  . PHE   L  12 156 ? -12.238 -145.563 13.010  1.00 119.35 ? 156 PHE   L CA  1 
ATOM   20753 C  C   . PHE   L  12 156 ? -11.198 -146.140 12.041  1.00 117.40 ? 156 PHE   L C   1 
ATOM   20754 O  O   . PHE   L  12 156 ? -11.559 -146.448 10.888  1.00 113.88 ? 156 PHE   L O   1 
ATOM   20755 C  CB  . PHE   L  12 156 ? -13.497 -145.144 12.249  1.00 124.32 ? 156 PHE   L CB  1 
ATOM   20756 C  CG  . PHE   L  12 156 ? -14.570 -144.533 13.113  1.00 130.30 ? 156 PHE   L CG  1 
ATOM   20757 C  CD1 . PHE   L  12 156 ? -14.984 -145.161 14.278  1.00 132.93 ? 156 PHE   L CD1 1 
ATOM   20758 C  CD2 . PHE   L  12 156 ? -15.170 -143.334 12.760  1.00 133.81 ? 156 PHE   L CD2 1 
ATOM   20759 C  CE1 . PHE   L  12 156 ? -15.968 -144.598 15.075  1.00 136.96 ? 156 PHE   L CE1 1 
ATOM   20760 C  CE2 . PHE   L  12 156 ? -16.158 -142.773 13.556  1.00 136.66 ? 156 PHE   L CE2 1 
ATOM   20761 C  CZ  . PHE   L  12 156 ? -16.555 -143.406 14.712  1.00 137.89 ? 156 PHE   L CZ  1 
ATOM   20762 N  N   . LYS   L  12 157 ? -9.958  -146.312 12.506  1.00 118.68 ? 157 LYS   L N   1 
ATOM   20763 C  CA  . LYS   L  12 157 ? -8.843  -146.904 11.717  1.00 125.33 ? 157 LYS   L CA  1 
ATOM   20764 C  C   . LYS   L  12 157 ? -9.108  -148.407 11.530  1.00 126.23 ? 157 LYS   L C   1 
ATOM   20765 O  O   . LYS   L  12 157 ? -9.641  -149.037 12.469  1.00 133.74 ? 157 LYS   L O   1 
ATOM   20766 C  CB  . LYS   L  12 157 ? -7.502  -146.630 12.410  1.00 128.08 ? 157 LYS   L CB  1 
ATOM   20767 C  CG  . LYS   L  12 157 ? -7.096  -145.162 12.490  1.00 130.58 ? 157 LYS   L CG  1 
ATOM   20768 C  CD  . LYS   L  12 157 ? -6.599  -144.586 11.178  1.00 133.99 ? 157 LYS   L CD  1 
ATOM   20769 C  CE  . LYS   L  12 157 ? -6.181  -143.133 11.278  1.00 138.29 ? 157 LYS   L CE  1 
ATOM   20770 N  NZ  . LYS   L  12 157 ? -4.915  -142.967 12.034  1.00 143.09 ? 157 LYS   L NZ  1 
ATOM   20771 N  N   . ASN   L  12 158 ? -8.788  -148.942 10.343  1.00 118.94 ? 158 ASN   L N   1 
ATOM   20772 C  CA  . ASN   L  12 158 ? -8.883  -150.384 9.971   1.00 115.78 ? 158 ASN   L CA  1 
ATOM   20773 C  C   . ASN   L  12 158 ? -10.348 -150.842 9.879   1.00 114.57 ? 158 ASN   L C   1 
ATOM   20774 O  O   . ASN   L  12 158 ? -10.562 -152.032 9.581   1.00 113.04 ? 158 ASN   L O   1 
ATOM   20775 C  CB  . ASN   L  12 158 ? -8.109  -151.291 10.936  1.00 110.81 ? 158 ASN   L CB  1 
ATOM   20776 C  CG  . ASN   L  12 158 ? -6.606  -151.176 10.797  1.00 108.28 ? 158 ASN   L CG  1 
ATOM   20777 O  OD1 . ASN   L  12 158 ? -5.924  -150.776 11.738  1.00 111.65 ? 158 ASN   L OD1 1 
ATOM   20778 N  ND2 . ASN   L  12 158 ? -6.078  -151.537 9.638   1.00 103.68 ? 158 ASN   L ND2 1 
ATOM   20779 N  N   . GLN   L  12 159 ? -11.317 -149.945 10.093  1.00 117.90 ? 159 GLN   L N   1 
ATOM   20780 C  CA  . GLN   L  12 159 ? -12.771 -150.265 10.069  1.00 120.20 ? 159 GLN   L CA  1 
ATOM   20781 C  C   . GLN   L  12 159 ? -13.348 -149.868 8.706   1.00 121.70 ? 159 GLN   L C   1 
ATOM   20782 O  O   . GLN   L  12 159 ? -13.365 -148.658 8.410   1.00 124.98 ? 159 GLN   L O   1 
ATOM   20783 C  CB  . GLN   L  12 159 ? -13.508 -149.536 11.194  1.00 123.78 ? 159 GLN   L CB  1 
ATOM   20784 C  CG  . GLN   L  12 159 ? -13.215 -150.095 12.579  1.00 122.79 ? 159 GLN   L CG  1 
ATOM   20785 C  CD  . GLN   L  12 159 ? -14.303 -149.782 13.579  1.00 123.60 ? 159 GLN   L CD  1 
ATOM   20786 O  OE1 . GLN   L  12 159 ? -14.088 -149.064 14.553  1.00 131.04 ? 159 GLN   L OE1 1 
ATOM   20787 N  NE2 . GLN   L  12 159 ? -15.490 -150.319 13.346  1.00 119.39 ? 159 GLN   L NE2 1 
ATOM   20788 N  N   . TYR   L  12 160 ? -13.805 -150.848 7.919   1.00 120.58 ? 160 TYR   L N   1 
ATOM   20789 C  CA  . TYR   L  12 160 ? -14.402 -150.649 6.571   1.00 120.49 ? 160 TYR   L CA  1 
ATOM   20790 C  C   . TYR   L  12 160 ? -15.914 -150.885 6.620   1.00 123.35 ? 160 TYR   L C   1 
ATOM   20791 O  O   . TYR   L  12 160 ? -16.387 -151.667 7.468   1.00 112.17 ? 160 TYR   L O   1 
ATOM   20792 C  CB  . TYR   L  12 160 ? -13.751 -151.573 5.541   1.00 119.53 ? 160 TYR   L CB  1 
ATOM   20793 C  CG  . TYR   L  12 160 ? -12.339 -151.193 5.185   1.00 119.50 ? 160 TYR   L CG  1 
ATOM   20794 C  CD1 . TYR   L  12 160 ? -11.261 -151.758 5.846   1.00 120.06 ? 160 TYR   L CD1 1 
ATOM   20795 C  CD2 . TYR   L  12 160 ? -12.078 -150.255 4.200   1.00 119.61 ? 160 TYR   L CD2 1 
ATOM   20796 C  CE1 . TYR   L  12 160 ? -9.958  -151.410 5.529   1.00 121.60 ? 160 TYR   L CE1 1 
ATOM   20797 C  CE2 . TYR   L  12 160 ? -10.782 -149.894 3.872   1.00 122.48 ? 160 TYR   L CE2 1 
ATOM   20798 C  CZ  . TYR   L  12 160 ? -9.717  -150.475 4.539   1.00 122.82 ? 160 TYR   L CZ  1 
ATOM   20799 O  OH  . TYR   L  12 160 ? -8.433  -150.132 4.227   1.00 125.23 ? 160 TYR   L OH  1 
ATOM   20800 N  N   . GLU   L  12 161 ? -16.637 -150.220 5.714   1.00 129.73 ? 161 GLU   L N   1 
ATOM   20801 C  CA  . GLU   L  12 161 ? -18.114 -150.316 5.564   1.00 138.35 ? 161 GLU   L CA  1 
ATOM   20802 C  C   . GLU   L  12 161 ? -18.460 -151.749 5.158   1.00 139.51 ? 161 GLU   L C   1 
ATOM   20803 O  O   . GLU   L  12 161 ? -17.992 -152.223 4.125   1.00 143.18 ? 161 GLU   L O   1 
ATOM   20804 C  CB  . GLU   L  12 161 ? -18.613 -149.300 4.532   1.00 143.74 ? 161 GLU   L CB  1 
ATOM   20805 C  CG  . GLU   L  12 161 ? -20.018 -148.787 4.801   1.00 149.84 ? 161 GLU   L CG  1 
ATOM   20806 C  CD  . GLU   L  12 161 ? -20.099 -147.562 5.699   1.00 151.90 ? 161 GLU   L CD  1 
ATOM   20807 O  OE1 . GLU   L  12 161 ? -19.249 -146.660 5.553   1.00 159.40 ? 161 GLU   L OE1 1 
ATOM   20808 O  OE2 . GLU   L  12 161 ? -21.017 -147.510 6.541   1.00 158.10 ? 161 GLU   L OE2 1 
ATOM   20809 N  N   . PRO   L  12 162 ? -19.250 -152.496 5.966   1.00 139.85 ? 162 PRO   L N   1 
ATOM   20810 C  CA  . PRO   L  12 162 ? -19.574 -153.890 5.652   1.00 137.44 ? 162 PRO   L CA  1 
ATOM   20811 C  C   . PRO   L  12 162 ? -20.153 -154.096 4.243   1.00 139.10 ? 162 PRO   L C   1 
ATOM   20812 O  O   . PRO   L  12 162 ? -21.036 -153.352 3.861   1.00 142.51 ? 162 PRO   L O   1 
ATOM   20813 C  CB  . PRO   L  12 162 ? -20.629 -154.258 6.707   1.00 138.32 ? 162 PRO   L CB  1 
ATOM   20814 C  CG  . PRO   L  12 162 ? -20.314 -153.349 7.874   1.00 137.74 ? 162 PRO   L CG  1 
ATOM   20815 C  CD  . PRO   L  12 162 ? -19.837 -152.058 7.243   1.00 138.97 ? 162 PRO   L CD  1 
ATOM   20816 N  N   . GLY   L  12 163 ? -19.634 -155.092 3.515   1.00 139.88 ? 163 GLY   L N   1 
ATOM   20817 C  CA  . GLY   L  12 163 ? -20.126 -155.504 2.185   1.00 142.84 ? 163 GLY   L CA  1 
ATOM   20818 C  C   . GLY   L  12 163 ? -19.492 -154.728 1.040   1.00 142.91 ? 163 GLY   L C   1 
ATOM   20819 O  O   . GLY   L  12 163 ? -19.771 -155.087 -0.115  1.00 142.76 ? 163 GLY   L O   1 
ATOM   20820 N  N   . THR   L  12 164 ? -18.658 -153.718 1.323   1.00 148.44 ? 164 THR   L N   1 
ATOM   20821 C  CA  . THR   L  12 164 ? -18.064 -152.808 0.302   1.00 154.15 ? 164 THR   L CA  1 
ATOM   20822 C  C   . THR   L  12 164 ? -16.748 -153.378 -0.248  1.00 159.00 ? 164 THR   L C   1 
ATOM   20823 O  O   . THR   L  12 164 ? -16.144 -152.699 -1.102  1.00 159.41 ? 164 THR   L O   1 
ATOM   20824 C  CB  . THR   L  12 164 ? -17.857 -151.390 0.853   1.00 154.57 ? 164 THR   L CB  1 
ATOM   20825 O  OG1 . THR   L  12 164 ? -16.959 -151.442 1.963   1.00 157.10 ? 164 THR   L OG1 1 
ATOM   20826 C  CG2 . THR   L  12 164 ? -19.155 -150.735 1.269   1.00 153.03 ? 164 THR   L CG2 1 
ATOM   20827 N  N   . ASN   L  12 165 ? -16.323 -154.563 0.209   1.00 158.63 ? 165 ASN   L N   1 
ATOM   20828 C  CA  . ASN   L  12 165 ? -15.116 -155.273 -0.295  1.00 158.99 ? 165 ASN   L CA  1 
ATOM   20829 C  C   . ASN   L  12 165 ? -13.852 -154.607 0.268   1.00 156.42 ? 165 ASN   L C   1 
ATOM   20830 O  O   . ASN   L  12 165 ? -12.790 -154.723 -0.374  1.00 152.97 ? 165 ASN   L O   1 
ATOM   20831 C  CB  . ASN   L  12 165 ? -15.103 -155.303 -1.829  1.00 164.21 ? 165 ASN   L CB  1 
ATOM   20832 C  CG  . ASN   L  12 165 ? -14.097 -156.260 -2.435  1.00 167.88 ? 165 ASN   L CG  1 
ATOM   20833 O  OD1 . ASN   L  12 165 ? -13.521 -155.963 -3.479  1.00 175.76 ? 165 ASN   L OD1 1 
ATOM   20834 N  ND2 . ASN   L  12 165 ? -13.876 -157.405 -1.808  1.00 170.77 ? 165 ASN   L ND2 1 
ATOM   20835 N  N   . GLY   L  12 166 ? -13.959 -153.948 1.428   1.00 150.66 ? 166 GLY   L N   1 
ATOM   20836 C  CA  . GLY   L  12 166 ? -12.857 -153.189 2.052   1.00 149.63 ? 166 GLY   L CA  1 
ATOM   20837 C  C   . GLY   L  12 166 ? -12.403 -152.038 1.170   1.00 153.72 ? 166 GLY   L C   1 
ATOM   20838 O  O   . GLY   L  12 166 ? -11.187 -151.763 1.137   1.00 157.94 ? 166 GLY   L O   1 
ATOM   20839 N  N   . LYS   L  12 167 ? -13.349 -151.394 0.478   1.00 149.84 ? 167 LYS   L N   1 
ATOM   20840 C  CA  . LYS   L  12 167 ? -13.095 -150.328 -0.530  1.00 151.40 ? 167 LYS   L CA  1 
ATOM   20841 C  C   . LYS   L  12 167 ? -13.571 -148.971 0.005   1.00 150.79 ? 167 LYS   L C   1 
ATOM   20842 O  O   . LYS   L  12 167 ? -12.967 -147.949 -0.377  1.00 152.03 ? 167 LYS   L O   1 
ATOM   20843 C  CB  . LYS   L  12 167 ? -13.812 -150.668 -1.840  1.00 151.17 ? 167 LYS   L CB  1 
ATOM   20844 C  CG  . LYS   L  12 167 ? -12.981 -150.505 -3.105  1.00 152.67 ? 167 LYS   L CG  1 
ATOM   20845 C  CD  . LYS   L  12 167 ? -12.411 -151.807 -3.635  1.00 155.51 ? 167 LYS   L CD  1 
ATOM   20846 C  CE  . LYS   L  12 167 ? -11.167 -152.271 -2.905  1.00 154.59 ? 167 LYS   L CE  1 
ATOM   20847 N  NZ  . LYS   L  12 167 ? -10.170 -152.841 -3.842  1.00 158.72 ? 167 LYS   L NZ  1 
ATOM   20848 N  N   . VAL   L  12 168 ? -14.619 -148.964 0.838   1.00 147.78 ? 168 VAL   L N   1 
ATOM   20849 C  CA  . VAL   L  12 168 ? -15.195 -147.744 1.478   1.00 144.55 ? 168 VAL   L CA  1 
ATOM   20850 C  C   . VAL   L  12 168 ? -14.878 -147.783 2.977   1.00 141.78 ? 168 VAL   L C   1 
ATOM   20851 O  O   . VAL   L  12 168 ? -15.349 -148.719 3.655   1.00 145.58 ? 168 VAL   L O   1 
ATOM   20852 C  CB  . VAL   L  12 168 ? -16.712 -147.644 1.227   1.00 143.03 ? 168 VAL   L CB  1 
ATOM   20853 C  CG1 . VAL   L  12 168 ? -17.353 -146.517 2.025   1.00 144.62 ? 168 VAL   L CG1 1 
ATOM   20854 C  CG2 . VAL   L  12 168 ? -17.019 -147.491 -0.253  1.00 142.36 ? 168 VAL   L CG2 1 
ATOM   20855 N  N   . LYS   L  12 169 ? -14.121 -146.797 3.465   1.00 138.22 ? 169 LYS   L N   1 
ATOM   20856 C  CA  . LYS   L  12 169 ? -13.765 -146.649 4.901   1.00 133.92 ? 169 LYS   L CA  1 
ATOM   20857 C  C   . LYS   L  12 169 ? -15.033 -146.280 5.678   1.00 128.95 ? 169 LYS   L C   1 
ATOM   20858 O  O   . LYS   L  12 169 ? -15.943 -145.677 5.075   1.00 125.79 ? 169 LYS   L O   1 
ATOM   20859 C  CB  . LYS   L  12 169 ? -12.676 -145.585 5.087   1.00 136.59 ? 169 LYS   L CB  1 
ATOM   20860 C  CG  . LYS   L  12 169 ? -11.365 -145.858 4.363   1.00 141.36 ? 169 LYS   L CG  1 
ATOM   20861 C  CD  . LYS   L  12 169 ? -10.365 -144.728 4.474   1.00 146.49 ? 169 LYS   L CD  1 
ATOM   20862 C  CE  . LYS   L  12 169 ? -9.619  -144.722 5.793   1.00 149.90 ? 169 LYS   L CE  1 
ATOM   20863 N  NZ  . LYS   L  12 169 ? -8.555  -143.690 5.822   1.00 153.26 ? 169 LYS   L NZ  1 
ATOM   20864 N  N   . LYS   L  12 170 ? -15.094 -146.655 6.958   1.00 128.54 ? 170 LYS   L N   1 
ATOM   20865 C  CA  . LYS   L  12 170 ? -16.089 -146.129 7.927   1.00 131.77 ? 170 LYS   L CA  1 
ATOM   20866 C  C   . LYS   L  12 170 ? -15.884 -144.620 8.025   1.00 131.68 ? 170 LYS   L C   1 
ATOM   20867 O  O   . LYS   L  12 170 ? -14.769 -144.171 8.283   1.00 134.73 ? 170 LYS   L O   1 
ATOM   20868 C  CB  . LYS   L  12 170 ? -15.912 -146.804 9.289   1.00 133.29 ? 170 LYS   L CB  1 
ATOM   20869 C  CG  . LYS   L  12 170 ? -16.981 -146.478 10.323  1.00 136.73 ? 170 LYS   L CG  1 
ATOM   20870 C  CD  . LYS   L  12 170 ? -16.862 -147.318 11.580  1.00 137.89 ? 170 LYS   L CD  1 
ATOM   20871 C  CE  . LYS   L  12 170 ? -18.142 -147.388 12.386  1.00 138.69 ? 170 LYS   L CE  1 
ATOM   20872 N  NZ  . LYS   L  12 170 ? -18.085 -146.522 13.587  1.00 137.21 ? 170 LYS   L NZ  1 
ATOM   20873 N  N   . PRO   L  12 171 ? -16.927 -143.787 7.803   1.00 132.43 ? 171 PRO   L N   1 
ATOM   20874 C  CA  . PRO   L  12 171 ? -16.749 -142.335 7.765   1.00 132.27 ? 171 PRO   L CA  1 
ATOM   20875 C  C   . PRO   L  12 171 ? -16.442 -141.728 9.143   1.00 135.58 ? 171 PRO   L C   1 
ATOM   20876 O  O   . PRO   L  12 171 ? -17.017 -142.178 10.120  1.00 142.63 ? 171 PRO   L O   1 
ATOM   20877 C  CB  . PRO   L  12 171 ? -18.099 -141.822 7.244   1.00 132.57 ? 171 PRO   L CB  1 
ATOM   20878 C  CG  . PRO   L  12 171 ? -19.089 -142.885 7.672   1.00 129.48 ? 171 PRO   L CG  1 
ATOM   20879 C  CD  . PRO   L  12 171 ? -18.325 -144.189 7.587   1.00 130.20 ? 171 PRO   L CD  1 
ATOM   20880 N  N   . LEU   L  12 172 ? -15.555 -140.726 9.180   1.00 135.28 ? 172 LEU   L N   1 
ATOM   20881 C  CA  . LEU   L  12 172 ? -15.211 -139.961 10.409  1.00 136.13 ? 172 LEU   L CA  1 
ATOM   20882 C  C   . LEU   L  12 172 ? -16.462 -139.196 10.856  1.00 135.97 ? 172 LEU   L C   1 
ATOM   20883 O  O   . LEU   L  12 172 ? -17.163 -138.658 9.978   1.00 143.60 ? 172 LEU   L O   1 
ATOM   20884 C  CB  . LEU   L  12 172 ? -14.055 -138.992 10.122  1.00 134.60 ? 172 LEU   L CB  1 
ATOM   20885 C  CG  . LEU   L  12 172 ? -12.746 -139.612 9.626   1.00 135.52 ? 172 LEU   L CG  1 
ATOM   20886 C  CD1 . LEU   L  12 172 ? -11.733 -138.528 9.282   1.00 132.93 ? 172 LEU   L CD1 1 
ATOM   20887 C  CD2 . LEU   L  12 172 ? -12.164 -140.573 10.654  1.00 133.02 ? 172 LEU   L CD2 1 
ATOM   20888 N  N   . LYS   L  12 173 ? -16.744 -139.167 12.160  1.00 136.34 ? 173 LYS   L N   1 
ATOM   20889 C  CA  . LYS   L  12 173 ? -17.811 -138.308 12.742  1.00 136.13 ? 173 LYS   L CA  1 
ATOM   20890 C  C   . LYS   L  12 173 ? -17.468 -137.973 14.198  1.00 134.27 ? 173 LYS   L C   1 
ATOM   20891 O  O   . LYS   L  12 173 ? -16.892 -138.838 14.893  1.00 134.32 ? 173 LYS   L O   1 
ATOM   20892 C  CB  . LYS   L  12 173 ? -19.186 -138.973 12.618  1.00 134.55 ? 173 LYS   L CB  1 
ATOM   20893 C  CG  . LYS   L  12 173 ? -19.405 -140.224 13.455  1.00 132.50 ? 173 LYS   L CG  1 
ATOM   20894 C  CD  . LYS   L  12 173 ? -20.867 -140.468 13.753  1.00 135.73 ? 173 LYS   L CD  1 
ATOM   20895 C  CE  . LYS   L  12 173 ? -21.112 -141.737 14.540  1.00 139.58 ? 173 LYS   L CE  1 
ATOM   20896 N  NZ  . LYS   L  12 173 ? -20.938 -142.944 13.698  1.00 147.00 ? 173 LYS   L NZ  1 
ATOM   20897 N  N   . TYR   L  12 174 ? -17.801 -136.750 14.620  1.00 135.24 ? 174 TYR   L N   1 
ATOM   20898 C  CA  . TYR   L  12 174 ? -17.650 -136.261 16.014  1.00 131.69 ? 174 TYR   L CA  1 
ATOM   20899 C  C   . TYR   L  12 174 ? -18.458 -137.175 16.941  1.00 123.88 ? 174 TYR   L C   1 
ATOM   20900 O  O   . TYR   L  12 174 ? -19.578 -137.587 16.564  1.00 116.50 ? 174 TYR   L O   1 
ATOM   20901 C  CB  . TYR   L  12 174 ? -18.101 -134.802 16.143  1.00 134.16 ? 174 TYR   L CB  1 
ATOM   20902 C  CG  . TYR   L  12 174 ? -17.149 -133.777 15.577  1.00 139.16 ? 174 TYR   L CG  1 
ATOM   20903 C  CD1 . TYR   L  12 174 ? -15.898 -133.571 16.141  1.00 139.86 ? 174 TYR   L CD1 1 
ATOM   20904 C  CD2 . TYR   L  12 174 ? -17.509 -132.982 14.499  1.00 139.88 ? 174 TYR   L CD2 1 
ATOM   20905 C  CE1 . TYR   L  12 174 ? -15.023 -132.620 15.637  1.00 143.11 ? 174 TYR   L CE1 1 
ATOM   20906 C  CE2 . TYR   L  12 174 ? -16.647 -132.027 13.984  1.00 142.54 ? 174 TYR   L CE2 1 
ATOM   20907 C  CZ  . TYR   L  12 174 ? -15.400 -131.844 14.555  1.00 144.80 ? 174 TYR   L CZ  1 
ATOM   20908 O  OH  . TYR   L  12 174 ? -14.547 -130.903 14.054  1.00 144.39 ? 174 TYR   L OH  1 
ATOM   20909 N  N   . LEU   L  12 175 ? -17.890 -137.493 18.106  1.00 121.65 ? 175 LEU   L N   1 
ATOM   20910 C  CA  . LEU   L  12 175 ? -18.552 -138.295 19.165  1.00 117.79 ? 175 LEU   L CA  1 
ATOM   20911 C  C   . LEU   L  12 175 ? -19.205 -137.342 20.168  1.00 115.19 ? 175 LEU   L C   1 
ATOM   20912 O  O   . LEU   L  12 175 ? -18.634 -136.263 20.417  1.00 112.00 ? 175 LEU   L O   1 
ATOM   20913 C  CB  . LEU   L  12 175 ? -17.515 -139.190 19.850  1.00 120.44 ? 175 LEU   L CB  1 
ATOM   20914 C  CG  . LEU   L  12 175 ? -17.061 -140.405 19.041  1.00 125.15 ? 175 LEU   L CG  1 
ATOM   20915 C  CD1 . LEU   L  12 175 ? -15.921 -140.045 18.100  1.00 126.76 ? 175 LEU   L CD1 1 
ATOM   20916 C  CD2 . LEU   L  12 175 ? -16.647 -141.541 19.963  1.00 127.89 ? 175 LEU   L CD2 1 
ATOM   20917 N  N   . SER   L  12 176 ? -20.361 -137.732 20.709  1.00 113.00 ? 176 SER   L N   1 
ATOM   20918 C  CA  . SER   L  12 176 ? -21.046 -137.034 21.827  1.00 116.83 ? 176 SER   L CA  1 
ATOM   20919 C  C   . SER   L  12 176 ? -20.209 -137.208 23.100  1.00 116.64 ? 176 SER   L C   1 
ATOM   20920 O  O   . SER   L  12 176 ? -19.425 -138.175 23.160  1.00 120.28 ? 176 SER   L O   1 
ATOM   20921 C  CB  . SER   L  12 176 ? -22.451 -137.547 22.003  1.00 115.50 ? 176 SER   L CB  1 
ATOM   20922 O  OG  . SER   L  12 176 ? -22.454 -138.934 22.308  1.00 113.42 ? 176 SER   L OG  1 
ATOM   20923 N  N   . VAL   L  12 177 ? -20.358 -136.301 24.071  1.00 122.95 ? 177 VAL   L N   1 
ATOM   20924 C  CA  . VAL   L  12 177 ? -19.593 -136.317 25.357  1.00 122.23 ? 177 VAL   L CA  1 
ATOM   20925 C  C   . VAL   L  12 177 ? -19.889 -137.622 26.106  1.00 122.52 ? 177 VAL   L C   1 
ATOM   20926 O  O   . VAL   L  12 177 ? -18.972 -138.122 26.785  1.00 122.07 ? 177 VAL   L O   1 
ATOM   20927 C  CB  . VAL   L  12 177 ? -19.892 -135.078 26.226  1.00 123.87 ? 177 VAL   L CB  1 
ATOM   20928 C  CG1 . VAL   L  12 177 ? -21.326 -135.059 26.739  1.00 125.83 ? 177 VAL   L CG1 1 
ATOM   20929 C  CG2 . VAL   L  12 177 ? -18.907 -134.954 27.379  1.00 120.96 ? 177 VAL   L CG2 1 
ATOM   20930 N  N   . GLU   L  12 178 ? -21.114 -138.147 25.982  1.00 124.29 ? 178 GLU   L N   1 
ATOM   20931 C  CA  . GLU   L  12 178 ? -21.544 -139.435 26.593  1.00 126.38 ? 178 GLU   L CA  1 
ATOM   20932 C  C   . GLU   L  12 178 ? -20.691 -140.570 26.008  1.00 122.11 ? 178 GLU   L C   1 
ATOM   20933 O  O   . GLU   L  12 178 ? -20.128 -141.350 26.804  1.00 116.13 ? 178 GLU   L O   1 
ATOM   20934 C  CB  . GLU   L  12 178 ? -23.037 -139.686 26.360  1.00 129.05 ? 178 GLU   L CB  1 
ATOM   20935 C  CG  . GLU   L  12 178 ? -23.953 -138.779 27.173  1.00 132.04 ? 178 GLU   L CG  1 
ATOM   20936 C  CD  . GLU   L  12 178 ? -24.181 -137.381 26.615  1.00 133.45 ? 178 GLU   L CD  1 
ATOM   20937 O  OE1 . GLU   L  12 178 ? -24.666 -136.514 27.373  1.00 129.65 ? 178 GLU   L OE1 1 
ATOM   20938 O  OE2 . GLU   L  12 178 ? -23.877 -137.156 25.426  1.00 140.34 ? 178 GLU   L OE2 1 
ATOM   20939 N  N   . GLU   L  12 179 ? -20.593 -140.637 24.673  1.00 123.78 ? 179 GLU   L N   1 
ATOM   20940 C  CA  . GLU   L  12 179 ? -19.815 -141.665 23.922  1.00 121.17 ? 179 GLU   L CA  1 
ATOM   20941 C  C   . GLU   L  12 179 ? -18.326 -141.565 24.277  1.00 118.35 ? 179 GLU   L C   1 
ATOM   20942 O  O   . GLU   L  12 179 ? -17.688 -142.624 24.432  1.00 119.59 ? 179 GLU   L O   1 
ATOM   20943 C  CB  . GLU   L  12 179 ? -20.002 -141.514 22.408  1.00 125.84 ? 179 GLU   L CB  1 
ATOM   20944 C  CG  . GLU   L  12 179 ? -21.044 -142.451 21.818  1.00 129.38 ? 179 GLU   L CG  1 
ATOM   20945 C  CD  . GLU   L  12 179 ? -20.764 -143.934 22.013  1.00 131.95 ? 179 GLU   L CD  1 
ATOM   20946 O  OE1 . GLU   L  12 179 ? -21.627 -144.626 22.592  1.00 135.35 ? 179 GLU   L OE1 1 
ATOM   20947 O  OE2 . GLU   L  12 179 ? -19.688 -144.397 21.581  1.00 134.85 ? 179 GLU   L OE2 1 
ATOM   20948 N  N   . VAL   L  12 180 ? -17.791 -140.345 24.382  1.00 110.44 ? 180 VAL   L N   1 
ATOM   20949 C  CA  . VAL   L  12 180 ? -16.347 -140.091 24.666  1.00 106.28 ? 180 VAL   L CA  1 
ATOM   20950 C  C   . VAL   L  12 180 ? -16.016 -140.601 26.075  1.00 105.87 ? 180 VAL   L C   1 
ATOM   20951 O  O   . VAL   L  12 180 ? -14.977 -141.270 26.218  1.00 107.89 ? 180 VAL   L O   1 
ATOM   20952 C  CB  . VAL   L  12 180 ? -15.986 -138.603 24.487  1.00 102.78 ? 180 VAL   L CB  1 
ATOM   20953 C  CG1 . VAL   L  12 180 ? -14.637 -138.262 25.100  1.00 100.50 ? 180 VAL   L CG1 1 
ATOM   20954 C  CG2 . VAL   L  12 180 ? -16.014 -138.203 23.022  1.00 103.30 ? 180 VAL   L CG2 1 
ATOM   20955 N  N   . ILE   L  12 181 ? -16.861 -140.309 27.069  1.00 106.00 ? 181 ILE   L N   1 
ATOM   20956 C  CA  . ILE   L  12 181 ? -16.620 -140.678 28.498  1.00 105.52 ? 181 ILE   L CA  1 
ATOM   20957 C  C   . ILE   L  12 181 ? -16.682 -142.204 28.647  1.00 104.44 ? 181 ILE   L C   1 
ATOM   20958 O  O   . ILE   L  12 181 ? -15.935 -142.727 29.495  1.00 104.38 ? 181 ILE   L O   1 
ATOM   20959 C  CB  . ILE   L  12 181 ? -17.585 -139.933 29.448  1.00 107.67 ? 181 ILE   L CB  1 
ATOM   20960 C  CG1 . ILE   L  12 181 ? -17.205 -138.450 29.546  1.00 106.02 ? 181 ILE   L CG1 1 
ATOM   20961 C  CG2 . ILE   L  12 181 ? -17.636 -140.601 30.819  1.00 109.25 ? 181 ILE   L CG2 1 
ATOM   20962 C  CD1 . ILE   L  12 181 ? -17.994 -137.654 30.561  1.00 105.16 ? 181 ILE   L CD1 1 
ATOM   20963 N  N   . LYS   L  12 182 ? -17.513 -142.890 27.850  1.00 104.01 ? 182 LYS   L N   1 
ATOM   20964 C  CA  . LYS   L  12 182 ? -17.576 -144.379 27.799  1.00 103.77 ? 182 LYS   L CA  1 
ATOM   20965 C  C   . LYS   L  12 182 ? -16.210 -144.932 27.371  1.00 95.60  ? 182 LYS   L C   1 
ATOM   20966 O  O   . LYS   L  12 182 ? -15.725 -145.865 28.038  1.00 91.59  ? 182 LYS   L O   1 
ATOM   20967 C  CB  . LYS   L  12 182 ? -18.664 -144.871 26.839  1.00 106.54 ? 182 LYS   L CB  1 
ATOM   20968 C  CG  . LYS   L  12 182 ? -20.092 -144.789 27.362  1.00 111.38 ? 182 LYS   L CG  1 
ATOM   20969 C  CD  . LYS   L  12 182 ? -21.108 -145.345 26.387  1.00 115.13 ? 182 LYS   L CD  1 
ATOM   20970 C  CE  . LYS   L  12 182 ? -22.541 -145.128 26.825  1.00 118.43 ? 182 LYS   L CE  1 
ATOM   20971 N  NZ  . LYS   L  12 182 ? -23.492 -145.430 25.730  1.00 121.40 ? 182 LYS   L NZ  1 
ATOM   20972 N  N   . LEU   L  12 183 ? -15.620 -144.373 26.308  1.00 95.05  ? 183 LEU   L N   1 
ATOM   20973 C  CA  . LEU   L  12 183 ? -14.298 -144.790 25.760  1.00 96.41  ? 183 LEU   L CA  1 
ATOM   20974 C  C   . LEU   L  12 183 ? -13.196 -144.529 26.791  1.00 97.72  ? 183 LEU   L C   1 
ATOM   20975 O  O   . LEU   L  12 183 ? -12.328 -145.407 26.944  1.00 98.25  ? 183 LEU   L O   1 
ATOM   20976 C  CB  . LEU   L  12 183 ? -13.998 -144.027 24.468  1.00 98.75  ? 183 LEU   L CB  1 
ATOM   20977 C  CG  . LEU   L  12 183 ? -14.912 -144.325 23.281  1.00 100.62 ? 183 LEU   L CG  1 
ATOM   20978 C  CD1 . LEU   L  12 183 ? -14.612 -143.376 22.132  1.00 101.92 ? 183 LEU   L CD1 1 
ATOM   20979 C  CD2 . LEU   L  12 183 ? -14.772 -145.770 22.826  1.00 100.39 ? 183 LEU   L CD2 1 
ATOM   20980 N  N   . VAL   L  12 184 ? -13.215 -143.362 27.445  1.00 96.82  ? 184 VAL   L N   1 
ATOM   20981 C  CA  . VAL   L  12 184 ? -12.241 -142.988 28.516  1.00 97.33  ? 184 VAL   L CA  1 
ATOM   20982 C  C   . VAL   L  12 184 ? -12.296 -144.055 29.620  1.00 100.32 ? 184 VAL   L C   1 
ATOM   20983 O  O   . VAL   L  12 184 ? -11.223 -144.577 29.990  1.00 99.30  ? 184 VAL   L O   1 
ATOM   20984 C  CB  . VAL   L  12 184 ? -12.509 -141.574 29.069  1.00 96.61  ? 184 VAL   L CB  1 
ATOM   20985 C  CG1 . VAL   L  12 184 ? -11.740 -141.301 30.356  1.00 93.28  ? 184 VAL   L CG1 1 
ATOM   20986 C  CG2 . VAL   L  12 184 ? -12.201 -140.499 28.038  1.00 97.35  ? 184 VAL   L CG2 1 
ATOM   20987 N  N   . ARG   L  12 185 ? -13.498 -144.378 30.110  1.00 102.33 ? 185 ARG   L N   1 
ATOM   20988 C  CA  . ARG   L  12 185 ? -13.714 -145.300 31.259  1.00 104.43 ? 185 ARG   L CA  1 
ATOM   20989 C  C   . ARG   L  12 185 ? -13.266 -146.719 30.885  1.00 105.60 ? 185 ARG   L C   1 
ATOM   20990 O  O   . ARG   L  12 185 ? -12.626 -147.372 31.734  1.00 109.27 ? 185 ARG   L O   1 
ATOM   20991 C  CB  . ARG   L  12 185 ? -15.178 -145.268 31.713  1.00 105.82 ? 185 ARG   L CB  1 
ATOM   20992 C  CG  . ARG   L  12 185 ? -15.561 -144.007 32.475  1.00 107.56 ? 185 ARG   L CG  1 
ATOM   20993 C  CD  . ARG   L  12 185 ? -16.913 -144.123 33.150  1.00 111.10 ? 185 ARG   L CD  1 
ATOM   20994 N  NE  . ARG   L  12 185 ? -16.898 -145.116 34.216  1.00 113.38 ? 185 ARG   L NE  1 
ATOM   20995 C  CZ  . ARG   L  12 185 ? -17.944 -145.444 34.970  1.00 115.99 ? 185 ARG   L CZ  1 
ATOM   20996 N  NH1 . ARG   L  12 185 ? -19.116 -144.857 34.787  1.00 116.89 ? 185 ARG   L NH1 1 
ATOM   20997 N  NH2 . ARG   L  12 185 ? -17.811 -146.363 35.911  1.00 119.97 ? 185 ARG   L NH2 1 
ATOM   20998 N  N   . ASP   L  12 186 ? -13.585 -147.178 29.669  1.00 104.73 ? 186 ASP   L N   1 
ATOM   20999 C  CA  . ASP   L  12 186 ? -13.194 -148.521 29.157  1.00 104.17 ? 186 ASP   L CA  1 
ATOM   21000 C  C   . ASP   L  12 186 ? -11.684 -148.555 28.884  1.00 103.46 ? 186 ASP   L C   1 
ATOM   21001 O  O   . ASP   L  12 186 ? -11.078 -149.617 29.114  1.00 106.04 ? 186 ASP   L O   1 
ATOM   21002 C  CB  . ASP   L  12 186 ? -13.994 -148.911 27.911  1.00 103.83 ? 186 ASP   L CB  1 
ATOM   21003 C  CG  . ASP   L  12 186 ? -15.408 -149.387 28.205  1.00 105.87 ? 186 ASP   L CG  1 
ATOM   21004 O  OD1 . ASP   L  12 186 ? -15.635 -149.910 29.315  1.00 109.86 ? 186 ASP   L OD1 1 
ATOM   21005 O  OD2 . ASP   L  12 186 ? -16.272 -149.236 27.319  1.00 103.85 ? 186 ASP   L OD2 1 
ATOM   21006 N  N   . SER   L  12 187 ? -11.105 -147.447 28.410  1.00 101.71 ? 187 SER   L N   1 
ATOM   21007 C  CA  . SER   L  12 187 ? -9.648  -147.295 28.144  1.00 101.71 ? 187 SER   L CA  1 
ATOM   21008 C  C   . SER   L  12 187 ? -8.846  -147.503 29.434  1.00 101.81 ? 187 SER   L C   1 
ATOM   21009 O  O   . SER   L  12 187 ? -7.814  -148.204 29.378  1.00 98.61  ? 187 SER   L O   1 
ATOM   21010 C  CB  . SER   L  12 187 ? -9.335  -145.955 27.529  1.00 99.56  ? 187 SER   L CB  1 
ATOM   21011 O  OG  . SER   L  12 187 ? -9.783  -145.901 26.185  1.00 98.39  ? 187 SER   L OG  1 
ATOM   21012 N  N   . PHE   L  12 188 ? -9.308  -146.916 30.545  1.00 105.53 ? 188 PHE   L N   1 
ATOM   21013 C  CA  . PHE   L  12 188 ? -8.591  -146.877 31.849  1.00 104.80 ? 188 PHE   L CA  1 
ATOM   21014 C  C   . PHE   L  12 188 ? -8.780  -148.201 32.602  1.00 105.50 ? 188 PHE   L C   1 
ATOM   21015 O  O   . PHE   L  12 188 ? -7.804  -148.656 33.234  1.00 109.37 ? 188 PHE   L O   1 
ATOM   21016 C  CB  . PHE   L  12 188 ? -9.018  -145.656 32.670  1.00 104.01 ? 188 PHE   L CB  1 
ATOM   21017 C  CG  . PHE   L  12 188 ? -8.141  -144.450 32.453  1.00 103.15 ? 188 PHE   L CG  1 
ATOM   21018 C  CD1 . PHE   L  12 188 ? -8.457  -143.499 31.495  1.00 103.51 ? 188 PHE   L CD1 1 
ATOM   21019 C  CD2 . PHE   L  12 188 ? -6.978  -144.284 33.189  1.00 104.20 ? 188 PHE   L CD2 1 
ATOM   21020 C  CE1 . PHE   L  12 188 ? -7.639  -142.398 31.294  1.00 103.95 ? 188 PHE   L CE1 1 
ATOM   21021 C  CE2 . PHE   L  12 188 ? -6.161  -143.182 32.986  1.00 104.02 ? 188 PHE   L CE2 1 
ATOM   21022 C  CZ  . PHE   L  12 188 ? -6.492  -142.241 32.039  1.00 103.93 ? 188 PHE   L CZ  1 
ATOM   21023 N  N   . THR   L  12 189 ? -9.971  -148.808 32.539  1.00 101.06 ? 189 THR   L N   1 
ATOM   21024 C  CA  . THR   L  12 189 ? -10.262 -150.116 33.190  1.00 100.50 ? 189 THR   L CA  1 
ATOM   21025 C  C   . THR   L  12 189 ? -9.469  -151.221 32.483  1.00 99.99  ? 189 THR   L C   1 
ATOM   21026 O  O   . THR   L  12 189 ? -9.028  -152.154 33.179  1.00 100.91 ? 189 THR   L O   1 
ATOM   21027 C  CB  . THR   L  12 189 ? -11.761 -150.434 33.222  1.00 102.49 ? 189 THR   L CB  1 
ATOM   21028 O  OG1 . THR   L  12 189 ? -12.297 -150.227 31.916  1.00 106.60 ? 189 THR   L OG1 1 
ATOM   21029 C  CG2 . THR   L  12 189 ? -12.510 -149.596 34.235  1.00 101.68 ? 189 THR   L CG2 1 
ATOM   21030 N  N   . SER   L  12 190 ? -9.292  -151.111 31.163  1.00 93.59  ? 190 SER   L N   1 
ATOM   21031 C  CA  . SER   L  12 190 ? -8.438  -152.012 30.342  1.00 93.47  ? 190 SER   L CA  1 
ATOM   21032 C  C   . SER   L  12 190 ? -6.968  -151.835 30.743  1.00 91.49  ? 190 SER   L C   1 
ATOM   21033 O  O   . SER   L  12 190 ? -6.300  -152.846 31.003  1.00 89.25  ? 190 SER   L O   1 
ATOM   21034 C  CB  . SER   L  12 190 ? -8.633  -151.766 28.868  1.00 92.78  ? 190 SER   L CB  1 
ATOM   21035 O  OG  . SER   L  12 190 ? -9.927  -152.179 28.451  1.00 92.26  ? 190 SER   L OG  1 
ATOM   21036 N  N   . ALA   L  12 191 ? -6.492  -150.589 30.786  1.00 92.58  ? 191 ALA   L N   1 
ATOM   21037 C  CA  . ALA   L  12 191 ? -5.114  -150.217 31.186  1.00 94.28  ? 191 ALA   L CA  1 
ATOM   21038 C  C   . ALA   L  12 191 ? -4.823  -150.727 32.605  1.00 95.91  ? 191 ALA   L C   1 
ATOM   21039 O  O   . ALA   L  12 191 ? -3.723  -151.280 32.818  1.00 93.46  ? 191 ALA   L O   1 
ATOM   21040 C  CB  . ALA   L  12 191 ? -4.938  -148.719 31.089  1.00 95.11  ? 191 ALA   L CB  1 
ATOM   21041 N  N   . THR   L  12 192 ? -5.774  -150.551 33.531  1.00 97.67  ? 192 THR   L N   1 
ATOM   21042 C  CA  . THR   L  12 192 ? -5.655  -150.920 34.970  1.00 99.48  ? 192 THR   L CA  1 
ATOM   21043 C  C   . THR   L  12 192 ? -5.423  -152.430 35.112  1.00 99.80  ? 192 THR   L C   1 
ATOM   21044 O  O   . THR   L  12 192 ? -4.639  -152.821 36.007  1.00 93.69  ? 192 THR   L O   1 
ATOM   21045 C  CB  . THR   L  12 192 ? -6.897  -150.490 35.761  1.00 102.18 ? 192 THR   L CB  1 
ATOM   21046 O  OG1 . THR   L  12 192 ? -7.035  -149.075 35.632  1.00 100.95 ? 192 THR   L OG1 1 
ATOM   21047 C  CG2 . THR   L  12 192 ? -6.823  -150.868 37.225  1.00 104.70 ? 192 THR   L CG2 1 
ATOM   21048 N  N   . GLU   L  12 193 ? -6.091  -153.233 34.276  1.00 101.19 ? 193 GLU   L N   1 
ATOM   21049 C  CA  . GLU   L  12 193 ? -6.018  -154.719 34.293  1.00 101.44 ? 193 GLU   L CA  1 
ATOM   21050 C  C   . GLU   L  12 193 ? -4.590  -155.189 33.994  1.00 100.67 ? 193 GLU   L C   1 
ATOM   21051 O  O   . GLU   L  12 193 ? -4.142  -156.141 34.664  1.00 98.29  ? 193 GLU   L O   1 
ATOM   21052 C  CB  . GLU   L  12 193 ? -6.976  -155.336 33.270  1.00 105.61 ? 193 GLU   L CB  1 
ATOM   21053 C  CG  . GLU   L  12 193 ? -8.434  -155.267 33.679  1.00 110.51 ? 193 GLU   L CG  1 
ATOM   21054 C  CD  . GLU   L  12 193 ? -8.794  -156.163 34.852  1.00 113.21 ? 193 GLU   L CD  1 
ATOM   21055 O  OE1 . GLU   L  12 193 ? -9.258  -155.627 35.878  1.00 119.09 ? 193 GLU   L OE1 1 
ATOM   21056 O  OE2 . GLU   L  12 193 ? -8.615  -157.393 34.736  1.00 112.79 ? 193 GLU   L OE2 1 
ATOM   21057 N  N   . ARG   L  12 194 ? -3.912  -154.558 33.029  1.00 98.17  ? 194 ARG   L N   1 
ATOM   21058 C  CA  . ARG   L  12 194 ? -2.666  -155.095 32.416  1.00 99.68  ? 194 ARG   L CA  1 
ATOM   21059 C  C   . ARG   L  12 194 ? -1.444  -154.213 32.693  1.00 98.56  ? 194 ARG   L C   1 
ATOM   21060 O  O   . ARG   L  12 194 ? -0.344  -154.625 32.279  1.00 106.26 ? 194 ARG   L O   1 
ATOM   21061 C  CB  . ARG   L  12 194 ? -2.862  -155.268 30.909  1.00 101.70 ? 194 ARG   L CB  1 
ATOM   21062 C  CG  . ARG   L  12 194 ? -3.844  -156.373 30.551  1.00 108.52 ? 194 ARG   L CG  1 
ATOM   21063 C  CD  . ARG   L  12 194 ? -3.305  -157.748 30.903  1.00 111.63 ? 194 ARG   L CD  1 
ATOM   21064 N  NE  . ARG   L  12 194 ? -4.189  -158.822 30.474  1.00 116.38 ? 194 ARG   L NE  1 
ATOM   21065 C  CZ  . ARG   L  12 194 ? -3.907  -160.117 30.569  1.00 119.91 ? 194 ARG   L CZ  1 
ATOM   21066 N  NH1 . ARG   L  12 194 ? -2.751  -160.519 31.074  1.00 122.99 ? 194 ARG   L NH1 1 
ATOM   21067 N  NH2 . ARG   L  12 194 ? -4.785  -161.013 30.151  1.00 127.88 ? 194 ARG   L NH2 1 
ATOM   21068 N  N   . HIS   L  12 195 ? -1.605  -153.069 33.366  1.00 97.68  ? 195 HIS   L N   1 
ATOM   21069 C  CA  . HIS   L  12 195 ? -0.475  -152.214 33.814  1.00 95.44  ? 195 HIS   L CA  1 
ATOM   21070 C  C   . HIS   L  12 195 ? -0.558  -152.048 35.337  1.00 93.06  ? 195 HIS   L C   1 
ATOM   21071 O  O   . HIS   L  12 195 ? -1.664  -151.766 35.846  1.00 90.07  ? 195 HIS   L O   1 
ATOM   21072 C  CB  . HIS   L  12 195 ? -0.449  -150.895 33.028  1.00 95.26  ? 195 HIS   L CB  1 
ATOM   21073 C  CG  . HIS   L  12 195 ? 0.915   -150.293 32.944  1.00 96.94  ? 195 HIS   L CG  1 
ATOM   21074 N  ND1 . HIS   L  12 195 ? 1.652   -150.270 31.774  1.00 97.53  ? 195 HIS   L ND1 1 
ATOM   21075 C  CD2 . HIS   L  12 195 ? 1.689   -149.715 33.887  1.00 98.10  ? 195 HIS   L CD2 1 
ATOM   21076 C  CE1 . HIS   L  12 195 ? 2.815   -149.689 32.002  1.00 97.86  ? 195 HIS   L CE1 1 
ATOM   21077 N  NE2 . HIS   L  12 195 ? 2.864   -149.344 33.293  1.00 96.73  ? 195 HIS   L NE2 1 
ATOM   21078 N  N   . ILE   L  12 196 ? 0.569   -152.251 36.029  1.00 91.65  ? 196 ILE   L N   1 
ATOM   21079 C  CA  . ILE   L  12 196 ? 0.655   -152.284 37.521  1.00 96.39  ? 196 ILE   L CA  1 
ATOM   21080 C  C   . ILE   L  12 196 ? 0.640   -150.855 38.084  1.00 99.28  ? 196 ILE   L C   1 
ATOM   21081 O  O   . ILE   L  12 196 ? 0.148   -150.687 39.215  1.00 105.27 ? 196 ILE   L O   1 
ATOM   21082 C  CB  . ILE   L  12 196 ? 1.888   -153.089 37.992  1.00 94.96  ? 196 ILE   L CB  1 
ATOM   21083 C  CG1 . ILE   L  12 196 ? 3.216   -152.452 37.568  1.00 95.71  ? 196 ILE   L CG1 1 
ATOM   21084 C  CG2 . ILE   L  12 196 ? 1.785   -154.533 37.528  1.00 95.32  ? 196 ILE   L CG2 1 
ATOM   21085 C  CD1 . ILE   L  12 196 ? 4.432   -153.055 38.240  1.00 96.77  ? 196 ILE   L CD1 1 
ATOM   21086 N  N   . GLN   L  12 197 ? 1.149   -149.875 37.325  1.00 100.50 ? 197 GLN   L N   1 
ATOM   21087 C  CA  . GLN   L  12 197 ? 1.289   -148.447 37.732  1.00 98.80  ? 197 GLN   L CA  1 
ATOM   21088 C  C   . GLN   L  12 197 ? -0.027  -147.676 37.547  1.00 99.26  ? 197 GLN   L C   1 
ATOM   21089 O  O   . GLN   L  12 197 ? -0.070  -146.504 37.973  1.00 104.54 ? 197 GLN   L O   1 
ATOM   21090 C  CB  . GLN   L  12 197 ? 2.392   -147.763 36.920  1.00 96.79  ? 197 GLN   L CB  1 
ATOM   21091 C  CG  . GLN   L  12 197 ? 3.769   -148.382 37.114  1.00 96.32  ? 197 GLN   L CG  1 
ATOM   21092 C  CD  . GLN   L  12 197 ? 4.825   -147.756 36.234  1.00 94.20  ? 197 GLN   L CD  1 
ATOM   21093 O  OE1 . GLN   L  12 197 ? 4.529   -147.106 35.234  1.00 92.92  ? 197 GLN   L OE1 1 
ATOM   21094 N  NE2 . GLN   L  12 197 ? 6.079   -147.954 36.603  1.00 96.30  ? 197 GLN   L NE2 1 
ATOM   21095 N  N   . VAL   L  12 198 ? -1.048  -148.287 36.936  1.00 95.23  ? 198 VAL   L N   1 
ATOM   21096 C  CA  . VAL   L  12 198 ? -2.360  -147.636 36.637  1.00 96.58  ? 198 VAL   L CA  1 
ATOM   21097 C  C   . VAL   L  12 198 ? -3.446  -148.256 37.525  1.00 99.61  ? 198 VAL   L C   1 
ATOM   21098 O  O   . VAL   L  12 198 ? -3.545  -149.499 37.544  1.00 99.86  ? 198 VAL   L O   1 
ATOM   21099 C  CB  . VAL   L  12 198 ? -2.716  -147.769 35.144  1.00 98.20  ? 198 VAL   L CB  1 
ATOM   21100 C  CG1 . VAL   L  12 198 ? -4.086  -147.184 34.829  1.00 98.83  ? 198 VAL   L CG1 1 
ATOM   21101 C  CG2 . VAL   L  12 198 ? -1.651  -147.143 34.256  1.00 97.87  ? 198 VAL   L CG2 1 
ATOM   21102 N  N   . GLY   L  12 199 ? -4.235  -147.419 38.213  1.00 97.81  ? 199 GLY   L N   1 
ATOM   21103 C  CA  . GLY   L  12 199 ? -5.405  -147.853 39.004  1.00 98.36  ? 199 GLY   L CA  1 
ATOM   21104 C  C   . GLY   L  12 199 ? -5.864  -146.812 40.015  1.00 97.69  ? 199 GLY   L C   1 
ATOM   21105 O  O   . GLY   L  12 199 ? -5.611  -145.613 39.794  1.00 93.22  ? 199 GLY   L O   1 
ATOM   21106 N  N   . ASP   L  12 200 ? -6.545  -147.275 41.071  1.00 100.21 ? 200 ASP   L N   1 
ATOM   21107 C  CA  . ASP   L  12 200 ? -7.024  -146.495 42.248  1.00 100.95 ? 200 ASP   L CA  1 
ATOM   21108 C  C   . ASP   L  12 200 ? -8.240  -145.639 41.870  1.00 98.11  ? 200 ASP   L C   1 
ATOM   21109 O  O   . ASP   L  12 200 ? -9.333  -145.912 42.408  1.00 92.14  ? 200 ASP   L O   1 
ATOM   21110 C  CB  . ASP   L  12 200 ? -5.895  -145.676 42.879  1.00 104.23 ? 200 ASP   L CB  1 
ATOM   21111 C  CG  . ASP   L  12 200 ? -4.825  -146.532 43.537  1.00 107.78 ? 200 ASP   L CG  1 
ATOM   21112 O  OD1 . ASP   L  12 200 ? -5.188  -147.545 44.167  1.00 109.85 ? 200 ASP   L OD1 1 
ATOM   21113 O  OD2 . ASP   L  12 200 ? -3.632  -146.186 43.411  1.00 110.00 ? 200 ASP   L OD2 1 
ATOM   21114 N  N   . GLY   L  12 201 ? -8.065  -144.639 41.000  1.00 97.50  ? 201 GLY   L N   1 
ATOM   21115 C  CA  . GLY   L  12 201 ? -9.145  -143.714 40.603  1.00 100.54 ? 201 GLY   L CA  1 
ATOM   21116 C  C   . GLY   L  12 201 ? -8.892  -143.051 39.259  1.00 97.99  ? 201 GLY   L C   1 
ATOM   21117 O  O   . GLY   L  12 201 ? -7.724  -143.002 38.824  1.00 94.70  ? 201 GLY   L O   1 
ATOM   21118 N  N   . LEU   L  12 202 ? -9.962  -142.546 38.637  1.00 100.10 ? 202 LEU   L N   1 
ATOM   21119 C  CA  . LEU   L  12 202 ? -9.942  -141.819 37.340  1.00 102.16 ? 202 LEU   L CA  1 
ATOM   21120 C  C   . LEU   L  12 202 ? -10.630 -140.459 37.514  1.00 102.86 ? 202 LEU   L C   1 
ATOM   21121 O  O   . LEU   L  12 202 ? -11.814 -140.442 37.909  1.00 99.18  ? 202 LEU   L O   1 
ATOM   21122 C  CB  . LEU   L  12 202 ? -10.666 -142.669 36.292  1.00 100.93 ? 202 LEU   L CB  1 
ATOM   21123 C  CG  . LEU   L  12 202 ? -10.980 -141.966 34.973  1.00 100.79 ? 202 LEU   L CG  1 
ATOM   21124 C  CD1 . LEU   L  12 202 ? -9.704  -141.523 34.275  1.00 99.29  ? 202 LEU   L CD1 1 
ATOM   21125 C  CD2 . LEU   L  12 202 ? -11.805 -142.864 34.066  1.00 101.22 ? 202 LEU   L CD2 1 
ATOM   21126 N  N   . GLU   L  12 203 ? -9.916  -139.367 37.220  1.00 104.19 ? 203 GLU   L N   1 
ATOM   21127 C  CA  . GLU   L  12 203 ? -10.459 -137.983 37.250  1.00 104.30 ? 203 GLU   L CA  1 
ATOM   21128 C  C   . GLU   L  12 203 ? -10.455 -137.419 35.826  1.00 103.27 ? 203 GLU   L C   1 
ATOM   21129 O  O   . GLU   L  12 203 ? -9.362  -137.315 35.232  1.00 100.13 ? 203 GLU   L O   1 
ATOM   21130 C  CB  . GLU   L  12 203 ? -9.653  -137.100 38.204  1.00 106.76 ? 203 GLU   L CB  1 
ATOM   21131 C  CG  . GLU   L  12 203 ? -10.354 -135.798 38.551  1.00 108.73 ? 203 GLU   L CG  1 
ATOM   21132 C  CD  . GLU   L  12 203 ? -9.946  -135.201 39.886  1.00 110.98 ? 203 GLU   L CD  1 
ATOM   21133 O  OE1 . GLU   L  12 203 ? -10.773 -135.230 40.819  1.00 113.34 ? 203 GLU   L OE1 1 
ATOM   21134 O  OE2 . GLU   L  12 203 ? -8.804  -134.708 39.988  1.00 107.05 ? 203 GLU   L OE2 1 
ATOM   21135 N  N   . ILE   L  12 204 ? -11.639 -137.085 35.306  1.00 104.71 ? 204 ILE   L N   1 
ATOM   21136 C  CA  . ILE   L  12 204 ? -11.837 -136.493 33.950  1.00 108.10 ? 204 ILE   L CA  1 
ATOM   21137 C  C   . ILE   L  12 204 ? -12.222 -135.021 34.121  1.00 105.21 ? 204 ILE   L C   1 
ATOM   21138 O  O   . ILE   L  12 204 ? -13.114 -134.742 34.949  1.00 102.79 ? 204 ILE   L O   1 
ATOM   21139 C  CB  . ILE   L  12 204 ? -12.908 -137.263 33.150  1.00 112.66 ? 204 ILE   L CB  1 
ATOM   21140 C  CG1 . ILE   L  12 204 ? -12.723 -138.781 33.242  1.00 114.93 ? 204 ILE   L CG1 1 
ATOM   21141 C  CG2 . ILE   L  12 204 ? -12.933 -136.783 31.705  1.00 115.11 ? 204 ILE   L CG2 1 
ATOM   21142 C  CD1 . ILE   L  12 204 ? -13.919 -139.580 32.769  1.00 118.21 ? 204 ILE   L CD1 1 
ATOM   21143 N  N   . LEU   L  12 205 ? -11.569 -134.129 33.369  1.00 105.02 ? 205 LEU   L N   1 
ATOM   21144 C  CA  . LEU   L  12 205 ? -11.933 -132.690 33.263  1.00 105.58 ? 205 LEU   L CA  1 
ATOM   21145 C  C   . LEU   L  12 205 ? -12.521 -132.432 31.871  1.00 105.49 ? 205 LEU   L C   1 
ATOM   21146 O  O   . LEU   L  12 205 ? -11.802 -132.651 30.876  1.00 104.45 ? 205 LEU   L O   1 
ATOM   21147 C  CB  . LEU   L  12 205 ? -10.703 -131.815 33.526  1.00 103.79 ? 205 LEU   L CB  1 
ATOM   21148 C  CG  . LEU   L  12 205 ? -10.433 -131.491 34.996  1.00 102.95 ? 205 LEU   L CG  1 
ATOM   21149 C  CD1 . LEU   L  12 205 ? -9.856  -132.695 35.725  1.00 105.34 ? 205 LEU   L CD1 1 
ATOM   21150 C  CD2 . LEU   L  12 205 ? -9.503  -130.297 35.132  1.00 100.66 ? 205 LEU   L CD2 1 
ATOM   21151 N  N   . ILE   L  12 206 ? -13.783 -131.994 31.823  1.00 107.27 ? 206 ILE   L N   1 
ATOM   21152 C  CA  . ILE   L  12 206 ? -14.562 -131.742 30.574  1.00 109.06 ? 206 ILE   L CA  1 
ATOM   21153 C  C   . ILE   L  12 206 ? -14.613 -130.229 30.350  1.00 108.21 ? 206 ILE   L C   1 
ATOM   21154 O  O   . ILE   L  12 206 ? -14.961 -129.510 31.306  1.00 113.46 ? 206 ILE   L O   1 
ATOM   21155 C  CB  . ILE   L  12 206 ? -15.977 -132.349 30.665  1.00 111.78 ? 206 ILE   L CB  1 
ATOM   21156 C  CG1 . ILE   L  12 206 ? -15.949 -133.806 31.138  1.00 114.51 ? 206 ILE   L CG1 1 
ATOM   21157 C  CG2 . ILE   L  12 206 ? -16.710 -132.200 29.339  1.00 112.31 ? 206 ILE   L CG2 1 
ATOM   21158 C  CD1 . ILE   L  12 206 ? -16.143 -133.985 32.630  1.00 117.18 ? 206 ILE   L CD1 1 
ATOM   21159 N  N   . VAL   L  12 207 ? -14.294 -129.776 29.134  1.00 104.72 ? 207 VAL   L N   1 
ATOM   21160 C  CA  . VAL   L  12 207 ? -14.195 -128.330 28.777  1.00 104.76 ? 207 VAL   L CA  1 
ATOM   21161 C  C   . VAL   L  12 207 ? -15.213 -128.002 27.680  1.00 102.86 ? 207 VAL   L C   1 
ATOM   21162 O  O   . VAL   L  12 207 ? -15.019 -128.457 26.538  1.00 102.05 ? 207 VAL   L O   1 
ATOM   21163 C  CB  . VAL   L  12 207 ? -12.773 -127.952 28.326  1.00 102.39 ? 207 VAL   L CB  1 
ATOM   21164 C  CG1 . VAL   L  12 207 ? -12.682 -126.472 27.984  1.00 104.20 ? 207 VAL   L CG1 1 
ATOM   21165 C  CG2 . VAL   L  12 207 ? -11.733 -128.323 29.370  1.00 99.67  ? 207 VAL   L CG2 1 
ATOM   21166 N  N   . THR   L  12 208 ? -16.231 -127.209 28.023  1.00 106.74 ? 208 THR   L N   1 
ATOM   21167 C  CA  . THR   L  12 208 ? -17.195 -126.587 27.078  1.00 110.25 ? 208 THR   L CA  1 
ATOM   21168 C  C   . THR   L  12 208 ? -17.079 -125.065 27.200  1.00 111.55 ? 208 THR   L C   1 
ATOM   21169 O  O   . THR   L  12 208 ? -16.300 -124.604 28.057  1.00 108.11 ? 208 THR   L O   1 
ATOM   21170 C  CB  . THR   L  12 208 ? -18.624 -127.065 27.355  1.00 113.23 ? 208 THR   L CB  1 
ATOM   21171 O  OG1 . THR   L  12 208 ? -19.007 -126.597 28.649  1.00 118.77 ? 208 THR   L OG1 1 
ATOM   21172 C  CG2 . THR   L  12 208 ? -18.759 -128.570 27.298  1.00 112.87 ? 208 THR   L CG2 1 
ATOM   21173 N  N   . LYS   L  12 209 ? -17.835 -124.322 26.385  1.00 114.54 ? 209 LYS   L N   1 
ATOM   21174 C  CA  . LYS   L  12 209 ? -17.874 -122.834 26.405  1.00 114.80 ? 209 LYS   L CA  1 
ATOM   21175 C  C   . LYS   L  12 209 ? -18.395 -122.344 27.765  1.00 116.45 ? 209 LYS   L C   1 
ATOM   21176 O  O   . LYS   L  12 209 ? -18.159 -121.162 28.081  1.00 117.40 ? 209 LYS   L O   1 
ATOM   21177 C  CB  . LYS   L  12 209 ? -18.714 -122.292 25.241  1.00 115.05 ? 209 LYS   L CB  1 
ATOM   21178 C  CG  . LYS   L  12 209 ? -20.164 -122.758 25.183  1.00 119.15 ? 209 LYS   L CG  1 
ATOM   21179 C  CD  . LYS   L  12 209 ? -20.996 -121.993 24.172  1.00 120.37 ? 209 LYS   L CD  1 
ATOM   21180 C  CE  . LYS   L  12 209 ? -22.348 -122.621 23.902  1.00 125.48 ? 209 LYS   L CE  1 
ATOM   21181 N  NZ  . LYS   L  12 209 ? -23.222 -122.592 25.098  1.00 127.79 ? 209 LYS   L NZ  1 
ATOM   21182 N  N   . ASP   L  12 210 ? -19.054 -123.218 28.541  1.00 118.35 ? 210 ASP   L N   1 
ATOM   21183 C  CA  . ASP   L  12 210 ? -19.650 -122.898 29.869  1.00 119.93 ? 210 ASP   L CA  1 
ATOM   21184 C  C   . ASP   L  12 210 ? -18.616 -123.046 30.995  1.00 115.27 ? 210 ASP   L C   1 
ATOM   21185 O  O   . ASP   L  12 210 ? -18.932 -122.619 32.124  1.00 115.86 ? 210 ASP   L O   1 
ATOM   21186 C  CB  . ASP   L  12 210 ? -20.872 -123.775 30.157  1.00 124.32 ? 210 ASP   L CB  1 
ATOM   21187 C  CG  . ASP   L  12 210 ? -22.065 -123.491 29.259  1.00 132.23 ? 210 ASP   L CG  1 
ATOM   21188 O  OD1 . ASP   L  12 210 ? -21.880 -122.802 28.235  1.00 134.83 ? 210 ASP   L OD1 1 
ATOM   21189 O  OD2 . ASP   L  12 210 ? -23.173 -123.957 29.595  1.00 137.13 ? 210 ASP   L OD2 1 
ATOM   21190 N  N   . GLY   L  12 211 ? -17.445 -123.632 30.723  1.00 112.18 ? 211 GLY   L N   1 
ATOM   21191 C  CA  . GLY   L  12 211 ? -16.338 -123.719 31.698  1.00 112.00 ? 211 GLY   L CA  1 
ATOM   21192 C  C   . GLY   L  12 211 ? -15.746 -125.114 31.788  1.00 111.11 ? 211 GLY   L C   1 
ATOM   21193 O  O   . GLY   L  12 211 ? -15.773 -125.839 30.773  1.00 113.35 ? 211 GLY   L O   1 
ATOM   21194 N  N   . VAL   L  12 212 ? -15.226 -125.470 32.968  1.00 108.39 ? 212 VAL   L N   1 
ATOM   21195 C  CA  . VAL   L  12 212 ? -14.528 -126.761 33.242  1.00 104.73 ? 212 VAL   L CA  1 
ATOM   21196 C  C   . VAL   L  12 212 ? -15.318 -127.531 34.305  1.00 105.26 ? 212 VAL   L C   1 
ATOM   21197 O  O   . VAL   L  12 212 ? -15.487 -126.991 35.415  1.00 104.21 ? 212 VAL   L O   1 
ATOM   21198 C  CB  . VAL   L  12 212 ? -13.071 -126.528 33.687  1.00 101.86 ? 212 VAL   L CB  1 
ATOM   21199 C  CG1 . VAL   L  12 212 ? -12.341 -127.839 33.929  1.00 104.18 ? 212 VAL   L CG1 1 
ATOM   21200 C  CG2 . VAL   L  12 212 ? -12.306 -125.673 32.689  1.00 99.57  ? 212 VAL   L CG2 1 
ATOM   21201 N  N   . ARG   L  12 213 ? -15.770 -128.744 33.965  1.00 107.82 ? 213 ARG   L N   1 
ATOM   21202 C  CA  . ARG   L  12 213 ? -16.494 -129.684 34.865  1.00 108.33 ? 213 ARG   L CA  1 
ATOM   21203 C  C   . ARG   L  12 213 ? -15.574 -130.866 35.189  1.00 105.36 ? 213 ARG   L C   1 
ATOM   21204 O  O   . ARG   L  12 213 ? -14.712 -131.180 34.345  1.00 100.05 ? 213 ARG   L O   1 
ATOM   21205 C  CB  . ARG   L  12 213 ? -17.788 -130.165 34.200  1.00 109.95 ? 213 ARG   L CB  1 
ATOM   21206 C  CG  . ARG   L  12 213 ? -18.668 -131.023 35.097  1.00 113.08 ? 213 ARG   L CG  1 
ATOM   21207 C  CD  . ARG   L  12 213 ? -20.015 -131.340 34.474  1.00 118.51 ? 213 ARG   L CD  1 
ATOM   21208 N  NE  . ARG   L  12 213 ? -19.938 -132.401 33.475  1.00 122.04 ? 213 ARG   L NE  1 
ATOM   21209 C  CZ  . ARG   L  12 213 ? -19.807 -132.228 32.158  1.00 121.76 ? 213 ARG   L CZ  1 
ATOM   21210 N  NH1 . ARG   L  12 213 ? -19.729 -131.016 31.631  1.00 119.86 ? 213 ARG   L NH1 1 
ATOM   21211 N  NH2 . ARG   L  12 213 ? -19.753 -133.284 31.364  1.00 123.24 ? 213 ARG   L NH2 1 
ATOM   21212 N  N   . LYS   L  12 214 ? -15.759 -131.488 36.360  1.00 109.63 ? 214 LYS   L N   1 
ATOM   21213 C  CA  . LYS   L  12 214 ? -14.991 -132.680 36.819  1.00 110.16 ? 214 LYS   L CA  1 
ATOM   21214 C  C   . LYS   L  12 214 ? -15.932 -133.873 37.010  1.00 111.18 ? 214 LYS   L C   1 
ATOM   21215 O  O   . LYS   L  12 214 ? -17.081 -133.666 37.443  1.00 112.95 ? 214 LYS   L O   1 
ATOM   21216 C  CB  . LYS   L  12 214 ? -14.254 -132.390 38.129  1.00 111.16 ? 214 LYS   L CB  1 
ATOM   21217 C  CG  . LYS   L  12 214 ? -12.995 -131.550 37.977  1.00 111.76 ? 214 LYS   L CG  1 
ATOM   21218 C  CD  . LYS   L  12 214 ? -12.331 -131.215 39.292  1.00 113.95 ? 214 LYS   L CD  1 
ATOM   21219 C  CE  . LYS   L  12 214 ? -11.481 -129.964 39.216  1.00 113.21 ? 214 LYS   L CE  1 
ATOM   21220 N  NZ  . LYS   L  12 214 ? -11.205 -129.414 40.564  1.00 114.72 ? 214 LYS   L NZ  1 
ATOM   21221 N  N   . GLU   L  12 215 ? -15.443 -135.074 36.691  1.00 110.95 ? 215 GLU   L N   1 
ATOM   21222 C  CA  . GLU   L  12 215 ? -16.092 -136.373 37.014  1.00 113.60 ? 215 GLU   L CA  1 
ATOM   21223 C  C   . GLU   L  12 215 ? -15.025 -137.309 37.589  1.00 109.22 ? 215 GLU   L C   1 
ATOM   21224 O  O   . GLU   L  12 215 ? -13.892 -137.304 37.064  1.00 105.55 ? 215 GLU   L O   1 
ATOM   21225 C  CB  . GLU   L  12 215 ? -16.756 -136.975 35.774  1.00 119.47 ? 215 GLU   L CB  1 
ATOM   21226 C  CG  . GLU   L  12 215 ? -18.020 -136.245 35.350  1.00 121.72 ? 215 GLU   L CG  1 
ATOM   21227 C  CD  . GLU   L  12 215 ? -18.772 -136.882 34.194  1.00 121.71 ? 215 GLU   L CD  1 
ATOM   21228 O  OE1 . GLU   L  12 215 ? -19.586 -136.178 33.563  1.00 124.77 ? 215 GLU   L OE1 1 
ATOM   21229 O  OE2 . GLU   L  12 215 ? -18.545 -138.079 33.930  1.00 125.49 ? 215 GLU   L OE2 1 
ATOM   21230 N  N   . PHE   L  12 216 ? -15.373 -138.060 38.638  1.00 108.86 ? 216 PHE   L N   1 
ATOM   21231 C  CA  . PHE   L  12 216 ? -14.480 -139.038 39.312  1.00 106.74 ? 216 PHE   L CA  1 
ATOM   21232 C  C   . PHE   L  12 216 ? -15.117 -140.430 39.274  1.00 105.07 ? 216 PHE   L C   1 
ATOM   21233 O  O   . PHE   L  12 216 ? -16.342 -140.542 39.477  1.00 108.63 ? 216 PHE   L O   1 
ATOM   21234 C  CB  . PHE   L  12 216 ? -14.195 -138.621 40.755  1.00 106.16 ? 216 PHE   L CB  1 
ATOM   21235 C  CG  . PHE   L  12 216 ? -13.283 -139.570 41.490  1.00 106.25 ? 216 PHE   L CG  1 
ATOM   21236 C  CD1 . PHE   L  12 216 ? -11.916 -139.556 41.260  1.00 104.80 ? 216 PHE   L CD1 1 
ATOM   21237 C  CD2 . PHE   L  12 216 ? -13.792 -140.492 42.392  1.00 106.65 ? 216 PHE   L CD2 1 
ATOM   21238 C  CE1 . PHE   L  12 216 ? -11.076 -140.436 41.926  1.00 103.64 ? 216 PHE   L CE1 1 
ATOM   21239 C  CE2 . PHE   L  12 216 ? -12.951 -141.371 43.057  1.00 106.49 ? 216 PHE   L CE2 1 
ATOM   21240 C  CZ  . PHE   L  12 216 ? -11.595 -141.341 42.823  1.00 104.55 ? 216 PHE   L CZ  1 
ATOM   21241 N  N   . TYR   L  12 217 ? -14.297 -141.454 39.029  1.00 102.49 ? 217 TYR   L N   1 
ATOM   21242 C  CA  . TYR   L  12 217 ? -14.698 -142.885 39.022  1.00 104.77 ? 217 TYR   L CA  1 
ATOM   21243 C  C   . TYR   L  12 217 ? -13.613 -143.732 39.693  1.00 101.77 ? 217 TYR   L C   1 
ATOM   21244 O  O   . TYR   L  12 217 ? -12.414 -143.514 39.421  1.00 93.98  ? 217 TYR   L O   1 
ATOM   21245 C  CB  . TYR   L  12 217 ? -14.960 -143.364 37.593  1.00 103.56 ? 217 TYR   L CB  1 
ATOM   21246 C  CG  . TYR   L  12 217 ? -16.049 -142.605 36.883  1.00 103.45 ? 217 TYR   L CG  1 
ATOM   21247 C  CD1 . TYR   L  12 217 ? -17.382 -142.816 37.194  1.00 104.26 ? 217 TYR   L CD1 1 
ATOM   21248 C  CD2 . TYR   L  12 217 ? -15.748 -141.660 35.916  1.00 103.53 ? 217 TYR   L CD2 1 
ATOM   21249 C  CE1 . TYR   L  12 217 ? -18.392 -142.116 36.555  1.00 106.68 ? 217 TYR   L CE1 1 
ATOM   21250 C  CE2 . TYR   L  12 217 ? -16.745 -140.950 35.267  1.00 106.58 ? 217 TYR   L CE2 1 
ATOM   21251 C  CZ  . TYR   L  12 217 ? -18.072 -141.179 35.588  1.00 107.47 ? 217 TYR   L CZ  1 
ATOM   21252 O  OH  . TYR   L  12 217 ? -19.065 -140.490 34.954  1.00 109.87 ? 217 TYR   L OH  1 
ATOM   21253 N  N   . GLU   L  12 218 ? -14.036 -144.673 40.541  1.00 103.05 ? 218 GLU   L N   1 
ATOM   21254 C  CA  . GLU   L  12 218 ? -13.147 -145.658 41.207  1.00 103.46 ? 218 GLU   L CA  1 
ATOM   21255 C  C   . GLU   L  12 218 ? -12.484 -146.517 40.126  1.00 102.67 ? 218 GLU   L C   1 
ATOM   21256 O  O   . GLU   L  12 218 ? -13.152 -146.798 39.108  1.00 101.86 ? 218 GLU   L O   1 
ATOM   21257 C  CB  . GLU   L  12 218 ? -13.946 -146.525 42.183  1.00 106.18 ? 218 GLU   L CB  1 
ATOM   21258 C  CG  . GLU   L  12 218 ? -14.465 -145.769 43.393  1.00 109.42 ? 218 GLU   L CG  1 
ATOM   21259 C  CD  . GLU   L  12 218 ? -13.493 -145.699 44.558  1.00 111.33 ? 218 GLU   L CD  1 
ATOM   21260 O  OE1 . GLU   L  12 218 ? -12.993 -146.763 44.975  1.00 112.88 ? 218 GLU   L OE1 1 
ATOM   21261 O  OE2 . GLU   L  12 218 ? -13.236 -144.582 45.042  1.00 114.78 ? 218 GLU   L OE2 1 
ATOM   21262 N  N   . LEU   L  12 219 ? -11.213 -146.877 40.326  1.00 104.83 ? 219 LEU   L N   1 
ATOM   21263 C  CA  . LEU   L  12 219 ? -10.493 -147.927 39.553  1.00 107.05 ? 219 LEU   L CA  1 
ATOM   21264 C  C   . LEU   L  12 219 ? -10.012 -149.009 40.531  1.00 108.70 ? 219 LEU   L C   1 
ATOM   21265 O  O   . LEU   L  12 219 ? -10.099 -148.786 41.758  1.00 112.88 ? 219 LEU   L O   1 
ATOM   21266 C  CB  . LEU   L  12 219 ? -9.320  -147.304 38.784  1.00 102.67 ? 219 LEU   L CB  1 
ATOM   21267 C  CG  . LEU   L  12 219 ? -9.681  -146.357 37.639  1.00 101.53 ? 219 LEU   L CG  1 
ATOM   21268 C  CD1 . LEU   L  12 219 ? -8.424  -145.822 36.970  1.00 99.96  ? 219 LEU   L CD1 1 
ATOM   21269 C  CD2 . LEU   L  12 219 ? -10.575 -147.034 36.608  1.00 101.69 ? 219 LEU   L CD2 1 
ATOM   21270 N  N   . LYS   L  12 220 ? -9.540  -150.143 40.010  1.00 106.26 ? 220 LYS   L N   1 
ATOM   21271 C  CA  . LYS   L  12 220 ? -9.048  -151.282 40.830  1.00 103.69 ? 220 LYS   L CA  1 
ATOM   21272 C  C   . LYS   L  12 220 ? -7.765  -150.866 41.556  1.00 100.16 ? 220 LYS   L C   1 
ATOM   21273 O  O   . LYS   L  12 220 ? -6.878  -150.279 40.907  1.00 93.64  ? 220 LYS   L O   1 
ATOM   21274 C  CB  . LYS   L  12 220 ? -8.834  -152.521 39.961  1.00 105.11 ? 220 LYS   L CB  1 
ATOM   21275 C  CG  . LYS   L  12 220 ? -10.092 -153.346 39.733  1.00 108.78 ? 220 LYS   L CG  1 
ATOM   21276 C  CD  . LYS   L  12 220 ? -9.904  -154.459 38.733  1.00 110.09 ? 220 LYS   L CD  1 
ATOM   21277 C  CE  . LYS   L  12 220 ? -8.893  -155.486 39.190  1.00 110.01 ? 220 LYS   L CE  1 
ATOM   21278 N  NZ  . LYS   L  12 220 ? -8.863  -156.664 38.294  1.00 112.44 ? 220 LYS   L NZ  1 
ATOM   21279 N  N   . ARG   L  12 221 ? -7.679  -151.190 42.850  1.00 103.15 ? 221 ARG   L N   1 
ATOM   21280 C  CA  . ARG   L  12 221 ? -6.665  -150.659 43.801  1.00 104.85 ? 221 ARG   L CA  1 
ATOM   21281 C  C   . ARG   L  12 221 ? -5.506  -151.652 43.982  1.00 105.63 ? 221 ARG   L C   1 
ATOM   21282 O  O   . ARG   L  12 221 ? -4.612  -151.353 44.797  1.00 104.72 ? 221 ARG   L O   1 
ATOM   21283 C  CB  . ARG   L  12 221 ? -7.349  -150.335 45.133  1.00 108.03 ? 221 ARG   L CB  1 
ATOM   21284 C  CG  . ARG   L  12 221 ? -8.265  -149.120 45.073  1.00 109.85 ? 221 ARG   L CG  1 
ATOM   21285 C  CD  . ARG   L  12 221 ? -9.335  -149.114 46.150  1.00 114.81 ? 221 ARG   L CD  1 
ATOM   21286 N  NE  . ARG   L  12 221 ? -8.800  -148.842 47.480  1.00 115.56 ? 221 ARG   L NE  1 
ATOM   21287 C  CZ  . ARG   L  12 221 ? -8.613  -147.632 48.008  1.00 112.91 ? 221 ARG   L CZ  1 
ATOM   21288 N  NH1 . ARG   L  12 221 ? -8.908  -146.538 47.323  1.00 112.65 ? 221 ARG   L NH1 1 
ATOM   21289 N  NH2 . ARG   L  12 221 ? -8.122  -147.521 49.231  1.00 112.89 ? 221 ARG   L NH2 1 
ATOM   21290 N  N   . ASP   L  12 222 ? -5.496  -152.765 43.240  1.00 110.82 ? 222 ASP   L N   1 
ATOM   21291 C  CA  . ASP   L  12 222 ? -4.459  -153.829 43.358  1.00 113.42 ? 222 ASP   L CA  1 
ATOM   21292 C  C   . ASP   L  12 222 ? -3.243  -153.446 42.502  1.00 113.22 ? 222 ASP   L C   1 
ATOM   21293 O  O   . ASP   L  12 222 ? -3.199  -152.396 41.849  1.00 111.30 ? 222 ASP   L O   1 
ATOM   21294 C  CB  . ASP   L  12 222 ? -5.026  -155.217 43.023  1.00 113.08 ? 222 ASP   L CB  1 
ATOM   21295 C  CG  . ASP   L  12 222 ? -5.475  -155.422 41.583  1.00 111.69 ? 222 ASP   L CG  1 
ATOM   21296 O  OD1 . ASP   L  12 222 ? -5.787  -154.419 40.912  1.00 114.10 ? 222 ASP   L OD1 1 
ATOM   21297 O  OD2 . ASP   L  12 222 ? -5.526  -156.590 41.148  1.00 105.84 ? 222 ASP   L OD2 1 
ATOM   21298 O  OXT . ASP   L  12 222 ? -2.255  -154.186 42.459  1.00 115.74 ? 222 ASP   L OXT 1 
ATOM   21299 N  N   . THR   M  13 14  ? 26.502  -133.396 43.613  1.00 116.47 ? 1   THR   M N   1 
ATOM   21300 C  CA  . THR   M  13 14  ? 26.392  -134.869 43.828  1.00 115.56 ? 1   THR   M CA  1 
ATOM   21301 C  C   . THR   M  13 14  ? 26.994  -135.224 45.192  1.00 103.64 ? 1   THR   M C   1 
ATOM   21302 O  O   . THR   M  13 14  ? 28.169  -134.887 45.430  1.00 104.05 ? 1   THR   M O   1 
ATOM   21303 C  CB  . THR   M  13 14  ? 27.058  -135.662 42.694  1.00 127.78 ? 1   THR   M CB  1 
ATOM   21304 O  OG1 . THR   M  13 14  ? 26.257  -135.511 41.521  1.00 129.71 ? 1   THR   M OG1 1 
ATOM   21305 C  CG2 . THR   M  13 14  ? 27.228  -137.133 43.017  1.00 129.31 ? 1   THR   M CG2 1 
ATOM   21306 N  N   . GLN   M  13 15  ? 26.213  -135.907 46.029  1.00 99.42  ? 2   GLN   M N   1 
ATOM   21307 C  CA  . GLN   M  13 15  ? 26.561  -136.250 47.430  1.00 94.37  ? 2   GLN   M CA  1 
ATOM   21308 C  C   . GLN   M  13 15  ? 26.513  -137.768 47.615  1.00 91.04  ? 2   GLN   M C   1 
ATOM   21309 O  O   . GLN   M  13 15  ? 26.135  -138.479 46.661  1.00 85.64  ? 2   GLN   M O   1 
ATOM   21310 C  CB  . GLN   M  13 15  ? 25.547  -135.638 48.395  1.00 93.84  ? 2   GLN   M CB  1 
ATOM   21311 C  CG  . GLN   M  13 15  ? 25.613  -134.125 48.515  1.00 92.81  ? 2   GLN   M CG  1 
ATOM   21312 C  CD  . GLN   M  13 15  ? 24.793  -133.638 49.686  1.00 90.03  ? 2   GLN   M CD  1 
ATOM   21313 O  OE1 . GLN   M  13 15  ? 24.588  -134.346 50.671  1.00 84.51  ? 2   GLN   M OE1 1 
ATOM   21314 N  NE2 . GLN   M  13 15  ? 24.306  -132.413 49.591  1.00 92.07  ? 2   GLN   M NE2 1 
ATOM   21315 N  N   . GLN   M  13 16  ? 26.885  -138.217 48.816  1.00 90.53  ? 3   GLN   M N   1 
ATOM   21316 C  CA  . GLN   M  13 16  ? 26.489  -139.518 49.408  1.00 88.71  ? 3   GLN   M CA  1 
ATOM   21317 C  C   . GLN   M  13 16  ? 26.185  -139.282 50.884  1.00 83.43  ? 3   GLN   M C   1 
ATOM   21318 O  O   . GLN   M  13 16  ? 26.955  -138.623 51.577  1.00 83.21  ? 3   GLN   M O   1 
ATOM   21319 C  CB  . GLN   M  13 16  ? 27.575  -140.576 49.204  1.00 93.73  ? 3   GLN   M CB  1 
ATOM   21320 C  CG  . GLN   M  13 16  ? 28.925  -140.226 49.818  1.00 99.04  ? 3   GLN   M CG  1 
ATOM   21321 C  CD  . GLN   M  13 16  ? 29.825  -141.434 49.924  1.00 106.89 ? 3   GLN   M CD  1 
ATOM   21322 O  OE1 . GLN   M  13 16  ? 29.369  -142.558 50.132  1.00 115.07 ? 3   GLN   M OE1 1 
ATOM   21323 N  NE2 . GLN   M  13 16  ? 31.123  -141.210 49.788  1.00 112.27 ? 3   GLN   M NE2 1 
ATOM   21324 N  N   . PRO   M  13 17  ? 25.058  -139.804 51.414  1.00 79.24  ? 4   PRO   M N   1 
ATOM   21325 C  CA  . PRO   M  13 17  ? 24.688  -139.573 52.809  1.00 79.53  ? 4   PRO   M CA  1 
ATOM   21326 C  C   . PRO   M  13 17  ? 25.676  -140.296 53.737  1.00 80.62  ? 4   PRO   M C   1 
ATOM   21327 O  O   . PRO   M  13 17  ? 26.110  -141.370 53.370  1.00 86.19  ? 4   PRO   M O   1 
ATOM   21328 C  CB  . PRO   M  13 17  ? 23.274  -140.161 52.901  1.00 78.31  ? 4   PRO   M CB  1 
ATOM   21329 C  CG  . PRO   M  13 17  ? 23.265  -141.246 51.847  1.00 79.12  ? 4   PRO   M CG  1 
ATOM   21330 C  CD  . PRO   M  13 17  ? 24.122  -140.702 50.723  1.00 78.84  ? 4   PRO   M CD  1 
ATOM   21331 N  N   . ILE   M  13 18  ? 26.026  -139.691 54.876  1.00 78.14  ? 5   ILE   M N   1 
ATOM   21332 C  CA  . ILE   M  13 18  ? 26.994  -140.263 55.860  1.00 77.98  ? 5   ILE   M CA  1 
ATOM   21333 C  C   . ILE   M  13 18  ? 26.215  -140.716 57.101  1.00 79.14  ? 5   ILE   M C   1 
ATOM   21334 O  O   . ILE   M  13 18  ? 25.895  -141.917 57.183  1.00 78.05  ? 5   ILE   M O   1 
ATOM   21335 C  CB  . ILE   M  13 18  ? 28.119  -139.258 56.183  1.00 77.44  ? 5   ILE   M CB  1 
ATOM   21336 C  CG1 . ILE   M  13 18  ? 28.820  -138.758 54.916  1.00 77.26  ? 5   ILE   M CG1 1 
ATOM   21337 C  CG2 . ILE   M  13 18  ? 29.108  -139.847 57.177  1.00 79.52  ? 5   ILE   M CG2 1 
ATOM   21338 C  CD1 . ILE   M  13 18  ? 29.432  -139.845 54.060  1.00 75.30  ? 5   ILE   M CD1 1 
ATOM   21339 N  N   . VAL   M  13 19  ? 25.915  -139.798 58.022  1.00 80.20  ? 6   VAL   M N   1 
ATOM   21340 C  CA  . VAL   M  13 19  ? 25.060  -140.068 59.215  1.00 81.93  ? 6   VAL   M CA  1 
ATOM   21341 C  C   . VAL   M  13 19  ? 23.609  -139.959 58.739  1.00 80.55  ? 6   VAL   M C   1 
ATOM   21342 O  O   . VAL   M  13 19  ? 23.279  -138.930 58.118  1.00 83.57  ? 6   VAL   M O   1 
ATOM   21343 C  CB  . VAL   M  13 19  ? 25.362  -139.101 60.379  1.00 85.01  ? 6   VAL   M CB  1 
ATOM   21344 C  CG1 . VAL   M  13 19  ? 24.565  -139.450 61.628  1.00 86.17  ? 6   VAL   M CG1 1 
ATOM   21345 C  CG2 . VAL   M  13 19  ? 26.849  -139.036 60.705  1.00 85.31  ? 6   VAL   M CG2 1 
ATOM   21346 N  N   . THR   M  13 20  ? 22.785  -140.980 58.988  1.00 77.71  ? 7   THR   M N   1 
ATOM   21347 C  CA  . THR   M  13 20  ? 21.414  -141.081 58.419  1.00 79.01  ? 7   THR   M CA  1 
ATOM   21348 C  C   . THR   M  13 20  ? 20.374  -141.387 59.500  1.00 75.61  ? 7   THR   M C   1 
ATOM   21349 O  O   . THR   M  13 20  ? 20.739  -141.954 60.547  1.00 75.65  ? 7   THR   M O   1 
ATOM   21350 C  CB  . THR   M  13 20  ? 21.352  -142.144 57.318  1.00 80.74  ? 7   THR   M CB  1 
ATOM   21351 O  OG1 . THR   M  13 20  ? 21.819  -143.379 57.866  1.00 81.17  ? 7   THR   M OG1 1 
ATOM   21352 C  CG2 . THR   M  13 20  ? 22.174  -141.759 56.108  1.00 82.98  ? 7   THR   M CG2 1 
ATOM   21353 N  N   . GLY   M  13 21  ? 19.124  -141.007 59.221  1.00 76.31  ? 8   GLY   M N   1 
ATOM   21354 C  CA  . GLY   M  13 21  ? 17.922  -141.368 59.994  1.00 78.77  ? 8   GLY   M CA  1 
ATOM   21355 C  C   . GLY   M  13 21  ? 16.981  -142.194 59.136  1.00 80.30  ? 8   GLY   M C   1 
ATOM   21356 O  O   . GLY   M  13 21  ? 16.849  -141.882 57.940  1.00 82.90  ? 8   GLY   M O   1 
ATOM   21357 N  N   . THR   M  13 22  ? 16.365  -143.226 59.713  1.00 83.42  ? 9   THR   M N   1 
ATOM   21358 C  CA  . THR   M  13 22  ? 15.501  -144.199 58.992  1.00 84.25  ? 9   THR   M CA  1 
ATOM   21359 C  C   . THR   M  13 22  ? 14.060  -143.666 58.962  1.00 82.98  ? 9   THR   M C   1 
ATOM   21360 O  O   . THR   M  13 22  ? 13.892  -142.434 58.998  1.00 81.63  ? 9   THR   M O   1 
ATOM   21361 C  CB  . THR   M  13 22  ? 15.660  -145.603 59.594  1.00 85.53  ? 9   THR   M CB  1 
ATOM   21362 O  OG1 . THR   M  13 22  ? 14.976  -146.520 58.739  1.00 87.60  ? 9   THR   M OG1 1 
ATOM   21363 C  CG2 . THR   M  13 22  ? 15.136  -145.724 61.009  1.00 87.43  ? 9   THR   M CG2 1 
ATOM   21364 N  N   . SER   M  13 23  ? 13.074  -144.566 58.892  1.00 85.28  ? 10  SER   M N   1 
ATOM   21365 C  CA  . SER   M  13 23  ? 11.629  -144.295 58.662  1.00 86.88  ? 10  SER   M CA  1 
ATOM   21366 C  C   . SER   M  13 23  ? 11.120  -143.096 59.475  1.00 86.62  ? 10  SER   M C   1 
ATOM   21367 O  O   . SER   M  13 23  ? 11.491  -142.965 60.662  1.00 86.09  ? 10  SER   M O   1 
ATOM   21368 C  CB  . SER   M  13 23  ? 10.804  -145.522 58.968  1.00 89.22  ? 10  SER   M CB  1 
ATOM   21369 O  OG  . SER   M  13 23  ? 11.402  -146.689 58.424  1.00 94.49  ? 10  SER   M OG  1 
ATOM   21370 N  N   . VAL   M  13 24  ? 10.292  -142.265 58.830  1.00 85.80  ? 11  VAL   M N   1 
ATOM   21371 C  CA  . VAL   M  13 24  ? 9.349   -141.290 59.457  1.00 85.37  ? 11  VAL   M CA  1 
ATOM   21372 C  C   . VAL   M  13 24  ? 7.936   -141.706 59.044  1.00 82.29  ? 11  VAL   M C   1 
ATOM   21373 O  O   . VAL   M  13 24  ? 7.680   -141.728 57.830  1.00 78.58  ? 11  VAL   M O   1 
ATOM   21374 C  CB  . VAL   M  13 24  ? 9.635   -139.845 59.006  1.00 85.13  ? 11  VAL   M CB  1 
ATOM   21375 C  CG1 . VAL   M  13 24  ? 8.608   -138.865 59.558  1.00 85.97  ? 11  VAL   M CG1 1 
ATOM   21376 C  CG2 . VAL   M  13 24  ? 11.046  -139.405 59.359  1.00 87.39  ? 11  VAL   M CG2 1 
ATOM   21377 N  N   . ILE   M  13 25  ? 7.059   -142.012 60.003  1.00 84.49  ? 12  ILE   M N   1 
ATOM   21378 C  CA  . ILE   M  13 25  ? 5.680   -142.524 59.735  1.00 88.21  ? 12  ILE   M CA  1 
ATOM   21379 C  C   . ILE   M  13 25  ? 4.659   -141.523 60.284  1.00 87.96  ? 12  ILE   M C   1 
ATOM   21380 O  O   . ILE   M  13 25  ? 4.983   -140.830 61.267  1.00 87.21  ? 12  ILE   M O   1 
ATOM   21381 C  CB  . ILE   M  13 25  ? 5.486   -143.943 60.311  1.00 90.24  ? 12  ILE   M CB  1 
ATOM   21382 C  CG1 . ILE   M  13 25  ? 5.578   -143.985 61.839  1.00 93.38  ? 12  ILE   M CG1 1 
ATOM   21383 C  CG2 . ILE   M  13 25  ? 6.473   -144.905 59.670  1.00 90.83  ? 12  ILE   M CG2 1 
ATOM   21384 C  CD1 . ILE   M  13 25  ? 5.005   -145.244 62.448  1.00 94.97  ? 12  ILE   M CD1 1 
ATOM   21385 N  N   . SER   M  13 26  ? 3.475   -141.461 59.667  1.00 89.84  ? 13  SER   M N   1 
ATOM   21386 C  CA  . SER   M  13 26  ? 2.423   -140.454 59.960  1.00 91.80  ? 13  SER   M CA  1 
ATOM   21387 C  C   . SER   M  13 26  ? 1.078   -140.868 59.364  1.00 91.29  ? 13  SER   M C   1 
ATOM   21388 O  O   . SER   M  13 26  ? 1.073   -141.620 58.374  1.00 93.56  ? 13  SER   M O   1 
ATOM   21389 C  CB  . SER   M  13 26  ? 2.816   -139.118 59.419  1.00 93.85  ? 13  SER   M CB  1 
ATOM   21390 O  OG  . SER   M  13 26  ? 2.961   -139.188 58.007  1.00 98.91  ? 13  SER   M OG  1 
ATOM   21391 N  N   . MET   M  13 27  ? -0.009  -140.334 59.926  1.00 93.83  ? 14  MET   M N   1 
ATOM   21392 C  CA  . MET   M  13 27  ? -1.394  -140.533 59.426  1.00 97.46  ? 14  MET   M CA  1 
ATOM   21393 C  C   . MET   M  13 27  ? -2.296  -139.402 59.935  1.00 98.67  ? 14  MET   M C   1 
ATOM   21394 O  O   . MET   M  13 27  ? -1.954  -138.773 60.960  1.00 101.52 ? 14  MET   M O   1 
ATOM   21395 C  CB  . MET   M  13 27  ? -1.958  -141.886 59.876  1.00 98.04  ? 14  MET   M CB  1 
ATOM   21396 C  CG  . MET   M  13 27  ? -2.085  -142.038 61.381  1.00 98.85  ? 14  MET   M CG  1 
ATOM   21397 S  SD  . MET   M  13 27  ? -2.705  -143.671 61.842  1.00 100.96 ? 14  MET   M SD  1 
ATOM   21398 C  CE  . MET   M  13 27  ? -4.443  -143.492 61.441  1.00 101.41 ? 14  MET   M CE  1 
ATOM   21399 N  N   . LYS   M  13 28  ? -3.397  -139.159 59.224  1.00 98.83  ? 15  LYS   M N   1 
ATOM   21400 C  CA  . LYS   M  13 28  ? -4.484  -138.233 59.631  1.00 98.80  ? 15  LYS   M CA  1 
ATOM   21401 C  C   . LYS   M  13 28  ? -5.505  -139.008 60.465  1.00 100.62 ? 15  LYS   M C   1 
ATOM   21402 O  O   . LYS   M  13 28  ? -5.721  -140.200 60.171  1.00 102.89 ? 15  LYS   M O   1 
ATOM   21403 C  CB  . LYS   M  13 28  ? -5.177  -137.646 58.400  1.00 99.42  ? 15  LYS   M CB  1 
ATOM   21404 C  CG  . LYS   M  13 28  ? -4.308  -136.767 57.512  1.00 98.70  ? 15  LYS   M CG  1 
ATOM   21405 C  CD  . LYS   M  13 28  ? -4.968  -136.466 56.189  1.00 99.12  ? 15  LYS   M CD  1 
ATOM   21406 C  CE  . LYS   M  13 28  ? -4.280  -135.372 55.405  1.00 98.02  ? 15  LYS   M CE  1 
ATOM   21407 N  NZ  . LYS   M  13 28  ? -4.986  -135.107 54.132  1.00 100.56 ? 15  LYS   M NZ  1 
ATOM   21408 N  N   . TYR   M  13 29  ? -6.095  -138.351 61.467  1.00 100.32 ? 16  TYR   M N   1 
ATOM   21409 C  CA  . TYR   M  13 29  ? -7.295  -138.819 62.208  1.00 102.65 ? 16  TYR   M CA  1 
ATOM   21410 C  C   . TYR   M  13 29  ? -8.334  -137.692 62.179  1.00 100.93 ? 16  TYR   M C   1 
ATOM   21411 O  O   . TYR   M  13 29  ? -8.061  -136.656 61.542  1.00 96.64  ? 16  TYR   M O   1 
ATOM   21412 C  CB  . TYR   M  13 29  ? -6.911  -139.288 63.616  1.00 105.93 ? 16  TYR   M CB  1 
ATOM   21413 C  CG  . TYR   M  13 29  ? -6.386  -138.206 64.525  1.00 107.02 ? 16  TYR   M CG  1 
ATOM   21414 C  CD1 . TYR   M  13 29  ? -5.047  -137.847 64.521  1.00 105.67 ? 16  TYR   M CD1 1 
ATOM   21415 C  CD2 . TYR   M  13 29  ? -7.230  -137.543 65.400  1.00 110.54 ? 16  TYR   M CD2 1 
ATOM   21416 C  CE1 . TYR   M  13 29  ? -4.563  -136.853 65.358  1.00 106.29 ? 16  TYR   M CE1 1 
ATOM   21417 C  CE2 . TYR   M  13 29  ? -6.764  -136.545 66.240  1.00 111.60 ? 16  TYR   M CE2 1 
ATOM   21418 C  CZ  . TYR   M  13 29  ? -5.424  -136.198 66.221  1.00 109.34 ? 16  TYR   M CZ  1 
ATOM   21419 O  OH  . TYR   M  13 29  ? -4.960  -135.216 67.048  1.00 109.91 ? 16  TYR   M OH  1 
ATOM   21420 N  N   . ASP   M  13 30  ? -9.482  -137.891 62.835  1.00 105.32 ? 17  ASP   M N   1 
ATOM   21421 C  CA  . ASP   M  13 30  ? -10.691 -137.030 62.704  1.00 109.22 ? 17  ASP   M CA  1 
ATOM   21422 C  C   . ASP   M  13 30  ? -10.348 -135.554 62.970  1.00 108.69 ? 17  ASP   M C   1 
ATOM   21423 O  O   . ASP   M  13 30  ? -10.844 -134.703 62.206  1.00 111.58 ? 17  ASP   M O   1 
ATOM   21424 C  CB  . ASP   M  13 30  ? -11.840 -137.527 63.592  1.00 112.66 ? 17  ASP   M CB  1 
ATOM   21425 C  CG  . ASP   M  13 30  ? -11.516 -137.674 65.072  1.00 113.42 ? 17  ASP   M CG  1 
ATOM   21426 O  OD1 . ASP   M  13 30  ? -10.474 -137.151 65.508  1.00 114.82 ? 17  ASP   M OD1 1 
ATOM   21427 O  OD2 . ASP   M  13 30  ? -12.315 -138.322 65.779  1.00 115.71 ? 17  ASP   M OD2 1 
ATOM   21428 N  N   . ASN   M  13 31  ? -9.532  -135.262 63.991  1.00 108.15 ? 18  ASN   M N   1 
ATOM   21429 C  CA  . ASN   M  13 31  ? -9.303  -133.886 64.516  1.00 108.12 ? 18  ASN   M CA  1 
ATOM   21430 C  C   . ASN   M  13 31  ? -7.897  -133.362 64.196  1.00 107.26 ? 18  ASN   M C   1 
ATOM   21431 O  O   . ASN   M  13 31  ? -7.673  -132.159 64.425  1.00 110.80 ? 18  ASN   M O   1 
ATOM   21432 C  CB  . ASN   M  13 31  ? -9.526  -133.814 66.029  1.00 109.40 ? 18  ASN   M CB  1 
ATOM   21433 C  CG  . ASN   M  13 31  ? -10.955 -134.077 66.457  1.00 110.70 ? 18  ASN   M CG  1 
ATOM   21434 O  OD1 . ASN   M  13 31  ? -11.191 -134.455 67.601  1.00 117.69 ? 18  ASN   M OD1 1 
ATOM   21435 N  ND2 . ASN   M  13 31  ? -11.918 -133.881 65.568  1.00 110.41 ? 18  ASN   M ND2 1 
ATOM   21436 N  N   . GLY   M  13 32  ? -6.975  -134.193 63.705  1.00 103.23 ? 19  GLY   M N   1 
ATOM   21437 C  CA  . GLY   M  13 32  ? -5.609  -133.727 63.397  1.00 102.36 ? 19  GLY   M CA  1 
ATOM   21438 C  C   . GLY   M  13 32  ? -4.738  -134.796 62.766  1.00 101.76 ? 19  GLY   M C   1 
ATOM   21439 O  O   . GLY   M  13 32  ? -5.281  -135.662 62.051  1.00 103.95 ? 19  GLY   M O   1 
ATOM   21440 N  N   . VAL   M  13 33  ? -3.428  -134.723 63.021  1.00 100.45 ? 20  VAL   M N   1 
ATOM   21441 C  CA  . VAL   M  13 33  ? -2.391  -135.618 62.429  1.00 99.45  ? 20  VAL   M CA  1 
ATOM   21442 C  C   . VAL   M  13 33  ? -1.452  -136.104 63.538  1.00 100.01 ? 20  VAL   M C   1 
ATOM   21443 O  O   . VAL   M  13 33  ? -1.243  -135.357 64.514  1.00 101.02 ? 20  VAL   M O   1 
ATOM   21444 C  CB  . VAL   M  13 33  ? -1.610  -134.906 61.306  1.00 96.64  ? 20  VAL   M CB  1 
ATOM   21445 C  CG1 . VAL   M  13 33  ? -2.498  -134.624 60.107  1.00 96.83  ? 20  VAL   M CG1 1 
ATOM   21446 C  CG2 . VAL   M  13 33  ? -0.944  -133.626 61.788  1.00 95.89  ? 20  VAL   M CG2 1 
ATOM   21447 N  N   . ILE   M  13 34  ? -0.927  -137.322 63.385  1.00 100.98 ? 21  ILE   M N   1 
ATOM   21448 C  CA  . ILE   M  13 34  ? 0.147   -137.903 64.242  1.00 99.12  ? 21  ILE   M CA  1 
ATOM   21449 C  C   . ILE   M  13 34  ? 1.356   -138.173 63.344  1.00 96.79  ? 21  ILE   M C   1 
ATOM   21450 O  O   . ILE   M  13 34  ? 1.150   -138.500 62.159  1.00 95.36  ? 21  ILE   M O   1 
ATOM   21451 C  CB  . ILE   M  13 34  ? -0.337  -139.173 64.974  1.00 101.47 ? 21  ILE   M CB  1 
ATOM   21452 C  CG1 . ILE   M  13 34  ? -1.631  -138.904 65.749  1.00 106.50 ? 21  ILE   M CG1 1 
ATOM   21453 C  CG2 . ILE   M  13 34  ? 0.759   -139.733 65.872  1.00 99.34  ? 21  ILE   M CG2 1 
ATOM   21454 C  CD1 . ILE   M  13 34  ? -2.213  -140.115 66.443  1.00 109.48 ? 21  ILE   M CD1 1 
ATOM   21455 N  N   . ILE   M  13 35  ? 2.562   -138.014 63.891  1.00 92.69  ? 22  ILE   M N   1 
ATOM   21456 C  CA  . ILE   M  13 35  ? 3.848   -138.288 63.186  1.00 89.30  ? 22  ILE   M CA  1 
ATOM   21457 C  C   . ILE   M  13 35  ? 4.862   -138.807 64.213  1.00 89.08  ? 22  ILE   M C   1 
ATOM   21458 O  O   . ILE   M  13 35  ? 4.849   -138.313 65.358  1.00 89.37  ? 22  ILE   M O   1 
ATOM   21459 C  CB  . ILE   M  13 35  ? 4.346   -137.033 62.439  1.00 87.96  ? 22  ILE   M CB  1 
ATOM   21460 C  CG1 . ILE   M  13 35  ? 5.655   -137.301 61.692  1.00 86.22  ? 22  ILE   M CG1 1 
ATOM   21461 C  CG2 . ILE   M  13 35  ? 4.462   -135.847 63.385  1.00 89.83  ? 22  ILE   M CG2 1 
ATOM   21462 C  CD1 . ILE   M  13 35  ? 6.004   -136.253 60.662  1.00 86.14  ? 22  ILE   M CD1 1 
ATOM   21463 N  N   . ALA   M  13 36  ? 5.692   -139.774 63.811  1.00 86.88  ? 23  ALA   M N   1 
ATOM   21464 C  CA  . ALA   M  13 36  ? 6.701   -140.438 64.669  1.00 86.00  ? 23  ALA   M CA  1 
ATOM   21465 C  C   . ALA   M  13 36  ? 7.971   -140.751 63.871  1.00 83.37  ? 23  ALA   M C   1 
ATOM   21466 O  O   . ALA   M  13 36  ? 7.877   -140.964 62.644  1.00 80.40  ? 23  ALA   M O   1 
ATOM   21467 C  CB  . ALA   M  13 36  ? 6.119   -141.695 65.259  1.00 89.33  ? 23  ALA   M CB  1 
ATOM   21468 N  N   . ALA   M  13 37  ? 9.110   -140.789 64.567  1.00 81.43  ? 24  ALA   M N   1 
ATOM   21469 C  CA  . ALA   M  13 37  ? 10.448  -141.125 64.028  1.00 83.37  ? 24  ALA   M CA  1 
ATOM   21470 C  C   . ALA   M  13 37  ? 11.374  -141.503 65.186  1.00 87.31  ? 24  ALA   M C   1 
ATOM   21471 O  O   . ALA   M  13 37  ? 11.365  -140.784 66.204  1.00 88.11  ? 24  ALA   M O   1 
ATOM   21472 C  CB  . ALA   M  13 37  ? 11.002  -139.958 63.253  1.00 84.59  ? 24  ALA   M CB  1 
ATOM   21473 N  N   . ASP   M  13 38  ? 12.151  -142.577 65.025  1.00 89.96  ? 25  ASP   M N   1 
ATOM   21474 C  CA  . ASP   M  13 38  ? 13.068  -143.093 66.077  1.00 94.86  ? 25  ASP   M CA  1 
ATOM   21475 C  C   . ASP   M  13 38  ? 14.221  -142.101 66.268  1.00 94.42  ? 25  ASP   M C   1 
ATOM   21476 O  O   . ASP   M  13 38  ? 14.348  -141.168 65.445  1.00 97.15  ? 25  ASP   M O   1 
ATOM   21477 C  CB  . ASP   M  13 38  ? 13.530  -144.526 65.784  1.00 100.40 ? 25  ASP   M CB  1 
ATOM   21478 C  CG  . ASP   M  13 38  ? 14.407  -144.701 64.554  1.00 106.79 ? 25  ASP   M CG  1 
ATOM   21479 O  OD1 . ASP   M  13 38  ? 15.284  -143.839 64.314  1.00 100.82 ? 25  ASP   M OD1 1 
ATOM   21480 O  OD2 . ASP   M  13 38  ? 14.208  -145.712 63.845  1.00 113.07 ? 25  ASP   M OD2 1 
ATOM   21481 N  N   . ASN   M  13 39  ? 15.017  -142.303 67.322  1.00 89.28  ? 26  ASN   M N   1 
ATOM   21482 C  CA  . ASN   M  13 39  ? 16.029  -141.333 67.813  1.00 89.55  ? 26  ASN   M CA  1 
ATOM   21483 C  C   . ASN   M  13 39  ? 17.439  -141.826 67.475  1.00 85.72  ? 26  ASN   M C   1 
ATOM   21484 O  O   . ASN   M  13 39  ? 18.336  -141.647 68.317  1.00 86.45  ? 26  ASN   M O   1 
ATOM   21485 C  CB  . ASN   M  13 39  ? 15.878  -141.098 69.317  1.00 93.59  ? 26  ASN   M CB  1 
ATOM   21486 C  CG  . ASN   M  13 39  ? 14.486  -140.643 69.698  1.00 99.33  ? 26  ASN   M CG  1 
ATOM   21487 O  OD1 . ASN   M  13 39  ? 13.846  -139.899 68.954  1.00 99.46  ? 26  ASN   M OD1 1 
ATOM   21488 N  ND2 . ASN   M  13 39  ? 14.010  -141.080 70.854  1.00 99.66  ? 26  ASN   M ND2 1 
ATOM   21489 N  N   . LEU   M  13 40  ? 17.637  -142.391 66.281  1.00 85.43  ? 27  LEU   M N   1 
ATOM   21490 C  CA  . LEU   M  13 40  ? 18.920  -143.031 65.886  1.00 89.41  ? 27  LEU   M CA  1 
ATOM   21491 C  C   . LEU   M  13 40  ? 19.591  -142.240 64.762  1.00 87.83  ? 27  LEU   M C   1 
ATOM   21492 O  O   . LEU   M  13 40  ? 18.897  -141.866 63.796  1.00 92.82  ? 27  LEU   M O   1 
ATOM   21493 C  CB  . LEU   M  13 40  ? 18.652  -144.472 65.443  1.00 92.30  ? 27  LEU   M CB  1 
ATOM   21494 C  CG  . LEU   M  13 40  ? 19.889  -145.305 65.108  1.00 95.85  ? 27  LEU   M CG  1 
ATOM   21495 C  CD1 . LEU   M  13 40  ? 20.874  -145.343 66.268  1.00 98.16  ? 27  LEU   M CD1 1 
ATOM   21496 C  CD2 . LEU   M  13 40  ? 19.490  -146.717 64.718  1.00 96.88  ? 27  LEU   M CD2 1 
ATOM   21497 N  N   . GLY   M  13 41  ? 20.900  -142.019 64.902  1.00 85.04  ? 28  GLY   M N   1 
ATOM   21498 C  CA  . GLY   M  13 41  ? 21.794  -141.506 63.849  1.00 86.79  ? 28  GLY   M CA  1 
ATOM   21499 C  C   . GLY   M  13 41  ? 22.766  -142.586 63.414  1.00 87.08  ? 28  GLY   M C   1 
ATOM   21500 O  O   . GLY   M  13 41  ? 23.814  -142.731 64.066  1.00 94.88  ? 28  GLY   M O   1 
ATOM   21501 N  N   . SER   M  13 42  ? 22.419  -143.334 62.365  1.00 86.79  ? 29  SER   M N   1 
ATOM   21502 C  CA  . SER   M  13 42  ? 23.222  -144.454 61.808  1.00 85.46  ? 29  SER   M CA  1 
ATOM   21503 C  C   . SER   M  13 42  ? 24.427  -143.906 61.036  1.00 86.43  ? 29  SER   M C   1 
ATOM   21504 O  O   . SER   M  13 42  ? 24.283  -142.857 60.380  1.00 89.82  ? 29  SER   M O   1 
ATOM   21505 C  CB  . SER   M  13 42  ? 22.375  -145.326 60.925  1.00 82.31  ? 29  SER   M CB  1 
ATOM   21506 O  OG  . SER   M  13 42  ? 21.299  -145.885 61.660  1.00 81.34  ? 29  SER   M OG  1 
ATOM   21507 N  N   . TYR   M  13 43  ? 25.560  -144.608 61.106  1.00 83.18  ? 30  TYR   M N   1 
ATOM   21508 C  CA  . TYR   M  13 43  ? 26.800  -144.337 60.331  1.00 84.01  ? 30  TYR   M CA  1 
ATOM   21509 C  C   . TYR   M  13 43  ? 27.120  -145.605 59.532  1.00 83.76  ? 30  TYR   M C   1 
ATOM   21510 O  O   . TYR   M  13 43  ? 27.966  -146.399 59.973  1.00 84.51  ? 30  TYR   M O   1 
ATOM   21511 C  CB  . TYR   M  13 43  ? 27.921  -143.909 61.284  1.00 84.52  ? 30  TYR   M CB  1 
ATOM   21512 C  CG  . TYR   M  13 43  ? 29.227  -143.508 60.642  1.00 87.12  ? 30  TYR   M CG  1 
ATOM   21513 C  CD1 . TYR   M  13 43  ? 29.459  -142.202 60.239  1.00 88.59  ? 30  TYR   M CD1 1 
ATOM   21514 C  CD2 . TYR   M  13 43  ? 30.256  -144.423 60.476  1.00 85.70  ? 30  TYR   M CD2 1 
ATOM   21515 C  CE1 . TYR   M  13 43  ? 30.664  -141.822 59.666  1.00 90.84  ? 30  TYR   M CE1 1 
ATOM   21516 C  CE2 . TYR   M  13 43  ? 31.466  -144.062 59.905  1.00 86.73  ? 30  TYR   M CE2 1 
ATOM   21517 C  CZ  . TYR   M  13 43  ? 31.672  -142.756 59.499  1.00 87.54  ? 30  TYR   M CZ  1 
ATOM   21518 O  OH  . TYR   M  13 43  ? 32.865  -142.402 58.938  1.00 90.99  ? 30  TYR   M OH  1 
ATOM   21519 N  N   . GLY   M  13 44  ? 26.423  -145.806 58.409  1.00 83.38  ? 31  GLY   M N   1 
ATOM   21520 C  CA  . GLY   M  13 44  ? 26.435  -147.077 57.661  1.00 84.30  ? 31  GLY   M CA  1 
ATOM   21521 C  C   . GLY   M  13 44  ? 25.767  -148.172 58.472  1.00 85.38  ? 31  GLY   M C   1 
ATOM   21522 O  O   . GLY   M  13 44  ? 24.573  -148.005 58.803  1.00 83.22  ? 31  GLY   M O   1 
ATOM   21523 N  N   . SER   M  13 45  ? 26.510  -149.232 58.816  1.00 87.46  ? 32  SER   M N   1 
ATOM   21524 C  CA  . SER   M  13 45  ? 26.029  -150.378 59.636  1.00 88.58  ? 32  SER   M CA  1 
ATOM   21525 C  C   . SER   M  13 45  ? 26.230  -150.102 61.133  1.00 88.42  ? 32  SER   M C   1 
ATOM   21526 O  O   . SER   M  13 45  ? 25.583  -150.793 61.942  1.00 85.43  ? 32  SER   M O   1 
ATOM   21527 C  CB  . SER   M  13 45  ? 26.702  -151.659 59.228  1.00 91.57  ? 32  SER   M CB  1 
ATOM   21528 O  OG  . SER   M  13 45  ? 28.077  -151.635 59.576  1.00 96.67  ? 32  SER   M OG  1 
ATOM   21529 N  N   . LEU   M  13 46  ? 27.093  -149.140 61.483  1.00 91.19  ? 33  LEU   M N   1 
ATOM   21530 C  CA  . LEU   M  13 46  ? 27.352  -148.706 62.885  1.00 91.28  ? 33  LEU   M CA  1 
ATOM   21531 C  C   . LEU   M  13 46  ? 26.190  -147.826 63.357  1.00 91.97  ? 33  LEU   M C   1 
ATOM   21532 O  O   . LEU   M  13 46  ? 25.954  -146.776 62.728  1.00 90.34  ? 33  LEU   M O   1 
ATOM   21533 C  CB  . LEU   M  13 46  ? 28.682  -147.945 62.953  1.00 90.85  ? 33  LEU   M CB  1 
ATOM   21534 C  CG  . LEU   M  13 46  ? 28.959  -147.210 64.264  1.00 93.56  ? 33  LEU   M CG  1 
ATOM   21535 C  CD1 . LEU   M  13 46  ? 29.000  -148.179 65.435  1.00 95.79  ? 33  LEU   M CD1 1 
ATOM   21536 C  CD2 . LEU   M  13 46  ? 30.255  -146.417 64.180  1.00 94.26  ? 33  LEU   M CD2 1 
ATOM   21537 N  N   . LEU   M  13 47  ? 25.503  -148.242 64.425  1.00 90.46  ? 34  LEU   M N   1 
ATOM   21538 C  CA  . LEU   M  13 47  ? 24.381  -147.488 65.046  1.00 92.97  ? 34  LEU   M CA  1 
ATOM   21539 C  C   . LEU   M  13 47  ? 24.994  -146.422 65.964  1.00 95.72  ? 34  LEU   M C   1 
ATOM   21540 O  O   . LEU   M  13 47  ? 25.053  -146.652 67.189  1.00 96.24  ? 34  LEU   M O   1 
ATOM   21541 C  CB  . LEU   M  13 47  ? 23.469  -148.460 65.809  1.00 94.00  ? 34  LEU   M CB  1 
ATOM   21542 C  CG  . LEU   M  13 47  ? 23.030  -149.715 65.050  1.00 94.92  ? 34  LEU   M CG  1 
ATOM   21543 C  CD1 . LEU   M  13 47  ? 22.231  -150.640 65.953  1.00 95.68  ? 34  LEU   M CD1 1 
ATOM   21544 C  CD2 . LEU   M  13 47  ? 22.226  -149.370 63.803  1.00 97.96  ? 34  LEU   M CD2 1 
ATOM   21545 N  N   . ARG   M  13 48  ? 25.444  -145.304 65.380  1.00 94.90  ? 35  ARG   M N   1 
ATOM   21546 C  CA  . ARG   M  13 48  ? 26.448  -144.385 65.990  1.00 96.76  ? 35  ARG   M CA  1 
ATOM   21547 C  C   . ARG   M  13 48  ? 25.821  -143.525 67.100  1.00 94.77  ? 35  ARG   M C   1 
ATOM   21548 O  O   . ARG   M  13 48  ? 26.379  -143.532 68.213  1.00 97.86  ? 35  ARG   M O   1 
ATOM   21549 C  CB  . ARG   M  13 48  ? 27.127  -143.526 64.914  1.00 97.29  ? 35  ARG   M CB  1 
ATOM   21550 C  CG  . ARG   M  13 48  ? 28.150  -142.531 65.450  1.00 101.53 ? 35  ARG   M CG  1 
ATOM   21551 C  CD  . ARG   M  13 48  ? 29.291  -143.188 66.212  1.00 105.43 ? 35  ARG   M CD  1 
ATOM   21552 N  NE  . ARG   M  13 48  ? 30.118  -142.252 66.975  1.00 109.33 ? 35  ARG   M NE  1 
ATOM   21553 C  CZ  . ARG   M  13 48  ? 29.907  -141.878 68.241  1.00 107.53 ? 35  ARG   M CZ  1 
ATOM   21554 N  NH1 . ARG   M  13 48  ? 28.870  -142.339 68.923  1.00 108.17 ? 35  ARG   M NH1 1 
ATOM   21555 N  NH2 . ARG   M  13 48  ? 30.740  -141.031 68.823  1.00 104.82 ? 35  ARG   M NH2 1 
ATOM   21556 N  N   . PHE   M  13 49  ? 24.729  -142.803 66.819  1.00 90.91  ? 36  PHE   M N   1 
ATOM   21557 C  CA  . PHE   M  13 49  ? 24.143  -141.771 67.719  1.00 89.99  ? 36  PHE   M CA  1 
ATOM   21558 C  C   . PHE   M  13 49  ? 22.729  -142.175 68.149  1.00 92.30  ? 36  PHE   M C   1 
ATOM   21559 O  O   . PHE   M  13 49  ? 21.943  -142.590 67.282  1.00 88.89  ? 36  PHE   M O   1 
ATOM   21560 C  CB  . PHE   M  13 49  ? 24.140  -140.412 67.018  1.00 89.02  ? 36  PHE   M CB  1 
ATOM   21561 C  CG  . PHE   M  13 49  ? 25.504  -139.966 66.558  1.00 88.48  ? 36  PHE   M CG  1 
ATOM   21562 C  CD1 . PHE   M  13 49  ? 26.518  -139.735 67.475  1.00 88.55  ? 36  PHE   M CD1 1 
ATOM   21563 C  CD2 . PHE   M  13 49  ? 25.781  -139.785 65.210  1.00 88.02  ? 36  PHE   M CD2 1 
ATOM   21564 C  CE1 . PHE   M  13 49  ? 27.776  -139.329 67.055  1.00 88.75  ? 36  PHE   M CE1 1 
ATOM   21565 C  CE2 . PHE   M  13 49  ? 27.039  -139.376 64.793  1.00 87.34  ? 36  PHE   M CE2 1 
ATOM   21566 C  CZ  . PHE   M  13 49  ? 28.035  -139.152 65.716  1.00 87.67  ? 36  PHE   M CZ  1 
ATOM   21567 N  N   . ASN   M  13 50  ? 22.412  -142.020 69.440  1.00 95.36  ? 37  ASN   M N   1 
ATOM   21568 C  CA  . ASN   M  13 50  ? 21.153  -142.522 70.058  1.00 102.58 ? 37  ASN   M CA  1 
ATOM   21569 C  C   . ASN   M  13 50  ? 20.297  -141.386 70.641  1.00 103.11 ? 37  ASN   M C   1 
ATOM   21570 O  O   . ASN   M  13 50  ? 19.177  -141.693 71.097  1.00 109.28 ? 37  ASN   M O   1 
ATOM   21571 C  CB  . ASN   M  13 50  ? 21.450  -143.571 71.134  1.00 109.37 ? 37  ASN   M CB  1 
ATOM   21572 C  CG  . ASN   M  13 50  ? 21.332  -144.993 70.626  1.00 116.46 ? 37  ASN   M CG  1 
ATOM   21573 O  OD1 . ASN   M  13 50  ? 22.283  -145.769 70.709  1.00 119.18 ? 37  ASN   M OD1 1 
ATOM   21574 N  ND2 . ASN   M  13 50  ? 20.167  -145.345 70.100  1.00 119.93 ? 37  ASN   M ND2 1 
ATOM   21575 N  N   . GLY   M  13 51  ? 20.772  -140.136 70.630  1.00 100.48 ? 38  GLY   M N   1 
ATOM   21576 C  CA  . GLY   M  13 51  ? 20.037  -138.986 71.193  1.00 99.84  ? 38  GLY   M CA  1 
ATOM   21577 C  C   . GLY   M  13 51  ? 19.604  -138.001 70.122  1.00 101.06 ? 38  GLY   M C   1 
ATOM   21578 O  O   . GLY   M  13 51  ? 19.554  -136.790 70.430  1.00 103.94 ? 38  GLY   M O   1 
ATOM   21579 N  N   . VAL   M  13 52  ? 19.287  -138.492 68.919  1.00 94.48  ? 39  VAL   M N   1 
ATOM   21580 C  CA  . VAL   M  13 52  ? 18.981  -137.654 67.721  1.00 92.26  ? 39  VAL   M CA  1 
ATOM   21581 C  C   . VAL   M  13 52  ? 17.465  -137.445 67.639  1.00 90.78  ? 39  VAL   M C   1 
ATOM   21582 O  O   . VAL   M  13 52  ? 16.740  -138.443 67.525  1.00 91.37  ? 39  VAL   M O   1 
ATOM   21583 C  CB  . VAL   M  13 52  ? 19.535  -138.288 66.429  1.00 90.97  ? 39  VAL   M CB  1 
ATOM   21584 C  CG1 . VAL   M  13 52  ? 19.260  -137.422 65.208  1.00 91.93  ? 39  VAL   M CG1 1 
ATOM   21585 C  CG2 . VAL   M  13 52  ? 21.023  -138.581 66.540  1.00 90.65  ? 39  VAL   M CG2 1 
ATOM   21586 N  N   . GLU   M  13 53  ? 17.014  -136.189 67.690  1.00 90.36  ? 40  GLU   M N   1 
ATOM   21587 C  CA  . GLU   M  13 53  ? 15.589  -135.805 67.510  1.00 92.29  ? 40  GLU   M CA  1 
ATOM   21588 C  C   . GLU   M  13 53  ? 15.364  -135.454 66.035  1.00 91.44  ? 40  GLU   M C   1 
ATOM   21589 O  O   . GLU   M  13 53  ? 15.971  -134.471 65.566  1.00 91.48  ? 40  GLU   M O   1 
ATOM   21590 C  CB  . GLU   M  13 53  ? 15.225  -134.634 68.424  1.00 93.43  ? 40  GLU   M CB  1 
ATOM   21591 C  CG  . GLU   M  13 53  ? 13.767  -134.230 68.326  1.00 95.27  ? 40  GLU   M CG  1 
ATOM   21592 C  CD  . GLU   M  13 53  ? 12.788  -135.360 68.588  1.00 98.55  ? 40  GLU   M CD  1 
ATOM   21593 O  OE1 . GLU   M  13 53  ? 12.214  -135.883 67.611  1.00 101.36 ? 40  GLU   M OE1 1 
ATOM   21594 O  OE2 . GLU   M  13 53  ? 12.603  -135.711 69.768  1.00 101.28 ? 40  GLU   M OE2 1 
ATOM   21595 N  N   . ARG   M  13 54  ? 14.536  -136.240 65.339  1.00 92.07  ? 41  ARG   M N   1 
ATOM   21596 C  CA  . ARG   M  13 54  ? 14.292  -136.121 63.877  1.00 89.91  ? 41  ARG   M CA  1 
ATOM   21597 C  C   . ARG   M  13 54  ? 12.900  -135.530 63.604  1.00 88.29  ? 41  ARG   M C   1 
ATOM   21598 O  O   . ARG   M  13 54  ? 12.577  -135.334 62.417  1.00 90.23  ? 41  ARG   M O   1 
ATOM   21599 C  CB  . ARG   M  13 54  ? 14.478  -137.487 63.211  1.00 89.55  ? 41  ARG   M CB  1 
ATOM   21600 C  CG  . ARG   M  13 54  ? 15.835  -138.120 63.489  1.00 90.42  ? 41  ARG   M CG  1 
ATOM   21601 C  CD  . ARG   M  13 54  ? 16.208  -139.216 62.509  1.00 90.19  ? 41  ARG   M CD  1 
ATOM   21602 N  NE  . ARG   M  13 54  ? 15.432  -140.435 62.713  1.00 91.59  ? 41  ARG   M NE  1 
ATOM   21603 C  CZ  . ARG   M  13 54  ? 14.467  -140.888 61.913  1.00 90.05  ? 41  ARG   M CZ  1 
ATOM   21604 N  NH1 . ARG   M  13 54  ? 14.125  -140.235 60.814  1.00 87.06  ? 41  ARG   M NH1 1 
ATOM   21605 N  NH2 . ARG   M  13 54  ? 13.843  -142.012 62.220  1.00 92.86  ? 41  ARG   M NH2 1 
ATOM   21606 N  N   . LEU   M  13 55  ? 12.106  -135.260 64.646  1.00 85.41  ? 42  LEU   M N   1 
ATOM   21607 C  CA  . LEU   M  13 55  ? 10.878  -134.423 64.559  1.00 88.37  ? 42  LEU   M CA  1 
ATOM   21608 C  C   . LEU   M  13 55  ? 11.220  -133.013 65.050  1.00 89.63  ? 42  LEU   M C   1 
ATOM   21609 O  O   . LEU   M  13 55  ? 11.695  -132.899 66.197  1.00 91.00  ? 42  LEU   M O   1 
ATOM   21610 C  CB  . LEU   M  13 55  ? 9.766   -135.018 65.429  1.00 86.82  ? 42  LEU   M CB  1 
ATOM   21611 C  CG  . LEU   M  13 55  ? 9.363   -136.461 65.138  1.00 89.02  ? 42  LEU   M CG  1 
ATOM   21612 C  CD1 . LEU   M  13 55  ? 8.390   -136.955 66.198  1.00 88.35  ? 42  LEU   M CD1 1 
ATOM   21613 C  CD2 . LEU   M  13 55  ? 8.752   -136.594 63.750  1.00 89.32  ? 42  LEU   M CD2 1 
ATOM   21614 N  N   . ILE   M  13 56  ? 10.973  -131.984 64.233  1.00 91.82  ? 43  ILE   M N   1 
ATOM   21615 C  CA  . ILE   M  13 56  ? 11.218  -130.559 64.614  1.00 93.01  ? 43  ILE   M CA  1 
ATOM   21616 C  C   . ILE   M  13 56  ? 9.912   -129.775 64.501  1.00 92.19  ? 43  ILE   M C   1 
ATOM   21617 O  O   . ILE   M  13 56  ? 9.336   -129.658 63.421  1.00 85.14  ? 43  ILE   M O   1 
ATOM   21618 C  CB  . ILE   M  13 56  ? 12.378  -129.944 63.802  1.00 92.87  ? 43  ILE   M CB  1 
ATOM   21619 C  CG1 . ILE   M  13 56  ? 12.102  -129.919 62.294  1.00 94.65  ? 43  ILE   M CG1 1 
ATOM   21620 C  CG2 . ILE   M  13 56  ? 13.677  -130.653 64.159  1.00 93.44  ? 43  ILE   M CG2 1 
ATOM   21621 C  CD1 . ILE   M  13 56  ? 13.165  -130.568 61.430  1.00 97.39  ? 43  ILE   M CD1 1 
ATOM   21622 N  N   . PRO   M  13 57  ? 9.390   -129.246 65.633  1.00 94.66  ? 44  PRO   M N   1 
ATOM   21623 C  CA  . PRO   M  13 57  ? 8.189   -128.414 65.621  1.00 96.98  ? 44  PRO   M CA  1 
ATOM   21624 C  C   . PRO   M  13 57  ? 8.481   -126.998 65.097  1.00 98.21  ? 44  PRO   M C   1 
ATOM   21625 O  O   . PRO   M  13 57  ? 9.511   -126.443 65.453  1.00 94.12  ? 44  PRO   M O   1 
ATOM   21626 C  CB  . PRO   M  13 57  ? 7.749   -128.346 67.095  1.00 99.53  ? 44  PRO   M CB  1 
ATOM   21627 C  CG  . PRO   M  13 57  ? 8.662   -129.310 67.839  1.00 97.38  ? 44  PRO   M CG  1 
ATOM   21628 C  CD  . PRO   M  13 57  ? 9.912   -129.425 66.995  1.00 95.52  ? 44  PRO   M CD  1 
ATOM   21629 N  N   . VAL   M  13 58  ? 7.574   -126.461 64.272  1.00 100.14 ? 45  VAL   M N   1 
ATOM   21630 C  CA  . VAL   M  13 58  ? 7.579   -125.049 63.784  1.00 98.66  ? 45  VAL   M CA  1 
ATOM   21631 C  C   . VAL   M  13 58  ? 6.300   -124.379 64.300  1.00 98.87  ? 45  VAL   M C   1 
ATOM   21632 O  O   . VAL   M  13 58  ? 5.207   -124.703 63.788  1.00 94.43  ? 45  VAL   M O   1 
ATOM   21633 C  CB  . VAL   M  13 58  ? 7.691   -124.968 62.249  1.00 96.75  ? 45  VAL   M CB  1 
ATOM   21634 C  CG1 . VAL   M  13 58  ? 7.839   -123.532 61.772  1.00 99.08  ? 45  VAL   M CG1 1 
ATOM   21635 C  CG2 . VAL   M  13 58  ? 8.833   -125.820 61.717  1.00 93.91  ? 45  VAL   M CG2 1 
ATOM   21636 N  N   . GLY   M  13 59  ? 6.435   -123.492 65.289  1.00 102.38 ? 46  GLY   M N   1 
ATOM   21637 C  CA  . GLY   M  13 59  ? 5.298   -122.900 66.017  1.00 106.21 ? 46  GLY   M CA  1 
ATOM   21638 C  C   . GLY   M  13 59  ? 4.561   -123.959 66.820  1.00 108.19 ? 46  GLY   M C   1 
ATOM   21639 O  O   . GLY   M  13 59  ? 5.219   -124.919 67.276  1.00 105.83 ? 46  GLY   M O   1 
ATOM   21640 N  N   . ASP   M  13 60  ? 3.242   -123.810 66.964  1.00 111.73 ? 47  ASP   M N   1 
ATOM   21641 C  CA  . ASP   M  13 60  ? 2.382   -124.689 67.801  1.00 113.38 ? 47  ASP   M CA  1 
ATOM   21642 C  C   . ASP   M  13 60  ? 1.410   -125.479 66.916  1.00 106.66 ? 47  ASP   M C   1 
ATOM   21643 O  O   . ASP   M  13 60  ? 0.502   -126.114 67.485  1.00 111.69 ? 47  ASP   M O   1 
ATOM   21644 C  CB  . ASP   M  13 60  ? 1.613   -123.868 68.840  1.00 123.90 ? 47  ASP   M CB  1 
ATOM   21645 C  CG  . ASP   M  13 60  ? 0.637   -122.866 68.240  1.00 132.30 ? 47  ASP   M CG  1 
ATOM   21646 O  OD1 . ASP   M  13 60  ? 0.798   -122.528 67.047  1.00 142.40 ? 47  ASP   M OD1 1 
ATOM   21647 O  OD2 . ASP   M  13 60  ? -0.276  -122.429 68.969  1.00 143.42 ? 47  ASP   M OD2 1 
ATOM   21648 N  N   . ASN   M  13 61  ? 1.589   -125.445 65.589  1.00 101.07 ? 48  ASN   M N   1 
ATOM   21649 C  CA  . ASN   M  13 61  ? 0.603   -125.992 64.613  1.00 99.00  ? 48  ASN   M CA  1 
ATOM   21650 C  C   . ASN   M  13 61  ? 1.263   -126.856 63.528  1.00 93.52  ? 48  ASN   M C   1 
ATOM   21651 O  O   . ASN   M  13 61  ? 0.517   -127.328 62.654  1.00 93.66  ? 48  ASN   M O   1 
ATOM   21652 C  CB  . ASN   M  13 61  ? -0.245  -124.880 63.984  1.00 101.12 ? 48  ASN   M CB  1 
ATOM   21653 C  CG  . ASN   M  13 61  ? 0.469   -123.980 62.991  1.00 102.96 ? 48  ASN   M CG  1 
ATOM   21654 O  OD1 . ASN   M  13 61  ? -0.193  -123.265 62.242  1.00 107.21 ? 48  ASN   M OD1 1 
ATOM   21655 N  ND2 . ASN   M  13 61  ? 1.795   -123.973 62.962  1.00 101.47 ? 48  ASN   M ND2 1 
ATOM   21656 N  N   . THR   M  13 62  ? 2.584   -127.069 63.570  1.00 92.73  ? 49  THR   M N   1 
ATOM   21657 C  CA  . THR   M  13 62  ? 3.339   -127.851 62.551  1.00 93.41  ? 49  THR   M CA  1 
ATOM   21658 C  C   . THR   M  13 62  ? 4.442   -128.672 63.226  1.00 93.22  ? 49  THR   M C   1 
ATOM   21659 O  O   . THR   M  13 62  ? 5.057   -128.161 64.184  1.00 96.66  ? 49  THR   M O   1 
ATOM   21660 C  CB  . THR   M  13 62  ? 3.956   -126.944 61.477  1.00 91.97  ? 49  THR   M CB  1 
ATOM   21661 O  OG1 . THR   M  13 62  ? 2.970   -126.005 61.050  1.00 94.94  ? 49  THR   M OG1 1 
ATOM   21662 C  CG2 . THR   M  13 62  ? 4.462   -127.714 60.276  1.00 91.72  ? 49  THR   M CG2 1 
ATOM   21663 N  N   . VAL   M  13 63  ? 4.669   -129.896 62.740  1.00 90.46  ? 50  VAL   M N   1 
ATOM   21664 C  CA  . VAL   M  13 63  ? 5.899   -130.698 63.016  1.00 89.48  ? 50  VAL   M CA  1 
ATOM   21665 C  C   . VAL   M  13 63  ? 6.456   -131.194 61.679  1.00 83.11  ? 50  VAL   M C   1 
ATOM   21666 O  O   . VAL   M  13 63  ? 5.676   -131.735 60.875  1.00 84.69  ? 50  VAL   M O   1 
ATOM   21667 C  CB  . VAL   M  13 63  ? 5.634   -131.862 63.990  1.00 90.35  ? 50  VAL   M CB  1 
ATOM   21668 C  CG1 . VAL   M  13 63  ? 6.831   -132.797 64.093  1.00 88.57  ? 50  VAL   M CG1 1 
ATOM   21669 C  CG2 . VAL   M  13 63  ? 5.243   -131.355 65.370  1.00 95.92  ? 50  VAL   M CG2 1 
ATOM   21670 N  N   . VAL   M  13 64  ? 7.756   -130.993 61.456  1.00 81.10  ? 51  VAL   M N   1 
ATOM   21671 C  CA  . VAL   M  13 64  ? 8.495   -131.501 60.266  1.00 82.13  ? 51  VAL   M CA  1 
ATOM   21672 C  C   . VAL   M  13 64  ? 9.297   -132.731 60.699  1.00 83.41  ? 51  VAL   M C   1 
ATOM   21673 O  O   . VAL   M  13 64  ? 10.169  -132.584 61.577  1.00 82.07  ? 51  VAL   M O   1 
ATOM   21674 C  CB  . VAL   M  13 64  ? 9.407   -130.417 59.659  1.00 81.57  ? 51  VAL   M CB  1 
ATOM   21675 C  CG1 . VAL   M  13 64  ? 10.188  -130.941 58.462  1.00 82.04  ? 51  VAL   M CG1 1 
ATOM   21676 C  CG2 . VAL   M  13 64  ? 8.626   -129.167 59.281  1.00 82.56  ? 51  VAL   M CG2 1 
ATOM   21677 N  N   . GLY   M  13 65  ? 8.993   -133.894 60.112  1.00 85.76  ? 52  GLY   M N   1 
ATOM   21678 C  CA  . GLY   M  13 65  ? 9.760   -135.145 60.279  1.00 87.07  ? 52  GLY   M CA  1 
ATOM   21679 C  C   . GLY   M  13 65  ? 10.720  -135.347 59.118  1.00 85.23  ? 52  GLY   M C   1 
ATOM   21680 O  O   . GLY   M  13 65  ? 10.284  -135.186 57.957  1.00 83.20  ? 52  GLY   M O   1 
ATOM   21681 N  N   . ILE   M  13 66  ? 11.984  -135.673 59.410  1.00 84.70  ? 53  ILE   M N   1 
ATOM   21682 C  CA  . ILE   M  13 66  ? 13.077  -135.762 58.395  1.00 85.24  ? 53  ILE   M CA  1 
ATOM   21683 C  C   . ILE   M  13 66  ? 13.845  -137.075 58.569  1.00 84.64  ? 53  ILE   M C   1 
ATOM   21684 O  O   . ILE   M  13 66  ? 14.341  -137.336 59.684  1.00 85.44  ? 53  ILE   M O   1 
ATOM   21685 C  CB  . ILE   M  13 66  ? 14.023  -134.548 58.488  1.00 85.96  ? 53  ILE   M CB  1 
ATOM   21686 C  CG1 . ILE   M  13 66  ? 13.257  -133.226 58.358  1.00 86.36  ? 53  ILE   M CG1 1 
ATOM   21687 C  CG2 . ILE   M  13 66  ? 15.142  -134.678 57.460  1.00 84.52  ? 53  ILE   M CG2 1 
ATOM   21688 C  CD1 . ILE   M  13 66  ? 14.111  -131.981 58.458  1.00 84.51  ? 53  ILE   M CD1 1 
ATOM   21689 N  N   . SER   M  13 67  ? 13.959  -137.842 57.481  1.00 83.89  ? 54  SER   M N   1 
ATOM   21690 C  CA  . SER   M  13 67  ? 14.864  -139.011 57.335  1.00 81.40  ? 54  SER   M CA  1 
ATOM   21691 C  C   . SER   M  13 67  ? 15.988  -138.647 56.358  1.00 77.20  ? 54  SER   M C   1 
ATOM   21692 O  O   . SER   M  13 67  ? 15.888  -137.589 55.708  1.00 73.44  ? 54  SER   M O   1 
ATOM   21693 C  CB  . SER   M  13 67  ? 14.105  -140.236 56.886  1.00 80.65  ? 54  SER   M CB  1 
ATOM   21694 O  OG  . SER   M  13 67  ? 13.332  -139.972 55.727  1.00 82.16  ? 54  SER   M OG  1 
ATOM   21695 N  N   . GLY   M  13 68  ? 17.013  -139.495 56.268  1.00 74.31  ? 55  GLY   M N   1 
ATOM   21696 C  CA  . GLY   M  13 68  ? 18.161  -139.313 55.359  1.00 75.35  ? 55  GLY   M CA  1 
ATOM   21697 C  C   . GLY   M  13 68  ? 19.320  -138.638 56.065  1.00 77.35  ? 55  GLY   M C   1 
ATOM   21698 O  O   . GLY   M  13 68  ? 19.399  -138.761 57.306  1.00 81.06  ? 55  GLY   M O   1 
ATOM   21699 N  N   . ASP   M  13 69  ? 20.176  -137.939 55.311  1.00 78.19  ? 56  ASP   M N   1 
ATOM   21700 C  CA  . ASP   M  13 69  ? 21.438  -137.345 55.830  1.00 82.28  ? 56  ASP   M CA  1 
ATOM   21701 C  C   . ASP   M  13 69  ? 21.109  -136.375 56.974  1.00 83.82  ? 56  ASP   M C   1 
ATOM   21702 O  O   . ASP   M  13 69  ? 20.217  -135.523 56.800  1.00 84.11  ? 56  ASP   M O   1 
ATOM   21703 C  CB  . ASP   M  13 69  ? 22.252  -136.665 54.728  1.00 85.35  ? 56  ASP   M CB  1 
ATOM   21704 C  CG  . ASP   M  13 69  ? 23.620  -136.207 55.211  1.00 88.44  ? 56  ASP   M CG  1 
ATOM   21705 O  OD1 . ASP   M  13 69  ? 24.604  -136.934 54.971  1.00 91.83  ? 56  ASP   M OD1 1 
ATOM   21706 O  OD2 . ASP   M  13 69  ? 23.688  -135.133 55.840  1.00 96.13  ? 56  ASP   M OD2 1 
ATOM   21707 N  N   . ILE   M  13 70  ? 21.816  -136.510 58.100  1.00 85.77  ? 57  ILE   M N   1 
ATOM   21708 C  CA  . ILE   M  13 70  ? 21.560  -135.749 59.359  1.00 86.70  ? 57  ILE   M CA  1 
ATOM   21709 C  C   . ILE   M  13 70  ? 22.192  -134.356 59.255  1.00 84.24  ? 57  ILE   M C   1 
ATOM   21710 O  O   . ILE   M  13 70  ? 21.571  -133.408 59.766  1.00 87.57  ? 57  ILE   M O   1 
ATOM   21711 C  CB  . ILE   M  13 70  ? 22.057  -136.540 60.589  1.00 86.59  ? 57  ILE   M CB  1 
ATOM   21712 C  CG1 . ILE   M  13 70  ? 21.246  -137.822 60.803  1.00 86.10  ? 57  ILE   M CG1 1 
ATOM   21713 C  CG2 . ILE   M  13 70  ? 22.067  -135.674 61.842  1.00 89.42  ? 57  ILE   M CG2 1 
ATOM   21714 C  CD1 . ILE   M  13 70  ? 19.761  -137.600 61.013  1.00 86.60  ? 57  ILE   M CD1 1 
ATOM   21715 N  N   . SER   M  13 71  ? 23.365  -134.222 58.626  1.00 82.69  ? 58  SER   M N   1 
ATOM   21716 C  CA  . SER   M  13 71  ? 24.025  -132.905 58.418  1.00 82.31  ? 58  SER   M CA  1 
ATOM   21717 C  C   . SER   M  13 71  ? 23.082  -132.000 57.614  1.00 82.81  ? 58  SER   M C   1 
ATOM   21718 O  O   . SER   M  13 71  ? 23.008  -130.796 57.930  1.00 84.89  ? 58  SER   M O   1 
ATOM   21719 C  CB  . SER   M  13 71  ? 25.378  -133.028 57.758  1.00 79.57  ? 58  SER   M CB  1 
ATOM   21720 O  OG  . SER   M  13 71  ? 25.252  -133.170 56.352  1.00 79.21  ? 58  SER   M OG  1 
ATOM   21721 N  N   . ASP   M  13 72  ? 22.375  -132.565 56.631  1.00 81.08  ? 59  ASP   M N   1 
ATOM   21722 C  CA  . ASP   M  13 72  ? 21.387  -131.841 55.786  1.00 84.06  ? 59  ASP   M CA  1 
ATOM   21723 C  C   . ASP   M  13 72  ? 20.123  -131.546 56.610  1.00 87.13  ? 59  ASP   M C   1 
ATOM   21724 O  O   . ASP   M  13 72  ? 19.503  -130.491 56.370  1.00 90.14  ? 59  ASP   M O   1 
ATOM   21725 C  CB  . ASP   M  13 72  ? 21.074  -132.613 54.499  1.00 85.21  ? 59  ASP   M CB  1 
ATOM   21726 C  CG  . ASP   M  13 72  ? 22.192  -132.601 53.464  1.00 86.08  ? 59  ASP   M CG  1 
ATOM   21727 O  OD1 . ASP   M  13 72  ? 23.044  -131.689 53.521  1.00 87.03  ? 59  ASP   M OD1 1 
ATOM   21728 O  OD2 . ASP   M  13 72  ? 22.199  -133.504 52.596  1.00 86.93  ? 59  ASP   M OD2 1 
ATOM   21729 N  N   . MET   M  13 73  ? 19.750  -132.438 57.534  1.00 85.51  ? 60  MET   M N   1 
ATOM   21730 C  CA  . MET   M  13 73  ? 18.606  -132.248 58.470  1.00 86.13  ? 60  MET   M CA  1 
ATOM   21731 C  C   . MET   M  13 73  ? 18.876  -131.031 59.364  1.00 84.31  ? 60  MET   M C   1 
ATOM   21732 O  O   . MET   M  13 73  ? 17.963  -130.198 59.527  1.00 87.40  ? 60  MET   M O   1 
ATOM   21733 C  CB  . MET   M  13 73  ? 18.399  -133.484 59.352  1.00 86.08  ? 60  MET   M CB  1 
ATOM   21734 C  CG  . MET   M  13 73  ? 17.164  -133.413 60.229  1.00 86.60  ? 60  MET   M CG  1 
ATOM   21735 S  SD  . MET   M  13 73  ? 17.059  -134.816 61.363  1.00 88.72  ? 60  MET   M SD  1 
ATOM   21736 C  CE  . MET   M  13 73  ? 17.977  -134.179 62.763  1.00 90.48  ? 60  MET   M CE  1 
ATOM   21737 N  N   . GLN   M  13 74  ? 20.086  -130.947 59.923  1.00 80.28  ? 61  GLN   M N   1 
ATOM   21738 C  CA  . GLN   M  13 74  ? 20.519  -129.858 60.840  1.00 81.78  ? 61  GLN   M CA  1 
ATOM   21739 C  C   . GLN   M  13 74  ? 20.532  -128.523 60.086  1.00 82.92  ? 61  GLN   M C   1 
ATOM   21740 O  O   . GLN   M  13 74  ? 20.246  -127.492 60.721  1.00 84.84  ? 61  GLN   M O   1 
ATOM   21741 C  CB  . GLN   M  13 74  ? 21.893  -130.179 61.427  1.00 80.47  ? 61  GLN   M CB  1 
ATOM   21742 C  CG  . GLN   M  13 74  ? 21.870  -131.348 62.400  1.00 79.75  ? 61  GLN   M CG  1 
ATOM   21743 C  CD  . GLN   M  13 74  ? 23.237  -131.669 62.950  1.00 79.64  ? 61  GLN   M CD  1 
ATOM   21744 O  OE1 . GLN   M  13 74  ? 24.250  -131.130 62.512  1.00 81.35  ? 61  GLN   M OE1 1 
ATOM   21745 N  NE2 . GLN   M  13 74  ? 23.275  -132.563 63.924  1.00 81.05  ? 61  GLN   M NE2 1 
ATOM   21746 N  N   . HIS   M  13 75  ? 20.858  -128.547 58.788  1.00 84.81  ? 62  HIS   M N   1 
ATOM   21747 C  CA  . HIS   M  13 75  ? 20.788  -127.370 57.882  1.00 83.19  ? 62  HIS   M CA  1 
ATOM   21748 C  C   . HIS   M  13 75  ? 19.326  -126.934 57.741  1.00 86.27  ? 62  HIS   M C   1 
ATOM   21749 O  O   . HIS   M  13 75  ? 19.065  -125.724 57.864  1.00 92.32  ? 62  HIS   M O   1 
ATOM   21750 C  CB  . HIS   M  13 75  ? 21.440  -127.670 56.526  1.00 83.45  ? 62  HIS   M CB  1 
ATOM   21751 C  CG  . HIS   M  13 75  ? 21.243  -126.589 55.517  1.00 83.75  ? 62  HIS   M CG  1 
ATOM   21752 N  ND1 . HIS   M  13 75  ? 21.872  -125.362 55.615  1.00 84.02  ? 62  HIS   M ND1 1 
ATOM   21753 C  CD2 . HIS   M  13 75  ? 20.487  -126.541 54.400  1.00 85.36  ? 62  HIS   M CD2 1 
ATOM   21754 C  CE1 . HIS   M  13 75  ? 21.512  -124.606 54.598  1.00 85.65  ? 62  HIS   M CE1 1 
ATOM   21755 N  NE2 . HIS   M  13 75  ? 20.662  -125.305 53.838  1.00 86.59  ? 62  HIS   M NE2 1 
ATOM   21756 N  N   . ILE   M  13 76  ? 18.415  -127.883 57.506  1.00 81.99  ? 63  ILE   M N   1 
ATOM   21757 C  CA  . ILE   M  13 76  ? 16.953  -127.623 57.334  1.00 83.76  ? 63  ILE   M CA  1 
ATOM   21758 C  C   . ILE   M  13 76  ? 16.367  -127.117 58.659  1.00 85.44  ? 63  ILE   M C   1 
ATOM   21759 O  O   . ILE   M  13 76  ? 15.449  -126.278 58.603  1.00 89.00  ? 63  ILE   M O   1 
ATOM   21760 C  CB  . ILE   M  13 76  ? 16.222  -128.877 56.812  1.00 84.15  ? 63  ILE   M CB  1 
ATOM   21761 C  CG1 . ILE   M  13 76  ? 16.635  -129.200 55.374  1.00 85.75  ? 63  ILE   M CG1 1 
ATOM   21762 C  CG2 . ILE   M  13 76  ? 14.712  -128.726 56.934  1.00 85.19  ? 63  ILE   M CG2 1 
ATOM   21763 C  CD1 . ILE   M  13 76  ? 16.404  -130.638 54.980  1.00 86.20  ? 63  ILE   M CD1 1 
ATOM   21764 N  N   . GLU   M  13 77  ? 16.862  -127.615 59.798  1.00 85.78  ? 64  GLU   M N   1 
ATOM   21765 C  CA  . GLU   M  13 77  ? 16.505  -127.111 61.154  1.00 89.98  ? 64  GLU   M CA  1 
ATOM   21766 C  C   . GLU   M  13 77  ? 16.756  -125.601 61.224  1.00 88.43  ? 64  GLU   M C   1 
ATOM   21767 O  O   . GLU   M  13 77  ? 15.849  -124.861 61.657  1.00 86.11  ? 64  GLU   M O   1 
ATOM   21768 C  CB  . GLU   M  13 77  ? 17.337  -127.795 62.240  1.00 93.65  ? 64  GLU   M CB  1 
ATOM   21769 C  CG  . GLU   M  13 77  ? 16.684  -129.028 62.830  1.00 97.90  ? 64  GLU   M CG  1 
ATOM   21770 C  CD  . GLU   M  13 77  ? 17.311  -129.503 64.131  1.00 101.05 ? 64  GLU   M CD  1 
ATOM   21771 O  OE1 . GLU   M  13 77  ? 17.850  -130.631 64.154  1.00 104.19 ? 64  GLU   M OE1 1 
ATOM   21772 O  OE2 . GLU   M  13 77  ? 17.254  -128.744 65.123  1.00 100.51 ? 64  GLU   M OE2 1 
ATOM   21773 N  N   . ARG   M  13 78  ? 17.956  -125.181 60.817  1.00 90.36  ? 65  ARG   M N   1 
ATOM   21774 C  CA  . ARG   M  13 78  ? 18.418  -123.770 60.850  1.00 93.51  ? 65  ARG   M CA  1 
ATOM   21775 C  C   . ARG   M  13 78  ? 17.560  -122.926 59.895  1.00 92.43  ? 65  ARG   M C   1 
ATOM   21776 O  O   . ARG   M  13 78  ? 17.273  -121.767 60.250  1.00 94.33  ? 65  ARG   M O   1 
ATOM   21777 C  CB  . ARG   M  13 78  ? 19.907  -123.693 60.498  1.00 99.50  ? 65  ARG   M CB  1 
ATOM   21778 C  CG  . ARG   M  13 78  ? 20.638  -122.533 61.158  1.00 107.87 ? 65  ARG   M CG  1 
ATOM   21779 C  CD  . ARG   M  13 78  ? 21.882  -122.147 60.383  1.00 117.79 ? 65  ARG   M CD  1 
ATOM   21780 N  NE  . ARG   M  13 78  ? 21.528  -121.460 59.145  1.00 123.45 ? 65  ARG   M NE  1 
ATOM   21781 C  CZ  . ARG   M  13 78  ? 22.116  -121.634 57.962  1.00 125.80 ? 65  ARG   M CZ  1 
ATOM   21782 N  NH1 . ARG   M  13 78  ? 23.108  -122.500 57.815  1.00 128.24 ? 65  ARG   M NH1 1 
ATOM   21783 N  NH2 . ARG   M  13 78  ? 21.695  -120.942 56.916  1.00 126.44 ? 65  ARG   M NH2 1 
ATOM   21784 N  N   . LEU   M  13 79  ? 17.162  -123.478 58.742  1.00 86.85  ? 66  LEU   M N   1 
ATOM   21785 C  CA  . LEU   M  13 79  ? 16.338  -122.770 57.720  1.00 87.25  ? 66  LEU   M CA  1 
ATOM   21786 C  C   . LEU   M  13 79  ? 14.944  -122.480 58.289  1.00 86.59  ? 66  LEU   M C   1 
ATOM   21787 O  O   . LEU   M  13 79  ? 14.443  -121.365 58.057  1.00 83.02  ? 66  LEU   M O   1 
ATOM   21788 C  CB  . LEU   M  13 79  ? 16.225  -123.605 56.438  1.00 86.77  ? 66  LEU   M CB  1 
ATOM   21789 C  CG  . LEU   M  13 79  ? 17.476  -123.694 55.562  1.00 88.10  ? 66  LEU   M CG  1 
ATOM   21790 C  CD1 . LEU   M  13 79  ? 17.240  -124.637 54.393  1.00 86.76  ? 66  LEU   M CD1 1 
ATOM   21791 C  CD2 . LEU   M  13 79  ? 17.902  -122.326 55.047  1.00 90.93  ? 66  LEU   M CD2 1 
ATOM   21792 N  N   . LEU   M  13 80  ? 14.334  -123.456 58.969  1.00 88.29  ? 67  LEU   M N   1 
ATOM   21793 C  CA  . LEU   M  13 80  ? 12.990  -123.328 59.601  1.00 91.00  ? 67  LEU   M CA  1 
ATOM   21794 C  C   . LEU   M  13 80  ? 13.065  -122.340 60.771  1.00 93.82  ? 67  LEU   M C   1 
ATOM   21795 O  O   . LEU   M  13 80  ? 12.164  -121.487 60.889  1.00 95.29  ? 67  LEU   M O   1 
ATOM   21796 C  CB  . LEU   M  13 80  ? 12.516  -124.704 60.079  1.00 90.70  ? 67  LEU   M CB  1 
ATOM   21797 C  CG  . LEU   M  13 80  ? 12.161  -125.700 58.978  1.00 91.14  ? 67  LEU   M CG  1 
ATOM   21798 C  CD1 . LEU   M  13 80  ? 11.995  -127.099 59.551  1.00 91.59  ? 67  LEU   M CD1 1 
ATOM   21799 C  CD2 . LEU   M  13 80  ? 10.901  -125.270 58.239  1.00 92.20  ? 67  LEU   M CD2 1 
ATOM   21800 N  N   . LYS   M  13 81  ? 14.095  -122.473 61.609  1.00 98.80  ? 68  LYS   M N   1 
ATOM   21801 C  CA  . LYS   M  13 81  ? 14.385  -121.567 62.753  1.00 103.41 ? 68  LYS   M CA  1 
ATOM   21802 C  C   . LYS   M  13 81  ? 14.436  -120.118 62.247  1.00 99.38  ? 68  LYS   M C   1 
ATOM   21803 O  O   . LYS   M  13 81  ? 13.833  -119.245 62.900  1.00 99.56  ? 68  LYS   M O   1 
ATOM   21804 C  CB  . LYS   M  13 81  ? 15.690  -122.012 63.422  1.00 111.41 ? 68  LYS   M CB  1 
ATOM   21805 C  CG  . LYS   M  13 81  ? 16.313  -121.034 64.410  1.00 117.31 ? 68  LYS   M CG  1 
ATOM   21806 C  CD  . LYS   M  13 81  ? 17.633  -121.531 64.966  1.00 122.55 ? 68  LYS   M CD  1 
ATOM   21807 C  CE  . LYS   M  13 81  ? 18.480  -120.439 65.586  1.00 123.15 ? 68  LYS   M CE  1 
ATOM   21808 N  NZ  . LYS   M  13 81  ? 17.895  -119.936 66.853  1.00 123.29 ? 68  LYS   M NZ  1 
ATOM   21809 N  N   . ASP   M  13 82  ? 15.116  -119.884 61.119  1.00 95.68  ? 69  ASP   M N   1 
ATOM   21810 C  CA  . ASP   M  13 82  ? 15.275  -118.547 60.489  1.00 96.31  ? 69  ASP   M CA  1 
ATOM   21811 C  C   . ASP   M  13 82  ? 13.927  -118.078 59.928  1.00 92.71  ? 69  ASP   M C   1 
ATOM   21812 O  O   . ASP   M  13 82  ? 13.631  -116.882 60.055  1.00 95.09  ? 69  ASP   M O   1 
ATOM   21813 C  CB  . ASP   M  13 82  ? 16.350  -118.565 59.400  1.00 104.90 ? 69  ASP   M CB  1 
ATOM   21814 C  CG  . ASP   M  13 82  ? 16.670  -117.188 58.845  1.00 116.32 ? 69  ASP   M CG  1 
ATOM   21815 O  OD1 . ASP   M  13 82  ? 17.366  -116.421 59.547  1.00 132.20 ? 69  ASP   M OD1 1 
ATOM   21816 O  OD2 . ASP   M  13 82  ? 16.206  -116.884 57.725  1.00 129.38 ? 69  ASP   M OD2 1 
ATOM   21817 N  N   . LEU   M  13 83  ? 13.147  -118.981 59.330  1.00 85.47  ? 70  LEU   M N   1 
ATOM   21818 C  CA  . LEU   M  13 83  ? 11.820  -118.673 58.726  1.00 86.77  ? 70  LEU   M CA  1 
ATOM   21819 C  C   . LEU   M  13 83  ? 10.891  -118.106 59.807  1.00 86.18  ? 70  LEU   M C   1 
ATOM   21820 O  O   . LEU   M  13 83  ? 10.124  -117.183 59.495  1.00 92.39  ? 70  LEU   M O   1 
ATOM   21821 C  CB  . LEU   M  13 83  ? 11.218  -119.943 58.112  1.00 87.99  ? 70  LEU   M CB  1 
ATOM   21822 C  CG  . LEU   M  13 83  ? 10.431  -119.775 56.810  1.00 90.58  ? 70  LEU   M CG  1 
ATOM   21823 C  CD1 . LEU   M  13 83  ? 9.579   -121.006 56.543  1.00 92.56  ? 70  LEU   M CD1 1 
ATOM   21824 C  CD2 . LEU   M  13 83  ? 9.552   -118.534 56.824  1.00 92.33  ? 70  LEU   M CD2 1 
ATOM   21825 N  N   . VAL   M  13 84  ? 10.951  -118.651 61.025  1.00 87.18  ? 71  VAL   M N   1 
ATOM   21826 C  CA  . VAL   M  13 84  ? 10.152  -118.185 62.200  1.00 89.45  ? 71  VAL   M CA  1 
ATOM   21827 C  C   . VAL   M  13 84  ? 10.560  -116.747 62.532  1.00 88.80  ? 71  VAL   M C   1 
ATOM   21828 O  O   . VAL   M  13 84  ? 9.657   -115.903 62.698  1.00 88.10  ? 71  VAL   M O   1 
ATOM   21829 C  CB  . VAL   M  13 84  ? 10.340  -119.104 63.423  1.00 90.78  ? 71  VAL   M CB  1 
ATOM   21830 C  CG1 . VAL   M  13 84  ? 9.725   -118.507 64.682  1.00 89.42  ? 71  VAL   M CG1 1 
ATOM   21831 C  CG2 . VAL   M  13 84  ? 9.793   -120.503 63.170  1.00 90.82  ? 71  VAL   M CG2 1 
ATOM   21832 N  N   . THR   M  13 85  ? 11.870  -116.500 62.641  1.00 91.09  ? 72  THR   M N   1 
ATOM   21833 C  CA  . THR   M  13 85  ? 12.471  -115.173 62.943  1.00 94.92  ? 72  THR   M CA  1 
ATOM   21834 C  C   . THR   M  13 85  ? 12.024  -114.157 61.885  1.00 95.69  ? 72  THR   M C   1 
ATOM   21835 O  O   . THR   M  13 85  ? 11.539  -113.072 62.274  1.00 104.80 ? 72  THR   M O   1 
ATOM   21836 C  CB  . THR   M  13 85  ? 14.004  -115.244 62.997  1.00 95.34  ? 72  THR   M CB  1 
ATOM   21837 O  OG1 . THR   M  13 85  ? 14.380  -116.312 63.868  1.00 94.77  ? 72  THR   M OG1 1 
ATOM   21838 C  CG2 . THR   M  13 85  ? 14.636  -113.952 63.468  1.00 96.87  ? 72  THR   M CG2 1 
ATOM   21839 N  N   . GLU   M  13 86  ? 12.184  -114.503 60.605  1.00 90.66  ? 73  GLU   M N   1 
ATOM   21840 C  CA  . GLU   M  13 86  ? 11.943  -113.597 59.451  1.00 91.96  ? 73  GLU   M CA  1 
ATOM   21841 C  C   . GLU   M  13 86  ? 10.451  -113.250 59.379  1.00 91.12  ? 73  GLU   M C   1 
ATOM   21842 O  O   . GLU   M  13 86  ? 10.139  -112.088 59.054  1.00 93.17  ? 73  GLU   M O   1 
ATOM   21843 C  CB  . GLU   M  13 86  ? 12.429  -114.236 58.149  1.00 92.74  ? 73  GLU   M CB  1 
ATOM   21844 C  CG  . GLU   M  13 86  ? 12.988  -113.230 57.159  1.00 96.72  ? 73  GLU   M CG  1 
ATOM   21845 C  CD  . GLU   M  13 86  ? 14.424  -112.810 57.425  1.00 97.67  ? 73  GLU   M CD  1 
ATOM   21846 O  OE1 . GLU   M  13 86  ? 14.754  -111.643 57.139  1.00 103.41 ? 73  GLU   M OE1 1 
ATOM   21847 O  OE2 . GLU   M  13 86  ? 15.211  -113.655 57.908  1.00 96.65  ? 73  GLU   M OE2 1 
ATOM   21848 N  N   . ASN   M  13 87  ? 9.576   -114.218 59.676  1.00 87.86  ? 74  ASN   M N   1 
ATOM   21849 C  CA  . ASN   M  13 87  ? 8.096   -114.057 59.646  1.00 88.97  ? 74  ASN   M CA  1 
ATOM   21850 C  C   . ASN   M  13 87  ? 7.663   -113.056 60.725  1.00 91.53  ? 74  ASN   M C   1 
ATOM   21851 O  O   . ASN   M  13 87  ? 6.711   -112.292 60.472  1.00 92.93  ? 74  ASN   M O   1 
ATOM   21852 C  CB  . ASN   M  13 87  ? 7.367   -115.390 59.834  1.00 87.35  ? 74  ASN   M CB  1 
ATOM   21853 C  CG  . ASN   M  13 87  ? 5.861   -115.246 59.771  1.00 87.33  ? 74  ASN   M CG  1 
ATOM   21854 O  OD1 . ASN   M  13 87  ? 5.300   -115.016 58.704  1.00 90.92  ? 74  ASN   M OD1 1 
ATOM   21855 N  ND2 . ASN   M  13 87  ? 5.194   -115.371 60.906  1.00 89.38  ? 74  ASN   M ND2 1 
ATOM   21856 N  N   . ALA   M  13 88  ? 8.338   -113.066 61.878  1.00 92.63  ? 75  ALA   M N   1 
ATOM   21857 C  CA  . ALA   M  13 88  ? 8.024   -112.217 63.051  1.00 94.77  ? 75  ALA   M CA  1 
ATOM   21858 C  C   . ALA   M  13 88  ? 8.367   -110.749 62.764  1.00 97.16  ? 75  ALA   M C   1 
ATOM   21859 O  O   . ALA   M  13 88  ? 7.771   -109.879 63.429  1.00 98.12  ? 75  ALA   M O   1 
ATOM   21860 C  CB  . ALA   M  13 88  ? 8.757   -112.722 64.269  1.00 95.95  ? 75  ALA   M CB  1 
ATOM   21861 N  N   . TYR   M  13 89  ? 9.285   -110.483 61.824  1.00 96.06  ? 76  TYR   M N   1 
ATOM   21862 C  CA  . TYR   M  13 89  ? 9.762   -109.116 61.470  1.00 96.14  ? 76  TYR   M CA  1 
ATOM   21863 C  C   . TYR   M  13 89  ? 8.609   -108.280 60.898  1.00 100.09 ? 76  TYR   M C   1 
ATOM   21864 O  O   . TYR   M  13 89  ? 7.954   -108.729 59.933  1.00 101.48 ? 76  TYR   M O   1 
ATOM   21865 C  CB  . TYR   M  13 89  ? 10.910  -109.156 60.456  1.00 93.48  ? 76  TYR   M CB  1 
ATOM   21866 C  CG  . TYR   M  13 89  ? 12.253  -109.615 60.973  1.00 93.25  ? 76  TYR   M CG  1 
ATOM   21867 C  CD1 . TYR   M  13 89  ? 12.603  -109.506 62.312  1.00 92.80  ? 76  TYR   M CD1 1 
ATOM   21868 C  CD2 . TYR   M  13 89  ? 13.206  -110.120 60.100  1.00 91.02  ? 76  TYR   M CD2 1 
ATOM   21869 C  CE1 . TYR   M  13 89  ? 13.845  -109.917 62.772  1.00 91.20  ? 76  TYR   M CE1 1 
ATOM   21870 C  CE2 . TYR   M  13 89  ? 14.453  -110.530 60.542  1.00 88.30  ? 76  TYR   M CE2 1 
ATOM   21871 C  CZ  . TYR   M  13 89  ? 14.775  -110.430 61.883  1.00 88.42  ? 76  TYR   M CZ  1 
ATOM   21872 O  OH  . TYR   M  13 89  ? 16.008  -110.830 62.308  1.00 87.74  ? 76  TYR   M OH  1 
ATOM   21873 N  N   . ASP   M  13 90  ? 8.389   -107.094 61.479  1.00 100.13 ? 77  ASP   M N   1 
ATOM   21874 C  CA  . ASP   M  13 90  ? 7.384   -106.089 61.036  1.00 100.98 ? 77  ASP   M CA  1 
ATOM   21875 C  C   . ASP   M  13 90  ? 6.032   -106.784 60.851  1.00 102.29 ? 77  ASP   M C   1 
ATOM   21876 O  O   . ASP   M  13 90  ? 5.359   -106.525 59.830  1.00 102.01 ? 77  ASP   M O   1 
ATOM   21877 C  CB  . ASP   M  13 90  ? 7.856   -105.386 59.761  1.00 102.47 ? 77  ASP   M CB  1 
ATOM   21878 C  CG  . ASP   M  13 90  ? 9.287   -104.879 59.842  1.00 100.79 ? 77  ASP   M CG  1 
ATOM   21879 O  OD1 . ASP   M  13 90  ? 9.737   -104.554 60.959  1.00 100.92 ? 77  ASP   M OD1 1 
ATOM   21880 O  OD2 . ASP   M  13 90  ? 9.945   -104.819 58.785  1.00 101.14 ? 77  ASP   M OD2 1 
ATOM   21881 N  N   . ASN   M  13 91  ? 5.666   -107.640 61.810  1.00 101.39 ? 78  ASN   M N   1 
ATOM   21882 C  CA  . ASN   M  13 91  ? 4.453   -108.495 61.767  1.00 101.24 ? 78  ASN   M CA  1 
ATOM   21883 C  C   . ASN   M  13 91  ? 3.776   -108.453 63.134  1.00 100.51 ? 78  ASN   M C   1 
ATOM   21884 O  O   . ASN   M  13 91  ? 4.072   -109.272 64.002  1.00 92.83  ? 78  ASN   M O   1 
ATOM   21885 C  CB  . ASN   M  13 91  ? 4.802   -109.919 61.330  1.00 99.47  ? 78  ASN   M CB  1 
ATOM   21886 C  CG  . ASN   M  13 91  ? 3.584   -110.752 60.998  1.00 102.90 ? 78  ASN   M CG  1 
ATOM   21887 O  OD1 . ASN   M  13 91  ? 2.484   -110.223 60.844  1.00 102.72 ? 78  ASN   M OD1 1 
ATOM   21888 N  ND2 . ASN   M  13 91  ? 3.772   -112.057 60.882  1.00 104.92 ? 78  ASN   M ND2 1 
ATOM   21889 N  N   . PRO   M  13 92  ? 2.859   -107.485 63.370  1.00 105.20 ? 79  PRO   M N   1 
ATOM   21890 C  CA  . PRO   M  13 92  ? 2.114   -107.415 64.628  1.00 107.33 ? 79  PRO   M CA  1 
ATOM   21891 C  C   . PRO   M  13 92  ? 1.239   -108.651 64.892  1.00 108.47 ? 79  PRO   M C   1 
ATOM   21892 O  O   . PRO   M  13 92  ? 0.895   -108.868 66.038  1.00 107.33 ? 79  PRO   M O   1 
ATOM   21893 C  CB  . PRO   M  13 92  ? 1.221   -106.173 64.470  1.00 108.80 ? 79  PRO   M CB  1 
ATOM   21894 C  CG  . PRO   M  13 92  ? 1.875   -105.365 63.367  1.00 109.43 ? 79  PRO   M CG  1 
ATOM   21895 C  CD  . PRO   M  13 92  ? 2.509   -106.390 62.452  1.00 106.37 ? 79  PRO   M CD  1 
ATOM   21896 N  N   . LEU   M  13 93  ? 0.906   -109.415 63.843  1.00 111.38 ? 80  LEU   M N   1 
ATOM   21897 C  CA  . LEU   M  13 93  ? 0.017   -110.609 63.906  1.00 114.13 ? 80  LEU   M CA  1 
ATOM   21898 C  C   . LEU   M  13 93  ? 0.831   -111.900 63.709  1.00 115.19 ? 80  LEU   M C   1 
ATOM   21899 O  O   . LEU   M  13 93  ? 0.279   -112.863 63.133  1.00 115.96 ? 80  LEU   M O   1 
ATOM   21900 C  CB  . LEU   M  13 93  ? -1.062  -110.469 62.825  1.00 112.43 ? 80  LEU   M CB  1 
ATOM   21901 C  CG  . LEU   M  13 93  ? -1.856  -109.164 62.835  1.00 113.64 ? 80  LEU   M CG  1 
ATOM   21902 C  CD1 . LEU   M  13 93  ? -2.722  -109.053 61.589  1.00 114.87 ? 80  LEU   M CD1 1 
ATOM   21903 C  CD2 . LEU   M  13 93  ? -2.708  -109.054 64.089  1.00 111.61 ? 80  LEU   M CD2 1 
ATOM   21904 N  N   . ALA   M  13 94  ? 2.077   -111.940 64.194  1.00 116.46 ? 81  ALA   M N   1 
ATOM   21905 C  CA  . ALA   M  13 94  ? 3.014   -113.081 64.028  1.00 113.34 ? 81  ALA   M CA  1 
ATOM   21906 C  C   . ALA   M  13 94  ? 2.557   -114.288 64.861  1.00 110.56 ? 81  ALA   M C   1 
ATOM   21907 O  O   . ALA   M  13 94  ? 2.966   -115.417 64.527  1.00 106.48 ? 81  ALA   M O   1 
ATOM   21908 C  CB  . ALA   M  13 94  ? 4.415   -112.661 64.401  1.00 116.67 ? 81  ALA   M CB  1 
ATOM   21909 N  N   . ASP   M  13 95  ? 1.757   -114.057 65.908  1.00 111.43 ? 82  ASP   M N   1 
ATOM   21910 C  CA  . ASP   M  13 95  ? 1.222   -115.111 66.813  1.00 111.40 ? 82  ASP   M CA  1 
ATOM   21911 C  C   . ASP   M  13 95  ? -0.302  -115.216 66.651  1.00 109.29 ? 82  ASP   M C   1 
ATOM   21912 O  O   . ASP   M  13 95  ? -0.945  -115.766 67.565  1.00 110.24 ? 82  ASP   M O   1 
ATOM   21913 C  CB  . ASP   M  13 95  ? 1.606   -114.830 68.270  1.00 114.36 ? 82  ASP   M CB  1 
ATOM   21914 C  CG  . ASP   M  13 95  ? 1.159   -113.471 68.786  1.00 118.91 ? 82  ASP   M CG  1 
ATOM   21915 O  OD1 . ASP   M  13 95  ? 0.935   -112.568 67.953  1.00 121.95 ? 82  ASP   M OD1 1 
ATOM   21916 O  OD2 . ASP   M  13 95  ? 1.038   -113.325 70.018  1.00 122.87 ? 82  ASP   M OD2 1 
ATOM   21917 N  N   . ALA   M  13 96  ? -0.857  -114.721 65.538  1.00 109.61 ? 83  ALA   M N   1 
ATOM   21918 C  CA  . ALA   M  13 96  ? -2.314  -114.709 65.257  1.00 112.08 ? 83  ALA   M CA  1 
ATOM   21919 C  C   . ALA   M  13 96  ? -2.573  -115.062 63.784  1.00 114.27 ? 83  ALA   M C   1 
ATOM   21920 O  O   . ALA   M  13 96  ? -2.232  -116.195 63.401  1.00 120.48 ? 83  ALA   M O   1 
ATOM   21921 C  CB  . ALA   M  13 96  ? -2.896  -113.372 65.652  1.00 112.77 ? 83  ALA   M CB  1 
ATOM   21922 N  N   . GLU   M  13 97  ? -3.146  -114.145 62.993  1.00 114.56 ? 84  GLU   M N   1 
ATOM   21923 C  CA  . GLU   M  13 97  ? -3.625  -114.411 61.606  1.00 114.60 ? 84  GLU   M CA  1 
ATOM   21924 C  C   . GLU   M  13 97  ? -2.441  -114.633 60.655  1.00 109.23 ? 84  GLU   M C   1 
ATOM   21925 O  O   . GLU   M  13 97  ? -2.625  -115.377 59.667  1.00 105.57 ? 84  GLU   M O   1 
ATOM   21926 C  CB  . GLU   M  13 97  ? -4.491  -113.260 61.086  1.00 117.35 ? 84  GLU   M CB  1 
ATOM   21927 C  CG  . GLU   M  13 97  ? -5.840  -113.140 61.776  1.00 122.05 ? 84  GLU   M CG  1 
ATOM   21928 C  CD  . GLU   M  13 97  ? -5.911  -112.112 62.893  1.00 125.79 ? 84  GLU   M CD  1 
ATOM   21929 O  OE1 . GLU   M  13 97  ? -6.989  -111.509 63.067  1.00 129.27 ? 84  GLU   M OE1 1 
ATOM   21930 O  OE2 . GLU   M  13 97  ? -4.893  -111.916 63.585  1.00 126.71 ? 84  GLU   M OE2 1 
ATOM   21931 N  N   . GLU   M  13 98  ? -1.288  -114.008 60.930  1.00 107.85 ? 85  GLU   M N   1 
ATOM   21932 C  CA  . GLU   M  13 98  ? -0.077  -114.054 60.064  1.00 103.89 ? 85  GLU   M CA  1 
ATOM   21933 C  C   . GLU   M  13 98  ? 1.011   -114.924 60.715  1.00 103.94 ? 85  GLU   M C   1 
ATOM   21934 O  O   . GLU   M  13 98  ? 2.205   -114.654 60.475  1.00 98.80  ? 85  GLU   M O   1 
ATOM   21935 C  CB  . GLU   M  13 98  ? 0.434   -112.638 59.785  1.00 104.37 ? 85  GLU   M CB  1 
ATOM   21936 C  CG  . GLU   M  13 98  ? -0.545  -111.768 59.013  1.00 103.53 ? 85  GLU   M CG  1 
ATOM   21937 C  CD  . GLU   M  13 98  ? -0.767  -112.161 57.561  1.00 102.19 ? 85  GLU   M CD  1 
ATOM   21938 O  OE1 . GLU   M  13 98  ? -1.790  -111.738 56.981  1.00 103.69 ? 85  GLU   M OE1 1 
ATOM   21939 O  OE2 . GLU   M  13 98  ? 0.088   -112.875 57.004  1.00 100.00 ? 85  GLU   M OE2 1 
ATOM   21940 N  N   . ALA   M  13 99  ? 0.617   -115.939 61.491  1.00 104.67 ? 86  ALA   M N   1 
ATOM   21941 C  CA  . ALA   M  13 99  ? 1.515   -117.007 61.992  1.00 105.26 ? 86  ALA   M CA  1 
ATOM   21942 C  C   . ALA   M  13 99  ? 1.804   -117.977 60.841  1.00 104.57 ? 86  ALA   M C   1 
ATOM   21943 O  O   . ALA   M  13 99  ? 0.976   -118.046 59.905  1.00 108.65 ? 86  ALA   M O   1 
ATOM   21944 C  CB  . ALA   M  13 99  ? 0.894   -117.711 63.174  1.00 106.56 ? 86  ALA   M CB  1 
ATOM   21945 N  N   . LEU   M  13 100 ? 2.936   -118.685 60.898  1.00 98.17  ? 87  LEU   M N   1 
ATOM   21946 C  CA  . LEU   M  13 100 ? 3.349   -119.651 59.845  1.00 95.31  ? 87  LEU   M CA  1 
ATOM   21947 C  C   . LEU   M  13 100 ? 2.373   -120.832 59.832  1.00 95.63  ? 87  LEU   M C   1 
ATOM   21948 O  O   . LEU   M  13 100 ? 2.236   -121.504 60.872  1.00 95.44  ? 87  LEU   M O   1 
ATOM   21949 C  CB  . LEU   M  13 100 ? 4.784   -120.126 60.094  1.00 92.86  ? 87  LEU   M CB  1 
ATOM   21950 C  CG  . LEU   M  13 100 ? 5.884   -119.198 59.583  1.00 93.75  ? 87  LEU   M CG  1 
ATOM   21951 C  CD1 . LEU   M  13 100 ? 7.250   -119.663 60.065  1.00 92.59  ? 87  LEU   M CD1 1 
ATOM   21952 C  CD2 . LEU   M  13 100 ? 5.863   -119.108 58.063  1.00 95.01  ? 87  LEU   M CD2 1 
ATOM   21953 N  N   . GLU   M  13 101 ? 1.714   -121.046 58.691  1.00 97.19  ? 88  GLU   M N   1 
ATOM   21954 C  CA  . GLU   M  13 101 ? 0.836   -122.214 58.411  1.00 97.63  ? 88  GLU   M CA  1 
ATOM   21955 C  C   . GLU   M  13 101 ? 1.699   -123.397 57.978  1.00 92.54  ? 88  GLU   M C   1 
ATOM   21956 O  O   . GLU   M  13 101 ? 2.743   -123.209 57.355  1.00 90.99  ? 88  GLU   M O   1 
ATOM   21957 C  CB  . GLU   M  13 101 ? -0.176  -121.870 57.316  1.00 99.49  ? 88  GLU   M CB  1 
ATOM   21958 C  CG  . GLU   M  13 101 ? -1.261  -120.911 57.765  1.00 101.70 ? 88  GLU   M CG  1 
ATOM   21959 C  CD  . GLU   M  13 101 ? -2.447  -121.590 58.427  1.00 101.97 ? 88  GLU   M CD  1 
ATOM   21960 O  OE1 . GLU   M  13 101 ? -2.254  -122.212 59.490  1.00 101.17 ? 88  GLU   M OE1 1 
ATOM   21961 O  OE2 . GLU   M  13 101 ? -3.557  -121.507 57.867  1.00 102.97 ? 88  GLU   M OE2 1 
ATOM   21962 N  N   . PRO   M  13 102 ? 1.294   -124.649 58.297  1.00 89.13  ? 89  PRO   M N   1 
ATOM   21963 C  CA  . PRO   M  13 102 ? 1.970   -125.836 57.775  1.00 85.98  ? 89  PRO   M CA  1 
ATOM   21964 C  C   . PRO   M  13 102 ? 2.193   -125.765 56.255  1.00 82.93  ? 89  PRO   M C   1 
ATOM   21965 O  O   . PRO   M  13 102 ? 3.290   -126.060 55.813  1.00 81.38  ? 89  PRO   M O   1 
ATOM   21966 C  CB  . PRO   M  13 102 ? 1.010   -126.983 58.122  1.00 85.99  ? 89  PRO   M CB  1 
ATOM   21967 C  CG  . PRO   M  13 102 ? 0.230   -126.491 59.324  1.00 87.98  ? 89  PRO   M CG  1 
ATOM   21968 C  CD  . PRO   M  13 102 ? 0.181   -124.984 59.199  1.00 89.52  ? 89  PRO   M CD  1 
ATOM   21969 N  N   . SER   M  13 103 ? 1.159   -125.358 55.507  1.00 82.06  ? 90  SER   M N   1 
ATOM   21970 C  CA  . SER   M  13 103 ? 1.148   -125.273 54.022  1.00 81.50  ? 90  SER   M CA  1 
ATOM   21971 C  C   . SER   M  13 103 ? 2.251   -124.327 53.524  1.00 80.84  ? 90  SER   M C   1 
ATOM   21972 O  O   . SER   M  13 103 ? 2.843   -124.635 52.471  1.00 75.72  ? 90  SER   M O   1 
ATOM   21973 C  CB  . SER   M  13 103 ? -0.208  -124.859 53.515  1.00 83.64  ? 90  SER   M CB  1 
ATOM   21974 O  OG  . SER   M  13 103 ? -0.530  -123.547 53.946  1.00 85.50  ? 90  SER   M OG  1 
ATOM   21975 N  N   . TYR   M  13 104 ? 2.524   -123.231 54.245  1.00 81.14  ? 91  TYR   M N   1 
ATOM   21976 C  CA  . TYR   M  13 104 ? 3.610   -122.265 53.916  1.00 83.37  ? 91  TYR   M CA  1 
ATOM   21977 C  C   . TYR   M  13 104 ? 4.966   -122.957 54.105  1.00 83.02  ? 91  TYR   M C   1 
ATOM   21978 O  O   . TYR   M  13 104 ? 5.815   -122.880 53.193  1.00 78.67  ? 91  TYR   M O   1 
ATOM   21979 C  CB  . TYR   M  13 104 ? 3.575   -120.992 54.775  1.00 85.86  ? 91  TYR   M CB  1 
ATOM   21980 C  CG  . TYR   M  13 104 ? 2.268   -120.239 54.855  1.00 88.52  ? 91  TYR   M CG  1 
ATOM   21981 C  CD1 . TYR   M  13 104 ? 1.259   -120.407 53.918  1.00 91.65  ? 91  TYR   M CD1 1 
ATOM   21982 C  CD2 . TYR   M  13 104 ? 2.055   -119.316 55.868  1.00 87.27  ? 91  TYR   M CD2 1 
ATOM   21983 C  CE1 . TYR   M  13 104 ? 0.065   -119.707 54.005  1.00 93.30  ? 91  TYR   M CE1 1 
ATOM   21984 C  CE2 . TYR   M  13 104 ? 0.868   -118.608 55.970  1.00 89.93  ? 91  TYR   M CE2 1 
ATOM   21985 C  CZ  . TYR   M  13 104 ? -0.132  -118.804 55.035  1.00 92.84  ? 91  TYR   M CZ  1 
ATOM   21986 O  OH  . TYR   M  13 104 ? -1.302  -118.106 55.127  1.00 97.96  ? 91  TYR   M OH  1 
ATOM   21987 N  N   . ILE   M  13 105 ? 5.150   -123.603 55.263  1.00 84.78  ? 92  ILE   M N   1 
ATOM   21988 C  CA  . ILE   M  13 105 ? 6.408   -124.298 55.677  1.00 84.80  ? 92  ILE   M CA  1 
ATOM   21989 C  C   . ILE   M  13 105 ? 6.739   -125.398 54.663  1.00 85.80  ? 92  ILE   M C   1 
ATOM   21990 O  O   . ILE   M  13 105 ? 7.936   -125.575 54.358  1.00 85.87  ? 92  ILE   M O   1 
ATOM   21991 C  CB  . ILE   M  13 105 ? 6.283   -124.869 57.102  1.00 85.01  ? 92  ILE   M CB  1 
ATOM   21992 C  CG1 . ILE   M  13 105 ? 6.223   -123.760 58.153  1.00 86.47  ? 92  ILE   M CG1 1 
ATOM   21993 C  CG2 . ILE   M  13 105 ? 7.409   -125.848 57.396  1.00 86.19  ? 92  ILE   M CG2 1 
ATOM   21994 C  CD1 . ILE   M  13 105 ? 5.429   -124.132 59.380  1.00 88.44  ? 92  ILE   M CD1 1 
ATOM   21995 N  N   . PHE   M  13 106 ? 5.729   -126.129 54.185  1.00 85.22  ? 93  PHE   M N   1 
ATOM   21996 C  CA  . PHE   M  13 106 ? 5.912   -127.207 53.182  1.00 87.49  ? 93  PHE   M CA  1 
ATOM   21997 C  C   . PHE   M  13 106 ? 6.398   -126.595 51.866  1.00 88.24  ? 93  PHE   M C   1 
ATOM   21998 O  O   . PHE   M  13 106 ? 7.493   -126.972 51.397  1.00 88.16  ? 93  PHE   M O   1 
ATOM   21999 C  CB  . PHE   M  13 106 ? 4.629   -128.005 52.944  1.00 87.14  ? 93  PHE   M CB  1 
ATOM   22000 C  CG  . PHE   M  13 106 ? 4.800   -129.085 51.908  1.00 88.28  ? 93  PHE   M CG  1 
ATOM   22001 C  CD1 . PHE   M  13 106 ? 5.257   -130.344 52.268  1.00 88.58  ? 93  PHE   M CD1 1 
ATOM   22002 C  CD2 . PHE   M  13 106 ? 4.561   -128.829 50.566  1.00 88.66  ? 93  PHE   M CD2 1 
ATOM   22003 C  CE1 . PHE   M  13 106 ? 5.439   -131.333 51.315  1.00 89.41  ? 93  PHE   M CE1 1 
ATOM   22004 C  CE2 . PHE   M  13 106 ? 4.750   -129.817 49.613  1.00 90.26  ? 93  PHE   M CE2 1 
ATOM   22005 C  CZ  . PHE   M  13 106 ? 5.186   -131.068 49.990  1.00 89.52  ? 93  PHE   M CZ  1 
ATOM   22006 N  N   . GLU   M  13 107 ? 5.606   -125.681 51.298  1.00 87.68  ? 94  GLU   M N   1 
ATOM   22007 C  CA  . GLU   M  13 107 ? 5.849   -125.091 49.955  1.00 88.39  ? 94  GLU   M CA  1 
ATOM   22008 C  C   . GLU   M  13 107 ? 7.271   -124.518 49.894  1.00 88.77  ? 94  GLU   M C   1 
ATOM   22009 O  O   . GLU   M  13 107 ? 7.916   -124.667 48.837  1.00 85.11  ? 94  GLU   M O   1 
ATOM   22010 C  CB  . GLU   M  13 107 ? 4.816   -124.014 49.622  1.00 90.19  ? 94  GLU   M CB  1 
ATOM   22011 C  CG  . GLU   M  13 107 ? 4.601   -123.850 48.129  1.00 94.01  ? 94  GLU   M CG  1 
ATOM   22012 C  CD  . GLU   M  13 107 ? 3.922   -125.038 47.468  1.00 97.94  ? 94  GLU   M CD  1 
ATOM   22013 O  OE1 . GLU   M  13 107 ? 4.346   -125.413 46.358  1.00 103.12 ? 94  GLU   M OE1 1 
ATOM   22014 O  OE2 . GLU   M  13 107 ? 2.977   -125.589 48.069  1.00 96.32  ? 94  GLU   M OE2 1 
ATOM   22015 N  N   . TYR   M  13 108 ? 7.734   -123.888 50.980  1.00 87.56  ? 95  TYR   M N   1 
ATOM   22016 C  CA  . TYR   M  13 108 ? 9.114   -123.346 51.118  1.00 89.49  ? 95  TYR   M CA  1 
ATOM   22017 C  C   . TYR   M  13 108 ? 10.129  -124.484 50.956  1.00 89.77  ? 95  TYR   M C   1 
ATOM   22018 O  O   . TYR   M  13 108 ? 10.985  -124.405 50.048  1.00 91.09  ? 95  TYR   M O   1 
ATOM   22019 C  CB  . TYR   M  13 108 ? 9.309   -122.638 52.463  1.00 88.30  ? 95  TYR   M CB  1 
ATOM   22020 C  CG  . TYR   M  13 108 ? 10.735  -122.239 52.752  1.00 89.36  ? 95  TYR   M CG  1 
ATOM   22021 C  CD1 . TYR   M  13 108 ? 11.373  -121.267 51.996  1.00 89.91  ? 95  TYR   M CD1 1 
ATOM   22022 C  CD2 . TYR   M  13 108 ? 11.455  -122.833 53.777  1.00 88.16  ? 95  TYR   M CD2 1 
ATOM   22023 C  CE1 . TYR   M  13 108 ? 12.684  -120.894 52.249  1.00 88.61  ? 95  TYR   M CE1 1 
ATOM   22024 C  CE2 . TYR   M  13 108 ? 12.766  -122.471 54.045  1.00 90.18  ? 95  TYR   M CE2 1 
ATOM   22025 C  CZ  . TYR   M  13 108 ? 13.383  -121.496 53.279  1.00 88.96  ? 95  TYR   M CZ  1 
ATOM   22026 O  OH  . TYR   M  13 108 ? 14.672  -121.120 53.523  1.00 91.92  ? 95  TYR   M OH  1 
ATOM   22027 N  N   . LEU   M  13 109 ? 10.033  -125.508 51.812  1.00 85.27  ? 96  LEU   M N   1 
ATOM   22028 C  CA  . LEU   M  13 109 ? 10.937  -126.688 51.796  1.00 78.66  ? 96  LEU   M CA  1 
ATOM   22029 C  C   . LEU   M  13 109 ? 10.867  -127.351 50.416  1.00 78.11  ? 96  LEU   M C   1 
ATOM   22030 O  O   . LEU   M  13 109 ? 11.938  -127.605 49.836  1.00 75.52  ? 96  LEU   M O   1 
ATOM   22031 C  CB  . LEU   M  13 109 ? 10.531  -127.664 52.904  1.00 77.24  ? 96  LEU   M CB  1 
ATOM   22032 C  CG  . LEU   M  13 109 ? 10.841  -127.225 54.334  1.00 78.57  ? 96  LEU   M CG  1 
ATOM   22033 C  CD1 . LEU   M  13 109 ? 10.390  -128.290 55.322  1.00 80.56  ? 96  LEU   M CD1 1 
ATOM   22034 C  CD2 . LEU   M  13 109 ? 12.323  -126.935 54.518  1.00 78.30  ? 96  LEU   M CD2 1 
ATOM   22035 N  N   . ALA   M  13 110 ? 9.653   -127.585 49.907  1.00 80.19  ? 97  ALA   M N   1 
ATOM   22036 C  CA  . ALA   M  13 110 ? 9.387   -128.215 48.590  1.00 84.03  ? 97  ALA   M CA  1 
ATOM   22037 C  C   . ALA   M  13 110 ? 10.117  -127.448 47.480  1.00 84.63  ? 97  ALA   M C   1 
ATOM   22038 O  O   . ALA   M  13 110 ? 10.687  -128.108 46.586  1.00 86.25  ? 97  ALA   M O   1 
ATOM   22039 C  CB  . ALA   M  13 110 ? 7.901   -128.282 48.329  1.00 84.73  ? 97  ALA   M CB  1 
ATOM   22040 N  N   . THR   M  13 111 ? 10.106  -126.112 47.537  1.00 82.37  ? 98  THR   M N   1 
ATOM   22041 C  CA  . THR   M  13 111 ? 10.808  -125.225 46.571  1.00 82.78  ? 98  THR   M CA  1 
ATOM   22042 C  C   . THR   M  13 111 ? 12.316  -125.480 46.664  1.00 81.73  ? 98  THR   M C   1 
ATOM   22043 O  O   . THR   M  13 111 ? 12.941  -125.728 45.613  1.00 80.72  ? 98  THR   M O   1 
ATOM   22044 C  CB  . THR   M  13 111 ? 10.484  -123.746 46.817  1.00 83.93  ? 98  THR   M CB  1 
ATOM   22045 O  OG1 . THR   M  13 111 ? 9.081   -123.568 46.621  1.00 83.84  ? 98  THR   M OG1 1 
ATOM   22046 C  CG2 . THR   M  13 111 ? 11.258  -122.815 45.908  1.00 84.65  ? 98  THR   M CG2 1 
ATOM   22047 N  N   . VAL   M  13 112 ? 12.862  -125.421 47.882  1.00 81.09  ? 99  VAL   M N   1 
ATOM   22048 C  CA  . VAL   M  13 112 ? 14.316  -125.600 48.175  1.00 81.60  ? 99  VAL   M CA  1 
ATOM   22049 C  C   . VAL   M  13 112 ? 14.766  -126.979 47.672  1.00 80.51  ? 99  VAL   M C   1 
ATOM   22050 O  O   . VAL   M  13 112 ? 15.780  -127.045 46.948  1.00 74.53  ? 99  VAL   M O   1 
ATOM   22051 C  CB  . VAL   M  13 112 ? 14.608  -125.426 49.679  1.00 83.49  ? 99  VAL   M CB  1 
ATOM   22052 C  CG1 . VAL   M  13 112 ? 16.007  -125.899 50.050  1.00 85.78  ? 99  VAL   M CG1 1 
ATOM   22053 C  CG2 . VAL   M  13 112 ? 14.400  -123.988 50.128  1.00 84.09  ? 99  VAL   M CG2 1 
ATOM   22054 N  N   . MET   M  13 113 ? 14.041  -128.036 48.045  1.00 81.28  ? 100 MET   M N   1 
ATOM   22055 C  CA  . MET   M  13 113 ? 14.407  -129.442 47.722  1.00 84.48  ? 100 MET   M CA  1 
ATOM   22056 C  C   . MET   M  13 113 ? 14.542  -129.594 46.201  1.00 83.30  ? 100 MET   M C   1 
ATOM   22057 O  O   . MET   M  13 113 ? 15.560  -130.175 45.760  1.00 80.52  ? 100 MET   M O   1 
ATOM   22058 C  CB  . MET   M  13 113 ? 13.371  -130.438 48.259  1.00 86.86  ? 100 MET   M CB  1 
ATOM   22059 C  CG  . MET   M  13 113 ? 13.302  -130.499 49.782  1.00 86.52  ? 100 MET   M CG  1 
ATOM   22060 S  SD  . MET   M  13 113 ? 14.877  -130.917 50.578  1.00 87.43  ? 100 MET   M SD  1 
ATOM   22061 C  CE  . MET   M  13 113 ? 14.863  -132.699 50.394  1.00 91.60  ? 100 MET   M CE  1 
ATOM   22062 N  N   . TYR   M  13 114 ? 13.578  -129.070 45.433  1.00 81.57  ? 101 TYR   M N   1 
ATOM   22063 C  CA  . TYR   M  13 114 ? 13.538  -129.184 43.950  1.00 81.82  ? 101 TYR   M CA  1 
ATOM   22064 C  C   . TYR   M  13 114 ? 14.624  -128.300 43.325  1.00 82.25  ? 101 TYR   M C   1 
ATOM   22065 O  O   . TYR   M  13 114 ? 15.219  -128.722 42.317  1.00 83.40  ? 101 TYR   M O   1 
ATOM   22066 C  CB  . TYR   M  13 114 ? 12.162  -128.829 43.381  1.00 81.09  ? 101 TYR   M CB  1 
ATOM   22067 C  CG  . TYR   M  13 114 ? 12.070  -129.005 41.886  1.00 83.31  ? 101 TYR   M CG  1 
ATOM   22068 C  CD1 . TYR   M  13 114 ? 11.996  -130.267 41.316  1.00 84.90  ? 101 TYR   M CD1 1 
ATOM   22069 C  CD2 . TYR   M  13 114 ? 12.097  -127.915 41.032  1.00 82.03  ? 101 TYR   M CD2 1 
ATOM   22070 C  CE1 . TYR   M  13 114 ? 11.930  -130.441 39.942  1.00 86.45  ? 101 TYR   M CE1 1 
ATOM   22071 C  CE2 . TYR   M  13 114 ? 12.030  -128.069 39.657  1.00 83.57  ? 101 TYR   M CE2 1 
ATOM   22072 C  CZ  . TYR   M  13 114 ? 11.944  -129.336 39.108  1.00 85.16  ? 101 TYR   M CZ  1 
ATOM   22073 O  OH  . TYR   M  13 114 ? 11.874  -129.479 37.752  1.00 86.44  ? 101 TYR   M OH  1 
ATOM   22074 N  N   . GLN   M  13 115 ? 14.861  -127.111 43.889  1.00 81.44  ? 102 GLN   M N   1 
ATOM   22075 C  CA  . GLN   M  13 115 ? 15.921  -126.175 43.423  1.00 83.63  ? 102 GLN   M CA  1 
ATOM   22076 C  C   . GLN   M  13 115 ? 17.293  -126.843 43.574  1.00 82.30  ? 102 GLN   M C   1 
ATOM   22077 O  O   . GLN   M  13 115 ? 18.128  -126.696 42.656  1.00 83.42  ? 102 GLN   M O   1 
ATOM   22078 C  CB  . GLN   M  13 115 ? 15.872  -124.858 44.199  1.00 87.69  ? 102 GLN   M CB  1 
ATOM   22079 C  CG  . GLN   M  13 115 ? 14.833  -123.878 43.670  1.00 94.04  ? 102 GLN   M CG  1 
ATOM   22080 C  CD  . GLN   M  13 115 ? 14.933  -122.494 44.269  1.00 99.11  ? 102 GLN   M CD  1 
ATOM   22081 O  OE1 . GLN   M  13 115 ? 14.519  -121.509 43.659  1.00 104.49 ? 102 GLN   M OE1 1 
ATOM   22082 N  NE2 . GLN   M  13 115 ? 15.477  -122.395 45.474  1.00 105.10 ? 102 GLN   M NE2 1 
ATOM   22083 N  N   . ARG   M  13 116 ? 17.512  -127.551 44.685  1.00 77.93  ? 103 ARG   M N   1 
ATOM   22084 C  CA  . ARG   M  13 116 ? 18.805  -128.210 45.010  1.00 78.57  ? 103 ARG   M CA  1 
ATOM   22085 C  C   . ARG   M  13 116 ? 19.025  -129.425 44.095  1.00 77.89  ? 103 ARG   M C   1 
ATOM   22086 O  O   . ARG   M  13 116 ? 20.190  -129.653 43.700  1.00 75.65  ? 103 ARG   M O   1 
ATOM   22087 C  CB  . ARG   M  13 116 ? 18.849  -128.602 46.491  1.00 76.35  ? 103 ARG   M CB  1 
ATOM   22088 C  CG  . ARG   M  13 116 ? 19.005  -127.429 47.449  1.00 75.67  ? 103 ARG   M CG  1 
ATOM   22089 C  CD  . ARG   M  13 116 ? 20.380  -126.787 47.385  1.00 74.65  ? 103 ARG   M CD  1 
ATOM   22090 N  NE  . ARG   M  13 116 ? 21.445  -127.712 47.742  1.00 75.00  ? 103 ARG   M NE  1 
ATOM   22091 C  CZ  . ARG   M  13 116 ? 21.972  -127.857 48.956  1.00 76.38  ? 103 ARG   M CZ  1 
ATOM   22092 N  NH1 . ARG   M  13 116 ? 21.550  -127.129 49.976  1.00 76.66  ? 103 ARG   M NH1 1 
ATOM   22093 N  NH2 . ARG   M  13 116 ? 22.933  -128.743 49.146  1.00 79.98  ? 103 ARG   M NH2 1 
ATOM   22094 N  N   . ARG   M  13 117 ? 17.967  -130.176 43.765  1.00 77.87  ? 104 ARG   M N   1 
ATOM   22095 C  CA  . ARG   M  13 117 ? 18.062  -131.341 42.841  1.00 79.68  ? 104 ARG   M CA  1 
ATOM   22096 C  C   . ARG   M  13 117 ? 18.381  -130.813 41.436  1.00 81.77  ? 104 ARG   M C   1 
ATOM   22097 O  O   . ARG   M  13 117 ? 19.124  -131.495 40.706  1.00 80.79  ? 104 ARG   M O   1 
ATOM   22098 C  CB  . ARG   M  13 117 ? 16.798  -132.214 42.891  1.00 81.77  ? 104 ARG   M CB  1 
ATOM   22099 C  CG  . ARG   M  13 117 ? 15.747  -131.927 41.826  1.00 82.15  ? 104 ARG   M CG  1 
ATOM   22100 C  CD  . ARG   M  13 117 ? 15.891  -132.752 40.555  1.00 82.55  ? 104 ARG   M CD  1 
ATOM   22101 N  NE  . ARG   M  13 117 ? 15.550  -131.985 39.357  1.00 84.32  ? 104 ARG   M NE  1 
ATOM   22102 C  CZ  . ARG   M  13 117 ? 15.327  -132.497 38.146  1.00 85.66  ? 104 ARG   M CZ  1 
ATOM   22103 N  NH1 . ARG   M  13 117 ? 15.385  -133.800 37.939  1.00 88.03  ? 104 ARG   M NH1 1 
ATOM   22104 N  NH2 . ARG   M  13 117 ? 15.034  -131.698 37.136  1.00 88.09  ? 104 ARG   M NH2 1 
ATOM   22105 N  N   . SER   M  13 118 ? 17.869  -129.626 41.094  1.00 81.98  ? 105 SER   M N   1 
ATOM   22106 C  CA  . SER   M  13 118 ? 18.010  -128.988 39.759  1.00 83.28  ? 105 SER   M CA  1 
ATOM   22107 C  C   . SER   M  13 118 ? 19.417  -128.401 39.587  1.00 85.28  ? 105 SER   M C   1 
ATOM   22108 O  O   . SER   M  13 118 ? 19.830  -128.206 38.427  1.00 85.58  ? 105 SER   M O   1 
ATOM   22109 C  CB  . SER   M  13 118 ? 16.951  -127.940 39.547  1.00 84.00  ? 105 SER   M CB  1 
ATOM   22110 O  OG  . SER   M  13 118 ? 15.652  -128.511 39.611  1.00 85.14  ? 105 SER   M OG  1 
ATOM   22111 N  N   . LYS   M  13 119 ? 20.118  -128.125 40.694  1.00 87.34  ? 106 LYS   M N   1 
ATOM   22112 C  CA  . LYS   M  13 119 ? 21.536  -127.668 40.699  1.00 88.16  ? 106 LYS   M CA  1 
ATOM   22113 C  C   . LYS   M  13 119 ? 22.473  -128.871 40.880  1.00 86.92  ? 106 LYS   M C   1 
ATOM   22114 O  O   . LYS   M  13 119 ? 23.687  -128.644 41.023  1.00 84.70  ? 106 LYS   M O   1 
ATOM   22115 C  CB  . LYS   M  13 119 ? 21.750  -126.607 41.783  1.00 94.02  ? 106 LYS   M CB  1 
ATOM   22116 C  CG  . LYS   M  13 119 ? 21.489  -125.175 41.332  1.00 96.89  ? 106 LYS   M CG  1 
ATOM   22117 C  CD  . LYS   M  13 119 ? 21.190  -124.218 42.467  1.00 104.13 ? 106 LYS   M CD  1 
ATOM   22118 C  CE  . LYS   M  13 119 ? 22.387  -123.940 43.353  1.00 109.90 ? 106 LYS   M CE  1 
ATOM   22119 N  NZ  . LYS   M  13 119 ? 21.983  -123.328 44.642  1.00 112.95 ? 106 LYS   M NZ  1 
ATOM   22120 N  N   . MET   M  13 120 ? 21.926  -130.094 40.861  1.00 87.49  ? 107 MET   M N   1 
ATOM   22121 C  CA  . MET   M  13 120 ? 22.666  -131.384 40.964  1.00 88.01  ? 107 MET   M CA  1 
ATOM   22122 C  C   . MET   M  13 120 ? 23.446  -131.442 42.283  1.00 84.98  ? 107 MET   M C   1 
ATOM   22123 O  O   . MET   M  13 120 ? 24.502  -132.098 42.314  1.00 89.38  ? 107 MET   M O   1 
ATOM   22124 C  CB  . MET   M  13 120 ? 23.636  -131.569 39.790  1.00 90.53  ? 107 MET   M CB  1 
ATOM   22125 C  CG  . MET   M  13 120 ? 22.945  -131.809 38.464  1.00 93.02  ? 107 MET   M CG  1 
ATOM   22126 S  SD  . MET   M  13 120 ? 21.936  -133.306 38.472  1.00 95.71  ? 107 MET   M SD  1 
ATOM   22127 C  CE  . MET   M  13 120 ? 23.202  -134.575 38.535  1.00 101.08 ? 107 MET   M CE  1 
ATOM   22128 N  N   . ASN   M  13 121 ? 22.937  -130.790 43.331  1.00 83.39  ? 108 ASN   M N   1 
ATOM   22129 C  CA  . ASN   M  13 121 ? 23.524  -130.814 44.696  1.00 83.37  ? 108 ASN   M CA  1 
ATOM   22130 C  C   . ASN   M  13 121 ? 22.374  -130.898 45.696  1.00 81.72  ? 108 ASN   M C   1 
ATOM   22131 O  O   . ASN   M  13 121 ? 22.029  -129.909 46.336  1.00 80.45  ? 108 ASN   M O   1 
ATOM   22132 C  CB  . ASN   M  13 121 ? 24.451  -129.614 44.915  1.00 84.34  ? 108 ASN   M CB  1 
ATOM   22133 C  CG  . ASN   M  13 121 ? 25.063  -129.550 46.299  1.00 89.41  ? 108 ASN   M CG  1 
ATOM   22134 O  OD1 . ASN   M  13 121 ? 25.203  -128.464 46.859  1.00 87.03  ? 108 ASN   M OD1 1 
ATOM   22135 N  ND2 . ASN   M  13 121 ? 25.440  -130.691 46.857  1.00 89.09  ? 108 ASN   M ND2 1 
ATOM   22136 N  N   . PRO   M  13 122 ? 21.747  -132.087 45.855  1.00 84.04  ? 109 PRO   M N   1 
ATOM   22137 C  CA  . PRO   M  13 122 ? 20.511  -132.213 46.626  1.00 82.66  ? 109 PRO   M CA  1 
ATOM   22138 C  C   . PRO   M  13 122 ? 20.740  -132.269 48.143  1.00 81.51  ? 109 PRO   M C   1 
ATOM   22139 O  O   . PRO   M  13 122 ? 21.819  -132.657 48.557  1.00 85.82  ? 109 PRO   M O   1 
ATOM   22140 C  CB  . PRO   M  13 122 ? 19.959  -133.559 46.135  1.00 82.13  ? 109 PRO   M CB  1 
ATOM   22141 C  CG  . PRO   M  13 122 ? 21.202  -134.378 45.851  1.00 82.50  ? 109 PRO   M CG  1 
ATOM   22142 C  CD  . PRO   M  13 122 ? 22.216  -133.381 45.330  1.00 83.28  ? 109 PRO   M CD  1 
ATOM   22143 N  N   . LEU   M  13 123 ? 19.724  -131.888 48.923  1.00 80.31  ? 110 LEU   M N   1 
ATOM   22144 C  CA  . LEU   M  13 123 ? 19.624  -132.222 50.370  1.00 82.14  ? 110 LEU   M CA  1 
ATOM   22145 C  C   . LEU   M  13 123 ? 19.101  -133.659 50.480  1.00 80.92  ? 110 LEU   M C   1 
ATOM   22146 O  O   . LEU   M  13 123 ? 17.932  -133.887 50.114  1.00 87.87  ? 110 LEU   M O   1 
ATOM   22147 C  CB  . LEU   M  13 123 ? 18.695  -131.226 51.071  1.00 81.77  ? 110 LEU   M CB  1 
ATOM   22148 C  CG  . LEU   M  13 123 ? 19.187  -129.779 51.127  1.00 80.09  ? 110 LEU   M CG  1 
ATOM   22149 C  CD1 . LEU   M  13 123 ? 18.073  -128.848 51.574  1.00 78.90  ? 110 LEU   M CD1 1 
ATOM   22150 C  CD2 . LEU   M  13 123 ? 20.393  -129.638 52.045  1.00 80.02  ? 110 LEU   M CD2 1 
ATOM   22151 N  N   . TRP   M  13 124 ? 19.943  -134.590 50.939  1.00 81.33  ? 111 TRP   M N   1 
ATOM   22152 C  CA  . TRP   M  13 124 ? 19.713  -136.057 50.829  1.00 80.06  ? 111 TRP   M CA  1 
ATOM   22153 C  C   . TRP   M  13 124 ? 18.693  -136.510 51.880  1.00 77.41  ? 111 TRP   M C   1 
ATOM   22154 O  O   . TRP   M  13 124 ? 19.086  -137.220 52.831  1.00 73.24  ? 111 TRP   M O   1 
ATOM   22155 C  CB  . TRP   M  13 124 ? 21.038  -136.816 50.955  1.00 80.77  ? 111 TRP   M CB  1 
ATOM   22156 C  CG  . TRP   M  13 124 ? 21.033  -138.129 50.239  1.00 80.67  ? 111 TRP   M CG  1 
ATOM   22157 C  CD1 . TRP   M  13 124 ? 20.474  -139.301 50.657  1.00 79.89  ? 111 TRP   M CD1 1 
ATOM   22158 C  CD2 . TRP   M  13 124 ? 21.616  -138.396 48.953  1.00 80.30  ? 111 TRP   M CD2 1 
ATOM   22159 N  NE1 . TRP   M  13 124 ? 20.673  -140.280 49.721  1.00 79.64  ? 111 TRP   M NE1 1 
ATOM   22160 C  CE2 . TRP   M  13 124 ? 21.368  -139.754 48.664  1.00 79.85  ? 111 TRP   M CE2 1 
ATOM   22161 C  CE3 . TRP   M  13 124 ? 22.321  -137.623 48.024  1.00 82.39  ? 111 TRP   M CE3 1 
ATOM   22162 C  CZ2 . TRP   M  13 124 ? 21.809  -140.350 47.484  1.00 81.54  ? 111 TRP   M CZ2 1 
ATOM   22163 C  CZ3 . TRP   M  13 124 ? 22.752  -138.212 46.856  1.00 82.18  ? 111 TRP   M CZ3 1 
ATOM   22164 C  CH2 . TRP   M  13 124 ? 22.498  -139.558 46.593  1.00 81.38  ? 111 TRP   M CH2 1 
ATOM   22165 N  N   . ASN   M  13 125 ? 17.427  -136.130 51.699  1.00 76.37  ? 112 ASN   M N   1 
ATOM   22166 C  CA  . ASN   M  13 125 ? 16.373  -136.263 52.737  1.00 76.52  ? 112 ASN   M CA  1 
ATOM   22167 C  C   . ASN   M  13 125 ? 15.042  -136.670 52.107  1.00 75.34  ? 112 ASN   M C   1 
ATOM   22168 O  O   . ASN   M  13 125 ? 14.773  -136.271 50.960  1.00 76.36  ? 112 ASN   M O   1 
ATOM   22169 C  CB  . ASN   M  13 125 ? 16.179  -134.955 53.507  1.00 79.25  ? 112 ASN   M CB  1 
ATOM   22170 C  CG  . ASN   M  13 125 ? 17.413  -134.542 54.279  1.00 81.29  ? 112 ASN   M CG  1 
ATOM   22171 O  OD1 . ASN   M  13 125 ? 17.996  -133.492 54.014  1.00 81.89  ? 112 ASN   M OD1 1 
ATOM   22172 N  ND2 . ASN   M  13 125 ? 17.828  -135.370 55.223  1.00 84.79  ? 112 ASN   M ND2 1 
ATOM   22173 N  N   . ALA   M  13 126 ? 14.260  -137.447 52.854  1.00 74.96  ? 113 ALA   M N   1 
ATOM   22174 C  CA  . ALA   M  13 126 ? 12.798  -137.597 52.700  1.00 79.57  ? 113 ALA   M CA  1 
ATOM   22175 C  C   . ALA   M  13 126 ? 12.151  -136.846 53.866  1.00 80.99  ? 113 ALA   M C   1 
ATOM   22176 O  O   . ALA   M  13 126 ? 12.578  -137.067 55.017  1.00 84.55  ? 113 ALA   M O   1 
ATOM   22177 C  CB  . ALA   M  13 126 ? 12.414  -139.056 52.672  1.00 80.63  ? 113 ALA   M CB  1 
ATOM   22178 N  N   . ILE   M  13 127 ? 11.198  -135.961 53.574  1.00 80.40  ? 114 ILE   M N   1 
ATOM   22179 C  CA  . ILE   M  13 127 ? 10.586  -135.031 54.567  1.00 84.66  ? 114 ILE   M CA  1 
ATOM   22180 C  C   . ILE   M  13 127 ? 9.065   -135.187 54.528  1.00 83.19  ? 114 ILE   M C   1 
ATOM   22181 O  O   . ILE   M  13 127 ? 8.496   -135.178 53.419  1.00 80.12  ? 114 ILE   M O   1 
ATOM   22182 C  CB  . ILE   M  13 127 ? 11.015  -133.579 54.282  1.00 85.16  ? 114 ILE   M CB  1 
ATOM   22183 C  CG1 . ILE   M  13 127 ? 12.531  -133.405 54.407  1.00 89.28  ? 114 ILE   M CG1 1 
ATOM   22184 C  CG2 . ILE   M  13 127 ? 10.254  -132.602 55.168  1.00 86.65  ? 114 ILE   M CG2 1 
ATOM   22185 C  CD1 . ILE   M  13 127 ? 13.060  -132.123 53.804  1.00 89.52  ? 114 ILE   M CD1 1 
ATOM   22186 N  N   . ILE   M  13 128 ? 8.443   -135.309 55.702  1.00 85.91  ? 115 ILE   M N   1 
ATOM   22187 C  CA  . ILE   M  13 128 ? 6.962   -135.269 55.882  1.00 88.03  ? 115 ILE   M CA  1 
ATOM   22188 C  C   . ILE   M  13 128 ? 6.628   -134.067 56.776  1.00 87.87  ? 115 ILE   M C   1 
ATOM   22189 O  O   . ILE   M  13 128 ? 7.166   -133.990 57.901  1.00 85.01  ? 115 ILE   M O   1 
ATOM   22190 C  CB  . ILE   M  13 128 ? 6.430   -136.600 56.452  1.00 90.79  ? 115 ILE   M CB  1 
ATOM   22191 C  CG1 . ILE   M  13 128 ? 6.638   -137.751 55.464  1.00 93.39  ? 115 ILE   M CG1 1 
ATOM   22192 C  CG2 . ILE   M  13 128 ? 4.968   -136.470 56.864  1.00 89.59  ? 115 ILE   M CG2 1 
ATOM   22193 C  CD1 . ILE   M  13 128 ? 6.351   -139.126 56.034  1.00 96.39  ? 115 ILE   M CD1 1 
ATOM   22194 N  N   . VAL   M  13 129 ? 5.784   -133.162 56.275  1.00 85.34  ? 116 VAL   M N   1 
ATOM   22195 C  CA  . VAL   M  13 129 ? 5.270   -131.975 57.018  1.00 87.62  ? 116 VAL   M CA  1 
ATOM   22196 C  C   . VAL   M  13 129 ? 3.855   -132.290 57.501  1.00 87.52  ? 116 VAL   M C   1 
ATOM   22197 O  O   . VAL   M  13 129 ? 2.947   -132.358 56.654  1.00 86.97  ? 116 VAL   M O   1 
ATOM   22198 C  CB  . VAL   M  13 129 ? 5.280   -130.712 56.138  1.00 89.17  ? 116 VAL   M CB  1 
ATOM   22199 C  CG1 . VAL   M  13 129 ? 4.583   -129.544 56.819  1.00 91.52  ? 116 VAL   M CG1 1 
ATOM   22200 C  CG2 . VAL   M  13 129 ? 6.693   -130.332 55.722  1.00 91.35  ? 116 VAL   M CG2 1 
ATOM   22201 N  N   . ALA   M  13 130 ? 3.687   -132.464 58.813  1.00 88.98  ? 117 ALA   M N   1 
ATOM   22202 C  CA  . ALA   M  13 130 ? 2.396   -132.754 59.475  1.00 90.99  ? 117 ALA   M CA  1 
ATOM   22203 C  C   . ALA   M  13 130 ? 1.981   -131.533 60.301  1.00 92.09  ? 117 ALA   M C   1 
ATOM   22204 O  O   . ALA   M  13 130 ? 2.826   -131.013 61.059  1.00 92.88  ? 117 ALA   M O   1 
ATOM   22205 C  CB  . ALA   M  13 130 ? 2.522   -133.992 60.328  1.00 91.95  ? 117 ALA   M CB  1 
ATOM   22206 N  N   . GLY   M  13 131 ? 0.735   -131.082 60.146  1.00 89.92  ? 118 GLY   M N   1 
ATOM   22207 C  CA  . GLY   M  13 131 ? 0.186   -129.965 60.935  1.00 91.36  ? 118 GLY   M CA  1 
ATOM   22208 C  C   . GLY   M  13 131 ? -1.310  -129.795 60.748  1.00 91.68  ? 118 GLY   M C   1 
ATOM   22209 O  O   . GLY   M  13 131 ? -1.927  -130.625 60.053  1.00 89.34  ? 118 GLY   M O   1 
ATOM   22210 N  N   . VAL   M  13 132 ? -1.863  -128.749 61.365  1.00 95.72  ? 119 VAL   M N   1 
ATOM   22211 C  CA  . VAL   M  13 132 ? -3.286  -128.322 61.235  1.00 98.67  ? 119 VAL   M CA  1 
ATOM   22212 C  C   . VAL   M  13 132 ? -3.297  -126.870 60.743  1.00 100.64 ? 119 VAL   M C   1 
ATOM   22213 O  O   . VAL   M  13 132 ? -2.582  -126.035 61.337  1.00 97.95  ? 119 VAL   M O   1 
ATOM   22214 C  CB  . VAL   M  13 132 ? -4.043  -128.481 62.568  1.00 99.21  ? 119 VAL   M CB  1 
ATOM   22215 C  CG1 . VAL   M  13 132 ? -5.443  -127.888 62.506  1.00 102.04 ? 119 VAL   M CG1 1 
ATOM   22216 C  CG2 . VAL   M  13 132 ? -4.107  -129.935 63.008  1.00 99.16  ? 119 VAL   M CG2 1 
ATOM   22217 N  N   . GLN   M  13 133 ? -4.078  -126.591 59.694  1.00 104.01 ? 120 GLN   M N   1 
ATOM   22218 C  CA  . GLN   M  13 133 ? -4.240  -125.237 59.099  1.00 106.35 ? 120 GLN   M CA  1 
ATOM   22219 C  C   . GLN   M  13 133 ? -5.069  -124.370 60.055  1.00 111.94 ? 120 GLN   M C   1 
ATOM   22220 O  O   . GLN   M  13 133 ? -5.596  -124.915 61.046  1.00 115.43 ? 120 GLN   M O   1 
ATOM   22221 C  CB  . GLN   M  13 133 ? -4.895  -125.336 57.718  1.00 105.68 ? 120 GLN   M CB  1 
ATOM   22222 C  CG  . GLN   M  13 133 ? -4.056  -126.086 56.691  1.00 101.40 ? 120 GLN   M CG  1 
ATOM   22223 C  CD  . GLN   M  13 133 ? -2.832  -125.312 56.262  1.00 94.36  ? 120 GLN   M CD  1 
ATOM   22224 O  OE1 . GLN   M  13 133 ? -1.718  -125.562 56.716  1.00 91.81  ? 120 GLN   M OE1 1 
ATOM   22225 N  NE2 . GLN   M  13 133 ? -3.030  -124.350 55.378  1.00 92.06  ? 120 GLN   M NE2 1 
ATOM   22226 N  N   . SER   M  13 134 ? -5.186  -123.073 59.757  1.00 112.53 ? 121 SER   M N   1 
ATOM   22227 C  CA  . SER   M  13 134 ? -5.895  -122.066 60.593  1.00 111.90 ? 121 SER   M CA  1 
ATOM   22228 C  C   . SER   M  13 134 ? -7.401  -122.357 60.610  1.00 109.98 ? 121 SER   M C   1 
ATOM   22229 O  O   . SER   M  13 134 ? -8.049  -122.023 61.621  1.00 112.47 ? 121 SER   M O   1 
ATOM   22230 C  CB  . SER   M  13 134 ? -5.608  -120.662 60.119  1.00 111.42 ? 121 SER   M CB  1 
ATOM   22231 O  OG  . SER   M  13 134 ? -6.126  -120.441 58.816  1.00 115.83 ? 121 SER   M OG  1 
ATOM   22232 N  N   . ASN   M  13 135 ? -7.927  -122.965 59.539  1.00 107.96 ? 122 ASN   M N   1 
ATOM   22233 C  CA  . ASN   M  13 135 ? -9.370  -123.293 59.369  1.00 108.67 ? 122 ASN   M CA  1 
ATOM   22234 C  C   . ASN   M  13 135 ? -9.675  -124.690 59.931  1.00 109.89 ? 122 ASN   M C   1 
ATOM   22235 O  O   . ASN   M  13 135 ? -10.807 -125.170 59.712  1.00 109.26 ? 122 ASN   M O   1 
ATOM   22236 C  CB  . ASN   M  13 135 ? -9.799  -123.182 57.903  1.00 109.63 ? 122 ASN   M CB  1 
ATOM   22237 C  CG  . ASN   M  13 135 ? -9.128  -124.200 57.005  1.00 107.17 ? 122 ASN   M CG  1 
ATOM   22238 O  OD1 . ASN   M  13 135 ? -8.109  -124.781 57.369  1.00 105.92 ? 122 ASN   M OD1 1 
ATOM   22239 N  ND2 . ASN   M  13 135 ? -9.685  -124.417 55.826  1.00 110.33 ? 122 ASN   M ND2 1 
ATOM   22240 N  N   . GLY   M  13 136 ? -8.709  -125.323 60.609  1.00 108.41 ? 123 GLY   M N   1 
ATOM   22241 C  CA  . GLY   M  13 136 ? -8.889  -126.611 61.311  1.00 110.15 ? 123 GLY   M CA  1 
ATOM   22242 C  C   . GLY   M  13 136 ? -8.554  -127.821 60.448  1.00 110.93 ? 123 GLY   M C   1 
ATOM   22243 O  O   . GLY   M  13 136 ? -8.520  -128.937 61.010  1.00 107.28 ? 123 GLY   M O   1 
ATOM   22244 N  N   . ASP   M  13 137 ? -8.315  -127.625 59.144  1.00 112.73 ? 124 ASP   M N   1 
ATOM   22245 C  CA  . ASP   M  13 137 ? -8.041  -128.713 58.164  1.00 112.39 ? 124 ASP   M CA  1 
ATOM   22246 C  C   . ASP   M  13 137 ? -6.731  -129.420 58.528  1.00 109.25 ? 124 ASP   M C   1 
ATOM   22247 O  O   . ASP   M  13 137 ? -5.772  -128.726 58.920  1.00 107.25 ? 124 ASP   M O   1 
ATOM   22248 C  CB  . ASP   M  13 137 ? -7.955  -128.187 56.727  1.00 116.05 ? 124 ASP   M CB  1 
ATOM   22249 C  CG  . ASP   M  13 137 ? -9.296  -127.873 56.084  1.00 123.17 ? 124 ASP   M CG  1 
ATOM   22250 O  OD1 . ASP   M  13 137 ? -10.333 -128.290 56.643  1.00 130.86 ? 124 ASP   M OD1 1 
ATOM   22251 O  OD2 . ASP   M  13 137 ? -9.292  -127.220 55.021  1.00 127.20 ? 124 ASP   M OD2 1 
ATOM   22252 N  N   . GLN   M  13 138 ? -6.703  -130.750 58.387  1.00 105.82 ? 125 GLN   M N   1 
ATOM   22253 C  CA  . GLN   M  13 138 ? -5.485  -131.587 58.554  1.00 98.86  ? 125 GLN   M CA  1 
ATOM   22254 C  C   . GLN   M  13 138 ? -4.551  -131.333 57.368  1.00 94.25  ? 125 GLN   M C   1 
ATOM   22255 O  O   . GLN   M  13 138 ? -5.046  -131.332 56.226  1.00 93.75  ? 125 GLN   M O   1 
ATOM   22256 C  CB  . GLN   M  13 138 ? -5.829  -133.077 58.613  1.00 97.11  ? 125 GLN   M CB  1 
ATOM   22257 C  CG  . GLN   M  13 138 ? -6.718  -133.468 59.785  1.00 97.94  ? 125 GLN   M CG  1 
ATOM   22258 C  CD  . GLN   M  13 138 ? -8.172  -133.599 59.399  1.00 98.29  ? 125 GLN   M CD  1 
ATOM   22259 O  OE1 . GLN   M  13 138 ? -8.705  -132.800 58.632  1.00 97.15  ? 125 GLN   M OE1 1 
ATOM   22260 N  NE2 . GLN   M  13 138 ? -8.830  -134.614 59.936  1.00 99.09  ? 125 GLN   M NE2 1 
ATOM   22261 N  N   . PHE   M  13 139 ? -3.258  -131.122 57.630  1.00 92.63  ? 126 PHE   M N   1 
ATOM   22262 C  CA  . PHE   M  13 139 ? -2.202  -131.023 56.591  1.00 93.88  ? 126 PHE   M CA  1 
ATOM   22263 C  C   . PHE   M  13 139 ? -1.172  -132.133 56.810  1.00 92.64  ? 126 PHE   M C   1 
ATOM   22264 O  O   . PHE   M  13 139 ? -0.583  -132.212 57.907  1.00 92.57  ? 126 PHE   M O   1 
ATOM   22265 C  CB  . PHE   M  13 139 ? -1.508  -129.660 56.598  1.00 97.33  ? 126 PHE   M CB  1 
ATOM   22266 C  CG  . PHE   M  13 139 ? -0.584  -129.456 55.424  1.00 98.51  ? 126 PHE   M CG  1 
ATOM   22267 C  CD1 . PHE   M  13 139 ? 0.758   -129.803 55.501  1.00 97.69  ? 126 PHE   M CD1 1 
ATOM   22268 C  CD2 . PHE   M  13 139 ? -1.064  -128.948 54.226  1.00 101.91 ? 126 PHE   M CD2 1 
ATOM   22269 C  CE1 . PHE   M  13 139 ? 1.600   -129.626 54.413  1.00 97.39  ? 126 PHE   M CE1 1 
ATOM   22270 C  CE2 . PHE   M  13 139 ? -0.220  -128.773 53.139  1.00 100.41 ? 126 PHE   M CE2 1 
ATOM   22271 C  CZ  . PHE   M  13 139 ? 1.110   -129.113 53.233  1.00 98.98  ? 126 PHE   M CZ  1 
ATOM   22272 N  N   . LEU   M  13 140 ? -0.970  -132.957 55.782  1.00 90.60  ? 127 LEU   M N   1 
ATOM   22273 C  CA  . LEU   M  13 140 ? 0.047   -134.039 55.754  1.00 91.59  ? 127 LEU   M CA  1 
ATOM   22274 C  C   . LEU   M  13 140 ? 0.545   -134.190 54.315  1.00 87.65  ? 127 LEU   M C   1 
ATOM   22275 O  O   . LEU   M  13 140 ? -0.257  -134.616 53.463  1.00 88.18  ? 127 LEU   M O   1 
ATOM   22276 C  CB  . LEU   M  13 140 ? -0.588  -135.337 56.264  1.00 94.76  ? 127 LEU   M CB  1 
ATOM   22277 C  CG  . LEU   M  13 140 ? 0.389   -136.464 56.593  1.00 95.67  ? 127 LEU   M CG  1 
ATOM   22278 C  CD1 . LEU   M  13 140 ? 1.170   -136.156 57.861  1.00 95.85  ? 127 LEU   M CD1 1 
ATOM   22279 C  CD2 . LEU   M  13 140 ? -0.341  -137.792 56.724  1.00 97.65  ? 127 LEU   M CD2 1 
ATOM   22280 N  N   . ARG   M  13 141 ? 1.806   -133.834 54.052  1.00 82.68  ? 128 ARG   M N   1 
ATOM   22281 C  CA  . ARG   M  13 141 ? 2.396   -133.925 52.692  1.00 83.06  ? 128 ARG   M CA  1 
ATOM   22282 C  C   . ARG   M  13 141 ? 3.879   -134.302 52.773  1.00 78.45  ? 128 ARG   M C   1 
ATOM   22283 O  O   . ARG   M  13 141 ? 4.546   -133.915 53.746  1.00 77.77  ? 128 ARG   M O   1 
ATOM   22284 C  CB  . ARG   M  13 141 ? 2.177   -132.616 51.928  1.00 85.79  ? 128 ARG   M CB  1 
ATOM   22285 C  CG  . ARG   M  13 141 ? 2.219   -132.789 50.417  1.00 89.05  ? 128 ARG   M CG  1 
ATOM   22286 C  CD  . ARG   M  13 141 ? 1.777   -131.558 49.649  1.00 91.98  ? 128 ARG   M CD  1 
ATOM   22287 N  NE  . ARG   M  13 141 ? 2.065   -131.688 48.223  1.00 92.29  ? 128 ARG   M NE  1 
ATOM   22288 C  CZ  . ARG   M  13 141 ? 1.302   -132.327 47.336  1.00 90.63  ? 128 ARG   M CZ  1 
ATOM   22289 N  NH1 . ARG   M  13 141 ? 0.171   -132.903 47.708  1.00 91.05  ? 128 ARG   M NH1 1 
ATOM   22290 N  NH2 . ARG   M  13 141 ? 1.675   -132.385 46.069  1.00 90.83  ? 128 ARG   M NH2 1 
ATOM   22291 N  N   . TYR   M  13 142 ? 4.347   -135.032 51.758  1.00 77.50  ? 129 TYR   M N   1 
ATOM   22292 C  CA  . TYR   M  13 142 ? 5.703   -135.628 51.636  1.00 79.90  ? 129 TYR   M CA  1 
ATOM   22293 C  C   . TYR   M  13 142 ? 6.497   -134.839 50.593  1.00 76.70  ? 129 TYR   M C   1 
ATOM   22294 O  O   . TYR   M  13 142 ? 5.891   -134.371 49.619  1.00 78.81  ? 129 TYR   M O   1 
ATOM   22295 C  CB  . TYR   M  13 142 ? 5.575   -137.104 51.238  1.00 82.51  ? 129 TYR   M CB  1 
ATOM   22296 C  CG  . TYR   M  13 142 ? 6.853   -137.807 50.844  1.00 83.53  ? 129 TYR   M CG  1 
ATOM   22297 C  CD1 . TYR   M  13 142 ? 7.400   -137.653 49.578  1.00 84.12  ? 129 TYR   M CD1 1 
ATOM   22298 C  CD2 . TYR   M  13 142 ? 7.496   -138.663 51.723  1.00 81.99  ? 129 TYR   M CD2 1 
ATOM   22299 C  CE1 . TYR   M  13 142 ? 8.562   -138.309 49.204  1.00 84.55  ? 129 TYR   M CE1 1 
ATOM   22300 C  CE2 . TYR   M  13 142 ? 8.659   -139.326 51.365  1.00 84.55  ? 129 TYR   M CE2 1 
ATOM   22301 C  CZ  . TYR   M  13 142 ? 9.194   -139.151 50.102  1.00 84.62  ? 129 TYR   M CZ  1 
ATOM   22302 O  OH  . TYR   M  13 142 ? 10.337  -139.808 49.750  1.00 90.17  ? 129 TYR   M OH  1 
ATOM   22303 N  N   . VAL   M  13 143 ? 7.810   -134.709 50.792  1.00 74.27  ? 130 VAL   M N   1 
ATOM   22304 C  CA  . VAL   M  13 143 ? 8.765   -134.181 49.773  1.00 78.04  ? 130 VAL   M CA  1 
ATOM   22305 C  C   . VAL   M  13 143 ? 10.135  -134.807 50.043  1.00 75.62  ? 130 VAL   M C   1 
ATOM   22306 O  O   . VAL   M  13 143 ? 10.438  -135.056 51.226  1.00 76.47  ? 130 VAL   M O   1 
ATOM   22307 C  CB  . VAL   M  13 143 ? 8.822   -132.639 49.772  1.00 79.25  ? 130 VAL   M CB  1 
ATOM   22308 C  CG1 . VAL   M  13 143 ? 9.330   -132.071 51.091  1.00 80.33  ? 130 VAL   M CG1 1 
ATOM   22309 C  CG2 . VAL   M  13 143 ? 9.646   -132.108 48.609  1.00 81.42  ? 130 VAL   M CG2 1 
ATOM   22310 N  N   . ASN   M  13 144 ? 10.924  -135.054 48.993  1.00 74.44  ? 131 ASN   M N   1 
ATOM   22311 C  CA  . ASN   M  13 144 ? 12.217  -135.783 49.095  1.00 76.83  ? 131 ASN   M CA  1 
ATOM   22312 C  C   . ASN   M  13 144 ? 13.297  -135.080 48.265  1.00 73.70  ? 131 ASN   M C   1 
ATOM   22313 O  O   . ASN   M  13 144 ? 13.000  -134.031 47.664  1.00 71.14  ? 131 ASN   M O   1 
ATOM   22314 C  CB  . ASN   M  13 144 ? 12.056  -137.250 48.688  1.00 78.66  ? 131 ASN   M CB  1 
ATOM   22315 C  CG  . ASN   M  13 144 ? 11.763  -137.441 47.214  1.00 80.84  ? 131 ASN   M CG  1 
ATOM   22316 O  OD1 . ASN   M  13 144 ? 11.732  -136.482 46.446  1.00 78.70  ? 131 ASN   M OD1 1 
ATOM   22317 N  ND2 . ASN   M  13 144 ? 11.551  -138.682 46.810  1.00 83.56  ? 131 ASN   M ND2 1 
ATOM   22318 N  N   . LEU   M  13 145 ? 14.499  -135.667 48.235  1.00 74.52  ? 132 LEU   M N   1 
ATOM   22319 C  CA  . LEU   M  13 145 ? 15.720  -135.117 47.583  1.00 75.95  ? 132 LEU   M CA  1 
ATOM   22320 C  C   . LEU   M  13 145 ? 15.484  -134.847 46.089  1.00 76.59  ? 132 LEU   M C   1 
ATOM   22321 O  O   . LEU   M  13 145 ? 16.209  -133.997 45.546  1.00 79.20  ? 132 LEU   M O   1 
ATOM   22322 C  CB  . LEU   M  13 145 ? 16.899  -136.076 47.802  1.00 77.53  ? 132 LEU   M CB  1 
ATOM   22323 C  CG  . LEU   M  13 145 ? 16.959  -137.328 46.924  1.00 78.63  ? 132 LEU   M CG  1 
ATOM   22324 C  CD1 . LEU   M  13 145 ? 18.323  -137.991 47.049  1.00 80.73  ? 132 LEU   M CD1 1 
ATOM   22325 C  CD2 . LEU   M  13 145 ? 15.860  -138.319 47.285  1.00 78.00  ? 132 LEU   M CD2 1 
ATOM   22326 N  N   . LEU   M  13 146 ? 14.529  -135.536 45.451  1.00 78.91  ? 133 LEU   M N   1 
ATOM   22327 C  CA  . LEU   M  13 146 ? 14.188  -135.349 44.011  1.00 80.92  ? 133 LEU   M CA  1 
ATOM   22328 C  C   . LEU   M  13 146 ? 13.239  -134.159 43.833  1.00 79.82  ? 133 LEU   M C   1 
ATOM   22329 O  O   . LEU   M  13 146 ? 13.047  -133.739 42.679  1.00 80.95  ? 133 LEU   M O   1 
ATOM   22330 C  CB  . LEU   M  13 146 ? 13.534  -136.620 43.456  1.00 82.66  ? 133 LEU   M CB  1 
ATOM   22331 C  CG  . LEU   M  13 146 ? 14.433  -137.847 43.325  1.00 84.40  ? 133 LEU   M CG  1 
ATOM   22332 C  CD1 . LEU   M  13 146 ? 13.624  -139.051 42.864  1.00 88.12  ? 133 LEU   M CD1 1 
ATOM   22333 C  CD2 . LEU   M  13 146 ? 15.594  -137.590 42.374  1.00 83.47  ? 133 LEU   M CD2 1 
ATOM   22334 N  N   . GLY   M  13 147 ? 12.649  -133.655 44.921  1.00 80.96  ? 134 GLY   M N   1 
ATOM   22335 C  CA  . GLY   M  13 147 ? 11.603  -132.613 44.882  1.00 82.60  ? 134 GLY   M CA  1 
ATOM   22336 C  C   . GLY   M  13 147 ? 10.250  -133.189 44.497  1.00 80.80  ? 134 GLY   M C   1 
ATOM   22337 O  O   . GLY   M  13 147 ? 9.375   -132.417 44.068  1.00 78.89  ? 134 GLY   M O   1 
ATOM   22338 N  N   . VAL   M  13 148 ? 10.084  -134.506 44.637  1.00 81.73  ? 135 VAL   M N   1 
ATOM   22339 C  CA  . VAL   M  13 148 ? 8.791   -135.218 44.422  1.00 82.23  ? 135 VAL   M CA  1 
ATOM   22340 C  C   . VAL   M  13 148 ? 7.906   -134.944 45.636  1.00 83.38  ? 135 VAL   M C   1 
ATOM   22341 O  O   . VAL   M  13 148 ? 8.363   -135.209 46.762  1.00 84.70  ? 135 VAL   M O   1 
ATOM   22342 C  CB  . VAL   M  13 148 ? 8.997   -136.731 44.228  1.00 83.19  ? 135 VAL   M CB  1 
ATOM   22343 C  CG1 . VAL   M  13 148 ? 7.672   -137.475 44.164  1.00 83.73  ? 135 VAL   M CG1 1 
ATOM   22344 C  CG2 . VAL   M  13 148 ? 9.846   -137.030 43.002  1.00 85.73  ? 135 VAL   M CG2 1 
ATOM   22345 N  N   . THR   M  13 149 ? 6.694   -134.438 45.408  1.00 81.96  ? 136 THR   M N   1 
ATOM   22346 C  CA  . THR   M  13 149 ? 5.685   -134.168 46.463  1.00 82.35  ? 136 THR   M CA  1 
ATOM   22347 C  C   . THR   M  13 149 ? 4.462   -135.056 46.218  1.00 82.99  ? 136 THR   M C   1 
ATOM   22348 O  O   . THR   M  13 149 ? 4.106   -135.264 45.039  1.00 85.12  ? 136 THR   M O   1 
ATOM   22349 C  CB  . THR   M  13 149 ? 5.311   -132.680 46.517  1.00 80.16  ? 136 THR   M CB  1 
ATOM   22350 O  OG1 . THR   M  13 149 ? 4.589   -132.325 45.338  1.00 79.61  ? 136 THR   M OG1 1 
ATOM   22351 C  CG2 . THR   M  13 149 ? 6.516   -131.775 46.648  1.00 81.23  ? 136 THR   M CG2 1 
ATOM   22352 N  N   . TYR   M  13 150 ? 3.862   -135.573 47.290  1.00 80.37  ? 137 TYR   M N   1 
ATOM   22353 C  CA  . TYR   M  13 150 ? 2.545   -136.258 47.256  1.00 83.16  ? 137 TYR   M CA  1 
ATOM   22354 C  C   . TYR   M  13 150 ? 1.899   -136.186 48.640  1.00 81.14  ? 137 TYR   M C   1 
ATOM   22355 O  O   . TYR   M  13 150 ? 2.608   -135.925 49.630  1.00 77.63  ? 137 TYR   M O   1 
ATOM   22356 C  CB  . TYR   M  13 150 ? 2.676   -137.695 46.741  1.00 84.20  ? 137 TYR   M CB  1 
ATOM   22357 C  CG  . TYR   M  13 150 ? 3.803   -138.522 47.312  1.00 84.51  ? 137 TYR   M CG  1 
ATOM   22358 C  CD1 . TYR   M  13 150 ? 3.711   -139.101 48.568  1.00 84.93  ? 137 TYR   M CD1 1 
ATOM   22359 C  CD2 . TYR   M  13 150 ? 4.945   -138.774 46.568  1.00 85.62  ? 137 TYR   M CD2 1 
ATOM   22360 C  CE1 . TYR   M  13 150 ? 4.736   -139.882 49.081  1.00 85.90  ? 137 TYR   M CE1 1 
ATOM   22361 C  CE2 . TYR   M  13 150 ? 5.978   -139.552 47.065  1.00 85.99  ? 137 TYR   M CE2 1 
ATOM   22362 C  CZ  . TYR   M  13 150 ? 5.873   -140.114 48.324  1.00 85.84  ? 137 TYR   M CZ  1 
ATOM   22363 O  OH  . TYR   M  13 150 ? 6.896   -140.880 48.807  1.00 86.16  ? 137 TYR   M OH  1 
ATOM   22364 N  N   . SER   M  13 151 ? 0.582   -136.397 48.684  1.00 85.99  ? 138 SER   M N   1 
ATOM   22365 C  CA  . SER   M  13 151 ? -0.253  -136.386 49.912  1.00 90.74  ? 138 SER   M CA  1 
ATOM   22366 C  C   . SER   M  13 151 ? -1.159  -137.624 49.933  1.00 95.15  ? 138 SER   M C   1 
ATOM   22367 O  O   . SER   M  13 151 ? -1.613  -138.051 48.852  1.00 97.05  ? 138 SER   M O   1 
ATOM   22368 C  CB  . SER   M  13 151 ? -1.050  -135.113 49.999  1.00 90.22  ? 138 SER   M CB  1 
ATOM   22369 O  OG  . SER   M  13 151 ? -1.440  -134.842 51.335  1.00 92.92  ? 138 SER   M OG  1 
ATOM   22370 N  N   . SER   M  13 152 ? -1.400  -138.172 51.125  1.00 95.29  ? 139 SER   M N   1 
ATOM   22371 C  CA  . SER   M  13 152 ? -2.213  -139.392 51.364  1.00 96.95  ? 139 SER   M CA  1 
ATOM   22372 C  C   . SER   M  13 152 ? -2.673  -139.408 52.820  1.00 94.34  ? 139 SER   M C   1 
ATOM   22373 O  O   . SER   M  13 152 ? -2.000  -138.841 53.677  1.00 97.74  ? 139 SER   M O   1 
ATOM   22374 C  CB  . SER   M  13 152 ? -1.416  -140.624 51.017  1.00 99.29  ? 139 SER   M CB  1 
ATOM   22375 O  OG  . SER   M  13 152 ? -2.200  -141.802 51.139  1.00 104.34 ? 139 SER   M OG  1 
ATOM   22376 N  N   . PRO   M  13 153 ? -3.832  -140.026 53.150  1.00 91.71  ? 140 PRO   M N   1 
ATOM   22377 C  CA  . PRO   M  13 153 ? -4.254  -140.175 54.545  1.00 93.85  ? 140 PRO   M CA  1 
ATOM   22378 C  C   . PRO   M  13 153 ? -3.167  -140.745 55.474  1.00 93.80  ? 140 PRO   M C   1 
ATOM   22379 O  O   . PRO   M  13 153 ? -3.165  -140.393 56.640  1.00 96.76  ? 140 PRO   M O   1 
ATOM   22380 C  CB  . PRO   M  13 153 ? -5.440  -141.143 54.445  1.00 94.50  ? 140 PRO   M CB  1 
ATOM   22381 C  CG  . PRO   M  13 153 ? -6.022  -140.859 53.080  1.00 94.65  ? 140 PRO   M CG  1 
ATOM   22382 C  CD  . PRO   M  13 153 ? -4.821  -140.568 52.205  1.00 91.89  ? 140 PRO   M CD  1 
ATOM   22383 N  N   . THR   M  13 154 ? -2.296  -141.612 54.942  1.00 96.49  ? 141 THR   M N   1 
ATOM   22384 C  CA  . THR   M  13 154 ? -1.079  -142.145 55.614  1.00 92.14  ? 141 THR   M CA  1 
ATOM   22385 C  C   . THR   M  13 154 ? 0.147   -141.853 54.743  1.00 89.30  ? 141 THR   M C   1 
ATOM   22386 O  O   . THR   M  13 154 ? 0.068   -142.078 53.520  1.00 88.24  ? 141 THR   M O   1 
ATOM   22387 C  CB  . THR   M  13 154 ? -1.179  -143.656 55.869  1.00 91.78  ? 141 THR   M CB  1 
ATOM   22388 O  OG1 . THR   M  13 154 ? -0.959  -144.336 54.633  1.00 88.43  ? 141 THR   M OG1 1 
ATOM   22389 C  CG2 . THR   M  13 154 ? -2.514  -144.076 56.442  1.00 93.98  ? 141 THR   M CG2 1 
ATOM   22390 N  N   . LEU   M  13 155 ? 1.238   -141.388 55.355  1.00 86.61  ? 142 LEU   M N   1 
ATOM   22391 C  CA  . LEU   M  13 155 ? 2.540   -141.166 54.674  1.00 87.23  ? 142 LEU   M CA  1 
ATOM   22392 C  C   . LEU   M  13 155 ? 3.663   -141.723 55.548  1.00 84.31  ? 142 LEU   M C   1 
ATOM   22393 O  O   . LEU   M  13 155 ? 3.566   -141.618 56.788  1.00 80.04  ? 142 LEU   M O   1 
ATOM   22394 C  CB  . LEU   M  13 155 ? 2.744   -139.671 54.417  1.00 88.80  ? 142 LEU   M CB  1 
ATOM   22395 C  CG  . LEU   M  13 155 ? 1.904   -139.065 53.293  1.00 93.09  ? 142 LEU   M CG  1 
ATOM   22396 C  CD1 . LEU   M  13 155 ? 2.060   -137.553 53.271  1.00 96.08  ? 142 LEU   M CD1 1 
ATOM   22397 C  CD2 . LEU   M  13 155 ? 2.278   -139.649 51.940  1.00 95.18  ? 142 LEU   M CD2 1 
ATOM   22398 N  N   . ALA   M  13 156 ? 4.684   -142.290 54.907  1.00 83.79  ? 143 ALA   M N   1 
ATOM   22399 C  CA  . ALA   M  13 156 ? 5.874   -142.875 55.560  1.00 85.96  ? 143 ALA   M CA  1 
ATOM   22400 C  C   . ALA   M  13 156 ? 7.062   -142.814 54.595  1.00 82.01  ? 143 ALA   M C   1 
ATOM   22401 O  O   . ALA   M  13 156 ? 6.830   -142.692 53.375  1.00 78.99  ? 143 ALA   M O   1 
ATOM   22402 C  CB  . ALA   M  13 156 ? 5.563   -144.287 56.002  1.00 89.36  ? 143 ALA   M CB  1 
ATOM   22403 N  N   . THR   M  13 157 ? 8.284   -142.883 55.130  1.00 83.59  ? 144 THR   M N   1 
ATOM   22404 C  CA  . THR   M  13 157 ? 9.559   -142.837 54.363  1.00 88.13  ? 144 THR   M CA  1 
ATOM   22405 C  C   . THR   M  13 157 ? 10.364  -144.119 54.610  1.00 89.60  ? 144 THR   M C   1 
ATOM   22406 O  O   . THR   M  13 157 ? 10.218  -144.709 55.700  1.00 94.69  ? 144 THR   M O   1 
ATOM   22407 C  CB  . THR   M  13 157 ? 10.375  -141.590 54.731  1.00 87.76  ? 144 THR   M CB  1 
ATOM   22408 O  OG1 . THR   M  13 157 ? 11.022  -141.799 55.988  1.00 86.88  ? 144 THR   M OG1 1 
ATOM   22409 C  CG2 . THR   M  13 157 ? 9.527   -140.340 54.810  1.00 88.40  ? 144 THR   M CG2 1 
ATOM   22410 N  N   . GLY   M  13 158 ? 11.174  -144.530 53.629  1.00 89.75  ? 145 GLY   M N   1 
ATOM   22411 C  CA  . GLY   M  13 158 ? 12.095  -145.680 53.733  1.00 90.01  ? 145 GLY   M CA  1 
ATOM   22412 C  C   . GLY   M  13 158 ? 11.350  -146.987 53.942  1.00 90.78  ? 145 GLY   M C   1 
ATOM   22413 O  O   . GLY   M  13 158 ? 10.424  -147.262 53.156  1.00 91.27  ? 145 GLY   M O   1 
ATOM   22414 N  N   . PHE   M  13 159 ? 11.734  -147.761 54.964  1.00 91.31  ? 146 PHE   M N   1 
ATOM   22415 C  CA  . PHE   M  13 159 ? 11.105  -149.058 55.333  1.00 92.66  ? 146 PHE   M CA  1 
ATOM   22416 C  C   . PHE   M  13 159 ? 9.657   -148.826 55.777  1.00 89.95  ? 146 PHE   M C   1 
ATOM   22417 O  O   . PHE   M  13 159 ? 8.819   -149.722 55.549  1.00 95.50  ? 146 PHE   M O   1 
ATOM   22418 C  CB  . PHE   M  13 159 ? 11.912  -149.790 56.410  1.00 95.62  ? 146 PHE   M CB  1 
ATOM   22419 C  CG  . PHE   M  13 159 ? 13.012  -150.657 55.857  1.00 97.09  ? 146 PHE   M CG  1 
ATOM   22420 C  CD1 . PHE   M  13 159 ? 12.718  -151.868 55.248  1.00 96.75  ? 146 PHE   M CD1 1 
ATOM   22421 C  CD2 . PHE   M  13 159 ? 14.338  -150.254 55.921  1.00 99.71  ? 146 PHE   M CD2 1 
ATOM   22422 C  CE1 . PHE   M  13 159 ? 13.727  -152.661 54.724  1.00 98.29  ? 146 PHE   M CE1 1 
ATOM   22423 C  CE2 . PHE   M  13 159 ? 15.346  -151.051 55.399  1.00 99.58  ? 146 PHE   M CE2 1 
ATOM   22424 C  CZ  . PHE   M  13 159 ? 15.039  -152.252 54.802  1.00 100.60 ? 146 PHE   M CZ  1 
ATOM   22425 N  N   . GLY   M  13 160 ? 9.375   -147.669 56.386  1.00 84.90  ? 147 GLY   M N   1 
ATOM   22426 C  CA  . GLY   M  13 160 ? 8.015   -147.260 56.785  1.00 84.51  ? 147 GLY   M CA  1 
ATOM   22427 C  C   . GLY   M  13 160 ? 7.051   -147.331 55.614  1.00 84.99  ? 147 GLY   M C   1 
ATOM   22428 O  O   . GLY   M  13 160 ? 5.908   -147.779 55.816  1.00 85.52  ? 147 GLY   M O   1 
ATOM   22429 N  N   . ALA   M  13 161 ? 7.503   -146.928 54.423  1.00 86.16  ? 148 ALA   M N   1 
ATOM   22430 C  CA  . ALA   M  13 161 ? 6.710   -146.920 53.171  1.00 89.53  ? 148 ALA   M CA  1 
ATOM   22431 C  C   . ALA   M  13 161 ? 6.272   -148.347 52.811  1.00 91.70  ? 148 ALA   M C   1 
ATOM   22432 O  O   . ALA   M  13 161 ? 5.200   -148.487 52.190  1.00 99.92  ? 148 ALA   M O   1 
ATOM   22433 C  CB  . ALA   M  13 161 ? 7.504   -146.291 52.051  1.00 87.04  ? 148 ALA   M CB  1 
ATOM   22434 N  N   . HIS   M  13 162 ? 7.063   -149.359 53.191  1.00 91.67  ? 149 HIS   M N   1 
ATOM   22435 C  CA  . HIS   M  13 162 ? 6.854   -150.788 52.831  1.00 89.68  ? 149 HIS   M CA  1 
ATOM   22436 C  C   . HIS   M  13 162 ? 6.100   -151.545 53.932  1.00 90.05  ? 149 HIS   M C   1 
ATOM   22437 O  O   . HIS   M  13 162 ? 5.346   -152.467 53.573  1.00 89.80  ? 149 HIS   M O   1 
ATOM   22438 C  CB  . HIS   M  13 162 ? 8.196   -151.466 52.526  1.00 87.86  ? 149 HIS   M CB  1 
ATOM   22439 C  CG  . HIS   M  13 162 ? 8.913   -150.875 51.361  1.00 85.29  ? 149 HIS   M CG  1 
ATOM   22440 N  ND1 . HIS   M  13 162 ? 10.093  -150.170 51.499  1.00 80.48  ? 149 HIS   M ND1 1 
ATOM   22441 C  CD2 . HIS   M  13 162 ? 8.622   -150.876 50.042  1.00 85.40  ? 149 HIS   M CD2 1 
ATOM   22442 C  CE1 . HIS   M  13 162 ? 10.502  -149.768 50.313  1.00 80.22  ? 149 HIS   M CE1 1 
ATOM   22443 N  NE2 . HIS   M  13 162 ? 9.616   -150.185 49.404  1.00 81.51  ? 149 HIS   M NE2 1 
ATOM   22444 N  N   . MET   M  13 163 ? 6.303   -151.192 55.207  1.00 90.81  ? 150 MET   M N   1 
ATOM   22445 C  CA  . MET   M  13 163 ? 5.815   -151.982 56.373  1.00 92.43  ? 150 MET   M CA  1 
ATOM   22446 C  C   . MET   M  13 163 ? 4.753   -151.210 57.168  1.00 94.15  ? 150 MET   M C   1 
ATOM   22447 O  O   . MET   M  13 163 ? 3.755   -151.842 57.562  1.00 98.74  ? 150 MET   M O   1 
ATOM   22448 C  CB  . MET   M  13 163 ? 6.976   -152.365 57.296  1.00 94.21  ? 150 MET   M CB  1 
ATOM   22449 C  CG  . MET   M  13 163 ? 8.029   -153.211 56.601  1.00 96.11  ? 150 MET   M CG  1 
ATOM   22450 S  SD  . MET   M  13 163 ? 8.946   -154.283 57.734  1.00 100.25 ? 150 MET   M SD  1 
ATOM   22451 C  CE  . MET   M  13 163 ? 7.730   -155.571 58.010  1.00 99.76  ? 150 MET   M CE  1 
ATOM   22452 N  N   . ALA   M  13 164 ? 4.947   -149.910 57.406  1.00 92.16  ? 151 ALA   M N   1 
ATOM   22453 C  CA  . ALA   M  13 164 ? 4.018   -149.065 58.197  1.00 94.06  ? 151 ALA   M CA  1 
ATOM   22454 C  C   . ALA   M  13 164 ? 2.750   -148.773 57.383  1.00 94.37  ? 151 ALA   M C   1 
ATOM   22455 O  O   . ALA   M  13 164 ? 1.648   -148.977 57.923  1.00 94.59  ? 151 ALA   M O   1 
ATOM   22456 C  CB  . ALA   M  13 164 ? 4.701   -147.794 58.640  1.00 94.38  ? 151 ALA   M CB  1 
ATOM   22457 N  N   . ASN   M  13 165 ? 2.904   -148.329 56.131  1.00 95.67  ? 152 ASN   M N   1 
ATOM   22458 C  CA  . ASN   M  13 165 ? 1.782   -147.889 55.253  1.00 96.10  ? 152 ASN   M CA  1 
ATOM   22459 C  C   . ASN   M  13 165 ? 0.719   -148.984 55.168  1.00 94.34  ? 152 ASN   M C   1 
ATOM   22460 O  O   . ASN   M  13 165 ? -0.454  -148.695 55.390  1.00 93.64  ? 152 ASN   M O   1 
ATOM   22461 C  CB  . ASN   M  13 165 ? 2.264   -147.442 53.867  1.00 99.19  ? 152 ASN   M CB  1 
ATOM   22462 C  CG  . ASN   M  13 165 ? 2.548   -145.955 53.780  1.00 98.76  ? 152 ASN   M CG  1 
ATOM   22463 O  OD1 . ASN   M  13 165 ? 2.005   -145.162 54.548  1.00 101.45 ? 152 ASN   M OD1 1 
ATOM   22464 N  ND2 . ASN   M  13 165 ? 3.388   -145.561 52.837  1.00 98.89  ? 152 ASN   M ND2 1 
ATOM   22465 N  N   . PRO   M  13 166 ? 1.067   -150.253 54.837  1.00 96.53  ? 153 PRO   M N   1 
ATOM   22466 C  CA  . PRO   M  13 166 ? 0.080   -151.337 54.813  1.00 95.89  ? 153 PRO   M CA  1 
ATOM   22467 C  C   . PRO   M  13 166 ? -0.752  -151.467 56.100  1.00 94.40  ? 153 PRO   M C   1 
ATOM   22468 O  O   . PRO   M  13 166 ? -1.942  -151.704 55.986  1.00 92.44  ? 153 PRO   M O   1 
ATOM   22469 C  CB  . PRO   M  13 166 ? 0.942   -152.590 54.603  1.00 96.06  ? 153 PRO   M CB  1 
ATOM   22470 C  CG  . PRO   M  13 166 ? 2.128   -152.080 53.822  1.00 95.22  ? 153 PRO   M CG  1 
ATOM   22471 C  CD  . PRO   M  13 166 ? 2.402   -150.714 54.417  1.00 94.91  ? 153 PRO   M CD  1 
ATOM   22472 N  N   . LEU   M  13 167 ? -0.120  -151.309 57.271  1.00 96.27  ? 154 LEU   M N   1 
ATOM   22473 C  CA  . LEU   M  13 167 ? -0.775  -151.411 58.608  1.00 97.73  ? 154 LEU   M CA  1 
ATOM   22474 C  C   . LEU   M  13 167 ? -1.675  -150.195 58.852  1.00 98.57  ? 154 LEU   M C   1 
ATOM   22475 O  O   . LEU   M  13 167 ? -2.815  -150.396 59.316  1.00 97.54  ? 154 LEU   M O   1 
ATOM   22476 C  CB  . LEU   M  13 167 ? 0.290   -151.505 59.706  1.00 96.85  ? 154 LEU   M CB  1 
ATOM   22477 C  CG  . LEU   M  13 167 ? 1.133   -152.777 59.717  1.00 94.52  ? 154 LEU   M CG  1 
ATOM   22478 C  CD1 . LEU   M  13 167 ? 2.238   -152.669 60.756  1.00 95.95  ? 154 LEU   M CD1 1 
ATOM   22479 C  CD2 . LEU   M  13 167 ? 0.273   -154.002 59.980  1.00 96.05  ? 154 LEU   M CD2 1 
ATOM   22480 N  N   . LEU   M  13 168 ? -1.167  -148.985 58.581  1.00 99.37  ? 155 LEU   M N   1 
ATOM   22481 C  CA  . LEU   M  13 168 ? -1.885  -147.700 58.812  1.00 98.53  ? 155 LEU   M CA  1 
ATOM   22482 C  C   . LEU   M  13 168 ? -3.067  -147.578 57.841  1.00 97.91  ? 155 LEU   M C   1 
ATOM   22483 O  O   . LEU   M  13 168 ? -4.067  -146.943 58.222  1.00 97.18  ? 155 LEU   M O   1 
ATOM   22484 C  CB  . LEU   M  13 168 ? -0.921  -146.521 58.633  1.00 97.47  ? 155 LEU   M CB  1 
ATOM   22485 C  CG  . LEU   M  13 168 ? 0.294   -146.475 59.561  1.00 97.18  ? 155 LEU   M CG  1 
ATOM   22486 C  CD1 . LEU   M  13 168 ? 1.106   -145.212 59.308  1.00 96.97  ? 155 LEU   M CD1 1 
ATOM   22487 C  CD2 . LEU   M  13 168 ? -0.110  -146.555 61.026  1.00 97.01  ? 155 LEU   M CD2 1 
ATOM   22488 N  N   . ARG   M  13 169 ? -2.951  -148.152 56.637  1.00 100.44 ? 156 ARG   M N   1 
ATOM   22489 C  CA  . ARG   M  13 169 ? -4.006  -148.118 55.584  1.00 102.18 ? 156 ARG   M CA  1 
ATOM   22490 C  C   . ARG   M  13 169 ? -5.180  -149.034 55.964  1.00 105.76 ? 156 ARG   M C   1 
ATOM   22491 O  O   . ARG   M  13 169 ? -6.276  -148.821 55.411  1.00 108.61 ? 156 ARG   M O   1 
ATOM   22492 C  CB  . ARG   M  13 169 ? -3.434  -148.498 54.213  1.00 99.99  ? 156 ARG   M CB  1 
ATOM   22493 C  CG  . ARG   M  13 169 ? -2.734  -147.348 53.502  1.00 98.87  ? 156 ARG   M CG  1 
ATOM   22494 C  CD  . ARG   M  13 169 ? -1.812  -147.793 52.379  1.00 95.42  ? 156 ARG   M CD  1 
ATOM   22495 N  NE  . ARG   M  13 169 ? -1.036  -146.678 51.845  1.00 93.61  ? 156 ARG   M NE  1 
ATOM   22496 C  CZ  . ARG   M  13 169 ? -0.099  -146.774 50.903  1.00 91.18  ? 156 ARG   M CZ  1 
ATOM   22497 N  NH1 . ARG   M  13 169 ? 0.204   -147.942 50.367  1.00 87.49  ? 156 ARG   M NH1 1 
ATOM   22498 N  NH2 . ARG   M  13 169 ? 0.538   -145.691 50.495  1.00 92.67  ? 156 ARG   M NH2 1 
ATOM   22499 N  N   . LYS   M  13 170 ? -4.972  -150.012 56.857  1.00 108.30 ? 157 LYS   M N   1 
ATOM   22500 C  CA  . LYS   M  13 170 ? -6.051  -150.898 57.380  1.00 109.87 ? 157 LYS   M CA  1 
ATOM   22501 C  C   . LYS   M  13 170 ? -6.991  -150.090 58.288  1.00 107.44 ? 157 LYS   M C   1 
ATOM   22502 O  O   . LYS   M  13 170 ? -8.158  -150.505 58.434  1.00 108.53 ? 157 LYS   M O   1 
ATOM   22503 C  CB  . LYS   M  13 170 ? -5.469  -152.105 58.127  1.00 112.49 ? 157 LYS   M CB  1 
ATOM   22504 C  CG  . LYS   M  13 170 ? -4.856  -153.181 57.238  1.00 114.11 ? 157 LYS   M CG  1 
ATOM   22505 C  CD  . LYS   M  13 170 ? -4.071  -154.232 58.001  1.00 116.12 ? 157 LYS   M CD  1 
ATOM   22506 C  CE  . LYS   M  13 170 ? -4.940  -155.312 58.612  1.00 118.21 ? 157 LYS   M CE  1 
ATOM   22507 N  NZ  . LYS   M  13 170 ? -5.369  -156.312 57.606  1.00 118.84 ? 157 LYS   M NZ  1 
ATOM   22508 N  N   . VAL   M  13 171 ? -6.500  -148.989 58.874  1.00 105.35 ? 158 VAL   M N   1 
ATOM   22509 C  CA  . VAL   M  13 171 ? -7.280  -148.069 59.759  1.00 103.60 ? 158 VAL   M CA  1 
ATOM   22510 C  C   . VAL   M  13 171 ? -7.924  -146.972 58.899  1.00 102.59 ? 158 VAL   M C   1 
ATOM   22511 O  O   . VAL   M  13 171 ? -9.154  -146.790 59.006  1.00 96.57  ? 158 VAL   M O   1 
ATOM   22512 C  CB  . VAL   M  13 171 ? -6.396  -147.471 60.872  1.00 102.84 ? 158 VAL   M CB  1 
ATOM   22513 C  CG1 . VAL   M  13 171 ? -7.178  -146.522 61.770  1.00 101.97 ? 158 VAL   M CG1 1 
ATOM   22514 C  CG2 . VAL   M  13 171 ? -5.729  -148.554 61.706  1.00 105.51 ? 158 VAL   M CG2 1 
ATOM   22515 N  N   . VAL   M  13 172 ? -7.122  -146.262 58.095  1.00 101.79 ? 159 VAL   M N   1 
ATOM   22516 C  CA  . VAL   M  13 172 ? -7.588  -145.176 57.176  1.00 103.09 ? 159 VAL   M CA  1 
ATOM   22517 C  C   . VAL   M  13 172 ? -7.194  -145.536 55.739  1.00 102.50 ? 159 VAL   M C   1 
ATOM   22518 O  O   . VAL   M  13 172 ? -6.077  -145.177 55.308  1.00 93.46  ? 159 VAL   M O   1 
ATOM   22519 C  CB  . VAL   M  13 172 ? -7.061  -143.785 57.586  1.00 104.38 ? 159 VAL   M CB  1 
ATOM   22520 C  CG1 . VAL   M  13 172 ? -7.902  -143.179 58.699  1.00 107.73 ? 159 VAL   M CG1 1 
ATOM   22521 C  CG2 . VAL   M  13 172 ? -5.591  -143.800 57.976  1.00 103.22 ? 159 VAL   M CG2 1 
ATOM   22522 N  N   . ASP   M  13 173 ? -8.102  -146.212 55.027  1.00 107.51 ? 160 ASP   M N   1 
ATOM   22523 C  CA  . ASP   M  13 173 ? -7.878  -146.742 53.656  1.00 110.76 ? 160 ASP   M CA  1 
ATOM   22524 C  C   . ASP   M  13 173 ? -8.270  -145.683 52.616  1.00 112.60 ? 160 ASP   M C   1 
ATOM   22525 O  O   . ASP   M  13 173 ? -7.747  -145.760 51.486  1.00 116.22 ? 160 ASP   M O   1 
ATOM   22526 C  CB  . ASP   M  13 173 ? -8.640  -148.053 53.441  1.00 111.26 ? 160 ASP   M CB  1 
ATOM   22527 C  CG  . ASP   M  13 173 ? -8.019  -148.955 52.388  1.00 110.71 ? 160 ASP   M CG  1 
ATOM   22528 O  OD1 . ASP   M  13 173 ? -6.779  -148.935 52.253  1.00 109.47 ? 160 ASP   M OD1 1 
ATOM   22529 O  OD2 . ASP   M  13 173 ? -8.781  -149.664 51.704  1.00 113.05 ? 160 ASP   M OD2 1 
ATOM   22530 N  N   . ARG   M  13 174 ? -9.157  -144.745 52.969  1.00 113.83 ? 161 ARG   M N   1 
ATOM   22531 C  CA  . ARG   M  13 174 ? -9.542  -143.610 52.086  1.00 115.93 ? 161 ARG   M CA  1 
ATOM   22532 C  C   . ARG   M  13 174 ? -10.000 -142.416 52.933  1.00 118.11 ? 161 ARG   M C   1 
ATOM   22533 O  O   . ARG   M  13 174 ? -10.005 -142.536 54.172  1.00 126.12 ? 161 ARG   M O   1 
ATOM   22534 C  CB  . ARG   M  13 174 ? -10.612 -144.041 51.076  1.00 119.34 ? 161 ARG   M CB  1 
ATOM   22535 C  CG  . ARG   M  13 174 ? -12.001 -144.283 51.652  1.00 124.31 ? 161 ARG   M CG  1 
ATOM   22536 C  CD  . ARG   M  13 174 ? -12.343 -145.743 51.907  1.00 125.80 ? 161 ARG   M CD  1 
ATOM   22537 N  NE  . ARG   M  13 174 ? -11.919 -146.663 50.855  1.00 129.24 ? 161 ARG   M NE  1 
ATOM   22538 C  CZ  . ARG   M  13 174 ? -12.418 -146.718 49.619  1.00 129.39 ? 161 ARG   M CZ  1 
ATOM   22539 N  NH1 . ARG   M  13 174 ? -13.372 -145.887 49.230  1.00 128.28 ? 161 ARG   M NH1 1 
ATOM   22540 N  NH2 . ARG   M  13 174 ? -11.948 -147.611 48.763  1.00 130.84 ? 161 ARG   M NH2 1 
ATOM   22541 N  N   . GLU   M  13 175 ? -10.366 -141.312 52.271  1.00 120.50 ? 162 GLU   M N   1 
ATOM   22542 C  CA  . GLU   M  13 175 ? -10.715 -140.010 52.902  1.00 121.18 ? 162 GLU   M CA  1 
ATOM   22543 C  C   . GLU   M  13 175 ? -11.828 -140.219 53.937  1.00 116.67 ? 162 GLU   M C   1 
ATOM   22544 O  O   . GLU   M  13 175 ? -11.673 -139.725 55.069  1.00 116.68 ? 162 GLU   M O   1 
ATOM   22545 C  CB  . GLU   M  13 175 ? -11.152 -138.995 51.842  1.00 128.04 ? 162 GLU   M CB  1 
ATOM   22546 C  CG  . GLU   M  13 175 ? -10.979 -137.545 52.271  1.00 134.18 ? 162 GLU   M CG  1 
ATOM   22547 C  CD  . GLU   M  13 175 ? -9.554  -137.012 52.247  1.00 138.83 ? 162 GLU   M CD  1 
ATOM   22548 O  OE1 . GLU   M  13 175 ? -9.350  -135.851 52.670  1.00 133.76 ? 162 GLU   M OE1 1 
ATOM   22549 O  OE2 . GLU   M  13 175 ? -8.649  -137.752 51.805  1.00 148.96 ? 162 GLU   M OE2 1 
ATOM   22550 N  N   . SER   M  13 176 ? -12.890 -140.942 53.563  1.00 113.45 ? 163 SER   M N   1 
ATOM   22551 C  CA  . SER   M  13 176 ? -14.122 -141.145 54.374  1.00 113.60 ? 163 SER   M CA  1 
ATOM   22552 C  C   . SER   M  13 176 ? -13.817 -141.864 55.696  1.00 110.75 ? 163 SER   M C   1 
ATOM   22553 O  O   . SER   M  13 176 ? -14.666 -141.785 56.603  1.00 114.33 ? 163 SER   M O   1 
ATOM   22554 C  CB  . SER   M  13 176 ? -15.169 -141.890 53.589  1.00 112.96 ? 163 SER   M CB  1 
ATOM   22555 O  OG  . SER   M  13 176 ? -14.633 -143.086 53.045  1.00 113.99 ? 163 SER   M OG  1 
ATOM   22556 N  N   . ASP   M  13 177 ? -12.670 -142.543 55.803  1.00 111.32 ? 164 ASP   M N   1 
ATOM   22557 C  CA  . ASP   M  13 177 ? -12.248 -143.270 57.032  1.00 114.37 ? 164 ASP   M CA  1 
ATOM   22558 C  C   . ASP   M  13 177 ? -11.721 -142.284 58.089  1.00 111.62 ? 164 ASP   M C   1 
ATOM   22559 O  O   . ASP   M  13 177 ? -11.714 -142.660 59.280  1.00 109.87 ? 164 ASP   M O   1 
ATOM   22560 C  CB  . ASP   M  13 177 ? -11.200 -144.345 56.719  1.00 118.21 ? 164 ASP   M CB  1 
ATOM   22561 C  CG  . ASP   M  13 177 ? -11.718 -145.524 55.909  1.00 121.01 ? 164 ASP   M CG  1 
ATOM   22562 O  OD1 . ASP   M  13 177 ? -12.951 -145.631 55.736  1.00 124.46 ? 164 ASP   M OD1 1 
ATOM   22563 O  OD2 . ASP   M  13 177 ? -10.880 -146.334 55.461  1.00 120.24 ? 164 ASP   M OD2 1 
ATOM   22564 N  N   . ILE   M  13 178 ? -11.299 -141.078 57.690  1.00 107.59 ? 165 ILE   M N   1 
ATOM   22565 C  CA  . ILE   M  13 178 ? -10.596 -140.106 58.584  1.00 106.19 ? 165 ILE   M CA  1 
ATOM   22566 C  C   . ILE   M  13 178 ? -11.536 -139.631 59.693  1.00 110.30 ? 165 ILE   M C   1 
ATOM   22567 O  O   . ILE   M  13 178 ? -11.146 -139.655 60.858  1.00 114.76 ? 165 ILE   M O   1 
ATOM   22568 C  CB  . ILE   M  13 178 ? -9.973  -138.941 57.785  1.00 103.81 ? 165 ILE   M CB  1 
ATOM   22569 C  CG1 . ILE   M  13 178 ? -8.785  -139.425 56.948  1.00 100.05 ? 165 ILE   M CG1 1 
ATOM   22570 C  CG2 . ILE   M  13 178 ? -9.582  -137.798 58.712  1.00 103.64 ? 165 ILE   M CG2 1 
ATOM   22571 C  CD1 . ILE   M  13 178 ? -8.275  -138.421 55.940  1.00 98.87  ? 165 ILE   M CD1 1 
ATOM   22572 N  N   . PRO   M  13 179 ? -12.779 -139.174 59.399  1.00 111.32 ? 166 PRO   M N   1 
ATOM   22573 C  CA  . PRO   M  13 179 ? -13.725 -138.801 60.455  1.00 112.56 ? 166 PRO   M CA  1 
ATOM   22574 C  C   . PRO   M  13 179 ? -14.071 -139.934 61.434  1.00 111.81 ? 166 PRO   M C   1 
ATOM   22575 O  O   . PRO   M  13 179 ? -14.447 -139.636 62.553  1.00 113.90 ? 166 PRO   M O   1 
ATOM   22576 C  CB  . PRO   M  13 179 ? -15.000 -138.405 59.695  1.00 115.03 ? 166 PRO   M CB  1 
ATOM   22577 C  CG  . PRO   M  13 179 ? -14.510 -138.025 58.317  1.00 113.54 ? 166 PRO   M CG  1 
ATOM   22578 C  CD  . PRO   M  13 179 ? -13.331 -138.939 58.056  1.00 111.09 ? 166 PRO   M CD  1 
ATOM   22579 N  N   . LYS   M  13 180 ? -13.942 -141.188 60.988  1.00 113.83 ? 167 LYS   M N   1 
ATOM   22580 C  CA  . LYS   M  13 180 ? -14.310 -142.405 61.761  1.00 116.23 ? 167 LYS   M CA  1 
ATOM   22581 C  C   . LYS   M  13 180 ? -13.149 -142.835 62.670  1.00 113.27 ? 167 LYS   M C   1 
ATOM   22582 O  O   . LYS   M  13 180 ? -13.366 -143.745 63.491  1.00 119.31 ? 167 LYS   M O   1 
ATOM   22583 C  CB  . LYS   M  13 180 ? -14.706 -143.535 60.804  1.00 116.06 ? 167 LYS   M CB  1 
ATOM   22584 C  CG  . LYS   M  13 180 ? -15.790 -143.173 59.796  1.00 116.45 ? 167 LYS   M CG  1 
ATOM   22585 C  CD  . LYS   M  13 180 ? -16.200 -144.311 58.890  1.00 117.26 ? 167 LYS   M CD  1 
ATOM   22586 C  CE  . LYS   M  13 180 ? -17.183 -143.879 57.822  1.00 119.17 ? 167 LYS   M CE  1 
ATOM   22587 N  NZ  . LYS   M  13 180 ? -17.612 -145.019 56.978  1.00 121.29 ? 167 LYS   M NZ  1 
ATOM   22588 N  N   . THR   M  13 181 ? -11.973 -142.208 62.546  1.00 108.71 ? 168 THR   M N   1 
ATOM   22589 C  CA  . THR   M  13 181 ? -10.741 -142.579 63.293  1.00 109.56 ? 168 THR   M CA  1 
ATOM   22590 C  C   . THR   M  13 181 ? -10.509 -141.598 64.445  1.00 112.74 ? 168 THR   M C   1 
ATOM   22591 O  O   . THR   M  13 181 ? -10.469 -140.382 64.178  1.00 115.25 ? 168 THR   M O   1 
ATOM   22592 C  CB  . THR   M  13 181 ? -9.513  -142.600 62.377  1.00 108.32 ? 168 THR   M CB  1 
ATOM   22593 O  OG1 . THR   M  13 181 ? -9.826  -143.411 61.245  1.00 106.90 ? 168 THR   M OG1 1 
ATOM   22594 C  CG2 . THR   M  13 181 ? -8.278  -143.126 63.076  1.00 109.04 ? 168 THR   M CG2 1 
ATOM   22595 N  N   . THR   M  13 182 ? -10.327 -142.117 65.663  1.00 111.04 ? 169 THR   M N   1 
ATOM   22596 C  CA  . THR   M  13 182 ? -10.031 -141.327 66.888  1.00 108.77 ? 169 THR   M CA  1 
ATOM   22597 C  C   . THR   M  13 182 ? -8.516  -141.285 67.111  1.00 106.26 ? 169 THR   M C   1 
ATOM   22598 O  O   . THR   M  13 182 ? -7.805  -142.118 66.518  1.00 99.25  ? 169 THR   M O   1 
ATOM   22599 C  CB  . THR   M  13 182 ? -10.760 -141.895 68.111  1.00 109.03 ? 169 THR   M CB  1 
ATOM   22600 O  OG1 . THR   M  13 182 ? -10.240 -143.198 68.378  1.00 105.22 ? 169 THR   M OG1 1 
ATOM   22601 C  CG2 . THR   M  13 182 ? -12.259 -141.962 67.918  1.00 110.60 ? 169 THR   M CG2 1 
ATOM   22602 N  N   . VAL   M  13 183 ? -8.055  -140.341 67.937  1.00 110.68 ? 170 VAL   M N   1 
ATOM   22603 C  CA  . VAL   M  13 183 ? -6.615  -140.142 68.284  1.00 111.92 ? 170 VAL   M CA  1 
ATOM   22604 C  C   . VAL   M  13 183 ? -6.097  -141.386 69.024  1.00 110.91 ? 170 VAL   M C   1 
ATOM   22605 O  O   . VAL   M  13 183 ? -4.909  -141.726 68.842  1.00 103.19 ? 170 VAL   M O   1 
ATOM   22606 C  CB  . VAL   M  13 183 ? -6.408  -138.849 69.100  1.00 113.79 ? 170 VAL   M CB  1 
ATOM   22607 C  CG1 . VAL   M  13 183 ? -6.998  -138.939 70.501  1.00 117.23 ? 170 VAL   M CG1 1 
ATOM   22608 C  CG2 . VAL   M  13 183 ? -4.940  -138.452 69.159  1.00 111.78 ? 170 VAL   M CG2 1 
ATOM   22609 N  N   . GLN   M  13 184 ? -6.954  -142.046 69.812  1.00 113.08 ? 171 GLN   M N   1 
ATOM   22610 C  CA  . GLN   M  13 184 ? -6.603  -143.278 70.571  1.00 115.02 ? 171 GLN   M CA  1 
ATOM   22611 C  C   . GLN   M  13 184 ? -6.283  -144.397 69.574  1.00 112.02 ? 171 GLN   M C   1 
ATOM   22612 O  O   . GLN   M  13 184 ? -5.214  -145.021 69.716  1.00 109.43 ? 171 GLN   M O   1 
ATOM   22613 C  CB  . GLN   M  13 184 ? -7.733  -143.699 71.515  1.00 118.57 ? 171 GLN   M CB  1 
ATOM   22614 C  CG  . GLN   M  13 184 ? -7.854  -142.830 72.761  1.00 123.36 ? 171 GLN   M CG  1 
ATOM   22615 C  CD  . GLN   M  13 184 ? -8.638  -141.558 72.534  1.00 124.56 ? 171 GLN   M CD  1 
ATOM   22616 O  OE1 . GLN   M  13 184 ? -9.383  -141.422 71.565  1.00 122.48 ? 171 GLN   M OE1 1 
ATOM   22617 N  NE2 . GLN   M  13 184 ? -8.480  -140.608 73.442  1.00 125.73 ? 171 GLN   M NE2 1 
ATOM   22618 N  N   . VAL   M  13 185 ? -7.174  -144.617 68.599  1.00 113.47 ? 172 VAL   M N   1 
ATOM   22619 C  CA  . VAL   M  13 185 ? -7.053  -145.670 67.544  1.00 110.71 ? 172 VAL   M CA  1 
ATOM   22620 C  C   . VAL   M  13 185 ? -5.829  -145.361 66.669  1.00 110.36 ? 172 VAL   M C   1 
ATOM   22621 O  O   . VAL   M  13 185 ? -5.054  -146.298 66.392  1.00 112.62 ? 172 VAL   M O   1 
ATOM   22622 C  CB  . VAL   M  13 185 ? -8.343  -145.781 66.703  1.00 110.07 ? 172 VAL   M CB  1 
ATOM   22623 C  CG1 . VAL   M  13 185 ? -8.152  -146.647 65.465  1.00 107.30 ? 172 VAL   M CG1 1 
ATOM   22624 C  CG2 . VAL   M  13 185 ? -9.513  -146.294 67.531  1.00 110.13 ? 172 VAL   M CG2 1 
ATOM   22625 N  N   . ALA   M  13 186 ? -5.670  -144.099 66.256  1.00 106.85 ? 173 ALA   M N   1 
ATOM   22626 C  CA  . ALA   M  13 186 ? -4.595  -143.622 65.353  1.00 101.79 ? 173 ALA   M CA  1 
ATOM   22627 C  C   . ALA   M  13 186 ? -3.225  -143.822 66.009  1.00 99.60  ? 173 ALA   M C   1 
ATOM   22628 O  O   . ALA   M  13 186 ? -2.341  -144.399 65.352  1.00 98.39  ? 173 ALA   M O   1 
ATOM   22629 C  CB  . ALA   M  13 186 ? -4.819  -142.174 64.998  1.00 102.01 ? 173 ALA   M CB  1 
ATOM   22630 N  N   . GLU   M  13 187 ? -3.059  -143.351 67.250  1.00 99.20  ? 174 GLU   M N   1 
ATOM   22631 C  CA  . GLU   M  13 187 ? -1.782  -143.435 68.009  1.00 100.63 ? 174 GLU   M CA  1 
ATOM   22632 C  C   . GLU   M  13 187 ? -1.410  -144.904 68.237  1.00 102.97 ? 174 GLU   M C   1 
ATOM   22633 O  O   . GLU   M  13 187 ? -0.207  -145.227 68.155  1.00 98.11  ? 174 GLU   M O   1 
ATOM   22634 C  CB  . GLU   M  13 187 ? -1.892  -142.711 69.349  1.00 101.72 ? 174 GLU   M CB  1 
ATOM   22635 C  CG  . GLU   M  13 187 ? -0.563  -142.602 70.071  1.00 104.55 ? 174 GLU   M CG  1 
ATOM   22636 C  CD  . GLU   M  13 187 ? -0.639  -141.923 71.423  1.00 108.89 ? 174 GLU   M CD  1 
ATOM   22637 O  OE1 . GLU   M  13 187 ? 0.420   -141.772 72.061  1.00 115.78 ? 174 GLU   M OE1 1 
ATOM   22638 O  OE2 . GLU   M  13 187 ? -1.755  -141.543 71.832  1.00 111.52 ? 174 GLU   M OE2 1 
ATOM   22639 N  N   . GLU   M  13 188 ? -2.407  -145.747 68.524  1.00 106.44 ? 175 GLU   M N   1 
ATOM   22640 C  CA  . GLU   M  13 188 ? -2.238  -147.212 68.718  1.00 108.47 ? 175 GLU   M CA  1 
ATOM   22641 C  C   . GLU   M  13 188 ? -1.608  -147.806 67.454  1.00 105.43 ? 175 GLU   M C   1 
ATOM   22642 O  O   . GLU   M  13 188 ? -0.635  -148.575 67.587  1.00 103.83 ? 175 GLU   M O   1 
ATOM   22643 C  CB  . GLU   M  13 188 ? -3.583  -147.874 69.030  1.00 115.51 ? 175 GLU   M CB  1 
ATOM   22644 C  CG  . GLU   M  13 188 ? -3.454  -149.191 69.772  1.00 120.76 ? 175 GLU   M CG  1 
ATOM   22645 C  CD  . GLU   M  13 188 ? -4.727  -149.656 70.457  1.00 129.01 ? 175 GLU   M CD  1 
ATOM   22646 O  OE1 . GLU   M  13 188 ? -5.377  -148.823 71.124  1.00 133.69 ? 175 GLU   M OE1 1 
ATOM   22647 O  OE2 . GLU   M  13 188 ? -5.067  -150.849 70.322  1.00 134.74 ? 175 GLU   M OE2 1 
ATOM   22648 N  N   . ALA   M  13 189 ? -2.136  -147.433 66.281  1.00 100.52 ? 176 ALA   M N   1 
ATOM   22649 C  CA  . ALA   M  13 189 ? -1.705  -147.918 64.948  1.00 99.34  ? 176 ALA   M CA  1 
ATOM   22650 C  C   . ALA   M  13 189 ? -0.280  -147.439 64.646  1.00 101.72 ? 176 ALA   M C   1 
ATOM   22651 O  O   . ALA   M  13 189 ? 0.493   -148.226 64.067  1.00 105.71 ? 176 ALA   M O   1 
ATOM   22652 C  CB  . ALA   M  13 189 ? -2.677  -147.462 63.887  1.00 96.20  ? 176 ALA   M CB  1 
ATOM   22653 N  N   . ILE   M  13 190 ? 0.053   -146.200 65.015  1.00 99.06  ? 177 ILE   M N   1 
ATOM   22654 C  CA  . ILE   M  13 190 ? 1.424   -145.627 64.855  1.00 99.96  ? 177 ILE   M CA  1 
ATOM   22655 C  C   . ILE   M  13 190 ? 2.392   -146.414 65.747  1.00 102.40 ? 177 ILE   M C   1 
ATOM   22656 O  O   . ILE   M  13 190 ? 3.424   -146.875 65.224  1.00 105.94 ? 177 ILE   M O   1 
ATOM   22657 C  CB  . ILE   M  13 190 ? 1.447   -144.115 65.168  1.00 100.09 ? 177 ILE   M CB  1 
ATOM   22658 C  CG1 . ILE   M  13 190 ? 0.695   -143.299 64.112  1.00 99.15  ? 177 ILE   M CG1 1 
ATOM   22659 C  CG2 . ILE   M  13 190 ? 2.875   -143.620 65.348  1.00 98.88  ? 177 ILE   M CG2 1 
ATOM   22660 C  CD1 . ILE   M  13 190 ? 1.360   -143.266 62.748  1.00 97.51  ? 177 ILE   M CD1 1 
ATOM   22661 N  N   . VAL   M  13 191 ? 2.064   -146.564 67.035  1.00 102.38 ? 178 VAL   M N   1 
ATOM   22662 C  CA  . VAL   M  13 191 ? 2.935   -147.219 68.060  1.00 100.80 ? 178 VAL   M CA  1 
ATOM   22663 C  C   . VAL   M  13 191 ? 3.171   -148.689 67.677  1.00 100.69 ? 178 VAL   M C   1 
ATOM   22664 O  O   . VAL   M  13 191 ? 4.283   -149.189 67.943  1.00 99.72  ? 178 VAL   M O   1 
ATOM   22665 C  CB  . VAL   M  13 191 ? 2.342   -147.080 69.477  1.00 100.98 ? 178 VAL   M CB  1 
ATOM   22666 C  CG1 . VAL   M  13 191 ? 3.013   -148.011 70.476  1.00 100.46 ? 178 VAL   M CG1 1 
ATOM   22667 C  CG2 . VAL   M  13 191 ? 2.414   -145.643 69.968  1.00 100.55 ? 178 VAL   M CG2 1 
ATOM   22668 N  N   . ASN   M  13 192 ? 2.172   -149.353 67.084  1.00 102.08 ? 179 ASN   M N   1 
ATOM   22669 C  CA  . ASN   M  13 192 ? 2.279   -150.755 66.597  1.00 103.50 ? 179 ASN   M CA  1 
ATOM   22670 C  C   . ASN   M  13 192 ? 3.261   -150.808 65.419  1.00 101.13 ? 179 ASN   M C   1 
ATOM   22671 O  O   . ASN   M  13 192 ? 4.135   -151.696 65.421  1.00 99.59  ? 179 ASN   M O   1 
ATOM   22672 C  CB  . ASN   M  13 192 ? 0.920   -151.335 66.197  1.00 108.11 ? 179 ASN   M CB  1 
ATOM   22673 C  CG  . ASN   M  13 192 ? 1.035   -152.683 65.516  1.00 110.40 ? 179 ASN   M CG  1 
ATOM   22674 O  OD1 . ASN   M  13 192 ? 0.689   -152.822 64.345  1.00 116.65 ? 179 ASN   M OD1 1 
ATOM   22675 N  ND2 . ASN   M  13 192 ? 1.543   -153.674 66.230  1.00 112.13 ? 179 ASN   M ND2 1 
ATOM   22676 N  N   . ALA   M  13 193 ? 3.110   -149.899 64.451  1.00 98.94  ? 180 ALA   M N   1 
ATOM   22677 C  CA  . ALA   M  13 193 ? 3.964   -149.789 63.244  1.00 96.81  ? 180 ALA   M CA  1 
ATOM   22678 C  C   . ALA   M  13 193 ? 5.425   -149.578 63.659  1.00 95.76  ? 180 ALA   M C   1 
ATOM   22679 O  O   . ALA   M  13 193 ? 6.310   -150.163 63.006  1.00 92.70  ? 180 ALA   M O   1 
ATOM   22680 C  CB  . ALA   M  13 193 ? 3.477   -148.668 62.358  1.00 96.18  ? 180 ALA   M CB  1 
ATOM   22681 N  N   . MET   M  13 194 ? 5.661   -148.776 64.703  1.00 97.86  ? 181 MET   M N   1 
ATOM   22682 C  CA  . MET   M  13 194 ? 7.016   -148.483 65.244  1.00 99.33  ? 181 MET   M CA  1 
ATOM   22683 C  C   . MET   M  13 194 ? 7.648   -149.773 65.782  1.00 97.81  ? 181 MET   M C   1 
ATOM   22684 O  O   . MET   M  13 194 ? 8.861   -149.959 65.566  1.00 96.88  ? 181 MET   M O   1 
ATOM   22685 C  CB  . MET   M  13 194 ? 6.965   -147.433 66.360  1.00 103.51 ? 181 MET   M CB  1 
ATOM   22686 C  CG  . MET   M  13 194 ? 6.650   -146.029 65.868  1.00 104.95 ? 181 MET   M CG  1 
ATOM   22687 S  SD  . MET   M  13 194 ? 7.771   -145.458 64.557  1.00 103.94 ? 181 MET   M SD  1 
ATOM   22688 C  CE  . MET   M  13 194 ? 9.324   -145.387 65.446  1.00 110.96 ? 181 MET   M CE  1 
ATOM   22689 N  N   . ARG   M  13 195 ? 6.859   -150.624 66.448  1.00 98.50  ? 182 ARG   M N   1 
ATOM   22690 C  CA  . ARG   M  13 195 ? 7.319   -151.939 66.976  1.00 98.23  ? 182 ARG   M CA  1 
ATOM   22691 C  C   . ARG   M  13 195 ? 7.726   -152.839 65.801  1.00 95.67  ? 182 ARG   M C   1 
ATOM   22692 O  O   . ARG   M  13 195 ? 8.824   -153.427 65.868  1.00 92.12  ? 182 ARG   M O   1 
ATOM   22693 C  CB  . ARG   M  13 195 ? 6.244   -152.618 67.836  1.00 100.50 ? 182 ARG   M CB  1 
ATOM   22694 C  CG  . ARG   M  13 195 ? 6.557   -154.071 68.165  1.00 99.69  ? 182 ARG   M CG  1 
ATOM   22695 C  CD  . ARG   M  13 195 ? 5.738   -154.636 69.308  1.00 102.90 ? 182 ARG   M CD  1 
ATOM   22696 N  NE  . ARG   M  13 195 ? 4.298   -154.553 69.086  1.00 106.86 ? 182 ARG   M NE  1 
ATOM   22697 C  CZ  . ARG   M  13 195 ? 3.447   -153.782 69.767  1.00 108.51 ? 182 ARG   M CZ  1 
ATOM   22698 N  NH1 . ARG   M  13 195 ? 2.158   -153.808 69.473  1.00 110.19 ? 182 ARG   M NH1 1 
ATOM   22699 N  NH2 . ARG   M  13 195 ? 3.870   -152.990 70.739  1.00 111.17 ? 182 ARG   M NH2 1 
ATOM   22700 N  N   . VAL   M  13 196 ? 6.876   -152.930 64.771  1.00 93.32  ? 183 VAL   M N   1 
ATOM   22701 C  CA  . VAL   M  13 196 ? 7.088   -153.789 63.565  1.00 90.54  ? 183 VAL   M CA  1 
ATOM   22702 C  C   . VAL   M  13 196 ? 8.392   -153.374 62.874  1.00 90.15  ? 183 VAL   M C   1 
ATOM   22703 O  O   . VAL   M  13 196 ? 9.131   -154.267 62.431  1.00 88.68  ? 183 VAL   M O   1 
ATOM   22704 C  CB  . VAL   M  13 196 ? 5.900   -153.715 62.587  1.00 89.95  ? 183 VAL   M CB  1 
ATOM   22705 C  CG1 . VAL   M  13 196 ? 6.219   -154.387 61.259  1.00 89.41  ? 183 VAL   M CG1 1 
ATOM   22706 C  CG2 . VAL   M  13 196 ? 4.636   -154.307 63.191  1.00 91.20  ? 183 VAL   M CG2 1 
ATOM   22707 N  N   . LEU   M  13 197 ? 8.648   -152.069 62.765  1.00 90.63  ? 184 LEU   M N   1 
ATOM   22708 C  CA  . LEU   M  13 197 ? 9.895   -151.526 62.163  1.00 89.13  ? 184 LEU   M CA  1 
ATOM   22709 C  C   . LEU   M  13 197 ? 11.103  -151.978 62.994  1.00 85.13  ? 184 LEU   M C   1 
ATOM   22710 O  O   . LEU   M  13 197 ? 12.146  -152.274 62.384  1.00 79.84  ? 184 LEU   M O   1 
ATOM   22711 C  CB  . LEU   M  13 197 ? 9.809   -149.997 62.081  1.00 90.16  ? 184 LEU   M CB  1 
ATOM   22712 C  CG  . LEU   M  13 197 ? 8.835   -149.436 61.044  1.00 90.05  ? 184 LEU   M CG  1 
ATOM   22713 C  CD1 . LEU   M  13 197 ? 8.810   -147.920 61.101  1.00 91.51  ? 184 LEU   M CD1 1 
ATOM   22714 C  CD2 . LEU   M  13 197 ? 9.186   -149.901 59.639  1.00 90.03  ? 184 LEU   M CD2 1 
ATOM   22715 N  N   . TYR   M  13 198 ? 10.973  -152.045 64.324  1.00 86.56  ? 185 TYR   M N   1 
ATOM   22716 C  CA  . TYR   M  13 198 ? 12.081  -152.431 65.239  1.00 88.83  ? 185 TYR   M CA  1 
ATOM   22717 C  C   . TYR   M  13 198 ? 12.415  -153.914 65.050  1.00 89.91  ? 185 TYR   M C   1 
ATOM   22718 O  O   . TYR   M  13 198 ? 13.607  -154.263 65.154  1.00 89.18  ? 185 TYR   M O   1 
ATOM   22719 C  CB  . TYR   M  13 198 ? 11.759  -152.119 66.703  1.00 90.67  ? 185 TYR   M CB  1 
ATOM   22720 C  CG  . TYR   M  13 198 ? 12.912  -152.393 67.637  1.00 91.87  ? 185 TYR   M CG  1 
ATOM   22721 C  CD1 . TYR   M  13 198 ? 14.130  -151.753 67.469  1.00 91.91  ? 185 TYR   M CD1 1 
ATOM   22722 C  CD2 . TYR   M  13 198 ? 12.800  -153.310 68.669  1.00 93.07  ? 185 TYR   M CD2 1 
ATOM   22723 C  CE1 . TYR   M  13 198 ? 15.202  -152.005 68.309  1.00 92.42  ? 185 TYR   M CE1 1 
ATOM   22724 C  CE2 . TYR   M  13 198 ? 13.863  -153.573 69.519  1.00 95.46  ? 185 TYR   M CE2 1 
ATOM   22725 C  CZ  . TYR   M  13 198 ? 15.068  -152.915 69.340  1.00 94.31  ? 185 TYR   M CZ  1 
ATOM   22726 O  OH  . TYR   M  13 198 ? 16.120  -153.162 70.173  1.00 98.32  ? 185 TYR   M OH  1 
ATOM   22727 N  N   . TYR   M  13 199 ? 11.405  -154.748 64.783  1.00 92.88  ? 186 TYR   M N   1 
ATOM   22728 C  CA  . TYR   M  13 199 ? 11.563  -156.199 64.497  1.00 95.44  ? 186 TYR   M CA  1 
ATOM   22729 C  C   . TYR   M  13 199 ? 12.381  -156.402 63.215  1.00 96.06  ? 186 TYR   M C   1 
ATOM   22730 O  O   . TYR   M  13 199 ? 13.184  -157.356 63.185  1.00 98.02  ? 186 TYR   M O   1 
ATOM   22731 C  CB  . TYR   M  13 199 ? 10.217  -156.903 64.291  1.00 93.01  ? 186 TYR   M CB  1 
ATOM   22732 C  CG  . TYR   M  13 199 ? 9.369   -157.160 65.514  1.00 94.97  ? 186 TYR   M CG  1 
ATOM   22733 C  CD1 . TYR   M  13 199 ? 9.923   -157.507 66.738  1.00 96.98  ? 186 TYR   M CD1 1 
ATOM   22734 C  CD2 . TYR   M  13 199 ? 7.986   -157.126 65.419  1.00 95.74  ? 186 TYR   M CD2 1 
ATOM   22735 C  CE1 . TYR   M  13 199 ? 9.126   -157.769 67.842  1.00 100.30 ? 186 TYR   M CE1 1 
ATOM   22736 C  CE2 . TYR   M  13 199 ? 7.176   -157.386 66.512  1.00 99.29  ? 186 TYR   M CE2 1 
ATOM   22737 C  CZ  . TYR   M  13 199 ? 7.748   -157.711 67.728  1.00 101.21 ? 186 TYR   M CZ  1 
ATOM   22738 O  OH  . TYR   M  13 199 ? 6.947   -157.969 68.802  1.00 103.35 ? 186 TYR   M OH  1 
ATOM   22739 N  N   . ARG   M  13 200 ? 12.173  -155.548 62.200  1.00 96.72  ? 187 ARG   M N   1 
ATOM   22740 C  CA  . ARG   M  13 200 ? 12.425  -155.873 60.766  1.00 95.62  ? 187 ARG   M CA  1 
ATOM   22741 C  C   . ARG   M  13 200 ? 13.397  -154.898 60.075  1.00 94.48  ? 187 ARG   M C   1 
ATOM   22742 O  O   . ARG   M  13 200 ? 14.011  -155.325 59.077  1.00 94.34  ? 187 ARG   M O   1 
ATOM   22743 C  CB  . ARG   M  13 200 ? 11.086  -155.931 60.023  1.00 96.66  ? 187 ARG   M CB  1 
ATOM   22744 C  CG  . ARG   M  13 200 ? 10.760  -157.300 59.442  1.00 97.14  ? 187 ARG   M CG  1 
ATOM   22745 C  CD  . ARG   M  13 200 ? 10.636  -158.437 60.444  1.00 97.42  ? 187 ARG   M CD  1 
ATOM   22746 N  NE  . ARG   M  13 200 ? 11.280  -159.647 59.935  1.00 96.52  ? 187 ARG   M NE  1 
ATOM   22747 C  CZ  . ARG   M  13 200 ? 10.931  -160.901 60.223  1.00 97.25  ? 187 ARG   M CZ  1 
ATOM   22748 N  NH1 . ARG   M  13 200 ? 9.911   -161.162 61.024  1.00 95.65  ? 187 ARG   M NH1 1 
ATOM   22749 N  NH2 . ARG   M  13 200 ? 11.609  -161.903 59.690  1.00 97.79  ? 187 ARG   M NH2 1 
ATOM   22750 N  N   . ASP   M  13 201 ? 13.521  -153.647 60.536  1.00 92.65  ? 188 ASP   M N   1 
ATOM   22751 C  CA  . ASP   M  13 201 ? 14.493  -152.651 59.998  1.00 91.77  ? 188 ASP   M CA  1 
ATOM   22752 C  C   . ASP   M  13 201 ? 15.802  -152.755 60.788  1.00 88.26  ? 188 ASP   M C   1 
ATOM   22753 O  O   . ASP   M  13 201 ? 15.755  -152.573 62.016  1.00 90.08  ? 188 ASP   M O   1 
ATOM   22754 C  CB  . ASP   M  13 201 ? 13.929  -151.228 60.065  1.00 93.01  ? 188 ASP   M CB  1 
ATOM   22755 C  CG  . ASP   M  13 201 ? 14.830  -150.137 59.502  1.00 93.45  ? 188 ASP   M CG  1 
ATOM   22756 O  OD1 . ASP   M  13 201 ? 15.947  -150.460 59.044  1.00 101.73 ? 188 ASP   M OD1 1 
ATOM   22757 O  OD2 . ASP   M  13 201 ? 14.403  -148.963 59.532  1.00 92.71  ? 188 ASP   M OD2 1 
ATOM   22758 N  N   . ALA   M  13 202 ? 16.924  -153.002 60.101  1.00 87.74  ? 189 ALA   M N   1 
ATOM   22759 C  CA  . ALA   M  13 202 ? 18.257  -153.253 60.704  1.00 93.72  ? 189 ALA   M CA  1 
ATOM   22760 C  C   . ALA   M  13 202 ? 18.944  -151.938 61.104  1.00 93.91  ? 189 ALA   M C   1 
ATOM   22761 O  O   . ALA   M  13 202 ? 20.023  -152.010 61.732  1.00 94.96  ? 189 ALA   M O   1 
ATOM   22762 C  CB  . ALA   M  13 202 ? 19.117  -154.047 59.749  1.00 95.38  ? 189 ALA   M CB  1 
ATOM   22763 N  N   . ARG   M  13 203 ? 18.363  -150.785 60.750  1.00 93.29  ? 190 ARG   M N   1 
ATOM   22764 C  CA  . ARG   M  13 203 ? 18.861  -149.440 61.151  1.00 93.92  ? 190 ARG   M CA  1 
ATOM   22765 C  C   . ARG   M  13 203 ? 17.772  -148.687 61.926  1.00 89.65  ? 190 ARG   M C   1 
ATOM   22766 O  O   . ARG   M  13 203 ? 17.703  -147.454 61.792  1.00 87.38  ? 190 ARG   M O   1 
ATOM   22767 C  CB  . ARG   M  13 203 ? 19.306  -148.645 59.920  1.00 93.67  ? 190 ARG   M CB  1 
ATOM   22768 C  CG  . ARG   M  13 203 ? 20.714  -148.966 59.441  1.00 100.23 ? 190 ARG   M CG  1 
ATOM   22769 C  CD  . ARG   M  13 203 ? 20.715  -150.100 58.436  1.00 104.00 ? 190 ARG   M CD  1 
ATOM   22770 N  NE  . ARG   M  13 203 ? 22.049  -150.430 57.943  1.00 110.85 ? 190 ARG   M NE  1 
ATOM   22771 C  CZ  . ARG   M  13 203 ? 22.682  -151.592 58.120  1.00 112.76 ? 190 ARG   M CZ  1 
ATOM   22772 N  NH1 . ARG   M  13 203 ? 22.117  -152.583 58.790  1.00 111.94 ? 190 ARG   M NH1 1 
ATOM   22773 N  NH2 . ARG   M  13 203 ? 23.891  -151.760 57.611  1.00 113.64 ? 190 ARG   M NH2 1 
ATOM   22774 N  N   . SER   M  13 204 ? 16.961  -149.395 62.716  1.00 92.32  ? 191 SER   M N   1 
ATOM   22775 C  CA  . SER   M  13 204 ? 15.945  -148.807 63.629  1.00 94.07  ? 191 SER   M CA  1 
ATOM   22776 C  C   . SER   M  13 204 ? 16.419  -148.966 65.075  1.00 92.45  ? 191 SER   M C   1 
ATOM   22777 O  O   . SER   M  13 204 ? 17.099  -149.967 65.364  1.00 95.71  ? 191 SER   M O   1 
ATOM   22778 C  CB  . SER   M  13 204 ? 14.596  -149.441 63.425  1.00 99.46  ? 191 SER   M CB  1 
ATOM   22779 O  OG  . SER   M  13 204 ? 14.664  -150.847 63.613  1.00 102.59 ? 191 SER   M OG  1 
ATOM   22780 N  N   . SER   M  13 205 ? 16.092  -148.007 65.942  1.00 96.19  ? 192 SER   M N   1 
ATOM   22781 C  CA  . SER   M  13 205 ? 16.314  -148.097 67.408  1.00 97.19  ? 192 SER   M CA  1 
ATOM   22782 C  C   . SER   M  13 205 ? 14.971  -148.305 68.109  1.00 96.71  ? 192 SER   M C   1 
ATOM   22783 O  O   . SER   M  13 205 ? 13.912  -148.074 67.480  1.00 95.70  ? 192 SER   M O   1 
ATOM   22784 C  CB  . SER   M  13 205 ? 17.038  -146.891 67.952  1.00 99.06  ? 192 SER   M CB  1 
ATOM   22785 O  OG  . SER   M  13 205 ? 16.129  -145.848 68.279  1.00 101.33 ? 192 SER   M OG  1 
ATOM   22786 N  N   . ARG   M  13 206 ? 15.035  -148.731 69.370  1.00 100.10 ? 193 ARG   M N   1 
ATOM   22787 C  CA  . ARG   M  13 206 ? 13.856  -149.029 70.220  1.00 105.32 ? 193 ARG   M CA  1 
ATOM   22788 C  C   . ARG   M  13 206 ? 13.231  -147.719 70.707  1.00 105.18 ? 193 ARG   M C   1 
ATOM   22789 O  O   . ARG   M  13 206 ? 12.004  -147.697 70.921  1.00 105.08 ? 193 ARG   M O   1 
ATOM   22790 C  CB  . ARG   M  13 206 ? 14.274  -149.894 71.409  1.00 110.16 ? 193 ARG   M CB  1 
ATOM   22791 C  CG  . ARG   M  13 206 ? 13.100  -150.548 72.119  1.00 114.96 ? 193 ARG   M CG  1 
ATOM   22792 C  CD  . ARG   M  13 206 ? 13.536  -151.529 73.187  1.00 120.00 ? 193 ARG   M CD  1 
ATOM   22793 N  NE  . ARG   M  13 206 ? 12.387  -152.122 73.857  1.00 124.67 ? 193 ARG   M NE  1 
ATOM   22794 C  CZ  . ARG   M  13 206 ? 12.449  -153.083 74.773  1.00 129.54 ? 193 ARG   M CZ  1 
ATOM   22795 N  NH1 . ARG   M  13 206 ? 13.617  -153.578 75.149  1.00 135.93 ? 193 ARG   M NH1 1 
ATOM   22796 N  NH2 . ARG   M  13 206 ? 11.336  -153.549 75.311  1.00 136.08 ? 193 ARG   M NH2 1 
ATOM   22797 N  N   . ASN   M  13 207 ? 14.060  -146.687 70.891  1.00 106.26 ? 194 ASN   M N   1 
ATOM   22798 C  CA  . ASN   M  13 207 ? 13.656  -145.350 71.402  1.00 104.72 ? 194 ASN   M CA  1 
ATOM   22799 C  C   . ASN   M  13 207 ? 13.172  -144.495 70.231  1.00 101.24 ? 194 ASN   M C   1 
ATOM   22800 O  O   . ASN   M  13 207 ? 13.824  -144.535 69.170  1.00 105.17 ? 194 ASN   M O   1 
ATOM   22801 C  CB  . ASN   M  13 207 ? 14.808  -144.682 72.150  1.00 108.28 ? 194 ASN   M CB  1 
ATOM   22802 C  CG  . ASN   M  13 207 ? 15.185  -145.452 73.396  1.00 109.78 ? 194 ASN   M CG  1 
ATOM   22803 O  OD1 . ASN   M  13 207 ? 16.199  -146.144 73.422  1.00 108.23 ? 194 ASN   M OD1 1 
ATOM   22804 N  ND2 . ASN   M  13 207 ? 14.348  -145.369 74.417  1.00 115.10 ? 194 ASN   M ND2 1 
ATOM   22805 N  N   . PHE   M  13 208 ? 12.073  -143.757 70.417  1.00 99.06  ? 195 PHE   M N   1 
ATOM   22806 C  CA  . PHE   M  13 208 ? 11.493  -142.865 69.379  1.00 97.32  ? 195 PHE   M CA  1 
ATOM   22807 C  C   . PHE   M  13 208 ? 10.712  -141.713 70.015  1.00 98.34  ? 195 PHE   M C   1 
ATOM   22808 O  O   . PHE   M  13 208 ? 10.381  -141.770 71.216  1.00 99.63  ? 195 PHE   M O   1 
ATOM   22809 C  CB  . PHE   M  13 208 ? 10.597  -143.656 68.422  1.00 92.48  ? 195 PHE   M CB  1 
ATOM   22810 C  CG  . PHE   M  13 208 ? 9.333   -144.212 69.028  1.00 92.55  ? 195 PHE   M CG  1 
ATOM   22811 C  CD1 . PHE   M  13 208 ? 9.358   -145.387 69.763  1.00 92.87  ? 195 PHE   M CD1 1 
ATOM   22812 C  CD2 . PHE   M  13 208 ? 8.115   -143.576 68.841  1.00 90.89  ? 195 PHE   M CD2 1 
ATOM   22813 C  CE1 . PHE   M  13 208 ? 8.195   -145.906 70.310  1.00 92.41  ? 195 PHE   M CE1 1 
ATOM   22814 C  CE2 . PHE   M  13 208 ? 6.952   -144.096 69.389  1.00 91.24  ? 195 PHE   M CE2 1 
ATOM   22815 C  CZ  . PHE   M  13 208 ? 6.995   -145.260 70.121  1.00 91.08  ? 195 PHE   M CZ  1 
ATOM   22816 N  N   . SER   M  13 209 ? 10.445  -140.690 69.198  1.00 100.31 ? 196 SER   M N   1 
ATOM   22817 C  CA  . SER   M  13 209 ? 9.577   -139.528 69.510  1.00 98.90  ? 196 SER   M CA  1 
ATOM   22818 C  C   . SER   M  13 209 ? 8.287   -139.631 68.690  1.00 97.19  ? 196 SER   M C   1 
ATOM   22819 O  O   . SER   M  13 209 ? 8.337   -140.162 67.562  1.00 93.27  ? 196 SER   M O   1 
ATOM   22820 C  CB  . SER   M  13 209 ? 10.301  -138.233 69.253  1.00 102.09 ? 196 SER   M CB  1 
ATOM   22821 O  OG  . SER   M  13 209 ? 11.387  -138.082 70.154  1.00 100.87 ? 196 SER   M OG  1 
ATOM   22822 N  N   . LEU   M  13 210 ? 7.176   -139.162 69.258  1.00 95.57  ? 197 LEU   M N   1 
ATOM   22823 C  CA  . LEU   M  13 210 ? 5.845   -139.110 68.601  1.00 97.95  ? 197 LEU   M CA  1 
ATOM   22824 C  C   . LEU   M  13 210 ? 5.231   -137.737 68.880  1.00 96.43  ? 197 LEU   M C   1 
ATOM   22825 O  O   . LEU   M  13 210 ? 5.339   -137.270 70.029  1.00 96.89  ? 197 LEU   M O   1 
ATOM   22826 C  CB  . LEU   M  13 210 ? 4.975   -140.244 69.151  1.00 99.18  ? 197 LEU   M CB  1 
ATOM   22827 C  CG  . LEU   M  13 210 ? 3.562   -140.350 68.574  1.00 101.76 ? 197 LEU   M CG  1 
ATOM   22828 C  CD1 . LEU   M  13 210 ? 3.110   -141.800 68.519  1.00 103.18 ? 197 LEU   M CD1 1 
ATOM   22829 C  CD2 . LEU   M  13 210 ? 2.566   -139.522 69.377  1.00 103.86 ? 197 LEU   M CD2 1 
ATOM   22830 N  N   . ALA   M  13 211 ? 4.619   -137.120 67.867  1.00 96.42  ? 198 ALA   M N   1 
ATOM   22831 C  CA  . ALA   M  13 211 ? 3.950   -135.805 67.975  1.00 97.84  ? 198 ALA   M CA  1 
ATOM   22832 C  C   . ALA   M  13 211 ? 2.512   -135.913 67.459  1.00 97.45  ? 198 ALA   M C   1 
ATOM   22833 O  O   . ALA   M  13 211 ? 2.300   -136.557 66.411  1.00 93.00  ? 198 ALA   M O   1 
ATOM   22834 C  CB  . ALA   M  13 211 ? 4.737   -134.757 67.226  1.00 98.50  ? 198 ALA   M CB  1 
ATOM   22835 N  N   . ILE   M  13 212 ? 1.573   -135.314 68.197  1.00 99.05  ? 199 ILE   M N   1 
ATOM   22836 C  CA  . ILE   M  13 212 ? 0.142   -135.143 67.811  1.00 99.97  ? 199 ILE   M CA  1 
ATOM   22837 C  C   . ILE   M  13 212 ? -0.118  -133.644 67.643  1.00 101.10 ? 199 ILE   M C   1 
ATOM   22838 O  O   . ILE   M  13 212 ? 0.154   -132.897 68.603  1.00 104.22 ? 199 ILE   M O   1 
ATOM   22839 C  CB  . ILE   M  13 212 ? -0.794  -135.747 68.876  1.00 101.78 ? 199 ILE   M CB  1 
ATOM   22840 C  CG1 . ILE   M  13 212 ? -0.427  -137.192 69.218  1.00 102.22 ? 199 ILE   M CG1 1 
ATOM   22841 C  CG2 . ILE   M  13 212 ? -2.251  -135.626 68.450  1.00 104.25 ? 199 ILE   M CG2 1 
ATOM   22842 C  CD1 . ILE   M  13 212 ? -0.826  -137.600 70.613  1.00 104.27 ? 199 ILE   M CD1 1 
ATOM   22843 N  N   . ILE   M  13 213 ? -0.622  -133.228 66.477  1.00 100.82 ? 200 ILE   M N   1 
ATOM   22844 C  CA  . ILE   M  13 213 ? -1.124  -131.844 66.230  1.00 101.59 ? 200 ILE   M CA  1 
ATOM   22845 C  C   . ILE   M  13 213 ? -2.645  -131.933 66.068  1.00 101.99 ? 200 ILE   M C   1 
ATOM   22846 O  O   . ILE   M  13 213 ? -3.103  -132.354 64.991  1.00 98.37  ? 200 ILE   M O   1 
ATOM   22847 C  CB  . ILE   M  13 213 ? -0.431  -131.183 65.019  1.00 97.32  ? 200 ILE   M CB  1 
ATOM   22848 C  CG1 . ILE   M  13 213 ? 1.095   -131.298 65.095  1.00 95.33  ? 200 ILE   M CG1 1 
ATOM   22849 C  CG2 . ILE   M  13 213 ? -0.868  -129.733 64.882  1.00 99.84  ? 200 ILE   M CG2 1 
ATOM   22850 C  CD1 . ILE   M  13 213 ? 1.674   -132.453 64.314  1.00 94.49  ? 200 ILE   M CD1 1 
ATOM   22851 N  N   . ASP   M  13 214 ? -3.381  -131.582 67.127  1.00 106.31 ? 201 ASP   M N   1 
ATOM   22852 C  CA  . ASP   M  13 214 ? -4.865  -131.635 67.197  1.00 110.69 ? 201 ASP   M CA  1 
ATOM   22853 C  C   . ASP   M  13 214 ? -5.416  -130.213 67.051  1.00 113.31 ? 201 ASP   M C   1 
ATOM   22854 O  O   . ASP   M  13 214 ? -4.786  -129.278 67.582  1.00 109.84 ? 201 ASP   M O   1 
ATOM   22855 C  CB  . ASP   M  13 214 ? -5.319  -132.280 68.508  1.00 116.15 ? 201 ASP   M CB  1 
ATOM   22856 C  CG  . ASP   M  13 214 ? -6.790  -132.659 68.535  1.00 120.39 ? 201 ASP   M CG  1 
ATOM   22857 O  OD1 . ASP   M  13 214 ? -7.632  -131.740 68.611  1.00 123.19 ? 201 ASP   M OD1 1 
ATOM   22858 O  OD2 . ASP   M  13 214 ? -7.082  -133.870 68.476  1.00 119.30 ? 201 ASP   M OD2 1 
ATOM   22859 N  N   . LYS   M  13 215 ? -6.560  -130.064 66.374  1.00 111.63 ? 202 LYS   M N   1 
ATOM   22860 C  CA  . LYS   M  13 215 ? -7.198  -128.748 66.100  1.00 111.37 ? 202 LYS   M CA  1 
ATOM   22861 C  C   . LYS   M  13 215 ? -7.840  -128.193 67.381  1.00 114.50 ? 202 LYS   M C   1 
ATOM   22862 O  O   . LYS   M  13 215 ? -8.172  -126.991 67.383  1.00 112.96 ? 202 LYS   M O   1 
ATOM   22863 C  CB  . LYS   M  13 215 ? -8.213  -128.858 64.955  1.00 107.24 ? 202 LYS   M CB  1 
ATOM   22864 C  CG  . LYS   M  13 215 ? -9.520  -129.570 65.274  1.00 105.74 ? 202 LYS   M CG  1 
ATOM   22865 C  CD  . LYS   M  13 215 ? -10.495 -129.513 64.121  1.00 108.02 ? 202 LYS   M CD  1 
ATOM   22866 C  CE  . LYS   M  13 215 ? -11.725 -130.367 64.336  1.00 114.06 ? 202 LYS   M CE  1 
ATOM   22867 N  NZ  . LYS   M  13 215 ? -12.649 -130.285 63.180  1.00 118.89 ? 202 LYS   M NZ  1 
ATOM   22868 N  N   . ASN   M  13 216 ? -8.005  -129.021 68.421  1.00 115.97 ? 203 ASN   M N   1 
ATOM   22869 C  CA  . ASN   M  13 216 ? -8.606  -128.622 69.723  1.00 118.36 ? 203 ASN   M CA  1 
ATOM   22870 C  C   . ASN   M  13 216 ? -7.516  -128.512 70.798  1.00 123.43 ? 203 ASN   M C   1 
ATOM   22871 O  O   . ASN   M  13 216 ? -7.403  -127.427 71.404  1.00 126.43 ? 203 ASN   M O   1 
ATOM   22872 C  CB  . ASN   M  13 216 ? -9.717  -129.584 70.146  1.00 120.85 ? 203 ASN   M CB  1 
ATOM   22873 C  CG  . ASN   M  13 216 ? -10.881 -129.586 69.176  1.00 122.08 ? 203 ASN   M CG  1 
ATOM   22874 O  OD1 . ASN   M  13 216 ? -11.376 -128.528 68.795  1.00 124.35 ? 203 ASN   M OD1 1 
ATOM   22875 N  ND2 . ASN   M  13 216 ? -11.326 -130.764 68.770  1.00 122.61 ? 203 ASN   M ND2 1 
ATOM   22876 N  N   . THR   M  13 217 ? -6.752  -129.586 71.034  1.00 122.51 ? 204 THR   M N   1 
ATOM   22877 C  CA  . THR   M  13 217 ? -5.761  -129.687 72.144  1.00 123.03 ? 204 THR   M CA  1 
ATOM   22878 C  C   . THR   M  13 217 ? -4.385  -129.153 71.719  1.00 117.02 ? 204 THR   M C   1 
ATOM   22879 O  O   . THR   M  13 217 ? -3.542  -128.966 72.617  1.00 117.10 ? 204 THR   M O   1 
ATOM   22880 C  CB  . THR   M  13 217 ? -5.660  -131.120 72.685  1.00 123.86 ? 204 THR   M CB  1 
ATOM   22881 O  OG1 . THR   M  13 217 ? -5.892  -132.043 71.620  1.00 124.53 ? 204 THR   M OG1 1 
ATOM   22882 C  CG2 . THR   M  13 217 ? -6.643  -131.382 73.804  1.00 126.06 ? 204 THR   M CG2 1 
ATOM   22883 N  N   . GLY   M  13 218 ? -4.157  -128.920 70.422  1.00 113.81 ? 205 GLY   M N   1 
ATOM   22884 C  CA  . GLY   M  13 218 ? -2.913  -128.314 69.905  1.00 110.28 ? 205 GLY   M CA  1 
ATOM   22885 C  C   . GLY   M  13 218 ? -1.795  -129.334 69.760  1.00 109.44 ? 205 GLY   M C   1 
ATOM   22886 O  O   . GLY   M  13 218 ? -2.104  -130.529 69.570  1.00 110.99 ? 205 GLY   M O   1 
ATOM   22887 N  N   . LEU   M  13 219 ? -0.540  -128.878 69.851  1.00 104.42 ? 206 LEU   M N   1 
ATOM   22888 C  CA  . LEU   M  13 219 ? 0.682   -129.706 69.651  1.00 103.52 ? 206 LEU   M CA  1 
ATOM   22889 C  C   . LEU   M  13 219 ? 1.046   -130.413 70.962  1.00 104.38 ? 206 LEU   M C   1 
ATOM   22890 O  O   . LEU   M  13 219 ? 1.338   -129.708 71.949  1.00 102.99 ? 206 LEU   M O   1 
ATOM   22891 C  CB  . LEU   M  13 219 ? 1.835   -128.815 69.171  1.00 102.74 ? 206 LEU   M CB  1 
ATOM   22892 C  CG  . LEU   M  13 219 ? 3.225   -129.454 69.186  1.00 101.36 ? 206 LEU   M CG  1 
ATOM   22893 C  CD1 . LEU   M  13 219 ? 3.284   -130.666 68.271  1.00 103.77 ? 206 LEU   M CD1 1 
ATOM   22894 C  CD2 . LEU   M  13 219 ? 4.293   -128.448 68.790  1.00 102.12 ? 206 LEU   M CD2 1 
ATOM   22895 N  N   . THR   M  13 220 ? 1.038   -131.751 70.954  1.00 103.88 ? 207 THR   M N   1 
ATOM   22896 C  CA  . THR   M  13 220 ? 1.551   -132.621 72.048  1.00 105.53 ? 207 THR   M CA  1 
ATOM   22897 C  C   . THR   M  13 220 ? 2.790   -133.369 71.547  1.00 104.02 ? 207 THR   M C   1 
ATOM   22898 O  O   . THR   M  13 220 ? 2.638   -134.225 70.656  1.00 105.46 ? 207 THR   M O   1 
ATOM   22899 C  CB  . THR   M  13 220 ? 0.496   -133.623 72.534  1.00 107.89 ? 207 THR   M CB  1 
ATOM   22900 O  OG1 . THR   M  13 220 ? -0.728  -132.922 72.751  1.00 112.06 ? 207 THR   M OG1 1 
ATOM   22901 C  CG2 . THR   M  13 220 ? 0.918   -134.331 73.803  1.00 108.60 ? 207 THR   M CG2 1 
ATOM   22902 N  N   . PHE   M  13 221 ? 3.963   -133.052 72.101  1.00 104.79 ? 208 PHE   M N   1 
ATOM   22903 C  CA  . PHE   M  13 221 ? 5.269   -133.659 71.739  1.00 104.56 ? 208 PHE   M CA  1 
ATOM   22904 C  C   . PHE   M  13 221 ? 5.678   -134.653 72.832  1.00 107.10 ? 208 PHE   M C   1 
ATOM   22905 O  O   . PHE   M  13 221 ? 5.837   -134.235 73.994  1.00 112.65 ? 208 PHE   M O   1 
ATOM   22906 C  CB  . PHE   M  13 221 ? 6.325   -132.570 71.543  1.00 102.86 ? 208 PHE   M CB  1 
ATOM   22907 C  CG  . PHE   M  13 221 ? 7.473   -132.982 70.660  1.00 101.08 ? 208 PHE   M CG  1 
ATOM   22908 C  CD1 . PHE   M  13 221 ? 8.571   -133.644 71.186  1.00 100.18 ? 208 PHE   M CD1 1 
ATOM   22909 C  CD2 . PHE   M  13 221 ? 7.448   -132.716 69.301  1.00 101.83 ? 208 PHE   M CD2 1 
ATOM   22910 C  CE1 . PHE   M  13 221 ? 9.625   -134.025 70.371  1.00 97.87  ? 208 PHE   M CE1 1 
ATOM   22911 C  CE2 . PHE   M  13 221 ? 8.504   -133.097 68.487  1.00 100.81 ? 208 PHE   M CE2 1 
ATOM   22912 C  CZ  . PHE   M  13 221 ? 9.589   -133.750 69.023  1.00 98.02  ? 208 PHE   M CZ  1 
ATOM   22913 N  N   . LYS   M  13 222 ? 5.833   -135.928 72.466  1.00 104.73 ? 209 LYS   M N   1 
ATOM   22914 C  CA  . LYS   M  13 222 ? 6.191   -137.037 73.393  1.00 105.21 ? 209 LYS   M CA  1 
ATOM   22915 C  C   . LYS   M  13 222 ? 7.605   -137.531 73.076  1.00 100.44 ? 209 LYS   M C   1 
ATOM   22916 O  O   . LYS   M  13 222 ? 7.816   -138.033 71.955  1.00 94.89  ? 209 LYS   M O   1 
ATOM   22917 C  CB  . LYS   M  13 222 ? 5.185   -138.182 73.267  1.00 107.05 ? 209 LYS   M CB  1 
ATOM   22918 C  CG  . LYS   M  13 222 ? 3.740   -137.806 73.562  1.00 111.64 ? 209 LYS   M CG  1 
ATOM   22919 C  CD  . LYS   M  13 222 ? 2.815   -138.999 73.584  1.00 113.42 ? 209 LYS   M CD  1 
ATOM   22920 C  CE  . LYS   M  13 222 ? 1.361   -138.619 73.754  1.00 116.56 ? 209 LYS   M CE  1 
ATOM   22921 N  NZ  . LYS   M  13 222 ? 0.515   -139.818 73.950  1.00 118.21 ? 209 LYS   M NZ  1 
ATOM   22922 N  N   . LYS   M  13 223 ? 8.524   -137.401 74.037  1.00 101.39 ? 210 LYS   M N   1 
ATOM   22923 C  CA  . LYS   M  13 223 ? 9.952   -137.796 73.907  1.00 104.41 ? 210 LYS   M CA  1 
ATOM   22924 C  C   . LYS   M  13 223 ? 10.214  -139.069 74.719  1.00 104.82 ? 210 LYS   M C   1 
ATOM   22925 O  O   . LYS   M  13 223 ? 9.453   -139.340 75.672  1.00 104.89 ? 210 LYS   M O   1 
ATOM   22926 C  CB  . LYS   M  13 223 ? 10.868  -136.669 74.393  1.00 105.18 ? 210 LYS   M CB  1 
ATOM   22927 C  CG  . LYS   M  13 223 ? 10.986  -135.474 73.458  1.00 108.21 ? 210 LYS   M CG  1 
ATOM   22928 C  CD  . LYS   M  13 223 ? 11.833  -134.352 74.026  1.00 110.66 ? 210 LYS   M CD  1 
ATOM   22929 C  CE  . LYS   M  13 223 ? 12.156  -133.274 73.013  1.00 110.94 ? 210 LYS   M CE  1 
ATOM   22930 N  NZ  . LYS   M  13 223 ? 13.218  -133.703 72.071  1.00 110.37 ? 210 LYS   M NZ  1 
ATOM   22931 N  N   . ASN   M  13 224 ? 11.261  -139.810 74.342  1.00 106.69 ? 211 ASN   M N   1 
ATOM   22932 C  CA  . ASN   M  13 224 ? 11.816  -140.971 75.091  1.00 110.16 ? 211 ASN   M CA  1 
ATOM   22933 C  C   . ASN   M  13 224 ? 10.780  -142.098 75.195  1.00 110.46 ? 211 ASN   M C   1 
ATOM   22934 O  O   . ASN   M  13 224 ? 10.790  -142.807 76.223  1.00 111.33 ? 211 ASN   M O   1 
ATOM   22935 C  CB  . ASN   M  13 224 ? 12.304  -140.558 76.482  1.00 113.04 ? 211 ASN   M CB  1 
ATOM   22936 C  CG  . ASN   M  13 224 ? 13.435  -139.555 76.438  1.00 115.38 ? 211 ASN   M CG  1 
ATOM   22937 O  OD1 . ASN   M  13 224 ? 13.272  -138.412 76.857  1.00 120.37 ? 211 ASN   M OD1 1 
ATOM   22938 N  ND2 . ASN   M  13 224 ? 14.583  -139.973 75.928  1.00 116.79 ? 211 ASN   M ND2 1 
ATOM   22939 N  N   . LEU   M  13 225 ? 9.930   -142.271 74.176  1.00 108.44 ? 212 LEU   M N   1 
ATOM   22940 C  CA  . LEU   M  13 225 ? 9.015   -143.441 74.058  1.00 106.37 ? 212 LEU   M CA  1 
ATOM   22941 C  C   . LEU   M  13 225 ? 9.858   -144.679 73.742  1.00 105.63 ? 212 LEU   M C   1 
ATOM   22942 O  O   . LEU   M  13 225 ? 10.910  -144.522 73.090  1.00 99.95  ? 212 LEU   M O   1 
ATOM   22943 C  CB  . LEU   M  13 225 ? 7.971   -143.197 72.960  1.00 103.57 ? 212 LEU   M CB  1 
ATOM   22944 C  CG  . LEU   M  13 225 ? 6.643   -142.575 73.396  1.00 102.27 ? 212 LEU   M CG  1 
ATOM   22945 C  CD1 . LEU   M  13 225 ? 6.832   -141.531 74.489  1.00 103.80 ? 212 LEU   M CD1 1 
ATOM   22946 C  CD2 . LEU   M  13 225 ? 5.928   -141.965 72.201  1.00 101.16 ? 212 LEU   M CD2 1 
ATOM   22947 N  N   . GLN   M  13 226 ? 9.413   -145.855 74.194  1.00 107.47 ? 213 GLN   M N   1 
ATOM   22948 C  CA  . GLN   M  13 226 ? 10.077  -147.157 73.920  1.00 107.33 ? 213 GLN   M CA  1 
ATOM   22949 C  C   . GLN   M  13 226 ? 9.081   -148.120 73.268  1.00 105.78 ? 213 GLN   M C   1 
ATOM   22950 O  O   . GLN   M  13 226 ? 7.882   -148.064 73.611  1.00 106.91 ? 213 GLN   M O   1 
ATOM   22951 C  CB  . GLN   M  13 226 ? 10.636  -147.773 75.204  1.00 108.82 ? 213 GLN   M CB  1 
ATOM   22952 C  CG  . GLN   M  13 226 ? 12.012  -147.243 75.586  1.00 110.86 ? 213 GLN   M CG  1 
ATOM   22953 C  CD  . GLN   M  13 226 ? 12.909  -148.273 76.232  1.00 112.86 ? 213 GLN   M CD  1 
ATOM   22954 O  OE1 . GLN   M  13 226 ? 14.130  -148.211 76.105  1.00 115.39 ? 213 GLN   M OE1 1 
ATOM   22955 N  NE2 . GLN   M  13 226 ? 12.321  -149.233 76.932  1.00 115.73 ? 213 GLN   M NE2 1 
ATOM   22956 N  N   . VAL   M  13 227 ? 9.577   -148.963 72.357  1.00 105.24 ? 214 VAL   M N   1 
ATOM   22957 C  CA  . VAL   M  13 227 ? 8.849   -150.147 71.814  1.00 108.02 ? 214 VAL   M CA  1 
ATOM   22958 C  C   . VAL   M  13 227 ? 8.737   -151.181 72.942  1.00 110.98 ? 214 VAL   M C   1 
ATOM   22959 O  O   . VAL   M  13 227 ? 9.766   -151.470 73.588  1.00 107.29 ? 214 VAL   M O   1 
ATOM   22960 C  CB  . VAL   M  13 227 ? 9.563   -150.725 70.576  1.00 107.76 ? 214 VAL   M CB  1 
ATOM   22961 C  CG1 . VAL   M  13 227 ? 8.987   -152.070 70.157  1.00 108.75 ? 214 VAL   M CG1 1 
ATOM   22962 C  CG2 . VAL   M  13 227 ? 9.547   -149.750 69.409  1.00 105.80 ? 214 VAL   M CG2 1 
ATOM   22963 N  N   . GLU   M  13 228 ? 7.533   -151.707 73.177  1.00 113.62 ? 215 GLU   M N   1 
ATOM   22964 C  CA  . GLU   M  13 228 ? 7.256   -152.690 74.257  1.00 117.44 ? 215 GLU   M CA  1 
ATOM   22965 C  C   . GLU   M  13 228 ? 6.116   -153.619 73.831  1.00 117.80 ? 215 GLU   M C   1 
ATOM   22966 O  O   . GLU   M  13 228 ? 5.536   -153.385 72.755  1.00 116.92 ? 215 GLU   M O   1 
ATOM   22967 C  CB  . GLU   M  13 228 ? 6.954   -151.950 75.562  1.00 125.51 ? 215 GLU   M CB  1 
ATOM   22968 C  CG  . GLU   M  13 228 ? 8.116   -151.969 76.542  1.00 131.89 ? 215 GLU   M CG  1 
ATOM   22969 C  CD  . GLU   M  13 228 ? 8.378   -150.667 77.279  1.00 138.06 ? 215 GLU   M CD  1 
ATOM   22970 O  OE1 . GLU   M  13 228 ? 7.447   -149.841 77.377  1.00 137.63 ? 215 GLU   M OE1 1 
ATOM   22971 O  OE2 . GLU   M  13 228 ? 9.520   -150.482 77.749  1.00 147.31 ? 215 GLU   M OE2 1 
ATOM   22972 N  N   . ASN   M  13 229 ? 5.829   -154.634 74.655  1.00 119.76 ? 216 ASN   M N   1 
ATOM   22973 C  CA  . ASN   M  13 229 ? 4.865   -155.732 74.371  1.00 120.02 ? 216 ASN   M CA  1 
ATOM   22974 C  C   . ASN   M  13 229 ? 5.335   -156.485 73.123  1.00 120.39 ? 216 ASN   M C   1 
ATOM   22975 O  O   . ASN   M  13 229 ? 4.504   -156.723 72.221  1.00 119.11 ? 216 ASN   M O   1 
ATOM   22976 C  CB  . ASN   M  13 229 ? 3.431   -155.215 74.222  1.00 122.63 ? 216 ASN   M CB  1 
ATOM   22977 C  CG  . ASN   M  13 229 ? 2.905   -154.560 75.482  1.00 124.33 ? 216 ASN   M CG  1 
ATOM   22978 O  OD1 . ASN   M  13 229 ? 3.318   -154.905 76.587  1.00 126.75 ? 216 ASN   M OD1 1 
ATOM   22979 N  ND2 . ASN   M  13 229 ? 1.986   -153.619 75.328  1.00 127.42 ? 216 ASN   M ND2 1 
ATOM   22980 N  N   . MET   M  13 230 ? 6.623   -156.843 73.085  1.00 117.58 ? 217 MET   M N   1 
ATOM   22981 C  CA  . MET   M  13 230 ? 7.265   -157.545 71.942  1.00 114.80 ? 217 MET   M CA  1 
ATOM   22982 C  C   . MET   M  13 230 ? 7.146   -159.059 72.145  1.00 115.31 ? 217 MET   M C   1 
ATOM   22983 O  O   . MET   M  13 230 ? 7.180   -159.503 73.309  1.00 109.29 ? 217 MET   M O   1 
ATOM   22984 C  CB  . MET   M  13 230 ? 8.743   -157.164 71.811  1.00 116.82 ? 217 MET   M CB  1 
ATOM   22985 C  CG  . MET   M  13 230 ? 8.954   -155.735 71.350  1.00 118.50 ? 217 MET   M CG  1 
ATOM   22986 S  SD  . MET   M  13 230 ? 10.663  -155.411 70.845  1.00 117.88 ? 217 MET   M SD  1 
ATOM   22987 C  CE  . MET   M  13 230 ? 11.524  -155.647 72.399  1.00 117.22 ? 217 MET   M CE  1 
ATOM   22988 N  N   . LYS   M  13 231 ? 7.002   -159.803 71.044  1.00 117.23 ? 218 LYS   M N   1 
ATOM   22989 C  CA  . LYS   M  13 231 ? 6.955   -161.289 71.019  1.00 119.52 ? 218 LYS   M CA  1 
ATOM   22990 C  C   . LYS   M  13 231 ? 8.340   -161.816 70.627  1.00 119.82 ? 218 LYS   M C   1 
ATOM   22991 O  O   . LYS   M  13 231 ? 8.753   -161.589 69.471  1.00 121.13 ? 218 LYS   M O   1 
ATOM   22992 C  CB  . LYS   M  13 231 ? 5.875   -161.778 70.050  1.00 120.94 ? 218 LYS   M CB  1 
ATOM   22993 C  CG  . LYS   M  13 231 ? 4.442   -161.565 70.522  1.00 125.09 ? 218 LYS   M CG  1 
ATOM   22994 C  CD  . LYS   M  13 231 ? 3.409   -162.259 69.656  1.00 127.09 ? 218 LYS   M CD  1 
ATOM   22995 C  CE  . LYS   M  13 231 ? 1.998   -162.138 70.194  1.00 129.10 ? 218 LYS   M CE  1 
ATOM   22996 N  NZ  . LYS   M  13 231 ? 1.499   -160.744 70.120  1.00 129.37 ? 218 LYS   M NZ  1 
ATOM   22997 N  N   . TRP   M  13 232 ? 9.034   -162.459 71.572  1.00 120.04 ? 219 TRP   M N   1 
ATOM   22998 C  CA  . TRP   M  13 232 ? 10.351  -163.122 71.367  1.00 115.99 ? 219 TRP   M CA  1 
ATOM   22999 C  C   . TRP   M  13 232 ? 10.331  -164.568 71.879  1.00 117.83 ? 219 TRP   M C   1 
ATOM   23000 O  O   . TRP   M  13 232 ? 11.234  -165.327 71.484  1.00 112.06 ? 219 TRP   M O   1 
ATOM   23001 C  CB  . TRP   M  13 232 ? 11.462  -162.320 72.052  1.00 115.06 ? 219 TRP   M CB  1 
ATOM   23002 C  CG  . TRP   M  13 232 ? 11.797  -161.044 71.347  1.00 110.73 ? 219 TRP   M CG  1 
ATOM   23003 C  CD1 . TRP   M  13 232 ? 11.426  -159.782 71.707  1.00 112.30 ? 219 TRP   M CD1 1 
ATOM   23004 C  CD2 . TRP   M  13 232 ? 12.569  -160.909 70.143  1.00 108.21 ? 219 TRP   M CD2 1 
ATOM   23005 N  NE1 . TRP   M  13 232 ? 11.919  -158.871 70.812  1.00 112.14 ? 219 TRP   M NE1 1 
ATOM   23006 C  CE2 . TRP   M  13 232 ? 12.625  -159.532 69.842  1.00 109.78 ? 219 TRP   M CE2 1 
ATOM   23007 C  CE3 . TRP   M  13 232 ? 13.219  -161.813 69.296  1.00 107.47 ? 219 TRP   M CE3 1 
ATOM   23008 C  CZ2 . TRP   M  13 232 ? 13.304  -159.041 68.728  1.00 107.87 ? 219 TRP   M CZ2 1 
ATOM   23009 C  CZ3 . TRP   M  13 232 ? 13.892  -161.326 68.197  1.00 107.68 ? 219 TRP   M CZ3 1 
ATOM   23010 C  CH2 . TRP   M  13 232 ? 13.930  -159.959 67.917  1.00 106.50 ? 219 TRP   M CH2 1 
ATOM   23011 N  N   . ASP   M  13 233 ? 9.354   -164.928 72.719  1.00 122.39 ? 220 ASP   M N   1 
ATOM   23012 C  CA  . ASP   M  13 233 ? 9.317   -166.210 73.473  1.00 125.23 ? 220 ASP   M CA  1 
ATOM   23013 C  C   . ASP   M  13 233 ? 9.436   -167.396 72.506  1.00 121.85 ? 220 ASP   M C   1 
ATOM   23014 O  O   . ASP   M  13 233 ? 10.201  -168.321 72.822  1.00 121.51 ? 220 ASP   M O   1 
ATOM   23015 C  CB  . ASP   M  13 233 ? 8.053   -166.312 74.330  1.00 132.41 ? 220 ASP   M CB  1 
ATOM   23016 C  CG  . ASP   M  13 233 ? 8.100   -167.443 75.341  1.00 136.28 ? 220 ASP   M CG  1 
ATOM   23017 O  OD1 . ASP   M  13 233 ? 8.998   -167.418 76.208  1.00 142.00 ? 220 ASP   M OD1 1 
ATOM   23018 O  OD2 . ASP   M  13 233 ? 7.254   -168.354 75.237  1.00 145.12 ? 220 ASP   M OD2 1 
ATOM   23019 N  N   . PHE   M  13 234 ? 8.732   -167.358 71.369  1.00 119.05 ? 221 PHE   M N   1 
ATOM   23020 C  CA  . PHE   M  13 234 ? 8.663   -168.453 70.358  1.00 115.57 ? 221 PHE   M CA  1 
ATOM   23021 C  C   . PHE   M  13 234 ? 10.056  -168.809 69.808  1.00 112.30 ? 221 PHE   M C   1 
ATOM   23022 O  O   . PHE   M  13 234 ? 10.181  -169.884 69.190  1.00 110.43 ? 221 PHE   M O   1 
ATOM   23023 C  CB  . PHE   M  13 234 ? 7.709   -168.082 69.217  1.00 114.06 ? 221 PHE   M CB  1 
ATOM   23024 C  CG  . PHE   M  13 234 ? 8.164   -166.944 68.337  1.00 110.23 ? 221 PHE   M CG  1 
ATOM   23025 C  CD1 . PHE   M  13 234 ? 7.831   -165.635 68.647  1.00 110.82 ? 221 PHE   M CD1 1 
ATOM   23026 C  CD2 . PHE   M  13 234 ? 8.911   -167.181 67.193  1.00 106.64 ? 221 PHE   M CD2 1 
ATOM   23027 C  CE1 . PHE   M  13 234 ? 8.247   -164.587 67.839  1.00 109.32 ? 221 PHE   M CE1 1 
ATOM   23028 C  CE2 . PHE   M  13 234 ? 9.326   -166.132 66.386  1.00 105.58 ? 221 PHE   M CE2 1 
ATOM   23029 C  CZ  . PHE   M  13 234 ? 8.992   -164.837 66.710  1.00 107.14 ? 221 PHE   M CZ  1 
ATOM   23030 N  N   . ALA   M  13 235 ? 11.058  -167.945 70.011  1.00 111.09 ? 222 ALA   M N   1 
ATOM   23031 C  CA  . ALA   M  13 235 ? 12.449  -168.105 69.516  1.00 106.80 ? 222 ALA   M CA  1 
ATOM   23032 C  C   . ALA   M  13 235 ? 13.095  -169.378 70.078  1.00 106.04 ? 222 ALA   M C   1 
ATOM   23033 O  O   . ALA   M  13 235 ? 13.868  -170.002 69.329  1.00 100.82 ? 222 ALA   M O   1 
ATOM   23034 C  CB  . ALA   M  13 235 ? 13.268  -166.889 69.874  1.00 108.13 ? 222 ALA   M CB  1 
ATOM   23035 N  N   . LYS   M  13 236 ? 12.814  -169.723 71.343  1.00 107.16 ? 223 LYS   M N   1 
ATOM   23036 C  CA  . LYS   M  13 236 ? 13.397  -170.893 72.069  1.00 109.91 ? 223 LYS   M CA  1 
ATOM   23037 C  C   . LYS   M  13 236 ? 13.101  -172.201 71.322  1.00 107.65 ? 223 LYS   M C   1 
ATOM   23038 O  O   . LYS   M  13 236 ? 13.959  -173.104 71.360  1.00 105.61 ? 223 LYS   M O   1 
ATOM   23039 C  CB  . LYS   M  13 236 ? 12.846  -171.003 73.496  1.00 112.70 ? 223 LYS   M CB  1 
ATOM   23040 C  CG  . LYS   M  13 236 ? 11.327  -170.992 73.605  1.00 115.41 ? 223 LYS   M CG  1 
ATOM   23041 C  CD  . LYS   M  13 236 ? 10.775  -171.451 74.939  1.00 118.72 ? 223 LYS   M CD  1 
ATOM   23042 C  CE  . LYS   M  13 236 ? 9.272   -171.283 75.066  1.00 122.45 ? 223 LYS   M CE  1 
ATOM   23043 N  NZ  . LYS   M  13 236 ? 8.729   -170.234 74.167  1.00 122.51 ? 223 LYS   M NZ  1 
ATOM   23044 N  N   . ASP   M  13 237 ? 11.930  -172.296 70.683  1.00 108.74 ? 224 ASP   M N   1 
ATOM   23045 C  CA  . ASP   M  13 237 ? 11.409  -173.533 70.042  1.00 109.20 ? 224 ASP   M CA  1 
ATOM   23046 C  C   . ASP   M  13 237 ? 12.047  -173.736 68.662  1.00 106.30 ? 224 ASP   M C   1 
ATOM   23047 O  O   . ASP   M  13 237 ? 11.902  -174.842 68.113  1.00 107.78 ? 224 ASP   M O   1 
ATOM   23048 C  CB  . ASP   M  13 237 ? 9.882   -173.489 69.941  1.00 112.49 ? 224 ASP   M CB  1 
ATOM   23049 C  CG  . ASP   M  13 237 ? 9.186   -173.392 71.287  1.00 117.41 ? 224 ASP   M CG  1 
ATOM   23050 O  OD1 . ASP   M  13 237 ? 8.253   -172.571 71.404  1.00 113.96 ? 224 ASP   M OD1 1 
ATOM   23051 O  OD2 . ASP   M  13 237 ? 9.579   -174.143 72.207  1.00 125.71 ? 224 ASP   M OD2 1 
ATOM   23052 N  N   . ILE   M  13 238 ? 12.719  -172.717 68.118  1.00 102.34 ? 225 ILE   M N   1 
ATOM   23053 C  CA  . ILE   M  13 238 ? 13.411  -172.783 66.796  1.00 102.62 ? 225 ILE   M CA  1 
ATOM   23054 C  C   . ILE   M  13 238 ? 14.837  -173.301 67.009  1.00 103.74 ? 225 ILE   M C   1 
ATOM   23055 O  O   . ILE   M  13 238 ? 15.623  -172.611 67.683  1.00 102.36 ? 225 ILE   M O   1 
ATOM   23056 C  CB  . ILE   M  13 238 ? 13.376  -171.414 66.085  1.00 101.85 ? 225 ILE   M CB  1 
ATOM   23057 C  CG1 . ILE   M  13 238 ? 11.989  -171.152 65.494  1.00 103.07 ? 225 ILE   M CG1 1 
ATOM   23058 C  CG2 . ILE   M  13 238 ? 14.466  -171.307 65.027  1.00 100.31 ? 225 ILE   M CG2 1 
ATOM   23059 C  CD1 . ILE   M  13 238 ? 11.721  -169.708 65.176  1.00 103.72 ? 225 ILE   M CD1 1 
ATOM   23060 N  N   . LYS   M  13 239 ? 15.141  -174.476 66.448  1.00 106.11 ? 226 LYS   M N   1 
ATOM   23061 C  CA  . LYS   M  13 239 ? 16.464  -175.149 66.544  1.00 110.48 ? 226 LYS   M CA  1 
ATOM   23062 C  C   . LYS   M  13 239 ? 16.938  -175.533 65.139  1.00 110.11 ? 226 LYS   M C   1 
ATOM   23063 O  O   . LYS   M  13 239 ? 16.147  -176.146 64.395  1.00 109.50 ? 226 LYS   M O   1 
ATOM   23064 C  CB  . LYS   M  13 239 ? 16.374  -176.400 67.424  1.00 115.14 ? 226 LYS   M CB  1 
ATOM   23065 C  CG  . LYS   M  13 239 ? 16.043  -176.153 68.891  1.00 119.78 ? 226 LYS   M CG  1 
ATOM   23066 C  CD  . LYS   M  13 239 ? 15.384  -177.342 69.562  1.00 124.03 ? 226 LYS   M CD  1 
ATOM   23067 C  CE  . LYS   M  13 239 ? 15.538  -177.353 71.069  1.00 128.96 ? 226 LYS   M CE  1 
ATOM   23068 N  NZ  . LYS   M  13 239 ? 15.151  -176.059 71.681  1.00 132.57 ? 226 LYS   M NZ  1 
ATOM   23069 N  N   . GLY   M  13 240 ? 18.182  -175.183 64.799  1.00 108.62 ? 227 GLY   M N   1 
ATOM   23070 C  CA  . GLY   M  13 240 ? 18.829  -175.536 63.521  1.00 109.99 ? 227 GLY   M CA  1 
ATOM   23071 C  C   . GLY   M  13 240 ? 18.250  -174.755 62.356  1.00 107.03 ? 227 GLY   M C   1 
ATOM   23072 O  O   . GLY   M  13 240 ? 17.389  -173.884 62.597  1.00 105.11 ? 227 GLY   M O   1 
ATOM   23073 N  N   . TYR   M  13 241 ? 18.693  -175.067 61.134  1.00 106.93 ? 228 TYR   M N   1 
ATOM   23074 C  CA  . TYR   M  13 241 ? 18.242  -174.417 59.873  1.00 103.62 ? 228 TYR   M CA  1 
ATOM   23075 C  C   . TYR   M  13 241 ? 17.438  -175.409 59.015  1.00 105.03 ? 228 TYR   M C   1 
ATOM   23076 O  O   . TYR   M  13 241 ? 17.196  -175.091 57.831  1.00 101.35 ? 228 TYR   M O   1 
ATOM   23077 C  CB  . TYR   M  13 241 ? 19.432  -173.810 59.118  1.00 99.00  ? 228 TYR   M CB  1 
ATOM   23078 C  CG  . TYR   M  13 241 ? 20.575  -174.745 58.811  1.00 99.21  ? 228 TYR   M CG  1 
ATOM   23079 C  CD1 . TYR   M  13 241 ? 20.463  -175.718 57.830  1.00 102.47 ? 228 TYR   M CD1 1 
ATOM   23080 C  CD2 . TYR   M  13 241 ? 21.787  -174.638 59.478  1.00 98.22  ? 228 TYR   M CD2 1 
ATOM   23081 C  CE1 . TYR   M  13 241 ? 21.511  -176.575 57.536  1.00 105.64 ? 228 TYR   M CE1 1 
ATOM   23082 C  CE2 . TYR   M  13 241 ? 22.846  -175.485 59.193  1.00 100.48 ? 228 TYR   M CE2 1 
ATOM   23083 C  CZ  . TYR   M  13 241 ? 22.709  -176.456 58.220  1.00 104.19 ? 228 TYR   M CZ  1 
ATOM   23084 O  OH  . TYR   M  13 241 ? 23.759  -177.281 57.950  1.00 109.35 ? 228 TYR   M OH  1 
ATOM   23085 N  N   . GLY   M  13 242 ? 17.018  -176.551 59.581  1.00 110.08 ? 229 GLY   M N   1 
ATOM   23086 C  CA  . GLY   M  13 242 ? 16.141  -177.518 58.888  1.00 111.53 ? 229 GLY   M CA  1 
ATOM   23087 C  C   . GLY   M  13 242 ? 16.044  -178.871 59.581  1.00 114.04 ? 229 GLY   M C   1 
ATOM   23088 O  O   . GLY   M  13 242 ? 14.951  -179.194 60.094  1.00 109.11 ? 229 GLY   M O   1 
ATOM   23089 N  N   . THR   M  13 243 ? 17.130  -179.652 59.573  1.00 116.84 ? 230 THR   M N   1 
ATOM   23090 C  CA  . THR   M  13 243 ? 17.149  -181.085 59.980  1.00 121.34 ? 230 THR   M CA  1 
ATOM   23091 C  C   . THR   M  13 243 ? 17.583  -181.263 61.441  1.00 124.63 ? 230 THR   M C   1 
ATOM   23092 O  O   . THR   M  13 243 ? 17.378  -182.374 61.968  1.00 130.14 ? 230 THR   M O   1 
ATOM   23093 C  CB  . THR   M  13 243 ? 18.081  -181.908 59.082  1.00 122.54 ? 230 THR   M CB  1 
ATOM   23094 O  OG1 . THR   M  13 243 ? 19.404  -181.385 59.212  1.00 120.47 ? 230 THR   M OG1 1 
ATOM   23095 C  CG2 . THR   M  13 243 ? 17.663  -181.888 57.629  1.00 121.90 ? 230 THR   M CG2 1 
ATOM   23096 N  N   . GLN   M  13 244 ? 18.169  -180.236 62.065  1.00 125.34 ? 231 GLN   M N   1 
ATOM   23097 C  CA  . GLN   M  13 244 ? 18.704  -180.310 63.452  1.00 126.25 ? 231 GLN   M CA  1 
ATOM   23098 C  C   . GLN   M  13 244 ? 17.541  -180.423 64.446  1.00 126.51 ? 231 GLN   M C   1 
ATOM   23099 O  O   . GLN   M  13 244 ? 16.541  -179.697 64.267  1.00 122.66 ? 231 GLN   M O   1 
ATOM   23100 C  CB  . GLN   M  13 244 ? 19.559  -179.083 63.758  1.00 126.08 ? 231 GLN   M CB  1 
ATOM   23101 C  CG  . GLN   M  13 244 ? 20.401  -179.235 65.014  1.00 127.91 ? 231 GLN   M CG  1 
ATOM   23102 C  CD  . GLN   M  13 244 ? 21.528  -178.233 65.058  1.00 126.80 ? 231 GLN   M CD  1 
ATOM   23103 O  OE1 . GLN   M  13 244 ? 22.347  -178.155 64.145  1.00 124.29 ? 231 GLN   M OE1 1 
ATOM   23104 N  NE2 . GLN   M  13 244 ? 21.577  -177.454 66.127  1.00 126.82 ? 231 GLN   M NE2 1 
ATOM   23105 N  N   . LYS   M  13 245 ? 17.680  -181.289 65.457  1.00 129.73 ? 232 LYS   M N   1 
ATOM   23106 C  CA  . LYS   M  13 245 ? 16.615  -181.617 66.446  1.00 134.03 ? 232 LYS   M CA  1 
ATOM   23107 C  C   . LYS   M  13 245 ? 16.932  -181.016 67.823  1.00 138.55 ? 232 LYS   M C   1 
ATOM   23108 O  O   . LYS   M  13 245 ? 16.081  -181.150 68.726  1.00 142.91 ? 232 LYS   M O   1 
ATOM   23109 C  CB  . LYS   M  13 245 ? 16.450  -183.135 66.554  1.00 132.76 ? 232 LYS   M CB  1 
ATOM   23110 C  CG  . LYS   M  13 245 ? 15.864  -183.792 65.314  1.00 128.39 ? 232 LYS   M CG  1 
ATOM   23111 C  CD  . LYS   M  13 245 ? 15.553  -185.255 65.489  1.00 130.31 ? 232 LYS   M CD  1 
ATOM   23112 C  CE  . LYS   M  13 245 ? 14.752  -185.808 64.331  1.00 129.40 ? 232 LYS   M CE  1 
ATOM   23113 N  NZ  . LYS   M  13 245 ? 14.547  -187.268 64.457  1.00 132.52 ? 232 LYS   M NZ  1 
ATOM   23114 N  N   . ILE   M  13 246 ? 18.093  -180.376 67.980  1.00 144.59 ? 233 ILE   M N   1 
ATOM   23115 C  CA  . ILE   M  13 246 ? 18.543  -179.777 69.273  1.00 147.01 ? 233 ILE   M CA  1 
ATOM   23116 C  C   . ILE   M  13 246 ? 19.369  -178.519 68.979  1.00 150.66 ? 233 ILE   M C   1 
ATOM   23117 O  O   . ILE   M  13 246 ? 20.257  -178.493 68.130  1.00 156.01 ? 233 ILE   M O   1 
ATOM   23118 C  CB  . ILE   M  13 246 ? 19.313  -180.813 70.120  1.00 147.29 ? 233 ILE   M CB  1 
ATOM   23119 C  CG1 . ILE   M  13 246 ? 19.917  -180.182 71.378  1.00 144.85 ? 233 ILE   M CG1 1 
ATOM   23120 C  CG2 . ILE   M  13 246 ? 20.366  -181.532 69.287  1.00 142.65 ? 233 ILE   M CG2 1 
ATOM   23121 C  CD1 . ILE   M  13 246 ? 20.109  -181.151 72.520  1.00 145.30 ? 233 ILE   M CD1 1 
ATOM   23122 O  OXT . ILE   M  13 246 ? 19.142  -177.488 69.605  1.00 151.32 ? 233 ILE   M OXT 1 
ATOM   23123 N  N   . THR   N  14 1   ? 44.429  -144.320 63.257  1.00 93.10  ? 1   THR   N N   1 
ATOM   23124 C  CA  . THR   N  14 1   ? 44.332  -143.169 64.206  1.00 92.11  ? 1   THR   N CA  1 
ATOM   23125 C  C   . THR   N  14 1   ? 43.297  -143.483 65.291  1.00 89.57  ? 1   THR   N C   1 
ATOM   23126 O  O   . THR   N  14 1   ? 42.176  -143.884 64.930  1.00 91.31  ? 1   THR   N O   1 
ATOM   23127 C  CB  . THR   N  14 1   ? 43.939  -141.877 63.479  1.00 91.99  ? 1   THR   N CB  1 
ATOM   23128 O  OG1 . THR   N  14 1   ? 44.968  -141.561 62.541  1.00 95.09  ? 1   THR   N OG1 1 
ATOM   23129 C  CG2 . THR   N  14 1   ? 43.725  -140.709 64.417  1.00 90.26  ? 1   THR   N CG2 1 
ATOM   23130 N  N   . SER   N  14 2   ? 43.656  -143.291 66.563  1.00 88.16  ? 2   SER   N N   1 
ATOM   23131 C  CA  . SER   N  14 2   ? 42.743  -143.416 67.729  1.00 88.11  ? 2   SER   N CA  1 
ATOM   23132 C  C   . SER   N  14 2   ? 42.773  -142.117 68.536  1.00 86.98  ? 2   SER   N C   1 
ATOM   23133 O  O   . SER   N  14 2   ? 43.862  -141.744 69.022  1.00 86.55  ? 2   SER   N O   1 
ATOM   23134 C  CB  . SER   N  14 2   ? 43.099  -144.593 68.592  1.00 89.16  ? 2   SER   N CB  1 
ATOM   23135 O  OG  . SER   N  14 2   ? 43.324  -145.752 67.806  1.00 90.92  ? 2   SER   N OG  1 
ATOM   23136 N  N   . ILE   N  14 3   ? 41.615  -141.463 68.658  1.00 84.23  ? 3   ILE   N N   1 
ATOM   23137 C  CA  . ILE   N  14 3   ? 41.438  -140.161 69.364  1.00 83.17  ? 3   ILE   N CA  1 
ATOM   23138 C  C   . ILE   N  14 3   ? 40.149  -140.224 70.186  1.00 77.50  ? 3   ILE   N C   1 
ATOM   23139 O  O   . ILE   N  14 3   ? 39.208  -140.921 69.766  1.00 72.63  ? 3   ILE   N O   1 
ATOM   23140 C  CB  . ILE   N  14 3   ? 41.413  -138.994 68.357  1.00 83.08  ? 3   ILE   N CB  1 
ATOM   23141 C  CG1 . ILE   N  14 3   ? 40.259  -139.125 67.358  1.00 84.11  ? 3   ILE   N CG1 1 
ATOM   23142 C  CG2 . ILE   N  14 3   ? 42.756  -138.860 67.654  1.00 85.47  ? 3   ILE   N CG2 1 
ATOM   23143 C  CD1 . ILE   N  14 3   ? 40.056  -137.909 66.484  1.00 84.35  ? 3   ILE   N CD1 1 
ATOM   23144 N  N   . MET   N  14 4   ? 40.103  -139.503 71.305  1.00 79.20  ? 4   MET   N N   1 
ATOM   23145 C  CA  . MET   N  14 4   ? 38.887  -139.409 72.150  1.00 82.60  ? 4   MET   N CA  1 
ATOM   23146 C  C   . MET   N  14 4   ? 38.971  -138.191 73.076  1.00 81.24  ? 4   MET   N C   1 
ATOM   23147 O  O   . MET   N  14 4   ? 40.084  -137.677 73.304  1.00 80.88  ? 4   MET   N O   1 
ATOM   23148 C  CB  . MET   N  14 4   ? 38.702  -140.689 72.973  1.00 84.52  ? 4   MET   N CB  1 
ATOM   23149 C  CG  . MET   N  14 4   ? 39.802  -140.950 73.992  1.00 87.91  ? 4   MET   N CG  1 
ATOM   23150 S  SD  . MET   N  14 4   ? 39.675  -142.599 74.744  1.00 88.71  ? 4   MET   N SD  1 
ATOM   23151 C  CE  . MET   N  14 4   ? 38.085  -142.472 75.563  1.00 91.23  ? 4   MET   N CE  1 
ATOM   23152 N  N   . ALA   N  14 5   ? 37.811  -137.745 73.562  1.00 81.80  ? 5   ALA   N N   1 
ATOM   23153 C  CA  . ALA   N  14 5   ? 37.649  -136.654 74.547  1.00 83.05  ? 5   ALA   N CA  1 
ATOM   23154 C  C   . ALA   N  14 5   ? 36.649  -137.109 75.612  1.00 82.10  ? 5   ALA   N C   1 
ATOM   23155 O  O   . ALA   N  14 5   ? 35.593  -137.651 75.236  1.00 81.30  ? 5   ALA   N O   1 
ATOM   23156 C  CB  . ALA   N  14 5   ? 37.190  -135.396 73.853  1.00 82.95  ? 5   ALA   N CB  1 
ATOM   23157 N  N   . VAL   N  14 6   ? 36.979  -136.909 76.889  1.00 83.86  ? 6   VAL   N N   1 
ATOM   23158 C  CA  . VAL   N  14 6   ? 36.125  -137.320 78.041  1.00 84.44  ? 6   VAL   N CA  1 
ATOM   23159 C  C   . VAL   N  14 6   ? 35.920  -136.117 78.968  1.00 85.22  ? 6   VAL   N C   1 
ATOM   23160 O  O   . VAL   N  14 6   ? 36.900  -135.390 79.235  1.00 82.91  ? 6   VAL   N O   1 
ATOM   23161 C  CB  . VAL   N  14 6   ? 36.728  -138.512 78.807  1.00 86.48  ? 6   VAL   N CB  1 
ATOM   23162 C  CG1 . VAL   N  14 6   ? 35.686  -139.182 79.691  1.00 86.99  ? 6   VAL   N CG1 1 
ATOM   23163 C  CG2 . VAL   N  14 6   ? 37.371  -139.528 77.874  1.00 86.30  ? 6   VAL   N CG2 1 
ATOM   23164 N  N   . THR   N  14 7   ? 34.689  -135.959 79.459  1.00 85.29  ? 7   THR   N N   1 
ATOM   23165 C  CA  . THR   N  14 7   ? 34.252  -134.877 80.377  1.00 87.39  ? 7   THR   N CA  1 
ATOM   23166 C  C   . THR   N  14 7   ? 34.191  -135.456 81.791  1.00 91.51  ? 7   THR   N C   1 
ATOM   23167 O  O   . THR   N  14 7   ? 33.517  -136.488 81.976  1.00 94.10  ? 7   THR   N O   1 
ATOM   23168 C  CB  . THR   N  14 7   ? 32.893  -134.296 79.962  1.00 85.62  ? 7   THR   N CB  1 
ATOM   23169 O  OG1 . THR   N  14 7   ? 31.849  -135.014 80.620  1.00 84.28  ? 7   THR   N OG1 1 
ATOM   23170 C  CG2 . THR   N  14 7   ? 32.662  -134.342 78.469  1.00 84.97  ? 7   THR   N CG2 1 
ATOM   23171 N  N   . PHE   N  14 8   ? 34.875  -134.827 82.750  1.00 91.63  ? 8   PHE   N N   1 
ATOM   23172 C  CA  . PHE   N  14 8   ? 34.815  -135.327 84.146  1.00 96.39  ? 8   PHE   N CA  1 
ATOM   23173 C  C   . PHE   N  14 8   ? 34.165  -134.298 85.069  1.00 99.77  ? 8   PHE   N C   1 
ATOM   23174 O  O   . PHE   N  14 8   ? 33.116  -133.760 84.713  1.00 102.47 ? 8   PHE   N O   1 
ATOM   23175 C  CB  . PHE   N  14 8   ? 36.156  -135.867 84.644  1.00 97.06  ? 8   PHE   N CB  1 
ATOM   23176 C  CG  . PHE   N  14 8   ? 37.365  -134.981 84.528  1.00 95.60  ? 8   PHE   N CG  1 
ATOM   23177 C  CD1 . PHE   N  14 8   ? 37.998  -134.799 83.318  1.00 96.06  ? 8   PHE   N CD1 1 
ATOM   23178 C  CD2 . PHE   N  14 8   ? 37.930  -134.413 85.651  1.00 97.35  ? 8   PHE   N CD2 1 
ATOM   23179 C  CE1 . PHE   N  14 8   ? 39.140  -134.022 83.230  1.00 96.86  ? 8   PHE   N CE1 1 
ATOM   23180 C  CE2 . PHE   N  14 8   ? 39.067  -133.633 85.561  1.00 97.86  ? 8   PHE   N CE2 1 
ATOM   23181 C  CZ  . PHE   N  14 8   ? 39.671  -133.437 84.349  1.00 97.63  ? 8   PHE   N CZ  1 
ATOM   23182 N  N   . LYS   N  14 9   ? 34.763  -134.081 86.238  1.00 103.44 ? 9   LYS   N N   1 
ATOM   23183 C  CA  . LYS   N  14 9   ? 34.242  -133.126 87.246  1.00 107.14 ? 9   LYS   N CA  1 
ATOM   23184 C  C   . LYS   N  14 9   ? 34.967  -131.786 87.103  1.00 105.08 ? 9   LYS   N C   1 
ATOM   23185 O  O   . LYS   N  14 9   ? 34.293  -130.756 87.079  1.00 104.81 ? 9   LYS   N O   1 
ATOM   23186 C  CB  . LYS   N  14 9   ? 34.498  -133.691 88.644  1.00 112.02 ? 9   LYS   N CB  1 
ATOM   23187 C  CG  . LYS   N  14 9   ? 33.395  -133.459 89.663  1.00 116.70 ? 9   LYS   N CG  1 
ATOM   23188 C  CD  . LYS   N  14 9   ? 33.917  -133.482 91.080  1.00 119.89 ? 9   LYS   N CD  1 
ATOM   23189 C  CE  . LYS   N  14 9   ? 35.419  -133.663 91.144  1.00 123.59 ? 9   LYS   N CE  1 
ATOM   23190 N  NZ  . LYS   N  14 9   ? 36.008  -132.933 92.290  1.00 125.91 ? 9   LYS   N NZ  1 
ATOM   23191 N  N   . ASP   N  14 10  ? 36.292  -131.821 86.972  1.00 105.78 ? 10  ASP   N N   1 
ATOM   23192 C  CA  . ASP   N  14 10  ? 37.114  -130.588 86.885  1.00 104.43 ? 10  ASP   N CA  1 
ATOM   23193 C  C   . ASP   N  14 10  ? 37.261  -130.102 85.445  1.00 100.66 ? 10  ASP   N C   1 
ATOM   23194 O  O   . ASP   N  14 10  ? 38.107  -129.226 85.232  1.00 99.37  ? 10  ASP   N O   1 
ATOM   23195 C  CB  . ASP   N  14 10  ? 38.529  -130.829 87.406  1.00 108.55 ? 10  ASP   N CB  1 
ATOM   23196 C  CG  . ASP   N  14 10  ? 38.570  -131.468 88.775  1.00 112.27 ? 10  ASP   N CG  1 
ATOM   23197 O  OD1 . ASP   N  14 10  ? 37.492  -131.695 89.337  1.00 119.01 ? 10  ASP   N OD1 1 
ATOM   23198 O  OD2 . ASP   N  14 10  ? 39.681  -131.726 89.260  1.00 116.33 ? 10  ASP   N OD2 1 
ATOM   23199 N  N   . GLY   N  14 11  ? 36.515  -130.655 84.490  1.00 95.86  ? 11  GLY   N N   1 
ATOM   23200 C  CA  . GLY   N  14 11  ? 36.670  -130.154 83.114  1.00 93.78  ? 11  GLY   N CA  1 
ATOM   23201 C  C   . GLY   N  14 11  ? 36.536  -131.217 82.046  1.00 91.06  ? 11  GLY   N C   1 
ATOM   23202 O  O   . GLY   N  14 11  ? 35.507  -131.881 82.020  1.00 90.66  ? 11  GLY   N O   1 
ATOM   23203 N  N   . VAL   N  14 12  ? 37.549  -131.323 81.187  1.00 92.13  ? 12  VAL   N N   1 
ATOM   23204 C  CA  . VAL   N  14 12  ? 37.592  -132.269 80.031  1.00 92.74  ? 12  VAL   N CA  1 
ATOM   23205 C  C   . VAL   N  14 12  ? 39.052  -132.653 79.753  1.00 93.37  ? 12  VAL   N C   1 
ATOM   23206 O  O   . VAL   N  14 12  ? 39.948  -131.830 80.043  1.00 95.17  ? 12  VAL   N O   1 
ATOM   23207 C  CB  . VAL   N  14 12  ? 36.907  -131.647 78.796  1.00 93.36  ? 12  VAL   N CB  1 
ATOM   23208 C  CG1 . VAL   N  14 12  ? 37.666  -130.438 78.270  1.00 95.23  ? 12  VAL   N CG1 1 
ATOM   23209 C  CG2 . VAL   N  14 12  ? 36.677  -132.662 77.685  1.00 91.61  ? 12  VAL   N CG2 1 
ATOM   23210 N  N   . ILE   N  14 13  ? 39.276  -133.862 79.224  1.00 92.25  ? 13  ILE   N N   1 
ATOM   23211 C  CA  . ILE   N  14 13  ? 40.616  -134.366 78.793  1.00 89.98  ? 13  ILE   N CA  1 
ATOM   23212 C  C   . ILE   N  14 13  ? 40.504  -134.909 77.366  1.00 85.37  ? 13  ILE   N C   1 
ATOM   23213 O  O   . ILE   N  14 13  ? 39.521  -135.614 77.072  1.00 82.21  ? 13  ILE   N O   1 
ATOM   23214 C  CB  . ILE   N  14 13  ? 41.167  -135.437 79.754  1.00 91.07  ? 13  ILE   N CB  1 
ATOM   23215 C  CG1 . ILE   N  14 13  ? 41.098  -134.980 81.214  1.00 94.13  ? 13  ILE   N CG1 1 
ATOM   23216 C  CG2 . ILE   N  14 13  ? 42.580  -135.834 79.347  1.00 90.43  ? 13  ILE   N CG2 1 
ATOM   23217 C  CD1 . ILE   N  14 13  ? 41.621  -135.986 82.216  1.00 93.83  ? 13  ILE   N CD1 1 
ATOM   23218 N  N   . LEU   N  14 14  ? 41.499  -134.591 76.534  1.00 84.79  ? 14  LEU   N N   1 
ATOM   23219 C  CA  . LEU   N  14 14  ? 41.618  -135.043 75.126  1.00 86.99  ? 14  LEU   N CA  1 
ATOM   23220 C  C   . LEU   N  14 14  ? 42.755  -136.060 75.061  1.00 87.10  ? 14  LEU   N C   1 
ATOM   23221 O  O   . LEU   N  14 14  ? 43.844  -135.743 75.567  1.00 91.56  ? 14  LEU   N O   1 
ATOM   23222 C  CB  . LEU   N  14 14  ? 41.921  -133.847 74.218  1.00 87.33  ? 14  LEU   N CB  1 
ATOM   23223 C  CG  . LEU   N  14 14  ? 40.886  -132.723 74.212  1.00 90.45  ? 14  LEU   N CG  1 
ATOM   23224 C  CD1 . LEU   N  14 14  ? 40.974  -131.880 75.478  1.00 92.06  ? 14  LEU   N CD1 1 
ATOM   23225 C  CD2 . LEU   N  14 14  ? 41.069  -131.844 72.984  1.00 90.87  ? 14  LEU   N CD2 1 
ATOM   23226 N  N   . GLY   N  14 15  ? 42.497  -137.227 74.469  1.00 85.43  ? 15  GLY   N N   1 
ATOM   23227 C  CA  . GLY   N  14 15  ? 43.487  -138.302 74.286  1.00 82.74  ? 15  GLY   N CA  1 
ATOM   23228 C  C   . GLY   N  14 15  ? 43.603  -138.692 72.827  1.00 80.57  ? 15  GLY   N C   1 
ATOM   23229 O  O   . GLY   N  14 15  ? 42.577  -138.658 72.122  1.00 78.98  ? 15  GLY   N O   1 
ATOM   23230 N  N   . ALA   N  14 16  ? 44.812  -139.048 72.393  1.00 79.77  ? 16  ALA   N N   1 
ATOM   23231 C  CA  . ALA   N  14 16  ? 45.111  -139.486 71.013  1.00 80.19  ? 16  ALA   N CA  1 
ATOM   23232 C  C   . ALA   N  14 16  ? 46.376  -140.350 71.003  1.00 80.77  ? 16  ALA   N C   1 
ATOM   23233 O  O   . ALA   N  14 16  ? 47.152  -140.287 71.975  1.00 80.51  ? 16  ALA   N O   1 
ATOM   23234 C  CB  . ALA   N  14 16  ? 45.255  -138.276 70.125  1.00 79.64  ? 16  ALA   N CB  1 
ATOM   23235 N  N   . ASP   N  14 17  ? 46.556  -141.136 69.940  1.00 80.45  ? 17  ASP   N N   1 
ATOM   23236 C  CA  . ASP   N  14 17  ? 47.816  -141.865 69.643  1.00 84.62  ? 17  ASP   N CA  1 
ATOM   23237 C  C   . ASP   N  14 17  ? 48.771  -140.878 68.962  1.00 86.51  ? 17  ASP   N C   1 
ATOM   23238 O  O   . ASP   N  14 17  ? 48.408  -139.683 68.866  1.00 89.22  ? 17  ASP   N O   1 
ATOM   23239 C  CB  . ASP   N  14 17  ? 47.540  -143.104 68.790  1.00 86.96  ? 17  ASP   N CB  1 
ATOM   23240 C  CG  . ASP   N  14 17  ? 47.039  -142.784 67.392  1.00 87.61  ? 17  ASP   N CG  1 
ATOM   23241 O  OD1 . ASP   N  14 17  ? 46.385  -141.733 67.230  1.00 89.23  ? 17  ASP   N OD1 1 
ATOM   23242 O  OD2 . ASP   N  14 17  ? 47.306  -143.583 66.476  1.00 90.41  ? 17  ASP   N OD2 1 
ATOM   23243 N  N   . SER   N  14 18  ? 49.939  -141.342 68.510  1.00 83.23  ? 18  SER   N N   1 
ATOM   23244 C  CA  . SER   N  14 18  ? 50.958  -140.493 67.838  1.00 82.23  ? 18  SER   N CA  1 
ATOM   23245 C  C   . SER   N  14 18  ? 51.364  -141.082 66.485  1.00 80.43  ? 18  SER   N C   1 
ATOM   23246 O  O   . SER   N  14 18  ? 52.418  -140.672 65.966  1.00 81.10  ? 18  SER   N O   1 
ATOM   23247 C  CB  . SER   N  14 18  ? 52.164  -140.308 68.712  1.00 82.28  ? 18  SER   N CB  1 
ATOM   23248 O  OG  . SER   N  14 18  ? 53.025  -141.435 68.626  1.00 79.68  ? 18  SER   N OG  1 
ATOM   23249 N  N   . ARG   N  14 19  ? 50.575  -142.001 65.930  1.00 80.72  ? 19  ARG   N N   1 
ATOM   23250 C  CA  . ARG   N  14 19  ? 50.949  -142.701 64.676  1.00 83.31  ? 19  ARG   N CA  1 
ATOM   23251 C  C   . ARG   N  14 19  ? 50.138  -142.155 63.502  1.00 80.81  ? 19  ARG   N C   1 
ATOM   23252 O  O   . ARG   N  14 19  ? 48.898  -142.228 63.544  1.00 80.11  ? 19  ARG   N O   1 
ATOM   23253 C  CB  . ARG   N  14 19  ? 50.743  -144.210 64.788  1.00 84.64  ? 19  ARG   N CB  1 
ATOM   23254 C  CG  . ARG   N  14 19  ? 50.843  -144.913 63.443  1.00 86.26  ? 19  ARG   N CG  1 
ATOM   23255 C  CD  . ARG   N  14 19  ? 50.754  -146.415 63.576  1.00 85.94  ? 19  ARG   N CD  1 
ATOM   23256 N  NE  . ARG   N  14 19  ? 51.903  -146.975 64.265  1.00 85.96  ? 19  ARG   N NE  1 
ATOM   23257 C  CZ  . ARG   N  14 19  ? 52.022  -148.252 64.595  1.00 84.82  ? 19  ARG   N CZ  1 
ATOM   23258 N  NH1 . ARG   N  14 19  ? 51.057  -149.106 64.298  1.00 86.29  ? 19  ARG   N NH1 1 
ATOM   23259 N  NH2 . ARG   N  14 19  ? 53.105  -148.674 65.218  1.00 86.96  ? 19  ARG   N NH2 1 
ATOM   23260 N  N   . THR   N  14 20  ? 50.844  -141.673 62.481  1.00 81.64  ? 20  THR   N N   1 
ATOM   23261 C  CA  . THR   N  14 20  ? 50.304  -141.288 61.154  1.00 83.47  ? 20  THR   N CA  1 
ATOM   23262 C  C   . THR   N  14 20  ? 50.982  -142.198 60.123  1.00 80.79  ? 20  THR   N C   1 
ATOM   23263 O  O   . THR   N  14 20  ? 52.227  -142.299 60.166  1.00 77.22  ? 20  THR   N O   1 
ATOM   23264 C  CB  . THR   N  14 20  ? 50.530  -139.790 60.910  1.00 85.06  ? 20  THR   N CB  1 
ATOM   23265 O  OG1 . THR   N  14 20  ? 49.752  -139.372 59.787  1.00 85.78  ? 20  THR   N OG1 1 
ATOM   23266 C  CG2 . THR   N  14 20  ? 51.989  -139.464 60.681  1.00 87.74  ? 20  THR   N CG2 1 
ATOM   23267 N  N   . THR   N  14 21  ? 50.211  -142.865 59.261  1.00 81.63  ? 21  THR   N N   1 
ATOM   23268 C  CA  . THR   N  14 21  ? 50.742  -143.863 58.294  1.00 81.93  ? 21  THR   N CA  1 
ATOM   23269 C  C   . THR   N  14 21  ? 50.297  -143.558 56.862  1.00 82.46  ? 21  THR   N C   1 
ATOM   23270 O  O   . THR   N  14 21  ? 49.198  -142.998 56.676  1.00 82.62  ? 21  THR   N O   1 
ATOM   23271 C  CB  . THR   N  14 21  ? 50.286  -145.285 58.630  1.00 81.91  ? 21  THR   N CB  1 
ATOM   23272 O  OG1 . THR   N  14 21  ? 48.863  -145.316 58.515  1.00 78.57  ? 21  THR   N OG1 1 
ATOM   23273 C  CG2 . THR   N  14 21  ? 50.709  -145.729 60.012  1.00 84.49  ? 21  THR   N CG2 1 
ATOM   23274 N  N   . THR   N  14 22  ? 51.141  -143.952 55.906  1.00 84.07  ? 22  THR   N N   1 
ATOM   23275 C  CA  . THR   N  14 22  ? 50.866  -144.014 54.447  1.00 84.94  ? 22  THR   N CA  1 
ATOM   23276 C  C   . THR   N  14 22  ? 50.845  -145.486 54.026  1.00 85.68  ? 22  THR   N C   1 
ATOM   23277 O  O   . THR   N  14 22  ? 51.928  -146.108 54.014  1.00 84.42  ? 22  THR   N O   1 
ATOM   23278 C  CB  . THR   N  14 22  ? 51.948  -143.279 53.651  1.00 83.71  ? 22  THR   N CB  1 
ATOM   23279 O  OG1 . THR   N  14 22  ? 52.111  -141.973 54.201  1.00 83.04  ? 22  THR   N OG1 1 
ATOM   23280 C  CG2 . THR   N  14 22  ? 51.627  -143.183 52.176  1.00 84.75  ? 22  THR   N CG2 1 
ATOM   23281 N  N   . GLY   N  14 23  ? 49.671  -146.019 53.687  1.00 87.31  ? 23  GLY   N N   1 
ATOM   23282 C  CA  . GLY   N  14 23  ? 49.486  -147.469 53.496  1.00 88.24  ? 23  GLY   N CA  1 
ATOM   23283 C  C   . GLY   N  14 23  ? 49.831  -148.209 54.777  1.00 88.38  ? 23  GLY   N C   1 
ATOM   23284 O  O   . GLY   N  14 23  ? 49.148  -147.968 55.791  1.00 88.04  ? 23  GLY   N O   1 
ATOM   23285 N  N   . ALA   N  14 24  ? 50.881  -149.037 54.746  1.00 90.35  ? 24  ALA   N N   1 
ATOM   23286 C  CA  . ALA   N  14 24  ? 51.383  -149.823 55.900  1.00 90.33  ? 24  ALA   N CA  1 
ATOM   23287 C  C   . ALA   N  14 24  ? 52.728  -149.268 56.394  1.00 88.52  ? 24  ALA   N C   1 
ATOM   23288 O  O   . ALA   N  14 24  ? 53.329  -149.893 57.289  1.00 83.51  ? 24  ALA   N O   1 
ATOM   23289 C  CB  . ALA   N  14 24  ? 51.502  -151.272 55.506  1.00 91.38  ? 24  ALA   N CB  1 
ATOM   23290 N  N   . TYR   N  14 25  ? 53.189  -148.144 55.835  1.00 86.43  ? 25  TYR   N N   1 
ATOM   23291 C  CA  . TYR   N  14 25  ? 54.414  -147.428 56.276  1.00 86.10  ? 25  TYR   N CA  1 
ATOM   23292 C  C   . TYR   N  14 25  ? 54.021  -146.324 57.258  1.00 85.04  ? 25  TYR   N C   1 
ATOM   23293 O  O   . TYR   N  14 25  ? 53.040  -145.609 56.984  1.00 84.04  ? 25  TYR   N O   1 
ATOM   23294 C  CB  . TYR   N  14 25  ? 55.171  -146.818 55.094  1.00 86.10  ? 25  TYR   N CB  1 
ATOM   23295 C  CG  . TYR   N  14 25  ? 56.398  -146.042 55.501  1.00 87.08  ? 25  TYR   N CG  1 
ATOM   23296 C  CD1 . TYR   N  14 25  ? 57.454  -146.672 56.141  1.00 89.49  ? 25  TYR   N CD1 1 
ATOM   23297 C  CD2 . TYR   N  14 25  ? 56.502  -144.680 55.271  1.00 86.86  ? 25  TYR   N CD2 1 
ATOM   23298 C  CE1 . TYR   N  14 25  ? 58.586  -145.975 56.530  1.00 87.70  ? 25  TYR   N CE1 1 
ATOM   23299 C  CE2 . TYR   N  14 25  ? 57.629  -143.968 55.652  1.00 87.67  ? 25  TYR   N CE2 1 
ATOM   23300 C  CZ  . TYR   N  14 25  ? 58.676  -144.618 56.286  1.00 87.27  ? 25  TYR   N CZ  1 
ATOM   23301 O  OH  . TYR   N  14 25  ? 59.800  -143.948 56.674  1.00 85.88  ? 25  TYR   N OH  1 
ATOM   23302 N  N   . ILE   N  14 26  ? 54.771  -146.190 58.354  1.00 84.76  ? 26  ILE   N N   1 
ATOM   23303 C  CA  . ILE   N  14 26  ? 54.582  -145.111 59.367  1.00 84.39  ? 26  ILE   N CA  1 
ATOM   23304 C  C   . ILE   N  14 26  ? 55.441  -143.915 58.946  1.00 85.45  ? 26  ILE   N C   1 
ATOM   23305 O  O   . ILE   N  14 26  ? 56.677  -143.993 59.102  1.00 87.52  ? 26  ILE   N O   1 
ATOM   23306 C  CB  . ILE   N  14 26  ? 54.923  -145.609 60.787  1.00 85.13  ? 26  ILE   N CB  1 
ATOM   23307 C  CG1 . ILE   N  14 26  ? 54.108  -146.852 61.160  1.00 85.66  ? 26  ILE   N CG1 1 
ATOM   23308 C  CG2 . ILE   N  14 26  ? 54.745  -144.488 61.803  1.00 84.96  ? 26  ILE   N CG2 1 
ATOM   23309 C  CD1 . ILE   N  14 26  ? 54.529  -147.513 62.452  1.00 86.49  ? 26  ILE   N CD1 1 
ATOM   23310 N  N   . ALA   N  14 27  ? 54.804  -142.865 58.416  1.00 85.28  ? 27  ALA   N N   1 
ATOM   23311 C  CA  . ALA   N  14 27  ? 55.456  -141.604 57.994  1.00 84.30  ? 27  ALA   N CA  1 
ATOM   23312 C  C   . ALA   N  14 27  ? 56.022  -140.906 59.232  1.00 83.89  ? 27  ALA   N C   1 
ATOM   23313 O  O   . ALA   N  14 27  ? 57.220  -140.566 59.211  1.00 83.53  ? 27  ALA   N O   1 
ATOM   23314 C  CB  . ALA   N  14 27  ? 54.480  -140.721 57.257  1.00 84.07  ? 27  ALA   N CB  1 
ATOM   23315 N  N   . ASN   N  14 28  ? 55.191  -140.733 60.268  1.00 85.91  ? 28  ASN   N N   1 
ATOM   23316 C  CA  . ASN   N  14 28  ? 55.558  -140.107 61.568  1.00 87.79  ? 28  ASN   N CA  1 
ATOM   23317 C  C   . ASN   N  14 28  ? 55.051  -141.000 62.707  1.00 85.64  ? 28  ASN   N C   1 
ATOM   23318 O  O   . ASN   N  14 28  ? 53.862  -141.393 62.668  1.00 76.40  ? 28  ASN   N O   1 
ATOM   23319 C  CB  . ASN   N  14 28  ? 55.005  -138.683 61.700  1.00 90.51  ? 28  ASN   N CB  1 
ATOM   23320 C  CG  . ASN   N  14 28  ? 55.747  -137.834 62.710  1.00 94.00  ? 28  ASN   N CG  1 
ATOM   23321 O  OD1 . ASN   N  14 28  ? 56.918  -138.075 63.000  1.00 96.61  ? 28  ASN   N OD1 1 
ATOM   23322 N  ND2 . ASN   N  14 28  ? 55.075  -136.829 63.249  1.00 98.56  ? 28  ASN   N ND2 1 
ATOM   23323 N  N   . ARG   N  14 29  ? 55.918  -141.306 63.679  1.00 85.22  ? 29  ARG   N N   1 
ATOM   23324 C  CA  . ARG   N  14 29  ? 55.576  -142.170 64.841  1.00 84.78  ? 29  ARG   N CA  1 
ATOM   23325 C  C   . ARG   N  14 29  ? 55.415  -141.324 66.109  1.00 83.36  ? 29  ARG   N C   1 
ATOM   23326 O  O   . ARG   N  14 29  ? 55.140  -141.918 67.164  1.00 81.76  ? 29  ARG   N O   1 
ATOM   23327 C  CB  . ARG   N  14 29  ? 56.623  -143.269 65.032  1.00 85.29  ? 29  ARG   N CB  1 
ATOM   23328 C  CG  . ARG   N  14 29  ? 58.031  -142.786 65.342  1.00 87.54  ? 29  ARG   N CG  1 
ATOM   23329 C  CD  . ARG   N  14 29  ? 58.920  -144.003 65.504  1.00 87.85  ? 29  ARG   N CD  1 
ATOM   23330 N  NE  . ARG   N  14 29  ? 60.276  -143.671 65.914  1.00 87.94  ? 29  ARG   N NE  1 
ATOM   23331 C  CZ  . ARG   N  14 29  ? 60.754  -143.771 67.151  1.00 89.30  ? 29  ARG   N CZ  1 
ATOM   23332 N  NH1 . ARG   N  14 29  ? 59.989  -144.200 68.142  1.00 87.73  ? 29  ARG   N NH1 1 
ATOM   23333 N  NH2 . ARG   N  14 29  ? 62.010  -143.435 67.395  1.00 94.49  ? 29  ARG   N NH2 1 
ATOM   23334 N  N   . VAL   N  14 30  ? 55.537  -139.997 66.007  1.00 85.05  ? 30  VAL   N N   1 
ATOM   23335 C  CA  . VAL   N  14 30  ? 55.445  -139.064 67.170  1.00 85.76  ? 30  VAL   N CA  1 
ATOM   23336 C  C   . VAL   N  14 30  ? 54.540  -137.876 66.809  1.00 85.67  ? 30  VAL   N C   1 
ATOM   23337 O  O   . VAL   N  14 30  ? 54.829  -136.756 67.265  1.00 90.57  ? 30  VAL   N O   1 
ATOM   23338 C  CB  . VAL   N  14 30  ? 56.851  -138.611 67.615  1.00 86.12  ? 30  VAL   N CB  1 
ATOM   23339 C  CG1 . VAL   N  14 30  ? 57.667  -139.771 68.164  1.00 85.66  ? 30  VAL   N CG1 1 
ATOM   23340 C  CG2 . VAL   N  14 30  ? 57.611  -137.915 66.495  1.00 87.06  ? 30  VAL   N CG2 1 
ATOM   23341 N  N   . THR   N  14 31  ? 53.464  -138.115 66.052  1.00 81.01  ? 31  THR   N N   1 
ATOM   23342 C  CA  . THR   N  14 31  ? 52.495  -137.075 65.607  1.00 81.85  ? 31  THR   N CA  1 
ATOM   23343 C  C   . THR   N  14 31  ? 51.758  -136.487 66.817  1.00 84.22  ? 31  THR   N C   1 
ATOM   23344 O  O   . THR   N  14 31  ? 51.422  -137.258 67.743  1.00 82.16  ? 31  THR   N O   1 
ATOM   23345 C  CB  . THR   N  14 31  ? 51.478  -137.635 64.606  1.00 80.06  ? 31  THR   N CB  1 
ATOM   23346 O  OG1 . THR   N  14 31  ? 52.189  -138.423 63.654  1.00 83.16  ? 31  THR   N OG1 1 
ATOM   23347 C  CG2 . THR   N  14 31  ? 50.711  -136.560 63.871  1.00 79.89  ? 31  THR   N CG2 1 
ATOM   23348 N  N   . ASP   N  14 32  ? 51.506  -135.174 66.794  1.00 84.92  ? 32  ASP   N N   1 
ATOM   23349 C  CA  . ASP   N  14 32  ? 50.660  -134.470 67.794  1.00 88.07  ? 32  ASP   N CA  1 
ATOM   23350 C  C   . ASP   N  14 32  ? 49.294  -134.195 67.156  1.00 86.47  ? 32  ASP   N C   1 
ATOM   23351 O  O   . ASP   N  14 32  ? 49.175  -133.208 66.409  1.00 85.02  ? 32  ASP   N O   1 
ATOM   23352 C  CB  . ASP   N  14 32  ? 51.334  -133.191 68.296  1.00 91.74  ? 32  ASP   N CB  1 
ATOM   23353 C  CG  . ASP   N  14 32  ? 50.586  -132.506 69.429  1.00 95.56  ? 32  ASP   N CG  1 
ATOM   23354 O  OD1 . ASP   N  14 32  ? 49.719  -133.160 70.052  1.00 92.02  ? 32  ASP   N OD1 1 
ATOM   23355 O  OD2 . ASP   N  14 32  ? 50.874  -131.319 69.678  1.00 104.79 ? 32  ASP   N OD2 1 
ATOM   23356 N  N   . LYS   N  14 33  ? 48.308  -135.048 67.448  1.00 89.99  ? 33  LYS   N N   1 
ATOM   23357 C  CA  . LYS   N  14 33  ? 46.950  -135.013 66.840  1.00 90.11  ? 33  LYS   N CA  1 
ATOM   23358 C  C   . LYS   N  14 33  ? 45.997  -134.211 67.732  1.00 89.74  ? 33  LYS   N C   1 
ATOM   23359 O  O   . LYS   N  14 33  ? 44.797  -134.144 67.397  1.00 92.36  ? 33  LYS   N O   1 
ATOM   23360 C  CB  . LYS   N  14 33  ? 46.438  -136.440 66.630  1.00 90.40  ? 33  LYS   N CB  1 
ATOM   23361 C  CG  . LYS   N  14 33  ? 47.343  -137.315 65.776  1.00 88.96  ? 33  LYS   N CG  1 
ATOM   23362 C  CD  . LYS   N  14 33  ? 46.890  -138.746 65.701  1.00 86.91  ? 33  LYS   N CD  1 
ATOM   23363 C  CE  . LYS   N  14 33  ? 47.613  -139.520 64.621  1.00 88.02  ? 33  LYS   N CE  1 
ATOM   23364 N  NZ  . LYS   N  14 33  ? 47.136  -140.919 64.542  1.00 88.08  ? 33  LYS   N NZ  1 
ATOM   23365 N  N   . LEU   N  14 34  ? 46.514  -133.649 68.828  1.00 89.87  ? 34  LEU   N N   1 
ATOM   23366 C  CA  . LEU   N  14 34  ? 45.811  -132.665 69.691  1.00 90.92  ? 34  LEU   N CA  1 
ATOM   23367 C  C   . LEU   N  14 34  ? 46.277  -131.266 69.283  1.00 89.43  ? 34  LEU   N C   1 
ATOM   23368 O  O   . LEU   N  14 34  ? 47.492  -131.000 69.374  1.00 91.57  ? 34  LEU   N O   1 
ATOM   23369 C  CB  . LEU   N  14 34  ? 46.142  -132.952 71.159  1.00 90.42  ? 34  LEU   N CB  1 
ATOM   23370 C  CG  . LEU   N  14 34  ? 45.959  -134.404 71.595  1.00 90.01  ? 34  LEU   N CG  1 
ATOM   23371 C  CD1 . LEU   N  14 34  ? 46.597  -134.647 72.952  1.00 89.83  ? 34  LEU   N CD1 1 
ATOM   23372 C  CD2 . LEU   N  14 34  ? 44.486  -134.778 71.616  1.00 90.61  ? 34  LEU   N CD2 1 
ATOM   23373 N  N   . THR   N  14 35  ? 45.359  -130.415 68.825  1.00 88.58  ? 35  THR   N N   1 
ATOM   23374 C  CA  . THR   N  14 35  ? 45.687  -129.058 68.322  1.00 87.74  ? 35  THR   N CA  1 
ATOM   23375 C  C   . THR   N  14 35  ? 44.894  -128.001 69.088  1.00 87.95  ? 35  THR   N C   1 
ATOM   23376 O  O   . THR   N  14 35  ? 43.738  -128.268 69.474  1.00 84.74  ? 35  THR   N O   1 
ATOM   23377 C  CB  . THR   N  14 35  ? 45.460  -128.957 66.813  1.00 87.90  ? 35  THR   N CB  1 
ATOM   23378 O  OG1 . THR   N  14 35  ? 44.123  -129.369 66.527  1.00 87.46  ? 35  THR   N OG1 1 
ATOM   23379 C  CG2 . THR   N  14 35  ? 46.439  -129.815 66.048  1.00 85.68  ? 35  THR   N CG2 1 
ATOM   23380 N  N   . ARG   N  14 36  ? 45.527  -126.845 69.277  1.00 88.81  ? 36  ARG   N N   1 
ATOM   23381 C  CA  . ARG   N  14 36  ? 44.995  -125.681 70.022  1.00 93.86  ? 36  ARG   N CA  1 
ATOM   23382 C  C   . ARG   N  14 36  ? 44.342  -124.740 69.013  1.00 88.96  ? 36  ARG   N C   1 
ATOM   23383 O  O   . ARG   N  14 36  ? 45.036  -124.338 68.061  1.00 91.30  ? 36  ARG   N O   1 
ATOM   23384 C  CB  . ARG   N  14 36  ? 46.139  -124.975 70.755  1.00 96.95  ? 36  ARG   N CB  1 
ATOM   23385 C  CG  . ARG   N  14 36  ? 45.685  -123.865 71.690  1.00 104.24 ? 36  ARG   N CG  1 
ATOM   23386 C  CD  . ARG   N  14 36  ? 46.743  -122.795 71.875  1.00 111.31 ? 36  ARG   N CD  1 
ATOM   23387 N  NE  . ARG   N  14 36  ? 46.464  -121.665 70.996  1.00 115.24 ? 36  ARG   N NE  1 
ATOM   23388 C  CZ  . ARG   N  14 36  ? 46.082  -120.453 71.395  1.00 118.41 ? 36  ARG   N CZ  1 
ATOM   23389 N  NH1 . ARG   N  14 36  ? 45.954  -120.177 72.683  1.00 122.78 ? 36  ARG   N NH1 1 
ATOM   23390 N  NH2 . ARG   N  14 36  ? 45.844  -119.508 70.501  1.00 120.52 ? 36  ARG   N NH2 1 
ATOM   23391 N  N   . VAL   N  14 37  ? 43.058  -124.432 69.196  1.00 87.36  ? 37  VAL   N N   1 
ATOM   23392 C  CA  . VAL   N  14 37  ? 42.340  -123.395 68.397  1.00 88.18  ? 37  VAL   N CA  1 
ATOM   23393 C  C   . VAL   N  14 37  ? 42.112  -122.160 69.278  1.00 91.11  ? 37  VAL   N C   1 
ATOM   23394 O  O   . VAL   N  14 37  ? 41.845  -121.084 68.716  1.00 94.39  ? 37  VAL   N O   1 
ATOM   23395 C  CB  . VAL   N  14 37  ? 41.030  -123.950 67.808  1.00 86.44  ? 37  VAL   N CB  1 
ATOM   23396 C  CG1 . VAL   N  14 37  ? 41.276  -125.254 67.069  1.00 84.18  ? 37  VAL   N CG1 1 
ATOM   23397 C  CG2 . VAL   N  14 37  ? 39.946  -124.133 68.858  1.00 87.88  ? 37  VAL   N CG2 1 
ATOM   23398 N  N   . HIS   N  14 38  ? 42.219  -122.317 70.602  1.00 91.54  ? 38  HIS   N N   1 
ATOM   23399 C  CA  . HIS   N  14 38  ? 42.108  -121.231 71.611  1.00 94.34  ? 38  HIS   N CA  1 
ATOM   23400 C  C   . HIS   N  14 38  ? 42.757  -121.693 72.922  1.00 96.21  ? 38  HIS   N C   1 
ATOM   23401 O  O   . HIS   N  14 38  ? 43.098  -122.887 73.017  1.00 95.25  ? 38  HIS   N O   1 
ATOM   23402 C  CB  . HIS   N  14 38  ? 40.640  -120.818 71.789  1.00 97.94  ? 38  HIS   N CB  1 
ATOM   23403 C  CG  . HIS   N  14 38  ? 40.476  -119.414 72.269  1.00 100.03 ? 38  HIS   N CG  1 
ATOM   23404 N  ND1 . HIS   N  14 38  ? 40.959  -118.333 71.557  1.00 98.67  ? 38  HIS   N ND1 1 
ATOM   23405 C  CD2 . HIS   N  14 38  ? 39.895  -118.911 73.379  1.00 102.16 ? 38  HIS   N CD2 1 
ATOM   23406 C  CE1 . HIS   N  14 38  ? 40.683  -117.224 72.208  1.00 99.69  ? 38  HIS   N CE1 1 
ATOM   23407 N  NE2 . HIS   N  14 38  ? 40.027  -117.551 73.327  1.00 101.31 ? 38  HIS   N NE2 1 
ATOM   23408 N  N   . ASP   N  14 39  ? 42.911  -120.787 73.894  1.00 97.03  ? 39  ASP   N N   1 
ATOM   23409 C  CA  . ASP   N  14 39  ? 43.621  -121.050 75.176  1.00 97.55  ? 39  ASP   N CA  1 
ATOM   23410 C  C   . ASP   N  14 39  ? 43.068  -122.327 75.816  1.00 93.65  ? 39  ASP   N C   1 
ATOM   23411 O  O   . ASP   N  14 39  ? 43.885  -123.187 76.201  1.00 91.34  ? 39  ASP   N O   1 
ATOM   23412 C  CB  . ASP   N  14 39  ? 43.518  -119.867 76.142  1.00 100.86 ? 39  ASP   N CB  1 
ATOM   23413 C  CG  . ASP   N  14 39  ? 44.129  -118.590 75.601  1.00 104.72 ? 39  ASP   N CG  1 
ATOM   23414 O  OD1 . ASP   N  14 39  ? 44.604  -117.779 76.418  1.00 114.21 ? 39  ASP   N OD1 1 
ATOM   23415 O  OD2 . ASP   N  14 39  ? 44.126  -118.423 74.365  1.00 108.23 ? 39  ASP   N OD2 1 
ATOM   23416 N  N   . LYS   N  14 40  ? 41.739  -122.444 75.910  1.00 94.14  ? 40  LYS   N N   1 
ATOM   23417 C  CA  . LYS   N  14 40  ? 41.050  -123.587 76.567  1.00 92.82  ? 40  LYS   N CA  1 
ATOM   23418 C  C   . LYS   N  14 40  ? 40.031  -124.236 75.619  1.00 89.07  ? 40  LYS   N C   1 
ATOM   23419 O  O   . LYS   N  14 40  ? 39.104  -124.884 76.132  1.00 90.81  ? 40  LYS   N O   1 
ATOM   23420 C  CB  . LYS   N  14 40  ? 40.413  -123.119 77.879  1.00 93.45  ? 40  LYS   N CB  1 
ATOM   23421 C  CG  . LYS   N  14 40  ? 41.254  -123.427 79.108  1.00 95.00  ? 40  LYS   N CG  1 
ATOM   23422 C  CD  . LYS   N  14 40  ? 41.000  -122.531 80.290  1.00 97.34  ? 40  LYS   N CD  1 
ATOM   23423 C  CE  . LYS   N  14 40  ? 41.948  -122.838 81.427  1.00 99.87  ? 40  LYS   N CE  1 
ATOM   23424 N  NZ  . LYS   N  14 40  ? 42.004  -121.738 82.415  1.00 104.50 ? 40  LYS   N NZ  1 
ATOM   23425 N  N   . ILE   N  14 41  ? 40.200  -124.094 74.299  1.00 88.15  ? 41  ILE   N N   1 
ATOM   23426 C  CA  . ILE   N  14 41  ? 39.455  -124.890 73.275  1.00 87.00  ? 41  ILE   N CA  1 
ATOM   23427 C  C   . ILE   N  14 41  ? 40.475  -125.606 72.383  1.00 85.21  ? 41  ILE   N C   1 
ATOM   23428 O  O   . ILE   N  14 41  ? 41.235  -124.929 71.666  1.00 80.83  ? 41  ILE   N O   1 
ATOM   23429 C  CB  . ILE   N  14 41  ? 38.476  -124.032 72.448  1.00 87.69  ? 41  ILE   N CB  1 
ATOM   23430 C  CG1 . ILE   N  14 41  ? 37.477  -123.279 73.333  1.00 91.31  ? 41  ILE   N CG1 1 
ATOM   23431 C  CG2 . ILE   N  14 41  ? 37.766  -124.899 71.417  1.00 86.20  ? 41  ILE   N CG2 1 
ATOM   23432 C  CD1 . ILE   N  14 41  ? 36.652  -122.242 72.598  1.00 90.14  ? 41  ILE   N CD1 1 
ATOM   23433 N  N   . TRP   N  14 42  ? 40.479  -126.937 72.444  1.00 83.02  ? 42  TRP   N N   1 
ATOM   23434 C  CA  . TRP   N  14 42  ? 41.372  -127.828 71.661  1.00 82.52  ? 42  TRP   N CA  1 
ATOM   23435 C  C   . TRP   N  14 42  ? 40.507  -128.775 70.826  1.00 81.40  ? 42  TRP   N C   1 
ATOM   23436 O  O   . TRP   N  14 42  ? 39.305  -128.904 71.134  1.00 82.44  ? 42  TRP   N O   1 
ATOM   23437 C  CB  . TRP   N  14 42  ? 42.307  -128.601 72.598  1.00 80.92  ? 42  TRP   N CB  1 
ATOM   23438 C  CG  . TRP   N  14 42  ? 43.350  -127.767 73.275  1.00 81.46  ? 42  TRP   N CG  1 
ATOM   23439 C  CD1 . TRP   N  14 42  ? 43.159  -126.721 74.131  1.00 82.31  ? 42  TRP   N CD1 1 
ATOM   23440 C  CD2 . TRP   N  14 42  ? 44.773  -127.943 73.174  1.00 80.56  ? 42  TRP   N CD2 1 
ATOM   23441 N  NE1 . TRP   N  14 42  ? 44.362  -126.226 74.556  1.00 83.12  ? 42  TRP   N NE1 1 
ATOM   23442 C  CE2 . TRP   N  14 42  ? 45.370  -126.956 73.986  1.00 82.03  ? 42  TRP   N CE2 1 
ATOM   23443 C  CE3 . TRP   N  14 42  ? 45.594  -128.830 72.473  1.00 80.77  ? 42  TRP   N CE3 1 
ATOM   23444 C  CZ2 . TRP   N  14 42  ? 46.752  -126.836 74.111  1.00 83.64  ? 42  TRP   N CZ2 1 
ATOM   23445 C  CZ3 . TRP   N  14 42  ? 46.960  -128.711 72.598  1.00 82.38  ? 42  TRP   N CZ3 1 
ATOM   23446 C  CH2 . TRP   N  14 42  ? 47.528  -127.728 73.408  1.00 84.09  ? 42  TRP   N CH2 1 
ATOM   23447 N  N   . CYS   N  14 43  ? 41.091  -129.412 69.811  1.00 83.09  ? 43  CYS   N N   1 
ATOM   23448 C  CA  . CYS   N  14 43  ? 40.388  -130.399 68.952  1.00 85.62  ? 43  CYS   N CA  1 
ATOM   23449 C  C   . CYS   N  14 43  ? 41.275  -131.627 68.715  1.00 86.43  ? 43  CYS   N C   1 
ATOM   23450 O  O   . CYS   N  14 43  ? 42.510  -131.516 68.859  1.00 86.92  ? 43  CYS   N O   1 
ATOM   23451 C  CB  . CYS   N  14 43  ? 39.957  -129.776 67.628  1.00 86.21  ? 43  CYS   N CB  1 
ATOM   23452 S  SG  . CYS   N  14 43  ? 41.326  -129.464 66.484  1.00 87.82  ? 43  CYS   N SG  1 
ATOM   23453 N  N   . CYS   N  14 44  ? 40.644  -132.755 68.382  1.00 87.77  ? 44  CYS   N N   1 
ATOM   23454 C  CA  . CYS   N  14 44  ? 41.292  -134.040 68.007  1.00 87.82  ? 44  CYS   N CA  1 
ATOM   23455 C  C   . CYS   N  14 44  ? 41.068  -134.286 66.513  1.00 83.25  ? 44  CYS   N C   1 
ATOM   23456 O  O   . CYS   N  14 44  ? 39.894  -134.310 66.090  1.00 75.06  ? 44  CYS   N O   1 
ATOM   23457 C  CB  . CYS   N  14 44  ? 40.718  -135.211 68.797  1.00 89.56  ? 44  CYS   N CB  1 
ATOM   23458 S  SG  . CYS   N  14 44  ? 40.887  -135.057 70.595  1.00 95.20  ? 44  CYS   N SG  1 
ATOM   23459 N  N   . ARG   N  14 45  ? 42.149  -134.465 65.749  1.00 82.04  ? 45  ARG   N N   1 
ATOM   23460 C  CA  . ARG   N  14 45  ? 42.094  -134.556 64.269  1.00 81.46  ? 45  ARG   N CA  1 
ATOM   23461 C  C   . ARG   N  14 45  ? 42.190  -136.018 63.822  1.00 82.09  ? 45  ARG   N C   1 
ATOM   23462 O  O   . ARG   N  14 45  ? 43.158  -136.708 64.211  1.00 82.76  ? 45  ARG   N O   1 
ATOM   23463 C  CB  . ARG   N  14 45  ? 43.210  -133.724 63.640  1.00 80.48  ? 45  ARG   N CB  1 
ATOM   23464 C  CG  . ARG   N  14 45  ? 43.076  -132.231 63.892  1.00 78.98  ? 45  ARG   N CG  1 
ATOM   23465 C  CD  . ARG   N  14 45  ? 44.180  -131.477 63.187  1.00 78.82  ? 45  ARG   N CD  1 
ATOM   23466 N  NE  . ARG   N  14 45  ? 45.484  -131.831 63.725  1.00 78.07  ? 45  ARG   N NE  1 
ATOM   23467 C  CZ  . ARG   N  14 45  ? 46.376  -132.628 63.145  1.00 77.56  ? 45  ARG   N CZ  1 
ATOM   23468 N  NH1 . ARG   N  14 45  ? 46.133  -133.179 61.967  1.00 79.87  ? 45  ARG   N NH1 1 
ATOM   23469 N  NH2 . ARG   N  14 45  ? 47.524  -132.871 63.753  1.00 80.95  ? 45  ARG   N NH2 1 
ATOM   23470 N  N   . SER   N  14 46  ? 41.209  -136.442 63.021  1.00 83.25  ? 46  SER   N N   1 
ATOM   23471 C  CA  . SER   N  14 46  ? 41.136  -137.756 62.335  1.00 81.25  ? 46  SER   N CA  1 
ATOM   23472 C  C   . SER   N  14 46  ? 40.817  -137.518 60.860  1.00 79.78  ? 46  SER   N C   1 
ATOM   23473 O  O   . SER   N  14 46  ? 40.120  -136.538 60.562  1.00 77.43  ? 46  SER   N O   1 
ATOM   23474 C  CB  . SER   N  14 46  ? 40.111  -138.653 62.963  1.00 82.11  ? 46  SER   N CB  1 
ATOM   23475 O  OG  . SER   N  14 46  ? 38.798  -138.300 62.565  1.00 86.70  ? 46  SER   N OG  1 
ATOM   23476 N  N   . GLY   N  14 47  ? 41.290  -138.404 59.985  1.00 80.02  ? 47  GLY   N N   1 
ATOM   23477 C  CA  . GLY   N  14 47  ? 41.097  -138.305 58.528  1.00 80.26  ? 47  GLY   N CA  1 
ATOM   23478 C  C   . GLY   N  14 47  ? 42.349  -137.776 57.855  1.00 80.04  ? 47  GLY   N C   1 
ATOM   23479 O  O   . GLY   N  14 47  ? 43.443  -137.961 58.420  1.00 81.15  ? 47  GLY   N O   1 
ATOM   23480 N  N   . SER   N  14 48  ? 42.199  -137.138 56.692  1.00 79.82  ? 48  SER   N N   1 
ATOM   23481 C  CA  . SER   N  14 48  ? 43.315  -136.558 55.898  1.00 82.74  ? 48  SER   N CA  1 
ATOM   23482 C  C   . SER   N  14 48  ? 44.035  -135.494 56.728  1.00 83.67  ? 48  SER   N C   1 
ATOM   23483 O  O   . SER   N  14 48  ? 43.387  -134.487 57.079  1.00 84.36  ? 48  SER   N O   1 
ATOM   23484 C  CB  . SER   N  14 48  ? 42.830  -135.965 54.608  1.00 84.18  ? 48  SER   N CB  1 
ATOM   23485 O  OG  . SER   N  14 48  ? 43.795  -135.061 54.087  1.00 86.31  ? 48  SER   N OG  1 
ATOM   23486 N  N   . ALA   N  14 49  ? 45.326  -135.700 57.007  1.00 86.87  ? 49  ALA   N N   1 
ATOM   23487 C  CA  . ALA   N  14 49  ? 46.176  -134.767 57.785  1.00 84.39  ? 49  ALA   N CA  1 
ATOM   23488 C  C   . ALA   N  14 49  ? 46.118  -133.382 57.133  1.00 80.94  ? 49  ALA   N C   1 
ATOM   23489 O  O   . ALA   N  14 49  ? 45.849  -132.411 57.851  1.00 82.06  ? 49  ALA   N O   1 
ATOM   23490 C  CB  . ALA   N  14 49  ? 47.592  -135.286 57.878  1.00 84.07  ? 49  ALA   N CB  1 
ATOM   23491 N  N   . ALA   N  14 50  ? 46.314  -133.309 55.814  1.00 79.20  ? 50  ALA   N N   1 
ATOM   23492 C  CA  . ALA   N  14 50  ? 46.319  -132.051 55.031  1.00 78.22  ? 50  ALA   N CA  1 
ATOM   23493 C  C   . ALA   N  14 50  ? 44.997  -131.306 55.240  1.00 78.68  ? 50  ALA   N C   1 
ATOM   23494 O  O   . ALA   N  14 50  ? 45.048  -130.096 55.520  1.00 79.13  ? 50  ALA   N O   1 
ATOM   23495 C  CB  . ALA   N  14 50  ? 46.556  -132.332 53.569  1.00 79.66  ? 50  ALA   N CB  1 
ATOM   23496 N  N   . ASP   N  14 51  ? 43.865  -132.004 55.116  1.00 77.47  ? 51  ASP   N N   1 
ATOM   23497 C  CA  . ASP   N  14 51  ? 42.509  -131.408 55.264  1.00 77.08  ? 51  ASP   N CA  1 
ATOM   23498 C  C   . ASP   N  14 51  ? 42.312  -130.939 56.712  1.00 75.12  ? 51  ASP   N C   1 
ATOM   23499 O  O   . ASP   N  14 51  ? 41.900  -129.786 56.890  1.00 71.71  ? 51  ASP   N O   1 
ATOM   23500 C  CB  . ASP   N  14 51  ? 41.411  -132.375 54.810  1.00 79.64  ? 51  ASP   N CB  1 
ATOM   23501 C  CG  . ASP   N  14 51  ? 41.367  -132.613 53.306  1.00 79.58  ? 51  ASP   N CG  1 
ATOM   23502 O  OD1 . ASP   N  14 51  ? 41.860  -131.751 52.555  1.00 79.54  ? 51  ASP   N OD1 1 
ATOM   23503 O  OD2 . ASP   N  14 51  ? 40.831  -133.660 52.896  1.00 86.59  ? 51  ASP   N OD2 1 
ATOM   23504 N  N   . THR   N  14 52  ? 42.608  -131.786 57.705  1.00 76.31  ? 52  THR   N N   1 
ATOM   23505 C  CA  . THR   N  14 52  ? 42.402  -131.483 59.150  1.00 75.69  ? 52  THR   N CA  1 
ATOM   23506 C  C   . THR   N  14 52  ? 43.308  -130.322 59.585  1.00 77.07  ? 52  THR   N C   1 
ATOM   23507 O  O   . THR   N  14 52  ? 42.818  -129.459 60.346  1.00 74.05  ? 52  THR   N O   1 
ATOM   23508 C  CB  . THR   N  14 52  ? 42.619  -132.716 60.035  1.00 77.33  ? 52  THR   N CB  1 
ATOM   23509 O  OG1 . THR   N  14 52  ? 43.934  -133.222 59.805  1.00 76.94  ? 52  THR   N OG1 1 
ATOM   23510 C  CG2 . THR   N  14 52  ? 41.593  -133.799 59.785  1.00 77.61  ? 52  THR   N CG2 1 
ATOM   23511 N  N   . GLN   N  14 53  ? 44.567  -130.302 59.132  1.00 75.34  ? 53  GLN   N N   1 
ATOM   23512 C  CA  . GLN   N  14 53  ? 45.548  -129.220 59.431  1.00 77.36  ? 53  GLN   N CA  1 
ATOM   23513 C  C   . GLN   N  14 53  ? 45.027  -127.880 58.893  1.00 77.98  ? 53  GLN   N C   1 
ATOM   23514 O  O   . GLN   N  14 53  ? 45.087  -126.882 59.639  1.00 81.41  ? 53  GLN   N O   1 
ATOM   23515 C  CB  . GLN   N  14 53  ? 46.918  -129.529 58.824  1.00 77.87  ? 53  GLN   N CB  1 
ATOM   23516 C  CG  . GLN   N  14 53  ? 47.717  -130.556 59.611  1.00 77.95  ? 53  GLN   N CG  1 
ATOM   23517 C  CD  . GLN   N  14 53  ? 49.144  -130.673 59.135  1.00 79.49  ? 53  GLN   N CD  1 
ATOM   23518 O  OE1 . GLN   N  14 53  ? 49.646  -129.839 58.382  1.00 80.20  ? 53  GLN   N OE1 1 
ATOM   23519 N  NE2 . GLN   N  14 53  ? 49.815  -131.723 59.579  1.00 81.15  ? 53  GLN   N NE2 1 
ATOM   23520 N  N   . ALA   N  14 54  ? 44.543  -127.868 57.646  1.00 76.32  ? 54  ALA   N N   1 
ATOM   23521 C  CA  . ALA   N  14 54  ? 44.024  -126.677 56.934  1.00 74.09  ? 54  ALA   N CA  1 
ATOM   23522 C  C   . ALA   N  14 54  ? 42.814  -126.095 57.677  1.00 76.06  ? 54  ALA   N C   1 
ATOM   23523 O  O   . ALA   N  14 54  ? 42.744  -124.857 57.797  1.00 76.22  ? 54  ALA   N O   1 
ATOM   23524 C  CB  . ALA   N  14 54  ? 43.667  -127.041 55.516  1.00 71.88  ? 54  ALA   N CB  1 
ATOM   23525 N  N   . ILE   N  14 55  ? 41.899  -126.950 58.147  1.00 75.77  ? 55  ILE   N N   1 
ATOM   23526 C  CA  . ILE   N  14 55  ? 40.644  -126.538 58.850  1.00 78.11  ? 55  ILE   N CA  1 
ATOM   23527 C  C   . ILE   N  14 55  ? 41.011  -125.919 60.204  1.00 78.78  ? 55  ILE   N C   1 
ATOM   23528 O  O   . ILE   N  14 55  ? 40.499  -124.819 60.496  1.00 78.50  ? 55  ILE   N O   1 
ATOM   23529 C  CB  . ILE   N  14 55  ? 39.666  -127.719 59.021  1.00 78.91  ? 55  ILE   N CB  1 
ATOM   23530 C  CG1 . ILE   N  14 55  ? 39.222  -128.299 57.677  1.00 79.94  ? 55  ILE   N CG1 1 
ATOM   23531 C  CG2 . ILE   N  14 55  ? 38.467  -127.310 59.865  1.00 80.33  ? 55  ILE   N CG2 1 
ATOM   23532 C  CD1 . ILE   N  14 55  ? 38.602  -129.674 57.786  1.00 80.34  ? 55  ILE   N CD1 1 
ATOM   23533 N  N   . ALA   N  14 56  ? 41.842  -126.608 60.998  1.00 79.33  ? 56  ALA   N N   1 
ATOM   23534 C  CA  . ALA   N  14 56  ? 42.268  -126.177 62.351  1.00 79.05  ? 56  ALA   N CA  1 
ATOM   23535 C  C   . ALA   N  14 56  ? 42.845  -124.760 62.267  1.00 79.44  ? 56  ALA   N C   1 
ATOM   23536 O  O   . ALA   N  14 56  ? 42.439  -123.912 63.085  1.00 82.76  ? 56  ALA   N O   1 
ATOM   23537 C  CB  . ALA   N  14 56  ? 43.270  -127.145 62.932  1.00 77.99  ? 56  ALA   N CB  1 
ATOM   23538 N  N   . ASP   N  14 57  ? 43.738  -124.522 61.299  1.00 79.27  ? 57  ASP   N N   1 
ATOM   23539 C  CA  . ASP   N  14 57  ? 44.401  -123.213 61.049  1.00 82.50  ? 57  ASP   N CA  1 
ATOM   23540 C  C   . ASP   N  14 57  ? 43.341  -122.124 60.827  1.00 82.35  ? 57  ASP   N C   1 
ATOM   23541 O  O   . ASP   N  14 57  ? 43.467  -121.049 61.455  1.00 80.79  ? 57  ASP   N O   1 
ATOM   23542 C  CB  . ASP   N  14 57  ? 45.366  -123.289 59.859  1.00 86.42  ? 57  ASP   N CB  1 
ATOM   23543 C  CG  . ASP   N  14 57  ? 46.662  -124.045 60.126  1.00 88.01  ? 57  ASP   N CG  1 
ATOM   23544 O  OD1 . ASP   N  14 57  ? 47.007  -124.228 61.312  1.00 89.93  ? 57  ASP   N OD1 1 
ATOM   23545 O  OD2 . ASP   N  14 57  ? 47.327  -124.438 59.141  1.00 89.37  ? 57  ASP   N OD2 1 
ATOM   23546 N  N   . ILE   N  14 58  ? 42.345  -122.388 59.972  1.00 80.49  ? 58  ILE   N N   1 
ATOM   23547 C  CA  . ILE   N  14 58  ? 41.254  -121.425 59.626  1.00 80.04  ? 58  ILE   N CA  1 
ATOM   23548 C  C   . ILE   N  14 58  ? 40.404  -121.155 60.874  1.00 82.44  ? 58  ILE   N C   1 
ATOM   23549 O  O   . ILE   N  14 58  ? 40.045  -119.985 61.090  1.00 88.01  ? 58  ILE   N O   1 
ATOM   23550 C  CB  . ILE   N  14 58  ? 40.395  -121.931 58.450  1.00 78.74  ? 58  ILE   N CB  1 
ATOM   23551 C  CG1 . ILE   N  14 58  ? 41.190  -121.948 57.142  1.00 80.31  ? 58  ILE   N CG1 1 
ATOM   23552 C  CG2 . ILE   N  14 58  ? 39.120  -121.110 58.315  1.00 77.35  ? 58  ILE   N CG2 1 
ATOM   23553 C  CD1 . ILE   N  14 58  ? 40.567  -122.795 56.057  1.00 80.44  ? 58  ILE   N CD1 1 
ATOM   23554 N  N   . VAL   N  14 59  ? 40.073  -122.192 61.647  1.00 79.73  ? 59  VAL   N N   1 
ATOM   23555 C  CA  . VAL   N  14 59  ? 39.268  -122.059 62.898  1.00 80.74  ? 59  VAL   N CA  1 
ATOM   23556 C  C   . VAL   N  14 59  ? 40.039  -121.178 63.887  1.00 81.10  ? 59  VAL   N C   1 
ATOM   23557 O  O   . VAL   N  14 59  ? 39.429  -120.240 64.434  1.00 81.65  ? 59  VAL   N O   1 
ATOM   23558 C  CB  . VAL   N  14 59  ? 38.926  -123.428 63.515  1.00 80.72  ? 59  VAL   N CB  1 
ATOM   23559 C  CG1 . VAL   N  14 59  ? 38.375  -123.287 64.928  1.00 81.97  ? 59  VAL   N CG1 1 
ATOM   23560 C  CG2 . VAL   N  14 59  ? 37.956  -124.209 62.642  1.00 81.36  ? 59  VAL   N CG2 1 
ATOM   23561 N  N   . GLN   N  14 60  ? 41.324  -121.474 64.108  1.00 80.91  ? 60  GLN   N N   1 
ATOM   23562 C  CA  . GLN   N  14 60  ? 42.194  -120.733 65.061  1.00 83.13  ? 60  GLN   N CA  1 
ATOM   23563 C  C   . GLN   N  14 60  ? 42.221  -119.249 64.677  1.00 84.84  ? 60  GLN   N C   1 
ATOM   23564 O  O   . GLN   N  14 60  ? 42.178  -118.405 65.596  1.00 86.45  ? 60  GLN   N O   1 
ATOM   23565 C  CB  . GLN   N  14 60  ? 43.611  -121.303 65.081  1.00 83.72  ? 60  GLN   N CB  1 
ATOM   23566 C  CG  . GLN   N  14 60  ? 44.462  -120.724 66.200  1.00 86.80  ? 60  GLN   N CG  1 
ATOM   23567 C  CD  . GLN   N  14 60  ? 45.886  -121.217 66.160  1.00 89.94  ? 60  GLN   N CD  1 
ATOM   23568 O  OE1 . GLN   N  14 60  ? 46.433  -121.513 65.100  1.00 92.70  ? 60  GLN   N OE1 1 
ATOM   23569 N  NE2 . GLN   N  14 60  ? 46.505  -121.297 67.328  1.00 92.45  ? 60  GLN   N NE2 1 
ATOM   23570 N  N   . TYR   N  14 61  ? 42.297  -118.954 63.374  1.00 84.27  ? 61  TYR   N N   1 
ATOM   23571 C  CA  . TYR   N  14 61  ? 42.238  -117.579 62.808  1.00 85.01  ? 61  TYR   N CA  1 
ATOM   23572 C  C   . TYR   N  14 61  ? 40.893  -116.933 63.164  1.00 82.31  ? 61  TYR   N C   1 
ATOM   23573 O  O   . TYR   N  14 61  ? 40.904  -115.801 63.660  1.00 86.08  ? 61  TYR   N O   1 
ATOM   23574 C  CB  . TYR   N  14 61  ? 42.464  -117.585 61.292  1.00 82.74  ? 61  TYR   N CB  1 
ATOM   23575 C  CG  . TYR   N  14 61  ? 41.846  -116.415 60.574  1.00 86.57  ? 61  TYR   N CG  1 
ATOM   23576 C  CD1 . TYR   N  14 61  ? 42.464  -115.174 60.561  1.00 90.36  ? 61  TYR   N CD1 1 
ATOM   23577 C  CD2 . TYR   N  14 61  ? 40.624  -116.536 59.932  1.00 87.92  ? 61  TYR   N CD2 1 
ATOM   23578 C  CE1 . TYR   N  14 61  ? 41.892  -114.086 59.920  1.00 93.79  ? 61  TYR   N CE1 1 
ATOM   23579 C  CE2 . TYR   N  14 61  ? 40.039  -115.459 59.284  1.00 92.47  ? 61  TYR   N CE2 1 
ATOM   23580 C  CZ  . TYR   N  14 61  ? 40.675  -114.229 59.278  1.00 91.90  ? 61  TYR   N CZ  1 
ATOM   23581 O  OH  . TYR   N  14 61  ? 40.111  -113.162 58.644  1.00 94.23  ? 61  TYR   N OH  1 
ATOM   23582 N  N   . HIS   N  14 62  ? 39.780  -117.628 62.920  1.00 80.42  ? 62  HIS   N N   1 
ATOM   23583 C  CA  . HIS   N  14 62  ? 38.399  -117.127 63.165  1.00 83.42  ? 62  HIS   N CA  1 
ATOM   23584 C  C   . HIS   N  14 62  ? 38.189  -116.810 64.650  1.00 83.90  ? 62  HIS   N C   1 
ATOM   23585 O  O   . HIS   N  14 62  ? 37.573  -115.768 64.936  1.00 88.00  ? 62  HIS   N O   1 
ATOM   23586 C  CB  . HIS   N  14 62  ? 37.345  -118.128 62.675  1.00 84.66  ? 62  HIS   N CB  1 
ATOM   23587 C  CG  . HIS   N  14 62  ? 36.838  -117.839 61.304  1.00 88.95  ? 62  HIS   N CG  1 
ATOM   23588 N  ND1 . HIS   N  14 62  ? 35.812  -116.943 61.073  1.00 92.17  ? 62  HIS   N ND1 1 
ATOM   23589 C  CD2 . HIS   N  14 62  ? 37.202  -118.322 60.096  1.00 89.95  ? 62  HIS   N CD2 1 
ATOM   23590 C  CE1 . HIS   N  14 62  ? 35.566  -116.886 59.780  1.00 92.06  ? 62  HIS   N CE1 1 
ATOM   23591 N  NE2 . HIS   N  14 62  ? 36.406  -117.723 59.158  1.00 90.03  ? 62  HIS   N NE2 1 
ATOM   23592 N  N   . LEU   N  14 63  ? 38.652  -117.682 65.552  1.00 84.07  ? 63  LEU   N N   1 
ATOM   23593 C  CA  . LEU   N  14 63  ? 38.483  -117.525 67.024  1.00 87.05  ? 63  LEU   N CA  1 
ATOM   23594 C  C   . LEU   N  14 63  ? 39.405  -116.413 67.548  1.00 89.09  ? 63  LEU   N C   1 
ATOM   23595 O  O   . LEU   N  14 63  ? 39.025  -115.753 68.536  1.00 89.02  ? 63  LEU   N O   1 
ATOM   23596 C  CB  . LEU   N  14 63  ? 38.768  -118.859 67.724  1.00 86.81  ? 63  LEU   N CB  1 
ATOM   23597 C  CG  . LEU   N  14 63  ? 37.823  -120.015 67.390  1.00 84.58  ? 63  LEU   N CG  1 
ATOM   23598 C  CD1 . LEU   N  14 63  ? 38.195  -121.249 68.198  1.00 84.04  ? 63  LEU   N CD1 1 
ATOM   23599 C  CD2 . LEU   N  14 63  ? 36.366  -119.645 67.640  1.00 81.84  ? 63  LEU   N CD2 1 
ATOM   23600 N  N   . GLU   N  14 64  ? 40.569  -116.215 66.921  1.00 90.02  ? 64  GLU   N N   1 
ATOM   23601 C  CA  . GLU   N  14 64  ? 41.497  -115.093 67.231  1.00 91.09  ? 64  GLU   N CA  1 
ATOM   23602 C  C   . GLU   N  14 64  ? 40.800  -113.766 66.906  1.00 91.90  ? 64  GLU   N C   1 
ATOM   23603 O  O   . GLU   N  14 64  ? 40.849  -112.853 67.753  1.00 94.81  ? 64  GLU   N O   1 
ATOM   23604 C  CB  . GLU   N  14 64  ? 42.808  -115.241 66.455  1.00 94.75  ? 64  GLU   N CB  1 
ATOM   23605 C  CG  . GLU   N  14 64  ? 43.829  -114.160 66.773  1.00 97.29  ? 64  GLU   N CG  1 
ATOM   23606 C  CD  . GLU   N  14 64  ? 45.278  -114.570 66.560  1.00 101.73 ? 64  GLU   N CD  1 
ATOM   23607 O  OE1 . GLU   N  14 64  ? 46.000  -113.848 65.840  1.00 102.47 ? 64  GLU   N OE1 1 
ATOM   23608 O  OE2 . GLU   N  14 64  ? 45.687  -115.606 67.126  1.00 105.25 ? 64  GLU   N OE2 1 
ATOM   23609 N  N   . LEU   N  14 65  ? 40.164  -113.677 65.733  1.00 86.95  ? 65  LEU   N N   1 
ATOM   23610 C  CA  . LEU   N  14 65  ? 39.456  -112.459 65.258  1.00 87.45  ? 65  LEU   N CA  1 
ATOM   23611 C  C   . LEU   N  14 65  ? 38.169  -112.265 66.069  1.00 86.13  ? 65  LEU   N C   1 
ATOM   23612 O  O   . LEU   N  14 65  ? 37.823  -111.103 66.337  1.00 87.94  ? 65  LEU   N O   1 
ATOM   23613 C  CB  . LEU   N  14 65  ? 39.175  -112.584 63.756  1.00 88.87  ? 65  LEU   N CB  1 
ATOM   23614 C  CG  . LEU   N  14 65  ? 38.545  -111.361 63.087  1.00 91.85  ? 65  LEU   N CG  1 
ATOM   23615 C  CD1 . LEU   N  14 65  ? 39.360  -110.098 63.341  1.00 94.89  ? 65  LEU   N CD1 1 
ATOM   23616 C  CD2 . LEU   N  14 65  ? 38.378  -111.585 61.592  1.00 92.46  ? 65  LEU   N CD2 1 
ATOM   23617 N  N   . TYR   N  14 66  ? 37.496  -113.355 66.454  1.00 84.40  ? 66  TYR   N N   1 
ATOM   23618 C  CA  . TYR   N  14 66  ? 36.321  -113.344 67.367  1.00 85.83  ? 66  TYR   N CA  1 
ATOM   23619 C  C   . TYR   N  14 66  ? 36.732  -112.702 68.694  1.00 88.78  ? 66  TYR   N C   1 
ATOM   23620 O  O   . TYR   N  14 66  ? 36.067  -111.743 69.131  1.00 90.53  ? 66  TYR   N O   1 
ATOM   23621 C  CB  . TYR   N  14 66  ? 35.783  -114.759 67.607  1.00 84.57  ? 66  TYR   N CB  1 
ATOM   23622 C  CG  . TYR   N  14 66  ? 34.542  -114.830 68.463  1.00 82.14  ? 66  TYR   N CG  1 
ATOM   23623 C  CD1 . TYR   N  14 66  ? 34.616  -114.767 69.846  1.00 82.94  ? 66  TYR   N CD1 1 
ATOM   23624 C  CD2 . TYR   N  14 66  ? 33.287  -114.959 67.891  1.00 81.74  ? 66  TYR   N CD2 1 
ATOM   23625 C  CE1 . TYR   N  14 66  ? 33.479  -114.827 70.636  1.00 84.70  ? 66  TYR   N CE1 1 
ATOM   23626 C  CE2 . TYR   N  14 66  ? 32.139  -115.021 68.667  1.00 82.98  ? 66  TYR   N CE2 1 
ATOM   23627 C  CZ  . TYR   N  14 66  ? 32.234  -114.956 70.046  1.00 84.55  ? 66  TYR   N CZ  1 
ATOM   23628 O  OH  . TYR   N  14 66  ? 31.106  -115.014 70.814  1.00 85.89  ? 66  TYR   N OH  1 
ATOM   23629 N  N   . THR   N  14 67  ? 37.798  -113.228 69.306  1.00 89.55  ? 67  THR   N N   1 
ATOM   23630 C  CA  . THR   N  14 67  ? 38.321  -112.799 70.631  1.00 93.73  ? 67  THR   N CA  1 
ATOM   23631 C  C   . THR   N  14 67  ? 38.659  -111.306 70.607  1.00 94.09  ? 67  THR   N C   1 
ATOM   23632 O  O   . THR   N  14 67  ? 38.308  -110.624 71.581  1.00 97.10  ? 67  THR   N O   1 
ATOM   23633 C  CB  . THR   N  14 67  ? 39.545  -113.618 71.054  1.00 94.12  ? 67  THR   N CB  1 
ATOM   23634 O  OG1 . THR   N  14 67  ? 39.193  -114.996 70.944  1.00 95.87  ? 67  THR   N OG1 1 
ATOM   23635 C  CG2 . THR   N  14 67  ? 39.995  -113.308 72.464  1.00 97.62  ? 67  THR   N CG2 1 
ATOM   23636 N  N   . SER   N  14 68  ? 39.313  -110.832 69.541  1.00 96.02  ? 68  SER   N N   1 
ATOM   23637 C  CA  . SER   N  14 68  ? 39.691  -109.407 69.336  1.00 98.33  ? 68  SER   N CA  1 
ATOM   23638 C  C   . SER   N  14 68  ? 38.469  -108.497 69.515  1.00 95.50  ? 68  SER   N C   1 
ATOM   23639 O  O   . SER   N  14 68  ? 38.640  -107.389 70.060  1.00 98.89  ? 68  SER   N O   1 
ATOM   23640 C  CB  . SER   N  14 68  ? 40.324  -109.191 67.983  1.00 100.51 ? 68  SER   N CB  1 
ATOM   23641 O  OG  . SER   N  14 68  ? 41.645  -109.709 67.950  1.00 104.76 ? 68  SER   N OG  1 
ATOM   23642 N  N   . GLN   N  14 69  ? 37.289  -108.949 69.077  1.00 93.66  ? 69  GLN   N N   1 
ATOM   23643 C  CA  . GLN   N  14 69  ? 36.055  -108.123 68.995  1.00 93.50  ? 69  GLN   N CA  1 
ATOM   23644 C  C   . GLN   N  14 69  ? 35.127  -108.403 70.182  1.00 94.46  ? 69  GLN   N C   1 
ATOM   23645 O  O   . GLN   N  14 69  ? 34.631  -107.422 70.768  1.00 96.69  ? 69  GLN   N O   1 
ATOM   23646 C  CB  . GLN   N  14 69  ? 35.344  -108.387 67.668  1.00 93.21  ? 69  GLN   N CB  1 
ATOM   23647 C  CG  . GLN   N  14 69  ? 36.218  -108.094 66.458  1.00 93.33  ? 69  GLN   N CG  1 
ATOM   23648 C  CD  . GLN   N  14 69  ? 35.467  -108.253 65.160  1.00 94.30  ? 69  GLN   N CD  1 
ATOM   23649 O  OE1 . GLN   N  14 69  ? 34.428  -107.633 64.943  1.00 93.70  ? 69  GLN   N OE1 1 
ATOM   23650 N  NE2 . GLN   N  14 69  ? 35.998  -109.083 64.277  1.00 93.82  ? 69  GLN   N NE2 1 
ATOM   23651 N  N   . TYR   N  14 70  ? 34.897  -109.676 70.523  1.00 93.60  ? 70  TYR   N N   1 
ATOM   23652 C  CA  . TYR   N  14 70  ? 33.802  -110.108 71.435  1.00 97.89  ? 70  TYR   N CA  1 
ATOM   23653 C  C   . TYR   N  14 70  ? 34.327  -110.908 72.635  1.00 98.09  ? 70  TYR   N C   1 
ATOM   23654 O  O   . TYR   N  14 70  ? 33.488  -111.506 73.341  1.00 101.68 ? 70  TYR   N O   1 
ATOM   23655 C  CB  . TYR   N  14 70  ? 32.783  -110.955 70.671  1.00 96.64  ? 70  TYR   N CB  1 
ATOM   23656 C  CG  . TYR   N  14 70  ? 32.561  -110.534 69.242  1.00 97.69  ? 70  TYR   N CG  1 
ATOM   23657 C  CD1 . TYR   N  14 70  ? 32.061  -109.280 68.934  1.00 98.65  ? 70  TYR   N CD1 1 
ATOM   23658 C  CD2 . TYR   N  14 70  ? 32.852  -111.391 68.193  1.00 97.51  ? 70  TYR   N CD2 1 
ATOM   23659 C  CE1 . TYR   N  14 70  ? 31.853  -108.888 67.621  1.00 98.40  ? 70  TYR   N CE1 1 
ATOM   23660 C  CE2 . TYR   N  14 70  ? 32.654  -111.015 66.875  1.00 96.29  ? 70  TYR   N CE2 1 
ATOM   23661 C  CZ  . TYR   N  14 70  ? 32.150  -109.761 66.588  1.00 96.58  ? 70  TYR   N CZ  1 
ATOM   23662 O  OH  . TYR   N  14 70  ? 31.952  -109.406 65.287  1.00 98.11  ? 70  TYR   N OH  1 
ATOM   23663 N  N   . GLY   N  14 71  ? 35.644  -110.923 72.868  1.00 100.39 ? 71  GLY   N N   1 
ATOM   23664 C  CA  . GLY   N  14 71  ? 36.264  -111.654 73.991  1.00 101.98 ? 71  GLY   N CA  1 
ATOM   23665 C  C   . GLY   N  14 71  ? 36.203  -113.157 73.780  1.00 98.82  ? 71  GLY   N C   1 
ATOM   23666 O  O   . GLY   N  14 71  ? 36.016  -113.584 72.623  1.00 94.52  ? 71  GLY   N O   1 
ATOM   23667 N  N   . THR   N  14 72  ? 36.335  -113.936 74.859  1.00 100.05 ? 72  THR   N N   1 
ATOM   23668 C  CA  . THR   N  14 72  ? 36.493  -115.414 74.806  1.00 95.38  ? 72  THR   N CA  1 
ATOM   23669 C  C   . THR   N  14 72  ? 35.258  -116.036 74.160  1.00 95.26  ? 72  THR   N C   1 
ATOM   23670 O  O   . THR   N  14 72  ? 34.136  -115.774 74.591  1.00 95.20  ? 72  THR   N O   1 
ATOM   23671 C  CB  . THR   N  14 72  ? 36.751  -116.017 76.191  1.00 96.70  ? 72  THR   N CB  1 
ATOM   23672 O  OG1 . THR   N  14 72  ? 37.790  -115.264 76.817  1.00 95.84  ? 72  THR   N OG1 1 
ATOM   23673 C  CG2 . THR   N  14 72  ? 37.149  -117.475 76.119  1.00 95.44  ? 72  THR   N CG2 1 
ATOM   23674 N  N   . PRO   N  14 73  ? 35.436  -116.868 73.105  1.00 94.78  ? 73  PRO   N N   1 
ATOM   23675 C  CA  . PRO   N  14 73  ? 34.329  -117.605 72.497  1.00 92.58  ? 73  PRO   N CA  1 
ATOM   23676 C  C   . PRO   N  14 73  ? 33.938  -118.835 73.327  1.00 91.28  ? 73  PRO   N C   1 
ATOM   23677 O  O   . PRO   N  14 73  ? 34.793  -119.380 74.003  1.00 89.83  ? 73  PRO   N O   1 
ATOM   23678 C  CB  . PRO   N  14 73  ? 34.904  -118.045 71.143  1.00 90.85  ? 73  PRO   N CB  1 
ATOM   23679 C  CG  . PRO   N  14 73  ? 36.382  -118.220 71.421  1.00 90.96  ? 73  PRO   N CG  1 
ATOM   23680 C  CD  . PRO   N  14 73  ? 36.719  -117.148 72.438  1.00 92.90  ? 73  PRO   N CD  1 
ATOM   23681 N  N   . SER   N  14 74  ? 32.671  -119.246 73.242  1.00 94.17  ? 74  SER   N N   1 
ATOM   23682 C  CA  . SER   N  14 74  ? 32.152  -120.489 73.868  1.00 95.24  ? 74  SER   N CA  1 
ATOM   23683 C  C   . SER   N  14 74  ? 32.671  -121.693 73.077  1.00 93.68  ? 74  SER   N C   1 
ATOM   23684 O  O   . SER   N  14 74  ? 33.006  -121.522 71.889  1.00 91.18  ? 74  SER   N O   1 
ATOM   23685 C  CB  . SER   N  14 74  ? 30.643  -120.483 73.959  1.00 97.13  ? 74  SER   N CB  1 
ATOM   23686 O  OG  . SER   N  14 74  ? 30.044  -120.578 72.674  1.00 97.86  ? 74  SER   N OG  1 
ATOM   23687 N  N   . THR   N  14 75  ? 32.758  -122.859 73.718  1.00 94.00  ? 75  THR   N N   1 
ATOM   23688 C  CA  . THR   N  14 75  ? 33.143  -124.133 73.059  1.00 95.21  ? 75  THR   N CA  1 
ATOM   23689 C  C   . THR   N  14 75  ? 32.162  -124.402 71.913  1.00 91.67  ? 75  THR   N C   1 
ATOM   23690 O  O   . THR   N  14 75  ? 32.627  -124.754 70.812  1.00 90.60  ? 75  THR   N O   1 
ATOM   23691 C  CB  . THR   N  14 75  ? 33.196  -125.293 74.060  1.00 98.42  ? 75  THR   N CB  1 
ATOM   23692 O  OG1 . THR   N  14 75  ? 34.000  -124.885 75.169  1.00 101.23 ? 75  THR   N OG1 1 
ATOM   23693 C  CG2 . THR   N  14 75  ? 33.746  -126.559 73.439  1.00 98.29  ? 75  THR   N CG2 1 
ATOM   23694 N  N   . GLU   N  14 76  ? 30.861  -124.209 72.164  1.00 91.45  ? 76  GLU   N N   1 
ATOM   23695 C  CA  . GLU   N  14 76  ? 29.774  -124.365 71.160  1.00 90.44  ? 76  GLU   N CA  1 
ATOM   23696 C  C   . GLU   N  14 76  ? 30.110  -123.551 69.905  1.00 88.67  ? 76  GLU   N C   1 
ATOM   23697 O  O   . GLU   N  14 76  ? 30.001  -124.110 68.800  1.00 83.95  ? 76  GLU   N O   1 
ATOM   23698 C  CB  . GLU   N  14 76  ? 28.428  -123.931 71.744  1.00 96.30  ? 76  GLU   N CB  1 
ATOM   23699 C  CG  . GLU   N  14 76  ? 27.256  -124.207 70.818  1.00 98.78  ? 76  GLU   N CG  1 
ATOM   23700 C  CD  . GLU   N  14 76  ? 25.890  -123.890 71.402  1.00 102.97 ? 76  GLU   N CD  1 
ATOM   23701 O  OE1 . GLU   N  14 76  ? 24.982  -124.742 71.272  1.00 106.15 ? 76  GLU   N OE1 1 
ATOM   23702 O  OE2 . GLU   N  14 76  ? 25.733  -122.791 71.976  1.00 105.58 ? 76  GLU   N OE2 1 
ATOM   23703 N  N   . THR   N  14 77  ? 30.507  -122.285 70.070  1.00 85.47  ? 77  THR   N N   1 
ATOM   23704 C  CA  . THR   N  14 77  ? 30.873  -121.372 68.952  1.00 86.64  ? 77  THR   N CA  1 
ATOM   23705 C  C   . THR   N  14 77  ? 32.000  -122.016 68.134  1.00 84.59  ? 77  THR   N C   1 
ATOM   23706 O  O   . THR   N  14 77  ? 31.865  -122.075 66.899  1.00 82.99  ? 77  THR   N O   1 
ATOM   23707 C  CB  . THR   N  14 77  ? 31.260  -119.971 69.449  1.00 87.29  ? 77  THR   N CB  1 
ATOM   23708 O  OG1 . THR   N  14 77  ? 30.110  -119.345 70.020  1.00 89.37  ? 77  THR   N OG1 1 
ATOM   23709 C  CG2 . THR   N  14 77  ? 31.799  -119.084 68.347  1.00 87.27  ? 77  THR   N CG2 1 
ATOM   23710 N  N   . ALA   N  14 78  ? 33.058  -122.489 68.798  1.00 82.24  ? 78  ALA   N N   1 
ATOM   23711 C  CA  . ALA   N  14 78  ? 34.245  -123.102 68.157  1.00 83.64  ? 78  ALA   N CA  1 
ATOM   23712 C  C   . ALA   N  14 78  ? 33.808  -124.303 67.309  1.00 82.91  ? 78  ALA   N C   1 
ATOM   23713 O  O   . ALA   N  14 78  ? 34.287  -124.422 66.163  1.00 86.14  ? 78  ALA   N O   1 
ATOM   23714 C  CB  . ALA   N  14 78  ? 35.260  -123.498 69.200  1.00 83.31  ? 78  ALA   N CB  1 
ATOM   23715 N  N   . ALA   N  14 79  ? 32.920  -125.145 67.848  1.00 82.18  ? 79  ALA   N N   1 
ATOM   23716 C  CA  . ALA   N  14 79  ? 32.370  -126.347 67.176  1.00 81.22  ? 79  ALA   N CA  1 
ATOM   23717 C  C   . ALA   N  14 79  ? 31.537  -125.933 65.955  1.00 79.12  ? 79  ALA   N C   1 
ATOM   23718 O  O   . ALA   N  14 79  ? 31.569  -126.656 64.945  1.00 78.49  ? 79  ALA   N O   1 
ATOM   23719 C  CB  . ALA   N  14 79  ? 31.556  -127.161 68.153  1.00 81.90  ? 79  ALA   N CB  1 
ATOM   23720 N  N   . SER   N  14 80  ? 30.825  -124.806 66.041  1.00 78.30  ? 80  SER   N N   1 
ATOM   23721 C  CA  . SER   N  14 80  ? 29.976  -124.258 64.950  1.00 76.83  ? 80  SER   N CA  1 
ATOM   23722 C  C   . SER   N  14 80  ? 30.852  -123.813 63.772  1.00 76.25  ? 80  SER   N C   1 
ATOM   23723 O  O   . SER   N  14 80  ? 30.417  -123.989 62.619  1.00 75.15  ? 80  SER   N O   1 
ATOM   23724 C  CB  . SER   N  14 80  ? 29.109  -123.129 65.449  1.00 75.59  ? 80  SER   N CB  1 
ATOM   23725 O  OG  . SER   N  14 80  ? 28.264  -122.641 64.418  1.00 72.88  ? 80  SER   N OG  1 
ATOM   23726 N  N   . VAL   N  14 81  ? 32.036  -123.261 64.047  1.00 76.28  ? 81  VAL   N N   1 
ATOM   23727 C  CA  . VAL   N  14 81  ? 32.987  -122.779 63.000  1.00 79.27  ? 81  VAL   N CA  1 
ATOM   23728 C  C   . VAL   N  14 81  ? 33.609  -123.998 62.306  1.00 79.85  ? 81  VAL   N C   1 
ATOM   23729 O  O   . VAL   N  14 81  ? 33.750  -123.951 61.067  1.00 83.13  ? 81  VAL   N O   1 
ATOM   23730 C  CB  . VAL   N  14 81  ? 34.057  -121.833 63.578  1.00 80.84  ? 81  VAL   N CB  1 
ATOM   23731 C  CG1 . VAL   N  14 81  ? 35.083  -121.420 62.531  1.00 81.54  ? 81  VAL   N CG1 1 
ATOM   23732 C  CG2 . VAL   N  14 81  ? 33.428  -120.599 64.207  1.00 81.58  ? 81  VAL   N CG2 1 
ATOM   23733 N  N   . PHE   N  14 82  ? 33.968  -125.039 63.068  1.00 79.64  ? 82  PHE   N N   1 
ATOM   23734 C  CA  . PHE   N  14 82  ? 34.437  -126.346 62.532  1.00 78.61  ? 82  PHE   N CA  1 
ATOM   23735 C  C   . PHE   N  14 82  ? 33.356  -126.920 61.614  1.00 76.88  ? 82  PHE   N C   1 
ATOM   23736 O  O   . PHE   N  14 82  ? 33.662  -127.202 60.442  1.00 75.69  ? 82  PHE   N O   1 
ATOM   23737 C  CB  . PHE   N  14 82  ? 34.769  -127.340 63.649  1.00 76.81  ? 82  PHE   N CB  1 
ATOM   23738 C  CG  . PHE   N  14 82  ? 36.206  -127.319 64.103  1.00 74.67  ? 82  PHE   N CG  1 
ATOM   23739 C  CD1 . PHE   N  14 82  ? 37.212  -127.800 63.281  1.00 73.75  ? 82  PHE   N CD1 1 
ATOM   23740 C  CD2 . PHE   N  14 82  ? 36.553  -126.821 65.349  1.00 75.86  ? 82  PHE   N CD2 1 
ATOM   23741 C  CE1 . PHE   N  14 82  ? 38.535  -127.781 63.694  1.00 75.65  ? 82  PHE   N CE1 1 
ATOM   23742 C  CE2 . PHE   N  14 82  ? 37.876  -126.805 65.761  1.00 77.26  ? 82  PHE   N CE2 1 
ATOM   23743 C  CZ  . PHE   N  14 82  ? 38.864  -127.286 64.934  1.00 77.03  ? 82  PHE   N CZ  1 
ATOM   23744 N  N   . LYS   N  14 83  ? 32.135  -127.063 62.140  1.00 79.39  ? 83  LYS   N N   1 
ATOM   23745 C  CA  . LYS   N  14 83  ? 30.954  -127.610 61.417  1.00 81.33  ? 83  LYS   N CA  1 
ATOM   23746 C  C   . LYS   N  14 83  ? 30.771  -126.866 60.091  1.00 84.07  ? 83  LYS   N C   1 
ATOM   23747 O  O   . LYS   N  14 83  ? 30.593  -127.533 59.055  1.00 82.73  ? 83  LYS   N O   1 
ATOM   23748 C  CB  . LYS   N  14 83  ? 29.680  -127.478 62.259  1.00 83.15  ? 83  LYS   N CB  1 
ATOM   23749 C  CG  . LYS   N  14 83  ? 28.390  -127.872 61.545  1.00 83.95  ? 83  LYS   N CG  1 
ATOM   23750 C  CD  . LYS   N  14 83  ? 27.242  -126.931 61.819  1.00 87.33  ? 83  LYS   N CD  1 
ATOM   23751 C  CE  . LYS   N  14 83  ? 27.363  -125.641 61.036  1.00 89.18  ? 83  LYS   N CE  1 
ATOM   23752 N  NZ  . LYS   N  14 83  ? 26.643  -124.526 61.694  1.00 91.78  ? 83  LYS   N NZ  1 
ATOM   23753 N  N   . GLU   N  14 84  ? 30.800  -125.533 60.134  1.00 86.05  ? 84  GLU   N N   1 
ATOM   23754 C  CA  . GLU   N  14 84  ? 30.527  -124.667 58.958  1.00 88.29  ? 84  GLU   N CA  1 
ATOM   23755 C  C   . GLU   N  14 84  ? 31.504  -125.019 57.830  1.00 86.74  ? 84  GLU   N C   1 
ATOM   23756 O  O   . GLU   N  14 84  ? 31.047  -125.131 56.678  1.00 86.59  ? 84  GLU   N O   1 
ATOM   23757 C  CB  . GLU   N  14 84  ? 30.622  -123.190 59.340  1.00 92.16  ? 84  GLU   N CB  1 
ATOM   23758 C  CG  . GLU   N  14 84  ? 29.854  -122.280 58.398  1.00 96.32  ? 84  GLU   N CG  1 
ATOM   23759 C  CD  . GLU   N  14 84  ? 28.342  -122.333 58.547  1.00 98.00  ? 84  GLU   N CD  1 
ATOM   23760 O  OE1 . GLU   N  14 84  ? 27.665  -121.481 57.944  1.00 105.18 ? 84  GLU   N OE1 1 
ATOM   23761 O  OE2 . GLU   N  14 84  ? 27.842  -123.221 59.266  1.00 100.49 ? 84  GLU   N OE2 1 
ATOM   23762 N  N   . LEU   N  14 85  ? 32.788  -125.197 58.154  1.00 86.19  ? 85  LEU   N N   1 
ATOM   23763 C  CA  . LEU   N  14 85  ? 33.849  -125.563 57.177  1.00 86.82  ? 85  LEU   N CA  1 
ATOM   23764 C  C   . LEU   N  14 85  ? 33.615  -126.994 56.678  1.00 88.49  ? 85  LEU   N C   1 
ATOM   23765 O  O   . LEU   N  14 85  ? 33.622  -127.196 55.446  1.00 88.49  ? 85  LEU   N O   1 
ATOM   23766 C  CB  . LEU   N  14 85  ? 35.226  -125.431 57.837  1.00 87.54  ? 85  LEU   N CB  1 
ATOM   23767 C  CG  . LEU   N  14 85  ? 35.624  -124.018 58.261  1.00 87.65  ? 85  LEU   N CG  1 
ATOM   23768 C  CD1 . LEU   N  14 85  ? 36.858  -124.046 59.151  1.00 91.66  ? 85  LEU   N CD1 1 
ATOM   23769 C  CD2 . LEU   N  14 85  ? 35.864  -123.135 57.051  1.00 86.91  ? 85  LEU   N CD2 1 
ATOM   23770 N  N   . CYS   N  14 86  ? 33.408  -127.943 57.600  1.00 86.50  ? 86  CYS   N N   1 
ATOM   23771 C  CA  . CYS   N  14 86  ? 33.269  -129.396 57.306  1.00 86.36  ? 86  CYS   N CA  1 
ATOM   23772 C  C   . CYS   N  14 86  ? 31.997  -129.660 56.487  1.00 84.77  ? 86  CYS   N C   1 
ATOM   23773 O  O   . CYS   N  14 86  ? 32.072  -130.475 55.545  1.00 91.93  ? 86  CYS   N O   1 
ATOM   23774 C  CB  . CYS   N  14 86  ? 33.284  -130.223 58.587  1.00 86.39  ? 86  CYS   N CB  1 
ATOM   23775 S  SG  . CYS   N  14 86  ? 34.881  -130.160 59.441  1.00 87.96  ? 86  CYS   N SG  1 
ATOM   23776 N  N   . TYR   N  14 87  ? 30.884  -128.995 56.812  1.00 79.06  ? 87  TYR   N N   1 
ATOM   23777 C  CA  . TYR   N  14 87  ? 29.560  -129.228 56.174  1.00 78.19  ? 87  TYR   N CA  1 
ATOM   23778 C  C   . TYR   N  14 87  ? 29.539  -128.650 54.756  1.00 80.16  ? 87  TYR   N C   1 
ATOM   23779 O  O   . TYR   N  14 87  ? 29.066  -129.339 53.839  1.00 78.60  ? 87  TYR   N O   1 
ATOM   23780 C  CB  . TYR   N  14 87  ? 28.419  -128.622 56.993  1.00 78.68  ? 87  TYR   N CB  1 
ATOM   23781 C  CG  . TYR   N  14 87  ? 27.067  -128.753 56.338  1.00 79.20  ? 87  TYR   N CG  1 
ATOM   23782 C  CD1 . TYR   N  14 87  ? 26.449  -129.986 56.223  1.00 80.02  ? 87  TYR   N CD1 1 
ATOM   23783 C  CD2 . TYR   N  14 87  ? 26.413  -127.653 55.810  1.00 78.73  ? 87  TYR   N CD2 1 
ATOM   23784 C  CE1 . TYR   N  14 87  ? 25.211  -130.122 55.615  1.00 81.30  ? 87  TYR   N CE1 1 
ATOM   23785 C  CE2 . TYR   N  14 87  ? 25.173  -127.770 55.203  1.00 80.67  ? 87  TYR   N CE2 1 
ATOM   23786 C  CZ  . TYR   N  14 87  ? 24.569  -129.010 55.104  1.00 81.29  ? 87  TYR   N CZ  1 
ATOM   23787 O  OH  . TYR   N  14 87  ? 23.349  -129.133 54.503  1.00 82.37  ? 87  TYR   N OH  1 
ATOM   23788 N  N   . GLU   N  14 88  ? 30.009  -127.412 54.591  1.00 81.01  ? 88  GLU   N N   1 
ATOM   23789 C  CA  . GLU   N  14 88  ? 29.934  -126.664 53.307  1.00 83.63  ? 88  GLU   N CA  1 
ATOM   23790 C  C   . GLU   N  14 88  ? 30.973  -127.197 52.313  1.00 82.22  ? 88  GLU   N C   1 
ATOM   23791 O  O   . GLU   N  14 88  ? 30.805  -126.926 51.113  1.00 82.80  ? 88  GLU   N O   1 
ATOM   23792 C  CB  . GLU   N  14 88  ? 30.126  -125.162 53.535  1.00 84.83  ? 88  GLU   N CB  1 
ATOM   23793 C  CG  . GLU   N  14 88  ? 28.982  -124.499 54.290  1.00 87.23  ? 88  GLU   N CG  1 
ATOM   23794 C  CD  . GLU   N  14 88  ? 27.623  -124.544 53.609  1.00 89.70  ? 88  GLU   N CD  1 
ATOM   23795 O  OE1 . GLU   N  14 88  ? 27.583  -124.676 52.368  1.00 93.34  ? 88  GLU   N OE1 1 
ATOM   23796 O  OE2 . GLU   N  14 88  ? 26.603  -124.444 54.324  1.00 91.70  ? 88  GLU   N OE2 1 
ATOM   23797 N  N   . ASN   N  14 89  ? 32.000  -127.916 52.780  1.00 83.70  ? 89  ASN   N N   1 
ATOM   23798 C  CA  . ASN   N  14 89  ? 33.080  -128.470 51.917  1.00 86.63  ? 89  ASN   N CA  1 
ATOM   23799 C  C   . ASN   N  14 89  ? 33.126  -129.997 52.042  1.00 90.48  ? 89  ASN   N C   1 
ATOM   23800 O  O   . ASN   N  14 89  ? 34.221  -130.568 51.861  1.00 98.32  ? 89  ASN   N O   1 
ATOM   23801 C  CB  . ASN   N  14 89  ? 34.434  -127.847 52.260  1.00 88.51  ? 89  ASN   N CB  1 
ATOM   23802 C  CG  . ASN   N  14 89  ? 34.456  -126.359 51.992  1.00 87.93  ? 89  ASN   N CG  1 
ATOM   23803 O  OD1 . ASN   N  14 89  ? 34.286  -125.929 50.854  1.00 88.11  ? 89  ASN   N OD1 1 
ATOM   23804 N  ND2 . ASN   N  14 89  ? 34.652  -125.565 53.032  1.00 92.44  ? 89  ASN   N ND2 1 
ATOM   23805 N  N   . LYS   N  14 90  ? 31.980  -130.633 52.303  1.00 88.97  ? 90  LYS   N N   1 
ATOM   23806 C  CA  . LYS   N  14 90  ? 31.882  -132.091 52.594  1.00 89.03  ? 90  LYS   N CA  1 
ATOM   23807 C  C   . LYS   N  14 90  ? 32.401  -132.908 51.401  1.00 91.04  ? 90  LYS   N C   1 
ATOM   23808 O  O   . LYS   N  14 90  ? 32.933  -134.014 51.639  1.00 93.25  ? 90  LYS   N O   1 
ATOM   23809 C  CB  . LYS   N  14 90  ? 30.445  -132.480 52.962  1.00 85.50  ? 90  LYS   N CB  1 
ATOM   23810 C  CG  . LYS   N  14 90  ? 29.373  -132.130 51.938  1.00 85.26  ? 90  LYS   N CG  1 
ATOM   23811 C  CD  . LYS   N  14 90  ? 28.062  -132.845 52.179  1.00 87.43  ? 90  LYS   N CD  1 
ATOM   23812 C  CE  . LYS   N  14 90  ? 27.365  -132.412 53.453  1.00 91.20  ? 90  LYS   N CE  1 
ATOM   23813 N  NZ  . LYS   N  14 90  ? 26.216  -133.293 53.774  1.00 96.33  ? 90  LYS   N NZ  1 
ATOM   23814 N  N   . ASP   N  14 91  ? 32.274  -132.384 50.177  1.00 91.01  ? 91  ASP   N N   1 
ATOM   23815 C  CA  . ASP   N  14 91  ? 32.662  -133.088 48.923  1.00 92.64  ? 91  ASP   N CA  1 
ATOM   23816 C  C   . ASP   N  14 91  ? 34.189  -133.120 48.756  1.00 90.47  ? 91  ASP   N C   1 
ATOM   23817 O  O   . ASP   N  14 91  ? 34.657  -133.939 47.939  1.00 95.70  ? 91  ASP   N O   1 
ATOM   23818 C  CB  . ASP   N  14 91  ? 32.017  -132.440 47.695  1.00 98.31  ? 91  ASP   N CB  1 
ATOM   23819 C  CG  . ASP   N  14 91  ? 30.495  -132.456 47.697  1.00 101.33 ? 91  ASP   N CG  1 
ATOM   23820 O  OD1 . ASP   N  14 91  ? 29.910  -133.158 48.548  1.00 109.45 ? 91  ASP   N OD1 1 
ATOM   23821 O  OD2 . ASP   N  14 91  ? 29.901  -131.765 46.842  1.00 104.62 ? 91  ASP   N OD2 1 
ATOM   23822 N  N   . ASN   N  14 92  ? 34.937  -132.280 49.481  1.00 85.84  ? 92  ASN   N N   1 
ATOM   23823 C  CA  . ASN   N  14 92  ? 36.403  -132.105 49.286  1.00 86.42  ? 92  ASN   N CA  1 
ATOM   23824 C  C   . ASN   N  14 92  ? 37.164  -132.250 50.608  1.00 84.60  ? 92  ASN   N C   1 
ATOM   23825 O  O   . ASN   N  14 92  ? 38.290  -131.718 50.687  1.00 84.90  ? 92  ASN   N O   1 
ATOM   23826 C  CB  . ASN   N  14 92  ? 36.714  -130.747 48.658  1.00 87.57  ? 92  ASN   N CB  1 
ATOM   23827 C  CG  . ASN   N  14 92  ? 35.898  -130.486 47.411  1.00 92.12  ? 92  ASN   N CG  1 
ATOM   23828 O  OD1 . ASN   N  14 92  ? 35.921  -131.280 46.475  1.00 92.79  ? 92  ASN   N OD1 1 
ATOM   23829 N  ND2 . ASN   N  14 92  ? 35.166  -129.383 47.390  1.00 97.62  ? 92  ASN   N ND2 1 
ATOM   23830 N  N   . LEU   N  14 93  ? 36.603  -132.959 51.593  1.00 85.24  ? 93  LEU   N N   1 
ATOM   23831 C  CA  . LEU   N  14 93  ? 37.234  -133.133 52.929  1.00 87.37  ? 93  LEU   N CA  1 
ATOM   23832 C  C   . LEU   N  14 93  ? 37.118  -134.587 53.395  1.00 87.47  ? 93  LEU   N C   1 
ATOM   23833 O  O   . LEU   N  14 93  ? 36.067  -135.214 53.162  1.00 87.60  ? 93  LEU   N O   1 
ATOM   23834 C  CB  . LEU   N  14 93  ? 36.572  -132.185 53.935  1.00 87.79  ? 93  LEU   N CB  1 
ATOM   23835 C  CG  . LEU   N  14 93  ? 36.928  -130.703 53.801  1.00 86.00  ? 93  LEU   N CG  1 
ATOM   23836 C  CD1 . LEU   N  14 93  ? 36.123  -129.870 54.787  1.00 85.22  ? 93  LEU   N CD1 1 
ATOM   23837 C  CD2 . LEU   N  14 93  ? 38.417  -130.465 54.010  1.00 87.40  ? 93  LEU   N CD2 1 
ATOM   23838 N  N   . THR   N  14 94  ? 38.184  -135.081 54.028  1.00 88.25  ? 94  THR   N N   1 
ATOM   23839 C  CA  . THR   N  14 94  ? 38.219  -136.324 54.838  1.00 88.39  ? 94  THR   N CA  1 
ATOM   23840 C  C   . THR   N  14 94  ? 38.722  -135.930 56.227  1.00 85.93  ? 94  THR   N C   1 
ATOM   23841 O  O   . THR   N  14 94  ? 39.935  -136.067 56.477  1.00 86.79  ? 94  THR   N O   1 
ATOM   23842 C  CB  . THR   N  14 94  ? 39.077  -137.406 54.168  1.00 90.80  ? 94  THR   N CB  1 
ATOM   23843 O  OG1 . THR   N  14 94  ? 38.643  -137.525 52.812  1.00 92.33  ? 94  THR   N OG1 1 
ATOM   23844 C  CG2 . THR   N  14 94  ? 38.975  -138.748 54.860  1.00 92.58  ? 94  THR   N CG2 1 
ATOM   23845 N  N   . ALA   N  14 95  ? 37.825  -135.407 57.066  1.00 84.80  ? 95  ALA   N N   1 
ATOM   23846 C  CA  . ALA   N  14 95  ? 38.138  -134.879 58.412  1.00 84.21  ? 95  ALA   N CA  1 
ATOM   23847 C  C   . ALA   N  14 95  ? 37.058  -135.317 59.405  1.00 81.77  ? 95  ALA   N C   1 
ATOM   23848 O  O   . ALA   N  14 95  ? 35.879  -134.971 59.197  1.00 82.27  ? 95  ALA   N O   1 
ATOM   23849 C  CB  . ALA   N  14 95  ? 38.266  -133.379 58.359  1.00 85.13  ? 95  ALA   N CB  1 
ATOM   23850 N  N   . GLY   N  14 96  ? 37.463  -136.078 60.423  1.00 83.39  ? 96  GLY   N N   1 
ATOM   23851 C  CA  . GLY   N  14 96  ? 36.655  -136.390 61.614  1.00 84.27  ? 96  GLY   N CA  1 
ATOM   23852 C  C   . GLY   N  14 96  ? 37.259  -135.716 62.826  1.00 85.90  ? 96  GLY   N C   1 
ATOM   23853 O  O   . GLY   N  14 96  ? 38.324  -136.166 63.280  1.00 91.86  ? 96  GLY   N O   1 
ATOM   23854 N  N   . ILE   N  14 97  ? 36.634  -134.644 63.309  1.00 84.32  ? 97  ILE   N N   1 
ATOM   23855 C  CA  . ILE   N  14 97  ? 37.212  -133.782 64.380  1.00 86.62  ? 97  ILE   N CA  1 
ATOM   23856 C  C   . ILE   N  14 97  ? 36.342  -133.892 65.635  1.00 83.48  ? 97  ILE   N C   1 
ATOM   23857 O  O   . ILE   N  14 97  ? 35.103  -133.797 65.509  1.00 84.91  ? 97  ILE   N O   1 
ATOM   23858 C  CB  . ILE   N  14 97  ? 37.359  -132.329 63.884  1.00 86.65  ? 97  ILE   N CB  1 
ATOM   23859 C  CG1 . ILE   N  14 97  ? 38.277  -132.252 62.663  1.00 86.34  ? 97  ILE   N CG1 1 
ATOM   23860 C  CG2 . ILE   N  14 97  ? 37.849  -131.418 64.999  1.00 88.82  ? 97  ILE   N CG2 1 
ATOM   23861 C  CD1 . ILE   N  14 97  ? 38.060  -131.028 61.818  1.00 86.76  ? 97  ILE   N CD1 1 
ATOM   23862 N  N   . ILE   N  14 98  ? 36.984  -134.109 66.788  1.00 83.21  ? 98  ILE   N N   1 
ATOM   23863 C  CA  . ILE   N  14 98  ? 36.371  -133.955 68.139  1.00 84.62  ? 98  ILE   N CA  1 
ATOM   23864 C  C   . ILE   N  14 98  ? 36.839  -132.610 68.698  1.00 82.48  ? 98  ILE   N C   1 
ATOM   23865 O  O   . ILE   N  14 98  ? 38.062  -132.410 68.786  1.00 83.31  ? 98  ILE   N O   1 
ATOM   23866 C  CB  . ILE   N  14 98  ? 36.741  -135.115 69.086  1.00 86.85  ? 98  ILE   N CB  1 
ATOM   23867 C  CG1 . ILE   N  14 98  ? 36.432  -136.484 68.472  1.00 87.97  ? 98  ILE   N CG1 1 
ATOM   23868 C  CG2 . ILE   N  14 98  ? 36.054  -134.931 70.434  1.00 88.68  ? 98  ILE   N CG2 1 
ATOM   23869 C  CD1 . ILE   N  14 98  ? 36.964  -137.658 69.268  1.00 88.95  ? 98  ILE   N CD1 1 
ATOM   23870 N  N   . VAL   N  14 99  ? 35.895  -131.735 69.048  1.00 80.93  ? 99  VAL   N N   1 
ATOM   23871 C  CA  . VAL   N  14 99  ? 36.151  -130.400 69.663  1.00 81.38  ? 99  VAL   N CA  1 
ATOM   23872 C  C   . VAL   N  14 99  ? 35.882  -130.521 71.165  1.00 80.51  ? 99  VAL   N C   1 
ATOM   23873 O  O   . VAL   N  14 99  ? 34.826  -131.071 71.525  1.00 78.44  ? 99  VAL   N O   1 
ATOM   23874 C  CB  . VAL   N  14 99  ? 35.271  -129.310 69.025  1.00 80.46  ? 99  VAL   N CB  1 
ATOM   23875 C  CG1 . VAL   N  14 99  ? 35.692  -127.924 69.478  1.00 81.82  ? 99  VAL   N CG1 1 
ATOM   23876 C  CG2 . VAL   N  14 99  ? 35.264  -129.395 67.506  1.00 79.89  ? 99  VAL   N CG2 1 
ATOM   23877 N  N   . ALA   N  14 100 ? 36.796  -130.021 72.001  1.00 81.10  ? 100 ALA   N N   1 
ATOM   23878 C  CA  . ALA   N  14 100 ? 36.717  -130.109 73.479  1.00 84.22  ? 100 ALA   N CA  1 
ATOM   23879 C  C   . ALA   N  14 100 ? 37.282  -128.837 74.115  1.00 86.28  ? 100 ALA   N C   1 
ATOM   23880 O  O   . ALA   N  14 100 ? 38.443  -128.498 73.817  1.00 88.83  ? 100 ALA   N O   1 
ATOM   23881 C  CB  . ALA   N  14 100 ? 37.460  -131.328 73.953  1.00 83.58  ? 100 ALA   N CB  1 
ATOM   23882 N  N   . GLY   N  14 101 ? 36.494  -128.181 74.974  1.00 90.39  ? 101 GLY   N N   1 
ATOM   23883 C  CA  . GLY   N  14 101 ? 36.847  -126.889 75.595  1.00 94.83  ? 101 GLY   N CA  1 
ATOM   23884 C  C   . GLY   N  14 101 ? 36.377  -126.791 77.035  1.00 99.73  ? 101 GLY   N C   1 
ATOM   23885 O  O   . GLY   N  14 101 ? 35.497  -127.585 77.426  1.00 97.54  ? 101 GLY   N O   1 
ATOM   23886 N  N   . TYR   N  14 102 ? 36.945  -125.842 77.790  1.00 107.40 ? 102 TYR   N N   1 
ATOM   23887 C  CA  . TYR   N  14 102 ? 36.567  -125.519 79.191  1.00 111.23 ? 102 TYR   N CA  1 
ATOM   23888 C  C   . TYR   N  14 102 ? 36.087  -124.064 79.293  1.00 115.93 ? 102 TYR   N C   1 
ATOM   23889 O  O   . TYR   N  14 102 ? 36.900  -123.129 79.115  1.00 113.36 ? 102 TYR   N O   1 
ATOM   23890 C  CB  . TYR   N  14 102 ? 37.726  -125.754 80.163  1.00 109.10 ? 102 TYR   N CB  1 
ATOM   23891 C  CG  . TYR   N  14 102 ? 37.359  -125.476 81.599  1.00 108.98 ? 102 TYR   N CG  1 
ATOM   23892 C  CD1 . TYR   N  14 102 ? 36.638  -126.398 82.340  1.00 108.22 ? 102 TYR   N CD1 1 
ATOM   23893 C  CD2 . TYR   N  14 102 ? 37.689  -124.274 82.206  1.00 111.44 ? 102 TYR   N CD2 1 
ATOM   23894 C  CE1 . TYR   N  14 102 ? 36.276  -126.146 83.654  1.00 109.10 ? 102 TYR   N CE1 1 
ATOM   23895 C  CE2 . TYR   N  14 102 ? 37.334  -124.005 83.519  1.00 110.71 ? 102 TYR   N CE2 1 
ATOM   23896 C  CZ  . TYR   N  14 102 ? 36.625  -124.945 84.247  1.00 108.79 ? 102 TYR   N CZ  1 
ATOM   23897 O  OH  . TYR   N  14 102 ? 36.267  -124.693 85.539  1.00 105.84 ? 102 TYR   N OH  1 
ATOM   23898 N  N   . ASP   N  14 103 ? 34.792  -123.895 79.574  1.00 121.64 ? 103 ASP   N N   1 
ATOM   23899 C  CA  . ASP   N  14 103 ? 34.177  -122.643 80.087  1.00 120.62 ? 103 ASP   N CA  1 
ATOM   23900 C  C   . ASP   N  14 103 ? 34.172  -122.715 81.614  1.00 120.67 ? 103 ASP   N C   1 
ATOM   23901 O  O   . ASP   N  14 103 ? 34.368  -123.822 82.149  1.00 120.34 ? 103 ASP   N O   1 
ATOM   23902 C  CB  . ASP   N  14 103 ? 32.748  -122.471 79.571  1.00 124.37 ? 103 ASP   N CB  1 
ATOM   23903 C  CG  . ASP   N  14 103 ? 32.661  -122.103 78.102  1.00 129.17 ? 103 ASP   N CG  1 
ATOM   23904 O  OD1 . ASP   N  14 103 ? 32.907  -120.922 77.782  1.00 137.59 ? 103 ASP   N OD1 1 
ATOM   23905 O  OD2 . ASP   N  14 103 ? 32.352  -123.003 77.288  1.00 121.02 ? 103 ASP   N OD2 1 
ATOM   23906 N  N   . ASP   N  14 104 ? 33.951  -121.585 82.286  1.00 122.25 ? 104 ASP   N N   1 
ATOM   23907 C  CA  . ASP   N  14 104 ? 33.748  -121.538 83.758  1.00 125.99 ? 104 ASP   N CA  1 
ATOM   23908 C  C   . ASP   N  14 104 ? 32.250  -121.709 84.038  1.00 123.13 ? 104 ASP   N C   1 
ATOM   23909 O  O   . ASP   N  14 104 ? 31.908  -122.323 85.067  1.00 119.48 ? 104 ASP   N O   1 
ATOM   23910 C  CB  . ASP   N  14 104 ? 34.346  -120.262 84.357  1.00 128.68 ? 104 ASP   N CB  1 
ATOM   23911 C  CG  . ASP   N  14 104 ? 35.055  -120.502 85.677  1.00 132.58 ? 104 ASP   N CG  1 
ATOM   23912 O  OD1 . ASP   N  14 104 ? 34.355  -120.714 86.686  1.00 135.95 ? 104 ASP   N OD1 1 
ATOM   23913 O  OD2 . ASP   N  14 104 ? 36.302  -120.501 85.678  1.00 132.25 ? 104 ASP   N OD2 1 
ATOM   23914 N  N   . LYS   N  14 105 ? 31.397  -121.208 83.137  1.00 123.96 ? 105 LYS   N N   1 
ATOM   23915 C  CA  . LYS   N  14 105 ? 29.916  -121.325 83.214  1.00 130.17 ? 105 LYS   N CA  1 
ATOM   23916 C  C   . LYS   N  14 105 ? 29.499  -122.755 82.851  1.00 129.22 ? 105 LYS   N C   1 
ATOM   23917 O  O   . LYS   N  14 105 ? 28.730  -123.354 83.626  1.00 138.79 ? 105 LYS   N O   1 
ATOM   23918 C  CB  . LYS   N  14 105 ? 29.248  -120.302 82.287  1.00 135.21 ? 105 LYS   N CB  1 
ATOM   23919 C  CG  . LYS   N  14 105 ? 27.726  -120.364 82.220  1.00 141.34 ? 105 LYS   N CG  1 
ATOM   23920 C  CD  . LYS   N  14 105 ? 27.109  -119.226 81.426  1.00 144.64 ? 105 LYS   N CD  1 
ATOM   23921 C  CE  . LYS   N  14 105 ? 26.910  -117.960 82.236  1.00 149.99 ? 105 LYS   N CE  1 
ATOM   23922 N  NZ  . LYS   N  14 105 ? 27.453  -116.771 81.538  1.00 147.82 ? 105 LYS   N NZ  1 
ATOM   23923 N  N   . ASN   N  14 106 ? 29.997  -123.272 81.722  1.00 128.48 ? 106 ASN   N N   1 
ATOM   23924 C  CA  . ASN   N  14 106 ? 29.545  -124.547 81.098  1.00 123.68 ? 106 ASN   N CA  1 
ATOM   23925 C  C   . ASN   N  14 106 ? 30.452  -125.720 81.497  1.00 119.70 ? 106 ASN   N C   1 
ATOM   23926 O  O   . ASN   N  14 106 ? 30.059  -126.867 81.209  1.00 116.84 ? 106 ASN   N O   1 
ATOM   23927 C  CB  . ASN   N  14 106 ? 29.479  -124.431 79.572  1.00 120.99 ? 106 ASN   N CB  1 
ATOM   23928 C  CG  . ASN   N  14 106 ? 28.462  -123.412 79.106  1.00 118.68 ? 106 ASN   N CG  1 
ATOM   23929 O  OD1 . ASN   N  14 106 ? 27.261  -123.609 79.271  1.00 114.87 ? 106 ASN   N OD1 1 
ATOM   23930 N  ND2 . ASN   N  14 106 ? 28.929  -122.320 78.523  1.00 123.28 ? 106 ASN   N ND2 1 
ATOM   23931 N  N   . LYS   N  14 107 ? 31.609  -125.450 82.117  1.00 124.69 ? 107 LYS   N N   1 
ATOM   23932 C  CA  . LYS   N  14 107 ? 32.614  -126.474 82.526  1.00 121.27 ? 107 LYS   N CA  1 
ATOM   23933 C  C   . LYS   N  14 107 ? 33.125  -127.201 81.272  1.00 115.11 ? 107 LYS   N C   1 
ATOM   23934 O  O   . LYS   N  14 107 ? 33.325  -126.523 80.243  1.00 108.86 ? 107 LYS   N O   1 
ATOM   23935 C  CB  . LYS   N  14 107 ? 32.010  -127.419 83.572  1.00 126.55 ? 107 LYS   N CB  1 
ATOM   23936 C  CG  . LYS   N  14 107 ? 31.541  -126.745 84.855  1.00 131.90 ? 107 LYS   N CG  1 
ATOM   23937 C  CD  . LYS   N  14 107 ? 32.682  -126.338 85.761  1.00 137.20 ? 107 LYS   N CD  1 
ATOM   23938 C  CE  . LYS   N  14 107 ? 32.288  -125.290 86.779  1.00 140.81 ? 107 LYS   N CE  1 
ATOM   23939 N  NZ  . LYS   N  14 107 ? 33.457  -124.834 87.568  1.00 144.91 ? 107 LYS   N NZ  1 
ATOM   23940 N  N   . GLY   N  14 108 ? 33.338  -128.520 81.353  1.00 111.48 ? 108 GLY   N N   1 
ATOM   23941 C  CA  . GLY   N  14 108 ? 33.818  -129.355 80.235  1.00 108.40 ? 108 GLY   N CA  1 
ATOM   23942 C  C   . GLY   N  14 108 ? 32.711  -129.626 79.232  1.00 103.42 ? 108 GLY   N C   1 
ATOM   23943 O  O   . GLY   N  14 108 ? 31.569  -129.877 79.667  1.00 105.53 ? 108 GLY   N O   1 
ATOM   23944 N  N   . GLU   N  14 109 ? 33.033  -129.570 77.938  1.00 100.85 ? 109 GLU   N N   1 
ATOM   23945 C  CA  . GLU   N  14 109 ? 32.081  -129.837 76.828  1.00 101.77 ? 109 GLU   N CA  1 
ATOM   23946 C  C   . GLU   N  14 109 ? 32.823  -130.544 75.692  1.00 97.57  ? 109 GLU   N C   1 
ATOM   23947 O  O   . GLU   N  14 109 ? 33.955  -130.122 75.377  1.00 93.12  ? 109 GLU   N O   1 
ATOM   23948 C  CB  . GLU   N  14 109 ? 31.443  -128.536 76.340  1.00 103.99 ? 109 GLU   N CB  1 
ATOM   23949 C  CG  . GLU   N  14 109 ? 30.208  -128.138 77.128  1.00 112.84 ? 109 GLU   N CG  1 
ATOM   23950 C  CD  . GLU   N  14 109 ? 29.481  -126.911 76.601  1.00 119.01 ? 109 GLU   N CD  1 
ATOM   23951 O  OE1 . GLU   N  14 109 ? 29.990  -126.280 75.650  1.00 128.78 ? 109 GLU   N OE1 1 
ATOM   23952 O  OE2 . GLU   N  14 109 ? 28.404  -126.588 77.144  1.00 129.74 ? 109 GLU   N OE2 1 
ATOM   23953 N  N   . VAL   N  14 110 ? 32.203  -131.581 75.119  1.00 94.60  ? 110 VAL   N N   1 
ATOM   23954 C  CA  . VAL   N  14 110 ? 32.725  -132.331 73.940  1.00 91.68  ? 110 VAL   N CA  1 
ATOM   23955 C  C   . VAL   N  14 110 ? 31.682  -132.269 72.821  1.00 86.85  ? 110 VAL   N C   1 
ATOM   23956 O  O   . VAL   N  14 110 ? 30.493  -132.524 73.096  1.00 90.38  ? 110 VAL   N O   1 
ATOM   23957 C  CB  . VAL   N  14 110 ? 33.093  -133.782 74.306  1.00 91.23  ? 110 VAL   N CB  1 
ATOM   23958 C  CG1 . VAL   N  14 110 ? 33.339  -134.644 73.074  1.00 90.48  ? 110 VAL   N CG1 1 
ATOM   23959 C  CG2 . VAL   N  14 110 ? 34.301  -133.825 75.226  1.00 94.02  ? 110 VAL   N CG2 1 
ATOM   23960 N  N   . TYR   N  14 111 ? 32.135  -131.923 71.614  1.00 85.08  ? 111 TYR   N N   1 
ATOM   23961 C  CA  . TYR   N  14 111 ? 31.371  -131.983 70.342  1.00 87.33  ? 111 TYR   N CA  1 
ATOM   23962 C  C   . TYR   N  14 111 ? 32.157  -132.851 69.356  1.00 84.67  ? 111 TYR   N C   1 
ATOM   23963 O  O   . TYR   N  14 111 ? 33.366  -132.601 69.186  1.00 90.53  ? 111 TYR   N O   1 
ATOM   23964 C  CB  . TYR   N  14 111 ? 31.156  -130.578 69.771  1.00 86.60  ? 111 TYR   N CB  1 
ATOM   23965 C  CG  . TYR   N  14 111 ? 30.374  -129.648 70.663  1.00 86.10  ? 111 TYR   N CG  1 
ATOM   23966 C  CD1 . TYR   N  14 111 ? 31.003  -128.906 71.649  1.00 86.03  ? 111 TYR   N CD1 1 
ATOM   23967 C  CD2 . TYR   N  14 111 ? 29.002  -129.508 70.523  1.00 85.51  ? 111 TYR   N CD2 1 
ATOM   23968 C  CE1 . TYR   N  14 111 ? 30.289  -128.053 72.476  1.00 86.74  ? 111 TYR   N CE1 1 
ATOM   23969 C  CE2 . TYR   N  14 111 ? 28.274  -128.658 71.339  1.00 85.03  ? 111 TYR   N CE2 1 
ATOM   23970 C  CZ  . TYR   N  14 111 ? 28.919  -127.927 72.319  1.00 86.38  ? 111 TYR   N CZ  1 
ATOM   23971 O  OH  . TYR   N  14 111 ? 28.197  -127.090 73.120  1.00 89.74  ? 111 TYR   N OH  1 
ATOM   23972 N  N   . THR   N  14 112 ? 31.506  -133.846 68.746  1.00 82.75  ? 112 THR   N N   1 
ATOM   23973 C  CA  . THR   N  14 112 ? 32.100  -134.683 67.670  1.00 84.39  ? 112 THR   N CA  1 
ATOM   23974 C  C   . THR   N  14 112 ? 31.487  -134.251 66.336  1.00 78.06  ? 112 THR   N C   1 
ATOM   23975 O  O   . THR   N  14 112 ? 30.271  -133.976 66.300  1.00 75.28  ? 112 THR   N O   1 
ATOM   23976 C  CB  . THR   N  14 112 ? 31.958  -136.185 67.955  1.00 85.41  ? 112 THR   N CB  1 
ATOM   23977 O  OG1 . THR   N  14 112 ? 32.744  -136.873 66.981  1.00 89.63  ? 112 THR   N OG1 1 
ATOM   23978 C  CG2 . THR   N  14 112 ? 30.536  -136.700 67.906  1.00 88.45  ? 112 THR   N CG2 1 
ATOM   23979 N  N   . ILE   N  14 113 ? 32.321  -134.165 65.299  1.00 78.78  ? 113 ILE   N N   1 
ATOM   23980 C  CA  . ILE   N  14 113 ? 31.923  -133.761 63.919  1.00 83.84  ? 113 ILE   N CA  1 
ATOM   23981 C  C   . ILE   N  14 113 ? 32.416  -134.830 62.947  1.00 83.38  ? 113 ILE   N C   1 
ATOM   23982 O  O   . ILE   N  14 113 ? 33.587  -134.828 62.567  1.00 80.37  ? 113 ILE   N O   1 
ATOM   23983 C  CB  . ILE   N  14 113 ? 32.469  -132.359 63.586  1.00 83.36  ? 113 ILE   N CB  1 
ATOM   23984 C  CG1 . ILE   N  14 113 ? 32.016  -131.327 64.623  1.00 84.32  ? 113 ILE   N CG1 1 
ATOM   23985 C  CG2 . ILE   N  14 113 ? 32.077  -131.949 62.173  1.00 84.74  ? 113 ILE   N CG2 1 
ATOM   23986 C  CD1 . ILE   N  14 113 ? 32.743  -130.009 64.543  1.00 83.51  ? 113 ILE   N CD1 1 
ATOM   23987 N  N   . PRO   N  14 114 ? 31.542  -135.778 62.526  1.00 86.04  ? 114 PRO   N N   1 
ATOM   23988 C  CA  . PRO   N  14 114 ? 31.935  -136.850 61.610  1.00 87.98  ? 114 PRO   N CA  1 
ATOM   23989 C  C   . PRO   N  14 114 ? 32.154  -136.335 60.177  1.00 89.77  ? 114 PRO   N C   1 
ATOM   23990 O  O   . PRO   N  14 114 ? 32.215  -135.130 59.991  1.00 90.88  ? 114 PRO   N O   1 
ATOM   23991 C  CB  . PRO   N  14 114 ? 30.762  -137.848 61.655  1.00 88.72  ? 114 PRO   N CB  1 
ATOM   23992 C  CG  . PRO   N  14 114 ? 29.865  -137.368 62.785  1.00 87.26  ? 114 PRO   N CG  1 
ATOM   23993 C  CD  . PRO   N  14 114 ? 30.128  -135.884 62.915  1.00 86.47  ? 114 PRO   N CD  1 
ATOM   23994 N  N   . LEU   N  14 115 ? 32.262  -137.254 59.210  1.00 91.01  ? 115 LEU   N N   1 
ATOM   23995 C  CA  . LEU   N  14 115 ? 32.566  -136.951 57.784  1.00 87.80  ? 115 LEU   N CA  1 
ATOM   23996 C  C   . LEU   N  14 115 ? 31.516  -135.998 57.201  1.00 89.42  ? 115 LEU   N C   1 
ATOM   23997 O  O   . LEU   N  14 115 ? 31.922  -135.054 56.494  1.00 93.60  ? 115 LEU   N O   1 
ATOM   23998 C  CB  . LEU   N  14 115 ? 32.637  -138.254 56.980  1.00 89.32  ? 115 LEU   N CB  1 
ATOM   23999 C  CG  . LEU   N  14 115 ? 34.041  -138.748 56.622  1.00 94.18  ? 115 LEU   N CG  1 
ATOM   24000 C  CD1 . LEU   N  14 115 ? 34.988  -138.701 57.817  1.00 95.58  ? 115 LEU   N CD1 1 
ATOM   24001 C  CD2 . LEU   N  14 115 ? 33.980  -140.160 56.057  1.00 96.28  ? 115 LEU   N CD2 1 
ATOM   24002 N  N   . GLY   N  14 116 ? 30.229  -136.213 57.495  1.00 82.18  ? 116 GLY   N N   1 
ATOM   24003 C  CA  . GLY   N  14 116 ? 29.118  -135.440 56.900  1.00 87.46  ? 116 GLY   N CA  1 
ATOM   24004 C  C   . GLY   N  14 116 ? 29.170  -133.954 57.239  1.00 84.87  ? 116 GLY   N C   1 
ATOM   24005 O  O   . GLY   N  14 116 ? 28.705  -133.145 56.414  1.00 82.98  ? 116 GLY   N O   1 
ATOM   24006 N  N   . GLY   N  14 117 ? 29.708  -133.600 58.410  1.00 85.53  ? 117 GLY   N N   1 
ATOM   24007 C  CA  . GLY   N  14 117 ? 29.707  -132.226 58.946  1.00 83.41  ? 117 GLY   N CA  1 
ATOM   24008 C  C   . GLY   N  14 117 ? 28.536  -131.981 59.884  1.00 85.07  ? 117 GLY   N C   1 
ATOM   24009 O  O   . GLY   N  14 117 ? 28.234  -130.804 60.137  1.00 85.11  ? 117 GLY   N O   1 
ATOM   24010 N  N   . SER   N  14 118 ? 27.898  -133.043 60.388  1.00 83.08  ? 118 SER   N N   1 
ATOM   24011 C  CA  . SER   N  14 118 ? 26.886  -132.981 61.476  1.00 84.38  ? 118 SER   N CA  1 
ATOM   24012 C  C   . SER   N  14 118 ? 27.602  -132.678 62.799  1.00 84.71  ? 118 SER   N C   1 
ATOM   24013 O  O   . SER   N  14 118 ? 28.818  -132.949 62.885  1.00 88.97  ? 118 SER   N O   1 
ATOM   24014 C  CB  . SER   N  14 118 ? 26.078  -134.260 61.553  1.00 85.50  ? 118 SER   N CB  1 
ATOM   24015 O  OG  . SER   N  14 118 ? 26.925  -135.398 61.660  1.00 85.73  ? 118 SER   N OG  1 
ATOM   24016 N  N   . VAL   N  14 119 ? 26.887  -132.121 63.783  1.00 82.49  ? 119 VAL   N N   1 
ATOM   24017 C  CA  . VAL   N  14 119 ? 27.433  -131.824 65.141  1.00 80.76  ? 119 VAL   N CA  1 
ATOM   24018 C  C   . VAL   N  14 119 ? 26.668  -132.653 66.168  1.00 81.32  ? 119 VAL   N C   1 
ATOM   24019 O  O   . VAL   N  14 119 ? 25.424  -132.684 66.105  1.00 83.91  ? 119 VAL   N O   1 
ATOM   24020 C  CB  . VAL   N  14 119 ? 27.352  -130.338 65.521  1.00 78.92  ? 119 VAL   N CB  1 
ATOM   24021 C  CG1 . VAL   N  14 119 ? 28.579  -129.922 66.314  1.00 77.91  ? 119 VAL   N CG1 1 
ATOM   24022 C  CG2 . VAL   N  14 119 ? 27.157  -129.439 64.315  1.00 79.38  ? 119 VAL   N CG2 1 
ATOM   24023 N  N   . HIS   N  14 120 ? 27.401  -133.258 67.100  1.00 82.70  ? 120 HIS   N N   1 
ATOM   24024 C  CA  . HIS   N  14 120 ? 26.853  -134.089 68.197  1.00 83.87  ? 120 HIS   N CA  1 
ATOM   24025 C  C   . HIS   N  14 120 ? 27.571  -133.713 69.494  1.00 82.66  ? 120 HIS   N C   1 
ATOM   24026 O  O   . HIS   N  14 120 ? 28.796  -133.929 69.578  1.00 84.20  ? 120 HIS   N O   1 
ATOM   24027 C  CB  . HIS   N  14 120 ? 26.968  -135.570 67.823  1.00 87.04  ? 120 HIS   N CB  1 
ATOM   24028 C  CG  . HIS   N  14 120 ? 26.417  -135.865 66.469  1.00 91.14  ? 120 HIS   N CG  1 
ATOM   24029 N  ND1 . HIS   N  14 120 ? 25.064  -136.040 66.245  1.00 92.94  ? 120 HIS   N ND1 1 
ATOM   24030 C  CD2 . HIS   N  14 120 ? 27.023  -135.975 65.266  1.00 92.69  ? 120 HIS   N CD2 1 
ATOM   24031 C  CE1 . HIS   N  14 120 ? 24.862  -136.268 64.963  1.00 94.90  ? 120 HIS   N CE1 1 
ATOM   24032 N  NE2 . HIS   N  14 120 ? 26.049  -136.234 64.340  1.00 94.61  ? 120 HIS   N NE2 1 
ATOM   24033 N  N   . LYS   N  14 121 ? 26.834  -133.126 70.436  1.00 82.64  ? 121 LYS   N N   1 
ATOM   24034 C  CA  . LYS   N  14 121 ? 27.314  -132.834 71.810  1.00 86.96  ? 121 LYS   N CA  1 
ATOM   24035 C  C   . LYS   N  14 121 ? 27.130  -134.098 72.657  1.00 85.78  ? 121 LYS   N C   1 
ATOM   24036 O  O   . LYS   N  14 121 ? 25.983  -134.573 72.756  1.00 91.34  ? 121 LYS   N O   1 
ATOM   24037 C  CB  . LYS   N  14 121 ? 26.545  -131.650 72.397  1.00 85.97  ? 121 LYS   N CB  1 
ATOM   24038 C  CG  . LYS   N  14 121 ? 27.103  -131.128 73.710  1.00 88.98  ? 121 LYS   N CG  1 
ATOM   24039 C  CD  . LYS   N  14 121 ? 26.306  -129.990 74.302  1.00 89.51  ? 121 LYS   N CD  1 
ATOM   24040 C  CE  . LYS   N  14 121 ? 26.919  -129.459 75.579  1.00 91.88  ? 121 LYS   N CE  1 
ATOM   24041 N  NZ  . LYS   N  14 121 ? 27.105  -130.532 76.585  1.00 96.20  ? 121 LYS   N NZ  1 
ATOM   24042 N  N   . LEU   N  14 122 ? 28.215  -134.627 73.229  1.00 84.19  ? 122 LEU   N N   1 
ATOM   24043 C  CA  . LEU   N  14 122 ? 28.200  -135.898 74.001  1.00 84.31  ? 122 LEU   N CA  1 
ATOM   24044 C  C   . LEU   N  14 122 ? 28.959  -135.725 75.313  1.00 85.42  ? 122 LEU   N C   1 
ATOM   24045 O  O   . LEU   N  14 122 ? 29.774  -134.813 75.443  1.00 85.60  ? 122 LEU   N O   1 
ATOM   24046 C  CB  . LEU   N  14 122 ? 28.835  -137.011 73.161  1.00 85.35  ? 122 LEU   N CB  1 
ATOM   24047 C  CG  . LEU   N  14 122 ? 28.218  -137.264 71.786  1.00 84.66  ? 122 LEU   N CG  1 
ATOM   24048 C  CD1 . LEU   N  14 122 ? 29.087  -138.226 70.990  1.00 83.06  ? 122 LEU   N CD1 1 
ATOM   24049 C  CD2 . LEU   N  14 122 ? 26.798  -137.802 71.908  1.00 85.59  ? 122 LEU   N CD2 1 
ATOM   24050 N  N   . PRO   N  14 123 ? 28.694  -136.588 76.324  1.00 83.42  ? 123 PRO   N N   1 
ATOM   24051 C  CA  . PRO   N  14 123 ? 29.526  -136.676 77.525  1.00 83.73  ? 123 PRO   N CA  1 
ATOM   24052 C  C   . PRO   N  14 123 ? 30.979  -137.088 77.243  1.00 80.77  ? 123 PRO   N C   1 
ATOM   24053 O  O   . PRO   N  14 123 ? 31.855  -136.673 77.958  1.00 76.53  ? 123 PRO   N O   1 
ATOM   24054 C  CB  . PRO   N  14 123 ? 28.861  -137.781 78.362  1.00 83.27  ? 123 PRO   N CB  1 
ATOM   24055 C  CG  . PRO   N  14 123 ? 27.437  -137.823 77.867  1.00 83.60  ? 123 PRO   N CG  1 
ATOM   24056 C  CD  . PRO   N  14 123 ? 27.528  -137.483 76.395  1.00 83.22  ? 123 PRO   N CD  1 
ATOM   24057 N  N   . TYR   N  14 124 ? 31.182  -137.957 76.256  1.00 83.01  ? 124 TYR   N N   1 
ATOM   24058 C  CA  . TYR   N  14 124 ? 32.514  -138.325 75.714  1.00 85.51  ? 124 TYR   N CA  1 
ATOM   24059 C  C   . TYR   N  14 124 ? 32.336  -138.731 74.252  1.00 83.42  ? 124 TYR   N C   1 
ATOM   24060 O  O   . TYR   N  14 124 ? 31.220  -139.130 73.866  1.00 83.46  ? 124 TYR   N O   1 
ATOM   24061 C  CB  . TYR   N  14 124 ? 33.162  -139.456 76.519  1.00 88.15  ? 124 TYR   N CB  1 
ATOM   24062 C  CG  . TYR   N  14 124 ? 32.592  -140.827 76.256  1.00 88.67  ? 124 TYR   N CG  1 
ATOM   24063 C  CD1 . TYR   N  14 124 ? 31.358  -141.195 76.767  1.00 89.13  ? 124 TYR   N CD1 1 
ATOM   24064 C  CD2 . TYR   N  14 124 ? 33.281  -141.758 75.494  1.00 89.14  ? 124 TYR   N CD2 1 
ATOM   24065 C  CE1 . TYR   N  14 124 ? 30.821  -142.450 76.530  1.00 90.11  ? 124 TYR   N CE1 1 
ATOM   24066 C  CE2 . TYR   N  14 124 ? 32.758  -143.018 75.246  1.00 91.69  ? 124 TYR   N CE2 1 
ATOM   24067 C  CZ  . TYR   N  14 124 ? 31.523  -143.365 75.767  1.00 91.37  ? 124 TYR   N CZ  1 
ATOM   24068 O  OH  . TYR   N  14 124 ? 30.992  -144.601 75.535  1.00 93.54  ? 124 TYR   N OH  1 
ATOM   24069 N  N   . ALA   N  14 125 ? 33.407  -138.623 73.470  1.00 81.26  ? 125 ALA   N N   1 
ATOM   24070 C  CA  . ALA   N  14 125 ? 33.425  -138.971 72.035  1.00 82.29  ? 125 ALA   N CA  1 
ATOM   24071 C  C   . ALA   N  14 125 ? 34.702  -139.752 71.732  1.00 83.01  ? 125 ALA   N C   1 
ATOM   24072 O  O   . ALA   N  14 125 ? 35.765  -139.397 72.281  1.00 83.30  ? 125 ALA   N O   1 
ATOM   24073 C  CB  . ALA   N  14 125 ? 33.324  -137.728 71.190  1.00 81.18  ? 125 ALA   N CB  1 
ATOM   24074 N  N   . ILE   N  14 126 ? 34.569  -140.787 70.904  1.00 84.94  ? 126 ILE   N N   1 
ATOM   24075 C  CA  . ILE   N  14 126 ? 35.698  -141.588 70.353  1.00 85.82  ? 126 ILE   N CA  1 
ATOM   24076 C  C   . ILE   N  14 126 ? 35.588  -141.524 68.828  1.00 82.65  ? 126 ILE   N C   1 
ATOM   24077 O  O   . ILE   N  14 126 ? 34.447  -141.511 68.319  1.00 82.32  ? 126 ILE   N O   1 
ATOM   24078 C  CB  . ILE   N  14 126 ? 35.668  -143.028 70.903  1.00 86.72  ? 126 ILE   N CB  1 
ATOM   24079 C  CG1 . ILE   N  14 126 ? 34.310  -143.702 70.688  1.00 88.73  ? 126 ILE   N CG1 1 
ATOM   24080 C  CG2 . ILE   N  14 126 ? 36.061  -143.039 72.371  1.00 87.09  ? 126 ILE   N CG2 1 
ATOM   24081 C  CD1 . ILE   N  14 126 ? 34.382  -145.208 70.603  1.00 88.74  ? 126 ILE   N CD1 1 
ATOM   24082 N  N   . ALA   N  14 127 ? 36.723  -141.432 68.135  1.00 84.01  ? 127 ALA   N N   1 
ATOM   24083 C  CA  . ALA   N  14 127 ? 36.785  -141.335 66.659  1.00 83.75  ? 127 ALA   N CA  1 
ATOM   24084 C  C   . ALA   N  14 127 ? 38.136  -141.850 66.150  1.00 86.09  ? 127 ALA   N C   1 
ATOM   24085 O  O   . ALA   N  14 127 ? 39.023  -142.142 66.981  1.00 89.06  ? 127 ALA   N O   1 
ATOM   24086 C  CB  . ALA   N  14 127 ? 36.531  -139.913 66.232  1.00 84.92  ? 127 ALA   N CB  1 
ATOM   24087 N  N   . GLY   N  14 128 ? 38.262  -141.968 64.826  1.00 85.38  ? 128 GLY   N N   1 
ATOM   24088 C  CA  . GLY   N  14 128 ? 39.432  -142.555 64.148  1.00 86.22  ? 128 GLY   N CA  1 
ATOM   24089 C  C   . GLY   N  14 128 ? 39.234  -144.043 63.911  1.00 83.36  ? 128 GLY   N C   1 
ATOM   24090 O  O   . GLY   N  14 128 ? 38.219  -144.590 64.389  1.00 81.93  ? 128 GLY   N O   1 
ATOM   24091 N  N   . SER   N  14 129 ? 40.173  -144.677 63.204  1.00 80.55  ? 129 SER   N N   1 
ATOM   24092 C  CA  . SER   N  14 129 ? 40.113  -146.102 62.783  1.00 81.95  ? 129 SER   N CA  1 
ATOM   24093 C  C   . SER   N  14 129 ? 40.057  -147.029 64.008  1.00 82.91  ? 129 SER   N C   1 
ATOM   24094 O  O   . SER   N  14 129 ? 39.288  -148.011 63.962  1.00 87.90  ? 129 SER   N O   1 
ATOM   24095 C  CB  . SER   N  14 129 ? 41.274  -146.437 61.886  1.00 81.17  ? 129 SER   N CB  1 
ATOM   24096 O  OG  . SER   N  14 129 ? 42.491  -145.957 62.433  1.00 81.95  ? 129 SER   N OG  1 
ATOM   24097 N  N   . GLY   N  14 130 ? 40.832  -146.729 65.057  1.00 82.55  ? 130 GLY   N N   1 
ATOM   24098 C  CA  . GLY   N  14 130 ? 40.938  -147.543 66.286  1.00 80.54  ? 130 GLY   N CA  1 
ATOM   24099 C  C   . GLY   N  14 130 ? 39.654  -147.552 67.099  1.00 80.44  ? 130 GLY   N C   1 
ATOM   24100 O  O   . GLY   N  14 130 ? 39.408  -148.558 67.788  1.00 79.25  ? 130 GLY   N O   1 
ATOM   24101 N  N   . SER   N  14 131 ? 38.874  -146.467 67.039  1.00 82.08  ? 131 SER   N N   1 
ATOM   24102 C  CA  . SER   N  14 131 ? 37.591  -146.273 67.769  1.00 84.01  ? 131 SER   N CA  1 
ATOM   24103 C  C   . SER   N  14 131 ? 36.731  -147.543 67.705  1.00 82.76  ? 131 SER   N C   1 
ATOM   24104 O  O   . SER   N  14 131 ? 36.222  -147.961 68.763  1.00 77.60  ? 131 SER   N O   1 
ATOM   24105 C  CB  . SER   N  14 131 ? 36.839  -145.076 67.232  1.00 86.27  ? 131 SER   N CB  1 
ATOM   24106 O  OG  . SER   N  14 131 ? 36.327  -145.324 65.929  1.00 88.36  ? 131 SER   N OG  1 
ATOM   24107 N  N   . THR   N  14 132 ? 36.593  -148.137 66.514  1.00 82.48  ? 132 THR   N N   1 
ATOM   24108 C  CA  . THR   N  14 132 ? 35.695  -149.295 66.237  1.00 87.08  ? 132 THR   N CA  1 
ATOM   24109 C  C   . THR   N  14 132 ? 35.895  -150.390 67.294  1.00 88.16  ? 132 THR   N C   1 
ATOM   24110 O  O   . THR   N  14 132 ? 34.892  -151.005 67.683  1.00 91.94  ? 132 THR   N O   1 
ATOM   24111 C  CB  . THR   N  14 132 ? 35.903  -149.876 64.831  1.00 90.86  ? 132 THR   N CB  1 
ATOM   24112 O  OG1 . THR   N  14 132 ? 37.274  -150.252 64.689  1.00 97.84  ? 132 THR   N OG1 1 
ATOM   24113 C  CG2 . THR   N  14 132 ? 35.516  -148.914 63.729  1.00 90.67  ? 132 THR   N CG2 1 
ATOM   24114 N  N   . PHE   N  14 133 ? 37.133  -150.605 67.750  1.00 84.91  ? 133 PHE   N N   1 
ATOM   24115 C  CA  . PHE   N  14 133 ? 37.531  -151.748 68.614  1.00 84.38  ? 133 PHE   N CA  1 
ATOM   24116 C  C   . PHE   N  14 133 ? 37.194  -151.481 70.089  1.00 84.07  ? 133 PHE   N C   1 
ATOM   24117 O  O   . PHE   N  14 133 ? 37.194  -152.463 70.870  1.00 79.16  ? 133 PHE   N O   1 
ATOM   24118 C  CB  . PHE   N  14 133 ? 39.013  -152.067 68.404  1.00 83.81  ? 133 PHE   N CB  1 
ATOM   24119 C  CG  . PHE   N  14 133 ? 39.368  -152.369 66.970  1.00 84.89  ? 133 PHE   N CG  1 
ATOM   24120 C  CD1 . PHE   N  14 133 ? 38.821  -153.468 66.323  1.00 85.82  ? 133 PHE   N CD1 1 
ATOM   24121 C  CD2 . PHE   N  14 133 ? 40.233  -151.551 66.260  1.00 84.31  ? 133 PHE   N CD2 1 
ATOM   24122 C  CE1 . PHE   N  14 133 ? 39.134  -153.745 65.001  1.00 86.76  ? 133 PHE   N CE1 1 
ATOM   24123 C  CE2 . PHE   N  14 133 ? 40.547  -151.830 64.939  1.00 86.64  ? 133 PHE   N CE2 1 
ATOM   24124 C  CZ  . PHE   N  14 133 ? 39.998  -152.927 64.312  1.00 86.83  ? 133 PHE   N CZ  1 
ATOM   24125 N  N   . ILE   N  14 134 ? 36.891  -150.231 70.467  1.00 81.91  ? 134 ILE   N N   1 
ATOM   24126 C  CA  . ILE   N  14 134 ? 36.721  -149.838 71.900  1.00 82.57  ? 134 ILE   N CA  1 
ATOM   24127 C  C   . ILE   N  14 134 ? 35.312  -149.295 72.179  1.00 80.88  ? 134 ILE   N C   1 
ATOM   24128 O  O   . ILE   N  14 134 ? 35.101  -148.817 73.313  1.00 82.91  ? 134 ILE   N O   1 
ATOM   24129 C  CB  . ILE   N  14 134 ? 37.817  -148.843 72.332  1.00 83.53  ? 134 ILE   N CB  1 
ATOM   24130 C  CG1 . ILE   N  14 134 ? 37.862  -147.600 71.441  1.00 84.47  ? 134 ILE   N CG1 1 
ATOM   24131 C  CG2 . ILE   N  14 134 ? 39.168  -149.535 72.396  1.00 83.27  ? 134 ILE   N CG2 1 
ATOM   24132 C  CD1 . ILE   N  14 134 ? 38.637  -146.446 72.037  1.00 86.81  ? 134 ILE   N CD1 1 
ATOM   24133 N  N   . TYR   N  14 135 ? 34.372  -149.378 71.231  1.00 78.35  ? 135 TYR   N N   1 
ATOM   24134 C  CA  . TYR   N  14 135 ? 32.957  -148.982 71.468  1.00 80.36  ? 135 TYR   N CA  1 
ATOM   24135 C  C   . TYR   N  14 135 ? 32.418  -149.780 72.658  1.00 80.86  ? 135 TYR   N C   1 
ATOM   24136 O  O   . TYR   N  14 135 ? 31.906  -149.166 73.614  1.00 77.95  ? 135 TYR   N O   1 
ATOM   24137 C  CB  . TYR   N  14 135 ? 32.094  -149.168 70.217  1.00 81.71  ? 135 TYR   N CB  1 
ATOM   24138 C  CG  . TYR   N  14 135 ? 32.138  -147.991 69.280  1.00 83.48  ? 135 TYR   N CG  1 
ATOM   24139 C  CD1 . TYR   N  14 135 ? 31.213  -146.962 69.373  1.00 84.35  ? 135 TYR   N CD1 1 
ATOM   24140 C  CD2 . TYR   N  14 135 ? 33.130  -147.888 68.321  1.00 86.60  ? 135 TYR   N CD2 1 
ATOM   24141 C  CE1 . TYR   N  14 135 ? 31.264  -145.871 68.520  1.00 85.71  ? 135 TYR   N CE1 1 
ATOM   24142 C  CE2 . TYR   N  14 135 ? 33.195  -146.805 67.460  1.00 87.49  ? 135 TYR   N CE2 1 
ATOM   24143 C  CZ  . TYR   N  14 135 ? 32.258  -145.792 67.560  1.00 86.92  ? 135 TYR   N CZ  1 
ATOM   24144 O  OH  . TYR   N  14 135 ? 32.323  -144.721 66.716  1.00 89.14  ? 135 TYR   N OH  1 
ATOM   24145 N  N   . GLY   N  14 136 ? 32.563  -151.107 72.598  1.00 81.49  ? 136 GLY   N N   1 
ATOM   24146 C  CA  . GLY   N  14 136 ? 32.152  -152.045 73.659  1.00 82.86  ? 136 GLY   N CA  1 
ATOM   24147 C  C   . GLY   N  14 136 ? 32.729  -151.657 75.006  1.00 82.41  ? 136 GLY   N C   1 
ATOM   24148 O  O   . GLY   N  14 136 ? 31.943  -151.473 75.955  1.00 82.82  ? 136 GLY   N O   1 
ATOM   24149 N  N   . TYR   N  14 137 ? 34.055  -151.527 75.077  1.00 85.99  ? 137 TYR   N N   1 
ATOM   24150 C  CA  . TYR   N  14 137 ? 34.821  -151.239 76.318  1.00 90.11  ? 137 TYR   N CA  1 
ATOM   24151 C  C   . TYR   N  14 137 ? 34.398  -149.886 76.902  1.00 90.51  ? 137 TYR   N C   1 
ATOM   24152 O  O   . TYR   N  14 137 ? 34.079  -149.830 78.107  1.00 93.58  ? 137 TYR   N O   1 
ATOM   24153 C  CB  . TYR   N  14 137 ? 36.326  -151.249 76.045  1.00 91.47  ? 137 TYR   N CB  1 
ATOM   24154 C  CG  . TYR   N  14 137 ? 37.161  -150.947 77.261  1.00 94.28  ? 137 TYR   N CG  1 
ATOM   24155 C  CD1 . TYR   N  14 137 ? 37.543  -151.953 78.132  1.00 95.51  ? 137 TYR   N CD1 1 
ATOM   24156 C  CD2 . TYR   N  14 137 ? 37.543  -149.650 77.563  1.00 96.75  ? 137 TYR   N CD2 1 
ATOM   24157 C  CE1 . TYR   N  14 137 ? 38.296  -151.683 79.262  1.00 98.27  ? 137 TYR   N CE1 1 
ATOM   24158 C  CE2 . TYR   N  14 137 ? 38.297  -149.362 78.689  1.00 98.50  ? 137 TYR   N CE2 1 
ATOM   24159 C  CZ  . TYR   N  14 137 ? 38.675  -150.383 79.541  1.00 97.52  ? 137 TYR   N CZ  1 
ATOM   24160 O  OH  . TYR   N  14 137 ? 39.419  -150.111 80.651  1.00 104.73 ? 137 TYR   N OH  1 
ATOM   24161 N  N   . CYS   N  14 138 ? 34.411  -148.834 76.077  1.00 88.83  ? 138 CYS   N N   1 
ATOM   24162 C  CA  . CYS   N  14 138 ? 34.184  -147.423 76.493  1.00 87.71  ? 138 CYS   N CA  1 
ATOM   24163 C  C   . CYS   N  14 138 ? 32.769  -147.254 77.055  1.00 87.66  ? 138 CYS   N C   1 
ATOM   24164 O  O   . CYS   N  14 138 ? 32.633  -146.595 78.102  1.00 88.17  ? 138 CYS   N O   1 
ATOM   24165 C  CB  . CYS   N  14 138 ? 34.412  -146.456 75.338  1.00 86.68  ? 138 CYS   N CB  1 
ATOM   24166 S  SG  . CYS   N  14 138 ? 36.155  -146.314 74.866  1.00 88.07  ? 138 CYS   N SG  1 
ATOM   24167 N  N   . ASP   N  14 139 ? 31.764  -147.830 76.390  1.00 86.65  ? 139 ASP   N N   1 
ATOM   24168 C  CA  . ASP   N  14 139 ? 30.341  -147.783 76.821  1.00 87.48  ? 139 ASP   N CA  1 
ATOM   24169 C  C   . ASP   N  14 139 ? 30.196  -148.448 78.194  1.00 87.75  ? 139 ASP   N C   1 
ATOM   24170 O  O   . ASP   N  14 139 ? 29.405  -147.946 79.015  1.00 85.69  ? 139 ASP   N O   1 
ATOM   24171 C  CB  . ASP   N  14 139 ? 29.423  -148.473 75.811  1.00 87.45  ? 139 ASP   N CB  1 
ATOM   24172 C  CG  . ASP   N  14 139 ? 27.954  -148.387 76.183  1.00 90.58  ? 139 ASP   N CG  1 
ATOM   24173 O  OD1 . ASP   N  14 139 ? 27.465  -147.258 76.364  1.00 93.11  ? 139 ASP   N OD1 1 
ATOM   24174 O  OD2 . ASP   N  14 139 ? 27.313  -149.447 76.305  1.00 92.54  ? 139 ASP   N OD2 1 
ATOM   24175 N  N   . LYS   N  14 140 ? 30.925  -149.543 78.417  1.00 87.72  ? 140 LYS   N N   1 
ATOM   24176 C  CA  . LYS   N  14 140 ? 30.844  -150.367 79.651  1.00 93.02  ? 140 LYS   N CA  1 
ATOM   24177 C  C   . LYS   N  14 140 ? 31.572  -149.680 80.809  1.00 92.91  ? 140 LYS   N C   1 
ATOM   24178 O  O   . LYS   N  14 140 ? 31.202  -149.962 81.961  1.00 95.82  ? 140 LYS   N O   1 
ATOM   24179 C  CB  . LYS   N  14 140 ? 31.435  -151.759 79.411  1.00 95.44  ? 140 LYS   N CB  1 
ATOM   24180 C  CG  . LYS   N  14 140 ? 30.465  -152.768 78.814  1.00 98.07  ? 140 LYS   N CG  1 
ATOM   24181 C  CD  . LYS   N  14 140 ? 29.331  -153.114 79.750  1.00 101.13 ? 140 LYS   N CD  1 
ATOM   24182 C  CE  . LYS   N  14 140 ? 28.504  -154.284 79.271  1.00 102.45 ? 140 LYS   N CE  1 
ATOM   24183 N  NZ  . LYS   N  14 140 ? 27.202  -154.333 79.973  1.00 105.70 ? 140 LYS   N NZ  1 
ATOM   24184 N  N   . ASN   N  14 141 ? 32.558  -148.823 80.522  1.00 96.67  ? 141 ASN   N N   1 
ATOM   24185 C  CA  . ASN   N  14 141 ? 33.514  -148.298 81.537  1.00 99.78  ? 141 ASN   N CA  1 
ATOM   24186 C  C   . ASN   N  14 141 ? 33.268  -146.812 81.844  1.00 100.67 ? 141 ASN   N C   1 
ATOM   24187 O  O   . ASN   N  14 141 ? 33.560  -146.416 82.990  1.00 106.57 ? 141 ASN   N O   1 
ATOM   24188 C  CB  . ASN   N  14 141 ? 34.961  -148.566 81.116  1.00 99.37  ? 141 ASN   N CB  1 
ATOM   24189 C  CG  . ASN   N  14 141 ? 35.409  -149.971 81.455  1.00 100.46 ? 141 ASN   N CG  1 
ATOM   24190 O  OD1 . ASN   N  14 141 ? 35.517  -150.822 80.576  1.00 98.26  ? 141 ASN   N OD1 1 
ATOM   24191 N  ND2 . ASN   N  14 141 ? 35.653  -150.225 82.732  1.00 103.27 ? 141 ASN   N ND2 1 
ATOM   24192 N  N   . PHE   N  14 142 ? 32.767  -146.010 80.896  1.00 98.34  ? 142 PHE   N N   1 
ATOM   24193 C  CA  . PHE   N  14 142 ? 32.548  -144.554 81.105  1.00 98.46  ? 142 PHE   N CA  1 
ATOM   24194 C  C   . PHE   N  14 142 ? 31.511  -144.342 82.214  1.00 99.93  ? 142 PHE   N C   1 
ATOM   24195 O  O   . PHE   N  14 142 ? 30.467  -145.023 82.209  1.00 101.76 ? 142 PHE   N O   1 
ATOM   24196 C  CB  . PHE   N  14 142 ? 32.092  -143.830 79.833  1.00 98.63  ? 142 PHE   N CB  1 
ATOM   24197 C  CG  . PHE   N  14 142 ? 31.697  -142.392 80.069  1.00 98.28  ? 142 PHE   N CG  1 
ATOM   24198 C  CD1 . PHE   N  14 142 ? 32.659  -141.398 80.171  1.00 97.92  ? 142 PHE   N CD1 1 
ATOM   24199 C  CD2 . PHE   N  14 142 ? 30.365  -142.034 80.228  1.00 100.65 ? 142 PHE   N CD2 1 
ATOM   24200 C  CE1 . PHE   N  14 142 ? 32.298  -140.079 80.408  1.00 98.68  ? 142 PHE   N CE1 1 
ATOM   24201 C  CE2 . PHE   N  14 142 ? 30.006  -140.715 80.463  1.00 100.66 ? 142 PHE   N CE2 1 
ATOM   24202 C  CZ  . PHE   N  14 142 ? 30.973  -139.740 80.554  1.00 99.80  ? 142 PHE   N CZ  1 
ATOM   24203 N  N   . ARG   N  14 143 ? 31.814  -143.419 83.131  1.00 101.75 ? 143 ARG   N N   1 
ATOM   24204 C  CA  . ARG   N  14 143 ? 30.886  -142.876 84.158  1.00 104.28 ? 143 ARG   N CA  1 
ATOM   24205 C  C   . ARG   N  14 143 ? 30.973  -141.344 84.128  1.00 102.33 ? 143 ARG   N C   1 
ATOM   24206 O  O   . ARG   N  14 143 ? 32.070  -140.816 83.859  1.00 99.86  ? 143 ARG   N O   1 
ATOM   24207 C  CB  . ARG   N  14 143 ? 31.253  -143.412 85.544  1.00 103.65 ? 143 ARG   N CB  1 
ATOM   24208 C  CG  . ARG   N  14 143 ? 31.107  -144.918 85.697  1.00 107.19 ? 143 ARG   N CG  1 
ATOM   24209 C  CD  . ARG   N  14 143 ? 31.739  -145.407 86.985  1.00 110.11 ? 143 ARG   N CD  1 
ATOM   24210 N  NE  . ARG   N  14 143 ? 33.198  -145.441 86.899  1.00 112.44 ? 143 ARG   N NE  1 
ATOM   24211 C  CZ  . ARG   N  14 143 ? 34.044  -144.633 87.544  1.00 112.10 ? 143 ARG   N CZ  1 
ATOM   24212 N  NH1 . ARG   N  14 143 ? 33.603  -143.690 88.362  1.00 110.97 ? 143 ARG   N NH1 1 
ATOM   24213 N  NH2 . ARG   N  14 143 ? 35.347  -144.784 87.371  1.00 109.36 ? 143 ARG   N NH2 1 
ATOM   24214 N  N   . GLU   N  14 144 ? 29.862  -140.651 84.386  1.00 102.82 ? 144 GLU   N N   1 
ATOM   24215 C  CA  . GLU   N  14 144 ? 29.830  -139.166 84.442  1.00 106.32 ? 144 GLU   N CA  1 
ATOM   24216 C  C   . GLU   N  14 144 ? 30.409  -138.710 85.785  1.00 104.19 ? 144 GLU   N C   1 
ATOM   24217 O  O   . GLU   N  14 144 ? 30.275  -139.455 86.771  1.00 106.47 ? 144 GLU   N O   1 
ATOM   24218 C  CB  . GLU   N  14 144 ? 28.412  -138.633 84.216  1.00 107.62 ? 144 GLU   N CB  1 
ATOM   24219 C  CG  . GLU   N  14 144 ? 28.186  -138.121 82.803  1.00 108.58 ? 144 GLU   N CG  1 
ATOM   24220 C  CD  . GLU   N  14 144 ? 26.734  -137.893 82.416  1.00 112.21 ? 144 GLU   N CD  1 
ATOM   24221 O  OE1 . GLU   N  14 144 ? 26.497  -137.393 81.296  1.00 114.26 ? 144 GLU   N OE1 1 
ATOM   24222 O  OE2 . GLU   N  14 144 ? 25.841  -138.215 83.230  1.00 113.57 ? 144 GLU   N OE2 1 
ATOM   24223 N  N   . ASN   N  14 145 ? 31.047  -137.537 85.796  1.00 108.12 ? 145 ASN   N N   1 
ATOM   24224 C  CA  . ASN   N  14 145 ? 31.615  -136.869 86.999  1.00 107.48 ? 145 ASN   N CA  1 
ATOM   24225 C  C   . ASN   N  14 145 ? 32.740  -137.725 87.593  1.00 105.47 ? 145 ASN   N C   1 
ATOM   24226 O  O   . ASN   N  14 145 ? 32.830  -137.798 88.834  1.00 105.57 ? 145 ASN   N O   1 
ATOM   24227 C  CB  . ASN   N  14 145 ? 30.539  -136.566 88.045  1.00 111.89 ? 145 ASN   N CB  1 
ATOM   24228 C  CG  . ASN   N  14 145 ? 29.440  -135.670 87.516  1.00 110.03 ? 145 ASN   N CG  1 
ATOM   24229 O  OD1 . ASN   N  14 145 ? 28.268  -136.034 87.553  1.00 118.08 ? 145 ASN   N OD1 1 
ATOM   24230 N  ND2 . ASN   N  14 145 ? 29.806  -134.500 87.017  1.00 111.48 ? 145 ASN   N ND2 1 
ATOM   24231 N  N   . MET   N  14 146 ? 33.575  -138.328 86.742  1.00 104.29 ? 146 MET   N N   1 
ATOM   24232 C  CA  . MET   N  14 146 ? 34.818  -139.030 87.163  1.00 104.10 ? 146 MET   N CA  1 
ATOM   24233 C  C   . MET   N  14 146 ? 35.814  -137.992 87.697  1.00 102.86 ? 146 MET   N C   1 
ATOM   24234 O  O   . MET   N  14 146 ? 35.602  -136.789 87.453  1.00 102.70 ? 146 MET   N O   1 
ATOM   24235 C  CB  . MET   N  14 146 ? 35.451  -139.799 85.997  1.00 108.10 ? 146 MET   N CB  1 
ATOM   24236 C  CG  . MET   N  14 146 ? 34.785  -141.134 85.724  1.00 106.28 ? 146 MET   N CG  1 
ATOM   24237 S  SD  . MET   N  14 146 ? 35.625  -142.090 84.433  1.00 105.36 ? 146 MET   N SD  1 
ATOM   24238 C  CE  . MET   N  14 146 ? 35.215  -141.131 82.976  1.00 105.83 ? 146 MET   N CE  1 
ATOM   24239 N  N   . SER   N  14 147 ? 36.846  -138.441 88.417  1.00 98.37  ? 147 SER   N N   1 
ATOM   24240 C  CA  . SER   N  14 147 ? 37.983  -137.599 88.873  1.00 96.52  ? 147 SER   N CA  1 
ATOM   24241 C  C   . SER   N  14 147 ? 39.010  -137.504 87.743  1.00 94.63  ? 147 SER   N C   1 
ATOM   24242 O  O   . SER   N  14 147 ? 38.833  -138.204 86.728  1.00 89.02  ? 147 SER   N O   1 
ATOM   24243 C  CB  . SER   N  14 147 ? 38.599  -138.138 90.134  1.00 95.87  ? 147 SER   N CB  1 
ATOM   24244 O  OG  . SER   N  14 147 ? 39.232  -139.384 89.900  1.00 95.63  ? 147 SER   N OG  1 
ATOM   24245 N  N   . LYS   N  14 148 ? 40.036  -136.668 87.913  1.00 98.18  ? 148 LYS   N N   1 
ATOM   24246 C  CA  . LYS   N  14 148 ? 41.124  -136.484 86.915  1.00 101.77 ? 148 LYS   N CA  1 
ATOM   24247 C  C   . LYS   N  14 148 ? 41.852  -137.820 86.717  1.00 104.32 ? 148 LYS   N C   1 
ATOM   24248 O  O   . LYS   N  14 148 ? 42.006  -138.242 85.554  1.00 100.73 ? 148 LYS   N O   1 
ATOM   24249 C  CB  . LYS   N  14 148 ? 42.094  -135.381 87.353  1.00 106.58 ? 148 LYS   N CB  1 
ATOM   24250 C  CG  . LYS   N  14 148 ? 43.151  -135.007 86.320  1.00 106.79 ? 148 LYS   N CG  1 
ATOM   24251 C  CD  . LYS   N  14 148 ? 44.305  -134.214 86.888  1.00 110.85 ? 148 LYS   N CD  1 
ATOM   24252 C  CE  . LYS   N  14 148 ? 45.517  -134.205 85.980  1.00 113.22 ? 148 LYS   N CE  1 
ATOM   24253 N  NZ  . LYS   N  14 148 ? 46.736  -133.778 86.706  1.00 118.58 ? 148 LYS   N NZ  1 
ATOM   24254 N  N   . GLU   N  14 149 ? 42.254  -138.471 87.813  1.00 105.88 ? 149 GLU   N N   1 
ATOM   24255 C  CA  . GLU   N  14 149 ? 43.061  -139.723 87.789  1.00 110.33 ? 149 GLU   N CA  1 
ATOM   24256 C  C   . GLU   N  14 149 ? 42.246  -140.853 87.145  1.00 104.25 ? 149 GLU   N C   1 
ATOM   24257 O  O   . GLU   N  14 149 ? 42.841  -141.648 86.392  1.00 99.62  ? 149 GLU   N O   1 
ATOM   24258 C  CB  . GLU   N  14 149 ? 43.519  -140.104 89.199  1.00 117.54 ? 149 GLU   N CB  1 
ATOM   24259 C  CG  . GLU   N  14 149 ? 44.665  -139.249 89.717  1.00 126.77 ? 149 GLU   N CG  1 
ATOM   24260 C  CD  . GLU   N  14 149 ? 44.310  -137.810 90.063  1.00 131.50 ? 149 GLU   N CD  1 
ATOM   24261 O  OE1 . GLU   N  14 149 ? 43.147  -137.560 90.446  1.00 137.82 ? 149 GLU   N OE1 1 
ATOM   24262 O  OE2 . GLU   N  14 149 ? 45.195  -136.938 89.945  1.00 134.43 ? 149 GLU   N OE2 1 
ATOM   24263 N  N   . GLU   N  14 150 ? 40.940  -140.913 87.426  1.00 103.45 ? 150 GLU   N N   1 
ATOM   24264 C  CA  . GLU   N  14 150 ? 40.006  -141.923 86.857  1.00 103.57 ? 150 GLU   N CA  1 
ATOM   24265 C  C   . GLU   N  14 150 ? 39.893  -141.719 85.342  1.00 103.70 ? 150 GLU   N C   1 
ATOM   24266 O  O   . GLU   N  14 150 ? 39.984  -142.724 84.604  1.00 105.59 ? 150 GLU   N O   1 
ATOM   24267 C  CB  . GLU   N  14 150 ? 38.628  -141.821 87.511  1.00 104.48 ? 150 GLU   N CB  1 
ATOM   24268 C  CG  . GLU   N  14 150 ? 38.586  -142.376 88.922  1.00 108.73 ? 150 GLU   N CG  1 
ATOM   24269 C  CD  . GLU   N  14 150 ? 37.253  -142.209 89.631  1.00 113.29 ? 150 GLU   N CD  1 
ATOM   24270 O  OE1 . GLU   N  14 150 ? 36.531  -141.241 89.318  1.00 115.81 ? 150 GLU   N OE1 1 
ATOM   24271 O  OE2 . GLU   N  14 150 ? 36.938  -143.053 90.491  1.00 122.51 ? 150 GLU   N OE2 1 
ATOM   24272 N  N   . THR   N  14 151 ? 39.695  -140.471 84.904  1.00 101.01 ? 151 THR   N N   1 
ATOM   24273 C  CA  . THR   N  14 151 ? 39.504  -140.094 83.477  1.00 97.55  ? 151 THR   N CA  1 
ATOM   24274 C  C   . THR   N  14 151 ? 40.797  -140.357 82.698  1.00 93.00  ? 151 THR   N C   1 
ATOM   24275 O  O   . THR   N  14 151 ? 40.694  -140.791 81.535  1.00 89.72  ? 151 THR   N O   1 
ATOM   24276 C  CB  . THR   N  14 151 ? 39.061  -138.634 83.327  1.00 96.31  ? 151 THR   N CB  1 
ATOM   24277 O  OG1 . THR   N  14 151 ? 37.956  -138.417 84.205  1.00 96.85  ? 151 THR   N OG1 1 
ATOM   24278 C  CG2 . THR   N  14 151 ? 38.664  -138.291 81.907  1.00 95.42  ? 151 THR   N CG2 1 
ATOM   24279 N  N   . VAL   N  14 152 ? 41.960  -140.091 83.301  1.00 93.38  ? 152 VAL   N N   1 
ATOM   24280 C  CA  . VAL   N  14 152 ? 43.285  -140.360 82.668  1.00 94.58  ? 152 VAL   N CA  1 
ATOM   24281 C  C   . VAL   N  14 152 ? 43.418  -141.869 82.449  1.00 95.22  ? 152 VAL   N C   1 
ATOM   24282 O  O   . VAL   N  14 152 ? 43.842  -142.266 81.351  1.00 100.49 ? 152 VAL   N O   1 
ATOM   24283 C  CB  . VAL   N  14 152 ? 44.464  -139.805 83.488  1.00 95.41  ? 152 VAL   N CB  1 
ATOM   24284 C  CG1 . VAL   N  14 152 ? 45.795  -140.394 83.038  1.00 92.33  ? 152 VAL   N CG1 1 
ATOM   24285 C  CG2 . VAL   N  14 152 ? 44.515  -138.286 83.430  1.00 96.39  ? 152 VAL   N CG2 1 
ATOM   24286 N  N   . ASP   N  14 153 ? 43.063  -142.667 83.458  1.00 99.14  ? 153 ASP   N N   1 
ATOM   24287 C  CA  . ASP   N  14 153 ? 43.122  -144.153 83.403  1.00 101.54 ? 153 ASP   N CA  1 
ATOM   24288 C  C   . ASP   N  14 153 ? 42.158  -144.658 82.324  1.00 98.23  ? 153 ASP   N C   1 
ATOM   24289 O  O   . ASP   N  14 153 ? 42.576  -145.526 81.536  1.00 100.78 ? 153 ASP   N O   1 
ATOM   24290 C  CB  . ASP   N  14 153 ? 42.822  -144.781 84.768  1.00 108.06 ? 153 ASP   N CB  1 
ATOM   24291 C  CG  . ASP   N  14 153 ? 43.965  -144.671 85.765  1.00 111.42 ? 153 ASP   N CG  1 
ATOM   24292 O  OD1 . ASP   N  14 153 ? 45.106  -144.410 85.331  1.00 114.00 ? 153 ASP   N OD1 1 
ATOM   24293 O  OD2 . ASP   N  14 153 ? 43.705  -144.848 86.970  1.00 117.46 ? 153 ASP   N OD2 1 
ATOM   24294 N  N   . PHE   N  14 154 ? 40.931  -144.127 82.284  1.00 94.48  ? 154 PHE   N N   1 
ATOM   24295 C  CA  . PHE   N  14 154 ? 39.878  -144.507 81.305  1.00 93.59  ? 154 PHE   N CA  1 
ATOM   24296 C  C   . PHE   N  14 154 ? 40.398  -144.311 79.876  1.00 95.69  ? 154 PHE   N C   1 
ATOM   24297 O  O   . PHE   N  14 154 ? 40.272  -145.248 79.063  1.00 94.41  ? 154 PHE   N O   1 
ATOM   24298 C  CB  . PHE   N  14 154 ? 38.593  -143.705 81.524  1.00 93.45  ? 154 PHE   N CB  1 
ATOM   24299 C  CG  . PHE   N  14 154 ? 37.531  -143.944 80.480  1.00 91.04  ? 154 PHE   N CG  1 
ATOM   24300 C  CD1 . PHE   N  14 154 ? 36.997  -145.209 80.290  1.00 89.77  ? 154 PHE   N CD1 1 
ATOM   24301 C  CD2 . PHE   N  14 154 ? 37.069  -142.908 79.683  1.00 91.64  ? 154 PHE   N CD2 1 
ATOM   24302 C  CE1 . PHE   N  14 154 ? 36.023  -145.431 79.328  1.00 89.56  ? 154 PHE   N CE1 1 
ATOM   24303 C  CE2 . PHE   N  14 154 ? 36.094  -143.131 78.722  1.00 90.71  ? 154 PHE   N CE2 1 
ATOM   24304 C  CZ  . PHE   N  14 154 ? 35.573  -144.392 78.546  1.00 90.07  ? 154 PHE   N CZ  1 
ATOM   24305 N  N   . ILE   N  14 155 ? 40.954  -143.131 79.582  1.00 94.33  ? 155 ILE   N N   1 
ATOM   24306 C  CA  . ILE   N  14 155 ? 41.521  -142.784 78.243  1.00 95.19  ? 155 ILE   N CA  1 
ATOM   24307 C  C   . ILE   N  14 155 ? 42.721  -143.699 77.963  1.00 98.05  ? 155 ILE   N C   1 
ATOM   24308 O  O   . ILE   N  14 155 ? 42.806  -144.227 76.834  1.00 98.14  ? 155 ILE   N O   1 
ATOM   24309 C  CB  . ILE   N  14 155 ? 41.887  -141.287 78.155  1.00 93.92  ? 155 ILE   N CB  1 
ATOM   24310 C  CG1 . ILE   N  14 155 ? 40.632  -140.410 78.190  1.00 95.72  ? 155 ILE   N CG1 1 
ATOM   24311 C  CG2 . ILE   N  14 155 ? 42.733  -141.006 76.920  1.00 92.09  ? 155 ILE   N CG2 1 
ATOM   24312 C  CD1 . ILE   N  14 155 ? 40.904  -138.926 78.322  1.00 97.69  ? 155 ILE   N CD1 1 
ATOM   24313 N  N   . LYS   N  14 156 ? 43.600  -143.888 78.954  1.00 99.33  ? 156 LYS   N N   1 
ATOM   24314 C  CA  . LYS   N  14 156 ? 44.869  -144.654 78.811  1.00 99.98  ? 156 LYS   N CA  1 
ATOM   24315 C  C   . LYS   N  14 156 ? 44.559  -146.112 78.451  1.00 98.33  ? 156 LYS   N C   1 
ATOM   24316 O  O   . LYS   N  14 156 ? 45.185  -146.627 77.507  1.00 98.48  ? 156 LYS   N O   1 
ATOM   24317 C  CB  . LYS   N  14 156 ? 45.706  -144.589 80.092  1.00 102.24 ? 156 LYS   N CB  1 
ATOM   24318 C  CG  . LYS   N  14 156 ? 47.180  -144.917 79.901  1.00 104.24 ? 156 LYS   N CG  1 
ATOM   24319 C  CD  . LYS   N  14 156 ? 47.918  -145.166 81.192  1.00 107.36 ? 156 LYS   N CD  1 
ATOM   24320 C  CE  . LYS   N  14 156 ? 48.032  -143.930 82.058  1.00 111.32 ? 156 LYS   N CE  1 
ATOM   24321 N  NZ  . LYS   N  14 156 ? 48.551  -144.260 83.406  1.00 113.90 ? 156 LYS   N NZ  1 
ATOM   24322 N  N   . HIS   N  14 157 ? 43.636  -146.743 79.185  1.00 96.32  ? 157 HIS   N N   1 
ATOM   24323 C  CA  . HIS   N  14 157 ? 43.190  -148.147 78.973  1.00 95.09  ? 157 HIS   N CA  1 
ATOM   24324 C  C   . HIS   N  14 157 ? 42.480  -148.274 77.620  1.00 92.96  ? 157 HIS   N C   1 
ATOM   24325 O  O   . HIS   N  14 157 ? 42.731  -149.276 76.918  1.00 94.52  ? 157 HIS   N O   1 
ATOM   24326 C  CB  . HIS   N  14 157 ? 42.292  -148.616 80.128  1.00 94.43  ? 157 HIS   N CB  1 
ATOM   24327 C  CG  . HIS   N  14 157 ? 43.042  -149.058 81.341  1.00 96.93  ? 157 HIS   N CG  1 
ATOM   24328 N  ND1 . HIS   N  14 157 ? 43.555  -148.167 82.265  1.00 96.70  ? 157 HIS   N ND1 1 
ATOM   24329 C  CD2 . HIS   N  14 157 ? 43.358  -150.291 81.791  1.00 97.65  ? 157 HIS   N CD2 1 
ATOM   24330 C  CE1 . HIS   N  14 157 ? 44.160  -148.833 83.227  1.00 98.83  ? 157 HIS   N CE1 1 
ATOM   24331 N  NE2 . HIS   N  14 157 ? 44.053  -150.138 82.959  1.00 97.24  ? 157 HIS   N NE2 1 
ATOM   24332 N  N   . SER   N  14 158 ? 41.625  -147.304 77.276  1.00 90.04  ? 158 SER   N N   1 
ATOM   24333 C  CA  . SER   N  14 158 ? 40.825  -147.279 76.022  1.00 87.44  ? 158 SER   N CA  1 
ATOM   24334 C  C   . SER   N  14 158 ? 41.757  -147.205 74.806  1.00 85.81  ? 158 SER   N C   1 
ATOM   24335 O  O   . SER   N  14 158 ? 41.667  -148.096 73.948  1.00 86.41  ? 158 SER   N O   1 
ATOM   24336 C  CB  . SER   N  14 158 ? 39.830  -146.148 76.023  1.00 85.68  ? 158 SER   N CB  1 
ATOM   24337 O  OG  . SER   N  14 158 ? 38.857  -146.335 77.039  1.00 85.85  ? 158 SER   N OG  1 
ATOM   24338 N  N   . LEU   N  14 159 ? 42.620  -146.187 74.735  1.00 85.97  ? 159 LEU   N N   1 
ATOM   24339 C  CA  . LEU   N  14 159 ? 43.561  -145.995 73.596  1.00 86.03  ? 159 LEU   N CA  1 
ATOM   24340 C  C   . LEU   N  14 159 ? 44.561  -147.160 73.548  1.00 86.84  ? 159 LEU   N C   1 
ATOM   24341 O  O   . LEU   N  14 159 ? 45.010  -147.498 72.436  1.00 83.03  ? 159 LEU   N O   1 
ATOM   24342 C  CB  . LEU   N  14 159 ? 44.282  -144.649 73.726  1.00 88.55  ? 159 LEU   N CB  1 
ATOM   24343 C  CG  . LEU   N  14 159 ? 43.416  -143.396 73.576  1.00 90.34  ? 159 LEU   N CG  1 
ATOM   24344 C  CD1 . LEU   N  14 159 ? 44.289  -142.150 73.586  1.00 92.83  ? 159 LEU   N CD1 1 
ATOM   24345 C  CD2 . LEU   N  14 159 ? 42.572  -143.432 72.309  1.00 88.21  ? 159 LEU   N CD2 1 
ATOM   24346 N  N   . SER   N  14 160 ? 44.892  -147.752 74.700  1.00 88.11  ? 160 SER   N N   1 
ATOM   24347 C  CA  . SER   N  14 160 ? 45.771  -148.947 74.813  1.00 92.04  ? 160 SER   N CA  1 
ATOM   24348 C  C   . SER   N  14 160 ? 45.189  -150.095 73.976  1.00 90.22  ? 160 SER   N C   1 
ATOM   24349 O  O   . SER   N  14 160 ? 45.946  -150.711 73.196  1.00 89.60  ? 160 SER   N O   1 
ATOM   24350 C  CB  . SER   N  14 160 ? 45.959  -149.358 76.251  1.00 96.36  ? 160 SER   N CB  1 
ATOM   24351 O  OG  . SER   N  14 160 ? 46.854  -150.453 76.351  1.00 102.30 ? 160 SER   N OG  1 
ATOM   24352 N  N   . GLN   N  14 161 ? 43.889  -150.361 74.128  1.00 87.86  ? 161 GLN   N N   1 
ATOM   24353 C  CA  . GLN   N  14 161 ? 43.166  -151.416 73.369  1.00 87.68  ? 161 GLN   N CA  1 
ATOM   24354 C  C   . GLN   N  14 161 ? 43.036  -150.984 71.904  1.00 88.69  ? 161 GLN   N C   1 
ATOM   24355 O  O   . GLN   N  14 161 ? 43.380  -151.798 71.030  1.00 92.21  ? 161 GLN   N O   1 
ATOM   24356 C  CB  . GLN   N  14 161 ? 41.807  -151.710 74.009  1.00 86.84  ? 161 GLN   N CB  1 
ATOM   24357 C  CG  . GLN   N  14 161 ? 41.910  -152.498 75.309  1.00 88.64  ? 161 GLN   N CG  1 
ATOM   24358 C  CD  . GLN   N  14 161 ? 42.652  -153.807 75.165  1.00 87.54  ? 161 GLN   N CD  1 
ATOM   24359 O  OE1 . GLN   N  14 161 ? 43.600  -154.090 75.893  1.00 88.71  ? 161 GLN   N OE1 1 
ATOM   24360 N  NE2 . GLN   N  14 161 ? 42.229  -154.623 74.219  1.00 83.91  ? 161 GLN   N NE2 1 
ATOM   24361 N  N   . ALA   N  14 162 ? 42.583  -149.753 71.641  1.00 86.07  ? 162 ALA   N N   1 
ATOM   24362 C  CA  . ALA   N  14 162 ? 42.456  -149.192 70.275  1.00 83.17  ? 162 ALA   N CA  1 
ATOM   24363 C  C   . ALA   N  14 162 ? 43.786  -149.375 69.531  1.00 84.22  ? 162 ALA   N C   1 
ATOM   24364 O  O   . ALA   N  14 162 ? 43.751  -149.867 68.388  1.00 84.48  ? 162 ALA   N O   1 
ATOM   24365 C  CB  . ALA   N  14 162 ? 42.037  -147.744 70.324  1.00 82.09  ? 162 ALA   N CB  1 
ATOM   24366 N  N   . ILE   N  14 163 ? 44.911  -149.030 70.170  1.00 84.08  ? 163 ILE   N N   1 
ATOM   24367 C  CA  . ILE   N  14 163 ? 46.284  -149.147 69.586  1.00 85.58  ? 163 ILE   N CA  1 
ATOM   24368 C  C   . ILE   N  14 163 ? 46.623  -150.625 69.356  1.00 85.94  ? 163 ILE   N C   1 
ATOM   24369 O  O   . ILE   N  14 163 ? 47.246  -150.924 68.316  1.00 85.91  ? 163 ILE   N O   1 
ATOM   24370 C  CB  . ILE   N  14 163 ? 47.340  -148.450 70.470  1.00 86.33  ? 163 ILE   N CB  1 
ATOM   24371 C  CG1 . ILE   N  14 163 ? 47.315  -146.933 70.264  1.00 87.40  ? 163 ILE   N CG1 1 
ATOM   24372 C  CG2 . ILE   N  14 163 ? 48.729  -149.022 70.219  1.00 85.77  ? 163 ILE   N CG2 1 
ATOM   24373 C  CD1 . ILE   N  14 163 ? 48.097  -146.149 71.293  1.00 90.34  ? 163 ILE   N CD1 1 
ATOM   24374 N  N   . LYS   N  14 164 ? 46.253  -151.503 70.295  1.00 87.21  ? 164 LYS   N N   1 
ATOM   24375 C  CA  . LYS   N  14 164 ? 46.628  -152.943 70.287  1.00 89.20  ? 164 LYS   N CA  1 
ATOM   24376 C  C   . LYS   N  14 164 ? 46.098  -153.633 69.024  1.00 89.54  ? 164 LYS   N C   1 
ATOM   24377 O  O   . LYS   N  14 164 ? 46.851  -154.436 68.439  1.00 90.13  ? 164 LYS   N O   1 
ATOM   24378 C  CB  . LYS   N  14 164 ? 46.079  -153.669 71.518  1.00 90.53  ? 164 LYS   N CB  1 
ATOM   24379 C  CG  . LYS   N  14 164 ? 46.448  -155.143 71.579  1.00 91.63  ? 164 LYS   N CG  1 
ATOM   24380 C  CD  . LYS   N  14 164 ? 46.025  -155.841 72.844  1.00 95.91  ? 164 LYS   N CD  1 
ATOM   24381 C  CE  . LYS   N  14 164 ? 46.486  -157.283 72.860  1.00 100.61 ? 164 LYS   N CE  1 
ATOM   24382 N  NZ  . LYS   N  14 164 ? 46.363  -157.891 74.205  1.00 105.33 ? 164 LYS   N NZ  1 
ATOM   24383 N  N   . TRP   N  14 165 ? 44.849  -153.350 68.641  1.00 88.33  ? 165 TRP   N N   1 
ATOM   24384 C  CA  . TRP   N  14 165 ? 44.128  -154.030 67.531  1.00 87.66  ? 165 TRP   N CA  1 
ATOM   24385 C  C   . TRP   N  14 165 ? 44.314  -153.272 66.214  1.00 87.48  ? 165 TRP   N C   1 
ATOM   24386 O  O   . TRP   N  14 165 ? 44.563  -153.938 65.194  1.00 90.40  ? 165 TRP   N O   1 
ATOM   24387 C  CB  . TRP   N  14 165 ? 42.648  -154.200 67.883  1.00 87.00  ? 165 TRP   N CB  1 
ATOM   24388 C  CG  . TRP   N  14 165 ? 42.453  -154.985 69.141  1.00 87.69  ? 165 TRP   N CG  1 
ATOM   24389 C  CD1 . TRP   N  14 165 ? 41.993  -154.522 70.338  1.00 86.16  ? 165 TRP   N CD1 1 
ATOM   24390 C  CD2 . TRP   N  14 165 ? 42.760  -156.377 69.337  1.00 88.44  ? 165 TRP   N CD2 1 
ATOM   24391 N  NE1 . TRP   N  14 165 ? 41.972  -155.533 71.259  1.00 87.04  ? 165 TRP   N NE1 1 
ATOM   24392 C  CE2 . TRP   N  14 165 ? 42.437  -156.680 70.675  1.00 87.14  ? 165 TRP   N CE2 1 
ATOM   24393 C  CE3 . TRP   N  14 165 ? 43.261  -157.395 68.516  1.00 88.31  ? 165 TRP   N CE3 1 
ATOM   24394 C  CZ2 . TRP   N  14 165 ? 42.603  -157.957 71.205  1.00 88.84  ? 165 TRP   N CZ2 1 
ATOM   24395 C  CZ3 . TRP   N  14 165 ? 43.426  -158.656 69.043  1.00 88.84  ? 165 TRP   N CZ3 1 
ATOM   24396 C  CH2 . TRP   N  14 165 ? 43.099  -158.931 70.370  1.00 90.10  ? 165 TRP   N CH2 1 
ATOM   24397 N  N   . ASP   N  14 166 ? 44.185  -151.942 66.232  1.00 86.15  ? 166 ASP   N N   1 
ATOM   24398 C  CA  . ASP   N  14 166 ? 44.309  -151.092 65.018  1.00 84.83  ? 166 ASP   N CA  1 
ATOM   24399 C  C   . ASP   N  14 166 ? 45.790  -150.950 64.651  1.00 81.81  ? 166 ASP   N C   1 
ATOM   24400 O  O   . ASP   N  14 166 ? 46.563  -150.429 65.475  1.00 80.79  ? 166 ASP   N O   1 
ATOM   24401 C  CB  . ASP   N  14 166 ? 43.644  -149.729 65.216  1.00 85.97  ? 166 ASP   N CB  1 
ATOM   24402 C  CG  . ASP   N  14 166 ? 43.661  -148.849 63.977  1.00 89.60  ? 166 ASP   N CG  1 
ATOM   24403 O  OD1 . ASP   N  14 166 ? 43.691  -149.406 62.857  1.00 87.62  ? 166 ASP   N OD1 1 
ATOM   24404 O  OD2 . ASP   N  14 166 ? 43.644  -147.614 64.144  1.00 89.08  ? 166 ASP   N OD2 1 
ATOM   24405 N  N   . GLY   N  14 167 ? 46.162  -151.408 63.454  1.00 81.21  ? 167 GLY   N N   1 
ATOM   24406 C  CA  . GLY   N  14 167 ? 47.518  -151.265 62.892  1.00 81.46  ? 167 GLY   N CA  1 
ATOM   24407 C  C   . GLY   N  14 167 ? 47.836  -149.814 62.584  1.00 79.81  ? 167 GLY   N C   1 
ATOM   24408 O  O   . GLY   N  14 167 ? 49.021  -149.442 62.643  1.00 76.92  ? 167 GLY   N O   1 
ATOM   24409 N  N   . SER   N  14 168 ? 46.807  -149.026 62.260  1.00 80.66  ? 168 SER   N N   1 
ATOM   24410 C  CA  . SER   N  14 168 ? 46.908  -147.588 61.901  1.00 83.51  ? 168 SER   N CA  1 
ATOM   24411 C  C   . SER   N  14 168 ? 47.226  -146.746 63.142  1.00 83.65  ? 168 SER   N C   1 
ATOM   24412 O  O   . SER   N  14 168 ? 47.733  -145.630 62.957  1.00 87.58  ? 168 SER   N O   1 
ATOM   24413 C  CB  . SER   N  14 168 ? 45.647  -147.110 61.223  1.00 83.94  ? 168 SER   N CB  1 
ATOM   24414 O  OG  . SER   N  14 168 ? 45.195  -148.056 60.261  1.00 83.94  ? 168 SER   N OG  1 
ATOM   24415 N  N   . SER   N  14 169 ? 46.927  -147.250 64.346  1.00 83.10  ? 169 SER   N N   1 
ATOM   24416 C  CA  . SER   N  14 169 ? 47.189  -146.571 65.644  1.00 82.52  ? 169 SER   N CA  1 
ATOM   24417 C  C   . SER   N  14 169 ? 48.460  -147.135 66.287  1.00 85.81  ? 169 SER   N C   1 
ATOM   24418 O  O   . SER   N  14 169 ? 48.765  -148.319 66.053  1.00 88.65  ? 169 SER   N O   1 
ATOM   24419 C  CB  . SER   N  14 169 ? 46.009  -146.697 66.570  1.00 81.91  ? 169 SER   N CB  1 
ATOM   24420 O  OG  . SER   N  14 169 ? 44.805  -146.365 65.896  1.00 78.96  ? 169 SER   N OG  1 
ATOM   24421 N  N   . GLY   N  14 170 ? 49.171  -146.316 67.069  1.00 86.44  ? 170 GLY   N N   1 
ATOM   24422 C  CA  . GLY   N  14 170 ? 50.405  -146.723 67.768  1.00 88.10  ? 170 GLY   N CA  1 
ATOM   24423 C  C   . GLY   N  14 170 ? 51.197  -145.545 68.307  1.00 87.34  ? 170 GLY   N C   1 
ATOM   24424 O  O   . GLY   N  14 170 ? 50.625  -144.444 68.434  1.00 83.82  ? 170 GLY   N O   1 
ATOM   24425 N  N   . GLY   N  14 171 ? 52.472  -145.782 68.624  1.00 86.62  ? 171 GLY   N N   1 
ATOM   24426 C  CA  . GLY   N  14 171 ? 53.402  -144.784 69.185  1.00 85.46  ? 171 GLY   N CA  1 
ATOM   24427 C  C   . GLY   N  14 171 ? 53.090  -144.474 70.640  1.00 86.70  ? 171 GLY   N C   1 
ATOM   24428 O  O   . GLY   N  14 171 ? 52.860  -145.429 71.405  1.00 83.46  ? 171 GLY   N O   1 
ATOM   24429 N  N   . VAL   N  14 172 ? 53.082  -143.185 71.005  1.00 85.89  ? 172 VAL   N N   1 
ATOM   24430 C  CA  . VAL   N  14 172 ? 52.791  -142.691 72.385  1.00 84.82  ? 172 VAL   N CA  1 
ATOM   24431 C  C   . VAL   N  14 172 ? 51.305  -142.331 72.485  1.00 84.21  ? 172 VAL   N C   1 
ATOM   24432 O  O   . VAL   N  14 172 ? 50.675  -142.078 71.434  1.00 82.35  ? 172 VAL   N O   1 
ATOM   24433 C  CB  . VAL   N  14 172 ? 53.677  -141.491 72.773  1.00 85.34  ? 172 VAL   N CB  1 
ATOM   24434 C  CG1 . VAL   N  14 172 ? 55.150  -141.856 72.752  1.00 86.88  ? 172 VAL   N CG1 1 
ATOM   24435 C  CG2 . VAL   N  14 172 ? 53.426  -140.263 71.909  1.00 85.99  ? 172 VAL   N CG2 1 
ATOM   24436 N  N   . ILE   N  14 173 ? 50.779  -142.318 73.712  1.00 84.90  ? 173 ILE   N N   1 
ATOM   24437 C  CA  . ILE   N  14 173 ? 49.440  -141.754 74.050  1.00 86.65  ? 173 ILE   N CA  1 
ATOM   24438 C  C   . ILE   N  14 173 ? 49.666  -140.343 74.595  1.00 84.52  ? 173 ILE   N C   1 
ATOM   24439 O  O   . ILE   N  14 173 ? 50.149  -140.222 75.732  1.00 88.49  ? 173 ILE   N O   1 
ATOM   24440 C  CB  . ILE   N  14 173 ? 48.682  -142.647 75.053  1.00 87.43  ? 173 ILE   N CB  1 
ATOM   24441 C  CG1 . ILE   N  14 173 ? 48.325  -144.002 74.433  1.00 89.26  ? 173 ILE   N CG1 1 
ATOM   24442 C  CG2 . ILE   N  14 173 ? 47.451  -141.930 75.594  1.00 86.06  ? 173 ILE   N CG2 1 
ATOM   24443 C  CD1 . ILE   N  14 173 ? 47.767  -145.013 75.411  1.00 90.20  ? 173 ILE   N CD1 1 
ATOM   24444 N  N   . ARG   N  14 174 ? 49.360  -139.323 73.794  1.00 85.31  ? 174 ARG   N N   1 
ATOM   24445 C  CA  . ARG   N  14 174 ? 49.328  -137.907 74.242  1.00 86.91  ? 174 ARG   N CA  1 
ATOM   24446 C  C   . ARG   N  14 174 ? 47.955  -137.620 74.848  1.00 88.20  ? 174 ARG   N C   1 
ATOM   24447 O  O   . ARG   N  14 174 ? 46.958  -138.189 74.360  1.00 85.05  ? 174 ARG   N O   1 
ATOM   24448 C  CB  . ARG   N  14 174 ? 49.583  -136.943 73.081  1.00 84.78  ? 174 ARG   N CB  1 
ATOM   24449 C  CG  . ARG   N  14 174 ? 50.879  -137.203 72.332  1.00 84.08  ? 174 ARG   N CG  1 
ATOM   24450 C  CD  . ARG   N  14 174 ? 51.221  -136.036 71.435  1.00 82.08  ? 174 ARG   N CD  1 
ATOM   24451 N  NE  . ARG   N  14 174 ? 52.412  -136.283 70.636  1.00 81.56  ? 174 ARG   N NE  1 
ATOM   24452 C  CZ  . ARG   N  14 174 ? 53.665  -136.139 71.061  1.00 82.53  ? 174 ARG   N CZ  1 
ATOM   24453 N  NH1 . ARG   N  14 174 ? 53.918  -135.751 72.302  1.00 83.07  ? 174 ARG   N NH1 1 
ATOM   24454 N  NH2 . ARG   N  14 174 ? 54.670  -136.387 70.239  1.00 82.08  ? 174 ARG   N NH2 1 
ATOM   24455 N  N   . MET   N  14 175 ? 47.918  -136.767 75.871  1.00 91.36  ? 175 MET   N N   1 
ATOM   24456 C  CA  . MET   N  14 175 ? 46.664  -136.274 76.491  1.00 92.79  ? 175 MET   N CA  1 
ATOM   24457 C  C   . MET   N  14 175 ? 46.837  -134.794 76.842  1.00 91.97  ? 175 MET   N C   1 
ATOM   24458 O  O   . MET   N  14 175 ? 47.977  -134.382 77.128  1.00 93.76  ? 175 MET   N O   1 
ATOM   24459 C  CB  . MET   N  14 175 ? 46.314  -137.085 77.742  1.00 98.15  ? 175 MET   N CB  1 
ATOM   24460 C  CG  . MET   N  14 175 ? 45.932  -138.524 77.431  1.00 99.42  ? 175 MET   N CG  1 
ATOM   24461 S  SD  . MET   N  14 175 ? 45.724  -139.544 78.907  1.00 105.54 ? 175 MET   N SD  1 
ATOM   24462 C  CE  . MET   N  14 175 ? 44.373  -138.670 79.691  1.00 107.02 ? 175 MET   N CE  1 
ATOM   24463 N  N   . VAL   N  14 176 ? 45.748  -134.026 76.767  1.00 90.31  ? 176 VAL   N N   1 
ATOM   24464 C  CA  . VAL   N  14 176 ? 45.703  -132.590 77.167  1.00 92.05  ? 176 VAL   N CA  1 
ATOM   24465 C  C   . VAL   N  14 176 ? 44.543  -132.408 78.150  1.00 89.56  ? 176 VAL   N C   1 
ATOM   24466 O  O   . VAL   N  14 176 ? 43.397  -132.719 77.777  1.00 86.73  ? 176 VAL   N O   1 
ATOM   24467 C  CB  . VAL   N  14 176 ? 45.576  -131.662 75.943  1.00 92.78  ? 176 VAL   N CB  1 
ATOM   24468 C  CG1 . VAL   N  14 176 ? 45.270  -130.228 76.347  1.00 95.70  ? 176 VAL   N CG1 1 
ATOM   24469 C  CG2 . VAL   N  14 176 ? 46.824  -131.710 75.077  1.00 93.37  ? 176 VAL   N CG2 1 
ATOM   24470 N  N   . VAL   N  14 177 ? 44.846  -131.921 79.356  1.00 91.22  ? 177 VAL   N N   1 
ATOM   24471 C  CA  . VAL   N  14 177 ? 43.863  -131.708 80.459  1.00 92.42  ? 177 VAL   N CA  1 
ATOM   24472 C  C   . VAL   N  14 177 ? 43.427  -130.239 80.436  1.00 93.15  ? 177 VAL   N C   1 
ATOM   24473 O  O   . VAL   N  14 177 ? 44.302  -129.362 80.557  1.00 94.14  ? 177 VAL   N O   1 
ATOM   24474 C  CB  . VAL   N  14 177 ? 44.458  -132.094 81.826  1.00 93.27  ? 177 VAL   N CB  1 
ATOM   24475 C  CG1 . VAL   N  14 177 ? 43.396  -132.115 82.913  1.00 94.74  ? 177 VAL   N CG1 1 
ATOM   24476 C  CG2 . VAL   N  14 177 ? 45.189  -133.425 81.771  1.00 93.19  ? 177 VAL   N CG2 1 
ATOM   24477 N  N   . LEU   N  14 178 ? 42.122  -129.998 80.283  1.00 95.10  ? 178 LEU   N N   1 
ATOM   24478 C  CA  . LEU   N  14 178 ? 41.494  -128.651 80.276  1.00 96.73  ? 178 LEU   N CA  1 
ATOM   24479 C  C   . LEU   N  14 178 ? 40.662  -128.488 81.554  1.00 97.22  ? 178 LEU   N C   1 
ATOM   24480 O  O   . LEU   N  14 178 ? 39.632  -129.178 81.677  1.00 95.25  ? 178 LEU   N O   1 
ATOM   24481 C  CB  . LEU   N  14 178 ? 40.628  -128.513 79.017  1.00 96.51  ? 178 LEU   N CB  1 
ATOM   24482 C  CG  . LEU   N  14 178 ? 41.250  -127.770 77.831  1.00 96.39  ? 178 LEU   N CG  1 
ATOM   24483 C  CD1 . LEU   N  14 178 ? 42.717  -128.121 77.635  1.00 96.10  ? 178 LEU   N CD1 1 
ATOM   24484 C  CD2 . LEU   N  14 178 ? 40.467  -128.052 76.557  1.00 95.57  ? 178 LEU   N CD2 1 
ATOM   24485 N  N   . THR   N  14 179 ? 41.115  -127.625 82.471  1.00 100.22 ? 179 THR   N N   1 
ATOM   24486 C  CA  . THR   N  14 179 ? 40.437  -127.293 83.754  1.00 101.10 ? 179 THR   N CA  1 
ATOM   24487 C  C   . THR   N  14 179 ? 40.588  -125.798 84.056  1.00 102.58 ? 179 THR   N C   1 
ATOM   24488 O  O   . THR   N  14 179 ? 41.350  -125.124 83.339  1.00 103.10 ? 179 THR   N O   1 
ATOM   24489 C  CB  . THR   N  14 179 ? 41.014  -128.111 84.914  1.00 101.97 ? 179 THR   N CB  1 
ATOM   24490 O  OG1 . THR   N  14 179 ? 42.399  -127.788 85.035  1.00 100.18 ? 179 THR   N OG1 1 
ATOM   24491 C  CG2 . THR   N  14 179 ? 40.853  -129.601 84.720  1.00 102.55 ? 179 THR   N CG2 1 
ATOM   24492 N  N   . ALA   N  14 180 ? 39.910  -125.312 85.101  1.00 103.06 ? 180 ALA   N N   1 
ATOM   24493 C  CA  . ALA   N  14 180 ? 40.030  -123.927 85.612  1.00 102.22 ? 180 ALA   N CA  1 
ATOM   24494 C  C   . ALA   N  14 180 ? 41.497  -123.630 85.951  1.00 104.29 ? 180 ALA   N C   1 
ATOM   24495 O  O   . ALA   N  14 180 ? 41.921  -122.476 85.755  1.00 99.79  ? 180 ALA   N O   1 
ATOM   24496 C  CB  . ALA   N  14 180 ? 39.135  -123.735 86.812  1.00 103.35 ? 180 ALA   N CB  1 
ATOM   24497 N  N   . ALA   N  14 181 ? 42.237  -124.642 86.422  1.00 104.84 ? 181 ALA   N N   1 
ATOM   24498 C  CA  . ALA   N  14 181 ? 43.654  -124.548 86.857  1.00 106.36 ? 181 ALA   N CA  1 
ATOM   24499 C  C   . ALA   N  14 181 ? 44.556  -124.133 85.686  1.00 106.02 ? 181 ALA   N C   1 
ATOM   24500 O  O   . ALA   N  14 181 ? 45.557  -123.438 85.939  1.00 110.86 ? 181 ALA   N O   1 
ATOM   24501 C  CB  . ALA   N  14 181 ? 44.102  -125.861 87.455  1.00 106.78 ? 181 ALA   N CB  1 
ATOM   24502 N  N   . GLY   N  14 182 ? 44.226  -124.552 84.459  1.00 103.05 ? 182 GLY   N N   1 
ATOM   24503 C  CA  . GLY   N  14 182 ? 44.985  -124.205 83.241  1.00 102.49 ? 182 GLY   N CA  1 
ATOM   24504 C  C   . GLY   N  14 182 ? 44.993  -125.337 82.227  1.00 100.34 ? 182 GLY   N C   1 
ATOM   24505 O  O   . GLY   N  14 182 ? 43.967  -126.036 82.107  1.00 102.64 ? 182 GLY   N O   1 
ATOM   24506 N  N   . VAL   N  14 183 ? 46.114  -125.504 81.519  1.00 99.18  ? 183 VAL   N N   1 
ATOM   24507 C  CA  . VAL   N  14 183 ? 46.309  -126.528 80.450  1.00 97.54  ? 183 VAL   N CA  1 
ATOM   24508 C  C   . VAL   N  14 183 ? 47.516  -127.395 80.826  1.00 99.15  ? 183 VAL   N C   1 
ATOM   24509 O  O   . VAL   N  14 183 ? 48.620  -126.835 80.964  1.00 102.80 ? 183 VAL   N O   1 
ATOM   24510 C  CB  . VAL   N  14 183 ? 46.497  -125.865 79.072  1.00 96.79  ? 183 VAL   N CB  1 
ATOM   24511 C  CG1 . VAL   N  14 183 ? 46.662  -126.891 77.961  1.00 95.50  ? 183 VAL   N CG1 1 
ATOM   24512 C  CG2 . VAL   N  14 183 ? 45.355  -124.915 78.746  1.00 98.41  ? 183 VAL   N CG2 1 
ATOM   24513 N  N   . GLU   N  14 184 ? 47.302  -128.707 80.978  1.00 97.59  ? 184 GLU   N N   1 
ATOM   24514 C  CA  . GLU   N  14 184 ? 48.355  -129.707 81.303  1.00 96.55  ? 184 GLU   N CA  1 
ATOM   24515 C  C   . GLU   N  14 184 ? 48.510  -130.687 80.136  1.00 93.16  ? 184 GLU   N C   1 
ATOM   24516 O  O   . GLU   N  14 184 ? 47.482  -131.194 79.651  1.00 90.08  ? 184 GLU   N O   1 
ATOM   24517 C  CB  . GLU   N  14 184 ? 47.999  -130.468 82.578  1.00 98.51  ? 184 GLU   N CB  1 
ATOM   24518 C  CG  . GLU   N  14 184 ? 49.160  -131.260 83.148  1.00 99.66  ? 184 GLU   N CG  1 
ATOM   24519 C  CD  . GLU   N  14 184 ? 48.825  -132.071 84.388  1.00 103.55 ? 184 GLU   N CD  1 
ATOM   24520 O  OE1 . GLU   N  14 184 ? 49.664  -132.905 84.791  1.00 103.32 ? 184 GLU   N OE1 1 
ATOM   24521 O  OE2 . GLU   N  14 184 ? 47.726  -131.871 84.947  1.00 102.96 ? 184 GLU   N OE2 1 
ATOM   24522 N  N   . ARG   N  14 185 ? 49.756  -130.941 79.724  1.00 93.57  ? 185 ARG   N N   1 
ATOM   24523 C  CA  . ARG   N  14 185 ? 50.117  -131.924 78.668  1.00 94.54  ? 185 ARG   N CA  1 
ATOM   24524 C  C   . ARG   N  14 185 ? 50.688  -133.184 79.321  1.00 92.99  ? 185 ARG   N C   1 
ATOM   24525 O  O   . ARG   N  14 185 ? 51.664  -133.060 80.076  1.00 99.91  ? 185 ARG   N O   1 
ATOM   24526 C  CB  . ARG   N  14 185 ? 51.148  -131.339 77.697  1.00 96.26  ? 185 ARG   N CB  1 
ATOM   24527 C  CG  . ARG   N  14 185 ? 50.551  -130.821 76.397  1.00 98.25  ? 185 ARG   N CG  1 
ATOM   24528 C  CD  . ARG   N  14 185 ? 51.545  -130.928 75.259  1.00 98.96  ? 185 ARG   N CD  1 
ATOM   24529 N  NE  . ARG   N  14 185 ? 50.992  -130.417 74.016  1.00 100.38 ? 185 ARG   N NE  1 
ATOM   24530 C  CZ  . ARG   N  14 185 ? 50.310  -131.121 73.118  1.00 100.49 ? 185 ARG   N CZ  1 
ATOM   24531 N  NH1 . ARG   N  14 185 ? 50.069  -132.409 73.296  1.00 100.92 ? 185 ARG   N NH1 1 
ATOM   24532 N  NH2 . ARG   N  14 185 ? 49.864  -130.519 72.029  1.00 102.23 ? 185 ARG   N NH2 1 
ATOM   24533 N  N   . LEU   N  14 186 ? 50.103  -134.346 79.017  1.00 92.93  ? 186 LEU   N N   1 
ATOM   24534 C  CA  . LEU   N  14 186 ? 50.553  -135.678 79.501  1.00 92.44  ? 186 LEU   N CA  1 
ATOM   24535 C  C   . LEU   N  14 186 ? 50.992  -136.532 78.307  1.00 90.56  ? 186 LEU   N C   1 
ATOM   24536 O  O   . LEU   N  14 186 ? 50.354  -136.441 77.240  1.00 88.60  ? 186 LEU   N O   1 
ATOM   24537 C  CB  . LEU   N  14 186 ? 49.402  -136.356 80.249  1.00 92.34  ? 186 LEU   N CB  1 
ATOM   24538 C  CG  . LEU   N  14 186 ? 48.905  -135.641 81.503  1.00 91.18  ? 186 LEU   N CG  1 
ATOM   24539 C  CD1 . LEU   N  14 186 ? 47.641  -136.304 82.027  1.00 91.93  ? 186 LEU   N CD1 1 
ATOM   24540 C  CD2 . LEU   N  14 186 ? 49.978  -135.615 82.579  1.00 92.64  ? 186 LEU   N CD2 1 
ATOM   24541 N  N   . ILE   N  14 187 ? 52.035  -137.341 78.502  1.00 89.85  ? 187 ILE   N N   1 
ATOM   24542 C  CA  . ILE   N  14 187 ? 52.542  -138.336 77.512  1.00 92.13  ? 187 ILE   N CA  1 
ATOM   24543 C  C   . ILE   N  14 187 ? 52.722  -139.677 78.233  1.00 94.09  ? 187 ILE   N C   1 
ATOM   24544 O  O   . ILE   N  14 187 ? 53.155  -139.667 79.400  1.00 100.40 ? 187 ILE   N O   1 
ATOM   24545 C  CB  . ILE   N  14 187 ? 53.846  -137.844 76.849  1.00 91.55  ? 187 ILE   N CB  1 
ATOM   24546 C  CG1 . ILE   N  14 187 ? 54.271  -138.763 75.702  1.00 92.94  ? 187 ILE   N CG1 1 
ATOM   24547 C  CG2 . ILE   N  14 187 ? 54.958  -137.671 77.874  1.00 92.09  ? 187 ILE   N CG2 1 
ATOM   24548 C  CD1 . ILE   N  14 187 ? 55.352  -138.187 74.816  1.00 94.91  ? 187 ILE   N CD1 1 
ATOM   24549 N  N   . PHE   N  14 188 ? 52.374  -140.783 77.568  1.00 95.90  ? 188 PHE   N N   1 
ATOM   24550 C  CA  . PHE   N  14 188 ? 52.525  -142.172 78.077  1.00 95.94  ? 188 PHE   N CA  1 
ATOM   24551 C  C   . PHE   N  14 188 ? 53.165  -143.031 76.983  1.00 97.25  ? 188 PHE   N C   1 
ATOM   24552 O  O   . PHE   N  14 188 ? 52.671  -143.020 75.835  1.00 93.79  ? 188 PHE   N O   1 
ATOM   24553 C  CB  . PHE   N  14 188 ? 51.175  -142.719 78.547  1.00 93.54  ? 188 PHE   N CB  1 
ATOM   24554 C  CG  . PHE   N  14 188 ? 50.547  -141.904 79.647  1.00 93.90  ? 188 PHE   N CG  1 
ATOM   24555 C  CD1 . PHE   N  14 188 ? 51.066  -141.936 80.930  1.00 95.30  ? 188 PHE   N CD1 1 
ATOM   24556 C  CD2 . PHE   N  14 188 ? 49.461  -141.078 79.396  1.00 94.64  ? 188 PHE   N CD2 1 
ATOM   24557 C  CE1 . PHE   N  14 188 ? 50.502  -141.176 81.943  1.00 97.59  ? 188 PHE   N CE1 1 
ATOM   24558 C  CE2 . PHE   N  14 188 ? 48.898  -140.318 80.411  1.00 94.17  ? 188 PHE   N CE2 1 
ATOM   24559 C  CZ  . PHE   N  14 188 ? 49.418  -140.370 81.681  1.00 95.17  ? 188 PHE   N CZ  1 
ATOM   24560 N  N   . TYR   N  14 189 ? 54.242  -143.738 77.336  1.00 98.05  ? 189 TYR   N N   1 
ATOM   24561 C  CA  . TYR   N  14 189 ? 55.120  -144.483 76.399  1.00 102.41 ? 189 TYR   N CA  1 
ATOM   24562 C  C   . TYR   N  14 189 ? 54.672  -145.941 76.324  1.00 106.61 ? 189 TYR   N C   1 
ATOM   24563 O  O   . TYR   N  14 189 ? 54.048  -146.447 77.256  1.00 112.36 ? 189 TYR   N O   1 
ATOM   24564 C  CB  . TYR   N  14 189 ? 56.580  -144.347 76.838  1.00 103.57 ? 189 TYR   N CB  1 
ATOM   24565 C  CG  . TYR   N  14 189 ? 57.053  -142.922 76.976  1.00 102.58 ? 189 TYR   N CG  1 
ATOM   24566 C  CD1 . TYR   N  14 189 ? 57.431  -142.183 75.866  1.00 103.93 ? 189 TYR   N CD1 1 
ATOM   24567 C  CD2 . TYR   N  14 189 ? 57.114  -142.303 78.215  1.00 103.37 ? 189 TYR   N CD2 1 
ATOM   24568 C  CE1 . TYR   N  14 189 ? 57.865  -140.871 75.982  1.00 103.88 ? 189 TYR   N CE1 1 
ATOM   24569 C  CE2 . TYR   N  14 189 ? 57.544  -140.992 78.348  1.00 103.30 ? 189 TYR   N CE2 1 
ATOM   24570 C  CZ  . TYR   N  14 189 ? 57.923  -140.272 77.229  1.00 102.64 ? 189 TYR   N CZ  1 
ATOM   24571 O  OH  . TYR   N  14 189 ? 58.349  -138.982 77.360  1.00 103.40 ? 189 TYR   N OH  1 
ATOM   24572 N  N   . PRO   N  14 190 ? 54.968  -146.652 75.209  1.00 109.79 ? 190 PRO   N N   1 
ATOM   24573 C  CA  . PRO   N  14 190 ? 54.570  -148.051 75.039  1.00 109.59 ? 190 PRO   N CA  1 
ATOM   24574 C  C   . PRO   N  14 190 ? 54.800  -148.934 76.274  1.00 108.11 ? 190 PRO   N C   1 
ATOM   24575 O  O   . PRO   N  14 190 ? 53.874  -149.610 76.679  1.00 108.27 ? 190 PRO   N O   1 
ATOM   24576 C  CB  . PRO   N  14 190 ? 55.468  -148.515 73.883  1.00 112.02 ? 190 PRO   N CB  1 
ATOM   24577 C  CG  . PRO   N  14 190 ? 55.633  -147.273 73.038  1.00 110.58 ? 190 PRO   N CG  1 
ATOM   24578 C  CD  . PRO   N  14 190 ? 55.690  -146.134 74.034  1.00 110.36 ? 190 PRO   N CD  1 
ATOM   24579 N  N   . ASP   N  14 191 ? 56.006  -148.883 76.847  1.00 109.60 ? 191 ASP   N N   1 
ATOM   24580 C  CA  . ASP   N  14 191 ? 56.454  -149.781 77.946  1.00 112.03 ? 191 ASP   N CA  1 
ATOM   24581 C  C   . ASP   N  14 191 ? 55.473  -149.710 79.124  1.00 112.28 ? 191 ASP   N C   1 
ATOM   24582 O  O   . ASP   N  14 191 ? 55.380  -150.713 79.858  1.00 114.54 ? 191 ASP   N O   1 
ATOM   24583 C  CB  . ASP   N  14 191 ? 57.891  -149.464 78.367  1.00 118.16 ? 191 ASP   N CB  1 
ATOM   24584 C  CG  . ASP   N  14 191 ? 58.919  -149.875 77.326  1.00 120.01 ? 191 ASP   N CG  1 
ATOM   24585 O  OD1 . ASP   N  14 191 ? 59.012  -151.086 77.041  1.00 120.41 ? 191 ASP   N OD1 1 
ATOM   24586 O  OD2 . ASP   N  14 191 ? 59.602  -148.980 76.792  1.00 126.74 ? 191 ASP   N OD2 1 
ATOM   24587 N  N   . GLU   N  14 192 ? 54.767  -148.589 79.298  1.00 110.45 ? 192 GLU   N N   1 
ATOM   24588 C  CA  . GLU   N  14 192 ? 53.698  -148.449 80.323  1.00 114.31 ? 192 GLU   N CA  1 
ATOM   24589 C  C   . GLU   N  14 192 ? 52.392  -149.065 79.804  1.00 112.38 ? 192 GLU   N C   1 
ATOM   24590 O  O   . GLU   N  14 192 ? 51.917  -150.030 80.430  1.00 114.53 ? 192 GLU   N O   1 
ATOM   24591 C  CB  . GLU   N  14 192 ? 53.480  -146.987 80.714  1.00 117.80 ? 192 GLU   N CB  1 
ATOM   24592 C  CG  . GLU   N  14 192 ? 52.486  -146.821 81.853  1.00 124.29 ? 192 GLU   N CG  1 
ATOM   24593 C  CD  . GLU   N  14 192 ? 52.288  -145.397 82.342  1.00 130.51 ? 192 GLU   N CD  1 
ATOM   24594 O  OE1 . GLU   N  14 192 ? 51.366  -145.180 83.155  1.00 135.42 ? 192 GLU   N OE1 1 
ATOM   24595 O  OE2 . GLU   N  14 192 ? 53.057  -144.510 81.916  1.00 138.15 ? 192 GLU   N OE2 1 
ATOM   24596 N  N   . TYR   N  14 193 ? 51.828  -148.530 78.715  1.00 110.96 ? 193 TYR   N N   1 
ATOM   24597 C  CA  . TYR   N  14 193 ? 50.422  -148.798 78.303  1.00 112.38 ? 193 TYR   N CA  1 
ATOM   24598 C  C   . TYR   N  14 193 ? 50.278  -150.209 77.708  1.00 112.69 ? 193 TYR   N C   1 
ATOM   24599 O  O   . TYR   N  14 193 ? 49.196  -150.798 77.900  1.00 110.89 ? 193 TYR   N O   1 
ATOM   24600 C  CB  . TYR   N  14 193 ? 49.876  -147.683 77.398  1.00 109.40 ? 193 TYR   N CB  1 
ATOM   24601 C  CG  . TYR   N  14 193 ? 50.343  -147.648 75.962  1.00 105.67 ? 193 TYR   N CG  1 
ATOM   24602 C  CD1 . TYR   N  14 193 ? 49.888  -148.569 75.031  1.00 103.67 ? 193 TYR   N CD1 1 
ATOM   24603 C  CD2 . TYR   N  14 193 ? 51.175  -146.635 75.511  1.00 105.63 ? 193 TYR   N CD2 1 
ATOM   24604 C  CE1 . TYR   N  14 193 ? 50.292  -148.519 73.706  1.00 105.40 ? 193 TYR   N CE1 1 
ATOM   24605 C  CE2 . TYR   N  14 193 ? 51.583  -146.566 74.189  1.00 106.60 ? 193 TYR   N CE2 1 
ATOM   24606 C  CZ  . TYR   N  14 193 ? 51.141  -147.513 73.283  1.00 106.55 ? 193 TYR   N CZ  1 
ATOM   24607 O  OH  . TYR   N  14 193 ? 51.536  -147.458 71.978  1.00 113.03 ? 193 TYR   N OH  1 
ATOM   24608 N  N   . GLU   N  14 194 ? 51.308  -150.744 77.038  1.00 114.74 ? 194 GLU   N N   1 
ATOM   24609 C  CA  . GLU   N  14 194 ? 51.236  -152.041 76.302  1.00 117.54 ? 194 GLU   N CA  1 
ATOM   24610 C  C   . GLU   N  14 194 ? 50.880  -153.186 77.259  1.00 121.22 ? 194 GLU   N C   1 
ATOM   24611 O  O   . GLU   N  14 194 ? 50.169  -154.110 76.816  1.00 128.57 ? 194 GLU   N O   1 
ATOM   24612 C  CB  . GLU   N  14 194 ? 52.544  -152.360 75.572  1.00 117.76 ? 194 GLU   N CB  1 
ATOM   24613 C  CG  . GLU   N  14 194 ? 52.638  -151.730 74.192  1.00 120.72 ? 194 GLU   N CG  1 
ATOM   24614 C  CD  . GLU   N  14 194 ? 53.888  -152.083 73.402  1.00 123.83 ? 194 GLU   N CD  1 
ATOM   24615 O  OE1 . GLU   N  14 194 ? 54.144  -151.420 72.373  1.00 125.14 ? 194 GLU   N OE1 1 
ATOM   24616 O  OE2 . GLU   N  14 194 ? 54.603  -153.022 73.811  1.00 128.24 ? 194 GLU   N OE2 1 
ATOM   24617 N  N   . GLN   N  14 195 ? 51.344  -153.129 78.512  1.00 123.61 ? 195 GLN   N N   1 
ATOM   24618 C  CA  . GLN   N  14 195 ? 51.198  -154.230 79.505  1.00 128.18 ? 195 GLN   N CA  1 
ATOM   24619 C  C   . GLN   N  14 195 ? 50.082  -153.913 80.513  1.00 125.02 ? 195 GLN   N C   1 
ATOM   24620 O  O   . GLN   N  14 195 ? 50.086  -154.530 81.596  1.00 132.35 ? 195 GLN   N O   1 
ATOM   24621 C  CB  . GLN   N  14 195 ? 52.532  -154.497 80.207  1.00 133.36 ? 195 GLN   N CB  1 
ATOM   24622 C  CG  . GLN   N  14 195 ? 53.059  -153.324 81.025  1.00 138.54 ? 195 GLN   N CG  1 
ATOM   24623 C  CD  . GLN   N  14 195 ? 54.406  -153.617 81.642  1.00 145.89 ? 195 GLN   N CD  1 
ATOM   24624 O  OE1 . GLN   N  14 195 ? 55.144  -154.491 81.190  1.00 157.93 ? 195 GLN   N OE1 1 
ATOM   24625 N  NE2 . GLN   N  14 195 ? 54.741  -152.882 82.690  1.00 149.45 ? 195 GLN   N NE2 1 
ATOM   24626 N  N   . LEU   N  14 196 ? 49.157  -153.006 80.178  1.00 121.09 ? 196 LEU   N N   1 
ATOM   24627 C  CA  . LEU   N  14 196 ? 47.926  -152.750 80.980  1.00 120.74 ? 196 LEU   N CA  1 
ATOM   24628 C  C   . LEU   N  14 196 ? 46.974  -153.941 80.826  1.00 121.57 ? 196 LEU   N C   1 
ATOM   24629 O  O   . LEU   N  14 196 ? 46.987  -154.642 79.813  1.00 127.19 ? 196 LEU   N O   1 
ATOM   24630 C  CB  . LEU   N  14 196 ? 47.247  -151.455 80.515  1.00 116.70 ? 196 LEU   N CB  1 
ATOM   24631 C  CG  . LEU   N  14 196 ? 47.893  -150.149 80.980  1.00 112.62 ? 196 LEU   N CG  1 
ATOM   24632 C  CD1 . LEU   N  14 196 ? 47.320  -148.969 80.215  1.00 109.20 ? 196 LEU   N CD1 1 
ATOM   24633 C  CD2 . LEU   N  14 196 ? 47.710  -149.945 82.476  1.00 111.26 ? 196 LEU   N CD2 1 
ATOM   24634 O  OXT . LEU   N  14 196 ? 46.171  -154.218 81.716  1.00 126.27 ? 196 LEU   N OXT 1 
ATOM   24635 N  N   . MET   O  1  1   ? 41.854  -204.453 35.732  1.00 164.02 ? 1   MET   O N   1 
ATOM   24636 C  CA  . MET   O  1  1   ? 40.457  -204.382 36.270  1.00 165.74 ? 1   MET   O CA  1 
ATOM   24637 C  C   . MET   O  1  1   ? 39.509  -203.901 35.158  1.00 161.59 ? 1   MET   O C   1 
ATOM   24638 O  O   . MET   O  1  1   ? 39.824  -204.148 33.972  1.00 141.98 ? 1   MET   O O   1 
ATOM   24639 C  CB  . MET   O  1  1   ? 40.386  -203.445 37.485  1.00 174.03 ? 1   MET   O CB  1 
ATOM   24640 C  CG  . MET   O  1  1   ? 39.225  -203.746 38.429  1.00 185.65 ? 1   MET   O CG  1 
ATOM   24641 S  SD  . MET   O  1  1   ? 38.210  -202.288 38.814  1.00 191.02 ? 1   MET   O SD  1 
ATOM   24642 C  CE  . MET   O  1  1   ? 39.396  -201.257 39.675  1.00 194.08 ? 1   MET   O CE  1 
ATOM   24643 N  N   . THR   O  1  2   ? 38.393  -203.258 35.530  1.00 156.25 ? 2   THR   O N   1 
ATOM   24644 C  CA  . THR   O  1  2   ? 37.293  -202.777 34.647  1.00 147.40 ? 2   THR   O CA  1 
ATOM   24645 C  C   . THR   O  1  2   ? 36.606  -203.976 33.979  1.00 139.20 ? 2   THR   O C   1 
ATOM   24646 O  O   . THR   O  1  2   ? 37.256  -205.028 33.802  1.00 132.45 ? 2   THR   O O   1 
ATOM   24647 C  CB  . THR   O  1  2   ? 37.773  -201.738 33.623  1.00 149.22 ? 2   THR   O CB  1 
ATOM   24648 O  OG1 . THR   O  1  2   ? 38.618  -200.799 34.289  1.00 154.78 ? 2   THR   O OG1 1 
ATOM   24649 C  CG2 . THR   O  1  2   ? 36.633  -200.992 32.961  1.00 142.55 ? 2   THR   O CG2 1 
ATOM   24650 N  N   . ASP   O  1  3   ? 35.323  -203.807 33.647  1.00 139.23 ? 3   ASP   O N   1 
ATOM   24651 C  CA  . ASP   O  1  3   ? 34.481  -204.799 32.928  1.00 132.80 ? 3   ASP   O CA  1 
ATOM   24652 C  C   . ASP   O  1  3   ? 35.147  -205.125 31.586  1.00 133.59 ? 3   ASP   O C   1 
ATOM   24653 O  O   . ASP   O  1  3   ? 34.936  -204.363 30.623  1.00 144.45 ? 3   ASP   O O   1 
ATOM   24654 C  CB  . ASP   O  1  3   ? 33.058  -204.260 32.751  1.00 128.87 ? 3   ASP   O CB  1 
ATOM   24655 C  CG  . ASP   O  1  3   ? 32.026  -205.316 32.402  1.00 129.42 ? 3   ASP   O CG  1 
ATOM   24656 O  OD1 . ASP   O  1  3   ? 32.417  -206.362 31.849  1.00 129.63 ? 3   ASP   O OD1 1 
ATOM   24657 O  OD2 . ASP   O  1  3   ? 30.836  -205.083 32.693  1.00 124.03 ? 3   ASP   O OD2 1 
ATOM   24658 N  N   . ARG   O  1  4   ? 35.932  -206.205 31.533  1.00 130.81 ? 4   ARG   O N   1 
ATOM   24659 C  CA  . ARG   O  1  4   ? 36.579  -206.700 30.286  1.00 131.85 ? 4   ARG   O CA  1 
ATOM   24660 C  C   . ARG   O  1  4   ? 35.549  -207.460 29.437  1.00 125.92 ? 4   ARG   O C   1 
ATOM   24661 O  O   . ARG   O  1  4   ? 35.842  -207.708 28.251  1.00 127.51 ? 4   ARG   O O   1 
ATOM   24662 C  CB  . ARG   O  1  4   ? 37.790  -207.589 30.599  1.00 139.19 ? 4   ARG   O CB  1 
ATOM   24663 C  CG  . ARG   O  1  4   ? 38.945  -206.883 31.300  1.00 143.93 ? 4   ARG   O CG  1 
ATOM   24664 C  CD  . ARG   O  1  4   ? 39.398  -205.596 30.628  1.00 149.45 ? 4   ARG   O CD  1 
ATOM   24665 N  NE  . ARG   O  1  4   ? 39.465  -205.691 29.171  1.00 153.37 ? 4   ARG   O NE  1 
ATOM   24666 C  CZ  . ARG   O  1  4   ? 40.548  -205.995 28.454  1.00 156.58 ? 4   ARG   O CZ  1 
ATOM   24667 N  NH1 . ARG   O  1  4   ? 41.707  -206.249 29.040  1.00 157.85 ? 4   ARG   O NH1 1 
ATOM   24668 N  NH2 . ARG   O  1  4   ? 40.463  -206.043 27.134  1.00 156.95 ? 4   ARG   O NH2 1 
ATOM   24669 N  N   . TYR   O  1  5   ? 34.392  -207.810 30.012  1.00 115.40 ? 5   TYR   O N   1 
ATOM   24670 C  CA  . TYR   O  1  5   ? 33.276  -208.506 29.318  1.00 112.83 ? 5   TYR   O CA  1 
ATOM   24671 C  C   . TYR   O  1  5   ? 32.489  -207.494 28.475  1.00 109.69 ? 5   TYR   O C   1 
ATOM   24672 O  O   . TYR   O  1  5   ? 31.357  -207.142 28.858  1.00 109.83 ? 5   TYR   O O   1 
ATOM   24673 C  CB  . TYR   O  1  5   ? 32.352  -209.209 30.317  1.00 111.52 ? 5   TYR   O CB  1 
ATOM   24674 C  CG  . TYR   O  1  5   ? 32.974  -210.348 31.085  1.00 111.01 ? 5   TYR   O CG  1 
ATOM   24675 C  CD1 . TYR   O  1  5   ? 33.725  -210.119 32.227  1.00 110.75 ? 5   TYR   O CD1 1 
ATOM   24676 C  CD2 . TYR   O  1  5   ? 32.794  -211.661 30.680  1.00 111.09 ? 5   TYR   O CD2 1 
ATOM   24677 C  CE1 . TYR   O  1  5   ? 34.291  -211.162 32.940  1.00 110.73 ? 5   TYR   O CE1 1 
ATOM   24678 C  CE2 . TYR   O  1  5   ? 33.354  -212.716 31.381  1.00 111.00 ? 5   TYR   O CE2 1 
ATOM   24679 C  CZ  . TYR   O  1  5   ? 34.106  -212.465 32.516  1.00 111.58 ? 5   TYR   O CZ  1 
ATOM   24680 O  OH  . TYR   O  1  5   ? 34.665  -213.494 33.215  1.00 111.90 ? 5   TYR   O OH  1 
ATOM   24681 N  N   . SER   O  1  6   ? 33.072  -207.052 27.356  1.00 110.07 ? 6   SER   O N   1 
ATOM   24682 C  CA  . SER   O  1  6   ? 32.468  -206.083 26.401  1.00 109.82 ? 6   SER   O CA  1 
ATOM   24683 C  C   . SER   O  1  6   ? 31.793  -206.820 25.235  1.00 106.89 ? 6   SER   O C   1 
ATOM   24684 O  O   . SER   O  1  6   ? 31.358  -206.133 24.288  1.00 106.06 ? 6   SER   O O   1 
ATOM   24685 C  CB  . SER   O  1  6   ? 33.504  -205.105 25.904  1.00 112.40 ? 6   SER   O CB  1 
ATOM   24686 O  OG  . SER   O  1  6   ? 34.675  -205.785 25.477  1.00 118.59 ? 6   SER   O OG  1 
ATOM   24687 N  N   . PHE   O  1  7   ? 31.696  -208.154 25.307  1.00 105.17 ? 7   PHE   O N   1 
ATOM   24688 C  CA  . PHE   O  1  7   ? 31.143  -209.043 24.247  1.00 100.77 ? 7   PHE   O CA  1 
ATOM   24689 C  C   . PHE   O  1  7   ? 29.851  -209.704 24.737  1.00 95.18  ? 7   PHE   O C   1 
ATOM   24690 O  O   . PHE   O  1  7   ? 29.666  -209.849 25.960  1.00 96.48  ? 7   PHE   O O   1 
ATOM   24691 C  CB  . PHE   O  1  7   ? 32.161  -210.112 23.842  1.00 99.88  ? 7   PHE   O CB  1 
ATOM   24692 C  CG  . PHE   O  1  7   ? 32.762  -210.884 24.990  1.00 101.21 ? 7   PHE   O CG  1 
ATOM   24693 C  CD1 . PHE   O  1  7   ? 32.113  -211.989 25.521  1.00 99.57  ? 7   PHE   O CD1 1 
ATOM   24694 C  CD2 . PHE   O  1  7   ? 33.974  -210.501 25.544  1.00 101.91 ? 7   PHE   O CD2 1 
ATOM   24695 C  CE1 . PHE   O  1  7   ? 32.664  -212.691 26.581  1.00 99.60  ? 7   PHE   O CE1 1 
ATOM   24696 C  CE2 . PHE   O  1  7   ? 34.525  -211.208 26.603  1.00 101.72 ? 7   PHE   O CE2 1 
ATOM   24697 C  CZ  . PHE   O  1  7   ? 33.868  -212.300 27.118  1.00 100.20 ? 7   PHE   O CZ  1 
ATOM   24698 N  N   . SER   O  1  8   ? 28.997  -210.118 23.798  1.00 93.68  ? 8   SER   O N   1 
ATOM   24699 C  CA  . SER   O  1  8   ? 27.684  -210.764 24.064  1.00 95.75  ? 8   SER   O CA  1 
ATOM   24700 C  C   . SER   O  1  8   ? 27.882  -212.105 24.785  1.00 98.56  ? 8   SER   O C   1 
ATOM   24701 O  O   . SER   O  1  8   ? 28.761  -212.889 24.362  1.00 100.79 ? 8   SER   O O   1 
ATOM   24702 C  CB  . SER   O  1  8   ? 26.903  -210.954 22.790  1.00 92.77  ? 8   SER   O CB  1 
ATOM   24703 O  OG  . SER   O  1  8   ? 26.292  -209.743 22.377  1.00 93.89  ? 8   SER   O OG  1 
ATOM   24704 N  N   . LEU   O  1  9   ? 27.083  -212.357 25.827  1.00 100.77 ? 9   LEU   O N   1 
ATOM   24705 C  CA  . LEU   O  1  9   ? 27.023  -213.658 26.546  1.00 98.73  ? 9   LEU   O CA  1 
ATOM   24706 C  C   . LEU   O  1  9   ? 25.829  -214.475 26.042  1.00 95.55  ? 9   LEU   O C   1 
ATOM   24707 O  O   . LEU   O  1  9   ? 25.750  -215.660 26.395  1.00 96.93  ? 9   LEU   O O   1 
ATOM   24708 C  CB  . LEU   O  1  9   ? 26.901  -213.410 28.051  1.00 99.62  ? 9   LEU   O CB  1 
ATOM   24709 C  CG  . LEU   O  1  9   ? 28.068  -212.674 28.706  1.00 100.70 ? 9   LEU   O CG  1 
ATOM   24710 C  CD1 . LEU   O  1  9   ? 27.819  -212.526 30.198  1.00 101.54 ? 9   LEU   O CD1 1 
ATOM   24711 C  CD2 . LEU   O  1  9   ? 29.390  -213.387 28.456  1.00 101.35 ? 9   LEU   O CD2 1 
ATOM   24712 N  N   . THR   O  1  10  ? 24.919  -213.855 25.285  1.00 93.22  ? 10  THR   O N   1 
ATOM   24713 C  CA  . THR   O  1  10  ? 23.825  -214.540 24.547  1.00 93.83  ? 10  THR   O CA  1 
ATOM   24714 C  C   . THR   O  1  10  ? 24.156  -214.520 23.053  1.00 92.52  ? 10  THR   O C   1 
ATOM   24715 O  O   . THR   O  1  10  ? 24.231  -213.419 22.483  1.00 87.02  ? 10  THR   O O   1 
ATOM   24716 C  CB  . THR   O  1  10  ? 22.462  -213.890 24.810  1.00 94.07  ? 10  THR   O CB  1 
ATOM   24717 O  OG1 . THR   O  1  10  ? 22.310  -213.712 26.219  1.00 98.64  ? 10  THR   O OG1 1 
ATOM   24718 C  CG2 . THR   O  1  10  ? 21.313  -214.705 24.258  1.00 94.55  ? 10  THR   O CG2 1 
ATOM   24719 N  N   . THR   O  1  11  ? 24.359  -215.695 22.455  1.00 94.26  ? 11  THR   O N   1 
ATOM   24720 C  CA  . THR   O  1  11  ? 24.704  -215.862 21.020  1.00 96.40  ? 11  THR   O CA  1 
ATOM   24721 C  C   . THR   O  1  11  ? 23.840  -216.974 20.422  1.00 99.05  ? 11  THR   O C   1 
ATOM   24722 O  O   . THR   O  1  11  ? 23.322  -217.805 21.193  1.00 105.54 ? 11  THR   O O   1 
ATOM   24723 C  CB  . THR   O  1  11  ? 26.204  -216.133 20.844  1.00 97.54  ? 11  THR   O CB  1 
ATOM   24724 O  OG1 . THR   O  1  11  ? 26.505  -217.403 21.423  1.00 96.82  ? 11  THR   O OG1 1 
ATOM   24725 C  CG2 . THR   O  1  11  ? 27.069  -215.059 21.469  1.00 96.95  ? 11  THR   O CG2 1 
ATOM   24726 N  N   . PHE   O  1  12  ? 23.684  -216.962 19.098  1.00 99.89  ? 12  PHE   O N   1 
ATOM   24727 C  CA  . PHE   O  1  12  ? 22.922  -217.959 18.304  1.00 101.43 ? 12  PHE   O CA  1 
ATOM   24728 C  C   . PHE   O  1  12  ? 23.706  -219.272 18.246  1.00 102.75 ? 12  PHE   O C   1 
ATOM   24729 O  O   . PHE   O  1  12  ? 24.906  -219.241 17.913  1.00 100.80 ? 12  PHE   O O   1 
ATOM   24730 C  CB  . PHE   O  1  12  ? 22.664  -217.432 16.890  1.00 101.44 ? 12  PHE   O CB  1 
ATOM   24731 C  CG  . PHE   O  1  12  ? 21.765  -216.224 16.827  1.00 98.47  ? 12  PHE   O CG  1 
ATOM   24732 C  CD1 . PHE   O  1  12  ? 20.388  -216.363 16.894  1.00 96.98  ? 12  PHE   O CD1 1 
ATOM   24733 C  CD2 . PHE   O  1  12  ? 22.294  -214.950 16.706  1.00 97.32  ? 12  PHE   O CD2 1 
ATOM   24734 C  CE1 . PHE   O  1  12  ? 19.557  -215.255 16.839  1.00 95.55  ? 12  PHE   O CE1 1 
ATOM   24735 C  CE2 . PHE   O  1  12  ? 21.463  -213.843 16.653  1.00 97.42  ? 12  PHE   O CE2 1 
ATOM   24736 C  CZ  . PHE   O  1  12  ? 20.096  -213.997 16.718  1.00 95.49  ? 12  PHE   O CZ  1 
ATOM   24737 N  N   . SER   O  1  13  ? 23.039  -220.384 18.569  1.00 105.24 ? 13  SER   O N   1 
ATOM   24738 C  CA  . SER   O  1  13  ? 23.549  -221.766 18.381  1.00 106.69 ? 13  SER   O CA  1 
ATOM   24739 C  C   . SER   O  1  13  ? 23.251  -222.195 16.947  1.00 104.68 ? 13  SER   O C   1 
ATOM   24740 O  O   . SER   O  1  13  ? 22.347  -221.645 16.322  1.00 101.00 ? 13  SER   O O   1 
ATOM   24741 C  CB  . SER   O  1  13  ? 22.943  -222.708 19.388  1.00 109.33 ? 13  SER   O CB  1 
ATOM   24742 O  OG  . SER   O  1  13  ? 21.525  -222.638 19.347  1.00 110.60 ? 13  SER   O OG  1 
ATOM   24743 N  N   . PRO   O  1  14  ? 24.004  -223.166 16.377  1.00 105.05 ? 14  PRO   O N   1 
ATOM   24744 C  CA  . PRO   O  1  14  ? 23.779  -223.615 15.001  1.00 104.37 ? 14  PRO   O CA  1 
ATOM   24745 C  C   . PRO   O  1  14  ? 22.304  -223.843 14.630  1.00 101.30 ? 14  PRO   O C   1 
ATOM   24746 O  O   . PRO   O  1  14  ? 21.938  -223.525 13.512  1.00 101.31 ? 14  PRO   O O   1 
ATOM   24747 C  CB  . PRO   O  1  14  ? 24.572  -224.928 14.940  1.00 105.40 ? 14  PRO   O CB  1 
ATOM   24748 C  CG  . PRO   O  1  14  ? 25.720  -224.707 15.897  1.00 106.99 ? 14  PRO   O CG  1 
ATOM   24749 C  CD  . PRO   O  1  14  ? 25.140  -223.858 17.010  1.00 106.83 ? 14  PRO   O CD  1 
ATOM   24750 N  N   . SER   O  1  15  ? 21.502  -224.365 15.566  1.00 103.77 ? 15  SER   O N   1 
ATOM   24751 C  CA  . SER   O  1  15  ? 20.059  -224.683 15.379  1.00 107.45 ? 15  SER   O CA  1 
ATOM   24752 C  C   . SER   O  1  15  ? 19.223  -223.398 15.290  1.00 106.99 ? 15  SER   O C   1 
ATOM   24753 O  O   . SER   O  1  15  ? 18.087  -223.472 14.781  1.00 107.09 ? 15  SER   O O   1 
ATOM   24754 C  CB  . SER   O  1  15  ? 19.554  -225.591 16.477  1.00 107.13 ? 15  SER   O CB  1 
ATOM   24755 O  OG  . SER   O  1  15  ? 19.919  -225.093 17.757  1.00 104.68 ? 15  SER   O OG  1 
ATOM   24756 N  N   . GLY   O  1  16  ? 19.757  -222.273 15.776  1.00 105.94 ? 16  GLY   O N   1 
ATOM   24757 C  CA  . GLY   O  1  16  ? 19.111  -220.947 15.712  1.00 105.30 ? 16  GLY   O CA  1 
ATOM   24758 C  C   . GLY   O  1  16  ? 18.593  -220.490 17.066  1.00 104.84 ? 16  GLY   O C   1 
ATOM   24759 O  O   . GLY   O  1  16  ? 18.146  -219.334 17.159  1.00 102.34 ? 16  GLY   O O   1 
ATOM   24760 N  N   . LYS   O  1  17  ? 18.655  -221.354 18.083  1.00 108.23 ? 17  LYS   O N   1 
ATOM   24761 C  CA  . LYS   O  1  17  ? 18.166  -221.043 19.453  1.00 109.93 ? 17  LYS   O CA  1 
ATOM   24762 C  C   . LYS   O  1  17  ? 19.103  -219.990 20.055  1.00 104.74 ? 17  LYS   O C   1 
ATOM   24763 O  O   . LYS   O  1  17  ? 20.300  -219.989 19.701  1.00 101.44 ? 17  LYS   O O   1 
ATOM   24764 C  CB  . LYS   O  1  17  ? 18.113  -222.281 20.362  1.00 115.46 ? 17  LYS   O CB  1 
ATOM   24765 C  CG  . LYS   O  1  17  ? 17.899  -223.635 19.691  1.00 121.58 ? 17  LYS   O CG  1 
ATOM   24766 C  CD  . LYS   O  1  17  ? 16.457  -223.967 19.340  1.00 128.92 ? 17  LYS   O CD  1 
ATOM   24767 C  CE  . LYS   O  1  17  ? 15.791  -224.912 20.321  1.00 132.94 ? 17  LYS   O CE  1 
ATOM   24768 N  NZ  . LYS   O  1  17  ? 15.314  -224.207 21.535  1.00 136.81 ? 17  LYS   O NZ  1 
ATOM   24769 N  N   . LEU   O  1  18  ? 18.570  -219.113 20.907  1.00 104.17 ? 18  LEU   O N   1 
ATOM   24770 C  CA  . LEU   O  1  18  ? 19.372  -218.226 21.789  1.00 106.70 ? 18  LEU   O CA  1 
ATOM   24771 C  C   . LEU   O  1  18  ? 19.379  -218.835 23.196  1.00 106.42 ? 18  LEU   O C   1 
ATOM   24772 O  O   . LEU   O  1  18  ? 18.432  -218.580 23.965  1.00 113.86 ? 18  LEU   O O   1 
ATOM   24773 C  CB  . LEU   O  1  18  ? 18.787  -216.810 21.756  1.00 107.18 ? 18  LEU   O CB  1 
ATOM   24774 C  CG  . LEU   O  1  18  ? 19.083  -216.025 20.477  1.00 109.07 ? 18  LEU   O CG  1 
ATOM   24775 C  CD1 . LEU   O  1  18  ? 18.202  -214.789 20.370  1.00 111.08 ? 18  LEU   O CD1 1 
ATOM   24776 C  CD2 . LEU   O  1  18  ? 20.552  -215.637 20.401  1.00 108.78 ? 18  LEU   O CD2 1 
ATOM   24777 N  N   . GLY   O  1  19  ? 20.409  -219.637 23.487  1.00 102.97 ? 19  GLY   O N   1 
ATOM   24778 C  CA  . GLY   O  1  19  ? 20.523  -220.481 24.691  1.00 100.18 ? 19  GLY   O CA  1 
ATOM   24779 C  C   . GLY   O  1  19  ? 20.021  -219.782 25.941  1.00 98.90  ? 19  GLY   O C   1 
ATOM   24780 O  O   . GLY   O  1  19  ? 19.099  -220.318 26.583  1.00 97.13  ? 19  GLY   O O   1 
ATOM   24781 N  N   . GLN   O  1  20  ? 20.591  -218.618 26.267  1.00 97.25  ? 20  GLN   O N   1 
ATOM   24782 C  CA  . GLN   O  1  20  ? 20.375  -217.925 27.566  1.00 98.07  ? 20  GLN   O CA  1 
ATOM   24783 C  C   . GLN   O  1  20  ? 18.908  -217.500 27.710  1.00 96.52  ? 20  GLN   O C   1 
ATOM   24784 O  O   . GLN   O  1  20  ? 18.410  -217.528 28.853  1.00 94.17  ? 20  GLN   O O   1 
ATOM   24785 C  CB  . GLN   O  1  20  ? 21.319  -216.730 27.709  1.00 97.61  ? 20  GLN   O CB  1 
ATOM   24786 C  CG  . GLN   O  1  20  ? 22.766  -217.124 27.970  1.00 100.81 ? 20  GLN   O CG  1 
ATOM   24787 C  CD  . GLN   O  1  20  ? 22.952  -217.833 29.292  1.00 101.10 ? 20  GLN   O CD  1 
ATOM   24788 O  OE1 . GLN   O  1  20  ? 22.472  -217.388 30.333  1.00 104.15 ? 20  GLN   O OE1 1 
ATOM   24789 N  NE2 . GLN   O  1  20  ? 23.660  -218.950 29.266  1.00 101.22 ? 20  GLN   O NE2 1 
ATOM   24790 N  N   . ILE   O  1  21  ? 18.246  -217.119 26.611  1.00 98.16  ? 21  ILE   O N   1 
ATOM   24791 C  CA  . ILE   O  1  21  ? 16.799  -216.735 26.602  1.00 99.32  ? 21  ILE   O CA  1 
ATOM   24792 C  C   . ILE   O  1  21  ? 15.958  -217.979 26.905  1.00 99.36  ? 21  ILE   O C   1 
ATOM   24793 O  O   . ILE   O  1  21  ? 15.046  -217.888 27.749  1.00 98.26  ? 21  ILE   O O   1 
ATOM   24794 C  CB  . ILE   O  1  21  ? 16.388  -216.078 25.269  1.00 100.88 ? 21  ILE   O CB  1 
ATOM   24795 C  CG1 . ILE   O  1  21  ? 17.065  -214.716 25.088  1.00 101.16 ? 21  ILE   O CG1 1 
ATOM   24796 C  CG2 . ILE   O  1  21  ? 14.870  -215.971 25.160  1.00 99.69  ? 21  ILE   O CG2 1 
ATOM   24797 C  CD1 . ILE   O  1  21  ? 16.962  -214.163 23.689  1.00 101.47 ? 21  ILE   O CD1 1 
ATOM   24798 N  N   . ASP   O  1  22  ? 16.245  -219.090 26.225  1.00 101.13 ? 22  ASP   O N   1 
ATOM   24799 C  CA  . ASP   O  1  22  ? 15.575  -220.396 26.459  1.00 102.66 ? 22  ASP   O CA  1 
ATOM   24800 C  C   . ASP   O  1  22  ? 15.726  -220.769 27.939  1.00 100.28 ? 22  ASP   O C   1 
ATOM   24801 O  O   . ASP   O  1  22  ? 14.703  -221.097 28.571  1.00 101.05 ? 22  ASP   O O   1 
ATOM   24802 C  CB  . ASP   O  1  22  ? 16.130  -221.478 25.531  1.00 107.38 ? 22  ASP   O CB  1 
ATOM   24803 C  CG  . ASP   O  1  22  ? 15.670  -221.346 24.088  1.00 110.31 ? 22  ASP   O CG  1 
ATOM   24804 O  OD1 . ASP   O  1  22  ? 14.833  -220.460 23.811  1.00 107.71 ? 22  ASP   O OD1 1 
ATOM   24805 O  OD2 . ASP   O  1  22  ? 16.151  -222.135 23.252  1.00 117.40 ? 22  ASP   O OD2 1 
ATOM   24806 N  N   . TYR   O  1  23  ? 16.950  -220.695 28.471  1.00 97.28  ? 23  TYR   O N   1 
ATOM   24807 C  CA  . TYR   O  1  23  ? 17.284  -221.093 29.865  1.00 98.56  ? 23  TYR   O CA  1 
ATOM   24808 C  C   . TYR   O  1  23  ? 16.605  -220.131 30.851  1.00 97.49  ? 23  TYR   O C   1 
ATOM   24809 O  O   . TYR   O  1  23  ? 16.218  -220.570 31.948  1.00 99.73  ? 23  TYR   O O   1 
ATOM   24810 C  CB  . TYR   O  1  23  ? 18.800  -221.155 30.082  1.00 98.34  ? 23  TYR   O CB  1 
ATOM   24811 C  CG  . TYR   O  1  23  ? 19.574  -222.041 29.133  1.00 98.30  ? 23  TYR   O CG  1 
ATOM   24812 C  CD1 . TYR   O  1  23  ? 18.961  -223.048 28.400  1.00 98.31  ? 23  TYR   O CD1 1 
ATOM   24813 C  CD2 . TYR   O  1  23  ? 20.944  -221.884 28.987  1.00 98.54  ? 23  TYR   O CD2 1 
ATOM   24814 C  CE1 . TYR   O  1  23  ? 19.683  -223.854 27.534  1.00 99.85  ? 23  TYR   O CE1 1 
ATOM   24815 C  CE2 . TYR   O  1  23  ? 21.681  -222.683 28.128  1.00 98.28  ? 23  TYR   O CE2 1 
ATOM   24816 C  CZ  . TYR   O  1  23  ? 21.047  -223.671 27.399  1.00 99.83  ? 23  TYR   O CZ  1 
ATOM   24817 O  OH  . TYR   O  1  23  ? 21.771  -224.461 26.555  1.00 105.22 ? 23  TYR   O OH  1 
ATOM   24818 N  N   . ALA   O  1  24  ? 16.451  -218.859 30.477  1.00 96.99  ? 24  ALA   O N   1 
ATOM   24819 C  CA  . ALA   O  1  24  ? 15.729  -217.847 31.283  1.00 96.27  ? 24  ALA   O CA  1 
ATOM   24820 C  C   . ALA   O  1  24  ? 14.248  -218.238 31.375  1.00 95.73  ? 24  ALA   O C   1 
ATOM   24821 O  O   . ALA   O  1  24  ? 13.697  -218.199 32.490  1.00 93.77  ? 24  ALA   O O   1 
ATOM   24822 C  CB  . ALA   O  1  24  ? 15.915  -216.471 30.695  1.00 96.11  ? 24  ALA   O CB  1 
ATOM   24823 N  N   . LEU   O  1  25  ? 13.634  -218.620 30.250  1.00 94.55  ? 25  LEU   O N   1 
ATOM   24824 C  CA  . LEU   O  1  25  ? 12.223  -219.092 30.202  1.00 94.83  ? 25  LEU   O CA  1 
ATOM   24825 C  C   . LEU   O  1  25  ? 12.077  -220.335 31.089  1.00 97.96  ? 25  LEU   O C   1 
ATOM   24826 O  O   . LEU   O  1  25  ? 11.013  -220.474 31.724  1.00 101.72 ? 25  LEU   O O   1 
ATOM   24827 C  CB  . LEU   O  1  25  ? 11.814  -219.391 28.757  1.00 93.90  ? 25  LEU   O CB  1 
ATOM   24828 C  CG  . LEU   O  1  25  ? 11.565  -218.166 27.882  1.00 93.45  ? 25  LEU   O CG  1 
ATOM   24829 C  CD1 . LEU   O  1  25  ? 11.752  -218.502 26.411  1.00 93.79  ? 25  LEU   O CD1 1 
ATOM   24830 C  CD2 . LEU   O  1  25  ? 10.178  -217.589 28.137  1.00 94.43  ? 25  LEU   O CD2 1 
ATOM   24831 N  N   . THR   O  1  26  ? 13.101  -221.196 31.136  1.00 99.24  ? 26  THR   O N   1 
ATOM   24832 C  CA  . THR   O  1  26  ? 13.127  -222.410 31.998  1.00 101.52 ? 26  THR   O CA  1 
ATOM   24833 C  C   . THR   O  1  26  ? 13.028  -221.976 33.464  1.00 100.97 ? 26  THR   O C   1 
ATOM   24834 O  O   . THR   O  1  26  ? 12.286  -222.634 34.216  1.00 104.52 ? 26  THR   O O   1 
ATOM   24835 C  CB  . THR   O  1  26  ? 14.371  -223.278 31.756  1.00 102.49 ? 26  THR   O CB  1 
ATOM   24836 O  OG1 . THR   O  1  26  ? 14.342  -223.773 30.417  1.00 104.03 ? 26  THR   O OG1 1 
ATOM   24837 C  CG2 . THR   O  1  26  ? 14.461  -224.448 32.711  1.00 105.15 ? 26  THR   O CG2 1 
ATOM   24838 N  N   . ALA   O  1  27  ? 13.750  -220.917 33.848  1.00 98.08  ? 27  ALA   O N   1 
ATOM   24839 C  CA  . ALA   O  1  27  ? 13.719  -220.327 35.208  1.00 96.17  ? 27  ALA   O CA  1 
ATOM   24840 C  C   . ALA   O  1  27  ? 12.307  -219.813 35.509  1.00 96.61  ? 27  ALA   O C   1 
ATOM   24841 O  O   . ALA   O  1  27  ? 11.859  -219.962 36.661  1.00 96.51  ? 27  ALA   O O   1 
ATOM   24842 C  CB  . ALA   O  1  27  ? 14.742  -219.227 35.333  1.00 94.23  ? 27  ALA   O CB  1 
ATOM   24843 N  N   . VAL   O  1  28  ? 11.637  -219.238 34.506  1.00 98.57  ? 28  VAL   O N   1 
ATOM   24844 C  CA  . VAL   O  1  28  ? 10.251  -218.695 34.631  1.00 100.90 ? 28  VAL   O CA  1 
ATOM   24845 C  C   . VAL   O  1  28  ? 9.284   -219.866 34.852  1.00 102.69 ? 28  VAL   O C   1 
ATOM   24846 O  O   . VAL   O  1  28  ? 8.382   -219.720 35.697  1.00 105.05 ? 28  VAL   O O   1 
ATOM   24847 C  CB  . VAL   O  1  28  ? 9.850   -217.843 33.410  1.00 100.97 ? 28  VAL   O CB  1 
ATOM   24848 C  CG1 . VAL   O  1  28  ? 8.421   -217.331 33.518  1.00 101.21 ? 28  VAL   O CG1 1 
ATOM   24849 C  CG2 . VAL   O  1  28  ? 10.809  -216.683 33.192  1.00 100.71 ? 28  VAL   O CG2 1 
ATOM   24850 N  N   . LYS   O  1  29  ? 9.472   -220.977 34.129  1.00 105.07 ? 29  LYS   O N   1 
ATOM   24851 C  CA  . LYS   O  1  29  ? 8.651   -222.212 34.274  1.00 109.23 ? 29  LYS   O CA  1 
ATOM   24852 C  C   . LYS   O  1  29  ? 8.697   -222.682 35.734  1.00 106.39 ? 29  LYS   O C   1 
ATOM   24853 O  O   . LYS   O  1  29  ? 7.617   -222.974 36.286  1.00 101.87 ? 29  LYS   O O   1 
ATOM   24854 C  CB  . LYS   O  1  29  ? 9.129   -223.316 33.323  1.00 115.18 ? 29  LYS   O CB  1 
ATOM   24855 C  CG  . LYS   O  1  29  ? 8.408   -223.387 31.981  1.00 122.38 ? 29  LYS   O CG  1 
ATOM   24856 C  CD  . LYS   O  1  29  ? 7.105   -224.171 32.011  1.00 130.49 ? 29  LYS   O CD  1 
ATOM   24857 C  CE  . LYS   O  1  29  ? 5.889   -223.317 32.306  1.00 135.27 ? 29  LYS   O CE  1 
ATOM   24858 N  NZ  . LYS   O  1  29  ? 4.643   -224.121 32.342  1.00 139.18 ? 29  LYS   O NZ  1 
ATOM   24859 N  N   . GLN   O  1  30  ? 9.894   -222.730 36.335  1.00 104.84 ? 30  GLN   O N   1 
ATOM   24860 C  CA  . GLN   O  1  30  ? 10.109  -223.178 37.740  1.00 105.84 ? 30  GLN   O CA  1 
ATOM   24861 C  C   . GLN   O  1  30  ? 9.399   -222.216 38.703  1.00 103.34 ? 30  GLN   O C   1 
ATOM   24862 O  O   . GLN   O  1  30  ? 8.957   -222.679 39.771  1.00 103.57 ? 30  GLN   O O   1 
ATOM   24863 C  CB  . GLN   O  1  30  ? 11.593  -223.242 38.124  1.00 107.22 ? 30  GLN   O CB  1 
ATOM   24864 C  CG  . GLN   O  1  30  ? 12.511  -223.961 37.140  1.00 111.32 ? 30  GLN   O CG  1 
ATOM   24865 C  CD  . GLN   O  1  30  ? 11.989  -225.273 36.607  1.00 116.48 ? 30  GLN   O CD  1 
ATOM   24866 O  OE1 . GLN   O  1  30  ? 12.164  -225.589 35.432  1.00 121.97 ? 30  GLN   O OE1 1 
ATOM   24867 N  NE2 . GLN   O  1  30  ? 11.360  -226.063 37.466  1.00 122.93 ? 30  GLN   O NE2 1 
ATOM   24868 N  N   . GLY   O  1  31  ? 9.305   -220.930 38.341  1.00 101.25 ? 31  GLY   O N   1 
ATOM   24869 C  CA  . GLY   O  1  31  ? 8.729   -219.856 39.177  1.00 100.20 ? 31  GLY   O CA  1 
ATOM   24870 C  C   . GLY   O  1  31  ? 7.281   -220.125 39.553  1.00 99.69  ? 31  GLY   O C   1 
ATOM   24871 O  O   . GLY   O  1  31  ? 6.600   -220.844 38.798  1.00 104.81 ? 31  GLY   O O   1 
ATOM   24872 N  N   . VAL   O  1  32  ? 6.827   -219.555 40.675  1.00 97.20  ? 32  VAL   O N   1 
ATOM   24873 C  CA  . VAL   O  1  32  ? 5.444   -219.713 41.223  1.00 98.10  ? 32  VAL   O CA  1 
ATOM   24874 C  C   . VAL   O  1  32  ? 4.440   -219.079 40.253  1.00 98.45  ? 32  VAL   O C   1 
ATOM   24875 O  O   . VAL   O  1  32  ? 4.785   -218.062 39.623  1.00 98.76  ? 32  VAL   O O   1 
ATOM   24876 C  CB  . VAL   O  1  32  ? 5.333   -219.112 42.638  1.00 97.51  ? 32  VAL   O CB  1 
ATOM   24877 C  CG1 . VAL   O  1  32  ? 3.893   -218.832 43.040  1.00 97.17  ? 32  VAL   O CG1 1 
ATOM   24878 C  CG2 . VAL   O  1  32  ? 6.007   -220.008 43.665  1.00 99.28  ? 32  VAL   O CG2 1 
ATOM   24879 N  N   . THR   O  1  33  ? 3.240   -219.658 40.148  1.00 97.85  ? 33  THR   O N   1 
ATOM   24880 C  CA  . THR   O  1  33  ? 2.198   -219.243 39.176  1.00 101.60 ? 33  THR   O CA  1 
ATOM   24881 C  C   . THR   O  1  33  ? 1.682   -217.849 39.534  1.00 102.42 ? 33  THR   O C   1 
ATOM   24882 O  O   . THR   O  1  33  ? 1.351   -217.628 40.716  1.00 102.11 ? 33  THR   O O   1 
ATOM   24883 C  CB  . THR   O  1  33  ? 1.007   -220.207 39.127  1.00 104.89 ? 33  THR   O CB  1 
ATOM   24884 O  OG1 . THR   O  1  33  ? 1.494   -221.549 39.088  1.00 108.05 ? 33  THR   O OG1 1 
ATOM   24885 C  CG2 . THR   O  1  33  ? 0.115   -219.943 37.933  1.00 106.21 ? 33  THR   O CG2 1 
ATOM   24886 N  N   . SER   O  1  34  ? 1.625   -216.965 38.534  1.00 105.84 ? 34  SER   O N   1 
ATOM   24887 C  CA  . SER   O  1  34  ? 0.911   -215.662 38.556  1.00 105.17 ? 34  SER   O CA  1 
ATOM   24888 C  C   . SER   O  1  34  ? 0.012   -215.586 37.319  1.00 104.75 ? 34  SER   O C   1 
ATOM   24889 O  O   . SER   O  1  34  ? 0.353   -216.233 36.306  1.00 104.28 ? 34  SER   O O   1 
ATOM   24890 C  CB  . SER   O  1  34  ? 1.878   -214.508 38.617  1.00 105.94 ? 34  SER   O CB  1 
ATOM   24891 O  OG  . SER   O  1  34  ? 2.828   -214.585 37.564  1.00 107.29 ? 34  SER   O OG  1 
ATOM   24892 N  N   . LEU   O  1  35  ? -1.094  -214.845 37.401  1.00 105.07 ? 35  LEU   O N   1 
ATOM   24893 C  CA  . LEU   O  1  35  ? -2.081  -214.726 36.294  1.00 107.09 ? 35  LEU   O CA  1 
ATOM   24894 C  C   . LEU   O  1  35  ? -2.630  -213.298 36.213  1.00 105.95 ? 35  LEU   O C   1 
ATOM   24895 O  O   . LEU   O  1  35  ? -2.439  -212.524 37.171  1.00 104.96 ? 35  LEU   O O   1 
ATOM   24896 C  CB  . LEU   O  1  35  ? -3.201  -215.753 36.499  1.00 109.18 ? 35  LEU   O CB  1 
ATOM   24897 C  CG  . LEU   O  1  35  ? -3.959  -215.696 37.828  1.00 110.03 ? 35  LEU   O CG  1 
ATOM   24898 C  CD1 . LEU   O  1  35  ? -5.113  -214.702 37.772  1.00 110.77 ? 35  LEU   O CD1 1 
ATOM   24899 C  CD2 . LEU   O  1  35  ? -4.485  -217.074 38.198  1.00 110.62 ? 35  LEU   O CD2 1 
ATOM   24900 N  N   . GLY   O  1  36  ? -3.271  -212.981 35.085  1.00 105.97 ? 36  GLY   O N   1 
ATOM   24901 C  CA  . GLY   O  1  36  ? -3.989  -211.717 34.840  1.00 107.26 ? 36  GLY   O CA  1 
ATOM   24902 C  C   . GLY   O  1  36  ? -5.254  -211.962 34.038  1.00 108.81 ? 36  GLY   O C   1 
ATOM   24903 O  O   . GLY   O  1  36  ? -5.193  -212.748 33.072  1.00 107.50 ? 36  GLY   O O   1 
ATOM   24904 N  N   . ILE   O  1  37  ? -6.366  -211.338 34.438  1.00 111.00 ? 37  ILE   O N   1 
ATOM   24905 C  CA  . ILE   O  1  37  ? -7.676  -211.401 33.723  1.00 112.96 ? 37  ILE   O CA  1 
ATOM   24906 C  C   . ILE   O  1  37  ? -8.146  -209.968 33.456  1.00 111.30 ? 37  ILE   O C   1 
ATOM   24907 O  O   . ILE   O  1  37  ? -8.084  -209.139 34.387  1.00 110.33 ? 37  ILE   O O   1 
ATOM   24908 C  CB  . ILE   O  1  37  ? -8.721  -212.210 34.521  1.00 114.69 ? 37  ILE   O CB  1 
ATOM   24909 C  CG1 . ILE   O  1  37  ? -8.139  -213.525 35.045  1.00 116.04 ? 37  ILE   O CG1 1 
ATOM   24910 C  CG2 . ILE   O  1  37  ? -9.971  -212.439 33.682  1.00 115.76 ? 37  ILE   O CG2 1 
ATOM   24911 C  CD1 . ILE   O  1  37  ? -9.072  -214.303 35.943  1.00 121.17 ? 37  ILE   O CD1 1 
ATOM   24912 N  N   . LYS   O  1  38  ? -8.597  -209.699 32.229  1.00 108.95 ? 38  LYS   O N   1 
ATOM   24913 C  CA  . LYS   O  1  38  ? -9.119  -208.379 31.793  1.00 107.87 ? 38  LYS   O CA  1 
ATOM   24914 C  C   . LYS   O  1  38  ? -10.649 -208.433 31.732  1.00 108.83 ? 38  LYS   O C   1 
ATOM   24915 O  O   . LYS   O  1  38  ? -11.179 -209.174 30.887  1.00 107.84 ? 38  LYS   O O   1 
ATOM   24916 C  CB  . LYS   O  1  38  ? -8.535  -208.003 30.429  1.00 108.77 ? 38  LYS   O CB  1 
ATOM   24917 C  CG  . LYS   O  1  38  ? -8.784  -206.563 30.011  1.00 109.40 ? 38  LYS   O CG  1 
ATOM   24918 C  CD  . LYS   O  1  38  ? -7.960  -206.125 28.828  1.00 111.60 ? 38  LYS   O CD  1 
ATOM   24919 C  CE  . LYS   O  1  38  ? -8.592  -206.493 27.505  1.00 113.68 ? 38  LYS   O CE  1 
ATOM   24920 N  NZ  . LYS   O  1  38  ? -7.737  -206.071 26.373  1.00 115.24 ? 38  LYS   O NZ  1 
ATOM   24921 N  N   . ALA   O  1  39  ? -11.326 -207.676 32.600  1.00 108.90 ? 39  ALA   O N   1 
ATOM   24922 C  CA  . ALA   O  1  39  ? -12.792 -207.463 32.574  1.00 114.10 ? 39  ALA   O CA  1 
ATOM   24923 C  C   . ALA   O  1  39  ? -13.103 -206.239 31.700  1.00 114.08 ? 39  ALA   O C   1 
ATOM   24924 O  O   . ALA   O  1  39  ? -12.153 -205.632 31.165  1.00 110.62 ? 39  ALA   O O   1 
ATOM   24925 C  CB  . ALA   O  1  39  ? -13.316 -207.305 33.981  1.00 114.33 ? 39  ALA   O CB  1 
ATOM   24926 N  N   . THR   O  1  40  ? -14.385 -205.901 31.543  1.00 117.58 ? 40  THR   O N   1 
ATOM   24927 C  CA  . THR   O  1  40  ? -14.855 -204.734 30.749  1.00 120.29 ? 40  THR   O CA  1 
ATOM   24928 C  C   . THR   O  1  40  ? -14.524 -203.435 31.491  1.00 120.75 ? 40  THR   O C   1 
ATOM   24929 O  O   . THR   O  1  40  ? -14.130 -202.466 30.816  1.00 126.94 ? 40  THR   O O   1 
ATOM   24930 C  CB  . THR   O  1  40  ? -16.356 -204.825 30.451  1.00 124.51 ? 40  THR   O CB  1 
ATOM   24931 O  OG1 . THR   O  1  40  ? -17.047 -204.951 31.694  1.00 127.57 ? 40  THR   O OG1 1 
ATOM   24932 C  CG2 . THR   O  1  40  ? -16.703 -205.989 29.548  1.00 125.84 ? 40  THR   O CG2 1 
ATOM   24933 N  N   . ASN   O  1  41  ? -14.676 -203.419 32.820  1.00 117.43 ? 41  ASN   O N   1 
ATOM   24934 C  CA  . ASN   O  1  41  ? -14.520 -202.202 33.661  1.00 115.49 ? 41  ASN   O CA  1 
ATOM   24935 C  C   . ASN   O  1  41  ? -13.345 -202.369 34.631  1.00 111.71 ? 41  ASN   O C   1 
ATOM   24936 O  O   . ASN   O  1  41  ? -13.389 -201.752 35.714  1.00 111.41 ? 41  ASN   O O   1 
ATOM   24937 C  CB  . ASN   O  1  41  ? -15.810 -201.881 34.419  1.00 118.53 ? 41  ASN   O CB  1 
ATOM   24938 C  CG  . ASN   O  1  41  ? -16.162 -202.938 35.443  1.00 118.85 ? 41  ASN   O CG  1 
ATOM   24939 O  OD1 . ASN   O  1  41  ? -15.941 -204.125 35.213  1.00 117.95 ? 41  ASN   O OD1 1 
ATOM   24940 N  ND2 . ASN   O  1  41  ? -16.697 -202.518 36.578  1.00 123.96 ? 41  ASN   O ND2 1 
ATOM   24941 N  N   . GLY   O  1  42  ? -12.329 -203.155 34.266  1.00 109.16 ? 42  GLY   O N   1 
ATOM   24942 C  CA  . GLY   O  1  42  ? -11.102 -203.282 35.075  1.00 110.35 ? 42  GLY   O CA  1 
ATOM   24943 C  C   . GLY   O  1  42  ? -10.252 -204.482 34.699  1.00 110.58 ? 42  GLY   O C   1 
ATOM   24944 O  O   . GLY   O  1  42  ? -10.659 -205.246 33.807  1.00 118.99 ? 42  GLY   O O   1 
ATOM   24945 N  N   . VAL   O  1  43  ? -9.100  -204.622 35.364  1.00 109.15 ? 43  VAL   O N   1 
ATOM   24946 C  CA  . VAL   O  1  43  ? -8.140  -205.756 35.208  1.00 109.02 ? 43  VAL   O CA  1 
ATOM   24947 C  C   . VAL   O  1  43  ? -7.736  -206.240 36.604  1.00 109.81 ? 43  VAL   O C   1 
ATOM   24948 O  O   . VAL   O  1  43  ? -7.552  -205.387 37.495  1.00 112.26 ? 43  VAL   O O   1 
ATOM   24949 C  CB  . VAL   O  1  43  ? -6.896  -205.348 34.395  1.00 106.36 ? 43  VAL   O CB  1 
ATOM   24950 C  CG1 . VAL   O  1  43  ? -6.004  -206.544 34.097  1.00 106.12 ? 43  VAL   O CG1 1 
ATOM   24951 C  CG2 . VAL   O  1  43  ? -7.266  -204.631 33.109  1.00 105.68 ? 43  VAL   O CG2 1 
ATOM   24952 N  N   . VAL   O  1  44  ? -7.588  -207.556 36.772  1.00 108.36 ? 44  VAL   O N   1 
ATOM   24953 C  CA  . VAL   O  1  44  ? -7.075  -208.191 38.022  1.00 106.52 ? 44  VAL   O CA  1 
ATOM   24954 C  C   . VAL   O  1  44  ? -5.762  -208.909 37.691  1.00 103.53 ? 44  VAL   O C   1 
ATOM   24955 O  O   . VAL   O  1  44  ? -5.700  -209.582 36.644  1.00 99.86  ? 44  VAL   O O   1 
ATOM   24956 C  CB  . VAL   O  1  44  ? -8.104  -209.145 38.663  1.00 109.92 ? 44  VAL   O CB  1 
ATOM   24957 C  CG1 . VAL   O  1  44  ? -8.693  -210.133 37.665  1.00 112.77 ? 44  VAL   O CG1 1 
ATOM   24958 C  CG2 . VAL   O  1  44  ? -7.514  -209.882 39.856  1.00 107.46 ? 44  VAL   O CG2 1 
ATOM   24959 N  N   . ILE   O  1  45  ? -4.753  -208.740 38.550  1.00 101.70 ? 45  ILE   O N   1 
ATOM   24960 C  CA  . ILE   O  1  45  ? -3.470  -209.503 38.524  1.00 100.18 ? 45  ILE   O CA  1 
ATOM   24961 C  C   . ILE   O  1  45  ? -3.262  -210.116 39.912  1.00 102.07 ? 45  ILE   O C   1 
ATOM   24962 O  O   . ILE   O  1  45  ? -3.360  -209.380 40.910  1.00 103.11 ? 45  ILE   O O   1 
ATOM   24963 C  CB  . ILE   O  1  45  ? -2.283  -208.621 38.089  1.00 98.69  ? 45  ILE   O CB  1 
ATOM   24964 C  CG1 . ILE   O  1  45  ? -2.292  -207.255 38.784  1.00 98.83  ? 45  ILE   O CG1 1 
ATOM   24965 C  CG2 . ILE   O  1  45  ? -2.251  -208.486 36.574  1.00 95.88  ? 45  ILE   O CG2 1 
ATOM   24966 C  CD1 . ILE   O  1  45  ? -0.999  -206.483 38.648  1.00 99.73  ? 45  ILE   O CD1 1 
ATOM   24967 N  N   . ALA   O  1  46  ? -3.010  -211.425 39.961  1.00 104.36 ? 46  ALA   O N   1 
ATOM   24968 C  CA  . ALA   O  1  46  ? -2.940  -212.232 41.200  1.00 107.23 ? 46  ALA   O CA  1 
ATOM   24969 C  C   . ALA   O  1  46  ? -1.700  -213.130 41.168  1.00 107.25 ? 46  ALA   O C   1 
ATOM   24970 O  O   . ALA   O  1  46  ? -1.187  -213.407 40.064  1.00 109.93 ? 46  ALA   O O   1 
ATOM   24971 C  CB  . ALA   O  1  46  ? -4.200  -213.050 41.343  1.00 108.74 ? 46  ALA   O CB  1 
ATOM   24972 N  N   . THR   O  1  47  ? -1.249  -213.572 42.343  1.00 104.25 ? 47  THR   O N   1 
ATOM   24973 C  CA  . THR   O  1  47  ? -0.160  -214.571 42.505  1.00 106.08 ? 47  THR   O CA  1 
ATOM   24974 C  C   . THR   O  1  47  ? -0.189  -215.142 43.927  1.00 109.35 ? 47  THR   O C   1 
ATOM   24975 O  O   . THR   O  1  47  ? -0.748  -214.482 44.827  1.00 110.16 ? 47  THR   O O   1 
ATOM   24976 C  CB  . THR   O  1  47  ? 1.206   -213.963 42.160  1.00 101.98 ? 47  THR   O CB  1 
ATOM   24977 O  OG1 . THR   O  1  47  ? 2.182   -215.004 42.134  1.00 99.94  ? 47  THR   O OG1 1 
ATOM   24978 C  CG2 . THR   O  1  47  ? 1.649   -212.904 43.144  1.00 100.26 ? 47  THR   O CG2 1 
ATOM   24979 N  N   . GLU   O  1  48  ? 0.384   -216.335 44.099  1.00 115.47 ? 48  GLU   O N   1 
ATOM   24980 C  CA  . GLU   O  1  48  ? 0.630   -216.976 45.416  1.00 119.63 ? 48  GLU   O CA  1 
ATOM   24981 C  C   . GLU   O  1  48  ? 1.853   -216.303 46.051  1.00 115.50 ? 48  GLU   O C   1 
ATOM   24982 O  O   . GLU   O  1  48  ? 2.828   -216.041 45.318  1.00 111.09 ? 48  GLU   O O   1 
ATOM   24983 C  CB  . GLU   O  1  48  ? 0.834   -218.483 45.228  1.00 124.03 ? 48  GLU   O CB  1 
ATOM   24984 C  CG  . GLU   O  1  48  ? 1.043   -219.253 46.522  1.00 129.42 ? 48  GLU   O CG  1 
ATOM   24985 C  CD  . GLU   O  1  48  ? 1.592   -220.658 46.342  1.00 133.79 ? 48  GLU   O CD  1 
ATOM   24986 O  OE1 . GLU   O  1  48  ? 1.346   -221.260 45.277  1.00 142.75 ? 48  GLU   O OE1 1 
ATOM   24987 O  OE2 . GLU   O  1  48  ? 2.274   -221.143 47.266  1.00 144.62 ? 48  GLU   O OE2 1 
ATOM   24988 N  N   . LYS   O  1  49  ? 1.791   -216.015 47.355  1.00 117.43 ? 49  LYS   O N   1 
ATOM   24989 C  CA  . LYS   O  1  49  ? 2.948   -215.540 48.161  1.00 121.94 ? 49  LYS   O CA  1 
ATOM   24990 C  C   . LYS   O  1  49  ? 3.647   -216.749 48.788  1.00 125.60 ? 49  LYS   O C   1 
ATOM   24991 O  O   . LYS   O  1  49  ? 3.330   -217.086 49.947  1.00 130.06 ? 49  LYS   O O   1 
ATOM   24992 C  CB  . LYS   O  1  49  ? 2.506   -214.541 49.235  1.00 122.34 ? 49  LYS   O CB  1 
ATOM   24993 C  CG  . LYS   O  1  49  ? 2.396   -213.101 48.756  1.00 123.33 ? 49  LYS   O CG  1 
ATOM   24994 C  CD  . LYS   O  1  49  ? 2.520   -212.077 49.864  1.00 125.73 ? 49  LYS   O CD  1 
ATOM   24995 C  CE  . LYS   O  1  49  ? 1.211   -211.804 50.571  1.00 128.13 ? 49  LYS   O CE  1 
ATOM   24996 N  NZ  . LYS   O  1  49  ? 1.334   -210.672 51.518  1.00 128.64 ? 49  LYS   O NZ  1 
ATOM   24997 N  N   . LYS   O  1  50  ? 4.555   -217.377 48.035  1.00 134.39 ? 50  LYS   O N   1 
ATOM   24998 C  CA  . LYS   O  1  50  ? 5.401   -218.507 48.506  1.00 138.46 ? 50  LYS   O CA  1 
ATOM   24999 C  C   . LYS   O  1  50  ? 6.329   -217.981 49.607  1.00 138.84 ? 50  LYS   O C   1 
ATOM   25000 O  O   . LYS   O  1  50  ? 7.301   -217.275 49.273  1.00 140.43 ? 50  LYS   O O   1 
ATOM   25001 C  CB  . LYS   O  1  50  ? 6.179   -219.121 47.335  1.00 144.35 ? 50  LYS   O CB  1 
ATOM   25002 C  CG  . LYS   O  1  50  ? 7.307   -220.079 47.705  1.00 141.10 ? 50  LYS   O CG  1 
ATOM   25003 C  CD  . LYS   O  1  50  ? 6.872   -221.510 47.912  1.00 142.27 ? 50  LYS   O CD  1 
ATOM   25004 C  CE  . LYS   O  1  50  ? 8.046   -222.423 48.191  1.00 145.40 ? 50  LYS   O CE  1 
ATOM   25005 N  NZ  . LYS   O  1  50  ? 7.662   -223.853 48.131  1.00 150.93 ? 50  LYS   O NZ  1 
ATOM   25006 N  N   . SER   O  1  51  ? 6.019   -218.298 50.868  1.00 134.91 ? 51  SER   O N   1 
ATOM   25007 C  CA  . SER   O  1  51  ? 6.810   -217.912 52.066  1.00 132.02 ? 51  SER   O CA  1 
ATOM   25008 C  C   . SER   O  1  51  ? 8.066   -218.791 52.162  1.00 139.91 ? 51  SER   O C   1 
ATOM   25009 O  O   . SER   O  1  51  ? 7.924   -220.031 52.085  1.00 144.64 ? 51  SER   O O   1 
ATOM   25010 C  CB  . SER   O  1  51  ? 5.968   -218.007 53.311  1.00 126.72 ? 51  SER   O CB  1 
ATOM   25011 O  OG  . SER   O  1  51  ? 6.638   -217.432 54.421  1.00 120.98 ? 51  SER   O OG  1 
ATOM   25012 N  N   . SER   O  1  52  ? 9.242   -218.170 52.322  1.00 136.73 ? 52  SER   O N   1 
ATOM   25013 C  CA  . SER   O  1  52  ? 10.572  -218.840 52.409  1.00 139.93 ? 52  SER   O CA  1 
ATOM   25014 C  C   . SER   O  1  52  ? 10.747  -219.503 53.782  1.00 137.48 ? 52  SER   O C   1 
ATOM   25015 O  O   . SER   O  1  52  ? 11.461  -220.522 53.864  1.00 130.48 ? 52  SER   O O   1 
ATOM   25016 C  CB  . SER   O  1  52  ? 11.696  -217.868 52.135  1.00 138.28 ? 52  SER   O CB  1 
ATOM   25017 O  OG  . SER   O  1  52  ? 11.633  -217.370 50.808  1.00 136.68 ? 52  SER   O OG  1 
ATOM   25018 N  N   . SER   O  1  53  ? 10.131  -218.923 54.816  1.00 140.00 ? 53  SER   O N   1 
ATOM   25019 C  CA  . SER   O  1  53  ? 10.133  -219.408 56.220  1.00 138.68 ? 53  SER   O CA  1 
ATOM   25020 C  C   . SER   O  1  53  ? 8.882   -218.879 56.918  1.00 137.08 ? 53  SER   O C   1 
ATOM   25021 O  O   . SER   O  1  53  ? 8.413   -217.792 56.587  1.00 140.56 ? 53  SER   O O   1 
ATOM   25022 C  CB  . SER   O  1  53  ? 11.397  -218.971 56.926  1.00 137.34 ? 53  SER   O CB  1 
ATOM   25023 O  OG  . SER   O  1  53  ? 11.391  -219.361 58.292  1.00 135.78 ? 53  SER   O OG  1 
ATOM   25024 N  N   . PRO   O  1  54  ? 8.283   -219.615 57.885  1.00 135.30 ? 54  PRO   O N   1 
ATOM   25025 C  CA  . PRO   O  1  54  ? 7.151   -219.085 58.648  1.00 130.72 ? 54  PRO   O CA  1 
ATOM   25026 C  C   . PRO   O  1  54  ? 7.544   -217.936 59.593  1.00 128.93 ? 54  PRO   O C   1 
ATOM   25027 O  O   . PRO   O  1  54  ? 6.652   -217.252 60.060  1.00 132.93 ? 54  PRO   O O   1 
ATOM   25028 C  CB  . PRO   O  1  54  ? 6.625   -220.296 59.432  1.00 132.11 ? 54  PRO   O CB  1 
ATOM   25029 C  CG  . PRO   O  1  54  ? 7.809   -221.235 59.520  1.00 137.50 ? 54  PRO   O CG  1 
ATOM   25030 C  CD  . PRO   O  1  54  ? 8.631   -220.991 58.270  1.00 136.67 ? 54  PRO   O CD  1 
ATOM   25031 N  N   . LEU   O  1  55  ? 8.847   -217.751 59.846  1.00 123.35 ? 55  LEU   O N   1 
ATOM   25032 C  CA  . LEU   O  1  55  ? 9.398   -216.606 60.623  1.00 119.87 ? 55  LEU   O CA  1 
ATOM   25033 C  C   . LEU   O  1  55  ? 9.461   -215.348 59.746  1.00 116.89 ? 55  LEU   O C   1 
ATOM   25034 O  O   . LEU   O  1  55  ? 9.449   -214.240 60.319  1.00 116.31 ? 55  LEU   O O   1 
ATOM   25035 C  CB  . LEU   O  1  55  ? 10.788  -216.966 61.157  1.00 116.69 ? 55  LEU   O CB  1 
ATOM   25036 C  CG  . LEU   O  1  55  ? 10.832  -218.031 62.250  1.00 115.93 ? 55  LEU   O CG  1 
ATOM   25037 C  CD1 . LEU   O  1  55  ? 12.262  -218.249 62.718  1.00 117.90 ? 55  LEU   O CD1 1 
ATOM   25038 C  CD2 . LEU   O  1  55  ? 9.945   -217.656 63.429  1.00 116.13 ? 55  LEU   O CD2 1 
ATOM   25039 N  N   . ALA   O  1  56  ? 9.542   -215.504 58.420  1.00 109.64 ? 56  ALA   O N   1 
ATOM   25040 C  CA  . ALA   O  1  56  ? 9.510   -214.386 57.449  1.00 105.24 ? 56  ALA   O CA  1 
ATOM   25041 C  C   . ALA   O  1  56  ? 8.144   -213.698 57.537  1.00 107.92 ? 56  ALA   O C   1 
ATOM   25042 O  O   . ALA   O  1  56  ? 7.148   -214.393 57.824  1.00 105.63 ? 56  ALA   O O   1 
ATOM   25043 C  CB  . ALA   O  1  56  ? 9.791   -214.877 56.049  1.00 101.80 ? 56  ALA   O CB  1 
ATOM   25044 N  N   . MET   O  1  57  ? 8.120   -212.379 57.328  1.00 109.11 ? 57  MET   O N   1 
ATOM   25045 C  CA  . MET   O  1  57  ? 6.890   -211.550 57.234  1.00 112.27 ? 57  MET   O CA  1 
ATOM   25046 C  C   . MET   O  1  57  ? 6.622   -211.274 55.750  1.00 105.88 ? 57  MET   O C   1 
ATOM   25047 O  O   . MET   O  1  57  ? 7.262   -210.373 55.190  1.00 102.66 ? 57  MET   O O   1 
ATOM   25048 C  CB  . MET   O  1  57  ? 7.060   -210.233 57.998  1.00 115.49 ? 57  MET   O CB  1 
ATOM   25049 C  CG  . MET   O  1  57  ? 7.392   -210.424 59.466  1.00 122.05 ? 57  MET   O CG  1 
ATOM   25050 S  SD  . MET   O  1  57  ? 7.468   -208.855 60.368  1.00 127.03 ? 57  MET   O SD  1 
ATOM   25051 C  CE  . MET   O  1  57  ? 8.915   -208.097 59.630  1.00 126.97 ? 57  MET   O CE  1 
ATOM   25052 N  N   . SER   O  1  58  ? 5.732   -212.054 55.131  1.00 110.07 ? 58  SER   O N   1 
ATOM   25053 C  CA  . SER   O  1  58  ? 5.489   -212.065 53.664  1.00 115.57 ? 58  SER   O CA  1 
ATOM   25054 C  C   . SER   O  1  58  ? 4.830   -210.757 53.205  1.00 114.33 ? 58  SER   O C   1 
ATOM   25055 O  O   . SER   O  1  58  ? 4.731   -210.561 51.979  1.00 116.90 ? 58  SER   O O   1 
ATOM   25056 C  CB  . SER   O  1  58  ? 4.668   -213.262 53.258  1.00 120.12 ? 58  SER   O CB  1 
ATOM   25057 O  OG  . SER   O  1  58  ? 3.432   -213.286 53.955  1.00 131.53 ? 58  SER   O OG  1 
ATOM   25058 N  N   . GLU   O  1  59  ? 4.399   -209.902 54.140  1.00 115.72 ? 59  GLU   O N   1 
ATOM   25059 C  CA  . GLU   O  1  59  ? 3.847   -208.549 53.845  1.00 114.84 ? 59  GLU   O CA  1 
ATOM   25060 C  C   . GLU   O  1  59  ? 4.993   -207.644 53.375  1.00 108.17 ? 59  GLU   O C   1 
ATOM   25061 O  O   . GLU   O  1  59  ? 4.755   -206.817 52.480  1.00 108.33 ? 59  GLU   O O   1 
ATOM   25062 C  CB  . GLU   O  1  59  ? 3.144   -207.921 55.056  1.00 117.83 ? 59  GLU   O CB  1 
ATOM   25063 C  CG  . GLU   O  1  59  ? 2.445   -208.912 55.976  1.00 123.94 ? 59  GLU   O CG  1 
ATOM   25064 C  CD  . GLU   O  1  59  ? 3.298   -209.430 57.125  1.00 127.00 ? 59  GLU   O CD  1 
ATOM   25065 O  OE1 . GLU   O  1  59  ? 3.801   -208.597 57.909  1.00 127.87 ? 59  GLU   O OE1 1 
ATOM   25066 O  OE2 . GLU   O  1  59  ? 3.470   -210.666 57.227  1.00 130.11 ? 59  GLU   O OE2 1 
ATOM   25067 N  N   . THR   O  1  60  ? 6.191   -207.814 53.947  1.00 105.51 ? 60  THR   O N   1 
ATOM   25068 C  CA  . THR   O  1  60  ? 7.408   -207.014 53.634  1.00 109.65 ? 60  THR   O CA  1 
ATOM   25069 C  C   . THR   O  1  60  ? 7.936   -207.359 52.235  1.00 111.16 ? 60  THR   O C   1 
ATOM   25070 O  O   . THR   O  1  60  ? 8.763   -206.585 51.723  1.00 116.54 ? 60  THR   O O   1 
ATOM   25071 C  CB  . THR   O  1  60  ? 8.515   -207.208 54.680  1.00 110.89 ? 60  THR   O CB  1 
ATOM   25072 O  OG1 . THR   O  1  60  ? 8.934   -208.572 54.652  1.00 110.30 ? 60  THR   O OG1 1 
ATOM   25073 C  CG2 . THR   O  1  60  ? 8.082   -206.823 56.078  1.00 113.38 ? 60  THR   O CG2 1 
ATOM   25074 N  N   . LEU   O  1  61  ? 7.497   -208.478 51.651  1.00 114.58 ? 61  LEU   O N   1 
ATOM   25075 C  CA  . LEU   O  1  61  ? 7.854   -208.891 50.268  1.00 121.42 ? 61  LEU   O CA  1 
ATOM   25076 C  C   . LEU   O  1  61  ? 6.621   -208.726 49.373  1.00 117.80 ? 61  LEU   O C   1 
ATOM   25077 O  O   . LEU   O  1  61  ? 5.680   -209.535 49.497  1.00 122.81 ? 61  LEU   O O   1 
ATOM   25078 C  CB  . LEU   O  1  61  ? 8.352   -210.340 50.281  1.00 125.21 ? 61  LEU   O CB  1 
ATOM   25079 C  CG  . LEU   O  1  61  ? 9.521   -210.647 49.345  1.00 132.96 ? 61  LEU   O CG  1 
ATOM   25080 C  CD1 . LEU   O  1  61  ? 9.859   -212.130 49.379  1.00 136.08 ? 61  LEU   O CD1 1 
ATOM   25081 C  CD2 . LEU   O  1  61  ? 9.231   -210.203 47.917  1.00 132.74 ? 61  LEU   O CD2 1 
ATOM   25082 N  N   . SER   O  1  62  ? 6.630   -207.703 48.519  1.00 114.76 ? 62  SER   O N   1 
ATOM   25083 C  CA  . SER   O  1  62  ? 5.527   -207.366 47.584  1.00 117.31 ? 62  SER   O CA  1 
ATOM   25084 C  C   . SER   O  1  62  ? 5.857   -207.920 46.194  1.00 113.14 ? 62  SER   O C   1 
ATOM   25085 O  O   . SER   O  1  62  ? 6.826   -207.432 45.579  1.00 121.94 ? 62  SER   O O   1 
ATOM   25086 C  CB  . SER   O  1  62  ? 5.291   -205.875 47.554  1.00 118.98 ? 62  SER   O CB  1 
ATOM   25087 O  OG  . SER   O  1  62  ? 4.173   -205.549 46.742  1.00 118.20 ? 62  SER   O OG  1 
ATOM   25088 N  N   . LYS   O  1  63  ? 5.091   -208.914 45.734  1.00 108.88 ? 63  LYS   O N   1 
ATOM   25089 C  CA  . LYS   O  1  63  ? 5.202   -209.504 44.372  1.00 109.45 ? 63  LYS   O CA  1 
ATOM   25090 C  C   . LYS   O  1  63  ? 4.445   -208.630 43.363  1.00 104.92 ? 63  LYS   O C   1 
ATOM   25091 O  O   . LYS   O  1  63  ? 4.906   -208.544 42.211  1.00 104.85 ? 63  LYS   O O   1 
ATOM   25092 C  CB  . LYS   O  1  63  ? 4.675   -210.942 44.362  1.00 110.00 ? 63  LYS   O CB  1 
ATOM   25093 C  CG  . LYS   O  1  63  ? 5.562   -211.954 45.076  1.00 111.71 ? 63  LYS   O CG  1 
ATOM   25094 C  CD  . LYS   O  1  63  ? 5.087   -213.382 44.936  1.00 111.56 ? 63  LYS   O CD  1 
ATOM   25095 C  CE  . LYS   O  1  63  ? 5.247   -213.926 43.532  1.00 113.59 ? 63  LYS   O CE  1 
ATOM   25096 N  NZ  . LYS   O  1  63  ? 4.906   -215.366 43.461  1.00 116.27 ? 63  LYS   O NZ  1 
ATOM   25097 N  N   . VAL   O  1  64  ? 3.326   -208.021 43.777  1.00 103.82 ? 64  VAL   O N   1 
ATOM   25098 C  CA  . VAL   O  1  64  ? 2.517   -207.074 42.951  1.00 106.21 ? 64  VAL   O CA  1 
ATOM   25099 C  C   . VAL   O  1  64  ? 2.953   -205.643 43.293  1.00 104.60 ? 64  VAL   O C   1 
ATOM   25100 O  O   . VAL   O  1  64  ? 2.823   -205.254 44.471  1.00 108.89 ? 64  VAL   O O   1 
ATOM   25101 C  CB  . VAL   O  1  64  ? 1.003   -207.262 43.175  1.00 107.31 ? 64  VAL   O CB  1 
ATOM   25102 C  CG1 . VAL   O  1  64  ? 0.187   -206.354 42.270  1.00 108.53 ? 64  VAL   O CG1 1 
ATOM   25103 C  CG2 . VAL   O  1  64  ? 0.569   -208.706 42.988  1.00 109.77 ? 64  VAL   O CG2 1 
ATOM   25104 N  N   . SER   O  1  65  ? 3.425   -204.886 42.295  1.00 101.03 ? 65  SER   O N   1 
ATOM   25105 C  CA  . SER   O  1  65  ? 4.009   -203.528 42.454  1.00 98.15  ? 65  SER   O CA  1 
ATOM   25106 C  C   . SER   O  1  65  ? 3.245   -202.505 41.602  1.00 96.70  ? 65  SER   O C   1 
ATOM   25107 O  O   . SER   O  1  65  ? 2.905   -202.824 40.446  1.00 91.32  ? 65  SER   O O   1 
ATOM   25108 C  CB  . SER   O  1  65  ? 5.474   -203.539 42.107  1.00 97.89  ? 65  SER   O CB  1 
ATOM   25109 O  OG  . SER   O  1  65  ? 6.173   -204.480 42.906  1.00 99.26  ? 65  SER   O OG  1 
ATOM   25110 N  N   . LEU   O  1  66  ? 2.987   -201.325 42.177  1.00 97.61  ? 66  LEU   O N   1 
ATOM   25111 C  CA  . LEU   O  1  66  ? 2.505   -200.104 41.473  1.00 97.46  ? 66  LEU   O CA  1 
ATOM   25112 C  C   . LEU   O  1  66  ? 3.677   -199.517 40.677  1.00 95.58  ? 66  LEU   O C   1 
ATOM   25113 O  O   . LEU   O  1  66  ? 4.735   -199.283 41.291  1.00 93.26  ? 66  LEU   O O   1 
ATOM   25114 C  CB  . LEU   O  1  66  ? 1.982   -199.109 42.519  1.00 98.59  ? 66  LEU   O CB  1 
ATOM   25115 C  CG  . LEU   O  1  66  ? 1.378   -197.801 41.999  1.00 99.00  ? 66  LEU   O CG  1 
ATOM   25116 C  CD1 . LEU   O  1  66  ? 0.514   -197.144 43.067  1.00 100.49 ? 66  LEU   O CD1 1 
ATOM   25117 C  CD2 . LEU   O  1  66  ? 2.450   -196.824 41.536  1.00 98.29  ? 66  LEU   O CD2 1 
ATOM   25118 N  N   . LEU   O  1  67  ? 3.494   -199.291 39.371  1.00 96.32  ? 67  LEU   O N   1 
ATOM   25119 C  CA  . LEU   O  1  67  ? 4.494   -198.630 38.485  1.00 97.55  ? 67  LEU   O CA  1 
ATOM   25120 C  C   . LEU   O  1  67  ? 4.107   -197.157 38.289  1.00 99.27  ? 67  LEU   O C   1 
ATOM   25121 O  O   . LEU   O  1  67  ? 4.987   -196.289 38.455  1.00 103.95 ? 67  LEU   O O   1 
ATOM   25122 C  CB  . LEU   O  1  67  ? 4.556   -199.363 37.142  1.00 96.10  ? 67  LEU   O CB  1 
ATOM   25123 C  CG  . LEU   O  1  67  ? 4.901   -200.851 37.194  1.00 93.59  ? 67  LEU   O CG  1 
ATOM   25124 C  CD1 . LEU   O  1  67  ? 5.156   -201.377 35.791  1.00 92.99  ? 67  LEU   O CD1 1 
ATOM   25125 C  CD2 . LEU   O  1  67  ? 6.105   -201.121 38.085  1.00 93.61  ? 67  LEU   O CD2 1 
ATOM   25126 N  N   . THR   O  1  68  ? 2.847   -196.902 37.919  1.00 98.46  ? 68  THR   O N   1 
ATOM   25127 C  CA  . THR   O  1  68  ? 2.199   -195.561 37.888  1.00 97.80  ? 68  THR   O CA  1 
ATOM   25128 C  C   . THR   O  1  68  ? 0.855   -195.669 38.603  1.00 97.93  ? 68  THR   O C   1 
ATOM   25129 O  O   . THR   O  1  68  ? 0.389   -196.772 38.868  1.00 100.31 ? 68  THR   O O   1 
ATOM   25130 C  CB  . THR   O  1  68  ? 2.046   -195.043 36.450  1.00 95.27  ? 68  THR   O CB  1 
ATOM   25131 O  OG1 . THR   O  1  68  ? 0.976   -195.745 35.820  1.00 98.02  ? 68  THR   O OG1 1 
ATOM   25132 C  CG2 . THR   O  1  68  ? 3.306   -195.188 35.624  1.00 94.70  ? 68  THR   O CG2 1 
ATOM   25133 N  N   . PRO   O  1  69  ? 0.183   -194.547 38.950  1.00 99.51  ? 69  PRO   O N   1 
ATOM   25134 C  CA  . PRO   O  1  69  ? -1.142  -194.610 39.573  1.00 99.13  ? 69  PRO   O CA  1 
ATOM   25135 C  C   . PRO   O  1  69  ? -2.193  -195.443 38.819  1.00 94.94  ? 69  PRO   O C   1 
ATOM   25136 O  O   . PRO   O  1  69  ? -3.191  -195.775 39.427  1.00 95.28  ? 69  PRO   O O   1 
ATOM   25137 C  CB  . PRO   O  1  69  ? -1.587  -193.140 39.597  1.00 100.76 ? 69  PRO   O CB  1 
ATOM   25138 C  CG  . PRO   O  1  69  ? -0.289  -192.364 39.667  1.00 102.58 ? 69  PRO   O CG  1 
ATOM   25139 C  CD  . PRO   O  1  69  ? 0.677   -193.166 38.820  1.00 101.28 ? 69  PRO   O CD  1 
ATOM   25140 N  N   . ASP   O  1  70  ? -1.962  -195.741 37.534  1.00 95.41  ? 70  ASP   O N   1 
ATOM   25141 C  CA  . ASP   O  1  70  ? -2.912  -196.485 36.662  1.00 98.40  ? 70  ASP   O CA  1 
ATOM   25142 C  C   . ASP   O  1  70  ? -2.273  -197.760 36.091  1.00 93.73  ? 70  ASP   O C   1 
ATOM   25143 O  O   . ASP   O  1  70  ? -2.928  -198.384 35.242  1.00 94.12  ? 70  ASP   O O   1 
ATOM   25144 C  CB  . ASP   O  1  70  ? -3.405  -195.601 35.511  1.00 102.22 ? 70  ASP   O CB  1 
ATOM   25145 C  CG  . ASP   O  1  70  ? -4.161  -194.358 35.948  1.00 105.43 ? 70  ASP   O CG  1 
ATOM   25146 O  OD1 . ASP   O  1  70  ? -4.773  -194.394 37.036  1.00 114.64 ? 70  ASP   O OD1 1 
ATOM   25147 O  OD2 . ASP   O  1  70  ? -4.136  -193.366 35.191  1.00 110.07 ? 70  ASP   O OD2 1 
ATOM   25148 N  N   . ILE   O  1  71  ? -1.061  -198.142 36.517  1.00 92.13  ? 71  ILE   O N   1 
ATOM   25149 C  CA  . ILE   O  1  71  ? -0.353  -199.363 36.012  1.00 94.30  ? 71  ILE   O CA  1 
ATOM   25150 C  C   . ILE   O  1  71  ? 0.230   -200.163 37.188  1.00 94.13  ? 71  ILE   O C   1 
ATOM   25151 O  O   . ILE   O  1  71  ? 0.899   -199.562 38.051  1.00 94.66  ? 71  ILE   O O   1 
ATOM   25152 C  CB  . ILE   O  1  71  ? 0.738   -199.000 34.982  1.00 91.20  ? 71  ILE   O CB  1 
ATOM   25153 C  CG1 . ILE   O  1  71  ? 0.150   -198.340 33.733  1.00 90.05  ? 71  ILE   O CG1 1 
ATOM   25154 C  CG2 . ILE   O  1  71  ? 1.564   -200.227 34.621  1.00 92.46  ? 71  ILE   O CG2 1 
ATOM   25155 C  CD1 . ILE   O  1  71  ? 1.166   -197.607 32.891  1.00 91.18  ? 71  ILE   O CD1 1 
ATOM   25156 N  N   . GLY   O  1  72  ? 0.015   -201.482 37.184  1.00 94.04  ? 72  GLY   O N   1 
ATOM   25157 C  CA  . GLY   O  1  72  ? 0.570   -202.430 38.170  1.00 95.15  ? 72  GLY   O CA  1 
ATOM   25158 C  C   . GLY   O  1  72  ? 1.218   -203.620 37.483  1.00 94.87  ? 72  GLY   O C   1 
ATOM   25159 O  O   . GLY   O  1  72  ? 0.806   -203.942 36.350  1.00 95.10  ? 72  GLY   O O   1 
ATOM   25160 N  N   . ALA   O  1  73  ? 2.197   -204.251 38.137  1.00 96.22  ? 73  ALA   O N   1 
ATOM   25161 C  CA  . ALA   O  1  73  ? 2.997   -205.371 37.586  1.00 98.80  ? 73  ALA   O CA  1 
ATOM   25162 C  C   . ALA   O  1  73  ? 3.039   -206.541 38.574  1.00 98.66  ? 73  ALA   O C   1 
ATOM   25163 O  O   . ALA   O  1  73  ? 3.068   -206.304 39.795  1.00 97.72  ? 73  ALA   O O   1 
ATOM   25164 C  CB  . ALA   O  1  73  ? 4.390   -204.898 37.256  1.00 99.67  ? 73  ALA   O CB  1 
ATOM   25165 N  N   . VAL   O  1  74  ? 3.048   -207.761 38.038  1.00 100.69 ? 74  VAL   O N   1 
ATOM   25166 C  CA  . VAL   O  1  74  ? 3.300   -209.033 38.777  1.00 101.14 ? 74  VAL   O CA  1 
ATOM   25167 C  C   . VAL   O  1  74  ? 4.186   -209.898 37.875  1.00 100.36 ? 74  VAL   O C   1 
ATOM   25168 O  O   . VAL   O  1  74  ? 4.263   -209.597 36.666  1.00 100.51 ? 74  VAL   O O   1 
ATOM   25169 C  CB  . VAL   O  1  74  ? 1.981   -209.733 39.159  1.00 99.73  ? 74  VAL   O CB  1 
ATOM   25170 C  CG1 . VAL   O  1  74  ? 1.316   -210.399 37.966  1.00 98.88  ? 74  VAL   O CG1 1 
ATOM   25171 C  CG2 . VAL   O  1  74  ? 2.174   -210.731 40.289  1.00 101.75 ? 74  VAL   O CG2 1 
ATOM   25172 N  N   . TYR   O  1  75  ? 4.840   -210.918 38.429  1.00 100.37 ? 75  TYR   O N   1 
ATOM   25173 C  CA  . TYR   O  1  75  ? 5.860   -211.714 37.701  1.00 100.88 ? 75  TYR   O CA  1 
ATOM   25174 C  C   . TYR   O  1  75  ? 5.802   -213.192 38.095  1.00 100.84 ? 75  TYR   O C   1 
ATOM   25175 O  O   . TYR   O  1  75  ? 5.182   -213.550 39.118  1.00 100.19 ? 75  TYR   O O   1 
ATOM   25176 C  CB  . TYR   O  1  75  ? 7.258   -211.174 38.003  1.00 101.31 ? 75  TYR   O CB  1 
ATOM   25177 C  CG  . TYR   O  1  75  ? 7.820   -211.668 39.311  1.00 99.11  ? 75  TYR   O CG  1 
ATOM   25178 C  CD1 . TYR   O  1  75  ? 7.284   -211.256 40.521  1.00 98.98  ? 75  TYR   O CD1 1 
ATOM   25179 C  CD2 . TYR   O  1  75  ? 8.863   -212.579 39.340  1.00 99.22  ? 75  TYR   O CD2 1 
ATOM   25180 C  CE1 . TYR   O  1  75  ? 7.785   -211.717 41.727  1.00 97.78  ? 75  TYR   O CE1 1 
ATOM   25181 C  CE2 . TYR   O  1  75  ? 9.378   -213.048 40.538  1.00 98.77  ? 75  TYR   O CE2 1 
ATOM   25182 C  CZ  . TYR   O  1  75  ? 8.836   -212.617 41.736  1.00 97.34  ? 75  TYR   O CZ  1 
ATOM   25183 O  OH  . TYR   O  1  75  ? 9.333   -213.079 42.920  1.00 96.93  ? 75  TYR   O OH  1 
ATOM   25184 N  N   . SER   O  1  76  ? 6.456   -214.013 37.272  1.00 100.37 ? 76  SER   O N   1 
ATOM   25185 C  CA  . SER   O  1  76  ? 6.890   -215.398 37.579  1.00 100.41 ? 76  SER   O CA  1 
ATOM   25186 C  C   . SER   O  1  76  ? 8.387   -215.504 37.274  1.00 97.68  ? 76  SER   O C   1 
ATOM   25187 O  O   . SER   O  1  76  ? 8.826   -214.919 36.262  1.00 98.22  ? 76  SER   O O   1 
ATOM   25188 C  CB  . SER   O  1  76  ? 6.080   -216.410 36.807  1.00 101.35 ? 76  SER   O CB  1 
ATOM   25189 O  OG  . SER   O  1  76  ? 4.783   -216.552 37.368  1.00 102.20 ? 76  SER   O OG  1 
ATOM   25190 N  N   . GLY   O  1  77  ? 9.141   -216.182 38.142  1.00 94.57  ? 77  GLY   O N   1 
ATOM   25191 C  CA  . GLY   O  1  77  ? 10.586  -216.412 37.969  1.00 93.10  ? 77  GLY   O CA  1 
ATOM   25192 C  C   . GLY   O  1  77  ? 11.374  -215.904 39.159  1.00 90.43  ? 77  GLY   O C   1 
ATOM   25193 O  O   . GLY   O  1  77  ? 10.958  -216.181 40.303  1.00 87.38  ? 77  GLY   O O   1 
ATOM   25194 N  N   . MET   O  1  78  ? 12.453  -215.160 38.897  1.00 91.25  ? 78  MET   O N   1 
ATOM   25195 C  CA  . MET   O  1  78  ? 13.460  -214.736 39.907  1.00 92.58  ? 78  MET   O CA  1 
ATOM   25196 C  C   . MET   O  1  78  ? 13.068  -213.376 40.502  1.00 91.69  ? 78  MET   O C   1 
ATOM   25197 O  O   . MET   O  1  78  ? 13.030  -212.389 39.747  1.00 90.60  ? 78  MET   O O   1 
ATOM   25198 C  CB  . MET   O  1  78  ? 14.849  -214.640 39.270  1.00 91.83  ? 78  MET   O CB  1 
ATOM   25199 C  CG  . MET   O  1  78  ? 15.313  -215.941 38.650  1.00 91.75  ? 78  MET   O CG  1 
ATOM   25200 S  SD  . MET   O  1  78  ? 16.852  -215.731 37.734  1.00 91.78  ? 78  MET   O SD  1 
ATOM   25201 C  CE  . MET   O  1  78  ? 18.000  -215.479 39.085  1.00 94.01  ? 78  MET   O CE  1 
ATOM   25202 N  N   . GLY   O  1  79  ? 12.808  -213.342 41.814  1.00 94.19  ? 79  GLY   O N   1 
ATOM   25203 C  CA  . GLY   O  1  79  ? 12.353  -212.156 42.568  1.00 91.56  ? 79  GLY   O CA  1 
ATOM   25204 C  C   . GLY   O  1  79  ? 13.316  -210.976 42.467  1.00 89.80  ? 79  GLY   O C   1 
ATOM   25205 O  O   . GLY   O  1  79  ? 12.906  -209.880 42.092  1.00 85.59  ? 79  GLY   O O   1 
ATOM   25206 N  N   . PRO   O  1  80  ? 14.610  -211.147 42.828  1.00 90.40  ? 80  PRO   O N   1 
ATOM   25207 C  CA  . PRO   O  1  80  ? 15.592  -210.065 42.718  1.00 91.61  ? 80  PRO   O CA  1 
ATOM   25208 C  C   . PRO   O  1  80  ? 15.614  -209.364 41.348  1.00 91.22  ? 80  PRO   O C   1 
ATOM   25209 O  O   . PRO   O  1  80  ? 15.664  -208.149 41.325  1.00 92.15  ? 80  PRO   O O   1 
ATOM   25210 C  CB  . PRO   O  1  80  ? 16.924  -210.784 42.986  1.00 91.83  ? 80  PRO   O CB  1 
ATOM   25211 C  CG  . PRO   O  1  80  ? 16.541  -211.915 43.911  1.00 91.94  ? 80  PRO   O CG  1 
ATOM   25212 C  CD  . PRO   O  1  80  ? 15.188  -212.371 43.405  1.00 91.12  ? 80  PRO   O CD  1 
ATOM   25213 N  N   . ASP   O  1  81  ? 15.579  -210.134 40.255  1.00 93.84  ? 81  ASP   O N   1 
ATOM   25214 C  CA  . ASP   O  1  81  ? 15.557  -209.617 38.858  1.00 92.92  ? 81  ASP   O CA  1 
ATOM   25215 C  C   . ASP   O  1  81  ? 14.314  -208.744 38.658  1.00 89.65  ? 81  ASP   O C   1 
ATOM   25216 O  O   . ASP   O  1  81  ? 14.437  -207.704 37.988  1.00 87.84  ? 81  ASP   O O   1 
ATOM   25217 C  CB  . ASP   O  1  81  ? 15.588  -210.752 37.829  1.00 95.75  ? 81  ASP   O CB  1 
ATOM   25218 C  CG  . ASP   O  1  81  ? 16.965  -211.348 37.584  1.00 99.04  ? 81  ASP   O CG  1 
ATOM   25219 O  OD1 . ASP   O  1  81  ? 17.860  -211.139 38.428  1.00 105.08 ? 81  ASP   O OD1 1 
ATOM   25220 O  OD2 . ASP   O  1  81  ? 17.131  -212.022 36.546  1.00 101.06 ? 81  ASP   O OD2 1 
ATOM   25221 N  N   . TYR   O  1  82  ? 13.166  -209.163 39.204  1.00 89.09  ? 82  TYR   O N   1 
ATOM   25222 C  CA  . TYR   O  1  82  ? 11.869  -208.435 39.132  1.00 91.51  ? 82  TYR   O CA  1 
ATOM   25223 C  C   . TYR   O  1  82  ? 11.973  -207.112 39.897  1.00 92.06  ? 82  TYR   O C   1 
ATOM   25224 O  O   . TYR   O  1  82  ? 11.532  -206.080 39.360  1.00 92.18  ? 82  TYR   O O   1 
ATOM   25225 C  CB  . TYR   O  1  82  ? 10.722  -209.285 39.688  1.00 90.16  ? 82  TYR   O CB  1 
ATOM   25226 C  CG  . TYR   O  1  82  ? 9.442   -208.532 39.953  1.00 88.40  ? 82  TYR   O CG  1 
ATOM   25227 C  CD1 . TYR   O  1  82  ? 8.651   -208.080 38.911  1.00 88.23  ? 82  TYR   O CD1 1 
ATOM   25228 C  CD2 . TYR   O  1  82  ? 9.012   -208.280 41.246  1.00 88.11  ? 82  TYR   O CD2 1 
ATOM   25229 C  CE1 . TYR   O  1  82  ? 7.468   -207.397 39.144  1.00 88.67  ? 82  TYR   O CE1 1 
ATOM   25230 C  CE2 . TYR   O  1  82  ? 7.833   -207.597 41.498  1.00 87.47  ? 82  TYR   O CE2 1 
ATOM   25231 C  CZ  . TYR   O  1  82  ? 7.058   -207.151 40.443  1.00 87.88  ? 82  TYR   O CZ  1 
ATOM   25232 O  OH  . TYR   O  1  82  ? 5.897   -206.477 40.692  1.00 87.83  ? 82  TYR   O OH  1 
ATOM   25233 N  N   . ARG   O  1  83  ? 12.537  -207.151 41.110  1.00 95.49  ? 83  ARG   O N   1 
ATOM   25234 C  CA  . ARG   O  1  83  ? 12.636  -205.986 42.034  1.00 95.44  ? 83  ARG   O CA  1 
ATOM   25235 C  C   . ARG   O  1  83  ? 13.363  -204.818 41.350  1.00 96.94  ? 83  ARG   O C   1 
ATOM   25236 O  O   . ARG   O  1  83  ? 12.841  -203.684 41.429  1.00 95.33  ? 83  ARG   O O   1 
ATOM   25237 C  CB  . ARG   O  1  83  ? 13.350  -206.369 43.335  1.00 98.72  ? 83  ARG   O CB  1 
ATOM   25238 C  CG  . ARG   O  1  83  ? 13.211  -205.325 44.434  1.00 98.18  ? 83  ARG   O CG  1 
ATOM   25239 C  CD  . ARG   O  1  83  ? 13.900  -205.713 45.728  1.00 100.80 ? 83  ARG   O CD  1 
ATOM   25240 N  NE  . ARG   O  1  83  ? 15.318  -205.974 45.521  1.00 101.13 ? 83  ARG   O NE  1 
ATOM   25241 C  CZ  . ARG   O  1  83  ? 15.920  -207.156 45.637  1.00 103.19 ? 83  ARG   O CZ  1 
ATOM   25242 N  NH1 . ARG   O  1  83  ? 15.240  -208.235 45.989  1.00 104.74 ? 83  ARG   O NH1 1 
ATOM   25243 N  NH2 . ARG   O  1  83  ? 17.219  -207.253 45.411  1.00 105.11 ? 83  ARG   O NH2 1 
ATOM   25244 N  N   . VAL   O  1  84  ? 14.517  -205.074 40.720  1.00 93.79  ? 84  VAL   O N   1 
ATOM   25245 C  CA  . VAL   O  1  84  ? 15.341  -204.026 40.041  1.00 93.93  ? 84  VAL   O CA  1 
ATOM   25246 C  C   . VAL   O  1  84  ? 14.637  -203.577 38.752  1.00 96.75  ? 84  VAL   O C   1 
ATOM   25247 O  O   . VAL   O  1  84  ? 14.795  -202.397 38.384  1.00 98.64  ? 84  VAL   O O   1 
ATOM   25248 C  CB  . VAL   O  1  84  ? 16.790  -204.479 39.763  1.00 93.24  ? 84  VAL   O CB  1 
ATOM   25249 C  CG1 . VAL   O  1  84  ? 17.517  -204.851 41.044  1.00 92.92  ? 84  VAL   O CG1 1 
ATOM   25250 C  CG2 . VAL   O  1  84  ? 16.877  -205.608 38.747  1.00 94.13  ? 84  VAL   O CG2 1 
ATOM   25251 N  N   . LEU   O  1  85  ? 13.904  -204.474 38.084  1.00 96.46  ? 85  LEU   O N   1 
ATOM   25252 C  CA  . LEU   O  1  85  ? 13.111  -204.132 36.870  1.00 97.52  ? 85  LEU   O CA  1 
ATOM   25253 C  C   . LEU   O  1  85  ? 11.992  -203.152 37.245  1.00 96.33  ? 85  LEU   O C   1 
ATOM   25254 O  O   . LEU   O  1  85  ? 11.697  -202.275 36.417  1.00 96.40  ? 85  LEU   O O   1 
ATOM   25255 C  CB  . LEU   O  1  85  ? 12.541  -205.400 36.222  1.00 99.21  ? 85  LEU   O CB  1 
ATOM   25256 C  CG  . LEU   O  1  85  ? 13.396  -206.020 35.116  1.00 99.74  ? 85  LEU   O CG  1 
ATOM   25257 C  CD1 . LEU   O  1  85  ? 12.806  -207.344 34.659  1.00 99.72  ? 85  LEU   O CD1 1 
ATOM   25258 C  CD2 . LEU   O  1  85  ? 13.541  -205.072 33.933  1.00 101.19 ? 85  LEU   O CD2 1 
ATOM   25259 N  N   . VAL   O  1  86  ? 11.400  -203.293 38.436  1.00 95.46  ? 86  VAL   O N   1 
ATOM   25260 C  CA  . VAL   O  1  86  ? 10.319  -202.392 38.940  1.00 98.18  ? 86  VAL   O CA  1 
ATOM   25261 C  C   . VAL   O  1  86  ? 10.918  -201.002 39.206  1.00 100.11 ? 86  VAL   O C   1 
ATOM   25262 O  O   . VAL   O  1  86  ? 10.290  -200.001 38.796  1.00 98.43  ? 86  VAL   O O   1 
ATOM   25263 C  CB  . VAL   O  1  86  ? 9.622   -202.966 40.191  1.00 97.50  ? 86  VAL   O CB  1 
ATOM   25264 C  CG1 . VAL   O  1  86  ? 8.663   -201.967 40.819  1.00 100.19 ? 86  VAL   O CG1 1 
ATOM   25265 C  CG2 . VAL   O  1  86  ? 8.889   -204.261 39.882  1.00 97.30  ? 86  VAL   O CG2 1 
ATOM   25266 N  N   . ASP   O  1  87  ? 12.079  -200.944 39.870  1.00 102.51 ? 87  ASP   O N   1 
ATOM   25267 C  CA  . ASP   O  1  87  ? 12.828  -199.686 40.149  1.00 101.94 ? 87  ASP   O CA  1 
ATOM   25268 C  C   . ASP   O  1  87  ? 13.080  -198.951 38.824  1.00 102.74 ? 87  ASP   O C   1 
ATOM   25269 O  O   . ASP   O  1  87  ? 12.733  -197.752 38.735  1.00 102.34 ? 87  ASP   O O   1 
ATOM   25270 C  CB  . ASP   O  1  87  ? 14.139  -199.963 40.894  1.00 102.15 ? 87  ASP   O CB  1 
ATOM   25271 C  CG  . ASP   O  1  87  ? 13.965  -200.485 42.314  1.00 102.44 ? 87  ASP   O CG  1 
ATOM   25272 O  OD1 . ASP   O  1  87  ? 12.988  -200.080 42.977  1.00 102.19 ? 87  ASP   O OD1 1 
ATOM   25273 O  OD2 . ASP   O  1  87  ? 14.813  -201.292 42.751  1.00 102.31 ? 87  ASP   O OD2 1 
ATOM   25274 N  N   . LYS   O  1  88  ? 13.646  -199.655 37.835  1.00 100.57 ? 88  LYS   O N   1 
ATOM   25275 C  CA  . LYS   O  1  88  ? 13.995  -199.120 36.489  1.00 96.37  ? 88  LYS   O CA  1 
ATOM   25276 C  C   . LYS   O  1  88  ? 12.725  -198.718 35.729  1.00 95.50  ? 88  LYS   O C   1 
ATOM   25277 O  O   . LYS   O  1  88  ? 12.762  -197.680 35.038  1.00 94.00  ? 88  LYS   O O   1 
ATOM   25278 C  CB  . LYS   O  1  88  ? 14.776  -200.157 35.675  1.00 95.96  ? 88  LYS   O CB  1 
ATOM   25279 C  CG  . LYS   O  1  88  ? 16.213  -200.389 36.121  1.00 96.73  ? 88  LYS   O CG  1 
ATOM   25280 C  CD  . LYS   O  1  88  ? 16.814  -201.655 35.549  1.00 99.17  ? 88  LYS   O CD  1 
ATOM   25281 C  CE  . LYS   O  1  88  ? 18.109  -202.064 36.219  1.00 100.81 ? 88  LYS   O CE  1 
ATOM   25282 N  NZ  . LYS   O  1  88  ? 19.245  -201.222 35.775  1.00 102.93 ? 88  LYS   O NZ  1 
ATOM   25283 N  N   . SER   O  1  89  ? 11.661  -199.522 35.828  1.00 94.17  ? 89  SER   O N   1 
ATOM   25284 C  CA  . SER   O  1  89  ? 10.351  -199.283 35.163  1.00 94.54  ? 89  SER   O CA  1 
ATOM   25285 C  C   . SER   O  1  89  ? 9.701   -198.008 35.708  1.00 95.65  ? 89  SER   O C   1 
ATOM   25286 O  O   . SER   O  1  89  ? 9.179   -197.222 34.895  1.00 98.07  ? 89  SER   O O   1 
ATOM   25287 C  CB  . SER   O  1  89  ? 9.425   -200.456 35.320  1.00 94.98  ? 89  SER   O CB  1 
ATOM   25288 O  OG  . SER   O  1  89  ? 9.900   -201.567 34.577  1.00 96.79  ? 89  SER   O OG  1 
ATOM   25289 N  N   . ARG   O  1  90  ? 9.709   -197.824 37.031  1.00 94.89  ? 90  ARG   O N   1 
ATOM   25290 C  CA  . ARG   O  1  90  ? 9.114   -196.638 37.705  1.00 94.91  ? 90  ARG   O CA  1 
ATOM   25291 C  C   . ARG   O  1  90  ? 9.845   -195.366 37.256  1.00 91.26  ? 90  ARG   O C   1 
ATOM   25292 O  O   . ARG   O  1  90  ? 9.159   -194.358 36.997  1.00 88.02  ? 90  ARG   O O   1 
ATOM   25293 C  CB  . ARG   O  1  90  ? 9.168   -196.796 39.227  1.00 96.28  ? 90  ARG   O CB  1 
ATOM   25294 C  CG  . ARG   O  1  90  ? 8.135   -197.764 39.783  1.00 96.69  ? 90  ARG   O CG  1 
ATOM   25295 C  CD  . ARG   O  1  90  ? 8.457   -198.161 41.208  1.00 95.69  ? 90  ARG   O CD  1 
ATOM   25296 N  NE  . ARG   O  1  90  ? 7.390   -198.937 41.820  1.00 93.02  ? 90  ARG   O NE  1 
ATOM   25297 C  CZ  . ARG   O  1  90  ? 7.462   -199.512 43.015  1.00 92.19  ? 90  ARG   O CZ  1 
ATOM   25298 N  NH1 . ARG   O  1  90  ? 8.563   -199.409 43.743  1.00 91.02  ? 90  ARG   O NH1 1 
ATOM   25299 N  NH2 . ARG   O  1  90  ? 6.429   -200.197 43.477  1.00 94.40  ? 90  ARG   O NH2 1 
ATOM   25300 N  N   . LYS   O  1  91  ? 11.178  -195.420 37.164  1.00 92.28  ? 91  LYS   O N   1 
ATOM   25301 C  CA  . LYS   O  1  91  ? 12.039  -194.258 36.819  1.00 92.91  ? 91  LYS   O CA  1 
ATOM   25302 C  C   . LYS   O  1  91  ? 11.827  -193.863 35.354  1.00 95.68  ? 91  LYS   O C   1 
ATOM   25303 O  O   . LYS   O  1  91  ? 11.763  -192.651 35.080  1.00 97.95  ? 91  LYS   O O   1 
ATOM   25304 C  CB  . LYS   O  1  91  ? 13.519  -194.565 37.061  1.00 94.75  ? 91  LYS   O CB  1 
ATOM   25305 C  CG  . LYS   O  1  91  ? 14.424  -193.342 37.023  1.00 95.85  ? 91  LYS   O CG  1 
ATOM   25306 C  CD  . LYS   O  1  91  ? 15.890  -193.663 37.156  1.00 99.71  ? 91  LYS   O CD  1 
ATOM   25307 C  CE  . LYS   O  1  91  ? 16.743  -192.421 37.287  1.00 103.05 ? 91  LYS   O CE  1 
ATOM   25308 N  NZ  . LYS   O  1  91  ? 18.162  -192.759 37.547  1.00 106.67 ? 91  LYS   O NZ  1 
ATOM   25309 N  N   . VAL   O  1  92  ? 11.737  -194.839 34.447  1.00 94.85  ? 92  VAL   O N   1 
ATOM   25310 C  CA  . VAL   O  1  92  ? 11.648  -194.590 32.976  1.00 95.38  ? 92  VAL   O CA  1 
ATOM   25311 C  C   . VAL   O  1  92  ? 10.271  -193.993 32.646  1.00 95.01  ? 92  VAL   O C   1 
ATOM   25312 O  O   . VAL   O  1  92  ? 10.189  -193.235 31.662  1.00 95.33  ? 92  VAL   O O   1 
ATOM   25313 C  CB  . VAL   O  1  92  ? 11.956  -195.860 32.156  1.00 95.08  ? 92  VAL   O CB  1 
ATOM   25314 C  CG1 . VAL   O  1  92  ? 10.800  -196.847 32.148  1.00 96.65  ? 92  VAL   O CG1 1 
ATOM   25315 C  CG2 . VAL   O  1  92  ? 12.373  -195.524 30.733  1.00 94.17  ? 92  VAL   O CG2 1 
ATOM   25316 N  N   . ALA   O  1  93  ? 9.239   -194.293 33.445  1.00 93.13  ? 93  ALA   O N   1 
ATOM   25317 C  CA  . ALA   O  1  93  ? 7.881   -193.712 33.315  1.00 95.05  ? 93  ALA   O CA  1 
ATOM   25318 C  C   . ALA   O  1  93  ? 7.940   -192.202 33.573  1.00 97.69  ? 93  ALA   O C   1 
ATOM   25319 O  O   . ALA   O  1  93  ? 7.069   -191.487 33.043  1.00 105.26 ? 93  ALA   O O   1 
ATOM   25320 C  CB  . ALA   O  1  93  ? 6.916   -194.384 34.260  1.00 94.29  ? 93  ALA   O CB  1 
ATOM   25321 N  N   . HIS   O  1  94  ? 8.922   -191.747 34.362  1.00 96.38  ? 94  HIS   O N   1 
ATOM   25322 C  CA  . HIS   O  1  94  ? 9.168   -190.316 34.687  1.00 95.94  ? 94  HIS   O CA  1 
ATOM   25323 C  C   . HIS   O  1  94  ? 10.105  -189.692 33.647  1.00 95.29  ? 94  HIS   O C   1 
ATOM   25324 O  O   . HIS   O  1  94  ? 9.668   -188.745 32.967  1.00 98.50  ? 94  HIS   O O   1 
ATOM   25325 C  CB  . HIS   O  1  94  ? 9.716   -190.162 36.113  1.00 93.67  ? 94  HIS   O CB  1 
ATOM   25326 C  CG  . HIS   O  1  94  ? 8.656   -190.185 37.161  1.00 95.68  ? 94  HIS   O CG  1 
ATOM   25327 N  ND1 . HIS   O  1  94  ? 8.117   -191.360 37.636  1.00 96.34  ? 94  HIS   O ND1 1 
ATOM   25328 C  CD2 . HIS   O  1  94  ? 8.028   -189.187 37.820  1.00 97.94  ? 94  HIS   O CD2 1 
ATOM   25329 C  CE1 . HIS   O  1  94  ? 7.205   -191.087 38.546  1.00 98.28  ? 94  HIS   O CE1 1 
ATOM   25330 N  NE2 . HIS   O  1  94  ? 7.130   -189.762 38.677  1.00 98.07  ? 94  HIS   O NE2 1 
ATOM   25331 N  N   . THR   O  1  95  ? 11.333  -190.208 33.526  1.00 93.42  ? 95  THR   O N   1 
ATOM   25332 C  CA  . THR   O  1  95  ? 12.438  -189.588 32.742  1.00 94.66  ? 95  THR   O CA  1 
ATOM   25333 C  C   . THR   O  1  95  ? 12.049  -189.475 31.265  1.00 96.01  ? 95  THR   O C   1 
ATOM   25334 O  O   . THR   O  1  95  ? 12.235  -188.383 30.691  1.00 99.16  ? 95  THR   O O   1 
ATOM   25335 C  CB  . THR   O  1  95  ? 13.752  -190.368 32.867  1.00 95.78  ? 95  THR   O CB  1 
ATOM   25336 O  OG1 . THR   O  1  95  ? 13.528  -191.698 32.393  1.00 97.20  ? 95  THR   O OG1 1 
ATOM   25337 C  CG2 . THR   O  1  95  ? 14.288  -190.393 34.281  1.00 97.46  ? 95  THR   O CG2 1 
ATOM   25338 N  N   . SER   O  1  96  ? 11.539  -190.557 30.674  1.00 94.85  ? 96  SER   O N   1 
ATOM   25339 C  CA  . SER   O  1  96  ? 11.282  -190.659 29.214  1.00 96.22  ? 96  SER   O CA  1 
ATOM   25340 C  C   . SER   O  1  96  ? 9.830   -190.305 28.863  1.00 92.90  ? 96  SER   O C   1 
ATOM   25341 O  O   . SER   O  1  96  ? 9.499   -190.405 27.667  1.00 91.34  ? 96  SER   O O   1 
ATOM   25342 C  CB  . SER   O  1  96  ? 11.639  -192.025 28.710  1.00 96.43  ? 96  SER   O CB  1 
ATOM   25343 O  OG  . SER   O  1  96  ? 10.674  -192.975 29.123  1.00 103.49 ? 96  SER   O OG  1 
ATOM   25344 N  N   . TYR   O  1  97  ? 8.994   -189.900 29.829  1.00 93.89  ? 97  TYR   O N   1 
ATOM   25345 C  CA  . TYR   O  1  97  ? 7.579   -189.529 29.552  1.00 93.92  ? 97  TYR   O CA  1 
ATOM   25346 C  C   . TYR   O  1  97  ? 7.087   -188.379 30.443  1.00 94.51  ? 97  TYR   O C   1 
ATOM   25347 O  O   . TYR   O  1  97  ? 6.837   -187.303 29.874  1.00 96.02  ? 97  TYR   O O   1 
ATOM   25348 C  CB  . TYR   O  1  97  ? 6.663   -190.750 29.642  1.00 94.96  ? 97  TYR   O CB  1 
ATOM   25349 C  CG  . TYR   O  1  97  ? 5.425   -190.608 28.797  1.00 96.92  ? 97  TYR   O CG  1 
ATOM   25350 C  CD1 . TYR   O  1  97  ? 4.280   -190.016 29.304  1.00 99.51  ? 97  TYR   O CD1 1 
ATOM   25351 C  CD2 . TYR   O  1  97  ? 5.410   -191.019 27.474  1.00 98.48  ? 97  TYR   O CD2 1 
ATOM   25352 C  CE1 . TYR   O  1  97  ? 3.142   -189.859 28.527  1.00 100.96 ? 97  TYR   O CE1 1 
ATOM   25353 C  CE2 . TYR   O  1  97  ? 4.280   -190.872 26.683  1.00 100.17 ? 97  TYR   O CE2 1 
ATOM   25354 C  CZ  . TYR   O  1  97  ? 3.140   -190.290 27.212  1.00 100.75 ? 97  TYR   O CZ  1 
ATOM   25355 O  OH  . TYR   O  1  97  ? 2.022   -190.137 26.444  1.00 101.73 ? 97  TYR   O OH  1 
ATOM   25356 N  N   . LYS   O  1  98  ? 6.907   -188.581 31.755  1.00 94.17  ? 98  LYS   O N   1 
ATOM   25357 C  CA  . LYS   O  1  98  ? 6.213   -187.591 32.631  1.00 95.82  ? 98  LYS   O CA  1 
ATOM   25358 C  C   . LYS   O  1  98  ? 6.968   -186.254 32.624  1.00 94.47  ? 98  LYS   O C   1 
ATOM   25359 O  O   . LYS   O  1  98  ? 6.298   -185.206 32.530  1.00 91.18  ? 98  LYS   O O   1 
ATOM   25360 C  CB  . LYS   O  1  98  ? 6.039   -188.078 34.074  1.00 97.84  ? 98  LYS   O CB  1 
ATOM   25361 C  CG  . LYS   O  1  98  ? 4.991   -187.290 34.852  1.00 100.69 ? 98  LYS   O CG  1 
ATOM   25362 C  CD  . LYS   O  1  98  ? 4.854   -187.653 36.312  1.00 103.37 ? 98  LYS   O CD  1 
ATOM   25363 C  CE  . LYS   O  1  98  ? 3.701   -186.926 36.975  1.00 105.01 ? 98  LYS   O CE  1 
ATOM   25364 N  NZ  . LYS   O  1  98  ? 4.103   -186.302 38.258  1.00 105.60 ? 98  LYS   O NZ  1 
ATOM   25365 N  N   . ARG   O  1  99  ? 8.303   -186.290 32.708  1.00 93.19  ? 99  ARG   O N   1 
ATOM   25366 C  CA  . ARG   O  1  99  ? 9.174   -185.082 32.726  1.00 92.99  ? 99  ARG   O CA  1 
ATOM   25367 C  C   . ARG   O  1  99  ? 9.129   -184.366 31.365  1.00 93.19  ? 99  ARG   O C   1 
ATOM   25368 O  O   . ARG   O  1  99  ? 9.631   -183.225 31.296  1.00 90.65  ? 99  ARG   O O   1 
ATOM   25369 C  CB  . ARG   O  1  99  ? 10.606  -185.456 33.126  1.00 93.86  ? 99  ARG   O CB  1 
ATOM   25370 C  CG  . ARG   O  1  99  ? 10.761  -185.792 34.603  1.00 94.05  ? 99  ARG   O CG  1 
ATOM   25371 C  CD  . ARG   O  1  99  ? 12.178  -186.163 35.001  1.00 95.69  ? 99  ARG   O CD  1 
ATOM   25372 N  NE  . ARG   O  1  99  ? 12.217  -186.747 36.335  1.00 96.79  ? 99  ARG   O NE  1 
ATOM   25373 C  CZ  . ARG   O  1  99  ? 13.322  -187.094 36.991  1.00 99.00  ? 99  ARG   O CZ  1 
ATOM   25374 N  NH1 . ARG   O  1  99  ? 14.514  -186.912 36.446  1.00 99.61  ? 99  ARG   O NH1 1 
ATOM   25375 N  NH2 . ARG   O  1  99  ? 13.228  -187.623 38.199  1.00 101.29 ? 99  ARG   O NH2 1 
ATOM   25376 N  N   . ILE   O  1  100 ? 8.551   -184.993 30.330  1.00 92.90  ? 100 ILE   O N   1 
ATOM   25377 C  CA  . ILE   O  1  100 ? 8.416   -184.410 28.959  1.00 92.82  ? 100 ILE   O CA  1 
ATOM   25378 C  C   . ILE   O  1  100 ? 6.975   -183.931 28.718  1.00 92.79  ? 100 ILE   O C   1 
ATOM   25379 O  O   . ILE   O  1  100 ? 6.827   -182.805 28.213  1.00 95.26  ? 100 ILE   O O   1 
ATOM   25380 C  CB  . ILE   O  1  100 ? 8.875   -185.410 27.877  1.00 92.02  ? 100 ILE   O CB  1 
ATOM   25381 C  CG1 . ILE   O  1  100 ? 10.354  -185.772 28.037  1.00 94.21  ? 100 ILE   O CG1 1 
ATOM   25382 C  CG2 . ILE   O  1  100 ? 8.585   -184.869 26.486  1.00 92.44  ? 100 ILE   O CG2 1 
ATOM   25383 C  CD1 . ILE   O  1  100 ? 10.780  -186.986 27.243  1.00 97.38  ? 100 ILE   O CD1 1 
ATOM   25384 N  N   . TYR   O  1  101 ? 5.959   -184.746 29.027  1.00 91.75  ? 101 TYR   O N   1 
ATOM   25385 C  CA  . TYR   O  1  101 ? 4.542   -184.505 28.627  1.00 92.09  ? 101 TYR   O CA  1 
ATOM   25386 C  C   . TYR   O  1  101 ? 3.663   -184.092 29.816  1.00 92.70  ? 101 TYR   O C   1 
ATOM   25387 O  O   . TYR   O  1  101 ? 2.487   -183.746 29.573  1.00 89.08  ? 101 TYR   O O   1 
ATOM   25388 C  CB  . TYR   O  1  101 ? 3.953   -185.747 27.955  1.00 91.10  ? 101 TYR   O CB  1 
ATOM   25389 C  CG  . TYR   O  1  101 ? 4.667   -186.160 26.695  1.00 89.17  ? 101 TYR   O CG  1 
ATOM   25390 C  CD1 . TYR   O  1  101 ? 4.577   -185.394 25.544  1.00 89.21  ? 101 TYR   O CD1 1 
ATOM   25391 C  CD2 . TYR   O  1  101 ? 5.441   -187.306 26.652  1.00 87.56  ? 101 TYR   O CD2 1 
ATOM   25392 C  CE1 . TYR   O  1  101 ? 5.236   -185.757 24.381  1.00 87.61  ? 101 TYR   O CE1 1 
ATOM   25393 C  CE2 . TYR   O  1  101 ? 6.107   -187.684 25.498  1.00 87.13  ? 101 TYR   O CE2 1 
ATOM   25394 C  CZ  . TYR   O  1  101 ? 6.004   -186.905 24.359  1.00 87.08  ? 101 TYR   O CZ  1 
ATOM   25395 O  OH  . TYR   O  1  101 ? 6.652   -187.256 23.211  1.00 87.68  ? 101 TYR   O OH  1 
ATOM   25396 N  N   . GLY   O  1  102 ? 4.190   -184.135 31.044  1.00 94.25  ? 102 GLY   O N   1 
ATOM   25397 C  CA  . GLY   O  1  102 ? 3.463   -183.726 32.263  1.00 99.30  ? 102 GLY   O CA  1 
ATOM   25398 C  C   . GLY   O  1  102 ? 2.286   -184.640 32.573  1.00 101.16 ? 102 GLY   O C   1 
ATOM   25399 O  O   . GLY   O  1  102 ? 1.354   -184.184 33.259  1.00 106.68 ? 102 GLY   O O   1 
ATOM   25400 N  N   . GLU   O  1  103 ? 2.320   -185.883 32.087  1.00 101.25 ? 103 GLU   O N   1 
ATOM   25401 C  CA  . GLU   O  1  103 ? 1.293   -186.923 32.367  1.00 102.71 ? 103 GLU   O CA  1 
ATOM   25402 C  C   . GLU   O  1  103 ? 1.960   -188.300 32.290  1.00 100.07 ? 103 GLU   O C   1 
ATOM   25403 O  O   . GLU   O  1  103 ? 3.063   -188.390 31.718  1.00 98.87  ? 103 GLU   O O   1 
ATOM   25404 C  CB  . GLU   O  1  103 ? 0.114   -186.799 31.399  1.00 106.79 ? 103 GLU   O CB  1 
ATOM   25405 C  CG  . GLU   O  1  103 ? 0.478   -187.058 29.946  1.00 110.49 ? 103 GLU   O CG  1 
ATOM   25406 C  CD  . GLU   O  1  103 ? -0.477  -186.450 28.931  1.00 118.26 ? 103 GLU   O CD  1 
ATOM   25407 O  OE1 . GLU   O  1  103 ? -0.515  -185.204 28.823  1.00 120.24 ? 103 GLU   O OE1 1 
ATOM   25408 O  OE2 . GLU   O  1  103 ? -1.183  -187.222 28.250  1.00 122.83 ? 103 GLU   O OE2 1 
ATOM   25409 N  N   . TYR   O  1  104 ? 1.317   -189.324 32.855  1.00 98.66  ? 104 TYR   O N   1 
ATOM   25410 C  CA  . TYR   O  1  104 ? 1.865   -190.700 32.943  1.00 97.68  ? 104 TYR   O CA  1 
ATOM   25411 C  C   . TYR   O  1  104 ? 1.727   -191.386 31.590  1.00 93.33  ? 104 TYR   O C   1 
ATOM   25412 O  O   . TYR   O  1  104 ? 0.782   -191.126 30.851  1.00 91.33  ? 104 TYR   O O   1 
ATOM   25413 C  CB  . TYR   O  1  104 ? 1.182   -191.485 34.064  1.00 99.89  ? 104 TYR   O CB  1 
ATOM   25414 C  CG  . TYR   O  1  104 ? 1.573   -191.017 35.441  1.00 101.05 ? 104 TYR   O CG  1 
ATOM   25415 C  CD1 . TYR   O  1  104 ? 2.791   -191.376 35.997  1.00 98.01  ? 104 TYR   O CD1 1 
ATOM   25416 C  CD2 . TYR   O  1  104 ? 0.741   -190.189 36.176  1.00 103.36 ? 104 TYR   O CD2 1 
ATOM   25417 C  CE1 . TYR   O  1  104 ? 3.166   -190.938 37.256  1.00 98.93  ? 104 TYR   O CE1 1 
ATOM   25418 C  CE2 . TYR   O  1  104 ? 1.099   -189.743 37.438  1.00 104.26 ? 104 TYR   O CE2 1 
ATOM   25419 C  CZ  . TYR   O  1  104 ? 2.316   -190.120 37.981  1.00 102.04 ? 104 TYR   O CZ  1 
ATOM   25420 O  OH  . TYR   O  1  104 ? 2.676   -189.681 39.222  1.00 101.04 ? 104 TYR   O OH  1 
ATOM   25421 N  N   . PRO   O  1  105 ? 2.665   -192.293 31.237  1.00 95.96  ? 105 PRO   O N   1 
ATOM   25422 C  CA  . PRO   O  1  105 ? 2.633   -192.977 29.946  1.00 96.05  ? 105 PRO   O CA  1 
ATOM   25423 C  C   . PRO   O  1  105 ? 1.451   -193.935 29.858  1.00 97.26  ? 105 PRO   O C   1 
ATOM   25424 O  O   . PRO   O  1  105 ? 1.025   -194.481 30.874  1.00 97.04  ? 105 PRO   O O   1 
ATOM   25425 C  CB  . PRO   O  1  105 ? 3.959   -193.752 29.921  1.00 94.65  ? 105 PRO   O CB  1 
ATOM   25426 C  CG  . PRO   O  1  105 ? 4.252   -194.005 31.385  1.00 96.33  ? 105 PRO   O CG  1 
ATOM   25427 C  CD  . PRO   O  1  105 ? 3.782   -192.745 32.082  1.00 96.47  ? 105 PRO   O CD  1 
ATOM   25428 N  N   . PRO   O  1  106 ? 0.882   -194.162 28.653  1.00 100.30 ? 106 PRO   O N   1 
ATOM   25429 C  CA  . PRO   O  1  106 ? -0.105  -195.225 28.466  1.00 101.44 ? 106 PRO   O CA  1 
ATOM   25430 C  C   . PRO   O  1  106 ? 0.570   -196.596 28.620  1.00 101.34 ? 106 PRO   O C   1 
ATOM   25431 O  O   . PRO   O  1  106 ? 1.758   -196.691 28.356  1.00 100.18 ? 106 PRO   O O   1 
ATOM   25432 C  CB  . PRO   O  1  106 ? -0.635  -194.996 27.044  1.00 104.30 ? 106 PRO   O CB  1 
ATOM   25433 C  CG  . PRO   O  1  106 ? 0.489   -194.262 26.340  1.00 105.02 ? 106 PRO   O CG  1 
ATOM   25434 C  CD  . PRO   O  1  106 ? 1.150   -193.419 27.412  1.00 102.50 ? 106 PRO   O CD  1 
ATOM   25435 N  N   . THR   O  1  107 ? -0.197  -197.606 29.043  1.00 101.39 ? 107 THR   O N   1 
ATOM   25436 C  CA  . THR   O  1  107 ? 0.289   -198.967 29.400  1.00 99.42  ? 107 THR   O CA  1 
ATOM   25437 C  C   . THR   O  1  107 ? 1.234   -199.508 28.316  1.00 97.60  ? 107 THR   O C   1 
ATOM   25438 O  O   . THR   O  1  107 ? 2.359   -199.911 28.669  1.00 92.28  ? 107 THR   O O   1 
ATOM   25439 C  CB  . THR   O  1  107 ? -0.882  -199.930 29.632  1.00 99.65  ? 107 THR   O CB  1 
ATOM   25440 O  OG1 . THR   O  1  107 ? -1.763  -199.346 30.593  1.00 99.07  ? 107 THR   O OG1 1 
ATOM   25441 C  CG2 . THR   O  1  107 ? -0.418  -201.295 30.094  1.00 100.35 ? 107 THR   O CG2 1 
ATOM   25442 N  N   . LYS   O  1  108 ? 0.797   -199.510 27.052  1.00 98.44  ? 108 LYS   O N   1 
ATOM   25443 C  CA  . LYS   O  1  108 ? 1.530   -200.125 25.909  1.00 100.95 ? 108 LYS   O CA  1 
ATOM   25444 C  C   . LYS   O  1  108 ? 2.943   -199.532 25.793  1.00 99.76  ? 108 LYS   O C   1 
ATOM   25445 O  O   . LYS   O  1  108 ? 3.863   -200.295 25.435  1.00 94.21  ? 108 LYS   O O   1 
ATOM   25446 C  CB  . LYS   O  1  108 ? 0.751   -199.942 24.601  1.00 105.44 ? 108 LYS   O CB  1 
ATOM   25447 C  CG  . LYS   O  1  108 ? 0.650   -198.506 24.103  1.00 108.53 ? 108 LYS   O CG  1 
ATOM   25448 C  CD  . LYS   O  1  108 ? -0.287  -198.343 22.928  1.00 112.75 ? 108 LYS   O CD  1 
ATOM   25449 C  CE  . LYS   O  1  108 ? -0.673  -196.902 22.670  1.00 114.73 ? 108 LYS   O CE  1 
ATOM   25450 N  NZ  . LYS   O  1  108 ? -1.435  -196.760 21.407  1.00 114.13 ? 108 LYS   O NZ  1 
ATOM   25451 N  N   . LEU   O  1  109 ? 3.113   -198.235 26.078  1.00 100.22 ? 109 LEU   O N   1 
ATOM   25452 C  CA  . LEU   O  1  109 ? 4.414   -197.523 25.927  1.00 100.98 ? 109 LEU   O CA  1 
ATOM   25453 C  C   . LEU   O  1  109 ? 5.330   -197.829 27.116  1.00 99.34  ? 109 LEU   O C   1 
ATOM   25454 O  O   . LEU   O  1  109 ? 6.520   -198.104 26.865  1.00 97.43  ? 109 LEU   O O   1 
ATOM   25455 C  CB  . LEU   O  1  109 ? 4.187   -196.015 25.780  1.00 103.22 ? 109 LEU   O CB  1 
ATOM   25456 C  CG  . LEU   O  1  109 ? 3.697   -195.554 24.408  1.00 107.76 ? 109 LEU   O CG  1 
ATOM   25457 C  CD1 . LEU   O  1  109 ? 3.577   -194.039 24.360  1.00 110.24 ? 109 LEU   O CD1 1 
ATOM   25458 C  CD2 . LEU   O  1  109 ? 4.614   -196.041 23.294  1.00 110.83 ? 109 LEU   O CD2 1 
ATOM   25459 N  N   . LEU   O  1  110 ? 4.822   -197.774 28.353  1.00 97.11  ? 110 LEU   O N   1 
ATOM   25460 C  CA  . LEU   O  1  110 ? 5.619   -198.163 29.548  1.00 97.64  ? 110 LEU   O CA  1 
ATOM   25461 C  C   . LEU   O  1  110 ? 6.090   -199.606 29.341  1.00 97.76  ? 110 LEU   O C   1 
ATOM   25462 O  O   . LEU   O  1  110 ? 7.302   -199.854 29.494  1.00 100.61 ? 110 LEU   O O   1 
ATOM   25463 C  CB  . LEU   O  1  110 ? 4.801   -198.016 30.837  1.00 93.48  ? 110 LEU   O CB  1 
ATOM   25464 C  CG  . LEU   O  1  110 ? 5.527   -198.440 32.116  1.00 93.36  ? 110 LEU   O CG  1 
ATOM   25465 C  CD1 . LEU   O  1  110 ? 6.841   -197.690 32.284  1.00 92.17  ? 110 LEU   O CD1 1 
ATOM   25466 C  CD2 . LEU   O  1  110 ? 4.649   -198.247 33.341  1.00 93.82  ? 110 LEU   O CD2 1 
ATOM   25467 N  N   . VAL   O  1  111 ? 5.167   -200.499 28.961  1.00 101.19 ? 111 VAL   O N   1 
ATOM   25468 C  CA  . VAL   O  1  111 ? 5.447   -201.928 28.623  1.00 100.72 ? 111 VAL   O CA  1 
ATOM   25469 C  C   . VAL   O  1  111 ? 6.579   -201.977 27.588  1.00 97.18  ? 111 VAL   O C   1 
ATOM   25470 O  O   . VAL   O  1  111 ? 7.514   -202.778 27.777  1.00 96.89  ? 111 VAL   O O   1 
ATOM   25471 C  CB  . VAL   O  1  111 ? 4.181   -202.656 28.123  1.00 104.40 ? 111 VAL   O CB  1 
ATOM   25472 C  CG1 . VAL   O  1  111 ? 4.509   -203.958 27.406  1.00 104.01 ? 111 VAL   O CG1 1 
ATOM   25473 C  CG2 . VAL   O  1  111 ? 3.197   -202.915 29.257  1.00 106.71 ? 111 VAL   O CG2 1 
ATOM   25474 N  N   . SER   O  1  112 ? 6.496   -201.145 26.545  1.00 94.99  ? 112 SER   O N   1 
ATOM   25475 C  CA  . SER   O  1  112 ? 7.510   -201.034 25.463  1.00 94.35  ? 112 SER   O CA  1 
ATOM   25476 C  C   . SER   O  1  112 ? 8.888   -200.703 26.055  1.00 94.14  ? 112 SER   O C   1 
ATOM   25477 O  O   . SER   O  1  112 ? 9.876   -201.328 25.616  1.00 88.16  ? 112 SER   O O   1 
ATOM   25478 C  CB  . SER   O  1  112 ? 7.097   -200.020 24.427  1.00 94.68  ? 112 SER   O CB  1 
ATOM   25479 O  OG  . SER   O  1  112 ? 8.124   -199.843 23.464  1.00 95.49  ? 112 SER   O OG  1 
ATOM   25480 N  N   . GLU   O  1  113 ? 8.950   -199.763 27.008  1.00 97.03  ? 113 GLU   O N   1 
ATOM   25481 C  CA  . GLU   O  1  113 ? 10.213  -199.282 27.637  1.00 99.19  ? 113 GLU   O CA  1 
ATOM   25482 C  C   . GLU   O  1  113 ? 10.824  -200.393 28.498  1.00 98.39  ? 113 GLU   O C   1 
ATOM   25483 O  O   . GLU   O  1  113 ? 12.066  -200.485 28.528  1.00 103.46 ? 113 GLU   O O   1 
ATOM   25484 C  CB  . GLU   O  1  113 ? 9.981   -198.035 28.495  1.00 101.90 ? 113 GLU   O CB  1 
ATOM   25485 C  CG  . GLU   O  1  113 ? 9.532   -196.809 27.713  1.00 103.67 ? 113 GLU   O CG  1 
ATOM   25486 C  CD  . GLU   O  1  113 ? 10.576  -196.166 26.811  1.00 102.92 ? 113 GLU   O CD  1 
ATOM   25487 O  OE1 . GLU   O  1  113 ? 11.745  -196.604 26.842  1.00 109.16 ? 113 GLU   O OE1 1 
ATOM   25488 O  OE2 . GLU   O  1  113 ? 10.218  -195.221 26.079  1.00 98.59  ? 113 GLU   O OE2 1 
ATOM   25489 N  N   . VAL   O  1  114 ? 9.993   -201.188 29.182  1.00 93.85  ? 114 VAL   O N   1 
ATOM   25490 C  CA  . VAL   O  1  114 ? 10.450  -202.325 30.038  1.00 92.53  ? 114 VAL   O CA  1 
ATOM   25491 C  C   . VAL   O  1  114 ? 11.026  -203.398 29.111  1.00 90.33  ? 114 VAL   O C   1 
ATOM   25492 O  O   . VAL   O  1  114 ? 12.120  -203.914 29.407  1.00 90.30  ? 114 VAL   O O   1 
ATOM   25493 C  CB  . VAL   O  1  114 ? 9.327   -202.902 30.925  1.00 91.97  ? 114 VAL   O CB  1 
ATOM   25494 C  CG1 . VAL   O  1  114 ? 9.869   -203.947 31.888  1.00 92.24  ? 114 VAL   O CG1 1 
ATOM   25495 C  CG2 . VAL   O  1  114 ? 8.587   -201.823 31.699  1.00 92.03  ? 114 VAL   O CG2 1 
ATOM   25496 N  N   . ALA   O  1  115 ? 10.309  -203.699 28.026  1.00 90.84  ? 115 ALA   O N   1 
ATOM   25497 C  CA  . ALA   O  1  115 ? 10.698  -204.676 26.983  1.00 90.62  ? 115 ALA   O CA  1 
ATOM   25498 C  C   . ALA   O  1  115 ? 12.063  -204.298 26.395  1.00 90.91  ? 115 ALA   O C   1 
ATOM   25499 O  O   . ALA   O  1  115 ? 12.854  -205.218 26.114  1.00 86.34  ? 115 ALA   O O   1 
ATOM   25500 C  CB  . ALA   O  1  115 ? 9.634   -204.733 25.915  1.00 91.32  ? 115 ALA   O CB  1 
ATOM   25501 N  N   . LYS   O  1  116 ? 12.324  -202.996 26.221  1.00 91.77  ? 116 LYS   O N   1 
ATOM   25502 C  CA  . LYS   O  1  116 ? 13.611  -202.467 25.694  1.00 92.98  ? 116 LYS   O CA  1 
ATOM   25503 C  C   . LYS   O  1  116 ? 14.739  -202.786 26.680  1.00 92.17  ? 116 LYS   O C   1 
ATOM   25504 O  O   . LYS   O  1  116 ? 15.812  -203.215 26.219  1.00 93.51  ? 116 LYS   O O   1 
ATOM   25505 C  CB  . LYS   O  1  116 ? 13.545  -200.954 25.466  1.00 92.95  ? 116 LYS   O CB  1 
ATOM   25506 C  CG  . LYS   O  1  116 ? 14.769  -200.362 24.780  1.00 96.85  ? 116 LYS   O CG  1 
ATOM   25507 C  CD  . LYS   O  1  116 ? 14.732  -198.856 24.677  1.00 98.78  ? 116 LYS   O CD  1 
ATOM   25508 C  CE  . LYS   O  1  116 ? 15.780  -198.298 23.736  1.00 105.57 ? 116 LYS   O CE  1 
ATOM   25509 N  NZ  . LYS   O  1  116 ? 16.880  -197.628 24.468  1.00 109.53 ? 116 LYS   O NZ  1 
ATOM   25510 N  N   . ILE   O  1  117 ? 14.506  -202.558 27.977  1.00 92.97  ? 117 ILE   O N   1 
ATOM   25511 C  CA  . ILE   O  1  117 ? 15.496  -202.801 29.071  1.00 96.82  ? 117 ILE   O CA  1 
ATOM   25512 C  C   . ILE   O  1  117 ? 15.846  -204.296 29.095  1.00 96.47  ? 117 ILE   O C   1 
ATOM   25513 O  O   . ILE   O  1  117 ? 17.036  -204.624 29.296  1.00 98.03  ? 117 ILE   O O   1 
ATOM   25514 C  CB  . ILE   O  1  117 ? 14.960  -202.303 30.433  1.00 97.15  ? 117 ILE   O CB  1 
ATOM   25515 C  CG1 . ILE   O  1  117 ? 14.868  -200.775 30.474  1.00 97.65  ? 117 ILE   O CG1 1 
ATOM   25516 C  CG2 . ILE   O  1  117 ? 15.798  -202.841 31.586  1.00 98.12  ? 117 ILE   O CG2 1 
ATOM   25517 C  CD1 . ILE   O  1  117 ? 14.142  -200.229 31.682  1.00 98.45  ? 117 ILE   O CD1 1 
ATOM   25518 N  N   . MET   O  1  118 ? 14.849  -205.162 28.893  1.00 95.61  ? 118 MET   O N   1 
ATOM   25519 C  CA  . MET   O  1  118 ? 15.010  -206.639 28.932  1.00 95.11  ? 118 MET   O CA  1 
ATOM   25520 C  C   . MET   O  1  118 ? 15.676  -207.126 27.638  1.00 96.27  ? 118 MET   O C   1 
ATOM   25521 O  O   . MET   O  1  118 ? 16.470  -208.085 27.719  1.00 98.92  ? 118 MET   O O   1 
ATOM   25522 C  CB  . MET   O  1  118 ? 13.659  -207.331 29.139  1.00 97.40  ? 118 MET   O CB  1 
ATOM   25523 C  CG  . MET   O  1  118 ? 13.151  -207.200 30.566  1.00 97.40  ? 118 MET   O CG  1 
ATOM   25524 S  SD  . MET   O  1  118 ? 11.415  -207.671 30.763  1.00 97.46  ? 118 MET   O SD  1 
ATOM   25525 C  CE  . MET   O  1  118 ? 11.579  -209.454 30.879  1.00 99.68  ? 118 MET   O CE  1 
ATOM   25526 N  N   . GLN   O  1  119 ? 15.384  -206.488 26.500  1.00 92.30  ? 119 GLN   O N   1 
ATOM   25527 C  CA  . GLN   O  1  119 ? 16.024  -206.799 25.192  1.00 92.93  ? 119 GLN   O CA  1 
ATOM   25528 C  C   . GLN   O  1  119 ? 17.531  -206.541 25.292  1.00 94.86  ? 119 GLN   O C   1 
ATOM   25529 O  O   . GLN   O  1  119 ? 18.303  -207.353 24.756  1.00 96.03  ? 119 GLN   O O   1 
ATOM   25530 C  CB  . GLN   O  1  119 ? 15.417  -205.969 24.057  1.00 91.99  ? 119 GLN   O CB  1 
ATOM   25531 C  CG  . GLN   O  1  119 ? 15.886  -206.397 22.669  1.00 92.51  ? 119 GLN   O CG  1 
ATOM   25532 C  CD  . GLN   O  1  119 ? 17.249  -205.867 22.286  1.00 92.31  ? 119 GLN   O CD  1 
ATOM   25533 O  OE1 . GLN   O  1  119 ? 17.680  -204.807 22.740  1.00 88.70  ? 119 GLN   O OE1 1 
ATOM   25534 N  NE2 . GLN   O  1  119 ? 17.942  -206.603 21.430  1.00 92.38  ? 119 GLN   O NE2 1 
ATOM   25535 N  N   . GLU   O  1  120 ? 17.933  -205.441 25.933  1.00 98.33  ? 120 GLU   O N   1 
ATOM   25536 C  CA  . GLU   O  1  120 ? 19.352  -204.992 25.989  1.00 100.10 ? 120 GLU   O CA  1 
ATOM   25537 C  C   . GLU   O  1  120 ? 20.173  -205.997 26.811  1.00 97.43  ? 120 GLU   O C   1 
ATOM   25538 O  O   . GLU   O  1  120 ? 21.337  -206.250 26.438  1.00 90.26  ? 120 GLU   O O   1 
ATOM   25539 C  CB  . GLU   O  1  120 ? 19.429  -203.553 26.510  1.00 103.75 ? 120 GLU   O CB  1 
ATOM   25540 C  CG  . GLU   O  1  120 ? 18.963  -202.532 25.484  1.00 106.66 ? 120 GLU   O CG  1 
ATOM   25541 C  CD  . GLU   O  1  120 ? 18.904  -201.093 25.966  1.00 113.26 ? 120 GLU   O CD  1 
ATOM   25542 O  OE1 . GLU   O  1  120 ? 18.435  -200.231 25.189  1.00 118.54 ? 120 GLU   O OE1 1 
ATOM   25543 O  OE2 . GLU   O  1  120 ? 19.327  -200.837 27.113  1.00 119.33 ? 120 GLU   O OE2 1 
ATOM   25544 N  N   . ALA   O  1  121 ? 19.573  -206.598 27.845  1.00 98.06  ? 121 ALA   O N   1 
ATOM   25545 C  CA  . ALA   O  1  121 ? 20.200  -207.640 28.698  1.00 100.95 ? 121 ALA   O CA  1 
ATOM   25546 C  C   . ALA   O  1  121 ? 20.428  -208.918 27.880  1.00 103.75 ? 121 ALA   O C   1 
ATOM   25547 O  O   . ALA   O  1  121 ? 21.115  -209.837 28.378  1.00 106.84 ? 121 ALA   O O   1 
ATOM   25548 C  CB  . ALA   O  1  121 ? 19.337  -207.911 29.907  1.00 101.27 ? 121 ALA   O CB  1 
ATOM   25549 N  N   . THR   O  1  122 ? 19.873  -208.960 26.666  1.00 101.10 ? 122 THR   O N   1 
ATOM   25550 C  CA  . THR   O  1  122 ? 19.930  -210.101 25.719  1.00 99.91  ? 122 THR   O CA  1 
ATOM   25551 C  C   . THR   O  1  122 ? 21.093  -209.902 24.734  1.00 99.95  ? 122 THR   O C   1 
ATOM   25552 O  O   . THR   O  1  122 ? 21.595  -210.914 24.226  1.00 98.66  ? 122 THR   O O   1 
ATOM   25553 C  CB  . THR   O  1  122 ? 18.564  -210.257 25.037  1.00 98.41  ? 122 THR   O CB  1 
ATOM   25554 O  OG1 . THR   O  1  122 ? 17.706  -210.951 25.943  1.00 100.07 ? 122 THR   O OG1 1 
ATOM   25555 C  CG2 . THR   O  1  122 ? 18.634  -210.974 23.709  1.00 99.19  ? 122 THR   O CG2 1 
ATOM   25556 N  N   . GLN   O  1  123 ? 21.517  -208.657 24.486  1.00 99.24  ? 123 GLN   O N   1 
ATOM   25557 C  CA  . GLN   O  1  123 ? 22.475  -208.312 23.398  1.00 97.21  ? 123 GLN   O CA  1 
ATOM   25558 C  C   . GLN   O  1  123 ? 23.726  -207.596 23.932  1.00 96.05  ? 123 GLN   O C   1 
ATOM   25559 O  O   . GLN   O  1  123 ? 24.796  -207.782 23.319  1.00 96.85  ? 123 GLN   O O   1 
ATOM   25560 C  CB  . GLN   O  1  123 ? 21.779  -207.446 22.350  1.00 94.83  ? 123 GLN   O CB  1 
ATOM   25561 C  CG  . GLN   O  1  123 ? 22.564  -207.325 21.053  1.00 94.65  ? 123 GLN   O CG  1 
ATOM   25562 C  CD  . GLN   O  1  123 ? 21.729  -206.771 19.925  1.00 94.57  ? 123 GLN   O CD  1 
ATOM   25563 O  OE1 . GLN   O  1  123 ? 20.685  -206.159 20.139  1.00 95.77  ? 123 GLN   O OE1 1 
ATOM   25564 N  NE2 . GLN   O  1  123 ? 22.189  -206.981 18.703  1.00 96.21  ? 123 GLN   O NE2 1 
ATOM   25565 N  N   . SER   O  1  124 ? 23.613  -206.794 24.997  1.00 93.97  ? 124 SER   O N   1 
ATOM   25566 C  CA  . SER   O  1  124 ? 24.723  -205.954 25.526  1.00 97.05  ? 124 SER   O CA  1 
ATOM   25567 C  C   . SER   O  1  124 ? 25.868  -206.836 26.035  1.00 97.45  ? 124 SER   O C   1 
ATOM   25568 O  O   . SER   O  1  124 ? 25.659  -208.053 26.222  1.00 96.32  ? 124 SER   O O   1 
ATOM   25569 C  CB  . SER   O  1  124 ? 24.255  -205.011 26.606  1.00 98.28  ? 124 SER   O CB  1 
ATOM   25570 O  OG  . SER   O  1  124 ? 23.087  -204.314 26.205  1.00 101.08 ? 124 SER   O OG  1 
ATOM   25571 N  N   . GLY   O  1  125 ? 27.031  -206.220 26.258  1.00 98.53  ? 125 GLY   O N   1 
ATOM   25572 C  CA  . GLY   O  1  125 ? 28.262  -206.886 26.720  1.00 94.48  ? 125 GLY   O CA  1 
ATOM   25573 C  C   . GLY   O  1  125 ? 28.168  -207.294 28.178  1.00 94.14  ? 125 GLY   O C   1 
ATOM   25574 O  O   . GLY   O  1  125 ? 27.700  -206.473 28.991  1.00 90.56  ? 125 GLY   O O   1 
ATOM   25575 N  N   . GLY   O  1  126 ? 28.567  -208.531 28.484  1.00 95.56  ? 126 GLY   O N   1 
ATOM   25576 C  CA  . GLY   O  1  126 ? 28.849  -209.025 29.847  1.00 94.97  ? 126 GLY   O CA  1 
ATOM   25577 C  C   . GLY   O  1  126 ? 27.635  -209.020 30.762  1.00 91.29  ? 126 GLY   O C   1 
ATOM   25578 O  O   . GLY   O  1  126 ? 27.809  -208.709 31.959  1.00 92.73  ? 126 GLY   O O   1 
ATOM   25579 N  N   . VAL   O  1  127 ? 26.454  -209.366 30.245  1.00 91.31  ? 127 VAL   O N   1 
ATOM   25580 C  CA  . VAL   O  1  127 ? 25.218  -209.544 31.065  1.00 94.81  ? 127 VAL   O CA  1 
ATOM   25581 C  C   . VAL   O  1  127 ? 24.439  -210.767 30.570  1.00 96.19  ? 127 VAL   O C   1 
ATOM   25582 O  O   . VAL   O  1  127 ? 24.425  -211.026 29.341  1.00 94.37  ? 127 VAL   O O   1 
ATOM   25583 C  CB  . VAL   O  1  127 ? 24.330  -208.288 31.052  1.00 95.81  ? 127 VAL   O CB  1 
ATOM   25584 C  CG1 . VAL   O  1  127 ? 24.935  -207.167 31.879  1.00 98.15  ? 127 VAL   O CG1 1 
ATOM   25585 C  CG2 . VAL   O  1  127 ? 24.029  -207.815 29.637  1.00 98.46  ? 127 VAL   O CG2 1 
ATOM   25586 N  N   . ARG   O  1  128 ? 23.821  -211.485 31.512  1.00 95.50  ? 128 ARG   O N   1 
ATOM   25587 C  CA  . ARG   O  1  128 ? 22.796  -212.524 31.242  1.00 94.04  ? 128 ARG   O CA  1 
ATOM   25588 C  C   . ARG   O  1  128 ? 21.441  -211.839 31.099  1.00 94.24  ? 128 ARG   O C   1 
ATOM   25589 O  O   . ARG   O  1  128 ? 21.229  -210.763 31.659  1.00 91.37  ? 128 ARG   O O   1 
ATOM   25590 C  CB  . ARG   O  1  128 ? 22.745  -213.562 32.368  1.00 93.97  ? 128 ARG   O CB  1 
ATOM   25591 C  CG  . ARG   O  1  128 ? 22.254  -213.019 33.703  1.00 94.48  ? 128 ARG   O CG  1 
ATOM   25592 C  CD  . ARG   O  1  128 ? 21.841  -214.109 34.671  1.00 94.58  ? 128 ARG   O CD  1 
ATOM   25593 N  NE  . ARG   O  1  128 ? 21.583  -213.561 35.996  1.00 94.30  ? 128 ARG   O NE  1 
ATOM   25594 C  CZ  . ARG   O  1  128 ? 20.457  -212.957 36.375  1.00 93.01  ? 128 ARG   O CZ  1 
ATOM   25595 N  NH1 . ARG   O  1  128 ? 19.447  -212.818 35.532  1.00 90.67  ? 128 ARG   O NH1 1 
ATOM   25596 N  NH2 . ARG   O  1  128 ? 20.349  -212.493 37.609  1.00 92.60  ? 128 ARG   O NH2 1 
ATOM   25597 N  N   . PRO   O  1  129 ? 20.489  -212.435 30.346  1.00 93.96  ? 129 PRO   O N   1 
ATOM   25598 C  CA  . PRO   O  1  129 ? 19.108  -211.954 30.323  1.00 93.77  ? 129 PRO   O CA  1 
ATOM   25599 C  C   . PRO   O  1  129 ? 18.447  -211.998 31.708  1.00 92.89  ? 129 PRO   O C   1 
ATOM   25600 O  O   . PRO   O  1  129 ? 18.924  -212.724 32.561  1.00 89.78  ? 129 PRO   O O   1 
ATOM   25601 C  CB  . PRO   O  1  129 ? 18.388  -212.933 29.383  1.00 93.49  ? 129 PRO   O CB  1 
ATOM   25602 C  CG  . PRO   O  1  129 ? 19.493  -213.505 28.524  1.00 93.76  ? 129 PRO   O CG  1 
ATOM   25603 C  CD  . PRO   O  1  129 ? 20.699  -213.570 29.436  1.00 93.98  ? 129 PRO   O CD  1 
ATOM   25604 N  N   . PHE   O  1  130 ? 17.375  -211.222 31.890  1.00 93.73  ? 130 PHE   O N   1 
ATOM   25605 C  CA  . PHE   O  1  130 ? 16.525  -211.235 33.109  1.00 94.17  ? 130 PHE   O CA  1 
ATOM   25606 C  C   . PHE   O  1  130 ? 15.774  -212.566 33.163  1.00 91.25  ? 130 PHE   O C   1 
ATOM   25607 O  O   . PHE   O  1  130 ? 15.294  -213.021 32.110  1.00 88.09  ? 130 PHE   O O   1 
ATOM   25608 C  CB  . PHE   O  1  130 ? 15.540  -210.062 33.117  1.00 96.24  ? 130 PHE   O CB  1 
ATOM   25609 C  CG  . PHE   O  1  130 ? 16.159  -208.710 33.373  1.00 96.65  ? 130 PHE   O CG  1 
ATOM   25610 C  CD1 . PHE   O  1  130 ? 16.352  -208.250 34.667  1.00 96.61  ? 130 PHE   O CD1 1 
ATOM   25611 C  CD2 . PHE   O  1  130 ? 16.542  -207.895 32.320  1.00 94.71  ? 130 PHE   O CD2 1 
ATOM   25612 C  CE1 . PHE   O  1  130 ? 16.917  -207.006 34.900  1.00 94.13  ? 130 PHE   O CE1 1 
ATOM   25613 C  CE2 . PHE   O  1  130 ? 17.110  -206.654 32.556  1.00 93.16  ? 130 PHE   O CE2 1 
ATOM   25614 C  CZ  . PHE   O  1  130 ? 17.296  -206.211 33.845  1.00 94.22  ? 130 PHE   O CZ  1 
ATOM   25615 N  N   . GLY   O  1  131 ? 15.678  -213.163 34.352  1.00 92.38  ? 131 GLY   O N   1 
ATOM   25616 C  CA  . GLY   O  1  131 ? 15.049  -214.482 34.558  1.00 93.79  ? 131 GLY   O CA  1 
ATOM   25617 C  C   . GLY   O  1  131 ? 13.608  -214.355 35.016  1.00 94.18  ? 131 GLY   O C   1 
ATOM   25618 O  O   . GLY   O  1  131 ? 13.240  -215.041 35.994  1.00 94.76  ? 131 GLY   O O   1 
ATOM   25619 N  N   . VAL   O  1  132 ? 12.812  -213.524 34.333  1.00 92.56  ? 132 VAL   O N   1 
ATOM   25620 C  CA  . VAL   O  1  132 ? 11.402  -213.223 34.722  1.00 93.05  ? 132 VAL   O CA  1 
ATOM   25621 C  C   . VAL   O  1  132 ? 10.538  -213.032 33.475  1.00 90.77  ? 132 VAL   O C   1 
ATOM   25622 O  O   . VAL   O  1  132 ? 11.059  -212.545 32.454  1.00 88.84  ? 132 VAL   O O   1 
ATOM   25623 C  CB  . VAL   O  1  132 ? 11.317  -211.978 35.624  1.00 93.24  ? 132 VAL   O CB  1 
ATOM   25624 C  CG1 . VAL   O  1  132 ? 11.786  -212.277 37.035  1.00 94.39  ? 132 VAL   O CG1 1 
ATOM   25625 C  CG2 . VAL   O  1  132 ? 12.081  -210.799 35.044  1.00 94.85  ? 132 VAL   O CG2 1 
ATOM   25626 N  N   . SER   O  1  133 ? 9.262   -213.409 33.586  1.00 93.58  ? 133 SER   O N   1 
ATOM   25627 C  CA  . SER   O  1  133 ? 8.147   -212.981 32.704  1.00 97.18  ? 133 SER   O CA  1 
ATOM   25628 C  C   . SER   O  1  133 ? 7.231   -212.060 33.515  1.00 99.44  ? 133 SER   O C   1 
ATOM   25629 O  O   . SER   O  1  133 ? 6.825   -212.467 34.621  1.00 101.14 ? 133 SER   O O   1 
ATOM   25630 C  CB  . SER   O  1  133 ? 7.386   -214.156 32.146  1.00 97.98  ? 133 SER   O CB  1 
ATOM   25631 O  OG  . SER   O  1  133 ? 8.055   -214.702 31.019  1.00 99.27  ? 133 SER   O OG  1 
ATOM   25632 N  N   . LEU   O  1  134 ? 6.948   -210.862 33.000  1.00 100.52 ? 134 LEU   O N   1 
ATOM   25633 C  CA  . LEU   O  1  134 ? 6.068   -209.863 33.661  1.00 101.11 ? 134 LEU   O CA  1 
ATOM   25634 C  C   . LEU   O  1  134 ? 4.654   -209.977 33.087  1.00 101.08 ? 134 LEU   O C   1 
ATOM   25635 O  O   . LEU   O  1  134 ? 4.527   -210.254 31.879  1.00 99.63  ? 134 LEU   O O   1 
ATOM   25636 C  CB  . LEU   O  1  134 ? 6.622   -208.454 33.430  1.00 100.27 ? 134 LEU   O CB  1 
ATOM   25637 C  CG  . LEU   O  1  134 ? 8.046   -208.201 33.918  1.00 100.49 ? 134 LEU   O CG  1 
ATOM   25638 C  CD1 . LEU   O  1  134 ? 8.496   -206.801 33.535  1.00 100.51 ? 134 LEU   O CD1 1 
ATOM   25639 C  CD2 . LEU   O  1  134 ? 8.158   -208.400 35.422  1.00 101.74 ? 134 LEU   O CD2 1 
ATOM   25640 N  N   . LEU   O  1  135 ? 3.645   -209.783 33.939  1.00 101.87 ? 135 LEU   O N   1 
ATOM   25641 C  CA  . LEU   O  1  135 ? 2.260   -209.426 33.537  1.00 103.67 ? 135 LEU   O CA  1 
ATOM   25642 C  C   . LEU   O  1  135 ? 1.983   -208.002 34.024  1.00 104.25 ? 135 LEU   O C   1 
ATOM   25643 O  O   . LEU   O  1  135 ? 1.938   -207.805 35.257  1.00 104.51 ? 135 LEU   O O   1 
ATOM   25644 C  CB  . LEU   O  1  135 ? 1.257   -210.408 34.149  1.00 104.64 ? 135 LEU   O CB  1 
ATOM   25645 C  CG  . LEU   O  1  135 ? 1.346   -211.858 33.679  1.00 106.22 ? 135 LEU   O CG  1 
ATOM   25646 C  CD1 . LEU   O  1  135 ? 0.300   -212.704 34.389  1.00 108.69 ? 135 LEU   O CD1 1 
ATOM   25647 C  CD2 . LEU   O  1  135 ? 1.185   -211.970 32.169  1.00 106.28 ? 135 LEU   O CD2 1 
ATOM   25648 N  N   . ILE   O  1  136 ? 1.826   -207.053 33.096  1.00 105.31 ? 136 ILE   O N   1 
ATOM   25649 C  CA  . ILE   O  1  136 ? 1.564   -205.615 33.403  1.00 103.34 ? 136 ILE   O CA  1 
ATOM   25650 C  C   . ILE   O  1  136 ? 0.118   -205.287 33.017  1.00 101.61 ? 136 ILE   O C   1 
ATOM   25651 O  O   . ILE   O  1  136 ? -0.213  -205.368 31.818  1.00 99.40  ? 136 ILE   O O   1 
ATOM   25652 C  CB  . ILE   O  1  136 ? 2.579   -204.700 32.694  1.00 104.55 ? 136 ILE   O CB  1 
ATOM   25653 C  CG1 . ILE   O  1  136 ? 4.016   -205.044 33.096  1.00 105.01 ? 136 ILE   O CG1 1 
ATOM   25654 C  CG2 . ILE   O  1  136 ? 2.255   -203.236 32.961  1.00 105.84 ? 136 ILE   O CG2 1 
ATOM   25655 C  CD1 . ILE   O  1  136 ? 5.064   -204.535 32.136  1.00 106.59 ? 136 ILE   O CD1 1 
ATOM   25656 N  N   . ALA   O  1  137 ? -0.697  -204.943 34.016  1.00 101.00 ? 137 ALA   O N   1 
ATOM   25657 C  CA  . ALA   O  1  137 ? -2.092  -204.470 33.871  1.00 103.14 ? 137 ALA   O CA  1 
ATOM   25658 C  C   . ALA   O  1  137 ? -2.111  -202.954 34.068  1.00 102.87 ? 137 ALA   O C   1 
ATOM   25659 O  O   . ALA   O  1  137 ? -1.375  -202.463 34.947  1.00 102.39 ? 137 ALA   O O   1 
ATOM   25660 C  CB  . ALA   O  1  137 ? -2.978  -205.163 34.874  1.00 104.93 ? 137 ALA   O CB  1 
ATOM   25661 N  N   . GLY   O  1  138 ? -2.918  -202.240 33.282  1.00 104.28 ? 138 GLY   O N   1 
ATOM   25662 C  CA  . GLY   O  1  138 ? -3.026  -200.774 33.389  1.00 105.57 ? 138 GLY   O CA  1 
ATOM   25663 C  C   . GLY   O  1  138 ? -4.200  -200.201 32.616  1.00 107.07 ? 138 GLY   O C   1 
ATOM   25664 O  O   . GLY   O  1  138 ? -4.847  -200.949 31.855  1.00 104.52 ? 138 GLY   O O   1 
ATOM   25665 N  N   . HIS   O  1  139 ? -4.460  -198.908 32.829  1.00 108.42 ? 139 HIS   O N   1 
ATOM   25666 C  CA  . HIS   O  1  139 ? -5.526  -198.111 32.166  1.00 109.64 ? 139 HIS   O CA  1 
ATOM   25667 C  C   . HIS   O  1  139 ? -4.942  -196.788 31.667  1.00 109.28 ? 139 HIS   O C   1 
ATOM   25668 O  O   . HIS   O  1  139 ? -3.996  -196.276 32.294  1.00 110.97 ? 139 HIS   O O   1 
ATOM   25669 C  CB  . HIS   O  1  139 ? -6.699  -197.856 33.124  1.00 109.64 ? 139 HIS   O CB  1 
ATOM   25670 C  CG  . HIS   O  1  139 ? -7.759  -196.980 32.545  1.00 109.35 ? 139 HIS   O CG  1 
ATOM   25671 N  ND1 . HIS   O  1  139 ? -7.732  -195.607 32.676  1.00 109.12 ? 139 HIS   O ND1 1 
ATOM   25672 C  CD2 . HIS   O  1  139 ? -8.862  -197.272 31.822  1.00 107.84 ? 139 HIS   O CD2 1 
ATOM   25673 C  CE1 . HIS   O  1  139 ? -8.779  -195.091 32.066  1.00 110.30 ? 139 HIS   O CE1 1 
ATOM   25674 N  NE2 . HIS   O  1  139 ? -9.489  -196.092 31.532  1.00 109.52 ? 139 HIS   O NE2 1 
ATOM   25675 N  N   . ASP   O  1  140 ? -5.502  -196.259 30.582  1.00 107.30 ? 140 ASP   O N   1 
ATOM   25676 C  CA  . ASP   O  1  140 ? -5.196  -194.898 30.078  1.00 110.78 ? 140 ASP   O CA  1 
ATOM   25677 C  C   . ASP   O  1  140 ? -6.392  -194.416 29.251  1.00 113.25 ? 140 ASP   O C   1 
ATOM   25678 O  O   . ASP   O  1  140 ? -7.128  -195.272 28.720  1.00 115.35 ? 140 ASP   O O   1 
ATOM   25679 C  CB  . ASP   O  1  140 ? -3.860  -194.878 29.331  1.00 112.42 ? 140 ASP   O CB  1 
ATOM   25680 C  CG  . ASP   O  1  140 ? -3.822  -195.787 28.118  1.00 114.46 ? 140 ASP   O CG  1 
ATOM   25681 O  OD1 . ASP   O  1  140 ? -4.240  -195.329 27.040  1.00 117.69 ? 140 ASP   O OD1 1 
ATOM   25682 O  OD2 . ASP   O  1  140 ? -3.380  -196.944 28.265  1.00 115.60 ? 140 ASP   O OD2 1 
ATOM   25683 N  N   . GLU   O  1  141 ? -6.567  -193.094 29.169  1.00 116.39 ? 141 GLU   O N   1 
ATOM   25684 C  CA  . GLU   O  1  141 ? -7.805  -192.418 28.703  1.00 116.08 ? 141 GLU   O CA  1 
ATOM   25685 C  C   . GLU   O  1  141 ? -8.182  -192.881 27.288  1.00 114.50 ? 141 GLU   O C   1 
ATOM   25686 O  O   . GLU   O  1  141 ? -9.393  -193.034 27.038  1.00 116.38 ? 141 GLU   O O   1 
ATOM   25687 C  CB  . GLU   O  1  141 ? -7.614  -190.902 28.762  1.00 118.08 ? 141 GLU   O CB  1 
ATOM   25688 C  CG  . GLU   O  1  141 ? -8.900  -190.119 28.585  1.00 124.29 ? 141 GLU   O CG  1 
ATOM   25689 C  CD  . GLU   O  1  141 ? -8.695  -188.619 28.497  1.00 129.40 ? 141 GLU   O CD  1 
ATOM   25690 O  OE1 . GLU   O  1  141 ? -9.466  -187.964 27.769  1.00 140.20 ? 141 GLU   O OE1 1 
ATOM   25691 O  OE2 . GLU   O  1  141 ? -7.762  -188.112 29.154  1.00 132.98 ? 141 GLU   O OE2 1 
ATOM   25692 N  N   . PHE   O  1  142 ? -7.201  -193.100 26.403  1.00 112.32 ? 142 PHE   O N   1 
ATOM   25693 C  CA  . PHE   O  1  142 ? -7.420  -193.285 24.941  1.00 120.15 ? 142 PHE   O CA  1 
ATOM   25694 C  C   . PHE   O  1  142 ? -7.345  -194.763 24.522  1.00 118.43 ? 142 PHE   O C   1 
ATOM   25695 O  O   . PHE   O  1  142 ? -7.704  -195.046 23.361  1.00 122.78 ? 142 PHE   O O   1 
ATOM   25696 C  CB  . PHE   O  1  142 ? -6.425  -192.439 24.139  1.00 122.50 ? 142 PHE   O CB  1 
ATOM   25697 C  CG  . PHE   O  1  142 ? -6.655  -190.949 24.225  1.00 125.70 ? 142 PHE   O CG  1 
ATOM   25698 C  CD1 . PHE   O  1  142 ? -6.194  -190.224 25.314  1.00 124.41 ? 142 PHE   O CD1 1 
ATOM   25699 C  CD2 . PHE   O  1  142 ? -7.332  -190.271 23.222  1.00 126.34 ? 142 PHE   O CD2 1 
ATOM   25700 C  CE1 . PHE   O  1  142 ? -6.404  -188.856 25.398  1.00 125.05 ? 142 PHE   O CE1 1 
ATOM   25701 C  CE2 . PHE   O  1  142 ? -7.539  -188.902 23.307  1.00 126.48 ? 142 PHE   O CE2 1 
ATOM   25702 C  CZ  . PHE   O  1  142 ? -7.077  -188.198 24.395  1.00 126.54 ? 142 PHE   O CZ  1 
ATOM   25703 N  N   . ASN   O  1  143 ? -6.899  -195.669 25.402  1.00 115.09 ? 143 ASN   O N   1 
ATOM   25704 C  CA  . ASN   O  1  143 ? -6.808  -197.128 25.110  1.00 115.32 ? 143 ASN   O CA  1 
ATOM   25705 C  C   . ASN   O  1  143 ? -7.691  -197.945 26.064  1.00 118.40 ? 143 ASN   O C   1 
ATOM   25706 O  O   . ASN   O  1  143 ? -7.887  -199.143 25.780  1.00 119.47 ? 143 ASN   O O   1 
ATOM   25707 C  CB  . ASN   O  1  143 ? -5.366  -197.635 25.181  1.00 112.01 ? 143 ASN   O CB  1 
ATOM   25708 C  CG  . ASN   O  1  143 ? -4.491  -197.046 24.097  1.00 112.03 ? 143 ASN   O CG  1 
ATOM   25709 O  OD1 . ASN   O  1  143 ? -4.499  -197.522 22.964  1.00 112.25 ? 143 ASN   O OD1 1 
ATOM   25710 N  ND2 . ASN   O  1  143 ? -3.739  -196.010 24.428  1.00 115.46 ? 143 ASN   O ND2 1 
ATOM   25711 N  N   . GLY   O  1  144 ? -8.198  -197.338 27.143  1.00 118.84 ? 144 GLY   O N   1 
ATOM   25712 C  CA  . GLY   O  1  144 ? -8.947  -198.042 28.202  1.00 119.83 ? 144 GLY   O CA  1 
ATOM   25713 C  C   . GLY   O  1  144 ? -8.058  -199.034 28.934  1.00 116.98 ? 144 GLY   O C   1 
ATOM   25714 O  O   . GLY   O  1  144 ? -6.845  -198.762 29.053  1.00 118.13 ? 144 GLY   O O   1 
ATOM   25715 N  N   . PHE   O  1  145 ? -8.630  -200.152 29.390  1.00 112.97 ? 145 PHE   O N   1 
ATOM   25716 C  CA  . PHE   O  1  145 ? -7.924  -201.201 30.171  1.00 107.92 ? 145 PHE   O CA  1 
ATOM   25717 C  C   . PHE   O  1  145 ? -7.164  -202.125 29.218  1.00 103.85 ? 145 PHE   O C   1 
ATOM   25718 O  O   . PHE   O  1  145 ? -7.654  -202.379 28.102  1.00 101.88 ? 145 PHE   O O   1 
ATOM   25719 C  CB  . PHE   O  1  145 ? -8.912  -201.984 31.036  1.00 108.45 ? 145 PHE   O CB  1 
ATOM   25720 C  CG  . PHE   O  1  145 ? -9.617  -201.140 32.064  1.00 109.92 ? 145 PHE   O CG  1 
ATOM   25721 C  CD1 . PHE   O  1  145 ? -8.985  -200.794 33.249  1.00 109.55 ? 145 PHE   O CD1 1 
ATOM   25722 C  CD2 . PHE   O  1  145 ? -10.904 -200.676 31.839  1.00 112.98 ? 145 PHE   O CD2 1 
ATOM   25723 C  CE1 . PHE   O  1  145 ? -9.632  -200.010 34.192  1.00 111.73 ? 145 PHE   O CE1 1 
ATOM   25724 C  CE2 . PHE   O  1  145 ? -11.548 -199.891 32.783  1.00 114.77 ? 145 PHE   O CE2 1 
ATOM   25725 C  CZ  . PHE   O  1  145 ? -10.912 -199.561 33.958  1.00 114.75 ? 145 PHE   O CZ  1 
ATOM   25726 N  N   . SER   O  1  146 ? -6.000  -202.611 29.657  1.00 103.97 ? 146 SER   O N   1 
ATOM   25727 C  CA  . SER   O  1  146 ? -5.118  -203.518 28.878  1.00 107.65 ? 146 SER   O CA  1 
ATOM   25728 C  C   . SER   O  1  146 ? -4.234  -204.356 29.811  1.00 109.29 ? 146 SER   O C   1 
ATOM   25729 O  O   . SER   O  1  146 ? -3.916  -203.889 30.927  1.00 109.17 ? 146 SER   O O   1 
ATOM   25730 C  CB  . SER   O  1  146 ? -4.296  -202.744 27.883  1.00 108.22 ? 146 SER   O CB  1 
ATOM   25731 O  OG  . SER   O  1  146 ? -3.613  -201.674 28.515  1.00 110.58 ? 146 SER   O OG  1 
ATOM   25732 N  N   . LEU   O  1  147 ? -3.864  -205.552 29.344  1.00 108.70 ? 147 LEU   O N   1 
ATOM   25733 C  CA  . LEU   O  1  147 ? -3.028  -206.555 30.056  1.00 105.38 ? 147 LEU   O CA  1 
ATOM   25734 C  C   . LEU   O  1  147 ? -1.947  -207.048 29.088  1.00 101.55 ? 147 LEU   O C   1 
ATOM   25735 O  O   . LEU   O  1  147 ? -2.310  -207.470 27.972  1.00 100.04 ? 147 LEU   O O   1 
ATOM   25736 C  CB  . LEU   O  1  147 ? -3.937  -207.699 30.517  1.00 105.53 ? 147 LEU   O CB  1 
ATOM   25737 C  CG  . LEU   O  1  147 ? -3.240  -208.915 31.125  1.00 104.16 ? 147 LEU   O CG  1 
ATOM   25738 C  CD1 . LEU   O  1  147 ? -2.685  -208.590 32.501  1.00 105.15 ? 147 LEU   O CD1 1 
ATOM   25739 C  CD2 . LEU   O  1  147 ? -4.198  -210.092 31.204  1.00 105.11 ? 147 LEU   O CD2 1 
ATOM   25740 N  N   . TYR   O  1  148 ? -0.678  -206.986 29.496  1.00 99.42  ? 148 TYR   O N   1 
ATOM   25741 C  CA  . TYR   O  1  148 ? 0.492   -207.353 28.657  1.00 99.61  ? 148 TYR   O CA  1 
ATOM   25742 C  C   . TYR   O  1  148 ? 1.364   -208.373 29.389  1.00 98.27  ? 148 TYR   O C   1 
ATOM   25743 O  O   . TYR   O  1  148 ? 1.465   -208.307 30.627  1.00 100.67 ? 148 TYR   O O   1 
ATOM   25744 C  CB  . TYR   O  1  148 ? 1.305   -206.109 28.296  1.00 98.28  ? 148 TYR   O CB  1 
ATOM   25745 C  CG  . TYR   O  1  148 ? 0.666   -205.249 27.239  1.00 100.83 ? 148 TYR   O CG  1 
ATOM   25746 C  CD1 . TYR   O  1  148 ? -0.277  -204.290 27.572  1.00 101.63 ? 148 TYR   O CD1 1 
ATOM   25747 C  CD2 . TYR   O  1  148 ? 0.988   -205.405 25.901  1.00 100.48 ? 148 TYR   O CD2 1 
ATOM   25748 C  CE1 . TYR   O  1  148 ? -0.878  -203.502 26.604  1.00 102.52 ? 148 TYR   O CE1 1 
ATOM   25749 C  CE2 . TYR   O  1  148 ? 0.396   -204.626 24.920  1.00 100.99 ? 148 TYR   O CE2 1 
ATOM   25750 C  CZ  . TYR   O  1  148 ? -0.541  -203.672 25.272  1.00 101.99 ? 148 TYR   O CZ  1 
ATOM   25751 O  OH  . TYR   O  1  148 ? -1.123  -202.898 24.310  1.00 108.02 ? 148 TYR   O OH  1 
ATOM   25752 N  N   . GLN   O  1  149 ? 1.971   -209.281 28.623  1.00 97.94  ? 149 GLN   O N   1 
ATOM   25753 C  CA  . GLN   O  1  149 ? 2.999   -210.242 29.095  1.00 99.28  ? 149 GLN   O CA  1 
ATOM   25754 C  C   . GLN   O  1  149 ? 4.334   -209.864 28.453  1.00 95.35  ? 149 GLN   O C   1 
ATOM   25755 O  O   . GLN   O  1  149 ? 4.369   -209.777 27.217  1.00 94.03  ? 149 GLN   O O   1 
ATOM   25756 C  CB  . GLN   O  1  149 ? 2.613   -211.674 28.719  1.00 101.70 ? 149 GLN   O CB  1 
ATOM   25757 C  CG  . GLN   O  1  149 ? 3.617   -212.715 29.195  1.00 102.48 ? 149 GLN   O CG  1 
ATOM   25758 C  CD  . GLN   O  1  149 ? 3.256   -214.116 28.768  1.00 103.62 ? 149 GLN   O CD  1 
ATOM   25759 O  OE1 . GLN   O  1  149 ? 2.089   -214.442 28.558  1.00 104.60 ? 149 GLN   O OE1 1 
ATOM   25760 N  NE2 . GLN   O  1  149 ? 4.267   -214.961 28.645  1.00 103.39 ? 149 GLN   O NE2 1 
ATOM   25761 N  N   . VAL   O  1  150 ? 5.378   -209.649 29.258  1.00 96.00  ? 150 VAL   O N   1 
ATOM   25762 C  CA  . VAL   O  1  150 ? 6.762   -209.357 28.777  1.00 97.22  ? 150 VAL   O CA  1 
ATOM   25763 C  C   . VAL   O  1  150 ? 7.656   -210.550 29.131  1.00 97.29  ? 150 VAL   O C   1 
ATOM   25764 O  O   . VAL   O  1  150 ? 7.732   -210.890 30.326  1.00 98.11  ? 150 VAL   O O   1 
ATOM   25765 C  CB  . VAL   O  1  150 ? 7.317   -208.049 29.371  1.00 98.23  ? 150 VAL   O CB  1 
ATOM   25766 C  CG1 . VAL   O  1  150 ? 8.605   -207.630 28.677  1.00 99.12  ? 150 VAL   O CG1 1 
ATOM   25767 C  CG2 . VAL   O  1  150 ? 6.296   -206.923 29.323  1.00 98.85  ? 150 VAL   O CG2 1 
ATOM   25768 N  N   . ASP   O  1  151 ? 8.308   -211.146 28.128  1.00 96.15  ? 151 ASP   O N   1 
ATOM   25769 C  CA  . ASP   O  1  151 ? 9.166   -212.350 28.284  1.00 98.04  ? 151 ASP   O CA  1 
ATOM   25770 C  C   . ASP   O  1  151 ? 10.633  -211.931 28.336  1.00 95.40  ? 151 ASP   O C   1 
ATOM   25771 O  O   . ASP   O  1  151 ? 10.992  -210.859 27.854  1.00 94.17  ? 151 ASP   O O   1 
ATOM   25772 C  CB  . ASP   O  1  151 ? 8.922   -213.359 27.156  1.00 102.38 ? 151 ASP   O CB  1 
ATOM   25773 C  CG  . ASP   O  1  151 ? 7.683   -214.223 27.335  1.00 103.42 ? 151 ASP   O CG  1 
ATOM   25774 O  OD1 . ASP   O  1  151 ? 7.041   -214.130 28.404  1.00 109.03 ? 151 ASP   O OD1 1 
ATOM   25775 O  OD2 . ASP   O  1  151 ? 7.371   -214.985 26.400  1.00 106.78 ? 151 ASP   O OD2 1 
ATOM   25776 N  N   . PRO   O  1  152 ? 11.517  -212.781 28.915  1.00 96.29  ? 152 PRO   O N   1 
ATOM   25777 C  CA  . PRO   O  1  152 ? 12.958  -212.514 28.977  1.00 93.45  ? 152 PRO   O CA  1 
ATOM   25778 C  C   . PRO   O  1  152 ? 13.611  -211.985 27.689  1.00 93.34  ? 152 PRO   O C   1 
ATOM   25779 O  O   . PRO   O  1  152 ? 14.555  -211.223 27.791  1.00 88.56  ? 152 PRO   O O   1 
ATOM   25780 C  CB  . PRO   O  1  152 ? 13.533  -213.903 29.294  1.00 94.39  ? 152 PRO   O CB  1 
ATOM   25781 C  CG  . PRO   O  1  152 ? 12.467  -214.550 30.146  1.00 94.80  ? 152 PRO   O CG  1 
ATOM   25782 C  CD  . PRO   O  1  152 ? 11.160  -214.054 29.566  1.00 96.26  ? 152 PRO   O CD  1 
ATOM   25783 N  N   . SER   O  1  153 ? 13.110  -212.415 26.526  1.00 94.85  ? 153 SER   O N   1 
ATOM   25784 C  CA  . SER   O  1  153 ? 13.573  -211.997 25.175  1.00 96.77  ? 153 SER   O CA  1 
ATOM   25785 C  C   . SER   O  1  153 ? 13.359  -210.492 24.983  1.00 98.07  ? 153 SER   O C   1 
ATOM   25786 O  O   . SER   O  1  153 ? 14.170  -209.863 24.271  1.00 96.95  ? 153 SER   O O   1 
ATOM   25787 C  CB  . SER   O  1  153 ? 12.857  -212.771 24.101  1.00 99.75  ? 153 SER   O CB  1 
ATOM   25788 O  OG  . SER   O  1  153 ? 11.456  -212.546 24.172  1.00 102.01 ? 153 SER   O OG  1 
ATOM   25789 N  N   . GLY   O  1  154 ? 12.297  -209.952 25.589  1.00 99.23  ? 154 GLY   O N   1 
ATOM   25790 C  CA  . GLY   O  1  154 ? 11.834  -208.566 25.400  1.00 100.11 ? 154 GLY   O CA  1 
ATOM   25791 C  C   . GLY   O  1  154 ? 10.574  -208.513 24.552  1.00 102.57 ? 154 GLY   O C   1 
ATOM   25792 O  O   . GLY   O  1  154 ? 10.124  -207.401 24.234  1.00 104.07 ? 154 GLY   O O   1 
ATOM   25793 N  N   . SER   O  1  155 ? 10.029  -209.671 24.171  1.00 101.50 ? 155 SER   O N   1 
ATOM   25794 C  CA  . SER   O  1  155 ? 8.743   -209.787 23.439  1.00 102.63 ? 155 SER   O CA  1 
ATOM   25795 C  C   . SER   O  1  155 ? 7.591   -209.533 24.410  1.00 104.72 ? 155 SER   O C   1 
ATOM   25796 O  O   . SER   O  1  155 ? 7.648   -210.066 25.536  1.00 105.69 ? 155 SER   O O   1 
ATOM   25797 C  CB  . SER   O  1  155 ? 8.603   -211.131 22.796  1.00 103.77 ? 155 SER   O CB  1 
ATOM   25798 O  OG  . SER   O  1  155 ? 9.677   -211.366 21.898  1.00 106.08 ? 155 SER   O OG  1 
ATOM   25799 N  N   . TYR   O  1  156 ? 6.593   -208.755 23.984  1.00 106.43 ? 156 TYR   O N   1 
ATOM   25800 C  CA  . TYR   O  1  156 ? 5.343   -208.506 24.746  1.00 104.87 ? 156 TYR   O CA  1 
ATOM   25801 C  C   . TYR   O  1  156 ? 4.137   -208.797 23.846  1.00 104.46 ? 156 TYR   O C   1 
ATOM   25802 O  O   . TYR   O  1  156 ? 4.204   -208.554 22.624  1.00 107.46 ? 156 TYR   O O   1 
ATOM   25803 C  CB  . TYR   O  1  156 ? 5.334   -207.097 25.352  1.00 103.28 ? 156 TYR   O CB  1 
ATOM   25804 C  CG  . TYR   O  1  156 ? 5.480   -205.958 24.375  1.00 101.52 ? 156 TYR   O CG  1 
ATOM   25805 C  CD1 . TYR   O  1  156 ? 6.731   -205.528 23.962  1.00 101.31 ? 156 TYR   O CD1 1 
ATOM   25806 C  CD2 . TYR   O  1  156 ? 4.370   -205.288 23.887  1.00 100.34 ? 156 TYR   O CD2 1 
ATOM   25807 C  CE1 . TYR   O  1  156 ? 6.875   -204.475 23.074  1.00 102.26 ? 156 TYR   O CE1 1 
ATOM   25808 C  CE2 . TYR   O  1  156 ? 4.496   -204.235 22.996  1.00 99.95  ? 156 TYR   O CE2 1 
ATOM   25809 C  CZ  . TYR   O  1  156 ? 5.753   -203.826 22.589  1.00 102.42 ? 156 TYR   O CZ  1 
ATOM   25810 O  OH  . TYR   O  1  156 ? 5.881   -202.785 21.715  1.00 105.40 ? 156 TYR   O OH  1 
ATOM   25811 N  N   . PHE   O  1  157 ? 3.076   -209.337 24.449  1.00 102.26 ? 157 PHE   O N   1 
ATOM   25812 C  CA  . PHE   O  1  157 ? 1.805   -209.713 23.782  1.00 106.81 ? 157 PHE   O CA  1 
ATOM   25813 C  C   . PHE   O  1  157 ? 0.645   -209.194 24.624  1.00 104.07 ? 157 PHE   O C   1 
ATOM   25814 O  O   . PHE   O  1  157 ? 0.687   -209.280 25.848  1.00 102.27 ? 157 PHE   O O   1 
ATOM   25815 C  CB  . PHE   O  1  157 ? 1.717   -211.231 23.613  1.00 111.86 ? 157 PHE   O CB  1 
ATOM   25816 C  CG  . PHE   O  1  157 ? 3.043   -211.948 23.646  1.00 118.90 ? 157 PHE   O CG  1 
ATOM   25817 C  CD1 . PHE   O  1  157 ? 3.517   -212.515 24.822  1.00 119.66 ? 157 PHE   O CD1 1 
ATOM   25818 C  CD2 . PHE   O  1  157 ? 3.824   -212.050 22.504  1.00 122.78 ? 157 PHE   O CD2 1 
ATOM   25819 C  CE1 . PHE   O  1  157 ? 4.739   -213.171 24.854  1.00 119.02 ? 157 PHE   O CE1 1 
ATOM   25820 C  CE2 . PHE   O  1  157 ? 5.045   -212.708 22.537  1.00 123.94 ? 157 PHE   O CE2 1 
ATOM   25821 C  CZ  . PHE   O  1  157 ? 5.501   -213.267 23.711  1.00 122.82 ? 157 PHE   O CZ  1 
ATOM   25822 N  N   . PRO   O  1  158 ? -0.418  -208.635 24.007  1.00 105.75 ? 158 PRO   O N   1 
ATOM   25823 C  CA  . PRO   O  1  158 ? -1.612  -208.245 24.750  1.00 108.42 ? 158 PRO   O CA  1 
ATOM   25824 C  C   . PRO   O  1  158 ? -2.506  -209.477 24.960  1.00 107.96 ? 158 PRO   O C   1 
ATOM   25825 O  O   . PRO   O  1  158 ? -2.603  -210.285 24.054  1.00 110.55 ? 158 PRO   O O   1 
ATOM   25826 C  CB  . PRO   O  1  158 ? -2.255  -207.176 23.857  1.00 110.61 ? 158 PRO   O CB  1 
ATOM   25827 C  CG  . PRO   O  1  158 ? -1.783  -207.501 22.445  1.00 111.07 ? 158 PRO   O CG  1 
ATOM   25828 C  CD  . PRO   O  1  158 ? -0.542  -208.364 22.569  1.00 107.93 ? 158 PRO   O CD  1 
ATOM   25829 N  N   . TRP   O  1  159 ? -3.108  -209.599 26.147  1.00 108.71 ? 159 TRP   O N   1 
ATOM   25830 C  CA  . TRP   O  1  159 ? -3.931  -210.767 26.563  1.00 109.53 ? 159 TRP   O CA  1 
ATOM   25831 C  C   . TRP   O  1  159 ? -5.302  -210.297 27.060  1.00 107.26 ? 159 TRP   O C   1 
ATOM   25832 O  O   . TRP   O  1  159 ? -5.371  -209.227 27.693  1.00 108.64 ? 159 TRP   O O   1 
ATOM   25833 C  CB  . TRP   O  1  159 ? -3.211  -211.573 27.651  1.00 109.65 ? 159 TRP   O CB  1 
ATOM   25834 C  CG  . TRP   O  1  159 ? -2.019  -212.347 27.177  1.00 114.45 ? 159 TRP   O CG  1 
ATOM   25835 C  CD1 . TRP   O  1  159 ? -0.707  -211.983 27.272  1.00 114.38 ? 159 TRP   O CD1 1 
ATOM   25836 C  CD2 . TRP   O  1  159 ? -2.028  -213.642 26.552  1.00 116.57 ? 159 TRP   O CD2 1 
ATOM   25837 N  NE1 . TRP   O  1  159 ? 0.098   -212.956 26.742  1.00 113.86 ? 159 TRP   O NE1 1 
ATOM   25838 C  CE2 . TRP   O  1  159 ? -0.684  -213.986 26.292  1.00 115.33 ? 159 TRP   O CE2 1 
ATOM   25839 C  CE3 . TRP   O  1  159 ? -3.037  -214.540 26.184  1.00 120.11 ? 159 TRP   O CE3 1 
ATOM   25840 C  CZ2 . TRP   O  1  159 ? -0.329  -215.187 25.680  1.00 115.98 ? 159 TRP   O CZ2 1 
ATOM   25841 C  CZ3 . TRP   O  1  159 ? -2.685  -215.727 25.581  1.00 121.84 ? 159 TRP   O CZ3 1 
ATOM   25842 C  CH2 . TRP   O  1  159 ? -1.348  -216.044 25.333  1.00 119.52 ? 159 TRP   O CH2 1 
ATOM   25843 N  N   . LYS   O  1  160 ? -6.344  -211.084 26.783  1.00 105.40 ? 160 LYS   O N   1 
ATOM   25844 C  CA  . LYS   O  1  160 ? -7.674  -210.981 27.442  1.00 107.80 ? 160 LYS   O CA  1 
ATOM   25845 C  C   . LYS   O  1  160 ? -7.558  -211.579 28.846  1.00 107.30 ? 160 LYS   O C   1 
ATOM   25846 O  O   . LYS   O  1  160 ? -8.118  -210.999 29.794  1.00 109.69 ? 160 LYS   O O   1 
ATOM   25847 C  CB  . LYS   O  1  160 ? -8.742  -211.722 26.635  1.00 109.75 ? 160 LYS   O CB  1 
ATOM   25848 C  CG  . LYS   O  1  160 ? -9.122  -211.062 25.319  1.00 111.66 ? 160 LYS   O CG  1 
ATOM   25849 C  CD  . LYS   O  1  160 ? -9.666  -212.030 24.300  1.00 113.93 ? 160 LYS   O CD  1 
ATOM   25850 C  CE  . LYS   O  1  160 ? -10.147 -211.345 23.041  1.00 116.40 ? 160 LYS   O CE  1 
ATOM   25851 N  NZ  . LYS   O  1  160 ? -10.402 -212.324 21.959  1.00 118.46 ? 160 LYS   O NZ  1 
ATOM   25852 N  N   . ALA   O  1  161 ? -6.857  -212.709 28.953  1.00 104.95 ? 161 ALA   O N   1 
ATOM   25853 C  CA  . ALA   O  1  161 ? -6.509  -213.388 30.221  1.00 104.57 ? 161 ALA   O CA  1 
ATOM   25854 C  C   . ALA   O  1  161 ? -5.385  -214.392 29.953  1.00 102.01 ? 161 ALA   O C   1 
ATOM   25855 O  O   . ALA   O  1  161 ? -5.360  -214.974 28.853  1.00 101.01 ? 161 ALA   O O   1 
ATOM   25856 C  CB  . ALA   O  1  161 ? -7.727  -214.061 30.800  1.00 106.50 ? 161 ALA   O CB  1 
ATOM   25857 N  N   . THR   O  1  162 ? -4.479  -214.573 30.913  1.00 100.72 ? 162 THR   O N   1 
ATOM   25858 C  CA  . THR   O  1  162 ? -3.374  -215.561 30.818  1.00 101.57 ? 162 THR   O CA  1 
ATOM   25859 C  C   . THR   O  1  162 ? -2.793  -215.848 32.201  1.00 102.63 ? 162 THR   O C   1 
ATOM   25860 O  O   . THR   O  1  162 ? -3.107  -215.108 33.153  1.00 104.56 ? 162 THR   O O   1 
ATOM   25861 C  CB  . THR   O  1  162 ? -2.257  -215.077 29.885  1.00 99.06  ? 162 THR   O CB  1 
ATOM   25862 O  OG1 . THR   O  1  162 ? -1.324  -216.144 29.710  1.00 98.25  ? 162 THR   O OG1 1 
ATOM   25863 C  CG2 . THR   O  1  162 ? -1.532  -213.859 30.410  1.00 97.65  ? 162 THR   O CG2 1 
ATOM   25864 N  N   . ALA   O  1  163 ? -1.965  -216.889 32.273  1.00 105.20 ? 163 ALA   O N   1 
ATOM   25865 C  CA  . ALA   O  1  163 ? -1.135  -217.252 33.441  1.00 107.31 ? 163 ALA   O CA  1 
ATOM   25866 C  C   . ALA   O  1  163 ? 0.298   -217.500 32.965  1.00 105.99 ? 163 ALA   O C   1 
ATOM   25867 O  O   . ALA   O  1  163 ? 0.496   -217.744 31.757  1.00 106.86 ? 163 ALA   O O   1 
ATOM   25868 C  CB  . ALA   O  1  163 ? -1.715  -218.461 34.132  1.00 108.01 ? 163 ALA   O CB  1 
ATOM   25869 N  N   . ILE   O  1  164 ? 1.256   -217.413 33.887  1.00 107.11 ? 164 ILE   O N   1 
ATOM   25870 C  CA  . ILE   O  1  164 ? 2.701   -217.697 33.647  1.00 108.67 ? 164 ILE   O CA  1 
ATOM   25871 C  C   . ILE   O  1  164 ? 3.244   -218.447 34.863  1.00 110.40 ? 164 ILE   O C   1 
ATOM   25872 O  O   . ILE   O  1  164 ? 2.708   -218.238 35.970  1.00 109.51 ? 164 ILE   O O   1 
ATOM   25873 C  CB  . ILE   O  1  164 ? 3.491   -216.400 33.389  1.00 107.53 ? 164 ILE   O CB  1 
ATOM   25874 C  CG1 . ILE   O  1  164 ? 3.121   -215.311 34.400  1.00 107.25 ? 164 ILE   O CG1 1 
ATOM   25875 C  CG2 . ILE   O  1  164 ? 3.298   -215.936 31.955  1.00 109.73 ? 164 ILE   O CG2 1 
ATOM   25876 C  CD1 . ILE   O  1  164 ? 4.090   -214.153 34.452  1.00 106.45 ? 164 ILE   O CD1 1 
ATOM   25877 N  N   . GLY   O  1  165 ? 4.261   -219.284 34.650  1.00 115.03 ? 165 GLY   O N   1 
ATOM   25878 C  CA  . GLY   O  1  165 ? 4.993   -219.985 35.722  1.00 117.98 ? 165 GLY   O CA  1 
ATOM   25879 C  C   . GLY   O  1  165 ? 4.567   -221.435 35.873  1.00 120.50 ? 165 GLY   O C   1 
ATOM   25880 O  O   . GLY   O  1  165 ? 4.139   -222.042 34.869  1.00 124.73 ? 165 GLY   O O   1 
ATOM   25881 N  N   . LYS   O  1  166 ? 4.664   -221.947 37.105  1.00 121.69 ? 166 LYS   O N   1 
ATOM   25882 C  CA  . LYS   O  1  166 ? 4.572   -223.383 37.489  1.00 121.86 ? 166 LYS   O CA  1 
ATOM   25883 C  C   . LYS   O  1  166 ? 3.434   -224.072 36.722  1.00 119.73 ? 166 LYS   O C   1 
ATOM   25884 O  O   . LYS   O  1  166 ? 3.742   -224.820 35.775  1.00 122.73 ? 166 LYS   O O   1 
ATOM   25885 C  CB  . LYS   O  1  166 ? 4.398   -223.497 39.008  1.00 120.72 ? 166 LYS   O CB  1 
ATOM   25886 C  CG  . LYS   O  1  166 ? 5.057   -224.704 39.653  1.00 124.98 ? 166 LYS   O CG  1 
ATOM   25887 C  CD  . LYS   O  1  166 ? 5.062   -224.625 41.165  1.00 129.51 ? 166 LYS   O CD  1 
ATOM   25888 C  CE  . LYS   O  1  166 ? 5.680   -225.839 41.824  1.00 135.63 ? 166 LYS   O CE  1 
ATOM   25889 N  NZ  . LYS   O  1  166 ? 7.153   -225.865 41.654  1.00 141.61 ? 166 LYS   O NZ  1 
ATOM   25890 N  N   . GLY   O  1  167 ? 2.177   -223.818 37.105  1.00 119.40 ? 167 GLY   O N   1 
ATOM   25891 C  CA  . GLY   O  1  167 ? 0.986   -224.499 36.558  1.00 120.16 ? 167 GLY   O CA  1 
ATOM   25892 C  C   . GLY   O  1  167 ? 0.233   -223.607 35.590  1.00 119.85 ? 167 GLY   O C   1 
ATOM   25893 O  O   . GLY   O  1  167 ? -1.003  -223.506 35.724  1.00 120.07 ? 167 GLY   O O   1 
ATOM   25894 N  N   . SER   O  1  168 ? 0.956   -222.988 34.649  1.00 116.00 ? 168 SER   O N   1 
ATOM   25895 C  CA  . SER   O  1  168 ? 0.421   -222.050 33.627  1.00 111.32 ? 168 SER   O CA  1 
ATOM   25896 C  C   . SER   O  1  168 ? -0.435  -222.810 32.607  1.00 113.72 ? 168 SER   O C   1 
ATOM   25897 O  O   . SER   O  1  168 ? -1.518  -222.299 32.255  1.00 110.17 ? 168 SER   O O   1 
ATOM   25898 C  CB  . SER   O  1  168 ? 1.533   -221.291 32.945  1.00 109.16 ? 168 SER   O CB  1 
ATOM   25899 O  OG  . SER   O  1  168 ? 2.459   -222.177 32.333  1.00 107.66 ? 168 SER   O OG  1 
ATOM   25900 N  N   . VAL   O  1  169 ? 0.027   -223.986 32.168  1.00 113.38 ? 169 VAL   O N   1 
ATOM   25901 C  CA  . VAL   O  1  169 ? -0.619  -224.792 31.088  1.00 113.66 ? 169 VAL   O CA  1 
ATOM   25902 C  C   . VAL   O  1  169 ? -2.063  -225.081 31.516  1.00 111.77 ? 169 VAL   O C   1 
ATOM   25903 O  O   . VAL   O  1  169 ? -2.976  -224.806 30.714  1.00 112.48 ? 169 VAL   O O   1 
ATOM   25904 C  CB  . VAL   O  1  169 ? 0.148   -226.093 30.773  1.00 113.18 ? 169 VAL   O CB  1 
ATOM   25905 C  CG1 . VAL   O  1  169 ? -0.382  -226.756 29.509  1.00 116.44 ? 169 VAL   O CG1 1 
ATOM   25906 C  CG2 . VAL   O  1  169 ? 1.650   -225.874 30.655  1.00 110.27 ? 169 VAL   O CG2 1 
ATOM   25907 N  N   . ALA   O  1  170 ? -2.254  -225.587 32.740  1.00 110.95 ? 170 ALA   O N   1 
ATOM   25908 C  CA  . ALA   O  1  170 ? -3.572  -225.954 33.315  1.00 115.24 ? 170 ALA   O CA  1 
ATOM   25909 C  C   . ALA   O  1  170 ? -4.405  -224.694 33.574  1.00 113.79 ? 170 ALA   O C   1 
ATOM   25910 O  O   . ALA   O  1  170 ? -5.618  -224.718 33.289  1.00 115.17 ? 170 ALA   O O   1 
ATOM   25911 C  CB  . ALA   O  1  170 ? -3.387  -226.751 34.582  1.00 117.04 ? 170 ALA   O CB  1 
ATOM   25912 N  N   . ALA   O  1  171 ? -3.777  -223.640 34.102  1.00 112.11 ? 171 ALA   O N   1 
ATOM   25913 C  CA  . ALA   O  1  171 ? -4.427  -222.352 34.443  1.00 112.60 ? 171 ALA   O CA  1 
ATOM   25914 C  C   . ALA   O  1  171 ? -4.994  -221.697 33.178  1.00 113.45 ? 171 ALA   O C   1 
ATOM   25915 O  O   . ALA   O  1  171 ? -6.145  -221.227 33.237  1.00 114.96 ? 171 ALA   O O   1 
ATOM   25916 C  CB  . ALA   O  1  171 ? -3.449  -221.443 35.143  1.00 110.74 ? 171 ALA   O CB  1 
ATOM   25917 N  N   . LYS   O  1  172 ? -4.222  -221.668 32.085  1.00 113.84 ? 172 LYS   O N   1 
ATOM   25918 C  CA  . LYS   O  1  172 ? -4.639  -221.064 30.787  1.00 116.50 ? 172 LYS   O CA  1 
ATOM   25919 C  C   . LYS   O  1  172 ? -5.887  -221.786 30.263  1.00 118.62 ? 172 LYS   O C   1 
ATOM   25920 O  O   . LYS   O  1  172 ? -6.829  -221.088 29.838  1.00 117.31 ? 172 LYS   O O   1 
ATOM   25921 C  CB  . LYS   O  1  172 ? -3.511  -221.106 29.749  1.00 117.63 ? 172 LYS   O CB  1 
ATOM   25922 C  CG  . LYS   O  1  172 ? -2.402  -220.078 29.945  1.00 117.34 ? 172 LYS   O CG  1 
ATOM   25923 C  CD  . LYS   O  1  172 ? -1.792  -219.561 28.651  1.00 117.50 ? 172 LYS   O CD  1 
ATOM   25924 C  CE  . LYS   O  1  172 ? -1.088  -220.627 27.837  1.00 119.00 ? 172 LYS   O CE  1 
ATOM   25925 N  NZ  . LYS   O  1  172 ? 0.195   -221.038 28.455  1.00 118.53 ? 172 LYS   O NZ  1 
ATOM   25926 N  N   . THR   O  1  173 ? -5.897  -223.124 30.295  1.00 120.87 ? 173 THR   O N   1 
ATOM   25927 C  CA  . THR   O  1  173 ? -7.047  -223.967 29.866  1.00 123.81 ? 173 THR   O CA  1 
ATOM   25928 C  C   . THR   O  1  173 ? -8.276  -223.631 30.720  1.00 120.98 ? 173 THR   O C   1 
ATOM   25929 O  O   . THR   O  1  173 ? -9.384  -223.566 30.151  1.00 121.93 ? 173 THR   O O   1 
ATOM   25930 C  CB  . THR   O  1  173 ? -6.742  -225.470 29.949  1.00 125.20 ? 173 THR   O CB  1 
ATOM   25931 O  OG1 . THR   O  1  173 ? -5.448  -225.720 29.399  1.00 128.61 ? 173 THR   O OG1 1 
ATOM   25932 C  CG2 . THR   O  1  173 ? -7.767  -226.308 29.215  1.00 126.24 ? 173 THR   O CG2 1 
ATOM   25933 N  N   . PHE   O  1  174 ? -8.087  -223.439 32.031  1.00 120.03 ? 174 PHE   O N   1 
ATOM   25934 C  CA  . PHE   O  1  174 ? -9.166  -223.075 32.987  1.00 122.40 ? 174 PHE   O CA  1 
ATOM   25935 C  C   . PHE   O  1  174 ? -9.752  -221.714 32.593  1.00 122.78 ? 174 PHE   O C   1 
ATOM   25936 O  O   . PHE   O  1  174 ? -10.990 -221.586 32.555  1.00 125.57 ? 174 PHE   O O   1 
ATOM   25937 C  CB  . PHE   O  1  174 ? -8.660  -223.055 34.433  1.00 122.83 ? 174 PHE   O CB  1 
ATOM   25938 C  CG  . PHE   O  1  174 ? -9.760  -222.991 35.463  1.00 125.50 ? 174 PHE   O CG  1 
ATOM   25939 C  CD1 . PHE   O  1  174 ? -10.357 -221.783 35.790  1.00 123.66 ? 174 PHE   O CD1 1 
ATOM   25940 C  CD2 . PHE   O  1  174 ? -10.214 -224.142 36.090  1.00 127.11 ? 174 PHE   O CD2 1 
ATOM   25941 C  CE1 . PHE   O  1  174 ? -11.378 -221.727 36.728  1.00 125.02 ? 174 PHE   O CE1 1 
ATOM   25942 C  CE2 . PHE   O  1  174 ? -11.233 -224.084 37.028  1.00 127.47 ? 174 PHE   O CE2 1 
ATOM   25943 C  CZ  . PHE   O  1  174 ? -11.813 -222.877 37.345  1.00 126.71 ? 174 PHE   O CZ  1 
ATOM   25944 N  N   . LEU   O  1  175 ? -8.886  -220.737 32.301  1.00 121.36 ? 175 LEU   O N   1 
ATOM   25945 C  CA  . LEU   O  1  175 ? -9.284  -219.343 31.964  1.00 121.63 ? 175 LEU   O CA  1 
ATOM   25946 C  C   . LEU   O  1  175 ? -10.059 -219.326 30.639  1.00 124.46 ? 175 LEU   O C   1 
ATOM   25947 O  O   . LEU   O  1  175 ? -10.999 -218.514 30.533  1.00 127.94 ? 175 LEU   O O   1 
ATOM   25948 C  CB  . LEU   O  1  175 ? -8.042  -218.444 31.901  1.00 118.51 ? 175 LEU   O CB  1 
ATOM   25949 C  CG  . LEU   O  1  175 ? -7.368  -218.132 33.240  1.00 114.42 ? 175 LEU   O CG  1 
ATOM   25950 C  CD1 . LEU   O  1  175 ? -6.056  -217.393 33.026  1.00 112.43 ? 175 LEU   O CD1 1 
ATOM   25951 C  CD2 . LEU   O  1  175 ? -8.282  -217.326 34.153  1.00 111.94 ? 175 LEU   O CD2 1 
ATOM   25952 N  N   . GLU   O  1  176 ? -9.699  -220.189 29.680  1.00 125.21 ? 176 GLU   O N   1 
ATOM   25953 C  CA  . GLU   O  1  176 ? -10.347 -220.260 28.339  1.00 126.57 ? 176 GLU   O CA  1 
ATOM   25954 C  C   . GLU   O  1  176 ? -11.822 -220.648 28.501  1.00 125.40 ? 176 GLU   O C   1 
ATOM   25955 O  O   . GLU   O  1  176 ? -12.663 -220.060 27.797  1.00 123.41 ? 176 GLU   O O   1 
ATOM   25956 C  CB  . GLU   O  1  176 ? -9.620  -221.242 27.416  1.00 130.36 ? 176 GLU   O CB  1 
ATOM   25957 C  CG  . GLU   O  1  176 ? -8.288  -220.717 26.909  1.00 131.76 ? 176 GLU   O CG  1 
ATOM   25958 C  CD  . GLU   O  1  176 ? -7.504  -221.681 26.034  1.00 135.61 ? 176 GLU   O CD  1 
ATOM   25959 O  OE1 . GLU   O  1  176 ? -8.137  -222.437 25.269  1.00 137.73 ? 176 GLU   O OE1 1 
ATOM   25960 O  OE2 . GLU   O  1  176 ? -6.261  -221.671 26.122  1.00 137.63 ? 176 GLU   O OE2 1 
ATOM   25961 N  N   . LYS   O  1  177 ? -12.121 -221.594 29.395  1.00 127.04 ? 177 LYS   O N   1 
ATOM   25962 C  CA  . LYS   O  1  177 ? -13.503 -222.083 29.658  1.00 130.52 ? 177 LYS   O CA  1 
ATOM   25963 C  C   . LYS   O  1  177 ? -14.347 -220.962 30.284  1.00 130.03 ? 177 LYS   O C   1 
ATOM   25964 O  O   . LYS   O  1  177 ? -15.548 -220.898 29.967  1.00 135.24 ? 177 LYS   O O   1 
ATOM   25965 C  CB  . LYS   O  1  177 ? -13.480 -223.331 30.548  1.00 132.68 ? 177 LYS   O CB  1 
ATOM   25966 C  CG  . LYS   O  1  177 ? -13.135 -224.626 29.823  1.00 133.24 ? 177 LYS   O CG  1 
ATOM   25967 C  CD  . LYS   O  1  177 ? -13.144 -225.851 30.711  1.00 135.59 ? 177 LYS   O CD  1 
ATOM   25968 C  CE  . LYS   O  1  177 ? -12.968 -227.138 29.932  1.00 136.56 ? 177 LYS   O CE  1 
ATOM   25969 N  NZ  . LYS   O  1  177 ? -12.700 -228.287 30.828  1.00 137.55 ? 177 LYS   O NZ  1 
ATOM   25970 N  N   . ARG   O  1  178 ? -13.749 -220.102 31.116  1.00 127.63 ? 178 ARG   O N   1 
ATOM   25971 C  CA  . ARG   O  1  178 ? -14.492 -219.159 31.999  1.00 132.97 ? 178 ARG   O CA  1 
ATOM   25972 C  C   . ARG   O  1  178 ? -14.547 -217.737 31.420  1.00 132.53 ? 178 ARG   O C   1 
ATOM   25973 O  O   . ARG   O  1  178 ? -15.480 -217.001 31.807  1.00 133.80 ? 178 ARG   O O   1 
ATOM   25974 C  CB  . ARG   O  1  178 ? -13.859 -219.108 33.391  1.00 134.81 ? 178 ARG   O CB  1 
ATOM   25975 C  CG  . ARG   O  1  178 ? -13.712 -220.463 34.069  1.00 139.23 ? 178 ARG   O CG  1 
ATOM   25976 C  CD  . ARG   O  1  178 ? -15.017 -221.231 34.165  1.00 147.28 ? 178 ARG   O CD  1 
ATOM   25977 N  NE  . ARG   O  1  178 ? -15.076 -222.050 35.370  1.00 151.48 ? 178 ARG   O NE  1 
ATOM   25978 C  CZ  . ARG   O  1  178 ? -15.597 -221.670 36.537  1.00 151.95 ? 178 ARG   O CZ  1 
ATOM   25979 N  NH1 . ARG   O  1  178 ? -16.124 -220.464 36.682  1.00 151.39 ? 178 ARG   O NH1 1 
ATOM   25980 N  NH2 . ARG   O  1  178 ? -15.590 -222.506 37.561  1.00 150.88 ? 178 ARG   O NH2 1 
ATOM   25981 N  N   . TRP   O  1  179 ? -13.600 -217.339 30.561  1.00 128.33 ? 179 TRP   O N   1 
ATOM   25982 C  CA  . TRP   O  1  179 ? -13.521 -215.948 30.035  1.00 127.68 ? 179 TRP   O CA  1 
ATOM   25983 C  C   . TRP   O  1  179 ? -14.566 -215.724 28.936  1.00 126.26 ? 179 TRP   O C   1 
ATOM   25984 O  O   . TRP   O  1  179 ? -14.638 -216.543 28.004  1.00 128.21 ? 179 TRP   O O   1 
ATOM   25985 C  CB  . TRP   O  1  179 ? -12.118 -215.591 29.527  1.00 126.70 ? 179 TRP   O CB  1 
ATOM   25986 C  CG  . TRP   O  1  179 ? -11.944 -214.117 29.308  1.00 126.65 ? 179 TRP   O CG  1 
ATOM   25987 C  CD1 . TRP   O  1  179 ? -11.492 -213.204 30.217  1.00 125.78 ? 179 TRP   O CD1 1 
ATOM   25988 C  CD2 . TRP   O  1  179 ? -12.257 -213.370 28.116  1.00 127.90 ? 179 TRP   O CD2 1 
ATOM   25989 N  NE1 . TRP   O  1  179 ? -11.488 -211.949 29.672  1.00 124.22 ? 179 TRP   O NE1 1 
ATOM   25990 C  CE2 . TRP   O  1  179 ? -11.953 -212.017 28.386  1.00 125.74 ? 179 TRP   O CE2 1 
ATOM   25991 C  CE3 . TRP   O  1  179 ? -12.756 -213.708 26.852  1.00 129.30 ? 179 TRP   O CE3 1 
ATOM   25992 C  CZ2 . TRP   O  1  179 ? -12.129 -211.011 27.436  1.00 124.82 ? 179 TRP   O CZ2 1 
ATOM   25993 C  CZ3 . TRP   O  1  179 ? -12.932 -212.711 25.915  1.00 127.48 ? 179 TRP   O CZ3 1 
ATOM   25994 C  CH2 . TRP   O  1  179 ? -12.619 -211.383 26.205  1.00 126.42 ? 179 TRP   O CH2 1 
ATOM   25995 N  N   . ASN   O  1  180 ? -15.327 -214.632 29.054  1.00 127.26 ? 180 ASN   O N   1 
ATOM   25996 C  CA  . ASN   O  1  180 ? -16.169 -214.044 27.976  1.00 129.79 ? 180 ASN   O CA  1 
ATOM   25997 C  C   . ASN   O  1  180 ? -15.888 -212.535 27.928  1.00 127.92 ? 180 ASN   O C   1 
ATOM   25998 O  O   . ASN   O  1  180 ? -15.237 -212.028 28.866  1.00 121.60 ? 180 ASN   O O   1 
ATOM   25999 C  CB  . ASN   O  1  180 ? -17.653 -214.370 28.173  1.00 131.85 ? 180 ASN   O CB  1 
ATOM   26000 C  CG  . ASN   O  1  180 ? -18.208 -213.872 29.492  1.00 129.21 ? 180 ASN   O CG  1 
ATOM   26001 O  OD1 . ASN   O  1  180 ? -18.423 -212.676 29.671  1.00 127.28 ? 180 ASN   O OD1 1 
ATOM   26002 N  ND2 . ASN   O  1  180 ? -18.458 -214.780 30.421  1.00 131.84 ? 180 ASN   O ND2 1 
ATOM   26003 N  N   . ASP   O  1  181 ? -16.365 -211.847 26.885  1.00 131.73 ? 181 ASP   O N   1 
ATOM   26004 C  CA  . ASP   O  1  181 ? -16.085 -210.404 26.639  1.00 130.77 ? 181 ASP   O CA  1 
ATOM   26005 C  C   . ASP   O  1  181 ? -17.074 -209.517 27.415  1.00 132.13 ? 181 ASP   O C   1 
ATOM   26006 O  O   . ASP   O  1  181 ? -17.030 -208.286 27.210  1.00 130.47 ? 181 ASP   O O   1 
ATOM   26007 C  CB  . ASP   O  1  181 ? -16.083 -210.086 25.139  1.00 138.03 ? 181 ASP   O CB  1 
ATOM   26008 C  CG  . ASP   O  1  181 ? -17.400 -210.336 24.421  1.00 143.38 ? 181 ASP   O CG  1 
ATOM   26009 O  OD1 . ASP   O  1  181 ? -18.378 -210.726 25.091  1.00 149.86 ? 181 ASP   O OD1 1 
ATOM   26010 O  OD2 . ASP   O  1  181 ? -17.434 -210.143 23.190  1.00 153.37 ? 181 ASP   O OD2 1 
ATOM   26011 N  N   . GLU   O  1  182 ? -17.914 -210.104 28.279  1.00 131.03 ? 182 GLU   O N   1 
ATOM   26012 C  CA  . GLU   O  1  182 ? -18.942 -209.387 29.086  1.00 132.73 ? 182 GLU   O CA  1 
ATOM   26013 C  C   . GLU   O  1  182 ? -18.648 -209.523 30.588  1.00 129.36 ? 182 GLU   O C   1 
ATOM   26014 O  O   . GLU   O  1  182 ? -19.538 -209.169 31.387  1.00 127.10 ? 182 GLU   O O   1 
ATOM   26015 C  CB  . GLU   O  1  182 ? -20.336 -209.930 28.760  1.00 135.40 ? 182 GLU   O CB  1 
ATOM   26016 C  CG  . GLU   O  1  182 ? -20.989 -209.255 27.567  1.00 137.51 ? 182 GLU   O CG  1 
ATOM   26017 C  CD  . GLU   O  1  182 ? -22.141 -210.031 26.952  1.00 140.88 ? 182 GLU   O CD  1 
ATOM   26018 O  OE1 . GLU   O  1  182 ? -21.893 -211.131 26.419  1.00 145.48 ? 182 GLU   O OE1 1 
ATOM   26019 O  OE2 . GLU   O  1  182 ? -23.284 -209.537 27.014  1.00 143.98 ? 182 GLU   O OE2 1 
ATOM   26020 N  N   . LEU   O  1  183 ? -17.457 -210.001 30.968  1.00 128.17 ? 183 LEU   O N   1 
ATOM   26021 C  CA  . LEU   O  1  183 ? -17.065 -210.166 32.396  1.00 129.40 ? 183 LEU   O CA  1 
ATOM   26022 C  C   . LEU   O  1  183 ? -16.978 -208.787 33.056  1.00 127.76 ? 183 LEU   O C   1 
ATOM   26023 O  O   . LEU   O  1  183 ? -16.320 -207.897 32.485  1.00 127.66 ? 183 LEU   O O   1 
ATOM   26024 C  CB  . LEU   O  1  183 ? -15.721 -210.894 32.511  1.00 129.31 ? 183 LEU   O CB  1 
ATOM   26025 C  CG  . LEU   O  1  183 ? -15.745 -212.406 32.295  1.00 130.66 ? 183 LEU   O CG  1 
ATOM   26026 C  CD1 . LEU   O  1  183 ? -14.332 -212.965 32.356  1.00 128.11 ? 183 LEU   O CD1 1 
ATOM   26027 C  CD2 . LEU   O  1  183 ? -16.631 -213.107 33.316  1.00 131.70 ? 183 LEU   O CD2 1 
ATOM   26028 N  N   . GLU   O  1  184 ? -17.628 -208.637 34.212  1.00 130.04 ? 184 GLU   O N   1 
ATOM   26029 C  CA  . GLU   O  1  184 ? -17.519 -207.456 35.106  1.00 130.17 ? 184 GLU   O CA  1 
ATOM   26030 C  C   . GLU   O  1  184 ? -16.335 -207.707 36.048  1.00 130.21 ? 184 GLU   O C   1 
ATOM   26031 O  O   . GLU   O  1  184 ? -16.003 -208.889 36.255  1.00 131.25 ? 184 GLU   O O   1 
ATOM   26032 C  CB  . GLU   O  1  184 ? -18.851 -207.253 35.832  1.00 134.58 ? 184 GLU   O CB  1 
ATOM   26033 C  CG  . GLU   O  1  184 ? -19.100 -205.825 36.282  1.00 137.89 ? 184 GLU   O CG  1 
ATOM   26034 C  CD  . GLU   O  1  184 ? -18.835 -205.576 37.757  1.00 141.20 ? 184 GLU   O CD  1 
ATOM   26035 O  OE1 . GLU   O  1  184 ? -19.346 -206.357 38.588  1.00 143.51 ? 184 GLU   O OE1 1 
ATOM   26036 O  OE2 . GLU   O  1  184 ? -18.118 -204.604 38.071  1.00 144.37 ? 184 GLU   O OE2 1 
ATOM   26037 N  N   . LEU   O  1  185 ? -15.710 -206.649 36.577  1.00 127.43 ? 185 LEU   O N   1 
ATOM   26038 C  CA  . LEU   O  1  185 ? -14.449 -206.739 37.367  1.00 128.62 ? 185 LEU   O CA  1 
ATOM   26039 C  C   . LEU   O  1  185 ? -14.607 -207.750 38.510  1.00 127.95 ? 185 LEU   O C   1 
ATOM   26040 O  O   . LEU   O  1  185 ? -13.650 -208.510 38.746  1.00 131.16 ? 185 LEU   O O   1 
ATOM   26041 C  CB  . LEU   O  1  185 ? -14.071 -205.357 37.910  1.00 126.87 ? 185 LEU   O CB  1 
ATOM   26042 C  CG  . LEU   O  1  185 ? -12.792 -205.303 38.749  1.00 128.11 ? 185 LEU   O CG  1 
ATOM   26043 C  CD1 . LEU   O  1  185 ? -11.603 -205.876 37.989  1.00 126.28 ? 185 LEU   O CD1 1 
ATOM   26044 C  CD2 . LEU   O  1  185 ? -12.497 -203.879 39.199  1.00 127.77 ? 185 LEU   O CD2 1 
ATOM   26045 N  N   . GLU   O  1  186 ? -15.760 -207.758 39.189  1.00 131.05 ? 186 GLU   O N   1 
ATOM   26046 C  CA  . GLU   O  1  186 ? -16.040 -208.668 40.335  1.00 133.79 ? 186 GLU   O CA  1 
ATOM   26047 C  C   . GLU   O  1  186 ? -16.089 -210.123 39.852  1.00 132.20 ? 186 GLU   O C   1 
ATOM   26048 O  O   . GLU   O  1  186 ? -15.671 -211.006 40.624  1.00 133.18 ? 186 GLU   O O   1 
ATOM   26049 C  CB  . GLU   O  1  186 ? -17.338 -208.277 41.048  1.00 137.52 ? 186 GLU   O CB  1 
ATOM   26050 C  CG  . GLU   O  1  186 ? -17.132 -207.255 42.153  1.00 138.73 ? 186 GLU   O CG  1 
ATOM   26051 C  CD  . GLU   O  1  186 ? -16.325 -207.746 43.345  1.00 138.83 ? 186 GLU   O CD  1 
ATOM   26052 O  OE1 . GLU   O  1  186 ? -15.991 -208.949 43.389  1.00 141.45 ? 186 GLU   O OE1 1 
ATOM   26053 O  OE2 . GLU   O  1  186 ? -16.029 -206.920 44.229  1.00 142.18 ? 186 GLU   O OE2 1 
ATOM   26054 N  N   . ASP   O  1  187 ? -16.572 -210.357 38.627  1.00 133.18 ? 187 ASP   O N   1 
ATOM   26055 C  CA  . ASP   O  1  187 ? -16.652 -211.704 38.000  1.00 134.55 ? 187 ASP   O CA  1 
ATOM   26056 C  C   . ASP   O  1  187 ? -15.236 -212.186 37.655  1.00 131.43 ? 187 ASP   O C   1 
ATOM   26057 O  O   . ASP   O  1  187 ? -14.993 -213.404 37.759  1.00 133.60 ? 187 ASP   O O   1 
ATOM   26058 C  CB  . ASP   O  1  187 ? -17.570 -211.696 36.773  1.00 138.46 ? 187 ASP   O CB  1 
ATOM   26059 C  CG  . ASP   O  1  187 ? -18.992 -211.241 37.067  1.00 140.61 ? 187 ASP   O CG  1 
ATOM   26060 O  OD1 . ASP   O  1  187 ? -19.511 -211.593 38.146  1.00 147.40 ? 187 ASP   O OD1 1 
ATOM   26061 O  OD2 . ASP   O  1  187 ? -19.569 -210.533 36.217  1.00 135.76 ? 187 ASP   O OD2 1 
ATOM   26062 N  N   . ALA   O  1  188 ? -14.342 -211.267 37.269  1.00 127.80 ? 188 ALA   O N   1 
ATOM   26063 C  CA  . ALA   O  1  188 ? -12.929 -211.551 36.915  1.00 126.05 ? 188 ALA   O CA  1 
ATOM   26064 C  C   . ALA   O  1  188 ? -12.126 -211.888 38.178  1.00 123.92 ? 188 ALA   O C   1 
ATOM   26065 O  O   . ALA   O  1  188 ? -11.270 -212.789 38.096  1.00 128.95 ? 188 ALA   O O   1 
ATOM   26066 C  CB  . ALA   O  1  188 ? -12.324 -210.383 36.175  1.00 124.34 ? 188 ALA   O CB  1 
ATOM   26067 N  N   . ILE   O  1  189 ? -12.382 -211.191 39.294  1.00 122.77 ? 189 ILE   O N   1 
ATOM   26068 C  CA  . ILE   O  1  189 ? -11.723 -211.447 40.613  1.00 121.67 ? 189 ILE   O CA  1 
ATOM   26069 C  C   . ILE   O  1  189 ? -12.097 -212.860 41.075  1.00 122.12 ? 189 ILE   O C   1 
ATOM   26070 O  O   . ILE   O  1  189 ? -11.201 -213.583 41.549  1.00 123.33 ? 189 ILE   O O   1 
ATOM   26071 C  CB  . ILE   O  1  189 ? -12.111 -210.391 41.671  1.00 121.26 ? 189 ILE   O CB  1 
ATOM   26072 C  CG1 . ILE   O  1  189 ? -11.618 -208.990 41.298  1.00 118.34 ? 189 ILE   O CG1 1 
ATOM   26073 C  CG2 . ILE   O  1  189 ? -11.608 -210.804 43.048  1.00 121.01 ? 189 ILE   O CG2 1 
ATOM   26074 C  CD1 . ILE   O  1  189 ? -12.264 -207.881 42.096  1.00 118.34 ? 189 ILE   O CD1 1 
ATOM   26075 N  N   . HIS   O  1  190 ? -13.378 -213.220 40.951  1.00 122.98 ? 190 HIS   O N   1 
ATOM   26076 C  CA  . HIS   O  1  190 ? -13.935 -214.542 41.343  1.00 124.63 ? 190 HIS   O CA  1 
ATOM   26077 C  C   . HIS   O  1  190 ? -13.201 -215.656 40.587  1.00 123.80 ? 190 HIS   O C   1 
ATOM   26078 O  O   . HIS   O  1  190 ? -12.831 -216.654 41.235  1.00 124.04 ? 190 HIS   O O   1 
ATOM   26079 C  CB  . HIS   O  1  190 ? -15.451 -214.580 41.103  1.00 126.06 ? 190 HIS   O CB  1 
ATOM   26080 C  CG  . HIS   O  1  190 ? -16.060 -215.906 41.405  1.00 127.76 ? 190 HIS   O CG  1 
ATOM   26081 N  ND1 . HIS   O  1  190 ? -16.281 -216.337 42.697  1.00 128.69 ? 190 HIS   O ND1 1 
ATOM   26082 C  CD2 . HIS   O  1  190 ? -16.477 -216.902 40.593  1.00 127.10 ? 190 HIS   O CD2 1 
ATOM   26083 C  CE1 . HIS   O  1  190 ? -16.819 -217.539 42.669  1.00 129.79 ? 190 HIS   O CE1 1 
ATOM   26084 N  NE2 . HIS   O  1  190 ? -16.950 -217.907 41.389  1.00 129.09 ? 190 HIS   O NE2 1 
ATOM   26085 N  N   . ILE   O  1  191 ? -12.994 -215.478 39.276  1.00 123.89 ? 191 ILE   O N   1 
ATOM   26086 C  CA  . ILE   O  1  191 ? -12.337 -216.474 38.374  1.00 122.72 ? 191 ILE   O CA  1 
ATOM   26087 C  C   . ILE   O  1  191 ? -10.841 -216.538 38.708  1.00 121.35 ? 191 ILE   O C   1 
ATOM   26088 O  O   . ILE   O  1  191 ? -10.285 -217.652 38.678  1.00 121.56 ? 191 ILE   O O   1 
ATOM   26089 C  CB  . ILE   O  1  191 ? -12.595 -216.141 36.888  1.00 121.77 ? 191 ILE   O CB  1 
ATOM   26090 C  CG1 . ILE   O  1  191 ? -14.084 -216.250 36.544  1.00 123.14 ? 191 ILE   O CG1 1 
ATOM   26091 C  CG2 . ILE   O  1  191 ? -11.751 -217.019 35.973  1.00 121.34 ? 191 ILE   O CG2 1 
ATOM   26092 C  CD1 . ILE   O  1  191 ? -14.488 -215.508 35.292  1.00 123.50 ? 191 ILE   O CD1 1 
ATOM   26093 N  N   . ALA   O  1  192 ? -10.221 -215.394 39.014  1.00 118.94 ? 192 ALA   O N   1 
ATOM   26094 C  CA  . ALA   O  1  192 ? -8.790  -215.283 39.387  1.00 118.91 ? 192 ALA   O CA  1 
ATOM   26095 C  C   . ALA   O  1  192 ? -8.510  -216.130 40.633  1.00 119.72 ? 192 ALA   O C   1 
ATOM   26096 O  O   . ALA   O  1  192 ? -7.469  -216.812 40.656  1.00 120.67 ? 192 ALA   O O   1 
ATOM   26097 C  CB  . ALA   O  1  192 ? -8.412  -213.839 39.611  1.00 117.10 ? 192 ALA   O CB  1 
ATOM   26098 N  N   . LEU   O  1  193 ? -9.408  -216.087 41.624  1.00 122.75 ? 193 LEU   O N   1 
ATOM   26099 C  CA  . LEU   O  1  193 ? -9.283  -216.842 42.901  1.00 127.15 ? 193 LEU   O CA  1 
ATOM   26100 C  C   . LEU   O  1  193 ? -9.493  -218.342 42.648  1.00 129.15 ? 193 LEU   O C   1 
ATOM   26101 O  O   . LEU   O  1  193 ? -8.741  -219.144 43.236  1.00 131.06 ? 193 LEU   O O   1 
ATOM   26102 C  CB  . LEU   O  1  193 ? -10.298 -216.305 43.916  1.00 131.07 ? 193 LEU   O CB  1 
ATOM   26103 C  CG  . LEU   O  1  193 ? -10.008 -214.909 44.468  1.00 130.68 ? 193 LEU   O CG  1 
ATOM   26104 C  CD1 . LEU   O  1  193 ? -11.220 -214.362 45.206  1.00 134.50 ? 193 LEU   O CD1 1 
ATOM   26105 C  CD2 . LEU   O  1  193 ? -8.789  -214.919 45.381  1.00 128.64 ? 193 LEU   O CD2 1 
ATOM   26106 N  N   . LEU   O  1  194 ? -10.479 -218.704 41.819  1.00 130.74 ? 194 LEU   O N   1 
ATOM   26107 C  CA  . LEU   O  1  194 ? -10.763 -220.114 41.427  1.00 129.34 ? 194 LEU   O CA  1 
ATOM   26108 C  C   . LEU   O  1  194 ? -9.530  -220.707 40.736  1.00 125.75 ? 194 LEU   O C   1 
ATOM   26109 O  O   . LEU   O  1  194 ? -9.107  -221.808 41.138  1.00 124.27 ? 194 LEU   O O   1 
ATOM   26110 C  CB  . LEU   O  1  194 ? -11.980 -220.169 40.497  1.00 130.74 ? 194 LEU   O CB  1 
ATOM   26111 C  CG  . LEU   O  1  194 ? -13.347 -220.195 41.180  1.00 134.18 ? 194 LEU   O CG  1 
ATOM   26112 C  CD1 . LEU   O  1  194 ? -14.447 -219.851 40.188  1.00 135.89 ? 194 LEU   O CD1 1 
ATOM   26113 C  CD2 . LEU   O  1  194 ? -13.617 -221.551 41.817  1.00 136.04 ? 194 LEU   O CD2 1 
ATOM   26114 N  N   . THR   O  1  195 ? -8.981  -220.000 39.741  1.00 123.80 ? 195 THR   O N   1 
ATOM   26115 C  CA  . THR   O  1  195 ? -7.852  -220.461 38.887  1.00 122.21 ? 195 THR   O CA  1 
ATOM   26116 C  C   . THR   O  1  195 ? -6.593  -220.658 39.737  1.00 121.87 ? 195 THR   O C   1 
ATOM   26117 O  O   . THR   O  1  195 ? -5.832  -221.601 39.447  1.00 123.05 ? 195 THR   O O   1 
ATOM   26118 C  CB  . THR   O  1  195 ? -7.546  -219.480 37.749  1.00 120.57 ? 195 THR   O CB  1 
ATOM   26119 O  OG1 . THR   O  1  195 ? -8.775  -219.105 37.128  1.00 123.38 ? 195 THR   O OG1 1 
ATOM   26120 C  CG2 . THR   O  1  195 ? -6.612  -220.070 36.714  1.00 119.41 ? 195 THR   O CG2 1 
ATOM   26121 N  N   . LEU   O  1  196 ? -6.379  -219.794 40.732  1.00 122.66 ? 196 LEU   O N   1 
ATOM   26122 C  CA  . LEU   O  1  196 ? -5.147  -219.781 41.565  1.00 126.27 ? 196 LEU   O CA  1 
ATOM   26123 C  C   . LEU   O  1  196 ? -5.176  -220.960 42.545  1.00 122.98 ? 196 LEU   O C   1 
ATOM   26124 O  O   . LEU   O  1  196 ? -4.095  -221.511 42.814  1.00 127.53 ? 196 LEU   O O   1 
ATOM   26125 C  CB  . LEU   O  1  196 ? -5.040  -218.437 42.296  1.00 128.89 ? 196 LEU   O CB  1 
ATOM   26126 C  CG  . LEU   O  1  196 ? -3.626  -217.958 42.634  1.00 128.58 ? 196 LEU   O CG  1 
ATOM   26127 C  CD1 . LEU   O  1  196 ? -2.728  -217.922 41.404  1.00 129.30 ? 196 LEU   O CD1 1 
ATOM   26128 C  CD2 . LEU   O  1  196 ? -3.677  -216.584 43.283  1.00 125.46 ? 196 LEU   O CD2 1 
ATOM   26129 N  N   . LYS   O  1  197 ? -6.362  -221.343 43.036  1.00 122.46 ? 197 LYS   O N   1 
ATOM   26130 C  CA  . LYS   O  1  197 ? -6.547  -222.456 44.008  1.00 123.68 ? 197 LYS   O CA  1 
ATOM   26131 C  C   . LYS   O  1  197 ? -6.011  -223.768 43.417  1.00 124.91 ? 197 LYS   O C   1 
ATOM   26132 O  O   . LYS   O  1  197 ? -5.464  -224.569 44.196  1.00 128.83 ? 197 LYS   O O   1 
ATOM   26133 C  CB  . LYS   O  1  197 ? -8.019  -222.605 44.405  1.00 124.29 ? 197 LYS   O CB  1 
ATOM   26134 C  CG  . LYS   O  1  197 ? -8.280  -223.630 45.501  1.00 127.65 ? 197 LYS   O CG  1 
ATOM   26135 C  CD  . LYS   O  1  197 ? -9.740  -223.808 45.845  1.00 130.56 ? 197 LYS   O CD  1 
ATOM   26136 C  CE  . LYS   O  1  197 ? -10.261 -222.743 46.784  1.00 131.79 ? 197 LYS   O CE  1 
ATOM   26137 N  NZ  . LYS   O  1  197 ? -11.631 -223.060 47.251  1.00 135.40 ? 197 LYS   O NZ  1 
ATOM   26138 N  N   . GLU   O  1  198 ? -6.161  -223.979 42.104  1.00 125.32 ? 198 GLU   O N   1 
ATOM   26139 C  CA  . GLU   O  1  198 ? -5.715  -225.211 41.393  1.00 132.04 ? 198 GLU   O CA  1 
ATOM   26140 C  C   . GLU   O  1  198 ? -4.194  -225.370 41.539  1.00 133.77 ? 198 GLU   O C   1 
ATOM   26141 O  O   . GLU   O  1  198 ? -3.744  -226.511 41.783  1.00 133.53 ? 198 GLU   O O   1 
ATOM   26142 C  CB  . GLU   O  1  198 ? -6.099  -225.172 39.910  1.00 133.41 ? 198 GLU   O CB  1 
ATOM   26143 C  CG  . GLU   O  1  198 ? -7.591  -225.054 39.652  1.00 137.89 ? 198 GLU   O CG  1 
ATOM   26144 C  CD  . GLU   O  1  198 ? -8.425  -226.226 40.137  1.00 145.38 ? 198 GLU   O CD  1 
ATOM   26145 O  OE1 . GLU   O  1  198 ? -8.237  -227.342 39.612  1.00 159.14 ? 198 GLU   O OE1 1 
ATOM   26146 O  OE2 . GLU   O  1  198 ? -9.259  -226.018 41.040  1.00 150.37 ? 198 GLU   O OE2 1 
ATOM   26147 N  N   . SER   O  1  199 ? -3.440  -224.272 41.401  1.00 136.01 ? 199 SER   O N   1 
ATOM   26148 C  CA  . SER   O  1  199 ? -1.951  -224.246 41.389  1.00 139.10 ? 199 SER   O CA  1 
ATOM   26149 C  C   . SER   O  1  199 ? -1.379  -224.086 42.807  1.00 139.00 ? 199 SER   O C   1 
ATOM   26150 O  O   . SER   O  1  199 ? -0.182  -224.388 42.981  1.00 138.00 ? 199 SER   O O   1 
ATOM   26151 C  CB  . SER   O  1  199 ? -1.427  -223.170 40.465  1.00 140.53 ? 199 SER   O CB  1 
ATOM   26152 O  OG  . SER   O  1  199 ? -1.995  -221.905 40.773  1.00 138.80 ? 199 SER   O OG  1 
ATOM   26153 N  N   . VAL   O  1  200 ? -2.182  -223.626 43.776  1.00 139.97 ? 200 VAL   O N   1 
ATOM   26154 C  CA  . VAL   O  1  200 ? -1.758  -223.469 45.202  1.00 143.62 ? 200 VAL   O CA  1 
ATOM   26155 C  C   . VAL   O  1  200 ? -2.020  -224.789 45.934  1.00 143.24 ? 200 VAL   O C   1 
ATOM   26156 O  O   . VAL   O  1  200 ? -3.118  -225.353 45.763  1.00 147.05 ? 200 VAL   O O   1 
ATOM   26157 C  CB  . VAL   O  1  200 ? -2.468  -222.293 45.903  1.00 142.91 ? 200 VAL   O CB  1 
ATOM   26158 C  CG1 . VAL   O  1  200 ? -2.102  -222.218 47.379  1.00 145.59 ? 200 VAL   O CG1 1 
ATOM   26159 C  CG2 . VAL   O  1  200 ? -2.173  -220.966 45.221  1.00 142.54 ? 200 VAL   O CG2 1 
ATOM   26160 N  N   . GLU   O  1  201 ? -1.052  -225.242 46.736  1.00 145.74 ? 201 GLU   O N   1 
ATOM   26161 C  CA  . GLU   O  1  201 ? -1.077  -226.564 47.415  1.00 148.62 ? 201 GLU   O CA  1 
ATOM   26162 C  C   . GLU   O  1  201 ? -1.465  -226.385 48.886  1.00 148.91 ? 201 GLU   O C   1 
ATOM   26163 O  O   . GLU   O  1  201 ? -2.435  -227.037 49.319  1.00 155.57 ? 201 GLU   O O   1 
ATOM   26164 C  CB  . GLU   O  1  201 ? 0.283   -227.250 47.281  1.00 154.31 ? 201 GLU   O CB  1 
ATOM   26165 C  CG  . GLU   O  1  201 ? 0.222   -228.749 47.512  1.00 156.79 ? 201 GLU   O CG  1 
ATOM   26166 C  CD  . GLU   O  1  201 ? 1.200   -229.551 46.673  1.00 162.29 ? 201 GLU   O CD  1 
ATOM   26167 O  OE1 . GLU   O  1  201 ? 0.767   -230.539 46.049  1.00 166.51 ? 201 GLU   O OE1 1 
ATOM   26168 O  OE2 . GLU   O  1  201 ? 2.390   -229.183 46.644  1.00 171.08 ? 201 GLU   O OE2 1 
ATOM   26169 N  N   . GLY   O  1  202 ? -0.737  -225.534 49.616  1.00 145.71 ? 202 GLY   O N   1 
ATOM   26170 C  CA  . GLY   O  1  202 ? -0.880  -225.353 51.074  1.00 143.11 ? 202 GLY   O CA  1 
ATOM   26171 C  C   . GLY   O  1  202 ? -2.052  -224.454 51.430  1.00 140.13 ? 202 GLY   O C   1 
ATOM   26172 O  O   . GLY   O  1  202 ? -3.155  -224.670 50.888  1.00 131.32 ? 202 GLY   O O   1 
ATOM   26173 N  N   . GLU   O  1  203 ? -1.819  -223.478 52.313  1.00 141.72 ? 203 GLU   O N   1 
ATOM   26174 C  CA  . GLU   O  1  203 ? -2.852  -222.531 52.816  1.00 145.48 ? 203 GLU   O CA  1 
ATOM   26175 C  C   . GLU   O  1  203 ? -3.315  -221.636 51.663  1.00 147.23 ? 203 GLU   O C   1 
ATOM   26176 O  O   . GLU   O  1  203 ? -2.449  -221.174 50.891  1.00 149.97 ? 203 GLU   O O   1 
ATOM   26177 C  CB  . GLU   O  1  203 ? -2.301  -221.670 53.955  1.00 146.45 ? 203 GLU   O CB  1 
ATOM   26178 C  CG  . GLU   O  1  203 ? -1.773  -222.458 55.141  1.00 150.03 ? 203 GLU   O CG  1 
ATOM   26179 C  CD  . GLU   O  1  203 ? -2.829  -223.180 55.960  1.00 152.76 ? 203 GLU   O CD  1 
ATOM   26180 O  OE1 . GLU   O  1  203 ? -2.971  -222.853 57.154  1.00 163.60 ? 203 GLU   O OE1 1 
ATOM   26181 O  OE2 . GLU   O  1  203 ? -3.498  -224.076 55.410  1.00 156.96 ? 203 GLU   O OE2 1 
ATOM   26182 N  N   . PHE   O  1  204 ? -4.627  -221.406 51.557  1.00 144.67 ? 204 PHE   O N   1 
ATOM   26183 C  CA  . PHE   O  1  204 ? -5.260  -220.522 50.541  1.00 142.67 ? 204 PHE   O CA  1 
ATOM   26184 C  C   . PHE   O  1  204 ? -6.138  -219.492 51.260  1.00 140.95 ? 204 PHE   O C   1 
ATOM   26185 O  O   . PHE   O  1  204 ? -7.327  -219.774 51.514  1.00 141.77 ? 204 PHE   O O   1 
ATOM   26186 C  CB  . PHE   O  1  204 ? -6.044  -221.347 49.516  1.00 139.69 ? 204 PHE   O CB  1 
ATOM   26187 C  CG  . PHE   O  1  204 ? -6.359  -220.604 48.242  1.00 138.84 ? 204 PHE   O CG  1 
ATOM   26188 C  CD1 . PHE   O  1  204 ? -5.359  -220.330 47.322  1.00 136.30 ? 204 PHE   O CD1 1 
ATOM   26189 C  CD2 . PHE   O  1  204 ? -7.647  -220.170 47.964  1.00 139.04 ? 204 PHE   O CD2 1 
ATOM   26190 C  CE1 . PHE   O  1  204 ? -5.639  -219.643 46.151  1.00 134.05 ? 204 PHE   O CE1 1 
ATOM   26191 C  CE2 . PHE   O  1  204 ? -7.926  -219.482 46.793  1.00 138.12 ? 204 PHE   O CE2 1 
ATOM   26192 C  CZ  . PHE   O  1  204 ? -6.921  -219.220 45.889  1.00 134.08 ? 204 PHE   O CZ  1 
ATOM   26193 N  N   . ASN   O  1  205 ? -5.552  -218.335 51.586  1.00 139.82 ? 205 ASN   O N   1 
ATOM   26194 C  CA  . ASN   O  1  205 ? -6.214  -217.220 52.318  1.00 137.19 ? 205 ASN   O CA  1 
ATOM   26195 C  C   . ASN   O  1  205 ? -5.596  -215.887 51.874  1.00 132.30 ? 205 ASN   O C   1 
ATOM   26196 O  O   . ASN   O  1  205 ? -4.713  -215.910 50.994  1.00 130.41 ? 205 ASN   O O   1 
ATOM   26197 C  CB  . ASN   O  1  205 ? -6.129  -217.430 53.833  1.00 138.70 ? 205 ASN   O CB  1 
ATOM   26198 C  CG  . ASN   O  1  205 ? -4.714  -217.653 54.327  1.00 136.09 ? 205 ASN   O CG  1 
ATOM   26199 O  OD1 . ASN   O  1  205 ? -3.802  -216.908 53.976  1.00 132.00 ? 205 ASN   O OD1 1 
ATOM   26200 N  ND2 . ASN   O  1  205 ? -4.520  -218.671 55.148  1.00 139.14 ? 205 ASN   O ND2 1 
ATOM   26201 N  N   . GLY   O  1  206 ? -6.036  -214.775 52.475  1.00 129.45 ? 206 GLY   O N   1 
ATOM   26202 C  CA  . GLY   O  1  206 ? -5.612  -213.405 52.122  1.00 125.76 ? 206 GLY   O CA  1 
ATOM   26203 C  C   . GLY   O  1  206 ? -4.176  -213.097 52.519  1.00 125.16 ? 206 GLY   O C   1 
ATOM   26204 O  O   . GLY   O  1  206 ? -3.678  -212.027 52.111  1.00 124.02 ? 206 GLY   O O   1 
ATOM   26205 N  N   . ASP   O  1  207 ? -3.530  -213.978 53.291  1.00 123.74 ? 207 ASP   O N   1 
ATOM   26206 C  CA  . ASP   O  1  207 ? -2.135  -213.804 53.781  1.00 123.98 ? 207 ASP   O CA  1 
ATOM   26207 C  C   . ASP   O  1  207 ? -1.153  -214.567 52.880  1.00 123.48 ? 207 ASP   O C   1 
ATOM   26208 O  O   . ASP   O  1  207 ? 0.046   -214.225 52.913  1.00 121.17 ? 207 ASP   O O   1 
ATOM   26209 C  CB  . ASP   O  1  207 ? -2.017  -214.242 55.244  1.00 125.87 ? 207 ASP   O CB  1 
ATOM   26210 C  CG  . ASP   O  1  207 ? -2.830  -213.385 56.203  1.00 124.70 ? 207 ASP   O CG  1 
ATOM   26211 O  OD1 . ASP   O  1  207 ? -2.622  -212.155 56.213  1.00 121.91 ? 207 ASP   O OD1 1 
ATOM   26212 O  OD2 . ASP   O  1  207 ? -3.672  -213.952 56.926  1.00 127.18 ? 207 ASP   O OD2 1 
ATOM   26213 N  N   . THR   O  1  208 ? -1.631  -215.559 52.117  1.00 124.24 ? 208 THR   O N   1 
ATOM   26214 C  CA  . THR   O  1  208 ? -0.816  -216.394 51.190  1.00 123.30 ? 208 THR   O CA  1 
ATOM   26215 C  C   . THR   O  1  208 ? -1.071  -215.992 49.733  1.00 120.88 ? 208 THR   O C   1 
ATOM   26216 O  O   . THR   O  1  208 ? -0.310  -216.456 48.863  1.00 117.59 ? 208 THR   O O   1 
ATOM   26217 C  CB  . THR   O  1  208 ? -1.103  -217.886 51.392  1.00 123.65 ? 208 THR   O CB  1 
ATOM   26218 O  OG1 . THR   O  1  208 ? -2.512  -218.092 51.278  1.00 123.86 ? 208 THR   O OG1 1 
ATOM   26219 C  CG2 . THR   O  1  208 ? -0.612  -218.389 52.730  1.00 125.84 ? 208 THR   O CG2 1 
ATOM   26220 N  N   . ILE   O  1  209 ? -2.097  -215.173 49.482  1.00 123.24 ? 209 ILE   O N   1 
ATOM   26221 C  CA  . ILE   O  1  209 ? -2.477  -214.681 48.125  1.00 126.86 ? 209 ILE   O CA  1 
ATOM   26222 C  C   . ILE   O  1  209 ? -2.244  -213.168 48.072  1.00 122.85 ? 209 ILE   O C   1 
ATOM   26223 O  O   . ILE   O  1  209 ? -2.623  -212.470 49.034  1.00 123.92 ? 209 ILE   O O   1 
ATOM   26224 C  CB  . ILE   O  1  209 ? -3.935  -215.066 47.791  1.00 130.65 ? 209 ILE   O CB  1 
ATOM   26225 C  CG1 . ILE   O  1  209 ? -4.137  -216.584 47.806  1.00 137.28 ? 209 ILE   O CG1 1 
ATOM   26226 C  CG2 . ILE   O  1  209 ? -4.382  -214.458 46.469  1.00 130.74 ? 209 ILE   O CG2 1 
ATOM   26227 C  CD1 . ILE   O  1  209 ? -3.170  -217.355 46.929  1.00 141.98 ? 209 ILE   O CD1 1 
ATOM   26228 N  N   . GLU   O  1  210 ? -1.626  -212.700 46.985  1.00 118.69 ? 210 GLU   O N   1 
ATOM   26229 C  CA  . GLU   O  1  210 ? -1.424  -211.263 46.670  1.00 119.49 ? 210 GLU   O CA  1 
ATOM   26230 C  C   . GLU   O  1  210 ? -2.213  -210.946 45.398  1.00 117.09 ? 210 GLU   O C   1 
ATOM   26231 O  O   . GLU   O  1  210 ? -1.999  -211.642 44.385  1.00 117.20 ? 210 GLU   O O   1 
ATOM   26232 C  CB  . GLU   O  1  210 ? 0.065   -210.963 46.497  1.00 118.27 ? 210 GLU   O CB  1 
ATOM   26233 C  CG  . GLU   O  1  210 ? 0.426   -209.518 46.788  1.00 120.97 ? 210 GLU   O CG  1 
ATOM   26234 C  CD  . GLU   O  1  210 ? 1.918   -209.232 46.822  1.00 119.82 ? 210 GLU   O CD  1 
ATOM   26235 O  OE1 . GLU   O  1  210 ? 2.321   -208.157 46.342  1.00 122.64 ? 210 GLU   O OE1 1 
ATOM   26236 O  OE2 . GLU   O  1  210 ? 2.677   -210.077 47.333  1.00 127.16 ? 210 GLU   O OE2 1 
ATOM   26237 N  N   . LEU   O  1  211 ? -3.094  -209.945 45.457  1.00 117.03 ? 211 LEU   O N   1 
ATOM   26238 C  CA  . LEU   O  1  211 ? -4.054  -209.624 44.369  1.00 115.08 ? 211 LEU   O CA  1 
ATOM   26239 C  C   . LEU   O  1  211 ? -4.301  -208.112 44.339  1.00 112.90 ? 211 LEU   O C   1 
ATOM   26240 O  O   . LEU   O  1  211 ? -4.613  -207.539 45.403  1.00 106.67 ? 211 LEU   O O   1 
ATOM   26241 C  CB  . LEU   O  1  211 ? -5.345  -210.410 44.617  1.00 114.69 ? 211 LEU   O CB  1 
ATOM   26242 C  CG  . LEU   O  1  211 ? -6.291  -210.536 43.422  1.00 114.92 ? 211 LEU   O CG  1 
ATOM   26243 C  CD1 . LEU   O  1  211 ? -7.090  -211.828 43.498  1.00 117.87 ? 211 LEU   O CD1 1 
ATOM   26244 C  CD2 . LEU   O  1  211 ? -7.226  -209.342 43.334  1.00 112.91 ? 211 LEU   O CD2 1 
ATOM   26245 N  N   . ALA   O  1  212 ? -4.152  -207.502 43.159  1.00 114.08 ? 212 ALA   O N   1 
ATOM   26246 C  CA  . ALA   O  1  212 ? -4.394  -206.063 42.901  1.00 113.49 ? 212 ALA   O CA  1 
ATOM   26247 C  C   . ALA   O  1  212 ? -5.286  -205.901 41.667  1.00 114.58 ? 212 ALA   O C   1 
ATOM   26248 O  O   . ALA   O  1  212 ? -5.288  -206.805 40.806  1.00 119.61 ? 212 ALA   O O   1 
ATOM   26249 C  CB  . ALA   O  1  212 ? -3.085  -205.343 42.715  1.00 115.62 ? 212 ALA   O CB  1 
ATOM   26250 N  N   . ILE   O  1  213 ? -5.997  -204.773 41.584  1.00 113.23 ? 213 ILE   O N   1 
ATOM   26251 C  CA  . ILE   O  1  213 ? -6.937  -204.455 40.470  1.00 112.09 ? 213 ILE   O CA  1 
ATOM   26252 C  C   . ILE   O  1  213 ? -6.555  -203.109 39.843  1.00 109.12 ? 213 ILE   O C   1 
ATOM   26253 O  O   . ILE   O  1  213 ? -5.979  -202.251 40.545  1.00 109.61 ? 213 ILE   O O   1 
ATOM   26254 C  CB  . ILE   O  1  213 ? -8.401  -204.466 40.955  1.00 111.09 ? 213 ILE   O CB  1 
ATOM   26255 C  CG1 . ILE   O  1  213 ? -8.650  -203.477 42.097  1.00 111.65 ? 213 ILE   O CG1 1 
ATOM   26256 C  CG2 . ILE   O  1  213 ? -8.820  -205.874 41.342  1.00 111.78 ? 213 ILE   O CG2 1 
ATOM   26257 C  CD1 . ILE   O  1  213 ? -10.002 -202.809 42.039  1.00 114.51 ? 213 ILE   O CD1 1 
ATOM   26258 N  N   . ILE   O  1  214 ? -6.847  -202.967 38.550  1.00 107.93 ? 214 ILE   O N   1 
ATOM   26259 C  CA  . ILE   O  1  214 ? -6.907  -201.678 37.804  1.00 106.69 ? 214 ILE   O CA  1 
ATOM   26260 C  C   . ILE   O  1  214 ? -8.383  -201.433 37.484  1.00 110.66 ? 214 ILE   O C   1 
ATOM   26261 O  O   . ILE   O  1  214 ? -8.913  -202.168 36.634  1.00 114.06 ? 214 ILE   O O   1 
ATOM   26262 C  CB  . ILE   O  1  214 ? -6.052  -201.742 36.524  1.00 103.01 ? 214 ILE   O CB  1 
ATOM   26263 C  CG1 . ILE   O  1  214 ? -4.636  -202.256 36.797  1.00 100.86 ? 214 ILE   O CG1 1 
ATOM   26264 C  CG2 . ILE   O  1  214 ? -6.044  -200.399 35.814  1.00 102.29 ? 214 ILE   O CG2 1 
ATOM   26265 C  CD1 . ILE   O  1  214 ? -3.853  -201.438 37.794  1.00 100.05 ? 214 ILE   O CD1 1 
ATOM   26266 N  N   . GLY   O  1  215 ? -9.024  -200.476 38.161  1.00 110.43 ? 215 GLY   O N   1 
ATOM   26267 C  CA  . GLY   O  1  215 ? -10.475 -200.234 38.045  1.00 113.20 ? 215 GLY   O CA  1 
ATOM   26268 C  C   . GLY   O  1  215 ? -10.807 -198.757 38.069  1.00 113.22 ? 215 GLY   O C   1 
ATOM   26269 O  O   . GLY   O  1  215 ? -10.144 -197.988 37.344  1.00 109.28 ? 215 GLY   O O   1 
ATOM   26270 N  N   . ASP   O  1  216 ? -11.803 -198.379 38.874  1.00 116.50 ? 216 ASP   O N   1 
ATOM   26271 C  CA  . ASP   O  1  216 ? -12.289 -196.982 39.018  1.00 116.37 ? 216 ASP   O CA  1 
ATOM   26272 C  C   . ASP   O  1  216 ? -11.205 -196.144 39.702  1.00 118.78 ? 216 ASP   O C   1 
ATOM   26273 O  O   . ASP   O  1  216 ? -10.354 -196.729 40.402  1.00 116.92 ? 216 ASP   O O   1 
ATOM   26274 C  CB  . ASP   O  1  216 ? -13.602 -196.926 39.805  1.00 117.09 ? 216 ASP   O CB  1 
ATOM   26275 C  CG  . ASP   O  1  216 ? -14.807 -197.473 39.056  1.00 116.63 ? 216 ASP   O CG  1 
ATOM   26276 O  OD1 . ASP   O  1  216 ? -14.662 -197.810 37.862  1.00 115.25 ? 216 ASP   O OD1 1 
ATOM   26277 O  OD2 . ASP   O  1  216 ? -15.885 -197.558 39.674  1.00 116.69 ? 216 ASP   O OD2 1 
ATOM   26278 N  N   . GLU   O  1  217 ? -11.243 -194.826 39.493  1.00 119.75 ? 217 GLU   O N   1 
ATOM   26279 C  CA  . GLU   O  1  217 ? -10.379 -193.843 40.197  1.00 120.41 ? 217 GLU   O CA  1 
ATOM   26280 C  C   . GLU   O  1  217 ? -10.750 -193.865 41.683  1.00 119.75 ? 217 GLU   O C   1 
ATOM   26281 O  O   . GLU   O  1  217 ? -11.958 -193.957 41.983  1.00 121.21 ? 217 GLU   O O   1 
ATOM   26282 C  CB  . GLU   O  1  217 ? -10.553 -192.445 39.598  1.00 121.59 ? 217 GLU   O CB  1 
ATOM   26283 C  CG  . GLU   O  1  217 ? -10.062 -192.327 38.164  1.00 123.21 ? 217 GLU   O CG  1 
ATOM   26284 C  CD  . GLU   O  1  217 ? -10.624 -191.147 37.389  1.00 122.92 ? 217 GLU   O CD  1 
ATOM   26285 O  OE1 . GLU   O  1  217 ? -9.854  -190.512 36.643  1.00 123.00 ? 217 GLU   O OE1 1 
ATOM   26286 O  OE2 . GLU   O  1  217 ? -11.833 -190.870 37.522  1.00 129.73 ? 217 GLU   O OE2 1 
ATOM   26287 N  N   . ASN   O  1  218 ? -9.747  -193.809 42.566  1.00 118.75 ? 218 ASN   O N   1 
ATOM   26288 C  CA  . ASN   O  1  218 ? -9.908  -193.849 44.044  1.00 117.82 ? 218 ASN   O CA  1 
ATOM   26289 C  C   . ASN   O  1  218 ? -9.554  -192.478 44.617  1.00 117.33 ? 218 ASN   O C   1 
ATOM   26290 O  O   . ASN   O  1  218 ? -8.405  -192.243 44.987  1.00 112.56 ? 218 ASN   O O   1 
ATOM   26291 C  CB  . ASN   O  1  218 ? -9.044  -194.943 44.679  1.00 115.31 ? 218 ASN   O CB  1 
ATOM   26292 C  CG  . ASN   O  1  218 ? -9.452  -196.344 44.279  1.00 115.77 ? 218 ASN   O CG  1 
ATOM   26293 O  OD1 . ASN   O  1  218 ? -10.036 -197.073 45.077  1.00 116.60 ? 218 ASN   O OD1 1 
ATOM   26294 N  ND2 . ASN   O  1  218 ? -9.145  -196.733 43.052  1.00 115.79 ? 218 ASN   O ND2 1 
ATOM   26295 N  N   . PRO   O  1  219 ? -10.516 -191.528 44.710  1.00 116.84 ? 219 PRO   O N   1 
ATOM   26296 C  CA  . PRO   O  1  219 ? -10.228 -190.195 45.243  1.00 116.60 ? 219 PRO   O CA  1 
ATOM   26297 C  C   . PRO   O  1  219 ? -9.711  -190.246 46.689  1.00 113.27 ? 219 PRO   O C   1 
ATOM   26298 O  O   . PRO   O  1  219 ? -8.866  -189.442 47.029  1.00 110.66 ? 219 PRO   O O   1 
ATOM   26299 C  CB  . PRO   O  1  219 ? -11.578 -189.460 45.175  1.00 117.44 ? 219 PRO   O CB  1 
ATOM   26300 C  CG  . PRO   O  1  219 ? -12.376 -190.237 44.149  1.00 118.47 ? 219 PRO   O CG  1 
ATOM   26301 C  CD  . PRO   O  1  219 ? -11.926 -191.673 44.319  1.00 118.80 ? 219 PRO   O CD  1 
ATOM   26302 N  N   . ASP   O  1  220 ? -10.213 -191.197 47.485  1.00 114.00 ? 220 ASP   O N   1 
ATOM   26303 C  CA  . ASP   O  1  220 ? -9.835  -191.398 48.910  1.00 117.65 ? 220 ASP   O CA  1 
ATOM   26304 C  C   . ASP   O  1  220 ? -8.339  -191.728 49.022  1.00 117.13 ? 220 ASP   O C   1 
ATOM   26305 O  O   . ASP   O  1  220 ? -7.753  -191.395 50.070  1.00 126.90 ? 220 ASP   O O   1 
ATOM   26306 C  CB  . ASP   O  1  220 ? -10.705 -192.468 49.580  1.00 117.95 ? 220 ASP   O CB  1 
ATOM   26307 C  CG  . ASP   O  1  220 ? -10.660 -193.836 48.918  1.00 118.77 ? 220 ASP   O CG  1 
ATOM   26308 O  OD1 . ASP   O  1  220 ? -10.869 -193.901 47.690  1.00 124.17 ? 220 ASP   O OD1 1 
ATOM   26309 O  OD2 . ASP   O  1  220 ? -10.426 -194.827 49.637  1.00 118.14 ? 220 ASP   O OD2 1 
ATOM   26310 N  N   . LEU   O  1  221 ? -7.739  -192.339 47.990  1.00 111.86 ? 221 LEU   O N   1 
ATOM   26311 C  CA  . LEU   O  1  221 ? -6.311  -192.770 47.989  1.00 110.65 ? 221 LEU   O CA  1 
ATOM   26312 C  C   . LEU   O  1  221 ? -5.406  -191.697 47.366  1.00 109.87 ? 221 LEU   O C   1 
ATOM   26313 O  O   . LEU   O  1  221 ? -4.196  -191.974 47.244  1.00 106.02 ? 221 LEU   O O   1 
ATOM   26314 C  CB  . LEU   O  1  221 ? -6.174  -194.090 47.219  1.00 110.55 ? 221 LEU   O CB  1 
ATOM   26315 C  CG  . LEU   O  1  221 ? -6.794  -195.329 47.867  1.00 110.76 ? 221 LEU   O CG  1 
ATOM   26316 C  CD1 . LEU   O  1  221 ? -6.674  -196.531 46.941  1.00 109.96 ? 221 LEU   O CD1 1 
ATOM   26317 C  CD2 . LEU   O  1  221 ? -6.149  -195.634 49.212  1.00 110.65 ? 221 LEU   O CD2 1 
ATOM   26318 N  N   . LEU   O  1  222 ? -5.943  -190.526 46.995  1.00 111.67 ? 222 LEU   O N   1 
ATOM   26319 C  CA  . LEU   O  1  222 ? -5.183  -189.454 46.288  1.00 108.92 ? 222 LEU   O CA  1 
ATOM   26320 C  C   . LEU   O  1  222 ? -4.299  -188.682 47.278  1.00 105.61 ? 222 LEU   O C   1 
ATOM   26321 O  O   . LEU   O  1  222 ? -3.165  -188.334 46.891  1.00 99.15  ? 222 LEU   O O   1 
ATOM   26322 C  CB  . LEU   O  1  222 ? -6.157  -188.513 45.571  1.00 110.30 ? 222 LEU   O CB  1 
ATOM   26323 C  CG  . LEU   O  1  222 ? -5.515  -187.415 44.721  1.00 111.48 ? 222 LEU   O CG  1 
ATOM   26324 C  CD1 . LEU   O  1  222 ? -4.538  -187.985 43.700  1.00 110.52 ? 222 LEU   O CD1 1 
ATOM   26325 C  CD2 . LEU   O  1  222 ? -6.581  -186.585 44.022  1.00 112.80 ? 222 LEU   O CD2 1 
ATOM   26326 N  N   . GLY   O  1  223 ? -4.809  -188.405 48.485  1.00 106.37 ? 223 GLY   O N   1 
ATOM   26327 C  CA  . GLY   O  1  223 ? -4.055  -187.785 49.595  1.00 104.31 ? 223 GLY   O CA  1 
ATOM   26328 C  C   . GLY   O  1  223 ? -4.213  -186.272 49.660  1.00 102.68 ? 223 GLY   O C   1 
ATOM   26329 O  O   . GLY   O  1  223 ? -3.569  -185.659 50.535  1.00 95.92  ? 223 GLY   O O   1 
ATOM   26330 N  N   . TYR   O  1  224 ? -5.031  -185.686 48.777  1.00 104.81 ? 224 TYR   O N   1 
ATOM   26331 C  CA  . TYR   O  1  224 ? -5.330  -184.228 48.724  1.00 105.67 ? 224 TYR   O CA  1 
ATOM   26332 C  C   . TYR   O  1  224 ? -6.589  -183.979 47.881  1.00 106.56 ? 224 TYR   O C   1 
ATOM   26333 O  O   . TYR   O  1  224 ? -6.964  -184.859 47.082  1.00 106.99 ? 224 TYR   O O   1 
ATOM   26334 C  CB  . TYR   O  1  224 ? -4.154  -183.452 48.124  1.00 106.19 ? 224 TYR   O CB  1 
ATOM   26335 C  CG  . TYR   O  1  224 ? -3.928  -183.767 46.670  1.00 106.04 ? 224 TYR   O CG  1 
ATOM   26336 C  CD1 . TYR   O  1  224 ? -3.155  -184.852 46.298  1.00 107.83 ? 224 TYR   O CD1 1 
ATOM   26337 C  CD2 . TYR   O  1  224 ? -4.537  -183.026 45.670  1.00 104.16 ? 224 TYR   O CD2 1 
ATOM   26338 C  CE1 . TYR   O  1  224 ? -2.962  -185.178 44.967  1.00 109.14 ? 224 TYR   O CE1 1 
ATOM   26339 C  CE2 . TYR   O  1  224 ? -4.360  -183.340 44.333  1.00 105.99 ? 224 TYR   O CE2 1 
ATOM   26340 C  CZ  . TYR   O  1  224 ? -3.578  -184.427 43.984  1.00 107.03 ? 224 TYR   O CZ  1 
ATOM   26341 O  OH  . TYR   O  1  224 ? -3.385  -184.748 42.671  1.00 110.34 ? 224 TYR   O OH  1 
ATOM   26342 N  N   . THR   O  1  225 ? -7.200  -182.800 48.041  1.00 104.33 ? 225 THR   O N   1 
ATOM   26343 C  CA  . THR   O  1  225 ? -8.390  -182.339 47.273  1.00 104.82 ? 225 THR   O CA  1 
ATOM   26344 C  C   . THR   O  1  225 ? -8.158  -180.910 46.775  1.00 105.86 ? 225 THR   O C   1 
ATOM   26345 O  O   . THR   O  1  225 ? -7.240  -180.246 47.294  1.00 103.61 ? 225 THR   O O   1 
ATOM   26346 C  CB  . THR   O  1  225 ? -9.663  -182.413 48.124  1.00 105.95 ? 225 THR   O CB  1 
ATOM   26347 O  OG1 . THR   O  1  225 ? -9.519  -181.522 49.231  1.00 104.46 ? 225 THR   O OG1 1 
ATOM   26348 C  CG2 . THR   O  1  225 ? -9.950  -183.809 48.629  1.00 104.50 ? 225 THR   O CG2 1 
ATOM   26349 N  N   . GLY   O  1  226 ? -8.965  -180.464 45.807  1.00 108.43 ? 226 GLY   O N   1 
ATOM   26350 C  CA  . GLY   O  1  226 ? -8.974  -179.072 45.316  1.00 110.40 ? 226 GLY   O CA  1 
ATOM   26351 C  C   . GLY   O  1  226 ? -8.708  -178.960 43.825  1.00 113.20 ? 226 GLY   O C   1 
ATOM   26352 O  O   . GLY   O  1  226 ? -8.983  -177.880 43.268  1.00 115.90 ? 226 GLY   O O   1 
ATOM   26353 N  N   . ILE   O  1  227 ? -8.165  -180.010 43.201  1.00 111.74 ? 227 ILE   O N   1 
ATOM   26354 C  CA  . ILE   O  1  227 ? -7.934  -180.079 41.726  1.00 113.68 ? 227 ILE   O CA  1 
ATOM   26355 C  C   . ILE   O  1  227 ? -8.956  -181.048 41.134  1.00 118.02 ? 227 ILE   O C   1 
ATOM   26356 O  O   . ILE   O  1  227 ? -8.832  -182.258 41.314  1.00 120.27 ? 227 ILE   O O   1 
ATOM   26357 C  CB  . ILE   O  1  227 ? -6.480  -180.479 41.401  1.00 111.56 ? 227 ILE   O CB  1 
ATOM   26358 C  CG1 . ILE   O  1  227 ? -5.476  -179.517 42.045  1.00 111.59 ? 227 ILE   O CG1 1 
ATOM   26359 C  CG2 . ILE   O  1  227 ? -6.276  -180.576 39.896  1.00 111.64 ? 227 ILE   O CG2 1 
ATOM   26360 C  CD1 . ILE   O  1  227 ? -4.037  -179.986 42.003  1.00 109.60 ? 227 ILE   O CD1 1 
ATOM   26361 N  N   . PRO   O  1  228 ? -10.000 -180.548 40.430  1.00 120.19 ? 228 PRO   O N   1 
ATOM   26362 C  CA  . PRO   O  1  228 ? -11.051 -181.405 39.874  1.00 123.00 ? 228 PRO   O CA  1 
ATOM   26363 C  C   . PRO   O  1  228 ? -10.557 -182.489 38.900  1.00 126.77 ? 228 PRO   O C   1 
ATOM   26364 O  O   . PRO   O  1  228 ? -11.129 -183.568 38.907  1.00 124.62 ? 228 PRO   O O   1 
ATOM   26365 C  CB  . PRO   O  1  228 ? -11.965 -180.429 39.114  1.00 122.54 ? 228 PRO   O CB  1 
ATOM   26366 C  CG  . PRO   O  1  228 ? -11.698 -179.083 39.749  1.00 123.88 ? 228 PRO   O CG  1 
ATOM   26367 C  CD  . PRO   O  1  228 ? -10.240 -179.124 40.149  1.00 121.29 ? 228 PRO   O CD  1 
ATOM   26368 N  N   . THR   O  1  229 ? -9.529  -182.183 38.098  1.00 129.65 ? 229 THR   O N   1 
ATOM   26369 C  CA  . THR   O  1  229 ? -8.996  -183.062 37.017  1.00 128.42 ? 229 THR   O CA  1 
ATOM   26370 C  C   . THR   O  1  229 ? -8.211  -184.243 37.609  1.00 130.91 ? 229 THR   O C   1 
ATOM   26371 O  O   . THR   O  1  229 ? -8.185  -185.302 36.952  1.00 133.63 ? 229 THR   O O   1 
ATOM   26372 C  CB  . THR   O  1  229 ? -8.161  -182.260 36.010  1.00 128.59 ? 229 THR   O CB  1 
ATOM   26373 O  OG1 . THR   O  1  229 ? -7.153  -181.535 36.714  1.00 127.53 ? 229 THR   O OG1 1 
ATOM   26374 C  CG2 . THR   O  1  229 ? -9.005  -181.301 35.199  1.00 127.44 ? 229 THR   O CG2 1 
ATOM   26375 N  N   . ASP   O  1  230 ? -7.594  -184.073 38.786  1.00 131.19 ? 230 ASP   O N   1 
ATOM   26376 C  CA  . ASP   O  1  230 ? -6.897  -185.150 39.545  1.00 132.64 ? 230 ASP   O CA  1 
ATOM   26377 C  C   . ASP   O  1  230 ? -7.933  -185.893 40.402  1.00 130.71 ? 230 ASP   O C   1 
ATOM   26378 O  O   . ASP   O  1  230 ? -8.467  -185.269 41.342  1.00 125.84 ? 230 ASP   O O   1 
ATOM   26379 C  CB  . ASP   O  1  230 ? -5.762  -184.579 40.406  1.00 131.32 ? 230 ASP   O CB  1 
ATOM   26380 C  CG  . ASP   O  1  230 ? -4.687  -183.838 39.625  1.00 131.11 ? 230 ASP   O CG  1 
ATOM   26381 O  OD1 . ASP   O  1  230 ? -4.845  -183.696 38.396  1.00 134.85 ? 230 ASP   O OD1 1 
ATOM   26382 O  OD2 . ASP   O  1  230 ? -3.698  -183.405 40.255  1.00 124.16 ? 230 ASP   O OD2 1 
ATOM   26383 N  N   . LYS   O  1  231 ? -8.211  -187.167 40.091  1.00 131.63 ? 231 LYS   O N   1 
ATOM   26384 C  CA  . LYS   O  1  231 ? -9.321  -187.950 40.711  1.00 127.90 ? 231 LYS   O CA  1 
ATOM   26385 C  C   . LYS   O  1  231 ? -8.813  -189.218 41.415  1.00 125.26 ? 231 LYS   O C   1 
ATOM   26386 O  O   . LYS   O  1  231 ? -9.659  -189.928 41.997  1.00 119.29 ? 231 LYS   O O   1 
ATOM   26387 C  CB  . LYS   O  1  231 ? -10.376 -188.291 39.654  1.00 132.07 ? 231 LYS   O CB  1 
ATOM   26388 C  CG  . LYS   O  1  231 ? -11.472 -187.246 39.497  1.00 135.05 ? 231 LYS   O CG  1 
ATOM   26389 C  CD  . LYS   O  1  231 ? -12.262 -187.386 38.219  1.00 139.42 ? 231 LYS   O CD  1 
ATOM   26390 C  CE  . LYS   O  1  231 ? -11.523 -186.842 37.015  1.00 139.64 ? 231 LYS   O CE  1 
ATOM   26391 N  NZ  . LYS   O  1  231 ? -12.278 -187.069 35.760  1.00 140.75 ? 231 LYS   O NZ  1 
ATOM   26392 N  N   . GLY   O  1  232 ? -7.505  -189.499 41.383  1.00 120.78 ? 232 GLY   O N   1 
ATOM   26393 C  CA  . GLY   O  1  232 ? -6.885  -190.557 42.205  1.00 120.58 ? 232 GLY   O CA  1 
ATOM   26394 C  C   . GLY   O  1  232 ? -6.459  -191.779 41.395  1.00 117.89 ? 232 GLY   O C   1 
ATOM   26395 O  O   . GLY   O  1  232 ? -6.834  -191.931 40.233  1.00 115.40 ? 232 GLY   O O   1 
ATOM   26396 N  N   . PRO   O  1  233 ? -5.672  -192.692 42.008  1.00 114.39 ? 233 PRO   O N   1 
ATOM   26397 C  CA  . PRO   O  1  233 ? -5.145  -193.868 41.313  1.00 113.36 ? 233 PRO   O CA  1 
ATOM   26398 C  C   . PRO   O  1  233 ? -6.216  -194.927 41.004  1.00 112.83 ? 233 PRO   O C   1 
ATOM   26399 O  O   . PRO   O  1  233 ? -7.104  -195.119 41.819  1.00 112.85 ? 233 PRO   O O   1 
ATOM   26400 C  CB  . PRO   O  1  233 ? -4.117  -194.428 42.310  1.00 112.30 ? 233 PRO   O CB  1 
ATOM   26401 C  CG  . PRO   O  1  233 ? -4.651  -194.005 43.661  1.00 113.62 ? 233 PRO   O CG  1 
ATOM   26402 C  CD  . PRO   O  1  233 ? -5.254  -192.638 43.419  1.00 113.82 ? 233 PRO   O CD  1 
ATOM   26403 N  N   . ARG   O  1  234 ? -6.102  -195.581 39.843  1.00 110.58 ? 234 ARG   O N   1 
ATOM   26404 C  CA  . ARG   O  1  234 ? -6.965  -196.721 39.426  1.00 112.63 ? 234 ARG   O CA  1 
ATOM   26405 C  C   . ARG   O  1  234 ? -6.346  -198.038 39.906  1.00 112.78 ? 234 ARG   O C   1 
ATOM   26406 O  O   . ARG   O  1  234 ? -7.102  -199.023 40.038  1.00 115.34 ? 234 ARG   O O   1 
ATOM   26407 C  CB  . ARG   O  1  234 ? -7.157  -196.737 37.908  1.00 110.88 ? 234 ARG   O CB  1 
ATOM   26408 C  CG  . ARG   O  1  234 ? -7.991  -195.581 37.379  1.00 111.50 ? 234 ARG   O CG  1 
ATOM   26409 C  CD  . ARG   O  1  234 ? -8.035  -195.571 35.864  1.00 111.67 ? 234 ARG   O CD  1 
ATOM   26410 N  NE  . ARG   O  1  234 ? -8.939  -194.552 35.343  1.00 112.30 ? 234 ARG   O NE  1 
ATOM   26411 C  CZ  . ARG   O  1  234 ? -10.244 -194.715 35.126  1.00 109.35 ? 234 ARG   O CZ  1 
ATOM   26412 N  NH1 . ARG   O  1  234 ? -10.836 -195.871 35.380  1.00 110.45 ? 234 ARG   O NH1 1 
ATOM   26413 N  NH2 . ARG   O  1  234 ? -10.957 -193.710 34.651  1.00 110.38 ? 234 ARG   O NH2 1 
ATOM   26414 N  N   . PHE   O  1  235 ? -5.030  -198.062 40.146  1.00 112.40 ? 235 PHE   O N   1 
ATOM   26415 C  CA  . PHE   O  1  235 ? -4.325  -199.198 40.795  1.00 110.72 ? 235 PHE   O CA  1 
ATOM   26416 C  C   . PHE   O  1  235 ? -4.736  -199.250 42.267  1.00 110.42 ? 235 PHE   O C   1 
ATOM   26417 O  O   . PHE   O  1  235 ? -4.647  -198.216 42.954  1.00 107.92 ? 235 PHE   O O   1 
ATOM   26418 C  CB  . PHE   O  1  235 ? -2.801  -199.082 40.685  1.00 109.70 ? 235 PHE   O CB  1 
ATOM   26419 C  CG  . PHE   O  1  235 ? -2.052  -200.157 41.435  1.00 110.74 ? 235 PHE   O CG  1 
ATOM   26420 C  CD1 . PHE   O  1  235 ? -1.767  -200.016 42.786  1.00 110.74 ? 235 PHE   O CD1 1 
ATOM   26421 C  CD2 . PHE   O  1  235 ? -1.654  -201.325 40.799  1.00 113.13 ? 235 PHE   O CD2 1 
ATOM   26422 C  CE1 . PHE   O  1  235 ? -1.092  -201.011 43.478  1.00 111.38 ? 235 PHE   O CE1 1 
ATOM   26423 C  CE2 . PHE   O  1  235 ? -0.976  -202.318 41.492  1.00 111.83 ? 235 PHE   O CE2 1 
ATOM   26424 C  CZ  . PHE   O  1  235 ? -0.696  -202.159 42.831  1.00 111.69 ? 235 PHE   O CZ  1 
ATOM   26425 N  N   . ARG   O  1  236 ? -5.172  -200.422 42.731  1.00 110.27 ? 236 ARG   O N   1 
ATOM   26426 C  CA  . ARG   O  1  236 ? -5.430  -200.688 44.168  1.00 110.74 ? 236 ARG   O CA  1 
ATOM   26427 C  C   . ARG   O  1  236 ? -5.048  -202.134 44.493  1.00 111.13 ? 236 ARG   O C   1 
ATOM   26428 O  O   . ARG   O  1  236 ? -5.406  -203.039 43.714  1.00 110.19 ? 236 ARG   O O   1 
ATOM   26429 C  CB  . ARG   O  1  236 ? -6.892  -200.425 44.537  1.00 111.76 ? 236 ARG   O CB  1 
ATOM   26430 C  CG  . ARG   O  1  236 ? -7.130  -200.397 46.040  1.00 113.62 ? 236 ARG   O CG  1 
ATOM   26431 C  CD  . ARG   O  1  236 ? -8.573  -200.171 46.442  1.00 120.52 ? 236 ARG   O CD  1 
ATOM   26432 N  NE  . ARG   O  1  236 ? -9.423  -201.300 46.087  1.00 129.02 ? 236 ARG   O NE  1 
ATOM   26433 C  CZ  . ARG   O  1  236 ? -10.556 -201.639 46.704  1.00 138.17 ? 236 ARG   O CZ  1 
ATOM   26434 N  NH1 . ARG   O  1  236 ? -11.001 -200.941 47.737  1.00 140.42 ? 236 ARG   O NH1 1 
ATOM   26435 N  NH2 . ARG   O  1  236 ? -11.242 -202.691 46.285  1.00 142.04 ? 236 ARG   O NH2 1 
ATOM   26436 N  N   . LYS   O  1  237 ? -4.340  -202.314 45.608  1.00 113.28 ? 237 LYS   O N   1 
ATOM   26437 C  CA  . LYS   O  1  237 ? -3.983  -203.627 46.197  1.00 112.85 ? 237 LYS   O CA  1 
ATOM   26438 C  C   . LYS   O  1  237 ? -5.127  -204.036 47.128  1.00 112.91 ? 237 LYS   O C   1 
ATOM   26439 O  O   . LYS   O  1  237 ? -5.457  -203.241 48.030  1.00 112.35 ? 237 LYS   O O   1 
ATOM   26440 C  CB  . LYS   O  1  237 ? -2.647  -203.499 46.938  1.00 114.17 ? 237 LYS   O CB  1 
ATOM   26441 C  CG  . LYS   O  1  237 ? -1.766  -204.739 46.941  1.00 117.37 ? 237 LYS   O CG  1 
ATOM   26442 C  CD  . LYS   O  1  237 ? -0.301  -204.406 47.123  1.00 119.77 ? 237 LYS   O CD  1 
ATOM   26443 C  CE  . LYS   O  1  237 ? 0.604   -205.611 46.993  1.00 123.23 ? 237 LYS   O CE  1 
ATOM   26444 N  NZ  . LYS   O  1  237 ? 0.618   -206.423 48.234  1.00 126.66 ? 237 LYS   O NZ  1 
ATOM   26445 N  N   . LEU   O  1  238 ? -5.745  -205.197 46.896  1.00 111.96 ? 238 LEU   O N   1 
ATOM   26446 C  CA  . LEU   O  1  238 ? -6.799  -205.735 47.795  1.00 113.77 ? 238 LEU   O CA  1 
ATOM   26447 C  C   . LEU   O  1  238 ? -6.137  -206.116 49.121  1.00 112.10 ? 238 LEU   O C   1 
ATOM   26448 O  O   . LEU   O  1  238 ? -5.030  -206.686 49.081  1.00 115.47 ? 238 LEU   O O   1 
ATOM   26449 C  CB  . LEU   O  1  238 ? -7.490  -206.946 47.159  1.00 113.37 ? 238 LEU   O CB  1 
ATOM   26450 C  CG  . LEU   O  1  238 ? -8.293  -206.698 45.881  1.00 115.17 ? 238 LEU   O CG  1 
ATOM   26451 C  CD1 . LEU   O  1  238 ? -9.439  -207.695 45.776  1.00 115.50 ? 238 LEU   O CD1 1 
ATOM   26452 C  CD2 . LEU   O  1  238 ? -8.836  -205.278 45.804  1.00 115.90 ? 238 LEU   O CD2 1 
ATOM   26453 N  N   . THR   O  1  239 ? -6.783  -205.793 50.244  1.00 115.37 ? 239 THR   O N   1 
ATOM   26454 C  CA  . THR   O  1  239 ? -6.290  -206.105 51.611  1.00 117.19 ? 239 THR   O CA  1 
ATOM   26455 C  C   . THR   O  1  239 ? -6.492  -207.598 51.886  1.00 117.55 ? 239 THR   O C   1 
ATOM   26456 O  O   . THR   O  1  239 ? -7.346  -208.220 51.220  1.00 115.85 ? 239 THR   O O   1 
ATOM   26457 C  CB  . THR   O  1  239 ? -6.978  -205.235 52.671  1.00 119.20 ? 239 THR   O CB  1 
ATOM   26458 O  OG1 . THR   O  1  239 ? -8.385  -205.474 52.633  1.00 120.94 ? 239 THR   O OG1 1 
ATOM   26459 C  CG2 . THR   O  1  239 ? -6.712  -203.760 52.475  1.00 118.00 ? 239 THR   O CG2 1 
ATOM   26460 N  N   . SER   O  1  240 ? -5.725  -208.142 52.832  1.00 117.57 ? 240 SER   O N   1 
ATOM   26461 C  CA  . SER   O  1  240 ? -5.840  -209.539 53.320  1.00 119.19 ? 240 SER   O CA  1 
ATOM   26462 C  C   . SER   O  1  240 ? -7.296  -209.826 53.717  1.00 123.93 ? 240 SER   O C   1 
ATOM   26463 O  O   . SER   O  1  240 ? -7.762  -210.953 53.464  1.00 129.66 ? 240 SER   O O   1 
ATOM   26464 C  CB  . SER   O  1  240 ? -4.884  -209.780 54.462  1.00 119.58 ? 240 SER   O CB  1 
ATOM   26465 O  OG  . SER   O  1  240 ? -4.952  -211.122 54.918  1.00 119.63 ? 240 SER   O OG  1 
ATOM   26466 N  N   . GLN   O  1  241 ? -7.989  -208.836 54.292  1.00 120.92 ? 241 GLN   O N   1 
ATOM   26467 C  CA  . GLN   O  1  241 ? -9.407  -208.946 54.735  1.00 122.91 ? 241 GLN   O CA  1 
ATOM   26468 C  C   . GLN   O  1  241 ? -10.342 -208.998 53.519  1.00 126.45 ? 241 GLN   O C   1 
ATOM   26469 O  O   . GLN   O  1  241 ? -11.300 -209.796 53.559  1.00 131.67 ? 241 GLN   O O   1 
ATOM   26470 C  CB  . GLN   O  1  241 ? -9.775  -207.779 55.654  1.00 122.51 ? 241 GLN   O CB  1 
ATOM   26471 C  CG  . GLN   O  1  241 ? -11.210 -207.823 56.162  1.00 126.09 ? 241 GLN   O CG  1 
ATOM   26472 C  CD  . GLN   O  1  241 ? -11.514 -209.107 56.894  1.00 128.42 ? 241 GLN   O CD  1 
ATOM   26473 O  OE1 . GLN   O  1  241 ? -10.774 -209.520 57.784  1.00 130.98 ? 241 GLN   O OE1 1 
ATOM   26474 N  NE2 . GLN   O  1  241 ? -12.609 -209.753 56.524  1.00 132.46 ? 241 GLN   O NE2 1 
ATOM   26475 N  N   . GLU   O  1  242 ? -10.084 -208.179 52.494  1.00 125.32 ? 242 GLU   O N   1 
ATOM   26476 C  CA  . GLU   O  1  242 ? -10.933 -208.060 51.273  1.00 128.14 ? 242 GLU   O CA  1 
ATOM   26477 C  C   . GLU   O  1  242 ? -10.909 -209.369 50.467  1.00 126.85 ? 242 GLU   O C   1 
ATOM   26478 O  O   . GLU   O  1  242 ? -11.913 -209.652 49.782  1.00 123.46 ? 242 GLU   O O   1 
ATOM   26479 C  CB  . GLU   O  1  242 ? -10.474 -206.890 50.400  1.00 124.65 ? 242 GLU   O CB  1 
ATOM   26480 C  CG  . GLU   O  1  242 ? -10.999 -205.542 50.863  1.00 125.68 ? 242 GLU   O CG  1 
ATOM   26481 C  CD  . GLU   O  1  242 ? -10.413 -204.342 50.135  1.00 123.71 ? 242 GLU   O CD  1 
ATOM   26482 O  OE1 . GLU   O  1  242 ? -9.579  -204.545 49.231  1.00 123.53 ? 242 GLU   O OE1 1 
ATOM   26483 O  OE2 . GLU   O  1  242 ? -10.795 -203.205 50.472  1.00 122.84 ? 242 GLU   O OE2 1 
ATOM   26484 N  N   . ILE   O  1  243 ? -9.812  -210.131 50.534  1.00 129.87 ? 243 ILE   O N   1 
ATOM   26485 C  CA  . ILE   O  1  243 ? -9.652  -211.435 49.820  1.00 131.00 ? 243 ILE   O CA  1 
ATOM   26486 C  C   . ILE   O  1  243 ? -10.516 -212.493 50.527  1.00 132.08 ? 243 ILE   O C   1 
ATOM   26487 O  O   . ILE   O  1  243 ? -11.276 -213.197 49.828  1.00 130.64 ? 243 ILE   O O   1 
ATOM   26488 C  CB  . ILE   O  1  243 ? -8.164  -211.843 49.728  1.00 131.47 ? 243 ILE   O CB  1 
ATOM   26489 C  CG1 . ILE   O  1  243 ? -7.344  -210.812 48.945  1.00 129.02 ? 243 ILE   O CG1 1 
ATOM   26490 C  CG2 . ILE   O  1  243 ? -8.015  -213.238 49.134  1.00 131.50 ? 243 ILE   O CG2 1 
ATOM   26491 C  CD1 . ILE   O  1  243 ? -5.847  -210.942 49.117  1.00 128.13 ? 243 ILE   O CD1 1 
ATOM   26492 N  N   . ASN   O  1  244 ? -10.419 -212.580 51.859  1.00 127.45 ? 244 ASN   O N   1 
ATOM   26493 C  CA  . ASN   O  1  244 ? -11.120 -213.591 52.700  1.00 127.86 ? 244 ASN   O CA  1 
ATOM   26494 C  C   . ASN   O  1  244 ? -12.642 -213.411 52.603  1.00 131.70 ? 244 ASN   O C   1 
ATOM   26495 O  O   . ASN   O  1  244 ? -13.361 -214.421 52.749  1.00 131.74 ? 244 ASN   O O   1 
ATOM   26496 C  CB  . ASN   O  1  244 ? -10.663 -213.530 54.160  1.00 129.67 ? 244 ASN   O CB  1 
ATOM   26497 C  CG  . ASN   O  1  244 ? -9.219  -213.946 54.354  1.00 126.06 ? 244 ASN   O CG  1 
ATOM   26498 O  OD1 . ASN   O  1  244 ? -8.729  -214.853 53.685  1.00 127.47 ? 244 ASN   O OD1 1 
ATOM   26499 N  ND2 . ASN   O  1  244 ? -8.528  -213.298 55.277  1.00 123.59 ? 244 ASN   O ND2 1 
ATOM   26500 N  N   . ASP   O  1  245 ? -13.112 -212.179 52.381  1.00 129.50 ? 245 ASP   O N   1 
ATOM   26501 C  CA  . ASP   O  1  245 ? -14.552 -211.856 52.184  1.00 133.87 ? 245 ASP   O CA  1 
ATOM   26502 C  C   . ASP   O  1  245 ? -15.066 -212.564 50.924  1.00 135.91 ? 245 ASP   O C   1 
ATOM   26503 O  O   . ASP   O  1  245 ? -16.215 -213.047 50.948  1.00 140.56 ? 245 ASP   O O   1 
ATOM   26504 C  CB  . ASP   O  1  245 ? -14.775 -210.343 52.097  1.00 134.49 ? 245 ASP   O CB  1 
ATOM   26505 C  CG  . ASP   O  1  245 ? -14.480 -209.597 53.389  1.00 135.40 ? 245 ASP   O CG  1 
ATOM   26506 O  OD1 . ASP   O  1  245 ? -14.525 -210.234 54.460  1.00 136.46 ? 245 ASP   O OD1 1 
ATOM   26507 O  OD2 . ASP   O  1  245 ? -14.198 -208.382 53.315  1.00 136.43 ? 245 ASP   O OD2 1 
ATOM   26508 N  N   . ARG   O  1  246 ? -14.241 -212.629 49.874  1.00 132.18 ? 246 ARG   O N   1 
ATOM   26509 C  CA  . ARG   O  1  246 ? -14.603 -213.209 48.552  1.00 132.77 ? 246 ARG   O CA  1 
ATOM   26510 C  C   . ARG   O  1  246 ? -14.370 -214.726 48.540  1.00 136.23 ? 246 ARG   O C   1 
ATOM   26511 O  O   . ARG   O  1  246 ? -14.943 -215.385 47.652  1.00 139.53 ? 246 ARG   O O   1 
ATOM   26512 C  CB  . ARG   O  1  246 ? -13.813 -212.521 47.435  1.00 130.92 ? 246 ARG   O CB  1 
ATOM   26513 C  CG  . ARG   O  1  246 ? -14.342 -211.140 47.078  1.00 131.54 ? 246 ARG   O CG  1 
ATOM   26514 C  CD  . ARG   O  1  246 ? -13.365 -210.329 46.250  1.00 128.79 ? 246 ARG   O CD  1 
ATOM   26515 N  NE  . ARG   O  1  246 ? -13.888 -209.007 45.927  1.00 127.33 ? 246 ARG   O NE  1 
ATOM   26516 C  CZ  . ARG   O  1  246 ? -13.947 -207.976 46.770  1.00 124.97 ? 246 ARG   O CZ  1 
ATOM   26517 N  NH1 . ARG   O  1  246 ? -13.516 -208.090 48.016  1.00 125.65 ? 246 ARG   O NH1 1 
ATOM   26518 N  NH2 . ARG   O  1  246 ? -14.445 -206.823 46.361  1.00 125.04 ? 246 ARG   O NH2 1 
ATOM   26519 N  N   . LEU   O  1  247 ? -13.576 -215.263 49.476  1.00 136.00 ? 247 LEU   O N   1 
ATOM   26520 C  CA  . LEU   O  1  247 ? -13.250 -216.717 49.551  1.00 139.66 ? 247 LEU   O CA  1 
ATOM   26521 C  C   . LEU   O  1  247 ? -14.387 -217.496 50.234  1.00 143.15 ? 247 LEU   O C   1 
ATOM   26522 O  O   . LEU   O  1  247 ? -14.347 -218.740 50.175  1.00 144.31 ? 247 LEU   O O   1 
ATOM   26523 C  CB  . LEU   O  1  247 ? -11.926 -216.924 50.298  1.00 133.95 ? 247 LEU   O CB  1 
ATOM   26524 C  CG  . LEU   O  1  247 ? -10.650 -216.602 49.516  1.00 130.66 ? 247 LEU   O CG  1 
ATOM   26525 C  CD1 . LEU   O  1  247 ? -9.435  -216.658 50.430  1.00 126.57 ? 247 LEU   O CD1 1 
ATOM   26526 C  CD2 . LEU   O  1  247 ? -10.462 -217.545 48.335  1.00 128.45 ? 247 LEU   O CD2 1 
ATOM   26527 N  N   . GLU   O  1  248 ? -15.354 -216.810 50.855  1.00 149.25 ? 248 GLU   O N   1 
ATOM   26528 C  CA  . GLU   O  1  248 ? -16.535 -217.442 51.510  1.00 153.27 ? 248 GLU   O CA  1 
ATOM   26529 C  C   . GLU   O  1  248 ? -17.620 -217.720 50.463  1.00 162.21 ? 248 GLU   O C   1 
ATOM   26530 O  O   . GLU   O  1  248 ? -18.208 -218.821 50.508  1.00 166.31 ? 248 GLU   O O   1 
ATOM   26531 C  CB  . GLU   O  1  248 ? -17.062 -216.561 52.643  1.00 153.57 ? 248 GLU   O CB  1 
ATOM   26532 C  CG  . GLU   O  1  248 ? -16.309 -216.754 53.948  1.00 152.82 ? 248 GLU   O CG  1 
ATOM   26533 C  CD  . GLU   O  1  248 ? -16.008 -215.478 54.717  1.00 152.17 ? 248 GLU   O CD  1 
ATOM   26534 O  OE1 . GLU   O  1  248 ? -16.712 -214.470 54.500  1.00 147.74 ? 248 GLU   O OE1 1 
ATOM   26535 O  OE2 . GLU   O  1  248 ? -15.061 -215.494 55.527  1.00 152.65 ? 248 GLU   O OE2 1 
ATOM   26536 N  N   . ALA   O  1  249 ? -17.874 -216.761 49.565  1.00 164.46 ? 249 ALA   O N   1 
ATOM   26537 C  CA  . ALA   O  1  249 ? -18.790 -216.899 48.406  1.00 166.13 ? 249 ALA   O CA  1 
ATOM   26538 C  C   . ALA   O  1  249 ? -17.987 -217.362 47.180  1.00 167.36 ? 249 ALA   O C   1 
ATOM   26539 O  O   . ALA   O  1  249 ? -18.058 -216.687 46.130  1.00 161.24 ? 249 ALA   O O   1 
ATOM   26540 C  CB  . ALA   O  1  249 ? -19.507 -215.592 48.156  1.00 164.40 ? 249 ALA   O CB  1 
ATOM   26541 N  N   . LEU   O  1  250 ? -17.262 -218.480 47.318  1.00 170.03 ? 250 LEU   O N   1 
ATOM   26542 C  CA  . LEU   O  1  250 ? -16.334 -219.044 46.297  1.00 170.48 ? 250 LEU   O CA  1 
ATOM   26543 C  C   . LEU   O  1  250 ? -17.004 -220.254 45.628  1.00 172.27 ? 250 LEU   O C   1 
ATOM   26544 O  O   . LEU   O  1  250 ? -17.904 -220.099 44.800  1.00 173.21 ? 250 LEU   O O   1 
ATOM   26545 C  CB  . LEU   O  1  250 ? -15.018 -219.421 46.995  1.00 166.02 ? 250 LEU   O CB  1 
ATOM   26546 C  CG  . LEU   O  1  250 ? -13.744 -219.453 46.144  1.00 161.83 ? 250 LEU   O CG  1 
ATOM   26547 C  CD1 . LEU   O  1  250 ? -13.704 -220.673 45.236  1.00 160.69 ? 250 LEU   O CD1 1 
ATOM   26548 C  CD2 . LEU   O  1  250 ? -13.563 -218.175 45.336  1.00 158.31 ? 250 LEU   O CD2 1 
ATOM   26549 O  OXT . LEU   O  1  250 ? -16.686 -221.418 45.882  1.00 175.05 ? 250 LEU   O OXT 1 
ATOM   26550 N  N   . GLY   P  2  2   ? 41.719  -214.272 31.911  1.00 123.23 ? 1   GLY   P N   1 
ATOM   26551 C  CA  . GLY   P  2  2   ? 40.714  -213.169 31.894  1.00 121.03 ? 1   GLY   P CA  1 
ATOM   26552 C  C   . GLY   P  2  2   ? 39.370  -213.632 31.362  1.00 121.80 ? 1   GLY   P C   1 
ATOM   26553 O  O   . GLY   P  2  2   ? 39.002  -214.797 31.616  1.00 125.38 ? 1   GLY   P O   1 
ATOM   26554 N  N   . SER   P  2  3   ? 38.667  -212.753 30.643  1.00 120.45 ? 2   SER   P N   1 
ATOM   26555 C  CA  . SER   P  2  3   ? 37.300  -212.984 30.104  1.00 124.68 ? 2   SER   P CA  1 
ATOM   26556 C  C   . SER   P  2  3   ? 37.354  -213.636 28.713  1.00 123.83 ? 2   SER   P C   1 
ATOM   26557 O  O   . SER   P  2  3   ? 36.294  -214.108 28.258  1.00 124.44 ? 2   SER   P O   1 
ATOM   26558 C  CB  . SER   P  2  3   ? 36.510  -211.698 30.083  1.00 127.56 ? 2   SER   P CB  1 
ATOM   26559 O  OG  . SER   P  2  3   ? 37.228  -210.662 29.424  1.00 132.81 ? 2   SER   P OG  1 
ATOM   26560 N  N   . ARG   P  2  4   ? 38.528  -213.676 28.070  1.00 123.91 ? 3   ARG   P N   1 
ATOM   26561 C  CA  . ARG   P  2  4   ? 38.747  -214.324 26.742  1.00 129.13 ? 3   ARG   P CA  1 
ATOM   26562 C  C   . ARG   P  2  4   ? 38.050  -215.693 26.699  1.00 128.06 ? 3   ARG   P C   1 
ATOM   26563 O  O   . ARG   P  2  4   ? 37.458  -216.024 25.650  1.00 124.40 ? 3   ARG   P O   1 
ATOM   26564 C  CB  . ARG   P  2  4   ? 40.247  -214.471 26.455  1.00 138.08 ? 3   ARG   P CB  1 
ATOM   26565 C  CG  . ARG   P  2  4   ? 40.609  -215.685 25.609  1.00 144.96 ? 3   ARG   P CG  1 
ATOM   26566 C  CD  . ARG   P  2  4   ? 42.048  -215.672 25.135  1.00 154.13 ? 3   ARG   P CD  1 
ATOM   26567 N  NE  . ARG   P  2  4   ? 43.000  -215.572 26.236  1.00 159.87 ? 3   ARG   P NE  1 
ATOM   26568 C  CZ  . ARG   P  2  4   ? 43.679  -214.476 26.580  1.00 163.30 ? 3   ARG   P CZ  1 
ATOM   26569 N  NH1 . ARG   P  2  4   ? 43.542  -213.345 25.905  1.00 161.08 ? 3   ARG   P NH1 1 
ATOM   26570 N  NH2 . ARG   P  2  4   ? 44.520  -214.525 27.600  1.00 165.43 ? 3   ARG   P NH2 1 
ATOM   26571 N  N   . ARG   P  2  5   ? 38.137  -216.450 27.796  1.00 123.66 ? 4   ARG   P N   1 
ATOM   26572 C  CA  . ARG   P  2  5   ? 37.608  -217.833 27.949  1.00 124.59 ? 4   ARG   P CA  1 
ATOM   26573 C  C   . ARG   P  2  5   ? 36.160  -217.926 27.444  1.00 119.57 ? 4   ARG   P C   1 
ATOM   26574 O  O   . ARG   P  2  5   ? 35.843  -218.927 26.773  1.00 119.11 ? 4   ARG   P O   1 
ATOM   26575 C  CB  . ARG   P  2  5   ? 37.683  -218.254 29.422  1.00 131.39 ? 4   ARG   P CB  1 
ATOM   26576 C  CG  . ARG   P  2  5   ? 38.172  -219.678 29.649  1.00 134.31 ? 4   ARG   P CG  1 
ATOM   26577 C  CD  . ARG   P  2  5   ? 38.210  -220.049 31.123  1.00 135.99 ? 4   ARG   P CD  1 
ATOM   26578 N  NE  . ARG   P  2  5   ? 38.915  -219.057 31.926  1.00 136.01 ? 4   ARG   P NE  1 
ATOM   26579 C  CZ  . ARG   P  2  5   ? 40.235  -218.999 32.097  1.00 137.57 ? 4   ARG   P CZ  1 
ATOM   26580 N  NH1 . ARG   P  2  5   ? 41.032  -219.889 31.527  1.00 135.08 ? 4   ARG   P NH1 1 
ATOM   26581 N  NH2 . ARG   P  2  5   ? 40.755  -218.041 32.847  1.00 141.48 ? 4   ARG   P NH2 1 
ATOM   26582 N  N   . TYR   P  2  6   ? 35.323  -216.926 27.750  1.00 115.76 ? 5   TYR   P N   1 
ATOM   26583 C  CA  . TYR   P  2  6   ? 33.843  -216.967 27.583  1.00 113.35 ? 5   TYR   P CA  1 
ATOM   26584 C  C   . TYR   P  2  6   ? 33.395  -216.168 26.351  1.00 108.16 ? 5   TYR   P C   1 
ATOM   26585 O  O   . TYR   P  2  6   ? 32.178  -215.941 26.215  1.00 107.03 ? 5   TYR   P O   1 
ATOM   26586 C  CB  . TYR   P  2  6   ? 33.153  -216.424 28.838  1.00 113.94 ? 5   TYR   P CB  1 
ATOM   26587 C  CG  . TYR   P  2  6   ? 33.778  -216.865 30.137  1.00 116.03 ? 5   TYR   P CG  1 
ATOM   26588 C  CD1 . TYR   P  2  6   ? 33.450  -218.081 30.716  1.00 117.44 ? 5   TYR   P CD1 1 
ATOM   26589 C  CD2 . TYR   P  2  6   ? 34.707  -216.070 30.789  1.00 116.66 ? 5   TYR   P CD2 1 
ATOM   26590 C  CE1 . TYR   P  2  6   ? 34.022  -218.493 31.908  1.00 118.00 ? 5   TYR   P CE1 1 
ATOM   26591 C  CE2 . TYR   P  2  6   ? 35.290  -216.467 31.981  1.00 117.36 ? 5   TYR   P CE2 1 
ATOM   26592 C  CZ  . TYR   P  2  6   ? 34.946  -217.683 32.545  1.00 117.26 ? 5   TYR   P CZ  1 
ATOM   26593 O  OH  . TYR   P  2  6   ? 35.516  -218.079 33.720  1.00 119.64 ? 5   TYR   P OH  1 
ATOM   26594 N  N   . ASP   P  2  7   ? 34.333  -215.765 25.487  1.00 107.02 ? 6   ASP   P N   1 
ATOM   26595 C  CA  . ASP   P  2  7   ? 34.058  -214.971 24.258  1.00 106.78 ? 6   ASP   P CA  1 
ATOM   26596 C  C   . ASP   P  2  7   ? 33.664  -215.924 23.123  1.00 105.33 ? 6   ASP   P C   1 
ATOM   26597 O  O   . ASP   P  2  7   ? 34.516  -216.739 22.719  1.00 107.74 ? 6   ASP   P O   1 
ATOM   26598 C  CB  . ASP   P  2  7   ? 35.273  -214.121 23.878  1.00 103.89 ? 6   ASP   P CB  1 
ATOM   26599 C  CG  . ASP   P  2  7   ? 34.965  -212.971 22.938  1.00 100.68 ? 6   ASP   P CG  1 
ATOM   26600 O  OD1 . ASP   P  2  7   ? 34.010  -213.088 22.147  1.00 101.56 ? 6   ASP   P OD1 1 
ATOM   26601 O  OD2 . ASP   P  2  7   ? 35.684  -211.964 23.013  1.00 101.83 ? 6   ASP   P OD2 1 
ATOM   26602 N  N   . SER   P  2  8   ? 32.426  -215.812 22.628  1.00 105.62 ? 7   SER   P N   1 
ATOM   26603 C  CA  . SER   P  2  8   ? 31.881  -216.606 21.494  1.00 106.71 ? 7   SER   P CA  1 
ATOM   26604 C  C   . SER   P  2  8   ? 32.581  -216.214 20.189  1.00 109.31 ? 7   SER   P C   1 
ATOM   26605 O  O   . SER   P  2  8   ? 32.613  -217.058 19.275  1.00 111.83 ? 7   SER   P O   1 
ATOM   26606 C  CB  . SER   P  2  8   ? 30.393  -216.427 21.366  1.00 107.50 ? 7   SER   P CB  1 
ATOM   26607 O  OG  . SER   P  2  8   ? 29.728  -216.801 22.562  1.00 107.12 ? 7   SER   P OG  1 
ATOM   26608 N  N   . ARG   P  2  9   ? 33.103  -214.983 20.112  1.00 109.48 ? 8   ARG   P N   1 
ATOM   26609 C  CA  . ARG   P  2  9   ? 33.683  -214.368 18.886  1.00 110.43 ? 8   ARG   P CA  1 
ATOM   26610 C  C   . ARG   P  2  9   ? 32.589  -214.315 17.812  1.00 110.61 ? 8   ARG   P C   1 
ATOM   26611 O  O   . ARG   P  2  9   ? 32.663  -215.092 16.843  1.00 110.73 ? 8   ARG   P O   1 
ATOM   26612 C  CB  . ARG   P  2  9   ? 34.922  -215.142 18.421  1.00 113.66 ? 8   ARG   P CB  1 
ATOM   26613 C  CG  . ARG   P  2  9   ? 36.106  -215.059 19.376  1.00 115.20 ? 8   ARG   P CG  1 
ATOM   26614 C  CD  . ARG   P  2  9   ? 36.826  -216.388 19.505  1.00 120.18 ? 8   ARG   P CD  1 
ATOM   26615 N  NE  . ARG   P  2  9   ? 37.553  -216.757 18.296  1.00 124.83 ? 8   ARG   P NE  1 
ATOM   26616 C  CZ  . ARG   P  2  9   ? 37.925  -217.996 17.972  1.00 128.90 ? 8   ARG   P CZ  1 
ATOM   26617 N  NH1 . ARG   P  2  9   ? 37.633  -219.021 18.757  1.00 128.89 ? 8   ARG   P NH1 1 
ATOM   26618 N  NH2 . ARG   P  2  9   ? 38.587  -218.207 16.847  1.00 131.90 ? 8   ARG   P NH2 1 
ATOM   26619 N  N   . THR   P  2  10  ? 31.602  -213.436 17.998  1.00 106.35 ? 9   THR   P N   1 
ATOM   26620 C  CA  . THR   P  2  10  ? 30.370  -213.363 17.168  1.00 106.06 ? 9   THR   P CA  1 
ATOM   26621 C  C   . THR   P  2  10  ? 30.706  -212.895 15.750  1.00 107.54 ? 9   THR   P C   1 
ATOM   26622 O  O   . THR   P  2  10  ? 29.978  -213.304 14.826  1.00 112.77 ? 9   THR   P O   1 
ATOM   26623 C  CB  . THR   P  2  10  ? 29.321  -212.442 17.801  1.00 104.33 ? 9   THR   P CB  1 
ATOM   26624 O  OG1 . THR   P  2  10  ? 29.909  -211.157 18.003  1.00 102.70 ? 9   THR   P OG1 1 
ATOM   26625 C  CG2 . THR   P  2  10  ? 28.797  -212.982 19.114  1.00 105.26 ? 9   THR   P CG2 1 
ATOM   26626 N  N   . THR   P  2  11  ? 31.757  -212.082 15.589  1.00 109.29 ? 10  THR   P N   1 
ATOM   26627 C  CA  . THR   P  2  11  ? 32.106  -211.388 14.319  1.00 107.98 ? 10  THR   P CA  1 
ATOM   26628 C  C   . THR   P  2  11  ? 33.357  -212.013 13.690  1.00 111.27 ? 10  THR   P C   1 
ATOM   26629 O  O   . THR   P  2  11  ? 34.305  -211.255 13.408  1.00 114.43 ? 10  THR   P O   1 
ATOM   26630 C  CB  . THR   P  2  11  ? 32.312  -209.883 14.549  1.00 104.80 ? 10  THR   P CB  1 
ATOM   26631 O  OG1 . THR   P  2  11  ? 33.463  -209.679 15.369  1.00 105.25 ? 10  THR   P OG1 1 
ATOM   26632 C  CG2 . THR   P  2  11  ? 31.119  -209.223 15.201  1.00 102.07 ? 10  THR   P CG2 1 
ATOM   26633 N  N   . ILE   P  2  12  ? 33.362  -213.331 13.461  1.00 112.07 ? 11  ILE   P N   1 
ATOM   26634 C  CA  . ILE   P  2  12  ? 34.482  -214.025 12.755  1.00 111.19 ? 11  ILE   P CA  1 
ATOM   26635 C  C   . ILE   P  2  12  ? 33.934  -214.833 11.577  1.00 107.69 ? 11  ILE   P C   1 
ATOM   26636 O  O   . ILE   P  2  12  ? 32.704  -215.021 11.489  1.00 104.02 ? 11  ILE   P O   1 
ATOM   26637 C  CB  . ILE   P  2  12  ? 35.324  -214.903 13.705  1.00 115.02 ? 11  ILE   P CB  1 
ATOM   26638 C  CG1 . ILE   P  2  12  ? 34.532  -216.071 14.299  1.00 113.48 ? 11  ILE   P CG1 1 
ATOM   26639 C  CG2 . ILE   P  2  12  ? 35.971  -214.047 14.783  1.00 119.06 ? 11  ILE   P CG2 1 
ATOM   26640 C  CD1 . ILE   P  2  12  ? 35.403  -217.201 14.797  1.00 115.75 ? 11  ILE   P CD1 1 
ATOM   26641 N  N   . PHE   P  2  13  ? 34.853  -215.286 10.724  1.00 108.21 ? 12  PHE   P N   1 
ATOM   26642 C  CA  . PHE   P  2  13  ? 34.605  -216.089 9.502   1.00 112.85 ? 12  PHE   P CA  1 
ATOM   26643 C  C   . PHE   P  2  13  ? 34.777  -217.573 9.839   1.00 116.65 ? 12  PHE   P C   1 
ATOM   26644 O  O   . PHE   P  2  13  ? 35.657  -217.912 10.658  1.00 119.60 ? 12  PHE   P O   1 
ATOM   26645 C  CB  . PHE   P  2  13  ? 35.586  -215.699 8.393   1.00 113.10 ? 12  PHE   P CB  1 
ATOM   26646 C  CG  . PHE   P  2  13  ? 35.244  -214.443 7.632   1.00 108.61 ? 12  PHE   P CG  1 
ATOM   26647 C  CD1 . PHE   P  2  13  ? 34.132  -214.398 6.806   1.00 107.79 ? 12  PHE   P CD1 1 
ATOM   26648 C  CD2 . PHE   P  2  13  ? 36.055  -213.321 7.708   1.00 105.40 ? 12  PHE   P CD2 1 
ATOM   26649 C  CE1 . PHE   P  2  13  ? 33.824  -213.251 6.093   1.00 105.98 ? 12  PHE   P CE1 1 
ATOM   26650 C  CE2 . PHE   P  2  13  ? 35.746  -212.174 6.994   1.00 105.31 ? 12  PHE   P CE2 1 
ATOM   26651 C  CZ  . PHE   P  2  13  ? 34.632  -212.141 6.187   1.00 105.37 ? 12  PHE   P CZ  1 
ATOM   26652 N  N   . SER   P  2  14  ? 33.966  -218.429 9.216   1.00 118.66 ? 13  SER   P N   1 
ATOM   26653 C  CA  . SER   P  2  14  ? 34.182  -219.897 9.173   1.00 121.30 ? 13  SER   P CA  1 
ATOM   26654 C  C   . SER   P  2  14  ? 35.310  -220.175 8.183   1.00 120.09 ? 13  SER   P C   1 
ATOM   26655 O  O   . SER   P  2  14  ? 35.616  -219.327 7.345   1.00 116.98 ? 13  SER   P O   1 
ATOM   26656 C  CB  . SER   P  2  14  ? 32.913  -220.629 8.809   1.00 122.04 ? 13  SER   P CB  1 
ATOM   26657 O  OG  . SER   P  2  14  ? 32.538  -220.368 7.464   1.00 124.50 ? 13  SER   P OG  1 
ATOM   26658 N  N   . PRO   P  2  15  ? 35.973  -221.352 8.243   1.00 122.23 ? 14  PRO   P N   1 
ATOM   26659 C  CA  . PRO   P  2  15  ? 36.978  -221.714 7.240   1.00 122.68 ? 14  PRO   P CA  1 
ATOM   26660 C  C   . PRO   P  2  15  ? 36.472  -221.604 5.790   1.00 119.99 ? 14  PRO   P C   1 
ATOM   26661 O  O   . PRO   P  2  15  ? 37.295  -221.444 4.906   1.00 114.89 ? 14  PRO   P O   1 
ATOM   26662 C  CB  . PRO   P  2  15  ? 37.312  -223.174 7.581   1.00 125.28 ? 14  PRO   P CB  1 
ATOM   26663 C  CG  . PRO   P  2  15  ? 37.001  -223.294 9.059   1.00 126.23 ? 14  PRO   P CG  1 
ATOM   26664 C  CD  . PRO   P  2  15  ? 35.816  -222.379 9.285   1.00 122.59 ? 14  PRO   P CD  1 
ATOM   26665 N  N   . GLU   P  2  16  ? 35.149  -221.683 5.592   1.00 123.12 ? 15  GLU   P N   1 
ATOM   26666 C  CA  . GLU   P  2  16  ? 34.466  -221.614 4.270   1.00 126.89 ? 15  GLU   P CA  1 
ATOM   26667 C  C   . GLU   P  2  16  ? 34.179  -220.154 3.885   1.00 122.96 ? 15  GLU   P C   1 
ATOM   26668 O  O   . GLU   P  2  16  ? 33.714  -219.935 2.753   1.00 128.90 ? 15  GLU   P O   1 
ATOM   26669 C  CB  . GLU   P  2  16  ? 33.165  -222.422 4.296   1.00 131.82 ? 15  GLU   P CB  1 
ATOM   26670 C  CG  . GLU   P  2  16  ? 33.372  -223.912 4.522   1.00 136.10 ? 15  GLU   P CG  1 
ATOM   26671 C  CD  . GLU   P  2  16  ? 33.521  -224.339 5.974   1.00 138.23 ? 15  GLU   P CD  1 
ATOM   26672 O  OE1 . GLU   P  2  16  ? 34.413  -225.164 6.257   1.00 137.33 ? 15  GLU   P OE1 1 
ATOM   26673 O  OE2 . GLU   P  2  16  ? 32.742  -223.849 6.820   1.00 144.97 ? 15  GLU   P OE2 1 
ATOM   26674 N  N   . GLY   P  2  17  ? 34.435  -219.194 4.781   1.00 120.06 ? 16  GLY   P N   1 
ATOM   26675 C  CA  . GLY   P  2  17  ? 34.236  -217.754 4.527   1.00 115.60 ? 16  GLY   P CA  1 
ATOM   26676 C  C   . GLY   P  2  17  ? 32.786  -217.333 4.701   1.00 112.66 ? 16  GLY   P C   1 
ATOM   26677 O  O   . GLY   P  2  17  ? 32.329  -216.471 3.925   1.00 111.39 ? 16  GLY   P O   1 
ATOM   26678 N  N   . ARG   P  2  18  ? 32.088  -217.924 5.677   1.00 110.38 ? 17  ARG   P N   1 
ATOM   26679 C  CA  . ARG   P  2  18  ? 30.716  -217.535 6.102   1.00 110.71 ? 17  ARG   P CA  1 
ATOM   26680 C  C   . ARG   P  2  18  ? 30.777  -216.980 7.526   1.00 105.95 ? 17  ARG   P C   1 
ATOM   26681 O  O   . ARG   P  2  18  ? 31.697  -217.367 8.271   1.00 105.01 ? 17  ARG   P O   1 
ATOM   26682 C  CB  . ARG   P  2  18  ? 29.764  -218.734 6.080   1.00 113.93 ? 17  ARG   P CB  1 
ATOM   26683 C  CG  . ARG   P  2  18  ? 29.535  -219.336 4.702   1.00 120.90 ? 17  ARG   P CG  1 
ATOM   26684 C  CD  . ARG   P  2  18  ? 28.864  -220.693 4.803   1.00 125.92 ? 17  ARG   P CD  1 
ATOM   26685 N  NE  . ARG   P  2  18  ? 28.598  -221.267 3.490   1.00 131.31 ? 17  ARG   P NE  1 
ATOM   26686 C  CZ  . ARG   P  2  18  ? 27.570  -220.947 2.705   1.00 132.86 ? 17  ARG   P CZ  1 
ATOM   26687 N  NH1 . ARG   P  2  18  ? 26.680  -220.043 3.085   1.00 132.44 ? 17  ARG   P NH1 1 
ATOM   26688 N  NH2 . ARG   P  2  18  ? 27.435  -221.538 1.530   1.00 137.37 ? 17  ARG   P NH2 1 
ATOM   26689 N  N   . LEU   P  2  19  ? 29.817  -216.126 7.887   1.00 106.11 ? 18  LEU   P N   1 
ATOM   26690 C  CA  . LEU   P  2  19  ? 29.688  -215.538 9.245   1.00 106.23 ? 18  LEU   P CA  1 
ATOM   26691 C  C   . LEU   P  2  19  ? 28.730  -216.410 10.065  1.00 105.64 ? 18  LEU   P C   1 
ATOM   26692 O  O   . LEU   P  2  19  ? 27.508  -216.321 9.843   1.00 104.09 ? 18  LEU   P O   1 
ATOM   26693 C  CB  . LEU   P  2  19  ? 29.199  -214.090 9.124   1.00 104.66 ? 18  LEU   P CB  1 
ATOM   26694 C  CG  . LEU   P  2  19  ? 30.125  -213.147 8.355   1.00 103.83 ? 18  LEU   P CG  1 
ATOM   26695 C  CD1 . LEU   P  2  19  ? 29.454  -211.804 8.121   1.00 103.95 ? 18  LEU   P CD1 1 
ATOM   26696 C  CD2 . LEU   P  2  19  ? 31.449  -212.957 9.081   1.00 104.99 ? 18  LEU   P CD2 1 
ATOM   26697 N  N   . TYR   P  2  20  ? 29.284  -217.234 10.959  1.00 107.15 ? 19  TYR   P N   1 
ATOM   26698 C  CA  . TYR   P  2  20  ? 28.551  -218.204 11.816  1.00 112.46 ? 19  TYR   P CA  1 
ATOM   26699 C  C   . TYR   P  2  20  ? 27.230  -217.592 12.297  1.00 110.85 ? 19  TYR   P C   1 
ATOM   26700 O  O   . TYR   P  2  20  ? 26.154  -218.143 11.990  1.00 107.90 ? 19  TYR   P O   1 
ATOM   26701 C  CB  . TYR   P  2  20  ? 29.403  -218.612 13.023  1.00 116.80 ? 19  TYR   P CB  1 
ATOM   26702 C  CG  . TYR   P  2  20  ? 30.568  -219.520 12.715  1.00 123.79 ? 19  TYR   P CG  1 
ATOM   26703 C  CD1 . TYR   P  2  20  ? 30.367  -220.808 12.239  1.00 127.54 ? 19  TYR   P CD1 1 
ATOM   26704 C  CD2 . TYR   P  2  20  ? 31.875  -219.105 12.926  1.00 127.89 ? 19  TYR   P CD2 1 
ATOM   26705 C  CE1 . TYR   P  2  20  ? 31.432  -221.652 11.966  1.00 129.83 ? 19  TYR   P CE1 1 
ATOM   26706 C  CE2 . TYR   P  2  20  ? 32.951  -219.938 12.660  1.00 131.47 ? 19  TYR   P CE2 1 
ATOM   26707 C  CZ  . TYR   P  2  20  ? 32.729  -221.217 12.178  1.00 132.36 ? 19  TYR   P CZ  1 
ATOM   26708 O  OH  . TYR   P  2  20  ? 33.783  -222.045 11.912  1.00 132.46 ? 19  TYR   P OH  1 
ATOM   26709 N  N   . GLN   P  2  21  ? 27.325  -216.474 13.023  1.00 108.95 ? 20  GLN   P N   1 
ATOM   26710 C  CA  . GLN   P  2  21  ? 26.201  -215.851 13.773  1.00 107.19 ? 20  GLN   P CA  1 
ATOM   26711 C  C   . GLN   P  2  21  ? 25.102  -215.390 12.810  1.00 108.02 ? 20  GLN   P C   1 
ATOM   26712 O  O   . GLN   P  2  21  ? 23.916  -215.557 13.162  1.00 109.43 ? 20  GLN   P O   1 
ATOM   26713 C  CB  . GLN   P  2  21  ? 26.718  -214.699 14.633  1.00 106.98 ? 20  GLN   P CB  1 
ATOM   26714 C  CG  . GLN   P  2  21  ? 27.393  -215.177 15.908  1.00 110.29 ? 20  GLN   P CG  1 
ATOM   26715 C  CD  . GLN   P  2  21  ? 26.388  -215.712 16.896  1.00 112.00 ? 20  GLN   P CD  1 
ATOM   26716 O  OE1 . GLN   P  2  21  ? 26.275  -216.917 17.113  1.00 112.81 ? 20  GLN   P OE1 1 
ATOM   26717 N  NE2 . GLN   P  2  21  ? 25.637  -214.803 17.497  1.00 114.29 ? 20  GLN   P NE2 1 
ATOM   26718 N  N   . VAL   P  2  22  ? 25.480  -214.839 11.652  1.00 105.05 ? 21  VAL   P N   1 
ATOM   26719 C  CA  . VAL   P  2  22  ? 24.527  -214.377 10.598  1.00 103.56 ? 21  VAL   P CA  1 
ATOM   26720 C  C   . VAL   P  2  22  ? 23.752  -215.596 10.088  1.00 104.30 ? 21  VAL   P C   1 
ATOM   26721 O  O   . VAL   P  2  22  ? 22.510  -215.515 10.005  1.00 98.52  ? 21  VAL   P O   1 
ATOM   26722 C  CB  . VAL   P  2  22  ? 25.243  -213.646 9.446   1.00 104.57 ? 21  VAL   P CB  1 
ATOM   26723 C  CG1 . VAL   P  2  22  ? 24.296  -213.344 8.294   1.00 104.67 ? 21  VAL   P CG1 1 
ATOM   26724 C  CG2 . VAL   P  2  22  ? 25.921  -212.371 9.922   1.00 103.83 ? 21  VAL   P CG2 1 
ATOM   26725 N  N   . GLU   P  2  23  ? 24.468  -216.676 9.766   1.00 105.13 ? 22  GLU   P N   1 
ATOM   26726 C  CA  . GLU   P  2  23  ? 23.879  -217.945 9.267   1.00 106.54 ? 22  GLU   P CA  1 
ATOM   26727 C  C   . GLU   P  2  23  ? 22.879  -218.464 10.305  1.00 101.40 ? 22  GLU   P C   1 
ATOM   26728 O  O   . GLU   P  2  23  ? 21.748  -218.801 9.910   1.00 102.34 ? 22  GLU   P O   1 
ATOM   26729 C  CB  . GLU   P  2  23  ? 24.971  -218.977 8.973   1.00 110.96 ? 22  GLU   P CB  1 
ATOM   26730 C  CG  . GLU   P  2  23  ? 25.928  -218.560 7.868   1.00 115.70 ? 22  GLU   P CG  1 
ATOM   26731 C  CD  . GLU   P  2  23  ? 25.269  -218.257 6.532   1.00 117.73 ? 22  GLU   P CD  1 
ATOM   26732 O  OE1 . GLU   P  2  23  ? 25.594  -217.211 5.935   1.00 120.71 ? 22  GLU   P OE1 1 
ATOM   26733 O  OE2 . GLU   P  2  23  ? 24.431  -219.069 6.091   1.00 125.09 ? 22  GLU   P OE2 1 
ATOM   26734 N  N   . TYR   P  2  24  ? 23.272  -218.493 11.583  1.00 100.14 ? 23  TYR   P N   1 
ATOM   26735 C  CA  . TYR   P  2  24  ? 22.462  -219.062 12.693  1.00 101.03 ? 23  TYR   P CA  1 
ATOM   26736 C  C   . TYR   P  2  24  ? 21.258  -218.158 12.983  1.00 100.72 ? 23  TYR   P C   1 
ATOM   26737 O  O   . TYR   P  2  24  ? 20.207  -218.680 13.405  1.00 102.63 ? 23  TYR   P O   1 
ATOM   26738 C  CB  . TYR   P  2  24  ? 23.309  -219.280 13.950  1.00 102.37 ? 23  TYR   P CB  1 
ATOM   26739 C  CG  . TYR   P  2  24  ? 24.507  -220.186 13.794  1.00 101.54 ? 23  TYR   P CG  1 
ATOM   26740 C  CD1 . TYR   P  2  24  ? 24.627  -221.078 12.737  1.00 101.66 ? 23  TYR   P CD1 1 
ATOM   26741 C  CD2 . TYR   P  2  24  ? 25.520  -220.171 14.736  1.00 102.66 ? 23  TYR   P CD2 1 
ATOM   26742 C  CE1 . TYR   P  2  24  ? 25.730  -221.908 12.609  1.00 102.66 ? 23  TYR   P CE1 1 
ATOM   26743 C  CE2 . TYR   P  2  24  ? 26.627  -220.997 14.628  1.00 102.62 ? 23  TYR   P CE2 1 
ATOM   26744 C  CZ  . TYR   P  2  24  ? 26.734  -221.869 13.560  1.00 102.51 ? 23  TYR   P CZ  1 
ATOM   26745 O  OH  . TYR   P  2  24  ? 27.824  -222.682 13.456  1.00 105.53 ? 23  TYR   P OH  1 
ATOM   26746 N  N   . ALA   P  2  25  ? 21.400  -216.847 12.769  1.00 99.13  ? 24  ALA   P N   1 
ATOM   26747 C  CA  . ALA   P  2  25  ? 20.306  -215.860 12.918  1.00 99.80  ? 24  ALA   P CA  1 
ATOM   26748 C  C   . ALA   P  2  25  ? 19.256  -216.088 11.825  1.00 100.30 ? 24  ALA   P C   1 
ATOM   26749 O  O   . ALA   P  2  25  ? 18.053  -216.028 12.147  1.00 98.77  ? 24  ALA   P O   1 
ATOM   26750 C  CB  . ALA   P  2  25  ? 20.856  -214.459 12.873  1.00 99.07  ? 24  ALA   P CB  1 
ATOM   26751 N  N   . LEU   P  2  26  ? 19.696  -216.337 10.585  1.00 103.68 ? 25  LEU   P N   1 
ATOM   26752 C  CA  . LEU   P  2  26  ? 18.810  -216.647 9.427   1.00 104.79 ? 25  LEU   P CA  1 
ATOM   26753 C  C   . LEU   P  2  26  ? 18.036  -217.938 9.714   1.00 107.26 ? 25  LEU   P C   1 
ATOM   26754 O  O   . LEU   P  2  26  ? 16.829  -217.979 9.398   1.00 107.67 ? 25  LEU   P O   1 
ATOM   26755 C  CB  . LEU   P  2  26  ? 19.641  -216.777 8.145   1.00 105.03 ? 25  LEU   P CB  1 
ATOM   26756 C  CG  . LEU   P  2  26  ? 20.124  -215.461 7.534   1.00 103.85 ? 25  LEU   P CG  1 
ATOM   26757 C  CD1 . LEU   P  2  26  ? 21.240  -215.707 6.531   1.00 103.75 ? 25  LEU   P CD1 1 
ATOM   26758 C  CD2 . LEU   P  2  26  ? 18.974  -214.708 6.878   1.00 103.49 ? 25  LEU   P CD2 1 
ATOM   26759 N  N   . GLU   P  2  27  ? 18.708  -218.940 10.293  1.00 110.09 ? 26  GLU   P N   1 
ATOM   26760 C  CA  . GLU   P  2  27  ? 18.101  -220.236 10.701  1.00 113.50 ? 26  GLU   P CA  1 
ATOM   26761 C  C   . GLU   P  2  27  ? 16.999  -219.964 11.734  1.00 112.77 ? 26  GLU   P C   1 
ATOM   26762 O  O   . GLU   P  2  27  ? 15.952  -220.640 11.667  1.00 116.91 ? 26  GLU   P O   1 
ATOM   26763 C  CB  . GLU   P  2  27  ? 19.172  -221.186 11.245  1.00 117.62 ? 26  GLU   P CB  1 
ATOM   26764 C  CG  . GLU   P  2  27  ? 18.636  -222.544 11.666  1.00 121.52 ? 26  GLU   P CG  1 
ATOM   26765 C  CD  . GLU   P  2  27  ? 17.936  -223.325 10.568  1.00 125.13 ? 26  GLU   P CD  1 
ATOM   26766 O  OE1 . GLU   P  2  27  ? 16.921  -223.987 10.869  1.00 130.61 ? 26  GLU   P OE1 1 
ATOM   26767 O  OE2 . GLU   P  2  27  ? 18.409  -223.271 9.414   1.00 126.96 ? 26  GLU   P OE2 1 
ATOM   26768 N  N   . SER   P  2  28  ? 17.229  -219.010 12.645  1.00 108.89 ? 27  SER   P N   1 
ATOM   26769 C  CA  . SER   P  2  28  ? 16.253  -218.550 13.669  1.00 106.00 ? 27  SER   P CA  1 
ATOM   26770 C  C   . SER   P  2  28  ? 15.025  -217.941 12.983  1.00 105.06 ? 27  SER   P C   1 
ATOM   26771 O  O   . SER   P  2  28  ? 13.895  -218.271 13.394  1.00 105.17 ? 27  SER   P O   1 
ATOM   26772 C  CB  . SER   P  2  28  ? 16.887  -217.568 14.623  1.00 104.07 ? 27  SER   P CB  1 
ATOM   26773 O  OG  . SER   P  2  28  ? 15.954  -217.123 15.595  1.00 105.48 ? 27  SER   P OG  1 
ATOM   26774 N  N   . ILE   P  2  29  ? 15.251  -217.094 11.974  1.00 104.02 ? 28  ILE   P N   1 
ATOM   26775 C  CA  . ILE   P  2  29  ? 14.194  -216.326 11.248  1.00 104.44 ? 28  ILE   P CA  1 
ATOM   26776 C  C   . ILE   P  2  29  ? 13.307  -217.292 10.452  1.00 104.56 ? 28  ILE   P C   1 
ATOM   26777 O  O   . ILE   P  2  29  ? 12.101  -217.006 10.334  1.00 100.15 ? 28  ILE   P O   1 
ATOM   26778 C  CB  . ILE   P  2  29  ? 14.825  -215.232 10.358  1.00 106.89 ? 28  ILE   P CB  1 
ATOM   26779 C  CG1 . ILE   P  2  29  ? 15.399  -214.093 11.206  1.00 105.87 ? 28  ILE   P CG1 1 
ATOM   26780 C  CG2 . ILE   P  2  29  ? 13.832  -214.707 9.328   1.00 109.26 ? 28  ILE   P CG2 1 
ATOM   26781 C  CD1 . ILE   P  2  29  ? 16.516  -213.328 10.539  1.00 102.81 ? 28  ILE   P CD1 1 
ATOM   26782 N  N   . SER   P  2  30  ? 13.870  -218.398 9.952   1.00 103.53 ? 29  SER   P N   1 
ATOM   26783 C  CA  . SER   P  2  30  ? 13.162  -219.410 9.123   1.00 103.69 ? 29  SER   P CA  1 
ATOM   26784 C  C   . SER   P  2  30  ? 12.042  -220.100 9.921   1.00 105.62 ? 29  SER   P C   1 
ATOM   26785 O  O   . SER   P  2  30  ? 11.218  -220.782 9.285   1.00 105.78 ? 29  SER   P O   1 
ATOM   26786 C  CB  . SER   P  2  30  ? 14.129  -220.416 8.553   1.00 103.44 ? 29  SER   P CB  1 
ATOM   26787 O  OG  . SER   P  2  30  ? 14.562  -221.323 9.555   1.00 105.06 ? 29  SER   P OG  1 
ATOM   26788 N  N   . HIS   P  2  31  ? 12.010  -219.946 11.251  1.00 103.33 ? 30  HIS   P N   1 
ATOM   26789 C  CA  . HIS   P  2  31  ? 10.952  -220.502 12.140  1.00 107.77 ? 30  HIS   P CA  1 
ATOM   26790 C  C   . HIS   P  2  31  ? 9.919   -219.429 12.515  1.00 105.74 ? 30  HIS   P C   1 
ATOM   26791 O  O   . HIS   P  2  31  ? 8.897   -219.799 13.123  1.00 104.24 ? 30  HIS   P O   1 
ATOM   26792 C  CB  . HIS   P  2  31  ? 11.568  -221.130 13.396  1.00 111.43 ? 30  HIS   P CB  1 
ATOM   26793 C  CG  . HIS   P  2  31  ? 12.601  -222.168 13.110  1.00 118.75 ? 30  HIS   P CG  1 
ATOM   26794 N  ND1 . HIS   P  2  31  ? 12.330  -223.294 12.352  1.00 120.92 ? 30  HIS   P ND1 1 
ATOM   26795 C  CD2 . HIS   P  2  31  ? 13.894  -222.264 13.487  1.00 118.87 ? 30  HIS   P CD2 1 
ATOM   26796 C  CE1 . HIS   P  2  31  ? 13.418  -224.033 12.267  1.00 123.78 ? 30  HIS   P CE1 1 
ATOM   26797 N  NE2 . HIS   P  2  31  ? 14.393  -223.423 12.956  1.00 122.05 ? 30  HIS   P NE2 1 
ATOM   26798 N  N   . ALA   P  2  32  ? 10.170  -218.158 12.183  1.00 103.52 ? 31  ALA   P N   1 
ATOM   26799 C  CA  . ALA   P  2  32  ? 9.244   -217.026 12.434  1.00 103.54 ? 31  ALA   P CA  1 
ATOM   26800 C  C   . ALA   P  2  32  ? 8.128   -217.029 11.383  1.00 105.01 ? 31  ALA   P C   1 
ATOM   26801 O  O   . ALA   P  2  32  ? 8.400   -217.426 10.232  1.00 109.35 ? 31  ALA   P O   1 
ATOM   26802 C  CB  . ALA   P  2  32  ? 9.994   -215.719 12.419  1.00 101.97 ? 31  ALA   P CB  1 
ATOM   26803 N  N   . GLY   P  2  33  ? 6.926   -216.588 11.771  1.00 104.49 ? 32  GLY   P N   1 
ATOM   26804 C  CA  . GLY   P  2  33  ? 5.739   -216.532 10.896  1.00 105.61 ? 32  GLY   P CA  1 
ATOM   26805 C  C   . GLY   P  2  33  ? 6.067   -215.874 9.569   1.00 105.34 ? 32  GLY   P C   1 
ATOM   26806 O  O   . GLY   P  2  33  ? 6.807   -214.872 9.575   1.00 106.76 ? 32  GLY   P O   1 
ATOM   26807 N  N   . THR   P  2  34  ? 5.557   -216.425 8.466   1.00 106.56 ? 33  THR   P N   1 
ATOM   26808 C  CA  . THR   P  2  34  ? 5.808   -215.915 7.092   1.00 106.73 ? 33  THR   P CA  1 
ATOM   26809 C  C   . THR   P  2  34  ? 5.284   -214.476 6.998   1.00 104.53 ? 33  THR   P C   1 
ATOM   26810 O  O   . THR   P  2  34  ? 4.269   -214.164 7.658   1.00 102.27 ? 33  THR   P O   1 
ATOM   26811 C  CB  . THR   P  2  34  ? 5.189   -216.827 6.022   1.00 109.76 ? 33  THR   P CB  1 
ATOM   26812 O  OG1 . THR   P  2  34  ? 5.466   -218.188 6.358   1.00 108.14 ? 33  THR   P OG1 1 
ATOM   26813 C  CG2 . THR   P  2  34  ? 5.709   -216.527 4.631   1.00 110.46 ? 33  THR   P CG2 1 
ATOM   26814 N  N   . ALA   P  2  35  ? 5.980   -213.633 6.234   1.00 102.20 ? 34  ALA   P N   1 
ATOM   26815 C  CA  . ALA   P  2  35  ? 5.527   -212.287 5.816   1.00 101.56 ? 34  ALA   P CA  1 
ATOM   26816 C  C   . ALA   P  2  35  ? 5.776   -212.136 4.315   1.00 103.40 ? 34  ALA   P C   1 
ATOM   26817 O  O   . ALA   P  2  35  ? 6.875   -212.509 3.864   1.00 104.41 ? 34  ALA   P O   1 
ATOM   26818 C  CB  . ALA   P  2  35  ? 6.238   -211.222 6.607   1.00 99.14  ? 34  ALA   P CB  1 
ATOM   26819 N  N   . ILE   P  2  36  ? 4.782   -211.635 3.578   1.00 105.91 ? 35  ILE   P N   1 
ATOM   26820 C  CA  . ILE   P  2  36  ? 4.833   -211.463 2.096   1.00 104.89 ? 35  ILE   P CA  1 
ATOM   26821 C  C   . ILE   P  2  36  ? 4.652   -209.978 1.766   1.00 103.29 ? 35  ILE   P C   1 
ATOM   26822 O  O   . ILE   P  2  36  ? 3.820   -209.312 2.414   1.00 99.30  ? 35  ILE   P O   1 
ATOM   26823 C  CB  . ILE   P  2  36  ? 3.790   -212.365 1.403   1.00 108.25 ? 35  ILE   P CB  1 
ATOM   26824 C  CG1 . ILE   P  2  36  ? 4.202   -213.837 1.501   1.00 110.78 ? 35  ILE   P CG1 1 
ATOM   26825 C  CG2 . ILE   P  2  36  ? 3.562   -211.936 -0.042  1.00 107.64 ? 35  ILE   P CG2 1 
ATOM   26826 C  CD1 . ILE   P  2  36  ? 3.175   -214.820 0.985   1.00 115.21 ? 35  ILE   P CD1 1 
ATOM   26827 N  N   . GLY   P  2  37  ? 5.440   -209.491 0.807   1.00 100.44 ? 36  GLY   P N   1 
ATOM   26828 C  CA  . GLY   P  2  37  ? 5.250   -208.190 0.144   1.00 102.06 ? 36  GLY   P CA  1 
ATOM   26829 C  C   . GLY   P  2  37  ? 5.052   -208.391 -1.346  1.00 103.94 ? 36  GLY   P C   1 
ATOM   26830 O  O   . GLY   P  2  37  ? 5.824   -209.174 -1.930  1.00 106.00 ? 36  GLY   P O   1 
ATOM   26831 N  N   . ILE   P  2  38  ? 4.042   -207.740 -1.935  1.00 106.85 ? 37  ILE   P N   1 
ATOM   26832 C  CA  . ILE   P  2  38  ? 3.768   -207.774 -3.404  1.00 108.18 ? 37  ILE   P CA  1 
ATOM   26833 C  C   . ILE   P  2  38  ? 3.551   -206.346 -3.909  1.00 108.10 ? 37  ILE   P C   1 
ATOM   26834 O  O   . ILE   P  2  38  ? 2.615   -205.682 -3.420  1.00 104.80 ? 37  ILE   P O   1 
ATOM   26835 C  CB  . ILE   P  2  38  ? 2.562   -208.670 -3.736  1.00 109.04 ? 37  ILE   P CB  1 
ATOM   26836 C  CG1 . ILE   P  2  38  ? 2.809   -210.120 -3.315  1.00 108.20 ? 37  ILE   P CG1 1 
ATOM   26837 C  CG2 . ILE   P  2  38  ? 2.216   -208.561 -5.214  1.00 112.65 ? 37  ILE   P CG2 1 
ATOM   26838 C  CD1 . ILE   P  2  38  ? 1.595   -211.006 -3.429  1.00 110.65 ? 37  ILE   P CD1 1 
ATOM   26839 N  N   . MET   P  2  39  ? 4.369   -205.928 -4.879  1.00 110.80 ? 38  MET   P N   1 
ATOM   26840 C  CA  . MET   P  2  39  ? 4.365   -204.569 -5.480  1.00 115.25 ? 38  MET   P CA  1 
ATOM   26841 C  C   . MET   P  2  39  ? 3.555   -204.609 -6.781  1.00 110.69 ? 38  MET   P C   1 
ATOM   26842 O  O   . MET   P  2  39  ? 3.992   -205.282 -7.733  1.00 103.59 ? 38  MET   P O   1 
ATOM   26843 C  CB  . MET   P  2  39  ? 5.800   -204.100 -5.754  1.00 120.14 ? 38  MET   P CB  1 
ATOM   26844 C  CG  . MET   P  2  39  ? 5.921   -202.628 -6.108  1.00 127.86 ? 38  MET   P CG  1 
ATOM   26845 S  SD  . MET   P  2  39  ? 5.999   -202.342 -7.892  1.00 140.28 ? 38  MET   P SD  1 
ATOM   26846 C  CE  . MET   P  2  39  ? 7.626   -202.990 -8.273  1.00 137.95 ? 38  MET   P CE  1 
ATOM   26847 N  N   . ALA   P  2  40  ? 2.400   -203.938 -6.792  1.00 114.03 ? 39  ALA   P N   1 
ATOM   26848 C  CA  . ALA   P  2  40  ? 1.552   -203.714 -7.986  1.00 116.23 ? 39  ALA   P CA  1 
ATOM   26849 C  C   . ALA   P  2  40  ? 1.896   -202.349 -8.593  1.00 117.55 ? 39  ALA   P C   1 
ATOM   26850 O  O   . ALA   P  2  40  ? 2.689   -201.607 -7.978  1.00 118.50 ? 39  ALA   P O   1 
ATOM   26851 C  CB  . ALA   P  2  40  ? 0.094   -203.805 -7.611  1.00 116.97 ? 39  ALA   P CB  1 
ATOM   26852 N  N   . SER   P  2  41  ? 1.320   -202.034 -9.755  1.00 118.99 ? 40  SER   P N   1 
ATOM   26853 C  CA  . SER   P  2  41  ? 1.560   -200.772 -10.503 1.00 118.63 ? 40  SER   P CA  1 
ATOM   26854 C  C   . SER   P  2  41  ? 0.897   -199.585 -9.792  1.00 117.04 ? 40  SER   P C   1 
ATOM   26855 O  O   . SER   P  2  41  ? 1.408   -198.464 -9.953  1.00 118.95 ? 40  SER   P O   1 
ATOM   26856 C  CB  . SER   P  2  41  ? 1.090   -200.887 -11.930 1.00 121.14 ? 40  SER   P CB  1 
ATOM   26857 O  OG  . SER   P  2  41  ? -0.235  -201.391 -11.987 1.00 120.85 ? 40  SER   P OG  1 
ATOM   26858 N  N   . ASP   P  2  42  ? -0.181  -199.823 -9.033  1.00 116.60 ? 41  ASP   P N   1 
ATOM   26859 C  CA  . ASP   P  2  42  ? -0.992  -198.764 -8.369  1.00 117.71 ? 41  ASP   P CA  1 
ATOM   26860 C  C   . ASP   P  2  42  ? -0.992  -198.950 -6.844  1.00 118.11 ? 41  ASP   P C   1 
ATOM   26861 O  O   . ASP   P  2  42  ? -1.930  -198.439 -6.195  1.00 122.06 ? 41  ASP   P O   1 
ATOM   26862 C  CB  . ASP   P  2  42  ? -2.425  -198.754 -8.905  1.00 118.33 ? 41  ASP   P CB  1 
ATOM   26863 C  CG  . ASP   P  2  42  ? -3.176  -200.043 -8.629  1.00 117.46 ? 41  ASP   P CG  1 
ATOM   26864 O  OD1 . ASP   P  2  42  ? -2.585  -201.117 -8.845  1.00 115.82 ? 41  ASP   P OD1 1 
ATOM   26865 O  OD2 . ASP   P  2  42  ? -4.335  -199.960 -8.184  1.00 120.83 ? 41  ASP   P OD2 1 
ATOM   26866 N  N   . GLY   P  2  43  ? 0.012   -199.634 -6.284  1.00 117.46 ? 42  GLY   P N   1 
ATOM   26867 C  CA  . GLY   P  2  43  ? 0.176   -199.774 -4.823  1.00 118.43 ? 42  GLY   P CA  1 
ATOM   26868 C  C   . GLY   P  2  43  ? 0.959   -201.014 -4.424  1.00 116.62 ? 42  GLY   P C   1 
ATOM   26869 O  O   . GLY   P  2  43  ? 1.371   -201.781 -5.319  1.00 120.92 ? 42  GLY   P O   1 
ATOM   26870 N  N   . ILE   P  2  44  ? 1.158   -201.191 -3.113  1.00 112.47 ? 43  ILE   P N   1 
ATOM   26871 C  CA  . ILE   P  2  44  ? 1.888   -202.340 -2.502  1.00 108.68 ? 43  ILE   P CA  1 
ATOM   26872 C  C   . ILE   P  2  44  ? 0.977   -203.003 -1.466  1.00 109.16 ? 43  ILE   P C   1 
ATOM   26873 O  O   . ILE   P  2  44  ? 0.230   -202.274 -0.780  1.00 106.87 ? 43  ILE   P O   1 
ATOM   26874 C  CB  . ILE   P  2  44  ? 3.216   -201.882 -1.866  1.00 107.43 ? 43  ILE   P CB  1 
ATOM   26875 C  CG1 . ILE   P  2  44  ? 4.097   -201.128 -2.864  1.00 107.61 ? 43  ILE   P CG1 1 
ATOM   26876 C  CG2 . ILE   P  2  44  ? 3.949   -203.066 -1.250  1.00 106.55 ? 43  ILE   P CG2 1 
ATOM   26877 C  CD1 . ILE   P  2  44  ? 5.255   -200.392 -2.230  1.00 107.34 ? 43  ILE   P CD1 1 
ATOM   26878 N  N   . VAL   P  2  45  ? 1.056   -204.334 -1.369  1.00 108.51 ? 44  VAL   P N   1 
ATOM   26879 C  CA  . VAL   P  2  45  ? 0.397   -205.168 -0.321  1.00 106.24 ? 44  VAL   P CA  1 
ATOM   26880 C  C   . VAL   P  2  45  ? 1.477   -205.658 0.647   1.00 104.96 ? 44  VAL   P C   1 
ATOM   26881 O  O   . VAL   P  2  45  ? 2.547   -206.081 0.169   1.00 104.71 ? 44  VAL   P O   1 
ATOM   26882 C  CB  . VAL   P  2  45  ? -0.369  -206.351 -0.943  1.00 106.23 ? 44  VAL   P CB  1 
ATOM   26883 C  CG1 . VAL   P  2  45  ? -0.996  -207.245 0.115   1.00 105.33 ? 44  VAL   P CG1 1 
ATOM   26884 C  CG2 . VAL   P  2  45  ? -1.424  -205.877 -1.928  1.00 108.83 ? 44  VAL   P CG2 1 
ATOM   26885 N  N   . LEU   P  2  46  ? 1.201   -205.582 1.952   1.00 106.09 ? 45  LEU   P N   1 
ATOM   26886 C  CA  . LEU   P  2  46  ? 1.960   -206.284 3.020   1.00 105.53 ? 45  LEU   P CA  1 
ATOM   26887 C  C   . LEU   P  2  46  ? 1.012   -207.252 3.730   1.00 107.36 ? 45  LEU   P C   1 
ATOM   26888 O  O   . LEU   P  2  46  ? -0.027  -206.794 4.245   1.00 109.42 ? 45  LEU   P O   1 
ATOM   26889 C  CB  . LEU   P  2  46  ? 2.540   -205.274 4.014   1.00 103.94 ? 45  LEU   P CB  1 
ATOM   26890 C  CG  . LEU   P  2  46  ? 3.795   -204.526 3.567   1.00 103.72 ? 45  LEU   P CG  1 
ATOM   26891 C  CD1 . LEU   P  2  46  ? 4.261   -203.587 4.669   1.00 105.56 ? 45  LEU   P CD1 1 
ATOM   26892 C  CD2 . LEU   P  2  46  ? 4.917   -205.481 3.181   1.00 100.94 ? 45  LEU   P CD2 1 
ATOM   26893 N  N   . ALA   P  2  47  ? 1.371   -208.536 3.741   1.00 109.06 ? 46  ALA   P N   1 
ATOM   26894 C  CA  . ALA   P  2  47  ? 0.647   -209.630 4.424   1.00 110.99 ? 46  ALA   P CA  1 
ATOM   26895 C  C   . ALA   P  2  47  ? 1.642   -210.375 5.317   1.00 109.18 ? 46  ALA   P C   1 
ATOM   26896 O  O   . ALA   P  2  47  ? 2.793   -210.563 4.879   1.00 110.89 ? 46  ALA   P O   1 
ATOM   26897 C  CB  . ALA   P  2  47  ? 0.020   -210.541 3.398   1.00 113.38 ? 46  ALA   P CB  1 
ATOM   26898 N  N   . ALA   P  2  48  ? 1.231   -210.755 6.528   1.00 108.21 ? 47  ALA   P N   1 
ATOM   26899 C  CA  . ALA   P  2  48  ? 2.078   -211.504 7.483   1.00 105.46 ? 47  ALA   P CA  1 
ATOM   26900 C  C   . ALA   P  2  48  ? 1.217   -212.399 8.378   1.00 108.75 ? 47  ALA   P C   1 
ATOM   26901 O  O   . ALA   P  2  48  ? 0.122   -211.963 8.791   1.00 109.96 ? 47  ALA   P O   1 
ATOM   26902 C  CB  . ALA   P  2  48  ? 2.910   -210.542 8.287   1.00 101.61 ? 47  ALA   P CB  1 
ATOM   26903 N  N   . GLU   P  2  49  ? 1.716   -213.609 8.651   1.00 110.52 ? 48  GLU   P N   1 
ATOM   26904 C  CA  . GLU   P  2  49  ? 1.055   -214.644 9.488   1.00 114.01 ? 48  GLU   P CA  1 
ATOM   26905 C  C   . GLU   P  2  49  ? 1.584   -214.521 10.919  1.00 112.30 ? 48  GLU   P C   1 
ATOM   26906 O  O   . GLU   P  2  49  ? 2.808   -214.651 11.104  1.00 105.81 ? 48  GLU   P O   1 
ATOM   26907 C  CB  . GLU   P  2  49  ? 1.333   -216.036 8.915   1.00 116.36 ? 48  GLU   P CB  1 
ATOM   26908 C  CG  . GLU   P  2  49  ? 0.422   -217.122 9.466   1.00 119.37 ? 48  GLU   P CG  1 
ATOM   26909 C  CD  . GLU   P  2  49  ? 0.747   -218.539 9.017   1.00 118.68 ? 48  GLU   P CD  1 
ATOM   26910 O  OE1 . GLU   P  2  49  ? 1.746   -218.723 8.289   1.00 114.28 ? 48  GLU   P OE1 1 
ATOM   26911 O  OE2 . GLU   P  2  49  ? -0.002  -219.459 9.401   1.00 121.72 ? 48  GLU   P OE2 1 
ATOM   26912 N  N   . ARG   P  2  50  ? 0.694   -214.268 11.882  1.00 119.55 ? 49  ARG   P N   1 
ATOM   26913 C  CA  . ARG   P  2  50  ? 1.022   -214.202 13.332  1.00 129.91 ? 49  ARG   P CA  1 
ATOM   26914 C  C   . ARG   P  2  50  ? 1.476   -215.586 13.802  1.00 132.98 ? 49  ARG   P C   1 
ATOM   26915 O  O   . ARG   P  2  50  ? 0.931   -216.586 13.296  1.00 131.61 ? 49  ARG   P O   1 
ATOM   26916 C  CB  . ARG   P  2  50  ? -0.191  -213.757 14.153  1.00 135.94 ? 49  ARG   P CB  1 
ATOM   26917 C  CG  . ARG   P  2  50  ? -0.556  -212.290 13.990  1.00 139.99 ? 49  ARG   P CG  1 
ATOM   26918 C  CD  . ARG   P  2  50  ? -1.913  -211.996 14.600  1.00 145.67 ? 49  ARG   P CD  1 
ATOM   26919 N  NE  . ARG   P  2  50  ? -2.253  -210.582 14.522  1.00 148.94 ? 49  ARG   P NE  1 
ATOM   26920 C  CZ  . ARG   P  2  50  ? -1.975  -209.665 15.449  1.00 153.67 ? 49  ARG   P CZ  1 
ATOM   26921 N  NH1 . ARG   P  2  50  ? -1.345  -209.995 16.566  1.00 155.63 ? 49  ARG   P NH1 1 
ATOM   26922 N  NH2 . ARG   P  2  50  ? -2.337  -208.409 15.248  1.00 155.44 ? 49  ARG   P NH2 1 
ATOM   26923 N  N   . LYS   P  2  51  ? 2.422   -215.638 14.743  1.00 144.61 ? 50  LYS   P N   1 
ATOM   26924 C  CA  . LYS   P  2  51  ? 2.973   -216.915 15.272  1.00 150.02 ? 50  LYS   P CA  1 
ATOM   26925 C  C   . LYS   P  2  51  ? 1.927   -217.556 16.194  1.00 155.26 ? 50  LYS   P C   1 
ATOM   26926 O  O   . LYS   P  2  51  ? 1.340   -216.825 17.019  1.00 151.02 ? 50  LYS   P O   1 
ATOM   26927 C  CB  . LYS   P  2  51  ? 4.322   -216.687 15.963  1.00 153.79 ? 50  LYS   P CB  1 
ATOM   26928 C  CG  . LYS   P  2  51  ? 5.244   -217.902 16.007  1.00 152.26 ? 50  LYS   P CG  1 
ATOM   26929 C  CD  . LYS   P  2  51  ? 5.639   -218.435 14.638  1.00 149.84 ? 50  LYS   P CD  1 
ATOM   26930 C  CE  . LYS   P  2  51  ? 4.818   -219.627 14.189  1.00 150.40 ? 50  LYS   P CE  1 
ATOM   26931 N  NZ  . LYS   P  2  51  ? 5.030   -219.935 12.755  1.00 150.79 ? 50  LYS   P NZ  1 
ATOM   26932 N  N   . VAL   P  2  52  ? 1.725   -218.871 16.041  1.00 159.95 ? 51  VAL   P N   1 
ATOM   26933 C  CA  . VAL   P  2  52  ? 0.591   -219.687 16.581  1.00 164.19 ? 51  VAL   P CA  1 
ATOM   26934 C  C   . VAL   P  2  52  ? -0.126  -218.921 17.703  1.00 167.37 ? 51  VAL   P C   1 
ATOM   26935 O  O   . VAL   P  2  52  ? 0.422   -218.842 18.821  1.00 169.27 ? 51  VAL   P O   1 
ATOM   26936 C  CB  . VAL   P  2  52  ? 1.060   -221.081 17.050  1.00 166.88 ? 51  VAL   P CB  1 
ATOM   26937 C  CG1 . VAL   P  2  52  ? -0.092  -221.904 17.611  1.00 167.81 ? 51  VAL   P CG1 1 
ATOM   26938 C  CG2 . VAL   P  2  52  ? 1.756   -221.854 15.937  1.00 164.40 ? 51  VAL   P CG2 1 
ATOM   26939 N  N   . THR   P  2  53  ? -1.324  -218.409 17.400  1.00 167.62 ? 52  THR   P N   1 
ATOM   26940 C  CA  . THR   P  2  53  ? -2.161  -217.549 18.283  1.00 163.62 ? 52  THR   P CA  1 
ATOM   26941 C  C   . THR   P  2  53  ? -2.819  -218.407 19.374  1.00 157.67 ? 52  THR   P C   1 
ATOM   26942 O  O   . THR   P  2  53  ? -2.986  -219.625 19.159  1.00 150.57 ? 52  THR   P O   1 
ATOM   26943 C  CB  . THR   P  2  53  ? -3.171  -216.746 17.443  1.00 168.43 ? 52  THR   P CB  1 
ATOM   26944 O  OG1 . THR   P  2  53  ? -2.737  -215.385 17.406  1.00 164.28 ? 52  THR   P OG1 1 
ATOM   26945 C  CG2 . THR   P  2  53  ? -4.593  -216.794 17.963  1.00 170.14 ? 52  THR   P CG2 1 
ATOM   26946 N  N   . SER   P  2  54  ? -3.149  -217.776 20.507  1.00 153.88 ? 53  SER   P N   1 
ATOM   26947 C  CA  . SER   P  2  54  ? -4.062  -218.282 21.566  1.00 152.42 ? 53  SER   P CA  1 
ATOM   26948 C  C   . SER   P  2  54  ? -5.386  -217.511 21.485  1.00 151.15 ? 53  SER   P C   1 
ATOM   26949 O  O   . SER   P  2  54  ? -5.342  -216.303 21.185  1.00 161.77 ? 53  SER   P O   1 
ATOM   26950 C  CB  . SER   P  2  54  ? -3.433  -218.153 22.931  1.00 151.79 ? 53  SER   P CB  1 
ATOM   26951 O  OG  . SER   P  2  54  ? -4.378  -218.424 23.956  1.00 153.42 ? 53  SER   P OG  1 
ATOM   26952 N  N   . THR   P  2  55  ? -6.512  -218.178 21.759  1.00 140.86 ? 54  THR   P N   1 
ATOM   26953 C  CA  . THR   P  2  55  ? -7.889  -217.618 21.625  1.00 138.78 ? 54  THR   P CA  1 
ATOM   26954 C  C   . THR   P  2  55  ? -8.088  -216.416 22.564  1.00 137.92 ? 54  THR   P C   1 
ATOM   26955 O  O   . THR   P  2  55  ? -8.965  -215.586 22.254  1.00 141.23 ? 54  THR   P O   1 
ATOM   26956 C  CB  . THR   P  2  55  ? -8.978  -218.684 21.832  1.00 136.98 ? 54  THR   P CB  1 
ATOM   26957 O  OG1 . THR   P  2  55  ? -10.162 -218.031 22.290  1.00 138.62 ? 54  THR   P OG1 1 
ATOM   26958 C  CG2 . THR   P  2  55  ? -8.612  -219.771 22.820  1.00 134.38 ? 54  THR   P CG2 1 
ATOM   26959 N  N   . LEU   P  2  56  ? -7.311  -216.312 23.650  1.00 136.50 ? 55  LEU   P N   1 
ATOM   26960 C  CA  . LEU   P  2  56  ? -7.428  -215.222 24.661  1.00 136.04 ? 55  LEU   P CA  1 
ATOM   26961 C  C   . LEU   P  2  56  ? -6.473  -214.057 24.352  1.00 133.56 ? 55  LEU   P C   1 
ATOM   26962 O  O   . LEU   P  2  56  ? -6.413  -213.127 25.177  1.00 132.83 ? 55  LEU   P O   1 
ATOM   26963 C  CB  . LEU   P  2  56  ? -7.163  -215.804 26.056  1.00 135.53 ? 55  LEU   P CB  1 
ATOM   26964 C  CG  . LEU   P  2  56  ? -8.364  -215.862 27.004  1.00 135.96 ? 55  LEU   P CG  1 
ATOM   26965 C  CD1 . LEU   P  2  56  ? -9.616  -216.388 26.315  1.00 136.45 ? 55  LEU   P CD1 1 
ATOM   26966 C  CD2 . LEU   P  2  56  ? -8.036  -216.708 28.223  1.00 136.95 ? 55  LEU   P CD2 1 
ATOM   26967 N  N   . LEU   P  2  57  ? -5.770  -214.075 23.214  1.00 130.49 ? 56  LEU   P N   1 
ATOM   26968 C  CA  . LEU   P  2  57  ? -4.932  -212.931 22.759  1.00 132.76 ? 56  LEU   P CA  1 
ATOM   26969 C  C   . LEU   P  2  57  ? -5.850  -211.790 22.305  1.00 139.36 ? 56  LEU   P C   1 
ATOM   26970 O  O   . LEU   P  2  57  ? -6.843  -212.082 21.611  1.00 144.19 ? 56  LEU   P O   1 
ATOM   26971 C  CB  . LEU   P  2  57  ? -4.018  -213.376 21.613  1.00 135.30 ? 56  LEU   P CB  1 
ATOM   26972 C  CG  . LEU   P  2  57  ? -2.832  -212.451 21.333  1.00 136.74 ? 56  LEU   P CG  1 
ATOM   26973 C  CD1 . LEU   P  2  57  ? -1.604  -212.894 22.116  1.00 136.60 ? 56  LEU   P CD1 1 
ATOM   26974 C  CD2 . LEU   P  2  57  ? -2.522  -212.387 19.844  1.00 139.05 ? 56  LEU   P CD2 1 
ATOM   26975 N  N   . GLU   P  2  58  ? -5.528  -210.547 22.682  1.00 141.75 ? 57  GLU   P N   1 
ATOM   26976 C  CA  . GLU   P  2  58  ? -6.234  -209.320 22.219  1.00 146.73 ? 57  GLU   P CA  1 
ATOM   26977 C  C   . GLU   P  2  58  ? -5.738  -208.997 20.805  1.00 151.82 ? 57  GLU   P C   1 
ATOM   26978 O  O   . GLU   P  2  58  ? -4.563  -208.616 20.670  1.00 152.73 ? 57  GLU   P O   1 
ATOM   26979 C  CB  . GLU   P  2  58  ? -5.994  -208.157 23.186  1.00 145.43 ? 57  GLU   P CB  1 
ATOM   26980 C  CG  . GLU   P  2  58  ? -6.911  -206.971 22.950  1.00 143.44 ? 57  GLU   P CG  1 
ATOM   26981 C  CD  . GLU   P  2  58  ? -8.378  -207.257 23.217  1.00 143.69 ? 57  GLU   P CD  1 
ATOM   26982 O  OE1 . GLU   P  2  58  ? -9.150  -207.349 22.244  1.00 144.87 ? 57  GLU   P OE1 1 
ATOM   26983 O  OE2 . GLU   P  2  58  ? -8.745  -207.387 24.401  1.00 136.45 ? 57  GLU   P OE2 1 
ATOM   26984 N  N   . GLN   P  2  59  ? -6.600  -209.153 19.796  1.00 156.15 ? 58  GLN   P N   1 
ATOM   26985 C  CA  . GLN   P  2  59  ? -6.203  -209.187 18.362  1.00 165.18 ? 58  GLN   P CA  1 
ATOM   26986 C  C   . GLN   P  2  59  ? -6.213  -207.773 17.760  1.00 167.74 ? 58  GLN   P C   1 
ATOM   26987 O  O   . GLN   P  2  59  ? -5.372  -207.521 16.874  1.00 163.10 ? 58  GLN   P O   1 
ATOM   26988 C  CB  . GLN   P  2  59  ? -7.117  -210.145 17.594  1.00 170.39 ? 58  GLN   P CB  1 
ATOM   26989 C  CG  . GLN   P  2  59  ? -6.416  -210.884 16.461  1.00 177.48 ? 58  GLN   P CG  1 
ATOM   26990 C  CD  . GLN   P  2  59  ? -6.561  -210.187 15.130  1.00 184.38 ? 58  GLN   P CD  1 
ATOM   26991 O  OE1 . GLN   P  2  59  ? -5.594  -209.682 14.564  1.00 189.79 ? 58  GLN   P OE1 1 
ATOM   26992 N  NE2 . GLN   P  2  59  ? -7.780  -210.163 14.615  1.00 189.64 ? 58  GLN   P NE2 1 
ATOM   26993 N  N   . ASP   P  2  60  ? -7.110  -206.887 18.215  1.00 173.81 ? 59  ASP   P N   1 
ATOM   26994 C  CA  . ASP   P  2  60  ? -7.325  -205.538 17.614  1.00 178.36 ? 59  ASP   P CA  1 
ATOM   26995 C  C   . ASP   P  2  60  ? -6.231  -204.559 18.072  1.00 182.45 ? 59  ASP   P C   1 
ATOM   26996 O  O   . ASP   P  2  60  ? -5.652  -203.886 17.194  1.00 184.70 ? 59  ASP   P O   1 
ATOM   26997 C  CB  . ASP   P  2  60  ? -8.733  -204.991 17.888  1.00 178.30 ? 59  ASP   P CB  1 
ATOM   26998 C  CG  . ASP   P  2  60  ? -9.204  -205.067 19.331  1.00 174.67 ? 59  ASP   P CG  1 
ATOM   26999 O  OD1 . ASP   P  2  60  ? -8.364  -205.319 20.216  1.00 171.76 ? 59  ASP   P OD1 1 
ATOM   27000 O  OD2 . ASP   P  2  60  ? -10.416 -204.875 19.556  1.00 169.12 ? 59  ASP   P OD2 1 
ATOM   27001 N  N   . THR   P  2  61  ? -5.951  -204.477 19.380  1.00 180.42 ? 60  THR   P N   1 
ATOM   27002 C  CA  . THR   P  2  61  ? -4.931  -203.562 19.970  1.00 176.78 ? 60  THR   P CA  1 
ATOM   27003 C  C   . THR   P  2  61  ? -3.534  -204.193 19.878  1.00 175.08 ? 60  THR   P C   1 
ATOM   27004 O  O   . THR   P  2  61  ? -2.677  -203.844 20.717  1.00 161.69 ? 60  THR   P O   1 
ATOM   27005 C  CB  . THR   P  2  61  ? -5.251  -203.212 21.431  1.00 178.02 ? 60  THR   P CB  1 
ATOM   27006 O  OG1 . THR   P  2  61  ? -5.194  -204.408 22.210  1.00 172.02 ? 60  THR   P OG1 1 
ATOM   27007 C  CG2 . THR   P  2  61  ? -6.603  -202.555 21.605  1.00 179.39 ? 60  THR   P CG2 1 
ATOM   27008 N  N   . SER   P  2  62  ? -3.306  -205.069 18.893  1.00 172.94 ? 61  SER   P N   1 
ATOM   27009 C  CA  . SER   P  2  62  ? -2.064  -205.870 18.742  1.00 173.38 ? 61  SER   P CA  1 
ATOM   27010 C  C   . SER   P  2  62  ? -1.270  -205.396 17.521  1.00 172.27 ? 61  SER   P C   1 
ATOM   27011 O  O   . SER   P  2  62  ? -1.893  -205.020 16.505  1.00 176.26 ? 61  SER   P O   1 
ATOM   27012 C  CB  . SER   P  2  62  ? -2.377  -207.341 18.658  1.00 171.61 ? 61  SER   P CB  1 
ATOM   27013 O  OG  . SER   P  2  62  ? -1.188  -208.113 18.574  1.00 172.71 ? 61  SER   P OG  1 
ATOM   27014 N  N   . THR   P  2  63  ? 0.060   -205.405 17.644  1.00 168.31 ? 62  THR   P N   1 
ATOM   27015 C  CA  . THR   P  2  63  ? 1.037   -205.163 16.551  1.00 165.37 ? 62  THR   P CA  1 
ATOM   27016 C  C   . THR   P  2  63  ? 2.270   -206.036 16.803  1.00 158.10 ? 62  THR   P C   1 
ATOM   27017 O  O   . THR   P  2  63  ? 2.892   -205.883 17.873  1.00 163.40 ? 62  THR   P O   1 
ATOM   27018 C  CB  . THR   P  2  63  ? 1.416   -203.682 16.444  1.00 165.23 ? 62  THR   P CB  1 
ATOM   27019 O  OG1 . THR   P  2  63  ? 0.229   -202.892 16.519  1.00 167.16 ? 62  THR   P OG1 1 
ATOM   27020 C  CG2 . THR   P  2  63  ? 2.147   -203.370 15.158  1.00 166.59 ? 62  THR   P CG2 1 
ATOM   27021 N  N   . GLU   P  2  64  ? 2.593   -206.917 15.855  1.00 150.85 ? 63  GLU   P N   1 
ATOM   27022 C  CA  . GLU   P  2  64  ? 3.667   -207.939 15.972  1.00 149.79 ? 63  GLU   P CA  1 
ATOM   27023 C  C   . GLU   P  2  64  ? 4.523   -207.926 14.700  1.00 139.02 ? 63  GLU   P C   1 
ATOM   27024 O  O   . GLU   P  2  64  ? 5.761   -208.028 14.820  1.00 140.97 ? 63  GLU   P O   1 
ATOM   27025 C  CB  . GLU   P  2  64  ? 3.029   -209.310 16.217  1.00 156.68 ? 63  GLU   P CB  1 
ATOM   27026 C  CG  . GLU   P  2  64  ? 4.014   -210.465 16.311  1.00 163.04 ? 63  GLU   P CG  1 
ATOM   27027 C  CD  . GLU   P  2  64  ? 3.388   -211.843 16.152  1.00 166.67 ? 63  GLU   P CD  1 
ATOM   27028 O  OE1 . GLU   P  2  64  ? 4.066   -212.744 15.613  1.00 170.44 ? 63  GLU   P OE1 1 
ATOM   27029 O  OE2 . GLU   P  2  64  ? 2.222   -212.016 16.566  1.00 173.06 ? 63  GLU   P OE2 1 
ATOM   27030 N  N   . LYS   P  2  65  ? 3.878   -207.793 13.537  1.00 130.10 ? 64  LYS   P N   1 
ATOM   27031 C  CA  . LYS   P  2  65  ? 4.466   -208.049 12.196  1.00 124.38 ? 64  LYS   P CA  1 
ATOM   27032 C  C   . LYS   P  2  65  ? 4.634   -206.736 11.418  1.00 113.81 ? 64  LYS   P C   1 
ATOM   27033 O  O   . LYS   P  2  65  ? 5.729   -206.538 10.857  1.00 100.69 ? 64  LYS   P O   1 
ATOM   27034 C  CB  . LYS   P  2  65  ? 3.572   -209.043 11.449  1.00 129.11 ? 64  LYS   P CB  1 
ATOM   27035 C  CG  . LYS   P  2  65  ? 3.679   -210.488 11.925  1.00 133.35 ? 64  LYS   P CG  1 
ATOM   27036 C  CD  . LYS   P  2  65  ? 4.900   -211.182 11.367  1.00 132.10 ? 64  LYS   P CD  1 
ATOM   27037 C  CE  . LYS   P  2  65  ? 5.228   -212.508 12.014  1.00 131.20 ? 64  LYS   P CE  1 
ATOM   27038 N  NZ  . LYS   P  2  65  ? 6.428   -213.108 11.386  1.00 129.76 ? 64  LYS   P NZ  1 
ATOM   27039 N  N   . LEU   P  2  66  ? 3.599   -205.884 11.392  1.00 113.21 ? 65  LEU   P N   1 
ATOM   27040 C  CA  . LEU   P  2  66  ? 3.501   -204.681 10.512  1.00 111.22 ? 65  LEU   P CA  1 
ATOM   27041 C  C   . LEU   P  2  66  ? 3.638   -203.392 11.330  1.00 108.11 ? 65  LEU   P C   1 
ATOM   27042 O  O   . LEU   P  2  66  ? 2.768   -203.143 12.185  1.00 106.42 ? 65  LEU   P O   1 
ATOM   27043 C  CB  . LEU   P  2  66  ? 2.154   -204.706 9.782   1.00 112.28 ? 65  LEU   P CB  1 
ATOM   27044 C  CG  . LEU   P  2  66  ? 2.154   -205.364 8.403   1.00 112.35 ? 65  LEU   P CG  1 
ATOM   27045 C  CD1 . LEU   P  2  66  ? 2.924   -206.678 8.405   1.00 111.46 ? 65  LEU   P CD1 1 
ATOM   27046 C  CD2 . LEU   P  2  66  ? 0.729   -205.585 7.925   1.00 114.60 ? 65  LEU   P CD2 1 
ATOM   27047 N  N   . TYR   P  2  67  ? 4.662   -202.585 11.030  1.00 104.80 ? 66  TYR   P N   1 
ATOM   27048 C  CA  . TYR   P  2  67  ? 4.979   -201.311 11.731  1.00 106.04 ? 66  TYR   P CA  1 
ATOM   27049 C  C   . TYR   P  2  67  ? 5.121   -200.170 10.720  1.00 102.75 ? 66  TYR   P C   1 
ATOM   27050 O  O   . TYR   P  2  67  ? 5.626   -200.389 9.600   1.00 100.61 ? 66  TYR   P O   1 
ATOM   27051 C  CB  . TYR   P  2  67  ? 6.258   -201.446 12.562  1.00 106.45 ? 66  TYR   P CB  1 
ATOM   27052 C  CG  . TYR   P  2  67  ? 6.152   -202.411 13.714  1.00 107.94 ? 66  TYR   P CG  1 
ATOM   27053 C  CD1 . TYR   P  2  67  ? 6.491   -203.745 13.559  1.00 109.10 ? 66  TYR   P CD1 1 
ATOM   27054 C  CD2 . TYR   P  2  67  ? 5.706   -201.996 14.958  1.00 109.32 ? 66  TYR   P CD2 1 
ATOM   27055 C  CE1 . TYR   P  2  67  ? 6.394   -204.644 14.609  1.00 111.75 ? 66  TYR   P CE1 1 
ATOM   27056 C  CE2 . TYR   P  2  67  ? 5.604   -202.881 16.020  1.00 111.83 ? 66  TYR   P CE2 1 
ATOM   27057 C  CZ  . TYR   P  2  67  ? 5.949   -204.211 15.845  1.00 112.57 ? 66  TYR   P CZ  1 
ATOM   27058 O  OH  . TYR   P  2  67  ? 5.854   -205.095 16.881  1.00 117.61 ? 66  TYR   P OH  1 
ATOM   27059 N  N   . LYS   P  2  68  ? 4.700   -198.976 11.141  1.00 102.42 ? 67  LYS   P N   1 
ATOM   27060 C  CA  . LYS   P  2  68  ? 4.725   -197.718 10.353  1.00 102.24 ? 67  LYS   P CA  1 
ATOM   27061 C  C   . LYS   P  2  68  ? 6.027   -196.974 10.677  1.00 99.19  ? 67  LYS   P C   1 
ATOM   27062 O  O   . LYS   P  2  68  ? 6.276   -196.743 11.874  1.00 96.87  ? 67  LYS   P O   1 
ATOM   27063 C  CB  . LYS   P  2  68  ? 3.480   -196.899 10.708  1.00 106.05 ? 67  LYS   P CB  1 
ATOM   27064 C  CG  . LYS   P  2  68  ? 3.105   -195.811 9.715   1.00 108.91 ? 67  LYS   P CG  1 
ATOM   27065 C  CD  . LYS   P  2  68  ? 1.762   -195.170 10.004  1.00 115.62 ? 67  LYS   P CD  1 
ATOM   27066 C  CE  . LYS   P  2  68  ? 0.587   -196.074 9.687   1.00 116.07 ? 67  LYS   P CE  1 
ATOM   27067 N  NZ  . LYS   P  2  68  ? -0.707  -195.374 9.864   1.00 119.72 ? 67  LYS   P NZ  1 
ATOM   27068 N  N   . LEU   P  2  69  ? 6.841   -196.652 9.664   1.00 96.30  ? 68  LEU   P N   1 
ATOM   27069 C  CA  . LEU   P  2  69  ? 8.116   -195.899 9.833   1.00 97.52  ? 68  LEU   P CA  1 
ATOM   27070 C  C   . LEU   P  2  69  ? 7.848   -194.399 9.661   1.00 101.17 ? 68  LEU   P C   1 
ATOM   27071 O  O   . LEU   P  2  69  ? 8.333   -193.610 10.498  1.00 101.79 ? 68  LEU   P O   1 
ATOM   27072 C  CB  . LEU   P  2  69  ? 9.155   -196.395 8.821   1.00 96.09  ? 68  LEU   P CB  1 
ATOM   27073 C  CG  . LEU   P  2  69  ? 9.613   -197.847 8.973   1.00 96.00  ? 68  LEU   P CG  1 
ATOM   27074 C  CD1 . LEU   P  2  69  ? 10.880  -198.090 8.168   1.00 94.96  ? 68  LEU   P CD1 1 
ATOM   27075 C  CD2 . LEU   P  2  69  ? 9.848   -198.221 10.431  1.00 96.62  ? 68  LEU   P CD2 1 
ATOM   27076 N  N   . ASN   P  2  70  ? 7.127   -194.028 8.600   1.00 100.57 ? 69  ASN   P N   1 
ATOM   27077 C  CA  . ASN   P  2  70  ? 6.568   -192.665 8.382   1.00 101.52 ? 69  ASN   P CA  1 
ATOM   27078 C  C   . ASN   P  2  70  ? 5.275   -192.808 7.568   1.00 104.45 ? 69  ASN   P C   1 
ATOM   27079 O  O   . ASN   P  2  70  ? 4.807   -193.951 7.420   1.00 107.78 ? 69  ASN   P O   1 
ATOM   27080 C  CB  . ASN   P  2  70  ? 7.600   -191.726 7.749   1.00 99.48  ? 69  ASN   P CB  1 
ATOM   27081 C  CG  . ASN   P  2  70  ? 7.946   -192.068 6.314   1.00 96.31  ? 69  ASN   P CG  1 
ATOM   27082 O  OD1 . ASN   P  2  70  ? 7.477   -193.063 5.772   1.00 92.70  ? 69  ASN   P OD1 1 
ATOM   27083 N  ND2 . ASN   P  2  70  ? 8.765   -191.243 5.685   1.00 98.47  ? 69  ASN   P ND2 1 
ATOM   27084 N  N   . ASP   P  2  71  ? 4.724   -191.705 7.053   1.00 106.63 ? 70  ASP   P N   1 
ATOM   27085 C  CA  . ASP   P  2  71  ? 3.424   -191.684 6.329   1.00 107.48 ? 70  ASP   P CA  1 
ATOM   27086 C  C   . ASP   P  2  71  ? 3.550   -192.316 4.935   1.00 100.73 ? 70  ASP   P C   1 
ATOM   27087 O  O   . ASP   P  2  71  ? 2.497   -192.494 4.292   1.00 98.09  ? 70  ASP   P O   1 
ATOM   27088 C  CB  . ASP   P  2  71  ? 2.881   -190.259 6.206   1.00 110.99 ? 70  ASP   P CB  1 
ATOM   27089 C  CG  . ASP   P  2  71  ? 2.386   -189.679 7.520   1.00 118.70 ? 70  ASP   P CG  1 
ATOM   27090 O  OD1 . ASP   P  2  71  ? 1.829   -190.451 8.327   1.00 121.06 ? 70  ASP   P OD1 1 
ATOM   27091 O  OD2 . ASP   P  2  71  ? 2.568   -188.460 7.729   1.00 121.20 ? 70  ASP   P OD2 1 
ATOM   27092 N  N   . LYS   P  2  72  ? 4.769   -192.627 4.475   1.00 100.75 ? 71  LYS   P N   1 
ATOM   27093 C  CA  . LYS   P  2  72  ? 5.024   -193.157 3.106   1.00 104.05 ? 71  LYS   P CA  1 
ATOM   27094 C  C   . LYS   P  2  72  ? 5.734   -194.521 3.126   1.00 102.10 ? 71  LYS   P C   1 
ATOM   27095 O  O   . LYS   P  2  72  ? 5.851   -195.110 2.036   1.00 103.24 ? 71  LYS   P O   1 
ATOM   27096 C  CB  . LYS   P  2  72  ? 5.857   -192.150 2.309   1.00 106.59 ? 71  LYS   P CB  1 
ATOM   27097 C  CG  . LYS   P  2  72  ? 5.258   -190.754 2.214   1.00 112.11 ? 71  LYS   P CG  1 
ATOM   27098 C  CD  . LYS   P  2  72  ? 3.943   -190.703 1.458   1.00 116.53 ? 71  LYS   P CD  1 
ATOM   27099 C  CE  . LYS   P  2  72  ? 3.296   -189.333 1.473   1.00 118.70 ? 71  LYS   P CE  1 
ATOM   27100 N  NZ  . LYS   P  2  72  ? 4.109   -188.330 0.747   1.00 120.68 ? 71  LYS   P NZ  1 
ATOM   27101 N  N   . ILE   P  2  73  ? 6.195   -195.012 4.284   1.00 100.55 ? 72  ILE   P N   1 
ATOM   27102 C  CA  . ILE   P  2  73  ? 6.997   -196.272 4.393   1.00 97.90  ? 72  ILE   P CA  1 
ATOM   27103 C  C   . ILE   P  2  73  ? 6.492   -197.110 5.574   1.00 97.99  ? 72  ILE   P C   1 
ATOM   27104 O  O   . ILE   P  2  73  ? 6.280   -196.540 6.664   1.00 96.16  ? 72  ILE   P O   1 
ATOM   27105 C  CB  . ILE   P  2  73  ? 8.502   -195.959 4.536   1.00 96.19  ? 72  ILE   P CB  1 
ATOM   27106 C  CG1 . ILE   P  2  73  ? 9.033   -195.116 3.373   1.00 97.27  ? 72  ILE   P CG1 1 
ATOM   27107 C  CG2 . ILE   P  2  73  ? 9.309   -197.237 4.707   1.00 95.95  ? 72  ILE   P CG2 1 
ATOM   27108 C  CD1 . ILE   P  2  73  ? 10.169  -194.196 3.758   1.00 97.40  ? 72  ILE   P CD1 1 
ATOM   27109 N  N   . ALA   P  2  74  ? 6.330   -198.419 5.359   1.00 96.38  ? 73  ALA   P N   1 
ATOM   27110 C  CA  . ALA   P  2  74  ? 6.002   -199.429 6.395   1.00 97.64  ? 73  ALA   P CA  1 
ATOM   27111 C  C   . ALA   P  2  74  ? 6.930   -200.637 6.228   1.00 96.81  ? 73  ALA   P C   1 
ATOM   27112 O  O   . ALA   P  2  74  ? 7.531   -200.781 5.140   1.00 94.67  ? 73  ALA   P O   1 
ATOM   27113 C  CB  . ALA   P  2  74  ? 4.551   -199.832 6.298   1.00 96.45  ? 73  ALA   P CB  1 
ATOM   27114 N  N   . VAL   P  2  75  ? 7.039   -201.464 7.271   1.00 99.83  ? 74  VAL   P N   1 
ATOM   27115 C  CA  . VAL   P  2  75  ? 7.878   -202.699 7.276   1.00 99.04  ? 74  VAL   P CA  1 
ATOM   27116 C  C   . VAL   P  2  75  ? 7.042   -203.874 7.789   1.00 99.23  ? 74  VAL   P C   1 
ATOM   27117 O  O   . VAL   P  2  75  ? 6.243   -203.672 8.727   1.00 95.72  ? 74  VAL   P O   1 
ATOM   27118 C  CB  . VAL   P  2  75  ? 9.160   -202.527 8.113   1.00 100.61 ? 74  VAL   P CB  1 
ATOM   27119 C  CG1 . VAL   P  2  75  ? 10.177  -201.653 7.401   1.00 100.33 ? 74  VAL   P CG1 1 
ATOM   27120 C  CG2 . VAL   P  2  75  ? 8.874   -201.995 9.511   1.00 102.49 ? 74  VAL   P CG2 1 
ATOM   27121 N  N   . ALA   P  2  76  ? 7.221   -205.045 7.169   1.00 100.33 ? 75  ALA   P N   1 
ATOM   27122 C  CA  . ALA   P  2  76  ? 6.818   -206.368 7.697   1.00 97.20  ? 75  ALA   P CA  1 
ATOM   27123 C  C   . ALA   P  2  76  ? 8.037   -206.995 8.385   1.00 95.58  ? 75  ALA   P C   1 
ATOM   27124 O  O   . ALA   P  2  76  ? 9.154   -206.867 7.842   1.00 92.26  ? 75  ALA   P O   1 
ATOM   27125 C  CB  . ALA   P  2  76  ? 6.283   -207.235 6.586   1.00 96.39  ? 75  ALA   P CB  1 
ATOM   27126 N  N   . VAL   P  2  77  ? 7.830   -207.626 9.543   1.00 95.43  ? 76  VAL   P N   1 
ATOM   27127 C  CA  . VAL   P  2  77  ? 8.915   -208.149 10.425  1.00 98.79  ? 76  VAL   P CA  1 
ATOM   27128 C  C   . VAL   P  2  77  ? 8.867   -209.680 10.438  1.00 97.35  ? 76  VAL   P C   1 
ATOM   27129 O  O   . VAL   P  2  77  ? 7.759   -210.234 10.533  1.00 98.94  ? 76  VAL   P O   1 
ATOM   27130 C  CB  . VAL   P  2  77  ? 8.786   -207.578 11.850  1.00 98.20  ? 76  VAL   P CB  1 
ATOM   27131 C  CG1 . VAL   P  2  77  ? 9.735   -208.254 12.829  1.00 98.56  ? 76  VAL   P CG1 1 
ATOM   27132 C  CG2 . VAL   P  2  77  ? 8.994   -206.075 11.863  1.00 99.18  ? 76  VAL   P CG2 1 
ATOM   27133 N  N   . ALA   P  2  78  ? 10.035  -210.323 10.353  1.00 100.22 ? 77  ALA   P N   1 
ATOM   27134 C  CA  . ALA   P  2  78  ? 10.243  -211.764 10.627  1.00 101.23 ? 77  ALA   P CA  1 
ATOM   27135 C  C   . ALA   P  2  78  ? 11.478  -211.921 11.521  1.00 100.04 ? 77  ALA   P C   1 
ATOM   27136 O  O   . ALA   P  2  78  ? 12.566  -211.479 11.105  1.00 101.80 ? 77  ALA   P O   1 
ATOM   27137 C  CB  . ALA   P  2  78  ? 10.389  -212.530 9.335   1.00 102.53 ? 77  ALA   P CB  1 
ATOM   27138 N  N   . GLY   P  2  79  ? 11.302  -212.505 12.710  1.00 100.69 ? 78  GLY   P N   1 
ATOM   27139 C  CA  . GLY   P  2  79  ? 12.380  -212.742 13.690  1.00 100.76 ? 78  GLY   P CA  1 
ATOM   27140 C  C   . GLY   P  2  79  ? 11.965  -212.329 15.092  1.00 99.84  ? 78  GLY   P C   1 
ATOM   27141 O  O   . GLY   P  2  79  ? 10.751  -212.345 15.371  1.00 101.06 ? 78  GLY   P O   1 
ATOM   27142 N  N   . LEU   P  2  80  ? 12.934  -211.980 15.945  1.00 99.93  ? 79  LEU   P N   1 
ATOM   27143 C  CA  . LEU   P  2  80  ? 12.681  -211.472 17.321  1.00 101.16 ? 79  LEU   P CA  1 
ATOM   27144 C  C   . LEU   P  2  80  ? 12.032  -210.089 17.197  1.00 100.53 ? 79  LEU   P C   1 
ATOM   27145 O  O   . LEU   P  2  80  ? 12.652  -209.216 16.565  1.00 103.67 ? 79  LEU   P O   1 
ATOM   27146 C  CB  . LEU   P  2  80  ? 13.990  -211.373 18.118  1.00 102.30 ? 79  LEU   P CB  1 
ATOM   27147 C  CG  . LEU   P  2  80  ? 14.728  -212.672 18.460  1.00 103.73 ? 79  LEU   P CG  1 
ATOM   27148 C  CD1 . LEU   P  2  80  ? 13.791  -213.870 18.529  1.00 106.35 ? 79  LEU   P CD1 1 
ATOM   27149 C  CD2 . LEU   P  2  80  ? 15.862  -212.941 17.481  1.00 104.99 ? 79  LEU   P CD2 1 
ATOM   27150 N  N   . THR   P  2  81  ? 10.838  -209.901 17.767  1.00 98.79  ? 80  THR   P N   1 
ATOM   27151 C  CA  . THR   P  2  81  ? 10.086  -208.616 17.737  1.00 100.47 ? 80  THR   P CA  1 
ATOM   27152 C  C   . THR   P  2  81  ? 10.846  -207.536 18.516  1.00 100.44 ? 80  THR   P C   1 
ATOM   27153 O  O   . THR   P  2  81  ? 10.897  -206.388 18.031  1.00 101.98 ? 80  THR   P O   1 
ATOM   27154 C  CB  . THR   P  2  81  ? 8.674   -208.759 18.318  1.00 102.43 ? 80  THR   P CB  1 
ATOM   27155 O  OG1 . THR   P  2  81  ? 8.000   -209.810 17.627  1.00 102.85 ? 80  THR   P OG1 1 
ATOM   27156 C  CG2 . THR   P  2  81  ? 7.876   -207.476 18.209  1.00 103.91 ? 80  THR   P CG2 1 
ATOM   27157 N  N   . ALA   P  2  82  ? 11.382  -207.884 19.690  1.00 99.07  ? 81  ALA   P N   1 
ATOM   27158 C  CA  . ALA   P  2  82  ? 12.145  -206.975 20.577  1.00 98.15  ? 81  ALA   P CA  1 
ATOM   27159 C  C   . ALA   P  2  82  ? 13.324  -206.368 19.807  1.00 95.26  ? 81  ALA   P C   1 
ATOM   27160 O  O   . ALA   P  2  82  ? 13.537  -205.156 19.940  1.00 95.22  ? 81  ALA   P O   1 
ATOM   27161 C  CB  . ALA   P  2  82  ? 12.612  -207.719 21.802  1.00 98.81  ? 81  ALA   P CB  1 
ATOM   27162 N  N   . ASP   P  2  83  ? 14.053  -207.184 19.038  1.00 96.59  ? 82  ASP   P N   1 
ATOM   27163 C  CA  . ASP   P  2  83  ? 15.184  -206.748 18.173  1.00 97.03  ? 82  ASP   P CA  1 
ATOM   27164 C  C   . ASP   P  2  83  ? 14.675  -205.786 17.094  1.00 96.94  ? 82  ASP   P C   1 
ATOM   27165 O  O   . ASP   P  2  83  ? 15.378  -204.800 16.811  1.00 98.26  ? 82  ASP   P O   1 
ATOM   27166 C  CB  . ASP   P  2  83  ? 15.884  -207.932 17.500  1.00 99.15  ? 82  ASP   P CB  1 
ATOM   27167 C  CG  . ASP   P  2  83  ? 16.766  -208.750 18.426  1.00 101.55 ? 82  ASP   P CG  1 
ATOM   27168 O  OD1 . ASP   P  2  83  ? 16.710  -208.519 19.650  1.00 102.55 ? 82  ASP   P OD1 1 
ATOM   27169 O  OD2 . ASP   P  2  83  ? 17.505  -209.615 17.912  1.00 105.90 ? 82  ASP   P OD2 1 
ATOM   27170 N  N   . ALA   P  2  84  ? 13.513  -206.079 16.503  1.00 96.12  ? 83  ALA   P N   1 
ATOM   27171 C  CA  . ALA   P  2  84  ? 12.911  -205.300 15.396  1.00 98.97  ? 83  ALA   P CA  1 
ATOM   27172 C  C   . ALA   P  2  84  ? 12.569  -203.883 15.877  1.00 99.43  ? 83  ALA   P C   1 
ATOM   27173 O  O   . ALA   P  2  84  ? 12.876  -202.925 15.139  1.00 103.66 ? 83  ALA   P O   1 
ATOM   27174 C  CB  . ALA   P  2  84  ? 11.698  -206.014 14.849  1.00 98.81  ? 83  ALA   P CB  1 
ATOM   27175 N  N   . GLU   P  2  85  ? 11.975  -203.748 17.068  1.00 98.36  ? 84  GLU   P N   1 
ATOM   27176 C  CA  . GLU   P  2  85  ? 11.510  -202.443 17.614  1.00 96.75  ? 84  GLU   P CA  1 
ATOM   27177 C  C   . GLU   P  2  85  ? 12.707  -201.515 17.847  1.00 94.90  ? 84  GLU   P C   1 
ATOM   27178 O  O   . GLU   P  2  85  ? 12.559  -200.308 17.583  1.00 92.98  ? 84  GLU   P O   1 
ATOM   27179 C  CB  . GLU   P  2  85  ? 10.698  -202.633 18.895  1.00 100.61 ? 84  GLU   P CB  1 
ATOM   27180 C  CG  . GLU   P  2  85  ? 9.339   -203.263 18.646  1.00 104.25 ? 84  GLU   P CG  1 
ATOM   27181 C  CD  . GLU   P  2  85  ? 8.281   -202.982 19.699  1.00 108.63 ? 84  GLU   P CD  1 
ATOM   27182 O  OE1 . GLU   P  2  85  ? 7.235   -203.661 19.667  1.00 110.98 ? 84  GLU   P OE1 1 
ATOM   27183 O  OE2 . GLU   P  2  85  ? 8.496   -202.082 20.539  1.00 111.67 ? 84  GLU   P OE2 1 
ATOM   27184 N  N   . ILE   P  2  86  ? 13.838  -202.052 18.321  1.00 91.56  ? 85  ILE   P N   1 
ATOM   27185 C  CA  . ILE   P  2  86  ? 15.125  -201.302 18.450  1.00 91.37  ? 85  ILE   P CA  1 
ATOM   27186 C  C   . ILE   P  2  86  ? 15.433  -200.649 17.098  1.00 92.38  ? 85  ILE   P C   1 
ATOM   27187 O  O   . ILE   P  2  86  ? 15.697  -199.431 17.075  1.00 96.15  ? 85  ILE   P O   1 
ATOM   27188 C  CB  . ILE   P  2  86  ? 16.283  -202.215 18.907  1.00 89.90  ? 85  ILE   P CB  1 
ATOM   27189 C  CG1 . ILE   P  2  86  ? 16.093  -202.731 20.337  1.00 90.78  ? 85  ILE   P CG1 1 
ATOM   27190 C  CG2 . ILE   P  2  86  ? 17.625  -201.514 18.735  1.00 90.24  ? 85  ILE   P CG2 1 
ATOM   27191 C  CD1 . ILE   P  2  86  ? 16.232  -201.678 21.414  1.00 91.84  ? 85  ILE   P CD1 1 
ATOM   27192 N  N   . LEU   P  2  87  ? 15.396  -201.436 16.020  1.00 89.10  ? 86  LEU   P N   1 
ATOM   27193 C  CA  . LEU   P  2  87  ? 15.758  -200.993 14.647  1.00 90.98  ? 86  LEU   P CA  1 
ATOM   27194 C  C   . LEU   P  2  87  ? 14.679  -200.056 14.084  1.00 93.45  ? 86  LEU   P C   1 
ATOM   27195 O  O   . LEU   P  2  87  ? 15.056  -199.083 13.395  1.00 92.76  ? 86  LEU   P O   1 
ATOM   27196 C  CB  . LEU   P  2  87  ? 15.953  -202.227 13.760  1.00 88.96  ? 86  LEU   P CB  1 
ATOM   27197 C  CG  . LEU   P  2  87  ? 17.164  -203.097 14.098  1.00 87.82  ? 86  LEU   P CG  1 
ATOM   27198 C  CD1 . LEU   P  2  87  ? 17.204  -204.329 13.210  1.00 88.26  ? 86  LEU   P CD1 1 
ATOM   27199 C  CD2 . LEU   P  2  87  ? 18.466  -202.320 13.969  1.00 85.99  ? 86  LEU   P CD2 1 
ATOM   27200 N  N   . ILE   P  2  88  ? 13.397  -200.329 14.360  1.00 96.67  ? 87  ILE   P N   1 
ATOM   27201 C  CA  . ILE   P  2  88  ? 12.240  -199.516 13.870  1.00 98.49  ? 87  ILE   P CA  1 
ATOM   27202 C  C   . ILE   P  2  88  ? 12.350  -198.091 14.435  1.00 101.99 ? 87  ILE   P C   1 
ATOM   27203 O  O   . ILE   P  2  88  ? 12.134  -197.137 13.658  1.00 104.34 ? 87  ILE   P O   1 
ATOM   27204 C  CB  . ILE   P  2  88  ? 10.890  -200.189 14.208  1.00 98.51  ? 87  ILE   P CB  1 
ATOM   27205 C  CG1 . ILE   P  2  88  ? 10.623  -201.390 13.298  1.00 98.89  ? 87  ILE   P CG1 1 
ATOM   27206 C  CG2 . ILE   P  2  88  ? 9.739   -199.193 14.148  1.00 98.92  ? 87  ILE   P CG2 1 
ATOM   27207 C  CD1 . ILE   P  2  88  ? 9.646   -202.388 13.872  1.00 100.93 ? 87  ILE   P CD1 1 
ATOM   27208 N  N   . ASN   P  2  89  ? 12.677  -197.948 15.725  1.00 99.71  ? 88  ASN   P N   1 
ATOM   27209 C  CA  . ASN   P  2  89  ? 12.790  -196.630 16.409  1.00 99.36  ? 88  ASN   P CA  1 
ATOM   27210 C  C   . ASN   P  2  89  ? 13.964  -195.846 15.823  1.00 96.68  ? 88  ASN   P C   1 
ATOM   27211 O  O   . ASN   P  2  89  ? 13.821  -194.622 15.672  1.00 98.66  ? 88  ASN   P O   1 
ATOM   27212 C  CB  . ASN   P  2  89  ? 12.933  -196.755 17.927  1.00 101.00 ? 88  ASN   P CB  1 
ATOM   27213 C  CG  . ASN   P  2  89  ? 11.591  -196.758 18.627  1.00 104.13 ? 88  ASN   P CG  1 
ATOM   27214 O  OD1 . ASN   P  2  89  ? 10.808  -195.819 18.477  1.00 101.20 ? 88  ASN   P OD1 1 
ATOM   27215 N  ND2 . ASN   P  2  89  ? 11.312  -197.809 19.382  1.00 106.75 ? 88  ASN   P ND2 1 
ATOM   27216 N  N   . THR   P  2  90  ? 15.074  -196.519 15.513  1.00 91.60  ? 89  THR   P N   1 
ATOM   27217 C  CA  . THR   P  2  90  ? 16.238  -195.911 14.821  1.00 91.13  ? 89  THR   P CA  1 
ATOM   27218 C  C   . THR   P  2  90  ? 15.793  -195.404 13.446  1.00 92.63  ? 89  THR   P C   1 
ATOM   27219 O  O   . THR   P  2  90  ? 16.082  -194.237 13.131  1.00 93.63  ? 89  THR   P O   1 
ATOM   27220 C  CB  . THR   P  2  90  ? 17.405  -196.894 14.699  1.00 92.09  ? 89  THR   P CB  1 
ATOM   27221 O  OG1 . THR   P  2  90  ? 17.793  -197.251 16.025  1.00 90.94  ? 89  THR   P OG1 1 
ATOM   27222 C  CG2 . THR   P  2  90  ? 18.581  -196.309 13.949  1.00 94.08  ? 89  THR   P CG2 1 
ATOM   27223 N  N   . ALA   P  2  91  ? 15.117  -196.255 12.671  1.00 93.69  ? 90  ALA   P N   1 
ATOM   27224 C  CA  . ALA   P  2  91  ? 14.601  -195.947 11.316  1.00 95.28  ? 90  ALA   P CA  1 
ATOM   27225 C  C   . ALA   P  2  91  ? 13.647  -194.747 11.372  1.00 93.24  ? 90  ALA   P C   1 
ATOM   27226 O  O   . ALA   P  2  91  ? 13.757  -193.878 10.490  1.00 95.79  ? 90  ALA   P O   1 
ATOM   27227 C  CB  . ALA   P  2  91  ? 13.916  -197.158 10.734  1.00 95.58  ? 90  ALA   P CB  1 
ATOM   27228 N  N   . ARG   P  2  92  ? 12.748  -194.709 12.363  1.00 93.35  ? 91  ARG   P N   1 
ATOM   27229 C  CA  . ARG   P  2  92  ? 11.748  -193.619 12.545  1.00 95.00  ? 91  ARG   P CA  1 
ATOM   27230 C  C   . ARG   P  2  92  ? 12.469  -192.282 12.769  1.00 95.51  ? 91  ARG   P C   1 
ATOM   27231 O  O   . ARG   P  2  92  ? 12.080  -191.293 12.117  1.00 96.16  ? 91  ARG   P O   1 
ATOM   27232 C  CB  . ARG   P  2  92  ? 10.796  -193.932 13.705  1.00 95.50  ? 91  ARG   P CB  1 
ATOM   27233 C  CG  . ARG   P  2  92  ? 9.675   -194.896 13.346  1.00 94.95  ? 91  ARG   P CG  1 
ATOM   27234 C  CD  . ARG   P  2  92  ? 8.869   -195.317 14.559  1.00 95.30  ? 91  ARG   P CD  1 
ATOM   27235 N  NE  . ARG   P  2  92  ? 7.728   -196.154 14.210  1.00 94.57  ? 91  ARG   P NE  1 
ATOM   27236 C  CZ  . ARG   P  2  92  ? 6.862   -196.662 15.083  1.00 95.02  ? 91  ARG   P CZ  1 
ATOM   27237 N  NH1 . ARG   P  2  92  ? 6.995   -196.429 16.379  1.00 97.16  ? 91  ARG   P NH1 1 
ATOM   27238 N  NH2 . ARG   P  2  92  ? 5.859   -197.407 14.655  1.00 96.15  ? 91  ARG   P NH2 1 
ATOM   27239 N  N   . ILE   P  2  93  ? 13.472  -192.261 13.656  1.00 95.64  ? 92  ILE   P N   1 
ATOM   27240 C  CA  . ILE   P  2  93  ? 14.300  -191.060 13.988  1.00 95.20  ? 92  ILE   P CA  1 
ATOM   27241 C  C   . ILE   P  2  93  ? 15.067  -190.615 12.737  1.00 96.46  ? 92  ILE   P C   1 
ATOM   27242 O  O   . ILE   P  2  93  ? 15.083  -189.401 12.460  1.00 97.23  ? 92  ILE   P O   1 
ATOM   27243 C  CB  . ILE   P  2  93  ? 15.244  -191.348 15.176  1.00 93.43  ? 92  ILE   P CB  1 
ATOM   27244 C  CG1 . ILE   P  2  93  ? 14.468  -191.402 16.495  1.00 93.64  ? 92  ILE   P CG1 1 
ATOM   27245 C  CG2 . ILE   P  2  93  ? 16.378  -190.333 15.229  1.00 93.71  ? 92  ILE   P CG2 1 
ATOM   27246 C  CD1 . ILE   P  2  93  ? 15.254  -191.954 17.663  1.00 92.92  ? 92  ILE   P CD1 1 
ATOM   27247 N  N   . HIS   P  2  94  ? 15.691  -191.562 12.029  1.00 95.72  ? 93  HIS   P N   1 
ATOM   27248 C  CA  . HIS   P  2  94  ? 16.489  -191.328 10.794  1.00 98.33  ? 93  HIS   P CA  1 
ATOM   27249 C  C   . HIS   P  2  94  ? 15.630  -190.628 9.734   1.00 93.39  ? 93  HIS   P C   1 
ATOM   27250 O  O   . HIS   P  2  94  ? 16.161  -189.738 9.050   1.00 95.59  ? 93  HIS   P O   1 
ATOM   27251 C  CB  . HIS   P  2  94  ? 17.071  -192.646 10.262  1.00 104.83 ? 93  HIS   P CB  1 
ATOM   27252 C  CG  . HIS   P  2  94  ? 18.399  -193.022 10.837  1.00 116.24 ? 93  HIS   P CG  1 
ATOM   27253 N  ND1 . HIS   P  2  94  ? 19.397  -192.095 11.090  1.00 123.89 ? 93  HIS   P ND1 1 
ATOM   27254 C  CD2 . HIS   P  2  94  ? 18.916  -194.229 11.165  1.00 119.99 ? 93  HIS   P CD2 1 
ATOM   27255 C  CE1 . HIS   P  2  94  ? 20.458  -192.713 11.575  1.00 124.75 ? 93  HIS   P CE1 1 
ATOM   27256 N  NE2 . HIS   P  2  94  ? 20.189  -194.025 11.629  1.00 119.81 ? 93  HIS   P NE2 1 
ATOM   27257 N  N   . ALA   P  2  95  ? 14.361  -191.025 9.601   1.00 90.46  ? 94  ALA   P N   1 
ATOM   27258 C  CA  . ALA   P  2  95  ? 13.376  -190.434 8.663   1.00 92.39  ? 94  ALA   P CA  1 
ATOM   27259 C  C   . ALA   P  2  95  ? 13.118  -188.966 9.020   1.00 92.19  ? 94  ALA   P C   1 
ATOM   27260 O  O   . ALA   P  2  95  ? 13.057  -188.138 8.091   1.00 93.78  ? 94  ALA   P O   1 
ATOM   27261 C  CB  . ALA   P  2  95  ? 12.093  -191.226 8.687   1.00 92.29  ? 94  ALA   P CB  1 
ATOM   27262 N  N   . GLN   P  2  96  ? 12.952  -188.668 10.312  1.00 93.36  ? 95  GLN   P N   1 
ATOM   27263 C  CA  . GLN   P  2  96  ? 12.668  -187.303 10.832  1.00 93.82  ? 95  GLN   P CA  1 
ATOM   27264 C  C   . GLN   P  2  96  ? 13.905  -186.407 10.681  1.00 97.43  ? 95  GLN   P C   1 
ATOM   27265 O  O   . GLN   P  2  96  ? 13.719  -185.216 10.350  1.00 99.75  ? 95  GLN   P O   1 
ATOM   27266 C  CB  . GLN   P  2  96  ? 12.210  -187.362 12.292  1.00 94.44  ? 95  GLN   P CB  1 
ATOM   27267 C  CG  . GLN   P  2  96  ? 10.827  -187.971 12.485  1.00 93.24  ? 95  GLN   P CG  1 
ATOM   27268 C  CD  . GLN   P  2  96  ? 9.803   -187.448 11.507  1.00 94.32  ? 95  GLN   P CD  1 
ATOM   27269 O  OE1 . GLN   P  2  96  ? 9.098   -188.214 10.860  1.00 94.35  ? 95  GLN   P OE1 1 
ATOM   27270 N  NE2 . GLN   P  2  96  ? 9.725   -186.133 11.375  1.00 93.75  ? 95  GLN   P NE2 1 
ATOM   27271 N  N   . ASN   P  2  97  ? 15.107  -186.945 10.928  1.00 96.04  ? 96  ASN   P N   1 
ATOM   27272 C  CA  . ASN   P  2  97  ? 16.401  -186.223 10.762  1.00 96.24  ? 96  ASN   P CA  1 
ATOM   27273 C  C   . ASN   P  2  97  ? 16.538  -185.723 9.322   1.00 96.55  ? 96  ASN   P C   1 
ATOM   27274 O  O   . ASN   P  2  97  ? 16.964  -184.571 9.136   1.00 101.74 ? 96  ASN   P O   1 
ATOM   27275 C  CB  . ASN   P  2  97  ? 17.616  -187.094 11.086  1.00 96.25  ? 96  ASN   P CB  1 
ATOM   27276 C  CG  . ASN   P  2  97  ? 17.931  -187.170 12.564  1.00 97.70  ? 96  ASN   P CG  1 
ATOM   27277 O  OD1 . ASN   P  2  97  ? 17.468  -186.347 13.351  1.00 95.46  ? 96  ASN   P OD1 1 
ATOM   27278 N  ND2 . ASN   P  2  97  ? 18.738  -188.148 12.944  1.00 99.31  ? 96  ASN   P ND2 1 
ATOM   27279 N  N   . TYR   P  2  98  ? 16.206  -186.571 8.348   1.00 95.17  ? 97  TYR   P N   1 
ATOM   27280 C  CA  . TYR   P  2  98  ? 16.253  -186.249 6.898   1.00 95.65  ? 97  TYR   P CA  1 
ATOM   27281 C  C   . TYR   P  2  98  ? 15.235  -185.147 6.574   1.00 95.08  ? 97  TYR   P C   1 
ATOM   27282 O  O   . TYR   P  2  98  ? 15.585  -184.234 5.803   1.00 97.03  ? 97  TYR   P O   1 
ATOM   27283 C  CB  . TYR   P  2  98  ? 15.998  -187.501 6.057   1.00 93.99  ? 97  TYR   P CB  1 
ATOM   27284 C  CG  . TYR   P  2  98  ? 16.269  -187.322 4.585   1.00 96.33  ? 97  TYR   P CG  1 
ATOM   27285 C  CD1 . TYR   P  2  98  ? 15.321  -186.754 3.749   1.00 97.10  ? 97  TYR   P CD1 1 
ATOM   27286 C  CD2 . TYR   P  2  98  ? 17.478  -187.706 4.026   1.00 95.57  ? 97  TYR   P CD2 1 
ATOM   27287 C  CE1 . TYR   P  2  98  ? 15.558  -186.578 2.395   1.00 97.23  ? 97  TYR   P CE1 1 
ATOM   27288 C  CE2 . TYR   P  2  98  ? 17.732  -187.538 2.673   1.00 97.09  ? 97  TYR   P CE2 1 
ATOM   27289 C  CZ  . TYR   P  2  98  ? 16.769  -186.971 1.853   1.00 96.76  ? 97  TYR   P CZ  1 
ATOM   27290 O  OH  . TYR   P  2  98  ? 16.987  -186.794 0.517   1.00 95.81  ? 97  TYR   P OH  1 
ATOM   27291 N  N   . LEU   P  2  99  ? 14.020  -185.235 7.130   1.00 90.97  ? 98  LEU   P N   1 
ATOM   27292 C  CA  . LEU   P  2  99  ? 12.927  -184.247 6.908   1.00 93.61  ? 98  LEU   P CA  1 
ATOM   27293 C  C   . LEU   P  2  99  ? 13.326  -182.892 7.507   1.00 96.68  ? 98  LEU   P C   1 
ATOM   27294 O  O   . LEU   P  2  99  ? 13.114  -181.861 6.834   1.00 98.01  ? 98  LEU   P O   1 
ATOM   27295 C  CB  . LEU   P  2  99  ? 11.627  -184.761 7.535   1.00 91.43  ? 98  LEU   P CB  1 
ATOM   27296 C  CG  . LEU   P  2  99  ? 10.397  -183.877 7.319   1.00 92.40  ? 98  LEU   P CG  1 
ATOM   27297 C  CD1 . LEU   P  2  99  ? 10.122  -183.674 5.836   1.00 92.98  ? 98  LEU   P CD1 1 
ATOM   27298 C  CD2 . LEU   P  2  99  ? 9.174   -184.463 8.006   1.00 91.97  ? 98  LEU   P CD2 1 
ATOM   27299 N  N   . LYS   P  2  100 ? 13.874  -182.900 8.727   1.00 98.47  ? 99  LYS   P N   1 
ATOM   27300 C  CA  . LYS   P  2  100 ? 14.350  -181.689 9.447   1.00 98.50  ? 99  LYS   P CA  1 
ATOM   27301 C  C   . LYS   P  2  100 ? 15.469  -181.020 8.635   1.00 95.86  ? 99  LYS   P C   1 
ATOM   27302 O  O   . LYS   P  2  100 ? 15.458  -179.775 8.553   1.00 95.89  ? 99  LYS   P O   1 
ATOM   27303 C  CB  . LYS   P  2  100 ? 14.801  -182.062 10.865  1.00 100.23 ? 99  LYS   P CB  1 
ATOM   27304 C  CG  . LYS   P  2  100 ? 15.331  -180.914 11.716  1.00 103.75 ? 99  LYS   P CG  1 
ATOM   27305 C  CD  . LYS   P  2  100 ? 15.785  -181.347 13.099  1.00 104.86 ? 99  LYS   P CD  1 
ATOM   27306 C  CE  . LYS   P  2  100 ? 16.817  -180.427 13.721  1.00 109.02 ? 99  LYS   P CE  1 
ATOM   27307 N  NZ  . LYS   P  2  100 ? 16.381  -179.009 13.725  1.00 113.67 ? 99  LYS   P NZ  1 
ATOM   27308 N  N   . THR   P  2  101 ? 16.383  -181.800 8.041   1.00 92.12  ? 100 THR   P N   1 
ATOM   27309 C  CA  . THR   P  2  101 ? 17.572  -181.278 7.308   1.00 90.28  ? 100 THR   P CA  1 
ATOM   27310 C  C   . THR   P  2  101 ? 17.152  -180.698 5.952   1.00 92.95  ? 100 THR   P C   1 
ATOM   27311 O  O   . THR   P  2  101 ? 17.522  -179.536 5.684   1.00 94.23  ? 100 THR   P O   1 
ATOM   27312 C  CB  . THR   P  2  101 ? 18.667  -182.338 7.143   1.00 88.17  ? 100 THR   P CB  1 
ATOM   27313 O  OG1 . THR   P  2  101 ? 19.118  -182.644 8.461   1.00 86.18  ? 100 THR   P OG1 1 
ATOM   27314 C  CG2 . THR   P  2  101 ? 19.842  -181.870 6.311   1.00 87.35  ? 100 THR   P CG2 1 
ATOM   27315 N  N   . TYR   P  2  102 ? 16.421  -181.469 5.137   1.00 91.20  ? 101 TYR   P N   1 
ATOM   27316 C  CA  . TYR   P  2  102 ? 16.176  -181.181 3.698   1.00 91.42  ? 101 TYR   P CA  1 
ATOM   27317 C  C   . TYR   P  2  102 ? 14.735  -180.729 3.428   1.00 91.38  ? 101 TYR   P C   1 
ATOM   27318 O  O   . TYR   P  2  102 ? 14.444  -180.399 2.262   1.00 90.89  ? 101 TYR   P O   1 
ATOM   27319 C  CB  . TYR   P  2  102 ? 16.480  -182.416 2.848   1.00 92.60  ? 101 TYR   P CB  1 
ATOM   27320 C  CG  . TYR   P  2  102 ? 17.907  -182.898 2.919   1.00 93.94  ? 101 TYR   P CG  1 
ATOM   27321 C  CD1 . TYR   P  2  102 ? 18.929  -182.194 2.302   1.00 93.66  ? 101 TYR   P CD1 1 
ATOM   27322 C  CD2 . TYR   P  2  102 ? 18.235  -184.066 3.587   1.00 92.30  ? 101 TYR   P CD2 1 
ATOM   27323 C  CE1 . TYR   P  2  102 ? 20.242  -182.629 2.356   1.00 92.65  ? 101 TYR   P CE1 1 
ATOM   27324 C  CE2 . TYR   P  2  102 ? 19.544  -184.517 3.650   1.00 92.53  ? 101 TYR   P CE2 1 
ATOM   27325 C  CZ  . TYR   P  2  102 ? 20.551  -183.795 3.032   1.00 92.62  ? 101 TYR   P CZ  1 
ATOM   27326 O  OH  . TYR   P  2  102 ? 21.846  -184.219 3.080   1.00 94.64  ? 101 TYR   P OH  1 
ATOM   27327 N  N   . ASN   P  2  103 ? 13.857  -180.729 4.437   1.00 90.17  ? 102 ASN   P N   1 
ATOM   27328 C  CA  . ASN   P  2  103 ? 12.431  -180.324 4.290   1.00 93.76  ? 102 ASN   P CA  1 
ATOM   27329 C  C   . ASN   P  2  103 ? 11.774  -181.131 3.163   1.00 95.08  ? 102 ASN   P C   1 
ATOM   27330 O  O   . ASN   P  2  103 ? 10.921  -180.571 2.448   1.00 97.16  ? 102 ASN   P O   1 
ATOM   27331 C  CB  . ASN   P  2  103 ? 12.292  -178.817 4.061   1.00 94.17  ? 102 ASN   P CB  1 
ATOM   27332 C  CG  . ASN   P  2  103 ? 11.705  -178.110 5.262   1.00 94.20  ? 102 ASN   P CG  1 
ATOM   27333 O  OD1 . ASN   P  2  103 ? 12.367  -177.968 6.288   1.00 91.87  ? 102 ASN   P OD1 1 
ATOM   27334 N  ND2 . ASN   P  2  103 ? 10.459  -177.681 5.149   1.00 96.59  ? 102 ASN   P ND2 1 
ATOM   27335 N  N   . GLU   P  2  104 ? 12.164  -182.400 3.019   1.00 95.76  ? 103 GLU   P N   1 
ATOM   27336 C  CA  . GLU   P  2  104 ? 11.554  -183.379 2.082   1.00 98.71  ? 103 GLU   P CA  1 
ATOM   27337 C  C   . GLU   P  2  104 ? 11.540  -184.748 2.768   1.00 98.90  ? 103 GLU   P C   1 
ATOM   27338 O  O   . GLU   P  2  104 ? 12.515  -185.055 3.482   1.00 98.22  ? 103 GLU   P O   1 
ATOM   27339 C  CB  . GLU   P  2  104 ? 12.331  -183.428 0.765   1.00 100.09 ? 103 GLU   P CB  1 
ATOM   27340 C  CG  . GLU   P  2  104 ? 12.208  -182.160 -0.060  1.00 102.55 ? 103 GLU   P CG  1 
ATOM   27341 C  CD  . GLU   P  2  104 ? 13.006  -182.152 -1.353  1.00 103.88 ? 103 GLU   P CD  1 
ATOM   27342 O  OE1 . GLU   P  2  104 ? 12.897  -181.158 -2.102  1.00 105.33 ? 103 GLU   P OE1 1 
ATOM   27343 O  OE2 . GLU   P  2  104 ? 13.736  -183.135 -1.606  1.00 105.77 ? 103 GLU   P OE2 1 
ATOM   27344 N  N   . ASP   P  2  105 ? 10.472  -185.526 2.565   1.00 99.80  ? 104 ASP   P N   1 
ATOM   27345 C  CA  . ASP   P  2  105 ? 10.343  -186.917 3.077   1.00 96.74  ? 104 ASP   P CA  1 
ATOM   27346 C  C   . ASP   P  2  105 ? 11.525  -187.733 2.544   1.00 93.96  ? 104 ASP   P C   1 
ATOM   27347 O  O   . ASP   P  2  105 ? 11.946  -187.485 1.397   1.00 89.37  ? 104 ASP   P O   1 
ATOM   27348 C  CB  . ASP   P  2  105 ? 8.999   -187.536 2.684   1.00 97.72  ? 104 ASP   P CB  1 
ATOM   27349 C  CG  . ASP   P  2  105 ? 7.796   -186.907 3.368   1.00 99.31  ? 104 ASP   P CG  1 
ATOM   27350 O  OD1 . ASP   P  2  105 ? 7.954   -186.413 4.507   1.00 99.60  ? 104 ASP   P OD1 1 
ATOM   27351 O  OD2 . ASP   P  2  105 ? 6.709   -186.919 2.756   1.00 101.75 ? 104 ASP   P OD2 1 
ATOM   27352 N  N   . ILE   P  2  106 ? 12.055  -188.651 3.353   1.00 93.31  ? 105 ILE   P N   1 
ATOM   27353 C  CA  . ILE   P  2  106 ? 13.268  -189.451 3.006   1.00 93.13  ? 105 ILE   P CA  1 
ATOM   27354 C  C   . ILE   P  2  106 ? 12.927  -190.427 1.880   1.00 93.72  ? 105 ILE   P C   1 
ATOM   27355 O  O   . ILE   P  2  106 ? 11.931  -191.144 1.958   1.00 94.60  ? 105 ILE   P O   1 
ATOM   27356 C  CB  . ILE   P  2  106 ? 13.864  -190.163 4.240   1.00 92.73  ? 105 ILE   P CB  1 
ATOM   27357 C  CG1 . ILE   P  2  106 ? 15.215  -190.797 3.902   1.00 91.38  ? 105 ILE   P CG1 1 
ATOM   27358 C  CG2 . ILE   P  2  106 ? 12.898  -191.178 4.842   1.00 92.95  ? 105 ILE   P CG2 1 
ATOM   27359 C  CD1 . ILE   P  2  106 ? 16.025  -191.191 5.107   1.00 90.35  ? 105 ILE   P CD1 1 
ATOM   27360 N  N   . PRO   P  2  107 ? 13.718  -190.440 0.779   1.00 92.95  ? 106 PRO   P N   1 
ATOM   27361 C  CA  . PRO   P  2  107 ? 13.661  -191.512 -0.217  1.00 92.24  ? 106 PRO   P CA  1 
ATOM   27362 C  C   . PRO   P  2  107 ? 13.863  -192.898 0.417   1.00 93.65  ? 106 PRO   P C   1 
ATOM   27363 O  O   . PRO   P  2  107 ? 14.732  -193.029 1.262   1.00 91.03  ? 106 PRO   P O   1 
ATOM   27364 C  CB  . PRO   P  2  107 ? 14.818  -191.179 -1.172  1.00 91.59  ? 106 PRO   P CB  1 
ATOM   27365 C  CG  . PRO   P  2  107 ? 14.977  -189.687 -1.051  1.00 92.12  ? 106 PRO   P CG  1 
ATOM   27366 C  CD  . PRO   P  2  107 ? 14.671  -189.385 0.401   1.00 93.40  ? 106 PRO   P CD  1 
ATOM   27367 N  N   . VAL   P  2  108 ? 13.077  -193.889 -0.020  1.00 93.51  ? 107 VAL   P N   1 
ATOM   27368 C  CA  . VAL   P  2  108 ? 12.944  -195.223 0.643   1.00 94.32  ? 107 VAL   P CA  1 
ATOM   27369 C  C   . VAL   P  2  108 ? 14.319  -195.897 0.743   1.00 91.19  ? 107 VAL   P C   1 
ATOM   27370 O  O   . VAL   P  2  108 ? 14.639  -196.391 1.837   1.00 90.15  ? 107 VAL   P O   1 
ATOM   27371 C  CB  . VAL   P  2  108 ? 11.935  -196.137 -0.078  1.00 95.65  ? 107 VAL   P CB  1 
ATOM   27372 C  CG1 . VAL   P  2  108 ? 11.849  -197.500 0.592   1.00 97.11  ? 107 VAL   P CG1 1 
ATOM   27373 C  CG2 . VAL   P  2  108 ? 10.552  -195.510 -0.168  1.00 96.94  ? 107 VAL   P CG2 1 
ATOM   27374 N  N   . GLU   P  2  109 ? 15.095  -195.921 -0.346  1.00 92.64  ? 108 GLU   P N   1 
ATOM   27375 C  CA  . GLU   P  2  109 ? 16.395  -196.646 -0.419  1.00 93.06  ? 108 GLU   P CA  1 
ATOM   27376 C  C   . GLU   P  2  109 ? 17.393  -196.079 0.599   1.00 94.01  ? 108 GLU   P C   1 
ATOM   27377 O  O   . GLU   P  2  109 ? 18.179  -196.875 1.147   1.00 91.30  ? 108 GLU   P O   1 
ATOM   27378 C  CB  . GLU   P  2  109 ? 17.019  -196.558 -1.811  1.00 95.29  ? 108 GLU   P CB  1 
ATOM   27379 C  CG  . GLU   P  2  109 ? 18.061  -197.635 -2.051  1.00 97.39  ? 108 GLU   P CG  1 
ATOM   27380 C  CD  . GLU   P  2  109 ? 19.146  -197.295 -3.057  1.00 102.42 ? 108 GLU   P CD  1 
ATOM   27381 O  OE1 . GLU   P  2  109 ? 19.075  -196.208 -3.664  1.00 102.98 ? 108 GLU   P OE1 1 
ATOM   27382 O  OE2 . GLU   P  2  109 ? 20.063  -198.122 -3.229  1.00 105.36 ? 108 GLU   P OE2 1 
ATOM   27383 N  N   . ILE   P  2  110 ? 17.388  -194.760 0.818   1.00 92.54  ? 109 ILE   P N   1 
ATOM   27384 C  CA  . ILE   P  2  110 ? 18.310  -194.075 1.774   1.00 92.55  ? 109 ILE   P CA  1 
ATOM   27385 C  C   . ILE   P  2  110 ? 18.026  -194.604 3.186   1.00 90.29  ? 109 ILE   P C   1 
ATOM   27386 O  O   . ILE   P  2  110 ? 19.001  -194.909 3.902   1.00 91.63  ? 109 ILE   P O   1 
ATOM   27387 C  CB  . ILE   P  2  110 ? 18.187  -192.539 1.686   1.00 92.49  ? 109 ILE   P CB  1 
ATOM   27388 C  CG1 . ILE   P  2  110 ? 18.582  -192.024 0.299   1.00 94.56  ? 109 ILE   P CG1 1 
ATOM   27389 C  CG2 . ILE   P  2  110 ? 19.002  -191.868 2.785   1.00 93.31  ? 109 ILE   P CG2 1 
ATOM   27390 C  CD1 . ILE   P  2  110 ? 18.372  -190.538 0.099   1.00 95.89  ? 109 ILE   P CD1 1 
ATOM   27391 N  N   . LEU   P  2  111 ? 16.746  -194.712 3.562   1.00 87.83  ? 110 LEU   P N   1 
ATOM   27392 C  CA  . LEU   P  2  111 ? 16.306  -195.240 4.882   1.00 88.26  ? 110 LEU   P CA  1 
ATOM   27393 C  C   . LEU   P  2  111 ? 16.724  -196.710 4.994   1.00 89.14  ? 110 LEU   P C   1 
ATOM   27394 O  O   . LEU   P  2  111 ? 17.283  -197.076 6.047   1.00 90.05  ? 110 LEU   P O   1 
ATOM   27395 C  CB  . LEU   P  2  111 ? 14.789  -195.070 5.033   1.00 85.66  ? 110 LEU   P CB  1 
ATOM   27396 C  CG  . LEU   P  2  111 ? 14.203  -195.511 6.375   1.00 85.81  ? 110 LEU   P CG  1 
ATOM   27397 C  CD1 . LEU   P  2  111 ? 12.970  -194.698 6.734   1.00 85.36  ? 110 LEU   P CD1 1 
ATOM   27398 C  CD2 . LEU   P  2  111 ? 13.859  -196.991 6.369   1.00 86.86  ? 110 LEU   P CD2 1 
ATOM   27399 N  N   . VAL   P  2  112 ? 16.477  -197.503 3.943   1.00 91.94  ? 111 VAL   P N   1 
ATOM   27400 C  CA  . VAL   P  2  112 ? 16.752  -198.973 3.904   1.00 94.59  ? 111 VAL   P CA  1 
ATOM   27401 C  C   . VAL   P  2  112 ? 18.266  -199.195 4.013   1.00 97.63  ? 111 VAL   P C   1 
ATOM   27402 O  O   . VAL   P  2  112 ? 18.663  -200.146 4.716   1.00 100.87 ? 111 VAL   P O   1 
ATOM   27403 C  CB  . VAL   P  2  112 ? 16.180  -199.651 2.640   1.00 94.90  ? 111 VAL   P CB  1 
ATOM   27404 C  CG1 . VAL   P  2  112 ? 16.525  -201.133 2.582   1.00 94.68  ? 111 VAL   P CG1 1 
ATOM   27405 C  CG2 . VAL   P  2  112 ? 14.675  -199.468 2.521   1.00 96.78  ? 111 VAL   P CG2 1 
ATOM   27406 N  N   . ARG   P  2  113 ? 19.072  -198.358 3.350   1.00 98.93  ? 112 ARG   P N   1 
ATOM   27407 C  CA  . ARG   P  2  113 ? 20.556  -198.477 3.341   1.00 100.20 ? 112 ARG   P CA  1 
ATOM   27408 C  C   . ARG   P  2  113 ? 21.100  -198.256 4.758   1.00 100.07 ? 112 ARG   P C   1 
ATOM   27409 O  O   . ARG   P  2  113 ? 21.940  -199.064 5.193   1.00 98.27  ? 112 ARG   P O   1 
ATOM   27410 C  CB  . ARG   P  2  113 ? 21.201  -197.482 2.372   1.00 102.64 ? 112 ARG   P CB  1 
ATOM   27411 C  CG  . ARG   P  2  113 ? 22.658  -197.802 2.067   1.00 105.35 ? 112 ARG   P CG  1 
ATOM   27412 C  CD  . ARG   P  2  113 ? 23.431  -196.618 1.523   1.00 107.71 ? 112 ARG   P CD  1 
ATOM   27413 N  NE  . ARG   P  2  113 ? 22.916  -196.183 0.230   1.00 109.67 ? 112 ARG   P NE  1 
ATOM   27414 C  CZ  . ARG   P  2  113 ? 22.401  -194.985 -0.039  1.00 111.71 ? 112 ARG   P CZ  1 
ATOM   27415 N  NH1 . ARG   P  2  113 ? 21.969  -194.726 -1.262  1.00 113.45 ? 112 ARG   P NH1 1 
ATOM   27416 N  NH2 . ARG   P  2  113 ? 22.322  -194.046 0.892   1.00 113.82 ? 112 ARG   P NH2 1 
ATOM   27417 N  N   . ARG   P  2  114 ? 20.644  -197.201 5.442   1.00 103.99 ? 113 ARG   P N   1 
ATOM   27418 C  CA  . ARG   P  2  114 ? 21.146  -196.807 6.787   1.00 107.84 ? 113 ARG   P CA  1 
ATOM   27419 C  C   . ARG   P  2  114 ? 20.786  -197.896 7.805   1.00 107.29 ? 113 ARG   P C   1 
ATOM   27420 O  O   . ARG   P  2  114 ? 21.643  -198.203 8.659   1.00 114.00 ? 113 ARG   P O   1 
ATOM   27421 C  CB  . ARG   P  2  114 ? 20.589  -195.445 7.212   1.00 113.59 ? 113 ARG   P CB  1 
ATOM   27422 C  CG  . ARG   P  2  114 ? 21.395  -194.758 8.307   1.00 115.98 ? 113 ARG   P CG  1 
ATOM   27423 C  CD  . ARG   P  2  114 ? 21.377  -193.250 8.133   1.00 121.32 ? 113 ARG   P CD  1 
ATOM   27424 N  NE  . ARG   P  2  114 ? 20.012  -192.735 8.053   1.00 124.03 ? 113 ARG   P NE  1 
ATOM   27425 C  CZ  . ARG   P  2  114 ? 19.599  -191.730 7.281   1.00 121.49 ? 113 ARG   P CZ  1 
ATOM   27426 N  NH1 . ARG   P  2  114 ? 20.436  -191.097 6.474   1.00 123.02 ? 113 ARG   P NH1 1 
ATOM   27427 N  NH2 . ARG   P  2  114 ? 18.331  -191.362 7.309   1.00 117.18 ? 113 ARG   P NH2 1 
ATOM   27428 N  N   . LEU   P  2  115 ? 19.576  -198.460 7.719   1.00 101.56 ? 114 LEU   P N   1 
ATOM   27429 C  CA  . LEU   P  2  115 ? 19.111  -199.526 8.648   1.00 98.49  ? 114 LEU   P CA  1 
ATOM   27430 C  C   . LEU   P  2  115 ? 19.935  -200.791 8.390   1.00 96.13  ? 114 LEU   P C   1 
ATOM   27431 O  O   . LEU   P  2  115 ? 20.300  -201.466 9.370   1.00 100.33 ? 114 LEU   P O   1 
ATOM   27432 C  CB  . LEU   P  2  115 ? 17.612  -199.794 8.460   1.00 98.42  ? 114 LEU   P CB  1 
ATOM   27433 C  CG  . LEU   P  2  115 ? 16.757  -199.727 9.728   1.00 99.35  ? 114 LEU   P CG  1 
ATOM   27434 C  CD1 . LEU   P  2  115 ? 15.395  -200.363 9.495   1.00 100.68 ? 114 LEU   P CD1 1 
ATOM   27435 C  CD2 . LEU   P  2  115 ? 17.441  -200.384 10.920  1.00 100.11 ? 114 LEU   P CD2 1 
ATOM   27436 N  N   . SER   P  2  116 ? 20.223  -201.080 7.118   1.00 92.95  ? 115 SER   P N   1 
ATOM   27437 C  CA  . SER   P  2  116 ? 21.051  -202.229 6.662   1.00 91.58  ? 115 SER   P CA  1 
ATOM   27438 C  C   . SER   P  2  116 ? 22.517  -202.026 7.070   1.00 92.04  ? 115 SER   P C   1 
ATOM   27439 O  O   . SER   P  2  116 ? 23.195  -203.034 7.348   1.00 85.89  ? 115 SER   P O   1 
ATOM   27440 C  CB  . SER   P  2  116 ? 20.917  -202.427 5.176   1.00 90.98  ? 115 SER   P CB  1 
ATOM   27441 O  OG  . SER   P  2  116 ? 19.569  -202.707 4.827   1.00 90.08  ? 115 SER   P OG  1 
ATOM   27442 N  N   . ASP   P  2  117 ? 22.985  -200.773 7.103   1.00 94.04  ? 116 ASP   P N   1 
ATOM   27443 C  CA  . ASP   P  2  117 ? 24.376  -200.401 7.485   1.00 95.72  ? 116 ASP   P CA  1 
ATOM   27444 C  C   . ASP   P  2  117 ? 24.577  -200.631 8.989   1.00 92.84  ? 116 ASP   P C   1 
ATOM   27445 O  O   . ASP   P  2  117 ? 25.703  -201.003 9.378   1.00 89.54  ? 116 ASP   P O   1 
ATOM   27446 C  CB  . ASP   P  2  117 ? 24.702  -198.953 7.103   1.00 98.95  ? 116 ASP   P CB  1 
ATOM   27447 C  CG  . ASP   P  2  117 ? 25.030  -198.742 5.631   1.00 103.33 ? 116 ASP   P CG  1 
ATOM   27448 O  OD1 . ASP   P  2  117 ? 25.280  -199.747 4.929   1.00 107.34 ? 116 ASP   P OD1 1 
ATOM   27449 O  OD2 . ASP   P  2  117 ? 25.041  -197.570 5.196   1.00 104.48 ? 116 ASP   P OD2 1 
ATOM   27450 N  N   . ILE   P  2  118 ? 23.538  -200.401 9.799   1.00 92.41  ? 117 ILE   P N   1 
ATOM   27451 C  CA  . ILE   P  2  118 ? 23.557  -200.635 11.275  1.00 93.89  ? 117 ILE   P CA  1 
ATOM   27452 C  C   . ILE   P  2  118 ? 23.733  -202.134 11.531  1.00 96.40  ? 117 ILE   P C   1 
ATOM   27453 O  O   . ILE   P  2  118 ? 24.569  -202.489 12.383  1.00 100.87 ? 117 ILE   P O   1 
ATOM   27454 C  CB  . ILE   P  2  118 ? 22.289  -200.071 11.946  1.00 94.09  ? 117 ILE   P CB  1 
ATOM   27455 C  CG1 . ILE   P  2  118 ? 22.344  -198.542 11.999  1.00 93.75  ? 117 ILE   P CG1 1 
ATOM   27456 C  CG2 . ILE   P  2  118 ? 22.081  -200.680 13.328  1.00 92.56  ? 117 ILE   P CG2 1 
ATOM   27457 C  CD1 . ILE   P  2  118 ? 21.021  -197.887 12.287  1.00 94.58  ? 117 ILE   P CD1 1 
ATOM   27458 N  N   . LYS   P  2  119 ? 22.967  -202.968 10.821  1.00 97.07  ? 118 LYS   P N   1 
ATOM   27459 C  CA  . LYS   P  2  119 ? 23.046  -204.451 10.903  1.00 98.41  ? 118 LYS   P CA  1 
ATOM   27460 C  C   . LYS   P  2  119 ? 24.458  -204.910 10.528  1.00 99.66  ? 118 LYS   P C   1 
ATOM   27461 O  O   . LYS   P  2  119 ? 25.014  -205.741 11.273  1.00 107.05 ? 118 LYS   P O   1 
ATOM   27462 C  CB  . LYS   P  2  119 ? 22.009  -205.102 9.986   1.00 100.37 ? 118 LYS   P CB  1 
ATOM   27463 C  CG  . LYS   P  2  119 ? 20.562  -204.971 10.439  1.00 102.37 ? 118 LYS   P CG  1 
ATOM   27464 C  CD  . LYS   P  2  119 ? 19.596  -205.551 9.433   1.00 103.21 ? 118 LYS   P CD  1 
ATOM   27465 C  CE  . LYS   P  2  119 ? 18.151  -205.502 9.875   1.00 102.97 ? 118 LYS   P CE  1 
ATOM   27466 N  NZ  . LYS   P  2  119 ? 17.290  -206.280 8.954   1.00 103.47 ? 118 LYS   P NZ  1 
ATOM   27467 N  N   . GLN   P  2  120 ? 25.007  -204.389 9.423   1.00 94.23  ? 119 GLN   P N   1 
ATOM   27468 C  CA  . GLN   P  2  120 ? 26.364  -204.730 8.907   1.00 95.40  ? 119 GLN   P CA  1 
ATOM   27469 C  C   . GLN   P  2  120 ? 27.403  -204.515 10.015  1.00 97.74  ? 119 GLN   P C   1 
ATOM   27470 O  O   . GLN   P  2  120 ? 28.276  -205.386 10.181  1.00 100.19 ? 119 GLN   P O   1 
ATOM   27471 C  CB  . GLN   P  2  120 ? 26.703  -203.888 7.675   1.00 93.65  ? 119 GLN   P CB  1 
ATOM   27472 C  CG  . GLN   P  2  120 ? 27.997  -204.293 6.973   1.00 93.61  ? 119 GLN   P CG  1 
ATOM   27473 C  CD  . GLN   P  2  120 ? 29.280  -203.852 7.643   1.00 93.94  ? 119 GLN   P CD  1 
ATOM   27474 O  OE1 . GLN   P  2  120 ? 30.301  -204.531 7.574   1.00 92.30  ? 119 GLN   P OE1 1 
ATOM   27475 N  NE2 . GLN   P  2  120 ? 29.260  -202.696 8.285   1.00 95.02  ? 119 GLN   P NE2 1 
ATOM   27476 N  N   . GLY   P  2  121 ? 27.314  -203.394 10.735  1.00 99.89  ? 120 GLY   P N   1 
ATOM   27477 C  CA  . GLY   P  2  121 ? 28.241  -203.036 11.827  1.00 102.17 ? 120 GLY   P CA  1 
ATOM   27478 C  C   . GLY   P  2  121 ? 28.341  -204.139 12.868  1.00 101.53 ? 120 GLY   P C   1 
ATOM   27479 O  O   . GLY   P  2  121 ? 29.475  -204.480 13.264  1.00 103.80 ? 120 GLY   P O   1 
ATOM   27480 N  N   . TYR   P  2  122 ? 27.196  -204.698 13.273  1.00 97.18  ? 121 TYR   P N   1 
ATOM   27481 C  CA  . TYR   P  2  122 ? 27.079  -205.736 14.332  1.00 97.88  ? 121 TYR   P CA  1 
ATOM   27482 C  C   . TYR   P  2  122 ? 27.692  -207.063 13.865  1.00 99.28  ? 121 TYR   P C   1 
ATOM   27483 O  O   . TYR   P  2  122 ? 27.789  -207.978 14.705  1.00 103.51 ? 121 TYR   P O   1 
ATOM   27484 C  CB  . TYR   P  2  122 ? 25.618  -205.928 14.748  1.00 97.19  ? 121 TYR   P CB  1 
ATOM   27485 C  CG  . TYR   P  2  122 ? 25.140  -204.965 15.805  1.00 98.72  ? 121 TYR   P CG  1 
ATOM   27486 C  CD1 . TYR   P  2  122 ? 25.027  -203.610 15.542  1.00 99.43  ? 121 TYR   P CD1 1 
ATOM   27487 C  CD2 . TYR   P  2  122 ? 24.804  -205.408 17.074  1.00 100.45 ? 121 TYR   P CD2 1 
ATOM   27488 C  CE1 . TYR   P  2  122 ? 24.596  -202.720 16.512  1.00 101.18 ? 121 TYR   P CE1 1 
ATOM   27489 C  CE2 . TYR   P  2  122 ? 24.367  -204.533 18.054  1.00 101.79 ? 121 TYR   P CE2 1 
ATOM   27490 C  CZ  . TYR   P  2  122 ? 24.264  -203.184 17.772  1.00 101.18 ? 121 TYR   P CZ  1 
ATOM   27491 O  OH  . TYR   P  2  122 ? 23.833  -202.327 18.741  1.00 104.28 ? 121 TYR   P OH  1 
ATOM   27492 N  N   . THR   P  2  123 ? 28.084  -207.172 12.589  1.00 96.86  ? 122 THR   P N   1 
ATOM   27493 C  CA  . THR   P  2  123 ? 28.707  -208.391 12.003  1.00 98.64  ? 122 THR   P CA  1 
ATOM   27494 C  C   . THR   P  2  123 ? 30.214  -208.203 11.782  1.00 99.15  ? 122 THR   P C   1 
ATOM   27495 O  O   . THR   P  2  123 ? 30.881  -209.222 11.514  1.00 101.93 ? 122 THR   P O   1 
ATOM   27496 C  CB  . THR   P  2  123 ? 28.046  -208.793 10.678  1.00 98.89  ? 122 THR   P CB  1 
ATOM   27497 O  OG1 . THR   P  2  123 ? 28.453  -207.886 9.652   1.00 98.44  ? 122 THR   P OG1 1 
ATOM   27498 C  CG2 . THR   P  2  123 ? 26.536  -208.832 10.763  1.00 99.79  ? 122 THR   P CG2 1 
ATOM   27499 N  N   . GLN   P  2  124 ? 30.732  -206.972 11.877  1.00 97.41  ? 123 GLN   P N   1 
ATOM   27500 C  CA  . GLN   P  2  124 ? 32.159  -206.668 11.578  1.00 99.32  ? 123 GLN   P CA  1 
ATOM   27501 C  C   . GLN   P  2  124 ? 32.918  -206.254 12.845  1.00 97.00  ? 123 GLN   P C   1 
ATOM   27502 O  O   . GLN   P  2  124 ? 34.108  -206.610 12.933  1.00 98.53  ? 123 GLN   P O   1 
ATOM   27503 C  CB  . GLN   P  2  124 ? 32.280  -205.594 10.496  1.00 100.06 ? 123 GLN   P CB  1 
ATOM   27504 C  CG  . GLN   P  2  124 ? 33.712  -205.393 10.016  1.00 101.93 ? 123 GLN   P CG  1 
ATOM   27505 C  CD  . GLN   P  2  124 ? 33.799  -204.808 8.626   1.00 101.04 ? 123 GLN   P CD  1 
ATOM   27506 O  OE1 . GLN   P  2  124 ? 34.542  -205.292 7.777   1.00 104.83 ? 123 GLN   P OE1 1 
ATOM   27507 N  NE2 . GLN   P  2  124 ? 33.041  -203.754 8.380   1.00 101.95 ? 123 GLN   P NE2 1 
ATOM   27508 N  N   . HIS   P  2  125 ? 32.285  -205.528 13.775  1.00 95.28  ? 124 HIS   P N   1 
ATOM   27509 C  CA  . HIS   P  2  125 ? 32.941  -205.018 15.011  1.00 97.09  ? 124 HIS   P CA  1 
ATOM   27510 C  C   . HIS   P  2  125 ? 31.986  -205.069 16.210  1.00 95.88  ? 124 HIS   P C   1 
ATOM   27511 O  O   . HIS   P  2  125 ? 30.764  -205.194 15.995  1.00 91.44  ? 124 HIS   P O   1 
ATOM   27512 C  CB  . HIS   P  2  125 ? 33.493  -203.604 14.782  1.00 97.80  ? 124 HIS   P CB  1 
ATOM   27513 C  CG  . HIS   P  2  125 ? 32.518  -202.643 14.187  1.00 98.77  ? 124 HIS   P CG  1 
ATOM   27514 N  ND1 . HIS   P  2  125 ? 31.561  -201.992 14.942  1.00 96.37  ? 124 HIS   P ND1 1 
ATOM   27515 C  CD2 . HIS   P  2  125 ? 32.361  -202.211 12.917  1.00 99.36  ? 124 HIS   P CD2 1 
ATOM   27516 C  CE1 . HIS   P  2  125 ? 30.850  -201.207 14.159  1.00 97.10  ? 124 HIS   P CE1 1 
ATOM   27517 N  NE2 . HIS   P  2  125 ? 31.321  -201.323 12.911  1.00 99.80  ? 124 HIS   P NE2 1 
ATOM   27518 N  N   . GLY   P  2  126 ? 32.552  -205.000 17.421  1.00 98.12  ? 125 GLY   P N   1 
ATOM   27519 C  CA  . GLY   P  2  126 ? 31.825  -204.759 18.685  1.00 100.06 ? 125 GLY   P CA  1 
ATOM   27520 C  C   . GLY   P  2  126 ? 31.592  -206.024 19.497  1.00 101.05 ? 125 GLY   P C   1 
ATOM   27521 O  O   . GLY   P  2  126 ? 31.232  -205.890 20.683  1.00 102.81 ? 125 GLY   P O   1 
ATOM   27522 N  N   . GLY   P  2  127 ? 31.767  -207.206 18.894  1.00 102.86 ? 126 GLY   P N   1 
ATOM   27523 C  CA  . GLY   P  2  127 ? 31.673  -208.514 19.577  1.00 102.30 ? 126 GLY   P CA  1 
ATOM   27524 C  C   . GLY   P  2  127 ? 30.293  -208.795 20.156  1.00 99.79  ? 126 GLY   P C   1 
ATOM   27525 O  O   . GLY   P  2  127 ? 30.212  -209.614 21.095  1.00 96.67  ? 126 GLY   P O   1 
ATOM   27526 N  N   . LEU   P  2  128 ? 29.246  -208.156 19.622  1.00 99.38  ? 127 LEU   P N   1 
ATOM   27527 C  CA  . LEU   P  2  128 ? 27.833  -208.381 20.033  1.00 96.22  ? 127 LEU   P CA  1 
ATOM   27528 C  C   . LEU   P  2  128 ? 27.162  -209.314 19.022  1.00 95.65  ? 127 LEU   P C   1 
ATOM   27529 O  O   . LEU   P  2  128 ? 27.635  -209.380 17.867  1.00 95.08  ? 127 LEU   P O   1 
ATOM   27530 C  CB  . LEU   P  2  128 ? 27.085  -207.045 20.107  1.00 95.05  ? 127 LEU   P CB  1 
ATOM   27531 C  CG  . LEU   P  2  128 ? 27.672  -205.983 21.034  1.00 94.62  ? 127 LEU   P CG  1 
ATOM   27532 C  CD1 . LEU   P  2  128 ? 26.749  -204.777 21.105  1.00 94.49  ? 127 LEU   P CD1 1 
ATOM   27533 C  CD2 . LEU   P  2  128 ? 27.927  -206.532 22.430  1.00 93.88  ? 127 LEU   P CD2 1 
ATOM   27534 N  N   . ARG   P  2  129 ? 26.095  -209.998 19.440  1.00 94.45  ? 128 ARG   P N   1 
ATOM   27535 C  CA  . ARG   P  2  129 ? 25.278  -210.856 18.543  1.00 95.43  ? 128 ARG   P CA  1 
ATOM   27536 C  C   . ARG   P  2  129 ? 24.575  -209.953 17.535  1.00 95.17  ? 128 ARG   P C   1 
ATOM   27537 O  O   . ARG   P  2  129 ? 24.206  -208.829 17.866  1.00 94.07  ? 128 ARG   P O   1 
ATOM   27538 C  CB  . ARG   P  2  129 ? 24.277  -211.709 19.334  1.00 93.62  ? 128 ARG   P CB  1 
ATOM   27539 C  CG  . ARG   P  2  129 ? 23.142  -210.935 19.992  1.00 93.17  ? 128 ARG   P CG  1 
ATOM   27540 C  CD  . ARG   P  2  129 ? 22.018  -211.843 20.455  1.00 92.50  ? 128 ARG   P CD  1 
ATOM   27541 N  NE  . ARG   P  2  129 ? 20.854  -211.088 20.901  1.00 92.66  ? 128 ARG   P NE  1 
ATOM   27542 C  CZ  . ARG   P  2  129 ? 19.866  -210.658 20.117  1.00 93.57  ? 128 ARG   P CZ  1 
ATOM   27543 N  NH1 . ARG   P  2  129 ? 19.877  -210.905 18.817  1.00 94.91  ? 128 ARG   P NH1 1 
ATOM   27544 N  NH2 . ARG   P  2  129 ? 18.862  -209.973 20.636  1.00 94.34  ? 128 ARG   P NH2 1 
ATOM   27545 N  N   . PRO   P  2  130 ? 24.375  -210.407 16.278  1.00 98.02  ? 129 PRO   P N   1 
ATOM   27546 C  CA  . PRO   P  2  130 ? 23.613  -209.636 15.298  1.00 98.83  ? 129 PRO   P CA  1 
ATOM   27547 C  C   . PRO   P  2  130 ? 22.127  -209.581 15.680  1.00 99.99  ? 129 PRO   P C   1 
ATOM   27548 O  O   . PRO   P  2  130 ? 21.700  -210.375 16.499  1.00 102.56 ? 129 PRO   P O   1 
ATOM   27549 C  CB  . PRO   P  2  130 ? 23.821  -210.402 13.983  1.00 99.79  ? 129 PRO   P CB  1 
ATOM   27550 C  CG  . PRO   P  2  130 ? 24.108  -211.821 14.422  1.00 100.51 ? 129 PRO   P CG  1 
ATOM   27551 C  CD  . PRO   P  2  130 ? 24.843  -211.692 15.740  1.00 99.95  ? 129 PRO   P CD  1 
ATOM   27552 N  N   . PHE   P  2  131 ? 21.384  -208.643 15.091  1.00 100.69 ? 130 PHE   P N   1 
ATOM   27553 C  CA  . PHE   P  2  131 ? 19.908  -208.550 15.220  1.00 101.15 ? 130 PHE   P CA  1 
ATOM   27554 C  C   . PHE   P  2  131 ? 19.281  -209.723 14.464  1.00 101.61 ? 130 PHE   P C   1 
ATOM   27555 O  O   . PHE   P  2  131 ? 19.533  -209.846 13.249  1.00 109.92 ? 130 PHE   P O   1 
ATOM   27556 C  CB  . PHE   P  2  131 ? 19.393  -207.216 14.679  1.00 103.82 ? 130 PHE   P CB  1 
ATOM   27557 C  CG  . PHE   P  2  131 ? 19.807  -206.014 15.488  1.00 103.22 ? 130 PHE   P CG  1 
ATOM   27558 C  CD1 . PHE   P  2  131 ? 19.065  -205.608 16.587  1.00 102.02 ? 130 PHE   P CD1 1 
ATOM   27559 C  CD2 . PHE   P  2  131 ? 20.940  -205.290 15.151  1.00 104.01 ? 130 PHE   P CD2 1 
ATOM   27560 C  CE1 . PHE   P  2  131 ? 19.448  -204.501 17.330  1.00 101.76 ? 130 PHE   P CE1 1 
ATOM   27561 C  CE2 . PHE   P  2  131 ? 21.323  -204.184 15.895  1.00 103.94 ? 130 PHE   P CE2 1 
ATOM   27562 C  CZ  . PHE   P  2  131 ? 20.576  -203.792 16.983  1.00 102.03 ? 130 PHE   P CZ  1 
ATOM   27563 N  N   . GLY   P  2  132 ? 18.504  -210.553 15.164  1.00 99.29  ? 131 GLY   P N   1 
ATOM   27564 C  CA  . GLY   P  2  132 ? 17.772  -211.689 14.572  1.00 96.78  ? 131 GLY   P CA  1 
ATOM   27565 C  C   . GLY   P  2  132 ? 16.488  -211.213 13.921  1.00 94.76  ? 131 GLY   P C   1 
ATOM   27566 O  O   . GLY   P  2  132 ? 15.405  -211.535 14.443  1.00 90.66  ? 131 GLY   P O   1 
ATOM   27567 N  N   . VAL   P  2  133 ? 16.606  -210.439 12.840  1.00 95.44  ? 132 VAL   P N   1 
ATOM   27568 C  CA  . VAL   P  2  133 ? 15.454  -209.789 12.149  1.00 98.15  ? 132 VAL   P CA  1 
ATOM   27569 C  C   . VAL   P  2  133 ? 15.719  -209.730 10.642  1.00 93.95  ? 132 VAL   P C   1 
ATOM   27570 O  O   . VAL   P  2  133 ? 16.854  -209.393 10.245  1.00 91.12  ? 132 VAL   P O   1 
ATOM   27571 C  CB  . VAL   P  2  133 ? 15.188  -208.383 12.717  1.00 99.94  ? 132 VAL   P CB  1 
ATOM   27572 C  CG1 . VAL   P  2  133 ? 14.298  -207.553 11.800  1.00 102.99 ? 132 VAL   P CG1 1 
ATOM   27573 C  CG2 . VAL   P  2  133 ? 14.593  -208.449 14.113  1.00 103.20 ? 132 VAL   P CG2 1 
ATOM   27574 N  N   . SER   P  2  134 ? 14.684  -210.037 9.856   1.00 95.73  ? 133 SER   P N   1 
ATOM   27575 C  CA  . SER   P  2  134 ? 14.572  -209.753 8.403   1.00 97.58  ? 133 SER   P CA  1 
ATOM   27576 C  C   . SER   P  2  134 ? 13.353  -208.852 8.182   1.00 94.89  ? 133 SER   P C   1 
ATOM   27577 O  O   . SER   P  2  134 ? 12.268  -209.193 8.697   1.00 95.14  ? 133 SER   P O   1 
ATOM   27578 C  CB  . SER   P  2  134 ? 14.473  -211.026 7.597   1.00 99.61  ? 133 SER   P CB  1 
ATOM   27579 O  OG  . SER   P  2  134 ? 15.744  -211.642 7.451   1.00 104.76 ? 133 SER   P OG  1 
ATOM   27580 N  N   . PHE   P  2  135 ? 13.536  -207.739 7.467   1.00 93.37  ? 134 PHE   P N   1 
ATOM   27581 C  CA  . PHE   P  2  135 ? 12.478  -206.742 7.162   1.00 95.05  ? 134 PHE   P CA  1 
ATOM   27582 C  C   . PHE   P  2  135 ? 12.049  -206.864 5.699   1.00 91.61  ? 134 PHE   P C   1 
ATOM   27583 O  O   . PHE   P  2  135 ? 12.924  -207.084 4.844   1.00 89.27  ? 134 PHE   P O   1 
ATOM   27584 C  CB  . PHE   P  2  135 ? 12.982  -205.315 7.384   1.00 93.19  ? 134 PHE   P CB  1 
ATOM   27585 C  CG  . PHE   P  2  135 ? 13.158  -204.907 8.824   1.00 94.97  ? 134 PHE   P CG  1 
ATOM   27586 C  CD1 . PHE   P  2  135 ? 12.069  -204.825 9.677   1.00 98.18  ? 134 PHE   P CD1 1 
ATOM   27587 C  CD2 . PHE   P  2  135 ? 14.408  -204.571 9.315   1.00 94.92  ? 134 PHE   P CD2 1 
ATOM   27588 C  CE1 . PHE   P  2  135 ? 12.233  -204.434 10.998  1.00 98.64  ? 134 PHE   P CE1 1 
ATOM   27589 C  CE2 . PHE   P  2  135 ? 14.570  -204.182 10.636  1.00 96.30  ? 134 PHE   P CE2 1 
ATOM   27590 C  CZ  . PHE   P  2  135 ? 13.482  -204.112 11.474  1.00 97.29  ? 134 PHE   P CZ  1 
ATOM   27591 N  N   . ILE   P  2  136 ? 10.747  -206.711 5.436   1.00 95.40  ? 135 ILE   P N   1 
ATOM   27592 C  CA  . ILE   P  2  136 ? 10.194  -206.324 4.103   1.00 101.35 ? 135 ILE   P CA  1 
ATOM   27593 C  C   . ILE   P  2  136 ? 9.796   -204.846 4.185   1.00 101.78 ? 135 ILE   P C   1 
ATOM   27594 O  O   . ILE   P  2  136 ? 8.844   -204.542 4.929   1.00 106.55 ? 135 ILE   P O   1 
ATOM   27595 C  CB  . ILE   P  2  136 ? 8.987   -207.189 3.681   1.00 103.09 ? 135 ILE   P CB  1 
ATOM   27596 C  CG1 . ILE   P  2  136 ? 9.336   -208.679 3.580   1.00 104.15 ? 135 ILE   P CG1 1 
ATOM   27597 C  CG2 . ILE   P  2  136 ? 8.396   -206.653 2.383   1.00 104.15 ? 135 ILE   P CG2 1 
ATOM   27598 C  CD1 . ILE   P  2  136 ? 8.158   -209.576 3.243   1.00 104.00 ? 135 ILE   P CD1 1 
ATOM   27599 N  N   . TYR   P  2  137 ? 10.485  -203.974 3.442   1.00 103.49 ? 136 TYR   P N   1 
ATOM   27600 C  CA  . TYR   P  2  137 ? 10.197  -202.516 3.359   1.00 100.33 ? 136 TYR   P CA  1 
ATOM   27601 C  C   . TYR   P  2  137 ? 9.252   -202.250 2.185   1.00 100.43 ? 136 TYR   P C   1 
ATOM   27602 O  O   . TYR   P  2  137 ? 9.626   -202.545 1.034   1.00 99.17  ? 136 TYR   P O   1 
ATOM   27603 C  CB  . TYR   P  2  137 ? 11.473  -201.695 3.161   1.00 96.69  ? 136 TYR   P CB  1 
ATOM   27604 C  CG  . TYR   P  2  137 ? 12.561  -201.949 4.170   1.00 93.23  ? 136 TYR   P CG  1 
ATOM   27605 C  CD1 . TYR   P  2  137 ? 13.453  -202.995 4.008   1.00 93.09  ? 136 TYR   P CD1 1 
ATOM   27606 C  CD2 . TYR   P  2  137 ? 12.713  -201.135 5.279   1.00 92.64  ? 136 TYR   P CD2 1 
ATOM   27607 C  CE1 . TYR   P  2  137 ? 14.461  -203.234 4.927   1.00 91.99  ? 136 TYR   P CE1 1 
ATOM   27608 C  CE2 . TYR   P  2  137 ? 13.715  -201.359 6.207   1.00 92.35  ? 136 TYR   P CE2 1 
ATOM   27609 C  CZ  . TYR   P  2  137 ? 14.594  -202.414 6.032   1.00 91.36  ? 136 TYR   P CZ  1 
ATOM   27610 O  OH  . TYR   P  2  137 ? 15.591  -202.648 6.935   1.00 89.62  ? 136 TYR   P OH  1 
ATOM   27611 N  N   . ALA   P  2  138 ? 8.070   -201.706 2.477   1.00 100.44 ? 137 ALA   P N   1 
ATOM   27612 C  CA  . ALA   P  2  138 ? 7.074   -201.247 1.483   1.00 100.59 ? 137 ALA   P CA  1 
ATOM   27613 C  C   . ALA   P  2  138 ? 6.932   -199.735 1.626   1.00 101.68 ? 137 ALA   P C   1 
ATOM   27614 O  O   . ALA   P  2  138 ? 6.622   -199.288 2.746   1.00 102.23 ? 137 ALA   P O   1 
ATOM   27615 C  CB  . ALA   P  2  138 ? 5.758   -201.944 1.710   1.00 101.93 ? 137 ALA   P CB  1 
ATOM   27616 N  N   . GLY   P  2  139 ? 7.176   -198.979 0.553   1.00 101.66 ? 138 GLY   P N   1 
ATOM   27617 C  CA  . GLY   P  2  139 ? 7.137   -197.506 0.608   1.00 102.55 ? 138 GLY   P CA  1 
ATOM   27618 C  C   . GLY   P  2  139 ? 7.030   -196.845 -0.753  1.00 101.61 ? 138 GLY   P C   1 
ATOM   27619 O  O   . GLY   P  2  139 ? 7.149   -197.540 -1.781  1.00 99.37  ? 138 GLY   P O   1 
ATOM   27620 N  N   . TYR   P  2  140 ? 6.815   -195.529 -0.741  1.00 103.65 ? 139 TYR   P N   1 
ATOM   27621 C  CA  . TYR   P  2  140 ? 6.671   -194.667 -1.940  1.00 106.10 ? 139 TYR   P CA  1 
ATOM   27622 C  C   . TYR   P  2  140 ? 7.495   -193.386 -1.770  1.00 105.74 ? 139 TYR   P C   1 
ATOM   27623 O  O   . TYR   P  2  140 ? 7.478   -192.784 -0.678  1.00 101.31 ? 139 TYR   P O   1 
ATOM   27624 C  CB  . TYR   P  2  140 ? 5.202   -194.307 -2.174  1.00 109.81 ? 139 TYR   P CB  1 
ATOM   27625 C  CG  . TYR   P  2  140 ? 4.977   -193.376 -3.338  1.00 112.06 ? 139 TYR   P CG  1 
ATOM   27626 C  CD1 . TYR   P  2  140 ? 5.113   -192.004 -3.196  1.00 111.55 ? 139 TYR   P CD1 1 
ATOM   27627 C  CD2 . TYR   P  2  140 ? 4.639   -193.869 -4.588  1.00 113.42 ? 139 TYR   P CD2 1 
ATOM   27628 C  CE1 . TYR   P  2  140 ? 4.915   -191.145 -4.264  1.00 114.07 ? 139 TYR   P CE1 1 
ATOM   27629 C  CE2 . TYR   P  2  140 ? 4.436   -193.024 -5.667  1.00 114.31 ? 139 TYR   P CE2 1 
ATOM   27630 C  CZ  . TYR   P  2  140 ? 4.577   -191.658 -5.503  1.00 113.97 ? 139 TYR   P CZ  1 
ATOM   27631 O  OH  . TYR   P  2  140 ? 4.376   -190.826 -6.564  1.00 119.23 ? 139 TYR   P OH  1 
ATOM   27632 N  N   . ASP   P  2  141 ? 8.179   -192.980 -2.841  1.00 102.61 ? 140 ASP   P N   1 
ATOM   27633 C  CA  . ASP   P  2  141 ? 8.783   -191.631 -2.992  1.00 105.58 ? 140 ASP   P CA  1 
ATOM   27634 C  C   . ASP   P  2  141 ? 8.590   -191.190 -4.447  1.00 107.03 ? 140 ASP   P C   1 
ATOM   27635 O  O   . ASP   P  2  141 ? 8.264   -192.052 -5.287  1.00 102.32 ? 140 ASP   P O   1 
ATOM   27636 C  CB  . ASP   P  2  141 ? 10.244  -191.612 -2.530  1.00 103.24 ? 140 ASP   P CB  1 
ATOM   27637 C  CG  . ASP   P  2  141 ? 11.171  -192.525 -3.313  1.00 102.06 ? 140 ASP   P CG  1 
ATOM   27638 O  OD1 . ASP   P  2  141 ? 11.216  -192.392 -4.552  1.00 101.86 ? 140 ASP   P OD1 1 
ATOM   27639 O  OD2 . ASP   P  2  141 ? 11.851  -193.356 -2.675  1.00 99.60  ? 140 ASP   P OD2 1 
ATOM   27640 N  N   . ASP   P  2  142 ? 8.782   -189.897 -4.726  1.00 111.60 ? 141 ASP   P N   1 
ATOM   27641 C  CA  . ASP   P  2  142 ? 8.472   -189.277 -6.042  1.00 112.89 ? 141 ASP   P CA  1 
ATOM   27642 C  C   . ASP   P  2  142 ? 9.595   -189.553 -7.054  1.00 111.03 ? 141 ASP   P C   1 
ATOM   27643 O  O   . ASP   P  2  142 ? 9.481   -189.045 -8.185  1.00 115.59 ? 141 ASP   P O   1 
ATOM   27644 C  CB  . ASP   P  2  142 ? 8.191   -187.777 -5.895  1.00 117.02 ? 141 ASP   P CB  1 
ATOM   27645 C  CG  . ASP   P  2  142 ? 9.372   -186.954 -5.405  1.00 119.80 ? 141 ASP   P CG  1 
ATOM   27646 O  OD1 . ASP   P  2  142 ? 10.427  -187.555 -5.105  1.00 115.20 ? 141 ASP   P OD1 1 
ATOM   27647 O  OD2 . ASP   P  2  142 ? 9.224   -185.714 -5.321  1.00 124.68 ? 141 ASP   P OD2 1 
ATOM   27648 N  N   . ARG   P  2  143 ? 10.631  -190.320 -6.687  1.00 105.26 ? 142 ARG   P N   1 
ATOM   27649 C  CA  . ARG   P  2  143 ? 11.755  -190.661 -7.603  1.00 106.22 ? 142 ARG   P CA  1 
ATOM   27650 C  C   . ARG   P  2  143 ? 11.473  -191.991 -8.311  1.00 107.06 ? 142 ARG   P C   1 
ATOM   27651 O  O   . ARG   P  2  143 ? 11.509  -192.004 -9.557  1.00 109.12 ? 142 ARG   P O   1 
ATOM   27652 C  CB  . ARG   P  2  143 ? 13.092  -190.731 -6.858  1.00 105.52 ? 142 ARG   P CB  1 
ATOM   27653 C  CG  . ARG   P  2  143 ? 14.287  -190.941 -7.779  1.00 108.00 ? 142 ARG   P CG  1 
ATOM   27654 C  CD  . ARG   P  2  143 ? 15.592  -191.145 -7.033  1.00 107.94 ? 142 ARG   P CD  1 
ATOM   27655 N  NE  . ARG   P  2  143 ? 16.705  -191.425 -7.933  1.00 108.92 ? 142 ARG   P NE  1 
ATOM   27656 C  CZ  . ARG   P  2  143 ? 17.969  -191.604 -7.555  1.00 107.23 ? 142 ARG   P CZ  1 
ATOM   27657 N  NH1 . ARG   P  2  143 ? 18.305  -191.535 -6.277  1.00 106.77 ? 142 ARG   P NH1 1 
ATOM   27658 N  NH2 . ARG   P  2  143 ? 18.899  -191.850 -8.462  1.00 108.60 ? 142 ARG   P NH2 1 
ATOM   27659 N  N   . TYR   P  2  144 ? 11.233  -193.065 -7.550  1.00 107.83 ? 143 TYR   P N   1 
ATOM   27660 C  CA  . TYR   P  2  144 ? 11.072  -194.455 -8.059  1.00 105.81 ? 143 TYR   P CA  1 
ATOM   27661 C  C   . TYR   P  2  144 ? 9.624   -194.942 -7.915  1.00 102.67 ? 143 TYR   P C   1 
ATOM   27662 O  O   . TYR   P  2  144 ? 9.334   -196.057 -8.389  1.00 100.73 ? 143 TYR   P O   1 
ATOM   27663 C  CB  . TYR   P  2  144 ? 12.021  -195.402 -7.322  1.00 105.28 ? 143 TYR   P CB  1 
ATOM   27664 C  CG  . TYR   P  2  144 ? 13.475  -195.226 -7.681  1.00 108.87 ? 143 TYR   P CG  1 
ATOM   27665 C  CD1 . TYR   P  2  144 ? 13.914  -195.402 -8.984  1.00 109.02 ? 143 TYR   P CD1 1 
ATOM   27666 C  CD2 . TYR   P  2  144 ? 14.416  -194.893 -6.720  1.00 109.29 ? 143 TYR   P CD2 1 
ATOM   27667 C  CE1 . TYR   P  2  144 ? 15.248  -195.244 -9.325  1.00 107.45 ? 143 TYR   P CE1 1 
ATOM   27668 C  CE2 . TYR   P  2  144 ? 15.755  -194.732 -7.043  1.00 107.43 ? 143 TYR   P CE2 1 
ATOM   27669 C  CZ  . TYR   P  2  144 ? 16.173  -194.908 -8.351  1.00 104.97 ? 143 TYR   P CZ  1 
ATOM   27670 O  OH  . TYR   P  2  144 ? 17.489  -194.750 -8.677  1.00 99.98  ? 143 TYR   P OH  1 
ATOM   27671 N  N   . GLY   P  2  145 ? 8.747   -194.146 -7.295  1.00 102.11 ? 144 GLY   P N   1 
ATOM   27672 C  CA  . GLY   P  2  145 ? 7.368   -194.555 -6.973  1.00 104.11 ? 144 GLY   P CA  1 
ATOM   27673 C  C   . GLY   P  2  145 ? 7.360   -195.685 -5.958  1.00 104.76 ? 144 GLY   P C   1 
ATOM   27674 O  O   . GLY   P  2  145 ? 8.101   -195.584 -4.956  1.00 107.61 ? 144 GLY   P O   1 
ATOM   27675 N  N   . TYR   P  2  146 ? 6.580   -196.738 -6.214  1.00 103.07 ? 145 TYR   P N   1 
ATOM   27676 C  CA  . TYR   P  2  146 ? 6.409   -197.898 -5.301  1.00 101.58 ? 145 TYR   P CA  1 
ATOM   27677 C  C   . TYR   P  2  146 ? 7.681   -198.751 -5.323  1.00 99.52  ? 145 TYR   P C   1 
ATOM   27678 O  O   . TYR   P  2  146 ? 8.235   -198.976 -6.420  1.00 95.99  ? 145 TYR   P O   1 
ATOM   27679 C  CB  . TYR   P  2  146 ? 5.164   -198.698 -5.685  1.00 103.03 ? 145 TYR   P CB  1 
ATOM   27680 C  CG  . TYR   P  2  146 ? 3.876   -197.935 -5.517  1.00 104.04 ? 145 TYR   P CG  1 
ATOM   27681 C  CD1 . TYR   P  2  146 ? 3.392   -197.630 -4.254  1.00 106.87 ? 145 TYR   P CD1 1 
ATOM   27682 C  CD2 . TYR   P  2  146 ? 3.147   -197.506 -6.614  1.00 103.74 ? 145 TYR   P CD2 1 
ATOM   27683 C  CE1 . TYR   P  2  146 ? 2.215   -196.920 -4.084  1.00 110.25 ? 145 TYR   P CE1 1 
ATOM   27684 C  CE2 . TYR   P  2  146 ? 1.965   -196.800 -6.461  1.00 106.09 ? 145 TYR   P CE2 1 
ATOM   27685 C  CZ  . TYR   P  2  146 ? 1.498   -196.505 -5.192  1.00 109.96 ? 145 TYR   P CZ  1 
ATOM   27686 O  OH  . TYR   P  2  146 ? 0.334   -195.813 -5.035  1.00 116.75 ? 145 TYR   P OH  1 
ATOM   27687 N  N   . GLN   P  2  147 ? 8.134   -199.183 -4.139  1.00 99.89  ? 146 GLN   P N   1 
ATOM   27688 C  CA  . GLN   P  2  147 ? 9.368   -199.992 -3.944  1.00 100.19 ? 146 GLN   P CA  1 
ATOM   27689 C  C   . GLN   P  2  147 ? 9.155   -201.022 -2.828  1.00 102.62 ? 146 GLN   P C   1 
ATOM   27690 O  O   . GLN   P  2  147 ? 8.679   -200.625 -1.743  1.00 102.56 ? 146 GLN   P O   1 
ATOM   27691 C  CB  . GLN   P  2  147 ? 10.543  -199.082 -3.585  1.00 98.44  ? 146 GLN   P CB  1 
ATOM   27692 C  CG  . GLN   P  2  147 ? 10.861  -198.039 -4.647  1.00 100.94 ? 146 GLN   P CG  1 
ATOM   27693 C  CD  . GLN   P  2  147 ? 11.726  -196.923 -4.113  1.00 100.49 ? 146 GLN   P CD  1 
ATOM   27694 O  OE1 . GLN   P  2  147 ? 12.946  -197.046 -4.022  1.00 101.92 ? 146 GLN   P OE1 1 
ATOM   27695 N  NE2 . GLN   P  2  147 ? 11.099  -195.810 -3.763  1.00 100.50 ? 146 GLN   P NE2 1 
ATOM   27696 N  N   . LEU   P  2  148 ? 9.495   -202.291 -3.095  1.00 101.65 ? 147 LEU   P N   1 
ATOM   27697 C  CA  . LEU   P  2  148 ? 9.683   -203.351 -2.066  1.00 99.68  ? 147 LEU   P CA  1 
ATOM   27698 C  C   . LEU   P  2  148 ? 11.178  -203.621 -1.907  1.00 98.20  ? 147 LEU   P C   1 
ATOM   27699 O  O   . LEU   P  2  148 ? 11.853  -203.809 -2.939  1.00 100.88 ? 147 LEU   P O   1 
ATOM   27700 C  CB  . LEU   P  2  148 ? 8.993   -204.652 -2.482  1.00 99.82  ? 147 LEU   P CB  1 
ATOM   27701 C  CG  . LEU   P  2  148 ? 7.504   -204.772 -2.174  1.00 101.24 ? 147 LEU   P CG  1 
ATOM   27702 C  CD1 . LEU   P  2  148 ? 6.957   -206.044 -2.796  1.00 103.39 ? 147 LEU   P CD1 1 
ATOM   27703 C  CD2 . LEU   P  2  148 ? 7.235   -204.760 -0.675  1.00 100.45 ? 147 LEU   P CD2 1 
ATOM   27704 N  N   . TYR   P  2  149 ? 11.655  -203.674 -0.662  1.00 96.40  ? 148 TYR   P N   1 
ATOM   27705 C  CA  . TYR   P  2  149 ? 13.026  -204.111 -0.302  1.00 95.96  ? 148 TYR   P CA  1 
ATOM   27706 C  C   . TYR   P  2  149 ? 12.933  -205.203 0.764   1.00 92.53  ? 148 TYR   P C   1 
ATOM   27707 O  O   . TYR   P  2  149 ? 11.867  -205.363 1.390   1.00 92.20  ? 148 TYR   P O   1 
ATOM   27708 C  CB  . TYR   P  2  149 ? 13.862  -202.936 0.210   1.00 94.93  ? 148 TYR   P CB  1 
ATOM   27709 C  CG  . TYR   P  2  149 ? 14.122  -201.848 -0.801  1.00 95.89  ? 148 TYR   P CG  1 
ATOM   27710 C  CD1 . TYR   P  2  149 ? 15.185  -201.937 -1.687  1.00 96.01  ? 148 TYR   P CD1 1 
ATOM   27711 C  CD2 . TYR   P  2  149 ? 13.316  -200.723 -0.866  1.00 94.50  ? 148 TYR   P CD2 1 
ATOM   27712 C  CE1 . TYR   P  2  149 ? 15.437  -200.942 -2.616  1.00 95.46  ? 148 TYR   P CE1 1 
ATOM   27713 C  CE2 . TYR   P  2  149 ? 13.554  -199.719 -1.790  1.00 94.39  ? 148 TYR   P CE2 1 
ATOM   27714 C  CZ  . TYR   P  2  149 ? 14.618  -199.829 -2.667  1.00 96.05  ? 148 TYR   P CZ  1 
ATOM   27715 O  OH  . TYR   P  2  149 ? 14.863  -198.845 -3.578  1.00 99.22  ? 148 TYR   P OH  1 
ATOM   27716 N  N   . THR   P  2  150 ? 14.026  -205.941 0.946   1.00 91.06  ? 149 THR   P N   1 
ATOM   27717 C  CA  . THR   P  2  150 ? 14.261  -206.805 2.127   1.00 92.88  ? 149 THR   P CA  1 
ATOM   27718 C  C   . THR   P  2  150 ? 15.684  -206.579 2.625   1.00 92.21  ? 149 THR   P C   1 
ATOM   27719 O  O   . THR   P  2  150 ? 16.572  -206.376 1.781   1.00 94.52  ? 149 THR   P O   1 
ATOM   27720 C  CB  . THR   P  2  150 ? 14.047  -208.289 1.817   1.00 92.15  ? 149 THR   P CB  1 
ATOM   27721 O  OG1 . THR   P  2  150 ? 14.789  -208.588 0.637   1.00 93.49  ? 149 THR   P OG1 1 
ATOM   27722 C  CG2 . THR   P  2  150 ? 12.586  -208.639 1.649   1.00 94.57  ? 149 THR   P CG2 1 
ATOM   27723 N  N   . SER   P  2  151 ? 15.865  -206.596 3.945   1.00 94.16  ? 150 SER   P N   1 
ATOM   27724 C  CA  . SER   P  2  151 ? 17.184  -206.667 4.621   1.00 97.83  ? 150 SER   P CA  1 
ATOM   27725 C  C   . SER   P  2  151 ? 17.166  -207.851 5.594   1.00 96.81  ? 150 SER   P C   1 
ATOM   27726 O  O   . SER   P  2  151 ? 16.061  -208.238 6.031   1.00 91.59  ? 150 SER   P O   1 
ATOM   27727 C  CB  . SER   P  2  151 ? 17.524  -205.367 5.308   1.00 100.09 ? 150 SER   P CB  1 
ATOM   27728 O  OG  . SER   P  2  151 ? 16.707  -205.159 6.452   1.00 104.27 ? 150 SER   P OG  1 
ATOM   27729 N  N   . ASN   P  2  152 ? 18.343  -208.409 5.890   1.00 98.72  ? 151 ASN   P N   1 
ATOM   27730 C  CA  . ASN   P  2  152 ? 18.521  -209.582 6.788   1.00 99.24  ? 151 ASN   P CA  1 
ATOM   27731 C  C   . ASN   P  2  152 ? 19.693  -209.308 7.732   1.00 99.04  ? 151 ASN   P C   1 
ATOM   27732 O  O   . ASN   P  2  152 ? 20.416  -208.329 7.553   1.00 97.45  ? 151 ASN   P O   1 
ATOM   27733 C  CB  . ASN   P  2  152 ? 18.678  -210.865 5.967   1.00 98.52  ? 151 ASN   P CB  1 
ATOM   27734 C  CG  . ASN   P  2  152 ? 19.976  -210.928 5.189   1.00 98.20  ? 151 ASN   P CG  1 
ATOM   27735 O  OD1 . ASN   P  2  152 ? 21.038  -210.593 5.708   1.00 93.63  ? 151 ASN   P OD1 1 
ATOM   27736 N  ND2 . ASN   P  2  152 ? 19.904  -211.372 3.946   1.00 101.21 ? 151 ASN   P ND2 1 
ATOM   27737 N  N   . PRO   P  2  153 ? 19.919  -210.163 8.758   1.00 99.78  ? 152 PRO   P N   1 
ATOM   27738 C  CA  . PRO   P  2  153 ? 20.957  -209.923 9.764   1.00 100.30 ? 152 PRO   P CA  1 
ATOM   27739 C  C   . PRO   P  2  153 ? 22.373  -209.615 9.244   1.00 104.81 ? 152 PRO   P C   1 
ATOM   27740 O  O   . PRO   P  2  153 ? 23.141  -209.040 10.004  1.00 106.38 ? 152 PRO   P O   1 
ATOM   27741 C  CB  . PRO   P  2  153 ? 20.988  -211.245 10.545  1.00 99.12  ? 152 PRO   P CB  1 
ATOM   27742 C  CG  . PRO   P  2  153 ? 19.574  -211.760 10.437  1.00 98.93  ? 152 PRO   P CG  1 
ATOM   27743 C  CD  . PRO   P  2  153 ? 19.160  -211.395 9.029   1.00 99.27  ? 152 PRO   P CD  1 
ATOM   27744 N  N   . SER   P  2  154 ? 22.694  -209.997 8.001   1.00 104.05 ? 153 SER   P N   1 
ATOM   27745 C  CA  . SER   P  2  154 ? 24.003  -209.727 7.345   1.00 106.05 ? 153 SER   P CA  1 
ATOM   27746 C  C   . SER   P  2  154 ? 24.156  -208.231 7.050   1.00 109.34 ? 153 SER   P C   1 
ATOM   27747 O  O   . SER   P  2  154 ? 25.311  -207.780 6.924   1.00 119.80 ? 153 SER   P O   1 
ATOM   27748 C  CB  . SER   P  2  154 ? 24.167  -210.518 6.077   1.00 104.09 ? 153 SER   P CB  1 
ATOM   27749 O  OG  . SER   P  2  154 ? 23.334  -210.004 5.051   1.00 104.30 ? 153 SER   P OG  1 
ATOM   27750 N  N   . GLY   P  2  155 ? 23.039  -207.507 6.919   1.00 108.85 ? 154 GLY   P N   1 
ATOM   27751 C  CA  . GLY   P  2  155 ? 23.014  -206.088 6.515   1.00 110.60 ? 154 GLY   P CA  1 
ATOM   27752 C  C   . GLY   P  2  155 ? 23.021  -205.952 5.003   1.00 110.62 ? 154 GLY   P C   1 
ATOM   27753 O  O   . GLY   P  2  155 ? 23.368  -204.865 4.499   1.00 112.22 ? 154 GLY   P O   1 
ATOM   27754 N  N   . ASN   P  2  156 ? 22.668  -207.030 4.303   1.00 109.37 ? 155 ASN   P N   1 
ATOM   27755 C  CA  . ASN   P  2  156 ? 22.500  -207.054 2.829   1.00 107.92 ? 155 ASN   P CA  1 
ATOM   27756 C  C   . ASN   P  2  156 ? 21.028  -206.760 2.526   1.00 104.86 ? 155 ASN   P C   1 
ATOM   27757 O  O   . ASN   P  2  156 ? 20.166  -207.353 3.201   1.00 106.67 ? 155 ASN   P O   1 
ATOM   27758 C  CB  . ASN   P  2  156 ? 22.966  -208.390 2.244   1.00 112.32 ? 155 ASN   P CB  1 
ATOM   27759 C  CG  . ASN   P  2  156 ? 22.769  -208.501 0.747   1.00 118.49 ? 155 ASN   P CG  1 
ATOM   27760 O  OD1 . ASN   P  2  156 ? 22.359  -209.549 0.251   1.00 126.78 ? 155 ASN   P OD1 1 
ATOM   27761 N  ND2 . ASN   P  2  156 ? 23.053  -207.434 0.017   1.00 118.69 ? 155 ASN   P ND2 1 
ATOM   27762 N  N   . TYR   P  2  157 ? 20.755  -205.863 1.575   1.00 100.51 ? 156 TYR   P N   1 
ATOM   27763 C  CA  . TYR   P  2  157 ? 19.380  -205.504 1.138   1.00 101.29 ? 156 TYR   P CA  1 
ATOM   27764 C  C   . TYR   P  2  157 ? 19.276  -205.622 -0.388  1.00 99.92  ? 156 TYR   P C   1 
ATOM   27765 O  O   . TYR   P  2  157 ? 20.290  -205.418 -1.089  1.00 100.33 ? 156 TYR   P O   1 
ATOM   27766 C  CB  . TYR   P  2  157 ? 18.985  -204.118 1.661   1.00 99.08  ? 156 TYR   P CB  1 
ATOM   27767 C  CG  . TYR   P  2  157 ? 19.593  -202.944 0.936   1.00 96.56  ? 156 TYR   P CG  1 
ATOM   27768 C  CD1 . TYR   P  2  157 ? 20.855  -202.474 1.265   1.00 96.33  ? 156 TYR   P CD1 1 
ATOM   27769 C  CD2 . TYR   P  2  157 ? 18.898  -202.282 -0.065  1.00 95.03  ? 156 TYR   P CD2 1 
ATOM   27770 C  CE1 . TYR   P  2  157 ? 21.417  -201.391 0.608   1.00 95.96  ? 156 TYR   P CE1 1 
ATOM   27771 C  CE2 . TYR   P  2  157 ? 19.447  -201.199 -0.733  1.00 94.67  ? 156 TYR   P CE2 1 
ATOM   27772 C  CZ  . TYR   P  2  157 ? 20.711  -200.751 -0.395  1.00 95.10  ? 156 TYR   P CZ  1 
ATOM   27773 O  OH  . TYR   P  2  157 ? 21.258  -199.684 -1.046  1.00 97.24  ? 156 TYR   P OH  1 
ATOM   27774 N  N   . THR   P  2  158 ? 18.080  -205.965 -0.876  1.00 99.20  ? 157 THR   P N   1 
ATOM   27775 C  CA  . THR   P  2  158 ? 17.758  -206.122 -2.320  1.00 102.85 ? 157 THR   P CA  1 
ATOM   27776 C  C   . THR   P  2  158 ? 16.316  -205.678 -2.584  1.00 102.18 ? 157 THR   P C   1 
ATOM   27777 O  O   . THR   P  2  158 ? 15.494  -205.748 -1.644  1.00 99.86  ? 157 THR   P O   1 
ATOM   27778 C  CB  . THR   P  2  158 ? 17.968  -207.567 -2.785  1.00 105.30 ? 157 THR   P CB  1 
ATOM   27779 O  OG1 . THR   P  2  158 ? 17.316  -208.430 -1.854  1.00 112.18 ? 157 THR   P OG1 1 
ATOM   27780 C  CG2 . THR   P  2  158 ? 19.427  -207.951 -2.889  1.00 106.94 ? 157 THR   P CG2 1 
ATOM   27781 N  N   . GLY   P  2  159 ? 16.040  -205.255 -3.823  1.00 104.03 ? 158 GLY   P N   1 
ATOM   27782 C  CA  . GLY   P  2  159 ? 14.722  -204.778 -4.287  1.00 103.73 ? 158 GLY   P CA  1 
ATOM   27783 C  C   . GLY   P  2  159 ? 13.946  -205.882 -4.986  1.00 101.78 ? 158 GLY   P C   1 
ATOM   27784 O  O   . GLY   P  2  159 ? 14.585  -206.706 -5.674  1.00 103.37 ? 158 GLY   P O   1 
ATOM   27785 N  N   . TRP   P  2  160 ? 12.618  -205.900 -4.824  1.00 101.23 ? 159 TRP   P N   1 
ATOM   27786 C  CA  . TRP   P  2  160 ? 11.734  -207.002 -5.290  1.00 103.13 ? 159 TRP   P CA  1 
ATOM   27787 C  C   . TRP   P  2  160 ? 10.444  -206.459 -5.910  1.00 104.54 ? 159 TRP   P C   1 
ATOM   27788 O  O   . TRP   P  2  160 ? 10.048  -205.330 -5.571  1.00 108.55 ? 159 TRP   P O   1 
ATOM   27789 C  CB  . TRP   P  2  160 ? 11.419  -207.951 -4.130  1.00 102.52 ? 159 TRP   P CB  1 
ATOM   27790 C  CG  . TRP   P  2  160 ? 12.643  -208.565 -3.532  1.00 102.93 ? 159 TRP   P CG  1 
ATOM   27791 C  CD1 . TRP   P  2  160 ? 13.318  -208.141 -2.425  1.00 102.89 ? 159 TRP   P CD1 1 
ATOM   27792 C  CD2 . TRP   P  2  160 ? 13.362  -209.705 -4.032  1.00 103.71 ? 159 TRP   P CD2 1 
ATOM   27793 N  NE1 . TRP   P  2  160 ? 14.399  -208.946 -2.194  1.00 103.09 ? 159 TRP   P NE1 1 
ATOM   27794 C  CE2 . TRP   P  2  160 ? 14.453  -209.915 -3.161  1.00 104.08 ? 159 TRP   P CE2 1 
ATOM   27795 C  CE3 . TRP   P  2  160 ? 13.188  -210.572 -5.117  1.00 103.63 ? 159 TRP   P CE3 1 
ATOM   27796 C  CZ2 . TRP   P  2  160 ? 15.363  -210.955 -3.345  1.00 102.88 ? 159 TRP   P CZ2 1 
ATOM   27797 C  CZ3 . TRP   P  2  160 ? 14.089  -211.599 -5.299  1.00 102.24 ? 159 TRP   P CZ3 1 
ATOM   27798 C  CH2 . TRP   P  2  160 ? 15.161  -211.785 -4.424  1.00 102.39 ? 159 TRP   P CH2 1 
ATOM   27799 N  N   . LYS   P  2  161 ? 9.832   -207.260 -6.785  1.00 102.98 ? 160 LYS   P N   1 
ATOM   27800 C  CA  . LYS   P  2  161 ? 8.449   -207.080 -7.302  1.00 104.59 ? 160 LYS   P CA  1 
ATOM   27801 C  C   . LYS   P  2  161 ? 7.474   -207.803 -6.369  1.00 104.08 ? 160 LYS   P C   1 
ATOM   27802 O  O   . LYS   P  2  161 ? 6.366   -207.284 -6.134  1.00 103.17 ? 160 LYS   P O   1 
ATOM   27803 C  CB  . LYS   P  2  161 ? 8.335   -207.645 -8.718  1.00 107.60 ? 160 LYS   P CB  1 
ATOM   27804 C  CG  . LYS   P  2  161 ? 9.081   -206.859 -9.784  1.00 110.47 ? 160 LYS   P CG  1 
ATOM   27805 C  CD  . LYS   P  2  161 ? 9.138   -207.574 -11.109 1.00 114.08 ? 160 LYS   P CD  1 
ATOM   27806 C  CE  . LYS   P  2  161 ? 9.838   -206.770 -12.183 1.00 116.35 ? 160 LYS   P CE  1 
ATOM   27807 N  NZ  . LYS   P  2  161 ? 9.937   -207.535 -13.447 1.00 118.88 ? 160 LYS   P NZ  1 
ATOM   27808 N  N   . ALA   P  2  162 ? 7.877   -208.980 -5.891  1.00 101.14 ? 161 ALA   P N   1 
ATOM   27809 C  CA  . ALA   P  2  162 ? 7.202   -209.753 -4.825  1.00 101.76 ? 161 ALA   P CA  1 
ATOM   27810 C  C   . ALA   P  2  162 ? 8.260   -210.571 -4.077  1.00 99.37  ? 161 ALA   P C   1 
ATOM   27811 O  O   . ALA   P  2  162 ? 9.210   -211.045 -4.733  1.00 100.43 ? 161 ALA   P O   1 
ATOM   27812 C  CB  . ALA   P  2  162 ? 6.131   -210.631 -5.420  1.00 103.04 ? 161 ALA   P CB  1 
ATOM   27813 N  N   . ILE   P  2  163 ? 8.117   -210.706 -2.757  1.00 97.80  ? 162 ILE   P N   1 
ATOM   27814 C  CA  . ILE   P  2  163 ? 9.115   -211.396 -1.889  1.00 96.73  ? 162 ILE   P CA  1 
ATOM   27815 C  C   . ILE   P  2  163 ? 8.438   -211.856 -0.596  1.00 96.97  ? 162 ILE   P C   1 
ATOM   27816 O  O   . ILE   P  2  163 ? 7.449   -211.219 -0.178  1.00 96.66  ? 162 ILE   P O   1 
ATOM   27817 C  CB  . ILE   P  2  163 ? 10.320  -210.473 -1.615  1.00 96.80  ? 162 ILE   P CB  1 
ATOM   27818 C  CG1 . ILE   P  2  163 ? 11.466  -211.205 -0.908  1.00 97.06  ? 162 ILE   P CG1 1 
ATOM   27819 C  CG2 . ILE   P  2  163 ? 9.892   -209.229 -0.849  1.00 96.57  ? 162 ILE   P CG2 1 
ATOM   27820 C  CD1 . ILE   P  2  163 ? 12.091  -212.318 -1.721  1.00 98.54  ? 162 ILE   P CD1 1 
ATOM   27821 N  N   . SER   P  2  164 ? 8.970   -212.928 -0.002  1.00 96.78  ? 163 SER   P N   1 
ATOM   27822 C  CA  . SER   P  2  164 ? 8.563   -213.493 1.310   1.00 96.65  ? 163 SER   P CA  1 
ATOM   27823 C  C   . SER   P  2  164 ? 9.782   -213.568 2.237   1.00 95.00  ? 163 SER   P C   1 
ATOM   27824 O  O   . SER   P  2  164 ? 10.914  -213.677 1.723   1.00 95.03  ? 163 SER   P O   1 
ATOM   27825 C  CB  . SER   P  2  164 ? 7.927   -214.845 1.130   1.00 97.75  ? 163 SER   P CB  1 
ATOM   27826 O  OG  . SER   P  2  164 ? 8.837   -215.745 0.516   1.00 98.55  ? 163 SER   P OG  1 
ATOM   27827 N  N   . VAL   P  2  165 ? 9.553   -213.502 3.552   1.00 94.14  ? 164 VAL   P N   1 
ATOM   27828 C  CA  . VAL   P  2  165 ? 10.588  -213.711 4.609   1.00 97.20  ? 164 VAL   P CA  1 
ATOM   27829 C  C   . VAL   P  2  165 ? 9.984   -214.554 5.735   1.00 94.13  ? 164 VAL   P C   1 
ATOM   27830 O  O   . VAL   P  2  165 ? 8.747   -214.549 5.887   1.00 95.35  ? 164 VAL   P O   1 
ATOM   27831 C  CB  . VAL   P  2  165 ? 11.120  -212.382 5.174   1.00 96.89  ? 164 VAL   P CB  1 
ATOM   27832 C  CG1 . VAL   P  2  165 ? 11.946  -211.622 4.149   1.00 98.53  ? 164 VAL   P CG1 1 
ATOM   27833 C  CG2 . VAL   P  2  165 ? 9.999   -211.514 5.731   1.00 99.15  ? 164 VAL   P CG2 1 
ATOM   27834 N  N   . GLY   P  2  166 ? 10.845  -215.203 6.520   1.00 93.44  ? 165 GLY   P N   1 
ATOM   27835 C  CA  . GLY   P  2  166 ? 10.447  -216.077 7.636   1.00 95.51  ? 165 GLY   P CA  1 
ATOM   27836 C  C   . GLY   P  2  166 ? 10.337  -217.520 7.182   1.00 96.77  ? 165 GLY   P C   1 
ATOM   27837 O  O   . GLY   P  2  166 ? 11.266  -217.986 6.494   1.00 96.64  ? 165 GLY   P O   1 
ATOM   27838 N  N   . ALA   P  2  167 ? 9.233   -218.190 7.532   1.00 100.40 ? 166 ALA   P N   1 
ATOM   27839 C  CA  . ALA   P  2  167 ? 9.003   -219.639 7.318   1.00 102.15 ? 166 ALA   P CA  1 
ATOM   27840 C  C   . ALA   P  2  167 ? 8.542   -219.906 5.882   1.00 103.60 ? 166 ALA   P C   1 
ATOM   27841 O  O   . ALA   P  2  167 ? 7.798   -219.070 5.330   1.00 105.20 ? 166 ALA   P O   1 
ATOM   27842 C  CB  . ALA   P  2  167 ? 7.992   -220.155 8.314   1.00 103.25 ? 166 ALA   P CB  1 
ATOM   27843 N  N   . ASN   P  2  168 ? 8.980   -221.035 5.313   1.00 104.66 ? 167 ASN   P N   1 
ATOM   27844 C  CA  . ASN   P  2  168 ? 8.479   -221.605 4.033   1.00 105.85 ? 167 ASN   P CA  1 
ATOM   27845 C  C   . ASN   P  2  168 ? 8.637   -220.590 2.894   1.00 104.18 ? 167 ASN   P C   1 
ATOM   27846 O  O   . ASN   P  2  168 ? 7.717   -220.498 2.053   1.00 100.52 ? 167 ASN   P O   1 
ATOM   27847 C  CB  . ASN   P  2  168 ? 7.015   -222.033 4.159   1.00 110.08 ? 167 ASN   P CB  1 
ATOM   27848 C  CG  . ASN   P  2  168 ? 6.766   -222.953 5.335   1.00 112.53 ? 167 ASN   P CG  1 
ATOM   27849 O  OD1 . ASN   P  2  168 ? 7.533   -223.882 5.575   1.00 115.67 ? 167 ASN   P OD1 1 
ATOM   27850 N  ND2 . ASN   P  2  168 ? 5.691   -222.710 6.068   1.00 113.04 ? 167 ASN   P ND2 1 
ATOM   27851 N  N   . THR   P  2  169 ? 9.753   -219.855 2.867   1.00 103.52 ? 168 THR   P N   1 
ATOM   27852 C  CA  . THR   P  2  169 ? 10.074  -218.864 1.804   1.00 102.84 ? 168 THR   P CA  1 
ATOM   27853 C  C   . THR   P  2  169 ? 10.262  -219.593 0.469   1.00 101.89 ? 168 THR   P C   1 
ATOM   27854 O  O   . THR   P  2  169 ? 9.821   -219.051 -0.565  1.00 97.78  ? 168 THR   P O   1 
ATOM   27855 C  CB  . THR   P  2  169 ? 11.320  -218.043 2.158   1.00 104.82 ? 168 THR   P CB  1 
ATOM   27856 O  OG1 . THR   P  2  169 ? 12.367  -218.965 2.466   1.00 105.63 ? 168 THR   P OG1 1 
ATOM   27857 C  CG2 . THR   P  2  169 ? 11.093  -217.099 3.319   1.00 105.22 ? 168 THR   P CG2 1 
ATOM   27858 N  N   . SER   P  2  170 ? 10.884  -220.775 0.502   1.00 102.81 ? 169 SER   P N   1 
ATOM   27859 C  CA  . SER   P  2  170 ? 11.199  -221.610 -0.686  1.00 103.11 ? 169 SER   P CA  1 
ATOM   27860 C  C   . SER   P  2  170 ? 9.910   -221.950 -1.442  1.00 101.55 ? 169 SER   P C   1 
ATOM   27861 O  O   . SER   P  2  170 ? 9.883   -221.763 -2.672  1.00 99.90  ? 169 SER   P O   1 
ATOM   27862 C  CB  . SER   P  2  170 ? 11.940  -222.859 -0.295  1.00 106.70 ? 169 SER   P CB  1 
ATOM   27863 O  OG  . SER   P  2  170 ? 12.487  -223.494 -1.439  1.00 108.43 ? 169 SER   P OG  1 
ATOM   27864 N  N   . ALA   P  2  171 ? 8.888   -222.430 -0.729  1.00 100.20 ? 170 ALA   P N   1 
ATOM   27865 C  CA  . ALA   P  2  171 ? 7.563   -222.774 -1.294  1.00 104.74 ? 170 ALA   P CA  1 
ATOM   27866 C  C   . ALA   P  2  171 ? 6.812   -221.496 -1.685  1.00 106.47 ? 170 ALA   P C   1 
ATOM   27867 O  O   . ALA   P  2  171 ? 6.228   -221.473 -2.787  1.00 112.66 ? 170 ALA   P O   1 
ATOM   27868 C  CB  . ALA   P  2  171 ? 6.772   -223.596 -0.311  1.00 106.01 ? 170 ALA   P CB  1 
ATOM   27869 N  N   . ALA   P  2  172 ? 6.829   -220.478 -0.818  1.00 104.31 ? 171 ALA   P N   1 
ATOM   27870 C  CA  . ALA   P  2  172 ? 6.134   -219.183 -1.014  1.00 103.00 ? 171 ALA   P CA  1 
ATOM   27871 C  C   . ALA   P  2  172 ? 6.662   -218.484 -2.272  1.00 101.60 ? 171 ALA   P C   1 
ATOM   27872 O  O   . ALA   P  2  172 ? 5.829   -217.996 -3.057  1.00 100.57 ? 171 ALA   P O   1 
ATOM   27873 C  CB  . ALA   P  2  172 ? 6.296   -218.314 0.209   1.00 102.06 ? 171 ALA   P CB  1 
ATOM   27874 N  N   . GLN   P  2  173 ? 7.986   -218.452 -2.461  1.00 100.37 ? 172 GLN   P N   1 
ATOM   27875 C  CA  . GLN   P  2  173 ? 8.649   -217.748 -3.593  1.00 102.59 ? 172 GLN   P CA  1 
ATOM   27876 C  C   . GLN   P  2  173 ? 8.271   -218.422 -4.919  1.00 105.63 ? 172 GLN   P C   1 
ATOM   27877 O  O   . GLN   P  2  173 ? 8.016   -217.689 -5.893  1.00 105.92 ? 172 GLN   P O   1 
ATOM   27878 C  CB  . GLN   P  2  173 ? 10.169  -217.708 -3.414  1.00 102.07 ? 172 GLN   P CB  1 
ATOM   27879 C  CG  . GLN   P  2  173 ? 10.839  -216.579 -4.188  1.00 103.17 ? 172 GLN   P CG  1 
ATOM   27880 C  CD  . GLN   P  2  173 ? 10.415  -215.213 -3.703  1.00 104.68 ? 172 GLN   P CD  1 
ATOM   27881 O  OE1 . GLN   P  2  173 ? 9.922   -215.051 -2.588  1.00 102.71 ? 172 GLN   P OE1 1 
ATOM   27882 N  NE2 . GLN   P  2  173 ? 10.602  -214.209 -4.547  1.00 107.21 ? 172 GLN   P NE2 1 
ATOM   27883 N  N   . THR   P  2  174 ? 8.237   -219.758 -4.957  1.00 104.36 ? 173 THR   P N   1 
ATOM   27884 C  CA  . THR   P  2  174 ? 7.839   -220.555 -6.150  1.00 108.25 ? 173 THR   P CA  1 
ATOM   27885 C  C   . THR   P  2  174 ? 6.411   -220.177 -6.567  1.00 109.30 ? 173 THR   P C   1 
ATOM   27886 O  O   . THR   P  2  174 ? 6.195   -219.965 -7.775  1.00 113.73 ? 173 THR   P O   1 
ATOM   27887 C  CB  . THR   P  2  174 ? 7.948   -222.067 -5.903  1.00 106.46 ? 173 THR   P CB  1 
ATOM   27888 O  OG1 . THR   P  2  174 ? 9.184   -222.354 -5.250  1.00 105.19 ? 173 THR   P OG1 1 
ATOM   27889 C  CG2 . THR   P  2  174 ? 7.873   -222.873 -7.181  1.00 108.24 ? 173 THR   P CG2 1 
ATOM   27890 N  N   . LEU   P  2  175 ? 5.484   -220.093 -5.603  1.00 110.51 ? 174 LEU   P N   1 
ATOM   27891 C  CA  . LEU   P  2  175 ? 4.042   -219.783 -5.829  1.00 112.21 ? 174 LEU   P CA  1 
ATOM   27892 C  C   . LEU   P  2  175 ? 3.872   -218.344 -6.332  1.00 111.83 ? 174 LEU   P C   1 
ATOM   27893 O  O   . LEU   P  2  175 ? 3.024   -218.136 -7.222  1.00 109.11 ? 174 LEU   P O   1 
ATOM   27894 C  CB  . LEU   P  2  175 ? 3.259   -219.981 -4.527  1.00 116.31 ? 174 LEU   P CB  1 
ATOM   27895 C  CG  . LEU   P  2  175 ? 3.067   -221.428 -4.076  1.00 120.33 ? 174 LEU   P CG  1 
ATOM   27896 C  CD1 . LEU   P  2  175 ? 2.427   -221.480 -2.697  1.00 121.79 ? 174 LEU   P CD1 1 
ATOM   27897 C  CD2 . LEU   P  2  175 ? 2.228   -222.207 -5.077  1.00 125.11 ? 174 LEU   P CD2 1 
ATOM   27898 N  N   . LEU   P  2  176 ? 4.619   -217.391 -5.761  1.00 110.50 ? 175 LEU   P N   1 
ATOM   27899 C  CA  . LEU   P  2  176 ? 4.608   -215.963 -6.182  1.00 111.25 ? 175 LEU   P CA  1 
ATOM   27900 C  C   . LEU   P  2  176 ? 5.179   -215.863 -7.601  1.00 112.72 ? 175 LEU   P C   1 
ATOM   27901 O  O   . LEU   P  2  176 ? 4.558   -215.178 -8.434  1.00 116.53 ? 175 LEU   P O   1 
ATOM   27902 C  CB  . LEU   P  2  176 ? 5.418   -215.115 -5.194  1.00 108.92 ? 175 LEU   P CB  1 
ATOM   27903 C  CG  . LEU   P  2  176 ? 4.778   -214.898 -3.822  1.00 107.77 ? 175 LEU   P CG  1 
ATOM   27904 C  CD1 . LEU   P  2  176 ? 5.768   -214.250 -2.866  1.00 108.02 ? 175 LEU   P CD1 1 
ATOM   27905 C  CD2 . LEU   P  2  176 ? 3.512   -214.058 -3.926  1.00 106.98 ? 175 LEU   P CD2 1 
ATOM   27906 N  N   . GLN   P  2  177 ? 6.298   -216.548 -7.861  1.00 112.86 ? 176 GLN   P N   1 
ATOM   27907 C  CA  . GLN   P  2  177 ? 6.992   -216.582 -9.179  1.00 114.55 ? 176 GLN   P CA  1 
ATOM   27908 C  C   . GLN   P  2  177 ? 6.040   -217.118 -10.254 1.00 115.56 ? 176 GLN   P C   1 
ATOM   27909 O  O   . GLN   P  2  177 ? 6.206   -216.746 -11.431 1.00 113.07 ? 176 GLN   P O   1 
ATOM   27910 C  CB  . GLN   P  2  177 ? 8.253   -217.444 -9.093  1.00 120.28 ? 176 GLN   P CB  1 
ATOM   27911 C  CG  . GLN   P  2  177 ? 9.187   -217.284 -10.286 1.00 125.03 ? 176 GLN   P CG  1 
ATOM   27912 C  CD  . GLN   P  2  177 ? 10.518  -217.988 -10.145 1.00 130.66 ? 176 GLN   P CD  1 
ATOM   27913 O  OE1 . GLN   P  2  177 ? 11.244  -218.161 -11.122 1.00 136.88 ? 176 GLN   P OE1 1 
ATOM   27914 N  NE2 . GLN   P  2  177 ? 10.869  -218.395 -8.932  1.00 132.70 ? 176 GLN   P NE2 1 
ATOM   27915 N  N   . MET   P  2  178 ? 5.085   -217.959 -9.853  1.00 117.00 ? 177 MET   P N   1 
ATOM   27916 C  CA  . MET   P  2  178 ? 4.132   -218.660 -10.752 1.00 121.91 ? 177 MET   P CA  1 
ATOM   27917 C  C   . MET   P  2  178 ? 3.027   -217.703 -11.219 1.00 121.30 ? 177 MET   P C   1 
ATOM   27918 O  O   . MET   P  2  178 ? 2.778   -217.668 -12.438 1.00 119.55 ? 177 MET   P O   1 
ATOM   27919 C  CB  . MET   P  2  178 ? 3.508   -219.853 -10.020 1.00 127.76 ? 177 MET   P CB  1 
ATOM   27920 C  CG  . MET   P  2  178 ? 2.740   -220.803 -10.914 1.00 132.27 ? 177 MET   P CG  1 
ATOM   27921 S  SD  . MET   P  2  178 ? 2.378   -222.369 -10.067 1.00 138.70 ? 177 MET   P SD  1 
ATOM   27922 C  CE  . MET   P  2  178 ? 3.941   -223.218 -10.281 1.00 139.73 ? 177 MET   P CE  1 
ATOM   27923 N  N   . ASP   P  2  179 ? 2.400   -216.958 -10.298 1.00 121.59 ? 178 ASP   P N   1 
ATOM   27924 C  CA  . ASP   P  2  179 ? 1.124   -216.223 -10.541 1.00 122.56 ? 178 ASP   P CA  1 
ATOM   27925 C  C   . ASP   P  2  179 ? 1.323   -214.700 -10.613 1.00 121.05 ? 178 ASP   P C   1 
ATOM   27926 O  O   . ASP   P  2  179 ? 0.320   -214.006 -10.872 1.00 122.63 ? 178 ASP   P O   1 
ATOM   27927 C  CB  . ASP   P  2  179 ? 0.087   -216.550 -9.462  1.00 121.31 ? 178 ASP   P CB  1 
ATOM   27928 C  CG  . ASP   P  2  179 ? -0.304  -218.015 -9.404  1.00 121.74 ? 178 ASP   P CG  1 
ATOM   27929 O  OD1 . ASP   P  2  179 ? 0.022   -218.749 -10.358 1.00 122.16 ? 178 ASP   P OD1 1 
ATOM   27930 O  OD2 . ASP   P  2  179 ? -0.933  -218.410 -8.404  1.00 120.42 ? 178 ASP   P OD2 1 
ATOM   27931 N  N   . TYR   P  2  180 ? 2.536   -214.182 -10.398 1.00 120.42 ? 179 TYR   P N   1 
ATOM   27932 C  CA  . TYR   P  2  180 ? 2.820   -212.725 -10.503 1.00 121.47 ? 179 TYR   P CA  1 
ATOM   27933 C  C   . TYR   P  2  180 ? 2.996   -212.350 -11.979 1.00 125.48 ? 179 TYR   P C   1 
ATOM   27934 O  O   . TYR   P  2  180 ? 3.585   -213.145 -12.739 1.00 126.70 ? 179 TYR   P O   1 
ATOM   27935 C  CB  . TYR   P  2  180 ? 4.050   -212.318 -9.685  1.00 118.59 ? 179 TYR   P CB  1 
ATOM   27936 C  CG  . TYR   P  2  180 ? 4.325   -210.835 -9.696  1.00 115.61 ? 179 TYR   P CG  1 
ATOM   27937 C  CD1 . TYR   P  2  180 ? 3.699   -209.986 -8.798  1.00 117.09 ? 179 TYR   P CD1 1 
ATOM   27938 C  CD2 . TYR   P  2  180 ? 5.189   -210.273 -10.623 1.00 115.65 ? 179 TYR   P CD2 1 
ATOM   27939 C  CE1 . TYR   P  2  180 ? 3.935   -208.620 -8.809  1.00 119.56 ? 179 TYR   P CE1 1 
ATOM   27940 C  CE2 . TYR   P  2  180 ? 5.435   -208.910 -10.649 1.00 118.74 ? 179 TYR   P CE2 1 
ATOM   27941 C  CZ  . TYR   P  2  180 ? 4.806   -208.079 -9.738  1.00 120.60 ? 179 TYR   P CZ  1 
ATOM   27942 O  OH  . TYR   P  2  180 ? 5.043   -206.735 -9.749  1.00 125.86 ? 179 TYR   P OH  1 
ATOM   27943 N  N   . LYS   P  2  181 ? 2.476   -211.179 -12.364 1.00 130.93 ? 180 LYS   P N   1 
ATOM   27944 C  CA  . LYS   P  2  181 ? 2.785   -210.491 -13.648 1.00 131.98 ? 180 LYS   P CA  1 
ATOM   27945 C  C   . LYS   P  2  181 ? 2.811   -208.974 -13.404 1.00 133.71 ? 180 LYS   P C   1 
ATOM   27946 O  O   . LYS   P  2  181 ? 2.230   -208.523 -12.399 1.00 135.33 ? 180 LYS   P O   1 
ATOM   27947 C  CB  . LYS   P  2  181 ? 1.808   -210.904 -14.756 1.00 132.63 ? 180 LYS   P CB  1 
ATOM   27948 C  CG  . LYS   P  2  181 ? 0.377   -211.200 -14.327 1.00 135.89 ? 180 LYS   P CG  1 
ATOM   27949 C  CD  . LYS   P  2  181 ? -0.369  -212.088 -15.310 1.00 138.34 ? 180 LYS   P CD  1 
ATOM   27950 C  CE  . LYS   P  2  181 ? -0.389  -211.553 -16.729 1.00 140.50 ? 180 LYS   P CE  1 
ATOM   27951 N  NZ  . LYS   P  2  181 ? -1.170  -210.299 -16.843 1.00 141.23 ? 180 LYS   P NZ  1 
ATOM   27952 N  N   . ASP   P  2  182 ? 3.470   -208.229 -14.297 1.00 134.73 ? 181 ASP   P N   1 
ATOM   27953 C  CA  . ASP   P  2  182 ? 3.931   -206.832 -14.070 1.00 132.08 ? 181 ASP   P CA  1 
ATOM   27954 C  C   . ASP   P  2  182 ? 2.748   -205.853 -14.060 1.00 131.38 ? 181 ASP   P C   1 
ATOM   27955 O  O   . ASP   P  2  182 ? 2.778   -204.919 -13.233 1.00 131.58 ? 181 ASP   P O   1 
ATOM   27956 C  CB  . ASP   P  2  182 ? 4.987   -206.440 -15.108 1.00 132.64 ? 181 ASP   P CB  1 
ATOM   27957 C  CG  . ASP   P  2  182 ? 6.286   -207.220 -14.979 1.00 131.38 ? 181 ASP   P CG  1 
ATOM   27958 O  OD1 . ASP   P  2  182 ? 6.540   -207.765 -13.885 1.00 130.09 ? 181 ASP   P OD1 1 
ATOM   27959 O  OD2 . ASP   P  2  182 ? 7.031   -207.281 -15.976 1.00 132.45 ? 181 ASP   P OD2 1 
ATOM   27960 N  N   . ASP   P  2  183 ? 1.748   -206.055 -14.926 1.00 131.89 ? 182 ASP   P N   1 
ATOM   27961 C  CA  . ASP   P  2  183 ? 0.587   -205.135 -15.095 1.00 131.63 ? 182 ASP   P CA  1 
ATOM   27962 C  C   . ASP   P  2  183 ? -0.459  -205.366 -13.992 1.00 126.70 ? 182 ASP   P C   1 
ATOM   27963 O  O   . ASP   P  2  183 ? -1.546  -204.764 -14.083 1.00 127.88 ? 182 ASP   P O   1 
ATOM   27964 C  CB  . ASP   P  2  183 ? -0.046  -205.282 -16.483 1.00 132.49 ? 182 ASP   P CB  1 
ATOM   27965 C  CG  . ASP   P  2  183 ? -0.506  -206.692 -16.822 1.00 132.02 ? 182 ASP   P CG  1 
ATOM   27966 O  OD1 . ASP   P  2  183 ? -1.047  -207.371 -15.926 1.00 132.76 ? 182 ASP   P OD1 1 
ATOM   27967 O  OD2 . ASP   P  2  183 ? -0.313  -207.102 -17.982 1.00 135.51 ? 182 ASP   P OD2 1 
ATOM   27968 N  N   . MET   P  2  184 ? -0.142  -206.199 -12.996 1.00 125.03 ? 183 MET   P N   1 
ATOM   27969 C  CA  . MET   P  2  184 ? -1.024  -206.561 -11.852 1.00 125.34 ? 183 MET   P CA  1 
ATOM   27970 C  C   . MET   P  2  184 ? -1.524  -205.299 -11.134 1.00 125.21 ? 183 MET   P C   1 
ATOM   27971 O  O   . MET   P  2  184 ? -0.781  -204.295 -11.112 1.00 124.74 ? 183 MET   P O   1 
ATOM   27972 C  CB  . MET   P  2  184 ? -0.247  -207.415 -10.848 1.00 123.71 ? 183 MET   P CB  1 
ATOM   27973 C  CG  . MET   P  2  184 ? -1.092  -208.417 -10.116 1.00 125.92 ? 183 MET   P CG  1 
ATOM   27974 S  SD  . MET   P  2  184 ? -0.049  -209.540 -9.167  1.00 127.68 ? 183 MET   P SD  1 
ATOM   27975 C  CE  . MET   P  2  184 ? -1.291  -210.669 -8.543  1.00 131.62 ? 183 MET   P CE  1 
ATOM   27976 N  N   . LYS   P  2  185 ? -2.727  -205.369 -10.551 1.00 124.08 ? 184 LYS   P N   1 
ATOM   27977 C  CA  . LYS   P  2  185 ? -3.347  -204.286 -9.736  1.00 127.00 ? 184 LYS   P CA  1 
ATOM   27978 C  C   . LYS   P  2  185 ? -3.299  -204.682 -8.256  1.00 123.94 ? 184 LYS   P C   1 
ATOM   27979 O  O   . LYS   P  2  185 ? -3.054  -205.869 -7.976  1.00 124.79 ? 184 LYS   P O   1 
ATOM   27980 C  CB  . LYS   P  2  185 ? -4.791  -204.033 -10.181 1.00 128.48 ? 184 LYS   P CB  1 
ATOM   27981 C  CG  . LYS   P  2  185 ? -4.954  -203.345 -11.532 1.00 132.20 ? 184 LYS   P CG  1 
ATOM   27982 C  CD  . LYS   P  2  185 ? -4.628  -201.859 -11.519 1.00 133.16 ? 184 LYS   P CD  1 
ATOM   27983 C  CE  . LYS   P  2  185 ? -3.384  -201.502 -12.307 1.00 131.49 ? 184 LYS   P CE  1 
ATOM   27984 N  NZ  . LYS   P  2  185 ? -3.644  -201.502 -13.766 1.00 132.28 ? 184 LYS   P NZ  1 
ATOM   27985 N  N   . VAL   P  2  186 ? -3.533  -203.722 -7.353  1.00 127.20 ? 185 VAL   P N   1 
ATOM   27986 C  CA  . VAL   P  2  186 ? -3.445  -203.900 -5.870  1.00 126.12 ? 185 VAL   P CA  1 
ATOM   27987 C  C   . VAL   P  2  186 ? -4.388  -205.030 -5.437  1.00 125.78 ? 185 VAL   P C   1 
ATOM   27988 O  O   . VAL   P  2  186 ? -3.949  -205.891 -4.654  1.00 120.15 ? 185 VAL   P O   1 
ATOM   27989 C  CB  . VAL   P  2  186 ? -3.762  -202.594 -5.112  1.00 128.26 ? 185 VAL   P CB  1 
ATOM   27990 C  CG1 . VAL   P  2  186 ? -4.009  -202.834 -3.628  1.00 127.60 ? 185 VAL   P CG1 1 
ATOM   27991 C  CG2 . VAL   P  2  186 ? -2.669  -201.551 -5.300  1.00 129.48 ? 185 VAL   P CG2 1 
ATOM   27992 N  N   . ASP   P  2  187 ? -5.633  -205.017 -5.923  1.00 127.48 ? 186 ASP   P N   1 
ATOM   27993 C  CA  . ASP   P  2  187 ? -6.703  -205.961 -5.498  1.00 130.48 ? 186 ASP   P CA  1 
ATOM   27994 C  C   . ASP   P  2  187 ? -6.320  -207.386 -5.916  1.00 126.66 ? 186 ASP   P C   1 
ATOM   27995 O  O   . ASP   P  2  187 ? -6.637  -208.322 -5.159  1.00 125.32 ? 186 ASP   P O   1 
ATOM   27996 C  CB  . ASP   P  2  187 ? -8.069  -205.550 -6.052  1.00 135.93 ? 186 ASP   P CB  1 
ATOM   27997 C  CG  . ASP   P  2  187 ? -8.476  -204.139 -5.663  1.00 139.55 ? 186 ASP   P CG  1 
ATOM   27998 O  OD1 . ASP   P  2  187 ? -7.800  -203.191 -6.112  1.00 142.31 ? 186 ASP   P OD1 1 
ATOM   27999 O  OD2 . ASP   P  2  187 ? -9.453  -204.001 -4.903  1.00 150.08 ? 186 ASP   P OD2 1 
ATOM   28000 N  N   . ASP   P  2  188 ? -5.661  -207.533 -7.070  1.00 125.55 ? 187 ASP   P N   1 
ATOM   28001 C  CA  . ASP   P  2  188 ? -5.111  -208.823 -7.565  1.00 125.21 ? 187 ASP   P CA  1 
ATOM   28002 C  C   . ASP   P  2  188 ? -3.985  -209.274 -6.627  1.00 121.84 ? 187 ASP   P C   1 
ATOM   28003 O  O   . ASP   P  2  188 ? -3.949  -210.470 -6.290  1.00 123.50 ? 187 ASP   P O   1 
ATOM   28004 C  CB  . ASP   P  2  188 ? -4.615  -208.706 -9.010  1.00 128.75 ? 187 ASP   P CB  1 
ATOM   28005 C  CG  . ASP   P  2  188 ? -5.692  -208.324 -10.012 1.00 131.12 ? 187 ASP   P CG  1 
ATOM   28006 O  OD1 . ASP   P  2  188 ? -6.855  -208.727 -9.809  1.00 136.34 ? 187 ASP   P OD1 1 
ATOM   28007 O  OD2 . ASP   P  2  188 ? -5.360  -207.620 -10.989 1.00 133.07 ? 187 ASP   P OD2 1 
ATOM   28008 N  N   . ALA   P  2  189 ? -3.109  -208.345 -6.226  1.00 119.19 ? 188 ALA   P N   1 
ATOM   28009 C  CA  . ALA   P  2  189 ? -1.937  -208.586 -5.348  1.00 115.33 ? 188 ALA   P CA  1 
ATOM   28010 C  C   . ALA   P  2  189 ? -2.397  -208.986 -3.940  1.00 113.04 ? 188 ALA   P C   1 
ATOM   28011 O  O   . ALA   P  2  189 ? -1.720  -209.832 -3.325  1.00 109.13 ? 188 ALA   P O   1 
ATOM   28012 C  CB  . ALA   P  2  189 ? -1.060  -207.361 -5.301  1.00 114.60 ? 188 ALA   P CB  1 
ATOM   28013 N  N   . ILE   P  2  190 ? -3.481  -208.379 -3.444  1.00 114.72 ? 189 ILE   P N   1 
ATOM   28014 C  CA  . ILE   P  2  190 ? -4.126  -208.734 -2.142  1.00 116.27 ? 189 ILE   P CA  1 
ATOM   28015 C  C   . ILE   P  2  190 ? -4.485  -210.224 -2.172  1.00 118.48 ? 189 ILE   P C   1 
ATOM   28016 O  O   . ILE   P  2  190 ? -4.172  -210.930 -1.193  1.00 119.72 ? 189 ILE   P O   1 
ATOM   28017 C  CB  . ILE   P  2  190 ? -5.358  -207.845 -1.863  1.00 119.15 ? 189 ILE   P CB  1 
ATOM   28018 C  CG1 . ILE   P  2  190 ? -4.942  -206.424 -1.471  1.00 119.05 ? 189 ILE   P CG1 1 
ATOM   28019 C  CG2 . ILE   P  2  190 ? -6.265  -208.476 -0.813  1.00 117.49 ? 189 ILE   P CG2 1 
ATOM   28020 C  CD1 . ILE   P  2  190 ? -6.073  -205.418 -1.463  1.00 122.24 ? 189 ILE   P CD1 1 
ATOM   28021 N  N   . GLU   P  2  191 ? -5.106  -210.674 -3.267  1.00 119.39 ? 190 GLU   P N   1 
ATOM   28022 C  CA  . GLU   P  2  191 ? -5.584  -212.069 -3.460  1.00 120.48 ? 190 GLU   P CA  1 
ATOM   28023 C  C   . GLU   P  2  191 ? -4.388  -213.027 -3.503  1.00 113.97 ? 190 GLU   P C   1 
ATOM   28024 O  O   . GLU   P  2  191 ? -4.442  -214.048 -2.794  1.00 112.59 ? 190 GLU   P O   1 
ATOM   28025 C  CB  . GLU   P  2  191 ? -6.418  -212.166 -4.738  1.00 125.20 ? 190 GLU   P CB  1 
ATOM   28026 C  CG  . GLU   P  2  191 ? -7.220  -213.448 -4.842  1.00 131.65 ? 190 GLU   P CG  1 
ATOM   28027 C  CD  . GLU   P  2  191 ? -8.231  -213.459 -5.977  1.00 137.81 ? 190 GLU   P CD  1 
ATOM   28028 O  OE1 . GLU   P  2  191 ? -8.964  -212.458 -6.126  1.00 141.79 ? 190 GLU   P OE1 1 
ATOM   28029 O  OE2 . GLU   P  2  191 ? -8.279  -214.464 -6.717  1.00 143.03 ? 190 GLU   P OE2 1 
ATOM   28030 N  N   . LEU   P  2  192 ? -3.356  -212.708 -4.297  1.00 109.48 ? 191 LEU   P N   1 
ATOM   28031 C  CA  . LEU   P  2  192 ? -2.132  -213.545 -4.466  1.00 108.96 ? 191 LEU   P CA  1 
ATOM   28032 C  C   . LEU   P  2  192 ? -1.475  -213.746 -3.093  1.00 111.01 ? 191 LEU   P C   1 
ATOM   28033 O  O   . LEU   P  2  192 ? -1.168  -214.905 -2.749  1.00 113.59 ? 191 LEU   P O   1 
ATOM   28034 C  CB  . LEU   P  2  192 ? -1.162  -212.870 -5.446  1.00 105.19 ? 191 LEU   P CB  1 
ATOM   28035 C  CG  . LEU   P  2  192 ? -0.296  -213.788 -6.318  1.00 105.12 ? 191 LEU   P CG  1 
ATOM   28036 C  CD1 . LEU   P  2  192 ? 0.996   -213.092 -6.716  1.00 103.12 ? 191 LEU   P CD1 1 
ATOM   28037 C  CD2 . LEU   P  2  192 ? 0.033   -215.111 -5.639  1.00 106.06 ? 191 LEU   P CD2 1 
ATOM   28038 N  N   . ALA   P  2  193 ? -1.281  -212.657 -2.342  1.00 110.08 ? 192 ALA   P N   1 
ATOM   28039 C  CA  . ALA   P  2  193 ? -0.661  -212.645 -0.996  1.00 112.36 ? 192 ALA   P CA  1 
ATOM   28040 C  C   . ALA   P  2  193 ? -1.386  -213.638 -0.081  1.00 114.94 ? 192 ALA   P C   1 
ATOM   28041 O  O   . ALA   P  2  193 ? -0.708  -214.515 0.489   1.00 118.05 ? 192 ALA   P O   1 
ATOM   28042 C  CB  . ALA   P  2  193 ? -0.697  -211.252 -0.419  1.00 111.26 ? 192 ALA   P CB  1 
ATOM   28043 N  N   . LEU   P  2  194 ? -2.712  -213.502 0.041   1.00 120.52 ? 193 LEU   P N   1 
ATOM   28044 C  CA  . LEU   P  2  194 ? -3.569  -214.340 0.927   1.00 124.79 ? 193 LEU   P CA  1 
ATOM   28045 C  C   . LEU   P  2  194 ? -3.567  -215.793 0.439   1.00 124.10 ? 193 LEU   P C   1 
ATOM   28046 O  O   . LEU   P  2  194 ? -3.511  -216.693 1.297   1.00 126.05 ? 193 LEU   P O   1 
ATOM   28047 C  CB  . LEU   P  2  194 ? -4.995  -213.779 0.958   1.00 131.49 ? 193 LEU   P CB  1 
ATOM   28048 C  CG  . LEU   P  2  194 ? -5.173  -212.446 1.683   1.00 137.22 ? 193 LEU   P CG  1 
ATOM   28049 C  CD1 . LEU   P  2  194 ? -6.560  -211.876 1.424   1.00 143.21 ? 193 LEU   P CD1 1 
ATOM   28050 C  CD2 . LEU   P  2  194 ? -4.929  -212.590 3.180   1.00 140.62 ? 193 LEU   P CD2 1 
ATOM   28051 N  N   . LYS   P  2  195 ? -3.634  -216.011 -0.879  1.00 123.47 ? 194 LYS   P N   1 
ATOM   28052 C  CA  . LYS   P  2  195 ? -3.651  -217.366 -1.498  1.00 124.56 ? 194 LYS   P CA  1 
ATOM   28053 C  C   . LYS   P  2  195 ? -2.332  -218.084 -1.197  1.00 122.32 ? 194 LYS   P C   1 
ATOM   28054 O  O   . LYS   P  2  195 ? -2.384  -219.297 -0.921  1.00 123.91 ? 194 LYS   P O   1 
ATOM   28055 C  CB  . LYS   P  2  195 ? -3.883  -217.298 -3.011  1.00 127.11 ? 194 LYS   P CB  1 
ATOM   28056 C  CG  . LYS   P  2  195 ? -5.338  -217.152 -3.440  1.00 130.74 ? 194 LYS   P CG  1 
ATOM   28057 C  CD  . LYS   P  2  195 ? -5.504  -216.900 -4.926  1.00 130.41 ? 194 LYS   P CD  1 
ATOM   28058 C  CE  . LYS   P  2  195 ? -5.407  -218.157 -5.764  1.00 129.93 ? 194 LYS   P CE  1 
ATOM   28059 N  NZ  . LYS   P  2  195 ? -6.692  -218.893 -5.788  1.00 132.22 ? 194 LYS   P NZ  1 
ATOM   28060 N  N   . THR   P  2  196 ? -1.201  -217.370 -1.250  1.00 117.64 ? 195 THR   P N   1 
ATOM   28061 C  CA  . THR   P  2  196 ? 0.159   -217.932 -1.014  1.00 114.63 ? 195 THR   P CA  1 
ATOM   28062 C  C   . THR   P  2  196 ? 0.293   -218.372 0.448   1.00 114.81 ? 195 THR   P C   1 
ATOM   28063 O  O   . THR   P  2  196 ? 0.689   -219.533 0.674   1.00 116.78 ? 195 THR   P O   1 
ATOM   28064 C  CB  . THR   P  2  196 ? 1.278   -216.941 -1.361  1.00 110.74 ? 195 THR   P CB  1 
ATOM   28065 O  OG1 . THR   P  2  196 ? 1.018   -216.364 -2.640  1.00 112.08 ? 195 THR   P OG1 1 
ATOM   28066 C  CG2 . THR   P  2  196 ? 2.639   -217.603 -1.372  1.00 108.05 ? 195 THR   P CG2 1 
ATOM   28067 N  N   . LEU   P  2  197 ? -0.013  -217.478 1.394   1.00 111.86 ? 196 LEU   P N   1 
ATOM   28068 C  CA  . LEU   P  2  197 ? 0.042   -217.754 2.857   1.00 111.88 ? 196 LEU   P CA  1 
ATOM   28069 C  C   . LEU   P  2  197 ? -0.831  -218.968 3.190   1.00 115.40 ? 196 LEU   P C   1 
ATOM   28070 O  O   . LEU   P  2  197 ? -0.387  -219.795 4.006   1.00 117.08 ? 196 LEU   P O   1 
ATOM   28071 C  CB  . LEU   P  2  197 ? -0.445  -216.530 3.639   1.00 111.27 ? 196 LEU   P CB  1 
ATOM   28072 C  CG  . LEU   P  2  197 ? 0.528   -215.356 3.732   1.00 109.31 ? 196 LEU   P CG  1 
ATOM   28073 C  CD1 . LEU   P  2  197 ? -0.152  -214.157 4.371   1.00 109.17 ? 196 LEU   P CD1 1 
ATOM   28074 C  CD2 . LEU   P  2  197 ? 1.781   -215.730 4.511   1.00 108.25 ? 196 LEU   P CD2 1 
ATOM   28075 N  N   . SER   P  2  198 ? -2.024  -219.048 2.589   1.00 119.11 ? 197 SER   P N   1 
ATOM   28076 C  CA  . SER   P  2  198 ? -3.023  -220.132 2.789   1.00 124.46 ? 197 SER   P CA  1 
ATOM   28077 C  C   . SER   P  2  198 ? -2.425  -221.498 2.428   1.00 123.85 ? 197 SER   P C   1 
ATOM   28078 O  O   . SER   P  2  198 ? -2.775  -222.485 3.104   1.00 123.84 ? 197 SER   P O   1 
ATOM   28079 C  CB  . SER   P  2  198 ? -4.283  -219.867 2.000   1.00 128.31 ? 197 SER   P CB  1 
ATOM   28080 O  OG  . SER   P  2  198 ? -5.320  -220.754 2.394   1.00 135.26 ? 197 SER   P OG  1 
ATOM   28081 N  N   . LYS   P  2  199 ? -1.569  -221.556 1.400   1.00 124.54 ? 198 LYS   P N   1 
ATOM   28082 C  CA  . LYS   P  2  199 ? -0.993  -222.819 0.860   1.00 125.72 ? 198 LYS   P CA  1 
ATOM   28083 C  C   . LYS   P  2  199 ? 0.312   -223.166 1.591   1.00 126.15 ? 198 LYS   P C   1 
ATOM   28084 O  O   . LYS   P  2  199 ? 0.611   -224.377 1.703   1.00 127.43 ? 198 LYS   P O   1 
ATOM   28085 C  CB  . LYS   P  2  199 ? -0.792  -222.703 -0.655  1.00 125.29 ? 198 LYS   P CB  1 
ATOM   28086 C  CG  . LYS   P  2  199 ? -2.082  -222.669 -1.464  1.00 124.89 ? 198 LYS   P CG  1 
ATOM   28087 C  CD  . LYS   P  2  199 ? -1.862  -222.578 -2.952  1.00 125.28 ? 198 LYS   P CD  1 
ATOM   28088 C  CE  . LYS   P  2  199 ? -1.162  -223.794 -3.514  1.00 127.50 ? 198 LYS   P CE  1 
ATOM   28089 N  NZ  . LYS   P  2  199 ? -1.059  -223.717 -4.988  1.00 129.48 ? 198 LYS   P NZ  1 
ATOM   28090 N  N   . THR   P  2  200 ? 1.050   -222.160 2.079   1.00 121.39 ? 199 THR   P N   1 
ATOM   28091 C  CA  . THR   P  2  200 ? 2.377   -222.323 2.739   1.00 122.18 ? 199 THR   P CA  1 
ATOM   28092 C  C   . THR   P  2  200 ? 2.258   -222.299 4.270   1.00 119.25 ? 199 THR   P C   1 
ATOM   28093 O  O   . THR   P  2  200 ? 3.287   -222.538 4.931   1.00 118.96 ? 199 THR   P O   1 
ATOM   28094 C  CB  . THR   P  2  200 ? 3.368   -221.229 2.323   1.00 121.23 ? 199 THR   P CB  1 
ATOM   28095 O  OG1 . THR   P  2  200 ? 2.817   -219.958 2.670   1.00 123.23 ? 199 THR   P OG1 1 
ATOM   28096 C  CG2 . THR   P  2  200 ? 3.710   -221.277 0.850   1.00 122.37 ? 199 THR   P CG2 1 
ATOM   28097 N  N   . THR   P  2  201 ? 1.078   -222.004 4.821   1.00 115.63 ? 200 THR   P N   1 
ATOM   28098 C  CA  . THR   P  2  201 ? 0.837   -221.966 6.291   1.00 117.98 ? 200 THR   P CA  1 
ATOM   28099 C  C   . THR   P  2  201 ? 1.107   -223.347 6.900   1.00 121.59 ? 200 THR   P C   1 
ATOM   28100 O  O   . THR   P  2  201 ? 0.834   -224.357 6.219   1.00 131.32 ? 200 THR   P O   1 
ATOM   28101 C  CB  . THR   P  2  201 ? -0.587  -221.508 6.632   1.00 113.98 ? 200 THR   P CB  1 
ATOM   28102 O  OG1 . THR   P  2  201 ? -0.693  -221.430 8.052   1.00 110.60 ? 200 THR   P OG1 1 
ATOM   28103 C  CG2 . THR   P  2  201 ? -1.666  -222.431 6.107   1.00 117.75 ? 200 THR   P CG2 1 
ATOM   28104 N  N   . ASP   P  2  202 ? 1.614   -223.380 8.137   1.00 121.52 ? 201 ASP   P N   1 
ATOM   28105 C  CA  . ASP   P  2  202 ? 1.797   -224.618 8.945   1.00 124.03 ? 201 ASP   P CA  1 
ATOM   28106 C  C   . ASP   P  2  202 ? 0.561   -224.843 9.827   1.00 123.89 ? 201 ASP   P C   1 
ATOM   28107 O  O   . ASP   P  2  202 ? 0.565   -225.819 10.598  1.00 129.49 ? 201 ASP   P O   1 
ATOM   28108 C  CB  . ASP   P  2  202 ? 3.069   -224.551 9.796   1.00 126.01 ? 201 ASP   P CB  1 
ATOM   28109 C  CG  . ASP   P  2  202 ? 4.363   -224.553 8.998   1.00 128.73 ? 201 ASP   P CG  1 
ATOM   28110 O  OD1 . ASP   P  2  202 ? 4.341   -225.010 7.839   1.00 133.71 ? 201 ASP   P OD1 1 
ATOM   28111 O  OD2 . ASP   P  2  202 ? 5.387   -224.095 9.544   1.00 129.01 ? 201 ASP   P OD2 1 
ATOM   28112 N  N   . SER   P  2  203 ? -0.450  -223.975 9.718   1.00 124.52 ? 202 SER   P N   1 
ATOM   28113 C  CA  . SER   P  2  203 ? -1.758  -224.090 10.416  1.00 131.00 ? 202 SER   P CA  1 
ATOM   28114 C  C   . SER   P  2  203 ? -2.719  -224.951 9.592   1.00 130.61 ? 202 SER   P C   1 
ATOM   28115 O  O   . SER   P  2  203 ? -2.424  -225.201 8.407   1.00 127.91 ? 202 SER   P O   1 
ATOM   28116 C  CB  . SER   P  2  203 ? -2.354  -222.736 10.670  1.00 134.16 ? 202 SER   P CB  1 
ATOM   28117 O  OG  . SER   P  2  203 ? -1.509  -221.961 11.504  1.00 141.86 ? 202 SER   P OG  1 
ATOM   28118 N  N   . SER   P  2  204 ? -3.835  -225.362 10.201  1.00 137.08 ? 203 SER   P N   1 
ATOM   28119 C  CA  . SER   P  2  204 ? -4.900  -226.183 9.565   1.00 140.90 ? 203 SER   P CA  1 
ATOM   28120 C  C   . SER   P  2  204 ? -5.629  -225.350 8.503   1.00 141.96 ? 203 SER   P C   1 
ATOM   28121 O  O   . SER   P  2  204 ? -5.774  -225.842 7.367   1.00 145.05 ? 203 SER   P O   1 
ATOM   28122 C  CB  . SER   P  2  204 ? -5.855  -226.736 10.593  1.00 143.19 ? 203 SER   P CB  1 
ATOM   28123 O  OG  . SER   P  2  204 ? -6.434  -225.694 11.364  1.00 143.82 ? 203 SER   P OG  1 
ATOM   28124 N  N   . ALA   P  2  205 ? -6.061  -224.136 8.860   1.00 141.35 ? 204 ALA   P N   1 
ATOM   28125 C  CA  . ALA   P  2  205 ? -6.766  -223.188 7.964   1.00 140.98 ? 204 ALA   P CA  1 
ATOM   28126 C  C   . ALA   P  2  205 ? -6.434  -221.744 8.357   1.00 139.46 ? 204 ALA   P C   1 
ATOM   28127 O  O   . ALA   P  2  205 ? -6.349  -221.457 9.566   1.00 140.92 ? 204 ALA   P O   1 
ATOM   28128 C  CB  . ALA   P  2  205 ? -8.252  -223.442 8.014   1.00 143.90 ? 204 ALA   P CB  1 
ATOM   28129 N  N   . LEU   P  2  206 ? -6.267  -220.873 7.359   1.00 138.10 ? 205 LEU   P N   1 
ATOM   28130 C  CA  . LEU   P  2  206 ? -5.931  -219.437 7.546   1.00 136.26 ? 205 LEU   P CA  1 
ATOM   28131 C  C   . LEU   P  2  206 ? -7.203  -218.686 7.959   1.00 133.90 ? 205 LEU   P C   1 
ATOM   28132 O  O   . LEU   P  2  206 ? -8.212  -218.794 7.232   1.00 132.03 ? 205 LEU   P O   1 
ATOM   28133 C  CB  . LEU   P  2  206 ? -5.347  -218.890 6.237   1.00 133.93 ? 205 LEU   P CB  1 
ATOM   28134 C  CG  . LEU   P  2  206 ? -4.380  -217.717 6.378   1.00 133.06 ? 205 LEU   P CG  1 
ATOM   28135 C  CD1 . LEU   P  2  206 ? -3.078  -218.153 7.036   1.00 131.70 ? 205 LEU   P CD1 1 
ATOM   28136 C  CD2 . LEU   P  2  206 ? -4.101  -217.088 5.021   1.00 133.52 ? 205 LEU   P CD2 1 
ATOM   28137 N  N   . THR   P  2  207 ? -7.159  -217.980 9.095   1.00 131.76 ? 206 THR   P N   1 
ATOM   28138 C  CA  . THR   P  2  207 ? -8.290  -217.189 9.657   1.00 132.12 ? 206 THR   P CA  1 
ATOM   28139 C  C   . THR   P  2  207 ? -7.830  -215.758 9.963   1.00 129.57 ? 206 THR   P C   1 
ATOM   28140 O  O   . THR   P  2  207 ? -6.604  -215.528 10.032  1.00 124.78 ? 206 THR   P O   1 
ATOM   28141 C  CB  . THR   P  2  207 ? -8.879  -217.863 10.902  1.00 133.46 ? 206 THR   P CB  1 
ATOM   28142 O  OG1 . THR   P  2  207 ? -7.812  -218.125 11.814  1.00 128.45 ? 206 THR   P OG1 1 
ATOM   28143 C  CG2 . THR   P  2  207 ? -9.615  -219.144 10.577  1.00 136.35 ? 206 THR   P CG2 1 
ATOM   28144 N  N   . TYR   P  2  208 ? -8.792  -214.847 10.153  1.00 129.85 ? 207 TYR   P N   1 
ATOM   28145 C  CA  . TYR   P  2  208 ? -8.592  -213.379 10.307  1.00 127.66 ? 207 TYR   P CA  1 
ATOM   28146 C  C   . TYR   P  2  208 ? -7.708  -213.074 11.524  1.00 123.97 ? 207 TYR   P C   1 
ATOM   28147 O  O   . TYR   P  2  208 ? -6.928  -212.104 11.461  1.00 118.58 ? 207 TYR   P O   1 
ATOM   28148 C  CB  . TYR   P  2  208 ? -9.940  -212.657 10.417  1.00 127.57 ? 207 TYR   P CB  1 
ATOM   28149 C  CG  . TYR   P  2  208 ? -10.651 -212.809 11.738  1.00 128.67 ? 207 TYR   P CG  1 
ATOM   28150 C  CD1 . TYR   P  2  208 ? -11.509 -213.872 11.973  1.00 131.48 ? 207 TYR   P CD1 1 
ATOM   28151 C  CD2 . TYR   P  2  208 ? -10.476 -211.882 12.754  1.00 125.77 ? 207 TYR   P CD2 1 
ATOM   28152 C  CE1 . TYR   P  2  208 ? -12.167 -214.016 13.184  1.00 133.37 ? 207 TYR   P CE1 1 
ATOM   28153 C  CE2 . TYR   P  2  208 ? -11.126 -212.011 13.970  1.00 128.21 ? 207 TYR   P CE2 1 
ATOM   28154 C  CZ  . TYR   P  2  208 ? -11.974 -213.082 14.186  1.00 132.92 ? 207 TYR   P CZ  1 
ATOM   28155 O  OH  . TYR   P  2  208 ? -12.616 -213.211 15.383  1.00 137.16 ? 207 TYR   P OH  1 
ATOM   28156 N  N   . ASP   P  2  209 ? -7.828  -213.871 12.591  1.00 125.78 ? 208 ASP   P N   1 
ATOM   28157 C  CA  . ASP   P  2  209 ? -7.171  -213.620 13.903  1.00 125.16 ? 208 ASP   P CA  1 
ATOM   28158 C  C   . ASP   P  2  209 ? -5.668  -213.929 13.834  1.00 125.04 ? 208 ASP   P C   1 
ATOM   28159 O  O   . ASP   P  2  209 ? -4.948  -213.434 14.722  1.00 119.16 ? 208 ASP   P O   1 
ATOM   28160 C  CB  . ASP   P  2  209 ? -7.849  -214.399 15.036  1.00 129.79 ? 208 ASP   P CB  1 
ATOM   28161 C  CG  . ASP   P  2  209 ? -7.851  -215.908 14.854  1.00 131.96 ? 208 ASP   P CG  1 
ATOM   28162 O  OD1 . ASP   P  2  209 ? -8.330  -216.372 13.799  1.00 134.40 ? 208 ASP   P OD1 1 
ATOM   28163 O  OD2 . ASP   P  2  209 ? -7.375  -216.608 15.772  1.00 132.87 ? 208 ASP   P OD2 1 
ATOM   28164 N  N   . ARG   P  2  210 ? -5.206  -214.704 12.842  1.00 128.06 ? 209 ARG   P N   1 
ATOM   28165 C  CA  . ARG   P  2  210 ? -3.777  -215.112 12.709  1.00 129.80 ? 209 ARG   P CA  1 
ATOM   28166 C  C   . ARG   P  2  210 ? -3.070  -214.274 11.631  1.00 125.03 ? 209 ARG   P C   1 
ATOM   28167 O  O   . ARG   P  2  210 ? -1.911  -214.608 11.310  1.00 120.41 ? 209 ARG   P O   1 
ATOM   28168 C  CB  . ARG   P  2  210 ? -3.652  -216.612 12.406  1.00 134.33 ? 209 ARG   P CB  1 
ATOM   28169 C  CG  . ARG   P  2  210 ? -2.477  -217.283 13.110  1.00 134.73 ? 209 ARG   P CG  1 
ATOM   28170 C  CD  . ARG   P  2  210 ? -1.985  -218.572 12.470  1.00 137.09 ? 209 ARG   P CD  1 
ATOM   28171 N  NE  . ARG   P  2  210 ? -3.032  -219.310 11.776  1.00 139.94 ? 209 ARG   P NE  1 
ATOM   28172 C  CZ  . ARG   P  2  210 ? -3.995  -220.017 12.364  1.00 145.79 ? 209 ARG   P CZ  1 
ATOM   28173 N  NH1 . ARG   P  2  210 ? -4.070  -220.095 13.684  1.00 150.49 ? 209 ARG   P NH1 1 
ATOM   28174 N  NH2 . ARG   P  2  210 ? -4.891  -220.646 11.623  1.00 149.73 ? 209 ARG   P NH2 1 
ATOM   28175 N  N   . LEU   P  2  211 ? -3.707  -213.216 11.111  1.00 122.56 ? 210 LEU   P N   1 
ATOM   28176 C  CA  . LEU   P  2  211 ? -3.149  -212.390 10.004  1.00 121.96 ? 210 LEU   P CA  1 
ATOM   28177 C  C   . LEU   P  2  211 ? -3.075  -210.916 10.402  1.00 121.99 ? 210 LEU   P C   1 
ATOM   28178 O  O   . LEU   P  2  211 ? -4.015  -210.422 11.055  1.00 125.86 ? 210 LEU   P O   1 
ATOM   28179 C  CB  . LEU   P  2  211 ? -4.022  -212.529 8.754   1.00 121.57 ? 210 LEU   P CB  1 
ATOM   28180 C  CG  . LEU   P  2  211 ? -3.883  -213.831 7.969   1.00 121.24 ? 210 LEU   P CG  1 
ATOM   28181 C  CD1 . LEU   P  2  211 ? -4.868  -213.851 6.813   1.00 120.93 ? 210 LEU   P CD1 1 
ATOM   28182 C  CD2 . LEU   P  2  211 ? -2.462  -214.025 7.455   1.00 121.87 ? 210 LEU   P CD2 1 
ATOM   28183 N  N   . GLU   P  2  212 ? -1.991  -210.255 9.984   1.00 123.70 ? 211 GLU   P N   1 
ATOM   28184 C  CA  . GLU   P  2  212 ? -1.875  -208.779 9.862   1.00 122.99 ? 211 GLU   P CA  1 
ATOM   28185 C  C   . GLU   P  2  212 ? -1.817  -208.449 8.371   1.00 119.09 ? 211 GLU   P C   1 
ATOM   28186 O  O   . GLU   P  2  212 ? -1.220  -209.239 7.613   1.00 115.71 ? 211 GLU   P O   1 
ATOM   28187 C  CB  . GLU   P  2  212 ? -0.629  -208.247 10.572  1.00 122.86 ? 211 GLU   P CB  1 
ATOM   28188 C  CG  . GLU   P  2  212 ? -0.643  -208.453 12.076  1.00 126.41 ? 211 GLU   P CG  1 
ATOM   28189 C  CD  . GLU   P  2  212 ? 0.358   -207.607 12.848  1.00 126.39 ? 211 GLU   P CD  1 
ATOM   28190 O  OE1 . GLU   P  2  212 ? 1.067   -208.168 13.706  1.00 127.83 ? 211 GLU   P OE1 1 
ATOM   28191 O  OE2 . GLU   P  2  212 ? 0.424   -206.386 12.596  1.00 130.24 ? 211 GLU   P OE2 1 
ATOM   28192 N  N   . PHE   P  2  213 ? -2.417  -207.329 7.973   1.00 120.09 ? 212 PHE   P N   1 
ATOM   28193 C  CA  . PHE   P  2  213 ? -2.570  -206.926 6.553   1.00 123.05 ? 212 PHE   P CA  1 
ATOM   28194 C  C   . PHE   P  2  213 ? -2.439  -205.402 6.443   1.00 123.92 ? 212 PHE   P C   1 
ATOM   28195 O  O   . PHE   P  2  213 ? -2.913  -204.686 7.352   1.00 122.31 ? 212 PHE   P O   1 
ATOM   28196 C  CB  . PHE   P  2  213 ? -3.904  -207.450 6.015   1.00 124.37 ? 212 PHE   P CB  1 
ATOM   28197 C  CG  . PHE   P  2  213 ? -3.863  -207.851 4.565   1.00 126.53 ? 212 PHE   P CG  1 
ATOM   28198 C  CD1 . PHE   P  2  213 ? -3.338  -209.076 4.184   1.00 124.60 ? 212 PHE   P CD1 1 
ATOM   28199 C  CD2 . PHE   P  2  213 ? -4.331  -206.993 3.582   1.00 129.26 ? 212 PHE   P CD2 1 
ATOM   28200 C  CE1 . PHE   P  2  213 ? -3.291  -209.439 2.848   1.00 126.02 ? 212 PHE   P CE1 1 
ATOM   28201 C  CE2 . PHE   P  2  213 ? -4.284  -207.358 2.246   1.00 131.60 ? 212 PHE   P CE2 1 
ATOM   28202 C  CZ  . PHE   P  2  213 ? -3.763  -208.579 1.882   1.00 129.54 ? 212 PHE   P CZ  1 
ATOM   28203 N  N   . ALA   P  2  214 ? -1.799  -204.922 5.373   1.00 122.61 ? 213 ALA   P N   1 
ATOM   28204 C  CA  . ALA   P  2  214 ? -1.633  -203.479 5.082   1.00 121.67 ? 213 ALA   P CA  1 
ATOM   28205 C  C   . ALA   P  2  214 ? -1.430  -203.243 3.583   1.00 121.17 ? 213 ALA   P C   1 
ATOM   28206 O  O   . ALA   P  2  214 ? -0.762  -204.070 2.933   1.00 124.72 ? 213 ALA   P O   1 
ATOM   28207 C  CB  . ALA   P  2  214 ? -0.480  -202.920 5.874   1.00 121.21 ? 213 ALA   P CB  1 
ATOM   28208 N  N   . THR   P  2  215 ? -1.983  -202.137 3.075   1.00 121.56 ? 214 THR   P N   1 
ATOM   28209 C  CA  . THR   P  2  215 ? -1.810  -201.648 1.681   1.00 120.47 ? 214 THR   P CA  1 
ATOM   28210 C  C   . THR   P  2  215 ? -1.242  -200.227 1.710   1.00 119.85 ? 214 THR   P C   1 
ATOM   28211 O  O   . THR   P  2  215 ? -1.635  -199.449 2.605   1.00 118.53 ? 214 THR   P O   1 
ATOM   28212 C  CB  . THR   P  2  215 ? -3.126  -201.680 0.894   1.00 123.68 ? 214 THR   P CB  1 
ATOM   28213 O  OG1 . THR   P  2  215 ? -4.111  -200.948 1.624   1.00 125.13 ? 214 THR   P OG1 1 
ATOM   28214 C  CG2 . THR   P  2  215 ? -3.621  -203.086 0.634   1.00 123.95 ? 214 THR   P CG2 1 
ATOM   28215 N  N   . ILE   P  2  216 ? -0.349  -199.918 0.768   1.00 116.88 ? 215 ILE   P N   1 
ATOM   28216 C  CA  . ILE   P  2  216 ? 0.153   -198.541 0.492   1.00 117.76 ? 215 ILE   P CA  1 
ATOM   28217 C  C   . ILE   P  2  216 ? -0.273  -198.173 -0.930  1.00 118.39 ? 215 ILE   P C   1 
ATOM   28218 O  O   . ILE   P  2  216 ? 0.425   -198.570 -1.882  1.00 116.46 ? 215 ILE   P O   1 
ATOM   28219 C  CB  . ILE   P  2  216 ? 1.676   -198.445 0.704   1.00 116.84 ? 215 ILE   P CB  1 
ATOM   28220 C  CG1 . ILE   P  2  216 ? 2.036   -198.747 2.161   1.00 119.07 ? 215 ILE   P CG1 1 
ATOM   28221 C  CG2 . ILE   P  2  216 ? 2.199   -197.087 0.256   1.00 116.26 ? 215 ILE   P CG2 1 
ATOM   28222 C  CD1 . ILE   P  2  216 ? 3.518   -198.792 2.448   1.00 120.27 ? 215 ILE   P CD1 1 
ATOM   28223 N  N   . ARG   P  2  217 ? -1.394  -197.458 -1.048  1.00 124.97 ? 216 ARG   P N   1 
ATOM   28224 C  CA  . ARG   P  2  217 ? -2.013  -197.051 -2.335  1.00 132.37 ? 216 ARG   P CA  1 
ATOM   28225 C  C   . ARG   P  2  217 ? -1.762  -195.559 -2.577  1.00 138.33 ? 216 ARG   P C   1 
ATOM   28226 O  O   . ARG   P  2  217 ? -1.403  -194.850 -1.613  1.00 137.24 ? 216 ARG   P O   1 
ATOM   28227 C  CB  . ARG   P  2  217 ? -3.525  -197.297 -2.306  1.00 133.56 ? 216 ARG   P CB  1 
ATOM   28228 C  CG  . ARG   P  2  217 ? -3.958  -198.754 -2.239  1.00 130.48 ? 216 ARG   P CG  1 
ATOM   28229 C  CD  . ARG   P  2  217 ? -5.455  -198.817 -1.989  1.00 130.71 ? 216 ARG   P CD  1 
ATOM   28230 N  NE  . ARG   P  2  217 ? -6.068  -200.080 -2.378  1.00 127.27 ? 216 ARG   P NE  1 
ATOM   28231 C  CZ  . ARG   P  2  217 ? -6.606  -200.340 -3.567  1.00 127.59 ? 216 ARG   P CZ  1 
ATOM   28232 N  NH1 . ARG   P  2  217 ? -6.612  -199.427 -4.526  1.00 127.48 ? 216 ARG   P NH1 1 
ATOM   28233 N  NH2 . ARG   P  2  217 ? -7.138  -201.528 -3.796  1.00 129.41 ? 216 ARG   P NH2 1 
ATOM   28234 N  N   . LYS   P  2  218 ? -1.957  -195.115 -3.823  1.00 146.43 ? 217 LYS   P N   1 
ATOM   28235 C  CA  . LYS   P  2  218 ? -2.242  -193.700 -4.189  1.00 150.35 ? 217 LYS   P CA  1 
ATOM   28236 C  C   . LYS   P  2  218 ? -3.766  -193.533 -4.261  1.00 157.42 ? 217 LYS   P C   1 
ATOM   28237 O  O   . LYS   P  2  218 ? -4.235  -192.618 -4.967  1.00 153.43 ? 217 LYS   P O   1 
ATOM   28238 C  CB  . LYS   P  2  218 ? -1.570  -193.337 -5.517  1.00 148.25 ? 217 LYS   P CB  1 
ATOM   28239 C  CG  . LYS   P  2  218 ? -1.343  -191.849 -5.745  1.00 146.37 ? 217 LYS   P CG  1 
ATOM   28240 C  CD  . LYS   P  2  218 ? -0.430  -191.559 -6.911  1.00 145.57 ? 217 LYS   P CD  1 
ATOM   28241 C  CE  . LYS   P  2  218 ? 1.032   -191.775 -6.583  1.00 141.50 ? 217 LYS   P CE  1 
ATOM   28242 N  NZ  . LYS   P  2  218 ? 1.872   -191.707 -7.801  1.00 140.02 ? 217 LYS   P NZ  1 
ATOM   28243 N  N   . GLY   P  2  219 ? -4.498  -194.380 -3.525  1.00 161.37 ? 218 GLY   P N   1 
ATOM   28244 C  CA  . GLY   P  2  219 ? -5.969  -194.475 -3.526  1.00 169.73 ? 218 GLY   P CA  1 
ATOM   28245 C  C   . GLY   P  2  219 ? -6.590  -193.495 -2.547  1.00 182.59 ? 218 GLY   P C   1 
ATOM   28246 O  O   . GLY   P  2  219 ? -7.760  -193.704 -2.167  1.00 191.51 ? 218 GLY   P O   1 
ATOM   28247 N  N   . ALA   P  2  220 ? -5.825  -192.477 -2.136  1.00 189.01 ? 219 ALA   P N   1 
ATOM   28248 C  CA  . ALA   P  2  220 ? -6.320  -191.234 -1.501  1.00 186.27 ? 219 ALA   P CA  1 
ATOM   28249 C  C   . ALA   P  2  220 ? -6.939  -190.352 -2.597  1.00 193.27 ? 219 ALA   P C   1 
ATOM   28250 O  O   . ALA   P  2  220 ? -7.370  -190.917 -3.626  1.00 170.30 ? 219 ALA   P O   1 
ATOM   28251 C  CB  . ALA   P  2  220 ? -5.190  -190.550 -0.767  1.00 183.64 ? 219 ALA   P CB  1 
ATOM   28252 N  N   . ASN   P  2  221 ? -6.993  -189.030 -2.397  1.00 186.46 ? 220 ASN   P N   1 
ATOM   28253 C  CA  . ASN   P  2  221 ? -7.607  -188.069 -3.354  1.00 185.12 ? 220 ASN   P CA  1 
ATOM   28254 C  C   . ASN   P  2  221 ? -6.507  -187.229 -4.020  1.00 178.16 ? 220 ASN   P C   1 
ATOM   28255 O  O   . ASN   P  2  221 ? -6.110  -186.199 -3.437  1.00 174.19 ? 220 ASN   P O   1 
ATOM   28256 C  CB  . ASN   P  2  221 ? -8.679  -187.215 -2.672  1.00 183.45 ? 220 ASN   P CB  1 
ATOM   28257 C  CG  . ASN   P  2  221 ? -9.844  -188.041 -2.164  1.00 180.72 ? 220 ASN   P CG  1 
ATOM   28258 O  OD1 . ASN   P  2  221 ? -9.647  -189.066 -1.514  1.00 175.74 ? 220 ASN   P OD1 1 
ATOM   28259 N  ND2 . ASN   P  2  221 ? -11.062 -187.612 -2.453  1.00 181.18 ? 220 ASN   P ND2 1 
ATOM   28260 N  N   . ASP   P  2  222 ? -6.040  -187.679 -5.193  1.00 175.67 ? 221 ASP   P N   1 
ATOM   28261 C  CA  . ASP   P  2  222 ? -5.151  -186.952 -6.143  1.00 170.36 ? 221 ASP   P CA  1 
ATOM   28262 C  C   . ASP   P  2  222 ? -3.701  -186.929 -5.640  1.00 170.03 ? 221 ASP   P C   1 
ATOM   28263 O  O   . ASP   P  2  222 ? -3.433  -186.256 -4.626  1.00 176.12 ? 221 ASP   P O   1 
ATOM   28264 C  CB  . ASP   P  2  222 ? -5.657  -185.534 -6.431  1.00 168.43 ? 221 ASP   P CB  1 
ATOM   28265 C  CG  . ASP   P  2  222 ? -6.605  -185.453 -7.616  1.00 167.21 ? 221 ASP   P CG  1 
ATOM   28266 O  OD1 . ASP   P  2  222 ? -7.433  -186.374 -7.772  1.00 163.36 ? 221 ASP   P OD1 1 
ATOM   28267 O  OD2 . ASP   P  2  222 ? -6.504  -184.472 -8.378  1.00 164.76 ? 221 ASP   P OD2 1 
ATOM   28268 N  N   . GLY   P  2  223 ? -2.817  -187.650 -6.342  1.00 167.78 ? 222 GLY   P N   1 
ATOM   28269 C  CA  . GLY   P  2  223 ? -1.346  -187.511 -6.308  1.00 168.91 ? 222 GLY   P CA  1 
ATOM   28270 C  C   . GLY   P  2  223 ? -0.746  -187.550 -4.911  1.00 167.84 ? 222 GLY   P C   1 
ATOM   28271 O  O   . GLY   P  2  223 ? 0.317   -186.925 -4.727  1.00 174.71 ? 222 GLY   P O   1 
ATOM   28272 N  N   . GLU   P  2  224 ? -1.373  -188.258 -3.964  1.00 170.43 ? 223 GLU   P N   1 
ATOM   28273 C  CA  . GLU   P  2  224 ? -0.853  -188.432 -2.578  1.00 166.39 ? 223 GLU   P CA  1 
ATOM   28274 C  C   . GLU   P  2  224 ? -1.114  -189.870 -2.113  1.00 161.18 ? 223 GLU   P C   1 
ATOM   28275 O  O   . GLU   P  2  224 ? -2.072  -190.501 -2.610  1.00 162.58 ? 223 GLU   P O   1 
ATOM   28276 C  CB  . GLU   P  2  224 ? -1.460  -187.389 -1.635  1.00 167.12 ? 223 GLU   P CB  1 
ATOM   28277 C  CG  . GLU   P  2  224 ? -2.914  -187.644 -1.277  1.00 168.38 ? 223 GLU   P CG  1 
ATOM   28278 C  CD  . GLU   P  2  224 ? -3.655  -186.431 -0.737  1.00 167.78 ? 223 GLU   P CD  1 
ATOM   28279 O  OE1 . GLU   P  2  224 ? -2.988  -185.454 -0.341  1.00 167.30 ? 223 GLU   P OE1 1 
ATOM   28280 O  OE2 . GLU   P  2  224 ? -4.901  -186.468 -0.713  1.00 172.10 ? 223 GLU   P OE2 1 
ATOM   28281 N  N   . VAL   P  2  225 ? -0.286  -190.351 -1.183  1.00 148.70 ? 224 VAL   P N   1 
ATOM   28282 C  CA  . VAL   P  2  225 ? -0.199  -191.783 -0.777  1.00 138.43 ? 224 VAL   P CA  1 
ATOM   28283 C  C   . VAL   P  2  225 ? -0.857  -191.958 0.593   1.00 134.89 ? 224 VAL   P C   1 
ATOM   28284 O  O   . VAL   P  2  225 ? -0.631  -191.107 1.473   1.00 133.37 ? 224 VAL   P O   1 
ATOM   28285 C  CB  . VAL   P  2  225 ? 1.267   -192.256 -0.783  1.00 137.54 ? 224 VAL   P CB  1 
ATOM   28286 C  CG1 . VAL   P  2  225 ? 1.476   -193.520 0.038   1.00 139.68 ? 224 VAL   P CG1 1 
ATOM   28287 C  CG2 . VAL   P  2  225 ? 1.765   -192.450 -2.205  1.00 134.06 ? 224 VAL   P CG2 1 
ATOM   28288 N  N   . TYR   P  2  226 ? -1.628  -193.038 0.751   1.00 134.73 ? 225 TYR   P N   1 
ATOM   28289 C  CA  . TYR   P  2  226 ? -2.347  -193.410 1.996   1.00 135.86 ? 225 TYR   P CA  1 
ATOM   28290 C  C   . TYR   P  2  226 ? -1.855  -194.785 2.465   1.00 129.20 ? 225 TYR   P C   1 
ATOM   28291 O  O   . TYR   P  2  226 ? -1.745  -195.707 1.633   1.00 130.00 ? 225 TYR   P O   1 
ATOM   28292 C  CB  . TYR   P  2  226 ? -3.859  -193.372 1.758   1.00 142.48 ? 225 TYR   P CB  1 
ATOM   28293 C  CG  . TYR   P  2  226 ? -4.702  -193.769 2.944   1.00 151.73 ? 225 TYR   P CG  1 
ATOM   28294 C  CD1 . TYR   P  2  226 ? -4.557  -193.136 4.169   1.00 151.96 ? 225 TYR   P CD1 1 
ATOM   28295 C  CD2 . TYR   P  2  226 ? -5.658  -194.768 2.841   1.00 152.37 ? 225 TYR   P CD2 1 
ATOM   28296 C  CE1 . TYR   P  2  226 ? -5.329  -193.493 5.263   1.00 156.86 ? 225 TYR   P CE1 1 
ATOM   28297 C  CE2 . TYR   P  2  226 ? -6.439  -195.136 3.925   1.00 156.50 ? 225 TYR   P CE2 1 
ATOM   28298 C  CZ  . TYR   P  2  226 ? -6.274  -194.496 5.140   1.00 156.40 ? 225 TYR   P CZ  1 
ATOM   28299 O  OH  . TYR   P  2  226 ? -7.040  -194.852 6.212   1.00 162.96 ? 225 TYR   P OH  1 
ATOM   28300 N  N   . GLN   P  2  227 ? -1.543  -194.897 3.760   1.00 124.95 ? 226 GLN   P N   1 
ATOM   28301 C  CA  . GLN   P  2  227 ? -1.186  -196.164 4.450   1.00 124.26 ? 226 GLN   P CA  1 
ATOM   28302 C  C   . GLN   P  2  227 ? -2.421  -196.701 5.171   1.00 124.87 ? 226 GLN   P C   1 
ATOM   28303 O  O   . GLN   P  2  227 ? -2.971  -195.967 6.017   1.00 130.07 ? 226 GLN   P O   1 
ATOM   28304 C  CB  . GLN   P  2  227 ? -0.075  -195.936 5.473   1.00 121.74 ? 226 GLN   P CB  1 
ATOM   28305 C  CG  . GLN   P  2  227 ? 1.321   -196.115 4.906   1.00 117.72 ? 226 GLN   P CG  1 
ATOM   28306 C  CD  . GLN   P  2  227 ? 2.359   -195.840 5.963   1.00 117.18 ? 226 GLN   P CD  1 
ATOM   28307 O  OE1 . GLN   P  2  227 ? 2.201   -194.947 6.791   1.00 116.63 ? 226 GLN   P OE1 1 
ATOM   28308 N  NE2 . GLN   P  2  227 ? 3.428   -196.619 5.951   1.00 115.64 ? 226 GLN   P NE2 1 
ATOM   28309 N  N   . LYS   P  2  228 ? -2.822  -197.933 4.857   1.00 123.07 ? 227 LYS   P N   1 
ATOM   28310 C  CA  . LYS   P  2  228 ? -3.984  -198.615 5.479   1.00 124.41 ? 227 LYS   P CA  1 
ATOM   28311 C  C   . LYS   P  2  228 ? -3.468  -199.854 6.216   1.00 126.09 ? 227 LYS   P C   1 
ATOM   28312 O  O   . LYS   P  2  228 ? -3.099  -200.827 5.537   1.00 133.65 ? 227 LYS   P O   1 
ATOM   28313 C  CB  . LYS   P  2  228 ? -5.022  -198.957 4.404   1.00 123.49 ? 227 LYS   P CB  1 
ATOM   28314 C  CG  . LYS   P  2  228 ? -6.439  -199.189 4.910   1.00 127.53 ? 227 LYS   P CG  1 
ATOM   28315 C  CD  . LYS   P  2  228 ? -7.403  -199.608 3.816   1.00 129.88 ? 227 LYS   P CD  1 
ATOM   28316 C  CE  . LYS   P  2  228 ? -8.854  -199.324 4.145   1.00 133.40 ? 227 LYS   P CE  1 
ATOM   28317 N  NZ  . LYS   P  2  228 ? -9.338  -200.159 5.269   1.00 135.74 ? 227 LYS   P NZ  1 
ATOM   28318 N  N   . ILE   P  2  229 ? -3.400  -199.793 7.549   1.00 125.88 ? 228 ILE   P N   1 
ATOM   28319 C  CA  . ILE   P  2  229 ? -3.164  -200.975 8.432   1.00 125.76 ? 228 ILE   P CA  1 
ATOM   28320 C  C   . ILE   P  2  229 ? -4.537  -201.578 8.747   1.00 125.63 ? 228 ILE   P C   1 
ATOM   28321 O  O   . ILE   P  2  229 ? -5.297  -200.941 9.503   1.00 135.31 ? 228 ILE   P O   1 
ATOM   28322 C  CB  . ILE   P  2  229 ? -2.393  -200.596 9.715   1.00 124.53 ? 228 ILE   P CB  1 
ATOM   28323 C  CG1 . ILE   P  2  229 ? -1.179  -199.702 9.434   1.00 123.23 ? 228 ILE   P CG1 1 
ATOM   28324 C  CG2 . ILE   P  2  229 ? -2.005  -201.848 10.489  1.00 124.09 ? 228 ILE   P CG2 1 
ATOM   28325 C  CD1 . ILE   P  2  229 ? -0.102  -200.347 8.587   1.00 121.00 ? 228 ILE   P CD1 1 
ATOM   28326 N  N   . PHE   P  2  230 ? -4.846  -202.746 8.179   1.00 121.78 ? 229 PHE   P N   1 
ATOM   28327 C  CA  . PHE   P  2  230 ? -6.204  -203.352 8.185   1.00 122.72 ? 229 PHE   P CA  1 
ATOM   28328 C  C   . PHE   P  2  230 ? -6.621  -203.695 9.619   1.00 121.69 ? 229 PHE   P C   1 
ATOM   28329 O  O   . PHE   P  2  230 ? -5.800  -204.263 10.365  1.00 117.63 ? 229 PHE   P O   1 
ATOM   28330 C  CB  . PHE   P  2  230 ? -6.253  -204.598 7.299   1.00 121.21 ? 229 PHE   P CB  1 
ATOM   28331 C  CG  . PHE   P  2  230 ? -6.427  -204.316 5.828   1.00 120.62 ? 229 PHE   P CG  1 
ATOM   28332 C  CD1 . PHE   P  2  230 ? -5.490  -203.568 5.133   1.00 116.51 ? 229 PHE   P CD1 1 
ATOM   28333 C  CD2 . PHE   P  2  230 ? -7.526  -204.804 5.138   1.00 122.08 ? 229 PHE   P CD2 1 
ATOM   28334 C  CE1 . PHE   P  2  230 ? -5.650  -203.313 3.780   1.00 116.58 ? 229 PHE   P CE1 1 
ATOM   28335 C  CE2 . PHE   P  2  230 ? -7.684  -204.549 3.785   1.00 121.23 ? 229 PHE   P CE2 1 
ATOM   28336 C  CZ  . PHE   P  2  230 ? -6.746  -203.804 3.108   1.00 119.88 ? 229 PHE   P CZ  1 
ATOM   28337 N  N   . LYS   P  2  231 ? -7.863  -203.354 9.977   1.00 126.84 ? 230 LYS   P N   1 
ATOM   28338 C  CA  . LYS   P  2  231 ? -8.512  -203.734 11.260  1.00 133.76 ? 230 LYS   P CA  1 
ATOM   28339 C  C   . LYS   P  2  231 ? -8.943  -205.196 11.174  1.00 137.40 ? 230 LYS   P C   1 
ATOM   28340 O  O   . LYS   P  2  231 ? -9.152  -205.713 10.077  1.00 135.43 ? 230 LYS   P O   1 
ATOM   28341 C  CB  . LYS   P  2  231 ? -9.720  -202.838 11.548  1.00 136.20 ? 230 LYS   P CB  1 
ATOM   28342 C  CG  . LYS   P  2  231 ? -9.422  -201.348 11.655  1.00 135.75 ? 230 LYS   P CG  1 
ATOM   28343 C  CD  . LYS   P  2  231 ? -10.666 -200.502 11.837  1.00 137.84 ? 230 LYS   P CD  1 
ATOM   28344 C  CE  . LYS   P  2  231 ? -10.406 -199.013 11.730  1.00 136.40 ? 230 LYS   P CE  1 
ATOM   28345 N  NZ  . LYS   P  2  231 ? -9.605  -198.507 12.871  1.00 135.81 ? 230 LYS   P NZ  1 
ATOM   28346 N  N   . PRO   P  2  232 ? -9.086  -205.904 12.319  1.00 143.56 ? 231 PRO   P N   1 
ATOM   28347 C  CA  . PRO   P  2  232 ? -9.515  -207.306 12.321  1.00 145.60 ? 231 PRO   P CA  1 
ATOM   28348 C  C   . PRO   P  2  232 ? -10.712 -207.620 11.408  1.00 149.56 ? 231 PRO   P C   1 
ATOM   28349 O  O   . PRO   P  2  232 ? -10.640 -208.585 10.667  1.00 150.23 ? 231 PRO   P O   1 
ATOM   28350 C  CB  . PRO   P  2  232 ? -9.907  -207.532 13.788  1.00 148.68 ? 231 PRO   P CB  1 
ATOM   28351 C  CG  . PRO   P  2  232 ? -8.970  -206.626 14.555  1.00 145.07 ? 231 PRO   P CG  1 
ATOM   28352 C  CD  . PRO   P  2  232 ? -8.812  -205.402 13.676  1.00 142.60 ? 231 PRO   P CD  1 
ATOM   28353 N  N   . GLN   P  2  233 ? -11.771 -206.806 11.489  1.00 150.57 ? 232 GLN   P N   1 
ATOM   28354 C  CA  . GLN   P  2  233 ? -13.040 -206.983 10.729  1.00 151.41 ? 232 GLN   P CA  1 
ATOM   28355 C  C   . GLN   P  2  233 ? -12.785 -206.801 9.226   1.00 153.97 ? 232 GLN   P C   1 
ATOM   28356 O  O   . GLN   P  2  233 ? -13.496 -207.445 8.429   1.00 158.77 ? 232 GLN   P O   1 
ATOM   28357 C  CB  . GLN   P  2  233 ? -14.099 -205.996 11.228  1.00 153.64 ? 232 GLN   P CB  1 
ATOM   28358 C  CG  . GLN   P  2  233 ? -15.426 -206.071 10.481  1.00 157.39 ? 232 GLN   P CG  1 
ATOM   28359 C  CD  . GLN   P  2  233 ? -16.055 -207.444 10.510  1.00 157.86 ? 232 GLN   P CD  1 
ATOM   28360 O  OE1 . GLN   P  2  233 ? -16.327 -208.042 9.471   1.00 163.92 ? 232 GLN   P OE1 1 
ATOM   28361 N  NE2 . GLN   P  2  233 ? -16.293 -207.960 11.706  1.00 159.52 ? 232 GLN   P NE2 1 
ATOM   28362 N  N   . GLU   P  2  234 ? -11.820 -205.954 8.856   1.00 150.43 ? 233 GLU   P N   1 
ATOM   28363 C  CA  . GLU   P  2  234 ? -11.461 -205.668 7.440   1.00 150.66 ? 233 GLU   P CA  1 
ATOM   28364 C  C   . GLU   P  2  234 ? -10.710 -206.867 6.846   1.00 151.84 ? 233 GLU   P C   1 
ATOM   28365 O  O   . GLU   P  2  234 ? -10.891 -207.130 5.640   1.00 156.87 ? 233 GLU   P O   1 
ATOM   28366 C  CB  . GLU   P  2  234 ? -10.634 -204.386 7.343   1.00 151.22 ? 233 GLU   P CB  1 
ATOM   28367 C  CG  . GLU   P  2  234 ? -11.357 -203.166 7.887   1.00 153.08 ? 233 GLU   P CG  1 
ATOM   28368 C  CD  . GLU   P  2  234 ? -10.587 -201.862 7.777   1.00 155.42 ? 233 GLU   P CD  1 
ATOM   28369 O  OE1 . GLU   P  2  234 ? -9.360  -201.878 7.996   1.00 156.27 ? 233 GLU   P OE1 1 
ATOM   28370 O  OE2 . GLU   P  2  234 ? -11.220 -200.831 7.475   1.00 157.99 ? 233 GLU   P OE2 1 
ATOM   28371 N  N   . ILE   P  2  235 ? -9.907  -207.565 7.659   1.00 146.40 ? 234 ILE   P N   1 
ATOM   28372 C  CA  . ILE   P  2  235 ? -9.188  -208.812 7.256   1.00 143.63 ? 234 ILE   P CA  1 
ATOM   28373 C  C   . ILE   P  2  235 ? -10.226 -209.932 7.121   1.00 139.92 ? 234 ILE   P C   1 
ATOM   28374 O  O   . ILE   P  2  235 ? -10.122 -210.707 6.157   1.00 140.08 ? 234 ILE   P O   1 
ATOM   28375 C  CB  . ILE   P  2  235 ? -8.061  -209.181 8.245   1.00 141.61 ? 234 ILE   P CB  1 
ATOM   28376 C  CG1 . ILE   P  2  235 ? -7.042  -208.048 8.396   1.00 144.15 ? 234 ILE   P CG1 1 
ATOM   28377 C  CG2 . ILE   P  2  235 ? -7.383  -210.481 7.831   1.00 141.43 ? 234 ILE   P CG2 1 
ATOM   28378 C  CD1 . ILE   P  2  235 ? -6.122  -208.194 9.589   1.00 144.05 ? 234 ILE   P CD1 1 
ATOM   28379 N  N   . LYS   P  2  236 ? -11.186 -210.002 8.051   1.00 138.79 ? 235 LYS   P N   1 
ATOM   28380 C  CA  . LYS   P  2  236 ? -12.298 -210.992 8.036   1.00 143.76 ? 235 LYS   P CA  1 
ATOM   28381 C  C   . LYS   P  2  236 ? -13.085 -210.847 6.725   1.00 149.52 ? 235 LYS   P C   1 
ATOM   28382 O  O   . LYS   P  2  236 ? -13.431 -211.888 6.129   1.00 152.45 ? 235 LYS   P O   1 
ATOM   28383 C  CB  . LYS   P  2  236 ? -13.208 -210.807 9.257   1.00 146.70 ? 235 LYS   P CB  1 
ATOM   28384 C  CG  . LYS   P  2  236 ? -14.234 -211.912 9.479   1.00 149.67 ? 235 LYS   P CG  1 
ATOM   28385 C  CD  . LYS   P  2  236 ? -15.385 -211.503 10.376  1.00 152.43 ? 235 LYS   P CD  1 
ATOM   28386 C  CE  . LYS   P  2  236 ? -16.450 -212.572 10.505  1.00 154.82 ? 235 LYS   P CE  1 
ATOM   28387 N  NZ  . LYS   P  2  236 ? -16.033 -213.660 11.421  1.00 155.49 ? 235 LYS   P NZ  1 
ATOM   28388 N  N   . ASP   P  2  237 ? -13.341 -209.608 6.291   1.00 148.05 ? 236 ASP   P N   1 
ATOM   28389 C  CA  . ASP   P  2  237 ? -14.131 -209.288 5.069   1.00 149.72 ? 236 ASP   P CA  1 
ATOM   28390 C  C   . ASP   P  2  237 ? -13.327 -209.639 3.811   1.00 147.25 ? 236 ASP   P C   1 
ATOM   28391 O  O   . ASP   P  2  237 ? -13.919 -210.249 2.899   1.00 147.66 ? 236 ASP   P O   1 
ATOM   28392 C  CB  . ASP   P  2  237 ? -14.564 -207.820 5.047   1.00 151.17 ? 236 ASP   P CB  1 
ATOM   28393 C  CG  . ASP   P  2  237 ? -15.646 -207.477 6.058   1.00 153.85 ? 236 ASP   P CG  1 
ATOM   28394 O  OD1 . ASP   P  2  237 ? -16.395 -208.392 6.454   1.00 152.76 ? 236 ASP   P OD1 1 
ATOM   28395 O  OD2 . ASP   P  2  237 ? -15.731 -206.293 6.440   1.00 157.49 ? 236 ASP   P OD2 1 
ATOM   28396 N  N   . ILE   P  2  238 ? -12.042 -209.268 3.758   1.00 148.34 ? 237 ILE   P N   1 
ATOM   28397 C  CA  . ILE   P  2  238 ? -11.156 -209.485 2.572   1.00 146.84 ? 237 ILE   P CA  1 
ATOM   28398 C  C   . ILE   P  2  238 ? -10.877 -210.987 2.413   1.00 142.78 ? 237 ILE   P C   1 
ATOM   28399 O  O   . ILE   P  2  238 ? -10.590 -211.411 1.275   1.00 140.70 ? 237 ILE   P O   1 
ATOM   28400 C  CB  . ILE   P  2  238 ? -9.852  -208.659 2.668   1.00 147.37 ? 237 ILE   P CB  1 
ATOM   28401 C  CG1 . ILE   P  2  238 ? -9.271  -208.355 1.283   1.00 150.03 ? 237 ILE   P CG1 1 
ATOM   28402 C  CG2 . ILE   P  2  238 ? -8.823  -209.325 3.570   1.00 147.25 ? 237 ILE   P CG2 1 
ATOM   28403 C  CD1 . ILE   P  2  238 ? -9.863  -207.132 0.623   1.00 149.66 ? 237 ILE   P CD1 1 
ATOM   28404 N  N   . LEU   P  2  239 ? -10.950 -211.754 3.508   1.00 140.16 ? 238 LEU   P N   1 
ATOM   28405 C  CA  . LEU   P  2  239 ? -10.726 -213.227 3.520   1.00 139.85 ? 238 LEU   P CA  1 
ATOM   28406 C  C   . LEU   P  2  239 ? -11.967 -213.930 2.951   1.00 140.48 ? 238 LEU   P C   1 
ATOM   28407 O  O   . LEU   P  2  239 ? -11.796 -214.974 2.293   1.00 138.58 ? 238 LEU   P O   1 
ATOM   28408 C  CB  . LEU   P  2  239 ? -10.418 -213.683 4.953   1.00 140.18 ? 238 LEU   P CB  1 
ATOM   28409 C  CG  . LEU   P  2  239 ? -9.347  -214.763 5.114   1.00 141.31 ? 238 LEU   P CG  1 
ATOM   28410 C  CD1 . LEU   P  2  239 ? -8.023  -214.348 4.483   1.00 137.47 ? 238 LEU   P CD1 1 
ATOM   28411 C  CD2 . LEU   P  2  239 ? -9.140  -215.091 6.587   1.00 141.94 ? 238 LEU   P CD2 1 
ATOM   28412 N  N   . VAL   P  2  240 ? -13.160 -213.372 3.192   1.00 141.71 ? 239 VAL   P N   1 
ATOM   28413 C  CA  . VAL   P  2  240 ? -14.460 -213.860 2.633   1.00 143.08 ? 239 VAL   P CA  1 
ATOM   28414 C  C   . VAL   P  2  240 ? -14.563 -213.451 1.158   1.00 147.55 ? 239 VAL   P C   1 
ATOM   28415 O  O   . VAL   P  2  240 ? -15.013 -214.286 0.349   1.00 147.86 ? 239 VAL   P O   1 
ATOM   28416 C  CB  . VAL   P  2  240 ? -15.664 -213.333 3.439   1.00 142.93 ? 239 VAL   P CB  1 
ATOM   28417 C  CG1 . VAL   P  2  240 ? -16.975 -213.478 2.676   1.00 143.24 ? 239 VAL   P CG1 1 
ATOM   28418 C  CG2 . VAL   P  2  240 ? -15.765 -214.007 4.797   1.00 142.21 ? 239 VAL   P CG2 1 
ATOM   28419 N  N   . LYS   P  2  241 ? -14.175 -212.213 0.831   1.00 151.55 ? 240 LYS   P N   1 
ATOM   28420 C  CA  . LYS   P  2  241 ? -14.299 -211.622 -0.530  1.00 156.83 ? 240 LYS   P CA  1 
ATOM   28421 C  C   . LYS   P  2  241 ? -13.531 -212.484 -1.543  1.00 156.29 ? 240 LYS   P C   1 
ATOM   28422 O  O   . LYS   P  2  241 ? -14.035 -212.632 -2.674  1.00 156.75 ? 240 LYS   P O   1 
ATOM   28423 C  CB  . LYS   P  2  241 ? -13.812 -210.167 -0.537  1.00 159.07 ? 240 LYS   P CB  1 
ATOM   28424 C  CG  . LYS   P  2  241 ? -14.332 -209.318 -1.692  1.00 163.09 ? 240 LYS   P CG  1 
ATOM   28425 C  CD  . LYS   P  2  241 ? -14.174 -207.823 -1.479  1.00 163.40 ? 240 LYS   P CD  1 
ATOM   28426 C  CE  . LYS   P  2  241 ? -12.742 -207.341 -1.595  1.00 163.29 ? 240 LYS   P CE  1 
ATOM   28427 N  NZ  . LYS   P  2  241 ? -12.281 -207.310 -3.004  1.00 163.33 ? 240 LYS   P NZ  1 
ATOM   28428 N  N   . THR   P  2  242 ? -12.375 -213.039 -1.154  1.00 154.46 ? 241 THR   P N   1 
ATOM   28429 C  CA  . THR   P  2  242 ? -11.517 -213.907 -2.013  1.00 155.58 ? 241 THR   P CA  1 
ATOM   28430 C  C   . THR   P  2  242 ? -11.875 -215.387 -1.805  1.00 156.59 ? 241 THR   P C   1 
ATOM   28431 O  O   . THR   P  2  242 ? -11.264 -216.233 -2.486  1.00 163.12 ? 241 THR   P O   1 
ATOM   28432 C  CB  . THR   P  2  242 ? -10.025 -213.641 -1.769  1.00 154.65 ? 241 THR   P CB  1 
ATOM   28433 O  OG1 . THR   P  2  242 ? -9.732  -213.908 -0.397  1.00 155.44 ? 241 THR   P OG1 1 
ATOM   28434 C  CG2 . THR   P  2  242 ? -9.619  -212.226 -2.119  1.00 153.25 ? 241 THR   P CG2 1 
ATOM   28435 N  N   . GLY   P  2  243 ? -12.818 -215.685 -0.903  1.00 155.84 ? 242 GLY   P N   1 
ATOM   28436 C  CA  . GLY   P  2  243 ? -13.432 -217.018 -0.736  1.00 156.68 ? 242 GLY   P CA  1 
ATOM   28437 C  C   . GLY   P  2  243 ? -12.491 -218.038 -0.112  1.00 155.40 ? 242 GLY   P C   1 
ATOM   28438 O  O   . GLY   P  2  243 ? -12.614 -219.228 -0.468  1.00 148.90 ? 242 GLY   P O   1 
ATOM   28439 N  N   . ILE   P  2  244 ? -11.593 -217.603 0.783   1.00 159.52 ? 243 ILE   P N   1 
ATOM   28440 C  CA  . ILE   P  2  244 ? -10.690 -218.495 1.577   1.00 156.26 ? 243 ILE   P CA  1 
ATOM   28441 C  C   . ILE   P  2  244 ? -11.470 -219.040 2.785   1.00 161.72 ? 243 ILE   P C   1 
ATOM   28442 O  O   . ILE   P  2  244 ? -11.166 -220.176 3.210   1.00 162.39 ? 243 ILE   P O   1 
ATOM   28443 C  CB  . ILE   P  2  244 ? -9.382  -217.772 1.978   1.00 152.27 ? 243 ILE   P CB  1 
ATOM   28444 C  CG1 . ILE   P  2  244 ? -8.501  -217.507 0.752   1.00 146.71 ? 243 ILE   P CG1 1 
ATOM   28445 C  CG2 . ILE   P  2  244 ? -8.626  -218.553 3.048   1.00 147.24 ? 243 ILE   P CG2 1 
ATOM   28446 C  CD1 . ILE   P  2  244 ? -7.287  -216.647 1.018   1.00 144.00 ? 243 ILE   P CD1 1 
ATOM   28447 N  N   . THR   P  2  245 ? -12.438 -218.275 3.309   1.00 162.49 ? 244 THR   P N   1 
ATOM   28448 C  CA  . THR   P  2  245 ? -13.363 -218.697 4.400   1.00 155.97 ? 244 THR   P CA  1 
ATOM   28449 C  C   . THR   P  2  245 ? -14.810 -218.345 4.030   1.00 158.76 ? 244 THR   P C   1 
ATOM   28450 O  O   . THR   P  2  245 ? -15.110 -217.299 3.458   1.00 155.83 ? 244 THR   P O   1 
ATOM   28451 C  CB  . THR   P  2  245 ? -12.961 -218.075 5.743   1.00 154.01 ? 244 THR   P CB  1 
ATOM   28452 O  OG1 . THR   P  2  245 ? -12.702 -216.687 5.534   1.00 148.04 ? 244 THR   P OG1 1 
ATOM   28453 C  CG2 . THR   P  2  245 ? -11.746 -218.739 6.353   1.00 150.09 ? 244 THR   P CG2 1 
ATOM   28454 N  N   . GLY   Q  3  3   ? 34.957  -200.596 25.349  1.00 122.92 ? 1   GLY   Q N   1 
ATOM   28455 C  CA  . GLY   Q  3  3   ? 34.953  -201.002 23.912  1.00 122.28 ? 1   GLY   Q CA  1 
ATOM   28456 C  C   . GLY   Q  3  3   ? 35.421  -202.436 23.731  1.00 118.44 ? 1   GLY   Q C   1 
ATOM   28457 O  O   . GLY   Q  3  3   ? 36.302  -202.872 24.499  1.00 119.41 ? 1   GLY   Q O   1 
ATOM   28458 N  N   . TYR   Q  3  4   ? 34.853  -203.152 22.756  1.00 116.56 ? 2   TYR   Q N   1 
ATOM   28459 C  CA  . TYR   Q  3  4   ? 35.260  -204.534 22.392  1.00 114.41 ? 2   TYR   Q CA  1 
ATOM   28460 C  C   . TYR   Q  3  4   ? 36.673  -204.479 21.802  1.00 113.38 ? 2   TYR   Q C   1 
ATOM   28461 O  O   . TYR   Q  3  4   ? 36.893  -203.719 20.843  1.00 113.02 ? 2   TYR   Q O   1 
ATOM   28462 C  CB  . TYR   Q  3  4   ? 34.252  -205.175 21.435  1.00 115.54 ? 2   TYR   Q CB  1 
ATOM   28463 C  CG  . TYR   Q  3  4   ? 34.531  -206.627 21.133  1.00 116.25 ? 2   TYR   Q CG  1 
ATOM   28464 C  CD1 . TYR   Q  3  4   ? 34.366  -207.606 22.101  1.00 115.81 ? 2   TYR   Q CD1 1 
ATOM   28465 C  CD2 . TYR   Q  3  4   ? 34.972  -207.027 19.881  1.00 117.94 ? 2   TYR   Q CD2 1 
ATOM   28466 C  CE1 . TYR   Q  3  4   ? 34.630  -208.940 21.833  1.00 114.78 ? 2   TYR   Q CE1 1 
ATOM   28467 C  CE2 . TYR   Q  3  4   ? 35.238  -208.358 19.597  1.00 116.30 ? 2   TYR   Q CE2 1 
ATOM   28468 C  CZ  . TYR   Q  3  4   ? 35.062  -209.320 20.576  1.00 114.95 ? 2   TYR   Q CZ  1 
ATOM   28469 O  OH  . TYR   Q  3  4   ? 35.318  -210.635 20.311  1.00 112.44 ? 2   TYR   Q OH  1 
ATOM   28470 N  N   . ASP   Q  3  5   ? 37.591  -205.268 22.367  1.00 116.09 ? 3   ASP   Q N   1 
ATOM   28471 C  CA  . ASP   Q  3  5   ? 39.062  -205.122 22.194  1.00 117.53 ? 3   ASP   Q CA  1 
ATOM   28472 C  C   . ASP   Q  3  5   ? 39.687  -206.337 21.486  1.00 117.24 ? 3   ASP   Q C   1 
ATOM   28473 O  O   . ASP   Q  3  5   ? 40.773  -206.160 20.894  1.00 105.91 ? 3   ASP   Q O   1 
ATOM   28474 C  CB  . ASP   Q  3  5   ? 39.723  -204.917 23.558  1.00 121.06 ? 3   ASP   Q CB  1 
ATOM   28475 C  CG  . ASP   Q  3  5   ? 41.059  -204.201 23.502  1.00 124.17 ? 3   ASP   Q CG  1 
ATOM   28476 O  OD1 . ASP   Q  3  5   ? 41.866  -204.402 24.432  1.00 128.24 ? 3   ASP   Q OD1 1 
ATOM   28477 O  OD2 . ASP   Q  3  5   ? 41.280  -203.443 22.536  1.00 129.13 ? 3   ASP   Q OD2 1 
ATOM   28478 N  N   . ARG   Q  3  6   ? 39.046  -207.513 21.559  1.00 117.13 ? 4   ARG   Q N   1 
ATOM   28479 C  CA  . ARG   Q  3  6   ? 39.587  -208.831 21.110  1.00 116.70 ? 4   ARG   Q CA  1 
ATOM   28480 C  C   . ARG   Q  3  6   ? 40.368  -208.699 19.797  1.00 114.57 ? 4   ARG   Q C   1 
ATOM   28481 O  O   . ARG   Q  3  6   ? 39.806  -208.164 18.822  1.00 114.10 ? 4   ARG   Q O   1 
ATOM   28482 C  CB  . ARG   Q  3  6   ? 38.456  -209.847 20.914  1.00 118.88 ? 4   ARG   Q CB  1 
ATOM   28483 C  CG  . ARG   Q  3  6   ? 38.408  -210.949 21.963  1.00 119.74 ? 4   ARG   Q CG  1 
ATOM   28484 C  CD  . ARG   Q  3  6   ? 39.267  -212.150 21.607  1.00 122.55 ? 4   ARG   Q CD  1 
ATOM   28485 N  NE  . ARG   Q  3  6   ? 38.719  -213.403 22.116  1.00 128.54 ? 4   ARG   Q NE  1 
ATOM   28486 C  CZ  . ARG   Q  3  6   ? 39.244  -214.610 21.903  1.00 131.09 ? 4   ARG   Q CZ  1 
ATOM   28487 N  NH1 . ARG   Q  3  6   ? 40.350  -214.746 21.188  1.00 133.32 ? 4   ARG   Q NH1 1 
ATOM   28488 N  NH2 . ARG   Q  3  6   ? 38.662  -215.684 22.411  1.00 129.63 ? 4   ARG   Q NH2 1 
ATOM   28489 N  N   . ALA   Q  3  7   ? 41.607  -209.200 19.782  1.00 111.10 ? 5   ALA   Q N   1 
ATOM   28490 C  CA  . ALA   Q  3  7   ? 42.435  -209.393 18.569  1.00 112.77 ? 5   ALA   Q CA  1 
ATOM   28491 C  C   . ALA   Q  3  7   ? 41.903  -210.607 17.797  1.00 112.68 ? 5   ALA   Q C   1 
ATOM   28492 O  O   . ALA   Q  3  7   ? 42.261  -211.748 18.164  1.00 116.45 ? 5   ALA   Q O   1 
ATOM   28493 C  CB  . ALA   Q  3  7   ? 43.885  -209.567 18.951  1.00 111.16 ? 5   ALA   Q CB  1 
ATOM   28494 N  N   . LEU   Q  3  8   ? 41.068  -210.368 16.779  1.00 112.37 ? 6   LEU   Q N   1 
ATOM   28495 C  CA  . LEU   Q  3  8   ? 40.399  -211.429 15.976  1.00 106.23 ? 6   LEU   Q CA  1 
ATOM   28496 C  C   . LEU   Q  3  8   ? 41.332  -211.890 14.851  1.00 103.76 ? 6   LEU   Q C   1 
ATOM   28497 O  O   . LEU   Q  3  8   ? 41.327  -213.095 14.549  1.00 101.95 ? 6   LEU   Q O   1 
ATOM   28498 C  CB  . LEU   Q  3  8   ? 39.075  -210.893 15.423  1.00 106.93 ? 6   LEU   Q CB  1 
ATOM   28499 C  CG  . LEU   Q  3  8   ? 38.054  -210.442 16.469  1.00 106.79 ? 6   LEU   Q CG  1 
ATOM   28500 C  CD1 . LEU   Q  3  8   ? 36.783  -209.940 15.802  1.00 109.24 ? 6   LEU   Q CD1 1 
ATOM   28501 C  CD2 . LEU   Q  3  8   ? 37.727  -211.560 17.448  1.00 105.63 ? 6   LEU   Q CD2 1 
ATOM   28502 N  N   . SER   Q  3  9   ? 42.095  -210.969 14.255  1.00 101.79 ? 7   SER   Q N   1 
ATOM   28503 C  CA  . SER   Q  3  9   ? 43.138  -211.268 13.239  1.00 99.47  ? 7   SER   Q CA  1 
ATOM   28504 C  C   . SER   Q  3  9   ? 44.491  -211.427 13.942  1.00 99.76  ? 7   SER   Q C   1 
ATOM   28505 O  O   . SER   Q  3  9   ? 45.038  -210.405 14.400  1.00 97.16  ? 7   SER   Q O   1 
ATOM   28506 C  CB  . SER   Q  3  9   ? 43.180  -210.201 12.180  1.00 99.70  ? 7   SER   Q CB  1 
ATOM   28507 O  OG  . SER   Q  3  9   ? 41.887  -209.972 11.641  1.00 100.26 ? 7   SER   Q OG  1 
ATOM   28508 N  N   . ILE   Q  3  10  ? 44.984  -212.667 14.049  1.00 102.19 ? 8   ILE   Q N   1 
ATOM   28509 C  CA  . ILE   Q  3  10  ? 46.281  -213.021 14.705  1.00 102.54 ? 8   ILE   Q CA  1 
ATOM   28510 C  C   . ILE   Q  3  10  ? 47.027  -214.052 13.851  1.00 105.30 ? 8   ILE   Q C   1 
ATOM   28511 O  O   . ILE   Q  3  10  ? 46.382  -214.722 13.021  1.00 106.79 ? 8   ILE   Q O   1 
ATOM   28512 C  CB  . ILE   Q  3  10  ? 46.059  -213.546 16.138  1.00 102.03 ? 8   ILE   Q CB  1 
ATOM   28513 C  CG1 . ILE   Q  3  10  ? 45.142  -214.772 16.167  1.00 99.58  ? 8   ILE   Q CG1 1 
ATOM   28514 C  CG2 . ILE   Q  3  10  ? 45.546  -212.437 17.042  1.00 101.88 ? 8   ILE   Q CG2 1 
ATOM   28515 C  CD1 . ILE   Q  3  10  ? 45.245  -215.582 17.438  1.00 98.82  ? 8   ILE   Q CD1 1 
ATOM   28516 N  N   . PHE   Q  3  11  ? 48.339  -214.170 14.071  1.00 104.73 ? 9   PHE   Q N   1 
ATOM   28517 C  CA  . PHE   Q  3  11  ? 49.239  -215.152 13.416  1.00 107.68 ? 9   PHE   Q CA  1 
ATOM   28518 C  C   . PHE   Q  3  11  ? 48.999  -216.551 13.992  1.00 111.44 ? 9   PHE   Q C   1 
ATOM   28519 O  O   . PHE   Q  3  11  ? 48.824  -216.677 15.219  1.00 116.50 ? 9   PHE   Q O   1 
ATOM   28520 C  CB  . PHE   Q  3  11  ? 50.703  -214.752 13.605  1.00 105.11 ? 9   PHE   Q CB  1 
ATOM   28521 C  CG  . PHE   Q  3  11  ? 51.105  -213.524 12.835  1.00 102.18 ? 9   PHE   Q CG  1 
ATOM   28522 C  CD1 . PHE   Q  3  11  ? 51.385  -213.601 11.480  1.00 103.59 ? 9   PHE   Q CD1 1 
ATOM   28523 C  CD2 . PHE   Q  3  11  ? 51.189  -212.291 13.459  1.00 102.78 ? 9   PHE   Q CD2 1 
ATOM   28524 C  CE1 . PHE   Q  3  11  ? 51.749  -212.471 10.766  1.00 102.93 ? 9   PHE   Q CE1 1 
ATOM   28525 C  CE2 . PHE   Q  3  11  ? 51.552  -211.161 12.743  1.00 104.72 ? 9   PHE   Q CE2 1 
ATOM   28526 C  CZ  . PHE   Q  3  11  ? 51.831  -211.254 11.399  1.00 103.75 ? 9   PHE   Q CZ  1 
ATOM   28527 N  N   . SER   Q  3  12  ? 48.999  -217.561 13.117  1.00 116.62 ? 10  SER   Q N   1 
ATOM   28528 C  CA  . SER   Q  3  12  ? 49.011  -219.005 13.465  1.00 119.46 ? 10  SER   Q CA  1 
ATOM   28529 C  C   . SER   Q  3  12  ? 50.448  -219.515 13.412  1.00 117.30 ? 10  SER   Q C   1 
ATOM   28530 O  O   . SER   Q  3  12  ? 51.303  -218.887 12.791  1.00 111.48 ? 10  SER   Q O   1 
ATOM   28531 C  CB  . SER   Q  3  12  ? 48.104  -219.793 12.551  1.00 124.18 ? 10  SER   Q CB  1 
ATOM   28532 O  OG  . SER   Q  3  12  ? 46.748  -219.669 12.955  1.00 129.04 ? 10  SER   Q OG  1 
ATOM   28533 N  N   . PRO   Q  3  13  ? 50.758  -220.656 14.072  1.00 118.16 ? 11  PRO   Q N   1 
ATOM   28534 C  CA  . PRO   Q  3  13  ? 52.114  -221.215 14.083  1.00 118.11 ? 11  PRO   Q CA  1 
ATOM   28535 C  C   . PRO   Q  3  13  ? 52.862  -221.234 12.737  1.00 118.19 ? 11  PRO   Q C   1 
ATOM   28536 O  O   . PRO   Q  3  13  ? 54.064  -221.027 12.748  1.00 109.53 ? 11  PRO   Q O   1 
ATOM   28537 C  CB  . PRO   Q  3  13  ? 51.862  -222.650 14.570  1.00 120.54 ? 11  PRO   Q CB  1 
ATOM   28538 C  CG  . PRO   Q  3  13  ? 50.697  -222.506 15.524  1.00 118.59 ? 11  PRO   Q CG  1 
ATOM   28539 C  CD  . PRO   Q  3  13  ? 49.824  -221.440 14.898  1.00 116.81 ? 11  PRO   Q CD  1 
ATOM   28540 N  N   . ASP   Q  3  14  ? 52.150  -221.473 11.628  1.00 122.28 ? 12  ASP   Q N   1 
ATOM   28541 C  CA  . ASP   Q  3  14  ? 52.727  -221.578 10.257  1.00 124.80 ? 12  ASP   Q CA  1 
ATOM   28542 C  C   . ASP   Q  3  14  ? 52.940  -220.183 9.649   1.00 123.30 ? 12  ASP   Q C   1 
ATOM   28543 O  O   . ASP   Q  3  14  ? 53.537  -220.111 8.555   1.00 117.06 ? 12  ASP   Q O   1 
ATOM   28544 C  CB  . ASP   Q  3  14  ? 51.856  -222.449 9.345   1.00 130.73 ? 12  ASP   Q CB  1 
ATOM   28545 C  CG  . ASP   Q  3  14  ? 50.422  -221.972 9.180   1.00 135.28 ? 12  ASP   Q CG  1 
ATOM   28546 O  OD1 . ASP   Q  3  14  ? 50.005  -221.075 9.943   1.00 137.96 ? 12  ASP   Q OD1 1 
ATOM   28547 O  OD2 . ASP   Q  3  14  ? 49.730  -222.510 8.293   1.00 141.81 ? 12  ASP   Q OD2 1 
ATOM   28548 N  N   . GLY   Q  3  15  ? 52.462  -219.126 10.318  1.00 122.12 ? 13  GLY   Q N   1 
ATOM   28549 C  CA  . GLY   Q  3  15  ? 52.678  -217.717 9.930   1.00 120.33 ? 13  GLY   Q CA  1 
ATOM   28550 C  C   . GLY   Q  3  15  ? 51.555  -217.163 9.068   1.00 120.66 ? 13  GLY   Q C   1 
ATOM   28551 O  O   . GLY   Q  3  15  ? 51.802  -216.168 8.360   1.00 115.86 ? 13  GLY   Q O   1 
ATOM   28552 N  N   . HIS   Q  3  16  ? 50.365  -217.772 9.121   1.00 121.72 ? 14  HIS   Q N   1 
ATOM   28553 C  CA  . HIS   Q  3  16  ? 49.147  -217.320 8.395   1.00 122.56 ? 14  HIS   Q CA  1 
ATOM   28554 C  C   . HIS   Q  3  16  ? 48.239  -216.535 9.348   1.00 115.42 ? 14  HIS   Q C   1 
ATOM   28555 O  O   . HIS   Q  3  16  ? 48.231  -216.853 10.554  1.00 115.36 ? 14  HIS   Q O   1 
ATOM   28556 C  CB  . HIS   Q  3  16  ? 48.410  -218.514 7.771   1.00 124.43 ? 14  HIS   Q CB  1 
ATOM   28557 C  CG  . HIS   Q  3  16  ? 49.146  -219.155 6.642   1.00 130.23 ? 14  HIS   Q CG  1 
ATOM   28558 N  ND1 . HIS   Q  3  16  ? 49.184  -220.524 6.470   1.00 133.20 ? 14  HIS   Q ND1 1 
ATOM   28559 C  CD2 . HIS   Q  3  16  ? 49.877  -218.625 5.637   1.00 128.41 ? 14  HIS   Q CD2 1 
ATOM   28560 C  CE1 . HIS   Q  3  16  ? 49.902  -220.811 5.403   1.00 137.60 ? 14  HIS   Q CE1 1 
ATOM   28561 N  NE2 . HIS   Q  3  16  ? 50.338  -219.661 4.873   1.00 132.65 ? 14  HIS   Q NE2 1 
ATOM   28562 N  N   . ILE   Q  3  17  ? 47.518  -215.542 8.820   1.00 112.99 ? 15  ILE   Q N   1 
ATOM   28563 C  CA  . ILE   Q  3  17  ? 46.421  -214.820 9.531   1.00 111.55 ? 15  ILE   Q CA  1 
ATOM   28564 C  C   . ILE   Q  3  17  ? 45.095  -215.357 8.979   1.00 110.23 ? 15  ILE   Q C   1 
ATOM   28565 O  O   . ILE   Q  3  17  ? 44.629  -214.839 7.946   1.00 105.75 ? 15  ILE   Q O   1 
ATOM   28566 C  CB  . ILE   Q  3  17  ? 46.549  -213.289 9.378   1.00 110.22 ? 15  ILE   Q CB  1 
ATOM   28567 C  CG1 . ILE   Q  3  17  ? 47.980  -212.803 9.636   1.00 112.34 ? 15  ILE   Q CG1 1 
ATOM   28568 C  CG2 . ILE   Q  3  17  ? 45.544  -212.580 10.275  1.00 110.33 ? 15  ILE   Q CG2 1 
ATOM   28569 C  CD1 . ILE   Q  3  17  ? 48.203  -211.333 9.346   1.00 112.32 ? 15  ILE   Q CD1 1 
ATOM   28570 N  N   . PHE   Q  3  18  ? 44.528  -216.370 9.641   1.00 108.27 ? 16  PHE   Q N   1 
ATOM   28571 C  CA  . PHE   Q  3  18  ? 43.407  -217.198 9.121   1.00 108.81 ? 16  PHE   Q CA  1 
ATOM   28572 C  C   . PHE   Q  3  18  ? 42.186  -216.324 8.820   1.00 110.03 ? 16  PHE   Q C   1 
ATOM   28573 O  O   . PHE   Q  3  18  ? 41.513  -216.596 7.809   1.00 114.20 ? 16  PHE   Q O   1 
ATOM   28574 C  CB  . PHE   Q  3  18  ? 43.056  -218.335 10.086  1.00 110.03 ? 16  PHE   Q CB  1 
ATOM   28575 C  CG  . PHE   Q  3  18  ? 43.976  -219.532 10.027  1.00 112.91 ? 16  PHE   Q CG  1 
ATOM   28576 C  CD1 . PHE   Q  3  18  ? 44.580  -219.920 8.837   1.00 111.15 ? 16  PHE   Q CD1 1 
ATOM   28577 C  CD2 . PHE   Q  3  18  ? 44.217  -220.292 11.161  1.00 111.44 ? 16  PHE   Q CD2 1 
ATOM   28578 C  CE1 . PHE   Q  3  18  ? 45.424  -221.018 8.792   1.00 109.72 ? 16  PHE   Q CE1 1 
ATOM   28579 C  CE2 . PHE   Q  3  18  ? 45.058  -221.393 11.112  1.00 110.95 ? 16  PHE   Q CE2 1 
ATOM   28580 C  CZ  . PHE   Q  3  18  ? 45.661  -221.753 9.929   1.00 111.01 ? 16  PHE   Q CZ  1 
ATOM   28581 N  N   . GLN   Q  3  19  ? 41.915  -215.310 9.646   1.00 106.97 ? 17  GLN   Q N   1 
ATOM   28582 C  CA  . GLN   Q  3  19  ? 40.736  -214.419 9.474   1.00 105.30 ? 17  GLN   Q CA  1 
ATOM   28583 C  C   . GLN   Q  3  19  ? 40.858  -213.654 8.148   1.00 104.88 ? 17  GLN   Q C   1 
ATOM   28584 O  O   . GLN   Q  3  19  ? 39.815  -213.473 7.487   1.00 104.56 ? 17  GLN   Q O   1 
ATOM   28585 C  CB  . GLN   Q  3  19  ? 40.576  -213.493 10.681  1.00 103.52 ? 17  GLN   Q CB  1 
ATOM   28586 C  CG  . GLN   Q  3  19  ? 39.784  -214.125 11.818  1.00 103.18 ? 17  GLN   Q CG  1 
ATOM   28587 C  CD  . GLN   Q  3  19  ? 38.354  -214.408 11.426  1.00 101.43 ? 17  GLN   Q CD  1 
ATOM   28588 O  OE1 . GLN   Q  3  19  ? 37.889  -215.543 11.473  1.00 100.35 ? 17  GLN   Q OE1 1 
ATOM   28589 N  NE2 . GLN   Q  3  19  ? 37.647  -213.367 11.020  1.00 104.04 ? 17  GLN   Q NE2 1 
ATOM   28590 N  N   . VAL   Q  3  20  ? 42.075  -213.245 7.765   1.00 105.71 ? 18  VAL   Q N   1 
ATOM   28591 C  CA  . VAL   Q  3  20  ? 42.367  -212.579 6.457   1.00 106.39 ? 18  VAL   Q CA  1 
ATOM   28592 C  C   . VAL   Q  3  20  ? 42.162  -213.602 5.336   1.00 109.31 ? 18  VAL   Q C   1 
ATOM   28593 O  O   . VAL   Q  3  20  ? 41.550  -213.244 4.312   1.00 110.02 ? 18  VAL   Q O   1 
ATOM   28594 C  CB  . VAL   Q  3  20  ? 43.788  -211.980 6.407   1.00 104.99 ? 18  VAL   Q CB  1 
ATOM   28595 C  CG1 . VAL   Q  3  20  ? 44.156  -211.497 5.011   1.00 105.27 ? 18  VAL   Q CG1 1 
ATOM   28596 C  CG2 . VAL   Q  3  20  ? 43.968  -210.857 7.418   1.00 102.25 ? 18  VAL   Q CG2 1 
ATOM   28597 N  N   . GLU   Q  3  21  ? 42.668  -214.824 5.522   1.00 110.98 ? 19  GLU   Q N   1 
ATOM   28598 C  CA  . GLU   Q  3  21  ? 42.594  -215.915 4.513   1.00 113.95 ? 19  GLU   Q CA  1 
ATOM   28599 C  C   . GLU   Q  3  21  ? 41.140  -216.378 4.353   1.00 108.45 ? 19  GLU   Q C   1 
ATOM   28600 O  O   . GLU   Q  3  21  ? 40.758  -216.687 3.212   1.00 109.29 ? 19  GLU   Q O   1 
ATOM   28601 C  CB  . GLU   Q  3  21  ? 43.528  -217.065 4.892   1.00 117.91 ? 19  GLU   Q CB  1 
ATOM   28602 C  CG  . GLU   Q  3  21  ? 44.901  -216.941 4.259   1.00 125.61 ? 19  GLU   Q CG  1 
ATOM   28603 C  CD  . GLU   Q  3  21  ? 45.990  -217.757 4.934   1.00 133.55 ? 19  GLU   Q CD  1 
ATOM   28604 O  OE1 . GLU   Q  3  21  ? 45.725  -218.926 5.287   1.00 138.63 ? 19  GLU   Q OE1 1 
ATOM   28605 O  OE2 . GLU   Q  3  21  ? 47.100  -217.218 5.108   1.00 144.77 ? 19  GLU   Q OE2 1 
ATOM   28606 N  N   . TYR   Q  3  22  ? 40.358  -216.418 5.438   1.00 107.70 ? 20  TYR   Q N   1 
ATOM   28607 C  CA  . TYR   Q  3  22  ? 38.925  -216.818 5.406   1.00 108.74 ? 20  TYR   Q CA  1 
ATOM   28608 C  C   . TYR   Q  3  22  ? 38.094  -215.704 4.762   1.00 108.85 ? 20  TYR   Q C   1 
ATOM   28609 O  O   . TYR   Q  3  22  ? 37.061  -216.022 4.146   1.00 112.10 ? 20  TYR   Q O   1 
ATOM   28610 C  CB  . TYR   Q  3  22  ? 38.390  -217.158 6.800   1.00 109.67 ? 20  TYR   Q CB  1 
ATOM   28611 C  CG  . TYR   Q  3  22  ? 39.063  -218.314 7.499   1.00 112.75 ? 20  TYR   Q CG  1 
ATOM   28612 C  CD1 . TYR   Q  3  22  ? 39.843  -219.235 6.813   1.00 114.29 ? 20  TYR   Q CD1 1 
ATOM   28613 C  CD2 . TYR   Q  3  22  ? 38.900  -218.498 8.863   1.00 114.95 ? 20  TYR   Q CD2 1 
ATOM   28614 C  CE1 . TYR   Q  3  22  ? 40.456  -220.294 7.465   1.00 116.23 ? 20  TYR   Q CE1 1 
ATOM   28615 C  CE2 . TYR   Q  3  22  ? 39.503  -219.553 9.529   1.00 115.67 ? 20  TYR   Q CE2 1 
ATOM   28616 C  CZ  . TYR   Q  3  22  ? 40.283  -220.456 8.829   1.00 113.31 ? 20  TYR   Q CZ  1 
ATOM   28617 O  OH  . TYR   Q  3  22  ? 40.882  -221.489 9.489   1.00 114.13 ? 20  TYR   Q OH  1 
ATOM   28618 N  N   . ALA   Q  3  23  ? 38.521  -214.445 4.897   1.00 108.28 ? 21  ALA   Q N   1 
ATOM   28619 C  CA  . ALA   Q  3  23  ? 37.908  -213.285 4.206   1.00 109.38 ? 21  ALA   Q CA  1 
ATOM   28620 C  C   . ALA   Q  3  23  ? 38.053  -213.459 2.688   1.00 107.71 ? 21  ALA   Q C   1 
ATOM   28621 O  O   . ALA   Q  3  23  ? 37.121  -213.072 1.962   1.00 109.38 ? 21  ALA   Q O   1 
ATOM   28622 C  CB  . ALA   Q  3  23  ? 38.523  -211.993 4.686   1.00 108.68 ? 21  ALA   Q CB  1 
ATOM   28623 N  N   . LEU   Q  3  24  ? 39.169  -214.037 2.228   1.00 108.68 ? 22  LEU   Q N   1 
ATOM   28624 C  CA  . LEU   Q  3  24  ? 39.419  -214.330 0.788   1.00 109.47 ? 22  LEU   Q CA  1 
ATOM   28625 C  C   . LEU   Q  3  24  ? 38.429  -215.392 0.292   1.00 113.51 ? 22  LEU   Q C   1 
ATOM   28626 O  O   . LEU   Q  3  24  ? 38.033  -215.307 -0.887  1.00 110.97 ? 22  LEU   Q O   1 
ATOM   28627 C  CB  . LEU   Q  3  24  ? 40.870  -214.783 0.584   1.00 110.48 ? 22  LEU   Q CB  1 
ATOM   28628 C  CG  . LEU   Q  3  24  ? 41.837  -213.700 0.107   1.00 110.00 ? 22  LEU   Q CG  1 
ATOM   28629 C  CD1 . LEU   Q  3  24  ? 43.279  -214.161 0.248   1.00 112.51 ? 22  LEU   Q CD1 1 
ATOM   28630 C  CD2 . LEU   Q  3  24  ? 41.545  -213.306 -1.332  1.00 110.87 ? 22  LEU   Q CD2 1 
ATOM   28631 N  N   . GLU   Q  3  25  ? 38.046  -216.350 1.148   1.00 115.72 ? 23  GLU   Q N   1 
ATOM   28632 C  CA  . GLU   Q  3  25  ? 37.072  -217.429 0.815   1.00 118.84 ? 23  GLU   Q CA  1 
ATOM   28633 C  C   . GLU   Q  3  25  ? 35.691  -216.812 0.561   1.00 118.30 ? 23  GLU   Q C   1 
ATOM   28634 O  O   . GLU   Q  3  25  ? 34.972  -217.334 -0.314  1.00 125.17 ? 23  GLU   Q O   1 
ATOM   28635 C  CB  . GLU   Q  3  25  ? 36.977  -218.482 1.924   1.00 118.22 ? 23  GLU   Q CB  1 
ATOM   28636 C  CG  . GLU   Q  3  25  ? 38.261  -219.260 2.155   1.00 120.76 ? 23  GLU   Q CG  1 
ATOM   28637 C  CD  . GLU   Q  3  25  ? 38.762  -220.058 0.963   1.00 122.85 ? 23  GLU   Q CD  1 
ATOM   28638 O  OE1 . GLU   Q  3  25  ? 37.924  -220.628 0.233   1.00 126.98 ? 23  GLU   Q OE1 1 
ATOM   28639 O  OE2 . GLU   Q  3  25  ? 39.990  -220.107 0.768   1.00 126.83 ? 23  GLU   Q OE2 1 
ATOM   28640 N  N   . ALA   Q  3  26  ? 35.332  -215.758 1.304   1.00 114.27 ? 24  ALA   Q N   1 
ATOM   28641 C  CA  . ALA   Q  3  26  ? 34.091  -214.972 1.105   1.00 109.62 ? 24  ALA   Q CA  1 
ATOM   28642 C  C   . ALA   Q  3  26  ? 34.126  -214.326 -0.285  1.00 108.62 ? 24  ALA   Q C   1 
ATOM   28643 O  O   . ALA   Q  3  26  ? 33.073  -214.318 -0.954  1.00 103.21 ? 24  ALA   Q O   1 
ATOM   28644 C  CB  . ALA   Q  3  26  ? 33.936  -213.940 2.195   1.00 107.62 ? 24  ALA   Q CB  1 
ATOM   28645 N  N   . VAL   Q  3  27  ? 35.296  -213.823 -0.700  1.00 111.66 ? 25  VAL   Q N   1 
ATOM   28646 C  CA  . VAL   Q  3  27  ? 35.530  -213.211 -2.044  1.00 115.99 ? 25  VAL   Q CA  1 
ATOM   28647 C  C   . VAL   Q  3  27  ? 35.329  -214.295 -3.109  1.00 117.36 ? 25  VAL   Q C   1 
ATOM   28648 O  O   . VAL   Q  3  27  ? 34.645  -214.015 -4.108  1.00 119.72 ? 25  VAL   Q O   1 
ATOM   28649 C  CB  . VAL   Q  3  27  ? 36.925  -212.563 -2.162  1.00 118.77 ? 25  VAL   Q CB  1 
ATOM   28650 C  CG1 . VAL   Q  3  27  ? 37.233  -212.124 -3.588  1.00 119.97 ? 25  VAL   Q CG1 1 
ATOM   28651 C  CG2 . VAL   Q  3  27  ? 37.090  -211.391 -1.205  1.00 118.52 ? 25  VAL   Q CG2 1 
ATOM   28652 N  N   . LYS   Q  3  28  ? 35.896  -215.485 -2.887  1.00 118.88 ? 26  LYS   Q N   1 
ATOM   28653 C  CA  . LYS   Q  3  28  ? 35.813  -216.646 -3.816  1.00 122.14 ? 26  LYS   Q CA  1 
ATOM   28654 C  C   . LYS   Q  3  28  ? 34.357  -217.109 -3.977  1.00 122.48 ? 26  LYS   Q C   1 
ATOM   28655 O  O   . LYS   Q  3  28  ? 34.070  -217.744 -5.006  1.00 121.19 ? 26  LYS   Q O   1 
ATOM   28656 C  CB  . LYS   Q  3  28  ? 36.686  -217.807 -3.328  1.00 124.53 ? 26  LYS   Q CB  1 
ATOM   28657 C  CG  . LYS   Q  3  28  ? 38.098  -217.833 -3.897  1.00 127.22 ? 26  LYS   Q CG  1 
ATOM   28658 C  CD  . LYS   Q  3  28  ? 38.735  -219.207 -3.873  1.00 128.01 ? 26  LYS   Q CD  1 
ATOM   28659 C  CE  . LYS   Q  3  28  ? 39.464  -219.505 -2.581  1.00 130.65 ? 26  LYS   Q CE  1 
ATOM   28660 N  NZ  . LYS   Q  3  28  ? 40.815  -218.894 -2.568  1.00 131.12 ? 26  LYS   Q NZ  1 
ATOM   28661 N  N   . ARG   Q  3  29  ? 33.488  -216.828 -2.998  1.00 125.43 ? 27  ARG   Q N   1 
ATOM   28662 C  CA  . ARG   Q  3  29  ? 32.040  -217.182 -3.025  1.00 127.90 ? 27  ARG   Q CA  1 
ATOM   28663 C  C   . ARG   Q  3  29  ? 31.254  -216.124 -3.810  1.00 125.67 ? 27  ARG   Q C   1 
ATOM   28664 O  O   . ARG   Q  3  29  ? 30.228  -216.490 -4.419  1.00 128.05 ? 27  ARG   Q O   1 
ATOM   28665 C  CB  . ARG   Q  3  29  ? 31.493  -217.319 -1.600  1.00 130.83 ? 27  ARG   Q CB  1 
ATOM   28666 C  CG  . ARG   Q  3  29  ? 30.016  -217.682 -1.523  1.00 134.48 ? 27  ARG   Q CG  1 
ATOM   28667 C  CD  . ARG   Q  3  29  ? 29.559  -218.001 -0.111  1.00 137.41 ? 27  ARG   Q CD  1 
ATOM   28668 N  NE  . ARG   Q  3  29  ? 30.062  -219.292 0.342   1.00 141.34 ? 27  ARG   Q NE  1 
ATOM   28669 C  CZ  . ARG   Q  3  29  ? 31.187  -219.493 1.028   1.00 144.69 ? 27  ARG   Q CZ  1 
ATOM   28670 N  NH1 . ARG   Q  3  29  ? 31.969  -218.481 1.372   1.00 144.47 ? 27  ARG   Q NH1 1 
ATOM   28671 N  NH2 . ARG   Q  3  29  ? 31.530  -220.723 1.371   1.00 147.81 ? 27  ARG   Q NH2 1 
ATOM   28672 N  N   . GLY   Q  3  30  ? 31.710  -214.867 -3.790  1.00 122.83 ? 28  GLY   Q N   1 
ATOM   28673 C  CA  . GLY   Q  3  30  ? 31.041  -213.731 -4.455  1.00 120.35 ? 28  GLY   Q CA  1 
ATOM   28674 C  C   . GLY   Q  3  30  ? 30.951  -213.924 -5.959  1.00 117.97 ? 28  GLY   Q C   1 
ATOM   28675 O  O   . GLY   Q  3  30  ? 31.721  -214.747 -6.497  1.00 108.99 ? 28  GLY   Q O   1 
ATOM   28676 N  N   . THR   Q  3  31  ? 30.051  -213.185 -6.616  1.00 119.44 ? 29  THR   Q N   1 
ATOM   28677 C  CA  . THR   Q  3  31  ? 29.811  -213.250 -8.084  1.00 120.48 ? 29  THR   Q CA  1 
ATOM   28678 C  C   . THR   Q  3  31  ? 31.058  -212.727 -8.804  1.00 118.63 ? 29  THR   Q C   1 
ATOM   28679 O  O   . THR   Q  3  31  ? 31.709  -211.814 -8.266  1.00 115.15 ? 29  THR   Q O   1 
ATOM   28680 C  CB  . THR   Q  3  31  ? 28.545  -212.484 -8.493  1.00 124.58 ? 29  THR   Q CB  1 
ATOM   28681 O  OG1 . THR   Q  3  31  ? 28.702  -211.109 -8.139  1.00 127.17 ? 29  THR   Q OG1 1 
ATOM   28682 C  CG2 . THR   Q  3  31  ? 27.293  -213.032 -7.846  1.00 124.99 ? 29  THR   Q CG2 1 
ATOM   28683 N  N   . CYS   Q  3  32  ? 31.386  -213.309 -9.959  1.00 122.57 ? 30  CYS   Q N   1 
ATOM   28684 C  CA  . CYS   Q  3  32  ? 32.601  -212.973 -10.747 1.00 126.94 ? 30  CYS   Q CA  1 
ATOM   28685 C  C   . CYS   Q  3  32  ? 32.532  -211.511 -11.198 1.00 123.41 ? 30  CYS   Q C   1 
ATOM   28686 O  O   . CYS   Q  3  32  ? 31.469  -211.087 -11.689 1.00 127.39 ? 30  CYS   Q O   1 
ATOM   28687 C  CB  . CYS   Q  3  32  ? 32.763  -213.877 -11.963 1.00 131.58 ? 30  CYS   Q CB  1 
ATOM   28688 S  SG  . CYS   Q  3  32  ? 34.259  -213.514 -12.921 1.00 136.65 ? 30  CYS   Q SG  1 
ATOM   28689 N  N   . ALA   Q  3  33  ? 33.629  -210.778 -11.008 1.00 123.00 ? 31  ALA   Q N   1 
ATOM   28690 C  CA  . ALA   Q  3  33  ? 33.844  -209.406 -11.518 1.00 125.17 ? 31  ALA   Q CA  1 
ATOM   28691 C  C   . ALA   Q  3  33  ? 35.136  -209.401 -12.337 1.00 124.21 ? 31  ALA   Q C   1 
ATOM   28692 O  O   . ALA   Q  3  33  ? 36.111  -210.048 -11.905 1.00 119.58 ? 31  ALA   Q O   1 
ATOM   28693 C  CB  . ALA   Q  3  33  ? 33.906  -208.423 -10.374 1.00 122.43 ? 31  ALA   Q CB  1 
ATOM   28694 N  N   . VAL   Q  3  34  ? 35.130  -208.714 -13.480 1.00 126.45 ? 32  VAL   Q N   1 
ATOM   28695 C  CA  . VAL   Q  3  34  ? 36.295  -208.636 -14.409 1.00 125.33 ? 32  VAL   Q CA  1 
ATOM   28696 C  C   . VAL   Q  3  34  ? 36.525  -207.173 -14.801 1.00 123.87 ? 32  VAL   Q C   1 
ATOM   28697 O  O   . VAL   Q  3  34  ? 35.535  -206.435 -14.997 1.00 117.83 ? 32  VAL   Q O   1 
ATOM   28698 C  CB  . VAL   Q  3  34  ? 36.104  -209.543 -15.642 1.00 128.88 ? 32  VAL   Q CB  1 
ATOM   28699 C  CG1 . VAL   Q  3  34  ? 34.820  -209.233 -16.395 1.00 130.33 ? 32  VAL   Q CG1 1 
ATOM   28700 C  CG2 . VAL   Q  3  34  ? 37.305  -209.486 -16.576 1.00 130.53 ? 32  VAL   Q CG2 1 
ATOM   28701 N  N   . GLY   Q  3  35  ? 37.800  -206.787 -14.878 1.00 123.14 ? 33  GLY   Q N   1 
ATOM   28702 C  CA  . GLY   Q  3  35  ? 38.270  -205.499 -15.416 1.00 121.72 ? 33  GLY   Q CA  1 
ATOM   28703 C  C   . GLY   Q  3  35  ? 39.219  -205.726 -16.578 1.00 122.43 ? 33  GLY   Q C   1 
ATOM   28704 O  O   . GLY   Q  3  35  ? 40.143  -206.552 -16.435 1.00 122.41 ? 33  GLY   Q O   1 
ATOM   28705 N  N   . VAL   Q  3  36  ? 38.976  -205.047 -17.701 1.00 122.79 ? 34  VAL   Q N   1 
ATOM   28706 C  CA  . VAL   Q  3  36  ? 39.844  -205.069 -18.916 1.00 122.11 ? 34  VAL   Q CA  1 
ATOM   28707 C  C   . VAL   Q  3  36  ? 40.041  -203.621 -19.369 1.00 119.88 ? 34  VAL   Q C   1 
ATOM   28708 O  O   . VAL   Q  3  36  ? 39.025  -202.929 -19.579 1.00 117.72 ? 34  VAL   Q O   1 
ATOM   28709 C  CB  . VAL   Q  3  36  ? 39.228  -205.925 -20.040 1.00 124.08 ? 34  VAL   Q CB  1 
ATOM   28710 C  CG1 . VAL   Q  3  36  ? 40.084  -205.912 -21.299 1.00 122.63 ? 34  VAL   Q CG1 1 
ATOM   28711 C  CG2 . VAL   Q  3  36  ? 38.968  -207.354 -19.586 1.00 127.18 ? 34  VAL   Q CG2 1 
ATOM   28712 N  N   . LYS   Q  3  37  ? 41.292  -203.176 -19.507 1.00 115.53 ? 35  LYS   Q N   1 
ATOM   28713 C  CA  . LYS   Q  3  37  ? 41.596  -201.807 -19.992 1.00 117.99 ? 35  LYS   Q CA  1 
ATOM   28714 C  C   . LYS   Q  3  37  ? 42.132  -201.896 -21.420 1.00 120.68 ? 35  LYS   Q C   1 
ATOM   28715 O  O   . LYS   Q  3  37  ? 43.014  -202.742 -21.679 1.00 116.85 ? 35  LYS   Q O   1 
ATOM   28716 C  CB  . LYS   Q  3  37  ? 42.532  -201.061 -19.035 1.00 118.23 ? 35  LYS   Q CB  1 
ATOM   28717 C  CG  . LYS   Q  3  37  ? 43.995  -201.475 -19.026 1.00 119.43 ? 35  LYS   Q CG  1 
ATOM   28718 C  CD  . LYS   Q  3  37  ? 44.712  -200.955 -17.796 1.00 117.85 ? 35  LYS   Q CD  1 
ATOM   28719 C  CE  . LYS   Q  3  37  ? 46.061  -200.341 -18.094 1.00 117.87 ? 35  LYS   Q CE  1 
ATOM   28720 N  NZ  . LYS   Q  3  37  ? 46.800  -200.043 -16.845 1.00 117.08 ? 35  LYS   Q NZ  1 
ATOM   28721 N  N   . GLY   Q  3  38  ? 41.570  -201.062 -22.300 1.00 124.10 ? 36  GLY   Q N   1 
ATOM   28722 C  CA  . GLY   Q  3  38  ? 41.931  -200.952 -23.724 1.00 126.96 ? 36  GLY   Q CA  1 
ATOM   28723 C  C   . GLY   Q  3  38  ? 42.991  -199.889 -23.936 1.00 125.99 ? 36  GLY   Q C   1 
ATOM   28724 O  O   . GLY   Q  3  38  ? 43.776  -199.634 -22.999 1.00 113.76 ? 36  GLY   Q O   1 
ATOM   28725 N  N   . LYS   Q  3  39  ? 43.002  -199.281 -25.123 1.00 131.59 ? 37  LYS   Q N   1 
ATOM   28726 C  CA  . LYS   Q  3  39  ? 44.003  -198.263 -25.535 1.00 137.52 ? 37  LYS   Q CA  1 
ATOM   28727 C  C   . LYS   Q  3  39  ? 43.552  -196.884 -25.032 1.00 135.86 ? 37  LYS   Q C   1 
ATOM   28728 O  O   . LYS   Q  3  39  ? 44.421  -196.012 -24.838 1.00 134.37 ? 37  LYS   Q O   1 
ATOM   28729 C  CB  . LYS   Q  3  39  ? 44.175  -198.302 -27.058 1.00 143.09 ? 37  LYS   Q CB  1 
ATOM   28730 C  CG  . LYS   Q  3  39  ? 45.595  -198.079 -27.561 1.00 148.74 ? 37  LYS   Q CG  1 
ATOM   28731 C  CD  . LYS   Q  3  39  ? 45.973  -196.620 -27.706 1.00 149.90 ? 37  LYS   Q CD  1 
ATOM   28732 C  CE  . LYS   Q  3  39  ? 47.456  -196.413 -27.929 1.00 149.46 ? 37  LYS   Q CE  1 
ATOM   28733 N  NZ  . LYS   Q  3  39  ? 47.818  -194.977 -27.899 1.00 148.38 ? 37  LYS   Q NZ  1 
ATOM   28734 N  N   . ASN   Q  3  40  ? 42.246  -196.713 -24.800 1.00 137.84 ? 38  ASN   Q N   1 
ATOM   28735 C  CA  . ASN   Q  3  40  ? 41.607  -195.396 -24.527 1.00 138.46 ? 38  ASN   Q CA  1 
ATOM   28736 C  C   . ASN   Q  3  40  ? 40.375  -195.550 -23.623 1.00 134.58 ? 38  ASN   Q C   1 
ATOM   28737 O  O   . ASN   Q  3  40  ? 39.498  -194.663 -23.682 1.00 135.05 ? 38  ASN   Q O   1 
ATOM   28738 C  CB  . ASN   Q  3  40  ? 41.227  -194.691 -25.834 1.00 145.57 ? 38  ASN   Q CB  1 
ATOM   28739 C  CG  . ASN   Q  3  40  ? 40.268  -195.457 -26.730 1.00 151.22 ? 38  ASN   Q CG  1 
ATOM   28740 O  OD1 . ASN   Q  3  40  ? 39.993  -195.009 -27.840 1.00 160.94 ? 38  ASN   Q OD1 1 
ATOM   28741 N  ND2 . ASN   Q  3  40  ? 39.744  -196.596 -26.297 1.00 152.53 ? 38  ASN   Q ND2 1 
ATOM   28742 N  N   . CYS   Q  3  41  ? 40.305  -196.618 -22.822 1.00 132.92 ? 39  CYS   Q N   1 
ATOM   28743 C  CA  . CYS   Q  3  41  ? 39.118  -196.970 -21.994 1.00 128.98 ? 39  CYS   Q CA  1 
ATOM   28744 C  C   . CYS   Q  3  41  ? 39.437  -198.137 -21.057 1.00 129.03 ? 39  CYS   Q C   1 
ATOM   28745 O  O   . CYS   Q  3  41  ? 40.371  -198.909 -21.357 1.00 128.89 ? 39  CYS   Q O   1 
ATOM   28746 C  CB  . CYS   Q  3  41  ? 37.922  -197.344 -22.863 1.00 127.19 ? 39  CYS   Q CB  1 
ATOM   28747 S  SG  . CYS   Q  3  41  ? 38.187  -198.828 -23.865 1.00 127.31 ? 39  CYS   Q SG  1 
ATOM   28748 N  N   . VAL   Q  3  42  ? 38.679  -198.238 -19.962 1.00 128.88 ? 40  VAL   Q N   1 
ATOM   28749 C  CA  . VAL   Q  3  42  ? 38.606  -199.433 -19.070 1.00 127.36 ? 40  VAL   Q CA  1 
ATOM   28750 C  C   . VAL   Q  3  42  ? 37.151  -199.906 -19.072 1.00 125.97 ? 40  VAL   Q C   1 
ATOM   28751 O  O   . VAL   Q  3  42  ? 36.250  -199.044 -19.064 1.00 128.93 ? 40  VAL   Q O   1 
ATOM   28752 C  CB  . VAL   Q  3  42  ? 39.100  -199.135 -17.639 1.00 127.80 ? 40  VAL   Q CB  1 
ATOM   28753 C  CG1 . VAL   Q  3  42  ? 39.372  -200.419 -16.869 1.00 128.40 ? 40  VAL   Q CG1 1 
ATOM   28754 C  CG2 . VAL   Q  3  42  ? 40.331  -198.239 -17.626 1.00 126.68 ? 40  VAL   Q CG2 1 
ATOM   28755 N  N   . VAL   Q  3  43  ? 36.934  -201.220 -19.110 1.00 124.55 ? 41  VAL   Q N   1 
ATOM   28756 C  CA  . VAL   Q  3  43  ? 35.577  -201.839 -19.061 1.00 126.40 ? 41  VAL   Q CA  1 
ATOM   28757 C  C   . VAL   Q  3  43  ? 35.507  -202.729 -17.818 1.00 126.24 ? 41  VAL   Q C   1 
ATOM   28758 O  O   . VAL   Q  3  43  ? 36.392  -203.591 -17.655 1.00 122.60 ? 41  VAL   Q O   1 
ATOM   28759 C  CB  . VAL   Q  3  43  ? 35.261  -202.626 -20.347 1.00 126.19 ? 41  VAL   Q CB  1 
ATOM   28760 C  CG1 . VAL   Q  3  43  ? 33.926  -203.350 -20.253 1.00 127.79 ? 41  VAL   Q CG1 1 
ATOM   28761 C  CG2 . VAL   Q  3  43  ? 35.290  -201.727 -21.573 1.00 127.04 ? 41  VAL   Q CG2 1 
ATOM   28762 N  N   . LEU   Q  3  44  ? 34.499  -202.504 -16.973 1.00 129.19 ? 42  LEU   Q N   1 
ATOM   28763 C  CA  . LEU   Q  3  44  ? 34.194  -203.356 -15.796 1.00 130.73 ? 42  LEU   Q CA  1 
ATOM   28764 C  C   . LEU   Q  3  44  ? 32.980  -204.230 -16.128 1.00 132.88 ? 42  LEU   Q C   1 
ATOM   28765 O  O   . LEU   Q  3  44  ? 31.892  -203.668 -16.377 1.00 128.78 ? 42  LEU   Q O   1 
ATOM   28766 C  CB  . LEU   Q  3  44  ? 33.944  -202.468 -14.571 1.00 129.75 ? 42  LEU   Q CB  1 
ATOM   28767 C  CG  . LEU   Q  3  44  ? 35.152  -201.687 -14.049 1.00 129.47 ? 42  LEU   Q CG  1 
ATOM   28768 C  CD1 . LEU   Q  3  44  ? 34.798  -200.954 -12.764 1.00 127.99 ? 42  LEU   Q CD1 1 
ATOM   28769 C  CD2 . LEU   Q  3  44  ? 36.356  -202.593 -13.819 1.00 128.81 ? 42  LEU   Q CD2 1 
ATOM   28770 N  N   . GLY   Q  3  45  ? 33.188  -205.551 -16.168 1.00 135.55 ? 43  GLY   Q N   1 
ATOM   28771 C  CA  . GLY   Q  3  45  ? 32.133  -206.568 -16.333 1.00 135.89 ? 43  GLY   Q CA  1 
ATOM   28772 C  C   . GLY   Q  3  45  ? 31.846  -207.257 -15.012 1.00 137.72 ? 43  GLY   Q C   1 
ATOM   28773 O  O   . GLY   Q  3  45  ? 32.799  -207.426 -14.224 1.00 134.90 ? 43  GLY   Q O   1 
ATOM   28774 N  N   . CYS   Q  3  46  ? 30.585  -207.621 -14.763 1.00 141.57 ? 44  CYS   Q N   1 
ATOM   28775 C  CA  . CYS   Q  3  46  ? 30.124  -208.217 -13.481 1.00 146.24 ? 44  CYS   Q CA  1 
ATOM   28776 C  C   . CYS   Q  3  46  ? 29.037  -209.267 -13.730 1.00 148.07 ? 44  CYS   Q C   1 
ATOM   28777 O  O   . CYS   Q  3  46  ? 28.053  -208.956 -14.426 1.00 150.27 ? 44  CYS   Q O   1 
ATOM   28778 C  CB  . CYS   Q  3  46  ? 29.609  -207.141 -12.533 1.00 151.53 ? 44  CYS   Q CB  1 
ATOM   28779 S  SG  . CYS   Q  3  46  ? 30.901  -205.990 -11.996 1.00 151.85 ? 44  CYS   Q SG  1 
ATOM   28780 N  N   . GLU   Q  3  47  ? 29.230  -210.465 -13.170 1.00 152.23 ? 45  GLU   Q N   1 
ATOM   28781 C  CA  . GLU   Q  3  47  ? 28.235  -211.569 -13.145 1.00 156.97 ? 45  GLU   Q CA  1 
ATOM   28782 C  C   . GLU   Q  3  47  ? 27.108  -211.191 -12.175 1.00 160.39 ? 45  GLU   Q C   1 
ATOM   28783 O  O   . GLU   Q  3  47  ? 27.408  -210.561 -11.140 1.00 159.57 ? 45  GLU   Q O   1 
ATOM   28784 C  CB  . GLU   Q  3  47  ? 28.912  -212.873 -12.715 1.00 155.97 ? 45  GLU   Q CB  1 
ATOM   28785 C  CG  . GLU   Q  3  47  ? 28.005  -214.092 -12.777 1.00 159.34 ? 45  GLU   Q CG  1 
ATOM   28786 C  CD  . GLU   Q  3  47  ? 28.481  -215.305 -11.995 1.00 155.51 ? 45  GLU   Q CD  1 
ATOM   28787 O  OE1 . GLU   Q  3  47  ? 27.684  -216.251 -11.848 1.00 158.89 ? 45  GLU   Q OE1 1 
ATOM   28788 O  OE2 . GLU   Q  3  47  ? 29.641  -215.307 -11.533 1.00 151.28 ? 45  GLU   Q OE2 1 
ATOM   28789 N  N   . ARG   Q  3  48  ? 25.865  -211.550 -12.510 1.00 160.37 ? 46  ARG   Q N   1 
ATOM   28790 C  CA  . ARG   Q  3  48  ? 24.695  -211.485 -11.593 1.00 166.44 ? 46  ARG   Q CA  1 
ATOM   28791 C  C   . ARG   Q  3  48  ? 23.967  -212.835 -11.624 1.00 163.85 ? 46  ARG   Q C   1 
ATOM   28792 O  O   . ARG   Q  3  48  ? 23.424  -213.189 -12.689 1.00 155.86 ? 46  ARG   Q O   1 
ATOM   28793 C  CB  . ARG   Q  3  48  ? 23.764  -210.327 -11.967 1.00 172.41 ? 46  ARG   Q CB  1 
ATOM   28794 C  CG  . ARG   Q  3  48  ? 24.210  -208.974 -11.428 1.00 175.52 ? 46  ARG   Q CG  1 
ATOM   28795 C  CD  . ARG   Q  3  48  ? 23.056  -208.024 -11.150 1.00 176.44 ? 46  ARG   Q CD  1 
ATOM   28796 N  NE  . ARG   Q  3  48  ? 22.371  -207.583 -12.363 1.00 176.27 ? 46  ARG   Q NE  1 
ATOM   28797 C  CZ  . ARG   Q  3  48  ? 21.215  -208.062 -12.828 1.00 178.24 ? 46  ARG   Q CZ  1 
ATOM   28798 N  NH1 . ARG   Q  3  48  ? 20.567  -209.024 -12.190 1.00 179.50 ? 46  ARG   Q NH1 1 
ATOM   28799 N  NH2 . ARG   Q  3  48  ? 20.704  -207.569 -13.944 1.00 175.11 ? 46  ARG   Q NH2 1 
ATOM   28800 N  N   . ARG   Q  3  49  ? 23.968  -213.549 -10.493 1.00 164.79 ? 47  ARG   Q N   1 
ATOM   28801 C  CA  . ARG   Q  3  49  ? 23.414  -214.926 -10.355 1.00 166.40 ? 47  ARG   Q CA  1 
ATOM   28802 C  C   . ARG   Q  3  49  ? 21.906  -214.906 -10.634 1.00 170.23 ? 47  ARG   Q C   1 
ATOM   28803 O  O   . ARG   Q  3  49  ? 21.245  -213.922 -10.248 1.00 168.06 ? 47  ARG   Q O   1 
ATOM   28804 C  CB  . ARG   Q  3  49  ? 23.742  -215.517 -8.979  1.00 167.36 ? 47  ARG   Q CB  1 
ATOM   28805 C  CG  . ARG   Q  3  49  ? 23.258  -214.720 -7.775  1.00 166.44 ? 47  ARG   Q CG  1 
ATOM   28806 C  CD  . ARG   Q  3  49  ? 23.933  -215.223 -6.509  1.00 165.54 ? 47  ARG   Q CD  1 
ATOM   28807 N  NE  . ARG   Q  3  49  ? 23.517  -214.506 -5.307  1.00 163.38 ? 47  ARG   Q NE  1 
ATOM   28808 C  CZ  . ARG   Q  3  49  ? 22.594  -214.914 -4.435  1.00 162.60 ? 47  ARG   Q CZ  1 
ATOM   28809 N  NH1 . ARG   Q  3  49  ? 21.951  -216.059 -4.605  1.00 162.85 ? 47  ARG   Q NH1 1 
ATOM   28810 N  NH2 . ARG   Q  3  49  ? 22.316  -214.165 -3.382  1.00 163.31 ? 47  ARG   Q NH2 1 
ATOM   28811 N  N   . SER   Q  3  50  ? 21.398  -215.962 -11.283 1.00 177.11 ? 48  SER   Q N   1 
ATOM   28812 C  CA  . SER   Q  3  50  ? 20.024  -216.049 -11.847 1.00 187.26 ? 48  SER   Q CA  1 
ATOM   28813 C  C   . SER   Q  3  50  ? 19.123  -216.973 -11.014 1.00 193.70 ? 48  SER   Q C   1 
ATOM   28814 O  O   . SER   Q  3  50  ? 18.037  -217.326 -11.519 1.00 201.67 ? 48  SER   Q O   1 
ATOM   28815 C  CB  . SER   Q  3  50  ? 20.065  -216.502 -13.282 1.00 188.42 ? 48  SER   Q CB  1 
ATOM   28816 O  OG  . SER   Q  3  50  ? 18.814  -216.280 -13.915 1.00 191.67 ? 48  SER   Q OG  1 
ATOM   28817 N  N   . THR   Q  3  51  ? 19.531  -217.341 -9.792  1.00 195.64 ? 49  THR   Q N   1 
ATOM   28818 C  CA  . THR   Q  3  51  ? 18.660  -218.028 -8.796  1.00 193.16 ? 49  THR   Q CA  1 
ATOM   28819 C  C   . THR   Q  3  51  ? 17.658  -217.019 -8.212  1.00 199.08 ? 49  THR   Q C   1 
ATOM   28820 O  O   . THR   Q  3  51  ? 16.778  -217.453 -7.440  1.00 207.33 ? 49  THR   Q O   1 
ATOM   28821 C  CB  . THR   Q  3  51  ? 19.470  -218.716 -7.687  1.00 185.98 ? 49  THR   Q CB  1 
ATOM   28822 O  OG1 . THR   Q  3  51  ? 20.549  -217.864 -7.303  1.00 173.70 ? 49  THR   Q OG1 1 
ATOM   28823 C  CG2 . THR   Q  3  51  ? 20.011  -220.066 -8.107  1.00 181.53 ? 49  THR   Q CG2 1 
ATOM   28824 N  N   . LEU   Q  3  52  ? 17.789  -215.733 -8.569  1.00 200.41 ? 50  LEU   Q N   1 
ATOM   28825 C  CA  . LEU   Q  3  52  ? 16.890  -214.627 -8.139  1.00 199.25 ? 50  LEU   Q CA  1 
ATOM   28826 C  C   . LEU   Q  3  52  ? 16.108  -214.107 -9.356  1.00 192.60 ? 50  LEU   Q C   1 
ATOM   28827 O  O   . LEU   Q  3  52  ? 16.617  -213.199 -10.046 1.00 197.39 ? 50  LEU   Q O   1 
ATOM   28828 C  CB  . LEU   Q  3  52  ? 17.716  -213.499 -7.500  1.00 198.68 ? 50  LEU   Q CB  1 
ATOM   28829 C  CG  . LEU   Q  3  52  ? 18.998  -213.899 -6.766  1.00 196.52 ? 50  LEU   Q CG  1 
ATOM   28830 C  CD1 . LEU   Q  3  52  ? 19.835  -212.669 -6.444  1.00 189.29 ? 50  LEU   Q CD1 1 
ATOM   28831 C  CD2 . LEU   Q  3  52  ? 18.694  -214.682 -5.498  1.00 198.48 ? 50  LEU   Q CD2 1 
ATOM   28832 N  N   . LYS   Q  3  53  ? 14.928  -214.676 -9.624  1.00 177.31 ? 51  LYS   Q N   1 
ATOM   28833 C  CA  . LYS   Q  3  53  ? 13.905  -214.090 -10.538 1.00 174.74 ? 51  LYS   Q CA  1 
ATOM   28834 C  C   . LYS   Q  3  53  ? 12.829  -213.418 -9.679  1.00 158.52 ? 51  LYS   Q C   1 
ATOM   28835 O  O   . LYS   Q  3  53  ? 12.709  -213.799 -8.497  1.00 168.61 ? 51  LYS   Q O   1 
ATOM   28836 C  CB  . LYS   Q  3  53  ? 13.331  -215.148 -11.487 1.00 175.01 ? 51  LYS   Q CB  1 
ATOM   28837 C  CG  . LYS   Q  3  53  ? 13.732  -214.984 -12.948 1.00 180.94 ? 51  LYS   Q CG  1 
ATOM   28838 C  CD  . LYS   Q  3  53  ? 15.232  -214.892 -13.176 1.00 182.05 ? 51  LYS   Q CD  1 
ATOM   28839 C  CE  . LYS   Q  3  53  ? 15.593  -214.253 -14.500 1.00 184.49 ? 51  LYS   Q CE  1 
ATOM   28840 N  NZ  . LYS   Q  3  53  ? 17.003  -213.798 -14.520 1.00 183.73 ? 51  LYS   Q NZ  1 
ATOM   28841 N  N   . LEU   Q  3  54  ? 12.100  -212.454 -10.255 1.00 144.77 ? 52  LEU   Q N   1 
ATOM   28842 C  CA  . LEU   Q  3  54  ? 11.187  -211.509 -9.547  1.00 135.71 ? 52  LEU   Q CA  1 
ATOM   28843 C  C   . LEU   Q  3  54  ? 11.989  -210.354 -8.926  1.00 130.55 ? 52  LEU   Q C   1 
ATOM   28844 O  O   . LEU   Q  3  54  ? 11.418  -209.639 -8.079  1.00 126.88 ? 52  LEU   Q O   1 
ATOM   28845 C  CB  . LEU   Q  3  54  ? 10.382  -212.252 -8.472  1.00 131.51 ? 52  LEU   Q CB  1 
ATOM   28846 C  CG  . LEU   Q  3  54  ? 8.926   -212.570 -8.806  1.00 129.78 ? 52  LEU   Q CG  1 
ATOM   28847 C  CD1 . LEU   Q  3  54  ? 8.778   -213.127 -10.214 1.00 129.91 ? 52  LEU   Q CD1 1 
ATOM   28848 C  CD2 . LEU   Q  3  54  ? 8.359   -213.542 -7.783  1.00 128.15 ? 52  LEU   Q CD2 1 
ATOM   28849 N  N   . GLN   Q  3  55  ? 13.248  -210.161 -9.337  1.00 131.69 ? 53  GLN   Q N   1 
ATOM   28850 C  CA  . GLN   Q  3  55  ? 14.083  -208.998 -8.928  1.00 133.25 ? 53  GLN   Q CA  1 
ATOM   28851 C  C   . GLN   Q  3  55  ? 13.516  -207.718 -9.556  1.00 135.08 ? 53  GLN   Q C   1 
ATOM   28852 O  O   . GLN   Q  3  55  ? 12.850  -207.814 -10.605 1.00 135.08 ? 53  GLN   Q O   1 
ATOM   28853 C  CB  . GLN   Q  3  55  ? 15.545  -209.173 -9.349  1.00 134.99 ? 53  GLN   Q CB  1 
ATOM   28854 C  CG  . GLN   Q  3  55  ? 16.378  -210.003 -8.380  1.00 135.81 ? 53  GLN   Q CG  1 
ATOM   28855 C  CD  . GLN   Q  3  55  ? 17.607  -209.262 -7.910  1.00 137.82 ? 53  GLN   Q CD  1 
ATOM   28856 O  OE1 . GLN   Q  3  55  ? 17.514  -208.235 -7.239  1.00 138.77 ? 53  GLN   Q OE1 1 
ATOM   28857 N  NE2 . GLN   Q  3  55  ? 18.777  -209.778 -8.254  1.00 140.55 ? 53  GLN   Q NE2 1 
ATOM   28858 N  N   . ASP   Q  3  56  ? 13.777  -206.570 -8.924  1.00 137.98 ? 54  ASP   Q N   1 
ATOM   28859 C  CA  . ASP   Q  3  56  ? 13.531  -205.211 -9.478  1.00 143.05 ? 54  ASP   Q CA  1 
ATOM   28860 C  C   . ASP   Q  3  56  ? 14.900  -204.565 -9.727  1.00 144.85 ? 54  ASP   Q C   1 
ATOM   28861 O  O   . ASP   Q  3  56  ? 15.549  -204.160 -8.742  1.00 147.45 ? 54  ASP   Q O   1 
ATOM   28862 C  CB  . ASP   Q  3  56  ? 12.635  -204.397 -8.537  1.00 141.55 ? 54  ASP   Q CB  1 
ATOM   28863 C  CG  . ASP   Q  3  56  ? 12.052  -203.132 -9.148  1.00 145.24 ? 54  ASP   Q CG  1 
ATOM   28864 O  OD1 . ASP   Q  3  56  ? 12.637  -202.621 -10.127 1.00 145.18 ? 54  ASP   Q OD1 1 
ATOM   28865 O  OD2 . ASP   Q  3  56  ? 11.013  -202.663 -8.635  1.00 141.16 ? 54  ASP   Q OD2 1 
ATOM   28866 N  N   . THR   Q  3  57  ? 15.329  -204.499 -10.993 1.00 150.04 ? 55  THR   Q N   1 
ATOM   28867 C  CA  . THR   Q  3  57  ? 16.695  -204.075 -11.413 1.00 149.45 ? 55  THR   Q CA  1 
ATOM   28868 C  C   . THR   Q  3  57  ? 16.808  -202.545 -11.465 1.00 149.80 ? 55  THR   Q C   1 
ATOM   28869 O  O   . THR   Q  3  57  ? 17.945  -202.058 -11.623 1.00 146.91 ? 55  THR   Q O   1 
ATOM   28870 C  CB  . THR   Q  3  57  ? 17.086  -204.695 -12.761 1.00 151.33 ? 55  THR   Q CB  1 
ATOM   28871 O  OG1 . THR   Q  3  57  ? 15.960  -204.636 -13.636 1.00 150.86 ? 55  THR   Q OG1 1 
ATOM   28872 C  CG2 . THR   Q  3  57  ? 17.551  -206.128 -12.628 1.00 148.39 ? 55  THR   Q CG2 1 
ATOM   28873 N  N   . ARG   Q  3  58  ? 15.691  -201.817 -11.345 1.00 153.36 ? 56  ARG   Q N   1 
ATOM   28874 C  CA  . ARG   Q  3  58  ? 15.684  -200.331 -11.263 1.00 155.38 ? 56  ARG   Q CA  1 
ATOM   28875 C  C   . ARG   Q  3  58  ? 16.343  -199.897 -9.948  1.00 160.91 ? 56  ARG   Q C   1 
ATOM   28876 O  O   . ARG   Q  3  58  ? 17.176  -198.967 -9.978  1.00 166.24 ? 56  ARG   Q O   1 
ATOM   28877 C  CB  . ARG   Q  3  58  ? 14.265  -199.752 -11.289 1.00 157.97 ? 56  ARG   Q CB  1 
ATOM   28878 C  CG  . ARG   Q  3  58  ? 13.384  -200.202 -12.446 1.00 156.16 ? 56  ARG   Q CG  1 
ATOM   28879 C  CD  . ARG   Q  3  58  ? 12.001  -199.593 -12.292 1.00 158.95 ? 56  ARG   Q CD  1 
ATOM   28880 N  NE  . ARG   Q  3  58  ? 11.393  -199.977 -11.020 1.00 156.22 ? 56  ARG   Q NE  1 
ATOM   28881 C  CZ  . ARG   Q  3  58  ? 10.657  -199.186 -10.236 1.00 157.28 ? 56  ARG   Q CZ  1 
ATOM   28882 N  NH1 . ARG   Q  3  58  ? 10.416  -197.927 -10.567 1.00 158.09 ? 56  ARG   Q NH1 1 
ATOM   28883 N  NH2 . ARG   Q  3  58  ? 10.169  -199.662 -9.102  1.00 153.72 ? 56  ARG   Q NH2 1 
ATOM   28884 N  N   . ILE   Q  3  59  ? 15.978  -200.558 -8.843  1.00 157.70 ? 57  ILE   Q N   1 
ATOM   28885 C  CA  . ILE   Q  3  59  ? 16.235  -200.095 -7.445  1.00 158.11 ? 57  ILE   Q CA  1 
ATOM   28886 C  C   . ILE   Q  3  59  ? 17.316  -200.952 -6.771  1.00 161.08 ? 57  ILE   Q C   1 
ATOM   28887 O  O   . ILE   Q  3  59  ? 17.968  -200.422 -5.848  1.00 166.21 ? 57  ILE   Q O   1 
ATOM   28888 C  CB  . ILE   Q  3  59  ? 14.928  -200.077 -6.625  1.00 152.91 ? 57  ILE   Q CB  1 
ATOM   28889 C  CG1 . ILE   Q  3  59  ? 14.185  -201.415 -6.688  1.00 151.62 ? 57  ILE   Q CG1 1 
ATOM   28890 C  CG2 . ILE   Q  3  59  ? 14.047  -198.918 -7.065  1.00 153.85 ? 57  ILE   Q CG2 1 
ATOM   28891 C  CD1 . ILE   Q  3  59  ? 13.129  -201.589 -5.621  1.00 150.27 ? 57  ILE   Q CD1 1 
ATOM   28892 N  N   . THR   Q  3  60  ? 17.491  -202.213 -7.185  1.00 162.88 ? 58  THR   Q N   1 
ATOM   28893 C  CA  . THR   Q  3  60  ? 18.537  -203.126 -6.645  1.00 164.86 ? 58  THR   Q CA  1 
ATOM   28894 C  C   . THR   Q  3  60  ? 19.902  -202.459 -6.789  1.00 165.80 ? 58  THR   Q C   1 
ATOM   28895 O  O   . THR   Q  3  60  ? 20.242  -201.987 -7.872  1.00 160.48 ? 58  THR   Q O   1 
ATOM   28896 C  CB  . THR   Q  3  60  ? 18.545  -204.490 -7.346  1.00 169.16 ? 58  THR   Q CB  1 
ATOM   28897 O  OG1 . THR   Q  3  60  ? 17.333  -205.169 -7.015  1.00 172.94 ? 58  THR   Q OG1 1 
ATOM   28898 C  CG2 . THR   Q  3  60  ? 19.730  -205.344 -6.947  1.00 167.90 ? 58  THR   Q CG2 1 
ATOM   28899 N  N   . PRO   Q  3  61  ? 20.716  -202.394 -5.709  1.00 166.60 ? 59  PRO   Q N   1 
ATOM   28900 C  CA  . PRO   Q  3  61  ? 22.077  -201.863 -5.800  1.00 165.25 ? 59  PRO   Q CA  1 
ATOM   28901 C  C   . PRO   Q  3  61  ? 22.852  -202.421 -7.006  1.00 159.86 ? 59  PRO   Q C   1 
ATOM   28902 O  O   . PRO   Q  3  61  ? 22.913  -203.631 -7.146  1.00 160.28 ? 59  PRO   Q O   1 
ATOM   28903 C  CB  . PRO   Q  3  61  ? 22.716  -202.317 -4.477  1.00 166.32 ? 59  PRO   Q CB  1 
ATOM   28904 C  CG  . PRO   Q  3  61  ? 21.556  -202.382 -3.505  1.00 164.92 ? 59  PRO   Q CG  1 
ATOM   28905 C  CD  . PRO   Q  3  61  ? 20.362  -202.801 -4.339  1.00 167.22 ? 59  PRO   Q CD  1 
ATOM   28906 N  N   . SER   Q  3  62  ? 23.402  -201.536 -7.847  1.00 155.52 ? 60  SER   Q N   1 
ATOM   28907 C  CA  . SER   Q  3  62  ? 24.258  -201.891 -9.011  1.00 144.56 ? 60  SER   Q CA  1 
ATOM   28908 C  C   . SER   Q  3  62  ? 25.613  -202.397 -8.504  1.00 141.14 ? 60  SER   Q C   1 
ATOM   28909 O  O   . SER   Q  3  62  ? 26.035  -201.965 -7.412  1.00 138.04 ? 60  SER   Q O   1 
ATOM   28910 C  CB  . SER   Q  3  62  ? 24.429  -200.728 -9.953  1.00 140.53 ? 60  SER   Q CB  1 
ATOM   28911 O  OG  . SER   Q  3  62  ? 25.123  -201.132 -11.124 1.00 136.13 ? 60  SER   Q OG  1 
ATOM   28912 N  N   . LYS   Q  3  63  ? 26.269  -203.271 -9.273  1.00 136.76 ? 61  LYS   Q N   1 
ATOM   28913 C  CA  . LYS   Q  3  63  ? 27.515  -203.970 -8.853  1.00 137.08 ? 61  LYS   Q CA  1 
ATOM   28914 C  C   . LYS   Q  3  63  ? 28.713  -203.026 -9.020  1.00 128.07 ? 61  LYS   Q C   1 
ATOM   28915 O  O   . LYS   Q  3  63  ? 29.673  -203.153 -8.233  1.00 127.00 ? 61  LYS   Q O   1 
ATOM   28916 C  CB  . LYS   Q  3  63  ? 27.701  -205.271 -9.642  1.00 139.79 ? 61  LYS   Q CB  1 
ATOM   28917 C  CG  . LYS   Q  3  63  ? 28.345  -206.406 -8.855  1.00 142.34 ? 61  LYS   Q CG  1 
ATOM   28918 C  CD  . LYS   Q  3  63  ? 27.351  -207.263 -8.090  1.00 141.05 ? 61  LYS   Q CD  1 
ATOM   28919 C  CE  . LYS   Q  3  63  ? 27.925  -207.894 -6.837  1.00 136.09 ? 61  LYS   Q CE  1 
ATOM   28920 N  NZ  . LYS   Q  3  63  ? 29.192  -208.618 -7.101  1.00 133.86 ? 61  LYS   Q NZ  1 
ATOM   28921 N  N   . VAL   Q  3  64  ? 28.658  -202.120 -10.004 1.00 122.68 ? 62  VAL   Q N   1 
ATOM   28922 C  CA  . VAL   Q  3  64  ? 29.694  -201.072 -10.252 1.00 117.89 ? 62  VAL   Q CA  1 
ATOM   28923 C  C   . VAL   Q  3  64  ? 29.189  -199.748 -9.665  1.00 113.30 ? 62  VAL   Q C   1 
ATOM   28924 O  O   . VAL   Q  3  64  ? 28.086  -199.316 -10.050 1.00 112.12 ? 62  VAL   Q O   1 
ATOM   28925 C  CB  . VAL   Q  3  64  ? 30.020  -200.937 -11.753 1.00 118.37 ? 62  VAL   Q CB  1 
ATOM   28926 C  CG1 . VAL   Q  3  64  ? 31.048  -199.845 -12.016 1.00 118.57 ? 62  VAL   Q CG1 1 
ATOM   28927 C  CG2 . VAL   Q  3  64  ? 30.484  -202.257 -12.347 1.00 117.44 ? 62  VAL   Q CG2 1 
ATOM   28928 N  N   . SER   Q  3  65  ? 29.973  -199.134 -8.774  1.00 110.42 ? 63  SER   Q N   1 
ATOM   28929 C  CA  . SER   Q  3  65  ? 29.650  -197.855 -8.091  1.00 108.26 ? 63  SER   Q CA  1 
ATOM   28930 C  C   . SER   Q  3  65  ? 30.589  -196.751 -8.587  1.00 108.31 ? 63  SER   Q C   1 
ATOM   28931 O  O   . SER   Q  3  65  ? 31.774  -197.050 -8.834  1.00 107.78 ? 63  SER   Q O   1 
ATOM   28932 C  CB  . SER   Q  3  65  ? 29.735  -197.998 -6.595  1.00 106.21 ? 63  SER   Q CB  1 
ATOM   28933 O  OG  . SER   Q  3  65  ? 28.921  -199.067 -6.140  1.00 109.52 ? 63  SER   Q OG  1 
ATOM   28934 N  N   . LYS   Q  3  66  ? 30.063  -195.530 -8.729  1.00 109.68 ? 64  LYS   Q N   1 
ATOM   28935 C  CA  . LYS   Q  3  66  ? 30.856  -194.297 -8.965  1.00 108.86 ? 64  LYS   Q CA  1 
ATOM   28936 C  C   . LYS   Q  3  66  ? 31.389  -193.808 -7.613  1.00 107.06 ? 64  LYS   Q C   1 
ATOM   28937 O  O   . LYS   Q  3  66  ? 30.577  -193.673 -6.678  1.00 104.42 ? 64  LYS   Q O   1 
ATOM   28938 C  CB  . LYS   Q  3  66  ? 30.001  -193.228 -9.653  1.00 110.95 ? 64  LYS   Q CB  1 
ATOM   28939 C  CG  . LYS   Q  3  66  ? 29.727  -193.468 -11.132 1.00 111.78 ? 64  LYS   Q CG  1 
ATOM   28940 C  CD  . LYS   Q  3  66  ? 28.801  -192.440 -11.752 1.00 114.55 ? 64  LYS   Q CD  1 
ATOM   28941 C  CE  . LYS   Q  3  66  ? 29.452  -191.086 -11.948 1.00 113.00 ? 64  LYS   Q CE  1 
ATOM   28942 N  NZ  . LYS   Q  3  66  ? 28.475  -190.070 -12.401 1.00 114.12 ? 64  LYS   Q NZ  1 
ATOM   28943 N  N   . ILE   Q  3  67  ? 32.705  -193.594 -7.512  1.00 107.73 ? 65  ILE   Q N   1 
ATOM   28944 C  CA  . ILE   Q  3  67  ? 33.380  -192.992 -6.321  1.00 109.40 ? 65  ILE   Q CA  1 
ATOM   28945 C  C   . ILE   Q  3  67  ? 33.481  -191.476 -6.530  1.00 110.24 ? 65  ILE   Q C   1 
ATOM   28946 O  O   . ILE   Q  3  67  ? 33.274  -190.724 -5.559  1.00 108.91 ? 65  ILE   Q O   1 
ATOM   28947 C  CB  . ILE   Q  3  67  ? 34.762  -193.633 -6.093  1.00 107.59 ? 65  ILE   Q CB  1 
ATOM   28948 C  CG1 . ILE   Q  3  67  ? 34.665  -195.154 -5.956  1.00 107.99 ? 65  ILE   Q CG1 1 
ATOM   28949 C  CG2 . ILE   Q  3  67  ? 35.460  -193.003 -4.897  1.00 106.35 ? 65  ILE   Q CG2 1 
ATOM   28950 C  CD1 . ILE   Q  3  67  ? 33.670  -195.624 -4.917  1.00 108.44 ? 65  ILE   Q CD1 1 
ATOM   28951 N  N   . ASP   Q  3  68  ? 33.834  -191.063 -7.748  1.00 113.75 ? 66  ASP   Q N   1 
ATOM   28952 C  CA  . ASP   Q  3  68  ? 33.738  -189.664 -8.243  1.00 116.20 ? 66  ASP   Q CA  1 
ATOM   28953 C  C   . ASP   Q  3  68  ? 33.210  -189.742 -9.681  1.00 120.70 ? 66  ASP   Q C   1 
ATOM   28954 O  O   . ASP   Q  3  68  ? 32.881  -190.864 -10.123 1.00 122.60 ? 66  ASP   Q O   1 
ATOM   28955 C  CB  . ASP   Q  3  68  ? 35.089  -188.949 -8.110  1.00 116.16 ? 66  ASP   Q CB  1 
ATOM   28956 C  CG  . ASP   Q  3  68  ? 35.005  -187.456 -7.817  1.00 117.47 ? 66  ASP   Q CG  1 
ATOM   28957 O  OD1 . ASP   Q  3  68  ? 33.973  -186.842 -8.163  1.00 117.37 ? 66  ASP   Q OD1 1 
ATOM   28958 O  OD2 . ASP   Q  3  68  ? 35.981  -186.913 -7.247  1.00 109.22 ? 66  ASP   Q OD2 1 
ATOM   28959 N  N   . SER   Q  3  69  ? 33.127  -188.613 -10.389 1.00 116.43 ? 67  SER   Q N   1 
ATOM   28960 C  CA  . SER   Q  3  69  ? 32.619  -188.548 -11.784 1.00 116.69 ? 67  SER   Q CA  1 
ATOM   28961 C  C   . SER   Q  3  69  ? 33.599  -189.220 -12.760 1.00 116.71 ? 67  SER   Q C   1 
ATOM   28962 O  O   . SER   Q  3  69  ? 33.179  -189.478 -13.904 1.00 118.50 ? 67  SER   Q O   1 
ATOM   28963 C  CB  . SER   Q  3  69  ? 32.335  -187.127 -12.185 1.00 115.54 ? 67  SER   Q CB  1 
ATOM   28964 O  OG  . SER   Q  3  69  ? 33.512  -186.339 -12.097 1.00 114.25 ? 67  SER   Q OG  1 
ATOM   28965 N  N   . HIS   Q  3  70  ? 34.839  -189.507 -12.332 1.00 115.47 ? 68  HIS   Q N   1 
ATOM   28966 C  CA  . HIS   Q  3  70  ? 35.945  -190.010 -13.199 1.00 115.16 ? 68  HIS   Q CA  1 
ATOM   28967 C  C   . HIS   Q  3  70  ? 36.468  -191.391 -12.764 1.00 114.35 ? 68  HIS   Q C   1 
ATOM   28968 O  O   . HIS   Q  3  70  ? 37.239  -191.974 -13.554 1.00 115.92 ? 68  HIS   Q O   1 
ATOM   28969 C  CB  . HIS   Q  3  70  ? 37.085  -188.980 -13.261 1.00 113.71 ? 68  HIS   Q CB  1 
ATOM   28970 C  CG  . HIS   Q  3  70  ? 37.849  -188.824 -11.988 1.00 112.43 ? 68  HIS   Q CG  1 
ATOM   28971 N  ND1 . HIS   Q  3  70  ? 37.282  -188.298 -10.843 1.00 112.75 ? 68  HIS   Q ND1 1 
ATOM   28972 C  CD2 . HIS   Q  3  70  ? 39.134  -189.102 -11.677 1.00 111.94 ? 68  HIS   Q CD2 1 
ATOM   28973 C  CE1 . HIS   Q  3  70  ? 38.181  -188.274 -9.880  1.00 110.25 ? 68  HIS   Q CE1 1 
ATOM   28974 N  NE2 . HIS   Q  3  70  ? 39.325  -188.759 -10.367 1.00 109.01 ? 68  HIS   Q NE2 1 
ATOM   28975 N  N   . VAL   Q  3  71  ? 36.097  -191.900 -11.579 1.00 112.87 ? 69  VAL   Q N   1 
ATOM   28976 C  CA  . VAL   Q  3  71  ? 36.573  -193.218 -11.045 1.00 112.50 ? 69  VAL   Q CA  1 
ATOM   28977 C  C   . VAL   Q  3  71  ? 35.366  -194.091 -10.676 1.00 112.56 ? 69  VAL   Q C   1 
ATOM   28978 O  O   . VAL   Q  3  71  ? 34.375  -193.545 -10.150 1.00 109.09 ? 69  VAL   Q O   1 
ATOM   28979 C  CB  . VAL   Q  3  71  ? 37.512  -193.046 -9.834  1.00 110.16 ? 69  VAL   Q CB  1 
ATOM   28980 C  CG1 . VAL   Q  3  71  ? 38.240  -194.339 -9.494  1.00 109.49 ? 69  VAL   Q CG1 1 
ATOM   28981 C  CG2 . VAL   Q  3  71  ? 38.511  -191.920 -10.043 1.00 110.16 ? 69  VAL   Q CG2 1 
ATOM   28982 N  N   . VAL   Q  3  72  ? 35.472  -195.405 -10.912 1.00 111.84 ? 70  VAL   Q N   1 
ATOM   28983 C  CA  . VAL   Q  3  72  ? 34.427  -196.419 -10.570 1.00 113.14 ? 70  VAL   Q CA  1 
ATOM   28984 C  C   . VAL   Q  3  72  ? 35.060  -197.557 -9.761  1.00 109.60 ? 70  VAL   Q C   1 
ATOM   28985 O  O   . VAL   Q  3  72  ? 36.278  -197.791 -9.903  1.00 109.48 ? 70  VAL   Q O   1 
ATOM   28986 C  CB  . VAL   Q  3  72  ? 33.715  -196.970 -11.820 1.00 114.99 ? 70  VAL   Q CB  1 
ATOM   28987 C  CG1 . VAL   Q  3  72  ? 32.642  -196.015 -12.313 1.00 117.47 ? 70  VAL   Q CG1 1 
ATOM   28988 C  CG2 . VAL   Q  3  72  ? 34.689  -197.321 -12.935 1.00 116.27 ? 70  VAL   Q CG2 1 
ATOM   28989 N  N   . LEU   Q  3  73  ? 34.239  -198.239 -8.958  1.00 107.92 ? 71  LEU   Q N   1 
ATOM   28990 C  CA  . LEU   Q  3  73  ? 34.643  -199.372 -8.085  1.00 107.56 ? 71  LEU   Q CA  1 
ATOM   28991 C  C   . LEU   Q  3  73  ? 33.638  -200.517 -8.245  1.00 106.42 ? 71  LEU   Q C   1 
ATOM   28992 O  O   . LEU   Q  3  73  ? 32.449  -200.309 -7.937  1.00 107.85 ? 71  LEU   Q O   1 
ATOM   28993 C  CB  . LEU   Q  3  73  ? 34.698  -198.882 -6.634  1.00 105.48 ? 71  LEU   Q CB  1 
ATOM   28994 C  CG  . LEU   Q  3  73  ? 35.268  -199.874 -5.618  1.00 105.06 ? 71  LEU   Q CG  1 
ATOM   28995 C  CD1 . LEU   Q  3  73  ? 36.034  -199.150 -4.521  1.00 104.53 ? 71  LEU   Q CD1 1 
ATOM   28996 C  CD2 . LEU   Q  3  73  ? 34.172  -200.739 -5.012  1.00 104.32 ? 71  LEU   Q CD2 1 
ATOM   28997 N  N   . SER   Q  3  74  ? 34.106  -201.674 -8.717  1.00 105.97 ? 72  SER   Q N   1 
ATOM   28998 C  CA  . SER   Q  3  74  ? 33.381  -202.970 -8.660  1.00 109.15 ? 72  SER   Q CA  1 
ATOM   28999 C  C   . SER   Q  3  74  ? 34.087  -203.872 -7.646  1.00 105.33 ? 72  SER   Q C   1 
ATOM   29000 O  O   . SER   Q  3  74  ? 35.267  -203.607 -7.345  1.00 106.17 ? 72  SER   Q O   1 
ATOM   29001 C  CB  . SER   Q  3  74  ? 33.287  -203.623 -10.014 1.00 111.17 ? 72  SER   Q CB  1 
ATOM   29002 O  OG  . SER   Q  3  74  ? 34.554  -204.094 -10.449 1.00 113.10 ? 72  SER   Q OG  1 
ATOM   29003 N  N   . PHE   Q  3  75  ? 33.395  -204.897 -7.146  1.00 106.85 ? 73  PHE   Q N   1 
ATOM   29004 C  CA  . PHE   Q  3  75  ? 33.892  -205.774 -6.055  1.00 107.93 ? 73  PHE   Q CA  1 
ATOM   29005 C  C   . PHE   Q  3  75  ? 33.386  -207.211 -6.232  1.00 108.29 ? 73  PHE   Q C   1 
ATOM   29006 O  O   . PHE   Q  3  75  ? 32.468  -207.460 -7.040  1.00 110.28 ? 73  PHE   Q O   1 
ATOM   29007 C  CB  . PHE   Q  3  75  ? 33.448  -205.213 -4.703  1.00 104.13 ? 73  PHE   Q CB  1 
ATOM   29008 C  CG  . PHE   Q  3  75  ? 31.970  -205.351 -4.437  1.00 104.62 ? 73  PHE   Q CG  1 
ATOM   29009 C  CD1 . PHE   Q  3  75  ? 31.071  -204.405 -4.901  1.00 104.50 ? 73  PHE   Q CD1 1 
ATOM   29010 C  CD2 . PHE   Q  3  75  ? 31.475  -206.444 -3.740  1.00 106.98 ? 73  PHE   Q CD2 1 
ATOM   29011 C  CE1 . PHE   Q  3  75  ? 29.712  -204.541 -4.662  1.00 105.27 ? 73  PHE   Q CE1 1 
ATOM   29012 C  CE2 . PHE   Q  3  75  ? 30.116  -206.579 -3.504  1.00 106.46 ? 73  PHE   Q CE2 1 
ATOM   29013 C  CZ  . PHE   Q  3  75  ? 29.236  -205.627 -3.965  1.00 105.29 ? 73  PHE   Q CZ  1 
ATOM   29014 N  N   . SER   Q  3  76  ? 33.995  -208.127 -5.477  1.00 110.91 ? 74  SER   Q N   1 
ATOM   29015 C  CA  . SER   Q  3  76  ? 33.539  -209.523 -5.256  1.00 114.56 ? 74  SER   Q CA  1 
ATOM   29016 C  C   . SER   Q  3  76  ? 33.557  -209.812 -3.752  1.00 112.40 ? 74  SER   Q C   1 
ATOM   29017 O  O   . SER   Q  3  76  ? 34.562  -209.466 -3.098  1.00 112.18 ? 74  SER   Q O   1 
ATOM   29018 C  CB  . SER   Q  3  76  ? 34.394  -210.508 -6.013  1.00 116.23 ? 74  SER   Q CB  1 
ATOM   29019 O  OG  . SER   Q  3  76  ? 34.045  -210.536 -7.388  1.00 122.54 ? 74  SER   Q OG  1 
ATOM   29020 N  N   . GLY   Q  3  77  ? 32.480  -210.405 -3.229  1.00 112.06 ? 75  GLY   Q N   1 
ATOM   29021 C  CA  . GLY   Q  3  77  ? 32.395  -210.861 -1.829  1.00 108.93 ? 75  GLY   Q CA  1 
ATOM   29022 C  C   . GLY   Q  3  77  ? 31.121  -210.388 -1.157  1.00 106.52 ? 75  GLY   Q C   1 
ATOM   29023 O  O   . GLY   Q  3  77  ? 30.071  -210.354 -1.833  1.00 103.13 ? 75  GLY   Q O   1 
ATOM   29024 N  N   . LEU   Q  3  78  ? 31.214  -210.036 0.129   1.00 107.26 ? 76  LEU   Q N   1 
ATOM   29025 C  CA  . LEU   Q  3  78  ? 30.063  -209.618 0.972   1.00 107.93 ? 76  LEU   Q CA  1 
ATOM   29026 C  C   . LEU   Q  3  78  ? 29.587  -208.234 0.520   1.00 108.13 ? 76  LEU   Q C   1 
ATOM   29027 O  O   . LEU   Q  3  78  ? 30.396  -207.285 0.550   1.00 105.67 ? 76  LEU   Q O   1 
ATOM   29028 C  CB  . LEU   Q  3  78  ? 30.484  -209.609 2.445   1.00 107.01 ? 76  LEU   Q CB  1 
ATOM   29029 C  CG  . LEU   Q  3  78  ? 30.885  -210.964 3.026   1.00 106.43 ? 76  LEU   Q CG  1 
ATOM   29030 C  CD1 . LEU   Q  3  78  ? 31.524  -210.792 4.393   1.00 106.68 ? 76  LEU   Q CD1 1 
ATOM   29031 C  CD2 . LEU   Q  3  78  ? 29.689  -211.900 3.113   1.00 106.23 ? 76  LEU   Q CD2 1 
ATOM   29032 N  N   . ASN   Q  3  79  ? 28.318  -208.139 0.119   1.00 111.42 ? 77  ASN   Q N   1 
ATOM   29033 C  CA  . ASN   Q  3  79  ? 27.697  -206.915 -0.453  1.00 112.56 ? 77  ASN   Q CA  1 
ATOM   29034 C  C   . ASN   Q  3  79  ? 27.639  -205.823 0.620   1.00 111.34 ? 77  ASN   Q C   1 
ATOM   29035 O  O   . ASN   Q  3  79  ? 28.013  -204.678 0.312   1.00 112.72 ? 77  ASN   Q O   1 
ATOM   29036 C  CB  . ASN   Q  3  79  ? 26.307  -207.207 -1.026  1.00 115.84 ? 77  ASN   Q CB  1 
ATOM   29037 C  CG  . ASN   Q  3  79  ? 26.329  -207.913 -2.367  1.00 117.52 ? 77  ASN   Q CG  1 
ATOM   29038 O  OD1 . ASN   Q  3  79  ? 25.358  -207.837 -3.114  1.00 122.51 ? 77  ASN   Q OD1 1 
ATOM   29039 N  ND2 . ASN   Q  3  79  ? 27.413  -208.602 -2.696  1.00 119.26 ? 77  ASN   Q ND2 1 
ATOM   29040 N  N   . ALA   Q  3  80  ? 27.184  -206.170 1.828   1.00 113.49 ? 78  ALA   Q N   1 
ATOM   29041 C  CA  . ALA   Q  3  80  ? 27.028  -205.247 2.978   1.00 112.17 ? 78  ALA   Q CA  1 
ATOM   29042 C  C   . ALA   Q  3  80  ? 28.379  -204.610 3.324   1.00 111.30 ? 78  ALA   Q C   1 
ATOM   29043 O  O   . ALA   Q  3  80  ? 28.398  -203.398 3.613   1.00 116.42 ? 78  ALA   Q O   1 
ATOM   29044 C  CB  . ALA   Q  3  80  ? 26.444  -205.983 4.158   1.00 113.08 ? 78  ALA   Q CB  1 
ATOM   29045 N  N   . ASP   Q  3  81  ? 29.461  -205.396 3.292   1.00 107.67 ? 79  ASP   Q N   1 
ATOM   29046 C  CA  . ASP   Q  3  81  ? 30.848  -204.936 3.576   1.00 107.12 ? 79  ASP   Q CA  1 
ATOM   29047 C  C   . ASP   Q  3  81  ? 31.281  -203.882 2.550   1.00 105.78 ? 79  ASP   Q C   1 
ATOM   29048 O  O   . ASP   Q  3  81  ? 31.931  -202.903 2.963   1.00 107.35 ? 79  ASP   Q O   1 
ATOM   29049 C  CB  . ASP   Q  3  81  ? 31.849  -206.096 3.566   1.00 105.91 ? 79  ASP   Q CB  1 
ATOM   29050 C  CG  . ASP   Q  3  81  ? 31.957  -206.854 4.879   1.00 105.01 ? 79  ASP   Q CG  1 
ATOM   29051 O  OD1 . ASP   Q  3  81  ? 31.125  -206.608 5.776   1.00 104.26 ? 79  ASP   Q OD1 1 
ATOM   29052 O  OD2 . ASP   Q  3  81  ? 32.882  -207.685 4.997   1.00 102.41 ? 79  ASP   Q OD2 1 
ATOM   29053 N  N   . SER   Q  3  82  ? 30.953  -204.082 1.269   1.00 106.37 ? 80  SER   Q N   1 
ATOM   29054 C  CA  . SER   Q  3  82  ? 31.410  -203.228 0.139   1.00 106.76 ? 80  SER   Q CA  1 
ATOM   29055 C  C   . SER   Q  3  82  ? 30.863  -201.801 0.285   1.00 106.27 ? 80  SER   Q C   1 
ATOM   29056 O  O   . SER   Q  3  82  ? 31.581  -200.866 -0.115  1.00 105.57 ? 80  SER   Q O   1 
ATOM   29057 C  CB  . SER   Q  3  82  ? 31.042  -203.821 -1.199  1.00 108.13 ? 80  SER   Q CB  1 
ATOM   29058 O  OG  . SER   Q  3  82  ? 29.641  -203.766 -1.419  1.00 110.95 ? 80  SER   Q OG  1 
ATOM   29059 N  N   . ARG   Q  3  83  ? 29.654  -201.640 0.837   1.00 106.02 ? 81  ARG   Q N   1 
ATOM   29060 C  CA  . ARG   Q  3  83  ? 28.989  -200.318 1.018   1.00 106.40 ? 81  ARG   Q CA  1 
ATOM   29061 C  C   . ARG   Q  3  83  ? 29.833  -199.430 1.942   1.00 106.65 ? 81  ARG   Q C   1 
ATOM   29062 O  O   . ARG   Q  3  83  ? 29.901  -198.211 1.678   1.00 110.37 ? 81  ARG   Q O   1 
ATOM   29063 C  CB  . ARG   Q  3  83  ? 27.572  -200.471 1.584   1.00 107.27 ? 81  ARG   Q CB  1 
ATOM   29064 C  CG  . ARG   Q  3  83  ? 26.556  -201.015 0.590   1.00 106.90 ? 81  ARG   Q CG  1 
ATOM   29065 C  CD  . ARG   Q  3  83  ? 25.138  -200.623 0.959   1.00 107.75 ? 81  ARG   Q CD  1 
ATOM   29066 N  NE  . ARG   Q  3  83  ? 24.825  -200.935 2.348   1.00 106.55 ? 81  ARG   Q NE  1 
ATOM   29067 C  CZ  . ARG   Q  3  83  ? 24.464  -202.132 2.807   1.00 105.34 ? 81  ARG   Q CZ  1 
ATOM   29068 N  NH1 . ARG   Q  3  83  ? 24.361  -203.169 1.990   1.00 105.80 ? 81  ARG   Q NH1 1 
ATOM   29069 N  NH2 . ARG   Q  3  83  ? 24.206  -202.288 4.094   1.00 104.53 ? 81  ARG   Q NH2 1 
ATOM   29070 N  N   . ILE   Q  3  84  ? 30.440  -200.013 2.982   1.00 104.23 ? 82  ILE   Q N   1 
ATOM   29071 C  CA  . ILE   Q  3  84  ? 31.292  -199.286 3.972   1.00 101.27 ? 82  ILE   Q CA  1 
ATOM   29072 C  C   . ILE   Q  3  84  ? 32.557  -198.781 3.264   1.00 100.70 ? 82  ILE   Q C   1 
ATOM   29073 O  O   . ILE   Q  3  84  ? 32.942  -197.628 3.523   1.00 102.38 ? 82  ILE   Q O   1 
ATOM   29074 C  CB  . ILE   Q  3  84  ? 31.605  -200.160 5.207   1.00 99.27  ? 82  ILE   Q CB  1 
ATOM   29075 C  CG1 . ILE   Q  3  84  ? 30.469  -200.119 6.235   1.00 98.46  ? 82  ILE   Q CG1 1 
ATOM   29076 C  CG2 . ILE   Q  3  84  ? 32.926  -199.757 5.848   1.00 97.82  ? 82  ILE   Q CG2 1 
ATOM   29077 C  CD1 . ILE   Q  3  84  ? 29.143  -200.654 5.739   1.00 98.87  ? 82  ILE   Q CD1 1 
ATOM   29078 N  N   . LEU   Q  3  85  ? 33.174  -199.598 2.404   1.00 99.60  ? 83  LEU   Q N   1 
ATOM   29079 C  CA  . LEU   Q  3  85  ? 34.395  -199.215 1.639   1.00 101.55 ? 83  LEU   Q CA  1 
ATOM   29080 C  C   . LEU   Q  3  85  ? 34.051  -198.121 0.621   1.00 103.68 ? 83  LEU   Q C   1 
ATOM   29081 O  O   . LEU   Q  3  85  ? 34.845  -197.170 0.502   1.00 103.70 ? 83  LEU   Q O   1 
ATOM   29082 C  CB  . LEU   Q  3  85  ? 34.991  -200.437 0.933   1.00 104.04 ? 83  LEU   Q CB  1 
ATOM   29083 C  CG  . LEU   Q  3  85  ? 35.841  -201.372 1.794   1.00 105.07 ? 83  LEU   Q CG  1 
ATOM   29084 C  CD1 . LEU   Q  3  85  ? 36.406  -202.504 0.949   1.00 108.44 ? 83  LEU   Q CD1 1 
ATOM   29085 C  CD2 . LEU   Q  3  85  ? 36.971  -200.625 2.490   1.00 102.57 ? 83  LEU   Q CD2 1 
ATOM   29086 N  N   . ILE   Q  3  86  ? 32.926  -198.260 -0.090  1.00 105.79 ? 84  ILE   Q N   1 
ATOM   29087 C  CA  . ILE   Q  3  86  ? 32.460  -197.294 -1.133  1.00 108.71 ? 84  ILE   Q CA  1 
ATOM   29088 C  C   . ILE   Q  3  86  ? 32.179  -195.938 -0.474  1.00 107.89 ? 84  ILE   Q C   1 
ATOM   29089 O  O   . ILE   Q  3  86  ? 32.606  -194.913 -1.040  1.00 109.92 ? 84  ILE   Q O   1 
ATOM   29090 C  CB  . ILE   Q  3  86  ? 31.225  -197.829 -1.890  1.00 111.84 ? 84  ILE   Q CB  1 
ATOM   29091 C  CG1 . ILE   Q  3  86  ? 31.578  -199.042 -2.757  1.00 111.84 ? 84  ILE   Q CG1 1 
ATOM   29092 C  CG2 . ILE   Q  3  86  ? 30.573  -196.727 -2.717  1.00 112.07 ? 84  ILE   Q CG2 1 
ATOM   29093 C  CD1 . ILE   Q  3  86  ? 30.388  -199.896 -3.135  1.00 113.91 ? 84  ILE   Q CD1 1 
ATOM   29094 N  N   . GLU   Q  3  87  ? 31.474  -195.932 0.661   1.00 106.15 ? 85  GLU   Q N   1 
ATOM   29095 C  CA  . GLU   Q  3  87  ? 31.100  -194.693 1.394   1.00 105.33 ? 85  GLU   Q CA  1 
ATOM   29096 C  C   . GLU   Q  3  87  ? 32.374  -193.923 1.760   1.00 104.28 ? 85  GLU   Q C   1 
ATOM   29097 O  O   . GLU   Q  3  87  ? 32.461  -192.736 1.403   1.00 106.19 ? 85  GLU   Q O   1 
ATOM   29098 C  CB  . GLU   Q  3  87  ? 30.272  -195.020 2.638   1.00 107.86 ? 85  GLU   Q CB  1 
ATOM   29099 C  CG  . GLU   Q  3  87  ? 29.902  -193.797 3.460   1.00 109.05 ? 85  GLU   Q CG  1 
ATOM   29100 C  CD  . GLU   Q  3  87  ? 29.155  -192.716 2.698   1.00 113.19 ? 85  GLU   Q CD  1 
ATOM   29101 O  OE1 . GLU   Q  3  87  ? 29.306  -191.529 3.059   1.00 115.00 ? 85  GLU   Q OE1 1 
ATOM   29102 O  OE2 . GLU   Q  3  87  ? 28.422  -193.063 1.746   1.00 118.23 ? 85  GLU   Q OE2 1 
ATOM   29103 N  N   . LYS   Q  3  88  ? 33.321  -194.581 2.434   1.00 100.42 ? 86  LYS   Q N   1 
ATOM   29104 C  CA  . LYS   Q  3  88  ? 34.614  -193.983 2.865   1.00 101.20 ? 86  LYS   Q CA  1 
ATOM   29105 C  C   . LYS   Q  3  88  ? 35.380  -193.441 1.654   1.00 103.10 ? 86  LYS   Q C   1 
ATOM   29106 O  O   . LYS   Q  3  88  ? 35.951  -192.341 1.773   1.00 108.99 ? 86  LYS   Q O   1 
ATOM   29107 C  CB  . LYS   Q  3  88  ? 35.472  -195.013 3.602   1.00 100.10 ? 86  LYS   Q CB  1 
ATOM   29108 C  CG  . LYS   Q  3  88  ? 35.001  -195.341 5.009   1.00 101.09 ? 86  LYS   Q CG  1 
ATOM   29109 C  CD  . LYS   Q  3  88  ? 35.874  -196.358 5.700   1.00 101.26 ? 86  LYS   Q CD  1 
ATOM   29110 C  CE  . LYS   Q  3  88  ? 35.271  -196.864 6.991   1.00 103.33 ? 86  LYS   Q CE  1 
ATOM   29111 N  NZ  . LYS   Q  3  88  ? 35.129  -195.778 7.988   1.00 105.30 ? 86  LYS   Q NZ  1 
ATOM   29112 N  N   . ALA   Q  3  89  ? 35.404  -194.191 0.546   1.00 100.85 ? 87  ALA   Q N   1 
ATOM   29113 C  CA  . ALA   Q  3  89  ? 36.095  -193.823 -0.714  1.00 101.12 ? 87  ALA   Q CA  1 
ATOM   29114 C  C   . ALA   Q  3  89  ? 35.486  -192.534 -1.286  1.00 103.67 ? 87  ALA   Q C   1 
ATOM   29115 O  O   . ALA   Q  3  89  ? 36.261  -191.639 -1.688  1.00 103.36 ? 87  ALA   Q O   1 
ATOM   29116 C  CB  . ALA   Q  3  89  ? 36.017  -194.961 -1.704  1.00 100.49 ? 87  ALA   Q CB  1 
ATOM   29117 N  N   . ARG   Q  3  90  ? 34.151  -192.444 -1.308  1.00 102.18 ? 88  ARG   Q N   1 
ATOM   29118 C  CA  . ARG   Q  3  90  ? 33.387  -191.287 -1.852  1.00 102.66 ? 88  ARG   Q CA  1 
ATOM   29119 C  C   . ARG   Q  3  90  ? 33.619  -190.036 -0.996  1.00 101.76 ? 88  ARG   Q C   1 
ATOM   29120 O  O   . ARG   Q  3  90  ? 33.646  -188.933 -1.580  1.00 99.57  ? 88  ARG   Q O   1 
ATOM   29121 C  CB  . ARG   Q  3  90  ? 31.892  -191.612 -1.920  1.00 106.36 ? 88  ARG   Q CB  1 
ATOM   29122 C  CG  . ARG   Q  3  90  ? 31.518  -192.532 -3.071  1.00 107.74 ? 88  ARG   Q CG  1 
ATOM   29123 C  CD  . ARG   Q  3  90  ? 30.098  -193.041 -2.947  1.00 109.21 ? 88  ARG   Q CD  1 
ATOM   29124 N  NE  . ARG   Q  3  90  ? 29.596  -193.584 -4.202  1.00 107.37 ? 88  ARG   Q NE  1 
ATOM   29125 C  CZ  . ARG   Q  3  90  ? 28.466  -194.272 -4.335  1.00 105.86 ? 88  ARG   Q CZ  1 
ATOM   29126 N  NH1 . ARG   Q  3  90  ? 27.706  -194.525 -3.281  1.00 105.32 ? 88  ARG   Q NH1 1 
ATOM   29127 N  NH2 . ARG   Q  3  90  ? 28.102  -194.710 -5.528  1.00 105.73 ? 88  ARG   Q NH2 1 
ATOM   29128 N  N   . VAL   Q  3  91  ? 33.756  -190.200 0.326   1.00 98.74  ? 89  VAL   Q N   1 
ATOM   29129 C  CA  . VAL   Q  3  91  ? 34.001  -189.086 1.293   1.00 96.54  ? 89  VAL   Q CA  1 
ATOM   29130 C  C   . VAL   Q  3  91  ? 35.439  -188.589 1.118   1.00 99.42  ? 89  VAL   Q C   1 
ATOM   29131 O  O   . VAL   Q  3  91  ? 35.638  -187.359 1.155   1.00 104.29 ? 89  VAL   Q O   1 
ATOM   29132 C  CB  . VAL   Q  3  91  ? 33.719  -189.502 2.750   1.00 94.02  ? 89  VAL   Q CB  1 
ATOM   29133 C  CG1 . VAL   Q  3  91  ? 34.153  -188.431 3.739   1.00 91.84  ? 89  VAL   Q CG1 1 
ATOM   29134 C  CG2 . VAL   Q  3  91  ? 32.254  -189.844 2.963   1.00 94.62  ? 89  VAL   Q CG2 1 
ATOM   29135 N  N   . GLU   Q  3  92  ? 36.400  -189.500 0.938   1.00 96.99  ? 90  GLU   Q N   1 
ATOM   29136 C  CA  . GLU   Q  3  92  ? 37.826  -189.156 0.693   1.00 99.03  ? 90  GLU   Q CA  1 
ATOM   29137 C  C   . GLU   Q  3  92  ? 37.960  -188.452 -0.663  1.00 101.36 ? 90  GLU   Q C   1 
ATOM   29138 O  O   . GLU   Q  3  92  ? 38.828  -187.562 -0.780  1.00 100.57 ? 90  GLU   Q O   1 
ATOM   29139 C  CB  . GLU   Q  3  92  ? 38.705  -190.406 0.740   1.00 100.22 ? 90  GLU   Q CB  1 
ATOM   29140 C  CG  . GLU   Q  3  92  ? 40.182  -190.123 0.519   1.00 102.33 ? 90  GLU   Q CG  1 
ATOM   29141 C  CD  . GLU   Q  3  92  ? 40.813  -189.178 1.528   1.00 104.53 ? 90  GLU   Q CD  1 
ATOM   29142 O  OE1 . GLU   Q  3  92  ? 41.807  -188.512 1.171   1.00 108.92 ? 90  GLU   Q OE1 1 
ATOM   29143 O  OE2 . GLU   Q  3  92  ? 40.313  -189.115 2.672   1.00 105.13 ? 90  GLU   Q OE2 1 
ATOM   29144 N  N   . ALA   Q  3  93  ? 37.141  -188.844 -1.646  1.00 103.61 ? 91  ALA   Q N   1 
ATOM   29145 C  CA  . ALA   Q  3  93  ? 37.108  -188.259 -3.007  1.00 107.25 ? 91  ALA   Q CA  1 
ATOM   29146 C  C   . ALA   Q  3  93  ? 36.795  -186.759 -2.922  1.00 108.01 ? 91  ALA   Q C   1 
ATOM   29147 O  O   . ALA   Q  3  93  ? 37.480  -185.980 -3.612  1.00 110.67 ? 91  ALA   Q O   1 
ATOM   29148 C  CB  . ALA   Q  3  93  ? 36.099  -188.983 -3.866  1.00 108.07 ? 91  ALA   Q CB  1 
ATOM   29149 N  N   . GLN   Q  3  94  ? 35.802  -186.382 -2.107  1.00 108.95 ? 92  GLN   Q N   1 
ATOM   29150 C  CA  . GLN   Q  3  94  ? 35.345  -184.977 -1.924  1.00 109.04 ? 92  GLN   Q CA  1 
ATOM   29151 C  C   . GLN   Q  3  94  ? 36.350  -184.207 -1.059  1.00 109.42 ? 92  GLN   Q C   1 
ATOM   29152 O  O   . GLN   Q  3  94  ? 36.592  -183.020 -1.358  1.00 111.70 ? 92  GLN   Q O   1 
ATOM   29153 C  CB  . GLN   Q  3  94  ? 33.949  -184.937 -1.296  1.00 110.50 ? 92  GLN   Q CB  1 
ATOM   29154 C  CG  . GLN   Q  3  94  ? 32.850  -185.469 -2.206  1.00 112.04 ? 92  GLN   Q CG  1 
ATOM   29155 C  CD  . GLN   Q  3  94  ? 32.848  -184.847 -3.582  1.00 116.40 ? 92  GLN   Q CD  1 
ATOM   29156 O  OE1 . GLN   Q  3  94  ? 32.714  -185.538 -4.590  1.00 121.13 ? 92  GLN   Q OE1 1 
ATOM   29157 N  NE2 . GLN   Q  3  94  ? 32.999  -183.532 -3.640  1.00 115.12 ? 92  GLN   Q NE2 1 
ATOM   29158 N  N   . SER   Q  3  95  ? 36.903  -184.855 -0.030  1.00 106.97 ? 93  SER   Q N   1 
ATOM   29159 C  CA  . SER   Q  3  95  ? 37.904  -184.272 0.904   1.00 107.36 ? 93  SER   Q CA  1 
ATOM   29160 C  C   . SER   Q  3  95  ? 39.189  -183.915 0.149   1.00 108.29 ? 93  SER   Q C   1 
ATOM   29161 O  O   . SER   Q  3  95  ? 39.781  -182.865 0.472   1.00 109.73 ? 93  SER   Q O   1 
ATOM   29162 C  CB  . SER   Q  3  95  ? 38.195  -185.212 2.041   1.00 106.28 ? 93  SER   Q CB  1 
ATOM   29163 O  OG  . SER   Q  3  95  ? 39.107  -184.631 2.960   1.00 108.06 ? 93  SER   Q OG  1 
ATOM   29164 N  N   . HIS   Q  3  96  ? 39.611  -184.760 -0.799  1.00 105.79 ? 94  HIS   Q N   1 
ATOM   29165 C  CA  . HIS   Q  3  96  ? 40.816  -184.537 -1.642  1.00 105.67 ? 94  HIS   Q CA  1 
ATOM   29166 C  C   . HIS   Q  3  96  ? 40.604  -183.299 -2.522  1.00 107.80 ? 94  HIS   Q C   1 
ATOM   29167 O  O   . HIS   Q  3  96  ? 41.506  -182.441 -2.545  1.00 114.80 ? 94  HIS   Q O   1 
ATOM   29168 C  CB  . HIS   Q  3  96  ? 41.153  -185.773 -2.483  1.00 105.68 ? 94  HIS   Q CB  1 
ATOM   29169 C  CG  . HIS   Q  3  96  ? 42.502  -185.692 -3.114  1.00 105.61 ? 94  HIS   Q CG  1 
ATOM   29170 N  ND1 . HIS   Q  3  96  ? 42.717  -185.053 -4.320  1.00 107.45 ? 94  HIS   Q ND1 1 
ATOM   29171 C  CD2 . HIS   Q  3  96  ? 43.707  -186.146 -2.707  1.00 105.77 ? 94  HIS   Q CD2 1 
ATOM   29172 C  CE1 . HIS   Q  3  96  ? 43.994  -185.126 -4.635  1.00 107.06 ? 94  HIS   Q CE1 1 
ATOM   29173 N  NE2 . HIS   Q  3  96  ? 44.624  -185.791 -3.661  1.00 106.13 ? 94  HIS   Q NE2 1 
ATOM   29174 N  N   . ARG   Q  3  97  ? 39.453  -183.208 -3.199  1.00 104.78 ? 95  ARG   Q N   1 
ATOM   29175 C  CA  . ARG   Q  3  97  ? 39.073  -182.057 -4.066  1.00 104.69 ? 95  ARG   Q CA  1 
ATOM   29176 C  C   . ARG   Q  3  97  ? 39.109  -180.759 -3.248  1.00 104.33 ? 95  ARG   Q C   1 
ATOM   29177 O  O   . ARG   Q  3  97  ? 39.436  -179.709 -3.830  1.00 104.70 ? 95  ARG   Q O   1 
ATOM   29178 C  CB  . ARG   Q  3  97  ? 37.673  -182.250 -4.658  1.00 105.29 ? 95  ARG   Q CB  1 
ATOM   29179 C  CG  . ARG   Q  3  97  ? 37.554  -183.396 -5.651  1.00 107.03 ? 95  ARG   Q CG  1 
ATOM   29180 C  CD  . ARG   Q  3  97  ? 36.107  -183.655 -6.027  1.00 110.07 ? 95  ARG   Q CD  1 
ATOM   29181 N  NE  . ARG   Q  3  97  ? 35.679  -182.837 -7.155  1.00 112.07 ? 95  ARG   Q NE  1 
ATOM   29182 C  CZ  . ARG   Q  3  97  ? 35.632  -183.236 -8.425  1.00 115.53 ? 95  ARG   Q CZ  1 
ATOM   29183 N  NH1 . ARG   Q  3  97  ? 35.990  -184.464 -8.765  1.00 113.09 ? 95  ARG   Q NH1 1 
ATOM   29184 N  NH2 . ARG   Q  3  97  ? 35.220  -182.395 -9.359  1.00 118.63 ? 95  ARG   Q NH2 1 
ATOM   29185 N  N   . LEU   Q  3  98  ? 38.780  -180.837 -1.954  1.00 101.13 ? 96  LEU   Q N   1 
ATOM   29186 C  CA  . LEU   Q  3  98  ? 38.614  -179.672 -1.043  1.00 99.53  ? 96  LEU   Q CA  1 
ATOM   29187 C  C   . LEU   Q  3  98  ? 39.979  -179.110 -0.620  1.00 103.49 ? 96  LEU   Q C   1 
ATOM   29188 O  O   . LEU   Q  3  98  ? 40.105  -177.872 -0.585  1.00 108.65 ? 96  LEU   Q O   1 
ATOM   29189 C  CB  . LEU   Q  3  98  ? 37.796  -180.106 0.178   1.00 97.00  ? 96  LEU   Q CB  1 
ATOM   29190 C  CG  . LEU   Q  3  98  ? 37.133  -178.990 0.986   1.00 94.88  ? 96  LEU   Q CG  1 
ATOM   29191 C  CD1 . LEU   Q  3  98  ? 36.171  -178.176 0.135   1.00 97.01  ? 96  LEU   Q CD1 1 
ATOM   29192 C  CD2 . LEU   Q  3  98  ? 36.400  -179.570 2.181   1.00 92.73  ? 96  LEU   Q CD2 1 
ATOM   29193 N  N   . THR   Q  3  99  ? 40.955  -179.966 -0.298  1.00 100.28 ? 97  THR   Q N   1 
ATOM   29194 C  CA  . THR   Q  3  99  ? 42.285  -179.547 0.229   1.00 100.08 ? 97  THR   Q CA  1 
ATOM   29195 C  C   . THR   Q  3  99  ? 43.314  -179.407 -0.903  1.00 101.93 ? 97  THR   Q C   1 
ATOM   29196 O  O   . THR   Q  3  99  ? 44.076  -178.426 -0.855  1.00 103.04 ? 97  THR   Q O   1 
ATOM   29197 C  CB  . THR   Q  3  99  ? 42.779  -180.492 1.330   1.00 97.66  ? 97  THR   Q CB  1 
ATOM   29198 O  OG1 . THR   Q  3  99  ? 42.795  -181.831 0.839   1.00 100.62 ? 97  THR   Q OG1 1 
ATOM   29199 C  CG2 . THR   Q  3  99  ? 41.914  -180.430 2.568   1.00 98.02  ? 97  THR   Q CG2 1 
ATOM   29200 N  N   . LEU   Q  3  100 ? 43.353  -180.338 -1.866  1.00 103.17 ? 98  LEU   Q N   1 
ATOM   29201 C  CA  . LEU   Q  3  100 ? 44.356  -180.342 -2.972  1.00 106.39 ? 98  LEU   Q CA  1 
ATOM   29202 C  C   . LEU   Q  3  100 ? 43.851  -179.526 -4.173  1.00 102.05 ? 98  LEU   Q C   1 
ATOM   29203 O  O   . LEU   Q  3  100 ? 44.682  -179.219 -5.049  1.00 101.90 ? 98  LEU   Q O   1 
ATOM   29204 C  CB  . LEU   Q  3  100 ? 44.669  -181.783 -3.401  1.00 108.80 ? 98  LEU   Q CB  1 
ATOM   29205 C  CG  . LEU   Q  3  100 ? 45.592  -182.605 -2.495  1.00 112.80 ? 98  LEU   Q CG  1 
ATOM   29206 C  CD1 . LEU   Q  3  100 ? 46.862  -181.847 -2.135  1.00 114.10 ? 98  LEU   Q CD1 1 
ATOM   29207 C  CD2 . LEU   Q  3  100 ? 44.873  -183.067 -1.239  1.00 112.18 ? 98  LEU   Q CD2 1 
ATOM   29208 N  N   . GLU   Q  3  101 ? 42.554  -179.196 -4.222  1.00 101.23 ? 99  GLU   Q N   1 
ATOM   29209 C  CA  . GLU   Q  3  101 ? 41.894  -178.494 -5.361  1.00 103.98 ? 99  GLU   Q CA  1 
ATOM   29210 C  C   . GLU   Q  3  101 ? 42.132  -179.282 -6.657  1.00 106.19 ? 99  GLU   Q C   1 
ATOM   29211 O  O   . GLU   Q  3  101 ? 42.418  -178.657 -7.698  1.00 101.62 ? 99  GLU   Q O   1 
ATOM   29212 C  CB  . GLU   Q  3  101 ? 42.392  -177.050 -5.477  1.00 103.99 ? 99  GLU   Q CB  1 
ATOM   29213 C  CG  . GLU   Q  3  101 ? 41.934  -176.152 -4.339  1.00 103.67 ? 99  GLU   Q CG  1 
ATOM   29214 C  CD  . GLU   Q  3  101 ? 41.978  -174.659 -4.631  1.00 104.08 ? 99  GLU   Q CD  1 
ATOM   29215 O  OE1 . GLU   Q  3  101 ? 41.344  -173.894 -3.877  1.00 102.45 ? 99  GLU   Q OE1 1 
ATOM   29216 O  OE2 . GLU   Q  3  101 ? 42.648  -174.260 -5.607  1.00 106.20 ? 99  GLU   Q OE2 1 
ATOM   29217 N  N   . ASP   Q  3  102 ? 42.011  -180.611 -6.590  1.00 107.72 ? 100 ASP   Q N   1 
ATOM   29218 C  CA  . ASP   Q  3  102 ? 42.172  -181.533 -7.746  1.00 111.79 ? 100 ASP   Q CA  1 
ATOM   29219 C  C   . ASP   Q  3  102 ? 41.533  -182.869 -7.376  1.00 109.21 ? 100 ASP   Q C   1 
ATOM   29220 O  O   . ASP   Q  3  102 ? 41.736  -183.350 -6.265  1.00 105.50 ? 100 ASP   Q O   1 
ATOM   29221 C  CB  . ASP   Q  3  102 ? 43.652  -181.694 -8.118  1.00 116.26 ? 100 ASP   Q CB  1 
ATOM   29222 C  CG  . ASP   Q  3  102 ? 43.931  -181.857 -9.604  1.00 120.75 ? 100 ASP   Q CG  1 
ATOM   29223 O  OD1 . ASP   Q  3  102 ? 43.014  -181.603 -10.413 1.00 124.57 ? 100 ASP   Q OD1 1 
ATOM   29224 O  OD2 . ASP   Q  3  102 ? 45.074  -182.226 -9.943  1.00 125.44 ? 100 ASP   Q OD2 1 
ATOM   29225 N  N   . PRO   Q  3  103 ? 40.727  -183.501 -8.262  1.00 112.22 ? 101 PRO   Q N   1 
ATOM   29226 C  CA  . PRO   Q  3  103 ? 40.195  -184.836 -7.983  1.00 112.01 ? 101 PRO   Q CA  1 
ATOM   29227 C  C   . PRO   Q  3  103 ? 41.322  -185.855 -7.755  1.00 107.32 ? 101 PRO   Q C   1 
ATOM   29228 O  O   . PRO   Q  3  103 ? 42.431  -185.626 -8.214  1.00 104.68 ? 101 PRO   Q O   1 
ATOM   29229 C  CB  . PRO   Q  3  103 ? 39.368  -185.191 -9.230  1.00 114.15 ? 101 PRO   Q CB  1 
ATOM   29230 C  CG  . PRO   Q  3  103 ? 39.071  -183.857 -9.886  1.00 115.94 ? 101 PRO   Q CG  1 
ATOM   29231 C  CD  . PRO   Q  3  103 ? 40.255  -182.972 -9.552  1.00 114.36 ? 101 PRO   Q CD  1 
ATOM   29232 N  N   . VAL   Q  3  104 ? 41.015  -186.941 -7.043  1.00 105.63 ? 102 VAL   Q N   1 
ATOM   29233 C  CA  . VAL   Q  3  104 ? 41.979  -188.041 -6.738  1.00 106.14 ? 102 VAL   Q CA  1 
ATOM   29234 C  C   . VAL   Q  3  104 ? 42.488  -188.651 -8.047  1.00 108.20 ? 102 VAL   Q C   1 
ATOM   29235 O  O   . VAL   Q  3  104 ? 41.727  -188.667 -9.035  1.00 109.14 ? 102 VAL   Q O   1 
ATOM   29236 C  CB  . VAL   Q  3  104 ? 41.353  -189.131 -5.847  1.00 106.52 ? 102 VAL   Q CB  1 
ATOM   29237 C  CG1 . VAL   Q  3  104 ? 41.155  -188.640 -4.424  1.00 106.66 ? 102 VAL   Q CG1 1 
ATOM   29238 C  CG2 . VAL   Q  3  104 ? 40.052  -189.689 -6.416  1.00 107.00 ? 102 VAL   Q CG2 1 
ATOM   29239 N  N   . THR   Q  3  105 ? 43.734  -189.134 -8.041  1.00 108.81 ? 103 THR   Q N   1 
ATOM   29240 C  CA  . THR   Q  3  105 ? 44.261  -190.110 -9.031  1.00 107.80 ? 103 THR   Q CA  1 
ATOM   29241 C  C   . THR   Q  3  105 ? 43.656  -191.474 -8.688  1.00 107.34 ? 103 THR   Q C   1 
ATOM   29242 O  O   . THR   Q  3  105 ? 43.260  -191.657 -7.519  1.00 106.15 ? 103 THR   Q O   1 
ATOM   29243 C  CB  . THR   Q  3  105 ? 45.794  -190.151 -9.033  1.00 107.08 ? 103 THR   Q CB  1 
ATOM   29244 O  OG1 . THR   Q  3  105 ? 46.239  -190.583 -7.747  1.00 108.16 ? 103 THR   Q OG1 1 
ATOM   29245 C  CG2 . THR   Q  3  105 ? 46.422  -188.814 -9.357  1.00 106.69 ? 103 THR   Q CG2 1 
ATOM   29246 N  N   . VAL   Q  3  106 ? 43.581  -192.388 -9.658  1.00 108.23 ? 104 VAL   Q N   1 
ATOM   29247 C  CA  . VAL   Q  3  106 ? 43.011  -193.751 -9.448  1.00 109.21 ? 104 VAL   Q CA  1 
ATOM   29248 C  C   . VAL   Q  3  106 ? 43.933  -194.491 -8.475  1.00 105.01 ? 104 VAL   Q C   1 
ATOM   29249 O  O   . VAL   Q  3  106 ? 43.412  -195.211 -7.601  1.00 103.79 ? 104 VAL   Q O   1 
ATOM   29250 C  CB  . VAL   Q  3  106 ? 42.833  -194.525 -10.769 1.00 111.61 ? 104 VAL   Q CB  1 
ATOM   29251 C  CG1 . VAL   Q  3  106 ? 42.123  -195.852 -10.544 1.00 113.15 ? 104 VAL   Q CG1 1 
ATOM   29252 C  CG2 . VAL   Q  3  106 ? 42.092  -193.704 -11.815 1.00 114.60 ? 104 VAL   Q CG2 1 
ATOM   29253 N  N   . GLU   Q  3  107 ? 45.249  -194.292 -8.614  1.00 105.67 ? 105 GLU   Q N   1 
ATOM   29254 C  CA  . GLU   Q  3  107 ? 46.288  -194.884 -7.730  1.00 106.21 ? 105 GLU   Q CA  1 
ATOM   29255 C  C   . GLU   Q  3  107 ? 46.021  -194.448 -6.284  1.00 104.21 ? 105 GLU   Q C   1 
ATOM   29256 O  O   . GLU   Q  3  107 ? 46.000  -195.330 -5.405  1.00 102.02 ? 105 GLU   Q O   1 
ATOM   29257 C  CB  . GLU   Q  3  107 ? 47.688  -194.481 -8.202  1.00 110.44 ? 105 GLU   Q CB  1 
ATOM   29258 C  CG  . GLU   Q  3  107 ? 48.811  -195.247 -7.517  1.00 112.71 ? 105 GLU   Q CG  1 
ATOM   29259 C  CD  . GLU   Q  3  107 ? 49.231  -194.721 -6.153  1.00 113.65 ? 105 GLU   Q CD  1 
ATOM   29260 O  OE1 . GLU   Q  3  107 ? 49.570  -195.549 -5.279  1.00 115.36 ? 105 GLU   Q OE1 1 
ATOM   29261 O  OE2 . GLU   Q  3  107 ? 49.228  -193.486 -5.967  1.00 116.49 ? 105 GLU   Q OE2 1 
ATOM   29262 N  N   . TYR   Q  3  108 ? 45.808  -193.147 -6.054  1.00 103.86 ? 106 TYR   Q N   1 
ATOM   29263 C  CA  . TYR   Q  3  108 ? 45.600  -192.555 -4.704  1.00 102.72 ? 106 TYR   Q CA  1 
ATOM   29264 C  C   . TYR   Q  3  108 ? 44.318  -193.109 -4.073  1.00 100.82 ? 106 TYR   Q C   1 
ATOM   29265 O  O   . TYR   Q  3  108 ? 44.374  -193.528 -2.902  1.00 99.69  ? 106 TYR   Q O   1 
ATOM   29266 C  CB  . TYR   Q  3  108 ? 45.522  -191.026 -4.747  1.00 102.55 ? 106 TYR   Q CB  1 
ATOM   29267 C  CG  . TYR   Q  3  108 ? 45.236  -190.412 -3.399  1.00 103.21 ? 106 TYR   Q CG  1 
ATOM   29268 C  CD1 . TYR   Q  3  108 ? 43.936  -190.276 -2.937  1.00 102.62 ? 106 TYR   Q CD1 1 
ATOM   29269 C  CD2 . TYR   Q  3  108 ? 46.265  -190.011 -2.562  1.00 102.28 ? 106 TYR   Q CD2 1 
ATOM   29270 C  CE1 . TYR   Q  3  108 ? 43.664  -189.739 -1.689  1.00 100.47 ? 106 TYR   Q CE1 1 
ATOM   29271 C  CE2 . TYR   Q  3  108 ? 46.011  -189.470 -1.312  1.00 99.86  ? 106 TYR   Q CE2 1 
ATOM   29272 C  CZ  . TYR   Q  3  108 ? 44.705  -189.335 -0.872  1.00 98.85  ? 106 TYR   Q CZ  1 
ATOM   29273 O  OH  . TYR   Q  3  108 ? 44.440  -188.805 0.357   1.00 96.06  ? 106 TYR   Q OH  1 
ATOM   29274 N  N   . LEU   Q  3  109 ? 43.201  -193.067 -4.809  1.00 100.23 ? 107 LEU   Q N   1 
ATOM   29275 C  CA  . LEU   Q  3  109 ? 41.874  -193.555 -4.340  1.00 102.08 ? 107 LEU   Q CA  1 
ATOM   29276 C  C   . LEU   Q  3  109 ? 42.004  -195.035 -3.959  1.00 102.42 ? 107 LEU   Q C   1 
ATOM   29277 O  O   . LEU   Q  3  109 ? 41.471  -195.421 -2.899  1.00 103.64 ? 107 LEU   Q O   1 
ATOM   29278 C  CB  . LEU   Q  3  109 ? 40.828  -193.339 -5.442  1.00 102.86 ? 107 LEU   Q CB  1 
ATOM   29279 C  CG  . LEU   Q  3  109 ? 39.355  -193.500 -5.048  1.00 103.93 ? 107 LEU   Q CG  1 
ATOM   29280 C  CD1 . LEU   Q  3  109 ? 38.921  -194.959 -5.071  1.00 106.40 ? 107 LEU   Q CD1 1 
ATOM   29281 C  CD2 . LEU   Q  3  109 ? 39.055  -192.875 -3.693  1.00 103.07 ? 107 LEU   Q CD2 1 
ATOM   29282 N  N   . THR   Q  3  110 ? 42.703  -195.823 -4.784  1.00 103.17 ? 108 THR   Q N   1 
ATOM   29283 C  CA  . THR   Q  3  110 ? 42.994  -197.261 -4.535  1.00 102.85 ? 108 THR   Q CA  1 
ATOM   29284 C  C   . THR   Q  3  110 ? 43.846  -197.390 -3.265  1.00 99.50  ? 108 THR   Q C   1 
ATOM   29285 O  O   . THR   Q  3  110 ? 43.471  -198.199 -2.396  1.00 102.03 ? 108 THR   Q O   1 
ATOM   29286 C  CB  . THR   Q  3  110 ? 43.670  -197.925 -5.743  1.00 104.03 ? 108 THR   Q CB  1 
ATOM   29287 O  OG1 . THR   Q  3  110 ? 42.770  -197.896 -6.853  1.00 103.94 ? 108 THR   Q OG1 1 
ATOM   29288 C  CG2 . THR   Q  3  110 ? 44.071  -199.358 -5.474  1.00 103.97 ? 108 THR   Q CG2 1 
ATOM   29289 N  N   . ARG   Q  3  111 ? 44.937  -196.622 -3.164  1.00 96.61  ? 109 ARG   Q N   1 
ATOM   29290 C  CA  . ARG   Q  3  111 ? 45.892  -196.668 -2.020  1.00 94.47  ? 109 ARG   Q CA  1 
ATOM   29291 C  C   . ARG   Q  3  111 ? 45.141  -196.393 -0.712  1.00 88.75  ? 109 ARG   Q C   1 
ATOM   29292 O  O   . ARG   Q  3  111 ? 45.506  -196.999 0.311   1.00 84.99  ? 109 ARG   Q O   1 
ATOM   29293 C  CB  . ARG   Q  3  111 ? 47.042  -195.673 -2.218  1.00 96.00  ? 109 ARG   Q CB  1 
ATOM   29294 C  CG  . ARG   Q  3  111 ? 47.873  -195.414 -0.968  1.00 97.40  ? 109 ARG   Q CG  1 
ATOM   29295 C  CD  . ARG   Q  3  111 ? 49.275  -194.924 -1.283  1.00 100.62 ? 109 ARG   Q CD  1 
ATOM   29296 N  NE  . ARG   Q  3  111 ? 49.304  -193.991 -2.406  1.00 102.87 ? 109 ARG   Q NE  1 
ATOM   29297 C  CZ  . ARG   Q  3  111 ? 49.277  -192.660 -2.316  1.00 102.39 ? 109 ARG   Q CZ  1 
ATOM   29298 N  NH1 . ARG   Q  3  111 ? 49.307  -191.933 -3.420  1.00 104.57 ? 109 ARG   Q NH1 1 
ATOM   29299 N  NH2 . ARG   Q  3  111 ? 49.225  -192.053 -1.142  1.00 103.42 ? 109 ARG   Q NH2 1 
ATOM   29300 N  N   . TYR   Q  3  112 ? 44.143  -195.506 -0.740  1.00 89.08  ? 110 TYR   Q N   1 
ATOM   29301 C  CA  . TYR   Q  3  112 ? 43.307  -195.167 0.440   1.00 91.08  ? 110 TYR   Q CA  1 
ATOM   29302 C  C   . TYR   Q  3  112 ? 42.425  -196.363 0.806   1.00 89.87  ? 110 TYR   Q C   1 
ATOM   29303 O  O   . TYR   Q  3  112 ? 42.417  -196.735 1.989   1.00 90.86  ? 110 TYR   Q O   1 
ATOM   29304 C  CB  . TYR   Q  3  112 ? 42.439  -193.932 0.198   1.00 91.75  ? 110 TYR   Q CB  1 
ATOM   29305 C  CG  . TYR   Q  3  112 ? 41.431  -193.701 1.295   1.00 93.65  ? 110 TYR   Q CG  1 
ATOM   29306 C  CD1 . TYR   Q  3  112 ? 41.810  -193.150 2.508   1.00 92.96  ? 110 TYR   Q CD1 1 
ATOM   29307 C  CD2 . TYR   Q  3  112 ? 40.106  -194.078 1.139   1.00 94.34  ? 110 TYR   Q CD2 1 
ATOM   29308 C  CE1 . TYR   Q  3  112 ? 40.893  -192.953 3.528   1.00 93.18  ? 110 TYR   Q CE1 1 
ATOM   29309 C  CE2 . TYR   Q  3  112 ? 39.176  -193.887 2.148   1.00 93.07  ? 110 TYR   Q CE2 1 
ATOM   29310 C  CZ  . TYR   Q  3  112 ? 39.571  -193.323 3.347   1.00 92.80  ? 110 TYR   Q CZ  1 
ATOM   29311 O  OH  . TYR   Q  3  112 ? 38.650  -193.141 4.337   1.00 91.22  ? 110 TYR   Q OH  1 
ATOM   29312 N  N   . VAL   Q  3  113 ? 41.707  -196.927 -0.172  1.00 93.00  ? 111 VAL   Q N   1 
ATOM   29313 C  CA  . VAL   Q  3  113 ? 40.753  -198.064 0.023   1.00 94.83  ? 111 VAL   Q CA  1 
ATOM   29314 C  C   . VAL   Q  3  113 ? 41.520  -199.268 0.589   1.00 93.51  ? 111 VAL   Q C   1 
ATOM   29315 O  O   . VAL   Q  3  113 ? 40.997  -199.916 1.516   1.00 92.45  ? 111 VAL   Q O   1 
ATOM   29316 C  CB  . VAL   Q  3  113 ? 40.008  -198.426 -1.281  1.00 98.81  ? 111 VAL   Q CB  1 
ATOM   29317 C  CG1 . VAL   Q  3  113 ? 39.213  -199.718 -1.151  1.00 98.28  ? 111 VAL   Q CG1 1 
ATOM   29318 C  CG2 . VAL   Q  3  113 ? 39.096  -197.297 -1.743  1.00 100.88 ? 111 VAL   Q CG2 1 
ATOM   29319 N  N   . ALA   Q  3  114 ? 42.712  -199.546 0.051   1.00 93.07  ? 112 ALA   Q N   1 
ATOM   29320 C  CA  . ALA   Q  3  114 ? 43.612  -200.641 0.483   1.00 92.94  ? 112 ALA   Q CA  1 
ATOM   29321 C  C   . ALA   Q  3  114 ? 44.101  -200.388 1.915   1.00 95.03  ? 112 ALA   Q C   1 
ATOM   29322 O  O   . ALA   Q  3  114 ? 44.189  -201.356 2.693   1.00 92.47  ? 112 ALA   Q O   1 
ATOM   29323 C  CB  . ALA   Q  3  114 ? 44.767  -200.762 -0.478  1.00 93.07  ? 112 ALA   Q CB  1 
ATOM   29324 N  N   . GLY   Q  3  115 ? 44.417  -199.131 2.241   1.00 95.06  ? 113 GLY   Q N   1 
ATOM   29325 C  CA  . GLY   Q  3  115 ? 44.833  -198.707 3.591   1.00 95.53  ? 113 GLY   Q CA  1 
ATOM   29326 C  C   . GLY   Q  3  115 ? 43.752  -198.997 4.618   1.00 94.25  ? 113 GLY   Q C   1 
ATOM   29327 O  O   . GLY   Q  3  115 ? 44.089  -199.520 5.699   1.00 91.95  ? 113 GLY   Q O   1 
ATOM   29328 N  N   . VAL   Q  3  116 ? 42.496  -198.681 4.286   1.00 96.02  ? 114 VAL   Q N   1 
ATOM   29329 C  CA  . VAL   Q  3  116 ? 41.304  -198.942 5.148   1.00 97.40  ? 114 VAL   Q CA  1 
ATOM   29330 C  C   . VAL   Q  3  116 ? 41.239  -200.447 5.416   1.00 96.38  ? 114 VAL   Q C   1 
ATOM   29331 O  O   . VAL   Q  3  116 ? 41.153  -200.830 6.595   1.00 98.73  ? 114 VAL   Q O   1 
ATOM   29332 C  CB  . VAL   Q  3  116 ? 40.000  -198.429 4.504   1.00 99.66  ? 114 VAL   Q CB  1 
ATOM   29333 C  CG1 . VAL   Q  3  116 ? 38.766  -198.909 5.255   1.00 98.07  ? 114 VAL   Q CG1 1 
ATOM   29334 C  CG2 . VAL   Q  3  116 ? 39.986  -196.912 4.381   1.00 102.03 ? 114 VAL   Q CG2 1 
ATOM   29335 N  N   . GLN   Q  3  117 ? 41.287  -201.257 4.355   1.00 98.00  ? 115 GLN   Q N   1 
ATOM   29336 C  CA  . GLN   Q  3  117 ? 41.203  -202.742 4.428   1.00 99.54  ? 115 GLN   Q CA  1 
ATOM   29337 C  C   . GLN   Q  3  117 ? 42.298  -203.272 5.360   1.00 96.44  ? 115 GLN   Q C   1 
ATOM   29338 O  O   . GLN   Q  3  117 ? 41.966  -204.085 6.242   1.00 102.18 ? 115 GLN   Q O   1 
ATOM   29339 C  CB  . GLN   Q  3  117 ? 41.307  -203.362 3.033   1.00 101.34 ? 115 GLN   Q CB  1 
ATOM   29340 C  CG  . GLN   Q  3  117 ? 40.008  -203.285 2.243   1.00 103.03 ? 115 GLN   Q CG  1 
ATOM   29341 C  CD  . GLN   Q  3  117 ? 40.141  -203.887 0.866   1.00 106.20 ? 115 GLN   Q CD  1 
ATOM   29342 O  OE1 . GLN   Q  3  117 ? 40.693  -203.276 -0.047  1.00 105.26 ? 115 GLN   Q OE1 1 
ATOM   29343 N  NE2 . GLN   Q  3  117 ? 39.626  -205.096 0.704   1.00 110.03 ? 115 GLN   Q NE2 1 
ATOM   29344 N  N   . GLN   Q  3  118 ? 43.542  -202.818 5.176   1.00 91.18  ? 116 GLN   Q N   1 
ATOM   29345 C  CA  . GLN   Q  3  118 ? 44.719  -203.234 5.986   1.00 90.77  ? 116 GLN   Q CA  1 
ATOM   29346 C  C   . GLN   Q  3  118 ? 44.468  -202.913 7.464   1.00 89.71  ? 116 GLN   Q C   1 
ATOM   29347 O  O   . GLN   Q  3  118 ? 44.771  -203.771 8.308   1.00 85.01  ? 116 GLN   Q O   1 
ATOM   29348 C  CB  . GLN   Q  3  118 ? 45.988  -202.535 5.494   1.00 90.45  ? 116 GLN   Q CB  1 
ATOM   29349 C  CG  . GLN   Q  3  118 ? 47.274  -203.105 6.082   1.00 90.99  ? 116 GLN   Q CG  1 
ATOM   29350 C  CD  . GLN   Q  3  118 ? 47.511  -202.754 7.532   1.00 92.87  ? 116 GLN   Q CD  1 
ATOM   29351 O  OE1 . GLN   Q  3  118 ? 47.838  -203.612 8.348   1.00 92.88  ? 116 GLN   Q OE1 1 
ATOM   29352 N  NE2 . GLN   Q  3  118 ? 47.354  -201.486 7.876   1.00 94.03  ? 116 GLN   Q NE2 1 
ATOM   29353 N  N   . ARG   Q  3  119 ? 43.939  -201.723 7.765   1.00 91.69  ? 117 ARG   Q N   1 
ATOM   29354 C  CA  . ARG   Q  3  119 ? 43.698  -201.255 9.160   1.00 93.31  ? 117 ARG   Q CA  1 
ATOM   29355 C  C   . ARG   Q  3  119 ? 42.829  -202.288 9.894   1.00 92.90  ? 117 ARG   Q C   1 
ATOM   29356 O  O   . ARG   Q  3  119 ? 43.102  -202.546 11.079  1.00 92.28  ? 117 ARG   Q O   1 
ATOM   29357 C  CB  . ARG   Q  3  119 ? 43.068  -199.856 9.178   1.00 96.55  ? 117 ARG   Q CB  1 
ATOM   29358 C  CG  . ARG   Q  3  119 ? 43.501  -199.007 10.366  1.00 98.88  ? 117 ARG   Q CG  1 
ATOM   29359 C  CD  . ARG   Q  3  119 ? 42.819  -197.651 10.461  1.00 103.43 ? 117 ARG   Q CD  1 
ATOM   29360 N  NE  . ARG   Q  3  119 ? 42.869  -196.890 9.213   1.00 105.01 ? 117 ARG   Q NE  1 
ATOM   29361 C  CZ  . ARG   Q  3  119 ? 41.815  -196.458 8.514   1.00 106.60 ? 117 ARG   Q CZ  1 
ATOM   29362 N  NH1 . ARG   Q  3  119 ? 40.576  -196.687 8.924   1.00 103.90 ? 117 ARG   Q NH1 1 
ATOM   29363 N  NH2 . ARG   Q  3  119 ? 42.012  -195.780 7.395   1.00 107.05 ? 117 ARG   Q NH2 1 
ATOM   29364 N  N   . TYR   Q  3  120 ? 41.854  -202.888 9.202   1.00 93.94  ? 118 TYR   Q N   1 
ATOM   29365 C  CA  . TYR   Q  3  120 ? 40.872  -203.846 9.778   1.00 97.78  ? 118 TYR   Q CA  1 
ATOM   29366 C  C   . TYR   Q  3  120 ? 41.519  -205.225 9.994   1.00 101.55 ? 118 TYR   Q C   1 
ATOM   29367 O  O   . TYR   Q  3  120 ? 40.843  -206.110 10.569  1.00 106.34 ? 118 TYR   Q O   1 
ATOM   29368 C  CB  . TYR   Q  3  120 ? 39.622  -203.918 8.893   1.00 98.19  ? 118 TYR   Q CB  1 
ATOM   29369 C  CG  . TYR   Q  3  120 ? 38.613  -202.822 9.133   1.00 96.70  ? 118 TYR   Q CG  1 
ATOM   29370 C  CD1 . TYR   Q  3  120 ? 38.935  -201.493 8.915   1.00 95.85  ? 118 TYR   Q CD1 1 
ATOM   29371 C  CD2 . TYR   Q  3  120 ? 37.330  -203.110 9.571   1.00 97.09  ? 118 TYR   Q CD2 1 
ATOM   29372 C  CE1 . TYR   Q  3  120 ? 38.014  -200.481 9.132   1.00 97.36  ? 118 TYR   Q CE1 1 
ATOM   29373 C  CE2 . TYR   Q  3  120 ? 36.396  -202.111 9.792   1.00 95.97  ? 118 TYR   Q CE2 1 
ATOM   29374 C  CZ  . TYR   Q  3  120 ? 36.738  -200.791 9.571   1.00 95.95  ? 118 TYR   Q CZ  1 
ATOM   29375 O  OH  . TYR   Q  3  120 ? 35.812  -199.814 9.789   1.00 100.81 ? 118 TYR   Q OH  1 
ATOM   29376 N  N   . THR   Q  3  121 ? 42.777  -205.417 9.574   1.00 101.01 ? 119 THR   Q N   1 
ATOM   29377 C  CA  . THR   Q  3  121 ? 43.521  -206.699 9.732   1.00 99.99  ? 119 THR   Q CA  1 
ATOM   29378 C  C   . THR   Q  3  121 ? 44.440  -206.660 10.962  1.00 102.75 ? 119 THR   Q C   1 
ATOM   29379 O  O   . THR   Q  3  121 ? 44.862  -207.749 11.384  1.00 103.78 ? 119 THR   Q O   1 
ATOM   29380 C  CB  . THR   Q  3  121 ? 44.319  -207.075 8.476   1.00 97.76  ? 119 THR   Q CB  1 
ATOM   29381 O  OG1 . THR   Q  3  121 ? 45.405  -206.163 8.320   1.00 95.56  ? 119 THR   Q OG1 1 
ATOM   29382 C  CG2 . THR   Q  3  121 ? 43.470  -207.098 7.224   1.00 96.61  ? 119 THR   Q CG2 1 
ATOM   29383 N  N   . GLN   Q  3  122 ? 44.767  -205.482 11.511  1.00 102.50 ? 120 GLN   Q N   1 
ATOM   29384 C  CA  . GLN   Q  3  122 ? 45.524  -205.391 12.794  1.00 100.10 ? 120 GLN   Q CA  1 
ATOM   29385 C  C   . GLN   Q  3  122 ? 44.930  -204.303 13.696  1.00 96.99  ? 120 GLN   Q C   1 
ATOM   29386 O  O   . GLN   Q  3  122 ? 45.709  -203.641 14.408  1.00 95.85  ? 120 GLN   Q O   1 
ATOM   29387 C  CB  . GLN   Q  3  122 ? 47.034  -205.238 12.561  1.00 101.52 ? 120 GLN   Q CB  1 
ATOM   29388 C  CG  . GLN   Q  3  122 ? 47.488  -203.947 11.891  1.00 103.10 ? 120 GLN   Q CG  1 
ATOM   29389 C  CD  . GLN   Q  3  122 ? 48.996  -203.898 11.777  1.00 103.76 ? 120 GLN   Q CD  1 
ATOM   29390 O  OE1 . GLN   Q  3  122 ? 49.721  -204.451 12.605  1.00 96.69  ? 120 GLN   Q OE1 1 
ATOM   29391 N  NE2 . GLN   Q  3  122 ? 49.488  -203.232 10.743  1.00 106.85 ? 120 GLN   Q NE2 1 
ATOM   29392 N  N   . SER   Q  3  123 ? 43.599  -204.174 13.703  1.00 96.71  ? 121 SER   Q N   1 
ATOM   29393 C  CA  . SER   Q  3  123 ? 42.821  -203.447 14.740  1.00 94.66  ? 121 SER   Q CA  1 
ATOM   29394 C  C   . SER   Q  3  123 ? 42.095  -204.465 15.624  1.00 95.47  ? 121 SER   Q C   1 
ATOM   29395 O  O   . SER   Q  3  123 ? 41.667  -205.516 15.102  1.00 93.97  ? 121 SER   Q O   1 
ATOM   29396 C  CB  . SER   Q  3  123 ? 41.852  -202.467 14.139  1.00 93.83  ? 121 SER   Q CB  1 
ATOM   29397 O  OG  . SER   Q  3  123 ? 42.539  -201.424 13.466  1.00 92.82  ? 121 SER   Q OG  1 
ATOM   29398 N  N   . GLY   Q  3  124 ? 41.976  -204.156 16.916  1.00 95.52  ? 122 GLY   Q N   1 
ATOM   29399 C  CA  . GLY   Q  3  124 ? 41.231  -204.964 17.896  1.00 95.77  ? 122 GLY   Q CA  1 
ATOM   29400 C  C   . GLY   Q  3  124 ? 39.733  -204.803 17.710  1.00 96.75  ? 122 GLY   Q C   1 
ATOM   29401 O  O   . GLY   Q  3  124 ? 39.290  -203.678 17.410  1.00 98.02  ? 122 GLY   Q O   1 
ATOM   29402 N  N   . GLY   Q  3  125 ? 38.981  -205.896 17.849  1.00 96.22  ? 123 GLY   Q N   1 
ATOM   29403 C  CA  . GLY   Q  3  125 ? 37.509  -205.885 17.923  1.00 97.12  ? 123 GLY   Q CA  1 
ATOM   29404 C  C   . GLY   Q  3  125 ? 36.838  -205.803 16.561  1.00 98.20  ? 123 GLY   Q C   1 
ATOM   29405 O  O   . GLY   Q  3  125 ? 35.602  -205.657 16.540  1.00 99.43  ? 123 GLY   Q O   1 
ATOM   29406 N  N   . VAL   Q  3  126 ? 37.602  -205.894 15.466  1.00 98.55  ? 124 VAL   Q N   1 
ATOM   29407 C  CA  . VAL   Q  3  126 ? 37.069  -205.859 14.070  1.00 99.47  ? 124 VAL   Q CA  1 
ATOM   29408 C  C   . VAL   Q  3  126 ? 37.566  -207.096 13.310  1.00 100.48 ? 124 VAL   Q C   1 
ATOM   29409 O  O   . VAL   Q  3  126 ? 38.686  -207.576 13.614  1.00 94.92  ? 124 VAL   Q O   1 
ATOM   29410 C  CB  . VAL   Q  3  126 ? 37.456  -204.560 13.334  1.00 99.58  ? 124 VAL   Q CB  1 
ATOM   29411 C  CG1 . VAL   Q  3  126 ? 37.037  -203.319 14.105  1.00 101.00 ? 124 VAL   Q CG1 1 
ATOM   29412 C  CG2 . VAL   Q  3  126 ? 38.940  -204.496 13.008  1.00 99.05  ? 124 VAL   Q CG2 1 
ATOM   29413 N  N   . ARG   Q  3  127 ? 36.760  -207.579 12.356  1.00 101.70 ? 125 ARG   Q N   1 
ATOM   29414 C  CA  . ARG   Q  3  127 ? 37.156  -208.623 11.371  1.00 101.79 ? 125 ARG   Q CA  1 
ATOM   29415 C  C   . ARG   Q  3  127 ? 37.524  -207.938 10.058  1.00 102.35 ? 125 ARG   Q C   1 
ATOM   29416 O  O   . ARG   Q  3  127 ? 37.037  -206.845 9.770   1.00 101.77 ? 125 ARG   Q O   1 
ATOM   29417 C  CB  . ARG   Q  3  127 ? 36.051  -209.666 11.155  1.00 102.71 ? 125 ARG   Q CB  1 
ATOM   29418 C  CG  . ARG   Q  3  127 ? 34.742  -209.118 10.602  1.00 100.89 ? 125 ARG   Q CG  1 
ATOM   29419 C  CD  . ARG   Q  3  127 ? 33.904  -210.174 9.907   1.00 101.78 ? 125 ARG   Q CD  1 
ATOM   29420 N  NE  . ARG   Q  3  127 ? 32.658  -209.624 9.384   1.00 102.50 ? 125 ARG   Q NE  1 
ATOM   29421 C  CZ  . ARG   Q  3  127 ? 32.535  -208.926 8.256   1.00 102.54 ? 125 ARG   Q CZ  1 
ATOM   29422 N  NH1 . ARG   Q  3  127 ? 33.590  -208.673 7.496   1.00 101.44 ? 125 ARG   Q NH1 1 
ATOM   29423 N  NH2 . ARG   Q  3  127 ? 31.345  -208.477 7.891   1.00 104.73 ? 125 ARG   Q NH2 1 
ATOM   29424 N  N   . PRO   Q  3  128 ? 38.403  -208.549 9.233   1.00 103.41 ? 126 PRO   Q N   1 
ATOM   29425 C  CA  . PRO   Q  3  128 ? 38.731  -208.007 7.915   1.00 102.49 ? 126 PRO   Q CA  1 
ATOM   29426 C  C   . PRO   Q  3  128 ? 37.505  -207.924 6.995   1.00 101.42 ? 126 PRO   Q C   1 
ATOM   29427 O  O   . PRO   Q  3  128 ? 36.537  -208.630 7.243   1.00 103.19 ? 126 PRO   Q O   1 
ATOM   29428 C  CB  . PRO   Q  3  128 ? 39.739  -209.009 7.335   1.00 102.04 ? 126 PRO   Q CB  1 
ATOM   29429 C  CG  . PRO   Q  3  128 ? 40.300  -209.719 8.548   1.00 102.45 ? 126 PRO   Q CG  1 
ATOM   29430 C  CD  . PRO   Q  3  128 ? 39.155  -209.773 9.536   1.00 101.83 ? 126 PRO   Q CD  1 
ATOM   29431 N  N   . PHE   Q  3  129 ? 37.580  -207.070 5.970   1.00 103.83 ? 127 PHE   Q N   1 
ATOM   29432 C  CA  . PHE   Q  3  129 ? 36.539  -206.924 4.921   1.00 105.81 ? 127 PHE   Q CA  1 
ATOM   29433 C  C   . PHE   Q  3  129 ? 36.529  -208.193 4.066   1.00 104.35 ? 127 PHE   Q C   1 
ATOM   29434 O  O   . PHE   Q  3  129 ? 37.606  -208.599 3.579   1.00 100.33 ? 127 PHE   Q O   1 
ATOM   29435 C  CB  . PHE   Q  3  129 ? 36.781  -205.677 4.065   1.00 106.65 ? 127 PHE   Q CB  1 
ATOM   29436 C  CG  . PHE   Q  3  129 ? 36.438  -204.378 4.747   1.00 106.96 ? 127 PHE   Q CG  1 
ATOM   29437 C  CD1 . PHE   Q  3  129 ? 35.125  -203.936 4.813   1.00 108.64 ? 127 PHE   Q CD1 1 
ATOM   29438 C  CD2 . PHE   Q  3  129 ? 37.426  -203.598 5.328   1.00 107.50 ? 127 PHE   Q CD2 1 
ATOM   29439 C  CE1 . PHE   Q  3  129 ? 34.809  -202.741 5.442   1.00 109.19 ? 127 PHE   Q CE1 1 
ATOM   29440 C  CE2 . PHE   Q  3  129 ? 37.109  -202.404 5.957   1.00 108.20 ? 127 PHE   Q CE2 1 
ATOM   29441 C  CZ  . PHE   Q  3  129 ? 35.802  -201.977 6.012   1.00 109.95 ? 127 PHE   Q CZ  1 
ATOM   29442 N  N   . GLY   Q  3  130 ? 35.351  -208.803 3.906   1.00 107.37 ? 128 GLY   Q N   1 
ATOM   29443 C  CA  . GLY   Q  3  130 ? 35.129  -209.949 3.006   1.00 108.10 ? 128 GLY   Q CA  1 
ATOM   29444 C  C   . GLY   Q  3  130 ? 34.901  -209.466 1.587   1.00 106.95 ? 128 GLY   Q C   1 
ATOM   29445 O  O   . GLY   Q  3  130 ? 33.856  -209.814 1.002   1.00 106.09 ? 128 GLY   Q O   1 
ATOM   29446 N  N   . VAL   Q  3  131 ? 35.839  -208.667 1.069   1.00 107.24 ? 129 VAL   Q N   1 
ATOM   29447 C  CA  . VAL   Q  3  131 ? 35.715  -207.937 -0.226  1.00 108.73 ? 129 VAL   Q CA  1 
ATOM   29448 C  C   . VAL   Q  3  131 ? 37.101  -207.801 -0.867  1.00 107.61 ? 129 VAL   Q C   1 
ATOM   29449 O  O   . VAL   Q  3  131 ? 38.062  -207.460 -0.152  1.00 107.55 ? 129 VAL   Q O   1 
ATOM   29450 C  CB  . VAL   Q  3  131 ? 35.066  -206.552 -0.033  1.00 109.79 ? 129 VAL   Q CB  1 
ATOM   29451 C  CG1 . VAL   Q  3  131 ? 35.022  -205.763 -1.333  1.00 110.85 ? 129 VAL   Q CG1 1 
ATOM   29452 C  CG2 . VAL   Q  3  131 ? 33.673  -206.652 0.569   1.00 112.64 ? 129 VAL   Q CG2 1 
ATOM   29453 N  N   . SER   Q  3  132 ? 37.178  -208.072 -2.171  1.00 108.88 ? 130 SER   Q N   1 
ATOM   29454 C  CA  . SER   Q  3  132 ? 38.246  -207.608 -3.092  1.00 112.45 ? 130 SER   Q CA  1 
ATOM   29455 C  C   . SER   Q  3  132 ? 37.606  -206.614 -4.064  1.00 110.23 ? 130 SER   Q C   1 
ATOM   29456 O  O   . SER   Q  3  132 ? 36.421  -206.805 -4.398  1.00 113.40 ? 130 SER   Q O   1 
ATOM   29457 C  CB  . SER   Q  3  132 ? 38.895  -208.758 -3.819  1.00 113.64 ? 130 SER   Q CB  1 
ATOM   29458 O  OG  . SER   Q  3  132 ? 39.662  -209.554 -2.931  1.00 118.67 ? 130 SER   Q OG  1 
ATOM   29459 N  N   . THR   Q  3  133 ? 38.339  -205.581 -4.476  1.00 108.27 ? 131 THR   Q N   1 
ATOM   29460 C  CA  . THR   Q  3  133 ? 37.808  -204.505 -5.351  1.00 110.24 ? 131 THR   Q CA  1 
ATOM   29461 C  C   . THR   Q  3  133 ? 38.621  -204.426 -6.644  1.00 106.39 ? 131 THR   Q C   1 
ATOM   29462 O  O   . THR   Q  3  133 ? 39.839  -204.682 -6.601  1.00 102.31 ? 131 THR   Q O   1 
ATOM   29463 C  CB  . THR   Q  3  133 ? 37.791  -203.154 -4.626  1.00 110.82 ? 131 THR   Q CB  1 
ATOM   29464 O  OG1 . THR   Q  3  133 ? 39.136  -202.794 -4.306  1.00 113.82 ? 131 THR   Q OG1 1 
ATOM   29465 C  CG2 . THR   Q  3  133 ? 36.954  -203.173 -3.366  1.00 111.38 ? 131 THR   Q CG2 1 
ATOM   29466 N  N   . LEU   Q  3  134 ? 37.939  -204.105 -7.745  1.00 107.66 ? 132 LEU   Q N   1 
ATOM   29467 C  CA  . LEU   Q  3  134 ? 38.534  -203.553 -8.987  1.00 111.38 ? 132 LEU   Q CA  1 
ATOM   29468 C  C   . LEU   Q  3  134 ? 38.193  -202.063 -9.039  1.00 110.43 ? 132 LEU   Q C   1 
ATOM   29469 O  O   . LEU   Q  3  134 ? 36.988  -201.738 -9.016  1.00 112.33 ? 132 LEU   Q O   1 
ATOM   29470 C  CB  . LEU   Q  3  134 ? 37.961  -204.280 -10.205 1.00 111.62 ? 132 LEU   Q CB  1 
ATOM   29471 C  CG  . LEU   Q  3  134 ? 38.244  -205.776 -10.281 1.00 114.03 ? 132 LEU   Q CG  1 
ATOM   29472 C  CD1 . LEU   Q  3  134 ? 37.414  -206.417 -11.383 1.00 117.50 ? 132 LEU   Q CD1 1 
ATOM   29473 C  CD2 . LEU   Q  3  134 ? 39.727  -206.040 -10.496 1.00 114.05 ? 132 LEU   Q CD2 1 
ATOM   29474 N  N   . ILE   Q  3  135 ? 39.211  -201.201 -9.080  1.00 109.41 ? 133 ILE   Q N   1 
ATOM   29475 C  CA  . ILE   Q  3  135 ? 39.051  -199.719 -9.148  1.00 108.53 ? 133 ILE   Q CA  1 
ATOM   29476 C  C   . ILE   Q  3  135 ? 39.642  -199.239 -10.475 1.00 109.22 ? 133 ILE   Q C   1 
ATOM   29477 O  O   . ILE   Q  3  135 ? 40.845  -199.467 -10.703 1.00 112.80 ? 133 ILE   Q O   1 
ATOM   29478 C  CB  . ILE   Q  3  135 ? 39.704  -199.037 -7.932  1.00 106.76 ? 133 ILE   Q CB  1 
ATOM   29479 C  CG1 . ILE   Q  3  135 ? 39.057  -199.507 -6.626  1.00 106.46 ? 133 ILE   Q CG1 1 
ATOM   29480 C  CG2 . ILE   Q  3  135 ? 39.655  -197.524 -8.074  1.00 107.29 ? 133 ILE   Q CG2 1 
ATOM   29481 C  CD1 . ILE   Q  3  135 ? 39.843  -199.164 -5.383  1.00 105.63 ? 133 ILE   Q CD1 1 
ATOM   29482 N  N   . ALA   Q  3  136 ? 38.814  -198.606 -11.308 1.00 108.78 ? 134 ALA   Q N   1 
ATOM   29483 C  CA  . ALA   Q  3  136 ? 39.154  -198.193 -12.688 1.00 112.82 ? 134 ALA   Q CA  1 
ATOM   29484 C  C   . ALA   Q  3  136 ? 38.738  -196.737 -12.914 1.00 111.69 ? 134 ALA   Q C   1 
ATOM   29485 O  O   . ALA   Q  3  136 ? 37.745  -196.294 -12.300 1.00 110.10 ? 134 ALA   Q O   1 
ATOM   29486 C  CB  . ALA   Q  3  136 ? 38.485  -199.116 -13.675 1.00 114.84 ? 134 ALA   Q CB  1 
ATOM   29487 N  N   . GLY   Q  3  137 ? 39.476  -196.030 -13.773 1.00 113.12 ? 135 GLY   Q N   1 
ATOM   29488 C  CA  . GLY   Q  3  137 ? 39.186  -194.635 -14.151 1.00 115.56 ? 135 GLY   Q CA  1 
ATOM   29489 C  C   . GLY   Q  3  137 ? 40.351  -193.981 -14.870 1.00 117.14 ? 135 GLY   Q C   1 
ATOM   29490 O  O   . GLY   Q  3  137 ? 41.217  -194.714 -15.394 1.00 118.35 ? 135 GLY   Q O   1 
ATOM   29491 N  N   . PHE   Q  3  138 ? 40.360  -192.645 -14.892 1.00 117.79 ? 136 PHE   Q N   1 
ATOM   29492 C  CA  . PHE   Q  3  138 ? 41.388  -191.796 -15.547 1.00 118.34 ? 136 PHE   Q CA  1 
ATOM   29493 C  C   . PHE   Q  3  138 ? 41.759  -190.643 -14.614 1.00 117.98 ? 136 PHE   Q C   1 
ATOM   29494 O  O   . PHE   Q  3  138 ? 40.840  -189.978 -14.104 1.00 120.19 ? 136 PHE   Q O   1 
ATOM   29495 C  CB  . PHE   Q  3  138 ? 40.861  -191.258 -16.877 1.00 118.64 ? 136 PHE   Q CB  1 
ATOM   29496 C  CG  . PHE   Q  3  138 ? 40.717  -192.300 -17.955 1.00 121.51 ? 136 PHE   Q CG  1 
ATOM   29497 C  CD1 . PHE   Q  3  138 ? 39.560  -193.055 -18.061 1.00 124.09 ? 136 PHE   Q CD1 1 
ATOM   29498 C  CD2 . PHE   Q  3  138 ? 41.742  -192.529 -18.859 1.00 123.09 ? 136 PHE   Q CD2 1 
ATOM   29499 C  CE1 . PHE   Q  3  138 ? 39.431  -194.017 -19.052 1.00 126.53 ? 136 PHE   Q CE1 1 
ATOM   29500 C  CE2 . PHE   Q  3  138 ? 41.610  -193.488 -19.851 1.00 124.65 ? 136 PHE   Q CE2 1 
ATOM   29501 C  CZ  . PHE   Q  3  138 ? 40.456  -194.230 -19.945 1.00 126.44 ? 136 PHE   Q CZ  1 
ATOM   29502 N  N   . ASP   Q  3  139 ? 43.060  -190.412 -14.413 1.00 119.33 ? 137 ASP   Q N   1 
ATOM   29503 C  CA  . ASP   Q  3  139 ? 43.589  -189.281 -13.605 1.00 118.77 ? 137 ASP   Q CA  1 
ATOM   29504 C  C   . ASP   Q  3  139 ? 43.128  -187.970 -14.239 1.00 117.88 ? 137 ASP   Q C   1 
ATOM   29505 O  O   . ASP   Q  3  139 ? 42.969  -187.895 -15.456 1.00 119.82 ? 137 ASP   Q O   1 
ATOM   29506 C  CB  . ASP   Q  3  139 ? 45.115  -189.336 -13.493 1.00 119.83 ? 137 ASP   Q CB  1 
ATOM   29507 C  CG  . ASP   Q  3  139 ? 45.644  -190.555 -12.754 1.00 118.31 ? 137 ASP   Q CG  1 
ATOM   29508 O  OD1 . ASP   Q  3  139 ? 44.824  -191.290 -12.169 1.00 121.33 ? 137 ASP   Q OD1 1 
ATOM   29509 O  OD2 . ASP   Q  3  139 ? 46.873  -190.758 -12.771 1.00 120.04 ? 137 ASP   Q OD2 1 
ATOM   29510 N  N   . PRO   Q  3  140 ? 42.873  -186.907 -13.441 1.00 116.56 ? 138 PRO   Q N   1 
ATOM   29511 C  CA  . PRO   Q  3  140 ? 42.526  -185.597 -13.991 1.00 115.18 ? 138 PRO   Q CA  1 
ATOM   29512 C  C   . PRO   Q  3  140 ? 43.469  -185.157 -15.122 1.00 116.81 ? 138 PRO   Q C   1 
ATOM   29513 O  O   . PRO   Q  3  140 ? 44.672  -185.265 -14.949 1.00 115.94 ? 138 PRO   Q O   1 
ATOM   29514 C  CB  . PRO   Q  3  140 ? 42.664  -184.666 -12.778 1.00 113.39 ? 138 PRO   Q CB  1 
ATOM   29515 C  CG  . PRO   Q  3  140 ? 42.327  -185.549 -11.601 1.00 112.48 ? 138 PRO   Q CG  1 
ATOM   29516 C  CD  . PRO   Q  3  140 ? 42.868  -186.915 -11.970 1.00 113.95 ? 138 PRO   Q CD  1 
ATOM   29517 N  N   . ARG   Q  3  141 ? 42.897  -184.701 -16.243 1.00 118.95 ? 139 ARG   Q N   1 
ATOM   29518 C  CA  . ARG   Q  3  141 ? 43.628  -184.175 -17.429 1.00 121.92 ? 139 ARG   Q CA  1 
ATOM   29519 C  C   . ARG   Q  3  141 ? 44.609  -185.233 -17.954 1.00 124.83 ? 139 ARG   Q C   1 
ATOM   29520 O  O   . ARG   Q  3  141 ? 45.719  -184.849 -18.377 1.00 121.84 ? 139 ARG   Q O   1 
ATOM   29521 C  CB  . ARG   Q  3  141 ? 44.375  -182.888 -17.063 1.00 122.68 ? 139 ARG   Q CB  1 
ATOM   29522 C  CG  . ARG   Q  3  141 ? 43.494  -181.790 -16.487 1.00 122.66 ? 139 ARG   Q CG  1 
ATOM   29523 C  CD  . ARG   Q  3  141 ? 44.321  -180.626 -15.977 1.00 124.81 ? 139 ARG   Q CD  1 
ATOM   29524 N  NE  . ARG   Q  3  141 ? 45.268  -181.046 -14.951 1.00 123.94 ? 139 ARG   Q NE  1 
ATOM   29525 C  CZ  . ARG   Q  3  141 ? 44.955  -181.323 -13.686 1.00 125.11 ? 139 ARG   Q CZ  1 
ATOM   29526 N  NH1 . ARG   Q  3  141 ? 43.703  -181.232 -13.264 1.00 125.11 ? 139 ARG   Q NH1 1 
ATOM   29527 N  NH2 . ARG   Q  3  141 ? 45.903  -181.694 -12.841 1.00 125.45 ? 139 ARG   Q NH2 1 
ATOM   29528 N  N   . ASP   Q  3  142 ? 44.216  -186.511 -17.926 1.00 125.92 ? 140 ASP   Q N   1 
ATOM   29529 C  CA  . ASP   Q  3  142 ? 45.044  -187.659 -18.385 1.00 130.22 ? 140 ASP   Q CA  1 
ATOM   29530 C  C   . ASP   Q  3  142 ? 44.153  -188.638 -19.158 1.00 132.22 ? 140 ASP   Q C   1 
ATOM   29531 O  O   . ASP   Q  3  142 ? 42.997  -188.844 -18.733 1.00 133.96 ? 140 ASP   Q O   1 
ATOM   29532 C  CB  . ASP   Q  3  142 ? 45.741  -188.346 -17.207 1.00 130.80 ? 140 ASP   Q CB  1 
ATOM   29533 C  CG  . ASP   Q  3  142 ? 46.794  -189.366 -17.609 1.00 133.19 ? 140 ASP   Q CG  1 
ATOM   29534 O  OD1 . ASP   Q  3  142 ? 47.636  -189.034 -18.470 1.00 134.50 ? 140 ASP   Q OD1 1 
ATOM   29535 O  OD2 . ASP   Q  3  142 ? 46.764  -190.487 -17.058 1.00 130.73 ? 140 ASP   Q OD2 1 
ATOM   29536 N  N   . ASP   Q  3  143 ? 44.682  -189.218 -20.241 1.00 135.60 ? 141 ASP   Q N   1 
ATOM   29537 C  CA  . ASP   Q  3  143 ? 43.938  -190.114 -21.169 1.00 137.56 ? 141 ASP   Q CA  1 
ATOM   29538 C  C   . ASP   Q  3  143 ? 44.470  -191.552 -21.077 1.00 138.67 ? 141 ASP   Q C   1 
ATOM   29539 O  O   . ASP   Q  3  143 ? 43.966  -192.400 -21.840 1.00 140.80 ? 141 ASP   Q O   1 
ATOM   29540 C  CB  . ASP   Q  3  143 ? 43.991  -189.588 -22.608 1.00 139.47 ? 141 ASP   Q CB  1 
ATOM   29541 C  CG  . ASP   Q  3  143 ? 45.384  -189.265 -23.123 1.00 139.55 ? 141 ASP   Q CG  1 
ATOM   29542 O  OD1 . ASP   Q  3  143 ? 46.366  -189.611 -22.435 1.00 137.61 ? 141 ASP   Q OD1 1 
ATOM   29543 O  OD2 . ASP   Q  3  143 ? 45.476  -188.661 -24.208 1.00 142.03 ? 141 ASP   Q OD2 1 
ATOM   29544 N  N   . GLU   Q  3  144 ? 45.434  -191.825 -20.189 1.00 137.15 ? 142 GLU   Q N   1 
ATOM   29545 C  CA  . GLU   Q  3  144 ? 45.993  -193.187 -19.970 1.00 135.92 ? 142 GLU   Q CA  1 
ATOM   29546 C  C   . GLU   Q  3  144 ? 45.037  -193.973 -19.074 1.00 133.93 ? 142 GLU   Q C   1 
ATOM   29547 O  O   . GLU   Q  3  144 ? 44.720  -193.526 -17.974 1.00 129.18 ? 142 GLU   Q O   1 
ATOM   29548 C  CB  . GLU   Q  3  144 ? 47.390  -193.122 -19.351 1.00 140.90 ? 142 GLU   Q CB  1 
ATOM   29549 C  CG  . GLU   Q  3  144 ? 48.119  -194.455 -19.375 1.00 144.74 ? 142 GLU   Q CG  1 
ATOM   29550 C  CD  . GLU   Q  3  144 ? 49.320  -194.542 -18.449 1.00 147.00 ? 142 GLU   Q CD  1 
ATOM   29551 O  OE1 . GLU   Q  3  144 ? 49.466  -195.579 -17.771 1.00 150.38 ? 142 GLU   Q OE1 1 
ATOM   29552 O  OE2 . GLU   Q  3  144 ? 50.110  -193.577 -18.413 1.00 152.79 ? 142 GLU   Q OE2 1 
ATOM   29553 N  N   . PRO   Q  3  145 ? 44.548  -195.159 -19.508 1.00 133.21 ? 143 PRO   Q N   1 
ATOM   29554 C  CA  . PRO   Q  3  145 ? 43.629  -195.955 -18.694 1.00 131.78 ? 143 PRO   Q CA  1 
ATOM   29555 C  C   . PRO   Q  3  145 ? 44.315  -196.502 -17.432 1.00 127.67 ? 143 PRO   Q C   1 
ATOM   29556 O  O   . PRO   Q  3  145 ? 45.504  -196.776 -17.480 1.00 131.37 ? 143 PRO   Q O   1 
ATOM   29557 C  CB  . PRO   Q  3  145 ? 43.183  -197.105 -19.617 1.00 134.05 ? 143 PRO   Q CB  1 
ATOM   29558 C  CG  . PRO   Q  3  145 ? 43.634  -196.694 -21.008 1.00 133.82 ? 143 PRO   Q CG  1 
ATOM   29559 C  CD  . PRO   Q  3  145 ? 44.841  -195.806 -20.796 1.00 133.11 ? 143 PRO   Q CD  1 
ATOM   29560 N  N   . LYS   Q  3  146 ? 43.553  -196.636 -16.343 1.00 120.56 ? 144 LYS   Q N   1 
ATOM   29561 C  CA  . LYS   Q  3  146 ? 44.039  -197.124 -15.025 1.00 115.37 ? 144 LYS   Q CA  1 
ATOM   29562 C  C   . LYS   Q  3  146 ? 43.084  -198.196 -14.497 1.00 110.61 ? 144 LYS   Q C   1 
ATOM   29563 O  O   . LYS   Q  3  146 ? 41.881  -197.901 -14.371 1.00 103.26 ? 144 LYS   Q O   1 
ATOM   29564 C  CB  . LYS   Q  3  146 ? 44.124  -195.971 -14.022 1.00 115.16 ? 144 LYS   Q CB  1 
ATOM   29565 C  CG  . LYS   Q  3  146 ? 44.956  -194.777 -14.469 1.00 116.56 ? 144 LYS   Q CG  1 
ATOM   29566 C  CD  . LYS   Q  3  146 ? 46.443  -195.008 -14.358 1.00 117.35 ? 144 LYS   Q CD  1 
ATOM   29567 C  CE  . LYS   Q  3  146 ? 47.250  -193.810 -14.805 1.00 117.73 ? 144 LYS   Q CE  1 
ATOM   29568 N  NZ  . LYS   Q  3  146 ? 48.655  -193.899 -14.347 1.00 118.05 ? 144 LYS   Q NZ  1 
ATOM   29569 N  N   . LEU   Q  3  147 ? 43.611  -199.389 -14.211 1.00 112.04 ? 145 LEU   Q N   1 
ATOM   29570 C  CA  . LEU   Q  3  147 ? 42.889  -200.494 -13.528 1.00 110.76 ? 145 LEU   Q CA  1 
ATOM   29571 C  C   . LEU   Q  3  147 ? 43.745  -200.954 -12.346 1.00 107.42 ? 145 LEU   Q C   1 
ATOM   29572 O  O   . LEU   Q  3  147 ? 44.942  -201.228 -12.554 1.00 105.45 ? 145 LEU   Q O   1 
ATOM   29573 C  CB  . LEU   Q  3  147 ? 42.630  -201.635 -14.518 1.00 112.08 ? 145 LEU   Q CB  1 
ATOM   29574 C  CG  . LEU   Q  3  147 ? 41.923  -202.865 -13.944 1.00 114.00 ? 145 LEU   Q CG  1 
ATOM   29575 C  CD1 . LEU   Q  3  147 ? 40.449  -202.581 -13.692 1.00 112.00 ? 145 LEU   Q CD1 1 
ATOM   29576 C  CD2 . LEU   Q  3  147 ? 42.084  -204.066 -14.865 1.00 114.28 ? 145 LEU   Q CD2 1 
ATOM   29577 N  N   . TYR   Q  3  148 ? 43.150  -201.002 -11.153 1.00 107.46 ? 146 TYR   Q N   1 
ATOM   29578 C  CA  . TYR   Q  3  148 ? 43.793  -201.470 -9.899  1.00 110.27 ? 146 TYR   Q CA  1 
ATOM   29579 C  C   . TYR   Q  3  148 ? 42.896  -202.509 -9.223  1.00 112.19 ? 146 TYR   Q C   1 
ATOM   29580 O  O   . TYR   Q  3  148 ? 41.663  -202.468 -9.410  1.00 117.24 ? 146 TYR   Q O   1 
ATOM   29581 C  CB  . TYR   Q  3  148 ? 44.065  -200.295 -8.958  1.00 108.63 ? 146 TYR   Q CB  1 
ATOM   29582 C  CG  . TYR   Q  3  148 ? 45.303  -199.500 -9.287  1.00 108.89 ? 146 TYR   Q CG  1 
ATOM   29583 C  CD1 . TYR   Q  3  148 ? 45.256  -198.430 -10.167 1.00 107.70 ? 146 TYR   Q CD1 1 
ATOM   29584 C  CD2 . TYR   Q  3  148 ? 46.525  -199.818 -8.717  1.00 106.62 ? 146 TYR   Q CD2 1 
ATOM   29585 C  CE1 . TYR   Q  3  148 ? 46.392  -197.698 -10.473 1.00 105.30 ? 146 TYR   Q CE1 1 
ATOM   29586 C  CE2 . TYR   Q  3  148 ? 47.669  -199.096 -9.011  1.00 104.63 ? 146 TYR   Q CE2 1 
ATOM   29587 C  CZ  . TYR   Q  3  148 ? 47.603  -198.032 -9.893  1.00 103.29 ? 146 TYR   Q CZ  1 
ATOM   29588 O  OH  . TYR   Q  3  148 ? 48.732  -197.325 -10.180 1.00 102.75 ? 146 TYR   Q OH  1 
ATOM   29589 N  N   . GLN   Q  3  149 ? 43.517  -203.412 -8.461  1.00 113.87 ? 147 GLN   Q N   1 
ATOM   29590 C  CA  . GLN   Q  3  149 ? 42.840  -204.468 -7.666  1.00 114.21 ? 147 GLN   Q CA  1 
ATOM   29591 C  C   . GLN   Q  3  149 ? 43.317  -204.355 -6.216  1.00 110.49 ? 147 GLN   Q C   1 
ATOM   29592 O  O   . GLN   Q  3  149 ? 44.527  -204.146 -6.021  1.00 108.95 ? 147 GLN   Q O   1 
ATOM   29593 C  CB  . GLN   Q  3  149 ? 43.165  -205.852 -8.232  1.00 118.65 ? 147 GLN   Q CB  1 
ATOM   29594 C  CG  . GLN   Q  3  149 ? 42.286  -206.965 -7.673  1.00 119.77 ? 147 GLN   Q CG  1 
ATOM   29595 C  CD  . GLN   Q  3  149 ? 43.068  -208.131 -7.116  1.00 119.89 ? 147 GLN   Q CD  1 
ATOM   29596 O  OE1 . GLN   Q  3  149 ? 42.806  -208.599 -6.010  1.00 120.68 ? 147 GLN   Q OE1 1 
ATOM   29597 N  NE2 . GLN   Q  3  149 ? 44.036  -208.615 -7.877  1.00 118.59 ? 147 GLN   Q NE2 1 
ATOM   29598 N  N   . THR   Q  3  150 ? 42.403  -204.473 -5.250  1.00 107.99 ? 148 THR   Q N   1 
ATOM   29599 C  CA  . THR   Q  3  150 ? 42.718  -204.587 -3.799  1.00 109.07 ? 148 THR   Q CA  1 
ATOM   29600 C  C   . THR   Q  3  150 ? 42.147  -205.908 -3.277  1.00 107.73 ? 148 THR   Q C   1 
ATOM   29601 O  O   . THR   Q  3  150 ? 41.315  -206.511 -3.984  1.00 109.34 ? 148 THR   Q O   1 
ATOM   29602 C  CB  . THR   Q  3  150 ? 42.182  -203.394 -2.995  1.00 107.15 ? 148 THR   Q CB  1 
ATOM   29603 O  OG1 . THR   Q  3  150 ? 40.782  -203.574 -2.783  1.00 108.77 ? 148 THR   Q OG1 1 
ATOM   29604 C  CG2 . THR   Q  3  150 ? 42.432  -202.063 -3.670  1.00 106.90 ? 148 THR   Q CG2 1 
ATOM   29605 N  N   . GLU   Q  3  151 ? 42.582  -206.335 -2.090  1.00 108.88 ? 149 GLU   Q N   1 
ATOM   29606 C  CA  . GLU   Q  3  151 ? 42.101  -207.583 -1.441  1.00 110.26 ? 149 GLU   Q CA  1 
ATOM   29607 C  C   . GLU   Q  3  151 ? 42.186  -207.432 0.077   1.00 109.33 ? 149 GLU   Q C   1 
ATOM   29608 O  O   . GLU   Q  3  151 ? 42.885  -206.550 0.575   1.00 107.16 ? 149 GLU   Q O   1 
ATOM   29609 C  CB  . GLU   Q  3  151 ? 42.880  -208.781 -1.993  1.00 115.17 ? 149 GLU   Q CB  1 
ATOM   29610 C  CG  . GLU   Q  3  151 ? 44.321  -208.875 -1.522  1.00 118.13 ? 149 GLU   Q CG  1 
ATOM   29611 C  CD  . GLU   Q  3  151 ? 45.098  -210.015 -2.161  1.00 122.86 ? 149 GLU   Q CD  1 
ATOM   29612 O  OE1 . GLU   Q  3  151 ? 45.652  -210.848 -1.409  1.00 126.22 ? 149 GLU   Q OE1 1 
ATOM   29613 O  OE2 . GLU   Q  3  151 ? 45.147  -210.071 -3.410  1.00 122.59 ? 149 GLU   Q OE2 1 
ATOM   29614 N  N   . PRO   Q  3  152 ? 41.464  -208.284 0.847   1.00 107.60 ? 150 PRO   Q N   1 
ATOM   29615 C  CA  . PRO   Q  3  152 ? 41.295  -208.104 2.294   1.00 105.87 ? 150 PRO   Q CA  1 
ATOM   29616 C  C   . PRO   Q  3  152 ? 42.566  -207.839 3.117   1.00 105.06 ? 150 PRO   Q C   1 
ATOM   29617 O  O   . PRO   Q  3  152 ? 42.474  -207.111 4.097   1.00 99.99  ? 150 PRO   Q O   1 
ATOM   29618 C  CB  . PRO   Q  3  152 ? 40.698  -209.447 2.736   1.00 106.35 ? 150 PRO   Q CB  1 
ATOM   29619 C  CG  . PRO   Q  3  152 ? 39.907  -209.903 1.536   1.00 107.10 ? 150 PRO   Q CG  1 
ATOM   29620 C  CD  . PRO   Q  3  152 ? 40.740  -209.466 0.351   1.00 107.55 ? 150 PRO   Q CD  1 
ATOM   29621 N  N   . SER   Q  3  153 ? 43.694  -208.443 2.723   1.00 105.23 ? 151 SER   Q N   1 
ATOM   29622 C  CA  . SER   Q  3  153 ? 45.020  -208.287 3.380   1.00 103.26 ? 151 SER   Q CA  1 
ATOM   29623 C  C   . SER   Q  3  153 ? 45.416  -206.807 3.402   1.00 102.43 ? 151 SER   Q C   1 
ATOM   29624 O  O   . SER   Q  3  153 ? 45.948  -206.356 4.436   1.00 101.80 ? 151 SER   Q O   1 
ATOM   29625 C  CB  . SER   Q  3  153 ? 46.079  -209.122 2.702   1.00 103.43 ? 151 SER   Q CB  1 
ATOM   29626 O  OG  . SER   Q  3  153 ? 46.351  -208.642 1.395   1.00 103.68 ? 151 SER   Q OG  1 
ATOM   29627 N  N   . GLY   Q  3  154 ? 45.157  -206.091 2.302   1.00 101.20 ? 152 GLY   Q N   1 
ATOM   29628 C  CA  . GLY   Q  3  154 ? 45.478  -204.661 2.138   1.00 100.15 ? 152 GLY   Q CA  1 
ATOM   29629 C  C   . GLY   Q  3  154 ? 46.452  -204.411 1.000   1.00 100.81 ? 152 GLY   Q C   1 
ATOM   29630 O  O   . GLY   Q  3  154 ? 46.753  -203.234 0.747   1.00 99.82  ? 152 GLY   Q O   1 
ATOM   29631 N  N   . ILE   Q  3  155 ? 46.949  -205.464 0.342   1.00 103.16 ? 153 ILE   Q N   1 
ATOM   29632 C  CA  . ILE   Q  3  155 ? 47.833  -205.324 -0.855  1.00 104.09 ? 153 ILE   Q CA  1 
ATOM   29633 C  C   . ILE   Q  3  155 ? 46.970  -204.843 -2.025  1.00 106.09 ? 153 ILE   Q C   1 
ATOM   29634 O  O   . ILE   Q  3  155 ? 45.787  -205.238 -2.104  1.00 107.83 ? 153 ILE   Q O   1 
ATOM   29635 C  CB  . ILE   Q  3  155 ? 48.613  -206.617 -1.184  1.00 104.85 ? 153 ILE   Q CB  1 
ATOM   29636 C  CG1 . ILE   Q  3  155 ? 47.701  -207.790 -1.562  1.00 108.97 ? 153 ILE   Q CG1 1 
ATOM   29637 C  CG2 . ILE   Q  3  155 ? 49.553  -206.967 -0.039  1.00 100.18 ? 153 ILE   Q CG2 1 
ATOM   29638 C  CD1 . ILE   Q  3  155 ? 48.441  -209.015 -2.066  1.00 112.20 ? 153 ILE   Q CD1 1 
ATOM   29639 N  N   . TYR   Q  3  156 ? 47.543  -203.983 -2.868  1.00 104.51 ? 154 TYR   Q N   1 
ATOM   29640 C  CA  . TYR   Q  3  156 ? 46.927  -203.469 -4.116  1.00 105.20 ? 154 TYR   Q CA  1 
ATOM   29641 C  C   . TYR   Q  3  156 ? 48.003  -203.418 -5.200  1.00 104.23 ? 154 TYR   Q C   1 
ATOM   29642 O  O   . TYR   Q  3  156 ? 49.197  -203.293 -4.863  1.00 103.36 ? 154 TYR   Q O   1 
ATOM   29643 C  CB  . TYR   Q  3  156 ? 46.300  -202.093 -3.884  1.00 104.30 ? 154 TYR   Q CB  1 
ATOM   29644 C  CG  . TYR   Q  3  156 ? 47.292  -200.975 -3.675  1.00 107.11 ? 154 TYR   Q CG  1 
ATOM   29645 C  CD1 . TYR   Q  3  156 ? 47.942  -200.813 -2.461  1.00 107.09 ? 154 TYR   Q CD1 1 
ATOM   29646 C  CD2 . TYR   Q  3  156 ? 47.579  -200.074 -4.688  1.00 107.52 ? 154 TYR   Q CD2 1 
ATOM   29647 C  CE1 . TYR   Q  3  156 ? 48.852  -199.787 -2.258  1.00 106.86 ? 154 TYR   Q CE1 1 
ATOM   29648 C  CE2 . TYR   Q  3  156 ? 48.485  -199.042 -4.501  1.00 107.73 ? 154 TYR   Q CE2 1 
ATOM   29649 C  CZ  . TYR   Q  3  156 ? 49.123  -198.898 -3.282  1.00 106.42 ? 154 TYR   Q CZ  1 
ATOM   29650 O  OH  . TYR   Q  3  156 ? 50.015  -197.882 -3.096  1.00 107.38 ? 154 TYR   Q OH  1 
ATOM   29651 N  N   . SER   Q  3  157 ? 47.587  -203.513 -6.462  1.00 104.09 ? 155 SER   Q N   1 
ATOM   29652 C  CA  . SER   Q  3  157 ? 48.495  -203.518 -7.635  1.00 106.08 ? 155 SER   Q CA  1 
ATOM   29653 C  C   . SER   Q  3  157 ? 47.725  -203.125 -8.897  1.00 104.96 ? 155 SER   Q C   1 
ATOM   29654 O  O   . SER   Q  3  157 ? 46.478  -203.160 -8.868  1.00 102.24 ? 155 SER   Q O   1 
ATOM   29655 C  CB  . SER   Q  3  157 ? 49.160  -204.859 -7.775  1.00 107.88 ? 155 SER   Q CB  1 
ATOM   29656 O  OG  . SER   Q  3  157 ? 48.212  -205.911 -7.683  1.00 111.97 ? 155 SER   Q OG  1 
ATOM   29657 N  N   . SER   Q  3  158 ? 48.457  -202.758 -9.951  1.00 108.04 ? 156 SER   Q N   1 
ATOM   29658 C  CA  . SER   Q  3  158 ? 47.922  -202.353 -11.278 1.00 111.55 ? 156 SER   Q CA  1 
ATOM   29659 C  C   . SER   Q  3  158 ? 47.876  -203.571 -12.211 1.00 113.36 ? 156 SER   Q C   1 
ATOM   29660 O  O   . SER   Q  3  158 ? 48.847  -204.356 -12.218 1.00 107.47 ? 156 SER   Q O   1 
ATOM   29661 C  CB  . SER   Q  3  158 ? 48.744  -201.232 -11.868 1.00 112.53 ? 156 SER   Q CB  1 
ATOM   29662 O  OG  . SER   Q  3  158 ? 48.124  -200.701 -13.031 1.00 111.82 ? 156 SER   Q OG  1 
ATOM   29663 N  N   . TRP   Q  3  159 ? 46.785  -203.715 -12.968 1.00 115.07 ? 157 TRP   Q N   1 
ATOM   29664 C  CA  . TRP   Q  3  159 ? 46.540  -204.852 -13.893 1.00 117.59 ? 157 TRP   Q CA  1 
ATOM   29665 C  C   . TRP   Q  3  159 ? 46.173  -204.324 -15.282 1.00 118.77 ? 157 TRP   Q C   1 
ATOM   29666 O  O   . TRP   Q  3  159 ? 45.431  -203.329 -15.359 1.00 118.19 ? 157 TRP   Q O   1 
ATOM   29667 C  CB  . TRP   Q  3  159 ? 45.441  -205.764 -13.336 1.00 121.29 ? 157 TRP   Q CB  1 
ATOM   29668 C  CG  . TRP   Q  3  159 ? 45.826  -206.464 -12.070 1.00 120.01 ? 157 TRP   Q CG  1 
ATOM   29669 C  CD1 . TRP   Q  3  159 ? 45.854  -205.936 -10.812 1.00 118.10 ? 157 TRP   Q CD1 1 
ATOM   29670 C  CD2 . TRP   Q  3  159 ? 46.238  -207.835 -11.938 1.00 120.26 ? 157 TRP   Q CD2 1 
ATOM   29671 N  NE1 . TRP   Q  3  159 ? 46.255  -206.882 -9.909  1.00 117.39 ? 157 TRP   Q NE1 1 
ATOM   29672 C  CE2 . TRP   Q  3  159 ? 46.496  -208.057 -10.569 1.00 120.56 ? 157 TRP   Q CE2 1 
ATOM   29673 C  CE3 . TRP   Q  3  159 ? 46.409  -208.893 -12.839 1.00 124.78 ? 157 TRP   Q CE3 1 
ATOM   29674 C  CZ2 . TRP   Q  3  159 ? 46.918  -209.294 -10.084 1.00 121.03 ? 157 TRP   Q CZ2 1 
ATOM   29675 C  CZ3 . TRP   Q  3  159 ? 46.827  -210.115 -12.357 1.00 126.17 ? 157 TRP   Q CZ3 1 
ATOM   29676 C  CH2 . TRP   Q  3  159 ? 47.076  -210.311 -10.998 1.00 123.55 ? 157 TRP   Q CH2 1 
ATOM   29677 N  N   . SER   Q  3  160 ? 46.685  -204.973 -16.330 1.00 121.23 ? 158 SER   Q N   1 
ATOM   29678 C  CA  . SER   Q  3  160 ? 46.282  -204.758 -17.744 1.00 121.79 ? 158 SER   Q CA  1 
ATOM   29679 C  C   . SER   Q  3  160 ? 44.852  -205.275 -17.918 1.00 120.17 ? 158 SER   Q C   1 
ATOM   29680 O  O   . SER   Q  3  160 ? 44.045  -204.615 -18.592 1.00 118.14 ? 158 SER   Q O   1 
ATOM   29681 C  CB  . SER   Q  3  160 ? 47.240  -205.437 -18.683 1.00 125.46 ? 158 SER   Q CB  1 
ATOM   29682 O  OG  . SER   Q  3  160 ? 48.572  -205.006 -18.442 1.00 126.46 ? 158 SER   Q OG  1 
ATOM   29683 N  N   . ALA   Q  3  161 ? 44.574  -206.430 -17.316 1.00 120.19 ? 159 ALA   Q N   1 
ATOM   29684 C  CA  . ALA   Q  3  161 ? 43.228  -207.021 -17.155 1.00 121.32 ? 159 ALA   Q CA  1 
ATOM   29685 C  C   . ALA   Q  3  161 ? 43.262  -207.946 -15.937 1.00 118.70 ? 159 ALA   Q C   1 
ATOM   29686 O  O   . ALA   Q  3  161 ? 44.298  -208.612 -15.728 1.00 122.59 ? 159 ALA   Q O   1 
ATOM   29687 C  CB  . ALA   Q  3  161 ? 42.829  -207.761 -18.409 1.00 125.57 ? 159 ALA   Q CB  1 
ATOM   29688 N  N   . GLN   Q  3  162 ? 42.185  -207.973 -15.152 1.00 112.22 ? 160 GLN   Q N   1 
ATOM   29689 C  CA  . GLN   Q  3  162 ? 42.093  -208.840 -13.951 1.00 111.59 ? 160 GLN   Q CA  1 
ATOM   29690 C  C   . GLN   Q  3  162 ? 40.631  -209.202 -13.689 1.00 109.89 ? 160 GLN   Q C   1 
ATOM   29691 O  O   . GLN   Q  3  162 ? 39.736  -208.461 -14.139 1.00 108.88 ? 160 GLN   Q O   1 
ATOM   29692 C  CB  . GLN   Q  3  162 ? 42.759  -208.149 -12.759 1.00 109.95 ? 160 GLN   Q CB  1 
ATOM   29693 C  CG  . GLN   Q  3  162 ? 42.577  -208.851 -11.416 1.00 111.22 ? 160 GLN   Q CG  1 
ATOM   29694 C  CD  . GLN   Q  3  162 ? 43.453  -210.065 -11.206 1.00 113.31 ? 160 GLN   Q CD  1 
ATOM   29695 O  OE1 . GLN   Q  3  162 ? 43.946  -210.300 -10.106 1.00 112.75 ? 160 GLN   Q OE1 1 
ATOM   29696 N  NE2 . GLN   Q  3  162 ? 43.657  -210.859 -12.246 1.00 115.42 ? 160 GLN   Q NE2 1 
ATOM   29697 N  N   . THR   Q  3  163 ? 40.425  -210.329 -13.006 1.00 111.97 ? 161 THR   Q N   1 
ATOM   29698 C  CA  . THR   Q  3  163 ? 39.110  -210.841 -12.554 1.00 112.67 ? 161 THR   Q CA  1 
ATOM   29699 C  C   . THR   Q  3  163 ? 39.222  -211.205 -11.071 1.00 109.42 ? 161 THR   Q C   1 
ATOM   29700 O  O   . THR   Q  3  163 ? 40.352  -211.447 -10.601 1.00 106.78 ? 161 THR   Q O   1 
ATOM   29701 C  CB  . THR   Q  3  163 ? 38.652  -212.009 -13.439 1.00 116.18 ? 161 THR   Q CB  1 
ATOM   29702 O  OG1 . THR   Q  3  163 ? 37.467  -212.574 -12.874 1.00 115.23 ? 161 THR   Q OG1 1 
ATOM   29703 C  CG2 . THR   Q  3  163 ? 39.709  -213.081 -13.597 1.00 118.64 ? 161 THR   Q CG2 1 
ATOM   29704 N  N   . ILE   Q  3  164 ? 38.088  -211.208 -10.372 1.00 109.60 ? 162 ILE   Q N   1 
ATOM   29705 C  CA  . ILE   Q  3  164 ? 37.952  -211.648 -8.952  1.00 113.09 ? 162 ILE   Q CA  1 
ATOM   29706 C  C   . ILE   Q  3  164 ? 36.569  -212.282 -8.782  1.00 115.22 ? 162 ILE   Q C   1 
ATOM   29707 O  O   . ILE   Q  3  164 ? 35.684  -211.991 -9.611  1.00 115.63 ? 162 ILE   Q O   1 
ATOM   29708 C  CB  . ILE   Q  3  164 ? 38.158  -210.465 -7.987  1.00 111.64 ? 162 ILE   Q CB  1 
ATOM   29709 C  CG1 . ILE   Q  3  164 ? 37.351  -209.241 -8.426  1.00 112.72 ? 162 ILE   Q CG1 1 
ATOM   29710 C  CG2 . ILE   Q  3  164 ? 39.636  -210.141 -7.831  1.00 112.10 ? 162 ILE   Q CG2 1 
ATOM   29711 C  CD1 . ILE   Q  3  164 ? 37.202  -208.185 -7.358  1.00 113.78 ? 162 ILE   Q CD1 1 
ATOM   29712 N  N   . GLY   Q  3  165 ? 36.397  -213.108 -7.748  1.00 118.49 ? 163 GLY   Q N   1 
ATOM   29713 C  CA  . GLY   Q  3  165 ? 35.126  -213.788 -7.432  1.00 119.31 ? 163 GLY   Q CA  1 
ATOM   29714 C  C   . GLY   Q  3  165 ? 35.182  -215.263 -7.780  1.00 119.49 ? 163 GLY   Q C   1 
ATOM   29715 O  O   . GLY   Q  3  165 ? 36.299  -215.779 -7.961  1.00 123.31 ? 163 GLY   Q O   1 
ATOM   29716 N  N   . ARG   Q  3  166 ? 34.019  -215.914 -7.875  1.00 121.68 ? 164 ARG   Q N   1 
ATOM   29717 C  CA  . ARG   Q  3  166 ? 33.903  -217.375 -8.136  1.00 123.90 ? 164 ARG   Q CA  1 
ATOM   29718 C  C   . ARG   Q  3  166 ? 34.257  -217.666 -9.597  1.00 122.89 ? 164 ARG   Q C   1 
ATOM   29719 O  O   . ARG   Q  3  166 ? 33.835  -216.894 -10.480 1.00 116.22 ? 164 ARG   Q O   1 
ATOM   29720 C  CB  . ARG   Q  3  166 ? 32.504  -217.896 -7.788  1.00 128.85 ? 164 ARG   Q CB  1 
ATOM   29721 C  CG  . ARG   Q  3  166 ? 31.379  -217.366 -8.666  1.00 131.05 ? 164 ARG   Q CG  1 
ATOM   29722 C  CD  . ARG   Q  3  166 ? 30.034  -217.669 -8.035  1.00 135.31 ? 164 ARG   Q CD  1 
ATOM   29723 N  NE  . ARG   Q  3  166 ? 28.911  -217.350 -8.905  1.00 139.64 ? 164 ARG   Q NE  1 
ATOM   29724 C  CZ  . ARG   Q  3  166 ? 27.630  -217.528 -8.587  1.00 146.66 ? 164 ARG   Q CZ  1 
ATOM   29725 N  NH1 . ARG   Q  3  166 ? 26.686  -217.214 -9.457  1.00 150.25 ? 164 ARG   Q NH1 1 
ATOM   29726 N  NH2 . ARG   Q  3  166 ? 27.290  -218.016 -7.405  1.00 150.38 ? 164 ARG   Q NH2 1 
ATOM   29727 N  N   . ASN   Q  3  167 ? 35.014  -218.744 -9.820  1.00 125.37 ? 165 ASN   Q N   1 
ATOM   29728 C  CA  . ASN   Q  3  167 ? 35.477  -219.209 -11.156 1.00 128.20 ? 165 ASN   Q CA  1 
ATOM   29729 C  C   . ASN   Q  3  167 ? 36.355  -218.129 -11.804 1.00 124.99 ? 165 ASN   Q C   1 
ATOM   29730 O  O   . ASN   Q  3  167 ? 36.478  -218.143 -13.041 1.00 123.89 ? 165 ASN   Q O   1 
ATOM   29731 C  CB  . ASN   Q  3  167 ? 34.297  -219.584 -12.059 1.00 131.57 ? 165 ASN   Q CB  1 
ATOM   29732 C  CG  . ASN   Q  3  167 ? 33.448  -220.705 -11.499 1.00 131.98 ? 165 ASN   Q CG  1 
ATOM   29733 O  OD1 . ASN   Q  3  167 ? 32.265  -220.514 -11.224 1.00 129.90 ? 165 ASN   Q OD1 1 
ATOM   29734 N  ND2 . ASN   Q  3  167 ? 34.040  -221.876 -11.327 1.00 133.88 ? 165 ASN   Q ND2 1 
ATOM   29735 N  N   . SER   Q  3  168 ? 36.960  -217.243 -11.004 1.00 122.44 ? 166 SER   Q N   1 
ATOM   29736 C  CA  . SER   Q  3  168 ? 37.859  -216.162 -11.490 1.00 121.68 ? 166 SER   Q CA  1 
ATOM   29737 C  C   . SER   Q  3  168 ? 39.121  -216.780 -12.105 1.00 126.06 ? 166 SER   Q C   1 
ATOM   29738 O  O   . SER   Q  3  168 ? 39.692  -216.160 -13.021 1.00 128.57 ? 166 SER   Q O   1 
ATOM   29739 C  CB  . SER   Q  3  168 ? 38.201  -215.173 -10.402 1.00 119.05 ? 166 SER   Q CB  1 
ATOM   29740 O  OG  . SER   Q  3  168 ? 38.807  -215.814 -9.292  1.00 115.50 ? 166 SER   Q OG  1 
ATOM   29741 N  N   . LYS   Q  3  169 ? 39.532  -217.960 -11.626 1.00 122.83 ? 167 LYS   Q N   1 
ATOM   29742 C  CA  . LYS   Q  3  169 ? 40.742  -218.675 -12.111 1.00 126.40 ? 167 LYS   Q CA  1 
ATOM   29743 C  C   . LYS   Q  3  169 ? 40.514  -219.115 -13.562 1.00 126.70 ? 167 LYS   Q C   1 
ATOM   29744 O  O   . LYS   Q  3  169 ? 41.481  -219.053 -14.345 1.00 124.25 ? 167 LYS   Q O   1 
ATOM   29745 C  CB  . LYS   Q  3  169 ? 41.077  -219.854 -11.192 1.00 129.56 ? 167 LYS   Q CB  1 
ATOM   29746 C  CG  . LYS   Q  3  169 ? 42.552  -220.228 -11.142 1.00 135.71 ? 167 LYS   Q CG  1 
ATOM   29747 C  CD  . LYS   Q  3  169 ? 42.989  -220.790 -9.806  1.00 140.06 ? 167 LYS   Q CD  1 
ATOM   29748 C  CE  . LYS   Q  3  169 ? 42.428  -222.168 -9.524  1.00 144.33 ? 167 LYS   Q CE  1 
ATOM   29749 N  NZ  . LYS   Q  3  169 ? 42.697  -222.588 -8.129  1.00 147.32 ? 167 LYS   Q NZ  1 
ATOM   29750 N  N   . THR   Q  3  170 ? 39.281  -219.518 -13.901 1.00 131.15 ? 168 THR   Q N   1 
ATOM   29751 C  CA  . THR   Q  3  170 ? 38.858  -219.942 -15.266 1.00 132.94 ? 168 THR   Q CA  1 
ATOM   29752 C  C   . THR   Q  3  170 ? 38.927  -218.751 -16.232 1.00 133.78 ? 168 THR   Q C   1 
ATOM   29753 O  O   . THR   Q  3  170 ? 39.460  -218.930 -17.343 1.00 133.85 ? 168 THR   Q O   1 
ATOM   29754 C  CB  . THR   Q  3  170 ? 37.446  -220.545 -15.267 1.00 132.01 ? 168 THR   Q CB  1 
ATOM   29755 O  OG1 . THR   Q  3  170 ? 37.410  -221.609 -14.315 1.00 131.37 ? 168 THR   Q OG1 1 
ATOM   29756 C  CG2 . THR   Q  3  170 ? 37.027  -221.058 -16.628 1.00 133.95 ? 168 THR   Q CG2 1 
ATOM   29757 N  N   . VAL   Q  3  171 ? 38.395  -217.590 -15.831 1.00 133.78 ? 169 VAL   Q N   1 
ATOM   29758 C  CA  . VAL   Q  3  171 ? 38.325  -216.366 -16.691 1.00 133.18 ? 169 VAL   Q CA  1 
ATOM   29759 C  C   . VAL   Q  3  171 ? 39.711  -215.702 -16.737 1.00 134.94 ? 169 VAL   Q C   1 
ATOM   29760 O  O   . VAL   Q  3  171 ? 40.033  -215.112 -17.788 1.00 139.25 ? 169 VAL   Q O   1 
ATOM   29761 C  CB  . VAL   Q  3  171 ? 37.210  -215.379 -16.273 1.00 129.01 ? 169 VAL   Q CB  1 
ATOM   29762 C  CG1 . VAL   Q  3  171 ? 36.835  -215.469 -14.805 1.00 128.18 ? 169 VAL   Q CG1 1 
ATOM   29763 C  CG2 . VAL   Q  3  171 ? 37.548  -213.940 -16.638 1.00 128.08 ? 169 VAL   Q CG2 1 
ATOM   29764 N  N   . ARG   Q  3  172 ? 40.505  -215.793 -15.662 1.00 132.23 ? 170 ARG   Q N   1 
ATOM   29765 C  CA  . ARG   Q  3  172 ? 41.915  -215.310 -15.652 1.00 131.06 ? 170 ARG   Q CA  1 
ATOM   29766 C  C   . ARG   Q  3  172 ? 42.718  -216.108 -16.686 1.00 134.05 ? 170 ARG   Q C   1 
ATOM   29767 O  O   . ARG   Q  3  172 ? 43.471  -215.477 -17.455 1.00 132.40 ? 170 ARG   Q O   1 
ATOM   29768 C  CB  . ARG   Q  3  172 ? 42.550  -215.426 -14.263 1.00 130.16 ? 170 ARG   Q CB  1 
ATOM   29769 C  CG  . ARG   Q  3  172 ? 43.834  -214.623 -14.108 1.00 127.84 ? 170 ARG   Q CG  1 
ATOM   29770 C  CD  . ARG   Q  3  172 ? 44.434  -214.717 -12.717 1.00 123.88 ? 170 ARG   Q CD  1 
ATOM   29771 N  NE  . ARG   Q  3  172 ? 43.576  -214.107 -11.707 1.00 121.59 ? 170 ARG   Q NE  1 
ATOM   29772 C  CZ  . ARG   Q  3  172 ? 42.757  -214.756 -10.882 1.00 124.13 ? 170 ARG   Q CZ  1 
ATOM   29773 N  NH1 . ARG   Q  3  172 ? 42.661  -216.074 -10.909 1.00 126.82 ? 170 ARG   Q NH1 1 
ATOM   29774 N  NH2 . ARG   Q  3  172 ? 42.029  -214.074 -10.016 1.00 125.91 ? 170 ARG   Q NH2 1 
ATOM   29775 N  N   . GLU   Q  3  173 ? 42.551  -217.436 -16.701 1.00 135.57 ? 171 GLU   Q N   1 
ATOM   29776 C  CA  . GLU   Q  3  173 ? 43.142  -218.361 -17.707 1.00 139.88 ? 171 GLU   Q CA  1 
ATOM   29777 C  C   . GLU   Q  3  173 ? 42.844  -217.821 -19.111 1.00 138.78 ? 171 GLU   Q C   1 
ATOM   29778 O  O   . GLU   Q  3  173 ? 43.800  -217.673 -19.899 1.00 138.04 ? 171 GLU   Q O   1 
ATOM   29779 C  CB  . GLU   Q  3  173 ? 42.580  -219.777 -17.542 1.00 140.90 ? 171 GLU   Q CB  1 
ATOM   29780 C  CG  . GLU   Q  3  173 ? 43.336  -220.846 -18.318 1.00 144.23 ? 171 GLU   Q CG  1 
ATOM   29781 C  CD  . GLU   Q  3  173 ? 44.484  -221.513 -17.580 1.00 148.19 ? 171 GLU   Q CD  1 
ATOM   29782 O  OE1 . GLU   Q  3  173 ? 45.433  -221.961 -18.255 1.00 149.18 ? 171 GLU   Q OE1 1 
ATOM   29783 O  OE2 . GLU   Q  3  173 ? 44.420  -221.604 -16.337 1.00 150.60 ? 171 GLU   Q OE2 1 
ATOM   29784 N  N   . PHE   Q  3  174 ? 41.568  -217.526 -19.395 1.00 139.38 ? 172 PHE   Q N   1 
ATOM   29785 C  CA  . PHE   Q  3  174 ? 41.073  -217.025 -20.706 1.00 142.56 ? 172 PHE   Q CA  1 
ATOM   29786 C  C   . PHE   Q  3  174 ? 41.800  -215.725 -21.072 1.00 141.68 ? 172 PHE   Q C   1 
ATOM   29787 O  O   . PHE   Q  3  174 ? 42.371  -215.649 -22.177 1.00 138.01 ? 172 PHE   Q O   1 
ATOM   29788 C  CB  . PHE   Q  3  174 ? 39.556  -216.811 -20.682 1.00 144.63 ? 172 PHE   Q CB  1 
ATOM   29789 C  CG  . PHE   Q  3  174 ? 39.004  -216.147 -21.919 1.00 148.05 ? 172 PHE   Q CG  1 
ATOM   29790 C  CD1 . PHE   Q  3  174 ? 38.880  -214.767 -21.990 1.00 146.94 ? 172 PHE   Q CD1 1 
ATOM   29791 C  CD2 . PHE   Q  3  174 ? 38.626  -216.899 -23.020 1.00 152.51 ? 172 PHE   Q CD2 1 
ATOM   29792 C  CE1 . PHE   Q  3  174 ? 38.383  -214.157 -23.131 1.00 147.89 ? 172 PHE   Q CE1 1 
ATOM   29793 C  CE2 . PHE   Q  3  174 ? 38.127  -216.287 -24.160 1.00 151.67 ? 172 PHE   Q CE2 1 
ATOM   29794 C  CZ  . PHE   Q  3  174 ? 38.007  -214.918 -24.214 1.00 149.35 ? 172 PHE   Q CZ  1 
ATOM   29795 N  N   . LEU   Q  3  175 ? 41.772  -214.740 -20.168 1.00 138.45 ? 173 LEU   Q N   1 
ATOM   29796 C  CA  . LEU   Q  3  175 ? 42.376  -213.394 -20.365 1.00 138.91 ? 173 LEU   Q CA  1 
ATOM   29797 C  C   . LEU   Q  3  175 ? 43.889  -213.520 -20.584 1.00 136.06 ? 173 LEU   Q C   1 
ATOM   29798 O  O   . LEU   Q  3  175 ? 44.429  -212.733 -21.383 1.00 130.76 ? 173 LEU   Q O   1 
ATOM   29799 C  CB  . LEU   Q  3  175 ? 42.081  -212.515 -19.145 1.00 140.63 ? 173 LEU   Q CB  1 
ATOM   29800 C  CG  . LEU   Q  3  175 ? 40.627  -212.082 -18.960 1.00 145.13 ? 173 LEU   Q CG  1 
ATOM   29801 C  CD1 . LEU   Q  3  175 ? 40.425  -211.469 -17.582 1.00 144.90 ? 173 LEU   Q CD1 1 
ATOM   29802 C  CD2 . LEU   Q  3  175 ? 40.199  -211.102 -20.043 1.00 146.84 ? 173 LEU   Q CD2 1 
ATOM   29803 N  N   . GLU   Q  3  176 ? 44.544  -214.467 -19.902 1.00 139.04 ? 174 GLU   Q N   1 
ATOM   29804 C  CA  . GLU   Q  3  176 ? 46.023  -214.637 -19.924 1.00 143.30 ? 174 GLU   Q CA  1 
ATOM   29805 C  C   . GLU   Q  3  176 ? 46.496  -215.033 -21.330 1.00 142.33 ? 174 GLU   Q C   1 
ATOM   29806 O  O   . GLU   Q  3  176 ? 47.634  -214.667 -21.675 1.00 143.84 ? 174 GLU   Q O   1 
ATOM   29807 C  CB  . GLU   Q  3  176 ? 46.482  -215.653 -18.873 1.00 147.33 ? 174 GLU   Q CB  1 
ATOM   29808 C  CG  . GLU   Q  3  176 ? 46.665  -215.048 -17.491 1.00 150.20 ? 174 GLU   Q CG  1 
ATOM   29809 C  CD  . GLU   Q  3  176 ? 47.203  -215.992 -16.428 1.00 155.09 ? 174 GLU   Q CD  1 
ATOM   29810 O  OE1 . GLU   Q  3  176 ? 47.617  -217.116 -16.783 1.00 160.38 ? 174 GLU   Q OE1 1 
ATOM   29811 O  OE2 . GLU   Q  3  176 ? 47.207  -215.600 -15.242 1.00 159.61 ? 174 GLU   Q OE2 1 
ATOM   29812 N  N   . LYS   Q  3  177 ? 45.672  -215.744 -22.111 1.00 144.56 ? 175 LYS   Q N   1 
ATOM   29813 C  CA  . LYS   Q  3  177 ? 46.026  -216.163 -23.497 1.00 149.71 ? 175 LYS   Q CA  1 
ATOM   29814 C  C   . LYS   Q  3  177 ? 45.368  -215.235 -24.531 1.00 150.48 ? 175 LYS   Q C   1 
ATOM   29815 O  O   . LYS   Q  3  177 ? 45.861  -215.215 -25.674 1.00 154.26 ? 175 LYS   Q O   1 
ATOM   29816 C  CB  . LYS   Q  3  177 ? 45.679  -217.637 -23.748 1.00 155.04 ? 175 LYS   Q CB  1 
ATOM   29817 C  CG  . LYS   Q  3  177 ? 44.202  -218.013 -23.728 1.00 157.99 ? 175 LYS   Q CG  1 
ATOM   29818 C  CD  . LYS   Q  3  177 ? 43.832  -219.102 -24.728 1.00 159.97 ? 175 LYS   Q CD  1 
ATOM   29819 C  CE  . LYS   Q  3  177 ? 44.472  -220.447 -24.446 1.00 161.20 ? 175 LYS   Q CE  1 
ATOM   29820 N  NZ  . LYS   Q  3  177 ? 43.830  -221.135 -23.301 1.00 161.71 ? 175 LYS   Q NZ  1 
ATOM   29821 N  N   . ASN   Q  3  178 ? 44.320  -214.486 -24.161 1.00 149.72 ? 176 ASN   Q N   1 
ATOM   29822 C  CA  . ASN   Q  3  178 ? 43.514  -213.669 -25.113 1.00 154.84 ? 176 ASN   Q CA  1 
ATOM   29823 C  C   . ASN   Q  3  178 ? 43.837  -212.170 -25.003 1.00 153.11 ? 176 ASN   Q C   1 
ATOM   29824 O  O   . ASN   Q  3  178 ? 43.307  -211.412 -25.841 1.00 160.54 ? 176 ASN   Q O   1 
ATOM   29825 C  CB  . ASN   Q  3  178 ? 42.009  -213.896 -24.937 1.00 155.33 ? 176 ASN   Q CB  1 
ATOM   29826 C  CG  . ASN   Q  3  178 ? 41.500  -215.096 -25.705 1.00 158.90 ? 176 ASN   Q CG  1 
ATOM   29827 O  OD1 . ASN   Q  3  178 ? 41.088  -214.966 -26.856 1.00 162.23 ? 176 ASN   Q OD1 1 
ATOM   29828 N  ND2 . ASN   Q  3  178 ? 41.532  -216.265 -25.088 1.00 160.18 ? 176 ASN   Q ND2 1 
ATOM   29829 N  N   . TYR   Q  3  179 ? 44.656  -211.740 -24.035 1.00 150.17 ? 177 TYR   Q N   1 
ATOM   29830 C  CA  . TYR   Q  3  179 ? 45.060  -210.315 -23.870 1.00 146.07 ? 177 TYR   Q CA  1 
ATOM   29831 C  C   . TYR   Q  3  179 ? 46.525  -210.135 -24.279 1.00 140.38 ? 177 TYR   Q C   1 
ATOM   29832 O  O   . TYR   Q  3  179 ? 47.415  -210.678 -23.594 1.00 134.27 ? 177 TYR   Q O   1 
ATOM   29833 C  CB  . TYR   Q  3  179 ? 44.850  -209.827 -22.434 1.00 145.18 ? 177 TYR   Q CB  1 
ATOM   29834 C  CG  . TYR   Q  3  179 ? 44.993  -208.334 -22.264 1.00 144.49 ? 177 TYR   Q CG  1 
ATOM   29835 C  CD1 . TYR   Q  3  179 ? 46.238  -207.742 -22.109 1.00 143.64 ? 177 TYR   Q CD1 1 
ATOM   29836 C  CD2 . TYR   Q  3  179 ? 43.881  -207.505 -22.267 1.00 141.67 ? 177 TYR   Q CD2 1 
ATOM   29837 C  CE1 . TYR   Q  3  179 ? 46.375  -206.371 -21.959 1.00 140.42 ? 177 TYR   Q CE1 1 
ATOM   29838 C  CE2 . TYR   Q  3  179 ? 44.000  -206.133 -22.114 1.00 138.74 ? 177 TYR   Q CE2 1 
ATOM   29839 C  CZ  . TYR   Q  3  179 ? 45.251  -205.563 -21.959 1.00 141.18 ? 177 TYR   Q CZ  1 
ATOM   29840 O  OH  . TYR   Q  3  179 ? 45.372  -204.211 -21.807 1.00 138.49 ? 177 TYR   Q OH  1 
ATOM   29841 N  N   . ASP   Q  3  180 ? 46.761  -209.368 -25.347 1.00 140.31 ? 178 ASP   Q N   1 
ATOM   29842 C  CA  . ASP   Q  3  180 ? 48.116  -208.994 -25.833 1.00 146.75 ? 178 ASP   Q CA  1 
ATOM   29843 C  C   . ASP   Q  3  180 ? 48.517  -207.663 -25.187 1.00 147.29 ? 178 ASP   Q C   1 
ATOM   29844 O  O   . ASP   Q  3  180 ? 47.810  -206.660 -25.412 1.00 149.09 ? 178 ASP   Q O   1 
ATOM   29845 C  CB  . ASP   Q  3  180 ? 48.158  -208.907 -27.361 1.00 149.34 ? 178 ASP   Q CB  1 
ATOM   29846 C  CG  . ASP   Q  3  180 ? 49.553  -208.717 -27.934 1.00 150.47 ? 178 ASP   Q CG  1 
ATOM   29847 O  OD1 . ASP   Q  3  180 ? 50.529  -209.099 -27.256 1.00 151.08 ? 178 ASP   Q OD1 1 
ATOM   29848 O  OD2 . ASP   Q  3  180 ? 49.654  -208.186 -29.058 1.00 151.70 ? 178 ASP   Q OD2 1 
ATOM   29849 N  N   . ARG   Q  3  181 ? 49.602  -207.667 -24.407 1.00 149.50 ? 179 ARG   Q N   1 
ATOM   29850 C  CA  . ARG   Q  3  181 ? 50.182  -206.461 -23.754 1.00 148.70 ? 179 ARG   Q CA  1 
ATOM   29851 C  C   . ARG   Q  3  181 ? 50.687  -205.486 -24.826 1.00 151.16 ? 179 ARG   Q C   1 
ATOM   29852 O  O   . ARG   Q  3  181 ? 50.544  -204.263 -24.622 1.00 148.70 ? 179 ARG   Q O   1 
ATOM   29853 C  CB  . ARG   Q  3  181 ? 51.314  -206.866 -22.804 1.00 146.10 ? 179 ARG   Q CB  1 
ATOM   29854 C  CG  . ARG   Q  3  181 ? 50.839  -207.381 -21.452 1.00 143.10 ? 179 ARG   Q CG  1 
ATOM   29855 C  CD  . ARG   Q  3  181 ? 50.998  -206.349 -20.351 1.00 140.47 ? 179 ARG   Q CD  1 
ATOM   29856 N  NE  . ARG   Q  3  181 ? 51.292  -206.979 -19.069 1.00 140.62 ? 179 ARG   Q NE  1 
ATOM   29857 C  CZ  . ARG   Q  3  181 ? 51.999  -206.428 -18.081 1.00 139.20 ? 179 ARG   Q CZ  1 
ATOM   29858 N  NH1 . ARG   Q  3  181 ? 52.509  -205.213 -18.205 1.00 139.24 ? 179 ARG   Q NH1 1 
ATOM   29859 N  NH2 . ARG   Q  3  181 ? 52.199  -207.107 -16.965 1.00 137.88 ? 179 ARG   Q NH2 1 
ATOM   29860 N  N   . LYS   Q  3  182 ? 51.253  -206.009 -25.919 1.00 154.46 ? 180 LYS   Q N   1 
ATOM   29861 C  CA  . LYS   Q  3  182 ? 51.796  -205.208 -27.053 1.00 158.57 ? 180 LYS   Q CA  1 
ATOM   29862 C  C   . LYS   Q  3  182 ? 50.659  -204.480 -27.789 1.00 158.13 ? 180 LYS   Q C   1 
ATOM   29863 O  O   . LYS   Q  3  182 ? 50.939  -203.409 -28.366 1.00 156.65 ? 180 LYS   Q O   1 
ATOM   29864 C  CB  . LYS   Q  3  182 ? 52.604  -206.086 -28.016 1.00 157.00 ? 180 LYS   Q CB  1 
ATOM   29865 C  CG  . LYS   Q  3  182 ? 54.114  -205.886 -27.959 1.00 156.15 ? 180 LYS   Q CG  1 
ATOM   29866 C  CD  . LYS   Q  3  182 ? 54.776  -206.448 -26.714 1.00 156.68 ? 180 LYS   Q CD  1 
ATOM   29867 C  CE  . LYS   Q  3  182 ? 55.356  -207.835 -26.910 1.00 158.08 ? 180 LYS   Q CE  1 
ATOM   29868 N  NZ  . LYS   Q  3  182 ? 54.306  -208.881 -26.941 1.00 158.39 ? 180 LYS   Q NZ  1 
ATOM   29869 N  N   . GLU   Q  3  183 ? 49.435  -205.027 -27.780 1.00 162.57 ? 181 GLU   Q N   1 
ATOM   29870 C  CA  . GLU   Q  3  183 ? 48.263  -204.437 -28.488 1.00 163.67 ? 181 GLU   Q CA  1 
ATOM   29871 C  C   . GLU   Q  3  183 ? 46.985  -204.648 -27.678 1.00 158.65 ? 181 GLU   Q C   1 
ATOM   29872 O  O   . GLU   Q  3  183 ? 46.244  -205.600 -27.918 1.00 160.40 ? 181 GLU   Q O   1 
ATOM   29873 C  CB  . GLU   Q  3  183 ? 48.130  -205.039 -29.887 1.00 166.62 ? 181 GLU   Q CB  1 
ATOM   29874 C  CG  . GLU   Q  3  183 ? 47.067  -204.361 -30.731 1.00 169.87 ? 181 GLU   Q CG  1 
ATOM   29875 C  CD  . GLU   Q  3  183 ? 47.233  -204.561 -32.226 1.00 175.22 ? 181 GLU   Q CD  1 
ATOM   29876 O  OE1 . GLU   Q  3  183 ? 46.321  -205.142 -32.848 1.00 179.77 ? 181 GLU   Q OE1 1 
ATOM   29877 O  OE2 . GLU   Q  3  183 ? 48.270  -204.130 -32.766 1.00 181.33 ? 181 GLU   Q OE2 1 
ATOM   29878 N  N   . PRO   Q  3  184 ? 46.685  -203.768 -26.695 1.00 157.46 ? 182 PRO   Q N   1 
ATOM   29879 C  CA  . PRO   Q  3  184 ? 45.393  -203.789 -26.006 1.00 153.43 ? 182 PRO   Q CA  1 
ATOM   29880 C  C   . PRO   Q  3  184 ? 44.220  -203.453 -26.925 1.00 154.72 ? 182 PRO   Q C   1 
ATOM   29881 O  O   . PRO   Q  3  184 ? 44.398  -202.754 -27.920 1.00 154.21 ? 182 PRO   Q O   1 
ATOM   29882 C  CB  . PRO   Q  3  184 ? 45.540  -202.717 -24.913 1.00 154.31 ? 182 PRO   Q CB  1 
ATOM   29883 C  CG  . PRO   Q  3  184 ? 46.655  -201.817 -25.407 1.00 155.56 ? 182 PRO   Q CG  1 
ATOM   29884 C  CD  . PRO   Q  3  184 ? 47.591  -202.740 -26.158 1.00 156.86 ? 182 PRO   Q CD  1 
ATOM   29885 N  N   . PRO   Q  3  185 ? 42.996  -203.955 -26.625 1.00 153.04 ? 183 PRO   Q N   1 
ATOM   29886 C  CA  . PRO   Q  3  185 ? 41.795  -203.620 -27.394 1.00 155.18 ? 183 PRO   Q CA  1 
ATOM   29887 C  C   . PRO   Q  3  185 ? 41.764  -202.144 -27.827 1.00 157.17 ? 183 PRO   Q C   1 
ATOM   29888 O  O   . PRO   Q  3  185 ? 41.565  -201.286 -26.983 1.00 159.49 ? 183 PRO   Q O   1 
ATOM   29889 C  CB  . PRO   Q  3  185 ? 40.655  -203.944 -26.414 1.00 153.23 ? 183 PRO   Q CB  1 
ATOM   29890 C  CG  . PRO   Q  3  185 ? 41.202  -205.057 -25.537 1.00 152.00 ? 183 PRO   Q CG  1 
ATOM   29891 C  CD  . PRO   Q  3  185 ? 42.710  -204.902 -25.538 1.00 152.37 ? 183 PRO   Q CD  1 
ATOM   29892 N  N   . ALA   Q  3  186 ? 41.965  -201.890 -29.125 1.00 153.69 ? 184 ALA   Q N   1 
ATOM   29893 C  CA  . ALA   Q  3  186 ? 42.221  -200.549 -29.705 1.00 152.34 ? 184 ALA   Q CA  1 
ATOM   29894 C  C   . ALA   Q  3  186 ? 40.986  -199.644 -29.598 1.00 151.80 ? 184 ALA   Q C   1 
ATOM   29895 O  O   . ALA   Q  3  186 ? 41.180  -198.413 -29.619 1.00 157.80 ? 184 ALA   Q O   1 
ATOM   29896 C  CB  . ALA   Q  3  186 ? 42.684  -200.677 -31.137 1.00 150.85 ? 184 ALA   Q CB  1 
ATOM   29897 N  N   . THR   Q  3  187 ? 39.774  -200.206 -29.492 1.00 146.85 ? 185 THR   Q N   1 
ATOM   29898 C  CA  . THR   Q  3  187 ? 38.505  -199.428 -29.412 1.00 146.10 ? 185 THR   Q CA  1 
ATOM   29899 C  C   . THR   Q  3  187 ? 37.647  -199.883 -28.228 1.00 146.52 ? 185 THR   Q C   1 
ATOM   29900 O  O   . THR   Q  3  187 ? 38.001  -200.889 -27.581 1.00 146.14 ? 185 THR   Q O   1 
ATOM   29901 C  CB  . THR   Q  3  187 ? 37.701  -199.527 -30.713 1.00 146.75 ? 185 THR   Q CB  1 
ATOM   29902 O  OG1 . THR   Q  3  187 ? 37.506  -200.908 -31.018 1.00 145.43 ? 185 THR   Q OG1 1 
ATOM   29903 C  CG2 . THR   Q  3  187 ? 38.386  -198.835 -31.868 1.00 147.27 ? 185 THR   Q CG2 1 
ATOM   29904 N  N   . VAL   Q  3  188 ? 36.562  -199.143 -27.975 1.00 147.40 ? 186 VAL   Q N   1 
ATOM   29905 C  CA  . VAL   Q  3  188 ? 35.530  -199.438 -26.936 1.00 147.42 ? 186 VAL   Q CA  1 
ATOM   29906 C  C   . VAL   Q  3  188 ? 34.889  -200.792 -27.270 1.00 150.11 ? 186 VAL   Q C   1 
ATOM   29907 O  O   . VAL   Q  3  188 ? 34.799  -201.639 -26.359 1.00 145.17 ? 186 VAL   Q O   1 
ATOM   29908 C  CB  . VAL   Q  3  188 ? 34.467  -198.323 -26.845 1.00 146.15 ? 186 VAL   Q CB  1 
ATOM   29909 C  CG1 . VAL   Q  3  188 ? 33.492  -198.571 -25.703 1.00 145.55 ? 186 VAL   Q CG1 1 
ATOM   29910 C  CG2 . VAL   Q  3  188 ? 35.082  -196.935 -26.713 1.00 144.32 ? 186 VAL   Q CG2 1 
ATOM   29911 N  N   . GLU   Q  3  189 ? 34.472  -200.982 -28.528 1.00 153.79 ? 187 GLU   Q N   1 
ATOM   29912 C  CA  . GLU   Q  3  189 ? 33.781  -202.211 -29.012 1.00 157.15 ? 187 GLU   Q CA  1 
ATOM   29913 C  C   . GLU   Q  3  189 ? 34.647  -203.444 -28.728 1.00 159.14 ? 187 GLU   Q C   1 
ATOM   29914 O  O   . GLU   Q  3  189 ? 34.106  -204.416 -28.168 1.00 162.91 ? 187 GLU   Q O   1 
ATOM   29915 C  CB  . GLU   Q  3  189 ? 33.454  -202.131 -30.506 1.00 161.79 ? 187 GLU   Q CB  1 
ATOM   29916 C  CG  . GLU   Q  3  189 ? 32.062  -201.593 -30.802 1.00 165.79 ? 187 GLU   Q CG  1 
ATOM   29917 C  CD  . GLU   Q  3  189 ? 31.390  -202.199 -32.024 1.00 167.75 ? 187 GLU   Q CD  1 
ATOM   29918 O  OE1 . GLU   Q  3  189 ? 30.150  -202.332 -32.009 1.00 169.83 ? 187 GLU   Q OE1 1 
ATOM   29919 O  OE2 . GLU   Q  3  189 ? 32.106  -202.538 -32.987 1.00 170.90 ? 187 GLU   Q OE2 1 
ATOM   29920 N  N   . GLU   Q  3  190 ? 35.930  -203.401 -29.105 1.00 156.56 ? 188 GLU   Q N   1 
ATOM   29921 C  CA  . GLU   Q  3  190 ? 36.903  -204.510 -28.897 1.00 157.30 ? 188 GLU   Q CA  1 
ATOM   29922 C  C   . GLU   Q  3  190 ? 36.997  -204.850 -27.404 1.00 158.54 ? 188 GLU   Q C   1 
ATOM   29923 O  O   . GLU   Q  3  190 ? 36.942  -206.052 -27.071 1.00 159.86 ? 188 GLU   Q O   1 
ATOM   29924 C  CB  . GLU   Q  3  190 ? 38.287  -204.143 -29.438 1.00 156.07 ? 188 GLU   Q CB  1 
ATOM   29925 C  CG  . GLU   Q  3  190 ? 38.469  -204.454 -30.910 1.00 158.57 ? 188 GLU   Q CG  1 
ATOM   29926 C  CD  . GLU   Q  3  190 ? 39.795  -203.983 -31.481 1.00 157.79 ? 188 GLU   Q CD  1 
ATOM   29927 O  OE1 . GLU   Q  3  190 ? 40.581  -204.837 -31.932 1.00 158.84 ? 188 GLU   Q OE1 1 
ATOM   29928 O  OE2 . GLU   Q  3  190 ? 40.037  -202.763 -31.475 1.00 158.33 ? 188 GLU   Q OE2 1 
ATOM   29929 N  N   . CYS   Q  3  191 ? 37.131  -203.831 -26.549 1.00 155.90 ? 189 CYS   Q N   1 
ATOM   29930 C  CA  . CYS   Q  3  191 ? 37.358  -203.970 -25.085 1.00 155.38 ? 189 CYS   Q CA  1 
ATOM   29931 C  C   . CYS   Q  3  191 ? 36.121  -204.574 -24.410 1.00 152.26 ? 189 CYS   Q C   1 
ATOM   29932 O  O   . CYS   Q  3  191 ? 36.305  -205.450 -23.543 1.00 155.26 ? 189 CYS   Q O   1 
ATOM   29933 C  CB  . CYS   Q  3  191 ? 37.697  -202.630 -24.442 1.00 158.16 ? 189 CYS   Q CB  1 
ATOM   29934 S  SG  . CYS   Q  3  191 ? 38.416  -202.790 -22.786 1.00 163.33 ? 189 CYS   Q SG  1 
ATOM   29935 N  N   . VAL   Q  3  192 ? 34.919  -204.124 -24.786 1.00 150.73 ? 190 VAL   Q N   1 
ATOM   29936 C  CA  . VAL   Q  3  192 ? 33.628  -204.649 -24.246 1.00 151.82 ? 190 VAL   Q CA  1 
ATOM   29937 C  C   . VAL   Q  3  192 ? 33.501  -206.126 -24.641 1.00 155.12 ? 190 VAL   Q C   1 
ATOM   29938 O  O   . VAL   Q  3  192 ? 33.125  -206.933 -23.769 1.00 165.96 ? 190 VAL   Q O   1 
ATOM   29939 C  CB  . VAL   Q  3  192 ? 32.414  -203.825 -24.723 1.00 149.82 ? 190 VAL   Q CB  1 
ATOM   29940 C  CG1 . VAL   Q  3  192 ? 31.093  -204.493 -24.363 1.00 149.09 ? 190 VAL   Q CG1 1 
ATOM   29941 C  CG2 . VAL   Q  3  192 ? 32.447  -202.406 -24.178 1.00 146.32 ? 190 VAL   Q CG2 1 
ATOM   29942 N  N   . LYS   Q  3  193 ? 33.817  -206.462 -25.897 1.00 155.41 ? 191 LYS   Q N   1 
ATOM   29943 C  CA  . LYS   Q  3  193 ? 33.664  -207.832 -26.463 1.00 153.40 ? 191 LYS   Q CA  1 
ATOM   29944 C  C   . LYS   Q  3  193 ? 34.567  -208.812 -25.705 1.00 148.09 ? 191 LYS   Q C   1 
ATOM   29945 O  O   . LYS   Q  3  193 ? 34.049  -209.855 -25.262 1.00 151.65 ? 191 LYS   Q O   1 
ATOM   29946 C  CB  . LYS   Q  3  193 ? 33.992  -207.855 -27.958 1.00 154.84 ? 191 LYS   Q CB  1 
ATOM   29947 C  CG  . LYS   Q  3  193 ? 33.566  -209.129 -28.673 1.00 156.03 ? 191 LYS   Q CG  1 
ATOM   29948 C  CD  . LYS   Q  3  193 ? 34.058  -209.225 -30.096 1.00 160.08 ? 191 LYS   Q CD  1 
ATOM   29949 C  CE  . LYS   Q  3  193 ? 33.797  -210.585 -30.706 1.00 160.55 ? 191 LYS   Q CE  1 
ATOM   29950 N  NZ  . LYS   Q  3  193 ? 34.385  -210.700 -32.060 1.00 162.15 ? 191 LYS   Q NZ  1 
ATOM   29951 N  N   . LEU   Q  3  194 ? 35.859  -208.489 -25.568 1.00 143.76 ? 192 LEU   Q N   1 
ATOM   29952 C  CA  . LEU   Q  3  194 ? 36.855  -209.331 -24.850 1.00 139.15 ? 192 LEU   Q CA  1 
ATOM   29953 C  C   . LEU   Q  3  194 ? 36.399  -209.537 -23.399 1.00 139.32 ? 192 LEU   Q C   1 
ATOM   29954 O  O   . LEU   Q  3  194 ? 36.630  -210.642 -22.868 1.00 137.80 ? 192 LEU   Q O   1 
ATOM   29955 C  CB  . LEU   Q  3  194 ? 38.239  -208.674 -24.908 1.00 136.48 ? 192 LEU   Q CB  1 
ATOM   29956 C  CG  . LEU   Q  3  194 ? 39.365  -209.441 -24.211 1.00 135.10 ? 192 LEU   Q CG  1 
ATOM   29957 C  CD1 . LEU   Q  3  194 ? 39.528  -210.836 -24.794 1.00 136.27 ? 192 LEU   Q CD1 1 
ATOM   29958 C  CD2 . LEU   Q  3  194 ? 40.678  -208.677 -24.291 1.00 134.74 ? 192 LEU   Q CD2 1 
ATOM   29959 N  N   . THR   Q  3  195 ? 35.779  -208.518 -22.789 1.00 136.68 ? 193 THR   Q N   1 
ATOM   29960 C  CA  . THR   Q  3  195 ? 35.215  -208.575 -21.412 1.00 137.45 ? 193 THR   Q CA  1 
ATOM   29961 C  C   . THR   Q  3  195 ? 34.011  -209.527 -21.395 1.00 143.62 ? 193 THR   Q C   1 
ATOM   29962 O  O   . THR   Q  3  195 ? 33.975  -210.403 -20.509 1.00 150.14 ? 193 THR   Q O   1 
ATOM   29963 C  CB  . THR   Q  3  195 ? 34.832  -207.185 -20.882 1.00 134.25 ? 193 THR   Q CB  1 
ATOM   29964 O  OG1 . THR   Q  3  195 ? 35.965  -206.322 -20.991 1.00 128.07 ? 193 THR   Q OG1 1 
ATOM   29965 C  CG2 . THR   Q  3  195 ? 34.366  -207.218 -19.442 1.00 130.66 ? 193 THR   Q CG2 1 
ATOM   29966 N  N   . VAL   Q  3  196 ? 33.068  -209.362 -22.330 1.00 144.70 ? 194 VAL   Q N   1 
ATOM   29967 C  CA  . VAL   Q  3  196 ? 31.829  -210.194 -22.420 1.00 149.35 ? 194 VAL   Q CA  1 
ATOM   29968 C  C   . VAL   Q  3  196 ? 32.228  -211.648 -22.705 1.00 151.76 ? 194 VAL   Q C   1 
ATOM   29969 O  O   . VAL   Q  3  196 ? 31.638  -212.544 -22.071 1.00 158.37 ? 194 VAL   Q O   1 
ATOM   29970 C  CB  . VAL   Q  3  196 ? 30.838  -209.653 -23.472 1.00 149.61 ? 194 VAL   Q CB  1 
ATOM   29971 C  CG1 . VAL   Q  3  196 ? 29.717  -210.640 -23.759 1.00 151.74 ? 194 VAL   Q CG1 1 
ATOM   29972 C  CG2 . VAL   Q  3  196 ? 30.256  -208.312 -23.054 1.00 150.41 ? 194 VAL   Q CG2 1 
ATOM   29973 N  N   . ARG   Q  3  197 ? 33.188  -211.872 -23.612 1.00 155.18 ? 195 ARG   Q N   1 
ATOM   29974 C  CA  . ARG   Q  3  197 ? 33.711  -213.224 -23.958 1.00 154.83 ? 195 ARG   Q CA  1 
ATOM   29975 C  C   . ARG   Q  3  197 ? 34.220  -213.921 -22.690 1.00 155.34 ? 195 ARG   Q C   1 
ATOM   29976 O  O   . ARG   Q  3  197 ? 33.859  -215.097 -22.477 1.00 154.02 ? 195 ARG   Q O   1 
ATOM   29977 C  CB  . ARG   Q  3  197 ? 34.847  -213.150 -24.986 1.00 154.64 ? 195 ARG   Q CB  1 
ATOM   29978 C  CG  . ARG   Q  3  197 ? 34.391  -213.126 -26.437 1.00 153.97 ? 195 ARG   Q CG  1 
ATOM   29979 C  CD  . ARG   Q  3  197 ? 35.558  -212.943 -27.390 1.00 151.65 ? 195 ARG   Q CD  1 
ATOM   29980 N  NE  . ARG   Q  3  197 ? 36.491  -214.065 -27.360 1.00 150.02 ? 195 ARG   Q NE  1 
ATOM   29981 C  CZ  . ARG   Q  3  197 ? 37.746  -214.034 -27.809 1.00 149.13 ? 195 ARG   Q CZ  1 
ATOM   29982 N  NH1 . ARG   Q  3  197 ? 38.254  -212.928 -28.330 1.00 149.02 ? 195 ARG   Q NH1 1 
ATOM   29983 N  NH2 . ARG   Q  3  197 ? 38.498  -215.118 -27.727 1.00 150.62 ? 195 ARG   Q NH2 1 
ATOM   29984 N  N   . SER   Q  3  198 ? 35.029  -213.219 -21.890 1.00 151.66 ? 196 SER   Q N   1 
ATOM   29985 C  CA  . SER   Q  3  198 ? 35.701  -213.753 -20.675 1.00 149.97 ? 196 SER   Q CA  1 
ATOM   29986 C  C   . SER   Q  3  198 ? 34.660  -214.175 -19.629 1.00 150.41 ? 196 SER   Q C   1 
ATOM   29987 O  O   . SER   Q  3  198 ? 34.910  -215.179 -18.933 1.00 153.55 ? 196 SER   Q O   1 
ATOM   29988 C  CB  . SER   Q  3  198 ? 36.689  -212.757 -20.113 1.00 144.11 ? 196 SER   Q CB  1 
ATOM   29989 O  OG  . SER   Q  3  198 ? 36.031  -211.621 -19.575 1.00 137.18 ? 196 SER   Q OG  1 
ATOM   29990 N  N   . LEU   Q  3  199 ? 33.541  -213.446 -19.525 1.00 149.66 ? 197 LEU   Q N   1 
ATOM   29991 C  CA  . LEU   Q  3  199 ? 32.435  -213.755 -18.574 1.00 147.89 ? 197 LEU   Q CA  1 
ATOM   29992 C  C   . LEU   Q  3  199 ? 31.626  -214.954 -19.085 1.00 149.35 ? 197 LEU   Q C   1 
ATOM   29993 O  O   . LEU   Q  3  199 ? 31.159  -215.742 -18.239 1.00 145.10 ? 197 LEU   Q O   1 
ATOM   29994 C  CB  . LEU   Q  3  199 ? 31.536  -212.526 -18.384 1.00 151.30 ? 197 LEU   Q CB  1 
ATOM   29995 C  CG  . LEU   Q  3  199 ? 31.989  -211.520 -17.324 1.00 151.95 ? 197 LEU   Q CG  1 
ATOM   29996 C  CD1 . LEU   Q  3  199 ? 31.173  -210.239 -17.409 1.00 152.88 ? 197 LEU   Q CD1 1 
ATOM   29997 C  CD2 . LEU   Q  3  199 ? 31.897  -212.107 -15.921 1.00 151.80 ? 197 LEU   Q CD2 1 
ATOM   29998 N  N   . LEU   Q  3  200 ? 31.474  -215.092 -20.408 1.00 147.82 ? 198 LEU   Q N   1 
ATOM   29999 C  CA  . LEU   Q  3  200 ? 30.679  -216.178 -21.047 1.00 151.48 ? 198 LEU   Q CA  1 
ATOM   30000 C  C   . LEU   Q  3  200 ? 31.359  -217.540 -20.846 1.00 152.04 ? 198 LEU   Q C   1 
ATOM   30001 O  O   . LEU   Q  3  200 ? 30.668  -218.562 -21.018 1.00 154.05 ? 198 LEU   Q O   1 
ATOM   30002 C  CB  . LEU   Q  3  200 ? 30.483  -215.878 -22.537 1.00 154.84 ? 198 LEU   Q CB  1 
ATOM   30003 C  CG  . LEU   Q  3  200 ? 29.446  -214.803 -22.859 1.00 156.42 ? 198 LEU   Q CG  1 
ATOM   30004 C  CD1 . LEU   Q  3  200 ? 29.547  -214.378 -24.316 1.00 157.76 ? 198 LEU   Q CD1 1 
ATOM   30005 C  CD2 . LEU   Q  3  200 ? 28.037  -215.284 -22.541 1.00 158.08 ? 198 LEU   Q CD2 1 
ATOM   30006 N  N   . GLU   Q  3  201 ? 32.651  -217.559 -20.500 1.00 150.11 ? 199 GLU   Q N   1 
ATOM   30007 C  CA  . GLU   Q  3  201 ? 33.387  -218.796 -20.121 1.00 149.93 ? 199 GLU   Q CA  1 
ATOM   30008 C  C   . GLU   Q  3  201 ? 32.798  -219.369 -18.826 1.00 152.26 ? 199 GLU   Q C   1 
ATOM   30009 O  O   . GLU   Q  3  201 ? 32.902  -220.596 -18.635 1.00 154.01 ? 199 GLU   Q O   1 
ATOM   30010 C  CB  . GLU   Q  3  201 ? 34.882  -218.519 -19.935 1.00 148.77 ? 199 GLU   Q CB  1 
ATOM   30011 C  CG  . GLU   Q  3  201 ? 35.594  -218.089 -21.206 1.00 151.08 ? 199 GLU   Q CG  1 
ATOM   30012 C  CD  . GLU   Q  3  201 ? 35.697  -219.163 -22.277 1.00 148.65 ? 199 GLU   Q CD  1 
ATOM   30013 O  OE1 . GLU   Q  3  201 ? 36.272  -220.231 -21.991 1.00 148.30 ? 199 GLU   Q OE1 1 
ATOM   30014 O  OE2 . GLU   Q  3  201 ? 35.196  -218.930 -23.395 1.00 152.91 ? 199 GLU   Q OE2 1 
ATOM   30015 N  N   . VAL   Q  3  202 ? 32.203  -218.518 -17.979 1.00 152.80 ? 200 VAL   Q N   1 
ATOM   30016 C  CA  . VAL   Q  3  202 ? 31.817  -218.851 -16.573 1.00 154.18 ? 200 VAL   Q CA  1 
ATOM   30017 C  C   . VAL   Q  3  202 ? 30.308  -218.666 -16.336 1.00 153.64 ? 200 VAL   Q C   1 
ATOM   30018 O  O   . VAL   Q  3  202 ? 29.771  -219.407 -15.492 1.00 149.51 ? 200 VAL   Q O   1 
ATOM   30019 C  CB  . VAL   Q  3  202 ? 32.649  -218.012 -15.581 1.00 157.42 ? 200 VAL   Q CB  1 
ATOM   30020 C  CG1 . VAL   Q  3  202 ? 32.072  -218.025 -14.172 1.00 157.48 ? 200 VAL   Q CG1 1 
ATOM   30021 C  CG2 . VAL   Q  3  202 ? 34.104  -218.457 -15.564 1.00 158.95 ? 200 VAL   Q CG2 1 
ATOM   30022 N  N   . VAL   Q  3  203 ? 29.645  -217.723 -17.018 1.00 158.47 ? 201 VAL   Q N   1 
ATOM   30023 C  CA  . VAL   Q  3  203 ? 28.337  -217.157 -16.555 1.00 161.26 ? 201 VAL   Q CA  1 
ATOM   30024 C  C   . VAL   Q  3  203 ? 27.210  -218.204 -16.657 1.00 162.65 ? 201 VAL   Q C   1 
ATOM   30025 O  O   . VAL   Q  3  203 ? 26.787  -218.672 -15.582 1.00 163.94 ? 201 VAL   Q O   1 
ATOM   30026 C  CB  . VAL   Q  3  203 ? 27.996  -215.817 -17.244 1.00 159.69 ? 201 VAL   Q CB  1 
ATOM   30027 C  CG1 . VAL   Q  3  203 ? 27.689  -215.945 -18.729 1.00 162.53 ? 201 VAL   Q CG1 1 
ATOM   30028 C  CG2 . VAL   Q  3  203 ? 26.859  -215.105 -16.529 1.00 158.15 ? 201 VAL   Q CG2 1 
ATOM   30029 N  N   . GLN   Q  3  204 ? 26.763  -218.580 -17.867 1.00 165.46 ? 202 GLN   Q N   1 
ATOM   30030 C  CA  . GLN   Q  3  204 ? 25.524  -219.376 -18.144 1.00 168.27 ? 202 GLN   Q CA  1 
ATOM   30031 C  C   . GLN   Q  3  204 ? 24.844  -218.797 -19.396 1.00 167.07 ? 202 GLN   Q C   1 
ATOM   30032 O  O   . GLN   Q  3  204 ? 25.321  -219.103 -20.505 1.00 170.85 ? 202 GLN   Q O   1 
ATOM   30033 C  CB  . GLN   Q  3  204 ? 24.597  -219.414 -16.919 1.00 167.53 ? 202 GLN   Q CB  1 
ATOM   30034 C  CG  . GLN   Q  3  204 ? 23.238  -220.071 -17.146 1.00 168.88 ? 202 GLN   Q CG  1 
ATOM   30035 C  CD  . GLN   Q  3  204 ? 23.326  -221.500 -17.623 1.00 169.20 ? 202 GLN   Q CD  1 
ATOM   30036 O  OE1 . GLN   Q  3  204 ? 24.275  -222.221 -17.321 1.00 165.88 ? 202 GLN   Q OE1 1 
ATOM   30037 N  NE2 . GLN   Q  3  204 ? 22.319  -221.927 -18.369 1.00 172.76 ? 202 GLN   Q NE2 1 
ATOM   30038 N  N   . THR   Q  3  205 ? 23.790  -217.987 -19.227 1.00 174.17 ? 203 THR   Q N   1 
ATOM   30039 C  CA  . THR   Q  3  205 ? 23.067  -217.272 -20.314 1.00 178.73 ? 203 THR   Q CA  1 
ATOM   30040 C  C   . THR   Q  3  205 ? 23.574  -215.828 -20.328 1.00 183.11 ? 203 THR   Q C   1 
ATOM   30041 O  O   . THR   Q  3  205 ? 23.784  -215.275 -19.230 1.00 186.50 ? 203 THR   Q O   1 
ATOM   30042 C  CB  . THR   Q  3  205 ? 21.543  -217.305 -20.113 1.00 183.14 ? 203 THR   Q CB  1 
ATOM   30043 O  OG1 . THR   Q  3  205 ? 21.232  -218.211 -19.054 1.00 178.97 ? 203 THR   Q OG1 1 
ATOM   30044 C  CG2 . THR   Q  3  205 ? 20.782  -217.713 -21.357 1.00 183.11 ? 203 THR   Q CG2 1 
ATOM   30045 N  N   . GLY   Q  3  206 ? 23.755  -215.239 -21.512 1.00 185.94 ? 204 GLY   Q N   1 
ATOM   30046 C  CA  . GLY   Q  3  206 ? 24.164  -213.829 -21.664 1.00 184.45 ? 204 GLY   Q CA  1 
ATOM   30047 C  C   . GLY   Q  3  206 ? 22.980  -212.881 -21.563 1.00 184.11 ? 204 GLY   Q C   1 
ATOM   30048 O  O   . GLY   Q  3  206 ? 23.063  -211.776 -22.132 1.00 183.01 ? 204 GLY   Q O   1 
ATOM   30049 N  N   . ALA   Q  3  207 ? 21.919  -213.288 -20.854 1.00 180.87 ? 205 ALA   Q N   1 
ATOM   30050 C  CA  . ALA   Q  3  207 ? 20.670  -212.516 -20.656 1.00 175.46 ? 205 ALA   Q CA  1 
ATOM   30051 C  C   . ALA   Q  3  207 ? 20.911  -211.451 -19.576 1.00 171.84 ? 205 ALA   Q C   1 
ATOM   30052 O  O   . ALA   Q  3  207 ? 21.889  -210.692 -19.723 1.00 167.41 ? 205 ALA   Q O   1 
ATOM   30053 C  CB  . ALA   Q  3  207 ? 19.539  -213.459 -20.316 1.00 176.86 ? 205 ALA   Q CB  1 
ATOM   30054 N  N   . LYS   Q  3  208 ? 20.082  -211.404 -18.525 1.00 172.05 ? 206 LYS   Q N   1 
ATOM   30055 C  CA  . LYS   Q  3  208 ? 20.212  -210.439 -17.399 1.00 174.08 ? 206 LYS   Q CA  1 
ATOM   30056 C  C   . LYS   Q  3  208 ? 21.179  -211.010 -16.352 1.00 174.44 ? 206 LYS   Q C   1 
ATOM   30057 O  O   . LYS   Q  3  208 ? 20.882  -210.893 -15.147 1.00 177.88 ? 206 LYS   Q O   1 
ATOM   30058 C  CB  . LYS   Q  3  208 ? 18.834  -210.128 -16.804 1.00 179.49 ? 206 LYS   Q CB  1 
ATOM   30059 C  CG  . LYS   Q  3  208 ? 17.920  -209.312 -17.708 1.00 180.72 ? 206 LYS   Q CG  1 
ATOM   30060 C  CD  . LYS   Q  3  208 ? 16.470  -209.303 -17.271 1.00 181.94 ? 206 LYS   Q CD  1 
ATOM   30061 C  CE  . LYS   Q  3  208 ? 15.569  -208.541 -18.222 1.00 180.91 ? 206 LYS   Q CE  1 
ATOM   30062 N  NZ  . LYS   Q  3  208 ? 15.412  -209.243 -19.519 1.00 182.81 ? 206 LYS   Q NZ  1 
ATOM   30063 N  N   . ASN   Q  3  209 ? 22.296  -211.594 -16.802 1.00 176.91 ? 207 ASN   Q N   1 
ATOM   30064 C  CA  . ASN   Q  3  209 ? 23.356  -212.184 -15.941 1.00 179.46 ? 207 ASN   Q CA  1 
ATOM   30065 C  C   . ASN   Q  3  209 ? 24.635  -211.340 -16.010 1.00 180.11 ? 207 ASN   Q C   1 
ATOM   30066 O  O   . ASN   Q  3  209 ? 25.444  -211.446 -15.067 1.00 177.98 ? 207 ASN   Q O   1 
ATOM   30067 C  CB  . ASN   Q  3  209 ? 23.662  -213.634 -16.327 1.00 183.48 ? 207 ASN   Q CB  1 
ATOM   30068 C  CG  . ASN   Q  3  209 ? 22.554  -214.601 -15.963 1.00 189.71 ? 207 ASN   Q CG  1 
ATOM   30069 O  OD1 . ASN   Q  3  209 ? 21.533  -214.205 -15.405 1.00 188.23 ? 207 ASN   Q OD1 1 
ATOM   30070 N  ND2 . ASN   Q  3  209 ? 22.749  -215.873 -16.273 1.00 188.17 ? 207 ASN   Q ND2 1 
ATOM   30071 N  N   . ILE   Q  3  210 ? 24.822  -210.548 -17.075 1.00 177.38 ? 208 ILE   Q N   1 
ATOM   30072 C  CA  . ILE   Q  3  210 ? 26.054  -209.733 -17.304 1.00 173.07 ? 208 ILE   Q CA  1 
ATOM   30073 C  C   . ILE   Q  3  210 ? 25.704  -208.240 -17.234 1.00 166.68 ? 208 ILE   Q C   1 
ATOM   30074 O  O   . ILE   Q  3  210 ? 24.755  -207.817 -17.923 1.00 170.30 ? 208 ILE   Q O   1 
ATOM   30075 C  CB  . ILE   Q  3  210 ? 26.730  -210.111 -18.639 1.00 172.05 ? 208 ILE   Q CB  1 
ATOM   30076 C  CG1 . ILE   Q  3  210 ? 27.260  -211.547 -18.603 1.00 170.58 ? 208 ILE   Q CG1 1 
ATOM   30077 C  CG2 . ILE   Q  3  210 ? 27.828  -209.113 -18.990 1.00 170.48 ? 208 ILE   Q CG2 1 
ATOM   30078 C  CD1 . ILE   Q  3  210 ? 27.805  -212.049 -19.922 1.00 172.08 ? 208 ILE   Q CD1 1 
ATOM   30079 N  N   . GLU   Q  3  211 ? 26.455  -207.491 -16.417 1.00 163.41 ? 209 GLU   Q N   1 
ATOM   30080 C  CA  . GLU   Q  3  211 ? 26.495  -206.003 -16.388 1.00 158.39 ? 209 GLU   Q CA  1 
ATOM   30081 C  C   . GLU   Q  3  211 ? 27.818  -205.545 -17.009 1.00 152.08 ? 209 GLU   Q C   1 
ATOM   30082 O  O   . GLU   Q  3  211 ? 28.854  -206.157 -16.688 1.00 151.96 ? 209 GLU   Q O   1 
ATOM   30083 C  CB  . GLU   Q  3  211 ? 26.400  -205.477 -14.954 1.00 155.99 ? 209 GLU   Q CB  1 
ATOM   30084 C  CG  . GLU   Q  3  211 ? 24.988  -205.430 -14.400 1.00 158.35 ? 209 GLU   Q CG  1 
ATOM   30085 C  CD  . GLU   Q  3  211 ? 24.884  -204.920 -12.971 1.00 156.34 ? 209 GLU   Q CD  1 
ATOM   30086 O  OE1 . GLU   Q  3  211 ? 25.921  -204.513 -12.405 1.00 158.67 ? 209 GLU   Q OE1 1 
ATOM   30087 O  OE2 . GLU   Q  3  211 ? 23.764  -204.929 -12.424 1.00 156.07 ? 209 GLU   Q OE2 1 
ATOM   30088 N  N   . ILE   Q  3  212 ? 27.782  -204.515 -17.858 1.00 148.41 ? 210 ILE   Q N   1 
ATOM   30089 C  CA  . ILE   Q  3  212 ? 28.994  -203.879 -18.458 1.00 147.00 ? 210 ILE   Q CA  1 
ATOM   30090 C  C   . ILE   Q  3  212 ? 28.922  -202.370 -18.211 1.00 145.45 ? 210 ILE   Q C   1 
ATOM   30091 O  O   . ILE   Q  3  212 ? 27.897  -201.762 -18.576 1.00 152.80 ? 210 ILE   Q O   1 
ATOM   30092 C  CB  . ILE   Q  3  212 ? 29.115  -204.198 -19.963 1.00 148.65 ? 210 ILE   Q CB  1 
ATOM   30093 C  CG1 . ILE   Q  3  212 ? 29.221  -205.704 -20.233 1.00 149.78 ? 210 ILE   Q CG1 1 
ATOM   30094 C  CG2 . ILE   Q  3  212 ? 30.273  -203.427 -20.584 1.00 147.99 ? 210 ILE   Q CG2 1 
ATOM   30095 C  CD1 . ILE   Q  3  212 ? 30.503  -206.346 -19.741 1.00 146.01 ? 210 ILE   Q CD1 1 
ATOM   30096 N  N   . THR   Q  3  213 ? 29.975  -201.800 -17.617 1.00 143.36 ? 211 THR   Q N   1 
ATOM   30097 C  CA  . THR   Q  3  213 ? 30.179  -200.334 -17.471 1.00 139.50 ? 211 THR   Q CA  1 
ATOM   30098 C  C   . THR   Q  3  213 ? 31.449  -199.937 -18.229 1.00 135.70 ? 211 THR   Q C   1 
ATOM   30099 O  O   . THR   Q  3  213 ? 32.481  -200.616 -18.051 1.00 134.28 ? 211 THR   Q O   1 
ATOM   30100 C  CB  . THR   Q  3  213 ? 30.254  -199.909 -16.000 1.00 133.93 ? 211 THR   Q CB  1 
ATOM   30101 O  OG1 . THR   Q  3  213 ? 29.142  -200.480 -15.310 1.00 134.85 ? 211 THR   Q OG1 1 
ATOM   30102 C  CG2 . THR   Q  3  213 ? 30.236  -198.406 -15.829 1.00 133.58 ? 211 THR   Q CG2 1 
ATOM   30103 N  N   . VAL   Q  3  214 ? 31.362  -198.881 -19.043 1.00 134.42 ? 212 VAL   Q N   1 
ATOM   30104 C  CA  . VAL   Q  3  214 ? 32.493  -198.332 -19.847 1.00 137.07 ? 212 VAL   Q CA  1 
ATOM   30105 C  C   . VAL   Q  3  214 ? 32.879  -196.967 -19.273 1.00 138.39 ? 212 VAL   Q C   1 
ATOM   30106 O  O   . VAL   Q  3  214 ? 32.022  -196.061 -19.290 1.00 145.55 ? 212 VAL   Q O   1 
ATOM   30107 C  CB  . VAL   Q  3  214 ? 32.128  -198.213 -21.338 1.00 140.07 ? 212 VAL   Q CB  1 
ATOM   30108 C  CG1 . VAL   Q  3  214 ? 33.306  -197.717 -22.162 1.00 139.09 ? 212 VAL   Q CG1 1 
ATOM   30109 C  CG2 . VAL   Q  3  214 ? 31.595  -199.523 -21.897 1.00 141.86 ? 212 VAL   Q CG2 1 
ATOM   30110 N  N   . VAL   Q  3  215 ? 34.122  -196.831 -18.803 1.00 137.26 ? 213 VAL   Q N   1 
ATOM   30111 C  CA  . VAL   Q  3  215 ? 34.719  -195.534 -18.365 1.00 133.73 ? 213 VAL   Q CA  1 
ATOM   30112 C  C   . VAL   Q  3  215 ? 35.695  -195.071 -19.455 1.00 137.17 ? 213 VAL   Q C   1 
ATOM   30113 O  O   . VAL   Q  3  215 ? 36.558  -195.874 -19.859 1.00 138.21 ? 213 VAL   Q O   1 
ATOM   30114 C  CB  . VAL   Q  3  215 ? 35.385  -195.622 -16.975 1.00 132.06 ? 213 VAL   Q CB  1 
ATOM   30115 C  CG1 . VAL   Q  3  215 ? 36.293  -196.832 -16.818 1.00 130.67 ? 213 VAL   Q CG1 1 
ATOM   30116 C  CG2 . VAL   Q  3  215 ? 36.141  -194.347 -16.633 1.00 131.48 ? 213 VAL   Q CG2 1 
ATOM   30117 N  N   . LYS   Q  3  216 ? 35.521  -193.831 -19.928 1.00 137.29 ? 214 LYS   Q N   1 
ATOM   30118 C  CA  . LYS   Q  3  216 ? 36.399  -193.139 -20.911 1.00 136.48 ? 214 LYS   Q CA  1 
ATOM   30119 C  C   . LYS   Q  3  216 ? 36.980  -191.888 -20.252 1.00 131.97 ? 214 LYS   Q C   1 
ATOM   30120 O  O   . LYS   Q  3  216 ? 36.494  -191.459 -19.207 1.00 131.38 ? 214 LYS   Q O   1 
ATOM   30121 C  CB  . LYS   Q  3  216 ? 35.602  -192.790 -22.174 1.00 137.58 ? 214 LYS   Q CB  1 
ATOM   30122 C  CG  . LYS   Q  3  216 ? 35.511  -193.894 -23.219 1.00 139.68 ? 214 LYS   Q CG  1 
ATOM   30123 C  CD  . LYS   Q  3  216 ? 34.559  -193.567 -24.349 1.00 138.80 ? 214 LYS   Q CD  1 
ATOM   30124 C  CE  . LYS   Q  3  216 ? 33.108  -193.776 -23.974 1.00 139.14 ? 214 LYS   Q CE  1 
ATOM   30125 N  NZ  . LYS   Q  3  216 ? 32.203  -193.476 -25.108 1.00 141.49 ? 214 LYS   Q NZ  1 
ATOM   30126 N  N   . PRO   Q  3  217 ? 38.037  -191.266 -20.829 1.00 128.60 ? 215 PRO   Q N   1 
ATOM   30127 C  CA  . PRO   Q  3  217 ? 38.655  -190.081 -20.231 1.00 125.09 ? 215 PRO   Q CA  1 
ATOM   30128 C  C   . PRO   Q  3  217 ? 37.690  -188.905 -20.009 1.00 125.42 ? 215 PRO   Q C   1 
ATOM   30129 O  O   . PRO   Q  3  217 ? 36.676  -188.837 -20.681 1.00 127.30 ? 215 PRO   Q O   1 
ATOM   30130 C  CB  . PRO   Q  3  217 ? 39.732  -189.672 -21.248 1.00 125.20 ? 215 PRO   Q CB  1 
ATOM   30131 C  CG  . PRO   Q  3  217 ? 40.035  -190.943 -22.009 1.00 126.19 ? 215 PRO   Q CG  1 
ATOM   30132 C  CD  . PRO   Q  3  217 ? 38.721  -191.692 -22.060 1.00 128.48 ? 215 PRO   Q CD  1 
ATOM   30133 N  N   . ASP   Q  3  218 ? 38.046  -188.017 -19.072 1.00 127.84 ? 216 ASP   Q N   1 
ATOM   30134 C  CA  . ASP   Q  3  218 ? 37.320  -186.763 -18.727 1.00 129.22 ? 216 ASP   Q CA  1 
ATOM   30135 C  C   . ASP   Q  3  218 ? 35.887  -187.095 -18.286 1.00 129.06 ? 216 ASP   Q C   1 
ATOM   30136 O  O   . ASP   Q  3  218 ? 34.937  -186.587 -18.917 1.00 129.35 ? 216 ASP   Q O   1 
ATOM   30137 C  CB  . ASP   Q  3  218 ? 37.348  -185.759 -19.886 1.00 131.23 ? 216 ASP   Q CB  1 
ATOM   30138 C  CG  . ASP   Q  3  218 ? 38.705  -185.121 -20.138 1.00 130.68 ? 216 ASP   Q CG  1 
ATOM   30139 O  OD1 . ASP   Q  3  218 ? 39.476  -184.967 -19.168 1.00 130.16 ? 216 ASP   Q OD1 1 
ATOM   30140 O  OD2 . ASP   Q  3  218 ? 38.977  -184.767 -21.304 1.00 129.64 ? 216 ASP   Q OD2 1 
ATOM   30141 N  N   . SER   Q  3  219 ? 35.751  -187.914 -17.238 1.00 127.77 ? 217 SER   Q N   1 
ATOM   30142 C  CA  . SER   Q  3  219 ? 34.477  -188.204 -16.526 1.00 127.55 ? 217 SER   Q CA  1 
ATOM   30143 C  C   . SER   Q  3  219 ? 33.397  -188.666 -17.512 1.00 126.45 ? 217 SER   Q C   1 
ATOM   30144 O  O   . SER   Q  3  219 ? 32.271  -188.134 -17.451 1.00 124.38 ? 217 SER   Q O   1 
ATOM   30145 C  CB  . SER   Q  3  219 ? 34.024  -186.994 -15.752 1.00 129.01 ? 217 SER   Q CB  1 
ATOM   30146 O  OG  . SER   Q  3  219 ? 35.043  -186.553 -14.868 1.00 130.66 ? 217 SER   Q OG  1 
ATOM   30147 N  N   . ASP   Q  3  220 ? 33.731  -189.623 -18.382 1.00 126.98 ? 218 ASP   Q N   1 
ATOM   30148 C  CA  . ASP   Q  3  220 ? 32.813  -190.177 -19.412 1.00 130.84 ? 218 ASP   Q CA  1 
ATOM   30149 C  C   . ASP   Q  3  220 ? 32.494  -191.637 -19.057 1.00 131.97 ? 218 ASP   Q C   1 
ATOM   30150 O  O   . ASP   Q  3  220 ? 33.124  -192.543 -19.642 1.00 135.42 ? 218 ASP   Q O   1 
ATOM   30151 C  CB  . ASP   Q  3  220 ? 33.422  -190.012 -20.808 1.00 129.80 ? 218 ASP   Q CB  1 
ATOM   30152 C  CG  . ASP   Q  3  220 ? 32.457  -190.289 -21.948 1.00 131.49 ? 218 ASP   Q CG  1 
ATOM   30153 O  OD1 . ASP   Q  3  220 ? 31.234  -190.257 -21.705 1.00 132.09 ? 218 ASP   Q OD1 1 
ATOM   30154 O  OD2 . ASP   Q  3  220 ? 32.939  -190.525 -23.074 1.00 131.95 ? 218 ASP   Q OD2 1 
ATOM   30155 N  N   . ILE   Q  3  221 ? 31.551  -191.849 -18.130 1.00 132.10 ? 219 ILE   Q N   1 
ATOM   30156 C  CA  . ILE   Q  3  221 ? 31.122  -193.193 -17.634 1.00 131.98 ? 219 ILE   Q CA  1 
ATOM   30157 C  C   . ILE   Q  3  221 ? 29.656  -193.426 -18.017 1.00 133.08 ? 219 ILE   Q C   1 
ATOM   30158 O  O   . ILE   Q  3  221 ? 28.817  -192.566 -17.680 1.00 134.11 ? 219 ILE   Q O   1 
ATOM   30159 C  CB  . ILE   Q  3  221 ? 31.330  -193.314 -16.110 1.00 132.22 ? 219 ILE   Q CB  1 
ATOM   30160 C  CG1 . ILE   Q  3  221 ? 32.780  -193.029 -15.712 1.00 132.72 ? 219 ILE   Q CG1 1 
ATOM   30161 C  CG2 . ILE   Q  3  221 ? 30.866  -194.676 -15.608 1.00 131.19 ? 219 ILE   Q CG2 1 
ATOM   30162 C  CD1 . ILE   Q  3  221 ? 32.967  -192.718 -14.247 1.00 133.32 ? 219 ILE   Q CD1 1 
ATOM   30163 N  N   . VAL   Q  3  222 ? 29.365  -194.556 -18.671 1.00 135.67 ? 220 VAL   Q N   1 
ATOM   30164 C  CA  . VAL   Q  3  222 ? 27.981  -194.995 -19.029 1.00 136.44 ? 220 VAL   Q CA  1 
ATOM   30165 C  C   . VAL   Q  3  222 ? 27.856  -196.511 -18.819 1.00 138.83 ? 220 VAL   Q C   1 
ATOM   30166 O  O   . VAL   Q  3  222 ? 28.826  -197.242 -19.119 1.00 140.53 ? 220 VAL   Q O   1 
ATOM   30167 C  CB  . VAL   Q  3  222 ? 27.612  -194.589 -20.470 1.00 133.88 ? 220 VAL   Q CB  1 
ATOM   30168 C  CG1 . VAL   Q  3  222 ? 28.433  -195.335 -21.512 1.00 134.12 ? 220 VAL   Q CG1 1 
ATOM   30169 C  CG2 . VAL   Q  3  222 ? 26.123  -194.762 -20.733 1.00 134.77 ? 220 VAL   Q CG2 1 
ATOM   30170 N  N   . ALA   Q  3  223 ? 26.698  -196.955 -18.318 1.00 138.68 ? 221 ALA   Q N   1 
ATOM   30171 C  CA  . ALA   Q  3  223 ? 26.325  -198.377 -18.137 1.00 137.63 ? 221 ALA   Q CA  1 
ATOM   30172 C  C   . ALA   Q  3  223 ? 25.507  -198.832 -19.350 1.00 141.17 ? 221 ALA   Q C   1 
ATOM   30173 O  O   . ALA   Q  3  223 ? 24.548  -198.123 -19.711 1.00 140.78 ? 221 ALA   Q O   1 
ATOM   30174 C  CB  . ALA   Q  3  223 ? 25.550  -198.552 -16.854 1.00 133.44 ? 221 ALA   Q CB  1 
ATOM   30175 N  N   . LEU   Q  3  224 ? 25.883  -199.964 -19.954 1.00 144.32 ? 222 LEU   Q N   1 
ATOM   30176 C  CA  . LEU   Q  3  224 ? 25.170  -200.582 -21.106 1.00 149.48 ? 222 LEU   Q CA  1 
ATOM   30177 C  C   . LEU   Q  3  224 ? 23.850  -201.190 -20.615 1.00 154.06 ? 222 LEU   Q C   1 
ATOM   30178 O  O   . LEU   Q  3  224 ? 23.807  -201.651 -19.456 1.00 157.61 ? 222 LEU   Q O   1 
ATOM   30179 C  CB  . LEU   Q  3  224 ? 26.058  -201.656 -21.748 1.00 148.35 ? 222 LEU   Q CB  1 
ATOM   30180 C  CG  . LEU   Q  3  224 ? 27.006  -201.185 -22.851 1.00 147.64 ? 222 LEU   Q CG  1 
ATOM   30181 C  CD1 . LEU   Q  3  224 ? 27.876  -200.027 -22.384 1.00 144.05 ? 222 LEU   Q CD1 1 
ATOM   30182 C  CD2 . LEU   Q  3  224 ? 27.872  -202.338 -23.335 1.00 146.93 ? 222 LEU   Q CD2 1 
ATOM   30183 N  N   . SER   Q  3  225 ? 22.823  -201.195 -21.472 1.00 161.30 ? 223 SER   Q N   1 
ATOM   30184 C  CA  . SER   Q  3  225 ? 21.497  -201.822 -21.218 1.00 162.96 ? 223 SER   Q CA  1 
ATOM   30185 C  C   . SER   Q  3  225 ? 21.535  -203.292 -21.651 1.00 165.55 ? 223 SER   Q C   1 
ATOM   30186 O  O   . SER   Q  3  225 ? 22.555  -203.711 -22.233 1.00 164.94 ? 223 SER   Q O   1 
ATOM   30187 C  CB  . SER   Q  3  225 ? 20.394  -201.072 -21.919 1.00 165.81 ? 223 SER   Q CB  1 
ATOM   30188 O  OG  . SER   Q  3  225 ? 20.469  -201.252 -23.326 1.00 166.81 ? 223 SER   Q OG  1 
ATOM   30189 N  N   . SER   Q  3  226 ? 20.459  -204.037 -21.378 1.00 164.28 ? 224 SER   Q N   1 
ATOM   30190 C  CA  . SER   Q  3  226 ? 20.315  -205.483 -21.699 1.00 166.23 ? 224 SER   Q CA  1 
ATOM   30191 C  C   . SER   Q  3  226 ? 20.580  -205.719 -23.191 1.00 166.27 ? 224 SER   Q C   1 
ATOM   30192 O  O   . SER   Q  3  226 ? 21.497  -206.501 -23.508 1.00 159.90 ? 224 SER   Q O   1 
ATOM   30193 C  CB  . SER   Q  3  226 ? 18.955  -205.998 -21.301 1.00 169.12 ? 224 SER   Q CB  1 
ATOM   30194 O  OG  . SER   Q  3  226 ? 18.785  -205.948 -19.892 1.00 172.56 ? 224 SER   Q OG  1 
ATOM   30195 N  N   . GLU   Q  3  227 ? 19.814  -205.051 -24.061 1.00 169.71 ? 225 GLU   Q N   1 
ATOM   30196 C  CA  . GLU   Q  3  227 ? 19.861  -205.217 -25.542 1.00 173.39 ? 225 GLU   Q CA  1 
ATOM   30197 C  C   . GLU   Q  3  227 ? 21.284  -204.968 -26.058 1.00 170.40 ? 225 GLU   Q C   1 
ATOM   30198 O  O   . GLU   Q  3  227 ? 21.764  -205.787 -26.868 1.00 169.13 ? 225 GLU   Q O   1 
ATOM   30199 C  CB  . GLU   Q  3  227 ? 18.875  -204.273 -26.236 1.00 174.18 ? 225 GLU   Q CB  1 
ATOM   30200 C  CG  . GLU   Q  3  227 ? 17.467  -204.833 -26.355 1.00 176.93 ? 225 GLU   Q CG  1 
ATOM   30201 C  CD  . GLU   Q  3  227 ? 16.634  -204.796 -25.084 1.00 177.24 ? 225 GLU   Q CD  1 
ATOM   30202 O  OE1 . GLU   Q  3  227 ? 17.165  -204.382 -24.034 1.00 180.86 ? 225 GLU   Q OE1 1 
ATOM   30203 O  OE2 . GLU   Q  3  227 ? 15.451  -205.183 -25.150 1.00 175.46 ? 225 GLU   Q OE2 1 
ATOM   30204 N  N   . GLU   Q  3  228 ? 21.922  -203.878 -25.615 1.00 171.59 ? 226 GLU   Q N   1 
ATOM   30205 C  CA  . GLU   Q  3  228 ? 23.298  -203.479 -26.027 1.00 169.42 ? 226 GLU   Q CA  1 
ATOM   30206 C  C   . GLU   Q  3  228 ? 24.268  -204.631 -25.736 1.00 169.69 ? 226 GLU   Q C   1 
ATOM   30207 O  O   . GLU   Q  3  228 ? 25.062  -204.971 -26.635 1.00 164.47 ? 226 GLU   Q O   1 
ATOM   30208 C  CB  . GLU   Q  3  228 ? 23.743  -202.203 -25.308 1.00 165.55 ? 226 GLU   Q CB  1 
ATOM   30209 C  CG  . GLU   Q  3  228 ? 22.959  -200.965 -25.710 1.00 163.14 ? 226 GLU   Q CG  1 
ATOM   30210 C  CD  . GLU   Q  3  228 ? 23.422  -199.672 -25.058 1.00 160.19 ? 226 GLU   Q CD  1 
ATOM   30211 O  OE1 . GLU   Q  3  228 ? 24.647  -199.459 -24.970 1.00 159.44 ? 226 GLU   Q OE1 1 
ATOM   30212 O  OE2 . GLU   Q  3  228 ? 22.556  -198.880 -24.639 1.00 158.53 ? 226 GLU   Q OE2 1 
ATOM   30213 N  N   . ILE   Q  3  229 ? 24.191  -205.207 -24.530 1.00 169.77 ? 227 ILE   Q N   1 
ATOM   30214 C  CA  . ILE   Q  3  229 ? 25.045  -206.348 -24.079 1.00 167.88 ? 227 ILE   Q CA  1 
ATOM   30215 C  C   . ILE   Q  3  229 ? 24.633  -207.600 -24.863 1.00 170.71 ? 227 ILE   Q C   1 
ATOM   30216 O  O   . ILE   Q  3  229 ? 25.534  -208.348 -25.283 1.00 175.54 ? 227 ILE   Q O   1 
ATOM   30217 C  CB  . ILE   Q  3  229 ? 24.948  -206.570 -22.552 1.00 166.14 ? 227 ILE   Q CB  1 
ATOM   30218 C  CG1 . ILE   Q  3  229 ? 25.336  -205.320 -21.758 1.00 162.76 ? 227 ILE   Q CG1 1 
ATOM   30219 C  CG2 . ILE   Q  3  229 ? 25.784  -207.769 -22.125 1.00 166.51 ? 227 ILE   Q CG2 1 
ATOM   30220 C  CD1 . ILE   Q  3  229 ? 24.792  -205.294 -20.348 1.00 161.44 ? 227 ILE   Q CD1 1 
ATOM   30221 N  N   . ASN   Q  3  230 ? 23.324  -207.808 -25.054 1.00 169.96 ? 228 ASN   Q N   1 
ATOM   30222 C  CA  . ASN   Q  3  230 ? 22.744  -209.007 -25.722 1.00 169.45 ? 228 ASN   Q CA  1 
ATOM   30223 C  C   . ASN   Q  3  230 ? 23.274  -209.110 -27.159 1.00 168.65 ? 228 ASN   Q C   1 
ATOM   30224 O  O   . ASN   Q  3  230 ? 23.413  -210.246 -27.651 1.00 172.17 ? 228 ASN   Q O   1 
ATOM   30225 C  CB  . ASN   Q  3  230 ? 21.211  -208.989 -25.705 1.00 168.59 ? 228 ASN   Q CB  1 
ATOM   30226 C  CG  . ASN   Q  3  230 ? 20.591  -210.370 -25.777 1.00 168.39 ? 228 ASN   Q CG  1 
ATOM   30227 O  OD1 . ASN   Q  3  230 ? 21.268  -211.354 -26.068 1.00 171.24 ? 228 ASN   Q OD1 1 
ATOM   30228 N  ND2 . ASN   Q  3  230 ? 19.299  -210.456 -25.505 1.00 169.36 ? 228 ASN   Q ND2 1 
ATOM   30229 N  N   . GLN   Q  3  231 ? 23.551  -207.972 -27.805 1.00 169.62 ? 229 GLN   Q N   1 
ATOM   30230 C  CA  . GLN   Q  3  231 ? 24.102  -207.906 -29.186 1.00 169.82 ? 229 GLN   Q CA  1 
ATOM   30231 C  C   . GLN   Q  3  231 ? 25.522  -208.483 -29.210 1.00 164.36 ? 229 GLN   Q C   1 
ATOM   30232 O  O   . GLN   Q  3  231 ? 25.852  -209.171 -30.195 1.00 164.11 ? 229 GLN   Q O   1 
ATOM   30233 C  CB  . GLN   Q  3  231 ? 24.080  -206.470 -29.711 1.00 170.15 ? 229 GLN   Q CB  1 
ATOM   30234 C  CG  . GLN   Q  3  231 ? 22.694  -206.017 -30.139 1.00 171.23 ? 229 GLN   Q CG  1 
ATOM   30235 C  CD  . GLN   Q  3  231 ? 22.594  -204.517 -30.265 1.00 171.25 ? 229 GLN   Q CD  1 
ATOM   30236 O  OE1 . GLN   Q  3  231 ? 23.523  -203.851 -30.715 1.00 170.52 ? 229 GLN   Q OE1 1 
ATOM   30237 N  NE2 . GLN   Q  3  231 ? 21.455  -203.973 -29.867 1.00 173.46 ? 229 GLN   Q NE2 1 
ATOM   30238 N  N   . TYR   Q  3  232 ? 26.327  -208.210 -28.176 1.00 165.73 ? 230 TYR   Q N   1 
ATOM   30239 C  CA  . TYR   Q  3  232 ? 27.690  -208.781 -28.000 1.00 167.43 ? 230 TYR   Q CA  1 
ATOM   30240 C  C   . TYR   Q  3  232 ? 27.588  -210.298 -27.806 1.00 171.16 ? 230 TYR   Q C   1 
ATOM   30241 O  O   . TYR   Q  3  232 ? 28.370  -211.027 -28.446 1.00 176.02 ? 230 TYR   Q O   1 
ATOM   30242 C  CB  . TYR   Q  3  232 ? 28.428  -208.117 -26.834 1.00 165.88 ? 230 TYR   Q CB  1 
ATOM   30243 C  CG  . TYR   Q  3  232 ? 28.988  -206.756 -27.154 1.00 162.73 ? 230 TYR   Q CG  1 
ATOM   30244 C  CD1 . TYR   Q  3  232 ? 30.239  -206.619 -27.734 1.00 160.94 ? 230 TYR   Q CD1 1 
ATOM   30245 C  CD2 . TYR   Q  3  232 ? 28.266  -205.605 -26.888 1.00 158.93 ? 230 TYR   Q CD2 1 
ATOM   30246 C  CE1 . TYR   Q  3  232 ? 30.763  -205.374 -28.037 1.00 155.97 ? 230 TYR   Q CE1 1 
ATOM   30247 C  CE2 . TYR   Q  3  232 ? 28.775  -204.351 -27.184 1.00 156.10 ? 230 TYR   Q CE2 1 
ATOM   30248 C  CZ  . TYR   Q  3  232 ? 30.027  -204.236 -27.760 1.00 157.27 ? 230 TYR   Q CZ  1 
ATOM   30249 O  OH  . TYR   Q  3  232 ? 30.538  -203.007 -28.056 1.00 158.36 ? 230 TYR   Q OH  1 
ATOM   30250 N  N   . VAL   Q  3  233 ? 26.647  -210.750 -26.967 1.00 172.39 ? 231 VAL   Q N   1 
ATOM   30251 C  CA  . VAL   Q  3  233 ? 26.403  -212.195 -26.663 1.00 172.14 ? 231 VAL   Q CA  1 
ATOM   30252 C  C   . VAL   Q  3  233 ? 26.046  -212.910 -27.972 1.00 166.77 ? 231 VAL   Q C   1 
ATOM   30253 O  O   . VAL   Q  3  233 ? 26.689  -213.935 -28.274 1.00 166.62 ? 231 VAL   Q O   1 
ATOM   30254 C  CB  . VAL   Q  3  233 ? 25.306  -212.394 -25.596 1.00 172.38 ? 231 VAL   Q CB  1 
ATOM   30255 C  CG1 . VAL   Q  3  233 ? 25.028  -213.869 -25.338 1.00 172.36 ? 231 VAL   Q CG1 1 
ATOM   30256 C  CG2 . VAL   Q  3  233 ? 25.641  -211.688 -24.289 1.00 171.54 ? 231 VAL   Q CG2 1 
ATOM   30257 N  N   . THR   Q  3  234 ? 25.068  -212.378 -28.717 1.00 163.83 ? 232 THR   Q N   1 
ATOM   30258 C  CA  . THR   Q  3  234 ? 24.549  -212.953 -29.990 1.00 161.56 ? 232 THR   Q CA  1 
ATOM   30259 C  C   . THR   Q  3  234 ? 25.681  -213.064 -31.018 1.00 168.63 ? 232 THR   Q C   1 
ATOM   30260 O  O   . THR   Q  3  234 ? 25.783  -214.125 -31.662 1.00 173.11 ? 232 THR   Q O   1 
ATOM   30261 C  CB  . THR   Q  3  234 ? 23.403  -212.118 -30.576 1.00 156.60 ? 232 THR   Q CB  1 
ATOM   30262 O  OG1 . THR   Q  3  234 ? 22.429  -211.883 -29.559 1.00 148.83 ? 232 THR   Q OG1 1 
ATOM   30263 C  CG2 . THR   Q  3  234 ? 22.743  -212.792 -31.758 1.00 155.25 ? 232 THR   Q CG2 1 
ATOM   30264 N  N   . GLN   Q  3  235 ? 26.483  -212.006 -31.168 1.00 170.24 ? 233 GLN   Q N   1 
ATOM   30265 C  CA  . GLN   Q  3  235 ? 27.574  -211.910 -32.177 1.00 176.75 ? 233 GLN   Q CA  1 
ATOM   30266 C  C   . GLN   Q  3  235 ? 28.675  -212.935 -31.866 1.00 178.00 ? 233 GLN   Q C   1 
ATOM   30267 O  O   . GLN   Q  3  235 ? 29.175  -213.557 -32.824 1.00 180.70 ? 233 GLN   Q O   1 
ATOM   30268 C  CB  . GLN   Q  3  235 ? 28.147  -210.491 -32.215 1.00 175.08 ? 233 GLN   Q CB  1 
ATOM   30269 C  CG  . GLN   Q  3  235 ? 29.089  -210.249 -33.387 1.00 177.18 ? 233 GLN   Q CG  1 
ATOM   30270 C  CD  . GLN   Q  3  235 ? 30.009  -209.076 -33.155 1.00 176.29 ? 233 GLN   Q CD  1 
ATOM   30271 O  OE1 . GLN   Q  3  235 ? 31.222  -209.230 -33.035 1.00 180.05 ? 233 GLN   Q OE1 1 
ATOM   30272 N  NE2 . GLN   Q  3  235 ? 29.435  -207.886 -33.082 1.00 177.24 ? 233 GLN   Q NE2 1 
ATOM   30273 N  N   . ILE   Q  3  236 ? 29.042  -213.097 -30.588 1.00 181.97 ? 234 ILE   Q N   1 
ATOM   30274 C  CA  . ILE   Q  3  236 ? 30.162  -213.979 -30.130 1.00 182.49 ? 234 ILE   Q CA  1 
ATOM   30275 C  C   . ILE   Q  3  236 ? 29.808  -215.449 -30.408 1.00 183.92 ? 234 ILE   Q C   1 
ATOM   30276 O  O   . ILE   Q  3  236 ? 30.712  -216.191 -30.843 1.00 185.03 ? 234 ILE   Q O   1 
ATOM   30277 C  CB  . ILE   Q  3  236 ? 30.500  -213.729 -28.643 1.00 181.17 ? 234 ILE   Q CB  1 
ATOM   30278 C  CG1 . ILE   Q  3  236 ? 31.174  -212.368 -28.441 1.00 178.67 ? 234 ILE   Q CG1 1 
ATOM   30279 C  CG2 . ILE   Q  3  236 ? 31.355  -214.854 -28.074 1.00 182.64 ? 234 ILE   Q CG2 1 
ATOM   30280 C  CD1 . ILE   Q  3  236 ? 31.094  -211.841 -27.025 1.00 176.17 ? 234 ILE   Q CD1 1 
ATOM   30281 N  N   . GLU   Q  3  237 ? 28.555  -215.850 -30.161 1.00 186.01 ? 235 GLU   Q N   1 
ATOM   30282 C  CA  . GLU   Q  3  237 ? 28.074  -217.256 -30.290 1.00 187.38 ? 235 GLU   Q CA  1 
ATOM   30283 C  C   . GLU   Q  3  237 ? 28.066  -217.690 -31.763 1.00 190.43 ? 235 GLU   Q C   1 
ATOM   30284 O  O   . GLU   Q  3  237 ? 28.339  -218.879 -32.022 1.00 190.20 ? 235 GLU   Q O   1 
ATOM   30285 C  CB  . GLU   Q  3  237 ? 26.679  -217.416 -29.681 1.00 184.44 ? 235 GLU   Q CB  1 
ATOM   30286 C  CG  . GLU   Q  3  237 ? 26.691  -217.552 -28.168 1.00 178.61 ? 235 GLU   Q CG  1 
ATOM   30287 C  CD  . GLU   Q  3  237 ? 25.323  -217.687 -27.520 1.00 175.04 ? 235 GLU   Q CD  1 
ATOM   30288 O  OE1 . GLU   Q  3  237 ? 25.248  -218.274 -26.424 1.00 173.58 ? 235 GLU   Q OE1 1 
ATOM   30289 O  OE2 . GLU   Q  3  237 ? 24.337  -217.200 -28.109 1.00 175.14 ? 235 GLU   Q OE2 1 
ATOM   30290 N  N   . GLN   Q  3  238 ? 27.755  -216.774 -32.686 1.00 190.32 ? 236 GLN   Q N   1 
ATOM   30291 C  CA  . GLN   Q  3  238 ? 27.651  -217.060 -34.144 1.00 195.06 ? 236 GLN   Q CA  1 
ATOM   30292 C  C   . GLN   Q  3  238 ? 29.051  -217.277 -34.735 1.00 195.31 ? 236 GLN   Q C   1 
ATOM   30293 O  O   . GLN   Q  3  238 ? 29.177  -218.130 -35.636 1.00 200.12 ? 236 GLN   Q O   1 
ATOM   30294 C  CB  . GLN   Q  3  238 ? 26.901  -215.936 -34.859 1.00 196.47 ? 236 GLN   Q CB  1 
ATOM   30295 C  CG  . GLN   Q  3  238 ? 25.416  -215.908 -34.527 1.00 202.62 ? 236 GLN   Q CG  1 
ATOM   30296 C  CD  . GLN   Q  3  238 ? 24.672  -214.801 -35.233 1.00 208.13 ? 236 GLN   Q CD  1 
ATOM   30297 O  OE1 . GLN   Q  3  238 ? 25.260  -213.836 -35.716 1.00 210.84 ? 236 GLN   Q OE1 1 
ATOM   30298 N  NE2 . GLN   Q  3  238 ? 23.356  -214.932 -35.293 1.00 213.59 ? 236 GLN   Q NE2 1 
ATOM   30299 N  N   . GLU   Q  3  239 ? 30.056  -216.542 -34.248 1.00 189.52 ? 237 GLU   Q N   1 
ATOM   30300 C  CA  . GLU   Q  3  239 ? 31.481  -216.699 -34.649 1.00 189.46 ? 237 GLU   Q CA  1 
ATOM   30301 C  C   . GLU   Q  3  239 ? 32.041  -218.002 -34.063 1.00 193.17 ? 237 GLU   Q C   1 
ATOM   30302 O  O   . GLU   Q  3  239 ? 32.955  -218.578 -34.687 1.00 198.46 ? 237 GLU   Q O   1 
ATOM   30303 C  CB  . GLU   Q  3  239 ? 32.312  -215.500 -34.185 1.00 183.73 ? 237 GLU   Q CB  1 
ATOM   30304 C  CG  . GLU   Q  3  239 ? 31.914  -214.194 -34.848 1.00 181.23 ? 237 GLU   Q CG  1 
ATOM   30305 C  CD  . GLU   Q  3  239 ? 32.641  -212.967 -34.327 1.00 175.62 ? 237 GLU   Q CD  1 
ATOM   30306 O  OE1 . GLU   Q  3  239 ? 33.873  -213.039 -34.157 1.00 177.01 ? 237 GLU   Q OE1 1 
ATOM   30307 O  OE2 . GLU   Q  3  239 ? 31.973  -211.943 -34.089 1.00 169.97 ? 237 GLU   Q OE2 1 
ATOM   30308 N  N   . LYS   Q  3  240 ? 31.511  -218.444 -32.915 1.00 192.38 ? 238 LYS   Q N   1 
ATOM   30309 C  CA  . LYS   Q  3  240 ? 31.978  -219.647 -32.170 1.00 191.65 ? 238 LYS   Q CA  1 
ATOM   30310 C  C   . LYS   Q  3  240 ? 31.660  -220.914 -32.976 1.00 193.45 ? 238 LYS   Q C   1 
ATOM   30311 O  O   . LYS   Q  3  240 ? 32.560  -221.768 -33.094 1.00 196.68 ? 238 LYS   Q O   1 
ATOM   30312 C  CB  . LYS   Q  3  240 ? 31.341  -219.709 -30.778 1.00 184.04 ? 238 LYS   Q CB  1 
ATOM   30313 C  CG  . LYS   Q  3  240 ? 31.954  -220.740 -29.839 1.00 177.19 ? 238 LYS   Q CG  1 
ATOM   30314 C  CD  . LYS   Q  3  240 ? 31.317  -220.773 -28.470 1.00 174.31 ? 238 LYS   Q CD  1 
ATOM   30315 C  CE  . LYS   Q  3  240 ? 31.898  -221.854 -27.584 1.00 172.19 ? 238 LYS   Q CE  1 
ATOM   30316 N  NZ  . LYS   Q  3  240 ? 31.283  -221.846 -26.237 1.00 171.28 ? 238 LYS   Q NZ  1 
ATOM   30317 N  N   . GLN   Q  3  241 ? 30.435  -221.031 -33.504 1.00 197.80 ? 239 GLN   Q N   1 
ATOM   30318 C  CA  . GLN   Q  3  241 ? 29.994  -222.188 -34.333 1.00 198.89 ? 239 GLN   Q CA  1 
ATOM   30319 C  C   . GLN   Q  3  241 ? 30.798  -222.186 -35.639 1.00 196.76 ? 239 GLN   Q C   1 
ATOM   30320 O  O   . GLN   Q  3  241 ? 30.283  -221.677 -36.656 1.00 194.18 ? 239 GLN   Q O   1 
ATOM   30321 C  CB  . GLN   Q  3  241 ? 28.485  -222.144 -34.585 1.00 201.22 ? 239 GLN   Q CB  1 
ATOM   30322 C  CG  . GLN   Q  3  241 ? 27.664  -222.603 -33.389 1.00 200.95 ? 239 GLN   Q CG  1 
ATOM   30323 C  CD  . GLN   Q  3  241 ? 26.207  -222.231 -33.510 1.00 200.32 ? 239 GLN   Q CD  1 
ATOM   30324 O  OE1 . GLN   Q  3  241 ? 25.632  -222.241 -34.596 1.00 199.56 ? 239 GLN   Q OE1 1 
ATOM   30325 N  NE2 . GLN   Q  3  241 ? 25.593  -221.902 -32.384 1.00 201.37 ? 239 GLN   Q NE2 1 
ATOM   30326 N  N   . GLU   Q  3  242 ? 32.021  -222.727 -35.589 1.00 199.43 ? 240 GLU   Q N   1 
ATOM   30327 C  CA  . GLU   Q  3  242 ? 32.991  -222.742 -36.717 1.00 198.71 ? 240 GLU   Q CA  1 
ATOM   30328 C  C   . GLU   Q  3  242 ? 33.865  -223.999 -36.616 1.00 198.64 ? 240 GLU   Q C   1 
ATOM   30329 O  O   . GLU   Q  3  242 ? 34.731  -224.115 -35.746 1.00 194.67 ? 240 GLU   Q O   1 
ATOM   30330 C  CB  . GLU   Q  3  242 ? 33.831  -221.462 -36.695 1.00 194.14 ? 240 GLU   Q CB  1 
ATOM   30331 C  CG  . GLU   Q  3  242 ? 34.107  -220.897 -38.076 1.00 195.05 ? 240 GLU   Q CG  1 
ATOM   30332 C  CD  . GLU   Q  3  242 ? 32.939  -220.156 -38.703 1.00 195.34 ? 240 GLU   Q CD  1 
ATOM   30333 O  OE1 . GLU   Q  3  242 ? 32.923  -220.030 -39.942 1.00 198.78 ? 240 GLU   Q OE1 1 
ATOM   30334 O  OE2 . GLU   Q  3  242 ? 32.050  -219.702 -37.954 1.00 193.56 ? 240 GLU   Q OE2 1 
ATOM   30335 N  N   . ASP   R  4  9   ? 41.293  -220.022 23.445  1.00 150.68 ? 1   ASP   R N   1 
ATOM   30336 C  CA  . ASP   R  4  9   ? 42.520  -219.443 22.812  1.00 151.10 ? 1   ASP   R CA  1 
ATOM   30337 C  C   . ASP   R  4  9   ? 43.506  -219.063 23.928  1.00 151.14 ? 1   ASP   R C   1 
ATOM   30338 O  O   . ASP   R  4  9   ? 43.647  -219.865 24.873  1.00 152.87 ? 1   ASP   R O   1 
ATOM   30339 C  CB  . ASP   R  4  9   ? 42.154  -218.291 21.868  1.00 150.51 ? 1   ASP   R CB  1 
ATOM   30340 C  CG  . ASP   R  4  9   ? 43.167  -218.045 20.758  1.00 146.65 ? 1   ASP   R CG  1 
ATOM   30341 O  OD1 . ASP   R  4  9   ? 44.324  -218.492 20.902  1.00 141.73 ? 1   ASP   R OD1 1 
ATOM   30342 O  OD2 . ASP   R  4  9   ? 42.789  -217.410 19.754  1.00 149.59 ? 1   ASP   R OD2 1 
ATOM   30343 N  N   . ARG   R  4  10  ? 44.161  -217.898 23.831  1.00 153.17 ? 2   ARG   R N   1 
ATOM   30344 C  CA  . ARG   R  4  10  ? 45.270  -217.479 24.730  1.00 151.20 ? 2   ARG   R CA  1 
ATOM   30345 C  C   . ARG   R  4  10  ? 45.630  -216.013 24.453  1.00 147.40 ? 2   ARG   R C   1 
ATOM   30346 O  O   . ARG   R  4  10  ? 45.327  -215.530 23.343  1.00 143.75 ? 2   ARG   R O   1 
ATOM   30347 C  CB  . ARG   R  4  10  ? 46.471  -218.396 24.488  1.00 149.92 ? 2   ARG   R CB  1 
ATOM   30348 C  CG  . ARG   R  4  10  ? 47.598  -218.288 25.504  1.00 150.74 ? 2   ARG   R CG  1 
ATOM   30349 C  CD  . ARG   R  4  10  ? 48.720  -219.224 25.093  1.00 150.73 ? 2   ARG   R CD  1 
ATOM   30350 N  NE  . ARG   R  4  10  ? 49.123  -218.970 23.712  1.00 150.86 ? 2   ARG   R NE  1 
ATOM   30351 C  CZ  . ARG   R  4  10  ? 49.534  -219.888 22.837  1.00 150.88 ? 2   ARG   R CZ  1 
ATOM   30352 N  NH1 . ARG   R  4  10  ? 49.610  -221.166 23.171  1.00 151.42 ? 2   ARG   R NH1 1 
ATOM   30353 N  NH2 . ARG   R  4  10  ? 49.863  -219.516 21.611  1.00 152.73 ? 2   ARG   R NH2 1 
ATOM   30354 N  N   . GLY   R  4  11  ? 46.250  -215.339 25.429  1.00 143.86 ? 3   GLY   R N   1 
ATOM   30355 C  CA  . GLY   R  4  11  ? 46.675  -213.927 25.338  1.00 140.65 ? 3   GLY   R CA  1 
ATOM   30356 C  C   . GLY   R  4  11  ? 47.596  -213.693 24.153  1.00 134.84 ? 3   GLY   R C   1 
ATOM   30357 O  O   . GLY   R  4  11  ? 48.352  -214.618 23.799  1.00 134.08 ? 3   GLY   R O   1 
ATOM   30358 N  N   . VAL   R  4  12  ? 47.525  -212.502 23.555  1.00 127.96 ? 4   VAL   R N   1 
ATOM   30359 C  CA  . VAL   R  4  12  ? 48.342  -212.102 22.370  1.00 122.34 ? 4   VAL   R CA  1 
ATOM   30360 C  C   . VAL   R  4  12  ? 49.787  -211.836 22.817  1.00 114.52 ? 4   VAL   R C   1 
ATOM   30361 O  O   . VAL   R  4  12  ? 50.701  -212.084 22.013  1.00 112.63 ? 4   VAL   R O   1 
ATOM   30362 C  CB  . VAL   R  4  12  ? 47.720  -210.888 21.650  1.00 124.69 ? 4   VAL   R CB  1 
ATOM   30363 C  CG1 . VAL   R  4  12  ? 48.700  -210.209 20.705  1.00 124.68 ? 4   VAL   R CG1 1 
ATOM   30364 C  CG2 . VAL   R  4  12  ? 46.449  -211.275 20.909  1.00 127.62 ? 4   VAL   R CG2 1 
ATOM   30365 N  N   . SER   R  4  13  ? 49.985  -211.352 24.048  1.00 113.68 ? 5   SER   R N   1 
ATOM   30366 C  CA  . SER   R  4  13  ? 51.317  -211.033 24.631  1.00 116.22 ? 5   SER   R CA  1 
ATOM   30367 C  C   . SER   R  4  13  ? 51.763  -212.145 25.588  1.00 116.35 ? 5   SER   R C   1 
ATOM   30368 O  O   . SER   R  4  13  ? 52.355  -211.816 26.632  1.00 119.06 ? 5   SER   R O   1 
ATOM   30369 C  CB  . SER   R  4  13  ? 51.291  -209.697 25.333  1.00 115.26 ? 5   SER   R CB  1 
ATOM   30370 O  OG  . SER   R  4  13  ? 50.937  -208.658 24.432  1.00 113.21 ? 5   SER   R OG  1 
ATOM   30371 N  N   . THR   R  4  14  ? 51.505  -213.412 25.247  1.00 115.84 ? 6   THR   R N   1 
ATOM   30372 C  CA  . THR   R  4  14  ? 51.850  -214.581 26.100  1.00 117.27 ? 6   THR   R CA  1 
ATOM   30373 C  C   . THR   R  4  14  ? 53.278  -215.034 25.784  1.00 111.61 ? 6   THR   R C   1 
ATOM   30374 O  O   . THR   R  4  14  ? 53.664  -214.988 24.601  1.00 106.21 ? 6   THR   R O   1 
ATOM   30375 C  CB  . THR   R  4  14  ? 50.847  -215.730 25.938  1.00 121.21 ? 6   THR   R CB  1 
ATOM   30376 O  OG1 . THR   R  4  14  ? 49.532  -215.182 26.037  1.00 124.84 ? 6   THR   R OG1 1 
ATOM   30377 C  CG2 . THR   R  4  14  ? 51.021  -216.808 26.986  1.00 124.35 ? 6   THR   R CG2 1 
ATOM   30378 N  N   . PHE   R  4  15  ? 54.023  -215.441 26.816  1.00 112.25 ? 7   PHE   R N   1 
ATOM   30379 C  CA  . PHE   R  4  15  ? 55.355  -216.089 26.705  1.00 115.17 ? 7   PHE   R CA  1 
ATOM   30380 C  C   . PHE   R  4  15  ? 55.176  -217.600 26.539  1.00 115.16 ? 7   PHE   R C   1 
ATOM   30381 O  O   . PHE   R  4  15  ? 54.312  -218.190 27.222  1.00 116.01 ? 7   PHE   R O   1 
ATOM   30382 C  CB  . PHE   R  4  15  ? 56.219  -215.813 27.939  1.00 116.15 ? 7   PHE   R CB  1 
ATOM   30383 C  CG  . PHE   R  4  15  ? 56.941  -214.491 27.922  1.00 117.61 ? 7   PHE   R CG  1 
ATOM   30384 C  CD1 . PHE   R  4  15  ? 58.003  -214.277 27.056  1.00 117.00 ? 7   PHE   R CD1 1 
ATOM   30385 C  CD2 . PHE   R  4  15  ? 56.569  -213.465 28.778  1.00 117.03 ? 7   PHE   R CD2 1 
ATOM   30386 C  CE1 . PHE   R  4  15  ? 58.672  -213.063 27.041  1.00 115.21 ? 7   PHE   R CE1 1 
ATOM   30387 C  CE2 . PHE   R  4  15  ? 57.241  -212.253 28.763  1.00 115.85 ? 7   PHE   R CE2 1 
ATOM   30388 C  CZ  . PHE   R  4  15  ? 58.290  -212.054 27.894  1.00 114.74 ? 7   PHE   R CZ  1 
ATOM   30389 N  N   . SER   R  4  16  ? 55.984  -218.208 25.666  1.00 113.58 ? 8   SER   R N   1 
ATOM   30390 C  CA  . SER   R  4  16  ? 56.157  -219.681 25.566  1.00 114.78 ? 8   SER   R CA  1 
ATOM   30391 C  C   . SER   R  4  16  ? 56.955  -220.155 26.777  1.00 114.90 ? 8   SER   R C   1 
ATOM   30392 O  O   . SER   R  4  16  ? 57.564  -219.343 27.471  1.00 110.31 ? 8   SER   R O   1 
ATOM   30393 C  CB  . SER   R  4  16  ? 56.829  -220.077 24.273  1.00 110.69 ? 8   SER   R CB  1 
ATOM   30394 O  OG  . SER   R  4  16  ? 58.238  -219.910 24.358  1.00 105.75 ? 8   SER   R OG  1 
ATOM   30395 N  N   . PRO   R  4  17  ? 56.980  -221.473 27.081  1.00 115.45 ? 9   PRO   R N   1 
ATOM   30396 C  CA  . PRO   R  4  17  ? 57.825  -221.989 28.160  1.00 115.31 ? 9   PRO   R CA  1 
ATOM   30397 C  C   . PRO   R  4  17  ? 59.329  -221.756 27.940  1.00 117.46 ? 9   PRO   R C   1 
ATOM   30398 O  O   . PRO   R  4  17  ? 60.058  -221.774 28.913  1.00 117.42 ? 9   PRO   R O   1 
ATOM   30399 C  CB  . PRO   R  4  17  ? 57.503  -223.489 28.187  1.00 115.41 ? 9   PRO   R CB  1 
ATOM   30400 C  CG  . PRO   R  4  17  ? 56.143  -223.593 27.529  1.00 114.01 ? 9   PRO   R CG  1 
ATOM   30401 C  CD  . PRO   R  4  17  ? 56.156  -222.521 26.461  1.00 113.22 ? 9   PRO   R CD  1 
ATOM   30402 N  N   . GLU   R  4  18  ? 59.750  -221.524 26.690  1.00 120.82 ? 10  GLU   R N   1 
ATOM   30403 C  CA  . GLU   R  4  18  ? 61.167  -221.271 26.307  1.00 127.06 ? 10  GLU   R CA  1 
ATOM   30404 C  C   . GLU   R  4  18  ? 61.495  -219.775 26.439  1.00 127.26 ? 10  GLU   R C   1 
ATOM   30405 O  O   . GLU   R  4  18  ? 62.649  -219.404 26.144  1.00 129.07 ? 10  GLU   R O   1 
ATOM   30406 C  CB  . GLU   R  4  18  ? 61.439  -221.763 24.882  1.00 129.77 ? 10  GLU   R CB  1 
ATOM   30407 C  CG  . GLU   R  4  18  ? 61.356  -223.273 24.727  1.00 134.20 ? 10  GLU   R CG  1 
ATOM   30408 C  CD  . GLU   R  4  18  ? 59.953  -223.835 24.569  1.00 137.02 ? 10  GLU   R CD  1 
ATOM   30409 O  OE1 . GLU   R  4  18  ? 59.635  -224.823 25.259  1.00 143.87 ? 10  GLU   R OE1 1 
ATOM   30410 O  OE2 . GLU   R  4  18  ? 59.185  -223.289 23.751  1.00 140.45 ? 10  GLU   R OE2 1 
ATOM   30411 N  N   . GLY   R  4  19  ? 60.530  -218.951 26.864  1.00 126.44 ? 11  GLY   R N   1 
ATOM   30412 C  CA  . GLY   R  4  19  ? 60.727  -217.516 27.160  1.00 124.14 ? 11  GLY   R CA  1 
ATOM   30413 C  C   . GLY   R  4  19  ? 60.664  -216.642 25.918  1.00 117.32 ? 11  GLY   R C   1 
ATOM   30414 O  O   . GLY   R  4  19  ? 61.359  -215.612 25.898  1.00 116.68 ? 11  GLY   R O   1 
ATOM   30415 N  N   . ARG   R  4  20  ? 59.856  -217.023 24.924  1.00 119.05 ? 12  ARG   R N   1 
ATOM   30416 C  CA  . ARG   R  4  20  ? 59.647  -216.248 23.671  1.00 116.22 ? 12  ARG   R CA  1 
ATOM   30417 C  C   . ARG   R  4  20  ? 58.163  -215.903 23.525  1.00 112.53 ? 12  ARG   R C   1 
ATOM   30418 O  O   . ARG   R  4  20  ? 57.321  -216.682 24.012  1.00 109.36 ? 12  ARG   R O   1 
ATOM   30419 C  CB  . ARG   R  4  20  ? 60.137  -217.041 22.457  1.00 118.79 ? 12  ARG   R CB  1 
ATOM   30420 C  CG  . ARG   R  4  20  ? 61.618  -217.387 22.500  1.00 123.91 ? 12  ARG   R CG  1 
ATOM   30421 C  CD  . ARG   R  4  20  ? 62.190  -217.615 21.114  1.00 126.24 ? 12  ARG   R CD  1 
ATOM   30422 N  NE  . ARG   R  4  20  ? 63.204  -218.663 21.094  1.00 131.85 ? 12  ARG   R NE  1 
ATOM   30423 C  CZ  . ARG   R  4  20  ? 62.962  -219.968 20.957  1.00 135.74 ? 12  ARG   R CZ  1 
ATOM   30424 N  NH1 . ARG   R  4  20  ? 61.725  -220.423 20.827  1.00 137.65 ? 12  ARG   R NH1 1 
ATOM   30425 N  NH2 . ARG   R  4  20  ? 63.970  -220.823 20.953  1.00 138.39 ? 12  ARG   R NH2 1 
ATOM   30426 N  N   . LEU   R  4  21  ? 57.867  -214.775 22.874  1.00 111.52 ? 13  LEU   R N   1 
ATOM   30427 C  CA  . LEU   R  4  21  ? 56.482  -214.303 22.609  1.00 111.20 ? 13  LEU   R CA  1 
ATOM   30428 C  C   . LEU   R  4  21  ? 55.943  -215.020 21.368  1.00 109.62 ? 13  LEU   R C   1 
ATOM   30429 O  O   . LEU   R  4  21  ? 56.514  -214.819 20.276  1.00 105.63 ? 13  LEU   R O   1 
ATOM   30430 C  CB  . LEU   R  4  21  ? 56.486  -212.782 22.422  1.00 111.37 ? 13  LEU   R CB  1 
ATOM   30431 C  CG  . LEU   R  4  21  ? 56.928  -211.973 23.640  1.00 113.02 ? 13  LEU   R CG  1 
ATOM   30432 C  CD1 . LEU   R  4  21  ? 57.123  -210.510 23.274  1.00 112.23 ? 13  LEU   R CD1 1 
ATOM   30433 C  CD2 . LEU   R  4  21  ? 55.931  -212.108 24.782  1.00 114.25 ? 13  LEU   R CD2 1 
ATOM   30434 N  N   . PHE   R  4  22  ? 54.888  -215.822 21.551  1.00 111.67 ? 14  PHE   R N   1 
ATOM   30435 C  CA  . PHE   R  4  22  ? 54.241  -216.667 20.512  1.00 112.03 ? 14  PHE   R CA  1 
ATOM   30436 C  C   . PHE   R  4  22  ? 54.027  -215.852 19.234  1.00 108.67 ? 14  PHE   R C   1 
ATOM   30437 O  O   . PHE   R  4  22  ? 54.506  -216.271 18.164  1.00 109.47 ? 14  PHE   R O   1 
ATOM   30438 C  CB  . PHE   R  4  22  ? 52.910  -217.226 21.023  1.00 113.27 ? 14  PHE   R CB  1 
ATOM   30439 C  CG  . PHE   R  4  22  ? 53.042  -218.404 21.955  1.00 115.41 ? 14  PHE   R CG  1 
ATOM   30440 C  CD1 . PHE   R  4  22  ? 53.462  -219.637 21.481  1.00 114.15 ? 14  PHE   R CD1 1 
ATOM   30441 C  CD2 . PHE   R  4  22  ? 52.743  -218.285 23.305  1.00 118.73 ? 14  PHE   R CD2 1 
ATOM   30442 C  CE1 . PHE   R  4  22  ? 53.584  -220.722 22.334  1.00 115.34 ? 14  PHE   R CE1 1 
ATOM   30443 C  CE2 . PHE   R  4  22  ? 52.864  -219.373 24.157  1.00 119.24 ? 14  PHE   R CE2 1 
ATOM   30444 C  CZ  . PHE   R  4  22  ? 53.283  -220.589 23.670  1.00 118.17 ? 14  PHE   R CZ  1 
ATOM   30445 N  N   . GLN   R  4  23  ? 53.342  -214.713 19.358  1.00 107.63 ? 15  GLN   R N   1 
ATOM   30446 C  CA  . GLN   R  4  23  ? 52.876  -213.890 18.213  1.00 105.61 ? 15  GLN   R CA  1 
ATOM   30447 C  C   . GLN   R  4  23  ? 54.078  -213.319 17.454  1.00 100.77 ? 15  GLN   R C   1 
ATOM   30448 O  O   . GLN   R  4  23  ? 53.984  -213.227 16.218  1.00 101.35 ? 15  GLN   R O   1 
ATOM   30449 C  CB  . GLN   R  4  23  ? 51.927  -212.796 18.702  1.00 106.90 ? 15  GLN   R CB  1 
ATOM   30450 C  CG  . GLN   R  4  23  ? 50.535  -213.323 19.023  1.00 111.31 ? 15  GLN   R CG  1 
ATOM   30451 C  CD  . GLN   R  4  23  ? 49.767  -213.700 17.778  1.00 107.76 ? 15  GLN   R CD  1 
ATOM   30452 O  OE1 . GLN   R  4  23  ? 49.420  -214.857 17.561  1.00 110.57 ? 15  GLN   R OE1 1 
ATOM   30453 N  NE2 . GLN   R  4  23  ? 49.500  -212.714 16.939  1.00 111.10 ? 15  GLN   R NE2 1 
ATOM   30454 N  N   . VAL   R  4  24  ? 55.157  -212.959 18.155  1.00 99.89  ? 16  VAL   R N   1 
ATOM   30455 C  CA  . VAL   R  4  24  ? 56.406  -212.432 17.527  1.00 102.28 ? 16  VAL   R CA  1 
ATOM   30456 C  C   . VAL   R  4  24  ? 57.068  -213.568 16.741  1.00 102.98 ? 16  VAL   R C   1 
ATOM   30457 O  O   . VAL   R  4  24  ? 57.516  -213.317 15.609  1.00 100.56 ? 16  VAL   R O   1 
ATOM   30458 C  CB  . VAL   R  4  24  ? 57.375  -211.828 18.562  1.00 106.17 ? 16  VAL   R CB  1 
ATOM   30459 C  CG1 . VAL   R  4  24  ? 58.712  -211.457 17.935  1.00 108.54 ? 16  VAL   R CG1 1 
ATOM   30460 C  CG2 . VAL   R  4  24  ? 56.769  -210.622 19.265  1.00 106.74 ? 16  VAL   R CG2 1 
ATOM   30461 N  N   . GLU   R  4  25  ? 57.129  -214.766 17.327  1.00 107.21 ? 17  GLU   R N   1 
ATOM   30462 C  CA  . GLU   R  4  25  ? 57.754  -215.966 16.706  1.00 112.13 ? 17  GLU   R CA  1 
ATOM   30463 C  C   . GLU   R  4  25  ? 56.960  -216.390 15.465  1.00 109.52 ? 17  GLU   R C   1 
ATOM   30464 O  O   . GLU   R  4  25  ? 57.598  -216.795 14.474  1.00 105.93 ? 17  GLU   R O   1 
ATOM   30465 C  CB  . GLU   R  4  25  ? 57.838  -217.111 17.716  1.00 115.54 ? 17  GLU   R CB  1 
ATOM   30466 C  CG  . GLU   R  4  25  ? 58.854  -216.866 18.816  1.00 120.28 ? 17  GLU   R CG  1 
ATOM   30467 C  CD  . GLU   R  4  25  ? 60.287  -216.704 18.330  1.00 126.42 ? 17  GLU   R CD  1 
ATOM   30468 O  OE1 . GLU   R  4  25  ? 60.828  -215.583 18.442  1.00 126.14 ? 17  GLU   R OE1 1 
ATOM   30469 O  OE2 . GLU   R  4  25  ? 60.861  -217.700 17.843  1.00 129.01 ? 17  GLU   R OE2 1 
ATOM   30470 N  N   . TYR   R  4  26  ? 55.626  -216.306 15.519  1.00 111.51 ? 18  TYR   R N   1 
ATOM   30471 C  CA  . TYR   R  4  26  ? 54.717  -216.698 14.408  1.00 111.87 ? 18  TYR   R CA  1 
ATOM   30472 C  C   . TYR   R  4  26  ? 54.817  -215.680 13.263  1.00 112.10 ? 18  TYR   R C   1 
ATOM   30473 O  O   . TYR   R  4  26  ? 54.738  -216.102 12.095  1.00 107.62 ? 18  TYR   R O   1 
ATOM   30474 C  CB  . TYR   R  4  26  ? 53.271  -216.847 14.890  1.00 111.37 ? 18  TYR   R CB  1 
ATOM   30475 C  CG  . TYR   R  4  26  ? 53.019  -217.910 15.933  1.00 111.32 ? 18  TYR   R CG  1 
ATOM   30476 C  CD1 . TYR   R  4  26  ? 53.946  -218.904 16.214  1.00 110.01 ? 18  TYR   R CD1 1 
ATOM   30477 C  CD2 . TYR   R  4  26  ? 51.818  -217.938 16.626  1.00 110.39 ? 18  TYR   R CD2 1 
ATOM   30478 C  CE1 . TYR   R  4  26  ? 53.696  -219.879 17.167  1.00 111.81 ? 18  TYR   R CE1 1 
ATOM   30479 C  CE2 . TYR   R  4  26  ? 51.552  -218.905 17.582  1.00 110.97 ? 18  TYR   R CE2 1 
ATOM   30480 C  CZ  . TYR   R  4  26  ? 52.494  -219.881 17.853  1.00 110.97 ? 18  TYR   R CZ  1 
ATOM   30481 O  OH  . TYR   R  4  26  ? 52.230  -220.836 18.793  1.00 112.50 ? 18  TYR   R OH  1 
ATOM   30482 N  N   . SER   R  4  27  ? 54.982  -214.388 13.571  1.00 113.16 ? 19  SER   R N   1 
ATOM   30483 C  CA  . SER   R  4  27  ? 55.135  -213.307 12.559  1.00 114.49 ? 19  SER   R CA  1 
ATOM   30484 C  C   . SER   R  4  27  ? 56.455  -213.490 11.796  1.00 115.57 ? 19  SER   R C   1 
ATOM   30485 O  O   . SER   R  4  27  ? 56.502  -213.109 10.612  1.00 120.67 ? 19  SER   R O   1 
ATOM   30486 C  CB  . SER   R  4  27  ? 55.033  -211.932 13.175  1.00 115.27 ? 19  SER   R CB  1 
ATOM   30487 O  OG  . SER   R  4  27  ? 56.121  -211.678 14.051  1.00 118.09 ? 19  SER   R OG  1 
ATOM   30488 N  N   . LEU   R  4  28  ? 57.481  -214.051 12.449  1.00 115.21 ? 20  LEU   R N   1 
ATOM   30489 C  CA  . LEU   R  4  28  ? 58.794  -214.386 11.828  1.00 114.18 ? 20  LEU   R CA  1 
ATOM   30490 C  C   . LEU   R  4  28  ? 58.603  -215.465 10.754  1.00 115.21 ? 20  LEU   R C   1 
ATOM   30491 O  O   . LEU   R  4  28  ? 59.390  -215.462 9.787   1.00 106.43 ? 20  LEU   R O   1 
ATOM   30492 C  CB  . LEU   R  4  28  ? 59.776  -214.856 12.909  1.00 117.55 ? 20  LEU   R CB  1 
ATOM   30493 C  CG  . LEU   R  4  28  ? 60.724  -213.804 13.494  1.00 119.47 ? 20  LEU   R CG  1 
ATOM   30494 C  CD1 . LEU   R  4  28  ? 60.124  -212.404 13.482  1.00 118.26 ? 20  LEU   R CD1 1 
ATOM   30495 C  CD2 . LEU   R  4  28  ? 61.133  -214.188 14.909  1.00 120.56 ? 20  LEU   R CD2 1 
ATOM   30496 N  N   . GLU   R  4  29  ? 57.613  -216.351 10.918  1.00 118.72 ? 21  GLU   R N   1 
ATOM   30497 C  CA  . GLU   R  4  29  ? 57.266  -217.407 9.924   1.00 122.71 ? 21  GLU   R CA  1 
ATOM   30498 C  C   . GLU   R  4  29  ? 56.615  -216.758 8.696   1.00 119.26 ? 21  GLU   R C   1 
ATOM   30499 O  O   . GLU   R  4  29  ? 56.917  -217.202 7.572   1.00 123.93 ? 21  GLU   R O   1 
ATOM   30500 C  CB  . GLU   R  4  29  ? 56.336  -218.469 10.519  1.00 124.30 ? 21  GLU   R CB  1 
ATOM   30501 C  CG  . GLU   R  4  29  ? 56.997  -219.355 11.560  1.00 127.88 ? 21  GLU   R CG  1 
ATOM   30502 C  CD  . GLU   R  4  29  ? 58.226  -220.107 11.077  1.00 130.90 ? 21  GLU   R CD  1 
ATOM   30503 O  OE1 . GLU   R  4  29  ? 59.115  -220.374 11.909  1.00 138.43 ? 21  GLU   R OE1 1 
ATOM   30504 O  OE2 . GLU   R  4  29  ? 58.291  -220.426 9.872   1.00 134.42 ? 21  GLU   R OE2 1 
ATOM   30505 N  N   . ALA   R  4  30  ? 55.750  -215.760 8.906   1.00 115.78 ? 22  ALA   R N   1 
ATOM   30506 C  CA  . ALA   R  4  30  ? 55.082  -214.983 7.835   1.00 113.30 ? 22  ALA   R CA  1 
ATOM   30507 C  C   . ALA   R  4  30  ? 56.142  -214.331 6.937   1.00 112.24 ? 22  ALA   R C   1 
ATOM   30508 O  O   . ALA   R  4  30  ? 55.946  -214.322 5.705   1.00 109.99 ? 22  ALA   R O   1 
ATOM   30509 C  CB  . ALA   R  4  30  ? 54.156  -213.953 8.434   1.00 113.00 ? 22  ALA   R CB  1 
ATOM   30510 N  N   . ILE   R  4  31  ? 57.225  -213.823 7.538   1.00 111.71 ? 23  ILE   R N   1 
ATOM   30511 C  CA  . ILE   R  4  31  ? 58.321  -213.084 6.838   1.00 110.71 ? 23  ILE   R CA  1 
ATOM   30512 C  C   . ILE   R  4  31  ? 59.122  -214.063 5.971   1.00 111.06 ? 23  ILE   R C   1 
ATOM   30513 O  O   . ILE   R  4  31  ? 59.558  -213.649 4.879   1.00 108.68 ? 23  ILE   R O   1 
ATOM   30514 C  CB  . ILE   R  4  31  ? 59.214  -212.326 7.844   1.00 109.86 ? 23  ILE   R CB  1 
ATOM   30515 C  CG1 . ILE   R  4  31  ? 58.423  -211.235 8.572   1.00 109.25 ? 23  ILE   R CG1 1 
ATOM   30516 C  CG2 . ILE   R  4  31  ? 60.450  -211.755 7.160   1.00 108.34 ? 23  ILE   R CG2 1 
ATOM   30517 C  CD1 . ILE   R  4  31  ? 59.081  -210.723 9.831   1.00 110.83 ? 23  ILE   R CD1 1 
ATOM   30518 N  N   . LYS   R  4  32  ? 59.299  -215.308 6.428   1.00 113.49 ? 24  LYS   R N   1 
ATOM   30519 C  CA  . LYS   R  4  32  ? 60.004  -216.377 5.668   1.00 114.33 ? 24  LYS   R CA  1 
ATOM   30520 C  C   . LYS   R  4  32  ? 59.246  -216.674 4.365   1.00 112.98 ? 24  LYS   R C   1 
ATOM   30521 O  O   . LYS   R  4  32  ? 59.907  -217.069 3.395   1.00 109.41 ? 24  LYS   R O   1 
ATOM   30522 C  CB  . LYS   R  4  32  ? 60.170  -217.643 6.516   1.00 117.01 ? 24  LYS   R CB  1 
ATOM   30523 C  CG  . LYS   R  4  32  ? 61.211  -217.548 7.624   1.00 118.58 ? 24  LYS   R CG  1 
ATOM   30524 C  CD  . LYS   R  4  32  ? 61.387  -218.837 8.399   1.00 119.93 ? 24  LYS   R CD  1 
ATOM   30525 C  CE  . LYS   R  4  32  ? 62.081  -218.641 9.731   1.00 119.45 ? 24  LYS   R CE  1 
ATOM   30526 N  NZ  . LYS   R  4  32  ? 62.098  -219.891 10.525  1.00 119.85 ? 24  LYS   R NZ  1 
ATOM   30527 N  N   . LEU   R  4  33  ? 57.921  -216.485 4.339   1.00 115.51 ? 25  LEU   R N   1 
ATOM   30528 C  CA  . LEU   R  4  33  ? 57.076  -216.694 3.129   1.00 119.07 ? 25  LEU   R CA  1 
ATOM   30529 C  C   . LEU   R  4  33  ? 57.225  -215.506 2.167   1.00 115.40 ? 25  LEU   R C   1 
ATOM   30530 O  O   . LEU   R  4  33  ? 56.918  -215.683 0.973   1.00 109.71 ? 25  LEU   R O   1 
ATOM   30531 C  CB  . LEU   R  4  33  ? 55.610  -216.887 3.538   1.00 125.27 ? 25  LEU   R CB  1 
ATOM   30532 C  CG  . LEU   R  4  33  ? 55.295  -218.159 4.327   1.00 129.49 ? 25  LEU   R CG  1 
ATOM   30533 C  CD1 . LEU   R  4  33  ? 53.891  -218.098 4.914   1.00 133.85 ? 25  LEU   R CD1 1 
ATOM   30534 C  CD2 . LEU   R  4  33  ? 55.455  -219.402 3.462   1.00 126.55 ? 25  LEU   R CD2 1 
ATOM   30535 N  N   . GLY   R  4  34  ? 57.679  -214.348 2.659   1.00 115.56 ? 26  GLY   R N   1 
ATOM   30536 C  CA  . GLY   R  4  34  ? 57.847  -213.112 1.867   1.00 112.48 ? 26  GLY   R CA  1 
ATOM   30537 C  C   . GLY   R  4  34  ? 58.867  -213.271 0.749   1.00 110.61 ? 26  GLY   R C   1 
ATOM   30538 O  O   . GLY   R  4  34  ? 59.621  -214.266 0.767   1.00 109.31 ? 26  GLY   R O   1 
ATOM   30539 N  N   . SER   R  4  35  ? 58.891  -212.320 -0.191  1.00 109.14 ? 27  SER   R N   1 
ATOM   30540 C  CA  . SER   R  4  35  ? 59.834  -212.274 -1.339  1.00 110.02 ? 27  SER   R CA  1 
ATOM   30541 C  C   . SER   R  4  35  ? 61.202  -211.790 -0.848  1.00 110.49 ? 27  SER   R C   1 
ATOM   30542 O  O   . SER   R  4  35  ? 61.233  -211.017 0.128   1.00 112.71 ? 27  SER   R O   1 
ATOM   30543 C  CB  . SER   R  4  35  ? 59.299  -211.404 -2.448  1.00 114.28 ? 27  SER   R CB  1 
ATOM   30544 O  OG  . SER   R  4  35  ? 59.150  -210.059 -2.017  1.00 115.54 ? 27  SER   R OG  1 
ATOM   30545 N  N   . THR   R  4  36  ? 62.288  -212.231 -1.492  1.00 110.44 ? 28  THR   R N   1 
ATOM   30546 C  CA  . THR   R  4  36  ? 63.682  -211.955 -1.051  1.00 115.22 ? 28  THR   R CA  1 
ATOM   30547 C  C   . THR   R  4  36  ? 63.992  -210.461 -1.203  1.00 113.70 ? 28  THR   R C   1 
ATOM   30548 O  O   . THR   R  4  36  ? 63.606  -209.873 -2.234  1.00 117.97 ? 28  THR   R O   1 
ATOM   30549 C  CB  . THR   R  4  36  ? 64.714  -212.799 -1.808  1.00 119.61 ? 28  THR   R CB  1 
ATOM   30550 O  OG1 . THR   R  4  36  ? 64.319  -214.168 -1.720  1.00 124.54 ? 28  THR   R OG1 1 
ATOM   30551 C  CG2 . THR   R  4  36  ? 66.113  -212.631 -1.254  1.00 120.18 ? 28  THR   R CG2 1 
ATOM   30552 N  N   . ALA   R  4  37  ? 64.659  -209.888 -0.199  1.00 110.46 ? 29  ALA   R N   1 
ATOM   30553 C  CA  . ALA   R  4  37  ? 65.233  -208.523 -0.210  1.00 108.56 ? 29  ALA   R CA  1 
ATOM   30554 C  C   . ALA   R  4  37  ? 66.669  -208.593 0.317   1.00 106.94 ? 29  ALA   R C   1 
ATOM   30555 O  O   . ALA   R  4  37  ? 66.874  -209.185 1.393   1.00 104.37 ? 29  ALA   R O   1 
ATOM   30556 C  CB  . ALA   R  4  37  ? 64.378  -207.597 0.618   1.00 107.90 ? 29  ALA   R CB  1 
ATOM   30557 N  N   . ILE   R  4  38  ? 67.623  -208.029 -0.429  1.00 107.94 ? 30  ILE   R N   1 
ATOM   30558 C  CA  . ILE   R  4  38  ? 69.079  -208.050 -0.096  1.00 109.52 ? 30  ILE   R CA  1 
ATOM   30559 C  C   . ILE   R  4  38  ? 69.584  -206.605 0.001   1.00 110.04 ? 30  ILE   R C   1 
ATOM   30560 O  O   . ILE   R  4  38  ? 69.186  -205.775 -0.842  1.00 108.43 ? 30  ILE   R O   1 
ATOM   30561 C  CB  . ILE   R  4  38  ? 69.865  -208.882 -1.131  1.00 109.92 ? 30  ILE   R CB  1 
ATOM   30562 C  CG1 . ILE   R  4  38  ? 69.422  -210.348 -1.109  1.00 110.78 ? 30  ILE   R CG1 1 
ATOM   30563 C  CG2 . ILE   R  4  38  ? 71.367  -208.747 -0.918  1.00 110.52 ? 30  ILE   R CG2 1 
ATOM   30564 C  CD1 . ILE   R  4  38  ? 69.930  -211.171 -2.269  1.00 113.61 ? 30  ILE   R CD1 1 
ATOM   30565 N  N   . GLY   R  4  39  ? 70.419  -206.331 1.007   1.00 109.29 ? 31  GLY   R N   1 
ATOM   30566 C  CA  . GLY   R  4  39  ? 71.135  -205.054 1.188   1.00 109.69 ? 31  GLY   R CA  1 
ATOM   30567 C  C   . GLY   R  4  39  ? 72.613  -205.291 1.441   1.00 112.40 ? 31  GLY   R C   1 
ATOM   30568 O  O   . GLY   R  4  39  ? 72.927  -206.174 2.261   1.00 111.79 ? 31  GLY   R O   1 
ATOM   30569 N  N   . ILE   R  4  40  ? 73.486  -204.555 0.745   1.00 116.23 ? 32  ILE   R N   1 
ATOM   30570 C  CA  . ILE   R  4  40  ? 74.969  -204.582 0.933   1.00 117.91 ? 32  ILE   R CA  1 
ATOM   30571 C  C   . ILE   R  4  40  ? 75.448  -203.147 1.183   1.00 117.81 ? 32  ILE   R C   1 
ATOM   30572 O  O   . ILE   R  4  40  ? 75.055  -202.252 0.409   1.00 116.15 ? 32  ILE   R O   1 
ATOM   30573 C  CB  . ILE   R  4  40  ? 75.684  -205.223 -0.276  1.00 118.23 ? 32  ILE   R CB  1 
ATOM   30574 C  CG1 . ILE   R  4  40  ? 75.214  -206.661 -0.513  1.00 118.23 ? 32  ILE   R CG1 1 
ATOM   30575 C  CG2 . ILE   R  4  40  ? 77.197  -205.145 -0.112  1.00 117.20 ? 32  ILE   R CG2 1 
ATOM   30576 C  CD1 . ILE   R  4  40  ? 75.765  -207.296 -1.770  1.00 121.36 ? 32  ILE   R CD1 1 
ATOM   30577 N  N   . ALA   R  4  41  ? 76.269  -202.953 2.221   1.00 119.89 ? 33  ALA   R N   1 
ATOM   30578 C  CA  . ALA   R  4  41  ? 76.871  -201.657 2.616   1.00 118.82 ? 33  ALA   R CA  1 
ATOM   30579 C  C   . ALA   R  4  41  ? 78.324  -201.600 2.135   1.00 122.81 ? 33  ALA   R C   1 
ATOM   30580 O  O   . ALA   R  4  41  ? 79.068  -202.554 2.413   1.00 125.17 ? 33  ALA   R O   1 
ATOM   30581 C  CB  . ALA   R  4  41  ? 76.795  -201.491 4.113   1.00 118.26 ? 33  ALA   R CB  1 
ATOM   30582 N  N   . THR   R  4  42  ? 78.702  -200.523 1.442   1.00 126.93 ? 34  THR   R N   1 
ATOM   30583 C  CA  . THR   R  4  42  ? 80.100  -200.218 1.033   1.00 130.25 ? 34  THR   R CA  1 
ATOM   30584 C  C   . THR   R  4  42  ? 80.486  -198.839 1.578   1.00 130.62 ? 34  THR   R C   1 
ATOM   30585 O  O   . THR   R  4  42  ? 79.621  -198.184 2.195   1.00 127.13 ? 34  THR   R O   1 
ATOM   30586 C  CB  . THR   R  4  42  ? 80.281  -200.276 -0.491  1.00 134.30 ? 34  THR   R CB  1 
ATOM   30587 O  OG1 . THR   R  4  42  ? 79.626  -199.153 -1.083  1.00 137.48 ? 34  THR   R OG1 1 
ATOM   30588 C  CG2 . THR   R  4  42  ? 79.753  -201.554 -1.107  1.00 133.84 ? 34  THR   R CG2 1 
ATOM   30589 N  N   . LYS   R  4  43  ? 81.735  -198.425 1.351   1.00 131.65 ? 35  LYS   R N   1 
ATOM   30590 C  CA  . LYS   R  4  43  ? 82.246  -197.073 1.703   1.00 130.60 ? 35  LYS   R CA  1 
ATOM   30591 C  C   . LYS   R  4  43  ? 81.877  -196.074 0.597   1.00 130.13 ? 35  LYS   R C   1 
ATOM   30592 O  O   . LYS   R  4  43  ? 82.027  -194.862 0.838   1.00 128.50 ? 35  LYS   R O   1 
ATOM   30593 C  CB  . LYS   R  4  43  ? 83.757  -197.123 1.948   1.00 131.85 ? 35  LYS   R CB  1 
ATOM   30594 C  CG  . LYS   R  4  43  ? 84.161  -197.779 3.261   1.00 134.17 ? 35  LYS   R CG  1 
ATOM   30595 C  CD  . LYS   R  4  43  ? 85.569  -197.446 3.704   1.00 137.78 ? 35  LYS   R CD  1 
ATOM   30596 C  CE  . LYS   R  4  43  ? 85.808  -197.725 5.173   1.00 138.67 ? 35  LYS   R CE  1 
ATOM   30597 N  NZ  . LYS   R  4  43  ? 85.797  -199.177 5.468   1.00 139.59 ? 35  LYS   R NZ  1 
ATOM   30598 N  N   . GLU   R  4  44  ? 81.408  -196.559 -0.561  1.00 129.94 ? 36  GLU   R N   1 
ATOM   30599 C  CA  . GLU   R  4  44  ? 80.940  -195.723 -1.701  1.00 132.32 ? 36  GLU   R CA  1 
ATOM   30600 C  C   . GLU   R  4  44  ? 79.410  -195.582 -1.679  1.00 130.47 ? 36  GLU   R C   1 
ATOM   30601 O  O   . GLU   R  4  44  ? 78.897  -194.745 -2.450  1.00 132.43 ? 36  GLU   R O   1 
ATOM   30602 C  CB  . GLU   R  4  44  ? 81.387  -196.325 -3.036  1.00 133.54 ? 36  GLU   R CB  1 
ATOM   30603 C  CG  . GLU   R  4  44  ? 82.880  -196.211 -3.294  1.00 135.58 ? 36  GLU   R CG  1 
ATOM   30604 C  CD  . GLU   R  4  44  ? 83.350  -196.846 -4.594  1.00 133.74 ? 36  GLU   R CD  1 
ATOM   30605 O  OE1 . GLU   R  4  44  ? 82.490  -197.244 -5.408  1.00 128.37 ? 36  GLU   R OE1 1 
ATOM   30606 O  OE2 . GLU   R  4  44  ? 84.577  -196.949 -4.790  1.00 136.03 ? 36  GLU   R OE2 1 
ATOM   30607 N  N   . GLY   R  4  45  ? 78.709  -196.366 -0.852  1.00 127.65 ? 37  GLY   R N   1 
ATOM   30608 C  CA  . GLY   R  4  45  ? 77.237  -196.317 -0.726  1.00 127.25 ? 37  GLY   R CA  1 
ATOM   30609 C  C   . GLY   R  4  45  ? 76.649  -197.636 -0.255  1.00 126.23 ? 37  GLY   R C   1 
ATOM   30610 O  O   . GLY   R  4  45  ? 77.409  -198.613 -0.131  1.00 132.63 ? 37  GLY   R O   1 
ATOM   30611 N  N   . VAL   R  4  46  ? 75.338  -197.655 0.008   1.00 123.61 ? 38  VAL   R N   1 
ATOM   30612 C  CA  . VAL   R  4  46  ? 74.554  -198.880 0.351   1.00 120.55 ? 38  VAL   R CA  1 
ATOM   30613 C  C   . VAL   R  4  46  ? 73.647  -199.208 -0.839  1.00 122.15 ? 38  VAL   R C   1 
ATOM   30614 O  O   . VAL   R  4  46  ? 73.041  -198.267 -1.386  1.00 124.61 ? 38  VAL   R O   1 
ATOM   30615 C  CB  . VAL   R  4  46  ? 73.727  -198.699 1.639   1.00 117.28 ? 38  VAL   R CB  1 
ATOM   30616 C  CG1 . VAL   R  4  46  ? 73.168  -200.026 2.127   1.00 117.21 ? 38  VAL   R CG1 1 
ATOM   30617 C  CG2 . VAL   R  4  46  ? 74.522  -198.023 2.744   1.00 115.90 ? 38  VAL   R CG2 1 
ATOM   30618 N  N   . VAL   R  4  47  ? 73.562  -200.488 -1.214  1.00 119.84 ? 39  VAL   R N   1 
ATOM   30619 C  CA  . VAL   R  4  47  ? 72.682  -200.995 -2.310  1.00 117.83 ? 39  VAL   R CA  1 
ATOM   30620 C  C   . VAL   R  4  47  ? 71.546  -201.813 -1.687  1.00 115.68 ? 39  VAL   R C   1 
ATOM   30621 O  O   . VAL   R  4  47  ? 71.833  -202.654 -0.816  1.00 112.69 ? 39  VAL   R O   1 
ATOM   30622 C  CB  . VAL   R  4  47  ? 73.467  -201.828 -3.339  1.00 121.13 ? 39  VAL   R CB  1 
ATOM   30623 C  CG1 . VAL   R  4  47  ? 72.555  -202.401 -4.416  1.00 122.35 ? 39  VAL   R CG1 1 
ATOM   30624 C  CG2 . VAL   R  4  47  ? 74.597  -201.026 -3.967  1.00 120.93 ? 39  VAL   R CG2 1 
ATOM   30625 N  N   . LEU   R  4  48  ? 70.312  -201.563 -2.134  1.00 114.92 ? 40  LEU   R N   1 
ATOM   30626 C  CA  . LEU   R  4  48  ? 69.082  -202.300 -1.743  1.00 112.68 ? 40  LEU   R CA  1 
ATOM   30627 C  C   . LEU   R  4  48  ? 68.461  -202.903 -3.006  1.00 113.21 ? 40  LEU   R C   1 
ATOM   30628 O  O   . LEU   R  4  48  ? 68.166  -202.136 -3.942  1.00 112.76 ? 40  LEU   R O   1 
ATOM   30629 C  CB  . LEU   R  4  48  ? 68.113  -201.331 -1.053  1.00 112.84 ? 40  LEU   R CB  1 
ATOM   30630 C  CG  . LEU   R  4  48  ? 67.928  -201.499 0.457   1.00 112.36 ? 40  LEU   R CG  1 
ATOM   30631 C  CD1 . LEU   R  4  48  ? 69.255  -201.670 1.183   1.00 113.26 ? 40  LEU   R CD1 1 
ATOM   30632 C  CD2 . LEU   R  4  48  ? 67.166  -200.314 1.030   1.00 111.72 ? 40  LEU   R CD2 1 
ATOM   30633 N  N   . GLY   R  4  49  ? 68.296  -204.228 -3.031  1.00 113.43 ? 41  GLY   R N   1 
ATOM   30634 C  CA  . GLY   R  4  49  ? 67.656  -204.971 -4.134  1.00 114.98 ? 41  GLY   R CA  1 
ATOM   30635 C  C   . GLY   R  4  49  ? 66.563  -205.886 -3.614  1.00 114.25 ? 41  GLY   R C   1 
ATOM   30636 O  O   . GLY   R  4  49  ? 66.730  -206.419 -2.499  1.00 115.61 ? 41  GLY   R O   1 
ATOM   30637 N  N   . VAL   R  4  50  ? 65.481  -206.055 -4.380  1.00 113.30 ? 42  VAL   R N   1 
ATOM   30638 C  CA  . VAL   R  4  50  ? 64.319  -206.913 -4.001  1.00 113.15 ? 42  VAL   R CA  1 
ATOM   30639 C  C   . VAL   R  4  50  ? 63.877  -207.748 -5.205  1.00 112.16 ? 42  VAL   R C   1 
ATOM   30640 O  O   . VAL   R  4  50  ? 64.035  -207.288 -6.351  1.00 107.12 ? 42  VAL   R O   1 
ATOM   30641 C  CB  . VAL   R  4  50  ? 63.139  -206.086 -3.452  1.00 113.64 ? 42  VAL   R CB  1 
ATOM   30642 C  CG1 . VAL   R  4  50  ? 63.516  -205.340 -2.183  1.00 115.03 ? 42  VAL   R CG1 1 
ATOM   30643 C  CG2 . VAL   R  4  50  ? 62.570  -205.129 -4.488  1.00 113.88 ? 42  VAL   R CG2 1 
ATOM   30644 N  N   . GLU   R  4  51  ? 63.340  -208.935 -4.920  1.00 115.20 ? 43  GLU   R N   1 
ATOM   30645 C  CA  . GLU   R  4  51  ? 62.536  -209.758 -5.857  1.00 117.29 ? 43  GLU   R CA  1 
ATOM   30646 C  C   . GLU   R  4  51  ? 61.107  -209.202 -5.842  1.00 115.78 ? 43  GLU   R C   1 
ATOM   30647 O  O   . GLU   R  4  51  ? 60.535  -209.085 -4.740  1.00 117.04 ? 43  GLU   R O   1 
ATOM   30648 C  CB  . GLU   R  4  51  ? 62.602  -211.229 -5.432  1.00 120.87 ? 43  GLU   R CB  1 
ATOM   30649 C  CG  . GLU   R  4  51  ? 61.585  -212.127 -6.117  1.00 122.83 ? 43  GLU   R CG  1 
ATOM   30650 C  CD  . GLU   R  4  51  ? 61.366  -213.472 -5.446  1.00 122.78 ? 43  GLU   R CD  1 
ATOM   30651 O  OE1 . GLU   R  4  51  ? 60.658  -214.307 -6.035  1.00 128.19 ? 43  GLU   R OE1 1 
ATOM   30652 O  OE2 . GLU   R  4  51  ? 61.901  -213.681 -4.338  1.00 123.09 ? 43  GLU   R OE2 1 
ATOM   30653 N  N   . LYS   R  4  52  ? 60.564  -208.850 -7.009  1.00 113.33 ? 44  LYS   R N   1 
ATOM   30654 C  CA  . LYS   R  4  52  ? 59.185  -208.308 -7.145  1.00 112.45 ? 44  LYS   R CA  1 
ATOM   30655 C  C   . LYS   R  4  52  ? 58.172  -209.445 -6.977  1.00 113.37 ? 44  LYS   R C   1 
ATOM   30656 O  O   . LYS   R  4  52  ? 57.230  -209.275 -6.177  1.00 104.04 ? 44  LYS   R O   1 
ATOM   30657 C  CB  . LYS   R  4  52  ? 59.018  -207.595 -8.489  1.00 112.77 ? 44  LYS   R CB  1 
ATOM   30658 C  CG  . LYS   R  4  52  ? 59.749  -206.265 -8.592  1.00 111.62 ? 44  LYS   R CG  1 
ATOM   30659 C  CD  . LYS   R  4  52  ? 59.218  -205.377 -9.686  1.00 113.68 ? 44  LYS   R CD  1 
ATOM   30660 C  CE  . LYS   R  4  52  ? 59.971  -204.071 -9.799  1.00 116.15 ? 44  LYS   R CE  1 
ATOM   30661 N  NZ  . LYS   R  4  52  ? 59.378  -203.199 -10.838 1.00 118.42 ? 44  LYS   R NZ  1 
ATOM   30662 N  N   . ARG   R  4  53  ? 58.369  -210.554 -7.701  1.00 118.43 ? 45  ARG   R N   1 
ATOM   30663 C  CA  . ARG   R  4  53  ? 57.529  -211.783 -7.632  1.00 120.83 ? 45  ARG   R CA  1 
ATOM   30664 C  C   . ARG   R  4  53  ? 56.063  -211.420 -7.908  1.00 119.02 ? 45  ARG   R C   1 
ATOM   30665 O  O   . ARG   R  4  53  ? 55.274  -211.355 -6.944  1.00 119.02 ? 45  ARG   R O   1 
ATOM   30666 C  CB  . ARG   R  4  53  ? 57.693  -212.462 -6.266  1.00 122.75 ? 45  ARG   R CB  1 
ATOM   30667 C  CG  . ARG   R  4  53  ? 57.015  -213.820 -6.152  1.00 123.40 ? 45  ARG   R CG  1 
ATOM   30668 C  CD  . ARG   R  4  53  ? 56.801  -214.249 -4.711  1.00 125.20 ? 45  ARG   R CD  1 
ATOM   30669 N  NE  . ARG   R  4  53  ? 58.004  -214.804 -4.103  1.00 126.30 ? 45  ARG   R NE  1 
ATOM   30670 C  CZ  . ARG   R  4  53  ? 58.145  -215.091 -2.810  1.00 125.61 ? 45  ARG   R CZ  1 
ATOM   30671 N  NH1 . ARG   R  4  53  ? 57.160  -214.861 -1.957  1.00 129.66 ? 45  ARG   R NH1 1 
ATOM   30672 N  NH2 . ARG   R  4  53  ? 59.284  -215.601 -2.371  1.00 123.46 ? 45  ARG   R NH2 1 
ATOM   30673 N  N   . ALA   R  4  54  ? 55.719  -211.189 -9.178  1.00 119.60 ? 46  ALA   R N   1 
ATOM   30674 C  CA  . ALA   R  4  54  ? 54.332  -210.974 -9.653  1.00 120.64 ? 46  ALA   R CA  1 
ATOM   30675 C  C   . ALA   R  4  54  ? 53.585  -212.312 -9.635  1.00 123.17 ? 46  ALA   R C   1 
ATOM   30676 O  O   . ALA   R  4  54  ? 54.104  -213.278 -10.230 1.00 126.78 ? 46  ALA   R O   1 
ATOM   30677 C  CB  . ALA   R  4  54  ? 54.343  -210.376 -11.038 1.00 119.09 ? 46  ALA   R CB  1 
ATOM   30678 N  N   . THR   R  4  55  ? 52.413  -212.359 -8.991  1.00 125.94 ? 47  THR   R N   1 
ATOM   30679 C  CA  . THR   R  4  55  ? 51.588  -213.587 -8.810  1.00 125.56 ? 47  THR   R CA  1 
ATOM   30680 C  C   . THR   R  4  55  ? 51.027  -214.058 -10.158 1.00 128.88 ? 47  THR   R C   1 
ATOM   30681 O  O   . THR   R  4  55  ? 50.716  -215.262 -10.271 1.00 129.38 ? 47  THR   R O   1 
ATOM   30682 C  CB  . THR   R  4  55  ? 50.458  -213.363 -7.797  1.00 125.44 ? 47  THR   R CB  1 
ATOM   30683 O  OG1 . THR   R  4  55  ? 49.732  -212.199 -8.192  1.00 121.65 ? 47  THR   R OG1 1 
ATOM   30684 C  CG2 . THR   R  4  55  ? 50.966  -213.199 -6.381  1.00 125.25 ? 47  THR   R CG2 1 
ATOM   30685 N  N   . SER   R  4  56  ? 50.902  -213.153 -11.135 1.00 128.52 ? 48  SER   R N   1 
ATOM   30686 C  CA  . SER   R  4  56  ? 50.342  -213.430 -12.484 1.00 129.81 ? 48  SER   R CA  1 
ATOM   30687 C  C   . SER   R  4  56  ? 51.038  -212.563 -13.532 1.00 127.87 ? 48  SER   R C   1 
ATOM   30688 O  O   . SER   R  4  56  ? 51.503  -211.469 -13.221 1.00 123.21 ? 48  SER   R O   1 
ATOM   30689 C  CB  . SER   R  4  56  ? 48.847  -213.219 -12.471 1.00 129.76 ? 48  SER   R CB  1 
ATOM   30690 O  OG  . SER   R  4  56  ? 48.309  -213.166 -13.786 1.00 129.24 ? 48  SER   R OG  1 
ATOM   30691 N  N   . PRO   R  4  57  ? 51.159  -213.033 -14.798 1.00 133.19 ? 49  PRO   R N   1 
ATOM   30692 C  CA  . PRO   R  4  57  ? 51.763  -212.233 -15.868 1.00 131.77 ? 49  PRO   R CA  1 
ATOM   30693 C  C   . PRO   R  4  57  ? 50.988  -210.975 -16.302 1.00 132.06 ? 49  PRO   R C   1 
ATOM   30694 O  O   . PRO   R  4  57  ? 51.602  -210.122 -16.917 1.00 128.45 ? 49  PRO   R O   1 
ATOM   30695 C  CB  . PRO   R  4  57  ? 51.837  -213.208 -17.055 1.00 134.91 ? 49  PRO   R CB  1 
ATOM   30696 C  CG  . PRO   R  4  57  ? 50.775  -214.245 -16.761 1.00 136.42 ? 49  PRO   R CG  1 
ATOM   30697 C  CD  . PRO   R  4  57  ? 50.782  -214.381 -15.253 1.00 135.14 ? 49  PRO   R CD  1 
ATOM   30698 N  N   . LEU   R  4  58  ? 49.686  -210.888 -16.001 1.00 130.34 ? 50  LEU   R N   1 
ATOM   30699 C  CA  . LEU   R  4  58  ? 48.818  -209.730 -16.368 1.00 130.27 ? 50  LEU   R CA  1 
ATOM   30700 C  C   . LEU   R  4  58  ? 49.074  -208.542 -15.427 1.00 125.77 ? 50  LEU   R C   1 
ATOM   30701 O  O   . LEU   R  4  58  ? 48.788  -207.399 -15.840 1.00 126.12 ? 50  LEU   R O   1 
ATOM   30702 C  CB  . LEU   R  4  58  ? 47.343  -210.152 -16.332 1.00 130.28 ? 50  LEU   R CB  1 
ATOM   30703 C  CG  . LEU   R  4  58  ? 46.827  -210.864 -17.582 1.00 132.53 ? 50  LEU   R CG  1 
ATOM   30704 C  CD1 . LEU   R  4  58  ? 45.449  -211.460 -17.339 1.00 136.53 ? 50  LEU   R CD1 1 
ATOM   30705 C  CD2 . LEU   R  4  58  ? 46.792  -209.921 -18.776 1.00 133.74 ? 50  LEU   R CD2 1 
ATOM   30706 N  N   . LEU   R  4  59  ? 49.581  -208.797 -14.215 1.00 126.11 ? 51  LEU   R N   1 
ATOM   30707 C  CA  . LEU   R  4  59  ? 49.891  -207.761 -13.189 1.00 122.46 ? 51  LEU   R CA  1 
ATOM   30708 C  C   . LEU   R  4  59  ? 51.094  -206.933 -13.663 1.00 119.77 ? 51  LEU   R C   1 
ATOM   30709 O  O   . LEU   R  4  59  ? 52.155  -207.521 -13.940 1.00 115.98 ? 51  LEU   R O   1 
ATOM   30710 C  CB  . LEU   R  4  59  ? 50.123  -208.454 -11.837 1.00 123.15 ? 51  LEU   R CB  1 
ATOM   30711 C  CG  . LEU   R  4  59  ? 51.119  -207.829 -10.857 1.00 122.43 ? 51  LEU   R CG  1 
ATOM   30712 C  CD1 . LEU   R  4  59  ? 50.809  -206.370 -10.569 1.00 121.63 ? 51  LEU   R CD1 1 
ATOM   30713 C  CD2 . LEU   R  4  59  ? 51.130  -208.619 -9.556  1.00 124.28 ? 51  LEU   R CD2 1 
ATOM   30714 N  N   . GLU   R  4  60  ? 50.909  -205.612 -13.760 1.00 120.34 ? 52  GLU   R N   1 
ATOM   30715 C  CA  . GLU   R  4  60  ? 51.931  -204.631 -14.217 1.00 120.88 ? 52  GLU   R CA  1 
ATOM   30716 C  C   . GLU   R  4  60  ? 52.995  -204.484 -13.124 1.00 117.65 ? 52  GLU   R C   1 
ATOM   30717 O  O   . GLU   R  4  60  ? 52.710  -203.826 -12.107 1.00 110.39 ? 52  GLU   R O   1 
ATOM   30718 C  CB  . GLU   R  4  60  ? 51.271  -203.290 -14.549 1.00 121.24 ? 52  GLU   R CB  1 
ATOM   30719 C  CG  . GLU   R  4  60  ? 50.172  -203.400 -15.592 1.00 123.08 ? 52  GLU   R CG  1 
ATOM   30720 C  CD  . GLU   R  4  60  ? 49.574  -202.079 -16.044 1.00 124.35 ? 52  GLU   R CD  1 
ATOM   30721 O  OE1 . GLU   R  4  60  ? 48.813  -202.088 -17.031 1.00 122.22 ? 52  GLU   R OE1 1 
ATOM   30722 O  OE2 . GLU   R  4  60  ? 49.865  -201.048 -15.407 1.00 125.22 ? 52  GLU   R OE2 1 
ATOM   30723 N  N   . SER   R  4  61  ? 54.176  -205.067 -13.346 1.00 123.87 ? 53  SER   R N   1 
ATOM   30724 C  CA  . SER   R  4  61  ? 55.217  -205.326 -12.315 1.00 127.86 ? 53  SER   R CA  1 
ATOM   30725 C  C   . SER   R  4  61  ? 55.741  -204.019 -11.705 1.00 128.15 ? 53  SER   R C   1 
ATOM   30726 O  O   . SER   R  4  61  ? 56.120  -204.047 -10.519 1.00 132.80 ? 53  SER   R O   1 
ATOM   30727 C  CB  . SER   R  4  61  ? 56.345  -206.151 -12.878 1.00 133.00 ? 53  SER   R CB  1 
ATOM   30728 O  OG  . SER   R  4  61  ? 57.065  -205.424 -13.864 1.00 143.08 ? 53  SER   R OG  1 
ATOM   30729 N  N   . ASP   R  4  62  ? 55.766  -202.923 -12.471 1.00 126.26 ? 54  ASP   R N   1 
ATOM   30730 C  CA  . ASP   R  4  62  ? 56.317  -201.614 -12.017 1.00 126.19 ? 54  ASP   R CA  1 
ATOM   30731 C  C   . ASP   R  4  62  ? 55.447  -201.024 -10.894 1.00 117.40 ? 54  ASP   R C   1 
ATOM   30732 O  O   . ASP   R  4  62  ? 55.968  -200.166 -10.157 1.00 112.22 ? 54  ASP   R O   1 
ATOM   30733 C  CB  . ASP   R  4  62  ? 56.524  -200.634 -13.179 1.00 132.60 ? 54  ASP   R CB  1 
ATOM   30734 C  CG  . ASP   R  4  62  ? 55.436  -200.651 -14.238 1.00 139.22 ? 54  ASP   R CG  1 
ATOM   30735 O  OD1 . ASP   R  4  62  ? 54.289  -201.005 -13.899 1.00 152.29 ? 54  ASP   R OD1 1 
ATOM   30736 O  OD2 . ASP   R  4  62  ? 55.748  -200.319 -15.399 1.00 145.38 ? 54  ASP   R OD2 1 
ATOM   30737 N  N   . SER   R  4  63  ? 54.194  -201.474 -10.743 1.00 114.16 ? 55  SER   R N   1 
ATOM   30738 C  CA  . SER   R  4  63  ? 53.273  -201.053 -9.651  1.00 111.78 ? 55  SER   R CA  1 
ATOM   30739 C  C   . SER   R  4  63  ? 53.626  -201.765 -8.337  1.00 109.92 ? 55  SER   R C   1 
ATOM   30740 O  O   . SER   R  4  63  ? 53.104  -201.338 -7.293  1.00 107.70 ? 55  SER   R O   1 
ATOM   30741 C  CB  . SER   R  4  63  ? 51.826  -201.274 -10.022 1.00 109.55 ? 55  SER   R CB  1 
ATOM   30742 O  OG  . SER   R  4  63  ? 51.478  -202.649 -9.945  1.00 108.85 ? 55  SER   R OG  1 
ATOM   30743 N  N   . ILE   R  4  64  ? 54.464  -202.809 -8.376  1.00 112.24 ? 56  ILE   R N   1 
ATOM   30744 C  CA  . ILE   R  4  64  ? 54.981  -203.500 -7.155  1.00 114.32 ? 56  ILE   R CA  1 
ATOM   30745 C  C   . ILE   R  4  64  ? 56.072  -202.612 -6.548  1.00 112.88 ? 56  ILE   R C   1 
ATOM   30746 O  O   . ILE   R  4  64  ? 57.123  -202.437 -7.196  1.00 113.98 ? 56  ILE   R O   1 
ATOM   30747 C  CB  . ILE   R  4  64  ? 55.497  -204.924 -7.454  1.00 116.14 ? 56  ILE   R CB  1 
ATOM   30748 C  CG1 . ILE   R  4  64  ? 54.451  -205.782 -8.173  1.00 118.23 ? 56  ILE   R CG1 1 
ATOM   30749 C  CG2 . ILE   R  4  64  ? 55.977  -205.591 -6.172  1.00 118.35 ? 56  ILE   R CG2 1 
ATOM   30750 C  CD1 . ILE   R  4  64  ? 54.993  -207.080 -8.733  1.00 119.90 ? 56  ILE   R CD1 1 
ATOM   30751 N  N   . GLU   R  4  65  ? 55.821  -202.083 -5.349  1.00 109.61 ? 57  GLU   R N   1 
ATOM   30752 C  CA  . GLU   R  4  65  ? 56.658  -201.050 -4.684  1.00 111.57 ? 57  GLU   R CA  1 
ATOM   30753 C  C   . GLU   R  4  65  ? 57.178  -201.611 -3.357  1.00 109.69 ? 57  GLU   R C   1 
ATOM   30754 O  O   . GLU   R  4  65  ? 56.526  -201.377 -2.321  1.00 108.87 ? 57  GLU   R O   1 
ATOM   30755 C  CB  . GLU   R  4  65  ? 55.824  -199.782 -4.487  1.00 115.50 ? 57  GLU   R CB  1 
ATOM   30756 C  CG  . GLU   R  4  65  ? 56.624  -198.583 -4.005  1.00 119.83 ? 57  GLU   R CG  1 
ATOM   30757 C  CD  . GLU   R  4  65  ? 55.797  -197.367 -3.619  1.00 121.12 ? 57  GLU   R CD  1 
ATOM   30758 O  OE1 . GLU   R  4  65  ? 56.378  -196.414 -3.068  1.00 123.28 ? 57  GLU   R OE1 1 
ATOM   30759 O  OE2 . GLU   R  4  65  ? 54.575  -197.373 -3.874  1.00 125.35 ? 57  GLU   R OE2 1 
ATOM   30760 N  N   . LYS   R  4  66  ? 58.306  -202.328 -3.393  1.00 108.67 ? 58  LYS   R N   1 
ATOM   30761 C  CA  . LYS   R  4  66  ? 58.913  -202.991 -2.204  1.00 110.94 ? 58  LYS   R CA  1 
ATOM   30762 C  C   . LYS   R  4  66  ? 60.226  -202.298 -1.806  1.00 109.05 ? 58  LYS   R C   1 
ATOM   30763 O  O   . LYS   R  4  66  ? 60.794  -202.693 -0.770  1.00 105.38 ? 58  LYS   R O   1 
ATOM   30764 C  CB  . LYS   R  4  66  ? 59.099  -204.486 -2.481  1.00 112.24 ? 58  LYS   R CB  1 
ATOM   30765 C  CG  . LYS   R  4  66  ? 57.805  -205.291 -2.456  1.00 113.20 ? 58  LYS   R CG  1 
ATOM   30766 C  CD  . LYS   R  4  66  ? 57.961  -206.746 -2.844  1.00 115.01 ? 58  LYS   R CD  1 
ATOM   30767 C  CE  . LYS   R  4  66  ? 56.629  -207.457 -2.964  1.00 116.78 ? 58  LYS   R CE  1 
ATOM   30768 N  NZ  . LYS   R  4  66  ? 56.787  -208.868 -3.391  1.00 118.38 ? 58  LYS   R NZ  1 
ATOM   30769 N  N   . ILE   R  4  67  ? 60.687  -201.311 -2.584  1.00 107.24 ? 59  ILE   R N   1 
ATOM   30770 C  CA  . ILE   R  4  67  ? 61.777  -200.367 -2.189  1.00 106.34 ? 59  ILE   R CA  1 
ATOM   30771 C  C   . ILE   R  4  67  ? 61.172  -198.960 -2.123  1.00 104.08 ? 59  ILE   R C   1 
ATOM   30772 O  O   . ILE   R  4  67  ? 60.461  -198.583 -3.072  1.00 106.22 ? 59  ILE   R O   1 
ATOM   30773 C  CB  . ILE   R  4  67  ? 62.980  -200.424 -3.152  1.00 111.36 ? 59  ILE   R CB  1 
ATOM   30774 C  CG1 . ILE   R  4  67  ? 63.473  -201.856 -3.382  1.00 112.61 ? 59  ILE   R CG1 1 
ATOM   30775 C  CG2 . ILE   R  4  67  ? 64.094  -199.523 -2.640  1.00 112.83 ? 59  ILE   R CG2 1 
ATOM   30776 C  CD1 . ILE   R  4  67  ? 64.579  -201.972 -4.411  1.00 115.57 ? 59  ILE   R CD1 1 
ATOM   30777 N  N   . VAL   R  4  68  ? 61.463  -198.215 -1.052  1.00 100.64 ? 60  VAL   R N   1 
ATOM   30778 C  CA  . VAL   R  4  68  ? 60.723  -196.975 -0.673  1.00 101.06 ? 60  VAL   R CA  1 
ATOM   30779 C  C   . VAL   R  4  68  ? 61.686  -195.950 -0.057  1.00 99.85  ? 60  VAL   R C   1 
ATOM   30780 O  O   . VAL   R  4  68  ? 62.583  -196.356 0.706   1.00 98.19  ? 60  VAL   R O   1 
ATOM   30781 C  CB  . VAL   R  4  68  ? 59.561  -197.326 0.277   1.00 98.71  ? 60  VAL   R CB  1 
ATOM   30782 C  CG1 . VAL   R  4  68  ? 59.262  -196.220 1.273   1.00 99.71  ? 60  VAL   R CG1 1 
ATOM   30783 C  CG2 . VAL   R  4  68  ? 58.306  -197.702 -0.496  1.00 99.44  ? 60  VAL   R CG2 1 
ATOM   30784 N  N   . GLU   R  4  69  ? 61.476  -194.666 -0.371  1.00 101.98 ? 61  GLU   R N   1 
ATOM   30785 C  CA  . GLU   R  4  69  ? 62.234  -193.514 0.189   1.00 105.00 ? 61  GLU   R CA  1 
ATOM   30786 C  C   . GLU   R  4  69  ? 61.592  -193.075 1.512   1.00 102.82 ? 61  GLU   R C   1 
ATOM   30787 O  O   . GLU   R  4  69  ? 60.358  -192.887 1.541   1.00 96.48  ? 61  GLU   R O   1 
ATOM   30788 C  CB  . GLU   R  4  69  ? 62.254  -192.343 -0.798  1.00 108.83 ? 61  GLU   R CB  1 
ATOM   30789 C  CG  . GLU   R  4  69  ? 63.126  -191.180 -0.345  1.00 111.43 ? 61  GLU   R CG  1 
ATOM   30790 C  CD  . GLU   R  4  69  ? 63.128  -189.964 -1.259  1.00 112.97 ? 61  GLU   R CD  1 
ATOM   30791 O  OE1 . GLU   R  4  69  ? 63.476  -188.866 -0.781  1.00 115.98 ? 61  GLU   R OE1 1 
ATOM   30792 O  OE2 . GLU   R  4  69  ? 62.792  -190.114 -2.448  1.00 117.13 ? 61  GLU   R OE2 1 
ATOM   30793 N  N   . ILE   R  4  70  ? 62.411  -192.906 2.555   1.00 103.05 ? 62  ILE   R N   1 
ATOM   30794 C  CA  . ILE   R  4  70  ? 62.000  -192.375 3.889   1.00 102.78 ? 62  ILE   R CA  1 
ATOM   30795 C  C   . ILE   R  4  70  ? 62.372  -190.889 3.953   1.00 105.85 ? 62  ILE   R C   1 
ATOM   30796 O  O   . ILE   R  4  70  ? 61.511  -190.082 4.360   1.00 102.67 ? 62  ILE   R O   1 
ATOM   30797 C  CB  . ILE   R  4  70  ? 62.647  -193.198 5.020   1.00 101.99 ? 62  ILE   R CB  1 
ATOM   30798 C  CG1 . ILE   R  4  70  ? 62.150  -194.646 4.982   1.00 102.34 ? 62  ILE   R CG1 1 
ATOM   30799 C  CG2 . ILE   R  4  70  ? 62.415  -192.541 6.374   1.00 100.52 ? 62  ILE   R CG2 1 
ATOM   30800 C  CD1 . ILE   R  4  70  ? 62.660  -195.519 6.105   1.00 104.75 ? 62  ILE   R CD1 1 
ATOM   30801 N  N   . ASP   R  4  71  ? 63.614  -190.559 3.582   1.00 108.65 ? 63  ASP   R N   1 
ATOM   30802 C  CA  . ASP   R  4  71  ? 64.102  -189.170 3.357   1.00 111.01 ? 63  ASP   R CA  1 
ATOM   30803 C  C   . ASP   R  4  71  ? 65.161  -189.220 2.246   1.00 106.37 ? 63  ASP   R C   1 
ATOM   30804 O  O   . ASP   R  4  71  ? 65.371  -190.314 1.686   1.00 101.77 ? 63  ASP   R O   1 
ATOM   30805 C  CB  . ASP   R  4  71  ? 64.618  -188.544 4.661   1.00 115.91 ? 63  ASP   R CB  1 
ATOM   30806 C  CG  . ASP   R  4  71  ? 64.448  -187.033 4.755   1.00 120.16 ? 63  ASP   R CG  1 
ATOM   30807 O  OD1 . ASP   R  4  71  ? 64.304  -186.384 3.698   1.00 120.59 ? 63  ASP   R OD1 1 
ATOM   30808 O  OD2 . ASP   R  4  71  ? 64.462  -186.512 5.891   1.00 126.37 ? 63  ASP   R OD2 1 
ATOM   30809 N  N   . ARG   R  4  72  ? 65.796  -188.086 1.931   1.00 107.12 ? 64  ARG   R N   1 
ATOM   30810 C  CA  . ARG   R  4  72  ? 66.807  -187.979 0.845   1.00 107.38 ? 64  ARG   R CA  1 
ATOM   30811 C  C   . ARG   R  4  72  ? 68.041  -188.824 1.193   1.00 103.82 ? 64  ARG   R C   1 
ATOM   30812 O  O   . ARG   R  4  72  ? 68.720  -189.281 0.255   1.00 100.22 ? 64  ARG   R O   1 
ATOM   30813 C  CB  . ARG   R  4  72  ? 67.211  -186.521 0.614   1.00 109.47 ? 64  ARG   R CB  1 
ATOM   30814 C  CG  . ARG   R  4  72  ? 67.550  -186.201 -0.834  1.00 113.45 ? 64  ARG   R CG  1 
ATOM   30815 C  CD  . ARG   R  4  72  ? 68.307  -184.894 -0.961  1.00 119.01 ? 64  ARG   R CD  1 
ATOM   30816 N  NE  . ARG   R  4  72  ? 69.752  -185.101 -0.968  1.00 123.22 ? 64  ARG   R NE  1 
ATOM   30817 C  CZ  . ARG   R  4  72  ? 70.527  -185.142 -2.054  1.00 123.43 ? 64  ARG   R CZ  1 
ATOM   30818 N  NH1 . ARG   R  4  72  ? 71.829  -185.338 -1.920  1.00 123.52 ? 64  ARG   R NH1 1 
ATOM   30819 N  NH2 . ARG   R  4  72  ? 70.016  -184.985 -3.264  1.00 125.54 ? 64  ARG   R NH2 1 
ATOM   30820 N  N   . HIS   R  4  73  ? 68.319  -189.017 2.487   1.00 102.96 ? 65  HIS   R N   1 
ATOM   30821 C  CA  . HIS   R  4  73  ? 69.528  -189.717 3.003   1.00 107.18 ? 65  HIS   R CA  1 
ATOM   30822 C  C   . HIS   R  4  73  ? 69.188  -191.120 3.537   1.00 105.31 ? 65  HIS   R C   1 
ATOM   30823 O  O   . HIS   R  4  73  ? 70.139  -191.813 3.945   1.00 106.53 ? 65  HIS   R O   1 
ATOM   30824 C  CB  . HIS   R  4  73  ? 70.232  -188.854 4.064   1.00 107.93 ? 65  HIS   R CB  1 
ATOM   30825 C  CG  . HIS   R  4  73  ? 69.470  -188.686 5.338   1.00 109.68 ? 65  HIS   R CG  1 
ATOM   30826 N  ND1 . HIS   R  4  73  ? 68.305  -187.945 5.414   1.00 110.42 ? 65  HIS   R ND1 1 
ATOM   30827 C  CD2 . HIS   R  4  73  ? 69.710  -189.141 6.587   1.00 109.23 ? 65  HIS   R CD2 1 
ATOM   30828 C  CE1 . HIS   R  4  73  ? 67.853  -187.967 6.652   1.00 110.46 ? 65  HIS   R CE1 1 
ATOM   30829 N  NE2 . HIS   R  4  73  ? 68.698  -188.693 7.390   1.00 108.81 ? 65  HIS   R NE2 1 
ATOM   30830 N  N   . ILE   R  4  74  ? 67.911  -191.533 3.540   1.00 107.62 ? 66  ILE   R N   1 
ATOM   30831 C  CA  . ILE   R  4  74  ? 67.461  -192.863 4.063   1.00 107.52 ? 66  ILE   R CA  1 
ATOM   30832 C  C   . ILE   R  4  74  ? 66.469  -193.511 3.089   1.00 109.35 ? 66  ILE   R C   1 
ATOM   30833 O  O   . ILE   R  4  74  ? 65.452  -192.870 2.761   1.00 112.46 ? 66  ILE   R O   1 
ATOM   30834 C  CB  . ILE   R  4  74  ? 66.853  -192.738 5.476   1.00 105.09 ? 66  ILE   R CB  1 
ATOM   30835 C  CG1 . ILE   R  4  74  ? 67.905  -192.315 6.503   1.00 106.16 ? 66  ILE   R CG1 1 
ATOM   30836 C  CG2 . ILE   R  4  74  ? 66.170  -194.035 5.888   1.00 103.55 ? 66  ILE   R CG2 1 
ATOM   30837 C  CD1 . ILE   R  4  74  ? 67.346  -191.987 7.867   1.00 107.35 ? 66  ILE   R CD1 1 
ATOM   30838 N  N   . GLY   R  4  75  ? 66.744  -194.762 2.702   1.00 110.97 ? 67  GLY   R N   1 
ATOM   30839 C  CA  . GLY   R  4  75  ? 65.856  -195.631 1.903   1.00 114.13 ? 67  GLY   R CA  1 
ATOM   30840 C  C   . GLY   R  4  75  ? 65.543  -196.921 2.643   1.00 114.00 ? 67  GLY   R C   1 
ATOM   30841 O  O   . GLY   R  4  75  ? 66.222  -197.204 3.651   1.00 115.17 ? 67  GLY   R O   1 
ATOM   30842 N  N   . CYS   R  4  76  ? 64.561  -197.690 2.164   1.00 114.55 ? 68  CYS   R N   1 
ATOM   30843 C  CA  . CYS   R  4  76  ? 63.997  -198.863 2.883   1.00 114.23 ? 68  CYS   R CA  1 
ATOM   30844 C  C   . CYS   R  4  76  ? 63.490  -199.920 1.892   1.00 114.02 ? 68  CYS   R C   1 
ATOM   30845 O  O   . CYS   R  4  76  ? 62.832  -199.541 0.904   1.00 116.68 ? 68  CYS   R O   1 
ATOM   30846 C  CB  . CYS   R  4  76  ? 62.883  -198.400 3.815   1.00 114.25 ? 68  CYS   R CB  1 
ATOM   30847 S  SG  . CYS   R  4  76  ? 62.074  -199.729 4.741   1.00 119.43 ? 68  CYS   R SG  1 
ATOM   30848 N  N   . ALA   R  4  77  ? 63.807  -201.194 2.157   1.00 111.03 ? 69  ALA   R N   1 
ATOM   30849 C  CA  . ALA   R  4  77  ? 63.295  -202.393 1.450   1.00 109.83 ? 69  ALA   R CA  1 
ATOM   30850 C  C   . ALA   R  4  77  ? 62.537  -203.273 2.451   1.00 107.33 ? 69  ALA   R C   1 
ATOM   30851 O  O   . ALA   R  4  77  ? 62.872  -203.223 3.649   1.00 103.99 ? 69  ALA   R O   1 
ATOM   30852 C  CB  . ALA   R  4  77  ? 64.434  -203.144 0.806   1.00 110.46 ? 69  ALA   R CB  1 
ATOM   30853 N  N   . MET   R  4  78  ? 61.569  -204.060 1.977   1.00 107.53 ? 70  MET   R N   1 
ATOM   30854 C  CA  . MET   R  4  78  ? 60.609  -204.802 2.839   1.00 111.08 ? 70  MET   R CA  1 
ATOM   30855 C  C   . MET   R  4  78  ? 60.460  -206.249 2.351   1.00 108.68 ? 70  MET   R C   1 
ATOM   30856 O  O   . MET   R  4  78  ? 60.757  -206.518 1.170   1.00 110.51 ? 70  MET   R O   1 
ATOM   30857 C  CB  . MET   R  4  78  ? 59.242  -204.108 2.841   1.00 114.33 ? 70  MET   R CB  1 
ATOM   30858 C  CG  . MET   R  4  78  ? 58.575  -204.045 1.477   1.00 117.20 ? 70  MET   R CG  1 
ATOM   30859 S  SD  . MET   R  4  78  ? 57.165  -202.909 1.449   1.00 119.48 ? 70  MET   R SD  1 
ATOM   30860 C  CE  . MET   R  4  78  ? 58.013  -201.335 1.351   1.00 123.26 ? 70  MET   R CE  1 
ATOM   30861 N  N   . SER   R  4  79  ? 60.021  -207.141 3.243   1.00 107.03 ? 71  SER   R N   1 
ATOM   30862 C  CA  . SER   R  4  79  ? 59.752  -208.574 2.961   1.00 107.27 ? 71  SER   R CA  1 
ATOM   30863 C  C   . SER   R  4  79  ? 58.737  -209.121 3.969   1.00 104.20 ? 71  SER   R C   1 
ATOM   30864 O  O   . SER   R  4  79  ? 58.937  -208.908 5.179   1.00 102.22 ? 71  SER   R O   1 
ATOM   30865 C  CB  . SER   R  4  79  ? 61.022  -209.375 2.982   1.00 110.16 ? 71  SER   R CB  1 
ATOM   30866 O  OG  . SER   R  4  79  ? 60.764  -210.734 2.665   1.00 113.48 ? 71  SER   R OG  1 
ATOM   30867 N  N   . GLY   R  4  80  ? 57.703  -209.809 3.473   1.00 105.84 ? 72  GLY   R N   1 
ATOM   30868 C  CA  . GLY   R  4  80  ? 56.616  -210.397 4.278   1.00 106.21 ? 72  GLY   R CA  1 
ATOM   30869 C  C   . GLY   R  4  80  ? 55.268  -209.828 3.875   1.00 101.74 ? 72  GLY   R C   1 
ATOM   30870 O  O   . GLY   R  4  80  ? 55.083  -209.552 2.671   1.00 99.29  ? 72  GLY   R O   1 
ATOM   30871 N  N   . LEU   R  4  81  ? 54.357  -209.660 4.839   1.00 102.45 ? 73  LEU   R N   1 
ATOM   30872 C  CA  . LEU   R  4  81  ? 53.028  -209.026 4.628   1.00 104.16 ? 73  LEU   R CA  1 
ATOM   30873 C  C   . LEU   R  4  81  ? 53.247  -207.533 4.355   1.00 107.15 ? 73  LEU   R C   1 
ATOM   30874 O  O   . LEU   R  4  81  ? 53.162  -206.737 5.310   1.00 108.75 ? 73  LEU   R O   1 
ATOM   30875 C  CB  . LEU   R  4  81  ? 52.147  -209.250 5.863   1.00 104.53 ? 73  LEU   R CB  1 
ATOM   30876 C  CG  . LEU   R  4  81  ? 51.770  -210.700 6.167   1.00 103.26 ? 73  LEU   R CG  1 
ATOM   30877 C  CD1 . LEU   R  4  81  ? 51.095  -210.807 7.525   1.00 103.81 ? 73  LEU   R CD1 1 
ATOM   30878 C  CD2 . LEU   R  4  81  ? 50.868  -211.275 5.088   1.00 103.19 ? 73  LEU   R CD2 1 
ATOM   30879 N  N   . THR   R  4  82  ? 53.525  -207.175 3.096   1.00 108.05 ? 74  THR   R N   1 
ATOM   30880 C  CA  . THR   R  4  82  ? 54.018  -205.833 2.674   1.00 108.37 ? 74  THR   R CA  1 
ATOM   30881 C  C   . THR   R  4  82  ? 52.973  -204.741 2.944   1.00 110.95 ? 74  THR   R C   1 
ATOM   30882 O  O   . THR   R  4  82  ? 53.381  -203.564 3.057   1.00 112.35 ? 74  THR   R O   1 
ATOM   30883 C  CB  . THR   R  4  82  ? 54.419  -205.818 1.195   1.00 107.47 ? 74  THR   R CB  1 
ATOM   30884 O  OG1 . THR   R  4  82  ? 53.312  -206.294 0.429   1.00 108.25 ? 74  THR   R OG1 1 
ATOM   30885 C  CG2 . THR   R  4  82  ? 55.647  -206.655 0.914   1.00 107.85 ? 74  THR   R CG2 1 
ATOM   30886 N  N   . ALA   R  4  83  ? 51.687  -205.097 3.028   1.00 110.48 ? 75  ALA   R N   1 
ATOM   30887 C  CA  . ALA   R  4  83  ? 50.587  -204.162 3.365   1.00 108.45 ? 75  ALA   R CA  1 
ATOM   30888 C  C   . ALA   R  4  83  ? 50.817  -203.580 4.768   1.00 107.17 ? 75  ALA   R C   1 
ATOM   30889 O  O   . ALA   R  4  83  ? 50.464  -202.404 4.979   1.00 107.36 ? 75  ALA   R O   1 
ATOM   30890 C  CB  . ALA   R  4  83  ? 49.253  -204.861 3.258   1.00 106.93 ? 75  ALA   R CB  1 
ATOM   30891 N  N   . ASP   R  4  84  ? 51.408  -204.365 5.677   1.00 106.47 ? 76  ASP   R N   1 
ATOM   30892 C  CA  . ASP   R  4  84  ? 51.702  -203.969 7.083   1.00 105.71 ? 76  ASP   R CA  1 
ATOM   30893 C  C   . ASP   R  4  84  ? 52.737  -202.833 7.124   1.00 105.44 ? 76  ASP   R C   1 
ATOM   30894 O  O   . ASP   R  4  84  ? 52.736  -202.081 8.121   1.00 100.66 ? 76  ASP   R O   1 
ATOM   30895 C  CB  . ASP   R  4  84  ? 52.183  -205.165 7.914   1.00 107.05 ? 76  ASP   R CB  1 
ATOM   30896 C  CG  . ASP   R  4  84  ? 51.092  -206.157 8.286   1.00 106.86 ? 76  ASP   R CG  1 
ATOM   30897 O  OD1 . ASP   R  4  84  ? 50.004  -206.093 7.678   1.00 106.78 ? 76  ASP   R OD1 1 
ATOM   30898 O  OD2 . ASP   R  4  84  ? 51.338  -206.990 9.184   1.00 108.45 ? 76  ASP   R OD2 1 
ATOM   30899 N  N   . ALA   R  4  85  ? 53.581  -202.705 6.093   1.00 105.02 ? 77  ALA   R N   1 
ATOM   30900 C  CA  . ALA   R  4  85  ? 54.736  -201.775 6.059   1.00 106.68 ? 77  ALA   R CA  1 
ATOM   30901 C  C   . ALA   R  4  85  ? 54.282  -200.326 5.832   1.00 111.19 ? 77  ALA   R C   1 
ATOM   30902 O  O   . ALA   R  4  85  ? 55.084  -199.426 6.136   1.00 114.42 ? 77  ALA   R O   1 
ATOM   30903 C  CB  . ALA   R  4  85  ? 55.719  -202.201 4.996   1.00 105.70 ? 77  ALA   R CB  1 
ATOM   30904 N  N   . ARG   R  4  86  ? 53.064  -200.096 5.326   1.00 113.50 ? 78  ARG   R N   1 
ATOM   30905 C  CA  . ARG   R  4  86  ? 52.596  -198.741 4.914   1.00 115.72 ? 78  ARG   R CA  1 
ATOM   30906 C  C   . ARG   R  4  86  ? 52.658  -197.784 6.111   1.00 109.81 ? 78  ARG   R C   1 
ATOM   30907 O  O   . ARG   R  4  86  ? 53.246  -196.694 5.956   1.00 109.76 ? 78  ARG   R O   1 
ATOM   30908 C  CB  . ARG   R  4  86  ? 51.188  -198.783 4.304   1.00 120.43 ? 78  ARG   R CB  1 
ATOM   30909 C  CG  . ARG   R  4  86  ? 51.082  -199.596 3.019   1.00 127.92 ? 78  ARG   R CG  1 
ATOM   30910 C  CD  . ARG   R  4  86  ? 51.997  -199.108 1.907   1.00 136.10 ? 78  ARG   R CD  1 
ATOM   30911 N  NE  . ARG   R  4  86  ? 52.442  -200.196 1.042   1.00 146.26 ? 78  ARG   R NE  1 
ATOM   30912 C  CZ  . ARG   R  4  86  ? 53.608  -200.243 0.393   1.00 156.02 ? 78  ARG   R CZ  1 
ATOM   30913 N  NH1 . ARG   R  4  86  ? 54.490  -199.261 0.501   1.00 158.94 ? 78  ARG   R NH1 1 
ATOM   30914 N  NH2 . ARG   R  4  86  ? 53.894  -201.290 -0.362  1.00 160.04 ? 78  ARG   R NH2 1 
ATOM   30915 N  N   . SER   R  4  87  ? 52.097  -198.179 7.258   1.00 104.43 ? 79  SER   R N   1 
ATOM   30916 C  CA  . SER   R  4  87  ? 52.056  -197.360 8.499   1.00 100.97 ? 79  SER   R CA  1 
ATOM   30917 C  C   . SER   R  4  87  ? 53.458  -197.248 9.112   1.00 99.76  ? 79  SER   R C   1 
ATOM   30918 O  O   . SER   R  4  87  ? 53.713  -196.247 9.802   1.00 101.68 ? 79  SER   R O   1 
ATOM   30919 C  CB  . SER   R  4  87  ? 51.068  -197.911 9.489   1.00 99.60  ? 79  SER   R CB  1 
ATOM   30920 O  OG  . SER   R  4  87  ? 51.406  -199.241 9.848   1.00 101.25 ? 79  SER   R OG  1 
ATOM   30921 N  N   . MET   R  4  88  ? 54.332  -198.232 8.879   1.00 98.80  ? 80  MET   R N   1 
ATOM   30922 C  CA  . MET   R  4  88  ? 55.748  -198.200 9.339   1.00 103.47 ? 80  MET   R CA  1 
ATOM   30923 C  C   . MET   R  4  88  ? 56.511  -197.142 8.533   1.00 101.74 ? 80  MET   R C   1 
ATOM   30924 O  O   . MET   R  4  88  ? 57.310  -196.407 9.143   1.00 104.71 ? 80  MET   R O   1 
ATOM   30925 C  CB  . MET   R  4  88  ? 56.442  -199.557 9.173   1.00 106.75 ? 80  MET   R CB  1 
ATOM   30926 C  CG  . MET   R  4  88  ? 55.802  -200.684 9.966   1.00 110.38 ? 80  MET   R CG  1 
ATOM   30927 S  SD  . MET   R  4  88  ? 56.676  -202.260 9.762   1.00 114.68 ? 80  MET   R SD  1 
ATOM   30928 C  CE  . MET   R  4  88  ? 58.026  -202.040 10.921  1.00 118.84 ? 80  MET   R CE  1 
ATOM   30929 N  N   . ILE   R  4  89  ? 56.270  -197.069 7.219   1.00 98.78  ? 81  ILE   R N   1 
ATOM   30930 C  CA  . ILE   R  4  89  ? 56.899  -196.071 6.301   1.00 102.05 ? 81  ILE   R CA  1 
ATOM   30931 C  C   . ILE   R  4  89  ? 56.362  -194.676 6.647   1.00 105.44 ? 81  ILE   R C   1 
ATOM   30932 O  O   . ILE   R  4  89  ? 57.178  -193.733 6.739   1.00 106.49 ? 81  ILE   R O   1 
ATOM   30933 C  CB  . ILE   R  4  89  ? 56.642  -196.425 4.821   1.00 100.37 ? 81  ILE   R CB  1 
ATOM   30934 C  CG1 . ILE   R  4  89  ? 57.237  -197.782 4.432   1.00 99.96  ? 81  ILE   R CG1 1 
ATOM   30935 C  CG2 . ILE   R  4  89  ? 57.141  -195.317 3.905   1.00 101.29 ? 81  ILE   R CG2 1 
ATOM   30936 C  CD1 . ILE   R  4  89  ? 58.722  -197.919 4.688   1.00 101.08 ? 81  ILE   R CD1 1 
ATOM   30937 N  N   . GLU   R  4  90  ? 55.040  -194.553 6.810   1.00 106.95 ? 82  GLU   R N   1 
ATOM   30938 C  CA  . GLU   R  4  90  ? 54.347  -193.281 7.150   1.00 108.29 ? 82  GLU   R CA  1 
ATOM   30939 C  C   . GLU   R  4  90  ? 54.969  -192.702 8.428   1.00 106.53 ? 82  GLU   R C   1 
ATOM   30940 O  O   . GLU   R  4  90  ? 55.290  -191.496 8.432   1.00 106.01 ? 82  GLU   R O   1 
ATOM   30941 C  CB  . GLU   R  4  90  ? 52.838  -193.522 7.278   1.00 109.70 ? 82  GLU   R CB  1 
ATOM   30942 C  CG  . GLU   R  4  90  ? 52.057  -192.334 7.816   1.00 111.75 ? 82  GLU   R CG  1 
ATOM   30943 C  CD  . GLU   R  4  90  ? 52.217  -191.036 7.040   1.00 117.04 ? 82  GLU   R CD  1 
ATOM   30944 O  OE1 . GLU   R  4  90  ? 52.621  -191.095 5.858   1.00 112.84 ? 82  GLU   R OE1 1 
ATOM   30945 O  OE2 . GLU   R  4  90  ? 51.928  -189.967 7.618   1.00 120.35 ? 82  GLU   R OE2 1 
ATOM   30946 N  N   . HIS   R  4  91  ? 55.156  -193.536 9.457   1.00 99.91  ? 83  HIS   R N   1 
ATOM   30947 C  CA  . HIS   R  4  91  ? 55.790  -193.157 10.748  1.00 97.60  ? 83  HIS   R CA  1 
ATOM   30948 C  C   . HIS   R  4  91  ? 57.235  -192.709 10.507  1.00 97.54  ? 83  HIS   R C   1 
ATOM   30949 O  O   . HIS   R  4  91  ? 57.605  -191.634 11.011  1.00 102.68 ? 83  HIS   R O   1 
ATOM   30950 C  CB  . HIS   R  4  91  ? 55.742  -194.311 11.753  1.00 97.03  ? 83  HIS   R CB  1 
ATOM   30951 C  CG  . HIS   R  4  91  ? 56.424  -193.990 13.041  1.00 97.70  ? 83  HIS   R CG  1 
ATOM   30952 N  ND1 . HIS   R  4  91  ? 55.737  -193.514 14.141  1.00 98.47  ? 83  HIS   R ND1 1 
ATOM   30953 C  CD2 . HIS   R  4  91  ? 57.724  -194.053 13.404  1.00 99.17  ? 83  HIS   R CD2 1 
ATOM   30954 C  CE1 . HIS   R  4  91  ? 56.584  -193.309 15.130  1.00 99.41  ? 83  HIS   R CE1 1 
ATOM   30955 N  NE2 . HIS   R  4  91  ? 57.811  -193.632 14.703  1.00 100.17 ? 83  HIS   R NE2 1 
ATOM   30956 N  N   . ALA   R  4  92  ? 58.015  -193.517 9.783   1.00 94.76  ? 84  ALA   R N   1 
ATOM   30957 C  CA  . ALA   R  4  92  ? 59.449  -193.283 9.488   1.00 94.92  ? 84  ALA   R CA  1 
ATOM   30958 C  C   . ALA   R  4  92  ? 59.633  -191.922 8.805   1.00 94.05  ? 84  ALA   R C   1 
ATOM   30959 O  O   . ALA   R  4  92  ? 60.551  -191.182 9.203   1.00 95.70  ? 84  ALA   R O   1 
ATOM   30960 C  CB  . ALA   R  4  92  ? 59.994  -194.398 8.631   1.00 95.03  ? 84  ALA   R CB  1 
ATOM   30961 N  N   . ARG   R  4  93  ? 58.792  -191.611 7.815   1.00 93.46  ? 85  ARG   R N   1 
ATOM   30962 C  CA  . ARG   R  4  93  ? 58.850  -190.343 7.038   1.00 95.55  ? 85  ARG   R CA  1 
ATOM   30963 C  C   . ARG   R  4  93  ? 58.547  -189.151 7.956   1.00 94.98  ? 85  ARG   R C   1 
ATOM   30964 O  O   . ARG   R  4  93  ? 59.276  -188.138 7.871   1.00 93.72  ? 85  ARG   R O   1 
ATOM   30965 C  CB  . ARG   R  4  93  ? 57.870  -190.389 5.863   1.00 97.13  ? 85  ARG   R CB  1 
ATOM   30966 C  CG  . ARG   R  4  93  ? 58.346  -191.264 4.715   1.00 97.05  ? 85  ARG   R CG  1 
ATOM   30967 C  CD  . ARG   R  4  93  ? 57.247  -191.555 3.717   1.00 98.74  ? 85  ARG   R CD  1 
ATOM   30968 N  NE  . ARG   R  4  93  ? 57.777  -192.187 2.517   1.00 97.47  ? 85  ARG   R NE  1 
ATOM   30969 C  CZ  . ARG   R  4  93  ? 57.040  -192.631 1.504   1.00 99.39  ? 85  ARG   R CZ  1 
ATOM   30970 N  NH1 . ARG   R  4  93  ? 55.721  -192.525 1.538   1.00 98.72  ? 85  ARG   R NH1 1 
ATOM   30971 N  NH2 . ARG   R  4  93  ? 57.627  -193.185 0.457   1.00 100.92 ? 85  ARG   R NH2 1 
ATOM   30972 N  N   . THR   R  4  94  ? 57.509  -189.265 8.790   1.00 92.92  ? 86  THR   R N   1 
ATOM   30973 C  CA  . THR   R  4  94  ? 57.083  -188.215 9.751   1.00 90.95  ? 86  THR   R CA  1 
ATOM   30974 C  C   . THR   R  4  94  ? 58.187  -188.009 10.793  1.00 92.42  ? 86  THR   R C   1 
ATOM   30975 O  O   . THR   R  4  94  ? 58.500  -186.843 11.086  1.00 92.98  ? 86  THR   R O   1 
ATOM   30976 C  CB  . THR   R  4  94  ? 55.751  -188.560 10.425  1.00 88.99  ? 86  THR   R CB  1 
ATOM   30977 O  OG1 . THR   R  4  94  ? 54.804  -188.891 9.411   1.00 88.54  ? 86  THR   R OG1 1 
ATOM   30978 C  CG2 . THR   R  4  94  ? 55.220  -187.419 11.261  1.00 89.44  ? 86  THR   R CG2 1 
ATOM   30979 N  N   . ALA   R  4  95  ? 58.750  -189.098 11.323  1.00 91.21  ? 87  ALA   R N   1 
ATOM   30980 C  CA  . ALA   R  4  95  ? 59.866  -189.080 12.297  1.00 91.85  ? 87  ALA   R CA  1 
ATOM   30981 C  C   . ALA   R  4  95  ? 61.060  -188.323 11.704  1.00 93.22  ? 87  ALA   R C   1 
ATOM   30982 O  O   . ALA   R  4  95  ? 61.661  -187.514 12.436  1.00 94.52  ? 87  ALA   R O   1 
ATOM   30983 C  CB  . ALA   R  4  95  ? 60.247  -190.488 12.682  1.00 92.13  ? 87  ALA   R CB  1 
ATOM   30984 N  N   . ALA   R  4  96  ? 61.375  -188.570 10.426  1.00 94.28  ? 88  ALA   R N   1 
ATOM   30985 C  CA  . ALA   R  4  96  ? 62.528  -187.983 9.699   1.00 98.92  ? 88  ALA   R CA  1 
ATOM   30986 C  C   . ALA   R  4  96  ? 62.308  -186.483 9.464   1.00 99.73  ? 88  ALA   R C   1 
ATOM   30987 O  O   . ALA   R  4  96  ? 63.227  -185.689 9.757   1.00 102.51 ? 88  ALA   R O   1 
ATOM   30988 C  CB  . ALA   R  4  96  ? 62.743  -188.705 8.393   1.00 100.18 ? 88  ALA   R CB  1 
ATOM   30989 N  N   . VAL   R  4  97  ? 61.139  -186.116 8.933   1.00 98.96  ? 89  VAL   R N   1 
ATOM   30990 C  CA  . VAL   R  4  97  ? 60.762  -184.708 8.613   1.00 96.77  ? 89  VAL   R CA  1 
ATOM   30991 C  C   . VAL   R  4  97  ? 60.592  -183.922 9.922   1.00 99.20  ? 89  VAL   R C   1 
ATOM   30992 O  O   . VAL   R  4  97  ? 61.043  -182.754 9.963   1.00 102.98 ? 89  VAL   R O   1 
ATOM   30993 C  CB  . VAL   R  4  97  ? 59.496  -184.651 7.735   1.00 96.06  ? 89  VAL   R CB  1 
ATOM   30994 C  CG1 . VAL   R  4  97  ? 58.925  -183.245 7.645   1.00 96.12  ? 89  VAL   R CG1 1 
ATOM   30995 C  CG2 . VAL   R  4  97  ? 59.759  -185.204 6.344   1.00 96.64  ? 89  VAL   R CG2 1 
ATOM   30996 N  N   . THR   R  4  98  ? 59.962  -184.519 10.942  1.00 91.75  ? 90  THR   R N   1 
ATOM   30997 C  CA  . THR   R  4  98  ? 59.688  -183.860 12.251  1.00 89.23  ? 90  THR   R CA  1 
ATOM   30998 C  C   . THR   R  4  98  ? 61.007  -183.478 12.923  1.00 90.05  ? 90  THR   R C   1 
ATOM   30999 O  O   . THR   R  4  98  ? 61.092  -182.359 13.458  1.00 90.89  ? 90  THR   R O   1 
ATOM   31000 C  CB  . THR   R  4  98  ? 58.870  -184.738 13.205  1.00 86.00  ? 90  THR   R CB  1 
ATOM   31001 O  OG1 . THR   R  4  98  ? 57.603  -184.999 12.604  1.00 84.11  ? 90  THR   R OG1 1 
ATOM   31002 C  CG2 . THR   R  4  98  ? 58.646  -184.083 14.550  1.00 85.13  ? 90  THR   R CG2 1 
ATOM   31003 N  N   . HIS   R  4  99  ? 61.986  -184.382 12.915  1.00 91.18  ? 91  HIS   R N   1 
ATOM   31004 C  CA  . HIS   R  4  99  ? 63.331  -184.141 13.498  1.00 92.64  ? 91  HIS   R CA  1 
ATOM   31005 C  C   . HIS   R  4  99  ? 63.998  -182.962 12.778  1.00 97.29  ? 91  HIS   R C   1 
ATOM   31006 O  O   . HIS   R  4  99  ? 64.663  -182.159 13.460  1.00 101.82 ? 91  HIS   R O   1 
ATOM   31007 C  CB  . HIS   R  4  99  ? 64.181  -185.413 13.444  1.00 93.66  ? 91  HIS   R CB  1 
ATOM   31008 C  CG  . HIS   R  4  99  ? 65.561  -185.218 13.970  1.00 92.08  ? 91  HIS   R CG  1 
ATOM   31009 N  ND1 . HIS   R  4  99  ? 65.910  -185.554 15.261  1.00 93.26  ? 91  HIS   R ND1 1 
ATOM   31010 C  CD2 . HIS   R  4  99  ? 66.670  -184.704 13.395  1.00 94.87  ? 91  HIS   R CD2 1 
ATOM   31011 C  CE1 . HIS   R  4  99  ? 67.182  -185.267 15.457  1.00 97.09  ? 91  HIS   R CE1 1 
ATOM   31012 N  NE2 . HIS   R  4  99  ? 67.670  -184.743 14.326  1.00 97.58  ? 91  HIS   R NE2 1 
ATOM   31013 N  N   . ASN   R  4  100 ? 63.822  -182.856 11.457  1.00 96.80  ? 92  ASN   R N   1 
ATOM   31014 C  CA  . ASN   R  4  100 ? 64.386  -181.752 10.634  1.00 98.55  ? 92  ASN   R CA  1 
ATOM   31015 C  C   . ASN   R  4  100 ? 63.722  -180.427 11.029  1.00 97.42  ? 92  ASN   R C   1 
ATOM   31016 O  O   . ASN   R  4  100 ? 64.434  -179.408 11.076  1.00 99.06  ? 92  ASN   R O   1 
ATOM   31017 C  CB  . ASN   R  4  100 ? 64.244  -182.023 9.135   1.00 99.80  ? 92  ASN   R CB  1 
ATOM   31018 C  CG  . ASN   R  4  100 ? 64.746  -180.875 8.287   1.00 101.59 ? 92  ASN   R CG  1 
ATOM   31019 O  OD1 . ASN   R  4  100 ? 63.968  -180.234 7.586   1.00 105.17 ? 92  ASN   R OD1 1 
ATOM   31020 N  ND2 . ASN   R  4  100 ? 66.038  -180.598 8.361   1.00 103.26 ? 92  ASN   R ND2 1 
ATOM   31021 N  N   . LEU   R  4  101 ? 62.416  -180.444 11.312  1.00 95.74  ? 93  LEU   R N   1 
ATOM   31022 C  CA  . LEU   R  4  101 ? 61.647  -179.244 11.738  1.00 94.91  ? 93  LEU   R CA  1 
ATOM   31023 C  C   . LEU   R  4  101 ? 62.119  -178.795 13.129  1.00 98.10  ? 93  LEU   R C   1 
ATOM   31024 O  O   . LEU   R  4  101 ? 62.275  -177.578 13.322  1.00 100.64 ? 93  LEU   R O   1 
ATOM   31025 C  CB  . LEU   R  4  101 ? 60.147  -179.563 11.725  1.00 92.53  ? 93  LEU   R CB  1 
ATOM   31026 C  CG  . LEU   R  4  101 ? 59.218  -178.417 12.126  1.00 92.39  ? 93  LEU   R CG  1 
ATOM   31027 C  CD1 . LEU   R  4  101 ? 59.282  -177.277 11.118  1.00 94.27  ? 93  LEU   R CD1 1 
ATOM   31028 C  CD2 . LEU   R  4  101 ? 57.787  -178.907 12.276  1.00 90.26  ? 93  LEU   R CD2 1 
ATOM   31029 N  N   . TYR   R  4  102 ? 62.350  -179.731 14.057  1.00 95.49  ? 94  TYR   R N   1 
ATOM   31030 C  CA  . TYR   R  4  102 ? 62.696  -179.433 15.474  1.00 95.48  ? 94  TYR   R CA  1 
ATOM   31031 C  C   . TYR   R  4  102 ? 64.180  -179.081 15.625  1.00 92.21  ? 94  TYR   R C   1 
ATOM   31032 O  O   . TYR   R  4  102 ? 64.491  -178.396 16.612  1.00 94.03  ? 94  TYR   R O   1 
ATOM   31033 C  CB  . TYR   R  4  102 ? 62.360  -180.600 16.409  1.00 97.64  ? 94  TYR   R CB  1 
ATOM   31034 C  CG  . TYR   R  4  102 ? 60.894  -180.828 16.690  1.00 105.08 ? 94  TYR   R CG  1 
ATOM   31035 C  CD1 . TYR   R  4  102 ? 59.947  -179.828 16.513  1.00 109.73 ? 94  TYR   R CD1 1 
ATOM   31036 C  CD2 . TYR   R  4  102 ? 60.452  -182.050 17.176  1.00 107.35 ? 94  TYR   R CD2 1 
ATOM   31037 C  CE1 . TYR   R  4  102 ? 58.604  -180.044 16.781  1.00 114.62 ? 94  TYR   R CE1 1 
ATOM   31038 C  CE2 . TYR   R  4  102 ? 59.114  -182.281 17.453  1.00 110.08 ? 94  TYR   R CE2 1 
ATOM   31039 C  CZ  . TYR   R  4  102 ? 58.185  -181.275 17.255  1.00 111.84 ? 94  TYR   R CZ  1 
ATOM   31040 O  OH  . TYR   R  4  102 ? 56.865  -181.491 17.525  1.00 116.12 ? 94  TYR   R OH  1 
ATOM   31041 N  N   . TYR   R  4  103 ? 65.062  -179.528 14.723  1.00 90.67  ? 95  TYR   R N   1 
ATOM   31042 C  CA  . TYR   R  4  103 ? 66.536  -179.428 14.914  1.00 93.21  ? 95  TYR   R CA  1 
ATOM   31043 C  C   . TYR   R  4  103 ? 67.281  -178.904 13.677  1.00 93.94  ? 95  TYR   R C   1 
ATOM   31044 O  O   . TYR   R  4  103 ? 68.521  -178.807 13.768  1.00 93.82  ? 95  TYR   R O   1 
ATOM   31045 C  CB  . TYR   R  4  103 ? 67.103  -180.787 15.328  1.00 92.77  ? 95  TYR   R CB  1 
ATOM   31046 C  CG  . TYR   R  4  103 ? 66.604  -181.283 16.661  1.00 92.75  ? 95  TYR   R CG  1 
ATOM   31047 C  CD1 . TYR   R  4  103 ? 67.066  -180.731 17.844  1.00 91.16  ? 95  TYR   R CD1 1 
ATOM   31048 C  CD2 . TYR   R  4  103 ? 65.667  -182.300 16.740  1.00 92.82  ? 95  TYR   R CD2 1 
ATOM   31049 C  CE1 . TYR   R  4  103 ? 66.611  -181.176 19.074  1.00 90.61  ? 95  TYR   R CE1 1 
ATOM   31050 C  CE2 . TYR   R  4  103 ? 65.202  -182.758 17.961  1.00 92.55  ? 95  TYR   R CE2 1 
ATOM   31051 C  CZ  . TYR   R  4  103 ? 65.676  -182.193 19.131  1.00 91.35  ? 95  TYR   R CZ  1 
ATOM   31052 O  OH  . TYR   R  4  103 ? 65.222  -182.639 20.337  1.00 94.72  ? 95  TYR   R OH  1 
ATOM   31053 N  N   . ASP   R  4  104 ? 66.592  -178.572 12.580  1.00 97.68  ? 96  ASP   R N   1 
ATOM   31054 C  CA  . ASP   R  4  104 ? 67.220  -177.976 11.368  1.00 102.25 ? 96  ASP   R CA  1 
ATOM   31055 C  C   . ASP   R  4  104 ? 68.438  -178.818 10.959  1.00 103.02 ? 96  ASP   R C   1 
ATOM   31056 O  O   . ASP   R  4  104 ? 69.515  -178.235 10.728  1.00 106.21 ? 96  ASP   R O   1 
ATOM   31057 C  CB  . ASP   R  4  104 ? 67.597  -176.513 11.630  1.00 105.46 ? 96  ASP   R CB  1 
ATOM   31058 C  CG  . ASP   R  4  104 ? 68.226  -175.797 10.445  1.00 111.01 ? 96  ASP   R CG  1 
ATOM   31059 O  OD1 . ASP   R  4  104 ? 67.937  -176.193 9.298   1.00 116.88 ? 96  ASP   R OD1 1 
ATOM   31060 O  OD2 . ASP   R  4  104 ? 69.009  -174.852 10.681  1.00 113.93 ? 96  ASP   R OD2 1 
ATOM   31061 N  N   . GLU   R  4  105 ? 68.277  -180.142 10.888  1.00 102.50 ? 97  GLU   R N   1 
ATOM   31062 C  CA  . GLU   R  4  105 ? 69.365  -181.094 10.528  1.00 105.76 ? 97  GLU   R CA  1 
ATOM   31063 C  C   . GLU   R  4  105 ? 68.753  -182.421 10.065  1.00 105.27 ? 97  GLU   R C   1 
ATOM   31064 O  O   . GLU   R  4  105 ? 67.553  -182.642 10.323  1.00 104.87 ? 97  GLU   R O   1 
ATOM   31065 C  CB  . GLU   R  4  105 ? 70.315  -181.300 11.714  1.00 107.06 ? 97  GLU   R CB  1 
ATOM   31066 C  CG  . GLU   R  4  105 ? 69.715  -182.082 12.873  1.00 105.86 ? 97  GLU   R CG  1 
ATOM   31067 C  CD  . GLU   R  4  105 ? 70.673  -182.370 14.020  1.00 105.41 ? 97  GLU   R CD  1 
ATOM   31068 O  OE1 . GLU   R  4  105 ? 70.323  -183.208 14.876  1.00 101.39 ? 97  GLU   R OE1 1 
ATOM   31069 O  OE2 . GLU   R  4  105 ? 71.766  -181.759 14.059  1.00 102.13 ? 97  GLU   R OE2 1 
ATOM   31070 N  N   . ASP   R  4  106 ? 69.552  -183.265 9.406   1.00 106.86 ? 98  ASP   R N   1 
ATOM   31071 C  CA  . ASP   R  4  106 ? 69.164  -184.650 9.027   1.00 108.43 ? 98  ASP   R CA  1 
ATOM   31072 C  C   . ASP   R  4  106 ? 69.207  -185.524 10.283  1.00 106.13 ? 98  ASP   R C   1 
ATOM   31073 O  O   . ASP   R  4  106 ? 70.103  -185.309 11.120  1.00 108.66 ? 98  ASP   R O   1 
ATOM   31074 C  CB  . ASP   R  4  106 ? 70.075  -185.222 7.937   1.00 110.36 ? 98  ASP   R CB  1 
ATOM   31075 C  CG  . ASP   R  4  106 ? 69.837  -184.635 6.556   1.00 111.93 ? 98  ASP   R CG  1 
ATOM   31076 O  OD1 . ASP   R  4  106 ? 69.007  -183.711 6.443   1.00 114.67 ? 98  ASP   R OD1 1 
ATOM   31077 O  OD2 . ASP   R  4  106 ? 70.482  -185.112 5.602   1.00 112.83 ? 98  ASP   R OD2 1 
ATOM   31078 N  N   . ILE   R  4  107 ? 68.281  -186.478 10.394  1.00 108.40 ? 99  ILE   R N   1 
ATOM   31079 C  CA  . ILE   R  4  107 ? 68.166  -187.394 11.569  1.00 106.96 ? 99  ILE   R CA  1 
ATOM   31080 C  C   . ILE   R  4  107 ? 69.075  -188.596 11.296  1.00 102.52 ? 99  ILE   R C   1 
ATOM   31081 O  O   . ILE   R  4  107 ? 69.122  -189.048 10.136  1.00 97.73  ? 99  ILE   R O   1 
ATOM   31082 C  CB  . ILE   R  4  107 ? 66.697  -187.784 11.871  1.00 105.18 ? 99  ILE   R CB  1 
ATOM   31083 C  CG1 . ILE   R  4  107 ? 66.426  -189.288 11.791  1.00 104.79 ? 99  ILE   R CG1 1 
ATOM   31084 C  CG2 . ILE   R  4  107 ? 65.723  -187.009 10.994  1.00 109.03 ? 99  ILE   R CG2 1 
ATOM   31085 C  CD1 . ILE   R  4  107 ? 66.051  -189.761 10.409  1.00 107.70 ? 99  ILE   R CD1 1 
ATOM   31086 N  N   . ASN   R  4  108 ? 69.797  -189.063 12.316  1.00 104.73 ? 100 ASN   R N   1 
ATOM   31087 C  CA  . ASN   R  4  108 ? 70.742  -190.206 12.204  1.00 105.26 ? 100 ASN   R CA  1 
ATOM   31088 C  C   . ASN   R  4  108 ? 69.961  -191.459 11.797  1.00 102.41 ? 100 ASN   R C   1 
ATOM   31089 O  O   . ASN   R  4  108 ? 68.833  -191.644 12.292  1.00 101.57 ? 100 ASN   R O   1 
ATOM   31090 C  CB  . ASN   R  4  108 ? 71.524  -190.440 13.501  1.00 107.46 ? 100 ASN   R CB  1 
ATOM   31091 C  CG  . ASN   R  4  108 ? 72.522  -189.346 13.830  1.00 108.96 ? 100 ASN   R CG  1 
ATOM   31092 O  OD1 . ASN   R  4  108 ? 72.750  -189.052 15.000  1.00 108.37 ? 100 ASN   R OD1 1 
ATOM   31093 N  ND2 . ASN   R  4  108 ? 73.133  -188.741 12.822  1.00 114.87 ? 100 ASN   R ND2 1 
ATOM   31094 N  N   . VAL   R  4  109 ? 70.556  -192.285 10.933  1.00 104.02 ? 101 VAL   R N   1 
ATOM   31095 C  CA  . VAL   R  4  109 ? 69.942  -193.530 10.379  1.00 104.85 ? 101 VAL   R CA  1 
ATOM   31096 C  C   . VAL   R  4  109 ? 69.545  -194.442 11.547  1.00 102.72 ? 101 VAL   R C   1 
ATOM   31097 O  O   . VAL   R  4  109 ? 68.446  -195.026 11.489  1.00 103.26 ? 101 VAL   R O   1 
ATOM   31098 C  CB  . VAL   R  4  109 ? 70.895  -194.250 9.403   1.00 105.70 ? 101 VAL   R CB  1 
ATOM   31099 C  CG1 . VAL   R  4  109 ? 70.291  -195.540 8.867   1.00 103.92 ? 101 VAL   R CG1 1 
ATOM   31100 C  CG2 . VAL   R  4  109 ? 71.318  -193.350 8.251   1.00 107.47 ? 101 VAL   R CG2 1 
ATOM   31101 N  N   . GLU   R  4  110 ? 70.407  -194.548 12.564  1.00 100.53 ? 102 GLU   R N   1 
ATOM   31102 C  CA  . GLU   R  4  110 ? 70.200  -195.419 13.752  1.00 99.62  ? 102 GLU   R CA  1 
ATOM   31103 C  C   . GLU   R  4  110 ? 69.004  -194.903 14.562  1.00 99.45  ? 102 GLU   R C   1 
ATOM   31104 O  O   . GLU   R  4  110 ? 68.200  -195.741 15.019  1.00 93.43  ? 102 GLU   R O   1 
ATOM   31105 C  CB  . GLU   R  4  110 ? 71.463  -195.470 14.613  1.00 101.96 ? 102 GLU   R CB  1 
ATOM   31106 C  CG  . GLU   R  4  110 ? 71.527  -196.689 15.515  1.00 104.71 ? 102 GLU   R CG  1 
ATOM   31107 C  CD  . GLU   R  4  110 ? 71.902  -196.387 16.955  1.00 107.37 ? 102 GLU   R CD  1 
ATOM   31108 O  OE1 . GLU   R  4  110 ? 73.028  -196.740 17.359  1.00 114.21 ? 102 GLU   R OE1 1 
ATOM   31109 O  OE2 . GLU   R  4  110 ? 71.064  -195.805 17.671  1.00 111.09 ? 102 GLU   R OE2 1 
ATOM   31110 N  N   . SER   R  4  111 ? 68.899  -193.578 14.727  1.00 100.16 ? 103 SER   R N   1 
ATOM   31111 C  CA  . SER   R  4  111 ? 67.792  -192.883 15.439  1.00 99.24  ? 103 SER   R CA  1 
ATOM   31112 C  C   . SER   R  4  111 ? 66.465  -193.124 14.711  1.00 97.61  ? 103 SER   R C   1 
ATOM   31113 O  O   . SER   R  4  111 ? 65.451  -193.356 15.401  1.00 99.02  ? 103 SER   R O   1 
ATOM   31114 C  CB  . SER   R  4  111 ? 68.078  -191.417 15.581  1.00 98.87  ? 103 SER   R CB  1 
ATOM   31115 O  OG  . SER   R  4  111 ? 69.263  -191.218 16.336  1.00 102.50 ? 103 SER   R OG  1 
ATOM   31116 N  N   . LEU   R  4  112 ? 66.475  -193.064 13.374  1.00 96.48  ? 104 LEU   R N   1 
ATOM   31117 C  CA  . LEU   R  4  112 ? 65.304  -193.391 12.516  1.00 97.84  ? 104 LEU   R CA  1 
ATOM   31118 C  C   . LEU   R  4  112 ? 64.881  -194.833 12.800  1.00 98.91  ? 104 LEU   R C   1 
ATOM   31119 O  O   . LEU   R  4  112 ? 63.690  -195.053 13.093  1.00 103.31 ? 104 LEU   R O   1 
ATOM   31120 C  CB  . LEU   R  4  112 ? 65.675  -193.224 11.038  1.00 94.88  ? 104 LEU   R CB  1 
ATOM   31121 C  CG  . LEU   R  4  112 ? 64.522  -193.252 10.029  1.00 95.39  ? 104 LEU   R CG  1 
ATOM   31122 C  CD1 . LEU   R  4  112 ? 64.191  -194.674 9.599   1.00 95.81  ? 104 LEU   R CD1 1 
ATOM   31123 C  CD2 . LEU   R  4  112 ? 63.276  -192.560 10.559  1.00 94.28  ? 104 LEU   R CD2 1 
ATOM   31124 N  N   . THR   R  4  113 ? 65.834  -195.767 12.711  1.00 103.41 ? 105 THR   R N   1 
ATOM   31125 C  CA  . THR   R  4  113 ? 65.604  -197.230 12.849  1.00 103.42 ? 105 THR   R CA  1 
ATOM   31126 C  C   . THR   R  4  113 ? 65.016  -197.511 14.236  1.00 102.82 ? 105 THR   R C   1 
ATOM   31127 O  O   . THR   R  4  113 ? 64.046  -198.293 14.306  1.00 100.36 ? 105 THR   R O   1 
ATOM   31128 C  CB  . THR   R  4  113 ? 66.886  -198.030 12.575  1.00 105.72 ? 105 THR   R CB  1 
ATOM   31129 O  OG1 . THR   R  4  113 ? 67.448  -197.576 11.343  1.00 112.06 ? 105 THR   R OG1 1 
ATOM   31130 C  CG2 . THR   R  4  113 ? 66.640  -199.519 12.487  1.00 105.17 ? 105 THR   R CG2 1 
ATOM   31131 N  N   . GLN   R  4  114 ? 65.564  -196.876 15.279  1.00 102.36 ? 106 GLN   R N   1 
ATOM   31132 C  CA  . GLN   R  4  114 ? 65.122  -197.043 16.691  1.00 102.56 ? 106 GLN   R CA  1 
ATOM   31133 C  C   . GLN   R  4  114 ? 63.681  -196.538 16.835  1.00 105.04 ? 106 GLN   R C   1 
ATOM   31134 O  O   . GLN   R  4  114 ? 62.924  -197.152 17.613  1.00 106.80 ? 106 GLN   R O   1 
ATOM   31135 C  CB  . GLN   R  4  114 ? 66.075  -196.323 17.650  1.00 103.70 ? 106 GLN   R CB  1 
ATOM   31136 C  CG  . GLN   R  4  114 ? 65.653  -196.395 19.114  1.00 105.21 ? 106 GLN   R CG  1 
ATOM   31137 C  CD  . GLN   R  4  114 ? 65.628  -197.806 19.649  1.00 104.51 ? 106 GLN   R CD  1 
ATOM   31138 O  OE1 . GLN   R  4  114 ? 64.586  -198.458 19.687  1.00 106.92 ? 106 GLN   R OE1 1 
ATOM   31139 N  NE2 . GLN   R  4  114 ? 66.785  -198.289 20.073  1.00 106.80 ? 106 GLN   R NE2 1 
ATOM   31140 N  N   . SER   R  4  115 ? 63.319  -195.471 16.112  1.00 106.83 ? 107 SER   R N   1 
ATOM   31141 C  CA  . SER   R  4  115 ? 61.961  -194.861 16.110  1.00 107.53 ? 107 SER   R CA  1 
ATOM   31142 C  C   . SER   R  4  115 ? 60.937  -195.827 15.503  1.00 106.29 ? 107 SER   R C   1 
ATOM   31143 O  O   . SER   R  4  115 ? 59.817  -195.910 16.044  1.00 104.87 ? 107 SER   R O   1 
ATOM   31144 C  CB  . SER   R  4  115 ? 61.945  -193.549 15.374  1.00 109.08 ? 107 SER   R CB  1 
ATOM   31145 O  OG  . SER   R  4  115 ? 60.711  -192.877 15.578  1.00 112.67 ? 107 SER   R OG  1 
ATOM   31146 N  N   . VAL   R  4  116 ? 61.299  -196.497 14.403  1.00 108.29 ? 108 VAL   R N   1 
ATOM   31147 C  CA  . VAL   R  4  116 ? 60.435  -197.491 13.696  1.00 108.79 ? 108 VAL   R CA  1 
ATOM   31148 C  C   . VAL   R  4  116 ? 60.255  -198.711 14.608  1.00 104.02 ? 108 VAL   R C   1 
ATOM   31149 O  O   . VAL   R  4  116 ? 59.108  -199.184 14.745  1.00 102.01 ? 108 VAL   R O   1 
ATOM   31150 C  CB  . VAL   R  4  116 ? 61.019  -197.883 12.323  1.00 110.86 ? 108 VAL   R CB  1 
ATOM   31151 C  CG1 . VAL   R  4  116 ? 60.254  -199.032 11.679  1.00 111.21 ? 108 VAL   R CG1 1 
ATOM   31152 C  CG2 . VAL   R  4  116 ? 61.072  -196.693 11.376  1.00 112.63 ? 108 VAL   R CG2 1 
ATOM   31153 N  N   . CYS   R  4  117 ? 61.345  -199.186 15.218  1.00 102.09 ? 109 CYS   R N   1 
ATOM   31154 C  CA  . CYS   R  4  117 ? 61.372  -200.388 16.096  1.00 104.24 ? 109 CYS   R CA  1 
ATOM   31155 C  C   . CYS   R  4  117 ? 60.528  -200.159 17.356  1.00 103.52 ? 109 CYS   R C   1 
ATOM   31156 O  O   . CYS   R  4  117 ? 60.095  -201.155 17.954  1.00 101.77 ? 109 CYS   R O   1 
ATOM   31157 C  CB  . CYS   R  4  117 ? 62.800  -200.767 16.470  1.00 104.67 ? 109 CYS   R CB  1 
ATOM   31158 S  SG  . CYS   R  4  117 ? 63.719  -201.520 15.102  1.00 111.09 ? 109 CYS   R SG  1 
ATOM   31159 N  N   . ASP   R  4  118 ? 60.295  -198.901 17.742  1.00 104.16 ? 110 ASP   R N   1 
ATOM   31160 C  CA  . ASP   R  4  118 ? 59.463  -198.541 18.922  1.00 109.35 ? 110 ASP   R CA  1 
ATOM   31161 C  C   . ASP   R  4  118 ? 57.998  -198.921 18.656  1.00 111.28 ? 110 ASP   R C   1 
ATOM   31162 O  O   . ASP   R  4  118 ? 57.321  -199.303 19.629  1.00 115.55 ? 110 ASP   R O   1 
ATOM   31163 C  CB  . ASP   R  4  118 ? 59.627  -197.064 19.300  1.00 111.46 ? 110 ASP   R CB  1 
ATOM   31164 C  CG  . ASP   R  4  118 ? 60.913  -196.743 20.049  1.00 113.58 ? 110 ASP   R CG  1 
ATOM   31165 O  OD1 . ASP   R  4  118 ? 61.636  -197.693 20.419  1.00 115.82 ? 110 ASP   R OD1 1 
ATOM   31166 O  OD2 . ASP   R  4  118 ? 61.181  -195.542 20.261  1.00 115.25 ? 110 ASP   R OD2 1 
ATOM   31167 N  N   . LEU   R  4  119 ? 57.526  -198.837 17.404  1.00 113.25 ? 111 LEU   R N   1 
ATOM   31168 C  CA  . LEU   R  4  119 ? 56.146  -199.249 17.012  1.00 112.79 ? 111 LEU   R CA  1 
ATOM   31169 C  C   . LEU   R  4  119 ? 55.956  -200.747 17.267  1.00 115.38 ? 111 LEU   R C   1 
ATOM   31170 O  O   . LEU   R  4  119 ? 54.830  -201.139 17.622  1.00 116.47 ? 111 LEU   R O   1 
ATOM   31171 C  CB  . LEU   R  4  119 ? 55.890  -198.968 15.527  1.00 109.62 ? 111 LEU   R CB  1 
ATOM   31172 C  CG  . LEU   R  4  119 ? 55.621  -197.521 15.119  1.00 109.08 ? 111 LEU   R CG  1 
ATOM   31173 C  CD1 . LEU   R  4  119 ? 55.461  -197.436 13.609  1.00 106.62 ? 111 LEU   R CD1 1 
ATOM   31174 C  CD2 . LEU   R  4  119 ? 54.384  -196.963 15.807  1.00 109.27 ? 111 LEU   R CD2 1 
ATOM   31175 N  N   . ALA   R  4  120 ? 57.012  -201.542 17.060  1.00 125.83 ? 112 ALA   R N   1 
ATOM   31176 C  CA  . ALA   R  4  120 ? 56.964  -203.015 16.890  1.00 130.02 ? 112 ALA   R CA  1 
ATOM   31177 C  C   . ALA   R  4  120 ? 56.175  -203.687 18.024  1.00 136.10 ? 112 ALA   R C   1 
ATOM   31178 O  O   . ALA   R  4  120 ? 55.162  -204.345 17.709  1.00 143.30 ? 112 ALA   R O   1 
ATOM   31179 C  CB  . ALA   R  4  120 ? 58.364  -203.569 16.786  1.00 133.70 ? 112 ALA   R CB  1 
ATOM   31180 N  N   . LEU   R  4  121 ? 56.610  -203.537 19.283  1.00 137.48 ? 113 LEU   R N   1 
ATOM   31181 C  CA  . LEU   R  4  121 ? 56.000  -204.241 20.450  1.00 137.48 ? 113 LEU   R CA  1 
ATOM   31182 C  C   . LEU   R  4  121 ? 54.761  -203.487 20.958  1.00 131.04 ? 113 LEU   R C   1 
ATOM   31183 O  O   . LEU   R  4  121 ? 54.181  -203.954 21.959  1.00 131.89 ? 113 LEU   R O   1 
ATOM   31184 C  CB  . LEU   R  4  121 ? 57.026  -204.412 21.581  1.00 136.66 ? 113 LEU   R CB  1 
ATOM   31185 C  CG  . LEU   R  4  121 ? 58.090  -205.503 21.412  1.00 136.02 ? 113 LEU   R CG  1 
ATOM   31186 C  CD1 . LEU   R  4  121 ? 58.850  -205.707 22.715  1.00 136.14 ? 113 LEU   R CD1 1 
ATOM   31187 C  CD2 . LEU   R  4  121 ? 57.496  -206.827 20.955  1.00 132.74 ? 113 LEU   R CD2 1 
ATOM   31188 N  N   . ARG   R  4  122 ? 54.339  -202.397 20.303  1.00 132.79 ? 114 ARG   R N   1 
ATOM   31189 C  CA  . ARG   R  4  122 ? 53.103  -201.648 20.675  1.00 129.96 ? 114 ARG   R CA  1 
ATOM   31190 C  C   . ARG   R  4  122 ? 51.868  -202.420 20.185  1.00 124.33 ? 114 ARG   R C   1 
ATOM   31191 O  O   . ARG   R  4  122 ? 51.018  -201.812 19.507  1.00 126.82 ? 114 ARG   R O   1 
ATOM   31192 C  CB  . ARG   R  4  122 ? 53.123  -200.208 20.142  1.00 133.74 ? 114 ARG   R CB  1 
ATOM   31193 C  CG  . ARG   R  4  122 ? 53.555  -199.176 21.174  1.00 137.70 ? 114 ARG   R CG  1 
ATOM   31194 C  CD  . ARG   R  4  122 ? 53.102  -197.762 20.849  1.00 142.30 ? 114 ARG   R CD  1 
ATOM   31195 N  NE  . ARG   R  4  122 ? 54.076  -197.020 20.058  1.00 149.20 ? 114 ARG   R NE  1 
ATOM   31196 C  CZ  . ARG   R  4  122 ? 55.222  -196.519 20.523  1.00 149.16 ? 114 ARG   R CZ  1 
ATOM   31197 N  NH1 . ARG   R  4  122 ? 55.568  -196.682 21.790  1.00 148.49 ? 114 ARG   R NH1 1 
ATOM   31198 N  NH2 . ARG   R  4  122 ? 56.029  -195.860 19.708  1.00 155.30 ? 114 ARG   R NH2 1 
ATOM   31199 N  N   . PHE   R  4  123 ? 51.771  -203.706 20.538  1.00 117.68 ? 115 PHE   R N   1 
ATOM   31200 C  CA  . PHE   R  4  123 ? 50.594  -204.578 20.285  1.00 113.51 ? 115 PHE   R CA  1 
ATOM   31201 C  C   . PHE   R  4  123 ? 50.163  -205.215 21.609  1.00 111.07 ? 115 PHE   R C   1 
ATOM   31202 O  O   . PHE   R  4  123 ? 50.902  -205.088 22.604  1.00 109.66 ? 115 PHE   R O   1 
ATOM   31203 C  CB  . PHE   R  4  123 ? 50.915  -205.644 19.234  1.00 114.14 ? 115 PHE   R CB  1 
ATOM   31204 C  CG  . PHE   R  4  123 ? 51.844  -206.733 19.706  1.00 115.24 ? 115 PHE   R CG  1 
ATOM   31205 C  CD1 . PHE   R  4  123 ? 53.218  -206.558 19.671  1.00 112.32 ? 115 PHE   R CD1 1 
ATOM   31206 C  CD2 . PHE   R  4  123 ? 51.343  -207.934 20.185  1.00 116.92 ? 115 PHE   R CD2 1 
ATOM   31207 C  CE1 . PHE   R  4  123 ? 54.071  -207.560 20.109  1.00 114.26 ? 115 PHE   R CE1 1 
ATOM   31208 C  CE2 . PHE   R  4  123 ? 52.196  -208.936 20.621  1.00 118.83 ? 115 PHE   R CE2 1 
ATOM   31209 C  CZ  . PHE   R  4  123 ? 53.559  -208.746 20.583  1.00 116.62 ? 115 PHE   R CZ  1 
ATOM   31210 N  N   . GLY   R  4  124 ? 49.008  -205.885 21.609  1.00 112.27 ? 116 GLY   R N   1 
ATOM   31211 C  CA  . GLY   R  4  124 ? 48.452  -206.576 22.787  1.00 115.39 ? 116 GLY   R CA  1 
ATOM   31212 C  C   . GLY   R  4  124 ? 46.973  -206.289 22.968  1.00 118.06 ? 116 GLY   R C   1 
ATOM   31213 O  O   . GLY   R  4  124 ? 46.308  -205.946 21.968  1.00 115.18 ? 116 GLY   R O   1 
ATOM   31214 N  N   . GLU   R  4  125 ? 46.485  -206.424 24.205  1.00 123.32 ? 117 GLU   R N   1 
ATOM   31215 C  CA  . GLU   R  4  125 ? 45.048  -206.323 24.578  1.00 128.27 ? 117 GLU   R CA  1 
ATOM   31216 C  C   . GLU   R  4  125 ? 44.913  -205.346 25.753  1.00 128.48 ? 117 GLU   R C   1 
ATOM   31217 O  O   . GLU   R  4  125 ? 43.846  -205.367 26.395  1.00 132.48 ? 117 GLU   R O   1 
ATOM   31218 C  CB  . GLU   R  4  125 ? 44.514  -207.719 24.918  1.00 134.80 ? 117 GLU   R CB  1 
ATOM   31219 C  CG  . GLU   R  4  125 ? 43.074  -207.958 24.490  1.00 139.10 ? 117 GLU   R CG  1 
ATOM   31220 C  CD  . GLU   R  4  125 ? 42.864  -209.195 23.629  1.00 141.49 ? 117 GLU   R CD  1 
ATOM   31221 O  OE1 . GLU   R  4  125 ? 41.830  -209.865 23.807  1.00 145.07 ? 117 GLU   R OE1 1 
ATOM   31222 O  OE2 . GLU   R  4  125 ? 43.730  -209.481 22.775  1.00 142.71 ? 117 GLU   R OE2 1 
ATOM   31223 N  N   . LEU   R  4  133 ? 47.120  -199.203 21.272  1.00 124.06 ? 125 LEU   R N   1 
ATOM   31224 C  CA  . LEU   R  4  133 ? 48.027  -200.208 20.646  1.00 123.73 ? 125 LEU   R CA  1 
ATOM   31225 C  C   . LEU   R  4  133 ? 47.237  -201.096 19.672  1.00 120.48 ? 125 LEU   R C   1 
ATOM   31226 O  O   . LEU   R  4  133 ? 46.011  -201.243 19.858  1.00 122.37 ? 125 LEU   R O   1 
ATOM   31227 C  CB  . LEU   R  4  133 ? 48.755  -201.039 21.717  1.00 125.22 ? 125 LEU   R CB  1 
ATOM   31228 C  CG  . LEU   R  4  133 ? 47.966  -201.486 22.953  1.00 126.91 ? 125 LEU   R CG  1 
ATOM   31229 C  CD1 . LEU   R  4  133 ? 47.019  -202.635 22.638  1.00 125.78 ? 125 LEU   R CD1 1 
ATOM   31230 C  CD2 . LEU   R  4  133 ? 48.921  -201.894 24.066  1.00 126.73 ? 125 LEU   R CD2 1 
ATOM   31231 N  N   . MET   R  4  134 ? 47.927  -201.642 18.662  1.00 116.30 ? 126 MET   R N   1 
ATOM   31232 C  CA  . MET   R  4  134 ? 47.357  -202.513 17.592  1.00 113.12 ? 126 MET   R CA  1 
ATOM   31233 C  C   . MET   R  4  134 ? 47.172  -203.943 18.125  1.00 111.12 ? 126 MET   R C   1 
ATOM   31234 O  O   . MET   R  4  134 ? 47.642  -204.228 19.242  1.00 114.12 ? 126 MET   R O   1 
ATOM   31235 C  CB  . MET   R  4  134 ? 48.252  -202.523 16.346  1.00 106.97 ? 126 MET   R CB  1 
ATOM   31236 C  CG  . MET   R  4  134 ? 49.661  -203.039 16.581  1.00 105.86 ? 126 MET   R CG  1 
ATOM   31237 S  SD  . MET   R  4  134 ? 50.844  -202.352 15.392  1.00 103.59 ? 126 MET   R SD  1 
ATOM   31238 C  CE  . MET   R  4  134 ? 52.381  -203.011 16.038  1.00 105.21 ? 126 MET   R CE  1 
ATOM   31239 N  N   . SER   R  4  135 ? 46.499  -204.806 17.356  1.00 110.03 ? 127 SER   R N   1 
ATOM   31240 C  CA  . SER   R  4  135 ? 45.984  -206.125 17.815  1.00 110.76 ? 127 SER   R CA  1 
ATOM   31241 C  C   . SER   R  4  135 ? 47.059  -207.213 17.705  1.00 104.99 ? 127 SER   R C   1 
ATOM   31242 O  O   . SER   R  4  135 ? 46.993  -208.173 18.494  1.00 105.10 ? 127 SER   R O   1 
ATOM   31243 C  CB  . SER   R  4  135 ? 44.736  -206.513 17.060  1.00 112.19 ? 127 SER   R CB  1 
ATOM   31244 O  OG  . SER   R  4  135 ? 45.050  -207.087 15.799  1.00 118.56 ? 127 SER   R OG  1 
ATOM   31245 N  N   . ARG   R  4  136 ? 47.997  -207.075 16.762  1.00 100.41 ? 128 ARG   R N   1 
ATOM   31246 C  CA  . ARG   R  4  136 ? 49.030  -208.102 16.454  1.00 101.05 ? 128 ARG   R CA  1 
ATOM   31247 C  C   . ARG   R  4  136 ? 50.327  -207.424 16.028  1.00 101.04 ? 128 ARG   R C   1 
ATOM   31248 O  O   . ARG   R  4  136 ? 50.303  -206.284 15.570  1.00 103.26 ? 128 ARG   R O   1 
ATOM   31249 C  CB  . ARG   R  4  136 ? 48.548  -209.027 15.333  1.00 100.05 ? 128 ARG   R CB  1 
ATOM   31250 C  CG  . ARG   R  4  136 ? 48.105  -208.300 14.070  1.00 100.85 ? 128 ARG   R CG  1 
ATOM   31251 C  CD  . ARG   R  4  136 ? 47.836  -209.250 12.917  1.00 102.70 ? 128 ARG   R CD  1 
ATOM   31252 N  NE  . ARG   R  4  136 ? 47.544  -208.551 11.671  1.00 101.75 ? 128 ARG   R NE  1 
ATOM   31253 C  CZ  . ARG   R  4  136 ? 48.453  -208.022 10.852  1.00 101.56 ? 128 ARG   R CZ  1 
ATOM   31254 N  NH1 . ARG   R  4  136 ? 49.745  -208.098 11.133  1.00 100.80 ? 128 ARG   R NH1 1 
ATOM   31255 N  NH2 . ARG   R  4  136 ? 48.058  -207.404 9.751   1.00 101.49 ? 128 ARG   R NH2 1 
ATOM   31256 N  N   . PRO   R  4  137 ? 51.491  -208.109 16.127  1.00 101.07 ? 129 PRO   R N   1 
ATOM   31257 C  CA  . PRO   R  4  137 ? 52.746  -207.568 15.609  1.00 99.77  ? 129 PRO   R CA  1 
ATOM   31258 C  C   . PRO   R  4  137 ? 52.665  -207.387 14.088  1.00 99.73  ? 129 PRO   R C   1 
ATOM   31259 O  O   . PRO   R  4  137 ? 51.763  -207.940 13.480  1.00 93.09  ? 129 PRO   R O   1 
ATOM   31260 C  CB  . PRO   R  4  137 ? 53.811  -208.621 15.948  1.00 101.06 ? 129 PRO   R CB  1 
ATOM   31261 C  CG  . PRO   R  4  137 ? 53.156  -209.514 16.985  1.00 102.64 ? 129 PRO   R CG  1 
ATOM   31262 C  CD  . PRO   R  4  137 ? 51.666  -209.442 16.719  1.00 101.90 ? 129 PRO   R CD  1 
ATOM   31263 N  N   . PHE   R  4  138 ? 53.599  -206.626 13.516  1.00 105.23 ? 130 PHE   R N   1 
ATOM   31264 C  CA  . PHE   R  4  138 ? 53.759  -206.473 12.048  1.00 105.96 ? 130 PHE   R CA  1 
ATOM   31265 C  C   . PHE   R  4  138 ? 54.208  -207.821 11.476  1.00 103.78 ? 130 PHE   R C   1 
ATOM   31266 O  O   . PHE   R  4  138 ? 54.983  -208.530 12.149  1.00 103.73 ? 130 PHE   R O   1 
ATOM   31267 C  CB  . PHE   R  4  138 ? 54.759  -205.366 11.704  1.00 109.03 ? 130 PHE   R CB  1 
ATOM   31268 C  CG  . PHE   R  4  138 ? 54.360  -203.985 12.162  1.00 111.52 ? 130 PHE   R CG  1 
ATOM   31269 C  CD1 . PHE   R  4  138 ? 53.213  -203.377 11.674  1.00 112.79 ? 130 PHE   R CD1 1 
ATOM   31270 C  CD2 . PHE   R  4  138 ? 55.140  -203.288 13.073  1.00 113.75 ? 130 PHE   R CD2 1 
ATOM   31271 C  CE1 . PHE   R  4  138 ? 52.852  -202.105 12.091  1.00 112.59 ? 130 PHE   R CE1 1 
ATOM   31272 C  CE2 . PHE   R  4  138 ? 54.779  -202.015 13.487  1.00 114.60 ? 130 PHE   R CE2 1 
ATOM   31273 C  CZ  . PHE   R  4  138 ? 53.635  -201.426 12.997  1.00 113.96 ? 130 PHE   R CZ  1 
ATOM   31274 N  N   . GLY   R  4  139 ? 53.718  -208.166 10.283  1.00 99.85  ? 131 GLY   R N   1 
ATOM   31275 C  CA  . GLY   R  4  139 ? 54.121  -209.381 9.552   1.00 98.73  ? 131 GLY   R CA  1 
ATOM   31276 C  C   . GLY   R  4  139 ? 55.126  -209.067 8.461   1.00 98.70  ? 131 GLY   R C   1 
ATOM   31277 O  O   . GLY   R  4  139 ? 55.095  -209.752 7.422   1.00 97.27  ? 131 GLY   R O   1 
ATOM   31278 N  N   . VAL   R  4  140 ? 55.990  -208.073 8.685   1.00 96.86  ? 132 VAL   R N   1 
ATOM   31279 C  CA  . VAL   R  4  140 ? 56.990  -207.600 7.684   1.00 98.81  ? 132 VAL   R CA  1 
ATOM   31280 C  C   . VAL   R  4  140 ? 58.289  -207.211 8.402   1.00 96.78  ? 132 VAL   R C   1 
ATOM   31281 O  O   . VAL   R  4  140 ? 58.220  -206.598 9.488   1.00 93.55  ? 132 VAL   R O   1 
ATOM   31282 C  CB  . VAL   R  4  140 ? 56.419  -206.442 6.841   1.00 101.86 ? 132 VAL   R CB  1 
ATOM   31283 C  CG1 . VAL   R  4  140 ? 56.055  -205.231 7.688   1.00 104.26 ? 132 VAL   R CG1 1 
ATOM   31284 C  CG2 . VAL   R  4  140 ? 57.356  -206.045 5.710   1.00 104.55 ? 132 VAL   R CG2 1 
ATOM   31285 N  N   . ALA   R  4  141 ? 59.427  -207.581 7.807   1.00 95.89  ? 133 ALA   R N   1 
ATOM   31286 C  CA  . ALA   R  4  141 ? 60.790  -207.152 8.198   1.00 100.90 ? 133 ALA   R CA  1 
ATOM   31287 C  C   . ALA   R  4  141 ? 61.248  -206.052 7.237   1.00 102.34 ? 133 ALA   R C   1 
ATOM   31288 O  O   . ALA   R  4  141 ? 60.906  -206.138 6.041   1.00 107.39 ? 133 ALA   R O   1 
ATOM   31289 C  CB  . ALA   R  4  141 ? 61.736  -208.326 8.164   1.00 101.50 ? 133 ALA   R CB  1 
ATOM   31290 N  N   . LEU   R  4  142 ? 61.992  -205.064 7.741   1.00 103.45 ? 134 LEU   R N   1 
ATOM   31291 C  CA  . LEU   R  4  142 ? 62.508  -203.922 6.940   1.00 103.59 ? 134 LEU   R CA  1 
ATOM   31292 C  C   . LEU   R  4  142 ? 64.040  -203.950 6.928   1.00 102.65 ? 134 LEU   R C   1 
ATOM   31293 O  O   . LEU   R  4  142 ? 64.641  -204.186 7.995   1.00 97.25  ? 134 LEU   R O   1 
ATOM   31294 C  CB  . LEU   R  4  142 ? 62.001  -202.603 7.533   1.00 105.03 ? 134 LEU   R CB  1 
ATOM   31295 C  CG  . LEU   R  4  142 ? 60.486  -202.393 7.545   1.00 107.27 ? 134 LEU   R CG  1 
ATOM   31296 C  CD1 . LEU   R  4  142 ? 60.152  -201.005 8.070   1.00 109.30 ? 134 LEU   R CD1 1 
ATOM   31297 C  CD2 . LEU   R  4  142 ? 59.877  -202.591 6.163   1.00 108.49 ? 134 LEU   R CD2 1 
ATOM   31298 N  N   . LEU   R  4  143 ? 64.632  -203.725 5.752   1.00 103.19 ? 135 LEU   R N   1 
ATOM   31299 C  CA  . LEU   R  4  143 ? 66.057  -203.341 5.580   1.00 105.64 ? 135 LEU   R CA  1 
ATOM   31300 C  C   . LEU   R  4  143 ? 66.111  -201.820 5.423   1.00 105.56 ? 135 LEU   R C   1 
ATOM   31301 O  O   . LEU   R  4  143 ? 65.596  -201.325 4.406   1.00 108.54 ? 135 LEU   R O   1 
ATOM   31302 C  CB  . LEU   R  4  143 ? 66.643  -204.032 4.344   1.00 111.00 ? 135 LEU   R CB  1 
ATOM   31303 C  CG  . LEU   R  4  143 ? 66.773  -205.554 4.415   1.00 114.15 ? 135 LEU   R CG  1 
ATOM   31304 C  CD1 . LEU   R  4  143 ? 67.257  -206.112 3.084   1.00 116.79 ? 135 LEU   R CD1 1 
ATOM   31305 C  CD2 . LEU   R  4  143 ? 67.707  -205.983 5.538   1.00 115.97 ? 135 LEU   R CD2 1 
ATOM   31306 N  N   . ILE   R  4  144 ? 66.684  -201.112 6.399   1.00 102.36 ? 136 ILE   R N   1 
ATOM   31307 C  CA  . ILE   R  4  144 ? 66.809  -199.624 6.390   1.00 102.75 ? 136 ILE   R CA  1 
ATOM   31308 C  C   . ILE   R  4  144 ? 68.266  -199.259 6.090   1.00 101.54 ? 136 ILE   R C   1 
ATOM   31309 O  O   . ILE   R  4  144 ? 69.144  -199.589 6.911   1.00 97.40  ? 136 ILE   R O   1 
ATOM   31310 C  CB  . ILE   R  4  144 ? 66.310  -199.021 7.717   1.00 102.02 ? 136 ILE   R CB  1 
ATOM   31311 C  CG1 . ILE   R  4  144 ? 64.806  -199.244 7.891   1.00 100.31 ? 136 ILE   R CG1 1 
ATOM   31312 C  CG2 . ILE   R  4  144 ? 66.675  -197.546 7.808   1.00 103.66 ? 136 ILE   R CG2 1 
ATOM   31313 C  CD1 . ILE   R  4  144 ? 64.304  -199.013 9.295   1.00 100.13 ? 136 ILE   R CD1 1 
ATOM   31314 N  N   . ALA   R  4  145 ? 68.492  -198.589 4.957   1.00 102.87 ? 137 ALA   R N   1 
ATOM   31315 C  CA  . ALA   R  4  145 ? 69.822  -198.208 4.430   1.00 108.10 ? 137 ALA   R CA  1 
ATOM   31316 C  C   . ALA   R  4  145 ? 69.892  -196.683 4.295   1.00 110.84 ? 137 ALA   R C   1 
ATOM   31317 O  O   . ALA   R  4  145 ? 68.946  -196.099 3.729   1.00 112.41 ? 137 ALA   R O   1 
ATOM   31318 C  CB  . ALA   R  4  145 ? 70.055  -198.893 3.107   1.00 108.66 ? 137 ALA   R CB  1 
ATOM   31319 N  N   . GLY   R  4  146 ? 70.965  -196.063 4.795   1.00 110.79 ? 138 GLY   R N   1 
ATOM   31320 C  CA  . GLY   R  4  146 ? 71.127  -194.597 4.760   1.00 112.64 ? 138 GLY   R CA  1 
ATOM   31321 C  C   . GLY   R  4  146 ? 72.561  -194.143 4.981   1.00 112.43 ? 138 GLY   R C   1 
ATOM   31322 O  O   . GLY   R  4  146 ? 73.462  -195.004 5.069   1.00 110.76 ? 138 GLY   R O   1 
ATOM   31323 N  N   . HIS   R  4  147 ? 72.748  -192.821 5.062   1.00 112.85 ? 139 HIS   R N   1 
ATOM   31324 C  CA  . HIS   R  4  147 ? 74.033  -192.137 5.363   1.00 109.58 ? 139 HIS   R CA  1 
ATOM   31325 C  C   . HIS   R  4  147 ? 73.778  -190.958 6.307   1.00 109.63 ? 139 HIS   R C   1 
ATOM   31326 O  O   . HIS   R  4  147 ? 72.783  -190.241 6.090   1.00 106.90 ? 139 HIS   R O   1 
ATOM   31327 C  CB  . HIS   R  4  147 ? 74.712  -191.657 4.074   1.00 107.95 ? 139 HIS   R CB  1 
ATOM   31328 C  CG  . HIS   R  4  147 ? 76.013  -190.971 4.317   1.00 104.60 ? 139 HIS   R CG  1 
ATOM   31329 N  ND1 . HIS   R  4  147 ? 76.101  -189.613 4.528   1.00 103.27 ? 139 HIS   R ND1 1 
ATOM   31330 C  CD2 . HIS   R  4  147 ? 77.271  -191.451 4.404   1.00 104.45 ? 139 HIS   R CD2 1 
ATOM   31331 C  CE1 . HIS   R  4  147 ? 77.360  -189.282 4.728   1.00 105.17 ? 139 HIS   R CE1 1 
ATOM   31332 N  NE2 . HIS   R  4  147 ? 78.098  -190.393 4.657   1.00 104.30 ? 139 HIS   R NE2 1 
ATOM   31333 N  N   . ASP   R  4  148 ? 74.642  -190.783 7.311   1.00 111.54 ? 140 ASP   R N   1 
ATOM   31334 C  CA  . ASP   R  4  148 ? 74.738  -189.548 8.136   1.00 113.49 ? 140 ASP   R CA  1 
ATOM   31335 C  C   . ASP   R  4  148 ? 76.220  -189.213 8.341   1.00 116.32 ? 140 ASP   R C   1 
ATOM   31336 O  O   . ASP   R  4  148 ? 77.070  -190.094 8.089   1.00 114.30 ? 140 ASP   R O   1 
ATOM   31337 C  CB  . ASP   R  4  148 ? 73.961  -189.674 9.451   1.00 112.60 ? 140 ASP   R CB  1 
ATOM   31338 C  CG  . ASP   R  4  148 ? 74.473  -190.741 10.405  1.00 111.82 ? 140 ASP   R CG  1 
ATOM   31339 O  OD1 . ASP   R  4  148 ? 75.668  -190.693 10.758  1.00 108.99 ? 140 ASP   R OD1 1 
ATOM   31340 O  OD2 . ASP   R  4  148 ? 73.663  -191.597 10.806  1.00 115.99 ? 140 ASP   R OD2 1 
ATOM   31341 N  N   . ALA   R  4  149 ? 76.507  -187.984 8.780   1.00 116.54 ? 141 ALA   R N   1 
ATOM   31342 C  CA  . ALA   R  4  149 ? 77.870  -187.415 8.900   1.00 119.00 ? 141 ALA   R CA  1 
ATOM   31343 C  C   . ALA   R  4  149 ? 78.659  -188.116 10.015  1.00 119.82 ? 141 ALA   R C   1 
ATOM   31344 O  O   . ALA   R  4  149 ? 79.903  -188.124 9.928   1.00 124.42 ? 141 ALA   R O   1 
ATOM   31345 C  CB  . ALA   R  4  149 ? 77.783  -185.927 9.141   1.00 117.14 ? 141 ALA   R CB  1 
ATOM   31346 N  N   . ASP   R  4  150 ? 77.972  -188.684 11.014  1.00 119.21 ? 142 ASP   R N   1 
ATOM   31347 C  CA  . ASP   R  4  150 ? 78.593  -189.251 12.242  1.00 120.03 ? 142 ASP   R CA  1 
ATOM   31348 C  C   . ASP   R  4  150 ? 79.134  -190.661 11.968  1.00 119.31 ? 142 ASP   R C   1 
ATOM   31349 O  O   . ASP   R  4  150 ? 80.323  -190.894 12.271  1.00 117.60 ? 142 ASP   R O   1 
ATOM   31350 C  CB  . ASP   R  4  150 ? 77.603  -189.263 13.410  1.00 122.72 ? 142 ASP   R CB  1 
ATOM   31351 C  CG  . ASP   R  4  150 ? 77.153  -187.879 13.842  1.00 125.86 ? 142 ASP   R CG  1 
ATOM   31352 O  OD1 . ASP   R  4  150 ? 75.931  -187.633 13.835  1.00 128.71 ? 142 ASP   R OD1 1 
ATOM   31353 O  OD2 . ASP   R  4  150 ? 78.029  -187.059 14.189  1.00 130.00 ? 142 ASP   R OD2 1 
ATOM   31354 N  N   . ASP   R  4  151 ? 78.298  -191.563 11.437  1.00 117.43 ? 143 ASP   R N   1 
ATOM   31355 C  CA  . ASP   R  4  151 ? 78.600  -193.018 11.318  1.00 115.90 ? 143 ASP   R CA  1 
ATOM   31356 C  C   . ASP   R  4  151 ? 78.614  -193.472 9.850   1.00 115.57 ? 143 ASP   R C   1 
ATOM   31357 O  O   . ASP   R  4  151 ? 78.689  -194.696 9.622   1.00 113.95 ? 143 ASP   R O   1 
ATOM   31358 C  CB  . ASP   R  4  151 ? 77.610  -193.838 12.149  1.00 116.80 ? 143 ASP   R CB  1 
ATOM   31359 C  CG  . ASP   R  4  151 ? 77.844  -193.729 13.647  1.00 117.75 ? 143 ASP   R CG  1 
ATOM   31360 O  OD1 . ASP   R  4  151 ? 78.161  -192.618 14.113  1.00 117.95 ? 143 ASP   R OD1 1 
ATOM   31361 O  OD2 . ASP   R  4  151 ? 77.718  -194.759 14.335  1.00 122.32 ? 143 ASP   R OD2 1 
ATOM   31362 N  N   . GLY   R  4  152 ? 78.567  -192.538 8.893   1.00 116.77 ? 144 GLY   R N   1 
ATOM   31363 C  CA  . GLY   R  4  152 ? 78.663  -192.828 7.448   1.00 117.13 ? 144 GLY   R CA  1 
ATOM   31364 C  C   . GLY   R  4  152 ? 77.557  -193.756 6.968   1.00 113.80 ? 144 GLY   R C   1 
ATOM   31365 O  O   . GLY   R  4  152 ? 76.431  -193.667 7.502   1.00 111.63 ? 144 GLY   R O   1 
ATOM   31366 N  N   . TYR   R  4  153 ? 77.866  -194.618 5.993   1.00 111.28 ? 145 TYR   R N   1 
ATOM   31367 C  CA  . TYR   R  4  153 ? 76.903  -195.539 5.335   1.00 109.41 ? 145 TYR   R CA  1 
ATOM   31368 C  C   . TYR   R  4  153 ? 76.556  -196.685 6.288   1.00 105.82 ? 145 TYR   R C   1 
ATOM   31369 O  O   . TYR   R  4  153 ? 77.479  -197.293 6.859   1.00 103.09 ? 145 TYR   R O   1 
ATOM   31370 C  CB  . TYR   R  4  153 ? 77.472  -196.072 4.019   1.00 110.83 ? 145 TYR   R CB  1 
ATOM   31371 C  CG  . TYR   R  4  153 ? 77.651  -195.016 2.960   1.00 111.23 ? 145 TYR   R CG  1 
ATOM   31372 C  CD1 . TYR   R  4  153 ? 76.555  -194.428 2.351   1.00 111.61 ? 145 TYR   R CD1 1 
ATOM   31373 C  CD2 . TYR   R  4  153 ? 78.913  -194.599 2.572   1.00 112.65 ? 145 TYR   R CD2 1 
ATOM   31374 C  CE1 . TYR   R  4  153 ? 76.708  -193.452 1.380   1.00 114.27 ? 145 TYR   R CE1 1 
ATOM   31375 C  CE2 . TYR   R  4  153 ? 79.084  -193.626 1.600   1.00 115.01 ? 145 TYR   R CE2 1 
ATOM   31376 C  CZ  . TYR   R  4  153 ? 77.978  -193.051 1.001   1.00 114.82 ? 145 TYR   R CZ  1 
ATOM   31377 O  OH  . TYR   R  4  153 ? 78.146  -192.093 0.044   1.00 116.70 ? 145 TYR   R OH  1 
ATOM   31378 N  N   . GLN   R  4  154 ? 75.258  -196.962 6.443   1.00 108.30 ? 146 GLN   R N   1 
ATOM   31379 C  CA  . GLN   R  4  154 ? 74.716  -197.940 7.422   1.00 108.21 ? 146 GLN   R CA  1 
ATOM   31380 C  C   . GLN   R  4  154 ? 73.576  -198.738 6.782   1.00 113.10 ? 146 GLN   R C   1 
ATOM   31381 O  O   . GLN   R  4  154 ? 72.797  -198.148 6.010   1.00 115.43 ? 146 GLN   R O   1 
ATOM   31382 C  CB  . GLN   R  4  154 ? 74.211  -197.214 8.670   1.00 108.38 ? 146 GLN   R CB  1 
ATOM   31383 C  CG  . GLN   R  4  154 ? 75.304  -196.493 9.446   1.00 108.68 ? 146 GLN   R CG  1 
ATOM   31384 C  CD  . GLN   R  4  154 ? 74.765  -195.356 10.282  1.00 106.70 ? 146 GLN   R CD  1 
ATOM   31385 O  OE1 . GLN   R  4  154 ? 74.854  -194.187 9.911   1.00 100.54 ? 146 GLN   R OE1 1 
ATOM   31386 N  NE2 . GLN   R  4  154 ? 74.189  -195.694 11.425  1.00 109.26 ? 146 GLN   R NE2 1 
ATOM   31387 N  N   . LEU   R  4  155 ? 73.504  -200.033 7.102   1.00 117.27 ? 147 LEU   R N   1 
ATOM   31388 C  CA  . LEU   R  4  155 ? 72.383  -200.948 6.761   1.00 118.34 ? 147 LEU   R CA  1 
ATOM   31389 C  C   . LEU   R  4  155 ? 71.856  -201.556 8.064   1.00 115.53 ? 147 LEU   R C   1 
ATOM   31390 O  O   . LEU   R  4  155 ? 72.681  -202.050 8.860   1.00 114.68 ? 147 LEU   R O   1 
ATOM   31391 C  CB  . LEU   R  4  155 ? 72.888  -202.029 5.800   1.00 119.93 ? 147 LEU   R CB  1 
ATOM   31392 C  CG  . LEU   R  4  155 ? 71.887  -203.126 5.434   1.00 120.45 ? 147 LEU   R CG  1 
ATOM   31393 C  CD1 . LEU   R  4  155 ? 70.795  -202.590 4.520   1.00 120.62 ? 147 LEU   R CD1 1 
ATOM   31394 C  CD2 . LEU   R  4  155 ? 72.598  -204.299 4.779   1.00 120.23 ? 147 LEU   R CD2 1 
ATOM   31395 N  N   . PHE   R  4  156 ? 70.539  -201.505 8.273   1.00 112.69 ? 148 PHE   R N   1 
ATOM   31396 C  CA  . PHE   R  4  156 ? 69.855  -202.016 9.488   1.00 109.50 ? 148 PHE   R CA  1 
ATOM   31397 C  C   . PHE   R  4  156 ? 68.760  -203.004 9.086   1.00 104.97 ? 148 PHE   R C   1 
ATOM   31398 O  O   . PHE   R  4  156 ? 68.026  -202.732 8.118   1.00 99.64  ? 148 PHE   R O   1 
ATOM   31399 C  CB  . PHE   R  4  156 ? 69.254  -200.866 10.299  1.00 110.59 ? 148 PHE   R CB  1 
ATOM   31400 C  CG  . PHE   R  4  156 ? 70.258  -200.034 11.056  1.00 111.05 ? 148 PHE   R CG  1 
ATOM   31401 C  CD1 . PHE   R  4  156 ? 70.800  -200.489 12.249  1.00 111.44 ? 148 PHE   R CD1 1 
ATOM   31402 C  CD2 . PHE   R  4  156 ? 70.659  -198.796 10.579  1.00 110.61 ? 148 PHE   R CD2 1 
ATOM   31403 C  CE1 . PHE   R  4  156 ? 71.722  -199.724 12.947  1.00 108.38 ? 148 PHE   R CE1 1 
ATOM   31404 C  CE2 . PHE   R  4  156 ? 71.583  -198.033 11.278  1.00 109.00 ? 148 PHE   R CE2 1 
ATOM   31405 C  CZ  . PHE   R  4  156 ? 72.113  -198.498 12.459  1.00 107.73 ? 148 PHE   R CZ  1 
ATOM   31406 N  N   . HIS   R  4  157 ? 68.671  -204.117 9.816   1.00 105.32 ? 149 HIS   R N   1 
ATOM   31407 C  CA  . HIS   R  4  157 ? 67.554  -205.096 9.755   1.00 104.85 ? 149 HIS   R CA  1 
ATOM   31408 C  C   . HIS   R  4  157 ? 66.618  -204.815 10.935  1.00 103.27 ? 149 HIS   R C   1 
ATOM   31409 O  O   . HIS   R  4  157 ? 67.064  -204.988 12.080  1.00 103.87 ? 149 HIS   R O   1 
ATOM   31410 C  CB  . HIS   R  4  157 ? 68.102  -206.531 9.744   1.00 106.14 ? 149 HIS   R CB  1 
ATOM   31411 C  CG  . HIS   R  4  157 ? 67.045  -207.584 9.741   1.00 104.92 ? 149 HIS   R CG  1 
ATOM   31412 N  ND1 . HIS   R  4  157 ? 67.162  -208.748 10.473  1.00 107.08 ? 149 HIS   R ND1 1 
ATOM   31413 C  CD2 . HIS   R  4  157 ? 65.849  -207.647 9.118   1.00 104.14 ? 149 HIS   R CD2 1 
ATOM   31414 C  CE1 . HIS   R  4  157 ? 66.089  -209.489 10.289  1.00 106.06 ? 149 HIS   R CE1 1 
ATOM   31415 N  NE2 . HIS   R  4  157 ? 65.265  -208.834 9.465   1.00 104.81 ? 149 HIS   R NE2 1 
ATOM   31416 N  N   . ALA   R  4  158 ? 65.390  -204.364 10.658  1.00 100.60 ? 150 ALA   R N   1 
ATOM   31417 C  CA  . ALA   R  4  158 ? 64.352  -204.044 11.666  1.00 101.49 ? 150 ALA   R CA  1 
ATOM   31418 C  C   . ALA   R  4  158 ? 63.289  -205.146 11.680  1.00 102.75 ? 150 ALA   R C   1 
ATOM   31419 O  O   . ALA   R  4  158 ? 62.609  -205.320 10.651  1.00 105.62 ? 150 ALA   R O   1 
ATOM   31420 C  CB  . ALA   R  4  158 ? 63.738  -202.702 11.359  1.00 101.47 ? 150 ALA   R CB  1 
ATOM   31421 N  N   . GLU   R  4  159 ? 63.142  -205.844 12.811  1.00 102.57 ? 151 GLU   R N   1 
ATOM   31422 C  CA  . GLU   R  4  159 ? 62.227  -207.006 12.970  1.00 107.98 ? 151 GLU   R CA  1 
ATOM   31423 C  C   . GLU   R  4  159 ? 60.989  -206.596 13.763  1.00 110.38 ? 151 GLU   R C   1 
ATOM   31424 O  O   . GLU   R  4  159 ? 61.018  -205.616 14.502  1.00 115.71 ? 151 GLU   R O   1 
ATOM   31425 C  CB  . GLU   R  4  159 ? 62.942  -208.158 13.675  1.00 111.29 ? 151 GLU   R CB  1 
ATOM   31426 C  CG  . GLU   R  4  159 ? 63.877  -208.933 12.768  1.00 114.01 ? 151 GLU   R CG  1 
ATOM   31427 C  CD  . GLU   R  4  159 ? 64.613  -210.055 13.476  1.00 119.64 ? 151 GLU   R CD  1 
ATOM   31428 O  OE1 . GLU   R  4  159 ? 64.632  -211.181 12.939  1.00 121.46 ? 151 GLU   R OE1 1 
ATOM   31429 O  OE2 . GLU   R  4  159 ? 65.161  -209.798 14.568  1.00 120.24 ? 151 GLU   R OE2 1 
ATOM   31430 N  N   . PRO   R  4  160 ? 59.862  -207.334 13.621  1.00 112.65 ? 152 PRO   R N   1 
ATOM   31431 C  CA  . PRO   R  4  160 ? 58.672  -207.123 14.452  1.00 112.41 ? 152 PRO   R CA  1 
ATOM   31432 C  C   . PRO   R  4  160 ? 58.837  -207.413 15.954  1.00 112.60 ? 152 PRO   R C   1 
ATOM   31433 O  O   . PRO   R  4  160 ? 57.887  -207.180 16.684  1.00 114.68 ? 152 PRO   R O   1 
ATOM   31434 C  CB  . PRO   R  4  160 ? 57.649  -208.125 13.893  1.00 113.33 ? 152 PRO   R CB  1 
ATOM   31435 C  CG  . PRO   R  4  160 ? 58.136  -208.426 12.496  1.00 114.12 ? 152 PRO   R CG  1 
ATOM   31436 C  CD  . PRO   R  4  160 ? 59.645  -208.358 12.589  1.00 112.31 ? 152 PRO   R CD  1 
ATOM   31437 N  N   . SER   R  4  161 ? 59.998  -207.933 16.370  1.00 113.46 ? 153 SER   R N   1 
ATOM   31438 C  CA  . SER   R  4  161 ? 60.385  -208.155 17.790  1.00 114.10 ? 153 SER   R CA  1 
ATOM   31439 C  C   . SER   R  4  161 ? 60.689  -206.821 18.482  1.00 116.09 ? 153 SER   R C   1 
ATOM   31440 O  O   . SER   R  4  161 ? 60.662  -206.787 19.730  1.00 111.06 ? 153 SER   R O   1 
ATOM   31441 C  CB  . SER   R  4  161 ? 61.572  -209.072 17.885  1.00 116.86 ? 153 SER   R CB  1 
ATOM   31442 O  OG  . SER   R  4  161 ? 62.677  -208.534 17.173  1.00 119.25 ? 153 SER   R OG  1 
ATOM   31443 N  N   . GLY   R  4  162 ? 60.995  -205.781 17.698  1.00 113.32 ? 154 GLY   R N   1 
ATOM   31444 C  CA  . GLY   R  4  162 ? 61.446  -204.465 18.186  1.00 111.73 ? 154 GLY   R CA  1 
ATOM   31445 C  C   . GLY   R  4  162 ? 62.961  -204.388 18.242  1.00 114.20 ? 154 GLY   R C   1 
ATOM   31446 O  O   . GLY   R  4  162 ? 63.478  -203.374 18.745  1.00 117.45 ? 154 GLY   R O   1 
ATOM   31447 N  N   . THR   R  4  163 ? 63.647  -205.420 17.742  1.00 112.81 ? 155 THR   R N   1 
ATOM   31448 C  CA  . THR   R  4  163 ? 65.128  -205.502 17.681  1.00 110.67 ? 155 THR   R CA  1 
ATOM   31449 C  C   . THR   R  4  163 ? 65.594  -205.083 16.286  1.00 109.24 ? 155 THR   R C   1 
ATOM   31450 O  O   . THR   R  4  163 ? 64.897  -205.411 15.305  1.00 110.66 ? 155 THR   R O   1 
ATOM   31451 C  CB  . THR   R  4  163 ? 65.628  -206.909 18.024  1.00 114.67 ? 155 THR   R CB  1 
ATOM   31452 O  OG1 . THR   R  4  163 ? 64.967  -207.317 19.223  1.00 107.99 ? 155 THR   R OG1 1 
ATOM   31453 C  CG2 . THR   R  4  163 ? 67.129  -206.963 18.204  1.00 118.79 ? 155 THR   R CG2 1 
ATOM   31454 N  N   . PHE   R  4  164 ? 66.726  -204.380 16.218  1.00 107.68 ? 156 PHE   R N   1 
ATOM   31455 C  CA  . PHE   R  4  164 ? 67.431  -204.031 14.960  1.00 108.54 ? 156 PHE   R CA  1 
ATOM   31456 C  C   . PHE   R  4  164 ? 68.929  -204.277 15.149  1.00 107.38 ? 156 PHE   R C   1 
ATOM   31457 O  O   . PHE   R  4  164 ? 69.481  -203.899 16.199  1.00 111.25 ? 156 PHE   R O   1 
ATOM   31458 C  CB  . PHE   R  4  164 ? 67.140  -202.587 14.543  1.00 107.83 ? 156 PHE   R CB  1 
ATOM   31459 C  CG  . PHE   R  4  164 ? 67.570  -201.541 15.539  1.00 106.26 ? 156 PHE   R CG  1 
ATOM   31460 C  CD1 . PHE   R  4  164 ? 66.825  -201.305 16.684  1.00 102.82 ? 156 PHE   R CD1 1 
ATOM   31461 C  CD2 . PHE   R  4  164 ? 68.720  -200.794 15.334  1.00 106.05 ? 156 PHE   R CD2 1 
ATOM   31462 C  CE1 . PHE   R  4  164 ? 67.223  -200.350 17.604  1.00 103.27 ? 156 PHE   R CE1 1 
ATOM   31463 C  CE2 . PHE   R  4  164 ? 69.116  -199.836 16.253  1.00 107.03 ? 156 PHE   R CE2 1 
ATOM   31464 C  CZ  . PHE   R  4  164 ? 68.366  -199.614 17.386  1.00 106.73 ? 156 PHE   R CZ  1 
ATOM   31465 N  N   . TYR   R  4  165 ? 69.545  -204.926 14.161  1.00 111.93 ? 157 TYR   R N   1 
ATOM   31466 C  CA  . TYR   R  4  165 ? 71.007  -205.148 14.055  1.00 115.72 ? 157 TYR   R CA  1 
ATOM   31467 C  C   . TYR   R  4  165 ? 71.536  -204.283 12.910  1.00 111.29 ? 157 TYR   R C   1 
ATOM   31468 O  O   . TYR   R  4  165 ? 70.814  -204.124 11.905  1.00 112.34 ? 157 TYR   R O   1 
ATOM   31469 C  CB  . TYR   R  4  165 ? 71.308  -206.629 13.805  1.00 121.07 ? 157 TYR   R CB  1 
ATOM   31470 C  CG  . TYR   R  4  165 ? 71.368  -207.490 15.042  1.00 129.00 ? 157 TYR   R CG  1 
ATOM   31471 C  CD1 . TYR   R  4  165 ? 72.535  -207.586 15.784  1.00 134.19 ? 157 TYR   R CD1 1 
ATOM   31472 C  CD2 . TYR   R  4  165 ? 70.270  -208.226 15.461  1.00 127.71 ? 157 TYR   R CD2 1 
ATOM   31473 C  CE1 . TYR   R  4  165 ? 72.608  -208.382 16.916  1.00 138.10 ? 157 TYR   R CE1 1 
ATOM   31474 C  CE2 . TYR   R  4  165 ? 70.326  -209.028 16.590  1.00 132.37 ? 157 TYR   R CE2 1 
ATOM   31475 C  CZ  . TYR   R  4  165 ? 71.500  -209.107 17.322  1.00 137.84 ? 157 TYR   R CZ  1 
ATOM   31476 O  OH  . TYR   R  4  165 ? 71.564  -209.894 18.436  1.00 135.84 ? 157 TYR   R OH  1 
ATOM   31477 N  N   . ARG   R  4  166 ? 72.740  -203.727 13.061  1.00 109.29 ? 158 ARG   R N   1 
ATOM   31478 C  CA  . ARG   R  4  166 ? 73.507  -203.161 11.923  1.00 112.22 ? 158 ARG   R CA  1 
ATOM   31479 C  C   . ARG   R  4  166 ? 74.157  -204.334 11.182  1.00 110.89 ? 158 ARG   R C   1 
ATOM   31480 O  O   . ARG   R  4  166 ? 74.625  -205.267 11.858  1.00 110.87 ? 158 ARG   R O   1 
ATOM   31481 C  CB  . ARG   R  4  166 ? 74.559  -202.147 12.381  1.00 109.58 ? 158 ARG   R CB  1 
ATOM   31482 C  CG  . ARG   R  4  166 ? 75.089  -201.286 11.245  1.00 111.76 ? 158 ARG   R CG  1 
ATOM   31483 C  CD  . ARG   R  4  166 ? 76.148  -200.290 11.678  1.00 112.43 ? 158 ARG   R CD  1 
ATOM   31484 N  NE  . ARG   R  4  166 ? 76.934  -199.825 10.541  1.00 114.03 ? 158 ARG   R NE  1 
ATOM   31485 C  CZ  . ARG   R  4  166 ? 77.873  -198.882 10.590  1.00 111.01 ? 158 ARG   R CZ  1 
ATOM   31486 N  NH1 . ARG   R  4  166 ? 78.159  -198.272 11.728  1.00 105.33 ? 158 ARG   R NH1 1 
ATOM   31487 N  NH2 . ARG   R  4  166 ? 78.522  -198.549 9.487   1.00 113.86 ? 158 ARG   R NH2 1 
ATOM   31488 N  N   . TYR   R  4  167 ? 74.162  -204.293 9.849   1.00 113.43 ? 159 TYR   R N   1 
ATOM   31489 C  CA  . TYR   R  4  167 ? 74.724  -205.351 8.972   1.00 111.58 ? 159 TYR   R CA  1 
ATOM   31490 C  C   . TYR   R  4  167 ? 75.656  -204.713 7.942   1.00 113.19 ? 159 TYR   R C   1 
ATOM   31491 O  O   . TYR   R  4  167 ? 75.369  -203.588 7.489   1.00 116.04 ? 159 TYR   R O   1 
ATOM   31492 C  CB  . TYR   R  4  167 ? 73.603  -206.123 8.272   1.00 111.73 ? 159 TYR   R CB  1 
ATOM   31493 C  CG  . TYR   R  4  167 ? 72.999  -207.248 9.073   1.00 110.52 ? 159 TYR   R CG  1 
ATOM   31494 C  CD1 . TYR   R  4  167 ? 71.835  -207.063 9.802   1.00 108.26 ? 159 TYR   R CD1 1 
ATOM   31495 C  CD2 . TYR   R  4  167 ? 73.575  -208.509 9.082   1.00 111.40 ? 159 TYR   R CD2 1 
ATOM   31496 C  CE1 . TYR   R  4  167 ? 71.266  -208.096 10.529  1.00 107.21 ? 159 TYR   R CE1 1 
ATOM   31497 C  CE2 . TYR   R  4  167 ? 73.018  -209.553 9.803   1.00 111.03 ? 159 TYR   R CE2 1 
ATOM   31498 C  CZ  . TYR   R  4  167 ? 71.860  -209.344 10.533  1.00 108.82 ? 159 TYR   R CZ  1 
ATOM   31499 O  OH  . TYR   R  4  167 ? 71.291  -210.354 11.251  1.00 106.45 ? 159 TYR   R OH  1 
ATOM   31500 N  N   . ASN   R  4  168 ? 76.740  -205.411 7.597   1.00 111.26 ? 160 ASN   R N   1 
ATOM   31501 C  CA  . ASN   R  4  168 ? 77.585  -205.098 6.415   1.00 114.82 ? 160 ASN   R CA  1 
ATOM   31502 C  C   . ASN   R  4  168 ? 76.824  -205.537 5.161   1.00 115.77 ? 160 ASN   R C   1 
ATOM   31503 O  O   . ASN   R  4  168 ? 76.937  -204.855 4.122   1.00 118.73 ? 160 ASN   R O   1 
ATOM   31504 C  CB  . ASN   R  4  168 ? 78.957  -205.770 6.496   1.00 117.06 ? 160 ASN   R CB  1 
ATOM   31505 C  CG  . ASN   R  4  168 ? 79.862  -205.179 7.557   1.00 117.36 ? 160 ASN   R CG  1 
ATOM   31506 O  OD1 . ASN   R  4  168 ? 80.503  -205.917 8.301   1.00 123.25 ? 160 ASN   R OD1 1 
ATOM   31507 N  ND2 . ASN   R  4  168 ? 79.941  -203.860 7.632   1.00 116.51 ? 160 ASN   R ND2 1 
ATOM   31508 N  N   . ALA   R  4  169 ? 76.082  -206.642 5.274   1.00 115.11 ? 161 ALA   R N   1 
ATOM   31509 C  CA  . ALA   R  4  169 ? 75.172  -207.185 4.239   1.00 115.44 ? 161 ALA   R CA  1 
ATOM   31510 C  C   . ALA   R  4  169 ? 74.115  -208.062 4.919   1.00 112.15 ? 161 ALA   R C   1 
ATOM   31511 O  O   . ALA   R  4  169 ? 74.424  -208.648 5.974   1.00 115.35 ? 161 ALA   R O   1 
ATOM   31512 C  CB  . ALA   R  4  169 ? 75.964  -207.957 3.214   1.00 117.75 ? 161 ALA   R CB  1 
ATOM   31513 N  N   . LYS   R  4  170 ? 72.912  -208.144 4.347   1.00 108.15 ? 162 LYS   R N   1 
ATOM   31514 C  CA  . LYS   R  4  170 ? 71.789  -208.909 4.949   1.00 109.24 ? 162 LYS   R CA  1 
ATOM   31515 C  C   . LYS   R  4  170 ? 70.725  -209.216 3.892   1.00 110.84 ? 162 LYS   R C   1 
ATOM   31516 O  O   . LYS   R  4  170 ? 70.335  -208.291 3.151   1.00 109.61 ? 162 LYS   R O   1 
ATOM   31517 C  CB  . LYS   R  4  170 ? 71.187  -208.122 6.115   1.00 105.93 ? 162 LYS   R CB  1 
ATOM   31518 C  CG  . LYS   R  4  170 ? 70.002  -208.780 6.808   1.00 105.86 ? 162 LYS   R CG  1 
ATOM   31519 C  CD  . LYS   R  4  170 ? 70.311  -210.136 7.396   1.00 108.67 ? 162 LYS   R CD  1 
ATOM   31520 C  CE  . LYS   R  4  170 ? 69.196  -210.646 8.285   1.00 111.78 ? 162 LYS   R CE  1 
ATOM   31521 N  NZ  . LYS   R  4  170 ? 69.416  -212.052 8.700   1.00 114.49 ? 162 LYS   R NZ  1 
ATOM   31522 N  N   . ALA   R  4  171 ? 70.281  -210.478 3.853   1.00 114.05 ? 163 ALA   R N   1 
ATOM   31523 C  CA  . ALA   R  4  171 ? 69.141  -210.978 3.053   1.00 112.35 ? 163 ALA   R CA  1 
ATOM   31524 C  C   . ALA   R  4  171 ? 67.984  -211.323 3.998   1.00 107.66 ? 163 ALA   R C   1 
ATOM   31525 O  O   . ALA   R  4  171 ? 68.254  -211.872 5.085   1.00 105.67 ? 163 ALA   R O   1 
ATOM   31526 C  CB  . ALA   R  4  171 ? 69.569  -212.179 2.247   1.00 114.55 ? 163 ALA   R CB  1 
ATOM   31527 N  N   . ILE   R  4  172 ? 66.750  -210.999 3.599   1.00 106.77 ? 164 ILE   R N   1 
ATOM   31528 C  CA  . ILE   R  4  172 ? 65.498  -211.357 4.333   1.00 107.79 ? 164 ILE   R CA  1 
ATOM   31529 C  C   . ILE   R  4  172 ? 64.498  -211.946 3.334   1.00 107.87 ? 164 ILE   R C   1 
ATOM   31530 O  O   . ILE   R  4  172 ? 64.516  -211.522 2.162   1.00 107.38 ? 164 ILE   R O   1 
ATOM   31531 C  CB  . ILE   R  4  172 ? 64.909  -210.141 5.078   1.00 106.92 ? 164 ILE   R CB  1 
ATOM   31532 C  CG1 . ILE   R  4  172 ? 64.797  -208.908 4.176   1.00 107.29 ? 164 ILE   R CG1 1 
ATOM   31533 C  CG2 . ILE   R  4  172 ? 65.710  -209.845 6.336   1.00 107.85 ? 164 ILE   R CG2 1 
ATOM   31534 C  CD1 . ILE   R  4  172 ? 63.882  -207.829 4.712   1.00 106.31 ? 164 ILE   R CD1 1 
ATOM   31535 N  N   . GLY   R  4  173 ? 63.671  -212.891 3.791   1.00 109.40 ? 165 GLY   R N   1 
ATOM   31536 C  CA  . GLY   R  4  173 ? 62.610  -213.533 2.992   1.00 111.97 ? 165 GLY   R CA  1 
ATOM   31537 C  C   . GLY   R  4  173 ? 62.873  -215.013 2.779   1.00 114.44 ? 165 GLY   R C   1 
ATOM   31538 O  O   . GLY   R  4  173 ? 63.699  -215.584 3.516   1.00 117.72 ? 165 GLY   R O   1 
ATOM   31539 N  N   . SER   R  4  174 ? 62.191  -215.610 1.799   1.00 118.19 ? 166 SER   R N   1 
ATOM   31540 C  CA  . SER   R  4  174 ? 62.191  -217.068 1.508   1.00 119.71 ? 166 SER   R CA  1 
ATOM   31541 C  C   . SER   R  4  174 ? 63.609  -217.573 1.214   1.00 123.66 ? 166 SER   R C   1 
ATOM   31542 O  O   . SER   R  4  174 ? 63.952  -218.667 1.706   1.00 132.38 ? 166 SER   R O   1 
ATOM   31543 C  CB  . SER   R  4  174 ? 61.252  -217.381 0.373   1.00 119.97 ? 166 SER   R CB  1 
ATOM   31544 O  OG  . SER   R  4  174 ? 61.465  -216.490 -0.712  1.00 116.52 ? 166 SER   R OG  1 
ATOM   31545 N  N   . GLY   R  4  175 ? 64.397  -216.811 0.449   1.00 123.20 ? 167 GLY   R N   1 
ATOM   31546 C  CA  . GLY   R  4  175 ? 65.737  -217.228 -0.011  1.00 125.38 ? 167 GLY   R CA  1 
ATOM   31547 C  C   . GLY   R  4  175 ? 66.857  -216.764 0.908   1.00 125.43 ? 167 GLY   R C   1 
ATOM   31548 O  O   . GLY   R  4  175 ? 68.020  -216.823 0.471   1.00 123.24 ? 167 GLY   R O   1 
ATOM   31549 N  N   . SER   R  4  176 ? 66.540  -216.350 2.141   1.00 127.84 ? 168 SER   R N   1 
ATOM   31550 C  CA  . SER   R  4  176 ? 67.452  -215.583 3.036   1.00 125.36 ? 168 SER   R CA  1 
ATOM   31551 C  C   . SER   R  4  176 ? 68.635  -216.437 3.518   1.00 129.92 ? 168 SER   R C   1 
ATOM   31552 O  O   . SER   R  4  176 ? 69.780  -215.969 3.365   1.00 128.90 ? 168 SER   R O   1 
ATOM   31553 C  CB  . SER   R  4  176 ? 66.710  -214.983 4.203   1.00 126.88 ? 168 SER   R CB  1 
ATOM   31554 O  OG  . SER   R  4  176 ? 66.196  -215.994 5.056   1.00 129.57 ? 168 SER   R OG  1 
ATOM   31555 N  N   . GLU   R  4  177 ? 68.384  -217.619 4.095   1.00 129.57 ? 169 GLU   R N   1 
ATOM   31556 C  CA  . GLU   R  4  177 ? 69.431  -218.432 4.780   1.00 125.94 ? 169 GLU   R CA  1 
ATOM   31557 C  C   . GLU   R  4  177 ? 70.477  -218.882 3.750   1.00 118.65 ? 169 GLU   R C   1 
ATOM   31558 O  O   . GLU   R  4  177 ? 71.671  -218.930 4.111   1.00 116.19 ? 169 GLU   R O   1 
ATOM   31559 C  CB  . GLU   R  4  177 ? 68.816  -219.603 5.554   1.00 129.71 ? 169 GLU   R CB  1 
ATOM   31560 C  CG  . GLU   R  4  177 ? 68.757  -220.911 4.783   1.00 132.88 ? 169 GLU   R CG  1 
ATOM   31561 C  CD  . GLU   R  4  177 ? 68.139  -222.067 5.550   1.00 138.68 ? 169 GLU   R CD  1 
ATOM   31562 O  OE1 . GLU   R  4  177 ? 67.086  -221.856 6.186   1.00 146.48 ? 169 GLU   R OE1 1 
ATOM   31563 O  OE2 . GLU   R  4  177 ? 68.715  -223.175 5.514   1.00 136.80 ? 169 GLU   R OE2 1 
ATOM   31564 N  N   . GLY   R  4  178 ? 70.045  -219.189 2.522   1.00 120.76 ? 170 GLY   R N   1 
ATOM   31565 C  CA  . GLY   R  4  178 ? 70.926  -219.538 1.390   1.00 127.71 ? 170 GLY   R CA  1 
ATOM   31566 C  C   . GLY   R  4  178 ? 71.690  -218.328 0.877   1.00 129.33 ? 170 GLY   R C   1 
ATOM   31567 O  O   . GLY   R  4  178 ? 72.902  -218.462 0.618   1.00 139.23 ? 170 GLY   R O   1 
ATOM   31568 N  N   . ALA   R  4  179 ? 71.005  -217.188 0.732   1.00 130.86 ? 171 ALA   R N   1 
ATOM   31569 C  CA  . ALA   R  4  179 ? 71.573  -215.902 0.258   1.00 130.92 ? 171 ALA   R CA  1 
ATOM   31570 C  C   . ALA   R  4  179 ? 72.543  -215.329 1.301   1.00 130.71 ? 171 ALA   R C   1 
ATOM   31571 O  O   . ALA   R  4  179 ? 73.570  -214.751 0.890   1.00 130.75 ? 171 ALA   R O   1 
ATOM   31572 C  CB  . ALA   R  4  179 ? 70.463  -214.925 -0.055  1.00 131.11 ? 171 ALA   R CB  1 
ATOM   31573 N  N   . GLN   R  4  180 ? 72.229  -215.474 2.594   1.00 126.14 ? 172 GLN   R N   1 
ATOM   31574 C  CA  . GLN   R  4  180 ? 73.045  -214.938 3.720   1.00 125.74 ? 172 GLN   R CA  1 
ATOM   31575 C  C   . GLN   R  4  180 ? 74.384  -215.681 3.774   1.00 126.89 ? 172 GLN   R C   1 
ATOM   31576 O  O   . GLN   R  4  180 ? 75.413  -215.017 4.012   1.00 121.04 ? 172 GLN   R O   1 
ATOM   31577 C  CB  . GLN   R  4  180 ? 72.295  -215.062 5.049   1.00 125.92 ? 172 GLN   R CB  1 
ATOM   31578 C  CG  . GLN   R  4  180 ? 72.990  -214.370 6.215   1.00 130.91 ? 172 GLN   R CG  1 
ATOM   31579 C  CD  . GLN   R  4  180 ? 72.962  -212.862 6.115   1.00 132.25 ? 172 GLN   R CD  1 
ATOM   31580 O  OE1 . GLN   R  4  180 ? 72.258  -212.283 5.290   1.00 134.00 ? 172 GLN   R OE1 1 
ATOM   31581 N  NE2 . GLN   R  4  180 ? 73.732  -212.208 6.969   1.00 137.74 ? 172 GLN   R NE2 1 
ATOM   31582 N  N   . ALA   R  4  181 ? 74.358  -217.004 3.568   1.00 130.07 ? 173 ALA   R N   1 
ATOM   31583 C  CA  . ALA   R  4  181 ? 75.547  -217.886 3.492   1.00 130.71 ? 173 ALA   R CA  1 
ATOM   31584 C  C   . ALA   R  4  181 ? 76.444  -217.449 2.327   1.00 132.57 ? 173 ALA   R C   1 
ATOM   31585 O  O   . ALA   R  4  181 ? 77.680  -217.538 2.469   1.00 132.78 ? 173 ALA   R O   1 
ATOM   31586 C  CB  . ALA   R  4  181 ? 75.118  -219.325 3.342   1.00 132.55 ? 173 ALA   R CB  1 
ATOM   31587 N  N   . GLU   R  4  182 ? 75.837  -217.001 1.220   1.00 132.24 ? 174 GLU   R N   1 
ATOM   31588 C  CA  . GLU   R  4  182 ? 76.547  -216.497 0.013   1.00 133.91 ? 174 GLU   R CA  1 
ATOM   31589 C  C   . GLU   R  4  182 ? 77.175  -215.135 0.333   1.00 132.20 ? 174 GLU   R C   1 
ATOM   31590 O  O   . GLU   R  4  182 ? 78.340  -214.924 -0.048  1.00 130.86 ? 174 GLU   R O   1 
ATOM   31591 C  CB  . GLU   R  4  182 ? 75.592  -216.398 -1.181  1.00 136.15 ? 174 GLU   R CB  1 
ATOM   31592 C  CG  . GLU   R  4  182 ? 76.284  -216.542 -2.526  1.00 141.55 ? 174 GLU   R CG  1 
ATOM   31593 C  CD  . GLU   R  4  182 ? 76.764  -217.948 -2.851  1.00 142.58 ? 174 GLU   R CD  1 
ATOM   31594 O  OE1 . GLU   R  4  182 ? 77.887  -218.082 -3.376  1.00 150.18 ? 174 GLU   R OE1 1 
ATOM   31595 O  OE2 . GLU   R  4  182 ? 76.008  -218.907 -2.592  1.00 144.89 ? 174 GLU   R OE2 1 
ATOM   31596 N  N   . LEU   R  4  183 ? 76.433  -214.255 1.015   1.00 131.25 ? 175 LEU   R N   1 
ATOM   31597 C  CA  . LEU   R  4  183 ? 76.894  -212.896 1.417   1.00 132.98 ? 175 LEU   R CA  1 
ATOM   31598 C  C   . LEU   R  4  183 ? 78.046  -212.997 2.426   1.00 132.08 ? 175 LEU   R C   1 
ATOM   31599 O  O   . LEU   R  4  183 ? 78.869  -212.061 2.465   1.00 128.20 ? 175 LEU   R O   1 
ATOM   31600 C  CB  . LEU   R  4  183 ? 75.720  -212.106 2.007   1.00 133.11 ? 175 LEU   R CB  1 
ATOM   31601 C  CG  . LEU   R  4  183 ? 74.731  -211.529 0.993   1.00 134.42 ? 175 LEU   R CG  1 
ATOM   31602 C  CD1 . LEU   R  4  183 ? 73.486  -211.005 1.692   1.00 132.29 ? 175 LEU   R CD1 1 
ATOM   31603 C  CD2 . LEU   R  4  183 ? 75.376  -210.429 0.160   1.00 136.73 ? 175 LEU   R CD2 1 
ATOM   31604 N  N   . LEU   R  4  184 ? 78.099  -214.077 3.214   1.00 134.08 ? 176 LEU   R N   1 
ATOM   31605 C  CA  . LEU   R  4  184 ? 79.179  -214.330 4.208   1.00 136.54 ? 176 LEU   R CA  1 
ATOM   31606 C  C   . LEU   R  4  184 ? 80.513  -214.474 3.464   1.00 137.16 ? 176 LEU   R C   1 
ATOM   31607 O  O   . LEU   R  4  184 ? 81.520  -213.923 3.947   1.00 133.87 ? 176 LEU   R O   1 
ATOM   31608 C  CB  . LEU   R  4  184 ? 78.861  -215.596 5.015   1.00 138.71 ? 176 LEU   R CB  1 
ATOM   31609 C  CG  . LEU   R  4  184 ? 79.135  -215.529 6.519   1.00 139.84 ? 176 LEU   R CG  1 
ATOM   31610 C  CD1 . LEU   R  4  184 ? 80.477  -214.875 6.829   1.00 136.92 ? 176 LEU   R CD1 1 
ATOM   31611 C  CD2 . LEU   R  4  184 ? 78.008  -214.805 7.240   1.00 139.22 ? 176 LEU   R CD2 1 
ATOM   31612 N  N   . ASN   R  4  185 ? 80.502  -215.182 2.329   1.00 141.87 ? 177 ASN   R N   1 
ATOM   31613 C  CA  . ASN   R  4  185 ? 81.701  -215.492 1.503   1.00 146.25 ? 177 ASN   R CA  1 
ATOM   31614 C  C   . ASN   R  4  185 ? 82.116  -214.256 0.695   1.00 146.73 ? 177 ASN   R C   1 
ATOM   31615 O  O   . ASN   R  4  185 ? 83.329  -213.984 0.628   1.00 151.08 ? 177 ASN   R O   1 
ATOM   31616 C  CB  . ASN   R  4  185 ? 81.457  -216.686 0.574   1.00 144.50 ? 177 ASN   R CB  1 
ATOM   31617 C  CG  . ASN   R  4  185 ? 81.392  -218.008 1.309   1.00 147.24 ? 177 ASN   R CG  1 
ATOM   31618 O  OD1 . ASN   R  4  185 ? 82.110  -218.215 2.284   1.00 145.94 ? 177 ASN   R OD1 1 
ATOM   31619 N  ND2 . ASN   R  4  185 ? 80.540  -218.912 0.849   1.00 147.95 ? 177 ASN   R ND2 1 
ATOM   31620 N  N   . GLU   R  4  186 ? 81.150  -213.538 0.114   1.00 145.45 ? 178 GLU   R N   1 
ATOM   31621 C  CA  . GLU   R  4  186 ? 81.391  -212.545 -0.969  1.00 148.18 ? 178 GLU   R CA  1 
ATOM   31622 C  C   . GLU   R  4  186 ? 81.812  -211.185 -0.391  1.00 147.69 ? 178 GLU   R C   1 
ATOM   31623 O  O   . GLU   R  4  186 ? 82.652  -210.525 -1.036  1.00 152.58 ? 178 GLU   R O   1 
ATOM   31624 C  CB  . GLU   R  4  186 ? 80.150  -212.395 -1.851  1.00 149.92 ? 178 GLU   R CB  1 
ATOM   31625 C  CG  . GLU   R  4  186 ? 79.726  -213.679 -2.546  1.00 152.39 ? 178 GLU   R CG  1 
ATOM   31626 C  CD  . GLU   R  4  186 ? 80.492  -214.015 -3.815  1.00 155.38 ? 178 GLU   R CD  1 
ATOM   31627 O  OE1 . GLU   R  4  186 ? 79.870  -214.558 -4.749  1.00 156.15 ? 178 GLU   R OE1 1 
ATOM   31628 O  OE2 . GLU   R  4  186 ? 81.707  -213.738 -3.869  1.00 155.87 ? 178 GLU   R OE2 1 
ATOM   31629 N  N   . TRP   R  4  187 ? 81.259  -210.771 0.756   1.00 143.55 ? 179 TRP   R N   1 
ATOM   31630 C  CA  . TRP   R  4  187 ? 81.461  -209.405 1.316   1.00 138.07 ? 179 TRP   R CA  1 
ATOM   31631 C  C   . TRP   R  4  187 ? 82.895  -209.234 1.834   1.00 135.67 ? 179 TRP   R C   1 
ATOM   31632 O  O   . TRP   R  4  187 ? 83.378  -210.122 2.560   1.00 140.29 ? 179 TRP   R O   1 
ATOM   31633 C  CB  . TRP   R  4  187 ? 80.450  -209.070 2.421   1.00 135.53 ? 179 TRP   R CB  1 
ATOM   31634 C  CG  . TRP   R  4  187 ? 80.556  -207.641 2.862   1.00 137.69 ? 179 TRP   R CG  1 
ATOM   31635 C  CD1 . TRP   R  4  187 ? 79.907  -206.570 2.319   1.00 137.02 ? 179 TRP   R CD1 1 
ATOM   31636 C  CD2 . TRP   R  4  187 ? 81.404  -207.109 3.899   1.00 136.89 ? 179 TRP   R CD2 1 
ATOM   31637 N  NE1 . TRP   R  4  187 ? 80.275  -205.416 2.956   1.00 136.33 ? 179 TRP   R NE1 1 
ATOM   31638 C  CE2 . TRP   R  4  187 ? 81.195  -205.713 3.926   1.00 136.20 ? 179 TRP   R CE2 1 
ATOM   31639 C  CE3 . TRP   R  4  187 ? 82.311  -207.670 4.807   1.00 137.06 ? 179 TRP   R CE3 1 
ATOM   31640 C  CZ2 . TRP   R  4  187 ? 81.852  -204.878 4.829   1.00 134.23 ? 179 TRP   R CZ2 1 
ATOM   31641 C  CZ3 . TRP   R  4  187 ? 82.961  -206.843 5.699   1.00 133.71 ? 179 TRP   R CZ3 1 
ATOM   31642 C  CH2 . TRP   R  4  187 ? 82.733  -205.467 5.708   1.00 133.02 ? 179 TRP   R CH2 1 
ATOM   31643 N  N   . HIS   R  4  188 ? 83.526  -208.110 1.482   1.00 133.89 ? 180 HIS   R N   1 
ATOM   31644 C  CA  . HIS   R  4  188 ? 84.771  -207.586 2.106   1.00 137.55 ? 180 HIS   R CA  1 
ATOM   31645 C  C   . HIS   R  4  188 ? 84.643  -206.064 2.267   1.00 135.56 ? 180 HIS   R C   1 
ATOM   31646 O  O   . HIS   R  4  188 ? 83.737  -205.473 1.643   1.00 128.72 ? 180 HIS   R O   1 
ATOM   31647 C  CB  . HIS   R  4  188 ? 86.012  -208.022 1.310   1.00 141.46 ? 180 HIS   R CB  1 
ATOM   31648 C  CG  . HIS   R  4  188 ? 86.043  -207.553 -0.106  1.00 146.06 ? 180 HIS   R CG  1 
ATOM   31649 N  ND1 . HIS   R  4  188 ? 86.755  -206.434 -0.498  1.00 146.00 ? 180 HIS   R ND1 1 
ATOM   31650 C  CD2 . HIS   R  4  188 ? 85.475  -208.052 -1.225  1.00 147.32 ? 180 HIS   R CD2 1 
ATOM   31651 C  CE1 . HIS   R  4  188 ? 86.612  -206.258 -1.796  1.00 149.08 ? 180 HIS   R CE1 1 
ATOM   31652 N  NE2 . HIS   R  4  188 ? 85.832  -207.239 -2.266  1.00 149.58 ? 180 HIS   R NE2 1 
ATOM   31653 N  N   . SER   R  4  189 ? 85.522  -205.459 3.071   1.00 135.37 ? 181 SER   R N   1 
ATOM   31654 C  CA  . SER   R  4  189 ? 85.444  -204.042 3.517   1.00 134.37 ? 181 SER   R CA  1 
ATOM   31655 C  C   . SER   R  4  189 ? 85.855  -203.073 2.398   1.00 136.33 ? 181 SER   R C   1 
ATOM   31656 O  O   . SER   R  4  189 ? 85.823  -201.852 2.653   1.00 133.83 ? 181 SER   R O   1 
ATOM   31657 C  CB  . SER   R  4  189 ? 86.282  -203.833 4.754   1.00 134.83 ? 181 SER   R CB  1 
ATOM   31658 O  OG  . SER   R  4  189 ? 87.646  -204.129 4.498   1.00 137.52 ? 181 SER   R OG  1 
ATOM   31659 N  N   . SER   R  4  190 ? 86.210  -203.579 1.210   1.00 136.70 ? 182 SER   R N   1 
ATOM   31660 C  CA  . SER   R  4  190 ? 86.756  -202.785 0.075   1.00 136.56 ? 182 SER   R CA  1 
ATOM   31661 C  C   . SER   R  4  190 ? 85.910  -202.956 -1.196  1.00 135.59 ? 182 SER   R C   1 
ATOM   31662 O  O   . SER   R  4  190 ? 86.420  -202.610 -2.282  1.00 133.82 ? 182 SER   R O   1 
ATOM   31663 C  CB  . SER   R  4  190 ? 88.193  -203.159 -0.179  1.00 137.84 ? 182 SER   R CB  1 
ATOM   31664 O  OG  . SER   R  4  190 ? 88.943  -203.116 1.025   1.00 137.47 ? 182 SER   R OG  1 
ATOM   31665 N  N   . LEU   R  4  191 ? 84.672  -203.454 -1.082  1.00 135.34 ? 183 LEU   R N   1 
ATOM   31666 C  CA  . LEU   R  4  191 ? 83.729  -203.572 -2.229  1.00 135.56 ? 183 LEU   R CA  1 
ATOM   31667 C  C   . LEU   R  4  191 ? 83.434  -202.171 -2.764  1.00 135.44 ? 183 LEU   R C   1 
ATOM   31668 O  O   . LEU   R  4  191 ? 83.158  -201.284 -1.941  1.00 132.99 ? 183 LEU   R O   1 
ATOM   31669 C  CB  . LEU   R  4  191 ? 82.422  -204.241 -1.791  1.00 136.15 ? 183 LEU   R CB  1 
ATOM   31670 C  CG  . LEU   R  4  191 ? 82.437  -205.764 -1.680  1.00 137.46 ? 183 LEU   R CG  1 
ATOM   31671 C  CD1 . LEU   R  4  191 ? 81.175  -206.251 -0.989  1.00 136.62 ? 183 LEU   R CD1 1 
ATOM   31672 C  CD2 . LEU   R  4  191 ? 82.575  -206.422 -3.046  1.00 139.04 ? 183 LEU   R CD2 1 
ATOM   31673 N  N   . THR   R  4  192 ? 83.480  -201.994 -4.086  1.00 139.34 ? 184 THR   R N   1 
ATOM   31674 C  CA  . THR   R  4  192 ? 83.021  -200.762 -4.782  1.00 143.19 ? 184 THR   R CA  1 
ATOM   31675 C  C   . THR   R  4  192 ? 81.494  -200.836 -4.907  1.00 141.82 ? 184 THR   R C   1 
ATOM   31676 O  O   . THR   R  4  192 ? 80.947  -201.943 -4.721  1.00 138.00 ? 184 THR   R O   1 
ATOM   31677 C  CB  . THR   R  4  192 ? 83.738  -200.586 -6.129  1.00 151.22 ? 184 THR   R CB  1 
ATOM   31678 O  OG1 . THR   R  4  192 ? 83.349  -201.651 -6.998  1.00 150.42 ? 184 THR   R OG1 1 
ATOM   31679 C  CG2 . THR   R  4  192 ? 85.245  -200.569 -5.993  1.00 154.37 ? 184 THR   R CG2 1 
ATOM   31680 N  N   . LEU   R  4  193 ? 80.833  -199.706 -5.181  1.00 145.67 ? 185 LEU   R N   1 
ATOM   31681 C  CA  . LEU   R  4  193 ? 79.355  -199.639 -5.351  1.00 143.54 ? 185 LEU   R CA  1 
ATOM   31682 C  C   . LEU   R  4  193 ? 78.941  -200.568 -6.499  1.00 138.43 ? 185 LEU   R C   1 
ATOM   31683 O  O   . LEU   R  4  193 ? 77.955  -201.302 -6.327  1.00 135.19 ? 185 LEU   R O   1 
ATOM   31684 C  CB  . LEU   R  4  193 ? 78.918  -198.196 -5.625  1.00 147.45 ? 185 LEU   R CB  1 
ATOM   31685 C  CG  . LEU   R  4  193 ? 77.406  -197.963 -5.624  1.00 150.13 ? 185 LEU   R CG  1 
ATOM   31686 C  CD1 . LEU   R  4  193 ? 76.857  -197.961 -4.204  1.00 150.90 ? 185 LEU   R CD1 1 
ATOM   31687 C  CD2 . LEU   R  4  193 ? 77.047  -196.668 -6.336  1.00 150.33 ? 185 LEU   R CD2 1 
ATOM   31688 N  N   . LYS   R  4  194 ? 79.675  -200.528 -7.618  1.00 138.52 ? 186 LYS   R N   1 
ATOM   31689 C  CA  . LYS   R  4  194 ? 79.432  -201.361 -8.830  1.00 142.69 ? 186 LYS   R CA  1 
ATOM   31690 C  C   . LYS   R  4  194 ? 79.564  -202.850 -8.485  1.00 143.33 ? 186 LYS   R C   1 
ATOM   31691 O  O   . LYS   R  4  194 ? 78.750  -203.642 -9.000  1.00 148.79 ? 186 LYS   R O   1 
ATOM   31692 C  CB  . LYS   R  4  194 ? 80.403  -200.985 -9.953  1.00 146.48 ? 186 LYS   R CB  1 
ATOM   31693 C  CG  . LYS   R  4  194 ? 80.041  -199.717 -10.714 1.00 145.81 ? 186 LYS   R CG  1 
ATOM   31694 C  CD  . LYS   R  4  194 ? 81.011  -199.381 -11.825 1.00 148.84 ? 186 LYS   R CD  1 
ATOM   31695 C  CE  . LYS   R  4  194 ? 80.411  -198.481 -12.884 1.00 148.73 ? 186 LYS   R CE  1 
ATOM   31696 N  NZ  . LYS   R  4  194 ? 79.453  -199.213 -13.746 1.00 149.29 ? 186 LYS   R NZ  1 
ATOM   31697 N  N   . GLU   R  4  195 ? 80.558  -203.214 -7.667  1.00 142.73 ? 187 GLU   R N   1 
ATOM   31698 C  CA  . GLU   R  4  195 ? 80.788  -204.612 -7.206  1.00 141.15 ? 187 GLU   R CA  1 
ATOM   31699 C  C   . GLU   R  4  195 ? 79.582  -205.082 -6.383  1.00 136.60 ? 187 GLU   R C   1 
ATOM   31700 O  O   . GLU   R  4  195 ? 79.152  -206.232 -6.588  1.00 134.63 ? 187 GLU   R O   1 
ATOM   31701 C  CB  . GLU   R  4  195 ? 82.088  -204.724 -6.406  1.00 141.03 ? 187 GLU   R CB  1 
ATOM   31702 C  CG  . GLU   R  4  195 ? 83.328  -204.804 -7.279  1.00 142.95 ? 187 GLU   R CG  1 
ATOM   31703 C  CD  . GLU   R  4  195 ? 84.643  -204.753 -6.522  1.00 143.08 ? 187 GLU   R CD  1 
ATOM   31704 O  OE1 . GLU   R  4  195 ? 84.815  -205.556 -5.585  1.00 142.57 ? 187 GLU   R OE1 1 
ATOM   31705 O  OE2 . GLU   R  4  195 ? 85.490  -203.905 -6.866  1.00 143.45 ? 187 GLU   R OE2 1 
ATOM   31706 N  N   . ALA   R  4  196 ? 79.055  -204.223 -5.503  1.00 135.59 ? 188 ALA   R N   1 
ATOM   31707 C  CA  . ALA   R  4  196 ? 77.884  -204.503 -4.637  1.00 134.30 ? 188 ALA   R CA  1 
ATOM   31708 C  C   . ALA   R  4  196 ? 76.632  -204.704 -5.502  1.00 136.89 ? 188 ALA   R C   1 
ATOM   31709 O  O   . ALA   R  4  196 ? 75.910  -205.690 -5.258  1.00 136.68 ? 188 ALA   R O   1 
ATOM   31710 C  CB  . ALA   R  4  196 ? 77.690  -203.391 -3.633  1.00 135.03 ? 188 ALA   R CB  1 
ATOM   31711 N  N   . GLU   R  4  197 ? 76.395  -203.810 -6.472  1.00 137.30 ? 189 GLU   R N   1 
ATOM   31712 C  CA  . GLU   R  4  197 ? 75.229  -203.847 -7.401  1.00 140.74 ? 189 GLU   R CA  1 
ATOM   31713 C  C   . GLU   R  4  197 ? 75.143  -205.230 -8.062  1.00 139.93 ? 189 GLU   R C   1 
ATOM   31714 O  O   . GLU   R  4  197 ? 74.058  -205.849 -8.008  1.00 136.25 ? 189 GLU   R O   1 
ATOM   31715 C  CB  . GLU   R  4  197 ? 75.348  -202.765 -8.479  1.00 144.65 ? 189 GLU   R CB  1 
ATOM   31716 C  CG  . GLU   R  4  197 ? 75.156  -201.347 -7.969  1.00 145.52 ? 189 GLU   R CG  1 
ATOM   31717 C  CD  . GLU   R  4  197 ? 75.556  -200.257 -8.952  1.00 153.22 ? 189 GLU   R CD  1 
ATOM   31718 O  OE1 . GLU   R  4  197 ? 75.355  -199.068 -8.626  1.00 153.72 ? 189 GLU   R OE1 1 
ATOM   31719 O  OE2 . GLU   R  4  197 ? 76.065  -200.596 -10.041 1.00 155.13 ? 189 GLU   R OE2 1 
ATOM   31720 N  N   . LEU   R  4  198 ? 76.250  -205.682 -8.662  1.00 140.53 ? 190 LEU   R N   1 
ATOM   31721 C  CA  . LEU   R  4  198 ? 76.381  -206.990 -9.366  1.00 137.82 ? 190 LEU   R CA  1 
ATOM   31722 C  C   . LEU   R  4  198 ? 76.152  -208.150 -8.386  1.00 136.93 ? 190 LEU   R C   1 
ATOM   31723 O  O   . LEU   R  4  198 ? 75.559  -209.166 -8.803  1.00 137.58 ? 190 LEU   R O   1 
ATOM   31724 C  CB  . LEU   R  4  198 ? 77.775  -207.083 -10.000 1.00 137.80 ? 190 LEU   R CB  1 
ATOM   31725 C  CG  . LEU   R  4  198 ? 77.889  -206.666 -11.469 1.00 134.74 ? 190 LEU   R CG  1 
ATOM   31726 C  CD1 . LEU   R  4  198 ? 77.061  -205.428 -11.782 1.00 132.37 ? 190 LEU   R CD1 1 
ATOM   31727 C  CD2 . LEU   R  4  198 ? 79.344  -206.434 -11.843 1.00 134.76 ? 190 LEU   R CD2 1 
ATOM   31728 N  N   . LEU   R  4  199 ? 76.615  -208.006 -7.141  1.00 133.82 ? 191 LEU   R N   1 
ATOM   31729 C  CA  . LEU   R  4  199 ? 76.565  -209.066 -6.097  1.00 131.29 ? 191 LEU   R CA  1 
ATOM   31730 C  C   . LEU   R  4  199 ? 75.112  -209.300 -5.664  1.00 126.10 ? 191 LEU   R C   1 
ATOM   31731 O  O   . LEU   R  4  199 ? 74.752  -210.467 -5.430  1.00 125.28 ? 191 LEU   R O   1 
ATOM   31732 C  CB  . LEU   R  4  199 ? 77.435  -208.640 -4.909  1.00 135.83 ? 191 LEU   R CB  1 
ATOM   31733 C  CG  . LEU   R  4  199 ? 78.184  -209.759 -4.187  1.00 139.25 ? 191 LEU   R CG  1 
ATOM   31734 C  CD1 . LEU   R  4  199 ? 79.173  -210.452 -5.115  1.00 142.60 ? 191 LEU   R CD1 1 
ATOM   31735 C  CD2 . LEU   R  4  199 ? 78.902  -209.201 -2.968  1.00 140.39 ? 191 LEU   R CD2 1 
ATOM   31736 N  N   . VAL   R  4  200 ? 74.318  -208.231 -5.552  1.00 120.89 ? 192 VAL   R N   1 
ATOM   31737 C  CA  . VAL   R  4  200 ? 72.870  -208.294 -5.187  1.00 119.18 ? 192 VAL   R CA  1 
ATOM   31738 C  C   . VAL   R  4  200 ? 72.111  -209.005 -6.314  1.00 119.63 ? 192 VAL   R C   1 
ATOM   31739 O  O   . VAL   R  4  200 ? 71.289  -209.882 -6.000  1.00 118.60 ? 192 VAL   R O   1 
ATOM   31740 C  CB  . VAL   R  4  200 ? 72.292  -206.893 -4.908  1.00 117.07 ? 192 VAL   R CB  1 
ATOM   31741 C  CG1 . VAL   R  4  200 ? 70.778  -206.917 -4.764  1.00 116.10 ? 192 VAL   R CG1 1 
ATOM   31742 C  CG2 . VAL   R  4  200 ? 72.926  -206.260 -3.680  1.00 115.47 ? 192 VAL   R CG2 1 
ATOM   31743 N  N   . LEU   R  4  201 ? 72.376  -208.623 -7.569  1.00 124.71 ? 193 LEU   R N   1 
ATOM   31744 C  CA  . LEU   R  4  201 ? 71.781  -209.235 -8.792  1.00 129.68 ? 193 LEU   R CA  1 
ATOM   31745 C  C   . LEU   R  4  201 ? 72.129  -210.729 -8.844  1.00 133.89 ? 193 LEU   R C   1 
ATOM   31746 O  O   . LEU   R  4  201 ? 71.206  -211.538 -9.070  1.00 142.20 ? 193 LEU   R O   1 
ATOM   31747 C  CB  . LEU   R  4  201 ? 72.315  -208.515 -10.039 1.00 129.55 ? 193 LEU   R CB  1 
ATOM   31748 C  CG  . LEU   R  4  201 ? 71.375  -207.536 -10.750 1.00 126.02 ? 193 LEU   R CG  1 
ATOM   31749 C  CD1 . LEU   R  4  201 ? 70.306  -206.963 -9.828  1.00 122.82 ? 193 LEU   R CD1 1 
ATOM   31750 C  CD2 . LEU   R  4  201 ? 72.173  -206.413 -11.396 1.00 124.43 ? 193 LEU   R CD2 1 
ATOM   31751 N  N   . LYS   R  4  202 ? 73.410  -211.066 -8.654  1.00 139.57 ? 194 LYS   R N   1 
ATOM   31752 C  CA  . LYS   R  4  202 ? 73.943  -212.456 -8.706  1.00 139.63 ? 194 LYS   R CA  1 
ATOM   31753 C  C   . LYS   R  4  202 ? 73.207  -213.329 -7.681  1.00 136.75 ? 194 LYS   R C   1 
ATOM   31754 O  O   . LYS   R  4  202 ? 72.729  -214.412 -8.070  1.00 139.70 ? 194 LYS   R O   1 
ATOM   31755 C  CB  . LYS   R  4  202 ? 75.454  -212.464 -8.445  1.00 145.66 ? 194 LYS   R CB  1 
ATOM   31756 C  CG  . LYS   R  4  202 ? 76.098  -213.843 -8.355  1.00 148.24 ? 194 LYS   R CG  1 
ATOM   31757 C  CD  . LYS   R  4  202 ? 77.608  -213.798 -8.239  1.00 151.75 ? 194 LYS   R CD  1 
ATOM   31758 C  CE  . LYS   R  4  202 ? 78.236  -215.160 -8.029  1.00 152.00 ? 194 LYS   R CE  1 
ATOM   31759 N  NZ  . LYS   R  4  202 ? 78.115  -215.612 -6.623  1.00 152.02 ? 194 LYS   R NZ  1 
ATOM   31760 N  N   . ILE   R  4  203 ? 73.123  -212.873 -6.427  1.00 130.47 ? 195 ILE   R N   1 
ATOM   31761 C  CA  . ILE   R  4  203 ? 72.563  -213.658 -5.286  1.00 127.06 ? 195 ILE   R CA  1 
ATOM   31762 C  C   . ILE   R  4  203 ? 71.032  -213.705 -5.398  1.00 124.15 ? 195 ILE   R C   1 
ATOM   31763 O  O   . ILE   R  4  203 ? 70.459  -214.740 -5.010  1.00 125.56 ? 195 ILE   R O   1 
ATOM   31764 C  CB  . ILE   R  4  203 ? 73.048  -213.108 -3.928  1.00 124.78 ? 195 ILE   R CB  1 
ATOM   31765 C  CG1 . ILE   R  4  203 ? 74.572  -213.201 -3.808  1.00 128.28 ? 195 ILE   R CG1 1 
ATOM   31766 C  CG2 . ILE   R  4  203 ? 72.354  -213.822 -2.775  1.00 122.26 ? 195 ILE   R CG2 1 
ATOM   31767 C  CD1 . ILE   R  4  203 ? 75.149  -212.528 -2.582  1.00 129.16 ? 195 ILE   R CD1 1 
ATOM   31768 N  N   . LEU   R  4  204 ? 70.388  -212.647 -5.904  1.00 122.71 ? 196 LEU   R N   1 
ATOM   31769 C  CA  . LEU   R  4  204 ? 68.919  -212.645 -6.159  1.00 125.44 ? 196 LEU   R CA  1 
ATOM   31770 C  C   . LEU   R  4  204 ? 68.590  -213.703 -7.219  1.00 126.01 ? 196 LEU   R C   1 
ATOM   31771 O  O   . LEU   R  4  204 ? 67.636  -214.474 -6.997  1.00 129.69 ? 196 LEU   R O   1 
ATOM   31772 C  CB  . LEU   R  4  204 ? 68.440  -211.258 -6.608  1.00 125.17 ? 196 LEU   R CB  1 
ATOM   31773 C  CG  . LEU   R  4  204 ? 68.058  -210.281 -5.494  1.00 125.80 ? 196 LEU   R CG  1 
ATOM   31774 C  CD1 . LEU   R  4  204 ? 67.709  -208.918 -6.071  1.00 125.94 ? 196 LEU   R CD1 1 
ATOM   31775 C  CD2 . LEU   R  4  204 ? 66.899  -210.807 -4.656  1.00 125.33 ? 196 LEU   R CD2 1 
ATOM   31776 N  N   . LYS   R  4  205 ? 69.359  -213.745 -8.314  1.00 127.35 ? 197 LYS   R N   1 
ATOM   31777 C  CA  . LYS   R  4  205 ? 69.167  -214.704 -9.438  1.00 130.55 ? 197 LYS   R CA  1 
ATOM   31778 C  C   . LYS   R  4  205 ? 69.264  -216.141 -8.909  1.00 128.09 ? 197 LYS   R C   1 
ATOM   31779 O  O   . LYS   R  4  205 ? 68.519  -217.001 -9.416  1.00 130.72 ? 197 LYS   R O   1 
ATOM   31780 C  CB  . LYS   R  4  205 ? 70.194  -214.473 -10.552 1.00 133.67 ? 197 LYS   R CB  1 
ATOM   31781 C  CG  . LYS   R  4  205 ? 69.903  -215.220 -11.849 1.00 135.53 ? 197 LYS   R CG  1 
ATOM   31782 C  CD  . LYS   R  4  205 ? 70.649  -214.696 -13.065 1.00 137.63 ? 197 LYS   R CD  1 
ATOM   31783 C  CE  . LYS   R  4  205 ? 71.909  -215.468 -13.396 1.00 139.62 ? 197 LYS   R CE  1 
ATOM   31784 N  NZ  . LYS   R  4  205 ? 73.028  -215.127 -12.486 1.00 138.45 ? 197 LYS   R NZ  1 
ATOM   31785 N  N   . GLN   R  4  206 ? 70.143  -216.380 -7.929  1.00 127.64 ? 198 GLN   R N   1 
ATOM   31786 C  CA  . GLN   R  4  206 ? 70.394  -217.715 -7.320  1.00 128.32 ? 198 GLN   R CA  1 
ATOM   31787 C  C   . GLN   R  4  206 ? 69.161  -218.196 -6.545  1.00 130.30 ? 198 GLN   R C   1 
ATOM   31788 O  O   . GLN   R  4  206 ? 68.815  -219.379 -6.697  1.00 130.82 ? 198 GLN   R O   1 
ATOM   31789 C  CB  . GLN   R  4  206 ? 71.607  -217.683 -6.386  1.00 132.07 ? 198 GLN   R CB  1 
ATOM   31790 C  CG  . GLN   R  4  206 ? 72.942  -217.825 -7.104  1.00 135.99 ? 198 GLN   R CG  1 
ATOM   31791 C  CD  . GLN   R  4  206 ? 74.128  -217.723 -6.173  1.00 139.23 ? 198 GLN   R CD  1 
ATOM   31792 O  OE1 . GLN   R  4  206 ? 75.161  -217.154 -6.519  1.00 140.11 ? 198 GLN   R OE1 1 
ATOM   31793 N  NE2 . GLN   R  4  206 ? 73.998  -218.281 -4.979  1.00 139.09 ? 198 GLN   R NE2 1 
ATOM   31794 N  N   . VAL   R  4  207 ? 68.531  -217.331 -5.741  1.00 125.39 ? 199 VAL   R N   1 
ATOM   31795 C  CA  . VAL   R  4  207 ? 67.466  -217.729 -4.765  1.00 124.32 ? 199 VAL   R CA  1 
ATOM   31796 C  C   . VAL   R  4  207 ? 66.062  -217.488 -5.339  1.00 124.42 ? 199 VAL   R C   1 
ATOM   31797 O  O   . VAL   R  4  207 ? 65.098  -217.988 -4.727  1.00 125.24 ? 199 VAL   R O   1 
ATOM   31798 C  CB  . VAL   R  4  207 ? 67.618  -217.011 -3.411  1.00 121.94 ? 199 VAL   R CB  1 
ATOM   31799 C  CG1 . VAL   R  4  207 ? 68.968  -217.291 -2.769  1.00 123.51 ? 199 VAL   R CG1 1 
ATOM   31800 C  CG2 . VAL   R  4  207 ? 67.368  -215.516 -3.522  1.00 118.59 ? 199 VAL   R CG2 1 
ATOM   31801 N  N   . MET   R  4  208 ? 65.933  -216.738 -6.436  1.00 126.42 ? 200 MET   R N   1 
ATOM   31802 C  CA  . MET   R  4  208 ? 64.621  -216.447 -7.079  1.00 133.99 ? 200 MET   R CA  1 
ATOM   31803 C  C   . MET   R  4  208 ? 64.099  -217.697 -7.792  1.00 137.98 ? 200 MET   R C   1 
ATOM   31804 O  O   . MET   R  4  208 ? 64.925  -218.444 -8.329  1.00 146.64 ? 200 MET   R O   1 
ATOM   31805 C  CB  . MET   R  4  208 ? 64.741  -215.319 -8.106  1.00 135.81 ? 200 MET   R CB  1 
ATOM   31806 C  CG  . MET   R  4  208 ? 64.545  -213.947 -7.503  1.00 137.48 ? 200 MET   R CG  1 
ATOM   31807 S  SD  . MET   R  4  208 ? 64.683  -212.620 -8.722  1.00 140.54 ? 200 MET   R SD  1 
ATOM   31808 C  CE  . MET   R  4  208 ? 63.239  -212.938 -9.733  1.00 140.98 ? 200 MET   R CE  1 
ATOM   31809 N  N   . GLU   R  4  209 ? 62.775  -217.888 -7.817  1.00 143.94 ? 201 GLU   R N   1 
ATOM   31810 C  CA  . GLU   R  4  209 ? 62.112  -219.022 -8.520  1.00 147.81 ? 201 GLU   R CA  1 
ATOM   31811 C  C   . GLU   R  4  209 ? 62.208  -218.792 -10.033 1.00 149.96 ? 201 GLU   R C   1 
ATOM   31812 O  O   . GLU   R  4  209 ? 62.964  -219.530 -10.695 1.00 155.75 ? 201 GLU   R O   1 
ATOM   31813 C  CB  . GLU   R  4  209 ? 60.656  -219.174 -8.070  1.00 152.73 ? 201 GLU   R CB  1 
ATOM   31814 C  CG  . GLU   R  4  209 ? 60.493  -219.974 -6.789  1.00 151.72 ? 201 GLU   R CG  1 
ATOM   31815 C  CD  . GLU   R  4  209 ? 60.821  -221.452 -6.919  1.00 153.99 ? 201 GLU   R CD  1 
ATOM   31816 O  OE1 . GLU   R  4  209 ? 60.311  -222.088 -7.863  1.00 151.43 ? 201 GLU   R OE1 1 
ATOM   31817 O  OE2 . GLU   R  4  209 ? 61.589  -221.964 -6.080  1.00 157.29 ? 201 GLU   R OE2 1 
ATOM   31818 N  N   . GLU   R  4  210 ? 61.477  -217.799 -10.548 1.00 147.51 ? 202 GLU   R N   1 
ATOM   31819 C  CA  . GLU   R  4  210 ? 61.476  -217.418 -11.989 1.00 145.08 ? 202 GLU   R CA  1 
ATOM   31820 C  C   . GLU   R  4  210 ? 62.808  -216.740 -12.337 1.00 138.35 ? 202 GLU   R C   1 
ATOM   31821 O  O   . GLU   R  4  210 ? 63.444  -216.173 -11.426 1.00 134.75 ? 202 GLU   R O   1 
ATOM   31822 C  CB  . GLU   R  4  210 ? 60.292  -216.512 -12.334 1.00 147.34 ? 202 GLU   R CB  1 
ATOM   31823 C  CG  . GLU   R  4  210 ? 59.972  -215.470 -11.273 1.00 148.86 ? 202 GLU   R CG  1 
ATOM   31824 C  CD  . GLU   R  4  210 ? 59.131  -214.293 -11.739 1.00 152.23 ? 202 GLU   R CD  1 
ATOM   31825 O  OE1 . GLU   R  4  210 ? 58.866  -213.395 -10.909 1.00 146.66 ? 202 GLU   R OE1 1 
ATOM   31826 O  OE2 . GLU   R  4  210 ? 58.742  -214.271 -12.926 1.00 159.50 ? 202 GLU   R OE2 1 
ATOM   31827 N  N   . LYS   R  4  211 ? 63.203  -216.806 -13.612 1.00 138.10 ? 203 LYS   R N   1 
ATOM   31828 C  CA  . LYS   R  4  211 ? 64.507  -216.303 -14.122 1.00 139.04 ? 203 LYS   R CA  1 
ATOM   31829 C  C   . LYS   R  4  211 ? 64.554  -214.783 -13.951 1.00 140.33 ? 203 LYS   R C   1 
ATOM   31830 O  O   . LYS   R  4  211 ? 63.609  -214.115 -14.409 1.00 140.36 ? 203 LYS   R O   1 
ATOM   31831 C  CB  . LYS   R  4  211 ? 64.702  -216.680 -15.593 1.00 138.87 ? 203 LYS   R CB  1 
ATOM   31832 C  CG  . LYS   R  4  211 ? 66.078  -216.349 -16.155 1.00 142.82 ? 203 LYS   R CG  1 
ATOM   31833 C  CD  . LYS   R  4  211 ? 66.117  -216.232 -17.661 1.00 145.87 ? 203 LYS   R CD  1 
ATOM   31834 C  CE  . LYS   R  4  211 ? 67.353  -215.504 -18.146 1.00 150.57 ? 203 LYS   R CE  1 
ATOM   31835 N  NZ  . LYS   R  4  211 ? 67.371  -215.373 -19.622 1.00 153.32 ? 203 LYS   R NZ  1 
ATOM   31836 N  N   . LEU   R  4  212 ? 65.621  -214.269 -13.330 1.00 143.91 ? 204 LEU   R N   1 
ATOM   31837 C  CA  . LEU   R  4  212 ? 65.790  -212.827 -13.000 1.00 145.59 ? 204 LEU   R CA  1 
ATOM   31838 C  C   . LEU   R  4  212 ? 65.914  -212.004 -14.289 1.00 146.82 ? 204 LEU   R C   1 
ATOM   31839 O  O   . LEU   R  4  212 ? 66.668  -212.423 -15.190 1.00 149.46 ? 204 LEU   R O   1 
ATOM   31840 C  CB  . LEU   R  4  212 ? 67.027  -212.646 -12.112 1.00 146.36 ? 204 LEU   R CB  1 
ATOM   31841 C  CG  . LEU   R  4  212 ? 67.330  -211.206 -11.688 1.00 143.92 ? 204 LEU   R CG  1 
ATOM   31842 C  CD1 . LEU   R  4  212 ? 67.815  -211.144 -10.248 1.00 143.04 ? 204 LEU   R CD1 1 
ATOM   31843 C  CD2 . LEU   R  4  212 ? 68.348  -210.556 -12.614 1.00 143.06 ? 204 LEU   R CD2 1 
ATOM   31844 N  N   . ASP   R  4  213 ? 65.197  -210.875 -14.353 1.00 146.96 ? 205 ASP   R N   1 
ATOM   31845 C  CA  . ASP   R  4  213 ? 65.329  -209.830 -15.406 1.00 143.68 ? 205 ASP   R CA  1 
ATOM   31846 C  C   . ASP   R  4  213 ? 65.021  -208.461 -14.780 1.00 143.37 ? 205 ASP   R C   1 
ATOM   31847 O  O   . ASP   R  4  213 ? 64.872  -208.399 -13.541 1.00 143.01 ? 205 ASP   R O   1 
ATOM   31848 C  CB  . ASP   R  4  213 ? 64.457  -210.152 -16.625 1.00 145.14 ? 205 ASP   R CB  1 
ATOM   31849 C  CG  . ASP   R  4  213 ? 62.958  -210.159 -16.370 1.00 143.45 ? 205 ASP   R CG  1 
ATOM   31850 O  OD1 . ASP   R  4  213 ? 62.524  -209.583 -15.353 1.00 140.99 ? 205 ASP   R OD1 1 
ATOM   31851 O  OD2 . ASP   R  4  213 ? 62.232  -210.736 -17.201 1.00 146.62 ? 205 ASP   R OD2 1 
ATOM   31852 N  N   . GLU   R  4  214 ? 64.923  -207.409 -15.601 1.00 139.17 ? 206 GLU   R N   1 
ATOM   31853 C  CA  . GLU   R  4  214 ? 64.727  -206.004 -15.142 1.00 136.17 ? 206 GLU   R CA  1 
ATOM   31854 C  C   . GLU   R  4  214 ? 63.279  -205.767 -14.686 1.00 132.88 ? 206 GLU   R C   1 
ATOM   31855 O  O   . GLU   R  4  214 ? 63.036  -204.704 -14.082 1.00 135.43 ? 206 GLU   R O   1 
ATOM   31856 C  CB  . GLU   R  4  214 ? 65.119  -205.006 -16.238 1.00 132.50 ? 206 GLU   R CB  1 
ATOM   31857 C  CG  . GLU   R  4  214 ? 64.214  -205.012 -17.463 1.00 131.42 ? 206 GLU   R CG  1 
ATOM   31858 C  CD  . GLU   R  4  214 ? 64.706  -205.832 -18.642 1.00 132.66 ? 206 GLU   R CD  1 
ATOM   31859 O  OE1 . GLU   R  4  214 ? 64.371  -205.469 -19.786 1.00 131.82 ? 206 GLU   R OE1 1 
ATOM   31860 O  OE2 . GLU   R  4  214 ? 65.416  -206.832 -18.416 1.00 132.91 ? 206 GLU   R OE2 1 
ATOM   31861 N  N   . ASN   R  4  215 ? 62.357  -206.699 -14.960 1.00 131.53 ? 207 ASN   R N   1 
ATOM   31862 C  CA  . ASN   R  4  215 ? 60.898  -206.539 -14.705 1.00 126.60 ? 207 ASN   R CA  1 
ATOM   31863 C  C   . ASN   R  4  215 ? 60.473  -207.220 -13.397 1.00 123.78 ? 207 ASN   R C   1 
ATOM   31864 O  O   . ASN   R  4  215 ? 59.444  -206.791 -12.844 1.00 122.22 ? 207 ASN   R O   1 
ATOM   31865 C  CB  . ASN   R  4  215 ? 60.055  -207.080 -15.862 1.00 128.62 ? 207 ASN   R CB  1 
ATOM   31866 C  CG  . ASN   R  4  215 ? 59.985  -206.130 -17.039 1.00 131.11 ? 207 ASN   R CG  1 
ATOM   31867 O  OD1 . ASN   R  4  215 ? 60.673  -205.112 -17.070 1.00 131.23 ? 207 ASN   R OD1 1 
ATOM   31868 N  ND2 . ASN   R  4  215 ? 59.153  -206.455 -18.014 1.00 134.22 ? 207 ASN   R ND2 1 
ATOM   31869 N  N   . ASN   R  4  216 ? 61.201  -208.242 -12.930 1.00 123.34 ? 208 ASN   R N   1 
ATOM   31870 C  CA  . ASN   R  4  216 ? 60.829  -209.037 -11.726 1.00 126.40 ? 208 ASN   R CA  1 
ATOM   31871 C  C   . ASN   R  4  216 ? 61.848  -208.833 -10.596 1.00 125.42 ? 208 ASN   R C   1 
ATOM   31872 O  O   . ASN   R  4  216 ? 61.684  -209.489 -9.546  1.00 127.50 ? 208 ASN   R O   1 
ATOM   31873 C  CB  . ASN   R  4  216 ? 60.663  -210.524 -12.054 1.00 129.59 ? 208 ASN   R CB  1 
ATOM   31874 C  CG  . ASN   R  4  216 ? 61.916  -211.168 -12.610 1.00 133.76 ? 208 ASN   R CG  1 
ATOM   31875 O  OD1 . ASN   R  4  216 ? 63.005  -210.603 -12.533 1.00 137.82 ? 208 ASN   R OD1 1 
ATOM   31876 N  ND2 . ASN   R  4  216 ? 61.772  -212.356 -13.174 1.00 136.93 ? 208 ASN   R ND2 1 
ATOM   31877 N  N   . ALA   R  4  217 ? 62.856  -207.976 -10.799 1.00 127.02 ? 209 ALA   R N   1 
ATOM   31878 C  CA  . ALA   R  4  217 ? 63.821  -207.537 -9.762  1.00 124.82 ? 209 ALA   R CA  1 
ATOM   31879 C  C   . ALA   R  4  217 ? 64.063  -206.031 -9.898  1.00 123.53 ? 209 ALA   R C   1 
ATOM   31880 O  O   . ALA   R  4  217 ? 63.994  -205.522 -11.034 1.00 120.29 ? 209 ALA   R O   1 
ATOM   31881 C  CB  . ALA   R  4  217 ? 65.110  -208.313 -9.875  1.00 129.39 ? 209 ALA   R CB  1 
ATOM   31882 N  N   . GLN   R  4  218 ? 64.334  -205.359 -8.776  1.00 120.54 ? 210 GLN   R N   1 
ATOM   31883 C  CA  . GLN   R  4  218 ? 64.551  -203.889 -8.699  1.00 118.58 ? 210 GLN   R CA  1 
ATOM   31884 C  C   . GLN   R  4  218 ? 65.795  -203.597 -7.856  1.00 113.97 ? 210 GLN   R C   1 
ATOM   31885 O  O   . GLN   R  4  218 ? 65.929  -204.201 -6.777  1.00 113.93 ? 210 GLN   R O   1 
ATOM   31886 C  CB  . GLN   R  4  218 ? 63.333  -203.199 -8.085  1.00 115.79 ? 210 GLN   R CB  1 
ATOM   31887 C  CG  . GLN   R  4  218 ? 63.371  -201.684 -8.212  1.00 113.29 ? 210 GLN   R CG  1 
ATOM   31888 C  CD  . GLN   R  4  218 ? 62.038  -201.051 -7.900  1.00 112.24 ? 210 GLN   R CD  1 
ATOM   31889 O  OE1 . GLN   R  4  218 ? 61.356  -200.536 -8.783  1.00 110.35 ? 210 GLN   R OE1 1 
ATOM   31890 N  NE2 . GLN   R  4  218 ? 61.646  -201.096 -6.638  1.00 112.71 ? 210 GLN   R NE2 1 
ATOM   31891 N  N   . LEU   R  4  219 ? 66.657  -202.696 -8.332  1.00 116.06 ? 211 LEU   R N   1 
ATOM   31892 C  CA  . LEU   R  4  219 ? 67.843  -202.203 -7.583  1.00 120.94 ? 211 LEU   R CA  1 
ATOM   31893 C  C   . LEU   R  4  219 ? 67.603  -200.759 -7.134  1.00 123.42 ? 211 LEU   R C   1 
ATOM   31894 O  O   . LEU   R  4  219 ? 66.812  -200.041 -7.782  1.00 124.01 ? 211 LEU   R O   1 
ATOM   31895 C  CB  . LEU   R  4  219 ? 69.091  -202.282 -8.466  1.00 122.32 ? 211 LEU   R CB  1 
ATOM   31896 C  CG  . LEU   R  4  219 ? 69.806  -203.629 -8.516  1.00 123.86 ? 211 LEU   R CG  1 
ATOM   31897 C  CD1 . LEU   R  4  219 ? 71.038  -203.528 -9.399  1.00 128.45 ? 211 LEU   R CD1 1 
ATOM   31898 C  CD2 . LEU   R  4  219 ? 70.192  -204.112 -7.124  1.00 124.67 ? 211 LEU   R CD2 1 
ATOM   31899 N  N   . SER   R  4  220 ? 68.287  -200.367 -6.060  1.00 127.99 ? 212 SER   R N   1 
ATOM   31900 C  CA  . SER   R  4  220 ? 68.335  -198.986 -5.521  1.00 129.07 ? 212 SER   R CA  1 
ATOM   31901 C  C   . SER   R  4  220 ? 69.652  -198.807 -4.766  1.00 132.68 ? 212 SER   R C   1 
ATOM   31902 O  O   . SER   R  4  220 ? 70.299  -199.828 -4.457  1.00 133.36 ? 212 SER   R O   1 
ATOM   31903 C  CB  . SER   R  4  220 ? 67.151  -198.703 -4.636  1.00 129.88 ? 212 SER   R CB  1 
ATOM   31904 O  OG  . SER   R  4  220 ? 67.331  -199.276 -3.349  1.00 129.42 ? 212 SER   R OG  1 
ATOM   31905 N  N   . CYS   R  4  221 ? 70.030  -197.561 -4.488  1.00 136.14 ? 213 CYS   R N   1 
ATOM   31906 C  CA  . CYS   R  4  221 ? 71.224  -197.220 -3.675  1.00 134.13 ? 213 CYS   R CA  1 
ATOM   31907 C  C   . CYS   R  4  221 ? 71.030  -195.856 -3.012  1.00 134.99 ? 213 CYS   R C   1 
ATOM   31908 O  O   . CYS   R  4  221 ? 70.220  -195.053 -3.517  1.00 138.61 ? 213 CYS   R O   1 
ATOM   31909 C  CB  . CYS   R  4  221 ? 72.489  -197.210 -4.524  1.00 133.62 ? 213 CYS   R CB  1 
ATOM   31910 S  SG  . CYS   R  4  221 ? 72.635  -195.749 -5.584  1.00 130.84 ? 213 CYS   R SG  1 
ATOM   31911 N  N   . ILE   R  4  222 ? 71.759  -195.627 -1.919  1.00 136.44 ? 214 ILE   R N   1 
ATOM   31912 C  CA  . ILE   R  4  222 ? 71.866  -194.311 -1.225  1.00 131.97 ? 214 ILE   R CA  1 
ATOM   31913 C  C   . ILE   R  4  222 ? 73.353  -193.943 -1.180  1.00 132.00 ? 214 ILE   R C   1 
ATOM   31914 O  O   . ILE   R  4  222 ? 74.158  -194.767 -0.691  1.00 127.75 ? 214 ILE   R O   1 
ATOM   31915 C  CB  . ILE   R  4  222 ? 71.183  -194.330 0.164   1.00 133.27 ? 214 ILE   R CB  1 
ATOM   31916 C  CG1 . ILE   R  4  222 ? 71.987  -193.578 1.231   1.00 132.69 ? 214 ILE   R CG1 1 
ATOM   31917 C  CG2 . ILE   R  4  222 ? 70.857  -195.748 0.615   1.00 133.54 ? 214 ILE   R CG2 1 
ATOM   31918 C  CD1 . ILE   R  4  222 ? 71.892  -192.074 1.134   1.00 134.24 ? 214 ILE   R CD1 1 
ATOM   31919 N  N   . THR   R  4  223 ? 73.692  -192.772 -1.725  1.00 127.26 ? 215 THR   R N   1 
ATOM   31920 C  CA  . THR   R  4  223 ? 75.051  -192.171 -1.712  1.00 127.45 ? 215 THR   R CA  1 
ATOM   31921 C  C   . THR   R  4  223 ? 74.963  -190.782 -1.076  1.00 127.83 ? 215 THR   R C   1 
ATOM   31922 O  O   . THR   R  4  223 ? 73.937  -190.106 -1.289  1.00 124.69 ? 215 THR   R O   1 
ATOM   31923 C  CB  . THR   R  4  223 ? 75.648  -192.100 -3.124  1.00 127.13 ? 215 THR   R CB  1 
ATOM   31924 O  OG1 . THR   R  4  223 ? 74.878  -191.190 -3.910  1.00 126.52 ? 215 THR   R OG1 1 
ATOM   31925 C  CG2 . THR   R  4  223 ? 75.687  -193.449 -3.807  1.00 126.94 ? 215 THR   R CG2 1 
ATOM   31926 N  N   . LYS   R  4  224 ? 75.996  -190.381 -0.329  1.00 132.02 ? 216 LYS   R N   1 
ATOM   31927 C  CA  . LYS   R  4  224 ? 76.076  -189.051 0.332   1.00 131.69 ? 216 LYS   R CA  1 
ATOM   31928 C  C   . LYS   R  4  224 ? 75.727  -187.966 -0.692  1.00 136.60 ? 216 LYS   R C   1 
ATOM   31929 O  O   . LYS   R  4  224 ? 74.908  -187.086 -0.362  1.00 138.04 ? 216 LYS   R O   1 
ATOM   31930 C  CB  . LYS   R  4  224 ? 77.469  -188.806 0.924   1.00 132.33 ? 216 LYS   R CB  1 
ATOM   31931 C  CG  . LYS   R  4  224 ? 77.778  -187.346 1.227   1.00 129.64 ? 216 LYS   R CG  1 
ATOM   31932 C  CD  . LYS   R  4  224 ? 78.957  -187.123 2.142   1.00 131.71 ? 216 LYS   R CD  1 
ATOM   31933 C  CE  . LYS   R  4  224 ? 79.086  -185.671 2.549   1.00 131.63 ? 216 LYS   R CE  1 
ATOM   31934 N  NZ  . LYS   R  4  224 ? 80.082  -185.485 3.629   1.00 134.14 ? 216 LYS   R NZ  1 
ATOM   31935 N  N   . GLN   R  4  225 ? 76.315  -188.046 -1.890  1.00 139.42 ? 217 GLN   R N   1 
ATOM   31936 C  CA  . GLN   R  4  225 ? 76.279  -186.969 -2.914  1.00 142.09 ? 217 GLN   R CA  1 
ATOM   31937 C  C   . GLN   R  4  225 ? 74.866  -186.835 -3.499  1.00 138.57 ? 217 GLN   R C   1 
ATOM   31938 O  O   . GLN   R  4  225 ? 74.328  -185.712 -3.468  1.00 145.66 ? 217 GLN   R O   1 
ATOM   31939 C  CB  . GLN   R  4  225 ? 77.305  -187.238 -4.017  1.00 146.77 ? 217 GLN   R CB  1 
ATOM   31940 C  CG  . GLN   R  4  225 ? 77.769  -185.973 -4.724  1.00 149.58 ? 217 GLN   R CG  1 
ATOM   31941 C  CD  . GLN   R  4  225 ? 78.287  -186.253 -6.114  1.00 154.74 ? 217 GLN   R CD  1 
ATOM   31942 O  OE1 . GLN   R  4  225 ? 77.537  -186.643 -7.006  1.00 157.66 ? 217 GLN   R OE1 1 
ATOM   31943 N  NE2 . GLN   R  4  225 ? 79.581  -186.054 -6.313  1.00 160.78 ? 217 GLN   R NE2 1 
ATOM   31944 N  N   . ASP   R  4  226 ? 74.291  -187.929 -4.009  1.00 137.56 ? 218 ASP   R N   1 
ATOM   31945 C  CA  . ASP   R  4  226 ? 73.040  -187.912 -4.818  1.00 134.59 ? 218 ASP   R CA  1 
ATOM   31946 C  C   . ASP   R  4  226 ? 71.840  -188.408 -4.001  1.00 130.96 ? 218 ASP   R C   1 
ATOM   31947 O  O   . ASP   R  4  226 ? 70.714  -188.350 -4.535  1.00 128.67 ? 218 ASP   R O   1 
ATOM   31948 C  CB  . ASP   R  4  226 ? 73.211  -188.743 -6.089  1.00 137.57 ? 218 ASP   R CB  1 
ATOM   31949 C  CG  . ASP   R  4  226 ? 74.384  -188.287 -6.938  1.00 140.03 ? 218 ASP   R CG  1 
ATOM   31950 O  OD1 . ASP   R  4  226 ? 74.519  -187.063 -7.137  1.00 139.18 ? 218 ASP   R OD1 1 
ATOM   31951 O  OD2 . ASP   R  4  226 ? 75.162  -189.156 -7.376  1.00 147.71 ? 218 ASP   R OD2 1 
ATOM   31952 N  N   . GLY   R  4  227 ? 72.060  -188.875 -2.767  1.00 128.97 ? 219 GLY   R N   1 
ATOM   31953 C  CA  . GLY   R  4  227 ? 70.996  -189.379 -1.876  1.00 125.71 ? 219 GLY   R CA  1 
ATOM   31954 C  C   . GLY   R  4  227 ? 70.442  -190.711 -2.351  1.00 122.17 ? 219 GLY   R C   1 
ATOM   31955 O  O   . GLY   R  4  227 ? 71.150  -191.417 -3.098  1.00 123.50 ? 219 GLY   R O   1 
ATOM   31956 N  N   . PHE   R  4  228 ? 69.213  -191.038 -1.938  1.00 118.48 ? 220 PHE   R N   1 
ATOM   31957 C  CA  . PHE   R  4  228 ? 68.517  -192.315 -2.246  1.00 119.70 ? 220 PHE   R CA  1 
ATOM   31958 C  C   . PHE   R  4  228 ? 67.900  -192.246 -3.648  1.00 120.21 ? 220 PHE   R C   1 
ATOM   31959 O  O   . PHE   R  4  228 ? 67.163  -191.283 -3.930  1.00 122.87 ? 220 PHE   R O   1 
ATOM   31960 C  CB  . PHE   R  4  228 ? 67.446  -192.614 -1.195  1.00 119.76 ? 220 PHE   R CB  1 
ATOM   31961 C  CG  . PHE   R  4  228 ? 66.577  -193.802 -1.518  1.00 124.10 ? 220 PHE   R CG  1 
ATOM   31962 C  CD1 . PHE   R  4  228 ? 67.048  -195.094 -1.333  1.00 126.51 ? 220 PHE   R CD1 1 
ATOM   31963 C  CD2 . PHE   R  4  228 ? 65.297  -193.629 -2.021  1.00 123.11 ? 220 PHE   R CD2 1 
ATOM   31964 C  CE1 . PHE   R  4  228 ? 66.250  -196.188 -1.636  1.00 128.44 ? 220 PHE   R CE1 1 
ATOM   31965 C  CE2 . PHE   R  4  228 ? 64.501  -194.722 -2.322  1.00 127.12 ? 220 PHE   R CE2 1 
ATOM   31966 C  CZ  . PHE   R  4  228 ? 64.979  -195.999 -2.129  1.00 130.19 ? 220 PHE   R CZ  1 
ATOM   31967 N  N   . LYS   R  4  229 ? 68.178  -193.256 -4.479  1.00 120.15 ? 221 LYS   R N   1 
ATOM   31968 C  CA  . LYS   R  4  229 ? 67.722  -193.356 -5.892  1.00 122.81 ? 221 LYS   R CA  1 
ATOM   31969 C  C   . LYS   R  4  229 ? 67.296  -194.797 -6.195  1.00 121.98 ? 221 LYS   R C   1 
ATOM   31970 O  O   . LYS   R  4  229 ? 68.129  -195.705 -6.010  1.00 120.00 ? 221 LYS   R O   1 
ATOM   31971 C  CB  . LYS   R  4  229 ? 68.849  -192.944 -6.845  1.00 127.03 ? 221 LYS   R CB  1 
ATOM   31972 C  CG  . LYS   R  4  229 ? 69.036  -191.444 -7.035  1.00 129.67 ? 221 LYS   R CG  1 
ATOM   31973 C  CD  . LYS   R  4  229 ? 68.083  -190.833 -8.047  1.00 131.77 ? 221 LYS   R CD  1 
ATOM   31974 C  CE  . LYS   R  4  229 ? 68.562  -189.505 -8.596  1.00 131.87 ? 221 LYS   R CE  1 
ATOM   31975 N  NZ  . LYS   R  4  229 ? 68.477  -188.422 -7.587  1.00 132.14 ? 221 LYS   R NZ  1 
ATOM   31976 N  N   . ILE   R  4  230 ? 66.052  -194.992 -6.644  1.00 123.79 ? 222 ILE   R N   1 
ATOM   31977 C  CA  . ILE   R  4  230 ? 65.570  -196.270 -7.250  1.00 124.06 ? 222 ILE   R CA  1 
ATOM   31978 C  C   . ILE   R  4  230 ? 66.002  -196.266 -8.721  1.00 128.74 ? 222 ILE   R C   1 
ATOM   31979 O  O   . ILE   R  4  230 ? 65.733  -195.262 -9.409  1.00 131.27 ? 222 ILE   R O   1 
ATOM   31980 C  CB  . ILE   R  4  230 ? 64.042  -196.440 -7.098  1.00 122.88 ? 222 ILE   R CB  1 
ATOM   31981 C  CG1 . ILE   R  4  230 ? 63.607  -196.421 -5.628  1.00 121.17 ? 222 ILE   R CG1 1 
ATOM   31982 C  CG2 . ILE   R  4  230 ? 63.572  -197.704 -7.808  1.00 124.65 ? 222 ILE   R CG2 1 
ATOM   31983 C  CD1 . ILE   R  4  230 ? 62.107  -196.399 -5.420  1.00 120.09 ? 222 ILE   R CD1 1 
ATOM   31984 N  N   . TYR   R  4  231 ? 66.646  -197.341 -9.183  1.00 127.49 ? 223 TYR   R N   1 
ATOM   31985 C  CA  . TYR   R  4  231 ? 67.196  -197.458 -10.560 1.00 127.94 ? 223 TYR   R CA  1 
ATOM   31986 C  C   . TYR   R  4  231 ? 66.058  -197.685 -11.560 1.00 127.94 ? 223 TYR   R C   1 
ATOM   31987 O  O   . TYR   R  4  231 ? 65.052  -198.329 -11.207 1.00 125.87 ? 223 TYR   R O   1 
ATOM   31988 C  CB  . TYR   R  4  231 ? 68.214  -198.597 -10.661 1.00 128.19 ? 223 TYR   R CB  1 
ATOM   31989 C  CG  . TYR   R  4  231 ? 69.486  -198.420 -9.868  1.00 129.98 ? 223 TYR   R CG  1 
ATOM   31990 C  CD1 . TYR   R  4  231 ? 69.793  -197.232 -9.219  1.00 131.45 ? 223 TYR   R CD1 1 
ATOM   31991 C  CD2 . TYR   R  4  231 ? 70.412  -199.447 -9.798  1.00 130.85 ? 223 TYR   R CD2 1 
ATOM   31992 C  CE1 . TYR   R  4  231 ? 70.967  -197.084 -8.498  1.00 133.27 ? 223 TYR   R CE1 1 
ATOM   31993 C  CE2 . TYR   R  4  231 ? 71.594  -199.313 -9.088  1.00 132.90 ? 223 TYR   R CE2 1 
ATOM   31994 C  CZ  . TYR   R  4  231 ? 71.875  -198.126 -8.436  1.00 133.36 ? 223 TYR   R CZ  1 
ATOM   31995 O  OH  . TYR   R  4  231 ? 73.040  -197.994 -7.736  1.00 132.01 ? 223 TYR   R OH  1 
ATOM   31996 N  N   . ASP   R  4  232 ? 66.233  -197.170 -12.781 1.00 132.01 ? 224 ASP   R N   1 
ATOM   31997 C  CA  . ASP   R  4  232 ? 65.325  -197.410 -13.935 1.00 137.45 ? 224 ASP   R CA  1 
ATOM   31998 C  C   . ASP   R  4  232 ? 65.433  -198.889 -14.321 1.00 135.66 ? 224 ASP   R C   1 
ATOM   31999 O  O   . ASP   R  4  232 ? 66.444  -199.524 -13.952 1.00 138.07 ? 224 ASP   R O   1 
ATOM   32000 C  CB  . ASP   R  4  232 ? 65.669  -196.519 -15.135 1.00 141.00 ? 224 ASP   R CB  1 
ATOM   32001 C  CG  . ASP   R  4  232 ? 65.952  -195.065 -14.792 1.00 142.98 ? 224 ASP   R CG  1 
ATOM   32002 O  OD1 . ASP   R  4  232 ? 65.211  -194.190 -15.284 1.00 144.09 ? 224 ASP   R OD1 1 
ATOM   32003 O  OD2 . ASP   R  4  232 ? 66.927  -194.817 -14.054 1.00 147.43 ? 224 ASP   R OD2 1 
ATOM   32004 N  N   . ASN   R  4  233 ? 64.438  -199.415 -15.039 1.00 134.49 ? 225 ASN   R N   1 
ATOM   32005 C  CA  . ASN   R  4  233 ? 64.466  -200.796 -15.588 1.00 134.24 ? 225 ASN   R CA  1 
ATOM   32006 C  C   . ASN   R  4  233 ? 65.550  -200.877 -16.670 1.00 138.67 ? 225 ASN   R C   1 
ATOM   32007 O  O   . ASN   R  4  233 ? 66.110  -201.972 -16.853 1.00 147.63 ? 225 ASN   R O   1 
ATOM   32008 C  CB  . ASN   R  4  233 ? 63.097  -201.236 -16.116 1.00 133.69 ? 225 ASN   R CB  1 
ATOM   32009 C  CG  . ASN   R  4  233 ? 62.024  -201.339 -15.049 1.00 132.04 ? 225 ASN   R CG  1 
ATOM   32010 O  OD1 . ASN   R  4  233 ? 60.840  -201.371 -15.372 1.00 137.31 ? 225 ASN   R OD1 1 
ATOM   32011 N  ND2 . ASN   R  4  233 ? 62.405  -201.401 -13.782 1.00 131.72 ? 225 ASN   R ND2 1 
ATOM   32012 N  N   . GLU   R  4  234 ? 65.846  -199.758 -17.341 1.00 137.21 ? 226 GLU   R N   1 
ATOM   32013 C  CA  . GLU   R  4  234 ? 66.901  -199.664 -18.388 1.00 142.48 ? 226 GLU   R CA  1 
ATOM   32014 C  C   . GLU   R  4  234 ? 68.284  -199.789 -17.736 1.00 139.66 ? 226 GLU   R C   1 
ATOM   32015 O  O   . GLU   R  4  234 ? 69.136  -200.497 -18.307 1.00 136.76 ? 226 GLU   R O   1 
ATOM   32016 C  CB  . GLU   R  4  234 ? 66.794  -198.353 -19.174 1.00 145.02 ? 226 GLU   R CB  1 
ATOM   32017 C  CG  . GLU   R  4  234 ? 65.687  -198.348 -20.214 1.00 149.32 ? 226 GLU   R CG  1 
ATOM   32018 C  CD  . GLU   R  4  234 ? 64.280  -198.202 -19.660 1.00 153.03 ? 226 GLU   R CD  1 
ATOM   32019 O  OE1 . GLU   R  4  234 ? 63.423  -199.038 -20.008 1.00 158.69 ? 226 GLU   R OE1 1 
ATOM   32020 O  OE2 . GLU   R  4  234 ? 64.042  -197.247 -18.892 1.00 154.06 ? 226 GLU   R OE2 1 
ATOM   32021 N  N   . LYS   R  4  235 ? 68.497  -199.132 -16.590 1.00 140.18 ? 227 LYS   R N   1 
ATOM   32022 C  CA  . LYS   R  4  235 ? 69.806  -199.100 -15.881 1.00 141.07 ? 227 LYS   R CA  1 
ATOM   32023 C  C   . LYS   R  4  235 ? 70.115  -200.485 -15.299 1.00 143.34 ? 227 LYS   R C   1 
ATOM   32024 O  O   . LYS   R  4  235 ? 71.275  -200.928 -15.436 1.00 140.02 ? 227 LYS   R O   1 
ATOM   32025 C  CB  . LYS   R  4  235 ? 69.816  -198.042 -14.774 1.00 141.07 ? 227 LYS   R CB  1 
ATOM   32026 C  CG  . LYS   R  4  235 ? 71.190  -197.779 -14.171 1.00 144.76 ? 227 LYS   R CG  1 
ATOM   32027 C  CD  . LYS   R  4  235 ? 71.181  -196.836 -12.990 1.00 146.21 ? 227 LYS   R CD  1 
ATOM   32028 C  CE  . LYS   R  4  235 ? 72.569  -196.584 -12.441 1.00 147.42 ? 227 LYS   R CE  1 
ATOM   32029 N  NZ  . LYS   R  4  235 ? 72.540  -195.680 -11.267 1.00 145.42 ? 227 LYS   R NZ  1 
ATOM   32030 N  N   . THR   R  4  236 ? 69.126  -201.133 -14.670 1.00 142.85 ? 228 THR   R N   1 
ATOM   32031 C  CA  . THR   R  4  236 ? 69.267  -202.468 -14.022 1.00 143.67 ? 228 THR   R CA  1 
ATOM   32032 C  C   . THR   R  4  236 ? 69.491  -203.541 -15.097 1.00 144.83 ? 228 THR   R C   1 
ATOM   32033 O  O   . THR   R  4  236 ? 70.259  -204.484 -14.824 1.00 150.01 ? 228 THR   R O   1 
ATOM   32034 C  CB  . THR   R  4  236 ? 68.063  -202.800 -13.128 1.00 141.94 ? 228 THR   R CB  1 
ATOM   32035 O  OG1 . THR   R  4  236 ? 67.969  -201.806 -12.107 1.00 139.31 ? 228 THR   R OG1 1 
ATOM   32036 C  CG2 . THR   R  4  236 ? 68.164  -204.167 -12.486 1.00 140.92 ? 228 THR   R CG2 1 
ATOM   32037 N  N   . ALA   R  4  237 ? 68.852  -203.404 -16.266 1.00 146.17 ? 229 ALA   R N   1 
ATOM   32038 C  CA  . ALA   R  4  237 ? 68.955  -204.348 -17.406 1.00 144.46 ? 229 ALA   R CA  1 
ATOM   32039 C  C   . ALA   R  4  237 ? 70.409  -204.436 -17.892 1.00 148.13 ? 229 ALA   R C   1 
ATOM   32040 O  O   . ALA   R  4  237 ? 70.847  -205.551 -18.237 1.00 144.91 ? 229 ALA   R O   1 
ATOM   32041 C  CB  . ALA   R  4  237 ? 68.029  -203.927 -18.521 1.00 142.63 ? 229 ALA   R CB  1 
ATOM   32042 N  N   . GLU   R  4  238 ? 71.123  -203.304 -17.921 1.00 151.65 ? 230 GLU   R N   1 
ATOM   32043 C  CA  . GLU   R  4  238 ? 72.543  -203.217 -18.362 1.00 157.29 ? 230 GLU   R CA  1 
ATOM   32044 C  C   . GLU   R  4  238 ? 73.462  -203.849 -17.309 1.00 151.48 ? 230 GLU   R C   1 
ATOM   32045 O  O   . GLU   R  4  238 ? 74.487  -204.432 -17.710 1.00 153.15 ? 230 GLU   R O   1 
ATOM   32046 C  CB  . GLU   R  4  238 ? 72.946  -201.764 -18.617 1.00 157.60 ? 230 GLU   R CB  1 
ATOM   32047 C  CG  . GLU   R  4  238 ? 72.233  -201.140 -19.800 1.00 164.37 ? 230 GLU   R CG  1 
ATOM   32048 C  CD  . GLU   R  4  238 ? 72.685  -199.727 -20.124 1.00 168.48 ? 230 GLU   R CD  1 
ATOM   32049 O  OE1 . GLU   R  4  238 ? 71.812  -198.854 -20.295 1.00 176.65 ? 230 GLU   R OE1 1 
ATOM   32050 O  OE2 . GLU   R  4  238 ? 73.909  -199.504 -20.207 1.00 171.06 ? 230 GLU   R OE2 1 
ATOM   32051 N  N   . LEU   R  4  239 ? 73.123  -203.720 -16.021 1.00 155.02 ? 231 LEU   R N   1 
ATOM   32052 C  CA  . LEU   R  4  239 ? 73.876  -204.337 -14.892 1.00 151.16 ? 231 LEU   R CA  1 
ATOM   32053 C  C   . LEU   R  4  239 ? 73.664  -205.858 -14.907 1.00 148.38 ? 231 LEU   R C   1 
ATOM   32054 O  O   . LEU   R  4  239 ? 74.619  -206.583 -14.562 1.00 149.99 ? 231 LEU   R O   1 
ATOM   32055 C  CB  . LEU   R  4  239 ? 73.426  -203.722 -13.560 1.00 148.94 ? 231 LEU   R CB  1 
ATOM   32056 C  CG  . LEU   R  4  239 ? 73.859  -202.276 -13.312 1.00 147.77 ? 231 LEU   R CG  1 
ATOM   32057 C  CD1 . LEU   R  4  239 ? 73.063  -201.663 -12.170 1.00 146.06 ? 231 LEU   R CD1 1 
ATOM   32058 C  CD2 . LEU   R  4  239 ? 75.351  -202.189 -13.025 1.00 143.04 ? 231 LEU   R CD2 1 
ATOM   32059 N  N   . ILE   R  4  240 ? 72.466  -206.320 -15.288 1.00 143.84 ? 232 ILE   R N   1 
ATOM   32060 C  CA  . ILE   R  4  240 ? 72.129  -207.769 -15.457 1.00 141.18 ? 232 ILE   R CA  1 
ATOM   32061 C  C   . ILE   R  4  240 ? 72.975  -208.340 -16.602 1.00 144.78 ? 232 ILE   R C   1 
ATOM   32062 O  O   . ILE   R  4  240 ? 73.493  -209.463 -16.447 1.00 143.69 ? 232 ILE   R O   1 
ATOM   32063 C  CB  . ILE   R  4  240 ? 70.618  -207.976 -15.699 1.00 137.96 ? 232 ILE   R CB  1 
ATOM   32064 C  CG1 . ILE   R  4  240 ? 69.799  -207.686 -14.437 1.00 134.93 ? 232 ILE   R CG1 1 
ATOM   32065 C  CG2 . ILE   R  4  240 ? 70.336  -209.374 -16.231 1.00 138.11 ? 232 ILE   R CG2 1 
ATOM   32066 C  CD1 . ILE   R  4  240 ? 68.327  -207.454 -14.692 1.00 133.63 ? 232 ILE   R CD1 1 
ATOM   32067 N  N   . LYS   R  4  241 ? 73.095  -207.598 -17.708 1.00 145.61 ? 233 LYS   R N   1 
ATOM   32068 C  CA  . LYS   R  4  241 ? 73.872  -208.001 -18.911 1.00 148.87 ? 233 LYS   R CA  1 
ATOM   32069 C  C   . LYS   R  4  241 ? 75.369  -208.025 -18.575 1.00 149.99 ? 233 LYS   R C   1 
ATOM   32070 O  O   . LYS   R  4  241 ? 76.054  -208.963 -19.022 1.00 155.73 ? 233 LYS   R O   1 
ATOM   32071 C  CB  . LYS   R  4  241 ? 73.588  -207.057 -20.083 1.00 150.47 ? 233 LYS   R CB  1 
ATOM   32072 C  CG  . LYS   R  4  241 ? 74.175  -207.506 -21.415 1.00 152.93 ? 233 LYS   R CG  1 
ATOM   32073 C  CD  . LYS   R  4  241 ? 73.365  -207.078 -22.621 1.00 153.08 ? 233 LYS   R CD  1 
ATOM   32074 C  CE  . LYS   R  4  241 ? 73.523  -205.611 -22.961 1.00 152.45 ? 233 LYS   R CE  1 
ATOM   32075 N  NZ  . LYS   R  4  241 ? 74.819  -205.340 -23.625 1.00 153.85 ? 233 LYS   R NZ  1 
ATOM   32076 N  N   . GLU   R  4  242 ? 75.850  -207.028 -17.825 1.00 151.26 ? 234 GLU   R N   1 
ATOM   32077 C  CA  . GLU   R  4  242 ? 77.263  -206.907 -17.369 1.00 153.48 ? 234 GLU   R CA  1 
ATOM   32078 C  C   . GLU   R  4  242 ? 77.613  -208.075 -16.438 1.00 151.94 ? 234 GLU   R C   1 
ATOM   32079 O  O   . GLU   R  4  242 ? 78.779  -208.512 -16.464 1.00 151.80 ? 234 GLU   R O   1 
ATOM   32080 C  CB  . GLU   R  4  242 ? 77.477  -205.569 -16.658 1.00 155.69 ? 234 GLU   R CB  1 
ATOM   32081 C  CG  . GLU   R  4  242 ? 78.930  -205.277 -16.325 1.00 160.08 ? 234 GLU   R CG  1 
ATOM   32082 C  CD  . GLU   R  4  242 ? 79.173  -203.915 -15.696 1.00 161.19 ? 234 GLU   R CD  1 
ATOM   32083 O  OE1 . GLU   R  4  242 ? 78.478  -202.952 -16.079 1.00 160.95 ? 234 GLU   R OE1 1 
ATOM   32084 O  OE2 . GLU   R  4  242 ? 80.054  -203.823 -14.820 1.00 164.18 ? 234 GLU   R OE2 1 
ATOM   32085 N  N   . LEU   R  4  243 ? 76.643  -208.546 -15.646 1.00 154.15 ? 235 LEU   R N   1 
ATOM   32086 C  CA  . LEU   R  4  243 ? 76.801  -209.661 -14.670 1.00 156.90 ? 235 LEU   R CA  1 
ATOM   32087 C  C   . LEU   R  4  243 ? 76.957  -210.988 -15.430 1.00 157.87 ? 235 LEU   R C   1 
ATOM   32088 O  O   . LEU   R  4  243 ? 77.918  -211.726 -15.127 1.00 156.23 ? 235 LEU   R O   1 
ATOM   32089 C  CB  . LEU   R  4  243 ? 75.586  -209.660 -13.729 1.00 156.90 ? 235 LEU   R CB  1 
ATOM   32090 C  CG  . LEU   R  4  243 ? 75.583  -210.644 -12.553 1.00 155.63 ? 235 LEU   R CG  1 
ATOM   32091 C  CD1 . LEU   R  4  243 ? 74.843  -211.926 -12.908 1.00 154.97 ? 235 LEU   R CD1 1 
ATOM   32092 C  CD2 . LEU   R  4  243 ? 76.985  -210.952 -12.041 1.00 157.65 ? 235 LEU   R CD2 1 
ATOM   32093 N  N   . LYS   R  4  244 ? 76.074  -211.267 -16.398 1.00 157.95 ? 236 LYS   R N   1 
ATOM   32094 C  CA  . LYS   R  4  244 ? 76.056  -212.544 -17.168 1.00 156.99 ? 236 LYS   R CA  1 
ATOM   32095 C  C   . LYS   R  4  244 ? 77.356  -212.692 -17.970 1.00 157.02 ? 236 LYS   R C   1 
ATOM   32096 O  O   . LYS   R  4  244 ? 77.876  -213.823 -18.041 1.00 155.76 ? 236 LYS   R O   1 
ATOM   32097 C  CB  . LYS   R  4  244 ? 74.851  -212.621 -18.112 1.00 160.43 ? 236 LYS   R CB  1 
ATOM   32098 C  CG  . LYS   R  4  244 ? 74.305  -214.028 -18.324 1.00 160.21 ? 236 LYS   R CG  1 
ATOM   32099 C  CD  . LYS   R  4  244 ? 73.942  -214.360 -19.757 1.00 161.12 ? 236 LYS   R CD  1 
ATOM   32100 C  CE  . LYS   R  4  244 ? 72.719  -213.624 -20.263 1.00 161.11 ? 236 LYS   R CE  1 
ATOM   32101 N  NZ  . LYS   R  4  244 ? 73.079  -212.390 -21.002 1.00 161.83 ? 236 LYS   R NZ  1 
ATOM   32102 N  N   . GLU   R  4  245 ? 77.846  -211.594 -18.556 1.00 157.81 ? 237 GLU   R N   1 
ATOM   32103 C  CA  . GLU   R  4  245 ? 79.099  -211.546 -19.359 1.00 161.21 ? 237 GLU   R CA  1 
ATOM   32104 C  C   . GLU   R  4  245 ? 80.308  -211.858 -18.467 1.00 165.27 ? 237 GLU   R C   1 
ATOM   32105 O  O   . GLU   R  4  245 ? 81.233  -212.538 -18.956 1.00 167.14 ? 237 GLU   R O   1 
ATOM   32106 C  CB  . GLU   R  4  245 ? 79.261  -210.177 -20.025 1.00 161.30 ? 237 GLU   R CB  1 
ATOM   32107 C  CG  . GLU   R  4  245 ? 78.338  -209.968 -21.213 1.00 160.47 ? 237 GLU   R CG  1 
ATOM   32108 C  CD  . GLU   R  4  245 ? 78.266  -208.538 -21.720 1.00 160.68 ? 237 GLU   R CD  1 
ATOM   32109 O  OE1 . GLU   R  4  245 ? 79.140  -207.732 -21.342 1.00 161.32 ? 237 GLU   R OE1 1 
ATOM   32110 O  OE2 . GLU   R  4  245 ? 77.334  -208.233 -22.488 1.00 157.55 ? 237 GLU   R OE2 1 
ATOM   32111 N  N   . LYS   R  4  246 ? 80.301  -211.382 -17.216 1.00 167.06 ? 238 LYS   R N   1 
ATOM   32112 C  CA  . LYS   R  4  246 ? 81.445  -211.502 -16.269 1.00 170.16 ? 238 LYS   R CA  1 
ATOM   32113 C  C   . LYS   R  4  246 ? 81.543  -212.937 -15.735 1.00 168.58 ? 238 LYS   R C   1 
ATOM   32114 O  O   . LYS   R  4  246 ? 82.682  -213.403 -15.549 1.00 175.28 ? 238 LYS   R O   1 
ATOM   32115 C  CB  . LYS   R  4  246 ? 81.335  -210.474 -15.137 1.00 170.93 ? 238 LYS   R CB  1 
ATOM   32116 C  CG  . LYS   R  4  246 ? 81.911  -209.105 -15.476 1.00 173.54 ? 238 LYS   R CG  1 
ATOM   32117 C  CD  . LYS   R  4  246 ? 81.903  -208.113 -14.333 1.00 173.17 ? 238 LYS   R CD  1 
ATOM   32118 C  CE  . LYS   R  4  246 ? 82.603  -206.819 -14.693 1.00 173.41 ? 238 LYS   R CE  1 
ATOM   32119 N  NZ  . LYS   R  4  246 ? 82.453  -205.792 -13.636 1.00 170.97 ? 238 LYS   R NZ  1 
ATOM   32120 N  N   . GLU   R  4  247 ? 80.409  -213.611 -15.506 1.00 170.48 ? 239 GLU   R N   1 
ATOM   32121 C  CA  . GLU   R  4  247 ? 80.363  -215.015 -15.003 1.00 169.81 ? 239 GLU   R CA  1 
ATOM   32122 C  C   . GLU   R  4  247 ? 80.852  -215.976 -16.094 1.00 173.80 ? 239 GLU   R C   1 
ATOM   32123 O  O   . GLU   R  4  247 ? 81.546  -216.955 -15.750 1.00 164.61 ? 239 GLU   R O   1 
ATOM   32124 C  CB  . GLU   R  4  247 ? 78.953  -215.388 -14.540 1.00 171.19 ? 239 GLU   R CB  1 
ATOM   32125 C  CG  . GLU   R  4  247 ? 78.511  -214.633 -13.299 1.00 168.29 ? 239 GLU   R CG  1 
ATOM   32126 C  CD  . GLU   R  4  247 ? 77.526  -215.377 -12.413 1.00 169.90 ? 239 GLU   R CD  1 
ATOM   32127 O  OE1 . GLU   R  4  247 ? 77.914  -215.751 -11.287 1.00 163.07 ? 239 GLU   R OE1 1 
ATOM   32128 O  OE2 . GLU   R  4  247 ? 76.372  -215.570 -12.845 1.00 169.81 ? 239 GLU   R OE2 1 
ATOM   32129 N  N   . ALA   R  4  248 ? 80.503  -215.705 -17.355 1.00 175.10 ? 240 ALA   R N   1 
ATOM   32130 C  CA  . ALA   R  4  248 ? 80.931  -216.484 -18.541 1.00 181.02 ? 240 ALA   R CA  1 
ATOM   32131 C  C   . ALA   R  4  248 ? 82.432  -216.286 -18.801 1.00 187.04 ? 240 ALA   R C   1 
ATOM   32132 O  O   . ALA   R  4  248 ? 83.040  -217.192 -19.405 1.00 190.38 ? 240 ALA   R O   1 
ATOM   32133 C  CB  . ALA   R  4  248 ? 80.109  -216.083 -19.742 1.00 182.40 ? 240 ALA   R CB  1 
ATOM   32134 N  N   . ALA   R  4  249 ? 83.009  -215.166 -18.345 1.00 186.87 ? 241 ALA   R N   1 
ATOM   32135 C  CA  . ALA   R  4  249 ? 84.387  -214.718 -18.668 1.00 190.23 ? 241 ALA   R CA  1 
ATOM   32136 C  C   . ALA   R  4  249 ? 85.436  -215.391 -17.766 1.00 193.22 ? 241 ALA   R C   1 
ATOM   32137 O  O   . ALA   R  4  249 ? 86.562  -214.856 -17.694 1.00 197.69 ? 241 ALA   R O   1 
ATOM   32138 C  CB  . ALA   R  4  249 ? 84.470  -213.211 -18.573 1.00 189.73 ? 241 ALA   R CB  1 
ATOM   32139 N  N   . GLU   R  4  250 ? 85.098  -216.509 -17.110 1.00 189.85 ? 242 GLU   R N   1 
ATOM   32140 C  CA  . GLU   R  4  250 ? 86.073  -217.412 -16.432 1.00 186.05 ? 242 GLU   R CA  1 
ATOM   32141 C  C   . GLU   R  4  250 ? 85.350  -218.694 -15.998 1.00 177.64 ? 242 GLU   R C   1 
ATOM   32142 O  O   . GLU   R  4  250 ? 85.663  -219.787 -16.470 1.00 176.83 ? 242 GLU   R O   1 
ATOM   32143 C  CB  . GLU   R  4  250 ? 86.737  -216.716 -15.239 1.00 185.20 ? 242 GLU   R CB  1 
ATOM   32144 C  CG  . GLU   R  4  250 ? 88.229  -216.989 -15.126 1.00 187.10 ? 242 GLU   R CG  1 
ATOM   32145 C  CD  . GLU   R  4  250 ? 88.599  -218.397 -14.689 1.00 185.20 ? 242 GLU   R CD  1 
ATOM   32146 O  OE1 . GLU   R  4  250 ? 89.092  -218.551 -13.553 1.00 179.98 ? 242 GLU   R OE1 1 
ATOM   32147 O  OE2 . GLU   R  4  250 ? 88.409  -219.334 -15.490 1.00 181.85 ? 242 GLU   R OE2 1 
ATOM   32148 N  N   . ASN   S  5  4   ? 51.447  -225.464 33.069  1.00 115.97 ? 3   ASN   S N   1 
ATOM   32149 C  CA  . ASN   S  5  4   ? 50.693  -226.456 32.238  1.00 121.43 ? 3   ASN   S CA  1 
ATOM   32150 C  C   . ASN   S  5  4   ? 49.334  -225.856 31.849  1.00 117.33 ? 3   ASN   S C   1 
ATOM   32151 O  O   . ASN   S  5  4   ? 49.214  -225.375 30.707  1.00 113.68 ? 3   ASN   S O   1 
ATOM   32152 C  CB  . ASN   S  5  4   ? 50.567  -227.805 32.955  1.00 126.63 ? 3   ASN   S CB  1 
ATOM   32153 C  CG  . ASN   S  5  4   ? 49.712  -228.804 32.203  1.00 133.36 ? 3   ASN   S CG  1 
ATOM   32154 O  OD1 . ASN   S  5  4   ? 49.982  -229.108 31.043  1.00 140.16 ? 3   ASN   S OD1 1 
ATOM   32155 N  ND2 . ASN   S  5  4   ? 48.683  -229.325 32.853  1.00 138.46 ? 3   ASN   S ND2 1 
ATOM   32156 N  N   . ASN   S  5  5   ? 48.357  -225.889 32.765  1.00 117.43 ? 4   ASN   S N   1 
ATOM   32157 C  CA  . ASN   S  5  5   ? 47.014  -225.262 32.610  1.00 116.87 ? 4   ASN   S CA  1 
ATOM   32158 C  C   . ASN   S  5  5   ? 47.024  -223.863 33.238  1.00 115.33 ? 4   ASN   S C   1 
ATOM   32159 O  O   . ASN   S  5  5   ? 46.015  -223.150 33.087  1.00 115.81 ? 4   ASN   S O   1 
ATOM   32160 C  CB  . ASN   S  5  5   ? 45.905  -226.102 33.253  1.00 117.44 ? 4   ASN   S CB  1 
ATOM   32161 C  CG  . ASN   S  5  5   ? 45.232  -227.058 32.291  1.00 119.60 ? 4   ASN   S CG  1 
ATOM   32162 O  OD1 . ASN   S  5  5   ? 45.263  -228.270 32.493  1.00 125.16 ? 4   ASN   S OD1 1 
ATOM   32163 N  ND2 . ASN   S  5  5   ? 44.610  -226.526 31.252  1.00 116.84 ? 4   ASN   S ND2 1 
ATOM   32164 N  N   . TYR   S  5  6   ? 48.117  -223.487 33.910  1.00 116.08 ? 5   TYR   S N   1 
ATOM   32165 C  CA  . TYR   S  5  6   ? 48.213  -222.279 34.773  1.00 115.39 ? 5   TYR   S CA  1 
ATOM   32166 C  C   . TYR   S  5  6   ? 49.270  -221.300 34.241  1.00 118.62 ? 5   TYR   S C   1 
ATOM   32167 O  O   . TYR   S  5  6   ? 49.703  -220.418 35.018  1.00 116.80 ? 5   TYR   S O   1 
ATOM   32168 C  CB  . TYR   S  5  6   ? 48.532  -222.707 36.207  1.00 117.29 ? 5   TYR   S CB  1 
ATOM   32169 C  CG  . TYR   S  5  6   ? 47.621  -223.779 36.746  1.00 113.73 ? 5   TYR   S CG  1 
ATOM   32170 C  CD1 . TYR   S  5  6   ? 47.912  -225.121 36.569  1.00 111.78 ? 5   TYR   S CD1 1 
ATOM   32171 C  CD2 . TYR   S  5  6   ? 46.458  -223.451 37.423  1.00 112.88 ? 5   TYR   S CD2 1 
ATOM   32172 C  CE1 . TYR   S  5  6   ? 47.077  -226.111 37.059  1.00 111.45 ? 5   TYR   S CE1 1 
ATOM   32173 C  CE2 . TYR   S  5  6   ? 45.612  -224.428 37.920  1.00 110.76 ? 5   TYR   S CE2 1 
ATOM   32174 C  CZ  . TYR   S  5  6   ? 45.923  -225.763 37.737  1.00 110.79 ? 5   TYR   S CZ  1 
ATOM   32175 O  OH  . TYR   S  5  6   ? 45.100  -226.737 38.218  1.00 112.54 ? 5   TYR   S OH  1 
ATOM   32176 N  N   . ASP   S  5  7   ? 49.654  -221.432 32.965  1.00 112.66 ? 6   ASP   S N   1 
ATOM   32177 C  CA  . ASP   S  5  7   ? 50.722  -220.617 32.322  1.00 110.95 ? 6   ASP   S CA  1 
ATOM   32178 C  C   . ASP   S  5  7   ? 50.146  -219.805 31.152  1.00 107.76 ? 6   ASP   S C   1 
ATOM   32179 O  O   . ASP   S  5  7   ? 50.947  -219.317 30.329  1.00 102.02 ? 6   ASP   S O   1 
ATOM   32180 C  CB  . ASP   S  5  7   ? 51.888  -221.500 31.867  1.00 113.95 ? 6   ASP   S CB  1 
ATOM   32181 C  CG  . ASP   S  5  7   ? 51.551  -222.468 30.742  1.00 116.33 ? 6   ASP   S CG  1 
ATOM   32182 O  OD1 . ASP   S  5  7   ? 50.348  -222.678 30.481  1.00 122.14 ? 6   ASP   S OD1 1 
ATOM   32183 O  OD2 . ASP   S  5  7   ? 52.498  -223.007 30.133  1.00 115.52 ? 6   ASP   S OD2 1 
ATOM   32184 N  N   . GLY   S  5  8   ? 48.818  -219.662 31.083  1.00 109.30 ? 7   GLY   S N   1 
ATOM   32185 C  CA  . GLY   S  5  8   ? 48.119  -218.908 30.024  1.00 112.22 ? 7   GLY   S CA  1 
ATOM   32186 C  C   . GLY   S  5  8   ? 48.357  -217.410 30.130  1.00 113.24 ? 7   GLY   S C   1 
ATOM   32187 O  O   . GLY   S  5  8   ? 48.418  -216.751 29.075  1.00 115.62 ? 7   GLY   S O   1 
ATOM   32188 N  N   . ASP   S  5  9   ? 48.482  -216.889 31.356  1.00 114.49 ? 8   ASP   S N   1 
ATOM   32189 C  CA  . ASP   S  5  9   ? 48.668  -215.441 31.641  1.00 114.06 ? 8   ASP   S CA  1 
ATOM   32190 C  C   . ASP   S  5  9   ? 49.302  -215.263 33.027  1.00 113.28 ? 8   ASP   S C   1 
ATOM   32191 O  O   . ASP   S  5  9   ? 49.400  -216.261 33.774  1.00 110.37 ? 8   ASP   S O   1 
ATOM   32192 C  CB  . ASP   S  5  9   ? 47.338  -214.693 31.518  1.00 117.96 ? 8   ASP   S CB  1 
ATOM   32193 C  CG  . ASP   S  5  9   ? 46.160  -215.469 32.080  1.00 117.97 ? 8   ASP   S CG  1 
ATOM   32194 O  OD1 . ASP   S  5  9   ? 46.228  -215.862 33.260  1.00 119.49 ? 8   ASP   S OD1 1 
ATOM   32195 O  OD2 . ASP   S  5  9   ? 45.195  -215.695 31.324  1.00 122.18 ? 8   ASP   S OD2 1 
ATOM   32196 N  N   . THR   S  5  10  ? 49.714  -214.031 33.346  1.00 110.59 ? 9   THR   S N   1 
ATOM   32197 C  CA  . THR   S  5  10  ? 50.446  -213.668 34.590  1.00 108.95 ? 9   THR   S CA  1 
ATOM   32198 C  C   . THR   S  5  10  ? 49.488  -213.609 35.782  1.00 105.10 ? 9   THR   S C   1 
ATOM   32199 O  O   . THR   S  5  10  ? 49.976  -213.672 36.926  1.00 106.73 ? 9   THR   S O   1 
ATOM   32200 C  CB  . THR   S  5  10  ? 51.146  -212.309 34.472  1.00 109.88 ? 9   THR   S CB  1 
ATOM   32201 O  OG1 . THR   S  5  10  ? 51.348  -212.002 33.092  1.00 110.43 ? 9   THR   S OG1 1 
ATOM   32202 C  CG2 . THR   S  5  10  ? 52.466  -212.290 35.210  1.00 111.80 ? 9   THR   S CG2 1 
ATOM   32203 N  N   . VAL   S  5  11  ? 48.186  -213.472 35.524  1.00 102.08 ? 10  VAL   S N   1 
ATOM   32204 C  CA  . VAL   S  5  11  ? 47.155  -213.234 36.576  1.00 103.34 ? 10  VAL   S CA  1 
ATOM   32205 C  C   . VAL   S  5  11  ? 46.786  -214.560 37.260  1.00 103.99 ? 10  VAL   S C   1 
ATOM   32206 O  O   . VAL   S  5  11  ? 46.032  -214.507 38.255  1.00 99.00  ? 10  VAL   S O   1 
ATOM   32207 C  CB  . VAL   S  5  11  ? 45.922  -212.516 35.990  1.00 104.15 ? 10  VAL   S CB  1 
ATOM   32208 C  CG1 . VAL   S  5  11  ? 44.892  -213.481 35.421  1.00 104.21 ? 10  VAL   S CG1 1 
ATOM   32209 C  CG2 . VAL   S  5  11  ? 45.281  -211.601 37.017  1.00 105.08 ? 10  VAL   S CG2 1 
ATOM   32210 N  N   . THR   S  5  12  ? 47.293  -215.698 36.766  1.00 103.80 ? 11  THR   S N   1 
ATOM   32211 C  CA  . THR   S  5  12  ? 46.976  -217.053 37.295  1.00 105.54 ? 11  THR   S CA  1 
ATOM   32212 C  C   . THR   S  5  12  ? 48.139  -217.609 38.124  1.00 104.62 ? 11  THR   S C   1 
ATOM   32213 O  O   . THR   S  5  12  ? 49.278  -217.659 37.608  1.00 104.57 ? 11  THR   S O   1 
ATOM   32214 C  CB  . THR   S  5  12  ? 46.632  -218.049 36.181  1.00 107.47 ? 11  THR   S CB  1 
ATOM   32215 O  OG1 . THR   S  5  12  ? 45.754  -217.418 35.249  1.00 107.85 ? 11  THR   S OG1 1 
ATOM   32216 C  CG2 . THR   S  5  12  ? 45.976  -219.302 36.723  1.00 108.96 ? 11  THR   S CG2 1 
ATOM   32217 N  N   . PHE   S  5  13  ? 47.822  -218.043 39.348  1.00 101.47 ? 12  PHE   S N   1 
ATOM   32218 C  CA  . PHE   S  5  13  ? 48.682  -218.830 40.267  1.00 103.38 ? 12  PHE   S CA  1 
ATOM   32219 C  C   . PHE   S  5  13  ? 48.533  -220.313 39.919  1.00 104.64 ? 12  PHE   S C   1 
ATOM   32220 O  O   . PHE   S  5  13  ? 47.407  -220.738 39.591  1.00 105.15 ? 12  PHE   S O   1 
ATOM   32221 C  CB  . PHE   S  5  13  ? 48.279  -218.619 41.731  1.00 101.32 ? 12  PHE   S CB  1 
ATOM   32222 C  CG  . PHE   S  5  13  ? 48.989  -217.495 42.443  1.00 101.45 ? 12  PHE   S CG  1 
ATOM   32223 C  CD1 . PHE   S  5  13  ? 50.355  -217.559 42.672  1.00 104.56 ? 12  PHE   S CD1 1 
ATOM   32224 C  CD2 . PHE   S  5  13  ? 48.293  -216.392 42.916  1.00 98.67  ? 12  PHE   S CD2 1 
ATOM   32225 C  CE1 . PHE   S  5  13  ? 51.013  -216.534 43.335  1.00 103.18 ? 12  PHE   S CE1 1 
ATOM   32226 C  CE2 . PHE   S  5  13  ? 48.953  -215.369 43.580  1.00 97.13  ? 12  PHE   S CE2 1 
ATOM   32227 C  CZ  . PHE   S  5  13  ? 50.311  -215.443 43.790  1.00 99.14  ? 12  PHE   S CZ  1 
ATOM   32228 N  N   . SER   S  5  14  ? 49.628  -221.072 39.996  1.00 106.15 ? 13  SER   S N   1 
ATOM   32229 C  CA  . SER   S  5  14  ? 49.629  -222.558 39.921  1.00 106.67 ? 13  SER   S CA  1 
ATOM   32230 C  C   . SER   S  5  14  ? 49.234  -223.126 41.283  1.00 105.31 ? 13  SER   S C   1 
ATOM   32231 O  O   . SER   S  5  14  ? 49.276  -222.416 42.286  1.00 106.38 ? 13  SER   S O   1 
ATOM   32232 C  CB  . SER   S  5  14  ? 50.967  -223.090 39.464  1.00 108.32 ? 13  SER   S CB  1 
ATOM   32233 O  OG  . SER   S  5  14  ? 51.923  -223.060 40.516  1.00 106.99 ? 13  SER   S OG  1 
ATOM   32234 N  N   . PRO   S  5  15  ? 48.825  -224.412 41.368  1.00 102.86 ? 14  PRO   S N   1 
ATOM   32235 C  CA  . PRO   S  5  15  ? 48.456  -225.023 42.648  1.00 102.09 ? 14  PRO   S CA  1 
ATOM   32236 C  C   . PRO   S  5  15  ? 49.540  -225.042 43.739  1.00 101.45 ? 14  PRO   S C   1 
ATOM   32237 O  O   . PRO   S  5  15  ? 49.170  -225.198 44.886  1.00 98.85  ? 14  PRO   S O   1 
ATOM   32238 C  CB  . PRO   S  5  15  ? 48.101  -226.464 42.264  1.00 103.38 ? 14  PRO   S CB  1 
ATOM   32239 C  CG  . PRO   S  5  15  ? 47.686  -226.363 40.815  1.00 103.14 ? 14  PRO   S CG  1 
ATOM   32240 C  CD  . PRO   S  5  15  ? 48.616  -225.322 40.233  1.00 102.30 ? 14  PRO   S CD  1 
ATOM   32241 N  N   . THR   S  5  16  ? 50.819  -224.889 43.376  1.00 103.57 ? 15  THR   S N   1 
ATOM   32242 C  CA  . THR   S  5  16  ? 51.954  -224.784 44.336  1.00 105.85 ? 15  THR   S CA  1 
ATOM   32243 C  C   . THR   S  5  16  ? 52.368  -223.316 44.531  1.00 105.60 ? 15  THR   S C   1 
ATOM   32244 O  O   . THR   S  5  16  ? 53.403  -223.091 45.186  1.00 106.34 ? 15  THR   S O   1 
ATOM   32245 C  CB  . THR   S  5  16  ? 53.137  -225.654 43.892  1.00 107.41 ? 15  THR   S CB  1 
ATOM   32246 O  OG1 . THR   S  5  16  ? 53.581  -225.222 42.606  1.00 108.79 ? 15  THR   S OG1 1 
ATOM   32247 C  CG2 . THR   S  5  16  ? 52.786  -227.122 43.816  1.00 108.01 ? 15  THR   S CG2 1 
ATOM   32248 N  N   . GLY   S  5  17  ? 51.594  -222.361 44.000  1.00 107.50 ? 16  GLY   S N   1 
ATOM   32249 C  CA  . GLY   S  5  17  ? 51.767  -220.912 44.236  1.00 108.15 ? 16  GLY   S CA  1 
ATOM   32250 C  C   . GLY   S  5  17  ? 52.845  -220.286 43.362  1.00 109.66 ? 16  GLY   S C   1 
ATOM   32251 O  O   . GLY   S  5  17  ? 53.494  -219.323 43.826  1.00 106.45 ? 16  GLY   S O   1 
ATOM   32252 N  N   . ARG   S  5  18  ? 53.025  -220.792 42.138  1.00 111.58 ? 17  ARG   S N   1 
ATOM   32253 C  CA  . ARG   S  5  18  ? 54.013  -220.269 41.155  1.00 112.76 ? 17  ARG   S CA  1 
ATOM   32254 C  C   . ARG   S  5  18  ? 53.297  -219.404 40.109  1.00 112.12 ? 17  ARG   S C   1 
ATOM   32255 O  O   . ARG   S  5  18  ? 52.099  -219.645 39.846  1.00 111.57 ? 17  ARG   S O   1 
ATOM   32256 C  CB  . ARG   S  5  18  ? 54.757  -221.419 40.469  1.00 113.13 ? 17  ARG   S CB  1 
ATOM   32257 C  CG  . ARG   S  5  18  ? 55.392  -222.421 41.423  1.00 112.16 ? 17  ARG   S CG  1 
ATOM   32258 C  CD  . ARG   S  5  18  ? 55.771  -223.708 40.717  1.00 112.80 ? 17  ARG   S CD  1 
ATOM   32259 N  NE  . ARG   S  5  18  ? 56.914  -223.545 39.827  1.00 111.01 ? 17  ARG   S NE  1 
ATOM   32260 C  CZ  . ARG   S  5  18  ? 57.382  -224.489 39.015  1.00 113.05 ? 17  ARG   S CZ  1 
ATOM   32261 N  NH1 . ARG   S  5  18  ? 56.807  -225.680 38.971  1.00 115.72 ? 17  ARG   S NH1 1 
ATOM   32262 N  NH2 . ARG   S  5  18  ? 58.428  -224.240 38.247  1.00 111.62 ? 17  ARG   S NH2 1 
ATOM   32263 N  N   . LEU   S  5  19  ? 54.016  -218.429 39.543  1.00 111.71 ? 18  LEU   S N   1 
ATOM   32264 C  CA  . LEU   S  5  19  ? 53.588  -217.624 38.368  1.00 111.74 ? 18  LEU   S CA  1 
ATOM   32265 C  C   . LEU   S  5  19  ? 54.460  -218.026 37.176  1.00 111.55 ? 18  LEU   S C   1 
ATOM   32266 O  O   . LEU   S  5  19  ? 55.616  -217.558 37.106  1.00 109.85 ? 18  LEU   S O   1 
ATOM   32267 C  CB  . LEU   S  5  19  ? 53.743  -216.133 38.682  1.00 111.22 ? 18  LEU   S CB  1 
ATOM   32268 C  CG  . LEU   S  5  19  ? 53.054  -215.648 39.956  1.00 111.04 ? 18  LEU   S CG  1 
ATOM   32269 C  CD1 . LEU   S  5  19  ? 53.449  -214.212 40.265  1.00 110.43 ? 18  LEU   S CD1 1 
ATOM   32270 C  CD2 . LEU   S  5  19  ? 51.545  -215.778 39.842  1.00 111.29 ? 18  LEU   S CD2 1 
ATOM   32271 N  N   . PHE   S  5  20  ? 53.936  -218.877 36.290  1.00 111.15 ? 19  PHE   S N   1 
ATOM   32272 C  CA  . PHE   S  5  20  ? 54.712  -219.514 35.194  1.00 109.85 ? 19  PHE   S CA  1 
ATOM   32273 C  C   . PHE   S  5  20  ? 55.139  -218.452 34.173  1.00 103.69 ? 19  PHE   S C   1 
ATOM   32274 O  O   . PHE   S  5  20  ? 56.296  -218.509 33.721  1.00 103.53 ? 19  PHE   S O   1 
ATOM   32275 C  CB  . PHE   S  5  20  ? 53.933  -220.673 34.565  1.00 111.50 ? 19  PHE   S CB  1 
ATOM   32276 C  CG  . PHE   S  5  20  ? 54.063  -221.972 35.321  1.00 114.53 ? 19  PHE   S CG  1 
ATOM   32277 C  CD1 . PHE   S  5  20  ? 55.248  -222.695 35.290  1.00 116.06 ? 19  PHE   S CD1 1 
ATOM   32278 C  CD2 . PHE   S  5  20  ? 53.009  -222.468 36.074  1.00 116.49 ? 19  PHE   S CD2 1 
ATOM   32279 C  CE1 . PHE   S  5  20  ? 55.373  -223.886 35.988  1.00 117.46 ? 19  PHE   S CE1 1 
ATOM   32280 C  CE2 . PHE   S  5  20  ? 53.136  -223.661 36.771  1.00 117.45 ? 19  PHE   S CE2 1 
ATOM   32281 C  CZ  . PHE   S  5  20  ? 54.317  -224.367 36.727  1.00 117.38 ? 19  PHE   S CZ  1 
ATOM   32282 N  N   . GLN   S  5  21  ? 54.257  -217.506 33.838  1.00 100.07 ? 20  GLN   S N   1 
ATOM   32283 C  CA  . GLN   S  5  21  ? 54.572  -216.408 32.882  1.00 100.77 ? 20  GLN   S CA  1 
ATOM   32284 C  C   . GLN   S  5  21  ? 55.810  -215.641 33.372  1.00 100.78 ? 20  GLN   S C   1 
ATOM   32285 O  O   . GLN   S  5  21  ? 56.660  -215.307 32.522  1.00 99.03  ? 20  GLN   S O   1 
ATOM   32286 C  CB  . GLN   S  5  21  ? 53.371  -215.480 32.690  1.00 99.91  ? 20  GLN   S CB  1 
ATOM   32287 C  CG  . GLN   S  5  21  ? 52.374  -215.983 31.654  1.00 98.96  ? 20  GLN   S CG  1 
ATOM   32288 C  CD  . GLN   S  5  21  ? 53.000  -216.165 30.292  1.00 99.59  ? 20  GLN   S CD  1 
ATOM   32289 O  OE1 . GLN   S  5  21  ? 53.495  -215.222 29.683  1.00 95.26  ? 20  GLN   S OE1 1 
ATOM   32290 N  NE2 . GLN   S  5  21  ? 52.985  -217.391 29.796  1.00 100.75 ? 20  GLN   S NE2 1 
ATOM   32291 N  N   . VAL   S  5  22  ? 55.915  -215.395 34.684  1.00 101.14 ? 21  VAL   S N   1 
ATOM   32292 C  CA  . VAL   S  5  22  ? 57.076  -214.704 35.324  1.00 100.23 ? 21  VAL   S CA  1 
ATOM   32293 C  C   . VAL   S  5  22  ? 58.311  -215.604 35.213  1.00 101.38 ? 21  VAL   S C   1 
ATOM   32294 O  O   . VAL   S  5  22  ? 59.403  -215.068 34.955  1.00 99.88  ? 21  VAL   S O   1 
ATOM   32295 C  CB  . VAL   S  5  22  ? 56.790  -214.331 36.792  1.00 101.57 ? 21  VAL   S CB  1 
ATOM   32296 C  CG1 . VAL   S  5  22  ? 58.022  -213.758 37.481  1.00 102.26 ? 21  VAL   S CG1 1 
ATOM   32297 C  CG2 . VAL   S  5  22  ? 55.617  -213.369 36.909  1.00 100.44 ? 21  VAL   S CG2 1 
ATOM   32298 N  N   . GLU   S  5  23  ? 58.143  -216.913 35.421  1.00 102.51 ? 22  GLU   S N   1 
ATOM   32299 C  CA  . GLU   S  5  23  ? 59.232  -217.921 35.313  1.00 106.73 ? 22  GLU   S CA  1 
ATOM   32300 C  C   . GLU   S  5  23  ? 59.694  -218.028 33.855  1.00 104.99 ? 22  GLU   S C   1 
ATOM   32301 O  O   . GLU   S  5  23  ? 60.908  -218.194 33.638  1.00 104.74 ? 22  GLU   S O   1 
ATOM   32302 C  CB  . GLU   S  5  23  ? 58.774  -219.282 35.844  1.00 110.02 ? 22  GLU   S CB  1 
ATOM   32303 C  CG  . GLU   S  5  23  ? 58.714  -219.348 37.360  1.00 113.57 ? 22  GLU   S CG  1 
ATOM   32304 C  CD  . GLU   S  5  23  ? 58.389  -220.716 37.937  1.00 115.65 ? 22  GLU   S CD  1 
ATOM   32305 O  OE1 . GLU   S  5  23  ? 58.528  -221.719 37.206  1.00 121.06 ? 22  GLU   S OE1 1 
ATOM   32306 O  OE2 . GLU   S  5  23  ? 57.999  -220.776 39.119  1.00 119.40 ? 22  GLU   S OE2 1 
ATOM   32307 N  N   . TYR   S  5  24  ? 58.767  -217.946 32.896  1.00 104.86 ? 23  TYR   S N   1 
ATOM   32308 C  CA  . TYR   S  5  24  ? 59.065  -218.008 31.440  1.00 108.81 ? 23  TYR   S CA  1 
ATOM   32309 C  C   . TYR   S  5  24  ? 59.834  -216.749 31.026  1.00 110.28 ? 23  TYR   S C   1 
ATOM   32310 O  O   . TYR   S  5  24  ? 60.755  -216.863 30.198  1.00 115.77 ? 23  TYR   S O   1 
ATOM   32311 C  CB  . TYR   S  5  24  ? 57.790  -218.183 30.610  1.00 108.41 ? 23  TYR   S CB  1 
ATOM   32312 C  CG  . TYR   S  5  24  ? 57.057  -219.492 30.784  1.00 107.96 ? 23  TYR   S CG  1 
ATOM   32313 C  CD1 . TYR   S  5  24  ? 57.602  -220.558 31.489  1.00 108.33 ? 23  TYR   S CD1 1 
ATOM   32314 C  CD2 . TYR   S  5  24  ? 55.810  -219.676 30.208  1.00 107.74 ? 23  TYR   S CD2 1 
ATOM   32315 C  CE1 . TYR   S  5  24  ? 56.918  -221.754 31.636  1.00 108.63 ? 23  TYR   S CE1 1 
ATOM   32316 C  CE2 . TYR   S  5  24  ? 55.115  -220.867 30.343  1.00 107.04 ? 23  TYR   S CE2 1 
ATOM   32317 C  CZ  . TYR   S  5  24  ? 55.670  -221.910 31.060  1.00 108.58 ? 23  TYR   S CZ  1 
ATOM   32318 O  OH  . TYR   S  5  24  ? 54.981  -223.081 31.184  1.00 109.67 ? 23  TYR   S OH  1 
ATOM   32319 N  N   . ALA   S  5  25  ? 59.477  -215.590 31.588  1.00 111.84 ? 24  ALA   S N   1 
ATOM   32320 C  CA  . ALA   S  5  25  ? 60.210  -214.315 31.403  1.00 113.44 ? 24  ALA   S CA  1 
ATOM   32321 C  C   . ALA   S  5  25  ? 61.645  -214.491 31.913  1.00 113.18 ? 24  ALA   S C   1 
ATOM   32322 O  O   . ALA   S  5  25  ? 62.581  -214.161 31.161  1.00 113.89 ? 24  ALA   S O   1 
ATOM   32323 C  CB  . ALA   S  5  25  ? 59.500  -213.191 32.115  1.00 113.48 ? 24  ALA   S CB  1 
ATOM   32324 N  N   . LEU   S  5  26  ? 61.795  -215.016 33.136  1.00 117.79 ? 25  LEU   S N   1 
ATOM   32325 C  CA  . LEU   S  5  26  ? 63.100  -215.350 33.779  1.00 118.79 ? 25  LEU   S CA  1 
ATOM   32326 C  C   . LEU   S  5  26  ? 63.946  -216.207 32.826  1.00 119.21 ? 25  LEU   S C   1 
ATOM   32327 O  O   . LEU   S  5  26  ? 65.180  -216.034 32.831  1.00 115.91 ? 25  LEU   S O   1 
ATOM   32328 C  CB  . LEU   S  5  26  ? 62.849  -216.083 35.106  1.00 122.09 ? 25  LEU   S CB  1 
ATOM   32329 C  CG  . LEU   S  5  26  ? 63.138  -215.315 36.402  1.00 123.32 ? 25  LEU   S CG  1 
ATOM   32330 C  CD1 . LEU   S  5  26  ? 62.724  -213.852 36.319  1.00 123.00 ? 25  LEU   S CD1 1 
ATOM   32331 C  CD2 . LEU   S  5  26  ? 62.449  -215.984 37.584  1.00 124.51 ? 25  LEU   S CD2 1 
ATOM   32332 N  N   . GLU   S  5  27  ? 63.309  -217.089 32.046  1.00 121.52 ? 26  GLU   S N   1 
ATOM   32333 C  CA  . GLU   S  5  27  ? 63.986  -218.054 31.134  1.00 125.92 ? 26  GLU   S CA  1 
ATOM   32334 C  C   . GLU   S  5  27  ? 64.646  -217.299 29.971  1.00 122.69 ? 26  GLU   S C   1 
ATOM   32335 O  O   . GLU   S  5  27  ? 65.728  -217.733 29.538  1.00 122.61 ? 26  GLU   S O   1 
ATOM   32336 C  CB  . GLU   S  5  27  ? 62.998  -219.108 30.626  1.00 129.63 ? 26  GLU   S CB  1 
ATOM   32337 C  CG  . GLU   S  5  27  ? 63.663  -220.342 30.032  1.00 134.53 ? 26  GLU   S CG  1 
ATOM   32338 C  CD  . GLU   S  5  27  ? 64.555  -221.131 30.979  1.00 138.37 ? 26  GLU   S CD  1 
ATOM   32339 O  OE1 . GLU   S  5  27  ? 65.595  -221.650 30.519  1.00 140.30 ? 26  GLU   S OE1 1 
ATOM   32340 O  OE2 . GLU   S  5  27  ? 64.206  -221.234 32.172  1.00 143.77 ? 26  GLU   S OE2 1 
ATOM   32341 N  N   . ALA   S  5  28  ? 64.025  -216.216 29.489  1.00 121.91 ? 27  ALA   S N   1 
ATOM   32342 C  CA  . ALA   S  5  28  ? 64.546  -215.351 28.401  1.00 121.02 ? 27  ALA   S CA  1 
ATOM   32343 C  C   . ALA   S  5  28  ? 65.900  -214.753 28.805  1.00 121.07 ? 27  ALA   S C   1 
ATOM   32344 O  O   . ALA   S  5  28  ? 66.747  -214.557 27.909  1.00 123.28 ? 27  ALA   S O   1 
ATOM   32345 C  CB  . ALA   S  5  28  ? 63.553  -214.264 28.067  1.00 116.15 ? 27  ALA   S CB  1 
ATOM   32346 N  N   . ILE   S  5  29  ? 66.087  -214.470 30.100  1.00 121.63 ? 28  ILE   S N   1 
ATOM   32347 C  CA  . ILE   S  5  29  ? 67.345  -213.897 30.671  1.00 123.42 ? 28  ILE   S CA  1 
ATOM   32348 C  C   . ILE   S  5  29  ? 68.455  -214.942 30.540  1.00 129.22 ? 28  ILE   S C   1 
ATOM   32349 O  O   . ILE   S  5  29  ? 69.564  -214.568 30.105  1.00 123.79 ? 28  ILE   S O   1 
ATOM   32350 C  CB  . ILE   S  5  29  ? 67.165  -213.460 32.140  1.00 122.71 ? 28  ILE   S CB  1 
ATOM   32351 C  CG1 . ILE   S  5  29  ? 66.025  -212.452 32.301  1.00 121.40 ? 28  ILE   S CG1 1 
ATOM   32352 C  CG2 . ILE   S  5  29  ? 68.473  -212.920 32.702  1.00 122.28 ? 28  ILE   S CG2 1 
ATOM   32353 C  CD1 . ILE   S  5  29  ? 65.618  -212.208 33.731  1.00 122.69 ? 28  ILE   S CD1 1 
ATOM   32354 N  N   . LYS   S  5  30  ? 68.150  -216.191 30.913  1.00 136.06 ? 29  LYS   S N   1 
ATOM   32355 C  CA  . LYS   S  5  30  ? 69.092  -217.345 30.897  1.00 138.08 ? 29  LYS   S CA  1 
ATOM   32356 C  C   . LYS   S  5  30  ? 69.649  -217.548 29.480  1.00 140.07 ? 29  LYS   S C   1 
ATOM   32357 O  O   . LYS   S  5  30  ? 70.837  -217.912 29.373  1.00 143.56 ? 29  LYS   S O   1 
ATOM   32358 C  CB  . LYS   S  5  30  ? 68.416  -218.618 31.423  1.00 142.26 ? 29  LYS   S CB  1 
ATOM   32359 C  CG  . LYS   S  5  30  ? 68.865  -219.059 32.811  1.00 147.61 ? 29  LYS   S CG  1 
ATOM   32360 C  CD  . LYS   S  5  30  ? 68.389  -218.158 33.937  1.00 146.50 ? 29  LYS   S CD  1 
ATOM   32361 C  CE  . LYS   S  5  30  ? 66.945  -218.393 34.333  1.00 146.19 ? 29  LYS   S CE  1 
ATOM   32362 N  NZ  . LYS   S  5  30  ? 66.751  -219.719 34.968  1.00 147.28 ? 29  LYS   S NZ  1 
ATOM   32363 N  N   . GLN   S  5  31  ? 68.838  -217.310 28.441  1.00 134.76 ? 30  GLN   S N   1 
ATOM   32364 C  CA  . GLN   S  5  31  ? 69.260  -217.455 27.019  1.00 138.05 ? 30  GLN   S CA  1 
ATOM   32365 C  C   . GLN   S  5  31  ? 70.133  -216.258 26.616  1.00 131.94 ? 30  GLN   S C   1 
ATOM   32366 O  O   . GLN   S  5  31  ? 70.887  -216.388 25.637  1.00 126.34 ? 30  GLN   S O   1 
ATOM   32367 C  CB  . GLN   S  5  31  ? 68.073  -217.551 26.054  1.00 145.76 ? 30  GLN   S CB  1 
ATOM   32368 C  CG  . GLN   S  5  31  ? 66.920  -218.438 26.513  1.00 153.05 ? 30  GLN   S CG  1 
ATOM   32369 C  CD  . GLN   S  5  31  ? 67.286  -219.884 26.757  1.00 159.95 ? 30  GLN   S CD  1 
ATOM   32370 O  OE1 . GLN   S  5  31  ? 68.381  -220.342 26.434  1.00 160.58 ? 30  GLN   S OE1 1 
ATOM   32371 N  NE2 . GLN   S  5  31  ? 66.345  -220.626 27.322  1.00 165.27 ? 30  GLN   S NE2 1 
ATOM   32372 N  N   . GLY   S  5  32  ? 70.023  -215.134 27.331  1.00 127.56 ? 31  GLY   S N   1 
ATOM   32373 C  CA  . GLY   S  5  32  ? 70.758  -213.886 27.041  1.00 127.49 ? 31  GLY   S CA  1 
ATOM   32374 C  C   . GLY   S  5  32  ? 72.257  -214.038 27.237  1.00 129.74 ? 31  GLY   S C   1 
ATOM   32375 O  O   . GLY   S  5  32  ? 72.667  -214.926 28.014  1.00 135.20 ? 31  GLY   S O   1 
ATOM   32376 N  N   . SER   S  5  33  ? 73.047  -213.201 26.554  1.00 124.67 ? 32  SER   S N   1 
ATOM   32377 C  CA  . SER   S  5  33  ? 74.532  -213.180 26.618  1.00 126.67 ? 32  SER   S CA  1 
ATOM   32378 C  C   . SER   S  5  33  ? 74.972  -212.747 28.019  1.00 125.19 ? 32  SER   S C   1 
ATOM   32379 O  O   . SER   S  5  33  ? 74.301  -211.874 28.600  1.00 126.94 ? 32  SER   S O   1 
ATOM   32380 C  CB  . SER   S  5  33  ? 75.115  -212.283 25.558  1.00 127.38 ? 32  SER   S CB  1 
ATOM   32381 O  OG  . SER   S  5  33  ? 76.532  -212.302 25.607  1.00 131.45 ? 32  SER   S OG  1 
ATOM   32382 N  N   . VAL   S  5  34  ? 76.049  -213.344 28.537  1.00 127.63 ? 33  VAL   S N   1 
ATOM   32383 C  CA  . VAL   S  5  34  ? 76.546  -213.113 29.926  1.00 129.84 ? 33  VAL   S CA  1 
ATOM   32384 C  C   . VAL   S  5  34  ? 76.946  -211.641 30.071  1.00 126.45 ? 33  VAL   S C   1 
ATOM   32385 O  O   . VAL   S  5  34  ? 77.557  -211.088 29.133  1.00 125.45 ? 33  VAL   S O   1 
ATOM   32386 C  CB  . VAL   S  5  34  ? 77.707  -214.057 30.300  1.00 132.65 ? 33  VAL   S CB  1 
ATOM   32387 C  CG1 . VAL   S  5  34  ? 78.949  -213.838 29.445  1.00 134.60 ? 33  VAL   S CG1 1 
ATOM   32388 C  CG2 . VAL   S  5  34  ? 78.055  -213.955 31.778  1.00 135.51 ? 33  VAL   S CG2 1 
ATOM   32389 N  N   . THR   S  5  35  ? 76.575  -211.034 31.200  1.00 126.66 ? 34  THR   S N   1 
ATOM   32390 C  CA  . THR   S  5  35  ? 77.061  -209.708 31.660  1.00 128.17 ? 34  THR   S CA  1 
ATOM   32391 C  C   . THR   S  5  35  ? 77.422  -209.818 33.143  1.00 128.78 ? 34  THR   S C   1 
ATOM   32392 O  O   . THR   S  5  35  ? 76.736  -210.571 33.863  1.00 128.34 ? 34  THR   S O   1 
ATOM   32393 C  CB  . THR   S  5  35  ? 76.033  -208.603 31.380  1.00 126.52 ? 34  THR   S CB  1 
ATOM   32394 O  OG1 . THR   S  5  35  ? 76.611  -207.352 31.759  1.00 126.18 ? 34  THR   S OG1 1 
ATOM   32395 C  CG2 . THR   S  5  35  ? 74.721  -208.812 32.104  1.00 125.96 ? 34  THR   S CG2 1 
ATOM   32396 N  N   . VAL   S  5  36  ? 78.462  -209.095 33.563  1.00 130.69 ? 35  VAL   S N   1 
ATOM   32397 C  CA  . VAL   S  5  36  ? 79.030  -209.134 34.941  1.00 132.68 ? 35  VAL   S CA  1 
ATOM   32398 C  C   . VAL   S  5  36  ? 78.956  -207.727 35.540  1.00 131.19 ? 35  VAL   S C   1 
ATOM   32399 O  O   . VAL   S  5  36  ? 79.104  -206.748 34.781  1.00 133.68 ? 35  VAL   S O   1 
ATOM   32400 C  CB  . VAL   S  5  36  ? 80.476  -209.666 34.929  1.00 135.26 ? 35  VAL   S CB  1 
ATOM   32401 C  CG1 . VAL   S  5  36  ? 81.139  -209.560 36.295  1.00 136.37 ? 35  VAL   S CG1 1 
ATOM   32402 C  CG2 . VAL   S  5  36  ? 80.541  -211.096 34.416  1.00 136.62 ? 35  VAL   S CG2 1 
ATOM   32403 N  N   . GLY   S  5  37  ? 78.728  -207.653 36.854  1.00 132.58 ? 36  GLY   S N   1 
ATOM   32404 C  CA  . GLY   S  5  37  ? 78.808  -206.424 37.664  1.00 127.87 ? 36  GLY   S CA  1 
ATOM   32405 C  C   . GLY   S  5  37  ? 79.626  -206.669 38.919  1.00 125.87 ? 36  GLY   S C   1 
ATOM   32406 O  O   . GLY   S  5  37  ? 79.438  -207.730 39.543  1.00 121.19 ? 36  GLY   S O   1 
ATOM   32407 N  N   . LEU   S  5  38  ? 80.523  -205.743 39.263  1.00 125.77 ? 37  LEU   S N   1 
ATOM   32408 C  CA  . LEU   S  5  38  ? 81.314  -205.784 40.522  1.00 126.59 ? 37  LEU   S CA  1 
ATOM   32409 C  C   . LEU   S  5  38  ? 81.720  -204.359 40.912  1.00 126.35 ? 37  LEU   S C   1 
ATOM   32410 O  O   . LEU   S  5  38  ? 81.704  -203.475 40.030  1.00 125.99 ? 37  LEU   S O   1 
ATOM   32411 C  CB  . LEU   S  5  38  ? 82.525  -206.710 40.342  1.00 127.21 ? 37  LEU   S CB  1 
ATOM   32412 C  CG  . LEU   S  5  38  ? 83.771  -206.107 39.691  1.00 128.27 ? 37  LEU   S CG  1 
ATOM   32413 C  CD1 . LEU   S  5  38  ? 84.962  -207.039 39.861  1.00 129.91 ? 37  LEU   S CD1 1 
ATOM   32414 C  CD2 . LEU   S  5  38  ? 83.543  -205.805 38.218  1.00 127.26 ? 37  LEU   S CD2 1 
ATOM   32415 N  N   . ARG   S  5  39  ? 82.055  -204.146 42.187  1.00 126.60 ? 38  ARG   S N   1 
ATOM   32416 C  CA  . ARG   S  5  39  ? 82.392  -202.802 42.726  1.00 125.88 ? 38  ARG   S CA  1 
ATOM   32417 C  C   . ARG   S  5  39  ? 83.417  -202.907 43.857  1.00 130.50 ? 38  ARG   S C   1 
ATOM   32418 O  O   . ARG   S  5  39  ? 83.518  -203.978 44.487  1.00 134.09 ? 38  ARG   S O   1 
ATOM   32419 C  CB  . ARG   S  5  39  ? 81.130  -202.085 43.217  1.00 121.08 ? 38  ARG   S CB  1 
ATOM   32420 C  CG  . ARG   S  5  39  ? 80.584  -202.563 44.557  1.00 120.56 ? 38  ARG   S CG  1 
ATOM   32421 C  CD  . ARG   S  5  39  ? 79.784  -201.465 45.231  1.00 118.49 ? 38  ARG   S CD  1 
ATOM   32422 N  NE  . ARG   S  5  39  ? 79.273  -201.829 46.549  1.00 119.83 ? 38  ARG   S NE  1 
ATOM   32423 C  CZ  . ARG   S  5  39  ? 79.846  -201.530 47.717  1.00 120.05 ? 38  ARG   S CZ  1 
ATOM   32424 N  NH1 . ARG   S  5  39  ? 80.986  -200.859 47.772  1.00 120.98 ? 38  ARG   S NH1 1 
ATOM   32425 N  NH2 . ARG   S  5  39  ? 79.268  -201.912 48.843  1.00 118.27 ? 38  ARG   S NH2 1 
ATOM   32426 N  N   . SER   S  5  40  ? 84.135  -201.805 44.088  1.00 130.70 ? 39  SER   S N   1 
ATOM   32427 C  CA  . SER   S  5  40  ? 84.994  -201.550 45.272  1.00 134.72 ? 39  SER   S CA  1 
ATOM   32428 C  C   . SER   S  5  40  ? 84.251  -200.567 46.188  1.00 132.42 ? 39  SER   S C   1 
ATOM   32429 O  O   . SER   S  5  40  ? 83.005  -200.629 46.211  1.00 136.45 ? 39  SER   S O   1 
ATOM   32430 C  CB  . SER   S  5  40  ? 86.356  -201.052 44.842  1.00 134.71 ? 39  SER   S CB  1 
ATOM   32431 O  OG  . SER   S  5  40  ? 86.301  -199.703 44.403  1.00 135.32 ? 39  SER   S OG  1 
ATOM   32432 N  N   . ASN   S  5  41  ? 84.968  -199.704 46.913  1.00 133.10 ? 40  ASN   S N   1 
ATOM   32433 C  CA  . ASN   S  5  41  ? 84.375  -198.620 47.742  1.00 130.97 ? 40  ASN   S CA  1 
ATOM   32434 C  C   . ASN   S  5  41  ? 84.410  -197.293 46.971  1.00 126.88 ? 40  ASN   S C   1 
ATOM   32435 O  O   . ASN   S  5  41  ? 83.705  -196.361 47.404  1.00 124.89 ? 40  ASN   S O   1 
ATOM   32436 C  CB  . ASN   S  5  41  ? 85.068  -198.521 49.104  1.00 133.86 ? 40  ASN   S CB  1 
ATOM   32437 C  CG  . ASN   S  5  41  ? 84.645  -199.627 50.048  1.00 136.33 ? 40  ASN   S CG  1 
ATOM   32438 O  OD1 . ASN   S  5  41  ? 83.535  -199.601 50.575  1.00 138.59 ? 40  ASN   S OD1 1 
ATOM   32439 N  ND2 . ASN   S  5  41  ? 85.512  -200.605 50.263  1.00 139.37 ? 40  ASN   S ND2 1 
ATOM   32440 N  N   . THR   S  5  42  ? 85.172  -197.214 45.869  1.00 124.02 ? 41  THR   S N   1 
ATOM   32441 C  CA  . THR   S  5  42  ? 85.397  -195.969 45.079  1.00 124.31 ? 41  THR   S CA  1 
ATOM   32442 C  C   . THR   S  5  42  ? 84.744  -196.056 43.691  1.00 122.46 ? 41  THR   S C   1 
ATOM   32443 O  O   . THR   S  5  42  ? 84.261  -195.010 43.223  1.00 123.68 ? 41  THR   S O   1 
ATOM   32444 C  CB  . THR   S  5  42  ? 86.891  -195.643 44.953  1.00 125.45 ? 41  THR   S CB  1 
ATOM   32445 O  OG1 . THR   S  5  42  ? 87.538  -196.734 44.297  1.00 123.87 ? 41  THR   S OG1 1 
ATOM   32446 C  CG2 . THR   S  5  42  ? 87.549  -195.374 46.289  1.00 126.36 ? 41  THR   S CG2 1 
ATOM   32447 N  N   . HIS   S  5  43  ? 84.738  -197.231 43.050  1.00 122.09 ? 42  HIS   S N   1 
ATOM   32448 C  CA  . HIS   S  5  43  ? 84.230  -197.427 41.664  1.00 122.31 ? 42  HIS   S CA  1 
ATOM   32449 C  C   . HIS   S  5  43  ? 83.292  -198.638 41.586  1.00 121.67 ? 42  HIS   S C   1 
ATOM   32450 O  O   . HIS   S  5  43  ? 83.456  -199.574 42.392  1.00 124.19 ? 42  HIS   S O   1 
ATOM   32451 C  CB  . HIS   S  5  43  ? 85.397  -197.588 40.682  1.00 122.48 ? 42  HIS   S CB  1 
ATOM   32452 C  CG  . HIS   S  5  43  ? 86.274  -196.389 40.575  1.00 123.18 ? 42  HIS   S CG  1 
ATOM   32453 N  ND1 . HIS   S  5  43  ? 87.234  -196.095 41.520  1.00 124.85 ? 42  HIS   S ND1 1 
ATOM   32454 C  CD2 . HIS   S  5  43  ? 86.355  -195.426 39.633  1.00 124.60 ? 42  HIS   S CD2 1 
ATOM   32455 C  CE1 . HIS   S  5  43  ? 87.863  -194.992 41.172  1.00 125.49 ? 42  HIS   S CE1 1 
ATOM   32456 N  NE2 . HIS   S  5  43  ? 87.343  -194.563 40.017  1.00 126.61 ? 42  HIS   S NE2 1 
ATOM   32457 N  N   . ALA   S  5  44  ? 82.354  -198.606 40.634  1.00 117.90 ? 43  ALA   S N   1 
ATOM   32458 C  CA  . ALA   S  5  44  ? 81.479  -199.733 40.232  1.00 117.86 ? 43  ALA   S CA  1 
ATOM   32459 C  C   . ALA   S  5  44  ? 81.664  -199.985 38.732  1.00 117.55 ? 43  ALA   S C   1 
ATOM   32460 O  O   . ALA   S  5  44  ? 81.656  -199.003 37.965  1.00 113.79 ? 43  ALA   S O   1 
ATOM   32461 C  CB  . ALA   S  5  44  ? 80.042  -199.421 40.564  1.00 117.28 ? 43  ALA   S CB  1 
ATOM   32462 N  N   . VAL   S  5  45  ? 81.820  -201.251 38.335  1.00 119.54 ? 44  VAL   S N   1 
ATOM   32463 C  CA  . VAL   S  5  45  ? 82.198  -201.651 36.946  1.00 121.10 ? 44  VAL   S CA  1 
ATOM   32464 C  C   . VAL   S  5  45  ? 81.184  -202.667 36.411  1.00 119.79 ? 44  VAL   S C   1 
ATOM   32465 O  O   . VAL   S  5  45  ? 80.902  -203.653 37.119  1.00 121.49 ? 44  VAL   S O   1 
ATOM   32466 C  CB  . VAL   S  5  45  ? 83.634  -202.209 36.903  1.00 124.16 ? 44  VAL   S CB  1 
ATOM   32467 C  CG1 . VAL   S  5  45  ? 83.951  -202.887 35.578  1.00 125.17 ? 44  VAL   S CG1 1 
ATOM   32468 C  CG2 . VAL   S  5  45  ? 84.658  -201.126 37.202  1.00 126.33 ? 44  VAL   S CG2 1 
ATOM   32469 N  N   . LEU   S  5  46  ? 80.665  -202.417 35.205  1.00 117.70 ? 45  LEU   S N   1 
ATOM   32470 C  CA  . LEU   S  5  46  ? 79.938  -203.411 34.374  1.00 118.54 ? 45  LEU   S CA  1 
ATOM   32471 C  C   . LEU   S  5  46  ? 80.898  -203.962 33.315  1.00 124.79 ? 45  LEU   S C   1 
ATOM   32472 O  O   . LEU   S  5  46  ? 81.686  -203.166 32.763  1.00 126.11 ? 45  LEU   S O   1 
ATOM   32473 C  CB  . LEU   S  5  46  ? 78.736  -202.749 33.695  1.00 114.95 ? 45  LEU   S CB  1 
ATOM   32474 C  CG  . LEU   S  5  46  ? 77.593  -202.329 34.613  1.00 114.43 ? 45  LEU   S CG  1 
ATOM   32475 C  CD1 . LEU   S  5  46  ? 76.620  -201.432 33.863  1.00 116.52 ? 45  LEU   S CD1 1 
ATOM   32476 C  CD2 . LEU   S  5  46  ? 76.872  -203.540 35.184  1.00 113.65 ? 45  LEU   S CD2 1 
ATOM   32477 N  N   . VAL   S  5  47  ? 80.826  -205.271 33.058  1.00 127.39 ? 46  VAL   S N   1 
ATOM   32478 C  CA  . VAL   S  5  47  ? 81.482  -205.953 31.904  1.00 131.29 ? 46  VAL   S CA  1 
ATOM   32479 C  C   . VAL   S  5  47  ? 80.417  -206.817 31.224  1.00 130.99 ? 46  VAL   S C   1 
ATOM   32480 O  O   . VAL   S  5  47  ? 79.742  -207.581 31.940  1.00 128.76 ? 46  VAL   S O   1 
ATOM   32481 C  CB  . VAL   S  5  47  ? 82.700  -206.791 32.340  1.00 134.57 ? 46  VAL   S CB  1 
ATOM   32482 C  CG1 . VAL   S  5  47  ? 83.445  -207.366 31.143  1.00 136.19 ? 46  VAL   S CG1 1 
ATOM   32483 C  CG2 . VAL   S  5  47  ? 83.650  -205.993 33.220  1.00 136.57 ? 46  VAL   S CG2 1 
ATOM   32484 N  N   . ALA   S  5  48  ? 80.269  -206.687 29.904  1.00 134.78 ? 47  ALA   S N   1 
ATOM   32485 C  CA  . ALA   S  5  48  ? 79.238  -207.386 29.104  1.00 137.44 ? 47  ALA   S CA  1 
ATOM   32486 C  C   . ALA   S  5  48  ? 79.871  -208.038 27.871  1.00 145.23 ? 47  ALA   S C   1 
ATOM   32487 O  O   . ALA   S  5  48  ? 80.627  -207.352 27.152  1.00 146.08 ? 47  ALA   S O   1 
ATOM   32488 C  CB  . ALA   S  5  48  ? 78.150  -206.417 28.716  1.00 134.28 ? 47  ALA   S CB  1 
ATOM   32489 N  N   . LEU   S  5  49  ? 79.565  -209.321 27.651  1.00 150.12 ? 48  LEU   S N   1 
ATOM   32490 C  CA  . LEU   S  5  49  ? 79.841  -210.053 26.388  1.00 154.73 ? 48  LEU   S CA  1 
ATOM   32491 C  C   . LEU   S  5  49  ? 78.714  -209.710 25.409  1.00 153.14 ? 48  LEU   S C   1 
ATOM   32492 O  O   . LEU   S  5  49  ? 77.546  -209.997 25.738  1.00 149.99 ? 48  LEU   S O   1 
ATOM   32493 C  CB  . LEU   S  5  49  ? 79.909  -211.560 26.668  1.00 159.54 ? 48  LEU   S CB  1 
ATOM   32494 C  CG  . LEU   S  5  49  ? 80.219  -212.453 25.464  1.00 162.32 ? 48  LEU   S CG  1 
ATOM   32495 C  CD1 . LEU   S  5  49  ? 81.668  -212.300 25.029  1.00 167.08 ? 48  LEU   S CD1 1 
ATOM   32496 C  CD2 . LEU   S  5  49  ? 79.910  -213.913 25.768  1.00 162.50 ? 48  LEU   S CD2 1 
ATOM   32497 N  N   . LYS   S  5  50  ? 79.047  -209.087 24.276  1.00 154.12 ? 49  LYS   S N   1 
ATOM   32498 C  CA  . LYS   S  5  50  ? 78.068  -208.703 23.225  1.00 153.60 ? 49  LYS   S CA  1 
ATOM   32499 C  C   . LYS   S  5  50  ? 77.903  -209.862 22.235  1.00 151.14 ? 49  LYS   S C   1 
ATOM   32500 O  O   . LYS   S  5  50  ? 78.876  -210.615 22.027  1.00 152.02 ? 49  LYS   S O   1 
ATOM   32501 C  CB  . LYS   S  5  50  ? 78.512  -207.426 22.511  1.00 150.93 ? 49  LYS   S CB  1 
ATOM   32502 C  CG  . LYS   S  5  50  ? 78.353  -206.154 23.328  1.00 152.50 ? 49  LYS   S CG  1 
ATOM   32503 C  CD  . LYS   S  5  50  ? 78.663  -204.902 22.540  1.00 158.62 ? 49  LYS   S CD  1 
ATOM   32504 C  CE  . LYS   S  5  50  ? 80.146  -204.705 22.305  1.00 162.30 ? 49  LYS   S CE  1 
ATOM   32505 N  NZ  . LYS   S  5  50  ? 80.423  -203.435 21.594  1.00 162.54 ? 49  LYS   S NZ  1 
ATOM   32506 N  N   . ARG   S  5  51  ? 76.713  -209.974 21.639  1.00 150.12 ? 50  ARG   S N   1 
ATOM   32507 C  CA  . ARG   S  5  51  ? 76.303  -211.103 20.765  1.00 148.53 ? 50  ARG   S CA  1 
ATOM   32508 C  C   . ARG   S  5  51  ? 75.878  -210.557 19.400  1.00 149.76 ? 50  ARG   S C   1 
ATOM   32509 O  O   . ARG   S  5  51  ? 75.118  -209.570 19.369  1.00 150.45 ? 50  ARG   S O   1 
ATOM   32510 C  CB  . ARG   S  5  51  ? 75.162  -211.882 21.426  1.00 148.20 ? 50  ARG   S CB  1 
ATOM   32511 C  CG  . ARG   S  5  51  ? 74.715  -213.117 20.658  1.00 148.22 ? 50  ARG   S CG  1 
ATOM   32512 C  CD  . ARG   S  5  51  ? 73.605  -213.842 21.391  1.00 148.83 ? 50  ARG   S CD  1 
ATOM   32513 N  NE  . ARG   S  5  51  ? 74.099  -214.576 22.550  1.00 148.97 ? 50  ARG   S NE  1 
ATOM   32514 C  CZ  . ARG   S  5  51  ? 73.338  -215.079 23.520  1.00 151.77 ? 50  ARG   S CZ  1 
ATOM   32515 N  NH1 . ARG   S  5  51  ? 72.022  -214.933 23.493  1.00 150.03 ? 50  ARG   S NH1 1 
ATOM   32516 N  NH2 . ARG   S  5  51  ? 73.902  -215.729 24.525  1.00 150.24 ? 50  ARG   S NH2 1 
ATOM   32517 N  N   . ASN   S  5  52  ? 76.347  -211.195 18.324  1.00 157.39 ? 51  ASN   S N   1 
ATOM   32518 C  CA  . ASN   S  5  52  ? 76.033  -210.840 16.914  1.00 158.85 ? 51  ASN   S CA  1 
ATOM   32519 C  C   . ASN   S  5  52  ? 75.041  -211.865 16.348  1.00 164.46 ? 51  ASN   S C   1 
ATOM   32520 O  O   . ASN   S  5  52  ? 74.888  -212.944 16.962  1.00 169.59 ? 51  ASN   S O   1 
ATOM   32521 C  CB  . ASN   S  5  52  ? 77.306  -210.741 16.064  1.00 159.23 ? 51  ASN   S CB  1 
ATOM   32522 C  CG  . ASN   S  5  52  ? 78.092  -212.034 15.967  1.00 161.20 ? 51  ASN   S CG  1 
ATOM   32523 O  OD1 . ASN   S  5  52  ? 77.865  -212.975 16.727  1.00 155.66 ? 51  ASN   S OD1 1 
ATOM   32524 N  ND2 . ASN   S  5  52  ? 79.031  -212.088 15.036  1.00 159.48 ? 51  ASN   S ND2 1 
ATOM   32525 N  N   . ALA   S  5  53  ? 74.395  -211.531 15.226  1.00 162.14 ? 52  ALA   S N   1 
ATOM   32526 C  CA  . ALA   S  5  53  ? 73.507  -212.434 14.455  1.00 156.79 ? 52  ALA   S CA  1 
ATOM   32527 C  C   . ALA   S  5  53  ? 74.368  -213.359 13.585  1.00 154.85 ? 52  ALA   S C   1 
ATOM   32528 O  O   . ALA   S  5  53  ? 74.078  -214.569 13.547  1.00 150.59 ? 52  ALA   S O   1 
ATOM   32529 C  CB  . ALA   S  5  53  ? 72.538  -211.626 13.628  1.00 156.40 ? 52  ALA   S CB  1 
ATOM   32530 N  N   . ASP   S  5  54  ? 75.381  -212.795 12.916  1.00 154.96 ? 53  ASP   S N   1 
ATOM   32531 C  CA  . ASP   S  5  54  ? 76.434  -213.532 12.163  1.00 158.21 ? 53  ASP   S CA  1 
ATOM   32532 C  C   . ASP   S  5  54  ? 77.659  -212.615 12.004  1.00 159.28 ? 53  ASP   S C   1 
ATOM   32533 O  O   . ASP   S  5  54  ? 77.710  -211.582 12.700  1.00 154.42 ? 53  ASP   S O   1 
ATOM   32534 C  CB  . ASP   S  5  54  ? 75.878  -214.070 10.840  1.00 162.00 ? 53  ASP   S CB  1 
ATOM   32535 C  CG  . ASP   S  5  54  ? 75.296  -213.012 9.917   1.00 160.27 ? 53  ASP   S CG  1 
ATOM   32536 O  OD1 . ASP   S  5  54  ? 75.734  -211.848 9.998   1.00 157.16 ? 53  ASP   S OD1 1 
ATOM   32537 O  OD2 . ASP   S  5  54  ? 74.407  -213.365 9.118   1.00 161.68 ? 53  ASP   S OD2 1 
ATOM   32538 N  N   . GLU   S  5  55  ? 78.608  -212.977 11.130  1.00 162.49 ? 54  GLU   S N   1 
ATOM   32539 C  CA  . GLU   S  5  55  ? 79.892  -212.245 10.925  1.00 167.95 ? 54  GLU   S CA  1 
ATOM   32540 C  C   . GLU   S  5  55  ? 79.676  -210.969 10.099  1.00 164.38 ? 54  GLU   S C   1 
ATOM   32541 O  O   . GLU   S  5  55  ? 80.627  -210.166 10.019  1.00 163.17 ? 54  GLU   S O   1 
ATOM   32542 C  CB  . GLU   S  5  55  ? 80.940  -213.144 10.256  1.00 169.15 ? 54  GLU   S CB  1 
ATOM   32543 C  CG  . GLU   S  5  55  ? 82.194  -213.347 11.092  1.00 172.95 ? 54  GLU   S CG  1 
ATOM   32544 C  CD  . GLU   S  5  55  ? 81.955  -213.841 12.508  1.00 170.96 ? 54  GLU   S CD  1 
ATOM   32545 O  OE1 . GLU   S  5  55  ? 82.437  -213.182 13.451  1.00 171.91 ? 54  GLU   S OE1 1 
ATOM   32546 O  OE2 . GLU   S  5  55  ? 81.289  -214.883 12.665  1.00 172.86 ? 54  GLU   S OE2 1 
ATOM   32547 N  N   . LEU   S  5  56  ? 78.491  -210.786 9.506   1.00 164.66 ? 55  LEU   S N   1 
ATOM   32548 C  CA  . LEU   S  5  56  ? 78.131  -209.571 8.724   1.00 163.12 ? 55  LEU   S CA  1 
ATOM   32549 C  C   . LEU   S  5  56  ? 77.455  -208.529 9.628   1.00 161.74 ? 55  LEU   S C   1 
ATOM   32550 O  O   . LEU   S  5  56  ? 77.440  -207.346 9.227   1.00 158.15 ? 55  LEU   S O   1 
ATOM   32551 C  CB  . LEU   S  5  56  ? 77.222  -209.968 7.553   1.00 164.32 ? 55  LEU   S CB  1 
ATOM   32552 C  CG  . LEU   S  5  56  ? 77.893  -210.104 6.183   1.00 166.50 ? 55  LEU   S CG  1 
ATOM   32553 C  CD1 . LEU   S  5  56  ? 79.289  -210.706 6.279   1.00 169.11 ? 55  LEU   S CD1 1 
ATOM   32554 C  CD2 . LEU   S  5  56  ? 77.029  -210.932 5.244   1.00 166.84 ? 55  LEU   S CD2 1 
ATOM   32555 N  N   . SER   S  5  57  ? 76.934  -208.931 10.796  1.00 155.97 ? 56  SER   S N   1 
ATOM   32556 C  CA  . SER   S  5  57  ? 76.101  -208.076 11.688  1.00 151.88 ? 56  SER   S CA  1 
ATOM   32557 C  C   . SER   S  5  57  ? 76.959  -207.357 12.737  1.00 149.62 ? 56  SER   S C   1 
ATOM   32558 O  O   . SER   S  5  57  ? 78.092  -207.807 13.003  1.00 153.58 ? 56  SER   S O   1 
ATOM   32559 C  CB  . SER   S  5  57  ? 75.003  -208.870 12.354  1.00 144.91 ? 56  SER   S CB  1 
ATOM   32560 O  OG  . SER   S  5  57  ? 75.481  -209.542 13.510  1.00 140.05 ? 56  SER   S OG  1 
ATOM   32561 N  N   . SER   S  5  58  ? 76.408  -206.285 13.315  1.00 150.13 ? 57  SER   S N   1 
ATOM   32562 C  CA  . SER   S  5  58  ? 76.945  -205.569 14.501  1.00 148.59 ? 57  SER   S CA  1 
ATOM   32563 C  C   . SER   S  5  58  ? 76.773  -206.452 15.738  1.00 148.09 ? 57  SER   S C   1 
ATOM   32564 O  O   . SER   S  5  58  ? 76.122  -207.510 15.626  1.00 141.63 ? 57  SER   S O   1 
ATOM   32565 C  CB  . SER   S  5  58  ? 76.264  -204.240 14.698  1.00 147.65 ? 57  SER   S CB  1 
ATOM   32566 O  OG  . SER   S  5  58  ? 74.854  -204.400 14.786  1.00 146.10 ? 57  SER   S OG  1 
ATOM   32567 N  N   . TYR   S  5  59  ? 77.318  -206.011 16.874  1.00 146.84 ? 58  TYR   S N   1 
ATOM   32568 C  CA  . TYR   S  5  59  ? 77.223  -206.697 18.188  1.00 145.87 ? 58  TYR   S CA  1 
ATOM   32569 C  C   . TYR   S  5  59  ? 76.247  -205.928 19.087  1.00 147.65 ? 58  TYR   S C   1 
ATOM   32570 O  O   . TYR   S  5  59  ? 76.557  -204.782 19.478  1.00 146.24 ? 58  TYR   S O   1 
ATOM   32571 C  CB  . TYR   S  5  59  ? 78.617  -206.855 18.797  1.00 145.84 ? 58  TYR   S CB  1 
ATOM   32572 C  CG  . TYR   S  5  59  ? 79.412  -207.990 18.203  1.00 147.52 ? 58  TYR   S CG  1 
ATOM   32573 C  CD1 . TYR   S  5  59  ? 80.082  -207.840 16.999  1.00 149.14 ? 58  TYR   S CD1 1 
ATOM   32574 C  CD2 . TYR   S  5  59  ? 79.476  -209.224 18.831  1.00 145.85 ? 58  TYR   S CD2 1 
ATOM   32575 C  CE1 . TYR   S  5  59  ? 80.805  -208.882 16.440  1.00 148.68 ? 58  TYR   S CE1 1 
ATOM   32576 C  CE2 . TYR   S  5  59  ? 80.194  -210.276 18.286  1.00 145.34 ? 58  TYR   S CE2 1 
ATOM   32577 C  CZ  . TYR   S  5  59  ? 80.860  -210.105 17.086  1.00 144.50 ? 58  TYR   S CZ  1 
ATOM   32578 O  OH  . TYR   S  5  59  ? 81.568  -211.135 16.541  1.00 142.57 ? 58  TYR   S OH  1 
ATOM   32579 N  N   . GLN   S  5  60  ? 75.098  -206.549 19.381  1.00 148.75 ? 59  GLN   S N   1 
ATOM   32580 C  CA  . GLN   S  5  60  ? 73.996  -205.989 20.210  1.00 145.84 ? 59  GLN   S CA  1 
ATOM   32581 C  C   . GLN   S  5  60  ? 74.585  -205.310 21.452  1.00 144.95 ? 59  GLN   S C   1 
ATOM   32582 O  O   . GLN   S  5  60  ? 75.200  -206.022 22.271  1.00 147.19 ? 59  GLN   S O   1 
ATOM   32583 C  CB  . GLN   S  5  60  ? 73.025  -207.100 20.615  1.00 147.68 ? 59  GLN   S CB  1 
ATOM   32584 C  CG  . GLN   S  5  60  ? 71.755  -206.595 21.287  1.00 145.00 ? 59  GLN   S CG  1 
ATOM   32585 C  CD  . GLN   S  5  60  ? 70.695  -206.173 20.299  1.00 143.58 ? 59  GLN   S CD  1 
ATOM   32586 O  OE1 . GLN   S  5  60  ? 70.979  -205.840 19.149  1.00 141.89 ? 59  GLN   S OE1 1 
ATOM   32587 N  NE2 . GLN   S  5  60  ? 69.450  -206.184 20.746  1.00 142.64 ? 59  GLN   S NE2 1 
ATOM   32588 N  N   . LYS   S  5  61  ? 74.405  -203.990 21.573  1.00 138.91 ? 60  LYS   S N   1 
ATOM   32589 C  CA  . LYS   S  5  61  ? 74.900  -203.175 22.718  1.00 134.35 ? 60  LYS   S CA  1 
ATOM   32590 C  C   . LYS   S  5  61  ? 74.113  -203.548 23.980  1.00 132.30 ? 60  LYS   S C   1 
ATOM   32591 O  O   . LYS   S  5  61  ? 72.867  -203.553 23.925  1.00 131.41 ? 60  LYS   S O   1 
ATOM   32592 C  CB  . LYS   S  5  61  ? 74.821  -201.671 22.428  1.00 132.50 ? 60  LYS   S CB  1 
ATOM   32593 C  CG  . LYS   S  5  61  ? 73.521  -201.160 21.818  1.00 132.86 ? 60  LYS   S CG  1 
ATOM   32594 C  CD  . LYS   S  5  61  ? 73.594  -199.701 21.413  1.00 133.15 ? 60  LYS   S CD  1 
ATOM   32595 C  CE  . LYS   S  5  61  ? 73.320  -198.743 22.554  1.00 130.62 ? 60  LYS   S CE  1 
ATOM   32596 N  NZ  . LYS   S  5  61  ? 71.869  -198.609 22.822  1.00 129.40 ? 60  LYS   S NZ  1 
ATOM   32597 N  N   . LYS   S  5  62  ? 74.833  -203.843 25.067  1.00 132.29 ? 61  LYS   S N   1 
ATOM   32598 C  CA  . LYS   S  5  62  ? 74.298  -204.433 26.324  1.00 134.52 ? 61  LYS   S CA  1 
ATOM   32599 C  C   . LYS   S  5  62  ? 74.200  -203.365 27.422  1.00 127.36 ? 61  LYS   S C   1 
ATOM   32600 O  O   . LYS   S  5  62  ? 73.434  -203.587 28.378  1.00 122.25 ? 61  LYS   S O   1 
ATOM   32601 C  CB  . LYS   S  5  62  ? 75.205  -205.576 26.795  1.00 141.86 ? 61  LYS   S CB  1 
ATOM   32602 C  CG  . LYS   S  5  62  ? 75.415  -206.708 25.795  1.00 146.09 ? 61  LYS   S CG  1 
ATOM   32603 C  CD  . LYS   S  5  62  ? 74.393  -207.819 25.900  1.00 147.19 ? 61  LYS   S CD  1 
ATOM   32604 C  CE  . LYS   S  5  62  ? 74.672  -208.768 27.047  1.00 145.98 ? 61  LYS   S CE  1 
ATOM   32605 N  NZ  . LYS   S  5  62  ? 73.487  -209.597 27.366  1.00 143.49 ? 61  LYS   S NZ  1 
ATOM   32606 N  N   . ILE   S  5  63  ? 74.944  -202.260 27.299  1.00 124.51 ? 62  ILE   S N   1 
ATOM   32607 C  CA  . ILE   S  5  63  ? 75.100  -201.232 28.373  1.00 122.22 ? 62  ILE   S CA  1 
ATOM   32608 C  C   . ILE   S  5  63  ? 74.413  -199.930 27.942  1.00 117.00 ? 62  ILE   S C   1 
ATOM   32609 O  O   . ILE   S  5  63  ? 74.586  -199.519 26.776  1.00 113.56 ? 62  ILE   S O   1 
ATOM   32610 C  CB  . ILE   S  5  63  ? 76.589  -201.015 28.714  1.00 123.88 ? 62  ILE   S CB  1 
ATOM   32611 C  CG1 . ILE   S  5  63  ? 77.239  -202.302 29.233  1.00 125.19 ? 62  ILE   S CG1 1 
ATOM   32612 C  CG2 . ILE   S  5  63  ? 76.752  -199.865 29.699  1.00 123.78 ? 62  ILE   S CG2 1 
ATOM   32613 C  CD1 . ILE   S  5  63  ? 78.747  -202.248 29.315  1.00 125.60 ? 62  ILE   S CD1 1 
ATOM   32614 N  N   . ILE   S  5  64  ? 73.677  -199.307 28.870  1.00 113.05 ? 63  ILE   S N   1 
ATOM   32615 C  CA  . ILE   S  5  64  ? 72.921  -198.036 28.657  1.00 110.99 ? 63  ILE   S CA  1 
ATOM   32616 C  C   . ILE   S  5  64  ? 73.208  -197.087 29.826  1.00 111.14 ? 63  ILE   S C   1 
ATOM   32617 O  O   . ILE   S  5  64  ? 73.191  -197.547 30.986  1.00 106.75 ? 63  ILE   S O   1 
ATOM   32618 C  CB  . ILE   S  5  64  ? 71.409  -198.303 28.513  1.00 107.26 ? 63  ILE   S CB  1 
ATOM   32619 C  CG1 . ILE   S  5  64  ? 71.114  -199.380 27.464  1.00 107.32 ? 63  ILE   S CG1 1 
ATOM   32620 C  CG2 . ILE   S  5  64  ? 70.669  -197.008 28.216  1.00 104.00 ? 63  ILE   S CG2 1 
ATOM   32621 C  CD1 . ILE   S  5  64  ? 69.711  -199.940 27.526  1.00 105.30 ? 63  ILE   S CD1 1 
ATOM   32622 N  N   . LYS   S  5  65  ? 73.444  -195.809 29.514  1.00 112.78 ? 64  LYS   S N   1 
ATOM   32623 C  CA  . LYS   S  5  65  ? 73.633  -194.708 30.496  1.00 113.79 ? 64  LYS   S CA  1 
ATOM   32624 C  C   . LYS   S  5  65  ? 72.259  -194.160 30.904  1.00 113.93 ? 64  LYS   S C   1 
ATOM   32625 O  O   . LYS   S  5  65  ? 71.429  -193.930 30.002  1.00 117.02 ? 64  LYS   S O   1 
ATOM   32626 C  CB  . LYS   S  5  65  ? 74.500  -193.605 29.882  1.00 113.71 ? 64  LYS   S CB  1 
ATOM   32627 C  CG  . LYS   S  5  65  ? 74.824  -192.442 30.808  1.00 113.88 ? 64  LYS   S CG  1 
ATOM   32628 C  CD  . LYS   S  5  65  ? 75.796  -191.461 30.196  1.00 114.41 ? 64  LYS   S CD  1 
ATOM   32629 C  CE  . LYS   S  5  65  ? 75.976  -190.202 31.016  1.00 113.13 ? 64  LYS   S CE  1 
ATOM   32630 N  NZ  . LYS   S  5  65  ? 76.906  -189.260 30.351  1.00 112.44 ? 64  LYS   S NZ  1 
ATOM   32631 N  N   . CYS   S  5  66  ? 72.039  -193.950 32.207  1.00 114.37 ? 65  CYS   S N   1 
ATOM   32632 C  CA  . CYS   S  5  66  ? 70.761  -193.455 32.793  1.00 116.22 ? 65  CYS   S CA  1 
ATOM   32633 C  C   . CYS   S  5  66  ? 70.900  -191.994 33.234  1.00 116.16 ? 65  CYS   S C   1 
ATOM   32634 O  O   . CYS   S  5  66  ? 69.968  -191.204 32.975  1.00 116.83 ? 65  CYS   S O   1 
ATOM   32635 C  CB  . CYS   S  5  66  ? 70.330  -194.311 33.976  1.00 117.98 ? 65  CYS   S CB  1 
ATOM   32636 S  SG  . CYS   S  5  66  ? 69.662  -195.918 33.475  1.00 122.16 ? 65  CYS   S SG  1 
ATOM   32637 N  N   . ASP   S  5  67  ? 72.006  -191.663 33.906  1.00 114.39 ? 66  ASP   S N   1 
ATOM   32638 C  CA  . ASP   S  5  67  ? 72.375  -190.275 34.296  1.00 114.35 ? 66  ASP   S CA  1 
ATOM   32639 C  C   . ASP   S  5  67  ? 73.905  -190.169 34.277  1.00 110.29 ? 66  ASP   S C   1 
ATOM   32640 O  O   . ASP   S  5  67  ? 74.551  -191.119 33.797  1.00 103.69 ? 66  ASP   S O   1 
ATOM   32641 C  CB  . ASP   S  5  67  ? 71.754  -189.910 35.649  1.00 119.50 ? 66  ASP   S CB  1 
ATOM   32642 C  CG  . ASP   S  5  67  ? 71.493  -188.424 35.853  1.00 123.04 ? 66  ASP   S CG  1 
ATOM   32643 O  OD1 . ASP   S  5  67  ? 72.053  -187.612 35.084  1.00 128.49 ? 66  ASP   S OD1 1 
ATOM   32644 O  OD2 . ASP   S  5  67  ? 70.729  -188.085 36.779  1.00 124.23 ? 66  ASP   S OD2 1 
ATOM   32645 N  N   . GLU   S  5  68  ? 74.458  -189.054 34.763  1.00 111.92 ? 67  GLU   S N   1 
ATOM   32646 C  CA  . GLU   S  5  68  ? 75.924  -188.810 34.853  1.00 113.17 ? 67  GLU   S CA  1 
ATOM   32647 C  C   . GLU   S  5  68  ? 76.544  -189.730 35.912  1.00 110.52 ? 67  GLU   S C   1 
ATOM   32648 O  O   . GLU   S  5  68  ? 77.766  -189.968 35.836  1.00 110.06 ? 67  GLU   S O   1 
ATOM   32649 C  CB  . GLU   S  5  68  ? 76.206  -187.343 35.190  1.00 115.48 ? 67  GLU   S CB  1 
ATOM   32650 C  CG  . GLU   S  5  68  ? 75.774  -186.375 34.102  1.00 116.30 ? 67  GLU   S CG  1 
ATOM   32651 C  CD  . GLU   S  5  68  ? 76.396  -186.634 32.740  1.00 116.77 ? 67  GLU   S CD  1 
ATOM   32652 O  OE1 . GLU   S  5  68  ? 77.611  -186.914 32.688  1.00 112.82 ? 67  GLU   S OE1 1 
ATOM   32653 O  OE2 . GLU   S  5  68  ? 75.660  -186.571 31.734  1.00 123.20 ? 67  GLU   S OE2 1 
ATOM   32654 N  N   . HIS   S  5  69  ? 75.731  -190.229 36.851  1.00 108.30 ? 68  HIS   S N   1 
ATOM   32655 C  CA  . HIS   S  5  69  ? 76.173  -191.006 38.041  1.00 109.27 ? 68  HIS   S CA  1 
ATOM   32656 C  C   . HIS   S  5  69  ? 75.578  -192.424 38.061  1.00 109.70 ? 68  HIS   S C   1 
ATOM   32657 O  O   . HIS   S  5  69  ? 75.844  -193.141 39.046  1.00 109.91 ? 68  HIS   S O   1 
ATOM   32658 C  CB  . HIS   S  5  69  ? 75.792  -190.246 39.318  1.00 107.66 ? 68  HIS   S CB  1 
ATOM   32659 C  CG  . HIS   S  5  69  ? 74.324  -190.233 39.573  1.00 103.89 ? 68  HIS   S CG  1 
ATOM   32660 N  ND1 . HIS   S  5  69  ? 73.735  -191.047 40.519  1.00 100.73 ? 68  HIS   S ND1 1 
ATOM   32661 C  CD2 . HIS   S  5  69  ? 73.322  -189.540 38.990  1.00 102.62 ? 68  HIS   S CD2 1 
ATOM   32662 C  CE1 . HIS   S  5  69  ? 72.436  -190.841 40.519  1.00 99.20  ? 68  HIS   S CE1 1 
ATOM   32663 N  NE2 . HIS   S  5  69  ? 72.155  -189.924 39.589  1.00 100.15 ? 68  HIS   S NE2 1 
ATOM   32664 N  N   . MET   S  5  70  ? 74.802  -192.822 37.044  1.00 108.86 ? 69  MET   S N   1 
ATOM   32665 C  CA  . MET   S  5  70  ? 74.071  -194.120 37.032  1.00 108.49 ? 69  MET   S CA  1 
ATOM   32666 C  C   . MET   S  5  70  ? 73.963  -194.670 35.604  1.00 110.18 ? 69  MET   S C   1 
ATOM   32667 O  O   . MET   S  5  70  ? 73.987  -193.872 34.649  1.00 106.42 ? 69  MET   S O   1 
ATOM   32668 C  CB  . MET   S  5  70  ? 72.664  -193.950 37.612  1.00 108.09 ? 69  MET   S CB  1 
ATOM   32669 C  CG  . MET   S  5  70  ? 72.101  -195.222 38.214  1.00 109.07 ? 69  MET   S CG  1 
ATOM   32670 S  SD  . MET   S  5  70  ? 70.361  -195.052 38.684  1.00 112.86 ? 69  MET   S SD  1 
ATOM   32671 C  CE  . MET   S  5  70  ? 70.486  -193.826 39.986  1.00 112.01 ? 69  MET   S CE  1 
ATOM   32672 N  N   . GLY   S  5  71  ? 73.844  -195.997 35.488  1.00 111.78 ? 70  GLY   S N   1 
ATOM   32673 C  CA  . GLY   S  5  71  ? 73.598  -196.738 34.233  1.00 112.56 ? 70  GLY   S CA  1 
ATOM   32674 C  C   . GLY   S  5  71  ? 73.464  -198.226 34.507  1.00 112.70 ? 70  GLY   S C   1 
ATOM   32675 O  O   . GLY   S  5  71  ? 73.744  -198.628 35.656  1.00 111.33 ? 70  GLY   S O   1 
ATOM   32676 N  N   . LEU   S  5  72  ? 73.050  -199.026 33.516  1.00 113.00 ? 71  LEU   S N   1 
ATOM   32677 C  CA  . LEU   S  5  72  ? 72.889  -200.495 33.703  1.00 113.96 ? 71  LEU   S CA  1 
ATOM   32678 C  C   . LEU   S  5  72  ? 73.394  -201.284 32.489  1.00 112.16 ? 71  LEU   S C   1 
ATOM   32679 O  O   . LEU   S  5  72  ? 73.695  -200.668 31.447  1.00 110.03 ? 71  LEU   S O   1 
ATOM   32680 C  CB  . LEU   S  5  72  ? 71.430  -200.831 34.056  1.00 114.15 ? 71  LEU   S CB  1 
ATOM   32681 C  CG  . LEU   S  5  72  ? 70.311  -200.621 33.024  1.00 113.14 ? 71  LEU   S CG  1 
ATOM   32682 C  CD1 . LEU   S  5  72  ? 69.568  -199.321 33.273  1.00 111.49 ? 71  LEU   S CD1 1 
ATOM   32683 C  CD2 . LEU   S  5  72  ? 70.769  -200.698 31.575  1.00 115.48 ? 71  LEU   S CD2 1 
ATOM   32684 N  N   . SER   S  5  73  ? 73.519  -202.603 32.665  1.00 115.50 ? 72  SER   S N   1 
ATOM   32685 C  CA  . SER   S  5  73  ? 73.724  -203.610 31.591  1.00 116.94 ? 72  SER   S CA  1 
ATOM   32686 C  C   . SER   S  5  73  ? 72.490  -204.515 31.537  1.00 115.11 ? 72  SER   S C   1 
ATOM   32687 O  O   . SER   S  5  73  ? 71.795  -204.623 32.570  1.00 106.74 ? 72  SER   S O   1 
ATOM   32688 C  CB  . SER   S  5  73  ? 74.996  -204.398 31.796  1.00 120.72 ? 72  SER   S CB  1 
ATOM   32689 O  OG  . SER   S  5  73  ? 74.839  -205.384 32.808  1.00 122.26 ? 72  SER   S OG  1 
ATOM   32690 N  N   . LEU   S  5  74  ? 72.230  -205.128 30.378  1.00 117.18 ? 73  LEU   S N   1 
ATOM   32691 C  CA  . LEU   S  5  74  ? 70.996  -205.913 30.108  1.00 117.22 ? 73  LEU   S CA  1 
ATOM   32692 C  C   . LEU   S  5  74  ? 71.357  -207.330 29.648  1.00 119.16 ? 73  LEU   S C   1 
ATOM   32693 O  O   . LEU   S  5  74  ? 72.427  -207.513 29.029  1.00 122.14 ? 73  LEU   S O   1 
ATOM   32694 C  CB  . LEU   S  5  74  ? 70.153  -205.182 29.056  1.00 117.62 ? 73  LEU   S CB  1 
ATOM   32695 C  CG  . LEU   S  5  74  ? 70.732  -205.138 27.640  1.00 119.39 ? 73  LEU   S CG  1 
ATOM   32696 C  CD1 . LEU   S  5  74  ? 70.099  -206.199 26.752  1.00 121.36 ? 73  LEU   S CD1 1 
ATOM   32697 C  CD2 . LEU   S  5  74  ? 70.546  -203.760 27.022  1.00 118.50 ? 73  LEU   S CD2 1 
ATOM   32698 N  N   . ALA   S  5  75  ? 70.478  -208.283 29.959  1.00 114.35 ? 74  ALA   S N   1 
ATOM   32699 C  CA  . ALA   S  5  75  ? 70.483  -209.670 29.448  1.00 114.06 ? 74  ALA   S CA  1 
ATOM   32700 C  C   . ALA   S  5  75  ? 69.027  -210.098 29.259  1.00 109.43 ? 74  ALA   S C   1 
ATOM   32701 O  O   . ALA   S  5  75  ? 68.281  -210.081 30.256  1.00 109.24 ? 74  ALA   S O   1 
ATOM   32702 C  CB  . ALA   S  5  75  ? 71.225  -210.571 30.405  1.00 117.09 ? 74  ALA   S CB  1 
ATOM   32703 N  N   . GLY   S  5  76  ? 68.637  -210.409 28.020  1.00 110.58 ? 75  GLY   S N   1 
ATOM   32704 C  CA  . GLY   S  5  76  ? 67.270  -210.829 27.654  1.00 113.76 ? 75  GLY   S CA  1 
ATOM   32705 C  C   . GLY   S  5  76  ? 66.704  -209.952 26.552  1.00 111.78 ? 75  GLY   S C   1 
ATOM   32706 O  O   . GLY   S  5  76  ? 67.498  -209.495 25.704  1.00 114.15 ? 75  GLY   S O   1 
ATOM   32707 N  N   . LEU   S  5  77  ? 65.387  -209.717 26.564  1.00 113.38 ? 76  LEU   S N   1 
ATOM   32708 C  CA  . LEU   S  5  77  ? 64.683  -208.875 25.556  1.00 114.23 ? 76  LEU   S CA  1 
ATOM   32709 C  C   . LEU   S  5  77  ? 65.218  -207.442 25.640  1.00 112.88 ? 76  LEU   S C   1 
ATOM   32710 O  O   . LEU   S  5  77  ? 64.964  -206.778 26.661  1.00 112.90 ? 76  LEU   S O   1 
ATOM   32711 C  CB  . LEU   S  5  77  ? 63.169  -208.903 25.801  1.00 116.22 ? 76  LEU   S CB  1 
ATOM   32712 C  CG  . LEU   S  5  77  ? 62.379  -209.971 25.045  1.00 119.35 ? 76  LEU   S CG  1 
ATOM   32713 C  CD1 . LEU   S  5  77  ? 60.912  -209.923 25.446  1.00 119.66 ? 76  LEU   S CD1 1 
ATOM   32714 C  CD2 . LEU   S  5  77  ? 62.518  -209.803 23.538  1.00 120.89 ? 76  LEU   S CD2 1 
ATOM   32715 N  N   . ALA   S  5  78  ? 65.924  -206.990 24.599  1.00 114.11 ? 77  ALA   S N   1 
ATOM   32716 C  CA  . ALA   S  5  78  ? 66.592  -205.667 24.536  1.00 113.50 ? 77  ALA   S CA  1 
ATOM   32717 C  C   . ALA   S  5  78  ? 65.565  -204.535 24.481  1.00 111.77 ? 77  ALA   S C   1 
ATOM   32718 O  O   . ALA   S  5  78  ? 65.780  -203.497 25.103  1.00 110.14 ? 77  ALA   S O   1 
ATOM   32719 C  CB  . ALA   S  5  78  ? 67.542  -205.619 23.365  1.00 115.89 ? 77  ALA   S CB  1 
ATOM   32720 N  N   . PRO   S  5  79  ? 64.433  -204.664 23.746  1.00 110.69 ? 78  PRO   S N   1 
ATOM   32721 C  CA  . PRO   S  5  79  ? 63.405  -203.621 23.743  1.00 109.10 ? 78  PRO   S CA  1 
ATOM   32722 C  C   . PRO   S  5  79  ? 62.820  -203.331 25.134  1.00 107.81 ? 78  PRO   S C   1 
ATOM   32723 O  O   . PRO   S  5  79  ? 62.514  -202.190 25.402  1.00 110.39 ? 78  PRO   S O   1 
ATOM   32724 C  CB  . PRO   S  5  79  ? 62.305  -204.178 22.829  1.00 109.34 ? 78  PRO   S CB  1 
ATOM   32725 C  CG  . PRO   S  5  79  ? 63.021  -205.184 21.956  1.00 112.04 ? 78  PRO   S CG  1 
ATOM   32726 C  CD  . PRO   S  5  79  ? 64.088  -205.781 22.851  1.00 112.21 ? 78  PRO   S CD  1 
ATOM   32727 N  N   . ASP   S  5  80  ? 62.671  -204.365 25.968  1.00 108.30 ? 79  ASP   S N   1 
ATOM   32728 C  CA  . ASP   S  5  80  ? 62.171  -204.255 27.366  1.00 105.04 ? 79  ASP   S CA  1 
ATOM   32729 C  C   . ASP   S  5  80  ? 63.184  -203.466 28.207  1.00 99.31  ? 79  ASP   S C   1 
ATOM   32730 O  O   . ASP   S  5  80  ? 62.741  -202.708 29.089  1.00 94.64  ? 79  ASP   S O   1 
ATOM   32731 C  CB  . ASP   S  5  80  ? 61.879  -205.636 27.964  1.00 106.59 ? 79  ASP   S CB  1 
ATOM   32732 C  CG  . ASP   S  5  80  ? 60.636  -206.308 27.401  1.00 107.25 ? 79  ASP   S CG  1 
ATOM   32733 O  OD1 . ASP   S  5  80  ? 60.019  -205.736 26.476  1.00 107.31 ? 79  ASP   S OD1 1 
ATOM   32734 O  OD2 . ASP   S  5  80  ? 60.291  -207.400 27.894  1.00 106.01 ? 79  ASP   S OD2 1 
ATOM   32735 N  N   . ALA   S  5  81  ? 64.485  -203.641 27.947  1.00 100.17 ? 80  ALA   S N   1 
ATOM   32736 C  CA  . ALA   S  5  81  ? 65.589  -202.920 28.628  1.00 102.77 ? 80  ALA   S CA  1 
ATOM   32737 C  C   . ALA   S  5  81  ? 65.544  -201.442 28.233  1.00 100.85 ? 80  ALA   S C   1 
ATOM   32738 O  O   . ALA   S  5  81  ? 65.847  -200.590 29.090  1.00 101.04 ? 80  ALA   S O   1 
ATOM   32739 C  CB  . ALA   S  5  81  ? 66.924  -203.533 28.280  1.00 104.99 ? 80  ALA   S CB  1 
ATOM   32740 N  N   . ARG   S  5  82  ? 65.185  -201.161 26.978  1.00 102.18 ? 81  ARG   S N   1 
ATOM   32741 C  CA  . ARG   S  5  82  ? 65.042  -199.783 26.441  1.00 102.23 ? 81  ARG   S CA  1 
ATOM   32742 C  C   . ARG   S  5  82  ? 63.887  -199.069 27.158  1.00 102.46 ? 81  ARG   S C   1 
ATOM   32743 O  O   . ARG   S  5  82  ? 64.051  -197.872 27.475  1.00 103.66 ? 81  ARG   S O   1 
ATOM   32744 C  CB  . ARG   S  5  82  ? 64.836  -199.808 24.924  1.00 105.38 ? 81  ARG   S CB  1 
ATOM   32745 C  CG  . ARG   S  5  82  ? 64.486  -198.451 24.335  1.00 105.93 ? 81  ARG   S CG  1 
ATOM   32746 C  CD  . ARG   S  5  82  ? 64.718  -198.386 22.840  1.00 108.99 ? 81  ARG   S CD  1 
ATOM   32747 N  NE  . ARG   S  5  82  ? 64.036  -197.247 22.243  1.00 109.24 ? 81  ARG   S NE  1 
ATOM   32748 C  CZ  . ARG   S  5  82  ? 64.408  -195.974 22.375  1.00 109.91 ? 81  ARG   S CZ  1 
ATOM   32749 N  NH1 . ARG   S  5  82  ? 65.469  -195.646 23.096  1.00 110.70 ? 81  ARG   S NH1 1 
ATOM   32750 N  NH2 . ARG   S  5  82  ? 63.705  -195.024 21.783  1.00 110.16 ? 81  ARG   S NH2 1 
ATOM   32751 N  N   . VAL   S  5  83  ? 62.770  -199.768 27.401  1.00 97.12  ? 82  VAL   S N   1 
ATOM   32752 C  CA  . VAL   S  5  83  ? 61.588  -199.226 28.140  1.00 94.88  ? 82  VAL   S CA  1 
ATOM   32753 C  C   . VAL   S  5  83  ? 62.005  -198.916 29.582  1.00 96.12  ? 82  VAL   S C   1 
ATOM   32754 O  O   . VAL   S  5  83  ? 61.740  -197.790 30.039  1.00 97.62  ? 82  VAL   S O   1 
ATOM   32755 C  CB  . VAL   S  5  83  ? 60.386  -200.190 28.108  1.00 92.95  ? 82  VAL   S CB  1 
ATOM   32756 C  CG1 . VAL   S  5  83  ? 59.276  -199.756 29.056  1.00 91.51  ? 82  VAL   S CG1 1 
ATOM   32757 C  CG2 . VAL   S  5  83  ? 59.838  -200.359 26.701  1.00 94.02  ? 82  VAL   S CG2 1 
ATOM   32758 N  N   . LEU   S  5  84  ? 62.626  -199.881 30.266  1.00 95.94  ? 83  LEU   S N   1 
ATOM   32759 C  CA  . LEU   S  5  84  ? 62.985  -199.784 31.707  1.00 98.66  ? 83  LEU   S CA  1 
ATOM   32760 C  C   . LEU   S  5  84  ? 64.103  -198.752 31.916  1.00 96.66  ? 83  LEU   S C   1 
ATOM   32761 O  O   . LEU   S  5  84  ? 64.053  -198.053 32.947  1.00 92.93  ? 83  LEU   S O   1 
ATOM   32762 C  CB  . LEU   S  5  84  ? 63.396  -201.166 32.230  1.00 100.33 ? 83  LEU   S CB  1 
ATOM   32763 C  CG  . LEU   S  5  84  ? 62.254  -202.162 32.436  1.00 102.59 ? 83  LEU   S CG  1 
ATOM   32764 C  CD1 . LEU   S  5  84  ? 62.794  -203.552 32.735  1.00 104.02 ? 83  LEU   S CD1 1 
ATOM   32765 C  CD2 . LEU   S  5  84  ? 61.318  -201.708 33.548  1.00 103.89 ? 83  LEU   S CD2 1 
ATOM   32766 N  N   . SER   S  5  85  ? 65.074  -198.665 30.997  1.00 99.84  ? 84  SER   S N   1 
ATOM   32767 C  CA  . SER   S  5  85  ? 66.179  -197.668 31.043  1.00 101.54 ? 84  SER   S CA  1 
ATOM   32768 C  C   . SER   S  5  85  ? 65.602  -196.262 30.858  1.00 101.60 ? 84  SER   S C   1 
ATOM   32769 O  O   . SER   S  5  85  ? 65.988  -195.361 31.624  1.00 101.89 ? 84  SER   S O   1 
ATOM   32770 C  CB  . SER   S  5  85  ? 67.248  -197.948 30.019  1.00 104.99 ? 84  SER   S CB  1 
ATOM   32771 O  OG  . SER   S  5  85  ? 66.704  -197.953 28.709  1.00 107.68 ? 84  SER   S OG  1 
ATOM   32772 N  N   . ASN   S  5  86  ? 64.713  -196.096 29.873  1.00 102.47 ? 85  ASN   S N   1 
ATOM   32773 C  CA  . ASN   S  5  86  ? 64.021  -194.817 29.564  1.00 102.39 ? 85  ASN   S CA  1 
ATOM   32774 C  C   . ASN   S  5  86  ? 63.233  -194.341 30.791  1.00 101.48 ? 85  ASN   S C   1 
ATOM   32775 O  O   . ASN   S  5  86  ? 63.220  -193.123 31.037  1.00 102.20 ? 85  ASN   S O   1 
ATOM   32776 C  CB  . ASN   S  5  86  ? 63.089  -194.941 28.359  1.00 103.64 ? 85  ASN   S CB  1 
ATOM   32777 C  CG  . ASN   S  5  86  ? 62.587  -193.595 27.884  1.00 103.38 ? 85  ASN   S CG  1 
ATOM   32778 O  OD1 . ASN   S  5  86  ? 61.511  -193.158 28.283  1.00 102.30 ? 85  ASN   S OD1 1 
ATOM   32779 N  ND2 . ASN   S  5  86  ? 63.374  -192.921 27.060  1.00 103.80 ? 85  ASN   S ND2 1 
ATOM   32780 N  N   . TYR   S  5  87  ? 62.589  -195.262 31.514  1.00 100.17 ? 86  TYR   S N   1 
ATOM   32781 C  CA  . TYR   S  5  87  ? 61.848  -194.975 32.771  1.00 100.09 ? 86  TYR   S CA  1 
ATOM   32782 C  C   . TYR   S  5  87  ? 62.823  -194.454 33.833  1.00 99.18  ? 86  TYR   S C   1 
ATOM   32783 O  O   . TYR   S  5  87  ? 62.501  -193.445 34.481  1.00 98.95  ? 86  TYR   S O   1 
ATOM   32784 C  CB  . TYR   S  5  87  ? 61.107  -196.212 33.281  1.00 100.57 ? 86  TYR   S CB  1 
ATOM   32785 C  CG  . TYR   S  5  87  ? 60.423  -196.006 34.608  1.00 100.56 ? 86  TYR   S CG  1 
ATOM   32786 C  CD1 . TYR   S  5  87  ? 59.295  -195.209 34.713  1.00 99.19  ? 86  TYR   S CD1 1 
ATOM   32787 C  CD2 . TYR   S  5  87  ? 60.915  -196.588 35.766  1.00 102.27 ? 86  TYR   S CD2 1 
ATOM   32788 C  CE1 . TYR   S  5  87  ? 58.663  -195.007 35.929  1.00 98.20  ? 86  TYR   S CE1 1 
ATOM   32789 C  CE2 . TYR   S  5  87  ? 60.296  -196.396 36.990  1.00 100.23 ? 86  TYR   S CE2 1 
ATOM   32790 C  CZ  . TYR   S  5  87  ? 59.167  -195.602 37.072  1.00 96.93  ? 86  TYR   S CZ  1 
ATOM   32791 O  OH  . TYR   S  5  87  ? 58.559  -195.416 38.278  1.00 98.50  ? 86  TYR   S OH  1 
ATOM   32792 N  N   . LEU   S  5  88  ? 63.968  -195.126 34.005  1.00 101.42 ? 87  LEU   S N   1 
ATOM   32793 C  CA  . LEU   S  5  88  ? 65.036  -194.728 34.967  1.00 100.31 ? 87  LEU   S CA  1 
ATOM   32794 C  C   . LEU   S  5  88  ? 65.586  -193.346 34.604  1.00 98.93  ? 87  LEU   S C   1 
ATOM   32795 O  O   . LEU   S  5  88  ? 65.828  -192.555 35.533  1.00 99.16  ? 87  LEU   S O   1 
ATOM   32796 C  CB  . LEU   S  5  88  ? 66.170  -195.759 34.974  1.00 103.03 ? 87  LEU   S CB  1 
ATOM   32797 C  CG  . LEU   S  5  88  ? 66.340  -196.545 36.273  1.00 105.18 ? 87  LEU   S CG  1 
ATOM   32798 C  CD1 . LEU   S  5  88  ? 67.531  -197.486 36.177  1.00 109.40 ? 87  LEU   S CD1 1 
ATOM   32799 C  CD2 . LEU   S  5  88  ? 66.502  -195.615 37.467  1.00 103.06 ? 87  LEU   S CD2 1 
ATOM   32800 N  N   . ARG   S  5  89  ? 65.808  -193.082 33.313  1.00 97.02  ? 88  ARG   S N   1 
ATOM   32801 C  CA  . ARG   S  5  89  ? 66.326  -191.779 32.816  1.00 97.39  ? 88  ARG   S CA  1 
ATOM   32802 C  C   . ARG   S  5  89  ? 65.389  -190.654 33.272  1.00 95.90  ? 88  ARG   S C   1 
ATOM   32803 O  O   . ARG   S  5  89  ? 65.907  -189.624 33.745  1.00 96.10  ? 88  ARG   S O   1 
ATOM   32804 C  CB  . ARG   S  5  89  ? 66.487  -191.795 31.293  1.00 97.35  ? 88  ARG   S CB  1 
ATOM   32805 C  CG  . ARG   S  5  89  ? 67.734  -192.521 30.812  1.00 97.86  ? 88  ARG   S CG  1 
ATOM   32806 C  CD  . ARG   S  5  89  ? 67.747  -192.672 29.306  1.00 97.72  ? 88  ARG   S CD  1 
ATOM   32807 N  NE  . ARG   S  5  89  ? 69.032  -193.131 28.796  1.00 97.67  ? 88  ARG   S NE  1 
ATOM   32808 C  CZ  . ARG   S  5  89  ? 69.296  -193.364 27.513  1.00 98.53  ? 88  ARG   S CZ  1 
ATOM   32809 N  NH1 . ARG   S  5  89  ? 68.360  -193.186 26.594  1.00 97.46  ? 88  ARG   S NH1 1 
ATOM   32810 N  NH2 . ARG   S  5  89  ? 70.499  -193.776 27.151  1.00 99.60  ? 88  ARG   S NH2 1 
ATOM   32811 N  N   . GLN   S  5  90  ? 64.072  -190.859 33.151  1.00 94.99  ? 89  GLN   S N   1 
ATOM   32812 C  CA  . GLN   S  5  90  ? 63.020  -189.888 33.564  1.00 95.67  ? 89  GLN   S CA  1 
ATOM   32813 C  C   . GLN   S  5  90  ? 63.033  -189.710 35.088  1.00 96.16  ? 89  GLN   S C   1 
ATOM   32814 O  O   . GLN   S  5  90  ? 62.959  -188.553 35.543  1.00 96.40  ? 89  GLN   S O   1 
ATOM   32815 C  CB  . GLN   S  5  90  ? 61.640  -190.343 33.086  1.00 96.46  ? 89  GLN   S CB  1 
ATOM   32816 C  CG  . GLN   S  5  90  ? 61.408  -190.109 31.601  1.00 98.92  ? 89  GLN   S CG  1 
ATOM   32817 C  CD  . GLN   S  5  90  ? 60.182  -190.824 31.090  1.00 102.81 ? 89  GLN   S CD  1 
ATOM   32818 O  OE1 . GLN   S  5  90  ? 59.448  -191.458 31.845  1.00 106.93 ? 89  GLN   S OE1 1 
ATOM   32819 N  NE2 . GLN   S  5  90  ? 59.952  -190.726 29.790  1.00 106.51 ? 89  GLN   S NE2 1 
ATOM   32820 N  N   . GLN   S  5  91  ? 63.117  -190.806 35.849  1.00 95.65  ? 90  GLN   S N   1 
ATOM   32821 C  CA  . GLN   S  5  91  ? 63.093  -190.786 37.339  1.00 95.41  ? 90  GLN   S CA  1 
ATOM   32822 C  C   . GLN   S  5  91  ? 64.333  -190.056 37.873  1.00 98.50  ? 90  GLN   S C   1 
ATOM   32823 O  O   . GLN   S  5  91  ? 64.169  -189.222 38.791  1.00 98.45  ? 90  GLN   S O   1 
ATOM   32824 C  CB  . GLN   S  5  91  ? 62.997  -192.204 37.904  1.00 95.19  ? 90  GLN   S CB  1 
ATOM   32825 C  CG  . GLN   S  5  91  ? 61.628  -192.844 37.717  1.00 94.35  ? 90  GLN   S CG  1 
ATOM   32826 C  CD  . GLN   S  5  91  ? 60.507  -191.969 38.224  1.00 93.40  ? 90  GLN   S CD  1 
ATOM   32827 O  OE1 . GLN   S  5  91  ? 60.518  -191.513 39.365  1.00 89.89  ? 90  GLN   S OE1 1 
ATOM   32828 N  NE2 . GLN   S  5  91  ? 59.529  -191.718 37.369  1.00 96.00  ? 90  GLN   S NE2 1 
ATOM   32829 N  N   . CYS   S  5  92  ? 65.518  -190.359 37.328  1.00 97.69  ? 91  CYS   S N   1 
ATOM   32830 C  CA  . CYS   S  5  92  ? 66.794  -189.645 37.615  1.00 101.01 ? 91  CYS   S CA  1 
ATOM   32831 C  C   . CYS   S  5  92  ? 66.637  -188.157 37.291  1.00 100.19 ? 91  CYS   S C   1 
ATOM   32832 O  O   . CYS   S  5  92  ? 67.137  -187.321 38.069  1.00 101.80 ? 91  CYS   S O   1 
ATOM   32833 C  CB  . CYS   S  5  92  ? 67.955  -190.185 36.789  1.00 103.95 ? 91  CYS   S CB  1 
ATOM   32834 S  SG  . CYS   S  5  92  ? 68.635  -191.741 37.416  1.00 106.33 ? 91  CYS   S SG  1 
ATOM   32835 N  N   . ASN   S  5  93  ? 65.979  -187.864 36.167  1.00 101.24 ? 92  ASN   S N   1 
ATOM   32836 C  CA  . ASN   S  5  93  ? 65.807  -186.496 35.617  1.00 100.59 ? 92  ASN   S CA  1 
ATOM   32837 C  C   . ASN   S  5  93  ? 64.835  -185.708 36.501  1.00 99.84  ? 92  ASN   S C   1 
ATOM   32838 O  O   . ASN   S  5  93  ? 65.159  -184.556 36.838  1.00 99.14  ? 92  ASN   S O   1 
ATOM   32839 C  CB  . ASN   S  5  93  ? 65.342  -186.542 34.160  1.00 101.52 ? 92  ASN   S CB  1 
ATOM   32840 C  CG  . ASN   S  5  93  ? 65.607  -185.257 33.411  1.00 104.51 ? 92  ASN   S CG  1 
ATOM   32841 O  OD1 . ASN   S  5  93  ? 64.849  -184.896 32.515  1.00 103.43 ? 92  ASN   S OD1 1 
ATOM   32842 N  ND2 . ASN   S  5  93  ? 66.676  -184.562 33.770  1.00 108.69 ? 92  ASN   S ND2 1 
ATOM   32843 N  N   . TYR   S  5  94  ? 63.692  -186.305 36.853  1.00 96.21  ? 93  TYR   S N   1 
ATOM   32844 C  CA  . TYR   S  5  94  ? 62.662  -185.705 37.742  1.00 96.12  ? 93  TYR   S CA  1 
ATOM   32845 C  C   . TYR   S  5  94  ? 63.321  -185.247 39.047  1.00 96.86  ? 93  TYR   S C   1 
ATOM   32846 O  O   . TYR   S  5  94  ? 63.075  -184.106 39.479  1.00 99.18  ? 93  TYR   S O   1 
ATOM   32847 C  CB  . TYR   S  5  94  ? 61.534  -186.698 38.028  1.00 95.51  ? 93  TYR   S CB  1 
ATOM   32848 C  CG  . TYR   S  5  94  ? 60.421  -186.155 38.888  1.00 96.52  ? 93  TYR   S CG  1 
ATOM   32849 C  CD1 . TYR   S  5  94  ? 59.365  -185.452 38.332  1.00 96.85  ? 93  TYR   S CD1 1 
ATOM   32850 C  CD2 . TYR   S  5  94  ? 60.416  -186.348 40.261  1.00 98.24  ? 93  TYR   S CD2 1 
ATOM   32851 C  CE1 . TYR   S  5  94  ? 58.334  -184.954 39.114  1.00 99.69  ? 93  TYR   S CE1 1 
ATOM   32852 C  CE2 . TYR   S  5  94  ? 59.394  -185.857 41.058  1.00 99.74  ? 93  TYR   S CE2 1 
ATOM   32853 C  CZ  . TYR   S  5  94  ? 58.349  -185.156 40.483  1.00 100.00 ? 93  TYR   S CZ  1 
ATOM   32854 O  OH  . TYR   S  5  94  ? 57.340  -184.669 41.264  1.00 102.67 ? 93  TYR   S OH  1 
ATOM   32855 N  N   . SER   S  5  95  ? 64.136  -186.117 39.649  1.00 96.59  ? 94  SER   S N   1 
ATOM   32856 C  CA  . SER   S  5  95  ? 64.878  -185.857 40.911  1.00 98.52  ? 94  SER   S CA  1 
ATOM   32857 C  C   . SER   S  5  95  ? 65.756  -184.608 40.765  1.00 97.84  ? 94  SER   S C   1 
ATOM   32858 O  O   . SER   S  5  95  ? 65.776  -183.798 41.711  1.00 99.36  ? 94  SER   S O   1 
ATOM   32859 C  CB  . SER   S  5  95  ? 65.701  -187.053 41.316  1.00 100.07 ? 94  SER   S CB  1 
ATOM   32860 O  OG  . SER   S  5  95  ? 66.277  -186.865 42.601  1.00 101.10 ? 94  SER   S OG  1 
ATOM   32861 N  N   . SER   S  5  96  ? 66.456  -184.469 39.632  1.00 97.41  ? 95  SER   S N   1 
ATOM   32862 C  CA  . SER   S  5  96  ? 67.387  -183.347 39.328  1.00 98.31  ? 95  SER   S CA  1 
ATOM   32863 C  C   . SER   S  5  96  ? 66.615  -182.038 39.147  1.00 99.06  ? 95  SER   S C   1 
ATOM   32864 O  O   . SER   S  5  96  ? 67.011  -181.038 39.762  1.00 102.12 ? 95  SER   S O   1 
ATOM   32865 C  CB  . SER   S  5  96  ? 68.229  -183.628 38.113  1.00 98.08  ? 95  SER   S CB  1 
ATOM   32866 O  OG  . SER   S  5  96  ? 69.178  -184.646 38.384  1.00 100.08 ? 95  SER   S OG  1 
ATOM   32867 N  N   . LEU   S  5  97  ? 65.571  -182.037 38.316  1.00 99.31  ? 96  LEU   S N   1 
ATOM   32868 C  CA  . LEU   S  5  97  ? 64.814  -180.804 37.977  1.00 101.37 ? 96  LEU   S CA  1 
ATOM   32869 C  C   . LEU   S  5  97  ? 64.056  -180.306 39.216  1.00 100.76 ? 96  LEU   S C   1 
ATOM   32870 O  O   . LEU   S  5  97  ? 64.165  -179.097 39.517  1.00 106.04 ? 96  LEU   S O   1 
ATOM   32871 C  CB  . LEU   S  5  97  ? 63.873  -181.077 36.797  1.00 104.84 ? 96  LEU   S CB  1 
ATOM   32872 C  CG  . LEU   S  5  97  ? 64.551  -181.428 35.470  1.00 108.01 ? 96  LEU   S CG  1 
ATOM   32873 C  CD1 . LEU   S  5  97  ? 63.513  -181.639 34.376  1.00 109.01 ? 96  LEU   S CD1 1 
ATOM   32874 C  CD2 . LEU   S  5  97  ? 65.550  -180.356 35.047  1.00 108.83 ? 96  LEU   S CD2 1 
ATOM   32875 N  N   . VAL   S  5  98  ? 63.352  -181.192 39.929  1.00 92.41  ? 97  VAL   S N   1 
ATOM   32876 C  CA  . VAL   S  5  98  ? 62.383  -180.802 40.999  1.00 91.11  ? 97  VAL   S CA  1 
ATOM   32877 C  C   . VAL   S  5  98  ? 63.116  -180.566 42.327  1.00 90.86  ? 97  VAL   S C   1 
ATOM   32878 O  O   . VAL   S  5  98  ? 62.753  -179.599 43.018  1.00 92.32  ? 97  VAL   S O   1 
ATOM   32879 C  CB  . VAL   S  5  98  ? 61.252  -181.837 41.155  1.00 91.64  ? 97  VAL   S CB  1 
ATOM   32880 C  CG1 . VAL   S  5  98  ? 60.296  -181.466 42.280  1.00 92.39  ? 97  VAL   S CG1 1 
ATOM   32881 C  CG2 . VAL   S  5  98  ? 60.486  -182.023 39.855  1.00 92.22  ? 97  VAL   S CG2 1 
ATOM   32882 N  N   . PHE   S  5  99  ? 64.086  -181.412 42.688  1.00 88.57  ? 98  PHE   S N   1 
ATOM   32883 C  CA  . PHE   S  5  99  ? 64.753  -181.390 44.019  1.00 88.82  ? 98  PHE   S CA  1 
ATOM   32884 C  C   . PHE   S  5  99  ? 66.237  -181.020 43.914  1.00 89.82  ? 98  PHE   S C   1 
ATOM   32885 O  O   . PHE   S  5  99  ? 66.890  -180.953 44.970  1.00 88.04  ? 98  PHE   S O   1 
ATOM   32886 C  CB  . PHE   S  5  99  ? 64.596  -182.743 44.714  1.00 86.49  ? 98  PHE   S CB  1 
ATOM   32887 C  CG  . PHE   S  5  99  ? 63.170  -183.103 45.031  1.00 86.54  ? 98  PHE   S CG  1 
ATOM   32888 C  CD1 . PHE   S  5  99  ? 62.530  -182.557 46.131  1.00 86.32  ? 98  PHE   S CD1 1 
ATOM   32889 C  CD2 . PHE   S  5  99  ? 62.463  -183.978 44.223  1.00 88.15  ? 98  PHE   S CD2 1 
ATOM   32890 C  CE1 . PHE   S  5  99  ? 61.214  -182.883 46.421  1.00 86.82  ? 98  PHE   S CE1 1 
ATOM   32891 C  CE2 . PHE   S  5  99  ? 61.147  -184.304 44.514  1.00 89.38  ? 98  PHE   S CE2 1 
ATOM   32892 C  CZ  . PHE   S  5  99  ? 60.525  -183.755 45.612  1.00 87.45  ? 98  PHE   S CZ  1 
ATOM   32893 N  N   . ASN   S  5  100 ? 66.757  -180.779 42.706  1.00 92.56  ? 99  ASN   S N   1 
ATOM   32894 C  CA  . ASN   S  5  100 ? 68.201  -180.505 42.475  1.00 98.18  ? 99  ASN   S CA  1 
ATOM   32895 C  C   . ASN   S  5  100 ? 69.010  -181.576 43.213  1.00 99.91  ? 99  ASN   S C   1 
ATOM   32896 O  O   . ASN   S  5  100 ? 69.971  -181.222 43.922  1.00 106.03 ? 99  ASN   S O   1 
ATOM   32897 C  CB  . ASN   S  5  100 ? 68.582  -179.085 42.912  1.00 100.55 ? 99  ASN   S CB  1 
ATOM   32898 C  CG  . ASN   S  5  100 ? 69.950  -178.628 42.443  1.00 102.89 ? 99  ASN   S CG  1 
ATOM   32899 O  OD1 . ASN   S  5  100 ? 70.487  -177.662 42.979  1.00 104.98 ? 99  ASN   S OD1 1 
ATOM   32900 N  ND2 . ASN   S  5  100 ? 70.527  -179.291 41.451  1.00 106.09 ? 99  ASN   S ND2 1 
ATOM   32901 N  N   . ARG   S  5  101 ? 68.605  -182.838 43.054  1.00 100.68 ? 100 ARG   S N   1 
ATOM   32902 C  CA  . ARG   S  5  101 ? 69.104  -184.002 43.830  1.00 101.19 ? 100 ARG   S CA  1 
ATOM   32903 C  C   . ARG   S  5  101 ? 69.391  -185.154 42.866  1.00 100.42 ? 100 ARG   S C   1 
ATOM   32904 O  O   . ARG   S  5  101 ? 68.531  -185.431 42.007  1.00 101.26 ? 100 ARG   S O   1 
ATOM   32905 C  CB  . ARG   S  5  101 ? 68.050  -184.412 44.861  1.00 101.25 ? 100 ARG   S CB  1 
ATOM   32906 C  CG  . ARG   S  5  101 ? 68.491  -185.501 45.828  1.00 101.38 ? 100 ARG   S CG  1 
ATOM   32907 C  CD  . ARG   S  5  101 ? 67.374  -185.810 46.807  1.00 102.67 ? 100 ARG   S CD  1 
ATOM   32908 N  NE  . ARG   S  5  101 ? 67.789  -186.665 47.913  1.00 101.45 ? 100 ARG   S NE  1 
ATOM   32909 C  CZ  . ARG   S  5  101 ? 67.034  -186.958 48.971  1.00 100.59 ? 100 ARG   S CZ  1 
ATOM   32910 N  NH1 . ARG   S  5  101 ? 65.811  -186.461 49.081  1.00 103.07 ? 100 ARG   S NH1 1 
ATOM   32911 N  NH2 . ARG   S  5  101 ? 67.506  -187.746 49.922  1.00 97.96  ? 100 ARG   S NH2 1 
ATOM   32912 N  N   . LYS   S  5  102 ? 70.550  -185.799 43.008  1.00 100.95 ? 101 LYS   S N   1 
ATOM   32913 C  CA  . LYS   S  5  102 ? 70.916  -187.012 42.232  1.00 100.61 ? 101 LYS   S CA  1 
ATOM   32914 C  C   . LYS   S  5  102 ? 70.180  -188.207 42.843  1.00 98.52  ? 101 LYS   S C   1 
ATOM   32915 O  O   . LYS   S  5  102 ? 70.298  -188.404 44.065  1.00 97.99  ? 101 LYS   S O   1 
ATOM   32916 C  CB  . LYS   S  5  102 ? 72.433  -187.208 42.225  1.00 104.58 ? 101 LYS   S CB  1 
ATOM   32917 C  CG  . LYS   S  5  102 ? 73.194  -186.195 41.382  1.00 108.66 ? 101 LYS   S CG  1 
ATOM   32918 C  CD  . LYS   S  5  102 ? 74.665  -186.140 41.704  1.00 113.43 ? 101 LYS   S CD  1 
ATOM   32919 C  CE  . LYS   S  5  102 ? 75.486  -185.513 40.599  1.00 117.30 ? 101 LYS   S CE  1 
ATOM   32920 N  NZ  . LYS   S  5  102 ? 76.869  -185.237 41.050  1.00 120.45 ? 101 LYS   S NZ  1 
ATOM   32921 N  N   . LEU   S  5  103 ? 69.430  -188.949 42.023  1.00 98.86  ? 102 LEU   S N   1 
ATOM   32922 C  CA  . LEU   S  5  103 ? 68.599  -190.102 42.460  1.00 99.13  ? 102 LEU   S CA  1 
ATOM   32923 C  C   . LEU   S  5  103 ? 69.504  -191.162 43.094  1.00 100.13 ? 102 LEU   S C   1 
ATOM   32924 O  O   . LEU   S  5  103 ? 70.448  -191.603 42.421  1.00 100.93 ? 102 LEU   S O   1 
ATOM   32925 C  CB  . LEU   S  5  103 ? 67.849  -190.672 41.251  1.00 98.10  ? 102 LEU   S CB  1 
ATOM   32926 C  CG  . LEU   S  5  103 ? 66.847  -191.786 41.553  1.00 96.74  ? 102 LEU   S CG  1 
ATOM   32927 C  CD1 . LEU   S  5  103 ? 65.702  -191.276 42.416  1.00 94.65  ? 102 LEU   S CD1 1 
ATOM   32928 C  CD2 . LEU   S  5  103 ? 66.311  -192.386 40.263  1.00 96.99  ? 102 LEU   S CD2 1 
ATOM   32929 N  N   . ALA   S  5  104 ? 69.226  -191.545 44.344  1.00 100.60 ? 103 ALA   S N   1 
ATOM   32930 C  CA  . ALA   S  5  104 ? 69.948  -192.613 45.077  1.00 101.85 ? 103 ALA   S CA  1 
ATOM   32931 C  C   . ALA   S  5  104 ? 69.759  -193.947 44.345  1.00 100.52 ? 103 ALA   S C   1 
ATOM   32932 O  O   . ALA   S  5  104 ? 68.598  -194.298 44.049  1.00 96.47  ? 103 ALA   S O   1 
ATOM   32933 C  CB  . ALA   S  5  104 ? 69.456  -192.693 46.500  1.00 102.24 ? 103 ALA   S CB  1 
ATOM   32934 N  N   . VAL   S  5  105 ? 70.859  -194.664 44.086  1.00 102.56 ? 104 VAL   S N   1 
ATOM   32935 C  CA  . VAL   S  5  105 ? 70.883  -195.961 43.338  1.00 103.76 ? 104 VAL   S CA  1 
ATOM   32936 C  C   . VAL   S  5  105 ? 69.878  -196.927 43.982  1.00 103.86 ? 104 VAL   S C   1 
ATOM   32937 O  O   . VAL   S  5  105 ? 69.306  -197.755 43.251  1.00 101.93 ? 104 VAL   S O   1 
ATOM   32938 C  CB  . VAL   S  5  105 ? 72.298  -196.575 43.285  1.00 103.04 ? 104 VAL   S CB  1 
ATOM   32939 C  CG1 . VAL   S  5  105 ? 72.304  -197.922 42.575  1.00 102.92 ? 104 VAL   S CG1 1 
ATOM   32940 C  CG2 . VAL   S  5  105 ? 73.309  -195.643 42.631  1.00 102.14 ? 104 VAL   S CG2 1 
ATOM   32941 N  N   . GLU   S  5  106 ? 69.672  -196.820 45.299  1.00 106.57 ? 105 GLU   S N   1 
ATOM   32942 C  CA  . GLU   S  5  106 ? 68.719  -197.661 46.071  1.00 108.69 ? 105 GLU   S CA  1 
ATOM   32943 C  C   . GLU   S  5  106 ? 67.280  -197.348 45.639  1.00 110.93 ? 105 GLU   S C   1 
ATOM   32944 O  O   . GLU   S  5  106 ? 66.532  -198.312 45.390  1.00 110.16 ? 105 GLU   S O   1 
ATOM   32945 C  CB  . GLU   S  5  106 ? 68.903  -197.450 47.575  1.00 115.43 ? 105 GLU   S CB  1 
ATOM   32946 C  CG  . GLU   S  5  106 ? 68.398  -198.616 48.403  1.00 120.75 ? 105 GLU   S CG  1 
ATOM   32947 C  CD  . GLU   S  5  106 ? 68.641  -198.501 49.899  1.00 129.14 ? 105 GLU   S CD  1 
ATOM   32948 O  OE1 . GLU   S  5  106 ? 67.673  -198.678 50.669  1.00 136.79 ? 105 GLU   S OE1 1 
ATOM   32949 O  OE2 . GLU   S  5  106 ? 69.799  -198.248 50.292  1.00 135.94 ? 105 GLU   S OE2 1 
ATOM   32950 N  N   . ARG   S  5  107 ? 66.908  -196.063 45.556  1.00 108.52 ? 106 ARG   S N   1 
ATOM   32951 C  CA  . ARG   S  5  107 ? 65.560  -195.613 45.099  1.00 108.66 ? 106 ARG   S CA  1 
ATOM   32952 C  C   . ARG   S  5  107 ? 65.332  -196.072 43.653  1.00 102.87 ? 106 ARG   S C   1 
ATOM   32953 O  O   . ARG   S  5  107 ? 64.203  -196.508 43.348  1.00 101.60 ? 106 ARG   S O   1 
ATOM   32954 C  CB  . ARG   S  5  107 ? 65.391  -194.094 45.218  1.00 107.79 ? 106 ARG   S CB  1 
ATOM   32955 C  CG  . ARG   S  5  107 ? 64.929  -193.622 46.589  1.00 111.59 ? 106 ARG   S CG  1 
ATOM   32956 C  CD  . ARG   S  5  107 ? 64.226  -192.277 46.544  1.00 112.01 ? 106 ARG   S CD  1 
ATOM   32957 N  NE  . ARG   S  5  107 ? 62.793  -192.402 46.285  1.00 113.91 ? 106 ARG   S NE  1 
ATOM   32958 C  CZ  . ARG   S  5  107 ? 62.128  -191.851 45.266  1.00 114.54 ? 106 ARG   S CZ  1 
ATOM   32959 N  NH1 . ARG   S  5  107 ? 62.749  -191.105 44.366  1.00 115.84 ? 106 ARG   S NH1 1 
ATOM   32960 N  NH2 . ARG   S  5  107 ? 60.825  -192.046 45.157  1.00 113.00 ? 106 ARG   S NH2 1 
ATOM   32961 N  N   . ALA   S  5  108 ? 66.364  -195.977 42.804  1.00 102.21 ? 107 ALA   S N   1 
ATOM   32962 C  CA  . ALA   S  5  108 ? 66.356  -196.447 41.398  1.00 101.01 ? 107 ALA   S CA  1 
ATOM   32963 C  C   . ALA   S  5  108 ? 65.882  -197.902 41.359  1.00 100.30 ? 107 ALA   S C   1 
ATOM   32964 O  O   . ALA   S  5  108 ? 65.039  -198.227 40.501  1.00 99.09  ? 107 ALA   S O   1 
ATOM   32965 C  CB  . ALA   S  5  108 ? 67.726  -196.295 40.784  1.00 100.50 ? 107 ALA   S CB  1 
ATOM   32966 N  N   . GLY   S  5  109 ? 66.398  -198.729 42.275  1.00 100.00 ? 108 GLY   S N   1 
ATOM   32967 C  CA  . GLY   S  5  109 ? 66.012  -200.143 42.443  1.00 101.72 ? 108 GLY   S CA  1 
ATOM   32968 C  C   . GLY   S  5  109 ? 64.546  -200.281 42.817  1.00 101.87 ? 108 GLY   S C   1 
ATOM   32969 O  O   . GLY   S  5  109 ? 63.834  -201.048 42.137  1.00 100.56 ? 108 GLY   S O   1 
ATOM   32970 N  N   . HIS   S  5  110 ? 64.108  -199.549 43.846  1.00 101.91 ? 109 HIS   S N   1 
ATOM   32971 C  CA  . HIS   S  5  110 ? 62.726  -199.585 44.400  1.00 103.36 ? 109 HIS   S CA  1 
ATOM   32972 C  C   . HIS   S  5  110 ? 61.707  -199.230 43.309  1.00 102.66 ? 109 HIS   S C   1 
ATOM   32973 O  O   . HIS   S  5  110 ? 60.620  -199.843 43.295  1.00 99.92  ? 109 HIS   S O   1 
ATOM   32974 C  CB  . HIS   S  5  110 ? 62.597  -198.641 45.605  1.00 104.07 ? 109 HIS   S CB  1 
ATOM   32975 C  CG  . HIS   S  5  110 ? 63.448  -199.011 46.775  1.00 105.43 ? 109 HIS   S CG  1 
ATOM   32976 N  ND1 . HIS   S  5  110 ? 63.406  -200.262 47.360  1.00 105.40 ? 109 HIS   S ND1 1 
ATOM   32977 C  CD2 . HIS   S  5  110 ? 64.342  -198.292 47.488  1.00 107.18 ? 109 HIS   S CD2 1 
ATOM   32978 C  CE1 . HIS   S  5  110 ? 64.250  -200.302 48.371  1.00 106.00 ? 109 HIS   S CE1 1 
ATOM   32979 N  NE2 . HIS   S  5  110 ? 64.836  -199.106 48.471  1.00 106.32 ? 109 HIS   S NE2 1 
ATOM   32980 N  N   . LEU   S  5  111 ? 62.049  -198.271 42.440  1.00 105.51 ? 110 LEU   S N   1 
ATOM   32981 C  CA  . LEU   S  5  111 ? 61.169  -197.766 41.351  1.00 106.53 ? 110 LEU   S CA  1 
ATOM   32982 C  C   . LEU   S  5  111 ? 61.025  -198.831 40.256  1.00 106.75 ? 110 LEU   S C   1 
ATOM   32983 O  O   . LEU   S  5  111 ? 59.899  -198.987 39.743  1.00 114.24 ? 110 LEU   S O   1 
ATOM   32984 C  CB  . LEU   S  5  111 ? 61.752  -196.465 40.791  1.00 106.34 ? 110 LEU   S CB  1 
ATOM   32985 C  CG  . LEU   S  5  111 ? 61.635  -195.252 41.713  1.00 103.42 ? 110 LEU   S CG  1 
ATOM   32986 C  CD1 . LEU   S  5  111 ? 62.575  -194.143 41.267  1.00 103.80 ? 110 LEU   S CD1 1 
ATOM   32987 C  CD2 . LEU   S  5  111 ? 60.200  -194.751 41.771  1.00 100.56 ? 110 LEU   S CD2 1 
ATOM   32988 N  N   . LEU   S  5  112 ? 62.116  -199.524 39.907  1.00 105.28 ? 111 LEU   S N   1 
ATOM   32989 C  CA  . LEU   S  5  112 ? 62.114  -200.610 38.888  1.00 104.19 ? 111 LEU   S CA  1 
ATOM   32990 C  C   . LEU   S  5  112 ? 61.283  -201.788 39.405  1.00 104.51 ? 111 LEU   S C   1 
ATOM   32991 O  O   . LEU   S  5  112 ? 60.447  -202.299 38.635  1.00 103.59 ? 111 LEU   S O   1 
ATOM   32992 C  CB  . LEU   S  5  112 ? 63.551  -201.041 38.576  1.00 106.32 ? 111 LEU   S CB  1 
ATOM   32993 C  CG  . LEU   S  5  112 ? 64.369  -200.061 37.735  1.00 106.95 ? 111 LEU   S CG  1 
ATOM   32994 C  CD1 . LEU   S  5  112 ? 65.805  -200.542 37.590  1.00 107.70 ? 111 LEU   S CD1 1 
ATOM   32995 C  CD2 . LEU   S  5  112 ? 63.742  -199.852 36.364  1.00 108.32 ? 111 LEU   S CD2 1 
ATOM   32996 N  N   . CYS   S  5  113 ? 61.504  -202.191 40.660  1.00 103.22 ? 112 CYS   S N   1 
ATOM   32997 C  CA  . CYS   S  5  113 ? 60.753  -203.270 41.356  1.00 103.78 ? 112 CYS   S CA  1 
ATOM   32998 C  C   . CYS   S  5  113 ? 59.244  -203.036 41.208  1.00 102.02 ? 112 CYS   S C   1 
ATOM   32999 O  O   . CYS   S  5  113 ? 58.540  -203.980 40.806  1.00 104.72 ? 112 CYS   S O   1 
ATOM   33000 C  CB  . CYS   S  5  113 ? 61.120  -203.344 42.835  1.00 104.19 ? 112 CYS   S CB  1 
ATOM   33001 S  SG  . CYS   S  5  113 ? 60.010  -204.401 43.802  1.00 106.08 ? 112 CYS   S SG  1 
ATOM   33002 N  N   . ASP   S  5  114 ? 58.778  -201.822 41.513  1.00 99.35  ? 113 ASP   S N   1 
ATOM   33003 C  CA  . ASP   S  5  114 ? 57.334  -201.473 41.570  1.00 98.52  ? 113 ASP   S CA  1 
ATOM   33004 C  C   . ASP   S  5  114 ? 56.753  -201.411 40.154  1.00 97.26  ? 113 ASP   S C   1 
ATOM   33005 O  O   . ASP   S  5  114 ? 55.544  -201.692 40.010  1.00 93.92  ? 113 ASP   S O   1 
ATOM   33006 C  CB  . ASP   S  5  114 ? 57.116  -200.163 42.331  1.00 100.36 ? 113 ASP   S CB  1 
ATOM   33007 C  CG  . ASP   S  5  114 ? 57.479  -200.249 43.804  1.00 102.25 ? 113 ASP   S CG  1 
ATOM   33008 O  OD1 . ASP   S  5  114 ? 57.559  -201.383 44.327  1.00 106.45 ? 113 ASP   S OD1 1 
ATOM   33009 O  OD2 . ASP   S  5  114 ? 57.684  -199.182 44.418  1.00 103.44 ? 113 ASP   S OD2 1 
ATOM   33010 N  N   . LYS   S  5  115 ? 57.572  -201.062 39.155  1.00 99.87  ? 114 LYS   S N   1 
ATOM   33011 C  CA  . LYS   S  5  115 ? 57.135  -200.943 37.736  1.00 102.69 ? 114 LYS   S CA  1 
ATOM   33012 C  C   . LYS   S  5  115 ? 56.946  -202.347 37.152  1.00 102.03 ? 114 LYS   S C   1 
ATOM   33013 O  O   . LYS   S  5  115 ? 55.942  -202.565 36.448  1.00 99.37  ? 114 LYS   S O   1 
ATOM   33014 C  CB  . LYS   S  5  115 ? 58.136  -200.144 36.894  1.00 105.27 ? 114 LYS   S CB  1 
ATOM   33015 C  CG  . LYS   S  5  115 ? 57.505  -199.389 35.731  1.00 106.53 ? 114 LYS   S CG  1 
ATOM   33016 C  CD  . LYS   S  5  115 ? 58.384  -199.268 34.507  1.00 110.39 ? 114 LYS   S CD  1 
ATOM   33017 C  CE  . LYS   S  5  115 ? 57.853  -198.266 33.502  1.00 111.71 ? 114 LYS   S CE  1 
ATOM   33018 N  NZ  . LYS   S  5  115 ? 56.521  -198.649 32.974  1.00 112.66 ? 114 LYS   S NZ  1 
ATOM   33019 N  N   . ALA   S  5  116 ? 57.882  -203.255 37.440  1.00 104.77 ? 115 ALA   S N   1 
ATOM   33020 C  CA  . ALA   S  5  116 ? 57.864  -204.669 36.996  1.00 106.07 ? 115 ALA   S CA  1 
ATOM   33021 C  C   . ALA   S  5  116 ? 56.697  -205.413 37.660  1.00 107.28 ? 115 ALA   S C   1 
ATOM   33022 O  O   . ALA   S  5  116 ? 56.060  -206.238 36.970  1.00 104.68 ? 115 ALA   S O   1 
ATOM   33023 C  CB  . ALA   S  5  116 ? 59.189  -205.323 37.305  1.00 108.72 ? 115 ALA   S CB  1 
ATOM   33024 N  N   . GLN   S  5  117 ? 56.427  -205.119 38.940  1.00 106.50 ? 116 GLN   S N   1 
ATOM   33025 C  CA  . GLN   S  5  117 ? 55.416  -205.815 39.785  1.00 107.10 ? 116 GLN   S CA  1 
ATOM   33026 C  C   . GLN   S  5  117 ? 54.016  -205.646 39.181  1.00 109.20 ? 116 GLN   S C   1 
ATOM   33027 O  O   . GLN   S  5  117 ? 53.280  -206.647 39.132  1.00 112.86 ? 116 GLN   S O   1 
ATOM   33028 C  CB  . GLN   S  5  117 ? 55.445  -205.276 41.218  1.00 105.98 ? 116 GLN   S CB  1 
ATOM   33029 C  CG  . GLN   S  5  117 ? 54.567  -206.054 42.195  1.00 106.81 ? 116 GLN   S CG  1 
ATOM   33030 C  CD  . GLN   S  5  117 ? 53.086  -205.764 42.096  1.00 107.15 ? 116 GLN   S CD  1 
ATOM   33031 O  OE1 . GLN   S  5  117 ? 52.257  -206.668 42.182  1.00 104.26 ? 116 GLN   S OE1 1 
ATOM   33032 N  NE2 . GLN   S  5  117 ? 52.732  -204.499 41.923  1.00 108.64 ? 116 GLN   S NE2 1 
ATOM   33033 N  N   . LYS   S  5  118 ? 53.662  -204.427 38.757  1.00 114.06 ? 117 LYS   S N   1 
ATOM   33034 C  CA  . LYS   S  5  118 ? 52.306  -204.075 38.247  1.00 113.72 ? 117 LYS   S CA  1 
ATOM   33035 C  C   . LYS   S  5  118 ? 51.966  -204.935 37.022  1.00 112.27 ? 117 LYS   S C   1 
ATOM   33036 O  O   . LYS   S  5  118 ? 50.772  -205.241 36.829  1.00 110.05 ? 117 LYS   S O   1 
ATOM   33037 C  CB  . LYS   S  5  118 ? 52.228  -202.577 37.931  1.00 116.26 ? 117 LYS   S CB  1 
ATOM   33038 C  CG  . LYS   S  5  118 ? 52.163  -201.680 39.160  1.00 119.15 ? 117 LYS   S CG  1 
ATOM   33039 C  CD  . LYS   S  5  118 ? 52.359  -200.211 38.862  1.00 120.94 ? 117 LYS   S CD  1 
ATOM   33040 C  CE  . LYS   S  5  118 ? 52.206  -199.341 40.091  1.00 123.31 ? 117 LYS   S CE  1 
ATOM   33041 N  NZ  . LYS   S  5  118 ? 52.241  -197.900 39.747  1.00 125.47 ? 117 LYS   S NZ  1 
ATOM   33042 N  N   . ASN   S  5  119 ? 52.982  -205.333 36.251  1.00 108.54 ? 118 ASN   S N   1 
ATOM   33043 C  CA  . ASN   S  5  119 ? 52.836  -206.130 35.004  1.00 110.15 ? 118 ASN   S CA  1 
ATOM   33044 C  C   . ASN   S  5  119 ? 52.600  -207.612 35.335  1.00 113.33 ? 118 ASN   S C   1 
ATOM   33045 O  O   . ASN   S  5  119 ? 52.369  -208.385 34.382  1.00 110.26 ? 118 ASN   S O   1 
ATOM   33046 C  CB  . ASN   S  5  119 ? 54.054  -205.953 34.092  1.00 109.62 ? 118 ASN   S CB  1 
ATOM   33047 C  CG  . ASN   S  5  119 ? 53.987  -204.701 33.244  1.00 109.94 ? 118 ASN   S CG  1 
ATOM   33048 O  OD1 . ASN   S  5  119 ? 54.130  -204.774 32.026  1.00 108.79 ? 118 ASN   S OD1 1 
ATOM   33049 N  ND2 . ASN   S  5  119 ? 53.769  -203.553 33.866  1.00 108.81 ? 118 ASN   S ND2 1 
ATOM   33050 N  N   . THR   S  5  120 ? 52.642  -207.995 36.619  1.00 113.00 ? 119 THR   S N   1 
ATOM   33051 C  CA  . THR   S  5  120 ? 52.530  -209.407 37.081  1.00 112.05 ? 119 THR   S CA  1 
ATOM   33052 C  C   . THR   S  5  120 ? 51.211  -209.658 37.827  1.00 111.88 ? 119 THR   S C   1 
ATOM   33053 O  O   . THR   S  5  120 ? 51.000  -210.819 38.233  1.00 113.32 ? 119 THR   S O   1 
ATOM   33054 C  CB  . THR   S  5  120 ? 53.723  -209.819 37.958  1.00 110.42 ? 119 THR   S CB  1 
ATOM   33055 O  OG1 . THR   S  5  120 ? 53.674  -209.112 39.198  1.00 106.94 ? 119 THR   S OG1 1 
ATOM   33056 C  CG2 . THR   S  5  120 ? 55.061  -209.583 37.291  1.00 111.01 ? 119 THR   S CG2 1 
ATOM   33057 N  N   . GLN   S  5  121 ? 50.359  -208.641 38.004  1.00 108.06 ? 120 GLN   S N   1 
ATOM   33058 C  CA  . GLN   S  5  121 ? 49.115  -208.751 38.818  1.00 108.45 ? 120 GLN   S CA  1 
ATOM   33059 C  C   . GLN   S  5  121 ? 47.867  -208.387 37.995  1.00 109.52 ? 120 GLN   S C   1 
ATOM   33060 O  O   . GLN   S  5  121 ? 46.757  -208.630 38.511  1.00 105.92 ? 120 GLN   S O   1 
ATOM   33061 C  CB  . GLN   S  5  121 ? 49.234  -207.878 40.071  1.00 108.24 ? 120 GLN   S CB  1 
ATOM   33062 C  CG  . GLN   S  5  121 ? 48.217  -208.217 41.156  1.00 107.48 ? 120 GLN   S CG  1 
ATOM   33063 C  CD  . GLN   S  5  121 ? 48.520  -207.651 42.525  1.00 106.73 ? 120 GLN   S CD  1 
ATOM   33064 O  OE1 . GLN   S  5  121 ? 47.906  -208.044 43.515  1.00 107.19 ? 120 GLN   S OE1 1 
ATOM   33065 N  NE2 . GLN   S  5  121 ? 49.456  -206.716 42.610  1.00 108.26 ? 120 GLN   S NE2 1 
ATOM   33066 N  N   . SER   S  5  122 ? 48.018  -207.859 36.772  1.00 111.37 ? 121 SER   S N   1 
ATOM   33067 C  CA  . SER   S  5  122 ? 46.892  -207.376 35.924  1.00 112.58 ? 121 SER   S CA  1 
ATOM   33068 C  C   . SER   S  5  122 ? 46.747  -208.228 34.658  1.00 114.14 ? 121 SER   S C   1 
ATOM   33069 O  O   . SER   S  5  122 ? 47.779  -208.667 34.114  1.00 109.67 ? 121 SER   S O   1 
ATOM   33070 C  CB  . SER   S  5  122 ? 47.061  -205.926 35.566  1.00 112.45 ? 121 SER   S CB  1 
ATOM   33071 O  OG  . SER   S  5  122 ? 47.080  -205.119 36.733  1.00 111.59 ? 121 SER   S OG  1 
ATOM   33072 N  N   . TYR   S  5  123 ? 45.501  -208.415 34.205  1.00 122.35 ? 122 TYR   S N   1 
ATOM   33073 C  CA  . TYR   S  5  123 ? 45.133  -209.138 32.958  1.00 127.56 ? 122 TYR   S CA  1 
ATOM   33074 C  C   . TYR   S  5  123 ? 45.545  -208.293 31.750  1.00 125.39 ? 122 TYR   S C   1 
ATOM   33075 O  O   . TYR   S  5  123 ? 45.469  -207.052 31.832  1.00 126.18 ? 122 TYR   S O   1 
ATOM   33076 C  CB  . TYR   S  5  123 ? 43.632  -209.445 32.911  1.00 139.46 ? 122 TYR   S CB  1 
ATOM   33077 C  CG  . TYR   S  5  123 ? 43.146  -209.985 31.587  1.00 152.34 ? 122 TYR   S CG  1 
ATOM   33078 C  CD1 . TYR   S  5  123 ? 43.507  -211.253 31.155  1.00 152.79 ? 122 TYR   S CD1 1 
ATOM   33079 C  CD2 . TYR   S  5  123 ? 42.336  -209.226 30.754  1.00 157.88 ? 122 TYR   S CD2 1 
ATOM   33080 C  CE1 . TYR   S  5  123 ? 43.074  -211.754 29.937  1.00 151.74 ? 122 TYR   S CE1 1 
ATOM   33081 C  CE2 . TYR   S  5  123 ? 41.892  -209.713 29.535  1.00 158.70 ? 122 TYR   S CE2 1 
ATOM   33082 C  CZ  . TYR   S  5  123 ? 42.261  -210.983 29.124  1.00 156.08 ? 122 TYR   S CZ  1 
ATOM   33083 O  OH  . TYR   S  5  123 ? 41.829  -211.471 27.925  1.00 154.97 ? 122 TYR   S OH  1 
ATOM   33084 N  N   . GLY   S  5  124 ? 45.973  -208.955 30.671  1.00 121.98 ? 123 GLY   S N   1 
ATOM   33085 C  CA  . GLY   S  5  124 ? 46.324  -208.320 29.385  1.00 120.99 ? 123 GLY   S CA  1 
ATOM   33086 C  C   . GLY   S  5  124 ? 47.813  -208.044 29.275  1.00 117.96 ? 123 GLY   S C   1 
ATOM   33087 O  O   . GLY   S  5  124 ? 48.363  -208.218 28.170  1.00 124.52 ? 123 GLY   S O   1 
ATOM   33088 N  N   . GLY   S  5  125 ? 48.446  -207.629 30.377  1.00 110.77 ? 124 GLY   S N   1 
ATOM   33089 C  CA  . GLY   S  5  125 ? 49.883  -207.305 30.426  1.00 110.37 ? 124 GLY   S CA  1 
ATOM   33090 C  C   . GLY   S  5  125 ? 50.738  -208.557 30.372  1.00 109.12 ? 124 GLY   S C   1 
ATOM   33091 O  O   . GLY   S  5  125 ? 50.171  -209.663 30.394  1.00 112.63 ? 124 GLY   S O   1 
ATOM   33092 N  N   . ARG   S  5  126 ? 52.059  -208.385 30.290  1.00 106.66 ? 125 ARG   S N   1 
ATOM   33093 C  CA  . ARG   S  5  126 ? 53.056  -209.481 30.400  1.00 106.05 ? 125 ARG   S CA  1 
ATOM   33094 C  C   . ARG   S  5  126 ? 54.224  -209.003 31.254  1.00 105.35 ? 125 ARG   S C   1 
ATOM   33095 O  O   . ARG   S  5  126 ? 54.496  -207.808 31.312  1.00 106.35 ? 125 ARG   S O   1 
ATOM   33096 C  CB  . ARG   S  5  126 ? 53.542  -209.919 29.015  1.00 105.89 ? 125 ARG   S CB  1 
ATOM   33097 C  CG  . ARG   S  5  126 ? 54.374  -208.882 28.273  1.00 103.18 ? 125 ARG   S CG  1 
ATOM   33098 C  CD  . ARG   S  5  126 ? 55.186  -209.514 27.159  1.00 104.03 ? 125 ARG   S CD  1 
ATOM   33099 N  NE  . ARG   S  5  126 ? 55.862  -208.526 26.330  1.00 102.46 ? 125 ARG   S NE  1 
ATOM   33100 C  CZ  . ARG   S  5  126 ? 57.022  -207.941 26.621  1.00 103.71 ? 125 ARG   S CZ  1 
ATOM   33101 N  NH1 . ARG   S  5  126 ? 57.666  -208.234 27.739  1.00 104.75 ? 125 ARG   S NH1 1 
ATOM   33102 N  NH2 . ARG   S  5  126 ? 57.534  -207.056 25.783  1.00 103.91 ? 125 ARG   S NH2 1 
ATOM   33103 N  N   . PRO   S  5  127 ? 54.961  -209.913 31.931  1.00 106.27 ? 126 PRO   S N   1 
ATOM   33104 C  CA  . PRO   S  5  127 ? 56.175  -209.530 32.645  1.00 104.32 ? 126 PRO   S CA  1 
ATOM   33105 C  C   . PRO   S  5  127 ? 57.234  -209.024 31.660  1.00 102.03 ? 126 PRO   S C   1 
ATOM   33106 O  O   . PRO   S  5  127 ? 57.229  -209.467 30.527  1.00 99.65  ? 126 PRO   S O   1 
ATOM   33107 C  CB  . PRO   S  5  127 ? 56.670  -210.822 33.311  1.00 105.51 ? 126 PRO   S CB  1 
ATOM   33108 C  CG  . PRO   S  5  127 ? 55.482  -211.762 33.263  1.00 107.07 ? 126 PRO   S CG  1 
ATOM   33109 C  CD  . PRO   S  5  127 ? 54.681  -211.352 32.043  1.00 106.99 ? 126 PRO   S CD  1 
ATOM   33110 N  N   . TYR   S  5  128 ? 58.104  -208.119 32.110  1.00 101.68 ? 127 TYR   S N   1 
ATOM   33111 C  CA  . TYR   S  5  128 ? 59.307  -207.687 31.353  1.00 102.70 ? 127 TYR   S CA  1 
ATOM   33112 C  C   . TYR   S  5  128 ? 60.200  -208.921 31.185  1.00 104.35 ? 127 TYR   S C   1 
ATOM   33113 O  O   . TYR   S  5  128 ? 60.305  -209.707 32.136  1.00 104.88 ? 127 TYR   S O   1 
ATOM   33114 C  CB  . TYR   S  5  128 ? 60.002  -206.516 32.055  1.00 103.29 ? 127 TYR   S CB  1 
ATOM   33115 C  CG  . TYR   S  5  128 ? 59.206  -205.234 32.064  1.00 100.27 ? 127 TYR   S CG  1 
ATOM   33116 C  CD1 . TYR   S  5  128 ? 59.321  -204.308 31.037  1.00 97.63  ? 127 TYR   S CD1 1 
ATOM   33117 C  CD2 . TYR   S  5  128 ? 58.325  -204.947 33.095  1.00 100.55 ? 127 TYR   S CD2 1 
ATOM   33118 C  CE1 . TYR   S  5  128 ? 58.586  -203.134 31.036  1.00 95.04  ? 127 TYR   S CE1 1 
ATOM   33119 C  CE2 . TYR   S  5  128 ? 57.583  -203.777 33.110  1.00 97.55  ? 127 TYR   S CE2 1 
ATOM   33120 C  CZ  . TYR   S  5  128 ? 57.715  -202.867 32.077  1.00 95.15  ? 127 TYR   S CZ  1 
ATOM   33121 O  OH  . TYR   S  5  128 ? 56.987  -201.714 32.091  1.00 94.13  ? 127 TYR   S OH  1 
ATOM   33122 N  N   . GLY   S  5  129 ? 60.768  -209.118 29.993  1.00 106.70 ? 128 GLY   S N   1 
ATOM   33123 C  CA  . GLY   S  5  129 ? 61.571  -210.310 29.658  1.00 108.34 ? 128 GLY   S CA  1 
ATOM   33124 C  C   . GLY   S  5  129 ? 63.059  -210.010 29.647  1.00 108.20 ? 128 GLY   S C   1 
ATOM   33125 O  O   . GLY   S  5  129 ? 63.748  -210.481 28.722  1.00 110.06 ? 128 GLY   S O   1 
ATOM   33126 N  N   . VAL   S  5  130 ? 63.550  -209.262 30.638  1.00 106.55 ? 129 VAL   S N   1 
ATOM   33127 C  CA  . VAL   S  5  130 ? 64.983  -208.852 30.706  1.00 108.78 ? 129 VAL   S CA  1 
ATOM   33128 C  C   . VAL   S  5  130 ? 65.428  -208.747 32.168  1.00 106.88 ? 129 VAL   S C   1 
ATOM   33129 O  O   . VAL   S  5  130 ? 64.597  -208.391 33.028  1.00 106.53 ? 129 VAL   S O   1 
ATOM   33130 C  CB  . VAL   S  5  130 ? 65.225  -207.534 29.944  1.00 109.75 ? 129 VAL   S CB  1 
ATOM   33131 C  CG1 . VAL   S  5  130 ? 64.659  -206.323 30.674  1.00 108.55 ? 129 VAL   S CG1 1 
ATOM   33132 C  CG2 . VAL   S  5  130 ? 66.701  -207.337 29.636  1.00 112.14 ? 129 VAL   S CG2 1 
ATOM   33133 N  N   . GLY   S  5  131 ? 66.705  -209.055 32.411  1.00 107.92 ? 130 GLY   S N   1 
ATOM   33134 C  CA  . GLY   S  5  131 ? 67.412  -208.829 33.684  1.00 108.56 ? 130 GLY   S CA  1 
ATOM   33135 C  C   . GLY   S  5  131 ? 68.417  -207.704 33.527  1.00 109.37 ? 130 GLY   S C   1 
ATOM   33136 O  O   . GLY   S  5  131 ? 69.041  -207.629 32.448  1.00 109.66 ? 130 GLY   S O   1 
ATOM   33137 N  N   . LEU   S  5  132 ? 68.562  -206.858 34.551  1.00 111.24 ? 131 LEU   S N   1 
ATOM   33138 C  CA  . LEU   S  5  132 ? 69.431  -205.650 34.521  1.00 112.25 ? 131 LEU   S CA  1 
ATOM   33139 C  C   . LEU   S  5  132 ? 70.426  -205.692 35.685  1.00 115.36 ? 131 LEU   S C   1 
ATOM   33140 O  O   . LEU   S  5  132 ? 70.034  -206.129 36.787  1.00 117.41 ? 131 LEU   S O   1 
ATOM   33141 C  CB  . LEU   S  5  132 ? 68.562  -204.391 34.607  1.00 109.65 ? 131 LEU   S CB  1 
ATOM   33142 C  CG  . LEU   S  5  132 ? 67.505  -204.231 33.516  1.00 109.34 ? 131 LEU   S CG  1 
ATOM   33143 C  CD1 . LEU   S  5  132 ? 66.537  -203.113 33.867  1.00 107.59 ? 131 LEU   S CD1 1 
ATOM   33144 C  CD2 . LEU   S  5  132 ? 68.153  -203.975 32.163  1.00 110.45 ? 131 LEU   S CD2 1 
ATOM   33145 N  N   . LEU   S  5  133 ? 71.663  -205.252 35.432  1.00 116.34 ? 132 LEU   S N   1 
ATOM   33146 C  CA  . LEU   S  5  133 ? 72.685  -204.947 36.468  1.00 115.36 ? 132 LEU   S CA  1 
ATOM   33147 C  C   . LEU   S  5  133 ? 72.903  -203.431 36.490  1.00 114.11 ? 132 LEU   S C   1 
ATOM   33148 O  O   . LEU   S  5  133 ? 73.512  -202.918 35.532  1.00 112.33 ? 132 LEU   S O   1 
ATOM   33149 C  CB  . LEU   S  5  133 ? 73.997  -205.671 36.145  1.00 115.67 ? 132 LEU   S CB  1 
ATOM   33150 C  CG  . LEU   S  5  133 ? 73.919  -207.188 35.995  1.00 115.92 ? 132 LEU   S CG  1 
ATOM   33151 C  CD1 . LEU   S  5  133 ? 75.304  -207.762 35.735  1.00 118.47 ? 132 LEU   S CD1 1 
ATOM   33152 C  CD2 . LEU   S  5  133 ? 73.296  -207.835 37.223  1.00 116.23 ? 132 LEU   S CD2 1 
ATOM   33153 N  N   . ILE   S  5  134 ? 72.423  -202.750 37.534  1.00 112.53 ? 133 ILE   S N   1 
ATOM   33154 C  CA  . ILE   S  5  134 ? 72.535  -201.268 37.692  1.00 112.25 ? 133 ILE   S CA  1 
ATOM   33155 C  C   . ILE   S  5  134 ? 73.748  -200.962 38.573  1.00 110.73 ? 133 ILE   S C   1 
ATOM   33156 O  O   . ILE   S  5  134 ? 73.806  -201.489 39.700  1.00 108.63 ? 133 ILE   S O   1 
ATOM   33157 C  CB  . ILE   S  5  134 ? 71.247  -200.653 38.279  1.00 112.22 ? 133 ILE   S CB  1 
ATOM   33158 C  CG1 . ILE   S  5  134 ? 70.004  -201.017 37.460  1.00 113.90 ? 133 ILE   S CG1 1 
ATOM   33159 C  CG2 . ILE   S  5  134 ? 71.397  -199.146 38.426  1.00 111.70 ? 133 ILE   S CG2 1 
ATOM   33160 C  CD1 . ILE   S  5  134 ? 69.253  -202.222 37.972  1.00 117.95 ? 133 ILE   S CD1 1 
ATOM   33161 N  N   . ILE   S  5  135 ? 74.669  -200.135 38.071  1.00 110.00 ? 134 ILE   S N   1 
ATOM   33162 C  CA  . ILE   S  5  135 ? 75.810  -199.568 38.849  1.00 113.18 ? 134 ILE   S CA  1 
ATOM   33163 C  C   . ILE   S  5  135 ? 75.589  -198.059 38.980  1.00 114.79 ? 134 ILE   S C   1 
ATOM   33164 O  O   . ILE   S  5  135 ? 74.914  -197.476 38.104  1.00 118.96 ? 134 ILE   S O   1 
ATOM   33165 C  CB  . ILE   S  5  135 ? 77.168  -199.910 38.201  1.00 112.46 ? 134 ILE   S CB  1 
ATOM   33166 C  CG1 . ILE   S  5  135 ? 77.308  -199.341 36.786  1.00 110.03 ? 134 ILE   S CG1 1 
ATOM   33167 C  CG2 . ILE   S  5  135 ? 77.399  -201.412 38.226  1.00 114.53 ? 134 ILE   S CG2 1 
ATOM   33168 C  CD1 . ILE   S  5  135 ? 78.738  -199.244 36.303  1.00 110.52 ? 134 ILE   S CD1 1 
ATOM   33169 N  N   . GLY   S  5  136 ? 76.124  -197.458 40.044  1.00 117.79 ? 135 GLY   S N   1 
ATOM   33170 C  CA  . GLY   S  5  136 ? 76.031  -196.007 40.290  1.00 115.90 ? 135 GLY   S CA  1 
ATOM   33171 C  C   . GLY   S  5  136 ? 76.917  -195.567 41.438  1.00 115.61 ? 135 GLY   S C   1 
ATOM   33172 O  O   . GLY   S  5  136 ? 77.292  -196.424 42.262  1.00 117.53 ? 135 GLY   S O   1 
ATOM   33173 N  N   . TYR   S  5  137 ? 77.249  -194.275 41.477  1.00 114.87 ? 136 TYR   S N   1 
ATOM   33174 C  CA  . TYR   S  5  137 ? 77.965  -193.608 42.595  1.00 114.90 ? 136 TYR   S CA  1 
ATOM   33175 C  C   . TYR   S  5  137 ? 77.125  -192.417 43.068  1.00 113.77 ? 136 TYR   S C   1 
ATOM   33176 O  O   . TYR   S  5  137 ? 76.893  -191.491 42.268  1.00 112.49 ? 136 TYR   S O   1 
ATOM   33177 C  CB  . TYR   S  5  137 ? 79.371  -193.177 42.172  1.00 116.69 ? 136 TYR   S CB  1 
ATOM   33178 C  CG  . TYR   S  5  137 ? 80.273  -192.832 43.328  1.00 118.19 ? 136 TYR   S CG  1 
ATOM   33179 C  CD1 . TYR   S  5  137 ? 80.273  -191.561 43.882  1.00 118.95 ? 136 TYR   S CD1 1 
ATOM   33180 C  CD2 . TYR   S  5  137 ? 81.110  -193.783 43.890  1.00 120.14 ? 136 TYR   S CD2 1 
ATOM   33181 C  CE1 . TYR   S  5  137 ? 81.090  -191.240 44.955  1.00 119.32 ? 136 TYR   S CE1 1 
ATOM   33182 C  CE2 . TYR   S  5  137 ? 81.935  -193.478 44.961  1.00 122.34 ? 136 TYR   S CE2 1 
ATOM   33183 C  CZ  . TYR   S  5  137 ? 81.926  -192.201 45.495  1.00 120.37 ? 136 TYR   S CZ  1 
ATOM   33184 O  OH  . TYR   S  5  137 ? 82.733  -191.889 46.551  1.00 120.58 ? 136 TYR   S OH  1 
ATOM   33185 N  N   . ASP   S  5  138 ? 76.676  -192.456 44.325  1.00 109.90 ? 137 ASP   S N   1 
ATOM   33186 C  CA  . ASP   S  5  138 ? 75.774  -191.440 44.928  1.00 108.10 ? 137 ASP   S CA  1 
ATOM   33187 C  C   . ASP   S  5  138 ? 76.381  -190.985 46.261  1.00 108.08 ? 137 ASP   S C   1 
ATOM   33188 O  O   . ASP   S  5  138 ? 77.594  -191.206 46.458  1.00 102.21 ? 137 ASP   S O   1 
ATOM   33189 C  CB  . ASP   S  5  138 ? 74.345  -191.988 45.036  1.00 108.85 ? 137 ASP   S CB  1 
ATOM   33190 C  CG  . ASP   S  5  138 ? 74.203  -193.222 45.915  1.00 108.78 ? 137 ASP   S CG  1 
ATOM   33191 O  OD1 . ASP   S  5  138 ? 75.119  -193.481 46.719  1.00 111.04 ? 137 ASP   S OD1 1 
ATOM   33192 O  OD2 . ASP   S  5  138 ? 73.173  -193.915 45.788  1.00 110.08 ? 137 ASP   S OD2 1 
ATOM   33193 N  N   . LYS   S  5  139 ? 75.568  -190.382 47.136  1.00 110.09 ? 138 LYS   S N   1 
ATOM   33194 C  CA  . LYS   S  5  139 ? 76.013  -189.755 48.411  1.00 112.41 ? 138 LYS   S CA  1 
ATOM   33195 C  C   . LYS   S  5  139 ? 76.456  -190.817 49.429  1.00 113.81 ? 138 LYS   S C   1 
ATOM   33196 O  O   . LYS   S  5  139 ? 77.082  -190.419 50.429  1.00 116.87 ? 138 LYS   S O   1 
ATOM   33197 C  CB  . LYS   S  5  139 ? 74.906  -188.865 48.989  1.00 113.15 ? 138 LYS   S CB  1 
ATOM   33198 C  CG  . LYS   S  5  139 ? 74.838  -187.460 48.404  1.00 113.28 ? 138 LYS   S CG  1 
ATOM   33199 C  CD  . LYS   S  5  139 ? 74.350  -186.415 49.385  1.00 114.94 ? 138 LYS   S CD  1 
ATOM   33200 C  CE  . LYS   S  5  139 ? 74.712  -185.007 48.967  1.00 118.59 ? 138 LYS   S CE  1 
ATOM   33201 N  NZ  . LYS   S  5  139 ? 74.461  -184.034 50.057  1.00 123.32 ? 138 LYS   S NZ  1 
ATOM   33202 N  N   . SER   S  5  140 ? 76.155  -192.104 49.206  1.00 113.13 ? 139 SER   S N   1 
ATOM   33203 C  CA  . SER   S  5  140 ? 76.603  -193.228 50.075  1.00 114.31 ? 139 SER   S CA  1 
ATOM   33204 C  C   . SER   S  5  140 ? 77.598  -194.133 49.332  1.00 115.20 ? 139 SER   S C   1 
ATOM   33205 O  O   . SER   S  5  140 ? 77.664  -195.329 49.669  1.00 118.03 ? 139 SER   S O   1 
ATOM   33206 C  CB  . SER   S  5  140 ? 75.427  -194.008 50.608  1.00 112.11 ? 139 SER   S CB  1 
ATOM   33207 O  OG  . SER   S  5  140 ? 74.778  -194.730 49.574  1.00 112.24 ? 139 SER   S OG  1 
ATOM   33208 N  N   . GLY   S  5  141 ? 78.349  -193.581 48.371  1.00 118.67 ? 140 GLY   S N   1 
ATOM   33209 C  CA  . GLY   S  5  141 ? 79.473  -194.260 47.693  1.00 119.60 ? 140 GLY   S CA  1 
ATOM   33210 C  C   . GLY   S  5  141 ? 79.028  -195.074 46.489  1.00 119.13 ? 140 GLY   S C   1 
ATOM   33211 O  O   . GLY   S  5  141 ? 77.997  -194.725 45.884  1.00 122.05 ? 140 GLY   S O   1 
ATOM   33212 N  N   . ALA   S  5  142 ? 79.789  -196.121 46.149  1.00 119.84 ? 141 ALA   S N   1 
ATOM   33213 C  CA  . ALA   S  5  142 ? 79.578  -196.992 44.967  1.00 118.78 ? 141 ALA   S CA  1 
ATOM   33214 C  C   . ALA   S  5  142 ? 78.530  -198.065 45.286  1.00 115.01 ? 141 ALA   S C   1 
ATOM   33215 O  O   . ALA   S  5  142 ? 78.466  -198.507 46.452  1.00 109.55 ? 141 ALA   S O   1 
ATOM   33216 C  CB  . ALA   S  5  142 ? 80.889  -197.610 44.540  1.00 122.34 ? 141 ALA   S CB  1 
ATOM   33217 N  N   . HIS   S  5  143 ? 77.743  -198.467 44.281  1.00 109.98 ? 142 HIS   S N   1 
ATOM   33218 C  CA  . HIS   S  5  143 ? 76.641  -199.459 44.404  1.00 110.28 ? 142 HIS   S CA  1 
ATOM   33219 C  C   . HIS   S  5  143 ? 76.561  -200.349 43.162  1.00 112.38 ? 142 HIS   S C   1 
ATOM   33220 O  O   . HIS   S  5  143 ? 76.881  -199.863 42.058  1.00 113.13 ? 142 HIS   S O   1 
ATOM   33221 C  CB  . HIS   S  5  143 ? 75.293  -198.762 44.605  1.00 107.86 ? 142 HIS   S CB  1 
ATOM   33222 C  CG  . HIS   S  5  143 ? 75.235  -197.905 45.820  1.00 110.84 ? 142 HIS   S CG  1 
ATOM   33223 N  ND1 . HIS   S  5  143 ? 74.886  -198.402 47.059  1.00 109.73 ? 142 HIS   S ND1 1 
ATOM   33224 C  CD2 . HIS   S  5  143 ? 75.480  -196.588 45.991  1.00 113.18 ? 142 HIS   S CD2 1 
ATOM   33225 C  CE1 . HIS   S  5  143 ? 74.915  -197.427 47.944  1.00 110.77 ? 142 HIS   S CE1 1 
ATOM   33226 N  NE2 . HIS   S  5  143 ? 75.280  -196.305 47.314  1.00 111.71 ? 142 HIS   S NE2 1 
ATOM   33227 N  N   . LEU   S  5  144 ? 76.123  -201.596 43.360  1.00 112.64 ? 143 LEU   S N   1 
ATOM   33228 C  CA  . LEU   S  5  144 ? 75.701  -202.535 42.289  1.00 111.72 ? 143 LEU   S CA  1 
ATOM   33229 C  C   . LEU   S  5  144 ? 74.368  -203.168 42.698  1.00 109.41 ? 143 LEU   S C   1 
ATOM   33230 O  O   . LEU   S  5  144 ? 74.276  -203.665 43.837  1.00 108.86 ? 143 LEU   S O   1 
ATOM   33231 C  CB  . LEU   S  5  144 ? 76.784  -203.599 42.086  1.00 114.43 ? 143 LEU   S CB  1 
ATOM   33232 C  CG  . LEU   S  5  144 ? 76.352  -204.852 41.324  1.00 116.17 ? 143 LEU   S CG  1 
ATOM   33233 C  CD1 . LEU   S  5  144 ? 76.072  -204.541 39.861  1.00 115.49 ? 143 LEU   S CD1 1 
ATOM   33234 C  CD2 . LEU   S  5  144 ? 77.408  -205.935 41.446  1.00 118.14 ? 143 LEU   S CD2 1 
ATOM   33235 N  N   . LEU   S  5  145 ? 73.386  -203.136 41.794  1.00 108.26 ? 144 LEU   S N   1 
ATOM   33236 C  CA  . LEU   S  5  145 ? 72.048  -203.763 41.955  1.00 109.16 ? 144 LEU   S CA  1 
ATOM   33237 C  C   . LEU   S  5  145 ? 71.887  -204.864 40.901  1.00 111.86 ? 144 LEU   S C   1 
ATOM   33238 O  O   . LEU   S  5  145 ? 72.504  -204.742 39.823  1.00 114.03 ? 144 LEU   S O   1 
ATOM   33239 C  CB  . LEU   S  5  145 ? 70.968  -202.687 41.791  1.00 106.27 ? 144 LEU   S CB  1 
ATOM   33240 C  CG  . LEU   S  5  145 ? 70.417  -202.069 43.075  1.00 105.26 ? 144 LEU   S CG  1 
ATOM   33241 C  CD1 . LEU   S  5  145 ? 71.530  -201.645 44.025  1.00 105.55 ? 144 LEU   S CD1 1 
ATOM   33242 C  CD2 . LEU   S  5  145 ? 69.523  -200.884 42.744  1.00 104.77 ? 144 LEU   S CD2 1 
ATOM   33243 N  N   . GLU   S  5  146 ? 71.101  -205.899 41.213  1.00 113.06 ? 145 GLU   S N   1 
ATOM   33244 C  CA  . GLU   S  5  146 ? 70.614  -206.907 40.235  1.00 114.49 ? 145 GLU   S CA  1 
ATOM   33245 C  C   . GLU   S  5  146 ? 69.088  -206.815 40.174  1.00 110.78 ? 145 GLU   S C   1 
ATOM   33246 O  O   . GLU   S  5  146 ? 68.448  -207.038 41.218  1.00 109.31 ? 145 GLU   S O   1 
ATOM   33247 C  CB  . GLU   S  5  146 ? 71.045  -208.325 40.617  1.00 118.90 ? 145 GLU   S CB  1 
ATOM   33248 C  CG  . GLU   S  5  146 ? 70.659  -209.365 39.574  1.00 124.32 ? 145 GLU   S CG  1 
ATOM   33249 C  CD  . GLU   S  5  146 ? 70.919  -210.818 39.943  1.00 127.86 ? 145 GLU   S CD  1 
ATOM   33250 O  OE1 . GLU   S  5  146 ? 71.924  -211.087 40.634  1.00 133.83 ? 145 GLU   S OE1 1 
ATOM   33251 O  OE2 . GLU   S  5  146 ? 70.117  -211.682 39.527  1.00 130.92 ? 145 GLU   S OE2 1 
ATOM   33252 N  N   . PHE   S  5  147 ? 68.544  -206.495 38.997  1.00 110.39 ? 146 PHE   S N   1 
ATOM   33253 C  CA  . PHE   S  5  147 ? 67.085  -206.437 38.719  1.00 109.74 ? 146 PHE   S CA  1 
ATOM   33254 C  C   . PHE   S  5  147 ? 66.650  -207.733 38.028  1.00 111.62 ? 146 PHE   S C   1 
ATOM   33255 O  O   . PHE   S  5  147 ? 67.254  -208.092 36.997  1.00 111.75 ? 146 PHE   S O   1 
ATOM   33256 C  CB  . PHE   S  5  147 ? 66.739  -205.230 37.844  1.00 106.33 ? 146 PHE   S CB  1 
ATOM   33257 C  CG  . PHE   S  5  147 ? 65.354  -205.269 37.249  1.00 104.52 ? 146 PHE   S CG  1 
ATOM   33258 C  CD1 . PHE   S  5  147 ? 64.258  -204.825 37.973  1.00 104.43 ? 146 PHE   S CD1 1 
ATOM   33259 C  CD2 . PHE   S  5  147 ? 65.140  -205.763 35.970  1.00 104.41 ? 146 PHE   S CD2 1 
ATOM   33260 C  CE1 . PHE   S  5  147 ? 62.983  -204.866 37.430  1.00 104.13 ? 146 PHE   S CE1 1 
ATOM   33261 C  CE2 . PHE   S  5  147 ? 63.863  -205.808 35.430  1.00 103.40 ? 146 PHE   S CE2 1 
ATOM   33262 C  CZ  . PHE   S  5  147 ? 62.787  -205.359 36.161  1.00 103.19 ? 146 PHE   S CZ  1 
ATOM   33263 N  N   . GLN   S  5  148 ? 65.631  -208.399 38.581  1.00 114.43 ? 147 GLN   S N   1 
ATOM   33264 C  CA  . GLN   S  5  148 ? 64.910  -209.528 37.934  1.00 118.61 ? 147 GLN   S CA  1 
ATOM   33265 C  C   . GLN   S  5  148 ? 63.471  -209.099 37.656  1.00 113.60 ? 147 GLN   S C   1 
ATOM   33266 O  O   . GLN   S  5  148 ? 62.841  -208.448 38.487  1.00 114.15 ? 147 GLN   S O   1 
ATOM   33267 C  CB  . GLN   S  5  148 ? 64.950  -210.782 38.808  1.00 120.24 ? 147 GLN   S CB  1 
ATOM   33268 C  CG  . GLN   S  5  148 ? 66.185  -211.639 38.574  1.00 127.78 ? 147 GLN   S CG  1 
ATOM   33269 C  CD  . GLN   S  5  148 ? 66.270  -212.836 39.492  1.00 134.56 ? 147 GLN   S CD  1 
ATOM   33270 O  OE1 . GLN   S  5  148 ? 67.359  -213.303 39.818  1.00 147.42 ? 147 GLN   S OE1 1 
ATOM   33271 N  NE2 . GLN   S  5  148 ? 65.128  -213.355 39.919  1.00 139.40 ? 147 GLN   S NE2 1 
ATOM   33272 N  N   . PRO   S  5  149 ? 62.907  -209.474 36.485  1.00 111.21 ? 148 PRO   S N   1 
ATOM   33273 C  CA  . PRO   S  5  149 ? 61.580  -209.017 36.068  1.00 109.24 ? 148 PRO   S CA  1 
ATOM   33274 C  C   . PRO   S  5  149 ? 60.408  -209.622 36.856  1.00 106.35 ? 148 PRO   S C   1 
ATOM   33275 O  O   . PRO   S  5  149 ? 59.271  -209.295 36.558  1.00 102.02 ? 148 PRO   S O   1 
ATOM   33276 C  CB  . PRO   S  5  149 ? 61.500  -209.475 34.608  1.00 109.75 ? 148 PRO   S CB  1 
ATOM   33277 C  CG  . PRO   S  5  149 ? 62.383  -210.697 34.560  1.00 111.86 ? 148 PRO   S CG  1 
ATOM   33278 C  CD  . PRO   S  5  149 ? 63.525  -210.369 35.497  1.00 111.94 ? 148 PRO   S CD  1 
ATOM   33279 N  N   . SER   S  5  150 ? 60.709  -210.496 37.819  1.00 106.40 ? 149 SER   S N   1 
ATOM   33280 C  CA  . SER   S  5  150 ? 59.773  -210.927 38.888  1.00 108.77 ? 149 SER   S CA  1 
ATOM   33281 C  C   . SER   S  5  150 ? 59.430  -209.724 39.775  1.00 110.29 ? 149 SER   S C   1 
ATOM   33282 O  O   . SER   S  5  150 ? 58.366  -209.762 40.427  1.00 115.14 ? 149 SER   S O   1 
ATOM   33283 C  CB  . SER   S  5  150 ? 60.360  -212.058 39.690  1.00 110.42 ? 149 SER   S CB  1 
ATOM   33284 O  OG  . SER   S  5  150 ? 61.528  -211.635 40.378  1.00 110.52 ? 149 SER   S OG  1 
ATOM   33285 N  N   . GLY   S  5  151 ? 60.299  -208.702 39.781  1.00 111.15 ? 150 GLY   S N   1 
ATOM   33286 C  CA  . GLY   S  5  151 ? 60.201  -207.494 40.626  1.00 110.55 ? 150 GLY   S CA  1 
ATOM   33287 C  C   . GLY   S  5  151 ? 61.329  -207.426 41.645  1.00 112.12 ? 150 GLY   S C   1 
ATOM   33288 O  O   . GLY   S  5  151 ? 61.553  -206.335 42.208  1.00 108.09 ? 150 GLY   S O   1 
ATOM   33289 N  N   . ASN   S  5  152 ? 62.018  -208.550 41.876  1.00 115.81 ? 151 ASN   S N   1 
ATOM   33290 C  CA  . ASN   S  5  152 ? 63.061  -208.705 42.926  1.00 112.95 ? 151 ASN   S CA  1 
ATOM   33291 C  C   . ASN   S  5  152 ? 64.329  -207.952 42.512  1.00 115.31 ? 151 ASN   S C   1 
ATOM   33292 O  O   . ASN   S  5  152 ? 64.948  -208.342 41.502  1.00 117.05 ? 151 ASN   S O   1 
ATOM   33293 C  CB  . ASN   S  5  152 ? 63.365  -210.178 43.210  1.00 115.90 ? 151 ASN   S CB  1 
ATOM   33294 C  CG  . ASN   S  5  152 ? 62.232  -210.878 43.930  1.00 112.50 ? 151 ASN   S CG  1 
ATOM   33295 O  OD1 . ASN   S  5  152 ? 61.925  -210.552 45.075  1.00 108.91 ? 151 ASN   S OD1 1 
ATOM   33296 N  ND2 . ASN   S  5  152 ? 61.606  -211.841 43.274  1.00 116.92 ? 151 ASN   S ND2 1 
ATOM   33297 N  N   . VAL   S  5  153 ? 64.687  -206.915 43.274  1.00 110.57 ? 152 VAL   S N   1 
ATOM   33298 C  CA  . VAL   S  5  153 ? 65.947  -206.130 43.116  1.00 110.35 ? 152 VAL   S CA  1 
ATOM   33299 C  C   . VAL   S  5  153 ? 66.828  -206.413 44.335  1.00 109.85 ? 152 VAL   S C   1 
ATOM   33300 O  O   . VAL   S  5  153 ? 66.290  -206.434 45.458  1.00 107.70 ? 152 VAL   S O   1 
ATOM   33301 C  CB  . VAL   S  5  153 ? 65.658  -204.627 42.952  1.00 109.22 ? 152 VAL   S CB  1 
ATOM   33302 C  CG1 . VAL   S  5  153 ? 66.937  -203.809 42.849  1.00 109.13 ? 152 VAL   S CG1 1 
ATOM   33303 C  CG2 . VAL   S  5  153 ? 64.758  -204.367 41.755  1.00 109.99 ? 152 VAL   S CG2 1 
ATOM   33304 N  N   . THR   S  5  154 ? 68.128  -206.624 44.114  1.00 113.92 ? 153 THR   S N   1 
ATOM   33305 C  CA  . THR   S  5  154 ? 69.099  -207.066 45.150  1.00 117.43 ? 153 THR   S CA  1 
ATOM   33306 C  C   . THR   S  5  154 ? 70.403  -206.271 45.031  1.00 120.02 ? 153 THR   S C   1 
ATOM   33307 O  O   . THR   S  5  154 ? 70.958  -206.224 43.915  1.00 125.70 ? 153 THR   S O   1 
ATOM   33308 C  CB  . THR   S  5  154 ? 69.370  -208.569 45.023  1.00 116.75 ? 153 THR   S CB  1 
ATOM   33309 O  OG1 . THR   S  5  154 ? 68.126  -209.250 45.180  1.00 119.55 ? 153 THR   S OG1 1 
ATOM   33310 C  CG2 . THR   S  5  154 ? 70.362  -209.075 46.045  1.00 118.08 ? 153 THR   S CG2 1 
ATOM   33311 N  N   . GLU   S  5  155 ? 70.877  -205.702 46.146  1.00 121.22 ? 154 GLU   S N   1 
ATOM   33312 C  CA  . GLU   S  5  155 ? 72.173  -204.973 46.236  1.00 120.66 ? 154 GLU   S CA  1 
ATOM   33313 C  C   . GLU   S  5  155 ? 73.282  -205.977 46.570  1.00 117.25 ? 154 GLU   S C   1 
ATOM   33314 O  O   . GLU   S  5  155 ? 73.121  -206.736 47.548  1.00 110.57 ? 154 GLU   S O   1 
ATOM   33315 C  CB  . GLU   S  5  155 ? 72.112  -203.853 47.279  1.00 119.37 ? 154 GLU   S CB  1 
ATOM   33316 C  CG  . GLU   S  5  155 ? 73.357  -202.978 47.289  1.00 121.56 ? 154 GLU   S CG  1 
ATOM   33317 C  CD  . GLU   S  5  155 ? 73.231  -201.646 48.013  1.00 121.15 ? 154 GLU   S CD  1 
ATOM   33318 O  OE1 . GLU   S  5  155 ? 74.138  -200.809 47.850  1.00 124.44 ? 154 GLU   S OE1 1 
ATOM   33319 O  OE2 . GLU   S  5  155 ? 72.236  -201.449 48.741  1.00 120.62 ? 154 GLU   S OE2 1 
ATOM   33320 N  N   . LEU   S  5  156 ? 74.366  -205.963 45.786  1.00 119.37 ? 155 LEU   S N   1 
ATOM   33321 C  CA  . LEU   S  5  156 ? 75.470  -206.959 45.838  1.00 122.55 ? 155 LEU   S CA  1 
ATOM   33322 C  C   . LEU   S  5  156 ? 76.818  -206.247 45.697  1.00 126.59 ? 155 LEU   S C   1 
ATOM   33323 O  O   . LEU   S  5  156 ? 76.836  -205.122 45.159  1.00 132.17 ? 155 LEU   S O   1 
ATOM   33324 C  CB  . LEU   S  5  156 ? 75.272  -207.958 44.694  1.00 122.85 ? 155 LEU   S CB  1 
ATOM   33325 C  CG  . LEU   S  5  156 ? 74.006  -208.810 44.776  1.00 124.08 ? 155 LEU   S CG  1 
ATOM   33326 C  CD1 . LEU   S  5  156 ? 73.359  -208.968 43.408  1.00 123.98 ? 155 LEU   S CD1 1 
ATOM   33327 C  CD2 . LEU   S  5  156 ? 74.302  -210.168 45.393  1.00 125.22 ? 155 LEU   S CD2 1 
ATOM   33328 N  N   . TYR   S  5  157 ? 77.897  -206.884 46.167  1.00 129.56 ? 156 TYR   S N   1 
ATOM   33329 C  CA  . TYR   S  5  157 ? 79.305  -206.473 45.917  1.00 129.67 ? 156 TYR   S CA  1 
ATOM   33330 C  C   . TYR   S  5  157 ? 79.661  -206.781 44.460  1.00 127.69 ? 156 TYR   S C   1 
ATOM   33331 O  O   . TYR   S  5  157 ? 80.307  -205.946 43.798  1.00 130.27 ? 156 TYR   S O   1 
ATOM   33332 C  CB  . TYR   S  5  157 ? 80.276  -207.199 46.851  1.00 130.92 ? 156 TYR   S CB  1 
ATOM   33333 C  CG  . TYR   S  5  157 ? 80.156  -206.824 48.306  1.00 131.48 ? 156 TYR   S CG  1 
ATOM   33334 C  CD1 . TYR   S  5  157 ? 80.481  -205.551 48.744  1.00 131.86 ? 156 TYR   S CD1 1 
ATOM   33335 C  CD2 . TYR   S  5  157 ? 79.730  -207.746 49.249  1.00 131.72 ? 156 TYR   S CD2 1 
ATOM   33336 C  CE1 . TYR   S  5  157 ? 80.376  -205.198 50.080  1.00 133.46 ? 156 TYR   S CE1 1 
ATOM   33337 C  CE2 . TYR   S  5  157 ? 79.624  -207.411 50.589  1.00 133.54 ? 156 TYR   S CE2 1 
ATOM   33338 C  CZ  . TYR   S  5  157 ? 79.946  -206.132 51.006  1.00 133.98 ? 156 TYR   S CZ  1 
ATOM   33339 O  OH  . TYR   S  5  157 ? 79.841  -205.794 52.324  1.00 139.81 ? 156 TYR   S OH  1 
ATOM   33340 N  N   . GLY   S  5  158 ? 79.249  -207.962 43.992  1.00 125.84 ? 157 GLY   S N   1 
ATOM   33341 C  CA  . GLY   S  5  158 ? 79.423  -208.427 42.604  1.00 125.61 ? 157 GLY   S CA  1 
ATOM   33342 C  C   . GLY   S  5  158 ? 78.344  -209.424 42.219  1.00 125.86 ? 157 GLY   S C   1 
ATOM   33343 O  O   . GLY   S  5  158 ? 77.720  -209.994 43.137  1.00 131.00 ? 157 GLY   S O   1 
ATOM   33344 N  N   . THR   S  5  159 ? 78.122  -209.624 40.916  1.00 122.91 ? 158 THR   S N   1 
ATOM   33345 C  CA  . THR   S  5  159 ? 77.177  -210.637 40.371  1.00 121.94 ? 158 THR   S CA  1 
ATOM   33346 C  C   . THR   S  5  159 ? 77.341  -210.770 38.853  1.00 120.67 ? 158 THR   S C   1 
ATOM   33347 O  O   . THR   S  5  159 ? 78.166  -210.039 38.268  1.00 116.00 ? 158 THR   S O   1 
ATOM   33348 C  CB  . THR   S  5  159 ? 75.719  -210.293 40.706  1.00 119.06 ? 158 THR   S CB  1 
ATOM   33349 O  OG1 . THR   S  5  159 ? 74.891  -211.384 40.302  1.00 119.06 ? 158 THR   S OG1 1 
ATOM   33350 C  CG2 . THR   S  5  159 ? 75.236  -209.030 40.030  1.00 117.72 ? 158 THR   S CG2 1 
ATOM   33351 N  N   . ALA   S  5  160 ? 76.561  -211.675 38.257  1.00 123.12 ? 159 ALA   S N   1 
ATOM   33352 C  CA  . ALA   S  5  160 ? 76.484  -211.917 36.800  1.00 123.11 ? 159 ALA   S CA  1 
ATOM   33353 C  C   . ALA   S  5  160 ? 75.123  -212.533 36.456  1.00 120.73 ? 159 ALA   S C   1 
ATOM   33354 O  O   . ALA   S  5  160 ? 74.609  -213.326 37.268  1.00 120.59 ? 159 ALA   S O   1 
ATOM   33355 C  CB  . ALA   S  5  160 ? 77.623  -212.809 36.372  1.00 125.54 ? 159 ALA   S CB  1 
ATOM   33356 N  N   . ILE   S  5  161 ? 74.565  -212.165 35.299  1.00 120.12 ? 160 ILE   S N   1 
ATOM   33357 C  CA  . ILE   S  5  161 ? 73.301  -212.733 34.740  1.00 118.96 ? 160 ILE   S CA  1 
ATOM   33358 C  C   . ILE   S  5  161 ? 73.534  -213.097 33.271  1.00 120.62 ? 160 ILE   S C   1 
ATOM   33359 O  O   . ILE   S  5  161 ? 74.413  -212.477 32.637  1.00 119.56 ? 160 ILE   S O   1 
ATOM   33360 C  CB  . ILE   S  5  161 ? 72.122  -211.753 34.899  1.00 116.68 ? 160 ILE   S CB  1 
ATOM   33361 C  CG1 . ILE   S  5  161 ? 72.475  -210.354 34.384  1.00 115.20 ? 160 ILE   S CG1 1 
ATOM   33362 C  CG2 . ILE   S  5  161 ? 71.636  -211.728 36.341  1.00 113.86 ? 160 ILE   S CG2 1 
ATOM   33363 C  CD1 . ILE   S  5  161 ? 71.279  -209.461 34.141  1.00 113.97 ? 160 ILE   S CD1 1 
ATOM   33364 N  N   . GLY   S  5  162 ? 72.765  -214.065 32.764  1.00 123.36 ? 161 GLY   S N   1 
ATOM   33365 C  CA  . GLY   S  5  162 ? 72.847  -214.567 31.379  1.00 126.43 ? 161 GLY   S CA  1 
ATOM   33366 C  C   . GLY   S  5  162 ? 73.289  -216.021 31.329  1.00 129.00 ? 161 GLY   S C   1 
ATOM   33367 O  O   . GLY   S  5  162 ? 73.369  -216.655 32.402  1.00 131.32 ? 161 GLY   S O   1 
ATOM   33368 N  N   . ALA   S  5  163 ? 73.566  -216.529 30.124  1.00 127.87 ? 162 ALA   S N   1 
ATOM   33369 C  CA  . ALA   S  5  163 ? 74.012  -217.918 29.865  1.00 129.53 ? 162 ALA   S CA  1 
ATOM   33370 C  C   . ALA   S  5  163 ? 75.408  -218.126 30.462  1.00 128.77 ? 162 ALA   S C   1 
ATOM   33371 O  O   . ALA   S  5  163 ? 76.310  -217.330 30.136  1.00 125.87 ? 162 ALA   S O   1 
ATOM   33372 C  CB  . ALA   S  5  163 ? 74.002  -218.195 28.383  1.00 132.80 ? 162 ALA   S CB  1 
ATOM   33373 N  N   . ARG   S  5  164 ? 75.561  -219.157 31.303  1.00 132.43 ? 163 ARG   S N   1 
ATOM   33374 C  CA  . ARG   S  5  164 ? 76.835  -219.559 31.964  1.00 135.47 ? 163 ARG   S CA  1 
ATOM   33375 C  C   . ARG   S  5  164 ? 77.315  -218.459 32.919  1.00 130.42 ? 163 ARG   S C   1 
ATOM   33376 O  O   . ARG   S  5  164 ? 78.538  -218.364 33.137  1.00 128.82 ? 163 ARG   S O   1 
ATOM   33377 C  CB  . ARG   S  5  164 ? 77.905  -219.887 30.917  1.00 146.98 ? 163 ARG   S CB  1 
ATOM   33378 C  CG  . ARG   S  5  164 ? 77.762  -221.269 30.297  1.00 153.07 ? 163 ARG   S CG  1 
ATOM   33379 C  CD  . ARG   S  5  164 ? 78.538  -221.376 29.000  1.00 162.62 ? 163 ARG   S CD  1 
ATOM   33380 N  NE  . ARG   S  5  164 ? 77.734  -220.983 27.847  1.00 166.38 ? 163 ARG   S NE  1 
ATOM   33381 C  CZ  . ARG   S  5  164 ? 78.180  -220.327 26.776  1.00 171.83 ? 163 ARG   S CZ  1 
ATOM   33382 N  NH1 . ARG   S  5  164 ? 79.444  -219.944 26.687  1.00 175.72 ? 163 ARG   S NH1 1 
ATOM   33383 N  NH2 . ARG   S  5  164 ? 77.343  -220.039 25.794  1.00 170.00 ? 163 ARG   S NH2 1 
ATOM   33384 N  N   . SER   S  5  165 ? 76.389  -217.687 33.497  1.00 126.11 ? 164 SER   S N   1 
ATOM   33385 C  CA  . SER   S  5  165 ? 76.678  -216.620 34.491  1.00 123.61 ? 164 SER   S CA  1 
ATOM   33386 C  C   . SER   S  5  165 ? 77.223  -217.237 35.784  1.00 128.74 ? 164 SER   S C   1 
ATOM   33387 O  O   . SER   S  5  165 ? 77.913  -216.519 36.532  1.00 123.57 ? 164 SER   S O   1 
ATOM   33388 C  CB  . SER   S  5  165 ? 75.456  -215.784 34.767  1.00 118.46 ? 164 SER   S CB  1 
ATOM   33389 O  OG  . SER   S  5  165 ? 74.425  -216.567 35.349  1.00 115.89 ? 164 SER   S OG  1 
ATOM   33390 N  N   . GLN   S  5  166 ? 76.920  -218.518 36.029  1.00 132.38 ? 165 GLN   S N   1 
ATOM   33391 C  CA  . GLN   S  5  166 ? 77.300  -219.265 37.259  1.00 138.10 ? 165 GLN   S CA  1 
ATOM   33392 C  C   . GLN   S  5  166 ? 78.829  -219.299 37.403  1.00 138.20 ? 165 GLN   S C   1 
ATOM   33393 O  O   . GLN   S  5  166 ? 79.304  -219.270 38.555  1.00 139.80 ? 165 GLN   S O   1 
ATOM   33394 C  CB  . GLN   S  5  166 ? 76.702  -220.675 37.223  1.00 142.64 ? 165 GLN   S CB  1 
ATOM   33395 C  CG  . GLN   S  5  166 ? 76.869  -221.461 38.520  1.00 146.97 ? 165 GLN   S CG  1 
ATOM   33396 C  CD  . GLN   S  5  166 ? 76.304  -220.737 39.719  1.00 148.02 ? 165 GLN   S CD  1 
ATOM   33397 O  OE1 . GLN   S  5  166 ? 76.988  -219.950 40.370  1.00 148.47 ? 165 GLN   S OE1 1 
ATOM   33398 N  NE2 . GLN   S  5  166 ? 75.044  -220.999 40.026  1.00 146.93 ? 165 GLN   S NE2 1 
ATOM   33399 N  N   . GLY   S  5  167 ? 79.565  -219.354 36.286  1.00 136.85 ? 166 GLY   S N   1 
ATOM   33400 C  CA  . GLY   S  5  167 ? 81.041  -219.382 36.265  1.00 140.21 ? 166 GLY   S CA  1 
ATOM   33401 C  C   . GLY   S  5  167 ? 81.636  -218.121 36.867  1.00 140.02 ? 166 GLY   S C   1 
ATOM   33402 O  O   . GLY   S  5  167 ? 82.462  -218.237 37.795  1.00 139.12 ? 166 GLY   S O   1 
ATOM   33403 N  N   . ALA   S  5  168 ? 81.227  -216.957 36.358  1.00 140.77 ? 167 ALA   S N   1 
ATOM   33404 C  CA  . ALA   S  5  168 ? 81.651  -215.620 36.836  1.00 141.64 ? 167 ALA   S CA  1 
ATOM   33405 C  C   . ALA   S  5  168 ? 81.183  -215.414 38.281  1.00 145.15 ? 167 ALA   S C   1 
ATOM   33406 O  O   . ALA   S  5  168 ? 81.969  -214.867 39.082  1.00 147.55 ? 167 ALA   S O   1 
ATOM   33407 C  CB  . ALA   S  5  168 ? 81.108  -214.549 35.922  1.00 138.36 ? 167 ALA   S CB  1 
ATOM   33408 N  N   . LYS   S  5  169 ? 79.956  -215.847 38.597  1.00 146.81 ? 168 LYS   S N   1 
ATOM   33409 C  CA  . LYS   S  5  169 ? 79.304  -215.644 39.921  1.00 145.77 ? 168 LYS   S CA  1 
ATOM   33410 C  C   . LYS   S  5  169 ? 80.066  -216.426 41.000  1.00 146.74 ? 168 LYS   S C   1 
ATOM   33411 O  O   . LYS   S  5  169 ? 80.180  -215.905 42.127  1.00 146.29 ? 168 LYS   S O   1 
ATOM   33412 C  CB  . LYS   S  5  169 ? 77.828  -216.053 39.875  1.00 145.60 ? 168 LYS   S CB  1 
ATOM   33413 C  CG  . LYS   S  5  169 ? 76.985  -215.526 41.029  1.00 142.94 ? 168 LYS   S CG  1 
ATOM   33414 C  CD  . LYS   S  5  169 ? 75.495  -215.650 40.807  1.00 142.22 ? 168 LYS   S CD  1 
ATOM   33415 C  CE  . LYS   S  5  169 ? 74.686  -215.067 41.946  1.00 139.19 ? 168 LYS   S CE  1 
ATOM   33416 N  NZ  . LYS   S  5  169 ? 73.232  -215.112 41.663  1.00 139.69 ? 168 LYS   S NZ  1 
ATOM   33417 N  N   . THR   S  5  170 ? 80.567  -217.622 40.671  1.00 147.62 ? 169 THR   S N   1 
ATOM   33418 C  CA  . THR   S  5  170 ? 81.423  -218.449 41.565  1.00 148.79 ? 169 THR   S CA  1 
ATOM   33419 C  C   . THR   S  5  170 ? 82.773  -217.748 41.754  1.00 150.35 ? 169 THR   S C   1 
ATOM   33420 O  O   . THR   S  5  170 ? 83.225  -217.657 42.913  1.00 151.26 ? 169 THR   S O   1 
ATOM   33421 C  CB  . THR   S  5  170 ? 81.625  -219.872 41.026  1.00 147.69 ? 169 THR   S CB  1 
ATOM   33422 O  OG1 . THR   S  5  170 ? 80.348  -220.494 40.886  1.00 147.43 ? 169 THR   S OG1 1 
ATOM   33423 C  CG2 . THR   S  5  170 ? 82.495  -220.724 41.926  1.00 147.48 ? 169 THR   S CG2 1 
ATOM   33424 N  N   . TYR   S  5  171 ? 83.386  -217.288 40.657  1.00 151.74 ? 170 TYR   S N   1 
ATOM   33425 C  CA  . TYR   S  5  171 ? 84.710  -216.610 40.638  1.00 151.64 ? 170 TYR   S CA  1 
ATOM   33426 C  C   . TYR   S  5  171 ? 84.677  -215.387 41.561  1.00 149.45 ? 170 TYR   S C   1 
ATOM   33427 O  O   . TYR   S  5  171 ? 85.562  -215.273 42.430  1.00 151.79 ? 170 TYR   S O   1 
ATOM   33428 C  CB  . TYR   S  5  171 ? 85.111  -216.198 39.219  1.00 151.83 ? 170 TYR   S CB  1 
ATOM   33429 C  CG  . TYR   S  5  171 ? 86.260  -215.222 39.162  1.00 153.04 ? 170 TYR   S CG  1 
ATOM   33430 C  CD1 . TYR   S  5  171 ? 86.040  -213.855 39.230  1.00 153.34 ? 170 TYR   S CD1 1 
ATOM   33431 C  CD2 . TYR   S  5  171 ? 87.571  -215.661 39.062  1.00 155.47 ? 170 TYR   S CD2 1 
ATOM   33432 C  CE1 . TYR   S  5  171 ? 87.087  -212.949 39.190  1.00 155.72 ? 170 TYR   S CE1 1 
ATOM   33433 C  CE2 . TYR   S  5  171 ? 88.630  -214.768 39.019  1.00 157.79 ? 170 TYR   S CE2 1 
ATOM   33434 C  CZ  . TYR   S  5  171 ? 88.388  -213.407 39.084  1.00 157.63 ? 170 TYR   S CZ  1 
ATOM   33435 O  OH  . TYR   S  5  171 ? 89.418  -212.514 39.042  1.00 163.77 ? 170 TYR   S OH  1 
ATOM   33436 N  N   . LEU   S  5  172 ? 83.696  -214.500 41.363  1.00 145.61 ? 171 LEU   S N   1 
ATOM   33437 C  CA  . LEU   S  5  172 ? 83.527  -213.256 42.164  1.00 144.50 ? 171 LEU   S CA  1 
ATOM   33438 C  C   . LEU   S  5  172 ? 83.331  -213.621 43.640  1.00 144.13 ? 171 LEU   S C   1 
ATOM   33439 O  O   . LEU   S  5  172 ? 83.834  -212.872 44.498  1.00 148.85 ? 171 LEU   S O   1 
ATOM   33440 C  CB  . LEU   S  5  172 ? 82.337  -212.451 41.632  1.00 142.64 ? 171 LEU   S CB  1 
ATOM   33441 C  CG  . LEU   S  5  172 ? 82.558  -211.741 40.296  1.00 142.22 ? 171 LEU   S CG  1 
ATOM   33442 C  CD1 . LEU   S  5  172 ? 81.247  -211.194 39.756  1.00 139.76 ? 171 LEU   S CD1 1 
ATOM   33443 C  CD2 . LEU   S  5  172 ? 83.584  -210.623 40.425  1.00 142.38 ? 171 LEU   S CD2 1 
ATOM   33444 N  N   . GLU   S  5  173 ? 82.638  -214.729 43.920  1.00 140.51 ? 172 GLU   S N   1 
ATOM   33445 C  CA  . GLU   S  5  173 ? 82.383  -215.223 45.301  1.00 140.61 ? 172 GLU   S CA  1 
ATOM   33446 C  C   . GLU   S  5  173 ? 83.724  -215.578 45.959  1.00 142.19 ? 172 GLU   S C   1 
ATOM   33447 O  O   . GLU   S  5  173 ? 83.877  -215.289 47.161  1.00 135.70 ? 172 GLU   S O   1 
ATOM   33448 C  CB  . GLU   S  5  173 ? 81.419  -216.411 45.277  1.00 142.77 ? 172 GLU   S CB  1 
ATOM   33449 C  CG  . GLU   S  5  173 ? 80.604  -216.555 46.550  1.00 142.39 ? 172 GLU   S CG  1 
ATOM   33450 C  CD  . GLU   S  5  173 ? 79.343  -217.390 46.408  1.00 142.28 ? 172 GLU   S CD  1 
ATOM   33451 O  OE1 . GLU   S  5  173 ? 78.531  -217.392 47.355  1.00 140.50 ? 172 GLU   S OE1 1 
ATOM   33452 O  OE2 . GLU   S  5  173 ? 79.171  -218.030 45.352  1.00 144.85 ? 172 GLU   S OE2 1 
ATOM   33453 N  N   . ARG   S  5  174 ? 84.654  -216.162 45.191  1.00 150.35 ? 173 ARG   S N   1 
ATOM   33454 C  CA  . ARG   S  5  174 ? 86.033  -216.506 45.639  1.00 155.02 ? 173 ARG   S CA  1 
ATOM   33455 C  C   . ARG   S  5  174 ? 86.877  -215.229 45.764  1.00 155.49 ? 173 ARG   S C   1 
ATOM   33456 O  O   . ARG   S  5  174 ? 87.649  -215.135 46.736  1.00 155.10 ? 173 ARG   S O   1 
ATOM   33457 C  CB  . ARG   S  5  174 ? 86.718  -217.469 44.662  1.00 162.53 ? 173 ARG   S CB  1 
ATOM   33458 C  CG  . ARG   S  5  174 ? 86.184  -218.895 44.687  1.00 165.44 ? 173 ARG   S CG  1 
ATOM   33459 C  CD  . ARG   S  5  174 ? 86.854  -219.786 43.651  1.00 170.87 ? 173 ARG   S CD  1 
ATOM   33460 N  NE  . ARG   S  5  174 ? 88.306  -219.617 43.613  1.00 174.24 ? 173 ARG   S NE  1 
ATOM   33461 C  CZ  . ARG   S  5  174 ? 88.993  -218.935 42.691  1.00 171.25 ? 173 ARG   S CZ  1 
ATOM   33462 N  NH1 . ARG   S  5  174 ? 88.380  -218.339 41.680  1.00 168.74 ? 173 ARG   S NH1 1 
ATOM   33463 N  NH2 . ARG   S  5  174 ? 90.310  -218.857 42.784  1.00 173.67 ? 173 ARG   S NH2 1 
ATOM   33464 N  N   . THR   S  5  175 ? 86.739  -214.294 44.817  1.00 152.42 ? 174 THR   S N   1 
ATOM   33465 C  CA  . THR   S  5  175 ? 87.590  -213.076 44.686  1.00 153.87 ? 174 THR   S CA  1 
ATOM   33466 C  C   . THR   S  5  175 ? 87.074  -211.935 45.579  1.00 152.76 ? 174 THR   S C   1 
ATOM   33467 O  O   . THR   S  5  175 ? 87.739  -210.877 45.604  1.00 150.31 ? 174 THR   S O   1 
ATOM   33468 C  CB  . THR   S  5  175 ? 87.668  -212.608 43.225  1.00 153.13 ? 174 THR   S CB  1 
ATOM   33469 O  OG1 . THR   S  5  175 ? 87.633  -213.750 42.368  1.00 152.28 ? 174 THR   S OG1 1 
ATOM   33470 C  CG2 . THR   S  5  175 ? 88.917  -211.806 42.929  1.00 155.23 ? 174 THR   S CG2 1 
ATOM   33471 N  N   . LEU   S  5  176 ? 85.959  -212.134 46.295  1.00 150.89 ? 175 LEU   S N   1 
ATOM   33472 C  CA  . LEU   S  5  176 ? 85.225  -211.065 47.031  1.00 147.81 ? 175 LEU   S CA  1 
ATOM   33473 C  C   . LEU   S  5  176 ? 86.202  -210.189 47.826  1.00 148.47 ? 175 LEU   S C   1 
ATOM   33474 O  O   . LEU   S  5  176 ? 86.147  -208.956 47.659  1.00 151.72 ? 175 LEU   S O   1 
ATOM   33475 C  CB  . LEU   S  5  176 ? 84.176  -211.694 47.955  1.00 145.21 ? 175 LEU   S CB  1 
ATOM   33476 C  CG  . LEU   S  5  176 ? 83.369  -210.714 48.810  1.00 144.22 ? 175 LEU   S CG  1 
ATOM   33477 C  CD1 . LEU   S  5  176 ? 82.801  -209.577 47.971  1.00 143.80 ? 175 LEU   S CD1 1 
ATOM   33478 C  CD2 . LEU   S  5  176 ? 82.251  -211.433 49.549  1.00 141.53 ? 175 LEU   S CD2 1 
ATOM   33479 N  N   . ASP   S  5  177 ? 87.061  -210.803 48.644  1.00 148.15 ? 176 ASP   S N   1 
ATOM   33480 C  CA  . ASP   S  5  177 ? 87.947  -210.096 49.610  1.00 146.80 ? 176 ASP   S CA  1 
ATOM   33481 C  C   . ASP   S  5  177 ? 89.000  -209.265 48.864  1.00 147.64 ? 176 ASP   S C   1 
ATOM   33482 O  O   . ASP   S  5  177 ? 89.429  -208.243 49.430  1.00 146.43 ? 176 ASP   S O   1 
ATOM   33483 C  CB  . ASP   S  5  177 ? 88.598  -211.081 50.584  1.00 146.06 ? 176 ASP   S CB  1 
ATOM   33484 C  CG  . ASP   S  5  177 ? 87.598  -211.775 51.490  1.00 144.80 ? 176 ASP   S CG  1 
ATOM   33485 O  OD1 . ASP   S  5  177 ? 86.779  -211.067 52.109  1.00 143.44 ? 176 ASP   S OD1 1 
ATOM   33486 O  OD2 . ASP   S  5  177 ? 87.637  -213.019 51.558  1.00 142.93 ? 176 ASP   S OD2 1 
ATOM   33487 N  N   . THR   S  5  178 ? 89.401  -209.676 47.654  1.00 149.17 ? 177 THR   S N   1 
ATOM   33488 C  CA  . THR   S  5  178 ? 90.425  -208.976 46.829  1.00 150.97 ? 177 THR   S CA  1 
ATOM   33489 C  C   . THR   S  5  178 ? 89.822  -207.724 46.180  1.00 150.55 ? 177 THR   S C   1 
ATOM   33490 O  O   . THR   S  5  178 ? 90.343  -206.623 46.451  1.00 158.35 ? 177 THR   S O   1 
ATOM   33491 C  CB  . THR   S  5  178 ? 91.027  -209.885 45.749  1.00 149.33 ? 177 THR   S CB  1 
ATOM   33492 O  OG1 . THR   S  5  178 ? 91.516  -211.073 46.373  1.00 151.44 ? 177 THR   S OG1 1 
ATOM   33493 C  CG2 . THR   S  5  178 ? 92.147  -209.216 44.982  1.00 148.76 ? 177 THR   S CG2 1 
ATOM   33494 N  N   . PHE   S  5  179 ? 88.785  -207.883 45.348  1.00 147.05 ? 178 PHE   S N   1 
ATOM   33495 C  CA  . PHE   S  5  179 ? 88.301  -206.829 44.415  1.00 142.83 ? 178 PHE   S CA  1 
ATOM   33496 C  C   . PHE   S  5  179 ? 87.572  -205.713 45.179  1.00 141.31 ? 178 PHE   S C   1 
ATOM   33497 O  O   . PHE   S  5  179 ? 87.550  -204.582 44.653  1.00 140.63 ? 178 PHE   S O   1 
ATOM   33498 C  CB  . PHE   S  5  179 ? 87.456  -207.420 43.279  1.00 142.89 ? 178 PHE   S CB  1 
ATOM   33499 C  CG  . PHE   S  5  179 ? 86.048  -207.835 43.628  1.00 143.35 ? 178 PHE   S CG  1 
ATOM   33500 C  CD1 . PHE   S  5  179 ? 85.038  -206.894 43.779  1.00 144.66 ? 178 PHE   S CD1 1 
ATOM   33501 C  CD2 . PHE   S  5  179 ? 85.717  -209.175 43.753  1.00 144.80 ? 178 PHE   S CD2 1 
ATOM   33502 C  CE1 . PHE   S  5  179 ? 83.741  -207.283 44.083  1.00 142.74 ? 178 PHE   S CE1 1 
ATOM   33503 C  CE2 . PHE   S  5  179 ? 84.419  -209.561 44.051  1.00 143.43 ? 178 PHE   S CE2 1 
ATOM   33504 C  CZ  . PHE   S  5  179 ? 83.434  -208.616 44.219  1.00 140.92 ? 178 PHE   S CZ  1 
ATOM   33505 N  N   . ILE   S  5  180 ? 87.005  -205.999 46.359  1.00 138.14 ? 179 ILE   S N   1 
ATOM   33506 C  CA  . ILE   S  5  180 ? 86.243  -204.996 47.169  1.00 137.39 ? 179 ILE   S CA  1 
ATOM   33507 C  C   . ILE   S  5  180 ? 87.194  -203.885 47.640  1.00 139.43 ? 179 ILE   S C   1 
ATOM   33508 O  O   . ILE   S  5  180 ? 86.710  -202.754 47.850  1.00 135.08 ? 179 ILE   S O   1 
ATOM   33509 C  CB  . ILE   S  5  180 ? 85.480  -205.648 48.347  1.00 135.73 ? 179 ILE   S CB  1 
ATOM   33510 C  CG1 . ILE   S  5  180 ? 84.500  -204.672 49.009  1.00 137.61 ? 179 ILE   S CG1 1 
ATOM   33511 C  CG2 . ILE   S  5  180 ? 86.434  -206.237 49.375  1.00 133.57 ? 179 ILE   S CG2 1 
ATOM   33512 C  CD1 . ILE   S  5  180 ? 83.483  -204.054 48.071  1.00 137.88 ? 179 ILE   S CD1 1 
ATOM   33513 N  N   . LYS   S  5  181 ? 88.491  -204.186 47.789  1.00 142.02 ? 180 LYS   S N   1 
ATOM   33514 C  CA  . LYS   S  5  181 ? 89.520  -203.229 48.283  1.00 145.12 ? 180 LYS   S CA  1 
ATOM   33515 C  C   . LYS   S  5  181 ? 90.400  -202.722 47.129  1.00 144.99 ? 180 LYS   S C   1 
ATOM   33516 O  O   . LYS   S  5  181 ? 91.518  -202.247 47.421  1.00 148.21 ? 180 LYS   S O   1 
ATOM   33517 C  CB  . LYS   S  5  181 ? 90.369  -203.884 49.377  1.00 147.04 ? 180 LYS   S CB  1 
ATOM   33518 C  CG  . LYS   S  5  181 ? 89.701  -203.964 50.745  1.00 145.74 ? 180 LYS   S CG  1 
ATOM   33519 C  CD  . LYS   S  5  181 ? 90.508  -204.703 51.793  1.00 146.61 ? 180 LYS   S CD  1 
ATOM   33520 C  CE  . LYS   S  5  181 ? 91.198  -205.941 51.258  1.00 148.26 ? 180 LYS   S CE  1 
ATOM   33521 N  NZ  . LYS   S  5  181 ? 91.577  -206.874 52.343  1.00 150.55 ? 180 LYS   S NZ  1 
ATOM   33522 N  N   . ILE   S  5  182 ? 89.927  -202.791 45.878  1.00 142.56 ? 181 ILE   S N   1 
ATOM   33523 C  CA  . ILE   S  5  182 ? 90.563  -202.080 44.726  1.00 140.91 ? 181 ILE   S CA  1 
ATOM   33524 C  C   . ILE   S  5  182 ? 89.977  -200.662 44.680  1.00 139.59 ? 181 ILE   S C   1 
ATOM   33525 O  O   . ILE   S  5  182 ? 89.112  -200.386 43.820  1.00 136.24 ? 181 ILE   S O   1 
ATOM   33526 C  CB  . ILE   S  5  182 ? 90.398  -202.842 43.394  1.00 140.38 ? 181 ILE   S CB  1 
ATOM   33527 C  CG1 . ILE   S  5  182 ? 90.876  -204.291 43.518  1.00 143.30 ? 181 ILE   S CG1 1 
ATOM   33528 C  CG2 . ILE   S  5  182 ? 91.119  -202.108 42.269  1.00 138.92 ? 181 ILE   S CG2 1 
ATOM   33529 C  CD1 . ILE   S  5  182 ? 90.650  -205.132 42.280  1.00 146.12 ? 181 ILE   S CD1 1 
ATOM   33530 N  N   . ASP   S  5  183 ? 90.434  -199.811 45.603  1.00 138.57 ? 182 ASP   S N   1 
ATOM   33531 C  CA  . ASP   S  5  183 ? 89.996  -198.400 45.764  1.00 136.46 ? 182 ASP   S CA  1 
ATOM   33532 C  C   . ASP   S  5  183 ? 91.000  -197.488 45.050  1.00 136.65 ? 182 ASP   S C   1 
ATOM   33533 O  O   . ASP   S  5  183 ? 92.215  -197.743 45.158  1.00 132.34 ? 182 ASP   S O   1 
ATOM   33534 C  CB  . ASP   S  5  183 ? 89.854  -198.041 47.246  1.00 137.84 ? 182 ASP   S CB  1 
ATOM   33535 C  CG  . ASP   S  5  183 ? 88.863  -198.916 47.997  1.00 134.67 ? 182 ASP   S CG  1 
ATOM   33536 O  OD1 . ASP   S  5  183 ? 87.878  -199.355 47.373  1.00 132.89 ? 182 ASP   S OD1 1 
ATOM   33537 O  OD2 . ASP   S  5  183 ? 89.089  -199.163 49.198  1.00 136.55 ? 182 ASP   S OD2 1 
ATOM   33538 N  N   . GLY   S  5  184 ? 90.501  -196.470 44.342  1.00 138.67 ? 183 GLY   S N   1 
ATOM   33539 C  CA  . GLY   S  5  184 ? 91.323  -195.474 43.628  1.00 142.79 ? 183 GLY   S CA  1 
ATOM   33540 C  C   . GLY   S  5  184 ? 92.187  -196.110 42.551  1.00 142.77 ? 183 GLY   S C   1 
ATOM   33541 O  O   . GLY   S  5  184 ? 93.313  -195.621 42.337  1.00 147.87 ? 183 GLY   S O   1 
ATOM   33542 N  N   . ASN   S  5  185 ? 91.688  -197.165 41.901  1.00 142.13 ? 184 ASN   S N   1 
ATOM   33543 C  CA  . ASN   S  5  185 ? 92.376  -197.847 40.772  1.00 141.92 ? 184 ASN   S CA  1 
ATOM   33544 C  C   . ASN   S  5  185 ? 91.317  -198.413 39.830  1.00 144.76 ? 184 ASN   S C   1 
ATOM   33545 O  O   . ASN   S  5  185 ? 90.877  -199.547 39.997  1.00 145.44 ? 184 ASN   S O   1 
ATOM   33546 C  CB  . ASN   S  5  185 ? 93.350  -198.919 41.272  1.00 143.08 ? 184 ASN   S CB  1 
ATOM   33547 C  CG  . ASN   S  5  185 ? 94.429  -199.304 40.277  1.00 143.15 ? 184 ASN   S CG  1 
ATOM   33548 O  OD1 . ASN   S  5  185 ? 95.333  -200.060 40.623  1.00 144.81 ? 184 ASN   S OD1 1 
ATOM   33549 N  ND2 . ASN   S  5  185 ? 94.366  -198.804 39.051  1.00 141.52 ? 184 ASN   S ND2 1 
ATOM   33550 N  N   . PRO   S  5  186 ? 90.857  -197.621 38.835  1.00 145.47 ? 185 PRO   S N   1 
ATOM   33551 C  CA  . PRO   S  5  186 ? 89.878  -198.090 37.852  1.00 146.93 ? 185 PRO   S CA  1 
ATOM   33552 C  C   . PRO   S  5  186 ? 90.323  -199.320 37.042  1.00 153.18 ? 185 PRO   S C   1 
ATOM   33553 O  O   . PRO   S  5  186 ? 89.579  -200.285 37.005  1.00 152.93 ? 185 PRO   S O   1 
ATOM   33554 C  CB  . PRO   S  5  186 ? 89.705  -196.881 36.918  1.00 144.43 ? 185 PRO   S CB  1 
ATOM   33555 C  CG  . PRO   S  5  186 ? 90.082  -195.695 37.773  1.00 143.31 ? 185 PRO   S CG  1 
ATOM   33556 C  CD  . PRO   S  5  186 ? 91.210  -196.207 38.641  1.00 143.38 ? 185 PRO   S CD  1 
ATOM   33557 N  N   . ASP   S  5  187 ? 91.511  -199.258 36.427  1.00 157.98 ? 186 ASP   S N   1 
ATOM   33558 C  CA  . ASP   S  5  187 ? 92.020  -200.272 35.460  1.00 160.31 ? 186 ASP   S CA  1 
ATOM   33559 C  C   . ASP   S  5  187 ? 92.115  -201.655 36.122  1.00 162.40 ? 186 ASP   S C   1 
ATOM   33560 O  O   . ASP   S  5  187 ? 91.934  -202.655 35.398  1.00 169.08 ? 186 ASP   S O   1 
ATOM   33561 C  CB  . ASP   S  5  187 ? 93.365  -199.850 34.860  1.00 162.22 ? 186 ASP   S CB  1 
ATOM   33562 C  CG  . ASP   S  5  187 ? 93.246  -198.773 33.795  1.00 158.38 ? 186 ASP   S CG  1 
ATOM   33563 O  OD1 . ASP   S  5  187 ? 92.246  -198.028 33.821  1.00 154.98 ? 186 ASP   S OD1 1 
ATOM   33564 O  OD2 . ASP   S  5  187 ? 94.152  -198.692 32.943  1.00 164.21 ? 186 ASP   S OD2 1 
ATOM   33565 N  N   . GLU   S  5  188 ? 92.388  -201.716 37.431  1.00 162.56 ? 187 GLU   S N   1 
ATOM   33566 C  CA  . GLU   S  5  188 ? 92.514  -202.990 38.195  1.00 157.96 ? 187 GLU   S CA  1 
ATOM   33567 C  C   . GLU   S  5  188 ? 91.124  -203.575 38.477  1.00 149.25 ? 187 GLU   S C   1 
ATOM   33568 O  O   . GLU   S  5  188 ? 90.995  -204.813 38.423  1.00 149.32 ? 187 GLU   S O   1 
ATOM   33569 C  CB  . GLU   S  5  188 ? 93.301  -202.787 39.494  1.00 156.53 ? 187 GLU   S CB  1 
ATOM   33570 C  CG  . GLU   S  5  188 ? 94.808  -202.848 39.308  1.00 159.17 ? 187 GLU   S CG  1 
ATOM   33571 C  CD  . GLU   S  5  188 ? 95.324  -204.138 38.690  1.00 158.02 ? 187 GLU   S CD  1 
ATOM   33572 O  OE1 . GLU   S  5  188 ? 96.172  -204.057 37.782  1.00 164.42 ? 187 GLU   S OE1 1 
ATOM   33573 O  OE2 . GLU   S  5  188 ? 94.875  -205.221 39.118  1.00 153.30 ? 187 GLU   S OE2 1 
ATOM   33574 N  N   . LEU   S  5  189 ? 90.129  -202.731 38.771  1.00 144.12 ? 188 LEU   S N   1 
ATOM   33575 C  CA  . LEU   S  5  189 ? 88.732  -203.172 39.047  1.00 139.18 ? 188 LEU   S CA  1 
ATOM   33576 C  C   . LEU   S  5  189 ? 88.124  -203.742 37.759  1.00 141.42 ? 188 LEU   S C   1 
ATOM   33577 O  O   . LEU   S  5  189 ? 87.324  -204.693 37.860  1.00 138.92 ? 188 LEU   S O   1 
ATOM   33578 C  CB  . LEU   S  5  189 ? 87.894  -201.998 39.568  1.00 134.77 ? 188 LEU   S CB  1 
ATOM   33579 C  CG  . LEU   S  5  189 ? 87.007  -202.282 40.782  1.00 131.42 ? 188 LEU   S CG  1 
ATOM   33580 C  CD1 . LEU   S  5  189 ? 85.955  -201.198 40.932  1.00 129.82 ? 188 LEU   S CD1 1 
ATOM   33581 C  CD2 . LEU   S  5  189 ? 86.336  -203.646 40.708  1.00 129.76 ? 188 LEU   S CD2 1 
ATOM   33582 N  N   . ILE   S  5  190 ? 88.485  -203.171 36.603  1.00 143.50 ? 189 ILE   S N   1 
ATOM   33583 C  CA  . ILE   S  5  190 ? 88.040  -203.632 35.252  1.00 146.44 ? 189 ILE   S CA  1 
ATOM   33584 C  C   . ILE   S  5  190 ? 88.681  -204.998 34.968  1.00 150.91 ? 189 ILE   S C   1 
ATOM   33585 O  O   . ILE   S  5  190 ? 87.941  -205.921 34.573  1.00 155.61 ? 189 ILE   S O   1 
ATOM   33586 C  CB  . ILE   S  5  190 ? 88.368  -202.591 34.159  1.00 144.57 ? 189 ILE   S CB  1 
ATOM   33587 C  CG1 . ILE   S  5  190 ? 87.607  -201.279 34.378  1.00 141.92 ? 189 ILE   S CG1 1 
ATOM   33588 C  CG2 . ILE   S  5  190 ? 88.101  -203.159 32.772  1.00 144.85 ? 189 ILE   S CG2 1 
ATOM   33589 C  CD1 . ILE   S  5  190 ? 88.150  -200.106 33.592  1.00 142.34 ? 189 ILE   S CD1 1 
ATOM   33590 N  N   . LYS   S  5  191 ? 90.000  -205.117 35.171  1.00 151.32 ? 190 LYS   S N   1 
ATOM   33591 C  CA  . LYS   S  5  191 ? 90.780  -206.373 34.974  1.00 150.08 ? 190 LYS   S CA  1 
ATOM   33592 C  C   . LYS   S  5  191 ? 90.113  -207.528 35.736  1.00 149.47 ? 190 LYS   S C   1 
ATOM   33593 O  O   . LYS   S  5  191 ? 90.027  -208.632 35.162  1.00 151.02 ? 190 LYS   S O   1 
ATOM   33594 C  CB  . LYS   S  5  191 ? 92.235  -206.192 35.421  1.00 147.93 ? 190 LYS   S CB  1 
ATOM   33595 C  CG  . LYS   S  5  191 ? 93.185  -205.707 34.335  1.00 147.35 ? 190 LYS   S CG  1 
ATOM   33596 C  CD  . LYS   S  5  191 ? 94.617  -205.563 34.802  1.00 148.15 ? 190 LYS   S CD  1 
ATOM   33597 C  CE  . LYS   S  5  191 ? 95.607  -205.523 33.658  1.00 149.03 ? 190 LYS   S CE  1 
ATOM   33598 N  NZ  . LYS   S  5  191 ? 96.994  -205.311 34.137  1.00 150.05 ? 190 LYS   S NZ  1 
ATOM   33599 N  N   . ALA   S  5  192 ? 89.664  -207.279 36.972  1.00 148.53 ? 191 ALA   S N   1 
ATOM   33600 C  CA  . ALA   S  5  192 ? 88.973  -208.258 37.847  1.00 148.56 ? 191 ALA   S CA  1 
ATOM   33601 C  C   . ALA   S  5  192 ? 87.622  -208.645 37.233  1.00 148.10 ? 191 ALA   S C   1 
ATOM   33602 O  O   . ALA   S  5  192 ? 87.259  -209.836 37.316  1.00 154.44 ? 191 ALA   S O   1 
ATOM   33603 C  CB  . ALA   S  5  192 ? 88.798  -207.689 39.235  1.00 147.52 ? 191 ALA   S CB  1 
ATOM   33604 N  N   . GLY   S  5  193 ? 86.910  -207.672 36.655  1.00 145.49 ? 192 GLY   S N   1 
ATOM   33605 C  CA  . GLY   S  5  193 ? 85.616  -207.868 35.972  1.00 143.76 ? 192 GLY   S CA  1 
ATOM   33606 C  C   . GLY   S  5  193 ? 85.771  -208.595 34.646  1.00 146.56 ? 192 GLY   S C   1 
ATOM   33607 O  O   . GLY   S  5  193 ? 84.853  -209.358 34.290  1.00 148.88 ? 192 GLY   S O   1 
ATOM   33608 N  N   . VAL   S  5  194 ? 86.877  -208.358 33.930  1.00 149.71 ? 193 VAL   S N   1 
ATOM   33609 C  CA  . VAL   S  5  194 ? 87.196  -209.014 32.624  1.00 151.98 ? 193 VAL   S CA  1 
ATOM   33610 C  C   . VAL   S  5  194 ? 87.631  -210.464 32.885  1.00 152.65 ? 193 VAL   S C   1 
ATOM   33611 O  O   . VAL   S  5  194 ? 87.303  -211.331 32.053  1.00 150.69 ? 193 VAL   S O   1 
ATOM   33612 C  CB  . VAL   S  5  194 ? 88.262  -208.227 31.835  1.00 152.28 ? 193 VAL   S CB  1 
ATOM   33613 C  CG1 . VAL   S  5  194 ? 88.744  -208.982 30.605  1.00 154.83 ? 193 VAL   S CG1 1 
ATOM   33614 C  CG2 . VAL   S  5  194 ? 87.753  -206.850 31.437  1.00 150.18 ? 193 VAL   S CG2 1 
ATOM   33615 N  N   . GLU   S  5  195 ? 88.346  -210.715 33.987  1.00 154.53 ? 194 GLU   S N   1 
ATOM   33616 C  CA  . GLU   S  5  195 ? 88.747  -212.082 34.420  1.00 156.99 ? 194 GLU   S CA  1 
ATOM   33617 C  C   . GLU   S  5  195 ? 87.507  -212.849 34.894  1.00 155.09 ? 194 GLU   S C   1 
ATOM   33618 O  O   . GLU   S  5  195 ? 87.455  -214.074 34.668  1.00 158.26 ? 194 GLU   S O   1 
ATOM   33619 C  CB  . GLU   S  5  195 ? 89.805  -212.023 35.523  1.00 162.95 ? 194 GLU   S CB  1 
ATOM   33620 C  CG  . GLU   S  5  195 ? 90.310  -213.394 35.939  1.00 168.11 ? 194 GLU   S CG  1 
ATOM   33621 C  CD  . GLU   S  5  195 ? 91.635  -213.387 36.680  1.00 174.49 ? 194 GLU   S CD  1 
ATOM   33622 O  OE1 . GLU   S  5  195 ? 91.668  -213.859 37.834  1.00 180.74 ? 194 GLU   S OE1 1 
ATOM   33623 O  OE2 . GLU   S  5  195 ? 92.633  -212.919 36.098  1.00 183.14 ? 194 GLU   S OE2 1 
ATOM   33624 N  N   . ALA   S  5  196 ? 86.557  -212.158 35.531  1.00 151.83 ? 195 ALA   S N   1 
ATOM   33625 C  CA  . ALA   S  5  196 ? 85.282  -212.730 36.026  1.00 151.37 ? 195 ALA   S CA  1 
ATOM   33626 C  C   . ALA   S  5  196 ? 84.469  -213.277 34.847  1.00 149.17 ? 195 ALA   S C   1 
ATOM   33627 O  O   . ALA   S  5  196 ? 84.062  -214.454 34.914  1.00 149.98 ? 195 ALA   S O   1 
ATOM   33628 C  CB  . ALA   S  5  196 ? 84.505  -211.694 36.803  1.00 148.13 ? 195 ALA   S CB  1 
ATOM   33629 N  N   . ILE   S  5  197 ? 84.266  -212.465 33.802  1.00 148.60 ? 196 ILE   S N   1 
ATOM   33630 C  CA  . ILE   S  5  197 ? 83.431  -212.818 32.612  1.00 147.65 ? 196 ILE   S CA  1 
ATOM   33631 C  C   . ILE   S  5  197 ? 84.127  -213.915 31.795  1.00 150.47 ? 196 ILE   S C   1 
ATOM   33632 O  O   . ILE   S  5  197 ? 83.422  -214.619 31.044  1.00 154.30 ? 196 ILE   S O   1 
ATOM   33633 C  CB  . ILE   S  5  197 ? 83.108  -211.579 31.749  1.00 145.94 ? 196 ILE   S CB  1 
ATOM   33634 C  CG1 . ILE   S  5  197 ? 81.882  -211.821 30.863  1.00 148.15 ? 196 ILE   S CG1 1 
ATOM   33635 C  CG2 . ILE   S  5  197 ? 84.313  -211.135 30.931  1.00 145.22 ? 196 ILE   S CG2 1 
ATOM   33636 C  CD1 . ILE   S  5  197 ? 81.240  -210.559 30.334  1.00 146.67 ? 196 ILE   S CD1 1 
ATOM   33637 N  N   . SER   S  5  198 ? 85.452  -214.053 31.927  1.00 148.96 ? 197 SER   S N   1 
ATOM   33638 C  CA  . SER   S  5  198 ? 86.269  -215.070 31.212  1.00 149.99 ? 197 SER   S CA  1 
ATOM   33639 C  C   . SER   S  5  198 ? 85.941  -216.484 31.714  1.00 152.91 ? 197 SER   S C   1 
ATOM   33640 O  O   . SER   S  5  198 ? 86.268  -217.446 30.990  1.00 155.75 ? 197 SER   S O   1 
ATOM   33641 C  CB  . SER   S  5  198 ? 87.740  -214.777 31.330  1.00 148.95 ? 197 SER   S CB  1 
ATOM   33642 O  OG  . SER   S  5  198 ? 88.061  -213.553 30.689  1.00 146.36 ? 197 SER   S OG  1 
ATOM   33643 N  N   . GLN   S  5  199 ? 85.318  -216.604 32.893  1.00 152.60 ? 198 GLN   S N   1 
ATOM   33644 C  CA  . GLN   S  5  199 ? 84.914  -217.901 33.505  1.00 152.43 ? 198 GLN   S CA  1 
ATOM   33645 C  C   . GLN   S  5  199 ? 83.567  -218.365 32.933  1.00 149.92 ? 198 GLN   S C   1 
ATOM   33646 O  O   . GLN   S  5  199 ? 83.108  -219.451 33.341  1.00 151.23 ? 198 GLN   S O   1 
ATOM   33647 C  CB  . GLN   S  5  199 ? 84.821  -217.783 35.030  1.00 151.40 ? 198 GLN   S CB  1 
ATOM   33648 C  CG  . GLN   S  5  199 ? 86.048  -217.164 35.688  1.00 151.84 ? 198 GLN   S CG  1 
ATOM   33649 C  CD  . GLN   S  5  199 ? 87.341  -217.817 35.264  1.00 153.22 ? 198 GLN   S CD  1 
ATOM   33650 O  OE1 . GLN   S  5  199 ? 87.479  -219.038 35.295  1.00 152.06 ? 198 GLN   S OE1 1 
ATOM   33651 N  NE2 . GLN   S  5  199 ? 88.309  -217.004 34.871  1.00 154.06 ? 198 GLN   S NE2 1 
ATOM   33652 N  N   . SER   S  5  200 ? 82.957  -217.583 32.033  1.00 149.74 ? 199 SER   S N   1 
ATOM   33653 C  CA  . SER   S  5  200 ? 81.630  -217.856 31.419  1.00 147.41 ? 199 SER   S CA  1 
ATOM   33654 C  C   . SER   S  5  200 ? 81.751  -218.082 29.905  1.00 146.83 ? 199 SER   S C   1 
ATOM   33655 O  O   . SER   S  5  200 ? 80.699  -218.266 29.259  1.00 140.24 ? 199 SER   S O   1 
ATOM   33656 C  CB  . SER   S  5  200 ? 80.672  -216.731 31.719  1.00 146.30 ? 199 SER   S CB  1 
ATOM   33657 O  OG  . SER   S  5  200 ? 80.554  -216.519 33.119  1.00 146.50 ? 199 SER   S OG  1 
ATOM   33658 N  N   . LEU   S  5  201 ? 82.974  -218.078 29.359  1.00 149.89 ? 200 LEU   S N   1 
ATOM   33659 C  CA  . LEU   S  5  201 ? 83.242  -218.236 27.902  1.00 155.19 ? 200 LEU   S CA  1 
ATOM   33660 C  C   . LEU   S  5  201 ? 83.369  -219.724 27.553  1.00 157.73 ? 200 LEU   S C   1 
ATOM   33661 O  O   . LEU   S  5  201 ? 83.932  -220.477 28.371  1.00 162.65 ? 200 LEU   S O   1 
ATOM   33662 C  CB  . LEU   S  5  201 ? 84.533  -217.496 27.539  1.00 156.50 ? 200 LEU   S CB  1 
ATOM   33663 C  CG  . LEU   S  5  201 ? 84.533  -215.986 27.771  1.00 155.26 ? 200 LEU   S CG  1 
ATOM   33664 C  CD1 . LEU   S  5  201 ? 85.937  -215.427 27.604  1.00 156.87 ? 200 LEU   S CD1 1 
ATOM   33665 C  CD2 . LEU   S  5  201 ? 83.562  -215.283 26.832  1.00 152.16 ? 200 LEU   S CD2 1 
ATOM   33666 N  N   . ARG   S  5  202 ? 82.878  -220.116 26.372  1.00 161.64 ? 201 ARG   S N   1 
ATOM   33667 C  CA  . ARG   S  5  202 ? 82.992  -221.492 25.813  1.00 166.87 ? 201 ARG   S CA  1 
ATOM   33668 C  C   . ARG   S  5  202 ? 83.238  -221.404 24.303  1.00 165.98 ? 201 ARG   S C   1 
ATOM   33669 O  O   . ARG   S  5  202 ? 82.355  -220.888 23.593  1.00 161.19 ? 201 ARG   S O   1 
ATOM   33670 C  CB  . ARG   S  5  202 ? 81.723  -222.302 26.099  1.00 166.93 ? 201 ARG   S CB  1 
ATOM   33671 C  CG  . ARG   S  5  202 ? 81.602  -222.788 27.537  1.00 172.70 ? 201 ARG   S CG  1 
ATOM   33672 C  CD  . ARG   S  5  202 ? 81.927  -224.262 27.695  1.00 174.43 ? 201 ARG   S CD  1 
ATOM   33673 N  NE  . ARG   S  5  202 ? 80.759  -225.098 27.444  1.00 176.79 ? 201 ARG   S NE  1 
ATOM   33674 C  CZ  . ARG   S  5  202 ? 79.777  -225.327 28.316  1.00 178.87 ? 201 ARG   S CZ  1 
ATOM   33675 N  NH1 . ARG   S  5  202 ? 79.803  -224.784 29.523  1.00 179.04 ? 201 ARG   S NH1 1 
ATOM   33676 N  NH2 . ARG   S  5  202 ? 78.763  -226.104 27.975  1.00 177.32 ? 201 ARG   S NH2 1 
ATOM   33677 N  N   . ASP   S  5  203 ? 84.407  -221.868 23.847  1.00 172.34 ? 202 ASP   S N   1 
ATOM   33678 C  CA  . ASP   S  5  203 ? 84.819  -221.941 22.415  1.00 179.94 ? 202 ASP   S CA  1 
ATOM   33679 C  C   . ASP   S  5  203 ? 85.099  -220.537 21.855  1.00 174.13 ? 202 ASP   S C   1 
ATOM   33680 O  O   . ASP   S  5  203 ? 85.869  -220.449 20.879  1.00 177.77 ? 202 ASP   S O   1 
ATOM   33681 C  CB  . ASP   S  5  203 ? 83.787  -222.692 21.566  1.00 184.03 ? 202 ASP   S CB  1 
ATOM   33682 C  CG  . ASP   S  5  203 ? 83.670  -224.167 21.912  1.00 188.58 ? 202 ASP   S CG  1 
ATOM   33683 O  OD1 . ASP   S  5  203 ? 83.329  -224.470 23.073  1.00 194.29 ? 202 ASP   S OD1 1 
ATOM   33684 O  OD2 . ASP   S  5  203 ? 83.928  -225.002 21.020  1.00 191.04 ? 202 ASP   S OD2 1 
ATOM   33685 N  N   . GLU   S  5  204 ? 84.507  -219.487 22.434  1.00 170.07 ? 203 GLU   S N   1 
ATOM   33686 C  CA  . GLU   S  5  204 ? 84.715  -218.069 22.036  1.00 169.74 ? 203 GLU   S CA  1 
ATOM   33687 C  C   . GLU   S  5  204 ? 85.591  -217.382 23.090  1.00 171.14 ? 203 GLU   S C   1 
ATOM   33688 O  O   . GLU   S  5  204 ? 85.486  -217.758 24.273  1.00 164.97 ? 203 GLU   S O   1 
ATOM   33689 C  CB  . GLU   S  5  204 ? 83.365  -217.362 21.897  1.00 168.24 ? 203 GLU   S CB  1 
ATOM   33690 C  CG  . GLU   S  5  204 ? 83.443  -216.030 21.169  1.00 165.72 ? 203 GLU   S CG  1 
ATOM   33691 C  CD  . GLU   S  5  204 ? 82.140  -215.250 21.113  1.00 162.45 ? 203 GLU   S CD  1 
ATOM   33692 O  OE1 . GLU   S  5  204 ? 82.012  -214.382 20.227  1.00 159.28 ? 203 GLU   S OE1 1 
ATOM   33693 O  OE2 . GLU   S  5  204 ? 81.260  -215.502 21.961  1.00 160.09 ? 203 GLU   S OE2 1 
ATOM   33694 N  N   . SER   S  5  205 ? 86.424  -216.422 22.671  1.00 173.70 ? 204 SER   S N   1 
ATOM   33695 C  CA  . SER   S  5  205 ? 87.272  -215.577 23.556  1.00 174.78 ? 204 SER   S CA  1 
ATOM   33696 C  C   . SER   S  5  205 ? 86.960  -214.094 23.315  1.00 173.00 ? 204 SER   S C   1 
ATOM   33697 O  O   . SER   S  5  205 ? 86.341  -213.782 22.276  1.00 177.87 ? 204 SER   S O   1 
ATOM   33698 C  CB  . SER   S  5  205 ? 88.739  -215.883 23.366  1.00 177.13 ? 204 SER   S CB  1 
ATOM   33699 O  OG  . SER   S  5  205 ? 89.114  -215.772 22.001  1.00 177.95 ? 204 SER   S OG  1 
ATOM   33700 N  N   . LEU   S  5  206 ? 87.369  -213.222 24.247  1.00 167.90 ? 205 LEU   S N   1 
ATOM   33701 C  CA  . LEU   S  5  206 ? 87.056  -211.765 24.239  1.00 160.43 ? 205 LEU   S CA  1 
ATOM   33702 C  C   . LEU   S  5  206 ? 87.872  -211.073 23.140  1.00 157.63 ? 205 LEU   S C   1 
ATOM   33703 O  O   . LEU   S  5  206 ? 89.114  -211.046 23.255  1.00 153.84 ? 205 LEU   S O   1 
ATOM   33704 C  CB  . LEU   S  5  206 ? 87.374  -211.152 25.609  1.00 156.42 ? 205 LEU   S CB  1 
ATOM   33705 C  CG  . LEU   S  5  206 ? 86.650  -211.756 26.812  1.00 154.50 ? 205 LEU   S CG  1 
ATOM   33706 C  CD1 . LEU   S  5  206 ? 87.168  -211.148 28.107  1.00 153.57 ? 205 LEU   S CD1 1 
ATOM   33707 C  CD2 . LEU   S  5  206 ? 85.143  -211.575 26.707  1.00 151.08 ? 205 LEU   S CD2 1 
ATOM   33708 N  N   . THR   S  5  207 ? 87.190  -210.539 22.121  1.00 155.42 ? 206 THR   S N   1 
ATOM   33709 C  CA  . THR   S  5  207 ? 87.783  -209.763 20.997  1.00 156.40 ? 206 THR   S CA  1 
ATOM   33710 C  C   . THR   S  5  207 ? 87.458  -208.276 21.196  1.00 155.00 ? 206 THR   S C   1 
ATOM   33711 O  O   . THR   S  5  207 ? 86.850  -207.942 22.233  1.00 154.93 ? 206 THR   S O   1 
ATOM   33712 C  CB  . THR   S  5  207 ? 87.308  -210.287 19.635  1.00 156.77 ? 206 THR   S CB  1 
ATOM   33713 O  OG1 . THR   S  5  207 ? 86.039  -209.709 19.329  1.00 154.46 ? 206 THR   S OG1 1 
ATOM   33714 C  CG2 . THR   S  5  207 ? 87.207  -211.796 19.579  1.00 157.66 ? 206 THR   S CG2 1 
ATOM   33715 N  N   . VAL   S  5  208 ? 87.836  -207.429 20.232  1.00 159.62 ? 207 VAL   S N   1 
ATOM   33716 C  CA  . VAL   S  5  208 ? 87.833  -205.939 20.359  1.00 157.05 ? 207 VAL   S CA  1 
ATOM   33717 C  C   . VAL   S  5  208 ? 86.427  -205.383 20.085  1.00 152.37 ? 207 VAL   S C   1 
ATOM   33718 O  O   . VAL   S  5  208 ? 86.113  -204.311 20.633  1.00 150.07 ? 207 VAL   S O   1 
ATOM   33719 C  CB  . VAL   S  5  208 ? 88.892  -205.298 19.438  1.00 161.19 ? 207 VAL   S CB  1 
ATOM   33720 C  CG1 . VAL   S  5  208 ? 88.377  -205.082 18.021  1.00 161.15 ? 207 VAL   S CG1 1 
ATOM   33721 C  CG2 . VAL   S  5  208 ? 89.420  -203.995 20.019  1.00 158.37 ? 207 VAL   S CG2 1 
ATOM   33722 N  N   . ASP   S  5  209 ? 85.623  -206.069 19.266  1.00 151.57 ? 208 ASP   S N   1 
ATOM   33723 C  CA  . ASP   S  5  209 ? 84.227  -205.670 18.926  1.00 150.26 ? 208 ASP   S CA  1 
ATOM   33724 C  C   . ASP   S  5  209 ? 83.250  -206.626 19.626  1.00 150.80 ? 208 ASP   S C   1 
ATOM   33725 O  O   . ASP   S  5  209 ? 82.069  -206.661 19.235  1.00 148.01 ? 208 ASP   S O   1 
ATOM   33726 C  CB  . ASP   S  5  209 ? 84.016  -205.613 17.409  1.00 148.85 ? 208 ASP   S CB  1 
ATOM   33727 C  CG  . ASP   S  5  209 ? 84.806  -206.647 16.628  1.00 150.11 ? 208 ASP   S CG  1 
ATOM   33728 O  OD1 . ASP   S  5  209 ? 84.788  -207.824 17.032  1.00 149.60 ? 208 ASP   S OD1 1 
ATOM   33729 O  OD2 . ASP   S  5  209 ? 85.445  -206.260 15.631  1.00 153.36 ? 208 ASP   S OD2 1 
ATOM   33730 N  N   . ASN   S  5  210 ? 83.734  -207.347 20.640  1.00 155.58 ? 209 ASN   S N   1 
ATOM   33731 C  CA  . ASN   S  5  210 ? 82.993  -208.393 21.396  1.00 163.92 ? 209 ASN   S CA  1 
ATOM   33732 C  C   . ASN   S  5  210 ? 82.776  -207.924 22.841  1.00 162.01 ? 209 ASN   S C   1 
ATOM   33733 O  O   . ASN   S  5  210 ? 81.713  -208.244 23.414  1.00 161.75 ? 209 ASN   S O   1 
ATOM   33734 C  CB  . ASN   S  5  210 ? 83.757  -209.719 21.334  1.00 171.97 ? 209 ASN   S CB  1 
ATOM   33735 C  CG  . ASN   S  5  210 ? 83.051  -210.886 21.993  1.00 177.60 ? 209 ASN   S CG  1 
ATOM   33736 O  OD1 . ASN   S  5  210 ? 81.830  -210.890 22.125  1.00 184.98 ? 209 ASN   S OD1 1 
ATOM   33737 N  ND2 . ASN   S  5  210 ? 83.813  -211.897 22.383  1.00 181.36 ? 209 ASN   S ND2 1 
ATOM   33738 N  N   . LEU   S  5  211 ? 83.742  -207.183 23.397  1.00 160.69 ? 210 LEU   S N   1 
ATOM   33739 C  CA  . LEU   S  5  211 ? 83.816  -206.809 24.835  1.00 155.48 ? 210 LEU   S CA  1 
ATOM   33740 C  C   . LEU   S  5  211 ? 83.238  -205.404 25.029  1.00 149.83 ? 210 LEU   S C   1 
ATOM   33741 O  O   . LEU   S  5  211 ? 83.569  -204.508 24.225  1.00 142.97 ? 210 LEU   S O   1 
ATOM   33742 C  CB  . LEU   S  5  211 ? 85.283  -206.884 25.277  1.00 158.01 ? 210 LEU   S CB  1 
ATOM   33743 C  CG  . LEU   S  5  211 ? 85.575  -206.575 26.746  1.00 158.25 ? 210 LEU   S CG  1 
ATOM   33744 C  CD1 . LEU   S  5  211 ? 84.835  -207.527 27.676  1.00 156.63 ? 210 LEU   S CD1 1 
ATOM   33745 C  CD2 . LEU   S  5  211 ? 87.072  -206.638 27.012  1.00 160.51 ? 210 LEU   S CD2 1 
ATOM   33746 N  N   . SER   S  5  212 ? 82.401  -205.236 26.058  1.00 146.47 ? 211 SER   S N   1 
ATOM   33747 C  CA  . SER   S  5  212 ? 81.786  -203.948 26.471  1.00 144.46 ? 211 SER   S CA  1 
ATOM   33748 C  C   . SER   S  5  212 ? 82.016  -203.735 27.969  1.00 142.24 ? 211 SER   S C   1 
ATOM   33749 O  O   . SER   S  5  212 ? 81.597  -204.605 28.759  1.00 139.06 ? 211 SER   S O   1 
ATOM   33750 C  CB  . SER   S  5  212 ? 80.319  -203.914 26.137  1.00 141.84 ? 211 SER   S CB  1 
ATOM   33751 O  OG  . SER   S  5  212 ? 79.865  -202.576 26.005  1.00 142.13 ? 211 SER   S OG  1 
ATOM   33752 N  N   . ILE   S  5  213 ? 82.663  -202.624 28.333  1.00 140.38 ? 212 ILE   S N   1 
ATOM   33753 C  CA  . ILE   S  5  213 ? 82.990  -202.253 29.742  1.00 139.76 ? 212 ILE   S CA  1 
ATOM   33754 C  C   . ILE   S  5  213 ? 82.396  -200.871 30.025  1.00 139.49 ? 212 ILE   S C   1 
ATOM   33755 O  O   . ILE   S  5  213 ? 82.510  -199.988 29.151  1.00 142.97 ? 212 ILE   S O   1 
ATOM   33756 C  CB  . ILE   S  5  213 ? 84.513  -202.283 29.987  1.00 141.13 ? 212 ILE   S CB  1 
ATOM   33757 C  CG1 . ILE   S  5  213 ? 85.112  -203.655 29.665  1.00 142.65 ? 212 ILE   S CG1 1 
ATOM   33758 C  CG2 . ILE   S  5  213 ? 84.844  -201.849 31.409  1.00 137.43 ? 212 ILE   S CG2 1 
ATOM   33759 C  CD1 . ILE   S  5  213 ? 86.602  -203.632 29.417  1.00 146.44 ? 212 ILE   S CD1 1 
ATOM   33760 N  N   . ALA   S  5  214 ? 81.783  -200.706 31.200  1.00 137.56 ? 213 ALA   S N   1 
ATOM   33761 C  CA  . ALA   S  5  214 ? 81.295  -199.415 31.737  1.00 132.05 ? 213 ALA   S CA  1 
ATOM   33762 C  C   . ALA   S  5  214 ? 81.864  -199.216 33.143  1.00 129.33 ? 213 ALA   S C   1 
ATOM   33763 O  O   . ALA   S  5  214 ? 82.093  -200.226 33.837  1.00 132.16 ? 213 ALA   S O   1 
ATOM   33764 C  CB  . ALA   S  5  214 ? 79.789  -199.387 31.744  1.00 130.27 ? 213 ALA   S CB  1 
ATOM   33765 N  N   . ILE   S  5  215 ? 82.092  -197.960 33.534  1.00 125.93 ? 214 ILE   S N   1 
ATOM   33766 C  CA  . ILE   S  5  215 ? 82.622  -197.593 34.879  1.00 122.96 ? 214 ILE   S CA  1 
ATOM   33767 C  C   . ILE   S  5  215 ? 81.985  -196.283 35.347  1.00 121.60 ? 214 ILE   S C   1 
ATOM   33768 O  O   . ILE   S  5  215 ? 81.787  -195.374 34.515  1.00 116.79 ? 214 ILE   S O   1 
ATOM   33769 C  CB  . ILE   S  5  215 ? 84.161  -197.499 34.880  1.00 122.18 ? 214 ILE   S CB  1 
ATOM   33770 C  CG1 . ILE   S  5  215 ? 84.692  -197.232 36.291  1.00 122.52 ? 214 ILE   S CG1 1 
ATOM   33771 C  CG2 . ILE   S  5  215 ? 84.655  -196.459 33.884  1.00 119.06 ? 214 ILE   S CG2 1 
ATOM   33772 C  CD1 . ILE   S  5  215 ? 86.150  -197.563 36.472  1.00 125.20 ? 214 ILE   S CD1 1 
ATOM   33773 N  N   . VAL   S  5  216 ? 81.689  -196.215 36.645  1.00 120.69 ? 215 VAL   S N   1 
ATOM   33774 C  CA  . VAL   S  5  216 ? 81.268  -194.983 37.372  1.00 122.87 ? 215 VAL   S CA  1 
ATOM   33775 C  C   . VAL   S  5  216 ? 81.964  -195.007 38.735  1.00 124.19 ? 215 VAL   S C   1 
ATOM   33776 O  O   . VAL   S  5  216 ? 82.255  -196.115 39.223  1.00 127.83 ? 215 VAL   S O   1 
ATOM   33777 C  CB  . VAL   S  5  216 ? 79.734  -194.901 37.500  1.00 124.66 ? 215 VAL   S CB  1 
ATOM   33778 C  CG1 . VAL   S  5  216 ? 79.174  -195.967 38.431  1.00 124.94 ? 215 VAL   S CG1 1 
ATOM   33779 C  CG2 . VAL   S  5  216 ? 79.276  -193.516 37.929  1.00 125.58 ? 215 VAL   S CG2 1 
ATOM   33780 N  N   . GLY   S  5  217 ? 82.243  -193.838 39.315  1.00 124.22 ? 216 GLY   S N   1 
ATOM   33781 C  CA  . GLY   S  5  217 ? 82.907  -193.747 40.628  1.00 125.23 ? 216 GLY   S CA  1 
ATOM   33782 C  C   . GLY   S  5  217 ? 83.099  -192.319 41.100  1.00 125.16 ? 216 GLY   S C   1 
ATOM   33783 O  O   . GLY   S  5  217 ? 82.495  -191.406 40.507  1.00 124.15 ? 216 GLY   S O   1 
ATOM   33784 N  N   . LYS   S  5  218 ? 83.936  -192.150 42.127  1.00 124.28 ? 217 LYS   S N   1 
ATOM   33785 C  CA  . LYS   S  5  218 ? 84.086  -190.906 42.927  1.00 128.25 ? 217 LYS   S CA  1 
ATOM   33786 C  C   . LYS   S  5  218 ? 84.374  -189.712 42.010  1.00 131.15 ? 217 LYS   S C   1 
ATOM   33787 O  O   . LYS   S  5  218 ? 83.655  -188.699 42.125  1.00 135.55 ? 217 LYS   S O   1 
ATOM   33788 C  CB  . LYS   S  5  218 ? 85.195  -191.076 43.967  1.00 128.56 ? 217 LYS   S CB  1 
ATOM   33789 C  CG  . LYS   S  5  218 ? 85.173  -190.038 45.078  1.00 128.91 ? 217 LYS   S CG  1 
ATOM   33790 C  CD  . LYS   S  5  218 ? 86.408  -190.034 45.940  1.00 128.80 ? 217 LYS   S CD  1 
ATOM   33791 C  CE  . LYS   S  5  218 ? 86.281  -189.075 47.101  1.00 129.01 ? 217 LYS   S CE  1 
ATOM   33792 N  NZ  . LYS   S  5  218 ? 87.586  -188.840 47.759  1.00 131.73 ? 217 LYS   S NZ  1 
ATOM   33793 N  N   . ASP   S  5  219 ? 85.391  -189.822 41.150  1.00 137.54 ? 218 ASP   S N   1 
ATOM   33794 C  CA  . ASP   S  5  219 ? 85.795  -188.756 40.193  1.00 137.76 ? 218 ASP   S CA  1 
ATOM   33795 C  C   . ASP   S  5  219 ? 85.760  -189.328 38.773  1.00 136.72 ? 218 ASP   S C   1 
ATOM   33796 O  O   . ASP   S  5  219 ? 86.759  -189.169 38.041  1.00 134.68 ? 218 ASP   S O   1 
ATOM   33797 C  CB  . ASP   S  5  219 ? 87.167  -188.179 40.557  1.00 143.14 ? 218 ASP   S CB  1 
ATOM   33798 C  CG  . ASP   S  5  219 ? 87.157  -187.304 41.799  1.00 146.66 ? 218 ASP   S CG  1 
ATOM   33799 O  OD1 . ASP   S  5  219 ? 86.129  -186.637 42.044  1.00 145.54 ? 218 ASP   S OD1 1 
ATOM   33800 O  OD2 . ASP   S  5  219 ? 88.179  -187.295 42.511  1.00 150.81 ? 218 ASP   S OD2 1 
ATOM   33801 N  N   . THR   S  5  220 ? 84.647  -189.970 38.407  1.00 134.29 ? 219 THR   S N   1 
ATOM   33802 C  CA  . THR   S  5  220 ? 84.421  -190.577 37.069  1.00 133.97 ? 219 THR   S CA  1 
ATOM   33803 C  C   . THR   S  5  220 ? 82.925  -190.612 36.770  1.00 129.23 ? 219 THR   S C   1 
ATOM   33804 O  O   . THR   S  5  220 ? 82.180  -191.337 37.427  1.00 129.30 ? 219 THR   S O   1 
ATOM   33805 C  CB  . THR   S  5  220 ? 85.029  -191.983 36.977  1.00 139.94 ? 219 THR   S CB  1 
ATOM   33806 O  OG1 . THR   S  5  220 ? 86.239  -192.022 37.736  1.00 142.98 ? 219 THR   S OG1 1 
ATOM   33807 C  CG2 . THR   S  5  220 ? 85.312  -192.394 35.549  1.00 142.05 ? 219 THR   S CG2 1 
ATOM   33808 N  N   . PRO   S  5  221 ? 82.434  -189.824 35.786  1.00 128.21 ? 220 PRO   S N   1 
ATOM   33809 C  CA  . PRO   S  5  221 ? 81.061  -189.968 35.300  1.00 126.32 ? 220 PRO   S CA  1 
ATOM   33810 C  C   . PRO   S  5  221 ? 80.850  -191.332 34.623  1.00 124.16 ? 220 PRO   S C   1 
ATOM   33811 O  O   . PRO   S  5  221 ? 81.808  -191.860 34.079  1.00 121.40 ? 220 PRO   S O   1 
ATOM   33812 C  CB  . PRO   S  5  221 ? 80.899  -188.832 34.276  1.00 126.00 ? 220 PRO   S CB  1 
ATOM   33813 C  CG  . PRO   S  5  221 ? 82.035  -187.872 34.577  1.00 124.69 ? 220 PRO   S CG  1 
ATOM   33814 C  CD  . PRO   S  5  221 ? 83.157  -188.738 35.107  1.00 125.43 ? 220 PRO   S CD  1 
ATOM   33815 N  N   . PHE   S  5  222 ? 79.623  -191.867 34.668  1.00 122.92 ? 221 PHE   S N   1 
ATOM   33816 C  CA  . PHE   S  5  222 ? 79.247  -193.135 33.988  1.00 122.98 ? 221 PHE   S CA  1 
ATOM   33817 C  C   . PHE   S  5  222 ? 79.639  -193.017 32.513  1.00 122.17 ? 221 PHE   S C   1 
ATOM   33818 O  O   . PHE   S  5  222 ? 79.027  -192.206 31.792  1.00 120.82 ? 221 PHE   S O   1 
ATOM   33819 C  CB  . PHE   S  5  222 ? 77.756  -193.458 34.125  1.00 122.45 ? 221 PHE   S CB  1 
ATOM   33820 C  CG  . PHE   S  5  222 ? 77.364  -194.794 33.540  1.00 123.12 ? 221 PHE   S CG  1 
ATOM   33821 C  CD1 . PHE   S  5  222 ? 77.095  -194.930 32.185  1.00 124.71 ? 221 PHE   S CD1 1 
ATOM   33822 C  CD2 . PHE   S  5  222 ? 77.285  -195.926 34.339  1.00 121.83 ? 221 PHE   S CD2 1 
ATOM   33823 C  CE1 . PHE   S  5  222 ? 76.749  -196.161 31.646  1.00 123.36 ? 221 PHE   S CE1 1 
ATOM   33824 C  CE2 . PHE   S  5  222 ? 76.938  -197.156 33.798  1.00 121.70 ? 221 PHE   S CE2 1 
ATOM   33825 C  CZ  . PHE   S  5  222 ? 76.671  -197.272 32.453  1.00 121.43 ? 221 PHE   S CZ  1 
ATOM   33826 N  N   . THR   S  5  223 ? 80.644  -193.788 32.093  1.00 125.65 ? 222 THR   S N   1 
ATOM   33827 C  CA  . THR   S  5  223 ? 81.177  -193.798 30.706  1.00 131.23 ? 222 THR   S CA  1 
ATOM   33828 C  C   . THR   S  5  223 ? 81.327  -195.244 30.222  1.00 133.28 ? 222 THR   S C   1 
ATOM   33829 O  O   . THR   S  5  223 ? 81.677  -196.116 31.044  1.00 136.74 ? 222 THR   S O   1 
ATOM   33830 C  CB  . THR   S  5  223 ? 82.495  -193.018 30.622  1.00 137.45 ? 222 THR   S CB  1 
ATOM   33831 O  OG1 . THR   S  5  223 ? 83.309  -193.396 31.734  1.00 144.36 ? 222 THR   S OG1 1 
ATOM   33832 C  CG2 . THR   S  5  223 ? 82.282  -191.520 30.623  1.00 135.88 ? 222 THR   S CG2 1 
ATOM   33833 N  N   . ILE   S  5  224 ? 81.068  -195.470 28.931  1.00 131.77 ? 223 ILE   S N   1 
ATOM   33834 C  CA  . ILE   S  5  224 ? 81.091  -196.809 28.275  1.00 132.51 ? 223 ILE   S CA  1 
ATOM   33835 C  C   . ILE   S  5  224 ? 82.305  -196.871 27.343  1.00 134.89 ? 223 ILE   S C   1 
ATOM   33836 O  O   . ILE   S  5  224 ? 82.580  -195.864 26.661  1.00 129.97 ? 223 ILE   S O   1 
ATOM   33837 C  CB  . ILE   S  5  224 ? 79.776  -197.071 27.516  1.00 130.34 ? 223 ILE   S CB  1 
ATOM   33838 C  CG1 . ILE   S  5  224 ? 78.550  -196.806 28.396  1.00 126.29 ? 223 ILE   S CG1 1 
ATOM   33839 C  CG2 . ILE   S  5  224 ? 79.765  -198.481 26.939  1.00 132.48 ? 223 ILE   S CG2 1 
ATOM   33840 C  CD1 . ILE   S  5  224 ? 77.248  -196.726 27.634  1.00 126.46 ? 223 ILE   S CD1 1 
ATOM   33841 N  N   . TYR   S  5  225 ? 82.987  -198.019 27.318  1.00 140.21 ? 224 TYR   S N   1 
ATOM   33842 C  CA  . TYR   S  5  225 ? 84.157  -198.302 26.447  1.00 149.09 ? 224 TYR   S CA  1 
ATOM   33843 C  C   . TYR   S  5  225 ? 83.819  -199.453 25.496  1.00 151.01 ? 224 TYR   S C   1 
ATOM   33844 O  O   . TYR   S  5  225 ? 83.472  -200.552 25.975  1.00 152.09 ? 224 TYR   S O   1 
ATOM   33845 C  CB  . TYR   S  5  225 ? 85.390  -198.628 27.291  1.00 152.79 ? 224 TYR   S CB  1 
ATOM   33846 C  CG  . TYR   S  5  225 ? 85.819  -197.514 28.211  1.00 155.74 ? 224 TYR   S CG  1 
ATOM   33847 C  CD1 . TYR   S  5  225 ? 86.177  -196.274 27.707  1.00 154.05 ? 224 TYR   S CD1 1 
ATOM   33848 C  CD2 . TYR   S  5  225 ? 85.866  -197.695 29.584  1.00 156.54 ? 224 TYR   S CD2 1 
ATOM   33849 C  CE1 . TYR   S  5  225 ? 86.571  -195.242 28.543  1.00 155.88 ? 224 TYR   S CE1 1 
ATOM   33850 C  CE2 . TYR   S  5  225 ? 86.259  -196.674 30.434  1.00 158.65 ? 224 TYR   S CE2 1 
ATOM   33851 C  CZ  . TYR   S  5  225 ? 86.612  -195.442 29.912  1.00 160.31 ? 224 TYR   S CZ  1 
ATOM   33852 O  OH  . TYR   S  5  225 ? 87.000  -194.428 30.740  1.00 162.56 ? 224 TYR   S OH  1 
ATOM   33853 N  N   . ASP   S  5  226 ? 83.914  -199.186 24.190  1.00 152.05 ? 225 ASP   S N   1 
ATOM   33854 C  CA  . ASP   S  5  226 ? 83.749  -200.176 23.094  1.00 152.68 ? 225 ASP   S CA  1 
ATOM   33855 C  C   . ASP   S  5  226 ? 84.960  -200.076 22.163  1.00 149.83 ? 225 ASP   S C   1 
ATOM   33856 O  O   . ASP   S  5  226 ? 85.798  -199.178 22.376  1.00 153.04 ? 225 ASP   S O   1 
ATOM   33857 C  CB  . ASP   S  5  226 ? 82.448  -199.935 22.325  1.00 156.27 ? 225 ASP   S CB  1 
ATOM   33858 C  CG  . ASP   S  5  226 ? 81.196  -200.177 23.151  1.00 157.93 ? 225 ASP   S CG  1 
ATOM   33859 O  OD1 . ASP   S  5  226 ? 81.092  -201.266 23.752  1.00 158.75 ? 225 ASP   S OD1 1 
ATOM   33860 O  OD2 . ASP   S  5  226 ? 80.338  -199.272 23.191  1.00 155.10 ? 225 ASP   S OD2 1 
ATOM   33861 N  N   . GLY   S  5  227 ? 85.041  -200.971 21.175  1.00 149.31 ? 226 GLY   S N   1 
ATOM   33862 C  CA  . GLY   S  5  227 ? 86.069  -200.957 20.117  1.00 148.78 ? 226 GLY   S CA  1 
ATOM   33863 C  C   . GLY   S  5  227 ? 87.474  -200.874 20.688  1.00 148.14 ? 226 GLY   S C   1 
ATOM   33864 O  O   . GLY   S  5  227 ? 87.759  -201.589 21.663  1.00 150.48 ? 226 GLY   S O   1 
ATOM   33865 N  N   . GLU   S  5  228 ? 88.314  -200.002 20.125  1.00 143.29 ? 227 GLU   S N   1 
ATOM   33866 C  CA  . GLU   S  5  228 ? 89.782  -199.978 20.373  1.00 146.87 ? 227 GLU   S CA  1 
ATOM   33867 C  C   . GLU   S  5  228 ? 90.085  -199.553 21.817  1.00 142.77 ? 227 GLU   S C   1 
ATOM   33868 O  O   . GLU   S  5  228 ? 91.232  -199.762 22.252  1.00 147.86 ? 227 GLU   S O   1 
ATOM   33869 C  CB  . GLU   S  5  228 ? 90.481  -199.049 19.377  1.00 148.08 ? 227 GLU   S CB  1 
ATOM   33870 C  CG  . GLU   S  5  228 ? 91.882  -199.508 19.008  1.00 152.90 ? 227 GLU   S CG  1 
ATOM   33871 C  CD  . GLU   S  5  228 ? 91.948  -200.877 18.349  1.00 155.29 ? 227 GLU   S CD  1 
ATOM   33872 O  OE1 . GLU   S  5  228 ? 91.086  -201.164 17.493  1.00 151.50 ? 227 GLU   S OE1 1 
ATOM   33873 O  OE2 . GLU   S  5  228 ? 92.852  -201.660 18.704  1.00 158.15 ? 227 GLU   S OE2 1 
ATOM   33874 N  N   . ALA   S  5  229 ? 89.107  -198.990 22.533  1.00 138.31 ? 228 ALA   S N   1 
ATOM   33875 C  CA  . ALA   S  5  229 ? 89.262  -198.506 23.925  1.00 139.59 ? 228 ALA   S CA  1 
ATOM   33876 C  C   . ALA   S  5  229 ? 89.272  -199.673 24.924  1.00 142.70 ? 228 ALA   S C   1 
ATOM   33877 O  O   . ALA   S  5  229 ? 89.667  -199.425 26.081  1.00 143.64 ? 228 ALA   S O   1 
ATOM   33878 C  CB  . ALA   S  5  229 ? 88.174  -197.514 24.254  1.00 136.74 ? 228 ALA   S CB  1 
ATOM   33879 N  N   . VAL   S  5  230 ? 88.858  -200.883 24.518  1.00 146.52 ? 229 VAL   S N   1 
ATOM   33880 C  CA  . VAL   S  5  230 ? 88.860  -202.095 25.397  1.00 149.60 ? 229 VAL   S CA  1 
ATOM   33881 C  C   . VAL   S  5  230 ? 90.019  -203.030 25.022  1.00 152.90 ? 229 VAL   S C   1 
ATOM   33882 O  O   . VAL   S  5  230 ? 90.219  -204.014 25.761  1.00 153.04 ? 229 VAL   S O   1 
ATOM   33883 C  CB  . VAL   S  5  230 ? 87.511  -202.845 25.378  1.00 150.87 ? 229 VAL   S CB  1 
ATOM   33884 C  CG1 . VAL   S  5  230 ? 86.358  -201.941 25.784  1.00 149.44 ? 229 VAL   S CG1 1 
ATOM   33885 C  CG2 . VAL   S  5  230 ? 87.221  -203.518 24.044  1.00 154.17 ? 229 VAL   S CG2 1 
ATOM   33886 N  N   . ALA   S  5  231 ? 90.755  -202.742 23.939  1.00 156.87 ? 230 ALA   S N   1 
ATOM   33887 C  CA  . ALA   S  5  231 ? 91.924  -203.531 23.473  1.00 158.63 ? 230 ALA   S CA  1 
ATOM   33888 C  C   . ALA   S  5  231 ? 92.942  -203.672 24.612  1.00 160.55 ? 230 ALA   S C   1 
ATOM   33889 O  O   . ALA   S  5  231 ? 93.594  -204.732 24.697  1.00 163.28 ? 230 ALA   S O   1 
ATOM   33890 C  CB  . ALA   S  5  231 ? 92.548  -202.885 22.260  1.00 158.90 ? 230 ALA   S CB  1 
ATOM   33891 N  N   . LYS   S  5  232 ? 93.052  -202.634 25.449  1.00 157.92 ? 231 LYS   S N   1 
ATOM   33892 C  CA  . LYS   S  5  232 ? 93.914  -202.565 26.662  1.00 157.73 ? 231 LYS   S CA  1 
ATOM   33893 C  C   . LYS   S  5  232 ? 93.691  -203.785 27.572  1.00 157.50 ? 231 LYS   S C   1 
ATOM   33894 O  O   . LYS   S  5  232 ? 94.663  -204.184 28.244  1.00 161.01 ? 231 LYS   S O   1 
ATOM   33895 C  CB  . LYS   S  5  232 ? 93.613  -201.264 27.416  1.00 157.40 ? 231 LYS   S CB  1 
ATOM   33896 C  CG  . LYS   S  5  232 ? 94.563  -200.913 28.555  1.00 158.42 ? 231 LYS   S CG  1 
ATOM   33897 C  CD  . LYS   S  5  232 ? 93.945  -200.006 29.607  1.00 155.90 ? 231 LYS   S CD  1 
ATOM   33898 C  CE  . LYS   S  5  232 ? 93.858  -198.549 29.199  1.00 152.78 ? 231 LYS   S CE  1 
ATOM   33899 N  NZ  . LYS   S  5  232 ? 92.664  -198.264 28.368  1.00 149.67 ? 231 LYS   S NZ  1 
ATOM   33900 N  N   . TYR   S  5  233 ? 92.479  -204.357 27.592  1.00 154.55 ? 232 TYR   S N   1 
ATOM   33901 C  CA  . TYR   S  5  233 ? 92.025  -205.354 28.602  1.00 152.41 ? 232 TYR   S CA  1 
ATOM   33902 C  C   . TYR   S  5  233 ? 91.918  -206.778 28.029  1.00 150.48 ? 232 TYR   S C   1 
ATOM   33903 O  O   . TYR   S  5  233 ? 91.335  -207.633 28.726  1.00 142.92 ? 232 TYR   S O   1 
ATOM   33904 C  CB  . TYR   S  5  233 ? 90.676  -204.920 29.181  1.00 153.01 ? 232 TYR   S CB  1 
ATOM   33905 C  CG  . TYR   S  5  233 ? 90.693  -203.572 29.855  1.00 152.90 ? 232 TYR   S CG  1 
ATOM   33906 C  CD1 . TYR   S  5  233 ? 91.214  -203.418 31.130  1.00 154.85 ? 232 TYR   S CD1 1 
ATOM   33907 C  CD2 . TYR   S  5  233 ? 90.189  -202.447 29.221  1.00 151.47 ? 232 TYR   S CD2 1 
ATOM   33908 C  CE1 . TYR   S  5  233 ? 91.232  -202.184 31.759  1.00 151.97 ? 232 TYR   S CE1 1 
ATOM   33909 C  CE2 . TYR   S  5  233 ? 90.200  -201.205 29.836  1.00 148.47 ? 232 TYR   S CE2 1 
ATOM   33910 C  CZ  . TYR   S  5  233 ? 90.722  -201.073 31.111  1.00 147.99 ? 232 TYR   S CZ  1 
ATOM   33911 O  OH  . TYR   S  5  233 ? 90.743  -199.856 31.726  1.00 145.66 ? 232 TYR   S OH  1 
ATOM   33912 N  N   . ILE   S  5  234 ? 92.459  -207.046 26.833  1.00 151.02 ? 233 ILE   S N   1 
ATOM   33913 C  CA  . ILE   S  5  234 ? 92.486  -208.412 26.222  1.00 151.96 ? 233 ILE   S CA  1 
ATOM   33914 C  C   . ILE   S  5  234 ? 93.918  -208.954 26.293  1.00 157.69 ? 233 ILE   S C   1 
ATOM   33915 O  O   . ILE   S  5  234 ? 94.870  -208.289 25.885  1.00 161.57 ? 233 ILE   S O   1 
ATOM   33916 C  CB  . ILE   S  5  234 ? 91.956  -208.406 24.773  1.00 149.70 ? 233 ILE   S CB  1 
ATOM   33917 C  CG1 . ILE   S  5  234 ? 90.578  -207.747 24.665  1.00 145.62 ? 233 ILE   S CG1 1 
ATOM   33918 C  CG2 . ILE   S  5  234 ? 91.944  -209.819 24.202  1.00 151.16 ? 233 ILE   S CG2 1 
ATOM   33919 C  CD1 . ILE   S  5  234 ? 90.233  -207.283 23.271  1.00 143.51 ? 233 ILE   S CD1 1 
ATOM   33920 O  OXT . ILE   S  5  234 ? 94.147  -210.072 26.753  1.00 160.30 ? 233 ILE   S OXT 1 
ATOM   33921 N  N   . THR   T  6  6   ? 35.537  -229.811 36.367  1.00 139.87 ? 2   THR   T N   1 
ATOM   33922 C  CA  . THR   T  6  6   ? 36.281  -228.848 37.242  1.00 138.56 ? 2   THR   T CA  1 
ATOM   33923 C  C   . THR   T  6  6   ? 36.794  -227.676 36.386  1.00 136.86 ? 2   THR   T C   1 
ATOM   33924 O  O   . THR   T  6  6   ? 36.067  -227.277 35.451  1.00 131.97 ? 2   THR   T O   1 
ATOM   33925 C  CB  . THR   T  6  6   ? 37.362  -229.585 38.048  1.00 145.05 ? 2   THR   T CB  1 
ATOM   33926 O  OG1 . THR   T  6  6   ? 38.127  -230.395 37.153  1.00 147.16 ? 2   THR   T OG1 1 
ATOM   33927 C  CG2 . THR   T  6  6   ? 36.783  -230.453 39.143  1.00 144.79 ? 2   THR   T CG2 1 
ATOM   33928 N  N   . GLY   T  6  7   ? 37.982  -227.139 36.693  1.00 131.45 ? 3   GLY   T N   1 
ATOM   33929 C  CA  . GLY   T  6  7   ? 38.516  -225.892 36.109  1.00 127.31 ? 3   GLY   T CA  1 
ATOM   33930 C  C   . GLY   T  6  7   ? 38.207  -224.679 36.976  1.00 120.83 ? 3   GLY   T C   1 
ATOM   33931 O  O   . GLY   T  6  7   ? 38.532  -223.551 36.551  1.00 118.05 ? 3   GLY   T O   1 
ATOM   33932 N  N   . TYR   T  6  8   ? 37.616  -224.901 38.157  1.00 118.50 ? 4   TYR   T N   1 
ATOM   33933 C  CA  . TYR   T  6  8   ? 37.210  -223.857 39.138  1.00 112.43 ? 4   TYR   T CA  1 
ATOM   33934 C  C   . TYR   T  6  8   ? 38.435  -223.119 39.696  1.00 107.64 ? 4   TYR   T C   1 
ATOM   33935 O  O   . TYR   T  6  8   ? 38.254  -222.015 40.246  1.00 106.11 ? 4   TYR   T O   1 
ATOM   33936 C  CB  . TYR   T  6  8   ? 36.427  -224.480 40.296  1.00 116.22 ? 4   TYR   T CB  1 
ATOM   33937 C  CG  . TYR   T  6  8   ? 35.078  -225.042 39.924  1.00 117.75 ? 4   TYR   T CG  1 
ATOM   33938 C  CD1 . TYR   T  6  8   ? 33.980  -224.212 39.768  1.00 117.78 ? 4   TYR   T CD1 1 
ATOM   33939 C  CD2 . TYR   T  6  8   ? 34.890  -226.404 39.742  1.00 120.88 ? 4   TYR   T CD2 1 
ATOM   33940 C  CE1 . TYR   T  6  8   ? 32.734  -224.716 39.433  1.00 113.88 ? 4   TYR   T CE1 1 
ATOM   33941 C  CE2 . TYR   T  6  8   ? 33.649  -226.925 39.408  1.00 118.72 ? 4   TYR   T CE2 1 
ATOM   33942 C  CZ  . TYR   T  6  8   ? 32.566  -226.077 39.253  1.00 115.34 ? 4   TYR   T CZ  1 
ATOM   33943 O  OH  . TYR   T  6  8   ? 31.332  -226.557 38.924  1.00 111.33 ? 4   TYR   T OH  1 
ATOM   33944 N  N   . ASP   T  6  9   ? 39.628  -223.715 39.585  1.00 100.32 ? 5   ASP   T N   1 
ATOM   33945 C  CA  . ASP   T  6  9   ? 40.894  -223.184 40.159  1.00 103.26 ? 5   ASP   T CA  1 
ATOM   33946 C  C   . ASP   T  6  9   ? 41.691  -222.383 39.116  1.00 105.09 ? 5   ASP   T C   1 
ATOM   33947 O  O   . ASP   T  6  9   ? 42.770  -221.876 39.482  1.00 106.65 ? 5   ASP   T O   1 
ATOM   33948 C  CB  . ASP   T  6  9   ? 41.759  -224.316 40.722  1.00 103.33 ? 5   ASP   T CB  1 
ATOM   33949 C  CG  . ASP   T  6  9   ? 42.399  -225.187 39.657  1.00 105.83 ? 5   ASP   T CG  1 
ATOM   33950 O  OD1 . ASP   T  6  9   ? 41.756  -225.406 38.610  1.00 110.91 ? 5   ASP   T OD1 1 
ATOM   33951 O  OD2 . ASP   T  6  9   ? 43.537  -225.632 39.882  1.00 107.45 ? 5   ASP   T OD2 1 
ATOM   33952 N  N   . LEU   T  6  10  ? 41.198  -222.264 37.877  1.00 103.69 ? 6   LEU   T N   1 
ATOM   33953 C  CA  . LEU   T  6  10  ? 41.940  -221.626 36.750  1.00 105.79 ? 6   LEU   T CA  1 
ATOM   33954 C  C   . LEU   T  6  10  ? 41.698  -220.111 36.712  1.00 101.94 ? 6   LEU   T C   1 
ATOM   33955 O  O   . LEU   T  6  10  ? 42.453  -219.419 36.001  1.00 97.16  ? 6   LEU   T O   1 
ATOM   33956 C  CB  . LEU   T  6  10  ? 41.501  -222.261 35.427  1.00 108.11 ? 6   LEU   T CB  1 
ATOM   33957 C  CG  . LEU   T  6  10  ? 41.854  -223.736 35.244  1.00 110.43 ? 6   LEU   T CG  1 
ATOM   33958 C  CD1 . LEU   T  6  10  ? 41.174  -224.294 34.003  1.00 112.32 ? 6   LEU   T CD1 1 
ATOM   33959 C  CD2 . LEU   T  6  10  ? 43.361  -223.938 35.163  1.00 109.18 ? 6   LEU   T CD2 1 
ATOM   33960 N  N   . SER   T  6  11  ? 40.685  -219.617 37.430  1.00 102.71 ? 7   SER   T N   1 
ATOM   33961 C  CA  . SER   T  6  11  ? 40.224  -218.207 37.374  1.00 101.10 ? 7   SER   T CA  1 
ATOM   33962 C  C   . SER   T  6  11  ? 39.984  -217.672 38.791  1.00 103.55 ? 7   SER   T C   1 
ATOM   33963 O  O   . SER   T  6  11  ? 39.314  -218.369 39.587  1.00 106.12 ? 7   SER   T O   1 
ATOM   33964 C  CB  . SER   T  6  11  ? 38.992  -218.096 36.514  1.00 102.14 ? 7   SER   T CB  1 
ATOM   33965 O  OG  . SER   T  6  11  ? 38.559  -216.748 36.410  1.00 103.34 ? 7   SER   T OG  1 
ATOM   33966 N  N   . ASN   T  6  12  ? 40.533  -216.488 39.088  1.00 97.93  ? 8   ASN   T N   1 
ATOM   33967 C  CA  . ASN   T  6  12  ? 40.336  -215.761 40.371  1.00 95.84  ? 8   ASN   T CA  1 
ATOM   33968 C  C   . ASN   T  6  12  ? 38.884  -215.272 40.431  1.00 94.67  ? 8   ASN   T C   1 
ATOM   33969 O  O   . ASN   T  6  12  ? 38.346  -214.917 39.368  1.00 91.10  ? 8   ASN   T O   1 
ATOM   33970 C  CB  . ASN   T  6  12  ? 41.340  -214.613 40.522  1.00 95.32  ? 8   ASN   T CB  1 
ATOM   33971 C  CG  . ASN   T  6  12  ? 41.251  -213.903 41.856  1.00 96.43  ? 8   ASN   T CG  1 
ATOM   33972 O  OD1 . ASN   T  6  12  ? 40.777  -214.468 42.838  1.00 100.86 ? 8   ASN   T OD1 1 
ATOM   33973 N  ND2 . ASN   T  6  12  ? 41.710  -212.664 41.909  1.00 94.49  ? 8   ASN   T ND2 1 
ATOM   33974 N  N   . SER   T  6  13  ? 38.279  -215.298 41.626  1.00 96.93  ? 9   SER   T N   1 
ATOM   33975 C  CA  . SER   T  6  13  ? 36.922  -214.773 41.951  1.00 96.48  ? 9   SER   T CA  1 
ATOM   33976 C  C   . SER   T  6  13  ? 35.830  -215.812 41.645  1.00 95.41  ? 9   SER   T C   1 
ATOM   33977 O  O   . SER   T  6  13  ? 34.645  -215.515 41.915  1.00 92.03  ? 9   SER   T O   1 
ATOM   33978 C  CB  . SER   T  6  13  ? 36.645  -213.467 41.241  1.00 97.63  ? 9   SER   T CB  1 
ATOM   33979 O  OG  . SER   T  6  13  ? 36.176  -213.693 39.921  1.00 101.87 ? 9   SER   T OG  1 
ATOM   33980 N  N   . VAL   T  6  14  ? 36.197  -216.978 41.105  1.00 94.09  ? 10  VAL   T N   1 
ATOM   33981 C  CA  . VAL   T  6  14  ? 35.249  -218.099 40.829  1.00 93.18  ? 10  VAL   T CA  1 
ATOM   33982 C  C   . VAL   T  6  14  ? 35.120  -218.960 42.091  1.00 91.65  ? 10  VAL   T C   1 
ATOM   33983 O  O   . VAL   T  6  14  ? 36.158  -219.469 42.575  1.00 89.59  ? 10  VAL   T O   1 
ATOM   33984 C  CB  . VAL   T  6  14  ? 35.700  -218.947 39.626  1.00 93.45  ? 10  VAL   T CB  1 
ATOM   33985 C  CG1 . VAL   T  6  14  ? 34.854  -220.202 39.480  1.00 96.86  ? 10  VAL   T CG1 1 
ATOM   33986 C  CG2 . VAL   T  6  14  ? 35.688  -218.146 38.336  1.00 92.16  ? 10  VAL   T CG2 1 
ATOM   33987 N  N   . PHE   T  6  15  ? 33.890  -219.127 42.585  1.00 88.68  ? 11  PHE   T N   1 
ATOM   33988 C  CA  . PHE   T  6  15  ? 33.546  -220.054 43.692  1.00 92.33  ? 11  PHE   T CA  1 
ATOM   33989 C  C   . PHE   T  6  15  ? 33.607  -221.495 43.173  1.00 92.27  ? 11  PHE   T C   1 
ATOM   33990 O  O   . PHE   T  6  15  ? 33.013  -221.796 42.119  1.00 93.71  ? 11  PHE   T O   1 
ATOM   33991 C  CB  . PHE   T  6  15  ? 32.157  -219.752 44.262  1.00 91.53  ? 11  PHE   T CB  1 
ATOM   33992 C  CG  . PHE   T  6  15  ? 32.078  -218.514 45.119  1.00 93.79  ? 11  PHE   T CG  1 
ATOM   33993 C  CD1 . PHE   T  6  15  ? 32.719  -218.461 46.348  1.00 94.45  ? 11  PHE   T CD1 1 
ATOM   33994 C  CD2 . PHE   T  6  15  ? 31.358  -217.404 44.702  1.00 93.81  ? 11  PHE   T CD2 1 
ATOM   33995 C  CE1 . PHE   T  6  15  ? 32.647  -217.322 47.136  1.00 93.24  ? 11  PHE   T CE1 1 
ATOM   33996 C  CE2 . PHE   T  6  15  ? 31.287  -216.266 45.492  1.00 92.51  ? 11  PHE   T CE2 1 
ATOM   33997 C  CZ  . PHE   T  6  15  ? 31.929  -216.229 46.708  1.00 91.49  ? 11  PHE   T CZ  1 
ATOM   33998 N  N   . SER   T  6  16  ? 34.312  -222.365 43.896  1.00 94.95  ? 12  SER   T N   1 
ATOM   33999 C  CA  . SER   T  6  16  ? 34.219  -223.839 43.743  1.00 96.26  ? 12  SER   T CA  1 
ATOM   34000 C  C   . SER   T  6  16  ? 32.873  -224.291 44.303  1.00 94.38  ? 12  SER   T C   1 
ATOM   34001 O  O   . SER   T  6  16  ? 32.197  -223.518 44.977  1.00 92.59  ? 12  SER   T O   1 
ATOM   34002 C  CB  . SER   T  6  16  ? 35.365  -224.528 44.435  1.00 100.59 ? 12  SER   T CB  1 
ATOM   34003 O  OG  . SER   T  6  16  ? 35.241  -224.428 45.848  1.00 101.31 ? 12  SER   T OG  1 
ATOM   34004 N  N   . PRO   T  6  17  ? 32.421  -225.536 44.035  1.00 93.42  ? 13  PRO   T N   1 
ATOM   34005 C  CA  . PRO   T  6  17  ? 31.222  -226.065 44.687  1.00 94.27  ? 13  PRO   T CA  1 
ATOM   34006 C  C   . PRO   T  6  17  ? 31.291  -226.098 46.223  1.00 96.14  ? 13  PRO   T C   1 
ATOM   34007 O  O   . PRO   T  6  17  ? 30.244  -226.114 46.831  1.00 98.11  ? 13  PRO   T O   1 
ATOM   34008 C  CB  . PRO   T  6  17  ? 31.111  -227.484 44.118  1.00 95.05  ? 13  PRO   T CB  1 
ATOM   34009 C  CG  . PRO   T  6  17  ? 31.804  -227.390 42.779  1.00 93.99  ? 13  PRO   T CG  1 
ATOM   34010 C  CD  . PRO   T  6  17  ? 32.967  -226.454 43.026  1.00 92.62  ? 13  PRO   T CD  1 
ATOM   34011 N  N   . ASP   T  6  18  ? 32.497  -226.102 46.803  1.00 99.95  ? 14  ASP   T N   1 
ATOM   34012 C  CA  . ASP   T  6  18  ? 32.724  -226.012 48.273  1.00 106.36 ? 14  ASP   T CA  1 
ATOM   34013 C  C   . ASP   T  6  18  ? 32.267  -224.642 48.786  1.00 106.28 ? 14  ASP   T C   1 
ATOM   34014 O  O   . ASP   T  6  18  ? 31.736  -224.585 49.910  1.00 111.83 ? 14  ASP   T O   1 
ATOM   34015 C  CB  . ASP   T  6  18  ? 34.199  -226.166 48.651  1.00 110.75 ? 14  ASP   T CB  1 
ATOM   34016 C  CG  . ASP   T  6  18  ? 34.943  -227.248 47.890  1.00 115.92 ? 14  ASP   T CG  1 
ATOM   34017 O  OD1 . ASP   T  6  18  ? 35.112  -228.342 48.455  1.00 121.17 ? 14  ASP   T OD1 1 
ATOM   34018 O  OD2 . ASP   T  6  18  ? 35.365  -226.979 46.748  1.00 121.40 ? 14  ASP   T OD2 1 
ATOM   34019 N  N   . GLY   T  6  19  ? 32.488  -223.593 47.987  1.00 105.81 ? 15  GLY   T N   1 
ATOM   34020 C  CA  . GLY   T  6  19  ? 32.352  -222.176 48.379  1.00 103.93 ? 15  GLY   T CA  1 
ATOM   34021 C  C   . GLY   T  6  19  ? 33.710  -221.532 48.607  1.00 107.32 ? 15  GLY   T C   1 
ATOM   34022 O  O   . GLY   T  6  19  ? 33.773  -220.557 49.381  1.00 108.64 ? 15  GLY   T O   1 
ATOM   34023 N  N   . ARG   T  6  20  ? 34.754  -222.049 47.946  1.00 106.25 ? 16  ARG   T N   1 
ATOM   34024 C  CA  . ARG   T  6  20  ? 36.169  -221.620 48.114  1.00 104.93 ? 16  ARG   T CA  1 
ATOM   34025 C  C   . ARG   T  6  20  ? 36.678  -220.938 46.841  1.00 103.08 ? 16  ARG   T C   1 
ATOM   34026 O  O   . ARG   T  6  20  ? 36.168  -221.249 45.747  1.00 101.77 ? 16  ARG   T O   1 
ATOM   34027 C  CB  . ARG   T  6  20  ? 37.058  -222.824 48.433  1.00 107.35 ? 16  ARG   T CB  1 
ATOM   34028 C  CG  . ARG   T  6  20  ? 36.880  -223.369 49.842  1.00 111.05 ? 16  ARG   T CG  1 
ATOM   34029 C  CD  . ARG   T  6  20  ? 37.194  -224.851 49.917  1.00 116.34 ? 16  ARG   T CD  1 
ATOM   34030 N  NE  . ARG   T  6  20  ? 38.579  -225.157 49.589  1.00 118.98 ? 16  ARG   T NE  1 
ATOM   34031 C  CZ  . ARG   T  6  20  ? 39.041  -226.368 49.286  1.00 123.73 ? 16  ARG   T CZ  1 
ATOM   34032 N  NH1 . ARG   T  6  20  ? 38.228  -227.412 49.259  1.00 128.84 ? 16  ARG   T NH1 1 
ATOM   34033 N  NH2 . ARG   T  6  20  ? 40.323  -226.531 49.005  1.00 126.65 ? 16  ARG   T NH2 1 
ATOM   34034 N  N   . ASN   T  6  21  ? 37.669  -220.058 46.999  1.00 99.41  ? 17  ASN   T N   1 
ATOM   34035 C  CA  . ASN   T  6  21  ? 38.376  -219.355 45.898  1.00 101.72 ? 17  ASN   T CA  1 
ATOM   34036 C  C   . ASN   T  6  21  ? 39.786  -219.945 45.803  1.00 99.61  ? 17  ASN   T C   1 
ATOM   34037 O  O   . ASN   T  6  21  ? 40.692  -219.420 46.471  1.00 97.83  ? 17  ASN   T O   1 
ATOM   34038 C  CB  . ASN   T  6  21  ? 38.381  -217.840 46.127  1.00 101.85 ? 17  ASN   T CB  1 
ATOM   34039 C  CG  . ASN   T  6  21  ? 38.962  -217.052 44.972  1.00 104.67 ? 17  ASN   T CG  1 
ATOM   34040 O  OD1 . ASN   T  6  21  ? 39.324  -217.615 43.940  1.00 107.68 ? 17  ASN   T OD1 1 
ATOM   34041 N  ND2 . ASN   T  6  21  ? 39.050  -215.743 45.138  1.00 102.21 ? 17  ASN   T ND2 1 
ATOM   34042 N  N   . PHE   T  6  22  ? 39.950  -221.006 45.011  1.00 102.61 ? 18  PHE   T N   1 
ATOM   34043 C  CA  . PHE   T  6  22  ? 41.186  -221.834 44.957  1.00 107.47 ? 18  PHE   T CA  1 
ATOM   34044 C  C   . PHE   T  6  22  ? 42.406  -220.951 44.662  1.00 104.14 ? 18  PHE   T C   1 
ATOM   34045 O  O   . PHE   T  6  22  ? 43.486  -221.218 45.223  1.00 104.09 ? 18  PHE   T O   1 
ATOM   34046 C  CB  . PHE   T  6  22  ? 41.037  -222.976 43.946  1.00 111.26 ? 18  PHE   T CB  1 
ATOM   34047 C  CG  . PHE   T  6  22  ? 40.488  -224.251 44.537  1.00 113.08 ? 18  PHE   T CG  1 
ATOM   34048 C  CD1 . PHE   T  6  22  ? 41.324  -225.319 44.823  1.00 116.63 ? 18  PHE   T CD1 1 
ATOM   34049 C  CD2 . PHE   T  6  22  ? 39.138  -224.374 44.832  1.00 116.73 ? 18  PHE   T CD2 1 
ATOM   34050 C  CE1 . PHE   T  6  22  ? 40.818  -226.487 45.375  1.00 120.23 ? 18  PHE   T CE1 1 
ATOM   34051 C  CE2 . PHE   T  6  22  ? 38.635  -225.541 45.387  1.00 117.77 ? 18  PHE   T CE2 1 
ATOM   34052 C  CZ  . PHE   T  6  22  ? 39.476  -226.596 45.657  1.00 119.36 ? 18  PHE   T CZ  1 
ATOM   34053 N  N   . GLN   T  6  23  ? 42.235  -219.920 43.832  1.00 102.55 ? 19  GLN   T N   1 
ATOM   34054 C  CA  . GLN   T  6  23  ? 43.332  -219.009 43.410  1.00 103.17 ? 19  GLN   T CA  1 
ATOM   34055 C  C   . GLN   T  6  23  ? 43.956  -218.313 44.629  1.00 102.97 ? 19  GLN   T C   1 
ATOM   34056 O  O   . GLN   T  6  23  ? 45.188  -218.118 44.616  1.00 104.71 ? 19  GLN   T O   1 
ATOM   34057 C  CB  . GLN   T  6  23  ? 42.812  -218.003 42.383  1.00 103.70 ? 19  GLN   T CB  1 
ATOM   34058 C  CG  . GLN   T  6  23  ? 42.970  -218.484 40.949  1.00 105.42 ? 19  GLN   T CG  1 
ATOM   34059 C  CD  . GLN   T  6  23  ? 44.414  -218.468 40.513  1.00 106.01 ? 19  GLN   T CD  1 
ATOM   34060 O  OE1 . GLN   T  6  23  ? 44.946  -219.458 40.018  1.00 109.27 ? 19  GLN   T OE1 1 
ATOM   34061 N  NE2 . GLN   T  6  23  ? 45.064  -217.333 40.710  1.00 107.14 ? 19  GLN   T NE2 1 
ATOM   34062 N  N   . VAL   T  6  24  ? 43.147  -217.948 45.632  1.00 100.67 ? 20  VAL   T N   1 
ATOM   34063 C  CA  . VAL   T  6  24  ? 43.617  -217.344 46.918  1.00 100.63 ? 20  VAL   T CA  1 
ATOM   34064 C  C   . VAL   T  6  24  ? 44.404  -218.405 47.694  1.00 101.94 ? 20  VAL   T C   1 
ATOM   34065 O  O   . VAL   T  6  24  ? 45.523  -218.097 48.157  1.00 96.22  ? 20  VAL   T O   1 
ATOM   34066 C  CB  . VAL   T  6  24  ? 42.448  -216.800 47.762  1.00 98.60  ? 20  VAL   T CB  1 
ATOM   34067 C  CG1 . VAL   T  6  24  ? 42.893  -216.400 49.159  1.00 100.43 ? 20  VAL   T CG1 1 
ATOM   34068 C  CG2 . VAL   T  6  24  ? 41.753  -215.637 47.075  1.00 97.75  ? 20  VAL   T CG2 1 
ATOM   34069 N  N   . GLU   T  6  25  ? 43.822  -219.600 47.836  1.00 103.91 ? 21  GLU   T N   1 
ATOM   34070 C  CA  . GLU   T  6  25  ? 44.450  -220.769 48.507  1.00 104.52 ? 21  GLU   T CA  1 
ATOM   34071 C  C   . GLU   T  6  25  ? 45.800  -221.063 47.844  1.00 100.06 ? 21  GLU   T C   1 
ATOM   34072 O  O   . GLU   T  6  25  ? 46.729  -221.469 48.567  1.00 102.68 ? 21  GLU   T O   1 
ATOM   34073 C  CB  . GLU   T  6  25  ? 43.516  -221.979 48.461  1.00 107.87 ? 21  GLU   T CB  1 
ATOM   34074 C  CG  . GLU   T  6  25  ? 42.318  -221.847 49.384  1.00 113.94 ? 21  GLU   T CG  1 
ATOM   34075 C  CD  . GLU   T  6  25  ? 41.395  -223.053 49.421  1.00 118.60 ? 21  GLU   T CD  1 
ATOM   34076 O  OE1 . GLU   T  6  25  ? 41.864  -224.177 49.133  1.00 124.80 ? 21  GLU   T OE1 1 
ATOM   34077 O  OE2 . GLU   T  6  25  ? 40.205  -222.868 49.741  1.00 129.33 ? 21  GLU   T OE2 1 
ATOM   34078 N  N   . TYR   T  6  26  ? 45.903  -220.853 46.527  1.00 96.91  ? 22  TYR   T N   1 
ATOM   34079 C  CA  . TYR   T  6  26  ? 47.142  -221.067 45.732  1.00 99.46  ? 22  TYR   T CA  1 
ATOM   34080 C  C   . TYR   T  6  26  ? 48.160  -219.968 46.056  1.00 99.46  ? 22  TYR   T C   1 
ATOM   34081 O  O   . TYR   T  6  26  ? 49.362  -220.277 46.136  1.00 101.10 ? 22  TYR   T O   1 
ATOM   34082 C  CB  . TYR   T  6  26  ? 46.821  -221.130 44.236  1.00 100.87 ? 22  TYR   T CB  1 
ATOM   34083 C  CG  . TYR   T  6  26  ? 46.156  -222.400 43.761  1.00 101.67 ? 22  TYR   T CG  1 
ATOM   34084 C  CD1 . TYR   T  6  26  ? 45.743  -223.392 44.642  1.00 101.42 ? 22  TYR   T CD1 1 
ATOM   34085 C  CD2 . TYR   T  6  26  ? 45.916  -222.601 42.411  1.00 103.05 ? 22  TYR   T CD2 1 
ATOM   34086 C  CE1 . TYR   T  6  26  ? 45.128  -224.550 44.194  1.00 100.83 ? 22  TYR   T CE1 1 
ATOM   34087 C  CE2 . TYR   T  6  26  ? 45.303  -223.754 41.947  1.00 102.51 ? 22  TYR   T CE2 1 
ATOM   34088 C  CZ  . TYR   T  6  26  ? 44.907  -224.731 42.841  1.00 101.89 ? 22  TYR   T CZ  1 
ATOM   34089 O  OH  . TYR   T  6  26  ? 44.303  -225.867 42.391  1.00 102.31 ? 22  TYR   T OH  1 
ATOM   34090 N  N   . ALA   T  6  27  ? 47.700  -218.728 46.241  1.00 98.65  ? 23  ALA   T N   1 
ATOM   34091 C  CA  . ALA   T  6  27  ? 48.540  -217.590 46.680  1.00 99.86  ? 23  ALA   T CA  1 
ATOM   34092 C  C   . ALA   T  6  27  ? 49.121  -217.889 48.067  1.00 100.14 ? 23  ALA   T C   1 
ATOM   34093 O  O   . ALA   T  6  27  ? 50.293  -217.545 48.296  1.00 102.76 ? 23  ALA   T O   1 
ATOM   34094 C  CB  . ALA   T  6  27  ? 47.744  -216.309 46.683  1.00 99.99  ? 23  ALA   T CB  1 
ATOM   34095 N  N   . VAL   T  6  28  ? 48.332  -218.518 48.945  1.00 100.50 ? 24  VAL   T N   1 
ATOM   34096 C  CA  . VAL   T  6  28  ? 48.753  -218.912 50.324  1.00 100.57 ? 24  VAL   T CA  1 
ATOM   34097 C  C   . VAL   T  6  28  ? 49.965  -219.849 50.226  1.00 100.58 ? 24  VAL   T C   1 
ATOM   34098 O  O   . VAL   T  6  28  ? 50.851  -219.745 51.094  1.00 97.48  ? 24  VAL   T O   1 
ATOM   34099 C  CB  . VAL   T  6  28  ? 47.591  -219.546 51.117  1.00 101.84 ? 24  VAL   T CB  1 
ATOM   34100 C  CG1 . VAL   T  6  28  ? 48.060  -220.195 52.411  1.00 103.15 ? 24  VAL   T CG1 1 
ATOM   34101 C  CG2 . VAL   T  6  28  ? 46.496  -218.531 51.405  1.00 101.59 ? 24  VAL   T CG2 1 
ATOM   34102 N  N   . LYS   T  6  29  ? 50.009  -220.721 49.211  1.00 102.64 ? 25  LYS   T N   1 
ATOM   34103 C  CA  . LYS   T  6  29  ? 51.135  -221.670 48.980  1.00 106.87 ? 25  LYS   T CA  1 
ATOM   34104 C  C   . LYS   T  6  29  ? 52.424  -220.875 48.724  1.00 104.67 ? 25  LYS   T C   1 
ATOM   34105 O  O   . LYS   T  6  29  ? 53.484  -221.292 49.227  1.00 105.67 ? 25  LYS   T O   1 
ATOM   34106 C  CB  . LYS   T  6  29  ? 50.830  -222.632 47.825  1.00 108.80 ? 25  LYS   T CB  1 
ATOM   34107 C  CG  . LYS   T  6  29  ? 49.715  -223.639 48.084  1.00 109.44 ? 25  LYS   T CG  1 
ATOM   34108 C  CD  . LYS   T  6  29  ? 50.081  -224.714 49.086  1.00 112.81 ? 25  LYS   T CD  1 
ATOM   34109 C  CE  . LYS   T  6  29  ? 49.085  -225.855 49.108  1.00 116.08 ? 25  LYS   T CE  1 
ATOM   34110 N  NZ  . LYS   T  6  29  ? 49.402  -226.844 50.166  1.00 119.58 ? 25  LYS   T NZ  1 
ATOM   34111 N  N   . ALA   T  6  30  ? 52.336  -219.768 47.981  1.00 103.59 ? 26  ALA   T N   1 
ATOM   34112 C  CA  . ALA   T  6  30  ? 53.474  -218.864 47.686  1.00 104.65 ? 26  ALA   T CA  1 
ATOM   34113 C  C   . ALA   T  6  30  ? 53.994  -218.243 48.988  1.00 105.04 ? 26  ALA   T C   1 
ATOM   34114 O  O   . ALA   T  6  30  ? 55.219  -218.031 49.090  1.00 104.99 ? 26  ALA   T O   1 
ATOM   34115 C  CB  . ALA   T  6  30  ? 53.063  -217.800 46.699  1.00 102.94 ? 26  ALA   T CB  1 
ATOM   34116 N  N   . VAL   T  6  31  ? 53.096  -217.964 49.940  1.00 105.66 ? 27  VAL   T N   1 
ATOM   34117 C  CA  . VAL   T  6  31  ? 53.429  -217.359 51.266  1.00 107.63 ? 27  VAL   T CA  1 
ATOM   34118 C  C   . VAL   T  6  31  ? 54.181  -218.403 52.097  1.00 111.13 ? 27  VAL   T C   1 
ATOM   34119 O  O   . VAL   T  6  31  ? 55.265  -218.075 52.620  1.00 118.09 ? 27  VAL   T O   1 
ATOM   34120 C  CB  . VAL   T  6  31  ? 52.177  -216.861 52.015  1.00 105.02 ? 27  VAL   T CB  1 
ATOM   34121 C  CG1 . VAL   T  6  31  ? 52.543  -216.231 53.351  1.00 104.91 ? 27  VAL   T CG1 1 
ATOM   34122 C  CG2 . VAL   T  6  31  ? 51.358  -215.889 51.183  1.00 103.03 ? 27  VAL   T CG2 1 
ATOM   34123 N  N   . GLU   T  6  32  ? 53.620  -219.611 52.206  1.00 113.53 ? 28  GLU   T N   1 
ATOM   34124 C  CA  . GLU   T  6  32  ? 54.209  -220.738 52.975  1.00 114.75 ? 28  GLU   T CA  1 
ATOM   34125 C  C   . GLU   T  6  32  ? 55.651  -220.958 52.494  1.00 112.45 ? 28  GLU   T C   1 
ATOM   34126 O  O   . GLU   T  6  32  ? 56.502  -221.292 53.336  1.00 113.93 ? 28  GLU   T O   1 
ATOM   34127 C  CB  . GLU   T  6  32  ? 53.330  -221.984 52.832  1.00 117.89 ? 28  GLU   T CB  1 
ATOM   34128 C  CG  . GLU   T  6  32  ? 51.990  -221.866 53.547  1.00 121.47 ? 28  GLU   T CG  1 
ATOM   34129 C  CD  . GLU   T  6  32  ? 50.985  -222.975 53.262  1.00 123.42 ? 28  GLU   T CD  1 
ATOM   34130 O  OE1 . GLU   T  6  32  ? 51.326  -223.919 52.516  1.00 125.72 ? 28  GLU   T OE1 1 
ATOM   34131 O  OE2 . GLU   T  6  32  ? 49.856  -222.891 53.789  1.00 127.38 ? 28  GLU   T OE2 1 
ATOM   34132 N  N   . ASN   T  6  33  ? 55.916  -220.735 51.200  1.00 110.61 ? 29  ASN   T N   1 
ATOM   34133 C  CA  . ASN   T  6  33  ? 57.237  -220.956 50.551  1.00 115.24 ? 29  ASN   T CA  1 
ATOM   34134 C  C   . ASN   T  6  33  ? 58.251  -219.904 51.020  1.00 113.21 ? 29  ASN   T C   1 
ATOM   34135 O  O   . ASN   T  6  33  ? 59.453  -220.228 51.058  1.00 115.69 ? 29  ASN   T O   1 
ATOM   34136 C  CB  . ASN   T  6  33  ? 57.122  -220.947 49.024  1.00 117.63 ? 29  ASN   T CB  1 
ATOM   34137 C  CG  . ASN   T  6  33  ? 58.375  -221.442 48.330  1.00 122.52 ? 29  ASN   T CG  1 
ATOM   34138 O  OD1 . ASN   T  6  33  ? 59.055  -220.674 47.651  1.00 122.01 ? 29  ASN   T OD1 1 
ATOM   34139 N  ND2 . ASN   T  6  33  ? 58.692  -222.717 48.504  1.00 125.01 ? 29  ASN   T ND2 1 
ATOM   34140 N  N   . GLY   T  6  34  ? 57.790  -218.697 51.361  1.00 111.07 ? 30  GLY   T N   1 
ATOM   34141 C  CA  . GLY   T  6  34  ? 58.649  -217.551 51.727  1.00 111.31 ? 30  GLY   T CA  1 
ATOM   34142 C  C   . GLY   T  6  34  ? 59.368  -217.753 53.053  1.00 113.40 ? 30  GLY   T C   1 
ATOM   34143 O  O   . GLY   T  6  34  ? 59.066  -218.742 53.752  1.00 113.49 ? 30  GLY   T O   1 
ATOM   34144 N  N   . THR   T  6  35  ? 60.283  -216.836 53.393  1.00 111.65 ? 31  THR   T N   1 
ATOM   34145 C  CA  . THR   T  6  35  ? 61.097  -216.866 54.641  1.00 112.99 ? 31  THR   T CA  1 
ATOM   34146 C  C   . THR   T  6  35  ? 60.202  -216.499 55.828  1.00 111.39 ? 31  THR   T C   1 
ATOM   34147 O  O   . THR   T  6  35  ? 59.105  -215.960 55.593  1.00 108.09 ? 31  THR   T O   1 
ATOM   34148 C  CB  . THR   T  6  35  ? 62.311  -215.926 54.574  1.00 112.42 ? 31  THR   T CB  1 
ATOM   34149 O  OG1 . THR   T  6  35  ? 61.855  -214.574 54.626  1.00 109.62 ? 31  THR   T OG1 1 
ATOM   34150 C  CG2 . THR   T  6  35  ? 63.152  -216.123 53.332  1.00 113.65 ? 31  THR   T CG2 1 
ATOM   34151 N  N   . THR   T  6  36  ? 60.659  -216.773 57.052  1.00 113.80 ? 32  THR   T N   1 
ATOM   34152 C  CA  . THR   T  6  36  ? 59.879  -216.541 58.295  1.00 115.14 ? 32  THR   T CA  1 
ATOM   34153 C  C   . THR   T  6  36  ? 59.930  -215.053 58.660  1.00 114.51 ? 32  THR   T C   1 
ATOM   34154 O  O   . THR   T  6  36  ? 61.024  -214.458 58.598  1.00 114.30 ? 32  THR   T O   1 
ATOM   34155 C  CB  . THR   T  6  36  ? 60.365  -217.415 59.458  1.00 119.42 ? 32  THR   T CB  1 
ATOM   34156 O  OG1 . THR   T  6  36  ? 60.592  -218.744 58.981  1.00 120.54 ? 32  THR   T OG1 1 
ATOM   34157 C  CG2 . THR   T  6  36  ? 59.371  -217.437 60.599  1.00 119.52 ? 32  THR   T CG2 1 
ATOM   34158 N  N   . SER   T  6  37  ? 58.775  -214.487 59.014  1.00 111.33 ? 33  SER   T N   1 
ATOM   34159 C  CA  . SER   T  6  37  ? 58.625  -213.136 59.612  1.00 113.47 ? 33  SER   T CA  1 
ATOM   34160 C  C   . SER   T  6  37  ? 57.652  -213.226 60.790  1.00 112.26 ? 33  SER   T C   1 
ATOM   34161 O  O   . SER   T  6  37  ? 56.716  -214.047 60.718  1.00 111.16 ? 33  SER   T O   1 
ATOM   34162 C  CB  . SER   T  6  37  ? 58.164  -212.132 58.590  1.00 112.43 ? 33  SER   T CB  1 
ATOM   34163 O  OG  . SER   T  6  37  ? 56.921  -212.515 58.023  1.00 114.86 ? 33  SER   T OG  1 
ATOM   34164 N  N   . ILE   T  6  38  ? 57.870  -212.418 61.830  1.00 113.87 ? 34  ILE   T N   1 
ATOM   34165 C  CA  . ILE   T  6  38  ? 57.073  -212.454 63.091  1.00 114.65 ? 34  ILE   T CA  1 
ATOM   34166 C  C   . ILE   T  6  38  ? 56.758  -211.031 63.557  1.00 114.13 ? 34  ILE   T C   1 
ATOM   34167 O  O   . ILE   T  6  38  ? 57.414  -210.077 63.088  1.00 112.45 ? 34  ILE   T O   1 
ATOM   34168 C  CB  . ILE   T  6  38  ? 57.817  -213.232 64.191  1.00 116.41 ? 34  ILE   T CB  1 
ATOM   34169 C  CG1 . ILE   T  6  38  ? 59.215  -212.660 64.438  1.00 119.59 ? 34  ILE   T CG1 1 
ATOM   34170 C  CG2 . ILE   T  6  38  ? 57.860  -214.713 63.860  1.00 118.89 ? 34  ILE   T CG2 1 
ATOM   34171 C  CD1 . ILE   T  6  38  ? 59.817  -213.056 65.765  1.00 122.07 ? 34  ILE   T CD1 1 
ATOM   34172 N  N   . GLY   T  6  39  ? 55.788  -210.929 64.467  1.00 115.58 ? 35  GLY   T N   1 
ATOM   34173 C  CA  . GLY   T  6  39  ? 55.430  -209.701 65.197  1.00 115.14 ? 35  GLY   T CA  1 
ATOM   34174 C  C   . GLY   T  6  39  ? 55.085  -210.024 66.639  1.00 116.08 ? 35  GLY   T C   1 
ATOM   34175 O  O   . GLY   T  6  39  ? 54.233  -210.912 66.850  1.00 117.33 ? 35  GLY   T O   1 
ATOM   34176 N  N   . ILE   T  6  40  ? 55.742  -209.358 67.594  1.00 115.25 ? 36  ILE   T N   1 
ATOM   34177 C  CA  . ILE   T  6  40  ? 55.462  -209.497 69.054  1.00 113.56 ? 36  ILE   T CA  1 
ATOM   34178 C  C   . ILE   T  6  40  ? 54.907  -208.168 69.575  1.00 112.12 ? 36  ILE   T C   1 
ATOM   34179 O  O   . ILE   T  6  40  ? 55.635  -207.155 69.527  1.00 111.71 ? 36  ILE   T O   1 
ATOM   34180 C  CB  . ILE   T  6  40  ? 56.715  -209.933 69.840  1.00 112.94 ? 36  ILE   T CB  1 
ATOM   34181 C  CG1 . ILE   T  6  40  ? 57.412  -211.131 69.190  1.00 113.24 ? 36  ILE   T CG1 1 
ATOM   34182 C  CG2 . ILE   T  6  40  ? 56.353  -210.211 71.293  1.00 112.71 ? 36  ILE   T CG2 1 
ATOM   34183 C  CD1 . ILE   T  6  40  ? 58.772  -211.443 69.770  1.00 114.85 ? 36  ILE   T CD1 1 
ATOM   34184 N  N   . LYS   T  6  41  ? 53.660  -208.190 70.052  1.00 112.95 ? 37  LYS   T N   1 
ATOM   34185 C  CA  . LYS   T  6  41  ? 53.009  -207.070 70.779  1.00 112.34 ? 37  LYS   T CA  1 
ATOM   34186 C  C   . LYS   T  6  41  ? 53.575  -207.047 72.202  1.00 116.75 ? 37  LYS   T C   1 
ATOM   34187 O  O   . LYS   T  6  41  ? 53.771  -208.141 72.771  1.00 120.61 ? 37  LYS   T O   1 
ATOM   34188 C  CB  . LYS   T  6  41  ? 51.491  -207.264 70.788  1.00 110.11 ? 37  LYS   T CB  1 
ATOM   34189 C  CG  . LYS   T  6  41  ? 50.677  -206.080 71.287  1.00 110.10 ? 37  LYS   T CG  1 
ATOM   34190 C  CD  . LYS   T  6  41  ? 49.226  -206.434 71.497  1.00 111.46 ? 37  LYS   T CD  1 
ATOM   34191 C  CE  . LYS   T  6  41  ? 48.390  -205.268 71.975  1.00 113.38 ? 37  LYS   T CE  1 
ATOM   34192 N  NZ  . LYS   T  6  41  ? 46.955  -205.628 72.034  1.00 115.21 ? 37  LYS   T NZ  1 
ATOM   34193 N  N   . CYS   T  6  42  ? 53.829  -205.857 72.750  1.00 113.99 ? 38  CYS   T N   1 
ATOM   34194 C  CA  . CYS   T  6  42  ? 54.458  -205.673 74.085  1.00 116.18 ? 38  CYS   T CA  1 
ATOM   34195 C  C   . CYS   T  6  42  ? 53.678  -204.632 74.898  1.00 115.52 ? 38  CYS   T C   1 
ATOM   34196 O  O   . CYS   T  6  42  ? 52.609  -204.194 74.427  1.00 111.99 ? 38  CYS   T O   1 
ATOM   34197 C  CB  . CYS   T  6  42  ? 55.932  -205.314 73.929  1.00 120.72 ? 38  CYS   T CB  1 
ATOM   34198 S  SG  . CYS   T  6  42  ? 56.229  -203.646 73.288  1.00 124.01 ? 38  CYS   T SG  1 
ATOM   34199 N  N   . ASN   T  6  43  ? 54.189  -204.293 76.087  1.00 118.15 ? 39  ASN   T N   1 
ATOM   34200 C  CA  . ASN   T  6  43  ? 53.575  -203.368 77.080  1.00 121.83 ? 39  ASN   T CA  1 
ATOM   34201 C  C   . ASN   T  6  43  ? 53.003  -202.123 76.395  1.00 122.06 ? 39  ASN   T C   1 
ATOM   34202 O  O   . ASN   T  6  43  ? 51.795  -201.869 76.561  1.00 126.63 ? 39  ASN   T O   1 
ATOM   34203 C  CB  . ASN   T  6  43  ? 54.588  -202.941 78.145  1.00 123.42 ? 39  ASN   T CB  1 
ATOM   34204 C  CG  . ASN   T  6  43  ? 54.808  -203.998 79.205  1.00 126.00 ? 39  ASN   T CG  1 
ATOM   34205 O  OD1 . ASN   T  6  43  ? 53.905  -204.772 79.513  1.00 127.12 ? 39  ASN   T OD1 1 
ATOM   34206 N  ND2 . ASN   T  6  43  ? 56.003  -204.038 79.770  1.00 130.58 ? 39  ASN   T ND2 1 
ATOM   34207 N  N   . ASP   T  6  44  ? 53.843  -201.375 75.672  1.00 122.13 ? 40  ASP   T N   1 
ATOM   34208 C  CA  . ASP   T  6  44  ? 53.503  -200.036 75.124  1.00 122.97 ? 40  ASP   T CA  1 
ATOM   34209 C  C   . ASP   T  6  44  ? 53.869  -199.951 73.636  1.00 122.14 ? 40  ASP   T C   1 
ATOM   34210 O  O   . ASP   T  6  44  ? 54.095  -198.821 73.158  1.00 121.59 ? 40  ASP   T O   1 
ATOM   34211 C  CB  . ASP   T  6  44  ? 54.205  -198.937 75.927  1.00 125.09 ? 40  ASP   T CB  1 
ATOM   34212 C  CG  . ASP   T  6  44  ? 55.724  -198.972 75.844  1.00 128.38 ? 40  ASP   T CG  1 
ATOM   34213 O  OD1 . ASP   T  6  44  ? 56.266  -200.002 75.392  1.00 129.10 ? 40  ASP   T OD1 1 
ATOM   34214 O  OD2 . ASP   T  6  44  ? 56.354  -197.966 76.232  1.00 130.80 ? 40  ASP   T OD2 1 
ATOM   34215 N  N   . GLY   T  6  45  ? 53.915  -201.081 72.921  1.00 119.91 ? 41  GLY   T N   1 
ATOM   34216 C  CA  . GLY   T  6  45  ? 54.288  -201.081 71.493  1.00 116.22 ? 41  GLY   T CA  1 
ATOM   34217 C  C   . GLY   T  6  45  ? 54.300  -202.460 70.854  1.00 112.36 ? 41  GLY   T C   1 
ATOM   34218 O  O   . GLY   T  6  45  ? 53.633  -203.372 71.378  1.00 109.29 ? 41  GLY   T O   1 
ATOM   34219 N  N   . VAL   T  6  46  ? 55.031  -202.581 69.742  1.00 108.12 ? 42  VAL   T N   1 
ATOM   34220 C  CA  . VAL   T  6  46  ? 55.134  -203.802 68.890  1.00 109.60 ? 42  VAL   T CA  1 
ATOM   34221 C  C   . VAL   T  6  46  ? 56.590  -203.963 68.443  1.00 107.43 ? 42  VAL   T C   1 
ATOM   34222 O  O   . VAL   T  6  46  ? 57.295  -202.942 68.346  1.00 103.40 ? 42  VAL   T O   1 
ATOM   34223 C  CB  . VAL   T  6  46  ? 54.183  -203.728 67.678  1.00 113.10 ? 42  VAL   T CB  1 
ATOM   34224 C  CG1 . VAL   T  6  46  ? 52.737  -203.972 68.082  1.00 116.16 ? 42  VAL   T CG1 1 
ATOM   34225 C  CG2 . VAL   T  6  46  ? 54.313  -202.415 66.917  1.00 114.18 ? 42  VAL   T CG2 1 
ATOM   34226 N  N   . VAL   T  6  47  ? 57.007  -205.205 68.181  1.00 106.97 ? 43  VAL   T N   1 
ATOM   34227 C  CA  . VAL   T  6  47  ? 58.364  -205.558 67.665  1.00 105.60 ? 43  VAL   T CA  1 
ATOM   34228 C  C   . VAL   T  6  47  ? 58.201  -206.464 66.444  1.00 106.93 ? 43  VAL   T C   1 
ATOM   34229 O  O   . VAL   T  6  47  ? 57.444  -207.448 66.537  1.00 110.13 ? 43  VAL   T O   1 
ATOM   34230 C  CB  . VAL   T  6  47  ? 59.220  -206.242 68.745  1.00 104.83 ? 43  VAL   T CB  1 
ATOM   34231 C  CG1 . VAL   T  6  47  ? 60.568  -206.680 68.194  1.00 103.63 ? 43  VAL   T CG1 1 
ATOM   34232 C  CG2 . VAL   T  6  47  ? 59.397  -205.348 69.960  1.00 104.88 ? 43  VAL   T CG2 1 
ATOM   34233 N  N   . PHE   T  6  48  ? 58.907  -206.140 65.358  1.00 107.97 ? 44  PHE   T N   1 
ATOM   34234 C  CA  . PHE   T  6  48  ? 58.927  -206.908 64.087  1.00 107.37 ? 44  PHE   T CA  1 
ATOM   34235 C  C   . PHE   T  6  48  ? 60.337  -207.458 63.872  1.00 107.95 ? 44  PHE   T C   1 
ATOM   34236 O  O   . PHE   T  6  48  ? 61.318  -206.754 64.181  1.00 106.50 ? 44  PHE   T O   1 
ATOM   34237 C  CB  . PHE   T  6  48  ? 58.483  -206.029 62.915  1.00 106.58 ? 44  PHE   T CB  1 
ATOM   34238 C  CG  . PHE   T  6  48  ? 57.215  -205.257 63.175  1.00 106.70 ? 44  PHE   T CG  1 
ATOM   34239 C  CD1 . PHE   T  6  48  ? 55.975  -205.865 63.045  1.00 106.12 ? 44  PHE   T CD1 1 
ATOM   34240 C  CD2 . PHE   T  6  48  ? 57.262  -203.931 63.573  1.00 106.15 ? 44  PHE   T CD2 1 
ATOM   34241 C  CE1 . PHE   T  6  48  ? 54.809  -205.159 63.298  1.00 105.28 ? 44  PHE   T CE1 1 
ATOM   34242 C  CE2 . PHE   T  6  48  ? 56.096  -203.224 63.823  1.00 106.22 ? 44  PHE   T CE2 1 
ATOM   34243 C  CZ  . PHE   T  6  48  ? 54.872  -203.840 63.686  1.00 104.96 ? 44  PHE   T CZ  1 
ATOM   34244 N  N   . ALA   T  6  49  ? 60.421  -208.692 63.376  1.00 108.08 ? 45  ALA   T N   1 
ATOM   34245 C  CA  . ALA   T  6  49  ? 61.679  -209.364 62.986  1.00 109.91 ? 45  ALA   T CA  1 
ATOM   34246 C  C   . ALA   T  6  49  ? 61.417  -210.214 61.742  1.00 109.88 ? 45  ALA   T C   1 
ATOM   34247 O  O   . ALA   T  6  49  ? 60.248  -210.587 61.518  1.00 108.29 ? 45  ALA   T O   1 
ATOM   34248 C  CB  . ALA   T  6  49  ? 62.199  -210.189 64.136  1.00 111.26 ? 45  ALA   T CB  1 
ATOM   34249 N  N   . VAL   T  6  50  ? 62.460  -210.482 60.953  1.00 114.47 ? 46  VAL   T N   1 
ATOM   34250 C  CA  . VAL   T  6  50  ? 62.361  -211.296 59.706  1.00 116.24 ? 46  VAL   T CA  1 
ATOM   34251 C  C   . VAL   T  6  50  ? 63.683  -212.032 59.458  1.00 119.61 ? 46  VAL   T C   1 
ATOM   34252 O  O   . VAL   T  6  50  ? 64.753  -211.513 59.845  1.00 118.48 ? 46  VAL   T O   1 
ATOM   34253 C  CB  . VAL   T  6  50  ? 61.950  -210.428 58.500  1.00 115.05 ? 46  VAL   T CB  1 
ATOM   34254 C  CG1 . VAL   T  6  50  ? 62.975  -209.348 58.186  1.00 113.88 ? 46  VAL   T CG1 1 
ATOM   34255 C  CG2 . VAL   T  6  50  ? 61.660  -211.271 57.266  1.00 116.04 ? 46  VAL   T CG2 1 
ATOM   34256 N  N   . GLU   T  6  51  ? 63.579  -213.208 58.835  1.00 121.96 ? 47  GLU   T N   1 
ATOM   34257 C  CA  . GLU   T  6  51  ? 64.705  -214.058 58.369  1.00 127.82 ? 47  GLU   T CA  1 
ATOM   34258 C  C   . GLU   T  6  51  ? 65.093  -213.611 56.954  1.00 122.60 ? 47  GLU   T C   1 
ATOM   34259 O  O   . GLU   T  6  51  ? 64.216  -213.637 56.068  1.00 120.73 ? 47  GLU   T O   1 
ATOM   34260 C  CB  . GLU   T  6  51  ? 64.272  -215.527 58.426  1.00 131.89 ? 47  GLU   T CB  1 
ATOM   34261 C  CG  . GLU   T  6  51  ? 65.173  -216.493 57.674  1.00 138.95 ? 47  GLU   T CG  1 
ATOM   34262 C  CD  . GLU   T  6  51  ? 64.677  -217.932 57.667  1.00 143.52 ? 47  GLU   T CD  1 
ATOM   34263 O  OE1 . GLU   T  6  51  ? 65.516  -218.841 57.525  1.00 150.61 ? 47  GLU   T OE1 1 
ATOM   34264 O  OE2 . GLU   T  6  51  ? 63.452  -218.144 57.797  1.00 144.98 ? 47  GLU   T OE2 1 
ATOM   34265 N  N   . LYS   T  6  52  ? 66.350  -213.200 56.762  1.00 121.78 ? 48  LYS   T N   1 
ATOM   34266 C  CA  . LYS   T  6  52  ? 66.933  -212.855 55.437  1.00 124.09 ? 48  LYS   T CA  1 
ATOM   34267 C  C   . LYS   T  6  52  ? 67.953  -213.931 55.054  1.00 124.49 ? 48  LYS   T C   1 
ATOM   34268 O  O   . LYS   T  6  52  ? 69.097  -213.850 55.544  1.00 123.95 ? 48  LYS   T O   1 
ATOM   34269 C  CB  . LYS   T  6  52  ? 67.614  -211.484 55.481  1.00 123.61 ? 48  LYS   T CB  1 
ATOM   34270 C  CG  . LYS   T  6  52  ? 66.700  -210.306 55.778  1.00 123.09 ? 48  LYS   T CG  1 
ATOM   34271 C  CD  . LYS   T  6  52  ? 67.449  -209.067 56.216  1.00 125.48 ? 48  LYS   T CD  1 
ATOM   34272 C  CE  . LYS   T  6  52  ? 68.364  -208.514 55.144  1.00 127.03 ? 48  LYS   T CE  1 
ATOM   34273 N  NZ  . LYS   T  6  52  ? 68.908  -207.187 55.519  1.00 127.35 ? 48  LYS   T NZ  1 
ATOM   34274 N  N   . LEU   T  6  53  ? 67.553  -214.902 54.225  1.00 127.48 ? 49  LEU   T N   1 
ATOM   34275 C  CA  . LEU   T  6  53  ? 68.449  -215.985 53.733  1.00 129.34 ? 49  LEU   T CA  1 
ATOM   34276 C  C   . LEU   T  6  53  ? 69.625  -215.342 52.993  1.00 127.01 ? 49  LEU   T C   1 
ATOM   34277 O  O   . LEU   T  6  53  ? 69.373  -214.588 52.033  1.00 120.61 ? 49  LEU   T O   1 
ATOM   34278 C  CB  . LEU   T  6  53  ? 67.690  -216.930 52.793  1.00 128.59 ? 49  LEU   T CB  1 
ATOM   34279 C  CG  . LEU   T  6  53  ? 66.541  -217.736 53.397  1.00 128.87 ? 49  LEU   T CG  1 
ATOM   34280 C  CD1 . LEU   T  6  53  ? 65.920  -218.635 52.339  1.00 128.71 ? 49  LEU   T CD1 1 
ATOM   34281 C  CD2 . LEU   T  6  53  ? 67.001  -218.564 54.589  1.00 134.03 ? 49  LEU   T CD2 1 
ATOM   34282 N  N   . ILE   T  6  54  ? 70.855  -215.619 53.431  1.00 131.16 ? 50  ILE   T N   1 
ATOM   34283 C  CA  . ILE   T  6  54  ? 72.096  -215.188 52.723  1.00 133.76 ? 50  ILE   T CA  1 
ATOM   34284 C  C   . ILE   T  6  54  ? 72.350  -216.203 51.606  1.00 136.28 ? 50  ILE   T C   1 
ATOM   34285 O  O   . ILE   T  6  54  ? 72.991  -217.239 51.879  1.00 142.33 ? 50  ILE   T O   1 
ATOM   34286 C  CB  . ILE   T  6  54  ? 73.298  -215.049 53.682  1.00 135.21 ? 50  ILE   T CB  1 
ATOM   34287 C  CG1 . ILE   T  6  54  ? 72.970  -214.157 54.884  1.00 136.30 ? 50  ILE   T CG1 1 
ATOM   34288 C  CG2 . ILE   T  6  54  ? 74.520  -214.547 52.924  1.00 134.40 ? 50  ILE   T CG2 1 
ATOM   34289 C  CD1 . ILE   T  6  54  ? 74.036  -214.141 55.959  1.00 139.98 ? 50  ILE   T CD1 1 
ATOM   34290 N  N   . THR   T  6  55  ? 71.821  -215.930 50.410  1.00 133.60 ? 51  THR   T N   1 
ATOM   34291 C  CA  . THR   T  6  55  ? 71.968  -216.781 49.199  1.00 134.14 ? 51  THR   T CA  1 
ATOM   34292 C  C   . THR   T  6  55  ? 73.453  -216.964 48.872  1.00 137.59 ? 51  THR   T C   1 
ATOM   34293 O  O   . THR   T  6  55  ? 73.840  -218.102 48.538  1.00 143.90 ? 51  THR   T O   1 
ATOM   34294 C  CB  . THR   T  6  55  ? 71.254  -216.180 47.984  1.00 130.41 ? 51  THR   T CB  1 
ATOM   34295 O  OG1 . THR   T  6  55  ? 69.968  -215.718 48.397  1.00 129.69 ? 51  THR   T OG1 1 
ATOM   34296 C  CG2 . THR   T  6  55  ? 71.109  -217.173 46.851  1.00 129.99 ? 51  THR   T CG2 1 
ATOM   34297 N  N   . SER   T  6  56  ? 74.240  -215.887 48.959  1.00 138.19 ? 52  SER   T N   1 
ATOM   34298 C  CA  . SER   T  6  56  ? 75.668  -215.853 48.549  1.00 139.45 ? 52  SER   T CA  1 
ATOM   34299 C  C   . SER   T  6  56  ? 76.477  -214.908 49.445  1.00 137.28 ? 52  SER   T C   1 
ATOM   34300 O  O   . SER   T  6  56  ? 75.877  -214.001 50.056  1.00 135.18 ? 52  SER   T O   1 
ATOM   34301 C  CB  . SER   T  6  56  ? 75.782  -215.464 47.099  1.00 140.75 ? 52  SER   T CB  1 
ATOM   34302 O  OG  . SER   T  6  56  ? 77.128  -215.181 46.749  1.00 143.80 ? 52  SER   T OG  1 
ATOM   34303 N  N   . LYS   T  6  57  ? 77.796  -215.130 49.496  1.00 139.74 ? 53  LYS   T N   1 
ATOM   34304 C  CA  . LYS   T  6  57  ? 78.807  -214.239 50.131  1.00 138.02 ? 53  LYS   T CA  1 
ATOM   34305 C  C   . LYS   T  6  57  ? 78.705  -212.824 49.540  1.00 133.87 ? 53  LYS   T C   1 
ATOM   34306 O  O   . LYS   T  6  57  ? 79.076  -211.868 50.247  1.00 126.02 ? 53  LYS   T O   1 
ATOM   34307 C  CB  . LYS   T  6  57  ? 80.220  -214.797 49.915  1.00 144.47 ? 53  LYS   T CB  1 
ATOM   34308 C  CG  . LYS   T  6  57  ? 80.724  -215.753 50.988  1.00 147.01 ? 53  LYS   T CG  1 
ATOM   34309 C  CD  . LYS   T  6  57  ? 81.366  -215.050 52.166  1.00 149.45 ? 53  LYS   T CD  1 
ATOM   34310 C  CE  . LYS   T  6  57  ? 82.019  -216.002 53.146  1.00 150.65 ? 53  LYS   T CE  1 
ATOM   34311 N  NZ  . LYS   T  6  57  ? 82.541  -215.287 54.334  1.00 152.05 ? 53  LYS   T NZ  1 
ATOM   34312 N  N   . LEU   T  6  58  ? 78.224  -212.706 48.296  1.00 131.51 ? 54  LEU   T N   1 
ATOM   34313 C  CA  . LEU   T  6  58  ? 78.248  -211.458 47.483  1.00 130.61 ? 54  LEU   T CA  1 
ATOM   34314 C  C   . LEU   T  6  58  ? 77.131  -210.488 47.899  1.00 128.39 ? 54  LEU   T C   1 
ATOM   34315 O  O   . LEU   T  6  58  ? 77.199  -209.319 47.466  1.00 125.35 ? 54  LEU   T O   1 
ATOM   34316 C  CB  . LEU   T  6  58  ? 78.123  -211.827 46.002  1.00 128.47 ? 54  LEU   T CB  1 
ATOM   34317 C  CG  . LEU   T  6  58  ? 79.277  -212.650 45.434  1.00 131.00 ? 54  LEU   T CG  1 
ATOM   34318 C  CD1 . LEU   T  6  58  ? 78.867  -213.344 44.144  1.00 133.13 ? 54  LEU   T CD1 1 
ATOM   34319 C  CD2 . LEU   T  6  58  ? 80.507  -211.784 45.209  1.00 130.09 ? 54  LEU   T CD2 1 
ATOM   34320 N  N   . LEU   T  6  59  ? 76.140  -210.935 48.680  1.00 129.12 ? 55  LEU   T N   1 
ATOM   34321 C  CA  . LEU   T  6  59  ? 75.115  -210.038 49.288  1.00 127.84 ? 55  LEU   T CA  1 
ATOM   34322 C  C   . LEU   T  6  59  ? 75.813  -209.083 50.260  1.00 129.56 ? 55  LEU   T C   1 
ATOM   34323 O  O   . LEU   T  6  59  ? 76.535  -209.580 51.147  1.00 133.29 ? 55  LEU   T O   1 
ATOM   34324 C  CB  . LEU   T  6  59  ? 74.060  -210.854 50.042  1.00 127.33 ? 55  LEU   T CB  1 
ATOM   34325 C  CG  . LEU   T  6  59  ? 73.074  -211.653 49.195  1.00 126.90 ? 55  LEU   T CG  1 
ATOM   34326 C  CD1 . LEU   T  6  59  ? 72.225  -212.546 50.084  1.00 130.37 ? 55  LEU   T CD1 1 
ATOM   34327 C  CD2 . LEU   T  6  59  ? 72.183  -210.741 48.367  1.00 122.99 ? 55  LEU   T CD2 1 
ATOM   34328 N  N   . VAL   T  6  60  ? 75.594  -207.773 50.114  1.00 128.76 ? 56  VAL   T N   1 
ATOM   34329 C  CA  . VAL   T  6  60  ? 76.133  -206.740 51.050  1.00 127.50 ? 56  VAL   T CA  1 
ATOM   34330 C  C   . VAL   T  6  60  ? 75.330  -206.818 52.345  1.00 124.70 ? 56  VAL   T C   1 
ATOM   34331 O  O   . VAL   T  6  60  ? 74.116  -206.624 52.326  1.00 117.78 ? 56  VAL   T O   1 
ATOM   34332 C  CB  . VAL   T  6  60  ? 76.089  -205.322 50.450  1.00 126.11 ? 56  VAL   T CB  1 
ATOM   34333 C  CG1 . VAL   T  6  60  ? 76.643  -204.289 51.421  1.00 127.41 ? 56  VAL   T CG1 1 
ATOM   34334 C  CG2 . VAL   T  6  60  ? 76.826  -205.247 49.122  1.00 127.71 ? 56  VAL   T CG2 1 
ATOM   34335 N  N   . PRO   T  6  61  ? 75.969  -207.117 53.502  1.00 127.89 ? 57  PRO   T N   1 
ATOM   34336 C  CA  . PRO   T  6  61  ? 75.252  -207.193 54.775  1.00 129.27 ? 57  PRO   T CA  1 
ATOM   34337 C  C   . PRO   T  6  61  ? 74.588  -205.861 55.153  1.00 130.20 ? 57  PRO   T C   1 
ATOM   34338 O  O   . PRO   T  6  61  ? 75.153  -204.827 54.849  1.00 132.60 ? 57  PRO   T O   1 
ATOM   34339 C  CB  . PRO   T  6  61  ? 76.339  -207.571 55.797  1.00 130.72 ? 57  PRO   T CB  1 
ATOM   34340 C  CG  . PRO   T  6  61  ? 77.444  -208.185 54.963  1.00 132.15 ? 57  PRO   T CG  1 
ATOM   34341 C  CD  . PRO   T  6  61  ? 77.399  -207.429 53.652  1.00 129.90 ? 57  PRO   T CD  1 
ATOM   34342 N  N   . GLN   T  6  62  ? 73.406  -205.935 55.777  1.00 133.20 ? 58  GLN   T N   1 
ATOM   34343 C  CA  . GLN   T  6  62  ? 72.607  -204.793 56.308  1.00 135.05 ? 58  GLN   T CA  1 
ATOM   34344 C  C   . GLN   T  6  62  ? 72.010  -203.942 55.173  1.00 136.92 ? 58  GLN   T C   1 
ATOM   34345 O  O   . GLN   T  6  62  ? 71.376  -202.920 55.506  1.00 142.81 ? 58  GLN   T O   1 
ATOM   34346 C  CB  . GLN   T  6  62  ? 73.455  -203.914 57.239  1.00 134.42 ? 58  GLN   T CB  1 
ATOM   34347 C  CG  . GLN   T  6  62  ? 73.255  -204.209 58.718  1.00 135.56 ? 58  GLN   T CG  1 
ATOM   34348 C  CD  . GLN   T  6  62  ? 73.720  -205.594 59.097  1.00 139.23 ? 58  GLN   T CD  1 
ATOM   34349 O  OE1 . GLN   T  6  62  ? 74.720  -206.094 58.587  1.00 142.22 ? 58  GLN   T OE1 1 
ATOM   34350 N  NE2 . GLN   T  6  62  ? 72.997  -206.224 60.009  1.00 142.01 ? 58  GLN   T NE2 1 
ATOM   34351 N  N   . LYS   T  6  63  ? 72.160  -204.333 53.899  1.00 136.85 ? 59  LYS   T N   1 
ATOM   34352 C  CA  . LYS   T  6  63  ? 71.882  -203.427 52.745  1.00 135.60 ? 59  LYS   T CA  1 
ATOM   34353 C  C   . LYS   T  6  63  ? 70.815  -203.995 51.795  1.00 128.09 ? 59  LYS   T C   1 
ATOM   34354 O  O   . LYS   T  6  63  ? 70.709  -203.468 50.669  1.00 131.33 ? 59  LYS   T O   1 
ATOM   34355 C  CB  . LYS   T  6  63  ? 73.182  -203.101 51.998  1.00 139.82 ? 59  LYS   T CB  1 
ATOM   34356 C  CG  . LYS   T  6  63  ? 73.955  -201.904 52.542  1.00 144.52 ? 59  LYS   T CG  1 
ATOM   34357 C  CD  . LYS   T  6  63  ? 73.124  -200.634 52.667  1.00 146.79 ? 59  LYS   T CD  1 
ATOM   34358 C  CE  . LYS   T  6  63  ? 73.457  -199.571 51.642  1.00 153.33 ? 59  LYS   T CE  1 
ATOM   34359 N  NZ  . LYS   T  6  63  ? 74.527  -198.666 52.126  1.00 159.88 ? 59  LYS   T NZ  1 
ATOM   34360 N  N   . ASN   T  6  64  ? 70.030  -204.990 52.223  1.00 122.78 ? 60  ASN   T N   1 
ATOM   34361 C  CA  . ASN   T  6  64  ? 68.810  -205.450 51.502  1.00 115.19 ? 60  ASN   T CA  1 
ATOM   34362 C  C   . ASN   T  6  64  ? 67.646  -205.445 52.499  1.00 113.89 ? 60  ASN   T C   1 
ATOM   34363 O  O   . ASN   T  6  64  ? 67.127  -206.528 52.827  1.00 111.45 ? 60  ASN   T O   1 
ATOM   34364 C  CB  . ASN   T  6  64  ? 69.009  -206.812 50.828  1.00 113.65 ? 60  ASN   T CB  1 
ATOM   34365 C  CG  . ASN   T  6  64  ? 69.914  -206.751 49.613  1.00 109.23 ? 60  ASN   T CG  1 
ATOM   34366 O  OD1 . ASN   T  6  64  ? 69.592  -206.092 48.628  1.00 107.19 ? 60  ASN   T OD1 1 
ATOM   34367 N  ND2 . ASN   T  6  64  ? 71.039  -207.446 49.663  1.00 109.36 ? 60  ASN   T ND2 1 
ATOM   34368 N  N   . VAL   T  6  65  ? 67.254  -204.251 52.947  1.00 112.80 ? 61  VAL   T N   1 
ATOM   34369 C  CA  . VAL   T  6  65  ? 66.284  -204.043 54.064  1.00 114.67 ? 61  VAL   T CA  1 
ATOM   34370 C  C   . VAL   T  6  65  ? 64.906  -204.531 53.597  1.00 114.96 ? 61  VAL   T C   1 
ATOM   34371 O  O   . VAL   T  6  65  ? 64.525  -204.205 52.456  1.00 114.65 ? 61  VAL   T O   1 
ATOM   34372 C  CB  . VAL   T  6  65  ? 66.258  -202.571 54.522  1.00 115.03 ? 61  VAL   T CB  1 
ATOM   34373 C  CG1 . VAL   T  6  65  ? 65.362  -202.375 55.735  1.00 117.18 ? 61  VAL   T CG1 1 
ATOM   34374 C  CG2 . VAL   T  6  65  ? 67.656  -202.035 54.811  1.00 116.28 ? 61  VAL   T CG2 1 
ATOM   34375 N  N   . LYS   T  6  66  ? 64.206  -205.300 54.438  1.00 114.89 ? 62  LYS   T N   1 
ATOM   34376 C  CA  . LYS   T  6  66  ? 62.911  -205.954 54.097  1.00 116.59 ? 62  LYS   T CA  1 
ATOM   34377 C  C   . LYS   T  6  66  ? 61.756  -205.355 54.910  1.00 115.38 ? 62  LYS   T C   1 
ATOM   34378 O  O   . LYS   T  6  66  ? 60.644  -205.267 54.346  1.00 114.93 ? 62  LYS   T O   1 
ATOM   34379 C  CB  . LYS   T  6  66  ? 63.001  -207.464 54.322  1.00 120.31 ? 62  LYS   T CB  1 
ATOM   34380 C  CG  . LYS   T  6  66  ? 63.870  -208.197 53.312  1.00 126.49 ? 62  LYS   T CG  1 
ATOM   34381 C  CD  . LYS   T  6  66  ? 63.869  -209.695 53.497  1.00 132.44 ? 62  LYS   T CD  1 
ATOM   34382 C  CE  . LYS   T  6  66  ? 62.659  -210.372 52.889  1.00 138.75 ? 62  LYS   T CE  1 
ATOM   34383 N  NZ  . LYS   T  6  66  ? 62.751  -211.849 52.992  1.00 141.22 ? 62  LYS   T NZ  1 
ATOM   34384 N  N   . ILE   T  6  67  ? 61.987  -204.984 56.176  1.00 112.82 ? 63  ILE   T N   1 
ATOM   34385 C  CA  . ILE   T  6  67  ? 60.974  -204.267 57.010  1.00 111.13 ? 63  ILE   T CA  1 
ATOM   34386 C  C   . ILE   T  6  67  ? 60.803  -202.863 56.417  1.00 107.74 ? 63  ILE   T C   1 
ATOM   34387 O  O   . ILE   T  6  67  ? 61.823  -202.241 56.062  1.00 108.97 ? 63  ILE   T O   1 
ATOM   34388 C  CB  . ILE   T  6  67  ? 61.356  -204.215 58.505  1.00 112.06 ? 63  ILE   T CB  1 
ATOM   34389 C  CG1 . ILE   T  6  67  ? 61.569  -205.609 59.104  1.00 114.70 ? 63  ILE   T CG1 1 
ATOM   34390 C  CG2 . ILE   T  6  67  ? 60.315  -203.428 59.292  1.00 111.09 ? 63  ILE   T CG2 1 
ATOM   34391 C  CD1 . ILE   T  6  67  ? 62.194  -205.598 60.483  1.00 116.92 ? 63  ILE   T CD1 1 
ATOM   34392 N  N   . GLN   T  6  68  ? 59.558  -202.397 56.302  1.00 102.93 ? 64  GLN   T N   1 
ATOM   34393 C  CA  . GLN   T  6  68  ? 59.208  -201.076 55.718  1.00 103.80 ? 64  GLN   T CA  1 
ATOM   34394 C  C   . GLN   T  6  68  ? 58.413  -200.262 56.740  1.00 102.10 ? 64  GLN   T C   1 
ATOM   34395 O  O   . GLN   T  6  68  ? 57.687  -200.872 57.548  1.00 111.21 ? 64  GLN   T O   1 
ATOM   34396 C  CB  . GLN   T  6  68  ? 58.405  -201.264 54.432  1.00 99.03  ? 64  GLN   T CB  1 
ATOM   34397 C  CG  . GLN   T  6  68  ? 59.264  -201.648 53.240  1.00 99.51  ? 64  GLN   T CG  1 
ATOM   34398 C  CD  . GLN   T  6  68  ? 58.460  -201.692 51.964  1.00 100.54 ? 64  GLN   T CD  1 
ATOM   34399 O  OE1 . GLN   T  6  68  ? 57.833  -202.697 51.639  1.00 102.24 ? 64  GLN   T OE1 1 
ATOM   34400 N  NE2 . GLN   T  6  68  ? 58.473  -200.596 51.225  1.00 99.40  ? 64  GLN   T NE2 1 
ATOM   34401 N  N   . VAL   T  6  69  ? 58.547  -198.936 56.691  1.00 100.24 ? 65  VAL   T N   1 
ATOM   34402 C  CA  . VAL   T  6  69  ? 57.771  -197.984 57.539  1.00 99.84  ? 65  VAL   T CA  1 
ATOM   34403 C  C   . VAL   T  6  69  ? 56.638  -197.392 56.693  1.00 96.49  ? 65  VAL   T C   1 
ATOM   34404 O  O   . VAL   T  6  69  ? 56.877  -197.095 55.506  1.00 95.22  ? 65  VAL   T O   1 
ATOM   34405 C  CB  . VAL   T  6  69  ? 58.673  -196.885 58.137  1.00 102.08 ? 65  VAL   T CB  1 
ATOM   34406 C  CG1 . VAL   T  6  69  ? 59.356  -196.049 57.066  1.00 103.35 ? 65  VAL   T CG1 1 
ATOM   34407 C  CG2 . VAL   T  6  69  ? 57.903  -195.990 59.097  1.00 102.66 ? 65  VAL   T CG2 1 
ATOM   34408 N  N   . VAL   T  6  70  ? 55.449  -197.251 57.286  1.00 94.92  ? 66  VAL   T N   1 
ATOM   34409 C  CA  . VAL   T  6  70  ? 54.304  -196.473 56.726  1.00 95.45  ? 66  VAL   T CA  1 
ATOM   34410 C  C   . VAL   T  6  70  ? 54.064  -195.277 57.656  1.00 95.29  ? 66  VAL   T C   1 
ATOM   34411 O  O   . VAL   T  6  70  ? 54.068  -195.481 58.887  1.00 99.14  ? 66  VAL   T O   1 
ATOM   34412 C  CB  . VAL   T  6  70  ? 53.043  -197.346 56.559  1.00 94.95  ? 66  VAL   T CB  1 
ATOM   34413 C  CG1 . VAL   T  6  70  ? 51.827  -196.520 56.166  1.00 96.52  ? 66  VAL   T CG1 1 
ATOM   34414 C  CG2 . VAL   T  6  70  ? 53.265  -198.462 55.550  1.00 93.95  ? 66  VAL   T CG2 1 
ATOM   34415 N  N   . ASP   T  6  71  ? 53.872  -194.084 57.081  1.00 94.63  ? 67  ASP   T N   1 
ATOM   34416 C  CA  . ASP   T  6  71  ? 53.792  -192.784 57.805  1.00 93.94  ? 67  ASP   T CA  1 
ATOM   34417 C  C   . ASP   T  6  71  ? 55.080  -192.621 58.629  1.00 92.55  ? 67  ASP   T C   1 
ATOM   34418 O  O   . ASP   T  6  71  ? 56.168  -192.703 58.024  1.00 88.12  ? 67  ASP   T O   1 
ATOM   34419 C  CB  . ASP   T  6  71  ? 52.480  -192.683 58.592  1.00 93.38  ? 67  ASP   T CB  1 
ATOM   34420 C  CG  . ASP   T  6  71  ? 52.068  -191.254 58.926  1.00 93.95  ? 67  ASP   T CG  1 
ATOM   34421 O  OD1 . ASP   T  6  71  ? 52.825  -190.580 59.651  1.00 94.67  ? 67  ASP   T OD1 1 
ATOM   34422 O  OD2 . ASP   T  6  71  ? 50.994  -190.819 58.449  1.00 93.20  ? 67  ASP   T OD2 1 
ATOM   34423 N  N   . ARG   T  6  72  ? 54.982  -192.387 59.941  1.00 92.56  ? 68  ARG   T N   1 
ATOM   34424 C  CA  . ARG   T  6  72  ? 56.158  -192.294 60.849  1.00 95.11  ? 68  ARG   T CA  1 
ATOM   34425 C  C   . ARG   T  6  72  ? 55.986  -193.212 62.070  1.00 94.59  ? 68  ARG   T C   1 
ATOM   34426 O  O   . ARG   T  6  72  ? 56.956  -193.320 62.846  1.00 93.09  ? 68  ARG   T O   1 
ATOM   34427 C  CB  . ARG   T  6  72  ? 56.385  -190.826 61.236  1.00 94.77  ? 68  ARG   T CB  1 
ATOM   34428 C  CG  . ARG   T  6  72  ? 57.463  -190.136 60.409  1.00 97.49  ? 68  ARG   T CG  1 
ATOM   34429 C  CD  . ARG   T  6  72  ? 57.039  -188.839 59.745  1.00 97.35  ? 68  ARG   T CD  1 
ATOM   34430 N  NE  . ARG   T  6  72  ? 57.342  -187.650 60.533  1.00 100.06 ? 68  ARG   T NE  1 
ATOM   34431 C  CZ  . ARG   T  6  72  ? 57.505  -186.421 60.037  1.00 100.00 ? 68  ARG   T CZ  1 
ATOM   34432 N  NH1 . ARG   T  6  72  ? 57.408  -186.194 58.738  1.00 102.28 ? 68  ARG   T NH1 1 
ATOM   34433 N  NH2 . ARG   T  6  72  ? 57.773  -185.414 60.848  1.00 101.65 ? 68  ARG   T NH2 1 
ATOM   34434 N  N   . HIS   T  6  73  ? 54.838  -193.888 62.209  1.00 96.35  ? 69  HIS   T N   1 
ATOM   34435 C  CA  . HIS   T  6  73  ? 54.429  -194.608 63.448  1.00 97.81  ? 69  HIS   T CA  1 
ATOM   34436 C  C   . HIS   T  6  73  ? 54.062  -196.077 63.184  1.00 98.63  ? 69  HIS   T C   1 
ATOM   34437 O  O   . HIS   T  6  73  ? 53.799  -196.773 64.183  1.00 101.14 ? 69  HIS   T O   1 
ATOM   34438 C  CB  . HIS   T  6  73  ? 53.268  -193.872 64.134  1.00 97.07  ? 69  HIS   T CB  1 
ATOM   34439 C  CG  . HIS   T  6  73  ? 51.982  -193.913 63.379  1.00 97.32  ? 69  HIS   T CG  1 
ATOM   34440 N  ND1 . HIS   T  6  73  ? 51.839  -193.345 62.126  1.00 98.50  ? 69  HIS   T ND1 1 
ATOM   34441 C  CD2 . HIS   T  6  73  ? 50.777  -194.434 63.697  1.00 99.19  ? 69  HIS   T CD2 1 
ATOM   34442 C  CE1 . HIS   T  6  73  ? 50.605  -193.523 61.702  1.00 97.32  ? 69  HIS   T CE1 1 
ATOM   34443 N  NE2 . HIS   T  6  73  ? 49.933  -194.186 62.648  1.00 98.18  ? 69  HIS   T NE2 1 
ATOM   34444 N  N   . ILE   T  6  74  ? 54.040  -196.536 61.924  1.00 98.25  ? 70  ILE   T N   1 
ATOM   34445 C  CA  . ILE   T  6  74  ? 53.643  -197.930 61.547  1.00 97.13  ? 70  ILE   T CA  1 
ATOM   34446 C  C   . ILE   T  6  74  ? 54.831  -198.650 60.899  1.00 98.52  ? 70  ILE   T C   1 
ATOM   34447 O  O   . ILE   T  6  74  ? 55.521  -198.033 60.066  1.00 98.16  ? 70  ILE   T O   1 
ATOM   34448 C  CB  . ILE   T  6  74  ? 52.419  -197.941 60.610  1.00 95.28  ? 70  ILE   T CB  1 
ATOM   34449 C  CG1 . ILE   T  6  74  ? 51.248  -197.135 61.178  1.00 93.91  ? 70  ILE   T CG1 1 
ATOM   34450 C  CG2 . ILE   T  6  74  ? 52.005  -199.371 60.294  1.00 95.39  ? 70  ILE   T CG2 1 
ATOM   34451 C  CD1 . ILE   T  6  74  ? 50.183  -196.803 60.159  1.00 92.54  ? 70  ILE   T CD1 1 
ATOM   34452 N  N   . GLY   T  6  75  ? 55.022  -199.924 61.253  1.00 99.81  ? 71  GLY   T N   1 
ATOM   34453 C  CA  . GLY   T  6  75  ? 56.006  -200.837 60.640  1.00 102.93 ? 71  GLY   T CA  1 
ATOM   34454 C  C   . GLY   T  6  75  ? 55.318  -202.019 59.979  1.00 100.76 ? 71  GLY   T C   1 
ATOM   34455 O  O   . GLY   T  6  75  ? 54.325  -202.515 60.547  1.00 98.89  ? 71  GLY   T O   1 
ATOM   34456 N  N   . CYS   T  6  76  ? 55.817  -202.452 58.818  1.00 102.45 ? 72  CYS   T N   1 
ATOM   34457 C  CA  . CYS   T  6  76  ? 55.264  -203.580 58.023  1.00 105.23 ? 72  CYS   T CA  1 
ATOM   34458 C  C   . CYS   T  6  76  ? 56.379  -204.565 57.671  1.00 104.13 ? 72  CYS   T C   1 
ATOM   34459 O  O   . CYS   T  6  76  ? 57.475  -204.118 57.281  1.00 107.76 ? 72  CYS   T O   1 
ATOM   34460 C  CB  . CYS   T  6  76  ? 54.606  -203.104 56.733  1.00 105.99 ? 72  CYS   T CB  1 
ATOM   34461 S  SG  . CYS   T  6  76  ? 53.234  -201.950 56.990  1.00 112.24 ? 72  CYS   T SG  1 
ATOM   34462 N  N   . VAL   T  6  77  ? 56.093  -205.857 57.813  1.00 104.58 ? 73  VAL   T N   1 
ATOM   34463 C  CA  . VAL   T  6  77  ? 56.969  -206.972 57.355  1.00 105.38 ? 73  VAL   T CA  1 
ATOM   34464 C  C   . VAL   T  6  77  ? 56.063  -208.054 56.761  1.00 103.25 ? 73  VAL   T C   1 
ATOM   34465 O  O   . VAL   T  6  77  ? 54.921  -208.202 57.242  1.00 101.11 ? 73  VAL   T O   1 
ATOM   34466 C  CB  . VAL   T  6  77  ? 57.838  -207.506 58.507  1.00 105.73 ? 73  VAL   T CB  1 
ATOM   34467 C  CG1 . VAL   T  6  77  ? 57.026  -208.307 59.516  1.00 105.72 ? 73  VAL   T CG1 1 
ATOM   34468 C  CG2 . VAL   T  6  77  ? 59.005  -208.322 57.981  1.00 108.51 ? 73  VAL   T CG2 1 
ATOM   34469 N  N   . TYR   T  6  78  ? 56.546  -208.772 55.747  1.00 104.88 ? 74  TYR   T N   1 
ATOM   34470 C  CA  . TYR   T  6  78  ? 55.745  -209.770 54.994  1.00 106.04 ? 74  TYR   T CA  1 
ATOM   34471 C  C   . TYR   T  6  78  ? 56.632  -210.933 54.539  1.00 108.26 ? 74  TYR   T C   1 
ATOM   34472 O  O   . TYR   T  6  78  ? 57.868  -210.777 54.433  1.00 110.72 ? 74  TYR   T O   1 
ATOM   34473 C  CB  . TYR   T  6  78  ? 55.033  -209.096 53.819  1.00 101.23 ? 74  TYR   T CB  1 
ATOM   34474 C  CG  . TYR   T  6  78  ? 55.856  -208.057 53.100  1.00 100.11 ? 74  TYR   T CG  1 
ATOM   34475 C  CD1 . TYR   T  6  78  ? 56.843  -208.424 52.198  1.00 101.38 ? 74  TYR   T CD1 1 
ATOM   34476 C  CD2 . TYR   T  6  78  ? 55.656  -206.704 53.323  1.00 98.59  ? 74  TYR   T CD2 1 
ATOM   34477 C  CE1 . TYR   T  6  78  ? 57.605  -207.477 51.535  1.00 100.11 ? 74  TYR   T CE1 1 
ATOM   34478 C  CE2 . TYR   T  6  78  ? 56.409  -205.743 52.668  1.00 97.64  ? 74  TYR   T CE2 1 
ATOM   34479 C  CZ  . TYR   T  6  78  ? 57.389  -206.130 51.770  1.00 97.62  ? 74  TYR   T CZ  1 
ATOM   34480 O  OH  . TYR   T  6  78  ? 58.139  -205.194 51.122  1.00 95.26  ? 74  TYR   T OH  1 
ATOM   34481 N  N   . SER   T  6  79  ? 55.988  -212.077 54.294  1.00 110.71 ? 75  SER   T N   1 
ATOM   34482 C  CA  . SER   T  6  79  ? 56.587  -213.314 53.734  1.00 113.74 ? 75  SER   T CA  1 
ATOM   34483 C  C   . SER   T  6  79  ? 55.889  -213.641 52.412  1.00 109.82 ? 75  SER   T C   1 
ATOM   34484 O  O   . SER   T  6  79  ? 54.676  -213.367 52.311  1.00 104.06 ? 75  SER   T O   1 
ATOM   34485 C  CB  . SER   T  6  79  ? 56.476  -214.454 54.710  1.00 117.89 ? 75  SER   T CB  1 
ATOM   34486 O  OG  . SER   T  6  79  ? 57.169  -214.161 55.914  1.00 125.07 ? 75  SER   T OG  1 
ATOM   34487 N  N   . GLY   T  6  80  ? 56.634  -214.192 51.449  1.00 111.85 ? 76  GLY   T N   1 
ATOM   34488 C  CA  . GLY   T  6  80  ? 56.128  -214.603 50.123  1.00 111.60 ? 76  GLY   T CA  1 
ATOM   34489 C  C   . GLY   T  6  80  ? 56.796  -213.826 49.001  1.00 110.28 ? 76  GLY   T C   1 
ATOM   34490 O  O   . GLY   T  6  80  ? 58.022  -213.602 49.092  1.00 113.46 ? 76  GLY   T O   1 
ATOM   34491 N  N   . LEU   T  6  81  ? 56.025  -213.428 47.983  1.00 107.93 ? 77  LEU   T N   1 
ATOM   34492 C  CA  . LEU   T  6  81  ? 56.514  -212.617 46.832  1.00 106.40 ? 77  LEU   T CA  1 
ATOM   34493 C  C   . LEU   T  6  81  ? 56.817  -211.199 47.328  1.00 104.58 ? 77  LEU   T C   1 
ATOM   34494 O  O   . LEU   T  6  81  ? 55.857  -210.452 47.595  1.00 97.54  ? 77  LEU   T O   1 
ATOM   34495 C  CB  . LEU   T  6  81  ? 55.459  -212.587 45.720  1.00 106.17 ? 77  LEU   T CB  1 
ATOM   34496 C  CG  . LEU   T  6  81  ? 54.946  -213.938 45.225  1.00 106.55 ? 77  LEU   T CG  1 
ATOM   34497 C  CD1 . LEU   T  6  81  ? 54.044  -213.747 44.016  1.00 108.01 ? 77  LEU   T CD1 1 
ATOM   34498 C  CD2 . LEU   T  6  81  ? 56.089  -214.883 44.889  1.00 109.14 ? 77  LEU   T CD2 1 
ATOM   34499 N  N   . ILE   T  6  82  ? 58.100  -210.844 47.439  1.00 105.45 ? 78  ILE   T N   1 
ATOM   34500 C  CA  . ILE   T  6  82  ? 58.565  -209.562 48.052  1.00 105.73 ? 78  ILE   T CA  1 
ATOM   34501 C  C   . ILE   T  6  82  ? 57.996  -208.373 47.274  1.00 104.10 ? 78  ILE   T C   1 
ATOM   34502 O  O   . ILE   T  6  82  ? 57.494  -207.429 47.885  1.00 101.21 ? 78  ILE   T O   1 
ATOM   34503 C  CB  . ILE   T  6  82  ? 60.105  -209.527 48.166  1.00 107.41 ? 78  ILE   T CB  1 
ATOM   34504 C  CG1 . ILE   T  6  82  ? 60.629  -210.627 49.095  1.00 109.65 ? 78  ILE   T CG1 1 
ATOM   34505 C  CG2 . ILE   T  6  82  ? 60.595  -208.153 48.601  1.00 107.40 ? 78  ILE   T CG2 1 
ATOM   34506 C  CD1 . ILE   T  6  82  ? 60.003  -210.636 50.476  1.00 109.43 ? 78  ILE   T CD1 1 
ATOM   34507 N  N   . PRO   T  6  83  ? 58.053  -208.354 45.921  1.00 104.46 ? 79  PRO   T N   1 
ATOM   34508 C  CA  . PRO   T  6  83  ? 57.437  -207.274 45.147  1.00 102.85 ? 79  PRO   T CA  1 
ATOM   34509 C  C   . PRO   T  6  83  ? 55.959  -207.017 45.484  1.00 102.44 ? 79  PRO   T C   1 
ATOM   34510 O  O   . PRO   T  6  83  ? 55.587  -205.866 45.561  1.00 104.58 ? 79  PRO   T O   1 
ATOM   34511 C  CB  . PRO   T  6  83  ? 57.585  -207.750 43.695  1.00 104.13 ? 79  PRO   T CB  1 
ATOM   34512 C  CG  . PRO   T  6  83  ? 58.829  -208.608 43.728  1.00 105.62 ? 79  PRO   T CG  1 
ATOM   34513 C  CD  . PRO   T  6  83  ? 58.758  -209.320 45.062  1.00 106.36 ? 79  PRO   T CD  1 
ATOM   34514 N  N   . ASP   T  6  84  ? 55.164  -208.076 45.670  1.00 102.02 ? 80  ASP   T N   1 
ATOM   34515 C  CA  . ASP   T  6  84  ? 53.720  -207.985 46.029  1.00 99.82  ? 80  ASP   T CA  1 
ATOM   34516 C  C   . ASP   T  6  84  ? 53.565  -207.251 47.365  1.00 97.66  ? 80  ASP   T C   1 
ATOM   34517 O  O   . ASP   T  6  84  ? 52.582  -206.498 47.510  1.00 92.89  ? 80  ASP   T O   1 
ATOM   34518 C  CB  . ASP   T  6  84  ? 53.054  -209.363 46.105  1.00 100.78 ? 80  ASP   T CB  1 
ATOM   34519 C  CG  . ASP   T  6  84  ? 52.515  -209.872 44.779  1.00 101.42 ? 80  ASP   T CG  1 
ATOM   34520 O  OD1 . ASP   T  6  84  ? 53.074  -209.491 43.730  1.00 104.36 ? 80  ASP   T OD1 1 
ATOM   34521 O  OD2 . ASP   T  6  84  ? 51.536  -210.647 44.806  1.00 99.73  ? 80  ASP   T OD2 1 
ATOM   34522 N  N   . GLY   T  6  85  ? 54.485  -207.482 48.306  1.00 98.30  ? 81  GLY   T N   1 
ATOM   34523 C  CA  . GLY   T  6  85  ? 54.512  -206.806 49.617  1.00 99.45  ? 81  GLY   T CA  1 
ATOM   34524 C  C   . GLY   T  6  85  ? 54.763  -205.314 49.470  1.00 98.34  ? 81  GLY   T C   1 
ATOM   34525 O  O   . GLY   T  6  85  ? 54.042  -204.528 50.115  1.00 95.40  ? 81  GLY   T O   1 
ATOM   34526 N  N   . ARG   T  6  86  ? 55.743  -204.938 48.641  1.00 98.64  ? 82  ARG   T N   1 
ATOM   34527 C  CA  . ARG   T  6  86  ? 56.117  -203.522 48.371  1.00 98.60  ? 82  ARG   T CA  1 
ATOM   34528 C  C   . ARG   T  6  86  ? 54.912  -202.781 47.777  1.00 99.59  ? 82  ARG   T C   1 
ATOM   34529 O  O   . ARG   T  6  86  ? 54.661  -201.639 48.208  1.00 99.14  ? 82  ARG   T O   1 
ATOM   34530 C  CB  . ARG   T  6  86  ? 57.334  -203.432 47.443  1.00 97.95  ? 82  ARG   T CB  1 
ATOM   34531 C  CG  . ARG   T  6  86  ? 58.669  -203.573 48.161  1.00 100.48 ? 82  ARG   T CG  1 
ATOM   34532 C  CD  . ARG   T  6  86  ? 59.852  -203.178 47.295  1.00 104.22 ? 82  ARG   T CD  1 
ATOM   34533 N  NE  . ARG   T  6  86  ? 59.678  -201.852 46.716  1.00 105.06 ? 82  ARG   T NE  1 
ATOM   34534 C  CZ  . ARG   T  6  86  ? 59.863  -200.699 47.360  1.00 106.23 ? 82  ARG   T CZ  1 
ATOM   34535 N  NH1 . ARG   T  6  86  ? 60.245  -200.684 48.628  1.00 110.05 ? 82  ARG   T NH1 1 
ATOM   34536 N  NH2 . ARG   T  6  86  ? 59.659  -199.555 46.729  1.00 103.90 ? 82  ARG   T NH2 1 
ATOM   34537 N  N   . HIS   T  6  87  ? 54.195  -203.407 46.838  1.00 98.86  ? 83  HIS   T N   1 
ATOM   34538 C  CA  . HIS   T  6  87  ? 52.956  -202.859 46.221  1.00 98.49  ? 83  HIS   T CA  1 
ATOM   34539 C  C   . HIS   T  6  87  ? 51.937  -202.528 47.317  1.00 99.25  ? 83  HIS   T C   1 
ATOM   34540 O  O   . HIS   T  6  87  ? 51.313  -201.454 47.229  1.00 99.35  ? 83  HIS   T O   1 
ATOM   34541 C  CB  . HIS   T  6  87  ? 52.361  -203.831 45.193  1.00 97.05  ? 83  HIS   T CB  1 
ATOM   34542 C  CG  . HIS   T  6  87  ? 51.109  -203.325 44.557  1.00 95.58  ? 83  HIS   T CG  1 
ATOM   34543 N  ND1 . HIS   T  6  87  ? 51.102  -202.716 43.320  1.00 96.35  ? 83  HIS   T ND1 1 
ATOM   34544 C  CD2 . HIS   T  6  87  ? 49.829  -203.320 44.989  1.00 95.82  ? 83  HIS   T CD2 1 
ATOM   34545 C  CE1 . HIS   T  6  87  ? 49.870  -202.371 43.010  1.00 97.52  ? 83  HIS   T CE1 1 
ATOM   34546 N  NE2 . HIS   T  6  87  ? 49.071  -202.728 44.019  1.00 96.46  ? 83  HIS   T NE2 1 
ATOM   34547 N  N   . LEU   T  6  88  ? 51.774  -203.421 48.302  1.00 99.50  ? 84  LEU   T N   1 
ATOM   34548 C  CA  . LEU   T  6  88  ? 50.780  -203.275 49.399  1.00 99.13  ? 84  LEU   T CA  1 
ATOM   34549 C  C   . LEU   T  6  88  ? 51.185  -202.111 50.317  1.00 99.55  ? 84  LEU   T C   1 
ATOM   34550 O  O   . LEU   T  6  88  ? 50.283  -201.364 50.751  1.00 98.26  ? 84  LEU   T O   1 
ATOM   34551 C  CB  . LEU   T  6  88  ? 50.671  -204.597 50.169  1.00 100.50 ? 84  LEU   T CB  1 
ATOM   34552 C  CG  . LEU   T  6  88  ? 49.513  -204.697 51.163  1.00 103.17 ? 84  LEU   T CG  1 
ATOM   34553 C  CD1 . LEU   T  6  88  ? 48.178  -204.377 50.506  1.00 102.12 ? 84  LEU   T CD1 1 
ATOM   34554 C  CD2 . LEU   T  6  88  ? 49.465  -206.082 51.788  1.00 107.33 ? 84  LEU   T CD2 1 
ATOM   34555 N  N   . VAL   T  6  89  ? 52.486  -201.953 50.590  1.00 98.19  ? 85  VAL   T N   1 
ATOM   34556 C  CA  . VAL   T  6  89  ? 53.036  -200.862 51.453  1.00 98.68  ? 85  VAL   T CA  1 
ATOM   34557 C  C   . VAL   T  6  89  ? 52.879  -199.522 50.725  1.00 98.26  ? 85  VAL   T C   1 
ATOM   34558 O  O   . VAL   T  6  89  ? 52.495  -198.540 51.391  1.00 102.07 ? 85  VAL   T O   1 
ATOM   34559 C  CB  . VAL   T  6  89  ? 54.504  -201.119 51.846  1.00 99.04  ? 85  VAL   T CB  1 
ATOM   34560 C  CG1 . VAL   T  6  89  ? 55.145  -199.896 52.485  1.00 99.12  ? 85  VAL   T CG1 1 
ATOM   34561 C  CG2 . VAL   T  6  89  ? 54.634  -202.323 52.766  1.00 100.12 ? 85  VAL   T CG2 1 
ATOM   34562 N  N   . ASN   T  6  90  ? 53.183  -199.477 49.423  1.00 95.57  ? 86  ASN   T N   1 
ATOM   34563 C  CA  . ASN   T  6  90  ? 53.021  -198.266 48.571  1.00 93.30  ? 86  ASN   T CA  1 
ATOM   34564 C  C   . ASN   T  6  90  ? 51.578  -197.763 48.677  1.00 93.89  ? 86  ASN   T C   1 
ATOM   34565 O  O   . ASN   T  6  90  ? 51.392  -196.542 48.829  1.00 96.13  ? 86  ASN   T O   1 
ATOM   34566 C  CB  . ASN   T  6  90  ? 53.395  -198.524 47.109  1.00 88.76  ? 86  ASN   T CB  1 
ATOM   34567 C  CG  . ASN   T  6  90  ? 54.888  -198.578 46.868  1.00 88.77  ? 86  ASN   T CG  1 
ATOM   34568 O  OD1 . ASN   T  6  90  ? 55.365  -199.407 46.101  1.00 88.66  ? 86  ASN   T OD1 1 
ATOM   34569 N  ND2 . ASN   T  6  90  ? 55.639  -197.695 47.502  1.00 90.38  ? 86  ASN   T ND2 1 
ATOM   34570 N  N   . ARG   T  6  91  ? 50.601  -198.671 48.605  1.00 93.29  ? 87  ARG   T N   1 
ATOM   34571 C  CA  . ARG   T  6  91  ? 49.161  -198.354 48.791  1.00 92.60  ? 87  ARG   T CA  1 
ATOM   34572 C  C   . ARG   T  6  91  ? 48.937  -197.880 50.231  1.00 89.41  ? 87  ARG   T C   1 
ATOM   34573 O  O   . ARG   T  6  91  ? 48.273  -196.847 50.415  1.00 84.92  ? 87  ARG   T O   1 
ATOM   34574 C  CB  . ARG   T  6  91  ? 48.292  -199.578 48.488  1.00 93.56  ? 87  ARG   T CB  1 
ATOM   34575 C  CG  . ARG   T  6  91  ? 46.804  -199.342 48.699  1.00 93.61  ? 87  ARG   T CG  1 
ATOM   34576 C  CD  . ARG   T  6  91  ? 46.226  -198.411 47.659  1.00 94.64  ? 87  ARG   T CD  1 
ATOM   34577 N  NE  . ARG   T  6  91  ? 44.822  -198.157 47.932  1.00 95.79  ? 87  ARG   T NE  1 
ATOM   34578 C  CZ  . ARG   T  6  91  ? 43.937  -197.725 47.039  1.00 95.97  ? 87  ARG   T CZ  1 
ATOM   34579 N  NH1 . ARG   T  6  91  ? 44.296  -197.503 45.785  1.00 94.99  ? 87  ARG   T NH1 1 
ATOM   34580 N  NH2 . ARG   T  6  91  ? 42.683  -197.523 47.407  1.00 97.68  ? 87  ARG   T NH2 1 
ATOM   34581 N  N   . GLY   T  6  92  ? 49.462  -198.628 51.205  1.00 91.84  ? 88  GLY   T N   1 
ATOM   34582 C  CA  . GLY   T  6  92  ? 49.397  -198.293 52.641  1.00 92.62  ? 88  GLY   T CA  1 
ATOM   34583 C  C   . GLY   T  6  92  ? 49.833  -196.861 52.906  1.00 91.72  ? 88  GLY   T C   1 
ATOM   34584 O  O   . GLY   T  6  92  ? 49.171  -196.184 53.715  1.00 90.38  ? 88  GLY   T O   1 
ATOM   34585 N  N   . ARG   T  6  93  ? 50.901  -196.414 52.238  1.00 90.74  ? 89  ARG   T N   1 
ATOM   34586 C  CA  . ARG   T  6  93  ? 51.470  -195.045 52.371  1.00 91.03  ? 89  ARG   T CA  1 
ATOM   34587 C  C   . ARG   T  6  93  ? 50.510  -194.019 51.753  1.00 88.37  ? 89  ARG   T C   1 
ATOM   34588 O  O   . ARG   T  6  93  ? 50.323  -192.948 52.361  1.00 85.19  ? 89  ARG   T O   1 
ATOM   34589 C  CB  . ARG   T  6  93  ? 52.865  -194.994 51.740  1.00 92.69  ? 89  ARG   T CB  1 
ATOM   34590 C  CG  . ARG   T  6  93  ? 53.918  -195.734 52.552  1.00 95.64  ? 89  ARG   T CG  1 
ATOM   34591 C  CD  . ARG   T  6  93  ? 55.185  -196.048 51.781  1.00 98.26  ? 89  ARG   T CD  1 
ATOM   34592 N  NE  . ARG   T  6  93  ? 56.205  -196.622 52.652  1.00 99.49  ? 89  ARG   T NE  1 
ATOM   34593 C  CZ  . ARG   T  6  93  ? 57.395  -197.066 52.252  1.00 100.22 ? 89  ARG   T CZ  1 
ATOM   34594 N  NH1 . ARG   T  6  93  ? 57.742  -197.004 50.976  1.00 101.13 ? 89  ARG   T NH1 1 
ATOM   34595 N  NH2 . ARG   T  6  93  ? 58.236  -197.571 53.139  1.00 100.95 ? 89  ARG   T NH2 1 
ATOM   34596 N  N   . GLU   T  6  94  ? 49.921  -194.334 50.597  1.00 88.47  ? 90  GLU   T N   1 
ATOM   34597 C  CA  . GLU   T  6  94  ? 48.918  -193.472 49.914  1.00 88.26  ? 90  GLU   T CA  1 
ATOM   34598 C  C   . GLU   T  6  94  ? 47.676  -193.323 50.803  1.00 88.59  ? 90  GLU   T C   1 
ATOM   34599 O  O   . GLU   T  6  94  ? 47.158  -192.194 50.899  1.00 85.87  ? 90  GLU   T O   1 
ATOM   34600 C  CB  . GLU   T  6  94  ? 48.543  -194.048 48.547  1.00 88.34  ? 90  GLU   T CB  1 
ATOM   34601 C  CG  . GLU   T  6  94  ? 49.608  -193.838 47.490  1.00 91.59  ? 90  GLU   T CG  1 
ATOM   34602 C  CD  . GLU   T  6  94  ? 49.353  -194.593 46.200  1.00 94.57  ? 90  GLU   T CD  1 
ATOM   34603 O  OE1 . GLU   T  6  94  ? 48.172  -194.839 45.882  1.00 97.58  ? 90  GLU   T OE1 1 
ATOM   34604 O  OE2 . GLU   T  6  94  ? 50.338  -194.942 45.523  1.00 103.77 ? 90  GLU   T OE2 1 
ATOM   34605 N  N   . GLU   T  6  95  ? 47.213  -194.419 51.416  1.00 90.17  ? 91  GLU   T N   1 
ATOM   34606 C  CA  . GLU   T  6  95  ? 46.014  -194.444 52.299  1.00 90.73  ? 91  GLU   T CA  1 
ATOM   34607 C  C   . GLU   T  6  95  ? 46.276  -193.571 53.530  1.00 87.81  ? 91  GLU   T C   1 
ATOM   34608 O  O   . GLU   T  6  95  ? 45.393  -192.765 53.880  1.00 87.24  ? 91  GLU   T O   1 
ATOM   34609 C  CB  . GLU   T  6  95  ? 45.670  -195.874 52.730  1.00 92.58  ? 91  GLU   T CB  1 
ATOM   34610 C  CG  . GLU   T  6  95  ? 45.200  -196.774 51.596  1.00 96.25  ? 91  GLU   T CG  1 
ATOM   34611 C  CD  . GLU   T  6  95  ? 43.777  -196.562 51.103  1.00 98.70  ? 91  GLU   T CD  1 
ATOM   34612 O  OE1 . GLU   T  6  95  ? 43.173  -195.520 51.432  1.00 100.57 ? 91  GLU   T OE1 1 
ATOM   34613 O  OE2 . GLU   T  6  95  ? 43.271  -197.450 50.383  1.00 104.19 ? 91  GLU   T OE2 1 
ATOM   34614 N  N   . ALA   T  6  96  ? 47.446  -193.738 54.156  1.00 89.80  ? 92  ALA   T N   1 
ATOM   34615 C  CA  . ALA   T  6  96  ? 47.864  -193.055 55.405  1.00 88.71  ? 92  ALA   T CA  1 
ATOM   34616 C  C   . ALA   T  6  96  ? 48.037  -191.551 55.166  1.00 87.47  ? 92  ALA   T C   1 
ATOM   34617 O  O   . ALA   T  6  96  ? 47.729  -190.771 56.087  1.00 85.26  ? 92  ALA   T O   1 
ATOM   34618 C  CB  . ALA   T  6  96  ? 49.142  -193.665 55.925  1.00 91.09  ? 92  ALA   T CB  1 
ATOM   34619 N  N   . ALA   T  6  97  ? 48.543  -191.174 53.988  1.00 88.26  ? 93  ALA   T N   1 
ATOM   34620 C  CA  . ALA   T  6  97  ? 48.783  -189.771 53.576  1.00 88.44  ? 93  ALA   T CA  1 
ATOM   34621 C  C   . ALA   T  6  97  ? 47.445  -189.038 53.411  1.00 89.03  ? 93  ALA   T C   1 
ATOM   34622 O  O   . ALA   T  6  97  ? 47.331  -187.917 53.942  1.00 90.70  ? 93  ALA   T O   1 
ATOM   34623 C  CB  . ALA   T  6  97  ? 49.603  -189.731 52.309  1.00 90.75  ? 93  ALA   T CB  1 
ATOM   34624 N  N   . SER   T  6  98  ? 46.471  -189.647 52.721  1.00 89.87  ? 94  SER   T N   1 
ATOM   34625 C  CA  . SER   T  6  98  ? 45.135  -189.049 52.445  1.00 88.91  ? 94  SER   T CA  1 
ATOM   34626 C  C   . SER   T  6  98  ? 44.345  -188.917 53.752  1.00 88.30  ? 94  SER   T C   1 
ATOM   34627 O  O   . SER   T  6  98  ? 43.552  -187.969 53.860  1.00 87.58  ? 94  SER   T O   1 
ATOM   34628 C  CB  . SER   T  6  98  ? 44.353  -189.833 51.416  1.00 89.41  ? 94  SER   T CB  1 
ATOM   34629 O  OG  . SER   T  6  98  ? 43.484  -190.769 52.040  1.00 86.91  ? 94  SER   T OG  1 
ATOM   34630 N  N   . PHE   T  6  99  ? 44.543  -189.840 54.699  1.00 90.14  ? 95  PHE   T N   1 
ATOM   34631 C  CA  . PHE   T  6  99  ? 43.915  -189.806 56.047  1.00 92.37  ? 95  PHE   T CA  1 
ATOM   34632 C  C   . PHE   T  6  99  ? 44.461  -188.602 56.826  1.00 92.64  ? 95  PHE   T C   1 
ATOM   34633 O  O   . PHE   T  6  99  ? 43.650  -187.820 57.360  1.00 94.26  ? 95  PHE   T O   1 
ATOM   34634 C  CB  . PHE   T  6  99  ? 44.145  -191.115 56.809  1.00 92.79  ? 95  PHE   T CB  1 
ATOM   34635 C  CG  . PHE   T  6  99  ? 43.321  -191.245 58.066  1.00 93.19  ? 95  PHE   T CG  1 
ATOM   34636 C  CD1 . PHE   T  6  99  ? 43.748  -190.679 59.257  1.00 94.32  ? 95  PHE   T CD1 1 
ATOM   34637 C  CD2 . PHE   T  6  99  ? 42.108  -191.916 58.056  1.00 92.77  ? 95  PHE   T CD2 1 
ATOM   34638 C  CE1 . PHE   T  6  99  ? 42.986  -190.788 60.410  1.00 96.04  ? 95  PHE   T CE1 1 
ATOM   34639 C  CE2 . PHE   T  6  99  ? 41.346  -192.024 59.210  1.00 94.44  ? 95  PHE   T CE2 1 
ATOM   34640 C  CZ  . PHE   T  6  99  ? 41.786  -191.460 60.385  1.00 95.21  ? 95  PHE   T CZ  1 
ATOM   34641 N  N   . LYS   T  6  100 ? 45.790  -188.460 56.881  1.00 92.97  ? 96  LYS   T N   1 
ATOM   34642 C  CA  . LYS   T  6  100 ? 46.488  -187.352 57.592  1.00 93.98  ? 96  LYS   T CA  1 
ATOM   34643 C  C   . LYS   T  6  100 ? 46.138  -186.016 56.917  1.00 93.88  ? 96  LYS   T C   1 
ATOM   34644 O  O   . LYS   T  6  100 ? 46.012  -185.007 57.639  1.00 94.79  ? 96  LYS   T O   1 
ATOM   34645 C  CB  . LYS   T  6  100 ? 47.999  -187.619 57.650  1.00 95.39  ? 96  LYS   T CB  1 
ATOM   34646 C  CG  . LYS   T  6  100 ? 48.868  -186.448 58.101  1.00 96.54  ? 96  LYS   T CG  1 
ATOM   34647 C  CD  . LYS   T  6  100 ? 49.696  -186.712 59.351  1.00 98.44  ? 96  LYS   T CD  1 
ATOM   34648 C  CE  . LYS   T  6  100 ? 50.789  -187.746 59.171  1.00 98.12  ? 96  LYS   T CE  1 
ATOM   34649 N  NZ  . LYS   T  6  100 ? 51.991  -187.184 58.511  1.00 98.88  ? 96  LYS   T NZ  1 
ATOM   34650 N  N   . LYS   T  6  101 ? 45.965  -186.010 55.592  1.00 93.63  ? 97  LYS   T N   1 
ATOM   34651 C  CA  . LYS   T  6  101 ? 45.622  -184.793 54.809  1.00 93.16  ? 97  LYS   T CA  1 
ATOM   34652 C  C   . LYS   T  6  101 ? 44.257  -184.257 55.261  1.00 92.35  ? 97  LYS   T C   1 
ATOM   34653 O  O   . LYS   T  6  101 ? 44.172  -183.052 55.568  1.00 94.11  ? 97  LYS   T O   1 
ATOM   34654 C  CB  . LYS   T  6  101 ? 45.610  -185.103 53.309  1.00 95.80  ? 97  LYS   T CB  1 
ATOM   34655 C  CG  . LYS   T  6  101 ? 45.501  -183.890 52.395  1.00 98.39  ? 97  LYS   T CG  1 
ATOM   34656 C  CD  . LYS   T  6  101 ? 45.484  -184.249 50.924  1.00 102.51 ? 97  LYS   T CD  1 
ATOM   34657 C  CE  . LYS   T  6  101 ? 45.561  -183.042 50.014  1.00 105.65 ? 97  LYS   T CE  1 
ATOM   34658 N  NZ  . LYS   T  6  101 ? 44.351  -182.191 50.111  1.00 109.15 ? 97  LYS   T NZ  1 
ATOM   34659 N  N   . LEU   T  6  102 ? 43.235  -185.118 55.299  1.00 89.21  ? 98  LEU   T N   1 
ATOM   34660 C  CA  . LEU   T  6  102 ? 41.818  -184.725 55.532  1.00 89.05  ? 98  LEU   T CA  1 
ATOM   34661 C  C   . LEU   T  6  102 ? 41.555  -184.550 57.034  1.00 86.85  ? 98  LEU   T C   1 
ATOM   34662 O  O   . LEU   T  6  102 ? 40.861  -183.579 57.392  1.00 84.38  ? 98  LEU   T O   1 
ATOM   34663 C  CB  . LEU   T  6  102 ? 40.890  -185.783 54.919  1.00 88.66  ? 98  LEU   T CB  1 
ATOM   34664 C  CG  . LEU   T  6  102 ? 39.387  -185.559 55.104  1.00 89.57  ? 98  LEU   T CG  1 
ATOM   34665 C  CD1 . LEU   T  6  102 ? 38.948  -184.203 54.568  1.00 90.95  ? 98  LEU   T CD1 1 
ATOM   34666 C  CD2 . LEU   T  6  102 ? 38.587  -186.666 54.436  1.00 90.04  ? 98  LEU   T CD2 1 
ATOM   34667 N  N   . TYR   T  6  103 ? 42.085  -185.445 57.875  1.00 87.86  ? 99  TYR   T N   1 
ATOM   34668 C  CA  . TYR   T  6  103 ? 41.730  -185.557 59.317  1.00 89.87  ? 99  TYR   T CA  1 
ATOM   34669 C  C   . TYR   T  6  103 ? 42.854  -185.047 60.233  1.00 89.96  ? 99  TYR   T C   1 
ATOM   34670 O  O   . TYR   T  6  103 ? 42.624  -185.032 61.459  1.00 87.40  ? 99  TYR   T O   1 
ATOM   34671 C  CB  . TYR   T  6  103 ? 41.370  -187.005 59.660  1.00 90.32  ? 99  TYR   T CB  1 
ATOM   34672 C  CG  . TYR   T  6  103 ? 40.250  -187.584 58.834  1.00 91.01  ? 99  TYR   T CG  1 
ATOM   34673 C  CD1 . TYR   T  6  103 ? 39.023  -186.944 58.745  1.00 90.65  ? 99  TYR   T CD1 1 
ATOM   34674 C  CD2 . TYR   T  6  103 ? 40.408  -188.777 58.146  1.00 90.31  ? 99  TYR   T CD2 1 
ATOM   34675 C  CE1 . TYR   T  6  103 ? 37.987  -187.469 57.989  1.00 90.86  ? 99  TYR   T CE1 1 
ATOM   34676 C  CE2 . TYR   T  6  103 ? 39.382  -189.317 57.387  1.00 89.53  ? 99  TYR   T CE2 1 
ATOM   34677 C  CZ  . TYR   T  6  103 ? 38.166  -188.660 57.309  1.00 89.14  ? 99  TYR   T CZ  1 
ATOM   34678 O  OH  . TYR   T  6  103 ? 37.149  -189.174 56.560  1.00 89.13  ? 99  TYR   T OH  1 
ATOM   34679 N  N   . LYS   T  6  104 ? 44.013  -184.662 59.682  1.00 93.58  ? 100 LYS   T N   1 
ATOM   34680 C  CA  . LYS   T  6  104 ? 45.151  -184.022 60.411  1.00 98.65  ? 100 LYS   T CA  1 
ATOM   34681 C  C   . LYS   T  6  104 ? 45.923  -185.061 61.238  1.00 97.87  ? 100 LYS   T C   1 
ATOM   34682 O  O   . LYS   T  6  104 ? 47.156  -185.136 61.072  1.00 98.21  ? 100 LYS   T O   1 
ATOM   34683 C  CB  . LYS   T  6  104 ? 44.670  -182.880 61.314  1.00 100.86 ? 100 LYS   T CB  1 
ATOM   34684 C  CG  . LYS   T  6  104 ? 45.776  -182.023 61.921  1.00 103.14 ? 100 LYS   T CG  1 
ATOM   34685 C  CD  . LYS   T  6  104 ? 46.514  -181.172 60.908  1.00 107.33 ? 100 LYS   T CD  1 
ATOM   34686 C  CE  . LYS   T  6  104 ? 47.369  -180.093 61.543  1.00 108.91 ? 100 LYS   T CE  1 
ATOM   34687 N  NZ  . LYS   T  6  104 ? 48.570  -180.657 62.202  1.00 110.73 ? 100 LYS   T NZ  1 
ATOM   34688 N  N   . THR   T  6  105 ? 45.240  -185.794 62.124  1.00 100.16 ? 101 THR   T N   1 
ATOM   34689 C  CA  . THR   T  6  105 ? 45.835  -186.838 63.008  1.00 102.37 ? 101 THR   T CA  1 
ATOM   34690 C  C   . THR   T  6  105 ? 46.417  -187.975 62.164  1.00 104.13 ? 101 THR   T C   1 
ATOM   34691 O  O   . THR   T  6  105 ? 45.832  -188.348 61.149  1.00 101.65 ? 101 THR   T O   1 
ATOM   34692 C  CB  . THR   T  6  105 ? 44.816  -187.362 64.031  1.00 103.43 ? 101 THR   T CB  1 
ATOM   34693 O  OG1 . THR   T  6  105 ? 45.447  -188.400 64.781  1.00 105.85 ? 101 THR   T OG1 1 
ATOM   34694 C  CG2 . THR   T  6  105 ? 43.543  -187.907 63.419  1.00 102.47 ? 101 THR   T CG2 1 
ATOM   34695 N  N   . PRO   T  6  106 ? 47.586  -188.552 62.543  1.00 103.53 ? 102 PRO   T N   1 
ATOM   34696 C  CA  . PRO   T  6  106 ? 48.114  -189.748 61.882  1.00 101.87 ? 102 PRO   T CA  1 
ATOM   34697 C  C   . PRO   T  6  106 ? 47.139  -190.931 61.988  1.00 100.12 ? 102 PRO   T C   1 
ATOM   34698 O  O   . PRO   T  6  106 ? 46.464  -191.034 62.998  1.00 105.93 ? 102 PRO   T O   1 
ATOM   34699 C  CB  . PRO   T  6  106 ? 49.413  -190.064 62.641  1.00 102.40 ? 102 PRO   T CB  1 
ATOM   34700 C  CG  . PRO   T  6  106 ? 49.801  -188.749 63.277  1.00 103.62 ? 102 PRO   T CG  1 
ATOM   34701 C  CD  . PRO   T  6  106 ? 48.487  -188.070 63.603  1.00 104.83 ? 102 PRO   T CD  1 
ATOM   34702 N  N   . ILE   T  6  107 ? 47.095  -191.784 60.960  1.00 97.29  ? 103 ILE   T N   1 
ATOM   34703 C  CA  . ILE   T  6  107 ? 46.075  -192.868 60.819  1.00 93.77  ? 103 ILE   T CA  1 
ATOM   34704 C  C   . ILE   T  6  107 ? 46.202  -193.846 61.988  1.00 91.99  ? 103 ILE   T C   1 
ATOM   34705 O  O   . ILE   T  6  107 ? 47.285  -194.363 62.246  1.00 92.04  ? 103 ILE   T O   1 
ATOM   34706 C  CB  . ILE   T  6  107 ? 46.172  -193.573 59.448  1.00 92.87  ? 103 ILE   T CB  1 
ATOM   34707 C  CG1 . ILE   T  6  107 ? 45.024  -194.568 59.260  1.00 93.25  ? 103 ILE   T CG1 1 
ATOM   34708 C  CG2 . ILE   T  6  107 ? 47.529  -194.233 59.232  1.00 94.46  ? 103 ILE   T CG2 1 
ATOM   34709 C  CD1 . ILE   T  6  107 ? 44.709  -194.879 57.818  1.00 92.05  ? 103 ILE   T CD1 1 
ATOM   34710 N  N   . PRO   T  6  108 ? 45.111  -194.096 62.755  1.00 90.50  ? 104 PRO   T N   1 
ATOM   34711 C  CA  . PRO   T  6  108 ? 45.080  -195.179 63.742  1.00 91.15  ? 104 PRO   T CA  1 
ATOM   34712 C  C   . PRO   T  6  108 ? 45.320  -196.554 63.101  1.00 92.60  ? 104 PRO   T C   1 
ATOM   34713 O  O   . PRO   T  6  108 ? 44.977  -196.723 61.944  1.00 91.58  ? 104 PRO   T O   1 
ATOM   34714 C  CB  . PRO   T  6  108 ? 43.661  -195.108 64.327  1.00 89.44  ? 104 PRO   T CB  1 
ATOM   34715 C  CG  . PRO   T  6  108 ? 43.239  -193.679 64.089  1.00 89.16  ? 104 PRO   T CG  1 
ATOM   34716 C  CD  . PRO   T  6  108 ? 43.868  -193.310 62.762  1.00 89.77  ? 104 PRO   T CD  1 
ATOM   34717 N  N   . ILE   T  6  109 ? 45.874  -197.499 63.869  1.00 94.28  ? 105 ILE   T N   1 
ATOM   34718 C  CA  . ILE   T  6  109 ? 46.351  -198.824 63.361  1.00 93.83  ? 105 ILE   T CA  1 
ATOM   34719 C  C   . ILE   T  6  109 ? 45.159  -199.663 62.896  1.00 89.80  ? 105 ILE   T C   1 
ATOM   34720 O  O   . ILE   T  6  109 ? 45.239  -200.281 61.837  1.00 89.78  ? 105 ILE   T O   1 
ATOM   34721 C  CB  . ILE   T  6  109 ? 47.213  -199.580 64.395  1.00 94.86  ? 105 ILE   T CB  1 
ATOM   34722 C  CG1 . ILE   T  6  109 ? 48.218  -198.678 65.121  1.00 97.81  ? 105 ILE   T CG1 1 
ATOM   34723 C  CG2 . ILE   T  6  109 ? 47.909  -200.753 63.726  1.00 96.27  ? 105 ILE   T CG2 1 
ATOM   34724 C  CD1 . ILE   T  6  109 ? 49.186  -197.956 64.206  1.00 98.45  ? 105 ILE   T CD1 1 
ATOM   34725 N  N   . PRO   T  6  110 ? 44.031  -199.735 63.646  1.00 90.06  ? 106 PRO   T N   1 
ATOM   34726 C  CA  . PRO   T  6  110 ? 42.836  -200.438 63.170  1.00 88.56  ? 106 PRO   T CA  1 
ATOM   34727 C  C   . PRO   T  6  110 ? 42.281  -199.867 61.855  1.00 87.16  ? 106 PRO   T C   1 
ATOM   34728 O  O   . PRO   T  6  110 ? 41.911  -200.646 60.998  1.00 84.03  ? 106 PRO   T O   1 
ATOM   34729 C  CB  . PRO   T  6  110 ? 41.812  -200.248 64.300  1.00 88.24  ? 106 PRO   T CB  1 
ATOM   34730 C  CG  . PRO   T  6  110 ? 42.655  -199.964 65.523  1.00 89.82  ? 106 PRO   T CG  1 
ATOM   34731 C  CD  . PRO   T  6  110 ? 43.836  -199.177 64.994  1.00 91.39  ? 106 PRO   T CD  1 
ATOM   34732 N  N   . ALA   T  6  111 ? 42.225  -198.535 61.737  1.00 86.65  ? 107 ALA   T N   1 
ATOM   34733 C  CA  . ALA   T  6  111 ? 41.826  -197.808 60.508  1.00 87.22  ? 107 ALA   T CA  1 
ATOM   34734 C  C   . ALA   T  6  111 ? 42.751  -198.212 59.355  1.00 83.98  ? 107 ALA   T C   1 
ATOM   34735 O  O   . ALA   T  6  111 ? 42.234  -198.529 58.268  1.00 82.90  ? 107 ALA   T O   1 
ATOM   34736 C  CB  . ALA   T  6  111 ? 41.867  -196.317 60.741  1.00 87.47  ? 107 ALA   T CB  1 
ATOM   34737 N  N   . PHE   T  6  112 ? 44.068  -198.196 59.594  1.00 85.06  ? 108 PHE   T N   1 
ATOM   34738 C  CA  . PHE   T  6  112 ? 45.113  -198.549 58.597  1.00 86.94  ? 108 PHE   T CA  1 
ATOM   34739 C  C   . PHE   T  6  112 ? 44.977  -200.023 58.204  1.00 89.35  ? 108 PHE   T C   1 
ATOM   34740 O  O   . PHE   T  6  112 ? 45.159  -200.337 57.011  1.00 90.19  ? 108 PHE   T O   1 
ATOM   34741 C  CB  . PHE   T  6  112 ? 46.521  -198.278 59.132  1.00 87.74  ? 108 PHE   T CB  1 
ATOM   34742 C  CG  . PHE   T  6  112 ? 47.613  -198.766 58.216  1.00 87.67  ? 108 PHE   T CG  1 
ATOM   34743 C  CD1 . PHE   T  6  112 ? 47.850  -198.133 57.007  1.00 86.33  ? 108 PHE   T CD1 1 
ATOM   34744 C  CD2 . PHE   T  6  112 ? 48.377  -199.877 58.542  1.00 87.94  ? 108 PHE   T CD2 1 
ATOM   34745 C  CE1 . PHE   T  6  112 ? 48.841  -198.588 56.152  1.00 86.97  ? 108 PHE   T CE1 1 
ATOM   34746 C  CE2 . PHE   T  6  112 ? 49.372  -200.327 57.687  1.00 88.33  ? 108 PHE   T CE2 1 
ATOM   34747 C  CZ  . PHE   T  6  112 ? 49.601  -199.681 56.493  1.00 88.60  ? 108 PHE   T CZ  1 
ATOM   34748 N  N   . ALA   T  6  113 ? 44.680  -200.893 59.176  1.00 92.25  ? 109 ALA   T N   1 
ATOM   34749 C  CA  . ALA   T  6  113 ? 44.526  -202.352 58.972  1.00 93.19  ? 109 ALA   T CA  1 
ATOM   34750 C  C   . ALA   T  6  113 ? 43.411  -202.606 57.950  1.00 93.71  ? 109 ALA   T C   1 
ATOM   34751 O  O   . ALA   T  6  113 ? 43.642  -203.407 57.021  1.00 94.56  ? 109 ALA   T O   1 
ATOM   34752 C  CB  . ALA   T  6  113 ? 44.258  -203.054 60.283  1.00 94.32  ? 109 ALA   T CB  1 
ATOM   34753 N  N   . ASP   T  6  114 ? 42.266  -201.928 58.092  1.00 92.12  ? 110 ASP   T N   1 
ATOM   34754 C  CA  . ASP   T  6  114 ? 41.087  -202.123 57.207  1.00 92.14  ? 110 ASP   T CA  1 
ATOM   34755 C  C   . ASP   T  6  114 ? 41.391  -201.552 55.816  1.00 90.21  ? 110 ASP   T C   1 
ATOM   34756 O  O   . ASP   T  6  114 ? 40.877  -202.116 54.840  1.00 88.15  ? 110 ASP   T O   1 
ATOM   34757 C  CB  . ASP   T  6  114 ? 39.806  -201.517 57.786  1.00 94.04  ? 110 ASP   T CB  1 
ATOM   34758 C  CG  . ASP   T  6  114 ? 38.542  -202.092 57.162  1.00 96.73  ? 110 ASP   T CG  1 
ATOM   34759 O  OD1 . ASP   T  6  114 ? 38.441  -203.336 57.064  1.00 94.93  ? 110 ASP   T OD1 1 
ATOM   34760 O  OD2 . ASP   T  6  114 ? 37.672  -201.294 56.760  1.00 102.42 ? 110 ASP   T OD2 1 
ATOM   34761 N  N   . ARG   T  6  115 ? 42.194  -200.486 55.729  1.00 92.83  ? 111 ARG   T N   1 
ATOM   34762 C  CA  . ARG   T  6  115 ? 42.610  -199.875 54.436  1.00 95.51  ? 111 ARG   T CA  1 
ATOM   34763 C  C   . ARG   T  6  115 ? 43.371  -200.909 53.602  1.00 92.85  ? 111 ARG   T C   1 
ATOM   34764 O  O   . ARG   T  6  115 ? 43.060  -201.024 52.406  1.00 99.49  ? 111 ARG   T O   1 
ATOM   34765 C  CB  . ARG   T  6  115 ? 43.491  -198.639 54.639  1.00 97.37  ? 111 ARG   T CB  1 
ATOM   34766 C  CG  . ARG   T  6  115 ? 42.770  -197.436 55.227  1.00 98.48  ? 111 ARG   T CG  1 
ATOM   34767 C  CD  . ARG   T  6  115 ? 41.634  -196.928 54.362  1.00 100.89 ? 111 ARG   T CD  1 
ATOM   34768 N  NE  . ARG   T  6  115 ? 40.959  -195.793 54.983  1.00 104.13 ? 111 ARG   T NE  1 
ATOM   34769 C  CZ  . ARG   T  6  115 ? 41.214  -194.504 54.744  1.00 107.32 ? 111 ARG   T CZ  1 
ATOM   34770 N  NH1 . ARG   T  6  115 ? 42.142  -194.140 53.872  1.00 111.37 ? 111 ARG   T NH1 1 
ATOM   34771 N  NH2 . ARG   T  6  115 ? 40.525  -193.571 55.383  1.00 103.83 ? 111 ARG   T NH2 1 
ATOM   34772 N  N   . LEU   T  6  116 ? 44.337  -201.613 54.201  1.00 94.46  ? 112 LEU   T N   1 
ATOM   34773 C  CA  . LEU   T  6  116 ? 45.062  -202.736 53.544  1.00 95.08  ? 112 LEU   T CA  1 
ATOM   34774 C  C   . LEU   T  6  116 ? 44.072  -203.875 53.279  1.00 93.23  ? 112 LEU   T C   1 
ATOM   34775 O  O   . LEU   T  6  116 ? 44.109  -204.429 52.167  1.00 95.67  ? 112 LEU   T O   1 
ATOM   34776 C  CB  . LEU   T  6  116 ? 46.216  -203.224 54.428  1.00 95.78  ? 112 LEU   T CB  1 
ATOM   34777 C  CG  . LEU   T  6  116 ? 47.374  -202.251 54.652  1.00 97.75  ? 112 LEU   T CG  1 
ATOM   34778 C  CD1 . LEU   T  6  116 ? 48.501  -202.940 55.405  1.00 98.26  ? 112 LEU   T CD1 1 
ATOM   34779 C  CD2 . LEU   T  6  116 ? 47.896  -201.681 53.341  1.00 99.89  ? 112 LEU   T CD2 1 
ATOM   34780 N  N   . GLY   T  6  117 ? 43.221  -204.192 54.263  1.00 91.70  ? 113 GLY   T N   1 
ATOM   34781 C  CA  . GLY   T  6  117 ? 42.259  -205.313 54.221  1.00 92.75  ? 113 GLY   T CA  1 
ATOM   34782 C  C   . GLY   T  6  117 ? 41.284  -205.205 53.059  1.00 91.13  ? 113 GLY   T C   1 
ATOM   34783 O  O   . GLY   T  6  117 ? 41.113  -206.207 52.337  1.00 93.59  ? 113 GLY   T O   1 
ATOM   34784 N  N   . GLN   T  6  118 ? 40.665  -204.034 52.887  1.00 87.31  ? 114 GLN   T N   1 
ATOM   34785 C  CA  . GLN   T  6  118 ? 39.692  -203.749 51.798  1.00 82.40  ? 114 GLN   T CA  1 
ATOM   34786 C  C   . GLN   T  6  118 ? 40.399  -203.825 50.441  1.00 80.14  ? 114 GLN   T C   1 
ATOM   34787 O  O   . GLN   T  6  118 ? 39.774  -204.319 49.483  1.00 79.04  ? 114 GLN   T O   1 
ATOM   34788 C  CB  . GLN   T  6  118 ? 39.066  -202.367 51.979  1.00 81.11  ? 114 GLN   T CB  1 
ATOM   34789 C  CG  . GLN   T  6  118 ? 38.212  -202.228 53.232  1.00 82.74  ? 114 GLN   T CG  1 
ATOM   34790 C  CD  . GLN   T  6  118 ? 36.898  -202.960 53.137  1.00 83.58  ? 114 GLN   T CD  1 
ATOM   34791 O  OE1 . GLN   T  6  118 ? 36.481  -203.392 52.065  1.00 85.18  ? 114 GLN   T OE1 1 
ATOM   34792 N  NE2 . GLN   T  6  118 ? 36.235  -203.104 54.274  1.00 85.77  ? 114 GLN   T NE2 1 
ATOM   34793 N  N   . TYR   T  6  119 ? 41.644  -203.346 50.364  1.00 79.94  ? 115 TYR   T N   1 
ATOM   34794 C  CA  . TYR   T  6  119 ? 42.463  -203.306 49.122  1.00 85.53  ? 115 TYR   T CA  1 
ATOM   34795 C  C   . TYR   T  6  119 ? 42.779  -204.735 48.667  1.00 87.66  ? 115 TYR   T C   1 
ATOM   34796 O  O   . TYR   T  6  119 ? 42.560  -205.049 47.481  1.00 91.34  ? 115 TYR   T O   1 
ATOM   34797 C  CB  . TYR   T  6  119 ? 43.749  -202.502 49.335  1.00 85.60  ? 115 TYR   T CB  1 
ATOM   34798 C  CG  . TYR   T  6  119 ? 44.525  -202.220 48.072  1.00 84.12  ? 115 TYR   T CG  1 
ATOM   34799 C  CD1 . TYR   T  6  119 ? 44.024  -201.362 47.107  1.00 83.17  ? 115 TYR   T CD1 1 
ATOM   34800 C  CD2 . TYR   T  6  119 ? 45.761  -202.803 47.843  1.00 84.46  ? 115 TYR   T CD2 1 
ATOM   34801 C  CE1 . TYR   T  6  119 ? 44.728  -201.095 45.945  1.00 83.48  ? 115 TYR   T CE1 1 
ATOM   34802 C  CE2 . TYR   T  6  119 ? 46.480  -202.543 46.688  1.00 84.17  ? 115 TYR   T CE2 1 
ATOM   34803 C  CZ  . TYR   T  6  119 ? 45.961  -201.686 45.733  1.00 84.32  ? 115 TYR   T CZ  1 
ATOM   34804 O  OH  . TYR   T  6  119 ? 46.660  -201.426 44.591  1.00 85.34  ? 115 TYR   T OH  1 
ATOM   34805 N  N   . VAL   T  6  120 ? 43.276  -205.571 49.584  1.00 89.36  ? 116 VAL   T N   1 
ATOM   34806 C  CA  . VAL   T  6  120 ? 43.636  -206.995 49.314  1.00 89.73  ? 116 VAL   T CA  1 
ATOM   34807 C  C   . VAL   T  6  120 ? 42.355  -207.768 48.972  1.00 89.85  ? 116 VAL   T C   1 
ATOM   34808 O  O   . VAL   T  6  120 ? 42.395  -208.560 48.012  1.00 93.70  ? 116 VAL   T O   1 
ATOM   34809 C  CB  . VAL   T  6  120 ? 44.401  -207.622 50.497  1.00 90.82  ? 116 VAL   T CB  1 
ATOM   34810 C  CG1 . VAL   T  6  120 ? 44.516  -209.136 50.374  1.00 92.07  ? 116 VAL   T CG1 1 
ATOM   34811 C  CG2 . VAL   T  6  120 ? 45.780  -206.999 50.652  1.00 88.94  ? 116 VAL   T CG2 1 
ATOM   34812 N  N   . GLN   T  6  121 ? 41.267  -207.535 49.716  1.00 88.48  ? 117 GLN   T N   1 
ATOM   34813 C  CA  . GLN   T  6  121 ? 39.942  -208.177 49.491  1.00 87.45  ? 117 GLN   T CA  1 
ATOM   34814 C  C   . GLN   T  6  121 ? 39.458  -207.851 48.075  1.00 85.21  ? 117 GLN   T C   1 
ATOM   34815 O  O   . GLN   T  6  121 ? 38.832  -208.726 47.451  1.00 81.61  ? 117 GLN   T O   1 
ATOM   34816 C  CB  . GLN   T  6  121 ? 38.923  -207.715 50.536  1.00 88.67  ? 117 GLN   T CB  1 
ATOM   34817 C  CG  . GLN   T  6  121 ? 37.617  -208.504 50.518  1.00 91.09  ? 117 GLN   T CG  1 
ATOM   34818 C  CD  . GLN   T  6  121 ? 36.588  -208.070 49.499  1.00 91.66  ? 117 GLN   T CD  1 
ATOM   34819 O  OE1 . GLN   T  6  121 ? 35.763  -208.868 49.059  1.00 90.53  ? 117 GLN   T OE1 1 
ATOM   34820 N  NE2 . GLN   T  6  121 ? 36.594  -206.799 49.127  1.00 94.71  ? 117 GLN   T NE2 1 
ATOM   34821 N  N   . ALA   T  6  122 ? 39.743  -206.637 47.594  1.00 85.61  ? 118 ALA   T N   1 
ATOM   34822 C  CA  . ALA   T  6  122 ? 39.323  -206.134 46.265  1.00 84.90  ? 118 ALA   T CA  1 
ATOM   34823 C  C   . ALA   T  6  122 ? 39.994  -206.946 45.152  1.00 86.39  ? 118 ALA   T C   1 
ATOM   34824 O  O   . ALA   T  6  122 ? 39.413  -207.016 44.052  1.00 84.36  ? 118 ALA   T O   1 
ATOM   34825 C  CB  . ALA   T  6  122 ? 39.643  -204.668 46.138  1.00 84.80  ? 118 ALA   T CB  1 
ATOM   34826 N  N   . HIS   T  6  123 ? 41.163  -207.536 45.429  1.00 88.19  ? 119 HIS   T N   1 
ATOM   34827 C  CA  . HIS   T  6  123 ? 41.939  -208.374 44.474  1.00 89.96  ? 119 HIS   T CA  1 
ATOM   34828 C  C   . HIS   T  6  123 ? 41.471  -209.837 44.509  1.00 90.54  ? 119 HIS   T C   1 
ATOM   34829 O  O   . HIS   T  6  123 ? 42.174  -210.684 43.922  1.00 90.59  ? 119 HIS   T O   1 
ATOM   34830 C  CB  . HIS   T  6  123 ? 43.441  -208.244 44.755  1.00 91.72  ? 119 HIS   T CB  1 
ATOM   34831 C  CG  . HIS   T  6  123 ? 44.014  -206.949 44.293  1.00 89.51  ? 119 HIS   T CG  1 
ATOM   34832 N  ND1 . HIS   T  6  123 ? 43.778  -205.765 44.957  1.00 90.44  ? 119 HIS   T ND1 1 
ATOM   34833 C  CD2 . HIS   T  6  123 ? 44.801  -206.648 43.239  1.00 90.45  ? 119 HIS   T CD2 1 
ATOM   34834 C  CE1 . HIS   T  6  123 ? 44.402  -204.787 44.335  1.00 89.79  ? 119 HIS   T CE1 1 
ATOM   34835 N  NE2 . HIS   T  6  123 ? 45.036  -205.302 43.277  1.00 89.83  ? 119 HIS   T NE2 1 
ATOM   34836 N  N   . THR   T  6  124 ? 40.343  -210.128 45.167  1.00 88.53  ? 120 THR   T N   1 
ATOM   34837 C  CA  . THR   T  6  124 ? 39.666  -211.453 45.134  1.00 90.34  ? 120 THR   T CA  1 
ATOM   34838 C  C   . THR   T  6  124 ? 38.302  -211.333 44.439  1.00 90.34  ? 120 THR   T C   1 
ATOM   34839 O  O   . THR   T  6  124 ? 37.619  -212.370 44.334  1.00 88.94  ? 120 THR   T O   1 
ATOM   34840 C  CB  . THR   T  6  124 ? 39.507  -212.042 46.544  1.00 89.70  ? 120 THR   T CB  1 
ATOM   34841 O  OG1 . THR   T  6  124 ? 38.498  -211.304 47.233  1.00 90.08  ? 120 THR   T OG1 1 
ATOM   34842 C  CG2 . THR   T  6  124 ? 40.785  -212.024 47.355  1.00 91.07  ? 120 THR   T CG2 1 
ATOM   34843 N  N   . LEU   T  6  125 ? 37.926  -210.135 43.968  1.00 91.44  ? 121 LEU   T N   1 
ATOM   34844 C  CA  . LEU   T  6  125 ? 36.563  -209.828 43.445  1.00 93.87  ? 121 LEU   T CA  1 
ATOM   34845 C  C   . LEU   T  6  125 ? 36.487  -210.014 41.923  1.00 92.04  ? 121 LEU   T C   1 
ATOM   34846 O  O   . LEU   T  6  125 ? 35.357  -210.169 41.423  1.00 95.99  ? 121 LEU   T O   1 
ATOM   34847 C  CB  . LEU   T  6  125 ? 36.182  -208.384 43.791  1.00 96.54  ? 121 LEU   T CB  1 
ATOM   34848 C  CG  . LEU   T  6  125 ? 35.863  -208.083 45.255  1.00 99.71  ? 121 LEU   T CG  1 
ATOM   34849 C  CD1 . LEU   T  6  125 ? 35.622  -206.593 45.434  1.00 99.49  ? 121 LEU   T CD1 1 
ATOM   34850 C  CD2 . LEU   T  6  125 ? 34.654  -208.875 45.740  1.00 101.14 ? 121 LEU   T CD2 1 
ATOM   34851 N  N   . TYR   T  6  126 ? 37.618  -209.950 41.211  1.00 91.67  ? 122 TYR   T N   1 
ATOM   34852 C  CA  . TYR   T  6  126 ? 37.672  -209.941 39.723  1.00 93.08  ? 122 TYR   T CA  1 
ATOM   34853 C  C   . TYR   T  6  126 ? 38.652  -210.999 39.210  1.00 95.09  ? 122 TYR   T C   1 
ATOM   34854 O  O   . TYR   T  6  126 ? 39.643  -211.297 39.906  1.00 98.70  ? 122 TYR   T O   1 
ATOM   34855 C  CB  . TYR   T  6  126 ? 38.081  -208.558 39.214  1.00 91.72  ? 122 TYR   T CB  1 
ATOM   34856 C  CG  . TYR   T  6  126 ? 37.427  -207.411 39.941  1.00 92.72  ? 122 TYR   T CG  1 
ATOM   34857 C  CD1 . TYR   T  6  126 ? 36.165  -206.966 39.585  1.00 91.87  ? 122 TYR   T CD1 1 
ATOM   34858 C  CD2 . TYR   T  6  126 ? 38.064  -206.783 40.999  1.00 90.73  ? 122 TYR   T CD2 1 
ATOM   34859 C  CE1 . TYR   T  6  126 ? 35.556  -205.917 40.253  1.00 90.81  ? 122 TYR   T CE1 1 
ATOM   34860 C  CE2 . TYR   T  6  126 ? 37.467  -205.736 41.681  1.00 89.45  ? 122 TYR   T CE2 1 
ATOM   34861 C  CZ  . TYR   T  6  126 ? 36.207  -205.304 41.308  1.00 89.72  ? 122 TYR   T CZ  1 
ATOM   34862 O  OH  . TYR   T  6  126 ? 35.609  -204.275 41.973  1.00 94.97  ? 122 TYR   T OH  1 
ATOM   34863 N  N   . ASN   T  6  127 ? 38.386  -211.525 38.009  1.00 94.76  ? 123 ASN   T N   1 
ATOM   34864 C  CA  . ASN   T  6  127 ? 39.242  -212.525 37.312  1.00 99.01  ? 123 ASN   T CA  1 
ATOM   34865 C  C   . ASN   T  6  127 ? 40.354  -211.828 36.513  1.00 98.95  ? 123 ASN   T C   1 
ATOM   34866 O  O   . ASN   T  6  127 ? 41.169  -212.544 35.902  1.00 99.76  ? 123 ASN   T O   1 
ATOM   34867 C  CB  . ASN   T  6  127 ? 38.424  -213.481 36.431  1.00 102.07 ? 123 ASN   T CB  1 
ATOM   34868 C  CG  . ASN   T  6  127 ? 37.694  -212.855 35.255  1.00 102.98 ? 123 ASN   T CG  1 
ATOM   34869 O  OD1 . ASN   T  6  127 ? 36.989  -213.560 34.537  1.00 107.70 ? 123 ASN   T OD1 1 
ATOM   34870 N  ND2 . ASN   T  6  127 ? 37.836  -211.558 35.023  1.00 105.81 ? 123 ASN   T ND2 1 
ATOM   34871 N  N   . SER   T  6  128 ? 40.391  -210.492 36.513  1.00 98.49  ? 124 SER   T N   1 
ATOM   34872 C  CA  . SER   T  6  128 ? 41.358  -209.672 35.736  1.00 100.52 ? 124 SER   T CA  1 
ATOM   34873 C  C   . SER   T  6  128 ? 42.533  -209.230 36.618  1.00 97.50  ? 124 SER   T C   1 
ATOM   34874 O  O   . SER   T  6  128 ? 43.470  -208.619 36.074  1.00 96.57  ? 124 SER   T O   1 
ATOM   34875 C  CB  . SER   T  6  128 ? 40.675  -208.491 35.106  1.00 100.84 ? 124 SER   T CB  1 
ATOM   34876 O  OG  . SER   T  6  128 ? 39.997  -207.724 36.088  1.00 103.75 ? 124 SER   T OG  1 
ATOM   34877 N  N   . VAL   T  6  129 ? 42.494  -209.530 37.921  1.00 99.29  ? 125 VAL   T N   1 
ATOM   34878 C  CA  . VAL   T  6  129 ? 43.631  -209.298 38.861  1.00 99.56  ? 125 VAL   T CA  1 
ATOM   34879 C  C   . VAL   T  6  129 ? 43.974  -210.605 39.582  1.00 97.50  ? 125 VAL   T C   1 
ATOM   34880 O  O   . VAL   T  6  129 ? 43.096  -211.492 39.686  1.00 92.78  ? 125 VAL   T O   1 
ATOM   34881 C  CB  . VAL   T  6  129 ? 43.344  -208.178 39.877  1.00 101.56 ? 125 VAL   T CB  1 
ATOM   34882 C  CG1 . VAL   T  6  129 ? 43.417  -206.806 39.230  1.00 103.67 ? 125 VAL   T CG1 1 
ATOM   34883 C  CG2 . VAL   T  6  129 ? 42.019  -208.373 40.599  1.00 100.80 ? 125 VAL   T CG2 1 
ATOM   34884 N  N   . ARG   T  6  130 ? 45.220  -210.692 40.053  1.00 98.02  ? 126 ARG   T N   1 
ATOM   34885 C  CA  . ARG   T  6  130 ? 45.784  -211.831 40.820  1.00 97.14  ? 126 ARG   T CA  1 
ATOM   34886 C  C   . ARG   T  6  130 ? 45.735  -211.474 42.302  1.00 94.74  ? 126 ARG   T C   1 
ATOM   34887 O  O   . ARG   T  6  130 ? 46.016  -210.336 42.670  1.00 96.24  ? 126 ARG   T O   1 
ATOM   34888 C  CB  . ARG   T  6  130 ? 47.217  -212.098 40.350  1.00 96.24  ? 126 ARG   T CB  1 
ATOM   34889 C  CG  . ARG   T  6  130 ? 47.964  -213.152 41.152  1.00 98.65  ? 126 ARG   T CG  1 
ATOM   34890 C  CD  . ARG   T  6  130 ? 49.358  -213.377 40.604  1.00 99.64  ? 126 ARG   T CD  1 
ATOM   34891 N  NE  . ARG   T  6  130 ? 50.170  -212.165 40.556  1.00 98.91  ? 126 ARG   T NE  1 
ATOM   34892 C  CZ  . ARG   T  6  130 ? 50.836  -211.642 41.586  1.00 99.29  ? 126 ARG   T CZ  1 
ATOM   34893 N  NH1 . ARG   T  6  130 ? 50.791  -212.212 42.779  1.00 100.48 ? 126 ARG   T NH1 1 
ATOM   34894 N  NH2 . ARG   T  6  130 ? 51.544  -210.539 41.419  1.00 98.07  ? 126 ARG   T NH2 1 
ATOM   34895 N  N   . PRO   T  6  131 ? 45.366  -212.413 43.200  1.00 93.96  ? 127 PRO   T N   1 
ATOM   34896 C  CA  . PRO   T  6  131 ? 45.488  -212.175 44.638  1.00 93.81  ? 127 PRO   T CA  1 
ATOM   34897 C  C   . PRO   T  6  131 ? 46.934  -211.832 45.025  1.00 92.09  ? 127 PRO   T C   1 
ATOM   34898 O  O   . PRO   T  6  131 ? 47.832  -212.118 44.258  1.00 91.13  ? 127 PRO   T O   1 
ATOM   34899 C  CB  . PRO   T  6  131 ? 45.048  -213.510 45.261  1.00 94.50  ? 127 PRO   T CB  1 
ATOM   34900 C  CG  . PRO   T  6  131 ? 44.159  -214.134 44.208  1.00 94.67  ? 127 PRO   T CG  1 
ATOM   34901 C  CD  . PRO   T  6  131 ? 44.790  -213.731 42.892  1.00 94.80  ? 127 PRO   T CD  1 
ATOM   34902 N  N   . PHE   T  6  132 ? 47.129  -211.224 46.194  1.00 92.84  ? 128 PHE   T N   1 
ATOM   34903 C  CA  . PHE   T  6  132 ? 48.474  -210.905 46.736  1.00 96.65  ? 128 PHE   T CA  1 
ATOM   34904 C  C   . PHE   T  6  132 ? 49.149  -212.199 47.202  1.00 98.66  ? 128 PHE   T C   1 
ATOM   34905 O  O   . PHE   T  6  132 ? 48.505  -212.996 47.917  1.00 97.91  ? 128 PHE   T O   1 
ATOM   34906 C  CB  . PHE   T  6  132 ? 48.375  -209.857 47.845  1.00 98.50  ? 128 PHE   T CB  1 
ATOM   34907 C  CG  . PHE   T  6  132 ? 48.157  -208.464 47.316  1.00 100.14 ? 128 PHE   T CG  1 
ATOM   34908 C  CD1 . PHE   T  6  132 ? 46.877  -207.972 47.116  1.00 102.26 ? 128 PHE   T CD1 1 
ATOM   34909 C  CD2 . PHE   T  6  132 ? 49.236  -207.663 46.973  1.00 101.49 ? 128 PHE   T CD2 1 
ATOM   34910 C  CE1 . PHE   T  6  132 ? 46.679  -206.698 46.607  1.00 99.86  ? 128 PHE   T CE1 1 
ATOM   34911 C  CE2 . PHE   T  6  132 ? 49.036  -206.390 46.461  1.00 100.10 ? 128 PHE   T CE2 1 
ATOM   34912 C  CZ  . PHE   T  6  132 ? 47.759  -205.910 46.279  1.00 99.16  ? 128 PHE   T CZ  1 
ATOM   34913 N  N   . GLY   T  6  133 ? 50.407  -212.398 46.792  1.00 99.80  ? 129 GLY   T N   1 
ATOM   34914 C  CA  . GLY   T  6  133 ? 51.248  -213.540 47.198  1.00 100.74 ? 129 GLY   T CA  1 
ATOM   34915 C  C   . GLY   T  6  133 ? 52.060  -213.220 48.441  1.00 99.99  ? 129 GLY   T C   1 
ATOM   34916 O  O   . GLY   T  6  133 ? 53.270  -213.530 48.449  1.00 96.45  ? 129 GLY   T O   1 
ATOM   34917 N  N   . VAL   T  6  134 ? 51.423  -212.618 49.452  1.00 98.70  ? 130 VAL   T N   1 
ATOM   34918 C  CA  . VAL   T  6  134 ? 52.063  -212.252 50.751  1.00 101.67 ? 130 VAL   T CA  1 
ATOM   34919 C  C   . VAL   T  6  134 ? 51.027  -212.327 51.876  1.00 101.08 ? 130 VAL   T C   1 
ATOM   34920 O  O   . VAL   T  6  134 ? 49.856  -211.965 51.641  1.00 100.89 ? 130 VAL   T O   1 
ATOM   34921 C  CB  . VAL   T  6  134 ? 52.710  -210.853 50.708  1.00 101.97 ? 130 VAL   T CB  1 
ATOM   34922 C  CG1 . VAL   T  6  134 ? 54.075  -210.879 50.041  1.00 105.46 ? 130 VAL   T CG1 1 
ATOM   34923 C  CG2 . VAL   T  6  134 ? 51.809  -209.818 50.052  1.00 102.06 ? 130 VAL   T CG2 1 
ATOM   34924 N  N   . SER   T  6  135 ? 51.467  -212.801 53.045  1.00 103.25 ? 131 SER   T N   1 
ATOM   34925 C  CA  . SER   T  6  135 ? 50.877  -212.500 54.374  1.00 107.93 ? 131 SER   T CA  1 
ATOM   34926 C  C   . SER   T  6  135 ? 51.715  -211.381 54.994  1.00 106.20 ? 131 SER   T C   1 
ATOM   34927 O  O   . SER   T  6  135 ? 52.954  -211.522 54.996  1.00 113.95 ? 131 SER   T O   1 
ATOM   34928 C  CB  . SER   T  6  135 ? 50.837  -213.713 55.270  1.00 109.12 ? 131 SER   T CB  1 
ATOM   34929 O  OG  . SER   T  6  135 ? 49.822  -214.619 54.867  1.00 114.46 ? 131 SER   T OG  1 
ATOM   34930 N  N   . THR   T  6  136 ? 51.077  -210.308 55.468  1.00 105.87 ? 132 THR   T N   1 
ATOM   34931 C  CA  . THR   T  6  136 ? 51.762  -209.104 56.008  1.00 104.25 ? 132 THR   T CA  1 
ATOM   34932 C  C   . THR   T  6  136 ? 51.470  -208.969 57.505  1.00 99.37  ? 132 THR   T C   1 
ATOM   34933 O  O   . THR   T  6  136 ? 50.284  -208.872 57.870  1.00 98.41  ? 132 THR   T O   1 
ATOM   34934 C  CB  . THR   T  6  136 ? 51.346  -207.832 55.260  1.00 104.55 ? 132 THR   T CB  1 
ATOM   34935 O  OG1 . THR   T  6  136 ? 51.472  -208.064 53.856  1.00 105.91 ? 132 THR   T OG1 1 
ATOM   34936 C  CG2 . THR   T  6  136 ? 52.173  -206.634 55.673  1.00 106.52 ? 132 THR   T CG2 1 
ATOM   34937 N  N   . ILE   T  6  137 ? 52.524  -208.967 58.325  1.00 100.27 ? 133 ILE   T N   1 
ATOM   34938 C  CA  . ILE   T  6  137 ? 52.476  -208.627 59.777  1.00 102.16 ? 133 ILE   T CA  1 
ATOM   34939 C  C   . ILE   T  6  137 ? 52.874  -207.156 59.918  1.00 97.86  ? 133 ILE   T C   1 
ATOM   34940 O  O   . ILE   T  6  137 ? 53.960  -206.791 59.434  1.00 97.75  ? 133 ILE   T O   1 
ATOM   34941 C  CB  . ILE   T  6  137 ? 53.397  -209.549 60.598  1.00 105.70 ? 133 ILE   T CB  1 
ATOM   34942 C  CG1 . ILE   T  6  137 ? 52.971  -211.017 60.493  1.00 108.98 ? 133 ILE   T CG1 1 
ATOM   34943 C  CG2 . ILE   T  6  137 ? 53.465  -209.084 62.046  1.00 107.70 ? 133 ILE   T CG2 1 
ATOM   34944 C  CD1 . ILE   T  6  137 ? 54.061  -212.002 60.856  1.00 111.61 ? 133 ILE   T CD1 1 
ATOM   34945 N  N   . PHE   T  6  138 ? 52.027  -206.352 60.560  1.00 95.71  ? 134 PHE   T N   1 
ATOM   34946 C  CA  . PHE   T  6  138 ? 52.195  -204.881 60.671  1.00 96.48  ? 134 PHE   T CA  1 
ATOM   34947 C  C   . PHE   T  6  138 ? 51.464  -204.363 61.909  1.00 95.56  ? 134 PHE   T C   1 
ATOM   34948 O  O   . PHE   T  6  138 ? 50.543  -205.038 62.405  1.00 98.47  ? 134 PHE   T O   1 
ATOM   34949 C  CB  . PHE   T  6  138 ? 51.650  -204.181 59.425  1.00 94.87  ? 134 PHE   T CB  1 
ATOM   34950 C  CG  . PHE   T  6  138 ? 50.159  -204.321 59.251  1.00 93.86  ? 134 PHE   T CG  1 
ATOM   34951 C  CD1 . PHE   T  6  138 ? 49.622  -205.427 58.613  1.00 94.03  ? 134 PHE   T CD1 1 
ATOM   34952 C  CD2 . PHE   T  6  138 ? 49.289  -203.363 59.748  1.00 93.69  ? 134 PHE   T CD2 1 
ATOM   34953 C  CE1 . PHE   T  6  138 ? 48.251  -205.564 58.463  1.00 92.43  ? 134 PHE   T CE1 1 
ATOM   34954 C  CE2 . PHE   T  6  138 ? 47.917  -203.503 59.599  1.00 91.22  ? 134 PHE   T CE2 1 
ATOM   34955 C  CZ  . PHE   T  6  138 ? 47.401  -204.602 58.955  1.00 90.14  ? 134 PHE   T CZ  1 
ATOM   34956 N  N   . GLY   T  6  139 ? 51.849  -203.169 62.357  1.00 96.27  ? 135 GLY   T N   1 
ATOM   34957 C  CA  . GLY   T  6  139 ? 51.299  -202.525 63.562  1.00 96.50  ? 135 GLY   T CA  1 
ATOM   34958 C  C   . GLY   T  6  139 ? 52.107  -201.309 63.972  1.00 95.69  ? 135 GLY   T C   1 
ATOM   34959 O  O   . GLY   T  6  139 ? 53.049  -200.937 63.244  1.00 92.68  ? 135 GLY   T O   1 
ATOM   34960 N  N   . GLY   T  6  140 ? 51.751  -200.716 65.109  1.00 95.21  ? 136 GLY   T N   1 
ATOM   34961 C  CA  . GLY   T  6  140 ? 52.394  -199.504 65.641  1.00 97.41  ? 136 GLY   T CA  1 
ATOM   34962 C  C   . GLY   T  6  140 ? 51.666  -199.001 66.869  1.00 101.02 ? 136 GLY   T C   1 
ATOM   34963 O  O   . GLY   T  6  140 ? 50.896  -199.788 67.457  1.00 104.84 ? 136 GLY   T O   1 
ATOM   34964 N  N   . VAL   T  6  141 ? 51.887  -197.733 67.225  1.00 103.17 ? 137 VAL   T N   1 
ATOM   34965 C  CA  . VAL   T  6  141 ? 51.289  -197.074 68.423  1.00 103.19 ? 137 VAL   T CA  1 
ATOM   34966 C  C   . VAL   T  6  141 ? 50.432  -195.893 67.963  1.00 101.59 ? 137 VAL   T C   1 
ATOM   34967 O  O   . VAL   T  6  141 ? 50.930  -195.069 67.172  1.00 100.33 ? 137 VAL   T O   1 
ATOM   34968 C  CB  . VAL   T  6  141 ? 52.377  -196.620 69.414  1.00 109.87 ? 137 VAL   T CB  1 
ATOM   34969 C  CG1 . VAL   T  6  141 ? 51.782  -195.887 70.608  1.00 113.01 ? 137 VAL   T CG1 1 
ATOM   34970 C  CG2 . VAL   T  6  141 ? 53.238  -197.789 69.872  1.00 109.89 ? 137 VAL   T CG2 1 
ATOM   34971 N  N   . ASP   T  6  142 ? 49.193  -195.823 68.453  1.00 96.82  ? 138 ASP   T N   1 
ATOM   34972 C  CA  . ASP   T  6  142 ? 48.269  -194.683 68.227  1.00 100.19 ? 138 ASP   T CA  1 
ATOM   34973 C  C   . ASP   T  6  142 ? 47.764  -194.202 69.593  1.00 99.16  ? 138 ASP   T C   1 
ATOM   34974 O  O   . ASP   T  6  142 ? 48.316  -194.643 70.619  1.00 96.24  ? 138 ASP   T O   1 
ATOM   34975 C  CB  . ASP   T  6  142 ? 47.163  -195.057 67.231  1.00 102.79 ? 138 ASP   T CB  1 
ATOM   34976 C  CG  . ASP   T  6  142 ? 46.140  -196.063 67.737  1.00 104.85 ? 138 ASP   T CG  1 
ATOM   34977 O  OD1 . ASP   T  6  142 ? 45.995  -196.188 68.971  1.00 110.47 ? 138 ASP   T OD1 1 
ATOM   34978 O  OD2 . ASP   T  6  142 ? 45.483  -196.707 66.888  1.00 108.15 ? 138 ASP   T OD2 1 
ATOM   34979 N  N   . LYS   T  6  143 ? 46.754  -193.325 69.582  1.00 106.03 ? 139 LYS   T N   1 
ATOM   34980 C  CA  . LYS   T  6  143 ? 46.151  -192.656 70.769  1.00 107.62 ? 139 LYS   T CA  1 
ATOM   34981 C  C   . LYS   T  6  143 ? 45.572  -193.699 71.743  1.00 104.20 ? 139 LYS   T C   1 
ATOM   34982 O  O   . LYS   T  6  143 ? 45.445  -193.364 72.936  1.00 104.85 ? 139 LYS   T O   1 
ATOM   34983 C  CB  . LYS   T  6  143 ? 45.137  -191.615 70.269  1.00 111.56 ? 139 LYS   T CB  1 
ATOM   34984 C  CG  . LYS   T  6  143 ? 44.029  -191.206 71.232  1.00 115.49 ? 139 LYS   T CG  1 
ATOM   34985 C  CD  . LYS   T  6  143 ? 42.665  -191.727 70.830  1.00 119.75 ? 139 LYS   T CD  1 
ATOM   34986 C  CE  . LYS   T  6  143 ? 42.047  -190.924 69.703  1.00 121.34 ? 139 LYS   T CE  1 
ATOM   34987 N  NZ  . LYS   T  6  143 ? 40.682  -191.398 69.375  1.00 124.56 ? 139 LYS   T NZ  1 
ATOM   34988 N  N   . ASN   T  6  144 ? 45.263  -194.916 71.278  1.00 101.45 ? 140 ASN   T N   1 
ATOM   34989 C  CA  . ASN   T  6  144 ? 44.663  -196.003 72.103  1.00 103.75 ? 140 ASN   T CA  1 
ATOM   34990 C  C   . ASN   T  6  144 ? 45.710  -197.068 72.468  1.00 103.26 ? 140 ASN   T C   1 
ATOM   34991 O  O   . ASN   T  6  144 ? 45.298  -198.157 72.908  1.00 103.84 ? 140 ASN   T O   1 
ATOM   34992 C  CB  . ASN   T  6  144 ? 43.471  -196.649 71.390  1.00 103.26 ? 140 ASN   T CB  1 
ATOM   34993 C  CG  . ASN   T  6  144 ? 42.290  -195.715 71.242  1.00 102.90 ? 140 ASN   T CG  1 
ATOM   34994 O  OD1 . ASN   T  6  144 ? 41.852  -195.431 70.129  1.00 105.10 ? 140 ASN   T OD1 1 
ATOM   34995 N  ND2 . ASN   T  6  144 ? 41.765  -195.234 72.356  1.00 104.20 ? 140 ASN   T ND2 1 
ATOM   34996 N  N   . GLY   T  6  145 ? 47.005  -196.770 72.319  1.00 106.12 ? 141 GLY   T N   1 
ATOM   34997 C  CA  . GLY   T  6  145 ? 48.109  -197.685 72.672  1.00 105.01 ? 141 GLY   T CA  1 
ATOM   34998 C  C   . GLY   T  6  145 ? 48.573  -198.508 71.481  1.00 106.01 ? 141 GLY   T C   1 
ATOM   34999 O  O   . GLY   T  6  145 ? 48.430  -198.029 70.340  1.00 106.02 ? 141 GLY   T O   1 
ATOM   35000 N  N   . ALA   T  6  146 ? 49.100  -199.709 71.739  1.00 105.02 ? 142 ALA   T N   1 
ATOM   35001 C  CA  . ALA   T  6  146 ? 49.771  -200.583 70.747  1.00 105.57 ? 142 ALA   T CA  1 
ATOM   35002 C  C   . ALA   T  6  146 ? 48.757  -201.526 70.089  1.00 104.06 ? 142 ALA   T C   1 
ATOM   35003 O  O   . ALA   T  6  146 ? 47.815  -201.970 70.778  1.00 101.94 ? 142 ALA   T O   1 
ATOM   35004 C  CB  . ALA   T  6  146 ? 50.879  -201.358 71.414  1.00 107.20 ? 142 ALA   T CB  1 
ATOM   35005 N  N   . HIS   T  6  147 ? 48.959  -201.813 68.799  1.00 104.49 ? 143 HIS   T N   1 
ATOM   35006 C  CA  . HIS   T  6  147 ? 48.183  -202.800 68.003  1.00 104.44 ? 143 HIS   T CA  1 
ATOM   35007 C  C   . HIS   T  6  147 ? 49.129  -203.577 67.086  1.00 103.87 ? 143 HIS   T C   1 
ATOM   35008 O  O   . HIS   T  6  147 ? 49.981  -202.933 66.439  1.00 102.17 ? 143 HIS   T O   1 
ATOM   35009 C  CB  . HIS   T  6  147 ? 47.093  -202.109 67.177  1.00 102.31 ? 143 HIS   T CB  1 
ATOM   35010 C  CG  . HIS   T  6  147 ? 46.200  -201.221 67.973  1.00 104.20 ? 143 HIS   T CG  1 
ATOM   35011 N  ND1 . HIS   T  6  147 ? 46.568  -199.939 68.327  1.00 105.40 ? 143 HIS   T ND1 1 
ATOM   35012 C  CD2 . HIS   T  6  147 ? 44.962  -201.418 68.475  1.00 104.49 ? 143 HIS   T CD2 1 
ATOM   35013 C  CE1 . HIS   T  6  147 ? 45.595  -199.384 69.019  1.00 106.83 ? 143 HIS   T CE1 1 
ATOM   35014 N  NE2 . HIS   T  6  147 ? 44.597  -200.270 69.123  1.00 105.02 ? 143 HIS   T NE2 1 
ATOM   35015 N  N   . LEU   T  6  148 ? 48.973  -204.904 67.041  1.00 106.28 ? 144 LEU   T N   1 
ATOM   35016 C  CA  . LEU   T  6  148 ? 49.640  -205.807 66.067  1.00 105.22 ? 144 LEU   T CA  1 
ATOM   35017 C  C   . LEU   T  6  148 ? 48.565  -206.478 65.206  1.00 104.03 ? 144 LEU   T C   1 
ATOM   35018 O  O   . LEU   T  6  148 ? 47.528  -206.879 65.768  1.00 103.33 ? 144 LEU   T O   1 
ATOM   35019 C  CB  . LEU   T  6  148 ? 50.466  -206.851 66.822  1.00 106.01 ? 144 LEU   T CB  1 
ATOM   35020 C  CG  . LEU   T  6  148 ? 51.131  -207.912 65.947  1.00 108.28 ? 144 LEU   T CG  1 
ATOM   35021 C  CD1 . LEU   T  6  148 ? 52.316  -207.326 65.196  1.00 107.51 ? 144 LEU   T CD1 1 
ATOM   35022 C  CD2 . LEU   T  6  148 ? 51.557  -209.113 66.779  1.00 109.47 ? 144 LEU   T CD2 1 
ATOM   35023 N  N   . TYR   T  6  149 ? 48.813  -206.588 63.898  1.00 104.06 ? 145 TYR   T N   1 
ATOM   35024 C  CA  . TYR   T  6  149 ? 47.890  -207.193 62.904  1.00 102.44 ? 145 TYR   T CA  1 
ATOM   35025 C  C   . TYR   T  6  149 ? 48.664  -208.140 61.984  1.00 104.57 ? 145 TYR   T C   1 
ATOM   35026 O  O   . TYR   T  6  149 ? 49.883  -207.954 61.791  1.00 104.78 ? 145 TYR   T O   1 
ATOM   35027 C  CB  . TYR   T  6  149 ? 47.179  -206.106 62.095  1.00 101.06 ? 145 TYR   T CB  1 
ATOM   35028 C  CG  . TYR   T  6  149 ? 46.094  -205.389 62.856  1.00 99.84  ? 145 TYR   T CG  1 
ATOM   35029 C  CD1 . TYR   T  6  149 ? 44.805  -205.897 62.910  1.00 98.67  ? 145 TYR   T CD1 1 
ATOM   35030 C  CD2 . TYR   T  6  149 ? 46.355  -204.216 63.544  1.00 98.97  ? 145 TYR   T CD2 1 
ATOM   35031 C  CE1 . TYR   T  6  149 ? 43.801  -205.254 63.615  1.00 96.28  ? 145 TYR   T CE1 1 
ATOM   35032 C  CE2 . TYR   T  6  149 ? 45.363  -203.562 64.258  1.00 99.18  ? 145 TYR   T CE2 1 
ATOM   35033 C  CZ  . TYR   T  6  149 ? 44.080  -204.083 64.294  1.00 95.74  ? 145 TYR   T CZ  1 
ATOM   35034 O  OH  . TYR   T  6  149 ? 43.086  -203.461 64.992  1.00 96.90  ? 145 TYR   T OH  1 
ATOM   35035 N  N   . MET   T  6  150 ? 47.955  -209.136 61.451  1.00 103.48 ? 146 MET   T N   1 
ATOM   35036 C  CA  . MET   T  6  150 ? 48.431  -210.024 60.361  1.00 105.34 ? 146 MET   T CA  1 
ATOM   35037 C  C   . MET   T  6  150 ? 47.336  -210.092 59.294  1.00 101.77 ? 146 MET   T C   1 
ATOM   35038 O  O   . MET   T  6  150 ? 46.174  -210.340 59.661  1.00 101.14 ? 146 MET   T O   1 
ATOM   35039 C  CB  . MET   T  6  150 ? 48.737  -211.430 60.882  1.00 108.76 ? 146 MET   T CB  1 
ATOM   35040 C  CG  . MET   T  6  150 ? 49.320  -212.346 59.828  1.00 112.92 ? 146 MET   T CG  1 
ATOM   35041 S  SD  . MET   T  6  150 ? 49.994  -213.862 60.541  1.00 115.56 ? 146 MET   T SD  1 
ATOM   35042 C  CE  . MET   T  6  150 ? 49.925  -214.936 59.108  1.00 117.55 ? 146 MET   T CE  1 
ATOM   35043 N  N   . LEU   T  6  151 ? 47.705  -209.857 58.032  1.00 103.59 ? 147 LEU   T N   1 
ATOM   35044 C  CA  . LEU   T  6  151 ? 46.780  -209.776 56.871  1.00 106.77 ? 147 LEU   T CA  1 
ATOM   35045 C  C   . LEU   T  6  151 ? 47.167  -210.858 55.861  1.00 108.22 ? 147 LEU   T C   1 
ATOM   35046 O  O   . LEU   T  6  151 ? 48.372  -210.971 55.565  1.00 114.18 ? 147 LEU   T O   1 
ATOM   35047 C  CB  . LEU   T  6  151 ? 46.887  -208.376 56.258  1.00 107.02 ? 147 LEU   T CB  1 
ATOM   35048 C  CG  . LEU   T  6  151 ? 46.142  -208.161 54.941  1.00 108.19 ? 147 LEU   T CG  1 
ATOM   35049 C  CD1 . LEU   T  6  151 ? 44.635  -208.205 55.149  1.00 108.47 ? 147 LEU   T CD1 1 
ATOM   35050 C  CD2 . LEU   T  6  151 ? 46.550  -206.840 54.316  1.00 107.97 ? 147 LEU   T CD2 1 
ATOM   35051 N  N   . GLU   T  6  152 ? 46.182  -211.604 55.352  1.00 107.31 ? 148 GLU   T N   1 
ATOM   35052 C  CA  . GLU   T  6  152 ? 46.400  -212.780 54.469  1.00 108.71 ? 148 GLU   T CA  1 
ATOM   35053 C  C   . GLU   T  6  152 ? 45.818  -212.515 53.083  1.00 103.05 ? 148 GLU   T C   1 
ATOM   35054 O  O   . GLU   T  6  152 ? 44.926  -211.684 52.924  1.00 104.00 ? 148 GLU   T O   1 
ATOM   35055 C  CB  . GLU   T  6  152 ? 45.802  -214.027 55.119  1.00 112.70 ? 148 GLU   T CB  1 
ATOM   35056 C  CG  . GLU   T  6  152 ? 46.731  -214.655 56.140  1.00 117.64 ? 148 GLU   T CG  1 
ATOM   35057 C  CD  . GLU   T  6  152 ? 46.082  -215.671 57.058  1.00 126.96 ? 148 GLU   T CD  1 
ATOM   35058 O  OE1 . GLU   T  6  152 ? 44.837  -215.671 57.149  1.00 133.11 ? 148 GLU   T OE1 1 
ATOM   35059 O  OE2 . GLU   T  6  152 ? 46.826  -216.461 57.679  1.00 134.25 ? 148 GLU   T OE2 1 
ATOM   35060 N  N   . PRO   T  6  153 ? 46.326  -213.219 52.044  1.00 98.06  ? 149 PRO   T N   1 
ATOM   35061 C  CA  . PRO   T  6  153 ? 45.896  -213.024 50.655  1.00 96.50  ? 149 PRO   T CA  1 
ATOM   35062 C  C   . PRO   T  6  153 ? 44.385  -212.916 50.386  1.00 95.65  ? 149 PRO   T C   1 
ATOM   35063 O  O   . PRO   T  6  153 ? 44.025  -212.274 49.413  1.00 94.06  ? 149 PRO   T O   1 
ATOM   35064 C  CB  . PRO   T  6  153 ? 46.422  -214.292 49.974  1.00 97.17  ? 149 PRO   T CB  1 
ATOM   35065 C  CG  . PRO   T  6  153 ? 47.690  -214.613 50.726  1.00 100.06 ? 149 PRO   T CG  1 
ATOM   35066 C  CD  . PRO   T  6  153 ? 47.389  -214.229 52.158  1.00 99.86  ? 149 PRO   T CD  1 
ATOM   35067 N  N   . SER   T  6  154 ? 43.552  -213.550 51.220  1.00 93.80  ? 150 SER   T N   1 
ATOM   35068 C  CA  . SER   T  6  154 ? 42.065  -213.515 51.137  1.00 96.91  ? 150 SER   T CA  1 
ATOM   35069 C  C   . SER   T  6  154 ? 41.528  -212.122 51.488  1.00 97.97  ? 150 SER   T C   1 
ATOM   35070 O  O   . SER   T  6  154 ? 40.389  -211.814 51.080  1.00 100.82 ? 150 SER   T O   1 
ATOM   35071 C  CB  . SER   T  6  154 ? 41.446  -214.555 52.034  1.00 95.90  ? 150 SER   T CB  1 
ATOM   35072 O  OG  . SER   T  6  154 ? 41.724  -214.278 53.399  1.00 99.04  ? 150 SER   T OG  1 
ATOM   35073 N  N   . GLY   T  6  155 ? 42.306  -211.325 52.230  1.00 98.10  ? 151 GLY   T N   1 
ATOM   35074 C  CA  . GLY   T  6  155 ? 41.888  -210.021 52.780  1.00 96.55  ? 151 GLY   T CA  1 
ATOM   35075 C  C   . GLY   T  6  155 ? 41.505  -210.145 54.245  1.00 98.24  ? 151 GLY   T C   1 
ATOM   35076 O  O   . GLY   T  6  155 ? 41.161  -209.109 54.863  1.00 90.97  ? 151 GLY   T O   1 
ATOM   35077 N  N   . SER   T  6  156 ? 41.554  -211.371 54.780  1.00 99.36  ? 152 SER   T N   1 
ATOM   35078 C  CA  . SER   T  6  156 ? 41.325  -211.679 56.214  1.00 100.78 ? 152 SER   T CA  1 
ATOM   35079 C  C   . SER   T  6  156 ? 42.478  -211.091 57.029  1.00 98.39  ? 152 SER   T C   1 
ATOM   35080 O  O   . SER   T  6  156 ? 43.644  -211.244 56.608  1.00 93.70  ? 152 SER   T O   1 
ATOM   35081 C  CB  . SER   T  6  156 ? 41.183  -213.163 56.452  1.00 105.07 ? 152 SER   T CB  1 
ATOM   35082 O  OG  . SER   T  6  156 ? 40.898  -213.438 57.819  1.00 109.17 ? 152 SER   T OG  1 
ATOM   35083 N  N   . TYR   T  6  157 ? 42.145  -210.416 58.130  1.00 98.98  ? 153 TYR   T N   1 
ATOM   35084 C  CA  . TYR   T  6  157 ? 43.104  -209.903 59.140  1.00 98.88  ? 153 TYR   T CA  1 
ATOM   35085 C  C   . TYR   T  6  157 ? 42.431  -209.926 60.515  1.00 96.50  ? 153 TYR   T C   1 
ATOM   35086 O  O   . TYR   T  6  157 ? 41.190  -209.811 60.587  1.00 96.78  ? 153 TYR   T O   1 
ATOM   35087 C  CB  . TYR   T  6  157 ? 43.592  -208.500 58.767  1.00 97.68  ? 153 TYR   T CB  1 
ATOM   35088 C  CG  . TYR   T  6  157 ? 42.573  -207.400 58.935  1.00 95.58  ? 153 TYR   T CG  1 
ATOM   35089 C  CD1 . TYR   T  6  157 ? 42.340  -206.827 60.175  1.00 94.43  ? 153 TYR   T CD1 1 
ATOM   35090 C  CD2 . TYR   T  6  157 ? 41.842  -206.928 57.857  1.00 94.25  ? 153 TYR   T CD2 1 
ATOM   35091 C  CE1 . TYR   T  6  157 ? 41.405  -205.819 60.343  1.00 93.07  ? 153 TYR   T CE1 1 
ATOM   35092 C  CE2 . TYR   T  6  157 ? 40.905  -205.918 58.006  1.00 93.58  ? 153 TYR   T CE2 1 
ATOM   35093 C  CZ  . TYR   T  6  157 ? 40.685  -205.362 59.254  1.00 92.62  ? 153 TYR   T CZ  1 
ATOM   35094 O  OH  . TYR   T  6  157 ? 39.765  -204.368 59.414  1.00 93.61  ? 153 TYR   T OH  1 
ATOM   35095 N  N   . TRP   T  6  158 ? 43.235  -210.079 61.566  1.00 96.58  ? 154 TRP   T N   1 
ATOM   35096 C  CA  . TRP   T  6  158 ? 42.801  -209.993 62.984  1.00 97.02  ? 154 TRP   T CA  1 
ATOM   35097 C  C   . TRP   T  6  158 ? 43.856  -209.223 63.779  1.00 95.48  ? 154 TRP   T C   1 
ATOM   35098 O  O   . TRP   T  6  158 ? 44.995  -209.103 63.289  1.00 96.24  ? 154 TRP   T O   1 
ATOM   35099 C  CB  . TRP   T  6  158 ? 42.587  -211.390 63.578  1.00 98.73  ? 154 TRP   T CB  1 
ATOM   35100 C  CG  . TRP   T  6  158 ? 41.625  -212.261 62.828  1.00 97.62  ? 154 TRP   T CG  1 
ATOM   35101 C  CD1 . TRP   T  6  158 ? 41.910  -213.413 62.156  1.00 96.75  ? 154 TRP   T CD1 1 
ATOM   35102 C  CD2 . TRP   T  6  158 ? 40.208  -212.058 62.693  1.00 96.66  ? 154 TRP   T CD2 1 
ATOM   35103 N  NE1 . TRP   T  6  158 ? 40.772  -213.936 61.605  1.00 94.92  ? 154 TRP   T NE1 1 
ATOM   35104 C  CE2 . TRP   T  6  158 ? 39.711  -213.130 61.920  1.00 95.30  ? 154 TRP   T CE2 1 
ATOM   35105 C  CE3 . TRP   T  6  158 ? 39.315  -211.078 63.142  1.00 97.25  ? 154 TRP   T CE3 1 
ATOM   35106 C  CZ2 . TRP   T  6  158 ? 38.361  -213.245 61.591  1.00 96.31  ? 154 TRP   T CZ2 1 
ATOM   35107 C  CZ3 . TRP   T  6  158 ? 37.982  -211.191 62.814  1.00 98.08  ? 154 TRP   T CZ3 1 
ATOM   35108 C  CH2 . TRP   T  6  158 ? 37.513  -212.263 62.052  1.00 97.74  ? 154 TRP   T CH2 1 
ATOM   35109 N  N   . GLY   T  6  159 ? 43.482  -208.732 64.960  1.00 95.22  ? 155 GLY   T N   1 
ATOM   35110 C  CA  . GLY   T  6  159 ? 44.440  -208.291 65.989  1.00 99.62  ? 155 GLY   T CA  1 
ATOM   35111 C  C   . GLY   T  6  159 ? 45.113  -209.499 66.615  1.00 100.72 ? 155 GLY   T C   1 
ATOM   35112 O  O   . GLY   T  6  159 ? 44.424  -210.525 66.785  1.00 100.07 ? 155 GLY   T O   1 
ATOM   35113 N  N   . TYR   T  6  160 ? 46.403  -209.395 66.946  1.00 105.25 ? 156 TYR   T N   1 
ATOM   35114 C  CA  . TYR   T  6  160 ? 47.220  -210.510 67.493  1.00 105.21 ? 156 TYR   T CA  1 
ATOM   35115 C  C   . TYR   T  6  160 ? 48.002  -210.047 68.726  1.00 107.70 ? 156 TYR   T C   1 
ATOM   35116 O  O   . TYR   T  6  160 ? 48.380  -208.861 68.802  1.00 108.24 ? 156 TYR   T O   1 
ATOM   35117 C  CB  . TYR   T  6  160 ? 48.163  -211.056 66.418  1.00 108.09 ? 156 TYR   T CB  1 
ATOM   35118 C  CG  . TYR   T  6  160 ? 47.493  -211.935 65.393  1.00 109.11 ? 156 TYR   T CG  1 
ATOM   35119 C  CD1 . TYR   T  6  160 ? 46.892  -211.384 64.273  1.00 108.24 ? 156 TYR   T CD1 1 
ATOM   35120 C  CD2 . TYR   T  6  160 ? 47.450  -213.314 65.541  1.00 107.76 ? 156 TYR   T CD2 1 
ATOM   35121 C  CE1 . TYR   T  6  160 ? 46.267  -212.177 63.324  1.00 106.06 ? 156 TYR   T CE1 1 
ATOM   35122 C  CE2 . TYR   T  6  160 ? 46.832  -214.122 64.600  1.00 106.52 ? 156 TYR   T CE2 1 
ATOM   35123 C  CZ  . TYR   T  6  160 ? 46.241  -213.550 63.487  1.00 104.51 ? 156 TYR   T CZ  1 
ATOM   35124 O  OH  . TYR   T  6  160 ? 45.621  -214.315 62.546  1.00 104.92 ? 156 TYR   T OH  1 
ATOM   35125 N  N   . LYS   T  6  161 ? 48.210  -210.971 69.667  1.00 108.18 ? 157 LYS   T N   1 
ATOM   35126 C  CA  . LYS   T  6  161 ? 49.205  -210.855 70.767  1.00 107.76 ? 157 LYS   T CA  1 
ATOM   35127 C  C   . LYS   T  6  161 ? 50.589  -211.141 70.181  1.00 106.03 ? 157 LYS   T C   1 
ATOM   35128 O  O   . LYS   T  6  161 ? 51.534  -210.388 70.469  1.00 105.53 ? 157 LYS   T O   1 
ATOM   35129 C  CB  . LYS   T  6  161 ? 48.873  -211.835 71.896  1.00 110.20 ? 157 LYS   T CB  1 
ATOM   35130 C  CG  . LYS   T  6  161 ? 47.668  -211.448 72.740  1.00 112.39 ? 157 LYS   T CG  1 
ATOM   35131 C  CD  . LYS   T  6  161 ? 47.061  -212.600 73.506  1.00 114.96 ? 157 LYS   T CD  1 
ATOM   35132 C  CE  . LYS   T  6  161 ? 45.858  -212.176 74.320  1.00 115.78 ? 157 LYS   T CE  1 
ATOM   35133 N  NZ  . LYS   T  6  161 ? 45.161  -213.338 74.917  1.00 117.76 ? 157 LYS   T NZ  1 
ATOM   35134 N  N   . GLY   T  6  162 ? 50.682  -212.210 69.390  1.00 104.54 ? 158 GLY   T N   1 
ATOM   35135 C  CA  . GLY   T  6  162 ? 51.857  -212.564 68.574  1.00 105.92 ? 158 GLY   T CA  1 
ATOM   35136 C  C   . GLY   T  6  162 ? 51.418  -213.071 67.215  1.00 105.80 ? 158 GLY   T C   1 
ATOM   35137 O  O   . GLY   T  6  162 ? 50.299  -213.605 67.118  1.00 106.70 ? 158 GLY   T O   1 
ATOM   35138 N  N   . ALA   T  6  163 ? 52.254  -212.895 66.192  1.00 105.49 ? 159 ALA   T N   1 
ATOM   35139 C  CA  . ALA   T  6  163 ? 51.950  -213.294 64.800  1.00 104.33 ? 159 ALA   T CA  1 
ATOM   35140 C  C   . ALA   T  6  163 ? 53.217  -213.822 64.125  1.00 104.78 ? 159 ALA   T C   1 
ATOM   35141 O  O   . ALA   T  6  163 ? 54.312  -213.298 64.406  1.00 104.23 ? 159 ALA   T O   1 
ATOM   35142 C  CB  . ALA   T  6  163 ? 51.364  -212.129 64.044  1.00 102.88 ? 159 ALA   T CB  1 
ATOM   35143 N  N   . ALA   T  6  164 ? 53.048  -214.832 63.273  1.00 104.80 ? 160 ALA   T N   1 
ATOM   35144 C  CA  . ALA   T  6  164 ? 54.127  -215.503 62.517  1.00 106.59 ? 160 ALA   T CA  1 
ATOM   35145 C  C   . ALA   T  6  164 ? 53.585  -215.940 61.153  1.00 106.57 ? 160 ALA   T C   1 
ATOM   35146 O  O   . ALA   T  6  164 ? 52.386  -216.280 61.069  1.00 107.27 ? 160 ALA   T O   1 
ATOM   35147 C  CB  . ALA   T  6  164 ? 54.646  -216.675 63.310  1.00 108.09 ? 160 ALA   T CB  1 
ATOM   35148 N  N   . THR   T  6  165 ? 54.437  -215.913 60.126  1.00 106.86 ? 161 THR   T N   1 
ATOM   35149 C  CA  . THR   T  6  165 ? 54.130  -216.411 58.759  1.00 107.03 ? 161 THR   T CA  1 
ATOM   35150 C  C   . THR   T  6  165 ? 55.432  -216.728 58.018  1.00 105.70 ? 161 THR   T C   1 
ATOM   35151 O  O   . THR   T  6  165 ? 56.472  -216.134 58.365  1.00 103.12 ? 161 THR   T O   1 
ATOM   35152 C  CB  . THR   T  6  165 ? 53.290  -215.394 57.979  1.00 105.14 ? 161 THR   T CB  1 
ATOM   35153 O  OG1 . THR   T  6  165 ? 52.859  -216.008 56.765  1.00 109.37 ? 161 THR   T OG1 1 
ATOM   35154 C  CG2 . THR   T  6  165 ? 54.047  -214.120 57.677  1.00 105.77 ? 161 THR   T CG2 1 
ATOM   35155 N  N   . GLY   T  6  166 ? 55.352  -217.616 57.023  1.00 106.74 ? 162 GLY   T N   1 
ATOM   35156 C  CA  . GLY   T  6  166 ? 56.503  -218.107 56.242  1.00 110.89 ? 162 GLY   T CA  1 
ATOM   35157 C  C   . GLY   T  6  166 ? 56.735  -219.592 56.465  1.00 113.78 ? 162 GLY   T C   1 
ATOM   35158 O  O   . GLY   T  6  166 ? 55.813  -220.271 56.962  1.00 114.85 ? 162 GLY   T O   1 
ATOM   35159 N  N   . LYS   T  6  167 ? 57.930  -220.079 56.126  1.00 117.10 ? 163 LYS   T N   1 
ATOM   35160 C  CA  . LYS   T  6  167 ? 58.261  -221.528 56.123  1.00 119.82 ? 163 LYS   T CA  1 
ATOM   35161 C  C   . LYS   T  6  167 ? 58.337  -222.053 57.562  1.00 120.48 ? 163 LYS   T C   1 
ATOM   35162 O  O   . LYS   T  6  167 ? 58.037  -223.246 57.757  1.00 122.40 ? 163 LYS   T O   1 
ATOM   35163 C  CB  . LYS   T  6  167 ? 59.561  -221.783 55.354  1.00 124.97 ? 163 LYS   T CB  1 
ATOM   35164 C  CG  . LYS   T  6  167 ? 59.737  -223.219 54.877  1.00 127.72 ? 163 LYS   T CG  1 
ATOM   35165 C  CD  . LYS   T  6  167 ? 60.060  -223.340 53.404  1.00 130.61 ? 163 LYS   T CD  1 
ATOM   35166 C  CE  . LYS   T  6  167 ? 61.487  -222.957 53.080  1.00 134.11 ? 163 LYS   T CE  1 
ATOM   35167 N  NZ  . LYS   T  6  167 ? 61.682  -222.758 51.625  1.00 135.93 ? 163 LYS   T NZ  1 
ATOM   35168 N  N   . GLY   T  6  168 ? 58.706  -221.203 58.527  1.00 122.14 ? 164 GLY   T N   1 
ATOM   35169 C  CA  . GLY   T  6  168 ? 58.865  -221.589 59.945  1.00 123.18 ? 164 GLY   T CA  1 
ATOM   35170 C  C   . GLY   T  6  168 ? 57.764  -221.033 60.837  1.00 119.99 ? 164 GLY   T C   1 
ATOM   35171 O  O   . GLY   T  6  168 ? 58.072  -220.719 62.004  1.00 115.97 ? 164 GLY   T O   1 
ATOM   35172 N  N   . ARG   T  6  169 ? 56.526  -220.946 60.333  1.00 118.70 ? 165 ARG   T N   1 
ATOM   35173 C  CA  . ARG   T  6  169 ? 55.384  -220.294 61.038  1.00 116.59 ? 165 ARG   T CA  1 
ATOM   35174 C  C   . ARG   T  6  169 ? 54.953  -221.141 62.245  1.00 121.34 ? 165 ARG   T C   1 
ATOM   35175 O  O   . ARG   T  6  169 ? 54.658  -220.539 63.295  1.00 116.15 ? 165 ARG   T O   1 
ATOM   35176 C  CB  . ARG   T  6  169 ? 54.221  -220.014 60.076  1.00 115.69 ? 165 ARG   T CB  1 
ATOM   35177 C  CG  . ARG   T  6  169 ? 53.239  -221.161 59.871  1.00 115.15 ? 165 ARG   T CG  1 
ATOM   35178 C  CD  . ARG   T  6  169 ? 52.530  -221.077 58.531  1.00 115.38 ? 165 ARG   T CD  1 
ATOM   35179 N  NE  . ARG   T  6  169 ? 53.423  -221.476 57.450  1.00 116.12 ? 165 ARG   T NE  1 
ATOM   35180 C  CZ  . ARG   T  6  169 ? 53.435  -222.664 56.844  1.00 116.67 ? 165 ARG   T CZ  1 
ATOM   35181 N  NH1 . ARG   T  6  169 ? 52.577  -223.616 57.179  1.00 119.02 ? 165 ARG   T NH1 1 
ATOM   35182 N  NH2 . ARG   T  6  169 ? 54.313  -222.894 55.882  1.00 120.42 ? 165 ARG   T NH2 1 
ATOM   35183 N  N   . GLN   T  6  170 ? 54.932  -222.474 62.112  1.00 123.12 ? 166 GLN   T N   1 
ATOM   35184 C  CA  . GLN   T  6  170 ? 54.445  -223.411 63.162  1.00 124.43 ? 166 GLN   T CA  1 
ATOM   35185 C  C   . GLN   T  6  170 ? 55.433  -223.415 64.334  1.00 125.05 ? 166 GLN   T C   1 
ATOM   35186 O  O   . GLN   T  6  170 ? 54.972  -223.332 65.490  1.00 121.35 ? 166 GLN   T O   1 
ATOM   35187 C  CB  . GLN   T  6  170 ? 54.262  -224.818 62.595  1.00 130.13 ? 166 GLN   T CB  1 
ATOM   35188 C  CG  . GLN   T  6  170 ? 53.139  -224.917 61.573  1.00 134.47 ? 166 GLN   T CG  1 
ATOM   35189 C  CD  . GLN   T  6  170 ? 53.050  -226.298 60.971  1.00 143.14 ? 166 GLN   T CD  1 
ATOM   35190 O  OE1 . GLN   T  6  170 ? 53.972  -226.762 60.303  1.00 152.63 ? 166 GLN   T OE1 1 
ATOM   35191 N  NE2 . GLN   T  6  170 ? 51.935  -226.974 61.201  1.00 148.87 ? 166 GLN   T NE2 1 
ATOM   35192 N  N   . SER   T  6  171 ? 56.733  -223.516 64.035  1.00 125.41 ? 167 SER   T N   1 
ATOM   35193 C  CA  . SER   T  6  171 ? 57.852  -223.404 65.008  1.00 128.95 ? 167 SER   T CA  1 
ATOM   35194 C  C   . SER   T  6  171 ? 57.721  -222.090 65.786  1.00 124.62 ? 167 SER   T C   1 
ATOM   35195 O  O   . SER   T  6  171 ? 57.713  -222.131 67.031  1.00 124.68 ? 167 SER   T O   1 
ATOM   35196 C  CB  . SER   T  6  171 ? 59.187  -223.495 64.308  1.00 131.51 ? 167 SER   T CB  1 
ATOM   35197 O  OG  . SER   T  6  171 ? 60.248  -223.135 65.179  1.00 136.16 ? 167 SER   T OG  1 
ATOM   35198 N  N   . ALA   T  6  172 ? 57.602  -220.974 65.063  1.00 122.26 ? 168 ALA   T N   1 
ATOM   35199 C  CA  . ALA   T  6  172 ? 57.504  -219.602 65.614  1.00 119.79 ? 168 ALA   T CA  1 
ATOM   35200 C  C   . ALA   T  6  172 ? 56.224  -219.447 66.445  1.00 118.54 ? 168 ALA   T C   1 
ATOM   35201 O  O   . ALA   T  6  172 ? 56.300  -218.818 67.518  1.00 118.06 ? 168 ALA   T O   1 
ATOM   35202 C  CB  . ALA   T  6  172 ? 57.556  -218.599 64.491  1.00 118.74 ? 168 ALA   T CB  1 
ATOM   35203 N  N   . LYS   T  6  173 ? 55.096  -219.987 65.966  1.00 119.54 ? 169 LYS   T N   1 
ATOM   35204 C  CA  . LYS   T  6  173 ? 53.776  -219.912 66.655  1.00 123.28 ? 169 LYS   T CA  1 
ATOM   35205 C  C   . LYS   T  6  173 ? 53.868  -220.599 68.022  1.00 126.60 ? 169 LYS   T C   1 
ATOM   35206 O  O   . LYS   T  6  173 ? 53.431  -219.986 69.013  1.00 131.02 ? 169 LYS   T O   1 
ATOM   35207 C  CB  . LYS   T  6  173 ? 52.662  -220.555 65.822  1.00 122.66 ? 169 LYS   T CB  1 
ATOM   35208 C  CG  . LYS   T  6  173 ? 51.984  -219.629 64.824  1.00 121.35 ? 169 LYS   T CG  1 
ATOM   35209 C  CD  . LYS   T  6  173 ? 50.590  -220.075 64.445  1.00 122.68 ? 169 LYS   T CD  1 
ATOM   35210 C  CE  . LYS   T  6  173 ? 50.009  -219.277 63.297  1.00 123.67 ? 169 LYS   T CE  1 
ATOM   35211 N  NZ  . LYS   T  6  173 ? 50.625  -219.650 62.002  1.00 124.73 ? 169 LYS   T NZ  1 
ATOM   35212 N  N   . ALA   T  6  174 ? 54.405  -221.822 68.065  1.00 130.33 ? 170 ALA   T N   1 
ATOM   35213 C  CA  . ALA   T  6  174 ? 54.614  -222.612 69.303  1.00 133.72 ? 170 ALA   T CA  1 
ATOM   35214 C  C   . ALA   T  6  174 ? 55.426  -221.788 70.309  1.00 136.24 ? 170 ALA   T C   1 
ATOM   35215 O  O   . ALA   T  6  174 ? 55.096  -221.829 71.511  1.00 138.61 ? 170 ALA   T O   1 
ATOM   35216 C  CB  . ALA   T  6  174 ? 55.304  -223.917 68.987  1.00 136.98 ? 170 ALA   T CB  1 
ATOM   35217 N  N   . GLU   T  6  175 ? 56.440  -221.063 69.825  1.00 135.72 ? 171 GLU   T N   1 
ATOM   35218 C  CA  . GLU   T  6  175 ? 57.368  -220.258 70.664  1.00 135.79 ? 171 GLU   T CA  1 
ATOM   35219 C  C   . GLU   T  6  175 ? 56.639  -219.006 71.165  1.00 132.59 ? 171 GLU   T C   1 
ATOM   35220 O  O   . GLU   T  6  175 ? 56.859  -218.630 72.335  1.00 125.92 ? 171 GLU   T O   1 
ATOM   35221 C  CB  . GLU   T  6  175 ? 58.635  -219.907 69.879  1.00 138.95 ? 171 GLU   T CB  1 
ATOM   35222 C  CG  . GLU   T  6  175 ? 59.885  -219.887 70.740  1.00 145.99 ? 171 GLU   T CG  1 
ATOM   35223 C  CD  . GLU   T  6  175 ? 60.188  -221.204 71.438  1.00 151.43 ? 171 GLU   T CD  1 
ATOM   35224 O  OE1 . GLU   T  6  175 ? 59.835  -222.262 70.879  1.00 155.59 ? 171 GLU   T OE1 1 
ATOM   35225 O  OE2 . GLU   T  6  175 ? 60.770  -221.171 72.540  1.00 161.59 ? 171 GLU   T OE2 1 
ATOM   35226 N  N   . LEU   T  6  176 ? 55.810  -218.397 70.311  1.00 131.04 ? 172 LEU   T N   1 
ATOM   35227 C  CA  . LEU   T  6  176 ? 54.964  -217.216 70.641  1.00 130.67 ? 172 LEU   T CA  1 
ATOM   35228 C  C   . LEU   T  6  176 ? 53.971  -217.589 71.751  1.00 131.87 ? 172 LEU   T C   1 
ATOM   35229 O  O   . LEU   T  6  176 ? 53.852  -216.807 72.715  1.00 132.93 ? 172 LEU   T O   1 
ATOM   35230 C  CB  . LEU   T  6  176 ? 54.233  -216.736 69.378  1.00 129.07 ? 172 LEU   T CB  1 
ATOM   35231 C  CG  . LEU   T  6  176 ? 54.701  -215.419 68.749  1.00 127.92 ? 172 LEU   T CG  1 
ATOM   35232 C  CD1 . LEU   T  6  176 ? 56.183  -215.157 68.970  1.00 126.67 ? 172 LEU   T CD1 1 
ATOM   35233 C  CD2 . LEU   T  6  176 ? 54.381  -215.394 67.261  1.00 129.78 ? 172 LEU   T CD2 1 
ATOM   35234 N  N   . GLU   T  6  177 ? 53.293  -218.735 71.622  1.00 130.78 ? 173 GLU   T N   1 
ATOM   35235 C  CA  . GLU   T  6  177 ? 52.237  -219.198 72.566  1.00 133.08 ? 173 GLU   T CA  1 
ATOM   35236 C  C   . GLU   T  6  177 ? 52.819  -219.342 73.978  1.00 131.23 ? 173 GLU   T C   1 
ATOM   35237 O  O   . GLU   T  6  177 ? 52.085  -219.043 74.939  1.00 134.85 ? 173 GLU   T O   1 
ATOM   35238 C  CB  . GLU   T  6  177 ? 51.624  -220.523 72.106  1.00 135.08 ? 173 GLU   T CB  1 
ATOM   35239 C  CG  . GLU   T  6  177 ? 50.644  -220.377 70.954  1.00 138.36 ? 173 GLU   T CG  1 
ATOM   35240 C  CD  . GLU   T  6  177 ? 49.964  -221.669 70.524  1.00 143.44 ? 173 GLU   T CD  1 
ATOM   35241 O  OE1 . GLU   T  6  177 ? 49.875  -221.910 69.303  1.00 147.44 ? 173 GLU   T OE1 1 
ATOM   35242 O  OE2 . GLU   T  6  177 ? 49.518  -222.429 71.410  1.00 150.22 ? 173 GLU   T OE2 1 
ATOM   35243 N  N   . LYS   T  6  178 ? 54.076  -219.790 74.093  1.00 134.75 ? 174 LYS   T N   1 
ATOM   35244 C  CA  . LYS   T  6  178 ? 54.791  -219.969 75.389  1.00 139.28 ? 174 LYS   T CA  1 
ATOM   35245 C  C   . LYS   T  6  178 ? 54.960  -218.609 76.077  1.00 137.32 ? 174 LYS   T C   1 
ATOM   35246 O  O   . LYS   T  6  178 ? 54.717  -218.539 77.299  1.00 137.05 ? 174 LYS   T O   1 
ATOM   35247 C  CB  . LYS   T  6  178 ? 56.141  -220.664 75.183  1.00 142.94 ? 174 LYS   T CB  1 
ATOM   35248 C  CG  . LYS   T  6  178 ? 56.079  -222.186 75.207  1.00 145.69 ? 174 LYS   T CG  1 
ATOM   35249 C  CD  . LYS   T  6  178 ? 57.058  -222.873 74.279  1.00 150.49 ? 174 LYS   T CD  1 
ATOM   35250 C  CE  . LYS   T  6  178 ? 56.701  -224.326 74.042  1.00 153.68 ? 174 LYS   T CE  1 
ATOM   35251 N  NZ  . LYS   T  6  178 ? 57.517  -224.933 72.964  1.00 157.79 ? 174 LYS   T NZ  1 
ATOM   35252 N  N   . LEU   T  6  179 ? 55.359  -217.577 75.323  1.00 137.09 ? 175 LEU   T N   1 
ATOM   35253 C  CA  . LEU   T  6  179 ? 55.522  -216.187 75.831  1.00 135.12 ? 175 LEU   T CA  1 
ATOM   35254 C  C   . LEU   T  6  179 ? 54.180  -215.669 76.362  1.00 133.89 ? 175 LEU   T C   1 
ATOM   35255 O  O   . LEU   T  6  179 ? 54.177  -215.084 77.463  1.00 135.60 ? 175 LEU   T O   1 
ATOM   35256 C  CB  . LEU   T  6  179 ? 56.057  -215.279 74.718  1.00 131.79 ? 175 LEU   T CB  1 
ATOM   35257 C  CG  . LEU   T  6  179 ? 57.547  -215.414 74.411  1.00 134.17 ? 175 LEU   T CG  1 
ATOM   35258 C  CD1 . LEU   T  6  179 ? 57.917  -214.602 73.179  1.00 131.77 ? 175 LEU   T CD1 1 
ATOM   35259 C  CD2 . LEU   T  6  179 ? 58.389  -214.987 75.604  1.00 137.57 ? 175 LEU   T CD2 1 
ATOM   35260 N  N   . VAL   T  6  180 ? 53.090  -215.878 75.616  1.00 129.96 ? 176 VAL   T N   1 
ATOM   35261 C  CA  . VAL   T  6  180 ? 51.721  -215.404 75.988  1.00 132.19 ? 176 VAL   T CA  1 
ATOM   35262 C  C   . VAL   T  6  180 ? 51.314  -216.067 77.310  1.00 134.32 ? 176 VAL   T C   1 
ATOM   35263 O  O   . VAL   T  6  180 ? 50.750  -215.367 78.172  1.00 130.01 ? 176 VAL   T O   1 
ATOM   35264 C  CB  . VAL   T  6  180 ? 50.690  -215.674 74.873  1.00 131.83 ? 176 VAL   T CB  1 
ATOM   35265 C  CG1 . VAL   T  6  180 ? 49.270  -215.357 75.321  1.00 133.04 ? 176 VAL   T CG1 1 
ATOM   35266 C  CG2 . VAL   T  6  180 ? 51.023  -214.902 73.604  1.00 131.87 ? 176 VAL   T CG2 1 
ATOM   35267 N  N   . ASP   T  6  181 ? 51.600  -217.362 77.464  1.00 139.10 ? 177 ASP   T N   1 
ATOM   35268 C  CA  . ASP   T  6  181 ? 51.264  -218.155 78.677  1.00 145.05 ? 177 ASP   T CA  1 
ATOM   35269 C  C   . ASP   T  6  181 ? 52.144  -217.702 79.851  1.00 145.47 ? 177 ASP   T C   1 
ATOM   35270 O  O   . ASP   T  6  181 ? 51.590  -217.514 80.951  1.00 145.06 ? 177 ASP   T O   1 
ATOM   35271 C  CB  . ASP   T  6  181 ? 51.398  -219.659 78.417  1.00 154.59 ? 177 ASP   T CB  1 
ATOM   35272 C  CG  . ASP   T  6  181 ? 50.357  -220.225 77.463  1.00 157.80 ? 177 ASP   T CG  1 
ATOM   35273 O  OD1 . ASP   T  6  181 ? 49.231  -219.686 77.421  1.00 160.26 ? 177 ASP   T OD1 1 
ATOM   35274 O  OD2 . ASP   T  6  181 ? 50.680  -221.208 76.768  1.00 168.93 ? 177 ASP   T OD2 1 
ATOM   35275 N  N   . HIS   T  6  182 ? 53.451  -217.522 79.628  1.00 144.93 ? 178 HIS   T N   1 
ATOM   35276 C  CA  . HIS   T  6  182 ? 54.461  -217.255 80.691  1.00 151.39 ? 178 HIS   T CA  1 
ATOM   35277 C  C   . HIS   T  6  182 ? 54.466  -215.779 81.113  1.00 146.43 ? 178 HIS   T C   1 
ATOM   35278 O  O   . HIS   T  6  182 ? 55.088  -215.484 82.147  1.00 151.53 ? 178 HIS   T O   1 
ATOM   35279 C  CB  . HIS   T  6  182 ? 55.862  -217.703 80.248  1.00 157.30 ? 178 HIS   T CB  1 
ATOM   35280 C  CG  . HIS   T  6  182 ? 56.037  -219.185 80.182  1.00 165.19 ? 178 HIS   T CG  1 
ATOM   35281 N  ND1 . HIS   T  6  182 ? 56.953  -219.781 79.336  1.00 171.81 ? 178 HIS   T ND1 1 
ATOM   35282 C  CD2 . HIS   T  6  182 ? 55.423  -220.192 80.843  1.00 168.05 ? 178 HIS   T CD2 1 
ATOM   35283 C  CE1 . HIS   T  6  182 ? 56.900  -221.089 79.483  1.00 173.79 ? 178 HIS   T CE1 1 
ATOM   35284 N  NE2 . HIS   T  6  182 ? 55.967  -221.368 80.400  1.00 168.06 ? 178 HIS   T NE2 1 
ATOM   35285 N  N   . HIS   T  6  183 ? 53.820  -214.886 80.355  1.00 145.22 ? 179 HIS   T N   1 
ATOM   35286 C  CA  . HIS   T  6  183 ? 53.783  -213.422 80.628  1.00 145.79 ? 179 HIS   T CA  1 
ATOM   35287 C  C   . HIS   T  6  183 ? 52.357  -212.895 80.466  1.00 147.91 ? 179 HIS   T C   1 
ATOM   35288 O  O   . HIS   T  6  183 ? 52.060  -212.203 79.494  1.00 147.85 ? 179 HIS   T O   1 
ATOM   35289 C  CB  . HIS   T  6  183 ? 54.783  -212.681 79.724  1.00 143.62 ? 179 HIS   T CB  1 
ATOM   35290 C  CG  . HIS   T  6  183 ? 56.185  -213.190 79.808  1.00 143.21 ? 179 HIS   T CG  1 
ATOM   35291 N  ND1 . HIS   T  6  183 ? 57.074  -212.769 80.782  1.00 140.02 ? 179 HIS   T ND1 1 
ATOM   35292 C  CD2 . HIS   T  6  183 ? 56.861  -214.070 79.037  1.00 145.91 ? 179 HIS   T CD2 1 
ATOM   35293 C  CE1 . HIS   T  6  183 ? 58.232  -213.374 80.609  1.00 142.33 ? 179 HIS   T CE1 1 
ATOM   35294 N  NE2 . HIS   T  6  183 ? 58.127  -214.178 79.547  1.00 145.01 ? 179 HIS   T NE2 1 
ATOM   35295 N  N   . PRO   T  6  184 ? 51.430  -213.199 81.407  1.00 145.41 ? 180 PRO   T N   1 
ATOM   35296 C  CA  . PRO   T  6  184 ? 50.055  -212.699 81.327  1.00 144.37 ? 180 PRO   T CA  1 
ATOM   35297 C  C   . PRO   T  6  184 ? 49.929  -211.191 81.602  1.00 142.26 ? 180 PRO   T C   1 
ATOM   35298 O  O   . PRO   T  6  184 ? 49.011  -210.579 81.079  1.00 132.45 ? 180 PRO   T O   1 
ATOM   35299 C  CB  . PRO   T  6  184 ? 49.316  -213.507 82.406  1.00 143.46 ? 180 PRO   T CB  1 
ATOM   35300 C  CG  . PRO   T  6  184 ? 50.392  -213.852 83.413  1.00 145.35 ? 180 PRO   T CG  1 
ATOM   35301 C  CD  . PRO   T  6  184 ? 51.650  -214.045 82.591  1.00 146.16 ? 180 PRO   T CD  1 
ATOM   35302 N  N   . GLU   T  6  185 ? 50.842  -210.635 82.405  1.00 145.78 ? 181 GLU   T N   1 
ATOM   35303 C  CA  . GLU   T  6  185 ? 50.861  -209.189 82.769  1.00 145.79 ? 181 GLU   T CA  1 
ATOM   35304 C  C   . GLU   T  6  185 ? 51.380  -208.374 81.575  1.00 149.01 ? 181 GLU   T C   1 
ATOM   35305 O  O   . GLU   T  6  185 ? 50.777  -207.319 81.291  1.00 155.37 ? 181 GLU   T O   1 
ATOM   35306 C  CB  . GLU   T  6  185 ? 51.658  -208.892 84.048  1.00 149.78 ? 181 GLU   T CB  1 
ATOM   35307 C  CG  . GLU   T  6  185 ? 52.521  -210.028 84.578  1.00 152.00 ? 181 GLU   T CG  1 
ATOM   35308 C  CD  . GLU   T  6  185 ? 53.703  -210.418 83.707  1.00 154.55 ? 181 GLU   T CD  1 
ATOM   35309 O  OE1 . GLU   T  6  185 ? 54.032  -211.621 83.668  1.00 157.64 ? 181 GLU   T OE1 1 
ATOM   35310 O  OE2 . GLU   T  6  185 ? 54.291  -209.519 83.073  1.00 151.51 ? 181 GLU   T OE2 1 
ATOM   35311 N  N   . GLY   T  6  186 ? 52.439  -208.838 80.901  1.00 141.80 ? 182 GLY   T N   1 
ATOM   35312 C  CA  . GLY   T  6  186 ? 52.968  -208.200 79.678  1.00 136.11 ? 182 GLY   T CA  1 
ATOM   35313 C  C   . GLY   T  6  186 ? 54.472  -208.353 79.530  1.00 132.97 ? 182 GLY   T C   1 
ATOM   35314 O  O   . GLY   T  6  186 ? 55.154  -208.581 80.547  1.00 132.95 ? 182 GLY   T O   1 
ATOM   35315 N  N   . LEU   T  6  187 ? 54.961  -208.214 78.294  1.00 132.08 ? 183 LEU   T N   1 
ATOM   35316 C  CA  . LEU   T  6  187 ? 56.397  -208.262 77.908  1.00 134.00 ? 183 LEU   T CA  1 
ATOM   35317 C  C   . LEU   T  6  187 ? 56.878  -206.829 77.646  1.00 132.45 ? 183 LEU   T C   1 
ATOM   35318 O  O   . LEU   T  6  187 ? 56.102  -206.055 77.051  1.00 130.63 ? 183 LEU   T O   1 
ATOM   35319 C  CB  . LEU   T  6  187 ? 56.522  -209.135 76.653  1.00 134.04 ? 183 LEU   T CB  1 
ATOM   35320 C  CG  . LEU   T  6  187 ? 57.896  -209.742 76.369  1.00 137.09 ? 183 LEU   T CG  1 
ATOM   35321 C  CD1 . LEU   T  6  187 ? 58.319  -210.691 77.480  1.00 139.90 ? 183 LEU   T CD1 1 
ATOM   35322 C  CD2 . LEU   T  6  187 ? 57.889  -210.470 75.032  1.00 136.87 ? 183 LEU   T CD2 1 
ATOM   35323 N  N   . SER   T  6  188 ? 58.091  -206.479 78.089  1.00 132.15 ? 184 SER   T N   1 
ATOM   35324 C  CA  . SER   T  6  188 ? 58.705  -205.140 77.877  1.00 130.65 ? 184 SER   T CA  1 
ATOM   35325 C  C   . SER   T  6  188 ? 59.282  -205.068 76.460  1.00 131.16 ? 184 SER   T C   1 
ATOM   35326 O  O   . SER   T  6  188 ? 59.656  -206.127 75.918  1.00 131.22 ? 184 SER   T O   1 
ATOM   35327 C  CB  . SER   T  6  188 ? 59.748  -204.818 78.921  1.00 129.95 ? 184 SER   T CB  1 
ATOM   35328 O  OG  . SER   T  6  188 ? 60.955  -205.525 78.684  1.00 130.23 ? 184 SER   T OG  1 
ATOM   35329 N  N   . ALA   T  6  189 ? 59.336  -203.862 75.889  1.00 132.87 ? 185 ALA   T N   1 
ATOM   35330 C  CA  . ALA   T  6  189 ? 59.801  -203.591 74.509  1.00 132.87 ? 185 ALA   T CA  1 
ATOM   35331 C  C   . ALA   T  6  189 ? 61.195  -204.200 74.304  1.00 133.58 ? 185 ALA   T C   1 
ATOM   35332 O  O   . ALA   T  6  189 ? 61.381  -204.910 73.298  1.00 132.19 ? 185 ALA   T O   1 
ATOM   35333 C  CB  . ALA   T  6  189 ? 59.795  -202.106 74.242  1.00 133.76 ? 185 ALA   T CB  1 
ATOM   35334 N  N   . ARG   T  6  190 ? 62.124  -203.947 75.233  1.00 134.30 ? 186 ARG   T N   1 
ATOM   35335 C  CA  . ARG   T  6  190 ? 63.539  -204.409 75.160  1.00 133.22 ? 186 ARG   T CA  1 
ATOM   35336 C  C   . ARG   T  6  190 ? 63.606  -205.937 75.286  1.00 133.44 ? 186 ARG   T C   1 
ATOM   35337 O  O   . ARG   T  6  190 ? 64.483  -206.536 74.631  1.00 130.36 ? 186 ARG   T O   1 
ATOM   35338 C  CB  . ARG   T  6  190 ? 64.388  -203.733 76.241  1.00 136.99 ? 186 ARG   T CB  1 
ATOM   35339 C  CG  . ARG   T  6  190 ? 64.617  -202.246 76.009  1.00 140.07 ? 186 ARG   T CG  1 
ATOM   35340 C  CD  . ARG   T  6  190 ? 65.440  -201.610 77.115  1.00 143.34 ? 186 ARG   T CD  1 
ATOM   35341 N  NE  . ARG   T  6  190 ? 66.210  -200.463 76.648  1.00 146.26 ? 186 ARG   T NE  1 
ATOM   35342 C  CZ  . ARG   T  6  190 ? 67.403  -200.524 76.055  1.00 146.08 ? 186 ARG   T CZ  1 
ATOM   35343 N  NH1 . ARG   T  6  190 ? 67.994  -201.688 75.837  1.00 144.67 ? 186 ARG   T NH1 1 
ATOM   35344 N  NH2 . ARG   T  6  190 ? 68.004  -199.408 75.677  1.00 146.11 ? 186 ARG   T NH2 1 
ATOM   35345 N  N   . GLU   T  6  191 ? 62.732  -206.539 76.103  1.00 131.43 ? 187 GLU   T N   1 
ATOM   35346 C  CA  . GLU   T  6  191 ? 62.597  -208.017 76.242  1.00 133.48 ? 187 GLU   T CA  1 
ATOM   35347 C  C   . GLU   T  6  191 ? 62.099  -208.615 74.921  1.00 129.43 ? 187 GLU   T C   1 
ATOM   35348 O  O   . GLU   T  6  191 ? 62.693  -209.610 74.468  1.00 128.91 ? 187 GLU   T O   1 
ATOM   35349 C  CB  . GLU   T  6  191 ? 61.641  -208.397 77.377  1.00 134.81 ? 187 GLU   T CB  1 
ATOM   35350 C  CG  . GLU   T  6  191 ? 62.345  -208.810 78.659  1.00 141.76 ? 187 GLU   T CG  1 
ATOM   35351 C  CD  . GLU   T  6  191 ? 62.834  -210.251 78.688  1.00 148.54 ? 187 GLU   T CD  1 
ATOM   35352 O  OE1 . GLU   T  6  191 ? 61.993  -211.167 78.562  1.00 151.00 ? 187 GLU   T OE1 1 
ATOM   35353 O  OE2 . GLU   T  6  191 ? 64.056  -210.457 78.839  1.00 155.60 ? 187 GLU   T OE2 1 
ATOM   35354 N  N   . ALA   T  6  192 ? 61.047  -208.030 74.337  1.00 125.87 ? 188 ALA   T N   1 
ATOM   35355 C  CA  . ALA   T  6  192 ? 60.384  -208.505 73.098  1.00 123.23 ? 188 ALA   T CA  1 
ATOM   35356 C  C   . ALA   T  6  192 ? 61.376  -208.506 71.926  1.00 121.20 ? 188 ALA   T C   1 
ATOM   35357 O  O   . ALA   T  6  192 ? 61.281  -209.421 71.086  1.00 119.49 ? 188 ALA   T O   1 
ATOM   35358 C  CB  . ALA   T  6  192 ? 59.173  -207.656 72.796  1.00 121.42 ? 188 ALA   T CB  1 
ATOM   35359 N  N   . VAL   T  6  193 ? 62.278  -207.518 71.864  1.00 120.63 ? 189 VAL   T N   1 
ATOM   35360 C  CA  . VAL   T  6  193 ? 63.358  -207.428 70.831  1.00 121.27 ? 189 VAL   T CA  1 
ATOM   35361 C  C   . VAL   T  6  193 ? 64.246  -208.676 70.936  1.00 123.22 ? 189 VAL   T C   1 
ATOM   35362 O  O   . VAL   T  6  193 ? 64.555  -209.267 69.881  1.00 123.44 ? 189 VAL   T O   1 
ATOM   35363 C  CB  . VAL   T  6  193 ? 64.183  -206.132 70.967  1.00 121.39 ? 189 VAL   T CB  1 
ATOM   35364 C  CG1 . VAL   T  6  193 ? 65.459  -206.173 70.135  1.00 120.29 ? 189 VAL   T CG1 1 
ATOM   35365 C  CG2 . VAL   T  6  193 ? 63.363  -204.902 70.605  1.00 119.61 ? 189 VAL   T CG2 1 
ATOM   35366 N  N   . LYS   T  6  194 ? 64.636  -209.053 72.159  1.00 126.85 ? 190 LYS   T N   1 
ATOM   35367 C  CA  . LYS   T  6  194 ? 65.505  -210.229 72.449  1.00 127.24 ? 190 LYS   T CA  1 
ATOM   35368 C  C   . LYS   T  6  194 ? 64.765  -211.522 72.085  1.00 123.71 ? 190 LYS   T C   1 
ATOM   35369 O  O   . LYS   T  6  194 ? 65.382  -212.392 71.442  1.00 121.66 ? 190 LYS   T O   1 
ATOM   35370 C  CB  . LYS   T  6  194 ? 65.915  -210.253 73.925  1.00 131.25 ? 190 LYS   T CB  1 
ATOM   35371 C  CG  . LYS   T  6  194 ? 66.771  -209.079 74.381  1.00 133.57 ? 190 LYS   T CG  1 
ATOM   35372 C  CD  . LYS   T  6  194 ? 66.816  -208.902 75.887  1.00 136.50 ? 190 LYS   T CD  1 
ATOM   35373 C  CE  . LYS   T  6  194 ? 68.133  -209.320 76.506  1.00 137.97 ? 190 LYS   T CE  1 
ATOM   35374 N  NZ  . LYS   T  6  194 ? 68.243  -208.865 77.912  1.00 138.52 ? 190 LYS   T NZ  1 
ATOM   35375 N  N   . GLN   T  6  195 ? 63.499  -211.641 72.495  1.00 122.24 ? 191 GLN   T N   1 
ATOM   35376 C  CA  . GLN   T  6  195 ? 62.628  -212.814 72.211  1.00 124.59 ? 191 GLN   T CA  1 
ATOM   35377 C  C   . GLN   T  6  195 ? 62.472  -212.986 70.695  1.00 123.90 ? 191 GLN   T C   1 
ATOM   35378 O  O   . GLN   T  6  195 ? 62.571  -214.134 70.228  1.00 124.07 ? 191 GLN   T O   1 
ATOM   35379 C  CB  . GLN   T  6  195 ? 61.264  -212.653 72.886  1.00 123.50 ? 191 GLN   T CB  1 
ATOM   35380 C  CG  . GLN   T  6  195 ? 61.314  -212.766 74.404  1.00 125.50 ? 191 GLN   T CG  1 
ATOM   35381 C  CD  . GLN   T  6  195 ? 61.973  -214.037 74.884  1.00 128.17 ? 191 GLN   T CD  1 
ATOM   35382 O  OE1 . GLN   T  6  195 ? 62.900  -214.012 75.692  1.00 129.09 ? 191 GLN   T OE1 1 
ATOM   35383 N  NE2 . GLN   T  6  195 ? 61.498  -215.169 74.392  1.00 130.11 ? 191 GLN   T NE2 1 
ATOM   35384 N  N   . ALA   T  6  196 ? 62.239  -211.888 69.966  1.00 125.49 ? 192 ALA   T N   1 
ATOM   35385 C  CA  . ALA   T  6  196 ? 62.106  -211.858 68.488  1.00 125.26 ? 192 ALA   T CA  1 
ATOM   35386 C  C   . ALA   T  6  196 ? 63.342  -212.502 67.851  1.00 125.42 ? 192 ALA   T C   1 
ATOM   35387 O  O   . ALA   T  6  196 ? 63.169  -213.332 66.939  1.00 125.12 ? 192 ALA   T O   1 
ATOM   35388 C  CB  . ALA   T  6  196 ? 61.917  -210.442 67.999  1.00 125.46 ? 192 ALA   T CB  1 
ATOM   35389 N  N   . ALA   T  6  197 ? 64.538  -212.126 68.316  1.00 127.16 ? 193 ALA   T N   1 
ATOM   35390 C  CA  . ALA   T  6  197 ? 65.835  -212.671 67.850  1.00 129.82 ? 193 ALA   T CA  1 
ATOM   35391 C  C   . ALA   T  6  197 ? 65.889  -214.178 68.128  1.00 132.61 ? 193 ALA   T C   1 
ATOM   35392 O  O   . ALA   T  6  197 ? 66.317  -214.923 67.228  1.00 133.54 ? 193 ALA   T O   1 
ATOM   35393 C  CB  . ALA   T  6  197 ? 66.982  -211.940 68.504  1.00 132.57 ? 193 ALA   T CB  1 
ATOM   35394 N  N   . LYS   T  6  198 ? 65.452  -214.616 69.314  1.00 132.48 ? 194 LYS   T N   1 
ATOM   35395 C  CA  . LYS   T  6  198 ? 65.451  -216.053 69.703  1.00 133.14 ? 194 LYS   T CA  1 
ATOM   35396 C  C   . LYS   T  6  198 ? 64.533  -216.841 68.760  1.00 129.61 ? 194 LYS   T C   1 
ATOM   35397 O  O   . LYS   T  6  198 ? 64.955  -217.917 68.297  1.00 131.23 ? 194 LYS   T O   1 
ATOM   35398 C  CB  . LYS   T  6  198 ? 65.007  -216.252 71.157  1.00 139.50 ? 194 LYS   T CB  1 
ATOM   35399 C  CG  . LYS   T  6  198 ? 64.938  -217.711 71.599  1.00 142.39 ? 194 LYS   T CG  1 
ATOM   35400 C  CD  . LYS   T  6  198 ? 64.753  -217.902 73.088  1.00 144.28 ? 194 LYS   T CD  1 
ATOM   35401 C  CE  . LYS   T  6  198 ? 63.324  -217.698 73.542  1.00 142.08 ? 194 LYS   T CE  1 
ATOM   35402 N  NZ  . LYS   T  6  198 ? 62.457  -218.849 73.197  1.00 142.70 ? 194 LYS   T NZ  1 
ATOM   35403 N  N   . ILE   T  6  199 ? 63.332  -216.321 68.492  1.00 122.87 ? 195 ILE   T N   1 
ATOM   35404 C  CA  . ILE   T  6  199 ? 62.252  -217.026 67.738  1.00 121.50 ? 195 ILE   T CA  1 
ATOM   35405 C  C   . ILE   T  6  199 ? 62.652  -217.158 66.263  1.00 122.26 ? 195 ILE   T C   1 
ATOM   35406 O  O   . ILE   T  6  199 ? 62.370  -218.221 65.682  1.00 125.60 ? 195 ILE   T O   1 
ATOM   35407 C  CB  . ILE   T  6  199 ? 60.897  -216.312 67.923  1.00 116.50 ? 195 ILE   T CB  1 
ATOM   35408 C  CG1 . ILE   T  6  199 ? 60.425  -216.403 69.376  1.00 116.95 ? 195 ILE   T CG1 1 
ATOM   35409 C  CG2 . ILE   T  6  199 ? 59.849  -216.857 66.964  1.00 115.22 ? 195 ILE   T CG2 1 
ATOM   35410 C  CD1 . ILE   T  6  199 ? 59.489  -215.298 69.788  1.00 115.42 ? 195 ILE   T CD1 1 
ATOM   35411 N  N   . ILE   T  6  200 ? 63.273  -216.129 65.677  1.00 121.95 ? 196 ILE   T N   1 
ATOM   35412 C  CA  . ILE   T  6  200 ? 63.759  -216.154 64.263  1.00 125.19 ? 196 ILE   T CA  1 
ATOM   35413 C  C   . ILE   T  6  200 ? 64.848  -217.228 64.131  1.00 126.87 ? 196 ILE   T C   1 
ATOM   35414 O  O   . ILE   T  6  200 ? 64.835  -217.949 63.113  1.00 125.86 ? 196 ILE   T O   1 
ATOM   35415 C  CB  . ILE   T  6  200 ? 64.251  -214.764 63.803  1.00 125.46 ? 196 ILE   T CB  1 
ATOM   35416 C  CG1 . ILE   T  6  200 ? 63.089  -213.781 63.611  1.00 124.36 ? 196 ILE   T CG1 1 
ATOM   35417 C  CG2 . ILE   T  6  200 ? 65.107  -214.870 62.547  1.00 127.87 ? 196 ILE   T CG2 1 
ATOM   35418 C  CD1 . ILE   T  6  200 ? 62.172  -214.103 62.446  1.00 123.53 ? 196 ILE   T CD1 1 
ATOM   35419 N  N   . TYR   T  6  201 ? 65.749  -217.329 65.116  1.00 129.89 ? 197 TYR   T N   1 
ATOM   35420 C  CA  . TYR   T  6  201 ? 66.838  -218.345 65.173  1.00 133.71 ? 197 TYR   T CA  1 
ATOM   35421 C  C   . TYR   T  6  201 ? 66.240  -219.753 65.317  1.00 134.47 ? 197 TYR   T C   1 
ATOM   35422 O  O   . TYR   T  6  201 ? 66.752  -220.683 64.665  1.00 135.27 ? 197 TYR   T O   1 
ATOM   35423 C  CB  . TYR   T  6  201 ? 67.829  -218.038 66.302  1.00 134.02 ? 197 TYR   T CB  1 
ATOM   35424 C  CG  . TYR   T  6  201 ? 69.011  -217.194 65.892  1.00 132.88 ? 197 TYR   T CG  1 
ATOM   35425 C  CD1 . TYR   T  6  201 ? 68.948  -215.810 65.909  1.00 130.80 ? 197 TYR   T CD1 1 
ATOM   35426 C  CD2 . TYR   T  6  201 ? 70.197  -217.779 65.477  1.00 134.42 ? 197 TYR   T CD2 1 
ATOM   35427 C  CE1 . TYR   T  6  201 ? 70.028  -215.030 65.531  1.00 131.02 ? 197 TYR   T CE1 1 
ATOM   35428 C  CE2 . TYR   T  6  201 ? 71.287  -217.014 65.094  1.00 133.85 ? 197 TYR   T CE2 1 
ATOM   35429 C  CZ  . TYR   T  6  201 ? 71.203  -215.634 65.122  1.00 132.41 ? 197 TYR   T CZ  1 
ATOM   35430 O  OH  . TYR   T  6  201 ? 72.273  -214.874 64.749  1.00 134.05 ? 197 TYR   T OH  1 
ATOM   35431 N  N   . LEU   T  6  202 ? 65.197  -219.907 66.142  1.00 133.78 ? 198 LEU   T N   1 
ATOM   35432 C  CA  . LEU   T  6  202 ? 64.493  -221.203 66.364  1.00 137.45 ? 198 LEU   T CA  1 
ATOM   35433 C  C   . LEU   T  6  202 ? 63.686  -221.585 65.116  1.00 135.89 ? 198 LEU   T C   1 
ATOM   35434 O  O   . LEU   T  6  202 ? 63.641  -222.786 64.799  1.00 142.10 ? 198 LEU   T O   1 
ATOM   35435 C  CB  . LEU   T  6  202 ? 63.595  -221.106 67.604  1.00 140.84 ? 198 LEU   T CB  1 
ATOM   35436 C  CG  . LEU   T  6  202 ? 64.139  -221.774 68.868  1.00 146.52 ? 198 LEU   T CG  1 
ATOM   35437 C  CD1 . LEU   T  6  202 ? 65.544  -221.290 69.201  1.00 150.50 ? 198 LEU   T CD1 1 
ATOM   35438 C  CD2 . LEU   T  6  202 ? 63.207  -221.537 70.045  1.00 147.47 ? 198 LEU   T CD2 1 
ATOM   35439 N  N   . ALA   T  6  203 ? 63.086  -220.607 64.431  1.00 133.43 ? 199 ALA   T N   1 
ATOM   35440 C  CA  . ALA   T  6  203 ? 62.273  -220.808 63.206  1.00 132.76 ? 199 ALA   T CA  1 
ATOM   35441 C  C   . ALA   T  6  203 ? 63.176  -221.016 61.982  1.00 132.85 ? 199 ALA   T C   1 
ATOM   35442 O  O   . ALA   T  6  203 ? 62.637  -221.386 60.921  1.00 131.85 ? 199 ALA   T O   1 
ATOM   35443 C  CB  . ALA   T  6  203 ? 61.351  -219.634 62.998  1.00 132.48 ? 199 ALA   T CB  1 
ATOM   35444 N  N   . HIS   T  6  204 ? 64.486  -220.770 62.113  1.00 136.65 ? 200 HIS   T N   1 
ATOM   35445 C  CA  . HIS   T  6  204 ? 65.497  -220.948 61.034  1.00 143.08 ? 200 HIS   T CA  1 
ATOM   35446 C  C   . HIS   T  6  204 ? 65.815  -222.438 60.827  1.00 146.39 ? 200 HIS   T C   1 
ATOM   35447 O  O   . HIS   T  6  204 ? 66.380  -222.768 59.765  1.00 153.11 ? 200 HIS   T O   1 
ATOM   35448 C  CB  . HIS   T  6  204 ? 66.769  -220.139 61.332  1.00 143.05 ? 200 HIS   T CB  1 
ATOM   35449 C  CG  . HIS   T  6  204 ? 67.808  -220.260 60.268  1.00 143.65 ? 200 HIS   T CG  1 
ATOM   35450 N  ND1 . HIS   T  6  204 ? 67.612  -219.770 58.994  1.00 141.13 ? 200 HIS   T ND1 1 
ATOM   35451 C  CD2 . HIS   T  6  204 ? 69.034  -220.829 60.272  1.00 145.67 ? 200 HIS   T CD2 1 
ATOM   35452 C  CE1 . HIS   T  6  204 ? 68.674  -220.021 58.258  1.00 141.85 ? 200 HIS   T CE1 1 
ATOM   35453 N  NE2 . HIS   T  6  204 ? 69.563  -220.670 59.019  1.00 143.42 ? 200 HIS   T NE2 1 
ATOM   35454 N  N   . GLU   T  6  205 ? 65.474  -223.299 61.796  1.00 150.85 ? 201 GLU   T N   1 
ATOM   35455 C  CA  . GLU   T  6  205 ? 65.683  -224.774 61.731  1.00 152.00 ? 201 GLU   T CA  1 
ATOM   35456 C  C   . GLU   T  6  205 ? 64.952  -225.368 60.520  1.00 148.36 ? 201 GLU   T C   1 
ATOM   35457 O  O   . GLU   T  6  205 ? 65.412  -226.405 60.008  1.00 143.90 ? 201 GLU   T O   1 
ATOM   35458 C  CB  . GLU   T  6  205 ? 65.189  -225.453 63.011  1.00 154.53 ? 201 GLU   T CB  1 
ATOM   35459 C  CG  . GLU   T  6  205 ? 66.027  -225.137 64.237  1.00 159.59 ? 201 GLU   T CG  1 
ATOM   35460 C  CD  . GLU   T  6  205 ? 67.512  -225.412 64.077  1.00 161.99 ? 201 GLU   T CD  1 
ATOM   35461 O  OE1 . GLU   T  6  205 ? 68.314  -224.502 64.367  1.00 163.73 ? 201 GLU   T OE1 1 
ATOM   35462 O  OE2 . GLU   T  6  205 ? 67.863  -226.532 63.658  1.00 170.29 ? 201 GLU   T OE2 1 
ATOM   35463 N  N   . ASP   T  6  206 ? 63.858  -224.733 60.086  1.00 148.19 ? 202 ASP   T N   1 
ATOM   35464 C  CA  . ASP   T  6  206 ? 63.006  -225.181 58.951  1.00 147.97 ? 202 ASP   T CA  1 
ATOM   35465 C  C   . ASP   T  6  206 ? 63.534  -224.612 57.623  1.00 147.55 ? 202 ASP   T C   1 
ATOM   35466 O  O   . ASP   T  6  206 ? 62.824  -224.757 56.606  1.00 141.09 ? 202 ASP   T O   1 
ATOM   35467 C  CB  . ASP   T  6  206 ? 61.549  -224.770 59.190  1.00 148.43 ? 202 ASP   T CB  1 
ATOM   35468 C  CG  . ASP   T  6  206 ? 60.965  -225.303 60.489  1.00 148.65 ? 202 ASP   T CG  1 
ATOM   35469 O  OD1 . ASP   T  6  206 ? 61.589  -226.199 61.094  1.00 148.78 ? 202 ASP   T OD1 1 
ATOM   35470 O  OD2 . ASP   T  6  206 ? 59.893  -224.811 60.892  1.00 150.54 ? 202 ASP   T OD2 1 
ATOM   35471 N  N   . ASN   T  6  207 ? 64.731  -224.009 57.623  1.00 149.83 ? 203 ASN   T N   1 
ATOM   35472 C  CA  . ASN   T  6  207 ? 65.319  -223.296 56.455  1.00 150.09 ? 203 ASN   T CA  1 
ATOM   35473 C  C   . ASN   T  6  207 ? 66.852  -223.280 56.581  1.00 151.53 ? 203 ASN   T C   1 
ATOM   35474 O  O   . ASN   T  6  207 ? 67.470  -222.264 56.193  1.00 149.76 ? 203 ASN   T O   1 
ATOM   35475 C  CB  . ASN   T  6  207 ? 64.753  -221.871 56.367  1.00 148.42 ? 203 ASN   T CB  1 
ATOM   35476 C  CG  . ASN   T  6  207 ? 64.236  -221.476 54.999  1.00 146.59 ? 203 ASN   T CG  1 
ATOM   35477 O  OD1 . ASN   T  6  207 ? 63.248  -220.750 54.902  1.00 141.18 ? 203 ASN   T OD1 1 
ATOM   35478 N  ND2 . ASN   T  6  207 ? 64.894  -221.926 53.941  1.00 147.99 ? 203 ASN   T ND2 1 
ATOM   35479 N  N   . LYS   T  6  208 ? 67.445  -224.374 57.073  1.00 152.26 ? 204 LYS   T N   1 
ATOM   35480 C  CA  . LYS   T  6  208 ? 68.801  -224.383 57.694  1.00 152.87 ? 204 LYS   T CA  1 
ATOM   35481 C  C   . LYS   T  6  208 ? 69.910  -224.682 56.672  1.00 153.04 ? 204 LYS   T C   1 
ATOM   35482 O  O   . LYS   T  6  208 ? 71.077  -224.742 57.110  1.00 156.42 ? 204 LYS   T O   1 
ATOM   35483 C  CB  . LYS   T  6  208 ? 68.849  -225.389 58.851  1.00 155.49 ? 204 LYS   T CB  1 
ATOM   35484 C  CG  . LYS   T  6  208 ? 68.802  -226.859 58.452  1.00 156.02 ? 204 LYS   T CG  1 
ATOM   35485 C  CD  . LYS   T  6  208 ? 68.354  -227.775 59.568  1.00 157.41 ? 204 LYS   T CD  1 
ATOM   35486 C  CE  . LYS   T  6  208 ? 69.343  -227.859 60.710  1.00 160.52 ? 204 LYS   T CE  1 
ATOM   35487 N  NZ  . LYS   T  6  208 ? 68.946  -228.898 61.690  1.00 162.96 ? 204 LYS   T NZ  1 
ATOM   35488 N  N   . GLU   T  6  209 ? 69.594  -224.853 55.380  1.00 150.14 ? 205 GLU   T N   1 
ATOM   35489 C  CA  . GLU   T  6  209 ? 70.622  -225.080 54.322  1.00 154.59 ? 205 GLU   T CA  1 
ATOM   35490 C  C   . GLU   T  6  209 ? 71.506  -223.834 54.227  1.00 153.15 ? 205 GLU   T C   1 
ATOM   35491 O  O   . GLU   T  6  209 ? 72.710  -223.932 54.538  1.00 150.60 ? 205 GLU   T O   1 
ATOM   35492 C  CB  . GLU   T  6  209 ? 70.003  -225.381 52.954  1.00 160.44 ? 205 GLU   T CB  1 
ATOM   35493 C  CG  . GLU   T  6  209 ? 69.409  -226.774 52.838  1.00 161.66 ? 205 GLU   T CG  1 
ATOM   35494 C  CD  . GLU   T  6  209 ? 67.920  -226.861 53.126  1.00 162.34 ? 205 GLU   T CD  1 
ATOM   35495 O  OE1 . GLU   T  6  209 ? 67.285  -227.820 52.643  1.00 162.20 ? 205 GLU   T OE1 1 
ATOM   35496 O  OE2 . GLU   T  6  209 ? 67.398  -225.971 53.832  1.00 158.11 ? 205 GLU   T OE2 1 
ATOM   35497 N  N   . LYS   T  6  210 ? 70.911  -222.712 53.815  1.00 152.85 ? 206 LYS   T N   1 
ATOM   35498 C  CA  . LYS   T  6  210 ? 71.541  -221.366 53.805  1.00 150.92 ? 206 LYS   T CA  1 
ATOM   35499 C  C   . LYS   T  6  210 ? 71.468  -220.782 55.219  1.00 150.00 ? 206 LYS   T C   1 
ATOM   35500 O  O   . LYS   T  6  210 ? 70.386  -220.877 55.831  1.00 145.38 ? 206 LYS   T O   1 
ATOM   35501 C  CB  . LYS   T  6  210 ? 70.805  -220.437 52.834  1.00 148.29 ? 206 LYS   T CB  1 
ATOM   35502 C  CG  . LYS   T  6  210 ? 70.748  -220.901 51.384  1.00 147.14 ? 206 LYS   T CG  1 
ATOM   35503 C  CD  . LYS   T  6  210 ? 71.944  -220.478 50.554  1.00 148.84 ? 206 LYS   T CD  1 
ATOM   35504 C  CE  . LYS   T  6  210 ? 73.041  -221.520 50.496  1.00 152.20 ? 206 LYS   T CE  1 
ATOM   35505 N  NZ  . LYS   T  6  210 ? 72.726  -222.591 49.521  1.00 154.66 ? 206 LYS   T NZ  1 
ATOM   35506 N  N   . ASP   T  6  211 ? 72.567  -220.205 55.717  1.00 150.88 ? 207 ASP   T N   1 
ATOM   35507 C  CA  . ASP   T  6  211 ? 72.563  -219.379 56.955  1.00 149.18 ? 207 ASP   T CA  1 
ATOM   35508 C  C   . ASP   T  6  211 ? 71.970  -218.015 56.580  1.00 146.71 ? 207 ASP   T C   1 
ATOM   35509 O  O   . ASP   T  6  211 ? 71.861  -217.739 55.366  1.00 144.96 ? 207 ASP   T O   1 
ATOM   35510 C  CB  . ASP   T  6  211 ? 73.946  -219.306 57.609  1.00 153.69 ? 207 ASP   T CB  1 
ATOM   35511 C  CG  . ASP   T  6  211 ? 75.022  -218.650 56.762  1.00 158.54 ? 207 ASP   T CG  1 
ATOM   35512 O  OD1 . ASP   T  6  211 ? 74.870  -218.639 55.523  1.00 160.43 ? 207 ASP   T OD1 1 
ATOM   35513 O  OD2 . ASP   T  6  211 ? 76.007  -218.161 57.349  1.00 161.71 ? 207 ASP   T OD2 1 
ATOM   35514 N  N   . PHE   T  6  212 ? 71.597  -217.204 57.573  1.00 144.37 ? 208 PHE   T N   1 
ATOM   35515 C  CA  . PHE   T  6  212 ? 70.685  -216.043 57.403  1.00 139.93 ? 208 PHE   T CA  1 
ATOM   35516 C  C   . PHE   T  6  212 ? 71.246  -214.793 58.085  1.00 138.57 ? 208 PHE   T C   1 
ATOM   35517 O  O   . PHE   T  6  212 ? 72.266  -214.883 58.798  1.00 145.54 ? 208 PHE   T O   1 
ATOM   35518 C  CB  . PHE   T  6  212 ? 69.300  -216.375 57.964  1.00 137.65 ? 208 PHE   T CB  1 
ATOM   35519 C  CG  . PHE   T  6  212 ? 69.221  -216.416 59.470  1.00 137.23 ? 208 PHE   T CG  1 
ATOM   35520 C  CD1 . PHE   T  6  212 ? 69.776  -217.468 60.183  1.00 139.79 ? 208 PHE   T CD1 1 
ATOM   35521 C  CD2 . PHE   T  6  212 ? 68.589  -215.403 60.174  1.00 134.71 ? 208 PHE   T CD2 1 
ATOM   35522 C  CE1 . PHE   T  6  212 ? 69.702  -217.504 61.567  1.00 140.89 ? 208 PHE   T CE1 1 
ATOM   35523 C  CE2 . PHE   T  6  212 ? 68.516  -215.440 61.558  1.00 135.99 ? 208 PHE   T CE2 1 
ATOM   35524 C  CZ  . PHE   T  6  212 ? 69.072  -216.490 62.252  1.00 138.69 ? 208 PHE   T CZ  1 
ATOM   35525 N  N   . GLU   T  6  213 ? 70.571  -213.661 57.856  1.00 135.91 ? 209 GLU   T N   1 
ATOM   35526 C  CA  . GLU   T  6  213 ? 70.829  -212.347 58.502  1.00 132.11 ? 209 GLU   T CA  1 
ATOM   35527 C  C   . GLU   T  6  213 ? 69.559  -211.904 59.237  1.00 122.73 ? 209 GLU   T C   1 
ATOM   35528 O  O   . GLU   T  6  213 ? 68.477  -211.921 58.618  1.00 114.89 ? 209 GLU   T O   1 
ATOM   35529 C  CB  . GLU   T  6  213 ? 71.245  -211.315 57.454  1.00 134.07 ? 209 GLU   T CB  1 
ATOM   35530 C  CG  . GLU   T  6  213 ? 71.708  -209.999 58.049  1.00 137.22 ? 209 GLU   T CG  1 
ATOM   35531 C  CD  . GLU   T  6  213 ? 72.305  -209.041 57.033  1.00 138.76 ? 209 GLU   T CD  1 
ATOM   35532 O  OE1 . GLU   T  6  213 ? 73.118  -209.495 56.203  1.00 145.31 ? 209 GLU   T OE1 1 
ATOM   35533 O  OE2 . GLU   T  6  213 ? 71.949  -207.846 57.067  1.00 136.00 ? 209 GLU   T OE2 1 
ATOM   35534 N  N   . LEU   T  6  214 ? 69.692  -211.531 60.511  1.00 122.33 ? 210 LEU   T N   1 
ATOM   35535 C  CA  . LEU   T  6  214 ? 68.559  -211.115 61.377  1.00 124.81 ? 210 LEU   T CA  1 
ATOM   35536 C  C   . LEU   T  6  214 ? 68.307  -209.617 61.181  1.00 121.38 ? 210 LEU   T C   1 
ATOM   35537 O  O   . LEU   T  6  214 ? 69.290  -208.854 61.120  1.00 125.38 ? 210 LEU   T O   1 
ATOM   35538 C  CB  . LEU   T  6  214 ? 68.897  -211.443 62.834  1.00 127.13 ? 210 LEU   T CB  1 
ATOM   35539 C  CG  . LEU   T  6  214 ? 67.893  -210.955 63.877  1.00 129.35 ? 210 LEU   T CG  1 
ATOM   35540 C  CD1 . LEU   T  6  214 ? 66.530  -211.606 63.683  1.00 129.04 ? 210 LEU   T CD1 1 
ATOM   35541 C  CD2 . LEU   T  6  214 ? 68.417  -211.220 65.279  1.00 131.18 ? 210 LEU   T CD2 1 
ATOM   35542 N  N   . GLU   T  6  215 ? 67.034  -209.229 61.076  1.00 119.57 ? 211 GLU   T N   1 
ATOM   35543 C  CA  . GLU   T  6  215 ? 66.586  -207.817 60.960  1.00 117.66 ? 211 GLU   T CA  1 
ATOM   35544 C  C   . GLU   T  6  215 ? 65.418  -207.599 61.927  1.00 114.41 ? 211 GLU   T C   1 
ATOM   35545 O  O   . GLU   T  6  215 ? 64.429  -208.349 61.827  1.00 109.25 ? 211 GLU   T O   1 
ATOM   35546 C  CB  . GLU   T  6  215 ? 66.188  -207.508 59.516  1.00 118.39 ? 211 GLU   T CB  1 
ATOM   35547 C  CG  . GLU   T  6  215 ? 65.943  -206.032 59.252  1.00 119.32 ? 211 GLU   T CG  1 
ATOM   35548 C  CD  . GLU   T  6  215 ? 65.727  -205.687 57.788  1.00 119.66 ? 211 GLU   T CD  1 
ATOM   35549 O  OE1 . GLU   T  6  215 ? 64.624  -205.210 57.449  1.00 118.71 ? 211 GLU   T OE1 1 
ATOM   35550 O  OE2 . GLU   T  6  215 ? 66.664  -205.894 56.991  1.00 119.26 ? 211 GLU   T OE2 1 
ATOM   35551 N  N   . ILE   T  6  216 ? 65.546  -206.623 62.833  1.00 115.99 ? 212 ILE   T N   1 
ATOM   35552 C  CA  . ILE   T  6  216 ? 64.520  -206.277 63.862  1.00 117.98 ? 212 ILE   T CA  1 
ATOM   35553 C  C   . ILE   T  6  216 ? 64.201  -204.783 63.760  1.00 117.62 ? 212 ILE   T C   1 
ATOM   35554 O  O   . ILE   T  6  216 ? 65.125  -203.995 63.476  1.00 121.87 ? 212 ILE   T O   1 
ATOM   35555 C  CB  . ILE   T  6  216 ? 64.993  -206.643 65.285  1.00 117.26 ? 212 ILE   T CB  1 
ATOM   35556 C  CG1 . ILE   T  6  216 ? 65.573  -208.058 65.360  1.00 119.40 ? 212 ILE   T CG1 1 
ATOM   35557 C  CG2 . ILE   T  6  216 ? 63.864  -206.445 66.288  1.00 117.00 ? 212 ILE   T CG2 1 
ATOM   35558 C  CD1 . ILE   T  6  216 ? 66.295  -208.355 66.654  1.00 120.19 ? 212 ILE   T CD1 1 
ATOM   35559 N  N   . SER   T  6  217 ? 62.935  -204.427 63.993  1.00 120.61 ? 213 SER   T N   1 
ATOM   35560 C  CA  . SER   T  6  217 ? 62.446  -203.037 64.191  1.00 120.53 ? 213 SER   T CA  1 
ATOM   35561 C  C   . SER   T  6  217 ? 61.459  -203.019 65.364  1.00 120.96 ? 213 SER   T C   1 
ATOM   35562 O  O   . SER   T  6  217 ? 61.079  -204.116 65.831  1.00 119.76 ? 213 SER   T O   1 
ATOM   35563 C  CB  . SER   T  6  217 ? 61.821  -202.495 62.931  1.00 121.63 ? 213 SER   T CB  1 
ATOM   35564 O  OG  . SER   T  6  217 ? 60.575  -203.126 62.672  1.00 119.75 ? 213 SER   T OG  1 
ATOM   35565 N  N   . TRP   T  6  218 ? 61.056  -201.828 65.817  1.00 119.76 ? 214 TRP   T N   1 
ATOM   35566 C  CA  . TRP   T  6  218 ? 60.133  -201.657 66.972  1.00 116.35 ? 214 TRP   T CA  1 
ATOM   35567 C  C   . TRP   T  6  218 ? 59.513  -200.255 66.995  1.00 112.77 ? 214 TRP   T C   1 
ATOM   35568 O  O   . TRP   T  6  218 ? 60.164  -199.293 66.541  1.00 106.62 ? 214 TRP   T O   1 
ATOM   35569 C  CB  . TRP   T  6  218 ? 60.839  -201.993 68.297  1.00 116.73 ? 214 TRP   T CB  1 
ATOM   35570 C  CG  . TRP   T  6  218 ? 62.015  -201.135 68.660  1.00 116.56 ? 214 TRP   T CG  1 
ATOM   35571 C  CD1 . TRP   T  6  218 ? 62.796  -200.382 67.830  1.00 116.84 ? 214 TRP   T CD1 1 
ATOM   35572 C  CD2 . TRP   T  6  218 ? 62.583  -200.986 69.973  1.00 117.81 ? 214 TRP   T CD2 1 
ATOM   35573 N  NE1 . TRP   T  6  218 ? 63.787  -199.757 68.536  1.00 117.33 ? 214 TRP   T NE1 1 
ATOM   35574 C  CE2 . TRP   T  6  218 ? 63.685  -200.111 69.854  1.00 118.01 ? 214 TRP   T CE2 1 
ATOM   35575 C  CE3 . TRP   T  6  218 ? 62.263  -201.497 71.237  1.00 118.35 ? 214 TRP   T CE3 1 
ATOM   35576 C  CZ2 . TRP   T  6  218 ? 64.463  -199.739 70.950  1.00 118.97 ? 214 TRP   T CZ2 1 
ATOM   35577 C  CZ3 . TRP   T  6  218 ? 63.031  -201.129 72.320  1.00 119.56 ? 214 TRP   T CZ3 1 
ATOM   35578 C  CH2 . TRP   T  6  218 ? 64.117  -200.263 72.176  1.00 120.24 ? 214 TRP   T CH2 1 
ATOM   35579 N  N   . CYS   T  6  219 ? 58.271  -200.183 67.482  1.00 112.50 ? 215 CYS   T N   1 
ATOM   35580 C  CA  . CYS   T  6  219 ? 57.580  -198.954 67.948  1.00 114.01 ? 215 CYS   T CA  1 
ATOM   35581 C  C   . CYS   T  6  219 ? 57.265  -199.131 69.434  1.00 113.81 ? 215 CYS   T C   1 
ATOM   35582 O  O   . CYS   T  6  219 ? 56.692  -200.176 69.780  1.00 117.30 ? 215 CYS   T O   1 
ATOM   35583 C  CB  . CYS   T  6  219 ? 56.280  -198.708 67.192  1.00 117.16 ? 215 CYS   T CB  1 
ATOM   35584 S  SG  . CYS   T  6  219 ? 56.458  -198.815 65.395  1.00 127.09 ? 215 CYS   T SG  1 
ATOM   35585 N  N   . SER   T  6  220 ? 57.648  -198.165 70.271  1.00 112.56 ? 216 SER   T N   1 
ATOM   35586 C  CA  . SER   T  6  220 ? 57.398  -198.169 71.736  1.00 111.50 ? 216 SER   T CA  1 
ATOM   35587 C  C   . SER   T  6  220 ? 57.162  -196.737 72.225  1.00 110.93 ? 216 SER   T C   1 
ATOM   35588 O  O   . SER   T  6  220 ? 57.955  -195.849 71.856  1.00 106.15 ? 216 SER   T O   1 
ATOM   35589 C  CB  . SER   T  6  220 ? 58.537  -198.824 72.470  1.00 110.98 ? 216 SER   T CB  1 
ATOM   35590 O  OG  . SER   T  6  220 ? 58.380  -198.704 73.876  1.00 108.69 ? 216 SER   T OG  1 
ATOM   35591 N  N   . LEU   T  6  221 ? 56.112  -196.541 73.028  1.00 114.61 ? 217 LEU   T N   1 
ATOM   35592 C  CA  . LEU   T  6  221 ? 55.690  -195.221 73.571  1.00 119.11 ? 217 LEU   T CA  1 
ATOM   35593 C  C   . LEU   T  6  221 ? 56.813  -194.634 74.440  1.00 123.85 ? 217 LEU   T C   1 
ATOM   35594 O  O   . LEU   T  6  221 ? 56.954  -193.394 74.450  1.00 131.41 ? 217 LEU   T O   1 
ATOM   35595 C  CB  . LEU   T  6  221 ? 54.392  -195.403 74.367  1.00 125.65 ? 217 LEU   T CB  1 
ATOM   35596 C  CG  . LEU   T  6  221 ? 53.764  -194.133 74.947  1.00 127.29 ? 217 LEU   T CG  1 
ATOM   35597 C  CD1 . LEU   T  6  221 ? 53.365  -193.154 73.851  1.00 127.08 ? 217 LEU   T CD1 1 
ATOM   35598 C  CD2 . LEU   T  6  221 ? 52.561  -194.479 75.812  1.00 127.93 ? 217 LEU   T CD2 1 
ATOM   35599 N  N   . SER   T  6  222 ? 57.582  -195.483 75.132  1.00 116.01 ? 218 SER   T N   1 
ATOM   35600 C  CA  . SER   T  6  222 ? 58.676  -195.070 76.052  1.00 116.39 ? 218 SER   T CA  1 
ATOM   35601 C  C   . SER   T  6  222 ? 60.040  -195.146 75.354  1.00 116.14 ? 218 SER   T C   1 
ATOM   35602 O  O   . SER   T  6  222 ? 60.824  -194.191 75.506  1.00 122.23 ? 218 SER   T O   1 
ATOM   35603 C  CB  . SER   T  6  222 ? 58.665  -195.897 77.309  1.00 115.53 ? 218 SER   T CB  1 
ATOM   35604 O  OG  . SER   T  6  222 ? 58.875  -197.269 77.013  1.00 113.45 ? 218 SER   T OG  1 
ATOM   35605 N  N   . GLU   T  6  223 ? 60.318  -196.234 74.629  1.00 116.12 ? 219 GLU   T N   1 
ATOM   35606 C  CA  . GLU   T  6  223 ? 61.673  -196.543 74.093  1.00 117.64 ? 219 GLU   T CA  1 
ATOM   35607 C  C   . GLU   T  6  223 ? 61.951  -195.751 72.807  1.00 115.71 ? 219 GLU   T C   1 
ATOM   35608 O  O   . GLU   T  6  223 ? 63.093  -195.277 72.671  1.00 116.95 ? 219 GLU   T O   1 
ATOM   35609 C  CB  . GLU   T  6  223 ? 61.833  -198.047 73.865  1.00 119.57 ? 219 GLU   T CB  1 
ATOM   35610 C  CG  . GLU   T  6  223 ? 61.880  -198.848 75.153  1.00 123.40 ? 219 GLU   T CG  1 
ATOM   35611 C  CD  . GLU   T  6  223 ? 63.133  -198.635 75.987  1.00 126.08 ? 219 GLU   T CD  1 
ATOM   35612 O  OE1 . GLU   T  6  223 ? 63.047  -198.773 77.223  1.00 128.63 ? 219 GLU   T OE1 1 
ATOM   35613 O  OE2 . GLU   T  6  223 ? 64.191  -198.332 75.398  1.00 128.49 ? 219 GLU   T OE2 1 
ATOM   35614 N  N   . THR   T  6  224 ? 60.978  -195.627 71.893  1.00 115.98 ? 220 THR   T N   1 
ATOM   35615 C  CA  . THR   T  6  224 ? 61.149  -194.946 70.574  1.00 117.04 ? 220 THR   T CA  1 
ATOM   35616 C  C   . THR   T  6  224 ? 60.202  -193.747 70.429  1.00 116.98 ? 220 THR   T C   1 
ATOM   35617 O  O   . THR   T  6  224 ? 60.152  -193.181 69.316  1.00 119.75 ? 220 THR   T O   1 
ATOM   35618 C  CB  . THR   T  6  224 ? 60.939  -195.912 69.401  1.00 115.80 ? 220 THR   T CB  1 
ATOM   35619 O  OG1 . THR   T  6  224 ? 59.584  -196.363 69.421  1.00 111.23 ? 220 THR   T OG1 1 
ATOM   35620 C  CG2 . THR   T  6  224 ? 61.888  -197.090 69.436  1.00 117.72 ? 220 THR   T CG2 1 
ATOM   35621 N  N   . ASN   T  6  225 ? 59.484  -193.370 71.493  1.00 114.95 ? 221 ASN   T N   1 
ATOM   35622 C  CA  . ASN   T  6  225 ? 58.630  -192.152 71.539  1.00 111.81 ? 221 ASN   T CA  1 
ATOM   35623 C  C   . ASN   T  6  225 ? 57.431  -192.317 70.590  1.00 107.17 ? 221 ASN   T C   1 
ATOM   35624 O  O   . ASN   T  6  225 ? 56.909  -191.293 70.114  1.00 103.01 ? 221 ASN   T O   1 
ATOM   35625 C  CB  . ASN   T  6  225 ? 59.459  -190.900 71.226  1.00 115.75 ? 221 ASN   T CB  1 
ATOM   35626 C  CG  . ASN   T  6  225 ? 59.149  -189.738 72.146  1.00 118.03 ? 221 ASN   T CG  1 
ATOM   35627 O  OD1 . ASN   T  6  225 ? 59.914  -189.451 73.064  1.00 125.37 ? 221 ASN   T OD1 1 
ATOM   35628 N  ND2 . ASN   T  6  225 ? 58.024  -189.078 71.922  1.00 119.98 ? 221 ASN   T ND2 1 
ATOM   35629 N  N   . GLY   T  6  226 ? 57.007  -193.559 70.332  1.00 101.75 ? 222 GLY   T N   1 
ATOM   35630 C  CA  . GLY   T  6  226 ? 55.815  -193.884 69.523  1.00 101.06 ? 222 GLY   T CA  1 
ATOM   35631 C  C   . GLY   T  6  226 ? 56.118  -193.996 68.038  1.00 101.22 ? 222 GLY   T C   1 
ATOM   35632 O  O   . GLY   T  6  226 ? 55.190  -194.348 67.285  1.00 104.39 ? 222 GLY   T O   1 
ATOM   35633 N  N   . LEU   T  6  227 ? 57.360  -193.720 67.624  1.00 101.47 ? 223 LEU   T N   1 
ATOM   35634 C  CA  . LEU   T  6  227 ? 57.787  -193.723 66.199  1.00 100.09 ? 223 LEU   T CA  1 
ATOM   35635 C  C   . LEU   T  6  227 ? 58.443  -195.067 65.869  1.00 99.69  ? 223 LEU   T C   1 
ATOM   35636 O  O   . LEU   T  6  227 ? 59.006  -195.693 66.786  1.00 97.37  ? 223 LEU   T O   1 
ATOM   35637 C  CB  . LEU   T  6  227 ? 58.759  -192.564 65.951  1.00 100.64 ? 223 LEU   T CB  1 
ATOM   35638 C  CG  . LEU   T  6  227 ? 58.236  -191.167 66.287  1.00 100.12 ? 223 LEU   T CG  1 
ATOM   35639 C  CD1 . LEU   T  6  227 ? 59.331  -190.128 66.103  1.00 101.73 ? 223 LEU   T CD1 1 
ATOM   35640 C  CD2 . LEU   T  6  227 ? 57.022  -190.813 65.441  1.00 99.94  ? 223 LEU   T CD2 1 
ATOM   35641 N  N   . HIS   T  6  228 ? 58.366  -195.480 64.601  1.00 99.63  ? 224 HIS   T N   1 
ATOM   35642 C  CA  . HIS   T  6  228 ? 59.019  -196.701 64.061  1.00 101.85 ? 224 HIS   T CA  1 
ATOM   35643 C  C   . HIS   T  6  228 ? 60.522  -196.451 63.909  1.00 105.28 ? 224 HIS   T C   1 
ATOM   35644 O  O   . HIS   T  6  228 ? 60.893  -195.435 63.299  1.00 108.51 ? 224 HIS   T O   1 
ATOM   35645 C  CB  . HIS   T  6  228 ? 58.395  -197.119 62.722  1.00 100.55 ? 224 HIS   T CB  1 
ATOM   35646 C  CG  . HIS   T  6  228 ? 58.913  -198.422 62.213  1.00 100.15 ? 224 HIS   T CG  1 
ATOM   35647 N  ND1 . HIS   T  6  228 ? 59.925  -198.503 61.276  1.00 98.75  ? 224 HIS   T ND1 1 
ATOM   35648 C  CD2 . HIS   T  6  228 ? 58.581  -199.693 62.524  1.00 98.80  ? 224 HIS   T CD2 1 
ATOM   35649 C  CE1 . HIS   T  6  228 ? 60.186  -199.769 61.024  1.00 98.83  ? 224 HIS   T CE1 1 
ATOM   35650 N  NE2 . HIS   T  6  228 ? 59.374  -200.518 61.776  1.00 97.34  ? 224 HIS   T NE2 1 
ATOM   35651 N  N   . LYS   T  6  229 ? 61.347  -197.352 64.442  1.00 108.77 ? 225 LYS   T N   1 
ATOM   35652 C  CA  . LYS   T  6  229 ? 62.828  -197.288 64.349  1.00 112.74 ? 225 LYS   T CA  1 
ATOM   35653 C  C   . LYS   T  6  229 ? 63.366  -198.701 64.108  1.00 111.23 ? 225 LYS   T C   1 
ATOM   35654 O  O   . LYS   T  6  229 ? 62.773  -199.658 64.639  1.00 107.78 ? 225 LYS   T O   1 
ATOM   35655 C  CB  . LYS   T  6  229 ? 63.417  -196.679 65.625  1.00 114.56 ? 225 LYS   T CB  1 
ATOM   35656 C  CG  . LYS   T  6  229 ? 63.084  -195.212 65.864  1.00 116.88 ? 225 LYS   T CG  1 
ATOM   35657 C  CD  . LYS   T  6  229 ? 63.915  -194.585 66.966  1.00 120.41 ? 225 LYS   T CD  1 
ATOM   35658 C  CE  . LYS   T  6  229 ? 63.311  -193.320 67.542  1.00 121.53 ? 225 LYS   T CE  1 
ATOM   35659 N  NZ  . LYS   T  6  229 ? 63.317  -192.203 66.567  1.00 119.83 ? 225 LYS   T NZ  1 
ATOM   35660 N  N   . PHE   T  6  230 ? 64.432  -198.818 63.313  1.00 112.26 ? 226 PHE   T N   1 
ATOM   35661 C  CA  . PHE   T  6  230 ? 65.201  -200.074 63.113  1.00 114.35 ? 226 PHE   T CA  1 
ATOM   35662 C  C   . PHE   T  6  230 ? 66.146  -200.279 64.298  1.00 116.39 ? 226 PHE   T C   1 
ATOM   35663 O  O   . PHE   T  6  230 ? 66.773  -199.296 64.744  1.00 120.32 ? 226 PHE   T O   1 
ATOM   35664 C  CB  . PHE   T  6  230 ? 65.992  -200.031 61.806  1.00 114.19 ? 226 PHE   T CB  1 
ATOM   35665 C  CG  . PHE   T  6  230 ? 65.136  -200.174 60.578  1.00 113.37 ? 226 PHE   T CG  1 
ATOM   35666 C  CD1 . PHE   T  6  230 ? 64.583  -199.063 59.964  1.00 111.98 ? 226 PHE   T CD1 1 
ATOM   35667 C  CD2 . PHE   T  6  230 ? 64.864  -201.426 60.053  1.00 115.88 ? 226 PHE   T CD2 1 
ATOM   35668 C  CE1 . PHE   T  6  230 ? 63.787  -199.201 58.839  1.00 110.54 ? 226 PHE   T CE1 1 
ATOM   35669 C  CE2 . PHE   T  6  230 ? 64.067  -201.561 58.928  1.00 114.99 ? 226 PHE   T CE2 1 
ATOM   35670 C  CZ  . PHE   T  6  230 ? 63.531  -200.449 58.324  1.00 113.27 ? 226 PHE   T CZ  1 
ATOM   35671 N  N   . VAL   T  6  231 ? 66.238  -201.519 64.788  1.00 116.52 ? 227 VAL   T N   1 
ATOM   35672 C  CA  . VAL   T  6  231 ? 67.198  -201.935 65.852  1.00 117.16 ? 227 VAL   T CA  1 
ATOM   35673 C  C   . VAL   T  6  231 ? 68.555  -202.186 65.187  1.00 118.47 ? 227 VAL   T C   1 
ATOM   35674 O  O   . VAL   T  6  231 ? 68.640  -203.113 64.359  1.00 117.14 ? 227 VAL   T O   1 
ATOM   35675 C  CB  . VAL   T  6  231 ? 66.700  -203.182 66.607  1.00 117.37 ? 227 VAL   T CB  1 
ATOM   35676 C  CG1 . VAL   T  6  231 ? 67.708  -203.650 67.644  1.00 120.79 ? 227 VAL   T CG1 1 
ATOM   35677 C  CG2 . VAL   T  6  231 ? 65.339  -202.949 67.247  1.00 115.42 ? 227 VAL   T CG2 1 
ATOM   35678 N  N   . LYS   T  6  232 ? 69.568  -201.382 65.529  1.00 120.21 ? 228 LYS   T N   1 
ATOM   35679 C  CA  . LYS   T  6  232 ? 70.921  -201.424 64.909  1.00 124.30 ? 228 LYS   T CA  1 
ATOM   35680 C  C   . LYS   T  6  232 ? 72.000  -201.384 65.996  1.00 122.77 ? 228 LYS   T C   1 
ATOM   35681 O  O   . LYS   T  6  232 ? 71.677  -201.047 67.153  1.00 117.81 ? 228 LYS   T O   1 
ATOM   35682 C  CB  . LYS   T  6  232 ? 71.123  -200.240 63.958  1.00 128.45 ? 228 LYS   T CB  1 
ATOM   35683 C  CG  . LYS   T  6  232 ? 70.007  -200.006 62.943  1.00 131.47 ? 228 LYS   T CG  1 
ATOM   35684 C  CD  . LYS   T  6  232 ? 69.768  -198.548 62.560  1.00 131.70 ? 228 LYS   T CD  1 
ATOM   35685 C  CE  . LYS   T  6  232 ? 69.679  -197.582 63.728  1.00 133.53 ? 228 LYS   T CE  1 
ATOM   35686 N  NZ  . LYS   T  6  232 ? 70.281  -196.268 63.397  1.00 134.22 ? 228 LYS   T NZ  1 
ATOM   35687 N  N   . GLY   T  6  233 ? 73.237  -201.714 65.613  1.00 125.93 ? 229 GLY   T N   1 
ATOM   35688 C  CA  . GLY   T  6  233 ? 74.449  -201.598 66.446  1.00 133.25 ? 229 GLY   T CA  1 
ATOM   35689 C  C   . GLY   T  6  233 ? 74.367  -202.420 67.723  1.00 138.75 ? 229 GLY   T C   1 
ATOM   35690 O  O   . GLY   T  6  233 ? 74.118  -203.641 67.627  1.00 140.88 ? 229 GLY   T O   1 
ATOM   35691 N  N   . ASP   T  6  234 ? 74.572  -201.767 68.874  1.00 142.71 ? 230 ASP   T N   1 
ATOM   35692 C  CA  . ASP   T  6  234 ? 74.744  -202.403 70.210  1.00 144.23 ? 230 ASP   T CA  1 
ATOM   35693 C  C   . ASP   T  6  234 ? 73.491  -203.200 70.594  1.00 143.62 ? 230 ASP   T C   1 
ATOM   35694 O  O   . ASP   T  6  234 ? 73.653  -204.332 71.093  1.00 145.31 ? 230 ASP   T O   1 
ATOM   35695 C  CB  . ASP   T  6  234 ? 75.082  -201.361 71.282  1.00 146.46 ? 230 ASP   T CB  1 
ATOM   35696 C  CG  . ASP   T  6  234 ? 76.518  -200.865 71.237  1.00 146.48 ? 230 ASP   T CG  1 
ATOM   35697 O  OD1 . ASP   T  6  234 ? 77.243  -201.237 70.291  1.00 147.43 ? 230 ASP   T OD1 1 
ATOM   35698 O  OD2 . ASP   T  6  234 ? 76.902  -200.111 72.153  1.00 145.79 ? 230 ASP   T OD2 1 
ATOM   35699 N  N   . LEU   T  6  235 ? 72.297  -202.638 70.381  1.00 138.76 ? 231 LEU   T N   1 
ATOM   35700 C  CA  . LEU   T  6  235 ? 71.008  -203.274 70.770  1.00 136.75 ? 231 LEU   T CA  1 
ATOM   35701 C  C   . LEU   T  6  235 ? 70.762  -204.521 69.909  1.00 132.85 ? 231 LEU   T C   1 
ATOM   35702 O  O   . LEU   T  6  235 ? 70.197  -205.496 70.445  1.00 131.43 ? 231 LEU   T O   1 
ATOM   35703 C  CB  . LEU   T  6  235 ? 69.864  -202.265 70.623  1.00 133.79 ? 231 LEU   T CB  1 
ATOM   35704 C  CG  . LEU   T  6  235 ? 68.539  -202.675 71.267  1.00 133.91 ? 231 LEU   T CG  1 
ATOM   35705 C  CD1 . LEU   T  6  235 ? 68.685  -202.829 72.774  1.00 134.16 ? 231 LEU   T CD1 1 
ATOM   35706 C  CD2 . LEU   T  6  235 ? 67.442  -201.671 70.943  1.00 132.04 ? 231 LEU   T CD2 1 
ATOM   35707 N  N   . LEU   T  6  236 ? 71.165  -204.487 68.632  1.00 135.32 ? 232 LEU   T N   1 
ATOM   35708 C  CA  . LEU   T  6  236 ? 71.015  -205.620 67.676  1.00 132.32 ? 232 LEU   T CA  1 
ATOM   35709 C  C   . LEU   T  6  236 ? 71.974  -206.751 68.066  1.00 133.13 ? 232 LEU   T C   1 
ATOM   35710 O  O   . LEU   T  6  236 ? 71.506  -207.898 68.158  1.00 134.18 ? 232 LEU   T O   1 
ATOM   35711 C  CB  . LEU   T  6  236 ? 71.283  -205.140 66.245  1.00 131.63 ? 232 LEU   T CB  1 
ATOM   35712 C  CG  . LEU   T  6  236 ? 71.075  -206.188 65.149  1.00 130.24 ? 232 LEU   T CG  1 
ATOM   35713 C  CD1 . LEU   T  6  236 ? 69.601  -206.537 64.993  1.00 129.25 ? 232 LEU   T CD1 1 
ATOM   35714 C  CD2 . LEU   T  6  236 ? 71.650  -205.712 63.825  1.00 129.35 ? 232 LEU   T CD2 1 
ATOM   35715 N  N   . GLN   T  6  237 ? 73.260  -206.444 68.279  1.00 132.82 ? 233 GLN   T N   1 
ATOM   35716 C  CA  . GLN   T  6  237 ? 74.307  -207.452 68.614  1.00 135.47 ? 233 GLN   T CA  1 
ATOM   35717 C  C   . GLN   T  6  237 ? 73.985  -208.101 69.966  1.00 135.69 ? 233 GLN   T C   1 
ATOM   35718 O  O   . GLN   T  6  237 ? 74.274  -209.301 70.121  1.00 135.52 ? 233 GLN   T O   1 
ATOM   35719 C  CB  . GLN   T  6  237 ? 75.704  -206.825 68.636  1.00 134.57 ? 233 GLN   T CB  1 
ATOM   35720 C  CG  . GLN   T  6  237 ? 76.828  -207.850 68.731  1.00 136.26 ? 233 GLN   T CG  1 
ATOM   35721 C  CD  . GLN   T  6  237 ? 76.817  -208.820 67.574  1.00 135.92 ? 233 GLN   T CD  1 
ATOM   35722 O  OE1 . GLN   T  6  237 ? 76.715  -208.426 66.415  1.00 133.20 ? 233 GLN   T OE1 1 
ATOM   35723 N  NE2 . GLN   T  6  237 ? 76.917  -210.106 67.875  1.00 137.36 ? 233 GLN   T NE2 1 
ATOM   35724 N  N   . GLU   T  6  238 ? 73.416  -207.332 70.900  1.00 136.83 ? 234 GLU   T N   1 
ATOM   35725 C  CA  . GLU   T  6  238 ? 72.950  -207.813 72.230  1.00 138.20 ? 234 GLU   T CA  1 
ATOM   35726 C  C   . GLU   T  6  238 ? 71.819  -208.833 72.044  1.00 136.93 ? 234 GLU   T C   1 
ATOM   35727 O  O   . GLU   T  6  238 ? 71.821  -209.849 72.763  1.00 138.60 ? 234 GLU   T O   1 
ATOM   35728 C  CB  . GLU   T  6  238 ? 72.482  -206.629 73.078  1.00 140.35 ? 234 GLU   T CB  1 
ATOM   35729 C  CG  . GLU   T  6  238 ? 72.029  -207.016 74.473  1.00 143.81 ? 234 GLU   T CG  1 
ATOM   35730 C  CD  . GLU   T  6  238 ? 71.337  -205.896 75.229  1.00 147.69 ? 234 GLU   T CD  1 
ATOM   35731 O  OE1 . GLU   T  6  238 ? 70.369  -206.190 75.956  1.00 149.20 ? 234 GLU   T OE1 1 
ATOM   35732 O  OE2 . GLU   T  6  238 ? 71.767  -204.734 75.084  1.00 152.27 ? 234 GLU   T OE2 1 
ATOM   35733 N  N   . ALA   T  6  239 ? 70.885  -208.560 71.127  1.00 137.67 ? 235 ALA   T N   1 
ATOM   35734 C  CA  . ALA   T  6  239 ? 69.718  -209.419 70.815  1.00 139.77 ? 235 ALA   T CA  1 
ATOM   35735 C  C   . ALA   T  6  239 ? 70.177  -210.694 70.093  1.00 139.65 ? 235 ALA   T C   1 
ATOM   35736 O  O   . ALA   T  6  239 ? 69.607  -211.764 70.387  1.00 142.05 ? 235 ALA   T O   1 
ATOM   35737 C  CB  . ALA   T  6  239 ? 68.709  -208.650 69.994  1.00 139.42 ? 235 ALA   T CB  1 
ATOM   35738 N  N   . ILE   T  6  240 ? 71.155  -210.584 69.182  1.00 137.10 ? 236 ILE   T N   1 
ATOM   35739 C  CA  . ILE   T  6  240 ? 71.759  -211.737 68.442  1.00 137.05 ? 236 ILE   T CA  1 
ATOM   35740 C  C   . ILE   T  6  240 ? 72.426  -212.679 69.453  1.00 140.84 ? 236 ILE   T C   1 
ATOM   35741 O  O   . ILE   T  6  240 ? 72.201  -213.901 69.354  1.00 141.45 ? 236 ILE   T O   1 
ATOM   35742 C  CB  . ILE   T  6  240 ? 72.760  -211.272 67.361  1.00 135.32 ? 236 ILE   T CB  1 
ATOM   35743 C  CG1 . ILE   T  6  240 ? 72.053  -210.604 66.179  1.00 130.97 ? 236 ILE   T CG1 1 
ATOM   35744 C  CG2 . ILE   T  6  240 ? 73.636  -212.431 66.901  1.00 136.96 ? 236 ILE   T CG2 1 
ATOM   35745 C  CD1 . ILE   T  6  240 ? 72.981  -209.882 65.226  1.00 131.26 ? 236 ILE   T CD1 1 
ATOM   35746 N  N   . ASP   T  6  241 ? 73.228  -212.125 70.369  1.00 142.53 ? 237 ASP   T N   1 
ATOM   35747 C  CA  . ASP   T  6  241 ? 73.991  -212.885 71.396  1.00 144.59 ? 237 ASP   T CA  1 
ATOM   35748 C  C   . ASP   T  6  241 ? 73.015  -213.670 72.279  1.00 144.68 ? 237 ASP   T C   1 
ATOM   35749 O  O   . ASP   T  6  241 ? 73.272  -214.868 72.504  1.00 147.27 ? 237 ASP   T O   1 
ATOM   35750 C  CB  . ASP   T  6  241 ? 74.878  -211.962 72.236  1.00 147.17 ? 237 ASP   T CB  1 
ATOM   35751 C  CG  . ASP   T  6  241 ? 76.025  -211.334 71.461  1.00 147.38 ? 237 ASP   T CG  1 
ATOM   35752 O  OD1 . ASP   T  6  241 ? 76.483  -211.955 70.480  1.00 150.69 ? 237 ASP   T OD1 1 
ATOM   35753 O  OD2 . ASP   T  6  241 ? 76.445  -210.223 71.838  1.00 147.73 ? 237 ASP   T OD2 1 
ATOM   35754 N  N   . PHE   T  6  242 ? 71.945  -213.020 72.750  1.00 143.16 ? 238 PHE   T N   1 
ATOM   35755 C  CA  . PHE   T  6  242 ? 70.865  -213.638 73.564  1.00 145.01 ? 238 PHE   T CA  1 
ATOM   35756 C  C   . PHE   T  6  242 ? 70.289  -214.852 72.826  1.00 146.67 ? 238 PHE   T C   1 
ATOM   35757 O  O   . PHE   T  6  242 ? 70.076  -215.888 73.476  1.00 152.18 ? 238 PHE   T O   1 
ATOM   35758 C  CB  . PHE   T  6  242 ? 69.753  -212.633 73.877  1.00 142.44 ? 238 PHE   T CB  1 
ATOM   35759 C  CG  . PHE   T  6  242 ? 68.584  -213.219 74.630  1.00 141.02 ? 238 PHE   T CG  1 
ATOM   35760 C  CD1 . PHE   T  6  242 ? 68.595  -213.292 76.015  1.00 141.93 ? 238 PHE   T CD1 1 
ATOM   35761 C  CD2 . PHE   T  6  242 ? 67.477  -213.709 73.954  1.00 140.42 ? 238 PHE   T CD2 1 
ATOM   35762 C  CE1 . PHE   T  6  242 ? 67.523  -213.836 76.705  1.00 140.48 ? 238 PHE   T CE1 1 
ATOM   35763 C  CE2 . PHE   T  6  242 ? 66.405  -214.253 74.647  1.00 138.87 ? 238 PHE   T CE2 1 
ATOM   35764 C  CZ  . PHE   T  6  242 ? 66.430  -214.316 76.021  1.00 139.10 ? 238 PHE   T CZ  1 
ATOM   35765 N  N   . ALA   T  6  243 ? 70.040  -214.720 71.518  1.00 150.26 ? 239 ALA   T N   1 
ATOM   35766 C  CA  . ALA   T  6  243 ? 69.464  -215.775 70.649  1.00 152.97 ? 239 ALA   T CA  1 
ATOM   35767 C  C   . ALA   T  6  243 ? 70.459  -216.934 70.486  1.00 155.39 ? 239 ALA   T C   1 
ATOM   35768 O  O   . ALA   T  6  243 ? 70.020  -218.099 70.577  1.00 157.52 ? 239 ALA   T O   1 
ATOM   35769 C  CB  . ALA   T  6  243 ? 69.075  -215.194 69.310  1.00 152.10 ? 239 ALA   T CB  1 
ATOM   35770 N  N   . GLN   T  6  244 ? 71.739  -216.624 70.245  1.00 157.69 ? 240 GLN   T N   1 
ATOM   35771 C  CA  . GLN   T  6  244 ? 72.832  -217.619 70.050  1.00 158.66 ? 240 GLN   T CA  1 
ATOM   35772 C  C   . GLN   T  6  244 ? 72.979  -218.496 71.300  1.00 158.11 ? 240 GLN   T C   1 
ATOM   35773 O  O   . GLN   T  6  244 ? 73.248  -219.703 71.140  1.00 158.88 ? 240 GLN   T O   1 
ATOM   35774 C  CB  . GLN   T  6  244 ? 74.162  -216.925 69.739  1.00 157.85 ? 240 GLN   T CB  1 
ATOM   35775 C  CG  . GLN   T  6  244 ? 74.352  -216.579 68.266  1.00 159.84 ? 240 GLN   T CG  1 
ATOM   35776 C  CD  . GLN   T  6  244 ? 74.466  -217.761 67.328  1.00 161.01 ? 240 GLN   T CD  1 
ATOM   35777 O  OE1 . GLN   T  6  244 ? 74.348  -217.608 66.115  1.00 165.56 ? 240 GLN   T OE1 1 
ATOM   35778 N  NE2 . GLN   T  6  244 ? 74.700  -218.952 67.860  1.00 163.33 ? 240 GLN   T NE2 1 
ATOM   35779 N  N   . LYS   T  6  245 ? 72.819  -217.908 72.491  1.00 153.97 ? 241 LYS   T N   1 
ATOM   35780 C  CA  . LYS   T  6  245 ? 72.984  -218.598 73.800  1.00 155.81 ? 241 LYS   T CA  1 
ATOM   35781 C  C   . LYS   T  6  245 ? 71.878  -219.647 73.987  1.00 158.15 ? 241 LYS   T C   1 
ATOM   35782 O  O   . LYS   T  6  245 ? 72.158  -220.682 74.624  1.00 157.41 ? 241 LYS   T O   1 
ATOM   35783 C  CB  . LYS   T  6  245 ? 72.974  -217.583 74.948  1.00 151.86 ? 241 LYS   T CB  1 
ATOM   35784 C  CG  . LYS   T  6  245 ? 73.565  -218.094 76.254  1.00 154.40 ? 241 LYS   T CG  1 
ATOM   35785 C  CD  . LYS   T  6  245 ? 73.660  -217.044 77.338  1.00 156.70 ? 241 LYS   T CD  1 
ATOM   35786 C  CE  . LYS   T  6  245 ? 74.347  -217.552 78.589  1.00 161.29 ? 241 LYS   T CE  1 
ATOM   35787 N  NZ  . LYS   T  6  245 ? 73.470  -217.443 79.778  1.00 163.05 ? 241 LYS   T NZ  1 
ATOM   35788 N  N   . GLU   T  6  246 ? 70.682  -219.397 73.439  1.00 159.06 ? 242 GLU   T N   1 
ATOM   35789 C  CA  . GLU   T  6  246 ? 69.451  -220.203 73.679  1.00 161.72 ? 242 GLU   T CA  1 
ATOM   35790 C  C   . GLU   T  6  246 ? 69.400  -221.432 72.760  1.00 166.22 ? 242 GLU   T C   1 
ATOM   35791 O  O   . GLU   T  6  246 ? 68.799  -222.439 73.185  1.00 164.06 ? 242 GLU   T O   1 
ATOM   35792 C  CB  . GLU   T  6  246 ? 68.202  -219.342 73.483  1.00 162.60 ? 242 GLU   T CB  1 
ATOM   35793 C  CG  . GLU   T  6  246 ? 68.114  -218.183 74.460  1.00 163.14 ? 242 GLU   T CG  1 
ATOM   35794 C  CD  . GLU   T  6  246 ? 67.798  -218.584 75.891  1.00 164.75 ? 242 GLU   T CD  1 
ATOM   35795 O  OE1 . GLU   T  6  246 ? 68.654  -218.358 76.769  1.00 165.18 ? 242 GLU   T OE1 1 
ATOM   35796 O  OE2 . GLU   T  6  246 ? 66.696  -219.118 76.123  1.00 160.38 ? 242 GLU   T OE2 1 
ATOM   35797 N  N   . ILE   T  6  247 ? 69.977  -221.363 71.553  1.00 170.08 ? 243 ILE   T N   1 
ATOM   35798 C  CA  . ILE   T  6  247 ? 69.996  -222.508 70.589  1.00 176.84 ? 243 ILE   T CA  1 
ATOM   35799 C  C   . ILE   T  6  247 ? 70.999  -223.565 71.079  1.00 181.65 ? 243 ILE   T C   1 
ATOM   35800 O  O   . ILE   T  6  247 ? 70.805  -224.749 70.739  1.00 186.28 ? 243 ILE   T O   1 
ATOM   35801 C  CB  . ILE   T  6  247 ? 70.275  -222.065 69.133  1.00 175.50 ? 243 ILE   T CB  1 
ATOM   35802 C  CG1 . ILE   T  6  247 ? 71.707  -221.565 68.913  1.00 177.77 ? 243 ILE   T CG1 1 
ATOM   35803 C  CG2 . ILE   T  6  247 ? 69.250  -221.039 68.673  1.00 172.34 ? 243 ILE   T CG2 1 
ATOM   35804 C  CD1 . ILE   T  6  247 ? 72.184  -221.701 67.483  1.00 175.63 ? 243 ILE   T CD1 1 
ATOM   35805 N  N   . ASN   T  6  248 ? 72.021  -223.155 71.845  1.00 180.38 ? 244 ASN   T N   1 
ATOM   35806 C  CA  . ASN   T  6  248 ? 73.038  -224.053 72.460  1.00 178.41 ? 244 ASN   T CA  1 
ATOM   35807 C  C   . ASN   T  6  248 ? 72.742  -224.205 73.957  1.00 179.12 ? 244 ASN   T C   1 
ATOM   35808 O  O   . ASN   T  6  248 ? 71.606  -224.057 74.411  1.00 173.91 ? 244 ASN   T O   1 
ATOM   35809 C  CB  . ASN   T  6  248 ? 74.465  -223.540 72.246  1.00 178.33 ? 244 ASN   T CB  1 
ATOM   35810 C  CG  . ASN   T  6  248 ? 74.740  -223.118 70.817  1.00 172.16 ? 244 ASN   T CG  1 
ATOM   35811 O  OD1 . ASN   T  6  248 ? 74.382  -223.824 69.877  1.00 174.11 ? 244 ASN   T OD1 1 
ATOM   35812 N  ND2 . ASN   T  6  248 ? 75.378  -221.973 70.642  1.00 168.77 ? 244 ASN   T ND2 1 
ATOM   35813 N  N   . GLY   U  7  11  ? 32.081  -226.715 30.561  1.00 134.38 ? 2   GLY   U N   1 
ATOM   35814 C  CA  . GLY   U  7  11  ? 30.901  -226.187 31.302  1.00 130.94 ? 2   GLY   U CA  1 
ATOM   35815 C  C   . GLY   U  7  11  ? 31.224  -224.885 32.016  1.00 128.85 ? 2   GLY   U C   1 
ATOM   35816 O  O   . GLY   U  7  11  ? 31.266  -224.891 33.262  1.00 128.78 ? 2   GLY   U O   1 
ATOM   35817 N  N   . TYR   U  7  12  ? 31.437  -223.806 31.257  1.00 128.86 ? 3   TYR   U N   1 
ATOM   35818 C  CA  . TYR   U  7  12  ? 31.810  -222.461 31.773  1.00 128.74 ? 3   TYR   U CA  1 
ATOM   35819 C  C   . TYR   U  7  12  ? 30.596  -221.755 32.392  1.00 124.72 ? 3   TYR   U C   1 
ATOM   35820 O  O   . TYR   U  7  12  ? 30.811  -220.738 33.074  1.00 123.78 ? 3   TYR   U O   1 
ATOM   35821 C  CB  . TYR   U  7  12  ? 32.431  -221.594 30.674  1.00 127.26 ? 3   TYR   U CB  1 
ATOM   35822 C  CG  . TYR   U  7  12  ? 33.848  -221.954 30.299  1.00 134.59 ? 3   TYR   U CG  1 
ATOM   35823 C  CD1 . TYR   U  7  12  ? 34.796  -222.255 31.266  1.00 135.50 ? 3   TYR   U CD1 1 
ATOM   35824 C  CD2 . TYR   U  7  12  ? 34.251  -221.973 28.972  1.00 137.79 ? 3   TYR   U CD2 1 
ATOM   35825 C  CE1 . TYR   U  7  12  ? 36.097  -222.586 30.926  1.00 140.86 ? 3   TYR   U CE1 1 
ATOM   35826 C  CE2 . TYR   U  7  12  ? 35.551  -222.298 28.615  1.00 142.36 ? 3   TYR   U CE2 1 
ATOM   35827 C  CZ  . TYR   U  7  12  ? 36.477  -222.608 29.595  1.00 142.73 ? 3   TYR   U CZ  1 
ATOM   35828 O  OH  . TYR   U  7  12  ? 37.759  -222.926 29.251  1.00 147.89 ? 3   TYR   U OH  1 
ATOM   35829 N  N   . ASP   U  7  13  ? 29.377  -222.269 32.181  1.00 122.40 ? 4   ASP   U N   1 
ATOM   35830 C  CA  . ASP   U  7  13  ? 28.123  -221.736 32.787  1.00 122.64 ? 4   ASP   U CA  1 
ATOM   35831 C  C   . ASP   U  7  13  ? 28.131  -221.927 34.313  1.00 121.12 ? 4   ASP   U C   1 
ATOM   35832 O  O   . ASP   U  7  13  ? 27.215  -221.384 34.974  1.00 112.31 ? 4   ASP   U O   1 
ATOM   35833 C  CB  . ASP   U  7  13  ? 26.877  -222.391 32.182  1.00 127.64 ? 4   ASP   U CB  1 
ATOM   35834 C  CG  . ASP   U  7  13  ? 26.816  -223.895 32.375  1.00 133.63 ? 4   ASP   U CG  1 
ATOM   35835 O  OD1 . ASP   U  7  13  ? 27.868  -224.548 32.219  1.00 142.63 ? 4   ASP   U OD1 1 
ATOM   35836 O  OD2 . ASP   U  7  13  ? 25.720  -224.400 32.684  1.00 143.70 ? 4   ASP   U OD2 1 
ATOM   35837 N  N   . ARG   U  7  14  ? 29.099  -222.680 34.850  1.00 118.15 ? 5   ARG   U N   1 
ATOM   35838 C  CA  . ARG   U  7  14  ? 29.282  -222.896 36.311  1.00 116.13 ? 5   ARG   U CA  1 
ATOM   35839 C  C   . ARG   U  7  14  ? 30.356  -221.954 36.875  1.00 112.26 ? 5   ARG   U C   1 
ATOM   35840 O  O   . ARG   U  7  14  ? 30.492  -221.912 38.111  1.00 109.43 ? 5   ARG   U O   1 
ATOM   35841 C  CB  . ARG   U  7  14  ? 29.659  -224.354 36.588  1.00 116.64 ? 5   ARG   U CB  1 
ATOM   35842 C  CG  . ARG   U  7  14  ? 28.742  -225.363 35.913  1.00 120.28 ? 5   ARG   U CG  1 
ATOM   35843 C  CD  . ARG   U  7  14  ? 28.527  -226.610 36.747  1.00 124.17 ? 5   ARG   U CD  1 
ATOM   35844 N  NE  . ARG   U  7  14  ? 27.400  -227.391 36.255  1.00 126.97 ? 5   ARG   U NE  1 
ATOM   35845 C  CZ  . ARG   U  7  14  ? 26.744  -228.316 36.953  1.00 128.35 ? 5   ARG   U CZ  1 
ATOM   35846 N  NH1 . ARG   U  7  14  ? 27.089  -228.594 38.200  1.00 130.27 ? 5   ARG   U NH1 1 
ATOM   35847 N  NH2 . ARG   U  7  14  ? 25.731  -228.959 36.397  1.00 132.26 ? 5   ARG   U NH2 1 
ATOM   35848 N  N   . HIS   U  7  15  ? 31.087  -221.228 36.020  1.00 108.09 ? 6   HIS   U N   1 
ATOM   35849 C  CA  . HIS   U  7  15  ? 32.230  -220.355 36.410  1.00 108.42 ? 6   HIS   U CA  1 
ATOM   35850 C  C   . HIS   U  7  15  ? 31.778  -218.898 36.573  1.00 106.12 ? 6   HIS   U C   1 
ATOM   35851 O  O   . HIS   U  7  15  ? 32.326  -218.217 37.462  1.00 103.15 ? 6   HIS   U O   1 
ATOM   35852 C  CB  . HIS   U  7  15  ? 33.372  -220.468 35.393  1.00 110.48 ? 6   HIS   U CB  1 
ATOM   35853 C  CG  . HIS   U  7  15  ? 34.000  -221.818 35.343  1.00 113.79 ? 6   HIS   U CG  1 
ATOM   35854 N  ND1 . HIS   U  7  15  ? 35.364  -221.990 35.233  1.00 116.69 ? 6   HIS   U ND1 1 
ATOM   35855 C  CD2 . HIS   U  7  15  ? 33.461  -223.055 35.396  1.00 118.81 ? 6   HIS   U CD2 1 
ATOM   35856 C  CE1 . HIS   U  7  15  ? 35.638  -223.278 35.211  1.00 120.68 ? 6   HIS   U CE1 1 
ATOM   35857 N  NE2 . HIS   U  7  15  ? 34.489  -223.952 35.312  1.00 121.98 ? 6   HIS   U NE2 1 
ATOM   35858 N  N   . ILE   U  7  16  ? 30.843  -218.433 35.737  1.00 104.15 ? 7   ILE   U N   1 
ATOM   35859 C  CA  . ILE   U  7  16  ? 30.309  -217.038 35.770  1.00 100.81 ? 7   ILE   U CA  1 
ATOM   35860 C  C   . ILE   U  7  16  ? 28.791  -217.083 35.980  1.00 99.53  ? 7   ILE   U C   1 
ATOM   35861 O  O   . ILE   U  7  16  ? 28.206  -218.179 35.877  1.00 98.70  ? 7   ILE   U O   1 
ATOM   35862 C  CB  . ILE   U  7  16  ? 30.703  -216.263 34.497  1.00 102.15 ? 7   ILE   U CB  1 
ATOM   35863 C  CG1 . ILE   U  7  16  ? 30.291  -216.993 33.216  1.00 103.30 ? 7   ILE   U CG1 1 
ATOM   35864 C  CG2 . ILE   U  7  16  ? 32.192  -215.949 34.508  1.00 104.83 ? 7   ILE   U CG2 1 
ATOM   35865 C  CD1 . ILE   U  7  16  ? 30.221  -216.096 32.002  1.00 104.06 ? 7   ILE   U CD1 1 
ATOM   35866 N  N   . THR   U  7  17  ? 28.189  -215.928 36.276  1.00 97.27  ? 8   THR   U N   1 
ATOM   35867 C  CA  . THR   U  7  17  ? 26.750  -215.781 36.622  1.00 98.76  ? 8   THR   U CA  1 
ATOM   35868 C  C   . THR   U  7  17  ? 25.932  -215.665 35.330  1.00 99.46  ? 8   THR   U C   1 
ATOM   35869 O  O   . THR   U  7  17  ? 25.367  -214.582 35.080  1.00 101.66 ? 8   THR   U O   1 
ATOM   35870 C  CB  . THR   U  7  17  ? 26.536  -214.614 37.597  1.00 96.86  ? 8   THR   U CB  1 
ATOM   35871 O  OG1 . THR   U  7  17  ? 27.151  -213.429 37.089  1.00 96.70  ? 8   THR   U OG1 1 
ATOM   35872 C  CG2 . THR   U  7  17  ? 27.101  -214.902 38.970  1.00 96.89  ? 8   THR   U CG2 1 
ATOM   35873 N  N   . ILE   U  7  18  ? 25.901  -216.743 34.539  1.00 101.38 ? 9   ILE   U N   1 
ATOM   35874 C  CA  . ILE   U  7  18  ? 24.945  -216.960 33.410  1.00 103.63 ? 9   ILE   U CA  1 
ATOM   35875 C  C   . ILE   U  7  18  ? 24.108  -218.205 33.727  1.00 107.40 ? 9   ILE   U C   1 
ATOM   35876 O  O   . ILE   U  7  18  ? 24.541  -219.016 34.575  1.00 109.16 ? 9   ILE   U O   1 
ATOM   35877 C  CB  . ILE   U  7  18  ? 25.664  -217.088 32.050  1.00 102.97 ? 9   ILE   U CB  1 
ATOM   35878 C  CG1 . ILE   U  7  18  ? 26.631  -218.275 32.008  1.00 100.39 ? 9   ILE   U CG1 1 
ATOM   35879 C  CG2 . ILE   U  7  18  ? 26.358  -215.785 31.685  1.00 103.82 ? 9   ILE   U CG2 1 
ATOM   35880 C  CD1 . ILE   U  7  18  ? 27.017  -218.700 30.613  1.00 99.21  ? 9   ILE   U CD1 1 
ATOM   35881 N  N   . PHE   U  7  19  ? 22.961  -218.351 33.059  1.00 107.17 ? 10  PHE   U N   1 
ATOM   35882 C  CA  . PHE   U  7  19  ? 21.983  -219.444 33.295  1.00 106.24 ? 10  PHE   U CA  1 
ATOM   35883 C  C   . PHE   U  7  19  ? 22.549  -220.777 32.796  1.00 108.01 ? 10  PHE   U C   1 
ATOM   35884 O  O   . PHE   U  7  19  ? 23.103  -220.826 31.680  1.00 113.67 ? 10  PHE   U O   1 
ATOM   35885 C  CB  . PHE   U  7  19  ? 20.653  -219.154 32.597  1.00 105.17 ? 10  PHE   U CB  1 
ATOM   35886 C  CG  . PHE   U  7  19  ? 19.860  -218.031 33.209  1.00 101.82 ? 10  PHE   U CG  1 
ATOM   35887 C  CD1 . PHE   U  7  19  ? 19.384  -218.130 34.506  1.00 102.96 ? 10  PHE   U CD1 1 
ATOM   35888 C  CD2 . PHE   U  7  19  ? 19.582  -216.883 32.488  1.00 101.25 ? 10  PHE   U CD2 1 
ATOM   35889 C  CE1 . PHE   U  7  19  ? 18.652  -217.100 35.073  1.00 103.02 ? 10  PHE   U CE1 1 
ATOM   35890 C  CE2 . PHE   U  7  19  ? 18.849  -215.854 33.056  1.00 102.62 ? 10  PHE   U CE2 1 
ATOM   35891 C  CZ  . PHE   U  7  19  ? 18.385  -215.963 34.346  1.00 102.82 ? 10  PHE   U CZ  1 
ATOM   35892 N  N   . SER   U  7  20  ? 22.402  -221.825 33.611  1.00 107.03 ? 11  SER   U N   1 
ATOM   35893 C  CA  . SER   U  7  20  ? 22.589  -223.241 33.207  1.00 108.02 ? 11  SER   U CA  1 
ATOM   35894 C  C   . SER   U  7  20  ? 21.360  -223.687 32.421  1.00 106.35 ? 11  SER   U C   1 
ATOM   35895 O  O   . SER   U  7  20  ? 20.314  -223.047 32.506  1.00 104.77 ? 11  SER   U O   1 
ATOM   35896 C  CB  . SER   U  7  20  ? 22.824  -224.117 34.407  1.00 107.04 ? 11  SER   U CB  1 
ATOM   35897 O  OG  . SER   U  7  20  ? 21.621  -224.304 35.139  1.00 105.02 ? 11  SER   U OG  1 
ATOM   35898 N  N   . PRO   U  7  21  ? 21.444  -224.783 31.630  1.00 106.73 ? 12  PRO   U N   1 
ATOM   35899 C  CA  . PRO   U  7  21  ? 20.288  -225.299 30.891  1.00 106.12 ? 12  PRO   U CA  1 
ATOM   35900 C  C   . PRO   U  7  21  ? 18.990  -225.477 31.697  1.00 107.00 ? 12  PRO   U C   1 
ATOM   35901 O  O   . PRO   U  7  21  ? 17.935  -225.385 31.095  1.00 107.93 ? 12  PRO   U O   1 
ATOM   35902 C  CB  . PRO   U  7  21  ? 20.783  -226.663 30.400  1.00 107.15 ? 12  PRO   U CB  1 
ATOM   35903 C  CG  . PRO   U  7  21  ? 22.271  -226.472 30.224  1.00 105.76 ? 12  PRO   U CG  1 
ATOM   35904 C  CD  . PRO   U  7  21  ? 22.674  -225.538 31.345  1.00 104.40 ? 12  PRO   U CD  1 
ATOM   35905 N  N   . GLU   U  7  22  ? 19.089  -225.709 33.012  1.00 108.22 ? 13  GLU   U N   1 
ATOM   35906 C  CA  . GLU   U  7  22  ? 17.923  -225.901 33.924  1.00 111.75 ? 13  GLU   U CA  1 
ATOM   35907 C  C   . GLU   U  7  22  ? 17.561  -224.569 34.605  1.00 108.50 ? 13  GLU   U C   1 
ATOM   35908 O  O   . GLU   U  7  22  ? 16.727  -224.586 35.532  1.00 107.18 ? 13  GLU   U O   1 
ATOM   35909 C  CB  . GLU   U  7  22  ? 18.183  -227.028 34.934  1.00 114.10 ? 13  GLU   U CB  1 
ATOM   35910 C  CG  . GLU   U  7  22  ? 19.563  -227.022 35.580  1.00 118.43 ? 13  GLU   U CG  1 
ATOM   35911 C  CD  . GLU   U  7  22  ? 20.671  -227.726 34.809  1.00 121.38 ? 13  GLU   U CD  1 
ATOM   35912 O  OE1 . GLU   U  7  22  ? 20.352  -228.531 33.912  1.00 125.96 ? 13  GLU   U OE1 1 
ATOM   35913 O  OE2 . GLU   U  7  22  ? 21.856  -227.468 35.109  1.00 119.33 ? 13  GLU   U OE2 1 
ATOM   35914 N  N   . GLY   U  7  23  ? 18.138  -223.453 34.145  1.00 107.46 ? 14  GLY   U N   1 
ATOM   35915 C  CA  . GLY   U  7  23  ? 17.774  -222.087 34.571  1.00 106.96 ? 14  GLY   U CA  1 
ATOM   35916 C  C   . GLY   U  7  23  ? 18.321  -221.734 35.945  1.00 106.88 ? 14  GLY   U C   1 
ATOM   35917 O  O   . GLY   U  7  23  ? 17.653  -220.963 36.661  1.00 107.00 ? 14  GLY   U O   1 
ATOM   35918 N  N   . ARG   U  7  24  ? 19.500  -222.258 36.294  1.00 106.76 ? 15  ARG   U N   1 
ATOM   35919 C  CA  . ARG   U  7  24  ? 20.148  -222.067 37.619  1.00 104.39 ? 15  ARG   U CA  1 
ATOM   35920 C  C   . ARG   U  7  24  ? 21.431  -221.241 37.462  1.00 100.52 ? 15  ARG   U C   1 
ATOM   35921 O  O   . ARG   U  7  24  ? 22.053  -221.293 36.382  1.00 97.48  ? 15  ARG   U O   1 
ATOM   35922 C  CB  . ARG   U  7  24  ? 20.468  -223.424 38.254  1.00 106.36 ? 15  ARG   U CB  1 
ATOM   35923 C  CG  . ARG   U  7  24  ? 19.258  -224.173 38.795  1.00 108.54 ? 15  ARG   U CG  1 
ATOM   35924 C  CD  . ARG   U  7  24  ? 19.554  -225.638 39.078  1.00 109.21 ? 15  ARG   U CD  1 
ATOM   35925 N  NE  . ARG   U  7  24  ? 20.595  -225.830 40.080  1.00 106.41 ? 15  ARG   U NE  1 
ATOM   35926 C  CZ  . ARG   U  7  24  ? 21.020  -227.009 40.520  1.00 107.06 ? 15  ARG   U CZ  1 
ATOM   35927 N  NH1 . ARG   U  7  24  ? 20.496  -228.130 40.049  1.00 111.75 ? 15  ARG   U NH1 1 
ATOM   35928 N  NH2 . ARG   U  7  24  ? 21.973  -227.067 41.433  1.00 106.47 ? 15  ARG   U NH2 1 
ATOM   35929 N  N   . LEU   U  7  25  ? 21.807  -220.519 38.521  1.00 100.92 ? 16  LEU   U N   1 
ATOM   35930 C  CA  . LEU   U  7  25  ? 23.078  -219.756 38.631  1.00 100.85 ? 16  LEU   U CA  1 
ATOM   35931 C  C   . LEU   U  7  25  ? 23.960  -220.447 39.673  1.00 100.23 ? 16  LEU   U C   1 
ATOM   35932 O  O   . LEU   U  7  25  ? 23.749  -220.200 40.875  1.00 97.87  ? 16  LEU   U O   1 
ATOM   35933 C  CB  . LEU   U  7  25  ? 22.777  -218.315 39.054  1.00 100.61 ? 16  LEU   U CB  1 
ATOM   35934 C  CG  . LEU   U  7  25  ? 21.914  -217.490 38.101  1.00 100.82 ? 16  LEU   U CG  1 
ATOM   35935 C  CD1 . LEU   U  7  25  ? 21.591  -216.139 38.720  1.00 100.41 ? 16  LEU   U CD1 1 
ATOM   35936 C  CD2 . LEU   U  7  25  ? 22.598  -217.304 36.755  1.00 101.80 ? 16  LEU   U CD2 1 
ATOM   35937 N  N   . TYR   U  7  26  ? 24.896  -221.289 39.232  1.00 100.46 ? 17  TYR   U N   1 
ATOM   35938 C  CA  . TYR   U  7  26  ? 25.725  -222.138 40.127  1.00 100.54 ? 17  TYR   U CA  1 
ATOM   35939 C  C   . TYR   U  7  26  ? 26.632  -221.263 40.998  1.00 97.40  ? 17  TYR   U C   1 
ATOM   35940 O  O   . TYR   U  7  26  ? 26.810  -221.604 42.184  1.00 96.51  ? 17  TYR   U O   1 
ATOM   35941 C  CB  . TYR   U  7  26  ? 26.512  -223.180 39.327  1.00 102.76 ? 17  TYR   U CB  1 
ATOM   35942 C  CG  . TYR   U  7  26  ? 25.672  -224.359 38.911  1.00 104.44 ? 17  TYR   U CG  1 
ATOM   35943 C  CD1 . TYR   U  7  26  ? 25.307  -225.334 39.826  1.00 104.39 ? 17  TYR   U CD1 1 
ATOM   35944 C  CD2 . TYR   U  7  26  ? 25.201  -224.478 37.614  1.00 106.55 ? 17  TYR   U CD2 1 
ATOM   35945 C  CE1 . TYR   U  7  26  ? 24.511  -226.406 39.459  1.00 107.18 ? 17  TYR   U CE1 1 
ATOM   35946 C  CE2 . TYR   U  7  26  ? 24.405  -225.544 37.230  1.00 106.82 ? 17  TYR   U CE2 1 
ATOM   35947 C  CZ  . TYR   U  7  26  ? 24.059  -226.512 38.155  1.00 109.06 ? 17  TYR   U CZ  1 
ATOM   35948 O  OH  . TYR   U  7  26  ? 23.279  -227.564 37.770  1.00 114.36 ? 17  TYR   U OH  1 
ATOM   35949 N  N   . GLN   U  7  27  ? 27.172  -220.173 40.447  1.00 95.82  ? 18  GLN   U N   1 
ATOM   35950 C  CA  . GLN   U  7  27  ? 28.087  -219.264 41.188  1.00 92.40  ? 18  GLN   U CA  1 
ATOM   35951 C  C   . GLN   U  7  27  ? 27.348  -218.668 42.391  1.00 90.83  ? 18  GLN   U C   1 
ATOM   35952 O  O   . GLN   U  7  27  ? 27.989  -218.528 43.450  1.00 91.53  ? 18  GLN   U O   1 
ATOM   35953 C  CB  . GLN   U  7  27  ? 28.657  -218.189 40.265  1.00 92.36  ? 18  GLN   U CB  1 
ATOM   35954 C  CG  . GLN   U  7  27  ? 29.826  -218.688 39.431  1.00 93.34  ? 18  GLN   U CG  1 
ATOM   35955 C  CD  . GLN   U  7  27  ? 31.011  -219.061 40.291  1.00 93.86  ? 18  GLN   U CD  1 
ATOM   35956 O  OE1 . GLN   U  7  27  ? 31.572  -218.234 41.005  1.00 92.96  ? 18  GLN   U OE1 1 
ATOM   35957 N  NE2 . GLN   U  7  27  ? 31.397  -220.324 40.242  1.00 94.65  ? 18  GLN   U NE2 1 
ATOM   35958 N  N   . VAL   U  7  28  ? 26.054  -218.364 42.241  1.00 89.45  ? 19  VAL   U N   1 
ATOM   35959 C  CA  . VAL   U  7  28  ? 25.178  -217.866 43.345  1.00 90.19  ? 19  VAL   U CA  1 
ATOM   35960 C  C   . VAL   U  7  28  ? 25.019  -218.987 44.379  1.00 93.03  ? 19  VAL   U C   1 
ATOM   35961 O  O   . VAL   U  7  28  ? 25.159  -218.701 45.586  1.00 88.58  ? 19  VAL   U O   1 
ATOM   35962 C  CB  . VAL   U  7  28  ? 23.812  -217.376 42.824  1.00 89.70  ? 19  VAL   U CB  1 
ATOM   35963 C  CG1 . VAL   U  7  28  ? 22.885  -216.964 43.959  1.00 88.03  ? 19  VAL   U CG1 1 
ATOM   35964 C  CG2 . VAL   U  7  28  ? 23.968  -216.233 41.832  1.00 90.47  ? 19  VAL   U CG2 1 
ATOM   35965 N  N   . GLU   U  7  29  ? 24.748  -220.211 43.914  1.00 95.70  ? 20  GLU   U N   1 
ATOM   35966 C  CA  . GLU   U  7  29  ? 24.531  -221.414 44.765  1.00 97.58  ? 20  GLU   U CA  1 
ATOM   35967 C  C   . GLU   U  7  29  ? 25.798  -221.724 45.569  1.00 96.49  ? 20  GLU   U C   1 
ATOM   35968 O  O   . GLU   U  7  29  ? 25.667  -222.095 46.750  1.00 97.06  ? 20  GLU   U O   1 
ATOM   35969 C  CB  . GLU   U  7  29  ? 24.154  -222.629 43.916  1.00 100.77 ? 20  GLU   U CB  1 
ATOM   35970 C  CG  . GLU   U  7  29  ? 22.791  -222.518 43.262  1.00 105.11 ? 20  GLU   U CG  1 
ATOM   35971 C  CD  . GLU   U  7  29  ? 22.312  -223.795 42.594  1.00 108.56 ? 20  GLU   U CD  1 
ATOM   35972 O  OE1 . GLU   U  7  29  ? 21.297  -223.732 41.875  1.00 119.00 ? 20  GLU   U OE1 1 
ATOM   35973 O  OE2 . GLU   U  7  29  ? 22.951  -224.850 42.794  1.00 111.29 ? 20  GLU   U OE2 1 
ATOM   35974 N  N   . TYR   U  7  30  ? 26.973  -221.597 44.946  1.00 95.44  ? 21  TYR   U N   1 
ATOM   35975 C  CA  . TYR   U  7  30  ? 28.287  -221.899 45.573  1.00 96.10  ? 21  TYR   U CA  1 
ATOM   35976 C  C   . TYR   U  7  30  ? 28.648  -220.789 46.567  1.00 94.92  ? 21  TYR   U C   1 
ATOM   35977 O  O   . TYR   U  7  30  ? 29.264  -221.099 47.602  1.00 94.88  ? 21  TYR   U O   1 
ATOM   35978 C  CB  . TYR   U  7  30  ? 29.376  -222.086 44.513  1.00 97.30  ? 21  TYR   U CB  1 
ATOM   35979 C  CG  . TYR   U  7  30  ? 29.140  -223.198 43.519  1.00 100.83 ? 21  TYR   U CG  1 
ATOM   35980 C  CD1 . TYR   U  7  30  ? 28.218  -224.212 43.751  1.00 103.73 ? 21  TYR   U CD1 1 
ATOM   35981 C  CD2 . TYR   U  7  30  ? 29.865  -223.253 42.339  1.00 102.90 ? 21  TYR   U CD2 1 
ATOM   35982 C  CE1 . TYR   U  7  30  ? 28.015  -225.234 42.836  1.00 104.97 ? 21  TYR   U CE1 1 
ATOM   35983 C  CE2 . TYR   U  7  30  ? 29.674  -224.268 41.413  1.00 104.41 ? 21  TYR   U CE2 1 
ATOM   35984 C  CZ  . TYR   U  7  30  ? 28.745  -225.263 41.661  1.00 104.10 ? 21  TYR   U CZ  1 
ATOM   35985 O  OH  . TYR   U  7  30  ? 28.550  -226.264 40.754  1.00 104.76 ? 21  TYR   U OH  1 
ATOM   35986 N  N   . ALA   U  7  31  ? 28.270  -219.542 46.274  1.00 92.71  ? 22  ALA   U N   1 
ATOM   35987 C  CA  . ALA   U  7  31  ? 28.437  -218.388 47.188  1.00 94.45  ? 22  ALA   U CA  1 
ATOM   35988 C  C   . ALA   U  7  31  ? 27.637  -218.633 48.473  1.00 96.31  ? 22  ALA   U C   1 
ATOM   35989 O  O   . ALA   U  7  31  ? 28.118  -218.225 49.549  1.00 98.34  ? 22  ALA   U O   1 
ATOM   35990 C  CB  . ALA   U  7  31  ? 28.017  -217.107 46.512  1.00 93.28  ? 22  ALA   U CB  1 
ATOM   35991 N  N   . PHE   U  7  32  ? 26.469  -219.278 48.368  1.00 97.06  ? 23  PHE   U N   1 
ATOM   35992 C  CA  . PHE   U  7  32  ? 25.632  -219.690 49.527  1.00 96.56  ? 23  PHE   U CA  1 
ATOM   35993 C  C   . PHE   U  7  32  ? 26.407  -220.683 50.401  1.00 95.28  ? 23  PHE   U C   1 
ATOM   35994 O  O   . PHE   U  7  32  ? 26.274  -220.615 51.630  1.00 94.17  ? 23  PHE   U O   1 
ATOM   35995 C  CB  . PHE   U  7  32  ? 24.304  -220.305 49.081  1.00 96.12  ? 23  PHE   U CB  1 
ATOM   35996 C  CG  . PHE   U  7  32  ? 23.154  -219.334 49.001  1.00 95.65  ? 23  PHE   U CG  1 
ATOM   35997 C  CD1 . PHE   U  7  32  ? 22.450  -218.973 50.139  1.00 94.09  ? 23  PHE   U CD1 1 
ATOM   35998 C  CD2 . PHE   U  7  32  ? 22.766  -218.795 47.785  1.00 94.97  ? 23  PHE   U CD2 1 
ATOM   35999 C  CE1 . PHE   U  7  32  ? 21.385  -218.090 50.061  1.00 95.50  ? 23  PHE   U CE1 1 
ATOM   36000 C  CE2 . PHE   U  7  32  ? 21.701  -217.912 47.708  1.00 94.64  ? 23  PHE   U CE2 1 
ATOM   36001 C  CZ  . PHE   U  7  32  ? 21.013  -217.560 48.846  1.00 96.03  ? 23  PHE   U CZ  1 
ATOM   36002 N  N   . LYS   U  7  33  ? 27.174  -221.588 49.790  1.00 97.06  ? 24  LYS   U N   1 
ATOM   36003 C  CA  . LYS   U  7  33  ? 27.963  -222.611 50.529  1.00 99.78  ? 24  LYS   U CA  1 
ATOM   36004 C  C   . LYS   U  7  33  ? 29.149  -221.925 51.222  1.00 96.62  ? 24  LYS   U C   1 
ATOM   36005 O  O   . LYS   U  7  33  ? 29.494  -222.354 52.335  1.00 101.53 ? 24  LYS   U O   1 
ATOM   36006 C  CB  . LYS   U  7  33  ? 28.371  -223.773 49.615  1.00 104.66 ? 24  LYS   U CB  1 
ATOM   36007 C  CG  . LYS   U  7  33  ? 27.501  -225.018 49.758  1.00 110.54 ? 24  LYS   U CG  1 
ATOM   36008 C  CD  . LYS   U  7  33  ? 27.855  -226.146 48.812  1.00 117.24 ? 24  LYS   U CD  1 
ATOM   36009 C  CE  . LYS   U  7  33  ? 27.154  -226.045 47.471  1.00 117.37 ? 24  LYS   U CE  1 
ATOM   36010 N  NZ  . LYS   U  7  33  ? 27.578  -227.118 46.540  1.00 117.06 ? 24  LYS   U NZ  1 
ATOM   36011 N  N   . ALA   U  7  34  ? 29.725  -220.880 50.621  1.00 92.92  ? 25  ALA   U N   1 
ATOM   36012 C  CA  . ALA   U  7  34  ? 30.804  -220.064 51.232  1.00 92.85  ? 25  ALA   U CA  1 
ATOM   36013 C  C   . ALA   U  7  34  ? 30.308  -219.442 52.546  1.00 91.56  ? 25  ALA   U C   1 
ATOM   36014 O  O   . ALA   U  7  34  ? 31.145  -219.216 53.437  1.00 91.60  ? 25  ALA   U O   1 
ATOM   36015 C  CB  . ALA   U  7  34  ? 31.274  -219.004 50.268  1.00 93.42  ? 25  ALA   U CB  1 
ATOM   36016 N  N   . THR   U  7  35  ? 29.000  -219.171 52.646  1.00 92.56  ? 26  THR   U N   1 
ATOM   36017 C  CA  . THR   U  7  35  ? 28.301  -218.606 53.836  1.00 92.25  ? 26  THR   U CA  1 
ATOM   36018 C  C   . THR   U  7  35  ? 28.689  -219.352 55.118  1.00 93.11  ? 26  THR   U C   1 
ATOM   36019 O  O   . THR   U  7  35  ? 28.909  -218.678 56.144  1.00 90.38  ? 26  THR   U O   1 
ATOM   36020 C  CB  . THR   U  7  35  ? 26.778  -218.655 53.651  1.00 92.88  ? 26  THR   U CB  1 
ATOM   36021 O  OG1 . THR   U  7  35  ? 26.389  -217.499 52.904  1.00 92.35  ? 26  THR   U OG1 1 
ATOM   36022 C  CG2 . THR   U  7  35  ? 26.008  -218.721 54.953  1.00 90.46  ? 26  THR   U CG2 1 
ATOM   36023 N  N   . ASN   U  7  36  ? 28.733  -220.687 55.071  1.00 93.55  ? 27  ASN   U N   1 
ATOM   36024 C  CA  . ASN   U  7  36  ? 28.912  -221.553 56.267  1.00 95.30  ? 27  ASN   U CA  1 
ATOM   36025 C  C   . ASN   U  7  36  ? 30.401  -221.808 56.533  1.00 96.57  ? 27  ASN   U C   1 
ATOM   36026 O  O   . ASN   U  7  36  ? 30.693  -222.483 57.533  1.00 102.16 ? 27  ASN   U O   1 
ATOM   36027 C  CB  . ASN   U  7  36  ? 28.136  -222.864 56.120  1.00 93.60  ? 27  ASN   U CB  1 
ATOM   36028 C  CG  . ASN   U  7  36  ? 26.635  -222.665 56.138  1.00 93.65  ? 27  ASN   U CG  1 
ATOM   36029 O  OD1 . ASN   U  7  36  ? 26.126  -221.827 56.878  1.00 95.69  ? 27  ASN   U OD1 1 
ATOM   36030 N  ND2 . ASN   U  7  36  ? 25.918  -223.433 55.335  1.00 95.26  ? 27  ASN   U ND2 1 
ATOM   36031 N  N   . GLN   U  7  37  ? 31.303  -221.265 55.708  1.00 99.03  ? 28  GLN   U N   1 
ATOM   36032 C  CA  . GLN   U  7  37  ? 32.765  -221.558 55.748  1.00 104.74 ? 28  GLN   U CA  1 
ATOM   36033 C  C   . GLN   U  7  37  ? 33.327  -221.280 57.153  1.00 104.19 ? 28  GLN   U C   1 
ATOM   36034 O  O   . GLN   U  7  37  ? 34.280  -221.982 57.546  1.00 101.75 ? 28  GLN   U O   1 
ATOM   36035 C  CB  . GLN   U  7  37  ? 33.495  -220.757 54.662  1.00 109.40 ? 28  GLN   U CB  1 
ATOM   36036 C  CG  . GLN   U  7  37  ? 34.853  -221.328 54.265  1.00 117.09 ? 28  GLN   U CG  1 
ATOM   36037 C  CD  . GLN   U  7  37  ? 36.010  -220.597 54.904  1.00 122.10 ? 28  GLN   U CD  1 
ATOM   36038 O  OE1 . GLN   U  7  37  ? 36.169  -219.389 54.743  1.00 121.95 ? 28  GLN   U OE1 1 
ATOM   36039 N  NE2 . GLN   U  7  37  ? 36.843  -221.333 55.625  1.00 134.14 ? 28  GLN   U NE2 1 
ATOM   36040 N  N   . THR   U  7  38  ? 32.750  -220.322 57.891  1.00 105.22 ? 29  THR   U N   1 
ATOM   36041 C  CA  . THR   U  7  38  ? 33.215  -219.880 59.237  1.00 105.97 ? 29  THR   U CA  1 
ATOM   36042 C  C   . THR   U  7  38  ? 32.706  -220.815 60.340  1.00 102.78 ? 29  THR   U C   1 
ATOM   36043 O  O   . THR   U  7  38  ? 33.230  -220.712 61.465  1.00 101.07 ? 29  THR   U O   1 
ATOM   36044 C  CB  . THR   U  7  38  ? 32.762  -218.448 59.551  1.00 106.44 ? 29  THR   U CB  1 
ATOM   36045 O  OG1 . THR   U  7  38  ? 31.336  -218.392 59.481  1.00 108.76 ? 29  THR   U OG1 1 
ATOM   36046 C  CG2 . THR   U  7  38  ? 33.363  -217.433 58.606  1.00 105.32 ? 29  THR   U CG2 1 
ATOM   36047 N  N   . ASN   U  7  39  ? 31.715  -221.662 60.040  1.00 104.95 ? 30  ASN   U N   1 
ATOM   36048 C  CA  . ASN   U  7  39  ? 31.116  -222.639 60.990  1.00 104.76 ? 30  ASN   U CA  1 
ATOM   36049 C  C   . ASN   U  7  39  ? 30.604  -221.892 62.229  1.00 105.82 ? 30  ASN   U C   1 
ATOM   36050 O  O   . ASN   U  7  39  ? 30.865  -222.356 63.357  1.00 107.92 ? 30  ASN   U O   1 
ATOM   36051 C  CB  . ASN   U  7  39  ? 32.113  -223.744 61.353  1.00 104.03 ? 30  ASN   U CB  1 
ATOM   36052 C  CG  . ASN   U  7  39  ? 31.478  -224.882 62.120  1.00 103.39 ? 30  ASN   U CG  1 
ATOM   36053 O  OD1 . ASN   U  7  39  ? 31.951  -225.243 63.194  1.00 105.65 ? 30  ASN   U OD1 1 
ATOM   36054 N  ND2 . ASN   U  7  39  ? 30.403  -225.442 61.588  1.00 103.13 ? 30  ASN   U ND2 1 
ATOM   36055 N  N   . ILE   U  7  40  ? 29.908  -220.771 62.014  1.00 106.07 ? 31  ILE   U N   1 
ATOM   36056 C  CA  . ILE   U  7  40  ? 29.321  -219.902 63.077  1.00 108.75 ? 31  ILE   U CA  1 
ATOM   36057 C  C   . ILE   U  7  40  ? 27.813  -219.795 62.835  1.00 108.26 ? 31  ILE   U C   1 
ATOM   36058 O  O   . ILE   U  7  40  ? 27.420  -219.580 61.670  1.00 110.69 ? 31  ILE   U O   1 
ATOM   36059 C  CB  . ILE   U  7  40  ? 29.998  -218.514 63.076  1.00 111.45 ? 31  ILE   U CB  1 
ATOM   36060 C  CG1 . ILE   U  7  40  ? 31.447  -218.581 63.572  1.00 113.61 ? 31  ILE   U CG1 1 
ATOM   36061 C  CG2 . ILE   U  7  40  ? 29.178  -217.496 63.857  1.00 114.10 ? 31  ILE   U CG2 1 
ATOM   36062 C  CD1 . ILE   U  7  40  ? 31.602  -219.020 65.013  1.00 115.00 ? 31  ILE   U CD1 1 
ATOM   36063 N  N   . ASN   U  7  41  ? 27.012  -219.920 63.898  1.00 105.85 ? 32  ASN   U N   1 
ATOM   36064 C  CA  . ASN   U  7  41  ? 25.535  -219.750 63.856  1.00 107.82 ? 32  ASN   U CA  1 
ATOM   36065 C  C   . ASN   U  7  41  ? 25.160  -218.412 64.499  1.00 109.86 ? 32  ASN   U C   1 
ATOM   36066 O  O   . ASN   U  7  41  ? 25.700  -218.103 65.584  1.00 104.88 ? 32  ASN   U O   1 
ATOM   36067 C  CB  . ASN   U  7  41  ? 24.798  -220.903 64.539  1.00 109.36 ? 32  ASN   U CB  1 
ATOM   36068 C  CG  . ASN   U  7  41  ? 24.937  -222.208 63.786  1.00 111.12 ? 32  ASN   U CG  1 
ATOM   36069 O  OD1 . ASN   U  7  41  ? 24.263  -222.420 62.780  1.00 109.63 ? 32  ASN   U OD1 1 
ATOM   36070 N  ND2 . ASN   U  7  41  ? 25.806  -223.085 64.262  1.00 114.90 ? 32  ASN   U ND2 1 
ATOM   36071 N  N   . SER   U  7  42  ? 24.262  -217.663 63.848  1.00 110.06 ? 33  SER   U N   1 
ATOM   36072 C  CA  . SER   U  7  42  ? 23.703  -216.371 64.327  1.00 110.79 ? 33  SER   U CA  1 
ATOM   36073 C  C   . SER   U  7  42  ? 22.192  -216.515 64.536  1.00 108.71 ? 33  SER   U C   1 
ATOM   36074 O  O   . SER   U  7  42  ? 21.594  -217.451 63.974  1.00 107.85 ? 33  SER   U O   1 
ATOM   36075 C  CB  . SER   U  7  42  ? 24.038  -215.234 63.385  1.00 114.23 ? 33  SER   U CB  1 
ATOM   36076 O  OG  . SER   U  7  42  ? 23.133  -215.176 62.288  1.00 111.67 ? 33  SER   U OG  1 
ATOM   36077 N  N   . LEU   U  7  43  ? 21.613  -215.613 65.329  1.00 107.73 ? 34  LEU   U N   1 
ATOM   36078 C  CA  . LEU   U  7  43  ? 20.187  -215.627 65.745  1.00 105.79 ? 34  LEU   U CA  1 
ATOM   36079 C  C   . LEU   U  7  43  ? 19.757  -214.181 66.019  1.00 102.91 ? 34  LEU   U C   1 
ATOM   36080 O  O   . LEU   U  7  43  ? 20.540  -213.449 66.654  1.00 106.81 ? 34  LEU   U O   1 
ATOM   36081 C  CB  . LEU   U  7  43  ? 20.066  -216.520 66.987  1.00 105.37 ? 34  LEU   U CB  1 
ATOM   36082 C  CG  . LEU   U  7  43  ? 18.718  -216.542 67.713  1.00 106.48 ? 34  LEU   U CG  1 
ATOM   36083 C  CD1 . LEU   U  7  43  ? 18.587  -217.801 68.553  1.00 106.82 ? 34  LEU   U CD1 1 
ATOM   36084 C  CD2 . LEU   U  7  43  ? 18.530  -215.321 68.602  1.00 107.30 ? 34  LEU   U CD2 1 
ATOM   36085 N  N   . ALA   U  7  44  ? 18.576  -213.783 65.541  1.00 100.56 ? 35  ALA   U N   1 
ATOM   36086 C  CA  . ALA   U  7  44  ? 17.965  -212.463 65.816  1.00 98.53  ? 35  ALA   U CA  1 
ATOM   36087 C  C   . ALA   U  7  44  ? 16.525  -212.656 66.299  1.00 97.32  ? 35  ALA   U C   1 
ATOM   36088 O  O   . ALA   U  7  44  ? 15.809  -213.501 65.725  1.00 96.07  ? 35  ALA   U O   1 
ATOM   36089 C  CB  . ALA   U  7  44  ? 18.027  -211.591 64.586  1.00 98.19  ? 35  ALA   U CB  1 
ATOM   36090 N  N   . VAL   U  7  45  ? 16.133  -211.900 67.328  1.00 97.44  ? 36  VAL   U N   1 
ATOM   36091 C  CA  . VAL   U  7  45  ? 14.742  -211.847 67.865  1.00 97.61  ? 36  VAL   U CA  1 
ATOM   36092 C  C   . VAL   U  7  45  ? 14.385  -210.391 68.166  1.00 96.98  ? 36  VAL   U C   1 
ATOM   36093 O  O   . VAL   U  7  45  ? 15.307  -209.556 68.277  1.00 94.42  ? 36  VAL   U O   1 
ATOM   36094 C  CB  . VAL   U  7  45  ? 14.575  -212.721 69.120  1.00 97.61  ? 36  VAL   U CB  1 
ATOM   36095 C  CG1 . VAL   U  7  45  ? 14.568  -214.198 68.768  1.00 99.48  ? 36  VAL   U CG1 1 
ATOM   36096 C  CG2 . VAL   U  7  45  ? 15.631  -212.416 70.172  1.00 96.27  ? 36  VAL   U CG2 1 
ATOM   36097 N  N   . ARG   U  7  46  ? 13.087  -210.119 68.309  1.00 99.29  ? 37  ARG   U N   1 
ATOM   36098 C  CA  . ARG   U  7  46  ? 12.540  -208.768 68.587  1.00 100.23 ? 37  ARG   U CA  1 
ATOM   36099 C  C   . ARG   U  7  46  ? 11.814  -208.783 69.931  1.00 105.10 ? 37  ARG   U C   1 
ATOM   36100 O  O   . ARG   U  7  46  ? 11.040  -209.732 70.171  1.00 105.17 ? 37  ARG   U O   1 
ATOM   36101 C  CB  . ARG   U  7  46  ? 11.556  -208.348 67.496  1.00 100.39 ? 37  ARG   U CB  1 
ATOM   36102 C  CG  . ARG   U  7  46  ? 12.111  -208.433 66.083  1.00 98.85  ? 37  ARG   U CG  1 
ATOM   36103 C  CD  . ARG   U  7  46  ? 11.101  -207.926 65.075  1.00 100.37 ? 37  ARG   U CD  1 
ATOM   36104 N  NE  . ARG   U  7  46  ? 9.833   -208.639 65.169  1.00 100.98 ? 37  ARG   U NE  1 
ATOM   36105 C  CZ  . ARG   U  7  46  ? 8.709   -208.281 64.557  1.00 103.27 ? 37  ARG   U CZ  1 
ATOM   36106 N  NH1 . ARG   U  7  46  ? 8.676   -207.205 63.786  1.00 105.01 ? 37  ARG   U NH1 1 
ATOM   36107 N  NH2 . ARG   U  7  46  ? 7.615   -209.003 64.720  1.00 103.19 ? 37  ARG   U NH2 1 
ATOM   36108 N  N   . GLY   U  7  47  ? 12.065  -207.764 70.758  1.00 108.17 ? 38  GLY   U N   1 
ATOM   36109 C  CA  . GLY   U  7  47  ? 11.279  -207.454 71.967  1.00 108.30 ? 38  GLY   U CA  1 
ATOM   36110 C  C   . GLY   U  7  47  ? 10.196  -206.441 71.651  1.00 108.18 ? 38  GLY   U C   1 
ATOM   36111 O  O   . GLY   U  7  47  ? 9.899   -206.251 70.456  1.00 106.99 ? 38  GLY   U O   1 
ATOM   36112 N  N   . LYS   U  7  48  ? 9.622   -205.814 72.679  1.00 111.90 ? 39  LYS   U N   1 
ATOM   36113 C  CA  . LYS   U  7  48  ? 8.658   -204.693 72.528  1.00 114.90 ? 39  LYS   U CA  1 
ATOM   36114 C  C   . LYS   U  7  48  ? 9.422   -203.433 72.109  1.00 112.75 ? 39  LYS   U C   1 
ATOM   36115 O  O   . LYS   U  7  48  ? 8.994   -202.782 71.140  1.00 112.12 ? 39  LYS   U O   1 
ATOM   36116 C  CB  . LYS   U  7  48  ? 7.895   -204.455 73.834  1.00 122.99 ? 39  LYS   U CB  1 
ATOM   36117 C  CG  . LYS   U  7  48  ? 6.806   -205.474 74.138  1.00 128.80 ? 39  LYS   U CG  1 
ATOM   36118 C  CD  . LYS   U  7  48  ? 6.461   -205.570 75.610  1.00 132.63 ? 39  LYS   U CD  1 
ATOM   36119 C  CE  . LYS   U  7  48  ? 5.920   -204.280 76.193  1.00 136.62 ? 39  LYS   U CE  1 
ATOM   36120 N  NZ  . LYS   U  7  48  ? 4.547   -203.991 75.715  1.00 140.75 ? 39  LYS   U NZ  1 
ATOM   36121 N  N   . ASP   U  7  49  ? 10.521  -203.131 72.809  1.00 113.74 ? 40  ASP   U N   1 
ATOM   36122 C  CA  . ASP   U  7  49  ? 11.284  -201.859 72.694  1.00 114.60 ? 40  ASP   U CA  1 
ATOM   36123 C  C   . ASP   U  7  49  ? 12.577  -202.056 71.894  1.00 110.32 ? 40  ASP   U C   1 
ATOM   36124 O  O   . ASP   U  7  49  ? 13.153  -201.040 71.477  1.00 111.67 ? 40  ASP   U O   1 
ATOM   36125 C  CB  . ASP   U  7  49  ? 11.610  -201.290 74.080  1.00 121.42 ? 40  ASP   U CB  1 
ATOM   36126 C  CG  . ASP   U  7  49  ? 10.502  -200.447 74.692  1.00 128.79 ? 40  ASP   U CG  1 
ATOM   36127 O  OD1 . ASP   U  7  49  ? 9.359   -200.521 74.198  1.00 136.17 ? 40  ASP   U OD1 1 
ATOM   36128 O  OD2 . ASP   U  7  49  ? 10.794  -199.716 75.661  1.00 137.51 ? 40  ASP   U OD2 1 
ATOM   36129 N  N   . CYS   U  7  50  ? 13.031  -203.294 71.688  1.00 109.11 ? 41  CYS   U N   1 
ATOM   36130 C  CA  . CYS   U  7  50  ? 14.404  -203.580 71.194  1.00 108.36 ? 41  CYS   U CA  1 
ATOM   36131 C  C   . CYS   U  7  50  ? 14.415  -204.723 70.174  1.00 108.75 ? 41  CYS   U C   1 
ATOM   36132 O  O   . CYS   U  7  50  ? 13.395  -205.434 70.041  1.00 107.57 ? 41  CYS   U O   1 
ATOM   36133 C  CB  . CYS   U  7  50  ? 15.326  -203.935 72.353  1.00 111.57 ? 41  CYS   U CB  1 
ATOM   36134 S  SG  . CYS   U  7  50  ? 14.795  -205.416 73.249  1.00 112.08 ? 41  CYS   U SG  1 
ATOM   36135 N  N   . THR   U  7  51  ? 15.549  -204.861 69.482  1.00 103.44 ? 42  THR   U N   1 
ATOM   36136 C  CA  . THR   U  7  51  ? 15.902  -205.996 68.592  1.00 102.95 ? 42  THR   U CA  1 
ATOM   36137 C  C   . THR   U  7  51  ? 17.276  -206.521 69.021  1.00 102.73 ? 42  THR   U C   1 
ATOM   36138 O  O   . THR   U  7  51  ? 18.250  -205.749 68.951  1.00 99.42  ? 42  THR   U O   1 
ATOM   36139 C  CB  . THR   U  7  51  ? 15.889  -205.578 67.116  1.00 101.92 ? 42  THR   U CB  1 
ATOM   36140 O  OG1 . THR   U  7  51  ? 14.656  -204.910 66.847  1.00 101.20 ? 42  THR   U OG1 1 
ATOM   36141 C  CG2 . THR   U  7  51  ? 16.042  -206.752 66.173  1.00 102.36 ? 42  THR   U CG2 1 
ATOM   36142 N  N   . VAL   U  7  52  ? 17.337  -207.778 69.468  1.00 104.96 ? 43  VAL   U N   1 
ATOM   36143 C  CA  . VAL   U  7  52  ? 18.592  -208.450 69.914  1.00 105.78 ? 43  VAL   U CA  1 
ATOM   36144 C  C   . VAL   U  7  52  ? 19.071  -209.381 68.799  1.00 102.74 ? 43  VAL   U C   1 
ATOM   36145 O  O   . VAL   U  7  52  ? 18.245  -210.157 68.277  1.00 103.24 ? 43  VAL   U O   1 
ATOM   36146 C  CB  . VAL   U  7  52  ? 18.392  -209.230 71.226  1.00 107.59 ? 43  VAL   U CB  1 
ATOM   36147 C  CG1 . VAL   U  7  52  ? 19.648  -209.999 71.609  1.00 108.68 ? 43  VAL   U CG1 1 
ATOM   36148 C  CG2 . VAL   U  7  52  ? 17.951  -208.319 72.361  1.00 109.98 ? 43  VAL   U CG2 1 
ATOM   36149 N  N   . VAL   U  7  53  ? 20.360  -209.297 68.466  1.00 99.71  ? 44  VAL   U N   1 
ATOM   36150 C  CA  . VAL   U  7  53  ? 21.067  -210.268 67.584  1.00 98.89  ? 44  VAL   U CA  1 
ATOM   36151 C  C   . VAL   U  7  53  ? 22.210  -210.887 68.396  1.00 99.84  ? 44  VAL   U C   1 
ATOM   36152 O  O   . VAL   U  7  53  ? 22.927  -210.124 69.072  1.00 96.44  ? 44  VAL   U O   1 
ATOM   36153 C  CB  . VAL   U  7  53  ? 21.556  -209.605 66.280  1.00 99.35  ? 44  VAL   U CB  1 
ATOM   36154 C  CG1 . VAL   U  7  53  ? 22.732  -208.664 66.495  1.00 98.53  ? 44  VAL   U CG1 1 
ATOM   36155 C  CG2 . VAL   U  7  53  ? 21.895  -210.642 65.225  1.00 100.84 ? 44  VAL   U CG2 1 
ATOM   36156 N  N   . ILE   U  7  54  ? 22.335  -212.219 68.367  1.00 101.80 ? 45  ILE   U N   1 
ATOM   36157 C  CA  . ILE   U  7  54  ? 23.464  -212.975 68.990  1.00 101.74 ? 45  ILE   U CA  1 
ATOM   36158 C  C   . ILE   U  7  54  ? 24.105  -213.882 67.934  1.00 100.88 ? 45  ILE   U C   1 
ATOM   36159 O  O   . ILE   U  7  54  ? 23.393  -214.357 67.025  1.00 96.11  ? 45  ILE   U O   1 
ATOM   36160 C  CB  . ILE   U  7  54  ? 23.019  -213.777 70.231  1.00 103.84 ? 45  ILE   U CB  1 
ATOM   36161 C  CG1 . ILE   U  7  54  ? 22.061  -214.915 69.876  1.00 103.48 ? 45  ILE   U CG1 1 
ATOM   36162 C  CG2 . ILE   U  7  54  ? 22.427  -212.853 71.283  1.00 105.20 ? 45  ILE   U CG2 1 
ATOM   36163 C  CD1 . ILE   U  7  54  ? 21.923  -215.950 70.961  1.00 105.04 ? 45  ILE   U CD1 1 
ATOM   36164 N  N   . SER   U  7  55  ? 25.409  -214.109 68.076  1.00 101.36 ? 46  SER   U N   1 
ATOM   36165 C  CA  . SER   U  7  55  ? 26.243  -214.926 67.162  1.00 102.68 ? 46  SER   U CA  1 
ATOM   36166 C  C   . SER   U  7  55  ? 27.300  -215.658 67.991  1.00 102.53 ? 46  SER   U C   1 
ATOM   36167 O  O   . SER   U  7  55  ? 27.742  -215.102 69.014  1.00 104.61 ? 46  SER   U O   1 
ATOM   36168 C  CB  . SER   U  7  55  ? 26.856  -214.062 66.085  1.00 103.63 ? 46  SER   U CB  1 
ATOM   36169 O  OG  . SER   U  7  55  ? 27.727  -214.813 65.252  1.00 107.83 ? 46  SER   U OG  1 
ATOM   36170 N  N   . GLN   U  7  56  ? 27.664  -216.874 67.583  1.00 102.64 ? 47  GLN   U N   1 
ATOM   36171 C  CA  . GLN   U  7  56  ? 28.766  -217.641 68.213  1.00 104.40 ? 47  GLN   U CA  1 
ATOM   36172 C  C   . GLN   U  7  56  ? 30.077  -216.890 67.963  1.00 103.32 ? 47  GLN   U C   1 
ATOM   36173 O  O   . GLN   U  7  56  ? 30.197  -216.245 66.906  1.00 103.33 ? 47  GLN   U O   1 
ATOM   36174 C  CB  . GLN   U  7  56  ? 28.838  -219.064 67.656  1.00 106.33 ? 47  GLN   U CB  1 
ATOM   36175 C  CG  . GLN   U  7  56  ? 27.628  -219.921 67.995  1.00 106.64 ? 47  GLN   U CG  1 
ATOM   36176 C  CD  . GLN   U  7  56  ? 27.790  -221.333 67.483  1.00 106.50 ? 47  GLN   U CD  1 
ATOM   36177 O  OE1 . GLN   U  7  56  ? 27.227  -221.715 66.460  1.00 106.11 ? 47  GLN   U OE1 1 
ATOM   36178 N  NE2 . GLN   U  7  56  ? 28.587  -222.121 68.185  1.00 107.42 ? 47  GLN   U NE2 1 
ATOM   36179 N  N   . LYS   U  7  57  ? 31.008  -216.964 68.914  1.00 105.88 ? 48  LYS   U N   1 
ATOM   36180 C  CA  . LYS   U  7  57  ? 32.373  -216.391 68.800  1.00 108.42 ? 48  LYS   U CA  1 
ATOM   36181 C  C   . LYS   U  7  57  ? 33.388  -217.507 69.053  1.00 108.74 ? 48  LYS   U C   1 
ATOM   36182 O  O   . LYS   U  7  57  ? 33.603  -217.852 70.232  1.00 111.59 ? 48  LYS   U O   1 
ATOM   36183 C  CB  . LYS   U  7  57  ? 32.561  -215.240 69.791  1.00 110.05 ? 48  LYS   U CB  1 
ATOM   36184 C  CG  . LYS   U  7  57  ? 33.935  -214.586 69.755  1.00 112.91 ? 48  LYS   U CG  1 
ATOM   36185 C  CD  . LYS   U  7  57  ? 34.029  -213.348 70.612  1.00 115.46 ? 48  LYS   U CD  1 
ATOM   36186 C  CE  . LYS   U  7  57  ? 35.379  -212.673 70.517  1.00 117.47 ? 48  LYS   U CE  1 
ATOM   36187 N  NZ  . LYS   U  7  57  ? 35.354  -211.326 71.134  1.00 119.21 ? 48  LYS   U NZ  1 
ATOM   36188 N  N   . LYS   U  7  58  ? 33.969  -218.052 67.983  1.00 109.14 ? 49  LYS   U N   1 
ATOM   36189 C  CA  . LYS   U  7  58  ? 35.000  -219.120 68.048  1.00 109.31 ? 49  LYS   U CA  1 
ATOM   36190 C  C   . LYS   U  7  58  ? 36.366  -218.495 67.753  1.00 107.83 ? 49  LYS   U C   1 
ATOM   36191 O  O   . LYS   U  7  58  ? 36.591  -218.067 66.605  1.00 107.54 ? 49  LYS   U O   1 
ATOM   36192 C  CB  . LYS   U  7  58  ? 34.642  -220.260 67.090  1.00 109.95 ? 49  LYS   U CB  1 
ATOM   36193 C  CG  . LYS   U  7  58  ? 33.378  -221.022 67.468  1.00 111.20 ? 49  LYS   U CG  1 
ATOM   36194 C  CD  . LYS   U  7  58  ? 33.022  -222.149 66.525  1.00 110.77 ? 49  LYS   U CD  1 
ATOM   36195 C  CE  . LYS   U  7  58  ? 31.710  -222.811 66.883  1.00 109.61 ? 49  LYS   U CE  1 
ATOM   36196 N  NZ  . LYS   U  7  58  ? 31.357  -223.880 65.921  1.00 111.69 ? 49  LYS   U NZ  1 
ATOM   36197 N  N   . VAL   U  7  59  ? 37.216  -218.409 68.778  1.00 108.42 ? 50  VAL   U N   1 
ATOM   36198 C  CA  . VAL   U  7  59  ? 38.635  -217.961 68.674  1.00 112.56 ? 50  VAL   U CA  1 
ATOM   36199 C  C   . VAL   U  7  59  ? 39.519  -219.183 68.908  1.00 115.79 ? 50  VAL   U C   1 
ATOM   36200 O  O   . VAL   U  7  59  ? 39.859  -219.497 70.048  1.00 117.36 ? 50  VAL   U O   1 
ATOM   36201 C  CB  . VAL   U  7  59  ? 38.943  -216.824 69.666  1.00 110.02 ? 50  VAL   U CB  1 
ATOM   36202 C  CG1 . VAL   U  7  59  ? 40.295  -216.189 69.379  1.00 111.09 ? 50  VAL   U CG1 1 
ATOM   36203 C  CG2 . VAL   U  7  59  ? 37.849  -215.766 69.673  1.00 108.63 ? 50  VAL   U CG2 1 
ATOM   36204 N  N   . PRO   U  7  60  ? 39.893  -219.928 67.840  1.00 119.64 ? 51  PRO   U N   1 
ATOM   36205 C  CA  . PRO   U  7  60  ? 40.667  -221.160 67.993  1.00 123.05 ? 51  PRO   U CA  1 
ATOM   36206 C  C   . PRO   U  7  60  ? 42.137  -220.901 68.356  1.00 122.35 ? 51  PRO   U C   1 
ATOM   36207 O  O   . PRO   U  7  60  ? 42.654  -221.605 69.201  1.00 120.54 ? 51  PRO   U O   1 
ATOM   36208 C  CB  . PRO   U  7  60  ? 40.552  -221.831 66.615  1.00 121.85 ? 51  PRO   U CB  1 
ATOM   36209 C  CG  . PRO   U  7  60  ? 40.347  -220.682 65.649  1.00 121.53 ? 51  PRO   U CG  1 
ATOM   36210 C  CD  . PRO   U  7  60  ? 39.587  -219.629 66.431  1.00 121.34 ? 51  PRO   U CD  1 
ATOM   36211 N  N   . ASP   U  7  61  ? 42.762  -219.906 67.715  1.00 128.90 ? 52  ASP   U N   1 
ATOM   36212 C  CA  . ASP   U  7  61  ? 44.199  -219.558 67.895  1.00 130.42 ? 52  ASP   U CA  1 
ATOM   36213 C  C   . ASP   U  7  61  ? 44.361  -218.801 69.220  1.00 125.77 ? 52  ASP   U C   1 
ATOM   36214 O  O   . ASP   U  7  61  ? 43.553  -217.888 69.490  1.00 122.24 ? 52  ASP   U O   1 
ATOM   36215 C  CB  . ASP   U  7  61  ? 44.724  -218.759 66.695  1.00 131.35 ? 52  ASP   U CB  1 
ATOM   36216 C  CG  . ASP   U  7  61  ? 46.240  -218.672 66.589  1.00 133.37 ? 52  ASP   U CG  1 
ATOM   36217 O  OD1 . ASP   U  7  61  ? 46.920  -218.881 67.615  1.00 141.49 ? 52  ASP   U OD1 1 
ATOM   36218 O  OD2 . ASP   U  7  61  ? 46.732  -218.390 65.475  1.00 127.54 ? 52  ASP   U OD2 1 
ATOM   36219 N  N   . LYS   U  7  62  ? 45.371  -219.179 70.011  1.00 127.38 ? 53  LYS   U N   1 
ATOM   36220 C  CA  . LYS   U  7  62  ? 45.700  -218.566 71.328  1.00 124.76 ? 53  LYS   U CA  1 
ATOM   36221 C  C   . LYS   U  7  62  ? 46.456  -217.247 71.105  1.00 120.41 ? 53  LYS   U C   1 
ATOM   36222 O  O   . LYS   U  7  62  ? 46.501  -216.433 72.048  1.00 115.48 ? 53  LYS   U O   1 
ATOM   36223 C  CB  . LYS   U  7  62  ? 46.527  -219.542 72.175  1.00 129.07 ? 53  LYS   U CB  1 
ATOM   36224 C  CG  . LYS   U  7  62  ? 46.051  -219.725 73.610  1.00 131.23 ? 53  LYS   U CG  1 
ATOM   36225 C  CD  . LYS   U  7  62  ? 47.094  -220.339 74.523  1.00 135.99 ? 53  LYS   U CD  1 
ATOM   36226 C  CE  . LYS   U  7  62  ? 47.464  -221.757 74.141  1.00 137.52 ? 53  LYS   U CE  1 
ATOM   36227 N  NZ  . LYS   U  7  62  ? 48.704  -222.202 74.819  1.00 143.72 ? 53  LYS   U NZ  1 
ATOM   36228 N  N   . LEU   U  7  63  ? 47.029  -217.055 69.909  1.00 116.96 ? 54  LEU   U N   1 
ATOM   36229 C  CA  . LEU   U  7  63  ? 47.841  -215.862 69.535  1.00 117.34 ? 54  LEU   U CA  1 
ATOM   36230 C  C   . LEU   U  7  63  ? 46.939  -214.712 69.064  1.00 115.49 ? 54  LEU   U C   1 
ATOM   36231 O  O   . LEU   U  7  63  ? 47.433  -213.567 69.024  1.00 112.79 ? 54  LEU   U O   1 
ATOM   36232 C  CB  . LEU   U  7  63  ? 48.832  -216.243 68.429  1.00 116.39 ? 54  LEU   U CB  1 
ATOM   36233 C  CG  . LEU   U  7  63  ? 49.916  -217.249 68.807  1.00 118.07 ? 54  LEU   U CG  1 
ATOM   36234 C  CD1 . LEU   U  7  63  ? 50.866  -217.475 67.639  1.00 119.10 ? 54  LEU   U CD1 1 
ATOM   36235 C  CD2 . LEU   U  7  63  ? 50.686  -216.796 70.039  1.00 118.84 ? 54  LEU   U CD2 1 
ATOM   36236 N  N   . LEU   U  7  64  ? 45.686  -214.994 68.691  1.00 116.95 ? 55  LEU   U N   1 
ATOM   36237 C  CA  . LEU   U  7  64  ? 44.710  -213.953 68.269  1.00 115.25 ? 55  LEU   U CA  1 
ATOM   36238 C  C   . LEU   U  7  64  ? 44.424  -213.025 69.454  1.00 114.81 ? 55  LEU   U C   1 
ATOM   36239 O  O   . LEU   U  7  64  ? 44.415  -213.510 70.605  1.00 113.58 ? 55  LEU   U O   1 
ATOM   36240 C  CB  . LEU   U  7  64  ? 43.409  -214.601 67.779  1.00 116.27 ? 55  LEU   U CB  1 
ATOM   36241 C  CG  . LEU   U  7  64  ? 43.445  -215.213 66.379  1.00 120.26 ? 55  LEU   U CG  1 
ATOM   36242 C  CD1 . LEU   U  7  64  ? 42.261  -216.151 66.171  1.00 123.53 ? 55  LEU   U CD1 1 
ATOM   36243 C  CD2 . LEU   U  7  64  ? 43.460  -214.133 65.309  1.00 117.19 ? 55  LEU   U CD2 1 
ATOM   36244 N  N   . ASP   U  7  65  ? 44.210  -211.739 69.168  1.00 114.61 ? 56  ASP   U N   1 
ATOM   36245 C  CA  . ASP   U  7  65  ? 43.592  -210.760 70.098  1.00 112.68 ? 56  ASP   U CA  1 
ATOM   36246 C  C   . ASP   U  7  65  ? 42.079  -210.935 70.001  1.00 108.55 ? 56  ASP   U C   1 
ATOM   36247 O  O   . ASP   U  7  65  ? 41.475  -210.541 69.005  1.00 102.40 ? 56  ASP   U O   1 
ATOM   36248 C  CB  . ASP   U  7  65  ? 44.015  -209.327 69.766  1.00 112.14 ? 56  ASP   U CB  1 
ATOM   36249 C  CG  . ASP   U  7  65  ? 43.435  -208.275 70.695  1.00 115.25 ? 56  ASP   U CG  1 
ATOM   36250 O  OD1 . ASP   U  7  65  ? 42.682  -208.654 71.619  1.00 114.16 ? 56  ASP   U OD1 1 
ATOM   36251 O  OD2 . ASP   U  7  65  ? 43.739  -207.082 70.485  1.00 112.96 ? 56  ASP   U OD2 1 
ATOM   36252 N  N   . PRO   U  7  66  ? 41.422  -211.536 71.021  1.00 109.46 ? 57  PRO   U N   1 
ATOM   36253 C  CA  . PRO   U  7  66  ? 40.007  -211.903 70.915  1.00 108.64 ? 57  PRO   U CA  1 
ATOM   36254 C  C   . PRO   U  7  66  ? 39.061  -210.710 70.700  1.00 108.20 ? 57  PRO   U C   1 
ATOM   36255 O  O   . PRO   U  7  66  ? 38.002  -210.912 70.131  1.00 105.40 ? 57  PRO   U O   1 
ATOM   36256 C  CB  . PRO   U  7  66  ? 39.706  -212.594 72.255  1.00 110.64 ? 57  PRO   U CB  1 
ATOM   36257 C  CG  . PRO   U  7  66  ? 40.767  -212.067 73.196  1.00 111.93 ? 57  PRO   U CG  1 
ATOM   36258 C  CD  . PRO   U  7  66  ? 41.994  -211.881 72.330  1.00 111.25 ? 57  PRO   U CD  1 
ATOM   36259 N  N   . THR   U  7  67  ? 39.463  -209.510 71.133  1.00 107.07 ? 58  THR   U N   1 
ATOM   36260 C  CA  . THR   U  7  67  ? 38.647  -208.266 71.051  1.00 104.68 ? 58  THR   U CA  1 
ATOM   36261 C  C   . THR   U  7  67  ? 38.463  -207.834 69.588  1.00 99.47  ? 58  THR   U C   1 
ATOM   36262 O  O   . THR   U  7  67  ? 37.471  -207.136 69.318  1.00 98.82  ? 58  THR   U O   1 
ATOM   36263 C  CB  . THR   U  7  67  ? 39.256  -207.140 71.900  1.00 106.31 ? 58  THR   U CB  1 
ATOM   36264 O  OG1 . THR   U  7  67  ? 40.631  -206.983 71.549  1.00 109.68 ? 58  THR   U OG1 1 
ATOM   36265 C  CG2 . THR   U  7  67  ? 39.153  -207.406 73.385  1.00 107.44 ? 58  THR   U CG2 1 
ATOM   36266 N  N   . THR   U  7  68  ? 39.365  -208.240 68.685  1.00 98.03  ? 59  THR   U N   1 
ATOM   36267 C  CA  . THR   U  7  68  ? 39.373  -207.846 67.250  1.00 96.34  ? 59  THR   U CA  1 
ATOM   36268 C  C   . THR   U  7  68  ? 38.610  -208.864 66.396  1.00 98.28  ? 59  THR   U C   1 
ATOM   36269 O  O   . THR   U  7  68  ? 38.370  -208.557 65.215  1.00 95.67  ? 59  THR   U O   1 
ATOM   36270 C  CB  . THR   U  7  68  ? 40.804  -207.676 66.726  1.00 97.24  ? 59  THR   U CB  1 
ATOM   36271 O  OG1 . THR   U  7  68  ? 41.450  -208.948 66.739  1.00 97.38  ? 59  THR   U OG1 1 
ATOM   36272 C  CG2 . THR   U  7  68  ? 41.600  -206.672 67.531  1.00 99.31  ? 59  THR   U CG2 1 
ATOM   36273 N  N   . VAL   U  7  69  ? 38.258  -210.026 66.956  1.00 98.80  ? 60  VAL   U N   1 
ATOM   36274 C  CA  . VAL   U  7  69  ? 37.447  -211.070 66.258  1.00 100.50 ? 60  VAL   U CA  1 
ATOM   36275 C  C   . VAL   U  7  69  ? 35.965  -210.732 66.460  1.00 101.48 ? 60  VAL   U C   1 
ATOM   36276 O  O   . VAL   U  7  69  ? 35.466  -210.915 67.588  1.00 102.77 ? 60  VAL   U O   1 
ATOM   36277 C  CB  . VAL   U  7  69  ? 37.786  -212.492 66.748  1.00 102.03 ? 60  VAL   U CB  1 
ATOM   36278 C  CG1 . VAL   U  7  69  ? 36.959  -213.547 66.026  1.00 102.15 ? 60  VAL   U CG1 1 
ATOM   36279 C  CG2 . VAL   U  7  69  ? 39.271  -212.798 66.611  1.00 101.32 ? 60  VAL   U CG2 1 
ATOM   36280 N  N   . SER   U  7  70  ? 35.296  -210.253 65.407  1.00 100.71 ? 61  SER   U N   1 
ATOM   36281 C  CA  . SER   U  7  70  ? 33.874  -209.819 65.440  1.00 102.20 ? 61  SER   U CA  1 
ATOM   36282 C  C   . SER   U  7  70  ? 33.222  -209.961 64.060  1.00 101.65 ? 61  SER   U C   1 
ATOM   36283 O  O   . SER   U  7  70  ? 33.856  -209.573 63.056  1.00 103.80 ? 61  SER   U O   1 
ATOM   36284 C  CB  . SER   U  7  70  ? 33.764  -208.406 65.936  1.00 103.03 ? 61  SER   U CB  1 
ATOM   36285 O  OG  . SER   U  7  70  ? 32.402  -208.013 66.040  1.00 104.23 ? 61  SER   U OG  1 
ATOM   36286 N  N   . TYR   U  7  71  ? 31.992  -210.481 64.030  1.00 100.20 ? 62  TYR   U N   1 
ATOM   36287 C  CA  . TYR   U  7  71  ? 31.128  -210.577 62.824  1.00 95.93  ? 62  TYR   U CA  1 
ATOM   36288 C  C   . TYR   U  7  71  ? 29.874  -209.715 63.014  1.00 93.15  ? 62  TYR   U C   1 
ATOM   36289 O  O   . TYR   U  7  71  ? 28.969  -209.815 62.169  1.00 94.15  ? 62  TYR   U O   1 
ATOM   36290 C  CB  . TYR   U  7  71  ? 30.789  -212.041 62.530  1.00 95.29  ? 62  TYR   U CB  1 
ATOM   36291 C  CG  . TYR   U  7  71  ? 31.951  -212.838 61.995  1.00 91.81  ? 62  TYR   U CG  1 
ATOM   36292 C  CD1 . TYR   U  7  71  ? 32.850  -213.451 62.850  1.00 91.68  ? 62  TYR   U CD1 1 
ATOM   36293 C  CD2 . TYR   U  7  71  ? 32.172  -212.952 60.631  1.00 91.06  ? 62  TYR   U CD2 1 
ATOM   36294 C  CE1 . TYR   U  7  71  ? 33.930  -214.172 62.366  1.00 92.36  ? 62  TYR   U CE1 1 
ATOM   36295 C  CE2 . TYR   U  7  71  ? 33.248  -213.667 60.131  1.00 89.84  ? 62  TYR   U CE2 1 
ATOM   36296 C  CZ  . TYR   U  7  71  ? 34.132  -214.279 61.001  1.00 91.05  ? 62  TYR   U CZ  1 
ATOM   36297 O  OH  . TYR   U  7  71  ? 35.193  -214.984 60.509  1.00 90.37  ? 62  TYR   U OH  1 
ATOM   36298 N  N   . ILE   U  7  72  ? 29.827  -208.899 64.075  1.00 91.98  ? 63  ILE   U N   1 
ATOM   36299 C  CA  . ILE   U  7  72  ? 28.765  -207.870 64.297  1.00 90.89  ? 63  ILE   U CA  1 
ATOM   36300 C  C   . ILE   U  7  72  ? 29.374  -206.487 64.038  1.00 89.40  ? 63  ILE   U C   1 
ATOM   36301 O  O   . ILE   U  7  72  ? 30.483  -206.227 64.542  1.00 84.28  ? 63  ILE   U O   1 
ATOM   36302 C  CB  . ILE   U  7  72  ? 28.147  -207.992 65.706  1.00 93.85  ? 63  ILE   U CB  1 
ATOM   36303 C  CG1 . ILE   U  7  72  ? 27.494  -209.365 65.896  1.00 92.33  ? 63  ILE   U CG1 1 
ATOM   36304 C  CG2 . ILE   U  7  72  ? 27.174  -206.847 65.969  1.00 94.11  ? 63  ILE   U CG2 1 
ATOM   36305 C  CD1 . ILE   U  7  72  ? 26.645  -209.502 67.140  1.00 93.95  ? 63  ILE   U CD1 1 
ATOM   36306 N  N   . PHE   U  7  73  ? 28.667  -205.646 63.277  1.00 89.53  ? 64  PHE   U N   1 
ATOM   36307 C  CA  . PHE   U  7  73  ? 29.120  -204.298 62.841  1.00 90.02  ? 64  PHE   U CA  1 
ATOM   36308 C  C   . PHE   U  7  73  ? 28.070  -203.243 63.203  1.00 91.40  ? 64  PHE   U C   1 
ATOM   36309 O  O   . PHE   U  7  73  ? 26.860  -203.505 63.052  1.00 87.30  ? 64  PHE   U O   1 
ATOM   36310 C  CB  . PHE   U  7  73  ? 29.389  -204.285 61.334  1.00 89.40  ? 64  PHE   U CB  1 
ATOM   36311 C  CG  . PHE   U  7  73  ? 30.438  -205.268 60.884  1.00 87.44  ? 64  PHE   U CG  1 
ATOM   36312 C  CD1 . PHE   U  7  73  ? 31.763  -204.881 60.753  1.00 87.49  ? 64  PHE   U CD1 1 
ATOM   36313 C  CD2 . PHE   U  7  73  ? 30.102  -206.581 60.598  1.00 87.32  ? 64  PHE   U CD2 1 
ATOM   36314 C  CE1 . PHE   U  7  73  ? 32.728  -205.787 60.342  1.00 87.10  ? 64  PHE   U CE1 1 
ATOM   36315 C  CE2 . PHE   U  7  73  ? 31.068  -207.484 60.185  1.00 88.70  ? 64  PHE   U CE2 1 
ATOM   36316 C  CZ  . PHE   U  7  73  ? 32.379  -207.086 60.058  1.00 88.33  ? 64  PHE   U CZ  1 
ATOM   36317 N  N   . CYS   U  7  74  ? 28.530  -202.078 63.664  1.00 96.44  ? 65  CYS   U N   1 
ATOM   36318 C  CA  . CYS   U  7  74  ? 27.698  -200.864 63.870  1.00 98.86  ? 65  CYS   U CA  1 
ATOM   36319 C  C   . CYS   U  7  74  ? 27.718  -200.043 62.576  1.00 97.58  ? 65  CYS   U C   1 
ATOM   36320 O  O   . CYS   U  7  74  ? 28.700  -199.310 62.357  1.00 104.56 ? 65  CYS   U O   1 
ATOM   36321 C  CB  . CYS   U  7  74  ? 28.196  -200.049 65.058  1.00 101.85 ? 65  CYS   U CB  1 
ATOM   36322 S  SG  . CYS   U  7  74  ? 28.419  -201.043 66.555  1.00 108.23 ? 65  CYS   U SG  1 
ATOM   36323 N  N   . ILE   U  7  75  ? 26.690  -200.199 61.736  1.00 97.03  ? 66  ILE   U N   1 
ATOM   36324 C  CA  . ILE   U  7  75  ? 26.594  -199.550 60.394  1.00 98.25  ? 66  ILE   U CA  1 
ATOM   36325 C  C   . ILE   U  7  75  ? 26.364  -198.050 60.601  1.00 93.96  ? 66  ILE   U C   1 
ATOM   36326 O  O   . ILE   U  7  75  ? 27.125  -197.245 60.038  1.00 95.08  ? 66  ILE   U O   1 
ATOM   36327 C  CB  . ILE   U  7  75  ? 25.481  -200.198 59.543  1.00 99.49  ? 66  ILE   U CB  1 
ATOM   36328 C  CG1 . ILE   U  7  75  ? 25.712  -201.700 59.341  1.00 99.46  ? 66  ILE   U CG1 1 
ATOM   36329 C  CG2 . ILE   U  7  75  ? 25.319  -199.473 58.215  1.00 101.00 ? 66  ILE   U CG2 1 
ATOM   36330 C  CD1 . ILE   U  7  75  ? 27.073  -202.054 58.779  1.00 99.27  ? 66  ILE   U CD1 1 
ATOM   36331 N  N   . SER   U  7  76  ? 25.349  -197.706 61.391  1.00 92.57  ? 67  SER   U N   1 
ATOM   36332 C  CA  . SER   U  7  76  ? 25.003  -196.316 61.776  1.00 94.00  ? 67  SER   U CA  1 
ATOM   36333 C  C   . SER   U  7  76  ? 24.731  -196.276 63.280  1.00 95.04  ? 67  SER   U C   1 
ATOM   36334 O  O   . SER   U  7  76  ? 24.918  -197.314 63.940  1.00 97.52  ? 67  SER   U O   1 
ATOM   36335 C  CB  . SER   U  7  76  ? 23.828  -195.815 60.975  1.00 94.77  ? 67  SER   U CB  1 
ATOM   36336 O  OG  . SER   U  7  76  ? 22.614  -196.397 61.426  1.00 95.87  ? 67  SER   U OG  1 
ATOM   36337 N  N   . ARG   U  7  77  ? 24.310  -195.124 63.802  1.00 96.18  ? 68  ARG   U N   1 
ATOM   36338 C  CA  . ARG   U  7  77  ? 23.940  -194.980 65.231  1.00 97.38  ? 68  ARG   U CA  1 
ATOM   36339 C  C   . ARG   U  7  77  ? 22.750  -195.901 65.531  1.00 93.09  ? 68  ARG   U C   1 
ATOM   36340 O  O   . ARG   U  7  77  ? 22.725  -196.458 66.636  1.00 93.12  ? 68  ARG   U O   1 
ATOM   36341 C  CB  . ARG   U  7  77  ? 23.638  -193.520 65.579  1.00 103.83 ? 68  ARG   U CB  1 
ATOM   36342 C  CG  . ARG   U  7  77  ? 23.621  -193.243 67.075  1.00 110.89 ? 68  ARG   U CG  1 
ATOM   36343 C  CD  . ARG   U  7  77  ? 23.601  -191.759 67.382  1.00 119.35 ? 68  ARG   U CD  1 
ATOM   36344 N  NE  . ARG   U  7  77  ? 24.849  -191.104 67.007  1.00 126.52 ? 68  ARG   U NE  1 
ATOM   36345 C  CZ  . ARG   U  7  77  ? 24.983  -189.806 66.734  1.00 133.95 ? 68  ARG   U CZ  1 
ATOM   36346 N  NH1 . ARG   U  7  77  ? 23.939  -188.992 66.784  1.00 138.44 ? 68  ARG   U NH1 1 
ATOM   36347 N  NH2 . ARG   U  7  77  ? 26.169  -189.324 66.401  1.00 137.99 ? 68  ARG   U NH2 1 
ATOM   36348 N  N   . THR   U  7  78  ? 21.832  -196.088 64.574  1.00 90.74  ? 69  THR   U N   1 
ATOM   36349 C  CA  . THR   U  7  78  ? 20.547  -196.819 64.766  1.00 91.91  ? 69  THR   U CA  1 
ATOM   36350 C  C   . THR   U  7  78  ? 20.605  -198.246 64.200  1.00 91.39  ? 69  THR   U C   1 
ATOM   36351 O  O   . THR   U  7  78  ? 19.850  -199.092 64.723  1.00 89.49  ? 69  THR   U O   1 
ATOM   36352 C  CB  . THR   U  7  78  ? 19.371  -196.039 64.164  1.00 90.80  ? 69  THR   U CB  1 
ATOM   36353 O  OG1 . THR   U  7  78  ? 19.628  -195.767 62.786  1.00 89.80  ? 69  THR   U OG1 1 
ATOM   36354 C  CG2 . THR   U  7  78  ? 19.117  -194.739 64.891  1.00 92.64  ? 69  THR   U CG2 1 
ATOM   36355 N  N   . ILE   U  7  79  ? 21.442  -198.514 63.188  1.00 93.20  ? 70  ILE   U N   1 
ATOM   36356 C  CA  . ILE   U  7  79  ? 21.479  -199.830 62.476  1.00 94.20  ? 70  ILE   U CA  1 
ATOM   36357 C  C   . ILE   U  7  79  ? 22.717  -200.628 62.899  1.00 93.18  ? 70  ILE   U C   1 
ATOM   36358 O  O   . ILE   U  7  79  ? 23.835  -200.071 62.877  1.00 88.96  ? 70  ILE   U O   1 
ATOM   36359 C  CB  . ILE   U  7  79  ? 21.418  -199.659 60.944  1.00 96.60  ? 70  ILE   U CB  1 
ATOM   36360 C  CG1 . ILE   U  7  79  ? 20.058  -199.113 60.503  1.00 100.56 ? 70  ILE   U CG1 1 
ATOM   36361 C  CG2 . ILE   U  7  79  ? 21.748  -200.971 60.243  1.00 96.46  ? 70  ILE   U CG2 1 
ATOM   36362 C  CD1 . ILE   U  7  79  ? 19.973  -198.754 59.036  1.00 103.01 ? 70  ILE   U CD1 1 
ATOM   36363 N  N   . GLY   U  7  80  ? 22.498  -201.903 63.236  1.00 93.97  ? 71  GLY   U N   1 
ATOM   36364 C  CA  . GLY   U  7  80  ? 23.537  -202.933 63.416  1.00 94.67  ? 71  GLY   U CA  1 
ATOM   36365 C  C   . GLY   U  7  80  ? 23.375  -204.037 62.387  1.00 93.45  ? 71  GLY   U C   1 
ATOM   36366 O  O   . GLY   U  7  80  ? 22.246  -204.220 61.888  1.00 94.26  ? 71  GLY   U O   1 
ATOM   36367 N  N   . MET   U  7  81  ? 24.462  -204.745 62.077  1.00 94.49  ? 72  MET   U N   1 
ATOM   36368 C  CA  . MET   U  7  81  ? 24.494  -205.809 61.042  1.00 95.00  ? 72  MET   U CA  1 
ATOM   36369 C  C   . MET   U  7  81  ? 25.442  -206.926 61.497  1.00 96.07  ? 72  MET   U C   1 
ATOM   36370 O  O   . MET   U  7  81  ? 26.613  -206.618 61.810  1.00 92.45  ? 72  MET   U O   1 
ATOM   36371 C  CB  . MET   U  7  81  ? 24.959  -205.219 59.706  1.00 94.49  ? 72  MET   U CB  1 
ATOM   36372 C  CG  . MET   U  7  81  ? 24.986  -206.203 58.552  1.00 97.39  ? 72  MET   U CG  1 
ATOM   36373 S  SD  . MET   U  7  81  ? 25.981  -205.572 57.171  1.00 99.90  ? 72  MET   U SD  1 
ATOM   36374 C  CE  . MET   U  7  81  ? 27.630  -205.764 57.847  1.00 99.82  ? 72  MET   U CE  1 
ATOM   36375 N  N   . VAL   U  7  82  ? 24.940  -208.166 61.557  1.00 95.42  ? 73  VAL   U N   1 
ATOM   36376 C  CA  . VAL   U  7  82  ? 25.755  -209.401 61.763  1.00 94.55  ? 73  VAL   U CA  1 
ATOM   36377 C  C   . VAL   U  7  82  ? 25.901  -210.101 60.408  1.00 94.54  ? 73  VAL   U C   1 
ATOM   36378 O  O   . VAL   U  7  82  ? 24.935  -210.067 59.616  1.00 93.31  ? 73  VAL   U O   1 
ATOM   36379 C  CB  . VAL   U  7  82  ? 25.157  -210.341 62.830  1.00 97.22  ? 73  VAL   U CB  1 
ATOM   36380 C  CG1 . VAL   U  7  82  ? 23.805  -210.907 62.425  1.00 98.37  ? 73  VAL   U CG1 1 
ATOM   36381 C  CG2 . VAL   U  7  82  ? 26.115  -211.470 63.174  1.00 98.62  ? 73  VAL   U CG2 1 
ATOM   36382 N  N   . VAL   U  7  83  ? 27.069  -210.701 60.160  1.00 93.50  ? 74  VAL   U N   1 
ATOM   36383 C  CA  . VAL   U  7  83  ? 27.415  -211.389 58.880  1.00 94.93  ? 74  VAL   U CA  1 
ATOM   36384 C  C   . VAL   U  7  83  ? 27.655  -212.876 59.156  1.00 95.53  ? 74  VAL   U C   1 
ATOM   36385 O  O   . VAL   U  7  83  ? 28.361  -213.199 60.133  1.00 100.43 ? 74  VAL   U O   1 
ATOM   36386 C  CB  . VAL   U  7  83  ? 28.653  -210.769 58.206  1.00 93.65  ? 74  VAL   U CB  1 
ATOM   36387 C  CG1 . VAL   U  7  83  ? 28.877  -211.362 56.823  1.00 94.09  ? 74  VAL   U CG1 1 
ATOM   36388 C  CG2 . VAL   U  7  83  ? 28.576  -209.253 58.130  1.00 92.55  ? 74  VAL   U CG2 1 
ATOM   36389 N  N   . ASN   U  7  84  ? 27.106  -213.735 58.294  1.00 93.21  ? 75  ASN   U N   1 
ATOM   36390 C  CA  . ASN   U  7  84  ? 27.453  -215.175 58.190  1.00 94.24  ? 75  ASN   U CA  1 
ATOM   36391 C  C   . ASN   U  7  84  ? 28.271  -215.372 56.913  1.00 89.64  ? 75  ASN   U C   1 
ATOM   36392 O  O   . ASN   U  7  84  ? 27.668  -215.357 55.826  1.00 89.61  ? 75  ASN   U O   1 
ATOM   36393 C  CB  . ASN   U  7  84  ? 26.205  -216.057 58.193  1.00 95.42  ? 75  ASN   U CB  1 
ATOM   36394 C  CG  . ASN   U  7  84  ? 25.620  -216.220 59.578  1.00 100.55 ? 75  ASN   U CG  1 
ATOM   36395 O  OD1 . ASN   U  7  84  ? 25.103  -215.263 60.150  1.00 103.60 ? 75  ASN   U OD1 1 
ATOM   36396 N  ND2 . ASN   U  7  84  ? 25.700  -217.423 60.124  1.00 104.22 ? 75  ASN   U ND2 1 
ATOM   36397 N  N   . GLY   U  7  85  ? 29.591  -215.520 57.043  1.00 90.33  ? 76  GLY   U N   1 
ATOM   36398 C  CA  . GLY   U  7  85  ? 30.499  -215.759 55.905  1.00 91.45  ? 76  GLY   U CA  1 
ATOM   36399 C  C   . GLY   U  7  85  ? 31.911  -215.252 56.178  1.00 92.43  ? 76  GLY   U C   1 
ATOM   36400 O  O   . GLY   U  7  85  ? 32.159  -214.638 57.216  1.00 89.75  ? 76  GLY   U O   1 
ATOM   36401 N  N   . PRO   U  7  86  ? 32.864  -215.484 55.243  1.00 93.08  ? 77  PRO   U N   1 
ATOM   36402 C  CA  . PRO   U  7  86  ? 34.264  -215.107 55.440  1.00 94.00  ? 77  PRO   U CA  1 
ATOM   36403 C  C   . PRO   U  7  86  ? 34.394  -213.611 55.763  1.00 94.40  ? 77  PRO   U C   1 
ATOM   36404 O  O   . PRO   U  7  86  ? 33.611  -212.830 55.251  1.00 94.26  ? 77  PRO   U O   1 
ATOM   36405 C  CB  . PRO   U  7  86  ? 34.937  -215.451 54.101  1.00 93.98  ? 77  PRO   U CB  1 
ATOM   36406 C  CG  . PRO   U  7  86  ? 34.038  -216.504 53.496  1.00 94.74  ? 77  PRO   U CG  1 
ATOM   36407 C  CD  . PRO   U  7  86  ? 32.644  -216.103 53.928  1.00 94.13  ? 77  PRO   U CD  1 
ATOM   36408 N  N   . ILE   U  7  87  ? 35.375  -213.258 56.597  1.00 96.39  ? 78  ILE   U N   1 
ATOM   36409 C  CA  . ILE   U  7  87  ? 35.535  -211.886 57.165  1.00 95.78  ? 78  ILE   U CA  1 
ATOM   36410 C  C   . ILE   U  7  87  ? 35.923  -210.883 56.075  1.00 94.79  ? 78  ILE   U C   1 
ATOM   36411 O  O   . ILE   U  7  87  ? 35.504  -209.730 56.159  1.00 95.93  ? 78  ILE   U O   1 
ATOM   36412 C  CB  . ILE   U  7  87  ? 36.499  -211.874 58.375  1.00 96.33  ? 78  ILE   U CB  1 
ATOM   36413 C  CG1 . ILE   U  7  87  ? 36.396  -210.562 59.159  1.00 95.78  ? 78  ILE   U CG1 1 
ATOM   36414 C  CG2 . ILE   U  7  87  ? 37.938  -212.178 57.976  1.00 97.90  ? 78  ILE   U CG2 1 
ATOM   36415 C  CD1 . ILE   U  7  87  ? 35.094  -210.387 59.909  1.00 94.51  ? 78  ILE   U CD1 1 
ATOM   36416 N  N   . PRO   U  7  88  ? 36.704  -211.234 55.020  1.00 94.36  ? 79  PRO   U N   1 
ATOM   36417 C  CA  . PRO   U  7  88  ? 37.054  -210.250 53.993  1.00 93.59  ? 79  PRO   U CA  1 
ATOM   36418 C  C   . PRO   U  7  88  ? 35.797  -209.710 53.292  1.00 92.63  ? 79  PRO   U C   1 
ATOM   36419 O  O   . PRO   U  7  88  ? 35.641  -208.500 53.211  1.00 91.04  ? 79  PRO   U O   1 
ATOM   36420 C  CB  . PRO   U  7  88  ? 37.955  -211.013 53.009  1.00 93.60  ? 79  PRO   U CB  1 
ATOM   36421 C  CG  . PRO   U  7  88  ? 38.433  -212.217 53.792  1.00 94.77  ? 79  PRO   U CG  1 
ATOM   36422 C  CD  . PRO   U  7  88  ? 37.296  -212.552 54.733  1.00 94.42  ? 79  PRO   U CD  1 
ATOM   36423 N  N   . ASP   U  7  89  ? 34.938  -210.616 52.818  1.00 92.56  ? 80  ASP   U N   1 
ATOM   36424 C  CA  . ASP   U  7  89  ? 33.628  -210.295 52.191  1.00 91.62  ? 80  ASP   U CA  1 
ATOM   36425 C  C   . ASP   U  7  89  ? 32.726  -209.603 53.216  1.00 87.33  ? 80  ASP   U C   1 
ATOM   36426 O  O   . ASP   U  7  89  ? 31.989  -208.690 52.818  1.00 86.03  ? 80  ASP   U O   1 
ATOM   36427 C  CB  . ASP   U  7  89  ? 32.941  -211.550 51.644  1.00 95.24  ? 80  ASP   U CB  1 
ATOM   36428 C  CG  . ASP   U  7  89  ? 33.551  -212.087 50.361  1.00 100.03 ? 80  ASP   U CG  1 
ATOM   36429 O  OD1 . ASP   U  7  89  ? 34.635  -211.603 49.978  1.00 105.74 ? 80  ASP   U OD1 1 
ATOM   36430 O  OD2 . ASP   U  7  89  ? 32.934  -212.986 49.751  1.00 104.11 ? 80  ASP   U OD2 1 
ATOM   36431 N  N   . ALA   U  7  90  ? 32.772  -210.037 54.479  1.00 88.19  ? 81  ALA   U N   1 
ATOM   36432 C  CA  . ALA   U  7  90  ? 31.949  -209.500 55.588  1.00 90.59  ? 81  ALA   U CA  1 
ATOM   36433 C  C   . ALA   U  7  90  ? 32.247  -208.010 55.784  1.00 91.81  ? 81  ALA   U C   1 
ATOM   36434 O  O   . ALA   U  7  90  ? 31.286  -207.228 55.909  1.00 93.65  ? 81  ALA   U O   1 
ATOM   36435 C  CB  . ALA   U  7  90  ? 32.204  -210.276 56.857  1.00 91.95  ? 81  ALA   U CB  1 
ATOM   36436 N  N   . ARG   U  7  91  ? 33.531  -207.641 55.805  1.00 92.44  ? 82  ARG   U N   1 
ATOM   36437 C  CA  . ARG   U  7  91  ? 33.996  -206.244 56.021  1.00 93.55  ? 82  ARG   U CA  1 
ATOM   36438 C  C   . ARG   U  7  91  ? 33.745  -205.408 54.759  1.00 94.85  ? 82  ARG   U C   1 
ATOM   36439 O  O   . ARG   U  7  91  ? 33.423  -204.207 54.901  1.00 91.75  ? 82  ARG   U O   1 
ATOM   36440 C  CB  . ARG   U  7  91  ? 35.474  -206.222 56.424  1.00 95.32  ? 82  ARG   U CB  1 
ATOM   36441 C  CG  . ARG   U  7  91  ? 35.714  -206.629 57.870  1.00 92.73  ? 82  ARG   U CG  1 
ATOM   36442 C  CD  . ARG   U  7  91  ? 37.166  -206.943 58.157  1.00 92.41  ? 82  ARG   U CD  1 
ATOM   36443 N  NE  . ARG   U  7  91  ? 37.363  -207.254 59.565  1.00 91.71  ? 82  ARG   U NE  1 
ATOM   36444 C  CZ  . ARG   U  7  91  ? 38.396  -207.930 60.062  1.00 93.47  ? 82  ARG   U CZ  1 
ATOM   36445 N  NH1 . ARG   U  7  91  ? 39.350  -208.385 59.267  1.00 95.07  ? 82  ARG   U NH1 1 
ATOM   36446 N  NH2 . ARG   U  7  91  ? 38.464  -208.160 61.361  1.00 93.73  ? 82  ARG   U NH2 1 
ATOM   36447 N  N   . ASN   U  7  92  ? 33.903  -206.009 53.576  1.00 93.34  ? 83  ASN   U N   1 
ATOM   36448 C  CA  . ASN   U  7  92  ? 33.565  -205.377 52.270  1.00 91.63  ? 83  ASN   U CA  1 
ATOM   36449 C  C   . ASN   U  7  92  ? 32.121  -204.863 52.320  1.00 89.66  ? 83  ASN   U C   1 
ATOM   36450 O  O   . ASN   U  7  92  ? 31.899  -203.701 51.950  1.00 88.60  ? 83  ASN   U O   1 
ATOM   36451 C  CB  . ASN   U  7  92  ? 33.778  -206.347 51.104  1.00 92.59  ? 83  ASN   U CB  1 
ATOM   36452 C  CG  . ASN   U  7  92  ? 33.366  -205.780 49.760  1.00 92.07  ? 83  ASN   U CG  1 
ATOM   36453 O  OD1 . ASN   U  7  92  ? 34.215  -205.502 48.918  1.00 93.88  ? 83  ASN   U OD1 1 
ATOM   36454 N  ND2 . ASN   U  7  92  ? 32.070  -205.616 49.541  1.00 90.42  ? 83  ASN   U ND2 1 
ATOM   36455 N  N   . ALA   U  7  93  ? 31.184  -205.712 52.750  1.00 89.68  ? 84  ALA   U N   1 
ATOM   36456 C  CA  . ALA   U  7  93  ? 29.734  -205.416 52.850  1.00 91.62  ? 84  ALA   U CA  1 
ATOM   36457 C  C   . ALA   U  7  93  ? 29.487  -204.323 53.896  1.00 88.86  ? 84  ALA   U C   1 
ATOM   36458 O  O   . ALA   U  7  93  ? 28.637  -203.448 53.642  1.00 89.20  ? 84  ALA   U O   1 
ATOM   36459 C  CB  . ALA   U  7  93  ? 28.974  -206.673 53.198  1.00 94.10  ? 84  ALA   U CB  1 
ATOM   36460 N  N   . ALA   U  7  94  ? 30.192  -204.390 55.031  1.00 90.64  ? 85  ALA   U N   1 
ATOM   36461 C  CA  . ALA   U  7  94  ? 30.033  -203.478 56.189  1.00 90.60  ? 85  ALA   U CA  1 
ATOM   36462 C  C   . ALA   U  7  94  ? 30.450  -202.052 55.809  1.00 87.66  ? 85  ALA   U C   1 
ATOM   36463 O  O   . ALA   U  7  94  ? 29.713  -201.119 56.173  1.00 88.10  ? 85  ALA   U O   1 
ATOM   36464 C  CB  . ALA   U  7  94  ? 30.824  -203.987 57.369  1.00 91.88  ? 85  ALA   U CB  1 
ATOM   36465 N  N   . LEU   U  7  95  ? 31.579  -201.886 55.111  1.00 86.85  ? 86  LEU   U N   1 
ATOM   36466 C  CA  . LEU   U  7  95  ? 32.087  -200.548 54.697  1.00 87.57  ? 86  LEU   U CA  1 
ATOM   36467 C  C   . LEU   U  7  95  ? 31.094  -199.916 53.715  1.00 86.55  ? 86  LEU   U C   1 
ATOM   36468 O  O   . LEU   U  7  95  ? 30.795  -198.721 53.877  1.00 89.32  ? 86  LEU   U O   1 
ATOM   36469 C  CB  . LEU   U  7  95  ? 33.481  -200.668 54.070  1.00 88.86  ? 86  LEU   U CB  1 
ATOM   36470 C  CG  . LEU   U  7  95  ? 34.083  -199.361 53.546  1.00 90.13  ? 86  LEU   U CG  1 
ATOM   36471 C  CD1 . LEU   U  7  95  ? 34.141  -198.298 54.636  1.00 91.14  ? 86  LEU   U CD1 1 
ATOM   36472 C  CD2 . LEU   U  7  95  ? 35.470  -199.591 52.963  1.00 89.92  ? 86  LEU   U CD2 1 
ATOM   36473 N  N   . ARG   U  7  96  ? 30.606  -200.688 52.740  1.00 84.70  ? 87  ARG   U N   1 
ATOM   36474 C  CA  . ARG   U  7  96  ? 29.633  -200.205 51.726  1.00 84.70  ? 87  ARG   U CA  1 
ATOM   36475 C  C   . ARG   U  7  96  ? 28.344  -199.772 52.433  1.00 85.96  ? 87  ARG   U C   1 
ATOM   36476 O  O   . ARG   U  7  96  ? 27.841  -198.686 52.107  1.00 89.04  ? 87  ARG   U O   1 
ATOM   36477 C  CB  . ARG   U  7  96  ? 29.342  -201.278 50.674  1.00 84.75  ? 87  ARG   U CB  1 
ATOM   36478 C  CG  . ARG   U  7  96  ? 28.428  -200.817 49.547  1.00 86.53  ? 87  ARG   U CG  1 
ATOM   36479 C  CD  . ARG   U  7  96  ? 28.859  -199.485 48.966  1.00 89.50  ? 87  ARG   U CD  1 
ATOM   36480 N  NE  . ARG   U  7  96  ? 28.098  -199.122 47.781  1.00 93.51  ? 87  ARG   U NE  1 
ATOM   36481 C  CZ  . ARG   U  7  96  ? 28.366  -199.525 46.541  1.00 95.99  ? 87  ARG   U CZ  1 
ATOM   36482 N  NH1 . ARG   U  7  96  ? 29.388  -200.330 46.297  1.00 98.43  ? 87  ARG   U NH1 1 
ATOM   36483 N  NH2 . ARG   U  7  96  ? 27.600  -199.120 45.543  1.00 98.12  ? 87  ARG   U NH2 1 
ATOM   36484 N  N   . ALA   U  7  97  ? 27.848  -200.588 53.368  1.00 87.07  ? 88  ALA   U N   1 
ATOM   36485 C  CA  . ALA   U  7  97  ? 26.603  -200.352 54.140  1.00 88.44  ? 88  ALA   U CA  1 
ATOM   36486 C  C   . ALA   U  7  97  ? 26.721  -199.052 54.943  1.00 85.75  ? 88  ALA   U C   1 
ATOM   36487 O  O   . ALA   U  7  97  ? 25.737  -198.291 54.976  1.00 86.79  ? 88  ALA   U O   1 
ATOM   36488 C  CB  . ALA   U  7  97  ? 26.324  -201.525 55.050  1.00 90.17  ? 88  ALA   U CB  1 
ATOM   36489 N  N   . LYS   U  7  98  ? 27.872  -198.832 55.589  1.00 86.64  ? 89  LYS   U N   1 
ATOM   36490 C  CA  . LYS   U  7  98  ? 28.190  -197.599 56.359  1.00 88.39  ? 89  LYS   U CA  1 
ATOM   36491 C  C   . LYS   U  7  98  ? 28.135  -196.389 55.418  1.00 87.99  ? 89  LYS   U C   1 
ATOM   36492 O  O   . LYS   U  7  98  ? 27.402  -195.431 55.730  1.00 92.07  ? 89  LYS   U O   1 
ATOM   36493 C  CB  . LYS   U  7  98  ? 29.562  -197.728 57.032  1.00 88.82  ? 89  LYS   U CB  1 
ATOM   36494 C  CG  . LYS   U  7  98  ? 29.609  -198.669 58.229  1.00 86.69  ? 89  LYS   U CG  1 
ATOM   36495 C  CD  . LYS   U  7  98  ? 31.009  -198.973 58.709  1.00 85.96  ? 89  LYS   U CD  1 
ATOM   36496 C  CE  . LYS   U  7  98  ? 31.030  -199.911 59.896  1.00 85.21  ? 89  LYS   U CE  1 
ATOM   36497 N  NZ  . LYS   U  7  98  ? 32.413  -200.187 60.348  1.00 86.65  ? 89  LYS   U NZ  1 
ATOM   36498 N  N   . ALA   U  7  99  ? 28.870  -196.448 54.304  1.00 87.42  ? 90  ALA   U N   1 
ATOM   36499 C  CA  . ALA   U  7  99  ? 28.962  -195.378 53.284  1.00 86.97  ? 90  ALA   U CA  1 
ATOM   36500 C  C   . ALA   U  7  99  ? 27.569  -195.073 52.720  1.00 87.84  ? 90  ALA   U C   1 
ATOM   36501 O  O   . ALA   U  7  99  ? 27.260  -193.884 52.549  1.00 93.71  ? 90  ALA   U O   1 
ATOM   36502 C  CB  . ALA   U  7  99  ? 29.920  -195.783 52.192  1.00 86.77  ? 90  ALA   U CB  1 
ATOM   36503 N  N   . GLU   U  7  100 ? 26.768  -196.104 52.438  1.00 85.76  ? 91  GLU   U N   1 
ATOM   36504 C  CA  . GLU   U  7  100 ? 25.397  -195.966 51.875  1.00 88.11  ? 91  GLU   U CA  1 
ATOM   36505 C  C   . GLU   U  7  100 ? 24.486  -195.263 52.888  1.00 84.74  ? 91  GLU   U C   1 
ATOM   36506 O  O   . GLU   U  7  100 ? 23.718  -194.377 52.468  1.00 86.45  ? 91  GLU   U O   1 
ATOM   36507 C  CB  . GLU   U  7  100 ? 24.818  -197.332 51.495  1.00 88.25  ? 91  GLU   U CB  1 
ATOM   36508 C  CG  . GLU   U  7  100 ? 25.437  -197.936 50.246  1.00 90.97  ? 91  GLU   U CG  1 
ATOM   36509 C  CD  . GLU   U  7  100 ? 25.148  -197.189 48.956  1.00 93.65  ? 91  GLU   U CD  1 
ATOM   36510 O  OE1 . GLU   U  7  100 ? 24.243  -196.327 48.955  1.00 96.77  ? 91  GLU   U OE1 1 
ATOM   36511 O  OE2 . GLU   U  7  100 ? 25.827  -197.475 47.949  1.00 98.94  ? 91  GLU   U OE2 1 
ATOM   36512 N  N   . ALA   U  7  101 ? 24.563  -195.649 54.166  1.00 82.23  ? 92  ALA   U N   1 
ATOM   36513 C  CA  . ALA   U  7  101 ? 23.727  -195.112 55.266  1.00 85.54  ? 92  ALA   U CA  1 
ATOM   36514 C  C   . ALA   U  7  101 ? 24.097  -193.648 55.550  1.00 86.77  ? 92  ALA   U C   1 
ATOM   36515 O  O   . ALA   U  7  101 ? 23.187  -192.860 55.889  1.00 85.18  ? 92  ALA   U O   1 
ATOM   36516 C  CB  . ALA   U  7  101 ? 23.876  -195.972 56.498  1.00 84.79  ? 92  ALA   U CB  1 
ATOM   36517 N  N   . ALA   U  7  102 ? 25.383  -193.301 55.418  1.00 90.49  ? 93  ALA   U N   1 
ATOM   36518 C  CA  . ALA   U  7  102 ? 25.921  -191.935 55.625  1.00 92.41  ? 93  ALA   U CA  1 
ATOM   36519 C  C   . ALA   U  7  102 ? 25.419  -191.010 54.510  1.00 94.70  ? 93  ALA   U C   1 
ATOM   36520 O  O   . ALA   U  7  102 ? 24.939  -189.903 54.834  1.00 95.29  ? 93  ALA   U O   1 
ATOM   36521 C  CB  . ALA   U  7  102 ? 27.431  -191.969 55.676  1.00 93.49  ? 93  ALA   U CB  1 
ATOM   36522 N  N   . GLU   U  7  103 ? 25.525  -191.456 53.252  1.00 93.89  ? 94  GLU   U N   1 
ATOM   36523 C  CA  . GLU   U  7  103 ? 25.107  -190.693 52.043  1.00 92.14  ? 94  GLU   U CA  1 
ATOM   36524 C  C   . GLU   U  7  103 ? 23.593  -190.445 52.086  1.00 89.40  ? 94  GLU   U C   1 
ATOM   36525 O  O   . GLU   U  7  103 ? 23.183  -189.301 51.808  1.00 88.04  ? 94  GLU   U O   1 
ATOM   36526 C  CB  . GLU   U  7  103 ? 25.498  -191.440 50.767  1.00 95.06  ? 94  GLU   U CB  1 
ATOM   36527 C  CG  . GLU   U  7  103 ? 25.119  -190.703 49.494  1.00 98.15  ? 94  GLU   U CG  1 
ATOM   36528 C  CD  . GLU   U  7  103 ? 25.206  -191.544 48.232  1.00 102.30 ? 94  GLU   U CD  1 
ATOM   36529 O  OE1 . GLU   U  7  103 ? 26.274  -192.139 47.991  1.00 112.84 ? 94  GLU   U OE1 1 
ATOM   36530 O  OE2 . GLU   U  7  103 ? 24.198  -191.613 47.499  1.00 105.82 ? 94  GLU   U OE2 1 
ATOM   36531 N  N   . PHE   U  7  104 ? 22.798  -191.475 52.406  1.00 89.24  ? 95  PHE   U N   1 
ATOM   36532 C  CA  . PHE   U  7  104 ? 21.316  -191.386 52.512  1.00 83.51  ? 95  PHE   U CA  1 
ATOM   36533 C  C   . PHE   U  7  104 ? 20.946  -190.207 53.421  1.00 84.69  ? 95  PHE   U C   1 
ATOM   36534 O  O   . PHE   U  7  104 ? 20.100  -189.382 53.027  1.00 81.57  ? 95  PHE   U O   1 
ATOM   36535 C  CB  . PHE   U  7  104 ? 20.705  -192.686 53.042  1.00 84.51  ? 95  PHE   U CB  1 
ATOM   36536 C  CG  . PHE   U  7  104 ? 19.196  -192.703 53.041  1.00 84.21  ? 95  PHE   U CG  1 
ATOM   36537 C  CD1 . PHE   U  7  104 ? 18.472  -192.152 54.088  1.00 85.24  ? 95  PHE   U CD1 1 
ATOM   36538 C  CD2 . PHE   U  7  104 ? 18.498  -193.262 51.983  1.00 85.06  ? 95  PHE   U CD2 1 
ATOM   36539 C  CE1 . PHE   U  7  104 ? 17.085  -192.162 54.078  1.00 86.13  ? 95  PHE   U CE1 1 
ATOM   36540 C  CE2 . PHE   U  7  104 ? 17.110  -193.277 51.977  1.00 86.26  ? 95  PHE   U CE2 1 
ATOM   36541 C  CZ  . PHE   U  7  104 ? 16.406  -192.726 53.022  1.00 86.34  ? 95  PHE   U CZ  1 
ATOM   36542 N  N   . ARG   U  7  105 ? 21.568  -190.136 54.602  1.00 86.99  ? 96  ARG   U N   1 
ATOM   36543 C  CA  . ARG   U  7  105 ? 21.291  -189.098 55.632  1.00 89.90  ? 96  ARG   U CA  1 
ATOM   36544 C  C   . ARG   U  7  105 ? 21.621  -187.710 55.070  1.00 88.78  ? 96  ARG   U C   1 
ATOM   36545 O  O   . ARG   U  7  105 ? 20.820  -186.775 55.299  1.00 88.45  ? 96  ARG   U O   1 
ATOM   36546 C  CB  . ARG   U  7  105 ? 22.084  -189.383 56.912  1.00 91.31  ? 96  ARG   U CB  1 
ATOM   36547 C  CG  . ARG   U  7  105 ? 21.964  -188.305 57.981  1.00 92.86  ? 96  ARG   U CG  1 
ATOM   36548 C  CD  . ARG   U  7  105 ? 20.534  -188.074 58.436  1.00 94.38  ? 96  ARG   U CD  1 
ATOM   36549 N  NE  . ARG   U  7  105 ? 20.428  -186.906 59.300  1.00 96.81  ? 96  ARG   U NE  1 
ATOM   36550 C  CZ  . ARG   U  7  105 ? 20.442  -185.642 58.879  1.00 96.84  ? 96  ARG   U CZ  1 
ATOM   36551 N  NH1 . ARG   U  7  105 ? 20.568  -185.361 57.593  1.00 96.75  ? 96  ARG   U NH1 1 
ATOM   36552 N  NH2 . ARG   U  7  105 ? 20.336  -184.653 59.750  1.00 98.67  ? 96  ARG   U NH2 1 
ATOM   36553 N  N   . TYR   U  7  106 ? 22.754  -187.576 54.372  1.00 88.19  ? 97  TYR   U N   1 
ATOM   36554 C  CA  . TYR   U  7  106 ? 23.213  -186.299 53.764  1.00 86.92  ? 97  TYR   U CA  1 
ATOM   36555 C  C   . TYR   U  7  106 ? 22.229  -185.861 52.672  1.00 88.54  ? 97  TYR   U C   1 
ATOM   36556 O  O   . TYR   U  7  106 ? 21.873  -184.675 52.635  1.00 89.11  ? 97  TYR   U O   1 
ATOM   36557 C  CB  . TYR   U  7  106 ? 24.631  -186.418 53.197  1.00 86.36  ? 97  TYR   U CB  1 
ATOM   36558 C  CG  . TYR   U  7  106 ? 25.074  -185.209 52.412  1.00 85.63  ? 97  TYR   U CG  1 
ATOM   36559 C  CD1 . TYR   U  7  106 ? 25.302  -183.992 53.039  1.00 86.08  ? 97  TYR   U CD1 1 
ATOM   36560 C  CD2 . TYR   U  7  106 ? 25.243  -185.269 51.039  1.00 83.85  ? 97  TYR   U CD2 1 
ATOM   36561 C  CE1 . TYR   U  7  106 ? 25.698  -182.871 52.326  1.00 84.93  ? 97  TYR   U CE1 1 
ATOM   36562 C  CE2 . TYR   U  7  106 ? 25.642  -184.158 50.313  1.00 82.97  ? 97  TYR   U CE2 1 
ATOM   36563 C  CZ  . TYR   U  7  106 ? 25.870  -182.956 50.957  1.00 84.05  ? 97  TYR   U CZ  1 
ATOM   36564 O  OH  . TYR   U  7  106 ? 26.261  -181.865 50.237  1.00 83.62  ? 97  TYR   U OH  1 
ATOM   36565 N  N   . LYS   U  7  107 ? 21.807  -186.794 51.815  1.00 90.15  ? 98  LYS   U N   1 
ATOM   36566 C  CA  . LYS   U  7  107 ? 20.960  -186.516 50.623  1.00 90.22  ? 98  LYS   U CA  1 
ATOM   36567 C  C   . LYS   U  7  107 ? 19.512  -186.211 51.027  1.00 90.95  ? 98  LYS   U C   1 
ATOM   36568 O  O   . LYS   U  7  107 ? 18.935  -185.292 50.422  1.00 90.12  ? 98  LYS   U O   1 
ATOM   36569 C  CB  . LYS   U  7  107 ? 20.983  -187.696 49.648  1.00 90.94  ? 98  LYS   U CB  1 
ATOM   36570 C  CG  . LYS   U  7  107 ? 22.068  -187.633 48.583  1.00 95.62  ? 98  LYS   U CG  1 
ATOM   36571 C  CD  . LYS   U  7  107 ? 21.799  -188.554 47.412  1.00 100.22 ? 98  LYS   U CD  1 
ATOM   36572 C  CE  . LYS   U  7  107 ? 22.660  -188.255 46.202  1.00 104.64 ? 98  LYS   U CE  1 
ATOM   36573 N  NZ  . LYS   U  7  107 ? 23.581  -189.373 45.890  1.00 107.23 ? 98  LYS   U NZ  1 
ATOM   36574 N  N   . TYR   U  7  108 ? 18.937  -186.959 51.977  1.00 91.91  ? 99  TYR   U N   1 
ATOM   36575 C  CA  . TYR   U  7  108 ? 17.469  -187.010 52.228  1.00 93.12  ? 99  TYR   U CA  1 
ATOM   36576 C  C   . TYR   U  7  108 ? 17.092  -186.454 53.610  1.00 92.87  ? 99  TYR   U C   1 
ATOM   36577 O  O   . TYR   U  7  108 ? 15.879  -186.359 53.875  1.00 96.02  ? 99  TYR   U O   1 
ATOM   36578 C  CB  . TYR   U  7  108 ? 16.956  -188.439 52.033  1.00 92.76  ? 99  TYR   U CB  1 
ATOM   36579 C  CG  . TYR   U  7  108 ? 17.249  -188.992 50.661  1.00 93.09  ? 99  TYR   U CG  1 
ATOM   36580 C  CD1 . TYR   U  7  108 ? 16.660  -188.444 49.534  1.00 91.77  ? 99  TYR   U CD1 1 
ATOM   36581 C  CD2 . TYR   U  7  108 ? 18.138  -190.041 50.481  1.00 94.38  ? 99  TYR   U CD2 1 
ATOM   36582 C  CE1 . TYR   U  7  108 ? 16.932  -188.931 48.267  1.00 90.30  ? 99  TYR   U CE1 1 
ATOM   36583 C  CE2 . TYR   U  7  108 ? 18.422  -190.539 49.220  1.00 92.44  ? 99  TYR   U CE2 1 
ATOM   36584 C  CZ  . TYR   U  7  108 ? 17.816  -189.982 48.108  1.00 90.59  ? 99  TYR   U CZ  1 
ATOM   36585 O  OH  . TYR   U  7  108 ? 18.087  -190.465 46.862  1.00 92.17  ? 99  TYR   U OH  1 
ATOM   36586 N  N   . GLY   U  7  109 ? 18.066  -186.105 54.457  1.00 90.63  ? 100 GLY   U N   1 
ATOM   36587 C  CA  . GLY   U  7  109 ? 17.830  -185.310 55.679  1.00 90.34  ? 100 GLY   U CA  1 
ATOM   36588 C  C   . GLY   U  7  109 ? 17.232  -186.109 56.828  1.00 91.73  ? 100 GLY   U C   1 
ATOM   36589 O  O   . GLY   U  7  109 ? 16.773  -185.474 57.796  1.00 90.00  ? 100 GLY   U O   1 
ATOM   36590 N  N   . TYR   U  7  110 ? 17.219  -187.442 56.746  1.00 90.91  ? 101 TYR   U N   1 
ATOM   36591 C  CA  . TYR   U  7  110 ? 16.768  -188.336 57.847  1.00 92.94  ? 101 TYR   U CA  1 
ATOM   36592 C  C   . TYR   U  7  110 ? 17.531  -189.662 57.775  1.00 94.33  ? 101 TYR   U C   1 
ATOM   36593 O  O   . TYR   U  7  110 ? 18.043  -190.004 56.691  1.00 95.67  ? 101 TYR   U O   1 
ATOM   36594 C  CB  . TYR   U  7  110 ? 15.246  -188.515 57.817  1.00 92.26  ? 101 TYR   U CB  1 
ATOM   36595 C  CG  . TYR   U  7  110 ? 14.708  -189.437 56.751  1.00 89.85  ? 101 TYR   U CG  1 
ATOM   36596 C  CD1 . TYR   U  7  110 ? 14.445  -188.978 55.470  1.00 91.01  ? 101 TYR   U CD1 1 
ATOM   36597 C  CD2 . TYR   U  7  110 ? 14.427  -190.764 57.029  1.00 88.95  ? 101 TYR   U CD2 1 
ATOM   36598 C  CE1 . TYR   U  7  110 ? 13.937  -189.817 54.490  1.00 90.15  ? 101 TYR   U CE1 1 
ATOM   36599 C  CE2 . TYR   U  7  110 ? 13.920  -191.616 56.062  1.00 88.50  ? 101 TYR   U CE2 1 
ATOM   36600 C  CZ  . TYR   U  7  110 ? 13.674  -191.143 54.787  1.00 88.83  ? 101 TYR   U CZ  1 
ATOM   36601 O  OH  . TYR   U  7  110 ? 13.172  -191.990 53.842  1.00 88.25  ? 101 TYR   U OH  1 
ATOM   36602 N  N   . ASP   U  7  111 ? 17.595  -190.374 58.905  1.00 94.16  ? 102 ASP   U N   1 
ATOM   36603 C  CA  . ASP   U  7  111 ? 18.408  -191.607 59.094  1.00 93.70  ? 102 ASP   U CA  1 
ATOM   36604 C  C   . ASP   U  7  111 ? 17.850  -192.739 58.225  1.00 93.76  ? 102 ASP   U C   1 
ATOM   36605 O  O   . ASP   U  7  111 ? 16.619  -192.953 58.247  1.00 91.13  ? 102 ASP   U O   1 
ATOM   36606 C  CB  . ASP   U  7  111 ? 18.435  -192.043 60.561  1.00 95.04  ? 102 ASP   U CB  1 
ATOM   36607 C  CG  . ASP   U  7  111 ? 19.008  -191.004 61.508  1.00 97.92  ? 102 ASP   U CG  1 
ATOM   36608 O  OD1 . ASP   U  7  111 ? 19.902  -190.247 61.079  1.00 98.34  ? 102 ASP   U OD1 1 
ATOM   36609 O  OD2 . ASP   U  7  111 ? 18.554  -190.961 62.668  1.00 100.25 ? 102 ASP   U OD2 1 
ATOM   36610 N  N   . MET   U  7  112 ? 18.732  -193.445 57.510  1.00 91.92  ? 103 MET   U N   1 
ATOM   36611 C  CA  . MET   U  7  112 ? 18.367  -194.567 56.604  1.00 89.60  ? 103 MET   U CA  1 
ATOM   36612 C  C   . MET   U  7  112 ? 17.664  -195.646 57.420  1.00 88.70  ? 103 MET   U C   1 
ATOM   36613 O  O   . MET   U  7  112 ? 18.230  -196.138 58.394  1.00 85.93  ? 103 MET   U O   1 
ATOM   36614 C  CB  . MET   U  7  112 ? 19.606  -195.160 55.928  1.00 86.72  ? 103 MET   U CB  1 
ATOM   36615 C  CG  . MET   U  7  112 ? 19.272  -196.077 54.777  1.00 86.94  ? 103 MET   U CG  1 
ATOM   36616 S  SD  . MET   U  7  112 ? 20.699  -196.368 53.707  1.00 91.12  ? 103 MET   U SD  1 
ATOM   36617 C  CE  . MET   U  7  112 ? 19.859  -196.838 52.193  1.00 94.73  ? 103 MET   U CE  1 
ATOM   36618 N  N   . PRO   U  7  113 ? 16.399  -196.007 57.090  1.00 92.27  ? 104 PRO   U N   1 
ATOM   36619 C  CA  . PRO   U  7  113 ? 15.731  -197.139 57.730  1.00 94.31  ? 104 PRO   U CA  1 
ATOM   36620 C  C   . PRO   U  7  113 ? 16.452  -198.466 57.455  1.00 94.48  ? 104 PRO   U C   1 
ATOM   36621 O  O   . PRO   U  7  113 ? 17.076  -198.605 56.420  1.00 95.75  ? 104 PRO   U O   1 
ATOM   36622 C  CB  . PRO   U  7  113 ? 14.327  -197.160 57.104  1.00 93.84  ? 104 PRO   U CB  1 
ATOM   36623 C  CG  . PRO   U  7  113 ? 14.133  -195.761 56.566  1.00 94.34  ? 104 PRO   U CG  1 
ATOM   36624 C  CD  . PRO   U  7  113 ? 15.517  -195.321 56.133  1.00 92.80  ? 104 PRO   U CD  1 
ATOM   36625 N  N   . CYS   U  7  114 ? 16.338  -199.404 58.393  1.00 98.01  ? 105 CYS   U N   1 
ATOM   36626 C  CA  . CYS   U  7  114 ? 16.948  -200.757 58.330  1.00 101.23 ? 105 CYS   U CA  1 
ATOM   36627 C  C   . CYS   U  7  114 ? 16.524  -201.462 57.034  1.00 101.89 ? 105 CYS   U C   1 
ATOM   36628 O  O   . CYS   U  7  114 ? 17.416  -201.973 56.324  1.00 101.63 ? 105 CYS   U O   1 
ATOM   36629 C  CB  . CYS   U  7  114 ? 16.554  -201.554 59.568  1.00 105.49 ? 105 CYS   U CB  1 
ATOM   36630 S  SG  . CYS   U  7  114 ? 17.093  -203.280 59.540  1.00 107.19 ? 105 CYS   U SG  1 
ATOM   36631 N  N   . ASP   U  7  115 ? 15.223  -201.452 56.720  1.00 103.08 ? 106 ASP   U N   1 
ATOM   36632 C  CA  . ASP   U  7  115 ? 14.625  -202.194 55.574  1.00 99.09  ? 106 ASP   U CA  1 
ATOM   36633 C  C   . ASP   U  7  115 ? 15.048  -201.568 54.239  1.00 96.35  ? 106 ASP   U C   1 
ATOM   36634 O  O   . ASP   U  7  115 ? 15.124  -202.320 53.247  1.00 100.17 ? 106 ASP   U O   1 
ATOM   36635 C  CB  . ASP   U  7  115 ? 13.099  -202.261 55.671  1.00 98.34  ? 106 ASP   U CB  1 
ATOM   36636 C  CG  . ASP   U  7  115 ? 12.429  -200.907 55.796  1.00 98.18  ? 106 ASP   U CG  1 
ATOM   36637 O  OD1 . ASP   U  7  115 ? 12.732  -200.199 56.776  1.00 95.01  ? 106 ASP   U OD1 1 
ATOM   36638 O  OD2 . ASP   U  7  115 ? 11.615  -200.573 54.913  1.00 93.62  ? 106 ASP   U OD2 1 
ATOM   36639 N  N   . VAL   U  7  116 ? 15.291  -200.253 54.203  1.00 90.20  ? 107 VAL   U N   1 
ATOM   36640 C  CA  . VAL   U  7  116 ? 15.719  -199.529 52.968  1.00 88.10  ? 107 VAL   U CA  1 
ATOM   36641 C  C   . VAL   U  7  116 ? 17.187  -199.879 52.684  1.00 85.67  ? 107 VAL   U C   1 
ATOM   36642 O  O   . VAL   U  7  116 ? 17.497  -200.169 51.513  1.00 83.58  ? 107 VAL   U O   1 
ATOM   36643 C  CB  . VAL   U  7  116 ? 15.491  -198.007 53.077  1.00 86.51  ? 107 VAL   U CB  1 
ATOM   36644 C  CG1 . VAL   U  7  116 ? 16.026  -197.262 51.861  1.00 86.27  ? 107 VAL   U CG1 1 
ATOM   36645 C  CG2 . VAL   U  7  116 ? 14.022  -197.670 53.294  1.00 85.23  ? 107 VAL   U CG2 1 
ATOM   36646 N  N   . LEU   U  7  117 ? 18.046  -199.856 53.713  1.00 85.65  ? 108 LEU   U N   1 
ATOM   36647 C  CA  . LEU   U  7  117 ? 19.483  -200.242 53.618  1.00 88.52  ? 108 LEU   U CA  1 
ATOM   36648 C  C   . LEU   U  7  117 ? 19.586  -201.706 53.171  1.00 90.56  ? 108 LEU   U C   1 
ATOM   36649 O  O   . LEU   U  7  117 ? 20.469  -202.011 52.342  1.00 96.21  ? 108 LEU   U O   1 
ATOM   36650 C  CB  . LEU   U  7  117 ? 20.172  -200.038 54.971  1.00 87.67  ? 108 LEU   U CB  1 
ATOM   36651 C  CG  . LEU   U  7  117 ? 21.603  -200.568 55.065  1.00 88.14  ? 108 LEU   U CG  1 
ATOM   36652 C  CD1 . LEU   U  7  117 ? 22.510  -199.917 54.032  1.00 88.15  ? 108 LEU   U CD1 1 
ATOM   36653 C  CD2 . LEU   U  7  117 ? 22.162  -200.367 56.461  1.00 89.05  ? 108 LEU   U CD2 1 
ATOM   36654 N  N   . ALA   U  7  118 ? 18.727  -202.576 53.711  1.00 90.93  ? 109 ALA   U N   1 
ATOM   36655 C  CA  . ALA   U  7  118 ? 18.616  -203.999 53.318  1.00 90.65  ? 109 ALA   U CA  1 
ATOM   36656 C  C   . ALA   U  7  118 ? 18.336  -204.087 51.812  1.00 88.16  ? 109 ALA   U C   1 
ATOM   36657 O  O   . ALA   U  7  118 ? 19.112  -204.764 51.109  1.00 85.94  ? 109 ALA   U O   1 
ATOM   36658 C  CB  . ALA   U  7  118 ? 17.541  -204.682 54.128  1.00 94.31  ? 109 ALA   U CB  1 
ATOM   36659 N  N   . LYS   U  7  119 ? 17.287  -203.402 51.340  1.00 87.47  ? 110 LYS   U N   1 
ATOM   36660 C  CA  . LYS   U  7  119 ? 16.860  -203.390 49.914  1.00 86.98  ? 110 LYS   U CA  1 
ATOM   36661 C  C   . LYS   U  7  119 ? 18.004  -202.892 49.024  1.00 85.53  ? 110 LYS   U C   1 
ATOM   36662 O  O   . LYS   U  7  119 ? 18.191  -203.461 47.933  1.00 84.84  ? 110 LYS   U O   1 
ATOM   36663 C  CB  . LYS   U  7  119 ? 15.634  -202.501 49.689  1.00 88.73  ? 110 LYS   U CB  1 
ATOM   36664 C  CG  . LYS   U  7  119 ? 15.063  -202.588 48.279  1.00 90.79  ? 110 LYS   U CG  1 
ATOM   36665 C  CD  . LYS   U  7  119 ? 14.129  -201.466 47.901  1.00 93.15  ? 110 LYS   U CD  1 
ATOM   36666 C  CE  . LYS   U  7  119 ? 13.784  -201.497 46.427  1.00 94.98  ? 110 LYS   U CE  1 
ATOM   36667 N  NZ  . LYS   U  7  119 ? 12.695  -200.550 46.095  1.00 97.77  ? 110 LYS   U NZ  1 
ATOM   36668 N  N   . ARG   U  7  120 ? 18.718  -201.854 49.462  1.00 84.47  ? 111 ARG   U N   1 
ATOM   36669 C  CA  . ARG   U  7  120 ? 19.843  -201.240 48.707  1.00 85.84  ? 111 ARG   U CA  1 
ATOM   36670 C  C   . ARG   U  7  120 ? 20.988  -202.255 48.591  1.00 86.04  ? 111 ARG   U C   1 
ATOM   36671 O  O   . ARG   U  7  120 ? 21.495  -202.442 47.469  1.00 83.75  ? 111 ARG   U O   1 
ATOM   36672 C  CB  . ARG   U  7  120 ? 20.293  -199.942 49.388  1.00 87.01  ? 111 ARG   U CB  1 
ATOM   36673 C  CG  . ARG   U  7  120 ? 21.570  -199.336 48.821  1.00 86.70  ? 111 ARG   U CG  1 
ATOM   36674 C  CD  . ARG   U  7  120 ? 21.502  -199.044 47.335  1.00 87.14  ? 111 ARG   U CD  1 
ATOM   36675 N  NE  . ARG   U  7  120 ? 22.729  -198.401 46.888  1.00 86.86  ? 111 ARG   U NE  1 
ATOM   36676 C  CZ  . ARG   U  7  120 ? 23.158  -198.345 45.631  1.00 89.24  ? 111 ARG   U CZ  1 
ATOM   36677 N  NH1 . ARG   U  7  120 ? 22.467  -198.909 44.651  1.00 89.72  ? 111 ARG   U NH1 1 
ATOM   36678 N  NH2 . ARG   U  7  120 ? 24.295  -197.728 45.359  1.00 90.10  ? 111 ARG   U NH2 1 
ATOM   36679 N  N   . MET   U  7  121 ? 21.374  -202.883 49.707  1.00 87.45  ? 112 MET   U N   1 
ATOM   36680 C  CA  . MET   U  7  121 ? 22.470  -203.890 49.764  1.00 87.07  ? 112 MET   U CA  1 
ATOM   36681 C  C   . MET   U  7  121 ? 22.077  -205.134 48.960  1.00 86.95  ? 112 MET   U C   1 
ATOM   36682 O  O   . MET   U  7  121 ? 22.975  -205.735 48.337  1.00 85.77  ? 112 MET   U O   1 
ATOM   36683 C  CB  . MET   U  7  121 ? 22.780  -204.289 51.210  1.00 87.35  ? 112 MET   U CB  1 
ATOM   36684 C  CG  . MET   U  7  121 ? 23.436  -203.181 52.002  1.00 87.80  ? 112 MET   U CG  1 
ATOM   36685 S  SD  . MET   U  7  121 ? 24.924  -202.566 51.184  1.00 91.15  ? 112 MET   U SD  1 
ATOM   36686 C  CE  . MET   U  7  121 ? 26.012  -203.981 51.353  1.00 90.92  ? 112 MET   U CE  1 
ATOM   36687 N  N   . ALA   U  7  122 ? 20.790  -205.495 48.981  1.00 87.18  ? 113 ALA   U N   1 
ATOM   36688 C  CA  . ALA   U  7  122 ? 20.203  -206.613 48.204  1.00 89.19  ? 113 ALA   U CA  1 
ATOM   36689 C  C   . ALA   U  7  122 ? 20.277  -206.297 46.704  1.00 89.09  ? 113 ALA   U C   1 
ATOM   36690 O  O   . ALA   U  7  122 ? 20.593  -207.216 45.919  1.00 87.28  ? 113 ALA   U O   1 
ATOM   36691 C  CB  . ALA   U  7  122 ? 18.782  -206.859 48.650  1.00 89.87  ? 113 ALA   U CB  1 
ATOM   36692 N  N   . ASN   U  7  123 ? 19.993  -205.046 46.327  1.00 87.87  ? 114 ASN   U N   1 
ATOM   36693 C  CA  . ASN   U  7  123 ? 20.033  -204.565 44.920  1.00 88.05  ? 114 ASN   U CA  1 
ATOM   36694 C  C   . ASN   U  7  123 ? 21.471  -204.649 44.393  1.00 84.45  ? 114 ASN   U C   1 
ATOM   36695 O  O   . ASN   U  7  123 ? 21.638  -205.053 43.231  1.00 82.88  ? 114 ASN   U O   1 
ATOM   36696 C  CB  . ASN   U  7  123 ? 19.494  -203.138 44.778  1.00 89.89  ? 114 ASN   U CB  1 
ATOM   36697 C  CG  . ASN   U  7  123 ? 17.987  -203.027 44.639  1.00 94.92  ? 114 ASN   U CG  1 
ATOM   36698 O  OD1 . ASN   U  7  123 ? 17.419  -201.967 44.904  1.00 101.31 ? 114 ASN   U OD1 1 
ATOM   36699 N  ND2 . ASN   U  7  123 ? 17.325  -204.080 44.190  1.00 93.33  ? 114 ASN   U ND2 1 
ATOM   36700 N  N   . LEU   U  7  124 ? 22.459  -204.257 45.205  1.00 86.16  ? 115 LEU   U N   1 
ATOM   36701 C  CA  . LEU   U  7  124 ? 23.909  -204.392 44.885  1.00 91.95  ? 115 LEU   U CA  1 
ATOM   36702 C  C   . LEU   U  7  124 ? 24.239  -205.878 44.675  1.00 92.63  ? 115 LEU   U C   1 
ATOM   36703 O  O   . LEU   U  7  124 ? 24.891  -206.204 43.661  1.00 94.10  ? 115 LEU   U O   1 
ATOM   36704 C  CB  . LEU   U  7  124 ? 24.751  -203.790 46.021  1.00 93.95  ? 115 LEU   U CB  1 
ATOM   36705 C  CG  . LEU   U  7  124 ? 25.215  -202.337 45.863  1.00 93.62  ? 115 LEU   U CG  1 
ATOM   36706 C  CD1 . LEU   U  7  124 ? 24.305  -201.524 44.955  1.00 95.27  ? 115 LEU   U CD1 1 
ATOM   36707 C  CD2 . LEU   U  7  124 ? 25.333  -201.660 47.223  1.00 94.43  ? 115 LEU   U CD2 1 
ATOM   36708 N  N   . SER   U  7  125 ? 23.804  -206.745 45.596  1.00 93.15  ? 116 SER   U N   1 
ATOM   36709 C  CA  . SER   U  7  125 ? 24.012  -208.216 45.531  1.00 92.87  ? 116 SER   U CA  1 
ATOM   36710 C  C   . SER   U  7  125 ? 23.409  -208.765 44.230  1.00 92.97  ? 116 SER   U C   1 
ATOM   36711 O  O   . SER   U  7  125 ? 24.076  -209.589 43.572  1.00 96.00  ? 116 SER   U O   1 
ATOM   36712 C  CB  . SER   U  7  125 ? 23.442  -208.912 46.744  1.00 92.99  ? 116 SER   U CB  1 
ATOM   36713 O  OG  . SER   U  7  125 ? 24.183  -208.597 47.912  1.00 93.10  ? 116 SER   U OG  1 
ATOM   36714 N  N   . GLN   U  7  126 ? 22.201  -208.314 43.875  1.00 89.37  ? 117 GLN   U N   1 
ATOM   36715 C  CA  . GLN   U  7  126 ? 21.482  -208.717 42.637  1.00 87.76  ? 117 GLN   U CA  1 
ATOM   36716 C  C   . GLN   U  7  126 ? 22.355  -208.408 41.416  1.00 86.84  ? 117 GLN   U C   1 
ATOM   36717 O  O   . GLN   U  7  126 ? 22.439  -209.269 40.530  1.00 86.16  ? 117 GLN   U O   1 
ATOM   36718 C  CB  . GLN   U  7  126 ? 20.132  -208.003 42.551  1.00 87.59  ? 117 GLN   U CB  1 
ATOM   36719 C  CG  . GLN   U  7  126 ? 19.266  -208.434 41.371  1.00 88.48  ? 117 GLN   U CG  1 
ATOM   36720 C  CD  . GLN   U  7  126 ? 19.727  -207.956 40.012  1.00 90.08  ? 117 GLN   U CD  1 
ATOM   36721 O  OE1 . GLN   U  7  126 ? 19.619  -208.676 39.023  1.00 88.71  ? 117 GLN   U OE1 1 
ATOM   36722 N  NE2 . GLN   U  7  126 ? 20.228  -206.732 39.931  1.00 90.13  ? 117 GLN   U NE2 1 
ATOM   36723 N  N   . ILE   U  7  127 ? 22.974  -207.225 41.366  1.00 87.25  ? 118 ILE   U N   1 
ATOM   36724 C  CA  . ILE   U  7  127 ? 23.803  -206.773 40.206  1.00 89.86  ? 118 ILE   U CA  1 
ATOM   36725 C  C   . ILE   U  7  127 ? 24.904  -207.810 39.947  1.00 89.22  ? 118 ILE   U C   1 
ATOM   36726 O  O   . ILE   U  7  127 ? 25.140  -208.120 38.768  1.00 90.36  ? 118 ILE   U O   1 
ATOM   36727 C  CB  . ILE   U  7  127 ? 24.377  -205.356 40.421  1.00 89.20  ? 118 ILE   U CB  1 
ATOM   36728 C  CG1 . ILE   U  7  127 ? 23.280  -204.290 40.339  1.00 91.87  ? 118 ILE   U CG1 1 
ATOM   36729 C  CG2 . ILE   U  7  127 ? 25.509  -205.070 39.442  1.00 87.69  ? 118 ILE   U CG2 1 
ATOM   36730 C  CD1 . ILE   U  7  127 ? 23.704  -202.917 40.824  1.00 92.80  ? 118 ILE   U CD1 1 
ATOM   36731 N  N   . TYR   U  7  128 ? 25.540  -208.339 40.998  1.00 90.94  ? 119 TYR   U N   1 
ATOM   36732 C  CA  . TYR   U  7  128 ? 26.677  -209.294 40.882  1.00 92.80  ? 119 TYR   U CA  1 
ATOM   36733 C  C   . TYR   U  7  128 ? 26.183  -210.630 40.297  1.00 91.02  ? 119 TYR   U C   1 
ATOM   36734 O  O   . TYR   U  7  128 ? 26.999  -211.355 39.675  1.00 84.98  ? 119 TYR   U O   1 
ATOM   36735 C  CB  . TYR   U  7  128 ? 27.386  -209.497 42.227  1.00 96.00  ? 119 TYR   U CB  1 
ATOM   36736 C  CG  . TYR   U  7  128 ? 27.666  -208.253 43.040  1.00 96.99  ? 119 TYR   U CG  1 
ATOM   36737 C  CD1 . TYR   U  7  128 ? 28.068  -207.065 42.449  1.00 95.91  ? 119 TYR   U CD1 1 
ATOM   36738 C  CD2 . TYR   U  7  128 ? 27.566  -208.280 44.422  1.00 96.72  ? 119 TYR   U CD2 1 
ATOM   36739 C  CE1 . TYR   U  7  128 ? 28.332  -205.934 43.206  1.00 96.78  ? 119 TYR   U CE1 1 
ATOM   36740 C  CE2 . TYR   U  7  128 ? 27.828  -207.161 45.194  1.00 95.97  ? 119 TYR   U CE2 1 
ATOM   36741 C  CZ  . TYR   U  7  128 ? 28.213  -205.982 44.585  1.00 95.75  ? 119 TYR   U CZ  1 
ATOM   36742 O  OH  . TYR   U  7  128 ? 28.467  -204.885 45.357  1.00 99.23  ? 119 TYR   U OH  1 
ATOM   36743 N  N   . THR   U  7  129 ? 24.893  -210.948 40.476  1.00 89.65  ? 120 THR   U N   1 
ATOM   36744 C  CA  . THR   U  7  129 ? 24.243  -212.179 39.946  1.00 90.94  ? 120 THR   U CA  1 
ATOM   36745 C  C   . THR   U  7  129 ? 23.918  -212.010 38.457  1.00 93.72  ? 120 THR   U C   1 
ATOM   36746 O  O   . THR   U  7  129 ? 23.673  -213.037 37.802  1.00 93.35  ? 120 THR   U O   1 
ATOM   36747 C  CB  . THR   U  7  129 ? 22.966  -212.563 40.711  1.00 90.24  ? 120 THR   U CB  1 
ATOM   36748 O  OG1 . THR   U  7  129 ? 21.922  -211.650 40.377  1.00 90.33  ? 120 THR   U OG1 1 
ATOM   36749 C  CG2 . THR   U  7  129 ? 23.154  -212.617 42.213  1.00 91.31  ? 120 THR   U CG2 1 
ATOM   36750 N  N   . GLN   U  7  130 ? 23.892  -210.772 37.950  1.00 95.63  ? 121 GLN   U N   1 
ATOM   36751 C  CA  . GLN   U  7  130 ? 23.539  -210.452 36.537  1.00 98.82  ? 121 GLN   U CA  1 
ATOM   36752 C  C   . GLN   U  7  130 ? 24.781  -209.985 35.764  1.00 101.80 ? 121 GLN   U C   1 
ATOM   36753 O  O   . GLN   U  7  130 ? 24.903  -210.359 34.582  1.00 105.90 ? 121 GLN   U O   1 
ATOM   36754 C  CB  . GLN   U  7  130 ? 22.429  -209.400 36.486  1.00 98.90  ? 121 GLN   U CB  1 
ATOM   36755 C  CG  . GLN   U  7  130 ? 21.873  -209.170 35.085  1.00 98.29  ? 121 GLN   U CG  1 
ATOM   36756 C  CD  . GLN   U  7  130 ? 20.467  -208.613 35.056  1.00 99.88  ? 121 GLN   U CD  1 
ATOM   36757 O  OE1 . GLN   U  7  130 ? 19.724  -208.824 34.098  1.00 96.07  ? 121 GLN   U OE1 1 
ATOM   36758 N  NE2 . GLN   U  7  130 ? 20.086  -207.889 36.100  1.00 101.20 ? 121 GLN   U NE2 1 
ATOM   36759 N  N   . ARG   U  7  131 ? 25.657  -209.194 36.395  1.00 104.78 ? 122 ARG   U N   1 
ATOM   36760 C  CA  . ARG   U  7  131 ? 26.919  -208.695 35.780  1.00 111.04 ? 122 ARG   U CA  1 
ATOM   36761 C  C   . ARG   U  7  131 ? 27.995  -209.776 35.954  1.00 110.47 ? 122 ARG   U C   1 
ATOM   36762 O  O   . ARG   U  7  131 ? 28.033  -210.408 37.032  1.00 112.04 ? 122 ARG   U O   1 
ATOM   36763 C  CB  . ARG   U  7  131 ? 27.332  -207.347 36.388  1.00 116.38 ? 122 ARG   U CB  1 
ATOM   36764 C  CG  . ARG   U  7  131 ? 27.818  -206.320 35.372  1.00 119.46 ? 122 ARG   U CG  1 
ATOM   36765 C  CD  . ARG   U  7  131 ? 26.749  -205.311 34.985  1.00 123.80 ? 122 ARG   U CD  1 
ATOM   36766 N  NE  . ARG   U  7  131 ? 26.717  -204.170 35.893  1.00 130.93 ? 122 ARG   U NE  1 
ATOM   36767 C  CZ  . ARG   U  7  131 ? 25.750  -203.253 35.947  1.00 139.99 ? 122 ARG   U CZ  1 
ATOM   36768 N  NH1 . ARG   U  7  131 ? 24.699  -203.331 35.146  1.00 144.84 ? 122 ARG   U NH1 1 
ATOM   36769 N  NH2 . ARG   U  7  131 ? 25.837  -202.256 36.813  1.00 141.95 ? 122 ARG   U NH2 1 
ATOM   36770 N  N   . ALA   U  7  132 ? 28.832  -209.984 34.932  1.00 108.12 ? 123 ALA   U N   1 
ATOM   36771 C  CA  . ALA   U  7  132 ? 29.763  -211.133 34.824  1.00 109.72 ? 123 ALA   U CA  1 
ATOM   36772 C  C   . ALA   U  7  132 ? 31.099  -210.840 35.521  1.00 110.83 ? 123 ALA   U C   1 
ATOM   36773 O  O   . ALA   U  7  132 ? 31.651  -211.784 36.119  1.00 113.51 ? 123 ALA   U O   1 
ATOM   36774 C  CB  . ALA   U  7  132 ? 29.976  -211.491 33.375  1.00 108.56 ? 123 ALA   U CB  1 
ATOM   36775 N  N   . TYR   U  7  133 ? 31.605  -209.601 35.441  1.00 114.82 ? 124 TYR   U N   1 
ATOM   36776 C  CA  . TYR   U  7  133 ? 32.969  -209.222 35.908  1.00 112.69 ? 124 TYR   U CA  1 
ATOM   36777 C  C   . TYR   U  7  133 ? 33.020  -209.240 37.442  1.00 110.79 ? 124 TYR   U C   1 
ATOM   36778 O  O   . TYR   U  7  133 ? 34.125  -209.430 37.991  1.00 107.45 ? 124 TYR   U O   1 
ATOM   36779 C  CB  . TYR   U  7  133 ? 33.420  -207.888 35.294  1.00 114.01 ? 124 TYR   U CB  1 
ATOM   36780 C  CG  . TYR   U  7  133 ? 33.021  -206.625 36.020  1.00 116.19 ? 124 TYR   U CG  1 
ATOM   36781 C  CD1 . TYR   U  7  133 ? 31.726  -206.135 35.953  1.00 115.74 ? 124 TYR   U CD1 1 
ATOM   36782 C  CD2 . TYR   U  7  133 ? 33.955  -205.883 36.730  1.00 115.15 ? 124 TYR   U CD2 1 
ATOM   36783 C  CE1 . TYR   U  7  133 ? 31.358  -204.966 36.602  1.00 116.36 ? 124 TYR   U CE1 1 
ATOM   36784 C  CE2 . TYR   U  7  133 ? 33.604  -204.712 37.384  1.00 116.45 ? 124 TYR   U CE2 1 
ATOM   36785 C  CZ  . TYR   U  7  133 ? 32.300  -204.251 37.320  1.00 118.58 ? 124 TYR   U CZ  1 
ATOM   36786 O  OH  . TYR   U  7  133 ? 31.938  -203.098 37.955  1.00 120.21 ? 124 TYR   U OH  1 
ATOM   36787 N  N   . MET   U  7  134 ? 31.865  -209.084 38.101  1.00 109.05 ? 125 MET   U N   1 
ATOM   36788 C  CA  . MET   U  7  134 ? 31.730  -209.042 39.582  1.00 109.95 ? 125 MET   U CA  1 
ATOM   36789 C  C   . MET   U  7  134 ? 31.230  -210.405 40.084  1.00 103.06 ? 125 MET   U C   1 
ATOM   36790 O  O   . MET   U  7  134 ? 30.205  -210.894 39.554  1.00 96.74  ? 125 MET   U O   1 
ATOM   36791 C  CB  . MET   U  7  134 ? 30.752  -207.936 39.996  1.00 116.24 ? 125 MET   U CB  1 
ATOM   36792 C  CG  . MET   U  7  134 ? 31.280  -206.526 39.735  1.00 119.36 ? 125 MET   U CG  1 
ATOM   36793 S  SD  . MET   U  7  134 ? 31.666  -205.586 41.243  1.00 122.34 ? 125 MET   U SD  1 
ATOM   36794 C  CE  . MET   U  7  134 ? 32.753  -206.728 42.098  1.00 126.94 ? 125 MET   U CE  1 
ATOM   36795 N  N   . ARG   U  7  135 ? 31.948  -211.006 41.042  1.00 99.76  ? 126 ARG   U N   1 
ATOM   36796 C  CA  . ARG   U  7  135 ? 31.500  -212.220 41.778  1.00 96.53  ? 126 ARG   U CA  1 
ATOM   36797 C  C   . ARG   U  7  135 ? 30.517  -211.789 42.861  1.00 94.75  ? 126 ARG   U C   1 
ATOM   36798 O  O   . ARG   U  7  135 ? 30.599  -210.668 43.357  1.00 97.89  ? 126 ARG   U O   1 
ATOM   36799 C  CB  . ARG   U  7  135 ? 32.682  -212.996 42.375  1.00 96.64  ? 126 ARG   U CB  1 
ATOM   36800 C  CG  . ARG   U  7  135 ? 33.381  -212.346 43.564  1.00 94.34  ? 126 ARG   U CG  1 
ATOM   36801 C  CD  . ARG   U  7  135 ? 34.262  -213.357 44.279  1.00 93.40  ? 126 ARG   U CD  1 
ATOM   36802 N  NE  . ARG   U  7  135 ? 35.080  -212.796 45.348  1.00 92.00  ? 126 ARG   U NE  1 
ATOM   36803 C  CZ  . ARG   U  7  135 ? 34.709  -212.657 46.620  1.00 91.06  ? 126 ARG   U CZ  1 
ATOM   36804 N  NH1 . ARG   U  7  135 ? 33.499  -213.018 47.019  1.00 89.00  ? 126 ARG   U NH1 1 
ATOM   36805 N  NH2 . ARG   U  7  135 ? 35.559  -212.144 47.493  1.00 92.33  ? 126 ARG   U NH2 1 
ATOM   36806 N  N   . PRO   U  7  136 ? 29.549  -212.647 43.252  1.00 94.04  ? 127 PRO   U N   1 
ATOM   36807 C  CA  . PRO   U  7  136 ? 28.766  -212.407 44.461  1.00 93.25  ? 127 PRO   U CA  1 
ATOM   36808 C  C   . PRO   U  7  136 ? 29.694  -212.436 45.682  1.00 92.04  ? 127 PRO   U C   1 
ATOM   36809 O  O   . PRO   U  7  136 ? 30.734  -213.064 45.603  1.00 94.16  ? 127 PRO   U O   1 
ATOM   36810 C  CB  . PRO   U  7  136 ? 27.768  -213.573 44.517  1.00 94.40  ? 127 PRO   U CB  1 
ATOM   36811 C  CG  . PRO   U  7  136 ? 27.766  -214.150 43.114  1.00 95.75  ? 127 PRO   U CG  1 
ATOM   36812 C  CD  . PRO   U  7  136 ? 29.148  -213.878 42.557  1.00 94.59  ? 127 PRO   U CD  1 
ATOM   36813 N  N   . LEU   U  7  137 ? 29.316  -211.751 46.763  1.00 92.67  ? 128 LEU   U N   1 
ATOM   36814 C  CA  . LEU   U  7  137 ? 29.989  -211.880 48.082  1.00 93.39  ? 128 LEU   U CA  1 
ATOM   36815 C  C   . LEU   U  7  137 ? 29.431  -213.131 48.768  1.00 93.15  ? 128 LEU   U C   1 
ATOM   36816 O  O   . LEU   U  7  137 ? 28.193  -213.293 48.780  1.00 96.47  ? 128 LEU   U O   1 
ATOM   36817 C  CB  . LEU   U  7  137 ? 29.743  -210.627 48.930  1.00 91.13  ? 128 LEU   U CB  1 
ATOM   36818 C  CG  . LEU   U  7  137 ? 30.203  -209.296 48.333  1.00 88.95  ? 128 LEU   U CG  1 
ATOM   36819 C  CD1 . LEU   U  7  137 ? 29.781  -208.147 49.232  1.00 87.09  ? 128 LEU   U CD1 1 
ATOM   36820 C  CD2 . LEU   U  7  137 ? 31.710  -209.270 48.115  1.00 87.59  ? 128 LEU   U CD2 1 
ATOM   36821 N  N   . GLY   U  7  138 ? 30.306  -213.989 49.296  1.00 94.59  ? 129 GLY   U N   1 
ATOM   36822 C  CA  . GLY   U  7  138 ? 29.913  -215.219 50.008  1.00 94.63  ? 129 GLY   U CA  1 
ATOM   36823 C  C   . GLY   U  7  138 ? 29.465  -214.908 51.423  1.00 92.38  ? 129 GLY   U C   1 
ATOM   36824 O  O   . GLY   U  7  138 ? 30.118  -215.389 52.361  1.00 95.88  ? 129 GLY   U O   1 
ATOM   36825 N  N   . VAL   U  7  139 ? 28.396  -214.123 51.575  1.00 89.79  ? 130 VAL   U N   1 
ATOM   36826 C  CA  . VAL   U  7  139 ? 27.920  -213.617 52.896  1.00 90.12  ? 130 VAL   U CA  1 
ATOM   36827 C  C   . VAL   U  7  139 ? 26.392  -213.536 52.899  1.00 88.37  ? 130 VAL   U C   1 
ATOM   36828 O  O   . VAL   U  7  139 ? 25.795  -213.295 51.831  1.00 85.06  ? 130 VAL   U O   1 
ATOM   36829 C  CB  . VAL   U  7  139 ? 28.540  -212.248 53.242  1.00 90.85  ? 130 VAL   U CB  1 
ATOM   36830 C  CG1 . VAL   U  7  139 ? 30.034  -212.355 53.506  1.00 93.16  ? 130 VAL   U CG1 1 
ATOM   36831 C  CG2 . VAL   U  7  139 ? 28.260  -211.202 52.172  1.00 91.48  ? 130 VAL   U CG2 1 
ATOM   36832 N  N   . ILE   U  7  140 ? 25.803  -213.728 54.079  1.00 88.32  ? 131 ILE   U N   1 
ATOM   36833 C  CA  . ILE   U  7  140 ? 24.381  -213.412 54.393  1.00 91.13  ? 131 ILE   U CA  1 
ATOM   36834 C  C   . ILE   U  7  140 ? 24.391  -212.308 55.456  1.00 89.79  ? 131 ILE   U C   1 
ATOM   36835 O  O   . ILE   U  7  140 ? 24.984  -212.518 56.530  1.00 86.47  ? 131 ILE   U O   1 
ATOM   36836 C  CB  . ILE   U  7  140 ? 23.627  -214.681 54.840  1.00 93.18  ? 131 ILE   U CB  1 
ATOM   36837 C  CG1 . ILE   U  7  140 ? 23.399  -215.626 53.656  1.00 98.50  ? 131 ILE   U CG1 1 
ATOM   36838 C  CG2 . ILE   U  7  140 ? 22.323  -214.333 55.546  1.00 92.54  ? 131 ILE   U CG2 1 
ATOM   36839 C  CD1 . ILE   U  7  140 ? 22.845  -216.989 54.028  1.00 100.71 ? 131 ILE   U CD1 1 
ATOM   36840 N  N   . LEU   U  7  141 ? 23.785  -211.161 55.147  1.00 89.84  ? 132 LEU   U N   1 
ATOM   36841 C  CA  . LEU   U  7  141 ? 23.781  -209.959 56.021  1.00 91.30  ? 132 LEU   U CA  1 
ATOM   36842 C  C   . LEU   U  7  141 ? 22.430  -209.864 56.734  1.00 94.21  ? 132 LEU   U C   1 
ATOM   36843 O  O   . LEU   U  7  141 ? 21.401  -209.773 56.037  1.00 91.42  ? 132 LEU   U O   1 
ATOM   36844 C  CB  . LEU   U  7  141 ? 24.029  -208.710 55.170  1.00 89.23  ? 132 LEU   U CB  1 
ATOM   36845 C  CG  . LEU   U  7  141 ? 25.180  -208.801 54.171  1.00 88.31  ? 132 LEU   U CG  1 
ATOM   36846 C  CD1 . LEU   U  7  141 ? 25.234  -207.554 53.308  1.00 87.42  ? 132 LEU   U CD1 1 
ATOM   36847 C  CD2 . LEU   U  7  141 ? 26.505  -209.015 54.886  1.00 89.51  ? 132 LEU   U CD2 1 
ATOM   36848 N  N   . THR   U  7  142 ? 22.442  -209.884 58.068  1.00 99.07  ? 133 THR   U N   1 
ATOM   36849 C  CA  . THR   U  7  142 ? 21.246  -209.657 58.920  1.00 101.31 ? 133 THR   U CA  1 
ATOM   36850 C  C   . THR   U  7  142 ? 21.315  -208.239 59.493  1.00 99.65  ? 133 THR   U C   1 
ATOM   36851 O  O   . THR   U  7  142 ? 22.231  -207.982 60.294  1.00 106.50 ? 133 THR   U O   1 
ATOM   36852 C  CB  . THR   U  7  142 ? 21.134  -210.687 60.051  1.00 103.19 ? 133 THR   U CB  1 
ATOM   36853 O  OG1 . THR   U  7  142 ? 21.478  -211.984 59.558  1.00 105.43 ? 133 THR   U OG1 1 
ATOM   36854 C  CG2 . THR   U  7  142 ? 19.746  -210.710 60.651  1.00 103.87 ? 133 THR   U CG2 1 
ATOM   36855 N  N   . PHE   U  7  143 ? 20.387  -207.364 59.090  1.00 97.61  ? 134 PHE   U N   1 
ATOM   36856 C  CA  . PHE   U  7  143 ? 20.281  -205.957 59.558  1.00 95.15  ? 134 PHE   U CA  1 
ATOM   36857 C  C   . PHE   U  7  143 ? 19.231  -205.880 60.671  1.00 92.29  ? 134 PHE   U C   1 
ATOM   36858 O  O   . PHE   U  7  143 ? 18.139  -206.462 60.510  1.00 89.81  ? 134 PHE   U O   1 
ATOM   36859 C  CB  . PHE   U  7  143 ? 19.940  -205.019 58.396  1.00 92.81  ? 134 PHE   U CB  1 
ATOM   36860 C  CG  . PHE   U  7  143 ? 21.001  -204.945 57.328  1.00 91.29  ? 134 PHE   U CG  1 
ATOM   36861 C  CD1 . PHE   U  7  143 ? 22.101  -204.114 57.474  1.00 90.55  ? 134 PHE   U CD1 1 
ATOM   36862 C  CD2 . PHE   U  7  143 ? 20.905  -205.717 56.182  1.00 92.66  ? 134 PHE   U CD2 1 
ATOM   36863 C  CE1 . PHE   U  7  143 ? 23.080  -204.054 56.494  1.00 90.37  ? 134 PHE   U CE1 1 
ATOM   36864 C  CE2 . PHE   U  7  143 ? 21.886  -205.658 55.203  1.00 92.80  ? 134 PHE   U CE2 1 
ATOM   36865 C  CZ  . PHE   U  7  143 ? 22.972  -204.828 55.362  1.00 91.62  ? 134 PHE   U CZ  1 
ATOM   36866 N  N   . VAL   U  7  144 ? 19.559  -205.178 61.761  1.00 91.96  ? 135 VAL   U N   1 
ATOM   36867 C  CA  . VAL   U  7  144 ? 18.677  -205.009 62.954  1.00 93.22  ? 135 VAL   U CA  1 
ATOM   36868 C  C   . VAL   U  7  144 ? 18.635  -203.530 63.348  1.00 93.48  ? 135 VAL   U C   1 
ATOM   36869 O  O   . VAL   U  7  144 ? 19.665  -202.839 63.202  1.00 92.31  ? 135 VAL   U O   1 
ATOM   36870 C  CB  . VAL   U  7  144 ? 19.141  -205.886 64.131  1.00 92.94  ? 135 VAL   U CB  1 
ATOM   36871 C  CG1 . VAL   U  7  144 ? 18.940  -207.360 63.828  1.00 93.50  ? 135 VAL   U CG1 1 
ATOM   36872 C  CG2 . VAL   U  7  144 ? 20.586  -205.607 64.520  1.00 93.01  ? 135 VAL   U CG2 1 
ATOM   36873 N  N   . SER   U  7  145 ? 17.476  -203.078 63.831  1.00 95.30  ? 136 SER   U N   1 
ATOM   36874 C  CA  . SER   U  7  145 ? 17.241  -201.701 64.332  1.00 96.12  ? 136 SER   U CA  1 
ATOM   36875 C  C   . SER   U  7  145 ? 15.936  -201.657 65.128  1.00 97.25  ? 136 SER   U C   1 
ATOM   36876 O  O   . SER   U  7  145 ? 15.234  -202.688 65.187  1.00 93.67  ? 136 SER   U O   1 
ATOM   36877 C  CB  . SER   U  7  145 ? 17.207  -200.704 63.199  1.00 97.09  ? 136 SER   U CB  1 
ATOM   36878 O  OG  . SER   U  7  145 ? 15.927  -200.671 62.583  1.00 98.95  ? 136 SER   U OG  1 
ATOM   36879 N  N   . VAL   U  7  146 ? 15.646  -200.494 65.714  1.00 99.98  ? 137 VAL   U N   1 
ATOM   36880 C  CA  . VAL   U  7  146 ? 14.289  -200.086 66.182  1.00 101.75 ? 137 VAL   U CA  1 
ATOM   36881 C  C   . VAL   U  7  146 ? 13.881  -198.879 65.331  1.00 102.29 ? 137 VAL   U C   1 
ATOM   36882 O  O   . VAL   U  7  146 ? 14.140  -197.734 65.757  1.00 103.39 ? 137 VAL   U O   1 
ATOM   36883 C  CB  . VAL   U  7  146 ? 14.264  -199.789 67.694  1.00 101.13 ? 137 VAL   U CB  1 
ATOM   36884 C  CG1 . VAL   U  7  146 ? 12.874  -199.398 68.178  1.00 98.61  ? 137 VAL   U CG1 1 
ATOM   36885 C  CG2 . VAL   U  7  146 ? 14.791  -200.970 68.493  1.00 100.90 ? 137 VAL   U CG2 1 
ATOM   36886 N  N   . ASP   U  7  147 ? 13.310  -199.144 64.152  1.00 103.36 ? 138 ASP   U N   1 
ATOM   36887 C  CA  . ASP   U  7  147 ? 12.929  -198.116 63.147  1.00 102.91 ? 138 ASP   U CA  1 
ATOM   36888 C  C   . ASP   U  7  147 ? 11.924  -197.154 63.787  1.00 106.77 ? 138 ASP   U C   1 
ATOM   36889 O  O   . ASP   U  7  147 ? 11.043  -197.631 64.530  1.00 107.56 ? 138 ASP   U O   1 
ATOM   36890 C  CB  . ASP   U  7  147 ? 12.350  -198.755 61.884  1.00 105.92 ? 138 ASP   U CB  1 
ATOM   36891 C  CG  . ASP   U  7  147 ? 12.259  -197.786 60.721  1.00 106.46 ? 138 ASP   U CG  1 
ATOM   36892 O  OD1 . ASP   U  7  147 ? 13.322  -197.328 60.264  1.00 108.68 ? 138 ASP   U OD1 1 
ATOM   36893 O  OD2 . ASP   U  7  147 ? 11.127  -197.480 60.298  1.00 112.09 ? 138 ASP   U OD2 1 
ATOM   36894 N  N   . GLU   U  7  148 ? 12.051  -195.853 63.509  1.00 106.21 ? 139 GLU   U N   1 
ATOM   36895 C  CA  . GLU   U  7  148 ? 11.199  -194.799 64.123  1.00 109.05 ? 139 GLU   U CA  1 
ATOM   36896 C  C   . GLU   U  7  148 ? 9.762   -194.904 63.589  1.00 104.59 ? 139 GLU   U C   1 
ATOM   36897 O  O   . GLU   U  7  148 ? 8.865   -194.353 64.251  1.00 108.15 ? 139 GLU   U O   1 
ATOM   36898 C  CB  . GLU   U  7  148 ? 11.803  -193.407 63.916  1.00 109.93 ? 139 GLU   U CB  1 
ATOM   36899 C  CG  . GLU   U  7  148 ? 11.872  -192.943 62.471  1.00 111.78 ? 139 GLU   U CG  1 
ATOM   36900 C  CD  . GLU   U  7  148 ? 12.373  -191.516 62.317  1.00 112.86 ? 139 GLU   U CD  1 
ATOM   36901 O  OE1 . GLU   U  7  148 ? 13.165  -191.261 61.386  1.00 111.90 ? 139 GLU   U OE1 1 
ATOM   36902 O  OE2 . GLU   U  7  148 ? 11.968  -190.658 63.128  1.00 116.71 ? 139 GLU   U OE2 1 
ATOM   36903 N  N   . GLU   U  7  149 ? 9.543   -195.595 62.463  1.00 104.62 ? 140 GLU   U N   1 
ATOM   36904 C  CA  . GLU   U  7  149 ? 8.193   -195.820 61.874  1.00 106.08 ? 140 GLU   U CA  1 
ATOM   36905 C  C   . GLU   U  7  149 ? 7.717   -197.256 62.133  1.00 104.56 ? 140 GLU   U C   1 
ATOM   36906 O  O   . GLU   U  7  149 ? 6.603   -197.404 62.671  1.00 104.59 ? 140 GLU   U O   1 
ATOM   36907 C  CB  . GLU   U  7  149 ? 8.198   -195.522 60.374  1.00 109.28 ? 140 GLU   U CB  1 
ATOM   36908 C  CG  . GLU   U  7  149 ? 8.245   -194.039 60.057  1.00 111.72 ? 140 GLU   U CG  1 
ATOM   36909 C  CD  . GLU   U  7  149 ? 7.930   -193.687 58.612  1.00 114.30 ? 140 GLU   U CD  1 
ATOM   36910 O  OE1 . GLU   U  7  149 ? 6.851   -194.085 58.128  1.00 118.05 ? 140 GLU   U OE1 1 
ATOM   36911 O  OE2 . GLU   U  7  149 ? 8.764   -193.015 57.972  1.00 118.17 ? 140 GLU   U OE2 1 
ATOM   36912 N  N   . LEU   U  7  150 ? 8.512   -198.266 61.758  1.00 101.49 ? 141 LEU   U N   1 
ATOM   36913 C  CA  . LEU   U  7  150 ? 8.101   -199.701 61.768  1.00 101.38 ? 141 LEU   U CA  1 
ATOM   36914 C  C   . LEU   U  7  150 ? 8.358   -200.349 63.137  1.00 99.68  ? 141 LEU   U C   1 
ATOM   36915 O  O   . LEU   U  7  150 ? 7.722   -201.384 63.410  1.00 99.32  ? 141 LEU   U O   1 
ATOM   36916 C  CB  . LEU   U  7  150 ? 8.841   -200.466 60.663  1.00 100.00 ? 141 LEU   U CB  1 
ATOM   36917 C  CG  . LEU   U  7  150 ? 8.516   -200.072 59.221  1.00 99.97  ? 141 LEU   U CG  1 
ATOM   36918 C  CD1 . LEU   U  7  150 ? 9.295   -200.939 58.243  1.00 98.05  ? 141 LEU   U CD1 1 
ATOM   36919 C  CD2 . LEU   U  7  150 ? 7.024   -200.166 58.932  1.00 100.26 ? 141 LEU   U CD2 1 
ATOM   36920 N  N   . GLY   U  7  151 ? 9.251   -199.789 63.961  1.00 99.60  ? 142 GLY   U N   1 
ATOM   36921 C  CA  . GLY   U  7  151 ? 9.607   -200.345 65.284  1.00 101.03 ? 142 GLY   U CA  1 
ATOM   36922 C  C   . GLY   U  7  151 ? 10.701  -201.406 65.179  1.00 100.00 ? 142 GLY   U C   1 
ATOM   36923 O  O   . GLY   U  7  151 ? 11.482  -201.393 64.229  1.00 102.15 ? 142 GLY   U O   1 
ATOM   36924 N  N   . PRO   U  7  152 ? 10.800  -202.353 66.145  1.00 96.80  ? 143 PRO   U N   1 
ATOM   36925 C  CA  . PRO   U  7  152 ? 11.818  -203.404 66.097  1.00 95.74  ? 143 PRO   U CA  1 
ATOM   36926 C  C   . PRO   U  7  152 ? 11.787  -204.126 64.744  1.00 94.68  ? 143 PRO   U C   1 
ATOM   36927 O  O   . PRO   U  7  152 ? 10.722  -204.575 64.364  1.00 94.47  ? 143 PRO   U O   1 
ATOM   36928 C  CB  . PRO   U  7  152 ? 11.424  -204.349 67.241  1.00 96.11  ? 143 PRO   U CB  1 
ATOM   36929 C  CG  . PRO   U  7  152 ? 10.678  -203.460 68.209  1.00 97.72  ? 143 PRO   U CG  1 
ATOM   36930 C  CD  . PRO   U  7  152 ? 9.942   -202.465 67.333  1.00 97.86  ? 143 PRO   U CD  1 
ATOM   36931 N  N   . SER   U  7  153 ? 12.932  -204.194 64.056  1.00 95.59  ? 144 SER   U N   1 
ATOM   36932 C  CA  . SER   U  7  153 ? 13.044  -204.652 62.646  1.00 96.57  ? 144 SER   U CA  1 
ATOM   36933 C  C   . SER   U  7  153 ? 14.233  -205.602 62.474  1.00 94.19  ? 144 SER   U C   1 
ATOM   36934 O  O   . SER   U  7  153 ? 15.345  -205.246 62.910  1.00 93.30  ? 144 SER   U O   1 
ATOM   36935 C  CB  . SER   U  7  153 ? 13.163  -203.480 61.706  1.00 95.89  ? 144 SER   U CB  1 
ATOM   36936 O  OG  . SER   U  7  153 ? 12.019  -202.642 61.780  1.00 98.92  ? 144 SER   U OG  1 
ATOM   36937 N  N   . ILE   U  7  154 ? 13.990  -206.760 61.852  1.00 94.56  ? 145 ILE   U N   1 
ATOM   36938 C  CA  . ILE   U  7  154 ? 15.035  -207.692 61.338  1.00 91.85  ? 145 ILE   U CA  1 
ATOM   36939 C  C   . ILE   U  7  154 ? 14.805  -207.858 59.834  1.00 92.65  ? 145 ILE   U C   1 
ATOM   36940 O  O   . ILE   U  7  154 ? 13.695  -208.277 59.455  1.00 94.91  ? 145 ILE   U O   1 
ATOM   36941 C  CB  . ILE   U  7  154 ? 15.004  -209.051 62.065  1.00 91.68  ? 145 ILE   U CB  1 
ATOM   36942 C  CG1 . ILE   U  7  154 ? 14.974  -208.894 63.587  1.00 92.50  ? 145 ILE   U CG1 1 
ATOM   36943 C  CG2 . ILE   U  7  154 ? 16.175  -209.910 61.616  1.00 89.59  ? 145 ILE   U CG2 1 
ATOM   36944 C  CD1 . ILE   U  7  154 ? 14.514  -210.132 64.317  1.00 95.64  ? 145 ILE   U CD1 1 
ATOM   36945 N  N   . TYR   U  7  155 ? 15.810  -207.521 59.023  1.00 92.43  ? 146 TYR   U N   1 
ATOM   36946 C  CA  . TYR   U  7  155 ? 15.820  -207.692 57.547  1.00 93.90  ? 146 TYR   U CA  1 
ATOM   36947 C  C   . TYR   U  7  155 ? 17.132  -208.381 57.154  1.00 92.77  ? 146 TYR   U C   1 
ATOM   36948 O  O   . TYR   U  7  155 ? 18.188  -207.999 57.698  1.00 94.36  ? 146 TYR   U O   1 
ATOM   36949 C  CB  . TYR   U  7  155 ? 15.608  -206.339 56.864  1.00 91.51  ? 146 TYR   U CB  1 
ATOM   36950 C  CG  . TYR   U  7  155 ? 14.189  -205.829 56.939  1.00 94.63  ? 146 TYR   U CG  1 
ATOM   36951 C  CD1 . TYR   U  7  155 ? 13.694  -205.244 58.094  1.00 94.34  ? 146 TYR   U CD1 1 
ATOM   36952 C  CD2 . TYR   U  7  155 ? 13.327  -205.949 55.860  1.00 94.82  ? 146 TYR   U CD2 1 
ATOM   36953 C  CE1 . TYR   U  7  155 ? 12.387  -204.787 58.174  1.00 95.52  ? 146 TYR   U CE1 1 
ATOM   36954 C  CE2 . TYR   U  7  155 ? 12.019  -205.493 55.920  1.00 95.06  ? 146 TYR   U CE2 1 
ATOM   36955 C  CZ  . TYR   U  7  155 ? 11.545  -204.912 57.084  1.00 94.99  ? 146 TYR   U CZ  1 
ATOM   36956 O  OH  . TYR   U  7  155 ? 10.260  -204.456 57.155  1.00 97.57  ? 146 TYR   U OH  1 
ATOM   36957 N  N   . LYS   U  7  156 ? 17.065  -209.382 56.268  1.00 92.70  ? 147 LYS   U N   1 
ATOM   36958 C  CA  . LYS   U  7  156 ? 18.216  -210.265 55.935  1.00 94.02  ? 147 LYS   U CA  1 
ATOM   36959 C  C   . LYS   U  7  156 ? 18.435  -210.319 54.420  1.00 89.50  ? 147 LYS   U C   1 
ATOM   36960 O  O   . LYS   U  7  156 ? 17.442  -210.402 53.678  1.00 85.87  ? 147 LYS   U O   1 
ATOM   36961 C  CB  . LYS   U  7  156 ? 17.994  -211.673 56.494  1.00 96.31  ? 147 LYS   U CB  1 
ATOM   36962 C  CG  . LYS   U  7  156 ? 19.244  -212.542 56.535  1.00 98.32  ? 147 LYS   U CG  1 
ATOM   36963 C  CD  . LYS   U  7  156 ? 19.153  -213.699 57.502  1.00 99.93  ? 147 LYS   U CD  1 
ATOM   36964 C  CE  . LYS   U  7  156 ? 18.396  -214.882 56.941  1.00 102.39 ? 147 LYS   U CE  1 
ATOM   36965 N  NZ  . LYS   U  7  156 ? 18.465  -216.044 57.858  1.00 106.19 ? 147 LYS   U NZ  1 
ATOM   36966 N  N   . THR   U  7  157 ? 19.707  -210.304 54.008  1.00 90.34  ? 148 THR   U N   1 
ATOM   36967 C  CA  . THR   U  7  157 ? 20.181  -210.302 52.598  1.00 95.54  ? 148 THR   U CA  1 
ATOM   36968 C  C   . THR   U  7  157 ? 21.034  -211.550 52.347  1.00 94.35  ? 148 THR   U C   1 
ATOM   36969 O  O   . THR   U  7  157 ? 21.699  -212.000 53.295  1.00 94.40  ? 148 THR   U O   1 
ATOM   36970 C  CB  . THR   U  7  157 ? 20.997  -209.036 52.306  1.00 97.83  ? 148 THR   U CB  1 
ATOM   36971 O  OG1 . THR   U  7  157 ? 20.114  -207.915 52.368  1.00 102.04 ? 148 THR   U OG1 1 
ATOM   36972 C  CG2 . THR   U  7  157 ? 21.691  -209.068 50.961  1.00 100.21 ? 148 THR   U CG2 1 
ATOM   36973 N  N   . ASP   U  7  158 ? 21.032  -212.066 51.114  1.00 94.68  ? 149 ASP   U N   1 
ATOM   36974 C  CA  . ASP   U  7  158 ? 21.828  -213.256 50.705  1.00 98.11  ? 149 ASP   U CA  1 
ATOM   36975 C  C   . ASP   U  7  158 ? 22.495  -212.981 49.357  1.00 98.17  ? 149 ASP   U C   1 
ATOM   36976 O  O   . ASP   U  7  158 ? 22.205  -211.970 48.722  1.00 100.29 ? 149 ASP   U O   1 
ATOM   36977 C  CB  . ASP   U  7  158 ? 20.957  -214.517 50.694  1.00 101.21 ? 149 ASP   U CB  1 
ATOM   36978 C  CG  . ASP   U  7  158 ? 19.722  -214.431 49.814  1.00 103.24 ? 149 ASP   U CG  1 
ATOM   36979 O  OD1 . ASP   U  7  158 ? 19.760  -213.691 48.808  1.00 102.63 ? 149 ASP   U OD1 1 
ATOM   36980 O  OD2 . ASP   U  7  158 ? 18.730  -215.115 50.139  1.00 107.03 ? 149 ASP   U OD2 1 
ATOM   36981 N  N   . PRO   U  7  159 ? 23.425  -213.853 48.893  1.00 96.39  ? 150 PRO   U N   1 
ATOM   36982 C  CA  . PRO   U  7  159 ? 24.108  -213.658 47.609  1.00 94.62  ? 150 PRO   U CA  1 
ATOM   36983 C  C   . PRO   U  7  159 ? 23.218  -213.655 46.352  1.00 93.03  ? 150 PRO   U C   1 
ATOM   36984 O  O   . PRO   U  7  159 ? 23.684  -213.194 45.322  1.00 93.23  ? 150 PRO   U O   1 
ATOM   36985 C  CB  . PRO   U  7  159 ? 25.087  -214.844 47.540  1.00 93.61  ? 150 PRO   U CB  1 
ATOM   36986 C  CG  . PRO   U  7  159 ? 25.302  -215.230 48.983  1.00 95.35  ? 150 PRO   U CG  1 
ATOM   36987 C  CD  . PRO   U  7  159 ? 23.943  -215.025 49.617  1.00 96.57  ? 150 PRO   U CD  1 
ATOM   36988 N  N   . ALA   U  7  160 ? 21.983  -214.160 46.449  1.00 93.15  ? 151 ALA   U N   1 
ATOM   36989 C  CA  . ALA   U  7  160 ? 20.996  -214.183 45.342  1.00 95.42  ? 151 ALA   U CA  1 
ATOM   36990 C  C   . ALA   U  7  160 ? 20.415  -212.782 45.124  1.00 94.87  ? 151 ALA   U C   1 
ATOM   36991 O  O   . ALA   U  7  160 ? 19.883  -212.535 44.027  1.00 94.03  ? 151 ALA   U O   1 
ATOM   36992 C  CB  . ALA   U  7  160 ? 19.900  -215.179 45.633  1.00 97.49  ? 151 ALA   U CB  1 
ATOM   36993 N  N   . GLY   U  7  161 ? 20.511  -211.912 46.134  1.00 95.60  ? 152 GLY   U N   1 
ATOM   36994 C  CA  . GLY   U  7  161 ? 19.912  -210.564 46.134  1.00 97.68  ? 152 GLY   U CA  1 
ATOM   36995 C  C   . GLY   U  7  161 ? 18.503  -210.581 46.700  1.00 98.58  ? 152 GLY   U C   1 
ATOM   36996 O  O   . GLY   U  7  161 ? 17.800  -209.571 46.551  1.00 102.14 ? 152 GLY   U O   1 
ATOM   36997 N  N   . TYR   U  7  162 ? 18.098  -211.691 47.321  1.00 100.35 ? 153 TYR   U N   1 
ATOM   36998 C  CA  . TYR   U  7  162 ? 16.806  -211.833 48.041  1.00 100.91 ? 153 TYR   U CA  1 
ATOM   36999 C  C   . TYR   U  7  162 ? 16.913  -211.063 49.363  1.00 97.36  ? 153 TYR   U C   1 
ATOM   37000 O  O   . TYR   U  7  162 ? 18.026  -210.960 49.921  1.00 96.18  ? 153 TYR   U O   1 
ATOM   37001 C  CB  . TYR   U  7  162 ? 16.474  -213.317 48.229  1.00 102.79 ? 153 TYR   U CB  1 
ATOM   37002 C  CG  . TYR   U  7  162 ? 15.254  -213.625 49.060  1.00 107.08 ? 153 TYR   U CG  1 
ATOM   37003 C  CD1 . TYR   U  7  162 ? 15.354  -213.841 50.425  1.00 108.91 ? 153 TYR   U CD1 1 
ATOM   37004 C  CD2 . TYR   U  7  162 ? 14.002  -213.741 48.478  1.00 112.28 ? 153 TYR   U CD2 1 
ATOM   37005 C  CE1 . TYR   U  7  162 ? 14.241  -214.142 51.194  1.00 115.57 ? 153 TYR   U CE1 1 
ATOM   37006 C  CE2 . TYR   U  7  162 ? 12.878  -214.041 49.232  1.00 117.10 ? 153 TYR   U CE2 1 
ATOM   37007 C  CZ  . TYR   U  7  162 ? 12.997  -214.244 50.595  1.00 118.23 ? 153 TYR   U CZ  1 
ATOM   37008 O  OH  . TYR   U  7  162 ? 11.891  -214.543 51.340  1.00 124.10 ? 153 TYR   U OH  1 
ATOM   37009 N  N   . TYR   U  7  163 ? 15.797  -210.504 49.831  1.00 92.71  ? 154 TYR   U N   1 
ATOM   37010 C  CA  . TYR   U  7  163 ? 15.678  -209.891 51.179  1.00 95.55  ? 154 TYR   U CA  1 
ATOM   37011 C  C   . TYR   U  7  163 ? 14.216  -209.933 51.623  1.00 96.15  ? 154 TYR   U C   1 
ATOM   37012 O  O   . TYR   U  7  163 ? 13.320  -209.835 50.763  1.00 101.27 ? 154 TYR   U O   1 
ATOM   37013 C  CB  . TYR   U  7  163 ? 16.250  -208.469 51.182  1.00 95.86  ? 154 TYR   U CB  1 
ATOM   37014 C  CG  . TYR   U  7  163 ? 15.240  -207.355 51.038  1.00 97.51  ? 154 TYR   U CG  1 
ATOM   37015 C  CD1 . TYR   U  7  163 ? 14.790  -206.947 49.793  1.00 96.59  ? 154 TYR   U CD1 1 
ATOM   37016 C  CD2 . TYR   U  7  163 ? 14.746  -206.690 52.151  1.00 98.03  ? 154 TYR   U CD2 1 
ATOM   37017 C  CE1 . TYR   U  7  163 ? 13.870  -205.919 49.657  1.00 95.68  ? 154 TYR   U CE1 1 
ATOM   37018 C  CE2 . TYR   U  7  163 ? 13.825  -205.661 52.033  1.00 96.90  ? 154 TYR   U CE2 1 
ATOM   37019 C  CZ  . TYR   U  7  163 ? 13.384  -205.274 50.780  1.00 92.96  ? 154 TYR   U CZ  1 
ATOM   37020 O  OH  . TYR   U  7  163 ? 12.472  -204.269 50.645  1.00 96.64  ? 154 TYR   U OH  1 
ATOM   37021 N  N   . VAL   U  7  164 ? 13.993  -210.084 52.929  1.00 97.14  ? 155 VAL   U N   1 
ATOM   37022 C  CA  . VAL   U  7  164 ? 12.635  -210.078 53.546  1.00 99.41  ? 155 VAL   U CA  1 
ATOM   37023 C  C   . VAL   U  7  164 ? 12.764  -209.723 55.031  1.00 102.02 ? 155 VAL   U C   1 
ATOM   37024 O  O   . VAL   U  7  164 ? 13.833  -209.997 55.620  1.00 101.56 ? 155 VAL   U O   1 
ATOM   37025 C  CB  . VAL   U  7  164 ? 11.921  -211.430 53.341  1.00 102.34 ? 155 VAL   U CB  1 
ATOM   37026 C  CG1 . VAL   U  7  164 ? 12.538  -212.542 54.182  1.00 102.83 ? 155 VAL   U CG1 1 
ATOM   37027 C  CG2 . VAL   U  7  164 ? 10.426  -211.320 53.602  1.00 101.01 ? 155 VAL   U CG2 1 
ATOM   37028 N  N   . GLY   U  7  165 ? 11.710  -209.127 55.597  1.00 104.37 ? 156 GLY   U N   1 
ATOM   37029 C  CA  . GLY   U  7  165 ? 11.575  -208.863 57.043  1.00 102.51 ? 156 GLY   U CA  1 
ATOM   37030 C  C   . GLY   U  7  165 ? 11.214  -210.132 57.795  1.00 101.43 ? 156 GLY   U C   1 
ATOM   37031 O  O   . GLY   U  7  165 ? 10.579  -211.009 57.182  1.00 96.58  ? 156 GLY   U O   1 
ATOM   37032 N  N   . TYR   U  7  166 ? 11.599  -210.222 59.073  1.00 103.21 ? 157 TYR   U N   1 
ATOM   37033 C  CA  . TYR   U  7  166 ? 11.427  -211.419 59.940  1.00 103.25 ? 157 TYR   U CA  1 
ATOM   37034 C  C   . TYR   U  7  166 ? 10.828  -211.030 61.296  1.00 106.69 ? 157 TYR   U C   1 
ATOM   37035 O  O   . TYR   U  7  166 ? 11.144  -209.934 61.810  1.00 108.32 ? 157 TYR   U O   1 
ATOM   37036 C  CB  . TYR   U  7  166 ? 12.771  -212.114 60.162  1.00 102.23 ? 157 TYR   U CB  1 
ATOM   37037 C  CG  . TYR   U  7  166 ? 13.320  -212.822 58.951  1.00 101.77 ? 157 TYR   U CG  1 
ATOM   37038 C  CD1 . TYR   U  7  166 ? 14.142  -212.163 58.051  1.00 100.32 ? 157 TYR   U CD1 1 
ATOM   37039 C  CD2 . TYR   U  7  166 ? 13.019  -214.151 58.700  1.00 102.62 ? 157 TYR   U CD2 1 
ATOM   37040 C  CE1 . TYR   U  7  166 ? 14.651  -212.804 56.935  1.00 100.13 ? 157 TYR   U CE1 1 
ATOM   37041 C  CE2 . TYR   U  7  166 ? 13.519  -214.807 57.587  1.00 102.33 ? 157 TYR   U CE2 1 
ATOM   37042 C  CZ  . TYR   U  7  166 ? 14.340  -214.131 56.700  1.00 100.03 ? 157 TYR   U CZ  1 
ATOM   37043 O  OH  . TYR   U  7  166 ? 14.842  -214.760 55.598  1.00 97.61  ? 157 TYR   U OH  1 
ATOM   37044 N  N   . LYS   U  7  167 ? 10.002  -211.923 61.855  1.00 107.57 ? 158 LYS   U N   1 
ATOM   37045 C  CA  . LYS   U  7  167 ? 9.550   -211.898 63.274  1.00 108.59 ? 158 LYS   U CA  1 
ATOM   37046 C  C   . LYS   U  7  167 ? 10.757  -212.231 64.156  1.00 105.32 ? 158 LYS   U C   1 
ATOM   37047 O  O   . LYS   U  7  167 ? 10.951  -211.573 65.200  1.00 101.49 ? 158 LYS   U O   1 
ATOM   37048 C  CB  . LYS   U  7  167 ? 8.426   -212.916 63.503  1.00 114.56 ? 158 LYS   U CB  1 
ATOM   37049 C  CG  . LYS   U  7  167 ? 7.150   -212.680 62.706  1.00 117.44 ? 158 LYS   U CG  1 
ATOM   37050 C  CD  . LYS   U  7  167 ? 6.246   -213.895 62.640  1.00 122.11 ? 158 LYS   U CD  1 
ATOM   37051 C  CE  . LYS   U  7  167 ? 5.026   -213.673 61.773  1.00 123.06 ? 158 LYS   U CE  1 
ATOM   37052 N  NZ  . LYS   U  7  167 ? 4.252   -214.922 61.585  1.00 126.78 ? 158 LYS   U NZ  1 
ATOM   37053 N  N   . ALA   U  7  168 ? 11.510  -213.250 63.735  1.00 103.41 ? 159 ALA   U N   1 
ATOM   37054 C  CA  . ALA   U  7  168 ? 12.840  -213.652 64.247  1.00 101.73 ? 159 ALA   U CA  1 
ATOM   37055 C  C   . ALA   U  7  168 ? 13.546  -214.417 63.125  1.00 98.34  ? 159 ALA   U C   1 
ATOM   37056 O  O   . ALA   U  7  168 ? 12.863  -214.764 62.147  1.00 95.81  ? 159 ALA   U O   1 
ATOM   37057 C  CB  . ALA   U  7  168 ? 12.684  -214.493 65.491  1.00 102.65 ? 159 ALA   U CB  1 
ATOM   37058 N  N   . THR   U  7  169 ? 14.848  -214.675 63.240  1.00 98.43  ? 160 THR   U N   1 
ATOM   37059 C  CA  . THR   U  7  169 ? 15.601  -215.445 62.214  1.00 98.79  ? 160 THR   U CA  1 
ATOM   37060 C  C   . THR   U  7  169 ? 16.877  -216.051 62.802  1.00 100.74 ? 160 THR   U C   1 
ATOM   37061 O  O   . THR   U  7  169 ? 17.341  -215.576 63.859  1.00 102.72 ? 160 THR   U O   1 
ATOM   37062 C  CB  . THR   U  7  169 ? 15.919  -214.576 60.991  1.00 97.20  ? 160 THR   U CB  1 
ATOM   37063 O  OG1 . THR   U  7  169 ? 16.389  -215.424 59.945  1.00 101.16 ? 160 THR   U OG1 1 
ATOM   37064 C  CG2 . THR   U  7  169 ? 16.962  -213.516 61.261  1.00 96.91  ? 160 THR   U CG2 1 
ATOM   37065 N  N   . ALA   U  7  170 ? 17.407  -217.063 62.110  1.00 97.80  ? 161 ALA   U N   1 
ATOM   37066 C  CA  . ALA   U  7  170 ? 18.694  -217.735 62.395  1.00 96.97  ? 161 ALA   U CA  1 
ATOM   37067 C  C   . ALA   U  7  170 ? 19.419  -218.005 61.074  1.00 95.97  ? 161 ALA   U C   1 
ATOM   37068 O  O   . ALA   U  7  170 ? 18.737  -218.164 60.039  1.00 89.99  ? 161 ALA   U O   1 
ATOM   37069 C  CB  . ALA   U  7  170 ? 18.455  -219.009 63.163  1.00 96.75  ? 161 ALA   U CB  1 
ATOM   37070 N  N   . THR   U  7  171 ? 20.753  -218.041 61.119  1.00 97.92  ? 162 THR   U N   1 
ATOM   37071 C  CA  . THR   U  7  171 ? 21.645  -218.289 59.956  1.00 101.84 ? 162 THR   U CA  1 
ATOM   37072 C  C   . THR   U  7  171 ? 22.869  -219.087 60.415  1.00 99.75  ? 162 THR   U C   1 
ATOM   37073 O  O   . THR   U  7  171 ? 23.313  -218.867 61.559  1.00 99.09  ? 162 THR   U O   1 
ATOM   37074 C  CB  . THR   U  7  171 ? 22.107  -216.980 59.302  1.00 104.95 ? 162 THR   U CB  1 
ATOM   37075 O  OG1 . THR   U  7  171 ? 21.021  -216.051 59.260  1.00 109.37 ? 162 THR   U OG1 1 
ATOM   37076 C  CG2 . THR   U  7  171 ? 22.661  -217.211 57.912  1.00 109.19 ? 162 THR   U CG2 1 
ATOM   37077 N  N   . GLY   U  7  172 ? 23.391  -219.962 59.548  1.00 101.44 ? 163 GLY   U N   1 
ATOM   37078 C  CA  . GLY   U  7  172 ? 24.599  -220.769 59.809  1.00 101.80 ? 163 GLY   U CA  1 
ATOM   37079 C  C   . GLY   U  7  172 ? 24.370  -222.256 59.547  1.00 101.24 ? 163 GLY   U C   1 
ATOM   37080 O  O   . GLY   U  7  172 ? 23.296  -222.658 59.102  1.00 99.57  ? 163 GLY   U O   1 
ATOM   37081 N  N   . PRO   U  7  173 ? 25.380  -223.113 59.821  1.00 100.91 ? 164 PRO   U N   1 
ATOM   37082 C  CA  . PRO   U  7  173 ? 25.292  -224.546 59.532  1.00 100.42 ? 164 PRO   U CA  1 
ATOM   37083 C  C   . PRO   U  7  173 ? 24.110  -225.244 60.223  1.00 100.77 ? 164 PRO   U C   1 
ATOM   37084 O  O   . PRO   U  7  173 ? 23.457  -226.045 59.581  1.00 98.37  ? 164 PRO   U O   1 
ATOM   37085 C  CB  . PRO   U  7  173 ? 26.624  -225.112 60.052  1.00 100.53 ? 164 PRO   U CB  1 
ATOM   37086 C  CG  . PRO   U  7  173 ? 27.559  -223.922 60.079  1.00 100.31 ? 164 PRO   U CG  1 
ATOM   37087 C  CD  . PRO   U  7  173 ? 26.675  -222.738 60.407  1.00 100.86 ? 164 PRO   U CD  1 
ATOM   37088 N  N   . LYS   U  7  174 ? 23.867  -224.927 61.499  1.00 102.03 ? 165 LYS   U N   1 
ATOM   37089 C  CA  . LYS   U  7  174 ? 22.778  -225.526 62.319  1.00 107.24 ? 165 LYS   U CA  1 
ATOM   37090 C  C   . LYS   U  7  174 ? 21.635  -224.514 62.469  1.00 107.22 ? 165 LYS   U C   1 
ATOM   37091 O  O   . LYS   U  7  174 ? 21.123  -224.354 63.594  1.00 105.94 ? 165 LYS   U O   1 
ATOM   37092 C  CB  . LYS   U  7  174 ? 23.328  -225.991 63.673  1.00 111.90 ? 165 LYS   U CB  1 
ATOM   37093 C  CG  . LYS   U  7  174 ? 24.179  -227.252 63.609  1.00 117.40 ? 165 LYS   U CG  1 
ATOM   37094 C  CD  . LYS   U  7  174 ? 24.205  -228.050 64.897  1.00 121.99 ? 165 LYS   U CD  1 
ATOM   37095 C  CE  . LYS   U  7  174 ? 25.327  -227.645 65.829  1.00 128.12 ? 165 LYS   U CE  1 
ATOM   37096 N  NZ  . LYS   U  7  174 ? 26.617  -228.251 65.422  1.00 133.01 ? 165 LYS   U NZ  1 
ATOM   37097 N  N   . GLN   U  7  175 ? 21.231  -223.887 61.362  1.00 107.05 ? 166 GLN   U N   1 
ATOM   37098 C  CA  . GLN   U  7  175 ? 20.183  -222.832 61.325  1.00 108.55 ? 166 GLN   U CA  1 
ATOM   37099 C  C   . GLN   U  7  175 ? 18.801  -223.483 61.470  1.00 113.39 ? 166 GLN   U C   1 
ATOM   37100 O  O   . GLN   U  7  175 ? 17.973  -222.922 62.217  1.00 111.82 ? 166 GLN   U O   1 
ATOM   37101 C  CB  . GLN   U  7  175 ? 20.335  -221.989 60.054  1.00 107.89 ? 166 GLN   U CB  1 
ATOM   37102 C  CG  . GLN   U  7  175 ? 19.029  -221.494 59.442  1.00 110.00 ? 166 GLN   U CG  1 
ATOM   37103 C  CD  . GLN   U  7  175 ? 18.671  -222.231 58.176  1.00 113.17 ? 166 GLN   U CD  1 
ATOM   37104 O  OE1 . GLN   U  7  175 ? 17.617  -222.856 58.076  1.00 116.87 ? 166 GLN   U OE1 1 
ATOM   37105 N  NE2 . GLN   U  7  175 ? 19.556  -222.160 57.193  1.00 116.02 ? 166 GLN   U NE2 1 
ATOM   37106 N  N   . GLN   U  7  176 ? 18.569  -224.620 60.803  1.00 112.79 ? 167 GLN   U N   1 
ATOM   37107 C  CA  . GLN   U  7  176 ? 17.244  -225.294 60.750  1.00 116.89 ? 167 GLN   U CA  1 
ATOM   37108 C  C   . GLN   U  7  176 ? 16.789  -225.660 62.169  1.00 117.39 ? 167 GLN   U C   1 
ATOM   37109 O  O   . GLN   U  7  176 ? 15.590  -225.465 62.460  1.00 114.70 ? 167 GLN   U O   1 
ATOM   37110 C  CB  . GLN   U  7  176 ? 17.287  -226.528 59.845  1.00 119.62 ? 167 GLN   U CB  1 
ATOM   37111 C  CG  . GLN   U  7  176 ? 15.916  -227.140 59.582  1.00 125.69 ? 167 GLN   U CG  1 
ATOM   37112 C  CD  . GLN   U  7  176 ? 14.911  -226.116 59.107  1.00 126.64 ? 167 GLN   U CD  1 
ATOM   37113 O  OE1 . GLN   U  7  176 ? 15.102  -225.457 58.089  1.00 132.70 ? 167 GLN   U OE1 1 
ATOM   37114 N  NE2 . GLN   U  7  176 ? 13.828  -225.967 59.852  1.00 130.91 ? 167 GLN   U NE2 1 
ATOM   37115 N  N   . GLU   U  7  177 ? 17.701  -226.163 63.013  1.00 121.49 ? 168 GLU   U N   1 
ATOM   37116 C  CA  . GLU   U  7  177 ? 17.416  -226.546 64.425  1.00 122.38 ? 168 GLU   U CA  1 
ATOM   37117 C  C   . GLU   U  7  177 ? 16.944  -225.311 65.205  1.00 117.09 ? 168 GLU   U C   1 
ATOM   37118 O  O   . GLU   U  7  177 ? 15.940  -225.423 65.937  1.00 119.92 ? 168 GLU   U O   1 
ATOM   37119 C  CB  . GLU   U  7  177 ? 18.644  -227.165 65.101  1.00 127.02 ? 168 GLU   U CB  1 
ATOM   37120 C  CG  . GLU   U  7  177 ? 18.911  -228.608 64.700  1.00 128.54 ? 168 GLU   U CG  1 
ATOM   37121 C  CD  . GLU   U  7  177 ? 19.917  -228.796 63.575  1.00 126.03 ? 168 GLU   U CD  1 
ATOM   37122 O  OE1 . GLU   U  7  177 ? 20.831  -229.629 63.736  1.00 132.37 ? 168 GLU   U OE1 1 
ATOM   37123 O  OE2 . GLU   U  7  177 ? 19.779  -228.118 62.538  1.00 117.48 ? 168 GLU   U OE2 1 
ATOM   37124 N  N   . ILE   U  7  178 ? 17.638  -224.179 65.043  1.00 112.59 ? 169 ILE   U N   1 
ATOM   37125 C  CA  . ILE   U  7  178 ? 17.334  -222.898 65.750  1.00 108.83 ? 169 ILE   U CA  1 
ATOM   37126 C  C   . ILE   U  7  178 ? 15.993  -222.368 65.230  1.00 106.12 ? 169 ILE   U C   1 
ATOM   37127 O  O   . ILE   U  7  178 ? 15.176  -221.923 66.058  1.00 105.54 ? 169 ILE   U O   1 
ATOM   37128 C  CB  . ILE   U  7  178 ? 18.460  -221.856 65.574  1.00 105.72 ? 169 ILE   U CB  1 
ATOM   37129 C  CG1 . ILE   U  7  178 ? 19.844  -222.409 65.928  1.00 105.75 ? 169 ILE   U CG1 1 
ATOM   37130 C  CG2 . ILE   U  7  178 ? 18.153  -220.608 66.387  1.00 105.90 ? 169 ILE   U CG2 1 
ATOM   37131 C  CD1 . ILE   U  7  178 ? 20.991  -221.600 65.363  1.00 101.96 ? 169 ILE   U CD1 1 
ATOM   37132 N  N   . THR   U  7  179 ? 15.784  -222.425 63.911  1.00 105.50 ? 170 THR   U N   1 
ATOM   37133 C  CA  . THR   U  7  179 ? 14.576  -221.903 63.214  1.00 107.13 ? 170 THR   U CA  1 
ATOM   37134 C  C   . THR   U  7  179 ? 13.320  -222.579 63.778  1.00 110.39 ? 170 THR   U C   1 
ATOM   37135 O  O   . THR   U  7  179 ? 12.401  -221.844 64.190  1.00 106.42 ? 170 THR   U O   1 
ATOM   37136 C  CB  . THR   U  7  179 ? 14.666  -222.101 61.695  1.00 106.14 ? 170 THR   U CB  1 
ATOM   37137 O  OG1 . THR   U  7  179 ? 15.902  -221.556 61.230  1.00 103.18 ? 170 THR   U OG1 1 
ATOM   37138 C  CG2 . THR   U  7  179 ? 13.517  -221.454 60.952  1.00 106.09 ? 170 THR   U CG2 1 
ATOM   37139 N  N   . THR   U  7  180 ? 13.284  -223.918 63.789  1.00 113.56 ? 171 THR   U N   1 
ATOM   37140 C  CA  . THR   U  7  180 ? 12.136  -224.726 64.290  1.00 115.56 ? 171 THR   U CA  1 
ATOM   37141 C  C   . THR   U  7  180 ? 11.937  -224.446 65.783  1.00 117.60 ? 171 THR   U C   1 
ATOM   37142 O  O   . THR   U  7  180 ? 10.770  -224.309 66.201  1.00 119.22 ? 171 THR   U O   1 
ATOM   37143 C  CB  . THR   U  7  180 ? 12.312  -226.227 64.021  1.00 115.59 ? 171 THR   U CB  1 
ATOM   37144 O  OG1 . THR   U  7  180 ? 13.694  -226.559 64.143  1.00 118.06 ? 171 THR   U OG1 1 
ATOM   37145 C  CG2 . THR   U  7  180 ? 11.807  -226.637 62.655  1.00 115.93 ? 171 THR   U CG2 1 
ATOM   37146 N  N   . ASN   U  7  181 ? 13.031  -224.356 66.547  1.00 115.52 ? 172 ASN   U N   1 
ATOM   37147 C  CA  . ASN   U  7  181 ? 13.008  -224.031 67.998  1.00 115.04 ? 172 ASN   U CA  1 
ATOM   37148 C  C   . ASN   U  7  181 ? 12.232  -222.725 68.204  1.00 113.86 ? 172 ASN   U C   1 
ATOM   37149 O  O   . ASN   U  7  181 ? 11.380  -222.684 69.115  1.00 113.36 ? 172 ASN   U O   1 
ATOM   37150 C  CB  . ASN   U  7  181 ? 14.418  -223.947 68.590  1.00 116.37 ? 172 ASN   U CB  1 
ATOM   37151 C  CG  . ASN   U  7  181 ? 14.414  -223.589 70.061  1.00 119.00 ? 172 ASN   U CG  1 
ATOM   37152 O  OD1 . ASN   U  7  181 ? 14.216  -222.431 70.422  1.00 121.74 ? 172 ASN   U OD1 1 
ATOM   37153 N  ND2 . ASN   U  7  181 ? 14.630  -224.572 70.921  1.00 121.40 ? 172 ASN   U ND2 1 
ATOM   37154 N  N   . LEU   U  7  182 ? 12.516  -221.710 67.382  1.00 112.14 ? 173 LEU   U N   1 
ATOM   37155 C  CA  . LEU   U  7  182 ? 11.864  -220.373 67.437  1.00 111.51 ? 173 LEU   U CA  1 
ATOM   37156 C  C   . LEU   U  7  182 ? 10.413  -220.478 66.944  1.00 112.82 ? 173 LEU   U C   1 
ATOM   37157 O  O   . LEU   U  7  182 ? 9.535   -219.890 67.606  1.00 112.03 ? 173 LEU   U O   1 
ATOM   37158 C  CB  . LEU   U  7  182 ? 12.673  -219.375 66.601  1.00 109.23 ? 173 LEU   U CB  1 
ATOM   37159 C  CG  . LEU   U  7  182 ? 14.005  -218.933 67.212  1.00 107.63 ? 173 LEU   U CG  1 
ATOM   37160 C  CD1 . LEU   U  7  182 ? 14.917  -218.326 66.157  1.00 104.13 ? 173 LEU   U CD1 1 
ATOM   37161 C  CD2 . LEU   U  7  182 ? 13.784  -217.950 68.353  1.00 107.40 ? 173 LEU   U CD2 1 
ATOM   37162 N  N   . GLU   U  7  183 ? 10.173  -221.193 65.837  1.00 115.38 ? 174 GLU   U N   1 
ATOM   37163 C  CA  . GLU   U  7  183 ? 8.815   -221.454 65.275  1.00 116.68 ? 174 GLU   U CA  1 
ATOM   37164 C  C   . GLU   U  7  183 ? 7.907   -222.044 66.358  1.00 116.62 ? 174 GLU   U C   1 
ATOM   37165 O  O   . GLU   U  7  183 ? 6.744   -221.603 66.467  1.00 117.15 ? 174 GLU   U O   1 
ATOM   37166 C  CB  . GLU   U  7  183 ? 8.856   -222.457 64.121  1.00 117.19 ? 174 GLU   U CB  1 
ATOM   37167 C  CG  . GLU   U  7  183 ? 9.378   -221.895 62.816  1.00 117.43 ? 174 GLU   U CG  1 
ATOM   37168 C  CD  . GLU   U  7  183 ? 9.574   -222.941 61.731  1.00 120.50 ? 174 GLU   U CD  1 
ATOM   37169 O  OE1 . GLU   U  7  183 ? 8.929   -224.008 61.811  1.00 124.94 ? 174 GLU   U OE1 1 
ATOM   37170 O  OE2 . GLU   U  7  183 ? 10.371  -222.685 60.807  1.00 120.52 ? 174 GLU   U OE2 1 
ATOM   37171 N  N   . ASN   U  7  184 ? 8.416   -223.033 67.097  1.00 116.94 ? 175 ASN   U N   1 
ATOM   37172 C  CA  . ASN   U  7  184 ? 7.655   -223.781 68.131  1.00 120.10 ? 175 ASN   U CA  1 
ATOM   37173 C  C   . ASN   U  7  184 ? 7.302   -222.831 69.282  1.00 120.29 ? 175 ASN   U C   1 
ATOM   37174 O  O   . ASN   U  7  184 ? 6.182   -222.952 69.811  1.00 124.79 ? 175 ASN   U O   1 
ATOM   37175 C  CB  . ASN   U  7  184 ? 8.416   -225.023 68.605  1.00 120.23 ? 175 ASN   U CB  1 
ATOM   37176 C  CG  . ASN   U  7  184 ? 8.623   -226.058 67.517  1.00 120.01 ? 175 ASN   U CG  1 
ATOM   37177 O  OD1 . ASN   U  7  184 ? 9.702   -226.637 67.411  1.00 117.62 ? 175 ASN   U OD1 1 
ATOM   37178 N  ND2 . ASN   U  7  184 ? 7.603   -226.311 66.711  1.00 120.56 ? 175 ASN   U ND2 1 
ATOM   37179 N  N   . HIS   U  7  185 ? 8.205   -221.914 69.644  1.00 121.39 ? 176 HIS   U N   1 
ATOM   37180 C  CA  . HIS   U  7  185 ? 7.973   -220.907 70.716  1.00 124.09 ? 176 HIS   U CA  1 
ATOM   37181 C  C   . HIS   U  7  185 ? 6.841   -219.955 70.309  1.00 124.95 ? 176 HIS   U C   1 
ATOM   37182 O  O   . HIS   U  7  185 ? 5.961   -219.697 71.153  1.00 126.55 ? 176 HIS   U O   1 
ATOM   37183 C  CB  . HIS   U  7  185 ? 9.246   -220.121 71.055  1.00 125.10 ? 176 HIS   U CB  1 
ATOM   37184 C  CG  . HIS   U  7  185 ? 8.993   -219.023 72.032  1.00 124.61 ? 176 HIS   U CG  1 
ATOM   37185 N  ND1 . HIS   U  7  185 ? 8.710   -217.732 71.630  1.00 125.74 ? 176 HIS   U ND1 1 
ATOM   37186 C  CD2 . HIS   U  7  185 ? 8.929   -219.023 73.381  1.00 126.21 ? 176 HIS   U CD2 1 
ATOM   37187 C  CE1 . HIS   U  7  185 ? 8.506   -216.978 72.691  1.00 127.47 ? 176 HIS   U CE1 1 
ATOM   37188 N  NE2 . HIS   U  7  185 ? 8.632   -217.748 73.779  1.00 125.27 ? 176 HIS   U NE2 1 
ATOM   37189 N  N   . PHE   U  7  186 ? 6.872   -219.447 69.073  1.00 123.48 ? 177 PHE   U N   1 
ATOM   37190 C  CA  . PHE   U  7  186 ? 5.910   -218.439 68.552  1.00 124.23 ? 177 PHE   U CA  1 
ATOM   37191 C  C   . PHE   U  7  186 ? 4.555   -219.096 68.255  1.00 128.00 ? 177 PHE   U C   1 
ATOM   37192 O  O   . PHE   U  7  186 ? 3.539   -218.372 68.293  1.00 129.97 ? 177 PHE   U O   1 
ATOM   37193 C  CB  . PHE   U  7  186 ? 6.483   -217.710 67.333  1.00 122.11 ? 177 PHE   U CB  1 
ATOM   37194 C  CG  . PHE   U  7  186 ? 7.592   -216.738 67.659  1.00 123.37 ? 177 PHE   U CG  1 
ATOM   37195 C  CD1 . PHE   U  7  186 ? 7.384   -215.696 68.552  1.00 121.19 ? 177 PHE   U CD1 1 
ATOM   37196 C  CD2 . PHE   U  7  186 ? 8.842   -216.857 67.069  1.00 120.85 ? 177 PHE   U CD2 1 
ATOM   37197 C  CE1 . PHE   U  7  186 ? 8.404   -214.808 68.857  1.00 118.25 ? 177 PHE   U CE1 1 
ATOM   37198 C  CE2 . PHE   U  7  186 ? 9.859   -215.963 67.371  1.00 117.21 ? 177 PHE   U CE2 1 
ATOM   37199 C  CZ  . PHE   U  7  186 ? 9.638   -214.943 68.265  1.00 116.64 ? 177 PHE   U CZ  1 
ATOM   37200 N  N   . LYS   U  7  187 ? 4.534   -220.404 67.967  1.00 128.58 ? 178 LYS   U N   1 
ATOM   37201 C  CA  . LYS   U  7  187 ? 3.287   -221.219 67.937  1.00 130.63 ? 178 LYS   U CA  1 
ATOM   37202 C  C   . LYS   U  7  187 ? 2.631   -221.146 69.320  1.00 129.04 ? 178 LYS   U C   1 
ATOM   37203 O  O   . LYS   U  7  187 ? 1.404   -220.946 69.382  1.00 128.93 ? 178 LYS   U O   1 
ATOM   37204 C  CB  . LYS   U  7  187 ? 3.568   -222.681 67.567  1.00 134.15 ? 178 LYS   U CB  1 
ATOM   37205 C  CG  . LYS   U  7  187 ? 3.323   -223.061 66.112  1.00 140.09 ? 178 LYS   U CG  1 
ATOM   37206 C  CD  . LYS   U  7  187 ? 3.030   -224.541 65.935  1.00 142.96 ? 178 LYS   U CD  1 
ATOM   37207 C  CE  . LYS   U  7  187 ? 3.040   -224.997 64.490  1.00 146.24 ? 178 LYS   U CE  1 
ATOM   37208 N  NZ  . LYS   U  7  187 ? 4.421   -225.172 63.980  1.00 148.13 ? 178 LYS   U NZ  1 
ATOM   37209 N  N   . LYS   U  7  188 ? 3.441   -221.282 70.377  1.00 128.86 ? 179 LYS   U N   1 
ATOM   37210 C  CA  . LYS   U  7  188 ? 3.007   -221.362 71.799  1.00 130.21 ? 179 LYS   U CA  1 
ATOM   37211 C  C   . LYS   U  7  188 ? 2.568   -219.973 72.284  1.00 130.56 ? 179 LYS   U C   1 
ATOM   37212 O  O   . LYS   U  7  188 ? 1.437   -219.861 72.796  1.00 134.33 ? 179 LYS   U O   1 
ATOM   37213 C  CB  . LYS   U  7  188 ? 4.146   -221.915 72.663  1.00 127.50 ? 179 LYS   U CB  1 
ATOM   37214 C  CG  . LYS   U  7  188 ? 3.724   -222.815 73.816  1.00 128.20 ? 179 LYS   U CG  1 
ATOM   37215 C  CD  . LYS   U  7  188 ? 4.907   -223.359 74.588  1.00 130.55 ? 179 LYS   U CD  1 
ATOM   37216 C  CE  . LYS   U  7  188 ? 4.615   -224.656 75.311  1.00 134.29 ? 179 LYS   U CE  1 
ATOM   37217 N  NZ  . LYS   U  7  188 ? 5.853   -225.254 75.865  1.00 136.49 ? 179 LYS   U NZ  1 
ATOM   37218 N  N   . SER   U  7  189 ? 3.429   -218.960 72.125  1.00 128.52 ? 180 SER   U N   1 
ATOM   37219 C  CA  . SER   U  7  189 ? 3.229   -217.576 72.637  1.00 127.76 ? 180 SER   U CA  1 
ATOM   37220 C  C   . SER   U  7  189 ? 2.092   -216.874 71.881  1.00 128.12 ? 180 SER   U C   1 
ATOM   37221 O  O   . SER   U  7  189 ? 1.437   -216.008 72.492  1.00 125.47 ? 180 SER   U O   1 
ATOM   37222 C  CB  . SER   U  7  189 ? 4.506   -216.775 72.575  1.00 124.13 ? 180 SER   U CB  1 
ATOM   37223 O  OG  . SER   U  7  189 ? 4.818   -216.406 71.240  1.00 121.60 ? 180 SER   U OG  1 
ATOM   37224 N  N   . LYS   U  7  190 ? 1.884   -217.222 70.605  1.00 131.16 ? 181 LYS   U N   1 
ATOM   37225 C  CA  . LYS   U  7  190 ? 0.763   -216.734 69.752  1.00 134.23 ? 181 LYS   U CA  1 
ATOM   37226 C  C   . LYS   U  7  190 ? 0.994   -215.268 69.345  1.00 134.41 ? 181 LYS   U C   1 
ATOM   37227 O  O   . LYS   U  7  190 ? 0.016   -214.629 68.901  1.00 133.32 ? 181 LYS   U O   1 
ATOM   37228 C  CB  . LYS   U  7  190 ? -0.570  -216.878 70.499  1.00 136.50 ? 181 LYS   U CB  1 
ATOM   37229 C  CG  . LYS   U  7  190 ? -1.792  -217.165 69.633  1.00 137.96 ? 181 LYS   U CG  1 
ATOM   37230 C  CD  . LYS   U  7  190 ? -2.322  -218.577 69.772  1.00 139.98 ? 181 LYS   U CD  1 
ATOM   37231 C  CE  . LYS   U  7  190 ? -1.522  -219.591 68.986  1.00 140.80 ? 181 LYS   U CE  1 
ATOM   37232 N  NZ  . LYS   U  7  190 ? -1.930  -220.978 69.312  1.00 144.29 ? 181 LYS   U NZ  1 
ATOM   37233 N  N   . ILE   U  7  191 ? 2.226   -214.756 69.473  1.00 134.77 ? 182 ILE   U N   1 
ATOM   37234 C  CA  . ILE   U  7  191 ? 2.579   -213.329 69.189  1.00 132.95 ? 182 ILE   U CA  1 
ATOM   37235 C  C   . ILE   U  7  191 ? 3.818   -213.266 68.286  1.00 128.93 ? 182 ILE   U C   1 
ATOM   37236 O  O   . ILE   U  7  191 ? 4.465   -214.310 68.079  1.00 127.39 ? 182 ILE   U O   1 
ATOM   37237 C  CB  . ILE   U  7  191 ? 2.779   -212.526 70.492  1.00 131.73 ? 182 ILE   U CB  1 
ATOM   37238 C  CG1 . ILE   U  7  191 ? 3.692   -213.251 71.486  1.00 131.74 ? 182 ILE   U CG1 1 
ATOM   37239 C  CG2 . ILE   U  7  191 ? 1.434   -212.172 71.110  1.00 131.53 ? 182 ILE   U CG2 1 
ATOM   37240 C  CD1 . ILE   U  7  191 ? 4.195   -212.376 72.611  1.00 132.32 ? 182 ILE   U CD1 1 
ATOM   37241 N  N   . ASP   U  7  192 ? 4.128   -212.065 67.788  1.00 129.01 ? 183 ASP   U N   1 
ATOM   37242 C  CA  . ASP   U  7  192 ? 5.148   -211.803 66.736  1.00 130.25 ? 183 ASP   U CA  1 
ATOM   37243 C  C   . ASP   U  7  192 ? 6.526   -211.514 67.349  1.00 130.12 ? 183 ASP   U C   1 
ATOM   37244 O  O   . ASP   U  7  192 ? 7.488   -211.383 66.564  1.00 132.48 ? 183 ASP   U O   1 
ATOM   37245 C  CB  . ASP   U  7  192 ? 4.717   -210.626 65.853  1.00 133.13 ? 183 ASP   U CB  1 
ATOM   37246 C  CG  . ASP   U  7  192 ? 3.788   -211.001 64.711  1.00 134.27 ? 183 ASP   U CG  1 
ATOM   37247 O  OD1 . ASP   U  7  192 ? 3.468   -212.199 64.576  1.00 141.65 ? 183 ASP   U OD1 1 
ATOM   37248 O  OD2 . ASP   U  7  192 ? 3.398   -210.087 63.958  1.00 135.47 ? 183 ASP   U OD2 1 
ATOM   37249 N  N   . HIS   U  7  193 ? 6.636   -211.420 68.680  1.00 125.54 ? 184 HIS   U N   1 
ATOM   37250 C  CA  . HIS   U  7  193 ? 7.845   -210.898 69.376  1.00 121.63 ? 184 HIS   U CA  1 
ATOM   37251 C  C   . HIS   U  7  193 ? 7.976   -211.488 70.784  1.00 121.99 ? 184 HIS   U C   1 
ATOM   37252 O  O   . HIS   U  7  193 ? 7.067   -212.231 71.204  1.00 130.77 ? 184 HIS   U O   1 
ATOM   37253 C  CB  . HIS   U  7  193 ? 7.781   -209.367 69.434  1.00 120.44 ? 184 HIS   U CB  1 
ATOM   37254 C  CG  . HIS   U  7  193 ? 6.581   -208.852 70.154  1.00 120.65 ? 184 HIS   U CG  1 
ATOM   37255 N  ND1 . HIS   U  7  193 ? 6.621   -208.478 71.485  1.00 120.02 ? 184 HIS   U ND1 1 
ATOM   37256 C  CD2 . HIS   U  7  193 ? 5.308   -208.661 69.745  1.00 119.15 ? 184 HIS   U CD2 1 
ATOM   37257 C  CE1 . HIS   U  7  193 ? 5.427   -208.071 71.861  1.00 119.93 ? 184 HIS   U CE1 1 
ATOM   37258 N  NE2 . HIS   U  7  193 ? 4.602   -208.174 70.812  1.00 118.45 ? 184 HIS   U NE2 1 
ATOM   37259 N  N   . ILE   U  7  194 ? 9.071   -211.151 71.476  1.00 114.63 ? 185 ILE   U N   1 
ATOM   37260 C  CA  . ILE   U  7  194 ? 9.328   -211.517 72.902  1.00 117.00 ? 185 ILE   U CA  1 
ATOM   37261 C  C   . ILE   U  7  194 ? 8.644   -210.470 73.788  1.00 115.28 ? 185 ILE   U C   1 
ATOM   37262 O  O   . ILE   U  7  194 ? 9.140   -209.333 73.842  1.00 114.65 ? 185 ILE   U O   1 
ATOM   37263 C  CB  . ILE   U  7  194 ? 10.839  -211.616 73.207  1.00 117.52 ? 185 ILE   U CB  1 
ATOM   37264 C  CG1 . ILE   U  7  194 ? 11.615  -212.388 72.134  1.00 117.19 ? 185 ILE   U CG1 1 
ATOM   37265 C  CG2 . ILE   U  7  194 ? 11.066  -212.208 74.591  1.00 119.89 ? 185 ILE   U CG2 1 
ATOM   37266 C  CD1 . ILE   U  7  194 ? 10.998  -213.712 71.737  1.00 117.85 ? 185 ILE   U CD1 1 
ATOM   37267 N  N   . ASN   U  7  195 ? 7.554   -210.847 74.463  1.00 118.20 ? 186 ASN   U N   1 
ATOM   37268 C  CA  . ASN   U  7  195 ? 6.738   -209.932 75.306  1.00 120.82 ? 186 ASN   U CA  1 
ATOM   37269 C  C   . ASN   U  7  195 ? 7.527   -209.598 76.578  1.00 120.26 ? 186 ASN   U C   1 
ATOM   37270 O  O   . ASN   U  7  195 ? 7.168   -210.112 77.655  1.00 120.55 ? 186 ASN   U O   1 
ATOM   37271 C  CB  . ASN   U  7  195 ? 5.362   -210.529 75.619  1.00 120.87 ? 186 ASN   U CB  1 
ATOM   37272 C  CG  . ASN   U  7  195 ? 4.410   -209.533 76.248  1.00 120.27 ? 186 ASN   U CG  1 
ATOM   37273 O  OD1 . ASN   U  7  195 ? 3.853   -209.790 77.312  1.00 120.20 ? 186 ASN   U OD1 1 
ATOM   37274 N  ND2 . ASN   U  7  195 ? 4.213   -208.395 75.602  1.00 118.85 ? 186 ASN   U ND2 1 
ATOM   37275 N  N   . GLU   U  7  196 ? 8.562   -208.764 76.447  1.00 123.74 ? 187 GLU   U N   1 
ATOM   37276 C  CA  . GLU   U  7  196 ? 9.497   -208.417 77.549  1.00 131.08 ? 187 GLU   U CA  1 
ATOM   37277 C  C   . GLU   U  7  196 ? 9.787   -206.911 77.531  1.00 134.76 ? 187 GLU   U C   1 
ATOM   37278 O  O   . GLU   U  7  196 ? 9.891   -206.333 76.428  1.00 137.42 ? 187 GLU   U O   1 
ATOM   37279 C  CB  . GLU   U  7  196 ? 10.780  -209.236 77.414  1.00 129.64 ? 187 GLU   U CB  1 
ATOM   37280 C  CG  . GLU   U  7  196 ? 11.514  -209.421 78.726  1.00 132.22 ? 187 GLU   U CG  1 
ATOM   37281 C  CD  . GLU   U  7  196 ? 10.847  -210.371 79.707  1.00 134.93 ? 187 GLU   U CD  1 
ATOM   37282 O  OE1 . GLU   U  7  196 ? 10.500  -211.499 79.297  1.00 137.18 ? 187 GLU   U OE1 1 
ATOM   37283 O  OE2 . GLU   U  7  196 ? 10.669  -209.980 80.878  1.00 137.16 ? 187 GLU   U OE2 1 
ATOM   37284 N  N   . GLU   U  7  197 ? 9.923   -206.313 78.719  1.00 140.04 ? 188 GLU   U N   1 
ATOM   37285 C  CA  . GLU   U  7  197 ? 10.116  -204.852 78.918  1.00 137.41 ? 188 GLU   U CA  1 
ATOM   37286 C  C   . GLU   U  7  197 ? 11.574  -204.485 78.624  1.00 130.43 ? 188 GLU   U C   1 
ATOM   37287 O  O   . GLU   U  7  197 ? 11.802  -203.644 77.735  1.00 131.77 ? 188 GLU   U O   1 
ATOM   37288 C  CB  . GLU   U  7  197 ? 9.748   -204.454 80.349  1.00 145.43 ? 188 GLU   U CB  1 
ATOM   37289 C  CG  . GLU   U  7  197 ? 8.300   -204.731 80.710  1.00 152.48 ? 188 GLU   U CG  1 
ATOM   37290 C  CD  . GLU   U  7  197 ? 7.316   -203.677 80.236  1.00 158.30 ? 188 GLU   U CD  1 
ATOM   37291 O  OE1 . GLU   U  7  197 ? 6.411   -203.330 81.018  1.00 173.08 ? 188 GLU   U OE1 1 
ATOM   37292 O  OE2 . GLU   U  7  197 ? 7.453   -203.209 79.088  1.00 164.19 ? 188 GLU   U OE2 1 
ATOM   37293 N  N   . SER   U  7  198 ? 12.513  -205.095 79.353  1.00 123.46 ? 189 SER   U N   1 
ATOM   37294 C  CA  . SER   U  7  198 ? 13.967  -204.796 79.289  1.00 117.86 ? 189 SER   U CA  1 
ATOM   37295 C  C   . SER   U  7  198 ? 14.606  -205.580 78.139  1.00 110.53 ? 189 SER   U C   1 
ATOM   37296 O  O   . SER   U  7  198 ? 14.140  -206.697 77.865  1.00 107.91 ? 189 SER   U O   1 
ATOM   37297 C  CB  . SER   U  7  198 ? 14.640  -205.094 80.607  1.00 116.10 ? 189 SER   U CB  1 
ATOM   37298 O  OG  . SER   U  7  198 ? 14.733  -206.493 80.832  1.00 113.32 ? 189 SER   U OG  1 
ATOM   37299 N  N   . TRP   U  7  199 ? 15.619  -205.001 77.485  1.00 111.13 ? 190 TRP   U N   1 
ATOM   37300 C  CA  . TRP   U  7  199 ? 16.448  -205.683 76.453  1.00 109.79 ? 190 TRP   U CA  1 
ATOM   37301 C  C   . TRP   U  7  199 ? 17.282  -206.786 77.113  1.00 111.69 ? 190 TRP   U C   1 
ATOM   37302 O  O   . TRP   U  7  199 ? 17.538  -207.803 76.438  1.00 114.68 ? 190 TRP   U O   1 
ATOM   37303 C  CB  . TRP   U  7  199 ? 17.329  -204.695 75.668  1.00 108.12 ? 190 TRP   U CB  1 
ATOM   37304 C  CG  . TRP   U  7  199 ? 18.311  -203.905 76.481  1.00 106.58 ? 190 TRP   U CG  1 
ATOM   37305 C  CD1 . TRP   U  7  199 ? 18.144  -202.634 76.946  1.00 107.20 ? 190 TRP   U CD1 1 
ATOM   37306 C  CD2 . TRP   U  7  199 ? 19.629  -204.311 76.897  1.00 108.93 ? 190 TRP   U CD2 1 
ATOM   37307 N  NE1 . TRP   U  7  199 ? 19.254  -202.228 77.635  1.00 106.81 ? 190 TRP   U NE1 1 
ATOM   37308 C  CE2 . TRP   U  7  199 ? 20.183  -203.232 77.621  1.00 107.19 ? 190 TRP   U CE2 1 
ATOM   37309 C  CE3 . TRP   U  7  199 ? 20.390  -205.478 76.746  1.00 111.50 ? 190 TRP   U CE3 1 
ATOM   37310 C  CZ2 . TRP   U  7  199 ? 21.457  -203.287 78.185  1.00 109.58 ? 190 TRP   U CZ2 1 
ATOM   37311 C  CZ3 . TRP   U  7  199 ? 21.649  -205.532 77.306  1.00 112.30 ? 190 TRP   U CZ3 1 
ATOM   37312 C  CH2 . TRP   U  7  199 ? 22.173  -204.450 78.016  1.00 111.65 ? 190 TRP   U CH2 1 
ATOM   37313 N  N   . GLU   U  7  200 ? 17.667  -206.595 78.381  1.00 110.86 ? 191 GLU   U N   1 
ATOM   37314 C  CA  . GLU   U  7  200 ? 18.505  -207.544 79.166  1.00 111.86 ? 191 GLU   U CA  1 
ATOM   37315 C  C   . GLU   U  7  200 ? 17.880  -208.945 79.130  1.00 108.98 ? 191 GLU   U C   1 
ATOM   37316 O  O   . GLU   U  7  200 ? 18.634  -209.911 78.928  1.00 106.28 ? 191 GLU   U O   1 
ATOM   37317 C  CB  . GLU   U  7  200 ? 18.671  -207.073 80.614  1.00 115.74 ? 191 GLU   U CB  1 
ATOM   37318 C  CG  . GLU   U  7  200 ? 19.665  -205.934 80.786  1.00 119.20 ? 191 GLU   U CG  1 
ATOM   37319 C  CD  . GLU   U  7  200 ? 19.074  -204.534 80.735  1.00 118.98 ? 191 GLU   U CD  1 
ATOM   37320 O  OE1 . GLU   U  7  200 ? 19.656  -203.630 81.365  1.00 123.13 ? 191 GLU   U OE1 1 
ATOM   37321 O  OE2 . GLU   U  7  200 ? 18.037  -204.347 80.065  1.00 123.41 ? 191 GLU   U OE2 1 
ATOM   37322 N  N   . LYS   U  7  201 ? 16.558  -209.044 79.309  1.00 109.11 ? 192 LYS   U N   1 
ATOM   37323 C  CA  . LYS   U  7  201 ? 15.814  -210.332 79.353  1.00 108.54 ? 192 LYS   U CA  1 
ATOM   37324 C  C   . LYS   U  7  201 ? 15.578  -210.864 77.931  1.00 107.94 ? 192 LYS   U C   1 
ATOM   37325 O  O   . LYS   U  7  201 ? 15.489  -212.098 77.784  1.00 109.81 ? 192 LYS   U O   1 
ATOM   37326 C  CB  . LYS   U  7  201 ? 14.493  -210.175 80.112  1.00 111.86 ? 192 LYS   U CB  1 
ATOM   37327 C  CG  . LYS   U  7  201 ? 14.624  -209.997 81.620  1.00 115.96 ? 192 LYS   U CG  1 
ATOM   37328 C  CD  . LYS   U  7  201 ? 13.579  -210.750 82.428  1.00 119.00 ? 192 LYS   U CD  1 
ATOM   37329 C  CE  . LYS   U  7  201 ? 14.133  -211.971 83.133  1.00 119.79 ? 192 LYS   U CE  1 
ATOM   37330 N  NZ  . LYS   U  7  201 ? 14.978  -211.594 84.291  1.00 121.91 ? 192 LYS   U NZ  1 
ATOM   37331 N  N   . VAL   U  7  202 ? 15.475  -209.992 76.924  1.00 102.38 ? 193 VAL   U N   1 
ATOM   37332 C  CA  . VAL   U  7  202 ? 15.344  -210.413 75.495  1.00 101.43 ? 193 VAL   U CA  1 
ATOM   37333 C  C   . VAL   U  7  202 ? 16.677  -211.031 75.055  1.00 100.05 ? 193 VAL   U C   1 
ATOM   37334 O  O   . VAL   U  7  202 ? 16.641  -212.004 74.279  1.00 99.93  ? 193 VAL   U O   1 
ATOM   37335 C  CB  . VAL   U  7  202 ? 14.918  -209.262 74.563  1.00 100.31 ? 193 VAL   U CB  1 
ATOM   37336 C  CG1 . VAL   U  7  202 ? 14.770  -209.730 73.121  1.00 99.24  ? 193 VAL   U CG1 1 
ATOM   37337 C  CG2 . VAL   U  7  202 ? 13.629  -208.602 75.026  1.00 101.45 ? 193 VAL   U CG2 1 
ATOM   37338 N  N   . VAL   U  7  203 ? 17.805  -210.489 75.526  1.00 99.04  ? 194 VAL   U N   1 
ATOM   37339 C  CA  . VAL   U  7  203 ? 19.163  -211.068 75.291  1.00 99.67  ? 194 VAL   U CA  1 
ATOM   37340 C  C   . VAL   U  7  203 ? 19.226  -212.445 75.964  1.00 99.98  ? 194 VAL   U C   1 
ATOM   37341 O  O   . VAL   U  7  203 ? 19.791  -213.371 75.353  1.00 99.87  ? 194 VAL   U O   1 
ATOM   37342 C  CB  . VAL   U  7  203 ? 20.292  -210.146 75.795  1.00 99.49  ? 194 VAL   U CB  1 
ATOM   37343 C  CG1 . VAL   U  7  203 ? 21.651  -210.828 75.719  1.00 99.15  ? 194 VAL   U CG1 1 
ATOM   37344 C  CG2 . VAL   U  7  203 ? 20.330  -208.823 75.045  1.00 99.63  ? 194 VAL   U CG2 1 
ATOM   37345 N  N   . GLU   U  7  204 ? 18.678  -212.565 77.178  1.00 102.95 ? 195 GLU   U N   1 
ATOM   37346 C  CA  . GLU   U  7  204 ? 18.651  -213.826 77.972  1.00 105.61 ? 195 GLU   U CA  1 
ATOM   37347 C  C   . GLU   U  7  204 ? 17.821  -214.883 77.234  1.00 104.52 ? 195 GLU   U C   1 
ATOM   37348 O  O   . GLU   U  7  204 ? 18.262  -216.047 77.198  1.00 104.83 ? 195 GLU   U O   1 
ATOM   37349 C  CB  . GLU   U  7  204 ? 18.105  -213.576 79.380  1.00 108.13 ? 195 GLU   U CB  1 
ATOM   37350 C  CG  . GLU   U  7  204 ? 19.101  -212.886 80.295  1.00 109.21 ? 195 GLU   U CG  1 
ATOM   37351 C  CD  . GLU   U  7  204 ? 18.539  -212.328 81.593  1.00 113.43 ? 195 GLU   U CD  1 
ATOM   37352 O  OE1 . GLU   U  7  204 ? 19.157  -211.391 82.148  1.00 111.05 ? 195 GLU   U OE1 1 
ATOM   37353 O  OE2 . GLU   U  7  204 ? 17.493  -212.830 82.050  1.00 117.65 ? 195 GLU   U OE2 1 
ATOM   37354 N  N   . PHE   U  7  205 ? 16.670  -214.492 76.674  1.00 105.39 ? 196 PHE   U N   1 
ATOM   37355 C  CA  . PHE   U  7  205 ? 15.788  -215.365 75.853  1.00 105.47 ? 196 PHE   U CA  1 
ATOM   37356 C  C   . PHE   U  7  205 ? 16.566  -215.889 74.641  1.00 106.06 ? 196 PHE   U C   1 
ATOM   37357 O  O   . PHE   U  7  205 ? 16.513  -217.103 74.379  1.00 106.49 ? 196 PHE   U O   1 
ATOM   37358 C  CB  . PHE   U  7  205 ? 14.534  -214.620 75.388  1.00 105.35 ? 196 PHE   U CB  1 
ATOM   37359 C  CG  . PHE   U  7  205 ? 13.677  -215.408 74.431  1.00 105.35 ? 196 PHE   U CG  1 
ATOM   37360 C  CD1 . PHE   U  7  205 ? 13.969  -215.436 73.075  1.00 104.69 ? 196 PHE   U CD1 1 
ATOM   37361 C  CD2 . PHE   U  7  205 ? 12.590  -216.136 74.888  1.00 107.15 ? 196 PHE   U CD2 1 
ATOM   37362 C  CE1 . PHE   U  7  205 ? 13.188  -216.172 72.196  1.00 106.81 ? 196 PHE   U CE1 1 
ATOM   37363 C  CE2 . PHE   U  7  205 ? 11.807  -216.867 74.008  1.00 108.75 ? 196 PHE   U CE2 1 
ATOM   37364 C  CZ  . PHE   U  7  205 ? 12.108  -216.885 72.664  1.00 108.69 ? 196 PHE   U CZ  1 
ATOM   37365 N  N   . ALA   U  7  206 ? 17.245  -214.991 73.919  1.00 105.38 ? 197 ALA   U N   1 
ATOM   37366 C  CA  . ALA   U  7  206 ? 18.031  -215.292 72.698  1.00 106.14 ? 197 ALA   U CA  1 
ATOM   37367 C  C   . ALA   U  7  206 ? 19.080  -216.368 73.002  1.00 108.32 ? 197 ALA   U C   1 
ATOM   37368 O  O   . ALA   U  7  206 ? 19.176  -217.329 72.214  1.00 109.66 ? 197 ALA   U O   1 
ATOM   37369 C  CB  . ALA   U  7  206 ? 18.674  -214.035 72.163  1.00 104.62 ? 197 ALA   U CB  1 
ATOM   37370 N  N   . ILE   U  7  207 ? 19.825  -216.216 74.103  1.00 108.71 ? 198 ILE   U N   1 
ATOM   37371 C  CA  . ILE   U  7  207 ? 20.923  -217.148 74.510  1.00 110.43 ? 198 ILE   U CA  1 
ATOM   37372 C  C   . ILE   U  7  207 ? 20.307  -218.480 74.962  1.00 111.61 ? 198 ILE   U C   1 
ATOM   37373 O  O   . ILE   U  7  207 ? 20.843  -219.534 74.567  1.00 111.92 ? 198 ILE   U O   1 
ATOM   37374 C  CB  . ILE   U  7  207 ? 21.823  -216.526 75.599  1.00 110.51 ? 198 ILE   U CB  1 
ATOM   37375 C  CG1 . ILE   U  7  207 ? 22.513  -215.255 75.097  1.00 109.12 ? 198 ILE   U CG1 1 
ATOM   37376 C  CG2 . ILE   U  7  207 ? 22.836  -217.544 76.108  1.00 111.59 ? 198 ILE   U CG2 1 
ATOM   37377 C  CD1 . ILE   U  7  207 ? 23.107  -214.403 76.192  1.00 111.61 ? 198 ILE   U CD1 1 
ATOM   37378 N  N   . THR   U  7  208 ? 19.235  -218.429 75.759  1.00 114.62 ? 199 THR   U N   1 
ATOM   37379 C  CA  . THR   U  7  208 ? 18.500  -219.616 76.277  1.00 115.17 ? 199 THR   U CA  1 
ATOM   37380 C  C   . THR   U  7  208 ? 18.069  -220.505 75.104  1.00 115.87 ? 199 THR   U C   1 
ATOM   37381 O  O   . THR   U  7  208 ? 18.361  -221.715 75.149  1.00 116.68 ? 199 THR   U O   1 
ATOM   37382 C  CB  . THR   U  7  208 ? 17.295  -219.205 77.133  1.00 116.59 ? 199 THR   U CB  1 
ATOM   37383 O  OG1 . THR   U  7  208 ? 17.796  -218.612 78.331  1.00 118.56 ? 199 THR   U OG1 1 
ATOM   37384 C  CG2 . THR   U  7  208 ? 16.388  -220.365 77.485  1.00 116.98 ? 199 THR   U CG2 1 
ATOM   37385 N  N   . HIS   U  7  209 ? 17.399  -219.927 74.102  1.00 113.85 ? 200 HIS   U N   1 
ATOM   37386 C  CA  . HIS   U  7  209 ? 16.796  -220.664 72.957  1.00 114.83 ? 200 HIS   U CA  1 
ATOM   37387 C  C   . HIS   U  7  209 ? 17.881  -221.103 71.963  1.00 115.98 ? 200 HIS   U C   1 
ATOM   37388 O  O   . HIS   U  7  209 ? 17.615  -222.056 71.206  1.00 116.39 ? 200 HIS   U O   1 
ATOM   37389 C  CB  . HIS   U  7  209 ? 15.679  -219.838 72.302  1.00 114.56 ? 200 HIS   U CB  1 
ATOM   37390 C  CG  . HIS   U  7  209 ? 14.384  -219.909 73.042  1.00 113.95 ? 200 HIS   U CG  1 
ATOM   37391 N  ND1 . HIS   U  7  209 ? 13.275  -220.548 72.526  1.00 115.91 ? 200 HIS   U ND1 1 
ATOM   37392 C  CD2 . HIS   U  7  209 ? 14.023  -219.448 74.259  1.00 114.28 ? 200 HIS   U CD2 1 
ATOM   37393 C  CE1 . HIS   U  7  209 ? 12.282  -220.464 73.388  1.00 114.83 ? 200 HIS   U CE1 1 
ATOM   37394 N  NE2 . HIS   U  7  209 ? 12.715  -219.797 74.461  1.00 114.27 ? 200 HIS   U NE2 1 
ATOM   37395 N  N   . MET   U  7  210 ? 19.049  -220.451 71.962  1.00 114.87 ? 201 MET   U N   1 
ATOM   37396 C  CA  . MET   U  7  210 ? 20.228  -220.895 71.168  1.00 115.62 ? 201 MET   U CA  1 
ATOM   37397 C  C   . MET   U  7  210 ? 20.858  -222.120 71.846  1.00 116.41 ? 201 MET   U C   1 
ATOM   37398 O  O   . MET   U  7  210 ? 21.220  -223.067 71.122  1.00 116.54 ? 201 MET   U O   1 
ATOM   37399 C  CB  . MET   U  7  210 ? 21.280  -219.790 71.025  1.00 115.55 ? 201 MET   U CB  1 
ATOM   37400 C  CG  . MET   U  7  210 ? 22.578  -220.281 70.400  1.00 120.32 ? 201 MET   U CG  1 
ATOM   37401 S  SD  . MET   U  7  210 ? 23.384  -219.060 69.341  1.00 124.26 ? 201 MET   U SD  1 
ATOM   37402 C  CE  . MET   U  7  210 ? 22.367  -219.196 67.871  1.00 126.43 ? 201 MET   U CE  1 
ATOM   37403 N  N   . ILE   U  7  211 ? 20.987  -222.095 73.177  1.00 115.63 ? 202 ILE   U N   1 
ATOM   37404 C  CA  . ILE   U  7  211 ? 21.541  -223.216 74.000  1.00 117.98 ? 202 ILE   U CA  1 
ATOM   37405 C  C   . ILE   U  7  211 ? 20.710  -224.481 73.749  1.00 115.76 ? 202 ILE   U C   1 
ATOM   37406 O  O   . ILE   U  7  211 ? 21.319  -225.539 73.509  1.00 113.54 ? 202 ILE   U O   1 
ATOM   37407 C  CB  . ILE   U  7  211 ? 21.588  -222.840 75.496  1.00 118.55 ? 202 ILE   U CB  1 
ATOM   37408 C  CG1 . ILE   U  7  211 ? 22.759  -221.901 75.794  1.00 123.31 ? 202 ILE   U CG1 1 
ATOM   37409 C  CG2 . ILE   U  7  211 ? 21.630  -224.079 76.380  1.00 119.19 ? 202 ILE   U CG2 1 
ATOM   37410 C  CD1 . ILE   U  7  211 ? 22.645  -221.164 77.110  1.00 127.44 ? 202 ILE   U CD1 1 
ATOM   37411 N  N   . ASP   U  7  212 ? 19.378  -224.368 73.804  1.00 119.30 ? 203 ASP   U N   1 
ATOM   37412 C  CA  . ASP   U  7  212 ? 18.423  -225.501 73.655  1.00 120.58 ? 203 ASP   U CA  1 
ATOM   37413 C  C   . ASP   U  7  212 ? 18.548  -226.109 72.252  1.00 120.36 ? 203 ASP   U C   1 
ATOM   37414 O  O   . ASP   U  7  212 ? 18.601  -227.352 72.154  1.00 119.75 ? 203 ASP   U O   1 
ATOM   37415 C  CB  . ASP   U  7  212 ? 16.979  -225.061 73.924  1.00 127.51 ? 203 ASP   U CB  1 
ATOM   37416 C  CG  . ASP   U  7  212 ? 16.729  -224.538 75.331  1.00 128.12 ? 203 ASP   U CG  1 
ATOM   37417 O  OD1 . ASP   U  7  212 ? 17.611  -224.716 76.197  1.00 133.81 ? 203 ASP   U OD1 1 
ATOM   37418 O  OD2 . ASP   U  7  212 ? 15.651  -223.952 75.549  1.00 135.27 ? 203 ASP   U OD2 1 
ATOM   37419 N  N   . ALA   U  7  213 ? 18.590  -225.268 71.213  1.00 115.77 ? 204 ALA   U N   1 
ATOM   37420 C  CA  . ALA   U  7  213 ? 18.587  -225.677 69.787  1.00 114.18 ? 204 ALA   U CA  1 
ATOM   37421 C  C   . ALA   U  7  213 ? 19.934  -226.307 69.400  1.00 113.74 ? 204 ALA   U C   1 
ATOM   37422 O  O   . ALA   U  7  213 ? 19.912  -227.354 68.718  1.00 112.15 ? 204 ALA   U O   1 
ATOM   37423 C  CB  . ALA   U  7  213 ? 18.251  -224.499 68.906  1.00 111.95 ? 204 ALA   U CB  1 
ATOM   37424 N  N   . LEU   U  7  214 ? 21.055  -225.698 69.806  1.00 111.50 ? 205 LEU   U N   1 
ATOM   37425 C  CA  . LEU   U  7  214 ? 22.428  -226.184 69.485  1.00 113.24 ? 205 LEU   U CA  1 
ATOM   37426 C  C   . LEU   U  7  214 ? 22.838  -227.305 70.452  1.00 112.11 ? 205 LEU   U C   1 
ATOM   37427 O  O   . LEU   U  7  214 ? 23.683  -228.133 70.059  1.00 114.75 ? 205 LEU   U O   1 
ATOM   37428 C  CB  . LEU   U  7  214 ? 23.428  -225.023 69.552  1.00 112.23 ? 205 LEU   U CB  1 
ATOM   37429 C  CG  . LEU   U  7  214 ? 23.308  -223.947 68.471  1.00 112.20 ? 205 LEU   U CG  1 
ATOM   37430 C  CD1 . LEU   U  7  214 ? 24.500  -223.005 68.530  1.00 111.33 ? 205 LEU   U CD1 1 
ATOM   37431 C  CD2 . LEU   U  7  214 ? 23.193  -224.551 67.078  1.00 114.20 ? 205 LEU   U CD2 1 
ATOM   37432 N  N   . GLY   U  7  215 ? 22.280  -227.318 71.668  1.00 113.72 ? 206 GLY   U N   1 
ATOM   37433 C  CA  . GLY   U  7  215 ? 22.562  -228.329 72.706  1.00 114.39 ? 206 GLY   U CA  1 
ATOM   37434 C  C   . GLY   U  7  215 ? 23.938  -228.155 73.331  1.00 116.20 ? 206 GLY   U C   1 
ATOM   37435 O  O   . GLY   U  7  215 ? 24.468  -229.150 73.861  1.00 113.56 ? 206 GLY   U O   1 
ATOM   37436 N  N   . THR   U  7  216 ? 24.496  -226.940 73.291  1.00 118.16 ? 207 THR   U N   1 
ATOM   37437 C  CA  . THR   U  7  216 ? 25.823  -226.596 73.875  1.00 122.47 ? 207 THR   U CA  1 
ATOM   37438 C  C   . THR   U  7  216 ? 25.667  -225.508 74.943  1.00 125.20 ? 207 THR   U C   1 
ATOM   37439 O  O   . THR   U  7  216 ? 24.713  -224.707 74.856  1.00 125.99 ? 207 THR   U O   1 
ATOM   37440 C  CB  . THR   U  7  216 ? 26.829  -226.141 72.808  1.00 121.06 ? 207 THR   U CB  1 
ATOM   37441 O  OG1 . THR   U  7  216 ? 26.133  -225.414 71.795  1.00 120.40 ? 207 THR   U OG1 1 
ATOM   37442 C  CG2 . THR   U  7  216 ? 27.582  -227.296 72.186  1.00 118.72 ? 207 THR   U CG2 1 
ATOM   37443 N  N   . GLU   U  7  217 ? 26.594  -225.497 75.903  1.00 126.35 ? 208 GLU   U N   1 
ATOM   37444 C  CA  . GLU   U  7  217 ? 26.732  -224.458 76.957  1.00 125.90 ? 208 GLU   U CA  1 
ATOM   37445 C  C   . GLU   U  7  217 ? 27.748  -223.419 76.472  1.00 121.38 ? 208 GLU   U C   1 
ATOM   37446 O  O   . GLU   U  7  217 ? 28.663  -223.807 75.719  1.00 115.66 ? 208 GLU   U O   1 
ATOM   37447 C  CB  . GLU   U  7  217 ? 27.191  -225.098 78.267  1.00 130.14 ? 208 GLU   U CB  1 
ATOM   37448 C  CG  . GLU   U  7  217 ? 26.606  -224.435 79.498  1.00 133.88 ? 208 GLU   U CG  1 
ATOM   37449 C  CD  . GLU   U  7  217 ? 25.225  -224.948 79.867  1.00 134.20 ? 208 GLU   U CD  1 
ATOM   37450 O  OE1 . GLU   U  7  217 ? 25.121  -226.136 80.229  1.00 133.73 ? 208 GLU   U OE1 1 
ATOM   37451 O  OE2 . GLU   U  7  217 ? 24.256  -224.167 79.771  1.00 125.98 ? 208 GLU   U OE2 1 
ATOM   37452 N  N   . PHE   U  7  218 ? 27.594  -222.156 76.881  1.00 118.81 ? 209 PHE   U N   1 
ATOM   37453 C  CA  . PHE   U  7  218 ? 28.458  -221.026 76.447  1.00 117.57 ? 209 PHE   U CA  1 
ATOM   37454 C  C   . PHE   U  7  218 ? 29.113  -220.365 77.662  1.00 116.49 ? 209 PHE   U C   1 
ATOM   37455 O  O   . PHE   U  7  218 ? 28.411  -220.083 78.655  1.00 118.28 ? 209 PHE   U O   1 
ATOM   37456 C  CB  . PHE   U  7  218 ? 27.656  -219.992 75.652  1.00 114.52 ? 209 PHE   U CB  1 
ATOM   37457 C  CG  . PHE   U  7  218 ? 27.047  -220.513 74.376  1.00 116.32 ? 209 PHE   U CG  1 
ATOM   37458 C  CD1 . PHE   U  7  218 ? 27.849  -220.956 73.334  1.00 117.54 ? 209 PHE   U CD1 1 
ATOM   37459 C  CD2 . PHE   U  7  218 ? 25.671  -220.556 74.215  1.00 118.38 ? 209 PHE   U CD2 1 
ATOM   37460 C  CE1 . PHE   U  7  218 ? 27.287  -221.438 72.162  1.00 120.07 ? 209 PHE   U CE1 1 
ATOM   37461 C  CE2 . PHE   U  7  218 ? 25.111  -221.039 73.043  1.00 122.05 ? 209 PHE   U CE2 1 
ATOM   37462 C  CZ  . PHE   U  7  218 ? 25.919  -221.478 72.018  1.00 121.87 ? 209 PHE   U CZ  1 
ATOM   37463 N  N   . SER   U  7  219 ? 30.425  -220.133 77.572  1.00 117.32 ? 210 SER   U N   1 
ATOM   37464 C  CA  . SER   U  7  219 ? 31.182  -219.184 78.429  1.00 119.42 ? 210 SER   U CA  1 
ATOM   37465 C  C   . SER   U  7  219 ? 31.021  -217.776 77.841  1.00 117.17 ? 210 SER   U C   1 
ATOM   37466 O  O   . SER   U  7  219 ? 30.468  -217.657 76.727  1.00 120.64 ? 210 SER   U O   1 
ATOM   37467 C  CB  . SER   U  7  219 ? 32.632  -219.592 78.561  1.00 120.45 ? 210 SER   U CB  1 
ATOM   37468 O  OG  . SER   U  7  219 ? 33.355  -219.330 77.368  1.00 121.21 ? 210 SER   U OG  1 
ATOM   37469 N  N   . LYS   U  7  220 ? 31.480  -216.749 78.560  1.00 114.94 ? 211 LYS   U N   1 
ATOM   37470 C  CA  . LYS   U  7  220 ? 31.331  -215.318 78.173  1.00 112.64 ? 211 LYS   U CA  1 
ATOM   37471 C  C   . LYS   U  7  220 ? 32.061  -215.029 76.853  1.00 110.63 ? 211 LYS   U C   1 
ATOM   37472 O  O   . LYS   U  7  220 ? 31.701  -214.029 76.205  1.00 112.37 ? 211 LYS   U O   1 
ATOM   37473 C  CB  . LYS   U  7  220 ? 31.846  -214.396 79.284  1.00 111.81 ? 211 LYS   U CB  1 
ATOM   37474 C  CG  . LYS   U  7  220 ? 33.312  -214.574 79.664  1.00 111.40 ? 211 LYS   U CG  1 
ATOM   37475 C  CD  . LYS   U  7  220 ? 33.760  -213.681 80.801  1.00 111.83 ? 211 LYS   U CD  1 
ATOM   37476 C  CE  . LYS   U  7  220 ? 35.210  -213.901 81.174  1.00 110.97 ? 211 LYS   U CE  1 
ATOM   37477 N  NZ  . LYS   U  7  220 ? 35.640  -213.001 82.268  1.00 112.11 ? 211 LYS   U NZ  1 
ATOM   37478 N  N   . ASN   U  7  221 ? 33.043  -215.856 76.473  1.00 108.12 ? 212 ASN   U N   1 
ATOM   37479 C  CA  . ASN   U  7  221 ? 33.919  -215.636 75.289  1.00 107.89 ? 212 ASN   U CA  1 
ATOM   37480 C  C   . ASN   U  7  221 ? 33.458  -216.491 74.101  1.00 107.59 ? 212 ASN   U C   1 
ATOM   37481 O  O   . ASN   U  7  221 ? 34.089  -216.381 73.030  1.00 106.36 ? 212 ASN   U O   1 
ATOM   37482 C  CB  . ASN   U  7  221 ? 35.385  -215.929 75.617  1.00 108.67 ? 212 ASN   U CB  1 
ATOM   37483 C  CG  . ASN   U  7  221 ? 35.835  -215.273 76.905  1.00 110.55 ? 212 ASN   U CG  1 
ATOM   37484 O  OD1 . ASN   U  7  221 ? 35.928  -214.050 76.983  1.00 109.82 ? 212 ASN   U OD1 1 
ATOM   37485 N  ND2 . ASN   U  7  221 ? 36.107  -216.074 77.923  1.00 112.21 ? 212 ASN   U ND2 1 
ATOM   37486 N  N   . ASP   U  7  222 ? 32.407  -217.301 74.274  1.00 110.06 ? 213 ASP   U N   1 
ATOM   37487 C  CA  . ASP   U  7  222 ? 31.836  -218.170 73.208  1.00 111.44 ? 213 ASP   U CA  1 
ATOM   37488 C  C   . ASP   U  7  222 ? 30.731  -217.422 72.453  1.00 108.93 ? 213 ASP   U C   1 
ATOM   37489 O  O   . ASP   U  7  222 ? 30.284  -217.947 71.414  1.00 109.00 ? 213 ASP   U O   1 
ATOM   37490 C  CB  . ASP   U  7  222 ? 31.274  -219.477 73.774  1.00 113.86 ? 213 ASP   U CB  1 
ATOM   37491 C  CG  . ASP   U  7  222 ? 32.291  -220.335 74.506  1.00 115.50 ? 213 ASP   U CG  1 
ATOM   37492 O  OD1 . ASP   U  7  222 ? 33.498  -220.181 74.233  1.00 120.66 ? 213 ASP   U OD1 1 
ATOM   37493 O  OD2 . ASP   U  7  222 ? 31.866  -221.152 75.346  1.00 118.32 ? 213 ASP   U OD2 1 
ATOM   37494 N  N   . LEU   U  7  223 ? 30.303  -216.256 72.949  1.00 109.35 ? 214 LEU   U N   1 
ATOM   37495 C  CA  . LEU   U  7  223 ? 29.156  -215.499 72.381  1.00 109.80 ? 214 LEU   U CA  1 
ATOM   37496 C  C   . LEU   U  7  223 ? 29.562  -214.077 71.994  1.00 108.25 ? 214 LEU   U C   1 
ATOM   37497 O  O   . LEU   U  7  223 ? 30.623  -213.594 72.443  1.00 106.01 ? 214 LEU   U O   1 
ATOM   37498 C  CB  . LEU   U  7  223 ? 28.012  -215.458 73.398  1.00 113.14 ? 214 LEU   U CB  1 
ATOM   37499 C  CG  . LEU   U  7  223 ? 27.091  -216.675 73.423  1.00 117.89 ? 214 LEU   U CG  1 
ATOM   37500 C  CD1 . LEU   U  7  223 ? 25.990  -216.470 74.449  1.00 121.50 ? 214 LEU   U CD1 1 
ATOM   37501 C  CD2 . LEU   U  7  223 ? 26.488  -216.956 72.051  1.00 119.93 ? 214 LEU   U CD2 1 
ATOM   37502 N  N   . GLU   U  7  224 ? 28.689  -213.454 71.201  1.00 105.21 ? 215 GLU   U N   1 
ATOM   37503 C  CA  . GLU   U  7  224 ? 28.774  -212.069 70.675  1.00 104.09 ? 215 GLU   U CA  1 
ATOM   37504 C  C   . GLU   U  7  224 ? 27.343  -211.528 70.609  1.00 99.57  ? 215 GLU   U C   1 
ATOM   37505 O  O   . GLU   U  7  224 ? 26.505  -212.207 69.991  1.00 97.75  ? 215 GLU   U O   1 
ATOM   37506 C  CB  . GLU   U  7  224 ? 29.435  -212.105 69.298  1.00 105.46 ? 215 GLU   U CB  1 
ATOM   37507 C  CG  . GLU   U  7  224 ? 29.845  -210.746 68.778  1.00 109.80 ? 215 GLU   U CG  1 
ATOM   37508 C  CD  . GLU   U  7  224 ? 30.693  -210.792 67.519  1.00 114.11 ? 215 GLU   U CD  1 
ATOM   37509 O  OE1 . GLU   U  7  224 ? 30.718  -211.852 66.856  1.00 111.69 ? 215 GLU   U OE1 1 
ATOM   37510 O  OE2 . GLU   U  7  224 ? 31.324  -209.765 67.205  1.00 118.91 ? 215 GLU   U OE2 1 
ATOM   37511 N  N   . VAL   U  7  225 ? 27.063  -210.385 71.242  1.00 99.85  ? 216 VAL   U N   1 
ATOM   37512 C  CA  . VAL   U  7  225 ? 25.677  -209.840 71.371  1.00 100.37 ? 216 VAL   U CA  1 
ATOM   37513 C  C   . VAL   U  7  225 ? 25.645  -208.394 70.868  1.00 99.68  ? 216 VAL   U C   1 
ATOM   37514 O  O   . VAL   U  7  225 ? 26.447  -207.579 71.357  1.00 103.69 ? 216 VAL   U O   1 
ATOM   37515 C  CB  . VAL   U  7  225 ? 25.154  -209.931 72.817  1.00 100.10 ? 216 VAL   U CB  1 
ATOM   37516 C  CG1 . VAL   U  7  225 ? 23.695  -209.507 72.912  1.00 99.25  ? 216 VAL   U CG1 1 
ATOM   37517 C  CG2 . VAL   U  7  225 ? 25.342  -211.323 73.397  1.00 101.34 ? 216 VAL   U CG2 1 
ATOM   37518 N  N   . GLY   U  7  226 ? 24.741  -208.117 69.924  1.00 101.03 ? 217 GLY   U N   1 
ATOM   37519 C  CA  . GLY   U  7  226 ? 24.327  -206.764 69.510  1.00 100.69 ? 217 GLY   U CA  1 
ATOM   37520 C  C   . GLY   U  7  226 ? 22.916  -206.481 69.993  1.00 102.61 ? 217 GLY   U C   1 
ATOM   37521 O  O   . GLY   U  7  226 ? 22.095  -207.422 69.995  1.00 101.45 ? 217 GLY   U O   1 
ATOM   37522 N  N   . VAL   U  7  227 ? 22.650  -205.245 70.420  1.00 103.11 ? 218 VAL   U N   1 
ATOM   37523 C  CA  . VAL   U  7  227 ? 21.306  -204.789 70.882  1.00 103.85 ? 218 VAL   U CA  1 
ATOM   37524 C  C   . VAL   U  7  227 ? 20.986  -203.453 70.207  1.00 102.22 ? 218 VAL   U C   1 
ATOM   37525 O  O   . VAL   U  7  227 ? 21.780  -202.506 70.372  1.00 102.40 ? 218 VAL   U O   1 
ATOM   37526 C  CB  . VAL   U  7  227 ? 21.240  -204.666 72.416  1.00 104.39 ? 218 VAL   U CB  1 
ATOM   37527 C  CG1 . VAL   U  7  227 ? 19.821  -204.395 72.893  1.00 104.29 ? 218 VAL   U CG1 1 
ATOM   37528 C  CG2 . VAL   U  7  227 ? 21.807  -205.895 73.109  1.00 106.85 ? 218 VAL   U CG2 1 
ATOM   37529 N  N   . ALA   U  7  228 ? 19.867  -203.400 69.476  1.00 101.16 ? 219 ALA   U N   1 
ATOM   37530 C  CA  . ALA   U  7  228 ? 19.278  -202.175 68.888  1.00 99.30  ? 219 ALA   U CA  1 
ATOM   37531 C  C   . ALA   U  7  228 ? 18.123  -201.697 69.774  1.00 100.03 ? 219 ALA   U C   1 
ATOM   37532 O  O   . ALA   U  7  228 ? 17.169  -202.479 69.967  1.00 95.23  ? 219 ALA   U O   1 
ATOM   37533 C  CB  . ALA   U  7  228 ? 18.801  -202.447 67.484  1.00 95.88  ? 219 ALA   U CB  1 
ATOM   37534 N  N   . THR   U  7  229 ? 18.226  -200.472 70.304  1.00 102.87 ? 220 THR   U N   1 
ATOM   37535 C  CA  . THR   U  7  229 ? 17.131  -199.738 70.996  1.00 104.36 ? 220 THR   U CA  1 
ATOM   37536 C  C   . THR   U  7  229 ? 16.819  -198.475 70.193  1.00 105.41 ? 220 THR   U C   1 
ATOM   37537 O  O   . THR   U  7  229 ? 17.504  -198.249 69.177  1.00 106.25 ? 220 THR   U O   1 
ATOM   37538 C  CB  . THR   U  7  229 ? 17.500  -199.408 72.447  1.00 106.52 ? 220 THR   U CB  1 
ATOM   37539 O  OG1 . THR   U  7  229 ? 18.710  -198.651 72.437  1.00 108.20 ? 220 THR   U OG1 1 
ATOM   37540 C  CG2 . THR   U  7  229 ? 17.667  -200.645 73.301  1.00 108.03 ? 220 THR   U CG2 1 
ATOM   37541 N  N   . LYS   U  7  230 ? 15.829  -197.691 70.627  1.00 111.38 ? 221 LYS   U N   1 
ATOM   37542 C  CA  . LYS   U  7  230 ? 15.484  -196.390 69.994  1.00 115.31 ? 221 LYS   U CA  1 
ATOM   37543 C  C   . LYS   U  7  230 ? 16.704  -195.462 70.065  1.00 115.99 ? 221 LYS   U C   1 
ATOM   37544 O  O   . LYS   U  7  230 ? 17.185  -195.197 71.184  1.00 114.17 ? 221 LYS   U O   1 
ATOM   37545 C  CB  . LYS   U  7  230 ? 14.271  -195.737 70.663  1.00 117.58 ? 221 LYS   U CB  1 
ATOM   37546 C  CG  . LYS   U  7  230 ? 13.586  -194.683 69.805  1.00 118.07 ? 221 LYS   U CG  1 
ATOM   37547 C  CD  . LYS   U  7  230 ? 12.829  -193.629 70.580  1.00 124.37 ? 221 LYS   U CD  1 
ATOM   37548 C  CE  . LYS   U  7  230 ? 12.389  -192.482 69.692  1.00 126.65 ? 221 LYS   U CE  1 
ATOM   37549 N  NZ  . LYS   U  7  230 ? 11.713  -191.408 70.457  1.00 129.13 ? 221 LYS   U NZ  1 
ATOM   37550 N  N   . ASP   U  7  231 ? 17.197  -195.023 68.902  1.00 120.64 ? 222 ASP   U N   1 
ATOM   37551 C  CA  . ASP   U  7  231 ? 18.229  -193.962 68.727  1.00 128.41 ? 222 ASP   U CA  1 
ATOM   37552 C  C   . ASP   U  7  231 ? 19.651  -194.485 68.995  1.00 126.56 ? 222 ASP   U C   1 
ATOM   37553 O  O   . ASP   U  7  231 ? 20.575  -193.645 68.951  1.00 129.01 ? 222 ASP   U O   1 
ATOM   37554 C  CB  . ASP   U  7  231 ? 17.936  -192.730 69.593  1.00 138.54 ? 222 ASP   U CB  1 
ATOM   37555 C  CG  . ASP   U  7  231 ? 16.759  -191.897 69.112  1.00 143.55 ? 222 ASP   U CG  1 
ATOM   37556 O  OD1 . ASP   U  7  231 ? 16.679  -191.641 67.892  1.00 153.12 ? 222 ASP   U OD1 1 
ATOM   37557 O  OD2 . ASP   U  7  231 ? 15.934  -191.504 69.962  1.00 154.19 ? 222 ASP   U OD2 1 
ATOM   37558 N  N   . LYS   U  7  232 ? 19.855  -195.789 69.232  1.00 120.84 ? 223 LYS   U N   1 
ATOM   37559 C  CA  . LYS   U  7  232 ? 21.227  -196.376 69.240  1.00 116.81 ? 223 LYS   U CA  1 
ATOM   37560 C  C   . LYS   U  7  232 ? 21.212  -197.910 69.159  1.00 111.58 ? 223 LYS   U C   1 
ATOM   37561 O  O   . LYS   U  7  232 ? 20.359  -198.544 69.811  1.00 111.36 ? 223 LYS   U O   1 
ATOM   37562 C  CB  . LYS   U  7  232 ? 22.029  -195.917 70.463  1.00 120.83 ? 223 LYS   U CB  1 
ATOM   37563 C  CG  . LYS   U  7  232 ? 21.466  -196.294 71.827  1.00 123.89 ? 223 LYS   U CG  1 
ATOM   37564 C  CD  . LYS   U  7  232 ? 22.260  -195.691 72.972  1.00 128.23 ? 223 LYS   U CD  1 
ATOM   37565 C  CE  . LYS   U  7  232 ? 23.664  -196.249 73.096  1.00 129.60 ? 223 LYS   U CE  1 
ATOM   37566 N  NZ  . LYS   U  7  232 ? 24.521  -195.401 73.960  1.00 131.26 ? 223 LYS   U NZ  1 
ATOM   37567 N  N   . PHE   U  7  233 ? 22.153  -198.461 68.381  1.00 104.95 ? 224 PHE   U N   1 
ATOM   37568 C  CA  . PHE   U  7  233 ? 22.566  -199.888 68.367  1.00 101.49 ? 224 PHE   U CA  1 
ATOM   37569 C  C   . PHE   U  7  233 ? 23.970  -200.005 68.971  1.00 100.38 ? 224 PHE   U C   1 
ATOM   37570 O  O   . PHE   U  7  233 ? 24.872  -199.270 68.518  1.00 96.88  ? 224 PHE   U O   1 
ATOM   37571 C  CB  . PHE   U  7  233 ? 22.578  -200.452 66.944  1.00 99.71  ? 224 PHE   U CB  1 
ATOM   37572 C  CG  . PHE   U  7  233 ? 23.277  -201.784 66.821  1.00 99.00  ? 224 PHE   U CG  1 
ATOM   37573 C  CD1 . PHE   U  7  233 ? 22.585  -202.967 67.028  1.00 97.51  ? 224 PHE   U CD1 1 
ATOM   37574 C  CD2 . PHE   U  7  233 ? 24.631  -201.855 66.524  1.00 96.92  ? 224 PHE   U CD2 1 
ATOM   37575 C  CE1 . PHE   U  7  233 ? 23.227  -204.191 66.925  1.00 98.44  ? 224 PHE   U CE1 1 
ATOM   37576 C  CE2 . PHE   U  7  233 ? 25.273  -203.079 66.423  1.00 97.94  ? 224 PHE   U CE2 1 
ATOM   37577 C  CZ  . PHE   U  7  233 ? 24.570  -204.245 66.625  1.00 99.51  ? 224 PHE   U CZ  1 
ATOM   37578 N  N   . PHE   U  7  234 ? 24.151  -200.921 69.931  1.00 100.59 ? 225 PHE   U N   1 
ATOM   37579 C  CA  . PHE   U  7  234 ? 25.429  -201.167 70.653  1.00 100.01 ? 225 PHE   U CA  1 
ATOM   37580 C  C   . PHE   U  7  234 ? 25.682  -202.674 70.784  1.00 99.51  ? 225 PHE   U C   1 
ATOM   37581 O  O   . PHE   U  7  234 ? 24.706  -203.454 70.825  1.00 97.65  ? 225 PHE   U O   1 
ATOM   37582 C  CB  . PHE   U  7  234 ? 25.405  -200.509 72.036  1.00 97.07  ? 225 PHE   U CB  1 
ATOM   37583 C  CG  . PHE   U  7  234 ? 24.242  -200.908 72.910  1.00 95.72  ? 225 PHE   U CG  1 
ATOM   37584 C  CD1 . PHE   U  7  234 ? 23.026  -200.249 72.815  1.00 96.23  ? 225 PHE   U CD1 1 
ATOM   37585 C  CD2 . PHE   U  7  234 ? 24.360  -201.940 73.826  1.00 96.64  ? 225 PHE   U CD2 1 
ATOM   37586 C  CE1 . PHE   U  7  234 ? 21.955  -200.613 73.616  1.00 96.76  ? 225 PHE   U CE1 1 
ATOM   37587 C  CE2 . PHE   U  7  234 ? 23.287  -202.305 74.627  1.00 97.35  ? 225 PHE   U CE2 1 
ATOM   37588 C  CZ  . PHE   U  7  234 ? 22.087  -201.640 74.522  1.00 96.43  ? 225 PHE   U CZ  1 
ATOM   37589 N  N   . THR   U  7  235 ? 26.964  -203.055 70.852  1.00 100.96 ? 226 THR   U N   1 
ATOM   37590 C  CA  . THR   U  7  235 ? 27.441  -204.435 71.145  1.00 98.01  ? 226 THR   U CA  1 
ATOM   37591 C  C   . THR   U  7  235 ? 27.769  -204.534 72.639  1.00 101.31 ? 226 THR   U C   1 
ATOM   37592 O  O   . THR   U  7  235 ? 28.124  -203.499 73.230  1.00 100.91 ? 226 THR   U O   1 
ATOM   37593 C  CB  . THR   U  7  235 ? 28.655  -204.822 70.289  1.00 97.12  ? 226 THR   U CB  1 
ATOM   37594 O  OG1 . THR   U  7  235 ? 29.756  -203.986 70.641  1.00 101.81 ? 226 THR   U OG1 1 
ATOM   37595 C  CG2 . THR   U  7  235 ? 28.398  -204.719 68.801  1.00 95.70  ? 226 THR   U CG2 1 
ATOM   37596 N  N   . LEU   U  7  236 ? 27.652  -205.733 73.218  1.00 100.66 ? 227 LEU   U N   1 
ATOM   37597 C  CA  . LEU   U  7  236 ? 27.925  -206.008 74.655  1.00 101.63 ? 227 LEU   U CA  1 
ATOM   37598 C  C   . LEU   U  7  236 ? 29.383  -206.441 74.827  1.00 100.15 ? 227 LEU   U C   1 
ATOM   37599 O  O   . LEU   U  7  236 ? 29.911  -207.124 73.933  1.00 98.26  ? 227 LEU   U O   1 
ATOM   37600 C  CB  . LEU   U  7  236 ? 26.986  -207.109 75.160  1.00 102.45 ? 227 LEU   U CB  1 
ATOM   37601 C  CG  . LEU   U  7  236 ? 25.490  -206.798 75.143  1.00 103.82 ? 227 LEU   U CG  1 
ATOM   37602 C  CD1 . LEU   U  7  236 ? 24.716  -207.890 75.863  1.00 104.42 ? 227 LEU   U CD1 1 
ATOM   37603 C  CD2 . LEU   U  7  236 ? 25.185  -205.443 75.766  1.00 106.88 ? 227 LEU   U CD2 1 
ATOM   37604 N  N   . SER   U  7  237 ? 29.991  -206.072 75.956  1.00 101.14 ? 228 SER   U N   1 
ATOM   37605 C  CA  . SER   U  7  237 ? 31.333  -206.539 76.388  1.00 105.27 ? 228 SER   U CA  1 
ATOM   37606 C  C   . SER   U  7  237 ? 31.215  -207.979 76.895  1.00 107.30 ? 228 SER   U C   1 
ATOM   37607 O  O   . SER   U  7  237 ? 30.074  -208.453 77.070  1.00 112.17 ? 228 SER   U O   1 
ATOM   37608 C  CB  . SER   U  7  237 ? 31.908  -205.641 77.450  1.00 105.54 ? 228 SER   U CB  1 
ATOM   37609 O  OG  . SER   U  7  237 ? 31.190  -205.776 78.668  1.00 105.37 ? 228 SER   U OG  1 
ATOM   37610 N  N   . ALA   U  7  238 ? 32.350  -208.638 77.137  1.00 107.54 ? 229 ALA   U N   1 
ATOM   37611 C  CA  . ALA   U  7  238 ? 32.418  -210.003 77.709  1.00 109.04 ? 229 ALA   U CA  1 
ATOM   37612 C  C   . ALA   U  7  238 ? 31.708  -210.012 79.069  1.00 109.48 ? 229 ALA   U C   1 
ATOM   37613 O  O   . ALA   U  7  238 ? 30.991  -210.988 79.349  1.00 113.16 ? 229 ALA   U O   1 
ATOM   37614 C  CB  . ALA   U  7  238 ? 33.853  -210.452 77.826  1.00 106.01 ? 229 ALA   U CB  1 
ATOM   37615 N  N   . GLU   U  7  239 ? 31.878  -208.948 79.862  1.00 111.04 ? 230 GLU   U N   1 
ATOM   37616 C  CA  . GLU   U  7  239 ? 31.319  -208.834 81.238  1.00 114.19 ? 230 GLU   U CA  1 
ATOM   37617 C  C   . GLU   U  7  239 ? 29.815  -208.540 81.184  1.00 107.79 ? 230 GLU   U C   1 
ATOM   37618 O  O   . GLU   U  7  239 ? 29.112  -208.956 82.123  1.00 106.80 ? 230 GLU   U O   1 
ATOM   37619 C  CB  . GLU   U  7  239 ? 32.068  -207.776 82.051  1.00 118.96 ? 230 GLU   U CB  1 
ATOM   37620 C  CG  . GLU   U  7  239 ? 33.166  -208.363 82.917  1.00 127.46 ? 230 GLU   U CG  1 
ATOM   37621 C  CD  . GLU   U  7  239 ? 34.162  -209.223 82.158  1.00 134.35 ? 230 GLU   U CD  1 
ATOM   37622 O  OE1 . GLU   U  7  239 ? 34.739  -208.720 81.171  1.00 143.62 ? 230 GLU   U OE1 1 
ATOM   37623 O  OE2 . GLU   U  7  239 ? 34.340  -210.400 82.542  1.00 140.08 ? 230 GLU   U OE2 1 
ATOM   37624 N  N   . ASN   U  7  240 ? 29.339  -207.846 80.147  1.00 107.66 ? 231 ASN   U N   1 
ATOM   37625 C  CA  . ASN   U  7  240 ? 27.887  -207.603 79.923  1.00 110.15 ? 231 ASN   U CA  1 
ATOM   37626 C  C   . ASN   U  7  240 ? 27.201  -208.941 79.631  1.00 107.87 ? 231 ASN   U C   1 
ATOM   37627 O  O   . ASN   U  7  240 ? 26.088  -209.157 80.152  1.00 101.91 ? 231 ASN   U O   1 
ATOM   37628 C  CB  . ASN   U  7  240 ? 27.629  -206.611 78.785  1.00 112.15 ? 231 ASN   U CB  1 
ATOM   37629 C  CG  . ASN   U  7  240 ? 28.101  -205.202 79.081  1.00 114.30 ? 231 ASN   U CG  1 
ATOM   37630 O  OD1 . ASN   U  7  240 ? 28.740  -204.571 78.240  1.00 116.65 ? 231 ASN   U OD1 1 
ATOM   37631 N  ND2 . ASN   U  7  240 ? 27.785  -204.691 80.259  1.00 118.58 ? 231 ASN   U ND2 1 
ATOM   37632 N  N   . ILE   U  7  241 ? 27.847  -209.794 78.828  1.00 107.80 ? 232 ILE   U N   1 
ATOM   37633 C  CA  . ILE   U  7  241 ? 27.357  -211.159 78.461  1.00 109.51 ? 232 ILE   U CA  1 
ATOM   37634 C  C   . ILE   U  7  241 ? 27.460  -212.070 79.692  1.00 111.99 ? 232 ILE   U C   1 
ATOM   37635 O  O   . ILE   U  7  241 ? 26.517  -212.853 79.920  1.00 110.09 ? 232 ILE   U O   1 
ATOM   37636 C  CB  . ILE   U  7  241 ? 28.129  -211.727 77.248  1.00 109.43 ? 232 ILE   U CB  1 
ATOM   37637 C  CG1 . ILE   U  7  241 ? 27.909  -210.884 75.987  1.00 106.47 ? 232 ILE   U CG1 1 
ATOM   37638 C  CG2 . ILE   U  7  241 ? 27.764  -213.188 77.012  1.00 109.90 ? 232 ILE   U CG2 1 
ATOM   37639 C  CD1 . ILE   U  7  241 ? 28.871  -211.187 74.859  1.00 104.16 ? 232 ILE   U CD1 1 
ATOM   37640 N  N   . GLU   U  7  242 ? 28.562  -211.973 80.446  1.00 113.31 ? 233 GLU   U N   1 
ATOM   37641 C  CA  . GLU   U  7  242 ? 28.823  -212.776 81.674  1.00 115.89 ? 233 GLU   U CA  1 
ATOM   37642 C  C   . GLU   U  7  242 ? 27.731  -212.490 82.712  1.00 114.60 ? 233 GLU   U C   1 
ATOM   37643 O  O   . GLU   U  7  242 ? 27.231  -213.450 83.322  1.00 116.15 ? 233 GLU   U O   1 
ATOM   37644 C  CB  . GLU   U  7  242 ? 30.210  -212.460 82.238  1.00 117.91 ? 233 GLU   U CB  1 
ATOM   37645 C  CG  . GLU   U  7  242 ? 30.516  -213.159 83.553  1.00 122.57 ? 233 GLU   U CG  1 
ATOM   37646 C  CD  . GLU   U  7  242 ? 30.415  -214.674 83.521  1.00 126.46 ? 233 GLU   U CD  1 
ATOM   37647 O  OE1 . GLU   U  7  242 ? 29.867  -215.246 84.484  1.00 130.16 ? 233 GLU   U OE1 1 
ATOM   37648 O  OE2 . GLU   U  7  242 ? 30.890  -215.276 82.538  1.00 127.58 ? 233 GLU   U OE2 1 
ATOM   37649 N  N   . GLU   U  7  243 ? 27.392  -211.213 82.904  1.00 116.21 ? 234 GLU   U N   1 
ATOM   37650 C  CA  . GLU   U  7  243 ? 26.280  -210.753 83.780  1.00 120.86 ? 234 GLU   U CA  1 
ATOM   37651 C  C   . GLU   U  7  243 ? 24.982  -211.440 83.333  1.00 118.40 ? 234 GLU   U C   1 
ATOM   37652 O  O   . GLU   U  7  243 ? 24.193  -211.851 84.207  1.00 113.70 ? 234 GLU   U O   1 
ATOM   37653 C  CB  . GLU   U  7  243 ? 26.168  -209.227 83.712  1.00 121.71 ? 234 GLU   U CB  1 
ATOM   37654 C  CG  . GLU   U  7  243 ? 25.322  -208.617 84.815  1.00 125.71 ? 234 GLU   U CG  1 
ATOM   37655 C  CD  . GLU   U  7  243 ? 25.170  -207.107 84.734  1.00 127.24 ? 234 GLU   U CD  1 
ATOM   37656 O  OE1 . GLU   U  7  243 ? 24.127  -206.598 85.185  1.00 131.64 ? 234 GLU   U OE1 1 
ATOM   37657 O  OE2 . GLU   U  7  243 ? 26.096  -206.441 84.223  1.00 128.32 ? 234 GLU   U OE2 1 
ATOM   37658 N  N   . ARG   U  7  244 ? 24.797  -211.574 82.015  1.00 120.48 ? 235 ARG   U N   1 
ATOM   37659 C  CA  . ARG   U  7  244 ? 23.587  -212.148 81.362  1.00 121.43 ? 235 ARG   U CA  1 
ATOM   37660 C  C   . ARG   U  7  244 ? 23.562  -213.672 81.557  1.00 120.72 ? 235 ARG   U C   1 
ATOM   37661 O  O   . ARG   U  7  244 ? 22.474  -214.214 81.840  1.00 127.44 ? 235 ARG   U O   1 
ATOM   37662 C  CB  . ARG   U  7  244 ? 23.576  -211.784 79.873  1.00 119.58 ? 235 ARG   U CB  1 
ATOM   37663 C  CG  . ARG   U  7  244 ? 22.209  -211.397 79.330  1.00 117.48 ? 235 ARG   U CG  1 
ATOM   37664 C  CD  . ARG   U  7  244 ? 21.880  -209.925 79.501  1.00 118.48 ? 235 ARG   U CD  1 
ATOM   37665 N  NE  . ARG   U  7  244 ? 21.181  -209.649 80.752  1.00 117.75 ? 235 ARG   U NE  1 
ATOM   37666 C  CZ  . ARG   U  7  244 ? 21.736  -209.177 81.869  1.00 116.53 ? 235 ARG   U CZ  1 
ATOM   37667 N  NH1 . ARG   U  7  244 ? 23.033  -208.916 81.929  1.00 113.18 ? 235 ARG   U NH1 1 
ATOM   37668 N  NH2 . ARG   U  7  244 ? 20.981  -208.969 82.934  1.00 118.75 ? 235 ARG   U NH2 1 
ATOM   37669 N  N   . LEU   U  7  245 ? 24.713  -214.334 81.392  1.00 115.78 ? 236 LEU   U N   1 
ATOM   37670 C  CA  . LEU   U  7  245 ? 24.882  -215.806 81.560  1.00 114.44 ? 236 LEU   U CA  1 
ATOM   37671 C  C   . LEU   U  7  245 ? 24.576  -216.204 83.011  1.00 114.75 ? 236 LEU   U C   1 
ATOM   37672 O  O   . LEU   U  7  245 ? 23.932  -217.251 83.210  1.00 112.55 ? 236 LEU   U O   1 
ATOM   37673 C  CB  . LEU   U  7  245 ? 26.312  -216.202 81.163  1.00 112.58 ? 236 LEU   U CB  1 
ATOM   37674 C  CG  . LEU   U  7  245 ? 26.493  -216.899 79.810  1.00 110.17 ? 236 LEU   U CG  1 
ATOM   37675 C  CD1 . LEU   U  7  245 ? 25.459  -216.462 78.780  1.00 109.61 ? 236 LEU   U CD1 1 
ATOM   37676 C  CD2 . LEU   U  7  245 ? 27.899  -216.666 79.274  1.00 110.22 ? 236 LEU   U CD2 1 
ATOM   37677 N  N   . VAL   U  7  246 ? 25.021  -215.400 83.982  1.00 115.82 ? 237 VAL   U N   1 
ATOM   37678 C  CA  . VAL   U  7  246 ? 24.789  -215.626 85.441  1.00 117.35 ? 237 VAL   U CA  1 
ATOM   37679 C  C   . VAL   U  7  246 ? 23.280  -215.603 85.712  1.00 118.46 ? 237 VAL   U C   1 
ATOM   37680 O  O   . VAL   U  7  246 ? 22.807  -216.476 86.461  1.00 119.83 ? 237 VAL   U O   1 
ATOM   37681 C  CB  . VAL   U  7  246 ? 25.539  -214.590 86.304  1.00 118.61 ? 237 VAL   U CB  1 
ATOM   37682 C  CG1 . VAL   U  7  246 ? 25.022  -214.550 87.735  1.00 120.87 ? 237 VAL   U CG1 1 
ATOM   37683 C  CG2 . VAL   U  7  246 ? 27.039  -214.836 86.292  1.00 117.39 ? 237 VAL   U CG2 1 
ATOM   37684 N  N   . ALA   U  7  247 ? 22.562  -214.638 85.128  1.00 121.53 ? 238 ALA   U N   1 
ATOM   37685 C  CA  . ALA   U  7  247 ? 21.105  -214.432 85.310  1.00 124.55 ? 238 ALA   U CA  1 
ATOM   37686 C  C   . ALA   U  7  247 ? 20.338  -215.678 84.848  1.00 125.10 ? 238 ALA   U C   1 
ATOM   37687 O  O   . ALA   U  7  247 ? 19.420  -216.104 85.579  1.00 122.69 ? 238 ALA   U O   1 
ATOM   37688 C  CB  . ALA   U  7  247 ? 20.656  -213.192 84.573  1.00 125.70 ? 238 ALA   U CB  1 
ATOM   37689 N  N   . ILE   U  7  248 ? 20.708  -216.245 83.692  1.00 123.37 ? 239 ILE   U N   1 
ATOM   37690 C  CA  . ILE   U  7  248 ? 20.062  -217.460 83.106  1.00 123.97 ? 239 ILE   U CA  1 
ATOM   37691 C  C   . ILE   U  7  248 ? 20.286  -218.643 84.052  1.00 127.96 ? 239 ILE   U C   1 
ATOM   37692 O  O   . ILE   U  7  248 ? 19.303  -219.347 84.350  1.00 130.40 ? 239 ILE   U O   1 
ATOM   37693 C  CB  . ILE   U  7  248 ? 20.587  -217.761 81.685  1.00 121.20 ? 239 ILE   U CB  1 
ATOM   37694 C  CG1 . ILE   U  7  248 ? 20.153  -216.687 80.683  1.00 120.54 ? 239 ILE   U CG1 1 
ATOM   37695 C  CG2 . ILE   U  7  248 ? 20.155  -219.152 81.235  1.00 119.57 ? 239 ILE   U CG2 1 
ATOM   37696 C  CD1 . ILE   U  7  248 ? 20.889  -216.737 79.362  1.00 118.13 ? 239 ILE   U CD1 1 
ATOM   37697 N  N   . ALA   U  7  249 ? 21.532  -218.842 84.497  1.00 132.66 ? 240 ALA   U N   1 
ATOM   37698 C  CA  . ALA   U  7  249 ? 21.970  -219.972 85.351  1.00 137.83 ? 240 ALA   U CA  1 
ATOM   37699 C  C   . ALA   U  7  249 ? 21.205  -219.968 86.682  1.00 140.81 ? 240 ALA   U C   1 
ATOM   37700 O  O   . ALA   U  7  249 ? 20.860  -221.064 87.155  1.00 147.10 ? 240 ALA   U O   1 
ATOM   37701 C  CB  . ALA   U  7  249 ? 23.461  -219.906 85.575  1.00 138.45 ? 240 ALA   U CB  1 
ATOM   37702 N  N   . GLU   U  7  250 ? 20.935  -218.785 87.249  1.00 147.29 ? 241 GLU   U N   1 
ATOM   37703 C  CA  . GLU   U  7  250 ? 20.245  -218.614 88.559  1.00 151.72 ? 241 GLU   U CA  1 
ATOM   37704 C  C   . GLU   U  7  250 ? 18.720  -218.638 88.364  1.00 150.28 ? 241 GLU   U C   1 
ATOM   37705 O  O   . GLU   U  7  250 ? 18.025  -217.904 89.095  1.00 154.42 ? 241 GLU   U O   1 
ATOM   37706 C  CB  . GLU   U  7  250 ? 20.693  -217.312 89.233  1.00 156.28 ? 241 GLU   U CB  1 
ATOM   37707 C  CG  . GLU   U  7  250 ? 22.113  -217.355 89.772  1.00 158.03 ? 241 GLU   U CG  1 
ATOM   37708 C  CD  . GLU   U  7  250 ? 22.626  -216.039 90.334  1.00 158.83 ? 241 GLU   U CD  1 
ATOM   37709 O  OE1 . GLU   U  7  250 ? 23.851  -215.924 90.540  1.00 154.36 ? 241 GLU   U OE1 1 
ATOM   37710 O  OE2 . GLU   U  7  250 ? 21.801  -215.133 90.569  1.00 159.76 ? 241 GLU   U OE2 1 
ATOM   37711 N  N   . GLN   U  7  251 ? 18.215  -219.453 87.431  1.00 147.46 ? 242 GLN   U N   1 
ATOM   37712 C  CA  . GLN   U  7  251 ? 16.758  -219.632 87.178  1.00 150.04 ? 242 GLN   U CA  1 
ATOM   37713 C  C   . GLN   U  7  251 ? 16.518  -220.974 86.479  1.00 144.27 ? 242 GLN   U C   1 
ATOM   37714 O  O   . GLN   U  7  251 ? 15.828  -221.839 87.013  1.00 141.68 ? 242 GLN   U O   1 
ATOM   37715 C  CB  . GLN   U  7  251 ? 16.214  -218.468 86.344  1.00 152.88 ? 242 GLN   U CB  1 
ATOM   37716 C  CG  . GLN   U  7  251 ? 14.759  -218.630 85.916  1.00 162.18 ? 242 GLN   U CG  1 
ATOM   37717 C  CD  . GLN   U  7  251 ? 13.781  -218.568 87.066  1.00 175.30 ? 242 GLN   U CD  1 
ATOM   37718 O  OE1 . GLN   U  7  251 ? 14.160  -218.486 88.233  1.00 190.01 ? 242 GLN   U OE1 1 
ATOM   37719 N  NE2 . GLN   U  7  251 ? 12.499  -218.599 86.741  1.00 177.41 ? 242 GLN   U NE2 1 
ATOM   37720 N  N   . THR   V  8  1   ? 3.539   -162.405 46.131  1.00 107.81 ? 2   THR   V N   1 
ATOM   37721 C  CA  . THR   V  8  1   ? 3.409   -162.447 47.610  1.00 104.49 ? 2   THR   V CA  1 
ATOM   37722 C  C   . THR   V  8  1   ? 3.160   -163.875 48.104  1.00 105.10 ? 2   THR   V C   1 
ATOM   37723 O  O   . THR   V  8  1   ? 2.015   -164.333 48.030  1.00 109.76 ? 2   THR   V O   1 
ATOM   37724 C  CB  . THR   V  8  1   ? 2.268   -161.535 48.054  1.00 101.78 ? 2   THR   V CB  1 
ATOM   37725 O  OG1 . THR   V  8  1   ? 2.527   -160.310 47.377  1.00 102.92 ? 2   THR   V OG1 1 
ATOM   37726 C  CG2 . THR   V  8  1   ? 2.228   -161.310 49.547  1.00 99.77  ? 2   THR   V CG2 1 
ATOM   37727 N  N   . ILE   V  8  2   ? 4.212   -164.525 48.604  1.00 99.99  ? 3   ILE   V N   1 
ATOM   37728 C  CA  . ILE   V  8  2   ? 4.191   -165.910 49.160  1.00 98.47  ? 3   ILE   V CA  1 
ATOM   37729 C  C   . ILE   V  8  2   ? 4.230   -165.773 50.680  1.00 92.22  ? 3   ILE   V C   1 
ATOM   37730 O  O   . ILE   V  8  2   ? 4.916   -164.879 51.115  1.00 91.14  ? 3   ILE   V O   1 
ATOM   37731 C  CB  . ILE   V  8  2   ? 5.468   -166.624 48.696  1.00 98.64  ? 3   ILE   V CB  1 
ATOM   37732 C  CG1 . ILE   V  8  2   ? 5.451   -166.929 47.202  1.00 100.64 ? 3   ILE   V CG1 1 
ATOM   37733 C  CG2 . ILE   V  8  2   ? 5.730   -167.858 49.531  1.00 100.08 ? 3   ILE   V CG2 1 
ATOM   37734 C  CD1 . ILE   V  8  2   ? 4.104   -166.756 46.577  1.00 104.33 ? 3   ILE   V CD1 1 
ATOM   37735 N  N   . VAL   V  8  3   ? 3.437   -166.553 51.429  1.00 90.46  ? 4   VAL   V N   1 
ATOM   37736 C  CA  . VAL   V  8  3   ? 3.396   -166.568 52.922  1.00 90.68  ? 4   VAL   V CA  1 
ATOM   37737 C  C   . VAL   V  8  3   ? 3.048   -167.977 53.420  1.00 88.73  ? 4   VAL   V C   1 
ATOM   37738 O  O   . VAL   V  8  3   ? 2.261   -168.649 52.749  1.00 84.32  ? 4   VAL   V O   1 
ATOM   37739 C  CB  . VAL   V  8  3   ? 2.370   -165.552 53.453  1.00 91.27  ? 4   VAL   V CB  1 
ATOM   37740 C  CG1 . VAL   V  8  3   ? 1.409   -165.091 52.375  1.00 93.83  ? 4   VAL   V CG1 1 
ATOM   37741 C  CG2 . VAL   V  8  3   ? 1.581   -166.131 54.606  1.00 91.01  ? 4   VAL   V CG2 1 
ATOM   37742 N  N   . GLY   V  8  4   ? 3.614   -168.382 54.564  1.00 88.97  ? 5   GLY   V N   1 
ATOM   37743 C  CA  . GLY   V  8  4   ? 3.367   -169.676 55.223  1.00 90.06  ? 5   GLY   V CA  1 
ATOM   37744 C  C   . GLY   V  8  4   ? 3.173   -169.470 56.713  1.00 90.41  ? 5   GLY   V C   1 
ATOM   37745 O  O   . GLY   V  8  4   ? 3.970   -168.720 57.303  1.00 86.72  ? 5   GLY   V O   1 
ATOM   37746 N  N   . VAL   V  8  5   ? 2.139   -170.084 57.294  1.00 93.31  ? 6   VAL   V N   1 
ATOM   37747 C  CA  . VAL   V  8  5   ? 1.766   -169.927 58.731  1.00 94.57  ? 6   VAL   V CA  1 
ATOM   37748 C  C   . VAL   V  8  5   ? 1.526   -171.314 59.337  1.00 94.35  ? 6   VAL   V C   1 
ATOM   37749 O  O   . VAL   V  8  5   ? 0.803   -172.117 58.722  1.00 92.74  ? 6   VAL   V O   1 
ATOM   37750 C  CB  . VAL   V  8  5   ? 0.535   -169.014 58.893  1.00 96.50  ? 6   VAL   V CB  1 
ATOM   37751 C  CG1 . VAL   V  8  5   ? 0.038   -168.970 60.330  1.00 99.47  ? 6   VAL   V CG1 1 
ATOM   37752 C  CG2 . VAL   V  8  5   ? 0.813   -167.608 58.389  1.00 97.82  ? 6   VAL   V CG2 1 
ATOM   37753 N  N   . LYS   V  8  6   ? 2.106   -171.562 60.513  1.00 95.16  ? 7   LYS   V N   1 
ATOM   37754 C  CA  . LYS   V  8  6   ? 1.947   -172.812 61.301  1.00 98.38  ? 7   LYS   V CA  1 
ATOM   37755 C  C   . LYS   V  8  6   ? 0.792   -172.620 62.289  1.00 101.97 ? 7   LYS   V C   1 
ATOM   37756 O  O   . LYS   V  8  6   ? 0.725   -171.534 62.902  1.00 104.09 ? 7   LYS   V O   1 
ATOM   37757 C  CB  . LYS   V  8  6   ? 3.253   -173.135 62.034  1.00 98.59  ? 7   LYS   V CB  1 
ATOM   37758 C  CG  . LYS   V  8  6   ? 4.320   -173.821 61.191  1.00 98.92  ? 7   LYS   V CG  1 
ATOM   37759 C  CD  . LYS   V  8  6   ? 4.555   -175.265 61.572  1.00 100.82 ? 7   LYS   V CD  1 
ATOM   37760 C  CE  . LYS   V  8  6   ? 5.356   -175.407 62.849  1.00 100.43 ? 7   LYS   V CE  1 
ATOM   37761 N  NZ  . LYS   V  8  6   ? 5.755   -176.811 63.095  1.00 100.75 ? 7   LYS   V NZ  1 
ATOM   37762 N  N   . PHE   V  8  7   ? -0.089  -173.619 62.419  1.00 103.73 ? 8   PHE   V N   1 
ATOM   37763 C  CA  . PHE   V  8  7   ? -1.173  -173.665 63.438  1.00 104.20 ? 8   PHE   V CA  1 
ATOM   37764 C  C   . PHE   V  8  7   ? -0.968  -174.923 64.295  1.00 105.16 ? 8   PHE   V C   1 
ATOM   37765 O  O   . PHE   V  8  7   ? 0.068   -175.585 64.099  1.00 102.61 ? 8   PHE   V O   1 
ATOM   37766 C  CB  . PHE   V  8  7   ? -2.543  -173.503 62.767  1.00 104.41 ? 8   PHE   V CB  1 
ATOM   37767 C  CG  . PHE   V  8  7   ? -3.002  -174.611 61.852  1.00 104.79 ? 8   PHE   V CG  1 
ATOM   37768 C  CD1 . PHE   V  8  7   ? -3.718  -175.686 62.353  1.00 107.56 ? 8   PHE   V CD1 1 
ATOM   37769 C  CD2 . PHE   V  8  7   ? -2.783  -174.547 60.483  1.00 102.88 ? 8   PHE   V CD2 1 
ATOM   37770 C  CE1 . PHE   V  8  7   ? -4.166  -176.694 61.514  1.00 109.27 ? 8   PHE   V CE1 1 
ATOM   37771 C  CE2 . PHE   V  8  7   ? -3.233  -175.555 59.643  1.00 103.56 ? 8   PHE   V CE2 1 
ATOM   37772 C  CZ  . PHE   V  8  7   ? -3.924  -176.626 60.160  1.00 107.23 ? 8   PHE   V CZ  1 
ATOM   37773 N  N   . ASN   V  8  8   ? -1.871  -175.213 65.242  1.00 109.67 ? 9   ASN   V N   1 
ATOM   37774 C  CA  . ASN   V  8  8   ? -1.671  -176.303 66.241  1.00 115.04 ? 9   ASN   V CA  1 
ATOM   37775 C  C   . ASN   V  8  8   ? -1.500  -177.640 65.517  1.00 118.65 ? 9   ASN   V C   1 
ATOM   37776 O  O   . ASN   V  8  8   ? -0.512  -178.345 65.805  1.00 120.27 ? 9   ASN   V O   1 
ATOM   37777 C  CB  . ASN   V  8  8   ? -2.822  -176.523 67.231  1.00 119.41 ? 9   ASN   V CB  1 
ATOM   37778 C  CG  . ASN   V  8  8   ? -3.635  -175.292 67.566  1.00 123.26 ? 9   ASN   V CG  1 
ATOM   37779 O  OD1 . ASN   V  8  8   ? -3.102  -174.306 68.074  1.00 127.79 ? 9   ASN   V OD1 1 
ATOM   37780 N  ND2 . ASN   V  8  8   ? -4.936  -175.364 67.327  1.00 124.36 ? 9   ASN   V ND2 1 
ATOM   37781 N  N   . ASN   V  8  9   ? -2.447  -177.976 64.636  1.00 122.02 ? 10  ASN   V N   1 
ATOM   37782 C  CA  . ASN   V  8  9   ? -2.608  -179.336 64.055  1.00 124.91 ? 10  ASN   V CA  1 
ATOM   37783 C  C   . ASN   V  8  9   ? -2.004  -179.417 62.646  1.00 119.94 ? 10  ASN   V C   1 
ATOM   37784 O  O   . ASN   V  8  9   ? -2.161  -180.480 62.016  1.00 121.40 ? 10  ASN   V O   1 
ATOM   37785 C  CB  . ASN   V  8  9   ? -4.079  -179.760 64.023  1.00 131.49 ? 10  ASN   V CB  1 
ATOM   37786 C  CG  . ASN   V  8  9   ? -4.263  -181.262 64.111  1.00 136.19 ? 10  ASN   V CG  1 
ATOM   37787 O  OD1 . ASN   V  8  9   ? -3.481  -181.953 64.761  1.00 142.87 ? 10  ASN   V OD1 1 
ATOM   37788 N  ND2 . ASN   V  8  9   ? -5.296  -181.779 63.464  1.00 142.19 ? 10  ASN   V ND2 1 
ATOM   37789 N  N   . GLY   V  8  10  ? -1.343  -178.363 62.155  1.00 114.09 ? 11  GLY   V N   1 
ATOM   37790 C  CA  . GLY   V  8  10  ? -0.721  -178.395 60.817  1.00 110.41 ? 11  GLY   V CA  1 
ATOM   37791 C  C   . GLY   V  8  10  ? -0.156  -177.058 60.374  1.00 107.94 ? 11  GLY   V C   1 
ATOM   37792 O  O   . GLY   V  8  10  ? 0.080   -176.186 61.234  1.00 111.61 ? 11  GLY   V O   1 
ATOM   37793 N  N   . VAL   V  8  11  ? 0.053   -176.923 59.062  1.00 100.48 ? 12  VAL   V N   1 
ATOM   37794 C  CA  . VAL   V  8  11  ? 0.636   -175.723 58.394  1.00 95.74  ? 12  VAL   V CA  1 
ATOM   37795 C  C   . VAL   V  8  11  ? -0.284  -175.321 57.236  1.00 96.26  ? 12  VAL   V C   1 
ATOM   37796 O  O   . VAL   V  8  11  ? -0.900  -176.214 56.623  1.00 92.52  ? 12  VAL   V O   1 
ATOM   37797 C  CB  . VAL   V  8  11  ? 2.075   -175.998 57.915  1.00 93.71  ? 12  VAL   V CB  1 
ATOM   37798 C  CG1 . VAL   V  8  11  ? 2.134   -177.131 56.905  1.00 95.26  ? 12  VAL   V CG1 1 
ATOM   37799 C  CG2 . VAL   V  8  11  ? 2.739   -174.755 57.350  1.00 92.37  ? 12  VAL   V CG2 1 
ATOM   37800 N  N   . VAL   V  8  12  ? -0.367  -174.016 56.965  1.00 96.65  ? 13  VAL   V N   1 
ATOM   37801 C  CA  . VAL   V  8  12  ? -1.160  -173.409 55.855  1.00 95.27  ? 13  VAL   V CA  1 
ATOM   37802 C  C   . VAL   V  8  12  ? -0.238  -172.458 55.087  1.00 88.45  ? 13  VAL   V C   1 
ATOM   37803 O  O   . VAL   V  8  12  ? 0.499   -171.697 55.731  1.00 88.23  ? 13  VAL   V O   1 
ATOM   37804 C  CB  . VAL   V  8  12  ? -2.421  -172.685 56.372  1.00 98.00  ? 13  VAL   V CB  1 
ATOM   37805 C  CG1 . VAL   V  8  12  ? -2.124  -171.806 57.577  1.00 97.17  ? 13  VAL   V CG1 1 
ATOM   37806 C  CG2 . VAL   V  8  12  ? -3.105  -171.874 55.279  1.00 98.46  ? 13  VAL   V CG2 1 
ATOM   37807 N  N   . ILE   V  8  13  ? -0.268  -172.530 53.758  1.00 89.60  ? 14  ILE   V N   1 
ATOM   37808 C  CA  . ILE   V  8  13  ? 0.469   -171.605 52.853  1.00 90.88  ? 14  ILE   V CA  1 
ATOM   37809 C  C   . ILE   V  8  13  ? -0.566  -170.924 51.960  1.00 90.98  ? 14  ILE   V C   1 
ATOM   37810 O  O   . ILE   V  8  13  ? -1.615  -171.535 51.677  1.00 88.54  ? 14  ILE   V O   1 
ATOM   37811 C  CB  . ILE   V  8  13  ? 1.554   -172.341 52.040  1.00 92.71  ? 14  ILE   V CB  1 
ATOM   37812 C  CG1 . ILE   V  8  13  ? 0.947   -173.256 50.969  1.00 94.36  ? 14  ILE   V CG1 1 
ATOM   37813 C  CG2 . ILE   V  8  13  ? 2.494   -173.089 52.976  1.00 93.37  ? 14  ILE   V CG2 1 
ATOM   37814 C  CD1 . ILE   V  8  13  ? 1.958   -173.949 50.084  1.00 95.03  ? 14  ILE   V CD1 1 
ATOM   37815 N  N   . ALA   V  8  14  ? -0.280  -169.689 51.566  1.00 91.42  ? 15  ALA   V N   1 
ATOM   37816 C  CA  . ALA   V  8  14  ? -1.107  -168.895 50.636  1.00 93.29  ? 15  ALA   V CA  1 
ATOM   37817 C  C   . ALA   V  8  14  ? -0.186  -168.071 49.734  1.00 91.59  ? 15  ALA   V C   1 
ATOM   37818 O  O   . ALA   V  8  14  ? 0.986   -167.847 50.102  1.00 91.06  ? 15  ALA   V O   1 
ATOM   37819 C  CB  . ALA   V  8  14  ? -2.073  -168.031 51.410  1.00 93.18  ? 15  ALA   V CB  1 
ATOM   37820 N  N   . ALA   V  8  15  ? -0.703  -167.673 48.575  1.00 90.44  ? 16  ALA   V N   1 
ATOM   37821 C  CA  . ALA   V  8  15  ? -0.002  -166.845 47.572  1.00 91.74  ? 16  ALA   V CA  1 
ATOM   37822 C  C   . ALA   V  8  15  ? -1.049  -166.073 46.767  1.00 91.45  ? 16  ALA   V C   1 
ATOM   37823 O  O   . ALA   V  8  15  ? -2.235  -166.453 46.815  1.00 93.75  ? 16  ALA   V O   1 
ATOM   37824 C  CB  . ALA   V  8  15  ? 0.853   -167.723 46.694  1.00 92.22  ? 16  ALA   V CB  1 
ATOM   37825 N  N   . ASP   V  8  16  ? -0.567  -165.094 46.000  1.00 90.57  ? 17  ASP   V N   1 
ATOM   37826 C  CA  . ASP   V  8  16  ? -1.397  -164.239 45.118  1.00 94.25  ? 17  ASP   V CA  1 
ATOM   37827 C  C   . ASP   V  8  16  ? -1.563  -164.935 43.767  1.00 96.34  ? 17  ASP   V C   1 
ATOM   37828 O  O   . ASP   V  8  16  ? -1.023  -166.018 43.573  1.00 100.90 ? 17  ASP   V O   1 
ATOM   37829 C  CB  . ASP   V  8  16  ? -0.794  -162.842 44.977  1.00 94.54  ? 17  ASP   V CB  1 
ATOM   37830 C  CG  . ASP   V  8  16  ? 0.414   -162.809 44.066  1.00 97.47  ? 17  ASP   V CG  1 
ATOM   37831 O  OD1 . ASP   V  8  16  ? 0.261   -163.149 42.892  1.00 95.85  ? 17  ASP   V OD1 1 
ATOM   37832 O  OD2 . ASP   V  8  16  ? 1.494   -162.456 44.539  1.00 99.97  ? 17  ASP   V OD2 1 
ATOM   37833 N  N   . THR   V  8  17  ? -2.203  -164.267 42.825  1.00 94.11  ? 18  THR   V N   1 
ATOM   37834 C  CA  . THR   V  8  17  ? -2.530  -164.891 41.513  1.00 96.04  ? 18  THR   V CA  1 
ATOM   37835 C  C   . THR   V  8  17  ? -1.941  -164.114 40.332  1.00 96.35  ? 18  THR   V C   1 
ATOM   37836 O  O   . THR   V  8  17  ? -2.251  -164.498 39.188  1.00 98.42  ? 18  THR   V O   1 
ATOM   37837 C  CB  . THR   V  8  17  ? -4.047  -165.001 41.329  1.00 98.48  ? 18  THR   V CB  1 
ATOM   37838 O  OG1 . THR   V  8  17  ? -4.637  -164.416 42.485  1.00 97.30  ? 18  THR   V OG1 1 
ATOM   37839 C  CG2 . THR   V  8  17  ? -4.526  -166.427 41.167  1.00 100.98 ? 18  THR   V CG2 1 
ATOM   37840 N  N   . ARG   V  8  18  ? -1.123  -163.087 40.562  1.00 94.93  ? 19  ARG   V N   1 
ATOM   37841 C  CA  . ARG   V  8  18  ? -0.656  -162.246 39.426  1.00 96.05  ? 19  ARG   V CA  1 
ATOM   37842 C  C   . ARG   V  8  18  ? 0.787   -162.543 39.020  1.00 91.02  ? 19  ARG   V C   1 
ATOM   37843 O  O   . ARG   V  8  18  ? 1.643   -162.577 39.892  1.00 92.53  ? 19  ARG   V O   1 
ATOM   37844 C  CB  . ARG   V  8  18  ? -0.790  -160.764 39.789  1.00 96.58  ? 19  ARG   V CB  1 
ATOM   37845 C  CG  . ARG   V  8  18  ? 0.012   -159.826 38.898  1.00 97.97  ? 19  ARG   V CG  1 
ATOM   37846 C  CD  . ARG   V  8  18  ? 0.013   -158.385 39.364  1.00 96.42  ? 19  ARG   V CD  1 
ATOM   37847 N  NE  . ARG   V  8  18  ? -1.339  -157.872 39.501  1.00 97.62  ? 19  ARG   V NE  1 
ATOM   37848 C  CZ  . ARG   V  8  18  ? -1.648  -156.608 39.749  1.00 98.15  ? 19  ARG   V CZ  1 
ATOM   37849 N  NH1 . ARG   V  8  18  ? -0.695  -155.707 39.893  1.00 104.62 ? 19  ARG   V NH1 1 
ATOM   37850 N  NH2 . ARG   V  8  18  ? -2.911  -156.249 39.862  1.00 96.14  ? 19  ARG   V NH2 1 
ATOM   37851 N  N   . SER   V  8  19  ? 1.025   -162.681 37.717  1.00 89.31  ? 20  SER   V N   1 
ATOM   37852 C  CA  . SER   V  8  19  ? 2.372   -162.935 37.148  1.00 88.91  ? 20  SER   V CA  1 
ATOM   37853 C  C   . SER   V  8  19  ? 2.716   -161.749 36.251  1.00 87.21  ? 20  SER   V C   1 
ATOM   37854 O  O   . SER   V  8  19  ? 1.814   -161.284 35.560  1.00 88.46  ? 20  SER   V O   1 
ATOM   37855 C  CB  . SER   V  8  19  ? 2.367   -164.208 36.366  1.00 88.77  ? 20  SER   V CB  1 
ATOM   37856 O  OG  . SER   V  8  19  ? 3.272   -164.139 35.280  1.00 90.95  ? 20  SER   V OG  1 
ATOM   37857 N  N   . THR   V  8  20  ? 3.967   -161.288 36.240  1.00 86.63  ? 21  THR   V N   1 
ATOM   37858 C  CA  . THR   V  8  20  ? 4.277   -160.071 35.450  1.00 87.38  ? 21  THR   V CA  1 
ATOM   37859 C  C   . THR   V  8  20  ? 5.593   -160.174 34.683  1.00 87.07  ? 21  THR   V C   1 
ATOM   37860 O  O   . THR   V  8  20  ? 6.508   -160.812 35.172  1.00 81.95  ? 21  THR   V O   1 
ATOM   37861 C  CB  . THR   V  8  20  ? 4.519   -158.887 36.390  1.00 88.41  ? 21  THR   V CB  1 
ATOM   37862 O  OG1 . THR   V  8  20  ? 5.698   -159.192 37.130  1.00 85.81  ? 21  THR   V OG1 1 
ATOM   37863 C  CG2 . THR   V  8  20  ? 3.386   -158.620 37.354  1.00 88.96  ? 21  THR   V CG2 1 
ATOM   37864 N  N   . GLN   V  8  21  ? 5.661   -159.509 33.530  1.00 92.91  ? 22  GLN   V N   1 
ATOM   37865 C  CA  . GLN   V  8  21  ? 6.889   -159.388 32.703  1.00 97.60  ? 22  GLN   V CA  1 
ATOM   37866 C  C   . GLN   V  8  21  ? 7.186   -157.888 32.632  1.00 93.54  ? 22  GLN   V C   1 
ATOM   37867 O  O   . GLN   V  8  21  ? 6.495   -157.184 31.895  1.00 88.59  ? 22  GLN   V O   1 
ATOM   37868 C  CB  . GLN   V  8  21  ? 6.678   -159.999 31.322  1.00 105.89 ? 22  GLN   V CB  1 
ATOM   37869 C  CG  . GLN   V  8  21  ? 7.983   -160.275 30.593  1.00 109.60 ? 22  GLN   V CG  1 
ATOM   37870 C  CD  . GLN   V  8  21  ? 7.804   -161.297 29.501  1.00 117.56 ? 22  GLN   V CD  1 
ATOM   37871 O  OE1 . GLN   V  8  21  ? 6.728   -161.862 29.332  1.00 120.61 ? 22  GLN   V OE1 1 
ATOM   37872 N  NE2 . GLN   V  8  21  ? 8.865   -161.543 28.751  1.00 120.39 ? 22  GLN   V NE2 1 
ATOM   37873 N  N   . GLY   V  8  22  ? 8.212   -157.440 33.349  1.00 94.22  ? 23  GLY   V N   1 
ATOM   37874 C  CA  . GLY   V  8  22  ? 8.475   -156.000 33.529  1.00 93.46  ? 23  GLY   V CA  1 
ATOM   37875 C  C   . GLY   V  8  22  ? 7.315   -155.346 34.277  1.00 92.07  ? 23  GLY   V C   1 
ATOM   37876 O  O   . GLY   V  8  22  ? 6.933   -155.820 35.344  1.00 93.22  ? 23  GLY   V O   1 
ATOM   37877 N  N   . PRO   V  8  23  ? 6.703   -154.265 33.738  1.00 93.08  ? 24  PRO   V N   1 
ATOM   37878 C  CA  . PRO   V  8  23  ? 5.523   -153.648 34.347  1.00 92.05  ? 24  PRO   V CA  1 
ATOM   37879 C  C   . PRO   V  8  23  ? 4.172   -154.133 33.787  1.00 93.22  ? 24  PRO   V C   1 
ATOM   37880 O  O   . PRO   V  8  23  ? 3.152   -153.568 34.154  1.00 91.40  ? 24  PRO   V O   1 
ATOM   37881 C  CB  . PRO   V  8  23  ? 5.764   -152.181 33.972  1.00 91.24  ? 24  PRO   V CB  1 
ATOM   37882 C  CG  . PRO   V  8  23  ? 6.339   -152.257 32.568  1.00 91.28  ? 24  PRO   V CG  1 
ATOM   37883 C  CD  . PRO   V  8  23  ? 7.122   -153.555 32.519  1.00 91.76  ? 24  PRO   V CD  1 
ATOM   37884 N  N   . ILE   V  8  24  ? 4.199   -155.155 32.922  1.00 93.77  ? 25  ILE   V N   1 
ATOM   37885 C  CA  . ILE   V  8  24  ? 3.012   -155.738 32.225  1.00 95.70  ? 25  ILE   V CA  1 
ATOM   37886 C  C   . ILE   V  8  24  ? 2.586   -157.016 32.958  1.00 96.04  ? 25  ILE   V C   1 
ATOM   37887 O  O   . ILE   V  8  24  ? 3.471   -157.829 33.288  1.00 99.62  ? 25  ILE   V O   1 
ATOM   37888 C  CB  . ILE   V  8  24  ? 3.343   -156.011 30.742  1.00 97.80  ? 25  ILE   V CB  1 
ATOM   37889 C  CG1 . ILE   V  8  24  ? 3.338   -154.724 29.912  1.00 99.16  ? 25  ILE   V CG1 1 
ATOM   37890 C  CG2 . ILE   V  8  24  ? 2.420   -157.069 30.150  1.00 100.37 ? 25  ILE   V CG2 1 
ATOM   37891 C  CD1 . ILE   V  8  24  ? 1.964   -154.127 29.694  1.00 101.38 ? 25  ILE   V CD1 1 
ATOM   37892 N  N   . VAL   V  8  25  ? 1.279   -157.194 33.176  1.00 95.14  ? 26  VAL   V N   1 
ATOM   37893 C  CA  . VAL   V  8  25  ? 0.692   -158.414 33.806  1.00 97.24  ? 26  VAL   V CA  1 
ATOM   37894 C  C   . VAL   V  8  25  ? 0.507   -159.476 32.714  1.00 98.38  ? 26  VAL   V C   1 
ATOM   37895 O  O   . VAL   V  8  25  ? -0.438  -159.337 31.914  1.00 101.74 ? 26  VAL   V O   1 
ATOM   37896 C  CB  . VAL   V  8  25  ? -0.634  -158.098 34.527  1.00 96.85  ? 26  VAL   V CB  1 
ATOM   37897 C  CG1 . VAL   V  8  25  ? -1.283  -159.351 35.094  1.00 99.11  ? 26  VAL   V CG1 1 
ATOM   37898 C  CG2 . VAL   V  8  25  ? -0.447  -157.061 35.622  1.00 97.17  ? 26  VAL   V CG2 1 
ATOM   37899 N  N   . ALA   V  8  26  ? 1.380   -160.490 32.686  1.00 100.66 ? 27  ALA   V N   1 
ATOM   37900 C  CA  . ALA   V  8  26  ? 1.345   -161.618 31.723  1.00 98.61  ? 27  ALA   V CA  1 
ATOM   37901 C  C   . ALA   V  8  26  ? 0.139   -162.520 32.012  1.00 99.88  ? 27  ALA   V C   1 
ATOM   37902 O  O   . ALA   V  8  26  ? -0.571  -162.873 31.047  1.00 99.32  ? 27  ALA   V O   1 
ATOM   37903 C  CB  . ALA   V  8  26  ? 2.636   -162.397 31.777  1.00 97.50  ? 27  ALA   V CB  1 
ATOM   37904 N  N   . ASP   V  8  27  ? -0.079  -162.881 33.284  1.00 97.84  ? 28  ASP   V N   1 
ATOM   37905 C  CA  . ASP   V  8  27  ? -1.206  -163.749 33.722  1.00 98.56  ? 28  ASP   V CA  1 
ATOM   37906 C  C   . ASP   V  8  27  ? -1.944  -163.086 34.891  1.00 93.88  ? 28  ASP   V C   1 
ATOM   37907 O  O   . ASP   V  8  27  ? -1.313  -162.859 35.941  1.00 89.12  ? 28  ASP   V O   1 
ATOM   37908 C  CB  . ASP   V  8  27  ? -0.713  -165.150 34.093  1.00 101.50 ? 28  ASP   V CB  1 
ATOM   37909 C  CG  . ASP   V  8  27  ? -1.777  -166.229 33.962  1.00 106.48 ? 28  ASP   V CG  1 
ATOM   37910 O  OD1 . ASP   V  8  27  ? -1.399  -167.413 33.840  1.00 109.98 ? 28  ASP   V OD1 1 
ATOM   37911 O  OD2 . ASP   V  8  27  ? -2.976  -165.880 33.982  1.00 113.83 ? 28  ASP   V OD2 1 
ATOM   37912 N  N   . LYS   V  8  28  ? -3.238  -162.805 34.708  1.00 93.62  ? 29  LYS   V N   1 
ATOM   37913 C  CA  . LYS   V  8  28  ? -4.131  -162.199 35.735  1.00 94.96  ? 29  LYS   V CA  1 
ATOM   37914 C  C   . LYS   V  8  28  ? -4.462  -163.231 36.816  1.00 95.47  ? 29  LYS   V C   1 
ATOM   37915 O  O   . LYS   V  8  28  ? -4.684  -162.821 37.970  1.00 95.17  ? 29  LYS   V O   1 
ATOM   37916 C  CB  . LYS   V  8  28  ? -5.416  -161.670 35.091  1.00 97.53  ? 29  LYS   V CB  1 
ATOM   37917 C  CG  . LYS   V  8  28  ? -5.252  -160.348 34.358  1.00 96.81  ? 29  LYS   V CG  1 
ATOM   37918 C  CD  . LYS   V  8  28  ? -6.558  -159.726 33.933  1.00 98.41  ? 29  LYS   V CD  1 
ATOM   37919 C  CE  . LYS   V  8  28  ? -7.086  -160.284 32.630  1.00 100.70 ? 29  LYS   V CE  1 
ATOM   37920 N  NZ  . LYS   V  8  28  ? -7.942  -159.296 31.938  1.00 103.32 ? 29  LYS   V NZ  1 
ATOM   37921 N  N   . ASN   V  8  29  ? -4.506  -164.514 36.448  1.00 95.35  ? 30  ASN   V N   1 
ATOM   37922 C  CA  . ASN   V  8  29  ? -4.838  -165.639 37.361  1.00 96.72  ? 30  ASN   V CA  1 
ATOM   37923 C  C   . ASN   V  8  29  ? -3.915  -166.825 37.047  1.00 97.98  ? 30  ASN   V C   1 
ATOM   37924 O  O   . ASN   V  8  29  ? -4.264  -167.632 36.162  1.00 102.01 ? 30  ASN   V O   1 
ATOM   37925 C  CB  . ASN   V  8  29  ? -6.325  -165.992 37.258  1.00 94.31  ? 30  ASN   V CB  1 
ATOM   37926 C  CG  . ASN   V  8  29  ? -6.810  -166.902 38.365  1.00 93.34  ? 30  ASN   V CG  1 
ATOM   37927 O  OD1 . ASN   V  8  29  ? -7.919  -166.740 38.863  1.00 93.06  ? 30  ASN   V OD1 1 
ATOM   37928 N  ND2 . ASN   V  8  29  ? -5.998  -167.865 38.756  1.00 93.38  ? 30  ASN   V ND2 1 
ATOM   37929 N  N   . CYS   V  8  30  ? -2.834  -166.945 37.813  1.00 99.76  ? 31  CYS   V N   1 
ATOM   37930 C  CA  . CYS   V  8  30  ? -1.863  -168.055 37.681  1.00 102.03 ? 31  CYS   V CA  1 
ATOM   37931 C  C   . CYS   V  8  30  ? -1.609  -168.606 39.087  1.00 102.27 ? 31  CYS   V C   1 
ATOM   37932 O  O   . CYS   V  8  30  ? -1.584  -167.795 40.014  1.00 106.75 ? 31  CYS   V O   1 
ATOM   37933 C  CB  . CYS   V  8  30  ? -0.555  -167.531 37.119  1.00 105.33 ? 31  CYS   V CB  1 
ATOM   37934 S  SG  . CYS   V  8  30  ? 0.418   -166.678 38.380  1.00 104.42 ? 31  CYS   V SG  1 
ATOM   37935 N  N   . ALA   V  8  31  ? -1.435  -169.924 39.226  1.00 102.94 ? 32  ALA   V N   1 
ATOM   37936 C  CA  . ALA   V  8  31  ? -1.204  -170.597 40.525  1.00 102.61 ? 32  ALA   V CA  1 
ATOM   37937 C  C   . ALA   V  8  31  ? 0.299   -170.614 40.815  1.00 100.52 ? 32  ALA   V C   1 
ATOM   37938 O  O   . ALA   V  8  31  ? 1.066   -171.070 39.943  1.00 98.06  ? 32  ALA   V O   1 
ATOM   37939 C  CB  . ALA   V  8  31  ? -1.786  -171.986 40.518  1.00 103.27 ? 32  ALA   V CB  1 
ATOM   37940 N  N   . LYS   V  8  32  ? 0.670   -170.171 42.014  1.00 101.36 ? 33  LYS   V N   1 
ATOM   37941 C  CA  . LYS   V  8  32  ? 2.085   -170.127 42.451  1.00 100.51 ? 33  LYS   V CA  1 
ATOM   37942 C  C   . LYS   V  8  32  ? 2.305   -171.257 43.455  1.00 98.71  ? 33  LYS   V C   1 
ATOM   37943 O  O   . LYS   V  8  32  ? 3.445   -171.448 43.882  1.00 97.30  ? 33  LYS   V O   1 
ATOM   37944 C  CB  . LYS   V  8  32  ? 2.377   -168.774 43.103  1.00 99.96  ? 33  LYS   V CB  1 
ATOM   37945 C  CG  . LYS   V  8  32  ? 2.685   -167.635 42.142  1.00 100.51 ? 33  LYS   V CG  1 
ATOM   37946 C  CD  . LYS   V  8  32  ? 1.997   -166.347 42.514  1.00 97.09  ? 33  LYS   V CD  1 
ATOM   37947 C  CE  . LYS   V  8  32  ? 2.361   -165.209 41.592  1.00 96.46  ? 33  LYS   V CE  1 
ATOM   37948 N  NZ  . LYS   V  8  32  ? 2.873   -164.040 42.340  1.00 95.40  ? 33  LYS   V NZ  1 
ATOM   37949 N  N   . LEU   V  8  33  ? 1.220   -171.945 43.813  1.00 100.47 ? 34  LEU   V N   1 
ATOM   37950 C  CA  . LEU   V  8  33  ? 1.217   -173.100 44.748  1.00 98.96  ? 34  LEU   V CA  1 
ATOM   37951 C  C   . LEU   V  8  33  ? 1.422   -174.380 43.942  1.00 99.17  ? 34  LEU   V C   1 
ATOM   37952 O  O   . LEU   V  8  33  ? 0.561   -174.687 43.096  1.00 99.27  ? 34  LEU   V O   1 
ATOM   37953 C  CB  . LEU   V  8  33  ? -0.116  -173.147 45.499  1.00 99.53  ? 34  LEU   V CB  1 
ATOM   37954 C  CG  . LEU   V  8  33  ? -0.156  -172.415 46.838  1.00 96.50  ? 34  LEU   V CG  1 
ATOM   37955 C  CD1 . LEU   V  8  33  ? 0.663   -171.135 46.799  1.00 93.89  ? 34  LEU   V CD1 1 
ATOM   37956 C  CD2 . LEU   V  8  33  ? -1.592  -172.117 47.233  1.00 97.13  ? 34  LEU   V CD2 1 
ATOM   37957 N  N   . HIS   V  8  34  ? 2.515   -175.092 44.210  1.00 102.63 ? 35  HIS   V N   1 
ATOM   37958 C  CA  . HIS   V  8  34  ? 2.879   -176.356 43.525  1.00 105.39 ? 35  HIS   V CA  1 
ATOM   37959 C  C   . HIS   V  8  34  ? 2.833   -177.516 44.521  1.00 103.10 ? 35  HIS   V C   1 
ATOM   37960 O  O   . HIS   V  8  34  ? 3.181   -177.313 45.704  1.00 100.66 ? 35  HIS   V O   1 
ATOM   37961 C  CB  . HIS   V  8  34  ? 4.258   -176.244 42.875  1.00 110.33 ? 35  HIS   V CB  1 
ATOM   37962 C  CG  . HIS   V  8  34  ? 4.520   -174.937 42.209  1.00 112.17 ? 35  HIS   V CG  1 
ATOM   37963 N  ND1 . HIS   V  8  34  ? 4.256   -174.722 40.872  1.00 115.17 ? 35  HIS   V ND1 1 
ATOM   37964 C  CD2 . HIS   V  8  34  ? 5.033   -173.783 42.688  1.00 114.59 ? 35  HIS   V CD2 1 
ATOM   37965 C  CE1 . HIS   V  8  34  ? 4.591   -173.487 40.557  1.00 116.33 ? 35  HIS   V CE1 1 
ATOM   37966 N  NE2 . HIS   V  8  34  ? 5.070   -172.889 41.654  1.00 118.14 ? 35  HIS   V NE2 1 
ATOM   37967 N  N   . ARG   V  8  35  ? 2.480   -178.697 44.015  1.00 100.41 ? 36  ARG   V N   1 
ATOM   37968 C  CA  . ARG   V  8  35  ? 2.406   -179.928 44.831  1.00 97.59  ? 36  ARG   V CA  1 
ATOM   37969 C  C   . ARG   V  8  35  ? 3.679   -180.739 44.598  1.00 93.60  ? 36  ARG   V C   1 
ATOM   37970 O  O   . ARG   V  8  35  ? 3.891   -181.162 43.465  1.00 93.99  ? 36  ARG   V O   1 
ATOM   37971 C  CB  . ARG   V  8  35  ? 1.173   -180.734 44.414  1.00 98.37  ? 36  ARG   V CB  1 
ATOM   37972 C  CG  . ARG   V  8  35  ? 1.008   -182.068 45.126  1.00 97.81  ? 36  ARG   V CG  1 
ATOM   37973 C  CD  . ARG   V  8  35  ? 0.026   -183.021 44.464  1.00 101.51 ? 36  ARG   V CD  1 
ATOM   37974 N  NE  . ARG   V  8  35  ? 0.337   -183.266 43.065  1.00 102.11 ? 36  ARG   V NE  1 
ATOM   37975 C  CZ  . ARG   V  8  35  ? -0.480  -183.082 42.033  1.00 105.55 ? 36  ARG   V CZ  1 
ATOM   37976 N  NH1 . ARG   V  8  35  ? -1.714  -182.630 42.197  1.00 108.78 ? 36  ARG   V NH1 1 
ATOM   37977 N  NH2 . ARG   V  8  35  ? -0.042  -183.351 40.820  1.00 109.32 ? 36  ARG   V NH2 1 
ATOM   37978 N  N   . ILE   V  8  36  ? 4.538   -180.826 45.612  1.00 94.64  ? 37  ILE   V N   1 
ATOM   37979 C  CA  . ILE   V  8  36  ? 5.742   -181.711 45.589  1.00 96.70  ? 37  ILE   V CA  1 
ATOM   37980 C  C   . ILE   V  8  36  ? 5.280   -183.155 45.815  1.00 94.78  ? 37  ILE   V C   1 
ATOM   37981 O  O   . ILE   V  8  36  ? 5.807   -184.061 45.141  1.00 93.09  ? 37  ILE   V O   1 
ATOM   37982 C  CB  . ILE   V  8  36  ? 6.785   -181.263 46.632  1.00 99.12  ? 37  ILE   V CB  1 
ATOM   37983 C  CG1 . ILE   V  8  36  ? 7.434   -179.940 46.214  1.00 99.59  ? 37  ILE   V CG1 1 
ATOM   37984 C  CG2 . ILE   V  8  36  ? 7.815   -182.361 46.874  1.00 100.78 ? 37  ILE   V CG2 1 
ATOM   37985 C  CD1 . ILE   V  8  36  ? 8.466   -179.411 47.183  1.00 101.45 ? 37  ILE   V CD1 1 
ATOM   37986 N  N   . SER   V  8  37  ? 4.340   -183.346 46.744  1.00 96.62  ? 38  SER   V N   1 
ATOM   37987 C  CA  . SER   V  8  37  ? 3.684   -184.639 47.068  1.00 99.19  ? 38  SER   V CA  1 
ATOM   37988 C  C   . SER   V  8  37  ? 2.271   -184.353 47.568  1.00 100.09 ? 38  SER   V C   1 
ATOM   37989 O  O   . SER   V  8  37  ? 1.926   -183.199 47.812  1.00 101.21 ? 38  SER   V O   1 
ATOM   37990 C  CB  . SER   V  8  37  ? 4.496   -185.424 48.074  1.00 98.58  ? 38  SER   V CB  1 
ATOM   37991 O  OG  . SER   V  8  37  ? 4.024   -185.227 49.399  1.00 97.83  ? 38  SER   V OG  1 
ATOM   37992 N  N   . PRO   V  8  38  ? 1.412   -185.379 47.755  1.00 101.46 ? 39  PRO   V N   1 
ATOM   37993 C  CA  . PRO   V  8  38  ? 0.032   -185.148 48.186  1.00 102.01 ? 39  PRO   V CA  1 
ATOM   37994 C  C   . PRO   V  8  38  ? -0.068  -184.276 49.447  1.00 100.62 ? 39  PRO   V C   1 
ATOM   37995 O  O   . PRO   V  8  38  ? -0.913  -183.405 49.478  1.00 98.39  ? 39  PRO   V O   1 
ATOM   37996 C  CB  . PRO   V  8  38  ? -0.488  -186.568 48.455  1.00 103.12 ? 39  PRO   V CB  1 
ATOM   37997 C  CG  . PRO   V  8  38  ? 0.338   -187.429 47.528  1.00 103.02 ? 39  PRO   V CG  1 
ATOM   37998 C  CD  . PRO   V  8  38  ? 1.717   -186.807 47.580  1.00 102.26 ? 39  PRO   V CD  1 
ATOM   37999 N  N   . LYS   V  8  39  ? 0.795   -184.523 50.438  1.00 101.42 ? 40  LYS   V N   1 
ATOM   38000 C  CA  . LYS   V  8  39  ? 0.767   -183.834 51.755  1.00 103.37 ? 40  LYS   V CA  1 
ATOM   38001 C  C   . LYS   V  8  39  ? 1.999   -182.937 51.931  1.00 100.61 ? 40  LYS   V C   1 
ATOM   38002 O  O   . LYS   V  8  39  ? 2.233   -182.498 53.072  1.00 102.46 ? 40  LYS   V O   1 
ATOM   38003 C  CB  . LYS   V  8  39  ? 0.664   -184.869 52.877  1.00 106.16 ? 40  LYS   V CB  1 
ATOM   38004 C  CG  . LYS   V  8  39  ? -0.649  -185.632 52.905  1.00 110.90 ? 40  LYS   V CG  1 
ATOM   38005 C  CD  . LYS   V  8  39  ? -1.303  -185.593 54.252  1.00 115.87 ? 40  LYS   V CD  1 
ATOM   38006 C  CE  . LYS   V  8  39  ? -2.569  -186.411 54.306  1.00 120.78 ? 40  LYS   V CE  1 
ATOM   38007 N  NZ  . LYS   V  8  39  ? -2.784  -186.904 55.677  1.00 123.34 ? 40  LYS   V NZ  1 
ATOM   38008 N  N   . ILE   V  8  40  ? 2.750   -182.667 50.858  1.00 98.28  ? 41  ILE   V N   1 
ATOM   38009 C  CA  . ILE   V  8  40  ? 3.850   -181.654 50.845  1.00 99.68  ? 41  ILE   V CA  1 
ATOM   38010 C  C   . ILE   V  8  40  ? 3.609   -180.674 49.695  1.00 99.26  ? 41  ILE   V C   1 
ATOM   38011 O  O   . ILE   V  8  40  ? 3.731   -181.086 48.526  1.00 99.30  ? 41  ILE   V O   1 
ATOM   38012 C  CB  . ILE   V  8  40  ? 5.243   -182.301 50.725  1.00 98.29  ? 41  ILE   V CB  1 
ATOM   38013 C  CG1 . ILE   V  8  40  ? 5.520   -183.269 51.878  1.00 100.89 ? 41  ILE   V CG1 1 
ATOM   38014 C  CG2 . ILE   V  8  40  ? 6.311   -181.220 50.606  1.00 96.76  ? 41  ILE   V CG2 1 
ATOM   38015 C  CD1 . ILE   V  8  40  ? 6.968   -183.673 52.009  1.00 101.31 ? 41  ILE   V CD1 1 
ATOM   38016 N  N   . TRP   V  8  41  ? 3.329   -179.413 50.025  1.00 100.29 ? 42  TRP   V N   1 
ATOM   38017 C  CA  . TRP   V  8  41  ? 3.124   -178.320 49.042  1.00 101.38 ? 42  TRP   V CA  1 
ATOM   38018 C  C   . TRP   V  8  41  ? 4.162   -177.221 49.266  1.00 99.41  ? 42  TRP   V C   1 
ATOM   38019 O  O   . TRP   V  8  41  ? 4.630   -177.052 50.407  1.00 99.63  ? 42  TRP   V O   1 
ATOM   38020 C  CB  . TRP   V  8  41  ? 1.702   -177.764 49.132  1.00 101.78 ? 42  TRP   V CB  1 
ATOM   38021 C  CG  . TRP   V  8  41  ? 0.653   -178.719 48.658  1.00 102.47 ? 42  TRP   V CG  1 
ATOM   38022 C  CD1 . TRP   V  8  41  ? 0.283   -179.897 49.239  1.00 102.42 ? 42  TRP   V CD1 1 
ATOM   38023 C  CD2 . TRP   V  8  41  ? -0.174  -178.568 47.493  1.00 102.77 ? 42  TRP   V CD2 1 
ATOM   38024 N  NE1 . TRP   V  8  41  ? -0.716  -180.489 48.514  1.00 102.68 ? 42  TRP   V NE1 1 
ATOM   38025 C  CE2 . TRP   V  8  41  ? -1.018  -179.698 47.437  1.00 103.89 ? 42  TRP   V CE2 1 
ATOM   38026 C  CE3 . TRP   V  8  41  ? -0.283  -177.593 46.496  1.00 103.79 ? 42  TRP   V CE3 1 
ATOM   38027 C  CZ2 . TRP   V  8  41  ? -1.957  -179.875 46.423  1.00 103.58 ? 42  TRP   V CZ2 1 
ATOM   38028 C  CZ3 . TRP   V  8  41  ? -1.211  -177.769 45.494  1.00 106.17 ? 42  TRP   V CZ3 1 
ATOM   38029 C  CH2 . TRP   V  8  41  ? -2.035  -178.896 45.460  1.00 104.67 ? 42  TRP   V CH2 1 
ATOM   38030 N  N   . CYS   V  8  42  ? 4.483   -176.495 48.199  1.00 97.39  ? 43  CYS   V N   1 
ATOM   38031 C  CA  . CYS   V  8  42  ? 5.511   -175.430 48.177  1.00 97.06  ? 43  CYS   V CA  1 
ATOM   38032 C  C   . CYS   V  8  42  ? 4.971   -174.239 47.378  1.00 94.10  ? 43  CYS   V C   1 
ATOM   38033 O  O   . CYS   V  8  42  ? 4.312   -174.470 46.346  1.00 92.30  ? 43  CYS   V O   1 
ATOM   38034 C  CB  . CYS   V  8  42  ? 6.800   -175.988 47.586  1.00 100.62 ? 43  CYS   V CB  1 
ATOM   38035 S  SG  . CYS   V  8  42  ? 7.777   -174.774 46.661  1.00 110.98 ? 43  CYS   V SG  1 
ATOM   38036 N  N   . ALA   V  8  43  ? 5.217   -173.019 47.862  1.00 93.48  ? 44  ALA   V N   1 
ATOM   38037 C  CA  . ALA   V  8  43  ? 4.843   -171.740 47.212  1.00 93.36  ? 44  ALA   V CA  1 
ATOM   38038 C  C   . ALA   V  8  43  ? 6.121   -171.017 46.773  1.00 91.20  ? 44  ALA   V C   1 
ATOM   38039 O  O   . ALA   V  8  43  ? 7.031   -170.882 47.611  1.00 93.13  ? 44  ALA   V O   1 
ATOM   38040 C  CB  . ALA   V  8  43  ? 4.027   -170.903 48.164  1.00 92.91  ? 44  ALA   V CB  1 
ATOM   38041 N  N   . GLY   V  8  44  ? 6.193   -170.619 45.501  1.00 89.47  ? 45  GLY   V N   1 
ATOM   38042 C  CA  . GLY   V  8  44  ? 7.428   -170.033 44.947  1.00 89.71  ? 45  GLY   V CA  1 
ATOM   38043 C  C   . GLY   V  8  44  ? 7.305   -168.596 44.478  1.00 88.47  ? 45  GLY   V C   1 
ATOM   38044 O  O   . GLY   V  8  44  ? 6.184   -168.125 44.304  1.00 90.17  ? 45  GLY   V O   1 
ATOM   38045 N  N   . ALA   V  8  45  ? 8.448   -167.946 44.250  1.00 86.17  ? 46  ALA   V N   1 
ATOM   38046 C  CA  . ALA   V  8  45  ? 8.499   -166.533 43.820  1.00 84.48  ? 46  ALA   V CA  1 
ATOM   38047 C  C   . ALA   V  8  45  ? 9.800   -166.285 43.060  1.00 85.63  ? 46  ALA   V C   1 
ATOM   38048 O  O   . ALA   V  8  45  ? 10.825  -166.777 43.493  1.00 90.25  ? 46  ALA   V O   1 
ATOM   38049 C  CB  . ALA   V  8  45  ? 8.425   -165.665 45.039  1.00 81.61  ? 46  ALA   V CB  1 
ATOM   38050 N  N   . GLY   V  8  46  ? 9.754   -165.516 41.980  1.00 84.82  ? 47  GLY   V N   1 
ATOM   38051 C  CA  . GLY   V  8  46  ? 10.959  -165.259 41.175  1.00 87.53  ? 47  GLY   V CA  1 
ATOM   38052 C  C   . GLY   V  8  46  ? 10.690  -165.677 39.750  1.00 89.13  ? 47  GLY   V C   1 
ATOM   38053 O  O   . GLY   V  8  46  ? 9.527   -165.590 39.352  1.00 90.87  ? 47  GLY   V O   1 
ATOM   38054 N  N   . THR   V  8  47  ? 11.714  -166.101 39.010  1.00 90.30  ? 48  THR   V N   1 
ATOM   38055 C  CA  . THR   V  8  47  ? 11.467  -166.572 37.628  1.00 91.27  ? 48  THR   V CA  1 
ATOM   38056 C  C   . THR   V  8  47  ? 10.451  -167.704 37.717  1.00 91.17  ? 48  THR   V C   1 
ATOM   38057 O  O   . THR   V  8  47  ? 10.772  -168.697 38.345  1.00 91.91  ? 48  THR   V O   1 
ATOM   38058 C  CB  . THR   V  8  47  ? 12.756  -167.078 36.987  1.00 92.51  ? 48  THR   V CB  1 
ATOM   38059 O  OG1 . THR   V  8  47  ? 13.744  -166.084 37.242  1.00 93.70  ? 48  THR   V OG1 1 
ATOM   38060 C  CG2 . THR   V  8  47  ? 12.610  -167.282 35.500  1.00 93.14  ? 48  THR   V CG2 1 
ATOM   38061 N  N   . ALA   V  8  48  ? 9.266   -167.527 37.139  1.00 91.21  ? 49  ALA   V N   1 
ATOM   38062 C  CA  . ALA   V  8  48  ? 8.180   -168.530 37.222  1.00 91.86  ? 49  ALA   V CA  1 
ATOM   38063 C  C   . ALA   V  8  48  ? 8.635   -169.887 36.675  1.00 92.19  ? 49  ALA   V C   1 
ATOM   38064 O  O   . ALA   V  8  48  ? 8.407   -170.907 37.327  1.00 92.20  ? 49  ALA   V O   1 
ATOM   38065 C  CB  . ALA   V  8  48  ? 6.983   -168.019 36.469  1.00 89.39  ? 49  ALA   V CB  1 
ATOM   38066 N  N   . ALA   V  8  49  ? 9.238   -169.886 35.496  1.00 95.76  ? 50  ALA   V N   1 
ATOM   38067 C  CA  . ALA   V  8  49  ? 9.693   -171.142 34.854  1.00 94.57  ? 50  ALA   V CA  1 
ATOM   38068 C  C   . ALA   V  8  49  ? 10.595  -171.919 35.817  1.00 95.38  ? 50  ALA   V C   1 
ATOM   38069 O  O   . ALA   V  8  49  ? 10.441  -173.148 35.891  1.00 98.98  ? 50  ALA   V O   1 
ATOM   38070 C  CB  . ALA   V  8  49  ? 10.412  -170.845 33.564  1.00 100.12 ? 50  ALA   V CB  1 
ATOM   38071 N  N   . ASP   V  8  50  ? 11.497  -171.225 36.521  1.00 89.19  ? 51  ASP   V N   1 
ATOM   38072 C  CA  . ASP   V  8  50  ? 12.476  -171.836 37.461  1.00 87.55  ? 51  ASP   V CA  1 
ATOM   38073 C  C   . ASP   V  8  50  ? 11.746  -172.458 38.656  1.00 89.08  ? 51  ASP   V C   1 
ATOM   38074 O  O   . ASP   V  8  50  ? 12.105  -173.589 39.012  1.00 89.32  ? 51  ASP   V O   1 
ATOM   38075 C  CB  . ASP   V  8  50  ? 13.530  -170.833 37.932  1.00 87.70  ? 51  ASP   V CB  1 
ATOM   38076 C  CG  . ASP   V  8  50  ? 14.608  -170.554 36.901  1.00 88.18  ? 51  ASP   V CG  1 
ATOM   38077 O  OD1 . ASP   V  8  50  ? 14.858  -171.437 36.058  1.00 89.36  ? 51  ASP   V OD1 1 
ATOM   38078 O  OD2 . ASP   V  8  50  ? 15.186  -169.454 36.944  1.00 92.27  ? 51  ASP   V OD2 1 
ATOM   38079 N  N   . THR   V  8  51  ? 10.782  -171.761 39.245  1.00 89.73  ? 52  THR   V N   1 
ATOM   38080 C  CA  . THR   V  8  51  ? 10.089  -172.343 40.419  1.00 91.55  ? 52  THR   V CA  1 
ATOM   38081 C  C   . THR   V  8  51  ? 9.310   -173.579 39.988  1.00 95.11  ? 52  THR   V C   1 
ATOM   38082 O  O   . THR   V  8  51  ? 9.439   -174.605 40.645  1.00 97.08  ? 52  THR   V O   1 
ATOM   38083 C  CB  . THR   V  8  51  ? 9.152   -171.339 41.090  1.00 92.64  ? 52  THR   V CB  1 
ATOM   38084 O  OG1 . THR   V  8  51  ? 7.922   -171.369 40.371  1.00 96.13  ? 52  THR   V OG1 1 
ATOM   38085 C  CG2 . THR   V  8  51  ? 9.719   -169.941 41.121  1.00 92.12  ? 52  THR   V CG2 1 
ATOM   38086 N  N   . GLU   V  8  52  ? 8.508   -173.461 38.937  1.00 94.83  ? 53  GLU   V N   1 
ATOM   38087 C  CA  . GLU   V  8  52  ? 7.712   -174.614 38.434  1.00 97.61  ? 53  GLU   V CA  1 
ATOM   38088 C  C   . GLU   V  8  52  ? 8.665   -175.782 38.145  1.00 94.17  ? 53  GLU   V C   1 
ATOM   38089 O  O   . GLU   V  8  52  ? 8.396   -176.892 38.647  1.00 93.89  ? 53  GLU   V O   1 
ATOM   38090 C  CB  . GLU   V  8  52  ? 6.898   -174.241 37.192  1.00 104.07 ? 53  GLU   V CB  1 
ATOM   38091 C  CG  . GLU   V  8  52  ? 6.005   -175.368 36.678  1.00 111.39 ? 53  GLU   V CG  1 
ATOM   38092 C  CD  . GLU   V  8  52  ? 4.625   -175.498 37.313  1.00 118.21 ? 53  GLU   V CD  1 
ATOM   38093 O  OE1 . GLU   V  8  52  ? 4.062   -174.468 37.736  1.00 132.87 ? 53  GLU   V OE1 1 
ATOM   38094 O  OE2 . GLU   V  8  52  ? 4.104   -176.634 37.367  1.00 119.92 ? 53  GLU   V OE2 1 
ATOM   38095 N  N   . ALA   V  8  53  ? 9.743   -175.529 37.393  1.00 88.17  ? 54  ALA   V N   1 
ATOM   38096 C  CA  . ALA   V  8  53  ? 10.695  -176.553 36.895  1.00 87.50  ? 54  ALA   V CA  1 
ATOM   38097 C  C   . ALA   V  8  53  ? 11.352  -177.293 38.066  1.00 88.73  ? 54  ALA   V C   1 
ATOM   38098 O  O   . ALA   V  8  53  ? 11.315  -178.540 38.056  1.00 91.05  ? 54  ALA   V O   1 
ATOM   38099 C  CB  . ALA   V  8  53  ? 11.731  -175.923 35.998  1.00 83.05  ? 54  ALA   V CB  1 
ATOM   38100 N  N   . VAL   V  8  54  ? 11.935  -176.562 39.023  1.00 86.04  ? 55  VAL   V N   1 
ATOM   38101 C  CA  . VAL   V  8  54  ? 12.670  -177.152 40.184  1.00 87.54  ? 55  VAL   V CA  1 
ATOM   38102 C  C   . VAL   V  8  54  ? 11.677  -177.926 41.061  1.00 90.16  ? 55  VAL   V C   1 
ATOM   38103 O  O   . VAL   V  8  54  ? 12.056  -179.000 41.554  1.00 91.30  ? 55  VAL   V O   1 
ATOM   38104 C  CB  . VAL   V  8  54  ? 13.454  -176.106 41.004  1.00 85.16  ? 55  VAL   V CB  1 
ATOM   38105 C  CG1 . VAL   V  8  54  ? 12.560  -175.075 41.673  1.00 85.69  ? 55  VAL   V CG1 1 
ATOM   38106 C  CG2 . VAL   V  8  54  ? 14.331  -176.776 42.047  1.00 86.63  ? 55  VAL   V CG2 1 
ATOM   38107 N  N   . THR   V  8  55  ? 10.460  -177.410 41.245  1.00 91.71  ? 56  THR   V N   1 
ATOM   38108 C  CA  . THR   V  8  55  ? 9.388   -178.075 42.033  1.00 97.52  ? 56  THR   V CA  1 
ATOM   38109 C  C   . THR   V  8  55  ? 9.051   -179.438 41.414  1.00 98.25  ? 56  THR   V C   1 
ATOM   38110 O  O   . THR   V  8  55  ? 8.967   -180.424 42.175  1.00 99.56  ? 56  THR   V O   1 
ATOM   38111 C  CB  . THR   V  8  55  ? 8.121   -177.217 42.119  1.00 99.27  ? 56  THR   V CB  1 
ATOM   38112 O  OG1 . THR   V  8  55  ? 8.324   -176.203 43.105  1.00 97.39  ? 56  THR   V OG1 1 
ATOM   38113 C  CG2 . THR   V  8  55  ? 6.902   -178.037 42.475  1.00 104.26 ? 56  THR   V CG2 1 
ATOM   38114 N  N   . GLN   V  8  56  ? 8.831   -179.475 40.096  1.00 101.14 ? 57  GLN   V N   1 
ATOM   38115 C  CA  . GLN   V  8  56  ? 8.440   -180.701 39.351  1.00 101.59 ? 57  GLN   V CA  1 
ATOM   38116 C  C   . GLN   V  8  56  ? 9.567   -181.737 39.432  1.00 96.28  ? 57  GLN   V C   1 
ATOM   38117 O  O   . GLN   V  8  56  ? 9.247   -182.920 39.644  1.00 100.39 ? 57  GLN   V O   1 
ATOM   38118 C  CB  . GLN   V  8  56  ? 8.114   -180.384 37.891  1.00 106.46 ? 57  GLN   V CB  1 
ATOM   38119 C  CG  . GLN   V  8  56  ? 6.746   -179.744 37.700  1.00 111.76 ? 57  GLN   V CG  1 
ATOM   38120 C  CD  . GLN   V  8  56  ? 6.312   -179.616 36.257  1.00 119.88 ? 57  GLN   V CD  1 
ATOM   38121 O  OE1 . GLN   V  8  56  ? 5.261   -179.049 35.967  1.00 125.53 ? 57  GLN   V OE1 1 
ATOM   38122 N  NE2 . GLN   V  8  56  ? 7.104   -180.141 35.331  1.00 125.27 ? 57  GLN   V NE2 1 
ATOM   38123 N  N   . LEU   V  8  57  ? 10.825  -181.313 39.264  1.00 91.20  ? 58  LEU   V N   1 
ATOM   38124 C  CA  . LEU   V  8  57  ? 12.008  -182.217 39.268  1.00 88.89  ? 58  LEU   V CA  1 
ATOM   38125 C  C   . LEU   V  8  57  ? 12.132  -182.902 40.633  1.00 89.71  ? 58  LEU   V C   1 
ATOM   38126 O  O   . LEU   V  8  57  ? 12.294  -184.133 40.653  1.00 93.19  ? 58  LEU   V O   1 
ATOM   38127 C  CB  . LEU   V  8  57  ? 13.282  -181.433 38.939  1.00 86.20  ? 58  LEU   V CB  1 
ATOM   38128 C  CG  . LEU   V  8  57  ? 14.582  -182.230 39.064  1.00 86.21  ? 58  LEU   V CG  1 
ATOM   38129 C  CD1 . LEU   V  8  57  ? 14.654  -183.324 38.012  1.00 87.25  ? 58  LEU   V CD1 1 
ATOM   38130 C  CD2 . LEU   V  8  57  ? 15.795  -181.322 38.967  1.00 86.00  ? 58  LEU   V CD2 1 
ATOM   38131 N  N   . ILE   V  8  58  ? 12.083  -182.138 41.727  1.00 87.34  ? 59  ILE   V N   1 
ATOM   38132 C  CA  . ILE   V  8  58  ? 12.186  -182.687 43.113  1.00 88.26  ? 59  ILE   V CA  1 
ATOM   38133 C  C   . ILE   V  8  58  ? 10.913  -183.494 43.403  1.00 88.50  ? 59  ILE   V C   1 
ATOM   38134 O  O   . ILE   V  8  58  ? 11.033  -184.555 44.037  1.00 94.28  ? 59  ILE   V O   1 
ATOM   38135 C  CB  . ILE   V  8  58  ? 12.448  -181.585 44.164  1.00 86.62  ? 59  ILE   V CB  1 
ATOM   38136 C  CG1 . ILE   V  8  58  ? 13.926  -181.185 44.222  1.00 87.35  ? 59  ILE   V CG1 1 
ATOM   38137 C  CG2 . ILE   V  8  58  ? 11.963  -182.020 45.539  1.00 86.79  ? 59  ILE   V CG2 1 
ATOM   38138 C  CD1 . ILE   V  8  58  ? 14.529  -180.768 42.900  1.00 87.89  ? 59  ILE   V CD1 1 
ATOM   38139 N  N   . GLY   V  8  59  ? 9.749   -183.020 42.947  1.00 87.68  ? 60  GLY   V N   1 
ATOM   38140 C  CA  . GLY   V  8  59  ? 8.467   -183.747 43.049  1.00 89.54  ? 60  GLY   V CA  1 
ATOM   38141 C  C   . GLY   V  8  59  ? 8.542   -185.125 42.403  1.00 90.46  ? 60  GLY   V C   1 
ATOM   38142 O  O   . GLY   V  8  59  ? 8.070   -186.101 43.024  1.00 87.96  ? 60  GLY   V O   1 
ATOM   38143 N  N   . SER   V  8  60  ? 9.112   -185.200 41.195  1.00 92.21  ? 61  SER   V N   1 
ATOM   38144 C  CA  . SER   V  8  60  ? 9.364   -186.451 40.430  1.00 93.13  ? 61  SER   V CA  1 
ATOM   38145 C  C   . SER   V  8  60  ? 10.283  -187.369 41.243  1.00 93.43  ? 61  SER   V C   1 
ATOM   38146 O  O   . SER   V  8  60  ? 9.909   -188.536 41.455  1.00 97.66  ? 61  SER   V O   1 
ATOM   38147 C  CB  . SER   V  8  60  ? 9.945   -186.150 39.068  1.00 92.22  ? 61  SER   V CB  1 
ATOM   38148 O  OG  . SER   V  8  60  ? 10.381  -187.335 38.423  1.00 92.51  ? 61  SER   V OG  1 
ATOM   38149 N  N   . ASN   V  8  61  ? 11.431  -186.849 41.691  1.00 90.15  ? 62  ASN   V N   1 
ATOM   38150 C  CA  . ASN   V  8  61  ? 12.463  -187.609 42.450  1.00 90.47  ? 62  ASN   V CA  1 
ATOM   38151 C  C   . ASN   V  8  61  ? 11.918  -188.029 43.823  1.00 90.41  ? 62  ASN   V C   1 
ATOM   38152 O  O   . ASN   V  8  61  ? 12.354  -189.084 44.323  1.00 86.57  ? 62  ASN   V O   1 
ATOM   38153 C  CB  . ASN   V  8  61  ? 13.762  -186.814 42.604  1.00 92.11  ? 62  ASN   V CB  1 
ATOM   38154 C  CG  . ASN   V  8  61  ? 14.591  -186.767 41.337  1.00 93.63  ? 62  ASN   V CG  1 
ATOM   38155 O  OD1 . ASN   V  8  61  ? 14.617  -187.724 40.567  1.00 93.53  ? 62  ASN   V OD1 1 
ATOM   38156 N  ND2 . ASN   V  8  61  ? 15.288  -185.663 41.118  1.00 94.14  ? 62  ASN   V ND2 1 
ATOM   38157 N  N   . ILE   V  8  62  ? 11.019  -187.236 44.417  1.00 91.44  ? 63  ILE   V N   1 
ATOM   38158 C  CA  . ILE   V  8  62  ? 10.372  -187.547 45.728  1.00 91.68  ? 63  ILE   V CA  1 
ATOM   38159 C  C   . ILE   V  8  62  ? 9.409   -188.724 45.536  1.00 92.81  ? 63  ILE   V C   1 
ATOM   38160 O  O   . ILE   V  8  62  ? 9.368   -189.589 46.428  1.00 93.88  ? 63  ILE   V O   1 
ATOM   38161 C  CB  . ILE   V  8  62  ? 9.670   -186.308 46.329  1.00 91.95  ? 63  ILE   V CB  1 
ATOM   38162 C  CG1 . ILE   V  8  62  ? 10.654  -185.402 47.078  1.00 89.88  ? 63  ILE   V CG1 1 
ATOM   38163 C  CG2 . ILE   V  8  62  ? 8.492   -186.707 47.212  1.00 91.94  ? 63  ILE   V CG2 1 
ATOM   38164 C  CD1 . ILE   V  8  62  ? 11.252  -186.008 48.330  1.00 89.97  ? 63  ILE   V CD1 1 
ATOM   38165 N  N   . GLU   V  8  63  ? 8.663   -188.748 44.426  1.00 93.42  ? 64  GLU   V N   1 
ATOM   38166 C  CA  . GLU   V  8  63  ? 7.697   -189.833 44.097  1.00 96.71  ? 64  GLU   V CA  1 
ATOM   38167 C  C   . GLU   V  8  63  ? 8.449   -191.162 43.954  1.00 96.03  ? 64  GLU   V C   1 
ATOM   38168 O  O   . GLU   V  8  63  ? 7.985   -192.156 44.543  1.00 98.10  ? 64  GLU   V O   1 
ATOM   38169 C  CB  . GLU   V  8  63  ? 6.919   -189.511 42.821  1.00 99.71  ? 64  GLU   V CB  1 
ATOM   38170 C  CG  . GLU   V  8  63  ? 5.842   -190.533 42.499  1.00 105.06 ? 64  GLU   V CG  1 
ATOM   38171 C  CD  . GLU   V  8  63  ? 4.968   -190.200 41.301  1.00 109.44 ? 64  GLU   V CD  1 
ATOM   38172 O  OE1 . GLU   V  8  63  ? 4.656   -191.123 40.521  1.00 114.66 ? 64  GLU   V OE1 1 
ATOM   38173 O  OE2 . GLU   V  8  63  ? 4.586   -189.023 41.156  1.00 112.61 ? 64  GLU   V OE2 1 
ATOM   38174 N  N   . LEU   V  8  64  ? 9.555   -191.173 43.198  1.00 94.06  ? 65  LEU   V N   1 
ATOM   38175 C  CA  . LEU   V  8  64  ? 10.432  -192.363 43.005  1.00 94.42  ? 65  LEU   V CA  1 
ATOM   38176 C  C   . LEU   V  8  64  ? 10.977  -192.832 44.360  1.00 95.70  ? 65  LEU   V C   1 
ATOM   38177 O  O   . LEU   V  8  64  ? 10.961  -194.055 44.615  1.00 99.67  ? 65  LEU   V O   1 
ATOM   38178 C  CB  . LEU   V  8  64  ? 11.589  -192.015 42.062  1.00 92.49  ? 65  LEU   V CB  1 
ATOM   38179 C  CG  . LEU   V  8  64  ? 11.230  -191.725 40.605  1.00 94.10  ? 65  LEU   V CG  1 
ATOM   38180 C  CD1 . LEU   V  8  64  ? 12.492  -191.429 39.807  1.00 94.30  ? 65  LEU   V CD1 1 
ATOM   38181 C  CD2 . LEU   V  8  64  ? 10.464  -192.879 39.970  1.00 94.05  ? 65  LEU   V CD2 1 
ATOM   38182 N  N   . HIS   V  8  65  ? 11.462  -191.897 45.181  1.00 94.09  ? 66  HIS   V N   1 
ATOM   38183 C  CA  . HIS   V  8  65  ? 12.032  -192.157 46.530  1.00 93.96  ? 66  HIS   V CA  1 
ATOM   38184 C  C   . HIS   V  8  65  ? 10.972  -192.814 47.420  1.00 92.18  ? 66  HIS   V C   1 
ATOM   38185 O  O   . HIS   V  8  65  ? 11.310  -193.799 48.098  1.00 92.94  ? 66  HIS   V O   1 
ATOM   38186 C  CB  . HIS   V  8  65  ? 12.564  -190.858 47.146  1.00 92.19  ? 66  HIS   V CB  1 
ATOM   38187 C  CG  . HIS   V  8  65  ? 13.331  -191.067 48.407  1.00 94.50  ? 66  HIS   V CG  1 
ATOM   38188 N  ND1 . HIS   V  8  65  ? 12.758  -190.904 49.654  1.00 94.77  ? 66  HIS   V ND1 1 
ATOM   38189 C  CD2 . HIS   V  8  65  ? 14.614  -191.426 48.620  1.00 96.21  ? 66  HIS   V CD2 1 
ATOM   38190 C  CE1 . HIS   V  8  65  ? 13.659  -191.149 50.582  1.00 95.29  ? 66  HIS   V CE1 1 
ATOM   38191 N  NE2 . HIS   V  8  65  ? 14.805  -191.471 49.973  1.00 95.23  ? 66  HIS   V NE2 1 
ATOM   38192 N  N   . SER   V  8  66  ? 9.749   -192.273 47.416  1.00 91.04  ? 67  SER   V N   1 
ATOM   38193 C  CA  . SER   V  8  66  ? 8.569   -192.782 48.167  1.00 94.66  ? 67  SER   V CA  1 
ATOM   38194 C  C   . SER   V  8  66  ? 8.291   -194.244 47.790  1.00 94.53  ? 67  SER   V C   1 
ATOM   38195 O  O   . SER   V  8  66  ? 8.126   -195.074 48.706  1.00 94.22  ? 67  SER   V O   1 
ATOM   38196 C  CB  . SER   V  8  66  ? 7.363   -191.914 47.914  1.00 95.14  ? 67  SER   V CB  1 
ATOM   38197 O  OG  . SER   V  8  66  ? 6.267   -192.319 48.715  1.00 100.87 ? 67  SER   V OG  1 
ATOM   38198 N  N   . LEU   V  8  67  ? 8.236   -194.533 46.486  1.00 94.61  ? 68  LEU   V N   1 
ATOM   38199 C  CA  . LEU   V  8  67  ? 8.022   -195.892 45.912  1.00 95.64  ? 68  LEU   V CA  1 
ATOM   38200 C  C   . LEU   V  8  67  ? 9.165   -196.833 46.323  1.00 95.45  ? 68  LEU   V C   1 
ATOM   38201 O  O   . LEU   V  8  67  ? 8.864   -197.994 46.664  1.00 94.80  ? 68  LEU   V O   1 
ATOM   38202 C  CB  . LEU   V  8  67  ? 7.913   -195.783 44.385  1.00 96.49  ? 68  LEU   V CB  1 
ATOM   38203 C  CG  . LEU   V  8  67  ? 6.501   -195.770 43.790  1.00 98.91  ? 68  LEU   V CG  1 
ATOM   38204 C  CD1 . LEU   V  8  67  ? 5.495   -195.049 44.679  1.00 99.08  ? 68  LEU   V CD1 1 
ATOM   38205 C  CD2 . LEU   V  8  67  ? 6.514   -195.141 42.404  1.00 99.85  ? 68  LEU   V CD2 1 
ATOM   38206 N  N   . TYR   V  8  68  ? 10.418  -196.360 46.297  1.00 95.55  ? 69  TYR   V N   1 
ATOM   38207 C  CA  . TYR   V  8  68  ? 11.636  -197.159 46.613  1.00 94.42  ? 69  TYR   V CA  1 
ATOM   38208 C  C   . TYR   V  8  68  ? 11.660  -197.540 48.098  1.00 95.03  ? 69  TYR   V C   1 
ATOM   38209 O  O   . TYR   V  8  68  ? 12.015  -198.689 48.402  1.00 96.93  ? 69  TYR   V O   1 
ATOM   38210 C  CB  . TYR   V  8  68  ? 12.918  -196.388 46.287  1.00 92.66  ? 69  TYR   V CB  1 
ATOM   38211 C  CG  . TYR   V  8  68  ? 14.197  -197.185 46.394  1.00 91.71  ? 69  TYR   V CG  1 
ATOM   38212 C  CD1 . TYR   V  8  68  ? 14.859  -197.339 47.604  1.00 92.00  ? 69  TYR   V CD1 1 
ATOM   38213 C  CD2 . TYR   V  8  68  ? 14.769  -197.761 45.271  1.00 92.24  ? 69  TYR   V CD2 1 
ATOM   38214 C  CE1 . TYR   V  8  68  ? 16.046  -198.049 47.696  1.00 91.94  ? 69  TYR   V CE1 1 
ATOM   38215 C  CE2 . TYR   V  8  68  ? 15.954  -198.474 45.345  1.00 91.84  ? 69  TYR   V CE2 1 
ATOM   38216 C  CZ  . TYR   V  8  68  ? 16.596  -198.621 46.561  1.00 92.06  ? 69  TYR   V CZ  1 
ATOM   38217 O  OH  . TYR   V  8  68  ? 17.761  -199.333 46.619  1.00 92.76  ? 69  TYR   V OH  1 
ATOM   38218 N  N   . THR   V  8  69  ? 11.333  -196.594 48.985  1.00 94.60  ? 70  THR   V N   1 
ATOM   38219 C  CA  . THR   V  8  69  ? 11.437  -196.740 50.464  1.00 96.01  ? 70  THR   V CA  1 
ATOM   38220 C  C   . THR   V  8  69  ? 10.128  -197.274 51.059  1.00 97.73  ? 70  THR   V C   1 
ATOM   38221 O  O   . THR   V  8  69  ? 10.126  -197.559 52.272  1.00 99.80  ? 70  THR   V O   1 
ATOM   38222 C  CB  . THR   V  8  69  ? 11.800  -195.408 51.133  1.00 94.91  ? 70  THR   V CB  1 
ATOM   38223 O  OG1 . THR   V  8  69  ? 10.758  -194.474 50.851  1.00 94.08  ? 70  THR   V OG1 1 
ATOM   38224 C  CG2 . THR   V  8  69  ? 13.126  -194.849 50.665  1.00 95.06  ? 70  THR   V CG2 1 
ATOM   38225 N  N   . SER   V  8  70  ? 9.064   -197.393 50.254  1.00 98.64  ? 71  SER   V N   1 
ATOM   38226 C  CA  . SER   V  8  70  ? 7.708   -197.818 50.695  1.00 99.63  ? 71  SER   V CA  1 
ATOM   38227 C  C   . SER   V  8  70  ? 7.253   -196.954 51.877  1.00 99.68  ? 71  SER   V C   1 
ATOM   38228 O  O   . SER   V  8  70  ? 6.671   -197.508 52.834  1.00 95.96  ? 71  SER   V O   1 
ATOM   38229 C  CB  . SER   V  8  70  ? 7.698   -199.279 51.043  1.00 99.90  ? 71  SER   V CB  1 
ATOM   38230 O  OG  . SER   V  8  70  ? 8.177   -200.048 49.952  1.00 101.78 ? 71  SER   V OG  1 
ATOM   38231 N  N   . ARG   V  8  71  ? 7.509   -195.645 51.796  1.00 101.76 ? 72  ARG   V N   1 
ATOM   38232 C  CA  . ARG   V  8  71  ? 7.280   -194.662 52.888  1.00 104.04 ? 72  ARG   V CA  1 
ATOM   38233 C  C   . ARG   V  8  71  ? 6.713   -193.364 52.312  1.00 105.63 ? 72  ARG   V C   1 
ATOM   38234 O  O   . ARG   V  8  71  ? 7.072   -193.014 51.170  1.00 108.96 ? 72  ARG   V O   1 
ATOM   38235 C  CB  . ARG   V  8  71  ? 8.587   -194.346 53.618  1.00 103.89 ? 72  ARG   V CB  1 
ATOM   38236 C  CG  . ARG   V  8  71  ? 8.887   -195.281 54.776  1.00 104.77 ? 72  ARG   V CG  1 
ATOM   38237 C  CD  . ARG   V  8  71  ? 10.262  -195.028 55.360  1.00 104.73 ? 72  ARG   V CD  1 
ATOM   38238 N  NE  . ARG   V  8  71  ? 10.503  -195.899 56.498  1.00 106.35 ? 72  ARG   V NE  1 
ATOM   38239 C  CZ  . ARG   V  8  71  ? 10.794  -197.192 56.415  1.00 106.50 ? 72  ARG   V CZ  1 
ATOM   38240 N  NH1 . ARG   V  8  71  ? 10.896  -197.788 55.238  1.00 105.31 ? 72  ARG   V NH1 1 
ATOM   38241 N  NH2 . ARG   V  8  71  ? 10.983  -197.888 57.521  1.00 110.56 ? 72  ARG   V NH2 1 
ATOM   38242 N  N   . GLU   V  8  72  ? 5.890   -192.668 53.098  1.00 109.22 ? 73  GLU   V N   1 
ATOM   38243 C  CA  . GLU   V  8  72  ? 5.388   -191.313 52.759  1.00 106.85 ? 73  GLU   V CA  1 
ATOM   38244 C  C   . GLU   V  8  72  ? 6.562   -190.344 52.827  1.00 103.38 ? 73  GLU   V C   1 
ATOM   38245 O  O   . GLU   V  8  72  ? 7.350   -190.385 53.771  1.00 95.28  ? 73  GLU   V O   1 
ATOM   38246 C  CB  . GLU   V  8  72  ? 4.250   -190.903 53.692  1.00 113.99 ? 73  GLU   V CB  1 
ATOM   38247 C  CG  . GLU   V  8  72  ? 3.044   -191.820 53.587  1.00 118.63 ? 73  GLU   V CG  1 
ATOM   38248 C  CD  . GLU   V  8  72  ? 1.710   -191.108 53.439  1.00 124.51 ? 73  GLU   V CD  1 
ATOM   38249 O  OE1 . GLU   V  8  72  ? 1.465   -190.148 54.198  1.00 129.40 ? 73  GLU   V OE1 1 
ATOM   38250 O  OE2 . GLU   V  8  72  ? 0.923   -191.510 52.556  1.00 129.31 ? 73  GLU   V OE2 1 
ATOM   38251 N  N   . PRO   V  8  73  ? 6.720   -189.457 51.820  1.00 99.29  ? 74  PRO   V N   1 
ATOM   38252 C  CA  . PRO   V  8  73  ? 7.869   -188.555 51.763  1.00 100.43 ? 74  PRO   V CA  1 
ATOM   38253 C  C   . PRO   V  8  73  ? 7.852   -187.536 52.911  1.00 98.90  ? 74  PRO   V C   1 
ATOM   38254 O  O   . PRO   V  8  73  ? 6.781   -187.219 53.406  1.00 99.77  ? 74  PRO   V O   1 
ATOM   38255 C  CB  . PRO   V  8  73  ? 7.718   -187.868 50.398  1.00 100.07 ? 74  PRO   V CB  1 
ATOM   38256 C  CG  . PRO   V  8  73  ? 6.232   -187.928 50.115  1.00 101.00 ? 74  PRO   V CG  1 
ATOM   38257 C  CD  . PRO   V  8  73  ? 5.787   -189.252 50.700  1.00 101.10 ? 74  PRO   V CD  1 
ATOM   38258 N  N   . ARG   V  8  74  ? 9.035   -187.056 53.300  1.00 97.61  ? 75  ARG   V N   1 
ATOM   38259 C  CA  . ARG   V  8  74  ? 9.220   -186.078 54.403  1.00 100.31 ? 75  ARG   V CA  1 
ATOM   38260 C  C   . ARG   V  8  74  ? 9.569   -184.705 53.822  1.00 99.70  ? 75  ARG   V C   1 
ATOM   38261 O  O   . ARG   V  8  74  ? 10.201  -184.650 52.746  1.00 100.40 ? 75  ARG   V O   1 
ATOM   38262 C  CB  . ARG   V  8  74  ? 10.304  -186.573 55.361  1.00 99.33  ? 75  ARG   V CB  1 
ATOM   38263 C  CG  . ARG   V  8  74  ? 9.992   -187.933 55.964  1.00 99.09  ? 75  ARG   V CG  1 
ATOM   38264 C  CD  . ARG   V  8  74  ? 10.986  -188.326 57.033  1.00 99.75  ? 75  ARG   V CD  1 
ATOM   38265 N  NE  . ARG   V  8  74  ? 10.646  -189.614 57.616  1.00 101.06 ? 75  ARG   V NE  1 
ATOM   38266 C  CZ  . ARG   V  8  74  ? 11.290  -190.182 58.628  1.00 100.68 ? 75  ARG   V CZ  1 
ATOM   38267 N  NH1 . ARG   V  8  74  ? 12.323  -189.575 59.189  1.00 102.14 ? 75  ARG   V NH1 1 
ATOM   38268 N  NH2 . ARG   V  8  74  ? 10.892  -191.357 59.080  1.00 102.10 ? 75  ARG   V NH2 1 
ATOM   38269 N  N   . VAL   V  8  75  ? 9.167   -183.639 54.520  1.00 99.81  ? 76  VAL   V N   1 
ATOM   38270 C  CA  . VAL   V  8  75  ? 9.357   -182.229 54.070  1.00 97.35  ? 76  VAL   V CA  1 
ATOM   38271 C  C   . VAL   V  8  75  ? 10.861  -181.936 54.037  1.00 94.11  ? 76  VAL   V C   1 
ATOM   38272 O  O   . VAL   V  8  75  ? 11.298  -181.249 53.094  1.00 94.14  ? 76  VAL   V O   1 
ATOM   38273 C  CB  . VAL   V  8  75  ? 8.578   -181.235 54.956  1.00 98.19  ? 76  VAL   V CB  1 
ATOM   38274 C  CG1 . VAL   V  8  75  ? 8.792   -179.794 54.515  1.00 97.72  ? 76  VAL   V CG1 1 
ATOM   38275 C  CG2 . VAL   V  8  75  ? 7.088   -181.552 54.986  1.00 98.95  ? 76  VAL   V CG2 1 
ATOM   38276 N  N   . VAL   V  8  76  ? 11.620  -182.467 55.001  1.00 92.67  ? 77  VAL   V N   1 
ATOM   38277 C  CA  . VAL   V  8  76  ? 13.095  -182.250 55.119  1.00 93.37  ? 77  VAL   V CA  1 
ATOM   38278 C  C   . VAL   V  8  76  ? 13.822  -182.863 53.914  1.00 95.59  ? 77  VAL   V C   1 
ATOM   38279 O  O   . VAL   V  8  76  ? 14.896  -182.334 53.566  1.00 98.36  ? 77  VAL   V O   1 
ATOM   38280 C  CB  . VAL   V  8  76  ? 13.665  -182.793 56.443  1.00 95.78  ? 77  VAL   V CB  1 
ATOM   38281 C  CG1 . VAL   V  8  76  ? 13.198  -181.962 57.627  1.00 95.94  ? 77  VAL   V CG1 1 
ATOM   38282 C  CG2 . VAL   V  8  76  ? 13.358  -184.269 56.655  1.00 95.24  ? 77  VAL   V CG2 1 
ATOM   38283 N  N   . SER   V  8  77  ? 13.286  -183.934 53.314  1.00 94.64  ? 78  SER   V N   1 
ATOM   38284 C  CA  . SER   V  8  77  ? 13.861  -184.580 52.103  1.00 95.44  ? 78  SER   V CA  1 
ATOM   38285 C  C   . SER   V  8  77  ? 13.715  -183.633 50.908  1.00 96.09  ? 78  SER   V C   1 
ATOM   38286 O  O   . SER   V  8  77  ? 14.725  -183.388 50.223  1.00 101.12 ? 78  SER   V O   1 
ATOM   38287 C  CB  . SER   V  8  77  ? 13.236  -185.920 51.817  1.00 94.70  ? 78  SER   V CB  1 
ATOM   38288 O  OG  . SER   V  8  77  ? 13.506  -186.846 52.860  1.00 95.71  ? 78  SER   V OG  1 
ATOM   38289 N  N   . ALA   V  8  78  ? 12.505  -183.112 50.682  1.00 95.31  ? 79  ALA   V N   1 
ATOM   38290 C  CA  . ALA   V  8  78  ? 12.206  -182.101 49.641  1.00 95.70  ? 79  ALA   V CA  1 
ATOM   38291 C  C   . ALA   V  8  78  ? 13.070  -180.855 49.885  1.00 95.13  ? 79  ALA   V C   1 
ATOM   38292 O  O   . ALA   V  8  78  ? 13.610  -180.310 48.901  1.00 95.67  ? 79  ALA   V O   1 
ATOM   38293 C  CB  . ALA   V  8  78  ? 10.731  -181.774 49.637  1.00 93.60  ? 79  ALA   V CB  1 
ATOM   38294 N  N   . LEU   V  8  79  ? 13.213  -180.443 51.150  1.00 94.05  ? 80  LEU   V N   1 
ATOM   38295 C  CA  . LEU   V  8  79  ? 13.999  -179.249 51.568  1.00 93.83  ? 80  LEU   V CA  1 
ATOM   38296 C  C   . LEU   V  8  79  ? 15.475  -179.462 51.215  1.00 92.44  ? 80  LEU   V C   1 
ATOM   38297 O  O   . LEU   V  8  79  ? 16.090  -178.535 50.654  1.00 95.69  ? 80  LEU   V O   1 
ATOM   38298 C  CB  . LEU   V  8  79  ? 13.822  -179.016 53.073  1.00 94.63  ? 80  LEU   V CB  1 
ATOM   38299 C  CG  . LEU   V  8  79  ? 14.461  -177.742 53.626  1.00 94.11  ? 80  LEU   V CG  1 
ATOM   38300 C  CD1 . LEU   V  8  79  ? 13.669  -176.516 53.205  1.00 94.74  ? 80  LEU   V CD1 1 
ATOM   38301 C  CD2 . LEU   V  8  79  ? 14.574  -177.800 55.141  1.00 95.06  ? 80  LEU   V CD2 1 
ATOM   38302 N  N   . GLN   V  8  80  ? 16.018  -180.638 51.536  1.00 89.15  ? 81  GLN   V N   1 
ATOM   38303 C  CA  . GLN   V  8  80  ? 17.446  -180.977 51.305  1.00 88.09  ? 81  GLN   V CA  1 
ATOM   38304 C  C   . GLN   V  8  80  ? 17.711  -181.030 49.796  1.00 88.74  ? 81  GLN   V C   1 
ATOM   38305 O  O   . GLN   V  8  80  ? 18.730  -180.463 49.353  1.00 85.98  ? 81  GLN   V O   1 
ATOM   38306 C  CB  . GLN   V  8  80  ? 17.796  -182.306 51.974  1.00 88.77  ? 81  GLN   V CB  1 
ATOM   38307 C  CG  . GLN   V  8  80  ? 19.293  -182.542 52.111  1.00 88.08  ? 81  GLN   V CG  1 
ATOM   38308 C  CD  . GLN   V  8  80  ? 19.884  -181.828 53.302  1.00 87.39  ? 81  GLN   V CD  1 
ATOM   38309 O  OE1 . GLN   V  8  80  ? 19.333  -180.852 53.806  1.00 85.71  ? 81  GLN   V OE1 1 
ATOM   38310 N  NE2 . GLN   V  8  80  ? 21.021  -182.322 53.766  1.00 87.05  ? 81  GLN   V NE2 1 
ATOM   38311 N  N   . MET   V  8  81  ? 16.819  -181.680 49.044  1.00 89.22  ? 82  MET   V N   1 
ATOM   38312 C  CA  . MET   V  8  81  ? 16.976  -181.928 47.586  1.00 91.55  ? 82  MET   V CA  1 
ATOM   38313 C  C   . MET   V  8  81  ? 16.881  -180.603 46.826  1.00 89.48  ? 82  MET   V C   1 
ATOM   38314 O  O   . MET   V  8  81  ? 17.695  -180.411 45.901  1.00 89.94  ? 82  MET   V O   1 
ATOM   38315 C  CB  . MET   V  8  81  ? 15.912  -182.904 47.073  1.00 93.54  ? 82  MET   V CB  1 
ATOM   38316 C  CG  . MET   V  8  81  ? 16.145  -184.332 47.536  1.00 96.74  ? 82  MET   V CG  1 
ATOM   38317 S  SD  . MET   V  8  81  ? 14.678  -185.386 47.360  1.00 97.89  ? 82  MET   V SD  1 
ATOM   38318 C  CE  . MET   V  8  81  ? 14.648  -185.623 45.586  1.00 96.28  ? 82  MET   V CE  1 
ATOM   38319 N  N   . LEU   V  8  82  ? 15.938  -179.730 47.208  1.00 90.64  ? 83  LEU   V N   1 
ATOM   38320 C  CA  . LEU   V  8  82  ? 15.761  -178.376 46.610  1.00 87.70  ? 83  LEU   V CA  1 
ATOM   38321 C  C   . LEU   V  8  82  ? 17.022  -177.544 46.872  1.00 83.27  ? 83  LEU   V C   1 
ATOM   38322 O  O   . LEU   V  8  82  ? 17.587  -177.029 45.894  1.00 81.80  ? 83  LEU   V O   1 
ATOM   38323 C  CB  . LEU   V  8  82  ? 14.515  -177.692 47.187  1.00 87.67  ? 83  LEU   V CB  1 
ATOM   38324 C  CG  . LEU   V  8  82  ? 13.175  -178.167 46.624  1.00 89.76  ? 83  LEU   V CG  1 
ATOM   38325 C  CD1 . LEU   V  8  82  ? 12.016  -177.678 47.479  1.00 90.07  ? 83  LEU   V CD1 1 
ATOM   38326 C  CD2 . LEU   V  8  82  ? 12.992  -177.714 45.183  1.00 90.58  ? 83  LEU   V CD2 1 
ATOM   38327 N  N   . LYS   V  8  83  ? 17.464  -177.457 48.131  1.00 83.70  ? 84  LYS   V N   1 
ATOM   38328 C  CA  . LYS   V  8  83  ? 18.554  -176.538 48.562  1.00 85.00  ? 84  LYS   V CA  1 
ATOM   38329 C  C   . LYS   V  8  83  ? 19.886  -176.948 47.919  1.00 85.91  ? 84  LYS   V C   1 
ATOM   38330 O  O   . LYS   V  8  83  ? 20.681  -176.047 47.599  1.00 84.06  ? 84  LYS   V O   1 
ATOM   38331 C  CB  . LYS   V  8  83  ? 18.672  -176.482 50.089  1.00 87.69  ? 84  LYS   V CB  1 
ATOM   38332 C  CG  . LYS   V  8  83  ? 19.366  -177.662 50.759  1.00 88.57  ? 84  LYS   V CG  1 
ATOM   38333 C  CD  . LYS   V  8  83  ? 20.301  -177.251 51.876  1.00 91.55  ? 84  LYS   V CD  1 
ATOM   38334 C  CE  . LYS   V  8  83  ? 19.580  -176.560 53.012  1.00 92.00  ? 84  LYS   V CE  1 
ATOM   38335 N  NZ  . LYS   V  8  83  ? 20.507  -176.121 54.079  1.00 93.27  ? 84  LYS   V NZ  1 
ATOM   38336 N  N   . GLN   V  8  84  ? 20.126  -178.249 47.743  1.00 85.96  ? 85  GLN   V N   1 
ATOM   38337 C  CA  . GLN   V  8  84  ? 21.402  -178.777 47.189  1.00 86.21  ? 85  GLN   V CA  1 
ATOM   38338 C  C   . GLN   V  8  84  ? 21.424  -178.557 45.673  1.00 85.71  ? 85  GLN   V C   1 
ATOM   38339 O  O   . GLN   V  8  84  ? 22.528  -178.361 45.127  1.00 85.02  ? 85  GLN   V O   1 
ATOM   38340 C  CB  . GLN   V  8  84  ? 21.587  -180.250 47.554  1.00 84.85  ? 85  GLN   V CB  1 
ATOM   38341 C  CG  . GLN   V  8  84  ? 22.014  -180.447 49.001  1.00 85.21  ? 85  GLN   V CG  1 
ATOM   38342 C  CD  . GLN   V  8  84  ? 22.233  -181.893 49.375  1.00 85.31  ? 85  GLN   V CD  1 
ATOM   38343 O  OE1 . GLN   V  8  84  ? 22.131  -182.796 48.548  1.00 81.83  ? 85  GLN   V OE1 1 
ATOM   38344 N  NE2 . GLN   V  8  84  ? 22.545  -182.121 50.642  1.00 83.79  ? 85  GLN   V NE2 1 
ATOM   38345 N  N   . HIS   V  8  85  ? 20.252  -178.590 45.029  1.00 86.37  ? 86  HIS   V N   1 
ATOM   38346 C  CA  . HIS   V  8  85  ? 20.067  -178.295 43.583  1.00 88.35  ? 86  HIS   V CA  1 
ATOM   38347 C  C   . HIS   V  8  85  ? 20.293  -176.800 43.337  1.00 88.95  ? 86  HIS   V C   1 
ATOM   38348 O  O   . HIS   V  8  85  ? 21.062  -176.459 42.416  1.00 93.99  ? 86  HIS   V O   1 
ATOM   38349 C  CB  . HIS   V  8  85  ? 18.678  -178.746 43.107  1.00 87.37  ? 86  HIS   V CB  1 
ATOM   38350 C  CG  . HIS   V  8  85  ? 18.458  -178.558 41.643  1.00 89.70  ? 86  HIS   V CG  1 
ATOM   38351 N  ND1 . HIS   V  8  85  ? 18.998  -179.410 40.698  1.00 89.29  ? 86  HIS   V ND1 1 
ATOM   38352 C  CD2 . HIS   V  8  85  ? 17.768  -177.621 40.956  1.00 90.21  ? 86  HIS   V CD2 1 
ATOM   38353 C  CE1 . HIS   V  8  85  ? 18.648  -179.008 39.494  1.00 90.38  ? 86  HIS   V CE1 1 
ATOM   38354 N  NE2 . HIS   V  8  85  ? 17.892  -177.912 39.624  1.00 92.36  ? 86  HIS   V NE2 1 
ATOM   38355 N  N   . LEU   V  8  86  ? 19.645  -175.946 44.135  1.00 85.62  ? 87  LEU   V N   1 
ATOM   38356 C  CA  . LEU   V  8  86  ? 19.709  -174.468 43.994  1.00 82.59  ? 87  LEU   V CA  1 
ATOM   38357 C  C   . LEU   V  8  86  ? 21.134  -173.986 44.286  1.00 83.86  ? 87  LEU   V C   1 
ATOM   38358 O  O   . LEU   V  8  86  ? 21.617  -173.129 43.519  1.00 84.53  ? 87  LEU   V O   1 
ATOM   38359 C  CB  . LEU   V  8  86  ? 18.678  -173.820 44.925  1.00 79.69  ? 87  LEU   V CB  1 
ATOM   38360 C  CG  . LEU   V  8  86  ? 17.225  -173.940 44.469  1.00 80.97  ? 87  LEU   V CG  1 
ATOM   38361 C  CD1 . LEU   V  8  86  ? 16.283  -173.328 45.493  1.00 79.98  ? 87  LEU   V CD1 1 
ATOM   38362 C  CD2 . LEU   V  8  86  ? 17.018  -173.284 43.110  1.00 83.50  ? 87  LEU   V CD2 1 
ATOM   38363 N  N   . PHE   V  8  87  ? 21.783  -174.527 45.326  1.00 82.93  ? 88  PHE   V N   1 
ATOM   38364 C  CA  . PHE   V  8  87  ? 23.165  -174.160 45.739  1.00 84.43  ? 88  PHE   V CA  1 
ATOM   38365 C  C   . PHE   V  8  87  ? 24.157  -174.487 44.621  1.00 84.21  ? 88  PHE   V C   1 
ATOM   38366 O  O   . PHE   V  8  87  ? 25.104  -173.711 44.391  1.00 83.63  ? 88  PHE   V O   1 
ATOM   38367 C  CB  . PHE   V  8  87  ? 23.616  -174.897 47.002  1.00 83.25  ? 88  PHE   V CB  1 
ATOM   38368 C  CG  . PHE   V  8  87  ? 25.003  -174.504 47.443  1.00 83.80  ? 88  PHE   V CG  1 
ATOM   38369 C  CD1 . PHE   V  8  87  ? 25.204  -173.356 48.193  1.00 85.56  ? 88  PHE   V CD1 1 
ATOM   38370 C  CD2 . PHE   V  8  87  ? 26.112  -175.243 47.061  1.00 82.44  ? 88  PHE   V CD2 1 
ATOM   38371 C  CE1 . PHE   V  8  87  ? 26.479  -172.977 48.580  1.00 85.07  ? 88  PHE   V CE1 1 
ATOM   38372 C  CE2 . PHE   V  8  87  ? 27.387  -174.862 47.450  1.00 82.45  ? 88  PHE   V CE2 1 
ATOM   38373 C  CZ  . PHE   V  8  87  ? 27.569  -173.731 48.210  1.00 82.42  ? 88  PHE   V CZ  1 
ATOM   38374 N  N   . LYS   V  8  88  ? 23.955  -175.635 43.975  1.00 86.65  ? 89  LYS   V N   1 
ATOM   38375 C  CA  . LYS   V  8  88  ? 24.799  -176.144 42.865  1.00 89.94  ? 89  LYS   V CA  1 
ATOM   38376 C  C   . LYS   V  8  88  ? 24.804  -175.150 41.700  1.00 87.98  ? 89  LYS   V C   1 
ATOM   38377 O  O   . LYS   V  8  88  ? 25.812  -175.132 40.970  1.00 84.17  ? 89  LYS   V O   1 
ATOM   38378 C  CB  . LYS   V  8  88  ? 24.269  -177.499 42.395  1.00 96.02  ? 89  LYS   V CB  1 
ATOM   38379 C  CG  . LYS   V  8  88  ? 25.113  -178.202 41.344  1.00 103.12 ? 89  LYS   V CG  1 
ATOM   38380 C  CD  . LYS   V  8  88  ? 24.651  -179.619 41.074  1.00 111.97 ? 89  LYS   V CD  1 
ATOM   38381 C  CE  . LYS   V  8  88  ? 23.323  -179.682 40.347  1.00 117.33 ? 89  LYS   V CE  1 
ATOM   38382 N  NZ  . LYS   V  8  88  ? 22.737  -181.044 40.383  1.00 120.18 ? 89  LYS   V NZ  1 
ATOM   38383 N  N   . TYR   V  8  89  ? 23.721  -174.379 41.532  1.00 91.93  ? 90  TYR   V N   1 
ATOM   38384 C  CA  . TYR   V  8  89  ? 23.523  -173.405 40.422  1.00 94.78  ? 90  TYR   V CA  1 
ATOM   38385 C  C   . TYR   V  8  89  ? 23.785  -171.962 40.884  1.00 93.67  ? 90  TYR   V C   1 
ATOM   38386 O  O   . TYR   V  8  89  ? 23.448  -171.033 40.129  1.00 89.80  ? 90  TYR   V O   1 
ATOM   38387 C  CB  . TYR   V  8  89  ? 22.123  -173.573 39.825  1.00 97.47  ? 90  TYR   V CB  1 
ATOM   38388 C  CG  . TYR   V  8  89  ? 22.029  -174.710 38.842  1.00 98.34  ? 90  TYR   V CG  1 
ATOM   38389 C  CD1 . TYR   V  8  89  ? 22.236  -174.498 37.489  1.00 98.55  ? 90  TYR   V CD1 1 
ATOM   38390 C  CD2 . TYR   V  8  89  ? 21.774  -176.005 39.264  1.00 99.96  ? 90  TYR   V CD2 1 
ATOM   38391 C  CE1 . TYR   V  8  89  ? 22.170  -175.539 36.577  1.00 100.01 ? 90  TYR   V CE1 1 
ATOM   38392 C  CE2 . TYR   V  8  89  ? 21.705  -177.058 38.366  1.00 101.53 ? 90  TYR   V CE2 1 
ATOM   38393 C  CZ  . TYR   V  8  89  ? 21.903  -176.823 37.017  1.00 100.84 ? 90  TYR   V CZ  1 
ATOM   38394 O  OH  . TYR   V  8  89  ? 21.836  -177.848 36.120  1.00 104.23 ? 90  TYR   V OH  1 
ATOM   38395 N  N   . GLN   V  8  90  ? 24.368  -171.781 42.073  1.00 92.23  ? 91  GLN   V N   1 
ATOM   38396 C  CA  . GLN   V  8  90  ? 24.917  -170.489 42.565  1.00 92.66  ? 91  GLN   V CA  1 
ATOM   38397 C  C   . GLN   V  8  90  ? 23.942  -169.336 42.272  1.00 95.42  ? 91  GLN   V C   1 
ATOM   38398 O  O   . GLN   V  8  90  ? 24.412  -168.261 41.848  1.00 101.25 ? 91  GLN   V O   1 
ATOM   38399 C  CB  . GLN   V  8  90  ? 26.282  -170.243 41.917  1.00 94.14  ? 91  GLN   V CB  1 
ATOM   38400 C  CG  . GLN   V  8  90  ? 27.369  -171.193 42.400  1.00 96.84  ? 91  GLN   V CG  1 
ATOM   38401 C  CD  . GLN   V  8  90  ? 27.780  -170.930 43.830  1.00 100.55 ? 91  GLN   V CD  1 
ATOM   38402 O  OE1 . GLN   V  8  90  ? 28.020  -169.793 44.235  1.00 106.90 ? 91  GLN   V OE1 1 
ATOM   38403 N  NE2 . GLN   V  8  90  ? 27.881  -171.989 44.614  1.00 100.97 ? 91  GLN   V NE2 1 
ATOM   38404 N  N   . GLY   V  8  91  ? 22.638  -169.553 42.483  1.00 93.27  ? 92  GLY   V N   1 
ATOM   38405 C  CA  . GLY   V  8  91  ? 21.602  -168.503 42.419  1.00 91.11  ? 92  GLY   V CA  1 
ATOM   38406 C  C   . GLY   V  8  91  ? 21.056  -168.272 41.017  1.00 89.42  ? 92  GLY   V C   1 
ATOM   38407 O  O   . GLY   V  8  91  ? 20.059  -167.535 40.907  1.00 91.36  ? 92  GLY   V O   1 
ATOM   38408 N  N   . HIS   V  8  92  ? 21.657  -168.873 39.983  1.00 86.77  ? 93  HIS   V N   1 
ATOM   38409 C  CA  . HIS   V  8  92  ? 21.278  -168.660 38.558  1.00 85.28  ? 93  HIS   V CA  1 
ATOM   38410 C  C   . HIS   V  8  92  ? 19.873  -169.209 38.296  1.00 85.76  ? 93  HIS   V C   1 
ATOM   38411 O  O   . HIS   V  8  92  ? 19.199  -168.677 37.401  1.00 93.72  ? 93  HIS   V O   1 
ATOM   38412 C  CB  . HIS   V  8  92  ? 22.317  -169.260 37.603  1.00 85.29  ? 93  HIS   V CB  1 
ATOM   38413 C  CG  . HIS   V  8  92  ? 23.604  -168.509 37.588  1.00 86.37  ? 93  HIS   V CG  1 
ATOM   38414 N  ND1 . HIS   V  8  92  ? 23.729  -167.279 36.973  1.00 88.17  ? 93  HIS   V ND1 1 
ATOM   38415 C  CD2 . HIS   V  8  92  ? 24.814  -168.801 38.111  1.00 83.76  ? 93  HIS   V CD2 1 
ATOM   38416 C  CE1 . HIS   V  8  92  ? 24.965  -166.845 37.118  1.00 90.35  ? 93  HIS   V CE1 1 
ATOM   38417 N  NE2 . HIS   V  8  92  ? 25.652  -167.765 37.811  1.00 87.42  ? 93  HIS   V NE2 1 
ATOM   38418 N  N   . ILE   V  8  93  ? 19.456  -170.239 39.034  1.00 82.35  ? 94  ILE   V N   1 
ATOM   38419 C  CA  . ILE   V  8  93  ? 18.032  -170.679 39.107  1.00 84.23  ? 94  ILE   V CA  1 
ATOM   38420 C  C   . ILE   V  8  93  ? 17.352  -169.822 40.177  1.00 80.95  ? 94  ILE   V C   1 
ATOM   38421 O  O   . ILE   V  8  93  ? 17.527  -170.115 41.378  1.00 79.84  ? 94  ILE   V O   1 
ATOM   38422 C  CB  . ILE   V  8  93  ? 17.917  -172.192 39.380  1.00 84.37  ? 94  ILE   V CB  1 
ATOM   38423 C  CG1 . ILE   V  8  93  ? 18.514  -172.997 38.221  1.00 87.44  ? 94  ILE   V CG1 1 
ATOM   38424 C  CG2 . ILE   V  8  93  ? 16.473  -172.586 39.657  1.00 83.68  ? 94  ILE   V CG2 1 
ATOM   38425 C  CD1 . ILE   V  8  93  ? 18.566  -174.493 38.446  1.00 88.38  ? 94  ILE   V CD1 1 
ATOM   38426 N  N   . GLY   V  8  94  ? 16.632  -168.787 39.738  1.00 80.47  ? 95  GLY   V N   1 
ATOM   38427 C  CA  . GLY   V  8  94  ? 16.003  -167.775 40.604  1.00 82.37  ? 95  GLY   V CA  1 
ATOM   38428 C  C   . GLY   V  8  94  ? 14.682  -168.262 41.164  1.00 82.28  ? 95  GLY   V C   1 
ATOM   38429 O  O   . GLY   V  8  94  ? 13.640  -167.644 40.855  1.00 83.65  ? 95  GLY   V O   1 
ATOM   38430 N  N   . ALA   V  8  95  ? 14.726  -169.332 41.957  1.00 83.07  ? 96  ALA   V N   1 
ATOM   38431 C  CA  . ALA   V  8  95  ? 13.574  -169.872 42.711  1.00 83.27  ? 96  ALA   V CA  1 
ATOM   38432 C  C   . ALA   V  8  95  ? 13.704  -169.430 44.173  1.00 80.91  ? 96  ALA   V C   1 
ATOM   38433 O  O   . ALA   V  8  95  ? 14.761  -169.673 44.779  1.00 80.35  ? 96  ALA   V O   1 
ATOM   38434 C  CB  . ALA   V  8  95  ? 13.519  -171.374 42.573  1.00 84.55  ? 96  ALA   V CB  1 
ATOM   38435 N  N   . TYR   V  8  96  ? 12.681  -168.752 44.691  1.00 80.84  ? 97  TYR   V N   1 
ATOM   38436 C  CA  . TYR   V  8  96  ? 12.504  -168.446 46.132  1.00 83.52  ? 97  TYR   V CA  1 
ATOM   38437 C  C   . TYR   V  8  96  ? 11.228  -169.154 46.591  1.00 83.51  ? 97  TYR   V C   1 
ATOM   38438 O  O   . TYR   V  8  96  ? 10.140  -168.783 46.120  1.00 84.61  ? 97  TYR   V O   1 
ATOM   38439 C  CB  . TYR   V  8  96  ? 12.479  -166.933 46.357  1.00 85.74  ? 97  TYR   V CB  1 
ATOM   38440 C  CG  . TYR   V  8  96  ? 13.729  -166.236 45.885  1.00 88.99  ? 97  TYR   V CG  1 
ATOM   38441 C  CD1 . TYR   V  8  96  ? 13.873  -165.854 44.560  1.00 91.13  ? 97  TYR   V CD1 1 
ATOM   38442 C  CD2 . TYR   V  8  96  ? 14.780  -165.980 46.752  1.00 88.33  ? 97  TYR   V CD2 1 
ATOM   38443 C  CE1 . TYR   V  8  96  ? 15.021  -165.222 44.112  1.00 94.32  ? 97  TYR   V CE1 1 
ATOM   38444 C  CE2 . TYR   V  8  96  ? 15.935  -165.347 46.321  1.00 91.28  ? 97  TYR   V CE2 1 
ATOM   38445 C  CZ  . TYR   V  8  96  ? 16.057  -164.969 44.995  1.00 93.16  ? 97  TYR   V CZ  1 
ATOM   38446 O  OH  . TYR   V  8  96  ? 17.193  -164.351 44.555  1.00 97.07  ? 97  TYR   V OH  1 
ATOM   38447 N  N   . LEU   V  8  97  ? 11.370  -170.161 47.455  1.00 82.57  ? 98  LEU   V N   1 
ATOM   38448 C  CA  . LEU   V  8  97  ? 10.290  -171.126 47.785  1.00 85.44  ? 98  LEU   V CA  1 
ATOM   38449 C  C   . LEU   V  8  97  ? 9.977   -171.078 49.283  1.00 84.58  ? 98  LEU   V C   1 
ATOM   38450 O  O   . LEU   V  8  97  ? 10.919  -170.922 50.082  1.00 81.38  ? 98  LEU   V O   1 
ATOM   38451 C  CB  . LEU   V  8  97  ? 10.738  -172.533 47.381  1.00 86.52  ? 98  LEU   V CB  1 
ATOM   38452 C  CG  . LEU   V  8  97  ? 11.207  -172.698 45.936  1.00 86.71  ? 98  LEU   V CG  1 
ATOM   38453 C  CD1 . LEU   V  8  97  ? 11.943  -174.014 45.757  1.00 87.96  ? 98  LEU   V CD1 1 
ATOM   38454 C  CD2 . LEU   V  8  97  ? 10.039  -172.605 44.966  1.00 88.51  ? 98  LEU   V CD2 1 
ATOM   38455 N  N   . ILE   V  8  98  ? 8.693   -171.211 49.625  1.00 86.50  ? 99  ILE   V N   1 
ATOM   38456 C  CA  . ILE   V  8  98  ? 8.202   -171.584 50.983  1.00 86.66  ? 99  ILE   V CA  1 
ATOM   38457 C  C   . ILE   V  8  98  ? 7.716   -173.034 50.904  1.00 88.48  ? 99  ILE   V C   1 
ATOM   38458 O  O   . ILE   V  8  98  ? 6.690   -173.270 50.238  1.00 90.42  ? 99  ILE   V O   1 
ATOM   38459 C  CB  . ILE   V  8  98  ? 7.104   -170.617 51.471  1.00 86.94  ? 99  ILE   V CB  1 
ATOM   38460 C  CG1 . ILE   V  8  98  ? 7.704   -169.247 51.802  1.00 85.13  ? 99  ILE   V CG1 1 
ATOM   38461 C  CG2 . ILE   V  8  98  ? 6.338   -171.213 52.646  1.00 88.27  ? 99  ILE   V CG2 1 
ATOM   38462 C  CD1 . ILE   V  8  98  ? 6.746   -168.269 52.444  1.00 85.91  ? 99  ILE   V CD1 1 
ATOM   38463 N  N   . VAL   V  8  99  ? 8.446   -173.955 51.541  1.00 88.63  ? 100 VAL   V N   1 
ATOM   38464 C  CA  . VAL   V  8  99  ? 8.165   -175.423 51.545  1.00 88.32  ? 100 VAL   V CA  1 
ATOM   38465 C  C   . VAL   V  8  99  ? 7.439   -175.763 52.848  1.00 84.00  ? 100 VAL   V C   1 
ATOM   38466 O  O   . VAL   V  8  99  ? 7.968   -175.419 53.919  1.00 84.11  ? 100 VAL   V O   1 
ATOM   38467 C  CB  . VAL   V  8  99  ? 9.457   -176.250 51.399  1.00 86.71  ? 100 VAL   V CB  1 
ATOM   38468 C  CG1 . VAL   V  8  99  ? 9.156   -177.714 51.139  1.00 87.59  ? 100 VAL   V CG1 1 
ATOM   38469 C  CG2 . VAL   V  8  99  ? 10.363  -175.703 50.309  1.00 88.34  ? 100 VAL   V CG2 1 
ATOM   38470 N  N   . ALA   V  8  100 ? 6.275   -176.408 52.753  1.00 84.55  ? 101 ALA   V N   1 
ATOM   38471 C  CA  . ALA   V  8  100 ? 5.446   -176.816 53.910  1.00 87.41  ? 101 ALA   V CA  1 
ATOM   38472 C  C   . ALA   V  8  100 ? 4.778   -178.166 53.632  1.00 89.58  ? 101 ALA   V C   1 
ATOM   38473 O  O   . ALA   V  8  100 ? 4.718   -178.580 52.459  1.00 91.70  ? 101 ALA   V O   1 
ATOM   38474 C  CB  . ALA   V  8  100 ? 4.426   -175.746 54.205  1.00 88.07  ? 101 ALA   V CB  1 
ATOM   38475 N  N   . GLY   V  8  101 ? 4.306   -178.829 54.689  1.00 89.09  ? 102 GLY   V N   1 
ATOM   38476 C  CA  . GLY   V  8  101 ? 3.530   -180.077 54.586  1.00 90.93  ? 102 GLY   V CA  1 
ATOM   38477 C  C   . GLY   V  8  101 ? 3.569   -180.883 55.866  1.00 92.40  ? 102 GLY   V C   1 
ATOM   38478 O  O   . GLY   V  8  101 ? 4.226   -180.444 56.831  1.00 90.28  ? 102 GLY   V O   1 
ATOM   38479 N  N   . VAL   V  8  102 ? 2.878   -182.025 55.858  1.00 96.01  ? 103 VAL   V N   1 
ATOM   38480 C  CA  . VAL   V  8  102 ? 2.804   -182.992 56.990  1.00 98.65  ? 103 VAL   V CA  1 
ATOM   38481 C  C   . VAL   V  8  102 ? 3.386   -184.327 56.512  1.00 102.31 ? 103 VAL   V C   1 
ATOM   38482 O  O   . VAL   V  8  102 ? 3.224   -184.656 55.319  1.00 103.46 ? 103 VAL   V O   1 
ATOM   38483 C  CB  . VAL   V  8  102 ? 1.362   -183.135 57.520  1.00 97.54  ? 103 VAL   V CB  1 
ATOM   38484 C  CG1 . VAL   V  8  102 ? 0.867   -181.836 58.133  1.00 96.76  ? 103 VAL   V CG1 1 
ATOM   38485 C  CG2 . VAL   V  8  102 ? 0.387   -183.619 56.455  1.00 97.67  ? 103 VAL   V CG2 1 
ATOM   38486 N  N   . ASP   V  8  103 ? 4.060   -185.043 57.413  1.00 106.11 ? 104 ASP   V N   1 
ATOM   38487 C  CA  . ASP   V  8  103 ? 4.683   -186.369 57.154  1.00 111.16 ? 104 ASP   V CA  1 
ATOM   38488 C  C   . ASP   V  8  103 ? 4.659   -187.163 58.459  1.00 113.65 ? 104 ASP   V C   1 
ATOM   38489 O  O   . ASP   V  8  103 ? 4.276   -186.628 59.499  1.00 107.67 ? 104 ASP   V O   1 
ATOM   38490 C  CB  . ASP   V  8  103 ? 6.083   -186.185 56.554  1.00 111.29 ? 104 ASP   V CB  1 
ATOM   38491 C  CG  . ASP   V  8  103 ? 7.018   -185.341 57.403  1.00 108.71 ? 104 ASP   V CG  1 
ATOM   38492 O  OD1 . ASP   V  8  103 ? 7.068   -185.575 58.624  1.00 108.76 ? 104 ASP   V OD1 1 
ATOM   38493 O  OD2 . ASP   V  8  103 ? 7.687   -184.455 56.835  1.00 103.81 ? 104 ASP   V OD2 1 
ATOM   38494 N  N   . PRO   V  8  104 ? 5.044   -188.460 58.457  1.00 115.60 ? 105 PRO   V N   1 
ATOM   38495 C  CA  . PRO   V  8  104 ? 5.104   -189.243 59.695  1.00 116.99 ? 105 PRO   V CA  1 
ATOM   38496 C  C   . PRO   V  8  104 ? 5.786   -188.534 60.880  1.00 114.78 ? 105 PRO   V C   1 
ATOM   38497 O  O   . PRO   V  8  104 ? 5.443   -188.848 62.006  1.00 118.62 ? 105 PRO   V O   1 
ATOM   38498 C  CB  . PRO   V  8  104 ? 5.901   -190.487 59.267  1.00 117.80 ? 105 PRO   V CB  1 
ATOM   38499 C  CG  . PRO   V  8  104 ? 5.544   -190.665 57.805  1.00 119.06 ? 105 PRO   V CG  1 
ATOM   38500 C  CD  . PRO   V  8  104 ? 5.387   -189.258 57.268  1.00 117.93 ? 105 PRO   V CD  1 
ATOM   38501 N  N   . THR   V  8  105 ? 6.707   -187.599 60.611  1.00 109.63 ? 106 THR   V N   1 
ATOM   38502 C  CA  . THR   V  8  105 ? 7.519   -186.880 61.634  1.00 110.55 ? 106 THR   V CA  1 
ATOM   38503 C  C   . THR   V  8  105 ? 6.691   -185.760 62.283  1.00 109.32 ? 106 THR   V C   1 
ATOM   38504 O  O   . THR   V  8  105 ? 6.971   -185.432 63.453  1.00 110.71 ? 106 THR   V O   1 
ATOM   38505 C  CB  . THR   V  8  105 ? 8.828   -186.354 61.022  1.00 110.06 ? 106 THR   V CB  1 
ATOM   38506 O  OG1 . THR   V  8  105 ? 9.631   -187.473 60.645  1.00 113.19 ? 106 THR   V OG1 1 
ATOM   38507 C  CG2 . THR   V  8  105 ? 9.619   -185.469 61.960  1.00 108.52 ? 106 THR   V CG2 1 
ATOM   38508 N  N   . GLY   V  8  106 ? 5.720   -185.194 61.559  1.00 111.21 ? 107 GLY   V N   1 
ATOM   38509 C  CA  . GLY   V  8  106 ? 4.870   -184.078 62.028  1.00 111.45 ? 107 GLY   V CA  1 
ATOM   38510 C  C   . GLY   V  8  106 ? 4.606   -183.066 60.923  1.00 109.99 ? 107 GLY   V C   1 
ATOM   38511 O  O   . GLY   V  8  106 ? 4.736   -183.440 59.739  1.00 107.58 ? 107 GLY   V O   1 
ATOM   38512 N  N   . SER   V  8  107 ? 4.247   -181.830 61.290  1.00 107.67 ? 108 SER   V N   1 
ATOM   38513 C  CA  . SER   V  8  107 ? 3.990   -180.702 60.352  1.00 105.79 ? 108 SER   V CA  1 
ATOM   38514 C  C   . SER   V  8  107 ? 5.197   -179.758 60.339  1.00 101.81 ? 108 SER   V C   1 
ATOM   38515 O  O   . SER   V  8  107 ? 5.797   -179.554 61.411  1.00 102.44 ? 108 SER   V O   1 
ATOM   38516 C  CB  . SER   V  8  107 ? 2.720   -179.969 60.705  1.00 107.56 ? 108 SER   V CB  1 
ATOM   38517 O  OG  . SER   V  8  107 ? 2.955   -178.974 61.693  1.00 107.75 ? 108 SER   V OG  1 
ATOM   38518 N  N   . HIS   V  8  108 ? 5.531   -179.201 59.170  1.00 99.75  ? 109 HIS   V N   1 
ATOM   38519 C  CA  . HIS   V  8  108 ? 6.790   -178.446 58.925  1.00 99.85  ? 109 HIS   V CA  1 
ATOM   38520 C  C   . HIS   V  8  108 ? 6.536   -177.203 58.066  1.00 99.49  ? 109 HIS   V C   1 
ATOM   38521 O  O   . HIS   V  8  108 ? 5.648   -177.252 57.190  1.00 102.66 ? 109 HIS   V O   1 
ATOM   38522 C  CB  . HIS   V  8  108 ? 7.833   -179.351 58.260  1.00 99.19  ? 109 HIS   V CB  1 
ATOM   38523 C  CG  . HIS   V  8  108 ? 8.112   -180.605 59.017  1.00 100.33 ? 109 HIS   V CG  1 
ATOM   38524 N  ND1 . HIS   V  8  108 ? 8.961   -180.637 60.105  1.00 97.52  ? 109 HIS   V ND1 1 
ATOM   38525 C  CD2 . HIS   V  8  108 ? 7.655   -181.863 58.849  1.00 100.49 ? 109 HIS   V CD2 1 
ATOM   38526 C  CE1 . HIS   V  8  108 ? 9.013   -181.864 60.576  1.00 98.75  ? 109 HIS   V CE1 1 
ATOM   38527 N  NE2 . HIS   V  8  108 ? 8.222   -182.637 59.822  1.00 102.67 ? 109 HIS   V NE2 1 
ATOM   38528 N  N   . LEU   V  8  109 ? 7.315   -176.144 58.308  1.00 96.44  ? 110 LEU   V N   1 
ATOM   38529 C  CA  . LEU   V  8  109 ? 7.326   -174.892 57.506  1.00 94.24  ? 110 LEU   V CA  1 
ATOM   38530 C  C   . LEU   V  8  109 ? 8.770   -174.410 57.345  1.00 91.91  ? 110 LEU   V C   1 
ATOM   38531 O  O   . LEU   V  8  109 ? 9.438   -174.167 58.369  1.00 91.58  ? 110 LEU   V O   1 
ATOM   38532 C  CB  . LEU   V  8  109 ? 6.468   -173.825 58.195  1.00 94.13  ? 110 LEU   V CB  1 
ATOM   38533 C  CG  . LEU   V  8  109 ? 6.383   -172.479 57.473  1.00 93.51  ? 110 LEU   V CG  1 
ATOM   38534 C  CD1 . LEU   V  8  109 ? 5.785   -172.632 56.080  1.00 92.19  ? 110 LEU   V CD1 1 
ATOM   38535 C  CD2 . LEU   V  8  109 ? 5.576   -171.479 58.284  1.00 92.93  ? 110 LEU   V CD2 1 
ATOM   38536 N  N   . PHE   V  8  110 ? 9.217   -174.268 56.098  1.00 90.53  ? 111 PHE   V N   1 
ATOM   38537 C  CA  . PHE   V  8  110 ? 10.578  -173.808 55.726  1.00 89.12  ? 111 PHE   V CA  1 
ATOM   38538 C  C   . PHE   V  8  110 ? 10.481  -172.758 54.618  1.00 89.57  ? 111 PHE   V C   1 
ATOM   38539 O  O   . PHE   V  8  110 ? 9.406   -172.614 53.997  1.00 88.48  ? 111 PHE   V O   1 
ATOM   38540 C  CB  . PHE   V  8  110 ? 11.434  -174.981 55.248  1.00 88.17  ? 111 PHE   V CB  1 
ATOM   38541 C  CG  . PHE   V  8  110 ? 11.568  -176.111 56.235  1.00 88.41  ? 111 PHE   V CG  1 
ATOM   38542 C  CD1 . PHE   V  8  110 ? 12.298  -175.951 57.401  1.00 87.41  ? 111 PHE   V CD1 1 
ATOM   38543 C  CD2 . PHE   V  8  110 ? 10.972  -177.339 55.991  1.00 89.04  ? 111 PHE   V CD2 1 
ATOM   38544 C  CE1 . PHE   V  8  110 ? 12.422  -176.992 58.307  1.00 88.89  ? 111 PHE   V CE1 1 
ATOM   38545 C  CE2 . PHE   V  8  110 ? 11.102  -178.381 56.895  1.00 89.02  ? 111 PHE   V CE2 1 
ATOM   38546 C  CZ  . PHE   V  8  110 ? 11.825  -178.205 58.052  1.00 89.66  ? 111 PHE   V CZ  1 
ATOM   38547 N  N   . SER   V  8  111 ? 11.591  -172.058 54.384  1.00 88.33  ? 112 SER   V N   1 
ATOM   38548 C  CA  . SER   V  8  111 ? 11.786  -171.105 53.263  1.00 90.17  ? 112 SER   V CA  1 
ATOM   38549 C  C   . SER   V  8  111 ? 13.129  -171.417 52.595  1.00 89.22  ? 112 SER   V C   1 
ATOM   38550 O  O   . SER   V  8  111 ? 14.073  -171.764 53.329  1.00 88.22  ? 112 SER   V O   1 
ATOM   38551 C  CB  . SER   V  8  111 ? 11.714  -169.678 53.747  1.00 89.63  ? 112 SER   V CB  1 
ATOM   38552 O  OG  . SER   V  8  111 ? 12.985  -169.214 54.174  1.00 91.68  ? 112 SER   V OG  1 
ATOM   38553 N  N   . ILE   V  8  112 ? 13.205  -171.327 51.263  1.00 90.84  ? 113 ILE   V N   1 
ATOM   38554 C  CA  . ILE   V  8  112 ? 14.458  -171.577 50.489  1.00 94.01  ? 113 ILE   V CA  1 
ATOM   38555 C  C   . ILE   V  8  112 ? 14.728  -170.387 49.568  1.00 90.57  ? 113 ILE   V C   1 
ATOM   38556 O  O   . ILE   V  8  112 ? 13.807  -169.994 48.827  1.00 91.45  ? 113 ILE   V O   1 
ATOM   38557 C  CB  . ILE   V  8  112 ? 14.394  -172.887 49.680  1.00 97.36  ? 113 ILE   V CB  1 
ATOM   38558 C  CG1 . ILE   V  8  112 ? 13.785  -174.039 50.484  1.00 100.71 ? 113 ILE   V CG1 1 
ATOM   38559 C  CG2 . ILE   V  8  112 ? 15.779  -173.231 49.146  1.00 98.81  ? 113 ILE   V CG2 1 
ATOM   38560 C  CD1 . ILE   V  8  112 ? 13.720  -175.351 49.732  1.00 101.68 ? 113 ILE   V CD1 1 
ATOM   38561 N  N   . HIS   V  8  113 ? 15.963  -169.879 49.597  1.00 89.53  ? 114 HIS   V N   1 
ATOM   38562 C  CA  . HIS   V  8  113 ? 16.467  -168.776 48.737  1.00 91.05  ? 114 HIS   V CA  1 
ATOM   38563 C  C   . HIS   V  8  113 ? 17.222  -169.375 47.545  1.00 84.89  ? 114 HIS   V C   1 
ATOM   38564 O  O   . HIS   V  8  113 ? 17.766  -170.482 47.686  1.00 81.85  ? 114 HIS   V O   1 
ATOM   38565 C  CB  . HIS   V  8  113 ? 17.330  -167.807 49.559  1.00 94.43  ? 114 HIS   V CB  1 
ATOM   38566 C  CG  . HIS   V  8  113 ? 16.544  -166.818 50.359  1.00 97.93  ? 114 HIS   V CG  1 
ATOM   38567 N  ND1 . HIS   V  8  113 ? 15.677  -167.196 51.369  1.00 97.60  ? 114 HIS   V ND1 1 
ATOM   38568 C  CD2 . HIS   V  8  113 ? 16.500  -165.468 50.312  1.00 99.41  ? 114 HIS   V CD2 1 
ATOM   38569 C  CE1 . HIS   V  8  113 ? 15.128  -166.123 51.903  1.00 97.70  ? 114 HIS   V CE1 1 
ATOM   38570 N  NE2 . HIS   V  8  113 ? 15.618  -165.050 51.273  1.00 97.34  ? 114 HIS   V NE2 1 
ATOM   38571 N  N   . ALA   V  8  114 ? 17.254  -168.648 46.425  1.00 85.80  ? 115 ALA   V N   1 
ATOM   38572 C  CA  . ALA   V  8  114 ? 17.822  -169.070 45.122  1.00 83.45  ? 115 ALA   V CA  1 
ATOM   38573 C  C   . ALA   V  8  114 ? 19.276  -169.533 45.282  1.00 83.28  ? 115 ALA   V C   1 
ATOM   38574 O  O   . ALA   V  8  114 ? 19.679  -170.443 44.533  1.00 83.00  ? 115 ALA   V O   1 
ATOM   38575 C  CB  . ALA   V  8  114 ? 17.717  -167.938 44.131  1.00 85.78  ? 115 ALA   V CB  1 
ATOM   38576 N  N   . HIS   V  8  115 ? 20.036  -168.923 46.197  1.00 82.33  ? 116 HIS   V N   1 
ATOM   38577 C  CA  . HIS   V  8  115 ? 21.477  -169.222 46.426  1.00 82.06  ? 116 HIS   V CA  1 
ATOM   38578 C  C   . HIS   V  8  115 ? 21.637  -170.532 47.211  1.00 80.55  ? 116 HIS   V C   1 
ATOM   38579 O  O   . HIS   V  8  115 ? 22.725  -171.140 47.110  1.00 78.68  ? 116 HIS   V O   1 
ATOM   38580 C  CB  . HIS   V  8  115 ? 22.190  -168.023 47.071  1.00 82.15  ? 116 HIS   V CB  1 
ATOM   38581 C  CG  . HIS   V  8  115 ? 22.616  -167.006 46.066  1.00 80.51  ? 116 HIS   V CG  1 
ATOM   38582 N  ND1 . HIS   V  8  115 ? 23.576  -167.282 45.112  1.00 79.75  ? 116 HIS   V ND1 1 
ATOM   38583 C  CD2 . HIS   V  8  115 ? 22.209  -165.739 45.843  1.00 81.64  ? 116 HIS   V CD2 1 
ATOM   38584 C  CE1 . HIS   V  8  115 ? 23.752  -166.225 44.350  1.00 80.00  ? 116 HIS   V CE1 1 
ATOM   38585 N  NE2 . HIS   V  8  115 ? 22.925  -165.265 44.777  1.00 80.72  ? 116 HIS   V NE2 1 
ATOM   38586 N  N   . GLY   V  8  116 ? 20.604  -170.952 47.951  1.00 82.59  ? 117 GLY   V N   1 
ATOM   38587 C  CA  . GLY   V  8  116 ? 20.532  -172.290 48.575  1.00 82.26  ? 117 GLY   V CA  1 
ATOM   38588 C  C   . GLY   V  8  116 ? 20.405  -172.263 50.092  1.00 84.18  ? 117 GLY   V C   1 
ATOM   38589 O  O   . GLY   V  8  116 ? 20.385  -173.361 50.673  1.00 82.61  ? 117 GLY   V O   1 
ATOM   38590 N  N   . SER   V  8  117 ? 20.318  -171.084 50.721  1.00 85.41  ? 118 SER   V N   1 
ATOM   38591 C  CA  . SER   V  8  117 ? 20.099  -170.930 52.186  1.00 85.04  ? 118 SER   V CA  1 
ATOM   38592 C  C   . SER   V  8  117 ? 18.653  -171.314 52.525  1.00 86.67  ? 118 SER   V C   1 
ATOM   38593 O  O   . SER   V  8  117 ? 17.771  -171.115 51.662  1.00 84.63  ? 118 SER   V O   1 
ATOM   38594 C  CB  . SER   V  8  117 ? 20.424  -169.533 52.657  1.00 85.65  ? 118 SER   V CB  1 
ATOM   38595 O  OG  . SER   V  8  117 ? 19.651  -168.564 51.963  1.00 87.00  ? 118 SER   V OG  1 
ATOM   38596 N  N   . THR   V  8  118 ? 18.429  -171.864 53.724  1.00 87.77  ? 119 THR   V N   1 
ATOM   38597 C  CA  . THR   V  8  118 ? 17.094  -172.280 54.237  1.00 93.78  ? 119 THR   V CA  1 
ATOM   38598 C  C   . THR   V  8  118 ? 16.831  -171.671 55.620  1.00 88.50  ? 119 THR   V C   1 
ATOM   38599 O  O   . THR   V  8  118 ? 17.799  -171.465 56.376  1.00 82.97  ? 119 THR   V O   1 
ATOM   38600 C  CB  . THR   V  8  118 ? 16.957  -173.807 54.287  1.00 95.65  ? 119 THR   V CB  1 
ATOM   38601 O  OG1 . THR   V  8  118 ? 17.958  -174.341 55.157  1.00 98.53  ? 119 THR   V OG1 1 
ATOM   38602 C  CG2 . THR   V  8  118 ? 17.077  -174.440 52.919  1.00 100.79 ? 119 THR   V CG2 1 
ATOM   38603 N  N   . ASP   V  8  119 ? 15.554  -171.420 55.926  1.00 91.81  ? 120 ASP   V N   1 
ATOM   38604 C  CA  . ASP   V  8  119 ? 15.070  -170.861 57.216  1.00 95.25  ? 120 ASP   V CA  1 
ATOM   38605 C  C   . ASP   V  8  119 ? 14.032  -171.808 57.821  1.00 92.10  ? 120 ASP   V C   1 
ATOM   38606 O  O   . ASP   V  8  119 ? 13.381  -172.538 57.053  1.00 95.02  ? 120 ASP   V O   1 
ATOM   38607 C  CB  . ASP   V  8  119 ? 14.417  -169.489 57.031  1.00 102.54 ? 120 ASP   V CB  1 
ATOM   38608 C  CG  . ASP   V  8  119 ? 15.349  -168.403 56.517  1.00 110.36 ? 120 ASP   V CG  1 
ATOM   38609 O  OD1 . ASP   V  8  119 ? 16.577  -168.621 56.539  1.00 118.12 ? 120 ASP   V OD1 1 
ATOM   38610 O  OD2 . ASP   V  8  119 ? 14.837  -167.338 56.104  1.00 123.91 ? 120 ASP   V OD2 1 
ATOM   38611 N  N   . VAL   V  8  120 ? 13.881  -171.766 59.146  1.00 88.42  ? 121 VAL   V N   1 
ATOM   38612 C  CA  . VAL   V  8  120 ? 12.776  -172.422 59.905  1.00 91.10  ? 121 VAL   V CA  1 
ATOM   38613 C  C   . VAL   V  8  120 ? 11.990  -171.318 60.614  1.00 89.13  ? 121 VAL   V C   1 
ATOM   38614 O  O   . VAL   V  8  120 ? 12.630  -170.362 61.094  1.00 91.35  ? 121 VAL   V O   1 
ATOM   38615 C  CB  . VAL   V  8  120 ? 13.307  -173.462 60.911  1.00 94.00  ? 121 VAL   V CB  1 
ATOM   38616 C  CG1 . VAL   V  8  120 ? 12.182  -174.317 61.477  1.00 97.04  ? 121 VAL   V CG1 1 
ATOM   38617 C  CG2 . VAL   V  8  120 ? 14.389  -174.343 60.304  1.00 94.71  ? 121 VAL   V CG2 1 
ATOM   38618 N  N   . GLY   V  8  121 ? 10.663  -171.442 60.674  1.00 86.54  ? 122 GLY   V N   1 
ATOM   38619 C  CA  . GLY   V  8  121 ? 9.795   -170.454 61.344  1.00 89.91  ? 122 GLY   V CA  1 
ATOM   38620 C  C   . GLY   V  8  121 ? 8.345   -170.895 61.394  1.00 92.20  ? 122 GLY   V C   1 
ATOM   38621 O  O   . GLY   V  8  121 ? 7.983   -171.816 60.637  1.00 94.32  ? 122 GLY   V O   1 
ATOM   38622 N  N   . TYR   V  8  122 ? 7.551   -170.251 62.257  1.00 93.63  ? 123 TYR   V N   1 
ATOM   38623 C  CA  . TYR   V  8  122 ? 6.092   -170.483 62.427  1.00 95.68  ? 123 TYR   V CA  1 
ATOM   38624 C  C   . TYR   V  8  122 ? 5.312   -169.657 61.402  1.00 93.64  ? 123 TYR   V C   1 
ATOM   38625 O  O   . TYR   V  8  122 ? 4.191   -170.060 61.041  1.00 90.24  ? 123 TYR   V O   1 
ATOM   38626 C  CB  . TYR   V  8  122 ? 5.646   -170.128 63.846  1.00 100.85 ? 123 TYR   V CB  1 
ATOM   38627 C  CG  . TYR   V  8  122 ? 6.166   -171.067 64.903  1.00 106.29 ? 123 TYR   V CG  1 
ATOM   38628 C  CD1 . TYR   V  8  122 ? 5.472   -172.219 65.235  1.00 110.11 ? 123 TYR   V CD1 1 
ATOM   38629 C  CD2 . TYR   V  8  122 ? 7.361   -170.816 65.559  1.00 106.35 ? 123 TYR   V CD2 1 
ATOM   38630 C  CE1 . TYR   V  8  122 ? 5.943   -173.093 66.200  1.00 113.17 ? 123 TYR   V CE1 1 
ATOM   38631 C  CE2 . TYR   V  8  122 ? 7.847   -171.679 66.527  1.00 109.25 ? 123 TYR   V CE2 1 
ATOM   38632 C  CZ  . TYR   V  8  122 ? 7.135   -172.822 66.848  1.00 113.41 ? 123 TYR   V CZ  1 
ATOM   38633 O  OH  . TYR   V  8  122 ? 7.604   -173.680 67.800  1.00 118.81 ? 123 TYR   V OH  1 
ATOM   38634 N  N   . TYR   V  8  123 ? 5.885   -168.528 60.978  1.00 92.68  ? 124 TYR   V N   1 
ATOM   38635 C  CA  . TYR   V  8  123 ? 5.334   -167.630 59.932  1.00 91.82  ? 124 TYR   V CA  1 
ATOM   38636 C  C   . TYR   V  8  123 ? 6.489   -167.091 59.083  1.00 89.17  ? 124 TYR   V C   1 
ATOM   38637 O  O   . TYR   V  8  123 ? 7.490   -166.614 59.654  1.00 87.69  ? 124 TYR   V O   1 
ATOM   38638 C  CB  . TYR   V  8  123 ? 4.511   -166.503 60.561  1.00 92.02  ? 124 TYR   V CB  1 
ATOM   38639 C  CG  . TYR   V  8  123 ? 5.289   -165.604 61.487  1.00 92.21  ? 124 TYR   V CG  1 
ATOM   38640 C  CD1 . TYR   V  8  123 ? 5.575   -165.996 62.784  1.00 93.33  ? 124 TYR   V CD1 1 
ATOM   38641 C  CD2 . TYR   V  8  123 ? 5.745   -164.365 61.069  1.00 92.49  ? 124 TYR   V CD2 1 
ATOM   38642 C  CE1 . TYR   V  8  123 ? 6.291   -165.181 63.644  1.00 94.30  ? 124 TYR   V CE1 1 
ATOM   38643 C  CE2 . TYR   V  8  123 ? 6.461   -163.535 61.917  1.00 94.34  ? 124 TYR   V CE2 1 
ATOM   38644 C  CZ  . TYR   V  8  123 ? 6.736   -163.945 63.211  1.00 93.89  ? 124 TYR   V CZ  1 
ATOM   38645 O  OH  . TYR   V  8  123 ? 7.443   -163.146 64.064  1.00 91.30  ? 124 TYR   V OH  1 
ATOM   38646 N  N   . LEU   V  8  124 ? 6.352   -167.195 57.760  1.00 89.26  ? 125 LEU   V N   1 
ATOM   38647 C  CA  . LEU   V  8  124 ? 7.344   -166.720 56.762  1.00 90.46  ? 125 LEU   V CA  1 
ATOM   38648 C  C   . LEU   V  8  124 ? 6.597   -166.026 55.623  1.00 89.43  ? 125 LEU   V C   1 
ATOM   38649 O  O   . LEU   V  8  124 ? 5.415   -166.357 55.409  1.00 91.49  ? 125 LEU   V O   1 
ATOM   38650 C  CB  . LEU   V  8  124 ? 8.135   -167.917 56.226  1.00 90.86  ? 125 LEU   V CB  1 
ATOM   38651 C  CG  . LEU   V  8  124 ? 8.866   -168.759 57.268  1.00 92.31  ? 125 LEU   V CG  1 
ATOM   38652 C  CD1 . LEU   V  8  124 ? 9.285   -170.092 56.671  1.00 94.47  ? 125 LEU   V CD1 1 
ATOM   38653 C  CD2 . LEU   V  8  124 ? 10.070  -168.016 57.826  1.00 91.15  ? 125 LEU   V CD2 1 
ATOM   38654 N  N   . SER   V  8  125 ? 7.261   -165.095 54.936  1.00 89.76  ? 126 SER   V N   1 
ATOM   38655 C  CA  . SER   V  8  125 ? 6.793   -164.518 53.651  1.00 89.75  ? 126 SER   V CA  1 
ATOM   38656 C  C   . SER   V  8  125 ? 7.990   -164.242 52.740  1.00 87.79  ? 126 SER   V C   1 
ATOM   38657 O  O   . SER   V  8  125 ? 9.053   -163.856 53.254  1.00 88.05  ? 126 SER   V O   1 
ATOM   38658 C  CB  . SER   V  8  125 ? 5.969   -163.279 53.863  1.00 90.71  ? 126 SER   V CB  1 
ATOM   38659 O  OG  . SER   V  8  125 ? 6.779   -162.211 54.326  1.00 91.55  ? 126 SER   V OG  1 
ATOM   38660 N  N   . LEU   V  8  126 ? 7.767   -164.357 51.440  1.00 90.44  ? 127 LEU   V N   1 
ATOM   38661 C  CA  . LEU   V  8  126 ? 8.838   -164.115 50.453  1.00 92.00  ? 127 LEU   V CA  1 
ATOM   38662 C  C   . LEU   V  8  126 ? 8.226   -163.412 49.242  1.00 89.69  ? 127 LEU   V C   1 
ATOM   38663 O  O   . LEU   V  8  126 ? 7.002   -163.457 49.090  1.00 89.35  ? 127 LEU   V O   1 
ATOM   38664 C  CB  . LEU   V  8  126 ? 9.437   -165.467 50.072  1.00 93.42  ? 127 LEU   V CB  1 
ATOM   38665 C  CG  . LEU   V  8  126 ? 10.893  -165.668 50.474  1.00 95.57  ? 127 LEU   V CG  1 
ATOM   38666 C  CD1 . LEU   V  8  126 ? 11.009  -166.034 51.938  1.00 94.11  ? 127 LEU   V CD1 1 
ATOM   38667 C  CD2 . LEU   V  8  126 ? 11.543  -166.730 49.616  1.00 98.61  ? 127 LEU   V CD2 1 
ATOM   38668 N  N   . GLY   V  8  127 ? 9.061   -162.765 48.431  1.00 88.34  ? 128 GLY   V N   1 
ATOM   38669 C  CA  . GLY   V  8  127 ? 8.573   -162.059 47.233  1.00 90.06  ? 128 GLY   V CA  1 
ATOM   38670 C  C   . GLY   V  8  127 ? 8.667   -160.553 47.377  1.00 87.05  ? 128 GLY   V C   1 
ATOM   38671 O  O   . GLY   V  8  127 ? 9.155   -160.084 48.414  1.00 85.61  ? 128 GLY   V O   1 
ATOM   38672 N  N   . SER   V  8  128 ? 8.195   -159.823 46.367  1.00 88.69  ? 129 SER   V N   1 
ATOM   38673 C  CA  . SER   V  8  128 ? 8.234   -158.341 46.400  1.00 87.69  ? 129 SER   V CA  1 
ATOM   38674 C  C   . SER   V  8  128 ? 7.238   -157.825 47.435  1.00 87.14  ? 129 SER   V C   1 
ATOM   38675 O  O   . SER   V  8  128 ? 7.505   -156.781 48.026  1.00 89.25  ? 129 SER   V O   1 
ATOM   38676 C  CB  . SER   V  8  128 ? 7.977   -157.756 45.045  1.00 86.19  ? 129 SER   V CB  1 
ATOM   38677 O  OG  . SER   V  8  128 ? 6.771   -158.247 44.503  1.00 83.85  ? 129 SER   V OG  1 
ATOM   38678 N  N   . GLY   V  8  129 ? 6.137   -158.537 47.644  1.00 86.85  ? 130 GLY   V N   1 
ATOM   38679 C  CA  . GLY   V  8  129 ? 5.135   -158.096 48.628  1.00 87.01  ? 130 GLY   V CA  1 
ATOM   38680 C  C   . GLY   V  8  129 ? 5.369   -158.746 49.971  1.00 86.42  ? 130 GLY   V C   1 
ATOM   38681 O  O   . GLY   V  8  129 ? 4.453   -158.762 50.783  1.00 87.34  ? 130 GLY   V O   1 
ATOM   38682 N  N   . SER   V  8  130 ? 6.574   -159.247 50.202  1.00 85.36  ? 131 SER   V N   1 
ATOM   38683 C  CA  . SER   V  8  130 ? 6.877   -159.940 51.484  1.00 87.60  ? 131 SER   V CA  1 
ATOM   38684 C  C   . SER   V  8  130 ? 6.878   -158.938 52.642  1.00 85.80  ? 131 SER   V C   1 
ATOM   38685 O  O   . SER   V  8  130 ? 6.499   -159.336 53.755  1.00 85.57  ? 131 SER   V O   1 
ATOM   38686 C  CB  . SER   V  8  130 ? 8.183   -160.698 51.419  1.00 90.80  ? 131 SER   V CB  1 
ATOM   38687 O  OG  . SER   V  8  130 ? 9.293   -159.812 51.415  1.00 92.59  ? 131 SER   V OG  1 
ATOM   38688 N  N   . LEU   V  8  131 ? 7.287   -157.692 52.394  1.00 84.85  ? 132 LEU   V N   1 
ATOM   38689 C  CA  . LEU   V  8  131 ? 7.388   -156.651 53.450  1.00 86.37  ? 132 LEU   V CA  1 
ATOM   38690 C  C   . LEU   V  8  131 ? 5.983   -156.211 53.879  1.00 83.44  ? 132 LEU   V C   1 
ATOM   38691 O  O   . LEU   V  8  131 ? 5.783   -156.027 55.092  1.00 82.36  ? 132 LEU   V O   1 
ATOM   38692 C  CB  . LEU   V  8  131 ? 8.233   -155.478 52.946  1.00 89.73  ? 132 LEU   V CB  1 
ATOM   38693 C  CG  . LEU   V  8  131 ? 9.731   -155.613 53.213  1.00 93.72  ? 132 LEU   V CG  1 
ATOM   38694 C  CD1 . LEU   V  8  131 ? 10.379  -156.571 52.226  1.00 91.08  ? 132 LEU   V CD1 1 
ATOM   38695 C  CD2 . LEU   V  8  131 ? 10.414  -154.253 53.172  1.00 97.66  ? 132 LEU   V CD2 1 
ATOM   38696 N  N   . ALA   V  8  132 ? 5.048   -156.059 52.936  1.00 84.97  ? 133 ALA   V N   1 
ATOM   38697 C  CA  . ALA   V  8  132 ? 3.627   -155.747 53.226  1.00 85.68  ? 133 ALA   V CA  1 
ATOM   38698 C  C   . ALA   V  8  132 ? 3.007   -156.906 54.016  1.00 86.30  ? 133 ALA   V C   1 
ATOM   38699 O  O   . ALA   V  8  132 ? 2.287   -156.638 54.999  1.00 81.38  ? 133 ALA   V O   1 
ATOM   38700 C  CB  . ALA   V  8  132 ? 2.871   -155.477 51.947  1.00 87.92  ? 133 ALA   V CB  1 
ATOM   38701 N  N   . ALA   V  8  133 ? 3.290   -158.145 53.598  1.00 86.55  ? 134 ALA   V N   1 
ATOM   38702 C  CA  . ALA   V  8  133 ? 2.801   -159.397 54.225  1.00 87.34  ? 134 ALA   V CA  1 
ATOM   38703 C  C   . ALA   V  8  133 ? 3.387   -159.539 55.634  1.00 86.19  ? 134 ALA   V C   1 
ATOM   38704 O  O   . ALA   V  8  133 ? 2.601   -159.711 56.582  1.00 85.56  ? 134 ALA   V O   1 
ATOM   38705 C  CB  . ALA   V  8  133 ? 3.155   -160.584 53.362  1.00 87.38  ? 134 ALA   V CB  1 
ATOM   38706 N  N   . MET   V  8  134 ? 4.716   -159.460 55.757  1.00 86.56  ? 135 MET   V N   1 
ATOM   38707 C  CA  . MET   V  8  134 ? 5.455   -159.674 57.031  1.00 88.21  ? 135 MET   V CA  1 
ATOM   38708 C  C   . MET   V  8  134 ? 4.986   -158.654 58.072  1.00 88.14  ? 135 MET   V C   1 
ATOM   38709 O  O   . MET   V  8  134 ? 4.915   -159.021 59.256  1.00 87.67  ? 135 MET   V O   1 
ATOM   38710 C  CB  . MET   V  8  134 ? 6.971   -159.546 56.837  1.00 88.73  ? 135 MET   V CB  1 
ATOM   38711 C  CG  . MET   V  8  134 ? 7.778   -159.788 58.108  1.00 91.25  ? 135 MET   V CG  1 
ATOM   38712 S  SD  . MET   V  8  134 ? 7.415   -161.378 58.927  1.00 95.31  ? 135 MET   V SD  1 
ATOM   38713 C  CE  . MET   V  8  134 ? 7.994   -162.528 57.679  1.00 95.39  ? 135 MET   V CE  1 
ATOM   38714 N  N   . ALA   V  8  135 ? 4.681   -157.426 57.646  1.00 90.36  ? 136 ALA   V N   1 
ATOM   38715 C  CA  . ALA   V  8  135 ? 4.151   -156.348 58.514  1.00 92.32  ? 136 ALA   V CA  1 
ATOM   38716 C  C   . ALA   V  8  135 ? 2.865   -156.841 59.192  1.00 91.68  ? 136 ALA   V C   1 
ATOM   38717 O  O   . ALA   V  8  135 ? 2.742   -156.674 60.421  1.00 91.62  ? 136 ALA   V O   1 
ATOM   38718 C  CB  . ALA   V  8  135 ? 3.923   -155.087 57.714  1.00 92.85  ? 136 ALA   V CB  1 
ATOM   38719 N  N   . VAL   V  8  136 ? 1.963   -157.456 58.421  1.00 92.50  ? 137 VAL   V N   1 
ATOM   38720 C  CA  . VAL   V  8  136 ? 0.660   -157.996 58.916  1.00 93.07  ? 137 VAL   V CA  1 
ATOM   38721 C  C   . VAL   V  8  136 ? 0.930   -159.191 59.839  1.00 93.37  ? 137 VAL   V C   1 
ATOM   38722 O  O   . VAL   V  8  136 ? 0.302   -159.248 60.914  1.00 93.70  ? 137 VAL   V O   1 
ATOM   38723 C  CB  . VAL   V  8  136 ? -0.275  -158.381 57.754  1.00 93.85  ? 137 VAL   V CB  1 
ATOM   38724 C  CG1 . VAL   V  8  136 ? -1.423  -159.266 58.216  1.00 95.02  ? 137 VAL   V CG1 1 
ATOM   38725 C  CG2 . VAL   V  8  136 ? -0.808  -157.151 57.039  1.00 94.65  ? 137 VAL   V CG2 1 
ATOM   38726 N  N   . LEU   V  8  137 ? 1.811   -160.111 59.425  1.00 96.18  ? 138 LEU   V N   1 
ATOM   38727 C  CA  . LEU   V  8  137 ? 2.177   -161.327 60.204  1.00 97.08  ? 138 LEU   V CA  1 
ATOM   38728 C  C   . LEU   V  8  137 ? 2.762   -160.899 61.556  1.00 95.44  ? 138 LEU   V C   1 
ATOM   38729 O  O   . LEU   V  8  137 ? 2.304   -161.424 62.583  1.00 94.72  ? 138 LEU   V O   1 
ATOM   38730 C  CB  . LEU   V  8  137 ? 3.181   -162.184 59.420  1.00 96.75  ? 138 LEU   V CB  1 
ATOM   38731 C  CG  . LEU   V  8  137 ? 2.655   -162.864 58.155  1.00 95.51  ? 138 LEU   V CG  1 
ATOM   38732 C  CD1 . LEU   V  8  137 ? 3.786   -163.555 57.408  1.00 94.30  ? 138 LEU   V CD1 1 
ATOM   38733 C  CD2 . LEU   V  8  137 ? 1.546   -163.859 58.473  1.00 95.63  ? 138 LEU   V CD2 1 
ATOM   38734 N  N   . GLU   V  8  138 ? 3.716   -159.963 61.550  1.00 97.70  ? 139 GLU   V N   1 
ATOM   38735 C  CA  . GLU   V  8  138 ? 4.401   -159.468 62.775  1.00 97.92  ? 139 GLU   V CA  1 
ATOM   38736 C  C   . GLU   V  8  138 ? 3.388   -158.767 63.686  1.00 96.69  ? 139 GLU   V C   1 
ATOM   38737 O  O   . GLU   V  8  138 ? 3.627   -158.745 64.906  1.00 99.36  ? 139 GLU   V O   1 
ATOM   38738 C  CB  . GLU   V  8  138 ? 5.558   -158.532 62.419  1.00 100.17 ? 139 GLU   V CB  1 
ATOM   38739 C  CG  . GLU   V  8  138 ? 6.778   -159.259 61.887  1.00 103.02 ? 139 GLU   V CG  1 
ATOM   38740 C  CD  . GLU   V  8  138 ? 7.643   -159.903 62.958  1.00 103.51 ? 139 GLU   V CD  1 
ATOM   38741 O  OE1 . GLU   V  8  138 ? 8.881   -159.851 62.823  1.00 107.78 ? 139 GLU   V OE1 1 
ATOM   38742 O  OE2 . GLU   V  8  138 ? 7.082   -160.456 63.924  1.00 107.24 ? 139 GLU   V OE2 1 
ATOM   38743 N  N   . SER   V  8  139 ? 2.304   -158.229 63.115  1.00 98.26  ? 140 SER   V N   1 
ATOM   38744 C  CA  . SER   V  8  139 ? 1.248   -157.472 63.838  1.00 96.67  ? 140 SER   V CA  1 
ATOM   38745 C  C   . SER   V  8  139 ? 0.225   -158.419 64.483  1.00 96.33  ? 140 SER   V C   1 
ATOM   38746 O  O   . SER   V  8  139 ? -0.207  -158.116 65.610  1.00 93.92  ? 140 SER   V O   1 
ATOM   38747 C  CB  . SER   V  8  139 ? 0.570   -156.478 62.927  1.00 97.94  ? 140 SER   V CB  1 
ATOM   38748 O  OG  . SER   V  8  139 ? 1.467   -155.443 62.558  1.00 96.98  ? 140 SER   V OG  1 
ATOM   38749 N  N   . HIS   V  8  140 ? -0.163  -159.505 63.803  1.00 100.04 ? 141 HIS   V N   1 
ATOM   38750 C  CA  . HIS   V  8  140 ? -1.344  -160.339 64.171  1.00 104.37 ? 141 HIS   V CA  1 
ATOM   38751 C  C   . HIS   V  8  140 ? -0.987  -161.805 64.472  1.00 102.49 ? 141 HIS   V C   1 
ATOM   38752 O  O   . HIS   V  8  140 ? -1.905  -162.532 64.907  1.00 97.16  ? 141 HIS   V O   1 
ATOM   38753 C  CB  . HIS   V  8  140 ? -2.415  -160.264 63.074  1.00 106.67 ? 141 HIS   V CB  1 
ATOM   38754 C  CG  . HIS   V  8  140 ? -2.953  -158.893 62.847  1.00 109.89 ? 141 HIS   V CG  1 
ATOM   38755 N  ND1 . HIS   V  8  140 ? -3.217  -158.022 63.886  1.00 111.06 ? 141 HIS   V ND1 1 
ATOM   38756 C  CD2 . HIS   V  8  140 ? -3.296  -158.248 61.711  1.00 113.66 ? 141 HIS   V CD2 1 
ATOM   38757 C  CE1 . HIS   V  8  140 ? -3.687  -156.892 63.398  1.00 115.02 ? 141 HIS   V CE1 1 
ATOM   38758 N  NE2 . HIS   V  8  140 ? -3.748  -157.006 62.065  1.00 116.63 ? 141 HIS   V NE2 1 
ATOM   38759 N  N   . TRP   V  8  141 ? 0.258   -162.250 64.260  1.00 106.19 ? 142 TRP   V N   1 
ATOM   38760 C  CA  . TRP   V  8  141 ? 0.657   -163.651 64.569  1.00 106.81 ? 142 TRP   V CA  1 
ATOM   38761 C  C   . TRP   V  8  141 ? 0.691   -163.844 66.087  1.00 108.47 ? 142 TRP   V C   1 
ATOM   38762 O  O   . TRP   V  8  141 ? 1.038   -162.883 66.801  1.00 108.64 ? 142 TRP   V O   1 
ATOM   38763 C  CB  . TRP   V  8  141 ? 2.002   -164.050 63.946  1.00 108.40 ? 142 TRP   V CB  1 
ATOM   38764 C  CG  . TRP   V  8  141 ? 2.374   -165.472 64.247  1.00 109.12 ? 142 TRP   V CG  1 
ATOM   38765 C  CD1 . TRP   V  8  141 ? 2.035   -166.580 63.525  1.00 108.24 ? 142 TRP   V CD1 1 
ATOM   38766 C  CD2 . TRP   V  8  141 ? 3.119   -165.951 65.382  1.00 109.60 ? 142 TRP   V CD2 1 
ATOM   38767 N  NE1 . TRP   V  8  141 ? 2.531   -167.708 64.120  1.00 107.16 ? 142 TRP   V NE1 1 
ATOM   38768 C  CE2 . TRP   V  8  141 ? 3.199   -167.356 65.262  1.00 107.41 ? 142 TRP   V CE2 1 
ATOM   38769 C  CE3 . TRP   V  8  141 ? 3.731   -165.335 66.481  1.00 112.07 ? 142 TRP   V CE3 1 
ATOM   38770 C  CZ2 . TRP   V  8  141 ? 3.869   -168.146 66.195  1.00 107.82 ? 142 TRP   V CZ2 1 
ATOM   38771 C  CZ3 . TRP   V  8  141 ? 4.392   -166.117 67.404  1.00 110.96 ? 142 TRP   V CZ3 1 
ATOM   38772 C  CH2 . TRP   V  8  141 ? 4.458   -167.504 67.260  1.00 108.34 ? 142 TRP   V CH2 1 
ATOM   38773 N  N   . LYS   V  8  142 ? 0.348   -165.050 66.545  1.00 108.75 ? 143 LYS   V N   1 
ATOM   38774 C  CA  . LYS   V  8  142 ? 0.520   -165.496 67.952  1.00 109.91 ? 143 LYS   V CA  1 
ATOM   38775 C  C   . LYS   V  8  142 ? 0.743   -167.010 67.974  1.00 112.10 ? 143 LYS   V C   1 
ATOM   38776 O  O   . LYS   V  8  142 ? 0.415   -167.672 66.973  1.00 111.94 ? 143 LYS   V O   1 
ATOM   38777 C  CB  . LYS   V  8  142 ? -0.688  -165.097 68.805  1.00 111.37 ? 143 LYS   V CB  1 
ATOM   38778 C  CG  . LYS   V  8  142 ? -2.050  -165.557 68.298  1.00 112.37 ? 143 LYS   V CG  1 
ATOM   38779 C  CD  . LYS   V  8  142 ? -3.159  -165.286 69.297  1.00 114.77 ? 143 LYS   V CD  1 
ATOM   38780 C  CE  . LYS   V  8  142 ? -4.539  -165.203 68.679  1.00 115.48 ? 143 LYS   V CE  1 
ATOM   38781 N  NZ  . LYS   V  8  142 ? -5.052  -166.538 68.293  1.00 115.89 ? 143 LYS   V NZ  1 
ATOM   38782 N  N   . GLN   V  8  143 ? 1.300   -167.518 69.075  1.00 116.11 ? 144 GLN   V N   1 
ATOM   38783 C  CA  . GLN   V  8  143 ? 1.468   -168.971 69.343  1.00 121.43 ? 144 GLN   V CA  1 
ATOM   38784 C  C   . GLN   V  8  143 ? 0.080   -169.591 69.556  1.00 118.34 ? 144 GLN   V C   1 
ATOM   38785 O  O   . GLN   V  8  143 ? -0.804  -168.887 70.089  1.00 124.49 ? 144 GLN   V O   1 
ATOM   38786 C  CB  . GLN   V  8  143 ? 2.379   -169.173 70.557  1.00 125.74 ? 144 GLN   V CB  1 
ATOM   38787 C  CG  . GLN   V  8  143 ? 2.839   -170.611 70.766  1.00 129.77 ? 144 GLN   V CG  1 
ATOM   38788 C  CD  . GLN   V  8  143 ? 3.946   -171.020 69.824  1.00 129.67 ? 144 GLN   V CD  1 
ATOM   38789 O  OE1 . GLN   V  8  143 ? 5.128   -170.922 70.147  1.00 127.62 ? 144 GLN   V OE1 1 
ATOM   38790 N  NE2 . GLN   V  8  143 ? 3.572   -171.489 68.643  1.00 133.12 ? 144 GLN   V NE2 1 
ATOM   38791 N  N   . ASP   V  8  144 ? -0.103  -170.848 69.135  1.00 116.77 ? 145 ASP   V N   1 
ATOM   38792 C  CA  . ASP   V  8  144 ? -1.350  -171.643 69.306  1.00 117.22 ? 145 ASP   V CA  1 
ATOM   38793 C  C   . ASP   V  8  144 ? -2.481  -171.022 68.476  1.00 111.15 ? 145 ASP   V C   1 
ATOM   38794 O  O   . ASP   V  8  144 ? -3.539  -170.713 69.057  1.00 111.87 ? 145 ASP   V O   1 
ATOM   38795 C  CB  . ASP   V  8  144 ? -1.743  -171.767 70.782  1.00 121.51 ? 145 ASP   V CB  1 
ATOM   38796 C  CG  . ASP   V  8  144 ? -0.744  -172.546 71.619  1.00 125.35 ? 145 ASP   V CG  1 
ATOM   38797 O  OD1 . ASP   V  8  144 ? -0.413  -173.683 71.227  1.00 129.72 ? 145 ASP   V OD1 1 
ATOM   38798 O  OD2 . ASP   V  8  144 ? -0.304  -172.009 72.654  1.00 131.98 ? 145 ASP   V OD2 1 
ATOM   38799 N  N   . LEU   V  8  145 ? -2.263  -170.853 67.168  1.00 108.23 ? 146 LEU   V N   1 
ATOM   38800 C  CA  . LEU   V  8  145 ? -3.320  -170.484 66.187  1.00 108.03 ? 146 LEU   V CA  1 
ATOM   38801 C  C   . LEU   V  8  145 ? -4.169  -171.722 65.890  1.00 107.32 ? 146 LEU   V C   1 
ATOM   38802 O  O   . LEU   V  8  145 ? -3.597  -172.823 65.863  1.00 104.33 ? 146 LEU   V O   1 
ATOM   38803 C  CB  . LEU   V  8  145 ? -2.676  -169.965 64.897  1.00 110.55 ? 146 LEU   V CB  1 
ATOM   38804 C  CG  . LEU   V  8  145 ? -2.146  -168.535 64.947  1.00 110.77 ? 146 LEU   V CG  1 
ATOM   38805 C  CD1 . LEU   V  8  145 ? -1.050  -168.333 63.911  1.00 113.07 ? 146 LEU   V CD1 1 
ATOM   38806 C  CD2 . LEU   V  8  145 ? -3.271  -167.532 64.742  1.00 111.96 ? 146 LEU   V CD2 1 
ATOM   38807 N  N   . THR   V  8  146 ? -5.472  -171.541 65.661  1.00 106.28 ? 147 THR   V N   1 
ATOM   38808 C  CA  . THR   V  8  146 ? -6.382  -172.589 65.124  1.00 109.98 ? 147 THR   V CA  1 
ATOM   38809 C  C   . THR   V  8  146 ? -6.278  -172.593 63.597  1.00 113.51 ? 147 THR   V C   1 
ATOM   38810 O  O   . THR   V  8  146 ? -5.679  -171.650 63.043  1.00 113.15 ? 147 THR   V O   1 
ATOM   38811 C  CB  . THR   V  8  146 ? -7.836  -172.383 65.569  1.00 108.63 ? 147 THR   V CB  1 
ATOM   38812 O  OG1 . THR   V  8  146 ? -8.341  -171.189 64.971  1.00 108.14 ? 147 THR   V OG1 1 
ATOM   38813 C  CG2 . THR   V  8  146 ? -7.982  -172.307 67.072  1.00 109.13 ? 147 THR   V CG2 1 
ATOM   38814 N  N   . LYS   V  8  147 ? -6.844  -173.618 62.954  1.00 120.46 ? 148 LYS   V N   1 
ATOM   38815 C  CA  . LYS   V  8  147 ? -6.894  -173.765 61.475  1.00 121.95 ? 148 LYS   V CA  1 
ATOM   38816 C  C   . LYS   V  8  147 ? -7.529  -172.510 60.857  1.00 124.39 ? 148 LYS   V C   1 
ATOM   38817 O  O   . LYS   V  8  147 ? -6.897  -171.918 59.962  1.00 125.51 ? 148 LYS   V O   1 
ATOM   38818 C  CB  . LYS   V  8  147 ? -7.666  -175.035 61.101  1.00 123.13 ? 148 LYS   V CB  1 
ATOM   38819 C  CG  . LYS   V  8  147 ? -7.748  -175.340 59.610  1.00 123.12 ? 148 LYS   V CG  1 
ATOM   38820 C  CD  . LYS   V  8  147 ? -8.782  -176.390 59.270  1.00 124.03 ? 148 LYS   V CD  1 
ATOM   38821 C  CE  . LYS   V  8  147 ? -9.108  -176.433 57.793  1.00 124.05 ? 148 LYS   V CE  1 
ATOM   38822 N  NZ  . LYS   V  8  147 ? -10.143 -177.448 57.489  1.00 126.33 ? 148 LYS   V NZ  1 
ATOM   38823 N  N   . GLU   V  8  148 ? -8.715  -172.107 61.332  1.00 123.32 ? 149 GLU   V N   1 
ATOM   38824 C  CA  . GLU   V  8  148 ? -9.526  -171.005 60.738  1.00 121.75 ? 149 GLU   V CA  1 
ATOM   38825 C  C   . GLU   V  8  148 ? -8.894  -169.642 61.052  1.00 116.62 ? 149 GLU   V C   1 
ATOM   38826 O  O   . GLU   V  8  148 ? -9.145  -168.696 60.280  1.00 108.53 ? 149 GLU   V O   1 
ATOM   38827 C  CB  . GLU   V  8  148 ? -10.976 -171.047 61.228  1.00 128.61 ? 149 GLU   V CB  1 
ATOM   38828 C  CG  . GLU   V  8  148 ? -11.821 -172.106 60.540  1.00 135.49 ? 149 GLU   V CG  1 
ATOM   38829 C  CD  . GLU   V  8  148 ? -11.595 -173.531 61.019  1.00 142.52 ? 149 GLU   V CD  1 
ATOM   38830 O  OE1 . GLU   V  8  148 ? -11.972 -174.466 60.284  1.00 150.11 ? 149 GLU   V OE1 1 
ATOM   38831 O  OE2 . GLU   V  8  148 ? -11.049 -173.705 62.128  1.00 149.86 ? 149 GLU   V OE2 1 
ATOM   38832 N  N   . GLU   V  8  149 ? -8.126  -169.539 62.142  1.00 112.41 ? 150 GLU   V N   1 
ATOM   38833 C  CA  . GLU   V  8  149 ? -7.347  -168.320 62.498  1.00 109.33 ? 150 GLU   V CA  1 
ATOM   38834 C  C   . GLU   V  8  149 ? -6.144  -168.190 61.557  1.00 106.40 ? 150 GLU   V C   1 
ATOM   38835 O  O   . GLU   V  8  149 ? -5.892  -167.073 61.066  1.00 105.79 ? 150 GLU   V O   1 
ATOM   38836 C  CB  . GLU   V  8  149 ? -6.873  -168.369 63.952  1.00 108.49 ? 150 GLU   V CB  1 
ATOM   38837 C  CG  . GLU   V  8  149 ? -7.950  -168.016 64.960  1.00 108.61 ? 150 GLU   V CG  1 
ATOM   38838 C  CD  . GLU   V  8  149 ? -7.511  -168.126 66.410  1.00 106.76 ? 150 GLU   V CD  1 
ATOM   38839 O  OE1 . GLU   V  8  149 ? -6.777  -169.077 66.737  1.00 105.70 ? 150 GLU   V OE1 1 
ATOM   38840 O  OE2 . GLU   V  8  149 ? -7.896  -167.252 67.207  1.00 107.43 ? 150 GLU   V OE2 1 
ATOM   38841 N  N   . ALA   V  8  150 ? -5.427  -169.294 61.331  1.00 104.10 ? 151 ALA   V N   1 
ATOM   38842 C  CA  . ALA   V  8  150 ? -4.194  -169.358 60.513  1.00 102.53 ? 151 ALA   V CA  1 
ATOM   38843 C  C   . ALA   V  8  150 ? -4.511  -169.052 59.046  1.00 101.00 ? 151 ALA   V C   1 
ATOM   38844 O  O   . ALA   V  8  150 ? -3.685  -168.375 58.407  1.00 103.55 ? 151 ALA   V O   1 
ATOM   38845 C  CB  . ALA   V  8  150 ? -3.544  -170.708 60.662  1.00 104.77 ? 151 ALA   V CB  1 
ATOM   38846 N  N   . ILE   V  8  151 ? -5.646  -169.543 58.531  1.00 101.32 ? 152 ILE   V N   1 
ATOM   38847 C  CA  . ILE   V  8  151 ? -6.127  -169.257 57.143  1.00 102.38 ? 152 ILE   V CA  1 
ATOM   38848 C  C   . ILE   V  8  151 ? -6.399  -167.752 57.030  1.00 100.60 ? 152 ILE   V C   1 
ATOM   38849 O  O   . ILE   V  8  151 ? -5.973  -167.145 56.025  1.00 96.88  ? 152 ILE   V O   1 
ATOM   38850 C  CB  . ILE   V  8  151 ? -7.379  -170.084 56.777  1.00 105.36 ? 152 ILE   V CB  1 
ATOM   38851 C  CG1 . ILE   V  8  151 ? -7.096  -171.589 56.749  1.00 105.95 ? 152 ILE   V CG1 1 
ATOM   38852 C  CG2 . ILE   V  8  151 ? -7.966  -169.610 55.453  1.00 104.16 ? 152 ILE   V CG2 1 
ATOM   38853 C  CD1 . ILE   V  8  151 ? -8.340  -172.451 56.804  1.00 106.75 ? 152 ILE   V CD1 1 
ATOM   38854 N  N   . LYS   V  8  152 ? -7.088  -167.183 58.024  1.00 101.36 ? 153 LYS   V N   1 
ATOM   38855 C  CA  . LYS   V  8  152 ? -7.457  -165.741 58.070  1.00 99.75  ? 153 LYS   V CA  1 
ATOM   38856 C  C   . LYS   V  8  152 ? -6.177  -164.895 58.049  1.00 95.82  ? 153 LYS   V C   1 
ATOM   38857 O  O   . LYS   V  8  152 ? -6.102  -163.970 57.223  1.00 90.14  ? 153 LYS   V O   1 
ATOM   38858 C  CB  . LYS   V  8  152 ? -8.313  -165.437 59.306  1.00 103.47 ? 153 LYS   V CB  1 
ATOM   38859 C  CG  . LYS   V  8  152 ? -9.476  -164.485 59.064  1.00 105.53 ? 153 LYS   V CG  1 
ATOM   38860 C  CD  . LYS   V  8  152 ? -9.093  -163.023 59.067  1.00 108.12 ? 153 LYS   V CD  1 
ATOM   38861 C  CE  . LYS   V  8  152 ? -10.208 -162.135 58.557  1.00 111.38 ? 153 LYS   V CE  1 
ATOM   38862 N  NZ  . LYS   V  8  152 ? -9.863  -160.698 58.667  1.00 113.82 ? 153 LYS   V NZ  1 
ATOM   38863 N  N   . LEU   V  8  153 ? -5.209  -165.222 58.912  1.00 92.95  ? 154 LEU   V N   1 
ATOM   38864 C  CA  . LEU   V  8  153 ? -3.905  -164.514 59.033  1.00 93.26  ? 154 LEU   V CA  1 
ATOM   38865 C  C   . LEU   V  8  153 ? -3.140  -164.603 57.709  1.00 95.06  ? 154 LEU   V C   1 
ATOM   38866 O  O   . LEU   V  8  153 ? -2.635  -163.562 57.255  1.00 98.12  ? 154 LEU   V O   1 
ATOM   38867 C  CB  . LEU   V  8  153 ? -3.089  -165.138 60.169  1.00 92.74  ? 154 LEU   V CB  1 
ATOM   38868 C  CG  . LEU   V  8  153 ? -1.719  -164.510 60.421  1.00 93.49  ? 154 LEU   V CG  1 
ATOM   38869 C  CD1 . LEU   V  8  153 ? -1.840  -163.022 60.716  1.00 93.95  ? 154 LEU   V CD1 1 
ATOM   38870 C  CD2 . LEU   V  8  153 ? -1.006  -165.218 61.561  1.00 94.35  ? 154 LEU   V CD2 1 
ATOM   38871 N  N   . ALA   V  8  154 ? -3.043  -165.804 57.133  1.00 96.59  ? 155 ALA   V N   1 
ATOM   38872 C  CA  . ALA   V  8  154 ? -2.311  -166.086 55.875  1.00 100.26 ? 155 ALA   V CA  1 
ATOM   38873 C  C   . ALA   V  8  154 ? -2.905  -165.258 54.730  1.00 101.97 ? 155 ALA   V C   1 
ATOM   38874 O  O   . ALA   V  8  154 ? -2.129  -164.560 54.052  1.00 104.59 ? 155 ALA   V O   1 
ATOM   38875 C  CB  . ALA   V  8  154 ? -2.346  -167.563 55.565  1.00 101.01 ? 155 ALA   V CB  1 
ATOM   38876 N  N   . SER   V  8  155 ? -4.227  -165.318 54.535  1.00 103.17 ? 156 SER   V N   1 
ATOM   38877 C  CA  . SER   V  8  155 ? -4.942  -164.642 53.417  1.00 103.66 ? 156 SER   V CA  1 
ATOM   38878 C  C   . SER   V  8  155 ? -4.931  -163.118 53.614  1.00 105.03 ? 156 SER   V C   1 
ATOM   38879 O  O   . SER   V  8  155 ? -4.897  -162.401 52.594  1.00 103.59 ? 156 SER   V O   1 
ATOM   38880 C  CB  . SER   V  8  155 ? -6.345  -165.167 53.252  1.00 104.54 ? 156 SER   V CB  1 
ATOM   38881 O  OG  . SER   V  8  155 ? -7.187  -164.702 54.294  1.00 107.04 ? 156 SER   V OG  1 
ATOM   38882 N  N   . ASP   V  8  156 ? -4.961  -162.648 54.868  1.00 105.19 ? 157 ASP   V N   1 
ATOM   38883 C  CA  . ASP   V  8  156 ? -4.835  -161.209 55.236  1.00 101.17 ? 157 ASP   V CA  1 
ATOM   38884 C  C   . ASP   V  8  156 ? -3.441  -160.701 54.851  1.00 97.30  ? 157 ASP   V C   1 
ATOM   38885 O  O   . ASP   V  8  156 ? -3.352  -159.576 54.319  1.00 90.82  ? 157 ASP   V O   1 
ATOM   38886 C  CB  . ASP   V  8  156 ? -5.086  -160.972 56.729  1.00 102.93 ? 157 ASP   V CB  1 
ATOM   38887 C  CG  . ASP   V  8  156 ? -6.554  -160.903 57.116  1.00 105.33 ? 157 ASP   V CG  1 
ATOM   38888 O  OD1 . ASP   V  8  156 ? -7.410  -161.182 56.249  1.00 105.26 ? 157 ASP   V OD1 1 
ATOM   38889 O  OD2 . ASP   V  8  156 ? -6.830  -160.572 58.285  1.00 107.96 ? 157 ASP   V OD2 1 
ATOM   38890 N  N   . ALA   V  8  157 ? -2.403  -161.496 55.127  1.00 96.08  ? 158 ALA   V N   1 
ATOM   38891 C  CA  . ALA   V  8  157 ? -0.989  -161.197 54.797  1.00 96.05  ? 158 ALA   V CA  1 
ATOM   38892 C  C   . ALA   V  8  157 ? -0.825  -161.105 53.275  1.00 95.11  ? 158 ALA   V C   1 
ATOM   38893 O  O   . ALA   V  8  157 ? -0.096  -160.206 52.815  1.00 93.38  ? 158 ALA   V O   1 
ATOM   38894 C  CB  . ALA   V  8  157 ? -0.078  -162.242 55.393  1.00 95.60  ? 158 ALA   V CB  1 
ATOM   38895 N  N   . ILE   V  8  158 ? -1.481  -161.999 52.525  1.00 96.94  ? 159 ILE   V N   1 
ATOM   38896 C  CA  . ILE   V  8  158 ? -1.465  -162.002 51.031  1.00 97.86  ? 159 ILE   V CA  1 
ATOM   38897 C  C   . ILE   V  8  158 ? -2.170  -160.734 50.532  1.00 98.31  ? 159 ILE   V C   1 
ATOM   38898 O  O   . ILE   V  8  158 ? -1.617  -160.080 49.622  1.00 95.34  ? 159 ILE   V O   1 
ATOM   38899 C  CB  . ILE   V  8  158 ? -2.097  -163.289 50.455  1.00 97.91  ? 159 ILE   V CB  1 
ATOM   38900 C  CG1 . ILE   V  8  158 ? -1.301  -164.540 50.839  1.00 97.51  ? 159 ILE   V CG1 1 
ATOM   38901 C  CG2 . ILE   V  8  158 ? -2.269  -163.184 48.945  1.00 97.83  ? 159 ILE   V CG2 1 
ATOM   38902 C  CD1 . ILE   V  8  158 ? 0.136   -164.541 50.358  1.00 96.59  ? 159 ILE   V CD1 1 
ATOM   38903 N  N   . GLN   V  8  159 ? -3.333  -160.403 51.106  1.00 99.81  ? 160 GLN   V N   1 
ATOM   38904 C  CA  . GLN   V  8  159 ? -4.144  -159.212 50.725  1.00 100.97 ? 160 GLN   V CA  1 
ATOM   38905 C  C   . GLN   V  8  159 ? -3.292  -157.945 50.876  1.00 101.01 ? 160 GLN   V C   1 
ATOM   38906 O  O   . GLN   V  8  159 ? -3.352  -157.095 49.968  1.00 105.76 ? 160 GLN   V O   1 
ATOM   38907 C  CB  . GLN   V  8  159 ? -5.432  -159.125 51.547  1.00 101.10 ? 160 GLN   V CB  1 
ATOM   38908 C  CG  . GLN   V  8  159 ? -6.547  -160.014 51.015  1.00 103.31 ? 160 GLN   V CG  1 
ATOM   38909 C  CD  . GLN   V  8  159 ? -7.901  -159.622 51.552  1.00 105.27 ? 160 GLN   V CD  1 
ATOM   38910 O  OE1 . GLN   V  8  159 ? -8.428  -158.559 51.234  1.00 105.03 ? 160 GLN   V OE1 1 
ATOM   38911 N  NE2 . GLN   V  8  159 ? -8.485  -160.486 52.368  1.00 109.09 ? 160 GLN   V NE2 1 
ATOM   38912 N  N   . ALA   V  8  160 ? -2.518  -157.833 51.961  1.00 98.96  ? 161 ALA   V N   1 
ATOM   38913 C  CA  . ALA   V  8  160 ? -1.583  -156.708 52.209  1.00 98.01  ? 161 ALA   V CA  1 
ATOM   38914 C  C   . ALA   V  8  160 ? -0.736  -156.474 50.955  1.00 96.24  ? 161 ALA   V C   1 
ATOM   38915 O  O   . ALA   V  8  160 ? -0.652  -155.319 50.511  1.00 100.38 ? 161 ALA   V O   1 
ATOM   38916 C  CB  . ALA   V  8  160 ? -0.712  -156.990 53.408  1.00 97.48  ? 161 ALA   V CB  1 
ATOM   38917 N  N   . GLY   V  8  161 ? -0.150  -157.541 50.403  1.00 96.13  ? 162 GLY   V N   1 
ATOM   38918 C  CA  . GLY   V  8  161 ? 0.671   -157.498 49.179  1.00 93.81  ? 162 GLY   V CA  1 
ATOM   38919 C  C   . GLY   V  8  161 ? -0.149  -157.099 47.964  1.00 92.53  ? 162 GLY   V C   1 
ATOM   38920 O  O   . GLY   V  8  161 ? 0.310   -156.223 47.210  1.00 92.17  ? 162 GLY   V O   1 
ATOM   38921 N  N   . ILE   V  8  162 ? -1.323  -157.714 47.785  1.00 93.21  ? 163 ILE   V N   1 
ATOM   38922 C  CA  . ILE   V  8  162 ? -2.229  -157.486 46.617  1.00 94.57  ? 163 ILE   V CA  1 
ATOM   38923 C  C   . ILE   V  8  162 ? -2.500  -155.981 46.487  1.00 93.23  ? 163 ILE   V C   1 
ATOM   38924 O  O   . ILE   V  8  162 ? -2.363  -155.452 45.363  1.00 86.98  ? 163 ILE   V O   1 
ATOM   38925 C  CB  . ILE   V  8  162 ? -3.524  -158.318 46.748  1.00 98.81  ? 163 ILE   V CB  1 
ATOM   38926 C  CG1 . ILE   V  8  162 ? -3.247  -159.809 46.524  1.00 102.02 ? 163 ILE   V CG1 1 
ATOM   38927 C  CG2 . ILE   V  8  162 ? -4.612  -157.804 45.813  1.00 97.77  ? 163 ILE   V CG2 1 
ATOM   38928 C  CD1 . ILE   V  8  162 ? -4.372  -160.732 46.948  1.00 104.29 ? 163 ILE   V CD1 1 
ATOM   38929 N  N   . TRP   V  8  163 ? -2.835  -155.317 47.597  1.00 90.55  ? 164 TRP   V N   1 
ATOM   38930 C  CA  . TRP   V  8  163 ? -3.258  -153.891 47.624  1.00 90.00  ? 164 TRP   V CA  1 
ATOM   38931 C  C   . TRP   V  8  163 ? -2.041  -152.955 47.560  1.00 91.46  ? 164 TRP   V C   1 
ATOM   38932 O  O   . TRP   V  8  163 ? -2.129  -151.942 46.836  1.00 90.88  ? 164 TRP   V O   1 
ATOM   38933 C  CB  . TRP   V  8  163 ? -4.132  -153.607 48.855  1.00 90.29  ? 164 TRP   V CB  1 
ATOM   38934 C  CG  . TRP   V  8  163 ? -5.321  -154.510 48.975  1.00 91.03  ? 164 TRP   V CG  1 
ATOM   38935 C  CD1 . TRP   V  8  163 ? -5.677  -155.260 50.057  1.00 92.51  ? 164 TRP   V CD1 1 
ATOM   38936 C  CD2 . TRP   V  8  163 ? -6.309  -154.775 47.964  1.00 94.30  ? 164 TRP   V CD2 1 
ATOM   38937 N  NE1 . TRP   V  8  163 ? -6.817  -155.969 49.793  1.00 94.57  ? 164 TRP   V NE1 1 
ATOM   38938 C  CE2 . TRP   V  8  163 ? -7.229  -155.693 48.517  1.00 95.45  ? 164 TRP   V CE2 1 
ATOM   38939 C  CE3 . TRP   V  8  163 ? -6.512  -154.326 46.654  1.00 95.15  ? 164 TRP   V CE3 1 
ATOM   38940 C  CZ2 . TRP   V  8  163 ? -8.329  -156.168 47.803  1.00 98.15  ? 164 TRP   V CZ2 1 
ATOM   38941 C  CZ3 . TRP   V  8  163 ? -7.600  -154.794 45.950  1.00 98.86  ? 164 TRP   V CZ3 1 
ATOM   38942 C  CH2 . TRP   V  8  163 ? -8.494  -155.703 46.519  1.00 99.57  ? 164 TRP   V CH2 1 
ATOM   38943 N  N   . ASN   V  8  164 ? -0.949  -153.281 48.263  1.00 89.57  ? 165 ASN   V N   1 
ATOM   38944 C  CA  . ASN   V  8  164 ? 0.170   -152.339 48.546  1.00 90.09  ? 165 ASN   V CA  1 
ATOM   38945 C  C   . ASN   V  8  164 ? 1.360   -152.576 47.605  1.00 90.42  ? 165 ASN   V C   1 
ATOM   38946 O  O   . ASN   V  8  164 ? 2.052   -151.586 47.302  1.00 91.17  ? 165 ASN   V O   1 
ATOM   38947 C  CB  . ASN   V  8  164 ? 0.598   -152.406 50.016  1.00 89.57  ? 165 ASN   V CB  1 
ATOM   38948 C  CG  . ASN   V  8  164 ? -0.530  -152.081 50.976  1.00 89.43  ? 165 ASN   V CG  1 
ATOM   38949 O  OD1 . ASN   V  8  164 ? -0.856  -152.874 51.856  1.00 89.64  ? 165 ASN   V OD1 1 
ATOM   38950 N  ND2 . ASN   V  8  164 ? -1.142  -150.920 50.818  1.00 87.82  ? 165 ASN   V ND2 1 
ATOM   38951 N  N   . ASP   V  8  165 ? 1.600   -153.816 47.164  1.00 89.35  ? 166 ASP   V N   1 
ATOM   38952 C  CA  . ASP   V  8  165 ? 2.708   -154.167 46.231  1.00 89.05  ? 166 ASP   V CA  1 
ATOM   38953 C  C   . ASP   V  8  165 ? 2.171   -154.189 44.794  1.00 88.76  ? 166 ASP   V C   1 
ATOM   38954 O  O   . ASP   V  8  165 ? 1.127   -154.830 44.561  1.00 84.31  ? 166 ASP   V O   1 
ATOM   38955 C  CB  . ASP   V  8  165 ? 3.356   -155.503 46.604  1.00 88.58  ? 166 ASP   V CB  1 
ATOM   38956 C  CG  . ASP   V  8  165 ? 4.547   -155.868 45.735  1.00 90.03  ? 166 ASP   V CG  1 
ATOM   38957 O  OD1 . ASP   V  8  165 ? 5.244   -154.937 45.275  1.00 90.19  ? 166 ASP   V OD1 1 
ATOM   38958 O  OD2 . ASP   V  8  165 ? 4.764   -157.079 45.517  1.00 88.86  ? 166 ASP   V OD2 1 
ATOM   38959 N  N   . LEU   V  8  166 ? 2.855   -153.502 43.873  1.00 90.21  ? 167 LEU   V N   1 
ATOM   38960 C  CA  . LEU   V  8  166 ? 2.497   -153.443 42.428  1.00 91.23  ? 167 LEU   V CA  1 
ATOM   38961 C  C   . LEU   V  8  166 ? 2.851   -154.773 41.755  1.00 91.52  ? 167 LEU   V C   1 
ATOM   38962 O  O   . LEU   V  8  166 ? 2.247   -155.076 40.707  1.00 90.98  ? 167 LEU   V O   1 
ATOM   38963 C  CB  . LEU   V  8  166 ? 3.242   -152.286 41.752  1.00 90.81  ? 167 LEU   V CB  1 
ATOM   38964 C  CG  . LEU   V  8  166 ? 2.946   -150.883 42.278  1.00 90.92  ? 167 LEU   V CG  1 
ATOM   38965 C  CD1 . LEU   V  8  166 ? 3.660   -149.843 41.428  1.00 90.53  ? 167 LEU   V CD1 1 
ATOM   38966 C  CD2 . LEU   V  8  166 ? 1.450   -150.604 42.311  1.00 89.68  ? 167 LEU   V CD2 1 
ATOM   38967 N  N   . GLY   V  8  167 ? 3.780   -155.531 42.327  1.00 92.05  ? 168 GLY   V N   1 
ATOM   38968 C  CA  . GLY   V  8  167 ? 4.161   -156.821 41.723  1.00 89.89  ? 168 GLY   V CA  1 
ATOM   38969 C  C   . GLY   V  8  167 ? 3.166   -157.905 42.081  1.00 87.52  ? 168 GLY   V C   1 
ATOM   38970 O  O   . GLY   V  8  167 ? 3.267   -158.997 41.527  1.00 89.54  ? 168 GLY   V O   1 
ATOM   38971 N  N   . SER   V  8  168 ? 2.214   -157.577 42.949  1.00 87.11  ? 169 SER   V N   1 
ATOM   38972 C  CA  . SER   V  8  168 ? 1.199   -158.543 43.424  1.00 86.24  ? 169 SER   V CA  1 
ATOM   38973 C  C   . SER   V  8  168 ? -0.191  -158.056 43.049  1.00 88.72  ? 169 SER   V C   1 
ATOM   38974 O  O   . SER   V  8  168 ? -0.378  -156.862 42.909  1.00 87.48  ? 169 SER   V O   1 
ATOM   38975 C  CB  . SER   V  8  168 ? 1.266   -158.683 44.908  1.00 90.08  ? 169 SER   V CB  1 
ATOM   38976 O  OG  . SER   V  8  168 ? 2.579   -158.468 45.391  1.00 93.81  ? 169 SER   V OG  1 
ATOM   38977 N  N   . GLY   V  8  169 ? -1.134  -158.972 42.908  1.00 84.93  ? 170 GLY   V N   1 
ATOM   38978 C  CA  . GLY   V  8  169 ? -2.528  -158.584 42.614  1.00 88.19  ? 170 GLY   V CA  1 
ATOM   38979 C  C   . GLY   V  8  169 ? -3.469  -159.764 42.429  1.00 90.46  ? 170 GLY   V C   1 
ATOM   38980 O  O   . GLY   V  8  169 ? -3.065  -160.908 42.711  1.00 92.30  ? 170 GLY   V O   1 
ATOM   38981 N  N   . SER   V  8  170 ? -4.696  -159.470 41.985  1.00 91.96  ? 171 SER   V N   1 
ATOM   38982 C  CA  . SER   V  8  170 ? -5.770  -160.433 41.617  1.00 92.97  ? 171 SER   V CA  1 
ATOM   38983 C  C   . SER   V  8  170 ? -6.275  -161.187 42.856  1.00 94.54  ? 171 SER   V C   1 
ATOM   38984 O  O   . SER   V  8  170 ? -6.861  -160.524 43.732  1.00 98.34  ? 171 SER   V O   1 
ATOM   38985 C  CB  . SER   V  8  170 ? -5.317  -161.359 40.517  1.00 92.84  ? 171 SER   V CB  1 
ATOM   38986 O  OG  . SER   V  8  170 ? -5.099  -160.636 39.316  1.00 93.95  ? 171 SER   V OG  1 
ATOM   38987 N  N   . ASN   V  8  171 ? -6.051  -162.504 42.936  1.00 94.06  ? 172 ASN   V N   1 
ATOM   38988 C  CA  . ASN   V  8  171 ? -6.781  -163.436 43.843  1.00 94.15  ? 172 ASN   V CA  1 
ATOM   38989 C  C   . ASN   V  8  171 ? -5.833  -164.019 44.896  1.00 92.19  ? 172 ASN   V C   1 
ATOM   38990 O  O   . ASN   V  8  171 ? -4.609  -163.837 44.768  1.00 92.31  ? 172 ASN   V O   1 
ATOM   38991 C  CB  . ASN   V  8  171 ? -7.448  -164.569 43.057  1.00 93.15  ? 172 ASN   V CB  1 
ATOM   38992 C  CG  . ASN   V  8  171 ? -8.210  -164.088 41.842  1.00 96.03  ? 172 ASN   V CG  1 
ATOM   38993 O  OD1 . ASN   V  8  171 ? -8.081  -164.664 40.765  1.00 93.77  ? 172 ASN   V OD1 1 
ATOM   38994 N  ND2 . ASN   V  8  171 ? -8.999  -163.035 41.998  1.00 95.22  ? 172 ASN   V ND2 1 
ATOM   38995 N  N   . VAL   V  8  172 ? -6.397  -164.707 45.892  1.00 93.09  ? 173 VAL   V N   1 
ATOM   38996 C  CA  . VAL   V  8  172 ? -5.650  -165.438 46.957  1.00 95.97  ? 173 VAL   V CA  1 
ATOM   38997 C  C   . VAL   V  8  172 ? -5.876  -166.943 46.767  1.00 99.01  ? 173 VAL   V C   1 
ATOM   38998 O  O   . VAL   V  8  172 ? -7.046  -167.379 46.839  1.00 101.43 ? 173 VAL   V O   1 
ATOM   38999 C  CB  . VAL   V  8  172 ? -6.088  -164.992 48.365  1.00 94.31  ? 173 VAL   V CB  1 
ATOM   39000 C  CG1 . VAL   V  8  172 ? -5.290  -165.695 49.453  1.00 94.22  ? 173 VAL   V CG1 1 
ATOM   39001 C  CG2 . VAL   V  8  172 ? -6.009  -163.483 48.533  1.00 93.07  ? 173 VAL   V CG2 1 
ATOM   39002 N  N   . ASP   V  8  173 ? -4.797  -167.698 46.533  1.00 100.36 ? 174 ASP   V N   1 
ATOM   39003 C  CA  . ASP   V  8  173 ? -4.777  -169.184 46.587  1.00 99.72  ? 174 ASP   V CA  1 
ATOM   39004 C  C   . ASP   V  8  173 ? -4.307  -169.609 47.980  1.00 97.21  ? 174 ASP   V C   1 
ATOM   39005 O  O   . ASP   V  8  173 ? -3.443  -168.921 48.548  1.00 93.86  ? 174 ASP   V O   1 
ATOM   39006 C  CB  . ASP   V  8  173 ? -3.872  -169.786 45.511  1.00 100.86 ? 174 ASP   V CB  1 
ATOM   39007 C  CG  . ASP   V  8  173 ? -4.347  -169.554 44.087  1.00 103.86 ? 174 ASP   V CG  1 
ATOM   39008 O  OD1 . ASP   V  8  173 ? -5.511  -169.136 43.913  1.00 100.76 ? 174 ASP   V OD1 1 
ATOM   39009 O  OD2 . ASP   V  8  173 ? -3.547  -169.803 43.161  1.00 109.45 ? 174 ASP   V OD2 1 
ATOM   39010 N  N   . VAL   V  8  174 ? -4.867  -170.700 48.500  1.00 100.13 ? 175 VAL   V N   1 
ATOM   39011 C  CA  . VAL   V  8  174 ? -4.558  -171.263 49.847  1.00 103.03 ? 175 VAL   V CA  1 
ATOM   39012 C  C   . VAL   V  8  174 ? -4.414  -172.779 49.693  1.00 104.07 ? 175 VAL   V C   1 
ATOM   39013 O  O   . VAL   V  8  174 ? -5.104  -173.347 48.825  1.00 102.84 ? 175 VAL   V O   1 
ATOM   39014 C  CB  . VAL   V  8  174 ? -5.655  -170.898 50.868  1.00 106.56 ? 175 VAL   V CB  1 
ATOM   39015 C  CG1 . VAL   V  8  174 ? -5.469  -171.609 52.202  1.00 109.11 ? 175 VAL   V CG1 1 
ATOM   39016 C  CG2 . VAL   V  8  174 ? -5.757  -169.395 51.080  1.00 106.18 ? 175 VAL   V CG2 1 
ATOM   39017 N  N   . CYS   V  8  175 ? -3.538  -173.396 50.491  1.00 103.40 ? 176 CYS   V N   1 
ATOM   39018 C  CA  . CYS   V  8  175 ? -3.474  -174.868 50.695  1.00 104.37 ? 176 CYS   V CA  1 
ATOM   39019 C  C   . CYS   V  8  175 ? -3.306  -175.162 52.187  1.00 103.61 ? 176 CYS   V C   1 
ATOM   39020 O  O   . CYS   V  8  175 ? -2.334  -174.658 52.785  1.00 100.46 ? 176 CYS   V O   1 
ATOM   39021 C  CB  . CYS   V  8  175 ? -2.339  -175.513 49.908  1.00 101.48 ? 176 CYS   V CB  1 
ATOM   39022 S  SG  . CYS   V  8  175 ? -2.402  -177.325 49.920  1.00 101.91 ? 176 CYS   V SG  1 
ATOM   39023 N  N   . VAL   V  8  176 ? -4.232  -175.940 52.754  1.00 108.32 ? 177 VAL   V N   1 
ATOM   39024 C  CA  . VAL   V  8  176 ? -4.234  -176.341 54.190  1.00 109.81 ? 177 VAL   V CA  1 
ATOM   39025 C  C   . VAL   V  8  176 ? -3.744  -177.789 54.282  1.00 109.99 ? 177 VAL   V C   1 
ATOM   39026 O  O   . VAL   V  8  176 ? -4.412  -178.678 53.716  1.00 112.34 ? 177 VAL   V O   1 
ATOM   39027 C  CB  . VAL   V  8  176 ? -5.626  -176.183 54.831  1.00 111.43 ? 177 VAL   V CB  1 
ATOM   39028 C  CG1 . VAL   V  8  176 ? -5.557  -176.369 56.339  1.00 112.22 ? 177 VAL   V CG1 1 
ATOM   39029 C  CG2 . VAL   V  8  176 ? -6.268  -174.848 54.484  1.00 111.06 ? 177 VAL   V CG2 1 
ATOM   39030 N  N   . MET   V  8  177 ? -2.613  -177.997 54.960  1.00 107.18 ? 178 MET   V N   1 
ATOM   39031 C  CA  . MET   V  8  177 ? -2.033  -179.332 55.252  1.00 105.75 ? 178 MET   V CA  1 
ATOM   39032 C  C   . MET   V  8  177 ? -2.157  -179.596 56.754  1.00 106.29 ? 178 MET   V C   1 
ATOM   39033 O  O   . MET   V  8  177 ? -1.354  -179.034 57.524  1.00 104.85 ? 178 MET   V O   1 
ATOM   39034 C  CB  . MET   V  8  177 ? -0.564  -179.392 54.829  1.00 102.96 ? 178 MET   V CB  1 
ATOM   39035 C  CG  . MET   V  8  177 ? -0.385  -179.499 53.331  1.00 104.94 ? 178 MET   V CG  1 
ATOM   39036 S  SD  . MET   V  8  177 ? 1.052   -178.574 52.748  1.00 104.44 ? 178 MET   V SD  1 
ATOM   39037 C  CE  . MET   V  8  177 ? 0.416   -176.902 52.826  1.00 104.74 ? 178 MET   V CE  1 
ATOM   39038 N  N   . GLU   V  8  178 ? -3.147  -180.405 57.139  1.00 108.22 ? 179 GLU   V N   1 
ATOM   39039 C  CA  . GLU   V  8  178 ? -3.447  -180.780 58.546  1.00 109.01 ? 179 GLU   V CA  1 
ATOM   39040 C  C   . GLU   V  8  178 ? -2.982  -182.224 58.773  1.00 109.33 ? 179 GLU   V C   1 
ATOM   39041 O  O   . GLU   V  8  178 ? -3.060  -183.018 57.816  1.00 108.44 ? 179 GLU   V O   1 
ATOM   39042 C  CB  . GLU   V  8  178 ? -4.944  -180.602 58.805  1.00 111.78 ? 179 GLU   V CB  1 
ATOM   39043 C  CG  . GLU   V  8  178 ? -5.347  -180.800 60.253  1.00 115.34 ? 179 GLU   V CG  1 
ATOM   39044 C  CD  . GLU   V  8  178 ? -6.675  -180.161 60.628  1.00 115.85 ? 179 GLU   V CD  1 
ATOM   39045 O  OE1 . GLU   V  8  178 ? -6.874  -179.882 61.826  1.00 117.78 ? 179 GLU   V OE1 1 
ATOM   39046 O  OE2 . GLU   V  8  178 ? -7.505  -179.938 59.722  1.00 114.66 ? 179 GLU   V OE2 1 
ATOM   39047 N  N   . ILE   V  8  179 ? -2.506  -182.544 59.982  1.00 106.33 ? 180 ILE   V N   1 
ATOM   39048 C  CA  . ILE   V  8  179 ? -2.018  -183.907 60.358  1.00 105.55 ? 180 ILE   V CA  1 
ATOM   39049 C  C   . ILE   V  8  179 ? -3.225  -184.848 60.445  1.00 106.12 ? 180 ILE   V C   1 
ATOM   39050 O  O   . ILE   V  8  179 ? -4.199  -184.492 61.136  1.00 105.36 ? 180 ILE   V O   1 
ATOM   39051 C  CB  . ILE   V  8  179 ? -1.226  -183.893 61.684  1.00 104.53 ? 180 ILE   V CB  1 
ATOM   39052 C  CG1 . ILE   V  8  179 ? -0.014  -182.959 61.634  1.00 102.27 ? 180 ILE   V CG1 1 
ATOM   39053 C  CG2 . ILE   V  8  179 ? -0.813  -185.304 62.072  1.00 105.56 ? 180 ILE   V CG2 1 
ATOM   39054 C  CD1 . ILE   V  8  179 ? 0.476   -182.524 62.996  1.00 101.58 ? 180 ILE   V CD1 1 
ATOM   39055 N  N   . GLY   V  8  180 ? -3.151  -186.002 59.771  1.00 106.43 ? 181 GLY   V N   1 
ATOM   39056 C  CA  . GLY   V  8  180 ? -4.176  -187.065 59.815  1.00 109.01 ? 181 GLY   V CA  1 
ATOM   39057 C  C   . GLY   V  8  180 ? -5.301  -186.863 58.807  1.00 111.23 ? 181 GLY   V C   1 
ATOM   39058 O  O   . GLY   V  8  180 ? -6.220  -187.707 58.793  1.00 112.15 ? 181 GLY   V O   1 
ATOM   39059 N  N   . LYS   V  8  181 ? -5.248  -185.797 57.998  1.00 109.95 ? 182 LYS   V N   1 
ATOM   39060 C  CA  . LYS   V  8  181 ? -6.309  -185.427 57.017  1.00 111.76 ? 182 LYS   V CA  1 
ATOM   39061 C  C   . LYS   V  8  181 ? -5.704  -185.046 55.669  1.00 109.41 ? 182 LYS   V C   1 
ATOM   39062 O  O   . LYS   V  8  181 ? -4.623  -184.432 55.679  1.00 111.89 ? 182 LYS   V O   1 
ATOM   39063 C  CB  . LYS   V  8  181 ? -7.071  -184.182 57.462  1.00 112.95 ? 182 LYS   V CB  1 
ATOM   39064 C  CG  . LYS   V  8  181 ? -7.938  -184.355 58.691  1.00 115.79 ? 182 LYS   V CG  1 
ATOM   39065 C  CD  . LYS   V  8  181 ? -9.008  -183.305 58.767  1.00 119.27 ? 182 LYS   V CD  1 
ATOM   39066 C  CE  . LYS   V  8  181 ? -9.995  -183.569 59.878  1.00 121.90 ? 182 LYS   V CE  1 
ATOM   39067 N  NZ  . LYS   V  8  181 ? -11.179 -182.690 59.752  1.00 126.21 ? 182 LYS   V NZ  1 
ATOM   39068 N  N   . ASP   V  8  182 ? -6.400  -185.336 54.566  1.00 109.80 ? 183 ASP   V N   1 
ATOM   39069 C  CA  . ASP   V  8  182 ? -5.944  -185.000 53.190  1.00 110.27 ? 183 ASP   V CA  1 
ATOM   39070 C  C   . ASP   V  8  182 ? -5.695  -183.490 53.109  1.00 107.51 ? 183 ASP   V C   1 
ATOM   39071 O  O   . ASP   V  8  182 ? -6.533  -182.726 53.626  1.00 106.56 ? 183 ASP   V O   1 
ATOM   39072 C  CB  . ASP   V  8  182 ? -6.962  -185.443 52.135  1.00 113.22 ? 183 ASP   V CB  1 
ATOM   39073 C  CG  . ASP   V  8  182 ? -7.076  -186.949 51.964  1.00 115.71 ? 183 ASP   V CG  1 
ATOM   39074 O  OD1 . ASP   V  8  182 ? -6.209  -187.673 52.499  1.00 120.59 ? 183 ASP   V OD1 1 
ATOM   39075 O  OD2 . ASP   V  8  182 ? -8.032  -187.388 51.296  1.00 118.60 ? 183 ASP   V OD2 1 
ATOM   39076 N  N   . ALA   V  8  183 ? -4.577  -183.082 52.501  1.00 104.75 ? 184 ALA   V N   1 
ATOM   39077 C  CA  . ALA   V  8  183 ? -4.271  -181.670 52.173  1.00 104.86 ? 184 ALA   V CA  1 
ATOM   39078 C  C   . ALA   V  8  183 ? -5.406  -181.121 51.302  1.00 107.02 ? 184 ALA   V C   1 
ATOM   39079 O  O   . ALA   V  8  183 ? -5.760  -181.806 50.330  1.00 109.15 ? 184 ALA   V O   1 
ATOM   39080 C  CB  . ALA   V  8  183 ? -2.948  -181.586 51.454  1.00 102.38 ? 184 ALA   V CB  1 
ATOM   39081 N  N   . GLU   V  8  184 ? -5.975  -179.955 51.631  1.00 108.44 ? 185 GLU   V N   1 
ATOM   39082 C  CA  . GLU   V  8  184 ? -7.036  -179.333 50.788  1.00 108.14 ? 185 GLU   V CA  1 
ATOM   39083 C  C   . GLU   V  8  184 ? -6.475  -178.073 50.116  1.00 104.18 ? 185 GLU   V C   1 
ATOM   39084 O  O   . GLU   V  8  184 ? -6.142  -177.105 50.824  1.00 97.86  ? 185 GLU   V O   1 
ATOM   39085 C  CB  . GLU   V  8  184 ? -8.341  -179.106 51.560  1.00 113.91 ? 185 GLU   V CB  1 
ATOM   39086 C  CG  . GLU   V  8  184 ? -8.244  -178.214 52.785  1.00 114.19 ? 185 GLU   V CG  1 
ATOM   39087 C  CD  . GLU   V  8  184 ? -9.594  -177.907 53.415  1.00 117.38 ? 185 GLU   V CD  1 
ATOM   39088 O  OE1 . GLU   V  8  184 ? -9.663  -177.823 54.657  1.00 122.85 ? 185 GLU   V OE1 1 
ATOM   39089 O  OE2 . GLU   V  8  184 ? -10.576 -177.752 52.660  1.00 118.26 ? 185 GLU   V OE2 1 
ATOM   39090 N  N   . TYR   V  8  185 ? -6.346  -178.135 48.787  1.00 103.57 ? 186 TYR   V N   1 
ATOM   39091 C  CA  . TYR   V  8  185 ? -5.940  -177.029 47.881  1.00 102.33 ? 186 TYR   V CA  1 
ATOM   39092 C  C   . TYR   V  8  185 ? -7.165  -176.160 47.575  1.00 102.46 ? 186 TYR   V C   1 
ATOM   39093 O  O   . TYR   V  8  185 ? -8.106  -176.645 46.925  1.00 103.40 ? 186 TYR   V O   1 
ATOM   39094 C  CB  . TYR   V  8  185 ? -5.329  -177.605 46.600  1.00 104.54 ? 186 TYR   V CB  1 
ATOM   39095 C  CG  . TYR   V  8  185 ? -4.921  -176.598 45.554  1.00 103.88 ? 186 TYR   V CG  1 
ATOM   39096 C  CD1 . TYR   V  8  185 ? -4.146  -175.496 45.877  1.00 102.29 ? 186 TYR   V CD1 1 
ATOM   39097 C  CD2 . TYR   V  8  185 ? -5.278  -176.769 44.226  1.00 105.21 ? 186 TYR   V CD2 1 
ATOM   39098 C  CE1 . TYR   V  8  185 ? -3.757  -174.578 44.913  1.00 104.94 ? 186 TYR   V CE1 1 
ATOM   39099 C  CE2 . TYR   V  8  185 ? -4.893  -175.865 43.249  1.00 107.02 ? 186 TYR   V CE2 1 
ATOM   39100 C  CZ  . TYR   V  8  185 ? -4.130  -174.763 43.593  1.00 105.41 ? 186 TYR   V CZ  1 
ATOM   39101 O  OH  . TYR   V  8  185 ? -3.750  -173.864 42.638  1.00 108.76 ? 186 TYR   V OH  1 
ATOM   39102 N  N   . LEU   V  8  186 ? -7.148  -174.908 48.033  1.00 101.00 ? 187 LEU   V N   1 
ATOM   39103 C  CA  . LEU   V  8  186 ? -8.260  -173.938 47.851  1.00 101.75 ? 187 LEU   V CA  1 
ATOM   39104 C  C   . LEU   V  8  186 ? -7.864  -172.920 46.777  1.00 97.85  ? 187 LEU   V C   1 
ATOM   39105 O  O   . LEU   V  8  186 ? -7.405  -171.823 47.138  1.00 94.69  ? 187 LEU   V O   1 
ATOM   39106 C  CB  . LEU   V  8  186 ? -8.558  -173.268 49.195  1.00 102.19 ? 187 LEU   V CB  1 
ATOM   39107 C  CG  . LEU   V  8  186 ? -9.137  -174.191 50.266  1.00 105.00 ? 187 LEU   V CG  1 
ATOM   39108 C  CD1 . LEU   V  8  186 ? -9.129  -173.516 51.627  1.00 104.35 ? 187 LEU   V CD1 1 
ATOM   39109 C  CD2 . LEU   V  8  186 ? -10.545 -174.639 49.899  1.00 107.84 ? 187 LEU   V CD2 1 
ATOM   39110 N  N   . ARG   V  8  187 ? -8.031  -173.301 45.508  1.00 100.60 ? 188 ARG   V N   1 
ATOM   39111 C  CA  . ARG   V  8  187 ? -7.732  -172.468 44.312  1.00 100.56 ? 188 ARG   V CA  1 
ATOM   39112 C  C   . ARG   V  8  187 ? -8.739  -171.314 44.241  1.00 100.45 ? 188 ARG   V C   1 
ATOM   39113 O  O   . ARG   V  8  187 ? -9.952  -171.594 44.210  1.00 96.88  ? 188 ARG   V O   1 
ATOM   39114 C  CB  . ARG   V  8  187 ? -7.773  -173.343 43.055  1.00 103.74 ? 188 ARG   V CB  1 
ATOM   39115 C  CG  . ARG   V  8  187 ? -7.766  -172.576 41.741  1.00 103.33 ? 188 ARG   V CG  1 
ATOM   39116 C  CD  . ARG   V  8  187 ? -6.517  -171.739 41.564  1.00 102.38 ? 188 ARG   V CD  1 
ATOM   39117 N  NE  . ARG   V  8  187 ? -6.306  -171.424 40.158  1.00 103.53 ? 188 ARG   V NE  1 
ATOM   39118 C  CZ  . ARG   V  8  187 ? -5.363  -170.615 39.686  1.00 101.74 ? 188 ARG   V CZ  1 
ATOM   39119 N  NH1 . ARG   V  8  187 ? -4.530  -169.997 40.508  1.00 101.08 ? 188 ARG   V NH1 1 
ATOM   39120 N  NH2 . ARG   V  8  187 ? -5.272  -170.413 38.382  1.00 101.42 ? 188 ARG   V NH2 1 
ATOM   39121 N  N   . ASN   V  8  188 ? -8.244  -170.072 44.212  1.00 99.18  ? 189 ASN   V N   1 
ATOM   39122 C  CA  . ASN   V  8  188 ? -9.057  -168.824 44.199  1.00 99.31  ? 189 ASN   V CA  1 
ATOM   39123 C  C   . ASN   V  8  188 ? -9.973  -168.810 45.429  1.00 98.86  ? 189 ASN   V C   1 
ATOM   39124 O  O   . ASN   V  8  188 ? -11.202 -168.670 45.261  1.00 96.60  ? 189 ASN   V O   1 
ATOM   39125 C  CB  . ASN   V  8  188 ? -9.832  -168.669 42.888  1.00 99.75  ? 189 ASN   V CB  1 
ATOM   39126 C  CG  . ASN   V  8  188 ? -8.932  -168.394 41.701  1.00 96.85  ? 189 ASN   V CG  1 
ATOM   39127 O  OD1 . ASN   V  8  188 ? -7.708  -168.402 41.820  1.00 92.57  ? 189 ASN   V OD1 1 
ATOM   39128 N  ND2 . ASN   V  8  188 ? -9.532  -168.146 40.549  1.00 98.18  ? 189 ASN   V ND2 1 
ATOM   39129 N  N   . TYR   V  8  189 ? -9.378  -168.957 46.616  1.00 100.14 ? 190 TYR   V N   1 
ATOM   39130 C  CA  . TYR   V  8  189 ? -10.057 -168.932 47.939  1.00 104.39 ? 190 TYR   V CA  1 
ATOM   39131 C  C   . TYR   V  8  189 ? -10.743 -167.574 48.130  1.00 106.46 ? 190 TYR   V C   1 
ATOM   39132 O  O   . TYR   V  8  189 ? -11.887 -167.546 48.626  1.00 108.85 ? 190 TYR   V O   1 
ATOM   39133 C  CB  . TYR   V  8  189 ? -9.053  -169.230 49.057  1.00 104.23 ? 190 TYR   V CB  1 
ATOM   39134 C  CG  . TYR   V  8  189 ? -9.590  -169.053 50.454  1.00 104.40 ? 190 TYR   V CG  1 
ATOM   39135 C  CD1 . TYR   V  8  189 ? -10.467 -169.972 51.008  1.00 102.32 ? 190 TYR   V CD1 1 
ATOM   39136 C  CD2 . TYR   V  8  189 ? -9.222  -167.962 51.226  1.00 104.16 ? 190 TYR   V CD2 1 
ATOM   39137 C  CE1 . TYR   V  8  189 ? -10.965 -169.813 52.291  1.00 102.06 ? 190 TYR   V CE1 1 
ATOM   39138 C  CE2 . TYR   V  8  189 ? -9.710  -167.789 52.510  1.00 103.62 ? 190 TYR   V CE2 1 
ATOM   39139 C  CZ  . TYR   V  8  189 ? -10.585 -168.717 53.044  1.00 102.66 ? 190 TYR   V CZ  1 
ATOM   39140 O  OH  . TYR   V  8  189 ? -11.072 -168.555 54.307  1.00 105.46 ? 190 TYR   V OH  1 
ATOM   39141 N  N   . LEU   V  8  190 ? -10.054 -166.492 47.751  1.00 107.80 ? 191 LEU   V N   1 
ATOM   39142 C  CA  . LEU   V  8  190 ? -10.601 -165.109 47.690  1.00 111.83 ? 191 LEU   V CA  1 
ATOM   39143 C  C   . LEU   V  8  190 ? -10.402 -164.551 46.279  1.00 108.35 ? 191 LEU   V C   1 
ATOM   39144 O  O   . LEU   V  8  190 ? -9.297  -164.722 45.731  1.00 109.03 ? 191 LEU   V O   1 
ATOM   39145 C  CB  . LEU   V  8  190 ? -9.881  -164.225 48.711  1.00 112.56 ? 191 LEU   V CB  1 
ATOM   39146 C  CG  . LEU   V  8  190 ? -10.289 -164.421 50.169  1.00 117.86 ? 191 LEU   V CG  1 
ATOM   39147 C  CD1 . LEU   V  8  190 ? -9.310  -163.717 51.098  1.00 118.96 ? 191 LEU   V CD1 1 
ATOM   39148 C  CD2 . LEU   V  8  190 ? -11.707 -163.925 50.408  1.00 119.41 ? 191 LEU   V CD2 1 
ATOM   39149 N  N   . THR   V  8  191 ? -11.424 -163.883 45.736  1.00 109.17 ? 192 THR   V N   1 
ATOM   39150 C  CA  . THR   V  8  191 ? -11.371 -163.171 44.430  1.00 108.23 ? 192 THR   V CA  1 
ATOM   39151 C  C   . THR   V  8  191 ? -11.857 -161.738 44.623  1.00 110.79 ? 192 THR   V C   1 
ATOM   39152 O  O   . THR   V  8  191 ? -12.954 -161.388 44.194  1.00 117.24 ? 192 THR   V O   1 
ATOM   39153 C  CB  . THR   V  8  191 ? -12.166 -163.923 43.358  1.00 105.25 ? 192 THR   V CB  1 
ATOM   39154 O  OG1 . THR   V  8  191 ? -13.512 -164.069 43.813  1.00 105.38 ? 192 THR   V OG1 1 
ATOM   39155 C  CG2 . THR   V  8  191 ? -11.570 -165.278 43.043  1.00 102.98 ? 192 THR   V CG2 1 
ATOM   39156 N  N   . PRO   V  8  192 ? -11.045 -160.866 45.266  1.00 108.52 ? 193 PRO   V N   1 
ATOM   39157 C  CA  . PRO   V  8  192 ? -11.464 -159.503 45.588  1.00 108.14 ? 193 PRO   V CA  1 
ATOM   39158 C  C   . PRO   V  8  192 ? -11.169 -158.467 44.490  1.00 106.52 ? 193 PRO   V C   1 
ATOM   39159 O  O   . PRO   V  8  192 ? -11.221 -157.288 44.793  1.00 105.86 ? 193 PRO   V O   1 
ATOM   39160 C  CB  . PRO   V  8  192 ? -10.645 -159.212 46.859  1.00 108.24 ? 193 PRO   V CB  1 
ATOM   39161 C  CG  . PRO   V  8  192 ? -9.372  -160.036 46.715  1.00 108.91 ? 193 PRO   V CG  1 
ATOM   39162 C  CD  . PRO   V  8  192 ? -9.679  -161.147 45.730  1.00 109.69 ? 193 PRO   V CD  1 
ATOM   39163 N  N   . ASN   V  8  193 ? -10.892 -158.912 43.257  1.00 105.70 ? 194 ASN   V N   1 
ATOM   39164 C  CA  . ASN   V  8  193 ? -10.467 -158.037 42.129  1.00 102.12 ? 194 ASN   V CA  1 
ATOM   39165 C  C   . ASN   V  8  193 ? -11.207 -158.442 40.850  1.00 101.38 ? 194 ASN   V C   1 
ATOM   39166 O  O   . ASN   V  8  193 ? -10.558 -158.529 39.791  1.00 104.60 ? 194 ASN   V O   1 
ATOM   39167 C  CB  . ASN   V  8  193 ? -8.947  -158.068 41.942  1.00 99.78  ? 194 ASN   V CB  1 
ATOM   39168 C  CG  . ASN   V  8  193 ? -8.223  -157.212 42.958  1.00 99.16  ? 194 ASN   V CG  1 
ATOM   39169 O  OD1 . ASN   V  8  193 ? -8.320  -155.988 42.919  1.00 94.48  ? 194 ASN   V OD1 1 
ATOM   39170 N  ND2 . ASN   V  8  193 ? -7.506  -157.842 43.875  1.00 99.58  ? 194 ASN   V ND2 1 
ATOM   39171 N  N   . VAL   V  8  194 ? -12.522 -158.655 40.942  1.00 101.51 ? 195 VAL   V N   1 
ATOM   39172 C  CA  . VAL   V  8  194 ? -13.391 -158.936 39.762  1.00 102.97 ? 195 VAL   V CA  1 
ATOM   39173 C  C   . VAL   V  8  194 ? -13.503 -157.639 38.954  1.00 103.27 ? 195 VAL   V C   1 
ATOM   39174 O  O   . VAL   V  8  194 ? -13.724 -156.579 39.570  1.00 105.43 ? 195 VAL   V O   1 
ATOM   39175 C  CB  . VAL   V  8  194 ? -14.774 -159.476 40.176  1.00 102.26 ? 195 VAL   V CB  1 
ATOM   39176 C  CG1 . VAL   V  8  194 ? -15.675 -159.715 38.973  1.00 98.82  ? 195 VAL   V CG1 1 
ATOM   39177 C  CG2 . VAL   V  8  194 ? -14.653 -160.746 41.005  1.00 105.21 ? 195 VAL   V CG2 1 
ATOM   39178 N  N   . ARG   V  8  195 ? -13.335 -157.730 37.632  1.00 108.22 ? 196 ARG   V N   1 
ATOM   39179 C  CA  . ARG   V  8  195 ? -13.442 -156.589 36.681  1.00 109.70 ? 196 ARG   V CA  1 
ATOM   39180 C  C   . ARG   V  8  195 ? -14.899 -156.116 36.637  1.00 110.44 ? 196 ARG   V C   1 
ATOM   39181 O  O   . ARG   V  8  195 ? -15.793 -156.977 36.528  1.00 114.97 ? 196 ARG   V O   1 
ATOM   39182 C  CB  . ARG   V  8  195 ? -12.979 -157.019 35.284  1.00 111.79 ? 196 ARG   V CB  1 
ATOM   39183 C  CG  . ARG   V  8  195 ? -12.101 -156.010 34.558  1.00 109.79 ? 196 ARG   V CG  1 
ATOM   39184 C  CD  . ARG   V  8  195 ? -12.786 -155.233 33.449  1.00 112.72 ? 196 ARG   V CD  1 
ATOM   39185 N  NE  . ARG   V  8  195 ? -12.031 -155.345 32.204  1.00 118.19 ? 196 ARG   V NE  1 
ATOM   39186 C  CZ  . ARG   V  8  195 ? -11.939 -154.412 31.254  1.00 123.59 ? 196 ARG   V CZ  1 
ATOM   39187 N  NH1 . ARG   V  8  195 ? -12.543 -153.240 31.380  1.00 124.64 ? 196 ARG   V NH1 1 
ATOM   39188 N  NH2 . ARG   V  8  195 ? -11.221 -154.659 30.171  1.00 126.69 ? 196 ARG   V NH2 1 
ATOM   39189 N  N   . GLU   V  8  196 ? -15.131 -154.804 36.714  1.00 112.16 ? 197 GLU   V N   1 
ATOM   39190 C  CA  . GLU   V  8  196 ? -16.490 -154.203 36.643  1.00 112.78 ? 197 GLU   V CA  1 
ATOM   39191 C  C   . GLU   V  8  196 ? -17.020 -154.344 35.212  1.00 111.36 ? 197 GLU   V C   1 
ATOM   39192 O  O   . GLU   V  8  196 ? -16.191 -154.428 34.278  1.00 106.25 ? 197 GLU   V O   1 
ATOM   39193 C  CB  . GLU   V  8  196 ? -16.470 -152.737 37.088  1.00 114.86 ? 197 GLU   V CB  1 
ATOM   39194 C  CG  . GLU   V  8  196 ? -15.874 -151.778 36.067  1.00 115.15 ? 197 GLU   V CG  1 
ATOM   39195 C  CD  . GLU   V  8  196 ? -15.979 -150.308 36.443  1.00 114.81 ? 197 GLU   V CD  1 
ATOM   39196 O  OE1 . GLU   V  8  196 ? -16.260 -149.487 35.545  1.00 116.63 ? 197 GLU   V OE1 1 
ATOM   39197 O  OE2 . GLU   V  8  196 ? -15.780 -149.985 37.630  1.00 109.87 ? 197 GLU   V OE2 1 
ATOM   39198 N  N   . GLU   V  8  197 ? -18.347 -154.367 35.055  1.00 111.11 ? 198 GLU   V N   1 
ATOM   39199 C  CA  . GLU   V  8  197 ? -19.028 -154.397 33.733  1.00 113.34 ? 198 GLU   V CA  1 
ATOM   39200 C  C   . GLU   V  8  197 ? -18.460 -153.281 32.854  1.00 113.07 ? 198 GLU   V C   1 
ATOM   39201 O  O   . GLU   V  8  197 ? -18.367 -152.137 33.343  1.00 114.10 ? 198 GLU   V O   1 
ATOM   39202 C  CB  . GLU   V  8  197 ? -20.538 -154.203 33.876  1.00 117.05 ? 198 GLU   V CB  1 
ATOM   39203 C  CG  . GLU   V  8  197 ? -21.333 -155.491 33.817  1.00 123.29 ? 198 GLU   V CG  1 
ATOM   39204 C  CD  . GLU   V  8  197 ? -22.730 -155.308 33.251  1.00 130.53 ? 198 GLU   V CD  1 
ATOM   39205 O  OE1 . GLU   V  8  197 ? -22.841 -154.950 32.059  1.00 133.10 ? 198 GLU   V OE1 1 
ATOM   39206 O  OE2 . GLU   V  8  197 ? -23.703 -155.504 34.005  1.00 140.29 ? 198 GLU   V OE2 1 
ATOM   39207 N  N   . LYS   V  8  198 ? -18.098 -153.606 31.610  1.00 113.25 ? 199 LYS   V N   1 
ATOM   39208 C  CA  . LYS   V  8  198 ? -17.625 -152.616 30.606  1.00 112.56 ? 199 LYS   V CA  1 
ATOM   39209 C  C   . LYS   V  8  198 ? -18.798 -151.708 30.223  1.00 107.77 ? 199 LYS   V C   1 
ATOM   39210 O  O   . LYS   V  8  198 ? -19.951 -152.171 30.270  1.00 107.58 ? 199 LYS   V O   1 
ATOM   39211 C  CB  . LYS   V  8  198 ? -17.016 -153.315 29.385  1.00 116.78 ? 199 LYS   V CB  1 
ATOM   39212 C  CG  . LYS   V  8  198 ? -15.580 -153.789 29.572  1.00 119.54 ? 199 LYS   V CG  1 
ATOM   39213 C  CD  . LYS   V  8  198 ? -14.791 -153.870 28.282  1.00 120.43 ? 199 LYS   V CD  1 
ATOM   39214 C  CE  . LYS   V  8  198 ? -15.011 -155.166 27.534  1.00 123.01 ? 199 LYS   V CE  1 
ATOM   39215 N  NZ  . LYS   V  8  198 ? -13.999 -156.184 27.904  1.00 125.27 ? 199 LYS   V NZ  1 
ATOM   39216 N  N   . GLN   V  8  199 ? -18.502 -150.456 29.869  1.00 107.57 ? 200 GLN   V N   1 
ATOM   39217 C  CA  . GLN   V  8  199 ? -19.504 -149.412 29.524  1.00 109.61 ? 200 GLN   V CA  1 
ATOM   39218 C  C   . GLN   V  8  199 ? -20.185 -149.742 28.191  1.00 109.77 ? 200 GLN   V C   1 
ATOM   39219 O  O   . GLN   V  8  199 ? -21.290 -149.214 27.952  1.00 108.66 ? 200 GLN   V O   1 
ATOM   39220 C  CB  . GLN   V  8  199 ? -18.835 -148.041 29.409  1.00 111.79 ? 200 GLN   V CB  1 
ATOM   39221 C  CG  . GLN   V  8  199 ? -18.302 -147.499 30.728  1.00 110.92 ? 200 GLN   V CG  1 
ATOM   39222 C  CD  . GLN   V  8  199 ? -19.401 -147.103 31.684  1.00 111.91 ? 200 GLN   V CD  1 
ATOM   39223 O  OE1 . GLN   V  8  199 ? -19.477 -147.596 32.807  1.00 107.03 ? 200 GLN   V OE1 1 
ATOM   39224 N  NE2 . GLN   V  8  199 ? -20.266 -146.201 31.246  1.00 115.16 ? 200 GLN   V NE2 1 
ATOM   39225 N  N   . LYS   V  8  200 ? -19.543 -150.565 27.355  1.00 111.57 ? 201 LYS   V N   1 
ATOM   39226 C  CA  . LYS   V  8  200 ? -19.896 -150.729 25.922  1.00 112.07 ? 201 LYS   V CA  1 
ATOM   39227 C  C   . LYS   V  8  200 ? -19.507 -152.129 25.434  1.00 111.03 ? 201 LYS   V C   1 
ATOM   39228 O  O   . LYS   V  8  200 ? -18.464 -152.644 25.886  1.00 111.00 ? 201 LYS   V O   1 
ATOM   39229 C  CB  . LYS   V  8  200 ? -19.162 -149.648 25.126  1.00 110.50 ? 201 LYS   V CB  1 
ATOM   39230 C  CG  . LYS   V  8  200 ? -19.693 -149.380 23.729  1.00 112.50 ? 201 LYS   V CG  1 
ATOM   39231 C  CD  . LYS   V  8  200 ? -18.965 -148.243 23.044  1.00 114.41 ? 201 LYS   V CD  1 
ATOM   39232 C  CE  . LYS   V  8  200 ? -19.479 -147.955 21.650  1.00 117.29 ? 201 LYS   V CE  1 
ATOM   39233 N  NZ  . LYS   V  8  200 ? -19.134 -149.040 20.702  1.00 119.62 ? 201 LYS   V NZ  1 
ATOM   39234 N  N   . SER   V  8  201 ? -20.322 -152.715 24.552  1.00 111.55 ? 202 SER   V N   1 
ATOM   39235 C  CA  . SER   V  8  201 ? -19.978 -153.915 23.743  1.00 112.04 ? 202 SER   V CA  1 
ATOM   39236 C  C   . SER   V  8  201 ? -19.251 -153.455 22.475  1.00 109.71 ? 202 SER   V C   1 
ATOM   39237 O  O   . SER   V  8  201 ? -19.815 -152.615 21.750  1.00 110.07 ? 202 SER   V O   1 
ATOM   39238 C  CB  . SER   V  8  201 ? -21.201 -154.727 23.404  1.00 113.56 ? 202 SER   V CB  1 
ATOM   39239 O  OG  . SER   V  8  201 ? -20.847 -155.897 22.680  1.00 115.99 ? 202 SER   V OG  1 
ATOM   39240 N  N   . TYR   V  8  202 ? -18.050 -153.982 22.223  1.00 109.50 ? 203 TYR   V N   1 
ATOM   39241 C  CA  . TYR   V  8  202 ? -17.199 -153.633 21.054  1.00 110.04 ? 203 TYR   V CA  1 
ATOM   39242 C  C   . TYR   V  8  202 ? -17.305 -154.735 19.995  1.00 109.41 ? 203 TYR   V C   1 
ATOM   39243 O  O   . TYR   V  8  202 ? -16.372 -154.891 19.181  1.00 109.43 ? 203 TYR   V O   1 
ATOM   39244 C  CB  . TYR   V  8  202 ? -15.767 -153.363 21.523  1.00 109.06 ? 203 TYR   V CB  1 
ATOM   39245 C  CG  . TYR   V  8  202 ? -15.663 -152.163 22.426  1.00 112.96 ? 203 TYR   V CG  1 
ATOM   39246 C  CD1 . TYR   V  8  202 ? -15.623 -150.882 21.901  1.00 115.02 ? 203 TYR   V CD1 1 
ATOM   39247 C  CD2 . TYR   V  8  202 ? -15.649 -152.298 23.805  1.00 113.27 ? 203 TYR   V CD2 1 
ATOM   39248 C  CE1 . TYR   V  8  202 ? -15.547 -149.766 22.718  1.00 118.07 ? 203 TYR   V CE1 1 
ATOM   39249 C  CE2 . TYR   V  8  202 ? -15.572 -151.193 24.638  1.00 116.30 ? 203 TYR   V CE2 1 
ATOM   39250 C  CZ  . TYR   V  8  202 ? -15.523 -149.922 24.092  1.00 115.75 ? 203 TYR   V CZ  1 
ATOM   39251 O  OH  . TYR   V  8  202 ? -15.448 -148.822 24.897  1.00 119.96 ? 203 TYR   V OH  1 
ATOM   39252 N  N   . LYS   V  8  203 ? -18.423 -155.469 20.014  1.00 111.07 ? 204 LYS   V N   1 
ATOM   39253 C  CA  . LYS   V  8  203 ? -18.834 -156.443 18.969  1.00 113.32 ? 204 LYS   V CA  1 
ATOM   39254 C  C   . LYS   V  8  203 ? -19.011 -155.692 17.646  1.00 113.56 ? 204 LYS   V C   1 
ATOM   39255 O  O   . LYS   V  8  203 ? -19.852 -154.775 17.603  1.00 115.75 ? 204 LYS   V O   1 
ATOM   39256 C  CB  . LYS   V  8  203 ? -20.140 -157.124 19.385  1.00 118.87 ? 204 LYS   V CB  1 
ATOM   39257 C  CG  . LYS   V  8  203 ? -20.524 -158.366 18.594  1.00 122.29 ? 204 LYS   V CG  1 
ATOM   39258 C  CD  . LYS   V  8  203 ? -21.460 -159.269 19.369  1.00 123.89 ? 204 LYS   V CD  1 
ATOM   39259 C  CE  . LYS   V  8  203 ? -22.505 -159.950 18.514  1.00 124.49 ? 204 LYS   V CE  1 
ATOM   39260 N  NZ  . LYS   V  8  203 ? -23.577 -160.535 19.353  1.00 126.02 ? 204 LYS   V NZ  1 
ATOM   39261 N  N   . PHE   V  8  204 ? -18.248 -156.065 16.616  1.00 111.40 ? 205 PHE   V N   1 
ATOM   39262 C  CA  . PHE   V  8  204 ? -18.207 -155.357 15.310  1.00 113.32 ? 205 PHE   V CA  1 
ATOM   39263 C  C   . PHE   V  8  204 ? -19.317 -155.880 14.403  1.00 117.15 ? 205 PHE   V C   1 
ATOM   39264 O  O   . PHE   V  8  204 ? -19.623 -157.071 14.424  1.00 117.52 ? 205 PHE   V O   1 
ATOM   39265 C  CB  . PHE   V  8  204 ? -16.839 -155.519 14.645  1.00 112.95 ? 205 PHE   V CB  1 
ATOM   39266 C  CG  . PHE   V  8  204 ? -15.711 -154.836 15.373  1.00 113.17 ? 205 PHE   V CG  1 
ATOM   39267 C  CD1 . PHE   V  8  204 ? -15.387 -153.514 15.106  1.00 112.34 ? 205 PHE   V CD1 1 
ATOM   39268 C  CD2 . PHE   V  8  204 ? -14.979 -155.515 16.334  1.00 112.31 ? 205 PHE   V CD2 1 
ATOM   39269 C  CE1 . PHE   V  8  204 ? -14.350 -152.889 15.781  1.00 112.60 ? 205 PHE   V CE1 1 
ATOM   39270 C  CE2 . PHE   V  8  204 ? -13.944 -154.888 17.009  1.00 112.43 ? 205 PHE   V CE2 1 
ATOM   39271 C  CZ  . PHE   V  8  204 ? -13.630 -153.577 16.731  1.00 112.26 ? 205 PHE   V CZ  1 
ATOM   39272 N  N   . PRO   V  8  205 ? -19.963 -155.001 13.599  1.00 117.28 ? 206 PRO   V N   1 
ATOM   39273 C  CA  . PRO   V  8  205 ? -20.801 -155.444 12.484  1.00 118.07 ? 206 PRO   V CA  1 
ATOM   39274 C  C   . PRO   V  8  205 ? -20.021 -156.393 11.560  1.00 118.98 ? 206 PRO   V C   1 
ATOM   39275 O  O   . PRO   V  8  205 ? -18.929 -156.035 11.157  1.00 123.37 ? 206 PRO   V O   1 
ATOM   39276 C  CB  . PRO   V  8  205 ? -21.160 -154.140 11.752  1.00 117.92 ? 206 PRO   V CB  1 
ATOM   39277 C  CG  . PRO   V  8  205 ? -21.049 -153.066 12.814  1.00 117.44 ? 206 PRO   V CG  1 
ATOM   39278 C  CD  . PRO   V  8  205 ? -19.946 -153.536 13.740  1.00 116.76 ? 206 PRO   V CD  1 
ATOM   39279 N  N   . ARG   V  8  206 ? -20.578 -157.572 11.262  1.00 117.97 ? 207 ARG   V N   1 
ATOM   39280 C  CA  . ARG   V  8  206 ? -19.912 -158.615 10.435  1.00 115.26 ? 207 ARG   V CA  1 
ATOM   39281 C  C   . ARG   V  8  206 ? -19.642 -158.046 9.038   1.00 110.55 ? 207 ARG   V C   1 
ATOM   39282 O  O   . ARG   V  8  206 ? -20.599 -157.558 8.405   1.00 105.66 ? 207 ARG   V O   1 
ATOM   39283 C  CB  . ARG   V  8  206 ? -20.757 -159.890 10.352  1.00 117.21 ? 207 ARG   V CB  1 
ATOM   39284 C  CG  . ARG   V  8  206 ? -20.920 -160.620 11.678  1.00 119.48 ? 207 ARG   V CG  1 
ATOM   39285 C  CD  . ARG   V  8  206 ? -21.533 -161.997 11.501  1.00 122.07 ? 207 ARG   V CD  1 
ATOM   39286 N  NE  . ARG   V  8  206 ? -22.009 -162.569 12.755  1.00 124.01 ? 207 ARG   V NE  1 
ATOM   39287 C  CZ  . ARG   V  8  206 ? -22.485 -163.804 12.900  1.00 123.52 ? 207 ARG   V CZ  1 
ATOM   39288 N  NH1 . ARG   V  8  206 ? -22.555 -164.624 11.864  1.00 123.06 ? 207 ARG   V NH1 1 
ATOM   39289 N  NH2 . ARG   V  8  206 ? -22.893 -164.218 14.088  1.00 124.14 ? 207 ARG   V NH2 1 
ATOM   39290 N  N   . GLY   V  8  207 ? -18.384 -158.111 8.592   1.00 108.84 ? 208 GLY   V N   1 
ATOM   39291 C  CA  . GLY   V  8  207 ? -17.910 -157.528 7.323   1.00 110.62 ? 208 GLY   V CA  1 
ATOM   39292 C  C   . GLY   V  8  207 ? -16.987 -156.342 7.543   1.00 110.54 ? 208 GLY   V C   1 
ATOM   39293 O  O   . GLY   V  8  207 ? -16.413 -155.868 6.544   1.00 114.38 ? 208 GLY   V O   1 
ATOM   39294 N  N   . THR   V  8  208 ? -16.838 -155.876 8.792   1.00 112.41 ? 209 THR   V N   1 
ATOM   39295 C  CA  . THR   V  8  208 ? -16.032 -154.677 9.157   1.00 115.52 ? 209 THR   V CA  1 
ATOM   39296 C  C   . THR   V  8  208 ? -14.601 -154.848 8.636   1.00 115.62 ? 209 THR   V C   1 
ATOM   39297 O  O   . THR   V  8  208 ? -14.064 -153.870 8.076   1.00 113.85 ? 209 THR   V O   1 
ATOM   39298 C  CB  . THR   V  8  208 ? -16.052 -154.412 10.670  1.00 119.29 ? 209 THR   V CB  1 
ATOM   39299 O  OG1 . THR   V  8  208 ? -17.410 -154.188 11.049  1.00 119.74 ? 209 THR   V OG1 1 
ATOM   39300 C  CG2 . THR   V  8  208 ? -15.207 -153.225 11.083  1.00 122.11 ? 209 THR   V CG2 1 
ATOM   39301 N  N   . THR   V  8  209 ? -14.016 -156.040 8.809   1.00 115.54 ? 210 THR   V N   1 
ATOM   39302 C  CA  . THR   V  8  209 ? -12.610 -156.347 8.431   1.00 112.69 ? 210 THR   V CA  1 
ATOM   39303 C  C   . THR   V  8  209 ? -12.537 -156.672 6.934   1.00 111.13 ? 210 THR   V C   1 
ATOM   39304 O  O   . THR   V  8  209 ? -13.288 -157.559 6.482   1.00 109.03 ? 210 THR   V O   1 
ATOM   39305 C  CB  . THR   V  8  209 ? -12.020 -157.501 9.253   1.00 111.06 ? 210 THR   V CB  1 
ATOM   39306 O  OG1 . THR   V  8  209 ? -12.275 -157.280 10.641  1.00 111.24 ? 210 THR   V OG1 1 
ATOM   39307 C  CG2 . THR   V  8  209 ? -10.532 -157.655 9.022   1.00 110.65 ? 210 THR   V CG2 1 
ATOM   39308 N  N   . ALA   V  8  210 ? -11.657 -155.975 6.210   1.00 111.13 ? 211 ALA   V N   1 
ATOM   39309 C  CA  . ALA   V  8  210 ? -11.341 -156.207 4.781   1.00 108.62 ? 211 ALA   V CA  1 
ATOM   39310 C  C   . ALA   V  8  210 ? -10.515 -157.490 4.650   1.00 108.44 ? 211 ALA   V C   1 
ATOM   39311 O  O   . ALA   V  8  210 ? -9.523  -157.632 5.394   1.00 106.95 ? 211 ALA   V O   1 
ATOM   39312 C  CB  . ALA   V  8  210 ? -10.605 -155.017 4.216   1.00 108.36 ? 211 ALA   V CB  1 
ATOM   39313 N  N   . VAL   V  8  211 ? -10.917 -158.382 3.737   1.00 107.46 ? 212 VAL   V N   1 
ATOM   39314 C  CA  . VAL   V  8  211 ? -10.314 -159.734 3.528   1.00 108.39 ? 212 VAL   V CA  1 
ATOM   39315 C  C   . VAL   V  8  211 ? -9.810  -159.845 2.084   1.00 107.02 ? 212 VAL   V C   1 
ATOM   39316 O  O   . VAL   V  8  211 ? -10.559 -159.460 1.171   1.00 107.26 ? 212 VAL   V O   1 
ATOM   39317 C  CB  . VAL   V  8  211 ? -11.333 -160.843 3.852   1.00 108.70 ? 212 VAL   V CB  1 
ATOM   39318 C  CG1 . VAL   V  8  211 ? -10.829 -162.217 3.438   1.00 108.43 ? 212 VAL   V CG1 1 
ATOM   39319 C  CG2 . VAL   V  8  211 ? -11.712 -160.837 5.326   1.00 109.33 ? 212 VAL   V CG2 1 
ATOM   39320 N  N   . LEU   V  8  212 ? -8.596  -160.375 1.893   1.00 108.72 ? 213 LEU   V N   1 
ATOM   39321 C  CA  . LEU   V  8  212 ? -7.961  -160.567 0.559   1.00 112.24 ? 213 LEU   V CA  1 
ATOM   39322 C  C   . LEU   V  8  212 ? -8.244  -161.986 0.044   1.00 114.18 ? 213 LEU   V C   1 
ATOM   39323 O  O   . LEU   V  8  212 ? -8.620  -162.109 -1.136  1.00 113.48 ? 213 LEU   V O   1 
ATOM   39324 C  CB  . LEU   V  8  212 ? -6.451  -160.315 0.661   1.00 113.73 ? 213 LEU   V CB  1 
ATOM   39325 C  CG  . LEU   V  8  212 ? -6.021  -158.897 1.042   1.00 115.52 ? 213 LEU   V CG  1 
ATOM   39326 C  CD1 . LEU   V  8  212 ? -4.512  -158.826 1.238   1.00 117.86 ? 213 LEU   V CD1 1 
ATOM   39327 C  CD2 . LEU   V  8  212 ? -6.463  -157.881 -0.002  1.00 116.18 ? 213 LEU   V CD2 1 
ATOM   39328 N  N   . LYS   V  8  213 ? -8.059  -163.011 0.887   1.00 116.22 ? 214 LYS   V N   1 
ATOM   39329 C  CA  . LYS   V  8  213 ? -8.166  -164.449 0.507   1.00 120.51 ? 214 LYS   V CA  1 
ATOM   39330 C  C   . LYS   V  8  213 ? -8.883  -165.262 1.592   1.00 121.93 ? 214 LYS   V C   1 
ATOM   39331 O  O   . LYS   V  8  213 ? -8.806  -164.884 2.777   1.00 123.75 ? 214 LYS   V O   1 
ATOM   39332 C  CB  . LYS   V  8  213 ? -6.781  -165.071 0.312   1.00 121.06 ? 214 LYS   V CB  1 
ATOM   39333 C  CG  . LYS   V  8  213 ? -6.014  -164.611 -0.916  1.00 123.58 ? 214 LYS   V CG  1 
ATOM   39334 C  CD  . LYS   V  8  213 ? -4.625  -165.202 -0.974  1.00 127.14 ? 214 LYS   V CD  1 
ATOM   39335 C  CE  . LYS   V  8  213 ? -3.928  -164.965 -2.296  1.00 130.66 ? 214 LYS   V CE  1 
ATOM   39336 N  NZ  . LYS   V  8  213 ? -2.708  -165.796 -2.421  1.00 132.77 ? 214 LYS   V NZ  1 
ATOM   39337 N  N   . GLU   V  8  214 ? -9.517  -166.363 1.178   1.00 122.97 ? 215 GLU   V N   1 
ATOM   39338 C  CA  . GLU   V  8  214 ? -10.090 -167.424 2.050   1.00 125.37 ? 215 GLU   V CA  1 
ATOM   39339 C  C   . GLU   V  8  214 ? -9.589  -168.786 1.556   1.00 124.60 ? 215 GLU   V C   1 
ATOM   39340 O  O   . GLU   V  8  214 ? -9.321  -168.907 0.345   1.00 125.70 ? 215 GLU   V O   1 
ATOM   39341 C  CB  . GLU   V  8  214 ? -11.618 -167.410 2.002   1.00 128.05 ? 215 GLU   V CB  1 
ATOM   39342 C  CG  . GLU   V  8  214 ? -12.257 -166.319 2.838   1.00 129.61 ? 215 GLU   V CG  1 
ATOM   39343 C  CD  . GLU   V  8  214 ? -13.742 -166.520 3.087   1.00 134.24 ? 215 GLU   V CD  1 
ATOM   39344 O  OE1 . GLU   V  8  214 ? -14.168 -167.686 3.221   1.00 134.79 ? 215 GLU   V OE1 1 
ATOM   39345 O  OE2 . GLU   V  8  214 ? -14.470 -165.509 3.153   1.00 137.66 ? 215 GLU   V OE2 1 
ATOM   39346 N  N   . SER   V  8  215 ? -9.479  -169.770 2.453   1.00 126.18 ? 216 SER   V N   1 
ATOM   39347 C  CA  . SER   V  8  215 ? -9.134  -171.176 2.109   1.00 125.89 ? 216 SER   V CA  1 
ATOM   39348 C  C   . SER   V  8  215 ? -9.431  -172.114 3.284   1.00 128.20 ? 216 SER   V C   1 
ATOM   39349 O  O   . SER   V  8  215 ? -9.306  -171.679 4.447   1.00 130.29 ? 216 SER   V O   1 
ATOM   39350 C  CB  . SER   V  8  215 ? -7.696  -171.292 1.662   1.00 124.78 ? 216 SER   V CB  1 
ATOM   39351 O  OG  . SER   V  8  215 ? -6.824  -170.627 2.563   1.00 121.59 ? 216 SER   V OG  1 
ATOM   39352 N  N   . ILE   V  8  216 ? -9.816  -173.355 2.973   1.00 128.90 ? 217 ILE   V N   1 
ATOM   39353 C  CA  . ILE   V  8  216 ? -10.034 -174.455 3.959   1.00 127.60 ? 217 ILE   V CA  1 
ATOM   39354 C  C   . ILE   V  8  216 ? -8.668  -175.067 4.280   1.00 125.02 ? 217 ILE   V C   1 
ATOM   39355 O  O   . ILE   V  8  216 ? -7.926  -175.379 3.328   1.00 121.73 ? 217 ILE   V O   1 
ATOM   39356 C  CB  . ILE   V  8  216 ? -11.019 -175.510 3.414   1.00 127.57 ? 217 ILE   V CB  1 
ATOM   39357 C  CG1 . ILE   V  8  216 ? -12.370 -174.898 3.028   1.00 127.53 ? 217 ILE   V CG1 1 
ATOM   39358 C  CG2 . ILE   V  8  216 ? -11.181 -176.662 4.398   1.00 127.62 ? 217 ILE   V CG2 1 
ATOM   39359 C  CD1 . ILE   V  8  216 ? -13.173 -174.355 4.193   1.00 125.89 ? 217 ILE   V CD1 1 
ATOM   39360 N  N   . VAL   V  8  217 ? -8.355  -175.226 5.568   1.00 127.00 ? 218 VAL   V N   1 
ATOM   39361 C  CA  . VAL   V  8  217 ? -7.085  -175.841 6.053   1.00 131.42 ? 218 VAL   V CA  1 
ATOM   39362 C  C   . VAL   V  8  217 ? -7.357  -177.325 6.323   1.00 136.51 ? 218 VAL   V C   1 
ATOM   39363 O  O   . VAL   V  8  217 ? -8.356  -177.626 7.007   1.00 142.35 ? 218 VAL   V O   1 
ATOM   39364 C  CB  . VAL   V  8  217 ? -6.540  -175.127 7.306   1.00 129.18 ? 218 VAL   V CB  1 
ATOM   39365 C  CG1 . VAL   V  8  217 ? -5.125  -175.575 7.640   1.00 128.06 ? 218 VAL   V CG1 1 
ATOM   39366 C  CG2 . VAL   V  8  217 ? -6.592  -173.615 7.167   1.00 129.33 ? 218 VAL   V CG2 1 
ATOM   39367 N  N   . ASN   V  8  218 ? -6.505  -178.207 5.790   1.00 143.50 ? 219 ASN   V N   1 
ATOM   39368 C  CA  . ASN   V  8  218 ? -6.608  -179.683 5.945   1.00 146.44 ? 219 ASN   V CA  1 
ATOM   39369 C  C   . ASN   V  8  218 ? -5.826  -180.124 7.191   1.00 144.97 ? 219 ASN   V C   1 
ATOM   39370 O  O   . ASN   V  8  218 ? -4.578  -180.059 7.162   1.00 140.88 ? 219 ASN   V O   1 
ATOM   39371 C  CB  . ASN   V  8  218 ? -6.114  -180.412 4.695   1.00 152.88 ? 219 ASN   V CB  1 
ATOM   39372 C  CG  . ASN   V  8  218 ? -6.419  -181.893 4.734   1.00 156.94 ? 219 ASN   V CG  1 
ATOM   39373 O  OD1 . ASN   V  8  218 ? -7.582  -182.289 4.715   1.00 167.46 ? 219 ASN   V OD1 1 
ATOM   39374 N  ND2 . ASN   V  8  218 ? -5.386  -182.718 4.796   1.00 160.73 ? 219 ASN   V ND2 1 
ATOM   39375 N  N   . ILE   V  8  219 ? -6.538  -180.569 8.233   1.00 144.17 ? 220 ILE   V N   1 
ATOM   39376 C  CA  . ILE   V  8  219 ? -5.952  -181.050 9.522   1.00 145.08 ? 220 ILE   V CA  1 
ATOM   39377 C  C   . ILE   V  8  219 ? -5.910  -182.585 9.536   1.00 146.20 ? 220 ILE   V C   1 
ATOM   39378 O  O   . ILE   V  8  219 ? -5.117  -183.133 10.326  1.00 143.04 ? 220 ILE   V O   1 
ATOM   39379 C  CB  . ILE   V  8  219 ? -6.713  -180.481 10.741  1.00 140.80 ? 220 ILE   V CB  1 
ATOM   39380 C  CG1 . ILE   V  8  219 ? -8.228  -180.693 10.650  1.00 140.25 ? 220 ILE   V CG1 1 
ATOM   39381 C  CG2 . ILE   V  8  219 ? -6.362  -179.015 10.943  1.00 139.05 ? 220 ILE   V CG2 1 
ATOM   39382 C  CD1 . ILE   V  8  219 ? -8.960  -180.512 11.964  1.00 139.08 ? 220 ILE   V CD1 1 
ATOM   39383 N  N   . CYS   V  8  220 ? -6.714  -183.248 8.694   1.00 156.00 ? 221 CYS   V N   1 
ATOM   39384 C  CA  . CYS   V  8  220 ? -6.815  -184.733 8.594   1.00 158.11 ? 221 CYS   V CA  1 
ATOM   39385 C  C   . CYS   V  8  220 ? -5.570  -185.302 7.898   1.00 165.44 ? 221 CYS   V C   1 
ATOM   39386 O  O   . CYS   V  8  220 ? -4.716  -184.502 7.462   1.00 170.70 ? 221 CYS   V O   1 
ATOM   39387 C  CB  . CYS   V  8  220 ? -8.071  -185.151 7.836   1.00 161.35 ? 221 CYS   V CB  1 
ATOM   39388 S  SG  . CYS   V  8  220 ? -9.610  -184.659 8.657   1.00 163.47 ? 221 CYS   V SG  1 
ATOM   39389 N  N   . ASP   V  8  221 ? -5.479  -186.635 7.808   1.00 164.19 ? 222 ASP   V N   1 
ATOM   39390 C  CA  . ASP   V  8  221 ? -4.373  -187.376 7.141   1.00 160.79 ? 222 ASP   V CA  1 
ATOM   39391 C  C   . ASP   V  8  221 ? -4.723  -187.583 5.662   1.00 161.75 ? 222 ASP   V C   1 
ATOM   39392 O  O   . ASP   V  8  221 ? -5.068  -188.683 5.226   1.00 148.26 ? 222 ASP   V O   1 
ATOM   39393 C  CB  . ASP   V  8  221 ? -4.105  -188.711 7.840   1.00 162.87 ? 222 ASP   V CB  1 
ATOM   39394 C  CG  . ASP   V  8  221 ? -3.511  -188.554 9.227   1.00 160.61 ? 222 ASP   V CG  1 
ATOM   39395 O  OD1 . ASP   V  8  221 ? -2.517  -187.813 9.355   1.00 161.17 ? 222 ASP   V OD1 1 
ATOM   39396 O  OD2 . ASP   V  8  221 ? -4.049  -189.168 10.169  1.00 164.66 ? 222 ASP   V OD2 1 
ATOM   39397 N  N   . SER   W  9  2   ? 20.560  -154.796 18.618  1.00 138.61 ? 1   SER   W N   1 
ATOM   39398 C  CA  . SER   W  9  2   ? 21.042  -156.177 18.950  1.00 135.59 ? 1   SER   W CA  1 
ATOM   39399 C  C   . SER   W  9  2   ? 20.274  -156.751 20.150  1.00 130.27 ? 1   SER   W C   1 
ATOM   39400 O  O   . SER   W  9  2   ? 20.927  -157.283 21.074  1.00 129.93 ? 1   SER   W O   1 
ATOM   39401 C  CB  . SER   W  9  2   ? 22.534  -156.185 19.190  1.00 137.76 ? 1   SER   W CB  1 
ATOM   39402 O  OG  . SER   W  9  2   ? 23.243  -155.991 17.976  1.00 139.80 ? 1   SER   W OG  1 
ATOM   39403 N  N   . ASP   W  9  3   ? 18.939  -156.645 20.134  1.00 124.83 ? 2   ASP   W N   1 
ATOM   39404 C  CA  . ASP   W  9  3   ? 18.017  -157.372 21.049  1.00 118.24 ? 2   ASP   W CA  1 
ATOM   39405 C  C   . ASP   W  9  3   ? 17.346  -158.485 20.251  1.00 114.14 ? 2   ASP   W C   1 
ATOM   39406 O  O   . ASP   W  9  3   ? 16.484  -158.212 19.418  1.00 114.01 ? 2   ASP   W O   1 
ATOM   39407 C  CB  . ASP   W  9  3   ? 16.957  -156.457 21.666  1.00 117.46 ? 2   ASP   W CB  1 
ATOM   39408 C  CG  . ASP   W  9  3   ? 15.916  -157.221 22.469  1.00 116.80 ? 2   ASP   W CG  1 
ATOM   39409 O  OD1 . ASP   W  9  3   ? 16.313  -158.135 23.218  1.00 116.76 ? 2   ASP   W OD1 1 
ATOM   39410 O  OD2 . ASP   W  9  3   ? 14.715  -156.913 22.321  1.00 117.73 ? 2   ASP   W OD2 1 
ATOM   39411 N  N   . PRO   W  9  4   ? 17.690  -159.770 20.496  1.00 108.12 ? 3   PRO   W N   1 
ATOM   39412 C  CA  . PRO   W  9  4   ? 17.313  -160.851 19.585  1.00 106.27 ? 3   PRO   W CA  1 
ATOM   39413 C  C   . PRO   W  9  4   ? 15.805  -160.908 19.294  1.00 103.47 ? 3   PRO   W C   1 
ATOM   39414 O  O   . PRO   W  9  4   ? 15.447  -161.250 18.183  1.00 102.11 ? 3   PRO   W O   1 
ATOM   39415 C  CB  . PRO   W  9  4   ? 17.767  -162.129 20.307  1.00 103.98 ? 3   PRO   W CB  1 
ATOM   39416 C  CG  . PRO   W  9  4   ? 18.819  -161.663 21.290  1.00 107.60 ? 3   PRO   W CG  1 
ATOM   39417 C  CD  . PRO   W  9  4   ? 18.411  -160.259 21.680  1.00 109.60 ? 3   PRO   W CD  1 
ATOM   39418 N  N   . SER   W  9  5   ? 14.967  -160.548 20.272  1.00 103.09 ? 4   SER   W N   1 
ATOM   39419 C  CA  . SER   W  9  5   ? 13.486  -160.665 20.198  1.00 104.19 ? 4   SER   W CA  1 
ATOM   39420 C  C   . SER   W  9  5   ? 12.866  -159.530 19.367  1.00 107.32 ? 4   SER   W C   1 
ATOM   39421 O  O   . SER   W  9  5   ? 11.639  -159.598 19.134  1.00 107.43 ? 4   SER   W O   1 
ATOM   39422 C  CB  . SER   W  9  5   ? 12.886  -160.722 21.579  1.00 104.32 ? 4   SER   W CB  1 
ATOM   39423 O  OG  . SER   W  9  5   ? 13.255  -159.580 22.337  1.00 107.11 ? 4   SER   W OG  1 
ATOM   39424 N  N   . SER   W  9  6   ? 13.656  -158.540 18.922  1.00 105.92 ? 5   SER   W N   1 
ATOM   39425 C  CA  . SER   W  9  6   ? 13.164  -157.362 18.156  1.00 105.09 ? 5   SER   W CA  1 
ATOM   39426 C  C   . SER   W  9  6   ? 14.093  -157.013 16.983  1.00 103.02 ? 5   SER   W C   1 
ATOM   39427 O  O   . SER   W  9  6   ? 14.190  -155.814 16.656  1.00 104.21 ? 5   SER   W O   1 
ATOM   39428 C  CB  . SER   W  9  6   ? 12.972  -156.178 19.073  1.00 107.20 ? 5   SER   W CB  1 
ATOM   39429 O  OG  . SER   W  9  6   ? 14.208  -155.754 19.627  1.00 112.52 ? 5   SER   W OG  1 
ATOM   39430 N  N   . ILE   W  9  7   ? 14.733  -158.005 16.355  1.00 97.40  ? 6   ILE   W N   1 
ATOM   39431 C  CA  . ILE   W  9  7   ? 15.525  -157.816 15.100  1.00 100.49 ? 6   ILE   W CA  1 
ATOM   39432 C  C   . ILE   W  9  7   ? 14.585  -157.983 13.897  1.00 100.63 ? 6   ILE   W C   1 
ATOM   39433 O  O   . ILE   W  9  7   ? 14.641  -157.133 12.985  1.00 101.27 ? 6   ILE   W O   1 
ATOM   39434 C  CB  . ILE   W  9  7   ? 16.734  -158.775 15.035  1.00 101.31 ? 6   ILE   W CB  1 
ATOM   39435 C  CG1 . ILE   W  9  7   ? 17.730  -158.499 16.164  1.00 104.17 ? 6   ILE   W CG1 1 
ATOM   39436 C  CG2 . ILE   W  9  7   ? 17.413  -158.706 13.672  1.00 103.88 ? 6   ILE   W CG2 1 
ATOM   39437 C  CD1 . ILE   W  9  7   ? 18.831  -159.530 16.295  1.00 106.53 ? 6   ILE   W CD1 1 
ATOM   39438 N  N   . ASN   W  9  8   ? 13.752  -159.030 13.901  1.00 98.64  ? 7   ASN   W N   1 
ATOM   39439 C  CA  . ASN   W  9  8   ? 12.898  -159.432 12.749  1.00 96.36  ? 7   ASN   W CA  1 
ATOM   39440 C  C   . ASN   W  9  8   ? 11.477  -158.881 12.896  1.00 95.86  ? 7   ASN   W C   1 
ATOM   39441 O  O   . ASN   W  9  8   ? 10.833  -158.650 11.853  1.00 94.72  ? 7   ASN   W O   1 
ATOM   39442 C  CB  . ASN   W  9  8   ? 12.832  -160.950 12.590  1.00 95.71  ? 7   ASN   W CB  1 
ATOM   39443 C  CG  . ASN   W  9  8   ? 14.198  -161.595 12.511  1.00 95.70  ? 7   ASN   W CG  1 
ATOM   39444 O  OD1 . ASN   W  9  8   ? 14.476  -162.546 13.237  1.00 95.30  ? 7   ASN   W OD1 1 
ATOM   39445 N  ND2 . ASN   W  9  8   ? 15.059  -161.086 11.643  1.00 95.73  ? 7   ASN   W ND2 1 
ATOM   39446 N  N   . GLY   W  9  9   ? 10.995  -158.716 14.131  1.00 94.42  ? 8   GLY   W N   1 
ATOM   39447 C  CA  . GLY   W  9  9   ? 9.644   -158.200 14.419  1.00 92.97  ? 8   GLY   W CA  1 
ATOM   39448 C  C   . GLY   W  9  9   ? 8.585   -159.246 14.129  1.00 90.09  ? 8   GLY   W C   1 
ATOM   39449 O  O   . GLY   W  9  9   ? 8.955   -160.335 13.661  1.00 92.28  ? 8   GLY   W O   1 
ATOM   39450 N  N   . GLY   W  9  10  ? 7.315   -158.921 14.383  1.00 89.41  ? 9   GLY   W N   1 
ATOM   39451 C  CA  . GLY   W  9  10  ? 6.173   -159.823 14.144  1.00 88.77  ? 9   GLY   W CA  1 
ATOM   39452 C  C   . GLY   W  9  10  ? 5.325   -160.011 15.385  1.00 88.30  ? 9   GLY   W C   1 
ATOM   39453 O  O   . GLY   W  9  10  ? 5.862   -159.829 16.496  1.00 87.65  ? 9   GLY   W O   1 
ATOM   39454 N  N   . ILE   W  9  11  ? 4.054   -160.388 15.202  1.00 88.43  ? 10  ILE   W N   1 
ATOM   39455 C  CA  . ILE   W  9  11  ? 3.074   -160.619 16.306  1.00 88.63  ? 10  ILE   W CA  1 
ATOM   39456 C  C   . ILE   W  9  11  ? 2.211   -161.851 16.015  1.00 88.79  ? 10  ILE   W C   1 
ATOM   39457 O  O   . ILE   W  9  11  ? 2.051   -162.227 14.833  1.00 85.93  ? 10  ILE   W O   1 
ATOM   39458 C  CB  . ILE   W  9  11  ? 2.188   -159.384 16.551  1.00 88.57  ? 10  ILE   W CB  1 
ATOM   39459 C  CG1 . ILE   W  9  11  ? 1.684   -158.767 15.245  1.00 91.15  ? 10  ILE   W CG1 1 
ATOM   39460 C  CG2 . ILE   W  9  11  ? 2.918   -158.370 17.410  1.00 88.66  ? 10  ILE   W CG2 1 
ATOM   39461 C  CD1 . ILE   W  9  11  ? 0.543   -157.796 15.436  1.00 93.84  ? 10  ILE   W CD1 1 
ATOM   39462 N  N   . VAL   W  9  12  ? 1.672   -162.427 17.091  1.00 89.12  ? 11  VAL   W N   1 
ATOM   39463 C  CA  . VAL   W  9  12  ? 0.681   -163.540 17.097  1.00 90.81  ? 11  VAL   W CA  1 
ATOM   39464 C  C   . VAL   W  9  12  ? -0.330  -163.242 18.208  1.00 91.75  ? 11  VAL   W C   1 
ATOM   39465 O  O   . VAL   W  9  12  ? 0.088   -162.717 19.259  1.00 90.69  ? 11  VAL   W O   1 
ATOM   39466 C  CB  . VAL   W  9  12  ? 1.368   -164.904 17.310  1.00 91.11  ? 11  VAL   W CB  1 
ATOM   39467 C  CG1 . VAL   W  9  12  ? 0.368   -166.012 17.609  1.00 90.80  ? 11  VAL   W CG1 1 
ATOM   39468 C  CG2 . VAL   W  9  12  ? 2.243   -165.283 16.125  1.00 91.07  ? 11  VAL   W CG2 1 
ATOM   39469 N  N   . VAL   W  9  13  ? -1.605  -163.562 17.978  1.00 93.10  ? 12  VAL   W N   1 
ATOM   39470 C  CA  . VAL   W  9  13  ? -2.690  -163.454 18.996  1.00 92.99  ? 12  VAL   W CA  1 
ATOM   39471 C  C   . VAL   W  9  13  ? -3.633  -164.650 18.822  1.00 94.42  ? 12  VAL   W C   1 
ATOM   39472 O  O   . VAL   W  9  13  ? -3.888  -165.040 17.668  1.00 98.02  ? 12  VAL   W O   1 
ATOM   39473 C  CB  . VAL   W  9  13  ? -3.432  -162.106 18.893  1.00 93.75  ? 12  VAL   W CB  1 
ATOM   39474 C  CG1 . VAL   W  9  13  ? -4.098  -161.912 17.539  1.00 95.08  ? 12  VAL   W CG1 1 
ATOM   39475 C  CG2 . VAL   W  9  13  ? -4.442  -161.929 20.016  1.00 94.41  ? 12  VAL   W CG2 1 
ATOM   39476 N  N   . ALA   W  9  14  ? -4.110  -165.214 19.934  1.00 93.64  ? 13  ALA   W N   1 
ATOM   39477 C  CA  . ALA   W  9  14  ? -5.091  -166.321 19.972  1.00 94.56  ? 13  ALA   W CA  1 
ATOM   39478 C  C   . ALA   W  9  14  ? -6.276  -165.915 20.850  1.00 95.31  ? 13  ALA   W C   1 
ATOM   39479 O  O   . ALA   W  9  14  ? -6.044  -165.248 21.874  1.00 94.98  ? 13  ALA   W O   1 
ATOM   39480 C  CB  . ALA   W  9  14  ? -4.431  -167.574 20.485  1.00 94.45  ? 13  ALA   W CB  1 
ATOM   39481 N  N   . MET   W  9  15  ? -7.491  -166.301 20.453  1.00 96.57  ? 14  MET   W N   1 
ATOM   39482 C  CA  . MET   W  9  15  ? -8.745  -166.025 21.202  1.00 101.96 ? 14  MET   W CA  1 
ATOM   39483 C  C   . MET   W  9  15  ? -9.625  -167.277 21.202  1.00 102.56 ? 14  MET   W C   1 
ATOM   39484 O  O   . MET   W  9  15  ? -9.550  -168.060 20.233  1.00 102.58 ? 14  MET   W O   1 
ATOM   39485 C  CB  . MET   W  9  15  ? -9.530  -164.869 20.575  1.00 106.35 ? 14  MET   W CB  1 
ATOM   39486 C  CG  . MET   W  9  15  ? -9.119  -163.497 21.074  1.00 109.68 ? 14  MET   W CG  1 
ATOM   39487 S  SD  . MET   W  9  15  ? -10.078 -162.185 20.274  1.00 114.02 ? 14  MET   W SD  1 
ATOM   39488 C  CE  . MET   W  9  15  ? -9.405  -160.732 21.072  1.00 114.28 ? 14  MET   W CE  1 
ATOM   39489 N  N   . THR   W  9  16  ? -10.432 -167.438 22.253  1.00 104.77 ? 15  THR   W N   1 
ATOM   39490 C  CA  . THR   W  9  16  ? -11.456 -168.503 22.393  1.00 106.20 ? 15  THR   W CA  1 
ATOM   39491 C  C   . THR   W  9  16  ? -12.840 -167.903 22.133  1.00 109.76 ? 15  THR   W C   1 
ATOM   39492 O  O   . THR   W  9  16  ? -13.087 -166.768 22.584  1.00 108.16 ? 15  THR   W O   1 
ATOM   39493 C  CB  . THR   W  9  16  ? -11.393 -169.153 23.780  1.00 106.25 ? 15  THR   W CB  1 
ATOM   39494 O  OG1 . THR   W  9  16  ? -11.752 -168.163 24.743  1.00 109.43 ? 15  THR   W OG1 1 
ATOM   39495 C  CG2 . THR   W  9  16  ? -10.028 -169.717 24.106  1.00 104.86 ? 15  THR   W CG2 1 
ATOM   39496 N  N   . GLY   W  9  17  ? -13.696 -168.644 21.427  1.00 112.54 ? 16  GLY   W N   1 
ATOM   39497 C  CA  . GLY   W  9  17  ? -15.123 -168.325 21.234  1.00 118.06 ? 16  GLY   W CA  1 
ATOM   39498 C  C   . GLY   W  9  17  ? -16.000 -169.474 21.697  1.00 122.03 ? 16  GLY   W C   1 
ATOM   39499 O  O   . GLY   W  9  17  ? -15.496 -170.335 22.449  1.00 122.81 ? 16  GLY   W O   1 
ATOM   39500 N  N   . LYS   W  9  18  ? -17.263 -169.493 21.264  1.00 124.68 ? 17  LYS   W N   1 
ATOM   39501 C  CA  . LYS   W  9  18  ? -18.238 -170.562 21.603  1.00 125.36 ? 17  LYS   W CA  1 
ATOM   39502 C  C   . LYS   W  9  18  ? -17.962 -171.777 20.711  1.00 125.00 ? 17  LYS   W C   1 
ATOM   39503 O  O   . LYS   W  9  18  ? -18.288 -171.710 19.509  1.00 124.30 ? 17  LYS   W O   1 
ATOM   39504 C  CB  . LYS   W  9  18  ? -19.675 -170.054 21.446  1.00 130.17 ? 17  LYS   W CB  1 
ATOM   39505 C  CG  . LYS   W  9  18  ? -20.743 -171.059 21.856  1.00 133.78 ? 17  LYS   W CG  1 
ATOM   39506 C  CD  . LYS   W  9  18  ? -22.003 -170.430 22.412  1.00 137.68 ? 17  LYS   W CD  1 
ATOM   39507 C  CE  . LYS   W  9  18  ? -22.868 -171.419 23.165  1.00 140.87 ? 17  LYS   W CE  1 
ATOM   39508 N  NZ  . LYS   W  9  18  ? -22.284 -171.769 24.482  1.00 141.78 ? 17  LYS   W NZ  1 
ATOM   39509 N  N   . ASP   W  9  19  ? -17.368 -172.830 21.286  1.00 122.92 ? 18  ASP   W N   1 
ATOM   39510 C  CA  . ASP   W  9  19  ? -17.035 -174.112 20.605  1.00 122.90 ? 18  ASP   W CA  1 
ATOM   39511 C  C   . ASP   W  9  19  ? -16.090 -173.846 19.423  1.00 116.21 ? 18  ASP   W C   1 
ATOM   39512 O  O   . ASP   W  9  19  ? -16.214 -174.545 18.399  1.00 116.70 ? 18  ASP   W O   1 
ATOM   39513 C  CB  . ASP   W  9  19  ? -18.302 -174.841 20.139  1.00 126.35 ? 18  ASP   W CB  1 
ATOM   39514 C  CG  . ASP   W  9  19  ? -19.248 -175.244 21.259  1.00 127.74 ? 18  ASP   W CG  1 
ATOM   39515 O  OD1 . ASP   W  9  19  ? -18.756 -175.711 22.305  1.00 130.07 ? 18  ASP   W OD1 1 
ATOM   39516 O  OD2 . ASP   W  9  19  ? -20.474 -175.096 21.071  1.00 126.10 ? 18  ASP   W OD2 1 
ATOM   39517 N  N   . CYS   W  9  20  ? -15.175 -172.883 19.555  1.00 113.62 ? 19  CYS   W N   1 
ATOM   39518 C  CA  . CYS   W  9  20  ? -14.219 -172.491 18.483  1.00 114.50 ? 19  CYS   W CA  1 
ATOM   39519 C  C   . CYS   W  9  20  ? -13.022 -171.745 19.083  1.00 111.63 ? 19  CYS   W C   1 
ATOM   39520 O  O   . CYS   W  9  20  ? -13.159 -171.215 20.203  1.00 116.06 ? 19  CYS   W O   1 
ATOM   39521 C  CB  . CYS   W  9  20  ? -14.907 -171.628 17.429  1.00 116.16 ? 19  CYS   W CB  1 
ATOM   39522 S  SG  . CYS   W  9  20  ? -15.416 -169.996 18.032  1.00 118.95 ? 19  CYS   W SG  1 
ATOM   39523 N  N   . VAL   W  9  21  ? -11.897 -171.720 18.361  1.00 108.04 ? 20  VAL   W N   1 
ATOM   39524 C  CA  . VAL   W  9  21  ? -10.692 -170.895 18.685  1.00 107.14 ? 20  VAL   W CA  1 
ATOM   39525 C  C   . VAL   W  9  21  ? -10.208 -170.203 17.412  1.00 107.22 ? 20  VAL   W C   1 
ATOM   39526 O  O   . VAL   W  9  21  ? -10.384 -170.775 16.320  1.00 112.81 ? 20  VAL   W O   1 
ATOM   39527 C  CB  . VAL   W  9  21  ? -9.546  -171.712 19.309  1.00 106.84 ? 20  VAL   W CB  1 
ATOM   39528 C  CG1 . VAL   W  9  21  ? -9.727  -171.876 20.804  1.00 108.22 ? 20  VAL   W CG1 1 
ATOM   39529 C  CG2 . VAL   W  9  21  ? -9.360  -173.059 18.632  1.00 109.64 ? 20  VAL   W CG2 1 
ATOM   39530 N  N   . ALA   W  9  22  ? -9.606  -169.024 17.576  1.00 104.87 ? 21  ALA   W N   1 
ATOM   39531 C  CA  . ALA   W  9  22  ? -8.974  -168.227 16.503  1.00 101.16 ? 21  ALA   W CA  1 
ATOM   39532 C  C   . ALA   W  9  22  ? -7.519  -167.946 16.886  1.00 97.28  ? 21  ALA   W C   1 
ATOM   39533 O  O   . ALA   W  9  22  ? -7.274  -167.606 18.061  1.00 94.54  ? 21  ALA   W O   1 
ATOM   39534 C  CB  . ALA   W  9  22  ? -9.747  -166.950 16.286  1.00 101.72 ? 21  ALA   W CB  1 
ATOM   39535 N  N   . ILE   W  9  23  ? -6.596  -168.111 15.936  1.00 94.50  ? 22  ILE   W N   1 
ATOM   39536 C  CA  . ILE   W  9  23  ? -5.171  -167.687 16.068  1.00 92.13  ? 22  ILE   W CA  1 
ATOM   39537 C  C   . ILE   W  9  23  ? -4.794  -166.908 14.805  1.00 92.14  ? 22  ILE   W C   1 
ATOM   39538 O  O   . ILE   W  9  23  ? -5.093  -167.393 13.700  1.00 90.33  ? 22  ILE   W O   1 
ATOM   39539 C  CB  . ILE   W  9  23  ? -4.235  -168.884 16.338  1.00 92.49  ? 22  ILE   W CB  1 
ATOM   39540 C  CG1 . ILE   W  9  23  ? -2.807  -168.418 16.637  1.00 94.23  ? 22  ILE   W CG1 1 
ATOM   39541 C  CG2 . ILE   W  9  23  ? -4.271  -169.896 15.202  1.00 92.75  ? 22  ILE   W CG2 1 
ATOM   39542 C  CD1 . ILE   W  9  23  ? -1.956  -169.450 17.346  1.00 94.64  ? 22  ILE   W CD1 1 
ATOM   39543 N  N   . ALA   W  9  24  ? -4.200  -165.726 14.981  1.00 91.28  ? 23  ALA   W N   1 
ATOM   39544 C  CA  . ALA   W  9  24  ? -3.848  -164.774 13.903  1.00 91.59  ? 23  ALA   W CA  1 
ATOM   39545 C  C   . ALA   W  9  24  ? -2.388  -164.339 14.056  1.00 90.58  ? 23  ALA   W C   1 
ATOM   39546 O  O   . ALA   W  9  24  ? -1.876  -164.367 15.192  1.00 93.05  ? 23  ALA   W O   1 
ATOM   39547 C  CB  . ALA   W  9  24  ? -4.777  -163.588 13.952  1.00 91.69  ? 23  ALA   W CB  1 
ATOM   39548 N  N   . CYS   W  9  25  ? -1.750  -163.954 12.951  1.00 89.22  ? 24  CYS   W N   1 
ATOM   39549 C  CA  . CYS   W  9  25  ? -0.348  -163.458 12.917  1.00 91.86  ? 24  CYS   W CA  1 
ATOM   39550 C  C   . CYS   W  9  25  ? -0.170  -162.484 11.750  1.00 90.87  ? 24  CYS   W C   1 
ATOM   39551 O  O   . CYS   W  9  25  ? -0.955  -162.563 10.788  1.00 92.20  ? 24  CYS   W O   1 
ATOM   39552 C  CB  . CYS   W  9  25  ? 0.644   -164.608 12.785  1.00 92.61  ? 24  CYS   W CB  1 
ATOM   39553 S  SG  . CYS   W  9  25  ? 0.759   -165.286 11.108  1.00 96.96  ? 24  CYS   W SG  1 
ATOM   39554 N  N   . ASP   W  9  26  ? 0.825   -161.601 11.851  1.00 92.61  ? 25  ASP   W N   1 
ATOM   39555 C  CA  . ASP   W  9  26  ? 1.264   -160.702 10.751  1.00 92.63  ? 25  ASP   W CA  1 
ATOM   39556 C  C   . ASP   W  9  26  ? 2.164   -161.512 9.809   1.00 92.34  ? 25  ASP   W C   1 
ATOM   39557 O  O   . ASP   W  9  26  ? 2.405   -162.702 10.104  1.00 89.01  ? 25  ASP   W O   1 
ATOM   39558 C  CB  . ASP   W  9  26  ? 1.960   -159.456 11.303  1.00 92.85  ? 25  ASP   W CB  1 
ATOM   39559 C  CG  . ASP   W  9  26  ? 3.369   -159.716 11.806  1.00 93.67  ? 25  ASP   W CG  1 
ATOM   39560 O  OD1 . ASP   W  9  26  ? 3.586   -160.780 12.420  1.00 95.01  ? 25  ASP   W OD1 1 
ATOM   39561 O  OD2 . ASP   W  9  26  ? 4.238   -158.857 11.574  1.00 94.95  ? 25  ASP   W OD2 1 
ATOM   39562 N  N   . LEU   W  9  27  ? 2.644   -160.892 8.728   1.00 93.13  ? 26  LEU   W N   1 
ATOM   39563 C  CA  . LEU   W  9  27  ? 3.460   -161.567 7.681   1.00 94.87  ? 26  LEU   W CA  1 
ATOM   39564 C  C   . LEU   W  9  27  ? 4.858   -160.942 7.575   1.00 93.17  ? 26  LEU   W C   1 
ATOM   39565 O  O   . LEU   W  9  27  ? 5.658   -161.449 6.764   1.00 93.74  ? 26  LEU   W O   1 
ATOM   39566 C  CB  . LEU   W  9  27  ? 2.727   -161.469 6.338   1.00 98.32  ? 26  LEU   W CB  1 
ATOM   39567 C  CG  . LEU   W  9  27  ? 1.435   -162.274 6.210   1.00 97.00  ? 26  LEU   W CG  1 
ATOM   39568 C  CD1 . LEU   W  9  27  ? 0.864   -162.130 4.811   1.00 99.31  ? 26  LEU   W CD1 1 
ATOM   39569 C  CD2 . LEU   W  9  27  ? 1.661   -163.741 6.532   1.00 95.26  ? 26  LEU   W CD2 1 
ATOM   39570 N  N   . ARG   W  9  28  ? 5.157   -159.890 8.341   1.00 92.75  ? 27  ARG   W N   1 
ATOM   39571 C  CA  . ARG   W  9  28  ? 6.437   -159.147 8.192   1.00 94.88  ? 27  ARG   W CA  1 
ATOM   39572 C  C   . ARG   W  9  28  ? 7.591   -160.030 8.672   1.00 93.44  ? 27  ARG   W C   1 
ATOM   39573 O  O   . ARG   W  9  28  ? 7.427   -160.721 9.695   1.00 93.50  ? 27  ARG   W O   1 
ATOM   39574 C  CB  . ARG   W  9  28  ? 6.439   -157.821 8.959   1.00 96.95  ? 27  ARG   W CB  1 
ATOM   39575 C  CG  . ARG   W  9  28  ? 7.623   -156.928 8.610   1.00 101.05 ? 27  ARG   W CG  1 
ATOM   39576 C  CD  . ARG   W  9  28  ? 7.525   -155.528 9.186   1.00 104.92 ? 27  ARG   W CD  1 
ATOM   39577 N  NE  . ARG   W  9  28  ? 8.722   -154.734 8.926   1.00 107.04 ? 27  ARG   W NE  1 
ATOM   39578 C  CZ  . ARG   W  9  28  ? 9.859   -154.791 9.621   1.00 104.73 ? 27  ARG   W CZ  1 
ATOM   39579 N  NH1 . ARG   W  9  28  ? 9.990   -155.617 10.647  1.00 101.62 ? 27  ARG   W NH1 1 
ATOM   39580 N  NH2 . ARG   W  9  28  ? 10.872  -154.012 9.283   1.00 110.83 ? 27  ARG   W NH2 1 
ATOM   39581 N  N   . LEU   W  9  29  ? 8.689   -160.029 7.915   1.00 92.29  ? 28  LEU   W N   1 
ATOM   39582 C  CA  . LEU   W  9  29  ? 10.053  -160.352 8.407   1.00 93.39  ? 28  LEU   W CA  1 
ATOM   39583 C  C   . LEU   W  9  29  ? 10.989  -159.246 7.921   1.00 91.46  ? 28  LEU   W C   1 
ATOM   39584 O  O   . LEU   W  9  29  ? 11.065  -159.032 6.691   1.00 86.65  ? 28  LEU   W O   1 
ATOM   39585 C  CB  . LEU   W  9  29  ? 10.503  -161.724 7.897   1.00 94.80  ? 28  LEU   W CB  1 
ATOM   39586 C  CG  . LEU   W  9  29  ? 11.891  -162.169 8.362   1.00 96.60  ? 28  LEU   W CG  1 
ATOM   39587 C  CD1 . LEU   W  9  29  ? 11.919  -163.662 8.644   1.00 96.85  ? 28  LEU   W CD1 1 
ATOM   39588 C  CD2 . LEU   W  9  29  ? 12.964  -161.806 7.343   1.00 97.97  ? 28  LEU   W CD2 1 
ATOM   39589 N  N   . GLY   W  9  30  ? 11.652  -158.565 8.857   1.00 91.25  ? 29  GLY   W N   1 
ATOM   39590 C  CA  . GLY   W  9  30  ? 12.590  -157.467 8.565   1.00 92.34  ? 29  GLY   W CA  1 
ATOM   39591 C  C   . GLY   W  9  30  ? 13.962  -157.737 9.146   1.00 92.13  ? 29  GLY   W C   1 
ATOM   39592 O  O   . GLY   W  9  30  ? 14.140  -158.779 9.798   1.00 89.33  ? 29  GLY   W O   1 
ATOM   39593 N  N   . SER   W  9  31  ? 14.905  -156.837 8.872   1.00 94.04  ? 30  SER   W N   1 
ATOM   39594 C  CA  . SER   W  9  31  ? 16.207  -156.714 9.569   1.00 95.37  ? 30  SER   W CA  1 
ATOM   39595 C  C   . SER   W  9  31  ? 16.296  -155.294 10.141  1.00 96.50  ? 30  SER   W C   1 
ATOM   39596 O  O   . SER   W  9  31  ? 16.680  -154.367 9.395   1.00 95.04  ? 30  SER   W O   1 
ATOM   39597 C  CB  . SER   W  9  31  ? 17.347  -157.050 8.648   1.00 97.87  ? 30  SER   W CB  1 
ATOM   39598 O  OG  . SER   W  9  31  ? 18.552  -157.203 9.380   1.00 99.23  ? 30  SER   W OG  1 
ATOM   39599 N  N   . GLN   W  9  32  ? 15.905  -155.141 11.412  1.00 100.74 ? 31  GLN   W N   1 
ATOM   39600 C  CA  . GLN   W  9  32  ? 15.676  -153.838 12.091  1.00 100.92 ? 31  GLN   W CA  1 
ATOM   39601 C  C   . GLN   W  9  32  ? 14.749  -152.999 11.198  1.00 96.89  ? 31  GLN   W C   1 
ATOM   39602 O  O   . GLN   W  9  32  ? 13.576  -153.401 11.053  1.00 89.45  ? 31  GLN   W O   1 
ATOM   39603 C  CB  . GLN   W  9  32  ? 17.019  -153.199 12.453  1.00 105.45 ? 31  GLN   W CB  1 
ATOM   39604 C  CG  . GLN   W  9  32  ? 17.651  -153.822 13.692  1.00 109.09 ? 31  GLN   W CG  1 
ATOM   39605 C  CD  . GLN   W  9  32  ? 19.076  -153.383 13.925  1.00 115.93 ? 31  GLN   W CD  1 
ATOM   39606 O  OE1 . GLN   W  9  32  ? 19.406  -152.822 14.967  1.00 123.96 ? 31  GLN   W OE1 1 
ATOM   39607 N  NE2 . GLN   W  9  32  ? 19.942  -153.641 12.957  1.00 121.41 ? 31  GLN   W NE2 1 
ATOM   39608 N  N   . SER   W  9  33  ? 15.250  -151.918 10.588  1.00 99.62  ? 32  SER   W N   1 
ATOM   39609 C  CA  . SER   W  9  33  ? 14.434  -150.915 9.848   1.00 99.84  ? 32  SER   W CA  1 
ATOM   39610 C  C   . SER   W  9  33  ? 13.975  -151.491 8.500   1.00 99.86  ? 32  SER   W C   1 
ATOM   39611 O  O   . SER   W  9  33  ? 12.820  -151.222 8.107   1.00 99.10  ? 32  SER   W O   1 
ATOM   39612 C  CB  . SER   W  9  33  ? 15.183  -149.612 9.673   1.00 103.00 ? 32  SER   W CB  1 
ATOM   39613 O  OG  . SER   W  9  33  ? 16.167  -149.715 8.654   1.00 102.67 ? 32  SER   W OG  1 
ATOM   39614 N  N   . LEU   W  9  34  ? 14.846  -152.259 7.834   1.00 97.23  ? 33  LEU   W N   1 
ATOM   39615 C  CA  . LEU   W  9  34  ? 14.622  -152.833 6.477   1.00 95.78  ? 33  LEU   W CA  1 
ATOM   39616 C  C   . LEU   W  9  34  ? 13.584  -153.956 6.554   1.00 95.61  ? 33  LEU   W C   1 
ATOM   39617 O  O   . LEU   W  9  34  ? 13.853  -154.951 7.247   1.00 95.23  ? 33  LEU   W O   1 
ATOM   39618 C  CB  . LEU   W  9  34  ? 15.952  -153.367 5.929   1.00 94.20  ? 33  LEU   W CB  1 
ATOM   39619 C  CG  . LEU   W  9  34  ? 15.876  -154.176 4.633   1.00 92.72  ? 33  LEU   W CG  1 
ATOM   39620 C  CD1 . LEU   W  9  34  ? 15.418  -153.309 3.473   1.00 94.03  ? 33  LEU   W CD1 1 
ATOM   39621 C  CD2 . LEU   W  9  34  ? 17.220  -154.811 4.315   1.00 92.35  ? 33  LEU   W CD2 1 
ATOM   39622 N  N   . GLY   W  9  35  ? 12.451  -153.802 5.863   1.00 96.61  ? 34  GLY   W N   1 
ATOM   39623 C  CA  . GLY   W  9  35  ? 11.527  -154.912 5.560   1.00 96.74  ? 34  GLY   W CA  1 
ATOM   39624 C  C   . GLY   W  9  35  ? 12.124  -155.821 4.494   1.00 97.88  ? 34  GLY   W C   1 
ATOM   39625 O  O   . GLY   W  9  35  ? 12.641  -155.279 3.496   1.00 100.25 ? 34  GLY   W O   1 
ATOM   39626 N  N   . VAL   W  9  36  ? 12.086  -157.145 4.690   1.00 96.29  ? 35  VAL   W N   1 
ATOM   39627 C  CA  . VAL   W  9  36  ? 12.755  -158.141 3.793   1.00 96.41  ? 35  VAL   W CA  1 
ATOM   39628 C  C   . VAL   W  9  36  ? 11.712  -159.054 3.129   1.00 96.03  ? 35  VAL   W C   1 
ATOM   39629 O  O   . VAL   W  9  36  ? 11.830  -159.284 1.901   1.00 96.66  ? 35  VAL   W O   1 
ATOM   39630 C  CB  . VAL   W  9  36  ? 13.815  -158.968 4.546   1.00 93.55  ? 35  VAL   W CB  1 
ATOM   39631 C  CG1 . VAL   W  9  36  ? 14.411  -160.052 3.661   1.00 92.01  ? 35  VAL   W CG1 1 
ATOM   39632 C  CG2 . VAL   W  9  36  ? 14.920  -158.089 5.111   1.00 95.82  ? 35  VAL   W CG2 1 
ATOM   39633 N  N   . SER   W  9  37  ? 10.765  -159.592 3.907   1.00 96.16  ? 36  SER   W N   1 
ATOM   39634 C  CA  . SER   W  9  37  ? 9.708   -160.518 3.420   1.00 96.76  ? 36  SER   W CA  1 
ATOM   39635 C  C   . SER   W  9  37  ? 8.331   -160.125 3.962   1.00 96.12  ? 36  SER   W C   1 
ATOM   39636 O  O   . SER   W  9  37  ? 8.218   -159.848 5.171   1.00 96.19  ? 36  SER   W O   1 
ATOM   39637 C  CB  . SER   W  9  37  ? 10.028  -161.940 3.777   1.00 96.24  ? 36  SER   W CB  1 
ATOM   39638 O  OG  . SER   W  9  37  ? 9.005   -162.818 3.323   1.00 95.26  ? 36  SER   W OG  1 
ATOM   39639 N  N   . ASN   W  9  38  ? 7.323   -160.176 3.087   1.00 97.70  ? 37  ASN   W N   1 
ATOM   39640 C  CA  . ASN   W  9  38  ? 5.889   -159.934 3.400   1.00 103.74 ? 37  ASN   W CA  1 
ATOM   39641 C  C   . ASN   W  9  38  ? 5.107   -161.235 3.174   1.00 101.80 ? 37  ASN   W C   1 
ATOM   39642 O  O   . ASN   W  9  38  ? 3.906   -161.155 2.853   1.00 100.87 ? 37  ASN   W O   1 
ATOM   39643 C  CB  . ASN   W  9  38  ? 5.308   -158.759 2.599   1.00 113.92 ? 37  ASN   W CB  1 
ATOM   39644 C  CG  . ASN   W  9  38  ? 6.018   -158.475 1.289   1.00 122.34 ? 37  ASN   W CG  1 
ATOM   39645 O  OD1 . ASN   W  9  38  ? 6.389   -157.333 1.019   1.00 133.54 ? 37  ASN   W OD1 1 
ATOM   39646 N  ND2 . ASN   W  9  38  ? 6.207   -159.495 0.466   1.00 121.01 ? 37  ASN   W ND2 1 
ATOM   39647 N  N   . LYS   W  9  39  ? 5.769   -162.384 3.346   1.00 99.20  ? 38  LYS   W N   1 
ATOM   39648 C  CA  . LYS   W  9  39  ? 5.186   -163.738 3.141   1.00 100.78 ? 38  LYS   W CA  1 
ATOM   39649 C  C   . LYS   W  9  39  ? 5.542   -164.670 4.306   1.00 99.46  ? 38  LYS   W C   1 
ATOM   39650 O  O   . LYS   W  9  39  ? 5.245   -165.873 4.196   1.00 99.69  ? 38  LYS   W O   1 
ATOM   39651 C  CB  . LYS   W  9  39  ? 5.708   -164.332 1.830   1.00 105.00 ? 38  LYS   W CB  1 
ATOM   39652 C  CG  . LYS   W  9  39  ? 5.105   -163.743 0.563   1.00 107.77 ? 38  LYS   W CG  1 
ATOM   39653 C  CD  . LYS   W  9  39  ? 6.051   -163.790 -0.617  1.00 109.35 ? 38  LYS   W CD  1 
ATOM   39654 C  CE  . LYS   W  9  39  ? 5.341   -163.811 -1.953  1.00 111.74 ? 38  LYS   W CE  1 
ATOM   39655 N  NZ  . LYS   W  9  39  ? 4.392   -162.682 -2.091  1.00 112.19 ? 38  LYS   W NZ  1 
ATOM   39656 N  N   . PHE   W  9  40  ? 6.139   -164.149 5.382   1.00 96.47  ? 39  PHE   W N   1 
ATOM   39657 C  CA  . PHE   W  9  40  ? 6.676   -164.958 6.509   1.00 95.44  ? 39  PHE   W CA  1 
ATOM   39658 C  C   . PHE   W  9  40  ? 5.555   -165.257 7.512   1.00 93.70  ? 39  PHE   W C   1 
ATOM   39659 O  O   . PHE   W  9  40  ? 5.327   -164.446 8.433   1.00 89.62  ? 39  PHE   W O   1 
ATOM   39660 C  CB  . PHE   W  9  40  ? 7.857   -164.249 7.174   1.00 93.41  ? 39  PHE   W CB  1 
ATOM   39661 C  CG  . PHE   W  9  40  ? 8.660   -165.134 8.093   1.00 94.39  ? 39  PHE   W CG  1 
ATOM   39662 C  CD1 . PHE   W  9  40  ? 9.581   -166.034 7.578   1.00 96.18  ? 39  PHE   W CD1 1 
ATOM   39663 C  CD2 . PHE   W  9  40  ? 8.485   -165.084 9.468   1.00 94.22  ? 39  PHE   W CD2 1 
ATOM   39664 C  CE1 . PHE   W  9  40  ? 10.318  -166.856 8.417   1.00 95.12  ? 39  PHE   W CE1 1 
ATOM   39665 C  CE2 . PHE   W  9  40  ? 9.224   -165.907 10.305  1.00 93.25  ? 39  PHE   W CE2 1 
ATOM   39666 C  CZ  . PHE   W  9  40  ? 10.139  -166.790 9.779   1.00 92.67  ? 39  PHE   W CZ  1 
ATOM   39667 N  N   . GLU   W  9  41  ? 4.884   -166.400 7.338   1.00 94.91  ? 40  GLU   W N   1 
ATOM   39668 C  CA  . GLU   W  9  41  ? 3.797   -166.875 8.237   1.00 94.56  ? 40  GLU   W CA  1 
ATOM   39669 C  C   . GLU   W  9  41  ? 4.424   -167.421 9.523   1.00 92.57  ? 40  GLU   W C   1 
ATOM   39670 O  O   . GLU   W  9  41  ? 5.476   -168.089 9.439   1.00 88.78  ? 40  GLU   W O   1 
ATOM   39671 C  CB  . GLU   W  9  41  ? 2.929   -167.926 7.544   1.00 97.25  ? 40  GLU   W CB  1 
ATOM   39672 C  CG  . GLU   W  9  41  ? 2.195   -167.386 6.329   1.00 98.02  ? 40  GLU   W CG  1 
ATOM   39673 C  CD  . GLU   W  9  41  ? 1.044   -168.240 5.826   1.00 98.58  ? 40  GLU   W CD  1 
ATOM   39674 O  OE1 . GLU   W  9  41  ? 0.533   -167.940 4.729   1.00 100.43 ? 40  GLU   W OE1 1 
ATOM   39675 O  OE2 . GLU   W  9  41  ? 0.653   -169.192 6.533   1.00 100.12 ? 40  GLU   W OE2 1 
ATOM   39676 N  N   . LYS   W  9  42  ? 3.796   -167.129 10.664  1.00 92.63  ? 41  LYS   W N   1 
ATOM   39677 C  CA  . LYS   W  9  42  ? 4.314   -167.451 12.019  1.00 92.98  ? 41  LYS   W CA  1 
ATOM   39678 C  C   . LYS   W  9  42  ? 3.414   -168.486 12.701  1.00 92.82  ? 41  LYS   W C   1 
ATOM   39679 O  O   . LYS   W  9  42  ? 3.696   -168.815 13.867  1.00 91.21  ? 41  LYS   W O   1 
ATOM   39680 C  CB  . LYS   W  9  42  ? 4.416   -166.163 12.839  1.00 94.00  ? 41  LYS   W CB  1 
ATOM   39681 C  CG  . LYS   W  9  42  ? 5.503   -165.213 12.359  1.00 94.53  ? 41  LYS   W CG  1 
ATOM   39682 C  CD  . LYS   W  9  42  ? 5.369   -163.804 12.872  1.00 95.64  ? 41  LYS   W CD  1 
ATOM   39683 C  CE  . LYS   W  9  42  ? 6.224   -162.835 12.085  1.00 96.46  ? 41  LYS   W CE  1 
ATOM   39684 N  NZ  . LYS   W  9  42  ? 5.600   -162.477 10.790  1.00 97.45  ? 41  LYS   W NZ  1 
ATOM   39685 N  N   . ILE   W  9  43  ? 2.390   -168.987 12.002  1.00 92.69  ? 42  ILE   W N   1 
ATOM   39686 C  CA  . ILE   W  9  43  ? 1.465   -170.041 12.517  1.00 93.75  ? 42  ILE   W CA  1 
ATOM   39687 C  C   . ILE   W  9  43  ? 1.710   -171.341 11.743  1.00 94.90  ? 42  ILE   W C   1 
ATOM   39688 O  O   . ILE   W  9  43  ? 1.732   -171.307 10.494  1.00 95.54  ? 42  ILE   W O   1 
ATOM   39689 C  CB  . ILE   W  9  43  ? -0.007  -169.585 12.449  1.00 94.57  ? 42  ILE   W CB  1 
ATOM   39690 C  CG1 . ILE   W  9  43  ? -0.253  -168.382 13.362  1.00 92.43  ? 42  ILE   W CG1 1 
ATOM   39691 C  CG2 . ILE   W  9  43  ? -0.947  -170.738 12.778  1.00 96.71  ? 42  ILE   W CG2 1 
ATOM   39692 C  CD1 . ILE   W  9  43  ? -1.569  -167.687 13.124  1.00 92.88  ? 42  ILE   W CD1 1 
ATOM   39693 N  N   . PHE   W  9  44  ? 1.882   -172.435 12.489  1.00 93.61  ? 43  PHE   W N   1 
ATOM   39694 C  CA  . PHE   W  9  44  ? 2.091   -173.820 11.996  1.00 93.70  ? 43  PHE   W CA  1 
ATOM   39695 C  C   . PHE   W  9  44  ? 1.067   -174.717 12.696  1.00 95.46  ? 43  PHE   W C   1 
ATOM   39696 O  O   . PHE   W  9  44  ? 0.504   -174.272 13.719  1.00 92.92  ? 43  PHE   W O   1 
ATOM   39697 C  CB  . PHE   W  9  44  ? 3.534   -174.254 12.270  1.00 91.22  ? 43  PHE   W CB  1 
ATOM   39698 C  CG  . PHE   W  9  44  ? 4.570   -173.206 11.946  1.00 89.32  ? 43  PHE   W CG  1 
ATOM   39699 C  CD1 . PHE   W  9  44  ? 5.136   -173.135 10.682  1.00 88.83  ? 43  PHE   W CD1 1 
ATOM   39700 C  CD2 . PHE   W  9  44  ? 4.966   -172.279 12.898  1.00 87.55  ? 43  PHE   W CD2 1 
ATOM   39701 C  CE1 . PHE   W  9  44  ? 6.083   -172.170 10.380  1.00 89.11  ? 43  PHE   W CE1 1 
ATOM   39702 C  CE2 . PHE   W  9  44  ? 5.913   -171.312 12.594  1.00 88.57  ? 43  PHE   W CE2 1 
ATOM   39703 C  CZ  . PHE   W  9  44  ? 6.470   -171.260 11.336  1.00 89.03  ? 43  PHE   W CZ  1 
ATOM   39704 N  N   . HIS   W  9  45  ? 0.816   -175.918 12.165  1.00 97.11  ? 44  HIS   W N   1 
ATOM   39705 C  CA  . HIS   W  9  45  ? -0.064  -176.928 12.814  1.00 97.88  ? 44  HIS   W CA  1 
ATOM   39706 C  C   . HIS   W  9  45  ? 0.517   -178.338 12.670  1.00 96.83  ? 44  HIS   W C   1 
ATOM   39707 O  O   . HIS   W  9  45  ? 1.178   -178.625 11.650  1.00 90.25  ? 44  HIS   W O   1 
ATOM   39708 C  CB  . HIS   W  9  45  ? -1.506  -176.825 12.295  1.00 102.50 ? 44  HIS   W CB  1 
ATOM   39709 C  CG  . HIS   W  9  45  ? -1.664  -177.105 10.839  1.00 104.69 ? 44  HIS   W CG  1 
ATOM   39710 N  ND1 . HIS   W  9  45  ? -1.945  -178.368 10.357  1.00 106.62 ? 44  HIS   W ND1 1 
ATOM   39711 C  CD2 . HIS   W  9  45  ? -1.601  -176.292 9.764   1.00 106.59 ? 44  HIS   W CD2 1 
ATOM   39712 C  CE1 . HIS   W  9  45  ? -2.041  -178.322 9.044   1.00 107.63 ? 44  HIS   W CE1 1 
ATOM   39713 N  NE2 . HIS   W  9  45  ? -1.834  -177.060 8.655   1.00 106.55 ? 44  HIS   W NE2 1 
ATOM   39714 N  N   . TYR   W  9  46  ? 0.270   -179.160 13.693  1.00 95.46  ? 45  TYR   W N   1 
ATOM   39715 C  CA  . TYR   W  9  46  ? 0.676   -180.583 13.808  1.00 93.46  ? 45  TYR   W CA  1 
ATOM   39716 C  C   . TYR   W  9  46  ? -0.587  -181.388 14.120  1.00 91.89  ? 45  TYR   W C   1 
ATOM   39717 O  O   . TYR   W  9  46  ? -1.007  -181.441 15.292  1.00 91.92  ? 45  TYR   W O   1 
ATOM   39718 C  CB  . TYR   W  9  46  ? 1.775   -180.715 14.866  1.00 92.72  ? 45  TYR   W CB  1 
ATOM   39719 C  CG  . TYR   W  9  46  ? 2.779   -179.591 14.831  1.00 91.19  ? 45  TYR   W CG  1 
ATOM   39720 C  CD1 . TYR   W  9  46  ? 3.801   -179.575 13.895  1.00 90.46  ? 45  TYR   W CD1 1 
ATOM   39721 C  CD2 . TYR   W  9  46  ? 2.688   -178.522 15.710  1.00 89.57  ? 45  TYR   W CD2 1 
ATOM   39722 C  CE1 . TYR   W  9  46  ? 4.720   -178.539 13.846  1.00 88.99  ? 45  TYR   W CE1 1 
ATOM   39723 C  CE2 . TYR   W  9  46  ? 3.599   -177.478 15.674  1.00 88.06  ? 45  TYR   W CE2 1 
ATOM   39724 C  CZ  . TYR   W  9  46  ? 4.619   -177.486 14.739  1.00 87.91  ? 45  TYR   W CZ  1 
ATOM   39725 O  OH  . TYR   W  9  46  ? 5.516   -176.457 14.698  1.00 84.46  ? 45  TYR   W OH  1 
ATOM   39726 N  N   . GLY   W  9  47  ? -1.196  -181.964 13.084  1.00 90.98  ? 46  GLY   W N   1 
ATOM   39727 C  CA  . GLY   W  9  47  ? -2.586  -182.445 13.144  1.00 93.89  ? 46  GLY   W CA  1 
ATOM   39728 C  C   . GLY   W  9  47  ? -3.525  -181.274 13.363  1.00 93.96  ? 46  GLY   W C   1 
ATOM   39729 O  O   . GLY   W  9  47  ? -3.445  -180.320 12.576  1.00 96.73  ? 46  GLY   W O   1 
ATOM   39730 N  N   . HIS   W  9  48  ? -4.334  -181.316 14.425  1.00 95.30  ? 47  HIS   W N   1 
ATOM   39731 C  CA  . HIS   W  9  48  ? -5.377  -180.303 14.748  1.00 96.43  ? 47  HIS   W CA  1 
ATOM   39732 C  C   . HIS   W  9  48  ? -4.871  -179.303 15.796  1.00 94.62  ? 47  HIS   W C   1 
ATOM   39733 O  O   . HIS   W  9  48  ? -5.673  -178.443 16.213  1.00 95.67  ? 47  HIS   W O   1 
ATOM   39734 C  CB  . HIS   W  9  48  ? -6.659  -180.989 15.235  1.00 99.18  ? 47  HIS   W CB  1 
ATOM   39735 C  CG  . HIS   W  9  48  ? -6.488  -181.708 16.531  1.00 100.46 ? 47  HIS   W CG  1 
ATOM   39736 N  ND1 . HIS   W  9  48  ? -6.091  -183.030 16.592  1.00 102.23 ? 47  HIS   W ND1 1 
ATOM   39737 C  CD2 . HIS   W  9  48  ? -6.634  -181.295 17.808  1.00 99.75  ? 47  HIS   W CD2 1 
ATOM   39738 C  CE1 . HIS   W  9  48  ? -6.011  -183.403 17.852  1.00 102.23 ? 47  HIS   W CE1 1 
ATOM   39739 N  NE2 . HIS   W  9  48  ? -6.338  -182.356 18.619  1.00 100.75 ? 47  HIS   W NE2 1 
ATOM   39740 N  N   . VAL   W  9  49  ? -3.611  -179.421 16.227  1.00 94.25  ? 48  VAL   W N   1 
ATOM   39741 C  CA  . VAL   W  9  49  ? -2.981  -178.514 17.233  1.00 95.34  ? 48  VAL   W CA  1 
ATOM   39742 C  C   . VAL   W  9  49  ? -2.177  -177.452 16.480  1.00 95.65  ? 48  VAL   W C   1 
ATOM   39743 O  O   . VAL   W  9  49  ? -1.229  -177.839 15.766  1.00 95.73  ? 48  VAL   W O   1 
ATOM   39744 C  CB  . VAL   W  9  49  ? -2.093  -179.290 18.224  1.00 94.00  ? 48  VAL   W CB  1 
ATOM   39745 C  CG1 . VAL   W  9  49  ? -1.439  -178.373 19.245  1.00 91.78  ? 48  VAL   W CG1 1 
ATOM   39746 C  CG2 . VAL   W  9  49  ? -2.871  -180.393 18.925  1.00 97.91  ? 48  VAL   W CG2 1 
ATOM   39747 N  N   . PHE   W  9  50  ? -2.545  -176.175 16.646  1.00 96.92  ? 49  PHE   W N   1 
ATOM   39748 C  CA  . PHE   W  9  50  ? -1.908  -175.002 15.988  1.00 93.98  ? 49  PHE   W CA  1 
ATOM   39749 C  C   . PHE   W  9  50  ? -0.917  -174.343 16.951  1.00 92.79  ? 49  PHE   W C   1 
ATOM   39750 O  O   . PHE   W  9  50  ? -1.242  -174.184 18.144  1.00 90.31  ? 49  PHE   W O   1 
ATOM   39751 C  CB  . PHE   W  9  50  ? -2.966  -174.002 15.516  1.00 94.73  ? 49  PHE   W CB  1 
ATOM   39752 C  CG  . PHE   W  9  50  ? -3.695  -174.428 14.269  1.00 98.06  ? 49  PHE   W CG  1 
ATOM   39753 C  CD1 . PHE   W  9  50  ? -4.684  -175.399 14.323  1.00 101.43 ? 49  PHE   W CD1 1 
ATOM   39754 C  CD2 . PHE   W  9  50  ? -3.386  -173.866 13.040  1.00 99.01  ? 49  PHE   W CD2 1 
ATOM   39755 C  CE1 . PHE   W  9  50  ? -5.351  -175.796 13.174  1.00 103.40 ? 49  PHE   W CE1 1 
ATOM   39756 C  CE2 . PHE   W  9  50  ? -4.054  -174.265 11.892  1.00 101.82 ? 49  PHE   W CE2 1 
ATOM   39757 C  CZ  . PHE   W  9  50  ? -5.035  -175.228 11.961  1.00 103.32 ? 49  PHE   W CZ  1 
ATOM   39758 N  N   . LEU   W  9  51  ? 0.258   -173.976 16.430  1.00 91.68  ? 50  LEU   W N   1 
ATOM   39759 C  CA  . LEU   W  9  51  ? 1.335   -173.266 17.168  1.00 94.49  ? 50  LEU   W CA  1 
ATOM   39760 C  C   . LEU   W  9  51  ? 1.744   -172.017 16.382  1.00 96.18  ? 50  LEU   W C   1 
ATOM   39761 O  O   . LEU   W  9  51  ? 2.153   -172.169 15.212  1.00 97.26  ? 50  LEU   W O   1 
ATOM   39762 C  CB  . LEU   W  9  51  ? 2.535   -174.200 17.347  1.00 94.49  ? 50  LEU   W CB  1 
ATOM   39763 C  CG  . LEU   W  9  51  ? 3.763   -173.576 18.013  1.00 94.21  ? 50  LEU   W CG  1 
ATOM   39764 C  CD1 . LEU   W  9  51  ? 3.478   -173.232 19.467  1.00 95.18  ? 50  LEU   W CD1 1 
ATOM   39765 C  CD2 . LEU   W  9  51  ? 4.967   -174.499 17.912  1.00 94.53  ? 50  LEU   W CD2 1 
ATOM   39766 N  N   . GLY   W  9  52  ? 1.639   -170.842 17.013  1.00 97.54  ? 51  GLY   W N   1 
ATOM   39767 C  CA  . GLY   W  9  52  ? 2.193   -169.566 16.518  1.00 95.04  ? 51  GLY   W CA  1 
ATOM   39768 C  C   . GLY   W  9  52  ? 3.453   -169.202 17.283  1.00 92.39  ? 51  GLY   W C   1 
ATOM   39769 O  O   . GLY   W  9  52  ? 3.457   -169.388 18.512  1.00 93.07  ? 51  GLY   W O   1 
ATOM   39770 N  N   . ILE   W  9  53  ? 4.494   -168.724 16.592  1.00 90.38  ? 52  ILE   W N   1 
ATOM   39771 C  CA  . ILE   W  9  53  ? 5.810   -168.375 17.210  1.00 90.39  ? 52  ILE   W CA  1 
ATOM   39772 C  C   . ILE   W  9  53  ? 6.261   -166.994 16.717  1.00 89.21  ? 52  ILE   W C   1 
ATOM   39773 O  O   . ILE   W  9  53  ? 6.460   -166.835 15.496  1.00 91.88  ? 52  ILE   W O   1 
ATOM   39774 C  CB  . ILE   W  9  53  ? 6.877   -169.448 16.914  1.00 91.30  ? 52  ILE   W CB  1 
ATOM   39775 C  CG1 . ILE   W  9  53  ? 6.324   -170.873 17.019  1.00 93.19  ? 52  ILE   W CG1 1 
ATOM   39776 C  CG2 . ILE   W  9  53  ? 8.083   -169.245 17.820  1.00 90.07  ? 52  ILE   W CG2 1 
ATOM   39777 C  CD1 . ILE   W  9  53  ? 7.270   -171.943 16.514  1.00 95.66  ? 52  ILE   W CD1 1 
ATOM   39778 N  N   . THR   W  9  54  ? 6.436   -166.047 17.646  1.00 86.57  ? 53  THR   W N   1 
ATOM   39779 C  CA  . THR   W  9  54  ? 7.061   -164.717 17.418  1.00 86.24  ? 53  THR   W CA  1 
ATOM   39780 C  C   . THR   W  9  54  ? 8.498   -164.738 17.943  1.00 83.10  ? 53  THR   W C   1 
ATOM   39781 O  O   . THR   W  9  54  ? 8.846   -165.686 18.661  1.00 84.17  ? 53  THR   W O   1 
ATOM   39782 C  CB  . THR   W  9  54  ? 6.283   -163.602 18.121  1.00 84.74  ? 53  THR   W CB  1 
ATOM   39783 O  OG1 . THR   W  9  54  ? 6.278   -163.890 19.519  1.00 84.03  ? 53  THR   W OG1 1 
ATOM   39784 C  CG2 . THR   W  9  54  ? 4.866   -163.466 17.615  1.00 86.96  ? 53  THR   W CG2 1 
ATOM   39785 N  N   . GLY   W  9  55  ? 9.284   -163.714 17.613  1.00 83.62  ? 54  GLY   W N   1 
ATOM   39786 C  CA  . GLY   W  9  55  ? 10.686  -163.575 18.050  1.00 83.31  ? 54  GLY   W CA  1 
ATOM   39787 C  C   . GLY   W  9  55  ? 11.648  -163.811 16.902  1.00 83.56  ? 54  GLY   W C   1 
ATOM   39788 O  O   . GLY   W  9  55  ? 11.229  -163.638 15.737  1.00 86.40  ? 54  GLY   W O   1 
ATOM   39789 N  N   . LEU   W  9  56  ? 12.885  -164.202 17.218  1.00 79.96  ? 55  LEU   W N   1 
ATOM   39790 C  CA  . LEU   W  9  56  ? 14.001  -164.345 16.244  1.00 81.92  ? 55  LEU   W CA  1 
ATOM   39791 C  C   . LEU   W  9  56  ? 13.613  -165.405 15.206  1.00 82.91  ? 55  LEU   W C   1 
ATOM   39792 O  O   . LEU   W  9  56  ? 13.320  -166.539 15.612  1.00 83.48  ? 55  LEU   W O   1 
ATOM   39793 C  CB  . LEU   W  9  56  ? 15.274  -164.719 17.009  1.00 80.67  ? 55  LEU   W CB  1 
ATOM   39794 C  CG  . LEU   W  9  56  ? 16.582  -164.636 16.225  1.00 82.37  ? 55  LEU   W CG  1 
ATOM   39795 C  CD1 . LEU   W  9  56  ? 16.882  -163.214 15.786  1.00 83.53  ? 55  LEU   W CD1 1 
ATOM   39796 C  CD2 . LEU   W  9  56  ? 17.733  -165.174 17.058  1.00 81.72  ? 55  LEU   W CD2 1 
ATOM   39797 N  N   . ALA   W  9  57  ? 13.585  -165.029 13.923  1.00 87.20  ? 56  ALA   W N   1 
ATOM   39798 C  CA  . ALA   W  9  57  ? 12.960  -165.795 12.816  1.00 89.64  ? 56  ALA   W CA  1 
ATOM   39799 C  C   . ALA   W  9  57  ? 13.659  -167.147 12.611  1.00 89.72  ? 56  ALA   W C   1 
ATOM   39800 O  O   . ALA   W  9  57  ? 12.961  -168.108 12.234  1.00 93.81  ? 56  ALA   W O   1 
ATOM   39801 C  CB  . ALA   W  9  57  ? 12.971  -164.979 11.549  1.00 90.30  ? 56  ALA   W CB  1 
ATOM   39802 N  N   . THR   W  9  58  ? 14.977  -167.224 12.827  1.00 90.07  ? 57  THR   W N   1 
ATOM   39803 C  CA  . THR   W  9  58  ? 15.768  -168.483 12.701  1.00 88.14  ? 57  THR   W CA  1 
ATOM   39804 C  C   . THR   W  9  58  ? 15.302  -169.499 13.754  1.00 88.61  ? 57  THR   W C   1 
ATOM   39805 O  O   . THR   W  9  58  ? 15.296  -170.703 13.441  1.00 92.35  ? 57  THR   W O   1 
ATOM   39806 C  CB  . THR   W  9  58  ? 17.279  -168.234 12.795  1.00 86.47  ? 57  THR   W CB  1 
ATOM   39807 O  OG1 . THR   W  9  58  ? 17.945  -169.492 12.686  1.00 85.71  ? 57  THR   W OG1 1 
ATOM   39808 C  CG2 . THR   W  9  58  ? 17.709  -167.566 14.082  1.00 85.41  ? 57  THR   W CG2 1 
ATOM   39809 N  N   . ASP   W  9  59  ? 14.932  -169.033 14.951  1.00 86.34  ? 58  ASP   W N   1 
ATOM   39810 C  CA  . ASP   W  9  59  ? 14.419  -169.883 16.061  1.00 85.68  ? 58  ASP   W CA  1 
ATOM   39811 C  C   . ASP   W  9  59  ? 12.957  -170.262 15.800  1.00 84.43  ? 58  ASP   W C   1 
ATOM   39812 O  O   . ASP   W  9  59  ? 12.569  -171.376 16.194  1.00 82.83  ? 58  ASP   W O   1 
ATOM   39813 C  CB  . ASP   W  9  59  ? 14.574  -169.187 17.415  1.00 83.77  ? 58  ASP   W CB  1 
ATOM   39814 C  CG  . ASP   W  9  59  ? 16.016  -169.082 17.876  1.00 84.15  ? 58  ASP   W CG  1 
ATOM   39815 O  OD1 . ASP   W  9  59  ? 16.893  -169.644 17.187  1.00 93.27  ? 58  ASP   W OD1 1 
ATOM   39816 O  OD2 . ASP   W  9  59  ? 16.250  -168.454 18.925  1.00 78.91  ? 58  ASP   W OD2 1 
ATOM   39817 N  N   . VAL   W  9  60  ? 12.175  -169.368 15.187  1.00 85.83  ? 59  VAL   W N   1 
ATOM   39818 C  CA  . VAL   W  9  60  ? 10.773  -169.647 14.749  1.00 87.44  ? 59  VAL   W CA  1 
ATOM   39819 C  C   . VAL   W  9  60  ? 10.809  -170.849 13.800  1.00 89.25  ? 59  VAL   W C   1 
ATOM   39820 O  O   . VAL   W  9  60  ? 10.048  -171.810 14.035  1.00 89.46  ? 59  VAL   W O   1 
ATOM   39821 C  CB  . VAL   W  9  60  ? 10.114  -168.426 14.075  1.00 89.26  ? 59  VAL   W CB  1 
ATOM   39822 C  CG1 . VAL   W  9  60  ? 8.820   -168.799 13.364  1.00 90.21  ? 59  VAL   W CG1 1 
ATOM   39823 C  CG2 . VAL   W  9  60  ? 9.868   -167.290 15.057  1.00 88.62  ? 59  VAL   W CG2 1 
ATOM   39824 N  N   . THR   W  9  61  ? 11.663  -170.785 12.773  1.00 89.52  ? 60  THR   W N   1 
ATOM   39825 C  CA  . THR   W  9  61  ? 11.859  -171.855 11.759  1.00 89.73  ? 60  THR   W CA  1 
ATOM   39826 C  C   . THR   W  9  61  ? 12.327  -173.138 12.453  1.00 91.06  ? 60  THR   W C   1 
ATOM   39827 O  O   . THR   W  9  61  ? 11.690  -174.186 12.235  1.00 94.91  ? 60  THR   W O   1 
ATOM   39828 C  CB  . THR   W  9  61  ? 12.864  -171.444 10.676  1.00 89.99  ? 60  THR   W CB  1 
ATOM   39829 O  OG1 . THR   W  9  61  ? 12.433  -170.209 10.103  1.00 89.58  ? 60  THR   W OG1 1 
ATOM   39830 C  CG2 . THR   W  9  61  ? 12.998  -172.488 9.588   1.00 90.88  ? 60  THR   W CG2 1 
ATOM   39831 N  N   . THR   W  9  62  ? 13.400  -173.055 13.245  1.00 86.95  ? 61  THR   W N   1 
ATOM   39832 C  CA  . THR   W  9  62  ? 14.016  -174.211 13.950  1.00 86.14  ? 61  THR   W CA  1 
ATOM   39833 C  C   . THR   W  9  62  ? 12.954  -174.925 14.794  1.00 87.33  ? 61  THR   W C   1 
ATOM   39834 O  O   . THR   W  9  62  ? 12.836  -176.157 14.657  1.00 91.32  ? 61  THR   W O   1 
ATOM   39835 C  CB  . THR   W  9  62  ? 15.207  -173.787 14.817  1.00 84.79  ? 61  THR   W CB  1 
ATOM   39836 O  OG1 . THR   W  9  62  ? 16.245  -173.323 13.953  1.00 84.05  ? 61  THR   W OG1 1 
ATOM   39837 C  CG2 . THR   W  9  62  ? 15.729  -174.915 15.681  1.00 83.30  ? 61  THR   W CG2 1 
ATOM   39838 N  N   . LEU   W  9  63  ? 12.217  -174.187 15.628  1.00 85.07  ? 62  LEU   W N   1 
ATOM   39839 C  CA  . LEU   W  9  63  ? 11.245  -174.773 16.593  1.00 86.16  ? 62  LEU   W CA  1 
ATOM   39840 C  C   . LEU   W  9  63  ? 10.083  -175.432 15.844  1.00 87.94  ? 62  LEU   W C   1 
ATOM   39841 O  O   . LEU   W  9  63  ? 9.616   -176.485 16.312  1.00 91.62  ? 62  LEU   W O   1 
ATOM   39842 C  CB  . LEU   W  9  63  ? 10.735  -173.698 17.558  1.00 87.44  ? 62  LEU   W CB  1 
ATOM   39843 C  CG  . LEU   W  9  63  ? 11.650  -173.371 18.737  1.00 88.16  ? 62  LEU   W CG  1 
ATOM   39844 C  CD1 . LEU   W  9  63  ? 10.934  -172.461 19.715  1.00 88.02  ? 62  LEU   W CD1 1 
ATOM   39845 C  CD2 . LEU   W  9  63  ? 12.126  -174.628 19.457  1.00 90.53  ? 62  LEU   W CD2 1 
ATOM   39846 N  N   . ASN   W  9  64  ? 9.633   -174.847 14.733  1.00 87.79  ? 63  ASN   W N   1 
ATOM   39847 C  CA  . ASN   W  9  64  ? 8.598   -175.461 13.859  1.00 91.05  ? 63  ASN   W CA  1 
ATOM   39848 C  C   . ASN   W  9  64  ? 9.091   -176.835 13.396  1.00 90.47  ? 63  ASN   W C   1 
ATOM   39849 O  O   . ASN   W  9  64  ? 8.348   -177.815 13.580  1.00 90.97  ? 63  ASN   W O   1 
ATOM   39850 C  CB  . ASN   W  9  64  ? 8.258   -174.589 12.650  1.00 91.29  ? 63  ASN   W CB  1 
ATOM   39851 C  CG  . ASN   W  9  64  ? 7.418   -175.327 11.631  1.00 92.79  ? 63  ASN   W CG  1 
ATOM   39852 O  OD1 . ASN   W  9  64  ? 6.485   -176.040 11.995  1.00 91.65  ? 63  ASN   W OD1 1 
ATOM   39853 N  ND2 . ASN   W  9  64  ? 7.746   -175.168 10.359  1.00 93.68  ? 63  ASN   W ND2 1 
ATOM   39854 N  N   . GLU   W  9  65  ? 10.299  -176.886 12.824  1.00 90.19  ? 64  GLU   W N   1 
ATOM   39855 C  CA  . GLU   W  9  65  ? 10.955  -178.126 12.324  1.00 92.61  ? 64  GLU   W CA  1 
ATOM   39856 C  C   . GLU   W  9  65  ? 11.110  -179.134 13.471  1.00 95.16  ? 64  GLU   W C   1 
ATOM   39857 O  O   . GLU   W  9  65  ? 10.943  -180.348 13.217  1.00 96.17  ? 64  GLU   W O   1 
ATOM   39858 C  CB  . GLU   W  9  65  ? 12.321  -177.801 11.716  1.00 94.23  ? 64  GLU   W CB  1 
ATOM   39859 C  CG  . GLU   W  9  65  ? 12.242  -176.984 10.440  1.00 95.31  ? 64  GLU   W CG  1 
ATOM   39860 C  CD  . GLU   W  9  65  ? 13.586  -176.539 9.889   1.00 97.84  ? 64  GLU   W CD  1 
ATOM   39861 O  OE1 . GLU   W  9  65  ? 13.604  -175.968 8.779   1.00 101.11 ? 64  GLU   W OE1 1 
ATOM   39862 O  OE2 . GLU   W  9  65  ? 14.612  -176.762 10.571  1.00 94.52  ? 64  GLU   W OE2 1 
ATOM   39863 N  N   . MET   W  9  66  ? 11.419  -178.643 14.676  1.00 94.02  ? 65  MET   W N   1 
ATOM   39864 C  CA  . MET   W  9  66  ? 11.686  -179.461 15.889  1.00 93.68  ? 65  MET   W CA  1 
ATOM   39865 C  C   . MET   W  9  66  ? 10.383  -180.082 16.405  1.00 92.61  ? 65  MET   W C   1 
ATOM   39866 O  O   . MET   W  9  66  ? 10.416  -181.264 16.779  1.00 94.89  ? 65  MET   W O   1 
ATOM   39867 C  CB  . MET   W  9  66  ? 12.313  -178.611 16.999  1.00 94.52  ? 65  MET   W CB  1 
ATOM   39868 C  CG  . MET   W  9  66  ? 12.881  -179.430 18.143  1.00 97.77  ? 65  MET   W CG  1 
ATOM   39869 S  SD  . MET   W  9  66  ? 13.293  -178.410 19.578  1.00 101.15 ? 65  MET   W SD  1 
ATOM   39870 C  CE  . MET   W  9  66  ? 11.656  -178.131 20.249  1.00 102.72 ? 65  MET   W CE  1 
ATOM   39871 N  N   . PHE   W  9  67  ? 9.287   -179.319 16.453  1.00 88.41  ? 66  PHE   W N   1 
ATOM   39872 C  CA  . PHE   W  9  67  ? 7.977   -179.791 16.979  1.00 90.26  ? 66  PHE   W CA  1 
ATOM   39873 C  C   . PHE   W  9  67  ? 7.287   -180.688 15.942  1.00 94.26  ? 66  PHE   W C   1 
ATOM   39874 O  O   . PHE   W  9  67  ? 6.513   -181.574 16.357  1.00 99.86  ? 66  PHE   W O   1 
ATOM   39875 C  CB  . PHE   W  9  67  ? 7.098   -178.619 17.425  1.00 88.70  ? 66  PHE   W CB  1 
ATOM   39876 C  CG  . PHE   W  9  67  ? 7.584   -177.937 18.679  1.00 89.31  ? 66  PHE   W CG  1 
ATOM   39877 C  CD1 . PHE   W  9  67  ? 7.855   -178.667 19.827  1.00 88.48  ? 66  PHE   W CD1 1 
ATOM   39878 C  CD2 . PHE   W  9  67  ? 7.779   -176.565 18.715  1.00 89.84  ? 66  PHE   W CD2 1 
ATOM   39879 C  CE1 . PHE   W  9  67  ? 8.312   -178.042 20.977  1.00 87.21  ? 66  PHE   W CE1 1 
ATOM   39880 C  CE2 . PHE   W  9  67  ? 8.235   -175.942 19.867  1.00 88.75  ? 66  PHE   W CE2 1 
ATOM   39881 C  CZ  . PHE   W  9  67  ? 8.501   -176.681 20.994  1.00 86.30  ? 66  PHE   W CZ  1 
ATOM   39882 N  N   . ARG   W  9  68  ? 7.557   -180.486 14.649  1.00 93.26  ? 67  ARG   W N   1 
ATOM   39883 C  CA  . ARG   W  9  68  ? 7.112   -181.408 13.569  1.00 95.45  ? 67  ARG   W CA  1 
ATOM   39884 C  C   . ARG   W  9  68  ? 7.779   -182.770 13.794  1.00 94.17  ? 67  ARG   W C   1 
ATOM   39885 O  O   . ARG   W  9  68  ? 7.062   -183.788 13.817  1.00 96.69  ? 67  ARG   W O   1 
ATOM   39886 C  CB  . ARG   W  9  68  ? 7.467   -180.851 12.189  1.00 96.13  ? 67  ARG   W CB  1 
ATOM   39887 C  CG  . ARG   W  9  68  ? 6.996   -181.723 11.034  1.00 99.39  ? 67  ARG   W CG  1 
ATOM   39888 C  CD  . ARG   W  9  68  ? 7.281   -181.103 9.683   1.00 101.05 ? 67  ARG   W CD  1 
ATOM   39889 N  NE  . ARG   W  9  68  ? 8.704   -180.875 9.461   1.00 102.51 ? 67  ARG   W NE  1 
ATOM   39890 C  CZ  . ARG   W  9  68  ? 9.229   -180.407 8.331   1.00 105.80 ? 67  ARG   W CZ  1 
ATOM   39891 N  NH1 . ARG   W  9  68  ? 8.450   -180.109 7.303   1.00 111.11 ? 67  ARG   W NH1 1 
ATOM   39892 N  NH2 . ARG   W  9  68  ? 10.537  -180.241 8.232   1.00 107.29 ? 67  ARG   W NH2 1 
ATOM   39893 N  N   . TYR   W  9  69  ? 9.106   -182.761 13.953  1.00 93.91  ? 68  TYR   W N   1 
ATOM   39894 C  CA  . TYR   W  9  69  ? 9.961   -183.930 14.291  1.00 92.57  ? 68  TYR   W CA  1 
ATOM   39895 C  C   . TYR   W  9  69  ? 9.361   -184.689 15.481  1.00 91.73  ? 68  TYR   W C   1 
ATOM   39896 O  O   . TYR   W  9  69  ? 9.212   -185.920 15.388  1.00 92.35  ? 68  TYR   W O   1 
ATOM   39897 C  CB  . TYR   W  9  69  ? 11.384  -183.448 14.588  1.00 94.64  ? 68  TYR   W CB  1 
ATOM   39898 C  CG  . TYR   W  9  69  ? 12.397  -184.505 14.953  1.00 93.96  ? 68  TYR   W CG  1 
ATOM   39899 C  CD1 . TYR   W  9  69  ? 12.302  -185.223 16.135  1.00 92.12  ? 68  TYR   W CD1 1 
ATOM   39900 C  CD2 . TYR   W  9  69  ? 13.497  -184.740 14.143  1.00 93.95  ? 68  TYR   W CD2 1 
ATOM   39901 C  CE1 . TYR   W  9  69  ? 13.247  -186.174 16.480  1.00 93.67  ? 68  TYR   W CE1 1 
ATOM   39902 C  CE2 . TYR   W  9  69  ? 14.452  -185.687 14.474  1.00 93.82  ? 68  TYR   W CE2 1 
ATOM   39903 C  CZ  . TYR   W  9  69  ? 14.326  -186.408 15.647  1.00 94.81  ? 68  TYR   W CZ  1 
ATOM   39904 O  OH  . TYR   W  9  69  ? 15.257  -187.346 15.990  1.00 96.55  ? 68  TYR   W OH  1 
ATOM   39905 N  N   . LYS   W  9  70  ? 9.034   -183.976 16.562  1.00 86.94  ? 69  LYS   W N   1 
ATOM   39906 C  CA  . LYS   W  9  70  ? 8.656   -184.573 17.871  1.00 88.80  ? 69  LYS   W CA  1 
ATOM   39907 C  C   . LYS   W  9  70  ? 7.214   -185.094 17.825  1.00 90.13  ? 69  LYS   W C   1 
ATOM   39908 O  O   . LYS   W  9  70  ? 6.965   -186.165 18.413  1.00 92.31  ? 69  LYS   W O   1 
ATOM   39909 C  CB  . LYS   W  9  70  ? 8.882   -183.568 19.005  1.00 86.68  ? 69  LYS   W CB  1 
ATOM   39910 C  CG  . LYS   W  9  70  ? 10.344  -183.398 19.394  1.00 86.20  ? 69  LYS   W CG  1 
ATOM   39911 C  CD  . LYS   W  9  70  ? 10.581  -182.523 20.599  1.00 87.02  ? 69  LYS   W CD  1 
ATOM   39912 C  CE  . LYS   W  9  70  ? 12.043  -182.480 20.985  1.00 89.46  ? 69  LYS   W CE  1 
ATOM   39913 N  NZ  . LYS   W  9  70  ? 12.249  -181.841 22.306  1.00 91.04  ? 69  LYS   W NZ  1 
ATOM   39914 N  N   . THR   W  9  71  ? 6.301   -184.388 17.156  1.00 90.22  ? 70  THR   W N   1 
ATOM   39915 C  CA  . THR   W  9  71  ? 4.873   -184.791 17.029  1.00 92.94  ? 70  THR   W CA  1 
ATOM   39916 C  C   . THR   W  9  71  ? 4.730   -185.959 16.045  1.00 94.27  ? 70  THR   W C   1 
ATOM   39917 O  O   . THR   W  9  71  ? 3.775   -186.745 16.211  1.00 97.37  ? 70  THR   W O   1 
ATOM   39918 C  CB  . THR   W  9  71  ? 3.985   -183.614 16.609  1.00 93.10  ? 70  THR   W CB  1 
ATOM   39919 O  OG1 . THR   W  9  71  ? 4.588   -182.954 15.495  1.00 91.46  ? 70  THR   W OG1 1 
ATOM   39920 C  CG2 . THR   W  9  71  ? 3.770   -182.630 17.735  1.00 92.52  ? 70  THR   W CG2 1 
ATOM   39921 N  N   . ASN   W  9  72  ? 5.622   -186.056 15.052  1.00 93.44  ? 71  ASN   W N   1 
ATOM   39922 C  CA  . ASN   W  9  72  ? 5.643   -187.162 14.057  1.00 93.20  ? 71  ASN   W CA  1 
ATOM   39923 C  C   . ASN   W  9  72  ? 5.991   -188.473 14.771  1.00 93.57  ? 71  ASN   W C   1 
ATOM   39924 O  O   . ASN   W  9  72  ? 5.279   -189.471 14.534  1.00 97.97  ? 71  ASN   W O   1 
ATOM   39925 C  CB  . ASN   W  9  72  ? 6.597   -186.870 12.894  1.00 92.41  ? 71  ASN   W CB  1 
ATOM   39926 C  CG  . ASN   W  9  72  ? 6.001   -185.929 11.866  1.00 91.72  ? 71  ASN   W CG  1 
ATOM   39927 O  OD1 . ASN   W  9  72  ? 5.018   -185.242 12.138  1.00 87.53  ? 71  ASN   W OD1 1 
ATOM   39928 N  ND2 . ASN   W  9  72  ? 6.582   -185.895 10.679  1.00 94.86  ? 71  ASN   W ND2 1 
ATOM   39929 N  N   . LEU   W  9  73  ? 7.030   -188.463 15.615  1.00 90.57  ? 72  LEU   W N   1 
ATOM   39930 C  CA  . LEU   W  9  73  ? 7.468   -189.640 16.415  1.00 89.57  ? 72  LEU   W CA  1 
ATOM   39931 C  C   . LEU   W  9  73  ? 6.402   -189.966 17.467  1.00 89.62  ? 72  LEU   W C   1 
ATOM   39932 O  O   . LEU   W  9  73  ? 6.187   -191.169 17.724  1.00 91.01  ? 72  LEU   W O   1 
ATOM   39933 C  CB  . LEU   W  9  73  ? 8.821   -189.358 17.081  1.00 88.03  ? 72  LEU   W CB  1 
ATOM   39934 C  CG  . LEU   W  9  73  ? 10.045  -189.355 16.164  1.00 88.21  ? 72  LEU   W CG  1 
ATOM   39935 C  CD1 . LEU   W  9  73  ? 11.311  -189.093 16.966  1.00 87.84  ? 72  LEU   W CD1 1 
ATOM   39936 C  CD2 . LEU   W  9  73  ? 10.179  -190.663 15.394  1.00 88.59  ? 72  LEU   W CD2 1 
ATOM   39937 N  N   . TYR   W  9  74  ? 5.775   -188.940 18.055  1.00 88.30  ? 73  TYR   W N   1 
ATOM   39938 C  CA  . TYR   W  9  74  ? 4.673   -189.079 19.044  1.00 88.48  ? 73  TYR   W CA  1 
ATOM   39939 C  C   . TYR   W  9  74  ? 3.554   -189.920 18.424  1.00 92.79  ? 73  TYR   W C   1 
ATOM   39940 O  O   . TYR   W  9  74  ? 3.124   -190.900 19.052  1.00 94.86  ? 73  TYR   W O   1 
ATOM   39941 C  CB  . TYR   W  9  74  ? 4.148   -187.711 19.493  1.00 86.91  ? 73  TYR   W CB  1 
ATOM   39942 C  CG  . TYR   W  9  74  ? 3.043   -187.759 20.520  1.00 89.04  ? 73  TYR   W CG  1 
ATOM   39943 C  CD1 . TYR   W  9  74  ? 1.711   -187.831 20.140  1.00 90.20  ? 73  TYR   W CD1 1 
ATOM   39944 C  CD2 . TYR   W  9  74  ? 3.323   -187.730 21.877  1.00 87.69  ? 73  TYR   W CD2 1 
ATOM   39945 C  CE1 . TYR   W  9  74  ? 0.689   -187.872 21.076  1.00 91.20  ? 73  TYR   W CE1 1 
ATOM   39946 C  CE2 . TYR   W  9  74  ? 2.314   -187.775 22.828  1.00 89.30  ? 73  TYR   W CE2 1 
ATOM   39947 C  CZ  . TYR   W  9  74  ? 0.991   -187.843 22.426  1.00 89.72  ? 73  TYR   W CZ  1 
ATOM   39948 O  OH  . TYR   W  9  74  ? -0.010  -187.885 23.353  1.00 91.38  ? 73  TYR   W OH  1 
ATOM   39949 N  N   . LYS   W  9  75  ? 3.126   -189.553 17.214  1.00 93.52  ? 74  LYS   W N   1 
ATOM   39950 C  CA  . LYS   W  9  75  ? 1.975   -190.171 16.505  1.00 97.18  ? 74  LYS   W CA  1 
ATOM   39951 C  C   . LYS   W  9  75  ? 2.293   -191.623 16.119  1.00 99.10  ? 74  LYS   W C   1 
ATOM   39952 O  O   . LYS   W  9  75  ? 1.374   -192.460 16.198  1.00 100.55 ? 74  LYS   W O   1 
ATOM   39953 C  CB  . LYS   W  9  75  ? 1.613   -189.356 15.262  1.00 97.88  ? 74  LYS   W CB  1 
ATOM   39954 C  CG  . LYS   W  9  75  ? 0.282   -189.737 14.636  1.00 101.56 ? 74  LYS   W CG  1 
ATOM   39955 C  CD  . LYS   W  9  75  ? -0.030  -188.975 13.383  1.00 103.99 ? 74  LYS   W CD  1 
ATOM   39956 C  CE  . LYS   W  9  75  ? -1.403  -189.310 12.847  1.00 110.08 ? 74  LYS   W CE  1 
ATOM   39957 N  NZ  . LYS   W  9  75  ? -1.835  -188.327 11.829  1.00 113.60 ? 74  LYS   W NZ  1 
ATOM   39958 N  N   . LEU   W  9  76  ? 3.531   -191.902 15.698  1.00 99.07  ? 75  LEU   W N   1 
ATOM   39959 C  CA  . LEU   W  9  76  ? 3.985   -193.258 15.286  1.00 101.42 ? 75  LEU   W CA  1 
ATOM   39960 C  C   . LEU   W  9  76  ? 3.920   -194.213 16.488  1.00 103.66 ? 75  LEU   W C   1 
ATOM   39961 O  O   . LEU   W  9  76  ? 3.495   -195.371 16.290  1.00 106.54 ? 75  LEU   W O   1 
ATOM   39962 C  CB  . LEU   W  9  76  ? 5.405   -193.171 14.714  1.00 98.49  ? 75  LEU   W CB  1 
ATOM   39963 C  CG  . LEU   W  9  76  ? 5.499   -192.719 13.256  1.00 98.06  ? 75  LEU   W CG  1 
ATOM   39964 C  CD1 . LEU   W  9  76  ? 6.859   -192.105 12.957  1.00 94.25  ? 75  LEU   W CD1 1 
ATOM   39965 C  CD2 . LEU   W  9  76  ? 5.220   -193.879 12.313  1.00 100.19 ? 75  LEU   W CD2 1 
ATOM   39966 N  N   . LYS   W  9  77  ? 4.307   -193.738 17.679  1.00 102.75 ? 76  LYS   W N   1 
ATOM   39967 C  CA  . LYS   W  9  77  ? 4.430   -194.551 18.922  1.00 101.80 ? 76  LYS   W CA  1 
ATOM   39968 C  C   . LYS   W  9  77  ? 3.086   -194.609 19.662  1.00 102.77 ? 76  LYS   W C   1 
ATOM   39969 O  O   . LYS   W  9  77  ? 2.749   -195.689 20.186  1.00 103.73 ? 76  LYS   W O   1 
ATOM   39970 C  CB  . LYS   W  9  77  ? 5.522   -193.973 19.828  1.00 103.22 ? 76  LYS   W CB  1 
ATOM   39971 C  CG  . LYS   W  9  77  ? 6.921   -193.978 19.225  1.00 104.99 ? 76  LYS   W CG  1 
ATOM   39972 C  CD  . LYS   W  9  77  ? 7.901   -193.080 19.947  1.00 106.71 ? 76  LYS   W CD  1 
ATOM   39973 C  CE  . LYS   W  9  77  ? 8.579   -193.758 21.117  1.00 105.94 ? 76  LYS   W CE  1 
ATOM   39974 N  NZ  . LYS   W  9  77  ? 9.579   -192.866 21.746  1.00 108.34 ? 76  LYS   W NZ  1 
ATOM   39975 N  N   . GLU   W  9  78  ? 2.356   -193.492 19.714  1.00 100.72 ? 77  GLU   W N   1 
ATOM   39976 C  CA  . GLU   W  9  78  ? 1.067   -193.363 20.449  1.00 104.97 ? 77  GLU   W CA  1 
ATOM   39977 C  C   . GLU   W  9  78  ? -0.104  -193.832 19.577  1.00 104.47 ? 77  GLU   W C   1 
ATOM   39978 O  O   . GLU   W  9  78  ? -1.166  -194.124 20.156  1.00 106.28 ? 77  GLU   W O   1 
ATOM   39979 C  CB  . GLU   W  9  78  ? 0.827   -191.912 20.870  1.00 105.43 ? 77  GLU   W CB  1 
ATOM   39980 C  CG  . GLU   W  9  78  ? 1.835   -191.385 21.880  1.00 105.72 ? 77  GLU   W CG  1 
ATOM   39981 C  CD  . GLU   W  9  78  ? 1.437   -191.495 23.343  1.00 107.58 ? 77  GLU   W CD  1 
ATOM   39982 O  OE1 . GLU   W  9  78  ? 0.320   -191.978 23.628  1.00 111.10 ? 77  GLU   W OE1 1 
ATOM   39983 O  OE2 . GLU   W  9  78  ? 2.250   -191.089 24.197  1.00 104.70 ? 77  GLU   W OE2 1 
ATOM   39984 N  N   . GLU   W  9  79  ? 0.072   -193.868 18.249  1.00 107.87 ? 78  GLU   W N   1 
ATOM   39985 C  CA  . GLU   W  9  79  ? -0.970  -194.234 17.245  1.00 113.04 ? 78  GLU   W CA  1 
ATOM   39986 C  C   . GLU   W  9  79  ? -2.184  -193.306 17.392  1.00 110.03 ? 78  GLU   W C   1 
ATOM   39987 O  O   . GLU   W  9  79  ? -3.322  -193.785 17.230  1.00 110.39 ? 78  GLU   W O   1 
ATOM   39988 C  CB  . GLU   W  9  79  ? -1.361  -195.710 17.377  1.00 116.39 ? 78  GLU   W CB  1 
ATOM   39989 C  CG  . GLU   W  9  79  ? -0.378  -196.660 16.718  1.00 122.09 ? 78  GLU   W CG  1 
ATOM   39990 C  CD  . GLU   W  9  79  ? -0.708  -198.134 16.887  1.00 128.09 ? 78  GLU   W CD  1 
ATOM   39991 O  OE1 . GLU   W  9  79  ? -1.071  -198.535 18.012  1.00 135.30 ? 78  GLU   W OE1 1 
ATOM   39992 O  OE2 . GLU   W  9  79  ? -0.606  -198.880 15.893  1.00 135.72 ? 78  GLU   W OE2 1 
ATOM   39993 N  N   . ARG   W  9  80  ? -1.949  -192.023 17.682  1.00 108.77 ? 79  ARG   W N   1 
ATOM   39994 C  CA  . ARG   W  9  80  ? -3.006  -190.978 17.750  1.00 109.33 ? 79  ARG   W CA  1 
ATOM   39995 C  C   . ARG   W  9  80  ? -2.363  -189.592 17.639  1.00 106.22 ? 79  ARG   W C   1 
ATOM   39996 O  O   . ARG   W  9  80  ? -1.162  -189.460 17.956  1.00 106.71 ? 79  ARG   W O   1 
ATOM   39997 C  CB  . ARG   W  9  80  ? -3.831  -191.107 19.037  1.00 110.10 ? 79  ARG   W CB  1 
ATOM   39998 C  CG  . ARG   W  9  80  ? -3.081  -190.770 20.317  1.00 108.82 ? 79  ARG   W CG  1 
ATOM   39999 C  CD  . ARG   W  9  80  ? -3.938  -191.062 21.534  1.00 111.18 ? 79  ARG   W CD  1 
ATOM   40000 N  NE  . ARG   W  9  80  ? -3.234  -190.824 22.787  1.00 112.33 ? 79  ARG   W NE  1 
ATOM   40001 C  CZ  . ARG   W  9  80  ? -3.138  -189.649 23.410  1.00 111.79 ? 79  ARG   W CZ  1 
ATOM   40002 N  NH1 . ARG   W  9  80  ? -3.699  -188.562 22.905  1.00 112.10 ? 79  ARG   W NH1 1 
ATOM   40003 N  NH2 . ARG   W  9  80  ? -2.469  -189.567 24.548  1.00 111.37 ? 79  ARG   W NH2 1 
ATOM   40004 N  N   . ALA   W  9  81  ? -3.143  -188.601 17.202  1.00 105.89 ? 80  ALA   W N   1 
ATOM   40005 C  CA  . ALA   W  9  81  ? -2.730  -187.183 17.106  1.00 102.75 ? 80  ALA   W CA  1 
ATOM   40006 C  C   . ALA   W  9  81  ? -2.577  -186.616 18.520  1.00 96.93  ? 80  ALA   W C   1 
ATOM   40007 O  O   . ALA   W  9  81  ? -3.408  -186.947 19.385  1.00 95.05  ? 80  ALA   W O   1 
ATOM   40008 C  CB  . ALA   W  9  81  ? -3.737  -186.399 16.300  1.00 105.98 ? 80  ALA   W CB  1 
ATOM   40009 N  N   . ILE   W  9  82  ? -1.542  -185.807 18.742  1.00 95.73  ? 81  ILE   W N   1 
ATOM   40010 C  CA  . ILE   W  9  82  ? -1.287  -185.119 20.042  1.00 95.87  ? 81  ILE   W CA  1 
ATOM   40011 C  C   . ILE   W  9  82  ? -2.407  -184.098 20.287  1.00 97.54  ? 81  ILE   W C   1 
ATOM   40012 O  O   . ILE   W  9  82  ? -2.877  -183.487 19.303  1.00 92.20  ? 81  ILE   W O   1 
ATOM   40013 C  CB  . ILE   W  9  82  ? 0.112   -184.471 20.059  1.00 94.66  ? 81  ILE   W CB  1 
ATOM   40014 C  CG1 . ILE   W  9  82  ? 0.529   -184.091 21.481  1.00 95.26  ? 81  ILE   W CG1 1 
ATOM   40015 C  CG2 . ILE   W  9  82  ? 0.188   -183.281 19.112  1.00 93.13  ? 81  ILE   W CG2 1 
ATOM   40016 C  CD1 . ILE   W  9  82  ? 2.016   -183.896 21.651  1.00 95.64  ? 81  ILE   W CD1 1 
ATOM   40017 N  N   . GLU   W  9  83  ? -2.822  -183.938 21.550  1.00 99.42  ? 82  GLU   W N   1 
ATOM   40018 C  CA  . GLU   W  9  83  ? -3.868  -182.970 21.982  1.00 102.73 ? 82  GLU   W CA  1 
ATOM   40019 C  C   . GLU   W  9  83  ? -3.197  -181.671 22.428  1.00 100.17 ? 82  GLU   W C   1 
ATOM   40020 O  O   . GLU   W  9  83  ? -2.026  -181.677 22.808  1.00 97.42  ? 82  GLU   W O   1 
ATOM   40021 C  CB  . GLU   W  9  83  ? -4.727  -183.554 23.109  1.00 104.60 ? 82  GLU   W CB  1 
ATOM   40022 C  CG  . GLU   W  9  83  ? -5.508  -184.798 22.720  1.00 108.08 ? 82  GLU   W CG  1 
ATOM   40023 C  CD  . GLU   W  9  83  ? -6.543  -184.610 21.621  1.00 111.21 ? 82  GLU   W CD  1 
ATOM   40024 O  OE1 . GLU   W  9  83  ? -6.933  -183.455 21.361  1.00 107.73 ? 82  GLU   W OE1 1 
ATOM   40025 O  OE2 . GLU   W  9  83  ? -6.962  -185.627 21.028  1.00 117.81 ? 82  GLU   W OE2 1 
ATOM   40026 N  N   . PRO   W  9  84  ? -3.912  -180.520 22.388  1.00 100.78 ? 83  PRO   W N   1 
ATOM   40027 C  CA  . PRO   W  9  84  ? -3.325  -179.225 22.740  1.00 99.28  ? 83  PRO   W CA  1 
ATOM   40028 C  C   . PRO   W  9  84  ? -2.659  -179.183 24.125  1.00 97.58  ? 83  PRO   W C   1 
ATOM   40029 O  O   . PRO   W  9  84  ? -1.592  -178.606 24.230  1.00 97.71  ? 83  PRO   W O   1 
ATOM   40030 C  CB  . PRO   W  9  84  ? -4.526  -178.267 22.703  1.00 101.28 ? 83  PRO   W CB  1 
ATOM   40031 C  CG  . PRO   W  9  84  ? -5.479  -178.910 21.722  1.00 102.59 ? 83  PRO   W CG  1 
ATOM   40032 C  CD  . PRO   W  9  84  ? -5.317  -180.396 21.962  1.00 103.14 ? 83  PRO   W CD  1 
ATOM   40033 N  N   . GLU   W  9  85  ? -3.291  -179.795 25.133  1.00 100.30 ? 84  GLU   W N   1 
ATOM   40034 C  CA  . GLU   W  9  85  ? -2.814  -179.801 26.545  1.00 99.86  ? 84  GLU   W CA  1 
ATOM   40035 C  C   . GLU   W  9  85  ? -1.467  -180.527 26.623  1.00 97.95  ? 84  GLU   W C   1 
ATOM   40036 O  O   . GLU   W  9  85  ? -0.558  -180.003 27.300  1.00 95.61  ? 84  GLU   W O   1 
ATOM   40037 C  CB  . GLU   W  9  85  ? -3.829  -180.467 27.478  1.00 101.69 ? 84  GLU   W CB  1 
ATOM   40038 C  CG  . GLU   W  9  85  ? -5.104  -179.664 27.676  1.00 104.85 ? 84  GLU   W CG  1 
ATOM   40039 C  CD  . GLU   W  9  85  ? -6.227  -179.955 26.694  1.00 106.79 ? 84  GLU   W CD  1 
ATOM   40040 O  OE1 . GLU   W  9  85  ? -5.933  -180.407 25.565  1.00 106.69 ? 84  GLU   W OE1 1 
ATOM   40041 O  OE2 . GLU   W  9  85  ? -7.400  -179.734 27.062  1.00 108.59 ? 84  GLU   W OE2 1 
ATOM   40042 N  N   . THR   W  9  86  ? -1.351  -181.683 25.961  1.00 98.15  ? 85  THR   W N   1 
ATOM   40043 C  CA  . THR   W  9  86  ? -0.107  -182.496 25.902  1.00 98.12  ? 85  THR   W CA  1 
ATOM   40044 C  C   . THR   W  9  86  ? 0.961   -181.707 25.136  1.00 94.76  ? 85  THR   W C   1 
ATOM   40045 O  O   . THR   W  9  86  ? 2.092   -181.607 25.650  1.00 95.47  ? 85  THR   W O   1 
ATOM   40046 C  CB  . THR   W  9  86  ? -0.352  -183.878 25.282  1.00 97.88  ? 85  THR   W CB  1 
ATOM   40047 O  OG1 . THR   W  9  86  ? -1.377  -184.523 26.039  1.00 99.43  ? 85  THR   W OG1 1 
ATOM   40048 C  CG2 . THR   W  9  86  ? 0.888   -184.746 25.263  1.00 98.29  ? 85  THR   W CG2 1 
ATOM   40049 N  N   . PHE   W  9  87  ? 0.617   -181.165 23.963  1.00 92.97  ? 86  PHE   W N   1 
ATOM   40050 C  CA  . PHE   W  9  87  ? 1.564   -180.427 23.087  1.00 92.48  ? 86  PHE   W CA  1 
ATOM   40051 C  C   . PHE   W  9  87  ? 2.141   -179.238 23.860  1.00 93.64  ? 86  PHE   W C   1 
ATOM   40052 O  O   . PHE   W  9  87  ? 3.364   -179.020 23.775  1.00 98.33  ? 86  PHE   W O   1 
ATOM   40053 C  CB  . PHE   W  9  87  ? 0.912   -179.949 21.789  1.00 91.08  ? 86  PHE   W CB  1 
ATOM   40054 C  CG  . PHE   W  9  87  ? 1.888   -179.278 20.857  1.00 89.38  ? 86  PHE   W CG  1 
ATOM   40055 C  CD1 . PHE   W  9  87  ? 2.859   -180.019 20.201  1.00 88.72  ? 86  PHE   W CD1 1 
ATOM   40056 C  CD2 . PHE   W  9  87  ? 1.869   -177.905 20.668  1.00 89.22  ? 86  PHE   W CD2 1 
ATOM   40057 C  CE1 . PHE   W  9  87  ? 3.771   -179.406 19.356  1.00 87.63  ? 86  PHE   W CE1 1 
ATOM   40058 C  CE2 . PHE   W  9  87  ? 2.782   -177.293 19.822  1.00 89.39  ? 86  PHE   W CE2 1 
ATOM   40059 C  CZ  . PHE   W  9  87  ? 3.730   -178.045 19.166  1.00 88.19  ? 86  PHE   W CZ  1 
ATOM   40060 N  N   . THR   W  9  88  ? 1.284   -178.507 24.584  1.00 93.81  ? 87  THR   W N   1 
ATOM   40061 C  CA  . THR   W  9  88  ? 1.662   -177.352 25.445  1.00 91.48  ? 87  THR   W CA  1 
ATOM   40062 C  C   . THR   W  9  88  ? 2.778   -177.775 26.407  1.00 91.45  ? 87  THR   W C   1 
ATOM   40063 O  O   . THR   W  9  88  ? 3.753   -177.010 26.555  1.00 88.60  ? 87  THR   W O   1 
ATOM   40064 C  CB  . THR   W  9  88  ? 0.460   -176.806 26.226  1.00 89.44  ? 87  THR   W CB  1 
ATOM   40065 O  OG1 . THR   W  9  88  ? -0.430  -176.185 25.299  1.00 87.76  ? 87  THR   W OG1 1 
ATOM   40066 C  CG2 . THR   W  9  88  ? 0.853   -175.807 27.291  1.00 87.63  ? 87  THR   W CG2 1 
ATOM   40067 N  N   . GLN   W  9  89  ? 2.625   -178.944 27.035  1.00 92.79  ? 88  GLN   W N   1 
ATOM   40068 C  CA  . GLN   W  9  89  ? 3.612   -179.515 27.987  1.00 91.97  ? 88  GLN   W CA  1 
ATOM   40069 C  C   . GLN   W  9  89  ? 4.924   -179.814 27.251  1.00 88.69  ? 88  GLN   W C   1 
ATOM   40070 O  O   . GLN   W  9  89  ? 5.987   -179.534 27.833  1.00 88.11  ? 88  GLN   W O   1 
ATOM   40071 C  CB  . GLN   W  9  89  ? 3.045   -180.764 28.664  1.00 93.94  ? 88  GLN   W CB  1 
ATOM   40072 C  CG  . GLN   W  9  89  ? 2.039   -180.456 29.765  1.00 96.47  ? 88  GLN   W CG  1 
ATOM   40073 C  CD  . GLN   W  9  89  ? 2.609   -179.573 30.848  1.00 94.24  ? 88  GLN   W CD  1 
ATOM   40074 O  OE1 . GLN   W  9  89  ? 2.007   -178.573 31.231  1.00 94.32  ? 88  GLN   W OE1 1 
ATOM   40075 N  NE2 . GLN   W  9  89  ? 3.780   -179.931 31.351  1.00 96.72  ? 88  GLN   W NE2 1 
ATOM   40076 N  N   . LEU   W  9  90  ? 4.854   -180.353 26.027  1.00 88.90  ? 89  LEU   W N   1 
ATOM   40077 C  CA  . LEU   W  9  90  ? 6.047   -180.690 25.198  1.00 89.51  ? 89  LEU   W CA  1 
ATOM   40078 C  C   . LEU   W  9  90  ? 6.815   -179.404 24.869  1.00 87.19  ? 89  LEU   W C   1 
ATOM   40079 O  O   . LEU   W  9  90  ? 8.059   -179.427 24.947  1.00 83.31  ? 89  LEU   W O   1 
ATOM   40080 C  CB  . LEU   W  9  90  ? 5.616   -181.423 23.920  1.00 91.93  ? 89  LEU   W CB  1 
ATOM   40081 C  CG  . LEU   W  9  90  ? 6.741   -181.768 22.939  1.00 91.71  ? 89  LEU   W CG  1 
ATOM   40082 C  CD1 . LEU   W  9  90  ? 7.695   -182.794 23.532  1.00 91.20  ? 89  LEU   W CD1 1 
ATOM   40083 C  CD2 . LEU   W  9  90  ? 6.179   -182.273 21.619  1.00 92.34  ? 89  LEU   W CD2 1 
ATOM   40084 N  N   . VAL   W  9  91  ? 6.102   -178.331 24.514  1.00 87.12  ? 90  VAL   W N   1 
ATOM   40085 C  CA  . VAL   W  9  91  ? 6.703   -177.006 24.173  1.00 85.65  ? 90  VAL   W CA  1 
ATOM   40086 C  C   . VAL   W  9  91  ? 7.450   -176.485 25.406  1.00 84.17  ? 90  VAL   W C   1 
ATOM   40087 O  O   . VAL   W  9  91  ? 8.611   -176.056 25.254  1.00 83.22  ? 90  VAL   W O   1 
ATOM   40088 C  CB  . VAL   W  9  91  ? 5.646   -175.999 23.671  1.00 85.58  ? 90  VAL   W CB  1 
ATOM   40089 C  CG1 . VAL   W  9  91  ? 6.203   -174.586 23.589  1.00 83.84  ? 90  VAL   W CG1 1 
ATOM   40090 C  CG2 . VAL   W  9  91  ? 5.068   -176.413 22.326  1.00 86.15  ? 90  VAL   W CG2 1 
ATOM   40091 N  N   . SER   W  9  92  ? 6.808   -176.538 26.577  1.00 83.83  ? 91  SER   W N   1 
ATOM   40092 C  CA  . SER   W  9  92  ? 7.372   -176.077 27.872  1.00 83.28  ? 91  SER   W CA  1 
ATOM   40093 C  C   . SER   W  9  92  ? 8.678   -176.823 28.165  1.00 84.85  ? 91  SER   W C   1 
ATOM   40094 O  O   . SER   W  9  92  ? 9.694   -176.143 28.406  1.00 85.24  ? 91  SER   W O   1 
ATOM   40095 C  CB  . SER   W  9  92  ? 6.384   -176.242 28.993  1.00 82.87  ? 91  SER   W CB  1 
ATOM   40096 O  OG  . SER   W  9  92  ? 6.840   -175.579 30.163  1.00 78.95  ? 91  SER   W OG  1 
ATOM   40097 N  N   . SER   W  9  93  ? 8.641   -178.161 28.135  1.00 86.72  ? 92  SER   W N   1 
ATOM   40098 C  CA  . SER   W  9  93  ? 9.801   -179.067 28.356  1.00 87.65  ? 92  SER   W CA  1 
ATOM   40099 C  C   . SER   W  9  93  ? 10.950  -178.664 27.427  1.00 86.21  ? 92  SER   W C   1 
ATOM   40100 O  O   . SER   W  9  93  ? 12.075  -178.462 27.926  1.00 85.26  ? 92  SER   W O   1 
ATOM   40101 C  CB  . SER   W  9  93  ? 9.428   -180.512 28.127  1.00 87.69  ? 92  SER   W CB  1 
ATOM   40102 O  OG  . SER   W  9  93  ? 8.183   -180.814 28.732  1.00 90.47  ? 92  SER   W OG  1 
ATOM   40103 N  N   . SER   W  9  94  ? 10.652  -178.556 26.128  1.00 87.46  ? 93  SER   W N   1 
ATOM   40104 C  CA  . SER   W  9  94  ? 11.629  -178.342 25.030  1.00 86.41  ? 93  SER   W CA  1 
ATOM   40105 C  C   . SER   W  9  94  ? 12.355  -177.005 25.212  1.00 87.80  ? 93  SER   W C   1 
ATOM   40106 O  O   . SER   W  9  94  ? 13.575  -176.964 24.953  1.00 85.34  ? 93  SER   W O   1 
ATOM   40107 C  CB  . SER   W  9  94  ? 10.953  -178.412 23.688  1.00 85.97  ? 93  SER   W CB  1 
ATOM   40108 O  OG  . SER   W  9  94  ? 10.303  -179.660 23.507  1.00 87.26  ? 93  SER   W OG  1 
ATOM   40109 N  N   . LEU   W  9  95  ? 11.629  -175.961 25.632  1.00 90.01  ? 94  LEU   W N   1 
ATOM   40110 C  CA  . LEU   W  9  95  ? 12.176  -174.590 25.825  1.00 90.27  ? 94  LEU   W CA  1 
ATOM   40111 C  C   . LEU   W  9  95  ? 13.068  -174.555 27.072  1.00 86.58  ? 94  LEU   W C   1 
ATOM   40112 O  O   . LEU   W  9  95  ? 14.179  -173.992 26.976  1.00 93.35  ? 94  LEU   W O   1 
ATOM   40113 C  CB  . LEU   W  9  95  ? 11.030  -173.576 25.937  1.00 94.14  ? 94  LEU   W CB  1 
ATOM   40114 C  CG  . LEU   W  9  95  ? 10.273  -173.274 24.642  1.00 94.91  ? 94  LEU   W CG  1 
ATOM   40115 C  CD1 . LEU   W  9  95  ? 9.079   -172.372 24.914  1.00 95.11  ? 94  LEU   W CD1 1 
ATOM   40116 C  CD2 . LEU   W  9  95  ? 11.184  -172.642 23.597  1.00 95.34  ? 94  LEU   W CD2 1 
ATOM   40117 N  N   . TYR   W  9  96  ? 12.614  -175.132 28.190  1.00 82.21  ? 95  TYR   W N   1 
ATOM   40118 C  CA  . TYR   W  9  96  ? 13.347  -175.118 29.484  1.00 81.08  ? 95  TYR   W CA  1 
ATOM   40119 C  C   . TYR   W  9  96  ? 14.621  -175.964 29.379  1.00 82.25  ? 95  TYR   W C   1 
ATOM   40120 O  O   . TYR   W  9  96  ? 15.558  -175.726 30.157  1.00 81.17  ? 95  TYR   W O   1 
ATOM   40121 C  CB  . TYR   W  9  96  ? 12.475  -175.590 30.650  1.00 80.06  ? 95  TYR   W CB  1 
ATOM   40122 C  CG  . TYR   W  9  96  ? 13.042  -175.190 31.988  1.00 79.37  ? 95  TYR   W CG  1 
ATOM   40123 C  CD1 . TYR   W  9  96  ? 12.787  -173.937 32.523  1.00 79.56  ? 95  TYR   W CD1 1 
ATOM   40124 C  CD2 . TYR   W  9  96  ? 13.890  -176.032 32.690  1.00 77.62  ? 95  TYR   W CD2 1 
ATOM   40125 C  CE1 . TYR   W  9  96  ? 13.328  -173.544 33.735  1.00 80.08  ? 95  TYR   W CE1 1 
ATOM   40126 C  CE2 . TYR   W  9  96  ? 14.438  -175.658 33.905  1.00 78.31  ? 95  TYR   W CE2 1 
ATOM   40127 C  CZ  . TYR   W  9  96  ? 14.156  -174.409 34.428  1.00 79.89  ? 95  TYR   W CZ  1 
ATOM   40128 O  OH  . TYR   W  9  96  ? 14.688  -174.028 35.624  1.00 81.98  ? 95  TYR   W OH  1 
ATOM   40129 N  N   . GLU   W  9  97  ? 14.655  -176.919 28.446  1.00 84.49  ? 96  GLU   W N   1 
ATOM   40130 C  CA  . GLU   W  9  97  ? 15.853  -177.748 28.141  1.00 90.52  ? 96  GLU   W CA  1 
ATOM   40131 C  C   . GLU   W  9  97  ? 17.020  -176.841 27.730  1.00 90.51  ? 96  GLU   W C   1 
ATOM   40132 O  O   . GLU   W  9  97  ? 18.176  -177.256 27.931  1.00 90.79  ? 96  GLU   W O   1 
ATOM   40133 C  CB  . GLU   W  9  97  ? 15.533  -178.755 27.035  1.00 95.84  ? 96  GLU   W CB  1 
ATOM   40134 C  CG  . GLU   W  9  97  ? 16.644  -179.756 26.780  1.00 101.54 ? 96  GLU   W CG  1 
ATOM   40135 C  CD  . GLU   W  9  97  ? 16.224  -180.949 25.940  1.00 105.28 ? 96  GLU   W CD  1 
ATOM   40136 O  OE1 . GLU   W  9  97  ? 16.759  -182.049 26.176  1.00 111.11 ? 96  GLU   W OE1 1 
ATOM   40137 O  OE2 . GLU   W  9  97  ? 15.362  -180.777 25.052  1.00 109.67 ? 96  GLU   W OE2 1 
ATOM   40138 N  N   . ARG   W  9  98  ? 16.722  -175.664 27.165  1.00 93.44  ? 97  ARG   W N   1 
ATOM   40139 C  CA  . ARG   W  9  98  ? 17.713  -174.623 26.781  1.00 95.70  ? 97  ARG   W CA  1 
ATOM   40140 C  C   . ARG   W  9  98  ? 17.615  -173.444 27.760  1.00 93.05  ? 97  ARG   W C   1 
ATOM   40141 O  O   . ARG   W  9  98  ? 17.569  -172.291 27.296  1.00 91.31  ? 97  ARG   W O   1 
ATOM   40142 C  CB  . ARG   W  9  98  ? 17.462  -174.187 25.332  1.00 101.91 ? 97  ARG   W CB  1 
ATOM   40143 C  CG  . ARG   W  9  98  ? 17.849  -175.226 24.290  1.00 109.46 ? 97  ARG   W CG  1 
ATOM   40144 C  CD  . ARG   W  9  98  ? 19.321  -175.145 23.932  1.00 115.37 ? 97  ARG   W CD  1 
ATOM   40145 N  NE  . ARG   W  9  98  ? 19.790  -176.344 23.246  1.00 124.12 ? 97  ARG   W NE  1 
ATOM   40146 C  CZ  . ARG   W  9  98  ? 20.285  -177.433 23.838  1.00 129.12 ? 97  ARG   W CZ  1 
ATOM   40147 N  NH1 . ARG   W  9  98  ? 20.390  -177.506 25.157  1.00 133.49 ? 97  ARG   W NH1 1 
ATOM   40148 N  NH2 . ARG   W  9  98  ? 20.679  -178.457 23.099  1.00 130.34 ? 97  ARG   W NH2 1 
ATOM   40149 N  N   . ARG   W  9  99  ? 17.577  -173.691 29.071  1.00 91.30  ? 98  ARG   W N   1 
ATOM   40150 C  CA  . ARG   W  9  99  ? 17.338  -172.607 30.072  1.00 89.50  ? 98  ARG   W CA  1 
ATOM   40151 C  C   . ARG   W  9  99  ? 18.462  -171.576 30.162  1.00 86.89  ? 98  ARG   W C   1 
ATOM   40152 O  O   . ARG   W  9  99  ? 18.172  -170.455 30.553  1.00 82.37  ? 98  ARG   W O   1 
ATOM   40153 C  CB  . ARG   W  9  99  ? 17.140  -173.164 31.479  1.00 92.10  ? 98  ARG   W CB  1 
ATOM   40154 C  CG  . ARG   W  9  99  ? 17.388  -172.126 32.561  1.00 93.49  ? 98  ARG   W CG  1 
ATOM   40155 C  CD  . ARG   W  9  99  ? 16.136  -171.313 32.781  1.00 93.78  ? 98  ARG   W CD  1 
ATOM   40156 N  NE  . ARG   W  9  99  ? 16.156  -170.446 33.947  1.00 97.12  ? 98  ARG   W NE  1 
ATOM   40157 C  CZ  . ARG   W  9  99  ? 16.825  -169.309 34.023  1.00 94.53  ? 98  ARG   W CZ  1 
ATOM   40158 N  NH1 . ARG   W  9  99  ? 16.771  -168.586 35.123  1.00 94.22  ? 98  ARG   W NH1 1 
ATOM   40159 N  NH2 . ARG   W  9  99  ? 17.553  -168.899 33.004  1.00 96.71  ? 98  ARG   W NH2 1 
ATOM   40160 N  N   . PHE   W  9  100 ? 19.704  -171.968 29.929  1.00 87.16  ? 99  PHE   W N   1 
ATOM   40161 C  CA  . PHE   W  9  100 ? 20.836  -171.004 29.990  1.00 89.30  ? 99  PHE   W CA  1 
ATOM   40162 C  C   . PHE   W  9  100 ? 21.455  -170.822 28.598  1.00 91.10  ? 99  PHE   W C   1 
ATOM   40163 O  O   . PHE   W  9  100 ? 22.669  -170.552 28.504  1.00 97.73  ? 99  PHE   W O   1 
ATOM   40164 C  CB  . PHE   W  9  100 ? 21.846  -171.451 31.048  1.00 89.94  ? 99  PHE   W CB  1 
ATOM   40165 C  CG  . PHE   W  9  100 ? 21.260  -171.573 32.432  1.00 90.76  ? 99  PHE   W CG  1 
ATOM   40166 C  CD1 . PHE   W  9  100 ? 20.842  -170.448 33.128  1.00 92.81  ? 99  PHE   W CD1 1 
ATOM   40167 C  CD2 . PHE   W  9  100 ? 21.108  -172.811 33.033  1.00 89.62  ? 99  PHE   W CD2 1 
ATOM   40168 C  CE1 . PHE   W  9  100 ? 20.293  -170.559 34.397  1.00 91.46  ? 99  PHE   W CE1 1 
ATOM   40169 C  CE2 . PHE   W  9  100 ? 20.562  -172.919 34.303  1.00 89.76  ? 99  PHE   W CE2 1 
ATOM   40170 C  CZ  . PHE   W  9  100 ? 20.154  -171.795 34.982  1.00 90.35  ? 99  PHE   W CZ  1 
ATOM   40171 N  N   . GLY   W  9  101 ? 20.633  -170.945 27.552  1.00 89.21  ? 100 GLY   W N   1 
ATOM   40172 C  CA  . GLY   W  9  101 ? 20.992  -170.639 26.153  1.00 87.78  ? 100 GLY   W CA  1 
ATOM   40173 C  C   . GLY   W  9  101 ? 19.751  -170.686 25.269  1.00 85.75  ? 100 GLY   W C   1 
ATOM   40174 O  O   . GLY   W  9  101 ? 19.701  -171.432 24.296  1.00 85.68  ? 100 GLY   W O   1 
ATOM   40175 N  N   . PRO   W  9  102 ? 18.715  -169.884 25.596  1.00 84.70  ? 101 PRO   W N   1 
ATOM   40176 C  CA  . PRO   W  9  102 ? 17.363  -170.134 25.103  1.00 85.44  ? 101 PRO   W CA  1 
ATOM   40177 C  C   . PRO   W  9  102 ? 17.112  -169.728 23.648  1.00 86.30  ? 101 PRO   W C   1 
ATOM   40178 O  O   . PRO   W  9  102 ? 17.865  -168.935 23.107  1.00 86.44  ? 101 PRO   W O   1 
ATOM   40179 C  CB  . PRO   W  9  102 ? 16.496  -169.261 26.020  1.00 83.84  ? 101 PRO   W CB  1 
ATOM   40180 C  CG  . PRO   W  9  102 ? 17.396  -168.105 26.393  1.00 83.92  ? 101 PRO   W CG  1 
ATOM   40181 C  CD  . PRO   W  9  102 ? 18.795  -168.685 26.443  1.00 83.88  ? 101 PRO   W CD  1 
ATOM   40182 N  N   . TYR   W  9  103 ? 16.055  -170.300 23.067  1.00 88.68  ? 102 TYR   W N   1 
ATOM   40183 C  CA  . TYR   W  9  103 ? 15.417  -169.828 21.814  1.00 89.99  ? 102 TYR   W CA  1 
ATOM   40184 C  C   . TYR   W  9  103 ? 14.709  -168.509 22.142  1.00 88.09  ? 102 TYR   W C   1 
ATOM   40185 O  O   . TYR   W  9  103 ? 13.968  -168.461 23.146  1.00 82.02  ? 102 TYR   W O   1 
ATOM   40186 C  CB  . TYR   W  9  103 ? 14.459  -170.886 21.253  1.00 90.26  ? 102 TYR   W CB  1 
ATOM   40187 C  CG  . TYR   W  9  103 ? 15.093  -172.212 20.906  1.00 92.28  ? 102 TYR   W CG  1 
ATOM   40188 C  CD1 . TYR   W  9  103 ? 15.943  -172.336 19.818  1.00 94.07  ? 102 TYR   W CD1 1 
ATOM   40189 C  CD2 . TYR   W  9  103 ? 14.835  -173.349 21.657  1.00 91.39  ? 102 TYR   W CD2 1 
ATOM   40190 C  CE1 . TYR   W  9  103 ? 16.528  -173.548 19.491  1.00 94.95  ? 102 TYR   W CE1 1 
ATOM   40191 C  CE2 . TYR   W  9  103 ? 15.410  -174.569 21.343  1.00 93.59  ? 102 TYR   W CE2 1 
ATOM   40192 C  CZ  . TYR   W  9  103 ? 16.260  -174.668 20.255  1.00 96.04  ? 102 TYR   W CZ  1 
ATOM   40193 O  OH  . TYR   W  9  103 ? 16.834  -175.861 19.927  1.00 102.88 ? 102 TYR   W OH  1 
ATOM   40194 N  N   . PHE   W  9  104 ? 14.964  -167.464 21.350  1.00 89.76  ? 103 PHE   W N   1 
ATOM   40195 C  CA  . PHE   W  9  104 ? 14.419  -166.096 21.551  1.00 86.76  ? 103 PHE   W CA  1 
ATOM   40196 C  C   . PHE   W  9  104 ? 13.063  -166.008 20.848  1.00 87.04  ? 103 PHE   W C   1 
ATOM   40197 O  O   . PHE   W  9  104 ? 12.968  -165.390 19.766  1.00 87.71  ? 103 PHE   W O   1 
ATOM   40198 C  CB  . PHE   W  9  104 ? 15.425  -165.050 21.069  1.00 87.17  ? 103 PHE   W CB  1 
ATOM   40199 C  CG  . PHE   W  9  104 ? 16.715  -165.064 21.846  1.00 87.19  ? 103 PHE   W CG  1 
ATOM   40200 C  CD1 . PHE   W  9  104 ? 16.767  -164.549 23.133  1.00 86.71  ? 103 PHE   W CD1 1 
ATOM   40201 C  CD2 . PHE   W  9  104 ? 17.868  -165.610 21.304  1.00 87.59  ? 103 PHE   W CD2 1 
ATOM   40202 C  CE1 . PHE   W  9  104 ? 17.949  -164.570 23.857  1.00 87.07  ? 103 PHE   W CE1 1 
ATOM   40203 C  CE2 . PHE   W  9  104 ? 19.050  -165.630 22.030  1.00 88.70  ? 103 PHE   W CE2 1 
ATOM   40204 C  CZ  . PHE   W  9  104 ? 19.088  -165.111 23.304  1.00 88.43  ? 103 PHE   W CZ  1 
ATOM   40205 N  N   . VAL   W  9  105 ? 12.049  -166.622 21.465  1.00 82.51  ? 104 VAL   W N   1 
ATOM   40206 C  CA  . VAL   W  9  105 ? 10.720  -166.887 20.843  1.00 83.80  ? 104 VAL   W CA  1 
ATOM   40207 C  C   . VAL   W  9  105 ? 9.604   -166.564 21.842  1.00 82.81  ? 104 VAL   W C   1 
ATOM   40208 O  O   . VAL   W  9  105 ? 9.879   -166.531 23.057  1.00 84.56  ? 104 VAL   W O   1 
ATOM   40209 C  CB  . VAL   W  9  105 ? 10.630  -168.346 20.359  1.00 84.02  ? 104 VAL   W CB  1 
ATOM   40210 C  CG1 . VAL   W  9  105 ? 11.599  -168.613 19.219  1.00 82.73  ? 104 VAL   W CG1 1 
ATOM   40211 C  CG2 . VAL   W  9  105 ? 10.854  -169.330 21.499  1.00 83.83  ? 104 VAL   W CG2 1 
ATOM   40212 N  N   . GLY   W  9  106 ? 8.394   -166.340 21.323  1.00 86.92  ? 105 GLY   W N   1 
ATOM   40213 C  CA  . GLY   W  9  106 ? 7.155   -166.145 22.100  1.00 88.88  ? 105 GLY   W CA  1 
ATOM   40214 C  C   . GLY   W  9  106 ? 6.037   -167.028 21.557  1.00 92.12  ? 105 GLY   W C   1 
ATOM   40215 O  O   . GLY   W  9  106 ? 5.124   -166.541 20.894  1.00 97.39  ? 105 GLY   W O   1 
ATOM   40216 N  N   . PRO   W  9  107 ? 6.088   -168.356 21.801  1.00 89.11  ? 106 PRO   W N   1 
ATOM   40217 C  CA  . PRO   W  9  107 ? 5.147   -169.282 21.179  1.00 88.56  ? 106 PRO   W CA  1 
ATOM   40218 C  C   . PRO   W  9  107 ? 3.741   -169.187 21.792  1.00 87.84  ? 106 PRO   W C   1 
ATOM   40219 O  O   . PRO   W  9  107 ? 3.617   -168.776 22.930  1.00 87.40  ? 106 PRO   W O   1 
ATOM   40220 C  CB  . PRO   W  9  107 ? 5.776   -170.666 21.399  1.00 88.30  ? 106 PRO   W CB  1 
ATOM   40221 C  CG  . PRO   W  9  107 ? 6.721   -170.504 22.575  1.00 87.68  ? 106 PRO   W CG  1 
ATOM   40222 C  CD  . PRO   W  9  107 ? 7.046   -169.028 22.688  1.00 87.99  ? 106 PRO   W CD  1 
ATOM   40223 N  N   . VAL   W  9  108 ? 2.729   -169.546 20.996  1.00 89.35  ? 107 VAL   W N   1 
ATOM   40224 C  CA  . VAL   W  9  108 ? 1.284   -169.560 21.370  1.00 92.69  ? 107 VAL   W CA  1 
ATOM   40225 C  C   . VAL   W  9  108 ? 0.667   -170.854 20.829  1.00 91.25  ? 107 VAL   W C   1 
ATOM   40226 O  O   . VAL   W  9  108 ? 0.671   -171.033 19.596  1.00 97.63  ? 107 VAL   W O   1 
ATOM   40227 C  CB  . VAL   W  9  108 ? 0.545   -168.324 20.816  1.00 93.15  ? 107 VAL   W CB  1 
ATOM   40228 C  CG1 . VAL   W  9  108 ? -0.949  -168.367 21.116  1.00 93.56  ? 107 VAL   W CG1 1 
ATOM   40229 C  CG2 . VAL   W  9  108 ? 1.153   -167.024 21.321  1.00 93.45  ? 107 VAL   W CG2 1 
ATOM   40230 N  N   . VAL   W  9  109 ? 0.157   -171.714 21.714  1.00 90.36  ? 108 VAL   W N   1 
ATOM   40231 C  CA  . VAL   W  9  109 ? -0.615  -172.936 21.339  1.00 90.24  ? 108 VAL   W CA  1 
ATOM   40232 C  C   . VAL   W  9  109 ? -2.098  -172.566 21.271  1.00 88.73  ? 108 VAL   W C   1 
ATOM   40233 O  O   . VAL   W  9  109 ? -2.562  -171.812 22.146  1.00 87.54  ? 108 VAL   W O   1 
ATOM   40234 C  CB  . VAL   W  9  109 ? -0.366  -174.096 22.321  1.00 89.95  ? 108 VAL   W CB  1 
ATOM   40235 C  CG1 . VAL   W  9  109 ? -1.388  -175.214 22.158  1.00 90.28  ? 108 VAL   W CG1 1 
ATOM   40236 C  CG2 . VAL   W  9  109 ? 1.047   -174.641 22.182  1.00 89.76  ? 108 VAL   W CG2 1 
ATOM   40237 N  N   . ALA   W  9  110 ? -2.799  -173.087 20.264  1.00 89.66  ? 109 ALA   W N   1 
ATOM   40238 C  CA  . ALA   W  9  110 ? -4.255  -172.925 20.056  1.00 93.36  ? 109 ALA   W CA  1 
ATOM   40239 C  C   . ALA   W  9  110 ? -4.809  -174.189 19.394  1.00 95.48  ? 109 ALA   W C   1 
ATOM   40240 O  O   . ALA   W  9  110 ? -4.127  -174.741 18.510  1.00 97.10  ? 109 ALA   W O   1 
ATOM   40241 C  CB  . ALA   W  9  110 ? -4.520  -171.701 19.218  1.00 94.71  ? 109 ALA   W CB  1 
ATOM   40242 N  N   . GLY   W  9  111 ? -5.992  -174.636 19.817  1.00 99.06  ? 110 GLY   W N   1 
ATOM   40243 C  CA  . GLY   W  9  111 ? -6.667  -175.815 19.242  1.00 102.33 ? 110 GLY   W CA  1 
ATOM   40244 C  C   . GLY   W  9  111 ? -7.827  -176.287 20.098  1.00 105.33 ? 110 GLY   W C   1 
ATOM   40245 O  O   . GLY   W  9  111 ? -8.044  -175.707 21.183  1.00 105.22 ? 110 GLY   W O   1 
ATOM   40246 N  N   . ILE   W  9  112 ? -8.547  -177.304 19.617  1.00 107.32 ? 111 ILE   W N   1 
ATOM   40247 C  CA  . ILE   W  9  112 ? -9.718  -177.921 20.305  1.00 110.02 ? 111 ILE   W CA  1 
ATOM   40248 C  C   . ILE   W  9  112 ? -9.384  -179.384 20.601  1.00 110.52 ? 111 ILE   W C   1 
ATOM   40249 O  O   . ILE   W  9  112 ? -9.116  -180.134 19.639  1.00 109.25 ? 111 ILE   W O   1 
ATOM   40250 C  CB  . ILE   W  9  112 ? -10.997 -177.799 19.455  1.00 110.81 ? 111 ILE   W CB  1 
ATOM   40251 C  CG1 . ILE   W  9  112 ? -11.359 -176.337 19.185  1.00 111.54 ? 111 ILE   W CG1 1 
ATOM   40252 C  CG2 . ILE   W  9  112 ? -12.154 -178.545 20.103  1.00 112.15 ? 111 ILE   W CG2 1 
ATOM   40253 C  CD1 . ILE   W  9  112 ? -12.089 -176.127 17.882  1.00 113.86 ? 111 ILE   W CD1 1 
ATOM   40254 N  N   . ASN   W  9  113 ? -9.409  -179.757 21.883  1.00 113.07 ? 112 ASN   W N   1 
ATOM   40255 C  CA  . ASN   W  9  113 ? -9.274  -181.159 22.355  1.00 113.94 ? 112 ASN   W CA  1 
ATOM   40256 C  C   . ASN   W  9  113 ? -10.354 -181.998 21.664  1.00 116.00 ? 112 ASN   W C   1 
ATOM   40257 O  O   . ASN   W  9  113 ? -11.550 -181.708 21.869  1.00 115.24 ? 112 ASN   W O   1 
ATOM   40258 C  CB  . ASN   W  9  113 ? -9.369  -181.255 23.879  1.00 115.04 ? 112 ASN   W CB  1 
ATOM   40259 C  CG  . ASN   W  9  113 ? -8.978  -182.617 24.406  1.00 114.82 ? 112 ASN   W CG  1 
ATOM   40260 O  OD1 . ASN   W  9  113 ? -9.651  -183.610 24.137  1.00 115.48 ? 112 ASN   W OD1 1 
ATOM   40261 N  ND2 . ASN   W  9  113 ? -7.893  -182.677 25.160  1.00 117.25 ? 112 ASN   W ND2 1 
ATOM   40262 N  N   . SER   W  9  114 ? -9.941  -182.986 20.866  1.00 116.92 ? 113 SER   W N   1 
ATOM   40263 C  CA  . SER   W  9  114 ? -10.831 -183.813 20.011  1.00 118.43 ? 113 SER   W CA  1 
ATOM   40264 C  C   . SER   W  9  114 ? -11.716 -184.726 20.872  1.00 120.82 ? 113 SER   W C   1 
ATOM   40265 O  O   . SER   W  9  114 ? -12.812 -185.083 20.402  1.00 126.15 ? 113 SER   W O   1 
ATOM   40266 C  CB  . SER   W  9  114 ? -10.028 -184.602 19.011  1.00 116.22 ? 113 SER   W CB  1 
ATOM   40267 O  OG  . SER   W  9  114 ? -9.206  -185.556 19.666  1.00 113.25 ? 113 SER   W OG  1 
ATOM   40268 N  N   . LYS   W  9  115 ? -11.267 -185.081 22.081  1.00 120.75 ? 114 LYS   W N   1 
ATOM   40269 C  CA  . LYS   W  9  115 ? -11.998 -185.995 23.002  1.00 123.44 ? 114 LYS   W CA  1 
ATOM   40270 C  C   . LYS   W  9  115 ? -13.075 -185.210 23.766  1.00 123.03 ? 114 LYS   W C   1 
ATOM   40271 O  O   . LYS   W  9  115 ? -14.232 -185.673 23.780  1.00 124.01 ? 114 LYS   W O   1 
ATOM   40272 C  CB  . LYS   W  9  115 ? -11.033 -186.687 23.971  1.00 124.95 ? 114 LYS   W CB  1 
ATOM   40273 C  CG  . LYS   W  9  115 ? -11.466 -188.077 24.418  1.00 129.78 ? 114 LYS   W CG  1 
ATOM   40274 C  CD  . LYS   W  9  115 ? -11.152 -189.153 23.399  1.00 132.40 ? 114 LYS   W CD  1 
ATOM   40275 C  CE  . LYS   W  9  115 ? -11.834 -190.475 23.683  1.00 135.83 ? 114 LYS   W CE  1 
ATOM   40276 N  NZ  . LYS   W  9  115 ? -11.294 -191.129 24.898  1.00 135.51 ? 114 LYS   W NZ  1 
ATOM   40277 N  N   . SER   W  9  116 ? -12.709 -184.075 24.375  1.00 119.32 ? 115 SER   W N   1 
ATOM   40278 C  CA  . SER   W  9  116 ? -13.583 -183.264 25.268  1.00 118.00 ? 115 SER   W CA  1 
ATOM   40279 C  C   . SER   W  9  116 ? -14.381 -182.220 24.471  1.00 116.66 ? 115 SER   W C   1 
ATOM   40280 O  O   . SER   W  9  116 ? -15.496 -181.879 24.913  1.00 113.97 ? 115 SER   W O   1 
ATOM   40281 C  CB  . SER   W  9  116 ? -12.784 -182.616 26.375  1.00 113.17 ? 115 SER   W CB  1 
ATOM   40282 O  OG  . SER   W  9  116 ? -11.980 -181.556 25.882  1.00 108.04 ? 115 SER   W OG  1 
ATOM   40283 N  N   . GLY   W  9  117 ? -13.832 -181.727 23.355  1.00 115.48 ? 116 GLY   W N   1 
ATOM   40284 C  CA  . GLY   W  9  117 ? -14.447 -180.672 22.523  1.00 118.56 ? 116 GLY   W CA  1 
ATOM   40285 C  C   . GLY   W  9  117 ? -14.211 -179.277 23.087  1.00 117.78 ? 116 GLY   W C   1 
ATOM   40286 O  O   . GLY   W  9  117 ? -14.837 -178.324 22.577  1.00 117.80 ? 116 GLY   W O   1 
ATOM   40287 N  N   . LYS   W  9  118 ? -13.335 -179.152 24.092  1.00 121.43 ? 117 LYS   W N   1 
ATOM   40288 C  CA  . LYS   W  9  118 ? -13.039 -177.880 24.806  1.00 120.28 ? 117 LYS   W CA  1 
ATOM   40289 C  C   . LYS   W  9  118 ? -12.033 -177.061 24.002  1.00 117.20 ? 117 LYS   W C   1 
ATOM   40290 O  O   . LYS   W  9  118 ? -11.013 -177.588 23.565  1.00 114.67 ? 117 LYS   W O   1 
ATOM   40291 C  CB  . LYS   W  9  118 ? -12.486 -178.152 26.208  1.00 124.61 ? 117 LYS   W CB  1 
ATOM   40292 C  CG  . LYS   W  9  118 ? -13.533 -178.520 27.249  1.00 132.22 ? 117 LYS   W CG  1 
ATOM   40293 C  CD  . LYS   W  9  118 ? -12.954 -179.148 28.499  1.00 137.85 ? 117 LYS   W CD  1 
ATOM   40294 C  CE  . LYS   W  9  118 ? -14.019 -179.622 29.467  1.00 143.78 ? 117 LYS   W CE  1 
ATOM   40295 N  NZ  . LYS   W  9  118 ? -14.672 -178.487 30.162  1.00 148.24 ? 117 LYS   W NZ  1 
ATOM   40296 N  N   . PRO   W  9  119 ? -12.294 -175.753 23.776  1.00 114.77 ? 118 PRO   W N   1 
ATOM   40297 C  CA  . PRO   W  9  119 ? -11.293 -174.847 23.211  1.00 111.26 ? 118 PRO   W CA  1 
ATOM   40298 C  C   . PRO   W  9  119 ? -10.152 -174.587 24.204  1.00 105.96 ? 118 PRO   W C   1 
ATOM   40299 O  O   . PRO   W  9  119 ? -10.443 -174.377 25.365  1.00 106.43 ? 118 PRO   W O   1 
ATOM   40300 C  CB  . PRO   W  9  119 ? -12.065 -173.544 22.947  1.00 112.99 ? 118 PRO   W CB  1 
ATOM   40301 C  CG  . PRO   W  9  119 ? -13.528 -173.925 23.034  1.00 116.06 ? 118 PRO   W CG  1 
ATOM   40302 C  CD  . PRO   W  9  119 ? -13.580 -175.081 24.009  1.00 116.68 ? 118 PRO   W CD  1 
ATOM   40303 N  N   . PHE   W  9  120 ? -8.903  -174.594 23.726  1.00 103.85 ? 119 PHE   W N   1 
ATOM   40304 C  CA  . PHE   W  9  120 ? -7.678  -174.463 24.559  1.00 102.79 ? 119 PHE   W CA  1 
ATOM   40305 C  C   . PHE   W  9  120 ? -6.657  -173.542 23.883  1.00 99.46  ? 119 PHE   W C   1 
ATOM   40306 O  O   . PHE   W  9  120 ? -6.258  -173.824 22.736  1.00 99.87  ? 119 PHE   W O   1 
ATOM   40307 C  CB  . PHE   W  9  120 ? -7.038  -175.830 24.805  1.00 102.74 ? 119 PHE   W CB  1 
ATOM   40308 C  CG  . PHE   W  9  120 ? -5.834  -175.783 25.710  1.00 104.45 ? 119 PHE   W CG  1 
ATOM   40309 C  CD1 . PHE   W  9  120 ? -4.565  -175.557 25.197  1.00 102.53 ? 119 PHE   W CD1 1 
ATOM   40310 C  CD2 . PHE   W  9  120 ? -5.975  -175.939 27.080  1.00 107.36 ? 119 PHE   W CD2 1 
ATOM   40311 C  CE1 . PHE   W  9  120 ? -3.462  -175.502 26.035  1.00 102.38 ? 119 PHE   W CE1 1 
ATOM   40312 C  CE2 . PHE   W  9  120 ? -4.871  -175.884 27.916  1.00 107.95 ? 119 PHE   W CE2 1 
ATOM   40313 C  CZ  . PHE   W  9  120 ? -3.617  -175.667 27.393  1.00 105.30 ? 119 PHE   W CZ  1 
ATOM   40314 N  N   . ILE   W  9  121 ? -6.228  -172.496 24.597  1.00 97.23  ? 120 ILE   W N   1 
ATOM   40315 C  CA  . ILE   W  9  121 ? -5.101  -171.597 24.205  1.00 98.08  ? 120 ILE   W CA  1 
ATOM   40316 C  C   . ILE   W  9  121 ? -4.093  -171.553 25.358  1.00 93.94  ? 120 ILE   W C   1 
ATOM   40317 O  O   . ILE   W  9  121 ? -4.501  -171.768 26.518  1.00 94.10  ? 120 ILE   W O   1 
ATOM   40318 C  CB  . ILE   W  9  121 ? -5.603  -170.189 23.815  1.00 97.45  ? 120 ILE   W CB  1 
ATOM   40319 C  CG1 . ILE   W  9  121 ? -6.449  -169.545 24.918  1.00 99.27  ? 120 ILE   W CG1 1 
ATOM   40320 C  CG2 . ILE   W  9  121 ? -6.349  -170.239 22.489  1.00 97.92  ? 120 ILE   W CG2 1 
ATOM   40321 C  CD1 . ILE   W  9  121 ? -6.662  -168.058 24.745  1.00 100.63 ? 120 ILE   W CD1 1 
ATOM   40322 N  N   . ALA   W  9  122 ? -2.822  -171.297 25.040  1.00 90.83  ? 121 ALA   W N   1 
ATOM   40323 C  CA  . ALA   W  9  122 ? -1.725  -171.142 26.021  1.00 90.92  ? 121 ALA   W CA  1 
ATOM   40324 C  C   . ALA   W  9  122 ? -0.591  -170.312 25.410  1.00 91.44  ? 121 ALA   W C   1 
ATOM   40325 O  O   . ALA   W  9  122 ? -0.400  -170.376 24.178  1.00 91.57  ? 121 ALA   W O   1 
ATOM   40326 C  CB  . ALA   W  9  122 ? -1.237  -172.496 26.463  1.00 91.83  ? 121 ALA   W CB  1 
ATOM   40327 N  N   . GLY   W  9  123 ? 0.118   -169.560 26.258  1.00 91.07  ? 122 GLY   W N   1 
ATOM   40328 C  CA  . GLY   W  9  123 ? 1.306   -168.761 25.901  1.00 90.81  ? 122 GLY   W CA  1 
ATOM   40329 C  C   . GLY   W  9  123 ? 2.505   -169.153 26.747  1.00 86.80  ? 122 GLY   W C   1 
ATOM   40330 O  O   . GLY   W  9  123 ? 2.302   -169.662 27.863  1.00 84.77  ? 122 GLY   W O   1 
ATOM   40331 N  N   . PHE   W  9  124 ? 3.714   -168.926 26.233  1.00 87.92  ? 123 PHE   W N   1 
ATOM   40332 C  CA  . PHE   W  9  124 ? 4.994   -169.242 26.915  1.00 91.13  ? 123 PHE   W CA  1 
ATOM   40333 C  C   . PHE   W  9  124 ? 5.936   -168.046 26.817  1.00 93.85  ? 123 PHE   W C   1 
ATOM   40334 O  O   . PHE   W  9  124 ? 5.864   -167.321 25.806  1.00 100.48 ? 123 PHE   W O   1 
ATOM   40335 C  CB  . PHE   W  9  124 ? 5.683   -170.446 26.271  1.00 94.53  ? 123 PHE   W CB  1 
ATOM   40336 C  CG  . PHE   W  9  124 ? 4.772   -171.590 25.914  1.00 97.41  ? 123 PHE   W CG  1 
ATOM   40337 C  CD1 . PHE   W  9  124 ? 3.973   -171.532 24.782  1.00 98.95  ? 123 PHE   W CD1 1 
ATOM   40338 C  CD2 . PHE   W  9  124 ? 4.725   -172.730 26.700  1.00 98.13  ? 123 PHE   W CD2 1 
ATOM   40339 C  CE1 . PHE   W  9  124 ? 3.137   -172.585 24.451  1.00 101.17 ? 123 PHE   W CE1 1 
ATOM   40340 C  CE2 . PHE   W  9  124 ? 3.891   -173.785 26.364  1.00 100.65 ? 123 PHE   W CE2 1 
ATOM   40341 C  CZ  . PHE   W  9  124 ? 3.099   -173.711 25.241  1.00 102.75 ? 123 PHE   W CZ  1 
ATOM   40342 N  N   . ASP   W  9  125 ? 6.900   -168.035 27.736  1.00 91.55  ? 124 ASP   W N   1 
ATOM   40343 C  CA  . ASP   W  9  125 ? 8.060   -167.112 27.708  1.00 94.79  ? 124 ASP   W CA  1 
ATOM   40344 C  C   . ASP   W  9  125 ? 9.213   -167.886 27.045  1.00 92.07  ? 124 ASP   W C   1 
ATOM   40345 O  O   . ASP   W  9  125 ? 9.167   -169.109 27.021  1.00 87.38  ? 124 ASP   W O   1 
ATOM   40346 C  CB  . ASP   W  9  125 ? 8.394   -166.622 29.112  1.00 97.63  ? 124 ASP   W CB  1 
ATOM   40347 C  CG  . ASP   W  9  125 ? 8.806   -167.765 30.005  1.00 97.00  ? 124 ASP   W CG  1 
ATOM   40348 O  OD1 . ASP   W  9  125 ? 8.755   -168.888 29.526  1.00 100.16 ? 124 ASP   W OD1 1 
ATOM   40349 O  OD2 . ASP   W  9  125 ? 9.182   -167.518 31.154  1.00 99.23  ? 124 ASP   W OD2 1 
ATOM   40350 N  N   . LEU   W  9  126 ? 10.226  -167.204 26.521  1.00 96.01  ? 125 LEU   W N   1 
ATOM   40351 C  CA  . LEU   W  9  126 ? 11.327  -167.890 25.792  1.00 94.48  ? 125 LEU   W CA  1 
ATOM   40352 C  C   . LEU   W  9  126 ? 11.972  -168.973 26.655  1.00 95.77  ? 125 LEU   W C   1 
ATOM   40353 O  O   . LEU   W  9  126 ? 12.837  -169.688 26.145  1.00 100.97 ? 125 LEU   W O   1 
ATOM   40354 C  CB  . LEU   W  9  126 ? 12.394  -166.852 25.460  1.00 91.70  ? 125 LEU   W CB  1 
ATOM   40355 C  CG  . LEU   W  9  126 ? 13.335  -166.563 26.622  1.00 89.28  ? 125 LEU   W CG  1 
ATOM   40356 C  CD1 . LEU   W  9  126 ? 14.530  -165.754 26.171  1.00 88.86  ? 125 LEU   W CD1 1 
ATOM   40357 C  CD2 . LEU   W  9  126 ? 12.596  -165.858 27.738  1.00 88.02  ? 125 LEU   W CD2 1 
ATOM   40358 N  N   . ILE   W  9  127 ? 11.570  -169.079 27.913  1.00 93.91  ? 126 ILE   W N   1 
ATOM   40359 C  CA  . ILE   W  9  127 ? 12.224  -170.043 28.845  1.00 94.55  ? 126 ILE   W CA  1 
ATOM   40360 C  C   . ILE   W  9  127 ? 11.230  -171.124 29.299  1.00 88.31  ? 126 ILE   W C   1 
ATOM   40361 O  O   . ILE   W  9  127 ? 11.641  -171.993 30.085  1.00 86.23  ? 126 ILE   W O   1 
ATOM   40362 C  CB  . ILE   W  9  127 ? 12.881  -169.264 30.007  1.00 94.48  ? 126 ILE   W CB  1 
ATOM   40363 C  CG1 . ILE   W  9  127 ? 14.238  -169.862 30.373  1.00 100.65 ? 126 ILE   W CG1 1 
ATOM   40364 C  CG2 . ILE   W  9  127 ? 11.973  -169.117 31.219  1.00 92.09  ? 126 ILE   W CG2 1 
ATOM   40365 C  CD1 . ILE   W  9  127 ? 15.329  -169.478 29.405  1.00 104.44 ? 126 ILE   W CD1 1 
ATOM   40366 N  N   . GLY   W  9  128 ? 9.984   -171.100 28.813  1.00 87.02  ? 127 GLY   W N   1 
ATOM   40367 C  CA  . GLY   W  9  128 ? 9.075   -172.263 28.860  1.00 89.15  ? 127 GLY   W CA  1 
ATOM   40368 C  C   . GLY   W  9  128 ? 7.871   -172.085 29.772  1.00 90.46  ? 127 GLY   W C   1 
ATOM   40369 O  O   . GLY   W  9  128 ? 7.005   -172.978 29.750  1.00 93.40  ? 127 GLY   W O   1 
ATOM   40370 N  N   . CYS   W  9  129 ? 7.840   -171.037 30.588  1.00 89.82  ? 128 CYS   W N   1 
ATOM   40371 C  CA  . CYS   W  9  129 ? 6.724   -170.812 31.544  1.00 92.96  ? 128 CYS   W CA  1 
ATOM   40372 C  C   . CYS   W  9  129 ? 5.376   -170.758 30.823  1.00 94.95  ? 128 CYS   W C   1 
ATOM   40373 O  O   . CYS   W  9  129 ? 5.165   -169.825 30.068  1.00 95.14  ? 128 CYS   W O   1 
ATOM   40374 C  CB  . CYS   W  9  129 ? 6.924   -169.504 32.290  1.00 94.26  ? 128 CYS   W CB  1 
ATOM   40375 S  SG  . CYS   W  9  129 ? 5.595   -169.153 33.464  1.00 98.77  ? 128 CYS   W SG  1 
ATOM   40376 N  N   . ILE   W  9  130 ? 4.488   -171.706 31.117  1.00 96.26  ? 129 ILE   W N   1 
ATOM   40377 C  CA  . ILE   W  9  130 ? 3.128   -171.831 30.509  1.00 97.95  ? 129 ILE   W CA  1 
ATOM   40378 C  C   . ILE   W  9  130 ? 2.229   -170.733 31.096  1.00 97.97  ? 129 ILE   W C   1 
ATOM   40379 O  O   . ILE   W  9  130 ? 2.216   -170.574 32.330  1.00 93.19  ? 129 ILE   W O   1 
ATOM   40380 C  CB  . ILE   W  9  130 ? 2.537   -173.244 30.719  1.00 98.23  ? 129 ILE   W CB  1 
ATOM   40381 C  CG1 . ILE   W  9  130 ? 3.439   -174.333 30.128  1.00 95.13  ? 129 ILE   W CG1 1 
ATOM   40382 C  CG2 . ILE   W  9  130 ? 1.125   -173.334 30.152  1.00 99.04  ? 129 ILE   W CG2 1 
ATOM   40383 C  CD1 . ILE   W  9  130 ? 3.199   -175.708 30.699  1.00 95.22  ? 129 ILE   W CD1 1 
ATOM   40384 N  N   . ASP   W  9  131 ? 1.529   -170.001 30.223  1.00 102.96 ? 130 ASP   W N   1 
ATOM   40385 C  CA  . ASP   W  9  131 ? 0.509   -168.973 30.562  1.00 111.22 ? 130 ASP   W CA  1 
ATOM   40386 C  C   . ASP   W  9  131 ? -0.819  -169.401 29.925  1.00 110.44 ? 130 ASP   W C   1 
ATOM   40387 O  O   . ASP   W  9  131 ? -0.998  -169.169 28.711  1.00 104.99 ? 130 ASP   W O   1 
ATOM   40388 C  CB  . ASP   W  9  131 ? 0.970   -167.580 30.113  1.00 117.84 ? 130 ASP   W CB  1 
ATOM   40389 C  CG  . ASP   W  9  131 ? -0.123  -166.522 30.047  1.00 125.98 ? 130 ASP   W CG  1 
ATOM   40390 O  OD1 . ASP   W  9  131 ? -1.096  -166.622 30.824  1.00 133.73 ? 130 ASP   W OD1 1 
ATOM   40391 O  OD2 . ASP   W  9  131 ? 0.011   -165.598 29.216  1.00 133.86 ? 130 ASP   W OD2 1 
ATOM   40392 N  N   . GLU   W  9  132 ? -1.701  -170.019 30.716  1.00 114.87 ? 131 GLU   W N   1 
ATOM   40393 C  CA  . GLU   W  9  132 ? -3.023  -170.531 30.267  1.00 117.80 ? 131 GLU   W CA  1 
ATOM   40394 C  C   . GLU   W  9  132 ? -4.061  -169.425 30.473  1.00 116.36 ? 131 GLU   W C   1 
ATOM   40395 O  O   . GLU   W  9  132 ? -3.970  -168.722 31.501  1.00 114.99 ? 131 GLU   W O   1 
ATOM   40396 C  CB  . GLU   W  9  132 ? -3.399  -171.794 31.043  1.00 121.03 ? 131 GLU   W CB  1 
ATOM   40397 C  CG  . GLU   W  9  132 ? -4.103  -172.840 30.199  1.00 125.38 ? 131 GLU   W CG  1 
ATOM   40398 C  CD  . GLU   W  9  132 ? -4.557  -174.065 30.976  1.00 128.95 ? 131 GLU   W CD  1 
ATOM   40399 O  OE1 . GLU   W  9  132 ? -3.770  -175.029 31.075  1.00 129.31 ? 131 GLU   W OE1 1 
ATOM   40400 O  OE2 . GLU   W  9  132 ? -5.699  -174.058 31.476  1.00 138.97 ? 131 GLU   W OE2 1 
ATOM   40401 N  N   . ALA   W  9  133 ? -5.000  -169.274 29.535  1.00 114.94 ? 132 ALA   W N   1 
ATOM   40402 C  CA  . ALA   W  9  133 ? -6.015  -168.194 29.537  1.00 114.73 ? 132 ALA   W CA  1 
ATOM   40403 C  C   . ALA   W  9  133 ? -7.355  -168.713 29.016  1.00 112.55 ? 132 ALA   W C   1 
ATOM   40404 O  O   . ALA   W  9  133 ? -7.357  -169.502 28.054  1.00 113.34 ? 132 ALA   W O   1 
ATOM   40405 C  CB  . ALA   W  9  133 ? -5.534  -167.032 28.707  1.00 117.64 ? 132 ALA   W CB  1 
ATOM   40406 N  N   . LYS   W  9  134 ? -8.446  -168.255 29.634  1.00 113.83 ? 133 LYS   W N   1 
ATOM   40407 C  CA  . LYS   W  9  134 ? -9.839  -168.502 29.184  1.00 119.75 ? 133 LYS   W CA  1 
ATOM   40408 C  C   . LYS   W  9  134 ? -10.098 -167.713 27.897  1.00 118.54 ? 133 LYS   W C   1 
ATOM   40409 O  O   . LYS   W  9  134 ? -10.777 -168.255 27.006  1.00 118.43 ? 133 LYS   W O   1 
ATOM   40410 C  CB  . LYS   W  9  134 ? -10.836 -168.078 30.267  1.00 129.33 ? 133 LYS   W CB  1 
ATOM   40411 C  CG  . LYS   W  9  134 ? -10.788 -168.889 31.554  1.00 135.43 ? 133 LYS   W CG  1 
ATOM   40412 C  CD  . LYS   W  9  134 ? -11.855 -168.482 32.547  1.00 142.35 ? 133 LYS   W CD  1 
ATOM   40413 C  CE  . LYS   W  9  134 ? -11.892 -169.360 33.781  1.00 145.27 ? 133 LYS   W CE  1 
ATOM   40414 N  NZ  . LYS   W  9  134 ? -13.282 -169.720 34.145  1.00 149.69 ? 133 LYS   W NZ  1 
ATOM   40415 N  N   . ASP   W  9  135 ? -9.554  -166.493 27.807  1.00 114.33 ? 134 ASP   W N   1 
ATOM   40416 C  CA  . ASP   W  9  135 ? -9.974  -165.457 26.824  1.00 111.27 ? 134 ASP   W CA  1 
ATOM   40417 C  C   . ASP   W  9  135 ? -8.959  -165.372 25.677  1.00 106.96 ? 134 ASP   W C   1 
ATOM   40418 O  O   . ASP   W  9  135 ? -9.303  -165.845 24.575  1.00 111.13 ? 134 ASP   W O   1 
ATOM   40419 C  CB  . ASP   W  9  135 ? -10.221 -164.111 27.513  1.00 113.24 ? 134 ASP   W CB  1 
ATOM   40420 C  CG  . ASP   W  9  135 ? -9.211  -163.744 28.589  1.00 111.23 ? 134 ASP   W CG  1 
ATOM   40421 O  OD1 . ASP   W  9  135 ? -8.072  -164.252 28.527  1.00 107.14 ? 134 ASP   W OD1 1 
ATOM   40422 O  OD2 . ASP   W  9  135 ? -9.573  -162.955 29.484  1.00 119.85 ? 134 ASP   W OD2 1 
ATOM   40423 N  N   . PHE   W  9  136 ? -7.772  -164.795 25.905  1.00 99.59  ? 135 PHE   W N   1 
ATOM   40424 C  CA  . PHE   W  9  136 ? -6.789  -164.482 24.832  1.00 97.60  ? 135 PHE   W CA  1 
ATOM   40425 C  C   . PHE   W  9  136 ? -5.346  -164.595 25.335  1.00 95.53  ? 135 PHE   W C   1 
ATOM   40426 O  O   . PHE   W  9  136 ? -5.082  -164.343 26.530  1.00 91.12  ? 135 PHE   W O   1 
ATOM   40427 C  CB  . PHE   W  9  136 ? -7.035  -163.082 24.265  1.00 98.49  ? 135 PHE   W CB  1 
ATOM   40428 C  CG  . PHE   W  9  136 ? -7.087  -161.987 25.300  1.00 98.57  ? 135 PHE   W CG  1 
ATOM   40429 C  CD1 . PHE   W  9  136 ? -5.935  -161.327 25.698  1.00 98.02  ? 135 PHE   W CD1 1 
ATOM   40430 C  CD2 . PHE   W  9  136 ? -8.293  -161.618 25.877  1.00 99.82  ? 135 PHE   W CD2 1 
ATOM   40431 C  CE1 . PHE   W  9  136 ? -5.989  -160.323 26.653  1.00 99.30  ? 135 PHE   W CE1 1 
ATOM   40432 C  CE2 . PHE   W  9  136 ? -8.346  -160.614 26.831  1.00 99.48  ? 135 PHE   W CE2 1 
ATOM   40433 C  CZ  . PHE   W  9  136 ? -7.194  -159.969 27.217  1.00 100.17 ? 135 PHE   W CZ  1 
ATOM   40434 N  N   . ILE   W  9  137 ? -4.449  -164.960 24.412  1.00 96.51  ? 136 ILE   W N   1 
ATOM   40435 C  CA  . ILE   W  9  137 ? -2.963  -164.922 24.555  1.00 97.43  ? 136 ILE   W CA  1 
ATOM   40436 C  C   . ILE   W  9  137 ? -2.420  -163.974 23.480  1.00 92.06  ? 136 ILE   W C   1 
ATOM   40437 O  O   . ILE   W  9  137 ? -2.974  -163.973 22.364  1.00 91.76  ? 136 ILE   W O   1 
ATOM   40438 C  CB  . ILE   W  9  137 ? -2.361  -166.339 24.434  1.00 98.68  ? 136 ILE   W CB  1 
ATOM   40439 C  CG1 . ILE   W  9  137 ? -2.873  -167.277 25.532  1.00 102.87 ? 136 ILE   W CG1 1 
ATOM   40440 C  CG2 . ILE   W  9  137 ? -0.839  -166.299 24.400  1.00 98.84  ? 136 ILE   W CG2 1 
ATOM   40441 C  CD1 . ILE   W  9  137 ? -2.554  -166.830 26.943  1.00 105.09 ? 136 ILE   W CD1 1 
ATOM   40442 N  N   . VAL   W  9  138 ? -1.386  -163.198 23.812  1.00 88.66  ? 137 VAL   W N   1 
ATOM   40443 C  CA  . VAL   W  9  138 ? -0.721  -162.236 22.882  1.00 86.72  ? 137 VAL   W CA  1 
ATOM   40444 C  C   . VAL   W  9  138 ? 0.785   -162.499 22.907  1.00 85.26  ? 137 VAL   W C   1 
ATOM   40445 O  O   . VAL   W  9  138 ? 1.285   -162.991 23.940  1.00 83.03  ? 137 VAL   W O   1 
ATOM   40446 C  CB  . VAL   W  9  138 ? -1.042  -160.775 23.248  1.00 87.48  ? 137 VAL   W CB  1 
ATOM   40447 C  CG1 . VAL   W  9  138 ? -2.541  -160.524 23.259  1.00 88.57  ? 137 VAL   W CG1 1 
ATOM   40448 C  CG2 . VAL   W  9  138 ? -0.422  -160.364 24.577  1.00 87.39  ? 137 VAL   W CG2 1 
ATOM   40449 N  N   . SER   W  9  139 ? 1.473   -162.164 21.815  1.00 85.51  ? 138 SER   W N   1 
ATOM   40450 C  CA  . SER   W  9  139 ? 2.934   -162.365 21.648  1.00 87.16  ? 138 SER   W CA  1 
ATOM   40451 C  C   . SER   W  9  139 ? 3.485   -161.401 20.595  1.00 87.24  ? 138 SER   W C   1 
ATOM   40452 O  O   . SER   W  9  139 ? 2.725   -161.036 19.682  1.00 90.23  ? 138 SER   W O   1 
ATOM   40453 C  CB  . SER   W  9  139 ? 3.232   -163.791 21.284  1.00 88.64  ? 138 SER   W CB  1 
ATOM   40454 O  OG  . SER   W  9  139 ? 4.603   -164.081 21.500  1.00 92.44  ? 138 SER   W OG  1 
ATOM   40455 N  N   . GLY   W  9  140 ? 4.753   -161.004 20.736  1.00 87.74  ? 139 GLY   W N   1 
ATOM   40456 C  CA  . GLY   W  9  140 ? 5.517   -160.274 19.706  1.00 89.63  ? 139 GLY   W CA  1 
ATOM   40457 C  C   . GLY   W  9  140 ? 5.863   -158.853 20.120  1.00 92.27  ? 139 GLY   W C   1 
ATOM   40458 O  O   . GLY   W  9  140 ? 5.713   -158.515 21.313  1.00 95.62  ? 139 GLY   W O   1 
ATOM   40459 N  N   . THR   W  9  141 ? 6.310   -158.050 19.151  1.00 91.96  ? 140 THR   W N   1 
ATOM   40460 C  CA  . THR   W  9  141 ? 6.873   -156.688 19.349  1.00 92.78  ? 140 THR   W CA  1 
ATOM   40461 C  C   . THR   W  9  141 ? 5.755   -155.679 19.643  1.00 94.95  ? 140 THR   W C   1 
ATOM   40462 O  O   . THR   W  9  141 ? 6.077   -154.602 20.192  1.00 98.78  ? 140 THR   W O   1 
ATOM   40463 C  CB  . THR   W  9  141 ? 7.730   -156.286 18.142  1.00 91.57  ? 140 THR   W CB  1 
ATOM   40464 O  OG1 . THR   W  9  141 ? 7.023   -156.642 16.953  1.00 88.90  ? 140 THR   W OG1 1 
ATOM   40465 C  CG2 . THR   W  9  141 ? 9.088   -156.953 18.148  1.00 91.31  ? 140 THR   W CG2 1 
ATOM   40466 N  N   . ALA   W  9  142 ? 4.503   -156.008 19.303  1.00 92.58  ? 141 ALA   W N   1 
ATOM   40467 C  CA  . ALA   W  9  142 ? 3.308   -155.172 19.569  1.00 94.46  ? 141 ALA   W CA  1 
ATOM   40468 C  C   . ALA   W  9  142 ? 2.405   -155.865 20.597  1.00 92.28  ? 141 ALA   W C   1 
ATOM   40469 O  O   . ALA   W  9  142 ? 1.168   -155.815 20.430  1.00 89.34  ? 141 ALA   W O   1 
ATOM   40470 C  CB  . ALA   W  9  142 ? 2.566   -154.896 18.283  1.00 96.72  ? 141 ALA   W CB  1 
ATOM   40471 N  N   . SER   W  9  143 ? 2.994   -156.477 21.629  1.00 92.96  ? 142 SER   W N   1 
ATOM   40472 C  CA  . SER   W  9  143 ? 2.256   -157.215 22.689  1.00 96.37  ? 142 SER   W CA  1 
ATOM   40473 C  C   . SER   W  9  143 ? 1.465   -156.225 23.555  1.00 97.80  ? 142 SER   W C   1 
ATOM   40474 O  O   . SER   W  9  143 ? 0.289   -156.516 23.856  1.00 93.82  ? 142 SER   W O   1 
ATOM   40475 C  CB  . SER   W  9  143 ? 3.178   -158.079 23.515  1.00 97.25  ? 142 SER   W CB  1 
ATOM   40476 O  OG  . SER   W  9  143 ? 4.036   -157.296 24.333  1.00 104.44 ? 142 SER   W OG  1 
ATOM   40477 N  N   . ASP   W  9  144 ? 2.088   -155.100 23.927  1.00 98.06  ? 143 ASP   W N   1 
ATOM   40478 C  CA  . ASP   W  9  144 ? 1.452   -153.994 24.696  1.00 100.09 ? 143 ASP   W CA  1 
ATOM   40479 C  C   . ASP   W  9  144 ? 0.180   -153.530 23.975  1.00 96.95  ? 143 ASP   W C   1 
ATOM   40480 O  O   . ASP   W  9  144 ? -0.865  -153.402 24.644  1.00 97.79  ? 143 ASP   W O   1 
ATOM   40481 C  CB  . ASP   W  9  144 ? 2.417   -152.821 24.890  1.00 105.61 ? 143 ASP   W CB  1 
ATOM   40482 C  CG  . ASP   W  9  144 ? 3.484   -153.061 25.945  1.00 109.00 ? 143 ASP   W CG  1 
ATOM   40483 O  OD1 . ASP   W  9  144 ? 3.790   -154.244 26.217  1.00 107.13 ? 143 ASP   W OD1 1 
ATOM   40484 O  OD2 . ASP   W  9  144 ? 4.004   -152.060 26.489  1.00 115.32 ? 143 ASP   W OD2 1 
ATOM   40485 N  N   . GLN   W  9  145 ? 0.274   -153.288 22.664  1.00 92.38  ? 144 GLN   W N   1 
ATOM   40486 C  CA  . GLN   W  9  145 ? -0.860  -152.847 21.809  1.00 92.77  ? 144 GLN   W CA  1 
ATOM   40487 C  C   . GLN   W  9  145 ? -1.931  -153.942 21.788  1.00 92.93  ? 144 GLN   W C   1 
ATOM   40488 O  O   . GLN   W  9  145 ? -3.115  -153.599 21.983  1.00 93.30  ? 144 GLN   W O   1 
ATOM   40489 C  CB  . GLN   W  9  145 ? -0.394  -152.531 20.387  1.00 90.72  ? 144 GLN   W CB  1 
ATOM   40490 C  CG  . GLN   W  9  145 ? 0.515   -151.314 20.294  1.00 91.88  ? 144 GLN   W CG  1 
ATOM   40491 C  CD  . GLN   W  9  145 ? 1.982   -151.655 20.406  1.00 89.06  ? 144 GLN   W CD  1 
ATOM   40492 O  OE1 . GLN   W  9  145 ? 2.384   -152.521 21.178  1.00 84.04  ? 144 GLN   W OE1 1 
ATOM   40493 N  NE2 . GLN   W  9  145 ? 2.802   -150.955 19.641  1.00 91.93  ? 144 GLN   W NE2 1 
ATOM   40494 N  N   . LEU   W  9  146 ? -1.522  -155.200 21.566  1.00 94.45  ? 145 LEU   W N   1 
ATOM   40495 C  CA  . LEU   W  9  146 ? -2.427  -156.383 21.519  1.00 93.85  ? 145 LEU   W CA  1 
ATOM   40496 C  C   . LEU   W  9  146 ? -3.136  -156.531 22.871  1.00 92.01  ? 145 LEU   W C   1 
ATOM   40497 O  O   . LEU   W  9  146 ? -4.355  -156.796 22.862  1.00 93.46  ? 145 LEU   W O   1 
ATOM   40498 C  CB  . LEU   W  9  146 ? -1.636  -157.649 21.162  1.00 94.07  ? 145 LEU   W CB  1 
ATOM   40499 C  CG  . LEU   W  9  146 ? -1.315  -157.849 19.680  1.00 93.34  ? 145 LEU   W CG  1 
ATOM   40500 C  CD1 . LEU   W  9  146 ? -0.318  -158.981 19.488  1.00 92.56  ? 145 LEU   W CD1 1 
ATOM   40501 C  CD2 . LEU   W  9  146 ? -2.574  -158.121 18.871  1.00 94.90  ? 145 LEU   W CD2 1 
ATOM   40502 N  N   . PHE   W  9  147 ? -2.410  -156.357 23.982  1.00 92.21  ? 146 PHE   W N   1 
ATOM   40503 C  CA  . PHE   W  9  147 ? -2.963  -156.422 25.363  1.00 95.92  ? 146 PHE   W CA  1 
ATOM   40504 C  C   . PHE   W  9  147 ? -4.082  -155.385 25.514  1.00 98.20  ? 146 PHE   W C   1 
ATOM   40505 O  O   . PHE   W  9  147 ? -5.141  -155.727 26.068  1.00 102.16 ? 146 PHE   W O   1 
ATOM   40506 C  CB  . PHE   W  9  147 ? -1.876  -156.211 26.423  1.00 95.86  ? 146 PHE   W CB  1 
ATOM   40507 C  CG  . PHE   W  9  147 ? -1.246  -157.476 26.949  1.00 95.54  ? 146 PHE   W CG  1 
ATOM   40508 C  CD1 . PHE   W  9  147 ? -2.032  -158.497 27.463  1.00 94.92  ? 146 PHE   W CD1 1 
ATOM   40509 C  CD2 . PHE   W  9  147 ? 0.131   -157.637 26.952  1.00 95.64  ? 146 PHE   W CD2 1 
ATOM   40510 C  CE1 . PHE   W  9  147 ? -1.453  -159.658 27.953  1.00 94.68  ? 146 PHE   W CE1 1 
ATOM   40511 C  CE2 . PHE   W  9  147 ? 0.708   -158.798 27.443  1.00 95.03  ? 146 PHE   W CE2 1 
ATOM   40512 C  CZ  . PHE   W  9  147 ? -0.085  -159.806 27.943  1.00 95.95  ? 146 PHE   W CZ  1 
ATOM   40513 N  N   . GLY   W  9  148 ? -3.850  -154.163 25.026  1.00 98.65  ? 147 GLY   W N   1 
ATOM   40514 C  CA  . GLY   W  9  148 ? -4.816  -153.050 25.079  1.00 100.14 ? 147 GLY   W CA  1 
ATOM   40515 C  C   . GLY   W  9  148 ? -6.005  -153.281 24.162  1.00 101.32 ? 147 GLY   W C   1 
ATOM   40516 O  O   . GLY   W  9  148 ? -7.141  -152.989 24.590  1.00 100.41 ? 147 GLY   W O   1 
ATOM   40517 N  N   . MET   W  9  149 ? -5.757  -153.777 22.943  1.00 102.51 ? 148 MET   W N   1 
ATOM   40518 C  CA  . MET   W  9  149 ? -6.805  -154.070 21.926  1.00 103.10 ? 148 MET   W CA  1 
ATOM   40519 C  C   . MET   W  9  149 ? -7.698  -155.210 22.429  1.00 105.51 ? 148 MET   W C   1 
ATOM   40520 O  O   . MET   W  9  149 ? -8.932  -155.044 22.402  1.00 107.31 ? 148 MET   W O   1 
ATOM   40521 C  CB  . MET   W  9  149 ? -6.197  -154.472 20.576  1.00 104.27 ? 148 MET   W CB  1 
ATOM   40522 C  CG  . MET   W  9  149 ? -5.623  -153.314 19.773  1.00 104.99 ? 148 MET   W CG  1 
ATOM   40523 S  SD  . MET   W  9  149 ? -6.741  -151.903 19.574  1.00 108.05 ? 148 MET   W SD  1 
ATOM   40524 C  CE  . MET   W  9  149 ? -8.174  -152.682 18.833  1.00 107.53 ? 148 MET   W CE  1 
ATOM   40525 N  N   . CYS   W  9  150 ? -7.095  -156.319 22.869  1.00 105.66 ? 149 CYS   W N   1 
ATOM   40526 C  CA  . CYS   W  9  150 ? -7.808  -157.545 23.322  1.00 105.28 ? 149 CYS   W CA  1 
ATOM   40527 C  C   . CYS   W  9  150 ? -8.612  -157.241 24.593  1.00 106.93 ? 149 CYS   W C   1 
ATOM   40528 O  O   . CYS   W  9  150 ? -9.807  -157.592 24.633  1.00 108.47 ? 149 CYS   W O   1 
ATOM   40529 C  CB  . CYS   W  9  150 ? -6.842  -158.700 23.565  1.00 105.89 ? 149 CYS   W CB  1 
ATOM   40530 S  SG  . CYS   W  9  150 ? -6.076  -159.338 22.051  1.00 101.91 ? 149 CYS   W SG  1 
ATOM   40531 N  N   . GLU   W  9  151 ? -7.987  -156.584 25.574  1.00 106.83 ? 150 GLU   W N   1 
ATOM   40532 C  CA  . GLU   W  9  151 ? -8.567  -156.344 26.923  1.00 109.89 ? 150 GLU   W CA  1 
ATOM   40533 C  C   . GLU   W  9  151 ? -9.858  -155.521 26.805  1.00 110.63 ? 150 GLU   W C   1 
ATOM   40534 O  O   . GLU   W  9  151 ? -10.750 -155.707 27.655  1.00 114.99 ? 150 GLU   W O   1 
ATOM   40535 C  CB  . GLU   W  9  151 ? -7.543  -155.653 27.824  1.00 112.37 ? 150 GLU   W CB  1 
ATOM   40536 C  CG  . GLU   W  9  151 ? -7.910  -155.687 29.293  1.00 113.07 ? 150 GLU   W CG  1 
ATOM   40537 C  CD  . GLU   W  9  151 ? -8.029  -157.087 29.865  1.00 113.31 ? 150 GLU   W CD  1 
ATOM   40538 O  OE1 . GLU   W  9  151 ? -7.034  -157.839 29.797  1.00 105.72 ? 150 GLU   W OE1 1 
ATOM   40539 O  OE2 . GLU   W  9  151 ? -9.117  -157.427 30.370  1.00 116.03 ? 150 GLU   W OE2 1 
ATOM   40540 N  N   . SER   W  9  152 ? -9.955  -154.652 25.795  1.00 112.53 ? 151 SER   W N   1 
ATOM   40541 C  CA  . SER   W  9  152 ? -11.127 -153.772 25.552  1.00 114.68 ? 151 SER   W CA  1 
ATOM   40542 C  C   . SER   W  9  152 ? -12.135 -154.464 24.623  1.00 115.18 ? 151 SER   W C   1 
ATOM   40543 O  O   . SER   W  9  152 ? -13.321 -154.518 25.001  1.00 112.57 ? 151 SER   W O   1 
ATOM   40544 C  CB  . SER   W  9  152 ? -10.691 -152.426 25.024  1.00 115.21 ? 151 SER   W CB  1 
ATOM   40545 O  OG  . SER   W  9  152 ? -9.779  -152.570 23.947  1.00 117.26 ? 151 SER   W OG  1 
ATOM   40546 N  N   . LEU   W  9  153 ? -11.687 -154.990 23.473  1.00 115.09 ? 152 LEU   W N   1 
ATOM   40547 C  CA  . LEU   W  9  153 ? -12.572 -155.511 22.388  1.00 114.61 ? 152 LEU   W CA  1 
ATOM   40548 C  C   . LEU   W  9  153 ? -13.244 -156.825 22.807  1.00 115.78 ? 152 LEU   W C   1 
ATOM   40549 O  O   . LEU   W  9  153 ? -14.425 -157.012 22.447  1.00 116.82 ? 152 LEU   W O   1 
ATOM   40550 C  CB  . LEU   W  9  153 ? -11.776 -155.727 21.095  1.00 113.27 ? 152 LEU   W CB  1 
ATOM   40551 C  CG  . LEU   W  9  153 ? -11.293 -154.480 20.352  1.00 113.63 ? 152 LEU   W CG  1 
ATOM   40552 C  CD1 . LEU   W  9  153 ? -10.826 -154.855 18.954  1.00 113.56 ? 152 LEU   W CD1 1 
ATOM   40553 C  CD2 . LEU   W  9  153 ? -12.368 -153.403 20.272  1.00 116.18 ? 152 LEU   W CD2 1 
ATOM   40554 N  N   . TYR   W  9  154 ? -12.528 -157.707 23.512  1.00 112.89 ? 153 TYR   W N   1 
ATOM   40555 C  CA  . TYR   W  9  154 ? -12.936 -159.119 23.744  1.00 113.02 ? 153 TYR   W CA  1 
ATOM   40556 C  C   . TYR   W  9  154 ? -14.199 -159.188 24.610  1.00 110.94 ? 153 TYR   W C   1 
ATOM   40557 O  O   . TYR   W  9  154 ? -14.333 -158.389 25.559  1.00 109.40 ? 153 TYR   W O   1 
ATOM   40558 C  CB  . TYR   W  9  154 ? -11.819 -159.927 24.409  1.00 111.88 ? 153 TYR   W CB  1 
ATOM   40559 C  CG  . TYR   W  9  154 ? -12.171 -161.377 24.632  1.00 116.22 ? 153 TYR   W CG  1 
ATOM   40560 C  CD1 . TYR   W  9  154 ? -11.994 -162.315 23.629  1.00 117.07 ? 153 TYR   W CD1 1 
ATOM   40561 C  CD2 . TYR   W  9  154 ? -12.715 -161.807 25.833  1.00 117.28 ? 153 TYR   W CD2 1 
ATOM   40562 C  CE1 . TYR   W  9  154 ? -12.332 -163.646 23.816  1.00 119.63 ? 153 TYR   W CE1 1 
ATOM   40563 C  CE2 . TYR   W  9  154 ? -13.060 -163.133 26.037  1.00 119.67 ? 153 TYR   W CE2 1 
ATOM   40564 C  CZ  . TYR   W  9  154 ? -12.866 -164.057 25.025  1.00 120.74 ? 153 TYR   W CZ  1 
ATOM   40565 O  OH  . TYR   W  9  154 ? -13.198 -165.366 25.220  1.00 124.98 ? 153 TYR   W OH  1 
ATOM   40566 N  N   . GLU   W  9  155 ? -15.088 -160.131 24.279  1.00 112.31 ? 154 GLU   W N   1 
ATOM   40567 C  CA  . GLU   W  9  155 ? -16.204 -160.604 25.145  1.00 116.89 ? 154 GLU   W CA  1 
ATOM   40568 C  C   . GLU   W  9  155 ? -16.323 -162.124 25.005  1.00 116.22 ? 154 GLU   W C   1 
ATOM   40569 O  O   . GLU   W  9  155 ? -16.006 -162.679 23.953  1.00 117.32 ? 154 GLU   W O   1 
ATOM   40570 C  CB  . GLU   W  9  155 ? -17.512 -159.879 24.811  1.00 119.55 ? 154 GLU   W CB  1 
ATOM   40571 C  CG  . GLU   W  9  155 ? -17.843 -159.814 23.330  1.00 122.69 ? 154 GLU   W CG  1 
ATOM   40572 C  CD  . GLU   W  9  155 ? -19.170 -159.133 23.034  1.00 126.84 ? 154 GLU   W CD  1 
ATOM   40573 O  OE1 . GLU   W  9  155 ? -20.219 -159.697 23.405  1.00 133.54 ? 154 GLU   W OE1 1 
ATOM   40574 O  OE2 . GLU   W  9  155 ? -19.152 -158.029 22.456  1.00 129.50 ? 154 GLU   W OE2 1 
ATOM   40575 N  N   . PRO   W  9  156 ? -16.766 -162.851 26.059  1.00 111.61 ? 155 PRO   W N   1 
ATOM   40576 C  CA  . PRO   W  9  156 ? -16.831 -164.312 26.014  1.00 110.57 ? 155 PRO   W CA  1 
ATOM   40577 C  C   . PRO   W  9  156 ? -17.902 -164.861 25.057  1.00 113.09 ? 155 PRO   W C   1 
ATOM   40578 O  O   . PRO   W  9  156 ? -18.839 -164.149 24.752  1.00 114.72 ? 155 PRO   W O   1 
ATOM   40579 C  CB  . PRO   W  9  156 ? -17.192 -164.723 27.453  1.00 109.15 ? 155 PRO   W CB  1 
ATOM   40580 C  CG  . PRO   W  9  156 ? -16.971 -163.481 28.292  1.00 108.75 ? 155 PRO   W CG  1 
ATOM   40581 C  CD  . PRO   W  9  156 ? -17.214 -162.319 27.354  1.00 110.89 ? 155 PRO   W CD  1 
ATOM   40582 N  N   . ASN   W  9  157 ? -17.727 -166.113 24.621  1.00 116.01 ? 156 ASN   W N   1 
ATOM   40583 C  CA  . ASN   W  9  157 ? -18.726 -166.928 23.874  1.00 118.64 ? 156 ASN   W CA  1 
ATOM   40584 C  C   . ASN   W  9  157 ? -19.150 -166.216 22.584  1.00 117.68 ? 156 ASN   W C   1 
ATOM   40585 O  O   . ASN   W  9  157 ? -20.366 -166.173 22.306  1.00 118.22 ? 156 ASN   W O   1 
ATOM   40586 C  CB  . ASN   W  9  157 ? -19.945 -167.252 24.742  1.00 124.46 ? 156 ASN   W CB  1 
ATOM   40587 C  CG  . ASN   W  9  157 ? -19.600 -168.121 25.930  1.00 125.93 ? 156 ASN   W CG  1 
ATOM   40588 O  OD1 . ASN   W  9  157 ? -19.766 -167.706 27.075  1.00 130.60 ? 156 ASN   W OD1 1 
ATOM   40589 N  ND2 . ASN   W  9  157 ? -19.110 -169.323 25.670  1.00 128.52 ? 156 ASN   W ND2 1 
ATOM   40590 N  N   . LEU   W  9  158 ? -18.187 -165.693 21.821  1.00 116.22 ? 157 LEU   W N   1 
ATOM   40591 C  CA  . LEU   W  9  158 ? -18.436 -165.127 20.469  1.00 118.40 ? 157 LEU   W CA  1 
ATOM   40592 C  C   . LEU   W  9  158 ? -18.629 -166.280 19.481  1.00 118.58 ? 157 LEU   W C   1 
ATOM   40593 O  O   . LEU   W  9  158 ? -17.952 -167.314 19.641  1.00 116.10 ? 157 LEU   W O   1 
ATOM   40594 C  CB  . LEU   W  9  158 ? -17.261 -164.241 20.045  1.00 118.57 ? 157 LEU   W CB  1 
ATOM   40595 C  CG  . LEU   W  9  158 ? -17.206 -162.859 20.695  1.00 118.52 ? 157 LEU   W CG  1 
ATOM   40596 C  CD1 . LEU   W  9  158 ? -15.822 -162.249 20.541  1.00 115.82 ? 157 LEU   W CD1 1 
ATOM   40597 C  CD2 . LEU   W  9  158 ? -18.265 -161.937 20.108  1.00 120.05 ? 157 LEU   W CD2 1 
ATOM   40598 N  N   . GLU   W  9  159 ? -19.520 -166.100 18.502  1.00 123.29 ? 158 GLU   W N   1 
ATOM   40599 C  CA  . GLU   W  9  159 ? -19.717 -167.046 17.372  1.00 125.96 ? 158 GLU   W CA  1 
ATOM   40600 C  C   . GLU   W  9  159 ? -18.506 -166.940 16.447  1.00 124.00 ? 158 GLU   W C   1 
ATOM   40601 O  O   . GLU   W  9  159 ? -17.903 -165.875 16.334  1.00 122.43 ? 158 GLU   W O   1 
ATOM   40602 C  CB  . GLU   W  9  159 ? -21.029 -166.753 16.639  1.00 125.68 ? 158 GLU   W CB  1 
ATOM   40603 C  CG  . GLU   W  9  159 ? -22.269 -167.089 17.452  1.00 129.42 ? 158 GLU   W CG  1 
ATOM   40604 C  CD  . GLU   W  9  159 ? -22.427 -168.561 17.802  1.00 128.85 ? 158 GLU   W CD  1 
ATOM   40605 O  OE1 . GLU   W  9  159 ? -22.097 -169.409 16.952  1.00 129.86 ? 158 GLU   W OE1 1 
ATOM   40606 O  OE2 . GLU   W  9  159 ? -22.874 -168.856 18.927  1.00 128.51 ? 158 GLU   W OE2 1 
ATOM   40607 N  N   . PRO   W  9  160 ? -18.099 -168.046 15.784  1.00 122.20 ? 159 PRO   W N   1 
ATOM   40608 C  CA  . PRO   W  9  160 ? -16.941 -168.046 14.886  1.00 120.57 ? 159 PRO   W CA  1 
ATOM   40609 C  C   . PRO   W  9  160 ? -16.806 -166.819 13.967  1.00 119.67 ? 159 PRO   W C   1 
ATOM   40610 O  O   . PRO   W  9  160 ? -15.702 -166.325 13.837  1.00 119.00 ? 159 PRO   W O   1 
ATOM   40611 C  CB  . PRO   W  9  160 ? -17.183 -169.307 14.045  1.00 121.36 ? 159 PRO   W CB  1 
ATOM   40612 C  CG  . PRO   W  9  160 ? -17.875 -170.259 14.999  1.00 123.32 ? 159 PRO   W CG  1 
ATOM   40613 C  CD  . PRO   W  9  160 ? -18.718 -169.376 15.897  1.00 124.21 ? 159 PRO   W CD  1 
ATOM   40614 N  N   . GLU   W  9  161 ? -17.911 -166.360 13.365  1.00 123.34 ? 160 GLU   W N   1 
ATOM   40615 C  CA  . GLU   W  9  161 ? -17.936 -165.230 12.391  1.00 123.86 ? 160 GLU   W CA  1 
ATOM   40616 C  C   . GLU   W  9  161 ? -17.696 -163.905 13.128  1.00 121.68 ? 160 GLU   W C   1 
ATOM   40617 O  O   . GLU   W  9  161 ? -17.046 -163.015 12.544  1.00 118.85 ? 160 GLU   W O   1 
ATOM   40618 C  CB  . GLU   W  9  161 ? -19.262 -165.187 11.625  1.00 127.06 ? 160 GLU   W CB  1 
ATOM   40619 C  CG  . GLU   W  9  161 ? -19.497 -166.399 10.738  1.00 129.12 ? 160 GLU   W CG  1 
ATOM   40620 C  CD  . GLU   W  9  161 ? -20.173 -167.588 11.405  1.00 131.45 ? 160 GLU   W CD  1 
ATOM   40621 O  OE1 . GLU   W  9  161 ? -20.243 -167.612 12.652  1.00 130.85 ? 160 GLU   W OE1 1 
ATOM   40622 O  OE2 . GLU   W  9  161 ? -20.627 -168.490 10.673  1.00 132.86 ? 160 GLU   W OE2 1 
ATOM   40623 N  N   . ASP   W  9  162 ? -18.208 -163.784 14.358  1.00 120.42 ? 161 ASP   W N   1 
ATOM   40624 C  CA  . ASP   W  9  162 ? -18.024 -162.596 15.235  1.00 119.49 ? 161 ASP   W CA  1 
ATOM   40625 C  C   . ASP   W  9  162 ? -16.591 -162.601 15.779  1.00 117.05 ? 161 ASP   W C   1 
ATOM   40626 O  O   . ASP   W  9  162 ? -15.935 -161.544 15.712  1.00 118.91 ? 161 ASP   W O   1 
ATOM   40627 C  CB  . ASP   W  9  162 ? -19.053 -162.573 16.370  1.00 117.26 ? 161 ASP   W CB  1 
ATOM   40628 C  CG  . ASP   W  9  162 ? -20.493 -162.480 15.897  1.00 119.12 ? 161 ASP   W CG  1 
ATOM   40629 O  OD1 . ASP   W  9  162 ? -20.754 -161.685 14.972  1.00 118.95 ? 161 ASP   W OD1 1 
ATOM   40630 O  OD2 . ASP   W  9  162 ? -21.341 -163.205 16.455  1.00 118.35 ? 161 ASP   W OD2 1 
ATOM   40631 N  N   . LEU   W  9  163 ? -16.128 -163.750 16.285  1.00 115.89 ? 162 LEU   W N   1 
ATOM   40632 C  CA  . LEU   W  9  163 ? -14.762 -163.934 16.850  1.00 113.60 ? 162 LEU   W CA  1 
ATOM   40633 C  C   . LEU   W  9  163 ? -13.712 -163.532 15.807  1.00 109.85 ? 162 LEU   W C   1 
ATOM   40634 O  O   . LEU   W  9  163 ? -12.669 -162.983 16.212  1.00 108.64 ? 162 LEU   W O   1 
ATOM   40635 C  CB  . LEU   W  9  163 ? -14.574 -165.393 17.278  1.00 114.25 ? 162 LEU   W CB  1 
ATOM   40636 C  CG  . LEU   W  9  163 ? -13.195 -165.742 17.840  1.00 113.72 ? 162 LEU   W CG  1 
ATOM   40637 C  CD1 . LEU   W  9  163 ? -12.947 -165.022 19.155  1.00 113.56 ? 162 LEU   W CD1 1 
ATOM   40638 C  CD2 . LEU   W  9  163 ? -13.040 -167.246 18.018  1.00 113.51 ? 162 LEU   W CD2 1 
ATOM   40639 N  N   . PHE   W  9  164 ? -13.973 -163.813 14.525  1.00 109.98 ? 163 PHE   W N   1 
ATOM   40640 C  CA  . PHE   W  9  164 ? -13.094 -163.451 13.383  1.00 108.55 ? 163 PHE   W CA  1 
ATOM   40641 C  C   . PHE   W  9  164 ? -12.931 -161.930 13.315  1.00 107.98 ? 163 PHE   W C   1 
ATOM   40642 O  O   . PHE   W  9  164 ? -11.793 -161.465 13.126  1.00 106.42 ? 163 PHE   W O   1 
ATOM   40643 C  CB  . PHE   W  9  164 ? -13.649 -163.963 12.052  1.00 110.01 ? 163 PHE   W CB  1 
ATOM   40644 C  CG  . PHE   W  9  164 ? -12.970 -163.351 10.854  1.00 110.83 ? 163 PHE   W CG  1 
ATOM   40645 C  CD1 . PHE   W  9  164 ? -11.681 -163.725 10.506  1.00 109.26 ? 163 PHE   W CD1 1 
ATOM   40646 C  CD2 . PHE   W  9  164 ? -13.599 -162.370 10.102  1.00 112.70 ? 163 PHE   W CD2 1 
ATOM   40647 C  CE1 . PHE   W  9  164 ? -11.045 -163.149 9.417   1.00 109.96 ? 163 PHE   W CE1 1 
ATOM   40648 C  CE2 . PHE   W  9  164 ? -12.962 -161.795 9.013   1.00 112.79 ? 163 PHE   W CE2 1 
ATOM   40649 C  CZ  . PHE   W  9  164 ? -11.687 -162.185 8.674   1.00 111.37 ? 163 PHE   W CZ  1 
ATOM   40650 N  N   . GLU   W  9  165 ? -14.038 -161.191 13.445  1.00 109.43 ? 164 GLU   W N   1 
ATOM   40651 C  CA  . GLU   W  9  165 ? -14.061 -159.705 13.362  1.00 110.18 ? 164 GLU   W CA  1 
ATOM   40652 C  C   . GLU   W  9  165 ? -13.251 -159.127 14.528  1.00 107.29 ? 164 GLU   W C   1 
ATOM   40653 O  O   . GLU   W  9  165 ? -12.450 -158.204 14.283  1.00 108.34 ? 164 GLU   W O   1 
ATOM   40654 C  CB  . GLU   W  9  165 ? -15.497 -159.168 13.371  1.00 112.56 ? 164 GLU   W CB  1 
ATOM   40655 C  CG  . GLU   W  9  165 ? -16.330 -159.611 12.179  1.00 113.27 ? 164 GLU   W CG  1 
ATOM   40656 C  CD  . GLU   W  9  165 ? -15.844 -159.123 10.824  1.00 110.88 ? 164 GLU   W CD  1 
ATOM   40657 O  OE1 . GLU   W  9  165 ? -16.306 -159.674 9.802   1.00 110.65 ? 164 GLU   W OE1 1 
ATOM   40658 O  OE2 . GLU   W  9  165 ? -15.011 -158.193 10.789  1.00 108.30 ? 164 GLU   W OE2 1 
ATOM   40659 N  N   . THR   W  9  166 ? -13.437 -159.666 15.738  1.00 104.51 ? 165 THR   W N   1 
ATOM   40660 C  CA  . THR   W  9  166 ? -12.797 -159.177 16.988  1.00 100.63 ? 165 THR   W CA  1 
ATOM   40661 C  C   . THR   W  9  166 ? -11.283 -159.404 16.912  1.00 99.72  ? 165 THR   W C   1 
ATOM   40662 O  O   . THR   W  9  166 ? -10.540 -158.436 17.142  1.00 98.39  ? 165 THR   W O   1 
ATOM   40663 C  CB  . THR   W  9  166 ? -13.413 -159.830 18.232  1.00 101.24 ? 165 THR   W CB  1 
ATOM   40664 O  OG1 . THR   W  9  166 ? -14.825 -159.627 18.172  1.00 100.53 ? 165 THR   W OG1 1 
ATOM   40665 C  CG2 . THR   W  9  166 ? -12.870 -159.263 19.526  1.00 100.70 ? 165 THR   W CG2 1 
ATOM   40666 N  N   . ILE   W  9  167 ? -10.841 -160.624 16.600  1.00 99.94  ? 166 ILE   W N   1 
ATOM   40667 C  CA  . ILE   W  9  167 ? -9.390  -160.989 16.590  1.00 100.62 ? 166 ILE   W CA  1 
ATOM   40668 C  C   . ILE   W  9  167 ? -8.677  -160.214 15.474  1.00 99.02  ? 166 ILE   W C   1 
ATOM   40669 O  O   . ILE   W  9  167 ? -7.510  -159.831 15.680  1.00 97.15  ? 166 ILE   W O   1 
ATOM   40670 C  CB  . ILE   W  9  167 ? -9.164  -162.514 16.473  1.00 100.17 ? 166 ILE   W CB  1 
ATOM   40671 C  CG1 . ILE   W  9  167 ? -7.706  -162.873 16.773  1.00 99.02  ? 166 ILE   W CG1 1 
ATOM   40672 C  CG2 . ILE   W  9  167 ? -9.604  -163.049 15.117  1.00 102.02 ? 166 ILE   W CG2 1 
ATOM   40673 C  CD1 . ILE   W  9  167 ? -7.479  -164.326 17.104  1.00 98.82  ? 166 ILE   W CD1 1 
ATOM   40674 N  N   . SER   W  9  168 ? -9.348  -159.993 14.339  1.00 100.73 ? 167 SER   W N   1 
ATOM   40675 C  CA  . SER   W  9  168 ? -8.790  -159.272 13.165  1.00 102.19 ? 167 SER   W CA  1 
ATOM   40676 C  C   . SER   W  9  168 ? -8.550  -157.803 13.525  1.00 106.08 ? 167 SER   W C   1 
ATOM   40677 O  O   . SER   W  9  168 ? -7.448  -157.295 13.231  1.00 107.55 ? 167 SER   W O   1 
ATOM   40678 C  CB  . SER   W  9  168 ? -9.688  -159.387 11.968  1.00 102.51 ? 167 SER   W CB  1 
ATOM   40679 O  OG  . SER   W  9  168 ? -9.850  -160.741 11.579  1.00 99.76  ? 167 SER   W OG  1 
ATOM   40680 N  N   . GLN   W  9  169 ? -9.549  -157.159 14.139  1.00 107.04 ? 168 GLN   W N   1 
ATOM   40681 C  CA  . GLN   W  9  169 ? -9.496  -155.735 14.567  1.00 106.76 ? 168 GLN   W CA  1 
ATOM   40682 C  C   . GLN   W  9  169 ? -8.479  -155.578 15.706  1.00 103.56 ? 168 GLN   W C   1 
ATOM   40683 O  O   . GLN   W  9  169 ? -7.903  -154.480 15.822  1.00 103.91 ? 168 GLN   W O   1 
ATOM   40684 C  CB  . GLN   W  9  169 ? -10.890 -155.237 14.963  1.00 106.05 ? 168 GLN   W CB  1 
ATOM   40685 C  CG  . GLN   W  9  169 ? -11.836 -155.065 13.781  1.00 106.67 ? 168 GLN   W CG  1 
ATOM   40686 C  CD  . GLN   W  9  169 ? -11.376 -153.988 12.829  1.00 107.13 ? 168 GLN   W CD  1 
ATOM   40687 O  OE1 . GLN   W  9  169 ? -11.003 -152.892 13.241  1.00 107.82 ? 168 GLN   W OE1 1 
ATOM   40688 N  NE2 . GLN   W  9  169 ? -11.397 -154.291 11.540  1.00 103.37 ? 168 GLN   W NE2 1 
ATOM   40689 N  N   . ALA   W  9  170 ? -8.246  -156.629 16.499  1.00 99.97  ? 169 ALA   W N   1 
ATOM   40690 C  CA  . ALA   W  9  170 ? -7.232  -156.645 17.580  1.00 98.30  ? 169 ALA   W CA  1 
ATOM   40691 C  C   . ALA   W  9  170 ? -5.830  -156.583 16.964  1.00 98.13  ? 169 ALA   W C   1 
ATOM   40692 O  O   . ALA   W  9  170 ? -5.029  -155.743 17.410  1.00 98.61  ? 169 ALA   W O   1 
ATOM   40693 C  CB  . ALA   W  9  170 ? -7.397  -157.866 18.450  1.00 97.55  ? 169 ALA   W CB  1 
ATOM   40694 N  N   . LEU   W  9  171 ? -5.554  -157.438 15.973  1.00 99.94  ? 170 LEU   W N   1 
ATOM   40695 C  CA  . LEU   W  9  171 ? -4.220  -157.573 15.323  1.00 98.98  ? 170 LEU   W CA  1 
ATOM   40696 C  C   . LEU   W  9  171 ? -3.915  -156.320 14.491  1.00 97.67  ? 170 LEU   W C   1 
ATOM   40697 O  O   . LEU   W  9  171 ? -2.835  -155.731 14.693  1.00 94.02  ? 170 LEU   W O   1 
ATOM   40698 C  CB  . LEU   W  9  171 ? -4.197  -158.836 14.452  1.00 97.98  ? 170 LEU   W CB  1 
ATOM   40699 C  CG  . LEU   W  9  171 ? -2.838  -159.186 13.841  1.00 95.85  ? 170 LEU   W CG  1 
ATOM   40700 C  CD1 . LEU   W  9  171 ? -2.635  -160.689 13.774  1.00 95.08  ? 170 LEU   W CD1 1 
ATOM   40701 C  CD2 . LEU   W  9  171 ? -2.671  -158.575 12.459  1.00 98.35  ? 170 LEU   W CD2 1 
ATOM   40702 N  N   . LEU   W  9  172 ? -4.824  -155.954 13.581  1.00 99.83  ? 171 LEU   W N   1 
ATOM   40703 C  CA  . LEU   W  9  172 ? -4.644  -154.853 12.591  1.00 101.89 ? 171 LEU   W CA  1 
ATOM   40704 C  C   . LEU   W  9  172 ? -4.265  -153.546 13.303  1.00 103.07 ? 171 LEU   W C   1 
ATOM   40705 O  O   . LEU   W  9  172 ? -3.248  -152.938 12.910  1.00 103.92 ? 171 LEU   W O   1 
ATOM   40706 C  CB  . LEU   W  9  172 ? -5.935  -154.681 11.779  1.00 103.46 ? 171 LEU   W CB  1 
ATOM   40707 C  CG  . LEU   W  9  172 ? -5.949  -155.257 10.359  1.00 99.58  ? 171 LEU   W CG  1 
ATOM   40708 C  CD1 . LEU   W  9  172 ? -5.046  -156.472 10.210  1.00 99.33  ? 171 LEU   W CD1 1 
ATOM   40709 C  CD2 . LEU   W  9  172 ? -7.368  -155.607 9.942   1.00 99.14  ? 171 LEU   W CD2 1 
ATOM   40710 N  N   . ASN   W  9  173 ? -5.049  -153.136 14.306  1.00 103.62 ? 172 ASN   W N   1 
ATOM   40711 C  CA  . ASN   W  9  173 ? -4.902  -151.828 15.003  1.00 101.09 ? 172 ASN   W CA  1 
ATOM   40712 C  C   . ASN   W  9  173 ? -3.664  -151.850 15.909  1.00 100.58 ? 172 ASN   W C   1 
ATOM   40713 O  O   . ASN   W  9  173 ? -3.077  -150.776 16.126  1.00 101.92 ? 172 ASN   W O   1 
ATOM   40714 C  CB  . ASN   W  9  173 ? -6.175  -151.452 15.765  1.00 102.16 ? 172 ASN   W CB  1 
ATOM   40715 C  CG  . ASN   W  9  173 ? -7.324  -151.137 14.832  1.00 102.23 ? 172 ASN   W CG  1 
ATOM   40716 O  OD1 . ASN   W  9  173 ? -7.415  -150.027 14.312  1.00 101.68 ? 172 ASN   W OD1 1 
ATOM   40717 N  ND2 . ASN   W  9  173 ? -8.192  -152.107 14.599  1.00 102.41 ? 172 ASN   W ND2 1 
ATOM   40718 N  N   . ALA   W  9  174 ? -3.276  -153.022 16.411  1.00 97.46  ? 173 ALA   W N   1 
ATOM   40719 C  CA  . ALA   W  9  174 ? -2.042  -153.215 17.207  1.00 99.41  ? 173 ALA   W CA  1 
ATOM   40720 C  C   . ALA   W  9  174 ? -0.820  -153.095 16.286  1.00 102.41 ? 173 ALA   W C   1 
ATOM   40721 O  O   . ALA   W  9  174 ? 0.138   -152.390 16.663  1.00 105.18 ? 173 ALA   W O   1 
ATOM   40722 C  CB  . ALA   W  9  174 ? -2.079  -154.547 17.916  1.00 100.11 ? 173 ALA   W CB  1 
ATOM   40723 N  N   . ALA   W  9  175 ? -0.869  -153.754 15.122  1.00 101.99 ? 174 ALA   W N   1 
ATOM   40724 C  CA  . ALA   W  9  175 ? 0.224   -153.837 14.121  1.00 101.94 ? 174 ALA   W CA  1 
ATOM   40725 C  C   . ALA   W  9  175 ? 0.545   -152.451 13.542  1.00 102.32 ? 174 ALA   W C   1 
ATOM   40726 O  O   . ALA   W  9  175 ? 1.710   -152.219 13.153  1.00 94.86  ? 174 ALA   W O   1 
ATOM   40727 C  CB  . ALA   W  9  175 ? -0.163  -154.801 13.026  1.00 101.33 ? 174 ALA   W CB  1 
ATOM   40728 N  N   . ASP   W  9  176 ? -0.453  -151.569 13.469  1.00 103.87 ? 175 ASP   W N   1 
ATOM   40729 C  CA  . ASP   W  9  176 ? -0.320  -150.226 12.845  1.00 106.83 ? 175 ASP   W CA  1 
ATOM   40730 C  C   . ASP   W  9  176 ? 0.304   -149.241 13.839  1.00 106.69 ? 175 ASP   W C   1 
ATOM   40731 O  O   . ASP   W  9  176 ? 0.723   -148.162 13.382  1.00 110.67 ? 175 ASP   W O   1 
ATOM   40732 C  CB  . ASP   W  9  176 ? -1.665  -149.740 12.303  1.00 111.94 ? 175 ASP   W CB  1 
ATOM   40733 C  CG  . ASP   W  9  176 ? -2.130  -150.524 11.085  1.00 113.48 ? 175 ASP   W CG  1 
ATOM   40734 O  OD1 . ASP   W  9  176 ? -1.348  -151.366 10.588  1.00 108.60 ? 175 ASP   W OD1 1 
ATOM   40735 O  OD2 . ASP   W  9  176 ? -3.269  -150.288 10.641  1.00 119.98 ? 175 ASP   W OD2 1 
ATOM   40736 N  N   . ARG   W  9  177 ? 0.378   -149.596 15.127  1.00 106.85 ? 176 ARG   W N   1 
ATOM   40737 C  CA  . ARG   W  9  177 ? 1.063   -148.784 16.170  1.00 107.28 ? 176 ARG   W CA  1 
ATOM   40738 C  C   . ARG   W  9  177 ? 2.455   -149.366 16.453  1.00 106.84 ? 176 ARG   W C   1 
ATOM   40739 O  O   . ARG   W  9  177 ? 3.124   -148.852 17.375  1.00 107.12 ? 176 ARG   W O   1 
ATOM   40740 C  CB  . ARG   W  9  177 ? 0.211   -148.692 17.443  1.00 107.75 ? 176 ARG   W CB  1 
ATOM   40741 C  CG  . ARG   W  9  177 ? -0.845  -147.596 17.406  1.00 109.41 ? 176 ARG   W CG  1 
ATOM   40742 C  CD  . ARG   W  9  177 ? -0.246  -146.201 17.482  1.00 110.37 ? 176 ARG   W CD  1 
ATOM   40743 N  NE  . ARG   W  9  177 ? -1.216  -145.169 17.149  1.00 112.68 ? 176 ARG   W NE  1 
ATOM   40744 C  CZ  . ARG   W  9  177 ? -0.962  -143.864 17.108  1.00 115.78 ? 176 ARG   W CZ  1 
ATOM   40745 N  NH1 . ARG   W  9  177 ? 0.246   -143.407 17.388  1.00 116.41 ? 176 ARG   W NH1 1 
ATOM   40746 N  NH2 . ARG   W  9  177 ? -1.922  -143.012 16.787  1.00 119.33 ? 176 ARG   W NH2 1 
ATOM   40747 N  N   . ASP   W  9  178 ? 2.886   -150.376 15.685  1.00 104.71 ? 177 ASP   W N   1 
ATOM   40748 C  CA  . ASP   W  9  178 ? 4.241   -150.983 15.792  1.00 103.54 ? 177 ASP   W CA  1 
ATOM   40749 C  C   . ASP   W  9  178 ? 4.952   -150.895 14.439  1.00 100.29 ? 177 ASP   W C   1 
ATOM   40750 O  O   . ASP   W  9  178 ? 4.375   -151.351 13.425  1.00 95.39  ? 177 ASP   W O   1 
ATOM   40751 C  CB  . ASP   W  9  178 ? 4.179   -152.430 16.282  1.00 105.80 ? 177 ASP   W CB  1 
ATOM   40752 C  CG  . ASP   W  9  178 ? 5.541   -153.038 16.596  1.00 110.41 ? 177 ASP   W CG  1 
ATOM   40753 O  OD1 . ASP   W  9  178 ? 6.494   -152.268 16.846  1.00 113.05 ? 177 ASP   W OD1 1 
ATOM   40754 O  OD2 . ASP   W  9  178 ? 5.640   -154.280 16.592  1.00 107.29 ? 177 ASP   W OD2 1 
ATOM   40755 N  N   . ALA   W  9  179 ? 6.168   -150.342 14.447  1.00 100.58 ? 178 ALA   W N   1 
ATOM   40756 C  CA  . ALA   W  9  179 ? 7.036   -150.148 13.263  1.00 101.02 ? 178 ALA   W CA  1 
ATOM   40757 C  C   . ALA   W  9  179 ? 7.448   -151.508 12.692  1.00 97.19  ? 178 ALA   W C   1 
ATOM   40758 O  O   . ALA   W  9  179 ? 7.535   -151.617 11.458  1.00 95.19  ? 178 ALA   W O   1 
ATOM   40759 C  CB  . ALA   W  9  179 ? 8.244   -149.323 13.639  1.00 103.31 ? 178 ALA   W CB  1 
ATOM   40760 N  N   . LEU   W  9  180 ? 7.675   -152.501 13.558  1.00 97.15  ? 179 LEU   W N   1 
ATOM   40761 C  CA  . LEU   W  9  180 ? 8.274   -153.813 13.189  1.00 99.83  ? 179 LEU   W CA  1 
ATOM   40762 C  C   . LEU   W  9  180 ? 7.198   -154.860 12.860  1.00 101.75 ? 179 LEU   W C   1 
ATOM   40763 O  O   . LEU   W  9  180 ? 7.582   -155.932 12.353  1.00 103.14 ? 179 LEU   W O   1 
ATOM   40764 C  CB  . LEU   W  9  180 ? 9.164   -154.298 14.338  1.00 101.83 ? 179 LEU   W CB  1 
ATOM   40765 C  CG  . LEU   W  9  180 ? 10.337  -153.394 14.713  1.00 104.30 ? 179 LEU   W CG  1 
ATOM   40766 C  CD1 . LEU   W  9  180 ? 11.239  -154.090 15.721  1.00 108.72 ? 179 LEU   W CD1 1 
ATOM   40767 C  CD2 . LEU   W  9  180 ? 11.141  -152.980 13.488  1.00 103.58 ? 179 LEU   W CD2 1 
ATOM   40768 N  N   . SER   W  9  181 ? 5.917   -154.592 13.137  1.00 103.83 ? 180 SER   W N   1 
ATOM   40769 C  CA  . SER   W  9  181 ? 4.793   -155.524 12.844  1.00 102.00 ? 180 SER   W CA  1 
ATOM   40770 C  C   . SER   W  9  181 ? 4.004   -155.033 11.625  1.00 101.93 ? 180 SER   W C   1 
ATOM   40771 O  O   . SER   W  9  181 ? 4.093   -153.830 11.301  1.00 99.72  ? 180 SER   W O   1 
ATOM   40772 C  CB  . SER   W  9  181 ? 3.895   -155.708 14.042  1.00 104.67 ? 180 SER   W CB  1 
ATOM   40773 O  OG  . SER   W  9  181 ? 4.599   -156.334 15.106  1.00 106.30 ? 180 SER   W OG  1 
ATOM   40774 N  N   . GLY   W  9  182 ? 3.280   -155.951 10.974  1.00 98.86  ? 181 GLY   W N   1 
ATOM   40775 C  CA  . GLY   W  9  182 ? 2.320   -155.665 9.888   1.00 99.66  ? 181 GLY   W CA  1 
ATOM   40776 C  C   . GLY   W  9  182 ? 2.716   -156.324 8.575   1.00 101.17 ? 181 GLY   W C   1 
ATOM   40777 O  O   . GLY   W  9  182 ? 3.083   -157.513 8.602   1.00 100.65 ? 181 GLY   W O   1 
ATOM   40778 N  N   . TRP   W  9  183 ? 2.624   -155.579 7.466   1.00 99.46  ? 182 TRP   W N   1 
ATOM   40779 C  CA  . TRP   W  9  183 ? 3.006   -155.998 6.086   1.00 101.06 ? 182 TRP   W CA  1 
ATOM   40780 C  C   . TRP   W  9  183 ? 2.146   -157.173 5.599   1.00 102.64 ? 182 TRP   W C   1 
ATOM   40781 O  O   . TRP   W  9  183 ? 2.632   -157.956 4.756   1.00 105.82 ? 182 TRP   W O   1 
ATOM   40782 C  CB  . TRP   W  9  183 ? 4.507   -156.317 6.026   1.00 98.57  ? 182 TRP   W CB  1 
ATOM   40783 C  CG  . TRP   W  9  183 ? 5.304   -155.308 5.262   1.00 99.73  ? 182 TRP   W CG  1 
ATOM   40784 C  CD1 . TRP   W  9  183 ? 5.013   -153.986 5.101   1.00 99.98  ? 182 TRP   W CD1 1 
ATOM   40785 C  CD2 . TRP   W  9  183 ? 6.545   -155.532 4.573   1.00 98.51  ? 182 TRP   W CD2 1 
ATOM   40786 N  NE1 . TRP   W  9  183 ? 5.978   -153.376 4.348   1.00 101.34 ? 182 TRP   W NE1 1 
ATOM   40787 C  CE2 . TRP   W  9  183 ? 6.933   -154.298 4.011   1.00 99.57  ? 182 TRP   W CE2 1 
ATOM   40788 C  CE3 . TRP   W  9  183 ? 7.366   -156.647 4.377   1.00 97.77  ? 182 TRP   W CE3 1 
ATOM   40789 C  CZ2 . TRP   W  9  183 ? 8.101   -154.154 3.265   1.00 100.42 ? 182 TRP   W CZ2 1 
ATOM   40790 C  CZ3 . TRP   W  9  183 ? 8.519   -156.505 3.637   1.00 98.55  ? 182 TRP   W CZ3 1 
ATOM   40791 C  CH2 . TRP   W  9  183 ? 8.879   -155.275 3.091   1.00 99.16  ? 182 TRP   W CH2 1 
ATOM   40792 N  N   . GLY   W  9  184 ? 0.897   -157.256 6.066   1.00 105.46 ? 183 GLY   W N   1 
ATOM   40793 C  CA  . GLY   W  9  184 ? -0.029  -158.370 5.785   1.00 107.87 ? 183 GLY   W CA  1 
ATOM   40794 C  C   . GLY   W  9  184 ? -0.361  -159.137 7.052   1.00 106.14 ? 183 GLY   W C   1 
ATOM   40795 O  O   . GLY   W  9  184 ? 0.367   -158.968 8.051   1.00 108.39 ? 183 GLY   W O   1 
ATOM   40796 N  N   . ALA   W  9  185 ? -1.414  -159.956 7.018   1.00 104.64 ? 184 ALA   W N   1 
ATOM   40797 C  CA  . ALA   W  9  185 ? -1.924  -160.713 8.185   1.00 101.96 ? 184 ALA   W CA  1 
ATOM   40798 C  C   . ALA   W  9  185 ? -2.652  -161.977 7.718   1.00 100.95 ? 184 ALA   W C   1 
ATOM   40799 O  O   . ALA   W  9  185 ? -3.147  -161.992 6.572   1.00 100.76 ? 184 ALA   W O   1 
ATOM   40800 C  CB  . ALA   W  9  185 ? -2.827  -159.829 9.012   1.00 101.32 ? 184 ALA   W CB  1 
ATOM   40801 N  N   . VAL   W  9  186 ? -2.691  -162.994 8.583   1.00 98.87  ? 185 VAL   W N   1 
ATOM   40802 C  CA  . VAL   W  9  186 ? -3.444  -164.268 8.384   1.00 97.92  ? 185 VAL   W CA  1 
ATOM   40803 C  C   . VAL   W  9  186 ? -4.224  -164.571 9.664   1.00 94.24  ? 185 VAL   W C   1 
ATOM   40804 O  O   . VAL   W  9  186 ? -3.616  -164.509 10.749  1.00 89.53  ? 185 VAL   W O   1 
ATOM   40805 C  CB  . VAL   W  9  186 ? -2.508  -165.437 8.027   1.00 98.60  ? 185 VAL   W CB  1 
ATOM   40806 C  CG1 . VAL   W  9  186 ? -3.254  -166.762 7.980   1.00 98.74  ? 185 VAL   W CG1 1 
ATOM   40807 C  CG2 . VAL   W  9  186 ? -1.781  -165.189 6.717   1.00 102.20 ? 185 VAL   W CG2 1 
ATOM   40808 N  N   . VAL   W  9  187 ? -5.508  -164.906 9.527   1.00 94.14  ? 186 VAL   W N   1 
ATOM   40809 C  CA  . VAL   W  9  187 ? -6.381  -165.347 10.652  1.00 96.84  ? 186 VAL   W CA  1 
ATOM   40810 C  C   . VAL   W  9  187 ? -6.838  -166.782 10.378  1.00 99.05  ? 186 VAL   W C   1 
ATOM   40811 O  O   . VAL   W  9  187 ? -7.320  -167.055 9.259   1.00 100.77 ? 186 VAL   W O   1 
ATOM   40812 C  CB  . VAL   W  9  187 ? -7.582  -164.406 10.851  1.00 98.23  ? 186 VAL   W CB  1 
ATOM   40813 C  CG1 . VAL   W  9  187 ? -8.459  -164.850 12.013  1.00 99.22  ? 186 VAL   W CG1 1 
ATOM   40814 C  CG2 . VAL   W  9  187 ? -7.137  -162.967 11.043  1.00 98.74  ? 186 VAL   W CG2 1 
ATOM   40815 N  N   . TYR   W  9  188 ? -6.685  -167.652 11.378  1.00 98.92  ? 187 TYR   W N   1 
ATOM   40816 C  CA  . TYR   W  9  188 ? -7.213  -169.037 11.398  1.00 100.90 ? 187 TYR   W CA  1 
ATOM   40817 C  C   . TYR   W  9  188 ? -8.437  -169.069 12.315  1.00 103.55 ? 187 TYR   W C   1 
ATOM   40818 O  O   . TYR   W  9  188 ? -8.282  -168.740 13.507  1.00 99.83  ? 187 TYR   W O   1 
ATOM   40819 C  CB  . TYR   W  9  188 ? -6.151  -170.020 11.897  1.00 99.76  ? 187 TYR   W CB  1 
ATOM   40820 C  CG  . TYR   W  9  188 ? -5.026  -170.304 10.933  1.00 98.92  ? 187 TYR   W CG  1 
ATOM   40821 C  CD1 . TYR   W  9  188 ? -3.915  -169.478 10.864  1.00 97.18  ? 187 TYR   W CD1 1 
ATOM   40822 C  CD2 . TYR   W  9  188 ? -5.058  -171.418 10.108  1.00 97.50  ? 187 TYR   W CD2 1 
ATOM   40823 C  CE1 . TYR   W  9  188 ? -2.871  -169.743 9.992   1.00 96.62  ? 187 TYR   W CE1 1 
ATOM   40824 C  CE2 . TYR   W  9  188 ? -4.024  -171.696 9.230   1.00 97.02  ? 187 TYR   W CE2 1 
ATOM   40825 C  CZ  . TYR   W  9  188 ? -2.927  -170.856 9.171   1.00 95.89  ? 187 TYR   W CZ  1 
ATOM   40826 O  OH  . TYR   W  9  188 ? -1.906  -171.126 8.308   1.00 100.75 ? 187 TYR   W OH  1 
ATOM   40827 N  N   . ILE   W  9  189 ? -9.604  -169.420 11.767  1.00 109.48 ? 188 ILE   W N   1 
ATOM   40828 C  CA  . ILE   W  9  189 ? -10.826 -169.785 12.544  1.00 108.85 ? 188 ILE   W CA  1 
ATOM   40829 C  C   . ILE   W  9  189 ? -10.894 -171.315 12.611  1.00 109.17 ? 188 ILE   W C   1 
ATOM   40830 O  O   . ILE   W  9  189 ? -10.882 -171.953 11.540  1.00 104.91 ? 188 ILE   W O   1 
ATOM   40831 C  CB  . ILE   W  9  189 ? -12.097 -169.166 11.925  1.00 115.66 ? 188 ILE   W CB  1 
ATOM   40832 C  CG1 . ILE   W  9  189 ? -11.985 -167.644 11.801  1.00 114.01 ? 188 ILE   W CG1 1 
ATOM   40833 C  CG2 . ILE   W  9  189 ? -13.340 -169.579 12.704  1.00 119.87 ? 188 ILE   W CG2 1 
ATOM   40834 C  CD1 . ILE   W  9  189 ? -11.773 -166.925 13.115  1.00 113.04 ? 188 ILE   W CD1 1 
ATOM   40835 N  N   . ILE   W  9  190 ? -10.954 -171.866 13.827  1.00 105.12 ? 189 ILE   W N   1 
ATOM   40836 C  CA  . ILE   W  9  190 ? -10.863 -173.330 14.104  1.00 106.46 ? 189 ILE   W CA  1 
ATOM   40837 C  C   . ILE   W  9  190 ? -12.147 -173.784 14.806  1.00 110.34 ? 189 ILE   W C   1 
ATOM   40838 O  O   . ILE   W  9  190 ? -12.418 -173.289 15.922  1.00 106.87 ? 189 ILE   W O   1 
ATOM   40839 C  CB  . ILE   W  9  190 ? -9.614  -173.652 14.946  1.00 101.49 ? 189 ILE   W CB  1 
ATOM   40840 C  CG1 . ILE   W  9  190 ? -8.336  -173.083 14.323  1.00 98.72  ? 189 ILE   W CG1 1 
ATOM   40841 C  CG2 . ILE   W  9  190 ? -9.495  -175.148 15.184  1.00 102.69 ? 189 ILE   W CG2 1 
ATOM   40842 C  CD1 . ILE   W  9  190 ? -7.191  -172.950 15.298  1.00 97.07  ? 189 ILE   W CD1 1 
ATOM   40843 N  N   . LYS   W  9  191 ? -12.892 -174.691 14.164  1.00 116.33 ? 190 LYS   W N   1 
ATOM   40844 C  CA  . LYS   W  9  191 ? -14.071 -175.399 14.730  1.00 120.44 ? 190 LYS   W CA  1 
ATOM   40845 C  C   . LYS   W  9  191 ? -13.685 -176.871 14.911  1.00 124.22 ? 190 LYS   W C   1 
ATOM   40846 O  O   . LYS   W  9  191 ? -12.556 -177.229 14.518  1.00 118.55 ? 190 LYS   W O   1 
ATOM   40847 C  CB  . LYS   W  9  191 ? -15.287 -175.199 13.819  1.00 121.99 ? 190 LYS   W CB  1 
ATOM   40848 C  CG  . LYS   W  9  191 ? -15.659 -173.744 13.565  1.00 120.86 ? 190 LYS   W CG  1 
ATOM   40849 C  CD  . LYS   W  9  191 ? -16.727 -173.566 12.513  1.00 124.16 ? 190 LYS   W CD  1 
ATOM   40850 C  CE  . LYS   W  9  191 ? -18.104 -173.950 13.005  1.00 127.11 ? 190 LYS   W CE  1 
ATOM   40851 N  NZ  . LYS   W  9  191 ? -19.133 -173.742 11.960  1.00 131.11 ? 190 LYS   W NZ  1 
ATOM   40852 N  N   . LYS   W  9  192 ? -14.578 -177.685 15.486  1.00 134.06 ? 191 LYS   W N   1 
ATOM   40853 C  CA  . LYS   W  9  192 ? -14.274 -179.075 15.933  1.00 139.68 ? 191 LYS   W CA  1 
ATOM   40854 C  C   . LYS   W  9  192 ? -13.722 -179.909 14.765  1.00 138.95 ? 191 LYS   W C   1 
ATOM   40855 O  O   . LYS   W  9  192 ? -12.801 -180.713 15.015  1.00 138.35 ? 191 LYS   W O   1 
ATOM   40856 C  CB  . LYS   W  9  192 ? -15.503 -179.753 16.548  1.00 144.49 ? 191 LYS   W CB  1 
ATOM   40857 C  CG  . LYS   W  9  192 ? -15.180 -180.956 17.427  1.00 146.77 ? 191 LYS   W CG  1 
ATOM   40858 C  CD  . LYS   W  9  192 ? -15.947 -182.211 17.055  1.00 149.08 ? 191 LYS   W CD  1 
ATOM   40859 C  CE  . LYS   W  9  192 ? -15.586 -183.438 17.872  1.00 151.95 ? 191 LYS   W CE  1 
ATOM   40860 N  NZ  . LYS   W  9  192 ? -14.197 -183.410 18.392  1.00 150.75 ? 191 LYS   W NZ  1 
ATOM   40861 N  N   . ASP   W  9  193 ? -14.253 -179.735 13.547  1.00 139.10 ? 192 ASP   W N   1 
ATOM   40862 C  CA  . ASP   W  9  193 ? -13.797 -180.482 12.341  1.00 140.46 ? 192 ASP   W CA  1 
ATOM   40863 C  C   . ASP   W  9  193 ? -13.992 -179.643 11.069  1.00 134.19 ? 192 ASP   W C   1 
ATOM   40864 O  O   . ASP   W  9  193 ? -14.433 -180.207 10.049  1.00 133.98 ? 192 ASP   W O   1 
ATOM   40865 C  CB  . ASP   W  9  193 ? -14.483 -181.850 12.255  1.00 146.43 ? 192 ASP   W CB  1 
ATOM   40866 C  CG  . ASP   W  9  193 ? -15.884 -181.882 12.842  1.00 155.36 ? 192 ASP   W CG  1 
ATOM   40867 O  OD1 . ASP   W  9  193 ? -16.598 -180.866 12.714  1.00 156.87 ? 192 ASP   W OD1 1 
ATOM   40868 O  OD2 . ASP   W  9  193 ? -16.245 -182.920 13.431  1.00 165.99 ? 192 ASP   W OD2 1 
ATOM   40869 N  N   . GLU   W  9  194 ? -13.663 -178.350 11.122  1.00 130.50 ? 193 GLU   W N   1 
ATOM   40870 C  CA  . GLU   W  9  194 ? -13.335 -177.526 9.925   1.00 129.84 ? 193 GLU   W CA  1 
ATOM   40871 C  C   . GLU   W  9  194 ? -12.501 -176.322 10.378  1.00 124.46 ? 193 GLU   W C   1 
ATOM   40872 O  O   . GLU   W  9  194 ? -12.781 -175.777 11.468  1.00 123.66 ? 193 GLU   W O   1 
ATOM   40873 C  CB  . GLU   W  9  194 ? -14.592 -177.129 9.141   1.00 135.35 ? 193 GLU   W CB  1 
ATOM   40874 C  CG  . GLU   W  9  194 ? -15.201 -175.788 9.525   1.00 139.31 ? 193 GLU   W CG  1 
ATOM   40875 C  CD  . GLU   W  9  194 ? -16.062 -175.158 8.443   1.00 147.47 ? 193 GLU   W CD  1 
ATOM   40876 O  OE1 . GLU   W  9  194 ? -15.677 -175.238 7.257   1.00 153.55 ? 193 GLU   W OE1 1 
ATOM   40877 O  OE2 . GLU   W  9  194 ? -17.113 -174.582 8.787   1.00 158.99 ? 193 GLU   W OE2 1 
ATOM   40878 N  N   . VAL   W  9  195 ? -11.493 -175.957 9.582   1.00 120.27 ? 194 VAL   W N   1 
ATOM   40879 C  CA  . VAL   W  9  195 ? -10.598 -174.787 9.823   1.00 117.30 ? 194 VAL   W CA  1 
ATOM   40880 C  C   . VAL   W  9  195 ? -10.624 -173.900 8.576   1.00 117.62 ? 194 VAL   W C   1 
ATOM   40881 O  O   . VAL   W  9  195 ? -10.394 -174.432 7.470   1.00 118.43 ? 194 VAL   W O   1 
ATOM   40882 C  CB  . VAL   W  9  195 ? -9.163  -175.230 10.166  1.00 114.36 ? 194 VAL   W CB  1 
ATOM   40883 C  CG1 . VAL   W  9  195 ? -8.239  -174.039 10.374  1.00 115.47 ? 194 VAL   W CG1 1 
ATOM   40884 C  CG2 . VAL   W  9  195 ? -9.131  -176.146 11.379  1.00 111.78 ? 194 VAL   W CG2 1 
ATOM   40885 N  N   . VAL   W  9  196 ? -10.891 -172.603 8.760   1.00 114.68 ? 195 VAL   W N   1 
ATOM   40886 C  CA  . VAL   W  9  196 ? -10.913 -171.577 7.676   1.00 115.08 ? 195 VAL   W CA  1 
ATOM   40887 C  C   . VAL   W  9  196 ? -9.758  -170.598 7.910   1.00 112.67 ? 195 VAL   W C   1 
ATOM   40888 O  O   . VAL   W  9  196 ? -9.671  -170.034 9.021   1.00 112.21 ? 195 VAL   W O   1 
ATOM   40889 C  CB  . VAL   W  9  196 ? -12.266 -170.843 7.613   1.00 117.32 ? 195 VAL   W CB  1 
ATOM   40890 C  CG1 . VAL   W  9  196 ? -12.331 -169.900 6.420   1.00 118.50 ? 195 VAL   W CG1 1 
ATOM   40891 C  CG2 . VAL   W  9  196 ? -13.436 -171.815 7.590   1.00 118.80 ? 195 VAL   W CG2 1 
ATOM   40892 N  N   . LYS   W  9  197 ? -8.919  -170.409 6.889   1.00 111.27 ? 196 LYS   W N   1 
ATOM   40893 C  CA  . LYS   W  9  197 ? -7.731  -169.517 6.903   1.00 111.21 ? 196 LYS   W CA  1 
ATOM   40894 C  C   . LYS   W  9  197 ? -8.011  -168.316 5.997   1.00 110.61 ? 196 LYS   W C   1 
ATOM   40895 O  O   . LYS   W  9  197 ? -8.227  -168.532 4.789   1.00 109.62 ? 196 LYS   W O   1 
ATOM   40896 C  CB  . LYS   W  9  197 ? -6.501  -170.290 6.421   1.00 112.53 ? 196 LYS   W CB  1 
ATOM   40897 C  CG  . LYS   W  9  197 ? -5.204  -169.499 6.338   1.00 113.22 ? 196 LYS   W CG  1 
ATOM   40898 C  CD  . LYS   W  9  197 ? -4.081  -170.310 5.738   1.00 116.29 ? 196 LYS   W CD  1 
ATOM   40899 C  CE  . LYS   W  9  197 ? -2.785  -169.542 5.607   1.00 116.41 ? 196 LYS   W CE  1 
ATOM   40900 N  NZ  . LYS   W  9  197 ? -1.740  -170.359 4.947   1.00 117.74 ? 196 LYS   W NZ  1 
ATOM   40901 N  N   . ARG   W  9  198 ? -8.004  -167.105 6.560   1.00 108.94 ? 197 ARG   W N   1 
ATOM   40902 C  CA  . ARG   W  9  198 ? -8.274  -165.850 5.813   1.00 110.45 ? 197 ARG   W CA  1 
ATOM   40903 C  C   . ARG   W  9  198 ? -7.046  -164.939 5.878   1.00 108.49 ? 197 ARG   W C   1 
ATOM   40904 O  O   . ARG   W  9  198 ? -6.448  -164.830 6.967   1.00 106.29 ? 197 ARG   W O   1 
ATOM   40905 C  CB  . ARG   W  9  198 ? -9.514  -165.154 6.378   1.00 110.60 ? 197 ARG   W CB  1 
ATOM   40906 C  CG  . ARG   W  9  198 ? -10.786 -165.982 6.272   1.00 115.64 ? 197 ARG   W CG  1 
ATOM   40907 C  CD  . ARG   W  9  198 ? -12.033 -165.119 6.342   1.00 117.41 ? 197 ARG   W CD  1 
ATOM   40908 N  NE  . ARG   W  9  198 ? -13.271 -165.889 6.383   1.00 119.52 ? 197 ARG   W NE  1 
ATOM   40909 C  CZ  . ARG   W  9  198 ? -13.780 -166.470 7.468   1.00 121.18 ? 197 ARG   W CZ  1 
ATOM   40910 N  NH1 . ARG   W  9  198 ? -13.157 -166.389 8.633   1.00 121.91 ? 197 ARG   W NH1 1 
ATOM   40911 N  NH2 . ARG   W  9  198 ? -14.917 -167.140 7.383   1.00 119.32 ? 197 ARG   W NH2 1 
ATOM   40912 N  N   . TYR   W  9  199 ? -6.688  -164.333 4.740   1.00 109.54 ? 198 TYR   W N   1 
ATOM   40913 C  CA  . TYR   W  9  199 ? -5.674  -163.252 4.616   1.00 110.84 ? 198 TYR   W CA  1 
ATOM   40914 C  C   . TYR   W  9  199 ? -6.390  -161.900 4.688   1.00 108.66 ? 198 TYR   W C   1 
ATOM   40915 O  O   . TYR   W  9  199 ? -7.352  -161.697 3.926   1.00 110.28 ? 198 TYR   W O   1 
ATOM   40916 C  CB  . TYR   W  9  199 ? -4.897  -163.374 3.303   1.00 113.59 ? 198 TYR   W CB  1 
ATOM   40917 C  CG  . TYR   W  9  199 ? -3.978  -164.567 3.218   1.00 114.01 ? 198 TYR   W CG  1 
ATOM   40918 C  CD1 . TYR   W  9  199 ? -4.480  -165.847 3.053   1.00 114.30 ? 198 TYR   W CD1 1 
ATOM   40919 C  CD2 . TYR   W  9  199 ? -2.603  -164.415 3.298   1.00 114.41 ? 198 TYR   W CD2 1 
ATOM   40920 C  CE1 . TYR   W  9  199 ? -3.641  -166.947 2.974   1.00 114.13 ? 198 TYR   W CE1 1 
ATOM   40921 C  CE2 . TYR   W  9  199 ? -1.750  -165.503 3.222   1.00 113.37 ? 198 TYR   W CE2 1 
ATOM   40922 C  CZ  . TYR   W  9  199 ? -2.272  -166.774 3.058   1.00 112.33 ? 198 TYR   W CZ  1 
ATOM   40923 O  OH  . TYR   W  9  199 ? -1.439  -167.850 2.980   1.00 114.04 ? 198 TYR   W OH  1 
ATOM   40924 N  N   . LEU   W  9  200 ? -5.936  -161.007 5.572   1.00 108.51 ? 199 LEU   W N   1 
ATOM   40925 C  CA  . LEU   W  9  200 ? -6.554  -159.671 5.785   1.00 109.45 ? 199 LEU   W CA  1 
ATOM   40926 C  C   . LEU   W  9  200 ? -5.880  -158.647 4.867   1.00 109.24 ? 199 LEU   W C   1 
ATOM   40927 O  O   . LEU   W  9  200 ? -4.678  -158.816 4.558   1.00 106.55 ? 199 LEU   W O   1 
ATOM   40928 C  CB  . LEU   W  9  200 ? -6.415  -159.265 7.257   1.00 106.53 ? 199 LEU   W CB  1 
ATOM   40929 C  CG  . LEU   W  9  200 ? -6.939  -160.266 8.288   1.00 107.95 ? 199 LEU   W CG  1 
ATOM   40930 C  CD1 . LEU   W  9  200 ? -6.829  -159.694 9.694   1.00 104.58 ? 199 LEU   W CD1 1 
ATOM   40931 C  CD2 . LEU   W  9  200 ? -8.378  -160.670 7.990   1.00 111.17 ? 199 LEU   W CD2 1 
ATOM   40932 N  N   . LYS   W  9  201 ? -6.646  -157.640 4.437   1.00 110.01 ? 200 LYS   W N   1 
ATOM   40933 C  CA  . LYS   W  9  201 ? -6.139  -156.413 3.769   1.00 112.35 ? 200 LYS   W CA  1 
ATOM   40934 C  C   . LYS   W  9  201 ? -5.777  -155.383 4.843   1.00 109.10 ? 200 LYS   W C   1 
ATOM   40935 O  O   . LYS   W  9  201 ? -6.689  -154.960 5.583   1.00 104.92 ? 200 LYS   W O   1 
ATOM   40936 C  CB  . LYS   W  9  201 ? -7.194  -155.815 2.836   1.00 115.37 ? 200 LYS   W CB  1 
ATOM   40937 C  CG  . LYS   W  9  201 ? -6.761  -154.536 2.133   1.00 120.06 ? 200 LYS   W CG  1 
ATOM   40938 C  CD  . LYS   W  9  201 ? -7.872  -153.851 1.379   1.00 124.57 ? 200 LYS   W CD  1 
ATOM   40939 C  CE  . LYS   W  9  201 ? -7.562  -152.399 1.088   1.00 128.07 ? 200 LYS   W CE  1 
ATOM   40940 N  NZ  . LYS   W  9  201 ? -8.621  -151.774 0.263   1.00 132.17 ? 200 LYS   W NZ  1 
ATOM   40941 N  N   . MET   W  9  202 ? -4.505  -154.984 4.911   1.00 110.24 ? 201 MET   W N   1 
ATOM   40942 C  CA  . MET   W  9  202 ? -4.010  -153.984 5.893   1.00 109.72 ? 201 MET   W CA  1 
ATOM   40943 C  C   . MET   W  9  202 ? -3.005  -153.047 5.211   1.00 108.90 ? 201 MET   W C   1 
ATOM   40944 O  O   . MET   W  9  202 ? -2.444  -153.436 4.167   1.00 104.78 ? 201 MET   W O   1 
ATOM   40945 C  CB  . MET   W  9  202 ? -3.378  -154.675 7.109   1.00 108.85 ? 201 MET   W CB  1 
ATOM   40946 C  CG  . MET   W  9  202 ? -1.997  -155.263 6.870   1.00 108.05 ? 201 MET   W CG  1 
ATOM   40947 S  SD  . MET   W  9  202 ? -1.249  -155.844 8.410   1.00 104.90 ? 201 MET   W SD  1 
ATOM   40948 C  CE  . MET   W  9  202 ? -1.065  -154.307 9.313   1.00 106.51 ? 201 MET   W CE  1 
ATOM   40949 N  N   . ARG   W  9  203 ? -2.806  -151.852 5.776   1.00 110.00 ? 202 ARG   W N   1 
ATOM   40950 C  CA  . ARG   W  9  203 ? -1.864  -150.827 5.248   1.00 111.93 ? 202 ARG   W CA  1 
ATOM   40951 C  C   . ARG   W  9  203 ? -0.463  -151.448 5.179   1.00 108.08 ? 202 ARG   W C   1 
ATOM   40952 O  O   . ARG   W  9  203 ? -0.113  -152.211 6.101   1.00 109.58 ? 202 ARG   W O   1 
ATOM   40953 C  CB  . ARG   W  9  203 ? -1.911  -149.549 6.095   1.00 112.11 ? 202 ARG   W CB  1 
ATOM   40954 C  CG  . ARG   W  9  203 ? -1.446  -149.701 7.538   1.00 112.71 ? 202 ARG   W CG  1 
ATOM   40955 C  CD  . ARG   W  9  203 ? -1.623  -148.418 8.333   1.00 112.41 ? 202 ARG   W CD  1 
ATOM   40956 N  NE  . ARG   W  9  203 ? -0.958  -147.277 7.707   1.00 112.17 ? 202 ARG   W NE  1 
ATOM   40957 C  CZ  . ARG   W  9  203 ? -1.561  -146.221 7.160   1.00 112.48 ? 202 ARG   W CZ  1 
ATOM   40958 N  NH1 . ARG   W  9  203 ? -2.880  -146.112 7.151   1.00 112.75 ? 202 ARG   W NH1 1 
ATOM   40959 N  NH2 . ARG   W  9  203 ? -0.829  -145.257 6.627   1.00 114.67 ? 202 ARG   W NH2 1 
ATOM   40960 N  N   . GLN   W  9  204 ? 0.296   -151.141 4.123   1.00 106.73 ? 203 GLN   W N   1 
ATOM   40961 C  CA  . GLN   W  9  204 ? 1.587   -151.806 3.794   1.00 106.27 ? 203 GLN   W CA  1 
ATOM   40962 C  C   . GLN   W  9  204 ? 2.762   -150.851 4.043   1.00 110.54 ? 203 GLN   W C   1 
ATOM   40963 O  O   . GLN   W  9  204 ? 3.663   -150.802 3.188   1.00 111.84 ? 203 GLN   W O   1 
ATOM   40964 C  CB  . GLN   W  9  204 ? 1.574   -152.274 2.338   1.00 108.49 ? 203 GLN   W CB  1 
ATOM   40965 C  CG  . GLN   W  9  204 ? 0.471   -153.276 2.027   1.00 110.77 ? 203 GLN   W CG  1 
ATOM   40966 C  CD  . GLN   W  9  204 ? 0.721   -154.631 2.644   1.00 109.63 ? 203 GLN   W CD  1 
ATOM   40967 O  OE1 . GLN   W  9  204 ? 1.724   -155.286 2.365   1.00 108.39 ? 203 GLN   W OE1 1 
ATOM   40968 N  NE2 . GLN   W  9  204 ? -0.198  -155.068 3.491   1.00 114.47 ? 203 GLN   W NE2 1 
ATOM   40969 N  N   . ASP   W  9  205 ? 2.758   -150.133 5.173   1.00 113.67 ? 204 ASP   W N   1 
ATOM   40970 C  CA  . ASP   W  9  205 ? 3.853   -149.210 5.584   1.00 113.90 ? 204 ASP   W CA  1 
ATOM   40971 C  C   . ASP   W  9  205 ? 4.337   -149.609 6.985   1.00 113.54 ? 204 ASP   W C   1 
ATOM   40972 O  O   . ASP   W  9  205 ? 4.908   -148.802 7.717   1.00 111.44 ? 204 ASP   W O   1 
ATOM   40973 C  CB  . ASP   W  9  205 ? 3.410   -147.745 5.486   1.00 116.75 ? 204 ASP   W CB  1 
ATOM   40974 C  CG  . ASP   W  9  205 ? 2.213   -147.372 6.345   1.00 116.14 ? 204 ASP   W CG  1 
ATOM   40975 O  OD1 . ASP   W  9  205 ? 1.555   -148.289 6.875   1.00 113.47 ? 204 ASP   W OD1 1 
ATOM   40976 O  OD2 . ASP   W  9  205 ? 1.946   -146.160 6.475   1.00 117.71 ? 204 ASP   W OD2 1 
ATOM   40977 O  OXT . ASP   W  9  205 ? 4.178   -150.756 7.412   1.00 110.79 ? 204 ASP   W OXT 1 
ATOM   40978 N  N   . MET   X  10 1   ? 34.337  -158.565 0.128   1.00 123.81 ? 1   MET   X N   1 
ATOM   40979 C  CA  . MET   X  10 1   ? 32.883  -158.932 0.085   1.00 119.91 ? 1   MET   X CA  1 
ATOM   40980 C  C   . MET   X  10 1   ? 32.054  -157.653 -0.118  1.00 116.67 ? 1   MET   X C   1 
ATOM   40981 O  O   . MET   X  10 1   ? 32.609  -156.706 -0.704  1.00 118.74 ? 1   MET   X O   1 
ATOM   40982 C  CB  . MET   X  10 1   ? 32.481  -159.684 1.360   1.00 127.88 ? 1   MET   X CB  1 
ATOM   40983 C  CG  . MET   X  10 1   ? 33.196  -161.032 1.509   1.00 137.69 ? 1   MET   X CG  1 
ATOM   40984 S  SD  . MET   X  10 1   ? 32.751  -162.263 0.235   1.00 146.44 ? 1   MET   X SD  1 
ATOM   40985 C  CE  . MET   X  10 1   ? 34.312  -163.120 0.027   1.00 136.64 ? 1   MET   X CE  1 
ATOM   40986 N  N   . ASP   X  10 2   ? 30.769  -157.661 0.259   1.00 111.61 ? 2   ASP   X N   1 
ATOM   40987 C  CA  . ASP   X  10 2   ? 29.879  -156.471 0.402   1.00 111.17 ? 2   ASP   X CA  1 
ATOM   40988 C  C   . ASP   X  10 2   ? 28.592  -156.704 -0.405  1.00 107.53 ? 2   ASP   X C   1 
ATOM   40989 O  O   . ASP   X  10 2   ? 27.588  -157.090 0.224   1.00 113.86 ? 2   ASP   X O   1 
ATOM   40990 C  CB  . ASP   X  10 2   ? 30.573  -155.147 0.051   1.00 107.62 ? 2   ASP   X CB  1 
ATOM   40991 C  CG  . ASP   X  10 2   ? 30.065  -153.957 0.853   1.00 105.95 ? 2   ASP   X CG  1 
ATOM   40992 O  OD1 . ASP   X  10 2   ? 28.834  -153.794 0.951   1.00 102.92 ? 2   ASP   X OD1 1 
ATOM   40993 O  OD2 . ASP   X  10 2   ? 30.909  -153.209 1.384   1.00 108.49 ? 2   ASP   X OD2 1 
ATOM   40994 N  N   . ILE   X  10 3   ? 28.609  -156.502 -1.730  1.00 107.96 ? 3   ILE   X N   1 
ATOM   40995 C  CA  . ILE   X  10 3   ? 27.374  -156.474 -2.577  1.00 104.42 ? 3   ILE   X CA  1 
ATOM   40996 C  C   . ILE   X  10 3   ? 27.123  -157.856 -3.185  1.00 99.53  ? 3   ILE   X C   1 
ATOM   40997 O  O   . ILE   X  10 3   ? 27.965  -158.320 -3.978  1.00 94.02  ? 3   ILE   X O   1 
ATOM   40998 C  CB  . ILE   X  10 3   ? 27.449  -155.392 -3.674  1.00 105.01 ? 3   ILE   X CB  1 
ATOM   40999 C  CG1 . ILE   X  10 3   ? 27.588  -153.996 -3.060  1.00 108.64 ? 3   ILE   X CG1 1 
ATOM   41000 C  CG2 . ILE   X  10 3   ? 26.250  -155.492 -4.613  1.00 100.84 ? 3   ILE   X CG2 1 
ATOM   41001 C  CD1 . ILE   X  10 3   ? 27.601  -152.863 -4.061  1.00 111.96 ? 3   ILE   X CD1 1 
ATOM   41002 N  N   . ILE   X  10 4   ? 25.984  -158.463 -2.840  1.00 97.81  ? 4   ILE   X N   1 
ATOM   41003 C  CA  . ILE   X  10 4   ? 25.411  -159.643 -3.551  1.00 99.44  ? 4   ILE   X CA  1 
ATOM   41004 C  C   . ILE   X  10 4   ? 23.913  -159.399 -3.773  1.00 97.30  ? 4   ILE   X C   1 
ATOM   41005 O  O   . ILE   X  10 4   ? 23.209  -159.059 -2.796  1.00 91.54  ? 4   ILE   X O   1 
ATOM   41006 C  CB  . ILE   X  10 4   ? 25.700  -160.960 -2.798  1.00 100.75 ? 4   ILE   X CB  1 
ATOM   41007 C  CG1 . ILE   X  10 4   ? 25.208  -160.937 -1.349  1.00 101.95 ? 4   ILE   X CG1 1 
ATOM   41008 C  CG2 . ILE   X  10 4   ? 27.182  -161.301 -2.873  1.00 103.72 ? 4   ILE   X CG2 1 
ATOM   41009 C  CD1 . ILE   X  10 4   ? 25.059  -162.312 -0.741  1.00 101.23 ? 4   ILE   X CD1 1 
ATOM   41010 N  N   . LEU   X  10 5   ? 23.469  -159.541 -5.027  1.00 98.21  ? 5   LEU   X N   1 
ATOM   41011 C  CA  . LEU   X  10 5   ? 22.061  -159.363 -5.473  1.00 98.23  ? 5   LEU   X CA  1 
ATOM   41012 C  C   . LEU   X  10 5   ? 21.571  -160.664 -6.111  1.00 96.42  ? 5   LEU   X C   1 
ATOM   41013 O  O   . LEU   X  10 5   ? 22.416  -161.495 -6.510  1.00 94.54  ? 5   LEU   X O   1 
ATOM   41014 C  CB  . LEU   X  10 5   ? 21.979  -158.215 -6.484  1.00 103.08 ? 5   LEU   X CB  1 
ATOM   41015 C  CG  . LEU   X  10 5   ? 22.537  -156.868 -6.025  1.00 105.56 ? 5   LEU   X CG  1 
ATOM   41016 C  CD1 . LEU   X  10 5   ? 22.634  -155.899 -7.194  1.00 107.91 ? 5   LEU   X CD1 1 
ATOM   41017 C  CD2 . LEU   X  10 5   ? 21.691  -156.276 -4.908  1.00 107.93 ? 5   LEU   X CD2 1 
ATOM   41018 N  N   . GLY   X  10 6   ? 20.250  -160.812 -6.204  1.00 93.57  ? 6   GLY   X N   1 
ATOM   41019 C  CA  . GLY   X  10 6   ? 19.580  -161.950 -6.856  1.00 93.61  ? 6   GLY   X CA  1 
ATOM   41020 C  C   . GLY   X  10 6   ? 18.223  -161.543 -7.397  1.00 93.80  ? 6   GLY   X C   1 
ATOM   41021 O  O   . GLY   X  10 6   ? 17.473  -160.886 -6.651  1.00 92.39  ? 6   GLY   X O   1 
ATOM   41022 N  N   . ILE   X  10 7   ? 17.928  -161.900 -8.651  1.00 96.17  ? 7   ILE   X N   1 
ATOM   41023 C  CA  . ILE   X  10 7   ? 16.600  -161.683 -9.298  1.00 98.27  ? 7   ILE   X CA  1 
ATOM   41024 C  C   . ILE   X  10 7   ? 16.135  -163.007 -9.910  1.00 97.82  ? 7   ILE   X C   1 
ATOM   41025 O  O   . ILE   X  10 7   ? 16.852  -163.548 -10.778 1.00 97.63  ? 7   ILE   X O   1 
ATOM   41026 C  CB  . ILE   X  10 7   ? 16.656  -160.550 -10.344 1.00 101.23 ? 7   ILE   X CB  1 
ATOM   41027 C  CG1 . ILE   X  10 7   ? 16.989  -159.205 -9.692  1.00 103.86 ? 7   ILE   X CG1 1 
ATOM   41028 C  CG2 . ILE   X  10 7   ? 15.357  -160.485 -11.135 1.00 101.40 ? 7   ILE   X CG2 1 
ATOM   41029 C  CD1 . ILE   X  10 7   ? 17.208  -158.067 -10.669 1.00 106.42 ? 7   ILE   X CD1 1 
ATOM   41030 N  N   . ARG   X  10 8   ? 14.979  -163.497 -9.454  1.00 97.75  ? 8   ARG   X N   1 
ATOM   41031 C  CA  . ARG   X  10 8   ? 14.225  -164.617 -10.074 1.00 98.59  ? 8   ARG   X CA  1 
ATOM   41032 C  C   . ARG   X  10 8   ? 13.238  -164.038 -11.093 1.00 100.47 ? 8   ARG   X C   1 
ATOM   41033 O  O   . ARG   X  10 8   ? 12.448  -163.159 -10.706 1.00 103.73 ? 8   ARG   X O   1 
ATOM   41034 C  CB  . ARG   X  10 8   ? 13.467  -165.413 -9.008  1.00 96.27  ? 8   ARG   X CB  1 
ATOM   41035 C  CG  . ARG   X  10 8   ? 12.445  -166.382 -9.579  1.00 98.54  ? 8   ARG   X CG  1 
ATOM   41036 C  CD  . ARG   X  10 8   ? 11.855  -167.283 -8.516  1.00 98.94  ? 8   ARG   X CD  1 
ATOM   41037 N  NE  . ARG   X  10 8   ? 11.159  -166.562 -7.457  1.00 98.78  ? 8   ARG   X NE  1 
ATOM   41038 C  CZ  . ARG   X  10 8   ? 9.951   -166.009 -7.564  1.00 99.04  ? 8   ARG   X CZ  1 
ATOM   41039 N  NH1 . ARG   X  10 8   ? 9.279   -166.056 -8.703  1.00 100.85 ? 8   ARG   X NH1 1 
ATOM   41040 N  NH2 . ARG   X  10 8   ? 9.417   -165.395 -6.523  1.00 99.55  ? 8   ARG   X NH2 1 
ATOM   41041 N  N   . VAL   X  10 9   ? 13.270  -164.532 -12.333 1.00 99.44  ? 9   VAL   X N   1 
ATOM   41042 C  CA  . VAL   X  10 9   ? 12.332  -164.133 -13.424 1.00 101.40 ? 9   VAL   X CA  1 
ATOM   41043 C  C   . VAL   X  10 9   ? 11.553  -165.377 -13.867 1.00 102.38 ? 9   VAL   X C   1 
ATOM   41044 O  O   . VAL   X  10 9   ? 11.604  -166.380 -13.137 1.00 99.65  ? 9   VAL   X O   1 
ATOM   41045 C  CB  . VAL   X  10 9   ? 13.076  -163.447 -14.587 1.00 104.12 ? 9   VAL   X CB  1 
ATOM   41046 C  CG1 . VAL   X  10 9   ? 13.548  -162.055 -14.200 1.00 105.45 ? 9   VAL   X CG1 1 
ATOM   41047 C  CG2 . VAL   X  10 9   ? 14.233  -164.280 -15.117 1.00 103.93 ? 9   VAL   X CG2 1 
ATOM   41048 N  N   . GLN   X  10 10  ? 10.841  -165.296 -14.996 1.00 104.87 ? 10  GLN   X N   1 
ATOM   41049 C  CA  . GLN   X  10 10  ? 9.962   -166.366 -15.546 1.00 108.49 ? 10  GLN   X CA  1 
ATOM   41050 C  C   . GLN   X  10 10  ? 10.692  -167.715 -15.535 1.00 106.38 ? 10  GLN   X C   1 
ATOM   41051 O  O   . GLN   X  10 10  ? 10.140  -168.670 -14.955 1.00 101.60 ? 10  GLN   X O   1 
ATOM   41052 C  CB  . GLN   X  10 10  ? 9.523   -165.992 -16.964 1.00 111.79 ? 10  GLN   X CB  1 
ATOM   41053 C  CG  . GLN   X  10 10  ? 8.641   -167.028 -17.650 1.00 114.42 ? 10  GLN   X CG  1 
ATOM   41054 C  CD  . GLN   X  10 10  ? 7.189   -166.907 -17.255 1.00 117.09 ? 10  GLN   X CD  1 
ATOM   41055 O  OE1 . GLN   X  10 10  ? 6.831   -167.068 -16.091 1.00 117.19 ? 10  GLN   X OE1 1 
ATOM   41056 N  NE2 . GLN   X  10 10  ? 6.336   -166.628 -18.230 1.00 120.28 ? 10  GLN   X NE2 1 
ATOM   41057 N  N   . ASP   X  10 11  ? 11.884  -167.782 -16.138 1.00 108.86 ? 11  ASP   X N   1 
ATOM   41058 C  CA  . ASP   X  10 11  ? 12.550  -169.059 -16.515 1.00 112.29 ? 11  ASP   X CA  1 
ATOM   41059 C  C   . ASP   X  10 11  ? 13.950  -169.197 -15.906 1.00 111.54 ? 11  ASP   X C   1 
ATOM   41060 O  O   . ASP   X  10 11  ? 14.573  -170.244 -16.162 1.00 114.50 ? 11  ASP   X O   1 
ATOM   41061 C  CB  . ASP   X  10 11  ? 12.664  -169.178 -18.035 1.00 117.89 ? 11  ASP   X CB  1 
ATOM   41062 C  CG  . ASP   X  10 11  ? 11.323  -169.165 -18.747 1.00 124.52 ? 11  ASP   X CG  1 
ATOM   41063 O  OD1 . ASP   X  10 11  ? 10.447  -169.963 -18.357 1.00 128.96 ? 11  ASP   X OD1 1 
ATOM   41064 O  OD2 . ASP   X  10 11  ? 11.164  -168.356 -19.681 1.00 131.63 ? 11  ASP   X OD2 1 
ATOM   41065 N  N   . SER   X  10 12  ? 14.448  -168.217 -15.146 1.00 109.11 ? 12  SER   X N   1 
ATOM   41066 C  CA  . SER   X  10 12  ? 15.845  -168.239 -14.637 1.00 106.81 ? 12  SER   X CA  1 
ATOM   41067 C  C   . SER   X  10 12  ? 16.002  -167.426 -13.350 1.00 104.51 ? 12  SER   X C   1 
ATOM   41068 O  O   . SER   X  10 12  ? 15.132  -166.590 -13.045 1.00 106.53 ? 12  SER   X O   1 
ATOM   41069 C  CB  . SER   X  10 12  ? 16.810  -167.765 -15.694 1.00 108.68 ? 12  SER   X CB  1 
ATOM   41070 O  OG  . SER   X  10 12  ? 16.549  -166.419 -16.054 1.00 109.54 ? 12  SER   X OG  1 
ATOM   41071 N  N   . VAL   X  10 13  ? 17.088  -167.705 -12.627 1.00 101.63 ? 13  VAL   X N   1 
ATOM   41072 C  CA  . VAL   X  10 13  ? 17.591  -166.912 -11.471 1.00 102.15 ? 13  VAL   X CA  1 
ATOM   41073 C  C   . VAL   X  10 13  ? 18.902  -166.262 -11.918 1.00 101.00 ? 13  VAL   X C   1 
ATOM   41074 O  O   . VAL   X  10 13  ? 19.751  -166.978 -12.486 1.00 97.72  ? 13  VAL   X O   1 
ATOM   41075 C  CB  . VAL   X  10 13  ? 17.798  -167.787 -10.220 1.00 102.21 ? 13  VAL   X CB  1 
ATOM   41076 C  CG1 . VAL   X  10 13  ? 18.055  -166.939 -8.984  1.00 103.94 ? 13  VAL   X CG1 1 
ATOM   41077 C  CG2 . VAL   X  10 13  ? 16.630  -168.732 -9.982  1.00 103.28 ? 13  VAL   X CG2 1 
ATOM   41078 N  N   . ILE   X  10 14  ? 19.043  -164.954 -11.687 1.00 101.76 ? 14  ILE   X N   1 
ATOM   41079 C  CA  . ILE   X  10 14  ? 20.266  -164.166 -12.018 1.00 103.62 ? 14  ILE   X CA  1 
ATOM   41080 C  C   . ILE   X  10 14  ? 20.890  -163.694 -10.701 1.00 99.82  ? 14  ILE   X C   1 
ATOM   41081 O  O   . ILE   X  10 14  ? 20.158  -163.079 -9.905  1.00 101.53 ? 14  ILE   X O   1 
ATOM   41082 C  CB  . ILE   X  10 14  ? 19.923  -162.993 -12.958 1.00 107.56 ? 14  ILE   X CB  1 
ATOM   41083 C  CG1 . ILE   X  10 14  ? 18.996  -163.425 -14.099 1.00 111.46 ? 14  ILE   X CG1 1 
ATOM   41084 C  CG2 . ILE   X  10 14  ? 21.194  -162.343 -13.483 1.00 110.84 ? 14  ILE   X CG2 1 
ATOM   41085 C  CD1 . ILE   X  10 14  ? 18.271  -162.285 -14.779 1.00 114.78 ? 14  ILE   X CD1 1 
ATOM   41086 N  N   . LEU   X  10 15  ? 22.173  -164.003 -10.477 1.00 100.19 ? 15  LEU   X N   1 
ATOM   41087 C  CA  . LEU   X  10 15  ? 22.968  -163.541 -9.305  1.00 97.02  ? 15  LEU   X CA  1 
ATOM   41088 C  C   . LEU   X  10 15  ? 24.061  -162.572 -9.770  1.00 98.08  ? 15  LEU   X C   1 
ATOM   41089 O  O   . LEU   X  10 15  ? 24.875  -162.962 -10.627 1.00 98.10  ? 15  LEU   X O   1 
ATOM   41090 C  CB  . LEU   X  10 15  ? 23.611  -164.739 -8.598  1.00 93.85  ? 15  LEU   X CB  1 
ATOM   41091 C  CG  . LEU   X  10 15  ? 22.670  -165.802 -8.033  1.00 90.66  ? 15  LEU   X CG  1 
ATOM   41092 C  CD1 . LEU   X  10 15  ? 23.449  -166.750 -7.137  1.00 89.89  ? 15  LEU   X CD1 1 
ATOM   41093 C  CD2 . LEU   X  10 15  ? 21.510  -165.189 -7.261  1.00 89.60  ? 15  LEU   X CD2 1 
ATOM   41094 N  N   . ALA   X  10 16  ? 24.084  -161.365 -9.200  1.00 97.68  ? 16  ALA   X N   1 
ATOM   41095 C  CA  . ALA   X  10 16  ? 25.159  -160.360 -9.371  1.00 98.53  ? 16  ALA   X CA  1 
ATOM   41096 C  C   . ALA   X  10 16  ? 25.920  -160.232 -8.051  1.00 93.64  ? 16  ALA   X C   1 
ATOM   41097 O  O   . ALA   X  10 16  ? 25.260  -160.141 -7.001  1.00 91.72  ? 16  ALA   X O   1 
ATOM   41098 C  CB  . ALA   X  10 16  ? 24.576  -159.038 -9.793  1.00 101.57 ? 16  ALA   X CB  1 
ATOM   41099 N  N   . SER   X  10 17  ? 27.253  -160.233 -8.111  1.00 93.66  ? 17  SER   X N   1 
ATOM   41100 C  CA  . SER   X  10 17  ? 28.150  -160.256 -6.926  1.00 96.35  ? 17  SER   X CA  1 
ATOM   41101 C  C   . SER   X  10 17  ? 29.374  -159.373 -7.194  1.00 96.26  ? 17  SER   X C   1 
ATOM   41102 O  O   . SER   X  10 17  ? 30.045  -159.599 -8.219  1.00 103.02 ? 17  SER   X O   1 
ATOM   41103 C  CB  . SER   X  10 17  ? 28.545  -161.675 -6.585  1.00 98.38  ? 17  SER   X CB  1 
ATOM   41104 O  OG  . SER   X  10 17  ? 27.421  -162.546 -6.632  1.00 100.08 ? 17  SER   X OG  1 
ATOM   41105 N  N   . SER   X  10 18  ? 29.645  -158.406 -6.309  1.00 93.25  ? 18  SER   X N   1 
ATOM   41106 C  CA  . SER   X  10 18  ? 30.732  -157.399 -6.446  1.00 94.53  ? 18  SER   X CA  1 
ATOM   41107 C  C   . SER   X  10 18  ? 32.091  -158.098 -6.561  1.00 93.27  ? 18  SER   X C   1 
ATOM   41108 O  O   . SER   X  10 18  ? 32.242  -159.187 -5.989  1.00 90.99  ? 18  SER   X O   1 
ATOM   41109 C  CB  . SER   X  10 18  ? 30.719  -156.413 -5.306  1.00 94.76  ? 18  SER   X CB  1 
ATOM   41110 O  OG  . SER   X  10 18  ? 30.757  -157.074 -4.050  1.00 95.01  ? 18  SER   X OG  1 
ATOM   41111 N  N   . LYS   X  10 19  ? 33.038  -157.480 -7.273  1.00 94.48  ? 19  LYS   X N   1 
ATOM   41112 C  CA  . LYS   X  10 19  ? 34.338  -158.093 -7.660  1.00 96.42  ? 19  LYS   X CA  1 
ATOM   41113 C  C   . LYS   X  10 19  ? 35.481  -157.603 -6.761  1.00 96.04  ? 19  LYS   X C   1 
ATOM   41114 O  O   . LYS   X  10 19  ? 36.598  -158.134 -6.906  1.00 96.91  ? 19  LYS   X O   1 
ATOM   41115 C  CB  . LYS   X  10 19  ? 34.669  -157.767 -9.119  1.00 100.13 ? 19  LYS   X CB  1 
ATOM   41116 C  CG  . LYS   X  10 19  ? 33.746  -158.398 -10.152 1.00 101.90 ? 19  LYS   X CG  1 
ATOM   41117 C  CD  . LYS   X  10 19  ? 34.342  -158.431 -11.546 1.00 105.08 ? 19  LYS   X CD  1 
ATOM   41118 C  CE  . LYS   X  10 19  ? 34.223  -157.112 -12.276 1.00 105.33 ? 19  LYS   X CE  1 
ATOM   41119 N  NZ  . LYS   X  10 19  ? 35.077  -157.086 -13.485 1.00 108.46 ? 19  LYS   X NZ  1 
ATOM   41120 N  N   . ALA   X  10 20  ? 35.233  -156.628 -5.883  1.00 97.06  ? 20  ALA   X N   1 
ATOM   41121 C  CA  . ALA   X  10 20  ? 36.275  -155.999 -5.037  1.00 100.07 ? 20  ALA   X CA  1 
ATOM   41122 C  C   . ALA   X  10 20  ? 36.527  -156.852 -3.790  1.00 98.35  ? 20  ALA   X C   1 
ATOM   41123 O  O   . ALA   X  10 20  ? 35.544  -157.318 -3.182  1.00 96.90  ? 20  ALA   X O   1 
ATOM   41124 C  CB  . ALA   X  10 20  ? 35.872  -154.598 -4.652  1.00 101.15 ? 20  ALA   X CB  1 
ATOM   41125 N  N   . VAL   X  10 21  ? 37.802  -157.045 -3.441  1.00 100.70 ? 21  VAL   X N   1 
ATOM   41126 C  CA  . VAL   X  10 21  ? 38.246  -157.541 -2.106  1.00 101.29 ? 21  VAL   X CA  1 
ATOM   41127 C  C   . VAL   X  10 21  ? 39.144  -156.464 -1.498  1.00 101.83 ? 21  VAL   X C   1 
ATOM   41128 O  O   . VAL   X  10 21  ? 40.317  -156.365 -1.914  1.00 99.02  ? 21  VAL   X O   1 
ATOM   41129 C  CB  . VAL   X  10 21  ? 38.972  -158.897 -2.183  1.00 103.77 ? 21  VAL   X CB  1 
ATOM   41130 C  CG1 . VAL   X  10 21  ? 39.483  -159.332 -0.816  1.00 104.05 ? 21  VAL   X CG1 1 
ATOM   41131 C  CG2 . VAL   X  10 21  ? 38.087  -159.973 -2.790  1.00 104.57 ? 21  VAL   X CG2 1 
ATOM   41132 N  N   . THR   X  10 22  ? 38.591  -155.686 -0.565  1.00 103.52 ? 22  THR   X N   1 
ATOM   41133 C  CA  . THR   X  10 22  ? 39.275  -154.564 0.128   1.00 107.77 ? 22  THR   X CA  1 
ATOM   41134 C  C   . THR   X  10 22  ? 39.705  -155.023 1.525   1.00 105.19 ? 22  THR   X C   1 
ATOM   41135 O  O   . THR   X  10 22  ? 38.891  -155.663 2.216   1.00 104.81 ? 22  THR   X O   1 
ATOM   41136 C  CB  . THR   X  10 22  ? 38.373  -153.326 0.208   1.00 108.86 ? 22  THR   X CB  1 
ATOM   41137 O  OG1 . THR   X  10 22  ? 37.926  -152.988 -1.105  1.00 111.72 ? 22  THR   X OG1 1 
ATOM   41138 C  CG2 . THR   X  10 22  ? 39.081  -152.135 0.816   1.00 111.86 ? 22  THR   X CG2 1 
ATOM   41139 N  N   . ARG   X  10 23  ? 40.944  -154.707 1.908   1.00 109.05 ? 23  ARG   X N   1 
ATOM   41140 C  CA  . ARG   X  10 23  ? 41.480  -154.900 3.280   1.00 112.07 ? 23  ARG   X CA  1 
ATOM   41141 C  C   . ARG   X  10 23  ? 42.222  -153.623 3.688   1.00 111.78 ? 23  ARG   X C   1 
ATOM   41142 O  O   . ARG   X  10 23  ? 43.265  -153.329 3.069   1.00 112.87 ? 23  ARG   X O   1 
ATOM   41143 C  CB  . ARG   X  10 23  ? 42.414  -156.113 3.321   1.00 116.28 ? 23  ARG   X CB  1 
ATOM   41144 C  CG  . ARG   X  10 23  ? 42.044  -157.162 4.360   1.00 119.22 ? 23  ARG   X CG  1 
ATOM   41145 C  CD  . ARG   X  10 23  ? 41.317  -158.361 3.772   1.00 122.46 ? 23  ARG   X CD  1 
ATOM   41146 N  NE  . ARG   X  10 23  ? 39.911  -158.099 3.489   1.00 124.94 ? 23  ARG   X NE  1 
ATOM   41147 C  CZ  . ARG   X  10 23  ? 39.036  -159.012 3.070   1.00 125.22 ? 23  ARG   X CZ  1 
ATOM   41148 N  NH1 . ARG   X  10 23  ? 37.779  -158.667 2.842   1.00 130.14 ? 23  ARG   X NH1 1 
ATOM   41149 N  NH2 . ARG   X  10 23  ? 39.413  -160.265 2.879   1.00 126.72 ? 23  ARG   X NH2 1 
ATOM   41150 N  N   . GLY   X  10 24  ? 41.694  -152.894 4.677   1.00 111.98 ? 24  GLY   X N   1 
ATOM   41151 C  CA  . GLY   X  10 24  ? 42.220  -151.586 5.117   1.00 111.48 ? 24  GLY   X CA  1 
ATOM   41152 C  C   . GLY   X  10 24  ? 41.995  -150.518 4.062   1.00 112.00 ? 24  GLY   X C   1 
ATOM   41153 O  O   . GLY   X  10 24  ? 40.852  -150.412 3.574   1.00 113.19 ? 24  GLY   X O   1 
ATOM   41154 N  N   . ILE   X  10 25  ? 43.044  -149.768 3.706   1.00 113.21 ? 25  ILE   X N   1 
ATOM   41155 C  CA  . ILE   X  10 25  ? 42.985  -148.664 2.699   1.00 114.44 ? 25  ILE   X CA  1 
ATOM   41156 C  C   . ILE   X  10 25  ? 43.518  -149.155 1.343   1.00 113.11 ? 25  ILE   X C   1 
ATOM   41157 O  O   . ILE   X  10 25  ? 43.949  -148.295 0.549   1.00 116.31 ? 25  ILE   X O   1 
ATOM   41158 C  CB  . ILE   X  10 25  ? 43.741  -147.411 3.194   1.00 116.93 ? 25  ILE   X CB  1 
ATOM   41159 C  CG1 . ILE   X  10 25  ? 45.230  -147.677 3.438   1.00 118.02 ? 25  ILE   X CG1 1 
ATOM   41160 C  CG2 . ILE   X  10 25  ? 43.065  -146.830 4.426   1.00 117.02 ? 25  ILE   X CG2 1 
ATOM   41161 C  CD1 . ILE   X  10 25  ? 46.081  -146.429 3.421   1.00 120.34 ? 25  ILE   X CD1 1 
ATOM   41162 N  N   . SER   X  10 26  ? 43.473  -150.466 1.073   1.00 109.72 ? 26  SER   X N   1 
ATOM   41163 C  CA  . SER   X  10 26  ? 43.929  -151.082 -0.203  1.00 108.09 ? 26  SER   X CA  1 
ATOM   41164 C  C   . SER   X  10 26  ? 42.856  -152.017 -0.771  1.00 106.06 ? 26  SER   X C   1 
ATOM   41165 O  O   . SER   X  10 26  ? 42.415  -152.924 -0.040  1.00 105.97 ? 26  SER   X O   1 
ATOM   41166 C  CB  . SER   X  10 26  ? 45.225  -151.825 -0.022  1.00 106.79 ? 26  SER   X CB  1 
ATOM   41167 O  OG  . SER   X  10 26  ? 46.303  -150.933 0.217   1.00 107.63 ? 26  SER   X OG  1 
ATOM   41168 N  N   . VAL   X  10 27  ? 42.477  -151.810 -2.037  1.00 106.35 ? 27  VAL   X N   1 
ATOM   41169 C  CA  . VAL   X  10 27  ? 41.687  -152.783 -2.847  1.00 104.71 ? 27  VAL   X CA  1 
ATOM   41170 C  C   . VAL   X  10 27  ? 42.678  -153.826 -3.377  1.00 107.35 ? 27  VAL   X C   1 
ATOM   41171 O  O   . VAL   X  10 27  ? 43.408  -153.514 -4.340  1.00 106.90 ? 27  VAL   X O   1 
ATOM   41172 C  CB  . VAL   X  10 27  ? 40.909  -152.100 -3.990  1.00 105.07 ? 27  VAL   X CB  1 
ATOM   41173 C  CG1 . VAL   X  10 27  ? 40.070  -153.098 -4.776  1.00 103.27 ? 27  VAL   X CG1 1 
ATOM   41174 C  CG2 . VAL   X  10 27  ? 40.036  -150.960 -3.486  1.00 104.32 ? 27  VAL   X CG2 1 
ATOM   41175 N  N   . LEU   X  10 28  ? 42.715  -155.006 -2.751  1.00 108.25 ? 28  LEU   X N   1 
ATOM   41176 C  CA  . LEU   X  10 28  ? 43.715  -156.071 -3.038  1.00 110.71 ? 28  LEU   X CA  1 
ATOM   41177 C  C   . LEU   X  10 28  ? 43.400  -156.752 -4.373  1.00 107.53 ? 28  LEU   X C   1 
ATOM   41178 O  O   . LEU   X  10 28  ? 44.360  -157.183 -5.039  1.00 107.28 ? 28  LEU   X O   1 
ATOM   41179 C  CB  . LEU   X  10 28  ? 43.725  -157.091 -1.894  1.00 110.41 ? 28  LEU   X CB  1 
ATOM   41180 C  CG  . LEU   X  10 28  ? 44.201  -156.572 -0.537  1.00 114.51 ? 28  LEU   X CG  1 
ATOM   41181 C  CD1 . LEU   X  10 28  ? 44.109  -157.669 0.514   1.00 111.94 ? 28  LEU   X CD1 1 
ATOM   41182 C  CD2 . LEU   X  10 28  ? 45.622  -156.026 -0.616  1.00 115.75 ? 28  LEU   X CD2 1 
ATOM   41183 N  N   . LYS   X  10 29  ? 42.119  -156.843 -4.750  1.00 106.43 ? 29  LYS   X N   1 
ATOM   41184 C  CA  . LYS   X  10 29  ? 41.670  -157.580 -5.962  1.00 107.62 ? 29  LYS   X CA  1 
ATOM   41185 C  C   . LYS   X  10 29  ? 40.354  -156.999 -6.487  1.00 104.88 ? 29  LYS   X C   1 
ATOM   41186 O  O   . LYS   X  10 29  ? 39.516  -156.602 -5.656  1.00 104.79 ? 29  LYS   X O   1 
ATOM   41187 C  CB  . LYS   X  10 29  ? 41.500  -159.064 -5.636  1.00 108.99 ? 29  LYS   X CB  1 
ATOM   41188 C  CG  . LYS   X  10 29  ? 41.530  -159.980 -6.849  1.00 112.36 ? 29  LYS   X CG  1 
ATOM   41189 C  CD  . LYS   X  10 29  ? 41.524  -161.447 -6.506  1.00 111.80 ? 29  LYS   X CD  1 
ATOM   41190 C  CE  . LYS   X  10 29  ? 41.342  -162.312 -7.734  1.00 113.30 ? 29  LYS   X CE  1 
ATOM   41191 N  NZ  . LYS   X  10 29  ? 41.331  -163.753 -7.391  1.00 113.78 ? 29  LYS   X NZ  1 
ATOM   41192 N  N   . ASP   X  10 30  ? 40.185  -156.987 -7.816  1.00 105.55 ? 30  ASP   X N   1 
ATOM   41193 C  CA  . ASP   X  10 30  ? 39.042  -156.348 -8.527  1.00 105.92 ? 30  ASP   X CA  1 
ATOM   41194 C  C   . ASP   X  10 30  ? 38.387  -157.346 -9.491  1.00 104.41 ? 30  ASP   X C   1 
ATOM   41195 O  O   . ASP   X  10 30  ? 37.680  -156.891 -10.409 1.00 100.90 ? 30  ASP   X O   1 
ATOM   41196 C  CB  . ASP   X  10 30  ? 39.507  -155.093 -9.274  1.00 109.39 ? 30  ASP   X CB  1 
ATOM   41197 C  CG  . ASP   X  10 30  ? 40.554  -155.350 -10.347 1.00 113.24 ? 30  ASP   X CG  1 
ATOM   41198 O  OD1 . ASP   X  10 30  ? 40.973  -156.520 -10.501 1.00 110.42 ? 30  ASP   X OD1 1 
ATOM   41199 O  OD2 . ASP   X  10 30  ? 40.946  -154.376 -11.022 1.00 116.79 ? 30  ASP   X OD2 1 
ATOM   41200 N  N   . SER   X  10 31  ? 38.608  -158.649 -9.291  1.00 103.39 ? 31  SER   X N   1 
ATOM   41201 C  CA  . SER   X  10 31  ? 38.114  -159.738 -10.177 1.00 103.92 ? 31  SER   X CA  1 
ATOM   41202 C  C   . SER   X  10 31  ? 37.662  -160.956 -9.360  1.00 101.49 ? 31  SER   X C   1 
ATOM   41203 O  O   . SER   X  10 31  ? 37.616  -162.054 -9.937  1.00 102.02 ? 31  SER   X O   1 
ATOM   41204 C  CB  . SER   X  10 31  ? 39.182  -160.120 -11.167 1.00 105.37 ? 31  SER   X CB  1 
ATOM   41205 O  OG  . SER   X  10 31  ? 40.317  -160.653 -10.497 1.00 102.41 ? 31  SER   X OG  1 
ATOM   41206 N  N   . ASP   X  10 32  ? 37.316  -160.772 -8.083  1.00 100.94 ? 32  ASP   X N   1 
ATOM   41207 C  CA  . ASP   X  10 32  ? 36.977  -161.882 -7.154  1.00 98.98  ? 32  ASP   X CA  1 
ATOM   41208 C  C   . ASP   X  10 32  ? 35.578  -162.413 -7.488  1.00 99.98  ? 32  ASP   X C   1 
ATOM   41209 O  O   . ASP   X  10 32  ? 34.648  -161.597 -7.637  1.00 100.27 ? 32  ASP   X O   1 
ATOM   41210 C  CB  . ASP   X  10 32  ? 37.068  -161.448 -5.691  1.00 99.79  ? 32  ASP   X CB  1 
ATOM   41211 C  CG  . ASP   X  10 32  ? 36.833  -162.585 -4.707  1.00 100.54 ? 32  ASP   X CG  1 
ATOM   41212 O  OD1 . ASP   X  10 32  ? 37.462  -163.646 -4.880  1.00 98.82  ? 32  ASP   X OD1 1 
ATOM   41213 O  OD2 . ASP   X  10 32  ? 36.017  -162.405 -3.781  1.00 103.48 ? 32  ASP   X OD2 1 
ATOM   41214 N  N   . ASP   X  10 33  ? 35.449  -163.738 -7.598  1.00 102.95 ? 33  ASP   X N   1 
ATOM   41215 C  CA  . ASP   X  10 33  ? 34.171  -164.442 -7.884  1.00 107.44 ? 33  ASP   X CA  1 
ATOM   41216 C  C   . ASP   X  10 33  ? 33.596  -164.961 -6.561  1.00 104.51 ? 33  ASP   X C   1 
ATOM   41217 O  O   . ASP   X  10 33  ? 34.072  -166.005 -6.079  1.00 103.18 ? 33  ASP   X O   1 
ATOM   41218 C  CB  . ASP   X  10 33  ? 34.371  -165.566 -8.904  1.00 110.70 ? 33  ASP   X CB  1 
ATOM   41219 C  CG  . ASP   X  10 33  ? 33.071  -166.122 -9.465  1.00 115.30 ? 33  ASP   X CG  1 
ATOM   41220 O  OD1 . ASP   X  10 33  ? 32.008  -165.513 -9.210  1.00 120.06 ? 33  ASP   X OD1 1 
ATOM   41221 O  OD2 . ASP   X  10 33  ? 33.130  -167.160 -10.154 1.00 120.78 ? 33  ASP   X OD2 1 
ATOM   41222 N  N   . LYS   X  10 34  ? 32.610  -164.254 -6.003  1.00 106.42 ? 34  LYS   X N   1 
ATOM   41223 C  CA  . LYS   X  10 34  ? 32.008  -164.550 -4.674  1.00 102.26 ? 34  LYS   X CA  1 
ATOM   41224 C  C   . LYS   X  10 34  ? 30.856  -165.546 -4.840  1.00 98.09  ? 34  LYS   X C   1 
ATOM   41225 O  O   . LYS   X  10 34  ? 29.747  -165.270 -4.335  1.00 88.08  ? 34  LYS   X O   1 
ATOM   41226 C  CB  . LYS   X  10 34  ? 31.535  -163.253 -4.010  1.00 104.51 ? 34  LYS   X CB  1 
ATOM   41227 C  CG  . LYS   X  10 34  ? 32.656  -162.300 -3.628  1.00 104.52 ? 34  LYS   X CG  1 
ATOM   41228 C  CD  . LYS   X  10 34  ? 32.181  -160.901 -3.339  1.00 105.97 ? 34  LYS   X CD  1 
ATOM   41229 C  CE  . LYS   X  10 34  ? 33.308  -159.963 -2.962  1.00 108.26 ? 34  LYS   X CE  1 
ATOM   41230 N  NZ  . LYS   X  10 34  ? 34.375  -159.903 -3.987  1.00 111.76 ? 34  LYS   X NZ  1 
ATOM   41231 N  N   . THR   X  10 35  ? 31.118  -166.673 -5.502  1.00 96.15  ? 35  THR   X N   1 
ATOM   41232 C  CA  . THR   X  10 35  ? 30.096  -167.706 -5.803  1.00 97.77  ? 35  THR   X CA  1 
ATOM   41233 C  C   . THR   X  10 35  ? 30.750  -169.091 -5.850  1.00 98.43  ? 35  THR   X C   1 
ATOM   41234 O  O   . THR   X  10 35  ? 31.948  -169.177 -6.193  1.00 99.25  ? 35  THR   X O   1 
ATOM   41235 C  CB  . THR   X  10 35  ? 29.350  -167.363 -7.100  1.00 101.72 ? 35  THR   X CB  1 
ATOM   41236 O  OG1 . THR   X  10 35  ? 28.009  -167.838 -6.983  1.00 104.67 ? 35  THR   X OG1 1 
ATOM   41237 C  CG2 . THR   X  10 35  ? 29.994  -167.951 -8.337  1.00 102.09 ? 35  THR   X CG2 1 
ATOM   41238 N  N   . ARG   X  10 36  ? 29.977  -170.122 -5.498  1.00 96.95  ? 36  ARG   X N   1 
ATOM   41239 C  CA  . ARG   X  10 36  ? 30.317  -171.551 -5.716  1.00 94.16  ? 36  ARG   X CA  1 
ATOM   41240 C  C   . ARG   X  10 36  ? 29.117  -172.234 -6.369  1.00 90.39  ? 36  ARG   X C   1 
ATOM   41241 O  O   . ARG   X  10 36  ? 27.971  -171.863 -6.028  1.00 82.83  ? 36  ARG   X O   1 
ATOM   41242 C  CB  . ARG   X  10 36  ? 30.683  -172.250 -4.401  1.00 92.56  ? 36  ARG   X CB  1 
ATOM   41243 C  CG  . ARG   X  10 36  ? 31.993  -171.786 -3.779  1.00 94.44  ? 36  ARG   X CG  1 
ATOM   41244 C  CD  . ARG   X  10 36  ? 33.188  -171.884 -4.710  1.00 96.90  ? 36  ARG   X CD  1 
ATOM   41245 N  NE  . ARG   X  10 36  ? 34.078  -170.743 -4.525  1.00 96.45  ? 36  ARG   X NE  1 
ATOM   41246 C  CZ  . ARG   X  10 36  ? 35.315  -170.796 -4.040  1.00 96.60  ? 36  ARG   X CZ  1 
ATOM   41247 N  NH1 . ARG   X  10 36  ? 35.859  -171.948 -3.685  1.00 98.22  ? 36  ARG   X NH1 1 
ATOM   41248 N  NH2 . ARG   X  10 36  ? 36.015  -169.682 -3.920  1.00 98.33  ? 36  ARG   X NH2 1 
ATOM   41249 N  N   . GLN   X  10 37  ? 29.390  -173.169 -7.283  1.00 91.17  ? 37  GLN   X N   1 
ATOM   41250 C  CA  . GLN   X  10 37  ? 28.394  -174.111 -7.854  1.00 90.55  ? 37  GLN   X CA  1 
ATOM   41251 C  C   . GLN   X  10 37  ? 28.268  -175.304 -6.902  1.00 89.18  ? 37  GLN   X C   1 
ATOM   41252 O  O   . GLN   X  10 37  ? 29.271  -176.014 -6.721  1.00 93.64  ? 37  GLN   X O   1 
ATOM   41253 C  CB  . GLN   X  10 37  ? 28.821  -174.557 -9.253  1.00 93.63  ? 37  GLN   X CB  1 
ATOM   41254 C  CG  . GLN   X  10 37  ? 27.822  -175.497 -9.911  1.00 93.58  ? 37  GLN   X CG  1 
ATOM   41255 C  CD  . GLN   X  10 37  ? 28.228  -175.937 -11.295 1.00 96.09  ? 37  GLN   X CD  1 
ATOM   41256 O  OE1 . GLN   X  10 37  ? 28.104  -177.106 -11.647 1.00 98.52  ? 37  GLN   X OE1 1 
ATOM   41257 N  NE2 . GLN   X  10 37  ? 28.710  -175.004 -12.100 1.00 97.16  ? 37  GLN   X NE2 1 
ATOM   41258 N  N   . LEU   X  10 38  ? 27.090  -175.498 -6.303  1.00 88.11  ? 38  LEU   X N   1 
ATOM   41259 C  CA  . LEU   X  10 38  ? 26.814  -176.616 -5.361  1.00 89.88  ? 38  LEU   X CA  1 
ATOM   41260 C  C   . LEU   X  10 38  ? 26.431  -177.865 -6.163  1.00 92.10  ? 38  LEU   X C   1 
ATOM   41261 O  O   . LEU   X  10 38  ? 26.864  -178.968 -5.779  1.00 92.78  ? 38  LEU   X O   1 
ATOM   41262 C  CB  . LEU   X  10 38  ? 25.702  -176.205 -4.392  1.00 90.20  ? 38  LEU   X CB  1 
ATOM   41263 C  CG  . LEU   X  10 38  ? 25.929  -174.892 -3.643  1.00 90.50  ? 38  LEU   X CG  1 
ATOM   41264 C  CD1 . LEU   X  10 38  ? 24.843  -174.676 -2.601  1.00 92.49  ? 38  LEU   X CD1 1 
ATOM   41265 C  CD2 . LEU   X  10 38  ? 27.305  -174.851 -2.989  1.00 91.77  ? 38  LEU   X CD2 1 
ATOM   41266 N  N   . SER   X  10 39  ? 25.655  -177.688 -7.234  1.00 92.09  ? 39  SER   X N   1 
ATOM   41267 C  CA  . SER   X  10 39  ? 25.245  -178.761 -8.178  1.00 94.93  ? 39  SER   X CA  1 
ATOM   41268 C  C   . SER   X  10 39  ? 25.030  -178.157 -9.567  1.00 97.31  ? 39  SER   X C   1 
ATOM   41269 O  O   . SER   X  10 39  ? 25.017  -176.936 -9.714  1.00 94.26  ? 39  SER   X O   1 
ATOM   41270 C  CB  . SER   X  10 39  ? 24.022  -179.487 -7.656  1.00 93.35  ? 39  SER   X CB  1 
ATOM   41271 O  OG  . SER   X  10 39  ? 22.850  -178.696 -7.778  1.00 92.81  ? 39  SER   X OG  1 
ATOM   41272 N  N   . PRO   X  10 40  ? 24.878  -178.979 -10.633 1.00 97.21  ? 40  PRO   X N   1 
ATOM   41273 C  CA  . PRO   X  10 40  ? 24.704  -178.460 -11.992 1.00 99.39  ? 40  PRO   X CA  1 
ATOM   41274 C  C   . PRO   X  10 40  ? 23.663  -177.339 -12.151 1.00 100.75 ? 40  PRO   X C   1 
ATOM   41275 O  O   . PRO   X  10 40  ? 23.888  -176.475 -12.978 1.00 99.09  ? 40  PRO   X O   1 
ATOM   41276 C  CB  . PRO   X  10 40  ? 24.239  -179.695 -12.775 1.00 100.83 ? 40  PRO   X CB  1 
ATOM   41277 C  CG  . PRO   X  10 40  ? 24.912  -180.843 -12.061 1.00 101.45 ? 40  PRO   X CG  1 
ATOM   41278 C  CD  . PRO   X  10 40  ? 24.893  -180.449 -10.599 1.00 98.68  ? 40  PRO   X CD  1 
ATOM   41279 N  N   . HIS   X  10 41  ? 22.570  -177.385 -11.377 1.00 100.67 ? 41  HIS   X N   1 
ATOM   41280 C  CA  . HIS   X  10 41  ? 21.433  -176.426 -11.444 1.00 101.62 ? 41  HIS   X CA  1 
ATOM   41281 C  C   . HIS   X  10 41  ? 21.253  -175.671 -10.118 1.00 101.25 ? 41  HIS   X C   1 
ATOM   41282 O  O   . HIS   X  10 41  ? 20.126  -175.190 -9.883  1.00 105.77 ? 41  HIS   X O   1 
ATOM   41283 C  CB  . HIS   X  10 41  ? 20.138  -177.156 -11.829 1.00 104.13 ? 41  HIS   X CB  1 
ATOM   41284 C  CG  . HIS   X  10 41  ? 20.219  -177.888 -13.125 1.00 109.01 ? 41  HIS   X CG  1 
ATOM   41285 N  ND1 . HIS   X  10 41  ? 20.423  -179.252 -13.192 1.00 112.65 ? 41  HIS   X ND1 1 
ATOM   41286 C  CD2 . HIS   X  10 41  ? 20.120  -177.458 -14.401 1.00 112.16 ? 41  HIS   X CD2 1 
ATOM   41287 C  CE1 . HIS   X  10 41  ? 20.446  -179.630 -14.454 1.00 114.03 ? 41  HIS   X CE1 1 
ATOM   41288 N  NE2 . HIS   X  10 41  ? 20.265  -178.548 -15.217 1.00 114.48 ? 41  HIS   X NE2 1 
ATOM   41289 N  N   . THR   X  10 42  ? 22.299  -175.558 -9.286  1.00 98.02  ? 42  THR   X N   1 
ATOM   41290 C  CA  . THR   X  10 42  ? 22.276  -174.758 -8.027  1.00 95.48  ? 42  THR   X CA  1 
ATOM   41291 C  C   . THR   X  10 42  ? 23.580  -173.968 -7.860  1.00 92.67  ? 42  THR   X C   1 
ATOM   41292 O  O   . THR   X  10 42  ? 24.662  -174.586 -7.870  1.00 91.48  ? 42  THR   X O   1 
ATOM   41293 C  CB  . THR   X  10 42  ? 22.011  -175.629 -6.793  1.00 93.39  ? 42  THR   X CB  1 
ATOM   41294 O  OG1 . THR   X  10 42  ? 20.670  -176.108 -6.889  1.00 95.28  ? 42  THR   X OG1 1 
ATOM   41295 C  CG2 . THR   X  10 42  ? 22.176  -174.877 -5.491  1.00 94.09  ? 42  THR   X CG2 1 
ATOM   41296 N  N   . LEU   X  10 43  ? 23.447  -172.652 -7.673  1.00 91.65  ? 43  LEU   X N   1 
ATOM   41297 C  CA  . LEU   X  10 43  ? 24.555  -171.684 -7.466  1.00 91.62  ? 43  LEU   X CA  1 
ATOM   41298 C  C   . LEU   X  10 43  ? 24.312  -170.933 -6.154  1.00 89.21  ? 43  LEU   X C   1 
ATOM   41299 O  O   . LEU   X  10 43  ? 23.143  -170.579 -5.884  1.00 86.54  ? 43  LEU   X O   1 
ATOM   41300 C  CB  . LEU   X  10 43  ? 24.590  -170.717 -8.654  1.00 91.89  ? 43  LEU   X CB  1 
ATOM   41301 C  CG  . LEU   X  10 43  ? 25.755  -169.729 -8.679  1.00 92.83  ? 43  LEU   X CG  1 
ATOM   41302 C  CD1 . LEU   X  10 43  ? 27.075  -170.437 -8.937  1.00 93.66  ? 43  LEU   X CD1 1 
ATOM   41303 C  CD2 . LEU   X  10 43  ? 25.522  -168.656 -9.729  1.00 95.77  ? 43  LEU   X CD2 1 
ATOM   41304 N  N   . MET   X  10 44  ? 25.374  -170.701 -5.376  1.00 87.46  ? 44  MET   X N   1 
ATOM   41305 C  CA  . MET   X  10 44  ? 25.314  -169.957 -4.092  1.00 87.45  ? 44  MET   X CA  1 
ATOM   41306 C  C   . MET   X  10 44  ? 26.336  -168.817 -4.118  1.00 85.92  ? 44  MET   X C   1 
ATOM   41307 O  O   . MET   X  10 44  ? 27.529  -169.107 -4.310  1.00 89.08  ? 44  MET   X O   1 
ATOM   41308 C  CB  . MET   X  10 44  ? 25.609  -170.875 -2.901  1.00 87.95  ? 44  MET   X CB  1 
ATOM   41309 C  CG  . MET   X  10 44  ? 25.414  -170.187 -1.560  1.00 87.68  ? 44  MET   X CG  1 
ATOM   41310 S  SD  . MET   X  10 44  ? 25.423  -171.324 -0.154  1.00 88.69  ? 44  MET   X SD  1 
ATOM   41311 C  CE  . MET   X  10 44  ? 27.187  -171.554 0.070   1.00 90.58  ? 44  MET   X CE  1 
ATOM   41312 N  N   . SER   X  10 45  ? 25.871  -167.576 -3.935  1.00 87.19  ? 45  SER   X N   1 
ATOM   41313 C  CA  . SER   X  10 45  ? 26.707  -166.372 -3.684  1.00 89.21  ? 45  SER   X CA  1 
ATOM   41314 C  C   . SER   X  10 45  ? 26.783  -166.123 -2.176  1.00 82.87  ? 45  SER   X C   1 
ATOM   41315 O  O   . SER   X  10 45  ? 25.833  -166.503 -1.466  1.00 81.71  ? 45  SER   X O   1 
ATOM   41316 C  CB  . SER   X  10 45  ? 26.169  -165.165 -4.404  1.00 91.06  ? 45  SER   X CB  1 
ATOM   41317 O  OG  . SER   X  10 45  ? 24.893  -164.796 -3.903  1.00 96.88  ? 45  SER   X OG  1 
ATOM   41318 N  N   . PHE   X  10 46  ? 27.861  -165.490 -1.712  1.00 82.84  ? 46  PHE   X N   1 
ATOM   41319 C  CA  . PHE   X  10 46  ? 28.152  -165.302 -0.266  1.00 84.08  ? 46  PHE   X CA  1 
ATOM   41320 C  C   . PHE   X  10 46  ? 28.873  -163.971 -0.025  1.00 86.20  ? 46  PHE   X C   1 
ATOM   41321 O  O   . PHE   X  10 46  ? 29.690  -163.540 -0.867  1.00 90.62  ? 46  PHE   X O   1 
ATOM   41322 C  CB  . PHE   X  10 46  ? 28.972  -166.479 0.265   1.00 80.88  ? 46  PHE   X CB  1 
ATOM   41323 C  CG  . PHE   X  10 46  ? 30.138  -166.871 -0.604  1.00 80.91  ? 46  PHE   X CG  1 
ATOM   41324 C  CD1 . PHE   X  10 46  ? 31.362  -166.234 -0.486  1.00 81.13  ? 46  PHE   X CD1 1 
ATOM   41325 C  CD2 . PHE   X  10 46  ? 30.009  -167.879 -1.544  1.00 83.01  ? 46  PHE   X CD2 1 
ATOM   41326 C  CE1 . PHE   X  10 46  ? 32.433  -166.598 -1.289  1.00 82.29  ? 46  PHE   X CE1 1 
ATOM   41327 C  CE2 . PHE   X  10 46  ? 31.080  -168.243 -2.345  1.00 84.81  ? 46  PHE   X CE2 1 
ATOM   41328 C  CZ  . PHE   X  10 46  ? 32.290  -167.602 -2.218  1.00 83.56  ? 46  PHE   X CZ  1 
ATOM   41329 N  N   . ALA   X  10 47  ? 28.572  -163.348 1.117   1.00 86.73  ? 47  ALA   X N   1 
ATOM   41330 C  CA  . ALA   X  10 47  ? 29.202  -162.103 1.608   1.00 87.15  ? 47  ALA   X CA  1 
ATOM   41331 C  C   . ALA   X  10 47  ? 29.237  -162.132 3.140   1.00 85.51  ? 47  ALA   X C   1 
ATOM   41332 O  O   . ALA   X  10 47  ? 28.278  -162.653 3.746   1.00 85.19  ? 47  ALA   X O   1 
ATOM   41333 C  CB  . ALA   X  10 47  ? 28.451  -160.903 1.085   1.00 89.10  ? 47  ALA   X CB  1 
ATOM   41334 N  N   . GLY   X  10 48  ? 30.310  -161.602 3.732   1.00 84.40  ? 48  GLY   X N   1 
ATOM   41335 C  CA  . GLY   X  10 48  ? 30.496  -161.536 5.193   1.00 84.13  ? 48  GLY   X CA  1 
ATOM   41336 C  C   . GLY   X  10 48  ? 31.961  -161.572 5.584   1.00 85.68  ? 48  GLY   X C   1 
ATOM   41337 O  O   . GLY   X  10 48  ? 32.808  -161.173 4.760   1.00 84.14  ? 48  GLY   X O   1 
ATOM   41338 N  N   . GLU   X  10 49  ? 32.237  -162.058 6.798   1.00 87.09  ? 49  GLU   X N   1 
ATOM   41339 C  CA  . GLU   X  10 49  ? 33.563  -162.023 7.472   1.00 91.17  ? 49  GLU   X CA  1 
ATOM   41340 C  C   . GLU   X  10 49  ? 34.614  -162.694 6.582   1.00 86.51  ? 49  GLU   X C   1 
ATOM   41341 O  O   . GLU   X  10 49  ? 34.308  -163.746 6.000   1.00 83.16  ? 49  GLU   X O   1 
ATOM   41342 C  CB  . GLU   X  10 49  ? 33.450  -162.709 8.835   1.00 95.43  ? 49  GLU   X CB  1 
ATOM   41343 C  CG  . GLU   X  10 49  ? 34.765  -162.852 9.585   1.00 103.28 ? 49  GLU   X CG  1 
ATOM   41344 C  CD  . GLU   X  10 49  ? 35.424  -161.551 10.011  1.00 113.04 ? 49  GLU   X CD  1 
ATOM   41345 O  OE1 . GLU   X  10 49  ? 34.694  -160.568 10.261  1.00 121.87 ? 49  GLU   X OE1 1 
ATOM   41346 O  OE2 . GLU   X  10 49  ? 36.671  -161.525 10.097  1.00 121.45 ? 49  GLU   X OE2 1 
ATOM   41347 N  N   . ALA   X  10 50  ? 35.806  -162.097 6.491   1.00 87.29  ? 50  ALA   X N   1 
ATOM   41348 C  CA  . ALA   X  10 50  ? 36.955  -162.603 5.704   1.00 91.77  ? 50  ALA   X CA  1 
ATOM   41349 C  C   . ALA   X  10 50  ? 37.339  -163.996 6.212   1.00 92.03  ? 50  ALA   X C   1 
ATOM   41350 O  O   . ALA   X  10 50  ? 37.334  -164.198 7.443   1.00 97.28  ? 50  ALA   X O   1 
ATOM   41351 C  CB  . ALA   X  10 50  ? 38.116  -161.644 5.800   1.00 93.05  ? 50  ALA   X CB  1 
ATOM   41352 N  N   . GLY   X  10 51  ? 37.647  -164.919 5.296   1.00 92.26  ? 51  GLY   X N   1 
ATOM   41353 C  CA  . GLY   X  10 51  ? 37.984  -166.319 5.615   1.00 92.93  ? 51  GLY   X CA  1 
ATOM   41354 C  C   . GLY   X  10 51  ? 36.737  -167.170 5.792   1.00 92.19  ? 51  GLY   X C   1 
ATOM   41355 O  O   . GLY   X  10 51  ? 36.613  -168.185 5.076   1.00 93.50  ? 51  GLY   X O   1 
ATOM   41356 N  N   . ASP   X  10 52  ? 35.847  -166.769 6.708   1.00 91.91  ? 52  ASP   X N   1 
ATOM   41357 C  CA  . ASP   X  10 52  ? 34.565  -167.458 7.029   1.00 91.58  ? 52  ASP   X CA  1 
ATOM   41358 C  C   . ASP   X  10 52  ? 33.775  -167.741 5.744   1.00 89.28  ? 52  ASP   X C   1 
ATOM   41359 O  O   . ASP   X  10 52  ? 33.271  -168.868 5.610   1.00 89.08  ? 52  ASP   X O   1 
ATOM   41360 C  CB  . ASP   X  10 52  ? 33.708  -166.633 7.997   1.00 92.03  ? 52  ASP   X CB  1 
ATOM   41361 C  CG  . ASP   X  10 52  ? 34.129  -166.714 9.457   1.00 93.76  ? 52  ASP   X CG  1 
ATOM   41362 O  OD1 . ASP   X  10 52  ? 35.117  -167.414 9.751   1.00 94.26  ? 52  ASP   X OD1 1 
ATOM   41363 O  OD2 . ASP   X  10 52  ? 33.458  -166.073 10.296  1.00 94.22  ? 52  ASP   X OD2 1 
ATOM   41364 N  N   . THR   X  10 53  ? 33.662  -166.751 4.850   1.00 91.22  ? 53  THR   X N   1 
ATOM   41365 C  CA  . THR   X  10 53  ? 32.834  -166.798 3.611   1.00 89.57  ? 53  THR   X CA  1 
ATOM   41366 C  C   . THR   X  10 53  ? 33.224  -168.007 2.754   1.00 85.74  ? 53  THR   X C   1 
ATOM   41367 O  O   . THR   X  10 53  ? 32.373  -168.896 2.586   1.00 84.90  ? 53  THR   X O   1 
ATOM   41368 C  CB  . THR   X  10 53  ? 32.962  -165.501 2.804   1.00 91.60  ? 53  THR   X CB  1 
ATOM   41369 O  OG1 . THR   X  10 53  ? 34.348  -165.180 2.678   1.00 92.04  ? 53  THR   X OG1 1 
ATOM   41370 C  CG2 . THR   X  10 53  ? 32.225  -164.345 3.441   1.00 92.12  ? 53  THR   X CG2 1 
ATOM   41371 N  N   . VAL   X  10 54  ? 34.456  -168.031 2.239   1.00 85.63  ? 54  VAL   X N   1 
ATOM   41372 C  CA  . VAL   X  10 54  ? 34.949  -169.072 1.287   1.00 86.53  ? 54  VAL   X CA  1 
ATOM   41373 C  C   . VAL   X  10 54  ? 34.959  -170.433 1.999   1.00 87.37  ? 54  VAL   X C   1 
ATOM   41374 O  O   . VAL   X  10 54  ? 34.566  -171.430 1.362   1.00 86.40  ? 54  VAL   X O   1 
ATOM   41375 C  CB  . VAL   X  10 54  ? 36.334  -168.715 0.711   1.00 88.20  ? 54  VAL   X CB  1 
ATOM   41376 C  CG1 . VAL   X  10 54  ? 36.867  -169.812 -0.201  1.00 88.90  ? 54  VAL   X CG1 1 
ATOM   41377 C  CG2 . VAL   X  10 54  ? 36.314  -167.385 -0.027  1.00 88.47  ? 54  VAL   X CG2 1 
ATOM   41378 N  N   . GLN   X  10 55  ? 35.382  -170.470 3.267   1.00 86.68  ? 55  GLN   X N   1 
ATOM   41379 C  CA  . GLN   X  10 55  ? 35.461  -171.708 4.094   1.00 86.91  ? 55  GLN   X CA  1 
ATOM   41380 C  C   . GLN   X  10 55  ? 34.081  -172.372 4.177   1.00 86.67  ? 55  GLN   X C   1 
ATOM   41381 O  O   . GLN   X  10 55  ? 34.012  -173.597 3.992   1.00 89.28  ? 55  GLN   X O   1 
ATOM   41382 C  CB  . GLN   X  10 55  ? 35.996  -171.401 5.495   1.00 86.68  ? 55  GLN   X CB  1 
ATOM   41383 C  CG  . GLN   X  10 55  ? 37.516  -171.280 5.562   1.00 88.73  ? 55  GLN   X CG  1 
ATOM   41384 C  CD  . GLN   X  10 55  ? 38.286  -172.572 5.397   1.00 88.89  ? 55  GLN   X CD  1 
ATOM   41385 O  OE1 . GLN   X  10 55  ? 39.493  -172.560 5.163   1.00 89.33  ? 55  GLN   X OE1 1 
ATOM   41386 N  NE2 . GLN   X  10 55  ? 37.615  -173.707 5.526   1.00 89.67  ? 55  GLN   X NE2 1 
ATOM   41387 N  N   . PHE   X  10 56  ? 33.027  -171.595 4.445   1.00 84.63  ? 56  PHE   X N   1 
ATOM   41388 C  CA  . PHE   X  10 56  ? 31.626  -172.081 4.555   1.00 84.38  ? 56  PHE   X CA  1 
ATOM   41389 C  C   . PHE   X  10 56  ? 31.105  -172.500 3.174   1.00 85.34  ? 56  PHE   X C   1 
ATOM   41390 O  O   . PHE   X  10 56  ? 30.459  -173.552 3.080   1.00 88.41  ? 56  PHE   X O   1 
ATOM   41391 C  CB  . PHE   X  10 56  ? 30.712  -171.015 5.162   1.00 82.78  ? 56  PHE   X CB  1 
ATOM   41392 C  CG  . PHE   X  10 56  ? 29.267  -171.429 5.247   1.00 81.93  ? 56  PHE   X CG  1 
ATOM   41393 C  CD1 . PHE   X  10 56  ? 28.835  -172.291 6.242   1.00 81.71  ? 56  PHE   X CD1 1 
ATOM   41394 C  CD2 . PHE   X  10 56  ? 28.342  -170.972 4.322   1.00 85.01  ? 56  PHE   X CD2 1 
ATOM   41395 C  CE1 . PHE   X  10 56  ? 27.506  -172.679 6.314   1.00 83.69  ? 56  PHE   X CE1 1 
ATOM   41396 C  CE2 . PHE   X  10 56  ? 27.013  -171.360 4.395   1.00 86.21  ? 56  PHE   X CE2 1 
ATOM   41397 C  CZ  . PHE   X  10 56  ? 26.597  -172.214 5.391   1.00 85.29  ? 56  PHE   X CZ  1 
ATOM   41398 N  N   . ALA   X  10 57  ? 31.355  -171.688 2.143   1.00 87.52  ? 57  ALA   X N   1 
ATOM   41399 C  CA  . ALA   X  10 57  ? 30.923  -171.932 0.745   1.00 89.42  ? 57  ALA   X CA  1 
ATOM   41400 C  C   . ALA   X  10 57  ? 31.442  -173.294 0.269   1.00 88.60  ? 57  ALA   X C   1 
ATOM   41401 O  O   . ALA   X  10 57  ? 30.625  -174.100 -0.214  1.00 89.31  ? 57  ALA   X O   1 
ATOM   41402 C  CB  . ALA   X  10 57  ? 31.410  -170.821 -0.154  1.00 90.92  ? 57  ALA   X CB  1 
ATOM   41403 N  N   . GLU   X  10 58  ? 32.751  -173.530 0.405   1.00 88.57  ? 58  GLU   X N   1 
ATOM   41404 C  CA  . GLU   X  10 58  ? 33.440  -174.761 -0.069  1.00 90.05  ? 58  GLU   X CA  1 
ATOM   41405 C  C   . GLU   X  10 58  ? 32.985  -175.970 0.757   1.00 89.43  ? 58  GLU   X C   1 
ATOM   41406 O  O   . GLU   X  10 58  ? 32.873  -177.068 0.177   1.00 89.58  ? 58  GLU   X O   1 
ATOM   41407 C  CB  . GLU   X  10 58  ? 34.956  -174.592 0.010   1.00 92.94  ? 58  GLU   X CB  1 
ATOM   41408 C  CG  . GLU   X  10 58  ? 35.508  -173.633 -1.025  1.00 96.90  ? 58  GLU   X CG  1 
ATOM   41409 C  CD  . GLU   X  10 58  ? 37.021  -173.491 -1.000  1.00 101.64 ? 58  GLU   X CD  1 
ATOM   41410 O  OE1 . GLU   X  10 58  ? 37.679  -174.283 -0.290  1.00 106.04 ? 58  GLU   X OE1 1 
ATOM   41411 O  OE2 . GLU   X  10 58  ? 37.541  -172.589 -1.688  1.00 104.46 ? 58  GLU   X OE2 1 
ATOM   41412 N  N   . TYR   X  10 59  ? 32.748  -175.780 2.059   1.00 89.69  ? 59  TYR   X N   1 
ATOM   41413 C  CA  . TYR   X  10 59  ? 32.259  -176.834 2.986   1.00 89.94  ? 59  TYR   X CA  1 
ATOM   41414 C  C   . TYR   X  10 59  ? 30.879  -177.317 2.527   1.00 90.84  ? 59  TYR   X C   1 
ATOM   41415 O  O   . TYR   X  10 59  ? 30.678  -178.541 2.486   1.00 93.38  ? 59  TYR   X O   1 
ATOM   41416 C  CB  . TYR   X  10 59  ? 32.214  -176.335 4.432   1.00 89.78  ? 59  TYR   X CB  1 
ATOM   41417 C  CG  . TYR   X  10 59  ? 31.395  -177.204 5.351   1.00 92.46  ? 59  TYR   X CG  1 
ATOM   41418 C  CD1 . TYR   X  10 59  ? 31.786  -178.501 5.643   1.00 92.05  ? 59  TYR   X CD1 1 
ATOM   41419 C  CD2 . TYR   X  10 59  ? 30.219  -176.738 5.917   1.00 92.64  ? 59  TYR   X CD2 1 
ATOM   41420 C  CE1 . TYR   X  10 59  ? 31.037  -179.311 6.483   1.00 94.34  ? 59  TYR   X CE1 1 
ATOM   41421 C  CE2 . TYR   X  10 59  ? 29.459  -177.533 6.760   1.00 94.83  ? 59  TYR   X CE2 1 
ATOM   41422 C  CZ  . TYR   X  10 59  ? 29.869  -178.825 7.045   1.00 94.07  ? 59  TYR   X CZ  1 
ATOM   41423 O  OH  . TYR   X  10 59  ? 29.131  -179.621 7.875   1.00 94.89  ? 59  TYR   X OH  1 
ATOM   41424 N  N   . ILE   X  10 60  ? 29.968  -176.393 2.197   1.00 86.95  ? 60  ILE   X N   1 
ATOM   41425 C  CA  . ILE   X  10 60  ? 28.609  -176.713 1.655   1.00 87.13  ? 60  ILE   X CA  1 
ATOM   41426 C  C   . ILE   X  10 60  ? 28.766  -177.415 0.301   1.00 88.05  ? 60  ILE   X C   1 
ATOM   41427 O  O   . ILE   X  10 60  ? 28.070  -178.427 0.076   1.00 87.29  ? 60  ILE   X O   1 
ATOM   41428 C  CB  . ILE   X  10 60  ? 27.724  -175.453 1.534   1.00 86.26  ? 60  ILE   X CB  1 
ATOM   41429 C  CG1 . ILE   X  10 60  ? 27.404  -174.831 2.897   1.00 88.70  ? 60  ILE   X CG1 1 
ATOM   41430 C  CG2 . ILE   X  10 60  ? 26.453  -175.754 0.750   1.00 84.64  ? 60  ILE   X CG2 1 
ATOM   41431 C  CD1 . ILE   X  10 60  ? 26.731  -175.771 3.874   1.00 90.19  ? 60  ILE   X CD1 1 
ATOM   41432 N  N   . GLN   X  10 61  ? 29.633  -176.885 -0.566  1.00 85.72  ? 61  GLN   X N   1 
ATOM   41433 C  CA  . GLN   X  10 61  ? 29.888  -177.423 -1.928  1.00 86.70  ? 61  GLN   X CA  1 
ATOM   41434 C  C   . GLN   X  10 61  ? 30.288  -178.900 -1.826  1.00 87.70  ? 61  GLN   X C   1 
ATOM   41435 O  O   . GLN   X  10 61  ? 29.722  -179.716 -2.579  1.00 87.24  ? 61  GLN   X O   1 
ATOM   41436 C  CB  . GLN   X  10 61  ? 30.973  -176.607 -2.630  1.00 86.69  ? 61  GLN   X CB  1 
ATOM   41437 C  CG  . GLN   X  10 61  ? 31.218  -177.035 -4.068  1.00 87.60  ? 61  GLN   X CG  1 
ATOM   41438 C  CD  . GLN   X  10 61  ? 32.251  -176.163 -4.738  1.00 87.33  ? 61  GLN   X CD  1 
ATOM   41439 O  OE1 . GLN   X  10 61  ? 33.310  -175.888 -4.180  1.00 93.19  ? 61  GLN   X OE1 1 
ATOM   41440 N  NE2 . GLN   X  10 61  ? 31.952  -175.717 -5.946  1.00 84.80  ? 61  GLN   X NE2 1 
ATOM   41441 N  N   . ALA   X  10 62  ? 31.220  -179.226 -0.924  1.00 87.43  ? 62  ALA   X N   1 
ATOM   41442 C  CA  . ALA   X  10 62  ? 31.741  -180.597 -0.701  1.00 88.98  ? 62  ALA   X CA  1 
ATOM   41443 C  C   . ALA   X  10 62  ? 30.592  -181.526 -0.293  1.00 89.01  ? 62  ALA   X C   1 
ATOM   41444 O  O   . ALA   X  10 62  ? 30.519  -182.640 -0.843  1.00 90.81  ? 62  ALA   X O   1 
ATOM   41445 C  CB  . ALA   X  10 62  ? 32.836  -180.583 0.338   1.00 88.30  ? 62  ALA   X CB  1 
ATOM   41446 N  N   . ASN   X  10 63  ? 29.724  -181.074 0.620   1.00 89.70  ? 63  ASN   X N   1 
ATOM   41447 C  CA  . ASN   X  10 63  ? 28.598  -181.870 1.185   1.00 90.03  ? 63  ASN   X CA  1 
ATOM   41448 C  C   . ASN   X  10 63  ? 27.556  -182.180 0.102   1.00 88.94  ? 63  ASN   X C   1 
ATOM   41449 O  O   . ASN   X  10 63  ? 27.051  -183.316 0.096   1.00 89.22  ? 63  ASN   X O   1 
ATOM   41450 C  CB  . ASN   X  10 63  ? 27.935  -181.174 2.378   1.00 89.35  ? 63  ASN   X CB  1 
ATOM   41451 C  CG  . ASN   X  10 63  ? 28.566  -181.548 3.702   1.00 90.03  ? 63  ASN   X CG  1 
ATOM   41452 O  OD1 . ASN   X  10 63  ? 29.127  -180.701 4.390   1.00 90.21  ? 63  ASN   X OD1 1 
ATOM   41453 N  ND2 . ASN   X  10 63  ? 28.482  -182.816 4.070   1.00 91.51  ? 63  ASN   X ND2 1 
ATOM   41454 N  N   . ILE   X  10 64  ? 27.226  -181.211 -0.759  1.00 90.46  ? 64  ILE   X N   1 
ATOM   41455 C  CA  . ILE   X  10 64  ? 26.215  -181.387 -1.846  1.00 92.41  ? 64  ILE   X CA  1 
ATOM   41456 C  C   . ILE   X  10 64  ? 26.803  -182.309 -2.922  1.00 93.34  ? 64  ILE   X C   1 
ATOM   41457 O  O   . ILE   X  10 64  ? 26.056  -183.171 -3.425  1.00 95.44  ? 64  ILE   X O   1 
ATOM   41458 C  CB  . ILE   X  10 64  ? 25.756  -180.033 -2.429  1.00 93.76  ? 64  ILE   X CB  1 
ATOM   41459 C  CG1 . ILE   X  10 64  ? 25.133  -179.123 -1.364  1.00 92.72  ? 64  ILE   X CG1 1 
ATOM   41460 C  CG2 . ILE   X  10 64  ? 24.808  -180.246 -3.603  1.00 94.80  ? 64  ILE   X CG2 1 
ATOM   41461 C  CD1 . ILE   X  10 64  ? 23.964  -179.734 -0.620  1.00 95.13  ? 64  ILE   X CD1 1 
ATOM   41462 N  N   . GLN   X  10 65  ? 28.085  -182.135 -3.257  1.00 92.49  ? 65  GLN   X N   1 
ATOM   41463 C  CA  . GLN   X  10 65  ? 28.812  -182.989 -4.236  1.00 93.94  ? 65  GLN   X CA  1 
ATOM   41464 C  C   . GLN   X  10 65  ? 28.914  -184.426 -3.703  1.00 95.26  ? 65  GLN   X C   1 
ATOM   41465 O  O   . GLN   X  10 65  ? 28.793  -185.356 -4.526  1.00 96.20  ? 65  GLN   X O   1 
ATOM   41466 C  CB  . GLN   X  10 65  ? 30.195  -182.409 -4.540  1.00 92.88  ? 65  GLN   X CB  1 
ATOM   41467 C  CG  . GLN   X  10 65  ? 30.155  -181.193 -5.455  1.00 92.26  ? 65  GLN   X CG  1 
ATOM   41468 C  CD  . GLN   X  10 65  ? 31.517  -180.575 -5.667  1.00 90.80  ? 65  GLN   X CD  1 
ATOM   41469 O  OE1 . GLN   X  10 65  ? 32.540  -181.116 -5.257  1.00 92.70  ? 65  GLN   X OE1 1 
ATOM   41470 N  NE2 . GLN   X  10 65  ? 31.543  -179.424 -6.318  1.00 90.44  ? 65  GLN   X NE2 1 
ATOM   41471 N  N   . LEU   X  10 66  ? 29.135  -184.602 -2.392  1.00 95.78  ? 66  LEU   X N   1 
ATOM   41472 C  CA  . LEU   X  10 66  ? 29.182  -185.933 -1.722  1.00 95.92  ? 66  LEU   X CA  1 
ATOM   41473 C  C   . LEU   X  10 66  ? 27.813  -186.607 -1.849  1.00 95.06  ? 66  LEU   X C   1 
ATOM   41474 O  O   . LEU   X  10 66  ? 27.783  -187.807 -2.160  1.00 99.52  ? 66  LEU   X O   1 
ATOM   41475 C  CB  . LEU   X  10 66  ? 29.573  -185.786 -0.245  1.00 95.56  ? 66  LEU   X CB  1 
ATOM   41476 C  CG  . LEU   X  10 66  ? 29.585  -187.082 0.568   1.00 96.00  ? 66  LEU   X CG  1 
ATOM   41477 C  CD1 . LEU   X  10 66  ? 30.569  -188.091 -0.011  1.00 97.92  ? 66  LEU   X CD1 1 
ATOM   41478 C  CD2 . LEU   X  10 66  ? 29.910  -186.806 2.026   1.00 94.80  ? 66  LEU   X CD2 1 
ATOM   41479 N  N   . TYR   X  10 67  ? 26.730  -185.862 -1.604  1.00 92.85  ? 67  TYR   X N   1 
ATOM   41480 C  CA  . TYR   X  10 67  ? 25.331  -186.350 -1.719  1.00 92.83  ? 67  TYR   X CA  1 
ATOM   41481 C  C   . TYR   X  10 67  ? 25.062  -186.794 -3.160  1.00 95.47  ? 67  TYR   X C   1 
ATOM   41482 O  O   . TYR   X  10 67  ? 24.493  -187.885 -3.356  1.00 97.66  ? 67  TYR   X O   1 
ATOM   41483 C  CB  . TYR   X  10 67  ? 24.323  -185.277 -1.302  1.00 91.57  ? 67  TYR   X CB  1 
ATOM   41484 C  CG  . TYR   X  10 67  ? 22.918  -185.799 -1.134  1.00 92.52  ? 67  TYR   X CG  1 
ATOM   41485 C  CD1 . TYR   X  10 67  ? 22.137  -186.124 -2.233  1.00 92.68  ? 67  TYR   X CD1 1 
ATOM   41486 C  CD2 . TYR   X  10 67  ? 22.371  -185.986 0.125   1.00 92.79  ? 67  TYR   X CD2 1 
ATOM   41487 C  CE1 . TYR   X  10 67  ? 20.851  -186.616 -2.088  1.00 94.08  ? 67  TYR   X CE1 1 
ATOM   41488 C  CE2 . TYR   X  10 67  ? 21.084  -186.472 0.289   1.00 94.95  ? 67  TYR   X CE2 1 
ATOM   41489 C  CZ  . TYR   X  10 67  ? 20.321  -186.789 -0.822  1.00 95.66  ? 67  TYR   X CZ  1 
ATOM   41490 O  OH  . TYR   X  10 67  ? 19.053  -187.272 -0.680  1.00 98.53  ? 67  TYR   X OH  1 
ATOM   41491 N  N   . SER   X  10 68  ? 25.439  -185.956 -4.132  1.00 95.30  ? 68  SER   X N   1 
ATOM   41492 C  CA  . SER   X  10 68  ? 25.282  -186.214 -5.589  1.00 98.76  ? 68  SER   X CA  1 
ATOM   41493 C  C   . SER   X  10 68  ? 25.888  -187.574 -5.954  1.00 100.10 ? 68  SER   X C   1 
ATOM   41494 O  O   . SER   X  10 68  ? 25.179  -188.387 -6.578  1.00 102.70 ? 68  SER   X O   1 
ATOM   41495 C  CB  . SER   X  10 68  ? 25.888  -185.106 -6.408  1.00 98.96  ? 68  SER   X CB  1 
ATOM   41496 O  OG  . SER   X  10 68  ? 25.101  -183.926 -6.319  1.00 98.77  ? 68  SER   X OG  1 
ATOM   41497 N  N   . ILE   X  10 69  ? 27.143  -187.808 -5.559  1.00 99.63  ? 69  ILE   X N   1 
ATOM   41498 C  CA  . ILE   X  10 69  ? 27.918  -189.040 -5.894  1.00 101.38 ? 69  ILE   X CA  1 
ATOM   41499 C  C   . ILE   X  10 69  ? 27.281  -190.248 -5.194  1.00 101.62 ? 69  ILE   X C   1 
ATOM   41500 O  O   . ILE   X  10 69  ? 27.273  -191.328 -5.811  1.00 108.12 ? 69  ILE   X O   1 
ATOM   41501 C  CB  . ILE   X  10 69  ? 29.415  -188.860 -5.552  1.00 102.75 ? 69  ILE   X CB  1 
ATOM   41502 C  CG1 . ILE   X  10 69  ? 30.148  -188.065 -6.638  1.00 104.33 ? 69  ILE   X CG1 1 
ATOM   41503 C  CG2 . ILE   X  10 69  ? 30.104  -190.190 -5.286  1.00 105.51 ? 69  ILE   X CG2 1 
ATOM   41504 C  CD1 . ILE   X  10 69  ? 30.199  -188.745 -7.995  1.00 104.76 ? 69  ILE   X CD1 1 
ATOM   41505 N  N   . ARG   X  10 70  ? 26.750  -190.080 -3.977  1.00 100.13 ? 70  ARG   X N   1 
ATOM   41506 C  CA  . ARG   X  10 70  ? 26.186  -191.196 -3.169  1.00 102.18 ? 70  ARG   X CA  1 
ATOM   41507 C  C   . ARG   X  10 70  ? 24.886  -191.697 -3.806  1.00 100.06 ? 70  ARG   X C   1 
ATOM   41508 O  O   . ARG   X  10 70  ? 24.767  -192.916 -3.990  1.00 103.61 ? 70  ARG   X O   1 
ATOM   41509 C  CB  . ARG   X  10 70  ? 25.928  -190.781 -1.716  1.00 102.21 ? 70  ARG   X CB  1 
ATOM   41510 C  CG  . ARG   X  10 70  ? 25.449  -191.922 -0.829  1.00 106.11 ? 70  ARG   X CG  1 
ATOM   41511 C  CD  . ARG   X  10 70  ? 25.162  -191.494 0.597   1.00 105.10 ? 70  ARG   X CD  1 
ATOM   41512 N  NE  . ARG   X  10 70  ? 26.364  -191.029 1.278   1.00 103.31 ? 70  ARG   X NE  1 
ATOM   41513 C  CZ  . ARG   X  10 70  ? 26.568  -189.798 1.738   1.00 102.48 ? 70  ARG   X CZ  1 
ATOM   41514 N  NH1 . ARG   X  10 70  ? 25.641  -188.862 1.612   1.00 105.78 ? 70  ARG   X NH1 1 
ATOM   41515 N  NH2 . ARG   X  10 70  ? 27.709  -189.506 2.337   1.00 103.69 ? 70  ARG   X NH2 1 
ATOM   41516 N  N   . GLU   X  10 71  ? 23.949  -190.797 -4.116  1.00 98.57  ? 71  GLU   X N   1 
ATOM   41517 C  CA  . GLU   X  10 71  ? 22.567  -191.145 -4.547  1.00 100.30 ? 71  GLU   X CA  1 
ATOM   41518 C  C   . GLU   X  10 71  ? 22.441  -191.121 -6.077  1.00 100.54 ? 71  GLU   X C   1 
ATOM   41519 O  O   . GLU   X  10 71  ? 21.350  -191.479 -6.572  1.00 99.20  ? 71  GLU   X O   1 
ATOM   41520 C  CB  . GLU   X  10 71  ? 21.553  -190.173 -3.940  1.00 100.41 ? 71  GLU   X CB  1 
ATOM   41521 C  CG  . GLU   X  10 71  ? 21.684  -190.000 -2.437  1.00 101.77 ? 71  GLU   X CG  1 
ATOM   41522 C  CD  . GLU   X  10 71  ? 21.523  -191.268 -1.619  1.00 102.53 ? 71  GLU   X CD  1 
ATOM   41523 O  OE1 . GLU   X  10 71  ? 22.011  -191.293 -0.473  1.00 108.41 ? 71  GLU   X OE1 1 
ATOM   41524 O  OE2 . GLU   X  10 71  ? 20.902  -192.222 -2.124  1.00 104.53 ? 71  GLU   X OE2 1 
ATOM   41525 N  N   . ASP   X  10 72  ? 23.496  -190.718 -6.796  1.00 102.87 ? 72  ASP   X N   1 
ATOM   41526 C  CA  . ASP   X  10 72  ? 23.478  -190.510 -8.270  1.00 104.33 ? 72  ASP   X CA  1 
ATOM   41527 C  C   . ASP   X  10 72  ? 22.261  -189.648 -8.628  1.00 103.76 ? 72  ASP   X C   1 
ATOM   41528 O  O   . ASP   X  10 72  ? 21.472  -190.062 -9.503  1.00 103.63 ? 72  ASP   X O   1 
ATOM   41529 C  CB  . ASP   X  10 72  ? 23.460  -191.847 -9.018  1.00 106.06 ? 72  ASP   X CB  1 
ATOM   41530 C  CG  . ASP   X  10 72  ? 23.704  -191.714 -10.513 1.00 107.98 ? 72  ASP   X CG  1 
ATOM   41531 O  OD1 . ASP   X  10 72  ? 24.546  -190.878 -10.896 1.00 107.06 ? 72  ASP   X OD1 1 
ATOM   41532 O  OD2 . ASP   X  10 72  ? 23.047  -192.444 -11.284 1.00 113.45 ? 72  ASP   X OD2 1 
ATOM   41533 N  N   . TYR   X  10 73  ? 22.109  -188.499 -7.962  1.00 102.51 ? 73  TYR   X N   1 
ATOM   41534 C  CA  . TYR   X  10 73  ? 20.888  -187.653 -8.010  1.00 104.18 ? 73  TYR   X CA  1 
ATOM   41535 C  C   . TYR   X  10 73  ? 21.195  -186.238 -7.514  1.00 104.02 ? 73  TYR   X C   1 
ATOM   41536 O  O   . TYR   X  10 73  ? 22.000  -186.088 -6.575  1.00 107.41 ? 73  TYR   X O   1 
ATOM   41537 C  CB  . TYR   X  10 73  ? 19.787  -188.272 -7.147  1.00 103.29 ? 73  TYR   X CB  1 
ATOM   41538 C  CG  . TYR   X  10 73  ? 18.387  -187.833 -7.489  1.00 104.16 ? 73  TYR   X CG  1 
ATOM   41539 C  CD1 . TYR   X  10 73  ? 17.803  -188.202 -8.690  1.00 107.57 ? 73  TYR   X CD1 1 
ATOM   41540 C  CD2 . TYR   X  10 73  ? 17.633  -187.077 -6.605  1.00 101.42 ? 73  TYR   X CD2 1 
ATOM   41541 C  CE1 . TYR   X  10 73  ? 16.512  -187.818 -9.015  1.00 107.87 ? 73  TYR   X CE1 1 
ATOM   41542 C  CE2 . TYR   X  10 73  ? 16.340  -186.687 -6.913  1.00 103.93 ? 73  TYR   X CE2 1 
ATOM   41543 C  CZ  . TYR   X  10 73  ? 15.778  -187.058 -8.122  1.00 106.52 ? 73  TYR   X CZ  1 
ATOM   41544 O  OH  . TYR   X  10 73  ? 14.506  -186.677 -8.433  1.00 109.20 ? 73  TYR   X OH  1 
ATOM   41545 N  N   . GLU   X  10 74  ? 20.539  -185.241 -8.114  1.00 102.57 ? 74  GLU   X N   1 
ATOM   41546 C  CA  . GLU   X  10 74  ? 20.670  -183.803 -7.760  1.00 100.15 ? 74  GLU   X CA  1 
ATOM   41547 C  C   . GLU   X  10 74  ? 19.543  -183.413 -6.792  1.00 96.79  ? 74  GLU   X C   1 
ATOM   41548 O  O   . GLU   X  10 74  ? 18.360  -183.548 -7.171  1.00 92.67  ? 74  GLU   X O   1 
ATOM   41549 C  CB  . GLU   X  10 74  ? 20.637  -182.949 -9.029  1.00 101.02 ? 74  GLU   X CB  1 
ATOM   41550 C  CG  . GLU   X  10 74  ? 20.809  -181.462 -8.774  1.00 100.82 ? 74  GLU   X CG  1 
ATOM   41551 C  CD  . GLU   X  10 74  ? 20.951  -180.611 -10.026 1.00 102.50 ? 74  GLU   X CD  1 
ATOM   41552 O  OE1 . GLU   X  10 74  ? 21.520  -179.503 -9.923  1.00 103.19 ? 74  GLU   X OE1 1 
ATOM   41553 O  OE2 . GLU   X  10 74  ? 20.488  -181.056 -11.099 1.00 98.14  ? 74  GLU   X OE2 1 
ATOM   41554 N  N   . LEU   X  10 75  ? 19.909  -182.952 -5.591  1.00 95.14  ? 75  LEU   X N   1 
ATOM   41555 C  CA  . LEU   X  10 75  ? 18.984  -182.365 -4.580  1.00 95.52  ? 75  LEU   X CA  1 
ATOM   41556 C  C   . LEU   X  10 75  ? 18.273  -181.146 -5.175  1.00 92.66  ? 75  LEU   X C   1 
ATOM   41557 O  O   . LEU   X  10 75  ? 18.940  -180.352 -5.872  1.00 88.93  ? 75  LEU   X O   1 
ATOM   41558 C  CB  . LEU   X  10 75  ? 19.788  -181.939 -3.346  1.00 97.75  ? 75  LEU   X CB  1 
ATOM   41559 C  CG  . LEU   X  10 75  ? 19.468  -182.620 -2.013  1.00 100.57 ? 75  LEU   X CG  1 
ATOM   41560 C  CD1 . LEU   X  10 75  ? 18.881  -184.013 -2.185  1.00 102.92 ? 75  LEU   X CD1 1 
ATOM   41561 C  CD2 . LEU   X  10 75  ? 20.716  -182.672 -1.145  1.00 103.22 ? 75  LEU   X CD2 1 
ATOM   41562 N  N   . SER   X  10 76  ? 16.984  -180.981 -4.864  1.00 92.09  ? 76  SER   X N   1 
ATOM   41563 C  CA  . SER   X  10 76  ? 16.160  -179.818 -5.285  1.00 93.28  ? 76  SER   X CA  1 
ATOM   41564 C  C   . SER   X  10 76  ? 16.747  -178.549 -4.671  1.00 92.04  ? 76  SER   X C   1 
ATOM   41565 O  O   . SER   X  10 76  ? 17.365  -178.607 -3.609  1.00 90.40  ? 76  SER   X O   1 
ATOM   41566 C  CB  . SER   X  10 76  ? 14.712  -179.999 -4.903  1.00 93.25  ? 76  SER   X CB  1 
ATOM   41567 O  OG  . SER   X  10 76  ? 14.519  -179.787 -3.512  1.00 91.90  ? 76  SER   X OG  1 
ATOM   41568 N  N   . PRO   X  10 77  ? 16.600  -177.372 -5.324  1.00 94.22  ? 77  PRO   X N   1 
ATOM   41569 C  CA  . PRO   X  10 77  ? 17.015  -176.106 -4.719  1.00 92.69  ? 77  PRO   X CA  1 
ATOM   41570 C  C   . PRO   X  10 77  ? 16.446  -175.910 -3.305  1.00 89.97  ? 77  PRO   X C   1 
ATOM   41571 O  O   . PRO   X  10 77  ? 17.179  -175.447 -2.457  1.00 93.18  ? 77  PRO   X O   1 
ATOM   41572 C  CB  . PRO   X  10 77  ? 16.465  -175.053 -5.690  1.00 93.45  ? 77  PRO   X CB  1 
ATOM   41573 C  CG  . PRO   X  10 77  ? 16.439  -175.766 -7.024  1.00 94.28  ? 77  PRO   X CG  1 
ATOM   41574 C  CD  . PRO   X  10 77  ? 16.081  -177.200 -6.690  1.00 94.79  ? 77  PRO   X CD  1 
ATOM   41575 N  N   . GLN   X  10 78  ? 15.179  -176.284 -3.089  1.00 91.17  ? 78  GLN   X N   1 
ATOM   41576 C  CA  . GLN   X  10 78  ? 14.485  -176.192 -1.773  1.00 90.52  ? 78  GLN   X CA  1 
ATOM   41577 C  C   . GLN   X  10 78  ? 15.260  -177.017 -0.737  1.00 87.92  ? 78  GLN   X C   1 
ATOM   41578 O  O   . GLN   X  10 78  ? 15.532  -176.489 0.356   1.00 82.57  ? 78  GLN   X O   1 
ATOM   41579 C  CB  . GLN   X  10 78  ? 13.033  -176.668 -1.891  1.00 93.11  ? 78  GLN   X CB  1 
ATOM   41580 C  CG  . GLN   X  10 78  ? 12.133  -176.206 -0.749  1.00 93.28  ? 78  GLN   X CG  1 
ATOM   41581 C  CD  . GLN   X  10 78  ? 12.462  -176.848 0.576   1.00 94.42  ? 78  GLN   X CD  1 
ATOM   41582 O  OE1 . GLN   X  10 78  ? 12.712  -176.169 1.569   1.00 94.62  ? 78  GLN   X OE1 1 
ATOM   41583 N  NE2 . GLN   X  10 78  ? 12.472  -178.171 0.604   1.00 94.01  ? 78  GLN   X NE2 1 
ATOM   41584 N  N   . ALA   X  10 79  ? 15.602  -178.263 -1.077  1.00 89.63  ? 79  ALA   X N   1 
ATOM   41585 C  CA  . ALA   X  10 79  ? 16.314  -179.219 -0.196  1.00 89.83  ? 79  ALA   X CA  1 
ATOM   41586 C  C   . ALA   X  10 79  ? 17.693  -178.661 0.174   1.00 87.40  ? 79  ALA   X C   1 
ATOM   41587 O  O   . ALA   X  10 79  ? 18.034  -178.695 1.371   1.00 85.62  ? 79  ALA   X O   1 
ATOM   41588 C  CB  . ALA   X  10 79  ? 16.420  -180.570 -0.864  1.00 92.38  ? 79  ALA   X CB  1 
ATOM   41589 N  N   . VAL   X  10 80  ? 18.450  -178.167 -0.812  1.00 86.06  ? 80  VAL   X N   1 
ATOM   41590 C  CA  . VAL   X  10 80  ? 19.817  -177.596 -0.613  1.00 87.47  ? 80  VAL   X CA  1 
ATOM   41591 C  C   . VAL   X  10 80  ? 19.717  -176.384 0.321   1.00 86.94  ? 80  VAL   X C   1 
ATOM   41592 O  O   . VAL   X  10 80  ? 20.548  -176.271 1.247   1.00 85.59  ? 80  VAL   X O   1 
ATOM   41593 C  CB  . VAL   X  10 80  ? 20.482  -177.214 -1.950  1.00 87.50  ? 80  VAL   X CB  1 
ATOM   41594 C  CG1 . VAL   X  10 80  ? 21.712  -176.344 -1.740  1.00 87.76  ? 80  VAL   X CG1 1 
ATOM   41595 C  CG2 . VAL   X  10 80  ? 20.842  -178.441 -2.770  1.00 89.81  ? 80  VAL   X CG2 1 
ATOM   41596 N  N   . SER   X  10 81  ? 18.749  -175.500 0.074   1.00 88.89  ? 81  SER   X N   1 
ATOM   41597 C  CA  . SER   X  10 81  ? 18.516  -174.270 0.873   1.00 90.65  ? 81  SER   X CA  1 
ATOM   41598 C  C   . SER   X  10 81  ? 18.256  -174.654 2.335   1.00 90.91  ? 81  SER   X C   1 
ATOM   41599 O  O   . SER   X  10 81  ? 18.824  -173.999 3.227   1.00 93.63  ? 81  SER   X O   1 
ATOM   41600 C  CB  . SER   X  10 81  ? 17.391  -173.445 0.301   1.00 93.21  ? 81  SER   X CB  1 
ATOM   41601 O  OG  . SER   X  10 81  ? 16.130  -174.009 0.628   1.00 97.48  ? 81  SER   X OG  1 
ATOM   41602 N  N   . SER   X  10 82  ? 17.451  -175.695 2.569   1.00 89.33  ? 82  SER   X N   1 
ATOM   41603 C  CA  . SER   X  10 82  ? 17.059  -176.170 3.923   1.00 88.29  ? 82  SER   X CA  1 
ATOM   41604 C  C   . SER   X  10 82  ? 18.279  -176.749 4.649   1.00 85.97  ? 82  SER   X C   1 
ATOM   41605 O  O   . SER   X  10 82  ? 18.385  -176.543 5.873   1.00 85.43  ? 82  SER   X O   1 
ATOM   41606 C  CB  . SER   X  10 82  ? 15.937  -177.171 3.856   1.00 88.64  ? 82  SER   X CB  1 
ATOM   41607 O  OG  . SER   X  10 82  ? 14.743  -176.559 3.392   1.00 91.31  ? 82  SER   X OG  1 
ATOM   41608 N  N   . PHE   X  10 83  ? 19.151  -177.459 3.926   1.00 85.46  ? 83  PHE   X N   1 
ATOM   41609 C  CA  . PHE   X  10 83  ? 20.439  -177.984 4.450   1.00 85.41  ? 83  PHE   X CA  1 
ATOM   41610 C  C   . PHE   X  10 83  ? 21.299  -176.800 4.903   1.00 83.27  ? 83  PHE   X C   1 
ATOM   41611 O  O   . PHE   X  10 83  ? 21.743  -176.788 6.065   1.00 84.02  ? 83  PHE   X O   1 
ATOM   41612 C  CB  . PHE   X  10 83  ? 21.171  -178.830 3.403   1.00 82.31  ? 83  PHE   X CB  1 
ATOM   41613 C  CG  . PHE   X  10 83  ? 22.568  -179.237 3.801   1.00 80.48  ? 83  PHE   X CG  1 
ATOM   41614 C  CD1 . PHE   X  10 83  ? 22.774  -180.172 4.804   1.00 81.96  ? 83  PHE   X CD1 1 
ATOM   41615 C  CD2 . PHE   X  10 83  ? 23.677  -178.685 3.177   1.00 80.53  ? 83  PHE   X CD2 1 
ATOM   41616 C  CE1 . PHE   X  10 83  ? 24.057  -180.547 5.174   1.00 82.28  ? 83  PHE   X CE1 1 
ATOM   41617 C  CE2 . PHE   X  10 83  ? 24.959  -179.060 3.549   1.00 81.83  ? 83  PHE   X CE2 1 
ATOM   41618 C  CZ  . PHE   X  10 83  ? 25.147  -179.991 4.546   1.00 82.52  ? 83  PHE   X CZ  1 
ATOM   41619 N  N   . VAL   X  10 84  ? 21.496  -175.825 4.012   1.00 85.78  ? 84  VAL   X N   1 
ATOM   41620 C  CA  . VAL   X  10 84  ? 22.382  -174.645 4.244   1.00 85.46  ? 84  VAL   X CA  1 
ATOM   41621 C  C   . VAL   X  10 84  ? 21.844  -173.835 5.429   1.00 85.67  ? 84  VAL   X C   1 
ATOM   41622 O  O   . VAL   X  10 84  ? 22.672  -173.400 6.257   1.00 85.41  ? 84  VAL   X O   1 
ATOM   41623 C  CB  . VAL   X  10 84  ? 22.524  -173.778 2.978   1.00 86.85  ? 84  VAL   X CB  1 
ATOM   41624 C  CG1 . VAL   X  10 84  ? 23.174  -172.434 3.278   1.00 85.93  ? 84  VAL   X CG1 1 
ATOM   41625 C  CG2 . VAL   X  10 84  ? 23.295  -174.512 1.890   1.00 87.00  ? 84  VAL   X CG2 1 
ATOM   41626 N  N   . ARG   X  10 85  ? 20.523  -173.635 5.507   1.00 85.34  ? 85  ARG   X N   1 
ATOM   41627 C  CA  . ARG   X  10 85  ? 19.877  -172.898 6.626   1.00 85.47  ? 85  ARG   X CA  1 
ATOM   41628 C  C   . ARG   X  10 85  ? 20.228  -173.579 7.951   1.00 87.54  ? 85  ARG   X C   1 
ATOM   41629 O  O   . ARG   X  10 85  ? 20.637  -172.865 8.885   1.00 86.51  ? 85  ARG   X O   1 
ATOM   41630 C  CB  . ARG   X  10 85  ? 18.354  -172.834 6.487   1.00 86.29  ? 85  ARG   X CB  1 
ATOM   41631 C  CG  . ARG   X  10 85  ? 17.717  -171.802 7.408   1.00 86.87  ? 85  ARG   X CG  1 
ATOM   41632 C  CD  . ARG   X  10 85  ? 16.285  -172.127 7.777   1.00 85.60  ? 85  ARG   X CD  1 
ATOM   41633 N  NE  . ARG   X  10 85  ? 16.196  -173.095 8.863   1.00 84.32  ? 85  ARG   X NE  1 
ATOM   41634 C  CZ  . ARG   X  10 85  ? 16.281  -172.805 10.159  1.00 82.96  ? 85  ARG   X CZ  1 
ATOM   41635 N  NH1 . ARG   X  10 85  ? 16.473  -171.563 10.564  1.00 83.82  ? 85  ARG   X NH1 1 
ATOM   41636 N  NH2 . ARG   X  10 85  ? 16.172  -173.767 11.056  1.00 84.39  ? 85  ARG   X NH2 1 
ATOM   41637 N  N   . GLN   X  10 86  ? 20.069  -174.906 8.021   1.00 90.06  ? 86  GLN   X N   1 
ATOM   41638 C  CA  . GLN   X  10 86  ? 20.260  -175.705 9.262   1.00 90.31  ? 86  GLN   X CA  1 
ATOM   41639 C  C   . GLN   X  10 86  ? 21.723  -175.628 9.708   1.00 89.78  ? 86  GLN   X C   1 
ATOM   41640 O  O   . GLN   X  10 86  ? 21.954  -175.581 10.929  1.00 91.56  ? 86  GLN   X O   1 
ATOM   41641 C  CB  . GLN   X  10 86  ? 19.858  -177.167 9.073   1.00 91.77  ? 86  GLN   X CB  1 
ATOM   41642 C  CG  . GLN   X  10 86  ? 19.747  -177.910 10.396  1.00 95.14  ? 86  GLN   X CG  1 
ATOM   41643 C  CD  . GLN   X  10 86  ? 19.467  -179.382 10.229  1.00 98.13  ? 86  GLN   X CD  1 
ATOM   41644 O  OE1 . GLN   X  10 86  ? 20.128  -180.080 9.462   1.00 102.98 ? 86  GLN   X OE1 1 
ATOM   41645 N  NE2 . GLN   X  10 86  ? 18.486  -179.872 10.968  1.00 99.09  ? 86  GLN   X NE2 1 
ATOM   41646 N  N   . GLU   X  10 87  ? 22.663  -175.631 8.759   1.00 89.14  ? 87  GLU   X N   1 
ATOM   41647 C  CA  . GLU   X  10 87  ? 24.121  -175.536 9.040   1.00 90.30  ? 87  GLU   X CA  1 
ATOM   41648 C  C   . GLU   X  10 87  ? 24.421  -174.186 9.698   1.00 89.69  ? 87  GLU   X C   1 
ATOM   41649 O  O   . GLU   X  10 87  ? 25.181  -174.172 10.687  1.00 90.38  ? 87  GLU   X O   1 
ATOM   41650 C  CB  . GLU   X  10 87  ? 24.944  -175.724 7.765   1.00 92.04  ? 87  GLU   X CB  1 
ATOM   41651 C  CG  . GLU   X  10 87  ? 25.037  -177.173 7.328   1.00 93.60  ? 87  GLU   X CG  1 
ATOM   41652 C  CD  . GLU   X  10 87  ? 25.689  -178.085 8.353   1.00 95.03  ? 87  GLU   X CD  1 
ATOM   41653 O  OE1 . GLU   X  10 87  ? 26.836  -177.800 8.750   1.00 98.17  ? 87  GLU   X OE1 1 
ATOM   41654 O  OE2 . GLU   X  10 87  ? 25.037  -179.062 8.770   1.00 98.63  ? 87  GLU   X OE2 1 
ATOM   41655 N  N   . LEU   X  10 88  ? 23.843  -173.102 9.171   1.00 88.49  ? 88  LEU   X N   1 
ATOM   41656 C  CA  . LEU   X  10 88  ? 23.998  -171.737 9.738   1.00 87.81  ? 88  LEU   X CA  1 
ATOM   41657 C  C   . LEU   X  10 88  ? 23.280  -171.678 11.094  1.00 86.44  ? 88  LEU   X C   1 
ATOM   41658 O  O   . LEU   X  10 88  ? 23.872  -171.129 12.040  1.00 88.01  ? 88  LEU   X O   1 
ATOM   41659 C  CB  . LEU   X  10 88  ? 23.466  -170.696 8.743   1.00 86.95  ? 88  LEU   X CB  1 
ATOM   41660 C  CG  . LEU   X  10 88  ? 24.362  -170.430 7.532   1.00 85.45  ? 88  LEU   X CG  1 
ATOM   41661 C  CD1 . LEU   X  10 88  ? 23.633  -169.614 6.475   1.00 85.05  ? 88  LEU   X CD1 1 
ATOM   41662 C  CD2 . LEU   X  10 88  ? 25.651  -169.730 7.940   1.00 84.96  ? 88  LEU   X CD2 1 
ATOM   41663 N  N   . ALA   X  10 89  ? 22.079  -172.260 11.201  1.00 84.74  ? 89  ALA   X N   1 
ATOM   41664 C  CA  . ALA   X  10 89  ? 21.250  -172.259 12.432  1.00 85.53  ? 89  ALA   X CA  1 
ATOM   41665 C  C   . ALA   X  10 89  ? 21.996  -172.976 13.567  1.00 88.21  ? 89  ALA   X C   1 
ATOM   41666 O  O   . ALA   X  10 89  ? 21.882  -172.526 14.725  1.00 84.62  ? 89  ALA   X O   1 
ATOM   41667 C  CB  . ALA   X  10 89  ? 19.904  -172.887 12.162  1.00 84.90  ? 89  ALA   X CB  1 
ATOM   41668 N  N   . LYS   X  10 90  ? 22.715  -174.057 13.245  1.00 93.52  ? 90  LYS   X N   1 
ATOM   41669 C  CA  . LYS   X  10 90  ? 23.683  -174.729 14.157  1.00 96.03  ? 90  LYS   X CA  1 
ATOM   41670 C  C   . LYS   X  10 90  ? 24.783  -173.737 14.537  1.00 94.68  ? 90  LYS   X C   1 
ATOM   41671 O  O   . LYS   X  10 90  ? 25.041  -173.567 15.740  1.00 89.95  ? 90  LYS   X O   1 
ATOM   41672 C  CB  . LYS   X  10 90  ? 24.364  -175.927 13.487  1.00 101.16 ? 90  LYS   X CB  1 
ATOM   41673 C  CG  . LYS   X  10 90  ? 23.583  -177.232 13.463  1.00 104.34 ? 90  LYS   X CG  1 
ATOM   41674 C  CD  . LYS   X  10 90  ? 24.425  -178.366 12.915  1.00 110.86 ? 90  LYS   X CD  1 
ATOM   41675 C  CE  . LYS   X  10 90  ? 23.618  -179.506 12.331  1.00 116.64 ? 90  LYS   X CE  1 
ATOM   41676 N  NZ  . LYS   X  10 90  ? 24.439  -180.330 11.412  1.00 122.91 ? 90  LYS   X NZ  1 
ATOM   41677 N  N   . SER   X  10 91  ? 25.399  -173.124 13.520  1.00 97.41  ? 91  SER   X N   1 
ATOM   41678 C  CA  . SER   X  10 91  ? 26.608  -172.266 13.617  1.00 99.70  ? 91  SER   X CA  1 
ATOM   41679 C  C   . SER   X  10 91  ? 26.393  -171.121 14.616  1.00 99.41  ? 91  SER   X C   1 
ATOM   41680 O  O   . SER   X  10 91  ? 27.337  -170.836 15.382  1.00 97.70  ? 91  SER   X O   1 
ATOM   41681 C  CB  . SER   X  10 91  ? 27.015  -171.748 12.254  1.00 101.90 ? 91  SER   X CB  1 
ATOM   41682 O  OG  . SER   X  10 91  ? 28.028  -170.759 12.361  1.00 108.31 ? 91  SER   X OG  1 
ATOM   41683 N  N   . ILE   X  10 92  ? 25.204  -170.504 14.630  1.00 100.10 ? 92  ILE   X N   1 
ATOM   41684 C  CA  . ILE   X  10 92  ? 24.957  -169.217 15.352  1.00 97.84  ? 92  ILE   X CA  1 
ATOM   41685 C  C   . ILE   X  10 92  ? 25.114  -169.416 16.869  1.00 95.76  ? 92  ILE   X C   1 
ATOM   41686 O  O   . ILE   X  10 92  ? 25.386  -168.413 17.556  1.00 95.07  ? 92  ILE   X O   1 
ATOM   41687 C  CB  . ILE   X  10 92  ? 23.599  -168.582 14.970  1.00 98.04  ? 92  ILE   X CB  1 
ATOM   41688 C  CG1 . ILE   X  10 92  ? 23.558  -167.090 15.319  1.00 99.86  ? 92  ILE   X CG1 1 
ATOM   41689 C  CG2 . ILE   X  10 92  ? 22.424  -169.327 15.589  1.00 91.54  ? 92  ILE   X CG2 1 
ATOM   41690 C  CD1 . ILE   X  10 92  ? 24.670  -166.263 14.701  1.00 102.83 ? 92  ILE   X CD1 1 
ATOM   41691 N  N   . ARG   X  10 93  ? 24.983  -170.649 17.373  1.00 94.54  ? 93  ARG   X N   1 
ATOM   41692 C  CA  . ARG   X  10 93  ? 25.115  -170.961 18.824  1.00 94.08  ? 93  ARG   X CA  1 
ATOM   41693 C  C   . ARG   X  10 93  ? 26.417  -171.727 19.094  1.00 93.75  ? 93  ARG   X C   1 
ATOM   41694 O  O   . ARG   X  10 93  ? 26.579  -172.215 20.227  1.00 91.95  ? 93  ARG   X O   1 
ATOM   41695 C  CB  . ARG   X  10 93  ? 23.877  -171.721 19.307  1.00 93.23  ? 93  ARG   X CB  1 
ATOM   41696 C  CG  . ARG   X  10 93  ? 22.628  -170.856 19.360  1.00 95.27  ? 93  ARG   X CG  1 
ATOM   41697 C  CD  . ARG   X  10 93  ? 21.356  -171.608 19.701  1.00 98.02  ? 93  ARG   X CD  1 
ATOM   41698 N  NE  . ARG   X  10 93  ? 20.176  -170.794 19.425  1.00 100.89 ? 93  ARG   X NE  1 
ATOM   41699 C  CZ  . ARG   X  10 93  ? 19.728  -169.792 20.187  1.00 101.22 ? 93  ARG   X CZ  1 
ATOM   41700 N  NH1 . ARG   X  10 93  ? 20.347  -169.455 21.309  1.00 99.92  ? 93  ARG   X NH1 1 
ATOM   41701 N  NH2 . ARG   X  10 93  ? 18.648  -169.124 19.818  1.00 98.87  ? 93  ARG   X NH2 1 
ATOM   41702 N  N   . SER   X  10 94  ? 27.325  -171.792 18.112  1.00 98.26  ? 94  SER   X N   1 
ATOM   41703 C  CA  . SER   X  10 94  ? 28.675  -172.404 18.244  1.00 102.37 ? 94  SER   X CA  1 
ATOM   41704 C  C   . SER   X  10 94  ? 29.576  -171.482 19.068  1.00 103.59 ? 94  SER   X C   1 
ATOM   41705 O  O   . SER   X  10 94  ? 29.146  -170.352 19.375  1.00 100.94 ? 94  SER   X O   1 
ATOM   41706 C  CB  . SER   X  10 94  ? 29.293  -172.687 16.899  1.00 106.87 ? 94  SER   X CB  1 
ATOM   41707 O  OG  . SER   X  10 94  ? 28.399  -173.413 16.072  1.00 114.04 ? 94  SER   X OG  1 
ATOM   41708 N  N   . ARG   X  10 95  ? 30.781  -171.951 19.403  1.00 107.18 ? 95  ARG   X N   1 
ATOM   41709 C  CA  . ARG   X  10 95  ? 31.808  -171.150 20.121  1.00 110.70 ? 95  ARG   X CA  1 
ATOM   41710 C  C   . ARG   X  10 95  ? 32.242  -169.986 19.224  1.00 105.12 ? 95  ARG   X C   1 
ATOM   41711 O  O   . ARG   X  10 95  ? 32.417  -168.877 19.761  1.00 104.18 ? 95  ARG   X O   1 
ATOM   41712 C  CB  . ARG   X  10 95  ? 33.010  -172.008 20.528  1.00 117.26 ? 95  ARG   X CB  1 
ATOM   41713 C  CG  . ARG   X  10 95  ? 33.968  -171.305 21.483  1.00 122.90 ? 95  ARG   X CG  1 
ATOM   41714 C  CD  . ARG   X  10 95  ? 35.245  -172.086 21.733  1.00 127.55 ? 95  ARG   X CD  1 
ATOM   41715 N  NE  . ARG   X  10 95  ? 35.871  -172.543 20.496  1.00 130.89 ? 95  ARG   X NE  1 
ATOM   41716 C  CZ  . ARG   X  10 95  ? 36.592  -171.787 19.668  1.00 131.53 ? 95  ARG   X CZ  1 
ATOM   41717 N  NH1 . ARG   X  10 95  ? 36.804  -170.506 19.926  1.00 134.20 ? 95  ARG   X NH1 1 
ATOM   41718 N  NH2 . ARG   X  10 95  ? 37.103  -172.321 18.571  1.00 132.06 ? 95  ARG   X NH2 1 
ATOM   41719 N  N   . ARG   X  10 96  ? 32.412  -170.232 17.920  1.00 104.89 ? 96  ARG   X N   1 
ATOM   41720 C  CA  . ARG   X  10 96  ? 32.677  -169.172 16.909  1.00 102.21 ? 96  ARG   X CA  1 
ATOM   41721 C  C   . ARG   X  10 96  ? 31.744  -169.363 15.716  1.00 99.15  ? 96  ARG   X C   1 
ATOM   41722 O  O   . ARG   X  10 96  ? 32.002  -170.193 14.849  1.00 101.29 ? 96  ARG   X O   1 
ATOM   41723 C  CB  . ARG   X  10 96  ? 34.149  -169.159 16.484  1.00 107.42 ? 96  ARG   X CB  1 
ATOM   41724 C  CG  . ARG   X  10 96  ? 34.568  -167.837 15.857  1.00 109.27 ? 96  ARG   X CG  1 
ATOM   41725 C  CD  . ARG   X  10 96  ? 36.036  -167.763 15.491  1.00 113.95 ? 96  ARG   X CD  1 
ATOM   41726 N  NE  . ARG   X  10 96  ? 36.411  -168.795 14.536  1.00 114.70 ? 96  ARG   X NE  1 
ATOM   41727 C  CZ  . ARG   X  10 96  ? 36.135  -168.773 13.234  1.00 116.89 ? 96  ARG   X CZ  1 
ATOM   41728 N  NH1 . ARG   X  10 96  ? 35.466  -167.763 12.698  1.00 117.15 ? 96  ARG   X NH1 1 
ATOM   41729 N  NH2 . ARG   X  10 96  ? 36.531  -169.773 12.467  1.00 118.12 ? 96  ARG   X NH2 1 
ATOM   41730 N  N   . PRO   X  10 97  ? 30.620  -168.612 15.649  1.00 94.12  ? 97  PRO   X N   1 
ATOM   41731 C  CA  . PRO   X  10 97  ? 29.690  -168.704 14.524  1.00 93.55  ? 97  PRO   X CA  1 
ATOM   41732 C  C   . PRO   X  10 97  ? 30.269  -168.198 13.196  1.00 95.32  ? 97  PRO   X C   1 
ATOM   41733 O  O   . PRO   X  10 97  ? 30.981  -167.214 13.199  1.00 98.36  ? 97  PRO   X O   1 
ATOM   41734 C  CB  . PRO   X  10 97  ? 28.516  -167.798 14.929  1.00 92.52  ? 97  PRO   X CB  1 
ATOM   41735 C  CG  . PRO   X  10 97  ? 28.663  -167.622 16.426  1.00 94.30  ? 97  PRO   X CG  1 
ATOM   41736 C  CD  . PRO   X  10 97  ? 30.155  -167.665 16.672  1.00 94.37  ? 97  PRO   X CD  1 
ATOM   41737 N  N   . TYR   X  10 98  ? 29.948  -168.893 12.102  1.00 95.18  ? 98  TYR   X N   1 
ATOM   41738 C  CA  . TYR   X  10 98  ? 30.121  -168.410 10.710  1.00 98.06  ? 98  TYR   X CA  1 
ATOM   41739 C  C   . TYR   X  10 98  ? 29.371  -167.083 10.578  1.00 99.21  ? 98  TYR   X C   1 
ATOM   41740 O  O   . TYR   X  10 98  ? 28.150  -167.068 10.844  1.00 103.12 ? 98  TYR   X O   1 
ATOM   41741 C  CB  . TYR   X  10 98  ? 29.575  -169.422 9.698   1.00 97.77  ? 98  TYR   X CB  1 
ATOM   41742 C  CG  . TYR   X  10 98  ? 30.415  -170.656 9.476   1.00 98.35  ? 98  TYR   X CG  1 
ATOM   41743 C  CD1 . TYR   X  10 98  ? 31.663  -170.575 8.878   1.00 100.12 ? 98  TYR   X CD1 1 
ATOM   41744 C  CD2 . TYR   X  10 98  ? 29.945  -171.913 9.822   1.00 97.92  ? 98  TYR   X CD2 1 
ATOM   41745 C  CE1 . TYR   X  10 98  ? 32.432  -171.706 8.653   1.00 102.44 ? 98  TYR   X CE1 1 
ATOM   41746 C  CE2 . TYR   X  10 98  ? 30.700  -173.054 9.604   1.00 100.28 ? 98  TYR   X CE2 1 
ATOM   41747 C  CZ  . TYR   X  10 98  ? 31.949  -172.952 9.017   1.00 103.36 ? 98  TYR   X CZ  1 
ATOM   41748 O  OH  . TYR   X  10 98  ? 32.691  -174.078 8.802   1.00 106.23 ? 98  TYR   X OH  1 
ATOM   41749 N  N   . GLN   X  10 99  ? 30.088  -166.012 10.225  1.00 97.72  ? 99  GLN   X N   1 
ATOM   41750 C  CA  . GLN   X  10 99  ? 29.511  -164.687 9.880   1.00 93.08  ? 99  GLN   X CA  1 
ATOM   41751 C  C   . GLN   X  10 99  ? 29.453  -164.582 8.353   1.00 87.25  ? 99  GLN   X C   1 
ATOM   41752 O  O   . GLN   X  10 99  ? 30.276  -163.843 7.775   1.00 82.39  ? 99  GLN   X O   1 
ATOM   41753 C  CB  . GLN   X  10 99  ? 30.335  -163.572 10.522  1.00 96.68  ? 99  GLN   X CB  1 
ATOM   41754 C  CG  . GLN   X  10 99  ? 30.189  -163.515 12.035  1.00 101.10 ? 99  GLN   X CG  1 
ATOM   41755 C  CD  . GLN   X  10 99  ? 30.977  -162.381 12.647  1.00 106.28 ? 99  GLN   X CD  1 
ATOM   41756 O  OE1 . GLN   X  10 99  ? 30.787  -161.212 12.311  1.00 110.31 ? 99  GLN   X OE1 1 
ATOM   41757 N  NE2 . GLN   X  10 99  ? 31.871  -162.715 13.563  1.00 109.30 ? 99  GLN   X NE2 1 
ATOM   41758 N  N   . VAL   X  10 100 ? 28.531  -165.332 7.738   1.00 84.18  ? 100 VAL   X N   1 
ATOM   41759 C  CA  . VAL   X  10 100 ? 28.362  -165.436 6.259   1.00 84.73  ? 100 VAL   X CA  1 
ATOM   41760 C  C   . VAL   X  10 100 ? 26.879  -165.285 5.917   1.00 83.70  ? 100 VAL   X C   1 
ATOM   41761 O  O   . VAL   X  10 100 ? 26.048  -165.964 6.552   1.00 83.46  ? 100 VAL   X O   1 
ATOM   41762 C  CB  . VAL   X  10 100 ? 28.910  -166.766 5.714   1.00 83.06  ? 100 VAL   X CB  1 
ATOM   41763 C  CG1 . VAL   X  10 100 ? 28.807  -166.838 4.199   1.00 84.67  ? 100 VAL   X CG1 1 
ATOM   41764 C  CG2 . VAL   X  10 100 ? 30.340  -167.014 6.161   1.00 85.14  ? 100 VAL   X CG2 1 
ATOM   41765 N  N   . ASN   X  10 101 ? 26.583  -164.436 4.932   1.00 85.14  ? 101 ASN   X N   1 
ATOM   41766 C  CA  . ASN   X  10 101 ? 25.234  -164.244 4.341   1.00 86.90  ? 101 ASN   X CA  1 
ATOM   41767 C  C   . ASN   X  10 101 ? 25.272  -164.798 2.914   1.00 84.60  ? 101 ASN   X C   1 
ATOM   41768 O  O   . ASN   X  10 101 ? 26.238  -164.483 2.191   1.00 81.89  ? 101 ASN   X O   1 
ATOM   41769 C  CB  . ASN   X  10 101 ? 24.822  -162.771 4.399   1.00 87.98  ? 101 ASN   X CB  1 
ATOM   41770 C  CG  . ASN   X  10 101 ? 24.770  -162.242 5.817   1.00 88.67  ? 101 ASN   X CG  1 
ATOM   41771 O  OD1 . ASN   X  10 101 ? 24.231  -162.896 6.706   1.00 85.54  ? 101 ASN   X OD1 1 
ATOM   41772 N  ND2 . ASN   X  10 101 ? 25.336  -161.067 6.043   1.00 92.09  ? 101 ASN   X ND2 1 
ATOM   41773 N  N   . VAL   X  10 102 ? 24.280  -165.608 2.534   1.00 83.06  ? 102 VAL   X N   1 
ATOM   41774 C  CA  . VAL   X  10 102 ? 24.257  -166.312 1.218   1.00 84.20  ? 102 VAL   X CA  1 
ATOM   41775 C  C   . VAL   X  10 102 ? 22.930  -166.054 0.498   1.00 84.16  ? 102 VAL   X C   1 
ATOM   41776 O  O   . VAL   X  10 102 ? 21.892  -165.916 1.176   1.00 84.47  ? 102 VAL   X O   1 
ATOM   41777 C  CB  . VAL   X  10 102 ? 24.491  -167.824 1.385   1.00 83.24  ? 102 VAL   X CB  1 
ATOM   41778 C  CG1 . VAL   X  10 102 ? 25.791  -168.111 2.118   1.00 83.87  ? 102 VAL   X CG1 1 
ATOM   41779 C  CG2 . VAL   X  10 102 ? 23.321  -168.510 2.076   1.00 82.80  ? 102 VAL   X CG2 1 
ATOM   41780 N  N   . LEU   X  10 103 ? 22.983  -166.011 -0.836  1.00 85.93  ? 103 LEU   X N   1 
ATOM   41781 C  CA  . LEU   X  10 103 ? 21.814  -166.179 -1.738  1.00 89.05  ? 103 LEU   X CA  1 
ATOM   41782 C  C   . LEU   X  10 103 ? 21.992  -167.504 -2.477  1.00 87.03  ? 103 LEU   X C   1 
ATOM   41783 O  O   . LEU   X  10 103 ? 23.123  -167.765 -2.932  1.00 89.56  ? 103 LEU   X O   1 
ATOM   41784 C  CB  . LEU   X  10 103 ? 21.744  -165.024 -2.740  1.00 90.14  ? 103 LEU   X CB  1 
ATOM   41785 C  CG  . LEU   X  10 103 ? 21.565  -163.628 -2.149  1.00 92.40  ? 103 LEU   X CG  1 
ATOM   41786 C  CD1 . LEU   X  10 103 ? 21.740  -162.570 -3.228  1.00 95.10  ? 103 LEU   X CD1 1 
ATOM   41787 C  CD2 . LEU   X  10 103 ? 20.210  -163.490 -1.472  1.00 92.72  ? 103 LEU   X CD2 1 
ATOM   41788 N  N   . ILE   X  10 104 ? 20.929  -168.304 -2.588  1.00 88.81  ? 104 ILE   X N   1 
ATOM   41789 C  CA  . ILE   X  10 104 ? 20.937  -169.580 -3.360  1.00 89.83  ? 104 ILE   X CA  1 
ATOM   41790 C  C   . ILE   X  10 104 ? 19.967  -169.449 -4.533  1.00 89.19  ? 104 ILE   X C   1 
ATOM   41791 O  O   . ILE   X  10 104 ? 18.742  -169.405 -4.293  1.00 89.02  ? 104 ILE   X O   1 
ATOM   41792 C  CB  . ILE   X  10 104 ? 20.604  -170.788 -2.467  1.00 90.11  ? 104 ILE   X CB  1 
ATOM   41793 C  CG1 . ILE   X  10 104 ? 21.724  -171.044 -1.457  1.00 90.07  ? 104 ILE   X CG1 1 
ATOM   41794 C  CG2 . ILE   X  10 104 ? 20.319  -172.019 -3.319  1.00 92.11  ? 104 ILE   X CG2 1 
ATOM   41795 C  CD1 . ILE   X  10 104 ? 21.366  -172.024 -0.369  1.00 90.27  ? 104 ILE   X CD1 1 
ATOM   41796 N  N   . GLY   X  10 105 ? 20.518  -169.387 -5.746  1.00 91.73  ? 105 GLY   X N   1 
ATOM   41797 C  CA  . GLY   X  10 105 ? 19.765  -169.428 -7.010  1.00 94.77  ? 105 GLY   X CA  1 
ATOM   41798 C  C   . GLY   X  10 105 ? 19.799  -170.826 -7.592  1.00 95.66  ? 105 GLY   X C   1 
ATOM   41799 O  O   . GLY   X  10 105 ? 20.911  -171.367 -7.755  1.00 98.53  ? 105 GLY   X O   1 
ATOM   41800 N  N   . GLY   X  10 106 ? 18.626  -171.403 -7.861  1.00 96.86  ? 106 GLY   X N   1 
ATOM   41801 C  CA  . GLY   X  10 106 ? 18.488  -172.774 -8.385  1.00 96.49  ? 106 GLY   X CA  1 
ATOM   41802 C  C   . GLY   X  10 106 ? 17.365  -172.882 -9.398  1.00 97.97  ? 106 GLY   X C   1 
ATOM   41803 O  O   . GLY   X  10 106 ? 16.449  -172.033 -9.367  1.00 90.91  ? 106 GLY   X O   1 
ATOM   41804 N  N   . TYR   X  10 107 ? 17.448  -173.888 -10.271 1.00 99.99  ? 107 TYR   X N   1 
ATOM   41805 C  CA  . TYR   X  10 107 ? 16.365  -174.303 -11.200 1.00 101.78 ? 107 TYR   X CA  1 
ATOM   41806 C  C   . TYR   X  10 107 ? 15.932  -175.732 -10.847 1.00 103.09 ? 107 TYR   X C   1 
ATOM   41807 O  O   . TYR   X  10 107 ? 16.700  -176.682 -11.109 1.00 101.11 ? 107 TYR   X O   1 
ATOM   41808 C  CB  . TYR   X  10 107 ? 16.812  -174.189 -12.659 1.00 103.46 ? 107 TYR   X CB  1 
ATOM   41809 C  CG  . TYR   X  10 107 ? 15.676  -174.300 -13.644 1.00 105.45 ? 107 TYR   X CG  1 
ATOM   41810 C  CD1 . TYR   X  10 107 ? 15.247  -175.535 -14.105 1.00 107.71 ? 107 TYR   X CD1 1 
ATOM   41811 C  CD2 . TYR   X  10 107 ? 15.005  -173.173 -14.092 1.00 105.51 ? 107 TYR   X CD2 1 
ATOM   41812 C  CE1 . TYR   X  10 107 ? 14.196  -175.649 -15.001 1.00 109.22 ? 107 TYR   X CE1 1 
ATOM   41813 C  CE2 . TYR   X  10 107 ? 13.952  -173.269 -14.988 1.00 108.92 ? 107 TYR   X CE2 1 
ATOM   41814 C  CZ  . TYR   X  10 107 ? 13.545  -174.511 -15.443 1.00 110.44 ? 107 TYR   X CZ  1 
ATOM   41815 O  OH  . TYR   X  10 107 ? 12.510  -174.620 -16.324 1.00 115.99 ? 107 TYR   X OH  1 
ATOM   41816 N  N   . ASP   X  10 108 ? 14.742  -175.866 -10.252 1.00 104.45 ? 108 ASP   X N   1 
ATOM   41817 C  CA  . ASP   X  10 108 ? 14.105  -177.170 -9.931  1.00 105.77 ? 108 ASP   X CA  1 
ATOM   41818 C  C   . ASP   X  10 108 ? 13.674  -177.818 -11.250 1.00 108.24 ? 108 ASP   X C   1 
ATOM   41819 O  O   . ASP   X  10 108 ? 12.756  -177.279 -11.897 1.00 113.32 ? 108 ASP   X O   1 
ATOM   41820 C  CB  . ASP   X  10 108 ? 12.926  -176.996 -8.970  1.00 107.69 ? 108 ASP   X CB  1 
ATOM   41821 C  CG  . ASP   X  10 108 ? 12.418  -178.295 -8.366  1.00 108.82 ? 108 ASP   X CG  1 
ATOM   41822 O  OD1 . ASP   X  10 108 ? 12.562  -179.350 -9.019  1.00 109.56 ? 108 ASP   X OD1 1 
ATOM   41823 O  OD2 . ASP   X  10 108 ? 11.888  -178.243 -7.241  1.00 114.86 ? 108 ASP   X OD2 1 
ATOM   41824 N  N   . LYS   X  10 109 ? 14.329  -178.918 -11.632 1.00 109.85 ? 109 LYS   X N   1 
ATOM   41825 C  CA  . LYS   X  10 109 ? 14.097  -179.631 -12.917 1.00 107.64 ? 109 LYS   X CA  1 
ATOM   41826 C  C   . LYS   X  10 109 ? 12.791  -180.432 -12.836 1.00 108.29 ? 109 LYS   X C   1 
ATOM   41827 O  O   . LYS   X  10 109 ? 12.158  -180.616 -13.893 1.00 107.39 ? 109 LYS   X O   1 
ATOM   41828 C  CB  . LYS   X  10 109 ? 15.298  -180.520 -13.252 1.00 106.57 ? 109 LYS   X CB  1 
ATOM   41829 C  CG  . LYS   X  10 109 ? 16.587  -179.765 -13.551 1.00 105.39 ? 109 LYS   X CG  1 
ATOM   41830 C  CD  . LYS   X  10 109 ? 16.636  -179.183 -14.945 1.00 107.17 ? 109 LYS   X CD  1 
ATOM   41831 C  CE  . LYS   X  10 109 ? 17.019  -180.206 -15.994 1.00 109.53 ? 109 LYS   X CE  1 
ATOM   41832 N  NZ  . LYS   X  10 109 ? 16.963  -179.639 -17.361 1.00 112.44 ? 109 LYS   X NZ  1 
ATOM   41833 N  N   . LYS   X  10 110 ? 12.402  -180.879 -11.636 1.00 109.24 ? 110 LYS   X N   1 
ATOM   41834 C  CA  . LYS   X  10 110 ? 11.143  -181.641 -11.400 1.00 115.31 ? 110 LYS   X CA  1 
ATOM   41835 C  C   . LYS   X  10 110 ? 9.938   -180.702 -11.551 1.00 115.30 ? 110 LYS   X C   1 
ATOM   41836 O  O   . LYS   X  10 110 ? 8.887   -181.173 -12.028 1.00 118.03 ? 110 LYS   X O   1 
ATOM   41837 C  CB  . LYS   X  10 110 ? 11.140  -182.308 -10.019 1.00 116.94 ? 110 LYS   X CB  1 
ATOM   41838 C  CG  . LYS   X  10 110 ? 12.328  -183.215 -9.724  1.00 118.29 ? 110 LYS   X CG  1 
ATOM   41839 C  CD  . LYS   X  10 110 ? 11.972  -184.446 -8.917  1.00 120.01 ? 110 LYS   X CD  1 
ATOM   41840 C  CE  . LYS   X  10 110 ? 11.433  -185.575 -9.773  1.00 123.63 ? 110 LYS   X CE  1 
ATOM   41841 N  NZ  . LYS   X  10 110 ? 11.433  -186.865 -9.044  1.00 124.29 ? 110 LYS   X NZ  1 
ATOM   41842 N  N   . LYS   X  10 111 ? 10.084  -179.431 -11.160 1.00 113.64 ? 111 LYS   X N   1 
ATOM   41843 C  CA  . LYS   X  10 111 ? 9.003   -178.406 -11.204 1.00 114.98 ? 111 LYS   X CA  1 
ATOM   41844 C  C   . LYS   X  10 111 ? 9.125   -177.527 -12.457 1.00 113.55 ? 111 LYS   X C   1 
ATOM   41845 O  O   . LYS   X  10 111 ? 8.117   -176.881 -12.807 1.00 112.45 ? 111 LYS   X O   1 
ATOM   41846 C  CB  . LYS   X  10 111 ? 9.049   -177.525 -9.953  1.00 115.79 ? 111 LYS   X CB  1 
ATOM   41847 C  CG  . LYS   X  10 111 ? 8.565   -178.191 -8.674  1.00 118.33 ? 111 LYS   X CG  1 
ATOM   41848 C  CD  . LYS   X  10 111 ? 8.611   -177.266 -7.481  1.00 121.66 ? 111 LYS   X CD  1 
ATOM   41849 C  CE  . LYS   X  10 111 ? 7.863   -177.808 -6.283  1.00 124.67 ? 111 LYS   X CE  1 
ATOM   41850 N  NZ  . LYS   X  10 111 ? 7.778   -176.802 -5.199  1.00 127.00 ? 111 LYS   X NZ  1 
ATOM   41851 N  N   . ASN   X  10 112 ? 10.303  -177.491 -13.093 1.00 114.93 ? 112 ASN   X N   1 
ATOM   41852 C  CA  . ASN   X  10 112 ? 10.627  -176.590 -14.234 1.00 114.94 ? 112 ASN   X CA  1 
ATOM   41853 C  C   . ASN   X  10 112 ? 10.379  -175.138 -13.809 1.00 114.94 ? 112 ASN   X C   1 
ATOM   41854 O  O   . ASN   X  10 112 ? 9.660   -174.426 -14.534 1.00 115.56 ? 112 ASN   X O   1 
ATOM   41855 C  CB  . ASN   X  10 112 ? 9.832   -176.956 -15.490 1.00 117.70 ? 112 ASN   X CB  1 
ATOM   41856 C  CG  . ASN   X  10 112 ? 10.323  -178.233 -16.137 1.00 118.99 ? 112 ASN   X CG  1 
ATOM   41857 O  OD1 . ASN   X  10 112 ? 11.440  -178.280 -16.649 1.00 115.01 ? 112 ASN   X OD1 1 
ATOM   41858 N  ND2 . ASN   X  10 112 ? 9.501   -179.270 -16.120 1.00 122.77 ? 112 ASN   X ND2 1 
ATOM   41859 N  N   . LYS   X  10 113 ? 10.950  -174.728 -12.671 1.00 113.90 ? 113 LYS   X N   1 
ATOM   41860 C  CA  . LYS   X  10 113 ? 10.748  -173.385 -12.059 1.00 113.88 ? 113 LYS   X CA  1 
ATOM   41861 C  C   . LYS   X  10 113 ? 12.058  -172.863 -11.481 1.00 110.31 ? 113 LYS   X C   1 
ATOM   41862 O  O   . LYS   X  10 113 ? 12.780  -173.602 -10.815 1.00 109.34 ? 113 LYS   X O   1 
ATOM   41863 C  CB  . LYS   X  10 113 ? 9.697   -173.452 -10.946 1.00 116.93 ? 113 LYS   X CB  1 
ATOM   41864 C  CG  . LYS   X  10 113 ? 8.277   -173.124 -11.380 1.00 121.95 ? 113 LYS   X CG  1 
ATOM   41865 C  CD  . LYS   X  10 113 ? 7.278   -173.186 -10.245 1.00 125.57 ? 113 LYS   X CD  1 
ATOM   41866 C  CE  . LYS   X  10 113 ? 6.008   -172.411 -10.528 1.00 128.71 ? 113 LYS   X CE  1 
ATOM   41867 N  NZ  . LYS   X  10 113 ? 5.260   -172.977 -11.674 1.00 132.50 ? 113 LYS   X NZ  1 
ATOM   41868 N  N   . PRO   X  10 114 ? 12.389  -171.568 -11.693 1.00 109.44 ? 114 PRO   X N   1 
ATOM   41869 C  CA  . PRO   X  10 114 ? 13.504  -170.933 -10.993 1.00 106.44 ? 114 PRO   X CA  1 
ATOM   41870 C  C   . PRO   X  10 114 ? 13.121  -170.646 -9.534  1.00 104.46 ? 114 PRO   X C   1 
ATOM   41871 O  O   . PRO   X  10 114 ? 11.954  -170.395 -9.281  1.00 103.51 ? 114 PRO   X O   1 
ATOM   41872 C  CB  . PRO   X  10 114 ? 13.730  -169.634 -11.778 1.00 106.79 ? 114 PRO   X CB  1 
ATOM   41873 C  CG  . PRO   X  10 114 ? 12.364  -169.302 -12.340 1.00 109.61 ? 114 PRO   X CG  1 
ATOM   41874 C  CD  . PRO   X  10 114 ? 11.698  -170.638 -12.600 1.00 110.12 ? 114 PRO   X CD  1 
ATOM   41875 N  N   . GLU   X  10 115 ? 14.097  -170.697 -8.623  1.00 100.59 ? 115 GLU   X N   1 
ATOM   41876 C  CA  . GLU   X  10 115 ? 13.896  -170.455 -7.169  1.00 101.63 ? 115 GLU   X CA  1 
ATOM   41877 C  C   . GLU   X  10 115 ? 15.096  -169.678 -6.616  1.00 95.35  ? 115 GLU   X C   1 
ATOM   41878 O  O   . GLU   X  10 115 ? 16.244  -170.059 -6.919  1.00 92.47  ? 115 GLU   X O   1 
ATOM   41879 C  CB  . GLU   X  10 115 ? 13.691  -171.782 -6.433  1.00 104.46 ? 115 GLU   X CB  1 
ATOM   41880 C  CG  . GLU   X  10 115 ? 12.283  -172.340 -6.570  1.00 110.02 ? 115 GLU   X CG  1 
ATOM   41881 C  CD  . GLU   X  10 115 ? 12.039  -173.691 -5.915  1.00 111.68 ? 115 GLU   X CD  1 
ATOM   41882 O  OE1 . GLU   X  10 115 ? 10.859  -174.071 -5.778  1.00 115.15 ? 115 GLU   X OE1 1 
ATOM   41883 O  OE2 . GLU   X  10 115 ? 13.025  -174.367 -5.550  1.00 113.49 ? 115 GLU   X OE2 1 
ATOM   41884 N  N   . LEU   X  10 116 ? 14.823  -168.629 -5.836  1.00 94.32  ? 116 LEU   X N   1 
ATOM   41885 C  CA  . LEU   X  10 116 ? 15.842  -167.778 -5.168  1.00 92.37  ? 116 LEU   X CA  1 
ATOM   41886 C  C   . LEU   X  10 116 ? 15.571  -167.786 -3.660  1.00 89.41  ? 116 LEU   X C   1 
ATOM   41887 O  O   . LEU   X  10 116 ? 14.444  -167.438 -3.265  1.00 94.58  ? 116 LEU   X O   1 
ATOM   41888 C  CB  . LEU   X  10 116 ? 15.760  -166.363 -5.749  1.00 91.84  ? 116 LEU   X CB  1 
ATOM   41889 C  CG  . LEU   X  10 116 ? 16.656  -165.318 -5.084  1.00 91.71  ? 116 LEU   X CG  1 
ATOM   41890 C  CD1 . LEU   X  10 116 ? 18.120  -165.577 -5.401  1.00 90.06  ? 116 LEU   X CD1 1 
ATOM   41891 C  CD2 . LEU   X  10 116 ? 16.257  -163.915 -5.513  1.00 93.74  ? 116 LEU   X CD2 1 
ATOM   41892 N  N   . TYR   X  10 117 ? 16.563  -168.179 -2.859  1.00 86.82  ? 117 TYR   X N   1 
ATOM   41893 C  CA  . TYR   X  10 117 ? 16.488  -168.211 -1.375  1.00 87.23  ? 117 TYR   X CA  1 
ATOM   41894 C  C   . TYR   X  10 117 ? 17.522  -167.247 -0.785  1.00 82.26  ? 117 TYR   X C   1 
ATOM   41895 O  O   . TYR   X  10 117 ? 18.710  -167.337 -1.148  1.00 79.76  ? 117 TYR   X O   1 
ATOM   41896 C  CB  . TYR   X  10 117 ? 16.715  -169.631 -0.852  1.00 87.87  ? 117 TYR   X CB  1 
ATOM   41897 C  CG  . TYR   X  10 117 ? 15.688  -170.636 -1.308  1.00 90.63  ? 117 TYR   X CG  1 
ATOM   41898 C  CD1 . TYR   X  10 117 ? 14.493  -170.797 -0.625  1.00 90.90  ? 117 TYR   X CD1 1 
ATOM   41899 C  CD2 . TYR   X  10 117 ? 15.910  -171.427 -2.424  1.00 89.94  ? 117 TYR   X CD2 1 
ATOM   41900 C  CE1 . TYR   X  10 117 ? 13.543  -171.718 -1.035  1.00 89.84  ? 117 TYR   X CE1 1 
ATOM   41901 C  CE2 . TYR   X  10 117 ? 14.971  -172.353 -2.849  1.00 89.76  ? 117 TYR   X CE2 1 
ATOM   41902 C  CZ  . TYR   X  10 117 ? 13.783  -172.497 -2.152  1.00 88.95  ? 117 TYR   X CZ  1 
ATOM   41903 O  OH  . TYR   X  10 117 ? 12.842  -173.397 -2.553  1.00 91.20  ? 117 TYR   X OH  1 
ATOM   41904 N  N   . GLN   X  10 118 ? 17.068  -166.353 0.097   1.00 82.46  ? 118 GLN   X N   1 
ATOM   41905 C  CA  . GLN   X  10 118 ? 17.927  -165.447 0.900   1.00 85.28  ? 118 GLN   X CA  1 
ATOM   41906 C  C   . GLN   X  10 118 ? 18.082  -166.057 2.298   1.00 80.42  ? 118 GLN   X C   1 
ATOM   41907 O  O   . GLN   X  10 118 ? 17.047  -166.299 2.947   1.00 77.36  ? 118 GLN   X O   1 
ATOM   41908 C  CB  . GLN   X  10 118 ? 17.317  -164.044 0.947   1.00 86.69  ? 118 GLN   X CB  1 
ATOM   41909 C  CG  . GLN   X  10 118 ? 18.231  -163.006 1.588   1.00 91.46  ? 118 GLN   X CG  1 
ATOM   41910 C  CD  . GLN   X  10 118 ? 17.684  -161.599 1.541   1.00 93.87  ? 118 GLN   X CD  1 
ATOM   41911 O  OE1 . GLN   X  10 118 ? 17.790  -160.847 2.507   1.00 101.45 ? 118 GLN   X OE1 1 
ATOM   41912 N  NE2 . GLN   X  10 118 ? 17.097  -161.218 0.416   1.00 99.01  ? 118 GLN   X NE2 1 
ATOM   41913 N  N   . ILE   X  10 119 ? 19.322  -166.329 2.719   1.00 81.12  ? 119 ILE   X N   1 
ATOM   41914 C  CA  . ILE   X  10 119 ? 19.655  -166.886 4.066   1.00 84.28  ? 119 ILE   X CA  1 
ATOM   41915 C  C   . ILE   X  10 119 ? 20.772  -166.046 4.692   1.00 84.46  ? 119 ILE   X C   1 
ATOM   41916 O  O   . ILE   X  10 119 ? 21.856  -165.957 4.081   1.00 85.48  ? 119 ILE   X O   1 
ATOM   41917 C  CB  . ILE   X  10 119 ? 20.070  -168.368 3.990   1.00 83.36  ? 119 ILE   X CB  1 
ATOM   41918 C  CG1 . ILE   X  10 119 ? 19.164  -169.184 3.065   1.00 84.13  ? 119 ILE   X CG1 1 
ATOM   41919 C  CG2 . ILE   X  10 119 ? 20.127  -168.960 5.389   1.00 84.46  ? 119 ILE   X CG2 1 
ATOM   41920 C  CD1 . ILE   X  10 119 ? 19.687  -170.566 2.747   1.00 83.84  ? 119 ILE   X CD1 1 
ATOM   41921 N  N   . ASP   X  10 120 ? 20.527  -165.489 5.881   1.00 87.27  ? 120 ASP   X N   1 
ATOM   41922 C  CA  . ASP   X  10 120 ? 21.523  -164.683 6.638   1.00 89.31  ? 120 ASP   X CA  1 
ATOM   41923 C  C   . ASP   X  10 120 ? 22.283  -165.613 7.593   1.00 87.03  ? 120 ASP   X C   1 
ATOM   41924 O  O   . ASP   X  10 120 ? 21.921  -166.800 7.672   1.00 88.53  ? 120 ASP   X O   1 
ATOM   41925 C  CB  . ASP   X  10 120 ? 20.856  -163.497 7.344   1.00 91.42  ? 120 ASP   X CB  1 
ATOM   41926 C  CG  . ASP   X  10 120 ? 20.081  -163.844 8.606   1.00 93.02  ? 120 ASP   X CG  1 
ATOM   41927 O  OD1 . ASP   X  10 120 ? 19.947  -165.047 8.908   1.00 91.61  ? 120 ASP   X OD1 1 
ATOM   41928 O  OD2 . ASP   X  10 120 ? 19.617  -162.900 9.284   1.00 92.77  ? 120 ASP   X OD2 1 
ATOM   41929 N  N   . TYR   X  10 121 ? 23.289  -165.078 8.291   1.00 86.06  ? 121 TYR   X N   1 
ATOM   41930 C  CA  . TYR   X  10 121 ? 24.234  -165.822 9.171   1.00 86.12  ? 121 TYR   X CA  1 
ATOM   41931 C  C   . TYR   X  10 121 ? 23.522  -166.404 10.403  1.00 82.31  ? 121 TYR   X C   1 
ATOM   41932 O  O   . TYR   X  10 121 ? 24.074  -167.344 11.011  1.00 77.50  ? 121 TYR   X O   1 
ATOM   41933 C  CB  . TYR   X  10 121 ? 25.405  -164.925 9.588   1.00 88.05  ? 121 TYR   X CB  1 
ATOM   41934 C  CG  . TYR   X  10 121 ? 25.078  -163.834 10.579  1.00 90.82  ? 121 TYR   X CG  1 
ATOM   41935 C  CD1 . TYR   X  10 121 ? 24.426  -162.674 10.188  1.00 93.09  ? 121 TYR   X CD1 1 
ATOM   41936 C  CD2 . TYR   X  10 121 ? 25.448  -163.945 11.909  1.00 93.85  ? 121 TYR   X CD2 1 
ATOM   41937 C  CE1 . TYR   X  10 121 ? 24.132  -161.666 11.092  1.00 94.44  ? 121 TYR   X CE1 1 
ATOM   41938 C  CE2 . TYR   X  10 121 ? 25.164  -162.944 12.826  1.00 95.96  ? 121 TYR   X CE2 1 
ATOM   41939 C  CZ  . TYR   X  10 121 ? 24.504  -161.799 12.417  1.00 97.08  ? 121 TYR   X CZ  1 
ATOM   41940 O  OH  . TYR   X  10 121 ? 24.223  -160.809 13.315  1.00 99.43  ? 121 TYR   X OH  1 
ATOM   41941 N  N   . LEU   X  10 122 ? 22.358  -165.864 10.779  1.00 81.93  ? 122 LEU   X N   1 
ATOM   41942 C  CA  . LEU   X  10 122 ? 21.519  -166.397 11.889  1.00 82.52  ? 122 LEU   X CA  1 
ATOM   41943 C  C   . LEU   X  10 122 ? 20.836  -167.698 11.448  1.00 83.19  ? 122 LEU   X C   1 
ATOM   41944 O  O   . LEU   X  10 122 ? 20.433  -168.478 12.335  1.00 80.23  ? 122 LEU   X O   1 
ATOM   41945 C  CB  . LEU   X  10 122 ? 20.463  -165.362 12.292  1.00 82.48  ? 122 LEU   X CB  1 
ATOM   41946 C  CG  . LEU   X  10 122 ? 20.988  -164.024 12.806  1.00 81.81  ? 122 LEU   X CG  1 
ATOM   41947 C  CD1 . LEU   X  10 122 ? 19.841  -163.055 13.022  1.00 84.53  ? 122 LEU   X CD1 1 
ATOM   41948 C  CD2 . LEU   X  10 122 ? 21.776  -164.200 14.090  1.00 81.98  ? 122 LEU   X CD2 1 
ATOM   41949 N  N   . GLY   X  10 123 ? 20.694  -167.905 10.135  1.00 86.29  ? 123 GLY   X N   1 
ATOM   41950 C  CA  . GLY   X  10 123 ? 19.887  -168.988 9.543   1.00 87.57  ? 123 GLY   X CA  1 
ATOM   41951 C  C   . GLY   X  10 123 ? 18.445  -168.546 9.360   1.00 89.12  ? 123 GLY   X C   1 
ATOM   41952 O  O   . GLY   X  10 123 ? 17.538  -169.309 9.741   1.00 91.84  ? 123 GLY   X O   1 
ATOM   41953 N  N   . THR   X  10 124 ? 18.246  -167.340 8.820   1.00 90.22  ? 124 THR   X N   1 
ATOM   41954 C  CA  . THR   X  10 124 ? 16.919  -166.773 8.466   1.00 88.90  ? 124 THR   X CA  1 
ATOM   41955 C  C   . THR   X  10 124 ? 16.702  -167.000 6.968   1.00 90.38  ? 124 THR   X C   1 
ATOM   41956 O  O   . THR   X  10 124 ? 17.332  -166.279 6.174   1.00 94.70  ? 124 THR   X O   1 
ATOM   41957 C  CB  . THR   X  10 124 ? 16.823  -165.292 8.859   1.00 90.70  ? 124 THR   X CB  1 
ATOM   41958 O  OG1 . THR   X  10 124 ? 17.396  -165.134 10.159  1.00 87.24  ? 124 THR   X OG1 1 
ATOM   41959 C  CG2 . THR   X  10 124 ? 15.399  -164.781 8.869   1.00 91.07  ? 124 THR   X CG2 1 
ATOM   41960 N  N   . LYS   X  10 125 ? 15.874  -167.984 6.602   1.00 86.73  ? 125 LYS   X N   1 
ATOM   41961 C  CA  . LYS   X  10 125 ? 15.593  -168.330 5.185   1.00 87.03  ? 125 LYS   X CA  1 
ATOM   41962 C  C   . LYS   X  10 125 ? 14.266  -167.701 4.749   1.00 83.79  ? 125 LYS   X C   1 
ATOM   41963 O  O   . LYS   X  10 125 ? 13.299  -167.735 5.539   1.00 78.85  ? 125 LYS   X O   1 
ATOM   41964 C  CB  . LYS   X  10 125 ? 15.549  -169.844 4.975   1.00 87.43  ? 125 LYS   X CB  1 
ATOM   41965 C  CG  . LYS   X  10 125 ? 15.619  -170.273 3.516   1.00 89.79  ? 125 LYS   X CG  1 
ATOM   41966 C  CD  . LYS   X  10 125 ? 15.514  -171.762 3.308   1.00 91.56  ? 125 LYS   X CD  1 
ATOM   41967 C  CE  . LYS   X  10 125 ? 14.093  -172.215 3.056   1.00 95.26  ? 125 LYS   X CE  1 
ATOM   41968 N  NZ  . LYS   X  10 125 ? 14.039  -173.652 2.701   1.00 97.07  ? 125 LYS   X NZ  1 
ATOM   41969 N  N   . VAL   X  10 126 ? 14.245  -167.145 3.534   1.00 84.34  ? 126 VAL   X N   1 
ATOM   41970 C  CA  . VAL   X  10 126 ? 13.020  -166.676 2.822   1.00 88.35  ? 126 VAL   X CA  1 
ATOM   41971 C  C   . VAL   X  10 126 ? 13.193  -166.960 1.326   1.00 86.30  ? 126 VAL   X C   1 
ATOM   41972 O  O   . VAL   X  10 126 ? 14.314  -166.762 0.816   1.00 85.58  ? 126 VAL   X O   1 
ATOM   41973 C  CB  . VAL   X  10 126 ? 12.755  -165.180 3.068   1.00 89.18  ? 126 VAL   X CB  1 
ATOM   41974 C  CG1 . VAL   X  10 126 ? 11.501  -164.720 2.345   1.00 95.16  ? 126 VAL   X CG1 1 
ATOM   41975 C  CG2 . VAL   X  10 126 ? 12.665  -164.845 4.548   1.00 88.75  ? 126 VAL   X CG2 1 
ATOM   41976 N  N   . GLU   X  10 127 ? 12.126  -167.411 0.660   1.00 89.84  ? 127 GLU   X N   1 
ATOM   41977 C  CA  . GLU   X  10 127 ? 12.042  -167.495 -0.823  1.00 95.02  ? 127 GLU   X CA  1 
ATOM   41978 C  C   . GLU   X  10 127 ? 11.520  -166.148 -1.334  1.00 93.50  ? 127 GLU   X C   1 
ATOM   41979 O  O   . GLU   X  10 127 ? 10.471  -165.703 -0.832  1.00 93.52  ? 127 GLU   X O   1 
ATOM   41980 C  CB  . GLU   X  10 127 ? 11.139  -168.653 -1.256  1.00 97.76  ? 127 GLU   X CB  1 
ATOM   41981 C  CG  . GLU   X  10 127 ? 11.420  -169.154 -2.665  1.00 102.57 ? 127 GLU   X CG  1 
ATOM   41982 C  CD  . GLU   X  10 127 ? 10.878  -168.283 -3.789  1.00 107.62 ? 127 GLU   X CD  1 
ATOM   41983 O  OE1 . GLU   X  10 127 ? 9.702   -167.870 -3.705  1.00 115.08 ? 127 GLU   X OE1 1 
ATOM   41984 O  OE2 . GLU   X  10 127 ? 11.633  -168.013 -4.749  1.00 108.92 ? 127 GLU   X OE2 1 
ATOM   41985 N  N   . LEU   X  10 128 ? 12.227  -165.529 -2.284  1.00 95.69  ? 128 LEU   X N   1 
ATOM   41986 C  CA  . LEU   X  10 128 ? 11.945  -164.150 -2.768  1.00 96.91  ? 128 LEU   X CA  1 
ATOM   41987 C  C   . LEU   X  10 128 ? 11.991  -164.102 -4.290  1.00 97.14  ? 128 LEU   X C   1 
ATOM   41988 O  O   . LEU   X  10 128 ? 12.740  -164.855 -4.909  1.00 98.21  ? 128 LEU   X O   1 
ATOM   41989 C  CB  . LEU   X  10 128 ? 12.985  -163.192 -2.181  1.00 100.80 ? 128 LEU   X CB  1 
ATOM   41990 C  CG  . LEU   X  10 128 ? 12.866  -162.913 -0.685  1.00 104.22 ? 128 LEU   X CG  1 
ATOM   41991 C  CD1 . LEU   X  10 128 ? 14.066  -162.117 -0.196  1.00 108.34 ? 128 LEU   X CD1 1 
ATOM   41992 C  CD2 . LEU   X  10 128 ? 11.571  -162.180 -0.361  1.00 106.87 ? 128 LEU   X CD2 1 
ATOM   41993 N  N   . PRO   X  10 129 ? 11.186  -163.225 -4.934  1.00 93.74  ? 129 PRO   X N   1 
ATOM   41994 C  CA  . PRO   X  10 129 ? 11.382  -162.892 -6.346  1.00 94.01  ? 129 PRO   X CA  1 
ATOM   41995 C  C   . PRO   X  10 129 ? 12.717  -162.168 -6.593  1.00 92.99  ? 129 PRO   X C   1 
ATOM   41996 O  O   . PRO   X  10 129 ? 13.334  -162.421 -7.612  1.00 88.19  ? 129 PRO   X O   1 
ATOM   41997 C  CB  . PRO   X  10 129 ? 10.167  -162.012 -6.692  1.00 95.72  ? 129 PRO   X CB  1 
ATOM   41998 C  CG  . PRO   X  10 129 ? 9.687   -161.474 -5.359  1.00 95.20  ? 129 PRO   X CG  1 
ATOM   41999 C  CD  . PRO   X  10 129 ? 10.003  -162.565 -4.360  1.00 92.67  ? 129 PRO   X CD  1 
ATOM   42000 N  N   . TYR   X  10 130 ? 13.131  -161.299 -5.664  1.00 94.25  ? 130 TYR   X N   1 
ATOM   42001 C  CA  . TYR   X  10 130 ? 14.432  -160.575 -5.700  1.00 96.85  ? 130 TYR   X CA  1 
ATOM   42002 C  C   . TYR   X  10 130 ? 14.979  -160.413 -4.278  1.00 94.53  ? 130 TYR   X C   1 
ATOM   42003 O  O   . TYR   X  10 130 ? 14.193  -160.139 -3.347  1.00 91.93  ? 130 TYR   X O   1 
ATOM   42004 C  CB  . TYR   X  10 130 ? 14.302  -159.222 -6.409  1.00 99.68  ? 130 TYR   X CB  1 
ATOM   42005 C  CG  . TYR   X  10 130 ? 13.035  -158.458 -6.119  1.00 100.52 ? 130 TYR   X CG  1 
ATOM   42006 C  CD1 . TYR   X  10 130 ? 12.969  -157.545 -5.078  1.00 101.57 ? 130 TYR   X CD1 1 
ATOM   42007 C  CD2 . TYR   X  10 130 ? 11.901  -158.639 -6.895  1.00 100.94 ? 130 TYR   X CD2 1 
ATOM   42008 C  CE1 . TYR   X  10 130 ? 11.808  -156.836 -4.811  1.00 102.33 ? 130 TYR   X CE1 1 
ATOM   42009 C  CE2 . TYR   X  10 130 ? 10.732  -157.941 -6.639  1.00 102.49 ? 130 TYR   X CE2 1 
ATOM   42010 C  CZ  . TYR   X  10 130 ? 10.685  -157.034 -5.596  1.00 102.72 ? 130 TYR   X CZ  1 
ATOM   42011 O  OH  . TYR   X  10 130 ? 9.534   -156.346 -5.345  1.00 103.17 ? 130 TYR   X OH  1 
ATOM   42012 N  N   . GLY   X  10 131 ? 16.299  -160.565 -4.134  1.00 93.14  ? 131 GLY   X N   1 
ATOM   42013 C  CA  . GLY   X  10 131 ? 17.000  -160.605 -2.837  1.00 92.41  ? 131 GLY   X CA  1 
ATOM   42014 C  C   . GLY   X  10 131 ? 18.323  -159.862 -2.878  1.00 92.80  ? 131 GLY   X C   1 
ATOM   42015 O  O   . GLY   X  10 131 ? 18.939  -159.791 -3.962  1.00 95.89  ? 131 GLY   X O   1 
ATOM   42016 N  N   . ALA   X  10 132 ? 18.739  -159.330 -1.726  1.00 91.04  ? 132 ALA   X N   1 
ATOM   42017 C  CA  . ALA   X  10 132 ? 20.004  -158.590 -1.520  1.00 94.04  ? 132 ALA   X CA  1 
ATOM   42018 C  C   . ALA   X  10 132 ? 20.480  -158.820 -0.085  1.00 91.93  ? 132 ALA   X C   1 
ATOM   42019 O  O   . ALA   X  10 132 ? 19.625  -159.084 0.779   1.00 95.67  ? 132 ALA   X O   1 
ATOM   42020 C  CB  . ALA   X  10 132 ? 19.786  -157.122 -1.797  1.00 97.07  ? 132 ALA   X CB  1 
ATOM   42021 N  N   . HIS   X  10 133 ? 21.789  -158.729 0.151   1.00 92.91  ? 133 HIS   X N   1 
ATOM   42022 C  CA  . HIS   X  10 133 ? 22.405  -158.805 1.502   1.00 94.47  ? 133 HIS   X CA  1 
ATOM   42023 C  C   . HIS   X  10 133 ? 23.237  -157.547 1.760   1.00 95.52  ? 133 HIS   X C   1 
ATOM   42024 O  O   . HIS   X  10 133 ? 23.881  -157.055 0.811   1.00 94.37  ? 133 HIS   X O   1 
ATOM   42025 C  CB  . HIS   X  10 133 ? 23.239  -160.082 1.652   1.00 94.07  ? 133 HIS   X CB  1 
ATOM   42026 C  CG  . HIS   X  10 133 ? 22.464  -161.262 2.136   1.00 94.65  ? 133 HIS   X CG  1 
ATOM   42027 N  ND1 . HIS   X  10 133 ? 21.744  -161.242 3.315   1.00 96.57  ? 133 HIS   X ND1 1 
ATOM   42028 C  CD2 . HIS   X  10 133 ? 22.314  -162.504 1.623   1.00 94.48  ? 133 HIS   X CD2 1 
ATOM   42029 C  CE1 . HIS   X  10 133 ? 21.170  -162.416 3.498   1.00 94.24  ? 133 HIS   X CE1 1 
ATOM   42030 N  NE2 . HIS   X  10 133 ? 21.506  -163.207 2.475   1.00 91.66  ? 133 HIS   X NE2 1 
ATOM   42031 N  N   . GLY   X  10 134 ? 23.214  -157.062 3.006   1.00 96.50  ? 134 GLY   X N   1 
ATOM   42032 C  CA  . GLY   X  10 134 ? 23.940  -155.858 3.449   1.00 99.35  ? 134 GLY   X CA  1 
ATOM   42033 C  C   . GLY   X  10 134 ? 23.208  -154.586 3.057   1.00 101.62 ? 134 GLY   X C   1 
ATOM   42034 O  O   . GLY   X  10 134 ? 21.963  -154.626 2.936   1.00 96.44  ? 134 GLY   X O   1 
ATOM   42035 N  N   . TYR   X  10 135 ? 23.960  -153.500 2.846   1.00 104.55 ? 135 TYR   X N   1 
ATOM   42036 C  CA  . TYR   X  10 135 ? 23.439  -152.131 2.588   1.00 106.03 ? 135 TYR   X CA  1 
ATOM   42037 C  C   . TYR   X  10 135 ? 22.805  -152.044 1.190   1.00 109.00 ? 135 TYR   X C   1 
ATOM   42038 O  O   . TYR   X  10 135 ? 22.026  -151.096 0.961   1.00 110.24 ? 135 TYR   X O   1 
ATOM   42039 C  CB  . TYR   X  10 135 ? 24.550  -151.091 2.762   1.00 106.74 ? 135 TYR   X CB  1 
ATOM   42040 C  CG  . TYR   X  10 135 ? 25.034  -150.923 4.180   1.00 107.74 ? 135 TYR   X CG  1 
ATOM   42041 C  CD1 . TYR   X  10 135 ? 24.160  -150.561 5.194   1.00 108.16 ? 135 TYR   X CD1 1 
ATOM   42042 C  CD2 . TYR   X  10 135 ? 26.367  -151.113 4.511   1.00 108.86 ? 135 TYR   X CD2 1 
ATOM   42043 C  CE1 . TYR   X  10 135 ? 24.595  -150.397 6.500   1.00 111.14 ? 135 TYR   X CE1 1 
ATOM   42044 C  CE2 . TYR   X  10 135 ? 26.818  -150.954 5.812   1.00 110.53 ? 135 TYR   X CE2 1 
ATOM   42045 C  CZ  . TYR   X  10 135 ? 25.929  -150.595 6.811   1.00 112.25 ? 135 TYR   X CZ  1 
ATOM   42046 O  OH  . TYR   X  10 135 ? 26.363  -150.438 8.096   1.00 113.61 ? 135 TYR   X OH  1 
ATOM   42047 N  N   . SER   X  10 136 ? 23.128  -152.981 0.289   1.00 106.85 ? 136 SER   X N   1 
ATOM   42048 C  CA  . SER   X  10 136 ? 22.628  -153.034 -1.113  1.00 105.27 ? 136 SER   X CA  1 
ATOM   42049 C  C   . SER   X  10 136 ? 21.096  -153.005 -1.146  1.00 99.74  ? 136 SER   X C   1 
ATOM   42050 O  O   . SER   X  10 136 ? 20.540  -152.275 -1.986  1.00 102.36 ? 136 SER   X O   1 
ATOM   42051 C  CB  . SER   X  10 136 ? 23.137  -154.255 -1.829  1.00 105.89 ? 136 SER   X CB  1 
ATOM   42052 O  OG  . SER   X  10 136 ? 24.533  -154.418 -1.637  1.00 109.85 ? 136 SER   X OG  1 
ATOM   42053 N  N   . GLY   X  10 137 ? 20.449  -153.794 -0.284  1.00 96.53  ? 137 GLY   X N   1 
ATOM   42054 C  CA  . GLY   X  10 137 ? 18.980  -153.856 -0.152  1.00 94.65  ? 137 GLY   X CA  1 
ATOM   42055 C  C   . GLY   X  10 137 ? 18.352  -152.472 -0.074  1.00 93.60  ? 137 GLY   X C   1 
ATOM   42056 O  O   . GLY   X  10 137 ? 17.331  -152.244 -0.752  1.00 89.41  ? 137 GLY   X O   1 
ATOM   42057 N  N   . PHE   X  10 138 ? 18.956  -151.570 0.705   1.00 92.10  ? 138 PHE   X N   1 
ATOM   42058 C  CA  . PHE   X  10 138 ? 18.415  -150.228 1.048   1.00 95.42  ? 138 PHE   X CA  1 
ATOM   42059 C  C   . PHE   X  10 138 ? 18.183  -149.387 -0.217  1.00 96.56  ? 138 PHE   X C   1 
ATOM   42060 O  O   . PHE   X  10 138 ? 17.332  -148.477 -0.159  1.00 97.74  ? 138 PHE   X O   1 
ATOM   42061 C  CB  . PHE   X  10 138 ? 19.337  -149.521 2.045   1.00 94.78  ? 138 PHE   X CB  1 
ATOM   42062 C  CG  . PHE   X  10 138 ? 19.197  -150.008 3.466   1.00 95.99  ? 138 PHE   X CG  1 
ATOM   42063 C  CD1 . PHE   X  10 138 ? 19.965  -151.062 3.937   1.00 95.46  ? 138 PHE   X CD1 1 
ATOM   42064 C  CD2 . PHE   X  10 138 ? 18.286  -149.418 4.328   1.00 96.22  ? 138 PHE   X CD2 1 
ATOM   42065 C  CE1 . PHE   X  10 138 ? 19.829  -151.510 5.242   1.00 95.87  ? 138 PHE   X CE1 1 
ATOM   42066 C  CE2 . PHE   X  10 138 ? 18.150  -149.867 5.633   1.00 97.27  ? 138 PHE   X CE2 1 
ATOM   42067 C  CZ  . PHE   X  10 138 ? 18.923  -150.911 6.087   1.00 96.11  ? 138 PHE   X CZ  1 
ATOM   42068 N  N   . TYR   X  10 139 ? 18.897  -149.670 -1.312  1.00 97.52  ? 139 TYR   X N   1 
ATOM   42069 C  CA  . TYR   X  10 139 ? 18.742  -148.973 -2.618  1.00 103.43 ? 139 TYR   X CA  1 
ATOM   42070 C  C   . TYR   X  10 139 ? 17.957  -149.822 -3.624  1.00 106.88 ? 139 TYR   X C   1 
ATOM   42071 O  O   . TYR   X  10 139 ? 17.156  -149.239 -4.382  1.00 114.44 ? 139 TYR   X O   1 
ATOM   42072 C  CB  . TYR   X  10 139 ? 20.104  -148.610 -3.208  1.00 106.85 ? 139 TYR   X CB  1 
ATOM   42073 C  CG  . TYR   X  10 139 ? 20.760  -147.446 -2.515  1.00 113.49 ? 139 TYR   X CG  1 
ATOM   42074 C  CD1 . TYR   X  10 139 ? 20.282  -146.154 -2.684  1.00 117.66 ? 139 TYR   X CD1 1 
ATOM   42075 C  CD2 . TYR   X  10 139 ? 21.839  -147.634 -1.668  1.00 113.82 ? 139 TYR   X CD2 1 
ATOM   42076 C  CE1 . TYR   X  10 139 ? 20.871  -145.078 -2.040  1.00 119.63 ? 139 TYR   X CE1 1 
ATOM   42077 C  CE2 . TYR   X  10 139 ? 22.441  -146.569 -1.018  1.00 116.17 ? 139 TYR   X CE2 1 
ATOM   42078 C  CZ  . TYR   X  10 139 ? 21.954  -145.287 -1.204  1.00 120.81 ? 139 TYR   X CZ  1 
ATOM   42079 O  OH  . TYR   X  10 139 ? 22.545  -144.234 -0.567  1.00 122.84 ? 139 TYR   X OH  1 
ATOM   42080 N  N   . THR   X  10 140 ? 18.194  -151.137 -3.653  1.00 105.04 ? 140 THR   X N   1 
ATOM   42081 C  CA  . THR   X  10 140 ? 17.681  -152.046 -4.709  1.00 103.97 ? 140 THR   X CA  1 
ATOM   42082 C  C   . THR   X  10 140 ? 16.194  -152.337 -4.456  1.00 97.19  ? 140 THR   X C   1 
ATOM   42083 O  O   . THR   X  10 140 ? 15.410  -152.134 -5.396  1.00 91.63  ? 140 THR   X O   1 
ATOM   42084 C  CB  . THR   X  10 140 ? 18.588  -153.278 -4.835  1.00 107.34 ? 140 THR   X CB  1 
ATOM   42085 O  OG1 . THR   X  10 140 ? 18.720  -153.893 -3.553  1.00 113.96 ? 140 THR   X OG1 1 
ATOM   42086 C  CG2 . THR   X  10 140 ? 19.958  -152.921 -5.372  1.00 106.90 ? 140 THR   X CG2 1 
ATOM   42087 N  N   . PHE   X  10 141 ? 15.811  -152.747 -3.238  1.00 99.19  ? 141 PHE   X N   1 
ATOM   42088 C  CA  . PHE   X  10 141 ? 14.459  -153.290 -2.920  1.00 103.60 ? 141 PHE   X CA  1 
ATOM   42089 C  C   . PHE   X  10 141 ? 13.373  -152.324 -3.420  1.00 101.08 ? 141 PHE   X C   1 
ATOM   42090 O  O   . PHE   X  10 141 ? 12.459  -152.770 -4.127  1.00 100.78 ? 141 PHE   X O   1 
ATOM   42091 C  CB  . PHE   X  10 141 ? 14.303  -153.604 -1.426  1.00 103.29 ? 141 PHE   X CB  1 
ATOM   42092 C  CG  . PHE   X  10 141 ? 14.727  -154.994 -1.016  1.00 105.46 ? 141 PHE   X CG  1 
ATOM   42093 C  CD1 . PHE   X  10 141 ? 14.090  -156.112 -1.533  1.00 107.26 ? 141 PHE   X CD1 1 
ATOM   42094 C  CD2 . PHE   X  10 141 ? 15.747  -155.186 -0.095  1.00 105.65 ? 141 PHE   X CD2 1 
ATOM   42095 C  CE1 . PHE   X  10 141 ? 14.474  -157.389 -1.151  1.00 109.93 ? 141 PHE   X CE1 1 
ATOM   42096 C  CE2 . PHE   X  10 141 ? 16.130  -156.463 0.286   1.00 107.73 ? 141 PHE   X CE2 1 
ATOM   42097 C  CZ  . PHE   X  10 141 ? 15.492  -157.563 -0.242  1.00 109.59 ? 141 PHE   X CZ  1 
ATOM   42098 N  N   . SER   X  10 142 ? 13.475  -151.041 -3.073  1.00 104.96 ? 142 SER   X N   1 
ATOM   42099 C  CA  . SER   X  10 142 ? 12.531  -149.966 -3.493  1.00 107.95 ? 142 SER   X CA  1 
ATOM   42100 C  C   . SER   X  10 142 ? 12.516  -149.828 -5.021  1.00 106.70 ? 142 SER   X C   1 
ATOM   42101 O  O   . SER   X  10 142 ? 11.430  -149.552 -5.582  1.00 108.39 ? 142 SER   X O   1 
ATOM   42102 C  CB  . SER   X  10 142 ? 12.880  -148.647 -2.842  1.00 109.95 ? 142 SER   X CB  1 
ATOM   42103 O  OG  . SER   X  10 142 ? 14.120  -148.145 -3.324  1.00 110.21 ? 142 SER   X OG  1 
ATOM   42104 N  N   . LEU   X  10 143 ? 13.686  -149.978 -5.652  1.00 110.43 ? 143 LEU   X N   1 
ATOM   42105 C  CA  . LEU   X  10 143 ? 13.882  -149.897 -7.127  1.00 112.52 ? 143 LEU   X CA  1 
ATOM   42106 C  C   . LEU   X  10 143 ? 13.162  -151.076 -7.793  1.00 106.92 ? 143 LEU   X C   1 
ATOM   42107 O  O   . LEU   X  10 143 ? 12.412  -150.837 -8.756  1.00 108.38 ? 143 LEU   X O   1 
ATOM   42108 C  CB  . LEU   X  10 143 ? 15.385  -149.912 -7.434  1.00 112.50 ? 143 LEU   X CB  1 
ATOM   42109 C  CG  . LEU   X  10 143 ? 15.788  -149.536 -8.861  1.00 114.29 ? 143 LEU   X CG  1 
ATOM   42110 C  CD1 . LEU   X  10 143 ? 17.210  -148.998 -8.895  1.00 114.55 ? 143 LEU   X CD1 1 
ATOM   42111 C  CD2 . LEU   X  10 143 ? 15.658  -150.724 -9.803  1.00 113.27 ? 143 LEU   X CD2 1 
ATOM   42112 N  N   . LEU   X  10 144 ? 13.397  -152.298 -7.296  1.00 110.44 ? 144 LEU   X N   1 
ATOM   42113 C  CA  . LEU   X  10 144 ? 12.806  -153.563 -7.823  1.00 108.39 ? 144 LEU   X CA  1 
ATOM   42114 C  C   . LEU   X  10 144 ? 11.307  -153.620 -7.496  1.00 107.61 ? 144 LEU   X C   1 
ATOM   42115 O  O   . LEU   X  10 144 ? 10.548  -154.088 -8.359  1.00 105.22 ? 144 LEU   X O   1 
ATOM   42116 C  CB  . LEU   X  10 144 ? 13.555  -154.767 -7.234  1.00 106.50 ? 144 LEU   X CB  1 
ATOM   42117 C  CG  . LEU   X  10 144 ? 14.649  -155.399 -8.102  1.00 107.90 ? 144 LEU   X CG  1 
ATOM   42118 C  CD1 . LEU   X  10 144 ? 15.117  -154.479 -9.222  1.00 110.23 ? 144 LEU   X CD1 1 
ATOM   42119 C  CD2 . LEU   X  10 144 ? 15.833  -155.834 -7.252  1.00 105.87 ? 144 LEU   X CD2 1 
ATOM   42120 N  N   . ASP   X  10 145 ? 10.895  -153.153 -6.311  1.00 106.73 ? 145 ASP   X N   1 
ATOM   42121 C  CA  . ASP   X  10 145 ? 9.462   -153.027 -5.923  1.00 109.65 ? 145 ASP   X CA  1 
ATOM   42122 C  C   . ASP   X  10 145 ? 8.702   -152.338 -7.063  1.00 111.71 ? 145 ASP   X C   1 
ATOM   42123 O  O   . ASP   X  10 145 ? 7.563   -152.757 -7.351  1.00 109.09 ? 145 ASP   X O   1 
ATOM   42124 C  CB  . ASP   X  10 145 ? 9.285   -152.256 -4.608  1.00 112.07 ? 145 ASP   X CB  1 
ATOM   42125 C  CG  . ASP   X  10 145 ? 9.477   -153.081 -3.345  1.00 114.01 ? 145 ASP   X CG  1 
ATOM   42126 O  OD1 . ASP   X  10 145 ? 9.568   -154.324 -3.455  1.00 115.86 ? 145 ASP   X OD1 1 
ATOM   42127 O  OD2 . ASP   X  10 145 ? 9.527   -152.469 -2.255  1.00 116.18 ? 145 ASP   X OD2 1 
ATOM   42128 N  N   . HIS   X  10 146 ? 9.331   -151.337 -7.689  1.00 115.33 ? 146 HIS   X N   1 
ATOM   42129 C  CA  . HIS   X  10 146 ? 8.755   -150.486 -8.766  1.00 116.58 ? 146 HIS   X CA  1 
ATOM   42130 C  C   . HIS   X  10 146 ? 8.798   -151.242 -10.104 1.00 114.96 ? 146 HIS   X C   1 
ATOM   42131 O  O   . HIS   X  10 146 ? 7.715   -151.512 -10.662 1.00 110.17 ? 146 HIS   X O   1 
ATOM   42132 C  CB  . HIS   X  10 146 ? 9.485   -149.128 -8.793  1.00 120.10 ? 146 HIS   X CB  1 
ATOM   42133 C  CG  . HIS   X  10 146 ? 8.918   -148.123 -9.741  1.00 121.02 ? 146 HIS   X CG  1 
ATOM   42134 N  ND1 . HIS   X  10 146 ? 7.572   -147.816 -9.782  1.00 120.38 ? 146 HIS   X ND1 1 
ATOM   42135 C  CD2 . HIS   X  10 146 ? 9.514   -147.335 -10.661 1.00 123.00 ? 146 HIS   X CD2 1 
ATOM   42136 C  CE1 . HIS   X  10 146 ? 7.364   -146.897 -10.702 1.00 122.89 ? 146 HIS   X CE1 1 
ATOM   42137 N  NE2 . HIS   X  10 146 ? 8.538   -146.584 -11.253 1.00 125.49 ? 146 HIS   X NE2 1 
ATOM   42138 N  N   . HIS   X  10 147 ? 9.997   -151.603 -10.574 1.00 112.26 ? 147 HIS   X N   1 
ATOM   42139 C  CA  . HIS   X  10 147 ? 10.276  -151.983 -11.987 1.00 114.70 ? 147 HIS   X CA  1 
ATOM   42140 C  C   . HIS   X  10 147 ? 10.056  -153.484 -12.235 1.00 111.09 ? 147 HIS   X C   1 
ATOM   42141 O  O   . HIS   X  10 147 ? 9.819   -153.835 -13.401 1.00 111.48 ? 147 HIS   X O   1 
ATOM   42142 C  CB  . HIS   X  10 147 ? 11.694  -151.549 -12.392 1.00 116.84 ? 147 HIS   X CB  1 
ATOM   42143 C  CG  . HIS   X  10 147 ? 11.872  -150.072 -12.534 1.00 121.20 ? 147 HIS   X CG  1 
ATOM   42144 N  ND1 . HIS   X  10 147 ? 12.752  -149.356 -11.742 1.00 122.59 ? 147 HIS   X ND1 1 
ATOM   42145 C  CD2 . HIS   X  10 147 ? 11.301  -149.175 -13.368 1.00 123.43 ? 147 HIS   X CD2 1 
ATOM   42146 C  CE1 . HIS   X  10 147 ? 12.714  -148.083 -12.081 1.00 124.68 ? 147 HIS   X CE1 1 
ATOM   42147 N  NE2 . HIS   X  10 147 ? 11.829  -147.946 -13.077 1.00 123.12 ? 147 HIS   X NE2 1 
ATOM   42148 N  N   . TYR   X  10 148 ? 10.142  -154.342 -11.211 1.00 111.88 ? 148 TYR   X N   1 
ATOM   42149 C  CA  . TYR   X  10 148 ? 10.092  -155.825 -11.360 1.00 112.17 ? 148 TYR   X CA  1 
ATOM   42150 C  C   . TYR   X  10 148 ? 8.674   -156.289 -11.711 1.00 115.55 ? 148 TYR   X C   1 
ATOM   42151 O  O   . TYR   X  10 148 ? 7.711   -155.820 -11.072 1.00 112.01 ? 148 TYR   X O   1 
ATOM   42152 C  CB  . TYR   X  10 148 ? 10.538  -156.551 -10.087 1.00 110.34 ? 148 TYR   X CB  1 
ATOM   42153 C  CG  . TYR   X  10 148 ? 10.357  -158.050 -10.129 1.00 109.14 ? 148 TYR   X CG  1 
ATOM   42154 C  CD1 . TYR   X  10 148 ? 11.327  -158.874 -10.679 1.00 108.18 ? 148 TYR   X CD1 1 
ATOM   42155 C  CD2 . TYR   X  10 148 ? 9.211   -158.649 -9.626  1.00 107.33 ? 148 TYR   X CD2 1 
ATOM   42156 C  CE1 . TYR   X  10 148 ? 11.165  -160.250 -10.725 1.00 106.23 ? 148 TYR   X CE1 1 
ATOM   42157 C  CE2 . TYR   X  10 148 ? 9.033   -160.023 -9.663  1.00 104.60 ? 148 TYR   X CE2 1 
ATOM   42158 C  CZ  . TYR   X  10 148 ? 10.013  -160.827 -10.218 1.00 103.20 ? 148 TYR   X CZ  1 
ATOM   42159 O  OH  . TYR   X  10 148 ? 9.834   -162.179 -10.262 1.00 101.22 ? 148 TYR   X OH  1 
ATOM   42160 N  N   . ARG   X  10 149 ? 8.575   -157.212 -12.677 1.00 119.33 ? 149 ARG   X N   1 
ATOM   42161 C  CA  . ARG   X  10 149 ? 7.339   -157.966 -13.031 1.00 124.58 ? 149 ARG   X CA  1 
ATOM   42162 C  C   . ARG   X  10 149 ? 7.652   -159.464 -13.015 1.00 121.48 ? 149 ARG   X C   1 
ATOM   42163 O  O   . ARG   X  10 149 ? 8.728   -159.882 -13.439 1.00 117.36 ? 149 ARG   X O   1 
ATOM   42164 C  CB  . ARG   X  10 149 ? 6.802   -157.531 -14.401 1.00 128.67 ? 149 ARG   X CB  1 
ATOM   42165 C  CG  . ARG   X  10 149 ? 6.480   -156.046 -14.523 1.00 133.67 ? 149 ARG   X CG  1 
ATOM   42166 C  CD  . ARG   X  10 149 ? 5.296   -155.603 -13.679 1.00 135.65 ? 149 ARG   X CD  1 
ATOM   42167 N  NE  . ARG   X  10 149 ? 4.965   -154.191 -13.861 1.00 137.35 ? 149 ARG   X NE  1 
ATOM   42168 C  CZ  . ARG   X  10 149 ? 5.526   -153.171 -13.208 1.00 136.51 ? 149 ARG   X CZ  1 
ATOM   42169 N  NH1 . ARG   X  10 149 ? 6.473   -153.376 -12.305 1.00 139.32 ? 149 ARG   X NH1 1 
ATOM   42170 N  NH2 . ARG   X  10 149 ? 5.134   -151.934 -13.464 1.00 134.97 ? 149 ARG   X NH2 1 
ATOM   42171 N  N   . PRO   X  10 150 ? 6.718   -160.322 -12.538 1.00 120.33 ? 150 PRO   X N   1 
ATOM   42172 C  CA  . PRO   X  10 150 ? 7.007   -161.744 -12.328 1.00 118.12 ? 150 PRO   X CA  1 
ATOM   42173 C  C   . PRO   X  10 150 ? 7.213   -162.572 -13.608 1.00 116.60 ? 150 PRO   X C   1 
ATOM   42174 O  O   . PRO   X  10 150 ? 7.713   -163.675 -13.498 1.00 116.70 ? 150 PRO   X O   1 
ATOM   42175 C  CB  . PRO   X  10 150 ? 5.760   -162.248 -11.582 1.00 117.45 ? 150 PRO   X CB  1 
ATOM   42176 C  CG  . PRO   X  10 150 ? 4.656   -161.313 -12.029 1.00 119.69 ? 150 PRO   X CG  1 
ATOM   42177 C  CD  . PRO   X  10 150 ? 5.335   -159.969 -12.178 1.00 121.23 ? 150 PRO   X CD  1 
ATOM   42178 N  N   . ASP   X  10 151 ? 6.839   -162.030 -14.772 1.00 117.08 ? 151 ASP   X N   1 
ATOM   42179 C  CA  . ASP   X  10 151 ? 6.823   -162.753 -16.075 1.00 116.98 ? 151 ASP   X CA  1 
ATOM   42180 C  C   . ASP   X  10 151 ? 7.948   -162.245 -16.989 1.00 113.35 ? 151 ASP   X C   1 
ATOM   42181 O  O   . ASP   X  10 151 ? 7.845   -162.456 -18.211 1.00 111.91 ? 151 ASP   X O   1 
ATOM   42182 C  CB  . ASP   X  10 151 ? 5.459   -162.604 -16.758 1.00 119.06 ? 151 ASP   X CB  1 
ATOM   42183 C  CG  . ASP   X  10 151 ? 5.105   -161.177 -17.137 1.00 121.68 ? 151 ASP   X CG  1 
ATOM   42184 O  OD1 . ASP   X  10 151 ? 5.579   -160.251 -16.448 1.00 125.35 ? 151 ASP   X OD1 1 
ATOM   42185 O  OD2 . ASP   X  10 151 ? 4.360   -161.004 -18.119 1.00 121.84 ? 151 ASP   X OD2 1 
ATOM   42186 N  N   . MET   X  10 152 ? 8.988   -161.621 -16.427 1.00 114.33 ? 152 MET   X N   1 
ATOM   42187 C  CA  . MET   X  10 152 ? 10.092  -160.998 -17.207 1.00 114.81 ? 152 MET   X CA  1 
ATOM   42188 C  C   . MET   X  10 152 ? 10.955  -162.095 -17.837 1.00 112.53 ? 152 MET   X C   1 
ATOM   42189 O  O   . MET   X  10 152 ? 11.009  -163.199 -17.270 1.00 108.99 ? 152 MET   X O   1 
ATOM   42190 C  CB  . MET   X  10 152 ? 10.964  -160.102 -16.321 1.00 118.19 ? 152 MET   X CB  1 
ATOM   42191 C  CG  . MET   X  10 152 ? 10.291  -158.797 -15.957 1.00 119.63 ? 152 MET   X CG  1 
ATOM   42192 S  SD  . MET   X  10 152 ? 11.230  -157.871 -14.724 1.00 123.72 ? 152 MET   X SD  1 
ATOM   42193 C  CE  . MET   X  10 152 ? 12.244  -156.847 -15.790 1.00 124.22 ? 152 MET   X CE  1 
ATOM   42194 N  N   . THR   X  10 153 ? 11.583  -161.796 -18.976 1.00 110.83 ? 153 THR   X N   1 
ATOM   42195 C  CA  . THR   X  10 153 ? 12.577  -162.671 -19.653 1.00 113.64 ? 153 THR   X CA  1 
ATOM   42196 C  C   . THR   X  10 153 ? 13.940  -162.486 -18.982 1.00 112.50 ? 153 THR   X C   1 
ATOM   42197 O  O   . THR   X  10 153 ? 14.096  -161.502 -18.236 1.00 109.80 ? 153 THR   X O   1 
ATOM   42198 C  CB  . THR   X  10 153 ? 12.661  -162.371 -21.155 1.00 117.24 ? 153 THR   X CB  1 
ATOM   42199 O  OG1 . THR   X  10 153 ? 12.944  -160.983 -21.333 1.00 120.34 ? 153 THR   X OG1 1 
ATOM   42200 C  CG2 . THR   X  10 153 ? 11.388  -162.725 -21.889 1.00 120.29 ? 153 THR   X CG2 1 
ATOM   42201 N  N   . THR   X  10 154 ? 14.882  -163.401 -19.235 1.00 115.45 ? 154 THR   X N   1 
ATOM   42202 C  CA  . THR   X  10 154 ? 16.284  -163.327 -18.744 1.00 118.01 ? 154 THR   X CA  1 
ATOM   42203 C  C   . THR   X  10 154 ? 16.894  -161.989 -19.180 1.00 120.05 ? 154 THR   X C   1 
ATOM   42204 O  O   . THR   X  10 154 ? 17.614  -161.382 -18.364 1.00 123.34 ? 154 THR   X O   1 
ATOM   42205 C  CB  . THR   X  10 154 ? 17.120  -164.519 -19.230 1.00 121.22 ? 154 THR   X CB  1 
ATOM   42206 O  OG1 . THR   X  10 154 ? 16.518  -165.719 -18.740 1.00 124.34 ? 154 THR   X OG1 1 
ATOM   42207 C  CG2 . THR   X  10 154 ? 18.561  -164.456 -18.771 1.00 118.19 ? 154 THR   X CG2 1 
ATOM   42208 N  N   . GLU   X  10 155 ? 16.599  -161.544 -20.406 1.00 120.63 ? 155 GLU   X N   1 
ATOM   42209 C  CA  . GLU   X  10 155 ? 17.122  -160.275 -20.985 1.00 122.36 ? 155 GLU   X CA  1 
ATOM   42210 C  C   . GLU   X  10 155 ? 16.562  -159.071 -20.217 1.00 117.51 ? 155 GLU   X C   1 
ATOM   42211 O  O   . GLU   X  10 155 ? 17.349  -158.147 -19.927 1.00 112.02 ? 155 GLU   X O   1 
ATOM   42212 C  CB  . GLU   X  10 155 ? 16.785  -160.173 -22.474 1.00 128.80 ? 155 GLU   X CB  1 
ATOM   42213 C  CG  . GLU   X  10 155 ? 17.894  -160.687 -23.372 1.00 135.02 ? 155 GLU   X CG  1 
ATOM   42214 C  CD  . GLU   X  10 155 ? 19.202  -159.928 -23.233 1.00 139.68 ? 155 GLU   X CD  1 
ATOM   42215 O  OE1 . GLU   X  10 155 ? 19.163  -158.679 -23.219 1.00 146.19 ? 155 GLU   X OE1 1 
ATOM   42216 O  OE2 . GLU   X  10 155 ? 20.255  -160.587 -23.117 1.00 144.21 ? 155 GLU   X OE2 1 
ATOM   42217 N  N   . GLU   X  10 156 ? 15.258  -159.076 -19.922 1.00 113.75 ? 156 GLU   X N   1 
ATOM   42218 C  CA  . GLU   X  10 156 ? 14.581  -158.040 -19.097 1.00 113.16 ? 156 GLU   X CA  1 
ATOM   42219 C  C   . GLU   X  10 156 ? 15.199  -158.034 -17.693 1.00 112.57 ? 156 GLU   X C   1 
ATOM   42220 O  O   . GLU   X  10 156 ? 15.483  -156.935 -17.180 1.00 112.29 ? 156 GLU   X O   1 
ATOM   42221 C  CB  . GLU   X  10 156 ? 13.072  -158.290 -19.040 1.00 114.47 ? 156 GLU   X CB  1 
ATOM   42222 C  CG  . GLU   X  10 156 ? 12.346  -157.893 -20.310 1.00 119.44 ? 156 GLU   X CG  1 
ATOM   42223 C  CD  . GLU   X  10 156 ? 10.878  -158.281 -20.344 1.00 123.12 ? 156 GLU   X CD  1 
ATOM   42224 O  OE1 . GLU   X  10 156 ? 10.028  -157.369 -20.365 1.00 126.35 ? 156 GLU   X OE1 1 
ATOM   42225 O  OE2 . GLU   X  10 156 ? 10.587  -159.495 -20.357 1.00 125.56 ? 156 GLU   X OE2 1 
ATOM   42226 N  N   . GLY   X  10 157 ? 15.403  -159.219 -17.110 1.00 109.48 ? 157 GLY   X N   1 
ATOM   42227 C  CA  . GLY   X  10 157 ? 16.058  -159.409 -15.801 1.00 107.11 ? 157 GLY   X CA  1 
ATOM   42228 C  C   . GLY   X  10 157 ? 17.430  -158.760 -15.756 1.00 107.62 ? 157 GLY   X C   1 
ATOM   42229 O  O   . GLY   X  10 157 ? 17.740  -158.130 -14.729 1.00 108.32 ? 157 GLY   X O   1 
ATOM   42230 N  N   . LEU   X  10 158 ? 18.223  -158.903 -16.825 1.00 108.62 ? 158 LEU   X N   1 
ATOM   42231 C  CA  . LEU   X  10 158 ? 19.606  -158.357 -16.922 1.00 109.22 ? 158 LEU   X CA  1 
ATOM   42232 C  C   . LEU   X  10 158 ? 19.565  -156.827 -17.014 1.00 110.95 ? 158 LEU   X C   1 
ATOM   42233 O  O   . LEU   X  10 158 ? 20.457  -156.191 -16.428 1.00 111.05 ? 158 LEU   X O   1 
ATOM   42234 C  CB  . LEU   X  10 158 ? 20.321  -158.958 -18.136 1.00 110.64 ? 158 LEU   X CB  1 
ATOM   42235 C  CG  . LEU   X  10 158 ? 20.726  -160.425 -18.006 1.00 109.69 ? 158 LEU   X CG  1 
ATOM   42236 C  CD1 . LEU   X  10 158 ? 21.110  -160.996 -19.361 1.00 112.64 ? 158 LEU   X CD1 1 
ATOM   42237 C  CD2 . LEU   X  10 158 ? 21.864  -160.600 -17.010 1.00 108.29 ? 158 LEU   X CD2 1 
ATOM   42238 N  N   . ASP   X  10 159 ? 18.583  -156.265 -17.727 1.00 112.63 ? 159 ASP   X N   1 
ATOM   42239 C  CA  . ASP   X  10 159 ? 18.373  -154.795 -17.855 1.00 114.56 ? 159 ASP   X CA  1 
ATOM   42240 C  C   . ASP   X  10 159 ? 17.933  -154.218 -16.503 1.00 113.22 ? 159 ASP   X C   1 
ATOM   42241 O  O   . ASP   X  10 159 ? 18.409  -153.119 -16.142 1.00 111.82 ? 159 ASP   X O   1 
ATOM   42242 C  CB  . ASP   X  10 159 ? 17.344  -154.468 -18.941 1.00 115.91 ? 159 ASP   X CB  1 
ATOM   42243 C  CG  . ASP   X  10 159 ? 17.819  -154.756 -20.355 1.00 118.38 ? 159 ASP   X CG  1 
ATOM   42244 O  OD1 . ASP   X  10 159 ? 19.047  -154.831 -20.562 1.00 120.06 ? 159 ASP   X OD1 1 
ATOM   42245 O  OD2 . ASP   X  10 159 ? 16.954  -154.898 -21.241 1.00 120.53 ? 159 ASP   X OD2 1 
ATOM   42246 N  N   . LEU   X  10 160 ? 17.051  -154.934 -15.797 1.00 112.78 ? 160 LEU   X N   1 
ATOM   42247 C  CA  . LEU   X  10 160 ? 16.553  -154.584 -14.438 1.00 109.39 ? 160 LEU   X CA  1 
ATOM   42248 C  C   . LEU   X  10 160 ? 17.722  -154.603 -13.447 1.00 108.15 ? 160 LEU   X C   1 
ATOM   42249 O  O   . LEU   X  10 160 ? 17.719  -153.779 -12.514 1.00 107.97 ? 160 LEU   X O   1 
ATOM   42250 C  CB  . LEU   X  10 160 ? 15.478  -155.599 -14.037 1.00 107.55 ? 160 LEU   X CB  1 
ATOM   42251 C  CG  . LEU   X  10 160 ? 14.609  -155.222 -12.839 1.00 105.81 ? 160 LEU   X CG  1 
ATOM   42252 C  CD1 . LEU   X  10 160 ? 13.674  -154.079 -13.185 1.00 106.96 ? 160 LEU   X CD1 1 
ATOM   42253 C  CD2 . LEU   X  10 160 ? 13.809  -156.422 -12.359 1.00 106.26 ? 160 LEU   X CD2 1 
ATOM   42254 N  N   . LEU   X  10 161 ? 18.674  -155.520 -13.654 1.00 108.59 ? 161 LEU   X N   1 
ATOM   42255 C  CA  . LEU   X  10 161 ? 19.895  -155.697 -12.823 1.00 110.26 ? 161 LEU   X CA  1 
ATOM   42256 C  C   . LEU   X  10 161 ? 20.892  -154.567 -13.117 1.00 110.39 ? 161 LEU   X C   1 
ATOM   42257 O  O   . LEU   X  10 161 ? 21.522  -154.083 -12.160 1.00 108.26 ? 161 LEU   X O   1 
ATOM   42258 C  CB  . LEU   X  10 161 ? 20.498  -157.070 -13.135 1.00 113.25 ? 161 LEU   X CB  1 
ATOM   42259 C  CG  . LEU   X  10 161 ? 21.542  -157.593 -12.151 1.00 116.11 ? 161 LEU   X CG  1 
ATOM   42260 C  CD1 . LEU   X  10 161 ? 20.911  -157.944 -10.809 1.00 116.87 ? 161 LEU   X CD1 1 
ATOM   42261 C  CD2 . LEU   X  10 161 ? 22.250  -158.805 -12.739 1.00 117.73 ? 161 LEU   X CD2 1 
ATOM   42262 N  N   . LYS   X  10 162 ? 21.034  -154.167 -14.387 1.00 111.93 ? 162 LYS   X N   1 
ATOM   42263 C  CA  . LYS   X  10 162 ? 21.890  -153.025 -14.817 1.00 115.45 ? 162 LYS   X CA  1 
ATOM   42264 C  C   . LYS   X  10 162 ? 21.446  -151.747 -14.098 1.00 114.28 ? 162 LYS   X C   1 
ATOM   42265 O  O   . LYS   X  10 162 ? 22.323  -150.946 -13.716 1.00 115.49 ? 162 LYS   X O   1 
ATOM   42266 C  CB  . LYS   X  10 162 ? 21.803  -152.795 -16.328 1.00 119.62 ? 162 LYS   X CB  1 
ATOM   42267 C  CG  . LYS   X  10 162 ? 22.666  -153.714 -17.178 1.00 122.23 ? 162 LYS   X CG  1 
ATOM   42268 C  CD  . LYS   X  10 162 ? 22.646  -153.345 -18.643 1.00 127.28 ? 162 LYS   X CD  1 
ATOM   42269 C  CE  . LYS   X  10 162 ? 23.502  -152.135 -18.953 1.00 130.46 ? 162 LYS   X CE  1 
ATOM   42270 N  NZ  . LYS   X  10 162 ? 23.312  -151.674 -20.348 1.00 133.09 ? 162 LYS   X NZ  1 
ATOM   42271 N  N   . LEU   X  10 163 ? 20.132  -151.567 -13.946 1.00 113.52 ? 163 LEU   X N   1 
ATOM   42272 C  CA  . LEU   X  10 163 ? 19.511  -150.404 -13.259 1.00 115.01 ? 163 LEU   X CA  1 
ATOM   42273 C  C   . LEU   X  10 163 ? 19.945  -150.395 -11.789 1.00 112.84 ? 163 LEU   X C   1 
ATOM   42274 O  O   . LEU   X  10 163 ? 20.206  -149.300 -11.263 1.00 120.90 ? 163 LEU   X O   1 
ATOM   42275 C  CB  . LEU   X  10 163 ? 17.986  -150.498 -13.388 1.00 115.43 ? 163 LEU   X CB  1 
ATOM   42276 C  CG  . LEU   X  10 163 ? 17.261  -149.205 -13.763 1.00 118.04 ? 163 LEU   X CG  1 
ATOM   42277 C  CD1 . LEU   X  10 163 ? 17.818  -148.606 -15.048 1.00 119.45 ? 163 LEU   X CD1 1 
ATOM   42278 C  CD2 . LEU   X  10 163 ? 15.769  -149.463 -13.909 1.00 119.55 ? 163 LEU   X CD2 1 
ATOM   42279 N  N   . CYS   X  10 164 ? 20.027  -151.572 -11.159 1.00 109.68 ? 164 CYS   X N   1 
ATOM   42280 C  CA  . CYS   X  10 164 ? 20.410  -151.741 -9.732  1.00 105.62 ? 164 CYS   X CA  1 
ATOM   42281 C  C   . CYS   X  10 164 ? 21.893  -151.398 -9.549  1.00 99.69  ? 164 CYS   X C   1 
ATOM   42282 O  O   . CYS   X  10 164 ? 22.192  -150.634 -8.622  1.00 96.81  ? 164 CYS   X O   1 
ATOM   42283 C  CB  . CYS   X  10 164 ? 20.109  -153.151 -9.236  1.00 105.64 ? 164 CYS   X CB  1 
ATOM   42284 S  SG  . CYS   X  10 164 ? 18.333  -153.504 -9.150  1.00 109.69 ? 164 CYS   X SG  1 
ATOM   42285 N  N   . VAL   X  10 165 ? 22.774  -151.929 -10.407 1.00 100.55 ? 165 VAL   X N   1 
ATOM   42286 C  CA  . VAL   X  10 165 ? 24.248  -151.680 -10.359 1.00 101.88 ? 165 VAL   X CA  1 
ATOM   42287 C  C   . VAL   X  10 165 ? 24.503  -150.180 -10.556 1.00 102.91 ? 165 VAL   X C   1 
ATOM   42288 O  O   . VAL   X  10 165 ? 25.370  -149.638 -9.845  1.00 104.77 ? 165 VAL   X O   1 
ATOM   42289 C  CB  . VAL   X  10 165 ? 25.019  -152.520 -11.398 1.00 102.96 ? 165 VAL   X CB  1 
ATOM   42290 C  CG1 . VAL   X  10 165 ? 26.479  -152.098 -11.505 1.00 103.90 ? 165 VAL   X CG1 1 
ATOM   42291 C  CG2 . VAL   X  10 165 ? 24.928  -154.007 -11.095 1.00 102.33 ? 165 VAL   X CG2 1 
ATOM   42292 N  N   . GLN   X  10 166 ? 23.781  -149.546 -11.486 1.00 103.49 ? 166 GLN   X N   1 
ATOM   42293 C  CA  . GLN   X  10 166 ? 23.903  -148.095 -11.805 1.00 103.95 ? 166 GLN   X CA  1 
ATOM   42294 C  C   . GLN   X  10 166 ? 23.587  -147.259 -10.559 1.00 100.57 ? 166 GLN   X C   1 
ATOM   42295 O  O   . GLN   X  10 166 ? 24.389  -146.365 -10.237 1.00 98.33  ? 166 GLN   X O   1 
ATOM   42296 C  CB  . GLN   X  10 166 ? 22.979  -147.714 -12.962 1.00 106.02 ? 166 GLN   X CB  1 
ATOM   42297 C  CG  . GLN   X  10 166 ? 23.607  -147.944 -14.328 1.00 107.94 ? 166 GLN   X CG  1 
ATOM   42298 C  CD  . GLN   X  10 166 ? 22.597  -147.929 -15.449 1.00 109.72 ? 166 GLN   X CD  1 
ATOM   42299 O  OE1 . GLN   X  10 166 ? 21.516  -147.357 -15.332 1.00 109.17 ? 166 GLN   X OE1 1 
ATOM   42300 N  NE2 . GLN   X  10 166 ? 22.948  -148.564 -16.554 1.00 111.59 ? 166 GLN   X NE2 1 
ATOM   42301 N  N   . GLU   X  10 167 ? 22.466  -147.554 -9.891  1.00 101.75 ? 167 GLU   X N   1 
ATOM   42302 C  CA  . GLU   X  10 167 ? 22.004  -146.858 -8.658  1.00 101.85 ? 167 GLU   X CA  1 
ATOM   42303 C  C   . GLU   X  10 167 ? 23.058  -147.012 -7.555  1.00 101.94 ? 167 GLU   X C   1 
ATOM   42304 O  O   . GLU   X  10 167 ? 23.350  -146.007 -6.889  1.00 103.28 ? 167 GLU   X O   1 
ATOM   42305 C  CB  . GLU   X  10 167 ? 20.651  -147.408 -8.195  1.00 102.01 ? 167 GLU   X CB  1 
ATOM   42306 C  CG  . GLU   X  10 167 ? 20.124  -146.762 -6.922  1.00 102.40 ? 167 GLU   X CG  1 
ATOM   42307 C  CD  . GLU   X  10 167 ? 19.921  -145.256 -7.000  1.00 104.66 ? 167 GLU   X CD  1 
ATOM   42308 O  OE1 . GLU   X  10 167 ? 19.765  -144.621 -5.936  1.00 104.29 ? 167 GLU   X OE1 1 
ATOM   42309 O  OE2 . GLU   X  10 167 ? 19.913  -144.720 -8.122  1.00 108.32 ? 167 GLU   X OE2 1 
ATOM   42310 N  N   . LEU   X  10 168 ? 23.594  -148.223 -7.369  1.00 100.20 ? 168 LEU   X N   1 
ATOM   42311 C  CA  . LEU   X  10 168 ? 24.626  -148.531 -6.342  1.00 99.86  ? 168 LEU   X CA  1 
ATOM   42312 C  C   . LEU   X  10 168 ? 25.917  -147.773 -6.676  1.00 100.64 ? 168 LEU   X C   1 
ATOM   42313 O  O   . LEU   X  10 168 ? 26.533  -147.242 -5.741  1.00 100.99 ? 168 LEU   X O   1 
ATOM   42314 C  CB  . LEU   X  10 168 ? 24.863  -150.046 -6.274  1.00 98.51  ? 168 LEU   X CB  1 
ATOM   42315 C  CG  . LEU   X  10 168 ? 23.690  -150.881 -5.758  1.00 97.74  ? 168 LEU   X CG  1 
ATOM   42316 C  CD1 . LEU   X  10 168 ? 23.925  -152.362 -6.010  1.00 97.37  ? 168 LEU   X CD1 1 
ATOM   42317 C  CD2 . LEU   X  10 168 ? 23.439  -150.628 -4.280  1.00 97.56  ? 168 LEU   X CD2 1 
ATOM   42318 N  N   . GLU   X  10 169 ? 26.296  -147.698 -7.957  1.00 101.50 ? 169 GLU   X N   1 
ATOM   42319 C  CA  . GLU   X  10 169 ? 27.540  -147.014 -8.413  1.00 105.16 ? 169 GLU   X CA  1 
ATOM   42320 C  C   . GLU   X  10 169 ? 27.405  -145.493 -8.253  1.00 104.59 ? 169 GLU   X C   1 
ATOM   42321 O  O   . GLU   X  10 169 ? 28.450  -144.812 -8.269  1.00 104.01 ? 169 GLU   X O   1 
ATOM   42322 C  CB  . GLU   X  10 169 ? 27.873  -147.378 -9.861  1.00 109.04 ? 169 GLU   X CB  1 
ATOM   42323 C  CG  . GLU   X  10 169 ? 28.594  -148.709 -9.992  1.00 111.65 ? 169 GLU   X CG  1 
ATOM   42324 C  CD  . GLU   X  10 169 ? 28.906  -149.144 -11.415 1.00 116.26 ? 169 GLU   X CD  1 
ATOM   42325 O  OE1 . GLU   X  10 169 ? 29.660  -150.127 -11.579 1.00 118.18 ? 169 GLU   X OE1 1 
ATOM   42326 O  OE2 . GLU   X  10 169 ? 28.392  -148.504 -12.357 1.00 123.85 ? 169 GLU   X OE2 1 
ATOM   42327 N  N   . LYS   X  10 170 ? 26.179  -144.983 -8.101  1.00 104.20 ? 170 LYS   X N   1 
ATOM   42328 C  CA  . LYS   X  10 170 ? 25.895  -143.531 -7.956  1.00 106.21 ? 170 LYS   X CA  1 
ATOM   42329 C  C   . LYS   X  10 170 ? 25.904  -143.134 -6.473  1.00 105.55 ? 170 LYS   X C   1 
ATOM   42330 O  O   . LYS   X  10 170 ? 26.506  -142.092 -6.161  1.00 106.95 ? 170 LYS   X O   1 
ATOM   42331 C  CB  . LYS   X  10 170 ? 24.556  -143.176 -8.612  1.00 108.11 ? 170 LYS   X CB  1 
ATOM   42332 C  CG  . LYS   X  10 170 ? 24.152  -141.712 -8.494  1.00 110.75 ? 170 LYS   X CG  1 
ATOM   42333 C  CD  . LYS   X  10 170 ? 23.069  -141.288 -9.465  1.00 113.06 ? 170 LYS   X CD  1 
ATOM   42334 C  CE  . LYS   X  10 170 ? 22.632  -139.850 -9.276  1.00 115.90 ? 170 LYS   X CE  1 
ATOM   42335 N  NZ  . LYS   X  10 170 ? 23.746  -138.894 -9.488  1.00 118.37 ? 170 LYS   X NZ  1 
ATOM   42336 N  N   . ARG   X  10 171 ? 25.273  -143.929 -5.600  1.00 102.95 ? 171 ARG   X N   1 
ATOM   42337 C  CA  . ARG   X  10 171 ? 24.891  -143.508 -4.221  1.00 104.20 ? 171 ARG   X CA  1 
ATOM   42338 C  C   . ARG   X  10 171 ? 25.683  -144.248 -3.133  1.00 104.10 ? 171 ARG   X C   1 
ATOM   42339 O  O   . ARG   X  10 171 ? 25.678  -143.753 -1.987  1.00 104.67 ? 171 ARG   X O   1 
ATOM   42340 C  CB  . ARG   X  10 171 ? 23.387  -143.711 -4.010  1.00 103.67 ? 171 ARG   X CB  1 
ATOM   42341 C  CG  . ARG   X  10 171 ? 22.509  -142.838 -4.894  1.00 106.94 ? 171 ARG   X CG  1 
ATOM   42342 C  CD  . ARG   X  10 171 ? 22.710  -141.358 -4.615  1.00 108.59 ? 171 ARG   X CD  1 
ATOM   42343 N  NE  . ARG   X  10 171 ? 21.804  -140.506 -5.370  1.00 112.63 ? 171 ARG   X NE  1 
ATOM   42344 C  CZ  . ARG   X  10 171 ? 21.798  -139.175 -5.331  1.00 115.38 ? 171 ARG   X CZ  1 
ATOM   42345 N  NH1 . ARG   X  10 171 ? 22.654  -138.521 -4.562  1.00 116.21 ? 171 ARG   X NH1 1 
ATOM   42346 N  NH2 . ARG   X  10 171 ? 20.931  -138.497 -6.064  1.00 118.86 ? 171 ARG   X NH2 1 
ATOM   42347 N  N   . MET   X  10 172 ? 26.321  -145.379 -3.441  1.00 104.02 ? 172 MET   X N   1 
ATOM   42348 C  CA  . MET   X  10 172 ? 27.109  -146.152 -2.444  1.00 106.82 ? 172 MET   X CA  1 
ATOM   42349 C  C   . MET   X  10 172 ? 28.434  -145.438 -2.186  1.00 104.21 ? 172 MET   X C   1 
ATOM   42350 O  O   . MET   X  10 172 ? 29.059  -144.939 -3.120  1.00 103.07 ? 172 MET   X O   1 
ATOM   42351 C  CB  . MET   X  10 172 ? 27.373  -147.585 -2.917  1.00 107.40 ? 172 MET   X CB  1 
ATOM   42352 C  CG  . MET   X  10 172 ? 26.194  -148.503 -2.691  1.00 111.19 ? 172 MET   X CG  1 
ATOM   42353 S  SD  . MET   X  10 172 ? 26.262  -149.226 -1.038  1.00 116.34 ? 172 MET   X SD  1 
ATOM   42354 C  CE  . MET   X  10 172 ? 24.546  -149.679 -0.798  1.00 118.73 ? 172 MET   X CE  1 
ATOM   42355 N  N   . PRO   X  10 173 ? 28.901  -145.363 -0.917  1.00 105.22 ? 173 PRO   X N   1 
ATOM   42356 C  CA  . PRO   X  10 173 ? 30.160  -144.690 -0.590  1.00 105.58 ? 173 PRO   X CA  1 
ATOM   42357 C  C   . PRO   X  10 173 ? 31.418  -145.358 -1.171  1.00 106.38 ? 173 PRO   X C   1 
ATOM   42358 O  O   . PRO   X  10 173 ? 32.330  -144.635 -1.515  1.00 102.36 ? 173 PRO   X O   1 
ATOM   42359 C  CB  . PRO   X  10 173 ? 30.231  -144.752 0.946   1.00 106.52 ? 173 PRO   X CB  1 
ATOM   42360 C  CG  . PRO   X  10 173 ? 28.815  -145.059 1.390   1.00 107.43 ? 173 PRO   X CG  1 
ATOM   42361 C  CD  . PRO   X  10 173 ? 28.241  -145.910 0.278   1.00 106.52 ? 173 PRO   X CD  1 
ATOM   42362 N  N   . MET   X  10 174 ? 31.441  -146.696 -1.259  1.00 108.61 ? 174 MET   X N   1 
ATOM   42363 C  CA  . MET   X  10 174 ? 32.660  -147.496 -1.576  1.00 114.38 ? 174 MET   X CA  1 
ATOM   42364 C  C   . MET   X  10 174 ? 32.650  -147.948 -3.044  1.00 111.10 ? 174 MET   X C   1 
ATOM   42365 O  O   . MET   X  10 174 ? 31.555  -148.177 -3.598  1.00 109.97 ? 174 MET   X O   1 
ATOM   42366 C  CB  . MET   X  10 174 ? 32.785  -148.716 -0.652  1.00 117.21 ? 174 MET   X CB  1 
ATOM   42367 C  CG  . MET   X  10 174 ? 31.907  -149.905 -1.029  1.00 125.37 ? 174 MET   X CG  1 
ATOM   42368 S  SD  . MET   X  10 174 ? 30.128  -149.550 -1.009  1.00 131.87 ? 174 MET   X SD  1 
ATOM   42369 C  CE  . MET   X  10 174 ? 29.480  -151.146 -1.504  1.00 131.95 ? 174 MET   X CE  1 
ATOM   42370 N  N   . ASP   X  10 175 ? 33.843  -148.067 -3.638  1.00 109.60 ? 175 ASP   X N   1 
ATOM   42371 C  CA  . ASP   X  10 175 ? 34.067  -148.592 -5.011  1.00 109.18 ? 175 ASP   X CA  1 
ATOM   42372 C  C   . ASP   X  10 175 ? 34.148  -150.119 -4.930  1.00 107.38 ? 175 ASP   X C   1 
ATOM   42373 O  O   . ASP   X  10 175 ? 35.139  -150.623 -4.370  1.00 112.79 ? 175 ASP   X O   1 
ATOM   42374 C  CB  . ASP   X  10 175 ? 35.335  -147.998 -5.630  1.00 110.77 ? 175 ASP   X CB  1 
ATOM   42375 C  CG  . ASP   X  10 175 ? 35.432  -148.195 -7.132  1.00 112.48 ? 175 ASP   X CG  1 
ATOM   42376 O  OD1 . ASP   X  10 175 ? 34.869  -149.188 -7.633  1.00 110.97 ? 175 ASP   X OD1 1 
ATOM   42377 O  OD2 . ASP   X  10 175 ? 36.067  -147.347 -7.790  1.00 114.42 ? 175 ASP   X OD2 1 
ATOM   42378 N  N   . PHE   X  10 176 ? 33.145  -150.817 -5.467  1.00 102.63 ? 176 PHE   X N   1 
ATOM   42379 C  CA  . PHE   X  10 176 ? 33.009  -152.297 -5.397  1.00 100.01 ? 176 PHE   X CA  1 
ATOM   42380 C  C   . PHE   X  10 176 ? 33.440  -152.933 -6.727  1.00 97.90  ? 176 PHE   X C   1 
ATOM   42381 O  O   . PHE   X  10 176 ? 33.259  -154.153 -6.885  1.00 96.17  ? 176 PHE   X O   1 
ATOM   42382 C  CB  . PHE   X  10 176 ? 31.584  -152.677 -4.987  1.00 97.42  ? 176 PHE   X CB  1 
ATOM   42383 C  CG  . PHE   X  10 176 ? 30.503  -152.258 -5.949  1.00 96.93  ? 176 PHE   X CG  1 
ATOM   42384 C  CD1 . PHE   X  10 176 ? 30.126  -153.087 -6.993  1.00 98.32  ? 176 PHE   X CD1 1 
ATOM   42385 C  CD2 . PHE   X  10 176 ? 29.850  -151.045 -5.800  1.00 97.78  ? 176 PHE   X CD2 1 
ATOM   42386 C  CE1 . PHE   X  10 176 ? 29.126  -152.706 -7.875  1.00 98.73  ? 176 PHE   X CE1 1 
ATOM   42387 C  CE2 . PHE   X  10 176 ? 28.849  -150.667 -6.682  1.00 99.16  ? 176 PHE   X CE2 1 
ATOM   42388 C  CZ  . PHE   X  10 176 ? 28.489  -151.498 -7.717  1.00 98.90  ? 176 PHE   X CZ  1 
ATOM   42389 N  N   . LYS   X  10 177 ? 33.990  -152.131 -7.647  1.00 99.37  ? 177 LYS   X N   1 
ATOM   42390 C  CA  . LYS   X  10 177 ? 34.708  -152.580 -8.873  1.00 99.05  ? 177 LYS   X CA  1 
ATOM   42391 C  C   . LYS   X  10 177 ? 33.798  -153.428 -9.774  1.00 97.76  ? 177 LYS   X C   1 
ATOM   42392 O  O   . LYS   X  10 177 ? 34.323  -154.344 -10.432 1.00 97.76  ? 177 LYS   X O   1 
ATOM   42393 C  CB  . LYS   X  10 177 ? 35.965  -153.367 -8.484  1.00 98.28  ? 177 LYS   X CB  1 
ATOM   42394 C  CG  . LYS   X  10 177 ? 36.972  -152.614 -7.625  1.00 98.98  ? 177 LYS   X CG  1 
ATOM   42395 C  CD  . LYS   X  10 177 ? 37.559  -151.394 -8.303  1.00 101.50 ? 177 LYS   X CD  1 
ATOM   42396 C  CE  . LYS   X  10 177 ? 38.554  -150.660 -7.430  1.00 101.93 ? 177 LYS   X CE  1 
ATOM   42397 N  NZ  . LYS   X  10 177 ? 38.807  -149.287 -7.925  1.00 104.08 ? 177 LYS   X NZ  1 
ATOM   42398 N  N   . GLY   X  10 178 ? 32.498  -153.122 -9.834  1.00 97.43  ? 178 GLY   X N   1 
ATOM   42399 C  CA  . GLY   X  10 178 ? 31.532  -153.813 -10.713 1.00 99.12  ? 178 GLY   X CA  1 
ATOM   42400 C  C   . GLY   X  10 178 ? 31.170  -155.195 -10.193 1.00 98.16  ? 178 GLY   X C   1 
ATOM   42401 O  O   . GLY   X  10 178 ? 31.622  -155.540 -9.084  1.00 98.92  ? 178 GLY   X O   1 
ATOM   42402 N  N   . VAL   X  10 179 ? 30.400  -155.968 -10.970 1.00 100.08 ? 179 VAL   X N   1 
ATOM   42403 C  CA  . VAL   X  10 179 ? 29.810  -157.274 -10.539 1.00 100.50 ? 179 VAL   X CA  1 
ATOM   42404 C  C   . VAL   X  10 179 ? 30.108  -158.370 -11.572 1.00 100.19 ? 179 VAL   X C   1 
ATOM   42405 O  O   . VAL   X  10 179 ? 30.282  -158.038 -12.765 1.00 101.28 ? 179 VAL   X O   1 
ATOM   42406 C  CB  . VAL   X  10 179 ? 28.291  -157.150 -10.295 1.00 100.20 ? 179 VAL   X CB  1 
ATOM   42407 C  CG1 . VAL   X  10 179 ? 27.984  -156.265 -9.098  1.00 99.72  ? 179 VAL   X CG1 1 
ATOM   42408 C  CG2 . VAL   X  10 179 ? 27.542  -156.664 -11.528 1.00 100.78 ? 179 VAL   X CG2 1 
ATOM   42409 N  N   . ILE   X  10 180 ? 30.158  -159.627 -11.110 1.00 97.46  ? 180 ILE   X N   1 
ATOM   42410 C  CA  . ILE   X  10 180 ? 30.118  -160.861 -11.952 1.00 96.50  ? 180 ILE   X CA  1 
ATOM   42411 C  C   . ILE   X  10 180 ? 28.676  -161.375 -11.937 1.00 94.02  ? 180 ILE   X C   1 
ATOM   42412 O  O   . ILE   X  10 180 ? 28.159  -161.657 -10.839 1.00 93.71  ? 180 ILE   X O   1 
ATOM   42413 C  CB  . ILE   X  10 180 ? 31.123  -161.924 -11.459 1.00 95.88  ? 180 ILE   X CB  1 
ATOM   42414 C  CG1 . ILE   X  10 180 ? 32.554  -161.562 -11.863 1.00 96.55  ? 180 ILE   X CG1 1 
ATOM   42415 C  CG2 . ILE   X  10 180 ? 30.739  -163.310 -11.955 1.00 97.96  ? 180 ILE   X CG2 1 
ATOM   42416 C  CD1 . ILE   X  10 180 ? 33.627  -162.367 -11.165 1.00 96.56  ? 180 ILE   X CD1 1 
ATOM   42417 N  N   . VAL   X  10 181 ? 28.057  -161.476 -13.113 1.00 94.69  ? 181 VAL   X N   1 
ATOM   42418 C  CA  . VAL   X  10 181 ? 26.636  -161.898 -13.282 1.00 99.43  ? 181 VAL   X CA  1 
ATOM   42419 C  C   . VAL   X  10 181 ? 26.620  -163.335 -13.806 1.00 98.30  ? 181 VAL   X C   1 
ATOM   42420 O  O   . VAL   X  10 181 ? 27.359  -163.620 -14.771 1.00 98.75  ? 181 VAL   X O   1 
ATOM   42421 C  CB  . VAL   X  10 181 ? 25.873  -160.945 -14.220 1.00 102.65 ? 181 VAL   X CB  1 
ATOM   42422 C  CG1 . VAL   X  10 181 ? 24.439  -161.401 -14.449 1.00 105.57 ? 181 VAL   X CG1 1 
ATOM   42423 C  CG2 . VAL   X  10 181 ? 25.899  -159.516 -13.703 1.00 104.17 ? 181 VAL   X CG2 1 
ATOM   42424 N  N   . LYS   X  10 182 ? 25.804  -164.192 -13.183 1.00 99.24  ? 182 LYS   X N   1 
ATOM   42425 C  CA  . LYS   X  10 182 ? 25.629  -165.622 -13.550 1.00 99.54  ? 182 LYS   X CA  1 
ATOM   42426 C  C   . LYS   X  10 182 ? 24.133  -165.940 -13.619 1.00 99.58  ? 182 LYS   X C   1 
ATOM   42427 O  O   . LYS   X  10 182 ? 23.375  -165.417 -12.777 1.00 97.67  ? 182 LYS   X O   1 
ATOM   42428 C  CB  . LYS   X  10 182 ? 26.349  -166.520 -12.542 1.00 96.79  ? 182 LYS   X CB  1 
ATOM   42429 C  CG  . LYS   X  10 182 ? 27.820  -166.188 -12.342 1.00 97.16  ? 182 LYS   X CG  1 
ATOM   42430 C  CD  . LYS   X  10 182 ? 28.637  -167.337 -11.809 1.00 98.44  ? 182 LYS   X CD  1 
ATOM   42431 C  CE  . LYS   X  10 182 ? 30.120  -167.036 -11.785 1.00 101.25 ? 182 LYS   X CE  1 
ATOM   42432 N  NZ  . LYS   X  10 182 ? 30.924  -168.263 -11.569 1.00 103.75 ? 182 LYS   X NZ  1 
ATOM   42433 N  N   . ILE   X  10 183 ? 23.739  -166.767 -14.592 1.00 102.55 ? 183 ILE   X N   1 
ATOM   42434 C  CA  . ILE   X  10 183 ? 22.322  -167.149 -14.861 1.00 105.24 ? 183 ILE   X CA  1 
ATOM   42435 C  C   . ILE   X  10 183 ? 22.155  -168.641 -14.567 1.00 103.25 ? 183 ILE   X C   1 
ATOM   42436 O  O   . ILE   X  10 183 ? 22.966  -169.438 -15.073 1.00 105.94 ? 183 ILE   X O   1 
ATOM   42437 C  CB  . ILE   X  10 183 ? 21.925  -166.814 -16.310 1.00 108.78 ? 183 ILE   X CB  1 
ATOM   42438 C  CG1 . ILE   X  10 183 ? 22.276  -165.368 -16.674 1.00 111.24 ? 183 ILE   X CG1 1 
ATOM   42439 C  CG2 . ILE   X  10 183 ? 20.450  -167.115 -16.541 1.00 109.17 ? 183 ILE   X CG2 1 
ATOM   42440 C  CD1 . ILE   X  10 183 ? 22.308  -165.098 -18.159 1.00 115.16 ? 183 ILE   X CD1 1 
ATOM   42441 N  N   . VAL   X  10 184 ? 21.128  -168.986 -13.788 1.00 103.93 ? 184 VAL   X N   1 
ATOM   42442 C  CA  . VAL   X  10 184 ? 20.727  -170.386 -13.467 1.00 105.29 ? 184 VAL   X CA  1 
ATOM   42443 C  C   . VAL   X  10 184 ? 19.381  -170.643 -14.145 1.00 107.24 ? 184 VAL   X C   1 
ATOM   42444 O  O   . VAL   X  10 184 ? 18.430  -169.897 -13.845 1.00 108.13 ? 184 VAL   X O   1 
ATOM   42445 C  CB  . VAL   X  10 184 ? 20.636  -170.608 -11.946 1.00 104.49 ? 184 VAL   X CB  1 
ATOM   42446 C  CG1 . VAL   X  10 184 ? 20.425  -172.076 -11.605 1.00 105.84 ? 184 VAL   X CG1 1 
ATOM   42447 C  CG2 . VAL   X  10 184 ? 21.852  -170.055 -11.217 1.00 103.04 ? 184 VAL   X CG2 1 
ATOM   42448 N  N   . ASP   X  10 185 ? 19.311  -171.643 -15.030 1.00 109.92 ? 185 ASP   X N   1 
ATOM   42449 C  CA  . ASP   X  10 185 ? 18.078  -172.006 -15.782 1.00 109.09 ? 185 ASP   X CA  1 
ATOM   42450 C  C   . ASP   X  10 185 ? 18.049  -173.522 -16.012 1.00 110.45 ? 185 ASP   X C   1 
ATOM   42451 O  O   . ASP   X  10 185 ? 18.840  -174.231 -15.357 1.00 113.34 ? 185 ASP   X O   1 
ATOM   42452 C  CB  . ASP   X  10 185 ? 17.983  -171.208 -17.087 1.00 110.78 ? 185 ASP   X CB  1 
ATOM   42453 C  CG  . ASP   X  10 185 ? 19.136  -171.434 -18.052 1.00 110.23 ? 185 ASP   X CG  1 
ATOM   42454 O  OD1 . ASP   X  10 185 ? 19.793  -172.489 -17.957 1.00 105.56 ? 185 ASP   X OD1 1 
ATOM   42455 O  OD2 . ASP   X  10 185 ? 19.370  -170.546 -18.893 1.00 112.69 ? 185 ASP   X OD2 1 
ATOM   42456 N  N   . LYS   X  10 186 ? 17.165  -173.985 -16.902 1.00 110.67 ? 186 LYS   X N   1 
ATOM   42457 C  CA  . LYS   X  10 186 ? 16.963  -175.419 -17.244 1.00 110.16 ? 186 LYS   X CA  1 
ATOM   42458 C  C   . LYS   X  10 186 ? 18.263  -176.034 -17.783 1.00 108.68 ? 186 LYS   X C   1 
ATOM   42459 O  O   . LYS   X  10 186 ? 18.443  -177.250 -17.592 1.00 109.81 ? 186 LYS   X O   1 
ATOM   42460 C  CB  . LYS   X  10 186 ? 15.817  -175.576 -18.250 1.00 113.58 ? 186 LYS   X CB  1 
ATOM   42461 C  CG  . LYS   X  10 186 ? 15.999  -174.870 -19.588 1.00 116.23 ? 186 LYS   X CG  1 
ATOM   42462 C  CD  . LYS   X  10 186 ? 14.801  -175.018 -20.505 1.00 118.04 ? 186 LYS   X CD  1 
ATOM   42463 C  CE  . LYS   X  10 186 ? 14.864  -174.122 -21.723 1.00 119.40 ? 186 LYS   X CE  1 
ATOM   42464 N  NZ  . LYS   X  10 186 ? 15.920  -174.555 -22.669 1.00 121.90 ? 186 LYS   X NZ  1 
ATOM   42465 N  N   . ASP   X  10 187 ? 19.132  -175.237 -18.417 1.00 106.72 ? 187 ASP   X N   1 
ATOM   42466 C  CA  . ASP   X  10 187 ? 20.388  -175.713 -19.062 1.00 107.13 ? 187 ASP   X CA  1 
ATOM   42467 C  C   . ASP   X  10 187 ? 21.590  -175.545 -18.124 1.00 105.59 ? 187 ASP   X C   1 
ATOM   42468 O  O   . ASP   X  10 187 ? 22.724  -175.776 -18.590 1.00 107.57 ? 187 ASP   X O   1 
ATOM   42469 C  CB  . ASP   X  10 187 ? 20.644  -174.979 -20.376 1.00 108.08 ? 187 ASP   X CB  1 
ATOM   42470 C  CG  . ASP   X  10 187 ? 19.521  -175.154 -21.379 1.00 111.99 ? 187 ASP   X CG  1 
ATOM   42471 O  OD1 . ASP   X  10 187 ? 19.143  -176.315 -21.637 1.00 113.19 ? 187 ASP   X OD1 1 
ATOM   42472 O  OD2 . ASP   X  10 187 ? 19.023  -174.128 -21.878 1.00 113.54 ? 187 ASP   X OD2 1 
ATOM   42473 N  N   . GLY   X  10 188 ? 21.361  -175.155 -16.866 1.00 105.26 ? 188 GLY   X N   1 
ATOM   42474 C  CA  . GLY   X  10 188 ? 22.399  -175.097 -15.819 1.00 103.08 ? 188 GLY   X CA  1 
ATOM   42475 C  C   . GLY   X  10 188 ? 22.877  -173.679 -15.567 1.00 102.19 ? 188 GLY   X C   1 
ATOM   42476 O  O   . GLY   X  10 188 ? 22.044  -172.755 -15.638 1.00 102.14 ? 188 GLY   X O   1 
ATOM   42477 N  N   . ILE   X  10 189 ? 24.176  -173.522 -15.288 1.00 101.65 ? 189 ILE   X N   1 
ATOM   42478 C  CA  . ILE   X  10 189 ? 24.817  -172.253 -14.829 1.00 100.93 ? 189 ILE   X CA  1 
ATOM   42479 C  C   . ILE   X  10 189 ? 25.792  -171.769 -15.906 1.00 101.27 ? 189 ILE   X C   1 
ATOM   42480 O  O   . ILE   X  10 189 ? 26.642  -172.568 -16.336 1.00 101.45 ? 189 ILE   X O   1 
ATOM   42481 C  CB  . ILE   X  10 189 ? 25.524  -172.470 -13.474 1.00 100.05 ? 189 ILE   X CB  1 
ATOM   42482 C  CG1 . ILE   X  10 189 ? 24.524  -172.830 -12.372 1.00 101.34 ? 189 ILE   X CG1 1 
ATOM   42483 C  CG2 . ILE   X  10 189 ? 26.368  -171.263 -13.089 1.00 99.72  ? 189 ILE   X CG2 1 
ATOM   42484 C  CD1 . ILE   X  10 189 ? 25.111  -173.658 -11.256 1.00 101.10 ? 189 ILE   X CD1 1 
ATOM   42485 N  N   . ARG   X  10 190 ? 25.679  -170.500 -16.307 1.00 100.97 ? 190 ARG   X N   1 
ATOM   42486 C  CA  . ARG   X  10 190 ? 26.612  -169.839 -17.257 1.00 103.67 ? 190 ARG   X CA  1 
ATOM   42487 C  C   . ARG   X  10 190 ? 26.867  -168.397 -16.803 1.00 103.15 ? 190 ARG   X C   1 
ATOM   42488 O  O   . ARG   X  10 190 ? 25.958  -167.793 -16.195 1.00 98.10  ? 190 ARG   X O   1 
ATOM   42489 C  CB  . ARG   X  10 190 ? 26.052  -169.893 -18.680 1.00 107.63 ? 190 ARG   X CB  1 
ATOM   42490 C  CG  . ARG   X  10 190 ? 24.857  -168.983 -18.920 1.00 110.74 ? 190 ARG   X CG  1 
ATOM   42491 C  CD  . ARG   X  10 190 ? 24.407  -169.048 -20.363 1.00 118.39 ? 190 ARG   X CD  1 
ATOM   42492 N  NE  . ARG   X  10 190 ? 23.367  -168.070 -20.655 1.00 122.21 ? 190 ARG   X NE  1 
ATOM   42493 C  CZ  . ARG   X  10 190 ? 22.078  -168.203 -20.342 1.00 124.85 ? 190 ARG   X CZ  1 
ATOM   42494 N  NH1 . ARG   X  10 190 ? 21.639  -169.284 -19.714 1.00 128.70 ? 190 ARG   X NH1 1 
ATOM   42495 N  NH2 . ARG   X  10 190 ? 21.225  -167.244 -20.660 1.00 124.09 ? 190 ARG   X NH2 1 
ATOM   42496 N  N   . GLN   X  10 191 ? 28.060  -167.875 -17.104 1.00 106.14 ? 191 GLN   X N   1 
ATOM   42497 C  CA  . GLN   X  10 191 ? 28.536  -166.536 -16.666 1.00 111.78 ? 191 GLN   X CA  1 
ATOM   42498 C  C   . GLN   X  10 191 ? 28.447  -165.546 -17.833 1.00 115.63 ? 191 GLN   X C   1 
ATOM   42499 O  O   . GLN   X  10 191 ? 28.932  -165.879 -18.931 1.00 121.24 ? 191 GLN   X O   1 
ATOM   42500 C  CB  . GLN   X  10 191 ? 29.976  -166.623 -16.157 1.00 113.45 ? 191 GLN   X CB  1 
ATOM   42501 C  CG  . GLN   X  10 191 ? 30.490  -165.316 -15.565 1.00 114.88 ? 191 GLN   X CG  1 
ATOM   42502 C  CD  . GLN   X  10 191 ? 31.943  -165.356 -15.156 1.00 115.20 ? 191 GLN   X CD  1 
ATOM   42503 O  OE1 . GLN   X  10 191 ? 32.683  -164.397 -15.362 1.00 118.76 ? 191 GLN   X OE1 1 
ATOM   42504 N  NE2 . GLN   X  10 191 ? 32.370  -166.463 -14.565 1.00 117.08 ? 191 GLN   X NE2 1 
ATOM   42505 N  N   . VAL   X  10 192 ? 27.863  -164.370 -17.586 1.00 117.03 ? 192 VAL   X N   1 
ATOM   42506 C  CA  . VAL   X  10 192 ? 27.885  -163.203 -18.518 1.00 118.17 ? 192 VAL   X CA  1 
ATOM   42507 C  C   . VAL   X  10 192 ? 29.256  -162.534 -18.379 1.00 127.94 ? 192 VAL   X C   1 
ATOM   42508 O  O   . VAL   X  10 192 ? 29.577  -162.093 -17.258 1.00 130.56 ? 192 VAL   X O   1 
ATOM   42509 C  CB  . VAL   X  10 192 ? 26.747  -162.210 -18.219 1.00 112.24 ? 192 VAL   X CB  1 
ATOM   42510 C  CG1 . VAL   X  10 192 ? 26.792  -161.013 -19.156 1.00 113.53 ? 192 VAL   X CG1 1 
ATOM   42511 C  CG2 . VAL   X  10 192 ? 25.382  -162.877 -18.270 1.00 108.39 ? 192 VAL   X CG2 1 
ATOM   42512 N  N   . ASP   X  10 193 ? 30.023  -162.463 -19.473 1.00 141.45 ? 193 ASP   X N   1 
ATOM   42513 C  CA  . ASP   X  10 193 ? 31.440  -162.002 -19.477 1.00 150.78 ? 193 ASP   X CA  1 
ATOM   42514 C  C   . ASP   X  10 193 ? 31.516  -160.482 -19.692 1.00 157.20 ? 193 ASP   X C   1 
ATOM   42515 O  O   . ASP   X  10 193 ? 32.522  -159.887 -19.252 1.00 164.06 ? 193 ASP   X O   1 
ATOM   42516 C  CB  . ASP   X  10 193 ? 32.283  -162.758 -20.512 1.00 156.87 ? 193 ASP   X CB  1 
ATOM   42517 C  CG  . ASP   X  10 193 ? 31.649  -162.892 -21.887 1.00 158.00 ? 193 ASP   X CG  1 
ATOM   42518 O  OD1 . ASP   X  10 193 ? 30.633  -162.212 -22.138 1.00 161.83 ? 193 ASP   X OD1 1 
ATOM   42519 O  OD2 . ASP   X  10 193 ? 32.175  -163.681 -22.694 1.00 163.25 ? 193 ASP   X OD2 1 
ATOM   42520 N  N   . ASP   X  10 194 ? 30.505  -159.879 -20.329 1.00 163.73 ? 194 ASP   X N   1 
ATOM   42521 C  CA  . ASP   X  10 194 ? 30.476  -158.426 -20.663 1.00 163.67 ? 194 ASP   X CA  1 
ATOM   42522 C  C   . ASP   X  10 194 ? 29.355  -157.737 -19.873 1.00 155.51 ? 194 ASP   X C   1 
ATOM   42523 O  O   . ASP   X  10 194 ? 28.222  -157.661 -20.388 1.00 158.07 ? 194 ASP   X O   1 
ATOM   42524 C  CB  . ASP   X  10 194 ? 30.352  -158.197 -22.175 1.00 173.71 ? 194 ASP   X CB  1 
ATOM   42525 C  CG  . ASP   X  10 194 ? 29.403  -159.142 -22.896 1.00 177.93 ? 194 ASP   X CG  1 
ATOM   42526 O  OD1 . ASP   X  10 194 ? 28.399  -159.556 -22.282 1.00 185.03 ? 194 ASP   X OD1 1 
ATOM   42527 O  OD2 . ASP   X  10 194 ? 29.680  -159.461 -24.069 1.00 182.97 ? 194 ASP   X OD2 1 
ATOM   42528 N  N   . PHE   X  10 195 ? 29.668  -157.249 -18.669 1.00 143.87 ? 195 PHE   X N   1 
ATOM   42529 C  CA  . PHE   X  10 195 ? 28.743  -156.459 -17.813 1.00 138.70 ? 195 PHE   X CA  1 
ATOM   42530 C  C   . PHE   X  10 195 ? 29.477  -155.225 -17.274 1.00 137.90 ? 195 PHE   X C   1 
ATOM   42531 O  O   . PHE   X  10 195 ? 29.270  -154.109 -17.759 1.00 129.57 ? 195 PHE   X O   1 
ATOM   42532 C  CB  . PHE   X  10 195 ? 28.172  -157.328 -16.690 1.00 137.49 ? 195 PHE   X CB  1 
ATOM   42533 C  CG  . PHE   X  10 195 ? 26.807  -156.897 -16.215 1.00 133.89 ? 195 PHE   X CG  1 
ATOM   42534 C  CD1 . PHE   X  10 195 ? 26.670  -155.952 -15.209 1.00 132.76 ? 195 PHE   X CD1 1 
ATOM   42535 C  CD2 . PHE   X  10 195 ? 25.658  -157.422 -16.788 1.00 132.18 ? 195 PHE   X CD2 1 
ATOM   42536 C  CE1 . PHE   X  10 195 ? 25.413  -155.551 -14.780 1.00 129.38 ? 195 PHE   X CE1 1 
ATOM   42537 C  CE2 . PHE   X  10 195 ? 24.403  -157.019 -16.357 1.00 129.72 ? 195 PHE   X CE2 1 
ATOM   42538 C  CZ  . PHE   X  10 195 ? 24.282  -156.085 -15.354 1.00 128.97 ? 195 PHE   X CZ  1 
ATOM   42539 N  N   . THR   Y  11 1   ? 57.646  -154.089 4.533   1.00 97.67  ? 2   THR   Y N   1 
ATOM   42540 C  CA  . THR   Y  11 1   ? 57.149  -153.927 3.146   1.00 97.66  ? 2   THR   Y CA  1 
ATOM   42541 C  C   . THR   Y  11 1   ? 57.503  -155.162 2.319   1.00 98.14  ? 2   THR   Y C   1 
ATOM   42542 O  O   . THR   Y  11 1   ? 58.702  -155.465 2.193   1.00 93.94  ? 2   THR   Y O   1 
ATOM   42543 C  CB  . THR   Y  11 1   ? 57.725  -152.662 2.512   1.00 99.05  ? 2   THR   Y CB  1 
ATOM   42544 O  OG1 . THR   Y  11 1   ? 57.216  -151.583 3.292   1.00 98.54  ? 2   THR   Y OG1 1 
ATOM   42545 C  CG2 . THR   Y  11 1   ? 57.323  -152.505 1.064   1.00 97.98  ? 2   THR   Y CG2 1 
ATOM   42546 N  N   . THR   Y  11 2   ? 56.481  -155.833 1.783   1.00 96.65  ? 3   THR   Y N   1 
ATOM   42547 C  CA  . THR   Y  11 2   ? 56.693  -157.049 0.949   1.00 99.69  ? 3   THR   Y CA  1 
ATOM   42548 C  C   . THR   Y  11 2   ? 55.782  -156.986 -0.279  1.00 96.91  ? 3   THR   Y C   1 
ATOM   42549 O  O   . THR   Y  11 2   ? 54.635  -156.522 -0.133  1.00 95.19  ? 3   THR   Y O   1 
ATOM   42550 C  CB  . THR   Y  11 2   ? 56.388  -158.346 1.713   1.00 98.83  ? 3   THR   Y CB  1 
ATOM   42551 O  OG1 . THR   Y  11 2   ? 54.977  -158.460 1.905   1.00 102.53 ? 3   THR   Y OG1 1 
ATOM   42552 C  CG2 . THR   Y  11 2   ? 57.082  -158.425 3.054   1.00 100.33 ? 3   THR   Y CG2 1 
ATOM   42553 N  N   . LEU   Y  11 3   ? 56.263  -157.458 -1.431  1.00 99.75  ? 4   LEU   Y N   1 
ATOM   42554 C  CA  . LEU   Y  11 3   ? 55.425  -157.627 -2.647  1.00 104.49 ? 4   LEU   Y CA  1 
ATOM   42555 C  C   . LEU   Y  11 3   ? 55.950  -158.790 -3.493  1.00 104.08 ? 4   LEU   Y C   1 
ATOM   42556 O  O   . LEU   Y  11 3   ? 57.101  -159.229 -3.290  1.00 102.45 ? 4   LEU   Y O   1 
ATOM   42557 C  CB  . LEU   Y  11 3   ? 55.329  -156.314 -3.441  1.00 106.17 ? 4   LEU   Y CB  1 
ATOM   42558 C  CG  . LEU   Y  11 3   ? 56.592  -155.721 -4.081  1.00 109.17 ? 4   LEU   Y CG  1 
ATOM   42559 C  CD1 . LEU   Y  11 3   ? 57.592  -155.276 -3.036  1.00 110.73 ? 4   LEU   Y CD1 1 
ATOM   42560 C  CD2 . LEU   Y  11 3   ? 57.254  -156.655 -5.083  1.00 109.84 ? 4   LEU   Y CD2 1 
ATOM   42561 N  N   . ALA   Y  11 4   ? 55.084  -159.290 -4.370  1.00 104.47 ? 5   ALA   Y N   1 
ATOM   42562 C  CA  . ALA   Y  11 4   ? 55.382  -160.298 -5.409  1.00 106.55 ? 5   ALA   Y CA  1 
ATOM   42563 C  C   . ALA   Y  11 4   ? 54.414  -160.069 -6.569  1.00 106.69 ? 5   ALA   Y C   1 
ATOM   42564 O  O   . ALA   Y  11 4   ? 53.248  -159.704 -6.302  1.00 100.47 ? 5   ALA   Y O   1 
ATOM   42565 C  CB  . ALA   Y  11 4   ? 55.251  -161.687 -4.840  1.00 108.31 ? 5   ALA   Y CB  1 
ATOM   42566 N  N   . PHE   Y  11 5   ? 54.882  -160.249 -7.803  1.00 109.91 ? 6   PHE   Y N   1 
ATOM   42567 C  CA  . PHE   Y  11 5   ? 54.052  -160.069 -9.019  1.00 112.64 ? 6   PHE   Y CA  1 
ATOM   42568 C  C   . PHE   Y  11 5   ? 54.455  -161.087 -10.087 1.00 114.59 ? 6   PHE   Y C   1 
ATOM   42569 O  O   . PHE   Y  11 5   ? 55.584  -161.616 -10.048 1.00 114.25 ? 6   PHE   Y O   1 
ATOM   42570 C  CB  . PHE   Y  11 5   ? 54.137  -158.627 -9.526  1.00 113.60 ? 6   PHE   Y CB  1 
ATOM   42571 C  CG  . PHE   Y  11 5   ? 55.494  -158.197 -10.026 1.00 117.23 ? 6   PHE   Y CG  1 
ATOM   42572 C  CD1 . PHE   Y  11 5   ? 55.995  -158.678 -11.227 1.00 120.61 ? 6   PHE   Y CD1 1 
ATOM   42573 C  CD2 . PHE   Y  11 5   ? 56.262  -157.293 -9.307  1.00 114.10 ? 6   PHE   Y CD2 1 
ATOM   42574 C  CE1 . PHE   Y  11 5   ? 57.239  -158.278 -11.689 1.00 121.96 ? 6   PHE   Y CE1 1 
ATOM   42575 C  CE2 . PHE   Y  11 5   ? 57.505  -156.892 -9.772  1.00 116.41 ? 6   PHE   Y CE2 1 
ATOM   42576 C  CZ  . PHE   Y  11 5   ? 57.990  -157.385 -10.962 1.00 119.58 ? 6   PHE   Y CZ  1 
ATOM   42577 N  N   . ARG   Y  11 6   ? 53.533  -161.318 -11.022 1.00 118.66 ? 7   ARG   Y N   1 
ATOM   42578 C  CA  . ARG   Y  11 6   ? 53.642  -162.288 -12.141 1.00 122.28 ? 7   ARG   Y CA  1 
ATOM   42579 C  C   . ARG   Y  11 6   ? 53.849  -161.527 -13.453 1.00 125.52 ? 7   ARG   Y C   1 
ATOM   42580 O  O   . ARG   Y  11 6   ? 53.262  -160.433 -13.604 1.00 121.34 ? 7   ARG   Y O   1 
ATOM   42581 C  CB  . ARG   Y  11 6   ? 52.355  -163.110 -12.233 1.00 121.99 ? 7   ARG   Y CB  1 
ATOM   42582 C  CG  . ARG   Y  11 6   ? 52.501  -164.587 -11.909 1.00 120.94 ? 7   ARG   Y CG  1 
ATOM   42583 C  CD  . ARG   Y  11 6   ? 51.118  -165.206 -11.847 1.00 119.74 ? 7   ARG   Y CD  1 
ATOM   42584 N  NE  . ARG   Y  11 6   ? 50.351  -164.899 -13.053 1.00 119.82 ? 7   ARG   Y NE  1 
ATOM   42585 C  CZ  . ARG   Y  11 6   ? 49.963  -165.777 -13.974 1.00 122.15 ? 7   ARG   Y CZ  1 
ATOM   42586 N  NH1 . ARG   Y  11 6   ? 50.234  -167.065 -13.842 1.00 122.50 ? 7   ARG   Y NH1 1 
ATOM   42587 N  NH2 . ARG   Y  11 6   ? 49.285  -165.360 -15.028 1.00 124.63 ? 7   ARG   Y NH2 1 
ATOM   42588 N  N   . PHE   Y  11 7   ? 54.631  -162.098 -14.369 1.00 128.09 ? 8   PHE   Y N   1 
ATOM   42589 C  CA  . PHE   Y  11 7   ? 54.867  -161.547 -15.728 1.00 129.08 ? 8   PHE   Y CA  1 
ATOM   42590 C  C   . PHE   Y  11 7   ? 55.321  -162.680 -16.656 1.00 131.45 ? 8   PHE   Y C   1 
ATOM   42591 O  O   . PHE   Y  11 7   ? 55.329  -163.853 -16.223 1.00 127.85 ? 8   PHE   Y O   1 
ATOM   42592 C  CB  . PHE   Y  11 7   ? 55.844  -160.368 -15.654 1.00 131.68 ? 8   PHE   Y CB  1 
ATOM   42593 C  CG  . PHE   Y  11 7   ? 57.291  -160.721 -15.416 1.00 132.23 ? 8   PHE   Y CG  1 
ATOM   42594 C  CD1 . PHE   Y  11 7   ? 57.696  -161.341 -14.242 1.00 127.66 ? 8   PHE   Y CD1 1 
ATOM   42595 C  CD2 . PHE   Y  11 7   ? 58.259  -160.392 -16.354 1.00 135.71 ? 8   PHE   Y CD2 1 
ATOM   42596 C  CE1 . PHE   Y  11 7   ? 59.031  -161.650 -14.027 1.00 128.38 ? 8   PHE   Y CE1 1 
ATOM   42597 C  CE2 . PHE   Y  11 7   ? 59.594  -160.701 -16.137 1.00 136.04 ? 8   PHE   Y CE2 1 
ATOM   42598 C  CZ  . PHE   Y  11 7   ? 59.977  -161.330 -14.975 1.00 132.57 ? 8   PHE   Y CZ  1 
ATOM   42599 N  N   . GLN   Y  11 8   ? 55.647  -162.331 -17.905 1.00 134.64 ? 9   GLN   Y N   1 
ATOM   42600 C  CA  . GLN   Y  11 8   ? 56.140  -163.263 -18.955 1.00 133.09 ? 9   GLN   Y CA  1 
ATOM   42601 C  C   . GLN   Y  11 8   ? 57.324  -164.072 -18.407 1.00 132.43 ? 9   GLN   Y C   1 
ATOM   42602 O  O   . GLN   Y  11 8   ? 57.291  -165.312 -18.523 1.00 128.54 ? 9   GLN   Y O   1 
ATOM   42603 C  CB  . GLN   Y  11 8   ? 56.497  -162.474 -20.220 1.00 138.82 ? 9   GLN   Y CB  1 
ATOM   42604 C  CG  . GLN   Y  11 8   ? 57.689  -163.019 -20.998 1.00 142.15 ? 9   GLN   Y CG  1 
ATOM   42605 C  CD  . GLN   Y  11 8   ? 58.972  -162.290 -20.674 1.00 144.21 ? 9   GLN   Y CD  1 
ATOM   42606 O  OE1 . GLN   Y  11 8   ? 59.936  -162.876 -20.186 1.00 138.96 ? 9   GLN   Y OE1 1 
ATOM   42607 N  NE2 . GLN   Y  11 8   ? 58.991  -160.993 -20.942 1.00 146.38 ? 9   GLN   Y NE2 1 
ATOM   42608 N  N   . GLY   Y  11 9   ? 58.321  -163.386 -17.837 1.00 131.25 ? 10  GLY   Y N   1 
ATOM   42609 C  CA  . GLY   Y  11 9   ? 59.563  -163.978 -17.299 1.00 128.17 ? 10  GLY   Y CA  1 
ATOM   42610 C  C   . GLY   Y  11 9   ? 59.311  -164.939 -16.147 1.00 122.36 ? 10  GLY   Y C   1 
ATOM   42611 O  O   . GLY   Y  11 9   ? 60.143  -165.843 -15.950 1.00 120.54 ? 10  GLY   Y O   1 
ATOM   42612 N  N   . GLY   Y  11 10  ? 58.223  -164.744 -15.395 1.00 119.32 ? 11  GLY   Y N   1 
ATOM   42613 C  CA  . GLY   Y  11 10  ? 57.817  -165.633 -14.290 1.00 118.78 ? 11  GLY   Y CA  1 
ATOM   42614 C  C   . GLY   Y  11 10  ? 57.230  -164.852 -13.129 1.00 117.23 ? 11  GLY   Y C   1 
ATOM   42615 O  O   . GLY   Y  11 10  ? 56.262  -164.101 -13.364 1.00 120.74 ? 11  GLY   Y O   1 
ATOM   42616 N  N   . ILE   Y  11 11  ? 57.787  -165.027 -11.925 1.00 116.52 ? 12  ILE   Y N   1 
ATOM   42617 C  CA  . ILE   Y  11 11  ? 57.371  -164.308 -10.682 1.00 113.75 ? 12  ILE   Y CA  1 
ATOM   42618 C  C   . ILE   Y  11 11  ? 58.597  -163.606 -10.092 1.00 114.36 ? 12  ILE   Y C   1 
ATOM   42619 O  O   . ILE   Y  11 11  ? 59.665  -164.242 -10.016 1.00 109.20 ? 12  ILE   Y O   1 
ATOM   42620 C  CB  . ILE   Y  11 11  ? 56.721  -165.265 -9.661  1.00 112.96 ? 12  ILE   Y CB  1 
ATOM   42621 C  CG1 . ILE   Y  11 11  ? 55.661  -166.154 -10.314 1.00 114.74 ? 12  ILE   Y CG1 1 
ATOM   42622 C  CG2 . ILE   Y  11 11  ? 56.154  -164.495 -8.477  1.00 109.42 ? 12  ILE   Y CG2 1 
ATOM   42623 C  CD1 . ILE   Y  11 11  ? 55.257  -167.337 -9.476  1.00 115.21 ? 12  ILE   Y CD1 1 
ATOM   42624 N  N   . ILE   Y  11 12  ? 58.429  -162.343 -9.692  1.00 113.57 ? 13  ILE   Y N   1 
ATOM   42625 C  CA  . ILE   Y  11 12  ? 59.460  -161.522 -8.992  1.00 111.91 ? 13  ILE   Y CA  1 
ATOM   42626 C  C   . ILE   Y  11 12  ? 58.989  -161.297 -7.553  1.00 107.35 ? 13  ILE   Y C   1 
ATOM   42627 O  O   . ILE   Y  11 12  ? 57.806  -160.948 -7.371  1.00 102.85 ? 13  ILE   Y O   1 
ATOM   42628 C  CB  . ILE   Y  11 12  ? 59.711  -160.200 -9.746  1.00 114.45 ? 13  ILE   Y CB  1 
ATOM   42629 C  CG1 . ILE   Y  11 12  ? 60.744  -160.379 -10.862 1.00 119.37 ? 13  ILE   Y CG1 1 
ATOM   42630 C  CG2 . ILE   Y  11 12  ? 60.103  -159.080 -8.790  1.00 113.19 ? 13  ILE   Y CG2 1 
ATOM   42631 C  CD1 . ILE   Y  11 12  ? 62.162  -160.535 -10.370 1.00 121.17 ? 13  ILE   Y CD1 1 
ATOM   42632 N  N   . VAL   Y  11 13  ? 59.884  -161.493 -6.581  1.00 105.23 ? 14  VAL   Y N   1 
ATOM   42633 C  CA  . VAL   Y  11 13  ? 59.597  -161.326 -5.126  1.00 103.79 ? 14  VAL   Y CA  1 
ATOM   42634 C  C   . VAL   Y  11 13  ? 60.627  -160.362 -4.533  1.00 102.49 ? 14  VAL   Y C   1 
ATOM   42635 O  O   . VAL   Y  11 13  ? 61.836  -160.661 -4.606  1.00 103.42 ? 14  VAL   Y O   1 
ATOM   42636 C  CB  . VAL   Y  11 13  ? 59.599  -162.676 -4.386  1.00 101.87 ? 14  VAL   Y CB  1 
ATOM   42637 C  CG1 . VAL   Y  11 13  ? 59.331  -162.505 -2.899  1.00 100.98 ? 14  VAL   Y CG1 1 
ATOM   42638 C  CG2 . VAL   Y  11 13  ? 58.605  -163.650 -4.998  1.00 103.57 ? 14  VAL   Y CG2 1 
ATOM   42639 N  N   . ALA   Y  11 14  ? 60.144  -159.255 -3.965  1.00 100.93 ? 15  ALA   Y N   1 
ATOM   42640 C  CA  . ALA   Y  11 14  ? 60.947  -158.211 -3.291  1.00 99.66  ? 15  ALA   Y CA  1 
ATOM   42641 C  C   . ALA   Y  11 14  ? 60.364  -157.960 -1.898  1.00 94.87  ? 15  ALA   Y C   1 
ATOM   42642 O  O   . ALA   Y  11 14  ? 59.135  -157.804 -1.785  1.00 92.76  ? 15  ALA   Y O   1 
ATOM   42643 C  CB  . ALA   Y  11 14  ? 60.958  -156.954 -4.122  1.00 100.67 ? 15  ALA   Y CB  1 
ATOM   42644 N  N   . VAL   Y  11 15  ? 61.221  -157.959 -0.877  1.00 94.00  ? 16  VAL   Y N   1 
ATOM   42645 C  CA  . VAL   Y  11 15  ? 60.851  -157.658 0.537   1.00 94.45  ? 16  VAL   Y CA  1 
ATOM   42646 C  C   . VAL   Y  11 15  ? 61.861  -156.635 1.066   1.00 93.18  ? 16  VAL   Y C   1 
ATOM   42647 O  O   . VAL   Y  11 15  ? 62.955  -156.532 0.475   1.00 95.17  ? 16  VAL   Y O   1 
ATOM   42648 C  CB  . VAL   Y  11 15  ? 60.822  -158.935 1.403   1.00 92.84  ? 16  VAL   Y CB  1 
ATOM   42649 C  CG1 . VAL   Y  11 15  ? 59.985  -160.032 0.763   1.00 93.01  ? 16  VAL   Y CG1 1 
ATOM   42650 C  CG2 . VAL   Y  11 15  ? 62.221  -159.452 1.718   1.00 94.05  ? 16  VAL   Y CG2 1 
ATOM   42651 N  N   . ASP   Y  11 16  ? 61.507  -155.910 2.128   1.00 91.17  ? 17  ASP   Y N   1 
ATOM   42652 C  CA  . ASP   Y  11 16  ? 62.463  -155.066 2.891   1.00 95.02  ? 17  ASP   Y CA  1 
ATOM   42653 C  C   . ASP   Y  11 16  ? 63.073  -155.951 3.985   1.00 96.59  ? 17  ASP   Y C   1 
ATOM   42654 O  O   . ASP   Y  11 16  ? 62.731  -157.150 4.017   1.00 99.97  ? 17  ASP   Y O   1 
ATOM   42655 C  CB  . ASP   Y  11 16  ? 61.785  -153.807 3.435   1.00 95.08  ? 17  ASP   Y CB  1 
ATOM   42656 C  CG  . ASP   Y  11 16  ? 61.052  -154.036 4.742   1.00 93.88  ? 17  ASP   Y CG  1 
ATOM   42657 O  OD1 . ASP   Y  11 16  ? 60.198  -154.942 4.775   1.00 98.17  ? 17  ASP   Y OD1 1 
ATOM   42658 O  OD2 . ASP   Y  11 16  ? 61.360  -153.330 5.720   1.00 90.88  ? 17  ASP   Y OD2 1 
ATOM   42659 N  N   . SER   Y  11 17  ? 63.937  -155.402 4.844   1.00 95.41  ? 18  SER   Y N   1 
ATOM   42660 C  CA  . SER   Y  11 17  ? 64.657  -156.180 5.887   1.00 96.01  ? 18  SER   Y CA  1 
ATOM   42661 C  C   . SER   Y  11 17  ? 64.633  -155.462 7.240   1.00 94.95  ? 18  SER   Y C   1 
ATOM   42662 O  O   . SER   Y  11 17  ? 65.647  -155.552 7.951   1.00 95.55  ? 18  SER   Y O   1 
ATOM   42663 C  CB  . SER   Y  11 17  ? 66.077  -156.461 5.458   1.00 96.82  ? 18  SER   Y CB  1 
ATOM   42664 O  OG  . SER   Y  11 17  ? 66.886  -155.301 5.596   1.00 95.09  ? 18  SER   Y OG  1 
ATOM   42665 N  N   . ARG   Y  11 18  ? 63.531  -154.800 7.607   1.00 95.88  ? 19  ARG   Y N   1 
ATOM   42666 C  CA  . ARG   Y  11 18  ? 63.455  -154.049 8.890   1.00 97.47  ? 19  ARG   Y CA  1 
ATOM   42667 C  C   . ARG   Y  11 18  ? 62.378  -154.623 9.812   1.00 95.68  ? 19  ARG   Y C   1 
ATOM   42668 O  O   . ARG   Y  11 18  ? 61.211  -154.723 9.382   1.00 89.14  ? 19  ARG   Y O   1 
ATOM   42669 C  CB  . ARG   Y  11 18  ? 63.162  -152.565 8.673   1.00 99.29  ? 19  ARG   Y CB  1 
ATOM   42670 C  CG  . ARG   Y  11 18  ? 63.110  -151.781 9.977   1.00 103.14 ? 19  ARG   Y CG  1 
ATOM   42671 C  CD  . ARG   Y  11 18  ? 62.790  -150.319 9.760   1.00 104.05 ? 19  ARG   Y CD  1 
ATOM   42672 N  NE  . ARG   Y  11 18  ? 63.996  -149.512 9.642   1.00 105.43 ? 19  ARG   Y NE  1 
ATOM   42673 C  CZ  . ARG   Y  11 18  ? 64.021  -148.252 9.224   1.00 107.83 ? 19  ARG   Y CZ  1 
ATOM   42674 N  NH1 . ARG   Y  11 18  ? 62.899  -147.643 8.876   1.00 109.40 ? 19  ARG   Y NH1 1 
ATOM   42675 N  NH2 . ARG   Y  11 18  ? 65.171  -147.604 9.152   1.00 107.53 ? 19  ARG   Y NH2 1 
ATOM   42676 N  N   . ALA   Y  11 19  ? 62.776  -154.918 11.053  1.00 100.29 ? 20  ALA   Y N   1 
ATOM   42677 C  CA  . ALA   Y  11 19  ? 61.911  -155.357 12.170  1.00 102.15 ? 20  ALA   Y CA  1 
ATOM   42678 C  C   . ALA   Y  11 19  ? 61.842  -154.235 13.206  1.00 101.37 ? 20  ALA   Y C   1 
ATOM   42679 O  O   . ALA   Y  11 19  ? 62.894  -153.626 13.492  1.00 95.76  ? 20  ALA   Y O   1 
ATOM   42680 C  CB  . ALA   Y  11 19  ? 62.452  -156.626 12.779  1.00 105.08 ? 20  ALA   Y CB  1 
ATOM   42681 N  N   . THR   Y  11 20  ? 60.646  -153.980 13.740  1.00 105.21 ? 21  THR   Y N   1 
ATOM   42682 C  CA  . THR   Y  11 20  ? 60.381  -152.912 14.735  1.00 108.12 ? 21  THR   Y CA  1 
ATOM   42683 C  C   . THR   Y  11 20  ? 59.592  -153.477 15.917  1.00 113.95 ? 21  THR   Y C   1 
ATOM   42684 O  O   . THR   Y  11 20  ? 58.679  -154.296 15.685  1.00 113.94 ? 21  THR   Y O   1 
ATOM   42685 C  CB  . THR   Y  11 20  ? 59.614  -151.745 14.103  1.00 108.41 ? 21  THR   Y CB  1 
ATOM   42686 O  OG1 . THR   Y  11 20  ? 58.349  -152.224 13.647  1.00 106.06 ? 21  THR   Y OG1 1 
ATOM   42687 C  CG2 . THR   Y  11 20  ? 60.365  -151.116 12.953  1.00 107.04 ? 21  THR   Y CG2 1 
ATOM   42688 N  N   . ALA   Y  11 21  ? 59.946  -153.042 17.129  1.00 123.61 ? 22  ALA   Y N   1 
ATOM   42689 C  CA  . ALA   Y  11 21  ? 59.172  -153.238 18.376  1.00 123.68 ? 22  ALA   Y CA  1 
ATOM   42690 C  C   . ALA   Y  11 21  ? 58.717  -151.861 18.874  1.00 124.95 ? 22  ALA   Y C   1 
ATOM   42691 O  O   . ALA   Y  11 21  ? 59.544  -151.134 19.462  1.00 115.17 ? 22  ALA   Y O   1 
ATOM   42692 C  CB  . ALA   Y  11 21  ? 60.005  -153.972 19.398  1.00 128.70 ? 22  ALA   Y CB  1 
ATOM   42693 N  N   . GLY   Y  11 22  ? 57.453  -151.511 18.618  1.00 123.24 ? 23  GLY   Y N   1 
ATOM   42694 C  CA  . GLY   Y  11 22  ? 56.930  -150.141 18.778  1.00 123.23 ? 23  GLY   Y CA  1 
ATOM   42695 C  C   . GLY   Y  11 22  ? 57.573  -149.203 17.769  1.00 126.34 ? 23  GLY   Y C   1 
ATOM   42696 O  O   . GLY   Y  11 22  ? 57.467  -149.486 16.558  1.00 127.41 ? 23  GLY   Y O   1 
ATOM   42697 N  N   . ASN   Y  11 23  ? 58.239  -148.145 18.248  1.00 123.70 ? 24  ASN   Y N   1 
ATOM   42698 C  CA  . ASN   Y  11 23  ? 58.963  -147.144 17.415  1.00 123.70 ? 24  ASN   Y CA  1 
ATOM   42699 C  C   . ASN   Y  11 23  ? 60.476  -147.369 17.522  1.00 116.62 ? 24  ASN   Y C   1 
ATOM   42700 O  O   . ASN   Y  11 23  ? 61.243  -146.495 17.066  1.00 111.79 ? 24  ASN   Y O   1 
ATOM   42701 C  CB  . ASN   Y  11 23  ? 58.595  -145.715 17.818  1.00 128.41 ? 24  ASN   Y CB  1 
ATOM   42702 C  CG  . ASN   Y  11 23  ? 57.153  -145.378 17.503  1.00 133.63 ? 24  ASN   Y CG  1 
ATOM   42703 O  OD1 . ASN   Y  11 23  ? 56.706  -145.558 16.372  1.00 132.03 ? 24  ASN   Y OD1 1 
ATOM   42704 N  ND2 . ASN   Y  11 23  ? 56.419  -144.889 18.490  1.00 136.77 ? 24  ASN   Y ND2 1 
ATOM   42705 N  N   . TRP   Y  11 24  ? 60.882  -148.500 18.102  1.00 114.89 ? 25  TRP   Y N   1 
ATOM   42706 C  CA  . TRP   Y  11 24  ? 62.297  -148.935 18.223  1.00 110.92 ? 25  TRP   Y CA  1 
ATOM   42707 C  C   . TRP   Y  11 24  ? 62.619  -149.890 17.070  1.00 110.44 ? 25  TRP   Y C   1 
ATOM   42708 O  O   . TRP   Y  11 24  ? 61.840  -150.847 16.862  1.00 110.98 ? 25  TRP   Y O   1 
ATOM   42709 C  CB  . TRP   Y  11 24  ? 62.530  -149.567 19.602  1.00 109.20 ? 25  TRP   Y CB  1 
ATOM   42710 C  CG  . TRP   Y  11 24  ? 63.611  -150.601 19.646  1.00 109.11 ? 25  TRP   Y CG  1 
ATOM   42711 C  CD1 . TRP   Y  11 24  ? 63.471  -151.951 19.506  1.00 108.84 ? 25  TRP   Y CD1 1 
ATOM   42712 C  CD2 . TRP   Y  11 24  ? 65.011  -150.365 19.865  1.00 107.53 ? 25  TRP   Y CD2 1 
ATOM   42713 N  NE1 . TRP   Y  11 24  ? 64.686  -152.570 19.614  1.00 108.02 ? 25  TRP   Y NE1 1 
ATOM   42714 C  CE2 . TRP   Y  11 24  ? 65.650  -151.623 19.836  1.00 108.41 ? 25  TRP   Y CE2 1 
ATOM   42715 C  CE3 . TRP   Y  11 24  ? 65.780  -149.218 20.078  1.00 107.08 ? 25  TRP   Y CE3 1 
ATOM   42716 C  CZ2 . TRP   Y  11 24  ? 67.024  -151.760 20.012  1.00 108.42 ? 25  TRP   Y CZ2 1 
ATOM   42717 C  CZ3 . TRP   Y  11 24  ? 67.138  -149.355 20.250  1.00 109.58 ? 25  TRP   Y CZ3 1 
ATOM   42718 C  CH2 . TRP   Y  11 24  ? 67.749  -150.610 20.217  1.00 110.34 ? 25  TRP   Y CH2 1 
ATOM   42719 N  N   . VAL   Y  11 25  ? 63.703  -149.617 16.335  1.00 108.91 ? 26  VAL   Y N   1 
ATOM   42720 C  CA  . VAL   Y  11 25  ? 64.216  -150.486 15.235  1.00 108.99 ? 26  VAL   Y CA  1 
ATOM   42721 C  C   . VAL   Y  11 25  ? 65.018  -151.620 15.880  1.00 105.73 ? 26  VAL   Y C   1 
ATOM   42722 O  O   . VAL   Y  11 25  ? 66.160  -151.366 16.315  1.00 106.56 ? 26  VAL   Y O   1 
ATOM   42723 C  CB  . VAL   Y  11 25  ? 65.059  -149.693 14.216  1.00 108.55 ? 26  VAL   Y CB  1 
ATOM   42724 C  CG1 . VAL   Y  11 25  ? 65.659  -150.595 13.146  1.00 111.64 ? 26  VAL   Y CG1 1 
ATOM   42725 C  CG2 . VAL   Y  11 25  ? 64.250  -148.582 13.568  1.00 108.43 ? 26  VAL   Y CG2 1 
ATOM   42726 N  N   . ALA   Y  11 26  ? 64.425  -152.814 15.954  1.00 106.36 ? 27  ALA   Y N   1 
ATOM   42727 C  CA  . ALA   Y  11 26  ? 65.040  -154.022 16.546  1.00 105.83 ? 27  ALA   Y CA  1 
ATOM   42728 C  C   . ALA   Y  11 26  ? 66.170  -154.508 15.632  1.00 104.51 ? 27  ALA   Y C   1 
ATOM   42729 O  O   . ALA   Y  11 26  ? 67.300  -154.689 16.131  1.00 100.17 ? 27  ALA   Y O   1 
ATOM   42730 C  CB  . ALA   Y  11 26  ? 63.991  -155.086 16.763  1.00 104.86 ? 27  ALA   Y CB  1 
ATOM   42731 N  N   . SER   Y  11 27  ? 65.879  -154.688 14.341  1.00 105.62 ? 28  SER   Y N   1 
ATOM   42732 C  CA  . SER   Y  11 27  ? 66.818  -155.263 13.345  1.00 108.57 ? 28  SER   Y CA  1 
ATOM   42733 C  C   . SER   Y  11 27  ? 66.665  -154.558 11.992  1.00 106.66 ? 28  SER   Y C   1 
ATOM   42734 O  O   . SER   Y  11 27  ? 65.590  -153.974 11.734  1.00 96.89  ? 28  SER   Y O   1 
ATOM   42735 C  CB  . SER   Y  11 27  ? 66.624  -156.761 13.233  1.00 109.13 ? 28  SER   Y CB  1 
ATOM   42736 O  OG  . SER   Y  11 27  ? 67.403  -157.301 12.173  1.00 110.60 ? 28  SER   Y OG  1 
ATOM   42737 N  N   . GLN   Y  11 28  ? 67.733  -154.595 11.188  1.00 110.81 ? 29  GLN   Y N   1 
ATOM   42738 C  CA  . GLN   Y  11 28  ? 67.779  -154.106 9.783   1.00 110.22 ? 29  GLN   Y CA  1 
ATOM   42739 C  C   . GLN   Y  11 28  ? 68.268  -155.217 8.843   1.00 112.01 ? 29  GLN   Y C   1 
ATOM   42740 O  O   . GLN   Y  11 28  ? 68.520  -154.900 7.662   1.00 107.74 ? 29  GLN   Y O   1 
ATOM   42741 C  CB  . GLN   Y  11 28  ? 68.729  -152.913 9.672   1.00 111.97 ? 29  GLN   Y CB  1 
ATOM   42742 C  CG  . GLN   Y  11 28  ? 68.305  -151.704 10.493  1.00 113.47 ? 29  GLN   Y CG  1 
ATOM   42743 C  CD  . GLN   Y  11 28  ? 67.607  -150.655 9.661   1.00 112.76 ? 29  GLN   Y CD  1 
ATOM   42744 O  OE1 . GLN   Y  11 28  ? 66.623  -150.929 8.979   1.00 119.00 ? 29  GLN   Y OE1 1 
ATOM   42745 N  NE2 . GLN   Y  11 28  ? 68.114  -149.435 9.712   1.00 112.11 ? 29  GLN   Y NE2 1 
ATOM   42746 N  N   . THR   Y  11 29  ? 68.397  -156.459 9.332   1.00 113.66 ? 30  THR   Y N   1 
ATOM   42747 C  CA  . THR   Y  11 29  ? 68.997  -157.596 8.580   1.00 115.83 ? 30  THR   Y CA  1 
ATOM   42748 C  C   . THR   Y  11 29  ? 68.054  -158.805 8.564   1.00 116.95 ? 30  THR   Y C   1 
ATOM   42749 O  O   . THR   Y  11 29  ? 68.544  -159.918 8.284   1.00 124.18 ? 30  THR   Y O   1 
ATOM   42750 C  CB  . THR   Y  11 29  ? 70.360  -157.977 9.172   1.00 120.10 ? 30  THR   Y CB  1 
ATOM   42751 O  OG1 . THR   Y  11 29  ? 70.160  -158.679 10.400  1.00 126.26 ? 30  THR   Y OG1 1 
ATOM   42752 C  CG2 . THR   Y  11 29  ? 71.234  -156.769 9.425   1.00 116.65 ? 30  THR   Y CG2 1 
ATOM   42753 N  N   . VAL   Y  11 30  ? 66.761  -158.603 8.826   1.00 109.56 ? 31  VAL   Y N   1 
ATOM   42754 C  CA  . VAL   Y  11 30  ? 65.771  -159.714 8.927   1.00 108.01 ? 31  VAL   Y CA  1 
ATOM   42755 C  C   . VAL   Y  11 30  ? 65.531  -160.294 7.532   1.00 107.11 ? 31  VAL   Y C   1 
ATOM   42756 O  O   . VAL   Y  11 30  ? 65.395  -159.508 6.572   1.00 102.80 ? 31  VAL   Y O   1 
ATOM   42757 C  CB  . VAL   Y  11 30  ? 64.445  -159.265 9.566   1.00 107.65 ? 31  VAL   Y CB  1 
ATOM   42758 C  CG1 . VAL   Y  11 30  ? 63.452  -160.414 9.623   1.00 110.07 ? 31  VAL   Y CG1 1 
ATOM   42759 C  CG2 . VAL   Y  11 30  ? 64.662  -158.682 10.950  1.00 105.99 ? 31  VAL   Y CG2 1 
ATOM   42760 N  N   . LYS   Y  11 31  ? 65.476  -161.624 7.451   1.00 108.70 ? 32  LYS   Y N   1 
ATOM   42761 C  CA  . LYS   Y  11 31  ? 65.040  -162.383 6.254   1.00 108.57 ? 32  LYS   Y CA  1 
ATOM   42762 C  C   . LYS   Y  11 31  ? 63.514  -162.520 6.318   1.00 108.14 ? 32  LYS   Y C   1 
ATOM   42763 O  O   . LYS   Y  11 31  ? 63.028  -163.212 7.233   1.00 111.54 ? 32  LYS   Y O   1 
ATOM   42764 C  CB  . LYS   Y  11 31  ? 65.727  -163.750 6.224   1.00 111.70 ? 32  LYS   Y CB  1 
ATOM   42765 C  CG  . LYS   Y  11 31  ? 67.162  -163.760 5.710   1.00 118.47 ? 32  LYS   Y CG  1 
ATOM   42766 C  CD  . LYS   Y  11 31  ? 67.592  -165.123 5.193   1.00 124.64 ? 32  LYS   Y CD  1 
ATOM   42767 C  CE  . LYS   Y  11 31  ? 66.703  -165.644 4.080   1.00 125.49 ? 32  LYS   Y CE  1 
ATOM   42768 N  NZ  . LYS   Y  11 31  ? 67.044  -167.033 3.696   1.00 128.35 ? 32  LYS   Y NZ  1 
ATOM   42769 N  N   . LYS   Y  11 32  ? 62.790  -161.856 5.409   1.00 104.80 ? 33  LYS   Y N   1 
ATOM   42770 C  CA  . LYS   Y  11 32  ? 61.301  -161.857 5.355   1.00 103.00 ? 33  LYS   Y CA  1 
ATOM   42771 C  C   . LYS   Y  11 32  ? 60.799  -162.744 4.212   1.00 102.28 ? 33  LYS   Y C   1 
ATOM   42772 O  O   . LYS   Y  11 32  ? 59.569  -162.783 3.994   1.00 95.17  ? 33  LYS   Y O   1 
ATOM   42773 C  CB  . LYS   Y  11 32  ? 60.784  -160.430 5.181   1.00 102.36 ? 33  LYS   Y CB  1 
ATOM   42774 C  CG  . LYS   Y  11 32  ? 61.083  -159.513 6.353   1.00 104.16 ? 33  LYS   Y CG  1 
ATOM   42775 C  CD  . LYS   Y  11 32  ? 60.541  -158.127 6.162   1.00 102.62 ? 33  LYS   Y CD  1 
ATOM   42776 C  CE  . LYS   Y  11 32  ? 60.814  -157.241 7.354   1.00 103.60 ? 33  LYS   Y CE  1 
ATOM   42777 N  NZ  . LYS   Y  11 32  ? 60.204  -155.909 7.170   1.00 103.76 ? 33  LYS   Y NZ  1 
ATOM   42778 N  N   . VAL   Y  11 33  ? 61.714  -163.408 3.503   1.00 103.61 ? 34  VAL   Y N   1 
ATOM   42779 C  CA  . VAL   Y  11 33  ? 61.405  -164.505 2.542   1.00 105.78 ? 34  VAL   Y CA  1 
ATOM   42780 C  C   . VAL   Y  11 33  ? 61.947  -165.798 3.153   1.00 107.03 ? 34  VAL   Y C   1 
ATOM   42781 O  O   . VAL   Y  11 33  ? 63.122  -165.797 3.571   1.00 102.89 ? 34  VAL   Y O   1 
ATOM   42782 C  CB  . VAL   Y  11 33  ? 62.005  -164.239 1.147   1.00 107.61 ? 34  VAL   Y CB  1 
ATOM   42783 C  CG1 . VAL   Y  11 33  ? 61.786  -165.408 0.202   1.00 109.86 ? 34  VAL   Y CG1 1 
ATOM   42784 C  CG2 . VAL   Y  11 33  ? 61.457  -162.962 0.537   1.00 107.49 ? 34  VAL   Y CG2 1 
ATOM   42785 N  N   . ILE   Y  11 34  ? 61.116  -166.841 3.209   1.00 107.91 ? 35  ILE   Y N   1 
ATOM   42786 C  CA  . ILE   Y  11 34  ? 61.502  -168.199 3.696   1.00 108.53 ? 35  ILE   Y CA  1 
ATOM   42787 C  C   . ILE   Y  11 34  ? 61.561  -169.123 2.477   1.00 107.47 ? 35  ILE   Y C   1 
ATOM   42788 O  O   . ILE   Y  11 34  ? 60.570  -169.172 1.718   1.00 101.56 ? 35  ILE   Y O   1 
ATOM   42789 C  CB  . ILE   Y  11 34  ? 60.549  -168.693 4.809   1.00 108.98 ? 35  ILE   Y CB  1 
ATOM   42790 C  CG1 . ILE   Y  11 34  ? 60.893  -170.097 5.317   1.00 114.43 ? 35  ILE   Y CG1 1 
ATOM   42791 C  CG2 . ILE   Y  11 34  ? 59.094  -168.584 4.389   1.00 107.89 ? 35  ILE   Y CG2 1 
ATOM   42792 C  CD1 . ILE   Y  11 34  ? 60.417  -171.232 4.435   1.00 119.02 ? 35  ILE   Y CD1 1 
ATOM   42793 N  N   . GLU   Y  11 35  ? 62.701  -169.789 2.282   1.00 111.16 ? 36  GLU   Y N   1 
ATOM   42794 C  CA  . GLU   Y  11 35  ? 62.907  -170.779 1.193   1.00 116.43 ? 36  GLU   Y CA  1 
ATOM   42795 C  C   . GLU   Y  11 35  ? 62.290  -172.113 1.630   1.00 115.58 ? 36  GLU   Y C   1 
ATOM   42796 O  O   . GLU   Y  11 35  ? 63.001  -172.922 2.265   1.00 113.36 ? 36  GLU   Y O   1 
ATOM   42797 C  CB  . GLU   Y  11 35  ? 64.395  -170.915 0.861   1.00 124.23 ? 36  GLU   Y CB  1 
ATOM   42798 C  CG  . GLU   Y  11 35  ? 65.080  -169.589 0.577   1.00 125.93 ? 36  GLU   Y CG  1 
ATOM   42799 C  CD  . GLU   Y  11 35  ? 66.361  -169.699 -0.233  1.00 131.60 ? 36  GLU   Y CD  1 
ATOM   42800 O  OE1 . GLU   Y  11 35  ? 66.942  -170.815 -0.274  1.00 137.09 ? 36  GLU   Y OE1 1 
ATOM   42801 O  OE2 . GLU   Y  11 35  ? 66.774  -168.669 -0.829  1.00 134.45 ? 36  GLU   Y OE2 1 
ATOM   42802 N  N   . ILE   Y  11 36  ? 61.003  -172.308 1.328   1.00 113.65 ? 37  ILE   Y N   1 
ATOM   42803 C  CA  . ILE   Y  11 36  ? 60.240  -173.553 1.641   1.00 113.88 ? 37  ILE   Y CA  1 
ATOM   42804 C  C   . ILE   Y  11 36  ? 60.897  -174.725 0.897   1.00 113.55 ? 37  ILE   Y C   1 
ATOM   42805 O  O   . ILE   Y  11 36  ? 61.103  -175.780 1.521   1.00 113.56 ? 37  ILE   Y O   1 
ATOM   42806 C  CB  . ILE   Y  11 36  ? 58.749  -173.384 1.282   1.00 113.77 ? 37  ILE   Y CB  1 
ATOM   42807 C  CG1 . ILE   Y  11 36  ? 58.047  -172.421 2.245   1.00 109.92 ? 37  ILE   Y CG1 1 
ATOM   42808 C  CG2 . ILE   Y  11 36  ? 58.054  -174.736 1.221   1.00 117.51 ? 37  ILE   Y CG2 1 
ATOM   42809 C  CD1 . ILE   Y  11 36  ? 56.686  -171.953 1.783   1.00 107.17 ? 37  ILE   Y CD1 1 
ATOM   42810 N  N   . ASN   Y  11 37  ? 61.213  -174.534 -0.387  1.00 115.89 ? 38  ASN   Y N   1 
ATOM   42811 C  CA  . ASN   Y  11 37  ? 61.895  -175.537 -1.249  1.00 121.98 ? 38  ASN   Y CA  1 
ATOM   42812 C  C   . ASN   Y  11 37  ? 62.456  -174.811 -2.472  1.00 124.08 ? 38  ASN   Y C   1 
ATOM   42813 O  O   . ASN   Y  11 37  ? 62.223  -173.617 -2.632  1.00 124.40 ? 38  ASN   Y O   1 
ATOM   42814 C  CB  . ASN   Y  11 37  ? 60.950  -176.703 -1.568  1.00 124.37 ? 38  ASN   Y CB  1 
ATOM   42815 C  CG  . ASN   Y  11 37  ? 59.969  -176.426 -2.690  1.00 127.80 ? 38  ASN   Y CG  1 
ATOM   42816 O  OD1 . ASN   Y  11 37  ? 60.284  -175.721 -3.647  1.00 132.35 ? 38  ASN   Y OD1 1 
ATOM   42817 N  ND2 . ASN   Y  11 37  ? 58.778  -176.995 -2.595  1.00 127.78 ? 38  ASN   Y ND2 1 
ATOM   42818 N  N   . PRO   Y  11 38  ? 63.204  -175.496 -3.369  1.00 129.67 ? 39  PRO   Y N   1 
ATOM   42819 C  CA  . PRO   Y  11 38  ? 63.787  -174.864 -4.557  1.00 131.10 ? 39  PRO   Y CA  1 
ATOM   42820 C  C   . PRO   Y  11 38  ? 62.815  -174.199 -5.546  1.00 127.11 ? 39  PRO   Y C   1 
ATOM   42821 O  O   . PRO   Y  11 38  ? 63.273  -173.374 -6.319  1.00 122.07 ? 39  PRO   Y O   1 
ATOM   42822 C  CB  . PRO   Y  11 38  ? 64.442  -176.034 -5.306  1.00 135.08 ? 39  PRO   Y CB  1 
ATOM   42823 C  CG  . PRO   Y  11 38  ? 64.719  -177.054 -4.230  1.00 138.99 ? 39  PRO   Y CG  1 
ATOM   42824 C  CD  . PRO   Y  11 38  ? 63.553  -176.920 -3.275  1.00 133.60 ? 39  PRO   Y CD  1 
ATOM   42825 N  N   . PHE   Y  11 39  ? 61.539  -174.606 -5.549  1.00 127.03 ? 40  PHE   Y N   1 
ATOM   42826 C  CA  . PHE   Y  11 39  ? 60.474  -174.060 -6.435  1.00 126.22 ? 40  PHE   Y CA  1 
ATOM   42827 C  C   . PHE   Y  11 39  ? 59.467  -173.215 -5.645  1.00 116.16 ? 40  PHE   Y C   1 
ATOM   42828 O  O   . PHE   Y  11 39  ? 58.619  -172.589 -6.308  1.00 117.73 ? 40  PHE   Y O   1 
ATOM   42829 C  CB  . PHE   Y  11 39  ? 59.737  -175.183 -7.171  1.00 132.78 ? 40  PHE   Y CB  1 
ATOM   42830 C  CG  . PHE   Y  11 39  ? 60.397  -175.627 -8.452  1.00 140.10 ? 40  PHE   Y CG  1 
ATOM   42831 C  CD1 . PHE   Y  11 39  ? 60.076  -175.025 -9.661  1.00 142.16 ? 40  PHE   Y CD1 1 
ATOM   42832 C  CD2 . PHE   Y  11 39  ? 61.345  -176.638 -8.449  1.00 140.72 ? 40  PHE   Y CD2 1 
ATOM   42833 C  CE1 . PHE   Y  11 39  ? 60.689  -175.426 -10.838 1.00 143.05 ? 40  PHE   Y CE1 1 
ATOM   42834 C  CE2 . PHE   Y  11 39  ? 61.955  -177.039 -9.628  1.00 145.53 ? 40  PHE   Y CE2 1 
ATOM   42835 C  CZ  . PHE   Y  11 39  ? 61.626  -176.432 -10.820 1.00 147.08 ? 40  PHE   Y CZ  1 
ATOM   42836 N  N   . LEU   Y  11 40  ? 59.541  -173.190 -4.308  1.00 114.82 ? 41  LEU   Y N   1 
ATOM   42837 C  CA  . LEU   Y  11 40  ? 58.527  -172.505 -3.457  1.00 111.44 ? 41  LEU   Y CA  1 
ATOM   42838 C  C   . LEU   Y  11 40  ? 59.164  -171.448 -2.545  1.00 110.53 ? 41  LEU   Y C   1 
ATOM   42839 O  O   . LEU   Y  11 40  ? 60.128  -171.773 -1.821  1.00 106.32 ? 41  LEU   Y O   1 
ATOM   42840 C  CB  . LEU   Y  11 40  ? 57.748  -173.543 -2.639  1.00 110.98 ? 41  LEU   Y CB  1 
ATOM   42841 C  CG  . LEU   Y  11 40  ? 56.310  -173.812 -3.087  1.00 109.22 ? 41  LEU   Y CG  1 
ATOM   42842 C  CD1 . LEU   Y  11 40  ? 55.446  -174.205 -1.900  1.00 106.78 ? 41  LEU   Y CD1 1 
ATOM   42843 C  CD2 . LEU   Y  11 40  ? 55.698  -172.606 -3.788  1.00 109.67 ? 41  LEU   Y CD2 1 
ATOM   42844 N  N   . LEU   Y  11 41  ? 58.589  -170.239 -2.568  1.00 108.30 ? 42  LEU   Y N   1 
ATOM   42845 C  CA  . LEU   Y  11 41  ? 58.996  -169.056 -1.762  1.00 105.80 ? 42  LEU   Y CA  1 
ATOM   42846 C  C   . LEU   Y  11 41  ? 57.805  -168.551 -0.940  1.00 102.83 ? 42  LEU   Y C   1 
ATOM   42847 O  O   . LEU   Y  11 41  ? 56.668  -168.565 -1.460  1.00 101.77 ? 42  LEU   Y O   1 
ATOM   42848 C  CB  . LEU   Y  11 41  ? 59.494  -167.952 -2.700  1.00 105.22 ? 42  LEU   Y CB  1 
ATOM   42849 C  CG  . LEU   Y  11 41  ? 60.993  -167.938 -2.991  1.00 109.68 ? 42  LEU   Y CG  1 
ATOM   42850 C  CD1 . LEU   Y  11 41  ? 61.389  -166.619 -3.634  1.00 109.10 ? 42  LEU   Y CD1 1 
ATOM   42851 C  CD2 . LEU   Y  11 41  ? 61.810  -168.180 -1.730  1.00 111.15 ? 42  LEU   Y CD2 1 
ATOM   42852 N  N   . GLY   Y  11 42  ? 58.078  -168.096 0.286   1.00 101.26 ? 43  GLY   Y N   1 
ATOM   42853 C  CA  . GLY   Y  11 42  ? 57.076  -167.562 1.227   1.00 102.28 ? 43  GLY   Y CA  1 
ATOM   42854 C  C   . GLY   Y  11 42  ? 57.465  -166.182 1.732   1.00 101.42 ? 43  GLY   Y C   1 
ATOM   42855 O  O   . GLY   Y  11 42  ? 58.587  -166.035 2.248   1.00 104.75 ? 43  GLY   Y O   1 
ATOM   42856 N  N   . THR   Y  11 43  ? 56.567  -165.206 1.584   1.00 102.31 ? 44  THR   Y N   1 
ATOM   42857 C  CA  . THR   Y  11 43  ? 56.712  -163.804 2.066   1.00 103.98 ? 44  THR   Y CA  1 
ATOM   42858 C  C   . THR   Y  11 43  ? 56.211  -163.711 3.507   1.00 100.86 ? 44  THR   Y C   1 
ATOM   42859 O  O   . THR   Y  11 43  ? 55.205  -164.369 3.793   1.00 104.80 ? 44  THR   Y O   1 
ATOM   42860 C  CB  . THR   Y  11 43  ? 55.861  -162.846 1.229   1.00 104.39 ? 44  THR   Y CB  1 
ATOM   42861 O  OG1 . THR   Y  11 43  ? 54.629  -163.537 1.042   1.00 110.85 ? 44  THR   Y OG1 1 
ATOM   42862 C  CG2 . THR   Y  11 43  ? 56.474  -162.474 -0.101  1.00 104.63 ? 44  THR   Y CG2 1 
ATOM   42863 N  N   . MET   Y  11 44  ? 56.849  -162.902 4.359   1.00 97.23  ? 45  MET   Y N   1 
ATOM   42864 C  CA  . MET   Y  11 44  ? 56.469  -162.749 5.791   1.00 97.38  ? 45  MET   Y CA  1 
ATOM   42865 C  C   . MET   Y  11 44  ? 56.035  -161.310 6.085   1.00 97.91  ? 45  MET   Y C   1 
ATOM   42866 O  O   . MET   Y  11 44  ? 56.811  -160.383 5.791   1.00 105.33 ? 45  MET   Y O   1 
ATOM   42867 C  CB  . MET   Y  11 44  ? 57.638  -163.092 6.715   1.00 97.46  ? 45  MET   Y CB  1 
ATOM   42868 C  CG  . MET   Y  11 44  ? 58.132  -164.500 6.561   1.00 97.50  ? 45  MET   Y CG  1 
ATOM   42869 S  SD  . MET   Y  11 44  ? 59.334  -164.903 7.841   1.00 97.36  ? 45  MET   Y SD  1 
ATOM   42870 C  CE  . MET   Y  11 44  ? 59.839  -166.517 7.251   1.00 103.47 ? 45  MET   Y CE  1 
ATOM   42871 N  N   . ALA   Y  11 45  ? 54.854  -161.150 6.686   1.00 97.59  ? 46  ALA   Y N   1 
ATOM   42872 C  CA  . ALA   Y  11 45  ? 54.296  -159.864 7.166   1.00 98.96  ? 46  ALA   Y CA  1 
ATOM   42873 C  C   . ALA   Y  11 45  ? 53.575  -160.105 8.493   1.00 95.92  ? 46  ALA   Y C   1 
ATOM   42874 O  O   . ALA   Y  11 45  ? 53.150  -161.248 8.728   1.00 98.62  ? 46  ALA   Y O   1 
ATOM   42875 C  CB  . ALA   Y  11 45  ? 53.358  -159.283 6.139   1.00 99.06  ? 46  ALA   Y CB  1 
ATOM   42876 N  N   . GLY   Y  11 46  ? 53.428  -159.063 9.312   1.00 95.50  ? 47  GLY   Y N   1 
ATOM   42877 C  CA  . GLY   Y  11 46  ? 52.812  -159.159 10.649  1.00 95.06  ? 47  GLY   Y CA  1 
ATOM   42878 C  C   . GLY   Y  11 46  ? 53.782  -159.751 11.655  1.00 96.00  ? 47  GLY   Y C   1 
ATOM   42879 O  O   . GLY   Y  11 46  ? 54.996  -159.485 11.527  1.00 97.55  ? 47  GLY   Y O   1 
ATOM   42880 N  N   . GLY   Y  11 47  ? 53.274  -160.536 12.610  1.00 95.76  ? 48  GLY   Y N   1 
ATOM   42881 C  CA  . GLY   Y  11 47  ? 54.079  -161.185 13.662  1.00 95.24  ? 48  GLY   Y CA  1 
ATOM   42882 C  C   . GLY   Y  11 47  ? 55.185  -162.034 13.061  1.00 94.92  ? 48  GLY   Y C   1 
ATOM   42883 O  O   . GLY   Y  11 47  ? 54.859  -162.952 12.283  1.00 97.35  ? 48  GLY   Y O   1 
ATOM   42884 N  N   . ALA   Y  11 48  ? 56.444  -161.724 13.388  1.00 94.20  ? 49  ALA   Y N   1 
ATOM   42885 C  CA  . ALA   Y  11 48  ? 57.657  -162.402 12.870  1.00 93.06  ? 49  ALA   Y CA  1 
ATOM   42886 C  C   . ALA   Y  11 48  ? 57.650  -163.876 13.290  1.00 91.75  ? 49  ALA   Y C   1 
ATOM   42887 O  O   . ALA   Y  11 48  ? 57.885  -164.738 12.424  1.00 90.70  ? 49  ALA   Y O   1 
ATOM   42888 C  CB  . ALA   Y  11 48  ? 58.894  -161.704 13.373  1.00 93.56  ? 49  ALA   Y CB  1 
ATOM   42889 N  N   . ALA   Y  11 49  ? 57.390  -164.141 14.575  1.00 93.70  ? 50  ALA   Y N   1 
ATOM   42890 C  CA  . ALA   Y  11 49  ? 57.376  -165.495 15.178  1.00 93.06  ? 50  ALA   Y CA  1 
ATOM   42891 C  C   . ALA   Y  11 49  ? 56.328  -166.356 14.473  1.00 87.73  ? 50  ALA   Y C   1 
ATOM   42892 O  O   . ALA   Y  11 49  ? 56.670  -167.477 14.082  1.00 88.93  ? 50  ALA   Y O   1 
ATOM   42893 C  CB  . ALA   Y  11 49  ? 57.107  -165.413 16.660  1.00 95.73  ? 50  ALA   Y CB  1 
ATOM   42894 N  N   . ASP   Y  11 50  ? 55.109  -165.837 14.304  1.00 87.10  ? 51  ASP   Y N   1 
ATOM   42895 C  CA  . ASP   Y  11 50  ? 53.973  -166.577 13.694  1.00 87.28  ? 51  ASP   Y CA  1 
ATOM   42896 C  C   . ASP   Y  11 50  ? 54.371  -167.021 12.279  1.00 88.24  ? 51  ASP   Y C   1 
ATOM   42897 O  O   . ASP   Y  11 50  ? 54.386  -168.241 12.040  1.00 88.71  ? 51  ASP   Y O   1 
ATOM   42898 C  CB  . ASP   Y  11 50  ? 52.686  -165.748 13.722  1.00 86.89  ? 51  ASP   Y CB  1 
ATOM   42899 C  CG  . ASP   Y  11 50  ? 52.194  -165.417 15.121  1.00 88.94  ? 51  ASP   Y CG  1 
ATOM   42900 O  OD1 . ASP   Y  11 50  ? 52.738  -165.988 16.088  1.00 88.66  ? 51  ASP   Y OD1 1 
ATOM   42901 O  OD2 . ASP   Y  11 50  ? 51.257  -164.597 15.230  1.00 90.78  ? 51  ASP   Y OD2 1 
ATOM   42902 N  N   . CYS   Y  11 51  ? 54.695  -166.082 11.383  1.00 88.53  ? 52  CYS   Y N   1 
ATOM   42903 C  CA  . CYS   Y  11 51  ? 55.070  -166.369 9.969   1.00 90.04  ? 52  CYS   Y CA  1 
ATOM   42904 C  C   . CYS   Y  11 51  ? 56.209  -167.392 9.937   1.00 89.37  ? 52  CYS   Y C   1 
ATOM   42905 O  O   . CYS   Y  11 51  ? 56.032  -168.459 9.322   1.00 88.08  ? 52  CYS   Y O   1 
ATOM   42906 C  CB  . CYS   Y  11 51  ? 55.519  -165.117 9.225   1.00 91.21  ? 52  CYS   Y CB  1 
ATOM   42907 S  SG  . CYS   Y  11 51  ? 54.235  -163.846 9.121   1.00 92.96  ? 52  CYS   Y SG  1 
ATOM   42908 N  N   . GLN   Y  11 52  ? 57.319  -167.063 10.603  1.00 90.34  ? 53  GLN   Y N   1 
ATOM   42909 C  CA  . GLN   Y  11 52  ? 58.584  -167.846 10.622  1.00 90.93  ? 53  GLN   Y CA  1 
ATOM   42910 C  C   . GLN   Y  11 52  ? 58.311  -169.283 11.082  1.00 88.98  ? 53  GLN   Y C   1 
ATOM   42911 O  O   . GLN   Y  11 52  ? 58.789  -170.213 10.414  1.00 88.86  ? 53  GLN   Y O   1 
ATOM   42912 C  CB  . GLN   Y  11 52  ? 59.588  -167.147 11.537  1.00 92.53  ? 53  GLN   Y CB  1 
ATOM   42913 C  CG  . GLN   Y  11 52  ? 60.945  -167.828 11.608  1.00 95.04  ? 53  GLN   Y CG  1 
ATOM   42914 C  CD  . GLN   Y  11 52  ? 61.949  -166.979 12.348  1.00 98.32  ? 53  GLN   Y CD  1 
ATOM   42915 O  OE1 . GLN   Y  11 52  ? 62.639  -167.450 13.249  1.00 101.44 ? 53  GLN   Y OE1 1 
ATOM   42916 N  NE2 . GLN   Y  11 52  ? 62.029  -165.708 11.984  1.00 98.25  ? 53  GLN   Y NE2 1 
ATOM   42917 N  N   . PHE   Y  11 53  ? 57.574  -169.455 12.183  1.00 86.15  ? 54  PHE   Y N   1 
ATOM   42918 C  CA  . PHE   Y  11 53  ? 57.249  -170.782 12.765  1.00 85.59  ? 54  PHE   Y CA  1 
ATOM   42919 C  C   . PHE   Y  11 53  ? 56.407  -171.590 11.772  1.00 85.78  ? 54  PHE   Y C   1 
ATOM   42920 O  O   . PHE   Y  11 53  ? 56.802  -172.720 11.436  1.00 89.21  ? 54  PHE   Y O   1 
ATOM   42921 C  CB  . PHE   Y  11 53  ? 56.514  -170.650 14.101  1.00 84.74  ? 54  PHE   Y CB  1 
ATOM   42922 C  CG  . PHE   Y  11 53  ? 56.184  -171.976 14.738  1.00 84.90  ? 54  PHE   Y CG  1 
ATOM   42923 C  CD1 . PHE   Y  11 53  ? 56.998  -172.513 15.725  1.00 85.49  ? 54  PHE   Y CD1 1 
ATOM   42924 C  CD2 . PHE   Y  11 53  ? 55.083  -172.708 14.320  1.00 83.29  ? 54  PHE   Y CD2 1 
ATOM   42925 C  CE1 . PHE   Y  11 53  ? 56.703  -173.741 16.295  1.00 83.89  ? 54  PHE   Y CE1 1 
ATOM   42926 C  CE2 . PHE   Y  11 53  ? 54.790  -173.936 14.891  1.00 82.06  ? 54  PHE   Y CE2 1 
ATOM   42927 C  CZ  . PHE   Y  11 53  ? 55.599  -174.448 15.879  1.00 82.59  ? 54  PHE   Y CZ  1 
ATOM   42928 N  N   . TRP   Y  11 54  ? 55.277  -171.034 11.329  1.00 82.99  ? 55  TRP   Y N   1 
ATOM   42929 C  CA  . TRP   Y  11 54  ? 54.247  -171.771 10.549  1.00 83.03  ? 55  TRP   Y CA  1 
ATOM   42930 C  C   . TRP   Y  11 54  ? 54.675  -171.966 9.091   1.00 83.82  ? 55  TRP   Y C   1 
ATOM   42931 O  O   . TRP   Y  11 54  ? 54.203  -172.937 8.487   1.00 83.85  ? 55  TRP   Y O   1 
ATOM   42932 C  CB  . TRP   Y  11 54  ? 52.886  -171.082 10.645  1.00 81.78  ? 55  TRP   Y CB  1 
ATOM   42933 C  CG  . TRP   Y  11 54  ? 52.252  -171.245 11.990  1.00 83.35  ? 55  TRP   Y CG  1 
ATOM   42934 C  CD1 . TRP   Y  11 54  ? 52.009  -170.272 12.914  1.00 84.11  ? 55  TRP   Y CD1 1 
ATOM   42935 C  CD2 . TRP   Y  11 54  ? 51.809  -172.476 12.584  1.00 83.78  ? 55  TRP   Y CD2 1 
ATOM   42936 N  NE1 . TRP   Y  11 54  ? 51.425  -170.806 14.029  1.00 85.45  ? 55  TRP   Y NE1 1 
ATOM   42937 C  CE2 . TRP   Y  11 54  ? 51.293  -172.156 13.858  1.00 85.10  ? 55  TRP   Y CE2 1 
ATOM   42938 C  CE3 . TRP   Y  11 54  ? 51.788  -173.811 12.164  1.00 82.61  ? 55  TRP   Y CE3 1 
ATOM   42939 C  CZ2 . TRP   Y  11 54  ? 50.765  -173.120 14.713  1.00 85.11  ? 55  TRP   Y CZ2 1 
ATOM   42940 C  CZ3 . TRP   Y  11 54  ? 51.264  -174.763 13.009  1.00 83.68  ? 55  TRP   Y CZ3 1 
ATOM   42941 C  CH2 . TRP   Y  11 54  ? 50.760  -174.420 14.265  1.00 84.17  ? 55  TRP   Y CH2 1 
ATOM   42942 N  N   . GLU   Y  11 55  ? 55.508  -171.087 8.530   1.00 88.14  ? 56  GLU   Y N   1 
ATOM   42943 C  CA  . GLU   Y  11 55  ? 55.982  -171.240 7.127   1.00 92.37  ? 56  GLU   Y CA  1 
ATOM   42944 C  C   . GLU   Y  11 55  ? 57.114  -172.279 7.056   1.00 91.70  ? 56  GLU   Y C   1 
ATOM   42945 O  O   . GLU   Y  11 55  ? 57.136  -173.026 6.059   1.00 91.19  ? 56  GLU   Y O   1 
ATOM   42946 C  CB  . GLU   Y  11 55  ? 56.399  -169.904 6.515   1.00 95.39  ? 56  GLU   Y CB  1 
ATOM   42947 C  CG  . GLU   Y  11 55  ? 55.222  -168.992 6.219   1.00 97.06  ? 56  GLU   Y CG  1 
ATOM   42948 C  CD  . GLU   Y  11 55  ? 55.497  -167.885 5.216   1.00 98.00  ? 56  GLU   Y CD  1 
ATOM   42949 O  OE1 . GLU   Y  11 55  ? 56.538  -167.925 4.547   1.00 105.28 ? 56  GLU   Y OE1 1 
ATOM   42950 O  OE2 . GLU   Y  11 55  ? 54.659  -166.996 5.097   1.00 100.16 ? 56  GLU   Y OE2 1 
ATOM   42951 N  N   . THR   Y  11 56  ? 58.028  -172.336 8.036   1.00 93.51  ? 57  THR   Y N   1 
ATOM   42952 C  CA  . THR   Y  11 56  ? 59.064  -173.409 8.097   1.00 93.42  ? 57  THR   Y CA  1 
ATOM   42953 C  C   . THR   Y  11 56  ? 58.358  -174.743 8.386   1.00 93.64  ? 57  THR   Y C   1 
ATOM   42954 O  O   . THR   Y  11 56  ? 58.853  -175.785 7.901   1.00 92.53  ? 57  THR   Y O   1 
ATOM   42955 C  CB  . THR   Y  11 56  ? 60.198  -173.145 9.101   1.00 95.21  ? 57  THR   Y CB  1 
ATOM   42956 O  OG1 . THR   Y  11 56  ? 59.675  -173.342 10.414  1.00 94.77  ? 57  THR   Y OG1 1 
ATOM   42957 C  CG2 . THR   Y  11 56  ? 60.841  -171.779 8.974   1.00 95.83  ? 57  THR   Y CG2 1 
ATOM   42958 N  N   . TRP   Y  11 57  ? 57.243  -174.707 9.133   1.00 91.65  ? 58  TRP   Y N   1 
ATOM   42959 C  CA  . TRP   Y  11 57  ? 56.324  -175.862 9.345   1.00 89.18  ? 58  TRP   Y CA  1 
ATOM   42960 C  C   . TRP   Y  11 57  ? 55.668  -176.252 8.018   1.00 88.99  ? 58  TRP   Y C   1 
ATOM   42961 O  O   . TRP   Y  11 57  ? 55.630  -177.454 7.721   1.00 92.72  ? 58  TRP   Y O   1 
ATOM   42962 C  CB  . TRP   Y  11 57  ? 55.253  -175.559 10.401  1.00 84.35  ? 58  TRP   Y CB  1 
ATOM   42963 C  CG  . TRP   Y  11 57  ? 54.156  -176.582 10.464  1.00 82.49  ? 58  TRP   Y CG  1 
ATOM   42964 C  CD1 . TRP   Y  11 57  ? 54.151  -177.734 11.196  1.00 81.46  ? 58  TRP   Y CD1 1 
ATOM   42965 C  CD2 . TRP   Y  11 57  ? 52.895  -176.552 9.769   1.00 80.54  ? 58  TRP   Y CD2 1 
ATOM   42966 N  NE1 . TRP   Y  11 57  ? 52.978  -178.415 11.009  1.00 79.74  ? 58  TRP   Y NE1 1 
ATOM   42967 C  CE2 . TRP   Y  11 57  ? 52.187  -177.716 10.139  1.00 78.64  ? 58  TRP   Y CE2 1 
ATOM   42968 C  CE3 . TRP   Y  11 57  ? 52.292  -175.660 8.875   1.00 81.91  ? 58  TRP   Y CE3 1 
ATOM   42969 C  CZ2 . TRP   Y  11 57  ? 50.915  -178.004 9.647   1.00 77.05  ? 58  TRP   Y CZ2 1 
ATOM   42970 C  CZ3 . TRP   Y  11 57  ? 51.034  -175.945 8.390   1.00 80.03  ? 58  TRP   Y CZ3 1 
ATOM   42971 C  CH2 . TRP   Y  11 57  ? 50.355  -177.102 8.773   1.00 77.66  ? 58  TRP   Y CH2 1 
ATOM   42972 N  N   . LEU   Y  11 58  ? 55.137  -175.273 7.280   1.00 88.72  ? 59  LEU   Y N   1 
ATOM   42973 C  CA  . LEU   Y  11 58  ? 54.549  -175.471 5.927   1.00 89.77  ? 59  LEU   Y CA  1 
ATOM   42974 C  C   . LEU   Y  11 58  ? 55.564  -176.212 5.051   1.00 91.53  ? 59  LEU   Y C   1 
ATOM   42975 O  O   . LEU   Y  11 58  ? 55.153  -177.140 4.331   1.00 91.03  ? 59  LEU   Y O   1 
ATOM   42976 C  CB  . LEU   Y  11 58  ? 54.185  -174.114 5.311   1.00 88.94  ? 59  LEU   Y CB  1 
ATOM   42977 C  CG  . LEU   Y  11 58  ? 53.760  -174.142 3.842   1.00 88.51  ? 59  LEU   Y CG  1 
ATOM   42978 C  CD1 . LEU   Y  11 58  ? 52.521  -175.000 3.651   1.00 87.69  ? 59  LEU   Y CD1 1 
ATOM   42979 C  CD2 . LEU   Y  11 58  ? 53.512  -172.738 3.317   1.00 88.40  ? 59  LEU   Y CD2 1 
ATOM   42980 N  N   . GLY   Y  11 59  ? 56.837  -175.805 5.117   1.00 94.81  ? 60  GLY   Y N   1 
ATOM   42981 C  CA  . GLY   Y  11 59  ? 57.948  -176.397 4.346   1.00 97.30  ? 60  GLY   Y CA  1 
ATOM   42982 C  C   . GLY   Y  11 59  ? 58.109  -177.882 4.615   1.00 98.15  ? 60  GLY   Y C   1 
ATOM   42983 O  O   . GLY   Y  11 59  ? 58.416  -178.629 3.664   1.00 96.77  ? 60  GLY   Y O   1 
ATOM   42984 N  N   . SER   Y  11 60  ? 57.907  -178.297 5.867   1.00 98.40  ? 61  SER   Y N   1 
ATOM   42985 C  CA  . SER   Y  11 60  ? 57.942  -179.716 6.306   1.00 99.30  ? 61  SER   Y CA  1 
ATOM   42986 C  C   . SER   Y  11 60  ? 56.742  -180.477 5.728   1.00 96.91  ? 61  SER   Y C   1 
ATOM   42987 O  O   . SER   Y  11 60  ? 56.934  -181.628 5.312   1.00 100.25 ? 61  SER   Y O   1 
ATOM   42988 C  CB  . SER   Y  11 60  ? 57.993  -179.818 7.805   1.00 98.38  ? 61  SER   Y CB  1 
ATOM   42989 O  OG  . SER   Y  11 60  ? 59.163  -179.197 8.308   1.00 103.14 ? 61  SER   Y OG  1 
ATOM   42990 N  N   . GLN   Y  11 61  ? 55.558  -179.858 5.690   1.00 96.93  ? 62  GLN   Y N   1 
ATOM   42991 C  CA  . GLN   Y  11 61  ? 54.316  -180.471 5.139   1.00 99.77  ? 62  GLN   Y CA  1 
ATOM   42992 C  C   . GLN   Y  11 61  ? 54.473  -180.695 3.629   1.00 97.95  ? 62  GLN   Y C   1 
ATOM   42993 O  O   . GLN   Y  11 61  ? 54.029  -181.753 3.144   1.00 94.01  ? 62  GLN   Y O   1 
ATOM   42994 C  CB  . GLN   Y  11 61  ? 53.093  -179.592 5.415   1.00 101.49 ? 62  GLN   Y CB  1 
ATOM   42995 C  CG  . GLN   Y  11 61  ? 52.794  -179.392 6.895   1.00 103.63 ? 62  GLN   Y CG  1 
ATOM   42996 C  CD  . GLN   Y  11 61  ? 52.618  -180.702 7.624   1.00 104.62 ? 62  GLN   Y CD  1 
ATOM   42997 O  OE1 . GLN   Y  11 61  ? 51.762  -181.513 7.282   1.00 107.36 ? 62  GLN   Y OE1 1 
ATOM   42998 N  NE2 . GLN   Y  11 61  ? 53.434  -180.921 8.642   1.00 109.04 ? 62  GLN   Y NE2 1 
ATOM   42999 N  N   . CYS   Y  11 62  ? 55.061  -179.724 2.920   1.00 101.67 ? 63  CYS   Y N   1 
ATOM   43000 C  CA  . CYS   Y  11 62  ? 55.357  -179.785 1.461   1.00 102.86 ? 63  CYS   Y CA  1 
ATOM   43001 C  C   . CYS   Y  11 62  ? 56.327  -180.935 1.169   1.00 101.11 ? 63  CYS   Y C   1 
ATOM   43002 O  O   . CYS   Y  11 62  ? 56.144  -181.602 0.137   1.00 96.75  ? 63  CYS   Y O   1 
ATOM   43003 C  CB  . CYS   Y  11 62  ? 55.929  -178.466 0.954   1.00 108.14 ? 63  CYS   Y CB  1 
ATOM   43004 S  SG  . CYS   Y  11 62  ? 54.746  -177.099 1.061   1.00 113.90 ? 63  CYS   Y SG  1 
ATOM   43005 N  N   . ARG   Y  11 63  ? 57.319  -181.150 2.041   1.00 102.22 ? 64  ARG   Y N   1 
ATOM   43006 C  CA  . ARG   Y  11 63  ? 58.305  -182.262 1.927   1.00 103.83 ? 64  ARG   Y CA  1 
ATOM   43007 C  C   . ARG   Y  11 63  ? 57.594  -183.611 2.114   1.00 104.03 ? 64  ARG   Y C   1 
ATOM   43008 O  O   . ARG   Y  11 63  ? 57.943  -184.563 1.387   1.00 104.44 ? 64  ARG   Y O   1 
ATOM   43009 C  CB  . ARG   Y  11 63  ? 59.440  -182.104 2.947   1.00 105.28 ? 64  ARG   Y CB  1 
ATOM   43010 C  CG  . ARG   Y  11 63  ? 60.458  -183.238 2.927   1.00 107.16 ? 64  ARG   Y CG  1 
ATOM   43011 C  CD  . ARG   Y  11 63  ? 61.302  -183.259 1.666   1.00 108.62 ? 64  ARG   Y CD  1 
ATOM   43012 N  NE  . ARG   Y  11 63  ? 62.238  -184.380 1.661   1.00 111.02 ? 64  ARG   Y NE  1 
ATOM   43013 C  CZ  . ARG   Y  11 63  ? 62.258  -185.376 0.775   1.00 112.50 ? 64  ARG   Y CZ  1 
ATOM   43014 N  NH1 . ARG   Y  11 63  ? 61.394  -185.415 -0.227  1.00 112.76 ? 64  ARG   Y NH1 1 
ATOM   43015 N  NH2 . ARG   Y  11 63  ? 63.160  -186.335 0.888   1.00 115.47 ? 64  ARG   Y NH2 1 
ATOM   43016 N  N   . LEU   Y  11 64  ? 56.659  -183.700 3.067   1.00 101.82 ? 65  LEU   Y N   1 
ATOM   43017 C  CA  . LEU   Y  11 64  ? 55.904  -184.946 3.371   1.00 100.52 ? 65  LEU   Y CA  1 
ATOM   43018 C  C   . LEU   Y  11 64  ? 54.950  -185.276 2.220   1.00 100.03 ? 65  LEU   Y C   1 
ATOM   43019 O  O   . LEU   Y  11 64  ? 54.692  -186.470 2.014   1.00 103.93 ? 65  LEU   Y O   1 
ATOM   43020 C  CB  . LEU   Y  11 64  ? 55.123  -184.792 4.680   1.00 98.15  ? 65  LEU   Y CB  1 
ATOM   43021 C  CG  . LEU   Y  11 64  ? 55.915  -185.029 5.964   1.00 98.27  ? 65  LEU   Y CG  1 
ATOM   43022 C  CD1 . LEU   Y  11 64  ? 55.092  -184.631 7.179   1.00 97.48  ? 65  LEU   Y CD1 1 
ATOM   43023 C  CD2 . LEU   Y  11 64  ? 56.360  -186.478 6.079   1.00 99.63  ? 65  LEU   Y CD2 1 
ATOM   43024 N  N   . HIS   Y  11 65  ? 54.424  -184.268 1.517   1.00 100.56 ? 66  HIS   Y N   1 
ATOM   43025 C  CA  . HIS   Y  11 65  ? 53.550  -184.465 0.330   1.00 101.76 ? 66  HIS   Y CA  1 
ATOM   43026 C  C   . HIS   Y  11 65  ? 54.347  -185.162 -0.779  1.00 102.33 ? 66  HIS   Y C   1 
ATOM   43027 O  O   . HIS   Y  11 65  ? 53.823  -186.137 -1.337  1.00 103.45 ? 66  HIS   Y O   1 
ATOM   43028 C  CB  . HIS   Y  11 65  ? 52.939  -183.147 -0.166  1.00 101.06 ? 66  HIS   Y CB  1 
ATOM   43029 C  CG  . HIS   Y  11 65  ? 52.202  -183.293 -1.457  1.00 100.65 ? 66  HIS   Y CG  1 
ATOM   43030 N  ND1 . HIS   Y  11 65  ? 50.837  -183.503 -1.518  1.00 96.10  ? 66  HIS   Y ND1 1 
ATOM   43031 C  CD2 . HIS   Y  11 65  ? 52.640  -183.279 -2.736  1.00 102.31 ? 66  HIS   Y CD2 1 
ATOM   43032 C  CE1 . HIS   Y  11 65  ? 50.466  -183.600 -2.780  1.00 96.16  ? 66  HIS   Y CE1 1 
ATOM   43033 N  NE2 . HIS   Y  11 65  ? 51.554  -183.467 -3.547  1.00 99.78  ? 66  HIS   Y NE2 1 
ATOM   43034 N  N   . GLU   Y  11 66  ? 55.558  -184.682 -1.086  1.00 106.79 ? 67  GLU   Y N   1 
ATOM   43035 C  CA  . GLU   Y  11 66  ? 56.370  -185.187 -2.229  1.00 112.95 ? 67  GLU   Y CA  1 
ATOM   43036 C  C   . GLU   Y  11 66  ? 56.971  -186.559 -1.881  1.00 114.06 ? 67  GLU   Y C   1 
ATOM   43037 O  O   . GLU   Y  11 66  ? 57.263  -187.315 -2.829  1.00 114.61 ? 67  GLU   Y O   1 
ATOM   43038 C  CB  . GLU   Y  11 66  ? 57.413  -184.160 -2.689  1.00 120.18 ? 67  GLU   Y CB  1 
ATOM   43039 C  CG  . GLU   Y  11 66  ? 58.568  -183.918 -1.731  1.00 124.99 ? 67  GLU   Y CG  1 
ATOM   43040 C  CD  . GLU   Y  11 66  ? 59.540  -182.838 -2.188  1.00 130.87 ? 67  GLU   Y CD  1 
ATOM   43041 O  OE1 . GLU   Y  11 66  ? 59.099  -181.679 -2.373  1.00 128.56 ? 67  GLU   Y OE1 1 
ATOM   43042 O  OE2 . GLU   Y  11 66  ? 60.738  -183.154 -2.368  1.00 137.69 ? 67  GLU   Y OE2 1 
ATOM   43043 N  N   . LEU   Y  11 67  ? 57.131  -186.888 -0.593  1.00 112.96 ? 68  LEU   Y N   1 
ATOM   43044 C  CA  . LEU   Y  11 67  ? 57.537  -188.252 -0.145  1.00 114.82 ? 68  LEU   Y CA  1 
ATOM   43045 C  C   . LEU   Y  11 67  ? 56.366  -189.218 -0.366  1.00 110.72 ? 68  LEU   Y C   1 
ATOM   43046 O  O   . LEU   Y  11 67  ? 56.601  -190.311 -0.917  1.00 108.68 ? 68  LEU   Y O   1 
ATOM   43047 C  CB  . LEU   Y  11 67  ? 57.965  -188.234 1.328   1.00 115.23 ? 68  LEU   Y CB  1 
ATOM   43048 C  CG  . LEU   Y  11 67  ? 59.416  -187.834 1.600   1.00 117.68 ? 68  LEU   Y CG  1 
ATOM   43049 C  CD1 . LEU   Y  11 67  ? 59.629  -187.530 3.077   1.00 118.44 ? 68  LEU   Y CD1 1 
ATOM   43050 C  CD2 . LEU   Y  11 67  ? 60.382  -188.916 1.138   1.00 119.84 ? 68  LEU   Y CD2 1 
ATOM   43051 N  N   . ARG   Y  11 68  ? 55.155  -188.816 0.038   1.00 108.39 ? 69  ARG   Y N   1 
ATOM   43052 C  CA  . ARG   Y  11 68  ? 53.937  -189.673 0.026   1.00 108.48 ? 69  ARG   Y CA  1 
ATOM   43053 C  C   . ARG   Y  11 68  ? 53.375  -189.790 -1.397  1.00 108.90 ? 69  ARG   Y C   1 
ATOM   43054 O  O   . ARG   Y  11 68  ? 52.923  -190.893 -1.747  1.00 112.99 ? 69  ARG   Y O   1 
ATOM   43055 C  CB  . ARG   Y  11 68  ? 52.871  -189.130 0.985   1.00 108.03 ? 69  ARG   Y CB  1 
ATOM   43056 C  CG  . ARG   Y  11 68  ? 53.147  -189.418 2.455   1.00 110.39 ? 69  ARG   Y CG  1 
ATOM   43057 C  CD  . ARG   Y  11 68  ? 51.960  -189.091 3.344   1.00 110.19 ? 69  ARG   Y CD  1 
ATOM   43058 N  NE  . ARG   Y  11 68  ? 51.869  -187.678 3.705   1.00 108.90 ? 69  ARG   Y NE  1 
ATOM   43059 C  CZ  . ARG   Y  11 68  ? 52.114  -187.167 4.913   1.00 109.71 ? 69  ARG   Y CZ  1 
ATOM   43060 N  NH1 . ARG   Y  11 68  ? 52.478  -187.942 5.921   1.00 111.76 ? 69  ARG   Y NH1 1 
ATOM   43061 N  NH2 . ARG   Y  11 68  ? 51.988  -185.866 5.113   1.00 110.43 ? 69  ARG   Y NH2 1 
ATOM   43062 N  N   . GLU   Y  11 69  ? 53.391  -188.708 -2.183  1.00 106.85 ? 70  GLU   Y N   1 
ATOM   43063 C  CA  . GLU   Y  11 69  ? 52.724  -188.640 -3.515  1.00 106.89 ? 70  GLU   Y CA  1 
ATOM   43064 C  C   . GLU   Y  11 69  ? 53.743  -188.722 -4.658  1.00 106.57 ? 70  GLU   Y C   1 
ATOM   43065 O  O   . GLU   Y  11 69  ? 53.295  -188.756 -5.820  1.00 104.85 ? 70  GLU   Y O   1 
ATOM   43066 C  CB  . GLU   Y  11 69  ? 51.896  -187.358 -3.633  1.00 104.94 ? 70  GLU   Y CB  1 
ATOM   43067 C  CG  . GLU   Y  11 69  ? 50.855  -187.199 -2.537  1.00 103.36 ? 70  GLU   Y CG  1 
ATOM   43068 C  CD  . GLU   Y  11 69  ? 49.978  -188.419 -2.313  1.00 104.32 ? 70  GLU   Y CD  1 
ATOM   43069 O  OE1 . GLU   Y  11 69  ? 49.618  -189.075 -3.309  1.00 105.34 ? 70  GLU   Y OE1 1 
ATOM   43070 O  OE2 . GLU   Y  11 69  ? 49.666  -188.714 -1.142  1.00 103.60 ? 70  GLU   Y OE2 1 
ATOM   43071 N  N   . LYS   Y  11 70  ? 55.047  -188.761 -4.356  1.00 109.95 ? 71  LYS   Y N   1 
ATOM   43072 C  CA  . LYS   Y  11 70  ? 56.137  -188.875 -5.365  1.00 117.09 ? 71  LYS   Y CA  1 
ATOM   43073 C  C   . LYS   Y  11 70  ? 55.941  -187.803 -6.445  1.00 117.55 ? 71  LYS   Y C   1 
ATOM   43074 O  O   . LYS   Y  11 70  ? 55.947  -188.155 -7.640  1.00 118.85 ? 71  LYS   Y O   1 
ATOM   43075 C  CB  . LYS   Y  11 70  ? 56.149  -190.282 -5.977  1.00 120.44 ? 71  LYS   Y CB  1 
ATOM   43076 C  CG  . LYS   Y  11 70  ? 56.622  -191.397 -5.053  1.00 121.89 ? 71  LYS   Y CG  1 
ATOM   43077 C  CD  . LYS   Y  11 70  ? 56.496  -192.773 -5.668  1.00 126.48 ? 71  LYS   Y CD  1 
ATOM   43078 C  CE  . LYS   Y  11 70  ? 57.257  -193.836 -4.904  1.00 131.81 ? 71  LYS   Y CE  1 
ATOM   43079 N  NZ  . LYS   Y  11 70  ? 57.321  -195.116 -5.650  1.00 136.09 ? 71  LYS   Y NZ  1 
ATOM   43080 N  N   . GLU   Y  11 71  ? 55.766  -186.544 -6.034  1.00 117.42 ? 72  GLU   Y N   1 
ATOM   43081 C  CA  . GLU   Y  11 71  ? 55.420  -185.404 -6.926  1.00 121.42 ? 72  GLU   Y CA  1 
ATOM   43082 C  C   . GLU   Y  11 71  ? 55.423  -184.108 -6.109  1.00 119.83 ? 72  GLU   Y C   1 
ATOM   43083 O  O   . GLU   Y  11 71  ? 54.858  -184.121 -4.999  1.00 117.91 ? 72  GLU   Y O   1 
ATOM   43084 C  CB  . GLU   Y  11 71  ? 54.042  -185.626 -7.552  1.00 124.24 ? 72  GLU   Y CB  1 
ATOM   43085 C  CG  . GLU   Y  11 71  ? 53.631  -184.548 -8.538  1.00 127.55 ? 72  GLU   Y CG  1 
ATOM   43086 C  CD  . GLU   Y  11 71  ? 52.270  -184.779 -9.172  1.00 132.62 ? 72  GLU   Y CD  1 
ATOM   43087 O  OE1 . GLU   Y  11 71  ? 52.086  -185.840 -9.801  1.00 139.27 ? 72  GLU   Y OE1 1 
ATOM   43088 O  OE2 . GLU   Y  11 71  ? 51.395  -183.903 -9.026  1.00 135.09 ? 72  GLU   Y OE2 1 
ATOM   43089 N  N   . ARG   Y  11 72  ? 56.008  -183.032 -6.646  1.00 122.28 ? 73  ARG   Y N   1 
ATOM   43090 C  CA  . ARG   Y  11 72  ? 56.109  -181.722 -5.944  1.00 118.05 ? 73  ARG   Y CA  1 
ATOM   43091 C  C   . ARG   Y  11 72  ? 54.706  -181.138 -5.767  1.00 109.11 ? 73  ARG   Y C   1 
ATOM   43092 O  O   . ARG   Y  11 72  ? 53.905  -181.217 -6.718  1.00 105.98 ? 73  ARG   Y O   1 
ATOM   43093 C  CB  . ARG   Y  11 72  ? 57.025  -180.745 -6.687  1.00 124.87 ? 73  ARG   Y CB  1 
ATOM   43094 C  CG  . ARG   Y  11 72  ? 58.415  -180.637 -6.075  1.00 132.14 ? 73  ARG   Y CG  1 
ATOM   43095 C  CD  . ARG   Y  11 72  ? 59.406  -179.910 -6.964  1.00 141.75 ? 73  ARG   Y CD  1 
ATOM   43096 N  NE  . ARG   Y  11 72  ? 58.797  -178.802 -7.698  1.00 147.50 ? 73  ARG   Y NE  1 
ATOM   43097 C  CZ  . ARG   Y  11 72  ? 58.495  -178.799 -8.999  1.00 153.90 ? 73  ARG   Y CZ  1 
ATOM   43098 N  NH1 . ARG   Y  11 72  ? 58.748  -179.851 -9.763  1.00 162.09 ? 73  ARG   Y NH1 1 
ATOM   43099 N  NH2 . ARG   Y  11 72  ? 57.941  -177.726 -9.537  1.00 149.54 ? 73  ARG   Y NH2 1 
ATOM   43100 N  N   . ILE   Y  11 73  ? 54.434  -180.586 -4.583  1.00 103.17 ? 74  ILE   Y N   1 
ATOM   43101 C  CA  . ILE   Y  11 73  ? 53.103  -180.031 -4.204  1.00 102.84 ? 74  ILE   Y CA  1 
ATOM   43102 C  C   . ILE   Y  11 73  ? 52.789  -178.836 -5.114  1.00 100.89 ? 74  ILE   Y C   1 
ATOM   43103 O  O   . ILE   Y  11 73  ? 53.731  -178.106 -5.486  1.00 101.15 ? 74  ILE   Y O   1 
ATOM   43104 C  CB  . ILE   Y  11 73  ? 53.051  -179.656 -2.708  1.00 101.74 ? 74  ILE   Y CB  1 
ATOM   43105 C  CG1 . ILE   Y  11 73  ? 51.623  -179.314 -2.276  1.00 102.03 ? 74  ILE   Y CG1 1 
ATOM   43106 C  CG2 . ILE   Y  11 73  ? 54.026  -178.531 -2.375  1.00 102.36 ? 74  ILE   Y CG2 1 
ATOM   43107 C  CD1 . ILE   Y  11 73  ? 51.386  -179.402 -0.787  1.00 102.27 ? 74  ILE   Y CD1 1 
ATOM   43108 N  N   . SER   Y  11 74  ? 51.511  -178.666 -5.466  1.00 101.55 ? 75  SER   Y N   1 
ATOM   43109 C  CA  . SER   Y  11 74  ? 50.985  -177.508 -6.236  1.00 102.69 ? 75  SER   Y CA  1 
ATOM   43110 C  C   . SER   Y  11 74  ? 50.976  -176.270 -5.336  1.00 101.79 ? 75  SER   Y C   1 
ATOM   43111 O  O   . SER   Y  11 74  ? 50.774  -176.421 -4.114  1.00 102.98 ? 75  SER   Y O   1 
ATOM   43112 C  CB  . SER   Y  11 74  ? 49.611  -177.785 -6.795  1.00 100.69 ? 75  SER   Y CB  1 
ATOM   43113 O  OG  . SER   Y  11 74  ? 48.659  -177.944 -5.754  1.00 96.86  ? 75  SER   Y OG  1 
ATOM   43114 N  N   . VAL   Y  11 75  ? 51.173  -175.090 -5.927  1.00 101.79 ? 76  VAL   Y N   1 
ATOM   43115 C  CA  . VAL   Y  11 75  ? 51.177  -173.784 -5.205  1.00 99.31  ? 76  VAL   Y CA  1 
ATOM   43116 C  C   . VAL   Y  11 75  ? 49.818  -173.623 -4.513  1.00 93.30  ? 76  VAL   Y C   1 
ATOM   43117 O  O   . VAL   Y  11 75  ? 49.794  -173.103 -3.386  1.00 88.81  ? 76  VAL   Y O   1 
ATOM   43118 C  CB  . VAL   Y  11 75  ? 51.487  -172.604 -6.148  1.00 102.73 ? 76  VAL   Y CB  1 
ATOM   43119 C  CG1 . VAL   Y  11 75  ? 51.563  -171.288 -5.391  1.00 103.96 ? 76  VAL   Y CG1 1 
ATOM   43120 C  CG2 . VAL   Y  11 75  ? 52.767  -172.822 -6.944  1.00 105.43 ? 76  VAL   Y CG2 1 
ATOM   43121 N  N   . ALA   Y  11 76  ? 48.738  -174.080 -5.158  1.00 94.14  ? 77  ALA   Y N   1 
ATOM   43122 C  CA  . ALA   Y  11 76  ? 47.350  -174.021 -4.643  1.00 95.98  ? 77  ALA   Y CA  1 
ATOM   43123 C  C   . ALA   Y  11 76  ? 47.227  -174.848 -3.359  1.00 96.38  ? 77  ALA   Y C   1 
ATOM   43124 O  O   . ALA   Y  11 76  ? 46.674  -174.323 -2.374  1.00 99.75  ? 77  ALA   Y O   1 
ATOM   43125 C  CB  . ALA   Y  11 76  ? 46.380  -174.505 -5.693  1.00 98.44  ? 77  ALA   Y CB  1 
ATOM   43126 N  N   . ALA   Y  11 77  ? 47.717  -176.091 -3.374  1.00 96.79  ? 78  ALA   Y N   1 
ATOM   43127 C  CA  . ALA   Y  11 77  ? 47.628  -177.044 -2.243  1.00 96.46  ? 78  ALA   Y CA  1 
ATOM   43128 C  C   . ALA   Y  11 77  ? 48.505  -176.559 -1.079  1.00 92.72  ? 78  ALA   Y C   1 
ATOM   43129 O  O   . ALA   Y  11 77  ? 48.041  -176.625 0.078   1.00 91.87  ? 78  ALA   Y O   1 
ATOM   43130 C  CB  . ALA   Y  11 77  ? 48.011  -178.432 -2.699  1.00 98.18  ? 78  ALA   Y CB  1 
ATOM   43131 N  N   . ALA   Y  11 78  ? 49.718  -176.079 -1.372  1.00 90.22  ? 79  ALA   Y N   1 
ATOM   43132 C  CA  . ALA   Y  11 78  ? 50.678  -175.566 -0.368  1.00 90.28  ? 79  ALA   Y CA  1 
ATOM   43133 C  C   . ALA   Y  11 78  ? 50.041  -174.387 0.379   1.00 89.78  ? 79  ALA   Y C   1 
ATOM   43134 O  O   . ALA   Y  11 78  ? 50.002  -174.424 1.625   1.00 91.60  ? 79  ALA   Y O   1 
ATOM   43135 C  CB  . ALA   Y  11 78  ? 51.976  -175.176 -1.033  1.00 89.79  ? 79  ALA   Y CB  1 
ATOM   43136 N  N   . SER   Y  11 79  ? 49.537  -173.394 -0.362  1.00 88.93  ? 80  SER   Y N   1 
ATOM   43137 C  CA  . SER   Y  11 79  ? 48.879  -172.176 0.181   1.00 87.25  ? 80  SER   Y CA  1 
ATOM   43138 C  C   . SER   Y  11 79  ? 47.673  -172.563 1.041   1.00 85.17  ? 80  SER   Y C   1 
ATOM   43139 O  O   . SER   Y  11 79  ? 47.416  -171.866 2.040   1.00 81.01  ? 80  SER   Y O   1 
ATOM   43140 C  CB  . SER   Y  11 79  ? 48.459  -171.240 -0.920  1.00 87.49  ? 80  SER   Y CB  1 
ATOM   43141 O  OG  . SER   Y  11 79  ? 47.465  -171.839 -1.740  1.00 88.05  ? 80  SER   Y OG  1 
ATOM   43142 N  N   . LYS   Y  11 80  ? 46.954  -173.623 0.658   1.00 87.15  ? 81  LYS   Y N   1 
ATOM   43143 C  CA  . LYS   Y  11 80  ? 45.701  -174.046 1.336   1.00 86.48  ? 81  LYS   Y CA  1 
ATOM   43144 C  C   . LYS   Y  11 80  ? 46.025  -174.825 2.613   1.00 85.22  ? 81  LYS   Y C   1 
ATOM   43145 O  O   . LYS   Y  11 80  ? 45.176  -174.813 3.522   1.00 84.59  ? 81  LYS   Y O   1 
ATOM   43146 C  CB  . LYS   Y  11 80  ? 44.806  -174.879 0.417   1.00 86.95  ? 81  LYS   Y CB  1 
ATOM   43147 C  CG  . LYS   Y  11 80  ? 43.337  -174.857 0.813   1.00 87.43  ? 81  LYS   Y CG  1 
ATOM   43148 C  CD  . LYS   Y  11 80  ? 42.408  -175.264 -0.300  1.00 90.20  ? 81  LYS   Y CD  1 
ATOM   43149 C  CE  . LYS   Y  11 80  ? 40.970  -174.881 -0.030  1.00 91.61  ? 81  LYS   Y CE  1 
ATOM   43150 N  NZ  . LYS   Y  11 80  ? 40.086  -175.307 -1.140  1.00 93.60  ? 81  LYS   Y NZ  1 
ATOM   43151 N  N   . ILE   Y  11 81  ? 47.185  -175.485 2.681   1.00 87.05  ? 82  ILE   Y N   1 
ATOM   43152 C  CA  . ILE   Y  11 81  ? 47.683  -176.097 3.950   1.00 90.67  ? 82  ILE   Y CA  1 
ATOM   43153 C  C   . ILE   Y  11 81  ? 47.819  -174.971 4.983   1.00 89.61  ? 82  ILE   Y C   1 
ATOM   43154 O  O   . ILE   Y  11 81  ? 47.260  -175.117 6.089   1.00 93.42  ? 82  ILE   Y O   1 
ATOM   43155 C  CB  . ILE   Y  11 81  ? 49.001  -176.876 3.747   1.00 92.96  ? 82  ILE   Y CB  1 
ATOM   43156 C  CG1 . ILE   Y  11 81  ? 48.751  -178.236 3.088   1.00 93.05  ? 82  ILE   Y CG1 1 
ATOM   43157 C  CG2 . ILE   Y  11 81  ? 49.756  -177.023 5.064   1.00 94.13  ? 82  ILE   Y CG2 1 
ATOM   43158 C  CD1 . ILE   Y  11 81  ? 50.010  -178.983 2.703   1.00 94.97  ? 82  ILE   Y CD1 1 
ATOM   43159 N  N   . LEU   Y  11 82  ? 48.511  -173.885 4.618   1.00 89.66  ? 83  LEU   Y N   1 
ATOM   43160 C  CA  . LEU   Y  11 82  ? 48.777  -172.722 5.508   1.00 87.46  ? 83  LEU   Y CA  1 
ATOM   43161 C  C   . LEU   Y  11 82  ? 47.450  -172.042 5.876   1.00 81.72  ? 83  LEU   Y C   1 
ATOM   43162 O  O   . LEU   Y  11 82  ? 47.247  -171.785 7.074   1.00 77.88  ? 83  LEU   Y O   1 
ATOM   43163 C  CB  . LEU   Y  11 82  ? 49.741  -171.751 4.814   1.00 89.42  ? 83  LEU   Y CB  1 
ATOM   43164 C  CG  . LEU   Y  11 82  ? 50.161  -170.530 5.635   1.00 89.70  ? 83  LEU   Y CG  1 
ATOM   43165 C  CD1 . LEU   Y  11 82  ? 50.940  -170.938 6.877   1.00 92.47  ? 83  LEU   Y CD1 1 
ATOM   43166 C  CD2 . LEU   Y  11 82  ? 50.982  -169.562 4.797   1.00 90.85  ? 83  LEU   Y CD2 1 
ATOM   43167 N  N   . SER   Y  11 83  ? 46.579  -171.775 4.894   1.00 80.19  ? 84  SER   Y N   1 
ATOM   43168 C  CA  . SER   Y  11 83  ? 45.296  -171.043 5.086   1.00 80.67  ? 84  SER   Y CA  1 
ATOM   43169 C  C   . SER   Y  11 83  ? 44.349  -171.851 5.983   1.00 81.50  ? 84  SER   Y C   1 
ATOM   43170 O  O   . SER   Y  11 83  ? 43.642  -171.230 6.799   1.00 81.02  ? 84  SER   Y O   1 
ATOM   43171 C  CB  . SER   Y  11 83  ? 44.636  -170.698 3.773   1.00 82.07  ? 84  SER   Y CB  1 
ATOM   43172 O  OG  . SER   Y  11 83  ? 44.009  -171.835 3.200   1.00 81.52  ? 84  SER   Y OG  1 
ATOM   43173 N  N   . ASN   Y  11 84  ? 44.317  -173.177 5.820   1.00 82.72  ? 85  ASN   Y N   1 
ATOM   43174 C  CA  . ASN   Y  11 84  ? 43.474  -174.093 6.638   1.00 84.06  ? 85  ASN   Y CA  1 
ATOM   43175 C  C   . ASN   Y  11 84  ? 44.045  -174.187 8.057   1.00 84.29  ? 85  ASN   Y C   1 
ATOM   43176 O  O   . ASN   Y  11 84  ? 43.238  -174.355 8.994   1.00 84.16  ? 85  ASN   Y O   1 
ATOM   43177 C  CB  . ASN   Y  11 84  ? 43.345  -175.486 6.017   1.00 84.74  ? 85  ASN   Y CB  1 
ATOM   43178 C  CG  . ASN   Y  11 84  ? 42.390  -175.569 4.840   1.00 88.00  ? 85  ASN   Y CG  1 
ATOM   43179 O  OD1 . ASN   Y  11 84  ? 42.276  -176.622 4.215   1.00 86.52  ? 85  ASN   Y OD1 1 
ATOM   43180 N  ND2 . ASN   Y  11 84  ? 41.694  -174.488 4.520   1.00 90.35  ? 85  ASN   Y ND2 1 
ATOM   43181 N  N   . LEU   Y  11 85  ? 45.372  -174.085 8.205   1.00 88.49  ? 86  LEU   Y N   1 
ATOM   43182 C  CA  . LEU   Y  11 85  ? 46.068  -174.106 9.522   1.00 90.15  ? 86  LEU   Y CA  1 
ATOM   43183 C  C   . LEU   Y  11 85  ? 45.670  -172.857 10.318  1.00 88.50  ? 86  LEU   Y C   1 
ATOM   43184 O  O   . LEU   Y  11 85  ? 45.204  -173.019 11.460  1.00 89.80  ? 86  LEU   Y O   1 
ATOM   43185 C  CB  . LEU   Y  11 85  ? 47.586  -174.185 9.303   1.00 90.54  ? 86  LEU   Y CB  1 
ATOM   43186 C  CG  . LEU   Y  11 85  ? 48.464  -174.235 10.556  1.00 90.89  ? 86  LEU   Y CG  1 
ATOM   43187 C  CD1 . LEU   Y  11 85  ? 48.633  -172.854 11.180  1.00 93.10  ? 86  LEU   Y CD1 1 
ATOM   43188 C  CD2 . LEU   Y  11 85  ? 47.933  -175.224 11.582  1.00 89.79  ? 86  LEU   Y CD2 1 
ATOM   43189 N  N   . VAL   Y  11 86  ? 45.842  -171.664 9.736   1.00 89.40  ? 87  VAL   Y N   1 
ATOM   43190 C  CA  . VAL   Y  11 86  ? 45.589  -170.356 10.419  1.00 88.34  ? 87  VAL   Y CA  1 
ATOM   43191 C  C   . VAL   Y  11 86  ? 44.085  -170.192 10.686  1.00 87.77  ? 87  VAL   Y C   1 
ATOM   43192 O  O   . VAL   Y  11 86  ? 43.746  -169.542 11.697  1.00 90.07  ? 87  VAL   Y O   1 
ATOM   43193 C  CB  . VAL   Y  11 86  ? 46.163  -169.150 9.645   1.00 88.32  ? 87  VAL   Y CB  1 
ATOM   43194 C  CG1 . VAL   Y  11 86  ? 47.679  -169.219 9.530   1.00 88.62  ? 87  VAL   Y CG1 1 
ATOM   43195 C  CG2 . VAL   Y  11 86  ? 45.530  -168.971 8.274   1.00 87.67  ? 87  VAL   Y CG2 1 
ATOM   43196 N  N   . TYR   Y  11 87  ? 43.216  -170.751 9.836   1.00 83.97  ? 88  TYR   Y N   1 
ATOM   43197 C  CA  . TYR   Y  11 87  ? 41.740  -170.675 10.010  1.00 82.41  ? 88  TYR   Y CA  1 
ATOM   43198 C  C   . TYR   Y  11 87  ? 41.329  -171.448 11.269  1.00 82.75  ? 88  TYR   Y C   1 
ATOM   43199 O  O   . TYR   Y  11 87  ? 40.332  -171.061 11.911  1.00 77.85  ? 88  TYR   Y O   1 
ATOM   43200 C  CB  . TYR   Y  11 87  ? 40.973  -171.206 8.797   1.00 80.52  ? 88  TYR   Y CB  1 
ATOM   43201 C  CG  . TYR   Y  11 87  ? 39.484  -171.014 8.932   1.00 80.78  ? 88  TYR   Y CG  1 
ATOM   43202 C  CD1 . TYR   Y  11 87  ? 38.917  -169.760 8.795   1.00 81.44  ? 88  TYR   Y CD1 1 
ATOM   43203 C  CD2 . TYR   Y  11 87  ? 38.649  -172.067 9.267   1.00 80.69  ? 88  TYR   Y CD2 1 
ATOM   43204 C  CE1 . TYR   Y  11 87  ? 37.554  -169.561 8.944   1.00 83.93  ? 88  TYR   Y CE1 1 
ATOM   43205 C  CE2 . TYR   Y  11 87  ? 37.284  -171.887 9.420   1.00 82.72  ? 88  TYR   Y CE2 1 
ATOM   43206 C  CZ  . TYR   Y  11 87  ? 36.732  -170.630 9.254   1.00 83.42  ? 88  TYR   Y CZ  1 
ATOM   43207 O  OH  . TYR   Y  11 87  ? 35.388  -170.449 9.408   1.00 86.48  ? 88  TYR   Y OH  1 
ATOM   43208 N  N   . GLN   Y  11 88  ? 42.064  -172.514 11.598  1.00 85.90  ? 89  GLN   Y N   1 
ATOM   43209 C  CA  . GLN   Y  11 88  ? 41.849  -173.323 12.828  1.00 90.02  ? 89  GLN   Y CA  1 
ATOM   43210 C  C   . GLN   Y  11 88  ? 42.134  -172.462 14.065  1.00 87.53  ? 89  GLN   Y C   1 
ATOM   43211 O  O   . GLN   Y  11 88  ? 41.472  -172.679 15.095  1.00 88.84  ? 89  GLN   Y O   1 
ATOM   43212 C  CB  . GLN   Y  11 88  ? 42.726  -174.576 12.829  1.00 92.84  ? 89  GLN   Y CB  1 
ATOM   43213 C  CG  . GLN   Y  11 88  ? 42.161  -175.716 11.997  1.00 98.85  ? 89  GLN   Y CG  1 
ATOM   43214 C  CD  . GLN   Y  11 88  ? 42.462  -177.052 12.628  1.00 103.65 ? 89  GLN   Y CD  1 
ATOM   43215 O  OE1 . GLN   Y  11 88  ? 43.614  -177.476 12.705  1.00 111.47 ? 89  GLN   Y OE1 1 
ATOM   43216 N  NE2 . GLN   Y  11 88  ? 41.422  -177.724 13.098  1.00 113.42 ? 89  GLN   Y NE2 1 
ATOM   43217 N  N   . TYR   Y  11 89  ? 43.076  -171.521 13.959  1.00 87.34  ? 90  TYR   Y N   1 
ATOM   43218 C  CA  . TYR   Y  11 89  ? 43.493  -170.610 15.058  1.00 88.64  ? 90  TYR   Y CA  1 
ATOM   43219 C  C   . TYR   Y  11 89  ? 42.715  -169.287 15.005  1.00 88.28  ? 90  TYR   Y C   1 
ATOM   43220 O  O   . TYR   Y  11 89  ? 42.987  -168.424 15.858  1.00 87.84  ? 90  TYR   Y O   1 
ATOM   43221 C  CB  . TYR   Y  11 89  ? 44.996  -170.341 14.977  1.00 86.11  ? 90  TYR   Y CB  1 
ATOM   43222 C  CG  . TYR   Y  11 89  ? 45.867  -171.474 15.454  1.00 86.37  ? 90  TYR   Y CG  1 
ATOM   43223 C  CD1 . TYR   Y  11 89  ? 46.320  -171.517 16.762  1.00 87.61  ? 90  TYR   Y CD1 1 
ATOM   43224 C  CD2 . TYR   Y  11 89  ? 46.248  -172.498 14.602  1.00 86.38  ? 90  TYR   Y CD2 1 
ATOM   43225 C  CE1 . TYR   Y  11 89  ? 47.125  -172.549 17.213  1.00 87.36  ? 90  TYR   Y CE1 1 
ATOM   43226 C  CE2 . TYR   Y  11 89  ? 47.055  -173.537 15.036  1.00 85.73  ? 90  TYR   Y CE2 1 
ATOM   43227 C  CZ  . TYR   Y  11 89  ? 47.493  -173.561 16.347  1.00 85.84  ? 90  TYR   Y CZ  1 
ATOM   43228 O  OH  . TYR   Y  11 89  ? 48.286  -174.571 16.799  1.00 89.42  ? 90  TYR   Y OH  1 
ATOM   43229 N  N   . LYS   Y  11 90  ? 41.782  -169.124 14.057  1.00 89.16  ? 91  LYS   Y N   1 
ATOM   43230 C  CA  . LYS   Y  11 90  ? 41.084  -167.831 13.811  1.00 90.83  ? 91  LYS   Y CA  1 
ATOM   43231 C  C   . LYS   Y  11 90  ? 40.455  -167.342 15.121  1.00 93.55  ? 91  LYS   Y C   1 
ATOM   43232 O  O   . LYS   Y  11 90  ? 39.670  -168.102 15.718  1.00 95.36  ? 91  LYS   Y O   1 
ATOM   43233 C  CB  . LYS   Y  11 90  ? 40.024  -167.952 12.711  1.00 92.57  ? 91  LYS   Y CB  1 
ATOM   43234 C  CG  . LYS   Y  11 90  ? 39.435  -166.620 12.260  1.00 95.00  ? 91  LYS   Y CG  1 
ATOM   43235 C  CD  . LYS   Y  11 90  ? 38.367  -166.729 11.193  1.00 97.61  ? 91  LYS   Y CD  1 
ATOM   43236 C  CE  . LYS   Y  11 90  ? 37.584  -165.444 11.008  1.00 98.80  ? 91  LYS   Y CE  1 
ATOM   43237 N  NZ  . LYS   Y  11 90  ? 38.420  -164.363 10.433  1.00 98.75  ? 91  LYS   Y NZ  1 
ATOM   43238 N  N   . GLY   Y  11 91  ? 40.805  -166.121 15.545  1.00 94.66  ? 92  GLY   Y N   1 
ATOM   43239 C  CA  . GLY   Y  11 91  ? 40.323  -165.485 16.786  1.00 95.41  ? 92  GLY   Y CA  1 
ATOM   43240 C  C   . GLY   Y  11 91  ? 41.349  -165.552 17.909  1.00 94.30  ? 92  GLY   Y C   1 
ATOM   43241 O  O   . GLY   Y  11 91  ? 41.270  -164.706 18.825  1.00 92.59  ? 92  GLY   Y O   1 
ATOM   43242 N  N   . ALA   Y  11 92  ? 42.278  -166.513 17.847  1.00 91.63  ? 93  ALA   Y N   1 
ATOM   43243 C  CA  . ALA   Y  11 92  ? 43.307  -166.777 18.883  1.00 89.11  ? 93  ALA   Y CA  1 
ATOM   43244 C  C   . ALA   Y  11 92  ? 44.304  -165.615 18.969  1.00 89.62  ? 93  ALA   Y C   1 
ATOM   43245 O  O   . ALA   Y  11 92  ? 44.922  -165.460 20.040  1.00 88.63  ? 93  ALA   Y O   1 
ATOM   43246 C  CB  . ALA   Y  11 92  ? 44.023  -168.070 18.592  1.00 87.83  ? 93  ALA   Y CB  1 
ATOM   43247 N  N   . GLY   Y  11 93  ? 44.479  -164.858 17.881  1.00 88.38  ? 94  GLY   Y N   1 
ATOM   43248 C  CA  . GLY   Y  11 93  ? 45.315  -163.642 17.858  1.00 88.14  ? 94  GLY   Y CA  1 
ATOM   43249 C  C   . GLY   Y  11 93  ? 46.579  -163.800 17.033  1.00 87.03  ? 94  GLY   Y C   1 
ATOM   43250 O  O   . GLY   Y  11 93  ? 47.452  -162.924 17.150  1.00 88.80  ? 94  GLY   Y O   1 
ATOM   43251 N  N   . LEU   Y  11 94  ? 46.694  -164.858 16.227  1.00 84.94  ? 95  LEU   Y N   1 
ATOM   43252 C  CA  . LEU   Y  11 94  ? 47.786  -164.979 15.226  1.00 86.81  ? 95  LEU   Y CA  1 
ATOM   43253 C  C   . LEU   Y  11 94  ? 47.710  -163.767 14.295  1.00 86.00  ? 95  LEU   Y C   1 
ATOM   43254 O  O   . LEU   Y  11 94  ? 46.591  -163.440 13.855  1.00 87.48  ? 95  LEU   Y O   1 
ATOM   43255 C  CB  . LEU   Y  11 94  ? 47.636  -166.275 14.423  1.00 88.18  ? 95  LEU   Y CB  1 
ATOM   43256 C  CG  . LEU   Y  11 94  ? 48.142  -167.552 15.092  1.00 89.65  ? 95  LEU   Y CG  1 
ATOM   43257 C  CD1 . LEU   Y  11 94  ? 47.891  -168.752 14.194  1.00 89.66  ? 95  LEU   Y CD1 1 
ATOM   43258 C  CD2 . LEU   Y  11 94  ? 49.621  -167.455 15.433  1.00 91.85  ? 95  LEU   Y CD2 1 
ATOM   43259 N  N   . SER   Y  11 95  ? 48.846  -163.122 14.026  1.00 85.55  ? 96  SER   Y N   1 
ATOM   43260 C  CA  . SER   Y  11 95  ? 48.965  -161.983 13.081  1.00 87.02  ? 96  SER   Y CA  1 
ATOM   43261 C  C   . SER   Y  11 95  ? 50.002  -162.331 12.008  1.00 86.98  ? 96  SER   Y C   1 
ATOM   43262 O  O   . SER   Y  11 95  ? 51.209  -162.323 12.331  1.00 85.42  ? 96  SER   Y O   1 
ATOM   43263 C  CB  . SER   Y  11 95  ? 49.301  -160.702 13.809  1.00 87.56  ? 96  SER   Y CB  1 
ATOM   43264 O  OG  . SER   Y  11 95  ? 49.733  -159.693 12.908  1.00 87.60  ? 96  SER   Y OG  1 
ATOM   43265 N  N   . MET   Y  11 96  ? 49.540  -162.656 10.793  1.00 85.91  ? 97  MET   Y N   1 
ATOM   43266 C  CA  . MET   Y  11 96  ? 50.405  -162.868 9.600   1.00 87.36  ? 97  MET   Y CA  1 
ATOM   43267 C  C   . MET   Y  11 96  ? 49.681  -162.427 8.327   1.00 82.90  ? 97  MET   Y C   1 
ATOM   43268 O  O   . MET   Y  11 96  ? 48.468  -162.677 8.209   1.00 81.16  ? 97  MET   Y O   1 
ATOM   43269 C  CB  . MET   Y  11 96  ? 50.792  -164.330 9.371   1.00 89.23  ? 97  MET   Y CB  1 
ATOM   43270 C  CG  . MET   Y  11 96  ? 50.563  -165.256 10.519  1.00 92.66  ? 97  MET   Y CG  1 
ATOM   43271 S  SD  . MET   Y  11 96  ? 50.637  -166.924 9.846   1.00 95.35  ? 97  MET   Y SD  1 
ATOM   43272 C  CE  . MET   Y  11 96  ? 51.354  -167.765 11.250  1.00 96.17  ? 97  MET   Y CE  1 
ATOM   43273 N  N   . GLY   Y  11 97  ? 50.446  -161.857 7.395   1.00 83.82  ? 98  GLY   Y N   1 
ATOM   43274 C  CA  . GLY   Y  11 97  ? 50.070  -161.660 5.985   1.00 85.64  ? 98  GLY   Y CA  1 
ATOM   43275 C  C   . GLY   Y  11 97  ? 51.180  -162.171 5.091   1.00 88.14  ? 98  GLY   Y C   1 
ATOM   43276 O  O   . GLY   Y  11 97  ? 52.285  -161.612 5.140   1.00 89.49  ? 98  GLY   Y O   1 
ATOM   43277 N  N   . THR   Y  11 98  ? 50.931  -163.237 4.336   1.00 90.60  ? 99  THR   Y N   1 
ATOM   43278 C  CA  . THR   Y  11 98  ? 51.966  -163.888 3.498   1.00 96.22  ? 99  THR   Y CA  1 
ATOM   43279 C  C   . THR   Y  11 98  ? 51.462  -164.071 2.071   1.00 100.10 ? 99  THR   Y C   1 
ATOM   43280 O  O   . THR   Y  11 98  ? 50.239  -164.001 1.835   1.00 100.96 ? 99  THR   Y O   1 
ATOM   43281 C  CB  . THR   Y  11 98  ? 52.387  -165.248 4.062   1.00 96.99  ? 99  THR   Y CB  1 
ATOM   43282 O  OG1 . THR   Y  11 98  ? 51.225  -166.074 4.142   1.00 92.44  ? 99  THR   Y OG1 1 
ATOM   43283 C  CG2 . THR   Y  11 98  ? 53.044  -165.132 5.420   1.00 100.89 ? 99  THR   Y CG2 1 
ATOM   43284 N  N   . MET   Y  11 99  ? 52.416  -164.306 1.176   1.00 105.68 ? 100 MET   Y N   1 
ATOM   43285 C  CA  . MET   Y  11 99  ? 52.200  -164.620 -0.253  1.00 111.50 ? 100 MET   Y CA  1 
ATOM   43286 C  C   . MET   Y  11 99  ? 52.977  -165.897 -0.568  1.00 111.51 ? 100 MET   Y C   1 
ATOM   43287 O  O   . MET   Y  11 99  ? 54.202  -165.920 -0.320  1.00 112.61 ? 100 MET   Y O   1 
ATOM   43288 C  CB  . MET   Y  11 99  ? 52.713  -163.485 -1.139  1.00 116.08 ? 100 MET   Y CB  1 
ATOM   43289 C  CG  . MET   Y  11 99  ? 52.844  -162.152 -0.409  1.00 118.82 ? 100 MET   Y CG  1 
ATOM   43290 S  SD  . MET   Y  11 99  ? 52.692  -160.773 -1.530  1.00 126.16 ? 100 MET   Y SD  1 
ATOM   43291 C  CE  . MET   Y  11 99  ? 51.233  -161.332 -2.403  1.00 128.13 ? 100 MET   Y CE  1 
ATOM   43292 N  N   . ILE   Y  11 100 ? 52.290  -166.927 -1.058  1.00 109.99 ? 101 ILE   Y N   1 
ATOM   43293 C  CA  . ILE   Y  11 100 ? 52.931  -168.200 -1.492  1.00 109.76 ? 101 ILE   Y CA  1 
ATOM   43294 C  C   . ILE   Y  11 100 ? 53.157  -168.118 -3.001  1.00 105.87 ? 101 ILE   Y C   1 
ATOM   43295 O  O   . ILE   Y  11 100 ? 52.162  -168.056 -3.746  1.00 104.37 ? 101 ILE   Y O   1 
ATOM   43296 C  CB  . ILE   Y  11 100 ? 52.083  -169.421 -1.088  1.00 110.35 ? 101 ILE   Y CB  1 
ATOM   43297 C  CG1 . ILE   Y  11 100 ? 51.817  -169.458 0.421   1.00 108.89 ? 101 ILE   Y CG1 1 
ATOM   43298 C  CG2 . ILE   Y  11 100 ? 52.733  -170.702 -1.589  1.00 114.81 ? 101 ILE   Y CG2 1 
ATOM   43299 C  CD1 . ILE   Y  11 100 ? 52.974  -168.987 1.281   1.00 107.13 ? 101 ILE   Y CD1 1 
ATOM   43300 N  N   . CYS   Y  11 101 ? 54.425  -168.113 -3.413  1.00 105.09 ? 102 CYS   Y N   1 
ATOM   43301 C  CA  . CYS   Y  11 101 ? 54.869  -167.896 -4.813  1.00 111.05 ? 102 CYS   Y CA  1 
ATOM   43302 C  C   . CYS   Y  11 101 ? 55.628  -169.133 -5.297  1.00 111.99 ? 102 CYS   Y C   1 
ATOM   43303 O  O   . CYS   Y  11 101 ? 56.452  -169.651 -4.521  1.00 111.90 ? 102 CYS   Y O   1 
ATOM   43304 C  CB  . CYS   Y  11 101 ? 55.764  -166.668 -4.903  1.00 114.58 ? 102 CYS   Y CB  1 
ATOM   43305 S  SG  . CYS   Y  11 101 ? 55.265  -165.338 -3.776  1.00 115.35 ? 102 CYS   Y SG  1 
ATOM   43306 N  N   . GLY   Y  11 102 ? 55.365  -169.580 -6.528  1.00 115.94 ? 103 GLY   Y N   1 
ATOM   43307 C  CA  . GLY   Y  11 102 ? 56.085  -170.715 -7.135  1.00 119.31 ? 103 GLY   Y CA  1 
ATOM   43308 C  C   . GLY   Y  11 102 ? 55.608  -171.051 -8.536  1.00 121.46 ? 103 GLY   Y C   1 
ATOM   43309 O  O   . GLY   Y  11 102 ? 54.563  -170.518 -8.963  1.00 120.26 ? 103 GLY   Y O   1 
ATOM   43310 N  N   . TYR   Y  11 103 ? 56.363  -171.915 -9.219  1.00 126.24 ? 104 TYR   Y N   1 
ATOM   43311 C  CA  . TYR   Y  11 103 ? 56.041  -172.471 -10.556 1.00 131.54 ? 104 TYR   Y CA  1 
ATOM   43312 C  C   . TYR   Y  11 103 ? 55.839  -173.985 -10.445 1.00 129.82 ? 104 TYR   Y C   1 
ATOM   43313 O  O   . TYR   Y  11 103 ? 56.665  -174.665 -9.802  1.00 134.49 ? 104 TYR   Y O   1 
ATOM   43314 C  CB  . TYR   Y  11 103 ? 57.154  -172.172 -11.563 1.00 140.60 ? 104 TYR   Y CB  1 
ATOM   43315 C  CG  . TYR   Y  11 103 ? 56.953  -172.845 -12.896 1.00 150.47 ? 104 TYR   Y CG  1 
ATOM   43316 C  CD1 . TYR   Y  11 103 ? 57.318  -174.169 -13.093 1.00 156.58 ? 104 TYR   Y CD1 1 
ATOM   43317 C  CD2 . TYR   Y  11 103 ? 56.369  -172.170 -13.956 1.00 152.03 ? 104 TYR   Y CD2 1 
ATOM   43318 C  CE1 . TYR   Y  11 103 ? 57.122  -174.801 -14.311 1.00 165.20 ? 104 TYR   Y CE1 1 
ATOM   43319 C  CE2 . TYR   Y  11 103 ? 56.169  -172.786 -15.182 1.00 162.36 ? 104 TYR   Y CE2 1 
ATOM   43320 C  CZ  . TYR   Y  11 103 ? 56.547  -174.107 -15.361 1.00 165.95 ? 104 TYR   Y CZ  1 
ATOM   43321 O  OH  . TYR   Y  11 103 ? 56.357  -174.730 -16.562 1.00 170.19 ? 104 TYR   Y OH  1 
ATOM   43322 N  N   . THR   Y  11 104 ? 54.774  -174.490 -11.070 1.00 122.72 ? 105 THR   Y N   1 
ATOM   43323 C  CA  . THR   Y  11 104 ? 54.560  -175.931 -11.357 1.00 122.50 ? 105 THR   Y CA  1 
ATOM   43324 C  C   . THR   Y  11 104 ? 54.142  -176.076 -12.822 1.00 125.61 ? 105 THR   Y C   1 
ATOM   43325 O  O   . THR   Y  11 104 ? 53.779  -175.054 -13.436 1.00 131.72 ? 105 THR   Y O   1 
ATOM   43326 C  CB  . THR   Y  11 104 ? 53.531  -176.543 -10.400 1.00 117.90 ? 105 THR   Y CB  1 
ATOM   43327 O  OG1 . THR   Y  11 104 ? 52.335  -175.767 -10.470 1.00 111.10 ? 105 THR   Y OG1 1 
ATOM   43328 C  CG2 . THR   Y  11 104 ? 54.021  -176.589 -8.970  1.00 114.81 ? 105 THR   Y CG2 1 
ATOM   43329 N  N   . ARG   Y  11 105 ? 54.200  -177.298 -13.354 1.00 125.67 ? 106 ARG   Y N   1 
ATOM   43330 C  CA  . ARG   Y  11 105 ? 53.812  -177.610 -14.754 1.00 128.57 ? 106 ARG   Y CA  1 
ATOM   43331 C  C   . ARG   Y  11 105 ? 52.311  -177.351 -14.938 1.00 120.83 ? 106 ARG   Y C   1 
ATOM   43332 O  O   . ARG   Y  11 105 ? 51.961  -176.646 -15.902 1.00 119.38 ? 106 ARG   Y O   1 
ATOM   43333 C  CB  . ARG   Y  11 105 ? 54.197  -179.049 -15.108 1.00 132.12 ? 106 ARG   Y CB  1 
ATOM   43334 C  CG  . ARG   Y  11 105 ? 55.398  -179.156 -16.037 1.00 139.92 ? 106 ARG   Y CG  1 
ATOM   43335 C  CD  . ARG   Y  11 105 ? 55.061  -178.728 -17.454 1.00 142.89 ? 106 ARG   Y CD  1 
ATOM   43336 N  NE  . ARG   Y  11 105 ? 55.576  -179.667 -18.442 1.00 147.85 ? 106 ARG   Y NE  1 
ATOM   43337 C  CZ  . ARG   Y  11 105 ? 55.043  -180.857 -18.722 1.00 151.61 ? 106 ARG   Y CZ  1 
ATOM   43338 N  NH1 . ARG   Y  11 105 ? 53.964  -181.285 -18.085 1.00 149.73 ? 106 ARG   Y NH1 1 
ATOM   43339 N  NH2 . ARG   Y  11 105 ? 55.600  -181.625 -19.644 1.00 155.03 ? 106 ARG   Y NH2 1 
ATOM   43340 N  N   . LYS   Y  11 106 ? 51.464  -177.874 -14.043 1.00 118.47 ? 107 LYS   Y N   1 
ATOM   43341 C  CA  . LYS   Y  11 106 ? 49.981  -177.864 -14.202 1.00 120.70 ? 107 LYS   Y CA  1 
ATOM   43342 C  C   . LYS   Y  11 106 ? 49.426  -176.444 -14.008 1.00 116.76 ? 107 LYS   Y C   1 
ATOM   43343 O  O   . LYS   Y  11 106 ? 48.375  -176.155 -14.608 1.00 116.13 ? 107 LYS   Y O   1 
ATOM   43344 C  CB  . LYS   Y  11 106 ? 49.300  -178.875 -13.267 1.00 121.70 ? 107 LYS   Y CB  1 
ATOM   43345 C  CG  . LYS   Y  11 106 ? 49.334  -178.571 -11.772 1.00 120.07 ? 107 LYS   Y CG  1 
ATOM   43346 C  CD  . LYS   Y  11 106 ? 48.028  -178.883 -11.051 1.00 122.30 ? 107 LYS   Y CD  1 
ATOM   43347 C  CE  . LYS   Y  11 106 ? 46.928  -177.883 -11.350 1.00 123.53 ? 107 LYS   Y CE  1 
ATOM   43348 N  NZ  . LYS   Y  11 106 ? 45.709  -178.133 -10.544 1.00 122.47 ? 107 LYS   Y NZ  1 
ATOM   43349 N  N   . GLU   Y  11 107 ? 50.097  -175.597 -13.215 1.00 114.87 ? 108 GLU   Y N   1 
ATOM   43350 C  CA  . GLU   Y  11 107 ? 49.613  -174.240 -12.828 1.00 112.93 ? 108 GLU   Y CA  1 
ATOM   43351 C  C   . GLU   Y  11 107 ? 50.337  -173.138 -13.613 1.00 113.97 ? 108 GLU   Y C   1 
ATOM   43352 O  O   . GLU   Y  11 107 ? 49.686  -172.119 -13.919 1.00 109.84 ? 108 GLU   Y O   1 
ATOM   43353 C  CB  . GLU   Y  11 107 ? 49.845  -173.977 -11.341 1.00 110.97 ? 108 GLU   Y CB  1 
ATOM   43354 C  CG  . GLU   Y  11 107 ? 49.029  -174.858 -10.420 1.00 111.61 ? 108 GLU   Y CG  1 
ATOM   43355 C  CD  . GLU   Y  11 107 ? 49.401  -174.702 -8.958  1.00 112.72 ? 108 GLU   Y CD  1 
ATOM   43356 O  OE1 . GLU   Y  11 107 ? 48.512  -174.359 -8.155  1.00 114.56 ? 108 GLU   Y OE1 1 
ATOM   43357 O  OE2 . GLU   Y  11 107 ? 50.585  -174.921 -8.630  1.00 116.01 ? 108 GLU   Y OE2 1 
ATOM   43358 N  N   . GLY   Y  11 108 ? 51.634  -173.315 -13.888 1.00 116.72 ? 109 GLY   Y N   1 
ATOM   43359 C  CA  . GLY   Y  11 108 ? 52.531  -172.240 -14.356 1.00 118.74 ? 109 GLY   Y CA  1 
ATOM   43360 C  C   . GLY   Y  11 108 ? 52.946  -171.351 -13.187 1.00 117.14 ? 109 GLY   Y C   1 
ATOM   43361 O  O   . GLY   Y  11 108 ? 52.771  -171.741 -12.034 1.00 115.64 ? 109 GLY   Y O   1 
ATOM   43362 N  N   . PRO   Y  11 109 ? 53.506  -170.142 -13.427 1.00 118.22 ? 110 PRO   Y N   1 
ATOM   43363 C  CA  . PRO   Y  11 109 ? 53.791  -169.202 -12.340 1.00 113.26 ? 110 PRO   Y CA  1 
ATOM   43364 C  C   . PRO   Y  11 109 ? 52.501  -168.812 -11.602 1.00 108.31 ? 110 PRO   Y C   1 
ATOM   43365 O  O   . PRO   Y  11 109 ? 51.574  -168.394 -12.260 1.00 108.47 ? 110 PRO   Y O   1 
ATOM   43366 C  CB  . PRO   Y  11 109 ? 54.428  -167.986 -13.032 1.00 112.80 ? 110 PRO   Y CB  1 
ATOM   43367 C  CG  . PRO   Y  11 109 ? 54.050  -168.126 -14.496 1.00 117.54 ? 110 PRO   Y CG  1 
ATOM   43368 C  CD  . PRO   Y  11 109 ? 53.895  -169.613 -14.744 1.00 120.44 ? 110 PRO   Y CD  1 
ATOM   43369 N  N   . THR   Y  11 110 ? 52.460  -168.989 -10.277 1.00 106.28 ? 111 THR   Y N   1 
ATOM   43370 C  CA  . THR   Y  11 110 ? 51.262  -168.751 -9.425  1.00 106.92 ? 111 THR   Y CA  1 
ATOM   43371 C  C   . THR   Y  11 110 ? 51.653  -168.020 -8.134  1.00 102.11 ? 111 THR   Y C   1 
ATOM   43372 O  O   . THR   Y  11 110 ? 52.698  -168.365 -7.548  1.00 99.48  ? 111 THR   Y O   1 
ATOM   43373 C  CB  . THR   Y  11 110 ? 50.555  -170.072 -9.095  1.00 108.12 ? 111 THR   Y CB  1 
ATOM   43374 O  OG1 . THR   Y  11 110 ? 50.322  -170.768 -10.319 1.00 114.67 ? 111 THR   Y OG1 1 
ATOM   43375 C  CG2 . THR   Y  11 110 ? 49.241  -169.877 -8.371  1.00 106.48 ? 111 THR   Y CG2 1 
ATOM   43376 N  N   . ILE   Y  11 111 ? 50.821  -167.062 -7.711  1.00 100.23 ? 112 ILE   Y N   1 
ATOM   43377 C  CA  . ILE   Y  11 111 ? 50.933  -166.329 -6.413  1.00 98.64  ? 112 ILE   Y CA  1 
ATOM   43378 C  C   . ILE   Y  11 111 ? 49.599  -166.452 -5.670  1.00 95.66  ? 112 ILE   Y C   1 
ATOM   43379 O  O   . ILE   Y  11 111 ? 48.554  -166.178 -6.289  1.00 97.00  ? 112 ILE   Y O   1 
ATOM   43380 C  CB  . ILE   Y  11 111 ? 51.300  -164.848 -6.627  1.00 99.01  ? 112 ILE   Y CB  1 
ATOM   43381 C  CG1 . ILE   Y  11 111 ? 52.482  -164.671 -7.584  1.00 104.12 ? 112 ILE   Y CG1 1 
ATOM   43382 C  CG2 . ILE   Y  11 111 ? 51.552  -164.167 -5.290  1.00 97.25  ? 112 ILE   Y CG2 1 
ATOM   43383 C  CD1 . ILE   Y  11 111 ? 52.655  -163.255 -8.081  1.00 107.21 ? 112 ILE   Y CD1 1 
ATOM   43384 N  N   . TYR   Y  11 112 ? 49.644  -166.826 -4.389  1.00 94.02  ? 113 TYR   Y N   1 
ATOM   43385 C  CA  . TYR   Y  11 112 ? 48.474  -166.876 -3.474  1.00 97.03  ? 113 TYR   Y CA  1 
ATOM   43386 C  C   . TYR   Y  11 112 ? 48.732  -165.963 -2.273  1.00 96.09  ? 113 TYR   Y C   1 
ATOM   43387 O  O   . TYR   Y  11 112 ? 49.786  -166.105 -1.628  1.00 101.06 ? 113 TYR   Y O   1 
ATOM   43388 C  CB  . TYR   Y  11 112 ? 48.195  -168.306 -3.004  1.00 98.08  ? 113 TYR   Y CB  1 
ATOM   43389 C  CG  . TYR   Y  11 112 ? 47.316  -169.111 -3.928  1.00 100.93 ? 113 TYR   Y CG  1 
ATOM   43390 C  CD1 . TYR   Y  11 112 ? 45.933  -169.021 -3.861  1.00 99.78  ? 113 TYR   Y CD1 1 
ATOM   43391 C  CD2 . TYR   Y  11 112 ? 47.864  -169.963 -4.875  1.00 102.04 ? 113 TYR   Y CD2 1 
ATOM   43392 C  CE1 . TYR   Y  11 112 ? 45.120  -169.755 -4.710  1.00 99.11  ? 113 TYR   Y CE1 1 
ATOM   43393 C  CE2 . TYR   Y  11 112 ? 47.065  -170.701 -5.733  1.00 102.30 ? 113 TYR   Y CE2 1 
ATOM   43394 C  CZ  . TYR   Y  11 112 ? 45.686  -170.598 -5.650  1.00 99.86  ? 113 TYR   Y CZ  1 
ATOM   43395 O  OH  . TYR   Y  11 112 ? 44.885  -171.320 -6.487  1.00 101.15 ? 113 TYR   Y OH  1 
ATOM   43396 N  N   . TYR   Y  11 113 ? 47.790  -165.060 -1.990  1.00 96.25  ? 114 TYR   Y N   1 
ATOM   43397 C  CA  . TYR   Y  11 113 ? 47.752  -164.233 -0.757  1.00 95.66  ? 114 TYR   Y CA  1 
ATOM   43398 C  C   . TYR   Y  11 113 ? 47.076  -165.058 0.344   1.00 92.21  ? 114 TYR   Y C   1 
ATOM   43399 O  O   . TYR   Y  11 113 ? 45.968  -165.574 0.098   1.00 88.74  ? 114 TYR   Y O   1 
ATOM   43400 C  CB  . TYR   Y  11 113 ? 47.017  -162.913 -1.007  1.00 94.07  ? 114 TYR   Y CB  1 
ATOM   43401 C  CG  . TYR   Y  11 113 ? 46.741  -162.104 0.235   1.00 91.41  ? 114 TYR   Y CG  1 
ATOM   43402 C  CD1 . TYR   Y  11 113 ? 47.687  -161.232 0.747   1.00 92.05  ? 114 TYR   Y CD1 1 
ATOM   43403 C  CD2 . TYR   Y  11 113 ? 45.534  -162.217 0.907   1.00 91.17  ? 114 TYR   Y CD2 1 
ATOM   43404 C  CE1 . TYR   Y  11 113 ? 47.439  -160.489 1.890   1.00 93.32  ? 114 TYR   Y CE1 1 
ATOM   43405 C  CE2 . TYR   Y  11 113 ? 45.271  -161.485 2.053   1.00 90.44  ? 114 TYR   Y CE2 1 
ATOM   43406 C  CZ  . TYR   Y  11 113 ? 46.226  -160.615 2.545   1.00 93.11  ? 114 TYR   Y CZ  1 
ATOM   43407 O  OH  . TYR   Y  11 113 ? 45.962  -159.890 3.671   1.00 97.11  ? 114 TYR   Y OH  1 
ATOM   43408 N  N   . VAL   Y  11 114 ? 47.731  -165.192 1.501   1.00 92.75  ? 115 VAL   Y N   1 
ATOM   43409 C  CA  . VAL   Y  11 114 ? 47.204  -165.930 2.690   1.00 92.71  ? 115 VAL   Y CA  1 
ATOM   43410 C  C   . VAL   Y  11 114 ? 47.465  -165.094 3.946   1.00 90.26  ? 115 VAL   Y C   1 
ATOM   43411 O  O   . VAL   Y  11 114 ? 48.650  -164.858 4.247   1.00 91.02  ? 115 VAL   Y O   1 
ATOM   43412 C  CB  . VAL   Y  11 114 ? 47.843  -167.326 2.822   1.00 93.72  ? 115 VAL   Y CB  1 
ATOM   43413 C  CG1 . VAL   Y  11 114 ? 47.383  -168.034 4.087   1.00 93.93  ? 115 VAL   Y CG1 1 
ATOM   43414 C  CG2 . VAL   Y  11 114 ? 47.578  -168.191 1.601   1.00 95.30  ? 115 VAL   Y CG2 1 
ATOM   43415 N  N   . ASP   Y  11 115 ? 46.406  -164.701 4.663   1.00 90.55  ? 116 ASP   Y N   1 
ATOM   43416 C  CA  . ASP   Y  11 115 ? 46.502  -163.897 5.912   1.00 94.00  ? 116 ASP   Y CA  1 
ATOM   43417 C  C   . ASP   Y  11 115 ? 45.836  -164.661 7.064   1.00 92.56  ? 116 ASP   Y C   1 
ATOM   43418 O  O   . ASP   Y  11 115 ? 45.196  -165.699 6.799   1.00 90.52  ? 116 ASP   Y O   1 
ATOM   43419 C  CB  . ASP   Y  11 115 ? 45.941  -162.482 5.717   1.00 97.33  ? 116 ASP   Y CB  1 
ATOM   43420 C  CG  . ASP   Y  11 115 ? 44.424  -162.372 5.650   1.00 103.44 ? 116 ASP   Y CG  1 
ATOM   43421 O  OD1 . ASP   Y  11 115 ? 43.740  -163.362 5.985   1.00 107.55 ? 116 ASP   Y OD1 1 
ATOM   43422 O  OD2 . ASP   Y  11 115 ? 43.934  -161.286 5.265   1.00 100.30 ? 116 ASP   Y OD2 1 
ATOM   43423 N  N   . SER   Y  11 116 ? 45.975  -164.142 8.288   1.00 90.71  ? 117 SER   Y N   1 
ATOM   43424 C  CA  . SER   Y  11 116 ? 45.682  -164.852 9.561   1.00 88.32  ? 117 SER   Y CA  1 
ATOM   43425 C  C   . SER   Y  11 116 ? 44.177  -164.918 9.856   1.00 91.65  ? 117 SER   Y C   1 
ATOM   43426 O  O   . SER   Y  11 116 ? 43.805  -165.761 10.695  1.00 90.92  ? 117 SER   Y O   1 
ATOM   43427 C  CB  . SER   Y  11 116 ? 46.427  -164.241 10.714  1.00 86.75  ? 117 SER   Y CB  1 
ATOM   43428 O  OG  . SER   Y  11 116 ? 46.275  -162.833 10.726  1.00 85.49  ? 117 SER   Y OG  1 
ATOM   43429 N  N   . ASP   Y  11 117 ? 43.340  -164.086 9.219   1.00 95.14  ? 118 ASP   Y N   1 
ATOM   43430 C  CA  . ASP   Y  11 117 ? 41.858  -164.196 9.356   1.00 99.78  ? 118 ASP   Y CA  1 
ATOM   43431 C  C   . ASP   Y  11 117 ? 41.319  -165.173 8.298   1.00 97.13  ? 118 ASP   Y C   1 
ATOM   43432 O  O   . ASP   Y  11 117 ? 40.084  -165.316 8.210   1.00 96.49  ? 118 ASP   Y O   1 
ATOM   43433 C  CB  . ASP   Y  11 117 ? 41.127  -162.843 9.378   1.00 104.45 ? 118 ASP   Y CB  1 
ATOM   43434 C  CG  . ASP   Y  11 117 ? 41.824  -161.674 8.706   1.00 108.95 ? 118 ASP   Y CG  1 
ATOM   43435 O  OD1 . ASP   Y  11 117 ? 41.897  -161.672 7.460   1.00 115.20 ? 118 ASP   Y OD1 1 
ATOM   43436 O  OD2 . ASP   Y  11 117 ? 42.259  -160.756 9.437   1.00 113.62 ? 118 ASP   Y OD2 1 
ATOM   43437 N  N   . GLY   Y  11 118 ? 42.207  -165.843 7.552   1.00 92.32  ? 119 GLY   Y N   1 
ATOM   43438 C  CA  . GLY   Y  11 118 ? 41.874  -167.017 6.722   1.00 93.20  ? 119 GLY   Y CA  1 
ATOM   43439 C  C   . GLY   Y  11 118 ? 41.563  -166.662 5.277   1.00 93.62  ? 119 GLY   Y C   1 
ATOM   43440 O  O   . GLY   Y  11 118 ? 41.049  -167.540 4.563   1.00 97.69  ? 119 GLY   Y O   1 
ATOM   43441 N  N   . THR   Y  11 119 ? 41.853  -165.432 4.846   1.00 90.35  ? 120 THR   Y N   1 
ATOM   43442 C  CA  . THR   Y  11 119 ? 41.699  -164.993 3.434   1.00 90.11  ? 120 THR   Y CA  1 
ATOM   43443 C  C   . THR   Y  11 119 ? 42.728  -165.739 2.581   1.00 86.61  ? 120 THR   Y C   1 
ATOM   43444 O  O   . THR   Y  11 119 ? 43.908  -165.762 2.977   1.00 84.43  ? 120 THR   Y O   1 
ATOM   43445 C  CB  . THR   Y  11 119 ? 41.863  -163.475 3.281   1.00 91.43  ? 120 THR   Y CB  1 
ATOM   43446 O  OG1 . THR   Y  11 119 ? 41.017  -162.831 4.235   1.00 93.84  ? 120 THR   Y OG1 1 
ATOM   43447 C  CG2 . THR   Y  11 119 ? 41.526  -162.985 1.889   1.00 92.24  ? 120 THR   Y CG2 1 
ATOM   43448 N  N   . ARG   Y  11 120 ? 42.281  -166.335 1.472   1.00 85.82  ? 121 ARG   Y N   1 
ATOM   43449 C  CA  . ARG   Y  11 120 ? 43.147  -166.976 0.448   1.00 87.20  ? 121 ARG   Y CA  1 
ATOM   43450 C  C   . ARG   Y  11 120 ? 42.710  -166.464 -0.928  1.00 85.87  ? 121 ARG   Y C   1 
ATOM   43451 O  O   . ARG   Y  11 120 ? 41.536  -166.674 -1.281  1.00 84.46  ? 121 ARG   Y O   1 
ATOM   43452 C  CB  . ARG   Y  11 120 ? 43.054  -168.501 0.553   1.00 88.89  ? 121 ARG   Y CB  1 
ATOM   43453 C  CG  . ARG   Y  11 120 ? 44.002  -169.254 -0.369  1.00 91.45  ? 121 ARG   Y CG  1 
ATOM   43454 C  CD  . ARG   Y  11 120 ? 44.096  -170.725 0.000   1.00 92.40  ? 121 ARG   Y CD  1 
ATOM   43455 N  NE  . ARG   Y  11 120 ? 44.617  -171.540 -1.091  1.00 90.70  ? 121 ARG   Y NE  1 
ATOM   43456 C  CZ  . ARG   Y  11 120 ? 43.892  -172.034 -2.094  1.00 90.58  ? 121 ARG   Y CZ  1 
ATOM   43457 N  NH1 . ARG   Y  11 120 ? 44.478  -172.760 -3.030  1.00 89.85  ? 121 ARG   Y NH1 1 
ATOM   43458 N  NH2 . ARG   Y  11 120 ? 42.591  -171.806 -2.166  1.00 92.71  ? 121 ARG   Y NH2 1 
ATOM   43459 N  N   . LEU   Y  11 121 ? 43.614  -165.791 -1.649  1.00 86.65  ? 122 LEU   Y N   1 
ATOM   43460 C  CA  . LEU   Y  11 121 ? 43.338  -165.153 -2.965  1.00 89.95  ? 122 LEU   Y CA  1 
ATOM   43461 C  C   . LEU   Y  11 121 ? 44.451  -165.498 -3.956  1.00 90.59  ? 122 LEU   Y C   1 
ATOM   43462 O  O   . LEU   Y  11 121 ? 45.628  -165.266 -3.626  1.00 90.01  ? 122 LEU   Y O   1 
ATOM   43463 C  CB  . LEU   Y  11 121 ? 43.261  -163.633 -2.798  1.00 89.62  ? 122 LEU   Y CB  1 
ATOM   43464 C  CG  . LEU   Y  11 121 ? 42.202  -163.113 -1.830  1.00 89.84  ? 122 LEU   Y CG  1 
ATOM   43465 C  CD1 . LEU   Y  11 121 ? 42.397  -161.626 -1.589  1.00 90.42  ? 122 LEU   Y CD1 1 
ATOM   43466 C  CD2 . LEU   Y  11 121 ? 40.798  -163.397 -2.344  1.00 90.10  ? 122 LEU   Y CD2 1 
ATOM   43467 N  N   . LYS   Y  11 122 ? 44.078  -166.005 -5.132  1.00 92.45  ? 123 LYS   Y N   1 
ATOM   43468 C  CA  . LYS   Y  11 122 ? 44.975  -166.078 -6.313  1.00 95.71  ? 123 LYS   Y CA  1 
ATOM   43469 C  C   . LYS   Y  11 122 ? 45.004  -164.683 -6.949  1.00 95.45  ? 123 LYS   Y C   1 
ATOM   43470 O  O   . LYS   Y  11 122 ? 43.947  -164.022 -6.969  1.00 94.93  ? 123 LYS   Y O   1 
ATOM   43471 C  CB  . LYS   Y  11 122 ? 44.502  -167.156 -7.294  1.00 97.02  ? 123 LYS   Y CB  1 
ATOM   43472 C  CG  . LYS   Y  11 122 ? 45.494  -167.491 -8.399  1.00 99.55  ? 123 LYS   Y CG  1 
ATOM   43473 C  CD  . LYS   Y  11 122 ? 45.250  -168.828 -9.054  1.00 102.42 ? 123 LYS   Y CD  1 
ATOM   43474 C  CE  . LYS   Y  11 122 ? 44.042  -168.832 -9.965  1.00 106.41 ? 123 LYS   Y CE  1 
ATOM   43475 N  NZ  . LYS   Y  11 122 ? 43.795  -170.182 -10.524 1.00 109.58 ? 123 LYS   Y NZ  1 
ATOM   43476 N  N   . GLY   Y  11 123 ? 46.170  -164.236 -7.414  1.00 95.02  ? 124 GLY   Y N   1 
ATOM   43477 C  CA  . GLY   Y  11 123 ? 46.314  -162.925 -8.072  1.00 96.80  ? 124 GLY   Y CA  1 
ATOM   43478 C  C   . GLY   Y  11 123 ? 47.640  -162.786 -8.792  1.00 100.32 ? 124 GLY   Y C   1 
ATOM   43479 O  O   . GLY   Y  11 123 ? 48.511  -163.660 -8.612  1.00 101.32 ? 124 GLY   Y O   1 
ATOM   43480 N  N   . ASP   Y  11 124 ? 47.777  -161.716 -9.579  1.00 103.20 ? 125 ASP   Y N   1 
ATOM   43481 C  CA  . ASP   Y  11 124 ? 48.984  -161.404 -10.388 1.00 105.77 ? 125 ASP   Y CA  1 
ATOM   43482 C  C   . ASP   Y  11 124 ? 49.899  -160.464 -9.597  1.00 103.63 ? 125 ASP   Y C   1 
ATOM   43483 O  O   . ASP   Y  11 124 ? 51.121  -160.683 -9.640  1.00 102.70 ? 125 ASP   Y O   1 
ATOM   43484 C  CB  . ASP   Y  11 124 ? 48.591  -160.810 -11.742 1.00 111.61 ? 125 ASP   Y CB  1 
ATOM   43485 C  CG  . ASP   Y  11 124 ? 47.802  -161.769 -12.618 1.00 117.87 ? 125 ASP   Y CG  1 
ATOM   43486 O  OD1 . ASP   Y  11 124 ? 47.911  -162.997 -12.400 1.00 120.14 ? 125 ASP   Y OD1 1 
ATOM   43487 O  OD2 . ASP   Y  11 124 ? 47.082  -161.283 -13.510 1.00 123.29 ? 125 ASP   Y OD2 1 
ATOM   43488 N  N   . ILE   Y  11 125 ? 49.326  -159.463 -8.916  1.00 102.63 ? 126 ILE   Y N   1 
ATOM   43489 C  CA  . ILE   Y  11 125 ? 50.066  -158.454 -8.097  1.00 101.60 ? 126 ILE   Y CA  1 
ATOM   43490 C  C   . ILE   Y  11 125 ? 49.462  -158.418 -6.693  1.00 99.46  ? 126 ILE   Y C   1 
ATOM   43491 O  O   . ILE   Y  11 125 ? 48.222  -158.354 -6.587  1.00 102.14 ? 126 ILE   Y O   1 
ATOM   43492 C  CB  . ILE   Y  11 125 ? 50.012  -157.048 -8.728  1.00 100.40 ? 126 ILE   Y CB  1 
ATOM   43493 C  CG1 . ILE   Y  11 125 ? 50.292  -157.066 -10.231 1.00 103.47 ? 126 ILE   Y CG1 1 
ATOM   43494 C  CG2 . ILE   Y  11 125 ? 50.953  -156.104 -7.995  1.00 98.71  ? 126 ILE   Y CG2 1 
ATOM   43495 C  CD1 . ILE   Y  11 125 ? 49.775  -155.849 -10.961 1.00 105.25 ? 126 ILE   Y CD1 1 
ATOM   43496 N  N   . PHE   Y  11 126 ? 50.315  -158.424 -5.668  1.00 96.84  ? 127 PHE   Y N   1 
ATOM   43497 C  CA  . PHE   Y  11 126 ? 49.943  -158.104 -4.268  1.00 96.63  ? 127 PHE   Y CA  1 
ATOM   43498 C  C   . PHE   Y  11 126 ? 51.108  -157.406 -3.563  1.00 92.16  ? 127 PHE   Y C   1 
ATOM   43499 O  O   . PHE   Y  11 126 ? 52.281  -157.726 -3.852  1.00 89.13  ? 127 PHE   Y O   1 
ATOM   43500 C  CB  . PHE   Y  11 126 ? 49.619  -159.359 -3.464  1.00 97.45  ? 127 PHE   Y CB  1 
ATOM   43501 C  CG  . PHE   Y  11 126 ? 48.403  -160.151 -3.868  1.00 102.49 ? 127 PHE   Y CG  1 
ATOM   43502 C  CD1 . PHE   Y  11 126 ? 47.130  -159.721 -3.528  1.00 104.70 ? 127 PHE   Y CD1 1 
ATOM   43503 C  CD2 . PHE   Y  11 126 ? 48.539  -161.366 -4.523  1.00 103.84 ? 127 PHE   Y CD2 1 
ATOM   43504 C  CE1 . PHE   Y  11 126 ? 46.015  -160.466 -3.879  1.00 108.80 ? 127 PHE   Y CE1 1 
ATOM   43505 C  CE2 . PHE   Y  11 126 ? 47.424  -162.113 -4.870  1.00 108.01 ? 127 PHE   Y CE2 1 
ATOM   43506 C  CZ  . PHE   Y  11 126 ? 46.164  -161.661 -4.548  1.00 110.55 ? 127 PHE   Y CZ  1 
ATOM   43507 N  N   . CYS   Y  11 127 ? 50.768  -156.503 -2.642  1.00 95.45  ? 128 CYS   Y N   1 
ATOM   43508 C  CA  . CYS   Y  11 127 ? 51.695  -155.820 -1.704  1.00 93.83  ? 128 CYS   Y CA  1 
ATOM   43509 C  C   . CYS   Y  11 127 ? 51.117  -155.935 -0.292  1.00 89.49  ? 128 CYS   Y C   1 
ATOM   43510 O  O   . CYS   Y  11 127 ? 49.919  -155.628 -0.108  1.00 87.44  ? 128 CYS   Y O   1 
ATOM   43511 C  CB  . CYS   Y  11 127 ? 51.897  -154.360 -2.081  1.00 97.67  ? 128 CYS   Y CB  1 
ATOM   43512 S  SG  . CYS   Y  11 127 ? 52.429  -154.136 -3.798  1.00 102.82 ? 128 CYS   Y SG  1 
ATOM   43513 N  N   . VAL   Y  11 128 ? 51.934  -156.398 0.652   1.00 87.58  ? 129 VAL   Y N   1 
ATOM   43514 C  CA  . VAL   Y  11 128 ? 51.513  -156.694 2.051   1.00 90.44  ? 129 VAL   Y CA  1 
ATOM   43515 C  C   . VAL   Y  11 128 ? 52.496  -156.006 2.996   1.00 88.27  ? 129 VAL   Y C   1 
ATOM   43516 O  O   . VAL   Y  11 128 ? 53.682  -155.872 2.628   1.00 85.64  ? 129 VAL   Y O   1 
ATOM   43517 C  CB  . VAL   Y  11 128 ? 51.445  -158.210 2.325   1.00 90.11  ? 129 VAL   Y CB  1 
ATOM   43518 C  CG1 . VAL   Y  11 128 ? 50.618  -158.514 3.563   1.00 88.77  ? 129 VAL   Y CG1 1 
ATOM   43519 C  CG2 . VAL   Y  11 128 ? 50.915  -158.987 1.129   1.00 93.10  ? 129 VAL   Y CG2 1 
ATOM   43520 N  N   . GLY   Y  11 129 ? 52.004  -155.599 4.166   1.00 90.56  ? 130 GLY   Y N   1 
ATOM   43521 C  CA  . GLY   Y  11 129 ? 52.792  -154.930 5.216   1.00 93.39  ? 130 GLY   Y CA  1 
ATOM   43522 C  C   . GLY   Y  11 129 ? 52.385  -153.477 5.368   1.00 93.20  ? 130 GLY   Y C   1 
ATOM   43523 O  O   . GLY   Y  11 129 ? 51.552  -153.009 4.569   1.00 89.81  ? 130 GLY   Y O   1 
ATOM   43524 N  N   . SER   Y  11 130 ? 52.957  -152.788 6.360   1.00 97.06  ? 131 SER   Y N   1 
ATOM   43525 C  CA  . SER   Y  11 130 ? 52.615  -151.390 6.739   1.00 99.98  ? 131 SER   Y CA  1 
ATOM   43526 C  C   . SER   Y  11 130 ? 52.941  -150.418 5.595   1.00 96.30  ? 131 SER   Y C   1 
ATOM   43527 O  O   . SER   Y  11 130 ? 52.290  -149.360 5.528   1.00 98.24  ? 131 SER   Y O   1 
ATOM   43528 C  CB  . SER   Y  11 130 ? 53.300  -150.990 8.027   1.00 100.38 ? 131 SER   Y CB  1 
ATOM   43529 O  OG  . SER   Y  11 130 ? 54.696  -151.238 7.976   1.00 104.19 ? 131 SER   Y OG  1 
ATOM   43530 N  N   . GLY   Y  11 131 ? 53.893  -150.764 4.720   1.00 94.93  ? 132 GLY   Y N   1 
ATOM   43531 C  CA  . GLY   Y  11 131 ? 54.300  -149.927 3.574   1.00 92.64  ? 132 GLY   Y CA  1 
ATOM   43532 C  C   . GLY   Y  11 131 ? 53.694  -150.377 2.252   1.00 91.31  ? 132 GLY   Y C   1 
ATOM   43533 O  O   . GLY   Y  11 131 ? 54.162  -149.877 1.208   1.00 86.80  ? 132 GLY   Y O   1 
ATOM   43534 N  N   . GLN   Y  11 132 ? 52.690  -151.269 2.281   1.00 94.51  ? 133 GLN   Y N   1 
ATOM   43535 C  CA  . GLN   Y  11 132 ? 52.080  -151.898 1.072   1.00 95.62  ? 133 GLN   Y CA  1 
ATOM   43536 C  C   . GLN   Y  11 132 ? 51.575  -150.814 0.110   1.00 93.34  ? 133 GLN   Y C   1 
ATOM   43537 O  O   . GLN   Y  11 132 ? 51.759  -150.979 -1.109  1.00 91.26  ? 133 GLN   Y O   1 
ATOM   43538 C  CB  . GLN   Y  11 132 ? 50.952  -152.870 1.440   1.00 99.48  ? 133 GLN   Y CB  1 
ATOM   43539 C  CG  . GLN   Y  11 132 ? 49.732  -152.232 2.090   1.00 101.05 ? 133 GLN   Y CG  1 
ATOM   43540 C  CD  . GLN   Y  11 132 ? 48.726  -153.283 2.491   1.00 106.62 ? 133 GLN   Y CD  1 
ATOM   43541 O  OE1 . GLN   Y  11 132 ? 49.000  -154.148 3.323   1.00 112.86 ? 133 GLN   Y OE1 1 
ATOM   43542 N  NE2 . GLN   Y  11 132 ? 47.551  -153.226 1.886   1.00 108.38 ? 133 GLN   Y NE2 1 
ATOM   43543 N  N   . THR   Y  11 133 ? 50.972  -149.746 0.638   1.00 90.78  ? 134 THR   Y N   1 
ATOM   43544 C  CA  . THR   Y  11 133 ? 50.337  -148.653 -0.151  1.00 89.25  ? 134 THR   Y CA  1 
ATOM   43545 C  C   . THR   Y  11 133 ? 51.400  -147.863 -0.923  1.00 87.76  ? 134 THR   Y C   1 
ATOM   43546 O  O   . THR   Y  11 133 ? 51.104  -147.427 -2.051  1.00 84.21  ? 134 THR   Y O   1 
ATOM   43547 C  CB  . THR   Y  11 133 ? 49.521  -147.710 0.742   1.00 87.90  ? 134 THR   Y CB  1 
ATOM   43548 O  OG1 . THR   Y  11 133 ? 50.399  -147.163 1.724   1.00 86.37  ? 134 THR   Y OG1 1 
ATOM   43549 C  CG2 . THR   Y  11 133 ? 48.354  -148.401 1.412   1.00 88.29  ? 134 THR   Y CG2 1 
ATOM   43550 N  N   . PHE   Y  11 134 ? 52.581  -147.672 -0.330  1.00 89.93  ? 135 PHE   Y N   1 
ATOM   43551 C  CA  . PHE   Y  11 134 ? 53.728  -146.947 -0.939  1.00 92.48  ? 135 PHE   Y CA  1 
ATOM   43552 C  C   . PHE   Y  11 134 ? 54.283  -147.777 -2.103  1.00 90.84  ? 135 PHE   Y C   1 
ATOM   43553 O  O   . PHE   Y  11 134 ? 54.572  -147.193 -3.159  1.00 87.01  ? 135 PHE   Y O   1 
ATOM   43554 C  CB  . PHE   Y  11 134 ? 54.808  -146.648 0.105   1.00 95.90  ? 135 PHE   Y CB  1 
ATOM   43555 C  CG  . PHE   Y  11 134 ? 54.346  -145.820 1.279   1.00 99.23  ? 135 PHE   Y CG  1 
ATOM   43556 C  CD1 . PHE   Y  11 134 ? 54.080  -144.468 1.140   1.00 98.73  ? 135 PHE   Y CD1 1 
ATOM   43557 C  CD2 . PHE   Y  11 134 ? 54.177  -146.397 2.530   1.00 101.62 ? 135 PHE   Y CD2 1 
ATOM   43558 C  CE1 . PHE   Y  11 134 ? 53.652  -143.714 2.223   1.00 101.99 ? 135 PHE   Y CE1 1 
ATOM   43559 C  CE2 . PHE   Y  11 134 ? 53.751  -145.643 3.612   1.00 102.66 ? 135 PHE   Y CE2 1 
ATOM   43560 C  CZ  . PHE   Y  11 134 ? 53.490  -144.302 3.456   1.00 102.84 ? 135 PHE   Y CZ  1 
ATOM   43561 N  N   . ALA   Y  11 135 ? 54.415  -149.094 -1.906  1.00 93.96  ? 136 ALA   Y N   1 
ATOM   43562 C  CA  . ALA   Y  11 135 ? 54.891  -150.079 -2.912  1.00 95.82  ? 136 ALA   Y CA  1 
ATOM   43563 C  C   . ALA   Y  11 135 ? 53.919  -150.144 -4.097  1.00 93.79  ? 136 ALA   Y C   1 
ATOM   43564 O  O   . ALA   Y  11 135 ? 54.390  -150.072 -5.249  1.00 89.52  ? 136 ALA   Y O   1 
ATOM   43565 C  CB  . ALA   Y  11 135 ? 55.059  -151.438 -2.274  1.00 96.35  ? 136 ALA   Y CB  1 
ATOM   43566 N  N   . TYR   Y  11 136 ? 52.619  -150.299 -3.819  1.00 97.23  ? 137 TYR   Y N   1 
ATOM   43567 C  CA  . TYR   Y  11 136 ? 51.521  -150.268 -4.824  1.00 102.52 ? 137 TYR   Y CA  1 
ATOM   43568 C  C   . TYR   Y  11 136 ? 51.671  -149.015 -5.691  1.00 108.66 ? 137 TYR   Y C   1 
ATOM   43569 O  O   . TYR   Y  11 136 ? 51.725  -149.152 -6.928  1.00 106.25 ? 137 TYR   Y O   1 
ATOM   43570 C  CB  . TYR   Y  11 136 ? 50.139  -150.274 -4.160  1.00 103.56 ? 137 TYR   Y CB  1 
ATOM   43571 C  CG  . TYR   Y  11 136 ? 49.565  -151.637 -3.864  1.00 105.32 ? 137 TYR   Y CG  1 
ATOM   43572 C  CD1 . TYR   Y  11 136 ? 49.538  -152.631 -4.832  1.00 106.13 ? 137 TYR   Y CD1 1 
ATOM   43573 C  CD2 . TYR   Y  11 136 ? 49.013  -151.928 -2.626  1.00 108.19 ? 137 TYR   Y CD2 1 
ATOM   43574 C  CE1 . TYR   Y  11 136 ? 49.007  -153.884 -4.570  1.00 106.49 ? 137 TYR   Y CE1 1 
ATOM   43575 C  CE2 . TYR   Y  11 136 ? 48.473  -153.175 -2.349  1.00 109.38 ? 137 TYR   Y CE2 1 
ATOM   43576 C  CZ  . TYR   Y  11 136 ? 48.469  -154.158 -3.325  1.00 107.43 ? 137 TYR   Y CZ  1 
ATOM   43577 O  OH  . TYR   Y  11 136 ? 47.942  -155.391 -3.061  1.00 104.27 ? 137 TYR   Y OH  1 
ATOM   43578 N  N   . GLY   Y  11 137 ? 51.744  -147.841 -5.048  1.00 115.32 ? 138 GLY   Y N   1 
ATOM   43579 C  CA  . GLY   Y  11 137 ? 51.826  -146.519 -5.701  1.00 120.63 ? 138 GLY   Y CA  1 
ATOM   43580 C  C   . GLY   Y  11 137 ? 52.788  -146.530 -6.877  1.00 121.83 ? 138 GLY   Y C   1 
ATOM   43581 O  O   . GLY   Y  11 137 ? 52.383  -146.104 -7.976  1.00 125.96 ? 138 GLY   Y O   1 
ATOM   43582 N  N   . VAL   Y  11 138 ? 54.009  -147.024 -6.654  1.00 124.25 ? 139 VAL   Y N   1 
ATOM   43583 C  CA  . VAL   Y  11 138 ? 55.107  -147.085 -7.666  1.00 122.82 ? 139 VAL   Y CA  1 
ATOM   43584 C  C   . VAL   Y  11 138 ? 54.859  -148.266 -8.610  1.00 117.78 ? 139 VAL   Y C   1 
ATOM   43585 O  O   . VAL   Y  11 138 ? 55.005  -148.083 -9.831  1.00 113.36 ? 139 VAL   Y O   1 
ATOM   43586 C  CB  . VAL   Y  11 138 ? 56.487  -147.194 -6.987  1.00 127.76 ? 139 VAL   Y CB  1 
ATOM   43587 C  CG1 . VAL   Y  11 138 ? 57.585  -147.583 -7.968  1.00 125.63 ? 139 VAL   Y CG1 1 
ATOM   43588 C  CG2 . VAL   Y  11 138 ? 56.853  -145.908 -6.258  1.00 134.63 ? 139 VAL   Y CG2 1 
ATOM   43589 N  N   . LEU   Y  11 139 ? 54.528  -149.436 -8.057  1.00 115.61 ? 140 LEU   Y N   1 
ATOM   43590 C  CA  . LEU   Y  11 139 ? 54.410  -150.711 -8.813  1.00 117.31 ? 140 LEU   Y CA  1 
ATOM   43591 C  C   . LEU   Y  11 139 ? 53.287  -150.595 -9.854  1.00 112.07 ? 140 LEU   Y C   1 
ATOM   43592 O  O   . LEU   Y  11 139 ? 53.574  -150.812 -11.044 1.00 109.37 ? 140 LEU   Y O   1 
ATOM   43593 C  CB  . LEU   Y  11 139 ? 54.172  -151.858 -7.823  1.00 117.53 ? 140 LEU   Y CB  1 
ATOM   43594 C  CG  . LEU   Y  11 139 ? 54.032  -153.257 -8.426  1.00 120.02 ? 140 LEU   Y CG  1 
ATOM   43595 C  CD1 . LEU   Y  11 139 ? 55.149  -153.551 -9.419  1.00 122.66 ? 140 LEU   Y CD1 1 
ATOM   43596 C  CD2 . LEU   Y  11 139 ? 54.008  -154.313 -7.331  1.00 117.62 ? 140 LEU   Y CD2 1 
ATOM   43597 N  N   . ASP   Y  11 140 ? 52.071  -150.235 -9.424  1.00 113.63 ? 141 ASP   Y N   1 
ATOM   43598 C  CA  . ASP   Y  11 140 ? 50.880  -150.053 -10.301 1.00 116.70 ? 141 ASP   Y CA  1 
ATOM   43599 C  C   . ASP   Y  11 140 ? 51.205  -149.080 -11.440 1.00 117.42 ? 141 ASP   Y C   1 
ATOM   43600 O  O   . ASP   Y  11 140 ? 50.886  -149.403 -12.601 1.00 108.52 ? 141 ASP   Y O   1 
ATOM   43601 C  CB  . ASP   Y  11 140 ? 49.674  -149.520 -9.521  1.00 118.25 ? 141 ASP   Y CB  1 
ATOM   43602 C  CG  . ASP   Y  11 140 ? 48.946  -150.568 -8.701  1.00 120.37 ? 141 ASP   Y CG  1 
ATOM   43603 O  OD1 . ASP   Y  11 140 ? 48.753  -151.691 -9.214  1.00 118.12 ? 141 ASP   Y OD1 1 
ATOM   43604 O  OD2 . ASP   Y  11 140 ? 48.568  -150.250 -7.555  1.00 127.93 ? 141 ASP   Y OD2 1 
ATOM   43605 N  N   . SER   Y  11 141 ? 51.817  -147.936 -11.110 1.00 122.97 ? 142 SER   Y N   1 
ATOM   43606 C  CA  . SER   Y  11 141 ? 52.032  -146.779 -12.022 1.00 128.96 ? 142 SER   Y CA  1 
ATOM   43607 C  C   . SER   Y  11 141 ? 53.190  -147.034 -12.999 1.00 128.54 ? 142 SER   Y C   1 
ATOM   43608 O  O   . SER   Y  11 141 ? 53.451  -146.141 -13.826 1.00 130.51 ? 142 SER   Y O   1 
ATOM   43609 C  CB  . SER   Y  11 141 ? 52.243  -145.501 -11.236 1.00 134.58 ? 142 SER   Y CB  1 
ATOM   43610 O  OG  . SER   Y  11 141 ? 53.415  -145.575 -10.434 1.00 138.53 ? 142 SER   Y OG  1 
ATOM   43611 N  N   . ASN   Y  11 142 ? 53.864  -148.187 -12.910 1.00 125.98 ? 143 ASN   Y N   1 
ATOM   43612 C  CA  . ASN   Y  11 142 ? 54.976  -148.573 -13.822 1.00 128.24 ? 143 ASN   Y CA  1 
ATOM   43613 C  C   . ASN   Y  11 142 ? 54.764  -149.983 -14.386 1.00 129.93 ? 143 ASN   Y C   1 
ATOM   43614 O  O   . ASN   Y  11 142 ? 55.520  -150.347 -15.307 1.00 131.16 ? 143 ASN   Y O   1 
ATOM   43615 C  CB  . ASN   Y  11 142 ? 56.333  -148.493 -13.118 1.00 129.59 ? 143 ASN   Y CB  1 
ATOM   43616 C  CG  . ASN   Y  11 142 ? 56.805  -147.071 -12.900 1.00 131.90 ? 143 ASN   Y CG  1 
ATOM   43617 O  OD1 . ASN   Y  11 142 ? 56.904  -146.610 -11.765 1.00 133.48 ? 143 ASN   Y OD1 1 
ATOM   43618 N  ND2 . ASN   Y  11 142 ? 57.095  -146.366 -13.981 1.00 136.05 ? 143 ASN   Y ND2 1 
ATOM   43619 N  N   . TYR   Y  11 143 ? 53.790  -150.745 -13.871 1.00 131.92 ? 144 TYR   Y N   1 
ATOM   43620 C  CA  . TYR   Y  11 143 ? 53.585  -152.177 -14.220 1.00 134.95 ? 144 TYR   Y CA  1 
ATOM   43621 C  C   . TYR   Y  11 143 ? 52.990  -152.301 -15.624 1.00 137.33 ? 144 TYR   Y C   1 
ATOM   43622 O  O   . TYR   Y  11 143 ? 51.982  -151.637 -15.929 1.00 143.59 ? 144 TYR   Y O   1 
ATOM   43623 C  CB  . TYR   Y  11 143 ? 52.664  -152.897 -13.230 1.00 130.47 ? 144 TYR   Y CB  1 
ATOM   43624 C  CG  . TYR   Y  11 143 ? 52.368  -154.330 -13.599 1.00 129.42 ? 144 TYR   Y CG  1 
ATOM   43625 C  CD1 . TYR   Y  11 143 ? 53.242  -155.352 -13.259 1.00 126.71 ? 144 TYR   Y CD1 1 
ATOM   43626 C  CD2 . TYR   Y  11 143 ? 51.221  -154.670 -14.300 1.00 130.99 ? 144 TYR   Y CD2 1 
ATOM   43627 C  CE1 . TYR   Y  11 143 ? 52.982  -156.671 -13.596 1.00 125.29 ? 144 TYR   Y CE1 1 
ATOM   43628 C  CE2 . TYR   Y  11 143 ? 50.947  -155.984 -14.647 1.00 130.75 ? 144 TYR   Y CE2 1 
ATOM   43629 C  CZ  . TYR   Y  11 143 ? 51.830  -156.989 -14.294 1.00 127.82 ? 144 TYR   Y CZ  1 
ATOM   43630 O  OH  . TYR   Y  11 143 ? 51.568  -158.287 -14.629 1.00 125.03 ? 144 TYR   Y OH  1 
ATOM   43631 N  N   . LYS   Y  11 144 ? 53.622  -153.143 -16.441 1.00 141.49 ? 145 LYS   Y N   1 
ATOM   43632 C  CA  . LYS   Y  11 144 ? 53.060  -153.733 -17.683 1.00 147.11 ? 145 LYS   Y CA  1 
ATOM   43633 C  C   . LYS   Y  11 144 ? 53.394  -155.230 -17.654 1.00 147.97 ? 145 LYS   Y C   1 
ATOM   43634 O  O   . LYS   Y  11 144 ? 54.402  -155.592 -17.011 1.00 145.00 ? 145 LYS   Y O   1 
ATOM   43635 C  CB  . LYS   Y  11 144 ? 53.626  -153.037 -18.927 1.00 151.09 ? 145 LYS   Y CB  1 
ATOM   43636 C  CG  . LYS   Y  11 144 ? 53.224  -151.578 -19.114 1.00 151.49 ? 145 LYS   Y CG  1 
ATOM   43637 C  CD  . LYS   Y  11 144 ? 54.060  -150.860 -20.154 1.00 153.56 ? 145 LYS   Y CD  1 
ATOM   43638 C  CE  . LYS   Y  11 144 ? 53.597  -149.446 -20.428 1.00 156.00 ? 145 LYS   Y CE  1 
ATOM   43639 N  NZ  . LYS   Y  11 144 ? 54.546  -148.725 -21.309 1.00 158.99 ? 145 LYS   Y NZ  1 
ATOM   43640 N  N   . TRP   Y  11 145 ? 52.575  -156.070 -18.293 1.00 149.82 ? 146 TRP   Y N   1 
ATOM   43641 C  CA  . TRP   Y  11 145 ? 52.807  -157.537 -18.383 1.00 149.16 ? 146 TRP   Y CA  1 
ATOM   43642 C  C   . TRP   Y  11 145 ? 54.120  -157.823 -19.128 1.00 153.23 ? 146 TRP   Y C   1 
ATOM   43643 O  O   . TRP   Y  11 145 ? 54.789  -158.822 -18.792 1.00 147.45 ? 146 TRP   Y O   1 
ATOM   43644 C  CB  . TRP   Y  11 145 ? 51.629  -158.248 -19.061 1.00 152.37 ? 146 TRP   Y CB  1 
ATOM   43645 C  CG  . TRP   Y  11 145 ? 51.877  -159.713 -19.256 1.00 150.39 ? 146 TRP   Y CG  1 
ATOM   43646 C  CD1 . TRP   Y  11 145 ? 52.381  -160.323 -20.368 1.00 154.55 ? 146 TRP   Y CD1 1 
ATOM   43647 C  CD2 . TRP   Y  11 145 ? 51.678  -160.756 -18.286 1.00 147.42 ? 146 TRP   Y CD2 1 
ATOM   43648 N  NE1 . TRP   Y  11 145 ? 52.491  -161.672 -20.165 1.00 149.35 ? 146 TRP   Y NE1 1 
ATOM   43649 C  CE2 . TRP   Y  11 145 ? 52.067  -161.969 -18.897 1.00 145.67 ? 146 TRP   Y CE2 1 
ATOM   43650 C  CE3 . TRP   Y  11 145 ? 51.201  -160.785 -16.971 1.00 147.08 ? 146 TRP   Y CE3 1 
ATOM   43651 C  CZ2 . TRP   Y  11 145 ? 51.990  -163.193 -18.234 1.00 142.63 ? 146 TRP   Y CZ2 1 
ATOM   43652 C  CZ3 . TRP   Y  11 145 ? 51.127  -161.996 -16.316 1.00 145.68 ? 146 TRP   Y CZ3 1 
ATOM   43653 C  CH2 . TRP   Y  11 145 ? 51.517  -163.182 -16.942 1.00 143.99 ? 146 TRP   Y CH2 1 
ATOM   43654 N  N   . ASP   Y  11 146 ? 54.472  -156.971 -20.096 1.00 158.70 ? 147 ASP   Y N   1 
ATOM   43655 C  CA  . ASP   Y  11 146 ? 55.540  -157.220 -21.101 1.00 166.18 ? 147 ASP   Y CA  1 
ATOM   43656 C  C   . ASP   Y  11 146 ? 56.904  -156.729 -20.598 1.00 163.57 ? 147 ASP   Y C   1 
ATOM   43657 O  O   . ASP   Y  11 146 ? 57.849  -156.741 -21.412 1.00 166.94 ? 147 ASP   Y O   1 
ATOM   43658 C  CB  . ASP   Y  11 146 ? 55.175  -156.559 -22.432 1.00 169.46 ? 147 ASP   Y CB  1 
ATOM   43659 C  CG  . ASP   Y  11 146 ? 53.814  -156.986 -22.950 1.00 174.99 ? 147 ASP   Y CG  1 
ATOM   43660 O  OD1 . ASP   Y  11 146 ? 53.629  -158.201 -23.171 1.00 177.25 ? 147 ASP   Y OD1 1 
ATOM   43661 O  OD2 . ASP   Y  11 146 ? 52.945  -156.106 -23.106 1.00 180.90 ? 147 ASP   Y OD2 1 
ATOM   43662 N  N   . LEU   Y  11 147 ? 57.016  -156.322 -19.325 1.00 161.29 ? 148 LEU   Y N   1 
ATOM   43663 C  CA  . LEU   Y  11 147 ? 58.307  -155.930 -18.689 1.00 154.05 ? 148 LEU   Y CA  1 
ATOM   43664 C  C   . LEU   Y  11 147 ? 59.351  -157.020 -18.969 1.00 149.73 ? 148 LEU   Y C   1 
ATOM   43665 O  O   . LEU   Y  11 147 ? 58.994  -158.216 -18.908 1.00 141.22 ? 148 LEU   Y O   1 
ATOM   43666 C  CB  . LEU   Y  11 147 ? 58.118  -155.733 -17.178 1.00 152.91 ? 148 LEU   Y CB  1 
ATOM   43667 C  CG  . LEU   Y  11 147 ? 57.965  -154.294 -16.677 1.00 156.56 ? 148 LEU   Y CG  1 
ATOM   43668 C  CD1 . LEU   Y  11 147 ? 57.034  -153.473 -17.558 1.00 160.07 ? 148 LEU   Y CD1 1 
ATOM   43669 C  CD2 . LEU   Y  11 147 ? 57.471  -154.283 -15.236 1.00 154.03 ? 148 LEU   Y CD2 1 
ATOM   43670 N  N   . SER   Y  11 148 ? 60.586  -156.616 -19.282 1.00 148.90 ? 149 SER   Y N   1 
ATOM   43671 C  CA  . SER   Y  11 148 ? 61.763  -157.518 -19.390 1.00 151.42 ? 149 SER   Y CA  1 
ATOM   43672 C  C   . SER   Y  11 148 ? 62.127  -158.014 -17.988 1.00 148.97 ? 149 SER   Y C   1 
ATOM   43673 O  O   . SER   Y  11 148 ? 61.736  -157.346 -17.008 1.00 154.43 ? 149 SER   Y O   1 
ATOM   43674 C  CB  . SER   Y  11 148 ? 62.934  -156.835 -20.057 1.00 153.90 ? 149 SER   Y CB  1 
ATOM   43675 O  OG  . SER   Y  11 148 ? 63.390  -155.732 -19.291 1.00 153.08 ? 149 SER   Y OG  1 
ATOM   43676 N  N   . VAL   Y  11 149 ? 62.832  -159.143 -17.896 1.00 147.85 ? 150 VAL   Y N   1 
ATOM   43677 C  CA  . VAL   Y  11 149 ? 63.340  -159.711 -16.610 1.00 145.94 ? 150 VAL   Y CA  1 
ATOM   43678 C  C   . VAL   Y  11 149 ? 64.161  -158.639 -15.881 1.00 144.73 ? 150 VAL   Y C   1 
ATOM   43679 O  O   . VAL   Y  11 149 ? 64.004  -158.511 -14.650 1.00 144.32 ? 150 VAL   Y O   1 
ATOM   43680 C  CB  . VAL   Y  11 149 ? 64.168  -160.988 -16.848 1.00 147.83 ? 150 VAL   Y CB  1 
ATOM   43681 C  CG1 . VAL   Y  11 149 ? 65.087  -161.303 -15.677 1.00 146.32 ? 150 VAL   Y CG1 1 
ATOM   43682 C  CG2 . VAL   Y  11 149 ? 63.273  -162.176 -17.163 1.00 147.41 ? 150 VAL   Y CG2 1 
ATOM   43683 N  N   . GLU   Y  11 150 ? 65.001  -157.908 -16.620 1.00 147.83 ? 151 GLU   Y N   1 
ATOM   43684 C  CA  . GLU   Y  11 150 ? 65.885  -156.837 -16.088 1.00 149.62 ? 151 GLU   Y CA  1 
ATOM   43685 C  C   . GLU   Y  11 150 ? 65.025  -155.715 -15.491 1.00 140.74 ? 151 GLU   Y C   1 
ATOM   43686 O  O   . GLU   Y  11 150 ? 65.305  -155.306 -14.349 1.00 133.96 ? 151 GLU   Y O   1 
ATOM   43687 C  CB  . GLU   Y  11 150 ? 66.794  -156.305 -17.198 1.00 155.36 ? 151 GLU   Y CB  1 
ATOM   43688 C  CG  . GLU   Y  11 150 ? 67.973  -155.502 -16.684 1.00 158.94 ? 151 GLU   Y CG  1 
ATOM   43689 C  CD  . GLU   Y  11 150 ? 68.762  -154.780 -17.762 1.00 166.28 ? 151 GLU   Y CD  1 
ATOM   43690 O  OE1 . GLU   Y  11 150 ? 69.971  -154.563 -17.557 1.00 172.22 ? 151 GLU   Y OE1 1 
ATOM   43691 O  OE2 . GLU   Y  11 150 ? 68.165  -154.433 -18.802 1.00 172.27 ? 151 GLU   Y OE2 1 
ATOM   43692 N  N   . ASP   Y  11 151 ? 64.015  -155.253 -16.237 1.00 142.11 ? 152 ASP   Y N   1 
ATOM   43693 C  CA  . ASP   Y  11 151 ? 63.123  -154.124 -15.853 1.00 142.59 ? 152 ASP   Y CA  1 
ATOM   43694 C  C   . ASP   Y  11 151 ? 62.245  -154.545 -14.668 1.00 138.94 ? 152 ASP   Y C   1 
ATOM   43695 O  O   . ASP   Y  11 151 ? 62.119  -153.741 -13.722 1.00 142.45 ? 152 ASP   Y O   1 
ATOM   43696 C  CB  . ASP   Y  11 151 ? 62.280  -153.644 -17.041 1.00 147.38 ? 152 ASP   Y CB  1 
ATOM   43697 C  CG  . ASP   Y  11 151 ? 63.068  -152.911 -18.117 1.00 150.93 ? 152 ASP   Y CG  1 
ATOM   43698 O  OD1 . ASP   Y  11 151 ? 64.153  -152.384 -17.801 1.00 160.84 ? 152 ASP   Y OD1 1 
ATOM   43699 O  OD2 . ASP   Y  11 151 ? 62.589  -152.871 -19.269 1.00 148.19 ? 152 ASP   Y OD2 1 
ATOM   43700 N  N   . ALA   Y  11 152 ? 61.665  -155.750 -14.718 1.00 132.35 ? 153 ALA   Y N   1 
ATOM   43701 C  CA  . ALA   Y  11 152 ? 60.785  -156.311 -13.664 1.00 129.07 ? 153 ALA   Y CA  1 
ATOM   43702 C  C   . ALA   Y  11 152 ? 61.544  -156.382 -12.333 1.00 126.34 ? 153 ALA   Y C   1 
ATOM   43703 O  O   . ALA   Y  11 152 ? 60.955  -156.011 -11.297 1.00 128.14 ? 153 ALA   Y O   1 
ATOM   43704 C  CB  . ALA   Y  11 152 ? 60.273  -157.668 -14.076 1.00 128.19 ? 153 ALA   Y CB  1 
ATOM   43705 N  N   . LEU   Y  11 153 ? 62.802  -156.832 -12.363 1.00 126.02 ? 154 LEU   Y N   1 
ATOM   43706 C  CA  . LEU   Y  11 153 ? 63.688  -156.906 -11.169 1.00 124.02 ? 154 LEU   Y CA  1 
ATOM   43707 C  C   . LEU   Y  11 153 ? 63.862  -155.507 -10.566 1.00 119.50 ? 154 LEU   Y C   1 
ATOM   43708 O  O   . LEU   Y  11 153 ? 63.705  -155.380 -9.336  1.00 120.01 ? 154 LEU   Y O   1 
ATOM   43709 C  CB  . LEU   Y  11 153 ? 65.041  -157.508 -11.564 1.00 127.84 ? 154 LEU   Y CB  1 
ATOM   43710 C  CG  . LEU   Y  11 153 ? 65.093  -159.034 -11.585 1.00 129.19 ? 154 LEU   Y CG  1 
ATOM   43711 C  CD1 . LEU   Y  11 153 ? 66.285  -159.530 -12.388 1.00 135.05 ? 154 LEU   Y CD1 1 
ATOM   43712 C  CD2 . LEU   Y  11 153 ? 65.136  -159.591 -10.170 1.00 124.90 ? 154 LEU   Y CD2 1 
ATOM   43713 N  N   . TYR   Y  11 154 ? 64.171  -154.502 -11.394 1.00 119.00 ? 155 TYR   Y N   1 
ATOM   43714 C  CA  . TYR   Y  11 154 ? 64.358  -153.092 -10.961 1.00 118.60 ? 155 TYR   Y CA  1 
ATOM   43715 C  C   . TYR   Y  11 154 ? 63.064  -152.594 -10.305 1.00 114.77 ? 155 TYR   Y C   1 
ATOM   43716 O  O   . TYR   Y  11 154 ? 63.142  -152.082 -9.174  1.00 114.43 ? 155 TYR   Y O   1 
ATOM   43717 C  CB  . TYR   Y  11 154 ? 64.793  -152.194 -12.124 1.00 121.58 ? 155 TYR   Y CB  1 
ATOM   43718 C  CG  . TYR   Y  11 154 ? 65.078  -150.765 -11.733 1.00 123.24 ? 155 TYR   Y CG  1 
ATOM   43719 C  CD1 . TYR   Y  11 154 ? 66.241  -150.426 -11.058 1.00 123.02 ? 155 TYR   Y CD1 1 
ATOM   43720 C  CD2 . TYR   Y  11 154 ? 64.179  -149.750 -12.022 1.00 122.99 ? 155 TYR   Y CD2 1 
ATOM   43721 C  CE1 . TYR   Y  11 154 ? 66.507  -149.119 -10.685 1.00 126.04 ? 155 TYR   Y CE1 1 
ATOM   43722 C  CE2 . TYR   Y  11 154 ? 64.429  -148.438 -11.656 1.00 127.25 ? 155 TYR   Y CE2 1 
ATOM   43723 C  CZ  . TYR   Y  11 154 ? 65.598  -148.120 -10.985 1.00 128.28 ? 155 TYR   Y CZ  1 
ATOM   43724 O  OH  . TYR   Y  11 154 ? 65.859  -146.830 -10.622 1.00 132.68 ? 155 TYR   Y OH  1 
ATOM   43725 N  N   . LEU   Y  11 155 ? 61.916  -152.756 -10.976 1.00 110.40 ? 156 LEU   Y N   1 
ATOM   43726 C  CA  . LEU   Y  11 155 ? 60.611  -152.207 -10.512 1.00 110.07 ? 156 LEU   Y CA  1 
ATOM   43727 C  C   . LEU   Y  11 155 ? 60.288  -152.763 -9.120  1.00 108.52 ? 156 LEU   Y C   1 
ATOM   43728 O  O   . LEU   Y  11 155 ? 59.926  -151.963 -8.235  1.00 103.28 ? 156 LEU   Y O   1 
ATOM   43729 C  CB  . LEU   Y  11 155 ? 59.497  -152.546 -11.508 1.00 113.36 ? 156 LEU   Y CB  1 
ATOM   43730 C  CG  . LEU   Y  11 155 ? 58.107  -152.025 -11.134 1.00 117.03 ? 156 LEU   Y CG  1 
ATOM   43731 C  CD1 . LEU   Y  11 155 ? 58.137  -150.539 -10.793 1.00 120.63 ? 156 LEU   Y CD1 1 
ATOM   43732 C  CD2 . LEU   Y  11 155 ? 57.108  -152.284 -12.250 1.00 119.05 ? 156 LEU   Y CD2 1 
ATOM   43733 N  N   . GLY   Y  11 156 ? 60.413  -154.080 -8.943  1.00 108.70 ? 157 GLY   Y N   1 
ATOM   43734 C  CA  . GLY   Y  11 156 ? 60.242  -154.749 -7.639  1.00 108.36 ? 157 GLY   Y CA  1 
ATOM   43735 C  C   . GLY   Y  11 156 ? 61.164  -154.150 -6.590  1.00 106.39 ? 157 GLY   Y C   1 
ATOM   43736 O  O   . GLY   Y  11 156 ? 60.685  -153.876 -5.471  1.00 107.93 ? 157 GLY   Y O   1 
ATOM   43737 N  N   . LYS   Y  11 157 ? 62.437  -153.943 -6.945  1.00 106.74 ? 158 LYS   Y N   1 
ATOM   43738 C  CA  . LYS   Y  11 157 ? 63.473  -153.330 -6.070  1.00 107.95 ? 158 LYS   Y CA  1 
ATOM   43739 C  C   . LYS   Y  11 157 ? 63.084  -151.878 -5.760  1.00 108.14 ? 158 LYS   Y C   1 
ATOM   43740 O  O   . LYS   Y  11 157 ? 63.163  -151.485 -4.579  1.00 106.10 ? 158 LYS   Y O   1 
ATOM   43741 C  CB  . LYS   Y  11 157 ? 64.848  -153.387 -6.743  1.00 108.63 ? 158 LYS   Y CB  1 
ATOM   43742 C  CG  . LYS   Y  11 157 ? 66.025  -153.006 -5.853  1.00 107.90 ? 158 LYS   Y CG  1 
ATOM   43743 C  CD  . LYS   Y  11 157 ? 67.212  -152.465 -6.618  1.00 111.14 ? 158 LYS   Y CD  1 
ATOM   43744 C  CE  . LYS   Y  11 157 ? 67.922  -153.520 -7.438  1.00 113.54 ? 158 LYS   Y CE  1 
ATOM   43745 N  NZ  . LYS   Y  11 157 ? 69.019  -152.931 -8.241  1.00 118.69 ? 158 LYS   Y NZ  1 
ATOM   43746 N  N   . ARG   Y  11 158 ? 62.680  -151.120 -6.786  1.00 111.87 ? 159 ARG   Y N   1 
ATOM   43747 C  CA  . ARG   Y  11 158 ? 62.369  -149.668 -6.688  1.00 112.87 ? 159 ARG   Y CA  1 
ATOM   43748 C  C   . ARG   Y  11 158 ? 61.110  -149.464 -5.835  1.00 114.17 ? 159 ARG   Y C   1 
ATOM   43749 O  O   . ARG   Y  11 158 ? 61.049  -148.439 -5.124  1.00 114.25 ? 159 ARG   Y O   1 
ATOM   43750 C  CB  . ARG   Y  11 158 ? 62.203  -149.057 -8.085  1.00 116.37 ? 159 ARG   Y CB  1 
ATOM   43751 C  CG  . ARG   Y  11 158 ? 61.937  -147.557 -8.093  1.00 120.20 ? 159 ARG   Y CG  1 
ATOM   43752 C  CD  . ARG   Y  11 158 ? 63.064  -146.742 -7.484  1.00 124.28 ? 159 ARG   Y CD  1 
ATOM   43753 N  NE  . ARG   Y  11 158 ? 62.782  -145.312 -7.448  1.00 128.92 ? 159 ARG   Y NE  1 
ATOM   43754 C  CZ  . ARG   Y  11 158 ? 61.966  -144.709 -6.581  1.00 129.44 ? 159 ARG   Y CZ  1 
ATOM   43755 N  NH1 . ARG   Y  11 158 ? 61.312  -145.405 -5.665  1.00 130.17 ? 159 ARG   Y NH1 1 
ATOM   43756 N  NH2 . ARG   Y  11 158 ? 61.800  -143.399 -6.637  1.00 133.46 ? 159 ARG   Y NH2 1 
ATOM   43757 N  N   . SER   Y  11 159 ? 60.150  -150.392 -5.902  1.00 109.33 ? 160 SER   Y N   1 
ATOM   43758 C  CA  . SER   Y  11 159 ? 58.859  -150.321 -5.166  1.00 107.31 ? 160 SER   Y CA  1 
ATOM   43759 C  C   . SER   Y  11 159 ? 59.095  -150.520 -3.664  1.00 105.29 ? 160 SER   Y C   1 
ATOM   43760 O  O   . SER   Y  11 159 ? 58.400  -149.855 -2.872  1.00 102.41 ? 160 SER   Y O   1 
ATOM   43761 C  CB  . SER   Y  11 159 ? 57.860  -151.314 -5.700  1.00 106.42 ? 160 SER   Y CB  1 
ATOM   43762 O  OG  . SER   Y  11 159 ? 57.603  -151.084 -7.076  1.00 109.11 ? 160 SER   Y OG  1 
ATOM   43763 N  N   . ILE   Y  11 160 ? 60.027  -151.401 -3.286  1.00 105.17 ? 161 ILE   Y N   1 
ATOM   43764 C  CA  . ILE   Y  11 160 ? 60.448  -151.599 -1.865  1.00 105.42 ? 161 ILE   Y CA  1 
ATOM   43765 C  C   . ILE   Y  11 160 ? 61.136  -150.314 -1.388  1.00 104.50 ? 161 ILE   Y C   1 
ATOM   43766 O  O   . ILE   Y  11 160 ? 60.775  -149.827 -0.301  1.00 107.96 ? 161 ILE   Y O   1 
ATOM   43767 C  CB  . ILE   Y  11 160 ? 61.352  -152.840 -1.696  1.00 105.82 ? 161 ILE   Y CB  1 
ATOM   43768 C  CG1 . ILE   Y  11 160 ? 60.578  -154.141 -1.921  1.00 108.01 ? 161 ILE   Y CG1 1 
ATOM   43769 C  CG2 . ILE   Y  11 160 ? 62.045  -152.838 -0.340  1.00 104.01 ? 161 ILE   Y CG2 1 
ATOM   43770 C  CD1 . ILE   Y  11 160 ? 59.540  -154.443 -0.856  1.00 107.46 ? 161 ILE   Y CD1 1 
ATOM   43771 N  N   . LEU   Y  11 161 ? 62.081  -149.789 -2.175  1.00 102.18 ? 162 LEU   Y N   1 
ATOM   43772 C  CA  . LEU   Y  11 161 ? 62.854  -148.557 -1.852  1.00 103.17 ? 162 LEU   Y CA  1 
ATOM   43773 C  C   . LEU   Y  11 161 ? 61.892  -147.391 -1.588  1.00 101.27 ? 162 LEU   Y C   1 
ATOM   43774 O  O   . LEU   Y  11 161 ? 62.126  -146.638 -0.622  1.00 100.83 ? 162 LEU   Y O   1 
ATOM   43775 C  CB  . LEU   Y  11 161 ? 63.801  -148.228 -3.010  1.00 103.71 ? 162 LEU   Y CB  1 
ATOM   43776 C  CG  . LEU   Y  11 161 ? 64.656  -146.974 -2.827  1.00 104.08 ? 162 LEU   Y CG  1 
ATOM   43777 C  CD1 . LEU   Y  11 161 ? 65.524  -147.075 -1.581  1.00 104.08 ? 162 LEU   Y CD1 1 
ATOM   43778 C  CD2 . LEU   Y  11 161 ? 65.520  -146.727 -4.053  1.00 104.59 ? 162 LEU   Y CD2 1 
ATOM   43779 N  N   . ALA   Y  11 162 ? 60.861  -147.251 -2.425  1.00 99.40  ? 163 ALA   Y N   1 
ATOM   43780 C  CA  . ALA   Y  11 162 ? 59.792  -146.232 -2.301  1.00 99.70  ? 163 ALA   Y CA  1 
ATOM   43781 C  C   . ALA   Y  11 162 ? 59.161  -146.299 -0.908  1.00 98.62  ? 163 ALA   Y C   1 
ATOM   43782 O  O   . ALA   Y  11 162 ? 59.059  -145.247 -0.254  1.00 101.59 ? 163 ALA   Y O   1 
ATOM   43783 C  CB  . ALA   Y  11 162 ? 58.753  -146.444 -3.371  1.00 100.34 ? 163 ALA   Y CB  1 
ATOM   43784 N  N   . ALA   Y  11 163 ? 58.749  -147.497 -0.484  1.00 98.55  ? 164 ALA   Y N   1 
ATOM   43785 C  CA  . ALA   Y  11 163 ? 58.107  -147.755 0.824   1.00 95.45  ? 164 ALA   Y CA  1 
ATOM   43786 C  C   . ALA   Y  11 163 ? 59.133  -147.558 1.946   1.00 92.69  ? 164 ALA   Y C   1 
ATOM   43787 O  O   . ALA   Y  11 163 ? 58.818  -146.824 2.901   1.00 91.84  ? 164 ALA   Y O   1 
ATOM   43788 C  CB  . ALA   Y  11 163 ? 57.515  -149.141 0.842   1.00 95.31  ? 164 ALA   Y CB  1 
ATOM   43789 N  N   . ALA   Y  11 164 ? 60.312  -148.183 1.820   1.00 95.02  ? 165 ALA   Y N   1 
ATOM   43790 C  CA  . ALA   Y  11 164 ? 61.427  -148.124 2.798   1.00 98.35  ? 165 ALA   Y CA  1 
ATOM   43791 C  C   . ALA   Y  11 164 ? 61.670  -146.667 3.195   1.00 99.26  ? 165 ALA   Y C   1 
ATOM   43792 O  O   . ALA   Y  11 164 ? 61.889  -146.394 4.391   1.00 95.65  ? 165 ALA   Y O   1 
ATOM   43793 C  CB  . ALA   Y  11 164 ? 62.678  -148.740 2.218   1.00 101.12 ? 165 ALA   Y CB  1 
ATOM   43794 N  N   . HIS   Y  11 165 ? 61.615  -145.772 2.211   1.00 99.72  ? 166 HIS   Y N   1 
ATOM   43795 C  CA  . HIS   Y  11 165 ? 61.835  -144.312 2.372   1.00 103.51 ? 166 HIS   Y CA  1 
ATOM   43796 C  C   . HIS   Y  11 165 ? 60.674  -143.665 3.143   1.00 104.15 ? 166 HIS   Y C   1 
ATOM   43797 O  O   . HIS   Y  11 165 ? 60.954  -142.927 4.106   1.00 101.37 ? 166 HIS   Y O   1 
ATOM   43798 C  CB  . HIS   Y  11 165 ? 62.062  -143.672 0.998   1.00 107.73 ? 166 HIS   Y CB  1 
ATOM   43799 C  CG  . HIS   Y  11 165 ? 62.246  -142.194 1.043   1.00 110.86 ? 166 HIS   Y CG  1 
ATOM   43800 N  ND1 . HIS   Y  11 165 ? 63.177  -141.593 1.866   1.00 114.64 ? 166 HIS   Y ND1 1 
ATOM   43801 C  CD2 . HIS   Y  11 165 ? 61.642  -141.196 0.361   1.00 111.70 ? 166 HIS   Y CD2 1 
ATOM   43802 C  CE1 . HIS   Y  11 165 ? 63.131  -140.287 1.698   1.00 115.13 ? 166 HIS   Y CE1 1 
ATOM   43803 N  NE2 . HIS   Y  11 165 ? 62.199  -140.017 0.777   1.00 112.58 ? 166 HIS   Y NE2 1 
ATOM   43804 N  N   . ARG   Y  11 166 ? 59.424  -143.929 2.746   1.00 105.30 ? 167 ARG   Y N   1 
ATOM   43805 C  CA  . ARG   Y  11 166 ? 58.228  -143.214 3.276   1.00 106.62 ? 167 ARG   Y CA  1 
ATOM   43806 C  C   . ARG   Y  11 166 ? 57.726  -143.864 4.572   1.00 107.67 ? 167 ARG   Y C   1 
ATOM   43807 O  O   . ARG   Y  11 166 ? 57.506  -143.107 5.544   1.00 107.45 ? 167 ARG   Y O   1 
ATOM   43808 C  CB  . ARG   Y  11 166 ? 57.124  -143.137 2.218   1.00 106.90 ? 167 ARG   Y CB  1 
ATOM   43809 C  CG  . ARG   Y  11 166 ? 57.325  -142.016 1.209   1.00 109.30 ? 167 ARG   Y CG  1 
ATOM   43810 C  CD  . ARG   Y  11 166 ? 57.077  -140.643 1.810   1.00 110.54 ? 167 ARG   Y CD  1 
ATOM   43811 N  NE  . ARG   Y  11 166 ? 57.361  -139.559 0.875   1.00 111.82 ? 167 ARG   Y NE  1 
ATOM   43812 C  CZ  . ARG   Y  11 166 ? 57.210  -138.260 1.136   1.00 111.76 ? 167 ARG   Y CZ  1 
ATOM   43813 N  NH1 . ARG   Y  11 166 ? 56.772  -137.855 2.317   1.00 109.45 ? 167 ARG   Y NH1 1 
ATOM   43814 N  NH2 . ARG   Y  11 166 ? 57.497  -137.367 0.204   1.00 110.45 ? 167 ARG   Y NH2 1 
ATOM   43815 N  N   . ASP   Y  11 167 ? 57.539  -145.191 4.591   1.00 105.78 ? 168 ASP   Y N   1 
ATOM   43816 C  CA  . ASP   Y  11 167 ? 57.078  -145.940 5.793   1.00 104.49 ? 168 ASP   Y CA  1 
ATOM   43817 C  C   . ASP   Y  11 167 ? 58.237  -145.977 6.796   1.00 102.32 ? 168 ASP   Y C   1 
ATOM   43818 O  O   . ASP   Y  11 167 ? 59.356  -146.355 6.396   1.00 101.81 ? 168 ASP   Y O   1 
ATOM   43819 C  CB  . ASP   Y  11 167 ? 56.549  -147.333 5.431   1.00 105.85 ? 168 ASP   Y CB  1 
ATOM   43820 C  CG  . ASP   Y  11 167 ? 56.012  -148.138 6.608   1.00 108.16 ? 168 ASP   Y CG  1 
ATOM   43821 O  OD1 . ASP   Y  11 167 ? 55.754  -147.534 7.672   1.00 111.83 ? 168 ASP   Y OD1 1 
ATOM   43822 O  OD2 . ASP   Y  11 167 ? 55.844  -149.365 6.449   1.00 110.92 ? 168 ASP   Y OD2 1 
ATOM   43823 N  N   . ALA   Y  11 168 ? 57.977  -145.562 8.039   1.00 103.75 ? 169 ALA   Y N   1 
ATOM   43824 C  CA  . ALA   Y  11 168 ? 58.961  -145.507 9.147   1.00 104.32 ? 169 ALA   Y CA  1 
ATOM   43825 C  C   . ALA   Y  11 168 ? 59.336  -146.925 9.596   1.00 101.00 ? 169 ALA   Y C   1 
ATOM   43826 O  O   . ALA   Y  11 168 ? 60.478  -147.106 10.059  1.00 100.30 ? 169 ALA   Y O   1 
ATOM   43827 C  CB  . ALA   Y  11 168 ? 58.397  -144.700 10.291  1.00 107.25 ? 169 ALA   Y CB  1 
ATOM   43828 N  N   . TYR   Y  11 169 ? 58.414  -147.884 9.459   1.00 97.90  ? 170 TYR   Y N   1 
ATOM   43829 C  CA  . TYR   Y  11 169 ? 58.553  -149.283 9.943   1.00 99.17  ? 170 TYR   Y CA  1 
ATOM   43830 C  C   . TYR   Y  11 169 ? 59.106  -150.179 8.828   1.00 97.52  ? 170 TYR   Y C   1 
ATOM   43831 O  O   . TYR   Y  11 169 ? 59.322  -151.378 9.088   1.00 100.89 ? 170 TYR   Y O   1 
ATOM   43832 C  CB  . TYR   Y  11 169 ? 57.210  -149.761 10.503  1.00 100.35 ? 170 TYR   Y CB  1 
ATOM   43833 C  CG  . TYR   Y  11 169 ? 56.646  -148.841 11.554  1.00 101.44 ? 170 TYR   Y CG  1 
ATOM   43834 C  CD1 . TYR   Y  11 169 ? 57.404  -148.476 12.655  1.00 103.35 ? 170 TYR   Y CD1 1 
ATOM   43835 C  CD2 . TYR   Y  11 169 ? 55.370  -148.314 11.440  1.00 102.13 ? 170 TYR   Y CD2 1 
ATOM   43836 C  CE1 . TYR   Y  11 169 ? 56.907  -147.621 13.624  1.00 106.14 ? 170 TYR   Y CE1 1 
ATOM   43837 C  CE2 . TYR   Y  11 169 ? 54.856  -147.460 12.401  1.00 106.04 ? 170 TYR   Y CE2 1 
ATOM   43838 C  CZ  . TYR   Y  11 169 ? 55.627  -147.110 13.496  1.00 108.72 ? 170 TYR   Y CZ  1 
ATOM   43839 O  OH  . TYR   Y  11 169 ? 55.126  -146.265 14.444  1.00 113.18 ? 170 TYR   Y OH  1 
ATOM   43840 N  N   . SER   Y  11 170 ? 59.342  -149.610 7.640   1.00 94.58  ? 171 SER   Y N   1 
ATOM   43841 C  CA  . SER   Y  11 170 ? 59.993  -150.267 6.475   1.00 94.02  ? 171 SER   Y CA  1 
ATOM   43842 C  C   . SER   Y  11 170 ? 61.420  -149.734 6.327   1.00 96.65  ? 171 SER   Y C   1 
ATOM   43843 O  O   . SER   Y  11 170 ? 61.639  -148.557 6.667   1.00 97.79  ? 171 SER   Y O   1 
ATOM   43844 C  CB  . SER   Y  11 170 ? 59.206  -150.023 5.222   1.00 94.20  ? 171 SER   Y CB  1 
ATOM   43845 O  OG  . SER   Y  11 170 ? 57.903  -150.574 5.325   1.00 94.56  ? 171 SER   Y OG  1 
ATOM   43846 N  N   . GLY   Y  11 171 ? 62.349  -150.559 5.832   1.00 98.06  ? 172 GLY   Y N   1 
ATOM   43847 C  CA  . GLY   Y  11 171 ? 63.739  -150.140 5.564   1.00 98.55  ? 172 GLY   Y CA  1 
ATOM   43848 C  C   . GLY   Y  11 171 ? 64.731  -151.289 5.612   1.00 98.31  ? 172 GLY   Y C   1 
ATOM   43849 O  O   . GLY   Y  11 171 ? 64.331  -152.440 5.337   1.00 96.00  ? 172 GLY   Y O   1 
ATOM   43850 N  N   . GLY   Y  11 172 ? 65.986  -150.973 5.944   1.00 98.08  ? 173 GLY   Y N   1 
ATOM   43851 C  CA  . GLY   Y  11 172 ? 67.104  -151.930 6.022   1.00 98.89  ? 173 GLY   Y CA  1 
ATOM   43852 C  C   . GLY   Y  11 172 ? 67.720  -152.162 4.657   1.00 100.76 ? 173 GLY   Y C   1 
ATOM   43853 O  O   . GLY   Y  11 172 ? 68.556  -151.337 4.240   1.00 98.71  ? 173 GLY   Y O   1 
ATOM   43854 N  N   . SER   Y  11 173 ? 67.312  -153.243 3.988   1.00 103.46 ? 174 SER   Y N   1 
ATOM   43855 C  CA  . SER   Y  11 173 ? 67.809  -153.656 2.651   1.00 106.41 ? 174 SER   Y CA  1 
ATOM   43856 C  C   . SER   Y  11 173 ? 66.657  -154.254 1.839   1.00 106.25 ? 174 SER   Y C   1 
ATOM   43857 O  O   . SER   Y  11 173 ? 65.579  -154.485 2.421   1.00 103.83 ? 174 SER   Y O   1 
ATOM   43858 C  CB  . SER   Y  11 173 ? 68.964  -154.616 2.790   1.00 109.93 ? 174 SER   Y CB  1 
ATOM   43859 O  OG  . SER   Y  11 173 ? 68.586  -155.765 3.531   1.00 113.21 ? 174 SER   Y OG  1 
ATOM   43860 N  N   . VAL   Y  11 174 ? 66.884  -154.467 0.540   1.00 108.99 ? 175 VAL   Y N   1 
ATOM   43861 C  CA  . VAL   Y  11 174 ? 65.941  -155.159 -0.386  1.00 112.22 ? 175 VAL   Y CA  1 
ATOM   43862 C  C   . VAL   Y  11 174 ? 66.512  -156.545 -0.691  1.00 112.80 ? 175 VAL   Y C   1 
ATOM   43863 O  O   . VAL   Y  11 174 ? 67.718  -156.633 -0.997  1.00 117.02 ? 175 VAL   Y O   1 
ATOM   43864 C  CB  . VAL   Y  11 174 ? 65.718  -154.355 -1.681  1.00 113.35 ? 175 VAL   Y CB  1 
ATOM   43865 C  CG1 . VAL   Y  11 174 ? 64.563  -154.917 -2.495  1.00 114.41 ? 175 VAL   Y CG1 1 
ATOM   43866 C  CG2 . VAL   Y  11 174 ? 65.501  -152.878 -1.398  1.00 114.68 ? 175 VAL   Y CG2 1 
ATOM   43867 N  N   . ASN   Y  11 175 ? 65.673  -157.579 -0.595  1.00 111.38 ? 176 ASN   Y N   1 
ATOM   43868 C  CA  . ASN   Y  11 175 ? 65.993  -158.961 -1.030  1.00 112.63 ? 176 ASN   Y CA  1 
ATOM   43869 C  C   . ASN   Y  11 175 ? 65.155  -159.272 -2.271  1.00 109.12 ? 176 ASN   Y C   1 
ATOM   43870 O  O   . ASN   Y  11 175 ? 63.915  -159.293 -2.153  1.00 107.82 ? 176 ASN   Y O   1 
ATOM   43871 C  CB  . ASN   Y  11 175 ? 65.776  -159.964 0.103   1.00 111.90 ? 176 ASN   Y CB  1 
ATOM   43872 C  CG  . ASN   Y  11 175 ? 66.898  -159.923 1.117   1.00 113.83 ? 176 ASN   Y CG  1 
ATOM   43873 O  OD1 . ASN   Y  11 175 ? 66.719  -159.428 2.227   1.00 111.14 ? 176 ASN   Y OD1 1 
ATOM   43874 N  ND2 . ASN   Y  11 175 ? 68.066  -160.412 0.729   1.00 116.43 ? 176 ASN   Y ND2 1 
ATOM   43875 N  N   . LEU   Y  11 176 ? 65.816  -159.477 -3.413  1.00 112.55 ? 177 LEU   Y N   1 
ATOM   43876 C  CA  . LEU   Y  11 176 ? 65.163  -159.787 -4.710  1.00 114.38 ? 177 LEU   Y CA  1 
ATOM   43877 C  C   . LEU   Y  11 176 ? 65.167  -161.301 -4.935  1.00 114.90 ? 177 LEU   Y C   1 
ATOM   43878 O  O   . LEU   Y  11 176 ? 66.101  -161.980 -4.458  1.00 111.94 ? 177 LEU   Y O   1 
ATOM   43879 C  CB  . LEU   Y  11 176 ? 65.889  -159.062 -5.849  1.00 115.17 ? 177 LEU   Y CB  1 
ATOM   43880 C  CG  . LEU   Y  11 176 ? 65.328  -157.694 -6.232  1.00 115.76 ? 177 LEU   Y CG  1 
ATOM   43881 C  CD1 . LEU   Y  11 176 ? 66.239  -157.012 -7.240  1.00 118.48 ? 177 LEU   Y CD1 1 
ATOM   43882 C  CD2 . LEU   Y  11 176 ? 63.917  -157.816 -6.792  1.00 114.59 ? 177 LEU   Y CD2 1 
ATOM   43883 N  N   . TYR   Y  11 177 ? 64.142  -161.788 -5.637  1.00 115.98 ? 178 TYR   Y N   1 
ATOM   43884 C  CA  . TYR   Y  11 177 ? 64.001  -163.182 -6.126  1.00 118.82 ? 178 TYR   Y CA  1 
ATOM   43885 C  C   . TYR   Y  11 177 ? 63.272  -163.171 -7.471  1.00 119.50 ? 178 TYR   Y C   1 
ATOM   43886 O  O   . TYR   Y  11 177 ? 62.316  -162.388 -7.619  1.00 119.99 ? 178 TYR   Y O   1 
ATOM   43887 C  CB  . TYR   Y  11 177 ? 63.208  -164.028 -5.131  1.00 113.48 ? 178 TYR   Y CB  1 
ATOM   43888 C  CG  . TYR   Y  11 177 ? 63.956  -164.412 -3.882  1.00 112.55 ? 178 TYR   Y CG  1 
ATOM   43889 C  CD1 . TYR   Y  11 177 ? 63.906  -163.624 -2.744  1.00 112.45 ? 178 TYR   Y CD1 1 
ATOM   43890 C  CD2 . TYR   Y  11 177 ? 64.702  -165.577 -3.831  1.00 114.59 ? 178 TYR   Y CD2 1 
ATOM   43891 C  CE1 . TYR   Y  11 177 ? 64.583  -163.979 -1.589  1.00 110.31 ? 178 TYR   Y CE1 1 
ATOM   43892 C  CE2 . TYR   Y  11 177 ? 65.381  -165.950 -2.683  1.00 114.02 ? 178 TYR   Y CE2 1 
ATOM   43893 C  CZ  . TYR   Y  11 177 ? 65.322  -165.147 -1.556  1.00 110.67 ? 178 TYR   Y CZ  1 
ATOM   43894 O  OH  . TYR   Y  11 177 ? 65.987  -165.494 -0.416  1.00 107.60 ? 178 TYR   Y OH  1 
ATOM   43895 N  N   . HIS   Y  11 178 ? 63.710  -164.021 -8.401  1.00 123.97 ? 179 HIS   Y N   1 
ATOM   43896 C  CA  . HIS   Y  11 178 ? 63.038  -164.292 -9.699  1.00 124.84 ? 179 HIS   Y CA  1 
ATOM   43897 C  C   . HIS   Y  11 178 ? 62.643  -165.767 -9.725  1.00 125.24 ? 179 HIS   Y C   1 
ATOM   43898 O  O   . HIS   Y  11 178 ? 63.518  -166.604 -9.463  1.00 125.97 ? 179 HIS   Y O   1 
ATOM   43899 C  CB  . HIS   Y  11 178 ? 63.944  -163.906 -10.877 1.00 128.33 ? 179 HIS   Y CB  1 
ATOM   43900 C  CG  . HIS   Y  11 178 ? 63.321  -164.112 -12.218 1.00 128.52 ? 179 HIS   Y CG  1 
ATOM   43901 N  ND1 . HIS   Y  11 178 ? 64.050  -164.528 -13.316 1.00 130.50 ? 179 HIS   Y ND1 1 
ATOM   43902 C  CD2 . HIS   Y  11 178 ? 62.047  -163.960 -12.644 1.00 129.07 ? 179 HIS   Y CD2 1 
ATOM   43903 C  CE1 . HIS   Y  11 178 ? 63.253  -164.611 -14.362 1.00 133.52 ? 179 HIS   Y CE1 1 
ATOM   43904 N  NE2 . HIS   Y  11 178 ? 62.018  -164.277 -13.975 1.00 131.42 ? 179 HIS   Y NE2 1 
ATOM   43905 N  N   . VAL   Y  11 179 ? 61.371  -166.058 -10.002 1.00 129.29 ? 180 VAL   Y N   1 
ATOM   43906 C  CA  . VAL   Y  11 179 ? 60.837  -167.445 -10.133 1.00 132.06 ? 180 VAL   Y CA  1 
ATOM   43907 C  C   . VAL   Y  11 179 ? 60.542  -167.702 -11.613 1.00 144.29 ? 180 VAL   Y C   1 
ATOM   43908 O  O   . VAL   Y  11 179 ? 59.733  -166.950 -12.190 1.00 143.32 ? 180 VAL   Y O   1 
ATOM   43909 C  CB  . VAL   Y  11 179 ? 59.582  -167.660 -9.268  1.00 128.43 ? 180 VAL   Y CB  1 
ATOM   43910 C  CG1 . VAL   Y  11 179 ? 59.187  -169.127 -9.220  1.00 130.17 ? 180 VAL   Y CG1 1 
ATOM   43911 C  CG2 . VAL   Y  11 179 ? 59.754  -167.105 -7.863  1.00 124.10 ? 180 VAL   Y CG2 1 
ATOM   43912 N  N   . THR   Y  11 180 ? 61.185  -168.721 -12.192 1.00 153.58 ? 181 THR   Y N   1 
ATOM   43913 C  CA  . THR   Y  11 180 ? 60.999  -169.168 -13.598 1.00 160.52 ? 181 THR   Y CA  1 
ATOM   43914 C  C   . THR   Y  11 180 ? 60.420  -170.587 -13.602 1.00 163.04 ? 181 THR   Y C   1 
ATOM   43915 O  O   . THR   Y  11 180 ? 60.134  -171.121 -12.506 1.00 149.77 ? 181 THR   Y O   1 
ATOM   43916 C  CB  . THR   Y  11 180 ? 62.315  -169.080 -14.384 1.00 168.51 ? 181 THR   Y CB  1 
ATOM   43917 O  OG1 . THR   Y  11 180 ? 63.270  -169.959 -13.787 1.00 164.25 ? 181 THR   Y OG1 1 
ATOM   43918 C  CG2 . THR   Y  11 180 ? 62.871  -167.673 -14.432 1.00 169.64 ? 181 THR   Y CG2 1 
ATOM   43919 N  N   . GLU   Y  11 181 ? 60.241  -171.153 -14.798 1.00 166.09 ? 182 GLU   Y N   1 
ATOM   43920 C  CA  . GLU   Y  11 181 ? 59.857  -172.573 -15.017 1.00 164.24 ? 182 GLU   Y CA  1 
ATOM   43921 C  C   . GLU   Y  11 181 ? 60.909  -173.502 -14.389 1.00 166.19 ? 182 GLU   Y C   1 
ATOM   43922 O  O   . GLU   Y  11 181 ? 60.540  -174.638 -14.037 1.00 170.55 ? 182 GLU   Y O   1 
ATOM   43923 C  CB  . GLU   Y  11 181 ? 59.641  -172.849 -16.510 1.00 167.61 ? 182 GLU   Y CB  1 
ATOM   43924 C  CG  . GLU   Y  11 181 ? 60.863  -172.617 -17.387 1.00 169.57 ? 182 GLU   Y CG  1 
ATOM   43925 C  CD  . GLU   Y  11 181 ? 60.616  -172.797 -18.876 1.00 172.30 ? 182 GLU   Y CD  1 
ATOM   43926 O  OE1 . GLU   Y  11 181 ? 61.571  -172.617 -19.657 1.00 174.45 ? 182 GLU   Y OE1 1 
ATOM   43927 O  OE2 . GLU   Y  11 181 ? 59.470  -173.116 -19.255 1.00 172.88 ? 182 GLU   Y OE2 1 
ATOM   43928 N  N   . ASP   Y  11 182 ? 62.155  -173.031 -14.236 1.00 164.32 ? 183 ASP   Y N   1 
ATOM   43929 C  CA  . ASP   Y  11 182 ? 63.313  -173.826 -13.738 1.00 162.30 ? 183 ASP   Y CA  1 
ATOM   43930 C  C   . ASP   Y  11 182 ? 63.426  -173.733 -12.206 1.00 153.58 ? 183 ASP   Y C   1 
ATOM   43931 O  O   . ASP   Y  11 182 ? 64.214  -174.513 -11.635 1.00 149.07 ? 183 ASP   Y O   1 
ATOM   43932 C  CB  . ASP   Y  11 182 ? 64.610  -173.379 -14.422 1.00 166.25 ? 183 ASP   Y CB  1 
ATOM   43933 C  CG  . ASP   Y  11 182 ? 64.581  -173.484 -15.940 1.00 168.21 ? 183 ASP   Y CG  1 
ATOM   43934 O  OD1 . ASP   Y  11 182 ? 64.154  -174.541 -16.449 1.00 166.16 ? 183 ASP   Y OD1 1 
ATOM   43935 O  OD2 . ASP   Y  11 182 ? 64.986  -172.507 -16.601 1.00 167.41 ? 183 ASP   Y OD2 1 
ATOM   43936 N  N   . GLY   Y  11 183 ? 62.675  -172.830 -11.561 1.00 150.11 ? 184 GLY   Y N   1 
ATOM   43937 C  CA  . GLY   Y  11 183 ? 62.713  -172.597 -10.101 1.00 146.00 ? 184 GLY   Y CA  1 
ATOM   43938 C  C   . GLY   Y  11 183 ? 62.984  -171.137 -9.770  1.00 144.88 ? 184 GLY   Y C   1 
ATOM   43939 O  O   . GLY   Y  11 183 ? 62.918  -170.312 -10.705 1.00 146.93 ? 184 GLY   Y O   1 
ATOM   43940 N  N   . TRP   Y  11 184 ? 63.276  -170.820 -8.498  1.00 138.23 ? 185 TRP   Y N   1 
ATOM   43941 C  CA  . TRP   Y  11 184 ? 63.608  -169.439 -8.039  1.00 136.28 ? 185 TRP   Y CA  1 
ATOM   43942 C  C   . TRP   Y  11 184 ? 65.114  -169.186 -8.167  1.00 134.78 ? 185 TRP   Y C   1 
ATOM   43943 O  O   . TRP   Y  11 184 ? 65.901  -170.134 -7.981  1.00 137.93 ? 185 TRP   Y O   1 
ATOM   43944 C  CB  . TRP   Y  11 184 ? 63.120  -169.131 -6.612  1.00 127.86 ? 185 TRP   Y CB  1 
ATOM   43945 C  CG  . TRP   Y  11 184 ? 63.676  -170.013 -5.536  1.00 127.24 ? 185 TRP   Y CG  1 
ATOM   43946 C  CD1 . TRP   Y  11 184 ? 63.013  -171.028 -4.915  1.00 130.29 ? 185 TRP   Y CD1 1 
ATOM   43947 C  CD2 . TRP   Y  11 184 ? 64.985  -169.961 -4.933  1.00 126.29 ? 185 TRP   Y CD2 1 
ATOM   43948 N  NE1 . TRP   Y  11 184 ? 63.818  -171.623 -3.985  1.00 132.77 ? 185 TRP   Y NE1 1 
ATOM   43949 C  CE2 . TRP   Y  11 184 ? 65.032  -170.994 -3.973  1.00 129.74 ? 185 TRP   Y CE2 1 
ATOM   43950 C  CE3 . TRP   Y  11 184 ? 66.123  -169.163 -5.111  1.00 124.07 ? 185 TRP   Y CE3 1 
ATOM   43951 C  CZ2 . TRP   Y  11 184 ? 66.163  -171.249 -3.199  1.00 130.23 ? 185 TRP   Y CZ2 1 
ATOM   43952 C  CZ3 . TRP   Y  11 184 ? 67.241  -169.414 -4.344  1.00 126.88 ? 185 TRP   Y CZ3 1 
ATOM   43953 C  CH2 . TRP   Y  11 184 ? 67.259  -170.443 -3.401  1.00 128.93 ? 185 TRP   Y CH2 1 
ATOM   43954 N  N   . ILE   Y  11 185 ? 65.472  -167.935 -8.463  1.00 135.66 ? 186 ILE   Y N   1 
ATOM   43955 C  CA  . ILE   Y  11 185 ? 66.869  -167.418 -8.556  1.00 139.03 ? 186 ILE   Y CA  1 
ATOM   43956 C  C   . ILE   Y  11 185 ? 66.959  -166.200 -7.628  1.00 135.73 ? 186 ILE   Y C   1 
ATOM   43957 O  O   . ILE   Y  11 185 ? 66.118  -165.286 -7.766  1.00 136.53 ? 186 ILE   Y O   1 
ATOM   43958 C  CB  . ILE   Y  11 185 ? 67.234  -167.068 -10.016 1.00 139.69 ? 186 ILE   Y CB  1 
ATOM   43959 C  CG1 . ILE   Y  11 185 ? 66.959  -168.227 -10.980 1.00 140.21 ? 186 ILE   Y CG1 1 
ATOM   43960 C  CG2 . ILE   Y  11 185 ? 68.678  -166.595 -10.119 1.00 140.54 ? 186 ILE   Y CG2 1 
ATOM   43961 C  CD1 . ILE   Y  11 185 ? 66.460  -167.793 -12.341 1.00 142.82 ? 186 ILE   Y CD1 1 
ATOM   43962 N  N   . TYR   Y  11 186 ? 67.916  -166.208 -6.698  1.00 132.71 ? 187 TYR   Y N   1 
ATOM   43963 C  CA  . TYR   Y  11 186 ? 68.212  -165.078 -5.780  1.00 127.18 ? 187 TYR   Y CA  1 
ATOM   43964 C  C   . TYR   Y  11 186 ? 68.960  -163.990 -6.560  1.00 131.10 ? 187 TYR   Y C   1 
ATOM   43965 O  O   . TYR   Y  11 186 ? 69.907  -164.328 -7.297  1.00 140.07 ? 187 TYR   Y O   1 
ATOM   43966 C  CB  . TYR   Y  11 186 ? 69.024  -165.578 -4.585  1.00 122.71 ? 187 TYR   Y CB  1 
ATOM   43967 C  CG  . TYR   Y  11 186 ? 69.313  -164.541 -3.529  1.00 118.11 ? 187 TYR   Y CG  1 
ATOM   43968 C  CD1 . TYR   Y  11 186 ? 68.287  -163.840 -2.915  1.00 112.49 ? 187 TYR   Y CD1 1 
ATOM   43969 C  CD2 . TYR   Y  11 186 ? 70.612  -164.280 -3.122  1.00 116.91 ? 187 TYR   Y CD2 1 
ATOM   43970 C  CE1 . TYR   Y  11 186 ? 68.544  -162.896 -1.933  1.00 110.80 ? 187 TYR   Y CE1 1 
ATOM   43971 C  CE2 . TYR   Y  11 186 ? 70.886  -163.342 -2.140  1.00 115.56 ? 187 TYR   Y CE2 1 
ATOM   43972 C  CZ  . TYR   Y  11 186 ? 69.848  -162.647 -1.545  1.00 113.38 ? 187 TYR   Y CZ  1 
ATOM   43973 O  OH  . TYR   Y  11 186 ? 70.109  -161.719 -0.580  1.00 114.67 ? 187 TYR   Y OH  1 
ATOM   43974 N  N   . HIS   Y  11 187 ? 68.541  -162.729 -6.411  1.00 129.38 ? 188 HIS   Y N   1 
ATOM   43975 C  CA  . HIS   Y  11 187 ? 69.151  -161.551 -7.084  1.00 130.72 ? 188 HIS   Y CA  1 
ATOM   43976 C  C   . HIS   Y  11 187 ? 69.635  -160.545 -6.032  1.00 128.69 ? 188 HIS   Y C   1 
ATOM   43977 O  O   . HIS   Y  11 187 ? 69.436  -159.331 -6.232  1.00 129.39 ? 188 HIS   Y O   1 
ATOM   43978 C  CB  . HIS   Y  11 187 ? 68.174  -160.957 -8.107  1.00 131.85 ? 188 HIS   Y CB  1 
ATOM   43979 C  CG  . HIS   Y  11 187 ? 68.090  -161.748 -9.369  1.00 133.73 ? 188 HIS   Y CG  1 
ATOM   43980 N  ND1 . HIS   Y  11 187 ? 68.911  -161.500 -10.452 1.00 137.80 ? 188 HIS   Y ND1 1 
ATOM   43981 C  CD2 . HIS   Y  11 187 ? 67.297  -162.783 -9.723  1.00 132.24 ? 188 HIS   Y CD2 1 
ATOM   43982 C  CE1 . HIS   Y  11 187 ? 68.622  -162.344 -11.422 1.00 138.15 ? 188 HIS   Y CE1 1 
ATOM   43983 N  NE2 . HIS   Y  11 187 ? 67.636  -163.143 -10.999 1.00 135.02 ? 188 HIS   Y NE2 1 
ATOM   43984 N  N   . GLY   Y  11 188 ? 70.244  -161.046 -4.953  1.00 126.31 ? 189 GLY   Y N   1 
ATOM   43985 C  CA  . GLY   Y  11 188 ? 71.126  -160.271 -4.058  1.00 123.13 ? 189 GLY   Y CA  1 
ATOM   43986 C  C   . GLY   Y  11 188 ? 70.383  -159.543 -2.951  1.00 118.22 ? 189 GLY   Y C   1 
ATOM   43987 O  O   . GLY   Y  11 188 ? 69.147  -159.395 -3.045  1.00 114.01 ? 189 GLY   Y O   1 
ATOM   43988 N  N   . ASN   Y  11 189 ? 71.137  -159.122 -1.931  1.00 118.94 ? 190 ASN   Y N   1 
ATOM   43989 C  CA  . ASN   Y  11 189 ? 70.719  -158.197 -0.843  1.00 118.49 ? 190 ASN   Y CA  1 
ATOM   43990 C  C   . ASN   Y  11 189 ? 71.212  -156.786 -1.189  1.00 118.51 ? 190 ASN   Y C   1 
ATOM   43991 O  O   . ASN   Y  11 189 ? 72.413  -156.644 -1.490  1.00 123.81 ? 190 ASN   Y O   1 
ATOM   43992 C  CB  . ASN   Y  11 189 ? 71.281  -158.641 0.509   1.00 115.39 ? 190 ASN   Y CB  1 
ATOM   43993 C  CG  . ASN   Y  11 189 ? 70.943  -157.684 1.631   1.00 111.65 ? 190 ASN   Y CG  1 
ATOM   43994 O  OD1 . ASN   Y  11 189 ? 71.724  -156.790 1.945   1.00 106.87 ? 190 ASN   Y OD1 1 
ATOM   43995 N  ND2 . ASN   Y  11 189 ? 69.777  -157.859 2.231   1.00 109.37 ? 190 ASN   Y ND2 1 
ATOM   43996 N  N   . HIS   Y  11 190 ? 70.331  -155.784 -1.139  1.00 116.35 ? 191 HIS   Y N   1 
ATOM   43997 C  CA  . HIS   Y  11 190 ? 70.623  -154.386 -1.559  1.00 119.31 ? 191 HIS   Y CA  1 
ATOM   43998 C  C   . HIS   Y  11 190 ? 70.319  -153.417 -0.411  1.00 119.16 ? 191 HIS   Y C   1 
ATOM   43999 O  O   . HIS   Y  11 190 ? 69.132  -153.079 -0.221  1.00 119.19 ? 191 HIS   Y O   1 
ATOM   44000 C  CB  . HIS   Y  11 190 ? 69.843  -154.041 -2.835  1.00 116.94 ? 191 HIS   Y CB  1 
ATOM   44001 C  CG  . HIS   Y  11 190 ? 70.033  -155.032 -3.931  1.00 118.14 ? 191 HIS   Y CG  1 
ATOM   44002 N  ND1 . HIS   Y  11 190 ? 71.038  -154.912 -4.870  1.00 119.61 ? 191 HIS   Y ND1 1 
ATOM   44003 C  CD2 . HIS   Y  11 190 ? 69.360  -156.163 -4.232  1.00 117.72 ? 191 HIS   Y CD2 1 
ATOM   44004 C  CE1 . HIS   Y  11 190 ? 70.972  -155.926 -5.708  1.00 122.65 ? 191 HIS   Y CE1 1 
ATOM   44005 N  NE2 . HIS   Y  11 190 ? 69.951  -156.706 -5.338  1.00 121.56 ? 191 HIS   Y NE2 1 
ATOM   44006 N  N   . ASP   Y  11 191 ? 71.359  -152.992 0.317   1.00 120.24 ? 192 ASP   Y N   1 
ATOM   44007 C  CA  . ASP   Y  11 191 ? 71.277  -152.012 1.436   1.00 118.86 ? 192 ASP   Y CA  1 
ATOM   44008 C  C   . ASP   Y  11 191 ? 70.661  -150.712 0.911   1.00 114.32 ? 192 ASP   Y C   1 
ATOM   44009 O  O   . ASP   Y  11 191 ? 71.133  -150.220 -0.129  1.00 116.19 ? 192 ASP   Y O   1 
ATOM   44010 C  CB  . ASP   Y  11 191 ? 72.656  -151.744 2.049   1.00 120.21 ? 192 ASP   Y CB  1 
ATOM   44011 C  CG  . ASP   Y  11 191 ? 72.617  -151.066 3.409   1.00 118.04 ? 192 ASP   Y CG  1 
ATOM   44012 O  OD1 . ASP   Y  11 191 ? 73.377  -151.495 4.299   1.00 122.47 ? 192 ASP   Y OD1 1 
ATOM   44013 O  OD2 . ASP   Y  11 191 ? 71.837  -150.109 3.567   1.00 117.61 ? 192 ASP   Y OD2 1 
ATOM   44014 N  N   . VAL   Y  11 192 ? 69.654  -150.181 1.611   1.00 113.04 ? 193 VAL   Y N   1 
ATOM   44015 C  CA  . VAL   Y  11 192 ? 68.958  -148.906 1.257   1.00 112.32 ? 193 VAL   Y CA  1 
ATOM   44016 C  C   . VAL   Y  11 192 ? 69.932  -147.742 1.480   1.00 111.64 ? 193 VAL   Y C   1 
ATOM   44017 O  O   . VAL   Y  11 192 ? 69.838  -146.745 0.736   1.00 108.45 ? 193 VAL   Y O   1 
ATOM   44018 C  CB  . VAL   Y  11 192 ? 67.657  -148.724 2.064   1.00 110.16 ? 193 VAL   Y CB  1 
ATOM   44019 C  CG1 . VAL   Y  11 192 ? 67.010  -147.372 1.807   1.00 110.91 ? 193 VAL   Y CG1 1 
ATOM   44020 C  CG2 . VAL   Y  11 192 ? 66.665  -149.844 1.791   1.00 110.30 ? 193 VAL   Y CG2 1 
ATOM   44021 N  N   . GLY   Y  11 193 ? 70.826  -147.876 2.467   1.00 115.18 ? 194 GLY   Y N   1 
ATOM   44022 C  CA  . GLY   Y  11 193 ? 71.902  -146.912 2.770   1.00 117.71 ? 194 GLY   Y CA  1 
ATOM   44023 C  C   . GLY   Y  11 193 ? 72.584  -146.415 1.506   1.00 120.12 ? 194 GLY   Y C   1 
ATOM   44024 O  O   . GLY   Y  11 193 ? 72.667  -145.186 1.335   1.00 119.63 ? 194 GLY   Y O   1 
ATOM   44025 N  N   . GLU   Y  11 194 ? 73.032  -147.337 0.645   1.00 122.82 ? 195 GLU   Y N   1 
ATOM   44026 C  CA  . GLU   Y  11 194 ? 73.746  -147.033 -0.627  1.00 124.13 ? 195 GLU   Y CA  1 
ATOM   44027 C  C   . GLU   Y  11 194 ? 72.748  -146.930 -1.788  1.00 118.48 ? 195 GLU   Y C   1 
ATOM   44028 O  O   . GLU   Y  11 194 ? 72.942  -146.045 -2.642  1.00 116.02 ? 195 GLU   Y O   1 
ATOM   44029 C  CB  . GLU   Y  11 194 ? 74.799  -148.100 -0.945  1.00 129.86 ? 195 GLU   Y CB  1 
ATOM   44030 C  CG  . GLU   Y  11 194 ? 75.995  -148.087 -0.009  1.00 136.81 ? 195 GLU   Y CG  1 
ATOM   44031 C  CD  . GLU   Y  11 194 ? 75.978  -149.181 1.046   1.00 141.24 ? 195 GLU   Y CD  1 
ATOM   44032 O  OE1 . GLU   Y  11 194 ? 75.792  -148.853 2.235   1.00 146.61 ? 195 GLU   Y OE1 1 
ATOM   44033 O  OE2 . GLU   Y  11 194 ? 76.161  -150.359 0.675   1.00 146.97 ? 195 GLU   Y OE2 1 
ATOM   44034 N  N   . LEU   Y  11 195 ? 71.735  -147.805 -1.825  1.00 117.99 ? 196 LEU   Y N   1 
ATOM   44035 C  CA  . LEU   Y  11 195 ? 70.796  -147.953 -2.973  1.00 117.41 ? 196 LEU   Y CA  1 
ATOM   44036 C  C   . LEU   Y  11 195 ? 70.045  -146.638 -3.215  1.00 116.70 ? 196 LEU   Y C   1 
ATOM   44037 O  O   . LEU   Y  11 195 ? 69.903  -146.266 -4.395  1.00 115.98 ? 196 LEU   Y O   1 
ATOM   44038 C  CB  . LEU   Y  11 195 ? 69.816  -149.101 -2.705  1.00 117.91 ? 196 LEU   Y CB  1 
ATOM   44039 C  CG  . LEU   Y  11 195 ? 68.747  -149.331 -3.776  1.00 116.99 ? 196 LEU   Y CG  1 
ATOM   44040 C  CD1 . LEU   Y  11 195 ? 69.375  -149.618 -5.132  1.00 117.98 ? 196 LEU   Y CD1 1 
ATOM   44041 C  CD2 . LEU   Y  11 195 ? 67.817  -150.466 -3.374  1.00 115.87 ? 196 LEU   Y CD2 1 
ATOM   44042 N  N   . PHE   Y  11 196 ? 69.577  -145.973 -2.152  1.00 115.27 ? 197 PHE   Y N   1 
ATOM   44043 C  CA  . PHE   Y  11 196 ? 68.768  -144.726 -2.234  1.00 114.00 ? 197 PHE   Y CA  1 
ATOM   44044 C  C   . PHE   Y  11 196 ? 69.542  -143.650 -3.004  1.00 110.53 ? 197 PHE   Y C   1 
ATOM   44045 O  O   . PHE   Y  11 196 ? 68.988  -143.101 -3.973  1.00 105.80 ? 197 PHE   Y O   1 
ATOM   44046 C  CB  . PHE   Y  11 196 ? 68.387  -144.195 -0.849  1.00 114.15 ? 197 PHE   Y CB  1 
ATOM   44047 C  CG  . PHE   Y  11 196 ? 67.561  -142.934 -0.899  1.00 115.74 ? 197 PHE   Y CG  1 
ATOM   44048 C  CD1 . PHE   Y  11 196 ? 66.177  -142.997 -0.959  1.00 116.07 ? 197 PHE   Y CD1 1 
ATOM   44049 C  CD2 . PHE   Y  11 196 ? 68.166  -141.686 -0.921  1.00 116.22 ? 197 PHE   Y CD2 1 
ATOM   44050 C  CE1 . PHE   Y  11 196 ? 65.416  -141.839 -1.020  1.00 116.24 ? 197 PHE   Y CE1 1 
ATOM   44051 C  CE2 . PHE   Y  11 196 ? 67.404  -140.529 -0.986  1.00 116.79 ? 197 PHE   Y CE2 1 
ATOM   44052 C  CZ  . PHE   Y  11 196 ? 66.031  -140.608 -1.035  1.00 116.78 ? 197 PHE   Y CZ  1 
ATOM   44053 N  N   . TRP   Y  11 197 ? 70.773  -143.358 -2.570  1.00 113.42 ? 198 TRP   Y N   1 
ATOM   44054 C  CA  . TRP   Y  11 197 ? 71.656  -142.310 -3.153  1.00 118.74 ? 198 TRP   Y CA  1 
ATOM   44055 C  C   . TRP   Y  11 197 ? 72.010  -142.677 -4.600  1.00 121.69 ? 198 TRP   Y C   1 
ATOM   44056 O  O   . TRP   Y  11 197 ? 72.049  -141.765 -5.448  1.00 123.72 ? 198 TRP   Y O   1 
ATOM   44057 C  CB  . TRP   Y  11 197 ? 72.916  -142.110 -2.300  1.00 122.76 ? 198 TRP   Y CB  1 
ATOM   44058 C  CG  . TRP   Y  11 197 ? 72.644  -141.624 -0.910  1.00 125.43 ? 198 TRP   Y CG  1 
ATOM   44059 C  CD1 . TRP   Y  11 197 ? 72.897  -142.288 0.254   1.00 127.60 ? 198 TRP   Y CD1 1 
ATOM   44060 C  CD2 . TRP   Y  11 197 ? 72.051  -140.369 -0.534  1.00 128.37 ? 198 TRP   Y CD2 1 
ATOM   44061 N  NE1 . TRP   Y  11 197 ? 72.509  -141.535 1.328   1.00 131.00 ? 198 TRP   Y NE1 1 
ATOM   44062 C  CE2 . TRP   Y  11 197 ? 71.986  -140.352 0.876   1.00 131.46 ? 198 TRP   Y CE2 1 
ATOM   44063 C  CE3 . TRP   Y  11 197 ? 71.570  -139.263 -1.245  1.00 129.07 ? 198 TRP   Y CE3 1 
ATOM   44064 C  CZ2 . TRP   Y  11 197 ? 71.463  -139.270 1.583   1.00 133.56 ? 198 TRP   Y CZ2 1 
ATOM   44065 C  CZ3 . TRP   Y  11 197 ? 71.053  -138.195 -0.545  1.00 131.74 ? 198 TRP   Y CZ3 1 
ATOM   44066 C  CH2 . TRP   Y  11 197 ? 71.001  -138.201 0.850   1.00 133.37 ? 198 TRP   Y CH2 1 
ATOM   44067 N  N   . LYS   Y  11 198 ? 72.257  -143.964 -4.860  1.00 121.45 ? 199 LYS   Y N   1 
ATOM   44068 C  CA  . LYS   Y  11 198 ? 72.590  -144.510 -6.205  1.00 124.72 ? 199 LYS   Y CA  1 
ATOM   44069 C  C   . LYS   Y  11 198 ? 71.395  -144.315 -7.146  1.00 117.85 ? 199 LYS   Y C   1 
ATOM   44070 O  O   . LYS   Y  11 198 ? 71.610  -143.846 -8.278  1.00 116.14 ? 199 LYS   Y O   1 
ATOM   44071 C  CB  . LYS   Y  11 198 ? 72.976  -145.988 -6.085  1.00 126.61 ? 199 LYS   Y CB  1 
ATOM   44072 C  CG  . LYS   Y  11 198 ? 73.275  -146.705 -7.395  1.00 132.84 ? 199 LYS   Y CG  1 
ATOM   44073 C  CD  . LYS   Y  11 198 ? 73.708  -148.147 -7.192  1.00 134.83 ? 199 LYS   Y CD  1 
ATOM   44074 C  CE  . LYS   Y  11 198 ? 73.270  -149.078 -8.304  1.00 136.55 ? 199 LYS   Y CE  1 
ATOM   44075 N  NZ  . LYS   Y  11 198 ? 74.033  -148.844 -9.552  1.00 141.65 ? 199 LYS   Y NZ  1 
ATOM   44076 N  N   . VAL   Y  11 199 ? 70.187  -144.668 -6.694  1.00 116.66 ? 200 VAL   Y N   1 
ATOM   44077 C  CA  . VAL   Y  11 199 ? 68.920  -144.507 -7.469  1.00 116.33 ? 200 VAL   Y CA  1 
ATOM   44078 C  C   . VAL   Y  11 199 ? 68.668  -143.008 -7.681  1.00 117.75 ? 200 VAL   Y C   1 
ATOM   44079 O  O   . VAL   Y  11 199 ? 68.414  -142.626 -8.836  1.00 117.81 ? 200 VAL   Y O   1 
ATOM   44080 C  CB  . VAL   Y  11 199 ? 67.730  -145.210 -6.782  1.00 113.30 ? 200 VAL   Y CB  1 
ATOM   44081 C  CG1 . VAL   Y  11 199 ? 66.386  -144.720 -7.304  1.00 113.44 ? 200 VAL   Y CG1 1 
ATOM   44082 C  CG2 . VAL   Y  11 199 ? 67.823  -146.722 -6.915  1.00 112.87 ? 200 VAL   Y CG2 1 
ATOM   44083 N  N   . LYS   Y  11 200 ? 68.755  -142.198 -6.617  1.00 118.30 ? 201 LYS   Y N   1 
ATOM   44084 C  CA  . LYS   Y  11 200 ? 68.495  -140.730 -6.656  1.00 120.51 ? 201 LYS   Y CA  1 
ATOM   44085 C  C   . LYS   Y  11 200 ? 69.358  -140.095 -7.751  1.00 119.75 ? 201 LYS   Y C   1 
ATOM   44086 O  O   . LYS   Y  11 200 ? 68.793  -139.394 -8.609  1.00 117.89 ? 201 LYS   Y O   1 
ATOM   44087 C  CB  . LYS   Y  11 200 ? 68.781  -140.064 -5.304  1.00 121.57 ? 201 LYS   Y CB  1 
ATOM   44088 C  CG  . LYS   Y  11 200 ? 68.577  -138.552 -5.280  1.00 124.97 ? 201 LYS   Y CG  1 
ATOM   44089 C  CD  . LYS   Y  11 200 ? 68.741  -137.916 -3.913  1.00 124.31 ? 201 LYS   Y CD  1 
ATOM   44090 C  CE  . LYS   Y  11 200 ? 68.874  -136.406 -3.958  1.00 125.38 ? 201 LYS   Y CE  1 
ATOM   44091 N  NZ  . LYS   Y  11 200 ? 67.790  -135.765 -4.741  1.00 122.92 ? 201 LYS   Y NZ  1 
ATOM   44092 N  N   . GLU   Y  11 201 ? 70.670  -140.347 -7.716  1.00 122.91 ? 202 GLU   Y N   1 
ATOM   44093 C  CA  . GLU   Y  11 201 ? 71.666  -139.775 -8.662  1.00 127.70 ? 202 GLU   Y CA  1 
ATOM   44094 C  C   . GLU   Y  11 201 ? 71.342  -140.234 -10.090 1.00 129.32 ? 202 GLU   Y C   1 
ATOM   44095 O  O   . GLU   Y  11 201 ? 71.159  -139.365 -10.960 1.00 131.49 ? 202 GLU   Y O   1 
ATOM   44096 C  CB  . GLU   Y  11 201 ? 73.086  -140.183 -8.260  1.00 131.82 ? 202 GLU   Y CB  1 
ATOM   44097 C  CG  . GLU   Y  11 201 ? 74.150  -139.745 -9.251  1.00 135.22 ? 202 GLU   Y CG  1 
ATOM   44098 C  CD  . GLU   Y  11 201 ? 75.573  -139.850 -8.737  1.00 140.11 ? 202 GLU   Y CD  1 
ATOM   44099 O  OE1 . GLU   Y  11 201 ? 75.939  -139.054 -7.850  1.00 143.51 ? 202 GLU   Y OE1 1 
ATOM   44100 O  OE2 . GLU   Y  11 201 ? 76.309  -140.733 -9.220  1.00 142.99 ? 202 GLU   Y OE2 1 
ATOM   44101 N  N   . GLU   Y  11 202 ? 71.265  -141.549 -10.311 1.00 129.27 ? 203 GLU   Y N   1 
ATOM   44102 C  CA  . GLU   Y  11 202 ? 71.152  -142.174 -11.658 1.00 131.06 ? 203 GLU   Y CA  1 
ATOM   44103 C  C   . GLU   Y  11 202 ? 69.761  -141.931 -12.259 1.00 129.09 ? 203 GLU   Y C   1 
ATOM   44104 O  O   . GLU   Y  11 202 ? 69.688  -141.705 -13.479 1.00 130.18 ? 203 GLU   Y O   1 
ATOM   44105 C  CB  . GLU   Y  11 202 ? 71.443  -143.673 -11.578 1.00 132.46 ? 203 GLU   Y CB  1 
ATOM   44106 C  CG  . GLU   Y  11 202 ? 72.894  -143.987 -11.257 1.00 135.01 ? 203 GLU   Y CG  1 
ATOM   44107 C  CD  . GLU   Y  11 202 ? 73.230  -145.466 -11.176 1.00 135.10 ? 203 GLU   Y CD  1 
ATOM   44108 O  OE1 . GLU   Y  11 202 ? 72.353  -146.292 -11.495 1.00 135.29 ? 203 GLU   Y OE1 1 
ATOM   44109 O  OE2 . GLU   Y  11 202 ? 74.371  -145.789 -10.792 1.00 134.59 ? 203 GLU   Y OE2 1 
ATOM   44110 N  N   . GLU   Y  11 203 ? 68.704  -141.991 -11.443 1.00 129.66 ? 204 GLU   Y N   1 
ATOM   44111 C  CA  . GLU   Y  11 203 ? 67.290  -141.896 -11.902 1.00 129.77 ? 204 GLU   Y CA  1 
ATOM   44112 C  C   . GLU   Y  11 203 ? 66.855  -140.425 -11.971 1.00 128.23 ? 204 GLU   Y C   1 
ATOM   44113 O  O   . GLU   Y  11 203 ? 66.108  -140.084 -12.909 1.00 124.95 ? 204 GLU   Y O   1 
ATOM   44114 C  CB  . GLU   Y  11 203 ? 66.375  -142.701 -10.976 1.00 128.82 ? 204 GLU   Y CB  1 
ATOM   44115 C  CG  . GLU   Y  11 203 ? 65.032  -143.042 -11.594 1.00 131.50 ? 204 GLU   Y CG  1 
ATOM   44116 C  CD  . GLU   Y  11 203 ? 64.237  -144.091 -10.833 1.00 128.79 ? 204 GLU   Y CD  1 
ATOM   44117 O  OE1 . GLU   Y  11 203 ? 63.953  -145.152 -11.421 1.00 128.51 ? 204 GLU   Y OE1 1 
ATOM   44118 O  OE2 . GLU   Y  11 203 ? 63.898  -143.843 -9.659  1.00 132.53 ? 204 GLU   Y OE2 1 
ATOM   44119 N  N   . GLY   Y  11 204 ? 67.296  -139.598 -11.015 1.00 129.30 ? 205 GLY   Y N   1 
ATOM   44120 C  CA  . GLY   Y  11 204 ? 66.927  -138.172 -10.903 1.00 129.70 ? 205 GLY   Y CA  1 
ATOM   44121 C  C   . GLY   Y  11 204 ? 65.649  -137.966 -10.104 1.00 128.34 ? 205 GLY   Y C   1 
ATOM   44122 O  O   . GLY   Y  11 204 ? 65.121  -136.836 -10.126 1.00 131.24 ? 205 GLY   Y O   1 
ATOM   44123 N  N   . SER   Y  11 205 ? 65.170  -139.010 -9.419  1.00 123.53 ? 206 SER   Y N   1 
ATOM   44124 C  CA  . SER   Y  11 205 ? 63.968  -138.990 -8.544  1.00 121.88 ? 206 SER   Y CA  1 
ATOM   44125 C  C   . SER   Y  11 205 ? 64.384  -138.582 -7.126  1.00 124.51 ? 206 SER   Y C   1 
ATOM   44126 O  O   . SER   Y  11 205 ? 65.567  -138.237 -6.941  1.00 122.44 ? 206 SER   Y O   1 
ATOM   44127 C  CB  . SER   Y  11 205 ? 63.275  -140.328 -8.570  1.00 118.81 ? 206 SER   Y CB  1 
ATOM   44128 O  OG  . SER   Y  11 205 ? 64.182  -141.368 -8.241  1.00 116.18 ? 206 SER   Y OG  1 
ATOM   44129 N  N   . PHE   Y  11 206 ? 63.444  -138.607 -6.173  1.00 129.30 ? 207 PHE   Y N   1 
ATOM   44130 C  CA  . PHE   Y  11 206 ? 63.649  -138.244 -4.745  1.00 131.28 ? 207 PHE   Y CA  1 
ATOM   44131 C  C   . PHE   Y  11 206 ? 64.187  -136.807 -4.669  1.00 136.45 ? 207 PHE   Y C   1 
ATOM   44132 O  O   . PHE   Y  11 206 ? 65.287  -136.581 -4.120  1.00 137.72 ? 207 PHE   Y O   1 
ATOM   44133 C  CB  . PHE   Y  11 206 ? 64.551  -139.271 -4.050  1.00 130.90 ? 207 PHE   Y CB  1 
ATOM   44134 C  CG  . PHE   Y  11 206 ? 63.922  -140.629 -3.855  1.00 128.92 ? 207 PHE   Y CG  1 
ATOM   44135 C  CD1 . PHE   Y  11 206 ? 62.774  -140.776 -3.088  1.00 127.27 ? 207 PHE   Y CD1 1 
ATOM   44136 C  CD2 . PHE   Y  11 206 ? 64.481  -141.763 -4.426  1.00 128.16 ? 207 PHE   Y CD2 1 
ATOM   44137 C  CE1 . PHE   Y  11 206 ? 62.194  -142.023 -2.908  1.00 124.98 ? 207 PHE   Y CE1 1 
ATOM   44138 C  CE2 . PHE   Y  11 206 ? 63.902  -143.009 -4.241  1.00 127.28 ? 207 PHE   Y CE2 1 
ATOM   44139 C  CZ  . PHE   Y  11 206 ? 62.759  -143.137 -3.484  1.00 125.52 ? 207 PHE   Y CZ  1 
ATOM   44140 N  N   . ASN   Y  11 207 ? 63.418  -135.861 -5.217  1.00 136.93 ? 208 ASN   Y N   1 
ATOM   44141 C  CA  . ASN   Y  11 207 ? 63.740  -134.408 -5.235  1.00 140.39 ? 208 ASN   Y CA  1 
ATOM   44142 C  C   . ASN   Y  11 207 ? 63.273  -133.751 -3.930  1.00 135.52 ? 208 ASN   Y C   1 
ATOM   44143 O  O   . ASN   Y  11 207 ? 63.810  -132.681 -3.595  1.00 131.24 ? 208 ASN   Y O   1 
ATOM   44144 C  CB  . ASN   Y  11 207 ? 63.130  -133.726 -6.459  1.00 142.29 ? 208 ASN   Y CB  1 
ATOM   44145 C  CG  . ASN   Y  11 207 ? 63.723  -134.236 -7.755  1.00 144.82 ? 208 ASN   Y CG  1 
ATOM   44146 O  OD1 . ASN   Y  11 207 ? 63.107  -135.040 -8.450  1.00 148.47 ? 208 ASN   Y OD1 1 
ATOM   44147 N  ND2 . ASN   Y  11 207 ? 64.929  -133.794 -8.072  1.00 146.92 ? 208 ASN   Y ND2 1 
ATOM   44148 N  N   . ASN   Y  11 208 ? 62.314  -134.367 -3.227  1.00 144.96 ? 209 ASN   Y N   1 
ATOM   44149 C  CA  . ASN   Y  11 208 ? 61.868  -133.963 -1.864  1.00 148.74 ? 209 ASN   Y CA  1 
ATOM   44150 C  C   . ASN   Y  11 208 ? 63.080  -133.907 -0.920  1.00 149.65 ? 209 ASN   Y C   1 
ATOM   44151 O  O   . ASN   Y  11 208 ? 63.108  -133.005 -0.058  1.00 150.89 ? 209 ASN   Y O   1 
ATOM   44152 C  CB  . ASN   Y  11 208 ? 60.773  -134.888 -1.312  1.00 152.93 ? 209 ASN   Y CB  1 
ATOM   44153 C  CG  . ASN   Y  11 208 ? 61.183  -136.346 -1.222  1.00 150.91 ? 209 ASN   Y CG  1 
ATOM   44154 O  OD1 . ASN   Y  11 208 ? 61.982  -136.825 -2.023  1.00 155.66 ? 209 ASN   Y OD1 1 
ATOM   44155 N  ND2 . ASN   Y  11 208 ? 60.628  -137.068 -0.261  1.00 153.57 ? 209 ASN   Y ND2 1 
ATOM   44156 N  N   . VAL   Y  11 209 ? 64.045  -134.823 -1.088  1.00 152.16 ? 210 VAL   Y N   1 
ATOM   44157 C  CA  . VAL   Y  11 209 ? 65.211  -135.023 -0.172  1.00 144.90 ? 210 VAL   Y CA  1 
ATOM   44158 C  C   . VAL   Y  11 209 ? 66.328  -134.037 -0.532  1.00 146.15 ? 210 VAL   Y C   1 
ATOM   44159 O  O   . VAL   Y  11 209 ? 66.594  -133.855 -1.739  1.00 140.64 ? 210 VAL   Y O   1 
ATOM   44160 C  CB  . VAL   Y  11 209 ? 65.717  -136.480 -0.214  1.00 143.71 ? 210 VAL   Y CB  1 
ATOM   44161 C  CG1 . VAL   Y  11 209 ? 67.068  -136.641 0.471   1.00 142.51 ? 210 VAL   Y CG1 1 
ATOM   44162 C  CG2 . VAL   Y  11 209 ? 64.698  -137.436 0.388   1.00 136.40 ? 210 VAL   Y CG2 1 
ATOM   44163 N  N   . ILE   Y  11 210 ? 66.968  -133.457 0.491   1.00 149.79 ? 211 ILE   Y N   1 
ATOM   44164 C  CA  . ILE   Y  11 210 ? 68.159  -132.564 0.359   1.00 148.51 ? 211 ILE   Y CA  1 
ATOM   44165 C  C   . ILE   Y  11 210 ? 69.305  -133.396 -0.233  1.00 145.35 ? 211 ILE   Y C   1 
ATOM   44166 O  O   . ILE   Y  11 210 ? 69.755  -134.351 0.437   1.00 136.98 ? 211 ILE   Y O   1 
ATOM   44167 C  CB  . ILE   Y  11 210 ? 68.522  -131.908 1.712   1.00 154.65 ? 211 ILE   Y CB  1 
ATOM   44168 C  CG1 . ILE   Y  11 210 ? 67.433  -130.929 2.165   1.00 150.93 ? 211 ILE   Y CG1 1 
ATOM   44169 C  CG2 . ILE   Y  11 210 ? 69.890  -131.238 1.649   1.00 157.33 ? 211 ILE   Y CG2 1 
ATOM   44170 C  CD1 . ILE   Y  11 210 ? 67.655  -130.320 3.533   1.00 151.28 ? 211 ILE   Y CD1 1 
ATOM   44171 N  N   . GLY   Y  11 211 ? 69.735  -133.047 -1.450  1.00 145.38 ? 212 GLY   Y N   1 
ATOM   44172 C  CA  . GLY   Y  11 211 ? 70.740  -133.787 -2.239  1.00 147.27 ? 212 GLY   Y CA  1 
ATOM   44173 C  C   . GLY   Y  11 211 ? 72.123  -133.714 -1.616  1.00 146.88 ? 212 GLY   Y C   1 
ATOM   44174 O  O   . GLY   Y  11 211 ? 72.424  -132.816 -0.832  1.00 157.71 ? 212 GLY   Y O   1 
ATOM   44175 O  OXT . GLY   Y  11 211 ? 72.977  -134.558 -1.886  1.00 143.92 ? 212 GLY   Y OXT 1 
ATOM   44176 N  N   . GLN   Z  12 1   ? 43.537  -157.882 40.660  1.00 114.35 ? 1   GLN   Z N   1 
ATOM   44177 C  CA  . GLN   Z  12 1   ? 43.681  -159.136 39.852  1.00 111.14 ? 1   GLN   Z CA  1 
ATOM   44178 C  C   . GLN   Z  12 1   ? 45.156  -159.560 39.864  1.00 103.65 ? 1   GLN   Z C   1 
ATOM   44179 O  O   . GLN   Z  12 1   ? 46.023  -158.672 39.774  1.00 106.96 ? 1   GLN   Z O   1 
ATOM   44180 C  CB  . GLN   Z  12 1   ? 43.162  -158.919 38.425  1.00 117.19 ? 1   GLN   Z CB  1 
ATOM   44181 C  CG  . GLN   Z  12 1   ? 42.381  -160.097 37.850  1.00 121.00 ? 1   GLN   Z CG  1 
ATOM   44182 C  CD  . GLN   Z  12 1   ? 43.207  -160.993 36.958  1.00 122.00 ? 1   GLN   Z CD  1 
ATOM   44183 O  OE1 . GLN   Z  12 1   ? 43.209  -160.852 35.738  1.00 125.20 ? 1   GLN   Z OE1 1 
ATOM   44184 N  NE2 . GLN   Z  12 1   ? 43.914  -161.937 37.560  1.00 125.75 ? 1   GLN   Z NE2 1 
ATOM   44185 N  N   . PHE   Z  12 2   ? 45.422  -160.861 40.002  1.00 99.50  ? 2   PHE   Z N   1 
ATOM   44186 C  CA  . PHE   Z  12 2   ? 46.785  -161.455 39.996  1.00 93.68  ? 2   PHE   Z CA  1 
ATOM   44187 C  C   . PHE   Z  12 2   ? 47.443  -161.243 38.626  1.00 87.90  ? 2   PHE   Z C   1 
ATOM   44188 O  O   . PHE   Z  12 2   ? 46.875  -161.677 37.604  1.00 84.78  ? 2   PHE   Z O   1 
ATOM   44189 C  CB  . PHE   Z  12 2   ? 46.738  -162.946 40.343  1.00 93.29  ? 2   PHE   Z CB  1 
ATOM   44190 C  CG  . PHE   Z  12 2   ? 48.065  -163.649 40.209  1.00 88.71  ? 2   PHE   Z CG  1 
ATOM   44191 C  CD1 . PHE   Z  12 2   ? 49.158  -163.243 40.961  1.00 89.80  ? 2   PHE   Z CD1 1 
ATOM   44192 C  CD2 . PHE   Z  12 2   ? 48.229  -164.702 39.325  1.00 86.88  ? 2   PHE   Z CD2 1 
ATOM   44193 C  CE1 . PHE   Z  12 2   ? 50.383  -163.881 40.836  1.00 88.10  ? 2   PHE   Z CE1 1 
ATOM   44194 C  CE2 . PHE   Z  12 2   ? 49.455  -165.340 39.202  1.00 87.11  ? 2   PHE   Z CE2 1 
ATOM   44195 C  CZ  . PHE   Z  12 2   ? 50.529  -164.928 39.957  1.00 86.48  ? 2   PHE   Z CZ  1 
ATOM   44196 N  N   . ASN   Z  12 3   ? 48.614  -160.597 38.626  1.00 85.17  ? 3   ASN   Z N   1 
ATOM   44197 C  CA  . ASN   Z  12 3   ? 49.477  -160.370 37.436  1.00 83.38  ? 3   ASN   Z CA  1 
ATOM   44198 C  C   . ASN   Z  12 3   ? 50.593  -161.408 37.471  1.00 83.14  ? 3   ASN   Z C   1 
ATOM   44199 O  O   . ASN   Z  12 3   ? 51.465  -161.339 38.334  1.00 81.45  ? 3   ASN   Z O   1 
ATOM   44200 C  CB  . ASN   Z  12 3   ? 50.012  -158.933 37.421  1.00 83.86  ? 3   ASN   Z CB  1 
ATOM   44201 C  CG  . ASN   Z  12 3   ? 50.964  -158.605 36.286  1.00 84.47  ? 3   ASN   Z CG  1 
ATOM   44202 O  OD1 . ASN   Z  12 3   ? 51.693  -157.619 36.364  1.00 90.60  ? 3   ASN   Z OD1 1 
ATOM   44203 N  ND2 . ASN   Z  12 3   ? 50.972  -159.395 35.226  1.00 84.81  ? 3   ASN   Z ND2 1 
ATOM   44204 N  N   . PRO   Z  12 4   ? 50.599  -162.411 36.561  1.00 83.65  ? 4   PRO   Z N   1 
ATOM   44205 C  CA  . PRO   Z  12 4   ? 51.587  -163.491 36.621  1.00 84.40  ? 4   PRO   Z CA  1 
ATOM   44206 C  C   . PRO   Z  12 4   ? 53.016  -163.093 36.219  1.00 81.32  ? 4   PRO   Z C   1 
ATOM   44207 O  O   . PRO   Z  12 4   ? 53.912  -163.883 36.444  1.00 78.60  ? 4   PRO   Z O   1 
ATOM   44208 C  CB  . PRO   Z  12 4   ? 51.035  -164.525 35.626  1.00 84.73  ? 4   PRO   Z CB  1 
ATOM   44209 C  CG  . PRO   Z  12 4   ? 50.262  -163.695 34.625  1.00 85.55  ? 4   PRO   Z CG  1 
ATOM   44210 C  CD  . PRO   Z  12 4   ? 49.645  -162.587 35.452  1.00 84.30  ? 4   PRO   Z CD  1 
ATOM   44211 N  N   . TYR   Z  12 5   ? 53.195  -161.901 35.643  1.00 82.67  ? 5   TYR   Z N   1 
ATOM   44212 C  CA  . TYR   Z  12 5   ? 54.495  -161.396 35.131  1.00 82.01  ? 5   TYR   Z CA  1 
ATOM   44213 C  C   . TYR   Z  12 5   ? 55.084  -160.355 36.089  1.00 82.93  ? 5   TYR   Z C   1 
ATOM   44214 O  O   . TYR   Z  12 5   ? 54.324  -159.672 36.806  1.00 86.78  ? 5   TYR   Z O   1 
ATOM   44215 C  CB  . TYR   Z  12 5   ? 54.323  -160.795 33.735  1.00 82.53  ? 5   TYR   Z CB  1 
ATOM   44216 C  CG  . TYR   Z  12 5   ? 53.941  -161.792 32.671  1.00 81.33  ? 5   TYR   Z CG  1 
ATOM   44217 C  CD1 . TYR   Z  12 5   ? 54.821  -162.789 32.288  1.00 81.14  ? 5   TYR   Z CD1 1 
ATOM   44218 C  CD2 . TYR   Z  12 5   ? 52.707  -161.738 32.044  1.00 80.40  ? 5   TYR   Z CD2 1 
ATOM   44219 C  CE1 . TYR   Z  12 5   ? 54.487  -163.713 31.312  1.00 79.42  ? 5   TYR   Z CE1 1 
ATOM   44220 C  CE2 . TYR   Z  12 5   ? 52.356  -162.653 31.064  1.00 79.89  ? 5   TYR   Z CE2 1 
ATOM   44221 C  CZ  . TYR   Z  12 5   ? 53.249  -163.645 30.698  1.00 79.49  ? 5   TYR   Z CZ  1 
ATOM   44222 O  OH  . TYR   Z  12 5   ? 52.921  -164.556 29.737  1.00 79.27  ? 5   TYR   Z OH  1 
ATOM   44223 N  N   . GLY   Z  12 6   ? 56.416  -160.252 36.074  1.00 82.46  ? 6   GLY   Z N   1 
ATOM   44224 C  CA  . GLY   Z  12 6   ? 57.214  -159.207 36.742  1.00 82.85  ? 6   GLY   Z CA  1 
ATOM   44225 C  C   . GLY   Z  12 6   ? 58.406  -158.817 35.883  1.00 82.42  ? 6   GLY   Z C   1 
ATOM   44226 O  O   . GLY   Z  12 6   ? 58.675  -159.524 34.898  1.00 79.33  ? 6   GLY   Z O   1 
ATOM   44227 N  N   . ASP   Z  12 7   ? 59.089  -157.724 36.225  1.00 87.14  ? 7   ASP   Z N   1 
ATOM   44228 C  CA  . ASP   Z  12 7   ? 60.303  -157.250 35.511  1.00 91.02  ? 7   ASP   Z CA  1 
ATOM   44229 C  C   . ASP   Z  12 7   ? 61.472  -157.250 36.498  1.00 92.29  ? 7   ASP   Z C   1 
ATOM   44230 O  O   . ASP   Z  12 7   ? 61.417  -156.488 37.485  1.00 91.38  ? 7   ASP   Z O   1 
ATOM   44231 C  CB  . ASP   Z  12 7   ? 60.088  -155.869 34.888  1.00 96.25  ? 7   ASP   Z CB  1 
ATOM   44232 C  CG  . ASP   Z  12 7   ? 61.249  -155.395 34.027  1.00 103.29 ? 7   ASP   Z CG  1 
ATOM   44233 O  OD1 . ASP   Z  12 7   ? 62.202  -156.189 33.826  1.00 98.57  ? 7   ASP   Z OD1 1 
ATOM   44234 O  OD2 . ASP   Z  12 7   ? 61.192  -154.232 33.560  1.00 105.92 ? 7   ASP   Z OD2 1 
ATOM   44235 N  N   . ASN   Z  12 8   ? 62.484  -158.078 36.227  1.00 91.31  ? 8   ASN   Z N   1 
ATOM   44236 C  CA  . ASN   Z  12 8   ? 63.682  -158.259 37.088  1.00 88.85  ? 8   ASN   Z CA  1 
ATOM   44237 C  C   . ASN   Z  12 8   ? 64.864  -157.473 36.510  1.00 88.29  ? 8   ASN   Z C   1 
ATOM   44238 O  O   . ASN   Z  12 8   ? 65.996  -157.669 37.002  1.00 87.28  ? 8   ASN   Z O   1 
ATOM   44239 C  CB  . ASN   Z  12 8   ? 64.000  -159.741 37.281  1.00 88.17  ? 8   ASN   Z CB  1 
ATOM   44240 C  CG  . ASN   Z  12 8   ? 62.933  -160.444 38.091  1.00 90.02  ? 8   ASN   Z CG  1 
ATOM   44241 O  OD1 . ASN   Z  12 8   ? 62.217  -161.296 37.569  1.00 91.59  ? 8   ASN   Z OD1 1 
ATOM   44242 N  ND2 . ASN   Z  12 8   ? 62.802  -160.075 39.355  1.00 87.37  ? 8   ASN   Z ND2 1 
ATOM   44243 N  N   . GLY   Z  12 9   ? 64.611  -156.616 35.515  1.00 87.05  ? 9   GLY   Z N   1 
ATOM   44244 C  CA  . GLY   Z  12 9   ? 65.583  -155.630 35.005  1.00 88.91  ? 9   GLY   Z CA  1 
ATOM   44245 C  C   . GLY   Z  12 9   ? 66.820  -156.296 34.432  1.00 89.88  ? 9   GLY   Z C   1 
ATOM   44246 O  O   . GLY   Z  12 9   ? 66.690  -157.385 33.849  1.00 89.91  ? 9   GLY   Z O   1 
ATOM   44247 N  N   . GLY   Z  12 10  ? 67.982  -155.655 34.592  1.00 94.10  ? 10  GLY   Z N   1 
ATOM   44248 C  CA  . GLY   Z  12 10  ? 69.270  -156.128 34.051  1.00 95.72  ? 10  GLY   Z CA  1 
ATOM   44249 C  C   . GLY   Z  12 10  ? 69.292  -156.078 32.533  1.00 95.68  ? 10  GLY   Z C   1 
ATOM   44250 O  O   . GLY   Z  12 10  ? 68.224  -155.860 31.928  1.00 93.11  ? 10  GLY   Z O   1 
ATOM   44251 N  N   . THR   Z  12 11  ? 70.469  -156.272 31.934  1.00 95.27  ? 11  THR   Z N   1 
ATOM   44252 C  CA  . THR   Z  12 11  ? 70.689  -156.225 30.464  1.00 95.66  ? 11  THR   Z CA  1 
ATOM   44253 C  C   . THR   Z  12 11  ? 71.766  -157.251 30.088  1.00 95.25  ? 11  THR   Z C   1 
ATOM   44254 O  O   . THR   Z  12 11  ? 72.573  -157.609 30.968  1.00 97.56  ? 11  THR   Z O   1 
ATOM   44255 C  CB  . THR   Z  12 11  ? 71.010  -154.790 30.015  1.00 98.95  ? 11  THR   Z CB  1 
ATOM   44256 O  OG1 . THR   Z  12 11  ? 70.724  -154.679 28.620  1.00 96.46  ? 11  THR   Z OG1 1 
ATOM   44257 C  CG2 . THR   Z  12 11  ? 72.442  -154.378 30.284  1.00 99.84  ? 11  THR   Z CG2 1 
ATOM   44258 N  N   . ILE   Z  12 12  ? 71.765  -157.707 28.832  1.00 92.55  ? 12  ILE   Z N   1 
ATOM   44259 C  CA  . ILE   Z  12 12  ? 72.718  -158.727 28.298  1.00 96.23  ? 12  ILE   Z CA  1 
ATOM   44260 C  C   . ILE   Z  12 12  ? 73.180  -158.308 26.899  1.00 97.06  ? 12  ILE   Z C   1 
ATOM   44261 O  O   . ILE   Z  12 12  ? 72.503  -157.471 26.275  1.00 99.03  ? 12  ILE   Z O   1 
ATOM   44262 C  CB  . ILE   Z  12 12  ? 72.073  -160.125 28.291  1.00 95.44  ? 12  ILE   Z CB  1 
ATOM   44263 C  CG1 . ILE   Z  12 12  ? 70.714  -160.118 27.586  1.00 96.47  ? 12  ILE   Z CG1 1 
ATOM   44264 C  CG2 . ILE   Z  12 12  ? 71.973  -160.670 29.707  1.00 94.30  ? 12  ILE   Z CG2 1 
ATOM   44265 C  CD1 . ILE   Z  12 12  ? 70.220  -161.488 27.193  1.00 97.14  ? 12  ILE   Z CD1 1 
ATOM   44266 N  N   . LEU   Z  12 13  ? 74.279  -158.900 26.425  1.00 98.79  ? 13  LEU   Z N   1 
ATOM   44267 C  CA  . LEU   Z  12 13  ? 75.010  -158.464 25.206  1.00 102.10 ? 13  LEU   Z CA  1 
ATOM   44268 C  C   . LEU   Z  12 13  ? 75.862  -159.628 24.680  1.00 103.50 ? 13  LEU   Z C   1 
ATOM   44269 O  O   . LEU   Z  12 13  ? 76.652  -160.183 25.468  1.00 107.90 ? 13  LEU   Z O   1 
ATOM   44270 C  CB  . LEU   Z  12 13  ? 75.837  -157.229 25.589  1.00 103.55 ? 13  LEU   Z CB  1 
ATOM   44271 C  CG  . LEU   Z  12 13  ? 77.199  -157.050 24.920  1.00 107.47 ? 13  LEU   Z CG  1 
ATOM   44272 C  CD1 . LEU   Z  12 13  ? 77.055  -156.870 23.421  1.00 105.28 ? 13  LEU   Z CD1 1 
ATOM   44273 C  CD2 . LEU   Z  12 13  ? 77.930  -155.856 25.519  1.00 111.62 ? 13  LEU   Z CD2 1 
ATOM   44274 N  N   . GLY   Z  12 14  ? 75.690  -159.986 23.401  1.00 101.25 ? 14  GLY   Z N   1 
ATOM   44275 C  CA  . GLY   Z  12 14  ? 76.409  -161.089 22.730  1.00 98.64  ? 14  GLY   Z CA  1 
ATOM   44276 C  C   . GLY   Z  12 14  ? 77.110  -160.630 21.462  1.00 97.39  ? 14  GLY   Z C   1 
ATOM   44277 O  O   . GLY   Z  12 14  ? 76.409  -160.164 20.543  1.00 96.74  ? 14  GLY   Z O   1 
ATOM   44278 N  N   . ILE   Z  12 15  ? 78.441  -160.760 21.411  1.00 99.44  ? 15  ILE   Z N   1 
ATOM   44279 C  CA  . ILE   Z  12 15  ? 79.294  -160.409 20.234  1.00 103.97 ? 15  ILE   Z CA  1 
ATOM   44280 C  C   . ILE   Z  12 15  ? 79.994  -161.687 19.754  1.00 105.55 ? 15  ILE   Z C   1 
ATOM   44281 O  O   . ILE   Z  12 15  ? 80.311  -162.542 20.608  1.00 108.42 ? 15  ILE   Z O   1 
ATOM   44282 C  CB  . ILE   Z  12 15  ? 80.295  -159.285 20.581  1.00 105.85 ? 15  ILE   Z CB  1 
ATOM   44283 C  CG1 . ILE   Z  12 15  ? 79.586  -158.043 21.132  1.00 106.50 ? 15  ILE   Z CG1 1 
ATOM   44284 C  CG2 . ILE   Z  12 15  ? 81.168  -158.945 19.378  1.00 106.69 ? 15  ILE   Z CG2 1 
ATOM   44285 C  CD1 . ILE   Z  12 15  ? 80.509  -157.021 21.769  1.00 106.62 ? 15  ILE   Z CD1 1 
ATOM   44286 N  N   . ALA   Z  12 16  ? 80.220  -161.805 18.441  1.00 104.11 ? 16  ALA   Z N   1 
ATOM   44287 C  CA  . ALA   Z  12 16  ? 80.843  -162.976 17.780  1.00 105.51 ? 16  ALA   Z CA  1 
ATOM   44288 C  C   . ALA   Z  12 16  ? 82.107  -162.554 17.023  1.00 108.43 ? 16  ALA   Z C   1 
ATOM   44289 O  O   . ALA   Z  12 16  ? 81.997  -161.690 16.135  1.00 110.49 ? 16  ALA   Z O   1 
ATOM   44290 C  CB  . ALA   Z  12 16  ? 79.849  -163.613 16.846  1.00 104.70 ? 16  ALA   Z CB  1 
ATOM   44291 N  N   . GLY   Z  12 17  ? 83.252  -163.164 17.353  1.00 113.92 ? 17  GLY   Z N   1 
ATOM   44292 C  CA  . GLY   Z  12 17  ? 84.528  -163.011 16.625  1.00 119.93 ? 17  GLY   Z CA  1 
ATOM   44293 C  C   . GLY   Z  12 17  ? 84.674  -164.057 15.531  1.00 122.80 ? 17  GLY   Z C   1 
ATOM   44294 O  O   . GLY   Z  12 17  ? 83.664  -164.710 15.197  1.00 123.85 ? 17  GLY   Z O   1 
ATOM   44295 N  N   . GLU   Z  12 18  ? 85.888  -164.217 14.995  1.00 127.82 ? 18  GLU   Z N   1 
ATOM   44296 C  CA  . GLU   Z  12 18  ? 86.197  -165.160 13.887  1.00 127.88 ? 18  GLU   Z CA  1 
ATOM   44297 C  C   . GLU   Z  12 18  ? 86.230  -166.599 14.418  1.00 125.66 ? 18  GLU   Z C   1 
ATOM   44298 O  O   . GLU   Z  12 18  ? 85.725  -167.480 13.705  1.00 124.82 ? 18  GLU   Z O   1 
ATOM   44299 C  CB  . GLU   Z  12 18  ? 87.525  -164.806 13.215  1.00 133.27 ? 18  GLU   Z CB  1 
ATOM   44300 C  CG  . GLU   Z  12 18  ? 87.768  -165.569 11.923  1.00 136.52 ? 18  GLU   Z CG  1 
ATOM   44301 C  CD  . GLU   Z  12 18  ? 89.043  -165.195 11.188  1.00 142.08 ? 18  GLU   Z CD  1 
ATOM   44302 O  OE1 . GLU   Z  12 18  ? 89.628  -164.142 11.514  1.00 143.83 ? 18  GLU   Z OE1 1 
ATOM   44303 O  OE2 . GLU   Z  12 18  ? 89.450  -165.960 10.290  1.00 144.88 ? 18  GLU   Z OE2 1 
ATOM   44304 N  N   . ASP   Z  12 19  ? 86.819  -166.828 15.598  1.00 124.24 ? 19  ASP   Z N   1 
ATOM   44305 C  CA  . ASP   Z  12 19  ? 86.983  -168.184 16.195  1.00 123.67 ? 19  ASP   Z CA  1 
ATOM   44306 C  C   . ASP   Z  12 19  ? 86.516  -168.199 17.658  1.00 121.59 ? 19  ASP   Z C   1 
ATOM   44307 O  O   . ASP   Z  12 19  ? 86.854  -169.172 18.366  1.00 119.33 ? 19  ASP   Z O   1 
ATOM   44308 C  CB  . ASP   Z  12 19  ? 88.432  -168.668 16.070  1.00 126.72 ? 19  ASP   Z CB  1 
ATOM   44309 C  CG  . ASP   Z  12 19  ? 89.433  -167.858 16.876  1.00 125.35 ? 19  ASP   Z CG  1 
ATOM   44310 O  OD1 . ASP   Z  12 19  ? 89.262  -166.625 16.959  1.00 124.31 ? 19  ASP   Z OD1 1 
ATOM   44311 O  OD2 . ASP   Z  12 19  ? 90.377  -168.469 17.414  1.00 130.54 ? 19  ASP   Z OD2 1 
ATOM   44312 N  N   . PHE   Z  12 20  ? 85.758  -167.187 18.093  1.00 118.61 ? 20  PHE   Z N   1 
ATOM   44313 C  CA  . PHE   Z  12 20  ? 85.227  -167.075 19.478  1.00 115.46 ? 20  PHE   Z CA  1 
ATOM   44314 C  C   . PHE   Z  12 20  ? 83.898  -166.315 19.470  1.00 110.85 ? 20  PHE   Z C   1 
ATOM   44315 O  O   . PHE   Z  12 20  ? 83.553  -165.700 18.444  1.00 113.75 ? 20  PHE   Z O   1 
ATOM   44316 C  CB  . PHE   Z  12 20  ? 86.235  -166.371 20.389  1.00 117.19 ? 20  PHE   Z CB  1 
ATOM   44317 C  CG  . PHE   Z  12 20  ? 86.338  -164.884 20.166  1.00 118.40 ? 20  PHE   Z CG  1 
ATOM   44318 C  CD1 . PHE   Z  12 20  ? 87.099  -164.376 19.124  1.00 120.74 ? 20  PHE   Z CD1 1 
ATOM   44319 C  CD2 . PHE   Z  12 20  ? 85.662  -163.994 20.987  1.00 119.79 ? 20  PHE   Z CD2 1 
ATOM   44320 C  CE1 . PHE   Z  12 20  ? 87.191  -163.009 18.914  1.00 122.77 ? 20  PHE   Z CE1 1 
ATOM   44321 C  CE2 . PHE   Z  12 20  ? 85.751  -162.628 20.772  1.00 121.12 ? 20  PHE   Z CE2 1 
ATOM   44322 C  CZ  . PHE   Z  12 20  ? 86.512  -162.138 19.734  1.00 123.54 ? 20  PHE   Z CZ  1 
ATOM   44323 N  N   . ALA   Z  12 21  ? 83.186  -166.357 20.599  1.00 108.17 ? 21  ALA   Z N   1 
ATOM   44324 C  CA  . ALA   Z  12 21  ? 81.947  -165.590 20.863  1.00 104.88 ? 21  ALA   Z CA  1 
ATOM   44325 C  C   . ALA   Z  12 21  ? 81.851  -165.298 22.362  1.00 105.02 ? 21  ALA   Z C   1 
ATOM   44326 O  O   . ALA   Z  12 21  ? 82.170  -166.201 23.161  1.00 108.45 ? 21  ALA   Z O   1 
ATOM   44327 C  CB  . ALA   Z  12 21  ? 80.746  -166.361 20.376  1.00 103.10 ? 21  ALA   Z CB  1 
ATOM   44328 N  N   . VAL   Z  12 22  ? 81.437  -164.081 22.720  1.00 102.32 ? 22  VAL   Z N   1 
ATOM   44329 C  CA  . VAL   Z  12 22  ? 81.211  -163.658 24.135  1.00 103.22 ? 22  VAL   Z CA  1 
ATOM   44330 C  C   . VAL   Z  12 22  ? 79.713  -163.429 24.342  1.00 98.43  ? 22  VAL   Z C   1 
ATOM   44331 O  O   . VAL   Z  12 22  ? 79.054  -162.931 23.410  1.00 95.72  ? 22  VAL   Z O   1 
ATOM   44332 C  CB  . VAL   Z  12 22  ? 82.026  -162.405 24.511  1.00 105.18 ? 22  VAL   Z CB  1 
ATOM   44333 C  CG1 . VAL   Z  12 22  ? 83.522  -162.677 24.471  1.00 110.66 ? 22  VAL   Z CG1 1 
ATOM   44334 C  CG2 . VAL   Z  12 22  ? 81.676  -161.202 23.649  1.00 105.14 ? 22  VAL   Z CG2 1 
ATOM   44335 N  N   . LEU   Z  12 23  ? 79.209  -163.807 25.518  1.00 98.13  ? 23  LEU   Z N   1 
ATOM   44336 C  CA  . LEU   Z  12 23  ? 77.837  -163.503 25.998  1.00 97.77  ? 23  LEU   Z CA  1 
ATOM   44337 C  C   . LEU   Z  12 23  ? 77.967  -162.892 27.395  1.00 99.04  ? 23  LEU   Z C   1 
ATOM   44338 O  O   . LEU   Z  12 23  ? 78.296  -163.636 28.337  1.00 103.24 ? 23  LEU   Z O   1 
ATOM   44339 C  CB  . LEU   Z  12 23  ? 77.000  -164.788 26.022  1.00 96.88  ? 23  LEU   Z CB  1 
ATOM   44340 C  CG  . LEU   Z  12 23  ? 75.515  -164.643 25.684  1.00 97.00  ? 23  LEU   Z CG  1 
ATOM   44341 C  CD1 . LEU   Z  12 23  ? 74.728  -165.840 26.198  1.00 96.17  ? 23  LEU   Z CD1 1 
ATOM   44342 C  CD2 . LEU   Z  12 23  ? 74.922  -163.356 26.241  1.00 96.92  ? 23  LEU   Z CD2 1 
ATOM   44343 N  N   . ALA   Z  12 24  ? 77.765  -161.578 27.509  1.00 96.93  ? 24  ALA   Z N   1 
ATOM   44344 C  CA  . ALA   Z  12 24  ? 77.933  -160.803 28.758  1.00 96.17  ? 24  ALA   Z CA  1 
ATOM   44345 C  C   . ALA   Z  12 24  ? 76.563  -160.401 29.312  1.00 89.69  ? 24  ALA   Z C   1 
ATOM   44346 O  O   . ALA   Z  12 24  ? 75.624  -160.210 28.519  1.00 86.84  ? 24  ALA   Z O   1 
ATOM   44347 C  CB  . ALA   Z  12 24  ? 78.797  -159.597 28.493  1.00 98.69  ? 24  ALA   Z CB  1 
ATOM   44348 N  N   . GLY   Z  12 25  ? 76.468  -160.282 30.636  1.00 90.34  ? 25  GLY   Z N   1 
ATOM   44349 C  CA  . GLY   Z  12 25  ? 75.270  -159.795 31.342  1.00 93.13  ? 25  GLY   Z CA  1 
ATOM   44350 C  C   . GLY   Z  12 25  ? 75.634  -159.270 32.716  1.00 95.68  ? 25  GLY   Z C   1 
ATOM   44351 O  O   . GLY   Z  12 25  ? 76.470  -159.911 33.384  1.00 103.71 ? 25  GLY   Z O   1 
ATOM   44352 N  N   . ASP   Z  12 26  ? 75.045  -158.142 33.122  1.00 96.79  ? 26  ASP   Z N   1 
ATOM   44353 C  CA  . ASP   Z  12 26  ? 75.210  -157.569 34.484  1.00 101.56 ? 26  ASP   Z CA  1 
ATOM   44354 C  C   . ASP   Z  12 26  ? 74.574  -158.534 35.487  1.00 98.15  ? 26  ASP   Z C   1 
ATOM   44355 O  O   . ASP   Z  12 26  ? 73.695  -159.315 35.078  1.00 99.16  ? 26  ASP   Z O   1 
ATOM   44356 C  CB  . ASP   Z  12 26  ? 74.596  -156.171 34.604  1.00 106.88 ? 26  ASP   Z CB  1 
ATOM   44357 C  CG  . ASP   Z  12 26  ? 73.080  -156.149 34.486  1.00 110.67 ? 26  ASP   Z CG  1 
ATOM   44358 O  OD1 . ASP   Z  12 26  ? 72.536  -157.001 33.753  1.00 115.71 ? 26  ASP   Z OD1 1 
ATOM   44359 O  OD2 . ASP   Z  12 26  ? 72.452  -155.285 35.133  1.00 109.93 ? 26  ASP   Z OD2 1 
ATOM   44360 N  N   . THR   Z  12 27  ? 74.993  -158.468 36.751  1.00 98.03  ? 27  THR   Z N   1 
ATOM   44361 C  CA  . THR   Z  12 27  ? 74.625  -159.450 37.804  1.00 96.44  ? 27  THR   Z CA  1 
ATOM   44362 C  C   . THR   Z  12 27  ? 73.567  -158.857 38.742  1.00 96.46  ? 27  THR   Z C   1 
ATOM   44363 O  O   . THR   Z  12 27  ? 73.216  -159.538 39.724  1.00 97.15  ? 27  THR   Z O   1 
ATOM   44364 C  CB  . THR   Z  12 27  ? 75.879  -159.911 38.555  1.00 95.40  ? 27  THR   Z CB  1 
ATOM   44365 O  OG1 . THR   Z  12 27  ? 76.481  -158.768 39.162  1.00 95.59  ? 27  THR   Z OG1 1 
ATOM   44366 C  CG2 . THR   Z  12 27  ? 76.876  -160.602 37.652  1.00 97.16  ? 27  THR   Z CG2 1 
ATOM   44367 N  N   . ARG   Z  12 28  ? 73.069  -157.652 38.451  1.00 97.08  ? 28  ARG   Z N   1 
ATOM   44368 C  CA  . ARG   Z  12 28  ? 72.032  -156.970 39.270  1.00 99.06  ? 28  ARG   Z CA  1 
ATOM   44369 C  C   . ARG   Z  12 28  ? 70.656  -157.572 38.954  1.00 95.55  ? 28  ARG   Z C   1 
ATOM   44370 O  O   . ARG   Z  12 28  ? 70.339  -157.736 37.758  1.00 98.24  ? 28  ARG   Z O   1 
ATOM   44371 C  CB  . ARG   Z  12 28  ? 72.045  -155.458 39.019  1.00 103.28 ? 28  ARG   Z CB  1 
ATOM   44372 C  CG  . ARG   Z  12 28  ? 70.959  -154.695 39.766  1.00 107.43 ? 28  ARG   Z CG  1 
ATOM   44373 C  CD  . ARG   Z  12 28  ? 71.036  -153.193 39.558  1.00 107.05 ? 28  ARG   Z CD  1 
ATOM   44374 N  NE  . ARG   Z  12 28  ? 71.950  -152.539 40.484  1.00 107.77 ? 28  ARG   Z NE  1 
ATOM   44375 C  CZ  . ARG   Z  12 28  ? 72.256  -151.247 40.461  1.00 110.04 ? 28  ARG   Z CZ  1 
ATOM   44376 N  NH1 . ARG   Z  12 28  ? 73.103  -150.754 41.350  1.00 113.20 ? 28  ARG   Z NH1 1 
ATOM   44377 N  NH2 . ARG   Z  12 28  ? 71.721  -150.446 39.554  1.00 116.18 ? 28  ARG   Z NH2 1 
ATOM   44378 N  N   . ASN   Z  12 29  ? 69.881  -157.874 40.000  1.00 90.73  ? 29  ASN   Z N   1 
ATOM   44379 C  CA  . ASN   Z  12 29  ? 68.483  -158.377 39.930  1.00 89.33  ? 29  ASN   Z CA  1 
ATOM   44380 C  C   . ASN   Z  12 29  ? 67.607  -157.445 40.775  1.00 89.54  ? 29  ASN   Z C   1 
ATOM   44381 O  O   . ASN   Z  12 29  ? 67.964  -157.227 41.948  1.00 92.35  ? 29  ASN   Z O   1 
ATOM   44382 C  CB  . ASN   Z  12 29  ? 68.402  -159.832 40.399  1.00 88.56  ? 29  ASN   Z CB  1 
ATOM   44383 C  CG  . ASN   Z  12 29  ? 67.025  -160.445 40.251  1.00 86.01  ? 29  ASN   Z CG  1 
ATOM   44384 O  OD1 . ASN   Z  12 29  ? 66.075  -160.021 40.904  1.00 86.27  ? 29  ASN   Z OD1 1 
ATOM   44385 N  ND2 . ASN   Z  12 29  ? 66.908  -161.461 39.412  1.00 86.19  ? 29  ASN   Z ND2 1 
ATOM   44386 N  N   . ILE   Z  12 30  ? 66.514  -156.923 40.205  1.00 91.41  ? 30  ILE   Z N   1 
ATOM   44387 C  CA  . ILE   Z  12 30  ? 65.675  -155.844 40.817  1.00 93.55  ? 30  ILE   Z CA  1 
ATOM   44388 C  C   . ILE   Z  12 30  ? 64.188  -156.213 40.737  1.00 93.20  ? 30  ILE   Z C   1 
ATOM   44389 O  O   . ILE   Z  12 30  ? 63.827  -157.058 39.903  1.00 92.43  ? 30  ILE   Z O   1 
ATOM   44390 C  CB  . ILE   Z  12 30  ? 65.953  -154.484 40.138  1.00 95.13  ? 30  ILE   Z CB  1 
ATOM   44391 C  CG1 . ILE   Z  12 30  ? 65.473  -154.433 38.682  1.00 96.16  ? 30  ILE   Z CG1 1 
ATOM   44392 C  CG2 . ILE   Z  12 30  ? 67.425  -154.121 40.252  1.00 96.36  ? 30  ILE   Z CG2 1 
ATOM   44393 C  CD1 . ILE   Z  12 30  ? 64.084  -153.849 38.498  1.00 96.86  ? 30  ILE   Z CD1 1 
ATOM   44394 N  N   . THR   Z  12 31  ? 63.370  -155.593 41.593  1.00 94.90  ? 31  THR   Z N   1 
ATOM   44395 C  CA  . THR   Z  12 31  ? 61.896  -155.447 41.430  1.00 98.96  ? 31  THR   Z CA  1 
ATOM   44396 C  C   . THR   Z  12 31  ? 61.516  -154.019 41.837  1.00 100.71 ? 31  THR   Z C   1 
ATOM   44397 O  O   . THR   Z  12 31  ? 61.894  -153.606 42.954  1.00 101.47 ? 31  THR   Z O   1 
ATOM   44398 C  CB  . THR   Z  12 31  ? 61.107  -156.490 42.234  1.00 100.14 ? 31  THR   Z CB  1 
ATOM   44399 O  OG1 . THR   Z  12 31  ? 61.616  -156.510 43.566  1.00 107.16 ? 31  THR   Z OG1 1 
ATOM   44400 C  CG2 . THR   Z  12 31  ? 61.183  -157.884 41.649  1.00 101.79 ? 31  THR   Z CG2 1 
ATOM   44401 N  N   . ASP   Z  12 32  ? 60.815  -153.297 40.957  1.00 99.74  ? 32  ASP   Z N   1 
ATOM   44402 C  CA  . ASP   Z  12 32  ? 60.450  -151.868 41.145  1.00 100.04 ? 32  ASP   Z CA  1 
ATOM   44403 C  C   . ASP   Z  12 32  ? 61.743  -151.084 41.413  1.00 99.96  ? 32  ASP   Z C   1 
ATOM   44404 O  O   . ASP   Z  12 32  ? 62.647  -151.154 40.554  1.00 93.66  ? 32  ASP   Z O   1 
ATOM   44405 C  CB  . ASP   Z  12 32  ? 59.377  -151.726 42.229  1.00 102.09 ? 32  ASP   Z CB  1 
ATOM   44406 C  CG  . ASP   Z  12 32  ? 58.089  -152.464 41.907  1.00 102.26 ? 32  ASP   Z CG  1 
ATOM   44407 O  OD1 . ASP   Z  12 32  ? 57.722  -152.517 40.713  1.00 105.92 ? 32  ASP   Z OD1 1 
ATOM   44408 O  OD2 . ASP   Z  12 32  ? 57.464  -152.985 42.852  1.00 103.70 ? 32  ASP   Z OD2 1 
ATOM   44409 N  N   . TYR   Z  12 33  ? 61.849  -150.407 42.564  1.00 102.21 ? 33  TYR   Z N   1 
ATOM   44410 C  CA  . TYR   Z  12 33  ? 62.963  -149.480 42.909  1.00 103.44 ? 33  TYR   Z CA  1 
ATOM   44411 C  C   . TYR   Z  12 33  ? 63.896  -150.109 43.954  1.00 101.18 ? 33  TYR   Z C   1 
ATOM   44412 O  O   . TYR   Z  12 33  ? 64.674  -149.356 44.577  1.00 102.19 ? 33  TYR   Z O   1 
ATOM   44413 C  CB  . TYR   Z  12 33  ? 62.400  -148.140 43.392  1.00 105.68 ? 33  TYR   Z CB  1 
ATOM   44414 C  CG  . TYR   Z  12 33  ? 61.941  -147.232 42.280  1.00 107.71 ? 33  TYR   Z CG  1 
ATOM   44415 C  CD1 . TYR   Z  12 33  ? 62.850  -146.468 41.567  1.00 109.19 ? 33  TYR   Z CD1 1 
ATOM   44416 C  CD2 . TYR   Z  12 33  ? 60.603  -147.148 41.928  1.00 110.78 ? 33  TYR   Z CD2 1 
ATOM   44417 C  CE1 . TYR   Z  12 33  ? 62.443  -145.635 40.537  1.00 112.07 ? 33  TYR   Z CE1 1 
ATOM   44418 C  CE2 . TYR   Z  12 33  ? 60.179  -146.321 40.900  1.00 112.73 ? 33  TYR   Z CE2 1 
ATOM   44419 C  CZ  . TYR   Z  12 33  ? 61.102  -145.560 40.202  1.00 115.00 ? 33  TYR   Z CZ  1 
ATOM   44420 O  OH  . TYR   Z  12 33  ? 60.691  -144.741 39.190  1.00 117.30 ? 33  TYR   Z OH  1 
ATOM   44421 N  N   . SER   Z  12 34  ? 63.846  -151.436 44.122  1.00 98.13  ? 34  SER   Z N   1 
ATOM   44422 C  CA  . SER   Z  12 34  ? 64.659  -152.199 45.107  1.00 96.22  ? 34  SER   Z CA  1 
ATOM   44423 C  C   . SER   Z  12 34  ? 65.637  -153.132 44.387  1.00 93.76  ? 34  SER   Z C   1 
ATOM   44424 O  O   . SER   Z  12 34  ? 65.306  -153.599 43.280  1.00 91.74  ? 34  SER   Z O   1 
ATOM   44425 C  CB  . SER   Z  12 34  ? 63.785  -152.981 46.051  1.00 97.69  ? 34  SER   Z CB  1 
ATOM   44426 O  OG  . SER   Z  12 34  ? 63.272  -152.152 47.080  1.00 101.19 ? 34  SER   Z OG  1 
ATOM   44427 N  N   . ILE   Z  12 35  ? 66.786  -153.400 45.016  1.00 92.74  ? 35  ILE   Z N   1 
ATOM   44428 C  CA  . ILE   Z  12 35  ? 67.780  -154.417 44.561  1.00 91.55  ? 35  ILE   Z CA  1 
ATOM   44429 C  C   . ILE   Z  12 35  ? 67.540  -155.707 45.350  1.00 91.81  ? 35  ILE   Z C   1 
ATOM   44430 O  O   . ILE   Z  12 35  ? 67.551  -155.653 46.594  1.00 87.09  ? 35  ILE   Z O   1 
ATOM   44431 C  CB  . ILE   Z  12 35  ? 69.229  -153.916 44.721  1.00 94.46  ? 35  ILE   Z CB  1 
ATOM   44432 C  CG1 . ILE   Z  12 35  ? 69.472  -152.642 43.908  1.00 96.27  ? 35  ILE   Z CG1 1 
ATOM   44433 C  CG2 . ILE   Z  12 35  ? 70.220  -155.012 44.353  1.00 91.49  ? 35  ILE   Z CG2 1 
ATOM   44434 C  CD1 . ILE   Z  12 35  ? 70.716  -151.885 44.305  1.00 99.87  ? 35  ILE   Z CD1 1 
ATOM   44435 N  N   . ASN   Z  12 36  ? 67.335  -156.814 44.633  1.00 91.54  ? 36  ASN   Z N   1 
ATOM   44436 C  CA  . ASN   Z  12 36  ? 67.147  -158.174 45.199  1.00 92.21  ? 36  ASN   Z CA  1 
ATOM   44437 C  C   . ASN   Z  12 36  ? 68.526  -158.774 45.493  1.00 88.88  ? 36  ASN   Z C   1 
ATOM   44438 O  O   . ASN   Z  12 36  ? 68.746  -159.242 46.632  1.00 90.33  ? 36  ASN   Z O   1 
ATOM   44439 C  CB  . ASN   Z  12 36  ? 66.342  -159.057 44.244  1.00 92.86  ? 36  ASN   Z CB  1 
ATOM   44440 C  CG  . ASN   Z  12 36  ? 64.972  -158.493 43.931  1.00 93.32  ? 36  ASN   Z CG  1 
ATOM   44441 O  OD1 . ASN   Z  12 36  ? 64.352  -157.845 44.773  1.00 91.67  ? 36  ASN   Z OD1 1 
ATOM   44442 N  ND2 . ASN   Z  12 36  ? 64.490  -158.738 42.724  1.00 96.11  ? 36  ASN   Z ND2 1 
ATOM   44443 N  N   . SER   Z  12 37  ? 69.419  -158.735 44.499  1.00 88.53  ? 37  SER   Z N   1 
ATOM   44444 C  CA  . SER   Z  12 37  ? 70.782  -159.320 44.549  1.00 89.52  ? 37  SER   Z CA  1 
ATOM   44445 C  C   . SER   Z  12 37  ? 71.741  -158.470 43.712  1.00 88.48  ? 37  SER   Z C   1 
ATOM   44446 O  O   . SER   Z  12 37  ? 71.334  -158.032 42.615  1.00 87.24  ? 37  SER   Z O   1 
ATOM   44447 C  CB  . SER   Z  12 37  ? 70.762  -160.747 44.075  1.00 88.77  ? 37  SER   Z CB  1 
ATOM   44448 O  OG  . SER   Z  12 37  ? 72.051  -161.333 44.180  1.00 90.98  ? 37  SER   Z OG  1 
ATOM   44449 N  N   . ARG   Z  12 38  ? 72.957  -158.245 44.220  1.00 87.92  ? 38  ARG   Z N   1 
ATOM   44450 C  CA  . ARG   Z  12 38  ? 74.051  -157.548 43.493  1.00 90.03  ? 38  ARG   Z CA  1 
ATOM   44451 C  C   . ARG   Z  12 38  ? 74.813  -158.561 42.628  1.00 90.19  ? 38  ARG   Z C   1 
ATOM   44452 O  O   . ARG   Z  12 38  ? 75.432  -158.132 41.635  1.00 87.83  ? 38  ARG   Z O   1 
ATOM   44453 C  CB  . ARG   Z  12 38  ? 74.990  -156.836 44.470  1.00 90.89  ? 38  ARG   Z CB  1 
ATOM   44454 C  CG  . ARG   Z  12 38  ? 74.326  -155.708 45.246  1.00 91.62  ? 38  ARG   Z CG  1 
ATOM   44455 C  CD  . ARG   Z  12 38  ? 75.330  -154.727 45.816  1.00 93.86  ? 38  ARG   Z CD  1 
ATOM   44456 N  NE  . ARG   Z  12 38  ? 74.710  -153.732 46.687  1.00 96.77  ? 38  ARG   Z NE  1 
ATOM   44457 C  CZ  . ARG   Z  12 38  ? 74.215  -152.552 46.302  1.00 95.83  ? 38  ARG   Z CZ  1 
ATOM   44458 N  NH1 . ARG   Z  12 38  ? 74.244  -152.174 45.035  1.00 94.39  ? 38  ARG   Z NH1 1 
ATOM   44459 N  NH2 . ARG   Z  12 38  ? 73.681  -151.744 47.200  1.00 97.65  ? 38  ARG   Z NH2 1 
ATOM   44460 N  N   . TYR   Z  12 39  ? 74.774  -159.849 42.990  1.00 91.08  ? 39  TYR   Z N   1 
ATOM   44461 C  CA  . TYR   Z  12 39  ? 75.370  -160.957 42.197  1.00 92.35  ? 39  TYR   Z CA  1 
ATOM   44462 C  C   . TYR   Z  12 39  ? 74.390  -162.133 42.090  1.00 93.10  ? 39  TYR   Z C   1 
ATOM   44463 O  O   . TYR   Z  12 39  ? 74.426  -163.040 42.946  1.00 92.81  ? 39  TYR   Z O   1 
ATOM   44464 C  CB  . TYR   Z  12 39  ? 76.706  -161.412 42.787  1.00 94.57  ? 39  TYR   Z CB  1 
ATOM   44465 C  CG  . TYR   Z  12 39  ? 77.397  -162.461 41.953  1.00 96.26  ? 39  TYR   Z CG  1 
ATOM   44466 C  CD1 . TYR   Z  12 39  ? 78.029  -162.123 40.767  1.00 98.40  ? 39  TYR   Z CD1 1 
ATOM   44467 C  CD2 . TYR   Z  12 39  ? 77.394  -163.794 42.329  1.00 96.98  ? 39  TYR   Z CD2 1 
ATOM   44468 C  CE1 . TYR   Z  12 39  ? 78.657  -163.077 39.984  1.00 99.99  ? 39  TYR   Z CE1 1 
ATOM   44469 C  CE2 . TYR   Z  12 39  ? 78.017  -164.761 41.557  1.00 99.64  ? 39  TYR   Z CE2 1 
ATOM   44470 C  CZ  . TYR   Z  12 39  ? 78.652  -164.401 40.382  1.00 100.63 ? 39  TYR   Z CZ  1 
ATOM   44471 O  OH  . TYR   Z  12 39  ? 79.267  -165.344 39.610  1.00 106.41 ? 39  TYR   Z OH  1 
ATOM   44472 N  N   . GLU   Z  12 40  ? 73.551  -162.104 41.049  1.00 93.98  ? 40  GLU   Z N   1 
ATOM   44473 C  CA  . GLU   Z  12 40  ? 72.679  -163.225 40.607  1.00 94.45  ? 40  GLU   Z CA  1 
ATOM   44474 C  C   . GLU   Z  12 40  ? 72.962  -163.476 39.128  1.00 93.05  ? 40  GLU   Z C   1 
ATOM   44475 O  O   . GLU   Z  12 40  ? 72.446  -162.759 38.273  1.00 92.08  ? 40  GLU   Z O   1 
ATOM   44476 C  CB  . GLU   Z  12 40  ? 71.205  -162.891 40.848  1.00 91.84  ? 40  GLU   Z CB  1 
ATOM   44477 C  CG  . GLU   Z  12 40  ? 70.263  -164.053 40.578  1.00 91.82  ? 40  GLU   Z CG  1 
ATOM   44478 C  CD  . GLU   Z  12 40  ? 70.408  -165.245 41.513  1.00 92.93  ? 40  GLU   Z CD  1 
ATOM   44479 O  OE1 . GLU   Z  12 40  ? 70.781  -165.043 42.689  1.00 89.31  ? 40  GLU   Z OE1 1 
ATOM   44480 O  OE2 . GLU   Z  12 40  ? 70.150  -166.379 41.060  1.00 92.83  ? 40  GLU   Z OE2 1 
ATOM   44481 N  N   . PRO   Z  12 41  ? 73.806  -164.474 38.776  1.00 95.48  ? 41  PRO   Z N   1 
ATOM   44482 C  CA  . PRO   Z  12 41  ? 74.172  -164.711 37.380  1.00 94.62  ? 41  PRO   Z CA  1 
ATOM   44483 C  C   . PRO   Z  12 41  ? 72.958  -165.148 36.545  1.00 93.11  ? 41  PRO   Z C   1 
ATOM   44484 O  O   . PRO   Z  12 41  ? 72.128  -165.873 37.066  1.00 92.29  ? 41  PRO   Z O   1 
ATOM   44485 C  CB  . PRO   Z  12 41  ? 75.219  -165.835 37.440  1.00 95.02  ? 41  PRO   Z CB  1 
ATOM   44486 C  CG  . PRO   Z  12 41  ? 75.655  -165.883 38.892  1.00 97.14  ? 41  PRO   Z CG  1 
ATOM   44487 C  CD  . PRO   Z  12 41  ? 74.449  -165.432 39.688  1.00 96.37  ? 41  PRO   Z CD  1 
ATOM   44488 N  N   . LYS   Z  12 42  ? 72.873  -164.674 35.298  1.00 94.97  ? 42  LYS   Z N   1 
ATOM   44489 C  CA  . LYS   Z  12 42  ? 71.796  -165.033 34.334  1.00 95.01  ? 42  LYS   Z CA  1 
ATOM   44490 C  C   . LYS   Z  12 42  ? 72.390  -165.430 32.975  1.00 93.06  ? 42  LYS   Z C   1 
ATOM   44491 O  O   . LYS   Z  12 42  ? 71.606  -165.564 32.013  1.00 89.11  ? 42  LYS   Z O   1 
ATOM   44492 C  CB  . LYS   Z  12 42  ? 70.811  -163.869 34.191  1.00 98.92  ? 42  LYS   Z CB  1 
ATOM   44493 C  CG  . LYS   Z  12 42  ? 71.376  -162.596 33.574  1.00 102.46 ? 42  LYS   Z CG  1 
ATOM   44494 C  CD  . LYS   Z  12 42  ? 70.556  -161.382 33.932  1.00 103.88 ? 42  LYS   Z CD  1 
ATOM   44495 C  CE  . LYS   Z  12 42  ? 71.187  -160.072 33.513  1.00 108.47 ? 42  LYS   Z CE  1 
ATOM   44496 N  NZ  . LYS   Z  12 42  ? 71.006  -159.041 34.562  1.00 109.86 ? 42  LYS   Z NZ  1 
ATOM   44497 N  N   . VAL   Z  12 43  ? 73.713  -165.616 32.899  1.00 93.67  ? 43  VAL   Z N   1 
ATOM   44498 C  CA  . VAL   Z  12 43  ? 74.417  -166.203 31.721  1.00 96.95  ? 43  VAL   Z CA  1 
ATOM   44499 C  C   . VAL   Z  12 43  ? 74.953  -167.572 32.145  1.00 97.52  ? 43  VAL   Z C   1 
ATOM   44500 O  O   . VAL   Z  12 43  ? 75.695  -167.626 33.145  1.00 103.82 ? 43  VAL   Z O   1 
ATOM   44501 C  CB  . VAL   Z  12 43  ? 75.553  -165.297 31.210  1.00 99.90  ? 43  VAL   Z CB  1 
ATOM   44502 C  CG1 . VAL   Z  12 43  ? 76.129  -165.822 29.905  1.00 102.50 ? 43  VAL   Z CG1 1 
ATOM   44503 C  CG2 . VAL   Z  12 43  ? 75.111  -163.850 31.055  1.00 100.72 ? 43  VAL   Z CG2 1 
ATOM   44504 N  N   . PHE   Z  12 44  ? 74.594  -168.631 31.415  1.00 96.82  ? 44  PHE   Z N   1 
ATOM   44505 C  CA  . PHE   Z  12 44  ? 74.833  -170.041 31.822  1.00 97.63  ? 44  PHE   Z CA  1 
ATOM   44506 C  C   . PHE   Z  12 44  ? 75.512  -170.828 30.697  1.00 97.74  ? 44  PHE   Z C   1 
ATOM   44507 O  O   . PHE   Z  12 44  ? 75.174  -170.624 29.515  1.00 94.21  ? 44  PHE   Z O   1 
ATOM   44508 C  CB  . PHE   Z  12 44  ? 73.514  -170.704 32.224  1.00 93.54  ? 44  PHE   Z CB  1 
ATOM   44509 C  CG  . PHE   Z  12 44  ? 72.805  -170.019 33.362  1.00 91.83  ? 44  PHE   Z CG  1 
ATOM   44510 C  CD1 . PHE   Z  12 44  ? 73.225  -170.206 34.670  1.00 91.92  ? 44  PHE   Z CD1 1 
ATOM   44511 C  CD2 . PHE   Z  12 44  ? 71.731  -169.175 33.127  1.00 91.95  ? 44  PHE   Z CD2 1 
ATOM   44512 C  CE1 . PHE   Z  12 44  ? 72.578  -169.572 35.719  1.00 90.72  ? 44  PHE   Z CE1 1 
ATOM   44513 C  CE2 . PHE   Z  12 44  ? 71.084  -168.542 34.178  1.00 91.23  ? 44  PHE   Z CE2 1 
ATOM   44514 C  CZ  . PHE   Z  12 44  ? 71.508  -168.742 35.472  1.00 90.89  ? 44  PHE   Z CZ  1 
ATOM   44515 N  N   . ASP   Z  12 45  ? 76.450  -171.699 31.084  1.00 100.01 ? 45  ASP   Z N   1 
ATOM   44516 C  CA  . ASP   Z  12 45  ? 77.029  -172.774 30.237  1.00 100.44 ? 45  ASP   Z CA  1 
ATOM   44517 C  C   . ASP   Z  12 45  ? 76.026  -173.933 30.218  1.00 100.92 ? 45  ASP   Z C   1 
ATOM   44518 O  O   . ASP   Z  12 45  ? 75.736  -174.468 31.304  1.00 101.70 ? 45  ASP   Z O   1 
ATOM   44519 C  CB  . ASP   Z  12 45  ? 78.400  -173.197 30.774  1.00 104.28 ? 45  ASP   Z CB  1 
ATOM   44520 C  CG  . ASP   Z  12 45  ? 79.190  -174.123 29.864  1.00 106.02 ? 45  ASP   Z CG  1 
ATOM   44521 O  OD1 . ASP   Z  12 45  ? 78.613  -174.627 28.878  1.00 107.83 ? 45  ASP   Z OD1 1 
ATOM   44522 O  OD2 . ASP   Z  12 45  ? 80.385  -174.331 30.151  1.00 108.81 ? 45  ASP   Z OD2 1 
ATOM   44523 N  N   . CYS   Z  12 46  ? 75.502  -174.286 29.039  1.00 99.84  ? 46  CYS   Z N   1 
ATOM   44524 C  CA  . CYS   Z  12 46  ? 74.432  -175.306 28.851  1.00 101.97 ? 46  CYS   Z CA  1 
ATOM   44525 C  C   . CYS   Z  12 46  ? 75.006  -176.612 28.276  1.00 103.00 ? 46  CYS   Z C   1 
ATOM   44526 O  O   . CYS   Z  12 46  ? 74.202  -177.495 27.902  1.00 98.07  ? 46  CYS   Z O   1 
ATOM   44527 C  CB  . CYS   Z  12 46  ? 73.338  -174.761 27.941  1.00 105.24 ? 46  CYS   Z CB  1 
ATOM   44528 S  SG  . CYS   Z  12 46  ? 72.595  -173.232 28.566  1.00 105.85 ? 46  CYS   Z SG  1 
ATOM   44529 N  N   . GLY   Z  12 47  ? 76.336  -176.740 28.226  1.00 101.72 ? 47  GLY   Z N   1 
ATOM   44530 C  CA  . GLY   Z  12 47  ? 77.034  -177.886 27.612  1.00 103.42 ? 47  GLY   Z CA  1 
ATOM   44531 C  C   . GLY   Z  12 47  ? 77.139  -177.738 26.103  1.00 104.99 ? 47  GLY   Z C   1 
ATOM   44532 O  O   . GLY   Z  12 47  ? 76.465  -176.850 25.544  1.00 102.83 ? 47  GLY   Z O   1 
ATOM   44533 N  N   . ASP   Z  12 48  ? 77.957  -178.583 25.467  1.00 107.29 ? 48  ASP   Z N   1 
ATOM   44534 C  CA  . ASP   Z  12 48  ? 78.199  -178.610 23.998  1.00 108.04 ? 48  ASP   Z CA  1 
ATOM   44535 C  C   . ASP   Z  12 48  ? 78.645  -177.227 23.504  1.00 106.00 ? 48  ASP   Z C   1 
ATOM   44536 O  O   . ASP   Z  12 48  ? 78.310  -176.881 22.354  1.00 103.77 ? 48  ASP   Z O   1 
ATOM   44537 C  CB  . ASP   Z  12 48  ? 76.954  -179.092 23.247  1.00 110.72 ? 48  ASP   Z CB  1 
ATOM   44538 C  CG  . ASP   Z  12 48  ? 76.644  -180.567 23.442  1.00 112.15 ? 48  ASP   Z CG  1 
ATOM   44539 O  OD1 . ASP   Z  12 48  ? 77.227  -181.179 24.363  1.00 109.96 ? 48  ASP   Z OD1 1 
ATOM   44540 O  OD2 . ASP   Z  12 48  ? 75.825  -181.094 22.664  1.00 114.91 ? 48  ASP   Z OD2 1 
ATOM   44541 N  N   . ASN   Z  12 49  ? 79.386  -176.477 24.327  1.00 103.58 ? 49  ASN   Z N   1 
ATOM   44542 C  CA  . ASN   Z  12 49  ? 79.918  -175.127 23.993  1.00 105.67 ? 49  ASN   Z CA  1 
ATOM   44543 C  C   . ASN   Z  12 49  ? 78.780  -174.201 23.556  1.00 102.06 ? 49  ASN   Z C   1 
ATOM   44544 O  O   . ASN   Z  12 49  ? 78.969  -173.448 22.581  1.00 105.52 ? 49  ASN   Z O   1 
ATOM   44545 C  CB  . ASN   Z  12 49  ? 81.003  -175.199 22.916  1.00 107.07 ? 49  ASN   Z CB  1 
ATOM   44546 C  CG  . ASN   Z  12 49  ? 82.400  -175.147 23.491  1.00 109.49 ? 49  ASN   Z CG  1 
ATOM   44547 O  OD1 . ASN   Z  12 49  ? 83.272  -174.490 22.930  1.00 109.33 ? 49  ASN   Z OD1 1 
ATOM   44548 N  ND2 . ASN   Z  12 49  ? 82.617  -175.827 24.607  1.00 111.50 ? 49  ASN   Z ND2 1 
ATOM   44549 N  N   . ILE   Z  12 50  ? 77.643  -174.263 24.250  1.00 101.58 ? 50  ILE   Z N   1 
ATOM   44550 C  CA  . ILE   Z  12 50  ? 76.521  -173.293 24.095  1.00 101.02 ? 50  ILE   Z CA  1 
ATOM   44551 C  C   . ILE   Z  12 50  ? 76.375  -172.546 25.420  1.00 99.97  ? 50  ILE   Z C   1 
ATOM   44552 O  O   . ILE   Z  12 50  ? 76.194  -173.219 26.456  1.00 98.91  ? 50  ILE   Z O   1 
ATOM   44553 C  CB  . ILE   Z  12 50  ? 75.210  -173.993 23.686  1.00 102.24 ? 50  ILE   Z CB  1 
ATOM   44554 C  CG1 . ILE   Z  12 50  ? 75.375  -174.809 22.401  1.00 102.93 ? 50  ILE   Z CG1 1 
ATOM   44555 C  CG2 . ILE   Z  12 50  ? 74.080  -172.980 23.562  1.00 103.90 ? 50  ILE   Z CG2 1 
ATOM   44556 C  CD1 . ILE   Z  12 50  ? 74.342  -175.896 22.231  1.00 101.95 ? 50  ILE   Z CD1 1 
ATOM   44557 N  N   . VAL   Z  12 51  ? 76.476  -171.216 25.374  1.00 98.01  ? 51  VAL   Z N   1 
ATOM   44558 C  CA  . VAL   Z  12 51  ? 76.130  -170.309 26.507  1.00 93.27  ? 51  VAL   Z CA  1 
ATOM   44559 C  C   . VAL   Z  12 51  ? 74.805  -169.631 26.158  1.00 91.03  ? 51  VAL   Z C   1 
ATOM   44560 O  O   . VAL   Z  12 51  ? 74.573  -169.372 24.961  1.00 89.05  ? 51  VAL   Z O   1 
ATOM   44561 C  CB  . VAL   Z  12 51  ? 77.248  -169.295 26.816  1.00 95.31  ? 51  VAL   Z CB  1 
ATOM   44562 C  CG1 . VAL   Z  12 51  ? 78.449  -169.978 27.450  1.00 96.00  ? 51  VAL   Z CG1 1 
ATOM   44563 C  CG2 . VAL   Z  12 51  ? 77.667  -168.493 25.594  1.00 97.17  ? 51  VAL   Z CG2 1 
ATOM   44564 N  N   . MET   Z  12 52  ? 73.968  -169.389 27.167  1.00 89.14  ? 52  MET   Z N   1 
ATOM   44565 C  CA  . MET   Z  12 52  ? 72.561  -168.942 26.999  1.00 89.55  ? 52  MET   Z CA  1 
ATOM   44566 C  C   . MET   Z  12 52  ? 72.212  -167.930 28.094  1.00 89.06  ? 52  MET   Z C   1 
ATOM   44567 O  O   . MET   Z  12 52  ? 72.671  -168.110 29.240  1.00 87.30  ? 52  MET   Z O   1 
ATOM   44568 C  CB  . MET   Z  12 52  ? 71.617  -170.146 27.080  1.00 89.98  ? 52  MET   Z CB  1 
ATOM   44569 C  CG  . MET   Z  12 52  ? 70.143  -169.797 27.007  1.00 93.03  ? 52  MET   Z CG  1 
ATOM   44570 S  SD  . MET   Z  12 52  ? 69.118  -171.288 26.921  1.00 96.74  ? 52  MET   Z SD  1 
ATOM   44571 C  CE  . MET   Z  12 52  ? 67.482  -170.590 27.145  1.00 96.53  ? 52  MET   Z CE  1 
ATOM   44572 N  N   . SER   Z  12 53  ? 71.437  -166.903 27.738  1.00 86.93  ? 53  SER   Z N   1 
ATOM   44573 C  CA  . SER   Z  12 53  ? 70.795  -165.958 28.688  1.00 87.19  ? 53  SER   Z CA  1 
ATOM   44574 C  C   . SER   Z  12 53  ? 69.370  -165.643 28.225  1.00 86.36  ? 53  SER   Z C   1 
ATOM   44575 O  O   . SER   Z  12 53  ? 69.186  -165.343 27.029  1.00 85.55  ? 53  SER   Z O   1 
ATOM   44576 C  CB  . SER   Z  12 53  ? 71.602  -164.705 28.844  1.00 87.95  ? 53  SER   Z CB  1 
ATOM   44577 O  OG  . SER   Z  12 53  ? 71.129  -163.954 29.951  1.00 89.93  ? 53  SER   Z OG  1 
ATOM   44578 N  N   . ALA   Z  12 54  ? 68.410  -165.719 29.150  1.00 87.05  ? 54  ALA   Z N   1 
ATOM   44579 C  CA  . ALA   Z  12 54  ? 66.991  -165.346 28.948  1.00 91.03  ? 54  ALA   Z CA  1 
ATOM   44580 C  C   . ALA   Z  12 54  ? 66.651  -164.198 29.905  1.00 90.90  ? 54  ALA   Z C   1 
ATOM   44581 O  O   . ALA   Z  12 54  ? 66.346  -164.469 31.082  1.00 93.96  ? 54  ALA   Z O   1 
ATOM   44582 C  CB  . ALA   Z  12 54  ? 66.106  -166.551 29.160  1.00 91.24  ? 54  ALA   Z CB  1 
ATOM   44583 N  N   . ASN   Z  12 55  ? 66.718  -162.959 29.413  1.00 91.33  ? 55  ASN   Z N   1 
ATOM   44584 C  CA  . ASN   Z  12 55  ? 66.651  -161.733 30.250  1.00 91.55  ? 55  ASN   Z CA  1 
ATOM   44585 C  C   . ASN   Z  12 55  ? 65.251  -161.124 30.173  1.00 90.64  ? 55  ASN   Z C   1 
ATOM   44586 O  O   . ASN   Z  12 55  ? 64.709  -161.026 29.058  1.00 94.12  ? 55  ASN   Z O   1 
ATOM   44587 C  CB  . ASN   Z  12 55  ? 67.703  -160.704 29.834  1.00 97.08  ? 55  ASN   Z CB  1 
ATOM   44588 C  CG  . ASN   Z  12 55  ? 67.820  -159.563 30.823  1.00 99.04  ? 55  ASN   Z CG  1 
ATOM   44589 O  OD1 . ASN   Z  12 55  ? 67.655  -158.401 30.463  1.00 101.78 ? 55  ASN   Z OD1 1 
ATOM   44590 N  ND2 . ASN   Z  12 55  ? 68.087  -159.884 32.078  1.00 104.41 ? 55  ASN   Z ND2 1 
ATOM   44591 N  N   . GLY   Z  12 56  ? 64.718  -160.707 31.324  1.00 87.44  ? 56  GLY   Z N   1 
ATOM   44592 C  CA  . GLY   Z  12 56  ? 63.402  -160.056 31.458  1.00 87.54  ? 56  GLY   Z CA  1 
ATOM   44593 C  C   . GLY   Z  12 56  ? 62.750  -160.430 32.774  1.00 85.58  ? 56  GLY   Z C   1 
ATOM   44594 O  O   . GLY   Z  12 56  ? 63.142  -159.857 33.810  1.00 92.01  ? 56  GLY   Z O   1 
ATOM   44595 N  N   . PHE   Z  12 57  ? 61.806  -161.373 32.734  1.00 83.75  ? 57  PHE   Z N   1 
ATOM   44596 C  CA  . PHE   Z  12 57  ? 61.129  -161.951 33.923  1.00 82.97  ? 57  PHE   Z CA  1 
ATOM   44597 C  C   . PHE   Z  12 57  ? 61.905  -163.202 34.345  1.00 83.86  ? 57  PHE   Z C   1 
ATOM   44598 O  O   . PHE   Z  12 57  ? 61.781  -164.230 33.657  1.00 83.78  ? 57  PHE   Z O   1 
ATOM   44599 C  CB  . PHE   Z  12 57  ? 59.661  -162.247 33.604  1.00 81.41  ? 57  PHE   Z CB  1 
ATOM   44600 C  CG  . PHE   Z  12 57  ? 58.885  -162.882 34.730  1.00 79.50  ? 57  PHE   Z CG  1 
ATOM   44601 C  CD1 . PHE   Z  12 57  ? 59.023  -162.429 36.033  1.00 80.93  ? 57  PHE   Z CD1 1 
ATOM   44602 C  CD2 . PHE   Z  12 57  ? 58.008  -163.926 34.486  1.00 77.43  ? 57  PHE   Z CD2 1 
ATOM   44603 C  CE1 . PHE   Z  12 57  ? 58.303  -163.009 37.065  1.00 81.24  ? 57  PHE   Z CE1 1 
ATOM   44604 C  CE2 . PHE   Z  12 57  ? 57.291  -164.507 35.519  1.00 77.19  ? 57  PHE   Z CE2 1 
ATOM   44605 C  CZ  . PHE   Z  12 57  ? 57.439  -164.048 36.806  1.00 79.10  ? 57  PHE   Z CZ  1 
ATOM   44606 N  N   . ALA   Z  12 58  ? 62.683  -163.104 35.428  1.00 84.82  ? 58  ALA   Z N   1 
ATOM   44607 C  CA  . ALA   Z  12 58  ? 63.702  -164.098 35.848  1.00 86.77  ? 58  ALA   Z CA  1 
ATOM   44608 C  C   . ALA   Z  12 58  ? 63.084  -165.492 36.024  1.00 87.71  ? 58  ALA   Z C   1 
ATOM   44609 O  O   . ALA   Z  12 58  ? 63.784  -166.472 35.708  1.00 90.04  ? 58  ALA   Z O   1 
ATOM   44610 C  CB  . ALA   Z  12 58  ? 64.384  -163.648 37.116  1.00 88.77  ? 58  ALA   Z CB  1 
ATOM   44611 N  N   . ALA   Z  12 59  ? 61.840  -165.580 36.513  1.00 88.36  ? 59  ALA   Z N   1 
ATOM   44612 C  CA  . ALA   Z  12 59  ? 61.106  -166.853 36.724  1.00 87.72  ? 59  ALA   Z CA  1 
ATOM   44613 C  C   . ALA   Z  12 59  ? 60.946  -167.584 35.384  1.00 85.88  ? 59  ALA   Z C   1 
ATOM   44614 O  O   . ALA   Z  12 59  ? 61.187  -168.806 35.352  1.00 87.76  ? 59  ALA   Z O   1 
ATOM   44615 C  CB  . ALA   Z  12 59  ? 59.770  -166.598 37.381  1.00 87.48  ? 59  ALA   Z CB  1 
ATOM   44616 N  N   . ASP   Z  12 60  ? 60.568  -166.860 34.325  1.00 82.21  ? 60  ASP   Z N   1 
ATOM   44617 C  CA  . ASP   Z  12 60  ? 60.429  -167.403 32.946  1.00 81.97  ? 60  ASP   Z CA  1 
ATOM   44618 C  C   . ASP   Z  12 60  ? 61.825  -167.645 32.361  1.00 82.74  ? 60  ASP   Z C   1 
ATOM   44619 O  O   . ASP   Z  12 60  ? 61.986  -168.630 31.624  1.00 86.32  ? 60  ASP   Z O   1 
ATOM   44620 C  CB  . ASP   Z  12 60  ? 59.586  -166.483 32.056  1.00 82.93  ? 60  ASP   Z CB  1 
ATOM   44621 C  CG  . ASP   Z  12 60  ? 58.084  -166.617 32.265  1.00 82.94  ? 60  ASP   Z CG  1 
ATOM   44622 O  OD1 . ASP   Z  12 60  ? 57.673  -167.430 33.114  1.00 83.06  ? 60  ASP   Z OD1 1 
ATOM   44623 O  OD2 . ASP   Z  12 60  ? 57.331  -165.903 31.575  1.00 87.02  ? 60  ASP   Z OD2 1 
ATOM   44624 N  N   . GLY   Z  12 61  ? 62.790  -166.776 32.675  1.00 83.51  ? 61  GLY   Z N   1 
ATOM   44625 C  CA  . GLY   Z  12 61  ? 64.194  -166.908 32.240  1.00 87.14  ? 61  GLY   Z CA  1 
ATOM   44626 C  C   . GLY   Z  12 61  ? 64.816  -168.192 32.753  1.00 89.95  ? 61  GLY   Z C   1 
ATOM   44627 O  O   . GLY   Z  12 61  ? 65.437  -168.912 31.944  1.00 92.14  ? 61  GLY   Z O   1 
ATOM   44628 N  N   . ASP   Z  12 62  ? 64.644  -168.473 34.048  1.00 92.26  ? 62  ASP   Z N   1 
ATOM   44629 C  CA  . ASP   Z  12 62  ? 65.189  -169.679 34.728  1.00 93.01  ? 62  ASP   Z CA  1 
ATOM   44630 C  C   . ASP   Z  12 62  ? 64.481  -170.928 34.190  1.00 89.65  ? 62  ASP   Z C   1 
ATOM   44631 O  O   . ASP   Z  12 62  ? 65.179  -171.921 33.914  1.00 91.69  ? 62  ASP   Z O   1 
ATOM   44632 C  CB  . ASP   Z  12 62  ? 65.073  -169.556 36.250  1.00 96.15  ? 62  ASP   Z CB  1 
ATOM   44633 C  CG  . ASP   Z  12 62  ? 66.079  -168.593 36.861  1.00 100.65 ? 62  ASP   Z CG  1 
ATOM   44634 O  OD1 . ASP   Z  12 62  ? 67.017  -168.181 36.141  1.00 100.80 ? 62  ASP   Z OD1 1 
ATOM   44635 O  OD2 . ASP   Z  12 62  ? 65.917  -168.259 38.052  1.00 104.61 ? 62  ASP   Z OD2 1 
ATOM   44636 N  N   . ALA   Z  12 63  ? 63.156  -170.871 34.034  1.00 87.46  ? 63  ALA   Z N   1 
ATOM   44637 C  CA  . ALA   Z  12 63  ? 62.320  -171.980 33.520  1.00 86.91  ? 63  ALA   Z CA  1 
ATOM   44638 C  C   . ALA   Z  12 63  ? 62.817  -172.402 32.133  1.00 88.94  ? 63  ALA   Z C   1 
ATOM   44639 O  O   . ALA   Z  12 63  ? 62.953  -173.619 31.908  1.00 91.06  ? 63  ALA   Z O   1 
ATOM   44640 C  CB  . ALA   Z  12 63  ? 60.867  -171.572 33.486  1.00 85.49  ? 63  ALA   Z CB  1 
ATOM   44641 N  N   . LEU   Z  12 64  ? 63.086  -171.434 31.249  1.00 87.76  ? 64  LEU   Z N   1 
ATOM   44642 C  CA  . LEU   Z  12 64  ? 63.508  -171.688 29.844  1.00 89.90  ? 64  LEU   Z CA  1 
ATOM   44643 C  C   . LEU   Z  12 64  ? 64.914  -172.302 29.831  1.00 90.25  ? 64  LEU   Z C   1 
ATOM   44644 O  O   . LEU   Z  12 64  ? 65.092  -173.335 29.159  1.00 90.90  ? 64  LEU   Z O   1 
ATOM   44645 C  CB  . LEU   Z  12 64  ? 63.472  -170.386 29.038  1.00 89.87  ? 64  LEU   Z CB  1 
ATOM   44646 C  CG  . LEU   Z  12 64  ? 63.741  -170.543 27.541  1.00 90.91  ? 64  LEU   Z CG  1 
ATOM   44647 C  CD1 . LEU   Z  12 64  ? 62.600  -171.282 26.856  1.00 93.28  ? 64  LEU   Z CD1 1 
ATOM   44648 C  CD2 . LEU   Z  12 64  ? 63.977  -169.195 26.881  1.00 90.40  ? 64  LEU   Z CD2 1 
ATOM   44649 N  N   . VAL   Z  12 65  ? 65.871  -171.685 30.531  1.00 91.67  ? 65  VAL   Z N   1 
ATOM   44650 C  CA  . VAL   Z  12 65  ? 67.278  -172.181 30.641  1.00 93.19  ? 65  VAL   Z CA  1 
ATOM   44651 C  C   . VAL   Z  12 65  ? 67.249  -173.621 31.168  1.00 89.58  ? 65  VAL   Z C   1 
ATOM   44652 O  O   . VAL   Z  12 65  ? 68.020  -174.454 30.657  1.00 89.87  ? 65  VAL   Z O   1 
ATOM   44653 C  CB  . VAL   Z  12 65  ? 68.140  -171.273 31.541  1.00 94.51  ? 65  VAL   Z CB  1 
ATOM   44654 C  CG1 . VAL   Z  12 65  ? 69.451  -171.938 31.941  1.00 98.29  ? 65  VAL   Z CG1 1 
ATOM   44655 C  CG2 . VAL   Z  12 65  ? 68.411  -169.928 30.886  1.00 95.86  ? 65  VAL   Z CG2 1 
ATOM   44656 N  N   . LYS   Z  12 66  ? 66.392  -173.885 32.158  1.00 87.44  ? 66  LYS   Z N   1 
ATOM   44657 C  CA  . LYS   Z  12 66  ? 66.220  -175.211 32.807  1.00 88.35  ? 66  LYS   Z CA  1 
ATOM   44658 C  C   . LYS   Z  12 66  ? 65.748  -176.235 31.765  1.00 87.26  ? 66  LYS   Z C   1 
ATOM   44659 O  O   . LYS   Z  12 66  ? 66.323  -177.342 31.731  1.00 86.55  ? 66  LYS   Z O   1 
ATOM   44660 C  CB  . LYS   Z  12 66  ? 65.232  -175.095 33.970  1.00 89.07  ? 66  LYS   Z CB  1 
ATOM   44661 C  CG  . LYS   Z  12 66  ? 65.252  -176.251 34.954  1.00 90.59  ? 66  LYS   Z CG  1 
ATOM   44662 C  CD  . LYS   Z  12 66  ? 64.810  -175.851 36.342  1.00 92.93  ? 66  LYS   Z CD  1 
ATOM   44663 C  CE  . LYS   Z  12 66  ? 64.918  -176.984 37.339  1.00 94.02  ? 66  LYS   Z CE  1 
ATOM   44664 N  NZ  . LYS   Z  12 66  ? 64.553  -176.543 38.705  1.00 95.81  ? 66  LYS   Z NZ  1 
ATOM   44665 N  N   . ARG   Z  12 67  ? 64.757  -175.869 30.942  1.00 87.82  ? 67  ARG   Z N   1 
ATOM   44666 C  CA  . ARG   Z  12 67  ? 64.145  -176.763 29.919  1.00 85.24  ? 67  ARG   Z CA  1 
ATOM   44667 C  C   . ARG   Z  12 67  ? 65.139  -177.024 28.781  1.00 86.89  ? 67  ARG   Z C   1 
ATOM   44668 O  O   . ARG   Z  12 67  ? 65.209  -178.180 28.330  1.00 83.70  ? 67  ARG   Z O   1 
ATOM   44669 C  CB  . ARG   Z  12 67  ? 62.841  -176.179 29.366  1.00 85.41  ? 67  ARG   Z CB  1 
ATOM   44670 C  CG  . ARG   Z  12 67  ? 61.655  -176.302 30.311  1.00 87.04  ? 67  ARG   Z CG  1 
ATOM   44671 C  CD  . ARG   Z  12 67  ? 60.416  -176.802 29.592  1.00 92.30  ? 67  ARG   Z CD  1 
ATOM   44672 N  NE  . ARG   Z  12 67  ? 59.870  -175.812 28.669  1.00 95.45  ? 67  ARG   Z NE  1 
ATOM   44673 C  CZ  . ARG   Z  12 67  ? 59.065  -176.077 27.640  1.00 98.83  ? 67  ARG   Z CZ  1 
ATOM   44674 N  NH1 . ARG   Z  12 67  ? 58.702  -177.320 27.369  1.00 100.42 ? 67  ARG   Z NH1 1 
ATOM   44675 N  NH2 . ARG   Z  12 67  ? 58.627  -175.089 26.877  1.00 100.26 ? 67  ARG   Z NH2 1 
ATOM   44676 N  N   . PHE   Z  12 68  ? 65.867  -176.000 28.323  1.00 85.70  ? 68  PHE   Z N   1 
ATOM   44677 C  CA  . PHE   Z  12 68  ? 66.874  -176.132 27.236  1.00 87.12  ? 68  PHE   Z CA  1 
ATOM   44678 C  C   . PHE   Z  12 68  ? 68.044  -177.004 27.710  1.00 91.06  ? 68  PHE   Z C   1 
ATOM   44679 O  O   . PHE   Z  12 68  ? 68.487  -177.861 26.924  1.00 94.82  ? 68  PHE   Z O   1 
ATOM   44680 C  CB  . PHE   Z  12 68  ? 67.397  -174.781 26.744  1.00 85.14  ? 68  PHE   Z CB  1 
ATOM   44681 C  CG  . PHE   Z  12 68  ? 68.513  -174.920 25.739  1.00 85.04  ? 68  PHE   Z CG  1 
ATOM   44682 C  CD1 . PHE   Z  12 68  ? 68.256  -175.383 24.457  1.00 84.78  ? 68  PHE   Z CD1 1 
ATOM   44683 C  CD2 . PHE   Z  12 68  ? 69.827  -174.645 26.086  1.00 85.19  ? 68  PHE   Z CD2 1 
ATOM   44684 C  CE1 . PHE   Z  12 68  ? 69.283  -175.538 23.539  1.00 86.23  ? 68  PHE   Z CE1 1 
ATOM   44685 C  CE2 . PHE   Z  12 68  ? 70.853  -174.799 25.167  1.00 85.79  ? 68  PHE   Z CE2 1 
ATOM   44686 C  CZ  . PHE   Z  12 68  ? 70.579  -175.247 23.895  1.00 86.13  ? 68  PHE   Z CZ  1 
ATOM   44687 N  N   . LYS   Z  12 69  ? 68.536  -176.788 28.935  1.00 90.99  ? 69  LYS   Z N   1 
ATOM   44688 C  CA  . LYS   Z  12 69  ? 69.622  -177.606 29.545  1.00 95.13  ? 69  LYS   Z CA  1 
ATOM   44689 C  C   . LYS   Z  12 69  ? 69.193  -179.077 29.556  1.00 96.01  ? 69  LYS   Z C   1 
ATOM   44690 O  O   . LYS   Z  12 69  ? 70.036  -179.955 29.273  1.00 96.36  ? 69  LYS   Z O   1 
ATOM   44691 C  CB  . LYS   Z  12 69  ? 69.938  -177.147 30.971  1.00 96.29  ? 69  LYS   Z CB  1 
ATOM   44692 C  CG  . LYS   Z  12 69  ? 70.973  -176.037 31.071  1.00 99.02  ? 69  LYS   Z CG  1 
ATOM   44693 C  CD  . LYS   Z  12 69  ? 71.486  -175.821 32.476  1.00 101.73 ? 69  LYS   Z CD  1 
ATOM   44694 C  CE  . LYS   Z  12 69  ? 72.636  -174.838 32.527  1.00 101.40 ? 69  LYS   Z CE  1 
ATOM   44695 N  NZ  . LYS   Z  12 69  ? 73.057  -174.556 33.918  1.00 102.37 ? 69  LYS   Z NZ  1 
ATOM   44696 N  N   . ASN   Z  12 70  ? 67.920  -179.315 29.875  1.00 99.03  ? 70  ASN   Z N   1 
ATOM   44697 C  CA  . ASN   Z  12 70  ? 67.291  -180.659 29.923  1.00 98.63  ? 70  ASN   Z CA  1 
ATOM   44698 C  C   . ASN   Z  12 70  ? 67.164  -181.210 28.499  1.00 97.28  ? 70  ASN   Z C   1 
ATOM   44699 O  O   . ASN   Z  12 70  ? 67.323  -182.426 28.324  1.00 99.64  ? 70  ASN   Z O   1 
ATOM   44700 C  CB  . ASN   Z  12 70  ? 65.937  -180.595 30.633  1.00 98.82  ? 70  ASN   Z CB  1 
ATOM   44701 C  CG  . ASN   Z  12 70  ? 65.424  -181.952 31.050  1.00 99.52  ? 70  ASN   Z CG  1 
ATOM   44702 O  OD1 . ASN   Z  12 70  ? 64.237  -182.237 30.918  1.00 101.83 ? 70  ASN   Z OD1 1 
ATOM   44703 N  ND2 . ASN   Z  12 70  ? 66.314  -182.791 31.550  1.00 105.25 ? 70  ASN   Z ND2 1 
ATOM   44704 N  N   . SER   Z  12 71  ? 66.885  -180.344 27.522  1.00 96.50  ? 71  SER   Z N   1 
ATOM   44705 C  CA  . SER   Z  12 71  ? 66.772  -180.694 26.082  1.00 98.30  ? 71  SER   Z CA  1 
ATOM   44706 C  C   . SER   Z  12 71  ? 68.120  -181.206 25.560  1.00 95.64  ? 71  SER   Z C   1 
ATOM   44707 O  O   . SER   Z  12 71  ? 68.111  -182.192 24.797  1.00 93.05  ? 71  SER   Z O   1 
ATOM   44708 C  CB  . SER   Z  12 71  ? 66.274  -179.523 25.273  1.00 98.98  ? 71  SER   Z CB  1 
ATOM   44709 O  OG  . SER   Z  12 71  ? 65.954  -179.920 23.948  1.00 104.52 ? 71  SER   Z OG  1 
ATOM   44710 N  N   . VAL   Z  12 72  ? 69.225  -180.559 25.953  1.00 97.43  ? 72  VAL   Z N   1 
ATOM   44711 C  CA  . VAL   Z  12 72  ? 70.619  -180.942 25.566  1.00 100.98 ? 72  VAL   Z CA  1 
ATOM   44712 C  C   . VAL   Z  12 72  ? 70.911  -182.347 26.105  1.00 100.29 ? 72  VAL   Z C   1 
ATOM   44713 O  O   . VAL   Z  12 72  ? 71.545  -183.140 25.380  1.00 99.77  ? 72  VAL   Z O   1 
ATOM   44714 C  CB  . VAL   Z  12 72  ? 71.663  -179.926 26.073  1.00 102.99 ? 72  VAL   Z CB  1 
ATOM   44715 C  CG1 . VAL   Z  12 72  ? 73.090  -180.424 25.877  1.00 104.59 ? 72  VAL   Z CG1 1 
ATOM   44716 C  CG2 . VAL   Z  12 72  ? 71.493  -178.561 25.422  1.00 103.00 ? 72  VAL   Z CG2 1 
ATOM   44717 N  N   . LYS   Z  12 73  ? 70.476  -182.630 27.337  1.00 100.52 ? 73  LYS   Z N   1 
ATOM   44718 C  CA  . LYS   Z  12 73  ? 70.692  -183.929 28.029  1.00 102.12 ? 73  LYS   Z CA  1 
ATOM   44719 C  C   . LYS   Z  12 73  ? 70.027  -185.057 27.230  1.00 103.17 ? 73  LYS   Z C   1 
ATOM   44720 O  O   . LYS   Z  12 73  ? 70.697  -186.078 26.978  1.00 103.44 ? 73  LYS   Z O   1 
ATOM   44721 C  CB  . LYS   Z  12 73  ? 70.131  -183.879 29.454  1.00 102.91 ? 73  LYS   Z CB  1 
ATOM   44722 C  CG  . LYS   Z  12 73  ? 70.617  -184.992 30.370  1.00 104.44 ? 73  LYS   Z CG  1 
ATOM   44723 C  CD  . LYS   Z  12 73  ? 69.920  -185.026 31.707  1.00 105.58 ? 73  LYS   Z CD  1 
ATOM   44724 C  CE  . LYS   Z  12 73  ? 70.469  -186.108 32.612  1.00 109.45 ? 73  LYS   Z CE  1 
ATOM   44725 N  NZ  . LYS   Z  12 73  ? 69.586  -186.348 33.777  1.00 112.28 ? 73  LYS   Z NZ  1 
ATOM   44726 N  N   . TRP   Z  12 74  ? 68.758  -184.877 26.851  1.00 100.97 ? 74  TRP   Z N   1 
ATOM   44727 C  CA  . TRP   Z  12 74  ? 67.932  -185.907 26.163  1.00 100.75 ? 74  TRP   Z CA  1 
ATOM   44728 C  C   . TRP   Z  12 74  ? 68.366  -186.060 24.702  1.00 99.90  ? 74  TRP   Z C   1 
ATOM   44729 O  O   . TRP   Z  12 74  ? 68.248  -187.178 24.178  1.00 100.44 ? 74  TRP   Z O   1 
ATOM   44730 C  CB  . TRP   Z  12 74  ? 66.437  -185.590 26.286  1.00 100.32 ? 74  TRP   Z CB  1 
ATOM   44731 C  CG  . TRP   Z  12 74  ? 65.869  -186.022 27.602  1.00 101.84 ? 74  TRP   Z CG  1 
ATOM   44732 C  CD1 . TRP   Z  12 74  ? 65.618  -185.242 28.693  1.00 101.56 ? 74  TRP   Z CD1 1 
ATOM   44733 C  CD2 . TRP   Z  12 74  ? 65.526  -187.364 27.984  1.00 103.38 ? 74  TRP   Z CD2 1 
ATOM   44734 N  NE1 . TRP   Z  12 74  ? 65.123  -186.002 29.717  1.00 101.67 ? 74  TRP   Z NE1 1 
ATOM   44735 C  CE2 . TRP   Z  12 74  ? 65.055  -187.308 29.313  1.00 102.25 ? 74  TRP   Z CE2 1 
ATOM   44736 C  CE3 . TRP   Z  12 74  ? 65.562  -188.601 27.331  1.00 104.04 ? 74  TRP   Z CE3 1 
ATOM   44737 C  CZ2 . TRP   Z  12 74  ? 64.624  -188.441 29.998  1.00 103.41 ? 74  TRP   Z CZ2 1 
ATOM   44738 C  CZ3 . TRP   Z  12 74  ? 65.134  -189.721 28.007  1.00 106.27 ? 74  TRP   Z CZ3 1 
ATOM   44739 C  CH2 . TRP   Z  12 74  ? 64.672  -189.639 29.322  1.00 105.68 ? 74  TRP   Z CH2 1 
ATOM   44740 N  N   . TYR   Z  12 75  ? 68.844  -184.986 24.070  1.00 99.34  ? 75  TYR   Z N   1 
ATOM   44741 C  CA  . TYR   Z  12 75  ? 69.422  -185.023 22.702  1.00 102.14 ? 75  TYR   Z CA  1 
ATOM   44742 C  C   . TYR   Z  12 75  ? 70.563  -186.047 22.667  1.00 102.25 ? 75  TYR   Z C   1 
ATOM   44743 O  O   . TYR   Z  12 75  ? 70.637  -186.807 21.686  1.00 105.68 ? 75  TYR   Z O   1 
ATOM   44744 C  CB  . TYR   Z  12 75  ? 69.915  -183.644 22.259  1.00 101.88 ? 75  TYR   Z CB  1 
ATOM   44745 C  CG  . TYR   Z  12 75  ? 70.427  -183.607 20.841  1.00 104.69 ? 75  TYR   Z CG  1 
ATOM   44746 C  CD1 . TYR   Z  12 75  ? 69.554  -183.525 19.767  1.00 102.49 ? 75  TYR   Z CD1 1 
ATOM   44747 C  CD2 . TYR   Z  12 75  ? 71.784  -183.670 20.569  1.00 104.18 ? 75  TYR   Z CD2 1 
ATOM   44748 C  CE1 . TYR   Z  12 75  ? 70.015  -183.495 18.461  1.00 101.58 ? 75  TYR   Z CE1 1 
ATOM   44749 C  CE2 . TYR   Z  12 75  ? 72.263  -183.639 19.269  1.00 103.53 ? 75  TYR   Z CE2 1 
ATOM   44750 C  CZ  . TYR   Z  12 75  ? 71.375  -183.552 18.211  1.00 102.41 ? 75  TYR   Z CZ  1 
ATOM   44751 O  OH  . TYR   Z  12 75  ? 71.839  -183.521 16.928  1.00 102.79 ? 75  TYR   Z OH  1 
ATOM   44752 N  N   . HIS   Z  12 76  ? 71.413  -186.063 23.702  1.00 101.74 ? 76  HIS   Z N   1 
ATOM   44753 C  CA  . HIS   Z  12 76  ? 72.528  -187.036 23.872  1.00 103.17 ? 76  HIS   Z CA  1 
ATOM   44754 C  C   . HIS   Z  12 76  ? 71.966  -188.455 24.024  1.00 105.97 ? 76  HIS   Z C   1 
ATOM   44755 O  O   . HIS   Z  12 76  ? 72.468  -189.365 23.330  1.00 102.94 ? 76  HIS   Z O   1 
ATOM   44756 C  CB  . HIS   Z  12 76  ? 73.417  -186.675 25.073  1.00 102.16 ? 76  HIS   Z CB  1 
ATOM   44757 C  CG  . HIS   Z  12 76  ? 74.178  -185.401 24.919  1.00 99.82  ? 76  HIS   Z CG  1 
ATOM   44758 N  ND1 . HIS   Z  12 76  ? 74.718  -185.005 23.713  1.00 100.48 ? 76  HIS   Z ND1 1 
ATOM   44759 C  CD2 . HIS   Z  12 76  ? 74.514  -184.450 25.817  1.00 97.40  ? 76  HIS   Z CD2 1 
ATOM   44760 C  CE1 . HIS   Z  12 76  ? 75.338  -183.855 23.870  1.00 98.01  ? 76  HIS   Z CE1 1 
ATOM   44761 N  NE2 . HIS   Z  12 76  ? 75.230  -183.493 25.152  1.00 95.84  ? 76  HIS   Z NE2 1 
ATOM   44762 N  N   . PHE   Z  12 77  ? 70.972  -188.629 24.904  1.00 106.04 ? 77  PHE   Z N   1 
ATOM   44763 C  CA  . PHE   Z  12 77  ? 70.323  -189.932 25.214  1.00 107.35 ? 77  PHE   Z CA  1 
ATOM   44764 C  C   . PHE   Z  12 77  ? 69.699  -190.534 23.947  1.00 111.03 ? 77  PHE   Z C   1 
ATOM   44765 O  O   . PHE   Z  12 77  ? 69.780  -191.767 23.780  1.00 115.39 ? 77  PHE   Z O   1 
ATOM   44766 C  CB  . PHE   Z  12 77  ? 69.262  -189.786 26.313  1.00 104.94 ? 77  PHE   Z CB  1 
ATOM   44767 C  CG  . PHE   Z  12 77  ? 69.780  -189.670 27.727  1.00 106.42 ? 77  PHE   Z CG  1 
ATOM   44768 C  CD1 . PHE   Z  12 77  ? 70.972  -190.269 28.113  1.00 109.87 ? 77  PHE   Z CD1 1 
ATOM   44769 C  CD2 . PHE   Z  12 77  ? 69.046  -188.993 28.692  1.00 105.82 ? 77  PHE   Z CD2 1 
ATOM   44770 C  CE1 . PHE   Z  12 77  ? 71.431  -190.165 29.418  1.00 113.54 ? 77  PHE   Z CE1 1 
ATOM   44771 C  CE2 . PHE   Z  12 77  ? 69.504  -188.894 29.998  1.00 107.45 ? 77  PHE   Z CE2 1 
ATOM   44772 C  CZ  . PHE   Z  12 77  ? 70.696  -189.479 30.358  1.00 111.53 ? 77  PHE   Z CZ  1 
ATOM   44773 N  N   . ASP   Z  12 78  ? 69.108  -189.702 23.083  1.00 106.72 ? 78  ASP   Z N   1 
ATOM   44774 C  CA  . ASP   Z  12 78  ? 68.263  -190.153 21.943  1.00 110.46 ? 78  ASP   Z CA  1 
ATOM   44775 C  C   . ASP   Z  12 78  ? 69.078  -190.256 20.645  1.00 113.64 ? 78  ASP   Z C   1 
ATOM   44776 O  O   . ASP   Z  12 78  ? 68.583  -190.923 19.714  1.00 117.44 ? 78  ASP   Z O   1 
ATOM   44777 C  CB  . ASP   Z  12 78  ? 67.058  -189.228 21.745  1.00 110.26 ? 78  ASP   Z CB  1 
ATOM   44778 C  CG  . ASP   Z  12 78  ? 66.037  -189.289 22.869  1.00 112.73 ? 78  ASP   Z CG  1 
ATOM   44779 O  OD1 . ASP   Z  12 78  ? 65.734  -190.409 23.324  1.00 111.96 ? 78  ASP   Z OD1 1 
ATOM   44780 O  OD2 . ASP   Z  12 78  ? 65.549  -188.215 23.277  1.00 113.62 ? 78  ASP   Z OD2 1 
ATOM   44781 N  N   . HIS   Z  12 79  ? 70.257  -189.627 20.563  1.00 114.10 ? 79  HIS   Z N   1 
ATOM   44782 C  CA  . HIS   Z  12 79  ? 71.068  -189.547 19.314  1.00 115.02 ? 79  HIS   Z CA  1 
ATOM   44783 C  C   . HIS   Z  12 79  ? 72.549  -189.824 19.605  1.00 114.34 ? 79  HIS   Z C   1 
ATOM   44784 O  O   . HIS   Z  12 79  ? 73.401  -189.047 19.132  1.00 115.27 ? 79  HIS   Z O   1 
ATOM   44785 C  CB  . HIS   Z  12 79  ? 70.824  -188.203 18.610  1.00 115.37 ? 79  HIS   Z CB  1 
ATOM   44786 C  CG  . HIS   Z  12 79  ? 69.378  -187.927 18.368  1.00 116.79 ? 79  HIS   Z CG  1 
ATOM   44787 N  ND1 . HIS   Z  12 79  ? 68.597  -187.255 19.288  1.00 118.89 ? 79  HIS   Z ND1 1 
ATOM   44788 C  CD2 . HIS   Z  12 79  ? 68.563  -188.252 17.340  1.00 116.99 ? 79  HIS   Z CD2 1 
ATOM   44789 C  CE1 . HIS   Z  12 79  ? 67.364  -187.165 18.831  1.00 119.55 ? 79  HIS   Z CE1 1 
ATOM   44790 N  NE2 . HIS   Z  12 79  ? 67.316  -187.772 17.637  1.00 118.17 ? 79  HIS   Z NE2 1 
ATOM   44791 N  N   . ASN   Z  12 80  ? 72.828  -190.904 20.340  1.00 116.51 ? 80  ASN   Z N   1 
ATOM   44792 C  CA  . ASN   Z  12 80  ? 74.174  -191.520 20.507  1.00 120.64 ? 80  ASN   Z CA  1 
ATOM   44793 C  C   . ASN   Z  12 80  ? 75.215  -190.451 20.869  1.00 117.83 ? 80  ASN   Z C   1 
ATOM   44794 O  O   . ASN   Z  12 80  ? 76.278  -190.416 20.217  1.00 115.59 ? 80  ASN   Z O   1 
ATOM   44795 C  CB  . ASN   Z  12 80  ? 74.566  -192.308 19.251  1.00 128.41 ? 80  ASN   Z CB  1 
ATOM   44796 C  CG  . ASN   Z  12 80  ? 75.690  -193.300 19.476  1.00 134.84 ? 80  ASN   Z CG  1 
ATOM   44797 O  OD1 . ASN   Z  12 80  ? 76.623  -193.373 18.680  1.00 143.10 ? 80  ASN   Z OD1 1 
ATOM   44798 N  ND2 . ASN   Z  12 80  ? 75.612  -194.077 20.546  1.00 136.80 ? 80  ASN   Z ND2 1 
ATOM   44799 N  N   . ASP   Z  12 81  ? 74.915  -189.619 21.874  1.00 115.92 ? 81  ASP   Z N   1 
ATOM   44800 C  CA  . ASP   Z  12 81  ? 75.835  -188.609 22.472  1.00 116.58 ? 81  ASP   Z CA  1 
ATOM   44801 C  C   . ASP   Z  12 81  ? 76.279  -187.564 21.434  1.00 113.84 ? 81  ASP   Z C   1 
ATOM   44802 O  O   . ASP   Z  12 81  ? 77.272  -186.858 21.712  1.00 116.16 ? 81  ASP   Z O   1 
ATOM   44803 C  CB  . ASP   Z  12 81  ? 77.057  -189.283 23.111  1.00 116.42 ? 81  ASP   Z CB  1 
ATOM   44804 C  CG  . ASP   Z  12 81  ? 76.908  -189.583 24.594  1.00 118.38 ? 81  ASP   Z CG  1 
ATOM   44805 O  OD1 . ASP   Z  12 81  ? 76.251  -188.787 25.294  1.00 112.24 ? 81  ASP   Z OD1 1 
ATOM   44806 O  OD2 . ASP   Z  12 81  ? 77.463  -190.607 25.040  1.00 120.83 ? 81  ASP   Z OD2 1 
ATOM   44807 N  N   . LYS   Z  12 82  ? 75.574  -187.435 20.303  1.00 112.05 ? 82  LYS   Z N   1 
ATOM   44808 C  CA  . LYS   Z  12 82  ? 75.915  -186.466 19.225  1.00 110.75 ? 82  LYS   Z CA  1 
ATOM   44809 C  C   . LYS   Z  12 82  ? 75.936  -185.055 19.818  1.00 107.72 ? 82  LYS   Z C   1 
ATOM   44810 O  O   . LYS   Z  12 82  ? 75.067  -184.761 20.664  1.00 104.67 ? 82  LYS   Z O   1 
ATOM   44811 C  CB  . LYS   Z  12 82  ? 74.908  -186.530 18.073  1.00 111.58 ? 82  LYS   Z CB  1 
ATOM   44812 C  CG  . LYS   Z  12 82  ? 75.093  -185.458 17.005  1.00 110.80 ? 82  LYS   Z CG  1 
ATOM   44813 C  CD  . LYS   Z  12 82  ? 74.191  -185.618 15.804  1.00 112.69 ? 82  LYS   Z CD  1 
ATOM   44814 C  CE  . LYS   Z  12 82  ? 74.372  -184.503 14.796  1.00 111.14 ? 82  LYS   Z CE  1 
ATOM   44815 N  NZ  . LYS   Z  12 82  ? 73.675  -184.793 13.522  1.00 112.80 ? 82  LYS   Z NZ  1 
ATOM   44816 N  N   . LYS   Z  12 83  ? 76.886  -184.222 19.381  1.00 110.31 ? 83  LYS   Z N   1 
ATOM   44817 C  CA  . LYS   Z  12 83  ? 77.010  -182.804 19.815  1.00 107.85 ? 83  LYS   Z CA  1 
ATOM   44818 C  C   . LYS   Z  12 83  ? 75.871  -181.990 19.190  1.00 103.35 ? 83  LYS   Z C   1 
ATOM   44819 O  O   . LYS   Z  12 83  ? 75.667  -182.097 17.963  1.00 98.52  ? 83  LYS   Z O   1 
ATOM   44820 C  CB  . LYS   Z  12 83  ? 78.368  -182.211 19.422  1.00 111.83 ? 83  LYS   Z CB  1 
ATOM   44821 C  CG  . LYS   Z  12 83  ? 78.717  -180.917 20.145  1.00 111.70 ? 83  LYS   Z CG  1 
ATOM   44822 C  CD  . LYS   Z  12 83  ? 79.785  -180.089 19.470  1.00 115.39 ? 83  LYS   Z CD  1 
ATOM   44823 C  CE  . LYS   Z  12 83  ? 80.105  -178.832 20.249  1.00 115.90 ? 83  LYS   Z CE  1 
ATOM   44824 N  NZ  . LYS   Z  12 83  ? 81.063  -177.967 19.525  1.00 121.67 ? 83  LYS   Z NZ  1 
ATOM   44825 N  N   . LEU   Z  12 84  ? 75.164  -181.208 20.010  1.00 100.71 ? 84  LEU   Z N   1 
ATOM   44826 C  CA  . LEU   Z  12 84  ? 74.090  -180.283 19.562  1.00 101.10 ? 84  LEU   Z CA  1 
ATOM   44827 C  C   . LEU   Z  12 84  ? 74.739  -179.010 19.010  1.00 100.29 ? 84  LEU   Z C   1 
ATOM   44828 O  O   . LEU   Z  12 84  ? 75.263  -178.213 19.815  1.00 94.27  ? 84  LEU   Z O   1 
ATOM   44829 C  CB  . LEU   Z  12 84  ? 73.160  -179.969 20.738  1.00 100.93 ? 84  LEU   Z CB  1 
ATOM   44830 C  CG  . LEU   Z  12 84  ? 71.963  -179.079 20.406  1.00 102.02 ? 84  LEU   Z CG  1 
ATOM   44831 C  CD1 . LEU   Z  12 84  ? 71.022  -179.764 19.427  1.00 101.88 ? 84  LEU   Z CD1 1 
ATOM   44832 C  CD2 . LEU   Z  12 84  ? 71.217  -178.685 21.670  1.00 103.69 ? 84  LEU   Z CD2 1 
ATOM   44833 N  N   . SER   Z  12 85  ? 74.717  -178.846 17.685  1.00 103.88 ? 85  SER   Z N   1 
ATOM   44834 C  CA  . SER   Z  12 85  ? 75.238  -177.657 16.961  1.00 107.61 ? 85  SER   Z CA  1 
ATOM   44835 C  C   . SER   Z  12 85  ? 74.393  -176.430 17.326  1.00 108.30 ? 85  SER   Z C   1 
ATOM   44836 O  O   . SER   Z  12 85  ? 73.193  -176.607 17.628  1.00 108.45 ? 85  SER   Z O   1 
ATOM   44837 C  CB  . SER   Z  12 85  ? 75.264  -177.899 15.473  1.00 110.85 ? 85  SER   Z CB  1 
ATOM   44838 O  OG  . SER   Z  12 85  ? 73.997  -178.343 15.005  1.00 111.95 ? 85  SER   Z OG  1 
ATOM   44839 N  N   . ILE   Z  12 86  ? 75.005  -175.239 17.306  1.00 109.26 ? 86  ILE   Z N   1 
ATOM   44840 C  CA  . ILE   Z  12 86  ? 74.379  -173.951 17.736  1.00 105.63 ? 86  ILE   Z CA  1 
ATOM   44841 C  C   . ILE   Z  12 86  ? 73.108  -173.698 16.910  1.00 103.78 ? 86  ILE   Z C   1 
ATOM   44842 O  O   . ILE   Z  12 86  ? 72.119  -173.212 17.496  1.00 100.01 ? 86  ILE   Z O   1 
ATOM   44843 C  CB  . ILE   Z  12 86  ? 75.384  -172.781 17.640  1.00 106.30 ? 86  ILE   Z CB  1 
ATOM   44844 C  CG1 . ILE   Z  12 86  ? 74.901  -171.554 18.421  1.00 105.46 ? 86  ILE   Z CG1 1 
ATOM   44845 C  CG2 . ILE   Z  12 86  ? 75.711  -172.438 16.192  1.00 107.18 ? 86  ILE   Z CG2 1 
ATOM   44846 C  CD1 . ILE   Z  12 86  ? 75.105  -171.654 19.916  1.00 104.80 ? 86  ILE   Z CD1 1 
ATOM   44847 N  N   . ASN   Z  12 87  ? 73.134  -174.017 15.611  1.00 105.47 ? 87  ASN   Z N   1 
ATOM   44848 C  CA  . ASN   Z  12 87  ? 71.998  -173.819 14.668  1.00 104.05 ? 87  ASN   Z CA  1 
ATOM   44849 C  C   . ASN   Z  12 87  ? 70.828  -174.731 15.064  1.00 103.56 ? 87  ASN   Z C   1 
ATOM   44850 O  O   . ASN   Z  12 87  ? 69.669  -174.294 14.924  1.00 103.89 ? 87  ASN   Z O   1 
ATOM   44851 C  CB  . ASN   Z  12 87  ? 72.407  -174.077 13.216  1.00 106.42 ? 87  ASN   Z CB  1 
ATOM   44852 C  CG  . ASN   Z  12 87  ? 72.647  -175.546 12.938  1.00 105.21 ? 87  ASN   Z CG  1 
ATOM   44853 O  OD1 . ASN   Z  12 87  ? 73.614  -176.123 13.429  1.00 104.27 ? 87  ASN   Z OD1 1 
ATOM   44854 N  ND2 . ASN   Z  12 87  ? 71.760  -176.166 12.177  1.00 107.01 ? 87  ASN   Z ND2 1 
ATOM   44855 N  N   . SER   Z  12 88  ? 71.121  -175.952 15.528  1.00 101.49 ? 88  SER   Z N   1 
ATOM   44856 C  CA  . SER   Z  12 88  ? 70.118  -176.945 15.998  1.00 99.18  ? 88  SER   Z CA  1 
ATOM   44857 C  C   . SER   Z  12 88  ? 69.562  -176.510 17.358  1.00 95.51  ? 88  SER   Z C   1 
ATOM   44858 O  O   . SER   Z  12 88  ? 68.337  -176.624 17.557  1.00 93.70  ? 88  SER   Z O   1 
ATOM   44859 C  CB  . SER   Z  12 88  ? 70.701  -178.334 16.060  1.00 98.53  ? 88  SER   Z CB  1 
ATOM   44860 O  OG  . SER   Z  12 88  ? 71.096  -178.780 14.770  1.00 98.99  ? 88  SER   Z OG  1 
ATOM   44861 N  N   . ALA   Z  12 89  ? 70.431  -176.030 18.253  1.00 95.45  ? 89  ALA   Z N   1 
ATOM   44862 C  CA  . ALA   Z  12 89  ? 70.056  -175.444 19.561  1.00 97.53  ? 89  ALA   Z CA  1 
ATOM   44863 C  C   . ALA   Z  12 89  ? 69.048  -174.312 19.331  1.00 97.16  ? 89  ALA   Z C   1 
ATOM   44864 O  O   . ALA   Z  12 89  ? 67.987  -174.328 19.987  1.00 91.97  ? 89  ALA   Z O   1 
ATOM   44865 C  CB  . ALA   Z  12 89  ? 71.283  -174.949 20.288  1.00 99.84  ? 89  ALA   Z CB  1 
ATOM   44866 N  N   . ALA   Z  12 90  ? 69.366  -173.387 18.416  1.00 99.30  ? 90  ALA   Z N   1 
ATOM   44867 C  CA  . ALA   Z  12 90  ? 68.526  -172.220 18.058  1.00 100.44 ? 90  ALA   Z CA  1 
ATOM   44868 C  C   . ALA   Z  12 90  ? 67.126  -172.701 17.662  1.00 99.55  ? 90  ALA   Z C   1 
ATOM   44869 O  O   . ALA   Z  12 90  ? 66.142  -172.220 18.257  1.00 102.81 ? 90  ALA   Z O   1 
ATOM   44870 C  CB  . ALA   Z  12 90  ? 69.168  -171.421 16.949  1.00 104.09 ? 90  ALA   Z CB  1 
ATOM   44871 N  N   . ARG   Z  12 91  ? 67.048  -173.631 16.707  1.00 99.37  ? 91  ARG   Z N   1 
ATOM   44872 C  CA  . ARG   Z  12 91  ? 65.766  -174.169 16.181  1.00 98.57  ? 91  ARG   Z CA  1 
ATOM   44873 C  C   . ARG   Z  12 91  ? 64.978  -174.832 17.317  1.00 94.10  ? 91  ARG   Z C   1 
ATOM   44874 O  O   . ARG   Z  12 91  ? 63.739  -174.719 17.318  1.00 90.54  ? 91  ARG   Z O   1 
ATOM   44875 C  CB  . ARG   Z  12 91  ? 66.021  -175.164 15.044  1.00 101.69 ? 91  ARG   Z CB  1 
ATOM   44876 C  CG  . ARG   Z  12 91  ? 64.755  -175.779 14.463  1.00 102.75 ? 91  ARG   Z CG  1 
ATOM   44877 C  CD  . ARG   Z  12 91  ? 63.795  -174.744 13.907  1.00 103.80 ? 91  ARG   Z CD  1 
ATOM   44878 N  NE  . ARG   Z  12 91  ? 64.260  -174.202 12.638  1.00 106.65 ? 91  ARG   Z NE  1 
ATOM   44879 C  CZ  . ARG   Z  12 91  ? 64.069  -174.769 11.450  1.00 107.33 ? 91  ARG   Z CZ  1 
ATOM   44880 N  NH1 . ARG   Z  12 91  ? 63.414  -175.913 11.349  1.00 109.57 ? 91  ARG   Z NH1 1 
ATOM   44881 N  NH2 . ARG   Z  12 91  ? 64.537  -174.187 10.360  1.00 108.49 ? 91  ARG   Z NH2 1 
ATOM   44882 N  N   . ASN   Z  12 92  ? 65.672  -175.506 18.238  1.00 95.00  ? 92  ASN   Z N   1 
ATOM   44883 C  CA  . ASN   Z  12 92  ? 65.051  -176.201 19.397  1.00 94.99  ? 92  ASN   Z CA  1 
ATOM   44884 C  C   . ASN   Z  12 92  ? 64.417  -175.154 20.321  1.00 94.38  ? 92  ASN   Z C   1 
ATOM   44885 O  O   . ASN   Z  12 92  ? 63.246  -175.354 20.709  1.00 93.76  ? 92  ASN   Z O   1 
ATOM   44886 C  CB  . ASN   Z  12 92  ? 66.055  -177.092 20.135  1.00 97.14  ? 92  ASN   Z CB  1 
ATOM   44887 C  CG  . ASN   Z  12 92  ? 65.490  -177.718 21.395  1.00 95.82  ? 92  ASN   Z CG  1 
ATOM   44888 O  OD1 . ASN   Z  12 92  ? 66.116  -177.669 22.451  1.00 97.38  ? 92  ASN   Z OD1 1 
ATOM   44889 N  ND2 . ASN   Z  12 92  ? 64.307  -178.304 21.302  1.00 97.06  ? 92  ASN   Z ND2 1 
ATOM   44890 N  N   . ILE   Z  12 93  ? 65.154  -174.080 20.637  1.00 92.57  ? 93  ILE   Z N   1 
ATOM   44891 C  CA  . ILE   Z  12 93  ? 64.710  -172.991 21.562  1.00 88.99  ? 93  ILE   Z CA  1 
ATOM   44892 C  C   . ILE   Z  12 93  ? 63.472  -172.309 20.964  1.00 83.53  ? 93  ILE   Z C   1 
ATOM   44893 O  O   . ILE   Z  12 93  ? 62.585  -171.939 21.755  1.00 80.88  ? 93  ILE   Z O   1 
ATOM   44894 C  CB  . ILE   Z  12 93  ? 65.856  -172.002 21.878  1.00 89.27  ? 93  ILE   Z CB  1 
ATOM   44895 C  CG1 . ILE   Z  12 93  ? 66.954  -172.674 22.708  1.00 91.38  ? 93  ILE   Z CG1 1 
ATOM   44896 C  CG2 . ILE   Z  12 93  ? 65.335  -170.750 22.573  1.00 89.10  ? 93  ILE   Z CG2 1 
ATOM   44897 C  CD1 . ILE   Z  12 93  ? 68.218  -171.854 22.865  1.00 92.06  ? 93  ILE   Z CD1 1 
ATOM   44898 N  N   . GLN   Z  12 94  ? 63.394  -172.172 19.632  1.00 83.87  ? 94  GLN   Z N   1 
ATOM   44899 C  CA  . GLN   Z  12 94  ? 62.206  -171.594 18.943  1.00 85.72  ? 94  GLN   Z CA  1 
ATOM   44900 C  C   . GLN   Z  12 94  ? 60.958  -172.378 19.362  1.00 88.09  ? 94  GLN   Z C   1 
ATOM   44901 O  O   . GLN   Z  12 94  ? 59.942  -171.748 19.707  1.00 85.92  ? 94  GLN   Z O   1 
ATOM   44902 C  CB  . GLN   Z  12 94  ? 62.335  -171.620 17.417  1.00 87.74  ? 94  GLN   Z CB  1 
ATOM   44903 C  CG  . GLN   Z  12 94  ? 61.037  -171.246 16.708  1.00 88.14  ? 94  GLN   Z CG  1 
ATOM   44904 C  CD  . GLN   Z  12 94  ? 61.215  -171.021 15.227  1.00 90.97  ? 94  GLN   Z CD  1 
ATOM   44905 O  OE1 . GLN   Z  12 94  ? 61.327  -171.965 14.447  1.00 90.72  ? 94  GLN   Z OE1 1 
ATOM   44906 N  NE2 . GLN   Z  12 94  ? 61.229  -169.761 14.822  1.00 91.21  ? 94  GLN   Z NE2 1 
ATOM   44907 N  N   . HIS   Z  12 95  ? 61.040  -173.708 19.326  1.00 87.03  ? 95  HIS   Z N   1 
ATOM   44908 C  CA  . HIS   Z  12 95  ? 59.914  -174.623 19.652  1.00 88.22  ? 95  HIS   Z CA  1 
ATOM   44909 C  C   . HIS   Z  12 95  ? 59.606  -174.581 21.152  1.00 89.70  ? 95  HIS   Z C   1 
ATOM   44910 O  O   . HIS   Z  12 95  ? 58.423  -174.762 21.499  1.00 92.95  ? 95  HIS   Z O   1 
ATOM   44911 C  CB  . HIS   Z  12 95  ? 60.207  -176.042 19.159  1.00 89.65  ? 95  HIS   Z CB  1 
ATOM   44912 C  CG  . HIS   Z  12 95  ? 59.923  -176.222 17.706  1.00 92.20  ? 95  HIS   Z CG  1 
ATOM   44913 N  ND1 . HIS   Z  12 95  ? 60.848  -175.906 16.729  1.00 94.22  ? 95  HIS   Z ND1 1 
ATOM   44914 C  CD2 . HIS   Z  12 95  ? 58.820  -176.658 17.060  1.00 93.69  ? 95  HIS   Z CD2 1 
ATOM   44915 C  CE1 . HIS   Z  12 95  ? 60.330  -176.150 15.543  1.00 96.12  ? 95  HIS   Z CE1 1 
ATOM   44916 N  NE2 . HIS   Z  12 95  ? 59.087  -176.613 15.719  1.00 93.94  ? 95  HIS   Z NE2 1 
ATOM   44917 N  N   . LEU   Z  12 96  ? 60.615  -174.358 22.001  1.00 91.12  ? 96  LEU   Z N   1 
ATOM   44918 C  CA  . LEU   Z  12 96  ? 60.422  -174.152 23.464  1.00 90.99  ? 96  LEU   Z CA  1 
ATOM   44919 C  C   . LEU   Z  12 96  ? 59.575  -172.891 23.679  1.00 89.99  ? 96  LEU   Z C   1 
ATOM   44920 O  O   . LEU   Z  12 96  ? 58.565  -172.969 24.414  1.00 90.41  ? 96  LEU   Z O   1 
ATOM   44921 C  CB  . LEU   Z  12 96  ? 61.778  -174.029 24.170  1.00 88.30  ? 96  LEU   Z CB  1 
ATOM   44922 C  CG  . LEU   Z  12 96  ? 62.607  -175.308 24.264  1.00 88.06  ? 96  LEU   Z CG  1 
ATOM   44923 C  CD1 . LEU   Z  12 96  ? 63.926  -175.041 24.974  1.00 87.33  ? 96  LEU   Z CD1 1 
ATOM   44924 C  CD2 . LEU   Z  12 96  ? 61.838  -176.408 24.979  1.00 86.64  ? 96  LEU   Z CD2 1 
ATOM   44925 N  N   . LEU   Z  12 97  ? 59.968  -171.782 23.047  1.00 88.33  ? 97  LEU   Z N   1 
ATOM   44926 C  CA  . LEU   Z  12 97  ? 59.311  -170.461 23.210  1.00 86.77  ? 97  LEU   Z CA  1 
ATOM   44927 C  C   . LEU   Z  12 97  ? 57.904  -170.511 22.601  1.00 86.06  ? 97  LEU   Z C   1 
ATOM   44928 O  O   . LEU   Z  12 97  ? 56.944  -170.205 23.341  1.00 86.11  ? 97  LEU   Z O   1 
ATOM   44929 C  CB  . LEU   Z  12 97  ? 60.181  -169.379 22.564  1.00 87.60  ? 97  LEU   Z CB  1 
ATOM   44930 C  CG  . LEU   Z  12 97  ? 61.446  -169.009 23.338  1.00 91.00  ? 97  LEU   Z CG  1 
ATOM   44931 C  CD1 . LEU   Z  12 97  ? 62.407  -168.220 22.461  1.00 91.98  ? 97  LEU   Z CD1 1 
ATOM   44932 C  CD2 . LEU   Z  12 97  ? 61.105  -168.215 24.593  1.00 95.22  ? 97  LEU   Z CD2 1 
ATOM   44933 N  N   . TYR   Z  12 98  ? 57.780  -170.908 21.326  1.00 84.19  ? 98  TYR   Z N   1 
ATOM   44934 C  CA  . TYR   Z  12 98  ? 56.504  -170.853 20.560  1.00 84.39  ? 98  TYR   Z CA  1 
ATOM   44935 C  C   . TYR   Z  12 98  ? 55.494  -171.853 21.136  1.00 83.53  ? 98  TYR   Z C   1 
ATOM   44936 O  O   . TYR   Z  12 98  ? 54.281  -171.669 20.924  1.00 83.55  ? 98  TYR   Z O   1 
ATOM   44937 C  CB  . TYR   Z  12 98  ? 56.693  -171.102 19.060  1.00 84.37  ? 98  TYR   Z CB  1 
ATOM   44938 C  CG  . TYR   Z  12 98  ? 55.540  -170.571 18.246  1.00 84.03  ? 98  TYR   Z CG  1 
ATOM   44939 C  CD1 . TYR   Z  12 98  ? 55.531  -169.259 17.806  1.00 85.19  ? 98  TYR   Z CD1 1 
ATOM   44940 C  CD2 . TYR   Z  12 98  ? 54.423  -171.347 17.982  1.00 84.50  ? 98  TYR   Z CD2 1 
ATOM   44941 C  CE1 . TYR   Z  12 98  ? 54.464  -168.741 17.093  1.00 85.55  ? 98  TYR   Z CE1 1 
ATOM   44942 C  CE2 . TYR   Z  12 98  ? 53.346  -170.845 17.269  1.00 84.57  ? 98  TYR   Z CE2 1 
ATOM   44943 C  CZ  . TYR   Z  12 98  ? 53.367  -169.537 16.823  1.00 85.10  ? 98  TYR   Z CZ  1 
ATOM   44944 O  OH  . TYR   Z  12 98  ? 52.320  -169.020 16.123  1.00 86.14  ? 98  TYR   Z OH  1 
ATOM   44945 N  N   . GLY   Z  12 99  ? 55.975  -172.879 21.840  1.00 84.43  ? 99  GLY   Z N   1 
ATOM   44946 C  CA  . GLY   Z  12 99  ? 55.121  -173.825 22.585  1.00 87.29  ? 99  GLY   Z CA  1 
ATOM   44947 C  C   . GLY   Z  12 99  ? 54.240  -173.106 23.594  1.00 86.90  ? 99  GLY   Z C   1 
ATOM   44948 O  O   . GLY   Z  12 99  ? 53.148  -173.622 23.898  1.00 90.04  ? 99  GLY   Z O   1 
ATOM   44949 N  N   . LYS   Z  12 100 ? 54.696  -171.955 24.096  1.00 85.14  ? 100 LYS   Z N   1 
ATOM   44950 C  CA  . LYS   Z  12 100 ? 53.923  -171.077 25.012  1.00 85.50  ? 100 LYS   Z CA  1 
ATOM   44951 C  C   . LYS   Z  12 100 ? 53.566  -169.774 24.285  1.00 87.22  ? 100 LYS   Z C   1 
ATOM   44952 O  O   . LYS   Z  12 100 ? 53.699  -168.700 24.899  1.00 88.22  ? 100 LYS   Z O   1 
ATOM   44953 C  CB  . LYS   Z  12 100 ? 54.733  -170.835 26.289  1.00 84.94  ? 100 LYS   Z CB  1 
ATOM   44954 C  CG  . LYS   Z  12 100 ? 54.619  -171.935 27.334  1.00 84.45  ? 100 LYS   Z CG  1 
ATOM   44955 C  CD  . LYS   Z  12 100 ? 55.518  -171.737 28.535  1.00 85.46  ? 100 LYS   Z CD  1 
ATOM   44956 C  CE  . LYS   Z  12 100 ? 55.244  -170.470 29.319  1.00 85.25  ? 100 LYS   Z CE  1 
ATOM   44957 N  NZ  . LYS   Z  12 100 ? 53.857  -170.421 29.844  1.00 87.07  ? 100 LYS   Z NZ  1 
ATOM   44958 N  N   . ARG   Z  12 101 ? 53.107  -169.866 23.032  1.00 84.75  ? 101 ARG   Z N   1 
ATOM   44959 C  CA  . ARG   Z  12 101 ? 52.727  -168.692 22.200  1.00 84.02  ? 101 ARG   Z CA  1 
ATOM   44960 C  C   . ARG   Z  12 101 ? 51.619  -167.899 22.904  1.00 84.43  ? 101 ARG   Z C   1 
ATOM   44961 O  O   . ARG   Z  12 101 ? 51.685  -166.661 22.881  1.00 85.34  ? 101 ARG   Z O   1 
ATOM   44962 C  CB  . ARG   Z  12 101 ? 52.280  -169.131 20.802  1.00 84.96  ? 101 ARG   Z CB  1 
ATOM   44963 C  CG  . ARG   Z  12 101 ? 51.574  -168.050 19.995  1.00 86.36  ? 101 ARG   Z CG  1 
ATOM   44964 C  CD  . ARG   Z  12 101 ? 52.432  -166.819 19.764  1.00 86.39  ? 101 ARG   Z CD  1 
ATOM   44965 N  NE  . ARG   Z  12 101 ? 51.819  -165.923 18.794  1.00 86.13  ? 101 ARG   Z NE  1 
ATOM   44966 C  CZ  . ARG   Z  12 101 ? 50.811  -165.089 19.048  1.00 85.45  ? 101 ARG   Z CZ  1 
ATOM   44967 N  NH1 . ARG   Z  12 101 ? 50.281  -165.015 20.259  1.00 85.25  ? 101 ARG   Z NH1 1 
ATOM   44968 N  NH2 . ARG   Z  12 101 ? 50.330  -164.327 18.081  1.00 88.69  ? 101 ARG   Z NH2 1 
ATOM   44969 N  N   . PHE   Z  12 102 ? 50.645  -168.582 23.510  1.00 82.92  ? 102 PHE   Z N   1 
ATOM   44970 C  CA  . PHE   Z  12 102 ? 49.432  -167.957 24.099  1.00 84.63  ? 102 PHE   Z CA  1 
ATOM   44971 C  C   . PHE   Z  12 102 ? 49.559  -167.833 25.623  1.00 85.33  ? 102 PHE   Z C   1 
ATOM   44972 O  O   . PHE   Z  12 102 ? 48.547  -167.506 26.270  1.00 90.32  ? 102 PHE   Z O   1 
ATOM   44973 C  CB  . PHE   Z  12 102 ? 48.195  -168.742 23.667  1.00 84.09  ? 102 PHE   Z CB  1 
ATOM   44974 C  CG  . PHE   Z  12 102 ? 48.056  -168.818 22.171  1.00 87.52  ? 102 PHE   Z CG  1 
ATOM   44975 C  CD1 . PHE   Z  12 102 ? 47.767  -167.680 21.433  1.00 87.89  ? 102 PHE   Z CD1 1 
ATOM   44976 C  CD2 . PHE   Z  12 102 ? 48.251  -170.013 21.496  1.00 87.89  ? 102 PHE   Z CD2 1 
ATOM   44977 C  CE1 . PHE   Z  12 102 ? 47.651  -167.741 20.053  1.00 90.45  ? 102 PHE   Z CE1 1 
ATOM   44978 C  CE2 . PHE   Z  12 102 ? 48.135  -170.072 20.115  1.00 88.86  ? 102 PHE   Z CE2 1 
ATOM   44979 C  CZ  . PHE   Z  12 102 ? 47.837  -168.937 19.397  1.00 89.75  ? 102 PHE   Z CZ  1 
ATOM   44980 N  N   . PHE   Z  12 103 ? 50.754  -168.070 26.173  1.00 86.18  ? 103 PHE   Z N   1 
ATOM   44981 C  CA  . PHE   Z  12 103 ? 51.137  -167.679 27.557  1.00 88.72  ? 103 PHE   Z CA  1 
ATOM   44982 C  C   . PHE   Z  12 103 ? 52.650  -167.486 27.602  1.00 88.44  ? 103 PHE   Z C   1 
ATOM   44983 O  O   . PHE   Z  12 103 ? 53.355  -168.206 28.304  1.00 89.23  ? 103 PHE   Z O   1 
ATOM   44984 C  CB  . PHE   Z  12 103 ? 50.626  -168.704 28.573  1.00 89.99  ? 103 PHE   Z CB  1 
ATOM   44985 C  CG  . PHE   Z  12 103 ? 50.731  -168.293 30.022  1.00 94.81  ? 103 PHE   Z CG  1 
ATOM   44986 C  CD1 . PHE   Z  12 103 ? 50.925  -166.967 30.389  1.00 96.92  ? 103 PHE   Z CD1 1 
ATOM   44987 C  CD2 . PHE   Z  12 103 ? 50.606  -169.238 31.029  1.00 94.65  ? 103 PHE   Z CD2 1 
ATOM   44988 C  CE1 . PHE   Z  12 103 ? 51.016  -166.604 31.724  1.00 99.66  ? 103 PHE   Z CE1 1 
ATOM   44989 C  CE2 . PHE   Z  12 103 ? 50.691  -168.872 32.364  1.00 96.25  ? 103 PHE   Z CE2 1 
ATOM   44990 C  CZ  . PHE   Z  12 103 ? 50.898  -167.556 32.709  1.00 98.55  ? 103 PHE   Z CZ  1 
ATOM   44991 N  N   . PRO   Z  12 104 ? 53.182  -166.479 26.872  1.00 89.19  ? 104 PRO   Z N   1 
ATOM   44992 C  CA  . PRO   Z  12 104 ? 54.606  -166.425 26.534  1.00 90.31  ? 104 PRO   Z CA  1 
ATOM   44993 C  C   . PRO   Z  12 104 ? 55.546  -166.381 27.746  1.00 89.90  ? 104 PRO   Z C   1 
ATOM   44994 O  O   . PRO   Z  12 104 ? 55.131  -165.934 28.802  1.00 91.67  ? 104 PRO   Z O   1 
ATOM   44995 C  CB  . PRO   Z  12 104 ? 54.746  -165.116 25.735  1.00 90.62  ? 104 PRO   Z CB  1 
ATOM   44996 C  CG  . PRO   Z  12 104 ? 53.343  -164.805 25.257  1.00 90.54  ? 104 PRO   Z CG  1 
ATOM   44997 C  CD  . PRO   Z  12 104 ? 52.441  -165.318 26.358  1.00 89.16  ? 104 PRO   Z CD  1 
ATOM   44998 N  N   . TYR   Z  12 105 ? 56.780  -166.856 27.558  1.00 90.81  ? 105 TYR   Z N   1 
ATOM   44999 C  CA  . TYR   Z  12 105 ? 57.939  -166.531 28.428  1.00 95.15  ? 105 TYR   Z CA  1 
ATOM   45000 C  C   . TYR   Z  12 105 ? 58.308  -165.063 28.187  1.00 90.98  ? 105 TYR   Z C   1 
ATOM   45001 O  O   . TYR   Z  12 105 ? 58.725  -164.746 27.054  1.00 90.50  ? 105 TYR   Z O   1 
ATOM   45002 C  CB  . TYR   Z  12 105 ? 59.157  -167.406 28.114  1.00 96.91  ? 105 TYR   Z CB  1 
ATOM   45003 C  CG  . TYR   Z  12 105 ? 59.044  -168.876 28.437  1.00 96.98  ? 105 TYR   Z CG  1 
ATOM   45004 C  CD1 . TYR   Z  12 105 ? 58.954  -169.322 29.747  1.00 99.06  ? 105 TYR   Z CD1 1 
ATOM   45005 C  CD2 . TYR   Z  12 105 ? 59.092  -169.831 27.436  1.00 98.41  ? 105 TYR   Z CD2 1 
ATOM   45006 C  CE1 . TYR   Z  12 105 ? 58.879  -170.672 30.050  1.00 99.31  ? 105 TYR   Z CE1 1 
ATOM   45007 C  CE2 . TYR   Z  12 105 ? 59.020  -171.185 27.721  1.00 99.87  ? 105 TYR   Z CE2 1 
ATOM   45008 C  CZ  . TYR   Z  12 105 ? 58.915  -171.610 29.034  1.00 100.05 ? 105 TYR   Z CZ  1 
ATOM   45009 O  OH  . TYR   Z  12 105 ? 58.839  -172.941 29.334  1.00 97.75  ? 105 TYR   Z OH  1 
ATOM   45010 N  N   . TYR   Z  12 106 ? 58.151  -164.198 29.194  1.00 91.18  ? 106 TYR   Z N   1 
ATOM   45011 C  CA  . TYR   Z  12 106 ? 58.508  -162.755 29.114  1.00 89.95  ? 106 TYR   Z CA  1 
ATOM   45012 C  C   . TYR   Z  12 106 ? 60.026  -162.616 29.249  1.00 87.10  ? 106 TYR   Z C   1 
ATOM   45013 O  O   . TYR   Z  12 106 ? 60.502  -162.086 30.272  1.00 85.43  ? 106 TYR   Z O   1 
ATOM   45014 C  CB  . TYR   Z  12 106 ? 57.765  -161.923 30.165  1.00 94.27  ? 106 TYR   Z CB  1 
ATOM   45015 C  CG  . TYR   Z  12 106 ? 56.667  -161.057 29.603  1.00 101.04 ? 106 TYR   Z CG  1 
ATOM   45016 C  CD1 . TYR   Z  12 106 ? 55.597  -161.620 28.926  1.00 106.57 ? 106 TYR   Z CD1 1 
ATOM   45017 C  CD2 . TYR   Z  12 106 ? 56.698  -159.678 29.735  1.00 103.24 ? 106 TYR   Z CD2 1 
ATOM   45018 C  CE1 . TYR   Z  12 106 ? 54.582  -160.840 28.396  1.00 112.70 ? 106 TYR   Z CE1 1 
ATOM   45019 C  CE2 . TYR   Z  12 106 ? 55.689  -158.882 29.214  1.00 111.10 ? 106 TYR   Z CE2 1 
ATOM   45020 C  CZ  . TYR   Z  12 106 ? 54.628  -159.465 28.542  1.00 112.03 ? 106 TYR   Z CZ  1 
ATOM   45021 O  OH  . TYR   Z  12 106 ? 53.627  -158.697 28.021  1.00 123.46 ? 106 TYR   Z OH  1 
ATOM   45022 N  N   . VAL   Z  12 107 ? 60.764  -163.095 28.245  1.00 82.60  ? 107 VAL   Z N   1 
ATOM   45023 C  CA  . VAL   Z  12 107 ? 62.252  -163.037 28.226  1.00 84.91  ? 107 VAL   Z CA  1 
ATOM   45024 C  C   . VAL   Z  12 107 ? 62.741  -162.762 26.808  1.00 85.95  ? 107 VAL   Z C   1 
ATOM   45025 O  O   . VAL   Z  12 107 ? 62.094  -163.207 25.842  1.00 83.93  ? 107 VAL   Z O   1 
ATOM   45026 C  CB  . VAL   Z  12 107 ? 62.891  -164.329 28.764  1.00 88.09  ? 107 VAL   Z CB  1 
ATOM   45027 C  CG1 . VAL   Z  12 107 ? 62.559  -164.546 30.231  1.00 91.15  ? 107 VAL   Z CG1 1 
ATOM   45028 C  CG2 . VAL   Z  12 107 ? 62.509  -165.542 27.929  1.00 89.58  ? 107 VAL   Z CG2 1 
ATOM   45029 N  N   . HIS   Z  12 108 ? 63.875  -162.070 26.732  1.00 90.85  ? 108 HIS   Z N   1 
ATOM   45030 C  CA  . HIS   Z  12 108 ? 64.699  -161.864 25.518  1.00 98.77  ? 108 HIS   Z CA  1 
ATOM   45031 C  C   . HIS   Z  12 108 ? 65.838  -162.879 25.574  1.00 98.89  ? 108 HIS   Z C   1 
ATOM   45032 O  O   . HIS   Z  12 108 ? 66.680  -162.755 26.489  1.00 102.71 ? 108 HIS   Z O   1 
ATOM   45033 C  CB  . HIS   Z  12 108 ? 65.239  -160.429 25.490  1.00 106.00 ? 108 HIS   Z CB  1 
ATOM   45034 C  CG  . HIS   Z  12 108 ? 64.858  -159.638 24.286  1.00 117.71 ? 108 HIS   Z CG  1 
ATOM   45035 N  ND1 . HIS   Z  12 108 ? 65.197  -158.306 24.165  1.00 124.93 ? 108 HIS   Z ND1 1 
ATOM   45036 C  CD2 . HIS   Z  12 108 ? 64.156  -159.959 23.177  1.00 119.07 ? 108 HIS   Z CD2 1 
ATOM   45037 C  CE1 . HIS   Z  12 108 ? 64.735  -157.841 23.023  1.00 129.64 ? 108 HIS   Z CE1 1 
ATOM   45038 N  NE2 . HIS   Z  12 108 ? 64.088  -158.836 22.397  1.00 130.62 ? 108 HIS   Z NE2 1 
ATOM   45039 N  N   . THR   Z  12 109 ? 65.852  -163.860 24.672  1.00 95.14  ? 109 THR   Z N   1 
ATOM   45040 C  CA  . THR   Z  12 109 ? 66.818  -164.983 24.728  1.00 90.15  ? 109 THR   Z CA  1 
ATOM   45041 C  C   . THR   Z  12 109 ? 67.936  -164.748 23.713  1.00 86.79  ? 109 THR   Z C   1 
ATOM   45042 O  O   . THR   Z  12 109 ? 67.622  -164.481 22.542  1.00 86.08  ? 109 THR   Z O   1 
ATOM   45043 C  CB  . THR   Z  12 109 ? 66.117  -166.327 24.530  1.00 91.28  ? 109 THR   Z CB  1 
ATOM   45044 O  OG1 . THR   Z  12 109 ? 64.865  -166.238 25.215  1.00 84.23  ? 109 THR   Z OG1 1 
ATOM   45045 C  CG2 . THR   Z  12 109 ? 66.957  -167.476 25.041  1.00 94.74  ? 109 THR   Z CG2 1 
ATOM   45046 N  N   . ILE   Z  12 110 ? 69.187  -164.816 24.173  1.00 86.80  ? 110 ILE   Z N   1 
ATOM   45047 C  CA  . ILE   Z  12 110 ? 70.409  -164.801 23.319  1.00 89.50  ? 110 ILE   Z CA  1 
ATOM   45048 C  C   . ILE   Z  12 110 ? 71.244  -166.028 23.684  1.00 89.99  ? 110 ILE   Z C   1 
ATOM   45049 O  O   . ILE   Z  12 110 ? 71.423  -166.272 24.894  1.00 88.23  ? 110 ILE   Z O   1 
ATOM   45050 C  CB  . ILE   Z  12 110 ? 71.212  -163.497 23.498  1.00 90.21  ? 110 ILE   Z CB  1 
ATOM   45051 C  CG1 . ILE   Z  12 110 ? 70.338  -162.253 23.318  1.00 92.55  ? 110 ILE   Z CG1 1 
ATOM   45052 C  CG2 . ILE   Z  12 110 ? 72.414  -163.484 22.564  1.00 90.93  ? 110 ILE   Z CG2 1 
ATOM   45053 C  CD1 . ILE   Z  12 110 ? 71.003  -160.959 23.738  1.00 95.07  ? 110 ILE   Z CD1 1 
ATOM   45054 N  N   . ILE   Z  12 111 ? 71.720  -166.767 22.676  1.00 91.81  ? 111 ILE   Z N   1 
ATOM   45055 C  CA  . ILE   Z  12 111 ? 72.707  -167.878 22.834  1.00 91.71  ? 111 ILE   Z CA  1 
ATOM   45056 C  C   . ILE   Z  12 111 ? 73.940  -167.550 21.990  1.00 92.38  ? 111 ILE   Z C   1 
ATOM   45057 O  O   . ILE   Z  12 111 ? 73.787  -166.899 20.934  1.00 93.63  ? 111 ILE   Z O   1 
ATOM   45058 C  CB  . ILE   Z  12 111 ? 72.107  -169.248 22.457  1.00 91.31  ? 111 ILE   Z CB  1 
ATOM   45059 C  CG1 . ILE   Z  12 111 ? 71.690  -169.311 20.985  1.00 94.05  ? 111 ILE   Z CG1 1 
ATOM   45060 C  CG2 . ILE   Z  12 111 ? 70.957  -169.599 23.385  1.00 89.43  ? 111 ILE   Z CG2 1 
ATOM   45061 C  CD1 . ILE   Z  12 111 ? 71.471  -170.710 20.463  1.00 94.95  ? 111 ILE   Z CD1 1 
ATOM   45062 N  N   . ALA   Z  12 112 ? 75.111  -167.988 22.452  1.00 91.50  ? 112 ALA   Z N   1 
ATOM   45063 C  CA  . ALA   Z  12 112 ? 76.409  -167.797 21.771  1.00 93.60  ? 112 ALA   Z CA  1 
ATOM   45064 C  C   . ALA   Z  12 112 ? 77.180  -169.120 21.769  1.00 93.58  ? 112 ALA   Z C   1 
ATOM   45065 O  O   . ALA   Z  12 112 ? 76.937  -169.968 22.653  1.00 91.78  ? 112 ALA   Z O   1 
ATOM   45066 C  CB  . ALA   Z  12 112 ? 77.189  -166.687 22.437  1.00 94.08  ? 112 ALA   Z CB  1 
ATOM   45067 N  N   . GLY   Z  12 113 ? 78.067  -169.279 20.788  1.00 93.08  ? 113 GLY   Z N   1 
ATOM   45068 C  CA  . GLY   Z  12 113 ? 78.921  -170.467 20.619  1.00 95.89  ? 113 GLY   Z CA  1 
ATOM   45069 C  C   . GLY   Z  12 113 ? 79.638  -170.431 19.285  1.00 98.59  ? 113 GLY   Z C   1 
ATOM   45070 O  O   . GLY   Z  12 113 ? 79.850  -169.322 18.758  1.00 98.98  ? 113 GLY   Z O   1 
ATOM   45071 N  N   . LEU   Z  12 114 ? 79.998  -171.602 18.757  1.00 100.40 ? 114 LEU   Z N   1 
ATOM   45072 C  CA  . LEU   Z  12 114 ? 80.671  -171.757 17.443  1.00 103.11 ? 114 LEU   Z CA  1 
ATOM   45073 C  C   . LEU   Z  12 114 ? 79.751  -172.554 16.514  1.00 105.70 ? 114 LEU   Z C   1 
ATOM   45074 O  O   . LEU   Z  12 114 ? 79.130  -173.528 16.988  1.00 107.23 ? 114 LEU   Z O   1 
ATOM   45075 C  CB  . LEU   Z  12 114 ? 82.014  -172.469 17.638  1.00 103.52 ? 114 LEU   Z CB  1 
ATOM   45076 C  CG  . LEU   Z  12 114 ? 82.959  -171.848 18.667  1.00 103.55 ? 114 LEU   Z CG  1 
ATOM   45077 C  CD1 . LEU   Z  12 114 ? 84.161  -172.746 18.907  1.00 103.58 ? 114 LEU   Z CD1 1 
ATOM   45078 C  CD2 . LEU   Z  12 114 ? 83.411  -170.462 18.232  1.00 105.01 ? 114 LEU   Z CD2 1 
ATOM   45079 N  N   . ASP   Z  12 115 ? 79.663  -172.145 15.245  1.00 108.04 ? 115 ASP   Z N   1 
ATOM   45080 C  CA  . ASP   Z  12 115 ? 78.953  -172.900 14.179  1.00 111.39 ? 115 ASP   Z CA  1 
ATOM   45081 C  C   . ASP   Z  12 115 ? 79.798  -174.132 13.840  1.00 111.35 ? 115 ASP   Z C   1 
ATOM   45082 O  O   . ASP   Z  12 115 ? 80.872  -174.297 14.451  1.00 110.34 ? 115 ASP   Z O   1 
ATOM   45083 C  CB  . ASP   Z  12 115 ? 78.655  -172.018 12.962  1.00 112.03 ? 115 ASP   Z CB  1 
ATOM   45084 C  CG  . ASP   Z  12 115 ? 79.874  -171.568 12.172  1.00 114.29 ? 115 ASP   Z CG  1 
ATOM   45085 O  OD1 . ASP   Z  12 115 ? 81.004  -171.914 12.570  1.00 118.07 ? 115 ASP   Z OD1 1 
ATOM   45086 O  OD2 . ASP   Z  12 115 ? 79.683  -170.872 11.156  1.00 116.72 ? 115 ASP   Z OD2 1 
ATOM   45087 N  N   . GLU   Z  12 116 ? 79.340  -174.954 12.895  1.00 115.84 ? 116 GLU   Z N   1 
ATOM   45088 C  CA  . GLU   Z  12 116 ? 79.985  -176.250 12.551  1.00 119.96 ? 116 GLU   Z CA  1 
ATOM   45089 C  C   . GLU   Z  12 116 ? 81.279  -176.015 11.755  1.00 118.03 ? 116 GLU   Z C   1 
ATOM   45090 O  O   . GLU   Z  12 116 ? 82.027  -176.995 11.580  1.00 121.36 ? 116 GLU   Z O   1 
ATOM   45091 C  CB  . GLU   Z  12 116 ? 78.991  -177.153 11.816  1.00 127.10 ? 116 GLU   Z CB  1 
ATOM   45092 C  CG  . GLU   Z  12 116 ? 78.061  -177.898 12.761  1.00 129.44 ? 116 GLU   Z CG  1 
ATOM   45093 C  CD  . GLU   Z  12 116 ? 76.776  -178.429 12.147  1.00 134.58 ? 116 GLU   Z CD  1 
ATOM   45094 O  OE1 . GLU   Z  12 116 ? 76.481  -179.627 12.337  1.00 135.84 ? 116 GLU   Z OE1 1 
ATOM   45095 O  OE2 . GLU   Z  12 116 ? 76.060  -177.640 11.499  1.00 144.53 ? 116 GLU   Z OE2 1 
ATOM   45096 N  N   . ASP   Z  12 117 ? 81.545  -174.779 11.310  1.00 119.68 ? 117 ASP   Z N   1 
ATOM   45097 C  CA  . ASP   Z  12 117 ? 82.799  -174.392 10.603  1.00 120.12 ? 117 ASP   Z CA  1 
ATOM   45098 C  C   . ASP   Z  12 117 ? 83.812  -173.795 11.590  1.00 119.55 ? 117 ASP   Z C   1 
ATOM   45099 O  O   . ASP   Z  12 117 ? 84.905  -173.406 11.132  1.00 120.19 ? 117 ASP   Z O   1 
ATOM   45100 C  CB  . ASP   Z  12 117 ? 82.514  -173.415 9.457   1.00 120.92 ? 117 ASP   Z CB  1 
ATOM   45101 C  CG  . ASP   Z  12 117 ? 81.791  -174.043 8.278   1.00 120.95 ? 117 ASP   Z CG  1 
ATOM   45102 O  OD1 . ASP   Z  12 117 ? 81.876  -175.274 8.127   1.00 125.18 ? 117 ASP   Z OD1 1 
ATOM   45103 O  OD2 . ASP   Z  12 117 ? 81.152  -173.296 7.516   1.00 120.46 ? 117 ASP   Z OD2 1 
ATOM   45104 N  N   . GLY   Z  12 118 ? 83.472  -173.727 12.884  1.00 121.12 ? 118 GLY   Z N   1 
ATOM   45105 C  CA  . GLY   Z  12 118 ? 84.375  -173.274 13.963  1.00 121.99 ? 118 GLY   Z CA  1 
ATOM   45106 C  C   . GLY   Z  12 118 ? 84.322  -171.772 14.195  1.00 121.92 ? 118 GLY   Z C   1 
ATOM   45107 O  O   . GLY   Z  12 118 ? 85.021  -171.305 15.117  1.00 118.64 ? 118 GLY   Z O   1 
ATOM   45108 N  N   . LYS   Z  12 119 ? 83.529  -171.037 13.404  1.00 122.64 ? 119 LYS   Z N   1 
ATOM   45109 C  CA  . LYS   Z  12 119 ? 83.419  -169.554 13.476  1.00 121.24 ? 119 LYS   Z CA  1 
ATOM   45110 C  C   . LYS   Z  12 119 ? 82.425  -169.154 14.573  1.00 119.92 ? 119 LYS   Z C   1 
ATOM   45111 O  O   . LYS   Z  12 119 ? 81.461  -169.910 14.804  1.00 118.99 ? 119 LYS   Z O   1 
ATOM   45112 C  CB  . LYS   Z  12 119 ? 83.003  -168.972 12.122  1.00 125.38 ? 119 LYS   Z CB  1 
ATOM   45113 C  CG  . LYS   Z  12 119 ? 84.088  -169.016 11.056  1.00 130.04 ? 119 LYS   Z CG  1 
ATOM   45114 C  CD  . LYS   Z  12 119 ? 83.782  -168.192 9.828   1.00 133.70 ? 119 LYS   Z CD  1 
ATOM   45115 C  CE  . LYS   Z  12 119 ? 84.963  -168.108 8.885   1.00 136.35 ? 119 LYS   Z CE  1 
ATOM   45116 N  NZ  . LYS   Z  12 119 ? 84.558  -168.333 7.478   1.00 138.08 ? 119 LYS   Z NZ  1 
ATOM   45117 N  N   . GLY   Z  12 120 ? 82.661  -168.000 15.210  1.00 116.21 ? 120 GLY   Z N   1 
ATOM   45118 C  CA  . GLY   Z  12 120 ? 81.821  -167.437 16.286  1.00 110.46 ? 120 GLY   Z CA  1 
ATOM   45119 C  C   . GLY   Z  12 120 ? 80.393  -167.192 15.826  1.00 105.12 ? 120 GLY   Z C   1 
ATOM   45120 O  O   . GLY   Z  12 120 ? 80.216  -166.707 14.690  1.00 104.22 ? 120 GLY   Z O   1 
ATOM   45121 N  N   . ALA   Z  12 121 ? 79.412  -167.502 16.680  1.00 98.80  ? 121 ALA   Z N   1 
ATOM   45122 C  CA  . ALA   Z  12 121 ? 77.964  -167.442 16.369  1.00 97.14  ? 121 ALA   Z CA  1 
ATOM   45123 C  C   . ALA   Z  12 121 ? 77.185  -166.855 17.548  1.00 95.10  ? 121 ALA   Z C   1 
ATOM   45124 O  O   . ALA   Z  12 121 ? 77.455  -167.244 18.696  1.00 91.88  ? 121 ALA   Z O   1 
ATOM   45125 C  CB  . ALA   Z  12 121 ? 77.456  -168.817 16.028  1.00 97.46  ? 121 ALA   Z CB  1 
ATOM   45126 N  N   . VAL   Z  12 122 ? 76.248  -165.954 17.248  1.00 98.95  ? 122 VAL   Z N   1 
ATOM   45127 C  CA  . VAL   Z  12 122 ? 75.277  -165.357 18.212  1.00 100.89 ? 122 VAL   Z CA  1 
ATOM   45128 C  C   . VAL   Z  12 122 ? 73.882  -165.449 17.583  1.00 99.40  ? 122 VAL   Z C   1 
ATOM   45129 O  O   . VAL   Z  12 122 ? 73.721  -164.980 16.438  1.00 104.59 ? 122 VAL   Z O   1 
ATOM   45130 C  CB  . VAL   Z  12 122 ? 75.658  -163.904 18.563  1.00 102.16 ? 122 VAL   Z CB  1 
ATOM   45131 C  CG1 . VAL   Z  12 122 ? 74.523  -163.158 19.251  1.00 103.01 ? 122 VAL   Z CG1 1 
ATOM   45132 C  CG2 . VAL   Z  12 122 ? 76.922  -163.842 19.407  1.00 103.69 ? 122 VAL   Z CG2 1 
ATOM   45133 N  N   . TYR   Z  12 123 ? 72.927  -166.051 18.296  1.00 97.43  ? 123 TYR   Z N   1 
ATOM   45134 C  CA  . TYR   Z  12 123 ? 71.499  -166.161 17.896  1.00 95.52  ? 123 TYR   Z CA  1 
ATOM   45135 C  C   . TYR   Z  12 123 ? 70.643  -165.419 18.923  1.00 92.07  ? 123 TYR   Z C   1 
ATOM   45136 O  O   . TYR   Z  12 123 ? 70.876  -165.612 20.131  1.00 90.10  ? 123 TYR   Z O   1 
ATOM   45137 C  CB  . TYR   Z  12 123 ? 71.061  -167.625 17.821  1.00 94.96  ? 123 TYR   Z CB  1 
ATOM   45138 C  CG  . TYR   Z  12 123 ? 71.532  -168.379 16.604  1.00 95.80  ? 123 TYR   Z CG  1 
ATOM   45139 C  CD1 . TYR   Z  12 123 ? 72.811  -168.910 16.539  1.00 96.71  ? 123 TYR   Z CD1 1 
ATOM   45140 C  CD2 . TYR   Z  12 123 ? 70.692  -168.581 15.521  1.00 94.81  ? 123 TYR   Z CD2 1 
ATOM   45141 C  CE1 . TYR   Z  12 123 ? 73.247  -169.607 15.424  1.00 96.55  ? 123 TYR   Z CE1 1 
ATOM   45142 C  CE2 . TYR   Z  12 123 ? 71.111  -169.279 14.399  1.00 93.61  ? 123 TYR   Z CE2 1 
ATOM   45143 C  CZ  . TYR   Z  12 123 ? 72.395  -169.792 14.349  1.00 95.88  ? 123 TYR   Z CZ  1 
ATOM   45144 O  OH  . TYR   Z  12 123 ? 72.813  -170.482 13.248  1.00 97.95  ? 123 TYR   Z OH  1 
ATOM   45145 N  N   . SER   Z  12 124 ? 69.684  -164.616 18.454  1.00 91.78  ? 124 SER   Z N   1 
ATOM   45146 C  CA  . SER   Z  12 124 ? 68.781  -163.796 19.304  1.00 93.63  ? 124 SER   Z CA  1 
ATOM   45147 C  C   . SER   Z  12 124 ? 67.319  -164.144 19.004  1.00 91.59  ? 124 SER   Z C   1 
ATOM   45148 O  O   . SER   Z  12 124 ? 66.979  -164.315 17.818  1.00 89.28  ? 124 SER   Z O   1 
ATOM   45149 C  CB  . SER   Z  12 124 ? 69.059  -162.322 19.133  1.00 95.41  ? 124 SER   Z CB  1 
ATOM   45150 O  OG  . SER   Z  12 124 ? 68.923  -161.922 17.778  1.00 100.51 ? 124 SER   Z OG  1 
ATOM   45151 N  N   . PHE   Z  12 125 ? 66.502  -164.248 20.057  1.00 89.76  ? 125 PHE   Z N   1 
ATOM   45152 C  CA  . PHE   Z  12 125 ? 65.072  -164.647 20.011  1.00 90.74  ? 125 PHE   Z CA  1 
ATOM   45153 C  C   . PHE   Z  12 125 ? 64.203  -163.565 20.646  1.00 91.95  ? 125 PHE   Z C   1 
ATOM   45154 O  O   . PHE   Z  12 125 ? 64.625  -162.980 21.662  1.00 96.65  ? 125 PHE   Z O   1 
ATOM   45155 C  CB  . PHE   Z  12 125 ? 64.830  -165.934 20.800  1.00 91.00  ? 125 PHE   Z CB  1 
ATOM   45156 C  CG  . PHE   Z  12 125 ? 65.740  -167.076 20.436  1.00 91.53  ? 125 PHE   Z CG  1 
ATOM   45157 C  CD1 . PHE   Z  12 125 ? 67.058  -167.097 20.866  1.00 92.66  ? 125 PHE   Z CD1 1 
ATOM   45158 C  CD2 . PHE   Z  12 125 ? 65.278  -168.132 19.670  1.00 90.68  ? 125 PHE   Z CD2 1 
ATOM   45159 C  CE1 . PHE   Z  12 125 ? 67.896  -168.145 20.528  1.00 93.60  ? 125 PHE   Z CE1 1 
ATOM   45160 C  CE2 . PHE   Z  12 125 ? 66.118  -169.180 19.330  1.00 91.37  ? 125 PHE   Z CE2 1 
ATOM   45161 C  CZ  . PHE   Z  12 125 ? 67.424  -169.185 19.762  1.00 93.25  ? 125 PHE   Z CZ  1 
ATOM   45162 N  N   . ASP   Z  12 126 ? 63.011  -163.349 20.087  1.00 90.67  ? 126 ASP   Z N   1 
ATOM   45163 C  CA  . ASP   Z  12 126 ? 61.934  -162.552 20.729  1.00 91.78  ? 126 ASP   Z CA  1 
ATOM   45164 C  C   . ASP   Z  12 126 ? 61.245  -163.464 21.745  1.00 87.65  ? 126 ASP   Z C   1 
ATOM   45165 O  O   . ASP   Z  12 126 ? 61.593  -164.639 21.866  1.00 83.78  ? 126 ASP   Z O   1 
ATOM   45166 C  CB  . ASP   Z  12 126 ? 61.016  -161.918 19.674  1.00 92.36  ? 126 ASP   Z CB  1 
ATOM   45167 C  CG  . ASP   Z  12 126 ? 59.983  -162.849 19.057  1.00 96.73  ? 126 ASP   Z CG  1 
ATOM   45168 O  OD1 . ASP   Z  12 126 ? 60.147  -164.080 19.184  1.00 102.52 ? 126 ASP   Z OD1 1 
ATOM   45169 O  OD2 . ASP   Z  12 126 ? 59.023  -162.332 18.442  1.00 90.28  ? 126 ASP   Z OD2 1 
ATOM   45170 N  N   . PRO   Z  12 127 ? 60.284  -162.948 22.543  1.00 88.52  ? 127 PRO   Z N   1 
ATOM   45171 C  CA  . PRO   Z  12 127 ? 59.595  -163.762 23.549  1.00 87.34  ? 127 PRO   Z CA  1 
ATOM   45172 C  C   . PRO   Z  12 127 ? 58.823  -164.985 23.021  1.00 85.97  ? 127 PRO   Z C   1 
ATOM   45173 O  O   . PRO   Z  12 127 ? 58.589  -165.889 23.807  1.00 80.96  ? 127 PRO   Z O   1 
ATOM   45174 C  CB  . PRO   Z  12 127 ? 58.615  -162.763 24.186  1.00 87.88  ? 127 PRO   Z CB  1 
ATOM   45175 C  CG  . PRO   Z  12 127 ? 59.284  -161.425 23.980  1.00 90.13  ? 127 PRO   Z CG  1 
ATOM   45176 C  CD  . PRO   Z  12 127 ? 59.879  -161.535 22.593  1.00 90.34  ? 127 PRO   Z CD  1 
ATOM   45177 N  N   . VAL   Z  12 128 ? 58.455  -165.001 21.735  1.00 84.33  ? 128 VAL   Z N   1 
ATOM   45178 C  CA  . VAL   Z  12 128 ? 57.597  -166.070 21.134  1.00 84.33  ? 128 VAL   Z CA  1 
ATOM   45179 C  C   . VAL   Z  12 128 ? 58.374  -166.879 20.082  1.00 84.89  ? 128 VAL   Z C   1 
ATOM   45180 O  O   . VAL   Z  12 128 ? 57.745  -167.726 19.422  1.00 85.11  ? 128 VAL   Z O   1 
ATOM   45181 C  CB  . VAL   Z  12 128 ? 56.283  -165.505 20.557  1.00 85.86  ? 128 VAL   Z CB  1 
ATOM   45182 C  CG1 . VAL   Z  12 128 ? 55.187  -165.469 21.610  1.00 83.51  ? 128 VAL   Z CG1 1 
ATOM   45183 C  CG2 . VAL   Z  12 128 ? 56.462  -164.135 19.920  1.00 87.07  ? 128 VAL   Z CG2 1 
ATOM   45184 N  N   . GLY   Z  12 129 ? 59.685  -166.659 19.938  1.00 85.75  ? 129 GLY   Z N   1 
ATOM   45185 C  CA  . GLY   Z  12 129 ? 60.592  -167.618 19.276  1.00 85.56  ? 129 GLY   Z CA  1 
ATOM   45186 C  C   . GLY   Z  12 129 ? 60.955  -167.242 17.851  1.00 86.63  ? 129 GLY   Z C   1 
ATOM   45187 O  O   . GLY   Z  12 129 ? 61.478  -168.119 17.140  1.00 87.38  ? 129 GLY   Z O   1 
ATOM   45188 N  N   . SER   Z  12 130 ? 60.717  -165.996 17.434  1.00 85.65  ? 130 SER   Z N   1 
ATOM   45189 C  CA  . SER   Z  12 130 ? 61.308  -165.434 16.194  1.00 87.51  ? 130 SER   Z CA  1 
ATOM   45190 C  C   . SER   Z  12 130 ? 62.815  -165.310 16.435  1.00 84.45  ? 130 SER   Z C   1 
ATOM   45191 O  O   . SER   Z  12 130 ? 63.184  -164.680 17.439  1.00 84.08  ? 130 SER   Z O   1 
ATOM   45192 C  CB  . SER   Z  12 130 ? 60.688  -164.109 15.827  1.00 88.36  ? 130 SER   Z CB  1 
ATOM   45193 O  OG  . SER   Z  12 130 ? 61.075  -163.711 14.520  1.00 92.64  ? 130 SER   Z OG  1 
ATOM   45194 N  N   . TYR   Z  12 131 ? 63.651  -165.937 15.603  1.00 85.07  ? 131 TYR   Z N   1 
ATOM   45195 C  CA  . TYR   Z  12 131 ? 65.123  -165.956 15.803  1.00 89.82  ? 131 TYR   Z CA  1 
ATOM   45196 C  C   . TYR   Z  12 131 ? 65.858  -165.653 14.497  1.00 90.68  ? 131 TYR   Z C   1 
ATOM   45197 O  O   . TYR   Z  12 131 ? 65.281  -165.776 13.403  1.00 94.23  ? 131 TYR   Z O   1 
ATOM   45198 C  CB  . TYR   Z  12 131 ? 65.578  -167.273 16.442  1.00 91.70  ? 131 TYR   Z CB  1 
ATOM   45199 C  CG  . TYR   Z  12 131 ? 65.697  -168.468 15.529  1.00 94.47  ? 131 TYR   Z CG  1 
ATOM   45200 C  CD1 . TYR   Z  12 131 ? 64.653  -169.367 15.390  1.00 94.64  ? 131 TYR   Z CD1 1 
ATOM   45201 C  CD2 . TYR   Z  12 131 ? 66.873  -168.733 14.843  1.00 98.12  ? 131 TYR   Z CD2 1 
ATOM   45202 C  CE1 . TYR   Z  12 131 ? 64.760  -170.481 14.572  1.00 97.77  ? 131 TYR   Z CE1 1 
ATOM   45203 C  CE2 . TYR   Z  12 131 ? 66.997  -169.841 14.018  1.00 99.86  ? 131 TYR   Z CE2 1 
ATOM   45204 C  CZ  . TYR   Z  12 131 ? 65.936  -170.721 13.882  1.00 99.63  ? 131 TYR   Z CZ  1 
ATOM   45205 O  OH  . TYR   Z  12 131 ? 66.050  -171.817 13.074  1.00 100.27 ? 131 TYR   Z OH  1 
ATOM   45206 N  N   . GLU   Z  12 132 ? 67.124  -165.274 14.654  1.00 92.46  ? 132 GLU   Z N   1 
ATOM   45207 C  CA  . GLU   Z  12 132 ? 68.002  -164.701 13.603  1.00 99.92  ? 132 GLU   Z CA  1 
ATOM   45208 C  C   . GLU   Z  12 132 ? 69.440  -164.809 14.117  1.00 102.65 ? 132 GLU   Z C   1 
ATOM   45209 O  O   . GLU   Z  12 132 ? 69.648  -164.557 15.321  1.00 99.57  ? 132 GLU   Z O   1 
ATOM   45210 C  CB  . GLU   Z  12 132 ? 67.592  -163.248 13.339  1.00 103.62 ? 132 GLU   Z CB  1 
ATOM   45211 C  CG  . GLU   Z  12 132 ? 68.383  -162.546 12.247  1.00 109.95 ? 132 GLU   Z CG  1 
ATOM   45212 C  CD  . GLU   Z  12 132 ? 68.259  -161.028 12.239  1.00 113.55 ? 132 GLU   Z CD  1 
ATOM   45213 O  OE1 . GLU   Z  12 132 ? 68.021  -160.433 13.316  1.00 114.46 ? 132 GLU   Z OE1 1 
ATOM   45214 O  OE2 . GLU   Z  12 132 ? 68.405  -160.438 11.154  1.00 117.86 ? 132 GLU   Z OE2 1 
ATOM   45215 N  N   . ARG   Z  12 133 ? 70.384  -165.195 13.258  1.00 106.06 ? 133 ARG   Z N   1 
ATOM   45216 C  CA  . ARG   Z  12 133 ? 71.831  -165.170 13.594  1.00 109.47 ? 133 ARG   Z CA  1 
ATOM   45217 C  C   . ARG   Z  12 133 ? 72.383  -163.777 13.267  1.00 114.06 ? 133 ARG   Z C   1 
ATOM   45218 O  O   . ARG   Z  12 133 ? 72.030  -163.237 12.199  1.00 114.94 ? 133 ARG   Z O   1 
ATOM   45219 C  CB  . ARG   Z  12 133 ? 72.601  -166.257 12.842  1.00 106.86 ? 133 ARG   Z CB  1 
ATOM   45220 C  CG  . ARG   Z  12 133 ? 74.019  -166.450 13.359  1.00 105.97 ? 133 ARG   Z CG  1 
ATOM   45221 C  CD  . ARG   Z  12 133 ? 74.837  -167.399 12.511  1.00 105.43 ? 133 ARG   Z CD  1 
ATOM   45222 N  NE  . ARG   Z  12 133 ? 76.232  -167.418 12.928  1.00 104.79 ? 133 ARG   Z NE  1 
ATOM   45223 C  CZ  . ARG   Z  12 133 ? 77.181  -168.168 12.378  1.00 105.13 ? 133 ARG   Z CZ  1 
ATOM   45224 N  NH1 . ARG   Z  12 133 ? 76.895  -168.985 11.378  1.00 105.80 ? 133 ARG   Z NH1 1 
ATOM   45225 N  NH2 . ARG   Z  12 133 ? 78.419  -168.102 12.836  1.00 107.09 ? 133 ARG   Z NH2 1 
ATOM   45226 N  N   . GLU   Z  12 134 ? 73.208  -163.223 14.162  1.00 118.85 ? 134 GLU   Z N   1 
ATOM   45227 C  CA  . GLU   Z  12 134 ? 73.849  -161.888 14.011  1.00 119.00 ? 134 GLU   Z CA  1 
ATOM   45228 C  C   . GLU   Z  12 134 ? 75.286  -161.939 14.542  1.00 120.42 ? 134 GLU   Z C   1 
ATOM   45229 O  O   . GLU   Z  12 134 ? 75.613  -162.886 15.288  1.00 121.55 ? 134 GLU   Z O   1 
ATOM   45230 C  CB  . GLU   Z  12 134 ? 73.051  -160.822 14.762  1.00 122.65 ? 134 GLU   Z CB  1 
ATOM   45231 C  CG  . GLU   Z  12 134 ? 71.711  -160.490 14.128  1.00 124.78 ? 134 GLU   Z CG  1 
ATOM   45232 C  CD  . GLU   Z  12 134 ? 70.756  -159.737 15.040  1.00 121.48 ? 134 GLU   Z CD  1 
ATOM   45233 O  OE1 . GLU   Z  12 134 ? 70.532  -158.537 14.796  1.00 129.00 ? 134 GLU   Z OE1 1 
ATOM   45234 O  OE2 . GLU   Z  12 134 ? 70.232  -160.354 15.989  1.00 117.86 ? 134 GLU   Z OE2 1 
ATOM   45235 N  N   . GLN   Z  12 135 ? 76.104  -160.952 14.162  1.00 116.63 ? 135 GLN   Z N   1 
ATOM   45236 C  CA  . GLN   Z  12 135 ? 77.453  -160.705 14.737  1.00 119.31 ? 135 GLN   Z CA  1 
ATOM   45237 C  C   . GLN   Z  12 135 ? 77.298  -160.112 16.141  1.00 114.19 ? 135 GLN   Z C   1 
ATOM   45238 O  O   . GLN   Z  12 135 ? 78.261  -160.199 16.928  1.00 117.38 ? 135 GLN   Z O   1 
ATOM   45239 C  CB  . GLN   Z  12 135 ? 78.249  -159.724 13.871  1.00 125.44 ? 135 GLN   Z CB  1 
ATOM   45240 C  CG  . GLN   Z  12 135 ? 78.909  -160.353 12.650  1.00 135.00 ? 135 GLN   Z CG  1 
ATOM   45241 C  CD  . GLN   Z  12 135 ? 80.075  -161.258 12.978  1.00 143.17 ? 135 GLN   Z CD  1 
ATOM   45242 O  OE1 . GLN   Z  12 135 ? 80.162  -162.384 12.491  1.00 151.77 ? 135 GLN   Z OE1 1 
ATOM   45243 N  NE2 . GLN   Z  12 135 ? 80.995  -160.774 13.798  1.00 148.73 ? 135 GLN   Z NE2 1 
ATOM   45244 N  N   . CYS   Z  12 136 ? 76.123  -159.548 16.438  1.00 108.59 ? 136 CYS   Z N   1 
ATOM   45245 C  CA  . CYS   Z  12 136 ? 75.937  -158.475 17.448  1.00 108.04 ? 136 CYS   Z CA  1 
ATOM   45246 C  C   . CYS   Z  12 136 ? 74.487  -158.409 17.937  1.00 98.48  ? 136 CYS   Z C   1 
ATOM   45247 O  O   . CYS   Z  12 136 ? 73.582  -158.277 17.090  1.00 94.58  ? 136 CYS   Z O   1 
ATOM   45248 C  CB  . CYS   Z  12 136 ? 76.291  -157.132 16.827  1.00 111.21 ? 136 CYS   Z CB  1 
ATOM   45249 S  SG  . CYS   Z  12 136 ? 77.337  -156.117 17.897  1.00 115.97 ? 136 CYS   Z SG  1 
ATOM   45250 N  N   . ARG   Z  12 137 ? 74.277  -158.451 19.253  1.00 95.15  ? 137 ARG   Z N   1 
ATOM   45251 C  CA  . ARG   Z  12 137 ? 72.940  -158.219 19.854  1.00 94.97  ? 137 ARG   Z CA  1 
ATOM   45252 C  C   . ARG   Z  12 137 ? 73.065  -157.903 21.345  1.00 95.44  ? 137 ARG   Z C   1 
ATOM   45253 O  O   . ARG   Z  12 137 ? 73.727  -158.669 22.069  1.00 98.29  ? 137 ARG   Z O   1 
ATOM   45254 C  CB  . ARG   Z  12 137 ? 72.022  -159.429 19.661  1.00 94.98  ? 137 ARG   Z CB  1 
ATOM   45255 C  CG  . ARG   Z  12 137 ? 70.638  -159.253 20.273  1.00 94.72  ? 137 ARG   Z CG  1 
ATOM   45256 C  CD  . ARG   Z  12 137 ? 69.901  -158.050 19.722  1.00 94.37  ? 137 ARG   Z CD  1 
ATOM   45257 N  NE  . ARG   Z  12 137 ? 69.425  -158.269 18.363  1.00 99.10  ? 137 ARG   Z NE  1 
ATOM   45258 C  CZ  . ARG   Z  12 137 ? 68.934  -157.323 17.567  1.00 101.77 ? 137 ARG   Z CZ  1 
ATOM   45259 N  NH1 . ARG   Z  12 137 ? 68.854  -156.067 17.976  1.00 100.76 ? 137 ARG   Z NH1 1 
ATOM   45260 N  NH2 . ARG   Z  12 137 ? 68.525  -157.636 16.350  1.00 108.36 ? 137 ARG   Z NH2 1 
ATOM   45261 N  N   . ALA   Z  12 138 ? 72.425  -156.811 21.761  1.00 94.59  ? 138 ALA   Z N   1 
ATOM   45262 C  CA  . ALA   Z  12 138 ? 72.128  -156.464 23.167  1.00 93.46  ? 138 ALA   Z CA  1 
ATOM   45263 C  C   . ALA   Z  12 138 ? 70.658  -156.786 23.436  1.00 90.60  ? 138 ALA   Z C   1 
ATOM   45264 O  O   . ALA   Z  12 138 ? 69.839  -156.610 22.518  1.00 91.12  ? 138 ALA   Z O   1 
ATOM   45265 C  CB  . ALA   Z  12 138 ? 72.429  -155.007 23.418  1.00 94.62  ? 138 ALA   Z CB  1 
ATOM   45266 N  N   . GLY   Z  12 139 ? 70.352  -157.256 24.644  1.00 90.40  ? 139 GLY   Z N   1 
ATOM   45267 C  CA  . GLY   Z  12 139 ? 68.984  -157.577 25.089  1.00 91.41  ? 139 GLY   Z CA  1 
ATOM   45268 C  C   . GLY   Z  12 139 ? 68.745  -157.086 26.502  1.00 92.58  ? 139 GLY   Z C   1 
ATOM   45269 O  O   . GLY   Z  12 139 ? 69.734  -156.934 27.248  1.00 94.71  ? 139 GLY   Z O   1 
ATOM   45270 N  N   . GLY   Z  12 140 ? 67.483  -156.835 26.854  1.00 93.41  ? 140 GLY   Z N   1 
ATOM   45271 C  CA  . GLY   Z  12 140 ? 67.081  -156.428 28.214  1.00 94.55  ? 140 GLY   Z CA  1 
ATOM   45272 C  C   . GLY   Z  12 140 ? 66.888  -154.926 28.339  1.00 92.96  ? 140 GLY   Z C   1 
ATOM   45273 O  O   . GLY   Z  12 140 ? 66.775  -154.248 27.300  1.00 90.56  ? 140 GLY   Z O   1 
ATOM   45274 N  N   . ALA   Z  12 141 ? 66.883  -154.431 29.580  1.00 94.26  ? 141 ALA   Z N   1 
ATOM   45275 C  CA  . ALA   Z  12 141 ? 66.438  -153.075 29.983  1.00 95.17  ? 141 ALA   Z CA  1 
ATOM   45276 C  C   . ALA   Z  12 141 ? 67.175  -151.983 29.193  1.00 93.70  ? 141 ALA   Z C   1 
ATOM   45277 O  O   . ALA   Z  12 141 ? 66.503  -151.034 28.741  1.00 96.65  ? 141 ALA   Z O   1 
ATOM   45278 C  CB  . ALA   Z  12 141 ? 66.634  -152.902 31.470  1.00 95.27  ? 141 ALA   Z CB  1 
ATOM   45279 N  N   . ALA   Z  12 142 ? 68.497  -152.104 29.038  1.00 94.27  ? 142 ALA   Z N   1 
ATOM   45280 C  CA  . ALA   Z  12 142 ? 69.379  -151.064 28.454  1.00 92.06  ? 142 ALA   Z CA  1 
ATOM   45281 C  C   . ALA   Z  12 142 ? 69.769  -151.417 27.013  1.00 92.04  ? 142 ALA   Z C   1 
ATOM   45282 O  O   . ALA   Z  12 142 ? 70.732  -150.809 26.509  1.00 90.46  ? 142 ALA   Z O   1 
ATOM   45283 C  CB  . ALA   Z  12 142 ? 70.601  -150.895 29.321  1.00 90.77  ? 142 ALA   Z CB  1 
ATOM   45284 N  N   . ALA   Z  12 143 ? 69.057  -152.351 26.370  1.00 94.12  ? 143 ALA   Z N   1 
ATOM   45285 C  CA  . ALA   Z  12 143 ? 69.299  -152.775 24.969  1.00 94.84  ? 143 ALA   Z CA  1 
ATOM   45286 C  C   . ALA   Z  12 143 ? 69.279  -151.544 24.053  1.00 92.26  ? 143 ALA   Z C   1 
ATOM   45287 O  O   . ALA   Z  12 143 ? 70.155  -151.436 23.174  1.00 84.01  ? 143 ALA   Z O   1 
ATOM   45288 C  CB  . ALA   Z  12 143 ? 68.277  -153.805 24.545  1.00 96.76  ? 143 ALA   Z CB  1 
ATOM   45289 N  N   . SER   Z  12 144 ? 68.333  -150.630 24.284  1.00 93.12  ? 144 SER   Z N   1 
ATOM   45290 C  CA  . SER   Z  12 144 ? 68.124  -149.407 23.467  1.00 94.08  ? 144 SER   Z CA  1 
ATOM   45291 C  C   . SER   Z  12 144 ? 69.318  -148.451 23.599  1.00 94.16  ? 144 SER   Z C   1 
ATOM   45292 O  O   . SER   Z  12 144 ? 69.547  -147.674 22.654  1.00 94.77  ? 144 SER   Z O   1 
ATOM   45293 C  CB  . SER   Z  12 144 ? 66.824  -148.729 23.819  1.00 93.62  ? 144 SER   Z CB  1 
ATOM   45294 O  OG  . SER   Z  12 144 ? 66.873  -148.189 25.132  1.00 94.27  ? 144 SER   Z OG  1 
ATOM   45295 N  N   . LEU   Z  12 145 ? 70.051  -148.504 24.718  1.00 93.25  ? 145 LEU   Z N   1 
ATOM   45296 C  CA  . LEU   Z  12 145 ? 71.265  -147.674 24.962  1.00 94.42  ? 145 LEU   Z CA  1 
ATOM   45297 C  C   . LEU   Z  12 145 ? 72.486  -148.298 24.272  1.00 95.11  ? 145 LEU   Z C   1 
ATOM   45298 O  O   . LEU   Z  12 145 ? 73.277  -147.545 23.679  1.00 92.63  ? 145 LEU   Z O   1 
ATOM   45299 C  CB  . LEU   Z  12 145 ? 71.520  -147.550 26.468  1.00 94.96  ? 145 LEU   Z CB  1 
ATOM   45300 C  CG  . LEU   Z  12 145 ? 70.655  -146.536 27.217  1.00 95.04  ? 145 LEU   Z CG  1 
ATOM   45301 C  CD1 . LEU   Z  12 145 ? 69.293  -147.123 27.559  1.00 97.37  ? 145 LEU   Z CD1 1 
ATOM   45302 C  CD2 . LEU   Z  12 145 ? 71.357  -146.063 28.479  1.00 94.13  ? 145 LEU   Z CD2 1 
ATOM   45303 N  N   . ILE   Z  12 146 ? 72.650  -149.619 24.372  1.00 97.60  ? 146 ILE   Z N   1 
ATOM   45304 C  CA  . ILE   Z  12 146 ? 73.908  -150.330 23.988  1.00 99.86  ? 146 ILE   Z CA  1 
ATOM   45305 C  C   . ILE   Z  12 146 ? 73.909  -150.604 22.478  1.00 98.19  ? 146 ILE   Z C   1 
ATOM   45306 O  O   . ILE   Z  12 146 ? 74.964  -150.398 21.853  1.00 95.73  ? 146 ILE   Z O   1 
ATOM   45307 C  CB  . ILE   Z  12 146 ? 74.095  -151.617 24.821  1.00 101.79 ? 146 ILE   Z CB  1 
ATOM   45308 C  CG1 . ILE   Z  12 146 ? 74.157  -151.308 26.321  1.00 105.44 ? 146 ILE   Z CG1 1 
ATOM   45309 C  CG2 . ILE   Z  12 146 ? 75.326  -152.383 24.354  1.00 100.63 ? 146 ILE   Z CG2 1 
ATOM   45310 C  CD1 . ILE   Z  12 146 ? 74.089  -152.524 27.220  1.00 106.60 ? 146 ILE   Z CD1 1 
ATOM   45311 N  N   . MET   Z  12 147 ? 72.780  -151.049 21.917  1.00 101.28 ? 147 MET   Z N   1 
ATOM   45312 C  CA  . MET   Z  12 147 ? 72.705  -151.601 20.535  1.00 102.38 ? 147 MET   Z CA  1 
ATOM   45313 C  C   . MET   Z  12 147 ? 73.191  -150.576 19.507  1.00 103.33 ? 147 MET   Z C   1 
ATOM   45314 O  O   . MET   Z  12 147 ? 73.957  -150.930 18.614  1.00 98.69  ? 147 MET   Z O   1 
ATOM   45315 C  CB  . MET   Z  12 147 ? 71.286  -152.065 20.182  1.00 103.32 ? 147 MET   Z CB  1 
ATOM   45316 C  CG  . MET   Z  12 147 ? 71.238  -152.980 18.968  1.00 101.70 ? 147 MET   Z CG  1 
ATOM   45317 S  SD  . MET   Z  12 147 ? 72.259  -154.467 19.159  1.00 101.79 ? 147 MET   Z SD  1 
ATOM   45318 C  CE  . MET   Z  12 147 ? 72.336  -155.030 17.458  1.00 105.37 ? 147 MET   Z CE  1 
ATOM   45319 N  N   . PRO   Z  12 148 ? 72.781  -149.286 19.563  1.00 104.31 ? 148 PRO   Z N   1 
ATOM   45320 C  CA  . PRO   Z  12 148 ? 73.254  -148.301 18.587  1.00 106.21 ? 148 PRO   Z CA  1 
ATOM   45321 C  C   . PRO   Z  12 148 ? 74.776  -148.088 18.611  1.00 108.13 ? 148 PRO   Z C   1 
ATOM   45322 O  O   . PRO   Z  12 148 ? 75.343  -147.808 17.568  1.00 111.48 ? 148 PRO   Z O   1 
ATOM   45323 C  CB  . PRO   Z  12 148 ? 72.530  -146.999 18.967  1.00 103.35 ? 148 PRO   Z CB  1 
ATOM   45324 C  CG  . PRO   Z  12 148 ? 72.075  -147.216 20.394  1.00 104.68 ? 148 PRO   Z CG  1 
ATOM   45325 C  CD  . PRO   Z  12 148 ? 71.820  -148.705 20.513  1.00 105.45 ? 148 PRO   Z CD  1 
ATOM   45326 N  N   . PHE   Z  12 149 ? 75.391  -148.217 19.791  1.00 106.72 ? 149 PHE   Z N   1 
ATOM   45327 C  CA  . PHE   Z  12 149 ? 76.862  -148.143 20.003  1.00 106.81 ? 149 PHE   Z CA  1 
ATOM   45328 C  C   . PHE   Z  12 149 ? 77.548  -149.323 19.302  1.00 106.03 ? 149 PHE   Z C   1 
ATOM   45329 O  O   . PHE   Z  12 149 ? 78.601  -149.112 18.665  1.00 102.80 ? 149 PHE   Z O   1 
ATOM   45330 C  CB  . PHE   Z  12 149 ? 77.183  -148.116 21.500  1.00 103.82 ? 149 PHE   Z CB  1 
ATOM   45331 C  CG  . PHE   Z  12 149 ? 78.648  -148.229 21.831  1.00 107.27 ? 149 PHE   Z CG  1 
ATOM   45332 C  CD1 . PHE   Z  12 149 ? 79.523  -147.197 21.533  1.00 107.86 ? 149 PHE   Z CD1 1 
ATOM   45333 C  CD2 . PHE   Z  12 149 ? 79.153  -149.368 22.440  1.00 107.86 ? 149 PHE   Z CD2 1 
ATOM   45334 C  CE1 . PHE   Z  12 149 ? 80.871  -147.301 21.839  1.00 112.47 ? 149 PHE   Z CE1 1 
ATOM   45335 C  CE2 . PHE   Z  12 149 ? 80.501  -149.473 22.743  1.00 109.83 ? 149 PHE   Z CE2 1 
ATOM   45336 C  CZ  . PHE   Z  12 149 ? 81.358  -148.439 22.442  1.00 111.60 ? 149 PHE   Z CZ  1 
ATOM   45337 N  N   . LEU   Z  12 150 ? 76.967  -150.523 19.431  1.00 108.67 ? 150 LEU   Z N   1 
ATOM   45338 C  CA  . LEU   Z  12 150 ? 77.457  -151.784 18.807  1.00 110.10 ? 150 LEU   Z CA  1 
ATOM   45339 C  C   . LEU   Z  12 150 ? 77.409  -151.652 17.281  1.00 109.57 ? 150 LEU   Z C   1 
ATOM   45340 O  O   . LEU   Z  12 150 ? 78.415  -152.006 16.638  1.00 111.24 ? 150 LEU   Z O   1 
ATOM   45341 C  CB  . LEU   Z  12 150 ? 76.598  -152.961 19.287  1.00 108.50 ? 150 LEU   Z CB  1 
ATOM   45342 C  CG  . LEU   Z  12 150 ? 77.143  -153.782 20.458  1.00 108.61 ? 150 LEU   Z CG  1 
ATOM   45343 C  CD1 . LEU   Z  12 150 ? 77.994  -152.957 21.416  1.00 107.25 ? 150 LEU   Z CD1 1 
ATOM   45344 C  CD2 . LEU   Z  12 150 ? 75.994  -154.442 21.202  1.00 111.99 ? 150 LEU   Z CD2 1 
ATOM   45345 N  N   . ASP   Z  12 151 ? 76.292  -151.161 16.729  1.00 111.56 ? 151 ASP   Z N   1 
ATOM   45346 C  CA  . ASP   Z  12 151 ? 76.129  -150.902 15.272  1.00 114.97 ? 151 ASP   Z CA  1 
ATOM   45347 C  C   . ASP   Z  12 151 ? 77.323  -150.082 14.776  1.00 117.41 ? 151 ASP   Z C   1 
ATOM   45348 O  O   . ASP   Z  12 151 ? 77.826  -150.371 13.675  1.00 124.56 ? 151 ASP   Z O   1 
ATOM   45349 C  CB  . ASP   Z  12 151 ? 74.841  -150.139 14.950  1.00 115.19 ? 151 ASP   Z CB  1 
ATOM   45350 C  CG  . ASP   Z  12 151 ? 73.568  -150.923 15.204  1.00 113.97 ? 151 ASP   Z CG  1 
ATOM   45351 O  OD1 . ASP   Z  12 151 ? 73.524  -152.113 14.832  1.00 118.38 ? 151 ASP   Z OD1 1 
ATOM   45352 O  OD2 . ASP   Z  12 151 ? 72.626  -150.334 15.767  1.00 112.68 ? 151 ASP   Z OD2 1 
ATOM   45353 N  N   . ASN   Z  12 152 ? 77.754  -149.104 15.575  1.00 114.18 ? 152 ASN   Z N   1 
ATOM   45354 C  CA  . ASN   Z  12 152 ? 78.794  -148.111 15.202  1.00 116.92 ? 152 ASN   Z CA  1 
ATOM   45355 C  C   . ASN   Z  12 152 ? 80.200  -148.710 15.339  1.00 121.21 ? 152 ASN   Z C   1 
ATOM   45356 O  O   . ASN   Z  12 152 ? 81.044  -148.389 14.482  1.00 123.23 ? 152 ASN   Z O   1 
ATOM   45357 C  CB  . ASN   Z  12 152 ? 78.667  -146.836 16.040  1.00 115.55 ? 152 ASN   Z CB  1 
ATOM   45358 C  CG  . ASN   Z  12 152 ? 79.575  -145.715 15.577  1.00 119.00 ? 152 ASN   Z CG  1 
ATOM   45359 O  OD1 . ASN   Z  12 152 ? 80.242  -145.078 16.390  1.00 117.30 ? 152 ASN   Z OD1 1 
ATOM   45360 N  ND2 . ASN   Z  12 152 ? 79.609  -145.455 14.278  1.00 120.61 ? 152 ASN   Z ND2 1 
ATOM   45361 N  N   . GLN   Z  12 153 ? 80.453  -149.525 16.370  1.00 124.39 ? 153 GLN   Z N   1 
ATOM   45362 C  CA  . GLN   Z  12 153 ? 81.827  -149.951 16.765  1.00 126.46 ? 153 GLN   Z CA  1 
ATOM   45363 C  C   . GLN   Z  12 153 ? 82.132  -151.391 16.322  1.00 129.61 ? 153 GLN   Z C   1 
ATOM   45364 O  O   . GLN   Z  12 153 ? 83.333  -151.699 16.168  1.00 132.13 ? 153 GLN   Z O   1 
ATOM   45365 C  CB  . GLN   Z  12 153 ? 82.013  -149.776 18.273  1.00 123.47 ? 153 GLN   Z CB  1 
ATOM   45366 C  CG  . GLN   Z  12 153 ? 81.986  -148.320 18.718  1.00 118.92 ? 153 GLN   Z CG  1 
ATOM   45367 C  CD  . GLN   Z  12 153 ? 83.076  -147.498 18.072  1.00 119.20 ? 153 GLN   Z CD  1 
ATOM   45368 O  OE1 . GLN   Z  12 153 ? 84.249  -147.861 18.100  1.00 121.48 ? 153 GLN   Z OE1 1 
ATOM   45369 N  NE2 . GLN   Z  12 153 ? 82.699  -146.376 17.481  1.00 117.54 ? 153 GLN   Z NE2 1 
ATOM   45370 N  N   . VAL   Z  12 154 ? 81.115  -152.238 16.126  1.00 131.87 ? 154 VAL   Z N   1 
ATOM   45371 C  CA  . VAL   Z  12 154 ? 81.297  -153.651 15.674  1.00 134.27 ? 154 VAL   Z CA  1 
ATOM   45372 C  C   . VAL   Z  12 154 ? 81.101  -153.699 14.152  1.00 135.04 ? 154 VAL   Z C   1 
ATOM   45373 O  O   . VAL   Z  12 154 ? 82.035  -154.153 13.462  1.00 137.60 ? 154 VAL   Z O   1 
ATOM   45374 C  CB  . VAL   Z  12 154 ? 80.365  -154.622 16.430  1.00 137.36 ? 154 VAL   Z CB  1 
ATOM   45375 C  CG1 . VAL   Z  12 154 ? 80.538  -156.066 15.971  1.00 140.54 ? 154 VAL   Z CG1 1 
ATOM   45376 C  CG2 . VAL   Z  12 154 ? 80.567  -154.528 17.937  1.00 134.50 ? 154 VAL   Z CG2 1 
ATOM   45377 N  N   . ASN   Z  12 155 ? 79.957  -153.215 13.650  1.00 135.79 ? 155 ASN   Z N   1 
ATOM   45378 C  CA  . ASN   Z  12 155 ? 79.554  -153.315 12.218  1.00 138.73 ? 155 ASN   Z CA  1 
ATOM   45379 C  C   . ASN   Z  12 155 ? 79.943  -152.038 11.451  1.00 138.41 ? 155 ASN   Z C   1 
ATOM   45380 O  O   . ASN   Z  12 155 ? 79.648  -151.979 10.239  1.00 140.74 ? 155 ASN   Z O   1 
ATOM   45381 C  CB  . ASN   Z  12 155 ? 78.059  -153.632 12.085  1.00 143.37 ? 155 ASN   Z CB  1 
ATOM   45382 C  CG  . ASN   Z  12 155 ? 77.691  -155.010 12.600  1.00 141.90 ? 155 ASN   Z CG  1 
ATOM   45383 O  OD1 . ASN   Z  12 155 ? 78.466  -155.956 12.473  1.00 143.73 ? 155 ASN   Z OD1 1 
ATOM   45384 N  ND2 . ASN   Z  12 155 ? 76.504  -155.141 13.172  1.00 143.28 ? 155 ASN   Z ND2 1 
ATOM   45385 N  N   . PHE   Z  12 156 ? 80.590  -151.071 12.117  1.00 135.14 ? 156 PHE   Z N   1 
ATOM   45386 C  CA  . PHE   Z  12 156 ? 81.132  -149.808 11.536  1.00 133.70 ? 156 PHE   Z CA  1 
ATOM   45387 C  C   . PHE   Z  12 156 ? 80.069  -149.068 10.713  1.00 130.20 ? 156 PHE   Z C   1 
ATOM   45388 O  O   . PHE   Z  12 156 ? 80.408  -148.557 9.625   1.00 127.98 ? 156 PHE   Z O   1 
ATOM   45389 C  CB  . PHE   Z  12 156 ? 82.367  -150.094 10.678  1.00 140.92 ? 156 PHE   Z CB  1 
ATOM   45390 C  CG  . PHE   Z  12 156 ? 83.462  -150.841 11.395  1.00 148.20 ? 156 PHE   Z CG  1 
ATOM   45391 C  CD1 . PHE   Z  12 156 ? 83.909  -150.420 12.638  1.00 147.73 ? 156 PHE   Z CD1 1 
ATOM   45392 C  CD2 . PHE   Z  12 156 ? 84.049  -151.962 10.826  1.00 154.50 ? 156 PHE   Z CD2 1 
ATOM   45393 C  CE1 . PHE   Z  12 156 ? 84.914  -151.109 13.301  1.00 150.45 ? 156 PHE   Z CE1 1 
ATOM   45394 C  CE2 . PHE   Z  12 156 ? 85.057  -152.646 11.488  1.00 156.15 ? 156 PHE   Z CE2 1 
ATOM   45395 C  CZ  . PHE   Z  12 156 ? 85.488  -152.219 12.724  1.00 154.19 ? 156 PHE   Z CZ  1 
ATOM   45396 N  N   . LYS   Z  12 157 ? 78.839  -148.986 11.230  1.00 127.41 ? 157 LYS   Z N   1 
ATOM   45397 C  CA  . LYS   Z  12 157 ? 77.700  -148.281 10.580  1.00 127.27 ? 157 LYS   Z CA  1 
ATOM   45398 C  C   . LYS   Z  12 157 ? 77.955  -146.767 10.644  1.00 125.12 ? 157 LYS   Z C   1 
ATOM   45399 O  O   . LYS   Z  12 157 ? 78.510  -146.304 11.660  1.00 125.86 ? 157 LYS   Z O   1 
ATOM   45400 C  CB  . LYS   Z  12 157 ? 76.376  -148.677 11.247  1.00 127.77 ? 157 LYS   Z CB  1 
ATOM   45401 C  CG  . LYS   Z  12 157 ? 75.974  -150.140 11.083  1.00 129.05 ? 157 LYS   Z CG  1 
ATOM   45402 C  CD  . LYS   Z  12 157 ? 75.441  -150.488 9.704   1.00 129.02 ? 157 LYS   Z CD  1 
ATOM   45403 C  CE  . LYS   Z  12 157 ? 75.024  -151.938 9.566   1.00 133.97 ? 157 LYS   Z CE  1 
ATOM   45404 N  NZ  . LYS   Z  12 157 ? 73.779  -152.234 10.315  1.00 137.27 ? 157 LYS   Z NZ  1 
ATOM   45405 N  N   . ASN   Z  12 158 ? 77.607  -146.042 9.572   1.00 123.35 ? 158 ASN   Z N   1 
ATOM   45406 C  CA  . ASN   Z  12 158 ? 77.696  -144.558 9.445   1.00 122.99 ? 158 ASN   Z CA  1 
ATOM   45407 C  C   . ASN   Z  12 158 ? 79.159  -144.089 9.398   1.00 121.67 ? 158 ASN   Z C   1 
ATOM   45408 O  O   . ASN   Z  12 158 ? 79.368  -142.866 9.320   1.00 121.96 ? 158 ASN   Z O   1 
ATOM   45409 C  CB  . ASN   Z  12 158 ? 76.952  -143.828 10.571  1.00 121.37 ? 158 ASN   Z CB  1 
ATOM   45410 C  CG  . ASN   Z  12 158 ? 75.445  -143.919 10.464  1.00 120.26 ? 158 ASN   Z CG  1 
ATOM   45411 O  OD1 . ASN   Z  12 158 ? 74.793  -144.474 11.346  1.00 120.66 ? 158 ASN   Z OD1 1 
ATOM   45412 N  ND2 . ASN   Z  12 158 ? 74.883  -143.373 9.397   1.00 120.18 ? 158 ASN   Z ND2 1 
ATOM   45413 N  N   . GLN   Z  12 159 ? 80.131  -145.007 9.420   1.00 125.56 ? 159 GLN   Z N   1 
ATOM   45414 C  CA  . GLN   Z  12 159 ? 81.583  -144.683 9.408   1.00 130.46 ? 159 GLN   Z CA  1 
ATOM   45415 C  C   . GLN   Z  12 159 ? 82.121  -144.839 7.982   1.00 134.13 ? 159 GLN   Z C   1 
ATOM   45416 O  O   . GLN   Z  12 159 ? 82.127  -145.980 7.480   1.00 142.26 ? 159 GLN   Z O   1 
ATOM   45417 C  CB  . GLN   Z  12 159 ? 82.350  -145.592 10.372  1.00 134.25 ? 159 GLN   Z CB  1 
ATOM   45418 C  CG  . GLN   Z  12 159 ? 82.095  -145.278 11.840  1.00 131.89 ? 159 GLN   Z CG  1 
ATOM   45419 C  CD  . GLN   Z  12 159 ? 83.203  -145.756 12.749  1.00 132.66 ? 159 GLN   Z CD  1 
ATOM   45420 O  OE1 . GLN   Z  12 159 ? 83.003  -146.621 13.599  1.00 135.43 ? 159 GLN   Z OE1 1 
ATOM   45421 N  NE2 . GLN   Z  12 159 ? 84.390  -145.196 12.578  1.00 129.82 ? 159 GLN   Z NE2 1 
ATOM   45422 N  N   . TYR   Z  12 160 ? 82.558  -143.737 7.364   1.00 131.46 ? 160 TYR   Z N   1 
ATOM   45423 C  CA  . TYR   Z  12 160 ? 83.119  -143.704 5.987   1.00 135.96 ? 160 TYR   Z CA  1 
ATOM   45424 C  C   . TYR   Z  12 160 ? 84.632  -143.475 6.037   1.00 139.18 ? 160 TYR   Z C   1 
ATOM   45425 O  O   . TYR   Z  12 160 ? 85.123  -142.833 6.989   1.00 127.12 ? 160 TYR   Z O   1 
ATOM   45426 C  CB  . TYR   Z  12 160 ? 82.441  -142.622 5.149   1.00 135.21 ? 160 TYR   Z CB  1 
ATOM   45427 C  CG  . TYR   Z  12 160 ? 81.018  -142.942 4.773   1.00 137.13 ? 160 TYR   Z CG  1 
ATOM   45428 C  CD1 . TYR   Z  12 160 ? 79.959  -142.505 5.552   1.00 134.85 ? 160 TYR   Z CD1 1 
ATOM   45429 C  CD2 . TYR   Z  12 160 ? 80.729  -143.700 3.650   1.00 140.14 ? 160 TYR   Z CD2 1 
ATOM   45430 C  CE1 . TYR   Z  12 160 ? 78.647  -142.797 5.216   1.00 134.99 ? 160 TYR   Z CE1 1 
ATOM   45431 C  CE2 . TYR   Z  12 160 ? 79.422  -144.004 3.301   1.00 141.09 ? 160 TYR   Z CE2 1 
ATOM   45432 C  CZ  . TYR   Z  12 160 ? 78.378  -143.549 4.087   1.00 136.51 ? 160 TYR   Z CZ  1 
ATOM   45433 O  OH  . TYR   Z  12 160 ? 77.085  -143.835 3.761   1.00 138.55 ? 160 TYR   Z OH  1 
ATOM   45434 N  N   . GLU   Z  12 161 ? 85.333  -143.982 5.016   1.00 149.12 ? 161 GLU   Z N   1 
ATOM   45435 C  CA  . GLU   Z  12 161 ? 86.805  -143.851 4.842   1.00 156.51 ? 161 GLU   Z CA  1 
ATOM   45436 C  C   . GLU   Z  12 161 ? 87.130  -142.366 4.680   1.00 155.20 ? 161 GLU   Z C   1 
ATOM   45437 O  O   . GLU   Z  12 161 ? 86.627  -141.725 3.761   1.00 164.55 ? 161 GLU   Z O   1 
ATOM   45438 C  CB  . GLU   Z  12 161 ? 87.276  -144.673 3.637   1.00 162.43 ? 161 GLU   Z CB  1 
ATOM   45439 C  CG  . GLU   Z  12 161 ? 88.687  -145.221 3.778   1.00 169.03 ? 161 GLU   Z CG  1 
ATOM   45440 C  CD  . GLU   Z  12 161 ? 88.788  -146.574 4.464   1.00 173.11 ? 161 GLU   Z CD  1 
ATOM   45441 O  OE1 . GLU   Z  12 161 ? 87.931  -147.441 4.196   1.00 178.80 ? 161 GLU   Z OE1 1 
ATOM   45442 O  OE2 . GLU   Z  12 161 ? 89.726  -146.760 5.264   1.00 180.89 ? 161 GLU   Z OE2 1 
ATOM   45443 N  N   . PRO   Z  12 162 ? 87.940  -141.759 5.580   1.00 149.19 ? 162 PRO   Z N   1 
ATOM   45444 C  CA  . PRO   Z  12 162 ? 88.260  -140.331 5.496   1.00 143.97 ? 162 PRO   Z CA  1 
ATOM   45445 C  C   . PRO   Z  12 162 ? 88.805  -139.888 4.129   1.00 144.63 ? 162 PRO   Z C   1 
ATOM   45446 O  O   . PRO   Z  12 162 ? 89.683  -140.549 3.609   1.00 144.55 ? 162 PRO   Z O   1 
ATOM   45447 C  CB  . PRO   Z  12 162 ? 89.346  -140.145 6.566   1.00 142.30 ? 162 PRO   Z CB  1 
ATOM   45448 C  CG  . PRO   Z  12 162 ? 89.064  -141.238 7.571   1.00 143.34 ? 162 PRO   Z CG  1 
ATOM   45449 C  CD  . PRO   Z  12 162 ? 88.567  -142.406 6.745   1.00 146.16 ? 162 PRO   Z CD  1 
ATOM   45450 N  N   . GLY   Z  12 163 ? 88.265  -138.790 3.586   1.00 144.95 ? 163 GLY   Z N   1 
ATOM   45451 C  CA  . GLY   Z  12 163 ? 88.725  -138.160 2.333   1.00 149.86 ? 163 GLY   Z CA  1 
ATOM   45452 C  C   . GLY   Z  12 163 ? 88.063  -138.732 1.087   1.00 151.96 ? 163 GLY   Z C   1 
ATOM   45453 O  O   . GLY   Z  12 163 ? 88.324  -138.184 -0.001  1.00 151.27 ? 163 GLY   Z O   1 
ATOM   45454 N  N   . THR   Z  12 164 ? 87.233  -139.776 1.218   1.00 155.53 ? 164 THR   Z N   1 
ATOM   45455 C  CA  . THR   Z  12 164 ? 86.607  -140.503 0.076   1.00 163.91 ? 164 THR   Z CA  1 
ATOM   45456 C  C   . THR   Z  12 164 ? 85.272  -139.855 -0.321  1.00 163.13 ? 164 THR   Z C   1 
ATOM   45457 O  O   . THR   Z  12 164 ? 84.632  -140.386 -1.246  1.00 167.35 ? 164 THR   Z O   1 
ATOM   45458 C  CB  . THR   Z  12 164 ? 86.416  -141.997 0.377   1.00 166.86 ? 164 THR   Z CB  1 
ATOM   45459 O  OG1 . THR   Z  12 164 ? 85.546  -142.142 1.500   1.00 173.30 ? 164 THR   Z OG1 1 
ATOM   45460 C  CG2 . THR   Z  12 164 ? 87.724  -142.712 0.639   1.00 168.86 ? 164 THR   Z CG2 1 
ATOM   45461 N  N   . ASN   Z  12 165 ? 84.871  -138.759 0.334   1.00 160.31 ? 165 ASN   Z N   1 
ATOM   45462 C  CA  . ASN   Z  12 165 ? 83.655  -137.975 -0.014  1.00 161.31 ? 165 ASN   Z CA  1 
ATOM   45463 C  C   . ASN   Z  12 165 ? 82.403  -138.726 0.462   1.00 158.13 ? 165 ASN   Z C   1 
ATOM   45464 O  O   . ASN   Z  12 165 ? 81.323  -138.499 -0.119  1.00 158.39 ? 165 ASN   Z O   1 
ATOM   45465 C  CB  . ASN   Z  12 165 ? 83.602  -137.689 -1.520  1.00 165.07 ? 165 ASN   Z CB  1 
ATOM   45466 C  CG  . ASN   Z  12 165 ? 82.578  -136.650 -1.928  1.00 168.42 ? 165 ASN   Z CG  1 
ATOM   45467 O  OD1 . ASN   Z  12 165 ? 81.974  -136.768 -2.991  1.00 176.16 ? 165 ASN   Z OD1 1 
ATOM   45468 N  ND2 . ASN   Z  12 165 ? 82.375  -135.628 -1.110  1.00 168.72 ? 165 ASN   Z ND2 1 
ATOM   45469 N  N   . GLY   Z  12 166 ? 82.539  -139.575 1.487   1.00 154.27 ? 166 GLY   Z N   1 
ATOM   45470 C  CA  . GLY   Z  12 166 ? 81.454  -140.435 2.000   1.00 155.31 ? 166 GLY   Z CA  1 
ATOM   45471 C  C   . GLY   Z  12 166 ? 80.972  -141.413 0.942   1.00 157.47 ? 166 GLY   Z C   1 
ATOM   45472 O  O   . GLY   Z  12 166 ? 79.753  -141.663 0.885   1.00 162.96 ? 166 GLY   Z O   1 
ATOM   45473 N  N   . LYS   Z  12 167 ? 81.899  -141.938 0.132   1.00 156.95 ? 167 LYS   Z N   1 
ATOM   45474 C  CA  . LYS   Z  12 167 ? 81.618  -142.823 -1.034  1.00 156.07 ? 167 LYS   Z CA  1 
ATOM   45475 C  C   . LYS   Z  12 167 ? 82.107  -144.250 -0.747  1.00 158.36 ? 167 LYS   Z C   1 
ATOM   45476 O  O   . LYS   Z  12 167 ? 81.494  -145.196 -1.283  1.00 157.67 ? 167 LYS   Z O   1 
ATOM   45477 C  CB  . LYS   Z  12 167 ? 82.299  -142.265 -2.287  1.00 157.09 ? 167 LYS   Z CB  1 
ATOM   45478 C  CG  . LYS   Z  12 167 ? 81.435  -142.215 -3.541  1.00 153.82 ? 167 LYS   Z CG  1 
ATOM   45479 C  CD  . LYS   Z  12 167 ? 80.853  -140.844 -3.827  1.00 152.19 ? 167 LYS   Z CD  1 
ATOM   45480 C  CE  . LYS   Z  12 167 ? 79.630  -140.516 -2.995  1.00 148.45 ? 167 LYS   Z CE  1 
ATOM   45481 N  NZ  . LYS   Z  12 167 ? 78.610  -139.798 -3.795  1.00 149.09 ? 167 LYS   Z NZ  1 
ATOM   45482 N  N   . VAL   Z  12 168 ? 83.178  -144.393 0.042   1.00 156.53 ? 168 VAL   Z N   1 
ATOM   45483 C  CA  . VAL   Z  12 168 ? 83.768  -145.701 0.453   1.00 153.81 ? 168 VAL   Z CA  1 
ATOM   45484 C  C   . VAL   Z  12 168 ? 83.488  -145.907 1.945   1.00 147.15 ? 168 VAL   Z C   1 
ATOM   45485 O  O   . VAL   Z  12 168 ? 83.972  -145.092 2.755   1.00 140.92 ? 168 VAL   Z O   1 
ATOM   45486 C  CB  . VAL   Z  12 168 ? 85.277  -145.756 0.145   1.00 160.58 ? 168 VAL   Z CB  1 
ATOM   45487 C  CG1 . VAL   Z  12 168 ? 85.937  -147.003 0.720   1.00 162.24 ? 168 VAL   Z CG1 1 
ATOM   45488 C  CG2 . VAL   Z  12 168 ? 85.542  -145.654 -1.349  1.00 163.06 ? 168 VAL   Z CG2 1 
ATOM   45489 N  N   . LYS   Z  12 169 ? 82.742  -146.963 2.282   1.00 149.33 ? 169 LYS   Z N   1 
ATOM   45490 C  CA  . LYS   Z  12 169 ? 82.427  -147.358 3.680   1.00 150.51 ? 169 LYS   Z CA  1 
ATOM   45491 C  C   . LYS   Z  12 169 ? 83.715  -147.854 4.349   1.00 149.05 ? 169 LYS   Z C   1 
ATOM   45492 O  O   . LYS   Z  12 169 ? 84.607  -148.352 3.630   1.00 150.75 ? 169 LYS   Z O   1 
ATOM   45493 C  CB  . LYS   Z  12 169 ? 81.345  -148.444 3.708   1.00 152.46 ? 169 LYS   Z CB  1 
ATOM   45494 C  CG  . LYS   Z  12 169 ? 80.015  -148.061 3.070   1.00 151.90 ? 169 LYS   Z CG  1 
ATOM   45495 C  CD  . LYS   Z  12 169 ? 79.021  -149.201 3.011   1.00 152.40 ? 169 LYS   Z CD  1 
ATOM   45496 C  CE  . LYS   Z  12 169 ? 78.311  -149.435 4.328   1.00 149.57 ? 169 LYS   Z CE  1 
ATOM   45497 N  NZ  . LYS   Z  12 169 ? 77.247  -150.459 4.208   1.00 150.47 ? 169 LYS   Z NZ  1 
ATOM   45498 N  N   . LYS   Z  12 170 ? 83.812  -147.704 5.671   1.00 145.59 ? 170 LYS   Z N   1 
ATOM   45499 C  CA  . LYS   Z  12 170 ? 84.834  -148.386 6.506   1.00 149.05 ? 170 LYS   Z CA  1 
ATOM   45500 C  C   . LYS   Z  12 170 ? 84.628  -149.891 6.347   1.00 148.58 ? 170 LYS   Z C   1 
ATOM   45501 O  O   . LYS   Z  12 170 ? 83.517  -150.380 6.547   1.00 154.81 ? 170 LYS   Z O   1 
ATOM   45502 C  CB  . LYS   Z  12 170 ? 84.698  -147.950 7.967   1.00 146.09 ? 170 LYS   Z CB  1 
ATOM   45503 C  CG  . LYS   Z  12 170 ? 85.796  -148.439 8.901   1.00 147.79 ? 170 LYS   Z CG  1 
ATOM   45504 C  CD  . LYS   Z  12 170 ? 85.713  -147.823 10.283  1.00 145.65 ? 170 LYS   Z CD  1 
ATOM   45505 C  CE  . LYS   Z  12 170 ? 87.014  -147.886 11.055  1.00 145.76 ? 170 LYS   Z CE  1 
ATOM   45506 N  NZ  . LYS   Z  12 170 ? 86.988  -148.941 12.095  1.00 145.79 ? 170 LYS   Z NZ  1 
ATOM   45507 N  N   . PRO   Z  12 171 ? 85.665  -150.671 5.964   1.00 147.21 ? 171 PRO   Z N   1 
ATOM   45508 C  CA  . PRO   Z  12 171 ? 85.485  -152.096 5.684   1.00 148.89 ? 171 PRO   Z CA  1 
ATOM   45509 C  C   . PRO   Z  12 171 ? 85.216  -152.927 6.948   1.00 150.48 ? 171 PRO   Z C   1 
ATOM   45510 O  O   . PRO   Z  12 171 ? 85.819  -152.647 7.971   1.00 150.44 ? 171 PRO   Z O   1 
ATOM   45511 C  CB  . PRO   Z  12 171 ? 86.820  -152.511 5.048   1.00 149.04 ? 171 PRO   Z CB  1 
ATOM   45512 C  CG  . PRO   Z  12 171 ? 87.822  -151.533 5.625   1.00 146.36 ? 171 PRO   Z CG  1 
ATOM   45513 C  CD  . PRO   Z  12 171 ? 87.058  -150.235 5.785   1.00 146.69 ? 171 PRO   Z CD  1 
ATOM   45514 N  N   . LEU   Z  12 172 ? 84.331  -153.924 6.837   1.00 157.89 ? 172 LEU   Z N   1 
ATOM   45515 C  CA  . LEU   Z  12 172 ? 84.022  -154.890 7.925   1.00 159.21 ? 172 LEU   Z CA  1 
ATOM   45516 C  C   . LEU   Z  12 172 ? 85.284  -155.715 8.195   1.00 158.47 ? 172 LEU   Z C   1 
ATOM   45517 O  O   . LEU   Z  12 172 ? 85.964  -156.085 7.216   1.00 158.05 ? 172 LEU   Z O   1 
ATOM   45518 C  CB  . LEU   Z  12 172 ? 82.855  -155.799 7.511   1.00 161.06 ? 172 LEU   Z CB  1 
ATOM   45519 C  CG  . LEU   Z  12 172 ? 81.534  -155.108 7.164   1.00 159.53 ? 172 LEU   Z CG  1 
ATOM   45520 C  CD1 . LEU   Z  12 172 ? 80.510  -156.121 6.671   1.00 157.96 ? 172 LEU   Z CD1 1 
ATOM   45521 C  CD2 . LEU   Z  12 172 ? 80.984  -154.335 8.354   1.00 156.15 ? 172 LEU   Z CD2 1 
ATOM   45522 N  N   . LYS   Z  12 173 ? 85.600  -155.968 9.468   1.00 155.05 ? 173 LYS   Z N   1 
ATOM   45523 C  CA  . LYS   Z  12 173 ? 86.679  -156.909 9.870   1.00 153.12 ? 173 LYS   Z CA  1 
ATOM   45524 C  C   . LYS   Z  12 173 ? 86.372  -157.484 11.257  1.00 152.86 ? 173 LYS   Z C   1 
ATOM   45525 O  O   . LYS   Z  12 173 ? 85.816  -156.745 12.100  1.00 144.97 ? 173 LYS   Z O   1 
ATOM   45526 C  CB  . LYS   Z  12 173 ? 88.051  -156.227 9.827   1.00 150.60 ? 173 LYS   Z CB  1 
ATOM   45527 C  CG  . LYS   Z  12 173 ? 88.293  -155.134 10.858  1.00 148.09 ? 173 LYS   Z CG  1 
ATOM   45528 C  CD  . LYS   Z  12 173 ? 89.763  -154.935 11.155  1.00 148.94 ? 173 LYS   Z CD  1 
ATOM   45529 C  CE  . LYS   Z  12 173 ? 90.032  -153.817 12.139  1.00 148.34 ? 173 LYS   Z CE  1 
ATOM   45530 N  NZ  . LYS   Z  12 173 ? 89.836  -152.485 11.520  1.00 149.86 ? 173 LYS   Z NZ  1 
ATOM   45531 N  N   . TYR   Z  12 174 ? 86.714  -158.761 11.461  1.00 159.61 ? 174 TYR   Z N   1 
ATOM   45532 C  CA  . TYR   Z  12 174 ? 86.605  -159.481 12.757  1.00 153.75 ? 174 TYR   Z CA  1 
ATOM   45533 C  C   . TYR   Z  12 174 ? 87.447  -158.744 13.805  1.00 141.90 ? 174 TYR   Z C   1 
ATOM   45534 O  O   . TYR   Z  12 174 ? 88.567  -158.290 13.482  1.00 129.67 ? 174 TYR   Z O   1 
ATOM   45535 C  CB  . TYR   Z  12 174 ? 87.058  -160.939 12.623  1.00 161.26 ? 174 TYR   Z CB  1 
ATOM   45536 C  CG  . TYR   Z  12 174 ? 86.089  -161.856 11.917  1.00 170.37 ? 174 TYR   Z CG  1 
ATOM   45537 C  CD1 . TYR   Z  12 174 ? 84.854  -162.159 12.471  1.00 175.02 ? 174 TYR   Z CD1 1 
ATOM   45538 C  CD2 . TYR   Z  12 174 ? 86.418  -162.453 10.709  1.00 175.04 ? 174 TYR   Z CD2 1 
ATOM   45539 C  CE1 . TYR   Z  12 174 ? 83.964  -163.010 11.835  1.00 176.90 ? 174 TYR   Z CE1 1 
ATOM   45540 C  CE2 . TYR   Z  12 174 ? 85.540  -163.308 10.061  1.00 177.10 ? 174 TYR   Z CE2 1 
ATOM   45541 C  CZ  . TYR   Z  12 174 ? 84.308  -163.589 10.626  1.00 176.93 ? 174 TYR   Z CZ  1 
ATOM   45542 O  OH  . TYR   Z  12 174 ? 83.439  -164.430 9.993   1.00 172.07 ? 174 TYR   Z OH  1 
ATOM   45543 N  N   . LEU   Z  12 175 ? 86.908  -158.621 15.020  1.00 134.90 ? 175 LEU   Z N   1 
ATOM   45544 C  CA  . LEU   Z  12 175 ? 87.600  -158.006 16.181  1.00 128.87 ? 175 LEU   Z CA  1 
ATOM   45545 C  C   . LEU   Z  12 175 ? 88.278  -159.114 16.991  1.00 124.29 ? 175 LEU   Z C   1 
ATOM   45546 O  O   . LEU   Z  12 175 ? 87.709  -160.221 17.071  1.00 123.73 ? 175 LEU   Z O   1 
ATOM   45547 C  CB  . LEU   Z  12 175 ? 86.584  -157.240 17.035  1.00 129.94 ? 175 LEU   Z CB  1 
ATOM   45548 C  CG  . LEU   Z  12 175 ? 86.112  -155.907 16.456  1.00 130.80 ? 175 LEU   Z CG  1 
ATOM   45549 C  CD1 . LEU   Z  12 175 ? 84.946  -156.104 15.498  1.00 133.14 ? 175 LEU   Z CD1 1 
ATOM   45550 C  CD2 . LEU   Z  12 175 ? 85.724  -154.944 17.567  1.00 130.69 ? 175 LEU   Z CD2 1 
ATOM   45551 N  N   . SER   Z  12 176 ? 89.451  -158.823 17.558  1.00 118.55 ? 176 SER   Z N   1 
ATOM   45552 C  CA  . SER   Z  12 176 ? 90.164  -159.702 18.520  1.00 118.04 ? 176 SER   Z CA  1 
ATOM   45553 C  C   . SER   Z  12 176 ? 89.362  -159.747 19.824  1.00 113.54 ? 176 SER   Z C   1 
ATOM   45554 O  O   . SER   Z  12 176 ? 88.588  -158.803 20.069  1.00 110.84 ? 176 SER   Z O   1 
ATOM   45555 C  CB  . SER   Z  12 176 ? 91.574  -159.231 18.752  1.00 119.15 ? 176 SER   Z CB  1 
ATOM   45556 O  OG  . SER   Z  12 176 ? 91.589  -157.927 19.313  1.00 121.85 ? 176 SER   Z OG  1 
ATOM   45557 N  N   . VAL   Z  12 177 ? 89.534  -160.806 20.620  1.00 115.03 ? 177 VAL   Z N   1 
ATOM   45558 C  CA  . VAL   Z  12 177 ? 88.805  -161.006 21.909  1.00 113.65 ? 177 VAL   Z CA  1 
ATOM   45559 C  C   . VAL   Z  12 177 ? 89.126  -159.845 22.863  1.00 115.76 ? 177 VAL   Z C   1 
ATOM   45560 O  O   . VAL   Z  12 177 ? 88.230  -159.470 23.644  1.00 114.79 ? 177 VAL   Z O   1 
ATOM   45561 C  CB  . VAL   Z  12 177 ? 89.124  -162.376 22.541  1.00 113.20 ? 177 VAL   Z CB  1 
ATOM   45562 C  CG1 . VAL   Z  12 177 ? 90.572  -162.477 23.004  1.00 114.21 ? 177 VAL   Z CG1 1 
ATOM   45563 C  CG2 . VAL   Z  12 177 ? 88.170  -162.696 23.682  1.00 109.80 ? 177 VAL   Z CG2 1 
ATOM   45564 N  N   . GLU   Z  12 178 ? 90.346  -159.299 22.795  1.00 118.96 ? 178 GLU   Z N   1 
ATOM   45565 C  CA  . GLU   Z  12 178 ? 90.790  -158.133 23.606  1.00 122.35 ? 178 GLU   Z CA  1 
ATOM   45566 C  C   . GLU   Z  12 178 ? 89.924  -156.918 23.248  1.00 119.78 ? 178 GLU   Z C   1 
ATOM   45567 O  O   . GLU   Z  12 178 ? 89.380  -156.290 24.178  1.00 114.88 ? 178 GLU   Z O   1 
ATOM   45568 C  CB  . GLU   Z  12 178 ? 92.276  -157.838 23.377  1.00 128.94 ? 178 GLU   Z CB  1 
ATOM   45569 C  CG  . GLU   Z  12 178 ? 93.210  -158.868 23.995  1.00 132.58 ? 178 GLU   Z CG  1 
ATOM   45570 C  CD  . GLU   Z  12 178 ? 93.411  -160.150 23.200  1.00 136.09 ? 178 GLU   Z CD  1 
ATOM   45571 O  OE1 . GLU   Z  12 178 ? 93.913  -161.134 23.783  1.00 136.97 ? 178 GLU   Z OE1 1 
ATOM   45572 O  OE2 . GLU   Z  12 178 ? 93.066  -160.166 22.000  1.00 140.55 ? 178 GLU   Z OE2 1 
ATOM   45573 N  N   . GLU   Z  12 179 ? 89.794  -156.623 21.949  1.00 121.18 ? 179 GLU   Z N   1 
ATOM   45574 C  CA  . GLU   Z  12 179 ? 88.997  -155.486 21.407  1.00 122.19 ? 179 GLU   Z CA  1 
ATOM   45575 C  C   . GLU   Z  12 179 ? 87.520  -155.651 21.789  1.00 119.53 ? 179 GLU   Z C   1 
ATOM   45576 O  O   . GLU   Z  12 179 ? 86.891  -154.639 22.146  1.00 118.88 ? 179 GLU   Z O   1 
ATOM   45577 C  CB  . GLU   Z  12 179 ? 89.141  -155.376 19.885  1.00 127.40 ? 179 GLU   Z CB  1 
ATOM   45578 C  CG  . GLU   Z  12 179 ? 90.169  -154.351 19.432  1.00 136.05 ? 179 GLU   Z CG  1 
ATOM   45579 C  CD  . GLU   Z  12 179 ? 89.899  -152.922 19.883  1.00 139.59 ? 179 GLU   Z CD  1 
ATOM   45580 O  OE1 . GLU   Z  12 179 ? 90.778  -152.334 20.548  1.00 146.80 ? 179 GLU   Z OE1 1 
ATOM   45581 O  OE2 . GLU   Z  12 179 ? 88.813  -152.395 19.564  1.00 147.78 ? 179 GLU   Z OE2 1 
ATOM   45582 N  N   . VAL   Z  12 180 ? 86.985  -156.871 21.697  1.00 115.99 ? 180 VAL   Z N   1 
ATOM   45583 C  CA  . VAL   Z  12 180 ? 85.547  -157.172 21.967  1.00 114.15 ? 180 VAL   Z CA  1 
ATOM   45584 C  C   . VAL   Z  12 180 ? 85.246  -156.913 23.449  1.00 112.25 ? 180 VAL   Z C   1 
ATOM   45585 O  O   . VAL   Z  12 180 ? 84.200  -156.303 23.725  1.00 110.40 ? 180 VAL   Z O   1 
ATOM   45586 C  CB  . VAL   Z  12 180 ? 85.178  -158.607 21.545  1.00 113.69 ? 180 VAL   Z CB  1 
ATOM   45587 C  CG1 . VAL   Z  12 180 ? 83.846  -159.054 22.131  1.00 112.47 ? 180 VAL   Z CG1 1 
ATOM   45588 C  CG2 . VAL   Z  12 180 ? 85.166  -158.752 20.032  1.00 115.08 ? 180 VAL   Z CG2 1 
ATOM   45589 N  N   . ILE   Z  12 181 ? 86.122  -157.357 24.359  1.00 114.85 ? 181 ILE   Z N   1 
ATOM   45590 C  CA  . ILE   Z  12 181 ? 85.920  -157.239 25.837  1.00 113.63 ? 181 ILE   Z CA  1 
ATOM   45591 C  C   . ILE   Z  12 181 ? 85.989  -155.758 26.242  1.00 111.17 ? 181 ILE   Z C   1 
ATOM   45592 O  O   . ILE   Z  12 181 ? 85.265  -155.382 27.187  1.00 104.91 ? 181 ILE   Z O   1 
ATOM   45593 C  CB  . ILE   Z  12 181 ? 86.911  -158.133 26.616  1.00 115.90 ? 181 ILE   Z CB  1 
ATOM   45594 C  CG1 . ILE   Z  12 181 ? 86.531  -159.611 26.471  1.00 118.29 ? 181 ILE   Z CG1 1 
ATOM   45595 C  CG2 . ILE   Z  12 181 ? 87.002  -157.712 28.078  1.00 116.16 ? 181 ILE   Z CG2 1 
ATOM   45596 C  CD1 . ILE   Z  12 181 ? 87.345  -160.568 27.317  1.00 120.41 ? 181 ILE   Z CD1 1 
ATOM   45597 N  N   . LYS   Z  12 182 ? 86.799  -154.947 25.550  1.00 113.78 ? 182 LYS   Z N   1 
ATOM   45598 C  CA  . LYS   Z  12 182 ? 86.863  -153.471 25.751  1.00 114.05 ? 182 LYS   Z CA  1 
ATOM   45599 C  C   . LYS   Z  12 182 ? 85.485  -152.858 25.465  1.00 109.81 ? 182 LYS   Z C   1 
ATOM   45600 O  O   . LYS   Z  12 182 ? 85.020  -152.051 26.294  1.00 100.25 ? 182 LYS   Z O   1 
ATOM   45601 C  CB  . LYS   Z  12 182 ? 87.927  -152.824 24.856  1.00 118.64 ? 182 LYS   Z CB  1 
ATOM   45602 C  CG  . LYS   Z  12 182 ? 89.368  -152.993 25.317  1.00 121.42 ? 182 LYS   Z CG  1 
ATOM   45603 C  CD  . LYS   Z  12 182 ? 90.359  -152.278 24.423  1.00 126.81 ? 182 LYS   Z CD  1 
ATOM   45604 C  CE  . LYS   Z  12 182 ? 91.804  -152.562 24.777  1.00 130.06 ? 182 LYS   Z CE  1 
ATOM   45605 N  NZ  . LYS   Z  12 182 ? 92.725  -152.078 23.722  1.00 133.52 ? 182 LYS   Z NZ  1 
ATOM   45606 N  N   . LEU   Z  12 183 ? 84.864  -153.234 24.339  1.00 109.27 ? 183 LEU   Z N   1 
ATOM   45607 C  CA  . LEU   Z  12 183 ? 83.528  -152.738 23.901  1.00 108.75 ? 183 LEU   Z CA  1 
ATOM   45608 C  C   . LEU   Z  12 183 ? 82.458  -153.172 24.910  1.00 105.17 ? 183 LEU   Z C   1 
ATOM   45609 O  O   . LEU   Z  12 183 ? 81.602  -152.337 25.246  1.00 104.46 ? 183 LEU   Z O   1 
ATOM   45610 C  CB  . LEU   Z  12 183 ? 83.193  -153.277 22.506  1.00 114.00 ? 183 LEU   Z CB  1 
ATOM   45611 C  CG  . LEU   Z  12 183 ? 84.071  -152.779 21.357  1.00 119.82 ? 183 LEU   Z CG  1 
ATOM   45612 C  CD1 . LEU   Z  12 183 ? 83.738  -153.523 20.072  1.00 120.13 ? 183 LEU   Z CD1 1 
ATOM   45613 C  CD2 . LEU   Z  12 183 ? 83.925  -151.276 21.155  1.00 121.18 ? 183 LEU   Z CD2 1 
ATOM   45614 N  N   . VAL   Z  12 184 ? 82.495  -154.432 25.352  1.00 102.56 ? 184 VAL   Z N   1 
ATOM   45615 C  CA  . VAL   Z  12 184 ? 81.548  -154.992 26.362  1.00 100.07 ? 184 VAL   Z CA  1 
ATOM   45616 C  C   . VAL   Z  12 184 ? 81.632  -154.142 27.636  1.00 100.96 ? 184 VAL   Z C   1 
ATOM   45617 O  O   . VAL   Z  12 184 ? 80.569  -153.723 28.132  1.00 97.41  ? 184 VAL   Z O   1 
ATOM   45618 C  CB  . VAL   Z  12 184 ? 81.830  -156.480 26.653  1.00 98.19  ? 184 VAL   Z CB  1 
ATOM   45619 C  CG1 . VAL   Z  12 184 ? 81.098  -156.967 27.895  1.00 97.45  ? 184 VAL   Z CG1 1 
ATOM   45620 C  CG2 . VAL   Z  12 184 ? 81.491  -157.364 25.462  1.00 96.93  ? 184 VAL   Z CG2 1 
ATOM   45621 N  N   . ARG   Z  12 185 ? 82.849  -153.893 28.133  1.00 102.98 ? 185 ARG   Z N   1 
ATOM   45622 C  CA  . ARG   Z  12 185 ? 83.100  -153.175 29.414  1.00 103.77 ? 185 ARG   Z CA  1 
ATOM   45623 C  C   . ARG   Z  12 185 ? 82.647  -151.712 29.299  1.00 103.40 ? 185 ARG   Z C   1 
ATOM   45624 O  O   . ARG   Z  12 185 ? 82.030  -151.214 30.260  1.00 98.06  ? 185 ARG   Z O   1 
ATOM   45625 C  CB  . ARG   Z  12 185 ? 84.575  -153.280 29.815  1.00 106.77 ? 185 ARG   Z CB  1 
ATOM   45626 C  CG  . ARG   Z  12 185 ? 84.975  -154.653 30.339  1.00 106.06 ? 185 ARG   Z CG  1 
ATOM   45627 C  CD  . ARG   Z  12 185 ? 86.346  -154.654 30.985  1.00 108.46 ? 185 ARG   Z CD  1 
ATOM   45628 N  NE  . ARG   Z  12 185 ? 86.361  -153.861 32.205  1.00 110.83 ? 185 ARG   Z NE  1 
ATOM   45629 C  CZ  . ARG   Z  12 185 ? 87.427  -153.665 32.976  1.00 115.91 ? 185 ARG   Z CZ  1 
ATOM   45630 N  NH1 . ARG   Z  12 185 ? 88.592  -154.210 32.665  1.00 118.14 ? 185 ARG   Z NH1 1 
ATOM   45631 N  NH2 . ARG   Z  12 185 ? 87.321  -152.919 34.063  1.00 119.56 ? 185 ARG   Z NH2 1 
ATOM   45632 N  N   . ASP   Z  12 186 ? 82.937  -151.052 28.174  1.00 104.66 ? 186 ASP   Z N   1 
ATOM   45633 C  CA  . ASP   Z  12 186 ? 82.531  -149.643 27.913  1.00 107.71 ? 186 ASP   Z CA  1 
ATOM   45634 C  C   . ASP   Z  12 186 ? 81.010  -149.574 27.701  1.00 109.08 ? 186 ASP   Z C   1 
ATOM   45635 O  O   . ASP   Z  12 186 ? 80.407  -148.573 28.144  1.00 114.06 ? 186 ASP   Z O   1 
ATOM   45636 C  CB  . ASP   Z  12 186 ? 83.307  -149.037 26.737  1.00 107.17 ? 186 ASP   Z CB  1 
ATOM   45637 C  CG  . ASP   Z  12 186 ? 84.726  -148.608 27.086  1.00 104.64 ? 186 ASP   Z CG  1 
ATOM   45638 O  OD1 . ASP   Z  12 186 ? 84.972  -148.286 28.264  1.00 104.09 ? 186 ASP   Z OD1 1 
ATOM   45639 O  OD2 . ASP   Z  12 186 ? 85.577  -148.596 26.178  1.00 104.00 ? 186 ASP   Z OD2 1 
ATOM   45640 N  N   . SER   Z  12 187 ? 80.418  -150.585 27.053  1.00 105.62 ? 187 SER   Z N   1 
ATOM   45641 C  CA  . SER   Z  12 187 ? 78.955  -150.699 26.796  1.00 102.53 ? 187 SER   Z CA  1 
ATOM   45642 C  C   . SER   Z  12 187 ? 78.183  -150.725 28.119  1.00 98.55  ? 187 SER   Z C   1 
ATOM   45643 O  O   . SER   Z  12 187 ? 77.131  -150.068 28.198  1.00 93.67  ? 187 SER   Z O   1 
ATOM   45644 C  CB  . SER   Z  12 187 ? 78.625  -151.918 25.972  1.00 103.04 ? 187 SER   Z CB  1 
ATOM   45645 O  OG  . SER   Z  12 187 ? 79.044  -151.753 24.627  1.00 108.73 ? 187 SER   Z OG  1 
ATOM   45646 N  N   . PHE   Z  12 188 ? 78.683  -151.472 29.107  1.00 101.48 ? 188 PHE   Z N   1 
ATOM   45647 C  CA  . PHE   Z  12 188 ? 77.997  -151.728 30.402  1.00 101.61 ? 188 PHE   Z CA  1 
ATOM   45648 C  C   . PHE   Z  12 188 ? 78.206  -150.549 31.362  1.00 100.97 ? 188 PHE   Z C   1 
ATOM   45649 O  O   . PHE   Z  12 188 ? 77.248  -150.202 32.084  1.00 100.54 ? 188 PHE   Z O   1 
ATOM   45650 C  CB  . PHE   Z  12 188 ? 78.442  -153.071 30.991  1.00 100.53 ? 188 PHE   Z CB  1 
ATOM   45651 C  CG  . PHE   Z  12 188 ? 77.552  -154.220 30.594  1.00 98.37  ? 188 PHE   Z CG  1 
ATOM   45652 C  CD1 . PHE   Z  12 188 ? 77.838  -154.991 29.478  1.00 100.56 ? 188 PHE   Z CD1 1 
ATOM   45653 C  CD2 . PHE   Z  12 188 ? 76.407  -154.507 31.320  1.00 97.59  ? 188 PHE   Z CD2 1 
ATOM   45654 C  CE1 . PHE   Z  12 188 ? 77.010  -156.040 29.112  1.00 100.73 ? 188 PHE   Z CE1 1 
ATOM   45655 C  CE2 . PHE   Z  12 188 ? 75.580  -155.557 30.951  1.00 99.21  ? 188 PHE   Z CE2 1 
ATOM   45656 C  CZ  . PHE   Z  12 188 ? 75.884  -156.322 29.849  1.00 101.36 ? 188 PHE   Z CZ  1 
ATOM   45657 N  N   . THR   Z  12 189 ? 79.398  -149.943 31.374  1.00 101.07 ? 189 THR   Z N   1 
ATOM   45658 C  CA  . THR   Z  12 189 ? 79.710  -148.768 32.231  1.00 103.65 ? 189 THR   Z CA  1 
ATOM   45659 C  C   . THR   Z  12 189 ? 78.895  -147.566 31.747  1.00 104.05 ? 189 THR   Z C   1 
ATOM   45660 O  O   . THR   Z  12 189 ? 78.465  -146.780 32.607  1.00 109.69 ? 189 THR   Z O   1 
ATOM   45661 C  CB  . THR   Z  12 189 ? 81.211  -148.457 32.269  1.00 104.65 ? 189 THR   Z CB  1 
ATOM   45662 O  OG1 . THR   Z  12 189 ? 81.710  -148.455 30.932  1.00 106.69 ? 189 THR   Z OG1 1 
ATOM   45663 C  CG2 . THR   Z  12 189 ? 81.987  -149.446 33.109  1.00 103.81 ? 189 THR   Z CG2 1 
ATOM   45664 N  N   . SER   Z  12 190 ? 78.688  -147.444 30.431  1.00 102.73 ? 190 SER   Z N   1 
ATOM   45665 C  CA  . SER   Z  12 190 ? 77.815  -146.420 29.795  1.00 103.45 ? 190 SER   Z CA  1 
ATOM   45666 C  C   . SER   Z  12 190 ? 76.354  -146.660 30.201  1.00 99.76  ? 190 SER   Z C   1 
ATOM   45667 O  O   . SER   Z  12 190 ? 75.695  -145.704 30.649  1.00 98.56  ? 190 SER   Z O   1 
ATOM   45668 C  CB  . SER   Z  12 190 ? 77.972  -146.423 28.292  1.00 102.96 ? 190 SER   Z CB  1 
ATOM   45669 O  OG  . SER   Z  12 190 ? 79.271  -145.986 27.917  1.00 103.76 ? 190 SER   Z OG  1 
ATOM   45670 N  N   . ALA   Z  12 191 ? 75.875  -147.895 30.041  1.00 98.72  ? 191 ALA   Z N   1 
ATOM   45671 C  CA  . ALA   Z  12 191 ? 74.508  -148.336 30.405  1.00 96.71  ? 191 ALA   Z CA  1 
ATOM   45672 C  C   . ALA   Z  12 191 ? 74.258  -148.070 31.894  1.00 94.92  ? 191 ALA   Z C   1 
ATOM   45673 O  O   . ALA   Z  12 191 ? 73.166  -147.565 32.220  1.00 89.81  ? 191 ALA   Z O   1 
ATOM   45674 C  CB  . ALA   Z  12 191 ? 74.330  -149.797 30.063  1.00 97.60  ? 191 ALA   Z CB  1 
ATOM   45675 N  N   . THR   Z  12 192 ? 75.235  -148.395 32.751  1.00 95.53  ? 192 THR   Z N   1 
ATOM   45676 C  CA  . THR   Z  12 192 ? 75.158  -148.279 34.235  1.00 97.77  ? 192 THR   Z CA  1 
ATOM   45677 C  C   . THR   Z  12 192 ? 74.937  -146.817 34.640  1.00 98.89  ? 192 THR   Z C   1 
ATOM   45678 O  O   . THR   Z  12 192 ? 74.185  -146.581 35.611  1.00 96.97  ? 192 THR   Z O   1 
ATOM   45679 C  CB  . THR   Z  12 192 ? 76.418  -148.838 34.909  1.00 98.41  ? 192 THR   Z CB  1 
ATOM   45680 O  OG1 . THR   Z  12 192 ? 76.538  -150.212 34.545  1.00 97.18  ? 192 THR   Z OG1 1 
ATOM   45681 C  CG2 . THR   Z  12 192 ? 76.385  -148.715 36.417  1.00 99.00  ? 192 THR   Z CG2 1 
ATOM   45682 N  N   . GLU   Z  12 193 ? 75.580  -145.882 33.933  1.00 104.31 ? 193 GLU   Z N   1 
ATOM   45683 C  CA  . GLU   Z  12 193 ? 75.510  -144.421 34.209  1.00 105.63 ? 193 GLU   Z CA  1 
ATOM   45684 C  C   . GLU   Z  12 193 ? 74.074  -143.914 34.036  1.00 101.65 ? 193 GLU   Z C   1 
ATOM   45685 O  O   . GLU   Z  12 193 ? 73.649  -143.089 34.867  1.00 101.07 ? 193 GLU   Z O   1 
ATOM   45686 C  CB  . GLU   Z  12 193 ? 76.438  -143.635 33.279  1.00 112.15 ? 193 GLU   Z CB  1 
ATOM   45687 C  CG  . GLU   Z  12 193 ? 77.910  -143.771 33.620  1.00 118.89 ? 193 GLU   Z CG  1 
ATOM   45688 C  CD  . GLU   Z  12 193 ? 78.331  -143.087 34.910  1.00 125.83 ? 193 GLU   Z CD  1 
ATOM   45689 O  OE1 . GLU   Z  12 193 ? 78.817  -143.792 35.816  1.00 134.31 ? 193 GLU   Z OE1 1 
ATOM   45690 O  OE2 . GLU   Z  12 193 ? 78.185  -141.851 35.003  1.00 127.76 ? 193 GLU   Z OE2 1 
ATOM   45691 N  N   . ARG   Z  12 194 ? 73.366  -144.375 32.999  1.00 99.43  ? 194 ARG   Z N   1 
ATOM   45692 C  CA  . ARG   Z  12 194 ? 72.106  -143.743 32.521  1.00 99.17  ? 194 ARG   Z CA  1 
ATOM   45693 C  C   . ARG   Z  12 194 ? 70.888  -144.659 32.699  1.00 96.17  ? 194 ARG   Z C   1 
ATOM   45694 O  O   . ARG   Z  12 194 ? 69.778  -144.170 32.428  1.00 98.61  ? 194 ARG   Z O   1 
ATOM   45695 C  CB  . ARG   Z  12 194 ? 72.262  -143.318 31.058  1.00 100.91 ? 194 ARG   Z CB  1 
ATOM   45696 C  CG  . ARG   Z  12 194 ? 73.236  -142.166 30.860  1.00 104.33 ? 194 ARG   Z CG  1 
ATOM   45697 C  CD  . ARG   Z  12 194 ? 72.710  -140.877 31.464  1.00 105.94 ? 194 ARG   Z CD  1 
ATOM   45698 N  NE  . ARG   Z  12 194 ? 73.587  -139.744 31.211  1.00 107.70 ? 194 ARG   Z NE  1 
ATOM   45699 C  CZ  . ARG   Z  12 194 ? 73.310  -138.486 31.535  1.00 108.85 ? 194 ARG   Z CZ  1 
ATOM   45700 N  NH1 . ARG   Z  12 194 ? 72.169  -138.179 32.131  1.00 108.71 ? 194 ARG   Z NH1 1 
ATOM   45701 N  NH2 . ARG   Z  12 194 ? 74.180  -137.531 31.253  1.00 112.17 ? 194 ARG   Z NH2 1 
ATOM   45702 N  N   . HIS   Z  12 195 ? 71.063  -145.909 33.141  1.00 96.49  ? 195 HIS   Z N   1 
ATOM   45703 C  CA  . HIS   Z  12 195 ? 69.944  -146.838 33.457  1.00 93.61  ? 195 HIS   Z CA  1 
ATOM   45704 C  C   . HIS   Z  12 195 ? 70.059  -147.286 34.919  1.00 94.37  ? 195 HIS   Z C   1 
ATOM   45705 O  O   . HIS   Z  12 195 ? 71.164  -147.697 35.326  1.00 93.98  ? 195 HIS   Z O   1 
ATOM   45706 C  CB  . HIS   Z  12 195 ? 69.897  -148.003 32.458  1.00 93.48  ? 195 HIS   Z CB  1 
ATOM   45707 C  CG  . HIS   Z  12 195 ? 68.529  -148.581 32.311  1.00 91.64  ? 195 HIS   Z CG  1 
ATOM   45708 N  ND1 . HIS   Z  12 195 ? 67.761  -148.411 31.173  1.00 90.46  ? 195 HIS   Z ND1 1 
ATOM   45709 C  CD2 . HIS   Z  12 195 ? 67.771  -149.292 33.172  1.00 91.71  ? 195 HIS   Z CD2 1 
ATOM   45710 C  CE1 . HIS   Z  12 195 ? 66.598  -149.011 31.336  1.00 90.08  ? 195 HIS   Z CE1 1 
ATOM   45711 N  NE2 . HIS   Z  12 195 ? 66.579  -149.555 32.555  1.00 91.14  ? 195 HIS   Z NE2 1 
ATOM   45712 N  N   . ILE   Z  12 196 ? 68.959  -147.188 35.674  1.00 93.62  ? 196 ILE   Z N   1 
ATOM   45713 C  CA  . ILE   Z  12 196 ? 68.918  -147.401 37.155  1.00 96.44  ? 196 ILE   Z CA  1 
ATOM   45714 C  C   . ILE   Z  12 196 ? 68.942  -148.904 37.474  1.00 97.34  ? 196 ILE   Z C   1 
ATOM   45715 O  O   . ILE   Z  12 196 ? 69.446  -149.259 38.559  1.00 102.76 ? 196 ILE   Z O   1 
ATOM   45716 C  CB  . ILE   Z  12 196 ? 67.703  -146.687 37.795  1.00 95.05  ? 196 ILE   Z CB  1 
ATOM   45717 C  CG1 . ILE   Z  12 196 ? 66.359  -147.244 37.312  1.00 94.79  ? 196 ILE   Z CG1 1 
ATOM   45718 C  CG2 . ILE   Z  12 196 ? 67.798  -145.186 37.577  1.00 96.53  ? 196 ILE   Z CG2 1 
ATOM   45719 C  CD1 . ILE   Z  12 196 ? 65.164  -146.767 38.113  1.00 94.27  ? 196 ILE   Z CD1 1 
ATOM   45720 N  N   . GLN   Z  12 197 ? 68.421  -149.743 36.570  1.00 96.62  ? 197 GLN   Z N   1 
ATOM   45721 C  CA  . GLN   Z  12 197 ? 68.291  -151.218 36.736  1.00 94.43  ? 197 GLN   Z CA  1 
ATOM   45722 C  C   . GLN   Z  12 197 ? 69.602  -151.934 36.385  1.00 96.10  ? 197 GLN   Z C   1 
ATOM   45723 O  O   . GLN   Z  12 197 ? 69.660  -153.163 36.599  1.00 97.55  ? 197 GLN   Z O   1 
ATOM   45724 C  CB  . GLN   Z  12 197 ? 67.164  -151.758 35.853  1.00 93.87  ? 197 GLN   Z CB  1 
ATOM   45725 C  CG  . GLN   Z  12 197 ? 65.795  -151.190 36.195  1.00 95.10  ? 197 GLN   Z CG  1 
ATOM   45726 C  CD  . GLN   Z  12 197 ? 64.717  -151.676 35.257  1.00 95.74  ? 197 GLN   Z CD  1 
ATOM   45727 O  OE1 . GLN   Z  12 197 ? 64.991  -152.170 34.165  1.00 92.62  ? 197 GLN   Z OE1 1 
ATOM   45728 N  NE2 . GLN   Z  12 197 ? 63.471  -151.534 35.681  1.00 98.68  ? 197 GLN   Z NE2 1 
ATOM   45729 N  N   . VAL   Z  12 198 ? 70.602  -151.219 35.859  1.00 91.68  ? 198 VAL   Z N   1 
ATOM   45730 C  CA  . VAL   Z  12 198 ? 71.904  -151.801 35.412  1.00 91.68  ? 198 VAL   Z CA  1 
ATOM   45731 C  C   . VAL   Z  12 198 ? 73.015  -151.339 36.360  1.00 94.24  ? 198 VAL   Z C   1 
ATOM   45732 O  O   . VAL   Z  12 198 ? 73.118  -150.120 36.584  1.00 92.26  ? 198 VAL   Z O   1 
ATOM   45733 C  CB  . VAL   Z  12 198 ? 72.218  -151.415 33.953  1.00 91.07  ? 198 VAL   Z CB  1 
ATOM   45734 C  CG1 . VAL   Z  12 198 ? 73.578  -151.936 33.509  1.00 90.58  ? 198 VAL   Z CG1 1 
ATOM   45735 C  CG2 . VAL   Z  12 198 ? 71.129  -151.889 33.001  1.00 89.92  ? 198 VAL   Z CG2 1 
ATOM   45736 N  N   . GLY   Z  12 199 ? 73.819  -152.278 36.878  1.00 95.10  ? 199 GLY   Z N   1 
ATOM   45737 C  CA  . GLY   Z  12 199 ? 75.010  -151.985 37.703  1.00 99.41  ? 199 GLY   Z CA  1 
ATOM   45738 C  C   . GLY   Z  12 199 ? 75.493  -153.180 38.513  1.00 100.76 ? 199 GLY   Z C   1 
ATOM   45739 O  O   . GLY   Z  12 199 ? 75.226  -154.328 38.101  1.00 100.98 ? 199 GLY   Z O   1 
ATOM   45740 N  N   . ASP   Z  12 200 ? 76.207  -152.901 39.612  1.00 101.90 ? 200 ASP   Z N   1 
ATOM   45741 C  CA  . ASP   Z  12 200 ? 76.719  -153.870 40.625  1.00 100.54 ? 200 ASP   Z CA  1 
ATOM   45742 C  C   . ASP   Z  12 200 ? 77.927  -154.640 40.075  1.00 97.93  ? 200 ASP   Z C   1 
ATOM   45743 O  O   . ASP   Z  12 200 ? 79.035  -154.446 40.618  1.00 93.94  ? 200 ASP   Z O   1 
ATOM   45744 C  CB  . ASP   Z  12 200 ? 75.609  -154.797 41.130  1.00 101.95 ? 200 ASP   Z CB  1 
ATOM   45745 C  CG  . ASP   Z  12 200 ? 74.554  -154.074 41.951  1.00 104.25 ? 200 ASP   Z CG  1 
ATOM   45746 O  OD1 . ASP   Z  12 200 ? 74.933  -153.189 42.739  1.00 111.07 ? 200 ASP   Z OD1 1 
ATOM   45747 O  OD2 . ASP   Z  12 200 ? 73.362  -154.393 41.790  1.00 107.69 ? 200 ASP   Z OD2 1 
ATOM   45748 N  N   . GLY   Z  12 201 ? 77.728  -155.487 39.059  1.00 96.79  ? 201 GLY   Z N   1 
ATOM   45749 C  CA  . GLY   Z  12 201 ? 78.794  -156.330 38.481  1.00 99.93  ? 201 GLY   Z CA  1 
ATOM   45750 C  C   . GLY   Z  12 201 ? 78.499  -156.759 37.054  1.00 100.57 ? 201 GLY   Z C   1 
ATOM   45751 O  O   . GLY   Z  12 201 ? 77.317  -156.729 36.653  1.00 100.83 ? 201 GLY   Z O   1 
ATOM   45752 N  N   . LEU   Z  12 202 ? 79.547  -157.152 36.322  1.00 101.82 ? 202 LEU   Z N   1 
ATOM   45753 C  CA  . LEU   Z  12 202 ? 79.489  -157.642 34.919  1.00 102.88 ? 202 LEU   Z CA  1 
ATOM   45754 C  C   . LEU   Z  12 202 ? 80.181  -159.006 34.839  1.00 103.76 ? 202 LEU   Z C   1 
ATOM   45755 O  O   . LEU   Z  12 202 ? 81.376  -159.072 35.190  1.00 108.35 ? 202 LEU   Z O   1 
ATOM   45756 C  CB  . LEU   Z  12 202 ? 80.188  -156.626 34.010  1.00 100.82 ? 202 LEU   Z CB  1 
ATOM   45757 C  CG  . LEU   Z  12 202 ? 80.469  -157.096 32.583  1.00 101.22 ? 202 LEU   Z CG  1 
ATOM   45758 C  CD1 . LEU   Z  12 202 ? 79.175  -157.419 31.854  1.00 100.55 ? 202 LEU   Z CD1 1 
ATOM   45759 C  CD2 . LEU   Z  12 202 ? 81.268  -156.054 31.817  1.00 101.21 ? 202 LEU   Z CD2 1 
ATOM   45760 N  N   . GLU   Z  12 203 ? 79.461  -160.036 34.383  1.00 103.21 ? 203 GLU   Z N   1 
ATOM   45761 C  CA  . GLU   Z  12 203 ? 80.004  -161.403 34.159  1.00 101.43 ? 203 GLU   Z CA  1 
ATOM   45762 C  C   . GLU   Z  12 203 ? 79.960  -161.711 32.659  1.00 97.13  ? 203 GLU   Z C   1 
ATOM   45763 O  O   . GLU   Z  12 203 ? 78.855  -161.700 32.082  1.00 90.15  ? 203 GLU   Z O   1 
ATOM   45764 C  CB  . GLU   Z  12 203 ? 79.224  -162.439 34.970  1.00 104.71 ? 203 GLU   Z CB  1 
ATOM   45765 C  CG  . GLU   Z  12 203 ? 79.932  -163.778 35.072  1.00 108.31 ? 203 GLU   Z CG  1 
ATOM   45766 C  CD  . GLU   Z  12 203 ? 79.563  -164.598 36.296  1.00 112.60 ? 203 GLU   Z CD  1 
ATOM   45767 O  OE1 . GLU   Z  12 203 ? 80.417  -164.728 37.196  1.00 117.26 ? 203 GLU   Z OE1 1 
ATOM   45768 O  OE2 . GLU   Z  12 203 ? 78.427  -165.110 36.346  1.00 114.81 ? 203 GLU   Z OE2 1 
ATOM   45769 N  N   . ILE   Z  12 204 ? 81.127  -161.954 32.060  1.00 97.07  ? 204 ILE   Z N   1 
ATOM   45770 C  CA  . ILE   Z  12 204 ? 81.287  -162.307 30.619  1.00 100.94 ? 204 ILE   Z CA  1 
ATOM   45771 C  C   . ILE   Z  12 204 ? 81.673  -163.786 30.533  1.00 101.75 ? 204 ILE   Z C   1 
ATOM   45772 O  O   . ILE   Z  12 204 ? 82.585  -164.197 31.276  1.00 107.33 ? 204 ILE   Z O   1 
ATOM   45773 C  CB  . ILE   Z  12 204 ? 82.338  -161.412 29.929  1.00 102.19 ? 204 ILE   Z CB  1 
ATOM   45774 C  CG1 . ILE   Z  12 204 ? 82.159  -159.932 30.280  1.00 103.77 ? 204 ILE   Z CG1 1 
ATOM   45775 C  CG2 . ILE   Z  12 204 ? 82.325  -161.640 28.424  1.00 102.91 ? 204 ILE   Z CG2 1 
ATOM   45776 C  CD1 . ILE   Z  12 204 ? 83.343  -159.063 29.915  1.00 104.66 ? 204 ILE   Z CD1 1 
ATOM   45777 N  N   . LEU   Z  12 205 ? 80.998  -164.543 29.662  1.00 99.55  ? 205 LEU   Z N   1 
ATOM   45778 C  CA  . LEU   Z  12 205 ? 81.360  -165.941 29.306  1.00 99.88  ? 205 LEU   Z CA  1 
ATOM   45779 C  C   . LEU   Z  12 205 ? 81.910  -165.952 27.877  1.00 101.92 ? 205 LEU   Z C   1 
ATOM   45780 O  O   . LEU   Z  12 205 ? 81.165  -165.566 26.956  1.00 102.15 ? 205 LEU   Z O   1 
ATOM   45781 C  CB  . LEU   Z  12 205 ? 80.134  -166.848 29.445  1.00 96.63  ? 205 LEU   Z CB  1 
ATOM   45782 C  CG  . LEU   Z  12 205 ? 79.902  -167.415 30.845  1.00 97.09  ? 205 LEU   Z CG  1 
ATOM   45783 C  CD1 . LEU   Z  12 205 ? 79.348  -166.353 31.780  1.00 96.81  ? 205 LEU   Z CD1 1 
ATOM   45784 C  CD2 . LEU   Z  12 205 ? 78.973  -168.617 30.798  1.00 97.32  ? 205 LEU   Z CD2 1 
ATOM   45785 N  N   . ILE   Z  12 206 ? 83.169  -166.374 27.717  1.00 104.88 ? 206 ILE   Z N   1 
ATOM   45786 C  CA  . ILE   Z  12 206 ? 83.907  -166.412 26.420  1.00 109.65 ? 206 ILE   Z CA  1 
ATOM   45787 C  C   . ILE   Z  12 206 ? 83.946  -167.866 25.943  1.00 107.93 ? 206 ILE   Z C   1 
ATOM   45788 O  O   . ILE   Z  12 206 ? 84.306  -168.739 26.755  1.00 109.02 ? 206 ILE   Z O   1 
ATOM   45789 C  CB  . ILE   Z  12 206 ? 85.326  -165.823 26.569  1.00 115.62 ? 206 ILE   Z CB  1 
ATOM   45790 C  CG1 . ILE   Z  12 206 ? 85.312  -164.468 27.285  1.00 120.58 ? 206 ILE   Z CG1 1 
ATOM   45791 C  CG2 . ILE   Z  12 206 ? 86.022  -165.740 25.217  1.00 118.56 ? 206 ILE   Z CG2 1 
ATOM   45792 C  CD1 . ILE   Z  12 206 ? 85.549  -164.546 28.779  1.00 123.94 ? 206 ILE   Z CD1 1 
ATOM   45793 N  N   . VAL   Z  12 207 ? 83.597  -168.107 24.676  1.00 106.02 ? 207 VAL   Z N   1 
ATOM   45794 C  CA  . VAL   Z  12 207 ? 83.490  -169.473 24.082  1.00 106.75 ? 207 VAL   Z CA  1 
ATOM   45795 C  C   . VAL   Z  12 207 ? 84.482  -169.595 22.923  1.00 107.57 ? 207 VAL   Z C   1 
ATOM   45796 O  O   . VAL   Z  12 207 ? 84.278  -168.915 21.900  1.00 104.71 ? 207 VAL   Z O   1 
ATOM   45797 C  CB  . VAL   Z  12 207 ? 82.057  -169.779 23.610  1.00 104.31 ? 207 VAL   Z CB  1 
ATOM   45798 C  CG1 . VAL   Z  12 207 ? 81.958  -171.177 23.018  1.00 105.75 ? 207 VAL   Z CG1 1 
ATOM   45799 C  CG2 . VAL   Z  12 207 ? 81.043  -169.600 24.728  1.00 100.65 ? 207 VAL   Z CG2 1 
ATOM   45800 N  N   . THR   Z  12 208 ? 85.499  -170.445 23.090  1.00 109.86 ? 208 THR   Z N   1 
ATOM   45801 C  CA  . THR   Z  12 208 ? 86.435  -170.889 22.023  1.00 110.21 ? 208 THR   Z CA  1 
ATOM   45802 C  C   . THR   Z  12 208 ? 86.304  -172.405 21.866  1.00 111.68 ? 208 THR   Z C   1 
ATOM   45803 O  O   . THR   Z  12 208 ? 85.514  -173.002 22.619  1.00 113.59 ? 208 THR   Z O   1 
ATOM   45804 C  CB  . THR   Z  12 208 ? 87.873  -170.470 22.345  1.00 111.58 ? 208 THR   Z CB  1 
ATOM   45805 O  OG1 . THR   Z  12 208 ? 88.285  -171.162 23.525  1.00 108.74 ? 208 THR   Z OG1 1 
ATOM   45806 C  CG2 . THR   Z  12 208 ? 88.010  -168.978 22.547  1.00 111.83 ? 208 THR   Z CG2 1 
ATOM   45807 N  N   . LYS   Z  12 209 ? 87.053  -172.996 20.931  1.00 115.05 ? 209 LYS   Z N   1 
ATOM   45808 C  CA  . LYS   Z  12 209 ? 87.095  -174.467 20.707  1.00 116.52 ? 209 LYS   Z CA  1 
ATOM   45809 C  C   . LYS   Z  12 209 ? 87.649  -175.173 21.955  1.00 116.32 ? 209 LYS   Z C   1 
ATOM   45810 O  O   . LYS   Z  12 209 ? 87.409  -176.389 22.084  1.00 118.76 ? 209 LYS   Z O   1 
ATOM   45811 C  CB  . LYS   Z  12 209 ? 87.902  -174.804 19.447  1.00 117.70 ? 209 LYS   Z CB  1 
ATOM   45812 C  CG  . LYS   Z  12 209 ? 89.351  -174.331 19.429  1.00 121.58 ? 209 LYS   Z CG  1 
ATOM   45813 C  CD  . LYS   Z  12 209 ? 90.152  -174.913 18.280  1.00 125.34 ? 209 LYS   Z CD  1 
ATOM   45814 C  CE  . LYS   Z  12 209 ? 91.496  -174.245 18.081  1.00 131.70 ? 209 LYS   Z CE  1 
ATOM   45815 N  NZ  . LYS   Z  12 209 ? 92.405  -174.473 19.230  1.00 135.18 ? 209 LYS   Z NZ  1 
ATOM   45816 N  N   . ASP   Z  12 210 ? 88.338  -174.444 22.845  1.00 116.50 ? 210 ASP   Z N   1 
ATOM   45817 C  CA  . ASP   Z  12 210 ? 88.968  -174.985 24.082  1.00 117.21 ? 210 ASP   Z CA  1 
ATOM   45818 C  C   . ASP   Z  12 210 ? 87.972  -175.027 25.249  1.00 111.50 ? 210 ASP   Z C   1 
ATOM   45819 O  O   . ASP   Z  12 210 ? 88.337  -175.604 26.288  1.00 114.76 ? 210 ASP   Z O   1 
ATOM   45820 C  CB  . ASP   Z  12 210 ? 90.197  -174.167 24.489  1.00 122.69 ? 210 ASP   Z CB  1 
ATOM   45821 C  CG  . ASP   Z  12 210 ? 91.366  -174.291 23.528  1.00 127.48 ? 210 ASP   Z CG  1 
ATOM   45822 O  OD1 . ASP   Z  12 210 ? 91.153  -174.781 22.404  1.00 134.14 ? 210 ASP   Z OD1 1 
ATOM   45823 O  OD2 . ASP   Z  12 210 ? 92.482  -173.900 23.917  1.00 135.29 ? 210 ASP   Z OD2 1 
ATOM   45824 N  N   . GLY   Z  12 211 ? 86.784  -174.427 25.109  1.00 110.38 ? 211 GLY   Z N   1 
ATOM   45825 C  CA  . GLY   Z  12 211 ? 85.706  -174.507 26.117  1.00 110.19 ? 211 GLY   Z CA  1 
ATOM   45826 C  C   . GLY   Z  12 211 ? 85.125  -173.145 26.459  1.00 110.82 ? 211 GLY   Z C   1 
ATOM   45827 O  O   . GLY   Z  12 211 ? 85.137  -172.253 25.583  1.00 112.69 ? 211 GLY   Z O   1 
ATOM   45828 N  N   . VAL   Z  12 212 ? 84.633  -172.996 27.694  1.00 109.57 ? 212 VAL   Z N   1 
ATOM   45829 C  CA  . VAL   Z  12 212 ? 83.947  -171.770 28.200  1.00 107.73 ? 212 VAL   Z CA  1 
ATOM   45830 C  C   . VAL   Z  12 212 ? 84.771  -171.192 29.356  1.00 107.40 ? 212 VAL   Z C   1 
ATOM   45831 O  O   . VAL   Z  12 212 ? 84.975  -171.917 30.348  1.00 106.87 ? 212 VAL   Z O   1 
ATOM   45832 C  CB  . VAL   Z  12 212 ? 82.501  -172.075 28.638  1.00 105.62 ? 212 VAL   Z CB  1 
ATOM   45833 C  CG1 . VAL   Z  12 212 ? 81.778  -170.825 29.116  1.00 104.92 ? 212 VAL   Z CG1 1 
ATOM   45834 C  CG2 . VAL   Z  12 212 ? 81.707  -172.753 27.532  1.00 105.62 ? 212 VAL   Z CG2 1 
ATOM   45835 N  N   . ARG   Z  12 213 ? 85.215  -169.937 29.218  1.00 109.92 ? 213 ARG   Z N   1 
ATOM   45836 C  CA  . ARG   Z  12 213 ? 85.963  -169.165 30.249  1.00 110.96 ? 213 ARG   Z CA  1 
ATOM   45837 C  C   . ARG   Z  12 213 ? 85.060  -168.050 30.789  1.00 111.36 ? 213 ARG   Z C   1 
ATOM   45838 O  O   . ARG   Z  12 213 ? 84.188  -167.582 30.030  1.00 114.37 ? 213 ARG   Z O   1 
ATOM   45839 C  CB  . ARG   Z  12 213 ? 87.241  -168.576 29.644  1.00 112.69 ? 213 ARG   Z CB  1 
ATOM   45840 C  CG  . ARG   Z  12 213 ? 88.143  -167.876 30.650  1.00 114.78 ? 213 ARG   Z CG  1 
ATOM   45841 C  CD  . ARG   Z  12 213 ? 89.471  -167.450 30.052  1.00 120.74 ? 213 ARG   Z CD  1 
ATOM   45842 N  NE  . ARG   Z  12 213 ? 89.368  -166.233 29.250  1.00 122.78 ? 213 ARG   Z NE  1 
ATOM   45843 C  CZ  . ARG   Z  12 213 ? 89.200  -166.181 27.926  1.00 120.66 ? 213 ARG   Z CZ  1 
ATOM   45844 N  NH1 . ARG   Z  12 213 ? 89.106  -167.286 27.202  1.00 123.54 ? 213 ARG   Z NH1 1 
ATOM   45845 N  NH2 . ARG   Z  12 213 ? 89.124  -165.007 27.323  1.00 119.62 ? 213 ARG   Z NH2 1 
ATOM   45846 N  N   . LYS   Z  12 214 ? 85.272  -167.640 32.046  1.00 113.16 ? 214 LYS   Z N   1 
ATOM   45847 C  CA  . LYS   Z  12 214 ? 84.516  -166.546 32.715  1.00 109.67 ? 214 LYS   Z CA  1 
ATOM   45848 C  C   . LYS   Z  12 214 ? 85.466  -165.401 33.078  1.00 110.86 ? 214 LYS   Z C   1 
ATOM   45849 O  O   . LYS   Z  12 214 ? 86.631  -165.680 33.427  1.00 105.80 ? 214 LYS   Z O   1 
ATOM   45850 C  CB  . LYS   Z  12 214 ? 83.807  -167.057 33.972  1.00 111.49 ? 214 LYS   Z CB  1 
ATOM   45851 C  CG  . LYS   Z  12 214 ? 82.545  -167.863 33.710  1.00 110.47 ? 214 LYS   Z CG  1 
ATOM   45852 C  CD  . LYS   Z  12 214 ? 81.919  -168.421 34.966  1.00 114.60 ? 214 LYS   Z CD  1 
ATOM   45853 C  CE  . LYS   Z  12 214 ? 81.066  -169.645 34.705  1.00 114.25 ? 214 LYS   Z CE  1 
ATOM   45854 N  NZ  . LYS   Z  12 214 ? 80.827  -170.415 35.948  1.00 115.28 ? 214 LYS   Z NZ  1 
ATOM   45855 N  N   . GLU   Z  12 215 ? 84.968  -164.165 32.984  1.00 111.23 ? 215 GLU   Z N   1 
ATOM   45856 C  CA  . GLU   Z  12 215 ? 85.622  -162.933 33.499  1.00 112.16 ? 215 GLU   Z CA  1 
ATOM   45857 C  C   . GLU   Z  12 215 ? 84.571  -162.108 34.247  1.00 108.14 ? 215 GLU   Z C   1 
ATOM   45858 O  O   . GLU   Z  12 215 ? 83.430  -162.015 33.747  1.00 103.95 ? 215 GLU   Z O   1 
ATOM   45859 C  CB  . GLU   Z  12 215 ? 86.247  -162.126 32.359  1.00 113.61 ? 215 GLU   Z CB  1 
ATOM   45860 C  CG  . GLU   Z  12 215 ? 87.496  -162.765 31.780  1.00 118.43 ? 215 GLU   Z CG  1 
ATOM   45861 C  CD  . GLU   Z  12 215 ? 88.206  -161.933 30.725  1.00 120.42 ? 215 GLU   Z CD  1 
ATOM   45862 O  OE1 . GLU   Z  12 215 ? 89.002  -162.512 29.959  1.00 127.67 ? 215 GLU   Z OE1 1 
ATOM   45863 O  OE2 . GLU   Z  12 215 ? 87.966  -160.710 30.674  1.00 120.61 ? 215 GLU   Z OE2 1 
ATOM   45864 N  N   . PHE   Z  12 216 ? 84.944  -161.551 35.404  1.00 107.57 ? 216 PHE   Z N   1 
ATOM   45865 C  CA  . PHE   Z  12 216 ? 84.073  -160.705 36.260  1.00 107.04 ? 216 PHE   Z CA  1 
ATOM   45866 C  C   . PHE   Z  12 216 ? 84.715  -159.327 36.442  1.00 110.11 ? 216 PHE   Z C   1 
ATOM   45867 O  O   . PHE   Z  12 216 ? 85.946  -159.251 36.637  1.00 117.78 ? 216 PHE   Z O   1 
ATOM   45868 C  CB  . PHE   Z  12 216 ? 83.829  -161.359 37.621  1.00 104.35 ? 216 PHE   Z CB  1 
ATOM   45869 C  CG  . PHE   Z  12 216 ? 82.939  -160.552 38.531  1.00 102.62 ? 216 PHE   Z CG  1 
ATOM   45870 C  CD1 . PHE   Z  12 216 ? 81.566  -160.531 38.340  1.00 100.60 ? 216 PHE   Z CD1 1 
ATOM   45871 C  CD2 . PHE   Z  12 216 ? 83.474  -159.793 39.560  1.00 104.63 ? 216 PHE   Z CD2 1 
ATOM   45872 C  CE1 . PHE   Z  12 216 ? 80.746  -159.778 39.167  1.00 100.63 ? 216 PHE   Z CE1 1 
ATOM   45873 C  CE2 . PHE   Z  12 216 ? 82.653  -159.041 40.387  1.00 105.01 ? 216 PHE   Z CE2 1 
ATOM   45874 C  CZ  . PHE   Z  12 216 ? 81.291  -159.035 40.189  1.00 103.02 ? 216 PHE   Z CZ  1 
ATOM   45875 N  N   . TYR   Z  12 217 ? 83.893  -158.276 36.390  1.00 109.26 ? 217 TYR   Z N   1 
ATOM   45876 C  CA  . TYR   Z  12 217 ? 84.297  -156.866 36.624  1.00 108.10 ? 217 TYR   Z CA  1 
ATOM   45877 C  C   . TYR   Z  12 217 ? 83.233  -156.173 37.476  1.00 105.87 ? 217 TYR   Z C   1 
ATOM   45878 O  O   . TYR   Z  12 217 ? 82.029  -156.401 37.243  1.00 105.02 ? 217 TYR   Z O   1 
ATOM   45879 C  CB  . TYR   Z  12 217 ? 84.518  -156.146 35.293  1.00 107.22 ? 217 TYR   Z CB  1 
ATOM   45880 C  CG  . TYR   Z  12 217 ? 85.586  -156.773 34.436  1.00 108.01 ? 217 TYR   Z CG  1 
ATOM   45881 C  CD1 . TYR   Z  12 217 ? 86.928  -156.613 34.740  1.00 110.94 ? 217 TYR   Z CD1 1 
ATOM   45882 C  CD2 . TYR   Z  12 217 ? 85.258  -157.547 33.335  1.00 107.61 ? 217 TYR   Z CD2 1 
ATOM   45883 C  CE1 . TYR   Z  12 217 ? 87.920  -157.195 33.966  1.00 112.37 ? 217 TYR   Z CE1 1 
ATOM   45884 C  CE2 . TYR   Z  12 217 ? 86.237  -158.134 32.549  1.00 109.38 ? 217 TYR   Z CE2 1 
ATOM   45885 C  CZ  . TYR   Z  12 217 ? 87.573  -157.959 32.866  1.00 110.99 ? 217 TYR   Z CZ  1 
ATOM   45886 O  OH  . TYR   Z  12 217 ? 88.547  -158.533 32.102  1.00 112.40 ? 217 TYR   Z OH  1 
ATOM   45887 N  N   . GLU   Z  12 218 ? 83.679  -155.367 38.443  1.00 107.33 ? 218 GLU   Z N   1 
ATOM   45888 C  CA  . GLU   Z  12 218 ? 82.807  -154.510 39.287  1.00 106.64 ? 218 GLU   Z CA  1 
ATOM   45889 C  C   . GLU   Z  12 218 ? 82.114  -153.486 38.381  1.00 101.10 ? 218 GLU   Z C   1 
ATOM   45890 O  O   . GLU   Z  12 218 ? 82.744  -153.048 37.399  1.00 95.94  ? 218 GLU   Z O   1 
ATOM   45891 C  CB  . GLU   Z  12 218 ? 83.631  -153.816 40.374  1.00 109.69 ? 218 GLU   Z CB  1 
ATOM   45892 C  CG  . GLU   Z  12 218 ? 84.181  -154.764 41.425  1.00 112.69 ? 218 GLU   Z CG  1 
ATOM   45893 C  CD  . GLU   Z  12 218 ? 83.240  -155.042 42.584  1.00 115.23 ? 218 GLU   Z CD  1 
ATOM   45894 O  OE1 . GLU   Z  12 218 ? 82.748  -154.070 43.194  1.00 115.59 ? 218 GLU   Z OE1 1 
ATOM   45895 O  OE2 . GLU   Z  12 218 ? 82.999  -156.232 42.874  1.00 117.73 ? 218 GLU   Z OE2 1 
ATOM   45896 N  N   . LEU   Z  12 219 ? 80.854  -153.161 38.680  1.00 103.41 ? 219 LEU   Z N   1 
ATOM   45897 C  CA  . LEU   Z  12 219 ? 80.117  -152.000 38.110  1.00 104.07 ? 219 LEU   Z CA  1 
ATOM   45898 C  C   . LEU   Z  12 219 ? 79.662  -151.104 39.267  1.00 106.64 ? 219 LEU   Z C   1 
ATOM   45899 O  O   . LEU   Z  12 219 ? 79.776  -151.538 40.431  1.00 108.73 ? 219 LEU   Z O   1 
ATOM   45900 C  CB  . LEU   Z  12 219 ? 78.925  -152.492 37.279  1.00 102.24 ? 219 LEU   Z CB  1 
ATOM   45901 C  CG  . LEU   Z  12 219 ? 79.257  -153.236 35.983  1.00 99.79  ? 219 LEU   Z CG  1 
ATOM   45902 C  CD1 . LEU   Z  12 219 ? 77.981  -153.652 35.265  1.00 97.94  ? 219 LEU   Z CD1 1 
ATOM   45903 C  CD2 . LEU   Z  12 219 ? 80.122  -152.393 35.058  1.00 100.79 ? 219 LEU   Z CD2 1 
ATOM   45904 N  N   . LYS   Z  12 220 ? 79.180  -149.898 38.961  1.00 108.32 ? 220 LYS   Z N   1 
ATOM   45905 C  CA  . LYS   Z  12 220 ? 78.713  -148.918 39.978  1.00 111.29 ? 220 LYS   Z CA  1 
ATOM   45906 C  C   . LYS   Z  12 220 ? 77.454  -149.463 40.663  1.00 113.63 ? 220 LYS   Z C   1 
ATOM   45907 O  O   . LYS   Z  12 220 ? 76.561  -149.970 39.952  1.00 115.97 ? 220 LYS   Z O   1 
ATOM   45908 C  CB  . LYS   Z  12 220 ? 78.479  -147.546 39.343  1.00 113.85 ? 220 LYS   Z CB  1 
ATOM   45909 C  CG  . LYS   Z  12 220 ? 79.731  -146.688 39.227  1.00 113.76 ? 220 LYS   Z CG  1 
ATOM   45910 C  CD  . LYS   Z  12 220 ? 79.517  -145.422 38.437  1.00 115.32 ? 220 LYS   Z CD  1 
ATOM   45911 C  CE  . LYS   Z  12 220 ? 78.520  -144.488 39.090  1.00 115.67 ? 220 LYS   Z CE  1 
ATOM   45912 N  NZ  . LYS   Z  12 220 ? 78.465  -143.174 38.410  1.00 116.63 ? 220 LYS   Z NZ  1 
ATOM   45913 N  N   . ARG   Z  12 221 ? 77.396  -149.343 41.994  1.00 114.73 ? 221 ARG   Z N   1 
ATOM   45914 C  CA  . ARG   Z  12 221 ? 76.408  -150.026 42.873  1.00 113.64 ? 221 ARG   Z CA  1 
ATOM   45915 C  C   . ARG   Z  12 221 ? 75.263  -149.078 43.262  1.00 113.05 ? 221 ARG   Z C   1 
ATOM   45916 O  O   . ARG   Z  12 221 ? 74.403  -149.503 44.062  1.00 109.45 ? 221 ARG   Z O   1 
ATOM   45917 C  CB  . ARG   Z  12 221 ? 77.132  -150.572 44.110  1.00 115.76 ? 221 ARG   Z CB  1 
ATOM   45918 C  CG  . ARG   Z  12 221 ? 78.039  -151.758 43.815  1.00 115.61 ? 221 ARG   Z CG  1 
ATOM   45919 C  CD  . ARG   Z  12 221 ? 79.138  -151.945 44.845  1.00 116.41 ? 221 ARG   Z CD  1 
ATOM   45920 N  NE  . ARG   Z  12 221 ? 78.636  -152.443 46.119  1.00 116.40 ? 221 ARG   Z NE  1 
ATOM   45921 C  CZ  . ARG   Z  12 221 ? 78.459  -153.727 46.434  1.00 112.99 ? 221 ARG   Z CZ  1 
ATOM   45922 N  NH1 . ARG   Z  12 221 ? 78.735  -154.686 45.565  1.00 111.22 ? 221 ARG   Z NH1 1 
ATOM   45923 N  NH2 . ARG   Z  12 221 ? 77.997  -154.047 47.630  1.00 114.40 ? 221 ARG   Z NH2 1 
ATOM   45924 N  N   . ASP   Z  12 222 ? 75.222  -147.863 42.704  1.00 116.06 ? 222 ASP   Z N   1 
ATOM   45925 C  CA  . ASP   Z  12 222 ? 74.188  -146.840 43.029  1.00 118.31 ? 222 ASP   Z CA  1 
ATOM   45926 C  C   . ASP   Z  12 222 ? 72.941  -147.084 42.164  1.00 116.82 ? 222 ASP   Z C   1 
ATOM   45927 O  O   . ASP   Z  12 222 ? 72.886  -147.979 41.312  1.00 118.38 ? 222 ASP   Z O   1 
ATOM   45928 C  CB  . ASP   Z  12 222 ? 74.750  -145.416 42.915  1.00 115.98 ? 222 ASP   Z CB  1 
ATOM   45929 C  CG  . ASP   Z  12 222 ? 75.159  -144.977 41.517  1.00 112.28 ? 222 ASP   Z CG  1 
ATOM   45930 O  OD1 . ASP   Z  12 222 ? 75.459  -145.855 40.683  1.00 109.10 ? 222 ASP   Z OD1 1 
ATOM   45931 O  OD2 . ASP   Z  12 222 ? 75.183  -143.753 41.277  1.00 106.52 ? 222 ASP   Z OD2 1 
ATOM   45932 O  OXT . ASP   Z  12 222 ? 71.934  -146.383 42.308  1.00 121.05 ? 222 ASP   Z OXT 1 
ATOM   45933 N  N   . THR   AA 13 14  ? 43.443  -167.266 40.589  1.00 99.43  ? 1   THR   a N   1 
ATOM   45934 C  CA  . THR   AA 13 14  ? 43.562  -165.843 41.041  1.00 107.29 ? 1   THR   a CA  1 
ATOM   45935 C  C   . THR   AA 13 14  ? 43.000  -165.719 42.459  1.00 96.46  ? 1   THR   a C   1 
ATOM   45936 O  O   . THR   AA 13 14  ? 41.832  -166.091 42.668  1.00 99.98  ? 1   THR   a O   1 
ATOM   45937 C  CB  . THR   AA 13 14  ? 42.864  -164.870 40.079  1.00 116.02 ? 1   THR   a CB  1 
ATOM   45938 O  OG1 . THR   AA 13 14  ? 43.637  -164.789 38.880  1.00 124.18 ? 1   THR   a OG1 1 
ATOM   45939 C  CG2 . THR   AA 13 14  ? 42.694  -163.479 40.656  1.00 119.59 ? 1   THR   a CG2 1 
ATOM   45940 N  N   . GLN   AA 13 15  ? 43.805  -165.189 43.380  1.00 95.35  ? 2   GLN   a N   1 
ATOM   45941 C  CA  . GLN   AA 13 15  ? 43.492  -165.098 44.826  1.00 92.64  ? 2   GLN   a CA  1 
ATOM   45942 C  C   . GLN   AA 13 15  ? 43.535  -163.636 45.276  1.00 90.64  ? 2   GLN   a C   1 
ATOM   45943 O  O   . GLN   AA 13 15  ? 43.875  -162.760 44.455  1.00 91.35  ? 2   GLN   a O   1 
ATOM   45944 C  CB  . GLN   AA 13 15  ? 44.530  -165.867 45.641  1.00 89.44  ? 2   GLN   a CB  1 
ATOM   45945 C  CG  . GLN   AA 13 15  ? 44.458  -167.377 45.500  1.00 91.67  ? 2   GLN   a CG  1 
ATOM   45946 C  CD  . GLN   AA 13 15  ? 45.316  -168.047 46.546  1.00 93.71  ? 2   GLN   a CD  1 
ATOM   45947 O  OE1 . GLN   AA 13 15  ? 45.558  -167.501 47.623  1.00 87.15  ? 2   GLN   a OE1 1 
ATOM   45948 N  NE2 . GLN   AA 13 15  ? 45.794  -169.242 46.237  1.00 99.86  ? 2   GLN   a NE2 1 
ATOM   45949 N  N   . GLN   AA 13 16  ? 43.201  -163.407 46.547  1.00 87.29  ? 3   GLN   a N   1 
ATOM   45950 C  CA  . GLN   AA 13 16  ? 43.628  -162.227 47.337  1.00 84.41  ? 3   GLN   a CA  1 
ATOM   45951 C  C   . GLN   AA 13 16  ? 43.976  -162.713 48.741  1.00 80.35  ? 3   GLN   a C   1 
ATOM   45952 O  O   . GLN   AA 13 16  ? 43.226  -163.484 49.333  1.00 79.80  ? 3   GLN   a O   1 
ATOM   45953 C  CB  . GLN   AA 13 16  ? 42.546  -161.147 47.346  1.00 88.71  ? 3   GLN   a CB  1 
ATOM   45954 C  CG  . GLN   AA 13 16  ? 41.212  -161.596 47.929  1.00 93.02  ? 3   GLN   a CG  1 
ATOM   45955 C  CD  . GLN   AA 13 16  ? 40.321  -160.426 48.270  1.00 99.07  ? 3   GLN   a CD  1 
ATOM   45956 O  OE1 . GLN   AA 13 16  ? 40.787  -159.355 48.658  1.00 103.46 ? 3   GLN   a OE1 1 
ATOM   45957 N  NE2 . GLN   AA 13 16  ? 39.019  -160.625 48.135  1.00 105.55 ? 3   GLN   a NE2 1 
ATOM   45958 N  N   . PRO   AA 13 17  ? 45.121  -162.287 49.318  1.00 76.96  ? 4   PRO   a N   1 
ATOM   45959 C  CA  . PRO   AA 13 17  ? 45.526  -162.749 50.643  1.00 75.88  ? 4   PRO   a CA  1 
ATOM   45960 C  C   . PRO   AA 13 17  ? 44.554  -162.196 51.694  1.00 76.28  ? 4   PRO   a C   1 
ATOM   45961 O  O   . PRO   AA 13 17  ? 44.093  -161.094 51.509  1.00 79.92  ? 4   PRO   a O   1 
ATOM   45962 C  CB  . PRO   AA 13 17  ? 46.943  -162.183 50.795  1.00 75.71  ? 4   PRO   a CB  1 
ATOM   45963 C  CG  . PRO   AA 13 17  ? 46.928  -160.935 49.943  1.00 76.09  ? 4   PRO   a CG  1 
ATOM   45964 C  CD  . PRO   AA 13 17  ? 46.040  -161.282 48.767  1.00 77.21  ? 4   PRO   a CD  1 
ATOM   45965 N  N   . ILE   AA 13 18  ? 44.243  -162.975 52.731  1.00 75.84  ? 5   ILE   a N   1 
ATOM   45966 C  CA  . ILE   AA 13 18  ? 43.307  -162.579 53.825  1.00 76.51  ? 5   ILE   a CA  1 
ATOM   45967 C  C   . ILE   AA 13 18  ? 44.129  -162.357 55.100  1.00 78.99  ? 5   ILE   a C   1 
ATOM   45968 O  O   . ILE   AA 13 18  ? 44.462  -161.192 55.375  1.00 77.69  ? 5   ILE   a O   1 
ATOM   45969 C  CB  . ILE   AA 13 18  ? 42.189  -163.626 54.001  1.00 78.74  ? 5   ILE   a CB  1 
ATOM   45970 C  CG1 . ILE   AA 13 18  ? 41.454  -163.910 52.687  1.00 78.18  ? 5   ILE   a CG1 1 
ATOM   45971 C  CG2 . ILE   AA 13 18  ? 41.229  -163.220 55.110  1.00 81.10  ? 5   ILE   a CG2 1 
ATOM   45972 C  CD1 . ILE   AA 13 18  ? 40.824  -162.698 52.046  1.00 76.67  ? 5   ILE   a CD1 1 
ATOM   45973 N  N   . VAL   AA 13 19  ? 44.450  -163.422 55.841  1.00 77.64  ? 6   VAL   a N   1 
ATOM   45974 C  CA  . VAL   AA 13 19  ? 45.342  -163.362 57.036  1.00 77.32  ? 6   VAL   a CA  1 
ATOM   45975 C  C   . VAL   AA 13 19  ? 46.775  -163.385 56.501  1.00 76.41  ? 6   VAL   a C   1 
ATOM   45976 O  O   . VAL   AA 13 19  ? 47.071  -164.271 55.688  1.00 77.65  ? 6   VAL   a O   1 
ATOM   45977 C  CB  . VAL   AA 13 19  ? 45.071  -164.515 58.023  1.00 79.42  ? 6   VAL   a CB  1 
ATOM   45978 C  CG1 . VAL   AA 13 19  ? 45.903  -164.385 59.290  1.00 80.86  ? 6   VAL   a CG1 1 
ATOM   45979 C  CG2 . VAL   AA 13 19  ? 43.595  -164.629 58.376  1.00 80.29  ? 6   VAL   a CG2 1 
ATOM   45980 N  N   . THR   AA 13 20  ? 47.616  -162.429 56.901  1.00 76.58  ? 7   THR   a N   1 
ATOM   45981 C  CA  . THR   AA 13 20  ? 48.969  -162.229 56.318  1.00 78.78  ? 7   THR   a CA  1 
ATOM   45982 C  C   . THR   AA 13 20  ? 50.040  -162.083 57.400  1.00 77.50  ? 7   THR   a C   1 
ATOM   45983 O  O   . THR   AA 13 20  ? 49.710  -161.664 58.526  1.00 77.76  ? 7   THR   a O   1 
ATOM   45984 C  CB  . THR   AA 13 20  ? 49.005  -160.997 55.411  1.00 81.67  ? 7   THR   a CB  1 
ATOM   45985 O  OG1 . THR   AA 13 20  ? 48.561  -159.879 56.181  1.00 84.91  ? 7   THR   a OG1 1 
ATOM   45986 C  CG2 . THR   AA 13 20  ? 48.144  -161.168 54.181  1.00 83.02  ? 7   THR   a CG2 1 
ATOM   45987 N  N   . GLY   AA 13 21  ? 51.277  -162.419 57.031  1.00 77.72  ? 8   GLY   a N   1 
ATOM   45988 C  CA  . GLY   AA 13 21  ? 52.499  -162.205 57.826  1.00 80.10  ? 8   GLY   a CA  1 
ATOM   45989 C  C   . GLY   AA 13 21  ? 53.429  -161.255 57.099  1.00 80.90  ? 8   GLY   a C   1 
ATOM   45990 O  O   . GLY   AA 13 21  ? 53.540  -161.377 55.863  1.00 78.87  ? 8   GLY   a O   1 
ATOM   45991 N  N   . THR   AA 13 22  ? 54.060  -160.333 57.831  1.00 83.44  ? 9   THR   a N   1 
ATOM   45992 C  CA  . THR   AA 13 22  ? 54.911  -159.251 57.267  1.00 85.63  ? 9   THR   a CA  1 
ATOM   45993 C  C   . THR   AA 13 22  ? 56.348  -159.770 57.109  1.00 83.42  ? 9   THR   a C   1 
ATOM   45994 O  O   . THR   AA 13 22  ? 56.516  -160.987 56.933  1.00 85.85  ? 9   THR   a O   1 
ATOM   45995 C  CB  . THR   AA 13 22  ? 54.785  -157.970 58.103  1.00 89.67  ? 9   THR   a CB  1 
ATOM   45996 O  OG1 . THR   AA 13 22  ? 55.474  -156.925 57.413  1.00 94.69  ? 9   THR   a OG1 1 
ATOM   45997 C  CG2 . THR   AA 13 22  ? 55.338  -158.098 59.506  1.00 91.98  ? 9   THR   a CG2 1 
ATOM   45998 N  N   . SER   AA 13 23  ? 57.332  -158.867 57.162  1.00 83.88  ? 10  SER   a N   1 
ATOM   45999 C  CA  . SER   AA 13 23  ? 58.768  -159.095 56.849  1.00 85.39  ? 10  SER   a CA  1 
ATOM   46000 C  C   . SER   AA 13 23  ? 59.295  -160.418 57.425  1.00 83.35  ? 10  SER   a C   1 
ATOM   46001 O  O   . SER   AA 13 23  ? 58.966  -160.761 58.584  1.00 82.26  ? 10  SER   a O   1 
ATOM   46002 C  CB  . SER   AA 13 23  ? 59.597  -157.936 57.342  1.00 89.14  ? 10  SER   a CB  1 
ATOM   46003 O  OG  . SER   AA 13 23  ? 58.958  -156.698 57.061  1.00 92.40  ? 10  SER   a OG  1 
ATOM   46004 N  N   . VAL   AA 13 24  ? 60.097  -161.121 56.620  1.00 81.41  ? 11  VAL   a N   1 
ATOM   46005 C  CA  . VAL   AA 13 24  ? 61.056  -162.183 57.046  1.00 82.56  ? 11  VAL   a CA  1 
ATOM   46006 C  C   . VAL   AA 13 24  ? 62.457  -161.690 56.674  1.00 79.73  ? 11  VAL   a C   1 
ATOM   46007 O  O   . VAL   AA 13 24  ? 62.675  -161.432 55.480  1.00 75.97  ? 11  VAL   a O   1 
ATOM   46008 C  CB  . VAL   AA 13 24  ? 60.755  -163.531 56.363  1.00 82.85  ? 11  VAL   a CB  1 
ATOM   46009 C  CG1 . VAL   AA 13 24  ? 61.794  -164.588 56.708  1.00 83.95  ? 11  VAL   a CG1 1 
ATOM   46010 C  CG2 . VAL   AA 13 24  ? 59.354  -164.031 56.681  1.00 84.87  ? 11  VAL   a CG2 1 
ATOM   46011 N  N   . ILE   AA 13 25  ? 63.361  -161.564 57.649  1.00 81.42  ? 12  ILE   a N   1 
ATOM   46012 C  CA  . ILE   AA 13 25  ? 64.738  -161.021 57.438  1.00 82.73  ? 12  ILE   a CA  1 
ATOM   46013 C  C   . ILE   AA 13 25  ? 65.761  -162.112 57.778  1.00 82.56  ? 12  ILE   a C   1 
ATOM   46014 O  O   . ILE   AA 13 25  ? 65.452  -162.980 58.618  1.00 81.16  ? 12  ILE   a O   1 
ATOM   46015 C  CB  . ILE   AA 13 25  ? 64.953  -159.721 58.242  1.00 82.59  ? 12  ILE   a CB  1 
ATOM   46016 C  CG1 . ILE   AA 13 25  ? 64.901  -159.937 59.756  1.00 83.48  ? 12  ILE   a CG1 1 
ATOM   46017 C  CG2 . ILE   AA 13 25  ? 63.952  -158.666 57.803  1.00 82.47  ? 12  ILE   a CG2 1 
ATOM   46018 C  CD1 . ILE   AA 13 25  ? 65.494  -158.799 60.553  1.00 84.00  ? 12  ILE   a CD1 1 
ATOM   46019 N  N   . SER   AA 13 26  ? 66.930  -162.064 57.134  1.00 85.32  ? 13  SER   a N   1 
ATOM   46020 C  CA  . SER   AA 13 26  ? 67.986  -163.105 57.224  1.00 86.00  ? 13  SER   a CA  1 
ATOM   46021 C  C   . SER   AA 13 26  ? 69.316  -162.588 56.674  1.00 87.65  ? 13  SER   a C   1 
ATOM   46022 O  O   . SER   AA 13 26  ? 69.297  -161.663 55.836  1.00 85.78  ? 13  SER   a O   1 
ATOM   46023 C  CB  . SER   AA 13 26  ? 67.567  -164.330 56.476  1.00 85.60  ? 13  SER   a CB  1 
ATOM   46024 O  OG  . SER   AA 13 26  ? 67.359  -164.023 55.106  1.00 87.09  ? 13  SER   a OG  1 
ATOM   46025 N  N   . MET   AA 13 27  ? 70.418  -163.208 57.102  1.00 90.21  ? 14  MET   a N   1 
ATOM   46026 C  CA  . MET   AA 13 27  ? 71.789  -162.923 56.600  1.00 93.49  ? 14  MET   a CA  1 
ATOM   46027 C  C   . MET   AA 13 27  ? 72.699  -164.125 56.876  1.00 93.20  ? 14  MET   a C   1 
ATOM   46028 O  O   . MET   AA 13 27  ? 72.383  -164.918 57.785  1.00 93.86  ? 14  MET   a O   1 
ATOM   46029 C  CB  . MET   AA 13 27  ? 72.375  -161.668 57.260  1.00 96.38  ? 14  MET   a CB  1 
ATOM   46030 C  CG  . MET   AA 13 27  ? 72.546  -161.780 58.769  1.00 99.19  ? 14  MET   a CG  1 
ATOM   46031 S  SD  . MET   AA 13 27  ? 73.194  -160.265 59.528  1.00 102.79 ? 14  MET   a SD  1 
ATOM   46032 C  CE  . MET   AA 13 27  ? 74.909  -160.346 59.012  1.00 103.51 ? 14  MET   a CE  1 
ATOM   46033 N  N   . LYS   AA 13 28  ? 73.776  -164.245 56.098  1.00 94.03  ? 15  LYS   a N   1 
ATOM   46034 C  CA  . LYS   AA 13 28  ? 74.874  -165.222 56.306  1.00 93.69  ? 15  LYS   a CA  1 
ATOM   46035 C  C   . LYS   AA 13 28  ? 75.924  -164.596 57.226  1.00 96.97  ? 15  LYS   a C   1 
ATOM   46036 O  O   . LYS   AA 13 28  ? 76.144  -163.377 57.112  1.00 96.44  ? 15  LYS   a O   1 
ATOM   46037 C  CB  . LYS   AA 13 28  ? 75.529  -165.587 54.972  1.00 94.92  ? 15  LYS   a CB  1 
ATOM   46038 C  CG  . LYS   AA 13 28  ? 74.633  -166.302 53.974  1.00 94.81  ? 15  LYS   a CG  1 
ATOM   46039 C  CD  . LYS   AA 13 28  ? 75.255  -166.375 52.602  1.00 99.35  ? 15  LYS   a CD  1 
ATOM   46040 C  CE  . LYS   AA 13 28  ? 74.541  -167.324 51.665  1.00 101.66 ? 15  LYS   a CE  1 
ATOM   46041 N  NZ  . LYS   AA 13 28  ? 75.208  -167.372 50.343  1.00 106.69 ? 15  LYS   a NZ  1 
ATOM   46042 N  N   . TYR   AA 13 29  ? 76.535  -165.405 58.095  1.00 98.28  ? 16  TYR   a N   1 
ATOM   46043 C  CA  . TYR   AA 13 29  ? 77.759  -165.068 58.870  1.00 102.10 ? 16  TYR   a CA  1 
ATOM   46044 C  C   . TYR   AA 13 29  ? 78.794  -166.174 58.624  1.00 106.95 ? 16  TYR   a C   1 
ATOM   46045 O  O   . TYR   AA 13 29  ? 78.496  -167.091 57.829  1.00 109.31 ? 16  TYR   a O   1 
ATOM   46046 C  CB  . TYR   AA 13 29  ? 77.419  -164.847 60.347  1.00 102.86 ? 16  TYR   a CB  1 
ATOM   46047 C  CG  . TYR   AA 13 29  ? 76.919  -166.069 61.072  1.00 103.90 ? 16  TYR   a CG  1 
ATOM   46048 C  CD1 . TYR   AA 13 29  ? 75.579  -166.422 61.045  1.00 105.63 ? 16  TYR   a CD1 1 
ATOM   46049 C  CD2 . TYR   AA 13 29  ? 77.787  -166.876 61.786  1.00 107.83 ? 16  TYR   a CD2 1 
ATOM   46050 C  CE1 . TYR   AA 13 29  ? 75.117  -167.550 61.707  1.00 107.73 ? 16  TYR   a CE1 1 
ATOM   46051 C  CE2 . TYR   AA 13 29  ? 77.344  -168.009 62.450  1.00 109.09 ? 16  TYR   a CE2 1 
ATOM   46052 C  CZ  . TYR   AA 13 29  ? 76.003  -168.348 62.412  1.00 107.66 ? 16  TYR   a CZ  1 
ATOM   46053 O  OH  . TYR   AA 13 29  ? 75.561  -169.460 63.068  1.00 105.41 ? 16  TYR   a OH  1 
ATOM   46054 N  N   . ASP   AA 13 30  ? 79.962  -166.088 59.271  1.00 109.94 ? 17  ASP   a N   1 
ATOM   46055 C  CA  . ASP   AA 13 30  ? 81.163  -166.914 58.958  1.00 112.61 ? 17  ASP   a CA  1 
ATOM   46056 C  C   . ASP   AA 13 30  ? 80.825  -168.414 58.981  1.00 111.69 ? 17  ASP   a C   1 
ATOM   46057 O  O   . ASP   AA 13 30  ? 81.304  -169.123 58.075  1.00 113.81 ? 17  ASP   a O   1 
ATOM   46058 C  CB  . ASP   AA 13 30  ? 82.340  -166.573 59.881  1.00 114.83 ? 17  ASP   a CB  1 
ATOM   46059 C  CG  . ASP   AA 13 30  ? 82.056  -166.674 61.373  1.00 115.42 ? 17  ASP   a CG  1 
ATOM   46060 O  OD1 . ASP   AA 13 30  ? 81.016  -167.253 61.740  1.00 120.39 ? 17  ASP   a OD1 1 
ATOM   46061 O  OD2 . ASP   AA 13 30  ? 82.880  -166.161 62.159  1.00 113.89 ? 17  ASP   a OD2 1 
ATOM   46062 N  N   . ASN   AA 13 31  ? 80.033  -168.879 59.956  1.00 111.05 ? 18  ASN   a N   1 
ATOM   46063 C  CA  . ASN   AA 13 31  ? 79.816  -170.327 60.238  1.00 112.51 ? 18  ASN   a CA  1 
ATOM   46064 C  C   . ASN   AA 13 31  ? 78.404  -170.792 59.861  1.00 111.69 ? 18  ASN   a C   1 
ATOM   46065 O  O   . ASN   AA 13 31  ? 78.195  -172.021 59.857  1.00 117.29 ? 18  ASN   a O   1 
ATOM   46066 C  CB  . ASN   AA 13 31  ? 80.076  -170.662 61.709  1.00 113.39 ? 18  ASN   a CB  1 
ATOM   46067 C  CG  . ASN   AA 13 31  ? 81.518  -170.480 62.136  1.00 115.87 ? 18  ASN   a CG  1 
ATOM   46068 O  OD1 . ASN   AA 13 31  ? 81.787  -170.323 63.324  1.00 120.40 ? 18  ASN   a OD1 1 
ATOM   46069 N  ND2 . ASN   AA 13 31  ? 82.454  -170.508 61.199  1.00 116.34 ? 18  ASN   a ND2 1 
ATOM   46070 N  N   . GLY   AA 13 32  ? 77.466  -169.890 59.560  1.00 104.99 ? 19  GLY   a N   1 
ATOM   46071 C  CA  . GLY   AA 13 32  ? 76.090  -170.300 59.215  1.00 101.69 ? 19  GLY   a CA  1 
ATOM   46072 C  C   . GLY   AA 13 32  ? 75.206  -169.142 58.799  1.00 99.15  ? 19  GLY   a C   1 
ATOM   46073 O  O   . GLY   AA 13 32  ? 75.732  -168.171 58.222  1.00 100.06 ? 19  GLY   a O   1 
ATOM   46074 N  N   . VAL   AA 13 33  ? 73.903  -169.257 59.078  1.00 96.97  ? 20  VAL   a N   1 
ATOM   46075 C  CA  . VAL   AA 13 33  ? 72.851  -168.277 58.675  1.00 97.21  ? 20  VAL   a CA  1 
ATOM   46076 C  C   . VAL   AA 13 33  ? 71.945  -167.988 59.875  1.00 96.97  ? 20  VAL   a C   1 
ATOM   46077 O  O   . VAL   AA 13 33  ? 71.754  -168.893 60.711  1.00 97.00  ? 20  VAL   a O   1 
ATOM   46078 C  CB  . VAL   AA 13 33  ? 72.037  -168.789 57.470  1.00 99.31  ? 20  VAL   a CB  1 
ATOM   46079 C  CG1 . VAL   AA 13 33  ? 72.888  -168.862 56.212  1.00 101.83 ? 20  VAL   a CG1 1 
ATOM   46080 C  CG2 . VAL   AA 13 33  ? 71.379  -170.133 57.746  1.00 99.43  ? 20  VAL   a CG2 1 
ATOM   46081 N  N   . ILE   AA 13 34  ? 71.425  -166.759 59.947  1.00 96.18  ? 21  ILE   a N   1 
ATOM   46082 C  CA  . ILE   AA 13 34  ? 70.380  -166.326 60.921  1.00 93.13  ? 21  ILE   a CA  1 
ATOM   46083 C  C   . ILE   AA 13 34  ? 69.149  -165.892 60.123  1.00 90.70  ? 21  ILE   a C   1 
ATOM   46084 O  O   . ILE   AA 13 34  ? 69.327  -165.322 59.028  1.00 87.85  ? 21  ILE   a O   1 
ATOM   46085 C  CB  . ILE   AA 13 34  ? 70.895  -165.200 61.841  1.00 93.73  ? 21  ILE   a CB  1 
ATOM   46086 C  CG1 . ILE   AA 13 34  ? 72.208  -165.599 62.520  1.00 96.78  ? 21  ILE   a CG1 1 
ATOM   46087 C  CG2 . ILE   AA 13 34  ? 69.826  -164.805 62.852  1.00 92.46  ? 21  ILE   a CG2 1 
ATOM   46088 C  CD1 . ILE   AA 13 34  ? 72.815  -164.529 63.398  1.00 97.58  ? 21  ILE   a CD1 1 
ATOM   46089 N  N   . ILE   AA 13 35  ? 67.958  -166.164 60.659  1.00 86.48  ? 22  ILE   a N   1 
ATOM   46090 C  CA  . ILE   AA 13 35  ? 66.653  -165.778 60.049  1.00 85.30  ? 22  ILE   a CA  1 
ATOM   46091 C  C   . ILE   AA 13 35  ? 65.670  -165.445 61.176  1.00 85.46  ? 22  ILE   a C   1 
ATOM   46092 O  O   . ILE   AA 13 35  ? 65.719  -166.120 62.219  1.00 86.67  ? 22  ILE   a O   1 
ATOM   46093 C  CB  . ILE   AA 13 35  ? 66.131  -166.889 59.116  1.00 84.47  ? 22  ILE   a CB  1 
ATOM   46094 C  CG1 . ILE   AA 13 35  ? 64.805  -166.497 58.461  1.00 84.05  ? 22  ILE   a CG1 1 
ATOM   46095 C  CG2 . ILE   AA 13 35  ? 66.030  -168.216 59.852  1.00 85.69  ? 22  ILE   a CG2 1 
ATOM   46096 C  CD1 . ILE   AA 13 35  ? 64.425  -167.355 57.279  1.00 83.74  ? 22  ILE   a CD1 1 
ATOM   46097 N  N   . ALA   AA 13 36  ? 64.827  -164.430 60.968  1.00 84.81  ? 23  ALA   a N   1 
ATOM   46098 C  CA  . ALA   AA 13 36  ? 63.850  -163.926 61.960  1.00 85.33  ? 23  ALA   a CA  1 
ATOM   46099 C  C   . ALA   AA 13 36  ? 62.557  -163.494 61.265  1.00 83.34  ? 23  ALA   a C   1 
ATOM   46100 O  O   . ALA   AA 13 36  ? 62.620  -163.079 60.092  1.00 78.95  ? 23  ALA   a O   1 
ATOM   46101 C  CB  . ALA   AA 13 36  ? 64.450  -162.783 62.735  1.00 89.53  ? 23  ALA   a CB  1 
ATOM   46102 N  N   . ALA   AA 13 37  ? 61.440  -163.580 61.993  1.00 82.93  ? 24  ALA   a N   1 
ATOM   46103 C  CA  . ALA   AA 13 37  ? 60.089  -163.155 61.561  1.00 85.54  ? 24  ALA   a CA  1 
ATOM   46104 C  C   . ALA   AA 13 37  ? 59.198  -162.976 62.793  1.00 85.42  ? 24  ALA   a C   1 
ATOM   46105 O  O   . ALA   AA 13 37  ? 59.232  -163.859 63.675  1.00 84.79  ? 24  ALA   a O   1 
ATOM   46106 C  CB  . ALA   AA 13 37  ? 59.507  -164.173 60.613  1.00 87.81  ? 24  ALA   a CB  1 
ATOM   46107 N  N   . ASP   AA 13 38  ? 58.424  -161.886 62.837  1.00 87.41  ? 25  ASP   a N   1 
ATOM   46108 C  CA  . ASP   AA 13 38  ? 57.534  -161.552 63.982  1.00 87.52  ? 25  ASP   a CA  1 
ATOM   46109 C  C   . ASP   AA 13 38  ? 56.383  -162.564 64.028  1.00 84.55  ? 25  ASP   a C   1 
ATOM   46110 O  O   . ASP   AA 13 38  ? 56.222  -163.329 63.059  1.00 83.57  ? 25  ASP   a O   1 
ATOM   46111 C  CB  . ASP   AA 13 38  ? 57.076  -160.089 63.947  1.00 92.27  ? 25  ASP   a CB  1 
ATOM   46112 C  CG  . ASP   AA 13 38  ? 56.181  -159.702 62.780  1.00 96.67  ? 25  ASP   a CG  1 
ATOM   46113 O  OD1 . ASP   AA 13 38  ? 55.285  -160.498 62.421  1.00 100.81 ? 25  ASP   a OD1 1 
ATOM   46114 O  OD2 . ASP   AA 13 38  ? 56.387  -158.596 62.242  1.00 98.38  ? 25  ASP   a OD2 1 
ATOM   46115 N  N   . ASN   AA 13 39  ? 55.618  -162.555 65.122  1.00 83.65  ? 26  ASN   a N   1 
ATOM   46116 C  CA  . ASN   AA 13 39  ? 54.621  -163.603 65.460  1.00 87.83  ? 26  ASN   a CA  1 
ATOM   46117 C  C   . ASN   AA 13 39  ? 53.201  -163.071 65.243  1.00 88.18  ? 26  ASN   a C   1 
ATOM   46118 O  O   . ASN   AA 13 39  ? 52.322  -163.413 66.055  1.00 90.73  ? 26  ASN   a O   1 
ATOM   46119 C  CB  . ASN   AA 13 39  ? 54.813  -164.090 66.899  1.00 90.28  ? 26  ASN   a CB  1 
ATOM   46120 C  CG  . ASN   AA 13 39  ? 56.213  -164.605 67.163  1.00 93.39  ? 26  ASN   a CG  1 
ATOM   46121 O  OD1 . ASN   AA 13 39  ? 56.834  -165.207 66.287  1.00 94.80  ? 26  ASN   a OD1 1 
ATOM   46122 N  ND2 . ASN   AA 13 39  ? 56.718  -164.375 68.365  1.00 94.62  ? 26  ASN   a ND2 1 
ATOM   46123 N  N   . LEU   AA 13 40  ? 52.978  -162.290 64.180  1.00 89.23  ? 27  LEU   a N   1 
ATOM   46124 C  CA  . LEU   AA 13 40  ? 51.687  -161.591 63.936  1.00 89.89  ? 27  LEU   a CA  1 
ATOM   46125 C  C   . LEU   AA 13 40  ? 50.985  -162.185 62.712  1.00 87.61  ? 27  LEU   a C   1 
ATOM   46126 O  O   . LEU   AA 13 40  ? 51.657  -162.400 61.683  1.00 84.78  ? 27  LEU   a O   1 
ATOM   46127 C  CB  . LEU   AA 13 40  ? 51.941  -160.093 63.745  1.00 93.22  ? 27  LEU   a CB  1 
ATOM   46128 C  CG  . LEU   AA 13 40  ? 50.694  -159.218 63.597  1.00 96.05  ? 27  LEU   a CG  1 
ATOM   46129 C  CD1 . LEU   AA 13 40  ? 49.742  -159.382 64.775  1.00 93.49  ? 27  LEU   a CD1 1 
ATOM   46130 C  CD2 . LEU   AA 13 40  ? 51.084  -157.756 63.442  1.00 98.61  ? 27  LEU   a CD2 1 
ATOM   46131 N  N   . GLY   AA 13 41  ? 49.678  -162.428 62.849  1.00 87.50  ? 28  GLY   a N   1 
ATOM   46132 C  CA  . GLY   AA 13 41  ? 48.746  -162.743 61.752  1.00 87.59  ? 28  GLY   a CA  1 
ATOM   46133 C  C   . GLY   AA 13 41  ? 47.771  -161.599 61.544  1.00 87.68  ? 28  GLY   a C   1 
ATOM   46134 O  O   . GLY   AA 13 41  ? 46.757  -161.547 62.268  1.00 94.71  ? 28  GLY   a O   1 
ATOM   46135 N  N   . SER   AA 13 42  ? 48.084  -160.695 60.611  1.00 85.62  ? 29  SER   a N   1 
ATOM   46136 C  CA  . SER   AA 13 42  ? 47.275  -159.495 60.275  1.00 83.82  ? 29  SER   a CA  1 
ATOM   46137 C  C   . SER   AA 13 42  ? 46.050  -159.893 59.446  1.00 80.62  ? 29  SER   a C   1 
ATOM   46138 O  O   . SER   AA 13 42  ? 46.175  -160.796 58.609  1.00 80.61  ? 29  SER   a O   1 
ATOM   46139 C  CB  . SER   AA 13 42  ? 48.112  -158.486 59.543  1.00 83.40  ? 29  SER   a CB  1 
ATOM   46140 O  OG  . SER   AA 13 42  ? 49.217  -158.080 60.336  1.00 84.25  ? 29  SER   a OG  1 
ATOM   46141 N  N   . TYR   AA 13 43  ? 44.918  -159.223 59.675  1.00 81.43  ? 30  TYR   a N   1 
ATOM   46142 C  CA  . TYR   AA 13 43  ? 43.654  -159.356 58.904  1.00 84.34  ? 30  TYR   a CA  1 
ATOM   46143 C  C   . TYR   AA 13 43  ? 43.315  -157.971 58.342  1.00 84.62  ? 30  TYR   a C   1 
ATOM   46144 O  O   . TYR   AA 13 43  ? 42.470  -157.265 58.921  1.00 89.86  ? 30  TYR   a O   1 
ATOM   46145 C  CB  . TYR   AA 13 43  ? 42.558  -159.935 59.807  1.00 84.62  ? 30  TYR   a CB  1 
ATOM   46146 C  CG  . TYR   AA 13 43  ? 41.233  -160.220 59.143  1.00 85.74  ? 30  TYR   a CG  1 
ATOM   46147 C  CD1 . TYR   AA 13 43  ? 40.987  -161.436 58.527  1.00 87.23  ? 30  TYR   a CD1 1 
ATOM   46148 C  CD2 . TYR   AA 13 43  ? 40.205  -159.292 59.167  1.00 84.85  ? 30  TYR   a CD2 1 
ATOM   46149 C  CE1 . TYR   AA 13 43  ? 39.768  -161.715 57.931  1.00 88.35  ? 30  TYR   a CE1 1 
ATOM   46150 C  CE2 . TYR   AA 13 43  ? 38.979  -159.553 58.577  1.00 86.12  ? 30  TYR   a CE2 1 
ATOM   46151 C  CZ  . TYR   AA 13 43  ? 38.760  -160.768 57.954  1.00 86.14  ? 30  TYR   a CZ  1 
ATOM   46152 O  OH  . TYR   AA 13 43  ? 37.554  -161.025 57.369  1.00 91.11  ? 30  TYR   a OH  1 
ATOM   46153 N  N   . GLY   AA 13 44  ? 43.996  -157.574 57.264  1.00 84.25  ? 31  GLY   a N   1 
ATOM   46154 C  CA  . GLY   AA 13 44  ? 43.963  -156.190 56.752  1.00 85.74  ? 31  GLY   a CA  1 
ATOM   46155 C  C   . GLY   AA 13 44  ? 44.655  -155.245 57.720  1.00 87.34  ? 31  GLY   a C   1 
ATOM   46156 O  O   . GLY   AA 13 44  ? 45.857  -155.455 57.983  1.00 82.55  ? 31  GLY   a O   1 
ATOM   46157 N  N   . SER   AA 13 45  ? 43.923  -154.261 58.258  1.00 90.73  ? 32  SER   a N   1 
ATOM   46158 C  CA  . SER   AA 13 45  ? 44.432  -153.275 59.250  1.00 92.38  ? 32  SER   a CA  1 
ATOM   46159 C  C   . SER   AA 13 45  ? 44.279  -153.821 60.676  1.00 91.66  ? 32  SER   a C   1 
ATOM   46160 O  O   . SER   AA 13 45  ? 44.967  -153.298 61.572  1.00 98.39  ? 32  SER   a O   1 
ATOM   46161 C  CB  . SER   AA 13 45  ? 43.760  -151.933 59.099  1.00 93.30  ? 32  SER   a CB  1 
ATOM   46162 O  OG  . SER   AA 13 45  ? 42.407  -151.991 59.520  1.00 98.56  ? 32  SER   a OG  1 
ATOM   46163 N  N   . LEU   AA 13 46  ? 43.415  -154.824 60.878  1.00 90.59  ? 33  LEU   a N   1 
ATOM   46164 C  CA  . LEU   AA 13 46  ? 43.196  -155.486 62.194  1.00 85.61  ? 33  LEU   a CA  1 
ATOM   46165 C  C   . LEU   AA 13 46  ? 44.370  -156.429 62.473  1.00 85.05  ? 33  LEU   a C   1 
ATOM   46166 O  O   . LEU   AA 13 46  ? 44.593  -157.339 61.659  1.00 83.77  ? 33  LEU   a O   1 
ATOM   46167 C  CB  . LEU   AA 13 46  ? 41.864  -156.245 62.175  1.00 83.86  ? 33  LEU   a CB  1 
ATOM   46168 C  CG  . LEU   AA 13 46  ? 41.620  -157.190 63.350  1.00 83.56  ? 33  LEU   a CG  1 
ATOM   46169 C  CD1 . LEU   AA 13 46  ? 41.613  -156.439 64.672  1.00 83.43  ? 33  LEU   a CD1 1 
ATOM   46170 C  CD2 . LEU   AA 13 46  ? 40.318  -157.955 63.165  1.00 84.76  ? 33  LEU   a CD2 1 
ATOM   46171 N  N   . LEU   AA 13 47  ? 45.085  -156.210 63.580  1.00 84.84  ? 34  LEU   a N   1 
ATOM   46172 C  CA  . LEU   AA 13 47  ? 46.224  -157.058 64.029  1.00 87.95  ? 34  LEU   a CA  1 
ATOM   46173 C  C   . LEU   AA 13 47  ? 45.643  -158.272 64.769  1.00 90.73  ? 34  LEU   a C   1 
ATOM   46174 O  O   . LEU   AA 13 47  ? 45.646  -158.272 66.016  1.00 88.63  ? 34  LEU   a O   1 
ATOM   46175 C  CB  . LEU   AA 13 47  ? 47.157  -156.229 64.922  1.00 87.81  ? 34  LEU   a CB  1 
ATOM   46176 C  CG  . LEU   AA 13 47  ? 47.584  -154.865 64.378  1.00 90.21  ? 34  LEU   a CG  1 
ATOM   46177 C  CD1 . LEU   AA 13 47  ? 48.413  -154.108 65.406  1.00 91.15  ? 34  LEU   a CD1 1 
ATOM   46178 C  CD2 . LEU   AA 13 47  ? 48.349  -154.993 63.069  1.00 92.30  ? 34  LEU   a CD2 1 
ATOM   46179 N  N   . ARG   AA 13 48  ? 45.159  -159.265 64.016  1.00 92.66  ? 35  ARG   a N   1 
ATOM   46180 C  CA  . ARG   AA 13 48  ? 44.166  -160.270 64.494  1.00 97.43  ? 35  ARG   a CA  1 
ATOM   46181 C  C   . ARG   AA 13 48  ? 44.821  -161.303 65.427  1.00 96.47  ? 35  ARG   a C   1 
ATOM   46182 O  O   . ARG   AA 13 48  ? 44.303  -161.475 66.551  1.00 97.27  ? 35  ARG   a O   1 
ATOM   46183 C  CB  . ARG   AA 13 48  ? 43.452  -160.929 63.305  1.00 98.39  ? 35  ARG   a CB  1 
ATOM   46184 C  CG  . ARG   AA 13 48  ? 42.434  -161.996 63.690  1.00 103.23 ? 35  ARG   a CG  1 
ATOM   46185 C  CD  . ARG   AA 13 48  ? 41.317  -161.479 64.583  1.00 108.25 ? 35  ARG   a CD  1 
ATOM   46186 N  NE  . ARG   AA 13 48  ? 40.510  -162.534 65.197  1.00 114.44 ? 35  ARG   a NE  1 
ATOM   46187 C  CZ  . ARG   AA 13 48  ? 40.760  -163.125 66.371  1.00 117.64 ? 35  ARG   a CZ  1 
ATOM   46188 N  NH1 . ARG   AA 13 48  ? 41.817  -162.787 67.094  1.00 118.77 ? 35  ARG   a NH1 1 
ATOM   46189 N  NH2 . ARG   AA 13 48  ? 39.943  -164.065 66.820  1.00 116.39 ? 35  ARG   a NH2 1 
ATOM   46190 N  N   . PHE   AA 13 49  ? 45.895  -161.973 64.989  1.00 93.29  ? 36  PHE   a N   1 
ATOM   46191 C  CA  . PHE   AA 13 49  ? 46.499  -163.147 65.678  1.00 92.43  ? 36  PHE   a CA  1 
ATOM   46192 C  C   . PHE   AA 13 49  ? 47.931  -162.834 66.118  1.00 94.98  ? 36  PHE   a C   1 
ATOM   46193 O  O   . PHE   AA 13 49  ? 48.695  -162.309 65.294  1.00 95.69  ? 36  PHE   a O   1 
ATOM   46194 C  CB  . PHE   AA 13 49  ? 46.480  -164.367 64.756  1.00 89.16  ? 36  PHE   a CB  1 
ATOM   46195 C  CG  . PHE   AA 13 49  ? 45.104  -164.734 64.264  1.00 87.02  ? 36  PHE   a CG  1 
ATOM   46196 C  CD1 . PHE   AA 13 49  ? 44.115  -165.115 65.158  1.00 85.77  ? 36  PHE   a CD1 1 
ATOM   46197 C  CD2 . PHE   AA 13 49  ? 44.794  -164.688 62.913  1.00 83.94  ? 36  PHE   a CD2 1 
ATOM   46198 C  CE1 . PHE   AA 13 49  ? 42.845  -165.443 64.712  1.00 84.83  ? 36  PHE   a CE1 1 
ATOM   46199 C  CE2 . PHE   AA 13 49  ? 43.524  -165.019 62.469  1.00 83.28  ? 36  PHE   a CE2 1 
ATOM   46200 C  CZ  . PHE   AA 13 49  ? 42.552  -165.395 63.368  1.00 83.97  ? 36  PHE   a CZ  1 
ATOM   46201 N  N   . ASN   AA 13 50  ? 48.282  -163.191 67.360  1.00 99.83  ? 37  ASN   a N   1 
ATOM   46202 C  CA  . ASN   AA 13 50  ? 49.559  -162.797 68.019  1.00 102.76 ? 37  ASN   a CA  1 
ATOM   46203 C  C   . ASN   AA 13 50  ? 50.423  -164.019 68.371  1.00 104.25 ? 37  ASN   a C   1 
ATOM   46204 O  O   . ASN   AA 13 50  ? 51.560  -163.800 68.835  1.00 111.72 ? 37  ASN   a O   1 
ATOM   46205 C  CB  . ASN   AA 13 50  ? 49.293  -161.941 69.262  1.00 105.89 ? 37  ASN   a CB  1 
ATOM   46206 C  CG  . ASN   AA 13 50  ? 49.399  -160.453 68.992  1.00 107.44 ? 37  ASN   a CG  1 
ATOM   46207 O  OD1 . ASN   AA 13 50  ? 48.446  -159.706 69.212  1.00 104.40 ? 37  ASN   a OD1 1 
ATOM   46208 N  ND2 . ASN   AA 13 50  ? 50.555  -160.015 68.515  1.00 107.48 ? 37  ASN   a ND2 1 
ATOM   46209 N  N   . GLY   AA 13 51  ? 49.935  -165.246 68.165  1.00 100.90 ? 38  GLY   a N   1 
ATOM   46210 C  CA  . GLY   AA 13 51  ? 50.683  -166.473 68.503  1.00 102.47 ? 38  GLY   a CA  1 
ATOM   46211 C  C   . GLY   AA 13 51  ? 51.079  -167.260 67.267  1.00 104.06 ? 38  GLY   a C   1 
ATOM   46212 O  O   . GLY   AA 13 51  ? 51.118  -168.502 67.358  1.00 111.76 ? 38  GLY   a O   1 
ATOM   46213 N  N   . VAL   AA 13 52  ? 51.376  -166.571 66.159  1.00 99.81  ? 39  VAL   a N   1 
ATOM   46214 C  CA  . VAL   AA 13 52  ? 51.643  -167.193 64.826  1.00 95.51  ? 39  VAL   a CA  1 
ATOM   46215 C  C   . VAL   AA 13 52  ? 53.154  -167.387 64.658  1.00 94.88  ? 39  VAL   a C   1 
ATOM   46216 O  O   . VAL   AA 13 52  ? 53.884  -166.382 64.681  1.00 94.22  ? 39  VAL   a O   1 
ATOM   46217 C  CB  . VAL   AA 13 52  ? 51.057  -166.347 63.678  1.00 91.70  ? 39  VAL   a CB  1 
ATOM   46218 C  CG1 . VAL   AA 13 52  ? 51.298  -166.989 62.319  1.00 90.02  ? 39  VAL   a CG1 1 
ATOM   46219 C  CG2 . VAL   AA 13 52  ? 49.573  -166.079 63.881  1.00 92.10  ? 39  VAL   a CG2 1 
ATOM   46220 N  N   . GLU   AA 13 53  ? 53.596  -168.634 64.485  1.00 91.44  ? 40  GLU   a N   1 
ATOM   46221 C  CA  . GLU   AA 13 53  ? 55.015  -168.975 64.207  1.00 92.01  ? 40  GLU   a CA  1 
ATOM   46222 C  C   . GLU   AA 13 53  ? 55.196  -169.066 62.690  1.00 90.27  ? 40  GLU   a C   1 
ATOM   46223 O  O   . GLU   AA 13 53  ? 54.568  -169.944 62.077  1.00 87.29  ? 40  GLU   a O   1 
ATOM   46224 C  CB  . GLU   AA 13 53  ? 55.407  -170.279 64.901  1.00 93.16  ? 40  GLU   a CB  1 
ATOM   46225 C  CG  . GLU   AA 13 53  ? 56.867  -170.643 64.705  1.00 97.01  ? 40  GLU   a CG  1 
ATOM   46226 C  CD  . GLU   AA 13 53  ? 57.847  -169.563 65.137  1.00 97.96  ? 40  GLU   a CD  1 
ATOM   46227 O  OE1 . GLU   AA 13 53  ? 58.403  -168.875 64.253  1.00 98.38  ? 40  GLU   a OE1 1 
ATOM   46228 O  OE2 . GLU   AA 13 53  ? 58.049  -169.408 66.359  1.00 99.44  ? 40  GLU   a OE2 1 
ATOM   46229 N  N   . ARG   AA 13 54  ? 56.011  -168.176 62.119  1.00 92.17  ? 41  ARG   a N   1 
ATOM   46230 C  CA  . ARG   AA 13 54  ? 56.211  -168.050 60.649  1.00 94.43  ? 41  ARG   a CA  1 
ATOM   46231 C  C   . ARG   AA 13 54  ? 57.587  -168.597 60.236  1.00 94.30  ? 41  ARG   a C   1 
ATOM   46232 O  O   . ARG   AA 13 54  ? 57.856  -168.617 59.018  1.00 92.92  ? 41  ARG   a O   1 
ATOM   46233 C  CB  . ARG   AA 13 54  ? 56.015  -166.589 60.229  1.00 94.25  ? 41  ARG   a CB  1 
ATOM   46234 C  CG  . ARG   AA 13 54  ? 54.670  -166.011 60.647  1.00 94.40  ? 41  ARG   a CG  1 
ATOM   46235 C  CD  . ARG   AA 13 54  ? 54.277  -164.758 59.885  1.00 94.02  ? 41  ARG   a CD  1 
ATOM   46236 N  NE  . ARG   AA 13 54  ? 55.059  -163.587 60.275  1.00 93.37  ? 41  ARG   a NE  1 
ATOM   46237 C  CZ  . ARG   AA 13 54  ? 56.007  -163.004 59.542  1.00 91.89  ? 41  ARG   a CZ  1 
ATOM   46238 N  NH1 . ARG   AA 13 54  ? 56.325  -163.464 58.343  1.00 90.74  ? 41  ARG   a NH1 1 
ATOM   46239 N  NH2 . ARG   AA 13 54  ? 56.640  -161.945 60.017  1.00 94.47  ? 41  ARG   a NH2 1 
ATOM   46240 N  N   . LEU   AA 13 55  ? 58.421  -169.023 61.195  1.00 95.08  ? 42  LEU   a N   1 
ATOM   46241 C  CA  . LEU   AA 13 55  ? 59.649  -169.830 60.938  1.00 97.74  ? 42  LEU   a CA  1 
ATOM   46242 C  C   . LEU   AA 13 55  ? 59.327  -171.308 61.191  1.00 99.35  ? 42  LEU   a C   1 
ATOM   46243 O  O   . LEU   AA 13 55  ? 58.894  -171.628 62.319  1.00 101.83 ? 42  LEU   a O   1 
ATOM   46244 C  CB  . LEU   AA 13 55  ? 60.787  -169.388 61.864  1.00 95.08  ? 42  LEU   a CB  1 
ATOM   46245 C  CG  . LEU   AA 13 55  ? 61.191  -167.918 61.810  1.00 93.48  ? 42  LEU   a CG  1 
ATOM   46246 C  CD1 . LEU   AA 13 55  ? 62.195  -167.613 62.909  1.00 93.72  ? 42  LEU   a CD1 1 
ATOM   46247 C  CD2 . LEU   AA 13 55  ? 61.764  -167.549 60.450  1.00 94.04  ? 42  LEU   a CD2 1 
ATOM   46248 N  N   . ILE   AA 13 56  ? 59.544  -172.180 60.201  1.00 99.43  ? 43  ILE   a N   1 
ATOM   46249 C  CA  . ILE   AA 13 56  ? 59.295  -173.646 60.342  1.00 97.64  ? 43  ILE   a CA  1 
ATOM   46250 C  C   . ILE   AA 13 56  ? 60.588  -174.404 60.055  1.00 92.41  ? 43  ILE   a C   1 
ATOM   46251 O  O   . ILE   AA 13 56  ? 61.120  -174.344 58.950  1.00 85.66  ? 43  ILE   a O   1 
ATOM   46252 C  CB  . ILE   AA 13 56  ? 58.110  -174.110 59.470  1.00 100.64 ? 43  ILE   a CB  1 
ATOM   46253 C  CG1 . ILE   AA 13 56  ? 58.345  -173.873 57.973  1.00 103.84 ? 43  ILE   a CG1 1 
ATOM   46254 C  CG2 . ILE   AA 13 56  ? 56.823  -173.478 59.984  1.00 102.08 ? 43  ILE   a CG2 1 
ATOM   46255 C  CD1 . ILE   AA 13 56  ? 57.261  -173.086 57.263  1.00 106.61 ? 43  ILE   a CD1 1 
ATOM   46256 N  N   . PRO   AA 13 57  ? 61.142  -175.116 61.063  1.00 93.92  ? 44  PRO   a N   1 
ATOM   46257 C  CA  . PRO   AA 13 57  ? 62.343  -175.925 60.875  1.00 95.36  ? 44  PRO   a CA  1 
ATOM   46258 C  C   . PRO   AA 13 57  ? 62.030  -177.223 60.115  1.00 96.25  ? 44  PRO   a C   1 
ATOM   46259 O  O   . PRO   AA 13 57  ? 61.000  -177.822 60.379  1.00 95.31  ? 44  PRO   a O   1 
ATOM   46260 C  CB  . PRO   AA 13 57  ? 62.820  -176.253 62.301  1.00 96.79  ? 44  PRO   a CB  1 
ATOM   46261 C  CG  . PRO   AA 13 57  ? 61.931  -175.433 63.224  1.00 97.18  ? 44  PRO   a CG  1 
ATOM   46262 C  CD  . PRO   AA 13 57  ? 60.658  -175.176 62.449  1.00 95.48  ? 44  PRO   a CD  1 
ATOM   46263 N  N   . VAL   AA 13 58  ? 62.920  -177.611 59.196  1.00 96.38  ? 45  VAL   a N   1 
ATOM   46264 C  CA  . VAL   AA 13 58  ? 62.890  -178.920 58.478  1.00 96.93  ? 45  VAL   a CA  1 
ATOM   46265 C  C   . VAL   AA 13 58  ? 64.176  -179.672 58.834  1.00 96.39  ? 45  VAL   a C   1 
ATOM   46266 O  O   . VAL   AA 13 58  ? 65.255  -179.271 58.351  1.00 95.07  ? 45  VAL   a O   1 
ATOM   46267 C  CB  . VAL   AA 13 58  ? 62.733  -178.740 56.955  1.00 95.06  ? 45  VAL   a CB  1 
ATOM   46268 C  CG1 . VAL   AA 13 58  ? 62.564  -180.076 56.246  1.00 96.39  ? 45  VAL   a CG1 1 
ATOM   46269 C  CG2 . VAL   AA 13 58  ? 61.578  -177.814 56.615  1.00 93.46  ? 45  VAL   a CG2 1 
ATOM   46270 N  N   . GLY   AA 13 59  ? 64.060  -180.713 59.661  1.00 98.39  ? 46  GLY   a N   1 
ATOM   46271 C  CA  . GLY   AA 13 59  ? 65.213  -181.421 60.245  1.00 98.81  ? 46  GLY   a CA  1 
ATOM   46272 C  C   . GLY   AA 13 59  ? 65.973  -180.512 61.194  1.00 100.31 ? 46  GLY   a C   1 
ATOM   46273 O  O   . GLY   AA 13 59  ? 65.329  -179.641 61.818  1.00 94.44  ? 46  GLY   a O   1 
ATOM   46274 N  N   . ASP   AA 13 60  ? 67.295  -180.685 61.275  1.00 104.16 ? 47  ASP   a N   1 
ATOM   46275 C  CA  . ASP   AA 13 60  ? 68.181  -179.962 62.227  1.00 107.66 ? 47  ASP   a CA  1 
ATOM   46276 C  C   . ASP   AA 13 60  ? 69.124  -179.018 61.466  1.00 106.22 ? 47  ASP   a C   1 
ATOM   46277 O  O   . ASP   AA 13 60  ? 70.036  -178.468 62.114  1.00 112.43 ? 47  ASP   a O   1 
ATOM   46278 C  CB  . ASP   AA 13 60  ? 68.973  -180.952 63.087  1.00 113.63 ? 47  ASP   a CB  1 
ATOM   46279 C  CG  . ASP   AA 13 60  ? 69.922  -181.838 62.295  1.00 118.08 ? 47  ASP   a CG  1 
ATOM   46280 O  OD1 . ASP   AA 13 60  ? 69.726  -181.962 61.067  1.00 118.86 ? 47  ASP   a OD1 1 
ATOM   46281 O  OD2 . ASP   AA 13 60  ? 70.850  -182.398 62.910  1.00 129.52 ? 47  ASP   a OD2 1 
ATOM   46282 N  N   . ASN   AA 13 61  ? 68.916  -178.831 60.155  1.00 102.35 ? 48  ASN   a N   1 
ATOM   46283 C  CA  . ASN   AA 13 61  ? 69.880  -178.127 59.260  1.00 99.61  ? 48  ASN   a CA  1 
ATOM   46284 C  C   . ASN   AA 13 61  ? 69.196  -177.080 58.365  1.00 95.00  ? 48  ASN   a C   1 
ATOM   46285 O  O   . ASN   AA 13 61  ? 69.923  -176.443 57.576  1.00 88.52  ? 48  ASN   a O   1 
ATOM   46286 C  CB  . ASN   AA 13 61  ? 70.701  -179.119 58.425  1.00 100.32 ? 48  ASN   a CB  1 
ATOM   46287 C  CG  . ASN   AA 13 61  ? 69.955  -179.833 57.311  1.00 99.90  ? 48  ASN   a CG  1 
ATOM   46288 O  OD1 . ASN   AA 13 61  ? 70.593  -180.406 56.432  1.00 102.63 ? 48  ASN   a OD1 1 
ATOM   46289 N  ND2 . ASN   AA 13 61  ? 68.630  -179.837 57.318  1.00 98.09  ? 48  ASN   a ND2 1 
ATOM   46290 N  N   . THR   AA 13 62  ? 67.875  -176.893 58.474  1.00 95.55  ? 49  THR   a N   1 
ATOM   46291 C  CA  . THR   AA 13 62  ? 67.091  -175.957 57.623  1.00 94.12  ? 49  THR   a CA  1 
ATOM   46292 C  C   . THR   AA 13 62  ? 65.999  -175.279 58.454  1.00 93.50  ? 49  THR   a C   1 
ATOM   46293 O  O   . THR   AA 13 62  ? 65.393  -175.957 59.310  1.00 91.14  ? 49  THR   a O   1 
ATOM   46294 C  CB  . THR   AA 13 62  ? 66.442  -176.668 56.427  1.00 94.14  ? 49  THR   a CB  1 
ATOM   46295 O  OG1 . THR   AA 13 62  ? 67.401  -177.535 55.820  1.00 94.16  ? 49  THR   a OG1 1 
ATOM   46296 C  CG2 . THR   AA 13 62  ? 65.913  -175.697 55.393  1.00 94.54  ? 49  THR   a CG2 1 
ATOM   46297 N  N   . VAL   AA 13 63  ? 65.770  -173.988 58.197  1.00 92.53  ? 50  VAL   a N   1 
ATOM   46298 C  CA  . VAL   AA 13 63  ? 64.556  -173.240 58.638  1.00 91.85  ? 50  VAL   a CA  1 
ATOM   46299 C  C   . VAL   AA 13 63  ? 63.983  -172.519 57.415  1.00 89.70  ? 50  VAL   a C   1 
ATOM   46300 O  O   . VAL   AA 13 63  ? 64.756  -171.857 56.695  1.00 90.34  ? 50  VAL   a O   1 
ATOM   46301 C  CB  . VAL   AA 13 63  ? 64.854  -172.264 59.794  1.00 93.86  ? 50  VAL   a CB  1 
ATOM   46302 C  CG1 . VAL   AA 13 63  ? 63.665  -171.359 60.088  1.00 93.81  ? 50  VAL   a CG1 1 
ATOM   46303 C  CG2 . VAL   AA 13 63  ? 65.281  -172.999 61.056  1.00 93.83  ? 50  VAL   a CG2 1 
ATOM   46304 N  N   . VAL   AA 13 64  ? 62.677  -172.672 57.190  1.00 88.91  ? 51  VAL   a N   1 
ATOM   46305 C  CA  . VAL   AA 13 64  ? 61.909  -171.962 56.127  1.00 87.07  ? 51  VAL   a CA  1 
ATOM   46306 C  C   . VAL   AA 13 64  ? 61.123  -170.831 56.797  1.00 86.77  ? 51  VAL   a C   1 
ATOM   46307 O  O   . VAL   AA 13 64  ? 60.282  -171.132 57.669  1.00 89.62  ? 51  VAL   a O   1 
ATOM   46308 C  CB  . VAL   AA 13 64  ? 60.978  -172.924 55.367  1.00 84.58  ? 51  VAL   a CB  1 
ATOM   46309 C  CG1 . VAL   AA 13 64  ? 60.163  -172.203 54.303  1.00 83.65  ? 51  VAL   a CG1 1 
ATOM   46310 C  CG2 . VAL   AA 13 64  ? 61.741  -174.092 54.761  1.00 84.54  ? 51  VAL   a CG2 1 
ATOM   46311 N  N   . GLY   AA 13 65  ? 61.409  -169.584 56.415  1.00 85.17  ? 52  GLY   a N   1 
ATOM   46312 C  CA  . GLY   AA 13 65  ? 60.640  -168.393 56.817  1.00 83.58  ? 52  GLY   a CA  1 
ATOM   46313 C  C   . GLY   AA 13 65  ? 59.642  -168.021 55.736  1.00 82.36  ? 52  GLY   a C   1 
ATOM   46314 O  O   . GLY   AA 13 65  ? 60.042  -168.023 54.552  1.00 79.65  ? 52  GLY   a O   1 
ATOM   46315 N  N   . ILE   AA 13 66  ? 58.392  -167.730 56.115  1.00 84.20  ? 53  ILE   a N   1 
ATOM   46316 C  CA  . ILE   AA 13 66  ? 57.273  -167.464 55.161  1.00 87.07  ? 53  ILE   a CA  1 
ATOM   46317 C  C   . ILE   AA 13 66  ? 56.511  -166.198 55.572  1.00 85.94  ? 53  ILE   a C   1 
ATOM   46318 O  O   . ILE   AA 13 66  ? 56.038  -166.134 56.722  1.00 93.27  ? 53  ILE   a O   1 
ATOM   46319 C  CB  . ILE   AA 13 66  ? 56.326  -168.674 55.073  1.00 87.76  ? 53  ILE   a CB  1 
ATOM   46320 C  CG1 . ILE   AA 13 66  ? 57.087  -169.947 54.693  1.00 90.73  ? 53  ILE   a CG1 1 
ATOM   46321 C  CG2 . ILE   AA 13 66  ? 55.181  -168.375 54.114  1.00 87.97  ? 53  ILE   a CG2 1 
ATOM   46322 C  CD1 . ILE   AA 13 66  ? 56.231  -171.191 54.605  1.00 93.18  ? 53  ILE   a CD1 1 
ATOM   46323 N  N   . SER   AA 13 67  ? 56.371  -165.257 54.634  1.00 85.84  ? 54  SER   a N   1 
ATOM   46324 C  CA  . SER   AA 13 67  ? 55.470  -164.079 54.713  1.00 85.10  ? 54  SER   a CA  1 
ATOM   46325 C  C   . SER   AA 13 67  ? 54.326  -164.259 53.709  1.00 78.35  ? 54  SER   a C   1 
ATOM   46326 O  O   . SER   AA 13 67  ? 54.421  -165.157 52.853  1.00 75.88  ? 54  SER   a O   1 
ATOM   46327 C  CB  . SER   AA 13 67  ? 56.223  -162.795 54.464  1.00 84.91  ? 54  SER   a CB  1 
ATOM   46328 O  OG  . SER   AA 13 67  ? 56.959  -162.858 53.254  1.00 89.67  ? 54  SER   a OG  1 
ATOM   46329 N  N   . GLY   AA 13 68  ? 53.294  -163.420 53.811  1.00 77.71  ? 55  GLY   a N   1 
ATOM   46330 C  CA  . GLY   AA 13 68  ? 52.119  -163.443 52.923  1.00 76.73  ? 55  GLY   a CA  1 
ATOM   46331 C  C   . GLY   AA 13 68  ? 50.979  -164.228 53.538  1.00 75.65  ? 55  GLY   a C   1 
ATOM   46332 O  O   . GLY   AA 13 68  ? 50.925  -164.308 54.777  1.00 72.29  ? 55  GLY   a O   1 
ATOM   46333 N  N   . ASP   AA 13 69  ? 50.109  -164.798 52.701  1.00 78.95  ? 56  ASP   a N   1 
ATOM   46334 C  CA  . ASP   AA 13 69  ? 48.860  -165.475 53.140  1.00 83.11  ? 56  ASP   a CA  1 
ATOM   46335 C  C   . ASP   AA 13 69  ? 49.212  -166.635 54.079  1.00 84.26  ? 56  ASP   a C   1 
ATOM   46336 O  O   . ASP   AA 13 69  ? 50.076  -167.461 53.715  1.00 82.51  ? 56  ASP   a O   1 
ATOM   46337 C  CB  . ASP   AA 13 69  ? 48.010  -165.953 51.961  1.00 85.69  ? 56  ASP   a CB  1 
ATOM   46338 C  CG  . ASP   AA 13 69  ? 46.661  -166.489 52.411  1.00 86.92  ? 56  ASP   a CG  1 
ATOM   46339 O  OD1 . ASP   AA 13 69  ? 45.672  -165.737 52.328  1.00 91.03  ? 56  ASP   a OD1 1 
ATOM   46340 O  OD2 . ASP   AA 13 69  ? 46.616  -167.648 52.864  1.00 94.35  ? 56  ASP   a OD2 1 
ATOM   46341 N  N   . ILE   AA 13 70  ? 48.547  -166.686 55.237  1.00 87.73  ? 57  ILE   a N   1 
ATOM   46342 C  CA  . ILE   AA 13 70  ? 48.829  -167.648 56.343  1.00 87.09  ? 57  ILE   a CA  1 
ATOM   46343 C  C   . ILE   AA 13 70  ? 48.183  -169.000 56.019  1.00 85.14  ? 57  ILE   a C   1 
ATOM   46344 O  O   . ILE   AA 13 70  ? 48.812  -170.020 56.340  1.00 90.12  ? 57  ILE   a O   1 
ATOM   46345 C  CB  . ILE   AA 13 70  ? 48.371  -167.077 57.703  1.00 89.23  ? 57  ILE   a CB  1 
ATOM   46346 C  CG1 . ILE   AA 13 70  ? 49.190  -165.846 58.108  1.00 90.99  ? 57  ILE   a CG1 1 
ATOM   46347 C  CG2 . ILE   AA 13 70  ? 48.393  -168.144 58.790  1.00 89.48  ? 57  ILE   a CG2 1 
ATOM   46348 C  CD1 . ILE   AA 13 70  ? 50.683  -166.093 58.236  1.00 91.84  ? 57  ILE   a CD1 1 
ATOM   46349 N  N   . SER   AA 13 71  ? 46.992  -169.025 55.407  1.00 81.03  ? 58  SER   a N   1 
ATOM   46350 C  CA  . SER   AA 13 71  ? 46.322  -170.287 54.990  1.00 79.53  ? 58  SER   a CA  1 
ATOM   46351 C  C   . SER   AA 13 71  ? 47.238  -171.040 54.016  1.00 79.51  ? 58  SER   a C   1 
ATOM   46352 O  O   . SER   AA 13 71  ? 47.301  -172.283 54.105  1.00 79.21  ? 58  SER   a O   1 
ATOM   46353 C  CB  . SER   AA 13 71  ? 44.954  -170.060 54.393  1.00 77.55  ? 58  SER   a CB  1 
ATOM   46354 O  OG  . SER   AA 13 71  ? 45.042  -169.724 53.015  1.00 76.75  ? 58  SER   a OG  1 
ATOM   46355 N  N   . ASP   AA 13 72  ? 47.928  -170.310 53.134  1.00 77.99  ? 59  ASP   a N   1 
ATOM   46356 C  CA  . ASP   AA 13 72  ? 48.890  -170.873 52.148  1.00 79.41  ? 59  ASP   a CA  1 
ATOM   46357 C  C   . ASP   AA 13 72  ? 50.184  -171.284 52.866  1.00 78.83  ? 59  ASP   a C   1 
ATOM   46358 O  O   . ASP   AA 13 72  ? 50.813  -172.258 52.418  1.00 77.56  ? 59  ASP   a O   1 
ATOM   46359 C  CB  . ASP   AA 13 72  ? 49.167  -169.893 51.003  1.00 82.02  ? 59  ASP   a CB  1 
ATOM   46360 C  CG  . ASP   AA 13 72  ? 48.028  -169.733 50.003  1.00 83.50  ? 59  ASP   a CG  1 
ATOM   46361 O  OD1 . ASP   AA 13 72  ? 47.172  -170.638 49.927  1.00 86.11  ? 59  ASP   a OD1 1 
ATOM   46362 O  OD2 . ASP   AA 13 72  ? 48.012  -168.704 49.292  1.00 83.56  ? 59  ASP   a OD2 1 
ATOM   46363 N  N   . MET   AA 13 73  ? 50.576  -170.568 53.924  1.00 78.18  ? 60  MET   a N   1 
ATOM   46364 C  CA  . MET   AA 13 73  ? 51.745  -170.917 54.780  1.00 80.05  ? 60  MET   a CA  1 
ATOM   46365 C  C   . MET   AA 13 73  ? 51.493  -172.274 55.453  1.00 79.86  ? 60  MET   a C   1 
ATOM   46366 O  O   . MET   AA 13 73  ? 52.409  -173.119 55.436  1.00 79.34  ? 60  MET   a O   1 
ATOM   46367 C  CB  . MET   AA 13 73  ? 51.983  -169.851 55.855  1.00 82.60  ? 60  MET   a CB  1 
ATOM   46368 C  CG  . MET   AA 13 73  ? 53.243  -170.074 56.675  1.00 85.49  ? 60  MET   a CG  1 
ATOM   46369 S  SD  . MET   AA 13 73  ? 53.398  -168.895 58.044  1.00 88.82  ? 60  MET   a SD  1 
ATOM   46370 C  CE  . MET   AA 13 73  ? 52.503  -169.764 59.331  1.00 89.71  ? 60  MET   a CE  1 
ATOM   46371 N  N   . GLN   AA 13 74  ? 50.298  -172.459 56.025  1.00 77.47  ? 61  GLN   a N   1 
ATOM   46372 C  CA  . GLN   AA 13 74  ? 49.880  -173.686 56.753  1.00 79.32  ? 61  GLN   a CA  1 
ATOM   46373 C  C   . GLN   AA 13 74  ? 49.842  -174.873 55.786  1.00 82.07  ? 61  GLN   a C   1 
ATOM   46374 O  O   . GLN   AA 13 74  ? 50.137  -176.003 56.230  1.00 85.97  ? 61  GLN   a O   1 
ATOM   46375 C  CB  . GLN   AA 13 74  ? 48.522  -173.471 57.419  1.00 76.97  ? 61  GLN   a CB  1 
ATOM   46376 C  CG  . GLN   AA 13 74  ? 48.576  -172.492 58.580  1.00 77.44  ? 61  GLN   a CG  1 
ATOM   46377 C  CD  . GLN   AA 13 74  ? 47.225  -172.283 59.218  1.00 78.47  ? 61  GLN   a CD  1 
ATOM   46378 O  OE1 . GLN   AA 13 74  ? 46.202  -172.754 58.727  1.00 80.29  ? 61  GLN   a OE1 1 
ATOM   46379 N  NE2 . GLN   AA 13 74  ? 47.214  -171.572 60.333  1.00 81.78  ? 61  GLN   a NE2 1 
ATOM   46380 N  N   . HIS   AA 13 75  ? 49.486  -174.629 54.521  1.00 81.93  ? 62  HIS   a N   1 
ATOM   46381 C  CA  . HIS   AA 13 75  ? 49.526  -175.640 53.431  1.00 83.86  ? 62  HIS   a CA  1 
ATOM   46382 C  C   . HIS   AA 13 75  ? 50.981  -176.052 53.180  1.00 85.05  ? 62  HIS   a C   1 
ATOM   46383 O  O   . HIS   AA 13 75  ? 51.241  -177.264 53.103  1.00 88.12  ? 62  HIS   a O   1 
ATOM   46384 C  CB  . HIS   AA 13 75  ? 48.840  -175.115 52.163  1.00 83.43  ? 62  HIS   a CB  1 
ATOM   46385 C  CG  . HIS   AA 13 75  ? 49.008  -176.005 50.976  1.00 83.07  ? 62  HIS   a CG  1 
ATOM   46386 N  ND1 . HIS   AA 13 75  ? 48.375  -177.229 50.875  1.00 84.06  ? 62  HIS   a ND1 1 
ATOM   46387 C  CD2 . HIS   AA 13 75  ? 49.729  -175.854 49.844  1.00 81.52  ? 62  HIS   a CD2 1 
ATOM   46388 C  CE1 . HIS   AA 13 75  ? 48.701  -177.794 49.731  1.00 84.47  ? 62  HIS   a CE1 1 
ATOM   46389 N  NE2 . HIS   AA 13 75  ? 49.530  -176.969 49.078  1.00 82.05  ? 62  HIS   a NE2 1 
ATOM   46390 N  N   . ILE   AA 13 76  ? 51.888  -175.077 53.076  1.00 85.07  ? 63  ILE   a N   1 
ATOM   46391 C  CA  . ILE   AA 13 76  ? 53.344  -175.300 52.824  1.00 87.59  ? 63  ILE   a CA  1 
ATOM   46392 C  C   . ILE   AA 13 76  ? 53.956  -176.035 54.024  1.00 89.57  ? 63  ILE   a C   1 
ATOM   46393 O  O   . ILE   AA 13 76  ? 54.851  -176.869 53.794  1.00 93.82  ? 63  ILE   a O   1 
ATOM   46394 C  CB  . ILE   AA 13 76  ? 54.064  -173.970 52.513  1.00 87.61  ? 63  ILE   a CB  1 
ATOM   46395 C  CG1 . ILE   AA 13 76  ? 53.613  -173.405 51.163  1.00 87.70  ? 63  ILE   a CG1 1 
ATOM   46396 C  CG2 . ILE   AA 13 76  ? 55.578  -174.128 52.570  1.00 86.95  ? 63  ILE   a CG2 1 
ATOM   46397 C  CD1 . ILE   AA 13 76  ? 53.833  -171.923 51.011  1.00 88.21  ? 63  ILE   a CD1 1 
ATOM   46398 N  N   . GLU   AA 13 77  ? 53.504  -175.730 55.246  1.00 91.72  ? 64  GLU   a N   1 
ATOM   46399 C  CA  . GLU   AA 13 77  ? 53.892  -176.455 56.488  1.00 94.34  ? 64  GLU   a CA  1 
ATOM   46400 C  C   . GLU   AA 13 77  ? 53.640  -177.954 56.301  1.00 93.22  ? 64  GLU   a C   1 
ATOM   46401 O  O   . GLU   AA 13 77  ? 54.560  -178.754 56.569  1.00 92.34  ? 64  GLU   a O   1 
ATOM   46402 C  CB  . GLU   AA 13 77  ? 53.087  -175.970 57.696  1.00 97.17  ? 64  GLU   a CB  1 
ATOM   46403 C  CG  . GLU   AA 13 77  ? 53.754  -174.855 58.472  1.00 100.95 ? 64  GLU   a CG  1 
ATOM   46404 C  CD  . GLU   AA 13 77  ? 53.137  -174.607 59.838  1.00 107.19 ? 64  GLU   a CD  1 
ATOM   46405 O  OE1 . GLU   AA 13 77  ? 52.612  -173.493 60.058  1.00 107.23 ? 64  GLU   a OE1 1 
ATOM   46406 O  OE2 . GLU   AA 13 77  ? 53.184  -175.532 60.680  1.00 107.92 ? 64  GLU   a OE2 1 
ATOM   46407 N  N   . ARG   AA 13 78  ? 52.425  -178.299 55.866  1.00 93.51  ? 65  ARG   a N   1 
ATOM   46408 C  CA  . ARG   AA 13 78  ? 51.958  -179.695 55.670  1.00 94.51  ? 65  ARG   a CA  1 
ATOM   46409 C  C   . ARG   AA 13 78  ? 52.785  -180.359 54.558  1.00 90.53  ? 65  ARG   a C   1 
ATOM   46410 O  O   . ARG   AA 13 78  ? 53.077  -181.556 54.698  1.00 96.03  ? 65  ARG   a O   1 
ATOM   46411 C  CB  . ARG   AA 13 78  ? 50.458  -179.712 55.358  1.00 97.42  ? 65  ARG   a CB  1 
ATOM   46412 C  CG  . ARG   AA 13 78  ? 49.741  -180.966 55.836  1.00 103.19 ? 65  ARG   a CG  1 
ATOM   46413 C  CD  . ARG   AA 13 78  ? 48.471  -181.214 55.048  1.00 111.97 ? 65  ARG   a CD  1 
ATOM   46414 N  NE  . ARG   AA 13 78  ? 48.787  -181.682 53.703  1.00 119.28 ? 65  ARG   a NE  1 
ATOM   46415 C  CZ  . ARG   AA 13 78  ? 48.169  -181.309 52.584  1.00 124.88 ? 65  ARG   a CZ  1 
ATOM   46416 N  NH1 . ARG   AA 13 78  ? 47.176  -180.434 52.614  1.00 130.73 ? 65  ARG   a NH1 1 
ATOM   46417 N  NH2 . ARG   AA 13 78  ? 48.557  -181.816 51.425  1.00 132.62 ? 65  ARG   a NH2 1 
ATOM   46418 N  N   . LEU   AA 13 79  ? 53.159  -179.619 53.508  1.00 85.28  ? 66  LEU   a N   1 
ATOM   46419 C  CA  . LEU   AA 13 79  ? 53.953  -180.144 52.358  1.00 84.90  ? 66  LEU   a CA  1 
ATOM   46420 C  C   . LEU   AA 13 79  ? 55.365  -180.522 52.822  1.00 85.59  ? 66  LEU   a C   1 
ATOM   46421 O  O   . LEU   AA 13 79  ? 55.869  -181.565 52.371  1.00 85.19  ? 66  LEU   a O   1 
ATOM   46422 C  CB  . LEU   AA 13 79  ? 54.032  -179.103 51.235  1.00 85.78  ? 66  LEU   a CB  1 
ATOM   46423 C  CG  . LEU   AA 13 79  ? 52.757  -178.866 50.426  1.00 86.00  ? 66  LEU   a CG  1 
ATOM   46424 C  CD1 . LEU   AA 13 79  ? 52.964  -177.730 49.437  1.00 88.87  ? 66  LEU   a CD1 1 
ATOM   46425 C  CD2 . LEU   AA 13 79  ? 52.310  -180.120 49.691  1.00 85.22  ? 66  LEU   a CD2 1 
ATOM   46426 N  N   . LEU   AA 13 80  ? 55.993  -179.681 53.648  1.00 87.25  ? 67  LEU   a N   1 
ATOM   46427 C  CA  . LEU   AA 13 80  ? 57.353  -179.912 54.209  1.00 90.47  ? 67  LEU   a CA  1 
ATOM   46428 C  C   . LEU   AA 13 80  ? 57.307  -181.085 55.194  1.00 92.47  ? 67  LEU   a C   1 
ATOM   46429 O  O   . LEU   AA 13 80  ? 58.207  -181.943 55.133  1.00 97.67  ? 67  LEU   a O   1 
ATOM   46430 C  CB  . LEU   AA 13 80  ? 57.842  -178.636 54.902  1.00 88.41  ? 67  LEU   a CB  1 
ATOM   46431 C  CG  . LEU   AA 13 80  ? 58.169  -177.463 53.980  1.00 86.70  ? 67  LEU   a CG  1 
ATOM   46432 C  CD1 . LEU   AA 13 80  ? 58.358  -176.186 54.783  1.00 85.39  ? 67  LEU   a CD1 1 
ATOM   46433 C  CD2 . LEU   AA 13 80  ? 59.405  -177.754 53.142  1.00 87.66  ? 67  LEU   a CD2 1 
ATOM   46434 N  N   . LYS   AA 13 81  ? 56.300  -181.099 56.073  1.00 96.98  ? 68  LYS   a N   1 
ATOM   46435 C  CA  . LYS   AA 13 81  ? 56.033  -182.183 57.057  1.00 101.78 ? 68  LYS   a CA  1 
ATOM   46436 C  C   . LYS   AA 13 81  ? 55.958  -183.527 56.319  1.00 99.97  ? 68  LYS   a C   1 
ATOM   46437 O  O   . LYS   AA 13 81  ? 56.567  -184.499 56.805  1.00 100.83 ? 68  LYS   a O   1 
ATOM   46438 C  CB  . LYS   AA 13 81  ? 54.748  -181.858 57.828  1.00 105.38 ? 68  LYS   a CB  1 
ATOM   46439 C  CG  . LYS   AA 13 81  ? 54.145  -182.991 58.649  1.00 109.76 ? 68  LYS   a CG  1 
ATOM   46440 C  CD  . LYS   AA 13 81  ? 52.841  -182.598 59.318  1.00 115.25 ? 68  LYS   a CD  1 
ATOM   46441 C  CE  . LYS   AA 13 81  ? 52.007  -183.781 59.764  1.00 119.37 ? 68  LYS   a CE  1 
ATOM   46442 N  NZ  . LYS   AA 13 81  ? 52.627  -184.499 60.905  1.00 124.16 ? 68  LYS   a NZ  1 
ATOM   46443 N  N   . ASP   AA 13 82  ? 55.248  -183.567 55.186  1.00 100.26 ? 69  ASP   a N   1 
ATOM   46444 C  CA  . ASP   AA 13 82  ? 55.067  -184.780 54.343  1.00 102.43 ? 69  ASP   a CA  1 
ATOM   46445 C  C   . ASP   AA 13 82  ? 56.397  -185.138 53.668  1.00 98.49  ? 69  ASP   a C   1 
ATOM   46446 O  O   . ASP   AA 13 82  ? 56.693  -186.339 53.577  1.00 106.11 ? 69  ASP   a O   1 
ATOM   46447 C  CB  . ASP   AA 13 82  ? 53.955  -184.584 53.308  1.00 111.49 ? 69  ASP   a CB  1 
ATOM   46448 C  CG  . ASP   AA 13 82  ? 53.599  -185.851 52.546  1.00 120.71 ? 69  ASP   a CG  1 
ATOM   46449 O  OD1 . ASP   AA 13 82  ? 52.902  -186.710 53.126  1.00 125.55 ? 69  ASP   a OD1 1 
ATOM   46450 O  OD2 . ASP   AA 13 82  ? 54.029  -185.974 51.378  1.00 141.45 ? 69  ASP   a OD2 1 
ATOM   46451 N  N   . LEU   AA 13 83  ? 57.164  -184.140 53.214  1.00 91.56  ? 70  LEU   a N   1 
ATOM   46452 C  CA  . LEU   AA 13 83  ? 58.471  -184.335 52.524  1.00 93.79  ? 70  LEU   a CA  1 
ATOM   46453 C  C   . LEU   AA 13 83  ? 59.435  -185.077 53.459  1.00 92.97  ? 70  LEU   a C   1 
ATOM   46454 O  O   . LEU   AA 13 83  ? 60.188  -185.936 52.965  1.00 97.92  ? 70  LEU   a O   1 
ATOM   46455 C  CB  . LEU   AA 13 83  ? 59.058  -182.977 52.119  1.00 92.95  ? 70  LEU   a CB  1 
ATOM   46456 C  CG  . LEU   AA 13 83  ? 59.810  -182.924 50.787  1.00 94.63  ? 70  LEU   a CG  1 
ATOM   46457 C  CD1 . LEU   AA 13 83  ? 60.662  -181.667 50.711  1.00 93.02  ? 70  LEU   a CD1 1 
ATOM   46458 C  CD2 . LEU   AA 13 83  ? 60.681  -184.155 50.565  1.00 96.87  ? 70  LEU   a CD2 1 
ATOM   46459 N  N   . VAL   AA 13 84  ? 59.418  -184.745 54.753  1.00 91.05  ? 71  VAL   a N   1 
ATOM   46460 C  CA  . VAL   AA 13 84  ? 60.236  -185.418 55.806  1.00 94.15  ? 71  VAL   a CA  1 
ATOM   46461 C  C   . VAL   AA 13 84  ? 59.819  -186.894 55.881  1.00 94.59  ? 71  VAL   a C   1 
ATOM   46462 O  O   . VAL   AA 13 84  ? 60.714  -187.765 55.857  1.00 97.01  ? 71  VAL   a O   1 
ATOM   46463 C  CB  . VAL   AA 13 84  ? 60.086  -184.724 57.174  1.00 95.00  ? 71  VAL   a CB  1 
ATOM   46464 C  CG1 . VAL   AA 13 84  ? 60.736  -185.524 58.295  1.00 94.91  ? 71  VAL   a CG1 1 
ATOM   46465 C  CG2 . VAL   AA 13 84  ? 60.625  -183.301 57.153  1.00 96.92  ? 71  VAL   a CG2 1 
ATOM   46466 N  N   . THR   AA 13 85  ? 58.511  -187.155 55.979  1.00 90.78  ? 72  THR   a N   1 
ATOM   46467 C  CA  . THR   AA 13 85  ? 57.916  -188.515 56.080  1.00 92.59  ? 72  THR   a CA  1 
ATOM   46468 C  C   . THR   AA 13 85  ? 58.335  -189.346 54.863  1.00 96.25  ? 72  THR   a C   1 
ATOM   46469 O  O   . THR   AA 13 85  ? 58.814  -190.487 55.055  1.00 100.92 ? 72  THR   a O   1 
ATOM   46470 C  CB  . THR   AA 13 85  ? 56.385  -188.458 56.181  1.00 90.22  ? 72  THR   a CB  1 
ATOM   46471 O  OG1 . THR   AA 13 85  ? 56.007  -187.544 57.210  1.00 86.94  ? 72  THR   a OG1 1 
ATOM   46472 C  CG2 . THR   AA 13 85  ? 55.766  -189.810 56.460  1.00 93.51  ? 72  THR   a CG2 1 
ATOM   46473 N  N   . GLU   AA 13 86  ? 58.156  -188.787 53.662  1.00 94.66  ? 73  GLU   a N   1 
ATOM   46474 C  CA  . GLU   AA 13 86  ? 58.364  -189.481 52.362  1.00 95.43  ? 73  GLU   a CA  1 
ATOM   46475 C  C   . GLU   AA 13 86  ? 59.854  -189.795 52.181  1.00 92.46  ? 73  GLU   a C   1 
ATOM   46476 O  O   . GLU   AA 13 86  ? 60.166  -190.864 51.628  1.00 94.28  ? 73  GLU   a O   1 
ATOM   46477 C  CB  . GLU   AA 13 86  ? 57.835  -188.629 51.205  1.00 97.62  ? 73  GLU   a CB  1 
ATOM   46478 C  CG  . GLU   AA 13 86  ? 57.246  -189.447 50.068  1.00 102.37 ? 73  GLU   a CG  1 
ATOM   46479 C  CD  . GLU   AA 13 86  ? 55.811  -189.900 50.281  1.00 106.30 ? 73  GLU   a CD  1 
ATOM   46480 O  OE1 . GLU   AA 13 86  ? 55.468  -191.009 49.816  1.00 110.76 ? 73  GLU   a OE1 1 
ATOM   46481 O  OE2 . GLU   AA 13 86  ? 55.034  -189.139 50.901  1.00 109.84 ? 73  GLU   a OE2 1 
ATOM   46482 N  N   . ASN   AA 13 87  ? 60.735  -188.896 52.632  1.00 88.78  ? 74  ASN   a N   1 
ATOM   46483 C  CA  . ASN   AA 13 87  ? 62.211  -189.045 52.530  1.00 88.81  ? 74  ASN   a CA  1 
ATOM   46484 C  C   . ASN   AA 13 87  ? 62.671  -190.211 53.413  1.00 90.14  ? 74  ASN   a C   1 
ATOM   46485 O  O   . ASN   AA 13 87  ? 63.625  -190.904 53.017  1.00 95.12  ? 74  ASN   a O   1 
ATOM   46486 C  CB  . ASN   AA 13 87  ? 62.944  -187.757 52.913  1.00 86.58  ? 74  ASN   a CB  1 
ATOM   46487 C  CG  . ASN   AA 13 87  ? 64.448  -187.874 52.775  1.00 86.59  ? 74  ASN   a CG  1 
ATOM   46488 O  OD1 . ASN   AA 13 87  ? 64.976  -187.882 51.667  1.00 83.93  ? 74  ASN   a OD1 1 
ATOM   46489 N  ND2 . ASN   AA 13 87  ? 65.148  -187.969 53.894  1.00 90.12  ? 74  ASN   a ND2 1 
ATOM   46490 N  N   . ALA   AA 13 88  ? 62.021  -190.408 54.565  1.00 89.64  ? 75  ALA   a N   1 
ATOM   46491 C  CA  . ALA   AA 13 88  ? 62.360  -191.446 55.567  1.00 91.69  ? 75  ALA   a CA  1 
ATOM   46492 C  C   . ALA   AA 13 88  ? 61.996  -192.837 55.037  1.00 92.87  ? 75  ALA   a C   1 
ATOM   46493 O  O   . ALA   AA 13 88  ? 62.606  -193.806 55.515  1.00 98.48  ? 75  ALA   a O   1 
ATOM   46494 C  CB  . ALA   AA 13 88  ? 61.662  -191.163 56.874  1.00 90.11  ? 75  ALA   a CB  1 
ATOM   46495 N  N   . TYR   AA 13 89  ? 61.051  -192.936 54.094  1.00 92.09  ? 76  TYR   a N   1 
ATOM   46496 C  CA  . TYR   AA 13 89  ? 60.564  -194.223 53.521  1.00 92.45  ? 76  TYR   a CA  1 
ATOM   46497 C  C   . TYR   AA 13 89  ? 61.703  -194.940 52.785  1.00 95.52  ? 76  TYR   a C   1 
ATOM   46498 O  O   . TYR   AA 13 89  ? 62.338  -194.318 51.908  1.00 93.95  ? 76  TYR   a O   1 
ATOM   46499 C  CB  . TYR   AA 13 89  ? 59.394  -194.019 52.552  1.00 89.16  ? 76  TYR   a CB  1 
ATOM   46500 C  CG  . TYR   AA 13 89  ? 58.065  -193.663 53.171  1.00 88.48  ? 76  TYR   a CG  1 
ATOM   46501 C  CD1 . TYR   AA 13 89  ? 57.754  -193.993 54.482  1.00 89.71  ? 76  TYR   a CD1 1 
ATOM   46502 C  CD2 . TYR   AA 13 89  ? 57.091  -193.022 52.422  1.00 86.36  ? 76  TYR   a CD2 1 
ATOM   46503 C  CE1 . TYR   AA 13 89  ? 56.528  -193.667 55.039  1.00 90.25  ? 76  TYR   a CE1 1 
ATOM   46504 C  CE2 . TYR   AA 13 89  ? 55.859  -192.691 52.961  1.00 86.29  ? 76  TYR   a CE2 1 
ATOM   46505 C  CZ  . TYR   AA 13 89  ? 55.576  -193.012 54.276  1.00 88.03  ? 76  TYR   a CZ  1 
ATOM   46506 O  OH  . TYR   AA 13 89  ? 54.355  -192.683 54.791  1.00 87.95  ? 76  TYR   a OH  1 
ATOM   46507 N  N   . ASP   AA 13 90  ? 61.933  -196.212 53.138  1.00 99.15  ? 77  ASP   a N   1 
ATOM   46508 C  CA  . ASP   AA 13 90  ? 62.924  -197.121 52.499  1.00 102.27 ? 77  ASP   a CA  1 
ATOM   46509 C  C   . ASP   AA 13 90  ? 64.277  -196.407 52.398  1.00 102.37 ? 77  ASP   a C   1 
ATOM   46510 O  O   . ASP   AA 13 90  ? 64.923  -196.491 51.328  1.00 97.86  ? 77  ASP   a O   1 
ATOM   46511 C  CB  . ASP   AA 13 90  ? 62.421  -197.587 51.132  1.00 103.92 ? 77  ASP   a CB  1 
ATOM   46512 C  CG  . ASP   AA 13 90  ? 60.985  -198.077 51.157  1.00 106.46 ? 77  ASP   a CG  1 
ATOM   46513 O  OD1 . ASP   AA 13 90  ? 60.561  -198.594 52.213  1.00 113.43 ? 77  ASP   a OD1 1 
ATOM   46514 O  OD2 . ASP   AA 13 90  ? 60.296  -197.924 50.128  1.00 102.56 ? 77  ASP   a OD2 1 
ATOM   46515 N  N   . ASN   AA 13 91  ? 64.674  -195.732 53.481  1.00 102.71 ? 78  ASN   a N   1 
ATOM   46516 C  CA  . ASN   AA 13 91  ? 65.890  -194.884 53.561  1.00 102.33 ? 78  ASN   a CA  1 
ATOM   46517 C  C   . ASN   AA 13 91  ? 66.593  -195.174 54.886  1.00 103.17 ? 78  ASN   a C   1 
ATOM   46518 O  O   . ASN   AA 13 91  ? 66.300  -194.551 55.904  1.00 96.81  ? 78  ASN   a O   1 
ATOM   46519 C  CB  . ASN   AA 13 91  ? 65.530  -193.408 53.379  1.00 99.56  ? 78  ASN   a CB  1 
ATOM   46520 C  CG  . ASN   AA 13 91  ? 66.733  -192.518 53.143  1.00 100.67 ? 78  ASN   a CG  1 
ATOM   46521 O  OD1 . ASN   AA 13 91  ? 67.822  -193.000 52.837  1.00 104.60 ? 78  ASN   a OD1 1 
ATOM   46522 N  ND2 . ASN   AA 13 91  ? 66.545  -191.216 53.282  1.00 98.91  ? 78  ASN   a ND2 1 
ATOM   46523 N  N   . PRO   AA 13 92  ? 67.518  -196.160 54.923  1.00 108.74 ? 79  PRO   a N   1 
ATOM   46524 C  CA  . PRO   AA 13 92  ? 68.297  -196.440 56.130  1.00 113.96 ? 79  PRO   a CA  1 
ATOM   46525 C  C   . PRO   AA 13 92  ? 69.177  -195.260 56.576  1.00 112.81 ? 79  PRO   a C   1 
ATOM   46526 O  O   . PRO   AA 13 92  ? 69.546  -195.232 57.735  1.00 121.92 ? 79  PRO   a O   1 
ATOM   46527 C  CB  . PRO   AA 13 92  ? 69.177  -197.642 55.738  1.00 117.06 ? 79  PRO   a CB  1 
ATOM   46528 C  CG  . PRO   AA 13 92  ? 68.487  -198.251 54.533  1.00 115.59 ? 79  PRO   a CG  1 
ATOM   46529 C  CD  . PRO   AA 13 92  ? 67.835  -197.084 53.823  1.00 112.47 ? 79  PRO   a CD  1 
ATOM   46530 N  N   . LEU   AA 13 93  ? 69.488  -194.332 55.662  1.00 109.87 ? 80  LEU   a N   1 
ATOM   46531 C  CA  . LEU   AA 13 93  ? 70.381  -193.164 55.904  1.00 110.78 ? 80  LEU   a CA  1 
ATOM   46532 C  C   . LEU   AA 13 93  ? 69.566  -191.861 55.945  1.00 107.97 ? 80  LEU   a C   1 
ATOM   46533 O  O   . LEU   AA 13 93  ? 70.100  -190.820 55.507  1.00 105.25 ? 80  LEU   a O   1 
ATOM   46534 C  CB  . LEU   AA 13 93  ? 71.430  -193.115 54.787  1.00 109.82 ? 80  LEU   a CB  1 
ATOM   46535 C  CG  . LEU   AA 13 93  ? 72.216  -194.402 54.548  1.00 111.62 ? 80  LEU   a CG  1 
ATOM   46536 C  CD1 . LEU   AA 13 93  ? 73.046  -194.299 53.277  1.00 109.75 ? 80  LEU   a CD1 1 
ATOM   46537 C  CD2 . LEU   AA 13 93  ? 73.103  -194.724 55.741  1.00 115.16 ? 80  LEU   a CD2 1 
ATOM   46538 N  N   . ALA   AA 13 94  ? 68.338  -191.903 56.475  1.00 107.22 ? 81  ALA   a N   1 
ATOM   46539 C  CA  . ALA   AA 13 94  ? 67.399  -190.756 56.536  1.00 105.40 ? 81  ALA   a CA  1 
ATOM   46540 C  C   . ALA   AA 13 94  ? 67.884  -189.710 57.550  1.00 105.88 ? 81  ALA   a C   1 
ATOM   46541 O  O   . ALA   AA 13 94  ? 67.474  -188.542 57.425  1.00 104.85 ? 81  ALA   a O   1 
ATOM   46542 C  CB  . ALA   AA 13 94  ? 66.009  -191.237 56.874  1.00 103.81 ? 81  ALA   a CB  1 
ATOM   46543 N  N   . ASP   AA 13 95  ? 68.710  -190.116 58.521  1.00 109.20 ? 82  ASP   a N   1 
ATOM   46544 C  CA  . ASP   AA 13 95  ? 69.273  -189.233 59.578  1.00 110.14 ? 82  ASP   a CA  1 
ATOM   46545 C  C   . ASP   AA 13 95  ? 70.791  -189.100 59.391  1.00 111.23 ? 82  ASP   a C   1 
ATOM   46546 O  O   . ASP   AA 13 95  ? 71.461  -188.709 60.364  1.00 115.98 ? 82  ASP   a O   1 
ATOM   46547 C  CB  . ASP   AA 13 95  ? 68.927  -189.761 60.975  1.00 114.68 ? 82  ASP   a CB  1 
ATOM   46548 C  CG  . ASP   AA 13 95  ? 69.368  -191.195 61.235  1.00 122.64 ? 82  ASP   a CG  1 
ATOM   46549 O  OD1 . ASP   AA 13 95  ? 69.553  -191.945 60.250  1.00 125.48 ? 82  ASP   a OD1 1 
ATOM   46550 O  OD2 . ASP   AA 13 95  ? 69.521  -191.555 62.422  1.00 125.52 ? 82  ASP   a OD2 1 
ATOM   46551 N  N   . ALA   AA 13 96  ? 71.312  -189.400 58.194  1.00 111.87 ? 83  ALA   a N   1 
ATOM   46552 C  CA  . ALA   AA 13 96  ? 72.761  -189.362 57.873  1.00 115.16 ? 83  ALA   a CA  1 
ATOM   46553 C  C   . ALA   AA 13 96  ? 72.980  -188.762 56.475  1.00 115.47 ? 83  ALA   a C   1 
ATOM   46554 O  O   . ALA   AA 13 96  ? 72.637  -187.576 56.297  1.00 117.78 ? 83  ALA   a O   1 
ATOM   46555 C  CB  . ALA   AA 13 96  ? 73.350  -190.744 58.020  1.00 116.29 ? 83  ALA   a CB  1 
ATOM   46556 N  N   . GLU   AA 13 97  ? 73.529  -189.533 55.525  1.00 115.77 ? 84  GLU   a N   1 
ATOM   46557 C  CA  . GLU   AA 13 97  ? 73.973  -189.035 54.192  1.00 116.31 ? 84  GLU   a CA  1 
ATOM   46558 C  C   . GLU   AA 13 97  ? 72.765  -188.650 53.330  1.00 114.79 ? 84  GLU   a C   1 
ATOM   46559 O  O   . GLU   AA 13 97  ? 72.922  -187.743 52.488  1.00 115.45 ? 84  GLU   a O   1 
ATOM   46560 C  CB  . GLU   AA 13 97  ? 74.818  -190.077 53.455  1.00 119.16 ? 84  GLU   a CB  1 
ATOM   46561 C  CG  . GLU   AA 13 97  ? 76.188  -190.310 54.070  1.00 123.96 ? 84  GLU   a CG  1 
ATOM   46562 C  CD  . GLU   AA 13 97  ? 76.289  -191.516 54.987  1.00 128.00 ? 84  GLU   a CD  1 
ATOM   46563 O  OE1 . GLU   AA 13 97  ? 77.372  -192.134 55.028  1.00 135.45 ? 84  GLU   a OE1 1 
ATOM   46564 O  OE2 . GLU   AA 13 97  ? 75.288  -191.836 55.659  1.00 133.18 ? 84  GLU   a OE2 1 
ATOM   46565 N  N   . GLU   AA 13 98  ? 71.617  -189.312 53.523  1.00 112.78 ? 85  GLU   a N   1 
ATOM   46566 C  CA  . GLU   AA 13 98  ? 70.386  -189.114 52.707  1.00 110.50 ? 85  GLU   a CA  1 
ATOM   46567 C  C   . GLU   AA 13 98  ? 69.320  -188.362 53.518  1.00 107.46 ? 85  GLU   a C   1 
ATOM   46568 O  O   . GLU   AA 13 98  ? 68.120  -188.572 53.248  1.00 104.90 ? 85  GLU   a O   1 
ATOM   46569 C  CB  . GLU   AA 13 98  ? 69.859  -190.463 52.208  1.00 112.29 ? 85  GLU   a CB  1 
ATOM   46570 C  CG  . GLU   AA 13 98  ? 70.814  -191.188 51.274  1.00 114.39 ? 85  GLU   a CG  1 
ATOM   46571 C  CD  . GLU   AA 13 98  ? 71.013  -190.547 49.908  1.00 113.35 ? 85  GLU   a CD  1 
ATOM   46572 O  OE1 . GLU   AA 13 98  ? 72.015  -190.874 49.240  1.00 110.05 ? 85  GLU   a OE1 1 
ATOM   46573 O  OE2 . GLU   AA 13 98  ? 70.160  -189.731 49.508  1.00 113.27 ? 85  GLU   a OE2 1 
ATOM   46574 N  N   . ALA   AA 13 99  ? 69.736  -187.504 54.457  1.00 107.28 ? 86  ALA   a N   1 
ATOM   46575 C  CA  . ALA   AA 13 99  ? 68.856  -186.542 55.162  1.00 106.07 ? 86  ALA   a CA  1 
ATOM   46576 C  C   . ALA   AA 13 99  ? 68.539  -185.388 54.205  1.00 103.60 ? 86  ALA   a C   1 
ATOM   46577 O  O   . ALA   AA 13 99  ? 69.337  -185.165 53.268  1.00 101.59 ? 86  ALA   a O   1 
ATOM   46578 C  CB  . ALA   AA 13 99  ? 69.513  -186.051 56.430  1.00 108.48 ? 86  ALA   a CB  1 
ATOM   46579 N  N   . LEU   AA 13 100 ? 67.416  -184.695 54.418  1.00 101.99 ? 87  LEU   a N   1 
ATOM   46580 C  CA  . LEU   AA 13 100 ? 66.976  -183.562 53.557  1.00 99.08  ? 87  LEU   a CA  1 
ATOM   46581 C  C   . LEU   AA 13 100 ? 67.954  -182.394 53.720  1.00 97.20  ? 87  LEU   a C   1 
ATOM   46582 O  O   . LEU   AA 13 100 ? 68.123  -181.911 54.856  1.00 94.05  ? 87  LEU   a O   1 
ATOM   46583 C  CB  . LEU   AA 13 100 ? 65.548  -183.137 53.916  1.00 98.05  ? 87  LEU   a CB  1 
ATOM   46584 C  CG  . LEU   AA 13 100 ? 64.430  -183.964 53.281  1.00 97.23  ? 87  LEU   a CG  1 
ATOM   46585 C  CD1 . LEU   AA 13 100 ? 63.078  -183.595 53.873  1.00 95.04  ? 87  LEU   a CD1 1 
ATOM   46586 C  CD2 . LEU   AA 13 100 ? 64.412  -183.797 51.767  1.00 96.18  ? 87  LEU   a CD2 1 
ATOM   46587 N  N   . GLU   AA 13 101 ? 68.584  -181.990 52.615  1.00 96.95  ? 88  GLU   a N   1 
ATOM   46588 C  CA  . GLU   AA 13 101 ? 69.461  -180.795 52.514  1.00 98.20  ? 88  GLU   a CA  1 
ATOM   46589 C  C   . GLU   AA 13 101 ? 68.590  -179.558 52.313  1.00 99.85  ? 88  GLU   a C   1 
ATOM   46590 O  O   . GLU   AA 13 101 ? 67.524  -179.645 51.704  1.00 103.12 ? 88  GLU   a O   1 
ATOM   46591 C  CB  . GLU   AA 13 101 ? 70.440  -180.946 51.347  1.00 99.15  ? 88  GLU   a CB  1 
ATOM   46592 C  CG  . GLU   AA 13 101 ? 71.534  -181.966 51.595  1.00 101.13 ? 88  GLU   a CG  1 
ATOM   46593 C  CD  . GLU   AA 13 101 ? 72.745  -181.412 52.326  1.00 100.97 ? 88  GLU   a CD  1 
ATOM   46594 O  OE1 . GLU   AA 13 101 ? 72.592  -180.992 53.490  1.00 100.88 ? 88  GLU   a OE1 1 
ATOM   46595 O  OE2 . GLU   AA 13 101 ? 73.836  -181.389 51.723  1.00 103.05 ? 88  GLU   a OE2 1 
ATOM   46596 N  N   . PRO   AA 13 102 ? 69.010  -178.376 52.826  1.00 97.22  ? 89  PRO   a N   1 
ATOM   46597 C  CA  . PRO   AA 13 102 ? 68.323  -177.118 52.532  1.00 94.24  ? 89  PRO   a CA  1 
ATOM   46598 C  C   . PRO   AA 13 102 ? 68.057  -176.935 51.029  1.00 91.39  ? 89  PRO   a C   1 
ATOM   46599 O  O   . PRO   AA 13 102 ? 66.948  -176.569 50.673  1.00 89.10  ? 89  PRO   a O   1 
ATOM   46600 C  CB  . PRO   AA 13 102 ? 69.296  -176.043 53.043  1.00 95.60  ? 89  PRO   a CB  1 
ATOM   46601 C  CG  . PRO   AA 13 102 ? 70.108  -176.734 54.121  1.00 96.75  ? 89  PRO   a CG  1 
ATOM   46602 C  CD  . PRO   AA 13 102 ? 70.149  -178.198 53.739  1.00 98.02  ? 89  PRO   a CD  1 
ATOM   46603 N  N   . SER   AA 13 103 ? 69.067  -177.213 50.195  1.00 90.15  ? 90  SER   a N   1 
ATOM   46604 C  CA  . SER   AA 13 103 ? 69.042  -177.037 48.718  1.00 88.64  ? 90  SER   a CA  1 
ATOM   46605 C  C   . SER   AA 13 103 ? 67.927  -177.883 48.089  1.00 89.92  ? 90  SER   a C   1 
ATOM   46606 O  O   . SER   AA 13 103 ? 67.329  -177.405 47.106  1.00 87.00  ? 90  SER   a O   1 
ATOM   46607 C  CB  . SER   AA 13 103 ? 70.381  -177.356 48.108  1.00 88.56  ? 90  SER   a CB  1 
ATOM   46608 O  OG  . SER   AA 13 103 ? 70.695  -178.731 48.264  1.00 87.88  ? 90  SER   a OG  1 
ATOM   46609 N  N   . TYR   AA 13 104 ? 67.660  -179.082 48.626  1.00 91.60  ? 91  TYR   a N   1 
ATOM   46610 C  CA  . TYR   AA 13 104 ? 66.561  -179.977 48.168  1.00 93.71  ? 91  TYR   a CA  1 
ATOM   46611 C  C   . TYR   AA 13 104 ? 65.215  -179.331 48.518  1.00 91.31  ? 91  TYR   a C   1 
ATOM   46612 O  O   . TYR   AA 13 104 ? 64.337  -179.245 47.636  1.00 90.15  ? 91  TYR   a O   1 
ATOM   46613 C  CB  . TYR   AA 13 104 ? 66.619  -181.379 48.791  1.00 95.50  ? 91  TYR   a CB  1 
ATOM   46614 C  CG  . TYR   AA 13 104 ? 67.925  -182.132 48.696  1.00 98.52  ? 91  TYR   a CG  1 
ATOM   46615 C  CD1 . TYR   AA 13 104 ? 68.907  -181.802 47.771  1.00 99.71  ? 91  TYR   a CD1 1 
ATOM   46616 C  CD2 . TYR   AA 13 104 ? 68.165  -183.219 49.523  1.00 99.10  ? 91  TYR   a CD2 1 
ATOM   46617 C  CE1 . TYR   AA 13 104 ? 70.099  -182.509 47.697  1.00 98.84  ? 91  TYR   a CE1 1 
ATOM   46618 C  CE2 . TYR   AA 13 104 ? 69.351  -183.934 49.464  1.00 99.08  ? 91  TYR   a CE2 1 
ATOM   46619 C  CZ  . TYR   AA 13 104 ? 70.322  -183.579 48.545  1.00 98.68  ? 91  TYR   a CZ  1 
ATOM   46620 O  OH  . TYR   AA 13 104 ? 71.492  -184.279 48.476  1.00 97.29  ? 91  TYR   a OH  1 
ATOM   46621 N  N   . ILE   AA 13 105 ? 65.068  -178.895 49.775  1.00 89.75  ? 92  ILE   a N   1 
ATOM   46622 C  CA  . ILE   AA 13 105 ? 63.823  -178.285 50.332  1.00 89.47  ? 92  ILE   a CA  1 
ATOM   46623 C  C   . ILE   AA 13 105 ? 63.461  -177.041 49.518  1.00 89.22  ? 92  ILE   a C   1 
ATOM   46624 O  O   . ILE   AA 13 105 ? 62.260  -176.850 49.251  1.00 93.64  ? 92  ILE   a O   1 
ATOM   46625 C  CB  . ILE   AA 13 105 ? 63.990  -177.955 51.828  1.00 89.40  ? 92  ILE   a CB  1 
ATOM   46626 C  CG1 . ILE   AA 13 105 ? 64.079  -179.226 52.674  1.00 92.48  ? 92  ILE   a CG1 1 
ATOM   46627 C  CG2 . ILE   AA 13 105 ? 62.874  -177.044 52.314  1.00 87.29  ? 92  ILE   a CG2 1 
ATOM   46628 C  CD1 . ILE   AA 13 105 ? 64.909  -179.069 53.923  1.00 95.70  ? 92  ILE   a CD1 1 
ATOM   46629 N  N   . PHE   AA 13 106 ? 64.452  -176.222 49.155  1.00 89.35  ? 93  PHE   a N   1 
ATOM   46630 C  CA  . PHE   AA 13 106 ? 64.243  -174.985 48.360  1.00 90.71  ? 93  PHE   a CA  1 
ATOM   46631 C  C   . PHE   AA 13 106 ? 63.728  -175.360 46.970  1.00 86.83  ? 93  PHE   a C   1 
ATOM   46632 O  O   . PHE   AA 13 106 ? 62.628  -174.916 46.601  1.00 87.91  ? 93  PHE   a O   1 
ATOM   46633 C  CB  . PHE   AA 13 106 ? 65.519  -174.152 48.222  1.00 91.24  ? 93  PHE   a CB  1 
ATOM   46634 C  CG  . PHE   AA 13 106 ? 65.325  -172.908 47.392  1.00 92.63  ? 93  PHE   a CG  1 
ATOM   46635 C  CD1 . PHE   AA 13 106 ? 64.887  -171.728 47.975  1.00 90.99  ? 93  PHE   a CD1 1 
ATOM   46636 C  CD2 . PHE   AA 13 106 ? 65.531  -172.928 46.020  1.00 92.86  ? 93  PHE   a CD2 1 
ATOM   46637 C  CE1 . PHE   AA 13 106 ? 64.688  -170.589 47.211  1.00 89.42  ? 93  PHE   a CE1 1 
ATOM   46638 C  CE2 . PHE   AA 13 106 ? 65.327  -171.788 45.256  1.00 91.63  ? 93  PHE   a CE2 1 
ATOM   46639 C  CZ  . PHE   AA 13 106 ? 64.910  -170.621 45.854  1.00 90.05  ? 93  PHE   a CZ  1 
ATOM   46640 N  N   . GLU   AA 13 107 ? 64.507  -176.151 46.230  1.00 88.35  ? 94  GLU   a N   1 
ATOM   46641 C  CA  . GLU   AA 13 107 ? 64.219  -176.501 44.815  1.00 91.11  ? 94  GLU   a CA  1 
ATOM   46642 C  C   . GLU   AA 13 107 ? 62.793  -177.053 44.706  1.00 88.03  ? 94  GLU   a C   1 
ATOM   46643 O  O   . GLU   AA 13 107 ? 62.114  -176.717 43.716  1.00 85.41  ? 94  GLU   a O   1 
ATOM   46644 C  CB  . GLU   AA 13 107 ? 65.232  -177.509 44.270  1.00 96.07  ? 94  GLU   a CB  1 
ATOM   46645 C  CG  . GLU   AA 13 107 ? 65.395  -177.414 42.765  1.00 100.00 ? 94  GLU   a CG  1 
ATOM   46646 C  CD  . GLU   AA 13 107 ? 66.052  -176.124 42.302  1.00 103.41 ? 94  GLU   a CD  1 
ATOM   46647 O  OE1 . GLU   AA 13 107 ? 65.593  -175.557 41.290  1.00 105.14 ? 94  GLU   a OE1 1 
ATOM   46648 O  OE2 . GLU   AA 13 107 ? 67.016  -175.684 42.962  1.00 108.80 ? 94  GLU   a OE2 1 
ATOM   46649 N  N   . TYR   AA 13 108 ? 62.364  -177.868 45.678  1.00 86.97  ? 95  TYR   a N   1 
ATOM   46650 C  CA  . TYR   AA 13 108 ? 60.990  -178.433 45.761  1.00 84.02  ? 95  TYR   a CA  1 
ATOM   46651 C  C   . TYR   AA 13 108 ? 59.978  -177.283 45.816  1.00 84.44  ? 95  TYR   a C   1 
ATOM   46652 O  O   . TYR   AA 13 108 ? 59.116  -177.206 44.919  1.00 79.76  ? 95  TYR   a O   1 
ATOM   46653 C  CB  . TYR   AA 13 108 ? 60.825  -179.359 46.970  1.00 83.35  ? 95  TYR   a CB  1 
ATOM   46654 C  CG  . TYR   AA 13 108 ? 59.403  -179.798 47.224  1.00 80.42  ? 95  TYR   a CG  1 
ATOM   46655 C  CD1 . TYR   AA 13 108 ? 58.738  -180.625 46.331  1.00 80.54  ? 95  TYR   a CD1 1 
ATOM   46656 C  CD2 . TYR   AA 13 108 ? 58.713  -179.382 48.352  1.00 78.85  ? 95  TYR   a CD2 1 
ATOM   46657 C  CE1 . TYR   AA 13 108 ? 57.431  -181.029 46.551  1.00 78.66  ? 95  TYR   a CE1 1 
ATOM   46658 C  CE2 . TYR   AA 13 108 ? 57.406  -179.778 48.589  1.00 78.90  ? 95  TYR   a CE2 1 
ATOM   46659 C  CZ  . TYR   AA 13 108 ? 56.763  -180.607 47.686  1.00 77.97  ? 95  TYR   a CZ  1 
ATOM   46660 O  OH  . TYR   AA 13 108 ? 55.477  -181.004 47.907  1.00 78.92  ? 95  TYR   a OH  1 
ATOM   46661 N  N   . LEU   AA 13 109 ? 60.093  -176.420 46.833  1.00 84.02  ? 96  LEU   a N   1 
ATOM   46662 C  CA  . LEU   AA 13 109 ? 59.193  -175.252 47.045  1.00 82.93  ? 96  LEU   a CA  1 
ATOM   46663 C  C   . LEU   AA 13 109 ? 59.222  -174.356 45.799  1.00 79.94  ? 96  LEU   a C   1 
ATOM   46664 O  O   . LEU   AA 13 109 ? 58.136  -173.997 45.307  1.00 76.08  ? 96  LEU   a O   1 
ATOM   46665 C  CB  . LEU   AA 13 109 ? 59.627  -174.477 48.295  1.00 84.36  ? 96  LEU   a CB  1 
ATOM   46666 C  CG  . LEU   AA 13 109 ? 59.357  -175.153 49.640  1.00 86.29  ? 96  LEU   a CG  1 
ATOM   46667 C  CD1 . LEU   AA 13 109 ? 59.840  -174.273 50.782  1.00 87.31  ? 96  LEU   a CD1 1 
ATOM   46668 C  CD2 . LEU   AA 13 109 ? 57.880  -175.480 49.818  1.00 87.13  ? 96  LEU   a CD2 1 
ATOM   46669 N  N   . ALA   AA 13 110 ? 60.421  -174.041 45.297  1.00 79.56  ? 97  ALA   a N   1 
ATOM   46670 C  CA  . ALA   AA 13 110 ? 60.655  -173.200 44.099  1.00 79.90  ? 97  ALA   a CA  1 
ATOM   46671 C  C   . ALA   AA 13 110 ? 59.890  -173.768 42.897  1.00 81.72  ? 97  ALA   a C   1 
ATOM   46672 O  O   . ALA   AA 13 110 ? 59.297  -172.968 42.148  1.00 78.79  ? 97  ALA   a O   1 
ATOM   46673 C  CB  . ALA   AA 13 110 ? 62.133  -173.097 43.812  1.00 80.83  ? 97  ALA   a CB  1 
ATOM   46674 N  N   . THR   AA 13 111 ? 59.900  -175.093 42.725  1.00 79.24  ? 98  THR   a N   1 
ATOM   46675 C  CA  . THR   AA 13 111 ? 59.168  -175.804 41.642  1.00 79.05  ? 98  THR   a CA  1 
ATOM   46676 C  C   . THR   AA 13 111 ? 57.663  -175.583 41.821  1.00 78.71  ? 98  THR   a C   1 
ATOM   46677 O  O   . THR   AA 13 111 ? 57.011  -175.175 40.844  1.00 80.46  ? 98  THR   a O   1 
ATOM   46678 C  CB  . THR   AA 13 111 ? 59.498  -177.300 41.615  1.00 79.02  ? 98  THR   a CB  1 
ATOM   46679 O  OG1 . THR   AA 13 111 ? 60.890  -177.420 41.322  1.00 77.51  ? 98  THR   a OG1 1 
ATOM   46680 C  CG2 . THR   AA 13 111 ? 58.686  -178.064 40.592  1.00 80.44  ? 98  THR   a CG2 1 
ATOM   46681 N  N   . VAL   AA 13 112 ? 57.149  -175.847 43.025  1.00 78.04  ? 99  VAL   a N   1 
ATOM   46682 C  CA  . VAL   AA 13 112 ? 55.705  -175.719 43.384  1.00 79.31  ? 99  VAL   a CA  1 
ATOM   46683 C  C   . VAL   AA 13 112 ? 55.252  -174.274 43.139  1.00 81.66  ? 99  VAL   a C   1 
ATOM   46684 O  O   . VAL   AA 13 112 ? 54.217  -174.084 42.466  1.00 78.42  ? 99  VAL   a O   1 
ATOM   46685 C  CB  . VAL   AA 13 112 ? 55.452  -176.148 44.842  1.00 79.63  ? 99  VAL   a CB  1 
ATOM   46686 C  CG1 . VAL   AA 13 112 ? 54.068  -175.747 45.331  1.00 79.85  ? 99  VAL   a CG1 1 
ATOM   46687 C  CG2 . VAL   AA 13 112 ? 55.666  -177.640 45.028  1.00 80.52  ? 99  VAL   a CG2 1 
ATOM   46688 N  N   . MET   AA 13 113 ? 55.993  -173.296 43.670  1.00 84.03  ? 100 MET   a N   1 
ATOM   46689 C  CA  . MET   AA 13 113 ? 55.623  -171.856 43.608  1.00 85.66  ? 100 MET   a CA  1 
ATOM   46690 C  C   . MET   AA 13 113 ? 55.452  -171.436 42.143  1.00 84.03  ? 100 MET   a C   1 
ATOM   46691 O  O   . MET   AA 13 113 ? 54.438  -170.770 41.845  1.00 84.27  ? 100 MET   a O   1 
ATOM   46692 C  CB  . MET   AA 13 113 ? 56.676  -170.965 44.279  1.00 86.10  ? 100 MET   a CB  1 
ATOM   46693 C  CG  . MET   AA 13 113 ? 56.779  -171.159 45.784  1.00 87.73  ? 100 MET   a CG  1 
ATOM   46694 S  SD  . MET   AA 13 113 ? 55.217  -170.869 46.653  1.00 90.23  ? 100 MET   a SD  1 
ATOM   46695 C  CE  . MET   AA 13 113 ? 55.254  -169.086 46.802  1.00 91.55  ? 100 MET   a CE  1 
ATOM   46696 N  N   . TYR   AA 13 114 ? 56.388  -171.825 41.267  1.00 83.27  ? 101 TYR   a N   1 
ATOM   46697 C  CA  . TYR   AA 13 114 ? 56.386  -171.457 39.825  1.00 81.77  ? 101 TYR   a CA  1 
ATOM   46698 C  C   . TYR   AA 13 114 ? 55.282  -172.219 39.081  1.00 82.12  ? 101 TYR   a C   1 
ATOM   46699 O  O   . TYR   AA 13 114 ? 54.674  -171.633 38.170  1.00 77.48  ? 101 TYR   a O   1 
ATOM   46700 C  CB  . TYR   AA 13 114 ? 57.745  -171.706 39.167  1.00 82.24  ? 101 TYR   a CB  1 
ATOM   46701 C  CG  . TYR   AA 13 114 ? 57.791  -171.276 37.722  1.00 81.89  ? 101 TYR   a CG  1 
ATOM   46702 C  CD1 . TYR   AA 13 114 ? 57.853  -169.934 37.378  1.00 80.95  ? 101 TYR   a CD1 1 
ATOM   46703 C  CD2 . TYR   AA 13 114 ? 57.724  -172.201 36.694  1.00 81.61  ? 101 TYR   a CD2 1 
ATOM   46704 C  CE1 . TYR   AA 13 114 ? 57.876  -169.525 36.055  1.00 79.69  ? 101 TYR   a CE1 1 
ATOM   46705 C  CE2 . TYR   AA 13 114 ? 57.749  -171.810 35.365  1.00 80.35  ? 101 TYR   a CE2 1 
ATOM   46706 C  CZ  . TYR   AA 13 114 ? 57.824  -170.467 35.043  1.00 79.56  ? 101 TYR   a CZ  1 
ATOM   46707 O  OH  . TYR   AA 13 114 ? 57.847  -170.075 33.737  1.00 77.97  ? 101 TYR   a OH  1 
ATOM   46708 N  N   . GLN   AA 13 115 ? 55.049  -173.485 39.440  1.00 85.14  ? 102 GLN   a N   1 
ATOM   46709 C  CA  . GLN   AA 13 115 ? 53.975  -174.332 38.849  1.00 89.31  ? 102 GLN   a CA  1 
ATOM   46710 C  C   . GLN   AA 13 115 ? 52.607  -173.707 39.153  1.00 88.45  ? 102 GLN   a C   1 
ATOM   46711 O  O   . GLN   AA 13 115 ? 51.744  -173.711 38.248  1.00 91.04  ? 102 GLN   a O   1 
ATOM   46712 C  CB  . GLN   AA 13 115 ? 54.039  -175.765 39.384  1.00 93.60  ? 102 GLN   a CB  1 
ATOM   46713 C  CG  . GLN   AA 13 115 ? 55.058  -176.640 38.666  1.00 99.13  ? 102 GLN   a CG  1 
ATOM   46714 C  CD  . GLN   AA 13 115 ? 54.958  -178.105 39.020  1.00 104.56 ? 102 GLN   a CD  1 
ATOM   46715 O  OE1 . GLN   AA 13 115 ? 55.338  -178.970 38.233  1.00 113.33 ? 102 GLN   a OE1 1 
ATOM   46716 N  NE2 . GLN   AA 13 115 ? 54.453  -178.407 40.207  1.00 109.20 ? 102 GLN   a NE2 1 
ATOM   46717 N  N   . ARG   AA 13 116 ? 52.420  -173.197 40.375  1.00 83.17  ? 103 ARG   a N   1 
ATOM   46718 C  CA  . ARG   AA 13 116 ? 51.136  -172.610 40.845  1.00 82.41  ? 103 ARG   a CA  1 
ATOM   46719 C  C   . ARG   AA 13 116 ? 50.889  -171.257 40.159  1.00 82.24  ? 103 ARG   a C   1 
ATOM   46720 O  O   . ARG   AA 13 116 ? 49.714  -170.969 39.847  1.00 81.29  ? 103 ARG   a O   1 
ATOM   46721 C  CB  . ARG   AA 13 116 ? 51.133  -172.476 42.372  1.00 79.90  ? 103 ARG   a CB  1 
ATOM   46722 C  CG  . ARG   AA 13 116 ? 51.008  -173.795 43.121  1.00 78.64  ? 103 ARG   a CG  1 
ATOM   46723 C  CD  . ARG   AA 13 116 ? 49.628  -174.410 42.988  1.00 79.04  ? 103 ARG   a CD  1 
ATOM   46724 N  NE  . ARG   AA 13 116 ? 48.582  -173.555 43.533  1.00 78.23  ? 103 ARG   a NE  1 
ATOM   46725 C  CZ  . ARG   AA 13 116 ? 48.086  -173.624 44.768  1.00 81.03  ? 103 ARG   a CZ  1 
ATOM   46726 N  NH1 . ARG   AA 13 116 ? 48.527  -174.521 45.636  1.00 80.11  ? 103 ARG   a NH1 1 
ATOM   46727 N  NH2 . ARG   AA 13 116 ? 47.133  -172.785 45.135  1.00 83.60  ? 103 ARG   a NH2 1 
ATOM   46728 N  N   . ARG   AA 13 117 ? 51.938  -170.454 39.931  1.00 82.92  ? 104 ARG   a N   1 
ATOM   46729 C  CA  . ARG   AA 13 117 ? 51.820  -169.146 39.225  1.00 82.34  ? 104 ARG   a CA  1 
ATOM   46730 C  C   . ARG   AA 13 117 ? 51.469  -169.419 37.757  1.00 78.83  ? 104 ARG   a C   1 
ATOM   46731 O  O   . ARG   AA 13 117 ? 50.723  -168.615 37.174  1.00 80.05  ? 104 ARG   a O   1 
ATOM   46732 C  CB  . ARG   AA 13 117 ? 53.088  -168.293 39.388  1.00 84.40  ? 104 ARG   a CB  1 
ATOM   46733 C  CG  . ARG   AA 13 117 ? 54.108  -168.393 38.260  1.00 86.47  ? 104 ARG   a CG  1 
ATOM   46734 C  CD  . ARG   AA 13 117 ? 53.931  -167.364 37.151  1.00 86.94  ? 104 ARG   a CD  1 
ATOM   46735 N  NE  . ARG   AA 13 117 ? 54.233  -167.911 35.828  1.00 87.24  ? 104 ARG   a NE  1 
ATOM   46736 C  CZ  . ARG   AA 13 117 ? 54.423  -167.198 34.716  1.00 85.27  ? 104 ARG   a CZ  1 
ATOM   46737 N  NH1 . ARG   AA 13 117 ? 54.356  -165.878 34.736  1.00 85.16  ? 104 ARG   a NH1 1 
ATOM   46738 N  NH2 . ARG   AA 13 117 ? 54.688  -167.815 33.577  1.00 85.20  ? 104 ARG   a NH2 1 
ATOM   46739 N  N   . SER   AA 13 118 ? 51.968  -170.527 37.200  1.00 78.50  ? 105 SER   a N   1 
ATOM   46740 C  CA  . SER   AA 13 118 ? 51.790  -170.922 35.778  1.00 78.32  ? 105 SER   a CA  1 
ATOM   46741 C  C   . SER   AA 13 118 ? 50.376  -171.470 35.549  1.00 78.58  ? 105 SER   a C   1 
ATOM   46742 O  O   . SER   AA 13 118 ? 49.931  -171.455 34.387  1.00 77.67  ? 105 SER   a O   1 
ATOM   46743 C  CB  . SER   AA 13 118 ? 52.842  -171.911 35.356  1.00 78.33  ? 105 SER   a CB  1 
ATOM   46744 O  OG  . SER   AA 13 118 ? 54.140  -171.341 35.453  1.00 76.15  ? 105 SER   a OG  1 
ATOM   46745 N  N   . LYS   AA 13 119 ? 49.707  -171.941 36.609  1.00 82.49  ? 106 LYS   a N   1 
ATOM   46746 C  CA  . LYS   AA 13 119 ? 48.288  -172.395 36.579  1.00 86.28  ? 106 LYS   a CA  1 
ATOM   46747 C  C   . LYS   AA 13 119 ? 47.365  -171.241 37.000  1.00 84.32  ? 106 LYS   a C   1 
ATOM   46748 O  O   . LYS   AA 13 119 ? 46.155  -171.488 37.159  1.00 81.12  ? 106 LYS   a O   1 
ATOM   46749 C  CB  . LYS   AA 13 119 ? 48.099  -173.629 37.471  1.00 94.27  ? 106 LYS   a CB  1 
ATOM   46750 C  CG  . LYS   AA 13 119 ? 48.335  -174.966 36.778  1.00 99.75  ? 106 LYS   a CG  1 
ATOM   46751 C  CD  . LYS   AA 13 119 ? 48.664  -176.103 37.727  1.00 106.03 ? 106 LYS   a CD  1 
ATOM   46752 C  CE  . LYS   AA 13 119 ? 47.494  -176.532 38.590  1.00 112.12 ? 106 LYS   a CE  1 
ATOM   46753 N  NZ  . LYS   AA 13 119 ? 47.937  -177.356 39.741  1.00 113.14 ? 106 LYS   a NZ  1 
ATOM   46754 N  N   . MET   AA 13 120 ? 47.920  -170.034 37.173  1.00 86.36  ? 107 MET   a N   1 
ATOM   46755 C  CA  . MET   AA 13 120 ? 47.188  -168.783 37.522  1.00 88.29  ? 107 MET   a CA  1 
ATOM   46756 C  C   . MET   AA 13 120 ? 46.448  -168.956 38.855  1.00 87.49  ? 107 MET   a C   1 
ATOM   46757 O  O   . MET   AA 13 120 ? 45.399  -168.308 39.042  1.00 90.78  ? 107 MET   a O   1 
ATOM   46758 C  CB  . MET   AA 13 120 ? 46.188  -168.399 36.423  1.00 91.01  ? 107 MET   a CB  1 
ATOM   46759 C  CG  . MET   AA 13 120 ? 46.840  -167.928 35.133  1.00 90.90  ? 107 MET   a CG  1 
ATOM   46760 S  SD  . MET   AA 13 120 ? 47.838  -166.425 35.335  1.00 91.65  ? 107 MET   a SD  1 
ATOM   46761 C  CE  . MET   AA 13 120 ? 46.570  -165.208 35.681  1.00 90.02  ? 107 MET   a CE  1 
ATOM   46762 N  N   . ASN   AA 13 121 ? 46.978  -169.787 39.754  1.00 85.21  ? 108 ASN   a N   1 
ATOM   46763 C  CA  . ASN   AA 13 121 ? 46.425  -169.994 41.117  1.00 85.87  ? 108 ASN   a CA  1 
ATOM   46764 C  C   . ASN   AA 13 121 ? 47.597  -170.082 42.087  1.00 85.92  ? 108 ASN   a C   1 
ATOM   46765 O  O   . ASN   AA 13 121 ? 47.953  -171.167 42.536  1.00 84.73  ? 108 ASN   a O   1 
ATOM   46766 C  CB  . ASN   AA 13 121 ? 45.502  -171.215 41.161  1.00 85.14  ? 108 ASN   a CB  1 
ATOM   46767 C  CG  . ASN   AA 13 121 ? 44.940  -171.510 42.537  1.00 87.08  ? 108 ASN   a CG  1 
ATOM   46768 O  OD1 . ASN   AA 13 121 ? 44.833  -172.672 42.921  1.00 83.59  ? 108 ASN   a OD1 1 
ATOM   46769 N  ND2 . ASN   AA 13 121 ? 44.572  -170.481 43.287  1.00 86.48  ? 108 ASN   a ND2 1 
ATOM   46770 N  N   . PRO   AA 13 122 ? 48.229  -168.938 42.434  1.00 90.94  ? 109 PRO   a N   1 
ATOM   46771 C  CA  . PRO   AA 13 122 ? 49.489  -168.944 43.177  1.00 90.03  ? 109 PRO   a CA  1 
ATOM   46772 C  C   . PRO   AA 13 122 ? 49.306  -169.137 44.686  1.00 88.14  ? 109 PRO   a C   1 
ATOM   46773 O  O   . PRO   AA 13 122 ? 48.248  -168.813 45.192  1.00 94.82  ? 109 PRO   a O   1 
ATOM   46774 C  CB  . PRO   AA 13 122 ? 50.034  -167.535 42.911  1.00 92.54  ? 109 PRO   a CB  1 
ATOM   46775 C  CG  . PRO   AA 13 122 ? 48.783  -166.680 42.809  1.00 92.48  ? 109 PRO   a CG  1 
ATOM   46776 C  CD  . PRO   AA 13 122 ? 47.750  -167.574 42.155  1.00 90.18  ? 109 PRO   a CD  1 
ATOM   46777 N  N   . LEU   AA 13 123 ? 50.340  -169.650 45.357  1.00 89.89  ? 110 LEU   a N   1 
ATOM   46778 C  CA  . LEU   AA 13 123 ? 50.484  -169.566 46.834  1.00 90.50  ? 110 LEU   a CA  1 
ATOM   46779 C  C   . LEU   AA 13 123 ? 51.016  -168.167 47.158  1.00 89.54  ? 110 LEU   a C   1 
ATOM   46780 O  O   . LEU   AA 13 123 ? 52.166  -167.869 46.775  1.00 87.43  ? 110 LEU   a O   1 
ATOM   46781 C  CB  . LEU   AA 13 123 ? 51.430  -170.665 47.329  1.00 90.11  ? 110 LEU   a CB  1 
ATOM   46782 C  CG  . LEU   AA 13 123 ? 50.937  -172.100 47.146  1.00 87.37  ? 110 LEU   a CG  1 
ATOM   46783 C  CD1 . LEU   AA 13 123 ? 52.064  -173.090 47.395  1.00 86.51  ? 110 LEU   a CD1 1 
ATOM   46784 C  CD2 . LEU   AA 13 123 ? 49.756  -172.399 48.059  1.00 85.55  ? 110 LEU   a CD2 1 
ATOM   46785 N  N   . TRP   AA 13 124 ? 50.193  -167.336 47.803  1.00 90.15  ? 111 TRP   a N   1 
ATOM   46786 C  CA  . TRP   AA 13 124 ? 50.426  -165.873 47.954  1.00 87.33  ? 111 TRP   a CA  1 
ATOM   46787 C  C   . TRP   AA 13 124 ? 51.479  -165.617 49.038  1.00 83.29  ? 111 TRP   a C   1 
ATOM   46788 O  O   . TRP   AA 13 124 ? 51.115  -165.077 50.105  1.00 79.42  ? 111 TRP   a O   1 
ATOM   46789 C  CB  . TRP   AA 13 124 ? 49.107  -165.146 48.251  1.00 90.35  ? 111 TRP   a CB  1 
ATOM   46790 C  CG  . TRP   AA 13 124 ? 49.092  -163.730 47.766  1.00 88.99  ? 111 TRP   a CG  1 
ATOM   46791 C  CD1 . TRP   AA 13 124 ? 49.662  -162.646 48.364  1.00 89.58  ? 111 TRP   a CD1 1 
ATOM   46792 C  CD2 . TRP   AA 13 124 ? 48.483  -163.249 46.557  1.00 89.54  ? 111 TRP   a CD2 1 
ATOM   46793 N  NE1 . TRP   AA 13 124 ? 49.443  -161.522 47.613  1.00 90.60  ? 111 TRP   a NE1 1 
ATOM   46794 C  CE2 . TRP   AA 13 124 ? 48.727  -161.862 46.497  1.00 88.57  ? 111 TRP   a CE2 1 
ATOM   46795 C  CE3 . TRP   AA 13 124 ? 47.756  -163.853 45.526  1.00 90.71  ? 111 TRP   a CE3 1 
ATOM   46796 C  CZ2 . TRP   AA 13 124 ? 48.262  -161.072 45.447  1.00 91.10  ? 111 TRP   a CZ2 1 
ATOM   46797 C  CZ3 . TRP   AA 13 124 ? 47.300  -163.074 44.486  1.00 90.88  ? 111 TRP   a CZ3 1 
ATOM   46798 C  CH2 . TRP   AA 13 124 ? 47.551  -161.701 44.449  1.00 90.64  ? 111 TRP   a CH2 1 
ATOM   46799 N  N   . ASN   AA 13 125 ? 52.738  -165.966 48.758  1.00 79.77  ? 112 ASN   a N   1 
ATOM   46800 C  CA  . ASN   AA 13 125 ? 53.825  -166.013 49.770  1.00 80.22  ? 112 ASN   a CA  1 
ATOM   46801 C  C   . ASN   AA 13 125 ? 55.141  -165.506 49.180  1.00 79.89  ? 112 ASN   a C   1 
ATOM   46802 O  O   . ASN   AA 13 125 ? 55.374  -165.709 47.977  1.00 82.39  ? 112 ASN   a O   1 
ATOM   46803 C  CB  . ASN   AA 13 125 ? 54.034  -167.432 50.299  1.00 80.75  ? 112 ASN   a CB  1 
ATOM   46804 C  CG  . ASN   AA 13 125 ? 52.819  -167.973 51.021  1.00 82.28  ? 112 ASN   a CG  1 
ATOM   46805 O  OD1 . ASN   AA 13 125 ? 52.234  -168.968 50.599  1.00 81.97  ? 112 ASN   a OD1 1 
ATOM   46806 N  ND2 . ASN   AA 13 125 ? 52.423  -167.313 52.097  1.00 85.22  ? 112 ASN   a ND2 1 
ATOM   46807 N  N   . ALA   AA 13 126 ? 55.945  -164.855 50.023  1.00 82.08  ? 113 ALA   a N   1 
ATOM   46808 C  CA  . ALA   AA 13 126 ? 57.402  -164.670 49.857  1.00 84.34  ? 113 ALA   a CA  1 
ATOM   46809 C  C   . ALA   AA 13 126 ? 58.086  -165.601 50.861  1.00 82.53  ? 113 ALA   a C   1 
ATOM   46810 O  O   . ALA   AA 13 126 ? 57.695  -165.578 52.046  1.00 78.95  ? 113 ALA   a O   1 
ATOM   46811 C  CB  . ALA   AA 13 126 ? 57.785  -163.225 50.067  1.00 86.22  ? 113 ALA   a CB  1 
ATOM   46812 N  N   . ILE   AA 13 127 ? 59.029  -166.419 50.391  1.00 82.91  ? 114 ILE   a N   1 
ATOM   46813 C  CA  . ILE   AA 13 127 ? 59.663  -167.511 51.185  1.00 86.02  ? 114 ILE   a CA  1 
ATOM   46814 C  C   . ILE   AA 13 127 ? 61.183  -167.345 51.133  1.00 83.61  ? 114 ILE   a C   1 
ATOM   46815 O  O   . ILE   AA 13 127 ? 61.721  -167.145 50.028  1.00 82.84  ? 114 ILE   a O   1 
ATOM   46816 C  CB  . ILE   AA 13 127 ? 59.219  -168.892 50.659  1.00 86.82  ? 114 ILE   a CB  1 
ATOM   46817 C  CG1 . ILE   AA 13 127 ? 57.706  -169.086 50.800  1.00 88.69  ? 114 ILE   a CG1 1 
ATOM   46818 C  CG2 . ILE   AA 13 127 ? 59.999  -170.008 51.342  1.00 88.80  ? 114 ILE   a CG2 1 
ATOM   46819 C  CD1 . ILE   AA 13 127 ? 57.155  -170.243 50.004  1.00 89.57  ? 114 ILE   a CD1 1 
ATOM   46820 N  N   . ILE   AA 13 128 ? 61.836  -167.436 52.293  1.00 85.25  ? 115 ILE   a N   1 
ATOM   46821 C  CA  . ILE   AA 13 128 ? 63.320  -167.501 52.426  1.00 87.96  ? 115 ILE   a CA  1 
ATOM   46822 C  C   . ILE   AA 13 128 ? 63.673  -168.832 53.096  1.00 86.27  ? 115 ILE   a C   1 
ATOM   46823 O  O   . ILE   AA 13 128 ? 63.163  -169.094 54.205  1.00 86.09  ? 115 ILE   a O   1 
ATOM   46824 C  CB  . ILE   AA 13 128 ? 63.870  -166.287 53.202  1.00 89.88  ? 115 ILE   a CB  1 
ATOM   46825 C  CG1 . ILE   AA 13 128 ? 63.640  -164.982 52.434  1.00 92.20  ? 115 ILE   a CG1 1 
ATOM   46826 C  CG2 . ILE   AA 13 128 ? 65.341  -166.485 53.546  1.00 91.90  ? 115 ILE   a CG2 1 
ATOM   46827 C  CD1 . ILE   AA 13 128 ? 63.949  -163.730 53.224  1.00 93.85  ? 115 ILE   a CD1 1 
ATOM   46828 N  N   . VAL   AA 13 129 ? 64.499  -169.638 52.425  1.00 85.98  ? 116 VAL   a N   1 
ATOM   46829 C  CA  . VAL   AA 13 129 ? 65.031  -170.934 52.938  1.00 86.50  ? 116 VAL   a CA  1 
ATOM   46830 C  C   . VAL   AA 13 129 ? 66.457  -170.692 53.432  1.00 83.58  ? 116 VAL   a C   1 
ATOM   46831 O  O   . VAL   AA 13 129 ? 67.336  -170.445 52.589  1.00 83.70  ? 116 VAL   a O   1 
ATOM   46832 C  CB  . VAL   AA 13 129 ? 64.994  -172.027 51.855  1.00 87.68  ? 116 VAL   a CB  1 
ATOM   46833 C  CG1 . VAL   AA 13 129 ? 65.703  -173.296 52.305  1.00 88.96  ? 116 VAL   a CG1 1 
ATOM   46834 C  CG2 . VAL   AA 13 129 ? 63.569  -172.332 51.419  1.00 89.14  ? 116 VAL   a CG2 1 
ATOM   46835 N  N   . ALA   AA 13 130 ? 66.662  -170.760 54.748  1.00 84.40  ? 117 ALA   a N   1 
ATOM   46836 C  CA  . ALA   AA 13 130 ? 67.972  -170.585 55.413  1.00 88.02  ? 117 ALA   a CA  1 
ATOM   46837 C  C   . ALA   AA 13 130 ? 68.407  -171.922 56.015  1.00 90.28  ? 117 ALA   a C   1 
ATOM   46838 O  O   . ALA   AA 13 130 ? 67.584  -172.550 56.711  1.00 91.98  ? 117 ALA   a O   1 
ATOM   46839 C  CB  . ALA   AA 13 130 ? 67.873  -169.511 56.466  1.00 89.44  ? 117 ALA   a CB  1 
ATOM   46840 N  N   . GLY   AA 13 131 ? 69.646  -172.342 55.747  1.00 91.52  ? 118 GLY   a N   1 
ATOM   46841 C  CA  . GLY   AA 13 131 ? 70.216  -173.578 56.314  1.00 93.39  ? 118 GLY   a CA  1 
ATOM   46842 C  C   . GLY   AA 13 131 ? 71.709  -173.707 56.072  1.00 92.66  ? 118 GLY   a C   1 
ATOM   46843 O  O   . GLY   AA 13 131 ? 72.324  -172.756 55.544  1.00 88.18  ? 118 GLY   a O   1 
ATOM   46844 N  N   . VAL   AA 13 132 ? 72.267  -174.854 56.468  1.00 94.83  ? 119 VAL   a N   1 
ATOM   46845 C  CA  . VAL   AA 13 132 ? 73.683  -175.254 56.225  1.00 95.31  ? 119 VAL   a CA  1 
ATOM   46846 C  C   . VAL   AA 13 132 ? 73.670  -176.596 55.485  1.00 96.62  ? 119 VAL   a C   1 
ATOM   46847 O  O   . VAL   AA 13 132 ? 72.953  -177.511 55.936  1.00 97.58  ? 119 VAL   a O   1 
ATOM   46848 C  CB  . VAL   AA 13 132 ? 74.477  -175.331 57.543  1.00 94.81  ? 119 VAL   a CB  1 
ATOM   46849 C  CG1 . VAL   AA 13 132 ? 75.870  -175.904 57.338  1.00 96.37  ? 119 VAL   a CG1 1 
ATOM   46850 C  CG2 . VAL   AA 13 132 ? 74.560  -173.976 58.225  1.00 94.67  ? 119 VAL   a CG2 1 
ATOM   46851 N  N   . GLN   AA 13 133 ? 74.427  -176.693 54.387  1.00 98.59  ? 120 GLN   a N   1 
ATOM   46852 C  CA  . GLN   AA 13 133 ? 74.570  -177.925 53.566  1.00 100.42 ? 120 GLN   a CA  1 
ATOM   46853 C  C   . GLN   AA 13 133 ? 75.423  -178.943 54.336  1.00 102.00 ? 120 GLN   a C   1 
ATOM   46854 O  O   . GLN   AA 13 133 ? 75.994  -178.575 55.384  1.00 98.76  ? 120 GLN   a O   1 
ATOM   46855 C  CB  . GLN   AA 13 133 ? 75.184  -177.589 52.204  1.00 100.60 ? 120 GLN   a CB  1 
ATOM   46856 C  CG  . GLN   AA 13 133 ? 74.323  -176.672 51.343  1.00 98.32  ? 120 GLN   a CG  1 
ATOM   46857 C  CD  . GLN   AA 13 133 ? 73.082  -177.354 50.815  1.00 97.05  ? 120 GLN   a CD  1 
ATOM   46858 O  OE1 . GLN   AA 13 133 ? 71.980  -177.170 51.327  1.00 95.09  ? 120 GLN   a OE1 1 
ATOM   46859 N  NE2 . GLN   AA 13 133 ? 73.252  -178.158 49.779  1.00 98.04  ? 120 GLN   a NE2 1 
ATOM   46860 N  N   . SER   AA 13 134 ? 75.516  -180.173 53.823  1.00 102.70 ? 121 SER   a N   1 
ATOM   46861 C  CA  . SER   AA 13 134 ? 76.242  -181.307 54.453  1.00 104.90 ? 121 SER   a CA  1 
ATOM   46862 C  C   . SER   AA 13 134 ? 77.749  -181.024 54.472  1.00 104.60 ? 121 SER   a C   1 
ATOM   46863 O  O   . SER   AA 13 134 ? 78.424  -181.525 55.389  1.00 106.17 ? 121 SER   a O   1 
ATOM   46864 C  CB  . SER   AA 13 134 ? 75.935  -182.605 53.751  1.00 105.66 ? 121 SER   a CB  1 
ATOM   46865 O  OG  . SER   AA 13 134 ? 76.412  -182.590 52.414  1.00 111.65 ? 121 SER   a OG  1 
ATOM   46866 N  N   . ASN   AA 13 135 ? 78.250  -180.246 53.503  1.00 104.74 ? 122 ASN   a N   1 
ATOM   46867 C  CA  . ASN   AA 13 135 ? 79.691  -179.899 53.355  1.00 106.08 ? 122 ASN   a CA  1 
ATOM   46868 C  C   . ASN   AA 13 135 ? 80.020  -178.622 54.141  1.00 104.55 ? 122 ASN   a C   1 
ATOM   46869 O  O   . ASN   AA 13 135 ? 81.152  -178.130 53.986  1.00 105.28 ? 122 ASN   a O   1 
ATOM   46870 C  CB  . ASN   AA 13 135 ? 80.087  -179.749 51.883  1.00 108.58 ? 122 ASN   a CB  1 
ATOM   46871 C  CG  . ASN   AA 13 135 ? 79.407  -178.580 51.202  1.00 107.60 ? 122 ASN   a CG  1 
ATOM   46872 O  OD1 . ASN   AA 13 135 ? 78.412  -178.059 51.700  1.00 107.94 ? 122 ASN   a OD1 1 
ATOM   46873 N  ND2 . ASN   AA 13 135 ? 79.928  -178.171 50.057  1.00 111.93 ? 122 ASN   a ND2 1 
ATOM   46874 N  N   . GLY   AA 13 136 ? 79.073  -178.103 54.934  1.00 103.42 ? 123 GLY   a N   1 
ATOM   46875 C  CA  . GLY   AA 13 136 ? 79.280  -176.951 55.837  1.00 106.34 ? 123 GLY   a CA  1 
ATOM   46876 C  C   . GLY   AA 13 136 ? 78.939  -175.609 55.200  1.00 107.12 ? 123 GLY   a C   1 
ATOM   46877 O  O   . GLY   AA 13 136 ? 78.936  -174.600 55.936  1.00 108.04 ? 123 GLY   a O   1 
ATOM   46878 N  N   . ASP   AA 13 137 ? 78.661  -175.577 53.891  1.00 105.87 ? 124 ASP   a N   1 
ATOM   46879 C  CA  . ASP   AA 13 137 ? 78.364  -174.333 53.128  1.00 104.30 ? 124 ASP   a CA  1 
ATOM   46880 C  C   . ASP   AA 13 137 ? 77.070  -173.702 53.653  1.00 103.68 ? 124 ASP   a C   1 
ATOM   46881 O  O   . ASP   AA 13 137 ? 76.123  -174.453 53.958  1.00 107.42 ? 124 ASP   a O   1 
ATOM   46882 C  CB  . ASP   AA 13 137 ? 78.231  -174.599 51.626  1.00 103.29 ? 124 ASP   a CB  1 
ATOM   46883 C  CG  . ASP   AA 13 137 ? 79.551  -174.794 50.901  1.00 103.76 ? 124 ASP   a CG  1 
ATOM   46884 O  OD1 . ASP   AA 13 137 ? 80.603  -174.482 51.494  1.00 105.85 ? 124 ASP   a OD1 1 
ATOM   46885 O  OD2 . ASP   AA 13 137 ? 79.514  -175.251 49.744  1.00 104.35 ? 124 ASP   a OD2 1 
ATOM   46886 N  N   . GLN   AA 13 138 ? 77.038  -172.370 53.740  1.00 102.22 ? 125 GLN   a N   1 
ATOM   46887 C  CA  . GLN   AA 13 138 ? 75.820  -171.590 54.081  1.00 102.08 ? 125 GLN   a CA  1 
ATOM   46888 C  C   . GLN   AA 13 138 ? 74.855  -171.672 52.896  1.00 96.68  ? 125 GLN   a C   1 
ATOM   46889 O  O   . GLN   AA 13 138 ? 75.328  -171.551 51.750  1.00 93.79  ? 125 GLN   a O   1 
ATOM   46890 C  CB  . GLN   AA 13 138 ? 76.163  -170.128 54.383  1.00 102.19 ? 125 GLN   a CB  1 
ATOM   46891 C  CG  . GLN   AA 13 138 ? 77.087  -169.936 55.578  1.00 104.89 ? 125 GLN   a CG  1 
ATOM   46892 C  CD  . GLN   AA 13 138 ? 78.530  -169.736 55.179  1.00 108.43 ? 125 GLN   a CD  1 
ATOM   46893 O  OE1 . GLN   AA 13 138 ? 79.037  -170.388 54.268  1.00 111.87 ? 125 GLN   a OE1 1 
ATOM   46894 N  NE2 . GLN   AA 13 138 ? 79.208  -168.830 55.865  1.00 108.33 ? 125 GLN   a NE2 1 
ATOM   46895 N  N   . PHE   AA 13 139 ? 73.564  -171.893 53.160  1.00 98.67  ? 126 PHE   a N   1 
ATOM   46896 C  CA  . PHE   AA 13 139 ? 72.477  -171.810 52.149  1.00 101.50 ? 126 PHE   a CA  1 
ATOM   46897 C  C   . PHE   AA 13 139 ? 71.455  -170.754 52.579  1.00 100.75 ? 126 PHE   a C   1 
ATOM   46898 O  O   . PHE   AA 13 139 ? 70.877  -170.873 53.679  1.00 102.50 ? 126 PHE   a O   1 
ATOM   46899 C  CB  . PHE   AA 13 139 ? 71.778  -173.155 51.942  1.00 102.02 ? 126 PHE   a CB  1 
ATOM   46900 C  CG  . PHE   AA 13 139 ? 70.821  -173.155 50.777  1.00 101.67 ? 126 PHE   a CG  1 
ATOM   46901 C  CD1 . PHE   AA 13 139 ? 69.483  -172.829 50.951  1.00 100.80 ? 126 PHE   a CD1 1 
ATOM   46902 C  CD2 . PHE   AA 13 139 ? 71.267  -173.446 49.497  1.00 102.84 ? 126 PHE   a CD2 1 
ATOM   46903 C  CE1 . PHE   AA 13 139 ? 68.609  -172.815 49.873  1.00 98.74  ? 126 PHE   a CE1 1 
ATOM   46904 C  CE2 . PHE   AA 13 139 ? 70.393  -173.432 48.420  1.00 102.12 ? 126 PHE   a CE2 1 
ATOM   46905 C  CZ  . PHE   AA 13 139 ? 69.066  -173.116 48.609  1.00 100.58 ? 126 PHE   a CZ  1 
ATOM   46906 N  N   . LEU   AA 13 140 ? 71.239  -169.758 51.717  1.00 98.46  ? 127 LEU   a N   1 
ATOM   46907 C  CA  . LEU   AA 13 140 ? 70.224  -168.690 51.899  1.00 94.53  ? 127 LEU   a CA  1 
ATOM   46908 C  C   . LEU   AA 13 140 ? 69.687  -168.304 50.519  1.00 88.89  ? 127 LEU   a C   1 
ATOM   46909 O  O   . LEU   AA 13 140 ? 70.475  -167.778 49.716  1.00 93.83  ? 127 LEU   a O   1 
ATOM   46910 C  CB  . LEU   AA 13 140 ? 70.879  -167.497 52.603  1.00 95.27  ? 127 LEU   a CB  1 
ATOM   46911 C  CG  . LEU   AA 13 140 ? 69.915  -166.444 53.146  1.00 95.93  ? 127 LEU   a CG  1 
ATOM   46912 C  CD1 . LEU   AA 13 140 ? 69.169  -166.966 54.364  1.00 96.11  ? 127 LEU   a CD1 1 
ATOM   46913 C  CD2 . LEU   AA 13 140 ? 70.651  -165.156 53.480  1.00 98.04  ? 127 LEU   a CD2 1 
ATOM   46914 N  N   . ARG   AA 13 141 ? 68.413  -168.589 50.240  1.00 86.50  ? 128 ARG   a N   1 
ATOM   46915 C  CA  . ARG   AA 13 141 ? 67.787  -168.267 48.930  1.00 87.95  ? 128 ARG   a CA  1 
ATOM   46916 C  C   . ARG   AA 13 141 ? 66.311  -167.897 49.122  1.00 89.21  ? 128 ARG   a C   1 
ATOM   46917 O  O   . ARG   AA 13 141 ? 65.670  -168.422 50.055  1.00 91.27  ? 128 ARG   a O   1 
ATOM   46918 C  CB  . ARG   AA 13 141 ? 67.966  -169.429 47.948  1.00 86.82  ? 128 ARG   a CB  1 
ATOM   46919 C  CG  . ARG   AA 13 141 ? 67.873  -169.006 46.489  1.00 86.19  ? 128 ARG   a CG  1 
ATOM   46920 C  CD  . ARG   AA 13 141 ? 68.291  -170.087 45.514  1.00 86.46  ? 128 ARG   a CD  1 
ATOM   46921 N  NE  . ARG   AA 13 141 ? 67.970  -169.711 44.142  1.00 86.42  ? 128 ARG   a NE  1 
ATOM   46922 C  CZ  . ARG   AA 13 141 ? 68.716  -168.931 43.358  1.00 87.21  ? 128 ARG   a CZ  1 
ATOM   46923 N  NH1 . ARG   AA 13 141 ? 69.858  -168.427 43.793  1.00 87.98  ? 128 ARG   a NH1 1 
ATOM   46924 N  NH2 . ARG   AA 13 141 ? 68.312  -168.657 42.130  1.00 88.32  ? 128 ARG   a NH2 1 
ATOM   46925 N  N   . TYR   AA 13 142 ? 65.816  -167.019 48.245  1.00 87.65  ? 129 TYR   a N   1 
ATOM   46926 C  CA  . TYR   AA 13 142 ? 64.459  -166.411 48.261  1.00 88.73  ? 129 TYR   a CA  1 
ATOM   46927 C  C   . TYR   AA 13 142 ? 63.627  -166.992 47.114  1.00 84.77  ? 129 TYR   a C   1 
ATOM   46928 O  O   . TYR   AA 13 142 ? 64.195  -167.245 46.041  1.00 89.34  ? 129 TYR   a O   1 
ATOM   46929 C  CB  . TYR   AA 13 142 ? 64.585  -164.890 48.126  1.00 87.53  ? 129 TYR   a CB  1 
ATOM   46930 C  CG  . TYR   AA 13 142 ? 63.304  -164.127 47.895  1.00 86.56  ? 129 TYR   a CG  1 
ATOM   46931 C  CD1 . TYR   AA 13 142 ? 62.724  -164.052 46.638  1.00 88.60  ? 129 TYR   a CD1 1 
ATOM   46932 C  CD2 . TYR   AA 13 142 ? 62.692  -163.435 48.928  1.00 85.69  ? 129 TYR   a CD2 1 
ATOM   46933 C  CE1 . TYR   AA 13 142 ? 61.559  -163.333 46.417  1.00 89.34  ? 129 TYR   a CE1 1 
ATOM   46934 C  CE2 . TYR   AA 13 142 ? 61.528  -162.711 48.724  1.00 86.13  ? 129 TYR   a CE2 1 
ATOM   46935 C  CZ  . TYR   AA 13 142 ? 60.959  -162.658 47.466  1.00 86.37  ? 129 TYR   a CZ  1 
ATOM   46936 O  OH  . TYR   AA 13 142 ? 59.815  -161.940 47.279  1.00 89.57  ? 129 TYR   a OH  1 
ATOM   46937 N  N   . VAL   AA 13 143 ? 62.325  -167.179 47.337  1.00 79.71  ? 130 VAL   a N   1 
ATOM   46938 C  CA  . VAL   AA 13 143 ? 61.333  -167.533 46.278  1.00 81.21  ? 130 VAL   a CA  1 
ATOM   46939 C  C   . VAL   AA 13 143 ? 59.970  -166.973 46.698  1.00 77.07  ? 130 VAL   a C   1 
ATOM   46940 O  O   . VAL   AA 13 143 ? 59.693  -166.957 47.912  1.00 74.97  ? 130 VAL   a O   1 
ATOM   46941 C  CB  . VAL   AA 13 143 ? 61.279  -169.052 46.016  1.00 82.90  ? 130 VAL   a CB  1 
ATOM   46942 C  CG1 . VAL   AA 13 143 ? 60.806  -169.838 47.232  1.00 85.75  ? 130 VAL   a CG1 1 
ATOM   46943 C  CG2 . VAL   AA 13 143 ? 60.425  -169.380 44.801  1.00 82.64  ? 130 VAL   a CG2 1 
ATOM   46944 N  N   . ASN   AA 13 144 ? 59.160  -166.531 45.730  1.00 75.89  ? 131 ASN   a N   1 
ATOM   46945 C  CA  . ASN   AA 13 144 ? 57.873  -165.830 45.985  1.00 78.10  ? 131 ASN   a CA  1 
ATOM   46946 C  C   . ASN   AA 13 144 ? 56.769  -166.376 45.070  1.00 76.25  ? 131 ASN   a C   1 
ATOM   46947 O  O   . ASN   AA 13 144 ? 57.052  -167.291 44.276  1.00 77.85  ? 131 ASN   a O   1 
ATOM   46948 C  CB  . ASN   AA 13 144 ? 58.029  -164.314 45.831  1.00 78.51  ? 131 ASN   a CB  1 
ATOM   46949 C  CG  . ASN   AA 13 144 ? 58.273  -163.871 44.404  1.00 79.56  ? 131 ASN   a CG  1 
ATOM   46950 O  OD1 . ASN   AA 13 144 ? 58.277  -164.677 43.477  1.00 79.83  ? 131 ASN   a OD1 1 
ATOM   46951 N  ND2 . ASN   AA 13 144 ? 58.477  -162.581 44.216  1.00 79.16  ? 131 ASN   a ND2 1 
ATOM   46952 N  N   . LEU   AA 13 145 ? 55.566  -165.802 45.178  1.00 77.30  ? 132 LEU   a N   1 
ATOM   46953 C  CA  . LEU   AA 13 145 ? 54.325  -166.236 44.476  1.00 76.97  ? 132 LEU   a CA  1 
ATOM   46954 C  C   . LEU   AA 13 145 ? 54.510  -166.238 42.951  1.00 76.08  ? 132 LEU   a C   1 
ATOM   46955 O  O   . LEU   AA 13 145 ? 53.757  -166.967 42.287  1.00 75.31  ? 132 LEU   a O   1 
ATOM   46956 C  CB  . LEU   AA 13 145 ? 53.157  -165.334 44.896  1.00 76.20  ? 132 LEU   a CB  1 
ATOM   46957 C  CG  . LEU   AA 13 145 ? 53.078  -163.947 44.257  1.00 77.14  ? 132 LEU   a CG  1 
ATOM   46958 C  CD1 . LEU   AA 13 145 ? 51.721  -163.320 44.540  1.00 74.47  ? 132 LEU   a CD1 1 
ATOM   46959 C  CD2 . LEU   AA 13 145 ? 54.193  -163.040 44.753  1.00 76.04  ? 132 LEU   a CD2 1 
ATOM   46960 N  N   . LEU   AA 13 146 ? 55.455  -165.458 42.415  1.00 78.76  ? 133 LEU   a N   1 
ATOM   46961 C  CA  . LEU   AA 13 146 ? 55.755  -165.397 40.956  1.00 80.56  ? 133 LEU   a CA  1 
ATOM   46962 C  C   . LEU   AA 13 146 ? 56.698  -166.534 40.549  1.00 79.14  ? 133 LEU   a C   1 
ATOM   46963 O  O   . LEU   AA 13 146 ? 56.865  -166.736 39.331  1.00 77.24  ? 133 LEU   a O   1 
ATOM   46964 C  CB  . LEU   AA 13 146 ? 56.400  -164.050 40.611  1.00 81.89  ? 133 LEU   a CB  1 
ATOM   46965 C  CG  . LEU   AA 13 146 ? 55.501  -162.820 40.713  1.00 83.48  ? 133 LEU   a CG  1 
ATOM   46966 C  CD1 . LEU   AA 13 146 ? 56.306  -161.559 40.435  1.00 85.22  ? 133 LEU   a CD1 1 
ATOM   46967 C  CD2 . LEU   AA 13 146 ? 54.314  -162.915 39.765  1.00 81.15  ? 133 LEU   a CD2 1 
ATOM   46968 N  N   . GLY   AA 13 147 ? 57.313  -167.218 41.518  1.00 80.19  ? 134 GLY   a N   1 
ATOM   46969 C  CA  . GLY   AA 13 147 ? 58.353  -168.238 41.274  1.00 82.65  ? 134 GLY   a CA  1 
ATOM   46970 C  C   . GLY   AA 13 147 ? 59.700  -167.606 40.960  1.00 84.19  ? 134 GLY   a C   1 
ATOM   46971 O  O   . GLY   AA 13 147 ? 60.567  -168.301 40.390  1.00 83.96  ? 134 GLY   a O   1 
ATOM   46972 N  N   . VAL   AA 13 148 ? 59.875  -166.330 41.314  1.00 85.73  ? 135 VAL   a N   1 
ATOM   46973 C  CA  . VAL   AA 13 148 ? 61.165  -165.592 41.188  1.00 86.55  ? 135 VAL   a CA  1 
ATOM   46974 C  C   . VAL   AA 13 148 ? 62.083  -166.064 42.315  1.00 87.50  ? 135 VAL   a C   1 
ATOM   46975 O  O   . VAL   AA 13 148 ? 61.664  -165.979 43.484  1.00 89.71  ? 135 VAL   a O   1 
ATOM   46976 C  CB  . VAL   AA 13 148 ? 60.961  -164.067 41.253  1.00 86.22  ? 135 VAL   a CB  1 
ATOM   46977 C  CG1 . VAL   AA 13 148 ? 62.286  -163.321 41.277  1.00 86.38  ? 135 VAL   a CG1 1 
ATOM   46978 C  CG2 . VAL   AA 13 148 ? 60.080  -163.570 40.120  1.00 86.66  ? 135 VAL   a CG2 1 
ATOM   46979 N  N   . THR   AA 13 149 ? 63.284  -166.529 41.972  1.00 87.63  ? 136 THR   a N   1 
ATOM   46980 C  CA  . THR   AA 13 149 ? 64.320  -166.969 42.941  1.00 89.00  ? 136 THR   a CA  1 
ATOM   46981 C  C   . THR   AA 13 149 ? 65.538  -166.053 42.809  1.00 86.66  ? 136 THR   a C   1 
ATOM   46982 O  O   . THR   AA 13 149 ? 65.858  -165.658 41.672  1.00 88.31  ? 136 THR   a O   1 
ATOM   46983 C  CB  . THR   AA 13 149 ? 64.693  -168.445 42.737  1.00 88.92  ? 136 THR   a CB  1 
ATOM   46984 O  OG1 . THR   AA 13 149 ? 65.396  -168.573 41.501  1.00 92.20  ? 136 THR   a OG1 1 
ATOM   46985 C  CG2 . THR   AA 13 149 ? 63.490  -169.364 42.738  1.00 89.36  ? 136 THR   a CG2 1 
ATOM   46986 N  N   . TYR   AA 13 150 ? 66.170  -165.714 43.932  1.00 84.40  ? 137 TYR   a N   1 
ATOM   46987 C  CA  . TYR   AA 13 150 ? 67.489  -165.035 43.973  1.00 88.51  ? 137 TYR   a CA  1 
ATOM   46988 C  C   . TYR   AA 13 150 ? 68.177  -165.343 45.305  1.00 87.74  ? 137 TYR   a C   1 
ATOM   46989 O  O   . TYR   AA 13 150 ? 67.494  -165.765 46.262  1.00 87.35  ? 137 TYR   a O   1 
ATOM   46990 C  CB  . TYR   AA 13 150 ? 67.354  -163.529 43.714  1.00 89.15  ? 137 TYR   a CB  1 
ATOM   46991 C  CG  . TYR   AA 13 150 ? 66.249  -162.810 44.451  1.00 90.01  ? 137 TYR   a CG  1 
ATOM   46992 C  CD1 . TYR   AA 13 150 ? 66.376  -162.459 45.787  1.00 89.30  ? 137 TYR   a CD1 1 
ATOM   46993 C  CD2 . TYR   AA 13 150 ? 65.086  -162.432 43.795  1.00 89.70  ? 137 TYR   a CD2 1 
ATOM   46994 C  CE1 . TYR   AA 13 150 ? 65.366  -161.783 46.457  1.00 88.82  ? 137 TYR   a CE1 1 
ATOM   46995 C  CE2 . TYR   AA 13 150 ? 64.068  -161.755 44.449  1.00 87.31  ? 137 TYR   a CE2 1 
ATOM   46996 C  CZ  . TYR   AA 13 150 ? 64.209  -161.426 45.785  1.00 87.03  ? 137 TYR   a CZ  1 
ATOM   46997 O  OH  . TYR   AA 13 150 ? 63.204  -160.759 46.426  1.00 87.07  ? 137 TYR   a OH  1 
ATOM   46998 N  N   . SER   AA 13 151 ? 69.498  -165.152 45.341  1.00 90.09  ? 138 SER   a N   1 
ATOM   46999 C  CA  . SER   AA 13 151 ? 70.364  -165.374 46.527  1.00 93.33  ? 138 SER   a CA  1 
ATOM   47000 C  C   . SER   AA 13 151 ? 71.274  -164.160 46.737  1.00 92.92  ? 138 SER   a C   1 
ATOM   47001 O  O   . SER   AA 13 151 ? 71.701  -163.560 45.733  1.00 96.37  ? 138 SER   a O   1 
ATOM   47002 C  CB  . SER   AA 13 151 ? 71.156  -166.637 46.370  1.00 96.19  ? 138 SER   a CB  1 
ATOM   47003 O  OG  . SER   AA 13 151 ? 71.583  -167.127 47.630  1.00 104.05 ? 138 SER   a OG  1 
ATOM   47004 N  N   . SER   AA 13 152 ? 71.550  -163.824 48.000  1.00 93.18  ? 139 SER   a N   1 
ATOM   47005 C  CA  . SER   AA 13 152 ? 72.372  -162.661 48.424  1.00 94.30  ? 139 SER   a CA  1 
ATOM   47006 C  C   . SER   AA 13 152 ? 72.871  -162.896 49.847  1.00 90.79  ? 139 SER   a C   1 
ATOM   47007 O  O   . SER   AA 13 152 ? 72.218  -163.601 50.613  1.00 94.60  ? 139 SER   a O   1 
ATOM   47008 C  CB  . SER   AA 13 152 ? 71.567  -161.391 48.317  1.00 95.56  ? 139 SER   a CB  1 
ATOM   47009 O  OG  . SER   AA 13 152 ? 72.355  -160.246 48.606  1.00 101.79 ? 139 SER   a OG  1 
ATOM   47010 N  N   . PRO   AA 13 153 ? 74.041  -162.342 50.245  1.00 87.50  ? 140 PRO   a N   1 
ATOM   47011 C  CA  . PRO   AA 13 153 ? 74.503  -162.433 51.632  1.00 87.58  ? 140 PRO   a CA  1 
ATOM   47012 C  C   . PRO   AA 13 153 ? 73.435  -162.044 52.667  1.00 84.42  ? 140 PRO   a C   1 
ATOM   47013 O  O   . PRO   AA 13 153 ? 73.436  -162.617 53.738  1.00 81.77  ? 140 PRO   a O   1 
ATOM   47014 C  CB  . PRO   AA 13 153 ? 75.686  -161.457 51.669  1.00 88.66  ? 140 PRO   a CB  1 
ATOM   47015 C  CG  . PRO   AA 13 153 ? 76.233  -161.506 50.260  1.00 90.50  ? 140 PRO   a CG  1 
ATOM   47016 C  CD  . PRO   AA 13 153 ? 75.009  -161.650 49.379  1.00 89.55  ? 140 PRO   a CD  1 
ATOM   47017 N  N   . THR   AA 13 154 ? 72.567  -161.087 52.323  1.00 83.74  ? 141 THR   a N   1 
ATOM   47018 C  CA  . THR   AA 13 154 ? 71.373  -160.678 53.114  1.00 84.86  ? 141 THR   a CA  1 
ATOM   47019 C  C   . THR   AA 13 154 ? 70.124  -160.822 52.240  1.00 86.37  ? 141 THR   a C   1 
ATOM   47020 O  O   . THR   AA 13 154 ? 70.172  -160.407 51.066  1.00 88.45  ? 141 THR   a O   1 
ATOM   47021 C  CB  . THR   AA 13 154 ? 71.487  -159.234 53.623  1.00 85.29  ? 141 THR   a CB  1 
ATOM   47022 O  OG1 . THR   AA 13 154 ? 71.231  -158.349 52.532  1.00 81.44  ? 141 THR   a OG1 1 
ATOM   47023 C  CG2 . THR   AA 13 154 ? 72.838  -158.914 54.223  1.00 85.89  ? 141 THR   a CG2 1 
ATOM   47024 N  N   . LEU   AA 13 155 ? 69.047  -161.376 52.796  1.00 85.68  ? 142 LEU   a N   1 
ATOM   47025 C  CA  . LEU   AA 13 155 ? 67.728  -161.475 52.119  1.00 87.94  ? 142 LEU   a CA  1 
ATOM   47026 C  C   . LEU   AA 13 155 ? 66.632  -161.063 53.101  1.00 85.25  ? 142 LEU   a C   1 
ATOM   47027 O  O   . LEU   AA 13 155 ? 66.757  -161.378 54.302  1.00 83.98  ? 142 LEU   a O   1 
ATOM   47028 C  CB  . LEU   AA 13 155 ? 67.513  -162.907 51.620  1.00 90.58  ? 142 LEU   a CB  1 
ATOM   47029 C  CG  . LEU   AA 13 155 ? 68.320  -163.312 50.387  1.00 94.89  ? 142 LEU   a CG  1 
ATOM   47030 C  CD1 . LEU   AA 13 155 ? 68.158  -164.797 50.110  1.00 97.86  ? 142 LEU   a CD1 1 
ATOM   47031 C  CD2 . LEU   AA 13 155 ? 67.910  -162.506 49.164  1.00 95.41  ? 142 LEU   a CD2 1 
ATOM   47032 N  N   . ALA   AA 13 156 ? 65.605  -160.381 52.593  1.00 84.93  ? 143 ALA   a N   1 
ATOM   47033 C  CA  . ALA   AA 13 156 ? 64.436  -159.914 53.371  1.00 86.66  ? 143 ALA   a CA  1 
ATOM   47034 C  C   . ALA   AA 13 156 ? 63.220  -159.778 52.447  1.00 84.32  ? 143 ALA   a C   1 
ATOM   47035 O  O   . ALA   AA 13 156 ? 63.417  -159.606 51.225  1.00 82.69  ? 143 ALA   a O   1 
ATOM   47036 C  CB  . ALA   AA 13 156 ? 64.769  -158.613 54.056  1.00 86.40  ? 143 ALA   a CB  1 
ATOM   47037 N  N   . THR   AA 13 157 ? 62.014  -159.861 53.019  1.00 86.95  ? 144 THR   a N   1 
ATOM   47038 C  CA  . THR   AA 13 157 ? 60.714  -159.787 52.298  1.00 88.49  ? 144 THR   a CA  1 
ATOM   47039 C  C   . THR   AA 13 157 ? 59.923  -158.572 52.794  1.00 90.50  ? 144 THR   a C   1 
ATOM   47040 O  O   . THR   AA 13 157 ? 60.095  -158.195 53.971  1.00 95.34  ? 144 THR   a O   1 
ATOM   47041 C  CB  . THR   AA 13 157 ? 59.902  -161.077 52.476  1.00 87.46  ? 144 THR   a CB  1 
ATOM   47042 O  OG1 . THR   AA 13 157 ? 59.286  -161.068 53.766  1.00 83.32  ? 144 THR   a OG1 1 
ATOM   47043 C  CG2 . THR   AA 13 157 ? 60.742  -162.326 52.323  1.00 85.78  ? 144 THR   a CG2 1 
ATOM   47044 N  N   . GLY   AA 13 158 ? 59.092  -157.991 51.924  1.00 93.18  ? 145 GLY   a N   1 
ATOM   47045 C  CA  . GLY   AA 13 158 ? 58.179  -156.879 52.256  1.00 94.15  ? 145 GLY   a CA  1 
ATOM   47046 C  C   . GLY   AA 13 158 ? 58.938  -155.633 52.678  1.00 95.00  ? 145 GLY   a C   1 
ATOM   47047 O  O   . GLY   AA 13 158 ? 59.852  -155.223 51.934  1.00 97.19  ? 145 GLY   a O   1 
ATOM   47048 N  N   . PHE   AA 13 159 ? 58.577  -155.052 53.828  1.00 93.20  ? 146 PHE   a N   1 
ATOM   47049 C  CA  . PHE   AA 13 159 ? 59.213  -153.830 54.392  1.00 93.37  ? 146 PHE   a CA  1 
ATOM   47050 C  C   . PHE   AA 13 159 ? 60.671  -154.121 54.753  1.00 91.59  ? 146 PHE   a C   1 
ATOM   47051 O  O   . PHE   AA 13 159 ? 61.494  -153.191 54.675  1.00 100.27 ? 146 PHE   a O   1 
ATOM   47052 C  CB  . PHE   AA 13 159 ? 58.436  -153.296 55.599  1.00 94.73  ? 146 PHE   a CB  1 
ATOM   47053 C  CG  . PHE   AA 13 159 ? 57.327  -152.347 55.231  1.00 95.05  ? 146 PHE   a CG  1 
ATOM   47054 C  CD1 . PHE   AA 13 159 ? 57.611  -151.050 54.832  1.00 96.42  ? 146 PHE   a CD1 1 
ATOM   47055 C  CD2 . PHE   AA 13 159 ? 56.002  -152.755 55.258  1.00 97.37  ? 146 PHE   a CD2 1 
ATOM   47056 C  CE1 . PHE   AA 13 159 ? 56.591  -150.179 54.479  1.00 96.01  ? 146 PHE   a CE1 1 
ATOM   47057 C  CE2 . PHE   AA 13 159 ? 54.985  -151.881 54.906  1.00 95.77  ? 146 PHE   a CE2 1 
ATOM   47058 C  CZ  . PHE   AA 13 159 ? 55.280  -150.595 54.518  1.00 96.35  ? 146 PHE   a CZ  1 
ATOM   47059 N  N   . GLY   AA 13 160 ? 60.975  -155.366 55.128  1.00 89.59  ? 147 GLY   a N   1 
ATOM   47060 C  CA  . GLY   AA 13 160 ? 62.348  -155.831 55.403  1.00 90.57  ? 147 GLY   a CA  1 
ATOM   47061 C  C   . GLY   AA 13 160 ? 63.275  -155.552 54.233  1.00 88.20  ? 147 GLY   a C   1 
ATOM   47062 O  O   . GLY   AA 13 160 ? 64.423  -155.131 54.472  1.00 87.33  ? 147 GLY   a O   1 
ATOM   47063 N  N   . ALA   AA 13 161 ? 62.787  -155.755 53.006  1.00 89.37  ? 148 ALA   a N   1 
ATOM   47064 C  CA  . ALA   AA 13 161 ? 63.547  -155.559 51.749  1.00 90.96  ? 148 ALA   a CA  1 
ATOM   47065 C  C   . ALA   AA 13 161 ? 63.985  -154.098 51.622  1.00 92.34  ? 148 ALA   a C   1 
ATOM   47066 O  O   . ALA   AA 13 161 ? 65.041  -153.864 51.009  1.00 95.24  ? 148 ALA   a O   1 
ATOM   47067 C  CB  . ALA   AA 13 161 ? 62.716  -155.984 50.564  1.00 93.74  ? 148 ALA   a CB  1 
ATOM   47068 N  N   . HIS   AA 13 162 ? 63.204  -153.166 52.183  1.00 92.57  ? 149 HIS   a N   1 
ATOM   47069 C  CA  . HIS   AA 13 162 ? 63.403  -151.694 52.071  1.00 93.94  ? 149 HIS   a CA  1 
ATOM   47070 C  C   . HIS   AA 13 162 ? 64.199  -151.145 53.264  1.00 92.52  ? 149 HIS   a C   1 
ATOM   47071 O  O   . HIS   AA 13 162 ? 64.971  -150.198 53.040  1.00 99.07  ? 149 HIS   a O   1 
ATOM   47072 C  CB  . HIS   AA 13 162 ? 62.054  -150.974 51.928  1.00 93.83  ? 149 HIS   a CB  1 
ATOM   47073 C  CG  . HIS   AA 13 162 ? 61.296  -151.349 50.698  1.00 95.06  ? 149 HIS   a CG  1 
ATOM   47074 N  ND1 . HIS   AA 13 162 ? 60.114  -152.069 50.744  1.00 94.34  ? 149 HIS   a ND1 1 
ATOM   47075 C  CD2 . HIS   AA 13 162 ? 61.544  -151.113 49.391  1.00 96.43  ? 149 HIS   a CD2 1 
ATOM   47076 C  CE1 . HIS   AA 13 162 ? 59.668  -152.257 49.518  1.00 93.88  ? 149 HIS   a CE1 1 
ATOM   47077 N  NE2 . HIS   AA 13 162 ? 60.528  -151.682 48.670  1.00 94.02  ? 149 HIS   a NE2 1 
ATOM   47078 N  N   . MET   AA 13 163 ? 64.018  -151.697 54.471  1.00 89.64  ? 150 MET   a N   1 
ATOM   47079 C  CA  . MET   AA 13 163 ? 64.545  -151.115 55.739  1.00 88.45  ? 150 MET   a CA  1 
ATOM   47080 C  C   . MET   AA 13 163 ? 65.628  -152.006 56.360  1.00 89.40  ? 150 MET   a C   1 
ATOM   47081 O  O   . MET   AA 13 163 ? 66.642  -151.441 56.822  1.00 89.94  ? 150 MET   a O   1 
ATOM   47082 C  CB  . MET   AA 13 163 ? 63.415  -150.904 56.750  1.00 89.34  ? 150 MET   a CB  1 
ATOM   47083 C  CG  . MET   AA 13 163 ? 62.347  -149.956 56.252  1.00 91.44  ? 150 MET   a CG  1 
ATOM   47084 S  SD  . MET   AA 13 163 ? 61.483  -149.122 57.600  1.00 96.14  ? 150 MET   a SD  1 
ATOM   47085 C  CE  . MET   AA 13 163 ? 62.695  -147.877 58.038  1.00 95.83  ? 150 MET   a CE  1 
ATOM   47086 N  N   . ALA   AA 13 164 ? 65.430  -153.330 56.386  1.00 86.66  ? 151 ALA   a N   1 
ATOM   47087 C  CA  . ALA   AA 13 164 ? 66.375  -154.300 56.990  1.00 84.46  ? 151 ALA   a CA  1 
ATOM   47088 C  C   . ALA   AA 13 164 ? 67.615  -154.448 56.100  1.00 84.63  ? 151 ALA   a C   1 
ATOM   47089 O  O   . ALA   AA 13 164 ? 68.733  -154.337 56.635  1.00 84.70  ? 151 ALA   a O   1 
ATOM   47090 C  CB  . ALA   AA 13 164 ? 65.696  -155.626 57.225  1.00 84.22  ? 151 ALA   a CB  1 
ATOM   47091 N  N   . ASN   AA 13 165 ? 67.425  -154.675 54.796  1.00 84.02  ? 152 ASN   a N   1 
ATOM   47092 C  CA  . ASN   AA 13 165 ? 68.523  -154.955 53.829  1.00 86.63  ? 152 ASN   a CA  1 
ATOM   47093 C  C   . ASN   AA 13 165 ? 69.588  -153.862 53.908  1.00 87.72  ? 152 ASN   a C   1 
ATOM   47094 O  O   . ASN   AA 13 165 ? 70.767  -154.181 54.046  1.00 86.39  ? 152 ASN   a O   1 
ATOM   47095 C  CB  . ASN   AA 13 165 ? 68.007  -155.158 52.400  1.00 89.41  ? 152 ASN   a CB  1 
ATOM   47096 C  CG  . ASN   AA 13 165 ? 67.718  -156.608 52.073  1.00 90.03  ? 152 ASN   a CG  1 
ATOM   47097 O  OD1 . ASN   AA 13 165 ? 68.279  -157.516 52.686  1.00 91.05  ? 152 ASN   a OD1 1 
ATOM   47098 N  ND2 . ASN   AA 13 165 ? 66.850  -156.839 51.101  1.00 93.91  ? 152 ASN   a ND2 1 
ATOM   47099 N  N   . PRO   AA 13 166 ? 69.235  -152.555 53.810  1.00 88.18  ? 153 PRO   a N   1 
ATOM   47100 C  CA  . PRO   AA 13 166 ? 70.225  -151.483 53.937  1.00 88.61  ? 153 PRO   a CA  1 
ATOM   47101 C  C   . PRO   AA 13 166 ? 71.093  -151.573 55.202  1.00 88.72  ? 153 PRO   a C   1 
ATOM   47102 O  O   . PRO   AA 13 166 ? 72.278  -151.316 55.098  1.00 91.63  ? 153 PRO   a O   1 
ATOM   47103 C  CB  . PRO   AA 13 166 ? 69.360  -150.215 53.975  1.00 88.40  ? 153 PRO   a CB  1 
ATOM   47104 C  CG  . PRO   AA 13 166 ? 68.154  -150.584 53.151  1.00 87.34  ? 153 PRO   a CG  1 
ATOM   47105 C  CD  . PRO   AA 13 166 ? 67.890  -152.031 53.512  1.00 87.32  ? 153 PRO   a CD  1 
ATOM   47106 N  N   . LEU   AA 13 167 ? 70.492  -151.932 56.343  1.00 88.98  ? 154 LEU   a N   1 
ATOM   47107 C  CA  . LEU   AA 13 167 ? 71.186  -152.063 57.656  1.00 89.72  ? 154 LEU   a CA  1 
ATOM   47108 C  C   . LEU   AA 13 167 ? 72.088  -153.303 57.651  1.00 90.24  ? 154 LEU   a C   1 
ATOM   47109 O  O   . LEU   AA 13 167 ? 73.248  -153.180 58.082  1.00 91.47  ? 154 LEU   a O   1 
ATOM   47110 C  CB  . LEU   AA 13 167 ? 70.156  -152.156 58.788  1.00 88.95  ? 154 LEU   a CB  1 
ATOM   47111 C  CG  . LEU   AA 13 167 ? 69.319  -150.904 59.043  1.00 87.28  ? 154 LEU   a CG  1 
ATOM   47112 C  CD1 . LEU   AA 13 167 ? 68.245  -151.187 60.081  1.00 87.34  ? 154 LEU   a CD1 1 
ATOM   47113 C  CD2 . LEU   AA 13 167 ? 70.190  -149.738 59.488  1.00 87.34  ? 154 LEU   a CD2 1 
ATOM   47114 N  N   . LEU   AA 13 168 ? 71.566  -154.450 57.202  1.00 89.43  ? 155 LEU   a N   1 
ATOM   47115 C  CA  . LEU   AA 13 168 ? 72.291  -155.753 57.196  1.00 89.18  ? 155 LEU   a CA  1 
ATOM   47116 C  C   . LEU   AA 13 168 ? 73.446  -155.700 56.187  1.00 90.77  ? 155 LEU   a C   1 
ATOM   47117 O  O   . LEU   AA 13 168 ? 74.459  -156.388 56.425  1.00 90.37  ? 155 LEU   a O   1 
ATOM   47118 C  CB  . LEU   AA 13 168 ? 71.323  -156.890 56.849  1.00 87.22  ? 155 LEU   a CB  1 
ATOM   47119 C  CG  . LEU   AA 13 168 ? 70.134  -157.094 57.790  1.00 85.82  ? 155 LEU   a CG  1 
ATOM   47120 C  CD1 . LEU   AA 13 168 ? 69.308  -158.292 57.346  1.00 84.66  ? 155 LEU   a CD1 1 
ATOM   47121 C  CD2 . LEU   AA 13 168 ? 70.580  -157.267 59.234  1.00 85.66  ? 155 LEU   a CD2 1 
ATOM   47122 N  N   . ARG   AA 13 169 ? 73.295  -154.926 55.105  1.00 92.50  ? 156 ARG   a N   1 
ATOM   47123 C  CA  . ARG   AA 13 169 ? 74.315  -154.777 54.028  1.00 94.55  ? 156 ARG   a CA  1 
ATOM   47124 C  C   . ARG   AA 13 169 ? 75.501  -153.938 54.525  1.00 94.71  ? 156 ARG   a C   1 
ATOM   47125 O  O   . ARG   AA 13 169 ? 76.576  -154.049 53.911  1.00 94.61  ? 156 ARG   a O   1 
ATOM   47126 C  CB  . ARG   AA 13 169 ? 73.706  -154.169 52.759  1.00 93.52  ? 156 ARG   a CB  1 
ATOM   47127 C  CG  . ARG   AA 13 169 ? 72.986  -155.182 51.880  1.00 94.48  ? 156 ARG   a CG  1 
ATOM   47128 C  CD  . ARG   AA 13 169 ? 72.040  -154.553 50.873  1.00 93.56  ? 156 ARG   a CD  1 
ATOM   47129 N  NE  . ARG   AA 13 169 ? 71.244  -155.560 50.180  1.00 96.08  ? 156 ARG   a NE  1 
ATOM   47130 C  CZ  . ARG   AA 13 169 ? 70.282  -155.308 49.294  1.00 95.18  ? 156 ARG   a CZ  1 
ATOM   47131 N  NH1 . ARG   AA 13 169 ? 69.970  -154.066 48.972  1.00 93.18  ? 156 ARG   a NH1 1 
ATOM   47132 N  NH2 . ARG   AA 13 169 ? 69.630  -156.309 48.727  1.00 97.29  ? 156 ARG   a NH2 1 
ATOM   47133 N  N   . LYS   AA 13 170 ? 75.323  -153.134 55.579  1.00 95.51  ? 157 LYS   a N   1 
ATOM   47134 C  CA  . LYS   AA 13 170 ? 76.425  -152.354 56.212  1.00 101.25 ? 157 LYS   a CA  1 
ATOM   47135 C  C   . LYS   AA 13 170 ? 77.390  -153.309 56.934  1.00 103.31 ? 157 LYS   a C   1 
ATOM   47136 O  O   . LYS   AA 13 170 ? 78.571  -152.933 57.097  1.00 107.36 ? 157 LYS   a O   1 
ATOM   47137 C  CB  . LYS   AA 13 170 ? 75.874  -151.292 57.172  1.00 103.32 ? 157 LYS   a CB  1 
ATOM   47138 C  CG  . LYS   AA 13 170 ? 75.240  -150.080 56.501  1.00 104.99 ? 157 LYS   a CG  1 
ATOM   47139 C  CD  . LYS   AA 13 170 ? 74.480  -149.177 57.456  1.00 105.50 ? 157 LYS   a CD  1 
ATOM   47140 C  CE  . LYS   AA 13 170 ? 75.370  -148.218 58.218  1.00 109.02 ? 157 LYS   a CE  1 
ATOM   47141 N  NZ  . LYS   AA 13 170 ? 75.775  -147.062 57.383  1.00 110.87 ? 157 LYS   a NZ  1 
ATOM   47142 N  N   . VAL   AA 13 171 ? 76.909  -154.491 57.345  1.00 104.54 ? 158 VAL   a N   1 
ATOM   47143 C  CA  . VAL   AA 13 171 ? 77.710  -155.547 58.038  1.00 103.37 ? 158 VAL   a CA  1 
ATOM   47144 C  C   . VAL   AA 13 171 ? 78.327  -156.479 56.986  1.00 104.89 ? 158 VAL   a C   1 
ATOM   47145 O  O   . VAL   AA 13 171 ? 79.560  -156.670 57.021  1.00 105.25 ? 158 VAL   a O   1 
ATOM   47146 C  CB  . VAL   AA 13 171 ? 76.854  -156.328 59.055  1.00 102.47 ? 158 VAL   a CB  1 
ATOM   47147 C  CG1 . VAL   AA 13 171 ? 77.659  -157.417 59.752  1.00 102.14 ? 158 VAL   a CG1 1 
ATOM   47148 C  CG2 . VAL   AA 13 171 ? 76.215  -155.403 60.080  1.00 101.50 ? 158 VAL   a CG2 1 
ATOM   47149 N  N   . VAL   AA 13 172 ? 77.499  -157.042 56.099  1.00 103.27 ? 159 VAL   a N   1 
ATOM   47150 C  CA  . VAL   AA 13 172 ? 77.938  -157.946 54.991  1.00 106.12 ? 159 VAL   a CA  1 
ATOM   47151 C  C   . VAL   AA 13 172 ? 77.501  -157.333 53.655  1.00 102.74 ? 159 VAL   a C   1 
ATOM   47152 O  O   . VAL   AA 13 172 ? 76.358  -157.579 53.218  1.00 95.50  ? 159 VAL   a O   1 
ATOM   47153 C  CB  . VAL   AA 13 172 ? 77.422  -159.390 55.169  1.00 108.46 ? 159 VAL   a CB  1 
ATOM   47154 C  CG1 . VAL   AA 13 172 ? 78.293  -160.176 56.138  1.00 110.84 ? 159 VAL   a CG1 1 
ATOM   47155 C  CG2 . VAL   AA 13 172 ? 75.963  -159.448 55.599  1.00 109.50 ? 159 VAL   a CG2 1 
ATOM   47156 N  N   . ASP   AA 13 173 ? 78.395  -156.558 53.036  1.00 104.71 ? 160 ASP   a N   1 
ATOM   47157 C  CA  . ASP   AA 13 173 ? 78.135  -155.802 51.783  1.00 109.16 ? 160 ASP   a CA  1 
ATOM   47158 C  C   . ASP   AA 13 173 ? 78.483  -156.675 50.571  1.00 110.51 ? 160 ASP   a C   1 
ATOM   47159 O  O   . ASP   AA 13 173 ? 77.916  -156.420 49.491  1.00 108.45 ? 160 ASP   a O   1 
ATOM   47160 C  CB  . ASP   AA 13 173 ? 78.905  -154.477 51.772  1.00 112.85 ? 160 ASP   a CB  1 
ATOM   47161 C  CG  . ASP   AA 13 173 ? 78.268  -153.390 50.919  1.00 114.60 ? 160 ASP   a CG  1 
ATOM   47162 O  OD1 . ASP   AA 13 173 ? 77.022  -153.367 50.823  1.00 119.12 ? 160 ASP   a OD1 1 
ATOM   47163 O  OD2 . ASP   AA 13 173 ? 79.025  -152.573 50.355  1.00 115.22 ? 160 ASP   a OD2 1 
ATOM   47164 N  N   . ARG   AA 13 174 ? 79.379  -157.656 50.735  1.00 113.85 ? 161 ARG   a N   1 
ATOM   47165 C  CA  . ARG   AA 13 174 ? 79.738  -158.626 49.662  1.00 117.09 ? 161 ARG   a CA  1 
ATOM   47166 C  C   . ARG   AA 13 174 ? 80.213  -159.948 50.279  1.00 120.70 ? 161 ARG   a C   1 
ATOM   47167 O  O   . ARG   AA 13 174 ? 80.237  -160.049 51.523  1.00 125.97 ? 161 ARG   a O   1 
ATOM   47168 C  CB  . ARG   AA 13 174 ? 80.779  -158.026 48.708  1.00 121.72 ? 161 ARG   a CB  1 
ATOM   47169 C  CG  . ARG   AA 13 174 ? 82.185  -157.878 49.276  1.00 123.95 ? 161 ARG   a CG  1 
ATOM   47170 C  CD  . ARG   AA 13 174 ? 82.534  -156.479 49.761  1.00 122.81 ? 161 ARG   a CD  1 
ATOM   47171 N  NE  . ARG   AA 13 174 ? 82.083  -155.393 48.894  1.00 121.79 ? 161 ARG   a NE  1 
ATOM   47172 C  CZ  . ARG   AA 13 174 ? 82.550  -155.125 47.673  1.00 119.46 ? 161 ARG   a CZ  1 
ATOM   47173 N  NH1 . ARG   AA 13 174 ? 83.491  -155.875 47.122  1.00 121.58 ? 161 ARG   a NH1 1 
ATOM   47174 N  NH2 . ARG   AA 13 174 ? 82.059  -154.101 46.996  1.00 116.39 ? 161 ARG   a NH2 1 
ATOM   47175 N  N   . GLU   AA 13 175 ? 80.567  -160.918 49.426  1.00 123.50 ? 162 GLU   a N   1 
ATOM   47176 C  CA  . GLU   AA 13 175 ? 80.927  -162.310 49.812  1.00 123.89 ? 162 GLU   a CA  1 
ATOM   47177 C  C   . GLU   AA 13 175 ? 82.065  -162.277 50.839  1.00 118.09 ? 162 GLU   a C   1 
ATOM   47178 O  O   . GLU   AA 13 175 ? 81.932  -162.942 51.882  1.00 119.17 ? 162 GLU   a O   1 
ATOM   47179 C  CB  . GLU   AA 13 175 ? 81.328  -163.127 48.580  1.00 129.21 ? 162 GLU   a CB  1 
ATOM   47180 C  CG  . GLU   AA 13 175 ? 81.157  -164.629 48.756  1.00 135.25 ? 162 GLU   a CG  1 
ATOM   47181 C  CD  . GLU   AA 13 175 ? 79.726  -165.142 48.683  1.00 140.83 ? 162 GLU   a CD  1 
ATOM   47182 O  OE1 . GLU   AA 13 175 ? 79.525  -166.356 48.903  1.00 145.23 ? 162 GLU   a OE1 1 
ATOM   47183 O  OE2 . GLU   AA 13 175 ? 78.815  -164.333 48.403  1.00 140.53 ? 162 GLU   a OE2 1 
ATOM   47184 N  N   . SER   AA 13 176 ? 83.122  -161.507 50.560  1.00 115.33 ? 163 SER   a N   1 
ATOM   47185 C  CA  . SER   AA 13 176 ? 84.376  -161.447 51.360  1.00 119.08 ? 163 SER   a CA  1 
ATOM   47186 C  C   . SER   AA 13 176 ? 84.104  -160.974 52.794  1.00 117.11 ? 163 SER   a C   1 
ATOM   47187 O  O   . SER   AA 13 176 ? 84.971  -161.221 53.654  1.00 121.86 ? 163 SER   a O   1 
ATOM   47188 C  CB  . SER   AA 13 176 ? 85.408  -160.574 50.692  1.00 121.35 ? 163 SER   a CB  1 
ATOM   47189 O  OG  . SER   AA 13 176 ? 84.870  -159.295 50.388  1.00 121.97 ? 163 SER   a OG  1 
ATOM   47190 N  N   . ASP   AA 13 177 ? 82.966  -160.315 53.044  1.00 115.32 ? 164 ASP   a N   1 
ATOM   47191 C  CA  . ASP   AA 13 177 ? 82.579  -159.807 54.390  1.00 114.70 ? 164 ASP   a CA  1 
ATOM   47192 C  C   . ASP   AA 13 177 ? 82.077  -160.957 55.278  1.00 110.65 ? 164 ASP   a C   1 
ATOM   47193 O  O   . ASP   AA 13 177 ? 82.104  -160.789 56.513  1.00 110.00 ? 164 ASP   a O   1 
ATOM   47194 C  CB  . ASP   AA 13 177 ? 81.525  -158.697 54.295  1.00 115.50 ? 164 ASP   a CB  1 
ATOM   47195 C  CG  . ASP   AA 13 177 ? 82.029  -157.394 53.693  1.00 117.59 ? 164 ASP   a CG  1 
ATOM   47196 O  OD1 . ASP   AA 13 177 ? 83.255  -157.267 53.495  1.00 121.57 ? 164 ASP   a OD1 1 
ATOM   47197 O  OD2 . ASP   AA 13 177 ? 81.188  -156.510 53.433  1.00 118.77 ? 164 ASP   a OD2 1 
ATOM   47198 N  N   . ILE   AA 13 178 ? 81.642  -162.078 54.691  1.00 106.93 ? 165 ILE   a N   1 
ATOM   47199 C  CA  . ILE   AA 13 178 ? 80.961  -163.189 55.426  1.00 104.22 ? 165 ILE   a CA  1 
ATOM   47200 C  C   . ILE   AA 13 178 ? 81.928  -163.848 56.413  1.00 106.78 ? 165 ILE   a C   1 
ATOM   47201 O  O   . ILE   AA 13 178 ? 81.573  -164.025 57.577  1.00 106.23 ? 165 ILE   a O   1 
ATOM   47202 C  CB  . ILE   AA 13 178 ? 80.313  -164.198 54.455  1.00 101.99 ? 165 ILE   a CB  1 
ATOM   47203 C  CG1 . ILE   AA 13 178 ? 79.106  -163.579 53.745  1.00 98.92  ? 165 ILE   a CG1 1 
ATOM   47204 C  CG2 . ILE   AA 13 178 ? 79.941  -165.484 55.180  1.00 103.15 ? 165 ILE   a CG2 1 
ATOM   47205 C  CD1 . ILE   AA 13 178 ? 78.567  -164.396 52.594  1.00 97.64  ? 165 ILE   a CD1 1 
ATOM   47206 N  N   . PRO   AA 13 179 ? 83.159  -164.250 56.009  1.00 107.59 ? 166 PRO   a N   1 
ATOM   47207 C  CA  . PRO   AA 13 179 ? 84.134  -164.796 56.958  1.00 109.22 ? 166 PRO   a CA  1 
ATOM   47208 C  C   . PRO   AA 13 179 ? 84.506  -163.847 58.109  1.00 109.76 ? 166 PRO   a C   1 
ATOM   47209 O  O   . PRO   AA 13 179 ? 84.905  -164.335 59.153  1.00 108.97 ? 166 PRO   a O   1 
ATOM   47210 C  CB  . PRO   AA 13 179 ? 85.386  -165.049 56.104  1.00 112.48 ? 166 PRO   a CB  1 
ATOM   47211 C  CG  . PRO   AA 13 179 ? 84.856  -165.192 54.696  1.00 111.35 ? 166 PRO   a CG  1 
ATOM   47212 C  CD  . PRO   AA 13 179 ? 83.673  -164.249 54.629  1.00 108.70 ? 166 PRO   a CD  1 
ATOM   47213 N  N   . LYS   AA 13 180 ? 84.373  -162.534 57.887  1.00 111.10 ? 167 LYS   a N   1 
ATOM   47214 C  CA  . LYS   AA 13 180 ? 84.766  -161.462 58.842  1.00 111.27 ? 167 LYS   a CA  1 
ATOM   47215 C  C   . LYS   AA 13 180 ? 83.630  -161.187 59.838  1.00 103.80 ? 167 LYS   a C   1 
ATOM   47216 O  O   . LYS   AA 13 180 ? 83.863  -160.416 60.787  1.00 100.84 ? 167 LYS   a O   1 
ATOM   47217 C  CB  . LYS   AA 13 180 ? 85.142  -160.187 58.078  1.00 114.48 ? 167 LYS   a CB  1 
ATOM   47218 C  CG  . LYS   AA 13 180 ? 86.199  -160.366 56.994  1.00 117.98 ? 167 LYS   a CG  1 
ATOM   47219 C  CD  . LYS   AA 13 180 ? 86.590  -159.084 56.291  1.00 117.60 ? 167 LYS   a CD  1 
ATOM   47220 C  CE  . LYS   AA 13 180 ? 87.543  -159.323 55.140  1.00 118.08 ? 167 LYS   a CE  1 
ATOM   47221 N  NZ  . LYS   AA 13 180 ? 87.952  -158.056 54.492  1.00 118.07 ? 167 LYS   a NZ  1 
ATOM   47222 N  N   . THR   AA 13 181 ? 82.453  -161.791 59.646  1.00 102.47 ? 168 THR   a N   1 
ATOM   47223 C  CA  . THR   AA 13 181 ? 81.244  -161.554 60.480  1.00 105.17 ? 168 THR   a CA  1 
ATOM   47224 C  C   . THR   AA 13 181 ? 81.041  -162.720 61.451  1.00 106.65 ? 168 THR   a C   1 
ATOM   47225 O  O   . THR   AA 13 181 ? 80.982  -163.871 60.979  1.00 110.40 ? 168 THR   a O   1 
ATOM   47226 C  CB  . THR   AA 13 181 ? 79.989  -161.379 59.619  1.00 105.57 ? 168 THR   a CB  1 
ATOM   47227 O  OG1 . THR   AA 13 181 ? 80.262  -160.389 58.627  1.00 107.70 ? 168 THR   a OG1 1 
ATOM   47228 C  CG2 . THR   AA 13 181 ? 78.779  -160.980 60.436  1.00 104.36 ? 168 THR   a CG2 1 
ATOM   47229 N  N   . THR   AA 13 182 ? 80.902  -162.418 62.746  1.00 106.74 ? 169 THR   a N   1 
ATOM   47230 C  CA  . THR   AA 13 182 ? 80.639  -163.406 63.826  1.00 105.57 ? 169 THR   a CA  1 
ATOM   47231 C  C   . THR   AA 13 182 ? 79.130  -163.488 64.082  1.00 105.04 ? 169 THR   a C   1 
ATOM   47232 O  O   . THR   AA 13 182 ? 78.406  -162.562 63.660  1.00 97.71  ? 169 THR   a O   1 
ATOM   47233 C  CB  . THR   AA 13 182 ? 81.408  -163.053 65.105  1.00 106.28 ? 169 THR   a CB  1 
ATOM   47234 O  OG1 . THR   AA 13 182 ? 80.910  -161.812 65.604  1.00 106.72 ? 169 THR   a OG1 1 
ATOM   47235 C  CG2 . THR   AA 13 182 ? 82.901  -162.954 64.884  1.00 106.98 ? 169 THR   a CG2 1 
ATOM   47236 N  N   . VAL   AA 13 183 ? 78.688  -164.560 64.748  1.00 105.53 ? 170 VAL   a N   1 
ATOM   47237 C  CA  . VAL   AA 13 183 ? 77.260  -164.823 65.102  1.00 104.09 ? 170 VAL   a CA  1 
ATOM   47238 C  C   . VAL   AA 13 183 ? 76.766  -163.735 66.067  1.00 105.17 ? 170 VAL   a C   1 
ATOM   47239 O  O   . VAL   AA 13 183 ? 75.567  -163.398 66.006  1.00 100.51 ? 170 VAL   a O   1 
ATOM   47240 C  CB  . VAL   AA 13 183 ? 77.071  -166.237 65.688  1.00 104.85 ? 170 VAL   a CB  1 
ATOM   47241 C  CG1 . VAL   AA 13 183 ? 77.697  -166.385 67.067  1.00 104.81 ? 170 VAL   a CG1 1 
ATOM   47242 C  CG2 . VAL   AA 13 183 ? 75.603  -166.640 65.719  1.00 104.43 ? 170 VAL   a CG2 1 
ATOM   47243 N  N   . GLN   AA 13 184 ? 77.651  -163.206 66.918  1.00 105.80 ? 171 GLN   a N   1 
ATOM   47244 C  CA  . GLN   AA 13 184 ? 77.326  -162.121 67.884  1.00 108.97 ? 171 GLN   a CA  1 
ATOM   47245 C  C   . GLN   AA 13 184 ? 76.985  -160.848 67.103  1.00 107.89 ? 171 GLN   a C   1 
ATOM   47246 O  O   . GLN   AA 13 184 ? 75.924  -160.258 67.381  1.00 107.88 ? 171 GLN   a O   1 
ATOM   47247 C  CB  . GLN   AA 13 184 ? 78.484  -161.865 68.853  1.00 114.46 ? 171 GLN   a CB  1 
ATOM   47248 C  CG  . GLN   AA 13 184 ? 78.635  -162.936 69.926  1.00 119.12 ? 171 GLN   a CG  1 
ATOM   47249 C  CD  . GLN   AA 13 184 ? 79.405  -164.150 69.464  1.00 120.46 ? 171 GLN   a CD  1 
ATOM   47250 O  OE1 . GLN   AA 13 184 ? 80.118  -164.119 68.463  1.00 124.10 ? 171 GLN   a OE1 1 
ATOM   47251 N  NE2 . GLN   AA 13 184 ? 79.269  -165.241 70.201  1.00 122.68 ? 171 GLN   a NE2 1 
ATOM   47252 N  N   . VAL   AA 13 185 ? 77.849  -160.466 66.154  1.00 106.11 ? 172 VAL   a N   1 
ATOM   47253 C  CA  . VAL   AA 13 185 ? 77.704  -159.250 65.296  1.00 102.91 ? 172 VAL   a CA  1 
ATOM   47254 C  C   . VAL   AA 13 185 ? 76.453  -159.403 64.419  1.00 102.01 ? 172 VAL   a C   1 
ATOM   47255 O  O   . VAL   AA 13 185 ? 75.669  -158.436 64.342  1.00 101.33 ? 172 VAL   a O   1 
ATOM   47256 C  CB  . VAL   AA 13 185 ? 78.969  -159.003 64.448  1.00 101.32 ? 172 VAL   a CB  1 
ATOM   47257 C  CG1 . VAL   AA 13 185 ? 78.745  -157.936 63.386  1.00 101.25 ? 172 VAL   a CG1 1 
ATOM   47258 C  CG2 . VAL   AA 13 185 ? 80.163  -158.639 65.316  1.00 100.43 ? 172 VAL   a CG2 1 
ATOM   47259 N  N   . ALA   AA 13 186 ? 76.279  -160.572 63.792  1.00 100.20 ? 173 ALA   a N   1 
ATOM   47260 C  CA  . ALA   AA 13 186 ? 75.173  -160.886 62.856  1.00 97.32  ? 173 ALA   a CA  1 
ATOM   47261 C  C   . ALA   AA 13 186 ? 73.823  -160.805 63.578  1.00 97.40  ? 173 ALA   a C   1 
ATOM   47262 O  O   . ALA   AA 13 186 ? 72.917  -160.135 63.048  1.00 99.11  ? 173 ALA   a O   1 
ATOM   47263 C  CB  . ALA   AA 13 186 ? 75.381  -162.250 62.253  1.00 97.64  ? 173 ALA   a CB  1 
ATOM   47264 N  N   . GLU   AA 13 187 ? 73.691  -161.476 64.727  1.00 97.85  ? 174 GLU   a N   1 
ATOM   47265 C  CA  . GLU   AA 13 187 ? 72.434  -161.531 65.524  1.00 100.55 ? 174 GLU   a CA  1 
ATOM   47266 C  C   . GLU   AA 13 187 ? 72.077  -160.130 66.026  1.00 101.29 ? 174 GLU   a C   1 
ATOM   47267 O  O   . GLU   AA 13 187 ? 70.874  -159.814 66.065  1.00 103.35 ? 174 GLU   a O   1 
ATOM   47268 C  CB  . GLU   AA 13 187 ? 72.573  -162.480 66.712  1.00 102.19 ? 174 GLU   a CB  1 
ATOM   47269 C  CG  . GLU   AA 13 187 ? 71.264  -162.717 67.442  1.00 103.28 ? 174 GLU   a CG  1 
ATOM   47270 C  CD  . GLU   AA 13 187 ? 71.373  -163.629 68.650  1.00 105.03 ? 174 GLU   a CD  1 
ATOM   47271 O  OE1 . GLU   AA 13 187 ? 70.329  -163.891 69.280  1.00 103.78 ? 174 GLU   a OE1 1 
ATOM   47272 O  OE2 . GLU   AA 13 187 ? 72.498  -164.079 68.957  1.00 106.31 ? 174 GLU   a OE2 1 
ATOM   47273 N  N   . GLU   AA 13 188 ? 73.085  -159.341 66.410  1.00 104.73 ? 175 GLU   a N   1 
ATOM   47274 C  CA  . GLU   AA 13 188 ? 72.927  -157.929 66.855  1.00 106.48 ? 175 GLU   a CA  1 
ATOM   47275 C  C   . GLU   AA 13 188 ? 72.269  -157.123 65.730  1.00 105.50 ? 175 GLU   a C   1 
ATOM   47276 O  O   . GLU   AA 13 188 ? 71.319  -156.371 66.025  1.00 106.69 ? 175 GLU   a O   1 
ATOM   47277 C  CB  . GLU   AA 13 188 ? 74.281  -157.327 67.236  1.00 111.10 ? 175 GLU   a CB  1 
ATOM   47278 C  CG  . GLU   AA 13 188 ? 74.179  -156.156 68.195  1.00 115.73 ? 175 GLU   a CG  1 
ATOM   47279 C  CD  . GLU   AA 13 188 ? 75.476  -155.821 68.911  1.00 121.77 ? 175 GLU   a CD  1 
ATOM   47280 O  OE1 . GLU   AA 13 188 ? 76.146  -156.760 69.394  1.00 120.29 ? 175 GLU   a OE1 1 
ATOM   47281 O  OE2 . GLU   AA 13 188 ? 75.815  -154.622 68.983  1.00 126.93 ? 175 GLU   a OE2 1 
ATOM   47282 N  N   . ALA   AA 13 189 ? 72.752  -157.298 64.495  1.00 102.73 ? 176 ALA   a N   1 
ATOM   47283 C  CA  . ALA   AA 13 189 ? 72.285  -156.590 63.278  1.00 102.75 ? 176 ALA   a CA  1 
ATOM   47284 C  C   . ALA   AA 13 189 ? 70.850  -157.008 62.941  1.00 101.44 ? 176 ALA   a C   1 
ATOM   47285 O  O   . ALA   AA 13 189 ? 70.065  -156.132 62.525  1.00 105.88 ? 176 ALA   a O   1 
ATOM   47286 C  CB  . ALA   AA 13 189 ? 73.222  -156.856 62.125  1.00 102.21 ? 176 ALA   a CB  1 
ATOM   47287 N  N   . ILE   AA 13 190 ? 70.523  -158.293 63.102  1.00 95.95  ? 177 ILE   a N   1 
ATOM   47288 C  CA  . ILE   AA 13 190 ? 69.146  -158.831 62.887  1.00 92.66  ? 177 ILE   a CA  1 
ATOM   47289 C  C   . ILE   AA 13 190 ? 68.206  -158.212 63.928  1.00 94.30  ? 177 ILE   a C   1 
ATOM   47290 O  O   . ILE   AA 13 190 ? 67.163  -157.675 63.521  1.00 96.59  ? 177 ILE   a O   1 
ATOM   47291 C  CB  . ILE   AA 13 190 ? 69.129  -160.372 62.934  1.00 92.49  ? 177 ILE   a CB  1 
ATOM   47292 C  CG1 . ILE   AA 13 190 ? 69.849  -160.990 61.731  1.00 90.73  ? 177 ILE   a CG1 1 
ATOM   47293 C  CG2 . ILE   AA 13 190 ? 67.703  -160.892 63.064  1.00 91.68  ? 177 ILE   a CG2 1 
ATOM   47294 C  CD1 . ILE   AA 13 190 ? 69.145  -160.790 60.404  1.00 89.79  ? 177 ILE   a CD1 1 
ATOM   47295 N  N   . VAL   AA 13 191 ? 68.568  -158.280 65.214  1.00 95.97  ? 178 VAL   a N   1 
ATOM   47296 C  CA  . VAL   AA 13 191 ? 67.732  -157.809 66.363  1.00 96.79  ? 178 VAL   a CA  1 
ATOM   47297 C  C   . VAL   AA 13 191 ? 67.495  -156.294 66.256  1.00 97.26  ? 178 VAL   a C   1 
ATOM   47298 O  O   . VAL   AA 13 191 ? 66.406  -155.837 66.668  1.00 93.76  ? 178 VAL   a O   1 
ATOM   47299 C  CB  . VAL   AA 13 191 ? 68.364  -158.193 67.718  1.00 96.79  ? 178 VAL   a CB  1 
ATOM   47300 C  CG1 . VAL   AA 13 191 ? 67.728  -157.446 68.882  1.00 95.99  ? 178 VAL   a CG1 1 
ATOM   47301 C  CG2 . VAL   AA 13 191 ? 68.300  -159.693 67.958  1.00 97.29  ? 178 VAL   a CG2 1 
ATOM   47302 N  N   . ASN   AA 13 192 ? 68.474  -155.542 65.742  1.00 96.85  ? 179 ASN   a N   1 
ATOM   47303 C  CA  . ASN   AA 13 192 ? 68.361  -154.077 65.503  1.00 96.91  ? 179 ASN   a CA  1 
ATOM   47304 C  C   . ASN   AA 13 192 ? 67.350  -153.818 64.380  1.00 94.93  ? 179 ASN   a C   1 
ATOM   47305 O  O   . ASN   AA 13 192 ? 66.483  -152.941 64.560  1.00 96.26  ? 179 ASN   a O   1 
ATOM   47306 C  CB  . ASN   AA 13 192 ? 69.711  -153.440 65.167  1.00 98.49  ? 179 ASN   a CB  1 
ATOM   47307 C  CG  . ASN   AA 13 192 ? 69.574  -151.999 64.727  1.00 98.30  ? 179 ASN   a CG  1 
ATOM   47308 O  OD1 . ASN   AA 13 192 ? 69.870  -151.667 63.582  1.00 101.20 ? 179 ASN   a OD1 1 
ATOM   47309 N  ND2 . ASN   AA 13 192 ? 69.092  -151.148 65.616  1.00 99.48  ? 179 ASN   a ND2 1 
ATOM   47310 N  N   . ALA   AA 13 193 ? 67.470  -154.547 63.264  1.00 92.54  ? 180 ALA   a N   1 
ATOM   47311 C  CA  . ALA   AA 13 193 ? 66.583  -154.453 62.081  1.00 89.84  ? 180 ALA   a CA  1 
ATOM   47312 C  C   . ALA   AA 13 193 ? 65.134  -154.737 62.493  1.00 89.63  ? 180 ALA   a C   1 
ATOM   47313 O  O   . ALA   AA 13 193 ? 64.236  -154.049 61.977  1.00 91.87  ? 180 ALA   a O   1 
ATOM   47314 C  CB  . ALA   AA 13 193 ? 67.044  -155.404 61.005  1.00 88.74  ? 180 ALA   a CB  1 
ATOM   47315 N  N   . MET   AA 13 194 ? 64.921  -155.711 63.385  1.00 90.18  ? 181 MET   a N   1 
ATOM   47316 C  CA  . MET   AA 13 194 ? 63.579  -156.097 63.903  1.00 92.58  ? 181 MET   a CA  1 
ATOM   47317 C  C   . MET   AA 13 194 ? 62.967  -154.920 64.672  1.00 92.84  ? 181 MET   a C   1 
ATOM   47318 O  O   . MET   AA 13 194 ? 61.741  -154.710 64.531  1.00 90.61  ? 181 MET   a O   1 
ATOM   47319 C  CB  . MET   AA 13 194 ? 63.658  -157.322 64.823  1.00 95.17  ? 181 MET   a CB  1 
ATOM   47320 C  CG  . MET   AA 13 194 ? 63.971  -158.629 64.099  1.00 97.12  ? 181 MET   a CG  1 
ATOM   47321 S  SD  . MET   AA 13 194 ? 62.835  -159.037 62.739  1.00 95.06  ? 181 MET   a SD  1 
ATOM   47322 C  CE  . MET   AA 13 194 ? 61.289  -159.201 63.633  1.00 101.62 ? 181 MET   a CE  1 
ATOM   47323 N  N   . ARG   AA 13 195 ? 63.781  -154.192 65.451  1.00 95.69  ? 182 ARG   a N   1 
ATOM   47324 C  CA  . ARG   AA 13 195 ? 63.345  -152.988 66.214  1.00 96.39  ? 182 ARG   a CA  1 
ATOM   47325 C  C   . ARG   AA 13 195 ? 62.911  -151.904 65.220  1.00 94.25  ? 182 ARG   a C   1 
ATOM   47326 O  O   . ARG   AA 13 195 ? 61.813  -151.341 65.408  1.00 96.77  ? 182 ARG   a O   1 
ATOM   47327 C  CB  . ARG   AA 13 195 ? 64.445  -152.466 67.148  1.00 98.79  ? 182 ARG   a CB  1 
ATOM   47328 C  CG  . ARG   AA 13 195 ? 64.146  -151.092 67.732  1.00 100.24 ? 182 ARG   a CG  1 
ATOM   47329 C  CD  . ARG   AA 13 195 ? 64.997  -150.724 68.932  1.00 103.19 ? 182 ARG   a CD  1 
ATOM   47330 N  NE  . ARG   AA 13 195 ? 66.431  -150.761 68.659  1.00 105.25 ? 182 ARG   a NE  1 
ATOM   47331 C  CZ  . ARG   AA 13 195 ? 67.298  -151.632 69.175  1.00 105.01 ? 182 ARG   a CZ  1 
ATOM   47332 N  NH1 . ARG   AA 13 195 ? 68.579  -151.550 68.854  1.00 107.33 ? 182 ARG   a NH1 1 
ATOM   47333 N  NH2 . ARG   AA 13 195 ? 66.903  -152.575 70.012  1.00 106.97 ? 182 ARG   a NH2 1 
ATOM   47334 N  N   . VAL   AA 13 196 ? 63.738  -151.638 64.203  1.00 90.58  ? 183 VAL   a N   1 
ATOM   47335 C  CA  . VAL   AA 13 196 ? 63.493  -150.586 63.170  1.00 89.98  ? 183 VAL   a CA  1 
ATOM   47336 C  C   . VAL   AA 13 196 ? 62.161  -150.881 62.474  1.00 90.69  ? 183 VAL   a C   1 
ATOM   47337 O  O   . VAL   AA 13 196 ? 61.396  -149.928 62.249  1.00 92.84  ? 183 VAL   a O   1 
ATOM   47338 C  CB  . VAL   AA 13 196 ? 64.651  -150.487 62.157  1.00 89.94  ? 183 VAL   a CB  1 
ATOM   47339 C  CG1 . VAL   AA 13 196 ? 64.299  -149.592 60.978  1.00 91.52  ? 183 VAL   a CG1 1 
ATOM   47340 C  CG2 . VAL   AA 13 196 ? 65.933  -150.005 62.815  1.00 90.05  ? 183 VAL   a CG2 1 
ATOM   47341 N  N   . LEU   AA 13 197 ? 61.899  -152.147 62.142  1.00 88.66  ? 184 LEU   a N   1 
ATOM   47342 C  CA  . LEU   AA 13 197 ? 60.635  -152.580 61.491  1.00 88.53  ? 184 LEU   a CA  1 
ATOM   47343 C  C   . LEU   AA 13 197 ? 59.447  -152.288 62.417  1.00 88.84  ? 184 LEU   a C   1 
ATOM   47344 O  O   . LEU   AA 13 197 ? 58.381  -151.920 61.891  1.00 86.71  ? 184 LEU   a O   1 
ATOM   47345 C  CB  . LEU   AA 13 197 ? 60.712  -154.070 61.140  1.00 89.87  ? 184 LEU   a CB  1 
ATOM   47346 C  CG  . LEU   AA 13 197 ? 61.654  -154.440 59.994  1.00 90.42  ? 184 LEU   a CG  1 
ATOM   47347 C  CD1 . LEU   AA 13 197 ? 61.673  -155.941 59.787  1.00 90.51  ? 184 LEU   a CD1 1 
ATOM   47348 C  CD2 . LEU   AA 13 197 ? 61.267  -153.742 58.698  1.00 91.63  ? 184 LEU   a CD2 1 
ATOM   47349 N  N   . TYR   AA 13 198 ? 59.618  -152.433 63.736  1.00 90.52  ? 185 TYR   a N   1 
ATOM   47350 C  CA  . TYR   AA 13 198 ? 58.537  -152.210 64.733  1.00 92.74  ? 185 TYR   a CA  1 
ATOM   47351 C  C   . TYR   AA 13 198 ? 58.202  -150.717 64.822  1.00 90.57  ? 185 TYR   a C   1 
ATOM   47352 O  O   . TYR   AA 13 198 ? 57.019  -150.395 65.049  1.00 90.64  ? 185 TYR   a O   1 
ATOM   47353 C  CB  . TYR   AA 13 198 ? 58.898  -152.767 66.112  1.00 94.93  ? 185 TYR   a CB  1 
ATOM   47354 C  CG  . TYR   AA 13 198 ? 57.773  -152.655 67.112  1.00 99.00  ? 185 TYR   a CG  1 
ATOM   47355 C  CD1 . TYR   AA 13 198 ? 56.548  -153.260 66.874  1.00 101.17 ? 185 TYR   a CD1 1 
ATOM   47356 C  CD2 . TYR   AA 13 198 ? 57.917  -151.927 68.283  1.00 99.64  ? 185 TYR   a CD2 1 
ATOM   47357 C  CE1 . TYR   AA 13 198 ? 55.502  -153.159 67.777  1.00 101.37 ? 185 TYR   a CE1 1 
ATOM   47358 C  CE2 . TYR   AA 13 198 ? 56.881  -151.816 69.197  1.00 102.04 ? 185 TYR   a CE2 1 
ATOM   47359 C  CZ  . TYR   AA 13 198 ? 55.669  -152.436 68.944  1.00 101.01 ? 185 TYR   a CZ  1 
ATOM   47360 O  OH  . TYR   AA 13 198 ? 54.642  -152.338 69.837  1.00 102.26 ? 185 TYR   a OH  1 
ATOM   47361 N  N   . TYR   AA 13 199 ? 59.205  -149.846 64.660  1.00 91.36  ? 186 TYR   a N   1 
ATOM   47362 C  CA  . TYR   AA 13 199 ? 59.043  -148.368 64.631  1.00 92.03  ? 186 TYR   a CA  1 
ATOM   47363 C  C   . TYR   AA 13 199 ? 58.190  -147.947 63.427  1.00 89.78  ? 186 TYR   a C   1 
ATOM   47364 O  O   . TYR   AA 13 199 ? 57.380  -147.012 63.589  1.00 88.25  ? 186 TYR   a O   1 
ATOM   47365 C  CB  . TYR   AA 13 199 ? 60.388  -147.641 64.515  1.00 90.32  ? 186 TYR   a CB  1 
ATOM   47366 C  CG  . TYR   AA 13 199 ? 61.270  -147.609 65.740  1.00 88.80  ? 186 TYR   a CG  1 
ATOM   47367 C  CD1 . TYR   AA 13 199 ? 60.752  -147.490 67.021  1.00 87.80  ? 186 TYR   a CD1 1 
ATOM   47368 C  CD2 . TYR   AA 13 199 ? 62.649  -147.626 65.602  1.00 88.74  ? 186 TYR   a CD2 1 
ATOM   47369 C  CE1 . TYR   AA 13 199 ? 61.579  -147.431 68.131  1.00 88.19  ? 186 TYR   a CE1 1 
ATOM   47370 C  CE2 . TYR   AA 13 199 ? 63.490  -147.566 66.700  1.00 89.53  ? 186 TYR   a CE2 1 
ATOM   47371 C  CZ  . TYR   AA 13 199 ? 62.953  -147.467 67.970  1.00 90.04  ? 186 TYR   a CZ  1 
ATOM   47372 O  OH  . TYR   AA 13 199 ? 63.783  -147.405 69.051  1.00 90.67  ? 186 TYR   a OH  1 
ATOM   47373 N  N   . ARG   AA 13 200 ? 58.375  -148.609 62.275  1.00 89.01  ? 187 ARG   a N   1 
ATOM   47374 C  CA  . ARG   AA 13 200 ? 58.085  -148.047 60.924  1.00 90.15  ? 187 ARG   a CA  1 
ATOM   47375 C  C   . ARG   AA 13 200 ? 57.085  -148.891 60.112  1.00 92.46  ? 187 ARG   a C   1 
ATOM   47376 O  O   . ARG   AA 13 200 ? 56.436  -148.298 59.226  1.00 93.56  ? 187 ARG   a O   1 
ATOM   47377 C  CB  . ARG   AA 13 200 ? 59.403  -147.863 60.163  1.00 90.79  ? 187 ARG   a CB  1 
ATOM   47378 C  CG  . ARG   AA 13 200 ? 59.720  -146.415 59.812  1.00 93.24  ? 187 ARG   a CG  1 
ATOM   47379 C  CD  . ARG   AA 13 200 ? 59.876  -145.462 60.988  1.00 92.99  ? 187 ARG   a CD  1 
ATOM   47380 N  NE  . ARG   AA 13 200 ? 59.224  -144.182 60.714  1.00 92.23  ? 187 ARG   a NE  1 
ATOM   47381 C  CZ  . ARG   AA 13 200 ? 59.582  -142.999 61.209  1.00 89.43  ? 187 ARG   a CZ  1 
ATOM   47382 N  NH1 . ARG   AA 13 200 ? 60.621  -142.880 62.018  1.00 87.67  ? 187 ARG   a NH1 1 
ATOM   47383 N  NH2 . ARG   AA 13 200 ? 58.894  -141.922 60.876  1.00 90.93  ? 187 ARG   a NH2 1 
ATOM   47384 N  N   . ASP   AA 13 201 ? 56.973  -150.204 60.351  1.00 91.56  ? 188 ASP   a N   1 
ATOM   47385 C  CA  . ASP   AA 13 201 ? 55.976  -151.089 59.679  1.00 91.76  ? 188 ASP   a CA  1 
ATOM   47386 C  C   . ASP   AA 13 201 ? 54.692  -151.112 60.517  1.00 89.70  ? 188 ASP   a C   1 
ATOM   47387 O  O   . ASP   AA 13 201 ? 54.770  -151.496 61.696  1.00 93.64  ? 188 ASP   a O   1 
ATOM   47388 C  CB  . ASP   AA 13 201 ? 56.529  -152.505 59.475  1.00 93.29  ? 188 ASP   a CB  1 
ATOM   47389 C  CG  . ASP   AA 13 201 ? 55.602  -153.481 58.758  1.00 92.93  ? 188 ASP   a CG  1 
ATOM   47390 O  OD1 . ASP   AA 13 201 ? 54.481  -153.080 58.387  1.00 96.22  ? 188 ASP   a OD1 1 
ATOM   47391 O  OD2 . ASP   AA 13 201 ? 56.014  -154.649 58.581  1.00 91.08  ? 188 ASP   a OD2 1 
ATOM   47392 N  N   . ALA   AA 13 202 ? 53.555  -150.748 59.917  1.00 87.30  ? 189 ALA   a N   1 
ATOM   47393 C  CA  . ALA   AA 13 202 ? 52.243  -150.605 60.596  1.00 90.08  ? 189 ALA   a CA  1 
ATOM   47394 C  C   . ALA   AA 13 202 ? 51.573  -151.973 60.798  1.00 89.06  ? 189 ALA   a C   1 
ATOM   47395 O  O   . ALA   AA 13 202 ? 50.538  -152.010 61.494  1.00 85.04  ? 189 ALA   a O   1 
ATOM   47396 C  CB  . ALA   AA 13 202 ? 51.356  -149.669 59.809  1.00 92.03  ? 189 ALA   a CB  1 
ATOM   47397 N  N   . ARG   AA 13 203 ? 52.121  -153.046 60.208  1.00 91.38  ? 190 ARG   a N   1 
ATOM   47398 C  CA  . ARG   AA 13 203 ? 51.630  -154.442 60.378  1.00 92.13  ? 190 ARG   a CA  1 
ATOM   47399 C  C   . ARG   AA 13 203 ? 52.737  -155.314 60.986  1.00 90.00  ? 190 ARG   a C   1 
ATOM   47400 O  O   . ARG   AA 13 203 ? 52.800  -156.504 60.638  1.00 89.60  ? 190 ARG   a O   1 
ATOM   47401 C  CB  . ARG   AA 13 203 ? 51.148  -155.018 59.041  1.00 91.88  ? 190 ARG   a CB  1 
ATOM   47402 C  CG  . ARG   AA 13 203 ? 49.725  -154.632 58.666  1.00 96.90  ? 190 ARG   a CG  1 
ATOM   47403 C  CD  . ARG   AA 13 203 ? 49.693  -153.346 57.870  1.00 99.00  ? 190 ARG   a CD  1 
ATOM   47404 N  NE  . ARG   AA 13 203 ? 48.345  -152.939 57.481  1.00 107.00 ? 190 ARG   a NE  1 
ATOM   47405 C  CZ  . ARG   AA 13 203 ? 47.724  -151.821 57.864  1.00 106.69 ? 190 ARG   a CZ  1 
ATOM   47406 N  NH1 . ARG   AA 13 203 ? 48.311  -150.952 58.672  1.00 108.90 ? 190 ARG   a NH1 1 
ATOM   47407 N  NH2 . ARG   AA 13 203 ? 46.502  -151.571 57.427  1.00 104.38 ? 190 ARG   a NH2 1 
ATOM   47408 N  N   . SER   AA 13 204 ? 53.567  -154.752 61.868  1.00 91.51  ? 191 SER   a N   1 
ATOM   47409 C  CA  . SER   AA 13 204 ? 54.605  -155.486 62.639  1.00 90.68  ? 191 SER   a CA  1 
ATOM   47410 C  C   . SER   AA 13 204 ? 54.170  -155.586 64.103  1.00 91.60  ? 191 SER   a C   1 
ATOM   47411 O  O   . SER   AA 13 204 ? 53.495  -154.658 64.582  1.00 94.50  ? 191 SER   a O   1 
ATOM   47412 C  CB  . SER   AA 13 204 ? 55.954  -154.827 62.515  1.00 93.08  ? 191 SER   a CB  1 
ATOM   47413 O  OG  . SER   AA 13 204 ? 55.903  -153.482 62.968  1.00 92.15  ? 191 SER   a OG  1 
ATOM   47414 N  N   . SER   AA 13 205 ? 54.527  -156.680 64.777  1.00 92.91  ? 192 SER   a N   1 
ATOM   47415 C  CA  . SER   AA 13 205 ? 54.352  -156.855 66.242  1.00 94.48  ? 192 SER   a CA  1 
ATOM   47416 C  C   . SER   AA 13 205 ? 55.717  -156.783 66.934  1.00 91.26  ? 192 SER   a C   1 
ATOM   47417 O  O   . SER   AA 13 205 ? 56.759  -156.932 66.255  1.00 83.67  ? 192 SER   a O   1 
ATOM   47418 C  CB  . SER   AA 13 205 ? 53.631  -158.137 66.580  1.00 94.95  ? 192 SER   a CB  1 
ATOM   47419 O  OG  . SER   AA 13 205 ? 54.533  -159.230 66.685  1.00 97.85  ? 192 SER   a OG  1 
ATOM   47420 N  N   . ARG   AA 13 206 ? 55.689  -156.562 68.246  1.00 93.81  ? 193 ARG   a N   1 
ATOM   47421 C  CA  . ARG   AA 13 206 ? 56.893  -156.418 69.105  1.00 98.05  ? 193 ARG   a CA  1 
ATOM   47422 C  C   . ARG   AA 13 206 ? 57.519  -157.797 69.348  1.00 98.22  ? 193 ARG   a C   1 
ATOM   47423 O  O   . ARG   AA 13 206 ? 58.752  -157.870 69.527  1.00 94.02  ? 193 ARG   a O   1 
ATOM   47424 C  CB  . ARG   AA 13 206 ? 56.512  -155.763 70.435  1.00 103.48 ? 193 ARG   a CB  1 
ATOM   47425 C  CG  . ARG   AA 13 206 ? 57.707  -155.242 71.215  1.00 105.54 ? 193 ARG   a CG  1 
ATOM   47426 C  CD  . ARG   AA 13 206 ? 57.303  -154.463 72.448  1.00 108.83 ? 193 ARG   a CD  1 
ATOM   47427 N  NE  . ARG   AA 13 206 ? 58.472  -153.997 73.180  1.00 110.43 ? 193 ARG   a NE  1 
ATOM   47428 C  CZ  . ARG   AA 13 206 ? 58.438  -153.205 74.246  1.00 112.98 ? 193 ARG   a CZ  1 
ATOM   47429 N  NH1 . ARG   AA 13 206 ? 57.282  -152.781 74.731  1.00 115.79 ? 193 ARG   a NH1 1 
ATOM   47430 N  NH2 . ARG   AA 13 206 ? 59.567  -152.837 74.824  1.00 117.85 ? 193 ARG   a NH2 1 
ATOM   47431 N  N   . ASN   AA 13 207 ? 56.687  -158.840 69.373  1.00 95.83  ? 194 ASN   a N   1 
ATOM   47432 C  CA  . ASN   AA 13 207 ? 57.099  -160.242 69.636  1.00 95.76  ? 194 ASN   a CA  1 
ATOM   47433 C  C   . ASN   AA 13 207 ? 57.547  -160.888 68.325  1.00 92.28  ? 194 ASN   a C   1 
ATOM   47434 O  O   . ASN   AA 13 207 ? 56.855  -160.686 67.310  1.00 96.00  ? 194 ASN   a O   1 
ATOM   47435 C  CB  . ASN   AA 13 207 ? 55.960  -161.026 70.285  1.00 98.84  ? 194 ASN   a CB  1 
ATOM   47436 C  CG  . ASN   AA 13 207 ? 55.618  -160.477 71.651  1.00 102.86 ? 194 ASN   a CG  1 
ATOM   47437 O  OD1 . ASN   AA 13 207 ? 54.604  -159.803 71.821  1.00 98.74  ? 194 ASN   a OD1 1 
ATOM   47438 N  ND2 . ASN   AA 13 207 ? 56.485  -160.729 72.619  1.00 109.54 ? 194 ASN   a ND2 1 
ATOM   47439 N  N   . PHE   AA 13 208 ? 58.653  -161.636 68.349  1.00 89.84  ? 195 PHE   a N   1 
ATOM   47440 C  CA  . PHE   AA 13 208 ? 59.197  -162.339 67.159  1.00 90.59  ? 195 PHE   a CA  1 
ATOM   47441 C  C   . PHE   AA 13 208 ? 59.985  -163.588 67.562  1.00 91.27  ? 195 PHE   a C   1 
ATOM   47442 O  O   . PHE   AA 13 208 ? 60.347  -163.746 68.743  1.00 92.78  ? 195 PHE   a O   1 
ATOM   47443 C  CB  . PHE   AA 13 208 ? 60.072  -161.396 66.330  1.00 88.11  ? 195 PHE   a CB  1 
ATOM   47444 C  CG  . PHE   AA 13 208 ? 61.353  -160.955 66.990  1.00 87.22  ? 195 PHE   a CG  1 
ATOM   47445 C  CD1 . PHE   AA 13 208 ? 61.354  -159.925 67.917  1.00 88.18  ? 195 PHE   a CD1 1 
ATOM   47446 C  CD2 . PHE   AA 13 208 ? 62.563  -161.550 66.663  1.00 85.80  ? 195 PHE   a CD2 1 
ATOM   47447 C  CE1 . PHE   AA 13 208 ? 62.534  -159.510 68.513  1.00 89.68  ? 195 PHE   a CE1 1 
ATOM   47448 C  CE2 . PHE   AA 13 208 ? 63.743  -161.132 67.258  1.00 86.04  ? 195 PHE   a CE2 1 
ATOM   47449 C  CZ  . PHE   AA 13 208 ? 63.726  -160.114 68.183  1.00 88.51  ? 195 PHE   a CZ  1 
ATOM   47450 N  N   . SER   AA 13 209 ? 60.225  -164.451 66.573  1.00 92.91  ? 196 SER   a N   1 
ATOM   47451 C  CA  . SER   AA 13 209 ? 61.101  -165.645 66.660  1.00 95.41  ? 196 SER   a CA  1 
ATOM   47452 C  C   . SER   AA 13 209 ? 62.368  -165.396 65.835  1.00 93.89  ? 196 SER   a C   1 
ATOM   47453 O  O   . SER   AA 13 209 ? 62.287  -164.676 64.818  1.00 91.05  ? 196 SER   a O   1 
ATOM   47454 C  CB  . SER   AA 13 209 ? 60.369  -166.883 66.209  1.00 96.81  ? 196 SER   a CB  1 
ATOM   47455 O  OG  . SER   AA 13 209 ? 59.317  -167.202 67.110  1.00 97.67  ? 196 SER   a OG  1 
ATOM   47456 N  N   . LEU   AA 13 210 ? 63.494  -165.955 66.281  1.00 95.38  ? 197 LEU   a N   1 
ATOM   47457 C  CA  . LEU   AA 13 210 ? 64.808  -165.897 65.588  1.00 96.89  ? 197 LEU   a CA  1 
ATOM   47458 C  C   . LEU   AA 13 210 ? 65.428  -167.298 65.613  1.00 97.84  ? 197 LEU   a C   1 
ATOM   47459 O  O   . LEU   AA 13 210 ? 65.352  -167.957 66.669  1.00 101.04 ? 197 LEU   a O   1 
ATOM   47460 C  CB  . LEU   AA 13 210 ? 65.696  -164.872 66.298  1.00 95.99  ? 197 LEU   a CB  1 
ATOM   47461 C  CG  . LEU   AA 13 210 ? 67.091  -164.669 65.704  1.00 97.05  ? 197 LEU   a CG  1 
ATOM   47462 C  CD1 . LEU   AA 13 210 ? 67.549  -163.231 65.883  1.00 97.89  ? 197 LEU   a CD1 1 
ATOM   47463 C  CD2 . LEU   AA 13 210 ? 68.104  -165.623 66.321  1.00 97.81  ? 197 LEU   a CD2 1 
ATOM   47464 N  N   . ALA   AA 13 211 ? 66.012  -167.732 64.493  1.00 97.44  ? 198 ALA   a N   1 
ATOM   47465 C  CA  . ALA   AA 13 211 ? 66.674  -169.048 64.351  1.00 98.03  ? 198 ALA   a CA  1 
ATOM   47466 C  C   . ALA   AA 13 211 ? 68.093  -168.861 63.807  1.00 97.48  ? 198 ALA   a C   1 
ATOM   47467 O  O   . ALA   AA 13 211 ? 68.273  -168.069 62.860  1.00 91.91  ? 198 ALA   a O   1 
ATOM   47468 C  CB  . ALA   AA 13 211 ? 65.857  -169.949 63.461  1.00 100.80 ? 198 ALA   a CB  1 
ATOM   47469 N  N   . ILE   AA 13 212 ? 69.052  -169.572 64.405  1.00 100.17 ? 199 ILE   a N   1 
ATOM   47470 C  CA  . ILE   AA 13 212 ? 70.472  -169.666 63.956  1.00 101.72 ? 199 ILE   a CA  1 
ATOM   47471 C  C   . ILE   AA 13 212 ? 70.723  -171.111 63.527  1.00 103.41 ? 199 ILE   a C   1 
ATOM   47472 O  O   . ILE   AA 13 212 ? 70.475  -172.006 64.351  1.00 110.06 ? 199 ILE   a O   1 
ATOM   47473 C  CB  . ILE   AA 13 212 ? 71.438  -169.254 65.085  1.00 102.88 ? 199 ILE   a CB  1 
ATOM   47474 C  CG1 . ILE   AA 13 212 ? 71.087  -167.888 65.679  1.00 102.93 ? 199 ILE   a CG1 1 
ATOM   47475 C  CG2 . ILE   AA 13 212 ? 72.882  -169.301 64.605  1.00 104.71 ? 199 ILE   a CG2 1 
ATOM   47476 C  CD1 . ILE   AA 13 212 ? 71.526  -167.723 67.111  1.00 104.10 ? 199 ILE   a CD1 1 
ATOM   47477 N  N   . ILE   AA 13 213 ? 71.193  -171.323 62.295  1.00 104.85 ? 200 ILE   a N   1 
ATOM   47478 C  CA  . ILE   AA 13 213 ? 71.678  -172.649 61.806  1.00 106.83 ? 200 ILE   a CA  1 
ATOM   47479 C  C   . ILE   AA 13 213 ? 73.195  -172.544 61.621  1.00 109.33 ? 200 ILE   a C   1 
ATOM   47480 O  O   . ILE   AA 13 213 ? 73.631  -171.964 60.608  1.00 111.65 ? 200 ILE   a O   1 
ATOM   47481 C  CB  . ILE   AA 13 213 ? 70.947  -173.094 60.520  1.00 105.06 ? 200 ILE   a CB  1 
ATOM   47482 C  CG1 . ILE   AA 13 213 ? 69.424  -172.989 60.660  1.00 104.27 ? 200 ILE   a CG1 1 
ATOM   47483 C  CG2 . ILE   AA 13 213 ? 71.372  -174.501 60.123  1.00 104.22 ? 200 ILE   a CG2 1 
ATOM   47484 C  CD1 . ILE   AA 13 213 ? 68.834  -171.714 60.103  1.00 102.92 ? 200 ILE   a CD1 1 
ATOM   47485 N  N   . ASP   AA 13 214 ? 73.956  -173.065 62.589  1.00 109.56 ? 201 ASP   a N   1 
ATOM   47486 C  CA  . ASP   AA 13 214 ? 75.442  -173.021 62.626  1.00 112.52 ? 201 ASP   a CA  1 
ATOM   47487 C  C   . ASP   AA 13 214 ? 75.992  -174.395 62.229  1.00 112.11 ? 201 ASP   a C   1 
ATOM   47488 O  O   . ASP   AA 13 214 ? 75.383  -175.408 62.624  1.00 113.39 ? 201 ASP   a O   1 
ATOM   47489 C  CB  . ASP   AA 13 214 ? 75.937  -172.607 64.014  1.00 117.45 ? 201 ASP   a CB  1 
ATOM   47490 C  CG  . ASP   AA 13 214 ? 77.411  -172.240 64.058  1.00 122.28 ? 201 ASP   a CG  1 
ATOM   47491 O  OD1 . ASP   AA 13 214 ? 78.248  -173.159 63.949  1.00 127.41 ? 201 ASP   a OD1 1 
ATOM   47492 O  OD2 . ASP   AA 13 214 ? 77.711  -171.034 64.193  1.00 125.73 ? 201 ASP   a OD2 1 
ATOM   47493 N  N   . LYS   AA 13 215 ? 77.111  -174.423 61.497  1.00 108.18 ? 202 LYS   a N   1 
ATOM   47494 C  CA  . LYS   AA 13 215 ? 77.737  -175.672 60.982  1.00 107.36 ? 202 LYS   a CA  1 
ATOM   47495 C  C   . LYS   AA 13 215 ? 78.412  -176.439 62.129  1.00 109.11 ? 202 LYS   a C   1 
ATOM   47496 O  O   . LYS   AA 13 215 ? 78.743  -177.620 61.916  1.00 108.69 ? 202 LYS   a O   1 
ATOM   47497 C  CB  . LYS   AA 13 215 ? 78.716  -175.365 59.843  1.00 105.83 ? 202 LYS   a CB  1 
ATOM   47498 C  CG  . LYS   AA 13 215 ? 80.031  -174.707 60.236  1.00 105.40 ? 202 LYS   a CG  1 
ATOM   47499 C  CD  . LYS   AA 13 215 ? 80.975  -174.557 59.063  1.00 108.70 ? 202 LYS   a CD  1 
ATOM   47500 C  CE  . LYS   AA 13 215 ? 82.215  -173.752 59.390  1.00 110.48 ? 202 LYS   a CE  1 
ATOM   47501 N  NZ  . LYS   AA 13 215 ? 83.112  -173.635 58.216  1.00 114.11 ? 202 LYS   a NZ  1 
ATOM   47502 N  N   . ASN   AA 13 216 ? 78.606  -175.804 63.291  1.00 110.78 ? 203 ASN   a N   1 
ATOM   47503 C  CA  . ASN   AA 13 216 ? 79.243  -176.419 64.487  1.00 113.73 ? 203 ASN   a CA  1 
ATOM   47504 C  C   . ASN   AA 13 216 ? 78.186  -176.708 65.561  1.00 119.86 ? 203 ASN   a C   1 
ATOM   47505 O  O   . ASN   AA 13 216 ? 78.087  -177.878 65.976  1.00 122.17 ? 203 ASN   a O   1 
ATOM   47506 C  CB  . ASN   AA 13 216 ? 80.371  -175.543 65.037  1.00 116.84 ? 203 ASN   a CB  1 
ATOM   47507 C  CG  . ASN   AA 13 216 ? 81.507  -175.378 64.050  1.00 117.55 ? 203 ASN   a CG  1 
ATOM   47508 O  OD1 . ASN   AA 13 216 ? 81.988  -176.358 63.486  1.00 115.90 ? 203 ASN   a OD1 1 
ATOM   47509 N  ND2 . ASN   AA 13 216 ? 81.941  -174.147 63.829  1.00 118.65 ? 203 ASN   a ND2 1 
ATOM   47510 N  N   . THR   AA 13 217 ? 77.435  -175.690 65.998  1.00 120.55 ? 204 THR   a N   1 
ATOM   47511 C  CA  . THR   AA 13 217 ? 76.475  -175.777 67.136  1.00 124.00 ? 204 THR   a CA  1 
ATOM   47512 C  C   . THR   AA 13 217 ? 75.085  -176.233 66.664  1.00 122.17 ? 204 THR   a C   1 
ATOM   47513 O  O   . THR   AA 13 217 ? 74.270  -176.581 67.542  1.00 123.72 ? 204 THR   a O   1 
ATOM   47514 C  CB  . THR   AA 13 217 ? 76.398  -174.457 67.915  1.00 125.48 ? 204 THR   a CB  1 
ATOM   47515 O  OG1 . THR   AA 13 217 ? 76.602  -173.364 67.018  1.00 128.88 ? 204 THR   a OG1 1 
ATOM   47516 C  CG2 . THR   AA 13 217 ? 77.414  -174.388 69.034  1.00 129.51 ? 204 THR   a CG2 1 
ATOM   47517 N  N   . GLY   AA 13 218 ? 74.818  -176.238 65.352  1.00 119.24 ? 205 GLY   a N   1 
ATOM   47518 C  CA  . GLY   AA 13 218 ? 73.557  -176.744 64.771  1.00 113.71 ? 205 GLY   a CA  1 
ATOM   47519 C  C   . GLY   AA 13 218 ? 72.441  -175.712 64.830  1.00 108.70 ? 205 GLY   a C   1 
ATOM   47520 O  O   . GLY   AA 13 218 ? 72.753  -174.502 64.825  1.00 106.03 ? 205 GLY   a O   1 
ATOM   47521 N  N   . LEU   AA 13 219 ? 71.186  -176.175 64.884  1.00 106.51 ? 206 LEU   a N   1 
ATOM   47522 C  CA  . LEU   AA 13 219 ? 69.959  -175.330 64.867  1.00 101.88 ? 206 LEU   a CA  1 
ATOM   47523 C  C   . LEU   AA 13 219 ? 69.630  -174.870 66.292  1.00 101.32 ? 206 LEU   a C   1 
ATOM   47524 O  O   . LEU   AA 13 219 ? 69.356  -175.737 67.145  1.00 96.37  ? 206 LEU   a O   1 
ATOM   47525 C  CB  . LEU   AA 13 219 ? 68.793  -176.126 64.267  1.00 102.65 ? 206 LEU   a CB  1 
ATOM   47526 C  CG  . LEU   AA 13 219 ? 67.404  -175.506 64.429  1.00 103.92 ? 206 LEU   a CG  1 
ATOM   47527 C  CD1 . LEU   AA 13 219 ? 67.322  -174.155 63.736  1.00 105.86 ? 206 LEU   a CD1 1 
ATOM   47528 C  CD2 . LEU   AA 13 219 ? 66.326  -176.436 63.898  1.00 103.78 ? 206 LEU   a CD2 1 
ATOM   47529 N  N   . THR   AA 13 220 ? 69.645  -173.553 66.523  1.00 98.48  ? 207 THR   a N   1 
ATOM   47530 C  CA  . THR   AA 13 220 ? 69.166  -172.888 67.764  1.00 99.26  ? 207 THR   a CA  1 
ATOM   47531 C  C   . THR   AA 13 220 ? 67.918  -172.068 67.429  1.00 99.50  ? 207 THR   a C   1 
ATOM   47532 O  O   . THR   AA 13 220 ? 68.051  -171.071 66.691  1.00 101.41 ? 207 THR   a O   1 
ATOM   47533 C  CB  . THR   AA 13 220 ? 70.241  -171.988 68.386  1.00 100.35 ? 207 THR   a CB  1 
ATOM   47534 O  OG1 . THR   AA 13 220 ? 71.457  -172.731 68.465  1.00 100.11 ? 207 THR   a OG1 1 
ATOM   47535 C  CG2 . THR   AA 13 220 ? 69.857  -171.495 69.763  1.00 100.12 ? 207 THR   a CG2 1 
ATOM   47536 N  N   . PHE   AA 13 221 ? 66.759  -172.482 67.947  1.00 98.98  ? 208 PHE   a N   1 
ATOM   47537 C  CA  . PHE   AA 13 221 ? 65.446  -171.822 67.730  1.00 99.15  ? 208 PHE   a CA  1 
ATOM   47538 C  C   . PHE   AA 13 221 ? 65.077  -171.025 68.987  1.00 99.78  ? 208 PHE   a C   1 
ATOM   47539 O  O   . PHE   AA 13 221 ? 64.951  -171.635 70.065  1.00 103.33 ? 208 PHE   a O   1 
ATOM   47540 C  CB  . PHE   AA 13 221 ? 64.382  -172.863 67.376  1.00 98.00  ? 208 PHE   a CB  1 
ATOM   47541 C  CG  . PHE   AA 13 221 ? 63.210  -172.314 66.606  1.00 97.89  ? 208 PHE   a CG  1 
ATOM   47542 C  CD1 . PHE   AA 13 221 ? 62.124  -171.761 67.267  1.00 98.64  ? 208 PHE   a CD1 1 
ATOM   47543 C  CD2 . PHE   AA 13 221 ? 63.198  -172.341 65.221  1.00 98.08  ? 208 PHE   a CD2 1 
ATOM   47544 C  CE1 . PHE   AA 13 221 ? 61.048  -171.251 66.559  1.00 99.36  ? 208 PHE   a CE1 1 
ATOM   47545 C  CE2 . PHE   AA 13 221 ? 62.121  -171.830 64.514  1.00 99.63  ? 208 PHE   a CE2 1 
ATOM   47546 C  CZ  . PHE   AA 13 221 ? 61.049  -171.284 65.184  1.00 99.79  ? 208 PHE   a CZ  1 
ATOM   47547 N  N   . LYS   AA 13 222 ? 64.922  -169.704 68.848  1.00 98.33  ? 209 LYS   a N   1 
ATOM   47548 C  CA  . LYS   AA 13 222 ? 64.592  -168.769 69.957  1.00 99.39  ? 209 LYS   a CA  1 
ATOM   47549 C  C   . LYS   AA 13 222 ? 63.172  -168.228 69.768  1.00 99.11  ? 209 LYS   a C   1 
ATOM   47550 O  O   . LYS   AA 13 222 ? 62.934  -167.540 68.757  1.00 97.21  ? 209 LYS   a O   1 
ATOM   47551 C  CB  . LYS   AA 13 222 ? 65.600  -167.619 69.996  1.00 101.89 ? 209 LYS   a CB  1 
ATOM   47552 C  CG  . LYS   AA 13 222 ? 67.049  -168.044 70.183  1.00 105.70 ? 209 LYS   a CG  1 
ATOM   47553 C  CD  . LYS   AA 13 222 ? 67.980  -166.876 70.390  1.00 108.39 ? 209 LYS   a CD  1 
ATOM   47554 C  CE  . LYS   AA 13 222 ? 69.437  -167.276 70.456  1.00 112.30 ? 209 LYS   a CE  1 
ATOM   47555 N  NZ  . LYS   AA 13 222 ? 70.292  -166.125 70.831  1.00 113.85 ? 209 LYS   a NZ  1 
ATOM   47556 N  N   . LYS   AA 13 223 ? 62.279  -168.522 70.719  1.00 99.73  ? 210 LYS   a N   1 
ATOM   47557 C  CA  . LYS   AA 13 223 ? 60.849  -168.110 70.697  1.00 102.41 ? 210 LYS   a CA  1 
ATOM   47558 C  C   . LYS   AA 13 223 ? 60.611  -166.994 71.721  1.00 102.67 ? 210 LYS   a C   1 
ATOM   47559 O  O   . LYS   AA 13 223 ? 61.394  -166.898 72.686  1.00 104.24 ? 210 LYS   a O   1 
ATOM   47560 C  CB  . LYS   AA 13 223 ? 59.941  -169.304 71.009  1.00 102.70 ? 210 LYS   a CB  1 
ATOM   47561 C  CG  . LYS   AA 13 223 ? 59.788  -170.318 69.886  1.00 102.59 ? 210 LYS   a CG  1 
ATOM   47562 C  CD  . LYS   AA 13 223 ? 58.950  -171.516 70.274  1.00 107.55 ? 210 LYS   a CD  1 
ATOM   47563 C  CE  . LYS   AA 13 223 ? 58.598  -172.406 69.099  1.00 109.38 ? 210 LYS   a CE  1 
ATOM   47564 N  NZ  . LYS   AA 13 223 ? 57.515  -171.825 68.270  1.00 109.03 ? 210 LYS   a NZ  1 
ATOM   47565 N  N   . ASN   AA 13 224 ? 59.558  -166.197 71.503  1.00 103.16 ? 211 ASN   a N   1 
ATOM   47566 C  CA  . ASN   AA 13 224 ? 59.025  -165.182 72.453  1.00 104.37 ? 211 ASN   a CA  1 
ATOM   47567 C  C   . ASN   AA 13 224 ? 60.066  -164.088 72.724  1.00 104.50 ? 211 ASN   a C   1 
ATOM   47568 O  O   . ASN   AA 13 224 ? 60.082  -163.568 73.857  1.00 106.42 ? 211 ASN   a O   1 
ATOM   47569 C  CB  . ASN   AA 13 224 ? 58.574  -165.824 73.768  1.00 108.12 ? 211 ASN   a CB  1 
ATOM   47570 C  CG  . ASN   AA 13 224 ? 57.438  -166.806 73.583  1.00 108.02 ? 211 ASN   a CG  1 
ATOM   47571 O  OD1 . ASN   AA 13 224 ? 57.612  -168.005 73.788  1.00 113.32 ? 211 ASN   a OD1 1 
ATOM   47572 N  ND2 . ASN   AA 13 224 ? 56.276  -166.310 73.192  1.00 108.03 ? 211 ASN   a ND2 1 
ATOM   47573 N  N   . LEU   AA 13 225 ? 60.894  -163.745 71.732  1.00 103.43 ? 212 LEU   a N   1 
ATOM   47574 C  CA  . LEU   AA 13 225 ? 61.810  -162.572 71.795  1.00 102.17 ? 212 LEU   a CA  1 
ATOM   47575 C  C   . LEU   AA 13 225 ? 60.961  -161.300 71.728  1.00 104.92 ? 212 LEU   a C   1 
ATOM   47576 O  O   . LEU   AA 13 225 ? 59.879  -161.350 71.111  1.00 106.02 ? 212 LEU   a O   1 
ATOM   47577 C  CB  . LEU   AA 13 225 ? 62.819  -162.621 70.641  1.00 101.33 ? 212 LEU   a CB  1 
ATOM   47578 C  CG  . LEU   AA 13 225 ? 64.154  -163.315 70.922  1.00 99.89  ? 212 LEU   a CG  1 
ATOM   47579 C  CD1 . LEU   AA 13 225 ? 63.987  -164.527 71.825  1.00 99.42  ? 212 LEU   a CD1 1 
ATOM   47580 C  CD2 . LEU   AA 13 225 ? 64.831  -163.717 69.620  1.00 100.89 ? 212 LEU   a CD2 1 
ATOM   47581 N  N   . GLN   AA 13 226 ? 61.429  -160.216 72.352  1.00 107.28 ? 213 GLN   a N   1 
ATOM   47582 C  CA  . GLN   AA 13 226 ? 60.762  -158.887 72.322  1.00 109.32 ? 213 GLN   a CA  1 
ATOM   47583 C  C   . GLN   AA 13 226 ? 61.745  -157.826 71.820  1.00 112.42 ? 213 GLN   a C   1 
ATOM   47584 O  O   . GLN   AA 13 226 ? 62.950  -157.937 72.126  1.00 115.91 ? 213 GLN   a O   1 
ATOM   47585 C  CB  . GLN   AA 13 226 ? 60.239  -158.501 73.707  1.00 111.26 ? 213 GLN   a CB  1 
ATOM   47586 C  CG  . GLN   AA 13 226 ? 58.873  -159.093 74.028  1.00 112.23 ? 213 GLN   a CG  1 
ATOM   47587 C  CD  . GLN   AA 13 226 ? 57.997  -158.189 74.864  1.00 114.70 ? 213 GLN   a CD  1 
ATOM   47588 O  OE1 . GLN   AA 13 226 ? 56.773  -158.228 74.758  1.00 116.71 ? 213 GLN   a OE1 1 
ATOM   47589 N  NE2 . GLN   AA 13 226 ? 58.607  -157.363 75.702  1.00 116.26 ? 213 GLN   a NE2 1 
ATOM   47590 N  N   . VAL   AA 13 227 ? 61.233  -156.844 71.071  1.00 111.80 ? 214 VAL   a N   1 
ATOM   47591 C  CA  . VAL   AA 13 227 ? 61.949  -155.583 70.719  1.00 113.94 ? 214 VAL   a CA  1 
ATOM   47592 C  C   . VAL   AA 13 227 ? 62.095  -154.765 72.008  1.00 113.13 ? 214 VAL   a C   1 
ATOM   47593 O  O   . VAL   AA 13 227 ? 61.084  -154.601 72.724  1.00 109.27 ? 214 VAL   a O   1 
ATOM   47594 C  CB  . VAL   AA 13 227 ? 61.199  -154.800 69.623  1.00 111.23 ? 214 VAL   a CB  1 
ATOM   47595 C  CG1 . VAL   AA 13 227 ? 61.765  -153.401 69.422  1.00 112.32 ? 214 VAL   a CG1 1 
ATOM   47596 C  CG2 . VAL   AA 13 227 ? 61.174  -155.561 68.307  1.00 111.20 ? 214 VAL   a CG2 1 
ATOM   47597 N  N   . GLU   AA 13 228 ? 63.307  -154.286 72.298  1.00 115.61 ? 215 GLU   a N   1 
ATOM   47598 C  CA  . GLU   AA 13 228 ? 63.615  -153.497 73.521  1.00 120.82 ? 215 GLU   a CA  1 
ATOM   47599 C  C   . GLU   AA 13 228 ? 64.749  -152.510 73.229  1.00 121.99 ? 215 GLU   a C   1 
ATOM   47600 O  O   . GLU   AA 13 228 ? 65.303  -152.562 72.113  1.00 127.95 ? 215 GLU   a O   1 
ATOM   47601 C  CB  . GLU   AA 13 228 ? 63.946  -154.442 74.678  1.00 123.66 ? 215 GLU   a CB  1 
ATOM   47602 C  CG  . GLU   AA 13 228 ? 62.810  -154.584 75.678  1.00 129.99 ? 215 GLU   a CG  1 
ATOM   47603 C  CD  . GLU   AA 13 228 ? 62.561  -155.989 76.200  1.00 134.29 ? 215 GLU   a CD  1 
ATOM   47604 O  OE1 . GLU   AA 13 228 ? 63.491  -156.818 76.148  1.00 140.60 ? 215 GLU   a OE1 1 
ATOM   47605 O  OE2 . GLU   AA 13 228 ? 61.430  -156.251 76.655  1.00 146.80 ? 215 GLU   a OE2 1 
ATOM   47606 N  N   . ASN   AA 13 229 ? 65.058  -151.643 74.200  1.00 124.96 ? 216 ASN   a N   1 
ATOM   47607 C  CA  . ASN   AA 13 229 ? 66.016  -150.511 74.072  1.00 123.80 ? 216 ASN   a CA  1 
ATOM   47608 C  C   . ASN   AA 13 229 ? 65.511  -149.557 72.982  1.00 119.29 ? 216 ASN   a C   1 
ATOM   47609 O  O   . ASN   AA 13 229 ? 66.314  -149.169 72.106  1.00 114.77 ? 216 ASN   a O   1 
ATOM   47610 C  CB  . ASN   AA 13 229 ? 67.442  -150.997 73.794  1.00 125.74 ? 216 ASN   a CB  1 
ATOM   47611 C  CG  . ASN   AA 13 229 ? 67.990  -151.872 74.900  1.00 128.68 ? 216 ASN   a CG  1 
ATOM   47612 O  OD1 . ASN   AA 13 229 ? 67.594  -151.738 76.056  1.00 136.32 ? 216 ASN   a OD1 1 
ATOM   47613 N  ND2 . ASN   AA 13 229 ? 68.906  -152.765 74.561  1.00 127.77 ? 216 ASN   a ND2 1 
ATOM   47614 N  N   . MET   AA 13 230 ? 64.226  -149.197 73.046  1.00 114.19 ? 217 MET   a N   1 
ATOM   47615 C  CA  . MET   AA 13 230 ? 63.555  -148.313 72.058  1.00 111.35 ? 217 MET   a CA  1 
ATOM   47616 C  C   . MET   AA 13 230 ? 63.693  -146.860 72.517  1.00 111.08 ? 217 MET   a C   1 
ATOM   47617 O  O   . MET   AA 13 230 ? 63.708  -146.629 73.742  1.00 117.67 ? 217 MET   a O   1 
ATOM   47618 C  CB  . MET   AA 13 230 ? 62.072  -148.669 71.908  1.00 111.33 ? 217 MET   a CB  1 
ATOM   47619 C  CG  . MET   AA 13 230 ? 61.844  -150.009 71.224  1.00 111.25 ? 217 MET   a CG  1 
ATOM   47620 S  SD  . MET   AA 13 230 ? 60.123  -150.316 70.727  1.00 107.98 ? 217 MET   a SD  1 
ATOM   47621 C  CE  . MET   AA 13 230 ? 59.300  -150.288 72.318  1.00 105.74 ? 217 MET   a CE  1 
ATOM   47622 N  N   . LYS   AA 13 231 ? 63.807  -145.934 71.560  1.00 111.24 ? 218 LYS   a N   1 
ATOM   47623 C  CA  . LYS   AA 13 231 ? 63.855  -144.468 71.796  1.00 108.39 ? 218 LYS   a CA  1 
ATOM   47624 C  C   . LYS   AA 13 231 ? 62.458  -143.893 71.545  1.00 102.28 ? 218 LYS   a C   1 
ATOM   47625 O  O   . LYS   AA 13 231 ? 62.003  -143.932 70.387  1.00 98.27  ? 218 LYS   a O   1 
ATOM   47626 C  CB  . LYS   AA 13 231 ? 64.909  -143.813 70.898  1.00 112.22 ? 218 LYS   a CB  1 
ATOM   47627 C  CG  . LYS   AA 13 231 ? 66.353  -144.101 71.287  1.00 114.42 ? 218 LYS   a CG  1 
ATOM   47628 C  CD  . LYS   AA 13 231 ? 67.365  -143.267 70.525  1.00 117.30 ? 218 LYS   a CD  1 
ATOM   47629 C  CE  . LYS   AA 13 231 ? 68.789  -143.476 70.996  1.00 115.67 ? 218 LYS   a CE  1 
ATOM   47630 N  NZ  . LYS   AA 13 231 ? 69.283  -144.833 70.665  1.00 115.80 ? 218 LYS   a NZ  1 
ATOM   47631 N  N   . TRP   AA 13 232 ? 61.798  -143.422 72.605  1.00 103.54 ? 219 TRP   a N   1 
ATOM   47632 C  CA  . TRP   AA 13 232 ? 60.483  -142.726 72.553  1.00 106.20 ? 219 TRP   a CA  1 
ATOM   47633 C  C   . TRP   AA 13 232 ? 60.526  -141.386 73.301  1.00 110.12 ? 219 TRP   a C   1 
ATOM   47634 O  O   . TRP   AA 13 232 ? 59.624  -140.561 73.059  1.00 112.14 ? 219 TRP   a O   1 
ATOM   47635 C  CB  . TRP   AA 13 232 ? 59.387  -143.633 73.118  1.00 104.24 ? 219 TRP   a CB  1 
ATOM   47636 C  CG  . TRP   AA 13 232 ? 59.030  -144.766 72.212  1.00 103.12 ? 219 TRP   a CG  1 
ATOM   47637 C  CD1 . TRP   AA 13 232 ? 59.404  -146.070 72.338  1.00 104.13 ? 219 TRP   a CD1 1 
ATOM   47638 C  CD2 . TRP   AA 13 232 ? 58.229  -144.689 71.020  1.00 104.32 ? 219 TRP   a CD2 1 
ATOM   47639 N  NE1 . TRP   AA 13 232 ? 58.886  -146.813 71.312  1.00 105.00 ? 219 TRP   a NE1 1 
ATOM   47640 C  CE2 . TRP   AA 13 232 ? 58.160  -145.994 70.488  1.00 103.65 ? 219 TRP   a CE2 1 
ATOM   47641 C  CE3 . TRP   AA 13 232 ? 57.563  -143.653 70.356  1.00 102.84 ? 219 TRP   a CE3 1 
ATOM   47642 C  CZ2 . TRP   AA 13 232 ? 57.451  -146.285 69.323  1.00 105.08 ? 219 TRP   a CZ2 1 
ATOM   47643 C  CZ3 . TRP   AA 13 232 ? 56.862  -143.941 69.207  1.00 101.45 ? 219 TRP   a CZ3 1 
ATOM   47644 C  CH2 . TRP   AA 13 232 ? 56.811  -145.239 68.698  1.00 102.99 ? 219 TRP   a CH2 1 
ATOM   47645 N  N   . ASP   AA 13 233 ? 61.525  -141.175 74.165  1.00 109.65 ? 220 ASP   a N   1 
ATOM   47646 C  CA  . ASP   AA 13 233 ? 61.582  -140.038 75.121  1.00 112.63 ? 220 ASP   a CA  1 
ATOM   47647 C  C   . ASP   AA 13 233 ? 61.432  -138.709 74.368  1.00 110.61 ? 220 ASP   a C   1 
ATOM   47648 O  O   . ASP   AA 13 233 ? 60.660  -137.865 74.844  1.00 112.93 ? 220 ASP   a O   1 
ATOM   47649 C  CB  . ASP   AA 13 233 ? 62.869  -140.075 75.946  1.00 115.83 ? 220 ASP   a CB  1 
ATOM   47650 C  CG  . ASP   AA 13 233 ? 62.843  -139.129 77.131  1.00 119.13 ? 220 ASP   a CG  1 
ATOM   47651 O  OD1 . ASP   AA 13 233 ? 61.971  -139.310 78.006  1.00 121.08 ? 220 ASP   a OD1 1 
ATOM   47652 O  OD2 . ASP   AA 13 233 ? 63.674  -138.199 77.155  1.00 120.85 ? 220 ASP   a OD2 1 
ATOM   47653 N  N   . PHE   AA 13 234 ? 62.115  -138.549 73.228  1.00 108.87 ? 221 PHE   a N   1 
ATOM   47654 C  CA  . PHE   AA 13 234 ? 62.162  -137.298 72.418  1.00 107.69 ? 221 PHE   a CA  1 
ATOM   47655 C  C   . PHE   AA 13 234 ? 60.754  -136.852 71.987  1.00 106.40 ? 221 PHE   a C   1 
ATOM   47656 O  O   . PHE   AA 13 234 ? 60.613  -135.683 71.575  1.00 107.21 ? 221 PHE   a O   1 
ATOM   47657 C  CB  . PHE   AA 13 234 ? 63.079  -137.469 71.201  1.00 106.83 ? 221 PHE   a CB  1 
ATOM   47658 C  CG  . PHE   AA 13 234 ? 62.596  -138.442 70.154  1.00 105.24 ? 221 PHE   a CG  1 
ATOM   47659 C  CD1 . PHE   AA 13 234 ? 62.932  -139.786 70.226  1.00 104.40 ? 221 PHE   a CD1 1 
ATOM   47660 C  CD2 . PHE   AA 13 234 ? 61.819  -138.013 69.088  1.00 103.74 ? 221 PHE   a CD2 1 
ATOM   47661 C  CE1 . PHE   AA 13 234 ? 62.489  -140.681 69.265  1.00 102.80 ? 221 PHE   a CE1 1 
ATOM   47662 C  CE2 . PHE   AA 13 234 ? 61.377  -138.910 68.127  1.00 102.81 ? 221 PHE   a CE2 1 
ATOM   47663 C  CZ  . PHE   AA 13 234 ? 61.713  -140.242 68.217  1.00 101.75 ? 221 PHE   a CZ  1 
ATOM   47664 N  N   . ALA   AA 13 235 ? 59.755  -137.739 72.068  1.00 104.87 ? 222 ALA   a N   1 
ATOM   47665 C  CA  . ALA   AA 13 235 ? 58.354  -137.494 71.648  1.00 104.78 ? 222 ALA   a CA  1 
ATOM   47666 C  C   . ALA   AA 13 235 ? 57.729  -136.336 72.437  1.00 104.77 ? 222 ALA   a C   1 
ATOM   47667 O  O   . ALA   AA 13 235 ? 56.943  -135.586 71.832  1.00 104.85 ? 222 ALA   a O   1 
ATOM   47668 C  CB  . ALA   AA 13 235 ? 57.539  -138.754 71.810  1.00 105.12 ? 222 ALA   a CB  1 
ATOM   47669 N  N   . LYS   AA 13 236 ? 58.043  -136.216 73.733  1.00 106.87 ? 223 LYS   a N   1 
ATOM   47670 C  CA  . LYS   AA 13 236 ? 57.481  -135.189 74.661  1.00 110.55 ? 223 LYS   a CA  1 
ATOM   47671 C  C   . LYS   AA 13 236 ? 57.759  -133.772 74.143  1.00 109.33 ? 223 LYS   a C   1 
ATOM   47672 O  O   . LYS   AA 13 236 ? 56.907  -132.891 74.364  1.00 108.50 ? 223 LYS   a O   1 
ATOM   47673 C  CB  . LYS   AA 13 236 ? 58.074  -135.322 76.069  1.00 113.27 ? 223 LYS   a CB  1 
ATOM   47674 C  CG  . LYS   AA 13 236 ? 59.596  -135.350 76.130  1.00 115.53 ? 223 LYS   a CG  1 
ATOM   47675 C  CD  . LYS   AA 13 236 ? 60.189  -135.126 77.508  1.00 118.41 ? 223 LYS   a CD  1 
ATOM   47676 C  CE  . LYS   AA 13 236 ? 61.695  -135.312 77.565  1.00 122.02 ? 223 LYS   a CE  1 
ATOM   47677 N  NZ  . LYS   AA 13 236 ? 62.210  -136.190 76.486  1.00 123.24 ? 223 LYS   a NZ  1 
ATOM   47678 N  N   . ASP   AA 13 237 ? 58.910  -133.566 73.495  1.00 110.21 ? 224 ASP   a N   1 
ATOM   47679 C  CA  . ASP   AA 13 237 ? 59.418  -132.235 73.066  1.00 113.01 ? 224 ASP   a CA  1 
ATOM   47680 C  C   . ASP   AA 13 237 ? 58.749  -131.800 71.755  1.00 111.61 ? 224 ASP   a C   1 
ATOM   47681 O  O   . ASP   AA 13 237 ? 58.890  -130.617 71.399  1.00 115.65 ? 224 ASP   a O   1 
ATOM   47682 C  CB  . ASP   AA 13 237 ? 60.942  -132.259 72.926  1.00 115.93 ? 224 ASP   a CB  1 
ATOM   47683 C  CG  . ASP   AA 13 237 ? 61.675  -132.585 74.218  1.00 118.92 ? 224 ASP   a CG  1 
ATOM   47684 O  OD1 . ASP   AA 13 237 ? 62.623  -133.399 74.166  1.00 119.31 ? 224 ASP   a OD1 1 
ATOM   47685 O  OD2 . ASP   AA 13 237 ? 61.297  -132.019 75.266  1.00 120.46 ? 224 ASP   a OD2 1 
ATOM   47686 N  N   . ILE   AA 13 238 ? 58.059  -132.712 71.063  1.00 108.33 ? 225 ILE   a N   1 
ATOM   47687 C  CA  . ILE   AA 13 238 ? 57.326  -132.426 69.792  1.00 108.40 ? 225 ILE   a CA  1 
ATOM   47688 C  C   . ILE   AA 13 238 ? 55.909  -131.952 70.138  1.00 109.22 ? 225 ILE   a C   1 
ATOM   47689 O  O   . ILE   AA 13 238 ? 55.138  -132.742 70.716  1.00 105.36 ? 225 ILE   a O   1 
ATOM   47690 C  CB  . ILE   AA 13 238 ? 57.337  -133.654 68.858  1.00 106.75 ? 225 ILE   a CB  1 
ATOM   47691 C  CG1 . ILE   AA 13 238 ? 58.706  -133.815 68.192  1.00 105.58 ? 225 ILE   a CG1 1 
ATOM   47692 C  CG2 . ILE   AA 13 238 ? 56.218  -133.578 67.826  1.00 105.90 ? 225 ILE   a CG2 1 
ATOM   47693 C  CD1 . ILE   AA 13 238 ? 58.960  -135.182 67.622  1.00 103.51 ? 225 ILE   a CD1 1 
ATOM   47694 N  N   . LYS   AA 13 239 ? 55.592  -130.702 69.790  1.00 112.22 ? 226 LYS   a N   1 
ATOM   47695 C  CA  . LYS   AA 13 239 ? 54.273  -130.062 70.033  1.00 116.81 ? 226 LYS   a CA  1 
ATOM   47696 C  C   . LYS   AA 13 239 ? 53.765  -129.449 68.723  1.00 115.11 ? 226 LYS   a C   1 
ATOM   47697 O  O   . LYS   AA 13 239 ? 54.542  -128.727 68.070  1.00 118.52 ? 226 LYS   a O   1 
ATOM   47698 C  CB  . LYS   AA 13 239 ? 54.392  -128.982 71.112  1.00 121.49 ? 226 LYS   a CB  1 
ATOM   47699 C  CG  . LYS   AA 13 239 ? 54.763  -129.478 72.503  1.00 126.49 ? 226 LYS   a CG  1 
ATOM   47700 C  CD  . LYS   AA 13 239 ? 55.444  -128.417 73.345  1.00 131.19 ? 226 LYS   a CD  1 
ATOM   47701 C  CE  . LYS   AA 13 239 ? 55.335  -128.661 74.836  1.00 135.33 ? 226 LYS   a CE  1 
ATOM   47702 N  NZ  . LYS   AA 13 239 ? 55.736  -130.040 75.204  1.00 137.46 ? 226 LYS   a NZ  1 
ATOM   47703 N  N   . GLY   AA 13 240 ? 52.509  -129.734 68.365  1.00 109.14 ? 227 GLY   a N   1 
ATOM   47704 C  CA  . GLY   AA 13 240 ? 51.826  -129.166 67.187  1.00 106.54 ? 227 GLY   a CA  1 
ATOM   47705 C  C   . GLY   AA 13 240 ? 52.355  -129.747 65.890  1.00 100.84 ? 227 GLY   a C   1 
ATOM   47706 O  O   . GLY   AA 13 240 ? 53.202  -130.657 65.951  1.00 98.56  ? 227 GLY   a O   1 
ATOM   47707 N  N   . TYR   AA 13 241 ? 51.887  -129.218 64.755  1.00 101.68 ? 228 TYR   a N   1 
ATOM   47708 C  CA  . TYR   AA 13 241 ? 52.305  -129.637 63.391  1.00 99.57  ? 228 TYR   a CA  1 
ATOM   47709 C  C   . TYR   AA 13 241 ? 53.093  -128.510 62.704  1.00 101.38 ? 228 TYR   a C   1 
ATOM   47710 O  O   . TYR   AA 13 241 ? 53.311  -128.621 61.481  1.00 103.89 ? 228 TYR   a O   1 
ATOM   47711 C  CB  . TYR   AA 13 241 ? 51.095  -130.099 62.571  1.00 96.64  ? 228 TYR   a CB  1 
ATOM   47712 C  CG  . TYR   AA 13 241 ? 49.955  -129.118 62.467  1.00 97.97  ? 228 TYR   a CG  1 
ATOM   47713 C  CD1 . TYR   AA 13 241 ? 50.051  -127.987 61.672  1.00 101.34 ? 228 TYR   a CD1 1 
ATOM   47714 C  CD2 . TYR   AA 13 241 ? 48.768  -129.330 63.148  1.00 98.48  ? 228 TYR   a CD2 1 
ATOM   47715 C  CE1 . TYR   AA 13 241 ? 49.006  -127.082 61.567  1.00 104.79 ? 228 TYR   a CE1 1 
ATOM   47716 C  CE2 . TYR   AA 13 241 ? 47.713  -128.436 63.054  1.00 101.51 ? 228 TYR   a CE2 1 
ATOM   47717 C  CZ  . TYR   AA 13 241 ? 47.831  -127.310 62.261  1.00 103.23 ? 228 TYR   a CZ  1 
ATOM   47718 O  OH  . TYR   AA 13 241 ? 46.781  -126.445 62.178  1.00 106.96 ? 228 TYR   a OH  1 
ATOM   47719 N  N   . GLY   AA 13 242 ? 53.531  -127.483 63.447  1.00 102.28 ? 229 GLY   a N   1 
ATOM   47720 C  CA  . GLY   AA 13 242 ? 54.392  -126.413 62.903  1.00 102.54 ? 229 GLY   a CA  1 
ATOM   47721 C  C   . GLY   AA 13 242 ? 54.518  -125.204 63.816  1.00 104.52 ? 229 GLY   a C   1 
ATOM   47722 O  O   . GLY   AA 13 242 ? 55.624  -124.991 64.350  1.00 105.09 ? 229 GLY   a O   1 
ATOM   47723 N  N   . THR   AA 13 243 ? 53.442  -124.421 63.966  1.00 106.02 ? 230 THR   a N   1 
ATOM   47724 C  CA  . THR   AA 13 243 ? 53.447  -123.075 64.608  1.00 107.35 ? 230 THR   a CA  1 
ATOM   47725 C  C   . THR   AA 13 243 ? 53.043  -123.150 66.085  1.00 109.58 ? 230 THR   a C   1 
ATOM   47726 O  O   . THR   AA 13 243 ? 53.255  -122.141 66.791  1.00 108.62 ? 230 THR   a O   1 
ATOM   47727 C  CB  . THR   AA 13 243 ? 52.501  -122.102 63.894  1.00 105.41 ? 230 THR   a CB  1 
ATOM   47728 O  OG1 . THR   AA 13 243 ? 51.173  -122.619 63.983  1.00 104.77 ? 230 THR   a OG1 1 
ATOM   47729 C  CG2 . THR   AA 13 243 ? 52.874  -121.873 62.446  1.00 104.77 ? 230 THR   a CG2 1 
ATOM   47730 N  N   . GLN   AA 13 244 ? 52.473  -124.272 66.533  1.00 110.37 ? 231 GLN   a N   1 
ATOM   47731 C  CA  . GLN   AA 13 244 ? 51.980  -124.444 67.926  1.00 115.36 ? 231 GLN   a CA  1 
ATOM   47732 C  C   . GLN   AA 13 244 ? 53.172  -124.507 68.890  1.00 118.36 ? 231 GLN   a C   1 
ATOM   47733 O  O   . GLN   AA 13 244 ? 54.158  -125.195 68.560  1.00 118.40 ? 231 GLN   a O   1 
ATOM   47734 C  CB  . GLN   AA 13 244 ? 51.132  -125.707 68.044  1.00 114.54 ? 231 GLN   a CB  1 
ATOM   47735 C  CG  . GLN   AA 13 244 ? 50.330  -125.773 69.332  1.00 117.30 ? 231 GLN   a CG  1 
ATOM   47736 C  CD  . GLN   AA 13 244 ? 49.207  -126.774 69.234  1.00 117.18 ? 231 GLN   a CD  1 
ATOM   47737 O  OE1 . GLN   AA 13 244 ? 48.367  -126.705 68.338  1.00 116.83 ? 231 GLN   a OE1 1 
ATOM   47738 N  NE2 . GLN   AA 13 244 ? 49.181  -127.719 70.160  1.00 117.55 ? 231 GLN   a NE2 1 
ATOM   47739 N  N   . LYS   AA 13 245 ? 53.069  -123.825 70.038  1.00 124.29 ? 232 LYS   a N   1 
ATOM   47740 C  CA  . LYS   AA 13 245 ? 54.165  -123.669 71.037  1.00 127.79 ? 232 LYS   a CA  1 
ATOM   47741 C  C   . LYS   AA 13 245 ? 53.887  -124.503 72.295  1.00 128.94 ? 232 LYS   a C   1 
ATOM   47742 O  O   . LYS   AA 13 245 ? 54.772  -124.540 73.173  1.00 128.87 ? 232 LYS   a O   1 
ATOM   47743 C  CB  . LYS   AA 13 245 ? 54.335  -122.190 71.400  1.00 128.60 ? 232 LYS   a CB  1 
ATOM   47744 C  CG  . LYS   AA 13 245 ? 54.888  -121.324 70.277  1.00 126.01 ? 232 LYS   a CG  1 
ATOM   47745 C  CD  . LYS   AA 13 245 ? 55.212  -119.912 70.695  1.00 124.02 ? 232 LYS   a CD  1 
ATOM   47746 C  CE  . LYS   AA 13 245 ? 55.984  -119.166 69.631  1.00 122.45 ? 232 LYS   a CE  1 
ATOM   47747 N  NZ  . LYS   AA 13 245 ? 56.195  -117.749 70.002  1.00 124.02 ? 232 LYS   a NZ  1 
ATOM   47748 N  N   . ILE   AA 13 246 ? 52.722  -125.151 72.379  1.00 136.75 ? 233 ILE   a N   1 
ATOM   47749 C  CA  . ILE   AA 13 246 ? 52.302  -125.961 73.562  1.00 139.48 ? 233 ILE   a CA  1 
ATOM   47750 C  C   . ILE   AA 13 246 ? 51.469  -127.155 73.078  1.00 141.86 ? 233 ILE   a C   1 
ATOM   47751 O  O   . ILE   AA 13 246 ? 50.571  -127.041 72.246  1.00 145.40 ? 233 ILE   a O   1 
ATOM   47752 C  CB  . ILE   AA 13 246 ? 51.556  -125.085 74.593  1.00 139.93 ? 233 ILE   a CB  1 
ATOM   47753 C  CG1 . ILE   AA 13 246 ? 50.985  -125.920 75.744  1.00 141.48 ? 233 ILE   a CG1 1 
ATOM   47754 C  CG2 . ILE   AA 13 246 ? 50.482  -124.234 73.928  1.00 135.96 ? 233 ILE   a CG2 1 
ATOM   47755 C  CD1 . ILE   AA 13 246 ? 50.828  -125.158 77.039  1.00 142.93 ? 233 ILE   a CD1 1 
ATOM   47756 O  OXT . ILE   AA 13 246 ? 51.699  -128.277 73.522  1.00 143.08 ? 233 ILE   a OXT 1 
ATOM   47757 N  N   . THR   BA 14 1   ? 26.186  -159.970 61.983  1.00 97.07  ? 1   THR   b N   1 
ATOM   47758 C  CA  . THR   BA 14 1   ? 26.314  -161.269 62.715  1.00 94.41  ? 1   THR   b CA  1 
ATOM   47759 C  C   . THR   BA 14 1   ? 27.383  -161.144 63.806  1.00 88.52  ? 1   THR   b C   1 
ATOM   47760 O  O   . THR   BA 14 1   ? 28.494  -160.690 63.481  1.00 86.57  ? 1   THR   b O   1 
ATOM   47761 C  CB  . THR   BA 14 1   ? 26.685  -162.416 61.767  1.00 93.92  ? 1   THR   b CB  1 
ATOM   47762 O  OG1 . THR   BA 14 1   ? 25.644  -162.562 60.800  1.00 98.49  ? 1   THR   b OG1 1 
ATOM   47763 C  CG2 . THR   BA 14 1   ? 26.896  -163.732 62.484  1.00 91.75  ? 1   THR   b CG2 1 
ATOM   47764 N  N   . SER   BA 14 2   ? 27.060  -161.546 65.039  1.00 88.17  ? 2   SER   b N   1 
ATOM   47765 C  CA  . SER   BA 14 2   ? 28.007  -161.626 66.183  1.00 88.61  ? 2   SER   b CA  1 
ATOM   47766 C  C   . SER   BA 14 2   ? 27.996  -163.046 66.759  1.00 86.13  ? 2   SER   b C   1 
ATOM   47767 O  O   . SER   BA 14 2   ? 26.926  -163.498 67.223  1.00 82.92  ? 2   SER   b O   1 
ATOM   47768 C  CB  . SER   BA 14 2   ? 27.689  -160.611 67.245  1.00 88.67  ? 2   SER   b CB  1 
ATOM   47769 O  OG  . SER   BA 14 2   ? 27.462  -159.332 66.679  1.00 90.29  ? 2   SER   b OG  1 
ATOM   47770 N  N   . ILE   BA 14 3   ? 29.153  -163.711 66.725  1.00 84.31  ? 3   ILE   b N   1 
ATOM   47771 C  CA  . ILE   BA 14 3   ? 29.348  -165.113 67.194  1.00 85.56  ? 3   ILE   b CA  1 
ATOM   47772 C  C   . ILE   BA 14 3   ? 30.662  -165.185 67.971  1.00 86.12  ? 3   ILE   b C   1 
ATOM   47773 O  O   . ILE   BA 14 3   ? 31.584  -164.408 67.647  1.00 84.48  ? 3   ILE   b O   1 
ATOM   47774 C  CB  . ILE   BA 14 3   ? 29.341  -166.090 66.003  1.00 83.91  ? 3   ILE   b CB  1 
ATOM   47775 C  CG1 . ILE   BA 14 3   ? 30.465  -165.787 65.007  1.00 82.71  ? 3   ILE   b CG1 1 
ATOM   47776 C  CG2 . ILE   BA 14 3   ? 27.976  -166.100 65.329  1.00 86.78  ? 3   ILE   b CG2 1 
ATOM   47777 C  CD1 . ILE   BA 14 3   ? 30.636  -166.831 63.927  1.00 81.51  ? 3   ILE   b CD1 1 
ATOM   47778 N  N   . MET   BA 14 4   ? 30.745  -166.091 68.946  1.00 88.03  ? 4   MET   b N   1 
ATOM   47779 C  CA  . MET   BA 14 4   ? 31.985  -166.322 69.729  1.00 91.90  ? 4   MET   b CA  1 
ATOM   47780 C  C   . MET   BA 14 4   ? 31.928  -167.679 70.439  1.00 91.63  ? 4   MET   b C   1 
ATOM   47781 O  O   . MET   BA 14 4   ? 30.819  -168.219 70.630  1.00 92.52  ? 4   MET   b O   1 
ATOM   47782 C  CB  . MET   BA 14 4   ? 32.204  -165.198 70.749  1.00 93.16  ? 4   MET   b CB  1 
ATOM   47783 C  CG  . MET   BA 14 4   ? 31.145  -165.114 71.838  1.00 96.77  ? 4   MET   b CG  1 
ATOM   47784 S  SD  . MET   BA 14 4   ? 31.310  -163.619 72.864  1.00 97.31  ? 4   MET   b SD  1 
ATOM   47785 C  CE  . MET   BA 14 4   ? 32.927  -163.881 73.590  1.00 96.32  ? 4   MET   b CE  1 
ATOM   47786 N  N   . ALA   BA 14 5   ? 33.104  -168.203 70.794  1.00 92.56  ? 5   ALA   b N   1 
ATOM   47787 C  CA  . ALA   BA 14 5   ? 33.299  -169.447 71.571  1.00 93.23  ? 5   ALA   b CA  1 
ATOM   47788 C  C   . ALA   BA 14 5   ? 34.340  -169.185 72.664  1.00 92.34  ? 5   ALA   b C   1 
ATOM   47789 O  O   . ALA   BA 14 5   ? 35.392  -168.598 72.341  1.00 90.77  ? 5   ALA   b O   1 
ATOM   47790 C  CB  . ALA   BA 14 5   ? 33.727  -170.562 70.652  1.00 92.90  ? 5   ALA   b CB  1 
ATOM   47791 N  N   . VAL   BA 14 6   ? 34.051  -169.591 73.904  1.00 93.62  ? 6   VAL   b N   1 
ATOM   47792 C  CA  . VAL   BA 14 6   ? 34.942  -169.374 75.083  1.00 93.17  ? 6   VAL   b CA  1 
ATOM   47793 C  C   . VAL   BA 14 6   ? 35.181  -170.713 75.788  1.00 92.00  ? 6   VAL   b C   1 
ATOM   47794 O  O   . VAL   BA 14 6   ? 34.208  -171.468 75.982  1.00 89.01  ? 6   VAL   b O   1 
ATOM   47795 C  CB  . VAL   BA 14 6   ? 34.363  -168.334 76.061  1.00 93.87  ? 6   VAL   b CB  1 
ATOM   47796 C  CG1 . VAL   BA 14 6   ? 35.432  -167.824 77.016  1.00 95.34  ? 6   VAL   b CG1 1 
ATOM   47797 C  CG2 . VAL   BA 14 6   ? 33.694  -167.173 75.340  1.00 93.99  ? 6   VAL   b CG2 1 
ATOM   47798 N  N   . THR   BA 14 7   ? 36.421  -170.971 76.210  1.00 92.38  ? 7   THR   b N   1 
ATOM   47799 C  CA  . THR   BA 14 7   ? 36.789  -172.249 76.873  1.00 94.69  ? 7   THR   b CA  1 
ATOM   47800 C  C   . THR   BA 14 7   ? 37.029  -172.050 78.372  1.00 97.32  ? 7   THR   b C   1 
ATOM   47801 O  O   . THR   BA 14 7   ? 38.014  -171.385 78.707  1.00 102.16 ? 7   THR   b O   1 
ATOM   47802 C  CB  . THR   BA 14 7   ? 38.063  -172.813 76.237  1.00 92.39  ? 7   THR   b CB  1 
ATOM   47803 O  OG1 . THR   BA 14 7   ? 39.212  -172.351 76.945  1.00 89.48  ? 7   THR   b OG1 1 
ATOM   47804 C  CG2 . THR   BA 14 7   ? 38.210  -172.397 74.794  1.00 92.05  ? 7   THR   b CG2 1 
ATOM   47805 N  N   . PHE   BA 14 8   ? 36.210  -172.658 79.234  1.00 96.36  ? 8   PHE   b N   1 
ATOM   47806 C  CA  . PHE   BA 14 8   ? 36.442  -172.506 80.691  1.00 99.67  ? 8   PHE   b CA  1 
ATOM   47807 C  C   . PHE   BA 14 8   ? 36.926  -173.821 81.299  1.00 100.31 ? 8   PHE   b C   1 
ATOM   47808 O  O   . PHE   BA 14 8   ? 37.527  -174.618 80.579  1.00 102.64 ? 8   PHE   b O   1 
ATOM   47809 C  CB  . PHE   BA 14 8   ? 35.196  -171.995 81.407  1.00 101.47 ? 8   PHE   b CB  1 
ATOM   47810 C  CG  . PHE   BA 14 8   ? 33.967  -172.848 81.267  1.00 102.01 ? 8   PHE   b CG  1 
ATOM   47811 C  CD1 . PHE   BA 14 8   ? 33.605  -173.380 80.049  1.00 101.01 ? 8   PHE   b CD1 1 
ATOM   47812 C  CD2 . PHE   BA 14 8   ? 33.163  -173.098 82.363  1.00 102.89 ? 8   PHE   b CD2 1 
ATOM   47813 C  CE1 . PHE   BA 14 8   ? 32.456  -174.140 79.937  1.00 100.93 ? 8   PHE   b CE1 1 
ATOM   47814 C  CE2 . PHE   BA 14 8   ? 32.014  -173.857 82.246  1.00 102.15 ? 8   PHE   b CE2 1 
ATOM   47815 C  CZ  . PHE   BA 14 8   ? 31.667  -174.383 81.031  1.00 102.06 ? 8   PHE   b CZ  1 
ATOM   47816 N  N   . LYS   BA 14 9   ? 36.680  -174.008 82.597  1.00 101.81 ? 9   LYS   b N   1 
ATOM   47817 C  CA  . LYS   BA 14 9   ? 37.095  -175.225 83.340  1.00 104.58 ? 9   LYS   b CA  1 
ATOM   47818 C  C   . LYS   BA 14 9   ? 36.317  -176.438 82.828  1.00 102.83 ? 9   LYS   b C   1 
ATOM   47819 O  O   . LYS   BA 14 9   ? 36.906  -177.253 82.113  1.00 101.12 ? 9   LYS   b O   1 
ATOM   47820 C  CB  . LYS   BA 14 9   ? 36.800  -175.035 84.828  1.00 106.82 ? 9   LYS   b CB  1 
ATOM   47821 C  CG  . LYS   BA 14 9   ? 38.020  -174.879 85.723  1.00 109.77 ? 9   LYS   b CG  1 
ATOM   47822 C  CD  . LYS   BA 14 9   ? 37.657  -174.656 87.174  1.00 115.12 ? 9   LYS   b CD  1 
ATOM   47823 C  CE  . LYS   BA 14 9   ? 38.054  -175.804 88.077  1.00 117.28 ? 9   LYS   b CE  1 
ATOM   47824 N  NZ  . LYS   BA 14 9   ? 36.910  -176.297 88.880  1.00 120.05 ? 9   LYS   b NZ  1 
ATOM   47825 N  N   . ASP   BA 14 10  ? 35.042  -176.533 83.200  1.00 105.66 ? 10  ASP   b N   1 
ATOM   47826 C  CA  . ASP   BA 14 10  ? 34.159  -177.663 82.814  1.00 107.84 ? 10  ASP   b CA  1 
ATOM   47827 C  C   . ASP   BA 14 10  ? 34.290  -178.008 81.331  1.00 107.41 ? 10  ASP   b C   1 
ATOM   47828 O  O   . ASP   BA 14 10  ? 34.449  -179.191 81.032  1.00 108.38 ? 10  ASP   b O   1 
ATOM   47829 C  CB  . ASP   BA 14 10  ? 32.703  -177.376 83.162  1.00 109.69 ? 10  ASP   b CB  1 
ATOM   47830 C  CG  . ASP   BA 14 10  ? 32.531  -177.124 84.641  1.00 115.81 ? 10  ASP   b CG  1 
ATOM   47831 O  OD1 . ASP   BA 14 10  ? 33.557  -177.099 85.335  1.00 120.26 ? 10  ASP   b OD1 1 
ATOM   47832 O  OD2 . ASP   BA 14 10  ? 31.381  -176.958 85.077  1.00 122.04 ? 10  ASP   b OD2 1 
ATOM   47833 N  N   . GLY   BA 14 11  ? 34.201  -177.028 80.435  1.00 103.25 ? 11  GLY   b N   1 
ATOM   47834 C  CA  . GLY   BA 14 11  ? 34.302  -177.371 79.005  1.00 100.28 ? 11  GLY   b CA  1 
ATOM   47835 C  C   . GLY   BA 14 11  ? 34.461  -176.170 78.097  1.00 97.31  ? 11  GLY   b C   1 
ATOM   47836 O  O   . GLY   BA 14 11  ? 35.542  -175.579 78.098  1.00 102.61 ? 11  GLY   b O   1 
ATOM   47837 N  N   . VAL   BA 14 12  ? 33.410  -175.844 77.345  1.00 90.89  ? 12  VAL   b N   1 
ATOM   47838 C  CA  . VAL   BA 14 12  ? 33.437  -174.715 76.375  1.00 88.23  ? 12  VAL   b CA  1 
ATOM   47839 C  C   . VAL   BA 14 12  ? 32.000  -174.256 76.125  1.00 86.02  ? 12  VAL   b C   1 
ATOM   47840 O  O   . VAL   BA 14 12  ? 31.094  -175.069 76.282  1.00 86.41  ? 12  VAL   b O   1 
ATOM   47841 C  CB  . VAL   BA 14 12  ? 34.081  -175.183 75.064  1.00 87.58  ? 12  VAL   b CB  1 
ATOM   47842 C  CG1 . VAL   BA 14 12  ? 33.028  -175.702 74.111  1.00 86.73  ? 12  VAL   b CG1 1 
ATOM   47843 C  CG2 . VAL   BA 14 12  ? 34.898  -174.091 74.408  1.00 88.17  ? 12  VAL   b CG2 1 
ATOM   47844 N  N   . ILE   BA 14 13  ? 31.815  -172.991 75.748  1.00 84.26  ? 13  ILE   b N   1 
ATOM   47845 C  CA  . ILE   BA 14 13  ? 30.461  -172.432 75.457  1.00 84.34  ? 13  ILE   b CA  1 
ATOM   47846 C  C   . ILE   BA 14 13  ? 30.523  -171.657 74.138  1.00 83.29  ? 13  ILE   b C   1 
ATOM   47847 O  O   . ILE   BA 14 13  ? 31.500  -170.912 73.929  1.00 82.50  ? 13  ILE   b O   1 
ATOM   47848 C  CB  . ILE   BA 14 13  ? 29.943  -171.544 76.605  1.00 83.56  ? 13  ILE   b CB  1 
ATOM   47849 C  CG1 . ILE   BA 14 13  ? 30.060  -172.239 77.963  1.00 85.14  ? 13  ILE   b CG1 1 
ATOM   47850 C  CG2 . ILE   BA 14 13  ? 28.518  -171.094 76.319  1.00 84.25  ? 13  ILE   b CG2 1 
ATOM   47851 C  CD1 . ILE   BA 14 13  ? 29.574  -171.416 79.135  1.00 84.82  ? 13  ILE   b CD1 1 
ATOM   47852 N  N   . LEU   BA 14 14  ? 29.498  -171.828 73.302  1.00 85.60  ? 14  LEU   b N   1 
ATOM   47853 C  CA  . LEU   BA 14 14  ? 29.335  -171.138 71.998  1.00 86.96  ? 14  LEU   b CA  1 
ATOM   47854 C  C   . LEU   BA 14 14  ? 28.202  -170.126 72.150  1.00 87.93  ? 14  LEU   b C   1 
ATOM   47855 O  O   . LEU   BA 14 14  ? 27.130  -170.527 72.639  1.00 88.42  ? 14  LEU   b O   1 
ATOM   47856 C  CB  . LEU   BA 14 14  ? 28.999  -172.159 70.908  1.00 87.60  ? 14  LEU   b CB  1 
ATOM   47857 C  CG  . LEU   BA 14 14  ? 30.029  -173.264 70.678  1.00 89.11  ? 14  LEU   b CG  1 
ATOM   47858 C  CD1 . LEU   BA 14 14  ? 29.978  -174.310 71.782  1.00 91.42  ? 14  LEU   b CD1 1 
ATOM   47859 C  CD2 . LEU   BA 14 14  ? 29.806  -173.921 69.325  1.00 89.04  ? 14  LEU   b CD2 1 
ATOM   47860 N  N   . GLY   BA 14 15  ? 28.447  -168.874 71.758  1.00 87.69  ? 15  GLY   b N   1 
ATOM   47861 C  CA  . GLY   BA 14 15  ? 27.457  -167.783 71.795  1.00 85.95  ? 15  GLY   b CA  1 
ATOM   47862 C  C   . GLY   BA 14 15  ? 27.292  -167.154 70.427  1.00 83.43  ? 15  GLY   b C   1 
ATOM   47863 O  O   . GLY   BA 14 15  ? 28.294  -167.069 69.690  1.00 78.64  ? 15  GLY   b O   1 
ATOM   47864 N  N   . ALA   BA 14 16  ? 26.070  -166.731 70.102  1.00 85.94  ? 16  ALA   b N   1 
ATOM   47865 C  CA  . ALA   BA 14 16  ? 25.727  -166.060 68.828  1.00 88.12  ? 16  ALA   b CA  1 
ATOM   47866 C  C   . ALA   BA 14 16  ? 24.466  -165.206 69.005  1.00 87.57  ? 16  ALA   b C   1 
ATOM   47867 O  O   . ALA   BA 14 16  ? 23.716  -165.430 69.974  1.00 87.33  ? 16  ALA   b O   1 
ATOM   47868 C  CB  . ALA   BA 14 16  ? 25.553  -167.098 67.747  1.00 88.16  ? 16  ALA   b CB  1 
ATOM   47869 N  N   . ASP   BA 14 17  ? 24.257  -164.253 68.095  1.00 87.78  ? 17  ASP   b N   1 
ATOM   47870 C  CA  . ASP   BA 14 17  ? 22.990  -163.488 67.962  1.00 90.71  ? 17  ASP   b CA  1 
ATOM   47871 C  C   . ASP   BA 14 17  ? 22.013  -164.345 67.147  1.00 91.90  ? 17  ASP   b C   1 
ATOM   47872 O  O   . ASP   BA 14 17  ? 22.378  -165.494 66.819  1.00 93.01  ? 17  ASP   b O   1 
ATOM   47873 C  CB  . ASP   BA 14 17  ? 23.248  -162.117 67.333  1.00 93.34  ? 17  ASP   b CB  1 
ATOM   47874 C  CG  . ASP   BA 14 17  ? 23.706  -162.182 65.887  1.00 94.64  ? 17  ASP   b CG  1 
ATOM   47875 O  OD1 . ASP   BA 14 17  ? 24.351  -163.186 65.518  1.00 99.03  ? 17  ASP   b OD1 1 
ATOM   47876 O  OD2 . ASP   BA 14 17  ? 23.411  -161.234 65.140  1.00 94.74  ? 17  ASP   b OD2 1 
ATOM   47877 N  N   . SER   BA 14 18  ? 20.828  -163.818 66.826  1.00 89.06  ? 18  SER   b N   1 
ATOM   47878 C  CA  . SER   BA 14 18  ? 19.783  -164.542 66.054  1.00 88.46  ? 18  SER   b CA  1 
ATOM   47879 C  C   . SER   BA 14 18  ? 19.328  -163.736 64.835  1.00 86.36  ? 18  SER   b C   1 
ATOM   47880 O  O   . SER   BA 14 18  ? 18.264  -164.068 64.283  1.00 82.92  ? 18  SER   b O   1 
ATOM   47881 C  CB  . SER   BA 14 18  ? 18.612  -164.881 66.930  1.00 89.64  ? 18  SER   b CB  1 
ATOM   47882 O  OG  . SER   BA 14 18  ? 17.752  -163.763 67.084  1.00 91.51  ? 18  SER   b OG  1 
ATOM   47883 N  N   . ARG   BA 14 19  ? 20.090  -162.723 64.421  1.00 88.95  ? 19  ARG   b N   1 
ATOM   47884 C  CA  . ARG   BA 14 19  ? 19.678  -161.823 63.313  1.00 91.82  ? 19  ARG   b CA  1 
ATOM   47885 C  C   . ARG   BA 14 19  ? 20.453  -162.161 62.038  1.00 88.59  ? 19  ARG   b C   1 
ATOM   47886 O  O   . ARG   BA 14 19  ? 21.695  -162.100 62.055  1.00 88.38  ? 19  ARG   b O   1 
ATOM   47887 C  CB  . ARG   BA 14 19  ? 19.898  -160.352 63.667  1.00 93.66  ? 19  ARG   b CB  1 
ATOM   47888 C  CG  . ARG   BA 14 19  ? 19.813  -159.433 62.458  1.00 94.42  ? 19  ARG   b CG  1 
ATOM   47889 C  CD  . ARG   BA 14 19  ? 19.894  -157.977 62.846  1.00 93.87  ? 19  ARG   b CD  1 
ATOM   47890 N  NE  . ARG   BA 14 19  ? 18.768  -157.557 63.667  1.00 94.85  ? 19  ARG   b NE  1 
ATOM   47891 C  CZ  . ARG   BA 14 19  ? 18.653  -156.354 64.216  1.00 94.72  ? 19  ARG   b CZ  1 
ATOM   47892 N  NH1 . ARG   BA 14 19  ? 19.599  -155.448 64.033  1.00 95.90  ? 19  ARG   b NH1 1 
ATOM   47893 N  NH2 . ARG   BA 14 19  ? 17.589  -156.059 64.942  1.00 95.69  ? 19  ARG   b NH2 1 
ATOM   47894 N  N   . THR   BA 14 20  ? 19.718  -162.459 60.970  1.00 86.72  ? 20  THR   b N   1 
ATOM   47895 C  CA  . THR   BA 14 20  ? 20.227  -162.605 59.583  1.00 86.40  ? 20  THR   b CA  1 
ATOM   47896 C  C   . THR   BA 14 20  ? 19.525  -161.536 58.739  1.00 86.41  ? 20  THR   b C   1 
ATOM   47897 O  O   . THR   BA 14 20  ? 18.282  -161.449 58.832  1.00 85.85  ? 20  THR   b O   1 
ATOM   47898 C  CB  . THR   BA 14 20  ? 19.992  -164.035 59.080  1.00 86.89  ? 20  THR   b CB  1 
ATOM   47899 O  OG1 . THR   BA 14 20  ? 20.727  -164.211 57.869  1.00 83.09  ? 20  THR   b OG1 1 
ATOM   47900 C  CG2 . THR   BA 14 20  ? 18.526  -164.332 58.854  1.00 89.45  ? 20  THR   b CG2 1 
ATOM   47901 N  N   . THR   BA 14 21  ? 20.274  -160.723 57.988  1.00 84.20  ? 21  THR   b N   1 
ATOM   47902 C  CA  . THR   BA 14 21  ? 19.713  -159.572 57.230  1.00 85.63  ? 21  THR   b CA  1 
ATOM   47903 C  C   . THR   BA 14 21  ? 20.096  -159.630 55.751  1.00 83.89  ? 21  THR   b C   1 
ATOM   47904 O  O   . THR   BA 14 21  ? 21.188  -160.133 55.434  1.00 85.39  ? 21  THR   b O   1 
ATOM   47905 C  CB  . THR   BA 14 21  ? 20.183  -158.223 57.786  1.00 84.32  ? 21  THR   b CB  1 
ATOM   47906 O  OG1 . THR   BA 14 21  ? 21.600  -158.141 57.630  1.00 81.47  ? 21  THR   b OG1 1 
ATOM   47907 C  CG2 . THR   BA 14 21  ? 19.804  -158.021 59.235  1.00 85.48  ? 21  THR   b CG2 1 
ATOM   47908 N  N   . THR   BA 14 22  ? 19.211  -159.094 54.907  1.00 86.11  ? 22  THR   b N   1 
ATOM   47909 C  CA  . THR   BA 14 22  ? 19.430  -158.775 53.473  1.00 89.71  ? 22  THR   b CA  1 
ATOM   47910 C  C   . THR   BA 14 22  ? 19.462  -157.252 53.315  1.00 91.15  ? 22  THR   b C   1 
ATOM   47911 O  O   . THR   BA 14 22  ? 18.388  -156.633 53.460  1.00 94.58  ? 22  THR   b O   1 
ATOM   47912 C  CB  . THR   BA 14 22  ? 18.299  -159.339 52.605  1.00 89.51  ? 22  THR   b CB  1 
ATOM   47913 O  OG1 . THR   BA 14 22  ? 18.156  -160.728 52.893  1.00 91.03  ? 22  THR   b OG1 1 
ATOM   47914 C  CG2 . THR   BA 14 22  ? 18.544  -159.141 51.126  1.00 90.86  ? 22  THR   b CG2 1 
ATOM   47915 N  N   . GLY   BA 14 23  ? 20.628  -156.670 53.024  1.00 92.45  ? 23  GLY   b N   1 
ATOM   47916 C  CA  . GLY   BA 14 23  ? 20.814  -155.208 53.076  1.00 91.22  ? 23  GLY   b CA  1 
ATOM   47917 C  C   . GLY   BA 14 23  ? 20.517  -154.690 54.474  1.00 91.36  ? 23  GLY   b C   1 
ATOM   47918 O  O   . GLY   BA 14 23  ? 21.237  -155.091 55.408  1.00 91.88  ? 23  GLY   b O   1 
ATOM   47919 N  N   . ALA   BA 14 24  ? 19.469  -153.872 54.623  1.00 91.80  ? 24  ALA   b N   1 
ATOM   47920 C  CA  . ALA   BA 14 24  ? 19.013  -153.296 55.911  1.00 91.87  ? 24  ALA   b CA  1 
ATOM   47921 C  C   . ALA   BA 14 24  ? 17.685  -153.928 56.350  1.00 90.21  ? 24  ALA   b C   1 
ATOM   47922 O  O   . ALA   BA 14 24  ? 17.123  -153.466 57.364  1.00 87.50  ? 24  ALA   b O   1 
ATOM   47923 C  CB  . ALA   BA 14 24  ? 18.884  -151.800 55.781  1.00 92.54  ? 24  ALA   b CB  1 
ATOM   47924 N  N   . TYR   BA 14 25  ? 17.196  -154.937 55.620  1.00 90.70  ? 25  TYR   b N   1 
ATOM   47925 C  CA  . TYR   BA 14 25  ? 15.984  -155.722 55.974  1.00 91.10  ? 25  TYR   b CA  1 
ATOM   47926 C  C   . TYR   BA 14 25  ? 16.418  -156.966 56.751  1.00 91.95  ? 25  TYR   b C   1 
ATOM   47927 O  O   . TYR   BA 14 25  ? 17.409  -157.601 56.348  1.00 94.26  ? 25  TYR   b O   1 
ATOM   47928 C  CB  . TYR   BA 14 25  ? 15.188  -156.119 54.728  1.00 90.23  ? 25  TYR   b CB  1 
ATOM   47929 C  CG  . TYR   BA 14 25  ? 13.971  -156.956 55.026  1.00 89.37  ? 25  TYR   b CG  1 
ATOM   47930 C  CD1 . TYR   BA 14 25  ? 12.932  -156.448 55.791  1.00 90.55  ? 25  TYR   b CD1 1 
ATOM   47931 C  CD2 . TYR   BA 14 25  ? 13.862  -158.260 54.572  1.00 89.23  ? 25  TYR   b CD2 1 
ATOM   47932 C  CE1 . TYR   BA 14 25  ? 11.812  -157.207 56.084  1.00 90.53  ? 25  TYR   b CE1 1 
ATOM   47933 C  CE2 . TYR   BA 14 25  ? 12.748  -159.034 54.858  1.00 89.74  ? 25  TYR   b CE2 1 
ATOM   47934 C  CZ  . TYR   BA 14 25  ? 11.718  -158.506 55.617  1.00 90.30  ? 25  TYR   b CZ  1 
ATOM   47935 O  OH  . TYR   BA 14 25  ? 10.613  -159.252 55.909  1.00 89.28  ? 25  TYR   b OH  1 
ATOM   47936 N  N   . ILE   BA 14 26  ? 15.695  -157.299 57.823  1.00 93.12  ? 26  ILE   b N   1 
ATOM   47937 C  CA  . ILE   BA 14 26  ? 15.909  -158.540 58.625  1.00 94.38  ? 26  ILE   b CA  1 
ATOM   47938 C  C   . ILE   BA 14 26  ? 15.029  -159.650 58.037  1.00 96.32  ? 26  ILE   b C   1 
ATOM   47939 O  O   . ILE   BA 14 26  ? 13.797  -159.602 58.249  1.00 94.31  ? 26  ILE   b O   1 
ATOM   47940 C  CB  . ILE   BA 14 26  ? 15.619  -158.291 60.119  1.00 94.46  ? 26  ILE   b CB  1 
ATOM   47941 C  CG1 . ILE   BA 14 26  ? 16.448  -157.126 60.670  1.00 92.53  ? 26  ILE   b CG1 1 
ATOM   47942 C  CG2 . ILE   BA 14 26  ? 15.830  -159.567 60.925  1.00 96.34  ? 26  ILE   b CG2 1 
ATOM   47943 C  CD1 . ILE   BA 14 26  ? 16.070  -156.702 62.069  1.00 92.81  ? 26  ILE   b CD1 1 
ATOM   47944 N  N   . ALA   BA 14 27  ? 15.641  -160.601 57.318  1.00 98.54  ? 27  ALA   b N   1 
ATOM   47945 C  CA  . ALA   BA 14 27  ? 14.973  -161.777 56.709  1.00 98.81  ? 27  ALA   b CA  1 
ATOM   47946 C  C   . ALA   BA 14 27  ? 14.448  -162.694 57.818  1.00 97.08  ? 27  ALA   b C   1 
ATOM   47947 O  O   . ALA   BA 14 27  ? 13.263  -163.076 57.761  1.00 97.19  ? 27  ALA   b O   1 
ATOM   47948 C  CB  . ALA   BA 14 27  ? 15.926  -162.514 55.798  1.00 100.76 ? 27  ALA   b CB  1 
ATOM   47949 N  N   . ASN   BA 14 28  ? 15.306  -163.017 58.789  1.00 93.94  ? 28  ASN   b N   1 
ATOM   47950 C  CA  . ASN   BA 14 28  ? 14.976  -163.852 59.974  1.00 94.32  ? 28  ASN   b CA  1 
ATOM   47951 C  C   . ASN   BA 14 28  ? 15.514  -163.153 61.229  1.00 91.31  ? 28  ASN   b C   1 
ATOM   47952 O  O   . ASN   BA 14 28  ? 16.695  -162.739 61.220  1.00 86.77  ? 28  ASN   b O   1 
ATOM   47953 C  CB  . ASN   BA 14 28  ? 15.535  -165.273 59.836  1.00 93.98  ? 28  ASN   b CB  1 
ATOM   47954 C  CG  . ASN   BA 14 28  ? 14.816  -166.288 60.695  1.00 94.21  ? 28  ASN   b CG  1 
ATOM   47955 O  OD1 . ASN   BA 14 28  ? 13.650  -166.105 61.037  1.00 96.87  ? 28  ASN   b OD1 1 
ATOM   47956 N  ND2 . ASN   BA 14 28  ? 15.503  -167.363 61.043  1.00 96.45  ? 28  ASN   b ND2 1 
ATOM   47957 N  N   . ARG   BA 14 29  ? 14.682  -163.022 62.265  1.00 89.29  ? 29  ARG   b N   1 
ATOM   47958 C  CA  . ARG   BA 14 29  ? 15.073  -162.375 63.546  1.00 91.42  ? 29  ARG   b CA  1 
ATOM   47959 C  C   . ARG   BA 14 29  ? 15.280  -163.429 64.643  1.00 92.48  ? 29  ARG   b C   1 
ATOM   47960 O  O   . ARG   BA 14 29  ? 15.582  -163.025 65.782  1.00 96.56  ? 29  ARG   b O   1 
ATOM   47961 C  CB  . ARG   BA 14 29  ? 14.041  -161.322 63.960  1.00 89.69  ? 29  ARG   b CB  1 
ATOM   47962 C  CG  . ARG   BA 14 29  ? 12.643  -161.851 64.241  1.00 91.10  ? 29  ARG   b CG  1 
ATOM   47963 C  CD  . ARG   BA 14 29  ? 11.764  -160.686 64.654  1.00 90.52  ? 29  ARG   b CD  1 
ATOM   47964 N  NE  . ARG   BA 14 29  ? 10.408  -161.080 65.006  1.00 90.98  ? 29  ARG   b NE  1 
ATOM   47965 C  CZ  . ARG   BA 14 29  ? 9.943   -161.192 66.246  1.00 92.89  ? 29  ARG   b CZ  1 
ATOM   47966 N  NH1 . ARG   BA 14 29  ? 10.725  -160.938 67.283  1.00 93.62  ? 29  ARG   b NH1 1 
ATOM   47967 N  NH2 . ARG   BA 14 29  ? 8.691   -161.559 66.446  1.00 95.39  ? 29  ARG   b NH2 1 
ATOM   47968 N  N   . VAL   BA 14 30  ? 15.158  -164.722 64.319  1.00 91.46  ? 30  VAL   b N   1 
ATOM   47969 C  CA  . VAL   BA 14 30  ? 15.281  -165.839 65.304  1.00 91.24  ? 30  VAL   b CA  1 
ATOM   47970 C  C   . VAL   BA 14 30  ? 16.168  -166.947 64.718  1.00 91.39  ? 30  VAL   b C   1 
ATOM   47971 O  O   . VAL   BA 14 30  ? 15.893  -168.130 64.989  1.00 91.90  ? 30  VAL   b O   1 
ATOM   47972 C  CB  . VAL   BA 14 30  ? 13.889  -166.363 65.711  1.00 90.26  ? 30  VAL   b CB  1 
ATOM   47973 C  CG1 . VAL   BA 14 30  ? 13.095  -165.317 66.476  1.00 91.35  ? 30  VAL   b CG1 1 
ATOM   47974 C  CG2 . VAL   BA 14 30  ? 13.090  -166.857 64.514  1.00 90.81  ? 30  VAL   b CG2 1 
ATOM   47975 N  N   . THR   BA 14 31  ? 17.217  -166.579 63.976  1.00 90.78  ? 31  THR   b N   1 
ATOM   47976 C  CA  . THR   BA 14 31  ? 18.165  -167.527 63.327  1.00 94.02  ? 31  THR   b CA  1 
ATOM   47977 C  C   . THR   BA 14 31  ? 18.924  -168.321 64.399  1.00 97.46  ? 31  THR   b C   1 
ATOM   47978 O  O   . THR   BA 14 31  ? 19.255  -167.738 65.453  1.00 99.68  ? 31  THR   b O   1 
ATOM   47979 C  CB  . THR   BA 14 31  ? 19.151  -166.802 62.400  1.00 91.25  ? 31  THR   b CB  1 
ATOM   47980 O  OG1 . THR   BA 14 31  ? 18.422  -165.851 61.626  1.00 94.69  ? 31  THR   b OG1 1 
ATOM   47981 C  CG2 . THR   BA 14 31  ? 19.880  -167.736 61.460  1.00 91.27  ? 31  THR   b CG2 1 
ATOM   47982 N  N   . ASP   BA 14 32  ? 19.188  -169.605 64.133  1.00 99.48  ? 32  ASP   b N   1 
ATOM   47983 C  CA  . ASP   BA 14 32  ? 20.067  -170.464 64.970  1.00 102.59 ? 32  ASP   b CA  1 
ATOM   47984 C  C   . ASP   BA 14 32  ? 21.410  -170.621 64.249  1.00 100.58 ? 32  ASP   b C   1 
ATOM   47985 O  O   . ASP   BA 14 32  ? 21.500  -171.469 63.341  1.00 107.18 ? 32  ASP   b O   1 
ATOM   47986 C  CB  . ASP   BA 14 32  ? 19.413  -171.814 65.271  1.00 105.16 ? 32  ASP   b CB  1 
ATOM   47987 C  CG  . ASP   BA 14 32  ? 20.216  -172.683 66.227  1.00 108.58 ? 32  ASP   b CG  1 
ATOM   47988 O  OD1 . ASP   BA 14 32  ? 21.100  -172.141 66.926  1.00 106.07 ? 32  ASP   b OD1 1 
ATOM   47989 O  OD2 . ASP   BA 14 32  ? 19.954  -173.901 66.263  1.00 112.25 ? 32  ASP   b OD2 1 
ATOM   47990 N  N   . LYS   BA 14 33  ? 22.408  -169.826 64.645  1.00 99.17  ? 33  LYS   b N   1 
ATOM   47991 C  CA  . LYS   BA 14 33  ? 23.744  -169.755 63.994  1.00 95.50  ? 33  LYS   b CA  1 
ATOM   47992 C  C   . LYS   BA 14 33  ? 24.721  -170.703 64.697  1.00 92.59  ? 33  LYS   b C   1 
ATOM   47993 O  O   . LYS   BA 14 33  ? 25.904  -170.729 64.298  1.00 90.41  ? 33  LYS   b O   1 
ATOM   47994 C  CB  . LYS   BA 14 33  ? 24.257  -168.314 64.023  1.00 94.49  ? 33  LYS   b CB  1 
ATOM   47995 C  CG  . LYS   BA 14 33  ? 23.330  -167.304 63.367  1.00 94.40  ? 33  LYS   b CG  1 
ATOM   47996 C  CD  . LYS   BA 14 33  ? 23.786  -165.879 63.526  1.00 93.60  ? 33  LYS   b CD  1 
ATOM   47997 C  CE  . LYS   BA 14 33  ? 23.027  -164.935 62.621  1.00 94.49  ? 33  LYS   b CE  1 
ATOM   47998 N  NZ  . LYS   BA 14 33  ? 23.503  -163.542 62.767  1.00 93.93  ? 33  LYS   b NZ  1 
ATOM   47999 N  N   . LEU   BA 14 34  ? 24.242  -171.430 65.712  1.00 93.36  ? 34  LEU   b N   1 
ATOM   48000 C  CA  . LEU   BA 14 34  ? 24.965  -172.545 66.374  1.00 95.93  ? 34  LEU   b CA  1 
ATOM   48001 C  C   . LEU   BA 14 34  ? 24.475  -173.848 65.743  1.00 96.27  ? 34  LEU   b C   1 
ATOM   48002 O  O   . LEU   BA 14 34  ? 23.255  -174.109 65.811  1.00 99.09  ? 34  LEU   b O   1 
ATOM   48003 C  CB  . LEU   BA 14 34  ? 24.678  -172.516 67.878  1.00 95.97  ? 34  LEU   b CB  1 
ATOM   48004 C  CG  . LEU   BA 14 34  ? 24.882  -171.161 68.552  1.00 95.50  ? 34  LEU   b CG  1 
ATOM   48005 C  CD1 . LEU   BA 14 34  ? 24.290  -171.155 69.951  1.00 97.57  ? 34  LEU   b CD1 1 
ATOM   48006 C  CD2 . LEU   BA 14 34  ? 26.356  -170.794 68.589  1.00 96.99  ? 34  LEU   b CD2 1 
ATOM   48007 N  N   . THR   BA 14 35  ? 25.375  -174.612 65.123  1.00 96.06  ? 35  THR   b N   1 
ATOM   48008 C  CA  . THR   BA 14 35  ? 25.026  -175.863 64.403  1.00 94.64  ? 35  THR   b CA  1 
ATOM   48009 C  C   . THR   BA 14 35  ? 25.840  -177.036 64.944  1.00 93.55  ? 35  THR   b C   1 
ATOM   48010 O  O   . THR   BA 14 35  ? 27.012  -176.837 65.317  1.00 87.38  ? 35  THR   b O   1 
ATOM   48011 C  CB  . THR   BA 14 35  ? 25.210  -175.705 62.892  1.00 97.10  ? 35  THR   b CB  1 
ATOM   48012 O  OG1 . THR   BA 14 35  ? 26.538  -175.253 62.628  1.00 99.40  ? 35  THR   b OG1 1 
ATOM   48013 C  CG2 . THR   BA 14 35  ? 24.213  -174.728 62.318  1.00 94.55  ? 35  THR   b CG2 1 
ATOM   48014 N  N   . ARG   BA 14 36  ? 25.208  -178.208 64.957  1.00 93.49  ? 36  ARG   b N   1 
ATOM   48015 C  CA  . ARG   BA 14 36  ? 25.766  -179.481 65.466  1.00 96.50  ? 36  ARG   b CA  1 
ATOM   48016 C  C   . ARG   BA 14 36  ? 26.383  -180.233 64.288  1.00 94.78  ? 36  ARG   b C   1 
ATOM   48017 O  O   . ARG   BA 14 36  ? 25.662  -180.462 63.299  1.00 94.97  ? 36  ARG   b O   1 
ATOM   48018 C  CB  . ARG   BA 14 36  ? 24.649  -180.310 66.103  1.00 101.95 ? 36  ARG   b CB  1 
ATOM   48019 C  CG  . ARG   BA 14 36  ? 25.138  -181.572 66.794  1.00 107.05 ? 36  ARG   b CG  1 
ATOM   48020 C  CD  . ARG   BA 14 36  ? 24.082  -182.656 66.827  1.00 114.19 ? 36  ARG   b CD  1 
ATOM   48021 N  NE  . ARG   BA 14 36  ? 24.323  -183.622 65.763  1.00 116.31 ? 36  ARG   b NE  1 
ATOM   48022 C  CZ  . ARG   BA 14 36  ? 24.706  -184.884 65.946  1.00 117.66 ? 36  ARG   b CZ  1 
ATOM   48023 N  NH1 . ARG   BA 14 36  ? 24.871  -185.369 67.167  1.00 119.50 ? 36  ARG   b NH1 1 
ATOM   48024 N  NH2 . ARG   BA 14 36  ? 24.909  -185.667 64.900  1.00 117.99 ? 36  ARG   b NH2 1 
ATOM   48025 N  N   . VAL   BA 14 37  ? 27.667  -180.581 64.383  1.00 92.84  ? 37  VAL   b N   1 
ATOM   48026 C  CA  . VAL   BA 14 37  ? 28.357  -181.468 63.399  1.00 94.42  ? 37  VAL   b CA  1 
ATOM   48027 C  C   . VAL   BA 14 37  ? 28.606  -182.839 64.050  1.00 96.70  ? 37  VAL   b C   1 
ATOM   48028 O  O   . VAL   BA 14 37  ? 28.842  -183.812 63.306  1.00 94.52  ? 37  VAL   b O   1 
ATOM   48029 C  CB  . VAL   BA 14 37  ? 29.649  -180.813 62.871  1.00 92.67  ? 37  VAL   b CB  1 
ATOM   48030 C  CG1 . VAL   BA 14 37  ? 29.384  -179.401 62.373  1.00 91.06  ? 37  VAL   b CG1 1 
ATOM   48031 C  CG2 . VAL   BA 14 37  ? 30.768  -180.806 63.901  1.00 93.43  ? 37  VAL   b CG2 1 
ATOM   48032 N  N   . HIS   BA 14 38  ? 28.543  -182.909 65.385  1.00 95.88  ? 38  HIS   b N   1 
ATOM   48033 C  CA  . HIS   BA 14 38  ? 28.686  -184.151 66.191  1.00 97.53  ? 38  HIS   b CA  1 
ATOM   48034 C  C   . HIS   BA 14 38  ? 28.084  -183.923 67.584  1.00 98.51  ? 38  HIS   b C   1 
ATOM   48035 O  O   . HIS   BA 14 38  ? 27.748  -182.768 67.893  1.00 102.23 ? 38  HIS   b O   1 
ATOM   48036 C  CB  . HIS   BA 14 38  ? 30.158  -184.585 66.245  1.00 99.66  ? 38  HIS   b CB  1 
ATOM   48037 C  CG  . HIS   BA 14 38  ? 30.336  -186.049 66.475  1.00 98.62  ? 38  HIS   b CG  1 
ATOM   48038 N  ND1 . HIS   BA 14 38  ? 29.828  -186.996 65.608  1.00 97.76  ? 38  HIS   b ND1 1 
ATOM   48039 C  CD2 . HIS   BA 14 38  ? 30.952  -186.732 67.464  1.00 100.20 ? 38  HIS   b CD2 1 
ATOM   48040 C  CE1 . HIS   BA 14 38  ? 30.122  -188.199 66.051  1.00 97.31  ? 38  HIS   b CE1 1 
ATOM   48041 N  NE2 . HIS   BA 14 38  ? 30.815  -188.066 67.185  1.00 97.18  ? 38  HIS   b NE2 1 
ATOM   48042 N  N   . ASP   BA 14 39  ? 27.959  -184.981 68.391  1.00 99.49  ? 39  ASP   b N   1 
ATOM   48043 C  CA  . ASP   BA 14 39  ? 27.291  -184.937 69.721  1.00 100.49 ? 39  ASP   b CA  1 
ATOM   48044 C  C   . ASP   BA 14 39  ? 27.869  -183.781 70.545  1.00 96.69  ? 39  ASP   b C   1 
ATOM   48045 O  O   . ASP   BA 14 39  ? 27.070  -182.987 71.085  1.00 90.93  ? 39  ASP   b O   1 
ATOM   48046 C  CB  . ASP   BA 14 39  ? 27.417  -186.270 70.462  1.00 104.33 ? 39  ASP   b CB  1 
ATOM   48047 C  CG  . ASP   BA 14 39  ? 26.808  -187.444 69.714  1.00 107.80 ? 39  ASP   b CG  1 
ATOM   48048 O  OD1 . ASP   BA 14 39  ? 26.386  -188.408 70.383  1.00 115.87 ? 39  ASP   b OD1 1 
ATOM   48049 O  OD2 . ASP   BA 14 39  ? 26.762  -187.384 68.466  1.00 109.42 ? 39  ASP   b OD2 1 
ATOM   48050 N  N   . LYS   BA 14 40  ? 29.201  -183.683 70.618  1.00 94.62  ? 40  LYS   b N   1 
ATOM   48051 C  CA  . LYS   BA 14 40  ? 29.915  -182.668 71.439  1.00 93.26  ? 40  LYS   b CA  1 
ATOM   48052 C  C   . LYS   BA 14 40  ? 30.913  -181.875 70.585  1.00 87.94  ? 40  LYS   b C   1 
ATOM   48053 O  O   . LYS   BA 14 40  ? 31.870  -181.340 71.171  1.00 89.61  ? 40  LYS   b O   1 
ATOM   48054 C  CB  . LYS   BA 14 40  ? 30.591  -183.347 72.634  1.00 93.67  ? 40  LYS   b CB  1 
ATOM   48055 C  CG  . LYS   BA 14 40  ? 29.790  -183.253 73.922  1.00 97.02  ? 40  LYS   b CG  1 
ATOM   48056 C  CD  . LYS   BA 14 40  ? 30.080  -184.341 74.922  1.00 99.09  ? 40  LYS   b CD  1 
ATOM   48057 C  CE  . LYS   BA 14 40  ? 29.170  -184.238 76.125  1.00 102.40 ? 40  LYS   b CE  1 
ATOM   48058 N  NZ  . LYS   BA 14 40  ? 29.142  -185.493 76.911  1.00 105.87 ? 40  LYS   b NZ  1 
ATOM   48059 N  N   . ILE   BA 14 41  ? 30.694  -181.783 69.268  1.00 86.82  ? 41  ILE   b N   1 
ATOM   48060 C  CA  . ILE   BA 14 41  ? 31.406  -180.818 68.373  1.00 86.72  ? 41  ILE   b CA  1 
ATOM   48061 C  C   . ILE   BA 14 41  ? 30.359  -179.957 67.658  1.00 83.41  ? 41  ILE   b C   1 
ATOM   48062 O  O   . ILE   BA 14 41  ? 29.570  -180.499 66.863  1.00 80.91  ? 41  ILE   b O   1 
ATOM   48063 C  CB  . ILE   BA 14 41  ? 32.351  -181.519 67.374  1.00 87.64  ? 41  ILE   b CB  1 
ATOM   48064 C  CG1 . ILE   BA 14 41  ? 33.376  -182.410 68.082  1.00 90.19  ? 41  ILE   b CG1 1 
ATOM   48065 C  CG2 . ILE   BA 14 41  ? 33.032  -180.489 66.482  1.00 86.71  ? 41  ILE   b CG2 1 
ATOM   48066 C  CD1 . ILE   BA 14 41  ? 34.171  -183.301 67.152  1.00 90.80  ? 41  ILE   b CD1 1 
ATOM   48067 N  N   . TRP   BA 14 42  ? 30.363  -178.656 67.944  1.00 82.02  ? 42  TRP   b N   1 
ATOM   48068 C  CA  . TRP   BA 14 42  ? 29.453  -177.648 67.342  1.00 82.91  ? 42  TRP   b CA  1 
ATOM   48069 C  C   . TRP   BA 14 42  ? 30.293  -176.573 66.642  1.00 82.41  ? 42  TRP   b C   1 
ATOM   48070 O  O   . TRP   BA 14 42  ? 31.514  -176.504 66.906  1.00 78.85  ? 42  TRP   b O   1 
ATOM   48071 C  CB  . TRP   BA 14 42  ? 28.541  -177.047 68.417  1.00 82.44  ? 42  TRP   b CB  1 
ATOM   48072 C  CG  . TRP   BA 14 42  ? 27.514  -177.987 68.968  1.00 82.09  ? 42  TRP   b CG  1 
ATOM   48073 C  CD1 . TRP   BA 14 42  ? 27.731  -179.162 69.624  1.00 84.05  ? 42  TRP   b CD1 1 
ATOM   48074 C  CD2 . TRP   BA 14 42  ? 26.090  -177.798 68.955  1.00 82.45  ? 42  TRP   b CD2 1 
ATOM   48075 N  NE1 . TRP   BA 14 42  ? 26.541  -179.723 70.001  1.00 85.15  ? 42  TRP   b NE1 1 
ATOM   48076 C  CE2 . TRP   BA 14 42  ? 25.516  -178.910 69.604  1.00 83.26  ? 42  TRP   b CE2 1 
ATOM   48077 C  CE3 . TRP   BA 14 42  ? 25.246  -176.802 68.455  1.00 85.05  ? 42  TRP   b CE3 1 
ATOM   48078 C  CZ2 . TRP   BA 14 42  ? 24.139  -179.054 69.762  1.00 85.02  ? 42  TRP   b CZ2 1 
ATOM   48079 C  CZ3 . TRP   BA 14 42  ? 23.885  -176.946 68.608  1.00 87.03  ? 42  TRP   b CZ3 1 
ATOM   48080 C  CH2 . TRP   BA 14 42  ? 23.341  -178.056 69.254  1.00 86.33  ? 42  TRP   b CH2 1 
ATOM   48081 N  N   . CYS   BA 14 43  ? 29.670  -175.771 65.777  1.00 84.87  ? 43  CYS   b N   1 
ATOM   48082 C  CA  . CYS   BA 14 43  ? 30.338  -174.649 65.068  1.00 88.63  ? 43  CYS   b CA  1 
ATOM   48083 C  C   . CYS   BA 14 43  ? 29.451  -173.398 65.077  1.00 88.72  ? 43  CYS   b C   1 
ATOM   48084 O  O   . CYS   BA 14 43  ? 28.220  -173.525 65.242  1.00 87.30  ? 43  CYS   b O   1 
ATOM   48085 C  CB  . CYS   BA 14 43  ? 30.716  -175.034 63.641  1.00 90.39  ? 43  CYS   b CB  1 
ATOM   48086 S  SG  . CYS   BA 14 43  ? 29.314  -175.131 62.494  1.00 92.99  ? 43  CYS   b SG  1 
ATOM   48087 N  N   . CYS   BA 14 44  ? 30.082  -172.233 64.920  1.00 89.34  ? 44  CYS   b N   1 
ATOM   48088 C  CA  . CYS   BA 14 44  ? 29.432  -170.904 64.794  1.00 90.20  ? 44  CYS   b CA  1 
ATOM   48089 C  C   . CYS   BA 14 44  ? 29.616  -170.397 63.362  1.00 86.33  ? 44  CYS   b C   1 
ATOM   48090 O  O   . CYS   BA 14 44  ? 30.779  -170.280 62.927  1.00 84.07  ? 44  CYS   b O   1 
ATOM   48091 C  CB  . CYS   BA 14 44  ? 30.040  -169.907 65.769  1.00 91.56  ? 44  CYS   b CB  1 
ATOM   48092 S  SG  . CYS   BA 14 44  ? 29.951  -170.449 67.494  1.00 100.03 ? 44  CYS   b SG  1 
ATOM   48093 N  N   . ARG   BA 14 45  ? 28.514  -170.106 62.667  1.00 85.53  ? 45  ARG   b N   1 
ATOM   48094 C  CA  . ARG   BA 14 45  ? 28.528  -169.759 61.224  1.00 87.11  ? 45  ARG   b CA  1 
ATOM   48095 C  C   . ARG   BA 14 45  ? 28.418  -168.243 61.050  1.00 83.98  ? 45  ARG   b C   1 
ATOM   48096 O  O   . ARG   BA 14 45  ? 27.461  -167.645 61.584  1.00 83.73  ? 45  ARG   b O   1 
ATOM   48097 C  CB  . ARG   BA 14 45  ? 27.388  -170.464 60.490  1.00 90.70  ? 45  ARG   b CB  1 
ATOM   48098 C  CG  . ARG   BA 14 45  ? 27.512  -171.980 60.466  1.00 91.35  ? 45  ARG   b CG  1 
ATOM   48099 C  CD  . ARG   BA 14 45  ? 26.376  -172.607 59.685  1.00 91.70  ? 45  ARG   b CD  1 
ATOM   48100 N  NE  . ARG   BA 14 45  ? 25.089  -172.359 60.322  1.00 91.03  ? 45  ARG   b NE  1 
ATOM   48101 C  CZ  . ARG   BA 14 45  ? 24.180  -171.469 59.930  1.00 87.35  ? 45  ARG   b CZ  1 
ATOM   48102 N  NH1 . ARG   BA 14 45  ? 24.388  -170.708 58.867  1.00 86.49  ? 45  ARG   b NH1 1 
ATOM   48103 N  NH2 . ARG   BA 14 45  ? 23.054  -171.347 60.611  1.00 88.44  ? 45  ARG   b NH2 1 
ATOM   48104 N  N   . SER   BA 14 46  ? 29.371  -167.671 60.313  1.00 84.69  ? 46  SER   b N   1 
ATOM   48105 C  CA  . SER   BA 14 46  ? 29.407  -166.253 59.869  1.00 84.44  ? 46  SER   b CA  1 
ATOM   48106 C  C   . SER   BA 14 46  ? 29.680  -166.229 58.365  1.00 83.37  ? 46  SER   b C   1 
ATOM   48107 O  O   . SER   BA 14 46  ? 30.357  -167.150 57.878  1.00 83.29  ? 46  SER   b O   1 
ATOM   48108 C  CB  . SER   BA 14 46  ? 30.446  -165.462 60.618  1.00 82.12  ? 46  SER   b CB  1 
ATOM   48109 O  OG  . SER   BA 14 46  ? 31.747  -165.724 60.123  1.00 84.93  ? 46  SER   b OG  1 
ATOM   48110 N  N   . GLY   BA 14 47  ? 29.180  -165.209 57.668  1.00 83.61  ? 47  GLY   b N   1 
ATOM   48111 C  CA  . GLY   BA 14 47  ? 29.330  -165.061 56.209  1.00 84.50  ? 47  GLY   b CA  1 
ATOM   48112 C  C   . GLY   BA 14 47  ? 28.057  -165.465 55.490  1.00 85.44  ? 47  GLY   b C   1 
ATOM   48113 O  O   . GLY   BA 14 47  ? 26.977  -165.363 56.106  1.00 88.52  ? 47  GLY   b O   1 
ATOM   48114 N  N   . SER   BA 14 48  ? 28.174  -165.909 54.235  1.00 83.70  ? 48  SER   b N   1 
ATOM   48115 C  CA  . SER   BA 14 48  ? 27.038  -166.350 53.383  1.00 85.57  ? 48  SER   b CA  1 
ATOM   48116 C  C   . SER   BA 14 48  ? 26.331  -167.534 54.047  1.00 85.09  ? 48  SER   b C   1 
ATOM   48117 O  O   . SER   BA 14 48  ? 26.988  -168.573 54.223  1.00 90.15  ? 48  SER   b O   1 
ATOM   48118 C  CB  . SER   BA 14 48  ? 27.495  -166.718 51.997  1.00 86.56  ? 48  SER   b CB  1 
ATOM   48119 O  OG  . SER   BA 14 48  ? 26.523  -167.523 51.345  1.00 88.80  ? 48  SER   b OG  1 
ATOM   48120 N  N   . ALA   BA 14 49  ? 25.045  -167.385 54.385  1.00 84.73  ? 49  ALA   b N   1 
ATOM   48121 C  CA  . ALA   BA 14 49  ? 24.215  -168.437 55.019  1.00 85.13  ? 49  ALA   b CA  1 
ATOM   48122 C  C   . ALA   BA 14 49  ? 24.232  -169.696 54.142  1.00 87.34  ? 49  ALA   b C   1 
ATOM   48123 O  O   . ALA   BA 14 49  ? 24.483  -170.791 54.685  1.00 89.48  ? 49  ALA   b O   1 
ATOM   48124 C  CB  . ALA   BA 14 49  ? 22.808  -167.939 55.250  1.00 83.48  ? 49  ALA   b CB  1 
ATOM   48125 N  N   . ALA   BA 14 50  ? 24.006  -169.542 52.834  1.00 86.75  ? 50  ALA   b N   1 
ATOM   48126 C  CA  . ALA   BA 14 50  ? 23.970  -170.649 51.849  1.00 87.90  ? 50  ALA   b CA  1 
ATOM   48127 C  C   . ALA   BA 14 50  ? 25.297  -171.415 51.881  1.00 88.97  ? 50  ALA   b C   1 
ATOM   48128 O  O   . ALA   BA 14 50  ? 25.251  -172.654 51.935  1.00 95.11  ? 50  ALA   b O   1 
ATOM   48129 C  CB  . ALA   BA 14 50  ? 23.683  -170.124 50.465  1.00 90.00  ? 50  ALA   b CB  1 
ATOM   48130 N  N   . ASP   BA 14 51  ? 26.428  -170.706 51.853  1.00 85.10  ? 51  ASP   b N   1 
ATOM   48131 C  CA  . ASP   BA 14 51  ? 27.785  -171.317 51.851  1.00 85.39  ? 51  ASP   b CA  1 
ATOM   48132 C  C   . ASP   BA 14 51  ? 28.027  -172.029 53.189  1.00 86.99  ? 51  ASP   b C   1 
ATOM   48133 O  O   . ASP   BA 14 51  ? 28.435  -173.204 53.153  1.00 86.84  ? 51  ASP   b O   1 
ATOM   48134 C  CB  . ASP   BA 14 51  ? 28.871  -170.283 51.542  1.00 85.71  ? 51  ASP   b CB  1 
ATOM   48135 C  CG  . ASP   BA 14 51  ? 28.859  -169.781 50.106  1.00 86.16  ? 51  ASP   b CG  1 
ATOM   48136 O  OD1 . ASP   BA 14 51  ? 28.313  -170.488 49.239  1.00 86.72  ? 51  ASP   b OD1 1 
ATOM   48137 O  OD2 . ASP   BA 14 51  ? 29.398  -168.684 49.867  1.00 89.78  ? 51  ASP   b OD2 1 
ATOM   48138 N  N   . THR   BA 14 52  ? 27.773  -171.362 54.320  1.00 85.40  ? 52  THR   b N   1 
ATOM   48139 C  CA  . THR   BA 14 52  ? 28.022  -171.908 55.685  1.00 87.33  ? 52  THR   b CA  1 
ATOM   48140 C  C   . THR   BA 14 52  ? 27.126  -173.131 55.940  1.00 89.45  ? 52  THR   b C   1 
ATOM   48141 O  O   . THR   BA 14 52  ? 27.638  -174.114 56.517  1.00 91.08  ? 52  THR   b O   1 
ATOM   48142 C  CB  . THR   BA 14 52  ? 27.847  -170.842 56.774  1.00 85.91  ? 52  THR   b CB  1 
ATOM   48143 O  OG1 . THR   BA 14 52  ? 26.530  -170.296 56.694  1.00 87.42  ? 52  THR   b OG1 1 
ATOM   48144 C  CG2 . THR   BA 14 52  ? 28.865  -169.729 56.669  1.00 84.59  ? 52  THR   b CG2 1 
ATOM   48145 N  N   . GLN   BA 14 53  ? 25.851  -173.074 55.535  1.00 88.23  ? 53  GLN   b N   1 
ATOM   48146 C  CA  . GLN   BA 14 53  ? 24.875  -174.191 55.677  1.00 89.11  ? 53  GLN   b CA  1 
ATOM   48147 C  C   . GLN   BA 14 53  ? 25.379  -175.417 54.902  1.00 88.49  ? 53  GLN   b C   1 
ATOM   48148 O  O   . GLN   BA 14 53  ? 25.341  -176.530 55.468  1.00 91.19  ? 53  GLN   b O   1 
ATOM   48149 C  CB  . GLN   BA 14 53  ? 23.489  -173.779 55.176  1.00 88.97  ? 53  GLN   b CB  1 
ATOM   48150 C  CG  . GLN   BA 14 53  ? 22.723  -172.894 56.149  1.00 89.73  ? 53  GLN   b CG  1 
ATOM   48151 C  CD  . GLN   BA 14 53  ? 21.285  -172.686 55.742  1.00 91.25  ? 53  GLN   b CD  1 
ATOM   48152 O  OE1 . GLN   BA 14 53  ? 20.754  -173.374 54.873  1.00 96.92  ? 53  GLN   b OE1 1 
ATOM   48153 N  NE2 . GLN   BA 14 53  ? 20.633  -171.730 56.380  1.00 91.27  ? 53  GLN   b NE2 1 
ATOM   48154 N  N   . ALA   BA 14 54  ? 25.828  -175.210 53.660  1.00 85.49  ? 54  ALA   b N   1 
ATOM   48155 C  CA  . ALA   BA 14 54  ? 26.318  -176.259 52.735  1.00 84.58  ? 54  ALA   b CA  1 
ATOM   48156 C  C   . ALA   BA 14 54  ? 27.552  -176.953 53.319  1.00 86.12  ? 54  ALA   b C   1 
ATOM   48157 O  O   . ALA   BA 14 54  ? 27.633  -178.188 53.201  1.00 90.38  ? 54  ALA   b O   1 
ATOM   48158 C  CB  . ALA   BA 14 54  ? 26.629  -175.658 51.388  1.00 83.21  ? 54  ALA   b CB  1 
ATOM   48159 N  N   . ILE   BA 14 55  ? 28.477  -176.190 53.907  1.00 83.96  ? 55  ILE   b N   1 
ATOM   48160 C  CA  . ILE   BA 14 55  ? 29.749  -176.717 54.490  1.00 84.36  ? 55  ILE   b CA  1 
ATOM   48161 C  C   . ILE   BA 14 55  ? 29.424  -177.559 55.728  1.00 83.99  ? 55  ILE   b C   1 
ATOM   48162 O  O   . ILE   BA 14 55  ? 29.953  -178.681 55.815  1.00 84.23  ? 55  ILE   b O   1 
ATOM   48163 C  CB  . ILE   BA 14 55  ? 30.735  -175.582 54.828  1.00 82.98  ? 55  ILE   b CB  1 
ATOM   48164 C  CG1 . ILE   BA 14 55  ? 31.136  -174.784 53.587  1.00 83.29  ? 55  ILE   b CG1 1 
ATOM   48165 C  CG2 . ILE   BA 14 55  ? 31.959  -176.129 55.547  1.00 83.80  ? 55  ILE   b CG2 1 
ATOM   48166 C  CD1 . ILE   BA 14 55  ? 31.767  -173.453 53.908  1.00 84.14  ? 55  ILE   b CD1 1 
ATOM   48167 N  N   . ALA   BA 14 56  ? 28.610  -177.029 56.649  1.00 83.88  ? 56  ALA   b N   1 
ATOM   48168 C  CA  . ALA   BA 14 56  ? 28.228  -177.686 57.923  1.00 86.28  ? 56  ALA   b CA  1 
ATOM   48169 C  C   . ALA   BA 14 56  ? 27.637  -179.070 57.629  1.00 88.71  ? 56  ALA   b C   1 
ATOM   48170 O  O   . ALA   BA 14 56  ? 28.044  -180.044 58.302  1.00 92.39  ? 56  ALA   b O   1 
ATOM   48171 C  CB  . ALA   BA 14 56  ? 27.254  -176.826 58.692  1.00 85.53  ? 56  ALA   b CB  1 
ATOM   48172 N  N   . ASP   BA 14 57  ? 26.723  -179.143 56.654  1.00 88.18  ? 57  ASP   b N   1 
ATOM   48173 C  CA  . ASP   BA 14 57  ? 26.048  -180.390 56.199  1.00 89.74  ? 57  ASP   b CA  1 
ATOM   48174 C  C   . ASP   BA 14 57  ? 27.090  -181.420 55.743  1.00 85.97  ? 57  ASP   b C   1 
ATOM   48175 O  O   . ASP   BA 14 57  ? 26.967  -182.587 56.154  1.00 88.82  ? 57  ASP   b O   1 
ATOM   48176 C  CB  . ASP   BA 14 57  ? 25.050  -180.111 55.070  1.00 91.41  ? 57  ASP   b CB  1 
ATOM   48177 C  CG  . ASP   BA 14 57  ? 23.770  -179.409 55.506  1.00 92.90  ? 57  ASP   b CG  1 
ATOM   48178 O  OD1 . ASP   BA 14 57  ? 23.461  -179.446 56.717  1.00 94.70  ? 57  ASP   b OD1 1 
ATOM   48179 O  OD2 . ASP   BA 14 57  ? 23.081  -178.842 54.623  1.00 90.53  ? 57  ASP   b OD2 1 
ATOM   48180 N  N   . ILE   BA 14 58  ? 28.064  -181.009 54.923  1.00 80.60  ? 58  ILE   b N   1 
ATOM   48181 C  CA  . ILE   BA 14 58  ? 29.142  -181.895 54.388  1.00 81.67  ? 58  ILE   b CA  1 
ATOM   48182 C  C   . ILE   BA 14 58  ? 30.029  -182.375 55.543  1.00 87.44  ? 58  ILE   b C   1 
ATOM   48183 O  O   . ILE   BA 14 58  ? 30.384  -183.573 55.546  1.00 92.70  ? 58  ILE   b O   1 
ATOM   48184 C  CB  . ILE   BA 14 58  ? 29.966  -181.191 53.293  1.00 80.33  ? 58  ILE   b CB  1 
ATOM   48185 C  CG1 . ILE   BA 14 58  ? 29.129  -180.953 52.035  1.00 80.96  ? 58  ILE   b CG1 1 
ATOM   48186 C  CG2 . ILE   BA 14 58  ? 31.235  -181.974 52.980  1.00 79.30  ? 58  ILE   b CG2 1 
ATOM   48187 C  CD1 . ILE   BA 14 58  ? 29.716  -179.936 51.088  1.00 81.78  ? 58  ILE   b CD1 1 
ATOM   48188 N  N   . VAL   BA 14 59  ? 30.394  -181.482 56.471  1.00 85.89  ? 59  VAL   b N   1 
ATOM   48189 C  CA  . VAL   BA 14 59  ? 31.236  -181.823 57.658  1.00 88.34  ? 59  VAL   b CA  1 
ATOM   48190 C  C   . VAL   BA 14 59  ? 30.488  -182.870 58.491  1.00 88.48  ? 59  VAL   b C   1 
ATOM   48191 O  O   . VAL   BA 14 59  ? 31.099  -183.908 58.811  1.00 93.19  ? 59  VAL   b O   1 
ATOM   48192 C  CB  . VAL   BA 14 59  ? 31.603  -180.582 58.498  1.00 87.18  ? 59  VAL   b CB  1 
ATOM   48193 C  CG1 . VAL   BA 14 59  ? 32.203  -180.960 59.846  1.00 87.41  ? 59  VAL   b CG1 1 
ATOM   48194 C  CG2 . VAL   BA 14 59  ? 32.550  -179.662 57.747  1.00 88.58  ? 59  VAL   b CG2 1 
ATOM   48195 N  N   . GLN   BA 14 60  ? 29.216  -182.611 58.812  1.00 87.42  ? 60  GLN   b N   1 
ATOM   48196 C  CA  . GLN   BA 14 60  ? 28.375  -183.509 59.650  1.00 88.40  ? 60  GLN   b CA  1 
ATOM   48197 C  C   . GLN   BA 14 60  ? 28.346  -184.906 59.021  1.00 89.88  ? 60  GLN   b C   1 
ATOM   48198 O  O   . GLN   BA 14 60  ? 28.452  -185.891 59.776  1.00 88.90  ? 60  GLN   b O   1 
ATOM   48199 C  CB  . GLN   BA 14 60  ? 26.960  -182.956 59.812  1.00 90.25  ? 60  GLN   b CB  1 
ATOM   48200 C  CG  . GLN   BA 14 60  ? 26.144  -183.720 60.844  1.00 92.54  ? 60  GLN   b CG  1 
ATOM   48201 C  CD  . GLN   BA 14 60  ? 24.721  -183.230 60.938  1.00 95.10  ? 60  GLN   b CD  1 
ATOM   48202 O  OE1 . GLN   BA 14 60  ? 24.143  -182.754 59.964  1.00 97.34  ? 60  GLN   b OE1 1 
ATOM   48203 N  NE2 . GLN   BA 14 60  ? 24.142  -183.351 62.123  1.00 97.76  ? 60  GLN   b NE2 1 
ATOM   48204 N  N   . TYR   BA 14 61  ? 28.213  -184.977 57.693  1.00 88.77  ? 61  TYR   b N   1 
ATOM   48205 C  CA  . TYR   BA 14 61  ? 28.249  -186.234 56.904  1.00 91.75  ? 61  TYR   b CA  1 
ATOM   48206 C  C   . TYR   BA 14 61  ? 29.605  -186.923 57.102  1.00 92.43  ? 61  TYR   b C   1 
ATOM   48207 O  O   . TYR   BA 14 61  ? 29.610  -188.131 57.386  1.00 98.00  ? 61  TYR   b O   1 
ATOM   48208 C  CB  . TYR   BA 14 61  ? 27.972  -185.972 55.420  1.00 91.66  ? 61  TYR   b CB  1 
ATOM   48209 C  CG  . TYR   BA 14 61  ? 28.561  -187.002 54.489  1.00 95.46  ? 61  TYR   b CG  1 
ATOM   48210 C  CD1 . TYR   BA 14 61  ? 27.939  -188.223 54.285  1.00 96.77  ? 61  TYR   b CD1 1 
ATOM   48211 C  CD2 . TYR   BA 14 61  ? 29.757  -186.767 53.830  1.00 95.95  ? 61  TYR   b CD2 1 
ATOM   48212 C  CE1 . TYR   BA 14 61  ? 28.483  -189.179 53.442  1.00 100.28 ? 61  TYR   b CE1 1 
ATOM   48213 C  CE2 . TYR   BA 14 61  ? 30.315  -187.711 52.983  1.00 98.98  ? 61  TYR   b CE2 1 
ATOM   48214 C  CZ  . TYR   BA 14 61  ? 29.675  -188.922 52.788  1.00 101.05 ? 61  TYR   b CZ  1 
ATOM   48215 O  OH  . TYR   BA 14 61  ? 30.218  -189.858 51.956  1.00 106.44 ? 61  TYR   b OH  1 
ATOM   48216 N  N   . HIS   BA 14 62  ? 30.710  -186.185 56.953  1.00 89.02  ? 62  HIS   b N   1 
ATOM   48217 C  CA  . HIS   BA 14 62  ? 32.098  -186.716 57.061  1.00 92.19  ? 62  HIS   b CA  1 
ATOM   48218 C  C   . HIS   BA 14 62  ? 32.348  -187.293 58.460  1.00 94.16  ? 62  HIS   b C   1 
ATOM   48219 O  O   . HIS   BA 14 62  ? 32.950  -188.381 58.537  1.00 100.60 ? 62  HIS   b O   1 
ATOM   48220 C  CB  . HIS   BA 14 62  ? 33.141  -185.644 56.715  1.00 92.95  ? 62  HIS   b CB  1 
ATOM   48221 C  CG  . HIS   BA 14 62  ? 33.606  -185.689 55.300  1.00 96.66  ? 62  HIS   b CG  1 
ATOM   48222 N  ND1 . HIS   BA 14 62  ? 34.626  -186.526 54.888  1.00 100.65 ? 62  HIS   b ND1 1 
ATOM   48223 C  CD2 . HIS   BA 14 62  ? 33.204  -185.009 54.204  1.00 97.89  ? 62  HIS   b CD2 1 
ATOM   48224 C  CE1 . HIS   BA 14 62  ? 34.828  -186.363 53.595  1.00 102.20 ? 62  HIS   b CE1 1 
ATOM   48225 N  NE2 . HIS   BA 14 62  ? 33.968  -185.437 53.152  1.00 100.39 ? 62  HIS   b NE2 1 
ATOM   48226 N  N   . LEU   BA 14 63  ? 31.921  -186.590 59.515  1.00 91.02  ? 63  LEU   b N   1 
ATOM   48227 C  CA  . LEU   BA 14 63  ? 32.135  -187.001 60.932  1.00 90.48  ? 63  LEU   b CA  1 
ATOM   48228 C  C   . LEU   BA 14 63  ? 31.223  -188.185 61.286  1.00 91.20  ? 63  LEU   b C   1 
ATOM   48229 O  O   . LEU   BA 14 63  ? 31.623  -189.002 62.145  1.00 87.72  ? 63  LEU   b O   1 
ATOM   48230 C  CB  . LEU   BA 14 63  ? 31.876  -185.808 61.859  1.00 88.73  ? 63  LEU   b CB  1 
ATOM   48231 C  CG  . LEU   BA 14 63  ? 32.814  -184.612 61.692  1.00 86.57  ? 63  LEU   b CG  1 
ATOM   48232 C  CD1 . LEU   BA 14 63  ? 32.474  -183.531 62.705  1.00 86.40  ? 63  LEU   b CD1 1 
ATOM   48233 C  CD2 . LEU   BA 14 63  ? 34.275  -185.021 61.825  1.00 86.47  ? 63  LEU   b CD2 1 
ATOM   48234 N  N   . GLU   BA 14 64  ? 30.045  -188.276 60.661  1.00 89.62  ? 64  GLU   b N   1 
ATOM   48235 C  CA  . GLU   BA 14 64  ? 29.124  -189.435 60.805  1.00 90.45  ? 64  GLU   b CA  1 
ATOM   48236 C  C   . GLU   BA 14 64  ? 29.801  -190.686 60.232  1.00 90.68  ? 64  GLU   b C   1 
ATOM   48237 O  O   . GLU   BA 14 64  ? 29.761  -191.740 60.904  1.00 91.16  ? 64  GLU   b O   1 
ATOM   48238 C  CB  . GLU   BA 14 64  ? 27.791  -189.156 60.110  1.00 91.82  ? 64  GLU   b CB  1 
ATOM   48239 C  CG  . GLU   BA 14 64  ? 26.778  -190.276 60.272  1.00 94.56  ? 64  GLU   b CG  1 
ATOM   48240 C  CD  . GLU   BA 14 64  ? 25.325  -189.839 60.178  1.00 96.67  ? 64  GLU   b CD  1 
ATOM   48241 O  OE1 . GLU   BA 14 64  ? 24.576  -190.435 59.378  1.00 99.20  ? 64  GLU   b OE1 1 
ATOM   48242 O  OE2 . GLU   BA 14 64  ? 24.943  -188.911 60.917  1.00 100.23 ? 64  GLU   b OE2 1 
ATOM   48243 N  N   . LEU   BA 14 65  ? 30.408  -190.568 59.046  1.00 87.31  ? 65  LEU   b N   1 
ATOM   48244 C  CA  . LEU   BA 14 65  ? 31.090  -191.689 58.345  1.00 89.30  ? 65  LEU   b CA  1 
ATOM   48245 C  C   . LEU   BA 14 65  ? 32.408  -192.025 59.056  1.00 91.79  ? 65  LEU   b C   1 
ATOM   48246 O  O   . LEU   BA 14 65  ? 32.767  -193.220 59.078  1.00 93.01  ? 65  LEU   b O   1 
ATOM   48247 C  CB  . LEU   BA 14 65  ? 31.318  -191.308 56.878  1.00 88.91  ? 65  LEU   b CB  1 
ATOM   48248 C  CG  . LEU   BA 14 65  ? 31.926  -192.396 55.992  1.00 91.87  ? 65  LEU   b CG  1 
ATOM   48249 C  CD1 . LEU   BA 14 65  ? 31.116  -193.686 56.049  1.00 94.30  ? 65  LEU   b CD1 1 
ATOM   48250 C  CD2 . LEU   BA 14 65  ? 32.050  -191.912 54.556  1.00 91.04  ? 65  LEU   b CD2 1 
ATOM   48251 N  N   . TYR   BA 14 66  ? 33.096  -191.020 59.613  1.00 88.94  ? 66  TYR   b N   1 
ATOM   48252 C  CA  . TYR   BA 14 66  ? 34.300  -191.188 60.475  1.00 89.22  ? 66  TYR   b CA  1 
ATOM   48253 C  C   . TYR   BA 14 66  ? 33.931  -192.045 61.692  1.00 92.58  ? 66  TYR   b C   1 
ATOM   48254 O  O   . TYR   BA 14 66  ? 34.605  -193.066 61.940  1.00 92.93  ? 66  TYR   b O   1 
ATOM   48255 C  CB  . TYR   BA 14 66  ? 34.854  -189.834 60.930  1.00 88.24  ? 66  TYR   b CB  1 
ATOM   48256 C  CG  . TYR   BA 14 66  ? 36.124  -189.907 61.742  1.00 86.25  ? 66  TYR   b CG  1 
ATOM   48257 C  CD1 . TYR   BA 14 66  ? 36.094  -190.198 63.098  1.00 85.92  ? 66  TYR   b CD1 1 
ATOM   48258 C  CD2 . TYR   BA 14 66  ? 37.360  -189.676 61.159  1.00 86.27  ? 66  TYR   b CD2 1 
ATOM   48259 C  CE1 . TYR   BA 14 66  ? 37.257  -190.263 63.849  1.00 87.38  ? 66  TYR   b CE1 1 
ATOM   48260 C  CE2 . TYR   BA 14 66  ? 38.532  -189.738 61.896  1.00 86.59  ? 66  TYR   b CE2 1 
ATOM   48261 C  CZ  . TYR   BA 14 66  ? 38.481  -190.031 63.246  1.00 87.75  ? 66  TYR   b CZ  1 
ATOM   48262 O  OH  . TYR   BA 14 66  ? 39.633  -190.093 63.977  1.00 91.64  ? 66  TYR   b OH  1 
ATOM   48263 N  N   . THR   BA 14 67  ? 32.887  -191.628 62.418  1.00 92.30  ? 67  THR   b N   1 
ATOM   48264 C  CA  . THR   BA 14 67  ? 32.390  -192.277 63.661  1.00 92.50  ? 67  THR   b CA  1 
ATOM   48265 C  C   . THR   BA 14 67  ? 32.047  -193.743 63.386  1.00 94.23  ? 67  THR   b C   1 
ATOM   48266 O  O   . THR   BA 14 67  ? 32.418  -194.585 64.219  1.00 97.45  ? 67  THR   b O   1 
ATOM   48267 C  CB  . THR   BA 14 67  ? 31.175  -191.547 64.244  1.00 91.42  ? 67  THR   b CB  1 
ATOM   48268 O  OG1 . THR   BA 14 67  ? 31.496  -190.158 64.327  1.00 88.94  ? 67  THR   b OG1 1 
ATOM   48269 C  CG2 . THR   BA 14 67  ? 30.781  -192.084 65.603  1.00 93.06  ? 67  THR   b CG2 1 
ATOM   48270 N  N   . SER   BA 14 68  ? 31.366  -194.025 62.270  1.00 92.30  ? 68  SER   b N   1 
ATOM   48271 C  CA  . SER   BA 14 68  ? 30.977  -195.393 61.835  1.00 94.88  ? 68  SER   b CA  1 
ATOM   48272 C  C   . SER   BA 14 68  ? 32.201  -196.310 61.803  1.00 95.16  ? 68  SER   b C   1 
ATOM   48273 O  O   . SER   BA 14 68  ? 32.043  -197.496 62.131  1.00 98.83  ? 68  SER   b O   1 
ATOM   48274 C  CB  . SER   BA 14 68  ? 30.308  -195.383 60.491  1.00 95.66  ? 68  SER   b CB  1 
ATOM   48275 O  OG  . SER   BA 14 68  ? 28.987  -194.879 60.588  1.00 101.40 ? 68  SER   b OG  1 
ATOM   48276 N  N   . GLN   BA 14 69  ? 33.366  -195.781 61.420  1.00 94.24  ? 69  GLN   b N   1 
ATOM   48277 C  CA  . GLN   BA 14 69  ? 34.593  -196.580 61.169  1.00 97.79  ? 69  GLN   b CA  1 
ATOM   48278 C  C   . GLN   BA 14 69  ? 35.563  -196.506 62.356  1.00 101.42 ? 69  GLN   b C   1 
ATOM   48279 O  O   . GLN   BA 14 69  ? 36.089  -197.572 62.740  1.00 110.48 ? 69  GLN   b O   1 
ATOM   48280 C  CB  . GLN   BA 14 69  ? 35.260  -196.096 59.885  1.00 97.19  ? 69  GLN   b CB  1 
ATOM   48281 C  CG  . GLN   BA 14 69  ? 34.341  -196.178 58.677  1.00 97.97  ? 69  GLN   b CG  1 
ATOM   48282 C  CD  . GLN   BA 14 69  ? 35.050  -195.780 57.407  1.00 99.59  ? 69  GLN   b CD  1 
ATOM   48283 O  OE1 . GLN   BA 14 69  ? 36.090  -196.330 57.055  1.00 101.85 ? 69  GLN   b OE1 1 
ATOM   48284 N  NE2 . GLN   BA 14 69  ? 34.485  -194.818 56.700  1.00 98.62  ? 69  GLN   b NE2 1 
ATOM   48285 N  N   . TYR   BA 14 70  ? 35.803  -195.312 62.911  1.00 98.59  ? 70  TYR   b N   1 
ATOM   48286 C  CA  . TYR   BA 14 70  ? 36.928  -195.042 63.848  1.00 98.70  ? 70  TYR   b CA  1 
ATOM   48287 C  C   . TYR   BA 14 70  ? 36.448  -194.456 65.183  1.00 97.53  ? 70  TYR   b C   1 
ATOM   48288 O  O   . TYR   BA 14 70  ? 37.309  -193.965 65.943  1.00 95.61  ? 70  TYR   b O   1 
ATOM   48289 C  CB  . TYR   BA 14 70  ? 37.928  -194.080 63.204  1.00 95.15  ? 70  TYR   b CB  1 
ATOM   48290 C  CG  . TYR   BA 14 70  ? 38.104  -194.253 61.717  1.00 96.09  ? 70  TYR   b CG  1 
ATOM   48291 C  CD1 . TYR   BA 14 70  ? 38.591  -195.435 61.183  1.00 96.85  ? 70  TYR   b CD1 1 
ATOM   48292 C  CD2 . TYR   BA 14 70  ? 37.787  -193.229 60.840  1.00 94.27  ? 70  TYR   b CD2 1 
ATOM   48293 C  CE1 . TYR   BA 14 70  ? 38.756  -195.597 59.816  1.00 96.06  ? 70  TYR   b CE1 1 
ATOM   48294 C  CE2 . TYR   BA 14 70  ? 37.945  -193.374 59.472  1.00 93.10  ? 70  TYR   b CE2 1 
ATOM   48295 C  CZ  . TYR   BA 14 70  ? 38.433  -194.560 58.957  1.00 93.38  ? 70  TYR   b CZ  1 
ATOM   48296 O  OH  . TYR   BA 14 70  ? 38.589  -194.688 57.609  1.00 90.27  ? 70  TYR   b OH  1 
ATOM   48297 N  N   . GLY   BA 14 71  ? 35.143  -194.502 65.467  1.00 98.50  ? 71  GLY   b N   1 
ATOM   48298 C  CA  . GLY   BA 14 71  ? 34.565  -193.975 66.719  1.00 98.85  ? 71  GLY   b CA  1 
ATOM   48299 C  C   . GLY   BA 14 71  ? 34.631  -192.457 66.762  1.00 98.11  ? 71  GLY   b C   1 
ATOM   48300 O  O   . GLY   BA 14 71  ? 34.795  -191.846 65.686  1.00 96.71  ? 71  GLY   b O   1 
ATOM   48301 N  N   . THR   BA 14 72  ? 34.534  -191.867 67.959  1.00 97.58  ? 72  THR   b N   1 
ATOM   48302 C  CA  . THR   BA 14 72  ? 34.378  -190.400 68.162  1.00 94.47  ? 72  THR   b CA  1 
ATOM   48303 C  C   . THR   BA 14 72  ? 35.591  -189.664 67.599  1.00 90.23  ? 72  THR   b C   1 
ATOM   48304 O  O   . THR   BA 14 72  ? 36.728  -189.974 67.951  1.00 86.39  ? 72  THR   b O   1 
ATOM   48305 C  CB  . THR   BA 14 72  ? 34.165  -190.039 69.637  1.00 93.67  ? 72  THR   b CB  1 
ATOM   48306 O  OG1 . THR   BA 14 72  ? 33.130  -190.868 70.163  1.00 99.15  ? 72  THR   b OG1 1 
ATOM   48307 C  CG2 . THR   BA 14 72  ? 33.775  -188.592 69.831  1.00 94.10  ? 72  THR   b CG2 1 
ATOM   48308 N  N   . PRO   BA 14 73  ? 35.381  -188.668 66.706  1.00 90.01  ? 73  PRO   b N   1 
ATOM   48309 C  CA  . PRO   BA 14 73  ? 36.469  -187.839 66.191  1.00 89.64  ? 73  PRO   b CA  1 
ATOM   48310 C  C   . PRO   BA 14 73  ? 36.886  -186.754 67.192  1.00 87.84  ? 73  PRO   b C   1 
ATOM   48311 O  O   . PRO   BA 14 73  ? 36.043  -186.305 67.955  1.00 85.16  ? 73  PRO   b O   1 
ATOM   48312 C  CB  . PRO   BA 14 73  ? 35.854  -187.178 64.952  1.00 88.16  ? 73  PRO   b CB  1 
ATOM   48313 C  CG  . PRO   BA 14 73  ? 34.386  -187.056 65.306  1.00 89.34  ? 73  PRO   b CG  1 
ATOM   48314 C  CD  . PRO   BA 14 73  ? 34.078  -188.285 66.138  1.00 90.63  ? 73  PRO   b CD  1 
ATOM   48315 N  N   . SER   BA 14 74  ? 38.157  -186.346 67.148  1.00 88.83  ? 74  SER   b N   1 
ATOM   48316 C  CA  . SER   BA 14 74  ? 38.705  -185.230 67.962  1.00 88.27  ? 74  SER   b CA  1 
ATOM   48317 C  C   . SER   BA 14 74  ? 38.173  -183.913 67.394  1.00 86.88  ? 74  SER   b C   1 
ATOM   48318 O  O   . SER   BA 14 74  ? 37.817  -183.884 66.198  1.00 85.64  ? 74  SER   b O   1 
ATOM   48319 C  CB  . SER   BA 14 74  ? 40.213  -185.248 68.003  1.00 86.09  ? 74  SER   b CB  1 
ATOM   48320 O  OG  . SER   BA 14 74  ? 40.766  -184.913 66.739  1.00 83.29  ? 74  SER   b OG  1 
ATOM   48321 N  N   . THR   BA 14 75  ? 38.100  -182.874 68.226  1.00 89.67  ? 75  THR   b N   1 
ATOM   48322 C  CA  . THR   BA 14 75  ? 37.698  -181.506 67.809  1.00 88.07  ? 75  THR   b CA  1 
ATOM   48323 C  C   . THR   BA 14 75  ? 38.648  -181.040 66.702  1.00 83.56  ? 75  THR   b C   1 
ATOM   48324 O  O   . THR   BA 14 75  ? 38.156  -180.506 65.697  1.00 82.80  ? 75  THR   b O   1 
ATOM   48325 C  CB  . THR   BA 14 75  ? 37.678  -180.540 68.997  1.00 89.00  ? 75  THR   b CB  1 
ATOM   48326 O  OG1 . THR   BA 14 75  ? 36.898  -181.139 70.035  1.00 92.31  ? 75  THR   b OG1 1 
ATOM   48327 C  CG2 . THR   BA 14 75  ? 37.122  -179.183 68.625  1.00 87.83  ? 75  THR   b CG2 1 
ATOM   48328 N  N   . GLU   BA 14 76  ? 39.953  -181.269 66.875  1.00 84.57  ? 76  GLU   b N   1 
ATOM   48329 C  CA  . GLU   BA 14 76  ? 41.006  -180.942 65.878  1.00 86.99  ? 76  GLU   b CA  1 
ATOM   48330 C  C   . GLU   BA 14 76  ? 40.629  -181.537 64.516  1.00 87.32  ? 76  GLU   b C   1 
ATOM   48331 O  O   . GLU   BA 14 76  ? 40.730  -180.808 63.514  1.00 83.00  ? 76  GLU   b O   1 
ATOM   48332 C  CB  . GLU   BA 14 76  ? 42.368  -181.468 66.332  1.00 93.05  ? 76  GLU   b CB  1 
ATOM   48333 C  CG  . GLU   BA 14 76  ? 43.511  -181.036 65.429  1.00 99.18  ? 76  GLU   b CG  1 
ATOM   48334 C  CD  . GLU   BA 14 76  ? 44.891  -181.454 65.909  1.00 106.45 ? 76  GLU   b CD  1 
ATOM   48335 O  OE1 . GLU   BA 14 76  ? 45.799  -180.592 65.914  1.00 116.63 ? 76  GLU   b OE1 1 
ATOM   48336 O  OE2 . GLU   BA 14 76  ? 45.057  -182.640 66.272  1.00 108.40 ? 76  GLU   b OE2 1 
ATOM   48337 N  N   . THR   BA 14 77  ? 40.222  -182.811 64.480  1.00 88.65  ? 77  THR   b N   1 
ATOM   48338 C  CA  . THR   BA 14 77  ? 39.824  -183.528 63.236  1.00 90.05  ? 77  THR   b CA  1 
ATOM   48339 C  C   . THR   BA 14 77  ? 38.671  -182.766 62.569  1.00 86.78  ? 77  THR   b C   1 
ATOM   48340 O  O   . THR   BA 14 77  ? 38.758  -182.528 61.351  1.00 86.15  ? 77  THR   b O   1 
ATOM   48341 C  CB  . THR   BA 14 77  ? 39.455  -184.997 63.497  1.00 91.11  ? 77  THR   b CB  1 
ATOM   48342 O  OG1 . THR   BA 14 77  ? 40.619  -185.713 63.913  1.00 93.53  ? 77  THR   b OG1 1 
ATOM   48343 C  CG2 . THR   BA 14 77  ? 38.881  -185.682 62.277  1.00 91.71  ? 77  THR   b CG2 1 
ATOM   48344 N  N   . ALA   BA 14 78  ? 37.641  -182.400 63.338  1.00 85.02  ? 78  ALA   b N   1 
ATOM   48345 C  CA  . ALA   BA 14 78  ? 36.437  -181.687 62.850  1.00 85.22  ? 78  ALA   b CA  1 
ATOM   48346 C  C   . ALA   BA 14 78  ? 36.848  -180.352 62.212  1.00 85.91  ? 78  ALA   b C   1 
ATOM   48347 O  O   . ALA   BA 14 78  ? 36.329  -180.028 61.123  1.00 89.06  ? 78  ALA   b O   1 
ATOM   48348 C  CB  . ALA   BA 14 78  ? 35.456  -181.486 63.979  1.00 84.25  ? 78  ALA   b CB  1 
ATOM   48349 N  N   . ALA   BA 14 79  ? 37.756  -179.616 62.860  1.00 84.12  ? 79  ALA   b N   1 
ATOM   48350 C  CA  . ALA   BA 14 79  ? 38.288  -178.315 62.388  1.00 83.48  ? 79  ALA   b CA  1 
ATOM   48351 C  C   . ALA   BA 14 79  ? 39.076  -178.514 61.087  1.00 83.53  ? 79  ALA   b C   1 
ATOM   48352 O  O   . ALA   BA 14 79  ? 39.001  -177.633 60.218  1.00 84.24  ? 79  ALA   b O   1 
ATOM   48353 C  CB  . ALA   BA 14 79  ? 39.140  -177.681 63.459  1.00 81.39  ? 79  ALA   b CB  1 
ATOM   48354 N  N   . SER   BA 14 80  ? 39.793  -179.633 60.956  1.00 84.28  ? 80  SER   b N   1 
ATOM   48355 C  CA  . SER   BA 14 80  ? 40.605  -179.980 59.759  1.00 86.02  ? 80  SER   b CA  1 
ATOM   48356 C  C   . SER   BA 14 80  ? 39.692  -180.212 58.550  1.00 84.68  ? 80  SER   b C   1 
ATOM   48357 O  O   . SER   BA 14 80  ? 40.099  -179.841 57.433  1.00 81.52  ? 80  SER   b O   1 
ATOM   48358 C  CB  . SER   BA 14 80  ? 41.483  -181.180 60.018  1.00 87.82  ? 80  SER   b CB  1 
ATOM   48359 O  OG  . SER   BA 14 80  ? 42.285  -181.479 58.883  1.00 89.31  ? 80  SER   b OG  1 
ATOM   48360 N  N   . VAL   BA 14 81  ? 38.514  -180.807 58.763  1.00 86.23  ? 81  VAL   b N   1 
ATOM   48361 C  CA  . VAL   BA 14 81  ? 37.526  -181.111 57.682  1.00 89.12  ? 81  VAL   b CA  1 
ATOM   48362 C  C   . VAL   BA 14 81  ? 36.882  -179.795 57.225  1.00 86.72  ? 81  VAL   b C   1 
ATOM   48363 O  O   . VAL   BA 14 81  ? 36.694  -179.636 56.003  1.00 86.27  ? 81  VAL   b O   1 
ATOM   48364 C  CB  . VAL   BA 14 81  ? 36.473  -182.147 58.127  1.00 92.38  ? 81  VAL   b CB  1 
ATOM   48365 C  CG1 . VAL   BA 14 81  ? 35.412  -182.379 57.058  1.00 93.27  ? 81  VAL   b CG1 1 
ATOM   48366 C  CG2 . VAL   BA 14 81  ? 37.118  -183.470 58.517  1.00 93.55  ? 81  VAL   b CG2 1 
ATOM   48367 N  N   . PHE   BA 14 82  ? 36.558  -178.895 58.163  1.00 84.71  ? 82  PHE   b N   1 
ATOM   48368 C  CA  . PHE   BA 14 82  ? 36.072  -177.516 57.878  1.00 79.21  ? 82  PHE   b CA  1 
ATOM   48369 C  C   . PHE   BA 14 82  ? 37.124  -176.773 57.051  1.00 76.35  ? 82  PHE   b C   1 
ATOM   48370 O  O   . PHE   BA 14 82  ? 36.781  -176.265 55.971  1.00 76.43  ? 82  PHE   b O   1 
ATOM   48371 C  CB  . PHE   BA 14 82  ? 35.777  -176.738 59.161  1.00 77.34  ? 82  PHE   b CB  1 
ATOM   48372 C  CG  . PHE   BA 14 82  ? 34.356  -176.843 59.649  1.00 76.20  ? 82  PHE   b CG  1 
ATOM   48373 C  CD1 . PHE   BA 14 82  ? 33.326  -176.220 58.962  1.00 75.62  ? 82  PHE   b CD1 1 
ATOM   48374 C  CD2 . PHE   BA 14 82  ? 34.048  -177.551 60.801  1.00 78.41  ? 82  PHE   b CD2 1 
ATOM   48375 C  CE1 . PHE   BA 14 82  ? 32.018  -176.310 59.413  1.00 76.32  ? 82  PHE   b CE1 1 
ATOM   48376 C  CE2 . PHE   BA 14 82  ? 32.738  -177.638 61.250  1.00 79.08  ? 82  PHE   b CE2 1 
ATOM   48377 C  CZ  . PHE   BA 14 82  ? 31.726  -177.016 60.556  1.00 78.01  ? 82  PHE   b CZ  1 
ATOM   48378 N  N   . LYS   BA 14 83  ? 38.364  -176.733 57.550  1.00 77.11  ? 83  LYS   b N   1 
ATOM   48379 C  CA  . LYS   BA 14 83  ? 39.523  -176.074 56.890  1.00 81.11  ? 83  LYS   b CA  1 
ATOM   48380 C  C   . LYS   BA 14 83  ? 39.662  -176.585 55.453  1.00 84.36  ? 83  LYS   b C   1 
ATOM   48381 O  O   . LYS   BA 14 83  ? 39.809  -175.750 54.548  1.00 83.17  ? 83  LYS   b O   1 
ATOM   48382 C  CB  . LYS   BA 14 83  ? 40.823  -176.347 57.651  1.00 84.64  ? 83  LYS   b CB  1 
ATOM   48383 C  CG  . LYS   BA 14 83  ? 42.089  -175.842 56.966  1.00 88.88  ? 83  LYS   b CG  1 
ATOM   48384 C  CD  . LYS   BA 14 83  ? 43.240  -176.820 57.035  1.00 96.34  ? 83  LYS   b CD  1 
ATOM   48385 C  CE  . LYS   BA 14 83  ? 43.088  -177.962 56.051  1.00 101.27 ? 83  LYS   b CE  1 
ATOM   48386 N  NZ  . LYS   BA 14 83  ? 43.825  -179.173 56.484  1.00 106.84 ? 83  LYS   b NZ  1 
ATOM   48387 N  N   . GLU   BA 14 84  ? 39.635  -177.906 55.263  1.00 85.96  ? 84  GLU   b N   1 
ATOM   48388 C  CA  . GLU   BA 14 84  ? 39.862  -178.556 53.944  1.00 89.43  ? 84  GLU   b CA  1 
ATOM   48389 C  C   . GLU   BA 14 84  ? 38.852  -178.007 52.926  1.00 87.65  ? 84  GLU   b C   1 
ATOM   48390 O  O   . GLU   BA 14 84  ? 39.273  -177.667 51.801  1.00 84.88  ? 84  GLU   b O   1 
ATOM   48391 C  CB  . GLU   BA 14 84  ? 39.773  -180.079 54.070  1.00 92.61  ? 84  GLU   b CB  1 
ATOM   48392 C  CG  . GLU   BA 14 84  ? 40.510  -180.815 52.967  1.00 98.27  ? 84  GLU   b CG  1 
ATOM   48393 C  CD  . GLU   BA 14 84  ? 42.027  -180.780 53.073  1.00 99.77  ? 84  GLU   b CD  1 
ATOM   48394 O  OE1 . GLU   BA 14 84  ? 42.682  -181.507 52.301  1.00 109.48 ? 84  GLU   b OE1 1 
ATOM   48395 O  OE2 . GLU   BA 14 84  ? 42.553  -180.031 53.924  1.00 95.88  ? 84  GLU   b OE2 1 
ATOM   48396 N  N   . LEU   BA 14 85  ? 37.577  -177.903 53.315  1.00 85.23  ? 85  LEU   b N   1 
ATOM   48397 C  CA  . LEU   BA 14 85  ? 36.483  -177.387 52.450  1.00 85.97  ? 85  LEU   b CA  1 
ATOM   48398 C  C   . LEU   BA 14 85  ? 36.713  -175.894 52.188  1.00 88.18  ? 85  LEU   b C   1 
ATOM   48399 O  O   . LEU   BA 14 85  ? 36.686  -175.498 51.003  1.00 91.14  ? 85  LEU   b O   1 
ATOM   48400 C  CB  . LEU   BA 14 85  ? 35.128  -177.630 53.125  1.00 84.74  ? 85  LEU   b CB  1 
ATOM   48401 C  CG  . LEU   BA 14 85  ? 34.734  -179.095 53.315  1.00 84.12  ? 85  LEU   b CG  1 
ATOM   48402 C  CD1 . LEU   BA 14 85  ? 33.527  -179.220 54.232  1.00 85.06  ? 85  LEU   b CD1 1 
ATOM   48403 C  CD2 . LEU   BA 14 85  ? 34.456  -179.767 51.980  1.00 84.78  ? 85  LEU   b CD2 1 
ATOM   48404 N  N   . CYS   BA 14 86  ? 36.944  -175.109 53.249  1.00 85.61  ? 86  CYS   b N   1 
ATOM   48405 C  CA  . CYS   BA 14 86  ? 37.076  -173.626 53.201  1.00 83.06  ? 86  CYS   b CA  1 
ATOM   48406 C  C   . CYS   BA 14 86  ? 38.315  -173.222 52.394  1.00 78.72  ? 86  CYS   b C   1 
ATOM   48407 O  O   . CYS   BA 14 86  ? 38.198  -172.292 51.583  1.00 79.39  ? 86  CYS   b O   1 
ATOM   48408 C  CB  . CYS   BA 14 86  ? 37.113  -173.031 54.603  1.00 81.50  ? 86  CYS   b CB  1 
ATOM   48409 S  SG  . CYS   BA 14 86  ? 35.536  -173.222 55.472  1.00 84.13  ? 86  CYS   b SG  1 
ATOM   48410 N  N   . TYR   BA 14 87  ? 39.445  -173.908 52.583  1.00 78.99  ? 87  TYR   b N   1 
ATOM   48411 C  CA  . TYR   BA 14 87  ? 40.746  -173.573 51.945  1.00 78.96  ? 87  TYR   b CA  1 
ATOM   48412 C  C   . TYR   BA 14 87  ? 40.714  -173.918 50.451  1.00 82.34  ? 87  TYR   b C   1 
ATOM   48413 O  O   . TYR   BA 14 87  ? 41.164  -173.092 49.644  1.00 81.29  ? 87  TYR   b O   1 
ATOM   48414 C  CB  . TYR   BA 14 87  ? 41.909  -174.307 52.615  1.00 78.04  ? 87  TYR   b CB  1 
ATOM   48415 C  CG  . TYR   BA 14 87  ? 43.241  -174.067 51.953  1.00 77.47  ? 87  TYR   b CG  1 
ATOM   48416 C  CD1 . TYR   BA 14 87  ? 43.862  -172.834 52.034  1.00 77.01  ? 87  TYR   b CD1 1 
ATOM   48417 C  CD2 . TYR   BA 14 87  ? 43.878  -175.062 51.231  1.00 79.38  ? 87  TYR   b CD2 1 
ATOM   48418 C  CE1 . TYR   BA 14 87  ? 45.084  -172.597 51.425  1.00 78.66  ? 87  TYR   b CE1 1 
ATOM   48419 C  CE2 . TYR   BA 14 87  ? 45.101  -174.844 50.617  1.00 80.06  ? 87  TYR   b CE2 1 
ATOM   48420 C  CZ  . TYR   BA 14 87  ? 45.708  -173.606 50.716  1.00 78.85  ? 87  TYR   b CZ  1 
ATOM   48421 O  OH  . TYR   BA 14 87  ? 46.913  -173.383 50.115  1.00 78.46  ? 87  TYR   b OH  1 
ATOM   48422 N  N   . GLU   BA 14 88  ? 40.235  -175.114 50.098  1.00 85.97  ? 88  GLU   b N   1 
ATOM   48423 C  CA  . GLU   BA 14 88  ? 40.267  -175.636 48.703  1.00 90.64  ? 88  GLU   b CA  1 
ATOM   48424 C  C   . GLU   BA 14 88  ? 39.193  -174.955 47.844  1.00 91.55  ? 88  GLU   b C   1 
ATOM   48425 O  O   . GLU   BA 14 88  ? 39.307  -175.048 46.608  1.00 93.14  ? 88  GLU   b O   1 
ATOM   48426 C  CB  . GLU   BA 14 88  ? 40.080  -177.155 48.675  1.00 92.66  ? 88  GLU   b CB  1 
ATOM   48427 C  CG  . GLU   BA 14 88  ? 41.248  -177.931 49.262  1.00 96.32  ? 88  GLU   b CG  1 
ATOM   48428 C  CD  . GLU   BA 14 88  ? 42.579  -177.753 48.546  1.00 100.36 ? 88  GLU   b CD  1 
ATOM   48429 O  OE1 . GLU   BA 14 88  ? 42.567  -177.406 47.347  1.00 101.58 ? 88  GLU   b OE1 1 
ATOM   48430 O  OE2 . GLU   BA 14 88  ? 43.627  -177.962 49.193  1.00 103.61 ? 88  GLU   b OE2 1 
ATOM   48431 N  N   . ASN   BA 14 89  ? 38.193  -174.313 48.460  1.00 92.26  ? 89  ASN   b N   1 
ATOM   48432 C  CA  . ASN   BA 14 89  ? 37.084  -173.618 47.748  1.00 91.08  ? 89  ASN   b CA  1 
ATOM   48433 C  C   . ASN   BA 14 89  ? 37.042  -172.138 48.143  1.00 91.82  ? 89  ASN   b C   1 
ATOM   48434 O  O   . ASN   BA 14 89  ? 35.940  -171.557 48.123  1.00 91.99  ? 89  ASN   b O   1 
ATOM   48435 C  CB  . ASN   BA 14 89  ? 35.744  -174.297 48.026  1.00 90.69  ? 89  ASN   b CB  1 
ATOM   48436 C  CG  . ASN   BA 14 89  ? 35.719  -175.719 47.515  1.00 91.03  ? 89  ASN   b CG  1 
ATOM   48437 O  OD1 . ASN   BA 14 89  ? 35.865  -175.948 46.318  1.00 91.59  ? 89  ASN   b OD1 1 
ATOM   48438 N  ND2 . ASN   BA 14 89  ? 35.553  -176.677 48.411  1.00 91.35  ? 89  ASN   b ND2 1 
ATOM   48439 N  N   . LYS   BA 14 90  ? 38.199  -171.549 48.459  1.00 92.78  ? 90  LYS   b N   1 
ATOM   48440 C  CA  . LYS   BA 14 90  ? 38.313  -170.164 48.995  1.00 92.46  ? 90  LYS   b CA  1 
ATOM   48441 C  C   . LYS   BA 14 90  ? 37.750  -169.159 47.977  1.00 91.76  ? 90  LYS   b C   1 
ATOM   48442 O  O   . LYS   BA 14 90  ? 37.209  -168.126 48.415  1.00 92.23  ? 90  LYS   b O   1 
ATOM   48443 C  CB  . LYS   BA 14 90  ? 39.764  -169.845 49.378  1.00 90.65  ? 90  LYS   b CB  1 
ATOM   48444 C  CG  . LYS   BA 14 90  ? 40.806  -170.015 48.278  1.00 92.27  ? 90  LYS   b CG  1 
ATOM   48445 C  CD  . LYS   BA 14 90  ? 42.130  -169.350 48.597  1.00 92.79  ? 90  LYS   b CD  1 
ATOM   48446 C  CE  . LYS   BA 14 90  ? 42.868  -169.995 49.751  1.00 92.68  ? 90  LYS   b CE  1 
ATOM   48447 N  NZ  . LYS   BA 14 90  ? 44.032  -169.183 50.178  1.00 94.92  ? 90  LYS   b NZ  1 
ATOM   48448 N  N   . ASP   BA 14 91  ? 37.849  -169.458 46.678  1.00 94.32  ? 91  ASP   b N   1 
ATOM   48449 C  CA  . ASP   BA 14 91  ? 37.426  -168.549 45.578  1.00 95.05  ? 91  ASP   b CA  1 
ATOM   48450 C  C   . ASP   BA 14 91  ? 35.896  -168.486 45.473  1.00 95.34  ? 91  ASP   b C   1 
ATOM   48451 O  O   . ASP   BA 14 91  ? 35.403  -167.537 44.832  1.00 97.62  ? 91  ASP   b O   1 
ATOM   48452 C  CB  . ASP   BA 14 91  ? 38.022  -168.979 44.235  1.00 99.41  ? 91  ASP   b CB  1 
ATOM   48453 C  CG  . ASP   BA 14 91  ? 39.542  -168.956 44.184  1.00 102.90 ? 91  ASP   b CG  1 
ATOM   48454 O  OD1 . ASP   BA 14 91  ? 40.160  -168.408 45.124  1.00 102.39 ? 91  ASP   b OD1 1 
ATOM   48455 O  OD2 . ASP   BA 14 91  ? 40.098  -169.487 43.201  1.00 107.37 ? 91  ASP   b OD2 1 
ATOM   48456 N  N   . ASN   BA 14 92  ? 35.173  -169.446 46.060  1.00 93.62  ? 92  ASN   b N   1 
ATOM   48457 C  CA  . ASN   BA 14 92  ? 33.702  -169.592 45.884  1.00 95.47  ? 92  ASN   b CA  1 
ATOM   48458 C  C   . ASN   BA 14 92  ? 32.987  -169.670 47.236  1.00 92.68  ? 92  ASN   b C   1 
ATOM   48459 O  O   . ASN   BA 14 92  ? 31.861  -170.202 47.259  1.00 99.18  ? 92  ASN   b O   1 
ATOM   48460 C  CB  . ASN   BA 14 92  ? 33.371  -170.829 45.048  1.00 98.90  ? 92  ASN   b CB  1 
ATOM   48461 C  CG  . ASN   BA 14 92  ? 34.142  -170.869 43.748  1.00 104.97 ? 92  ASN   b CG  1 
ATOM   48462 O  OD1 . ASN   BA 14 92  ? 34.080  -169.925 42.961  1.00 106.73 ? 92  ASN   b OD1 1 
ATOM   48463 N  ND2 . ASN   BA 14 92  ? 34.874  -171.947 43.515  1.00 108.41 ? 92  ASN   b ND2 1 
ATOM   48464 N  N   . LEU   BA 14 93  ? 33.584  -169.145 48.311  1.00 90.87  ? 93  LEU   b N   1 
ATOM   48465 C  CA  . LEU   BA 14 93  ? 32.991  -169.207 49.675  1.00 88.71  ? 93  LEU   b CA  1 
ATOM   48466 C  C   . LEU   BA 14 93  ? 33.130  -167.857 50.383  1.00 86.32  ? 93  LEU   b C   1 
ATOM   48467 O  O   . LEU   BA 14 93  ? 34.171  -167.198 50.220  1.00 88.80  ? 93  LEU   b O   1 
ATOM   48468 C  CB  . LEU   BA 14 93  ? 33.677  -170.314 50.483  1.00 89.41  ? 93  LEU   b CB  1 
ATOM   48469 C  CG  . LEU   BA 14 93  ? 33.310  -171.750 50.106  1.00 88.70  ? 93  LEU   b CG  1 
ATOM   48470 C  CD1 . LEU   BA 14 93  ? 34.145  -172.737 50.908  1.00 90.11  ? 93  LEU   b CD1 1 
ATOM   48471 C  CD2 . LEU   BA 14 93  ? 31.828  -172.022 50.321  1.00 85.84  ? 93  LEU   b CD2 1 
ATOM   48472 N  N   . THR   BA 14 94  ? 32.089  -167.481 51.129  1.00 85.43  ? 94  THR   b N   1 
ATOM   48473 C  CA  . THR   BA 14 94  ? 32.084  -166.386 52.130  1.00 84.35  ? 94  THR   b CA  1 
ATOM   48474 C  C   . THR   BA 14 94  ? 31.624  -166.996 53.452  1.00 83.63  ? 94  THR   b C   1 
ATOM   48475 O  O   . THR   BA 14 94  ? 30.424  -166.884 53.763  1.00 82.16  ? 94  THR   b O   1 
ATOM   48476 C  CB  . THR   BA 14 94  ? 31.208  -165.213 51.676  1.00 86.16  ? 94  THR   b CB  1 
ATOM   48477 O  OG1 . THR   BA 14 94  ? 31.612  -164.869 50.350  1.00 87.28  ? 94  THR   b OG1 1 
ATOM   48478 C  CG2 . THR   BA 14 94  ? 31.325  -164.008 52.586  1.00 87.18  ? 94  THR   b CG2 1 
ATOM   48479 N  N   . ALA   BA 14 95  ? 32.543  -167.658 54.159  1.00 83.77  ? 95  ALA   b N   1 
ATOM   48480 C  CA  . ALA   BA 14 95  ? 32.275  -168.416 55.402  1.00 84.28  ? 95  ALA   b CA  1 
ATOM   48481 C  C   . ALA   BA 14 95  ? 33.389  -168.150 56.420  1.00 82.67  ? 95  ALA   b C   1 
ATOM   48482 O  O   . ALA   BA 14 95  ? 34.564  -168.446 56.120  1.00 84.88  ? 95  ALA   b O   1 
ATOM   48483 C  CB  . ALA   BA 14 95  ? 32.139  -169.888 55.092  1.00 84.41  ? 95  ALA   b CB  1 
ATOM   48484 N  N   . GLY   BA 14 96  ? 33.018  -167.579 57.566  1.00 83.08  ? 96  GLY   b N   1 
ATOM   48485 C  CA  . GLY   BA 14 96  ? 33.861  -167.479 58.769  1.00 83.11  ? 96  GLY   b CA  1 
ATOM   48486 C  C   . GLY   BA 14 96  ? 33.287  -168.354 59.864  1.00 82.94  ? 96  GLY   b C   1 
ATOM   48487 O  O   . GLY   BA 14 96  ? 32.232  -167.996 60.418  1.00 85.08  ? 96  GLY   b O   1 
ATOM   48488 N  N   . ILE   BA 14 97  ? 33.923  -169.489 60.139  1.00 81.68  ? 97  ILE   b N   1 
ATOM   48489 C  CA  . ILE   BA 14 97  ? 33.375  -170.519 61.065  1.00 84.04  ? 97  ILE   b CA  1 
ATOM   48490 C  C   . ILE   BA 14 97  ? 34.286  -170.616 62.290  1.00 82.26  ? 97  ILE   b C   1 
ATOM   48491 O  O   . ILE   BA 14 97  ? 35.518  -170.663 62.110  1.00 80.34  ? 97  ILE   b O   1 
ATOM   48492 C  CB  . ILE   BA 14 97  ? 33.210  -171.867 60.335  1.00 84.05  ? 97  ILE   b CB  1 
ATOM   48493 C  CG1 . ILE   BA 14 97  ? 32.257  -171.739 59.144  1.00 85.27  ? 97  ILE   b CG1 1 
ATOM   48494 C  CG2 . ILE   BA 14 97  ? 32.756  -172.958 61.293  1.00 86.21  ? 97  ILE   b CG2 1 
ATOM   48495 C  CD1 . ILE   BA 14 97  ? 32.448  -172.800 58.091  1.00 85.86  ? 97  ILE   b CD1 1 
ATOM   48496 N  N   . ILE   BA 14 98  ? 33.688  -170.611 63.483  1.00 84.69  ? 98  ILE   b N   1 
ATOM   48497 C  CA  . ILE   BA 14 98  ? 34.352  -170.999 64.762  1.00 90.68  ? 98  ILE   b CA  1 
ATOM   48498 C  C   . ILE   BA 14 98  ? 33.901  -172.423 65.096  1.00 91.30  ? 98  ILE   b C   1 
ATOM   48499 O  O   . ILE   BA 14 98  ? 32.681  -172.640 65.192  1.00 96.07  ? 98  ILE   b O   1 
ATOM   48500 C  CB  . ILE   BA 14 98  ? 34.023  -170.021 65.907  1.00 92.96  ? 98  ILE   b CB  1 
ATOM   48501 C  CG1 . ILE   BA 14 98  ? 34.319  -168.567 65.527  1.00 94.01  ? 98  ILE   b CG1 1 
ATOM   48502 C  CG2 . ILE   BA 14 98  ? 34.751  -170.435 67.179  1.00 95.83  ? 98  ILE   b CG2 1 
ATOM   48503 C  CD1 . ILE   BA 14 98  ? 33.815  -167.548 66.530  1.00 93.65  ? 98  ILE   b CD1 1 
ATOM   48504 N  N   . VAL   BA 14 99  ? 34.854  -173.344 65.258  1.00 90.55  ? 99  VAL   b N   1 
ATOM   48505 C  CA  . VAL   BA 14 99  ? 34.612  -174.767 65.641  1.00 89.71  ? 99  VAL   b CA  1 
ATOM   48506 C  C   . VAL   BA 14 99  ? 34.932  -174.920 67.130  1.00 89.06  ? 99  VAL   b C   1 
ATOM   48507 O  O   . VAL   BA 14 99  ? 36.013  -174.464 67.545  1.00 89.10  ? 99  VAL   b O   1 
ATOM   48508 C  CB  . VAL   BA 14 99  ? 35.468  -175.729 64.798  1.00 88.59  ? 99  VAL   b CB  1 
ATOM   48509 C  CG1 . VAL   BA 14 99  ? 35.052  -177.172 65.018  1.00 90.54  ? 99  VAL   b CG1 1 
ATOM   48510 C  CG2 . VAL   BA 14 99  ? 35.428  -175.380 63.319  1.00 89.03  ? 99  VAL   b CG2 1 
ATOM   48511 N  N   . ALA   BA 14 100 ? 34.037  -175.552 67.893  1.00 88.05  ? 100 ALA   b N   1 
ATOM   48512 C  CA  . ALA   BA 14 100 ? 34.160  -175.718 69.360  1.00 92.14  ? 100 ALA   b CA  1 
ATOM   48513 C  C   . ALA   BA 14 100 ? 33.612  -177.085 69.781  1.00 92.63  ? 100 ALA   b C   1 
ATOM   48514 O  O   . ALA   BA 14 100 ? 32.445  -177.377 69.457  1.00 93.19  ? 100 ALA   b O   1 
ATOM   48515 C  CB  . ALA   BA 14 100 ? 33.440  -174.595 70.061  1.00 93.48  ? 100 ALA   b CB  1 
ATOM   48516 N  N   . GLY   BA 14 101 ? 34.424  -177.875 70.494  1.00 95.56  ? 101 GLY   b N   1 
ATOM   48517 C  CA  . GLY   BA 14 101 ? 34.087  -179.253 70.901  1.00 98.36  ? 101 GLY   b CA  1 
ATOM   48518 C  C   . GLY   BA 14 101 ? 34.606  -179.596 72.287  1.00 102.92 ? 101 GLY   b C   1 
ATOM   48519 O  O   . GLY   BA 14 101 ? 35.507  -178.884 72.777  1.00 104.83 ? 101 GLY   b O   1 
ATOM   48520 N  N   . TYR   BA 14 102 ? 34.055  -180.654 72.893  1.00 107.22 ? 102 TYR   b N   1 
ATOM   48521 C  CA  . TYR   BA 14 102 ? 34.480  -181.205 74.206  1.00 110.80 ? 102 TYR   b CA  1 
ATOM   48522 C  C   . TYR   BA 14 102 ? 34.958  -182.654 74.043  1.00 113.87 ? 102 TYR   b C   1 
ATOM   48523 O  O   . TYR   BA 14 102 ? 34.135  -183.540 73.731  1.00 113.43 ? 102 TYR   b O   1 
ATOM   48524 C  CB  . TYR   BA 14 102 ? 33.356  -181.141 75.244  1.00 108.97 ? 102 TYR   b CB  1 
ATOM   48525 C  CG  . TYR   BA 14 102 ? 33.769  -181.658 76.599  1.00 108.35 ? 102 TYR   b CG  1 
ATOM   48526 C  CD1 . TYR   BA 14 102 ? 34.517  -180.874 77.463  1.00 106.34 ? 102 TYR   b CD1 1 
ATOM   48527 C  CD2 . TYR   BA 14 102 ? 33.457  -182.947 77.003  1.00 110.26 ? 102 TYR   b CD2 1 
ATOM   48528 C  CE1 . TYR   BA 14 102 ? 34.923  -181.346 78.701  1.00 107.43 ? 102 TYR   b CE1 1 
ATOM   48529 C  CE2 . TYR   BA 14 102 ? 33.854  -183.435 78.237  1.00 110.24 ? 102 TYR   b CE2 1 
ATOM   48530 C  CZ  . TYR   BA 14 102 ? 34.589  -182.631 79.090  1.00 107.35 ? 102 TYR   b CZ  1 
ATOM   48531 O  OH  . TYR   BA 14 102 ? 34.985  -183.101 80.306  1.00 111.44 ? 102 TYR   b OH  1 
ATOM   48532 N  N   . ASP   BA 14 103 ? 36.262  -182.868 74.249  1.00 124.11 ? 103 ASP   b N   1 
ATOM   48533 C  CA  . ASP   BA 14 103 ? 36.887  -184.190 74.522  1.00 124.90 ? 103 ASP   b CA  1 
ATOM   48534 C  C   . ASP   BA 14 103 ? 36.933  -184.385 76.039  1.00 123.23 ? 103 ASP   b C   1 
ATOM   48535 O  O   . ASP   BA 14 103 ? 36.740  -183.392 76.767  1.00 118.86 ? 103 ASP   b O   1 
ATOM   48536 C  CB  . ASP   BA 14 103 ? 38.300  -184.275 73.942  1.00 131.80 ? 103 ASP   b CB  1 
ATOM   48537 C  CG  . ASP   BA 14 103 ? 38.348  -184.403 72.429  1.00 137.03 ? 103 ASP   b CG  1 
ATOM   48538 O  OD1 . ASP   BA 14 103 ? 38.103  -185.518 71.931  1.00 139.83 ? 103 ASP   b OD1 1 
ATOM   48539 O  OD2 . ASP   BA 14 103 ? 38.634  -183.383 71.762  1.00 141.37 ? 103 ASP   b OD2 1 
ATOM   48540 N  N   . ASP   BA 14 104 ? 37.181  -185.612 76.496  1.00 123.44 ? 104 ASP   b N   1 
ATOM   48541 C  CA  . ASP   BA 14 104 ? 37.429  -185.914 77.931  1.00 126.29 ? 104 ASP   b CA  1 
ATOM   48542 C  C   . ASP   BA 14 104 ? 38.937  -185.803 78.190  1.00 124.48 ? 104 ASP   b C   1 
ATOM   48543 O  O   . ASP   BA 14 104 ? 39.312  -185.393 79.304  1.00 120.27 ? 104 ASP   b O   1 
ATOM   48544 C  CB  . ASP   BA 14 104 ? 36.842  -187.273 78.319  1.00 130.32 ? 104 ASP   b CB  1 
ATOM   48545 C  CG  . ASP   BA 14 104 ? 36.173  -187.269 79.682  1.00 137.76 ? 104 ASP   b CG  1 
ATOM   48546 O  OD1 . ASP   BA 14 104 ? 36.904  -187.235 80.693  1.00 147.03 ? 104 ASP   b OD1 1 
ATOM   48547 O  OD2 . ASP   BA 14 104 ? 34.925  -187.277 79.720  1.00 135.83 ? 104 ASP   b OD2 1 
ATOM   48548 N  N   . LYS   BA 14 105 ? 39.759  -186.131 77.186  1.00 127.42 ? 105 LYS   b N   1 
ATOM   48549 C  CA  . LYS   BA 14 105 ? 41.243  -186.019 77.233  1.00 129.93 ? 105 LYS   b CA  1 
ATOM   48550 C  C   . LYS   BA 14 105 ? 41.650  -184.545 77.105  1.00 128.50 ? 105 LYS   b C   1 
ATOM   48551 O  O   . LYS   BA 14 105 ? 42.444  -184.083 77.946  1.00 132.54 ? 105 LYS   b O   1 
ATOM   48552 C  CB  . LYS   BA 14 105 ? 41.878  -186.868 76.125  1.00 136.26 ? 105 LYS   b CB  1 
ATOM   48553 C  CG  . LYS   BA 14 105 ? 43.397  -186.788 76.020  1.00 141.57 ? 105 LYS   b CG  1 
ATOM   48554 C  CD  . LYS   BA 14 105 ? 43.981  -187.771 75.023  1.00 147.19 ? 105 LYS   b CD  1 
ATOM   48555 C  CE  . LYS   BA 14 105 ? 44.202  -189.155 75.600  1.00 149.07 ? 105 LYS   b CE  1 
ATOM   48556 N  NZ  . LYS   BA 14 105 ? 43.632  -190.210 74.728  1.00 150.76 ? 105 LYS   b NZ  1 
ATOM   48557 N  N   . ASN   BA 14 106 ? 41.117  -183.844 76.097  1.00 123.28 ? 106 ASN   b N   1 
ATOM   48558 C  CA  . ASN   BA 14 106 ? 41.552  -182.479 75.687  1.00 117.37 ? 106 ASN   b CA  1 
ATOM   48559 C  C   . ASN   BA 14 106 ? 40.659  -181.394 76.306  1.00 112.08 ? 106 ASN   b C   1 
ATOM   48560 O  O   . ASN   BA 14 106 ? 41.042  -180.212 76.199  1.00 105.33 ? 106 ASN   b O   1 
ATOM   48561 C  CB  . ASN   BA 14 106 ? 41.577  -182.340 74.163  1.00 119.28 ? 106 ASN   b CB  1 
ATOM   48562 C  CG  . ASN   BA 14 106 ? 42.572  -183.274 73.507  1.00 120.79 ? 106 ASN   b CG  1 
ATOM   48563 O  OD1 . ASN   BA 14 106 ? 43.780  -183.117 73.674  1.00 124.28 ? 106 ASN   b OD1 1 
ATOM   48564 N  ND2 . ASN   BA 14 106 ? 42.081  -184.248 72.758  1.00 120.83 ? 106 ASN   b ND2 1 
ATOM   48565 N  N   . LYS   BA 14 107 ? 39.528  -181.767 76.918  1.00 110.91 ? 107 LYS   b N   1 
ATOM   48566 C  CA  . LYS   BA 14 107 ? 38.543  -180.831 77.530  1.00 110.51 ? 107 LYS   b CA  1 
ATOM   48567 C  C   . LYS   BA 14 107 ? 37.995  -179.902 76.435  1.00 111.10 ? 107 LYS   b C   1 
ATOM   48568 O  O   . LYS   BA 14 107 ? 37.759  -180.402 75.311  1.00 106.55 ? 107 LYS   b O   1 
ATOM   48569 C  CB  . LYS   BA 14 107 ? 39.188  -180.076 78.699  1.00 110.52 ? 107 LYS   b CB  1 
ATOM   48570 C  CG  . LYS   BA 14 107 ? 39.699  -180.956 79.829  1.00 111.40 ? 107 LYS   b CG  1 
ATOM   48571 C  CD  . LYS   BA 14 107 ? 38.586  -181.515 80.684  1.00 115.80 ? 107 LYS   b CD  1 
ATOM   48572 C  CE  . LYS   BA 14 107 ? 39.008  -182.720 81.496  1.00 117.93 ? 107 LYS   b CE  1 
ATOM   48573 N  NZ  . LYS   BA 14 107 ? 37.864  -183.306 82.234  1.00 120.82 ? 107 LYS   b NZ  1 
ATOM   48574 N  N   . GLY   BA 14 108 ? 37.794  -178.614 76.744  1.00 108.43 ? 108 GLY   b N   1 
ATOM   48575 C  CA  . GLY   BA 14 108 ? 37.285  -177.598 75.802  1.00 103.25 ? 108 GLY   b CA  1 
ATOM   48576 C  C   . GLY   BA 14 108 ? 38.363  -177.153 74.829  1.00 99.16  ? 108 GLY   b C   1 
ATOM   48577 O  O   . GLY   BA 14 108 ? 39.520  -176.980 75.262  1.00 100.21 ? 108 GLY   b O   1 
ATOM   48578 N  N   . GLU   BA 14 109 ? 37.999  -176.981 73.557  1.00 97.61  ? 109 GLU   b N   1 
ATOM   48579 C  CA  . GLU   BA 14 109 ? 38.916  -176.526 72.480  1.00 97.23  ? 109 GLU   b CA  1 
ATOM   48580 C  C   . GLU   BA 14 109 ? 38.139  -175.630 71.513  1.00 94.10  ? 109 GLU   b C   1 
ATOM   48581 O  O   . GLU   BA 14 109 ? 36.988  -175.982 71.183  1.00 93.35  ? 109 GLU   b O   1 
ATOM   48582 C  CB  . GLU   BA 14 109 ? 39.529  -177.723 71.751  1.00 99.05  ? 109 GLU   b CB  1 
ATOM   48583 C  CG  . GLU   BA 14 109 ? 40.790  -178.253 72.411  1.00 103.29 ? 109 GLU   b CG  1 
ATOM   48584 C  CD  . GLU   BA 14 109 ? 41.492  -179.366 71.649  1.00 106.27 ? 109 GLU   b CD  1 
ATOM   48585 O  OE1 . GLU   BA 14 109 ? 40.938  -179.830 70.633  1.00 110.72 ? 109 GLU   b OE1 1 
ATOM   48586 O  OE2 . GLU   BA 14 109 ? 42.593  -179.767 72.075  1.00 109.35 ? 109 GLU   b OE2 1 
ATOM   48587 N  N   . VAL   BA 14 110 ? 38.751  -174.518 71.097  1.00 90.72  ? 110 VAL   b N   1 
ATOM   48588 C  CA  . VAL   BA 14 110 ? 38.190  -173.581 70.081  1.00 88.45  ? 110 VAL   b CA  1 
ATOM   48589 C  C   . VAL   BA 14 110 ? 39.197  -173.441 68.937  1.00 86.60  ? 110 VAL   b C   1 
ATOM   48590 O  O   . VAL   BA 14 110 ? 40.394  -173.221 69.218  1.00 82.43  ? 110 VAL   b O   1 
ATOM   48591 C  CB  . VAL   BA 14 110 ? 37.830  -172.218 70.699  1.00 88.88  ? 110 VAL   b CB  1 
ATOM   48592 C  CG1 . VAL   BA 14 110 ? 37.547  -171.165 69.636  1.00 90.13  ? 110 VAL   b CG1 1 
ATOM   48593 C  CG2 . VAL   BA 14 110 ? 36.652  -172.338 71.652  1.00 89.11  ? 110 VAL   b CG2 1 
ATOM   48594 N  N   . TYR   BA 14 111 ? 38.702  -173.585 67.704  1.00 88.69  ? 111 TYR   b N   1 
ATOM   48595 C  CA  . TYR   BA 14 111 ? 39.413  -173.308 66.429  1.00 88.39  ? 111 TYR   b CA  1 
ATOM   48596 C  C   . TYR   BA 14 111 ? 38.596  -172.284 65.633  1.00 85.35  ? 111 TYR   b C   1 
ATOM   48597 O  O   . TYR   BA 14 111 ? 37.381  -172.494 65.452  1.00 87.79  ? 111 TYR   b O   1 
ATOM   48598 C  CB  . TYR   BA 14 111 ? 39.601  -174.598 65.624  1.00 89.14  ? 111 TYR   b CB  1 
ATOM   48599 C  CG  . TYR   BA 14 111 ? 40.408  -175.669 66.313  1.00 88.19  ? 111 TYR   b CG  1 
ATOM   48600 C  CD1 . TYR   BA 14 111 ? 39.810  -176.573 67.175  1.00 89.13  ? 111 TYR   b CD1 1 
ATOM   48601 C  CD2 . TYR   BA 14 111 ? 41.773  -175.785 66.099  1.00 87.04  ? 111 TYR   b CD2 1 
ATOM   48602 C  CE1 . TYR   BA 14 111 ? 40.545  -177.561 67.812  1.00 89.71  ? 111 TYR   b CE1 1 
ATOM   48603 C  CE2 . TYR   BA 14 111 ? 42.523  -176.769 66.725  1.00 86.43  ? 111 TYR   b CE2 1 
ATOM   48604 C  CZ  . TYR   BA 14 111 ? 41.909  -177.660 67.586  1.00 85.82  ? 111 TYR   b CZ  1 
ATOM   48605 O  OH  . TYR   BA 14 111 ? 42.654  -178.621 68.206  1.00 87.66  ? 111 TYR   b OH  1 
ATOM   48606 N  N   . THR   BA 14 112 ? 39.232  -171.201 65.185  1.00 82.59  ? 112 THR   b N   1 
ATOM   48607 C  CA  . THR   BA 14 112 ? 38.607  -170.192 64.291  1.00 82.12  ? 112 THR   b CA  1 
ATOM   48608 C  C   . THR   BA 14 112 ? 39.178  -170.383 62.884  1.00 81.35  ? 112 THR   b C   1 
ATOM   48609 O  O   . THR   BA 14 112 ? 40.394  -170.634 62.762  1.00 82.29  ? 112 THR   b O   1 
ATOM   48610 C  CB  . THR   BA 14 112 ? 38.765  -168.766 64.837  1.00 80.78  ? 112 THR   b CB  1 
ATOM   48611 O  OG1 . THR   BA 14 112 ? 37.930  -167.922 64.048  1.00 81.44  ? 112 THR   b OG1 1 
ATOM   48612 C  CG2 . THR   BA 14 112 ? 40.185  -168.244 64.809  1.00 82.14  ? 112 THR   b CG2 1 
ATOM   48613 N  N   . ILE   BA 14 113 ? 38.310  -170.303 61.874  1.00 80.30  ? 113 ILE   b N   1 
ATOM   48614 C  CA  . ILE   BA 14 113 ? 38.661  -170.453 60.433  1.00 84.14  ? 113 ILE   b CA  1 
ATOM   48615 C  C   . ILE   BA 14 113 ? 38.135  -169.225 59.692  1.00 84.74  ? 113 ILE   b C   1 
ATOM   48616 O  O   . ILE   BA 14 113 ? 36.945  -169.141 59.394  1.00 85.86  ? 113 ILE   b O   1 
ATOM   48617 C  CB  . ILE   BA 14 113 ? 38.105  -171.778 59.876  1.00 85.56  ? 113 ILE   b CB  1 
ATOM   48618 C  CG1 . ILE   BA 14 113 ? 38.585  -172.973 60.706  1.00 89.27  ? 113 ILE   b CG1 1 
ATOM   48619 C  CG2 . ILE   BA 14 113 ? 38.455  -171.937 58.404  1.00 85.62  ? 113 ILE   b CG2 1 
ATOM   48620 C  CD1 . ILE   BA 14 113 ? 37.849  -174.263 60.426  1.00 91.35  ? 113 ILE   b CD1 1 
ATOM   48621 N  N   . PRO   BA 14 114 ? 39.001  -168.226 59.395  1.00 85.48  ? 114 PRO   b N   1 
ATOM   48622 C  CA  . PRO   BA 14 114 ? 38.581  -167.019 58.684  1.00 86.54  ? 114 PRO   b CA  1 
ATOM   48623 C  C   . PRO   BA 14 114 ? 38.308  -167.282 57.194  1.00 88.41  ? 114 PRO   b C   1 
ATOM   48624 O  O   . PRO   BA 14 114 ? 38.234  -168.433 56.806  1.00 89.49  ? 114 PRO   b O   1 
ATOM   48625 C  CB  . PRO   BA 14 114 ? 39.763  -166.047 58.857  1.00 88.38  ? 114 PRO   b CB  1 
ATOM   48626 C  CG  . PRO   BA 14 114 ? 40.691  -166.708 59.860  1.00 86.96  ? 114 PRO   b CG  1 
ATOM   48627 C  CD  . PRO   BA 14 114 ? 40.428  -168.191 59.739  1.00 86.80  ? 114 PRO   b CD  1 
ATOM   48628 N  N   . LEU   BA 14 115 ? 38.168  -166.214 56.404  1.00 88.47  ? 115 LEU   b N   1 
ATOM   48629 C  CA  . LEU   BA 14 115 ? 37.818  -166.275 54.958  1.00 89.15  ? 115 LEU   b CA  1 
ATOM   48630 C  C   . LEU   BA 14 115 ? 38.844  -167.130 54.199  1.00 92.32  ? 115 LEU   b C   1 
ATOM   48631 O  O   . LEU   BA 14 115 ? 38.406  -167.979 53.391  1.00 95.43  ? 115 LEU   b O   1 
ATOM   48632 C  CB  . LEU   BA 14 115 ? 37.731  -164.853 54.386  1.00 88.97  ? 115 LEU   b CB  1 
ATOM   48633 C  CG  . LEU   BA 14 115 ? 36.321  -164.299 54.161  1.00 88.86  ? 115 LEU   b CG  1 
ATOM   48634 C  CD1 . LEU   BA 14 115 ? 35.411  -164.548 55.359  1.00 91.41  ? 115 LEU   b CD1 1 
ATOM   48635 C  CD2 . LEU   BA 14 115 ? 36.374  -162.813 53.846  1.00 87.30  ? 115 LEU   b CD2 1 
ATOM   48636 N  N   . GLY   BA 14 116 ? 40.143  -166.947 54.464  1.00 87.13  ? 116 GLY   b N   1 
ATOM   48637 C  CA  . GLY   BA 14 116 ? 41.234  -167.599 53.708  1.00 91.95  ? 116 GLY   b CA  1 
ATOM   48638 C  C   . GLY   BA 14 116 ? 41.195  -169.122 53.787  1.00 92.29  ? 116 GLY   b C   1 
ATOM   48639 O  O   . GLY   BA 14 116 ? 41.631  -169.770 52.814  1.00 90.46  ? 116 GLY   b O   1 
ATOM   48640 N  N   . GLY   BA 14 117 ? 40.698  -169.678 54.899  1.00 92.96  ? 117 GLY   b N   1 
ATOM   48641 C  CA  . GLY   BA 14 117 ? 40.711  -171.124 55.196  1.00 89.50  ? 117 GLY   b CA  1 
ATOM   48642 C  C   . GLY   BA 14 117 ? 41.903  -171.524 56.054  1.00 89.10  ? 117 GLY   b C   1 
ATOM   48643 O  O   . GLY   BA 14 117 ? 42.205  -172.726 56.109  1.00 86.83  ? 117 GLY   b O   1 
ATOM   48644 N  N   . SER   BA 14 118 ? 42.562  -170.559 56.704  1.00 87.29  ? 118 SER   b N   1 
ATOM   48645 C  CA  . SER   BA 14 118 ? 43.609  -170.800 57.732  1.00 85.74  ? 118 SER   b CA  1 
ATOM   48646 C  C   . SER   BA 14 118 ? 42.934  -171.327 59.003  1.00 85.37  ? 118 SER   b C   1 
ATOM   48647 O  O   . SER   BA 14 118 ? 41.726  -171.078 59.171  1.00 85.18  ? 118 SER   b O   1 
ATOM   48648 C  CB  . SER   BA 14 118 ? 44.416  -169.550 58.006  1.00 85.73  ? 118 SER   b CB  1 
ATOM   48649 O  OG  . SER   BA 14 118 ? 43.571  -168.456 58.338  1.00 83.80  ? 118 SER   b OG  1 
ATOM   48650 N  N   . VAL   BA 14 119 ? 43.677  -172.040 59.852  1.00 83.90  ? 119 VAL   b N   1 
ATOM   48651 C  CA  . VAL   BA 14 119 ? 43.168  -172.570 61.152  1.00 85.04  ? 119 VAL   b CA  1 
ATOM   48652 C  C   . VAL   BA 14 119 ? 43.964  -171.930 62.284  1.00 86.38  ? 119 VAL   b C   1 
ATOM   48653 O  O   . VAL   BA 14 119 ? 45.204  -171.894 62.186  1.00 92.00  ? 119 VAL   b O   1 
ATOM   48654 C  CB  . VAL   BA 14 119 ? 43.261  -174.101 61.265  1.00 85.87  ? 119 VAL   b CB  1 
ATOM   48655 C  CG1 . VAL   BA 14 119 ? 42.060  -174.653 62.015  1.00 85.22  ? 119 VAL   b CG1 1 
ATOM   48656 C  CG2 . VAL   BA 14 119 ? 43.415  -174.775 59.914  1.00 87.51  ? 119 VAL   b CG2 1 
ATOM   48657 N  N   . HIS   BA 14 120 ? 43.264  -171.489 63.328  1.00 86.25  ? 120 HIS   b N   1 
ATOM   48658 C  CA  . HIS   BA 14 120 ? 43.856  -170.850 64.528  1.00 87.66  ? 120 HIS   b CA  1 
ATOM   48659 C  C   . HIS   BA 14 120 ? 43.189  -171.441 65.770  1.00 88.30  ? 120 HIS   b C   1 
ATOM   48660 O  O   . HIS   BA 14 120 ? 41.973  -171.233 65.941  1.00 92.17  ? 120 HIS   b O   1 
ATOM   48661 C  CB  . HIS   BA 14 120 ? 43.729  -169.325 64.424  1.00 88.11  ? 120 HIS   b CB  1 
ATOM   48662 C  CG  . HIS   BA 14 120 ? 44.236  -168.791 63.128  1.00 88.84  ? 120 HIS   b CG  1 
ATOM   48663 N  ND1 . HIS   BA 14 120 ? 45.580  -168.572 62.897  1.00 89.70  ? 120 HIS   b ND1 1 
ATOM   48664 C  CD2 . HIS   BA 14 120 ? 43.594  -168.470 61.984  1.00 89.82  ? 120 HIS   b CD2 1 
ATOM   48665 C  CE1 . HIS   BA 14 120 ? 45.743  -168.118 61.670  1.00 91.24  ? 120 HIS   b CE1 1 
ATOM   48666 N  NE2 . HIS   BA 14 120 ? 44.539  -168.047 61.088  1.00 91.51  ? 120 HIS   b NE2 1 
ATOM   48667 N  N   . LYS   BA 14 121 ? 43.958  -172.187 66.565  1.00 87.56  ? 121 LYS   b N   1 
ATOM   48668 C  CA  . LYS   BA 14 121 ? 43.525  -172.714 67.882  1.00 88.07  ? 121 LYS   b CA  1 
ATOM   48669 C  C   . LYS   BA 14 121 ? 43.747  -171.620 68.928  1.00 85.43  ? 121 LYS   b C   1 
ATOM   48670 O  O   . LYS   BA 14 121 ? 44.903  -171.181 69.062  1.00 90.10  ? 121 LYS   b O   1 
ATOM   48671 C  CB  . LYS   BA 14 121 ? 44.311  -173.977 68.237  1.00 86.74  ? 121 LYS   b CB  1 
ATOM   48672 C  CG  . LYS   BA 14 121 ? 43.793  -174.710 69.463  1.00 87.13  ? 121 LYS   b CG  1 
ATOM   48673 C  CD  . LYS   BA 14 121 ? 44.603  -175.925 69.829  1.00 85.62  ? 121 LYS   b CD  1 
ATOM   48674 C  CE  . LYS   BA 14 121 ? 44.026  -176.662 71.016  1.00 88.60  ? 121 LYS   b CE  1 
ATOM   48675 N  NZ  . LYS   BA 14 121 ? 43.877  -175.776 72.194  1.00 89.96  ? 121 LYS   b NZ  1 
ATOM   48676 N  N   . LEU   BA 14 122 ? 42.686  -171.195 69.622  1.00 85.93  ? 122 LEU   b N   1 
ATOM   48677 C  CA  . LEU   BA 14 122 ? 42.729  -170.075 70.603  1.00 85.33  ? 122 LEU   b CA  1 
ATOM   48678 C  C   . LEU   BA 14 122 ? 42.009  -170.475 71.889  1.00 86.52  ? 122 LEU   b C   1 
ATOM   48679 O  O   . LEU   BA 14 122 ? 41.186  -171.387 71.882  1.00 87.91  ? 122 LEU   b O   1 
ATOM   48680 C  CB  . LEU   BA 14 122 ? 42.071  -168.832 69.995  1.00 84.85  ? 122 LEU   b CB  1 
ATOM   48681 C  CG  . LEU   BA 14 122 ? 42.640  -168.346 68.664  1.00 83.67  ? 122 LEU   b CG  1 
ATOM   48682 C  CD1 . LEU   BA 14 122 ? 41.748  -167.267 68.071  1.00 84.14  ? 122 LEU   b CD1 1 
ATOM   48683 C  CD2 . LEU   BA 14 122 ? 44.065  -167.834 68.827  1.00 83.81  ? 122 LEU   b CD2 1 
ATOM   48684 N  N   . PRO   BA 14 123 ? 42.316  -169.807 73.026  1.00 84.43  ? 123 PRO   b N   1 
ATOM   48685 C  CA  . PRO   BA 14 123 ? 41.519  -169.923 74.250  1.00 84.37  ? 123 PRO   b CA  1 
ATOM   48686 C  C   . PRO   BA 14 123 ? 40.062  -169.462 74.099  1.00 83.08  ? 123 PRO   b C   1 
ATOM   48687 O  O   . PRO   BA 14 123 ? 39.213  -169.989 74.770  1.00 78.42  ? 123 PRO   b O   1 
ATOM   48688 C  CB  . PRO   BA 14 123 ? 42.216  -168.981 75.241  1.00 85.27  ? 123 PRO   b CB  1 
ATOM   48689 C  CG  . PRO   BA 14 123 ? 43.627  -168.857 74.715  1.00 86.17  ? 123 PRO   b CG  1 
ATOM   48690 C  CD  . PRO   BA 14 123 ? 43.489  -168.940 73.210  1.00 85.30  ? 123 PRO   b CD  1 
ATOM   48691 N  N   . TYR   BA 14 124 ? 39.826  -168.436 73.283  1.00 83.67  ? 124 TYR   b N   1 
ATOM   48692 C  CA  . TYR   BA 14 124 ? 38.477  -167.991 72.851  1.00 86.36  ? 124 TYR   b CA  1 
ATOM   48693 C  C   . TYR   BA 14 124 ? 38.618  -167.374 71.463  1.00 84.74  ? 124 TYR   b C   1 
ATOM   48694 O  O   . TYR   BA 14 124 ? 39.740  -166.969 71.108  1.00 88.97  ? 124 TYR   b O   1 
ATOM   48695 C  CB  . TYR   BA 14 124 ? 37.854  -167.007 73.848  1.00 87.69  ? 124 TYR   b CB  1 
ATOM   48696 C  CG  . TYR   BA 14 124 ? 38.419  -165.609 73.808  1.00 89.90  ? 124 TYR   b CG  1 
ATOM   48697 C  CD1 . TYR   BA 14 124 ? 39.669  -165.331 74.336  1.00 93.22  ? 124 TYR   b CD1 1 
ATOM   48698 C  CD2 . TYR   BA 14 124 ? 37.708  -164.559 73.246  1.00 91.11  ? 124 TYR   b CD2 1 
ATOM   48699 C  CE1 . TYR   BA 14 124 ? 40.200  -164.050 74.306  1.00 93.21  ? 124 TYR   b CE1 1 
ATOM   48700 C  CE2 . TYR   BA 14 124 ? 38.225  -163.272 73.205  1.00 92.51  ? 124 TYR   b CE2 1 
ATOM   48701 C  CZ  . TYR   BA 14 124 ? 39.477  -163.016 73.739  1.00 89.78  ? 124 TYR   b CZ  1 
ATOM   48702 O  OH  . TYR   BA 14 124 ? 40.014  -161.762 73.717  1.00 87.32  ? 124 TYR   b OH  1 
ATOM   48703 N  N   . ALA   BA 14 125 ? 37.519  -167.326 70.712  1.00 85.50  ? 125 ALA   b N   1 
ATOM   48704 C  CA  . ALA   BA 14 125 ? 37.453  -166.720 69.365  1.00 85.17  ? 125 ALA   b CA  1 
ATOM   48705 C  C   . ALA   BA 14 125 ? 36.176  -165.889 69.253  1.00 84.43  ? 125 ALA   b C   1 
ATOM   48706 O  O   . ALA   BA 14 125 ? 35.136  -166.320 69.788  1.00 83.58  ? 125 ALA   b O   1 
ATOM   48707 C  CB  . ALA   BA 14 125 ? 37.513  -167.796 68.311  1.00 85.38  ? 125 ALA   b CB  1 
ATOM   48708 N  N   . ILE   BA 14 126 ? 36.280  -164.735 68.597  1.00 85.88  ? 126 ILE   b N   1 
ATOM   48709 C  CA  . ILE   BA 14 126 ? 35.132  -163.860 68.223  1.00 86.26  ? 126 ILE   b CA  1 
ATOM   48710 C  C   . ILE   BA 14 126 ? 35.186  -163.662 66.706  1.00 84.01  ? 126 ILE   b C   1 
ATOM   48711 O  O   . ILE   BA 14 126 ? 36.305  -163.578 66.159  1.00 87.42  ? 126 ILE   b O   1 
ATOM   48712 C  CB  . ILE   BA 14 126 ? 35.178  -162.534 69.005  1.00 87.48  ? 126 ILE   b CB  1 
ATOM   48713 C  CG1 . ILE   BA 14 126 ? 36.528  -161.825 68.857  1.00 91.39  ? 126 ILE   b CG1 1 
ATOM   48714 C  CG2 . ILE   BA 14 126 ? 34.834  -162.773 70.468  1.00 86.91  ? 126 ILE   b CG2 1 
ATOM   48715 C  CD1 . ILE   BA 14 126 ? 36.459  -160.325 69.033  1.00 91.51  ? 126 ILE   b CD1 1 
ATOM   48716 N  N   . ALA   BA 14 127 ? 34.028  -163.637 66.048  1.00 83.23  ? 127 ALA   b N   1 
ATOM   48717 C  CA  . ALA   BA 14 127 ? 33.917  -163.477 64.581  1.00 84.81  ? 127 ALA   b CA  1 
ATOM   48718 C  C   . ALA   BA 14 127 ? 32.552  -162.883 64.214  1.00 85.05  ? 127 ALA   b C   1 
ATOM   48719 O  O   . ALA   BA 14 127 ? 31.691  -162.745 65.114  1.00 80.59  ? 127 ALA   b O   1 
ATOM   48720 C  CB  . ALA   BA 14 127 ? 34.153  -164.806 63.905  1.00 84.04  ? 127 ALA   b CB  1 
ATOM   48721 N  N   . GLY   BA 14 128 ? 32.383  -162.536 62.935  1.00 87.04  ? 128 GLY   b N   1 
ATOM   48722 C  CA  . GLY   BA 14 128 ? 31.191  -161.850 62.404  1.00 88.81  ? 128 GLY   b CA  1 
ATOM   48723 C  C   . GLY   BA 14 128 ? 31.384  -160.344 62.414  1.00 89.19  ? 128 GLY   b C   1 
ATOM   48724 O  O   . GLY   BA 14 128 ? 32.421  -159.888 62.936  1.00 92.07  ? 128 GLY   b O   1 
ATOM   48725 N  N   . SER   BA 14 129 ? 30.422  -159.599 61.862  1.00 88.56  ? 129 SER   b N   1 
ATOM   48726 C  CA  . SER   BA 14 129 ? 30.472  -158.122 61.693  1.00 88.02  ? 129 SER   b CA  1 
ATOM   48727 C  C   . SER   BA 14 129 ? 30.572  -157.421 63.055  1.00 88.65  ? 129 SER   b C   1 
ATOM   48728 O  O   . SER   BA 14 129 ? 31.335  -156.439 63.149  1.00 94.10  ? 129 SER   b O   1 
ATOM   48729 C  CB  . SER   BA 14 129 ? 29.286  -157.630 60.911  1.00 85.70  ? 129 SER   b CB  1 
ATOM   48730 O  OG  . SER   BA 14 129 ? 28.080  -158.170 61.426  1.00 85.67  ? 129 SER   b OG  1 
ATOM   48731 N  N   . GLY   BA 14 130 ? 29.837  -157.907 64.064  1.00 86.51  ? 130 GLY   b N   1 
ATOM   48732 C  CA  . GLY   BA 14 130 ? 29.769  -157.320 65.419  1.00 83.96  ? 130 GLY   b CA  1 
ATOM   48733 C  C   . GLY   BA 14 130 ? 31.064  -157.469 66.203  1.00 82.40  ? 130 GLY   b C   1 
ATOM   48734 O  O   . GLY   BA 14 130 ? 31.305  -156.638 67.097  1.00 79.46  ? 130 GLY   b O   1 
ATOM   48735 N  N   . SER   BA 14 131 ? 31.855  -158.504 65.901  1.00 83.84  ? 131 SER   b N   1 
ATOM   48736 C  CA  . SER   BA 14 131 ? 33.166  -158.813 66.537  1.00 88.01  ? 131 SER   b CA  1 
ATOM   48737 C  C   . SER   BA 14 131 ? 34.025  -157.550 66.669  1.00 86.71  ? 131 SER   b C   1 
ATOM   48738 O  O   . SER   BA 14 131 ? 34.573  -157.335 67.767  1.00 86.43  ? 131 SER   b O   1 
ATOM   48739 C  CB  . SER   BA 14 131 ? 33.904  -159.895 65.777  1.00 88.69  ? 131 SER   b CB  1 
ATOM   48740 O  OG  . SER   BA 14 131 ? 34.386  -159.425 64.525  1.00 92.57  ? 131 SER   b OG  1 
ATOM   48741 N  N   . THR   BA 14 132 ? 34.127  -156.754 65.596  1.00 86.99  ? 132 THR   b N   1 
ATOM   48742 C  CA  . THR   BA 14 132 ? 35.018  -155.563 65.489  1.00 89.14  ? 132 THR   b CA  1 
ATOM   48743 C  C   . THR   BA 14 132 ? 34.862  -154.666 66.726  1.00 88.06  ? 132 THR   b C   1 
ATOM   48744 O  O   . THR   BA 14 132 ? 35.882  -154.120 67.179  1.00 89.79  ? 132 THR   b O   1 
ATOM   48745 C  CB  . THR   BA 14 132 ? 34.760  -154.753 64.208  1.00 92.08  ? 132 THR   b CB  1 
ATOM   48746 O  OG1 . THR   BA 14 132 ? 33.386  -154.365 64.179  1.00 94.59  ? 132 THR   b OG1 1 
ATOM   48747 C  CG2 . THR   BA 14 132 ? 35.110  -155.510 62.944  1.00 92.14  ? 132 THR   b CG2 1 
ATOM   48748 N  N   . PHE   BA 14 133 ? 33.641  -154.538 67.258  1.00 85.19  ? 133 PHE   b N   1 
ATOM   48749 C  CA  . PHE   BA 14 133 ? 33.272  -153.559 68.315  1.00 83.76  ? 133 PHE   b CA  1 
ATOM   48750 C  C   . PHE   BA 14 133 ? 33.645  -154.073 69.714  1.00 82.52  ? 133 PHE   b C   1 
ATOM   48751 O  O   . PHE   BA 14 133 ? 33.654  -153.248 70.651  1.00 82.09  ? 133 PHE   b O   1 
ATOM   48752 C  CB  . PHE   BA 14 133 ? 31.787  -153.204 68.204  1.00 83.31  ? 133 PHE   b CB  1 
ATOM   48753 C  CG  . PHE   BA 14 133 ? 31.391  -152.661 66.852  1.00 86.27  ? 133 PHE   b CG  1 
ATOM   48754 C  CD1 . PHE   BA 14 133 ? 31.919  -151.464 66.386  1.00 86.81  ? 133 PHE   b CD1 1 
ATOM   48755 C  CD2 . PHE   BA 14 133 ? 30.506  -153.352 66.036  1.00 85.28  ? 133 PHE   b CD2 1 
ATOM   48756 C  CE1 . PHE   BA 14 133 ? 31.566  -150.967 65.140  1.00 87.24  ? 133 PHE   b CE1 1 
ATOM   48757 C  CE2 . PHE   BA 14 133 ? 30.153  -152.853 64.791  1.00 86.91  ? 133 PHE   b CE2 1 
ATOM   48758 C  CZ  . PHE   BA 14 133 ? 30.682  -151.662 64.346  1.00 87.24  ? 133 PHE   b CZ  1 
ATOM   48759 N  N   . ILE   BA 14 134 ? 33.969  -155.362 69.865  1.00 80.62  ? 134 ILE   b N   1 
ATOM   48760 C  CA  . ILE   BA 14 134 ? 34.186  -155.991 71.205  1.00 81.46  ? 134 ILE   b CA  1 
ATOM   48761 C  C   . ILE   BA 14 134 ? 35.604  -156.565 71.347  1.00 79.37  ? 134 ILE   b C   1 
ATOM   48762 O  O   . ILE   BA 14 134 ? 35.856  -157.194 72.390  1.00 80.17  ? 134 ILE   b O   1 
ATOM   48763 C  CB  . ILE   BA 14 134 ? 33.104  -157.053 71.493  1.00 81.08  ? 134 ILE   b CB  1 
ATOM   48764 C  CG1 . ILE   BA 14 134 ? 33.029  -158.122 70.400  1.00 82.00  ? 134 ILE   b CG1 1 
ATOM   48765 C  CG2 . ILE   BA 14 134 ? 31.758  -156.385 71.724  1.00 80.02  ? 134 ILE   b CG2 1 
ATOM   48766 C  CD1 . ILE   BA 14 134 ? 32.269  -159.364 70.809  1.00 82.01  ? 134 ILE   b CD1 1 
ATOM   48767 N  N   . TYR   BA 14 135 ? 36.511  -156.344 70.388  1.00 78.81  ? 135 TYR   b N   1 
ATOM   48768 C  CA  . TYR   BA 14 135 ? 37.934  -156.765 70.503  1.00 80.37  ? 135 TYR   b CA  1 
ATOM   48769 C  C   . TYR   BA 14 135 ? 38.518  -156.173 71.789  1.00 82.56  ? 135 TYR   b C   1 
ATOM   48770 O  O   . TYR   BA 14 135 ? 39.067  -156.927 72.611  1.00 77.70  ? 135 TYR   b O   1 
ATOM   48771 C  CB  . TYR   BA 14 135 ? 38.751  -156.365 69.271  1.00 82.71  ? 135 TYR   b CB  1 
ATOM   48772 C  CG  . TYR   BA 14 135 ? 38.666  -157.365 68.148  1.00 85.62  ? 135 TYR   b CG  1 
ATOM   48773 C  CD1 . TYR   BA 14 135 ? 39.587  -158.393 68.034  1.00 86.99  ? 135 TYR   b CD1 1 
ATOM   48774 C  CD2 . TYR   BA 14 135 ? 37.643  -157.303 67.218  1.00 88.33  ? 135 TYR   b CD2 1 
ATOM   48775 C  CE1 . TYR   BA 14 135 ? 39.501  -159.328 67.015  1.00 90.50  ? 135 TYR   b CE1 1 
ATOM   48776 C  CE2 . TYR   BA 14 135 ? 37.543  -158.226 66.191  1.00 91.88  ? 135 TYR   b CE2 1 
ATOM   48777 C  CZ  . TYR   BA 14 135 ? 38.474  -159.247 66.090  1.00 94.40  ? 135 TYR   b CZ  1 
ATOM   48778 O  OH  . TYR   BA 14 135 ? 38.384  -160.168 65.084  1.00 102.52 ? 135 TYR   b OH  1 
ATOM   48779 N  N   . GLY   BA 14 136 ? 38.373  -154.857 71.959  1.00 83.71  ? 136 GLY   b N   1 
ATOM   48780 C  CA  . GLY   BA 14 136 ? 38.824  -154.117 73.152  1.00 85.74  ? 136 GLY   b CA  1 
ATOM   48781 C  C   . GLY   BA 14 136 ? 38.291  -154.734 74.432  1.00 83.97  ? 136 GLY   b C   1 
ATOM   48782 O  O   . GLY   BA 14 136 ? 39.107  -155.073 75.309  1.00 83.40  ? 136 GLY   b O   1 
ATOM   48783 N  N   . TYR   BA 14 137 ? 36.966  -154.878 74.523  1.00 86.11  ? 137 TYR   b N   1 
ATOM   48784 C  CA  . TYR   BA 14 137 ? 36.237  -155.368 75.722  1.00 85.77  ? 137 TYR   b CA  1 
ATOM   48785 C  C   . TYR   BA 14 137 ? 36.655  -156.803 76.055  1.00 85.85  ? 137 TYR   b C   1 
ATOM   48786 O  O   . TYR   BA 14 137 ? 36.973  -157.070 77.228  1.00 86.13  ? 137 TYR   b O   1 
ATOM   48787 C  CB  . TYR   BA 14 137 ? 34.724  -155.315 75.503  1.00 85.47  ? 137 TYR   b CB  1 
ATOM   48788 C  CG  . TYR   BA 14 137 ? 33.931  -155.828 76.676  1.00 87.05  ? 137 TYR   b CG  1 
ATOM   48789 C  CD1 . TYR   BA 14 137 ? 33.580  -154.990 77.720  1.00 88.98  ? 137 TYR   b CD1 1 
ATOM   48790 C  CD2 . TYR   BA 14 137 ? 33.556  -157.158 76.762  1.00 88.58  ? 137 TYR   b CD2 1 
ATOM   48791 C  CE1 . TYR   BA 14 137 ? 32.864  -155.453 78.811  1.00 90.79  ? 137 TYR   b CE1 1 
ATOM   48792 C  CE2 . TYR   BA 14 137 ? 32.839  -157.639 77.846  1.00 90.08  ? 137 TYR   b CE2 1 
ATOM   48793 C  CZ  . TYR   BA 14 137 ? 32.492  -156.783 78.874  1.00 90.06  ? 137 TYR   b CZ  1 
ATOM   48794 O  OH  . TYR   BA 14 137 ? 31.786  -157.251 79.944  1.00 94.00  ? 137 TYR   b OH  1 
ATOM   48795 N  N   . CYS   BA 14 138 ? 36.624  -157.698 75.061  1.00 86.17  ? 138 CYS   b N   1 
ATOM   48796 C  CA  . CYS   BA 14 138 ? 36.853  -159.159 75.230  1.00 87.62  ? 138 CYS   b CA  1 
ATOM   48797 C  C   . CYS   BA 14 138 ? 38.286  -159.419 75.707  1.00 90.44  ? 138 CYS   b C   1 
ATOM   48798 O  O   . CYS   BA 14 138 ? 38.453  -160.252 76.616  1.00 96.73  ? 138 CYS   b O   1 
ATOM   48799 C  CB  . CYS   BA 14 138 ? 36.581  -159.931 73.945  1.00 85.01  ? 138 CYS   b CB  1 
ATOM   48800 S  SG  . CYS   BA 14 138 ? 34.815  -160.088 73.575  1.00 84.86  ? 138 CYS   b SG  1 
ATOM   48801 N  N   . ASP   BA 14 139 ? 39.272  -158.732 75.121  1.00 90.01  ? 139 ASP   b N   1 
ATOM   48802 C  CA  . ASP   BA 14 139 ? 40.709  -158.852 75.491  1.00 90.71  ? 139 ASP   b CA  1 
ATOM   48803 C  C   . ASP   BA 14 139 ? 40.902  -158.436 76.953  1.00 92.82  ? 139 ASP   b C   1 
ATOM   48804 O  O   . ASP   BA 14 139 ? 41.704  -159.081 77.656  1.00 94.16  ? 139 ASP   b O   1 
ATOM   48805 C  CB  . ASP   BA 14 139 ? 41.593  -157.995 74.587  1.00 89.55  ? 139 ASP   b CB  1 
ATOM   48806 C  CG  . ASP   BA 14 139 ? 43.075  -158.136 74.888  1.00 91.65  ? 139 ASP   b CG  1 
ATOM   48807 O  OD1 . ASP   BA 14 139 ? 43.580  -159.272 74.821  1.00 90.08  ? 139 ASP   b OD1 1 
ATOM   48808 O  OD2 . ASP   BA 14 139 ? 43.710  -157.110 75.199  1.00 92.48  ? 139 ASP   b OD2 1 
ATOM   48809 N  N   . LYS   BA 14 140 ? 40.196  -157.389 77.380  1.00 95.03  ? 140 LYS   b N   1 
ATOM   48810 C  CA  . LYS   BA 14 140 ? 40.318  -156.793 78.736  1.00 96.99  ? 140 LYS   b CA  1 
ATOM   48811 C  C   . LYS   BA 14 140 ? 39.630  -157.684 79.777  1.00 93.58  ? 140 LYS   b C   1 
ATOM   48812 O  O   . LYS   BA 14 140 ? 40.047  -157.625 80.943  1.00 95.21  ? 140 LYS   b O   1 
ATOM   48813 C  CB  . LYS   BA 14 140 ? 39.726  -155.379 78.754  1.00 98.92  ? 140 LYS   b CB  1 
ATOM   48814 C  CG  . LYS   BA 14 140 ? 40.678  -154.280 78.304  1.00 102.22 ? 140 LYS   b CG  1 
ATOM   48815 C  CD  . LYS   BA 14 140 ? 41.847  -154.093 79.246  1.00 105.90 ? 140 LYS   b CD  1 
ATOM   48816 C  CE  . LYS   BA 14 140 ? 42.661  -152.852 78.955  1.00 107.22 ? 140 LYS   b CE  1 
ATOM   48817 N  NZ  . LYS   BA 14 140 ? 43.987  -152.918 79.611  1.00 109.68 ? 140 LYS   b NZ  1 
ATOM   48818 N  N   . ASN   BA 14 141 ? 38.626  -158.472 79.381  1.00 92.51  ? 141 ASN   b N   1 
ATOM   48819 C  CA  . ASN   BA 14 141 ? 37.704  -159.159 80.325  1.00 97.60  ? 141 ASN   b CA  1 
ATOM   48820 C  C   . ASN   BA 14 141 ? 37.947  -160.676 80.366  1.00 99.14  ? 141 ASN   b C   1 
ATOM   48821 O  O   . ASN   BA 14 141 ? 37.677  -161.267 81.433  1.00 101.43 ? 141 ASN   b O   1 
ATOM   48822 C  CB  . ASN   BA 14 141 ? 36.245  -158.831 80.002  1.00 98.15  ? 141 ASN   b CB  1 
ATOM   48823 C  CG  . ASN   BA 14 141 ? 35.813  -157.510 80.596  1.00 100.79 ? 141 ASN   b CG  1 
ATOM   48824 O  OD1 . ASN   BA 14 141 ? 35.670  -156.520 79.882  1.00 106.42 ? 141 ASN   b OD1 1 
ATOM   48825 N  ND2 . ASN   BA 14 141 ? 35.620  -157.484 81.905  1.00 102.78 ? 141 ASN   b ND2 1 
ATOM   48826 N  N   . PHE   BA 14 142 ? 38.419  -161.298 79.279  1.00 100.17 ? 142 PHE   b N   1 
ATOM   48827 C  CA  . PHE   BA 14 142 ? 38.643  -162.768 79.225  1.00 101.53 ? 142 PHE   b CA  1 
ATOM   48828 C  C   . PHE   BA 14 142 ? 39.724  -163.166 80.235  1.00 100.78 ? 142 PHE   b C   1 
ATOM   48829 O  O   . PHE   BA 14 142 ? 40.777  -162.507 80.291  1.00 95.45  ? 142 PHE   b O   1 
ATOM   48830 C  CB  . PHE   BA 14 142 ? 39.053  -163.264 77.835  1.00 102.52 ? 142 PHE   b CB  1 
ATOM   48831 C  CG  . PHE   BA 14 142 ? 39.450  -164.722 77.811  1.00 101.81 ? 142 PHE   b CG  1 
ATOM   48832 C  CD1 . PHE   BA 14 142 ? 38.487  -165.720 77.776  1.00 100.52 ? 142 PHE   b CD1 1 
ATOM   48833 C  CD2 . PHE   BA 14 142 ? 40.785  -165.099 77.859  1.00 101.59 ? 142 PHE   b CD2 1 
ATOM   48834 C  CE1 . PHE   BA 14 142 ? 38.851  -167.058 77.768  1.00 98.96  ? 142 PHE   b CE1 1 
ATOM   48835 C  CE2 . PHE   BA 14 142 ? 41.146  -166.438 77.853  1.00 99.08  ? 142 PHE   b CE2 1 
ATOM   48836 C  CZ  . PHE   BA 14 142 ? 40.179  -167.415 77.806  1.00 98.56  ? 142 PHE   b CZ  1 
ATOM   48837 N  N   . ARG   BA 14 143 ? 39.449  -164.229 80.996  1.00 105.68 ? 143 ARG   b N   1 
ATOM   48838 C  CA  . ARG   BA 14 143 ? 40.408  -164.935 81.886  1.00 109.62 ? 143 ARG   b CA  1 
ATOM   48839 C  C   . ARG   BA 14 143 ? 40.307  -166.438 81.601  1.00 109.42 ? 143 ARG   b C   1 
ATOM   48840 O  O   . ARG   BA 14 143 ? 39.193  -166.901 81.285  1.00 107.83 ? 143 ARG   b O   1 
ATOM   48841 C  CB  . ARG   BA 14 143 ? 40.087  -164.646 83.355  1.00 114.64 ? 143 ARG   b CB  1 
ATOM   48842 C  CG  . ARG   BA 14 143 ? 40.236  -163.186 83.757  1.00 119.79 ? 143 ARG   b CG  1 
ATOM   48843 C  CD  . ARG   BA 14 143 ? 39.645  -162.918 85.128  1.00 126.28 ? 143 ARG   b CD  1 
ATOM   48844 N  NE  . ARG   BA 14 143 ? 38.186  -162.868 85.100  1.00 128.13 ? 143 ARG   b NE  1 
ATOM   48845 C  CZ  . ARG   BA 14 143 ? 37.360  -163.776 85.624  1.00 129.10 ? 143 ARG   b CZ  1 
ATOM   48846 N  NH1 . ARG   BA 14 143 ? 37.826  -164.845 86.251  1.00 129.38 ? 143 ARG   b NH1 1 
ATOM   48847 N  NH2 . ARG   BA 14 143 ? 36.053  -163.601 85.523  1.00 127.84 ? 143 ARG   b NH2 1 
ATOM   48848 N  N   . GLU   BA 14 144 ? 41.420  -167.170 81.696  1.00 108.86 ? 144 GLU   b N   1 
ATOM   48849 C  CA  . GLU   BA 14 144 ? 41.446  -168.645 81.491  1.00 108.28 ? 144 GLU   b CA  1 
ATOM   48850 C  C   . GLU   BA 14 144 ? 40.910  -169.334 82.751  1.00 105.99 ? 144 GLU   b C   1 
ATOM   48851 O  O   . GLU   BA 14 144 ? 41.083  -168.776 83.848  1.00 109.48 ? 144 GLU   b O   1 
ATOM   48852 C  CB  . GLU   BA 14 144 ? 42.851  -169.136 81.132  1.00 106.83 ? 144 GLU   b CB  1 
ATOM   48853 C  CG  . GLU   BA 14 144 ? 43.023  -169.408 79.648  1.00 108.02 ? 144 GLU   b CG  1 
ATOM   48854 C  CD  . GLU   BA 14 144 ? 44.457  -169.595 79.181  1.00 110.70 ? 144 GLU   b CD  1 
ATOM   48855 O  OE1 . GLU   BA 14 144 ? 44.648  -169.916 77.990  1.00 115.78 ? 144 GLU   b OE1 1 
ATOM   48856 O  OE2 . GLU   BA 14 144 ? 45.379  -169.421 80.005  1.00 110.67 ? 144 GLU   b OE2 1 
ATOM   48857 N  N   . ASN   BA 14 145 ? 40.264  -170.491 82.577  1.00 105.92 ? 145 ASN   b N   1 
ATOM   48858 C  CA  . ASN   BA 14 145 ? 39.731  -171.360 83.662  1.00 106.15 ? 145 ASN   b CA  1 
ATOM   48859 C  C   . ASN   BA 14 145 ? 38.622  -170.632 84.432  1.00 102.64 ? 145 ASN   b C   1 
ATOM   48860 O  O   . ASN   BA 14 145 ? 38.556  -170.796 85.666  1.00 101.71 ? 145 ASN   b O   1 
ATOM   48861 C  CB  . ASN   BA 14 145 ? 40.842  -171.831 84.604  1.00 111.09 ? 145 ASN   b CB  1 
ATOM   48862 C  CG  . ASN   BA 14 145 ? 41.921  -172.621 83.896  1.00 115.11 ? 145 ASN   b CG  1 
ATOM   48863 O  OD1 . ASN   BA 14 145 ? 43.096  -172.266 83.957  1.00 123.49 ? 145 ASN   b OD1 1 
ATOM   48864 N  ND2 . ASN   BA 14 145 ? 41.536  -173.692 83.221  1.00 114.72 ? 145 ASN   b ND2 1 
ATOM   48865 N  N   . MET   BA 14 146 ? 37.770  -169.879 83.732  1.00 101.16 ? 146 MET   b N   1 
ATOM   48866 C  CA  . MET   BA 14 146 ? 36.551  -169.256 84.314  1.00 99.63  ? 146 MET   b CA  1 
ATOM   48867 C  C   . MET   BA 14 146 ? 35.570  -170.369 84.700  1.00 98.40  ? 146 MET   b C   1 
ATOM   48868 O  O   . MET   BA 14 146 ? 35.772  -171.511 84.254  1.00 95.41  ? 146 MET   b O   1 
ATOM   48869 C  CB  . MET   BA 14 146 ? 35.883  -168.297 83.321  1.00 101.47 ? 146 MET   b CB  1 
ATOM   48870 C  CG  . MET   BA 14 146 ? 36.546  -166.936 83.258  1.00 100.80 ? 146 MET   b CG  1 
ATOM   48871 S  SD  . MET   BA 14 146 ? 35.657  -165.782 82.185  1.00 100.45 ? 146 MET   b SD  1 
ATOM   48872 C  CE  . MET   BA 14 146 ? 36.022  -166.460 80.566  1.00 101.15 ? 146 MET   b CE  1 
ATOM   48873 N  N   . SER   BA 14 147 ? 34.563  -170.047 85.516  1.00 97.24  ? 147 SER   b N   1 
ATOM   48874 C  CA  . SER   BA 14 147 ? 33.434  -170.952 85.857  1.00 99.89  ? 147 SER   b CA  1 
ATOM   48875 C  C   . SER   BA 14 147 ? 32.370  -170.852 84.759  1.00 101.86 ? 147 SER   b C   1 
ATOM   48876 O  O   . SER   BA 14 147 ? 32.516  -169.985 83.874  1.00 101.24 ? 147 SER   b O   1 
ATOM   48877 C  CB  . SER   BA 14 147 ? 32.866  -170.643 87.218  1.00 99.79  ? 147 SER   b CB  1 
ATOM   48878 O  OG  . SER   BA 14 147 ? 32.233  -169.375 87.242  1.00 100.88 ? 147 SER   b OG  1 
ATOM   48879 N  N   . LYS   BA 14 148 ? 31.348  -171.713 84.810  1.00 105.15 ? 148 LYS   b N   1 
ATOM   48880 C  CA  . LYS   BA 14 148 ? 30.228  -171.727 83.831  1.00 107.59 ? 148 LYS   b CA  1 
ATOM   48881 C  C   . LYS   BA 14 148 ? 29.495  -170.381 83.893  1.00 110.58 ? 148 LYS   b C   1 
ATOM   48882 O  O   . LYS   BA 14 148 ? 29.298  -169.772 82.825  1.00 113.75 ? 148 LYS   b O   1 
ATOM   48883 C  CB  . LYS   BA 14 148 ? 29.269  -172.889 84.105  1.00 107.00 ? 148 LYS   b CB  1 
ATOM   48884 C  CG  . LYS   BA 14 148 ? 28.177  -173.084 83.061  1.00 106.63 ? 148 LYS   b CG  1 
ATOM   48885 C  CD  . LYS   BA 14 148 ? 27.040  -173.968 83.527  1.00 108.79 ? 148 LYS   b CD  1 
ATOM   48886 C  CE  . LYS   BA 14 148 ? 25.796  -173.828 82.674  1.00 110.11 ? 148 LYS   b CE  1 
ATOM   48887 N  NZ  . LYS   BA 14 148 ? 24.602  -174.379 83.357  1.00 113.53 ? 148 LYS   b NZ  1 
ATOM   48888 N  N   . GLU   BA 14 149 ? 29.134  -169.928 85.098  1.00 112.88 ? 149 GLU   b N   1 
ATOM   48889 C  CA  . GLU   BA 14 149 ? 28.333  -168.692 85.321  1.00 114.49 ? 149 GLU   b CA  1 
ATOM   48890 C  C   . GLU   BA 14 149 ? 29.131  -167.468 84.858  1.00 111.91 ? 149 GLU   b C   1 
ATOM   48891 O  O   . GLU   BA 14 149 ? 28.508  -166.547 84.292  1.00 112.12 ? 149 GLU   b O   1 
ATOM   48892 C  CB  . GLU   BA 14 149 ? 27.925  -168.549 86.789  1.00 119.66 ? 149 GLU   b CB  1 
ATOM   48893 C  CG  . GLU   BA 14 149 ? 26.791  -169.474 87.192  1.00 125.98 ? 149 GLU   b CG  1 
ATOM   48894 C  CD  . GLU   BA 14 149 ? 27.156  -170.946 87.278  1.00 132.45 ? 149 GLU   b CD  1 
ATOM   48895 O  OE1 . GLU   BA 14 149 ? 28.329  -171.250 87.582  1.00 133.58 ? 149 GLU   b OE1 1 
ATOM   48896 O  OE2 . GLU   BA 14 149 ? 26.268  -171.785 87.033  1.00 139.43 ? 149 GLU   b OE2 1 
ATOM   48897 N  N   . GLU   BA 14 150 ? 30.448  -167.461 85.091  1.00 106.05 ? 150 GLU   b N   1 
ATOM   48898 C  CA  . GLU   BA 14 150 ? 31.366  -166.368 84.670  1.00 104.56 ? 150 GLU   b CA  1 
ATOM   48899 C  C   . GLU   BA 14 150 ? 31.429  -166.311 83.139  1.00 104.23 ? 150 GLU   b C   1 
ATOM   48900 O  O   . GLU   BA 14 150 ? 31.311  -165.197 82.583  1.00 102.74 ? 150 GLU   b O   1 
ATOM   48901 C  CB  . GLU   BA 14 150 ? 32.764  -166.573 85.257  1.00 104.66 ? 150 GLU   b CB  1 
ATOM   48902 C  CG  . GLU   BA 14 150 ? 32.849  -166.263 86.740  1.00 108.72 ? 150 GLU   b CG  1 
ATOM   48903 C  CD  . GLU   BA 14 150 ? 34.202  -166.548 87.371  1.00 110.01 ? 150 GLU   b CD  1 
ATOM   48904 O  OE1 . GLU   BA 14 150 ? 34.907  -167.454 86.886  1.00 110.72 ? 150 GLU   b OE1 1 
ATOM   48905 O  OE2 . GLU   BA 14 150 ? 34.550  -165.858 88.346  1.00 116.90 ? 150 GLU   b OE2 1 
ATOM   48906 N  N   . THR   BA 14 151 ? 31.607  -167.466 82.490  1.00 99.27  ? 151 THR   b N   1 
ATOM   48907 C  CA  . THR   BA 14 151 ? 31.747  -167.591 81.015  1.00 95.75  ? 151 THR   b CA  1 
ATOM   48908 C  C   . THR   BA 14 151 ? 30.431  -167.205 80.331  1.00 96.72  ? 151 THR   b C   1 
ATOM   48909 O  O   . THR   BA 14 151 ? 30.498  -166.572 79.259  1.00 95.92  ? 151 THR   b O   1 
ATOM   48910 C  CB  . THR   BA 14 151 ? 32.178  -169.002 80.599  1.00 93.35  ? 151 THR   b CB  1 
ATOM   48911 O  OG1 . THR   BA 14 151 ? 33.305  -169.367 81.394  1.00 90.91  ? 151 THR   b OG1 1 
ATOM   48912 C  CG2 . THR   BA 14 151 ? 32.533  -169.089 79.131  1.00 92.55  ? 151 THR   b CG2 1 
ATOM   48913 N  N   . VAL   BA 14 152 ? 29.287  -167.575 80.914  1.00 94.97  ? 152 VAL   b N   1 
ATOM   48914 C  CA  . VAL   BA 14 152 ? 27.944  -167.194 80.385  1.00 98.81  ? 152 VAL   b CA  1 
ATOM   48915 C  C   . VAL   BA 14 152 ? 27.820  -165.666 80.426  1.00 102.74 ? 152 VAL   b C   1 
ATOM   48916 O  O   . VAL   BA 14 152 ? 27.380  -165.085 79.411  1.00 105.07 ? 152 VAL   b O   1 
ATOM   48917 C  CB  . VAL   BA 14 152 ? 26.791  -167.884 81.142  1.00 99.75  ? 152 VAL   b CB  1 
ATOM   48918 C  CG1 . VAL   BA 14 152 ? 25.446  -167.229 80.849  1.00 101.01 ? 152 VAL   b CG1 1 
ATOM   48919 C  CG2 . VAL   BA 14 152 ? 26.728  -169.371 80.829  1.00 98.68  ? 152 VAL   b CG2 1 
ATOM   48920 N  N   . ASP   BA 14 153 ? 28.202  -165.049 81.549  1.00 103.01 ? 153 ASP   b N   1 
ATOM   48921 C  CA  . ASP   BA 14 153 ? 28.148  -163.576 81.754  1.00 102.18 ? 153 ASP   b CA  1 
ATOM   48922 C  C   . ASP   BA 14 153 ? 29.078  -162.895 80.746  1.00 96.56  ? 153 ASP   b C   1 
ATOM   48923 O  O   . ASP   BA 14 153 ? 28.638  -161.910 80.127  1.00 99.16  ? 153 ASP   b O   1 
ATOM   48924 C  CB  . ASP   BA 14 153 ? 28.495  -163.193 83.196  1.00 103.60 ? 153 ASP   b CB  1 
ATOM   48925 C  CG  . ASP   BA 14 153 ? 27.388  -163.478 84.196  1.00 107.31 ? 153 ASP   b CG  1 
ATOM   48926 O  OD1 . ASP   BA 14 153 ? 26.231  -163.658 83.761  1.00 107.36 ? 153 ASP   b OD1 1 
ATOM   48927 O  OD2 . ASP   BA 14 153 ? 27.690  -163.514 85.406  1.00 110.50 ? 153 ASP   b OD2 1 
ATOM   48928 N  N   . PHE   BA 14 154 ? 30.301  -163.410 80.579  1.00 91.27  ? 154 PHE   b N   1 
ATOM   48929 C  CA  . PHE   BA 14 154 ? 31.324  -162.870 79.644  1.00 90.19  ? 154 PHE   b CA  1 
ATOM   48930 C  C   . PHE   BA 14 154 ? 30.754  -162.822 78.222  1.00 94.27  ? 154 PHE   b C   1 
ATOM   48931 O  O   . PHE   BA 14 154 ? 30.855  -161.762 77.572  1.00 97.84  ? 154 PHE   b O   1 
ATOM   48932 C  CB  . PHE   BA 14 154 ? 32.611  -163.696 79.687  1.00 88.42  ? 154 PHE   b CB  1 
ATOM   48933 C  CG  . PHE   BA 14 154 ? 33.642  -163.283 78.667  1.00 86.76  ? 154 PHE   b CG  1 
ATOM   48934 C  CD1 . PHE   BA 14 154 ? 34.173  -162.003 78.676  1.00 88.10  ? 154 PHE   b CD1 1 
ATOM   48935 C  CD2 . PHE   BA 14 154 ? 34.074  -164.167 77.691  1.00 86.86  ? 154 PHE   b CD2 1 
ATOM   48936 C  CE1 . PHE   BA 14 154 ? 35.114  -161.617 77.733  1.00 90.63  ? 154 PHE   b CE1 1 
ATOM   48937 C  CE2 . PHE   BA 14 154 ? 35.017  -163.781 76.750  1.00 88.11  ? 154 PHE   b CE2 1 
ATOM   48938 C  CZ  . PHE   BA 14 154 ? 35.535  -162.507 76.772  1.00 89.41  ? 154 PHE   b CZ  1 
ATOM   48939 N  N   . ILE   BA 14 155 ? 30.178  -163.933 77.752  1.00 93.83  ? 155 ILE   b N   1 
ATOM   48940 C  CA  . ILE   BA 14 155 ? 29.571  -164.045 76.391  1.00 94.44  ? 155 ILE   b CA  1 
ATOM   48941 C  C   . ILE   BA 14 155 ? 28.366  -163.101 76.311  1.00 93.29  ? 155 ILE   b C   1 
ATOM   48942 O  O   . ILE   BA 14 155 ? 28.245  -162.401 75.289  1.00 93.48  ? 155 ILE   b O   1 
ATOM   48943 C  CB  . ILE   BA 14 155 ? 29.196  -165.505 76.055  1.00 94.34  ? 155 ILE   b CB  1 
ATOM   48944 C  CG1 . ILE   BA 14 155 ? 30.448  -166.375 75.900  1.00 93.63  ? 155 ILE   b CG1 1 
ATOM   48945 C  CG2 . ILE   BA 14 155 ? 28.312  -165.568 74.815  1.00 94.24  ? 155 ILE   b CG2 1 
ATOM   48946 C  CD1 . ILE   BA 14 155 ? 30.175  -167.858 75.785  1.00 93.25  ? 155 ILE   b CD1 1 
ATOM   48947 N  N   . LYS   BA 14 156 ? 27.522  -163.081 77.348  1.00 95.79  ? 156 LYS   b N   1 
ATOM   48948 C  CA  . LYS   BA 14 156 ? 26.254  -162.300 77.376  1.00 96.97  ? 156 LYS   b CA  1 
ATOM   48949 C  C   . LYS   BA 14 156 ? 26.562  -160.803 77.261  1.00 96.39  ? 156 LYS   b C   1 
ATOM   48950 O  O   . LYS   BA 14 156 ? 25.912  -160.131 76.437  1.00 95.84  ? 156 LYS   b O   1 
ATOM   48951 C  CB  . LYS   BA 14 156 ? 25.457  -162.583 78.653  1.00 98.72  ? 156 LYS   b CB  1 
ATOM   48952 C  CG  . LYS   BA 14 156 ? 23.979  -162.230 78.569  1.00 98.37  ? 156 LYS   b CG  1 
ATOM   48953 C  CD  . LYS   BA 14 156 ? 23.284  -162.207 79.910  1.00 99.06  ? 156 LYS   b CD  1 
ATOM   48954 C  CE  . LYS   BA 14 156 ? 23.192  -163.573 80.555  1.00 100.38 ? 156 LYS   b CE  1 
ATOM   48955 N  NZ  . LYS   BA 14 156 ? 22.716  -163.481 81.954  1.00 101.75 ? 156 LYS   b NZ  1 
ATOM   48956 N  N   . HIS   BA 14 157 ? 27.509  -160.306 78.062  1.00 96.41  ? 157 HIS   b N   1 
ATOM   48957 C  CA  . HIS   BA 14 157 ? 27.950  -158.884 78.080  1.00 99.31  ? 157 HIS   b CA  1 
ATOM   48958 C  C   . HIS   BA 14 157 ? 28.612  -158.522 76.744  1.00 99.28  ? 157 HIS   b C   1 
ATOM   48959 O  O   . HIS   BA 14 157 ? 28.334  -157.417 76.232  1.00 101.61 ? 157 HIS   b O   1 
ATOM   48960 C  CB  . HIS   BA 14 157 ? 28.887  -158.615 79.267  1.00 99.19  ? 157 HIS   b CB  1 
ATOM   48961 C  CG  . HIS   BA 14 157 ? 28.180  -158.395 80.564  1.00 103.07 ? 157 HIS   b CG  1 
ATOM   48962 N  ND1 . HIS   BA 14 157 ? 27.691  -159.434 81.333  1.00 102.71 ? 157 HIS   b ND1 1 
ATOM   48963 C  CD2 . HIS   BA 14 157 ? 27.887  -157.262 81.235  1.00 105.22 ? 157 HIS   b CD2 1 
ATOM   48964 C  CE1 . HIS   BA 14 157 ? 27.121  -158.948 82.417  1.00 106.01 ? 157 HIS   b CE1 1 
ATOM   48965 N  NE2 . HIS   BA 14 157 ? 27.230  -157.617 82.382  1.00 106.68 ? 157 HIS   b NE2 1 
ATOM   48966 N  N   . SER   BA 14 158 ? 29.455  -159.414 76.210  1.00 95.08  ? 158 SER   b N   1 
ATOM   48967 C  CA  . SER   BA 14 158 ? 30.213  -159.219 74.944  1.00 92.46  ? 158 SER   b CA  1 
ATOM   48968 C  C   . SER   BA 14 158 ? 29.237  -159.073 73.767  1.00 91.50  ? 158 SER   b C   1 
ATOM   48969 O  O   . SER   BA 14 158 ? 29.290  -158.032 73.083  1.00 87.93  ? 158 SER   b O   1 
ATOM   48970 C  CB  . SER   BA 14 158 ? 31.202  -160.340 74.711  1.00 89.69  ? 158 SER   b CB  1 
ATOM   48971 O  OG  . SER   BA 14 158 ? 32.217  -160.341 75.705  1.00 88.39  ? 158 SER   b OG  1 
ATOM   48972 N  N   . LEU   BA 14 159 ? 28.373  -160.070 73.547  1.00 90.51  ? 159 LEU   b N   1 
ATOM   48973 C  CA  . LEU   BA 14 159 ? 27.390  -160.079 72.429  1.00 88.69  ? 159 LEU   b CA  1 
ATOM   48974 C  C   . LEU   BA 14 159 ? 26.389  -158.932 72.620  1.00 88.48  ? 159 LEU   b C   1 
ATOM   48975 O  O   . LEU   BA 14 159 ? 25.903  -158.411 71.600  1.00 90.02  ? 159 LEU   b O   1 
ATOM   48976 C  CB  . LEU   BA 14 159 ? 26.671  -161.433 72.357  1.00 90.17  ? 159 LEU   b CB  1 
ATOM   48977 C  CG  . LEU   BA 14 159 ? 27.522  -162.645 71.966  1.00 91.26  ? 159 LEU   b CG  1 
ATOM   48978 C  CD1 . LEU   BA 14 159 ? 26.642  -163.871 71.789  1.00 92.42  ? 159 LEU   b CD1 1 
ATOM   48979 C  CD2 . LEU   BA 14 159 ? 28.327  -162.397 70.696  1.00 91.11  ? 159 LEU   b CD2 1 
ATOM   48980 N  N   . SER   BA 14 160 ? 26.097  -158.554 73.869  1.00 85.46  ? 160 SER   b N   1 
ATOM   48981 C  CA  . SER   BA 14 160 ? 25.231  -157.395 74.214  1.00 87.51  ? 160 SER   b CA  1 
ATOM   48982 C  C   . SER   BA 14 160 ? 25.789  -156.127 73.559  1.00 85.70  ? 160 SER   b C   1 
ATOM   48983 O  O   . SER   BA 14 160 ? 25.008  -155.399 72.916  1.00 81.20  ? 160 SER   b O   1 
ATOM   48984 C  CB  . SER   BA 14 160 ? 25.105  -157.223 75.705  1.00 90.63  ? 160 SER   b CB  1 
ATOM   48985 O  OG  . SER   BA 14 160 ? 24.247  -156.139 76.021  1.00 95.45  ? 160 SER   b OG  1 
ATOM   48986 N  N   . GLN   BA 14 161 ? 27.095  -155.889 73.711  1.00 84.45  ? 161 GLN   b N   1 
ATOM   48987 C  CA  . GLN   BA 14 161 ? 27.799  -154.718 73.127  1.00 84.00  ? 161 GLN   b CA  1 
ATOM   48988 C  C   . GLN   BA 14 161 ? 27.888  -154.887 71.607  1.00 85.49  ? 161 GLN   b C   1 
ATOM   48989 O  O   . GLN   BA 14 161 ? 27.527  -153.929 70.899  1.00 88.40  ? 161 GLN   b O   1 
ATOM   48990 C  CB  . GLN   BA 14 161 ? 29.176  -154.530 73.767  1.00 84.62  ? 161 GLN   b CB  1 
ATOM   48991 C  CG  . GLN   BA 14 161 ? 29.118  -153.969 75.186  1.00 86.08  ? 161 GLN   b CG  1 
ATOM   48992 C  CD  . GLN   BA 14 161 ? 28.379  -152.655 75.305  1.00 84.73  ? 161 GLN   b CD  1 
ATOM   48993 O  OE1 . GLN   BA 14 161 ? 27.466  -152.508 76.113  1.00 84.12  ? 161 GLN   b OE1 1 
ATOM   48994 N  NE2 . GLN   BA 14 161 ? 28.767  -151.681 74.499  1.00 82.88  ? 161 GLN   b NE2 1 
ATOM   48995 N  N   . ALA   BA 14 162 ? 28.327  -156.053 71.123  1.00 83.30  ? 162 ALA   b N   1 
ATOM   48996 C  CA  . ALA   BA 14 162 ? 28.401  -156.363 69.675  1.00 83.29  ? 162 ALA   b CA  1 
ATOM   48997 C  C   . ALA   BA 14 162 ? 27.047  -156.049 69.025  1.00 84.18  ? 162 ALA   b C   1 
ATOM   48998 O  O   . ALA   BA 14 162 ? 27.045  -155.351 67.997  1.00 85.77  ? 162 ALA   b O   1 
ATOM   48999 C  CB  . ALA   BA 14 162 ? 28.815  -157.796 69.449  1.00 84.82  ? 162 ALA   b CB  1 
ATOM   49000 N  N   . ILE   BA 14 163 ? 25.943  -156.506 69.628  1.00 83.23  ? 163 ILE   b N   1 
ATOM   49001 C  CA  . ILE   BA 14 163 ? 24.553  -156.292 69.117  1.00 84.99  ? 163 ILE   b CA  1 
ATOM   49002 C  C   . ILE   BA 14 163 ? 24.216  -154.796 69.146  1.00 86.20  ? 163 ILE   b C   1 
ATOM   49003 O  O   . ILE   BA 14 163 ? 23.583  -154.319 68.179  1.00 83.14  ? 163 ILE   b O   1 
ATOM   49004 C  CB  . ILE   BA 14 163 ? 23.525  -157.131 69.905  1.00 87.69  ? 163 ILE   b CB  1 
ATOM   49005 C  CG1 . ILE   BA 14 163 ? 23.534  -158.588 69.434  1.00 90.20  ? 163 ILE   b CG1 1 
ATOM   49006 C  CG2 . ILE   BA 14 163 ? 22.131  -156.522 69.811  1.00 88.11  ? 163 ILE   b CG2 1 
ATOM   49007 C  CD1 . ILE   BA 14 163 ? 22.781  -159.542 70.334  1.00 91.96  ? 163 ILE   b CD1 1 
ATOM   49008 N  N   . LYS   BA 14 164 ? 24.611  -154.093 70.210  1.00 86.51  ? 164 LYS   b N   1 
ATOM   49009 C  CA  . LYS   BA 14 164 ? 24.244  -152.672 70.455  1.00 89.09  ? 164 LYS   b CA  1 
ATOM   49010 C  C   . LYS   BA 14 164 ? 24.730  -151.779 69.308  1.00 88.51  ? 164 LYS   b C   1 
ATOM   49011 O  O   . LYS   BA 14 164 ? 23.954  -150.900 68.886  1.00 89.16  ? 164 LYS   b O   1 
ATOM   49012 C  CB  . LYS   BA 14 164 ? 24.842  -152.165 71.770  1.00 88.94  ? 164 LYS   b CB  1 
ATOM   49013 C  CG  . LYS   BA 14 164 ? 24.478  -150.726 72.099  1.00 90.69  ? 164 LYS   b CG  1 
ATOM   49014 C  CD  . LYS   BA 14 164 ? 24.942  -150.258 73.454  1.00 93.19  ? 164 LYS   b CD  1 
ATOM   49015 C  CE  . LYS   BA 14 164 ? 24.487  -148.843 73.737  1.00 94.75  ? 164 LYS   b CE  1 
ATOM   49016 N  NZ  . LYS   BA 14 164 ? 24.659  -148.480 75.161  1.00 95.53  ? 164 LYS   b NZ  1 
ATOM   49017 N  N   . TRP   BA 14 165 ? 25.969  -151.983 68.848  1.00 89.34  ? 165 TRP   b N   1 
ATOM   49018 C  CA  . TRP   BA 14 165 ? 26.654  -151.118 67.848  1.00 89.24  ? 165 TRP   b CA  1 
ATOM   49019 C  C   . TRP   BA 14 165 ? 26.419  -151.640 66.429  1.00 89.61  ? 165 TRP   b C   1 
ATOM   49020 O  O   . TRP   BA 14 165 ? 26.126  -150.809 65.553  1.00 94.11  ? 165 TRP   b O   1 
ATOM   49021 C  CB  . TRP   BA 14 165 ? 28.147  -151.005 68.171  1.00 88.82  ? 165 TRP   b CB  1 
ATOM   49022 C  CG  . TRP   BA 14 165 ? 28.390  -150.451 69.539  1.00 91.71  ? 165 TRP   b CG  1 
ATOM   49023 C  CD1 . TRP   BA 14 165 ? 28.886  -151.116 70.621  1.00 91.18  ? 165 TRP   b CD1 1 
ATOM   49024 C  CD2 . TRP   BA 14 165 ? 28.099  -149.115 69.987  1.00 93.67  ? 165 TRP   b CD2 1 
ATOM   49025 N  NE1 . TRP   BA 14 165 ? 28.943  -150.282 71.704  1.00 92.37  ? 165 TRP   b NE1 1 
ATOM   49026 C  CE2 . TRP   BA 14 165 ? 28.465  -149.049 71.348  1.00 92.36  ? 165 TRP   b CE2 1 
ATOM   49027 C  CE3 . TRP   BA 14 165 ? 27.576  -147.970 69.374  1.00 94.42  ? 165 TRP   b CE3 1 
ATOM   49028 C  CZ2 . TRP   BA 14 165 ? 28.323  -147.885 72.100  1.00 92.89  ? 165 TRP   b CZ2 1 
ATOM   49029 C  CZ3 . TRP   BA 14 165 ? 27.436  -146.819 70.118  1.00 94.42  ? 165 TRP   b CZ3 1 
ATOM   49030 C  CH2 . TRP   BA 14 165 ? 27.807  -146.780 71.463  1.00 93.56  ? 165 TRP   b CH2 1 
ATOM   49031 N  N   . ASP   BA 14 166 ? 26.548  -152.953 66.211  1.00 88.43  ? 166 ASP   b N   1 
ATOM   49032 C  CA  . ASP   BA 14 166 ? 26.382  -153.585 64.874  1.00 87.16  ? 166 ASP   b CA  1 
ATOM   49033 C  C   . ASP   BA 14 166 ? 24.888  -153.662 64.539  1.00 84.22  ? 166 ASP   b C   1 
ATOM   49034 O  O   . ASP   BA 14 166 ? 24.135  -154.310 65.296  1.00 77.24  ? 166 ASP   b O   1 
ATOM   49035 C  CB  . ASP   BA 14 166 ? 27.052  -154.960 64.812  1.00 87.70  ? 166 ASP   b CB  1 
ATOM   49036 C  CG  . ASP   BA 14 166 ? 27.003  -155.616 63.442  1.00 91.22  ? 166 ASP   b CG  1 
ATOM   49037 O  OD1 . ASP   BA 14 166 ? 26.908  -154.877 62.435  1.00 91.71  ? 166 ASP   b OD1 1 
ATOM   49038 O  OD2 . ASP   BA 14 166 ? 27.060  -156.864 63.392  1.00 91.38  ? 166 ASP   b OD2 1 
ATOM   49039 N  N   . GLY   BA 14 167 ? 24.482  -153.009 63.447  1.00 84.15  ? 167 GLY   b N   1 
ATOM   49040 C  CA  . GLY   BA 14 167 ? 23.110  -153.061 62.908  1.00 85.96  ? 167 GLY   b CA  1 
ATOM   49041 C  C   . GLY   BA 14 167 ? 22.778  -154.444 62.375  1.00 85.42  ? 167 GLY   b C   1 
ATOM   49042 O  O   . GLY   BA 14 167 ? 21.594  -154.832 62.427  1.00 79.61  ? 167 GLY   b O   1 
ATOM   49043 N  N   . SER   BA 14 168 ? 23.793  -155.163 61.885  1.00 86.16  ? 168 SER   b N   1 
ATOM   49044 C  CA  . SER   BA 14 168 ? 23.681  -156.522 61.292  1.00 87.14  ? 168 SER   b CA  1 
ATOM   49045 C  C   . SER   BA 14 168 ? 23.407  -157.576 62.378  1.00 87.75  ? 168 SER   b C   1 
ATOM   49046 O  O   . SER   BA 14 168 ? 22.907  -158.659 62.018  1.00 88.60  ? 168 SER   b O   1 
ATOM   49047 C  CB  . SER   BA 14 168 ? 24.918  -156.862 60.500  1.00 87.27  ? 168 SER   b CB  1 
ATOM   49048 O  OG  . SER   BA 14 168 ? 25.351  -155.746 59.731  1.00 86.21  ? 168 SER   b OG  1 
ATOM   49049 N  N   . SER   BA 14 169 ? 23.732  -157.285 63.645  1.00 84.36  ? 169 SER   b N   1 
ATOM   49050 C  CA  . SER   BA 14 169 ? 23.507  -158.183 64.811  1.00 81.60  ? 169 SER   b CA  1 
ATOM   49051 C  C   . SER   BA 14 169 ? 22.279  -157.725 65.605  1.00 84.80  ? 169 SER   b C   1 
ATOM   49052 O  O   . SER   BA 14 169 ? 21.996  -156.514 65.605  1.00 86.14  ? 169 SER   b O   1 
ATOM   49053 C  CB  . SER   BA 14 169 ? 24.721  -158.237 65.692  1.00 80.36  ? 169 SER   b CB  1 
ATOM   49054 O  OG  . SER   BA 14 169 ? 25.895  -158.423 64.918  1.00 78.87  ? 169 SER   b OG  1 
ATOM   49055 N  N   . GLY   BA 14 170 ? 21.587  -158.663 66.260  1.00 84.11  ? 170 GLY   b N   1 
ATOM   49056 C  CA  . GLY   BA 14 170 ? 20.379  -158.382 67.060  1.00 85.65  ? 170 GLY   b CA  1 
ATOM   49057 C  C   . GLY   BA 14 170 ? 19.606  -159.638 67.421  1.00 86.43  ? 170 GLY   b C   1 
ATOM   49058 O  O   . GLY   BA 14 170 ? 20.181  -160.742 67.346  1.00 81.58  ? 170 GLY   b O   1 
ATOM   49059 N  N   . GLY   BA 14 171 ? 18.336  -159.464 67.798  1.00 90.04  ? 171 GLY   b N   1 
ATOM   49060 C  CA  . GLY   BA 14 171 ? 17.417  -160.547 68.196  1.00 92.00  ? 171 GLY   b CA  1 
ATOM   49061 C  C   . GLY   BA 14 171 ? 17.776  -161.108 69.560  1.00 92.89  ? 171 GLY   b C   1 
ATOM   49062 O  O   . GLY   BA 14 171 ? 18.038  -160.303 70.475  1.00 94.55  ? 171 GLY   b O   1 
ATOM   49063 N  N   . VAL   BA 14 172 ? 17.786  -162.438 69.694  1.00 91.75  ? 172 VAL   b N   1 
ATOM   49064 C  CA  . VAL   BA 14 172 ? 18.118  -163.154 70.962  1.00 90.07  ? 172 VAL   b CA  1 
ATOM   49065 C  C   . VAL   BA 14 172 ? 19.604  -163.522 70.950  1.00 89.71  ? 172 VAL   b C   1 
ATOM   49066 O  O   . VAL   BA 14 172 ? 20.195  -163.592 69.851  1.00 89.09  ? 172 VAL   b O   1 
ATOM   49067 C  CB  . VAL   BA 14 172 ? 17.237  -164.401 71.174  1.00 90.95  ? 172 VAL   b CB  1 
ATOM   49068 C  CG1 . VAL   BA 14 172 ? 15.765  -164.037 71.271  1.00 90.80  ? 172 VAL   b CG1 1 
ATOM   49069 C  CG2 . VAL   BA 14 172 ? 17.452  -165.462 70.103  1.00 92.55  ? 172 VAL   b CG2 1 
ATOM   49070 N  N   . ILE   BA 14 173 ? 20.173  -163.740 72.138  1.00 91.06  ? 173 ILE   b N   1 
ATOM   49071 C  CA  . ILE   BA 14 173 ? 21.520  -164.350 72.336  1.00 92.30  ? 173 ILE   b CA  1 
ATOM   49072 C  C   . ILE   BA 14 173 ? 21.311  -165.835 72.642  1.00 90.90  ? 173 ILE   b C   1 
ATOM   49073 O  O   . ILE   BA 14 173 ? 20.873  -166.154 73.765  1.00 90.94  ? 173 ILE   b O   1 
ATOM   49074 C  CB  . ILE   BA 14 173 ? 22.313  -163.634 73.449  1.00 93.56  ? 173 ILE   b CB  1 
ATOM   49075 C  CG1 . ILE   BA 14 173 ? 22.655  -162.194 73.057  1.00 95.06  ? 173 ILE   b CG1 1 
ATOM   49076 C  CG2 . ILE   BA 14 173 ? 23.559  -164.428 73.821  1.00 94.35  ? 173 ILE   b CG2 1 
ATOM   49077 C  CD1 . ILE   BA 14 173 ? 23.248  -161.364 74.176  1.00 96.51  ? 173 ILE   b CD1 1 
ATOM   49078 N  N   . ARG   BA 14 174 ? 21.585  -166.700 71.665  1.00 89.52  ? 174 ARG   b N   1 
ATOM   49079 C  CA  . ARG   BA 14 174 ? 21.631  -168.171 71.859  1.00 90.38  ? 174 ARG   b CA  1 
ATOM   49080 C  C   . ARG   BA 14 174 ? 23.020  -168.551 72.375  1.00 88.40  ? 174 ARG   b C   1 
ATOM   49081 O  O   . ARG   BA 14 174 ? 24.006  -167.904 71.969  1.00 81.54  ? 174 ARG   b O   1 
ATOM   49082 C  CB  . ARG   BA 14 174 ? 21.336  -168.915 70.554  1.00 90.29  ? 174 ARG   b CB  1 
ATOM   49083 C  CG  . ARG   BA 14 174 ? 20.018  -168.531 69.900  1.00 90.35  ? 174 ARG   b CG  1 
ATOM   49084 C  CD  . ARG   BA 14 174 ? 19.636  -169.528 68.827  1.00 90.09  ? 174 ARG   b CD  1 
ATOM   49085 N  NE  . ARG   BA 14 174 ? 18.415  -169.156 68.124  1.00 89.07  ? 174 ARG   b NE  1 
ATOM   49086 C  CZ  . ARG   BA 14 174 ? 17.175  -169.383 68.561  1.00 90.90  ? 174 ARG   b CZ  1 
ATOM   49087 N  NH1 . ARG   BA 14 174 ? 16.962  -169.981 69.723  1.00 93.41  ? 174 ARG   b NH1 1 
ATOM   49088 N  NH2 . ARG   BA 14 174 ? 16.140  -169.004 67.830  1.00 90.63  ? 174 ARG   b NH2 1 
ATOM   49089 N  N   . MET   BA 14 175 ? 23.084  -169.564 73.239  1.00 90.37  ? 175 MET   b N   1 
ATOM   49090 C  CA  . MET   BA 14 175 ? 24.354  -170.157 73.728  1.00 92.77  ? 175 MET   b CA  1 
ATOM   49091 C  C   . MET   BA 14 175 ? 24.192  -171.677 73.842  1.00 92.21  ? 175 MET   b C   1 
ATOM   49092 O  O   . MET   BA 14 175 ? 23.075  -172.133 74.158  1.00 92.99  ? 175 MET   b O   1 
ATOM   49093 C  CB  . MET   BA 14 175 ? 24.744  -169.568 75.086  1.00 94.65  ? 175 MET   b CB  1 
ATOM   49094 C  CG  . MET   BA 14 175 ? 25.117  -168.098 75.017  1.00 94.24  ? 175 MET   b CG  1 
ATOM   49095 S  SD  . MET   BA 14 175 ? 25.383  -167.357 76.649  1.00 94.87  ? 175 MET   b SD  1 
ATOM   49096 C  CE  . MET   BA 14 175 ? 26.764  -168.346 77.207  1.00 93.57  ? 175 MET   b CE  1 
ATOM   49097 N  N   . VAL   BA 14 176 ? 25.266  -172.423 73.572  1.00 93.13  ? 176 VAL   b N   1 
ATOM   49098 C  CA  . VAL   BA 14 176 ? 25.319  -173.907 73.713  1.00 94.63  ? 176 VAL   b CA  1 
ATOM   49099 C  C   . VAL   BA 14 176 ? 26.510  -174.260 74.606  1.00 94.27  ? 176 VAL   b C   1 
ATOM   49100 O  O   . VAL   BA 14 176 ? 27.645  -173.901 74.239  1.00 96.59  ? 176 VAL   b O   1 
ATOM   49101 C  CB  . VAL   BA 14 176 ? 25.406  -174.612 72.347  1.00 94.07  ? 176 VAL   b CB  1 
ATOM   49102 C  CG1 . VAL   BA 14 176 ? 25.719  -176.091 72.493  1.00 94.33  ? 176 VAL   b CG1 1 
ATOM   49103 C  CG2 . VAL   BA 14 176 ? 24.131  -174.421 71.542  1.00 96.81  ? 176 VAL   b CG2 1 
ATOM   49104 N  N   . VAL   BA 14 177 ? 26.244  -174.943 75.724  1.00 95.38  ? 177 VAL   b N   1 
ATOM   49105 C  CA  . VAL   BA 14 177 ? 27.258  -175.339 76.746  1.00 95.43  ? 177 VAL   b CA  1 
ATOM   49106 C  C   . VAL   BA 14 177 ? 27.687  -176.780 76.451  1.00 94.29  ? 177 VAL   b C   1 
ATOM   49107 O  O   . VAL   BA 14 177 ? 26.807  -177.661 76.427  1.00 97.18  ? 177 VAL   b O   1 
ATOM   49108 C  CB  . VAL   BA 14 177 ? 26.708  -175.197 78.179  1.00 94.54  ? 177 VAL   b CB  1 
ATOM   49109 C  CG1 . VAL   BA 14 177 ? 27.803  -175.360 79.221  1.00 93.23  ? 177 VAL   b CG1 1 
ATOM   49110 C  CG2 . VAL   BA 14 177 ? 25.980  -173.876 78.382  1.00 95.32  ? 177 VAL   b CG2 1 
ATOM   49111 N  N   . LEU   BA 14 178 ? 28.987  -176.993 76.226  1.00 95.70  ? 178 LEU   b N   1 
ATOM   49112 C  CA  . LEU   BA 14 178 ? 29.609  -178.321 75.967  1.00 97.78  ? 178 LEU   b CA  1 
ATOM   49113 C  C   . LEU   BA 14 178 ? 30.486  -178.705 77.166  1.00 98.99  ? 178 LEU   b C   1 
ATOM   49114 O  O   . LEU   BA 14 178 ? 31.538  -178.065 77.359  1.00 98.29  ? 178 LEU   b O   1 
ATOM   49115 C  CB  . LEU   BA 14 178 ? 30.430  -178.239 74.674  1.00 95.00  ? 178 LEU   b CB  1 
ATOM   49116 C  CG  . LEU   BA 14 178 ? 29.767  -178.768 73.400  1.00 92.00  ? 178 LEU   b CG  1 
ATOM   49117 C  CD1 . LEU   BA 14 178 ? 28.296  -178.393 73.317  1.00 91.30  ? 178 LEU   b CD1 1 
ATOM   49118 C  CD2 . LEU   BA 14 178 ? 30.506  -178.263 72.169  1.00 89.79  ? 178 LEU   b CD2 1 
ATOM   49119 N  N   . THR   BA 14 179 ? 30.056  -179.701 77.947  1.00 103.51 ? 179 THR   b N   1 
ATOM   49120 C  CA  . THR   BA 14 179 ? 30.778  -180.236 79.134  1.00 105.62 ? 179 THR   b CA  1 
ATOM   49121 C  C   . THR   BA 14 179 ? 30.641  -181.760 79.177  1.00 107.54 ? 179 THR   b C   1 
ATOM   49122 O  O   . THR   BA 14 179 ? 29.868  -182.296 78.367  1.00 110.34 ? 179 THR   b O   1 
ATOM   49123 C  CB  . THR   BA 14 179 ? 30.236  -179.633 80.435  1.00 107.05 ? 179 THR   b CB  1 
ATOM   49124 O  OG1 . THR   BA 14 179 ? 28.853  -179.971 80.543  1.00 107.41 ? 179 THR   b OG1 1 
ATOM   49125 C  CG2 . THR   BA 14 179 ? 30.403  -178.131 80.498  1.00 106.92 ? 179 THR   b CG2 1 
ATOM   49126 N  N   . ALA   BA 14 180 ? 31.343  -182.416 80.106  1.00 107.99 ? 180 ALA   b N   1 
ATOM   49127 C  CA  . ALA   BA 14 180 ? 31.234  -183.869 80.374  1.00 107.85 ? 180 ALA   b CA  1 
ATOM   49128 C  C   . ALA   BA 14 180 ? 29.779  -184.226 80.711  1.00 110.77 ? 180 ALA   b C   1 
ATOM   49129 O  O   . ALA   BA 14 180 ? 29.352  -185.338 80.349  1.00 111.92 ? 180 ALA   b O   1 
ATOM   49130 C  CB  . ALA   BA 14 180 ? 32.170  -184.267 81.488  1.00 109.92 ? 180 ALA   b CB  1 
ATOM   49131 N  N   . ALA   BA 14 181 ? 29.052  -183.309 81.364  1.00 112.27 ? 181 ALA   b N   1 
ATOM   49132 C  CA  . ALA   BA 14 181 ? 27.651  -183.480 81.825  1.00 114.24 ? 181 ALA   b CA  1 
ATOM   49133 C  C   . ALA   BA 14 181 ? 26.707  -183.694 80.633  1.00 110.14 ? 181 ALA   b C   1 
ATOM   49134 O  O   . ALA   BA 14 181 ? 25.725  -184.446 80.791  1.00 112.49 ? 181 ALA   b O   1 
ATOM   49135 C  CB  . ALA   BA 14 181 ? 27.226  -182.288 82.652  1.00 114.39 ? 181 ALA   b CB  1 
ATOM   49136 N  N   . GLY   BA 14 182 ? 26.985  -183.056 79.491  1.00 106.13 ? 182 GLY   b N   1 
ATOM   49137 C  CA  . GLY   BA 14 182 ? 26.189  -183.198 78.256  1.00 102.78 ? 182 GLY   b CA  1 
ATOM   49138 C  C   . GLY   BA 14 182 ? 26.160  -181.918 77.440  1.00 100.98 ? 182 GLY   b C   1 
ATOM   49139 O  O   . GLY   BA 14 182 ? 27.192  -181.218 77.400  1.00 98.90  ? 182 GLY   b O   1 
ATOM   49140 N  N   . VAL   BA 14 183 ? 25.018  -181.633 76.806  1.00 96.47  ? 183 VAL   b N   1 
ATOM   49141 C  CA  . VAL   BA 14 183 ? 24.792  -180.445 75.928  1.00 95.80  ? 183 VAL   b CA  1 
ATOM   49142 C  C   . VAL   BA 14 183 ? 23.597  -179.654 76.472  1.00 96.64  ? 183 VAL   b C   1 
ATOM   49143 O  O   . VAL   BA 14 183 ? 22.487  -180.222 76.516  1.00 94.56  ? 183 VAL   b O   1 
ATOM   49144 C  CB  . VAL   BA 14 183 ? 24.562  -180.864 74.463  1.00 93.87  ? 183 VAL   b CB  1 
ATOM   49145 C  CG1 . VAL   BA 14 183 ? 24.364  -179.662 73.554  1.00 93.92  ? 183 VAL   b CG1 1 
ATOM   49146 C  CG2 . VAL   BA 14 183 ? 25.692  -181.737 73.942  1.00 93.46  ? 183 VAL   b CG2 1 
ATOM   49147 N  N   . GLU   BA 14 184 ? 23.824  -178.392 76.857  1.00 96.87  ? 184 GLU   b N   1 
ATOM   49148 C  CA  . GLU   BA 14 184 ? 22.788  -177.463 77.383  1.00 100.64 ? 184 GLU   b CA  1 
ATOM   49149 C  C   . GLU   BA 14 184 ? 22.600  -176.307 76.396  1.00 98.62  ? 184 GLU   b C   1 
ATOM   49150 O  O   . GLU   BA 14 184 ? 23.616  -175.742 75.944  1.00 98.76  ? 184 GLU   b O   1 
ATOM   49151 C  CB  . GLU   BA 14 184 ? 23.187  -176.927 78.758  1.00 101.44 ? 184 GLU   b CB  1 
ATOM   49152 C  CG  . GLU   BA 14 184 ? 22.047  -176.246 79.492  1.00 103.10 ? 184 GLU   b CG  1 
ATOM   49153 C  CD  . GLU   BA 14 184 ? 22.424  -175.652 80.837  1.00 106.34 ? 184 GLU   b CD  1 
ATOM   49154 O  OE1 . GLU   BA 14 184 ? 21.600  -174.904 81.398  1.00 108.27 ? 184 GLU   b OE1 1 
ATOM   49155 O  OE2 . GLU   BA 14 184 ? 23.539  -175.938 81.319  1.00 109.86 ? 184 GLU   b OE2 1 
ATOM   49156 N  N   . ARG   BA 14 185 ? 21.342  -175.978 76.087  1.00 102.00 ? 185 ARG   b N   1 
ATOM   49157 C  CA  . ARG   BA 14 185 ? 20.951  -174.825 75.233  1.00 101.25 ? 185 ARG   b CA  1 
ATOM   49158 C  C   . ARG   BA 14 185 ? 20.417  -173.697 76.121  1.00 100.80 ? 185 ARG   b C   1 
ATOM   49159 O  O   . ARG   BA 14 185 ? 19.480  -173.953 76.905  1.00 100.59 ? 185 ARG   b O   1 
ATOM   49160 C  CB  . ARG   BA 14 185 ? 19.891  -175.240 74.209  1.00 101.95 ? 185 ARG   b CB  1 
ATOM   49161 C  CG  . ARG   BA 14 185 ? 20.445  -175.533 72.824  1.00 104.05 ? 185 ARG   b CG  1 
ATOM   49162 C  CD  . ARG   BA 14 185 ? 19.416  -175.229 71.755  1.00 107.76 ? 185 ARG   b CD  1 
ATOM   49163 N  NE  . ARG   BA 14 185 ? 19.927  -175.514 70.424  1.00 113.47 ? 185 ARG   b NE  1 
ATOM   49164 C  CZ  . ARG   BA 14 185 ? 20.582  -174.662 69.635  1.00 114.41 ? 185 ARG   b CZ  1 
ATOM   49165 N  NH1 . ARG   BA 14 185 ? 20.830  -173.420 70.018  1.00 112.36 ? 185 ARG   b NH1 1 
ATOM   49166 N  NH2 . ARG   BA 14 185 ? 20.987  -175.070 68.445  1.00 116.35 ? 185 ARG   b NH2 1 
ATOM   49167 N  N   . LEU   BA 14 186 ? 20.992  -172.499 75.987  1.00 98.97  ? 186 LEU   b N   1 
ATOM   49168 C  CA  . LEU   BA 14 186 ? 20.566  -171.271 76.707  1.00 99.23  ? 186 LEU   b CA  1 
ATOM   49169 C  C   . LEU   BA 14 186 ? 20.092  -170.230 75.691  1.00 98.79  ? 186 LEU   b C   1 
ATOM   49170 O  O   . LEU   BA 14 186 ? 20.692  -170.150 74.602  1.00 96.56  ? 186 LEU   b O   1 
ATOM   49171 C  CB  . LEU   BA 14 186 ? 21.743  -170.728 77.521  1.00 98.91  ? 186 LEU   b CB  1 
ATOM   49172 C  CG  . LEU   BA 14 186 ? 22.277  -171.645 78.618  1.00 99.49  ? 186 LEU   b CG  1 
ATOM   49173 C  CD1 . LEU   BA 14 186 ? 23.559  -171.080 79.207  1.00 99.78  ? 186 LEU   b CD1 1 
ATOM   49174 C  CD2 . LEU   BA 14 186 ? 21.237  -171.855 79.708  1.00 102.95 ? 186 LEU   b CD2 1 
ATOM   49175 N  N   . ILE   BA 14 187 ? 19.061  -169.464 76.056  1.00 103.37 ? 187 ILE   b N   1 
ATOM   49176 C  CA  . ILE   BA 14 187 ? 18.521  -168.316 75.269  1.00 106.13 ? 187 ILE   b CA  1 
ATOM   49177 C  C   . ILE   BA 14 187 ? 18.373  -167.120 76.216  1.00 107.85 ? 187 ILE   b C   1 
ATOM   49178 O  O   . ILE   BA 14 187 ? 17.983  -167.334 77.382  1.00 108.56 ? 187 ILE   b O   1 
ATOM   49179 C  CB  . ILE   BA 14 187 ? 17.192  -168.685 74.574  1.00 108.21 ? 187 ILE   b CB  1 
ATOM   49180 C  CG1 . ILE   BA 14 187 ? 16.732  -167.583 73.614  1.00 107.68 ? 187 ILE   b CG1 1 
ATOM   49181 C  CG2 . ILE   BA 14 187 ? 16.113  -169.038 75.592  1.00 111.13 ? 187 ILE   b CG2 1 
ATOM   49182 C  CD1 . ILE   BA 14 187 ? 15.621  -167.998 72.675  1.00 106.76 ? 187 ILE   b CD1 1 
ATOM   49183 N  N   . PHE   BA 14 188 ? 18.699  -165.918 75.734  1.00 109.68 ? 188 PHE   b N   1 
ATOM   49184 C  CA  . PHE   BA 14 188 ? 18.567  -164.635 76.475  1.00 108.27 ? 188 PHE   b CA  1 
ATOM   49185 C  C   . PHE   BA 14 188 ? 17.892  -163.610 75.561  1.00 108.85 ? 188 PHE   b C   1 
ATOM   49186 O  O   . PHE   BA 14 188 ? 18.342  -163.438 74.411  1.00 106.17 ? 188 PHE   b O   1 
ATOM   49187 C  CB  . PHE   BA 14 188 ? 19.933  -164.175 76.986  1.00 106.52 ? 188 PHE   b CB  1 
ATOM   49188 C  CG  . PHE   BA 14 188 ? 20.592  -165.169 77.907  1.00 106.18 ? 188 PHE   b CG  1 
ATOM   49189 C  CD1 . PHE   BA 14 188 ? 20.114  -165.356 79.194  1.00 109.30 ? 188 PHE   b CD1 1 
ATOM   49190 C  CD2 . PHE   BA 14 188 ? 21.663  -165.939 77.481  1.00 106.42 ? 188 PHE   b CD2 1 
ATOM   49191 C  CE1 . PHE   BA 14 188 ? 20.704  -166.280 80.042  1.00 111.24 ? 188 PHE   b CE1 1 
ATOM   49192 C  CE2 . PHE   BA 14 188 ? 22.254  -166.861 78.332  1.00 106.16 ? 188 PHE   b CE2 1 
ATOM   49193 C  CZ  . PHE   BA 14 188 ? 21.774  -167.031 79.611  1.00 108.80 ? 188 PHE   b CZ  1 
ATOM   49194 N  N   . TYR   BA 14 189 ? 16.836  -162.968 76.066  1.00 111.51 ? 189 TYR   b N   1 
ATOM   49195 C  CA  . TYR   BA 14 189 ? 15.929  -162.072 75.302  1.00 111.86 ? 189 TYR   b CA  1 
ATOM   49196 C  C   . TYR   BA 14 189 ? 16.376  -160.620 75.465  1.00 115.69 ? 189 TYR   b C   1 
ATOM   49197 O  O   . TYR   BA 14 189 ? 17.030  -160.276 76.449  1.00 114.85 ? 189 TYR   b O   1 
ATOM   49198 C  CB  . TYR   BA 14 189 ? 14.484  -162.287 75.760  1.00 112.78 ? 189 TYR   b CB  1 
ATOM   49199 C  CG  . TYR   BA 14 189 ? 14.007  -163.716 75.670  1.00 111.31 ? 189 TYR   b CG  1 
ATOM   49200 C  CD1 . TYR   BA 14 189 ? 13.580  -164.252 74.466  1.00 113.24 ? 189 TYR   b CD1 1 
ATOM   49201 C  CD2 . TYR   BA 14 189 ? 13.981  -164.536 76.787  1.00 108.85 ? 189 TYR   b CD2 1 
ATOM   49202 C  CE1 . TYR   BA 14 189 ? 13.139  -165.563 74.373  1.00 113.19 ? 189 TYR   b CE1 1 
ATOM   49203 C  CE2 . TYR   BA 14 189 ? 13.543  -165.848 76.712  1.00 108.72 ? 189 TYR   b CE2 1 
ATOM   49204 C  CZ  . TYR   BA 14 189 ? 13.120  -166.365 75.500  1.00 110.28 ? 189 TYR   b CZ  1 
ATOM   49205 O  OH  . TYR   BA 14 189 ? 12.688  -167.657 75.423  1.00 109.54 ? 189 TYR   b OH  1 
ATOM   49206 N  N   . PRO   BA 14 190 ? 16.042  -159.730 74.500  1.00 115.28 ? 190 PRO   b N   1 
ATOM   49207 C  CA  . PRO   BA 14 190 ? 16.438  -158.322 74.559  1.00 115.25 ? 190 PRO   b CA  1 
ATOM   49208 C  C   . PRO   BA 14 190 ? 16.249  -157.661 75.933  1.00 119.43 ? 190 PRO   b C   1 
ATOM   49209 O  O   . PRO   BA 14 190 ? 17.185  -157.045 76.408  1.00 124.20 ? 190 PRO   b O   1 
ATOM   49210 C  CB  . PRO   BA 14 190 ? 15.506  -157.671 73.528  1.00 116.12 ? 190 PRO   b CB  1 
ATOM   49211 C  CG  . PRO   BA 14 190 ? 15.309  -158.748 72.489  1.00 113.83 ? 190 PRO   b CG  1 
ATOM   49212 C  CD  . PRO   BA 14 190 ? 15.280  -160.039 73.279  1.00 114.29 ? 190 PRO   b CD  1 
ATOM   49213 N  N   . ASP   BA 14 191 ? 15.066  -157.822 76.535  1.00 119.82 ? 191 ASP   b N   1 
ATOM   49214 C  CA  . ASP   BA 14 191 ? 14.655  -157.126 77.786  1.00 120.08 ? 191 ASP   b CA  1 
ATOM   49215 C  C   . ASP   BA 14 191 ? 15.671  -157.396 78.906  1.00 120.76 ? 191 ASP   b C   1 
ATOM   49216 O  O   . ASP   BA 14 191 ? 15.778  -156.540 79.806  1.00 122.14 ? 191 ASP   b O   1 
ATOM   49217 C  CB  . ASP   BA 14 191 ? 13.232  -157.511 78.197  1.00 120.08 ? 191 ASP   b CB  1 
ATOM   49218 C  CG  . ASP   BA 14 191 ? 12.167  -156.930 77.281  1.00 119.11 ? 191 ASP   b CG  1 
ATOM   49219 O  OD1 . ASP   BA 14 191 ? 12.081  -155.691 77.196  1.00 118.15 ? 191 ASP   b OD1 1 
ATOM   49220 O  OD2 . ASP   BA 14 191 ? 11.446  -157.722 76.646  1.00 125.14 ? 191 ASP   b OD2 1 
ATOM   49221 N  N   . GLU   BA 14 192 ? 16.388  -158.524 78.857  1.00 118.60 ? 192 GLU   b N   1 
ATOM   49222 C  CA  . GLU   BA 14 192 ? 17.492  -158.832 79.806  1.00 121.39 ? 192 GLU   b CA  1 
ATOM   49223 C  C   . GLU   BA 14 192 ? 18.783  -158.134 79.356  1.00 118.67 ? 192 GLU   b C   1 
ATOM   49224 O  O   . GLU   BA 14 192 ? 19.280  -157.288 80.123  1.00 125.64 ? 192 GLU   b O   1 
ATOM   49225 C  CB  . GLU   BA 14 192 ? 17.717  -160.339 79.936  1.00 122.06 ? 192 GLU   b CB  1 
ATOM   49226 C  CG  . GLU   BA 14 192 ? 18.746  -160.697 80.996  1.00 127.35 ? 192 GLU   b CG  1 
ATOM   49227 C  CD  . GLU   BA 14 192 ? 18.950  -162.186 81.220  1.00 130.46 ? 192 GLU   b CD  1 
ATOM   49228 O  OE1 . GLU   BA 14 192 ? 19.891  -162.545 81.956  1.00 135.78 ? 192 GLU   b OE1 1 
ATOM   49229 O  OE2 . GLU   BA 14 192 ? 18.168  -162.984 80.662  1.00 135.86 ? 192 GLU   b OE2 1 
ATOM   49230 N  N   . TYR   BA 14 193 ? 19.311  -158.474 78.174  1.00 114.25 ? 193 TYR   b N   1 
ATOM   49231 C  CA  . TYR   BA 14 193 ? 20.705  -158.142 77.766  1.00 111.29 ? 193 TYR   b CA  1 
ATOM   49232 C  C   . TYR   BA 14 193 ? 20.840  -156.652 77.413  1.00 112.69 ? 193 TYR   b C   1 
ATOM   49233 O  O   . TYR   BA 14 193 ? 21.934  -156.109 77.664  1.00 110.61 ? 193 TYR   b O   1 
ATOM   49234 C  CB  . TYR   BA 14 193 ? 21.215  -159.086 76.667  1.00 108.34 ? 193 TYR   b CB  1 
ATOM   49235 C  CG  . TYR   BA 14 193 ? 20.697  -158.881 75.264  1.00 105.17 ? 193 TYR   b CG  1 
ATOM   49236 C  CD1 . TYR   BA 14 193 ? 21.118  -157.811 74.488  1.00 107.71 ? 193 TYR   b CD1 1 
ATOM   49237 C  CD2 . TYR   BA 14 193 ? 19.845  -159.804 74.676  1.00 103.46 ? 193 TYR   b CD2 1 
ATOM   49238 C  CE1 . TYR   BA 14 193 ? 20.667  -157.634 73.190  1.00 109.42 ? 193 TYR   b CE1 1 
ATOM   49239 C  CE2 . TYR   BA 14 193 ? 19.388  -159.645 73.377  1.00 104.36 ? 193 TYR   b CE2 1 
ATOM   49240 C  CZ  . TYR   BA 14 193 ? 19.799  -158.554 72.632  1.00 107.40 ? 193 TYR   b CZ  1 
ATOM   49241 O  OH  . TYR   BA 14 193 ? 19.359  -158.381 71.352  1.00 114.23 ? 193 TYR   b OH  1 
ATOM   49242 N  N   . GLU   BA 14 194 ? 19.791  -156.011 76.879  1.00 114.17 ? 194 GLU   b N   1 
ATOM   49243 C  CA  . GLU   BA 14 194 ? 19.841  -154.606 76.376  1.00 116.23 ? 194 GLU   b CA  1 
ATOM   49244 C  C   . GLU   BA 14 194 ? 20.236  -153.644 77.506  1.00 118.36 ? 194 GLU   b C   1 
ATOM   49245 O  O   . GLU   BA 14 194 ? 20.952  -152.666 77.209  1.00 119.87 ? 194 GLU   b O   1 
ATOM   49246 C  CB  . GLU   BA 14 194 ? 18.509  -154.175 75.752  1.00 115.32 ? 194 GLU   b CB  1 
ATOM   49247 C  CG  . GLU   BA 14 194 ? 18.372  -154.564 74.288  1.00 116.47 ? 194 GLU   b CG  1 
ATOM   49248 C  CD  . GLU   BA 14 194 ? 17.105  -154.081 73.600  1.00 118.93 ? 194 GLU   b CD  1 
ATOM   49249 O  OE1 . GLU   BA 14 194 ? 16.819  -154.570 72.487  1.00 115.50 ? 194 GLU   b OE1 1 
ATOM   49250 O  OE2 . GLU   BA 14 194 ? 16.410  -153.214 74.170  1.00 126.30 ? 194 GLU   b OE2 1 
ATOM   49251 N  N   . GLN   BA 14 195 ? 19.802  -153.911 78.744  1.00 119.37 ? 195 GLN   b N   1 
ATOM   49252 C  CA  . GLN   BA 14 195 ? 19.984  -152.995 79.905  1.00 122.47 ? 195 GLN   b CA  1 
ATOM   49253 C  C   . GLN   BA 14 195 ? 21.125  -153.483 80.810  1.00 122.17 ? 195 GLN   b C   1 
ATOM   49254 O  O   . GLN   BA 14 195 ? 21.155  -153.064 81.983  1.00 127.45 ? 195 GLN   b O   1 
ATOM   49255 C  CB  . GLN   BA 14 195 ? 18.677  -152.846 80.688  1.00 122.95 ? 195 GLN   b CB  1 
ATOM   49256 C  CG  . GLN   BA 14 195 ? 18.172  -154.138 81.314  1.00 125.89 ? 195 GLN   b CG  1 
ATOM   49257 C  CD  . GLN   BA 14 195 ? 16.853  -153.944 82.023  1.00 130.72 ? 195 GLN   b CD  1 
ATOM   49258 O  OE1 . GLN   BA 14 195 ? 16.116  -152.997 81.756  1.00 130.70 ? 195 GLN   b OE1 1 
ATOM   49259 N  NE2 . GLN   BA 14 195 ? 16.543  -154.851 82.936  1.00 136.91 ? 195 GLN   b NE2 1 
ATOM   49260 N  N   . LEU   BA 14 196 ? 22.035  -154.319 80.296  1.00 122.89 ? 196 LEU   b N   1 
ATOM   49261 C  CA  . LEU   BA 14 196 ? 23.289  -154.697 81.004  1.00 127.42 ? 196 LEU   b CA  1 
ATOM   49262 C  C   . LEU   BA 14 196 ? 24.227  -153.484 81.033  1.00 131.44 ? 196 LEU   b C   1 
ATOM   49263 O  O   . LEU   BA 14 196 ? 24.182  -152.616 80.157  1.00 137.56 ? 196 LEU   b O   1 
ATOM   49264 C  CB  . LEU   BA 14 196 ? 23.954  -155.887 80.302  1.00 122.19 ? 196 LEU   b CB  1 
ATOM   49265 C  CG  . LEU   BA 14 196 ? 23.319  -157.254 80.553  1.00 119.67 ? 196 LEU   b CG  1 
ATOM   49266 C  CD1 . LEU   BA 14 196 ? 23.865  -158.285 79.578  1.00 118.68 ? 196 LEU   b CD1 1 
ATOM   49267 C  CD2 . LEU   BA 14 196 ? 23.547  -157.710 81.987  1.00 119.54 ? 196 LEU   b CD2 1 
ATOM   49268 O  OXT . LEU   BA 14 196 ? 25.052  -153.350 81.937  1.00 138.44 ? 196 LEU   b OXT 1 
HETATM 49269 MG MG  . MG    CA 15 .   ? 40.747  -88.396  49.619  1.00 84.52  ? 301 MG    G MG  1 
HETATM 49270 C  C5  . A1H71 DA 16 .   ? 59.532  -139.300 41.309  1.00 102.41 ? 301 A1H71 H C5  1 
HETATM 49271 C  C6  . A1H71 DA 16 .   ? 59.095  -138.976 39.913  1.00 100.77 ? 301 A1H71 H C6  1 
HETATM 49272 C  C7  . A1H71 DA 16 .   ? 59.610  -137.614 39.536  1.00 100.62 ? 301 A1H71 H C7  1 
HETATM 49273 C  C8  . A1H71 DA 16 .   ? 61.012  -137.723 39.052  1.00 99.76  ? 301 A1H71 H C8  1 
HETATM 49274 C  C15 . A1H71 DA 16 .   ? 58.496  -134.499 33.602  1.00 96.22  ? 301 A1H71 H C15 1 
HETATM 49275 C  C17 . A1H71 DA 16 .   ? 56.546  -133.923 34.988  1.00 83.01  ? 301 A1H71 H C17 1 
HETATM 49276 C  C21 . A1H71 DA 16 .   ? 63.061  -134.822 35.231  1.00 96.94  ? 301 A1H71 H C21 1 
HETATM 49277 C  C28 . A1H71 DA 16 .   ? 63.575  -136.227 42.128  1.00 106.15 ? 301 A1H71 H C28 1 
HETATM 49278 C  C19 . A1H71 DA 16 .   ? 54.199  -133.975 34.231  1.00 82.66  ? 301 A1H71 H C19 1 
HETATM 49279 C  C18 . A1H71 DA 16 .   ? 55.139  -134.325 35.370  1.00 82.50  ? 301 A1H71 H C18 1 
HETATM 49280 C  C16 . A1H71 DA 16 .   ? 57.094  -134.913 33.991  1.00 82.89  ? 301 A1H71 H C16 1 
HETATM 49281 C  C14 . A1H71 DA 16 .   ? 59.462  -135.256 34.472  1.00 95.49  ? 301 A1H71 H C14 1 
HETATM 49282 O  O20 . A1H71 DA 16 .   ? 59.103  -136.259 35.056  1.00 99.00  ? 301 A1H71 H O20 1 
HETATM 49283 N  N13 . A1H71 DA 16 .   ? 60.677  -134.744 34.574  1.00 96.81  ? 301 A1H71 H N13 1 
HETATM 49284 C  C12 . A1H71 DA 16 .   ? 61.673  -135.423 35.378  1.00 95.38  ? 301 A1H71 H C12 1 
HETATM 49285 C  C23 . A1H71 DA 16 .   ? 63.074  -133.719 34.202  1.00 96.97  ? 301 A1H71 H C23 1 
HETATM 49286 O  O22 . A1H71 DA 16 .   ? 63.498  -134.324 36.456  1.00 100.72 ? 301 A1H71 H O22 1 
HETATM 49287 C  C11 . A1H71 DA 16 .   ? 61.186  -135.511 36.803  1.00 95.97  ? 301 A1H71 H C11 1 
HETATM 49288 O  O24 . A1H71 DA 16 .   ? 60.084  -135.117 37.117  1.00 96.24  ? 301 A1H71 H O24 1 
HETATM 49289 N  N10 . A1H71 DA 16 .   ? 62.007  -136.122 37.628  1.00 97.53  ? 301 A1H71 H N10 1 
HETATM 49290 C  C9  . A1H71 DA 16 .   ? 61.624  -136.377 39.005  1.00 101.67 ? 301 A1H71 H C9  1 
HETATM 49291 C  C25 . A1H71 DA 16 .   ? 62.708  -136.407 39.838  1.00 99.45  ? 301 A1H71 H C25 1 
HETATM 49292 O  O26 . A1H71 DA 16 .   ? 63.851  -136.581 39.445  1.00 97.11  ? 301 A1H71 H O26 1 
HETATM 49293 N  N27 . A1H71 DA 16 .   ? 62.475  -136.267 41.178  1.00 101.31 ? 301 A1H71 H N27 1 
HETATM 49294 N  N4  . A1H71 DA 16 .   ? 60.970  -139.058 41.431  1.00 105.31 ? 301 A1H71 H N4  1 
HETATM 49295 C  C3  . A1H71 DA 16 .   ? 61.579  -138.724 42.632  1.00 103.10 ? 301 A1H71 H C3  1 
HETATM 49296 O  O37 . A1H71 DA 16 .   ? 60.927  -138.675 43.666  1.00 95.06  ? 301 A1H71 H O37 1 
HETATM 49297 C  C2  . A1H71 DA 16 .   ? 62.945  -138.527 42.624  1.00 106.46 ? 301 A1H71 H C2  1 
HETATM 49298 C  C1  . A1H71 DA 16 .   ? 63.342  -137.213 43.202  1.00 105.74 ? 301 A1H71 H C1  1 
HETATM 49299 O  OG1 . A1H71 DA 16 .   ? 64.567  -137.374 43.865  1.00 111.53 ? 301 A1H71 H OG1 1 
HETATM 49300 C  CB  . A1H71 DA 16 .   ? 64.295  -138.154 45.009  1.00 115.34 ? 301 A1H71 H CB  1 
HETATM 49301 C  CG2 . A1H71 DA 16 .   ? 63.929  -137.231 46.148  1.00 113.99 ? 301 A1H71 H CG2 1 
HETATM 49302 C  CA  . A1H71 DA 16 .   ? 65.532  -138.927 45.389  1.00 116.74 ? 301 A1H71 H CA  1 
HETATM 49303 C  C   . A1H71 DA 16 .   ? 65.456  -139.266 46.842  1.00 114.19 ? 301 A1H71 H C   1 
HETATM 49304 O  O   . A1H71 DA 16 .   ? 64.416  -139.678 47.336  1.00 114.08 ? 301 A1H71 H O   1 
HETATM 49305 N  N   . A1H71 DA 16 .   ? 65.573  -140.201 44.679  1.00 121.66 ? 301 A1H71 H N   1 
HETATM 49306 C  C29 . A1H71 DA 16 .   ? 63.572  -134.868 42.826  1.00 105.36 ? 301 A1H71 H C29 1 
HETATM 49307 C  C30 . A1H71 DA 16 .   ? 64.386  -133.916 42.226  1.00 87.86  ? 301 A1H71 H C30 1 
HETATM 49308 C  C35 . A1H71 DA 16 .   ? 64.140  -132.582 42.454  1.00 87.34  ? 301 A1H71 H C35 1 
HETATM 49309 C  C34 . A1H71 DA 16 .   ? 64.934  -131.614 41.878  1.00 86.85  ? 301 A1H71 H C34 1 
HETATM 49310 C  C33 . A1H71 DA 16 .   ? 65.984  -131.975 41.067  1.00 87.19  ? 301 A1H71 H C33 1 
HETATM 49311 C  C32 . A1H71 DA 16 .   ? 66.243  -133.305 40.836  1.00 87.91  ? 301 A1H71 H C32 1 
HETATM 49312 C  C31 . A1H71 DA 16 .   ? 65.443  -134.271 41.417  1.00 88.34  ? 301 A1H71 H C31 1 
HETATM 49313 MG MG  . MG    EA 15 .   ? 40.854  -132.987 49.262  1.00 102.46 ? 302 MG    H MG  1 
HETATM 49314 MG MG  . MG    FA 15 .   ? 65.521  -143.256 10.672  1.00 103.88 ? 301 MG    I MG  1 
HETATM 49315 C  C5  . A1H71 GA 16 .   ? 15.442  -140.028 14.431  1.00 99.81  ? 301 A1H71 K C5  1 
HETATM 49316 C  C6  . A1H71 GA 16 .   ? 15.195  -140.419 15.832  1.00 104.53 ? 301 A1H71 K C6  1 
HETATM 49317 C  C7  . A1H71 GA 16 .   ? 14.318  -139.378 16.440  1.00 101.93 ? 301 A1H71 K C7  1 
HETATM 49318 C  C8  . A1H71 GA 16 .   ? 12.908  -139.694 16.134  1.00 98.61  ? 301 A1H71 K C8  1 
HETATM 49319 C  C15 . A1H71 GA 16 .   ? 11.603  -137.357 22.428  1.00 92.64  ? 301 A1H71 K C15 1 
HETATM 49320 C  C17 . A1H71 GA 16 .   ? 13.007  -136.476 24.194  1.00 87.13  ? 301 A1H71 K C17 1 
HETATM 49321 C  C21 . A1H71 GA 16 .   ? 8.767   -137.414 18.741  1.00 92.90  ? 301 A1H71 K C21 1 
HETATM 49322 C  C28 . A1H71 GA 16 .   ? 11.474  -138.029 12.444  1.00 96.99  ? 301 A1H71 K C28 1 
HETATM 49323 C  C19 . A1H71 GA 16 .   ? 14.033  -137.020 26.338  1.00 89.59  ? 301 A1H71 K C19 1 
HETATM 49324 C  C18 . A1H71 GA 16 .   ? 14.333  -136.680 24.890  1.00 88.51  ? 301 A1H71 K C18 1 
HETATM 49325 C  C16 . A1H71 GA 16 .   ? 13.040  -137.106 22.816  1.00 86.30  ? 301 A1H71 K C16 1 
HETATM 49326 C  C14 . A1H71 GA 16 .   ? 11.550  -137.766 20.992  1.00 90.11  ? 301 A1H71 K C14 1 
HETATM 49327 O  O20 . A1H71 GA 16 .   ? 12.566  -138.102 20.406  1.00 89.50  ? 301 A1H71 K O20 1 
HETATM 49328 N  N13 . A1H71 GA 16 .   ? 10.334  -137.700 20.474  1.00 91.86  ? 301 A1H71 K N13 1 
HETATM 49329 C  C12 . A1H71 GA 16 .   ? 10.008  -138.116 19.125  1.00 91.82  ? 301 A1H71 K C12 1 
HETATM 49330 C  C23 . A1H71 GA 16 .   ? 7.754   -137.623 19.839  1.00 95.39  ? 301 A1H71 K C23 1 
HETATM 49331 O  O22 . A1H71 GA 16 .   ? 9.131   -136.085 18.769  1.00 92.64  ? 301 A1H71 K O22 1 
HETATM 49332 C  C11 . A1H71 GA 16 .   ? 11.091  -137.738 18.172  1.00 92.07  ? 301 A1H71 K C11 1 
HETATM 49333 O  O24 . A1H71 GA 16 .   ? 11.799  -136.780 18.365  1.00 87.63  ? 301 A1H71 K O24 1 
HETATM 49334 N  N10 . A1H71 GA 16 .   ? 11.170  -138.552 17.155  1.00 92.69  ? 301 A1H71 K N10 1 
HETATM 49335 C  C9  . A1H71 GA 16 .   ? 12.132  -138.457 16.072  1.00 96.35  ? 301 A1H71 K C9  1 
HETATM 49336 C  C25 . A1H71 GA 16 .   ? 11.500  -138.454 14.845  1.00 94.94  ? 301 A1H71 K C25 1 
HETATM 49337 O  O26 . A1H71 GA 16 .   ? 10.344  -138.819 14.690  1.00 98.48  ? 301 A1H71 K O26 1 
HETATM 49338 N  N27 . A1H71 GA 16 .   ? 12.193  -138.077 13.720  1.00 96.22  ? 301 A1H71 K N27 1 
HETATM 49339 N  N4  . A1H71 GA 16 .   ? 14.172  -140.092 13.757  1.00 97.67  ? 301 A1H71 K N4  1 
HETATM 49340 C  C3  . A1H71 GA 16 .   ? 14.042  -139.710 12.460  1.00 94.90  ? 301 A1H71 K C3  1 
HETATM 49341 O  O37 . A1H71 GA 16 .   ? 15.018  -139.348 11.819  1.00 90.23  ? 301 A1H71 K O37 1 
HETATM 49342 C  C2  . A1H71 GA 16 .   ? 12.809  -139.884 11.898  1.00 97.85  ? 301 A1H71 K C2  1 
HETATM 49343 C  C1  . A1H71 GA 16 .   ? 12.261  -138.636 11.389  1.00 96.26  ? 301 A1H71 K C1  1 
HETATM 49344 O  OG1 . A1H71 GA 16 .   ? 11.368  -138.956 10.368  1.00 97.64  ? 301 A1H71 K OG1 1 
HETATM 49345 C  CB  . A1H71 GA 16 .   ? 12.203  -139.466 9.366   1.00 97.09  ? 301 A1H71 K CB  1 
HETATM 49346 C  CG2 . A1H71 GA 16 .   ? 12.661  -138.285 8.534   1.00 96.65  ? 301 A1H71 K CG2 1 
HETATM 49347 C  CA  . A1H71 GA 16 .   ? 11.455  -140.487 8.532   1.00 98.74  ? 301 A1H71 K CA  1 
HETATM 49348 C  C   . A1H71 GA 16 .   ? 12.016  -140.424 7.155   1.00 98.16  ? 301 A1H71 K C   1 
HETATM 49349 O  O   . A1H71 GA 16 .   ? 13.194  -140.663 6.947   1.00 94.10  ? 301 A1H71 K O   1 
HETATM 49350 N  N   . A1H71 GA 16 .   ? 11.715  -141.818 9.051   1.00 101.35 ? 301 A1H71 K N   1 
HETATM 49351 C  C29 . A1H71 GA 16 .   ? 11.295  -136.600 11.987  1.00 96.09  ? 301 A1H71 K C29 1 
HETATM 49352 C  C30 . A1H71 GA 16 .   ? 10.193  -136.026 12.559  1.00 81.54  ? 301 A1H71 K C30 1 
HETATM 49353 C  C35 . A1H71 GA 16 .   ? 9.992   -134.673 12.415  1.00 80.92  ? 301 A1H71 K C35 1 
HETATM 49354 C  C34 . A1H71 GA 16 .   ? 8.887   -134.084 12.991  1.00 81.12  ? 301 A1H71 K C34 1 
HETATM 49355 C  C33 . A1H71 GA 16 .   ? 7.985   -134.838 13.706  1.00 81.86  ? 301 A1H71 K C33 1 
HETATM 49356 C  C32 . A1H71 GA 16 .   ? 8.193   -136.191 13.843  1.00 82.56  ? 301 A1H71 K C32 1 
HETATM 49357 C  C31 . A1H71 GA 16 .   ? 9.296   -136.786 13.267  1.00 82.26  ? 301 A1H71 K C31 1 
HETATM 49358 MG MG  . MG    HA 15 .   ? 7.241   -148.480 6.606   1.00 90.60  ? 302 MG    K MG  1 
HETATM 49359 MG MG  . MG    IA 15 .   ? 49.642  -150.960 67.163  1.00 83.70  ? 201 MG    N MG  1 
HETATM 49360 C  C5  . A1H71 JA 16 .   ? 10.461  -161.056 39.724  1.00 105.09 ? 301 A1H71 V C5  1 
HETATM 49361 C  C6  . A1H71 JA 16 .   ? 10.886  -161.112 38.286  1.00 107.18 ? 301 A1H71 V C6  1 
HETATM 49362 C  C7  . A1H71 JA 16 .   ? 10.385  -162.388 37.636  1.00 106.55 ? 301 A1H71 V C7  1 
HETATM 49363 C  C8  . A1H71 JA 16 .   ? 8.935   -162.244 37.299  1.00 103.53 ? 301 A1H71 V C8  1 
HETATM 49364 C  C15 . A1H71 JA 16 .   ? 11.193  -164.287 31.410  1.00 90.69  ? 301 A1H71 V C15 1 
HETATM 49365 C  C17 . A1H71 JA 16 .   ? 13.594  -164.791 31.262  1.00 81.96  ? 301 A1H71 V C17 1 
HETATM 49366 C  C21 . A1H71 JA 16 .   ? 6.601   -164.480 32.945  1.00 98.35  ? 301 A1H71 V C21 1 
HETATM 49367 C  C28 . A1H71 JA 16 .   ? 6.422   -163.936 40.254  1.00 97.56  ? 301 A1H71 V C28 1 
HETATM 49368 C  C19 . A1H71 JA 16 .   ? 16.035  -165.053 31.097  1.00 81.86  ? 301 A1H71 V C19 1 
HETATM 49369 C  C18 . A1H71 JA 16 .   ? 14.863  -164.967 32.067  1.00 81.75  ? 301 A1H71 V C18 1 
HETATM 49370 C  C16 . A1H71 JA 16 .   ? 12.471  -164.444 32.199  1.00 81.65  ? 301 A1H71 V C16 1 
HETATM 49371 C  C14 . A1H71 JA 16 .   ? 10.180  -163.833 32.408  1.00 94.81  ? 301 A1H71 V C14 1 
HETATM 49372 O  O20 . A1H71 JA 16 .   ? 10.508  -163.069 33.291  1.00 99.34  ? 301 A1H71 V O20 1 
HETATM 49373 N  N13 . A1H71 JA 16 .   ? 8.966   -164.312 32.292  1.00 93.28  ? 301 A1H71 V N13 1 
HETATM 49374 C  C12 . A1H71 JA 16 .   ? 7.959   -163.886 33.254  1.00 97.47  ? 301 A1H71 V C12 1 
HETATM 49375 C  C23 . A1H71 JA 16 .   ? 6.709   -165.621 31.961  1.00 101.57 ? 301 A1H71 V C23 1 
HETATM 49376 O  O22 . A1H71 JA 16 .   ? 6.005   -164.928 34.132  1.00 101.72 ? 301 A1H71 V O22 1 
HETATM 49377 C  C11 . A1H71 JA 16 .   ? 8.462   -164.153 34.666  1.00 99.57  ? 301 A1H71 V C11 1 
HETATM 49378 O  O24 . A1H71 JA 16 .   ? 9.461   -164.819 34.827  1.00 97.07  ? 301 A1H71 V O24 1 
HETATM 49379 N  N10 . A1H71 JA 16 .   ? 7.845   -163.507 35.651  1.00 99.37  ? 301 A1H71 V N10 1 
HETATM 49380 C  C9  . A1H71 JA 16 .   ? 8.293   -163.550 37.044  1.00 101.14 ? 301 A1H71 V C9  1 
HETATM 49381 C  C25 . A1H71 JA 16 .   ? 7.258   -163.593 37.941  1.00 97.12  ? 301 A1H71 V C25 1 
HETATM 49382 O  O26 . A1H71 JA 16 .   ? 6.119   -163.313 37.624  1.00 93.56  ? 301 A1H71 V O26 1 
HETATM 49383 N  N27 . A1H71 JA 16 .   ? 7.513   -163.877 39.272  1.00 96.54  ? 301 A1H71 V N27 1 
HETATM 49384 N  N4  . A1H71 JA 16 .   ? 9.011   -161.183 39.812  1.00 104.25 ? 301 A1H71 V N4  1 
HETATM 49385 C  C3  . A1H71 JA 16 .   ? 8.426   -161.605 40.988  1.00 101.47 ? 301 A1H71 V C3  1 
HETATM 49386 O  O37 . A1H71 JA 16 .   ? 9.120   -161.837 41.962  1.00 103.12 ? 301 A1H71 V O37 1 
HETATM 49387 C  C2  . A1H71 JA 16 .   ? 7.067   -161.728 41.059  1.00 103.15 ? 301 A1H71 V C2  1 
HETATM 49388 C  C1  . A1H71 JA 16 .   ? 6.701   -163.104 41.457  1.00 99.38  ? 301 A1H71 V C1  1 
HETATM 49389 O  OG1 . A1H71 JA 16 .   ? 5.490   -163.029 42.141  1.00 103.87 ? 301 A1H71 V OG1 1 
HETATM 49390 C  CB  . A1H71 JA 16 .   ? 5.707   -162.785 43.506  1.00 107.88 ? 301 A1H71 V CB  1 
HETATM 49391 C  CG2 . A1H71 JA 16 .   ? 5.533   -164.095 44.205  1.00 109.24 ? 301 A1H71 V CG2 1 
HETATM 49392 C  CA  . A1H71 JA 16 .   ? 4.622   -161.896 44.035  1.00 111.01 ? 301 A1H71 V CA  1 
HETATM 49393 C  C   . A1H71 JA 16 .   ? 4.626   -161.915 45.538  1.00 108.02 ? 301 A1H71 V C   1 
HETATM 49394 O  O   . A1H71 JA 16 .   ? 5.593   -161.513 46.150  1.00 104.69 ? 301 A1H71 V O   1 
HETATM 49395 N  N   . A1H71 JA 16 .   ? 4.930   -160.545 43.630  1.00 113.07 ? 301 A1H71 V N   1 
HETATM 49396 C  C29 . A1H71 JA 16 .   ? 6.273   -165.337 40.810  1.00 97.44  ? 301 A1H71 V C29 1 
HETATM 49397 C  C30 . A1H71 JA 16 .   ? 5.577   -166.226 40.003  1.00 81.55  ? 301 A1H71 V C30 1 
HETATM 49398 C  C35 . A1H71 JA 16 .   ? 5.852   -167.572 40.087  1.00 81.60  ? 301 A1H71 V C35 1 
HETATM 49399 C  C34 . A1H71 JA 16 .   ? 5.169   -168.476 39.303  1.00 81.78  ? 301 A1H71 V C34 1 
HETATM 49400 C  C33 . A1H71 JA 16 .   ? 4.203   -168.057 38.420  1.00 81.85  ? 301 A1H71 V C33 1 
HETATM 49401 C  C32 . A1H71 JA 16 .   ? 3.917   -166.721 38.334  1.00 81.90  ? 301 A1H71 V C32 1 
HETATM 49402 C  C31 . A1H71 JA 16 .   ? 4.606   -165.814 39.121  1.00 81.95  ? 301 A1H71 V C31 1 
HETATM 49403 MG MG  . MG    KA 15 .   ? -0.809  -153.611 44.419  1.00 127.15 ? 302 MG    V MG  1 
HETATM 49404 C  C5  . A1H71 LA 16 .   ? 53.344  -155.131 12.913  1.00 93.32  ? 301 A1H71 Y C5  1 
HETATM 49405 C  C6  . A1H71 LA 16 .   ? 53.623  -155.218 14.373  1.00 97.18  ? 301 A1H71 Y C6  1 
HETATM 49406 C  C7  . A1H71 LA 16 .   ? 54.479  -156.426 14.623  1.00 97.59  ? 301 A1H71 Y C7  1 
HETATM 49407 C  C8  . A1H71 LA 16 .   ? 55.907  -156.126 14.289  1.00 100.17 ? 301 A1H71 Y C8  1 
HETATM 49408 C  C15 . A1H71 LA 16 .   ? 57.102  -160.231 19.876  1.00 97.83  ? 301 A1H71 Y C15 1 
HETATM 49409 C  C17 . A1H71 LA 16 .   ? 55.978  -160.346 21.999  1.00 81.42  ? 301 A1H71 Y C17 1 
HETATM 49410 C  C21 . A1H71 LA 16 .   ? 60.072  -158.464 16.553  1.00 100.20 ? 301 A1H71 Y C21 1 
HETATM 49411 C  C28 . A1H71 LA 16 .   ? 57.247  -157.039 10.477  1.00 97.94  ? 301 A1H71 Y C28 1 
HETATM 49412 C  C19 . A1H71 LA 16 .   ? 54.737  -159.945 24.072  1.00 83.76  ? 301 A1H71 Y C19 1 
HETATM 49413 C  C18 . A1H71 LA 16 .   ? 54.644  -160.542 22.676  1.00 82.57  ? 301 A1H71 Y C18 1 
HETATM 49414 C  C16 . A1H71 LA 16 .   ? 55.758  -160.067 20.533  1.00 80.37  ? 301 A1H71 Y C16 1 
HETATM 49415 C  C14 . A1H71 LA 16 .   ? 57.228  -159.249 18.756  1.00 97.47  ? 301 A1H71 Y C14 1 
HETATM 49416 O  O20 . A1H71 LA 16 .   ? 56.265  -158.588 18.401  1.00 96.12  ? 301 A1H71 Y O20 1 
HETATM 49417 N  N13 . A1H71 LA 16 .   ? 58.434  -159.187 18.215  1.00 97.69  ? 301 A1H71 Y N13 1 
HETATM 49418 C  C12 . A1H71 LA 16 .   ? 58.694  -158.259 17.139  1.00 99.99  ? 301 A1H71 Y C12 1 
HETATM 49419 C  C23 . A1H71 LA 16 .   ? 60.998  -158.972 17.631  1.00 100.04 ? 301 A1H71 Y C23 1 
HETATM 49420 O  O22 . A1H71 LA 16 .   ? 60.014  -159.406 15.521  1.00 98.00  ? 301 A1H71 Y O22 1 
HETATM 49421 C  C11 . A1H71 LA 16 .   ? 57.644  -158.432 16.084  1.00 100.67 ? 301 A1H71 Y C11 1 
HETATM 49422 O  O24 . A1H71 LA 16 .   ? 56.913  -159.404 16.075  1.00 104.52 ? 301 A1H71 Y O24 1 
HETATM 49423 N  N10 . A1H71 LA 16 .   ? 57.637  -157.463 15.194  1.00 103.76 ? 301 A1H71 Y N10 1 
HETATM 49424 C  C9  . A1H71 LA 16 .   ? 56.698  -157.382 14.088  1.00 99.63  ? 301 A1H71 Y C9  1 
HETATM 49425 C  C25 . A1H71 LA 16 .   ? 57.345  -157.240 12.885  1.00 98.13  ? 301 A1H71 Y C25 1 
HETATM 49426 O  O26 . A1H71 LA 16 .   ? 58.551  -157.080 12.769  1.00 98.59  ? 301 A1H71 Y O26 1 
HETATM 49427 N  N27 . A1H71 LA 16 .   ? 56.579  -157.206 11.757  1.00 96.62  ? 301 A1H71 Y N27 1 
HETATM 49428 N  N4  . A1H71 LA 16 .   ? 54.609  -154.910 12.228  1.00 92.43  ? 301 A1H71 Y N4  1 
HETATM 49429 C  C3  . A1H71 LA 16 .   ? 54.770  -155.188 10.894  1.00 92.88  ? 301 A1H71 Y C3  1 
HETATM 49430 O  O37 . A1H71 LA 16 .   ? 53.826  -155.594 10.235  1.00 94.81  ? 301 A1H71 Y O37 1 
HETATM 49431 C  C2  . A1H71 LA 16 .   ? 55.994  -154.942 10.330  1.00 97.77  ? 301 A1H71 Y C2  1 
HETATM 49432 C  C1  . A1H71 LA 16 .   ? 56.489  -156.116 9.570   1.00 97.76  ? 301 A1H71 Y C1  1 
HETATM 49433 O  OG1 . A1H71 LA 16 .   ? 57.411  -155.636 8.642   1.00 99.66  ? 301 A1H71 Y OG1 1 
HETATM 49434 C  CB  . A1H71 LA 16 .   ? 56.658  -155.090 7.598   1.00 100.87 ? 301 A1H71 Y CB  1 
HETATM 49435 C  CG2 . A1H71 LA 16 .   ? 56.417  -156.194 6.609   1.00 101.68 ? 301 A1H71 Y CG2 1 
HETATM 49436 C  CA  . A1H71 LA 16 .   ? 57.448  -154.010 6.908   1.00 101.39 ? 301 A1H71 Y CA  1 
HETATM 49437 C  C   . A1H71 LA 16 .   ? 56.854  -153.812 5.563   1.00 99.51  ? 301 A1H71 Y C   1 
HETATM 49438 O  O   . A1H71 LA 16 .   ? 55.708  -153.419 5.441   1.00 94.74  ? 301 A1H71 Y O   1 
HETATM 49439 N  N   . A1H71 LA 16 .   ? 57.252  -152.749 7.600   1.00 103.27 ? 301 A1H71 Y N   1 
HETATM 49440 C  C29 . A1H71 LA 16 .   ? 57.345  -158.382 9.800   1.00 99.75  ? 301 A1H71 Y C29 1 
HETATM 49441 C  C30 . A1H71 LA 16 .   ? 58.558  -158.963 10.074  1.00 79.45  ? 301 A1H71 Y C30 1 
HETATM 49442 C  C35 . A1H71 LA 16 .   ? 58.728  -160.313 9.855   1.00 79.11  ? 301 A1H71 Y C35 1 
HETATM 49443 C  C34 . A1H71 LA 16 .   ? 59.935  -160.919 10.123  1.00 79.69  ? 301 A1H71 Y C34 1 
HETATM 49444 C  C33 . A1H71 LA 16 .   ? 60.986  -160.177 10.609  1.00 80.63  ? 301 A1H71 Y C33 1 
HETATM 49445 C  C32 . A1H71 LA 16 .   ? 60.814  -158.829 10.825  1.00 81.06  ? 301 A1H71 Y C32 1 
HETATM 49446 C  C31 . A1H71 LA 16 .   ? 59.604  -158.217 10.559  1.00 80.29  ? 301 A1H71 Y C31 1 
HETATM 49447 MG MG  . MG    MA 15 .   ? 61.261  -144.864 6.639   1.00 98.34  ? 302 MG    Y MG  1 
HETATM 49448 MG MG  . MG    NA 15 .   ? 72.599  -147.566 37.969  1.00 123.39 ? 301 MG    Z MG  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . MET   A  1   ? 2.7165 1.3036 2.4942 0.4184  -0.2676 -0.5982 1   MET   A N   
2     C  CA  . MET   A  1   ? 2.6908 1.1858 2.5064 0.4308  -0.2448 -0.5805 1   MET   A CA  
3     C  C   . MET   A  1   ? 2.5564 0.9841 2.6437 0.2749  -0.1129 -0.4418 1   MET   A C   
4     O  O   . MET   A  1   ? 2.3803 0.3109 2.7464 0.2642  0.0048  -0.3628 1   MET   A O   
5     C  CB  . MET   A  1   ? 2.6778 1.2966 2.4442 0.6037  -0.4899 -0.6044 1   MET   A CB  
6     C  CG  . MET   A  1   ? 2.8588 1.2782 2.4283 0.6503  -0.6181 -0.6483 1   MET   A CG  
7     S  SD  . MET   A  1   ? 2.9803 1.2504 2.2972 0.6332  -0.9980 -0.5012 1   MET   A SD  
8     C  CE  . MET   A  1   ? 2.9441 1.3450 2.4459 0.5604  -0.9751 -0.4812 1   MET   A CE  
9     N  N   . THR   A  2   ? 2.3043 1.1855 2.6024 0.1167  -0.0183 -0.3459 2   THR   A N   
10    C  CA  . THR   A  2   ? 2.2456 1.1834 2.4171 -0.1958 -0.0428 -0.3444 2   THR   A CA  
11    C  C   . THR   A  2   ? 2.2389 1.0821 2.4798 -0.0676 0.0187  -0.3052 2   THR   A C   
12    O  O   . THR   A  2   ? 2.3763 0.9344 2.4887 -0.1278 0.0759  -0.3902 2   THR   A O   
13    C  CB  . THR   A  2   ? 2.1491 1.1260 2.3818 -0.2808 -0.0439 -0.2862 2   THR   A CB  
14    O  OG1 . THR   A  2   ? 2.3468 0.6795 2.3504 -0.3454 -0.3536 -0.4467 2   THR   A OG1 
15    C  CG2 . THR   A  2   ? 2.1625 0.9435 2.2036 -0.2994 -0.1371 -0.3696 2   THR   A CG2 
16    N  N   . ASP   A  3   ? 2.2092 1.2472 2.2646 -0.2076 0.0016  -0.2141 3   ASP   A N   
17    C  CA  . ASP   A  3   ? 2.0367 1.2804 1.9469 -0.1605 -0.0431 -0.2445 3   ASP   A CA  
18    C  C   . ASP   A  3   ? 2.0342 1.2615 1.9377 -0.1676 -0.0269 -0.2239 3   ASP   A C   
19    O  O   . ASP   A  3   ? 2.0308 1.3651 1.9013 -0.1111 0.0183  -0.1940 3   ASP   A O   
20    C  CB  . ASP   A  3   ? 2.0447 1.3707 1.8126 -0.1500 -0.0391 -0.3010 3   ASP   A CB  
21    C  CG  . ASP   A  3   ? 1.9963 1.3535 1.7439 -0.1058 -0.0139 -0.3162 3   ASP   A CG  
22    O  OD1 . ASP   A  3   ? 2.0469 1.4361 1.7308 -0.0485 -0.0326 -0.2319 3   ASP   A OD1 
23    O  OD2 . ASP   A  3   ? 1.9668 1.4970 1.6811 0.0056  0.1803  -0.4562 3   ASP   A OD2 
24    N  N   . ARG   A  4   ? 1.9569 1.1868 1.8450 -0.2405 -0.1147 -0.2373 4   ARG   A N   
25    C  CA  . ARG   A  4   ? 1.8460 1.1851 1.7919 -0.3368 -0.1171 -0.2397 4   ARG   A CA  
26    C  C   . ARG   A  4   ? 1.8417 0.9123 1.6020 -0.2645 -0.2152 -0.2535 4   ARG   A C   
27    O  O   . ARG   A  4   ? 1.8024 0.6767 1.6136 -0.3490 -0.2772 -0.3091 4   ARG   A O   
28    C  CB  . ARG   A  4   ? 1.7943 1.3707 1.8852 -0.3107 -0.1218 -0.2637 4   ARG   A CB  
29    C  CG  . ARG   A  4   ? 1.7219 1.7036 2.0115 -0.2838 -0.0152 -0.2012 4   ARG   A CG  
30    C  CD  . ARG   A  4   ? 1.7378 1.8473 2.1236 -0.2974 -0.0199 -0.2952 4   ARG   A CD  
31    N  NE  . ARG   A  4   ? 1.7557 2.1199 2.1801 -0.2379 0.0299  -0.1829 4   ARG   A NE  
32    C  CZ  . ARG   A  4   ? 1.6038 2.3088 2.4203 -0.2643 0.0691  -0.1780 4   ARG   A CZ  
33    N  NH1 . ARG   A  4   ? 1.5724 2.4039 2.5010 -0.2904 0.0750  -0.1882 4   ARG   A NH1 
34    N  NH2 . ARG   A  4   ? 1.6169 2.3430 2.4362 -0.3508 0.1162  -0.1503 4   ARG   A NH2 
35    N  N   . TYR   A  5   ? 1.7566 0.8154 1.4880 -0.2220 -0.1397 -0.1527 5   TYR   A N   
36    C  CA  . TYR   A  5   ? 1.7290 0.7193 1.3685 -0.1294 -0.1218 -0.1417 5   TYR   A CA  
37    C  C   . TYR   A  5   ? 1.6352 0.6282 1.3087 -0.1127 -0.1759 -0.0954 5   TYR   A C   
38    O  O   . TYR   A  5   ? 1.6122 0.5876 1.2170 -0.1238 -0.1866 -0.2263 5   TYR   A O   
39    C  CB  . TYR   A  5   ? 1.7428 0.6839 1.3903 -0.1626 -0.1133 -0.1462 5   TYR   A CB  
40    C  CG  . TYR   A  5   ? 1.8209 0.7172 1.4056 -0.1656 -0.0878 -0.1774 5   TYR   A CG  
41    C  CD1 . TYR   A  5   ? 1.8478 0.7018 1.4252 -0.1713 -0.0488 -0.2127 5   TYR   A CD1 
42    C  CD2 . TYR   A  5   ? 1.8628 0.7033 1.4023 -0.1230 -0.0815 -0.1885 5   TYR   A CD2 
43    C  CE1 . TYR   A  5   ? 1.8798 0.7299 1.4802 -0.1253 0.0006  -0.1998 5   TYR   A CE1 
44    C  CE2 . TYR   A  5   ? 1.8954 0.7161 1.4459 -0.1221 -0.0305 -0.1855 5   TYR   A CE2 
45    C  CZ  . TYR   A  5   ? 1.9135 0.7448 1.5100 -0.1390 0.0068  -0.1568 5   TYR   A CZ  
46    O  OH  . TYR   A  5   ? 1.9434 0.7610 1.5388 -0.1846 0.0838  -0.1675 5   TYR   A OH  
47    N  N   . SER   A  6   ? 1.5962 0.6206 1.2815 -0.1021 -0.1626 -0.0448 6   SER   A N   
48    C  CA  . SER   A  6   ? 1.5651 0.7498 1.2196 -0.0841 -0.1545 -0.0148 6   SER   A CA  
49    C  C   . SER   A  6   ? 1.6091 0.7252 1.1785 -0.0738 -0.1574 -0.0317 6   SER   A C   
50    O  O   . SER   A  6   ? 1.6183 0.7869 1.1420 -0.1026 -0.2129 -0.0741 6   SER   A O   
51    C  CB  . SER   A  6   ? 1.5200 0.8869 1.2133 -0.0977 -0.1714 -0.0074 6   SER   A CB  
52    O  OG  . SER   A  6   ? 1.5172 1.0092 1.2651 -0.0810 -0.1667 0.0830  6   SER   A OG  
53    N  N   . PHE   A  7   ? 1.6632 0.7118 1.2085 -0.0710 -0.1388 -0.0019 7   PHE   A N   
54    C  CA  . PHE   A  7   ? 1.6813 0.6333 1.2285 -0.0273 -0.1669 0.0111  7   PHE   A CA  
55    C  C   . PHE   A  7   ? 1.6933 0.5744 1.2393 -0.0493 -0.1515 0.0195  7   PHE   A C   
56    O  O   . PHE   A  7   ? 1.7398 0.7959 1.2353 -0.0879 -0.1589 -0.0513 7   PHE   A O   
57    C  CB  . PHE   A  7   ? 1.7412 0.5398 1.1898 -0.0498 -0.1356 0.0626  7   PHE   A CB  
58    C  CG  . PHE   A  7   ? 1.7777 0.4781 1.1854 -0.0286 -0.1190 0.0893  7   PHE   A CG  
59    C  CD1 . PHE   A  7   ? 1.7851 0.5271 1.1717 -0.0493 -0.1094 0.0771  7   PHE   A CD1 
60    C  CD2 . PHE   A  7   ? 1.7813 0.4436 1.1889 -0.0266 -0.1170 0.0728  7   PHE   A CD2 
61    C  CE1 . PHE   A  7   ? 1.8344 0.5666 1.1807 -0.0515 -0.0916 0.0732  7   PHE   A CE1 
62    C  CE2 . PHE   A  7   ? 1.8102 0.4796 1.2015 -0.0129 -0.1007 0.0729  7   PHE   A CE2 
63    C  CZ  . PHE   A  7   ? 1.8339 0.5389 1.2091 -0.0581 -0.1013 0.0737  7   PHE   A CZ  
64    N  N   . SER   A  8   ? 1.6720 0.4382 1.2526 -0.0321 -0.1634 0.0082  8   SER   A N   
65    C  CA  . SER   A  8   ? 1.7018 0.4201 1.3111 -0.0698 -0.1478 -0.0342 8   SER   A CA  
66    C  C   . SER   A  8   ? 1.6995 0.4828 1.3110 -0.0862 -0.1764 -0.0777 8   SER   A C   
67    O  O   . SER   A  8   ? 1.7196 0.5198 1.4043 -0.0542 -0.1903 -0.1288 8   SER   A O   
68    C  CB  . SER   A  8   ? 1.7015 0.4349 1.3380 -0.0863 -0.1353 -0.0356 8   SER   A CB  
69    O  OG  . SER   A  8   ? 1.7397 0.3621 1.4633 -0.0996 -0.1193 -0.0191 8   SER   A OG  
70    N  N   . LEU   A  9   ? 1.6711 0.4900 1.3211 -0.0938 -0.1793 -0.0627 9   LEU   A N   
71    C  CA  . LEU   A  9   ? 1.6199 0.5039 1.2535 -0.0663 -0.2285 -0.0430 9   LEU   A CA  
72    C  C   . LEU   A  9   ? 1.6172 0.4497 1.2227 -0.0406 -0.2407 -0.0172 9   LEU   A C   
73    O  O   . LEU   A  9   ? 1.6262 0.3640 1.1723 -0.0208 -0.2422 0.0778  9   LEU   A O   
74    C  CB  . LEU   A  9   ? 1.6235 0.4720 1.2543 -0.0736 -0.2286 -0.0456 9   LEU   A CB  
75    C  CG  . LEU   A  9   ? 1.6372 0.3956 1.2918 -0.0566 -0.2215 -0.0541 9   LEU   A CG  
76    C  CD1 . LEU   A  9   ? 1.6506 0.3746 1.2955 -0.0499 -0.2167 -0.0559 9   LEU   A CD1 
77    C  CD2 . LEU   A  9   ? 1.6602 0.4275 1.2953 -0.0269 -0.2323 -0.0485 9   LEU   A CD2 
78    N  N   . THR   A  10  ? 1.6111 0.4832 1.2111 -0.0559 -0.2430 -0.0360 10  THR   A N   
79    C  CA  . THR   A  10  ? 1.6274 0.4558 1.1733 -0.0609 -0.2665 -0.0266 10  THR   A CA  
80    C  C   . THR   A  10  ? 1.6346 0.5079 1.1480 -0.0649 -0.2725 -0.1007 10  THR   A C   
81    O  O   . THR   A  10  ? 1.6316 0.3879 1.0723 -0.0564 -0.2892 0.0071  10  THR   A O   
82    C  CB  . THR   A  10  ? 1.6213 0.4420 1.1794 -0.0696 -0.2786 -0.0342 10  THR   A CB  
83    O  OG1 . THR   A  10  ? 1.5808 0.5679 1.1473 -0.0557 -0.3227 -0.0932 10  THR   A OG1 
84    C  CG2 . THR   A  10  ? 1.6186 0.4963 1.1732 -0.0723 -0.2704 -0.0050 10  THR   A CG2 
85    N  N   . THR   A  11  ? 1.6411 0.5215 1.1743 -0.0141 -0.2535 -0.1076 11  THR   A N   
86    C  CA  . THR   A  11  ? 1.6508 0.5477 1.1486 -0.0032 -0.2338 -0.1364 11  THR   A CA  
87    C  C   . THR   A  11  ? 1.6819 0.5762 1.2090 0.0148  -0.1732 -0.0859 11  THR   A C   
88    O  O   . THR   A  11  ? 1.7127 0.7258 1.1470 0.0290  -0.1542 -0.1212 11  THR   A O   
89    C  CB  . THR   A  11  ? 1.6548 0.5596 1.1721 0.0027  -0.2359 -0.1441 11  THR   A CB  
90    O  OG1 . THR   A  11  ? 1.6215 0.5804 1.1571 -0.0388 -0.2542 -0.1696 11  THR   A OG1 
91    C  CG2 . THR   A  11  ? 1.6480 0.5929 1.1746 -0.0060 -0.2067 -0.1582 11  THR   A CG2 
92    N  N   . PHE   A  12  ? 1.6874 0.6044 1.1859 0.0299  -0.2250 -0.1300 12  PHE   A N   
93    C  CA  . PHE   A  12  ? 1.7169 0.6488 1.2438 0.0166  -0.2488 -0.0691 12  PHE   A CA  
94    C  C   . PHE   A  12  ? 1.7398 0.6515 1.2633 0.0264  -0.2721 -0.0661 12  PHE   A C   
95    O  O   . PHE   A  12  ? 1.7509 0.7197 1.1993 -0.0479 -0.3152 -0.1093 12  PHE   A O   
96    C  CB  . PHE   A  12  ? 1.6965 0.6367 1.2526 0.0468  -0.2458 -0.0679 12  PHE   A CB  
97    C  CG  . PHE   A  12  ? 1.6592 0.6322 1.2821 0.0357  -0.2516 -0.0602 12  PHE   A CG  
98    C  CD1 . PHE   A  12  ? 1.6545 0.6051 1.2992 0.0509  -0.2609 -0.0536 12  PHE   A CD1 
99    C  CD2 . PHE   A  12  ? 1.6170 0.6188 1.2440 0.0623  -0.2483 -0.0663 12  PHE   A CD2 
100   C  CE1 . PHE   A  12  ? 1.6357 0.5936 1.2774 0.0483  -0.2787 -0.0374 12  PHE   A CE1 
101   C  CE2 . PHE   A  12  ? 1.6170 0.5909 1.2089 0.0508  -0.2693 -0.0663 12  PHE   A CE2 
102   C  CZ  . PHE   A  12  ? 1.6164 0.5936 1.2334 0.0610  -0.2707 -0.0551 12  PHE   A CZ  
103   N  N   . SER   A  13  ? 1.8211 0.6135 1.3617 0.0038  -0.2729 -0.0499 13  SER   A N   
104   C  CA  . SER   A  13  ? 1.8566 0.6032 1.3533 0.0099  -0.2792 0.0453  13  SER   A CA  
105   C  C   . SER   A  13  ? 1.8520 0.5369 1.3868 0.0389  -0.2685 0.0771  13  SER   A C   
106   O  O   . SER   A  13  ? 1.8890 0.5241 1.3549 0.0322  -0.2162 0.1474  13  SER   A O   
107   C  CB  . SER   A  13  ? 1.8936 0.6191 1.4246 -0.0045 -0.3113 0.0146  13  SER   A CB  
108   O  OG  . SER   A  13  ? 1.8895 0.6670 1.4839 -0.0429 -0.3215 0.0206  13  SER   A OG  
109   N  N   . PRO   A  14  ? 1.8532 0.4704 1.3574 -0.0038 -0.2486 0.0885  14  PRO   A N   
110   C  CA  . PRO   A  14  ? 1.8752 0.3789 1.4118 0.0132  -0.2584 0.1272  14  PRO   A CA  
111   C  C   . PRO   A  14  ? 1.8914 0.3606 1.3970 -0.0249 -0.2749 0.1699  14  PRO   A C   
112   O  O   . PRO   A  14  ? 1.9222 0.4217 1.4050 -0.0046 -0.2383 0.2553  14  PRO   A O   
113   C  CB  . PRO   A  14  ? 1.8917 0.3613 1.4299 0.0018  -0.2492 0.1111  14  PRO   A CB  
114   C  CG  . PRO   A  14  ? 1.8734 0.3165 1.4152 0.0179  -0.2539 0.0925  14  PRO   A CG  
115   C  CD  . PRO   A  14  ? 1.8490 0.3501 1.3733 0.0143  -0.2784 0.0723  14  PRO   A CD  
116   N  N   . SER   A  15  ? 1.9372 0.3290 1.3924 -0.0428 -0.2834 0.1562  15  SER   A N   
117   C  CA  . SER   A  15  ? 1.9331 0.4129 1.4242 -0.0420 -0.2967 0.1809  15  SER   A CA  
118   C  C   . SER   A  15  ? 1.8703 0.4773 1.3921 -0.0346 -0.3218 0.1188  15  SER   A C   
119   O  O   . SER   A  15  ? 1.8363 0.3762 1.3952 -0.1005 -0.3731 0.1218  15  SER   A O   
120   C  CB  . SER   A  15  ? 1.9565 0.4401 1.3891 -0.0386 -0.3160 0.2246  15  SER   A CB  
121   O  OG  . SER   A  15  ? 1.9638 0.3719 1.4562 0.0101  -0.3652 0.3021  15  SER   A OG  
122   N  N   . GLY   A  16  ? 1.8496 0.5120 1.3827 -0.0612 -0.3106 0.1141  16  GLY   A N   
123   C  CA  . GLY   A  16  ? 1.8602 0.5764 1.4006 -0.0266 -0.2742 0.0658  16  GLY   A CA  
124   C  C   . GLY   A  16  ? 1.8665 0.6425 1.3604 -0.0371 -0.2741 0.0447  16  GLY   A C   
125   O  O   . GLY   A  16  ? 1.8823 0.6815 1.4216 -0.0156 -0.2028 -0.0237 16  GLY   A O   
126   N  N   . LYS   A  17  ? 1.8583 0.6668 1.4010 -0.0274 -0.2812 0.0024  17  LYS   A N   
127   C  CA  . LYS   A  17  ? 1.8170 0.7303 1.4335 0.0050  -0.2997 0.0127  17  LYS   A CA  
128   C  C   . LYS   A  17  ? 1.7626 0.6692 1.3526 0.0239  -0.3201 -0.0599 17  LYS   A C   
129   O  O   . LYS   A  17  ? 1.7747 0.5409 1.3366 0.0340  -0.3656 -0.1319 17  LYS   A O   
130   C  CB  . LYS   A  17  ? 1.8438 0.8697 1.4401 0.0054  -0.3154 -0.0447 17  LYS   A CB  
131   C  CG  . LYS   A  17  ? 1.9227 0.9683 1.5442 -0.0183 -0.3144 0.0669  17  LYS   A CG  
132   C  CD  . LYS   A  17  ? 1.9078 1.2256 1.5614 -0.0121 -0.3147 0.0921  17  LYS   A CD  
133   C  CE  . LYS   A  17  ? 1.8994 1.2819 1.5663 -0.0140 -0.3667 0.1213  17  LYS   A CE  
134   N  NZ  . LYS   A  17  ? 1.8864 1.3560 1.5930 0.0290  -0.3843 0.1360  17  LYS   A NZ  
135   N  N   . LEU   A  18  ? 1.7789 0.6083 1.3266 -0.0094 -0.2680 -0.0541 18  LEU   A N   
136   C  CA  . LEU   A  18  ? 1.7654 0.6487 1.2935 -0.0071 -0.2484 -0.0578 18  LEU   A CA  
137   C  C   . LEU   A  18  ? 1.7359 0.5619 1.3183 0.0342  -0.2018 -0.1056 18  LEU   A C   
138   O  O   . LEU   A  18  ? 1.7516 0.6114 1.2976 0.0098  -0.2419 -0.1598 18  LEU   A O   
139   C  CB  . LEU   A  18  ? 1.7683 0.6486 1.2642 -0.0175 -0.2421 -0.0515 18  LEU   A CB  
140   C  CG  . LEU   A  18  ? 1.7616 0.7202 1.2257 -0.0454 -0.2562 -0.0063 18  LEU   A CG  
141   C  CD1 . LEU   A  18  ? 1.7418 0.7261 1.1660 -0.0606 -0.2378 -0.0182 18  LEU   A CD1 
142   C  CD2 . LEU   A  18  ? 1.7530 0.7134 1.2016 -0.0280 -0.2762 0.0005  18  LEU   A CD2 
143   N  N   . GLY   A  19  ? 1.7123 0.5202 1.3390 0.0163  -0.1894 -0.0806 19  GLY   A N   
144   C  CA  . GLY   A  19  ? 1.6846 0.4384 1.3405 0.0213  -0.1837 -0.0611 19  GLY   A CA  
145   C  C   . GLY   A  19  ? 1.6601 0.4167 1.3541 0.0659  -0.1696 -0.0780 19  GLY   A C   
146   O  O   . GLY   A  19  ? 1.6243 0.2912 1.3837 0.0542  -0.1401 -0.0655 19  GLY   A O   
147   N  N   . GLN   A  20  ? 1.6379 0.3829 1.3421 0.1036  -0.1769 -0.0881 20  GLN   A N   
148   C  CA  . GLN   A  20  ? 1.6382 0.3629 1.3345 0.0971  -0.1964 -0.1063 20  GLN   A CA  
149   C  C   . GLN   A  20  ? 1.6532 0.3130 1.3268 0.1135  -0.1615 -0.0964 20  GLN   A C   
150   O  O   . GLN   A  20  ? 1.6745 0.2584 1.4059 0.2009  -0.2085 -0.0419 20  GLN   A O   
151   C  CB  . GLN   A  20  ? 1.5967 0.3910 1.3313 0.0977  -0.2100 -0.1487 20  GLN   A CB  
152   C  CG  . GLN   A  20  ? 1.5930 0.4102 1.3508 0.1133  -0.2240 -0.1519 20  GLN   A CG  
153   C  CD  . GLN   A  20  ? 1.5828 0.4066 1.3497 0.1065  -0.2420 -0.1546 20  GLN   A CD  
154   O  OE1 . GLN   A  20  ? 1.6159 0.3449 1.3612 0.0602  -0.2056 -0.1024 20  GLN   A OE1 
155   N  NE2 . GLN   A  20  ? 1.5549 0.4556 1.3609 0.1280  -0.2542 -0.1923 20  GLN   A NE2 
156   N  N   . ILE   A  21  ? 1.6449 0.2722 1.2990 0.1022  -0.1779 -0.0938 21  ILE   A N   
157   C  CA  . ILE   A  21  ? 1.6398 0.3446 1.2995 0.0995  -0.1657 -0.0785 21  ILE   A CA  
158   C  C   . ILE   A  21  ? 1.6554 0.3555 1.3572 0.0827  -0.1538 -0.0771 21  ILE   A C   
159   O  O   . ILE   A  21  ? 1.6442 0.2401 1.3924 0.1378  -0.1255 -0.0227 21  ILE   A O   
160   C  CB  . ILE   A  21  ? 1.6496 0.4247 1.2832 0.0548  -0.1830 -0.0875 21  ILE   A CB  
161   C  CG1 . ILE   A  21  ? 1.6454 0.4503 1.2810 0.0338  -0.1590 -0.0973 21  ILE   A CG1 
162   C  CG2 . ILE   A  21  ? 1.6460 0.4337 1.2674 0.0174  -0.1896 -0.0934 21  ILE   A CG2 
163   C  CD1 . ILE   A  21  ? 1.6549 0.4401 1.2845 0.0394  -0.1581 -0.1098 21  ILE   A CD1 
164   N  N   . ASP   A  22  ? 1.7356 0.4013 1.3721 0.0956  -0.1544 -0.0232 22  ASP   A N   
165   C  CA  . ASP   A  22  ? 1.8154 0.4220 1.4082 0.0739  -0.1554 -0.0561 22  ASP   A CA  
166   C  C   . ASP   A  22  ? 1.7716 0.4201 1.4017 0.0576  -0.1904 -0.0618 22  ASP   A C   
167   O  O   . ASP   A  22  ? 1.7629 0.4722 1.3690 0.0790  -0.1854 -0.0780 22  ASP   A O   
168   C  CB  . ASP   A  22  ? 1.8941 0.4500 1.4716 0.1027  -0.1412 -0.0187 22  ASP   A CB  
169   C  CG  . ASP   A  22  ? 1.9406 0.4796 1.5253 0.1051  -0.0352 -0.0622 22  ASP   A CG  
170   O  OD1 . ASP   A  22  ? 2.0897 0.3263 1.5492 0.1262  -0.0225 -0.0426 22  ASP   A OD1 
171   O  OD2 . ASP   A  22  ? 1.9798 0.5680 1.6378 0.0503  -0.0463 0.0721  22  ASP   A OD2 
172   N  N   . TYR   A  23  ? 1.7461 0.3993 1.3973 0.0217  -0.2249 -0.0733 23  TYR   A N   
173   C  CA  . TYR   A  23  ? 1.7198 0.4256 1.3899 -0.0030 -0.2484 -0.0759 23  TYR   A CA  
174   C  C   . TYR   A  23  ? 1.7282 0.4064 1.3494 -0.0140 -0.2371 -0.0874 23  TYR   A C   
175   O  O   . TYR   A  23  ? 1.7652 0.4147 1.2993 0.0089  -0.2028 -0.0271 23  TYR   A O   
176   C  CB  . TYR   A  23  ? 1.7048 0.3989 1.4196 -0.0245 -0.2706 -0.0814 23  TYR   A CB  
177   C  CG  . TYR   A  23  ? 1.7110 0.4337 1.4805 0.0172  -0.2929 -0.1005 23  TYR   A CG  
178   C  CD1 . TYR   A  23  ? 1.7328 0.4662 1.4955 0.0451  -0.2797 -0.0467 23  TYR   A CD1 
179   C  CD2 . TYR   A  23  ? 1.7052 0.3709 1.4953 0.0289  -0.2815 -0.1069 23  TYR   A CD2 
180   C  CE1 . TYR   A  23  ? 1.7528 0.4883 1.5156 0.0695  -0.2815 -0.0378 23  TYR   A CE1 
181   C  CE2 . TYR   A  23  ? 1.6995 0.4291 1.5187 0.0850  -0.2688 -0.1085 23  TYR   A CE2 
182   C  CZ  . TYR   A  23  ? 1.7468 0.5172 1.5172 0.0682  -0.2592 -0.0400 23  TYR   A CZ  
183   O  OH  . TYR   A  23  ? 1.7441 0.7020 1.5263 0.1242  -0.2848 0.0000  23  TYR   A OH  
184   N  N   . ALA   A  24  ? 1.6921 0.3968 1.3130 -0.0335 -0.2674 -0.0799 24  ALA   A N   
185   C  CA  . ALA   A  24  ? 1.7044 0.4238 1.2660 -0.0325 -0.2710 -0.0673 24  ALA   A CA  
186   C  C   . ALA   A  24  ? 1.7077 0.3824 1.2385 -0.0378 -0.2390 -0.0612 24  ALA   A C   
187   O  O   . ALA   A  24  ? 1.6839 0.4397 1.2343 0.0287  -0.2294 -0.1114 24  ALA   A O   
188   C  CB  . ALA   A  24  ? 1.7008 0.4704 1.2632 -0.0533 -0.2687 -0.0905 24  ALA   A CB  
189   N  N   . LEU   A  25  ? 1.7224 0.3335 1.2430 -0.0526 -0.2603 -0.0394 25  LEU   A N   
190   C  CA  . LEU   A  25  ? 1.7374 0.3434 1.2588 -0.0803 -0.2550 0.0024  25  LEU   A CA  
191   C  C   . LEU   A  25  ? 1.7555 0.3613 1.2398 -0.0665 -0.2668 0.0050  25  LEU   A C   
192   O  O   . LEU   A  25  ? 1.7760 0.2935 1.1985 -0.0489 -0.2733 0.0636  25  LEU   A O   
193   C  CB  . LEU   A  25  ? 1.7652 0.3895 1.2693 -0.1137 -0.2294 -0.0059 25  LEU   A CB  
194   C  CG  . LEU   A  25  ? 1.7684 0.4055 1.3176 -0.1164 -0.1863 -0.0250 25  LEU   A CG  
195   C  CD1 . LEU   A  25  ? 1.8059 0.4876 1.3301 -0.1151 -0.1710 0.0034  25  LEU   A CD1 
196   C  CD2 . LEU   A  25  ? 1.7535 0.4037 1.2975 -0.1366 -0.1995 0.0151  25  LEU   A CD2 
197   N  N   . THR   A  26  ? 1.7362 0.4584 1.2745 -0.0403 -0.2755 -0.0209 26  THR   A N   
198   C  CA  . THR   A  26  ? 1.7690 0.4811 1.3142 -0.0391 -0.2937 -0.0515 26  THR   A CA  
199   C  C   . THR   A  26  ? 1.7766 0.4335 1.3240 -0.0575 -0.2863 -0.0500 26  THR   A C   
200   O  O   . THR   A  26  ? 1.8517 0.3177 1.3373 -0.0520 -0.2596 -0.1250 26  THR   A O   
201   C  CB  . THR   A  26  ? 1.8089 0.4507 1.2934 -0.0233 -0.2970 -0.0392 26  THR   A CB  
202   O  OG1 . THR   A  26  ? 1.8841 0.3642 1.3561 -0.0255 -0.2721 -0.0048 26  THR   A OG1 
203   C  CG2 . THR   A  26  ? 1.8078 0.4107 1.3291 0.0017  -0.3123 -0.0442 26  THR   A CG2 
204   N  N   . ALA   A  27  ? 1.7431 0.5065 1.3565 -0.1073 -0.2816 -0.0612 27  ALA   A N   
205   C  CA  . ALA   A  27  ? 1.7388 0.5984 1.2943 -0.1117 -0.2706 -0.0834 27  ALA   A CA  
206   C  C   . ALA   A  27  ? 1.7418 0.5562 1.3460 -0.1006 -0.2418 -0.0916 27  ALA   A C   
207   O  O   . ALA   A  27  ? 1.7426 0.4777 1.3049 -0.0919 -0.1959 -0.1118 27  ALA   A O   
208   C  CB  . ALA   A  27  ? 1.7216 0.6419 1.2680 -0.1244 -0.2840 -0.0971 27  ALA   A CB  
209   N  N   . VAL   A  28  ? 1.7279 0.5382 1.3814 -0.0860 -0.2505 -0.1337 28  VAL   A N   
210   C  CA  . VAL   A  28  ? 1.7182 0.5857 1.4204 -0.0944 -0.2807 -0.1424 28  VAL   A CA  
211   C  C   . VAL   A  28  ? 1.7241 0.6350 1.4664 -0.1024 -0.3105 -0.1827 28  VAL   A C   
212   O  O   . VAL   A  28  ? 1.7557 0.5014 1.4332 -0.1239 -0.3229 -0.1867 28  VAL   A O   
213   C  CB  . VAL   A  28  ? 1.6836 0.6265 1.4133 -0.0956 -0.3000 -0.1507 28  VAL   A CB  
214   C  CG1 . VAL   A  28  ? 1.6779 0.5891 1.4017 -0.0975 -0.3099 -0.1388 28  VAL   A CG1 
215   C  CG2 . VAL   A  28  ? 1.6910 0.6473 1.4211 -0.1036 -0.3013 -0.1633 28  VAL   A CG2 
216   N  N   . LYS   A  29  ? 1.7785 0.6797 1.4917 -0.0605 -0.3113 -0.1447 29  LYS   A N   
217   C  CA  . LYS   A  29  ? 1.8246 0.7131 1.4743 -0.0689 -0.3021 -0.2158 29  LYS   A CA  
218   C  C   . LYS   A  29  ? 1.8768 0.5289 1.4913 -0.0079 -0.3029 -0.2751 29  LYS   A C   
219   O  O   . LYS   A  29  ? 1.8598 0.3144 1.5190 0.0370  -0.2928 -0.3092 29  LYS   A O   
220   C  CB  . LYS   A  29  ? 1.8195 0.8344 1.4700 -0.0450 -0.3068 -0.1522 29  LYS   A CB  
221   C  CG  . LYS   A  29  ? 1.8151 1.0154 1.5237 -0.1217 -0.2811 -0.1130 29  LYS   A CG  
222   C  CD  . LYS   A  29  ? 1.8344 1.1135 1.5681 -0.1677 -0.2885 -0.0974 29  LYS   A CD  
223   C  CE  . LYS   A  29  ? 1.8654 1.1903 1.5889 -0.1272 -0.2943 -0.0539 29  LYS   A CE  
224   N  NZ  . LYS   A  29  ? 1.8751 1.2462 1.6126 -0.1353 -0.3245 -0.0601 29  LYS   A NZ  
225   N  N   . GLN   A  30  ? 1.8739 0.5210 1.4652 -0.0073 -0.3101 -0.2955 30  GLN   A N   
226   C  CA  . GLN   A  30  ? 1.8952 0.6508 1.4597 -0.0075 -0.3069 -0.2826 30  GLN   A CA  
227   C  C   . GLN   A  30  ? 1.8423 0.6577 1.4266 -0.0030 -0.2867 -0.2929 30  GLN   A C   
228   O  O   . GLN   A  30  ? 1.8573 0.7071 1.3822 0.1057  -0.2552 -0.3144 30  GLN   A O   
229   C  CB  . GLN   A  30  ? 1.8987 0.7231 1.4584 -0.0367 -0.3084 -0.2978 30  GLN   A CB  
230   C  CG  . GLN   A  30  ? 1.9329 0.8510 1.4964 0.0213  -0.3369 -0.3026 30  GLN   A CG  
231   C  CD  . GLN   A  30  ? 2.0549 0.9037 1.6059 -0.0515 -0.2888 -0.3455 30  GLN   A CD  
232   O  OE1 . GLN   A  30  ? 2.1962 1.0568 1.5876 -0.0735 -0.2762 -0.3251 30  GLN   A OE1 
233   N  NE2 . GLN   A  30  ? 2.1062 1.0742 1.5681 0.0070  -0.3299 -0.3852 30  GLN   A NE2 
234   N  N   . GLY   A  31  ? 1.8022 0.6345 1.4308 -0.0316 -0.2679 -0.2687 31  GLY   A N   
235   C  CA  . GLY   A  31  ? 1.7679 0.6226 1.4203 -0.0613 -0.2676 -0.2696 31  GLY   A CA  
236   C  C   . GLY   A  31  ? 1.7898 0.5771 1.3453 -0.1119 -0.2910 -0.2822 31  GLY   A C   
237   O  O   . GLY   A  31  ? 1.7356 0.6127 1.4627 -0.2416 -0.3026 -0.3580 31  GLY   A O   
238   N  N   . VAL   A  32  ? 1.7333 0.6462 1.2579 -0.1033 -0.3071 -0.3206 32  VAL   A N   
239   C  CA  . VAL   A  32  ? 1.7220 0.7111 1.2495 -0.0797 -0.2989 -0.2441 32  VAL   A CA  
240   C  C   . VAL   A  32  ? 1.7089 0.6835 1.2143 -0.0851 -0.3015 -0.1984 32  VAL   A C   
241   O  O   . VAL   A  32  ? 1.6684 0.7219 1.1707 -0.0633 -0.2834 -0.2123 32  VAL   A O   
242   C  CB  . VAL   A  32  ? 1.7130 0.7643 1.2903 -0.0433 -0.2909 -0.2027 32  VAL   A CB  
243   C  CG1 . VAL   A  32  ? 1.7152 0.7255 1.3252 -0.0245 -0.2822 -0.1840 32  VAL   A CG1 
244   C  CG2 . VAL   A  32  ? 1.7417 0.8983 1.2875 -0.0099 -0.2536 -0.1911 32  VAL   A CG2 
245   N  N   . THR   A  33  ? 1.7257 0.6337 1.2258 -0.0833 -0.3162 -0.1638 33  THR   A N   
246   C  CA  . THR   A  33  ? 1.7193 0.5955 1.2743 -0.0763 -0.3013 -0.1707 33  THR   A CA  
247   C  C   . THR   A  33  ? 1.7235 0.6146 1.2480 -0.0653 -0.3206 -0.0993 33  THR   A C   
248   O  O   . THR   A  33  ? 1.7864 0.6010 1.2281 -0.0923 -0.3197 -0.1052 33  THR   A O   
249   C  CB  . THR   A  33  ? 1.7167 0.6795 1.3529 -0.1100 -0.3054 -0.1897 33  THR   A CB  
250   O  OG1 . THR   A  33  ? 1.7443 0.7050 1.4565 -0.1116 -0.3117 -0.2449 33  THR   A OG1 
251   C  CG2 . THR   A  33  ? 1.6682 0.5917 1.3923 -0.1089 -0.2939 -0.2299 33  THR   A CG2 
252   N  N   . SER   A  34  ? 1.7092 0.5521 1.2688 -0.0550 -0.3025 -0.0945 34  SER   A N   
253   C  CA  . SER   A  34  ? 1.7051 0.5702 1.2697 -0.0334 -0.2717 -0.0771 34  SER   A CA  
254   C  C   . SER   A  34  ? 1.7011 0.4996 1.3122 -0.0351 -0.2383 -0.0741 34  SER   A C   
255   O  O   . SER   A  34  ? 1.6799 0.3413 1.3108 -0.0110 -0.1997 -0.1433 34  SER   A O   
256   C  CB  . SER   A  34  ? 1.6832 0.5955 1.2873 -0.0323 -0.2832 -0.0749 34  SER   A CB  
257   O  OG  . SER   A  34  ? 1.6790 0.6305 1.3363 -0.0386 -0.3093 -0.0936 34  SER   A OG  
258   N  N   . LEU   A  35  ? 1.6795 0.5585 1.3214 -0.0344 -0.2170 -0.0101 35  LEU   A N   
259   C  CA  . LEU   A  35  ? 1.6967 0.5311 1.3261 -0.0827 -0.2157 0.0151  35  LEU   A CA  
260   C  C   . LEU   A  35  ? 1.7398 0.4641 1.2782 -0.1183 -0.2186 0.0737  35  LEU   A C   
261   O  O   . LEU   A  35  ? 1.7446 0.2683 1.3462 -0.1104 -0.2629 0.0048  35  LEU   A O   
262   C  CB  . LEU   A  35  ? 1.7068 0.5491 1.3447 -0.0994 -0.2243 0.0082  35  LEU   A CB  
263   C  CG  . LEU   A  35  ? 1.6979 0.5733 1.3511 -0.1020 -0.2300 0.0044  35  LEU   A CG  
264   C  CD1 . LEU   A  35  ? 1.6696 0.5985 1.3792 -0.0990 -0.2354 0.0448  35  LEU   A CD1 
265   C  CD2 . LEU   A  35  ? 1.7221 0.5777 1.3725 -0.0962 -0.2278 -0.0089 35  LEU   A CD2 
266   N  N   . GLY   A  36  ? 1.7509 0.4231 1.2936 -0.1068 -0.2109 0.0235  36  GLY   A N   
267   C  CA  . GLY   A  36  ? 1.7180 0.4100 1.3459 -0.1078 -0.2186 0.0420  36  GLY   A CA  
268   C  C   . GLY   A  36  ? 1.6800 0.4779 1.4195 -0.1423 -0.2398 0.0393  36  GLY   A C   
269   O  O   . GLY   A  36  ? 1.6516 0.4250 1.4599 -0.2005 -0.2264 0.0294  36  GLY   A O   
270   N  N   . ILE   A  37  ? 1.6602 0.5426 1.3839 -0.1527 -0.2595 0.0696  37  ILE   A N   
271   C  CA  . ILE   A  37  ? 1.6843 0.6035 1.3550 -0.1616 -0.2453 0.0551  37  ILE   A CA  
272   C  C   . ILE   A  37  ? 1.6651 0.6187 1.3402 -0.1504 -0.2439 0.0555  37  ILE   A C   
273   O  O   . ILE   A  37  ? 1.6245 0.6586 1.2177 -0.1240 -0.2688 0.0336  37  ILE   A O   
274   C  CB  . ILE   A  37  ? 1.7385 0.6223 1.3734 -0.1646 -0.2730 0.0314  37  ILE   A CB  
275   C  CG1 . ILE   A  37  ? 1.7721 0.6728 1.3848 -0.1350 -0.2723 0.0155  37  ILE   A CG1 
276   C  CG2 . ILE   A  37  ? 1.7436 0.5998 1.3713 -0.1511 -0.2561 -0.0060 37  ILE   A CG2 
277   C  CD1 . ILE   A  37  ? 1.7837 0.8136 1.4230 -0.1498 -0.3139 0.0272  37  ILE   A CD1 
278   N  N   . LYS   A  38  ? 1.6900 0.6995 1.3619 -0.1526 -0.2222 0.0479  38  LYS   A N   
279   C  CA  . LYS   A  38  ? 1.6808 0.7026 1.4915 -0.1487 -0.2138 0.0194  38  LYS   A CA  
280   C  C   . LYS   A  38  ? 1.6729 0.7215 1.5292 -0.1539 -0.2313 0.0049  38  LYS   A C   
281   O  O   . LYS   A  38  ? 1.6318 0.7766 1.5953 -0.2020 -0.2055 0.0025  38  LYS   A O   
282   C  CB  . LYS   A  38  ? 1.7153 0.7564 1.5171 -0.1550 -0.2433 0.0118  38  LYS   A CB  
283   C  CG  . LYS   A  38  ? 1.7315 0.8414 1.4945 -0.1260 -0.2504 -0.0495 38  LYS   A CG  
284   C  CD  . LYS   A  38  ? 1.7420 0.9791 1.4439 -0.0836 -0.2401 -0.0196 38  LYS   A CD  
285   C  CE  . LYS   A  38  ? 1.7470 1.0083 1.4335 -0.0631 -0.2435 -0.0003 38  LYS   A CE  
286   N  NZ  . LYS   A  38  ? 1.7693 1.0597 1.4025 -0.0179 -0.2476 0.0360  38  LYS   A NZ  
287   N  N   . ALA   A  39  ? 1.6011 0.6946 1.5017 -0.1733 -0.2159 -0.0153 39  ALA   A N   
288   C  CA  . ALA   A  39  ? 1.5980 0.6365 1.5156 -0.1743 -0.1975 -0.0466 39  ALA   A CA  
289   C  C   . ALA   A  39  ? 1.5375 0.6134 1.5575 -0.1686 -0.1847 -0.0551 39  ALA   A C   
290   O  O   . ALA   A  39  ? 1.5219 0.5469 1.5208 -0.1317 -0.1510 -0.1085 39  ALA   A O   
291   C  CB  . ALA   A  39  ? 1.5948 0.6216 1.5284 -0.1744 -0.2027 -0.0367 39  ALA   A CB  
292   N  N   . THR   A  40  ? 1.5323 0.6147 1.6051 -0.1819 -0.1771 -0.0873 40  THR   A N   
293   C  CA  . THR   A  40  ? 1.5197 0.6473 1.6403 -0.1582 -0.1511 -0.0949 40  THR   A CA  
294   C  C   . THR   A  40  ? 1.5377 0.6147 1.7078 -0.1298 -0.1516 -0.1029 40  THR   A C   
295   O  O   . THR   A  40  ? 1.5950 0.4328 1.8273 -0.1027 -0.1402 -0.1009 40  THR   A O   
296   C  CB  . THR   A  40  ? 1.5109 0.7362 1.6287 -0.1627 -0.1700 -0.1258 40  THR   A CB  
297   O  OG1 . THR   A  40  ? 1.5185 0.7783 1.6405 -0.1350 -0.1884 -0.1363 40  THR   A OG1 
298   C  CG2 . THR   A  40  ? 1.5354 0.7175 1.6522 -0.1860 -0.1579 -0.1495 40  THR   A CG2 
299   N  N   . ASN   A  41  ? 1.5275 0.5741 1.7232 -0.1261 -0.1544 -0.0708 41  ASN   A N   
300   C  CA  . ASN   A  41  ? 1.5216 0.6246 1.7351 -0.1211 -0.1522 -0.0146 41  ASN   A CA  
301   C  C   . ASN   A  41  ? 1.5205 0.5759 1.7260 -0.0784 -0.1507 -0.0109 41  ASN   A C   
302   O  O   . ASN   A  41  ? 1.5212 0.7916 1.6654 -0.0699 -0.1233 0.0391  41  ASN   A O   
303   C  CB  . ASN   A  41  ? 1.4925 0.7124 1.7774 -0.1892 -0.1927 -0.0188 41  ASN   A CB  
304   C  CG  . ASN   A  41  ? 1.4860 0.6008 1.8428 -0.2232 -0.2042 -0.0086 41  ASN   A CG  
305   O  OD1 . ASN   A  41  ? 1.4013 0.6170 1.8816 -0.1856 -0.2233 -0.0190 41  ASN   A OD1 
306   N  ND2 . ASN   A  41  ? 1.5248 0.7269 1.8369 -0.2432 -0.2178 0.0231  41  ASN   A ND2 
307   N  N   . GLY   A  42  ? 1.4967 0.5238 1.6990 -0.1062 -0.1293 -0.0370 42  GLY   A N   
308   C  CA  . GLY   A  42  ? 1.5128 0.5724 1.6387 -0.1678 -0.1400 -0.0418 42  GLY   A CA  
309   C  C   . GLY   A  42  ? 1.4795 0.5864 1.6015 -0.1748 -0.1555 -0.0529 42  GLY   A C   
310   O  O   . GLY   A  42  ? 1.5067 0.5797 1.5612 -0.1735 -0.2157 -0.0464 42  GLY   A O   
311   N  N   . VAL   A  43  ? 1.4777 0.5702 1.5557 -0.1938 -0.1657 -0.0456 43  VAL   A N   
312   C  CA  . VAL   A  43  ? 1.5182 0.5545 1.5143 -0.1838 -0.1517 -0.0505 43  VAL   A CA  
313   C  C   . VAL   A  43  ? 1.5250 0.5412 1.4853 -0.1926 -0.1925 -0.0546 43  VAL   A C   
314   O  O   . VAL   A  43  ? 1.5195 0.4019 1.4428 -0.2115 -0.2036 -0.1648 43  VAL   A O   
315   C  CB  . VAL   A  43  ? 1.4904 0.5847 1.5457 -0.1661 -0.1383 -0.0310 43  VAL   A CB  
316   C  CG1 . VAL   A  43  ? 1.4821 0.6394 1.5874 -0.1364 -0.1162 -0.0317 43  VAL   A CG1 
317   C  CG2 . VAL   A  43  ? 1.5053 0.5742 1.5521 -0.1765 -0.1074 -0.0256 43  VAL   A CG2 
318   N  N   . VAL   A  44  ? 1.5747 0.5526 1.4750 -0.1914 -0.1847 -0.0653 44  VAL   A N   
319   C  CA  . VAL   A  44  ? 1.5902 0.5953 1.4603 -0.1778 -0.2034 -0.0626 44  VAL   A CA  
320   C  C   . VAL   A  44  ? 1.5941 0.5718 1.4599 -0.1770 -0.2249 -0.0758 44  VAL   A C   
321   O  O   . VAL   A  44  ? 1.5004 0.6033 1.4623 -0.1959 -0.2525 -0.0612 44  VAL   A O   
322   C  CB  . VAL   A  44  ? 1.6585 0.6673 1.4343 -0.1948 -0.2302 -0.0943 44  VAL   A CB  
323   C  CG1 . VAL   A  44  ? 1.6607 0.7403 1.4455 -0.2271 -0.2011 -0.0881 44  VAL   A CG1 
324   C  CG2 . VAL   A  44  ? 1.6864 0.6983 1.4005 -0.1888 -0.2284 -0.0571 44  VAL   A CG2 
325   N  N   . ILE   A  45  ? 1.5802 0.5471 1.4200 -0.1079 -0.2285 -0.0864 45  ILE   A N   
326   C  CA  . ILE   A  45  ? 1.6421 0.5503 1.4102 -0.0477 -0.2497 -0.0847 45  ILE   A CA  
327   C  C   . ILE   A  45  ? 1.6557 0.6082 1.3907 -0.0082 -0.2768 -0.0563 45  ILE   A C   
328   O  O   . ILE   A  45  ? 1.6835 0.5354 1.3886 0.0404  -0.2797 -0.0981 45  ILE   A O   
329   C  CB  . ILE   A  45  ? 1.6145 0.5835 1.4299 -0.0471 -0.2408 -0.0651 45  ILE   A CB  
330   C  CG1 . ILE   A  45  ? 1.6555 0.6519 1.4281 -0.0145 -0.2201 0.0301  45  ILE   A CG1 
331   C  CG2 . ILE   A  45  ? 1.6234 0.5332 1.4369 -0.0304 -0.2207 -0.0357 45  ILE   A CG2 
332   C  CD1 . ILE   A  45  ? 1.6338 0.6940 1.4099 -0.0102 -0.2065 0.0364  45  ILE   A CD1 
333   N  N   . ALA   A  46  ? 1.6468 0.6245 1.3773 -0.0114 -0.3041 -0.0906 46  ALA   A N   
334   C  CA  . ALA   A  46  ? 1.5821 0.5809 1.3659 -0.0100 -0.3304 -0.0816 46  ALA   A CA  
335   C  C   . ALA   A  46  ? 1.5806 0.5414 1.3322 -0.0204 -0.3228 -0.0910 46  ALA   A C   
336   O  O   . ALA   A  46  ? 1.5474 0.5207 1.3345 0.0320  -0.3050 -0.1170 46  ALA   A O   
337   C  CB  . ALA   A  46  ? 1.6243 0.5979 1.3644 -0.0404 -0.3432 -0.0996 46  ALA   A CB  
338   N  N   . THR   A  47  ? 1.5560 0.5280 1.3027 -0.0146 -0.3353 -0.0239 47  THR   A N   
339   C  CA  . THR   A  47  ? 1.5605 0.5466 1.3433 -0.0062 -0.3371 -0.0273 47  THR   A CA  
340   C  C   . THR   A  47  ? 1.6315 0.5399 1.3351 0.0060  -0.3387 0.0047  47  THR   A C   
341   O  O   . THR   A  47  ? 1.6005 0.4379 1.3593 -0.0371 -0.3105 0.0135  47  THR   A O   
342   C  CB  . THR   A  47  ? 1.5522 0.5509 1.2923 -0.0014 -0.3341 -0.0378 47  THR   A CB  
343   O  OG1 . THR   A  47  ? 1.5034 0.6269 1.3330 0.0047  -0.3106 -0.0841 47  THR   A OG1 
344   C  CG2 . THR   A  47  ? 1.5109 0.5508 1.2490 -0.0057 -0.3549 -0.0534 47  THR   A CG2 
345   N  N   . GLU   A  48  ? 1.7241 0.6047 1.4355 0.0590  -0.3179 -0.0450 48  GLU   A N   
346   C  CA  . GLU   A  48  ? 1.8358 0.7124 1.4326 0.0559  -0.3471 -0.0625 48  GLU   A CA  
347   C  C   . GLU   A  48  ? 1.8526 0.6703 1.4700 0.0556  -0.3600 -0.0289 48  GLU   A C   
348   O  O   . GLU   A  48  ? 1.8726 0.6364 1.4726 0.0306  -0.3748 0.0475  48  GLU   A O   
349   C  CB  . GLU   A  48  ? 1.9598 0.7235 1.5490 0.0707  -0.3305 -0.1087 48  GLU   A CB  
350   C  CG  . GLU   A  48  ? 2.0759 0.8532 1.5713 0.1328  -0.2989 -0.1337 48  GLU   A CG  
351   C  CD  . GLU   A  48  ? 2.1838 0.8790 1.6580 0.1807  -0.2492 -0.1668 48  GLU   A CD  
352   O  OE1 . GLU   A  48  ? 2.2012 0.7798 1.7741 0.2173  -0.2112 -0.1348 48  GLU   A OE1 
353   O  OE2 . GLU   A  48  ? 2.3533 0.7704 1.6370 0.2437  -0.2753 -0.2434 48  GLU   A OE2 
354   N  N   . LYS   A  49  ? 1.8533 0.7406 1.4567 0.0488  -0.3796 -0.0387 49  LYS   A N   
355   C  CA  . LYS   A  49  ? 1.8727 0.8481 1.5222 0.0104  -0.3571 -0.0223 49  LYS   A CA  
356   C  C   . LYS   A  49  ? 1.8814 0.9198 1.5918 0.0224  -0.3190 -0.0484 49  LYS   A C   
357   O  O   . LYS   A  49  ? 1.9363 1.0186 1.5875 0.0227  -0.3310 0.0099  49  LYS   A O   
358   C  CB  . LYS   A  49  ? 1.8926 0.9426 1.5411 0.0260  -0.3105 0.0593  49  LYS   A CB  
359   C  CG  . LYS   A  49  ? 1.9302 0.9278 1.5846 0.0519  -0.2820 0.0954  49  LYS   A CG  
360   C  CD  . LYS   A  49  ? 1.9954 0.9848 1.6732 0.0566  -0.2428 0.1641  49  LYS   A CD  
361   C  CE  . LYS   A  49  ? 2.0194 1.0995 1.7688 0.0721  -0.2743 0.1685  49  LYS   A CE  
362   N  NZ  . LYS   A  49  ? 2.1020 1.1770 1.8032 0.0652  -0.2506 0.2373  49  LYS   A NZ  
363   N  N   . LYS   A  50  ? 1.8628 0.9675 1.6374 -0.0027 -0.3621 -0.0469 50  LYS   A N   
364   C  CA  . LYS   A  50  ? 1.9618 0.9940 1.6770 -0.0388 -0.3113 -0.1131 50  LYS   A CA  
365   C  C   . LYS   A  50  ? 1.9650 0.8690 1.6661 -0.1130 -0.3561 -0.1560 50  LYS   A C   
366   O  O   . LYS   A  50  ? 2.0942 0.5769 1.7567 -0.2162 -0.2503 -0.1455 50  LYS   A O   
367   C  CB  . LYS   A  50  ? 2.0311 1.0698 1.7150 -0.0224 -0.3122 -0.0517 50  LYS   A CB  
368   C  CG  . LYS   A  50  ? 2.1043 0.9965 1.7222 -0.0319 -0.3007 -0.0923 50  LYS   A CG  
369   C  CD  . LYS   A  50  ? 2.1557 0.9777 1.7782 -0.0421 -0.3022 -0.0977 50  LYS   A CD  
370   C  CE  . LYS   A  50  ? 2.1300 1.1255 1.8252 -0.0543 -0.2680 -0.1555 50  LYS   A CE  
371   N  NZ  . LYS   A  50  ? 2.1587 1.1896 1.8761 -0.1077 -0.2860 -0.2463 50  LYS   A NZ  
372   N  N   . SER   A  51  ? 2.0195 1.0053 1.6533 -0.0674 -0.3436 -0.1661 51  SER   A N   
373   C  CA  . SER   A  51  ? 2.0392 1.1772 1.6215 -0.0404 -0.3322 -0.1567 51  SER   A CA  
374   C  C   . SER   A  51  ? 2.1184 1.2942 1.7251 0.0283  -0.3188 -0.2706 51  SER   A C   
375   O  O   . SER   A  51  ? 2.2317 1.3011 1.8458 0.0401  -0.2307 -0.3077 51  SER   A O   
376   C  CB  . SER   A  51  ? 2.0544 1.3009 1.6373 -0.0390 -0.3392 -0.0382 51  SER   A CB  
377   O  OG  . SER   A  51  ? 2.0977 1.3412 1.6409 -0.0275 -0.4162 0.0700  51  SER   A OG  
378   N  N   . SER   A  52  ? 2.0318 1.2662 1.7321 0.0996  -0.3306 -0.4615 52  SER   A N   
379   C  CA  . SER   A  52  ? 2.1111 1.2520 1.7343 0.1598  -0.2829 -0.5513 52  SER   A CA  
380   C  C   . SER   A  52  ? 2.0744 1.1502 1.7338 0.1980  -0.2998 -0.5471 52  SER   A C   
381   O  O   . SER   A  52  ? 2.0564 1.2064 1.8243 0.2475  -0.3481 -0.5368 52  SER   A O   
382   C  CB  . SER   A  52  ? 2.0254 1.2528 1.8413 0.2012  -0.2091 -0.5994 52  SER   A CB  
383   O  OG  . SER   A  52  ? 2.1544 1.2003 1.8835 0.2619  -0.1441 -0.6702 52  SER   A OG  
384   N  N   . SER   A  53  ? 2.1127 0.9774 1.7962 0.2237  -0.2176 -0.4961 53  SER   A N   
385   C  CA  . SER   A  53  ? 2.0926 0.9244 1.7783 0.1971  -0.2193 -0.4053 53  SER   A CA  
386   C  C   . SER   A  53  ? 2.1493 0.8378 1.7896 0.1922  -0.2653 -0.4076 53  SER   A C   
387   O  O   . SER   A  53  ? 2.1854 0.6755 1.8134 0.0193  -0.2063 -0.3910 53  SER   A O   
388   C  CB  . SER   A  53  ? 2.0749 0.8477 1.7554 0.2218  -0.2100 -0.4014 53  SER   A CB  
389   O  OG  . SER   A  53  ? 1.9666 0.8530 1.7354 0.2381  -0.1372 -0.4264 53  SER   A OG  
390   N  N   . PRO   A  54  ? 2.1763 0.9387 1.7859 0.1760  -0.3210 -0.3696 54  PRO   A N   
391   C  CA  . PRO   A  54  ? 2.1368 0.9017 1.7519 0.1345  -0.2952 -0.3198 54  PRO   A CA  
392   C  C   . PRO   A  54  ? 1.9840 0.8989 1.7112 0.1747  -0.3384 -0.2952 54  PRO   A C   
393   O  O   . PRO   A  54  ? 1.9834 0.9898 1.7427 0.1914  -0.3803 -0.2694 54  PRO   A O   
394   C  CB  . PRO   A  54  ? 2.1783 0.9907 1.7479 0.1540  -0.3227 -0.3710 54  PRO   A CB  
395   C  CG  . PRO   A  54  ? 2.2366 1.0205 1.7456 0.1790  -0.2912 -0.4114 54  PRO   A CG  
396   C  CD  . PRO   A  54  ? 2.2254 0.9944 1.7596 0.1541  -0.2981 -0.4298 54  PRO   A CD  
397   N  N   . LEU   A  55  ? 2.0069 0.7589 1.5838 0.1191  -0.3244 -0.2510 55  LEU   A N   
398   C  CA  . LEU   A  55  ? 1.8802 0.8321 1.4993 0.1386  -0.2889 -0.2060 55  LEU   A CA  
399   C  C   . LEU   A  55  ? 1.8610 0.7359 1.4523 0.1224  -0.2833 -0.1304 55  LEU   A C   
400   O  O   . LEU   A  55  ? 1.7938 0.7366 1.3718 0.1333  -0.2702 -0.1312 55  LEU   A O   
401   C  CB  . LEU   A  55  ? 1.8883 0.7225 1.4386 0.1384  -0.2863 -0.2373 55  LEU   A CB  
402   C  CG  . LEU   A  55  ? 1.8524 0.7027 1.4523 0.1516  -0.2924 -0.2445 55  LEU   A CG  
403   C  CD1 . LEU   A  55  ? 1.8642 0.7222 1.4570 0.1551  -0.2789 -0.2376 55  LEU   A CD1 
404   C  CD2 . LEU   A  55  ? 1.8527 0.7015 1.4377 0.1490  -0.2894 -0.2461 55  LEU   A CD2 
405   N  N   . ALA   A  56  ? 1.8520 0.8862 1.4268 0.1178  -0.2829 -0.1631 56  ALA   A N   
406   C  CA  . ALA   A  56  ? 1.7926 0.7846 1.5265 0.1006  -0.2406 -0.1822 56  ALA   A CA  
407   C  C   . ALA   A  56  ? 1.7597 0.7859 1.5105 0.0789  -0.2599 -0.1277 56  ALA   A C   
408   O  O   . ALA   A  56  ? 1.7613 0.7267 1.4511 0.1314  -0.2937 -0.1704 56  ALA   A O   
409   C  CB  . ALA   A  56  ? 1.8044 0.8585 1.4988 0.0777  -0.2415 -0.1966 56  ALA   A CB  
410   N  N   . MET   A  57  ? 1.7410 0.7780 1.5344 0.0875  -0.2319 -0.1114 57  MET   A N   
411   C  CA  . MET   A  57  ? 1.7363 0.8241 1.6084 0.1083  -0.2369 -0.0972 57  MET   A CA  
412   C  C   . MET   A  57  ? 1.7649 0.7116 1.6246 0.0520  -0.2133 -0.1476 57  MET   A C   
413   O  O   . MET   A  57  ? 1.7379 0.4390 1.6552 0.0926  -0.1205 -0.0888 57  MET   A O   
414   C  CB  . MET   A  57  ? 1.7255 0.8384 1.6227 0.1767  -0.2318 -0.0629 57  MET   A CB  
415   C  CG  . MET   A  57  ? 1.7732 1.0399 1.6253 0.2559  -0.2330 -0.1002 57  MET   A CG  
416   S  SD  . MET   A  57  ? 1.8098 1.1514 1.6603 0.4077  -0.2768 0.0457  57  MET   A SD  
417   C  CE  . MET   A  57  ? 1.8137 1.1480 1.6421 0.3864  -0.2623 0.0421  57  MET   A CE  
418   N  N   . SER   A  58  ? 1.8131 0.8490 1.8167 -0.0670 -0.1613 -0.2011 58  SER   A N   
419   C  CA  . SER   A  58  ? 1.8232 0.8918 1.8363 -0.1592 -0.0983 -0.2696 58  SER   A CA  
420   C  C   . SER   A  58  ? 1.8218 0.8249 1.9374 -0.1305 -0.1239 -0.2315 58  SER   A C   
421   O  O   . SER   A  58  ? 1.8384 0.9530 1.9593 -0.1757 -0.0039 -0.2169 58  SER   A O   
422   C  CB  . SER   A  58  ? 1.8122 0.9659 1.9091 -0.2291 -0.1147 -0.2944 58  SER   A CB  
423   O  OG  . SER   A  58  ? 1.7526 0.9300 2.0015 -0.3339 -0.1066 -0.3367 58  SER   A OG  
424   N  N   . GLU   A  59  ? 1.8175 0.7696 1.9028 -0.1457 -0.1932 -0.2836 59  GLU   A N   
425   C  CA  . GLU   A  59  ? 1.8345 0.7635 1.9009 -0.1507 -0.2106 -0.2966 59  GLU   A CA  
426   C  C   . GLU   A  59  ? 1.8148 0.5847 1.8455 -0.0543 -0.1776 -0.3707 59  GLU   A C   
427   O  O   . GLU   A  59  ? 1.8257 0.3727 2.0622 -0.0324 -0.1677 -0.3917 59  GLU   A O   
428   C  CB  . GLU   A  59  ? 1.9223 0.7522 1.8927 -0.1394 -0.2171 -0.2863 59  GLU   A CB  
429   C  CG  . GLU   A  59  ? 2.0070 0.8234 1.9387 -0.2130 -0.2639 -0.2794 59  GLU   A CG  
430   C  CD  . GLU   A  59  ? 2.0575 0.9763 1.9150 -0.2776 -0.2442 -0.2439 59  GLU   A CD  
431   O  OE1 . GLU   A  59  ? 2.0320 0.7851 1.9624 -0.1958 -0.3052 -0.2714 59  GLU   A OE1 
432   O  OE2 . GLU   A  59  ? 2.1643 1.0622 2.0331 -0.1902 -0.2461 -0.3584 59  GLU   A OE2 
433   N  N   . THR   A  60  ? 1.7475 0.6025 1.7565 -0.0944 -0.2457 -0.3262 60  THR   A N   
434   C  CA  . THR   A  60  ? 1.6940 0.6142 1.6728 -0.0845 -0.2049 -0.2962 60  THR   A CA  
435   C  C   . THR   A  60  ? 1.6762 0.7908 1.6766 -0.1435 -0.2745 -0.3131 60  THR   A C   
436   O  O   . THR   A  60  ? 1.6479 0.9331 1.7463 -0.2355 -0.2553 -0.3051 60  THR   A O   
437   C  CB  . THR   A  60  ? 1.6856 0.6283 1.5985 -0.0577 -0.2356 -0.3038 60  THR   A CB  
438   O  OG1 . THR   A  60  ? 1.6871 0.6348 1.5157 -0.0574 -0.2001 -0.2885 60  THR   A OG1 
439   C  CG2 . THR   A  60  ? 1.6687 0.5896 1.6101 -0.0041 -0.2199 -0.3156 60  THR   A CG2 
440   N  N   . LEU   A  61  ? 1.7976 0.8710 1.6205 -0.1115 -0.2671 -0.1718 61  LEU   A N   
441   C  CA  . LEU   A  61  ? 1.8716 0.9612 1.6071 -0.0234 -0.2373 -0.1460 61  LEU   A CA  
442   C  C   . LEU   A  61  ? 1.8806 0.9093 1.5183 -0.0134 -0.2658 -0.1194 61  LEU   A C   
443   O  O   . LEU   A  61  ? 1.8075 1.0273 1.4028 -0.0073 -0.3411 -0.0607 61  LEU   A O   
444   C  CB  . LEU   A  61  ? 1.9483 1.0351 1.6636 0.0706  -0.1834 -0.1517 61  LEU   A CB  
445   C  CG  . LEU   A  61  ? 1.9110 1.2414 1.7224 0.0822  -0.1933 -0.1991 61  LEU   A CG  
446   C  CD1 . LEU   A  61  ? 1.8886 1.2967 1.7627 0.1876  -0.1715 -0.1987 61  LEU   A CD1 
447   C  CD2 . LEU   A  61  ? 1.9354 1.1917 1.7349 0.0423  -0.1967 -0.2626 61  LEU   A CD2 
448   N  N   . SER   A  62  ? 1.8897 0.8867 1.5425 0.0324  -0.2173 -0.1265 62  SER   A N   
449   C  CA  . SER   A  62  ? 1.8164 0.8769 1.6309 0.0592  -0.2094 -0.0839 62  SER   A CA  
450   C  C   . SER   A  62  ? 1.7467 0.7573 1.6319 -0.0373 -0.2160 -0.0951 62  SER   A C   
451   O  O   . SER   A  62  ? 1.7515 0.9942 1.6289 -0.0096 -0.2612 -0.0883 62  SER   A O   
452   C  CB  . SER   A  62  ? 1.8330 0.8919 1.6829 0.1763  -0.1847 -0.0303 62  SER   A CB  
453   O  OG  . SER   A  62  ? 1.8593 0.8723 1.7194 0.1849  -0.1599 -0.0233 62  SER   A OG  
454   N  N   . LYS   A  63  ? 1.7273 0.7045 1.5272 -0.0225 -0.2933 -0.1053 63  LYS   A N   
455   C  CA  . LYS   A  63  ? 1.7081 0.7520 1.4237 -0.0353 -0.2901 -0.1617 63  LYS   A CA  
456   C  C   . LYS   A  63  ? 1.7060 0.5972 1.4023 -0.0440 -0.3221 -0.1528 63  LYS   A C   
457   O  O   . LYS   A  63  ? 1.7715 0.7086 1.3941 -0.0117 -0.3230 -0.1781 63  LYS   A O   
458   C  CB  . LYS   A  63  ? 1.6791 0.7670 1.4508 -0.0569 -0.2918 -0.1386 63  LYS   A CB  
459   C  CG  . LYS   A  63  ? 1.6701 0.7429 1.4303 -0.0608 -0.3227 -0.1589 63  LYS   A CG  
460   C  CD  . LYS   A  63  ? 1.6554 0.7590 1.4154 -0.0646 -0.3437 -0.2130 63  LYS   A CD  
461   C  CE  . LYS   A  63  ? 1.6700 0.8114 1.4294 -0.0580 -0.3228 -0.1952 63  LYS   A CE  
462   N  NZ  . LYS   A  63  ? 1.6779 0.8430 1.4951 -0.0993 -0.3244 -0.2345 63  LYS   A NZ  
463   N  N   . VAL   A  64  ? 1.6959 0.4899 1.3387 -0.0781 -0.3086 -0.1459 64  VAL   A N   
464   C  CA  . VAL   A  64  ? 1.6878 0.5524 1.3597 -0.0885 -0.2398 -0.1116 64  VAL   A CA  
465   C  C   . VAL   A  64  ? 1.6972 0.5798 1.3307 -0.1182 -0.2134 -0.0372 64  VAL   A C   
466   O  O   . VAL   A  64  ? 1.7426 0.4830 1.3801 -0.1528 -0.1875 0.0031  64  VAL   A O   
467   C  CB  . VAL   A  64  ? 1.6955 0.6023 1.4068 -0.1011 -0.2404 -0.1443 64  VAL   A CB  
468   C  CG1 . VAL   A  64  ? 1.6738 0.7339 1.4358 -0.0797 -0.1966 -0.1345 64  VAL   A CG1 
469   C  CG2 . VAL   A  64  ? 1.7377 0.5785 1.4068 -0.0707 -0.2521 -0.1690 64  VAL   A CG2 
470   N  N   . SER   A  65  ? 1.6707 0.4694 1.3122 -0.1342 -0.1746 -0.0148 65  SER   A N   
471   C  CA  . SER   A  65  ? 1.6156 0.4316 1.2851 -0.0844 -0.1831 0.0031  65  SER   A CA  
472   C  C   . SER   A  65  ? 1.6252 0.4360 1.2534 -0.1258 -0.1518 0.0152  65  SER   A C   
473   O  O   . SER   A  65  ? 1.6529 0.2701 1.2965 -0.1903 -0.1663 0.0270  65  SER   A O   
474   C  CB  . SER   A  65  ? 1.6126 0.3786 1.2771 -0.0658 -0.2000 0.0060  65  SER   A CB  
475   O  OG  . SER   A  65  ? 1.5707 0.4079 1.2842 -0.0409 -0.2117 0.0175  65  SER   A OG  
476   N  N   . LEU   A  66  ? 1.5728 0.4441 1.3173 -0.0614 -0.1462 -0.0179 66  LEU   A N   
477   C  CA  . LEU   A  66  ? 1.5612 0.4394 1.3378 -0.0413 -0.1214 -0.0032 66  LEU   A CA  
478   C  C   . LEU   A  66  ? 1.5323 0.4284 1.3515 -0.0230 -0.1106 0.0015  66  LEU   A C   
479   O  O   . LEU   A  66  ? 1.5317 0.3761 1.3230 0.0587  -0.0820 0.0258  66  LEU   A O   
480   C  CB  . LEU   A  66  ? 1.5725 0.4695 1.3200 -0.0529 -0.1191 0.0206  66  LEU   A CB  
481   C  CG  . LEU   A  66  ? 1.5887 0.4976 1.3177 -0.0508 -0.1107 -0.0035 66  LEU   A CG  
482   C  CD1 . LEU   A  66  ? 1.5790 0.5204 1.3237 -0.0267 -0.1269 -0.0399 66  LEU   A CD1 
483   C  CD2 . LEU   A  66  ? 1.5883 0.4576 1.3198 -0.0302 -0.1054 -0.0196 66  LEU   A CD2 
484   N  N   . LEU   A  67  ? 1.5525 0.4716 1.3542 -0.0447 -0.1135 -0.0117 67  LEU   A N   
485   C  CA  . LEU   A  67  ? 1.5524 0.4788 1.3994 -0.0860 -0.1053 -0.0346 67  LEU   A CA  
486   C  C   . LEU   A  67  ? 1.5653 0.4104 1.4575 -0.1789 -0.0993 -0.0176 67  LEU   A C   
487   O  O   . LEU   A  67  ? 1.5778 0.5528 1.5623 -0.2527 -0.0806 -0.0321 67  LEU   A O   
488   C  CB  . LEU   A  67  ? 1.5485 0.5008 1.3469 -0.0695 -0.1270 -0.0684 67  LEU   A CB  
489   C  CG  . LEU   A  67  ? 1.5469 0.4991 1.3394 -0.0988 -0.1420 -0.1068 67  LEU   A CG  
490   C  CD1 . LEU   A  67  ? 1.5302 0.4634 1.3210 -0.1039 -0.1322 -0.1227 67  LEU   A CD1 
491   C  CD2 . LEU   A  67  ? 1.5394 0.4985 1.3311 -0.1023 -0.1463 -0.1131 67  LEU   A CD2 
492   N  N   . THR   A  68  ? 1.5397 0.4222 1.4831 -0.2145 -0.1212 -0.0020 68  THR   A N   
493   C  CA  . THR   A  68  ? 1.4919 0.4498 1.5368 -0.1858 -0.1568 0.0110  68  THR   A CA  
494   C  C   . THR   A  68  ? 1.4821 0.4993 1.5571 -0.1868 -0.1595 -0.0325 68  THR   A C   
495   O  O   . THR   A  68  ? 1.4312 0.5187 1.6010 -0.2091 -0.1805 -0.0175 68  THR   A O   
496   C  CB  . THR   A  68  ? 1.4837 0.4032 1.5203 -0.2054 -0.1514 0.0749  68  THR   A CB  
497   O  OG1 . THR   A  68  ? 1.5080 0.2281 1.5605 -0.2111 -0.2383 0.1053  68  THR   A OG1 
498   C  CG2 . THR   A  68  ? 1.5182 0.4512 1.5144 -0.1937 -0.1742 0.0883  68  THR   A CG2 
499   N  N   . PRO   A  69  ? 1.4830 0.5533 1.5819 -0.1332 -0.1489 -0.0697 69  PRO   A N   
500   C  CA  . PRO   A  69  ? 1.4764 0.6200 1.6021 -0.1467 -0.1393 -0.0839 69  PRO   A CA  
501   C  C   . PRO   A  69  ? 1.4828 0.6115 1.5577 -0.1250 -0.0958 -0.1176 69  PRO   A C   
502   O  O   . PRO   A  69  ? 1.4774 0.7822 1.6244 -0.1032 -0.1174 -0.1511 69  PRO   A O   
503   C  CB  . PRO   A  69  ? 1.4951 0.6137 1.6652 -0.1502 -0.1350 -0.0575 69  PRO   A CB  
504   C  CG  . PRO   A  69  ? 1.5041 0.6192 1.6762 -0.1594 -0.1704 -0.0405 69  PRO   A CG  
505   C  CD  . PRO   A  69  ? 1.5075 0.5665 1.6294 -0.1667 -0.1596 -0.0531 69  PRO   A CD  
506   N  N   . ASP   A  70  ? 1.4785 0.6017 1.5188 -0.1072 -0.0793 -0.1502 70  ASP   A N   
507   C  CA  . ASP   A  70  ? 1.5026 0.6898 1.4752 -0.1233 -0.0702 -0.1341 70  ASP   A CA  
508   C  C   . ASP   A  70  ? 1.4336 0.6715 1.4494 -0.1480 -0.0938 -0.1676 70  ASP   A C   
509   O  O   . ASP   A  70  ? 1.3809 0.5516 1.4856 -0.1969 -0.1414 -0.2157 70  ASP   A O   
510   C  CB  . ASP   A  70  ? 1.6057 0.8068 1.4642 -0.1706 -0.0179 -0.1473 70  ASP   A CB  
511   C  CG  . ASP   A  70  ? 1.6750 0.8202 1.4682 -0.1552 0.0364  -0.1724 70  ASP   A CG  
512   O  OD1 . ASP   A  70  ? 1.7584 1.0806 1.4807 -0.2487 0.0014  -0.1467 70  ASP   A OD1 
513   O  OD2 . ASP   A  70  ? 1.7867 1.0919 1.3261 -0.2731 0.0970  -0.2262 70  ASP   A OD2 
514   N  N   . ILE   A  71  ? 1.4505 0.5940 1.4287 -0.0803 -0.1273 -0.1757 71  ILE   A N   
515   C  CA  . ILE   A  71  ? 1.4841 0.5562 1.4214 -0.1094 -0.1495 -0.1504 71  ILE   A CA  
516   C  C   . ILE   A  71  ? 1.5219 0.5425 1.4205 -0.0845 -0.1374 -0.1255 71  ILE   A C   
517   O  O   . ILE   A  71  ? 1.4888 0.4751 1.4460 -0.1119 -0.1769 -0.1383 71  ILE   A O   
518   C  CB  . ILE   A  71  ? 1.4658 0.5002 1.3760 -0.0670 -0.1340 -0.1171 71  ILE   A CB  
519   C  CG1 . ILE   A  71  ? 1.4353 0.4894 1.3726 -0.0587 -0.1211 -0.0938 71  ILE   A CG1 
520   C  CG2 . ILE   A  71  ? 1.4839 0.4823 1.3641 -0.0776 -0.1570 -0.1154 71  ILE   A CG2 
521   C  CD1 . ILE   A  71  ? 1.4238 0.4953 1.3637 -0.0595 -0.1022 -0.1154 71  ILE   A CD1 
522   N  N   . GLY   A  72  ? 1.5675 0.5289 1.4591 -0.0703 -0.1250 -0.1002 72  GLY   A N   
523   C  CA  . GLY   A  72  ? 1.5376 0.4928 1.4377 -0.0523 -0.1362 -0.0685 72  GLY   A CA  
524   C  C   . GLY   A  72  ? 1.5043 0.4961 1.3530 -0.0815 -0.1365 -0.0364 72  GLY   A C   
525   O  O   . GLY   A  72  ? 1.4668 0.3733 1.3558 -0.0609 -0.1944 -0.0106 72  GLY   A O   
526   N  N   . ALA   A  73  ? 1.4817 0.4443 1.3419 -0.0459 -0.1728 -0.0113 73  ALA   A N   
527   C  CA  . ALA   A  73  ? 1.5312 0.4045 1.3332 -0.0742 -0.1908 0.0148  73  ALA   A CA  
528   C  C   . ALA   A  73  ? 1.5577 0.4440 1.3159 -0.0809 -0.2187 0.0079  73  ALA   A C   
529   O  O   . ALA   A  73  ? 1.5895 0.1993 1.3549 -0.0546 -0.2503 0.0169  73  ALA   A O   
530   C  CB  . ALA   A  73  ? 1.5375 0.4204 1.3409 -0.0672 -0.1993 0.0044  73  ALA   A CB  
531   N  N   . VAL   A  74  ? 1.5880 0.4419 1.3334 -0.0830 -0.2026 -0.0032 74  VAL   A N   
532   C  CA  . VAL   A  74  ? 1.5702 0.5015 1.3117 -0.0907 -0.2202 -0.0340 74  VAL   A CA  
533   C  C   . VAL   A  74  ? 1.5738 0.4540 1.3363 -0.0826 -0.2141 -0.0543 74  VAL   A C   
534   O  O   . VAL   A  74  ? 1.5599 0.3565 1.3393 -0.0717 -0.2257 -0.0582 74  VAL   A O   
535   C  CB  . VAL   A  74  ? 1.5842 0.5828 1.2989 -0.1187 -0.2271 -0.0533 74  VAL   A CB  
536   C  CG1 . VAL   A  74  ? 1.5707 0.6398 1.3023 -0.1371 -0.2140 -0.0514 74  VAL   A CG1 
537   C  CG2 . VAL   A  74  ? 1.5980 0.6548 1.2802 -0.1081 -0.2460 -0.0597 74  VAL   A CG2 
538   N  N   . TYR   A  75  ? 1.5168 0.4895 1.3031 -0.0530 -0.2421 -0.0432 75  TYR   A N   
539   C  CA  . TYR   A  75  ? 1.4850 0.5081 1.2850 -0.0542 -0.2430 -0.0652 75  TYR   A CA  
540   C  C   . TYR   A  75  ? 1.5045 0.5109 1.2684 -0.0168 -0.2471 -0.0717 75  TYR   A C   
541   O  O   . TYR   A  75  ? 1.5058 0.5434 1.2096 -0.0006 -0.2128 -0.0524 75  TYR   A O   
542   C  CB  . TYR   A  75  ? 1.4821 0.5213 1.2434 -0.0600 -0.2449 -0.0841 75  TYR   A CB  
543   C  CG  . TYR   A  75  ? 1.4968 0.5018 1.2048 -0.0325 -0.2954 -0.0990 75  TYR   A CG  
544   C  CD1 . TYR   A  75  ? 1.5081 0.4713 1.2063 -0.0130 -0.2719 -0.0879 75  TYR   A CD1 
545   C  CD2 . TYR   A  75  ? 1.4969 0.5648 1.1875 -0.0185 -0.2900 -0.1385 75  TYR   A CD2 
546   C  CE1 . TYR   A  75  ? 1.5261 0.4718 1.2042 0.0045  -0.2577 -0.0608 75  TYR   A CE1 
547   C  CE2 . TYR   A  75  ? 1.5071 0.6262 1.1679 -0.0004 -0.2917 -0.0918 75  TYR   A CE2 
548   C  CZ  . TYR   A  75  ? 1.5157 0.5424 1.1844 0.0218  -0.2417 -0.0606 75  TYR   A CZ  
549   O  OH  . TYR   A  75  ? 1.5220 0.6070 1.1570 0.0253  -0.2369 0.0005  75  TYR   A OH  
550   N  N   . SER   A  76  ? 1.5367 0.4256 1.3247 -0.0059 -0.2381 -0.1025 76  SER   A N   
551   C  CA  . SER   A  76  ? 1.6097 0.3930 1.3550 0.0042  -0.2784 -0.0890 76  SER   A CA  
552   C  C   . SER   A  76  ? 1.6032 0.2515 1.3190 -0.0053 -0.2238 -0.0940 76  SER   A C   
553   O  O   . SER   A  76  ? 1.6567 0.2333 1.3740 -0.1043 -0.2569 -0.0892 76  SER   A O   
554   C  CB  . SER   A  76  ? 1.5519 0.4183 1.4074 -0.0169 -0.2989 -0.1136 76  SER   A CB  
555   O  OG  . SER   A  76  ? 1.5669 0.4853 1.4803 0.0465  -0.3359 -0.1646 76  SER   A OG  
556   N  N   . GLY   A  77  ? 1.6889 0.2323 1.2670 -0.0014 -0.2225 -0.0925 77  GLY   A N   
557   C  CA  . GLY   A  77  ? 1.6827 0.2765 1.2336 -0.0163 -0.2069 -0.1031 77  GLY   A CA  
558   C  C   . GLY   A  77  ? 1.7080 0.1763 1.2376 -0.0334 -0.2144 -0.1205 77  GLY   A C   
559   O  O   . GLY   A  77  ? 1.6914 0.2202 1.2597 -0.0502 -0.2306 -0.1010 77  GLY   A O   
560   N  N   . MET   A  78  ? 1.7406 0.1822 1.1761 -0.0227 -0.2448 -0.1737 78  MET   A N   
561   C  CA  . MET   A  78  ? 1.7421 0.3671 1.1772 -0.0157 -0.2347 -0.1545 78  MET   A CA  
562   C  C   . MET   A  78  ? 1.7572 0.3862 1.1221 0.0085  -0.2311 -0.1537 78  MET   A C   
563   O  O   . MET   A  78  ? 1.7716 0.3839 1.1826 -0.0796 -0.1927 -0.1855 78  MET   A O   
564   C  CB  . MET   A  78  ? 1.7489 0.4084 1.2188 -0.0068 -0.2564 -0.1248 78  MET   A CB  
565   C  CG  . MET   A  78  ? 1.7986 0.4052 1.2947 -0.0373 -0.2672 -0.0759 78  MET   A CG  
566   S  SD  . MET   A  78  ? 1.8035 0.5329 1.3541 -0.0449 -0.2766 0.0054  78  MET   A SD  
567   C  CE  . MET   A  78  ? 1.8054 0.5446 1.3892 -0.0601 -0.2590 0.0369  78  MET   A CE  
568   N  N   . GLY   A  79  ? 1.7514 0.5054 1.1386 0.0305  -0.2355 -0.1084 79  GLY   A N   
569   C  CA  . GLY   A  79  ? 1.6728 0.4854 1.1429 0.0362  -0.2751 -0.1535 79  GLY   A CA  
570   C  C   . GLY   A  79  ? 1.6155 0.4594 1.1270 0.0716  -0.3157 -0.1136 79  GLY   A C   
571   O  O   . GLY   A  79  ? 1.5722 0.4531 1.1386 0.1122  -0.3046 -0.0699 79  GLY   A O   
572   N  N   . PRO   A  80  ? 1.5893 0.4774 1.1201 0.0649  -0.3484 -0.1516 80  PRO   A N   
573   C  CA  . PRO   A  80  ? 1.5582 0.4884 1.1764 0.0646  -0.3316 -0.1072 80  PRO   A CA  
574   C  C   . PRO   A  80  ? 1.5580 0.5212 1.1744 0.0841  -0.3080 -0.1042 80  PRO   A C   
575   O  O   . PRO   A  80  ? 1.5135 0.5528 1.1550 0.0736  -0.3527 -0.1823 80  PRO   A O   
576   C  CB  . PRO   A  80  ? 1.5849 0.4892 1.1235 0.0626  -0.3329 -0.1599 80  PRO   A CB  
577   C  CG  . PRO   A  80  ? 1.5982 0.5386 1.1207 0.0471  -0.3463 -0.1722 80  PRO   A CG  
578   C  CD  . PRO   A  80  ? 1.5951 0.5458 1.1280 0.0529  -0.3315 -0.1934 80  PRO   A CD  
579   N  N   . ASP   A  81  ? 1.5677 0.6139 1.1853 0.0563  -0.2558 -0.0565 81  ASP   A N   
580   C  CA  . ASP   A  81  ? 1.5538 0.5639 1.2012 0.0467  -0.2311 -0.0935 81  ASP   A CA  
581   C  C   . ASP   A  81  ? 1.5316 0.4715 1.2702 0.0042  -0.2254 -0.1121 81  ASP   A C   
582   O  O   . ASP   A  81  ? 1.4730 0.4445 1.3237 0.0207  -0.1746 -0.1263 81  ASP   A O   
583   C  CB  . ASP   A  81  ? 1.6124 0.6602 1.1775 0.0551  -0.2595 -0.0229 81  ASP   A CB  
584   C  CG  . ASP   A  81  ? 1.6426 0.6897 1.1765 0.0828  -0.2687 0.0318  81  ASP   A CG  
585   O  OD1 . ASP   A  81  ? 1.6869 0.6967 1.1343 0.0976  -0.3137 0.1640  81  ASP   A OD1 
586   O  OD2 . ASP   A  81  ? 1.7408 0.7602 1.1548 0.0731  -0.2240 0.0649  81  ASP   A OD2 
587   N  N   . TYR   A  82  ? 1.5315 0.4186 1.2773 -0.0024 -0.2205 -0.1131 82  TYR   A N   
588   C  CA  . TYR   A  82  ? 1.5545 0.4443 1.2970 0.0055  -0.1809 -0.1026 82  TYR   A CA  
589   C  C   . TYR   A  82  ? 1.5623 0.4777 1.2956 -0.0383 -0.1636 -0.0711 82  TYR   A C   
590   O  O   . TYR   A  82  ? 1.5101 0.5750 1.3255 0.0232  -0.0968 -0.0692 82  TYR   A O   
591   C  CB  . TYR   A  82  ? 1.5421 0.4785 1.2886 0.0111  -0.1900 -0.0674 82  TYR   A CB  
592   C  CG  . TYR   A  82  ? 1.5616 0.4603 1.2551 0.0280  -0.1817 -0.0812 82  TYR   A CG  
593   C  CD1 . TYR   A  82  ? 1.5769 0.4040 1.2562 0.0210  -0.1776 -0.0915 82  TYR   A CD1 
594   C  CD2 . TYR   A  82  ? 1.5565 0.4854 1.2333 0.0308  -0.1837 -0.1079 82  TYR   A CD2 
595   C  CE1 . TYR   A  82  ? 1.5449 0.4393 1.2200 -0.0006 -0.1869 -0.1080 82  TYR   A CE1 
596   C  CE2 . TYR   A  82  ? 1.5444 0.4538 1.2287 0.0073  -0.1918 -0.1208 82  TYR   A CE2 
597   C  CZ  . TYR   A  82  ? 1.5222 0.4366 1.2171 -0.0148 -0.2054 -0.1260 82  TYR   A CZ  
598   O  OH  . TYR   A  82  ? 1.4910 0.3704 1.1355 -0.0536 -0.2223 -0.1163 82  TYR   A OH  
599   N  N   . ARG   A  83  ? 1.5874 0.4235 1.2811 -0.0296 -0.1698 -0.0846 83  ARG   A N   
600   C  CA  . ARG   A  83  ? 1.5685 0.4301 1.2890 0.0111  -0.1957 -0.0651 83  ARG   A CA  
601   C  C   . ARG   A  83  ? 1.5425 0.4101 1.3621 -0.0234 -0.2138 -0.0287 83  ARG   A C   
602   O  O   . ARG   A  83  ? 1.4956 0.4357 1.4357 -0.0338 -0.2133 -0.1197 83  ARG   A O   
603   C  CB  . ARG   A  83  ? 1.5569 0.3862 1.2526 0.0245  -0.2196 -0.0472 83  ARG   A CB  
604   C  CG  . ARG   A  83  ? 1.5388 0.4243 1.2026 0.0093  -0.2096 -0.0363 83  ARG   A CG  
605   C  CD  . ARG   A  83  ? 1.5482 0.4125 1.1990 0.0222  -0.2113 -0.0227 83  ARG   A CD  
606   N  NE  . ARG   A  83  ? 1.5590 0.2998 1.1935 0.0340  -0.2214 -0.0218 83  ARG   A NE  
607   C  CZ  . ARG   A  83  ? 1.5931 0.2894 1.2104 0.0516  -0.2195 0.0040  83  ARG   A CZ  
608   N  NH1 . ARG   A  83  ? 1.6254 0.3145 1.2432 0.0161  -0.2215 0.0110  83  ARG   A NH1 
609   N  NH2 . ARG   A  83  ? 1.5863 0.2310 1.1740 0.0356  -0.2382 -0.0279 83  ARG   A NH2 
610   N  N   . VAL   A  84  ? 1.5595 0.3315 1.3626 -0.0067 -0.2019 0.0222  84  VAL   A N   
611   C  CA  . VAL   A  84  ? 1.5474 0.3135 1.3069 0.0243  -0.1861 0.0122  84  VAL   A CA  
612   C  C   . VAL   A  84  ? 1.6079 0.3132 1.2935 0.0098  -0.1995 -0.0638 84  VAL   A C   
613   O  O   . VAL   A  84  ? 1.5865 0.4266 1.2629 -0.0613 -0.2021 -0.1364 84  VAL   A O   
614   C  CB  . VAL   A  84  ? 1.5644 0.2894 1.3057 0.0487  -0.2079 0.0698  84  VAL   A CB  
615   C  CG1 . VAL   A  84  ? 1.5485 0.2680 1.3059 0.0919  -0.2102 0.0903  84  VAL   A CG1 
616   C  CG2 . VAL   A  84  ? 1.5824 0.3387 1.2908 0.0476  -0.2260 0.1009  84  VAL   A CG2 
617   N  N   . LEU   A  85  ? 1.6475 0.2882 1.2649 -0.0075 -0.1964 -0.1076 85  LEU   A N   
618   C  CA  . LEU   A  85  ? 1.7144 0.3702 1.2643 -0.0278 -0.1896 -0.1559 85  LEU   A CA  
619   C  C   . LEU   A  85  ? 1.7174 0.3906 1.3229 -0.0305 -0.1859 -0.1183 85  LEU   A C   
620   O  O   . LEU   A  85  ? 1.8003 0.5697 1.2880 -0.0194 -0.1040 -0.1188 85  LEU   A O   
621   C  CB  . LEU   A  85  ? 1.7391 0.3885 1.2855 -0.0707 -0.1907 -0.1818 85  LEU   A CB  
622   C  CG  . LEU   A  85  ? 1.7523 0.5008 1.2983 -0.0684 -0.2253 -0.1876 85  LEU   A CG  
623   C  CD1 . LEU   A  85  ? 1.8016 0.5486 1.3627 -0.1192 -0.2085 -0.1585 85  LEU   A CD1 
624   C  CD2 . LEU   A  85  ? 1.7580 0.5405 1.3229 -0.0692 -0.1713 -0.2335 85  LEU   A CD2 
625   N  N   . VAL   A  86  ? 1.7249 0.3983 1.3306 -0.0625 -0.2024 -0.1421 86  VAL   A N   
626   C  CA  . VAL   A  86  ? 1.6894 0.5308 1.3548 -0.0371 -0.2231 -0.1190 86  VAL   A CA  
627   C  C   . VAL   A  86  ? 1.6765 0.5457 1.3378 -0.0406 -0.1920 -0.0793 86  VAL   A C   
628   O  O   . VAL   A  86  ? 1.6679 0.5188 1.3185 -0.0254 -0.2065 -0.0541 86  VAL   A O   
629   C  CB  . VAL   A  86  ? 1.6819 0.4625 1.3976 -0.0557 -0.2324 -0.1521 86  VAL   A CB  
630   C  CG1 . VAL   A  86  ? 1.6756 0.4790 1.4311 -0.0570 -0.2216 -0.1133 86  VAL   A CG1 
631   C  CG2 . VAL   A  86  ? 1.7156 0.4468 1.4128 -0.0469 -0.2373 -0.1207 86  VAL   A CG2 
632   N  N   . ASP   A  87  ? 1.7089 0.6109 1.3088 -0.0758 -0.1890 -0.0181 87  ASP   A N   
633   C  CA  . ASP   A  87  ? 1.7511 0.5791 1.3199 -0.0672 -0.1875 -0.0449 87  ASP   A CA  
634   C  C   . ASP   A  87  ? 1.7041 0.6038 1.3330 -0.0591 -0.2201 -0.0445 87  ASP   A C   
635   O  O   . ASP   A  87  ? 1.6899 0.6580 1.2973 0.0375  -0.2573 -0.0314 87  ASP   A O   
636   C  CB  . ASP   A  87  ? 1.7732 0.6418 1.3540 -0.0966 -0.1536 -0.0160 87  ASP   A CB  
637   C  CG  . ASP   A  87  ? 1.8188 0.7599 1.3581 -0.1460 -0.1129 -0.0434 87  ASP   A CG  
638   O  OD1 . ASP   A  87  ? 1.7806 0.8956 1.3445 -0.2594 -0.2153 -0.0741 87  ASP   A OD1 
639   O  OD2 . ASP   A  87  ? 1.8098 0.7249 1.4135 -0.0857 -0.0655 0.0813  87  ASP   A OD2 
640   N  N   . LYS   A  88  ? 1.6123 0.4646 1.3198 -0.0879 -0.2127 -0.1196 88  LYS   A N   
641   C  CA  . LYS   A  88  ? 1.5384 0.4729 1.3097 -0.1037 -0.1814 -0.1300 88  LYS   A CA  
642   C  C   . LYS   A  88  ? 1.5296 0.4068 1.3047 -0.1232 -0.1762 -0.1360 88  LYS   A C   
643   O  O   . LYS   A  88  ? 1.5621 0.4285 1.3403 -0.0571 -0.1210 -0.1729 88  LYS   A O   
644   C  CB  . LYS   A  88  ? 1.5226 0.4818 1.2954 -0.1292 -0.2224 -0.1304 88  LYS   A CB  
645   C  CG  . LYS   A  88  ? 1.5017 0.5757 1.3446 -0.1605 -0.2345 -0.1195 88  LYS   A CG  
646   C  CD  . LYS   A  88  ? 1.4924 0.6223 1.3934 -0.1667 -0.2642 -0.0466 88  LYS   A CD  
647   C  CE  . LYS   A  88  ? 1.4687 0.7210 1.4366 -0.1952 -0.2601 -0.0363 88  LYS   A CE  
648   N  NZ  . LYS   A  88  ? 1.4853 0.8174 1.4845 -0.2233 -0.2884 -0.0400 88  LYS   A NZ  
649   N  N   . SER   A  89  ? 1.5256 0.3476 1.2925 -0.1148 -0.1381 -0.1140 89  SER   A N   
650   C  CA  . SER   A  89  ? 1.5434 0.3877 1.2753 -0.1027 -0.1265 -0.0981 89  SER   A CA  
651   C  C   . SER   A  89  ? 1.5483 0.3712 1.2852 -0.1063 -0.1138 -0.1226 89  SER   A C   
652   O  O   . SER   A  89  ? 1.5458 0.4814 1.2345 -0.1362 -0.1353 -0.1591 89  SER   A O   
653   C  CB  . SER   A  89  ? 1.5277 0.3913 1.2547 -0.1089 -0.1110 -0.0702 89  SER   A CB  
654   O  OG  . SER   A  89  ? 1.5165 0.3690 1.1969 -0.1761 -0.0792 -0.0352 89  SER   A OG  
655   N  N   . ARG   A  90  ? 1.5665 0.3312 1.3250 -0.0772 -0.1044 -0.0622 90  ARG   A N   
656   C  CA  . ARG   A  90  ? 1.5666 0.3502 1.3333 -0.0613 -0.0968 -0.0430 90  ARG   A CA  
657   C  C   . ARG   A  90  ? 1.5245 0.3406 1.3441 -0.0398 -0.0936 -0.0518 90  ARG   A C   
658   O  O   . ARG   A  90  ? 1.5258 0.3020 1.3440 -0.1045 -0.0829 -0.1100 90  ARG   A O   
659   C  CB  . ARG   A  90  ? 1.5766 0.3329 1.3362 -0.0115 -0.1066 -0.0270 90  ARG   A CB  
660   C  CG  . ARG   A  90  ? 1.5797 0.3061 1.3394 0.0018  -0.1411 0.0072  90  ARG   A CG  
661   C  CD  . ARG   A  90  ? 1.6258 0.3039 1.3284 0.0501  -0.1522 0.0653  90  ARG   A CD  
662   N  NE  . ARG   A  90  ? 1.6417 0.2881 1.3131 0.0879  -0.1801 0.0774  90  ARG   A NE  
663   C  CZ  . ARG   A  90  ? 1.7162 0.3348 1.2978 0.1532  -0.1489 0.1136  90  ARG   A CZ  
664   N  NH1 . ARG   A  90  ? 1.7219 0.2766 1.3129 0.1600  -0.1447 0.1443  90  ARG   A NH1 
665   N  NH2 . ARG   A  90  ? 1.7099 0.4164 1.3504 0.1419  -0.1644 0.1471  90  ARG   A NH2 
666   N  N   . LYS   A  91  ? 1.5211 0.3590 1.3443 -0.0535 -0.1263 -0.0440 91  LYS   A N   
667   C  CA  . LYS   A  91  ? 1.5237 0.3447 1.3347 -0.0349 -0.0936 -0.0835 91  LYS   A CA  
668   C  C   . LYS   A  91  ? 1.5517 0.2902 1.3349 -0.0342 -0.1005 -0.1429 91  LYS   A C   
669   O  O   . LYS   A  91  ? 1.5545 0.3240 1.2714 -0.1566 -0.1377 -0.1786 91  LYS   A O   
670   C  CB  . LYS   A  91  ? 1.5091 0.3474 1.3910 -0.0441 -0.1023 -0.0631 91  LYS   A CB  
671   C  CG  . LYS   A  91  ? 1.5227 0.3102 1.4371 -0.0194 -0.1039 -0.1278 91  LYS   A CG  
672   C  CD  . LYS   A  91  ? 1.5269 0.4001 1.4705 -0.0037 -0.1097 -0.1235 91  LYS   A CD  
673   C  CE  . LYS   A  91  ? 1.4853 0.5365 1.5557 -0.0708 -0.0961 -0.1337 91  LYS   A CE  
674   N  NZ  . LYS   A  91  ? 1.4961 0.6762 1.6026 -0.0106 -0.1112 -0.1373 91  LYS   A NZ  
675   N  N   . VAL   A  92  ? 1.5573 0.3673 1.2684 -0.0464 -0.0927 -0.1110 92  VAL   A N   
676   C  CA  . VAL   A  92  ? 1.5205 0.4150 1.2687 -0.0744 -0.1135 -0.1601 92  VAL   A CA  
677   C  C   . VAL   A  92  ? 1.5063 0.3725 1.2825 -0.0763 -0.1239 -0.1615 92  VAL   A C   
678   O  O   . VAL   A  92  ? 1.5019 0.4333 1.2502 -0.0658 -0.0651 -0.1359 92  VAL   A O   
679   C  CB  . VAL   A  92  ? 1.5273 0.4357 1.2499 -0.1285 -0.1430 -0.1179 92  VAL   A CB  
680   C  CG1 . VAL   A  92  ? 1.5330 0.4290 1.2863 -0.1349 -0.1221 -0.0550 92  VAL   A CG1 
681   C  CG2 . VAL   A  92  ? 1.5034 0.4743 1.2492 -0.1511 -0.1436 -0.1081 92  VAL   A CG2 
682   N  N   . ALA   A  93  ? 1.4676 0.3427 1.3136 -0.0636 -0.1178 -0.1578 93  ALA   A N   
683   C  CA  . ALA   A  93  ? 1.4642 0.4640 1.3216 -0.0492 -0.1170 -0.1682 93  ALA   A CA  
684   C  C   . ALA   A  93  ? 1.4464 0.4677 1.3394 -0.0098 -0.0878 -0.1983 93  ALA   A C   
685   O  O   . ALA   A  93  ? 1.4651 0.6281 1.3418 0.0220  -0.0445 -0.1922 93  ALA   A O   
686   C  CB  . ALA   A  93  ? 1.4934 0.4286 1.3468 -0.0650 -0.1374 -0.1498 93  ALA   A CB  
687   N  N   . HIS   A  94  ? 1.4080 0.5342 1.3635 -0.0004 -0.0796 -0.2083 94  HIS   A N   
688   C  CA  . HIS   A  94  ? 1.4145 0.5124 1.4015 0.0373  -0.0970 -0.2497 94  HIS   A CA  
689   C  C   . HIS   A  94  ? 1.4121 0.5480 1.3798 0.0306  -0.0814 -0.2612 94  HIS   A C   
690   O  O   . HIS   A  94  ? 1.4077 0.7612 1.3138 0.0407  -0.0472 -0.3037 94  HIS   A O   
691   C  CB  . HIS   A  94  ? 1.4331 0.4756 1.3912 0.0713  -0.1306 -0.2306 94  HIS   A CB  
692   C  CG  . HIS   A  94  ? 1.4908 0.4623 1.4035 0.0897  -0.1685 -0.2298 94  HIS   A CG  
693   N  ND1 . HIS   A  94  ? 1.5276 0.4622 1.3729 0.0830  -0.2204 -0.1944 94  HIS   A ND1 
694   C  CD2 . HIS   A  94  ? 1.5032 0.5505 1.4238 0.1230  -0.2079 -0.1917 94  HIS   A CD2 
695   C  CE1 . HIS   A  94  ? 1.5510 0.4681 1.3993 0.1152  -0.2260 -0.1886 94  HIS   A CE1 
696   N  NE2 . HIS   A  94  ? 1.5639 0.4773 1.4212 0.1204  -0.2046 -0.2501 94  HIS   A NE2 
697   N  N   . THR   A  95  ? 1.4197 0.4885 1.3436 0.0291  -0.0958 -0.2819 95  THR   A N   
698   C  CA  . THR   A  95  ? 1.4406 0.5344 1.3437 -0.0029 -0.1016 -0.2830 95  THR   A CA  
699   C  C   . THR   A  95  ? 1.4453 0.5633 1.3528 -0.0389 -0.1060 -0.2192 95  THR   A C   
700   O  O   . THR   A  95  ? 1.4289 0.6624 1.3047 -0.0194 -0.1112 -0.2636 95  THR   A O   
701   C  CB  . THR   A  95  ? 1.4053 0.6102 1.3623 -0.0072 -0.1304 -0.3043 95  THR   A CB  
702   O  OG1 . THR   A  95  ? 1.3609 0.7042 1.3645 -0.0714 -0.1408 -0.1368 95  THR   A OG1 
703   C  CG2 . THR   A  95  ? 1.4078 0.6125 1.3913 -0.0042 -0.1058 -0.2842 95  THR   A CG2 
704   N  N   . SER   A  96  ? 1.5162 0.5666 1.3117 -0.0715 -0.1110 -0.2334 96  SER   A N   
705   C  CA  . SER   A  96  ? 1.5500 0.5952 1.3242 -0.0992 -0.1110 -0.2134 96  SER   A CA  
706   C  C   . SER   A  96  ? 1.5536 0.5330 1.3560 -0.0605 -0.1185 -0.1999 96  SER   A C   
707   O  O   . SER   A  96  ? 1.5735 0.5716 1.3779 -0.0817 -0.0633 -0.2124 96  SER   A O   
708   C  CB  . SER   A  96  ? 1.5942 0.5931 1.2870 -0.1225 -0.1269 -0.1935 96  SER   A CB  
709   O  OG  . SER   A  96  ? 1.6380 0.6392 1.2506 -0.1593 -0.1254 -0.1915 96  SER   A OG  
710   N  N   . TYR   A  97  ? 1.5369 0.4593 1.3943 -0.0387 -0.1051 -0.2026 97  TYR   A N   
711   C  CA  . TYR   A  97  ? 1.5452 0.4938 1.3909 -0.0109 -0.1059 -0.2214 97  TYR   A CA  
712   C  C   . TYR   A  97  ? 1.5296 0.5094 1.4189 -0.0413 -0.1214 -0.1896 97  TYR   A C   
713   O  O   . TYR   A  97  ? 1.5583 0.6682 1.3994 -0.0121 -0.1032 -0.2605 97  TYR   A O   
714   C  CB  . TYR   A  97  ? 1.5121 0.4679 1.3642 0.0202  -0.1067 -0.1988 97  TYR   A CB  
715   C  CG  . TYR   A  97  ? 1.5505 0.4770 1.3442 0.0788  -0.0869 -0.1872 97  TYR   A CG  
716   C  CD1 . TYR   A  97  ? 1.5746 0.4764 1.4015 0.1108  -0.0608 -0.1750 97  TYR   A CD1 
717   C  CD2 . TYR   A  97  ? 1.5427 0.5208 1.3243 0.0988  -0.1093 -0.1941 97  TYR   A CD2 
718   C  CE1 . TYR   A  97  ? 1.5725 0.4983 1.4032 0.0894  -0.0602 -0.1603 97  TYR   A CE1 
719   C  CE2 . TYR   A  97  ? 1.5466 0.5191 1.3507 0.0908  -0.1005 -0.1932 97  TYR   A CE2 
720   C  CZ  . TYR   A  97  ? 1.5304 0.4950 1.3781 0.0848  -0.0714 -0.1841 97  TYR   A CZ  
721   O  OH  . TYR   A  97  ? 1.5006 0.4796 1.4098 0.0477  -0.0715 -0.2183 97  TYR   A OH  
722   N  N   . LYS   A  98  ? 1.5528 0.3926 1.4102 -0.0592 -0.1110 -0.2143 98  LYS   A N   
723   C  CA  . LYS   A  98  ? 1.6066 0.3914 1.4370 -0.0431 -0.1103 -0.2054 98  LYS   A CA  
724   C  C   . LYS   A  98  ? 1.5871 0.3444 1.4461 -0.0094 -0.1113 -0.1681 98  LYS   A C   
725   O  O   . LYS   A  98  ? 1.6408 0.1889 1.4565 -0.1009 -0.1205 -0.1611 98  LYS   A O   
726   C  CB  . LYS   A  98  ? 1.6519 0.4077 1.4502 -0.0434 -0.1225 -0.2358 98  LYS   A CB  
727   C  CG  . LYS   A  98  ? 1.6907 0.3934 1.5121 -0.0287 -0.1214 -0.2140 98  LYS   A CG  
728   C  CD  . LYS   A  98  ? 1.7646 0.4216 1.5089 -0.0160 -0.1139 -0.1638 98  LYS   A CD  
729   C  CE  . LYS   A  98  ? 1.7691 0.4455 1.6379 -0.0017 -0.1043 -0.1417 98  LYS   A CE  
730   N  NZ  . LYS   A  98  ? 1.8477 0.5405 1.6916 -0.0243 -0.0810 -0.0881 98  LYS   A NZ  
731   N  N   . ARG   A  99  ? 1.5720 0.3118 1.4183 -0.0055 -0.1382 -0.1517 99  ARG   A N   
732   C  CA  . ARG   A  99  ? 1.5119 0.3681 1.4478 -0.0087 -0.1523 -0.1840 99  ARG   A CA  
733   C  C   . ARG   A  99  ? 1.5343 0.4368 1.4293 0.0314  -0.1406 -0.1640 99  ARG   A C   
734   O  O   . ARG   A  99  ? 1.5732 0.4068 1.4087 0.1063  -0.1426 -0.2637 99  ARG   A O   
735   C  CB  . ARG   A  99  ? 1.5234 0.3796 1.4460 0.0329  -0.1554 -0.1956 99  ARG   A CB  
736   C  CG  . ARG   A  99  ? 1.5064 0.3787 1.4492 0.0481  -0.1367 -0.1978 99  ARG   A CG  
737   C  CD  . ARG   A  99  ? 1.5111 0.3714 1.4622 0.0637  -0.1336 -0.1789 99  ARG   A CD  
738   N  NE  . ARG   A  99  ? 1.5281 0.4276 1.4513 0.0739  -0.1274 -0.1551 99  ARG   A NE  
739   C  CZ  . ARG   A  99  ? 1.5033 0.5472 1.5071 0.1136  -0.1318 -0.1241 99  ARG   A CZ  
740   N  NH1 . ARG   A  99  ? 1.5213 0.5265 1.4910 0.1596  -0.1646 -0.1169 99  ARG   A NH1 
741   N  NH2 . ARG   A  99  ? 1.5135 0.6497 1.5116 0.0958  -0.1077 -0.1488 99  ARG   A NH2 
742   N  N   . ILE   A  100 ? 1.5117 0.3812 1.4157 0.0048  -0.1684 -0.1908 100 ILE   A N   
743   C  CA  . ILE   A  100 ? 1.5260 0.4187 1.4366 0.0035  -0.1626 -0.2464 100 ILE   A CA  
744   C  C   . ILE   A  100 ? 1.5206 0.3986 1.4607 0.0086  -0.1678 -0.2187 100 ILE   A C   
745   O  O   . ILE   A  100 ? 1.5137 0.4608 1.4618 0.0228  -0.1419 -0.2548 100 ILE   A O   
746   C  CB  . ILE   A  100 ? 1.5342 0.4362 1.3576 -0.0213 -0.1764 -0.2597 100 ILE   A CB  
747   C  CG1 . ILE   A  100 ? 1.5376 0.4729 1.3675 -0.0115 -0.1822 -0.2649 100 ILE   A CG1 
748   C  CG2 . ILE   A  100 ? 1.5348 0.5194 1.3617 -0.0363 -0.1652 -0.2721 100 ILE   A CG2 
749   C  CD1 . ILE   A  100 ? 1.5472 0.5198 1.3510 0.0047  -0.1919 -0.2303 100 ILE   A CD1 
750   N  N   . TYR   A  101 ? 1.5842 0.2735 1.4788 0.0060  -0.1603 -0.2242 101 TYR   A N   
751   C  CA  . TYR   A  101 ? 1.6086 0.3551 1.5220 0.0086  -0.1473 -0.2457 101 TYR   A CA  
752   C  C   . TYR   A  101 ? 1.6218 0.3200 1.5533 -0.0181 -0.1721 -0.2415 101 TYR   A C   
753   O  O   . TYR   A  101 ? 1.6215 0.2262 1.5574 -0.0584 -0.1634 -0.2680 101 TYR   A O   
754   C  CB  . TYR   A  101 ? 1.6407 0.3840 1.5164 -0.0053 -0.1645 -0.2179 101 TYR   A CB  
755   C  CG  . TYR   A  101 ? 1.6870 0.5093 1.5087 0.0101  -0.1933 -0.2218 101 TYR   A CG  
756   C  CD1 . TYR   A  101 ? 1.7016 0.4799 1.5339 0.0201  -0.2031 -0.2482 101 TYR   A CD1 
757   C  CD2 . TYR   A  101 ? 1.6950 0.5226 1.4978 0.0297  -0.1972 -0.1700 101 TYR   A CD2 
758   C  CE1 . TYR   A  101 ? 1.7569 0.4976 1.4974 -0.0046 -0.1917 -0.2205 101 TYR   A CE1 
759   C  CE2 . TYR   A  101 ? 1.7544 0.5472 1.4748 0.0035  -0.1930 -0.1345 101 TYR   A CE2 
760   C  CZ  . TYR   A  101 ? 1.7742 0.5167 1.4916 0.0291  -0.1833 -0.1482 101 TYR   A CZ  
761   O  OH  . TYR   A  101 ? 1.8354 0.5991 1.4809 0.0614  -0.1572 -0.1063 101 TYR   A OH  
762   N  N   . GLY   A  102 ? 1.6035 0.4174 1.5662 -0.0222 -0.1598 -0.2587 102 GLY   A N   
763   C  CA  . GLY   A  102 ? 1.5658 0.5600 1.6271 0.0041  -0.1873 -0.2408 102 GLY   A CA  
764   C  C   . GLY   A  102 ? 1.5276 0.5872 1.6707 0.0079  -0.1900 -0.2123 102 GLY   A C   
765   O  O   . GLY   A  102 ? 1.4670 0.6660 1.7747 -0.0161 -0.2266 -0.2221 102 GLY   A O   
766   N  N   . GLU   A  103 ? 1.5590 0.6104 1.6571 0.0457  -0.1580 -0.1728 103 GLU   A N   
767   C  CA  . GLU   A  103 ? 1.5277 0.6544 1.6112 0.0621  -0.1518 -0.1883 103 GLU   A CA  
768   C  C   . GLU   A  103 ? 1.5296 0.6294 1.5540 0.0556  -0.1862 -0.1495 103 GLU   A C   
769   O  O   . GLU   A  103 ? 1.5903 0.6097 1.5069 0.1073  -0.2281 -0.0789 103 GLU   A O   
770   C  CB  . GLU   A  103 ? 1.5560 0.7473 1.6029 0.1066  -0.1295 -0.1695 103 GLU   A CB  
771   C  CG  . GLU   A  103 ? 1.5598 0.7693 1.6223 0.1221  -0.1215 -0.1320 103 GLU   A CG  
772   C  CD  . GLU   A  103 ? 1.5744 0.8665 1.6345 0.1303  -0.0776 -0.0601 103 GLU   A CD  
773   O  OE1 . GLU   A  103 ? 1.6036 0.8933 1.6933 0.1926  -0.0898 -0.0963 103 GLU   A OE1 
774   O  OE2 . GLU   A  103 ? 1.6484 0.7529 1.6205 0.1222  -0.1031 -0.0917 103 GLU   A OE2 
775   N  N   . TYR   A  104 ? 1.5746 0.5104 1.5193 0.0685  -0.0796 -0.1699 104 TYR   A N   
776   C  CA  . TYR   A  104 ? 1.5418 0.5043 1.4593 0.0079  -0.0710 -0.2415 104 TYR   A CA  
777   C  C   . TYR   A  104 ? 1.5007 0.4667 1.4475 0.0176  -0.0559 -0.2692 104 TYR   A C   
778   O  O   . TYR   A  104 ? 1.5570 0.3585 1.4946 0.0297  -0.0132 -0.3295 104 TYR   A O   
779   C  CB  . TYR   A  104 ? 1.5591 0.5108 1.4213 0.0070  -0.0597 -0.2289 104 TYR   A CB  
780   C  CG  . TYR   A  104 ? 1.5718 0.4798 1.4037 0.0143  -0.0441 -0.2554 104 TYR   A CG  
781   C  CD1 . TYR   A  104 ? 1.5861 0.4836 1.3723 0.0272  -0.0493 -0.2775 104 TYR   A CD1 
782   C  CD2 . TYR   A  104 ? 1.5620 0.5198 1.4305 0.0671  -0.0175 -0.2815 104 TYR   A CD2 
783   C  CE1 . TYR   A  104 ? 1.6146 0.5380 1.3518 0.0413  -0.0110 -0.2999 104 TYR   A CE1 
784   C  CE2 . TYR   A  104 ? 1.6046 0.5655 1.4250 0.0813  0.0126  -0.2875 104 TYR   A CE2 
785   C  CZ  . TYR   A  104 ? 1.6090 0.5671 1.4122 0.0753  0.0075  -0.3101 104 TYR   A CZ  
786   O  OH  . TYR   A  104 ? 1.6258 0.5836 1.4392 0.0637  0.0981  -0.3281 104 TYR   A OH  
787   N  N   . PRO   A  105 ? 1.4462 0.5326 1.4637 0.0086  -0.1075 -0.2434 105 PRO   A N   
788   C  CA  . PRO   A  105 ? 1.4411 0.5422 1.4572 -0.0258 -0.0980 -0.2487 105 PRO   A CA  
789   C  C   . PRO   A  105 ? 1.4473 0.5236 1.4865 -0.0260 -0.1024 -0.2532 105 PRO   A C   
790   O  O   . PRO   A  105 ? 1.4052 0.4099 1.5290 -0.0051 -0.1054 -0.2804 105 PRO   A O   
791   C  CB  . PRO   A  105 ? 1.4710 0.4886 1.4452 -0.0140 -0.1039 -0.2657 105 PRO   A CB  
792   C  CG  . PRO   A  105 ? 1.4587 0.4716 1.4394 -0.0130 -0.1082 -0.2677 105 PRO   A CG  
793   C  CD  . PRO   A  105 ? 1.4525 0.5106 1.4415 -0.0068 -0.1093 -0.2282 105 PRO   A CD  
794   N  N   . PRO   A  106 ? 1.4902 0.5765 1.4657 -0.0324 -0.1153 -0.2400 106 PRO   A N   
795   C  CA  . PRO   A  106 ? 1.4957 0.6703 1.4379 -0.0764 -0.1265 -0.1808 106 PRO   A CA  
796   C  C   . PRO   A  106 ? 1.5061 0.7028 1.4516 -0.0237 -0.1595 -0.1522 106 PRO   A C   
797   O  O   . PRO   A  106 ? 1.5280 0.8375 1.3791 -0.0026 -0.2108 -0.0562 106 PRO   A O   
798   C  CB  . PRO   A  106 ? 1.4856 0.6812 1.4576 -0.0639 -0.0955 -0.2148 106 PRO   A CB  
799   C  CG  . PRO   A  106 ? 1.4921 0.6277 1.4802 -0.0684 -0.0896 -0.2293 106 PRO   A CG  
800   C  CD  . PRO   A  106 ? 1.4747 0.6134 1.4614 -0.0593 -0.0998 -0.2386 106 PRO   A CD  
801   N  N   . THR   A  107 ? 1.5536 0.6540 1.5079 -0.0507 -0.1579 -0.1247 107 THR   A N   
802   C  CA  . THR   A  107 ? 1.5617 0.5963 1.5119 -0.0992 -0.1441 -0.1001 107 THR   A CA  
803   C  C   . THR   A  107 ? 1.5421 0.6496 1.4364 -0.0941 -0.1313 -0.1438 107 THR   A C   
804   O  O   . THR   A  107 ? 1.5413 0.7470 1.4887 -0.0980 -0.1252 -0.2121 107 THR   A O   
805   C  CB  . THR   A  107 ? 1.5608 0.5483 1.5306 -0.1215 -0.1461 0.0167  107 THR   A CB  
806   O  OG1 . THR   A  107 ? 1.5528 0.5829 1.5941 -0.1410 -0.1815 0.0453  107 THR   A OG1 
807   C  CG2 . THR   A  107 ? 1.5636 0.5132 1.5533 -0.1562 -0.1353 0.0205  107 THR   A CG2 
808   N  N   . LYS   A  108 ? 1.5682 0.6627 1.4348 -0.1160 -0.1058 -0.1750 108 LYS   A N   
809   C  CA  . LYS   A  108 ? 1.6011 0.6557 1.4498 -0.0648 -0.0674 -0.1586 108 LYS   A CA  
810   C  C   . LYS   A  108 ? 1.5921 0.5933 1.4437 -0.0419 -0.0679 -0.1572 108 LYS   A C   
811   O  O   . LYS   A  108 ? 1.5872 0.4863 1.4320 -0.0874 -0.0665 -0.1683 108 LYS   A O   
812   C  CB  . LYS   A  108 ? 1.6502 0.7761 1.4872 -0.0492 -0.0185 -0.1442 108 LYS   A CB  
813   C  CG  . LYS   A  108 ? 1.7244 0.8020 1.5184 -0.0173 0.0432  -0.1599 108 LYS   A CG  
814   C  CD  . LYS   A  108 ? 1.7889 0.9445 1.5584 0.0083  0.0890  -0.1213 108 LYS   A CD  
815   C  CE  . LYS   A  108 ? 1.8418 0.9971 1.6203 0.0286  0.1225  -0.1793 108 LYS   A CE  
816   N  NZ  . LYS   A  108 ? 1.8675 1.1015 1.6468 0.0297  0.1522  -0.1881 108 LYS   A NZ  
817   N  N   . LEU   A  109 ? 1.5569 0.5969 1.4619 -0.0541 -0.0750 -0.1805 109 LEU   A N   
818   C  CA  . LEU   A  109 ? 1.5265 0.6520 1.4034 -0.0295 -0.1115 -0.1863 109 LEU   A CA  
819   C  C   . LEU   A  109 ? 1.4929 0.5120 1.3993 -0.0100 -0.1285 -0.2126 109 LEU   A C   
820   O  O   . LEU   A  109 ? 1.5094 0.4623 1.3279 0.0002  -0.1588 -0.1920 109 LEU   A O   
821   C  CB  . LEU   A  109 ? 1.5488 0.6688 1.3901 -0.0499 -0.1284 -0.2203 109 LEU   A CB  
822   C  CG  . LEU   A  109 ? 1.6027 0.7573 1.3680 -0.0521 -0.1539 -0.2148 109 LEU   A CG  
823   C  CD1 . LEU   A  109 ? 1.6340 0.7677 1.3932 -0.0168 -0.1550 -0.2254 109 LEU   A CD1 
824   C  CD2 . LEU   A  109 ? 1.6175 0.7901 1.3946 -0.0350 -0.1523 -0.1931 109 LEU   A CD2 
825   N  N   . LEU   A  110 ? 1.5155 0.4333 1.3981 -0.0132 -0.1373 -0.2393 110 LEU   A N   
826   C  CA  . LEU   A  110 ? 1.5097 0.4855 1.3797 -0.0203 -0.1570 -0.2329 110 LEU   A CA  
827   C  C   . LEU   A  110 ? 1.4721 0.5086 1.3848 0.0026  -0.1642 -0.2180 110 LEU   A C   
828   O  O   . LEU   A  110 ? 1.4658 0.6001 1.2933 0.0097  -0.1760 -0.2543 110 LEU   A O   
829   C  CB  . LEU   A  110 ? 1.5163 0.4081 1.4012 0.0057  -0.1640 -0.2283 110 LEU   A CB  
830   C  CG  . LEU   A  110 ? 1.5123 0.4261 1.4045 0.0174  -0.1710 -0.2427 110 LEU   A CG  
831   C  CD1 . LEU   A  110 ? 1.5052 0.4133 1.4234 0.0254  -0.1767 -0.2571 110 LEU   A CD1 
832   C  CD2 . LEU   A  110 ? 1.5010 0.4611 1.4184 0.0107  -0.1889 -0.2719 110 LEU   A CD2 
833   N  N   . VAL   A  111 ? 1.4855 0.5651 1.3920 -0.0229 -0.1774 -0.1563 111 VAL   A N   
834   C  CA  . VAL   A  111 ? 1.4638 0.5771 1.3310 -0.0110 -0.1866 -0.0948 111 VAL   A CA  
835   C  C   . VAL   A  111 ? 1.4560 0.5494 1.3053 -0.0314 -0.1802 -0.1142 111 VAL   A C   
836   O  O   . VAL   A  111 ? 1.4148 0.5773 1.3787 -0.0338 -0.1808 -0.0961 111 VAL   A O   
837   C  CB  . VAL   A  111 ? 1.4713 0.6383 1.3159 -0.0100 -0.1716 -0.0568 111 VAL   A CB  
838   C  CG1 . VAL   A  111 ? 1.4702 0.6450 1.2856 0.0103  -0.1766 -0.0643 111 VAL   A CG1 
839   C  CG2 . VAL   A  111 ? 1.4606 0.6643 1.3491 -0.0276 -0.1807 -0.0576 111 VAL   A CG2 
840   N  N   . SER   A  112 ? 1.4727 0.5402 1.2989 -0.0332 -0.1738 -0.1121 112 SER   A N   
841   C  CA  . SER   A  112 ? 1.5258 0.5773 1.2476 0.0068  -0.1730 -0.1120 112 SER   A CA  
842   C  C   . SER   A  112 ? 1.4892 0.5420 1.2113 0.0535  -0.1835 -0.1489 112 SER   A C   
843   O  O   . SER   A  112 ? 1.5048 0.4661 1.1645 0.0398  -0.1995 -0.1732 112 SER   A O   
844   C  CB  . SER   A  112 ? 1.5669 0.6568 1.2144 0.0049  -0.1538 -0.1036 112 SER   A CB  
845   O  OG  . SER   A  112 ? 1.5697 0.7586 1.2597 0.0210  -0.1740 -0.0276 112 SER   A OG  
846   N  N   . GLU   A  113 ? 1.5184 0.5693 1.2145 0.0578  -0.1687 -0.1317 113 GLU   A N   
847   C  CA  . GLU   A  113 ? 1.5081 0.6456 1.2115 0.0660  -0.1639 -0.1352 113 GLU   A CA  
848   C  C   . GLU   A  113 ? 1.5076 0.6081 1.1669 0.1046  -0.1995 -0.0924 113 GLU   A C   
849   O  O   . GLU   A  113 ? 1.4861 0.6504 1.0913 0.1422  -0.3271 -0.0537 113 GLU   A O   
850   C  CB  . GLU   A  113 ? 1.5440 0.6520 1.2452 0.0714  -0.1303 -0.1286 113 GLU   A CB  
851   C  CG  . GLU   A  113 ? 1.5398 0.7150 1.2698 0.0467  -0.1059 -0.1751 113 GLU   A CG  
852   C  CD  . GLU   A  113 ? 1.5562 0.6759 1.2443 0.0284  -0.0722 -0.2201 113 GLU   A CD  
853   O  OE1 . GLU   A  113 ? 1.5425 0.7658 1.2672 0.0251  -0.0610 -0.1578 113 GLU   A OE1 
854   O  OE2 . GLU   A  113 ? 1.5363 0.6111 1.3347 -0.0099 -0.0384 -0.2452 113 GLU   A OE2 
855   N  N   . VAL   A  114 ? 1.5577 0.6285 1.1853 0.0639  -0.2091 -0.0767 114 VAL   A N   
856   C  CA  . VAL   A  114 ? 1.5853 0.6115 1.2351 0.0788  -0.1947 -0.0851 114 VAL   A CA  
857   C  C   . VAL   A  114 ? 1.5913 0.5768 1.2384 0.0740  -0.1418 -0.0831 114 VAL   A C   
858   O  O   . VAL   A  114 ? 1.6470 0.5958 1.2557 0.0720  -0.0779 -0.1318 114 VAL   A O   
859   C  CB  . VAL   A  114 ? 1.6045 0.6340 1.2836 0.0586  -0.2075 -0.1301 114 VAL   A CB  
860   C  CG1 . VAL   A  114 ? 1.6014 0.6525 1.3045 0.0861  -0.2142 -0.1389 114 VAL   A CG1 
861   C  CG2 . VAL   A  114 ? 1.5693 0.6439 1.3337 0.0602  -0.2291 -0.1453 114 VAL   A CG2 
862   N  N   . ALA   A  115 ? 1.5859 0.5761 1.2601 0.0403  -0.1557 -0.0616 115 ALA   A N   
863   C  CA  . ALA   A  115 ? 1.5493 0.5705 1.2223 -0.0168 -0.1817 -0.0576 115 ALA   A CA  
864   C  C   . ALA   A  115 ? 1.5698 0.5669 1.2150 -0.0111 -0.2198 -0.0195 115 ALA   A C   
865   O  O   . ALA   A  115 ? 1.5528 0.5208 1.2018 -0.0519 -0.2592 -0.0141 115 ALA   A O   
866   C  CB  . ALA   A  115 ? 1.5568 0.5301 1.1956 -0.0190 -0.1914 -0.0420 115 ALA   A CB  
867   N  N   . LYS   A  116 ? 1.5778 0.5608 1.2650 -0.0433 -0.1963 0.0032  116 LYS   A N   
868   C  CA  . LYS   A  116 ? 1.5804 0.5545 1.2911 -0.0732 -0.1805 0.0357  116 LYS   A CA  
869   C  C   . LYS   A  116 ? 1.6276 0.4055 1.2759 -0.0476 -0.1700 0.0192  116 LYS   A C   
870   O  O   . LYS   A  116 ? 1.6450 0.2164 1.2759 -0.0599 -0.1435 0.0181  116 LYS   A O   
871   C  CB  . LYS   A  116 ? 1.6071 0.5741 1.3066 -0.0917 -0.1717 0.0194  116 LYS   A CB  
872   C  CG  . LYS   A  116 ? 1.6014 0.7162 1.3369 -0.1192 -0.1890 0.0519  116 LYS   A CG  
873   C  CD  . LYS   A  116 ? 1.5907 0.7279 1.4100 -0.1945 -0.2027 0.0279  116 LYS   A CD  
874   C  CE  . LYS   A  116 ? 1.6258 0.8951 1.4244 -0.1844 -0.2498 0.0479  116 LYS   A CE  
875   N  NZ  . LYS   A  116 ? 1.6065 1.0143 1.4920 -0.1822 -0.2352 0.0822  116 LYS   A NZ  
876   N  N   . ILE   A  117 ? 1.6236 0.4392 1.2624 -0.0194 -0.2037 -0.0195 117 ILE   A N   
877   C  CA  . ILE   A  117 ? 1.6172 0.4971 1.2338 -0.0022 -0.2308 -0.0128 117 ILE   A CA  
878   C  C   . ILE   A  117 ? 1.5996 0.4931 1.2267 0.0121  -0.2904 0.0077  117 ILE   A C   
879   O  O   . ILE   A  117 ? 1.5958 0.5157 1.1483 0.1077  -0.3805 0.0129  117 ILE   A O   
880   C  CB  . ILE   A  117 ? 1.6040 0.5264 1.2261 -0.0028 -0.2210 -0.0041 117 ILE   A CB  
881   C  CG1 . ILE   A  117 ? 1.5833 0.5259 1.2571 0.0230  -0.2087 0.0166  117 ILE   A CG1 
882   C  CG2 . ILE   A  117 ? 1.6231 0.5143 1.2084 -0.0056 -0.2288 -0.0062 117 ILE   A CG2 
883   C  CD1 . ILE   A  117 ? 1.5565 0.5556 1.2907 0.0511  -0.2039 0.0244  117 ILE   A CD1 
884   N  N   . MET   A  118 ? 1.6013 0.4713 1.2469 0.0135  -0.3012 0.0224  118 MET   A N   
885   C  CA  . MET   A  118 ? 1.6022 0.4560 1.2709 0.0209  -0.2683 0.0562  118 MET   A CA  
886   C  C   . MET   A  118 ? 1.5699 0.3911 1.2362 -0.0030 -0.2538 0.0289  118 MET   A C   
887   O  O   . MET   A  118 ? 1.4888 0.4828 1.2638 0.0790  -0.2906 0.1995  118 MET   A O   
888   C  CB  . MET   A  118 ? 1.6073 0.4722 1.3059 0.0098  -0.2688 0.0713  118 MET   A CB  
889   C  CG  . MET   A  118 ? 1.6318 0.4968 1.2985 0.0005  -0.2758 0.0571  118 MET   A CG  
890   S  SD  . MET   A  118 ? 1.6631 0.5434 1.3364 -0.0712 -0.2268 0.0492  118 MET   A SD  
891   C  CE  . MET   A  118 ? 1.7364 0.5502 1.2697 0.0001  -0.2332 0.0671  118 MET   A CE  
892   N  N   . GLN   A  119 ? 1.5418 0.3048 1.2702 -0.0400 -0.2379 -0.0145 119 GLN   A N   
893   C  CA  . GLN   A  119 ? 1.5533 0.3474 1.2579 -0.0282 -0.2274 -0.0136 119 GLN   A CA  
894   C  C   . GLN   A  119 ? 1.5599 0.3855 1.2920 -0.0276 -0.2112 -0.0599 119 GLN   A C   
895   O  O   . GLN   A  119 ? 1.5462 0.3547 1.3505 -0.0032 -0.1865 -0.1269 119 GLN   A O   
896   C  CB  . GLN   A  119 ? 1.5390 0.3913 1.2577 -0.0562 -0.1968 -0.0046 119 GLN   A CB  
897   C  CG  . GLN   A  119 ? 1.5795 0.4285 1.2337 -0.0714 -0.1820 0.0029  119 GLN   A CG  
898   C  CD  . GLN   A  119 ? 1.5740 0.4758 1.2359 -0.0818 -0.1661 0.0193  119 GLN   A CD  
899   O  OE1 . GLN   A  119 ? 1.6329 0.5380 1.2466 -0.1160 -0.0975 0.0778  119 GLN   A OE1 
900   N  NE2 . GLN   A  119 ? 1.5746 0.4585 1.2500 -0.0888 -0.1709 0.0191  119 GLN   A NE2 
901   N  N   . GLU   A  120 ? 1.5934 0.4659 1.2405 -0.0416 -0.2121 0.0176  120 GLU   A N   
902   C  CA  . GLU   A  120 ? 1.6110 0.5137 1.2332 -0.0738 -0.2418 -0.0038 120 GLU   A CA  
903   C  C   . GLU   A  120 ? 1.6339 0.4515 1.1860 -0.0824 -0.2688 0.0108  120 GLU   A C   
904   O  O   . GLU   A  120 ? 1.6611 0.2675 1.1181 -0.0650 -0.2888 0.0068  120 GLU   A O   
905   C  CB  . GLU   A  120 ? 1.6579 0.5063 1.3437 -0.0605 -0.2485 -0.0060 120 GLU   A CB  
906   C  CG  . GLU   A  120 ? 1.7516 0.6262 1.3950 -0.0375 -0.1861 -0.0348 120 GLU   A CG  
907   C  CD  . GLU   A  120 ? 1.9126 0.6247 1.5651 -0.0664 -0.1592 -0.0531 120 GLU   A CD  
908   O  OE1 . GLU   A  120 ? 2.0670 0.6240 1.6927 -0.1547 -0.1916 -0.2313 120 GLU   A OE1 
909   O  OE2 . GLU   A  120 ? 2.0463 0.7783 1.6901 -0.1755 -0.0981 0.0555  120 GLU   A OE2 
910   N  N   . ALA   A  121 ? 1.6776 0.4378 1.2101 -0.1326 -0.2809 0.0132  121 ALA   A N   
911   C  CA  . ALA   A  121 ? 1.6696 0.4730 1.2289 -0.1690 -0.2892 -0.0312 121 ALA   A CA  
912   C  C   . ALA   A  121 ? 1.6814 0.4985 1.2314 -0.1592 -0.3269 -0.0232 121 ALA   A C   
913   O  O   . ALA   A  121 ? 1.6762 0.7345 1.2208 -0.2205 -0.3031 -0.1889 121 ALA   A O   
914   C  CB  . ALA   A  121 ? 1.6705 0.4597 1.2460 -0.1778 -0.2996 -0.0046 121 ALA   A CB  
915   N  N   . THR   A  122 ? 1.6707 0.4915 1.2583 -0.1356 -0.3048 -0.0071 122 THR   A N   
916   C  CA  . THR   A  122 ? 1.6602 0.4029 1.3694 -0.1200 -0.3089 -0.0411 122 THR   A CA  
917   C  C   . THR   A  122 ? 1.6674 0.4320 1.3725 -0.0637 -0.3176 0.0359  122 THR   A C   
918   O  O   . THR   A  122 ? 1.6959 0.3812 1.4680 -0.0588 -0.3755 -0.0569 122 THR   A O   
919   C  CB  . THR   A  122 ? 1.6950 0.2344 1.3874 -0.0908 -0.2780 0.0315  122 THR   A CB  
920   O  OG1 . THR   A  122 ? 1.7363 0.1648 1.3869 -0.0561 -0.3012 0.0496  122 THR   A OG1 
921   C  CG2 . THR   A  122 ? 1.6862 0.3317 1.3295 -0.0761 -0.2829 0.0257  122 THR   A CG2 
922   N  N   . GLN   A  123 ? 1.5804 0.5632 1.3272 -0.1229 -0.3021 -0.0477 123 GLN   A N   
923   C  CA  . GLN   A  123 ? 1.5278 0.6491 1.2904 -0.0947 -0.2625 -0.0331 123 GLN   A CA  
924   C  C   . GLN   A  123 ? 1.4665 0.7104 1.3013 -0.0723 -0.2512 -0.0738 123 GLN   A C   
925   O  O   . GLN   A  123 ? 1.4839 0.7692 1.3293 0.0165  -0.2155 -0.0253 123 GLN   A O   
926   C  CB  . GLN   A  123 ? 1.5191 0.6713 1.3015 -0.1253 -0.2181 -0.0274 123 GLN   A CB  
927   C  CG  . GLN   A  123 ? 1.5001 0.6732 1.2776 -0.1277 -0.1930 -0.0243 123 GLN   A CG  
928   C  CD  . GLN   A  123 ? 1.5049 0.7101 1.2858 -0.1534 -0.1734 -0.0251 123 GLN   A CD  
929   O  OE1 . GLN   A  123 ? 1.4853 0.8103 1.3143 -0.1396 -0.1276 -0.0237 123 GLN   A OE1 
930   N  NE2 . GLN   A  123 ? 1.4637 0.7269 1.2809 -0.1666 -0.1741 -0.0363 123 GLN   A NE2 
931   N  N   . SER   A  124 ? 1.4340 0.6110 1.3037 -0.0988 -0.2326 -0.1213 124 SER   A N   
932   C  CA  . SER   A  124 ? 1.4522 0.5662 1.3604 -0.1216 -0.2559 -0.1410 124 SER   A CA  
933   C  C   . SER   A  124 ? 1.4249 0.6106 1.2894 -0.1294 -0.2644 -0.0987 124 SER   A C   
934   O  O   . SER   A  124 ? 1.4519 0.6695 1.2644 -0.1001 -0.3386 -0.1630 124 SER   A O   
935   C  CB  . SER   A  124 ? 1.4242 0.4943 1.4482 -0.1229 -0.2230 -0.1467 124 SER   A CB  
936   O  OG  . SER   A  124 ? 1.4517 0.5904 1.6304 -0.1479 -0.1381 -0.1825 124 SER   A OG  
937   N  N   . GLY   A  125 ? 1.5029 0.4749 1.2502 -0.1666 -0.2835 -0.0986 125 GLY   A N   
938   C  CA  . GLY   A  125 ? 1.5451 0.3839 1.2554 -0.1357 -0.2871 -0.1027 125 GLY   A CA  
939   C  C   . GLY   A  125 ? 1.6017 0.3960 1.2591 -0.1049 -0.2701 -0.1193 125 GLY   A C   
940   O  O   . GLY   A  125 ? 1.6149 0.4507 1.2859 -0.0242 -0.3054 -0.1541 125 GLY   A O   
941   N  N   . GLY   A  126 ? 1.6535 0.3265 1.3265 -0.0517 -0.2835 -0.0278 126 GLY   A N   
942   C  CA  . GLY   A  126 ? 1.6470 0.3020 1.3383 -0.0388 -0.3054 -0.0621 126 GLY   A CA  
943   C  C   . GLY   A  126 ? 1.6141 0.2404 1.3827 -0.0528 -0.3083 -0.0824 126 GLY   A C   
944   O  O   . GLY   A  126 ? 1.6191 0.2225 1.3748 0.0285  -0.3818 -0.0696 126 GLY   A O   
945   N  N   . VAL   A  127 ? 1.6145 0.2403 1.3684 -0.0640 -0.3044 -0.0801 127 VAL   A N   
946   C  CA  . VAL   A  127 ? 1.5931 0.2928 1.3757 0.0001  -0.2874 -0.0765 127 VAL   A CA  
947   C  C   . VAL   A  127 ? 1.5903 0.3455 1.4126 -0.0588 -0.3093 -0.1151 127 VAL   A C   
948   O  O   . VAL   A  127 ? 1.6029 0.3244 1.4253 -0.0397 -0.2848 -0.1285 127 VAL   A O   
949   C  CB  . VAL   A  127 ? 1.6075 0.2592 1.3705 -0.0155 -0.2658 -0.0793 127 VAL   A CB  
950   C  CG1 . VAL   A  127 ? 1.5678 0.3462 1.3755 -0.0217 -0.2097 -0.0466 127 VAL   A CG1 
951   C  CG2 . VAL   A  127 ? 1.6138 0.2124 1.3530 -0.0070 -0.2690 -0.0159 127 VAL   A CG2 
952   N  N   . ARG   A  128 ? 1.5987 0.2925 1.3305 -0.0310 -0.2909 -0.0806 128 ARG   A N   
953   C  CA  . ARG   A  128 ? 1.5819 0.3049 1.2422 -0.0270 -0.2745 -0.0773 128 ARG   A CA  
954   C  C   . ARG   A  128 ? 1.5807 0.3427 1.1293 -0.0403 -0.2495 -0.1050 128 ARG   A C   
955   O  O   . ARG   A  128 ? 1.5561 0.3671 1.0163 -0.0168 -0.2359 -0.1018 128 ARG   A O   
956   C  CB  . ARG   A  128 ? 1.5850 0.3238 1.2469 -0.0088 -0.2801 -0.0817 128 ARG   A CB  
957   C  CG  . ARG   A  128 ? 1.5842 0.3053 1.2768 -0.0126 -0.2763 -0.0599 128 ARG   A CG  
958   C  CD  . ARG   A  128 ? 1.5995 0.3564 1.2784 -0.0078 -0.2797 -0.0821 128 ARG   A CD  
959   N  NE  . ARG   A  128 ? 1.6408 0.3704 1.2762 -0.0279 -0.2648 -0.0700 128 ARG   A NE  
960   C  CZ  . ARG   A  128 ? 1.6343 0.4237 1.3185 -0.0138 -0.2523 -0.0921 128 ARG   A CZ  
961   N  NH1 . ARG   A  128 ? 1.6317 0.4124 1.3035 -0.0006 -0.2564 -0.0714 128 ARG   A NH1 
962   N  NH2 . ARG   A  128 ? 1.6444 0.4268 1.3107 -0.0012 -0.2483 -0.1055 128 ARG   A NH2 
963   N  N   . PRO   A  129 ? 1.5894 0.3928 1.1355 -0.0422 -0.2298 -0.0984 129 PRO   A N   
964   C  CA  . PRO   A  129 ? 1.5729 0.4045 1.1825 -0.0556 -0.2496 -0.0656 129 PRO   A CA  
965   C  C   . PRO   A  129 ? 1.5641 0.4042 1.2028 -0.0577 -0.2522 -0.0412 129 PRO   A C   
966   O  O   . PRO   A  129 ? 1.5378 0.3827 1.3092 0.0310  -0.2099 -0.0584 129 PRO   A O   
967   C  CB  . PRO   A  129 ? 1.5860 0.4464 1.1819 -0.0667 -0.2347 -0.0579 129 PRO   A CB  
968   C  CG  . PRO   A  129 ? 1.5988 0.4793 1.2008 -0.0383 -0.2292 -0.0652 129 PRO   A CG  
969   C  CD  . PRO   A  129 ? 1.6126 0.4382 1.1702 -0.0326 -0.2291 -0.0561 129 PRO   A CD  
970   N  N   . PHE   A  130 ? 1.5579 0.3796 1.3315 -0.0789 -0.2630 -0.0154 130 PHE   A N   
971   C  CA  . PHE   A  130 ? 1.6100 0.3724 1.3095 -0.0898 -0.2690 -0.0160 130 PHE   A CA  
972   C  C   . PHE   A  130 ? 1.6806 0.3034 1.2496 -0.0581 -0.2325 -0.0216 130 PHE   A C   
973   O  O   . PHE   A  130 ? 1.7195 0.1266 1.2996 -0.1350 -0.1836 -0.1094 130 PHE   A O   
974   C  CB  . PHE   A  130 ? 1.5973 0.4248 1.3321 -0.0702 -0.2977 -0.0522 130 PHE   A CB  
975   C  CG  . PHE   A  130 ? 1.6175 0.4348 1.2966 -0.0845 -0.3170 -0.0643 130 PHE   A CG  
976   C  CD1 . PHE   A  130 ? 1.6102 0.4778 1.2870 -0.0513 -0.2894 -0.0612 130 PHE   A CD1 
977   C  CD2 . PHE   A  130 ? 1.6597 0.5202 1.2801 -0.0726 -0.3452 -0.0610 130 PHE   A CD2 
978   C  CE1 . PHE   A  130 ? 1.6195 0.4671 1.2572 -0.0386 -0.2846 -0.0648 130 PHE   A CE1 
979   C  CE2 . PHE   A  130 ? 1.6537 0.5039 1.2905 -0.0535 -0.3438 -0.0405 130 PHE   A CE2 
980   C  CZ  . PHE   A  130 ? 1.6276 0.4979 1.2712 -0.0404 -0.3220 -0.0624 130 PHE   A CZ  
981   N  N   . GLY   A  131 ? 1.6902 0.2439 1.2070 -0.0517 -0.2334 0.0470  131 GLY   A N   
982   C  CA  . GLY   A  131 ? 1.6500 0.3000 1.1631 -0.0752 -0.2784 0.0575  131 GLY   A CA  
983   C  C   . GLY   A  131 ? 1.6611 0.3349 1.1326 -0.0336 -0.2820 0.0831  131 GLY   A C   
984   O  O   . GLY   A  131 ? 1.6408 0.2859 1.1396 -0.0124 -0.2928 0.0960  131 GLY   A O   
985   N  N   . VAL   A  132 ? 1.7012 0.3308 1.0623 -0.0758 -0.3141 0.0184  132 VAL   A N   
986   C  CA  . VAL   A  132 ? 1.6931 0.4201 1.0795 -0.1086 -0.3259 -0.0526 132 VAL   A CA  
987   C  C   . VAL   A  132 ? 1.6852 0.4244 1.1274 -0.1347 -0.2974 -0.0868 132 VAL   A C   
988   O  O   . VAL   A  132 ? 1.6738 0.4333 1.1690 -0.1345 -0.3511 -0.0479 132 VAL   A O   
989   C  CB  . VAL   A  132 ? 1.7169 0.4218 1.0378 -0.1293 -0.3374 -0.0592 132 VAL   A CB  
990   C  CG1 . VAL   A  132 ? 1.7365 0.4288 1.0385 -0.1067 -0.3354 -0.0236 132 VAL   A CG1 
991   C  CG2 . VAL   A  132 ? 1.6976 0.4871 1.0414 -0.1510 -0.3481 -0.0689 132 VAL   A CG2 
992   N  N   . SER   A  133 ? 1.6963 0.4713 1.1694 -0.1552 -0.3313 -0.1479 133 SER   A N   
993   C  CA  . SER   A  133 ? 1.6742 0.5566 1.2210 -0.1586 -0.3296 -0.1607 133 SER   A CA  
994   C  C   . SER   A  133 ? 1.6599 0.6270 1.2417 -0.1658 -0.3733 -0.1400 133 SER   A C   
995   O  O   . SER   A  133 ? 1.6988 0.6852 1.2235 -0.1648 -0.3823 -0.1011 133 SER   A O   
996   C  CB  . SER   A  133 ? 1.6954 0.5689 1.2340 -0.1730 -0.3359 -0.1581 133 SER   A CB  
997   O  OG  . SER   A  133 ? 1.7127 0.6596 1.1995 -0.1716 -0.3261 -0.1396 133 SER   A OG  
998   N  N   . LEU   A  134 ? 1.6484 0.6316 1.3183 -0.1424 -0.3140 -0.1444 134 LEU   A N   
999   C  CA  . LEU   A  134 ? 1.5823 0.6643 1.3229 -0.1428 -0.2626 -0.1123 134 LEU   A CA  
1000  C  C   . LEU   A  134 ? 1.5804 0.5955 1.3472 -0.1567 -0.2582 -0.0790 134 LEU   A C   
1001  O  O   . LEU   A  134 ? 1.4798 0.5142 1.4050 -0.1746 -0.2260 -0.0301 134 LEU   A O   
1002  C  CB  . LEU   A  134 ? 1.5963 0.7115 1.3234 -0.1900 -0.2511 -0.1196 134 LEU   A CB  
1003  C  CG  . LEU   A  134 ? 1.6061 0.8112 1.2416 -0.1844 -0.2319 -0.1256 134 LEU   A CG  
1004  C  CD1 . LEU   A  134 ? 1.5697 0.8362 1.2442 -0.2017 -0.2315 -0.1390 134 LEU   A CD1 
1005  C  CD2 . LEU   A  134 ? 1.6167 0.8432 1.2347 -0.1611 -0.2262 -0.1539 134 LEU   A CD2 
1006  N  N   . LEU   A  135 ? 1.6044 0.5987 1.3149 -0.1621 -0.2630 -0.0772 135 LEU   A N   
1007  C  CA  . LEU   A  135 ? 1.6251 0.6163 1.3199 -0.1458 -0.2447 -0.0428 135 LEU   A CA  
1008  C  C   . LEU   A  135 ? 1.6255 0.6395 1.2980 -0.0935 -0.2518 -0.0293 135 LEU   A C   
1009  O  O   . LEU   A  135 ? 1.6570 0.7071 1.3054 -0.0492 -0.2384 -0.0047 135 LEU   A O   
1010  C  CB  . LEU   A  135 ? 1.6688 0.6143 1.3069 -0.1615 -0.2481 -0.0440 135 LEU   A CB  
1011  C  CG  . LEU   A  135 ? 1.7057 0.6131 1.3323 -0.1904 -0.2201 -0.0281 135 LEU   A CG  
1012  C  CD1 . LEU   A  135 ? 1.7127 0.5992 1.3530 -0.2282 -0.2186 0.0036  135 LEU   A CD1 
1013  C  CD2 . LEU   A  135 ? 1.7023 0.6163 1.3231 -0.2052 -0.2176 -0.0484 135 LEU   A CD2 
1014  N  N   . ILE   A  136 ? 1.5979 0.6032 1.3366 -0.0832 -0.2397 -0.0424 136 ILE   A N   
1015  C  CA  . ILE   A  136 ? 1.5601 0.5947 1.3344 -0.0896 -0.2060 -0.0670 136 ILE   A CA  
1016  C  C   . ILE   A  136 ? 1.5711 0.5049 1.3120 -0.1060 -0.1885 -0.1153 136 ILE   A C   
1017  O  O   . ILE   A  136 ? 1.5670 0.4249 1.2841 -0.1002 -0.1843 -0.1867 136 ILE   A O   
1018  C  CB  . ILE   A  136 ? 1.5677 0.5707 1.3635 -0.0846 -0.2249 -0.0473 136 ILE   A CB  
1019  C  CG1 . ILE   A  136 ? 1.5878 0.5802 1.3832 -0.0614 -0.2188 -0.0266 136 ILE   A CG1 
1020  C  CG2 . ILE   A  136 ? 1.5583 0.5860 1.3869 -0.0590 -0.1946 -0.0286 136 ILE   A CG2 
1021  C  CD1 . ILE   A  136 ? 1.6088 0.5680 1.3910 -0.0771 -0.2264 -0.0280 136 ILE   A CD1 
1022  N  N   . ALA   A  137 ? 1.5521 0.4898 1.3132 -0.1135 -0.1700 -0.1001 137 ALA   A N   
1023  C  CA  . ALA   A  137 ? 1.5541 0.5552 1.3537 -0.1185 -0.1333 -0.0678 137 ALA   A CA  
1024  C  C   . ALA   A  137 ? 1.5324 0.5536 1.3737 -0.0972 -0.1107 -0.0129 137 ALA   A C   
1025  O  O   . ALA   A  137 ? 1.4986 0.5976 1.4118 -0.0864 -0.0883 -0.0052 137 ALA   A O   
1026  C  CB  . ALA   A  137 ? 1.5713 0.5431 1.3757 -0.1349 -0.1406 -0.0712 137 ALA   A CB  
1027  N  N   . GLY   A  138 ? 1.5247 0.6158 1.3712 -0.0943 -0.0853 0.0133  138 GLY   A N   
1028  C  CA  . GLY   A  138 ? 1.5451 0.6298 1.4084 -0.0968 -0.1020 -0.0382 138 GLY   A CA  
1029  C  C   . GLY   A  138 ? 1.5308 0.7117 1.4374 -0.1242 -0.0708 -0.0019 138 GLY   A C   
1030  O  O   . GLY   A  138 ? 1.6137 0.6236 1.4668 -0.1332 -0.1172 0.0135  138 GLY   A O   
1031  N  N   . HIS   A  139 ? 1.5172 0.7374 1.4874 -0.0646 -0.0794 -0.0269 139 HIS   A N   
1032  C  CA  . HIS   A  139 ? 1.5153 0.7812 1.5208 -0.0509 -0.0491 -0.0090 139 HIS   A CA  
1033  C  C   . HIS   A  139 ? 1.4597 0.8264 1.5199 -0.0654 -0.0622 -0.0080 139 HIS   A C   
1034  O  O   . HIS   A  139 ? 1.3678 0.9273 1.5223 -0.0213 -0.0510 -0.0167 139 HIS   A O   
1035  C  CB  . HIS   A  139 ? 1.5243 0.7501 1.5280 -0.0294 -0.0415 -0.0122 139 HIS   A CB  
1036  C  CG  . HIS   A  139 ? 1.5543 0.7189 1.5727 -0.0280 -0.0098 -0.0037 139 HIS   A CG  
1037  N  ND1 . HIS   A  139 ? 1.5447 0.7156 1.6146 0.0103  0.0075  -0.0253 139 HIS   A ND1 
1038  C  CD2 . HIS   A  139 ? 1.5585 0.7106 1.5752 -0.0014 0.0058  0.0107  139 HIS   A CD2 
1039  C  CE1 . HIS   A  139 ? 1.5340 0.7020 1.6329 0.0062  0.0171  -0.0068 139 HIS   A CE1 
1040  N  NE2 . HIS   A  139 ? 1.5480 0.7064 1.6153 0.0083  0.0094  0.0170  139 HIS   A NE2 
1041  N  N   . ASP   A  140 ? 1.4718 0.8768 1.5019 -0.0875 -0.0486 0.0321  140 ASP   A N   
1042  C  CA  . ASP   A  140 ? 1.5039 0.8905 1.5341 -0.0914 -0.0330 0.0114  140 ASP   A CA  
1043  C  C   . ASP   A  140 ? 1.4837 0.8735 1.5486 -0.1104 -0.0267 0.0235  140 ASP   A C   
1044  O  O   . ASP   A  140 ? 1.4904 0.7551 1.5077 -0.0413 -0.0272 0.0210  140 ASP   A O   
1045  C  CB  . ASP   A  140 ? 1.4999 0.9960 1.5408 -0.1218 -0.0251 0.0287  140 ASP   A CB  
1046  C  CG  . ASP   A  140 ? 1.5684 1.1137 1.5021 -0.1708 -0.0169 0.0705  140 ASP   A CG  
1047  O  OD1 . ASP   A  140 ? 1.6093 1.2401 1.4964 -0.1864 -0.0193 0.0462  140 ASP   A OD1 
1048  O  OD2 . ASP   A  140 ? 1.5285 1.1429 1.5642 -0.1964 0.0465  0.0501  140 ASP   A OD2 
1049  N  N   . GLU   A  141 ? 1.5566 0.9399 1.6036 -0.0819 -0.0378 -0.1040 141 GLU   A N   
1050  C  CA  . GLU   A  141 ? 1.5597 0.9549 1.6580 -0.0921 -0.0464 -0.1608 141 GLU   A CA  
1051  C  C   . GLU   A  141 ? 1.4983 0.8611 1.6577 -0.1333 -0.0940 -0.1723 141 GLU   A C   
1052  O  O   . GLU   A  141 ? 1.5203 0.8161 1.6602 -0.2391 -0.1055 -0.1793 141 GLU   A O   
1053  C  CB  . GLU   A  141 ? 1.6199 0.9563 1.7508 -0.0819 -0.0804 -0.1555 141 GLU   A CB  
1054  C  CG  . GLU   A  141 ? 1.6273 1.0286 1.8078 -0.0412 -0.1057 -0.1571 141 GLU   A CG  
1055  C  CD  . GLU   A  141 ? 1.6863 1.0577 1.8118 -0.0415 -0.1204 -0.2175 141 GLU   A CD  
1056  O  OE1 . GLU   A  141 ? 1.6342 1.2811 1.8185 0.0170  -0.1441 -0.2342 141 GLU   A OE1 
1057  O  OE2 . GLU   A  141 ? 1.7423 1.1097 1.7921 -0.0592 -0.0767 -0.2289 141 GLU   A OE2 
1058  N  N   . PHE   A  142 ? 1.4906 0.8083 1.6731 -0.0998 -0.0901 -0.1882 142 PHE   A N   
1059  C  CA  . PHE   A  142 ? 1.4292 0.8713 1.6809 -0.0936 -0.1190 -0.1638 142 PHE   A CA  
1060  C  C   . PHE   A  142 ? 1.3518 0.8737 1.6280 -0.1375 -0.1678 -0.1396 142 PHE   A C   
1061  O  O   . PHE   A  142 ? 1.2480 0.9177 1.6252 -0.1892 -0.2105 -0.1261 142 PHE   A O   
1062  C  CB  . PHE   A  142 ? 1.3922 0.9104 1.7340 -0.0918 -0.1260 -0.1690 142 PHE   A CB  
1063  C  CG  . PHE   A  142 ? 1.4337 0.9264 1.8004 -0.0798 -0.0851 -0.2069 142 PHE   A CG  
1064  C  CD1 . PHE   A  142 ? 1.4515 0.9506 1.8174 -0.0573 -0.0545 -0.2037 142 PHE   A CD1 
1065  C  CD2 . PHE   A  142 ? 1.4611 0.9292 1.8076 -0.0898 -0.0606 -0.2118 142 PHE   A CD2 
1066  C  CE1 . PHE   A  142 ? 1.5006 0.9781 1.8668 0.0102  -0.0534 -0.2590 142 PHE   A CE1 
1067  C  CE2 . PHE   A  142 ? 1.4882 0.9666 1.8531 -0.0206 -0.0394 -0.2716 142 PHE   A CE2 
1068  C  CZ  . PHE   A  142 ? 1.5129 1.0356 1.8544 -0.0084 -0.0382 -0.2458 142 PHE   A CZ  
1069  N  N   . ASN   A  143 ? 1.3680 0.8468 1.5975 -0.1475 -0.1928 -0.1268 143 ASN   A N   
1070  C  CA  . ASN   A  143 ? 1.4544 0.8455 1.5804 -0.1306 -0.1860 -0.0817 143 ASN   A CA  
1071  C  C   . ASN   A  143 ? 1.4481 0.7387 1.5778 -0.1166 -0.1505 -0.1019 143 ASN   A C   
1072  O  O   . ASN   A  143 ? 1.4528 0.7314 1.5898 -0.0909 -0.1468 -0.0655 143 ASN   A O   
1073  C  CB  . ASN   A  143 ? 1.4596 0.7897 1.5785 -0.1367 -0.2031 -0.0470 143 ASN   A CB  
1074  C  CG  . ASN   A  143 ? 1.5287 0.7986 1.6000 -0.1690 -0.2377 -0.0282 143 ASN   A CG  
1075  O  OD1 . ASN   A  143 ? 1.5772 0.7075 1.6869 -0.2413 -0.2819 0.0067  143 ASN   A OD1 
1076  N  ND2 . ASN   A  143 ? 1.5454 0.8261 1.6186 -0.1699 -0.1932 0.0391  143 ASN   A ND2 
1077  N  N   . GLY   A  144 ? 1.4792 0.8059 1.5126 -0.0882 -0.1552 -0.1324 144 GLY   A N   
1078  C  CA  . GLY   A  144 ? 1.5205 0.7457 1.5031 -0.0813 -0.1454 -0.1566 144 GLY   A CA  
1079  C  C   . GLY   A  144 ? 1.5828 0.6642 1.4875 -0.0761 -0.1726 -0.1623 144 GLY   A C   
1080  O  O   . GLY   A  144 ? 1.5869 0.5253 1.4656 -0.1016 -0.2354 -0.2343 144 GLY   A O   
1081  N  N   . PHE   A  145 ? 1.6217 0.6316 1.4730 -0.0827 -0.1430 -0.1490 145 PHE   A N   
1082  C  CA  . PHE   A  145 ? 1.6340 0.5612 1.4627 -0.1237 -0.1410 -0.1469 145 PHE   A CA  
1083  C  C   . PHE   A  145 ? 1.6867 0.4701 1.4386 -0.1396 -0.0755 -0.1328 145 PHE   A C   
1084  O  O   . PHE   A  145 ? 1.7052 0.3112 1.4573 -0.1234 -0.0350 -0.1656 145 PHE   A O   
1085  C  CB  . PHE   A  145 ? 1.6333 0.5786 1.5039 -0.1798 -0.1155 -0.1778 145 PHE   A CB  
1086  C  CG  . PHE   A  145 ? 1.6089 0.6601 1.4785 -0.1875 -0.1432 -0.1749 145 PHE   A CG  
1087  C  CD1 . PHE   A  145 ? 1.6201 0.7337 1.4585 -0.1921 -0.1350 -0.1915 145 PHE   A CD1 
1088  C  CD2 . PHE   A  145 ? 1.5897 0.7545 1.4941 -0.2384 -0.1014 -0.1815 145 PHE   A CD2 
1089  C  CE1 . PHE   A  145 ? 1.6307 0.7580 1.4673 -0.1910 -0.1396 -0.1788 145 PHE   A CE1 
1090  C  CE2 . PHE   A  145 ? 1.6096 0.7776 1.5014 -0.2326 -0.1163 -0.1774 145 PHE   A CE2 
1091  C  CZ  . PHE   A  145 ? 1.6318 0.7652 1.4894 -0.2085 -0.1167 -0.1797 145 PHE   A CZ  
1092  N  N   . SER   A  146 ? 1.6850 0.4896 1.4462 -0.1428 -0.0713 -0.1124 146 SER   A N   
1093  C  CA  . SER   A  146 ? 1.6791 0.5249 1.4569 -0.1551 -0.0909 -0.0896 146 SER   A CA  
1094  C  C   . SER   A  146 ? 1.6721 0.5549 1.4178 -0.1610 -0.0932 -0.0729 146 SER   A C   
1095  O  O   . SER   A  146 ? 1.6354 0.5687 1.4173 -0.1030 -0.1095 -0.0468 146 SER   A O   
1096  C  CB  . SER   A  146 ? 1.6979 0.5165 1.4845 -0.1734 -0.0697 -0.1439 146 SER   A CB  
1097  O  OG  . SER   A  146 ? 1.6417 0.5449 1.5087 -0.2258 -0.0661 -0.2129 146 SER   A OG  
1098  N  N   . LEU   A  147 ? 1.6764 0.5603 1.4233 -0.1408 -0.1287 -0.1107 147 LEU   A N   
1099  C  CA  . LEU   A  147 ? 1.6681 0.5713 1.3628 -0.1331 -0.1413 -0.0763 147 LEU   A CA  
1100  C  C   . LEU   A  147 ? 1.6637 0.5685 1.3629 -0.1723 -0.1493 -0.0276 147 LEU   A C   
1101  O  O   . LEU   A  147 ? 1.7008 0.4852 1.4177 -0.2125 -0.2076 0.0251  147 LEU   A O   
1102  C  CB  . LEU   A  147 ? 1.7074 0.5188 1.3381 -0.1250 -0.1268 -0.0790 147 LEU   A CB  
1103  C  CG  . LEU   A  147 ? 1.7364 0.4404 1.3200 -0.1423 -0.1512 -0.0632 147 LEU   A CG  
1104  C  CD1 . LEU   A  147 ? 1.7335 0.4053 1.3032 -0.1256 -0.1420 -0.0959 147 LEU   A CD1 
1105  C  CD2 . LEU   A  147 ? 1.7280 0.4497 1.3254 -0.1497 -0.1463 -0.0393 147 LEU   A CD2 
1106  N  N   . TYR   A  148 ? 1.6243 0.5748 1.3420 -0.1483 -0.1873 -0.0311 148 TYR   A N   
1107  C  CA  . TYR   A  148 ? 1.6246 0.5565 1.3186 -0.1212 -0.1643 -0.0357 148 TYR   A CA  
1108  C  C   . TYR   A  148 ? 1.6253 0.4868 1.2940 -0.1345 -0.2025 -0.0446 148 TYR   A C   
1109  O  O   . TYR   A  148 ? 1.6484 0.3455 1.2763 -0.1072 -0.2008 -0.0945 148 TYR   A O   
1110  C  CB  . TYR   A  148 ? 1.6180 0.5980 1.3124 -0.1285 -0.1709 -0.0508 148 TYR   A CB  
1111  C  CG  . TYR   A  148 ? 1.6426 0.7011 1.2615 -0.1221 -0.1722 -0.0329 148 TYR   A CG  
1112  C  CD1 . TYR   A  148 ? 1.6385 0.7506 1.2941 -0.0994 -0.1536 -0.0534 148 TYR   A CD1 
1113  C  CD2 . TYR   A  148 ? 1.6217 0.7112 1.2704 -0.1184 -0.2021 -0.0394 148 TYR   A CD2 
1114  C  CE1 . TYR   A  148 ? 1.6511 0.7836 1.2751 -0.1164 -0.1772 -0.0867 148 TYR   A CE1 
1115  C  CE2 . TYR   A  148 ? 1.6323 0.7333 1.2738 -0.1229 -0.2130 -0.0670 148 TYR   A CE2 
1116  C  CZ  . TYR   A  148 ? 1.6269 0.7735 1.2401 -0.0883 -0.1641 -0.1402 148 TYR   A CZ  
1117  O  OH  . TYR   A  148 ? 1.6487 0.9754 1.2876 -0.0277 -0.0900 -0.1514 148 TYR   A OH  
1118  N  N   . GLN   A  149 ? 1.6073 0.5139 1.3210 -0.1389 -0.2271 -0.0302 149 GLN   A N   
1119  C  CA  . GLN   A  149 ? 1.5893 0.5511 1.3620 -0.0987 -0.2616 -0.0228 149 GLN   A CA  
1120  C  C   . GLN   A  149 ? 1.5914 0.5278 1.4083 -0.1403 -0.2586 -0.0178 149 GLN   A C   
1121  O  O   . GLN   A  149 ? 1.5905 0.5413 1.4112 -0.1623 -0.2462 -0.0079 149 GLN   A O   
1122  C  CB  . GLN   A  149 ? 1.6030 0.5557 1.4026 -0.0843 -0.2886 0.0205  149 GLN   A CB  
1123  C  CG  . GLN   A  149 ? 1.6029 0.5741 1.4259 -0.0440 -0.3322 0.0202  149 GLN   A CG  
1124  C  CD  . GLN   A  149 ? 1.5940 0.5366 1.4504 0.0131  -0.3889 0.0149  149 GLN   A CD  
1125  O  OE1 . GLN   A  149 ? 1.5839 0.5161 1.4407 0.0366  -0.4053 0.0539  149 GLN   A OE1 
1126  N  NE2 . GLN   A  149 ? 1.5967 0.5265 1.4551 0.0132  -0.4033 0.0139  149 GLN   A NE2 
1127  N  N   . VAL   A  150 ? 1.5949 0.5440 1.4193 -0.1476 -0.2516 -0.0286 150 VAL   A N   
1128  C  CA  . VAL   A  150 ? 1.5901 0.5221 1.4065 -0.1123 -0.2510 -0.0476 150 VAL   A CA  
1129  C  C   . VAL   A  150 ? 1.6415 0.4541 1.3129 -0.1583 -0.2684 -0.0904 150 VAL   A C   
1130  O  O   . VAL   A  150 ? 1.6611 0.3316 1.3145 -0.0993 -0.2482 -0.1343 150 VAL   A O   
1131  C  CB  . VAL   A  150 ? 1.5762 0.5122 1.4509 -0.1044 -0.2558 -0.0524 150 VAL   A CB  
1132  C  CG1 . VAL   A  150 ? 1.5863 0.5218 1.4371 -0.0828 -0.2708 -0.0544 150 VAL   A CG1 
1133  C  CG2 . VAL   A  150 ? 1.5871 0.5451 1.4738 -0.0913 -0.2317 -0.0781 150 VAL   A CG2 
1134  N  N   . ASP   A  151 ? 1.6321 0.4368 1.3242 -0.1928 -0.2772 -0.0796 151 ASP   A N   
1135  C  CA  . ASP   A  151 ? 1.6187 0.4658 1.3320 -0.1874 -0.2664 -0.0725 151 ASP   A CA  
1136  C  C   . ASP   A  151 ? 1.6186 0.3820 1.3114 -0.1837 -0.2634 -0.0693 151 ASP   A C   
1137  O  O   . ASP   A  151 ? 1.5835 0.3396 1.4117 -0.2645 -0.2243 -0.0387 151 ASP   A O   
1138  C  CB  . ASP   A  151 ? 1.6673 0.5285 1.3536 -0.2181 -0.2742 -0.0322 151 ASP   A CB  
1139  C  CG  . ASP   A  151 ? 1.7225 0.5266 1.4365 -0.2689 -0.2656 -0.0077 151 ASP   A CG  
1140  O  OD1 . ASP   A  151 ? 1.7958 0.6278 1.4370 -0.2420 -0.2734 -0.0003 151 ASP   A OD1 
1141  O  OD2 . ASP   A  151 ? 1.7973 0.5856 1.4923 -0.2487 -0.3118 0.0816  151 ASP   A OD2 
1142  N  N   . PRO   A  152 ? 1.6172 0.4126 1.2819 -0.1361 -0.2853 -0.0476 152 PRO   A N   
1143  C  CA  . PRO   A  152 ? 1.6167 0.3975 1.2795 -0.1364 -0.2833 -0.0499 152 PRO   A CA  
1144  C  C   . PRO   A  152 ? 1.6487 0.4470 1.2711 -0.0845 -0.2884 -0.0521 152 PRO   A C   
1145  O  O   . PRO   A  152 ? 1.5847 0.4758 1.3736 -0.0427 -0.3416 -0.1354 152 PRO   A O   
1146  C  CB  . PRO   A  152 ? 1.6349 0.4064 1.2659 -0.1211 -0.2893 -0.0445 152 PRO   A CB  
1147  C  CG  . PRO   A  152 ? 1.6432 0.4688 1.2866 -0.1211 -0.3072 -0.0420 152 PRO   A CG  
1148  C  CD  . PRO   A  152 ? 1.6537 0.4435 1.2907 -0.1267 -0.3022 -0.0687 152 PRO   A CD  
1149  N  N   . SER   A  153 ? 1.6157 0.5212 1.2897 -0.1140 -0.2769 -0.0379 153 SER   A N   
1150  C  CA  . SER   A  153 ? 1.5793 0.6154 1.2798 -0.0979 -0.2716 -0.0197 153 SER   A CA  
1151  C  C   . SER   A  153 ? 1.5618 0.6173 1.2698 -0.0785 -0.2493 -0.0075 153 SER   A C   
1152  O  O   . SER   A  153 ? 1.5838 0.6414 1.3236 -0.1253 -0.2328 -0.0480 153 SER   A O   
1153  C  CB  . SER   A  153 ? 1.5248 0.6846 1.2667 -0.0792 -0.2698 0.0029  153 SER   A CB  
1154  O  OG  . SER   A  153 ? 1.5183 0.7709 1.2560 -0.0765 -0.2375 0.0082  153 SER   A OG  
1155  N  N   . GLY   A  154 ? 1.5617 0.6057 1.2266 -0.0799 -0.2347 0.0094  154 GLY   A N   
1156  C  CA  . GLY   A  154 ? 1.5676 0.5979 1.2699 -0.0813 -0.2312 0.0081  154 GLY   A CA  
1157  C  C   . GLY   A  154 ? 1.5860 0.6030 1.3174 -0.0954 -0.2111 0.0462  154 GLY   A C   
1158  O  O   . GLY   A  154 ? 1.6244 0.6035 1.4093 -0.0973 -0.1929 0.0267  154 GLY   A O   
1159  N  N   . SER   A  155 ? 1.6181 0.5964 1.3322 -0.0943 -0.2061 0.0489  155 SER   A N   
1160  C  CA  . SER   A  155 ? 1.6182 0.5857 1.3613 -0.1015 -0.1970 0.0468  155 SER   A CA  
1161  C  C   . SER   A  155 ? 1.6036 0.4739 1.3506 -0.0785 -0.1684 0.0445  155 SER   A C   
1162  O  O   . SER   A  155 ? 1.5970 0.4024 1.3604 -0.0948 -0.1994 0.0421  155 SER   A O   
1163  C  CB  . SER   A  155 ? 1.6305 0.5932 1.4204 -0.1214 -0.1897 0.0559  155 SER   A CB  
1164  O  OG  . SER   A  155 ? 1.6577 0.6539 1.4507 -0.0908 -0.2108 0.0620  155 SER   A OG  
1165  N  N   . TYR   A  156 ? 1.6323 0.5130 1.3574 -0.0675 -0.1436 0.0265  156 TYR   A N   
1166  C  CA  . TYR   A  156 ? 1.6060 0.5470 1.3702 -0.0849 -0.1332 0.0005  156 TYR   A CA  
1167  C  C   . TYR   A  156 ? 1.6568 0.4556 1.3949 -0.1473 -0.1283 0.0205  156 TYR   A C   
1168  O  O   . TYR   A  156 ? 1.6616 0.4500 1.3821 -0.1973 -0.0790 0.1649  156 TYR   A O   
1169  C  CB  . TYR   A  156 ? 1.5993 0.5477 1.3711 -0.0603 -0.1428 -0.0002 156 TYR   A CB  
1170  C  CG  . TYR   A  156 ? 1.5620 0.5725 1.3489 -0.0313 -0.1481 -0.0092 156 TYR   A CG  
1171  C  CD1 . TYR   A  156 ? 1.5601 0.6139 1.3173 -0.0120 -0.1555 -0.0298 156 TYR   A CD1 
1172  C  CD2 . TYR   A  156 ? 1.5510 0.6328 1.3459 -0.0265 -0.1578 -0.0349 156 TYR   A CD2 
1173  C  CE1 . TYR   A  156 ? 1.5677 0.6915 1.3192 0.0096  -0.1393 -0.0625 156 TYR   A CE1 
1174  C  CE2 . TYR   A  156 ? 1.5650 0.7451 1.3033 -0.0184 -0.1400 -0.0568 156 TYR   A CE2 
1175  C  CZ  . TYR   A  156 ? 1.5694 0.7207 1.3052 -0.0082 -0.1327 -0.0931 156 TYR   A CZ  
1176  O  OH  . TYR   A  156 ? 1.6263 0.6598 1.3797 0.0080  -0.0521 -0.1426 156 TYR   A OH  
1177  N  N   . PHE   A  157 ? 1.6846 0.3870 1.4014 -0.1554 -0.1286 -0.0180 157 PHE   A N   
1178  C  CA  . PHE   A  157 ? 1.6753 0.5939 1.4208 -0.1257 -0.0996 -0.0179 157 PHE   A CA  
1179  C  C   . PHE   A  157 ? 1.6847 0.5274 1.4310 -0.1024 -0.1020 -0.0754 157 PHE   A C   
1180  O  O   . PHE   A  157 ? 1.7551 0.5077 1.4356 -0.1036 -0.1108 -0.0929 157 PHE   A O   
1181  C  CB  . PHE   A  157 ? 1.7175 0.5938 1.4897 -0.0969 -0.1092 0.0179  157 PHE   A CB  
1182  C  CG  . PHE   A  157 ? 1.7027 0.6661 1.5276 -0.0826 -0.1116 0.0659  157 PHE   A CG  
1183  C  CD1 . PHE   A  157 ? 1.6839 0.5832 1.5097 -0.0845 -0.1443 0.0601  157 PHE   A CD1 
1184  C  CD2 . PHE   A  157 ? 1.7009 0.6808 1.5499 -0.1009 -0.1114 0.1129  157 PHE   A CD2 
1185  C  CE1 . PHE   A  157 ? 1.7144 0.4492 1.4970 -0.1025 -0.1164 0.0222  157 PHE   A CE1 
1186  C  CE2 . PHE   A  157 ? 1.7174 0.5881 1.5429 -0.1189 -0.1000 0.0952  157 PHE   A CE2 
1187  C  CZ  . PHE   A  157 ? 1.7144 0.4731 1.5460 -0.1087 -0.1350 0.0470  157 PHE   A CZ  
1188  N  N   . PRO   A  158 ? 1.6922 0.6212 1.3772 -0.1309 -0.0965 -0.1193 158 PRO   A N   
1189  C  CA  . PRO   A  158 ? 1.6549 0.7102 1.3848 -0.1557 -0.0921 -0.1121 158 PRO   A CA  
1190  C  C   . PRO   A  158 ? 1.6458 0.7157 1.3789 -0.1748 -0.0844 -0.0709 158 PRO   A C   
1191  O  O   . PRO   A  158 ? 1.6612 0.6961 1.3478 -0.2392 -0.0530 -0.1045 158 PRO   A O   
1192  C  CB  . PRO   A  158 ? 1.6596 0.8003 1.3891 -0.1434 -0.0681 -0.1227 158 PRO   A CB  
1193  C  CG  . PRO   A  158 ? 1.6601 0.7983 1.4193 -0.1306 -0.0786 -0.1046 158 PRO   A CG  
1194  C  CD  . PRO   A  158 ? 1.6880 0.6961 1.3771 -0.1307 -0.1031 -0.1129 158 PRO   A CD  
1195  N  N   . TRP   A  159 ? 1.6200 0.7678 1.4160 -0.1597 -0.1065 -0.0388 159 TRP   A N   
1196  C  CA  . TRP   A  159 ? 1.6354 0.7680 1.4434 -0.1853 -0.1231 -0.0041 159 TRP   A CA  
1197  C  C   . TRP   A  159 ? 1.6078 0.8731 1.4868 -0.1744 -0.0991 -0.0428 159 TRP   A C   
1198  O  O   . TRP   A  159 ? 1.5932 0.8771 1.4938 -0.2423 -0.1060 -0.0362 159 TRP   A O   
1199  C  CB  . TRP   A  159 ? 1.6235 0.7522 1.3939 -0.2042 -0.1669 0.0027  159 TRP   A CB  
1200  C  CG  . TRP   A  159 ? 1.6193 0.7510 1.4076 -0.2316 -0.2225 0.0313  159 TRP   A CG  
1201  C  CD1 . TRP   A  159 ? 1.6230 0.7753 1.4336 -0.2381 -0.2215 0.0425  159 TRP   A CD1 
1202  C  CD2 . TRP   A  159 ? 1.6242 0.7370 1.4591 -0.2674 -0.2530 0.0152  159 TRP   A CD2 
1203  N  NE1 . TRP   A  159 ? 1.6384 0.7471 1.4757 -0.2469 -0.2061 0.0400  159 TRP   A NE1 
1204  C  CE2 . TRP   A  159 ? 1.6461 0.7031 1.4924 -0.2344 -0.2416 0.0308  159 TRP   A CE2 
1205  C  CE3 . TRP   A  159 ? 1.6486 0.7048 1.5299 -0.2687 -0.2686 0.0433  159 TRP   A CE3 
1206  C  CZ2 . TRP   A  159 ? 1.6476 0.6774 1.5595 -0.2518 -0.2480 0.0219  159 TRP   A CZ2 
1207  C  CZ3 . TRP   A  159 ? 1.6493 0.7224 1.6213 -0.2686 -0.2545 0.0842  159 TRP   A CZ3 
1208  C  CH2 . TRP   A  159 ? 1.6445 0.7362 1.6257 -0.2675 -0.2504 0.0627  159 TRP   A CH2 
1209  N  N   . LYS   A  160 ? 1.6614 0.7849 1.5189 -0.1616 -0.0832 -0.0207 160 LYS   A N   
1210  C  CA  . LYS   A  160 ? 1.6807 0.7749 1.5183 -0.1944 -0.0958 -0.0006 160 LYS   A CA  
1211  C  C   . LYS   A  160 ? 1.7157 0.6464 1.5606 -0.1610 -0.0729 -0.0734 160 LYS   A C   
1212  O  O   . LYS   A  160 ? 1.8301 0.8503 1.5680 -0.1013 -0.1234 -0.0490 160 LYS   A O   
1213  C  CB  . LYS   A  160 ? 1.7831 0.7109 1.5742 -0.2414 -0.0905 0.0158  160 LYS   A CB  
1214  C  CG  . LYS   A  160 ? 1.7940 0.8134 1.5505 -0.2830 -0.0554 0.0595  160 LYS   A CG  
1215  C  CD  . LYS   A  160 ? 1.8524 0.8462 1.5820 -0.2815 -0.0593 0.1009  160 LYS   A CD  
1216  C  CE  . LYS   A  160 ? 1.8887 0.9627 1.5754 -0.2688 -0.0384 0.1202  160 LYS   A CE  
1217  N  NZ  . LYS   A  160 ? 1.9353 1.0302 1.6108 -0.2613 -0.0178 0.1729  160 LYS   A NZ  
1218  N  N   . ALA   A  161 ? 1.6424 0.5359 1.5226 -0.2145 -0.1221 0.0079  161 ALA   A N   
1219  C  CA  . ALA   A  161 ? 1.6247 0.6068 1.5036 -0.2303 -0.1355 0.0089  161 ALA   A CA  
1220  C  C   . ALA   A  161 ? 1.5605 0.6792 1.4989 -0.2364 -0.1337 -0.0630 161 ALA   A C   
1221  O  O   . ALA   A  161 ? 1.5744 0.8677 1.4776 -0.2526 -0.1480 -0.0196 161 ALA   A O   
1222  C  CB  . ALA   A  161 ? 1.6285 0.6114 1.4832 -0.2205 -0.1436 0.0132  161 ALA   A CB  
1223  N  N   . THR   A  162 ? 1.5824 0.5638 1.4111 -0.2655 -0.1686 -0.0537 162 THR   A N   
1224  C  CA  . THR   A  162 ? 1.6056 0.5375 1.4364 -0.2654 -0.1611 -0.0713 162 THR   A CA  
1225  C  C   . THR   A  162 ? 1.6117 0.4594 1.4360 -0.2471 -0.1601 -0.0081 162 THR   A C   
1226  O  O   . THR   A  162 ? 1.6061 0.4114 1.5174 -0.3157 -0.1522 0.0319  162 THR   A O   
1227  C  CB  . THR   A  162 ? 1.5643 0.5054 1.4435 -0.2395 -0.1360 -0.1037 162 THR   A CB  
1228  O  OG1 . THR   A  162 ? 1.6189 0.3971 1.4241 -0.2753 -0.1313 -0.2192 162 THR   A OG1 
1229  C  CG2 . THR   A  162 ? 1.5690 0.5268 1.4299 -0.2297 -0.1102 -0.0566 162 THR   A CG2 
1230  N  N   . ALA   A  163 ? 1.6535 0.4263 1.4377 -0.2291 -0.1832 0.0251  163 ALA   A N   
1231  C  CA  . ALA   A  163 ? 1.6772 0.3812 1.4183 -0.2103 -0.1894 0.0356  163 ALA   A CA  
1232  C  C   . ALA   A  163 ? 1.7014 0.3134 1.3673 -0.1878 -0.2013 0.0593  163 ALA   A C   
1233  O  O   . ALA   A  163 ? 1.7536 0.3139 1.4048 -0.1696 -0.1882 0.1165  163 ALA   A O   
1234  C  CB  . ALA   A  163 ? 1.7176 0.4124 1.4474 -0.2299 -0.1997 0.0218  163 ALA   A CB  
1235  N  N   . ILE   A  164 ? 1.7259 0.3269 1.3266 -0.1530 -0.1988 0.0343  164 ILE   A N   
1236  C  CA  . ILE   A  164 ? 1.7491 0.3996 1.3474 -0.1142 -0.2215 0.0490  164 ILE   A CA  
1237  C  C   . ILE   A  164 ? 1.7675 0.4132 1.3526 -0.0834 -0.2247 0.0576  164 ILE   A C   
1238  O  O   . ILE   A  164 ? 1.8337 0.4611 1.3646 -0.1293 -0.2422 0.1043  164 ILE   A O   
1239  C  CB  . ILE   A  164 ? 1.7015 0.4443 1.3136 -0.1055 -0.2218 0.0166  164 ILE   A CB  
1240  C  CG1 . ILE   A  164 ? 1.6843 0.4651 1.2823 -0.0955 -0.2100 0.0204  164 ILE   A CG1 
1241  C  CG2 . ILE   A  164 ? 1.7069 0.5065 1.3083 -0.0769 -0.2132 0.0523  164 ILE   A CG2 
1242  C  CD1 . ILE   A  164 ? 1.6676 0.4611 1.2721 -0.0895 -0.1962 0.0371  164 ILE   A CD1 
1243  N  N   . GLY   A  165 ? 1.7771 0.4551 1.3562 -0.0552 -0.2286 0.0638  165 GLY   A N   
1244  C  CA  . GLY   A  165 ? 1.7910 0.4821 1.3462 -0.0490 -0.2353 0.0510  165 GLY   A CA  
1245  C  C   . GLY   A  165 ? 1.8422 0.4892 1.3741 -0.0831 -0.2228 0.0643  165 GLY   A C   
1246  O  O   . GLY   A  165 ? 1.8654 0.3371 1.4578 -0.1697 -0.2080 0.0104  165 GLY   A O   
1247  N  N   . LYS   A  166 ? 1.8706 0.5152 1.4075 -0.0562 -0.2225 -0.0002 166 LYS   A N   
1248  C  CA  . LYS   A  166 ? 1.9104 0.5232 1.5349 -0.0587 -0.2140 -0.0465 166 LYS   A CA  
1249  C  C   . LYS   A  166 ? 1.8726 0.5760 1.5263 -0.0728 -0.1993 -0.1343 166 LYS   A C   
1250  O  O   . LYS   A  166 ? 1.9179 0.6342 1.5060 -0.0715 -0.2778 -0.1480 166 LYS   A O   
1251  C  CB  . LYS   A  166 ? 1.9200 0.5811 1.5251 -0.1008 -0.1645 -0.0787 166 LYS   A CB  
1252  C  CG  . LYS   A  166 ? 1.9599 0.6952 1.6491 -0.0332 -0.0504 -0.0848 166 LYS   A CG  
1253  C  CD  . LYS   A  166 ? 2.0156 0.8853 1.6593 0.0040  0.0204  -0.0703 166 LYS   A CD  
1254  C  CE  . LYS   A  166 ? 2.1123 0.9405 1.7657 0.0458  0.0531  -0.1140 166 LYS   A CE  
1255  N  NZ  . LYS   A  166 ? 2.1242 0.9975 1.8410 0.0900  0.0542  -0.0800 166 LYS   A NZ  
1256  N  N   . GLY   A  167 ? 1.9200 0.5303 1.5361 0.0419  -0.1841 -0.1453 167 GLY   A N   
1257  C  CA  . GLY   A  167 ? 1.9154 0.5823 1.6201 0.0288  -0.1801 -0.1286 167 GLY   A CA  
1258  C  C   . GLY   A  167 ? 1.8741 0.6190 1.6201 0.0440  -0.1529 -0.0826 167 GLY   A C   
1259  O  O   . GLY   A  167 ? 1.8627 0.6209 1.6967 0.0056  -0.1451 -0.0544 167 GLY   A O   
1260  N  N   . SER   A  168 ? 1.8843 0.7070 1.6312 0.0039  -0.1889 -0.0258 168 SER   A N   
1261  C  CA  . SER   A  168 ? 1.8523 0.6511 1.6445 -0.0630 -0.1522 -0.0130 168 SER   A CA  
1262  C  C   . SER   A  168 ? 1.8464 0.6954 1.7241 -0.1353 -0.1511 -0.0115 168 SER   A C   
1263  O  O   . SER   A  168 ? 1.8182 0.6356 1.7220 -0.1435 -0.1628 0.0440  168 SER   A O   
1264  C  CB  . SER   A  168 ? 1.8582 0.6420 1.6939 -0.0754 -0.1569 -0.0178 168 SER   A CB  
1265  O  OG  . SER   A  168 ? 1.8604 0.7079 1.7222 -0.0484 -0.1607 -0.0036 168 SER   A OG  
1266  N  N   . VAL   A  169 ? 1.8176 0.6172 1.7400 -0.2424 -0.1122 0.0020  169 VAL   A N   
1267  C  CA  . VAL   A  169 ? 1.8397 0.5521 1.7804 -0.2331 -0.1244 0.0144  169 VAL   A CA  
1268  C  C   . VAL   A  169 ? 1.8604 0.5228 1.7816 -0.3025 -0.1124 0.0440  169 VAL   A C   
1269  O  O   . VAL   A  169 ? 1.9404 0.4613 1.7675 -0.3779 -0.0683 0.0469  169 VAL   A O   
1270  C  CB  . VAL   A  169 ? 1.7796 0.6093 1.7839 -0.2017 -0.1409 0.0230  169 VAL   A CB  
1271  C  CG1 . VAL   A  169 ? 1.7751 0.7195 1.7719 -0.1918 -0.1248 0.0482  169 VAL   A CG1 
1272  C  CG2 . VAL   A  169 ? 1.7812 0.5504 1.7598 -0.2086 -0.1472 0.0078  169 VAL   A CG2 
1273  N  N   . ALA   A  170 ? 1.8972 0.5375 1.7785 -0.3006 -0.1236 0.0524  170 ALA   A N   
1274  C  CA  . ALA   A  170 ? 1.8899 0.6121 1.7724 -0.2555 -0.1386 0.0908  170 ALA   A CA  
1275  C  C   . ALA   A  170 ? 1.8301 0.6032 1.7427 -0.2777 -0.1557 0.1362  170 ALA   A C   
1276  O  O   . ALA   A  170 ? 1.8020 0.6500 1.7908 -0.2437 -0.1860 0.1719  170 ALA   A O   
1277  C  CB  . ALA   A  170 ? 1.9449 0.6648 1.7647 -0.2360 -0.1348 0.0888  170 ALA   A CB  
1278  N  N   . ALA   A  171 ? 1.8195 0.5622 1.6817 -0.2237 -0.1730 0.1579  171 ALA   A N   
1279  C  CA  . ALA   A  171 ? 1.7839 0.5875 1.6417 -0.2030 -0.1705 0.1544  171 ALA   A CA  
1280  C  C   . ALA   A  171 ? 1.7327 0.5540 1.6762 -0.2003 -0.1424 0.1564  171 ALA   A C   
1281  O  O   . ALA   A  171 ? 1.7026 0.5001 1.6476 -0.2450 -0.1468 0.2370  171 ALA   A O   
1282  C  CB  . ALA   A  171 ? 1.7640 0.5555 1.5637 -0.1866 -0.1856 0.1294  171 ALA   A CB  
1283  N  N   . LYS   A  172 ? 1.6894 0.5777 1.7582 -0.1676 -0.1750 0.1373  172 LYS   A N   
1284  C  CA  . LYS   A  172 ? 1.6877 0.6766 1.7946 -0.1339 -0.1728 0.0955  172 LYS   A CA  
1285  C  C   . LYS   A  172 ? 1.6976 0.7506 1.8893 -0.1719 -0.1920 0.1042  172 LYS   A C   
1286  O  O   . LYS   A  172 ? 1.7904 0.8448 1.9704 -0.1604 -0.1226 0.0394  172 LYS   A O   
1287  C  CB  . LYS   A  172 ? 1.6576 0.6523 1.8430 -0.1140 -0.1718 0.0867  172 LYS   A CB  
1288  C  CG  . LYS   A  172 ? 1.6110 0.6674 1.8334 -0.0961 -0.1614 0.0649  172 LYS   A CG  
1289  C  CD  . LYS   A  172 ? 1.5382 0.6957 1.8668 -0.1075 -0.1608 0.0419  172 LYS   A CD  
1290  C  CE  . LYS   A  172 ? 1.5440 0.7026 1.9090 -0.0943 -0.1835 0.0293  172 LYS   A CE  
1291  N  NZ  . LYS   A  172 ? 1.5614 0.7040 1.9107 -0.1108 -0.1795 -0.0182 172 LYS   A NZ  
1292  N  N   . THR   A  173 ? 1.7274 0.7675 1.8710 -0.1233 -0.2549 0.0573  173 THR   A N   
1293  C  CA  . THR   A  173 ? 1.7558 0.8642 1.8809 -0.1757 -0.2607 0.0571  173 THR   A CA  
1294  C  C   . THR   A  173 ? 1.8108 0.8582 1.8789 -0.1897 -0.3168 0.0329  173 THR   A C   
1295  O  O   . THR   A  173 ? 1.8728 1.0391 1.9110 -0.2413 -0.2560 0.0571  173 THR   A O   
1296  C  CB  . THR   A  173 ? 1.7405 0.8767 1.8606 -0.1454 -0.2708 0.0703  173 THR   A CB  
1297  O  OG1 . THR   A  173 ? 1.7675 0.9874 1.8419 -0.1153 -0.2825 0.1090  173 THR   A OG1 
1298  C  CG2 . THR   A  173 ? 1.7510 0.8608 1.8789 -0.1665 -0.2889 0.0703  173 THR   A CG2 
1299  N  N   . PHE   A  174 ? 1.8970 0.7486 1.8538 -0.2164 -0.3663 -0.0140 174 PHE   A N   
1300  C  CA  . PHE   A  174 ? 1.9263 0.7195 1.8819 -0.2177 -0.3873 -0.0056 174 PHE   A CA  
1301  C  C   . PHE   A  174 ? 1.8718 0.7806 1.8841 -0.2303 -0.3787 -0.0597 174 PHE   A C   
1302  O  O   . PHE   A  174 ? 1.8958 0.9954 2.0178 -0.1838 -0.3334 -0.0986 174 PHE   A O   
1303  C  CB  . PHE   A  174 ? 1.9823 0.5873 1.8694 -0.2329 -0.4194 0.0457  174 PHE   A CB  
1304  C  CG  . PHE   A  174 ? 2.0379 0.6137 1.8451 -0.2766 -0.4401 0.1147  174 PHE   A CG  
1305  C  CD1 . PHE   A  174 ? 2.0224 0.6086 1.8163 -0.3039 -0.4610 0.1756  174 PHE   A CD1 
1306  C  CD2 . PHE   A  174 ? 2.0746 0.6177 1.8598 -0.2473 -0.4915 0.1099  174 PHE   A CD2 
1307  C  CE1 . PHE   A  174 ? 2.0631 0.6594 1.8174 -0.3204 -0.4880 0.1887  174 PHE   A CE1 
1308  C  CE2 . PHE   A  174 ? 2.1135 0.6353 1.8621 -0.2783 -0.5182 0.1338  174 PHE   A CE2 
1309  C  CZ  . PHE   A  174 ? 2.1028 0.6341 1.8474 -0.2903 -0.5011 0.1738  174 PHE   A CZ  
1310  N  N   . LEU   A  175 ? 1.7895 0.7233 1.7805 -0.1794 -0.3168 -0.0800 175 LEU   A N   
1311  C  CA  . LEU   A  175 ? 1.7569 0.7332 1.7447 -0.2087 -0.2665 -0.0919 175 LEU   A CA  
1312  C  C   . LEU   A  175 ? 1.7625 0.7632 1.8133 -0.2414 -0.2109 -0.0709 175 LEU   A C   
1313  O  O   . LEU   A  175 ? 1.7630 0.8050 1.9152 -0.2437 -0.1441 -0.0530 175 LEU   A O   
1314  C  CB  . LEU   A  175 ? 1.7262 0.7424 1.6948 -0.1781 -0.2582 -0.1288 175 LEU   A CB  
1315  C  CG  . LEU   A  175 ? 1.7200 0.7186 1.6235 -0.1579 -0.2764 -0.1869 175 LEU   A CG  
1316  C  CD1 . LEU   A  175 ? 1.7073 0.6418 1.6051 -0.1461 -0.2396 -0.1800 175 LEU   A CD1 
1317  C  CD2 . LEU   A  175 ? 1.6981 0.7004 1.5779 -0.1967 -0.3063 -0.2071 175 LEU   A CD2 
1318  N  N   . GLU   A  176 ? 1.7510 0.8085 1.8163 -0.2127 -0.1661 -0.0395 176 GLU   A N   
1319  C  CA  . GLU   A  176 ? 1.8207 0.9061 1.8729 -0.2391 -0.1183 0.0329  176 GLU   A CA  
1320  C  C   . GLU   A  176 ? 1.8472 0.9169 1.8088 -0.2853 -0.1164 0.0471  176 GLU   A C   
1321  O  O   . GLU   A  176 ? 1.8374 1.0568 1.7608 -0.2809 -0.0652 0.1580  176 GLU   A O   
1322  C  CB  . GLU   A  176 ? 1.8447 0.9588 1.9398 -0.2121 -0.1019 0.0836  176 GLU   A CB  
1323  C  CG  . GLU   A  176 ? 1.8659 1.0357 1.9961 -0.2503 -0.1137 0.1168  176 GLU   A CG  
1324  C  CD  . GLU   A  176 ? 1.9074 1.2229 2.0690 -0.1969 -0.1674 0.1844  176 GLU   A CD  
1325  O  OE1 . GLU   A  176 ? 1.9239 1.3815 2.2646 -0.3638 -0.0771 0.1475  176 GLU   A OE1 
1326  O  OE2 . GLU   A  176 ? 1.9069 1.4458 2.1095 -0.2837 -0.1844 0.1689  176 GLU   A OE2 
1327  N  N   . LYS   A  177 ? 1.9069 0.8774 1.8195 -0.2856 -0.0968 0.0343  177 LYS   A N   
1328  C  CA  . LYS   A  177 ? 1.9388 0.9895 1.8451 -0.3324 -0.1119 0.0027  177 LYS   A CA  
1329  C  C   . LYS   A  177 ? 1.9322 1.0042 1.7850 -0.3496 -0.1539 -0.0001 177 LYS   A C   
1330  O  O   . LYS   A  177 ? 1.9343 1.0566 1.7351 -0.5524 -0.1559 0.0566  177 LYS   A O   
1331  C  CB  . LYS   A  177 ? 2.0433 1.0922 1.8866 -0.3028 -0.0964 -0.0627 177 LYS   A CB  
1332  C  CG  . LYS   A  177 ? 2.1306 1.0681 1.9676 -0.2861 -0.0725 -0.1010 177 LYS   A CG  
1333  C  CD  . LYS   A  177 ? 2.2077 1.1018 2.0453 -0.2661 -0.0515 -0.1666 177 LYS   A CD  
1334  C  CE  . LYS   A  177 ? 2.2723 1.0782 2.0617 -0.2547 -0.0534 -0.2106 177 LYS   A CE  
1335  N  NZ  . LYS   A  177 ? 2.3239 1.1385 2.0873 -0.2869 -0.0753 -0.2629 177 LYS   A NZ  
1336  N  N   . ARG   A  178 ? 1.9114 1.0132 1.7417 -0.3026 -0.1606 0.0188  178 ARG   A N   
1337  C  CA  . ARG   A  178 ? 1.9413 1.0900 1.7711 -0.2347 -0.1785 0.0198  178 ARG   A CA  
1338  C  C   . ARG   A  178 ? 1.8519 1.0791 1.7445 -0.1820 -0.1750 0.0353  178 ARG   A C   
1339  O  O   . ARG   A  178 ? 1.8991 1.0115 1.7668 -0.1426 -0.0657 0.0241  178 ARG   A O   
1340  C  CB  . ARG   A  178 ? 1.9460 1.1297 1.7560 -0.1856 -0.2045 0.0629  178 ARG   A CB  
1341  C  CG  . ARG   A  178 ? 1.9854 1.1691 1.7431 -0.1202 -0.2500 0.0470  178 ARG   A CG  
1342  C  CD  . ARG   A  178 ? 1.9703 1.3150 1.7907 -0.1174 -0.3012 0.0806  178 ARG   A CD  
1343  N  NE  . ARG   A  178 ? 2.0524 1.4348 1.7723 -0.0419 -0.3285 0.0783  178 ARG   A NE  
1344  C  CZ  . ARG   A  178 ? 2.0734 1.5639 1.7752 -0.0237 -0.3336 0.1063  178 ARG   A CZ  
1345  N  NH1 . ARG   A  178 ? 2.0956 1.5532 1.7524 -0.0450 -0.2779 0.0703  178 ARG   A NH1 
1346  N  NH2 . ARG   A  178 ? 2.1014 1.5890 1.7688 0.0088  -0.3426 0.1111  178 ARG   A NH2 
1347  N  N   . TRP   A  179 ? 1.7873 1.0501 1.8148 -0.2189 -0.1574 0.0007  179 TRP   A N   
1348  C  CA  . TRP   A  179 ? 1.7632 1.0127 1.8342 -0.2313 -0.1589 0.0231  179 TRP   A CA  
1349  C  C   . TRP   A  179 ? 1.6781 1.0155 1.9001 -0.2817 -0.1598 -0.0665 179 TRP   A C   
1350  O  O   . TRP   A  179 ? 1.6802 1.1508 1.9094 -0.3656 -0.1432 0.0027  179 TRP   A O   
1351  C  CB  . TRP   A  179 ? 1.7740 0.9970 1.8212 -0.2243 -0.1581 0.0093  179 TRP   A CB  
1352  C  CG  . TRP   A  179 ? 1.8136 1.0022 1.7933 -0.1993 -0.1784 0.0000  179 TRP   A CG  
1353  C  CD1 . TRP   A  179 ? 1.7967 1.0454 1.7766 -0.2078 -0.1804 0.0091  179 TRP   A CD1 
1354  C  CD2 . TRP   A  179 ? 1.8646 1.0835 1.7624 -0.2001 -0.1828 0.0179  179 TRP   A CD2 
1355  N  NE1 . TRP   A  179 ? 1.8010 1.0715 1.7563 -0.2298 -0.1660 -0.0006 179 TRP   A NE1 
1356  C  CE2 . TRP   A  179 ? 1.8543 1.1031 1.7479 -0.2304 -0.1806 0.0267  179 TRP   A CE2 
1357  C  CE3 . TRP   A  179 ? 1.9066 1.0826 1.7624 -0.2175 -0.2133 0.0404  179 TRP   A CE3 
1358  C  CZ2 . TRP   A  179 ? 1.8659 1.1452 1.7110 -0.2367 -0.1955 0.0344  179 TRP   A CZ2 
1359  C  CZ3 . TRP   A  179 ? 1.9248 1.1763 1.7222 -0.2159 -0.2122 0.0378  179 TRP   A CZ3 
1360  C  CH2 . TRP   A  179 ? 1.9202 1.1870 1.7057 -0.2254 -0.2050 0.0529  179 TRP   A CH2 
1361  N  N   . ASN   A  180 ? 1.6909 0.9029 1.8502 -0.3588 -0.1488 -0.1184 180 ASN   A N   
1362  C  CA  . ASN   A  180 ? 1.6978 0.9784 1.9097 -0.3405 -0.1182 -0.1522 180 ASN   A CA  
1363  C  C   . ASN   A  180 ? 1.6673 0.9744 1.8998 -0.2893 -0.1076 -0.1599 180 ASN   A C   
1364  O  O   . ASN   A  180 ? 1.5290 1.1740 1.9374 -0.2895 -0.0943 -0.1138 180 ASN   A O   
1365  C  CB  . ASN   A  180 ? 1.7378 0.8412 1.9286 -0.4236 -0.1231 -0.2219 180 ASN   A CB  
1366  C  CG  . ASN   A  180 ? 1.7390 0.7654 1.9276 -0.4498 -0.1243 -0.2421 180 ASN   A CG  
1367  O  OD1 . ASN   A  180 ? 1.7284 0.7465 1.8841 -0.5150 -0.1747 -0.3076 180 ASN   A OD1 
1368  N  ND2 . ASN   A  180 ? 1.7897 0.7756 1.9504 -0.4378 -0.0975 -0.2759 180 ASN   A ND2 
1369  N  N   . ASP   A  181 ? 1.6971 1.0569 1.9000 -0.2026 -0.1202 -0.1647 181 ASP   A N   
1370  C  CA  . ASP   A  181 ? 1.6839 1.0233 1.8471 -0.1316 -0.1351 -0.1584 181 ASP   A CA  
1371  C  C   . ASP   A  181 ? 1.7290 1.0480 1.8384 -0.1128 -0.1412 -0.1296 181 ASP   A C   
1372  O  O   . ASP   A  181 ? 1.7365 1.0249 1.8256 -0.0602 -0.1479 -0.0919 181 ASP   A O   
1373  C  CB  . ASP   A  181 ? 1.7185 1.0345 1.8486 -0.1108 -0.1449 -0.1835 181 ASP   A CB  
1374  C  CG  . ASP   A  181 ? 1.7570 1.0566 1.7955 -0.1054 -0.1251 -0.1975 181 ASP   A CG  
1375  O  OD1 . ASP   A  181 ? 1.7894 1.0889 1.9013 -0.1018 -0.1666 -0.2606 181 ASP   A OD1 
1376  O  OD2 . ASP   A  181 ? 1.7452 1.0924 1.7895 -0.0657 -0.1524 -0.1818 181 ASP   A OD2 
1377  N  N   . GLU   A  182 ? 1.7440 0.9387 1.8122 -0.0288 -0.1802 -0.0898 182 GLU   A N   
1378  C  CA  . GLU   A  182 ? 1.7625 0.9144 1.8572 -0.0101 -0.1634 -0.0689 182 GLU   A CA  
1379  C  C   . GLU   A  182 ? 1.7669 0.8319 1.8415 0.0015  -0.2111 -0.0800 182 GLU   A C   
1380  O  O   . GLU   A  182 ? 1.8043 0.7397 1.8480 0.0071  -0.2154 -0.0749 182 GLU   A O   
1381  C  CB  . GLU   A  182 ? 1.7222 0.9561 1.8961 0.0282  -0.1754 -0.0077 182 GLU   A CB  
1382  C  CG  . GLU   A  182 ? 1.6908 0.9909 1.9083 0.0600  -0.1515 0.0365  182 GLU   A CG  
1383  C  CD  . GLU   A  182 ? 1.6408 1.0562 1.9453 0.0764  -0.1564 0.0742  182 GLU   A CD  
1384  O  OE1 . GLU   A  182 ? 1.7475 1.0719 1.9392 0.0325  -0.1256 0.1445  182 GLU   A OE1 
1385  O  OE2 . GLU   A  182 ? 1.6135 1.0542 1.9490 0.0529  -0.1696 0.1072  182 GLU   A OE2 
1386  N  N   . LEU   A  183 ? 1.7271 0.8563 1.8473 -0.0334 -0.2291 -0.0945 183 LEU   A N   
1387  C  CA  . LEU   A  183 ? 1.6633 0.9432 1.8308 -0.0365 -0.2615 -0.1353 183 LEU   A CA  
1388  C  C   . LEU   A  183 ? 1.6610 0.9596 1.8062 -0.0715 -0.2647 -0.1329 183 LEU   A C   
1389  O  O   . LEU   A  183 ? 1.6168 1.0485 1.7755 -0.0588 -0.2748 -0.1591 183 LEU   A O   
1390  C  CB  . LEU   A  183 ? 1.6731 0.8702 1.8182 -0.0358 -0.2917 -0.1688 183 LEU   A CB  
1391  C  CG  . LEU   A  183 ? 1.6962 0.8688 1.8343 -0.0020 -0.3244 -0.2407 183 LEU   A CG  
1392  C  CD1 . LEU   A  183 ? 1.7082 0.8174 1.8460 -0.0047 -0.3455 -0.2942 183 LEU   A CD1 
1393  C  CD2 . LEU   A  183 ? 1.6770 0.9138 1.8397 0.0456  -0.3527 -0.2303 183 LEU   A CD2 
1394  N  N   . GLU   A  184 ? 1.6895 1.0515 1.8009 -0.1102 -0.2694 -0.1052 184 GLU   A N   
1395  C  CA  . GLU   A  184 ? 1.6895 0.9979 1.8030 -0.1624 -0.2522 -0.1507 184 GLU   A CA  
1396  C  C   . GLU   A  184 ? 1.6033 0.9804 1.8132 -0.1933 -0.2797 -0.0950 184 GLU   A C   
1397  O  O   . GLU   A  184 ? 1.5412 1.0615 1.7985 -0.1059 -0.2169 -0.0964 184 GLU   A O   
1398  C  CB  . GLU   A  184 ? 1.7492 1.0183 1.7967 -0.1817 -0.3206 -0.1624 184 GLU   A CB  
1399  C  CG  . GLU   A  184 ? 1.8237 1.0235 1.8137 -0.1570 -0.3507 -0.2077 184 GLU   A CG  
1400  C  CD  . GLU   A  184 ? 1.9160 1.1559 1.7482 -0.1694 -0.3899 -0.2703 184 GLU   A CD  
1401  O  OE1 . GLU   A  184 ? 2.0488 1.0400 1.8976 -0.2024 -0.3832 -0.3747 184 GLU   A OE1 
1402  O  OE2 . GLU   A  184 ? 1.9119 1.2903 1.7515 -0.2423 -0.3791 -0.2244 184 GLU   A OE2 
1403  N  N   . LEU   A  185 ? 1.5222 0.9757 1.8095 -0.1774 -0.2877 -0.1028 185 LEU   A N   
1404  C  CA  . LEU   A  185 ? 1.5219 0.9737 1.8027 -0.1810 -0.2959 -0.0216 185 LEU   A CA  
1405  C  C   . LEU   A  185 ? 1.5504 1.0125 1.8054 -0.2241 -0.3075 -0.0135 185 LEU   A C   
1406  O  O   . LEU   A  185 ? 1.5936 1.0978 1.8771 -0.1779 -0.2527 0.0219  185 LEU   A O   
1407  C  CB  . LEU   A  185 ? 1.4888 0.9836 1.7462 -0.1692 -0.3270 0.0241  185 LEU   A CB  
1408  C  CG  . LEU   A  185 ? 1.4433 0.9163 1.7369 -0.1846 -0.3660 0.0219  185 LEU   A CG  
1409  C  CD1 . LEU   A  185 ? 1.4034 0.9071 1.6984 -0.2164 -0.3541 0.0099  185 LEU   A CD1 
1410  C  CD2 . LEU   A  185 ? 1.4289 0.9231 1.7710 -0.1845 -0.3800 0.0368  185 LEU   A CD2 
1411  N  N   . GLU   A  186 ? 1.5315 1.0619 1.8609 -0.2531 -0.3034 0.0434  186 GLU   A N   
1412  C  CA  . GLU   A  186 ? 1.6058 1.1298 1.8654 -0.2846 -0.3016 0.0214  186 GLU   A CA  
1413  C  C   . GLU   A  186 ? 1.6030 1.1076 1.8404 -0.2743 -0.3259 -0.0510 186 GLU   A C   
1414  O  O   . GLU   A  186 ? 1.5686 1.1980 1.7332 -0.3018 -0.3616 -0.0495 186 GLU   A O   
1415  C  CB  . GLU   A  186 ? 1.5900 1.2361 1.9103 -0.3070 -0.3133 0.0291  186 GLU   A CB  
1416  C  CG  . GLU   A  186 ? 1.6329 1.2827 1.9418 -0.3850 -0.2871 0.0436  186 GLU   A CG  
1417  C  CD  . GLU   A  186 ? 1.6499 1.2415 1.9762 -0.4086 -0.2748 -0.0068 186 GLU   A CD  
1418  O  OE1 . GLU   A  186 ? 1.7010 1.2113 2.0135 -0.4398 -0.2974 -0.0628 186 GLU   A OE1 
1419  O  OE2 . GLU   A  186 ? 1.6133 1.4350 2.0241 -0.4632 -0.2678 0.1146  186 GLU   A OE2 
1420  N  N   . ASP   A  187 ? 1.6200 1.0829 1.8856 -0.2848 -0.2914 -0.0372 187 ASP   A N   
1421  C  CA  . ASP   A  187 ? 1.6501 1.0892 1.9572 -0.2686 -0.2814 -0.0233 187 ASP   A CA  
1422  C  C   . ASP   A  187 ? 1.6426 1.0715 1.9406 -0.2801 -0.2648 -0.0397 187 ASP   A C   
1423  O  O   . ASP   A  187 ? 1.7395 1.1345 1.9434 -0.1640 -0.2185 -0.0574 187 ASP   A O   
1424  C  CB  . ASP   A  187 ? 1.6001 1.1207 1.9880 -0.2459 -0.2755 -0.0239 187 ASP   A CB  
1425  C  CG  . ASP   A  187 ? 1.6100 1.1428 1.9862 -0.2213 -0.2873 -0.0539 187 ASP   A CG  
1426  O  OD1 . ASP   A  187 ? 1.5739 1.3804 2.0366 -0.1546 -0.3560 -0.0155 187 ASP   A OD1 
1427  O  OD2 . ASP   A  187 ? 1.5914 0.8824 2.0088 -0.2704 -0.3420 -0.0942 187 ASP   A OD2 
1428  N  N   . ALA   A  188 ? 1.6813 0.9601 1.8827 -0.2677 -0.2234 -0.0506 188 ALA   A N   
1429  C  CA  . ALA   A  188 ? 1.6803 0.8932 1.7954 -0.2523 -0.1846 -0.0593 188 ALA   A CA  
1430  C  C   . ALA   A  188 ? 1.6629 0.7502 1.7419 -0.1921 -0.2289 -0.0451 188 ALA   A C   
1431  O  O   . ALA   A  188 ? 1.7382 0.6125 1.6986 -0.2219 -0.1893 -0.0107 188 ALA   A O   
1432  C  CB  . ALA   A  188 ? 1.6927 0.9668 1.7789 -0.2619 -0.1820 -0.0823 188 ALA   A CB  
1433  N  N   . ILE   A  189 ? 1.6850 0.8441 1.6906 -0.1688 -0.2639 -0.0442 189 ILE   A N   
1434  C  CA  . ILE   A  189 ? 1.6943 0.8739 1.6545 -0.1329 -0.3065 -0.0324 189 ILE   A CA  
1435  C  C   . ILE   A  189 ? 1.6822 0.8886 1.6506 -0.1500 -0.3462 -0.0243 189 ILE   A C   
1436  O  O   . ILE   A  189 ? 1.6114 0.9477 1.5842 -0.1546 -0.4088 -0.0366 189 ILE   A O   
1437  C  CB  . ILE   A  189 ? 1.7319 0.9091 1.6571 -0.1350 -0.3157 -0.0075 189 ILE   A CB  
1438  C  CG1 . ILE   A  189 ? 1.7039 0.8367 1.6521 -0.1150 -0.2790 0.0440  189 ILE   A CG1 
1439  C  CG2 . ILE   A  189 ? 1.7475 0.9380 1.6362 -0.1277 -0.3414 -0.0059 189 ILE   A CG2 
1440  C  CD1 . ILE   A  189 ? 1.6978 0.8446 1.6647 -0.1054 -0.2542 0.0666  189 ILE   A CD1 
1441  N  N   . HIS   A  190 ? 1.6955 0.8684 1.6415 -0.1658 -0.3311 -0.0429 190 HIS   A N   
1442  C  CA  . HIS   A  190 ? 1.7748 0.8782 1.6824 -0.1560 -0.3283 -0.0858 190 HIS   A CA  
1443  C  C   . HIS   A  190 ? 1.8157 0.8252 1.6585 -0.1497 -0.3179 -0.1353 190 HIS   A C   
1444  O  O   . HIS   A  190 ? 1.9103 0.8265 1.6890 -0.0884 -0.2801 -0.1181 190 HIS   A O   
1445  C  CB  . HIS   A  190 ? 1.7744 0.9593 1.7533 -0.1482 -0.3270 -0.0644 190 HIS   A CB  
1446  C  CG  . HIS   A  190 ? 1.8110 0.9511 1.8264 -0.1558 -0.3287 -0.0691 190 HIS   A CG  
1447  N  ND1 . HIS   A  190 ? 1.8697 0.9485 1.8315 -0.1242 -0.3572 -0.0651 190 HIS   A ND1 
1448  C  CD2 . HIS   A  190 ? 1.8248 0.9810 1.8721 -0.1728 -0.3006 -0.0489 190 HIS   A CD2 
1449  C  CE1 . HIS   A  190 ? 1.8817 1.0152 1.8766 -0.1911 -0.3504 -0.0807 190 HIS   A CE1 
1450  N  NE2 . HIS   A  190 ? 1.8543 1.0833 1.8759 -0.1918 -0.3292 -0.0722 190 HIS   A NE2 
1451  N  N   . ILE   A  191 ? 1.7897 0.7552 1.6512 -0.1899 -0.3031 -0.1757 191 ILE   A N   
1452  C  CA  . ILE   A  191 ? 1.7545 0.6783 1.6693 -0.2082 -0.2673 -0.2102 191 ILE   A CA  
1453  C  C   . ILE   A  191 ? 1.7426 0.6501 1.6537 -0.2523 -0.2707 -0.2208 191 ILE   A C   
1454  O  O   . ILE   A  191 ? 1.6634 0.6646 1.6527 -0.2618 -0.2704 -0.2127 191 ILE   A O   
1455  C  CB  . ILE   A  191 ? 1.7905 0.6777 1.6732 -0.2001 -0.2543 -0.2221 191 ILE   A CB  
1456  C  CG1 . ILE   A  191 ? 1.8106 0.7113 1.6712 -0.1894 -0.2149 -0.2574 191 ILE   A CG1 
1457  C  CG2 . ILE   A  191 ? 1.7834 0.6911 1.6764 -0.1947 -0.2543 -0.2145 191 ILE   A CG2 
1458  C  CD1 . ILE   A  191 ? 1.8190 0.7276 1.6770 -0.1716 -0.1974 -0.2577 191 ILE   A CD1 
1459  N  N   . ALA   A  192 ? 1.7030 0.6478 1.6355 -0.2320 -0.2396 -0.1987 192 ALA   A N   
1460  C  CA  . ALA   A  192 ? 1.6956 0.6480 1.6003 -0.1941 -0.2437 -0.1860 192 ALA   A CA  
1461  C  C   . ALA   A  192 ? 1.7113 0.5669 1.6068 -0.2162 -0.2920 -0.1998 192 ALA   A C   
1462  O  O   . ALA   A  192 ? 1.7345 0.5174 1.6003 -0.2229 -0.3042 -0.2367 192 ALA   A O   
1463  C  CB  . ALA   A  192 ? 1.6558 0.6575 1.5771 -0.2032 -0.2486 -0.1643 192 ALA   A CB  
1464  N  N   . LEU   A  193 ? 1.6715 0.6055 1.6345 -0.2109 -0.2919 -0.1912 193 LEU   A N   
1465  C  CA  . LEU   A  193 ? 1.6745 0.7597 1.6018 -0.1544 -0.2889 -0.1581 193 LEU   A CA  
1466  C  C   . LEU   A  193 ? 1.7130 0.7610 1.6468 -0.1395 -0.2656 -0.1491 193 LEU   A C   
1467  O  O   . LEU   A  193 ? 1.7663 0.8723 1.6134 -0.1136 -0.2734 -0.1912 193 LEU   A O   
1468  C  CB  . LEU   A  193 ? 1.6738 0.7433 1.6638 -0.1502 -0.2835 -0.1219 193 LEU   A CB  
1469  C  CG  . LEU   A  193 ? 1.6522 0.7433 1.6391 -0.1383 -0.2857 -0.1092 193 LEU   A CG  
1470  C  CD1 . LEU   A  193 ? 1.6600 0.7860 1.6556 -0.1239 -0.2758 -0.0830 193 LEU   A CD1 
1471  C  CD2 . LEU   A  193 ? 1.6460 0.7034 1.5947 -0.1227 -0.3071 -0.0907 193 LEU   A CD2 
1472  N  N   . LEU   A  194 ? 1.7141 0.8499 1.6608 -0.1057 -0.2243 -0.1409 194 LEU   A N   
1473  C  CA  . LEU   A  194 ? 1.7146 0.8503 1.6721 -0.1190 -0.2283 -0.1570 194 LEU   A CA  
1474  C  C   . LEU   A  194 ? 1.7476 0.8500 1.7232 -0.1032 -0.2335 -0.1055 194 LEU   A C   
1475  O  O   . LEU   A  194 ? 1.7670 0.8757 1.7790 -0.0926 -0.2733 -0.1480 194 LEU   A O   
1476  C  CB  . LEU   A  194 ? 1.7132 0.8823 1.6914 -0.1574 -0.2221 -0.1921 194 LEU   A CB  
1477  C  CG  . LEU   A  194 ? 1.7173 0.9163 1.6990 -0.1936 -0.2370 -0.2189 194 LEU   A CG  
1478  C  CD1 . LEU   A  194 ? 1.6925 0.9047 1.7522 -0.2230 -0.2213 -0.2155 194 LEU   A CD1 
1479  C  CD2 . LEU   A  194 ? 1.7305 0.9783 1.6659 -0.1927 -0.2399 -0.2492 194 LEU   A CD2 
1480  N  N   . THR   A  195 ? 1.6824 0.7528 1.7073 -0.0563 -0.2224 -0.0863 195 THR   A N   
1481  C  CA  . THR   A  195 ? 1.6985 0.7686 1.6879 -0.0633 -0.2441 -0.0824 195 THR   A CA  
1482  C  C   . THR   A  195 ? 1.6843 0.8120 1.6713 -0.1173 -0.2608 -0.0305 195 THR   A C   
1483  O  O   . THR   A  195 ? 1.6369 0.9220 1.6604 -0.0846 -0.3178 0.0259  195 THR   A O   
1484  C  CB  . THR   A  195 ? 1.6518 0.7132 1.6913 -0.0411 -0.2042 -0.0927 195 THR   A CB  
1485  O  OG1 . THR   A  195 ? 1.6479 0.7404 1.7195 0.0084  -0.2122 -0.0549 195 THR   A OG1 
1486  C  CG2 . THR   A  195 ? 1.6091 0.7418 1.7059 -0.0323 -0.2010 -0.1192 195 THR   A CG2 
1487  N  N   . LEU   A  196 ? 1.7342 0.7258 1.7000 -0.1010 -0.2974 -0.0588 196 LEU   A N   
1488  C  CA  . LEU   A  196 ? 1.7777 0.7457 1.6597 -0.1022 -0.2864 -0.0864 196 LEU   A CA  
1489  C  C   . LEU   A  196 ? 1.8262 0.6967 1.6852 -0.0666 -0.2970 -0.0797 196 LEU   A C   
1490  O  O   . LEU   A  196 ? 1.8509 0.6994 1.7601 -0.0483 -0.2768 -0.0918 196 LEU   A O   
1491  C  CB  . LEU   A  196 ? 1.8232 0.7303 1.6003 -0.1209 -0.3037 -0.1273 196 LEU   A CB  
1492  C  CG  . LEU   A  196 ? 1.8469 0.6797 1.5488 -0.1422 -0.3054 -0.1728 196 LEU   A CG  
1493  C  CD1 . LEU   A  196 ? 1.8492 0.6897 1.5286 -0.1451 -0.2897 -0.1753 196 LEU   A CD1 
1494  C  CD2 . LEU   A  196 ? 1.8579 0.6823 1.5154 -0.1293 -0.3255 -0.1729 196 LEU   A CD2 
1495  N  N   . LYS   A  197 ? 1.8221 0.7380 1.6839 -0.0488 -0.3108 -0.0449 197 LYS   A N   
1496  C  CA  . LYS   A  197 ? 1.8280 0.8149 1.7079 -0.0892 -0.3471 -0.0733 197 LYS   A CA  
1497  C  C   . LYS   A  197 ? 1.8852 0.8117 1.7888 -0.0660 -0.3916 -0.1211 197 LYS   A C   
1498  O  O   . LYS   A  197 ? 1.9282 0.9103 1.7803 -0.0214 -0.4310 -0.1676 197 LYS   A O   
1499  C  CB  . LYS   A  197 ? 1.7999 0.8007 1.7460 -0.0974 -0.3130 -0.0353 197 LYS   A CB  
1500  C  CG  . LYS   A  197 ? 1.8060 0.9089 1.7367 -0.0859 -0.3429 -0.0430 197 LYS   A CG  
1501  C  CD  . LYS   A  197 ? 1.8085 1.0172 1.7532 -0.0524 -0.3598 -0.0034 197 LYS   A CD  
1502  C  CE  . LYS   A  197 ? 1.8186 1.0608 1.7231 -0.0652 -0.3674 0.0299  197 LYS   A CE  
1503  N  NZ  . LYS   A  197 ? 1.8189 1.1721 1.7862 -0.0718 -0.3766 0.0227  197 LYS   A NZ  
1504  N  N   . GLU   A  198 ? 1.9246 0.8519 1.8167 -0.0562 -0.3739 -0.0895 198 GLU   A N   
1505  C  CA  . GLU   A  198 ? 1.9444 0.8856 1.9860 0.0293  -0.3892 -0.1071 198 GLU   A CA  
1506  C  C   . GLU   A  198 ? 1.9734 0.8621 1.9484 0.1043  -0.3241 -0.1467 198 GLU   A C   
1507  O  O   . GLU   A  198 ? 1.9923 0.9526 1.9469 0.0910  -0.2903 -0.2594 198 GLU   A O   
1508  C  CB  . GLU   A  198 ? 1.9380 1.0017 1.9965 -0.0057 -0.4073 -0.1058 198 GLU   A CB  
1509  C  CG  . GLU   A  198 ? 1.8989 1.0174 2.1069 -0.0133 -0.4717 -0.0811 198 GLU   A CG  
1510  C  CD  . GLU   A  198 ? 1.8243 1.0653 2.2040 -0.0070 -0.5342 -0.0675 198 GLU   A CD  
1511  O  OE1 . GLU   A  198 ? 1.9179 1.0802 2.2769 0.0305  -0.5567 -0.0497 198 GLU   A OE1 
1512  O  OE2 . GLU   A  198 ? 1.7389 1.0659 2.3298 0.0655  -0.5384 -0.0992 198 GLU   A OE2 
1513  N  N   . SER   A  199 ? 1.9387 0.7385 1.9849 0.1692  -0.2766 -0.0642 199 SER   A N   
1514  C  CA  . SER   A  199 ? 1.9447 0.7845 1.9788 0.2957  -0.1993 -0.0965 199 SER   A CA  
1515  C  C   . SER   A  199 ? 1.9654 0.7221 1.9340 0.3961  -0.1883 -0.1421 199 SER   A C   
1516  O  O   . SER   A  199 ? 2.0205 0.6039 1.8727 0.4649  -0.1652 -0.2009 199 SER   A O   
1517  C  CB  . SER   A  199 ? 1.9376 0.8144 1.9789 0.2898  -0.1881 -0.1153 199 SER   A CB  
1518  O  OG  . SER   A  199 ? 1.9160 0.8748 1.8813 0.3537  -0.1821 -0.1271 199 SER   A OG  
1519  N  N   . VAL   A  200 ? 1.9617 0.8292 1.8724 0.3705  -0.1915 -0.1363 200 VAL   A N   
1520  C  CA  . VAL   A  200 ? 1.9783 0.9254 1.9033 0.3175  -0.1546 -0.1115 200 VAL   A CA  
1521  C  C   . VAL   A  200 ? 2.0691 0.9552 1.9817 0.2536  -0.1470 -0.1356 200 VAL   A C   
1522  O  O   . VAL   A  200 ? 1.9960 1.0618 2.1504 0.2985  -0.1227 -0.1609 200 VAL   A O   
1523  C  CB  . VAL   A  200 ? 1.8816 1.0002 1.8137 0.2947  -0.2175 -0.0681 200 VAL   A CB  
1524  C  CG1 . VAL   A  200 ? 1.8375 1.0710 1.7871 0.3288  -0.2605 -0.0678 200 VAL   A CG1 
1525  C  CG2 . VAL   A  200 ? 1.8515 0.9698 1.8111 0.2766  -0.2084 -0.0445 200 VAL   A CG2 
1526  N  N   . GLU   A  201 ? 2.1565 1.1146 1.9441 0.2010  -0.0591 -0.0150 201 GLU   A N   
1527  C  CA  . GLU   A  201 ? 2.2438 1.1291 1.9359 0.1956  -0.0889 -0.0138 201 GLU   A CA  
1528  C  C   . GLU   A  201 ? 2.1549 1.0644 1.9611 0.1806  -0.1371 -0.0375 201 GLU   A C   
1529  O  O   . GLU   A  201 ? 2.0687 0.8272 1.9669 0.2408  -0.0843 -0.0301 201 GLU   A O   
1530  C  CB  . GLU   A  201 ? 2.2652 1.2840 1.9608 0.2522  -0.0798 0.0269  201 GLU   A CB  
1531  C  CG  . GLU   A  201 ? 2.3727 1.3192 2.0087 0.1763  -0.1070 0.0146  201 GLU   A CG  
1532  C  CD  . GLU   A  201 ? 2.4443 1.4075 2.0497 0.1917  -0.1145 0.1048  201 GLU   A CD  
1533  O  OE1 . GLU   A  201 ? 2.5092 1.4366 2.0308 0.0705  -0.0899 0.0100  201 GLU   A OE1 
1534  O  OE2 . GLU   A  201 ? 2.5231 1.4301 2.0839 0.0481  -0.0228 0.2712  201 GLU   A OE2 
1535  N  N   . GLY   A  202 ? 2.1899 1.0318 1.9884 0.1546  -0.1553 -0.0632 202 GLY   A N   
1536  C  CA  . GLY   A  202 ? 2.1038 0.7867 2.0124 0.1881  -0.2015 -0.0782 202 GLY   A CA  
1537  C  C   . GLY   A  202 ? 2.1325 0.5394 1.9736 0.1091  -0.2365 -0.0894 202 GLY   A C   
1538  O  O   . GLY   A  202 ? 2.0679 0.4201 2.0479 0.1498  -0.2809 -0.0526 202 GLY   A O   
1539  N  N   . GLU   A  203 ? 2.1246 0.6089 1.8539 -0.0123 -0.2376 -0.1128 203 GLU   A N   
1540  C  CA  . GLU   A  203 ? 2.0681 0.7224 1.8313 -0.0103 -0.2734 -0.0998 203 GLU   A CA  
1541  C  C   . GLU   A  203 ? 2.0597 0.6797 1.8681 -0.0419 -0.2037 -0.0820 203 GLU   A C   
1542  O  O   . GLU   A  203 ? 2.0630 0.6980 1.9419 -0.1173 -0.1853 -0.0690 203 GLU   A O   
1543  C  CB  . GLU   A  203 ? 2.0992 0.7953 1.7544 0.0171  -0.2758 -0.0817 203 GLU   A CB  
1544  C  CG  . GLU   A  203 ? 2.1376 0.8962 1.7552 0.0204  -0.2754 -0.1063 203 GLU   A CG  
1545  C  CD  . GLU   A  203 ? 2.1448 0.9598 1.7942 0.0056  -0.2956 -0.1019 203 GLU   A CD  
1546  O  OE1 . GLU   A  203 ? 2.1416 1.0340 1.7739 0.0679  -0.3290 -0.1265 203 GLU   A OE1 
1547  O  OE2 . GLU   A  203 ? 2.1611 1.0039 1.8117 -0.0257 -0.2944 -0.0842 203 GLU   A OE2 
1548  N  N   . PHE   A  204 ? 2.0116 0.6164 1.8651 -0.0630 -0.3314 -0.1034 204 PHE   A N   
1549  C  CA  . PHE   A  204 ? 2.0251 0.6479 1.9174 -0.0555 -0.3449 -0.1674 204 PHE   A CA  
1550  C  C   . PHE   A  204 ? 1.9829 0.7408 1.8569 -0.0264 -0.3789 -0.1990 204 PHE   A C   
1551  O  O   . PHE   A  204 ? 2.0160 0.7116 1.8834 -0.1053 -0.3819 -0.2475 204 PHE   A O   
1552  C  CB  . PHE   A  204 ? 2.0238 0.6405 1.9167 -0.0445 -0.3487 -0.1720 204 PHE   A CB  
1553  C  CG  . PHE   A  204 ? 2.0553 0.4787 1.9741 -0.0120 -0.3390 -0.2151 204 PHE   A CG  
1554  C  CD1 . PHE   A  204 ? 2.0573 0.3314 1.9819 -0.0882 -0.3260 -0.2852 204 PHE   A CD1 
1555  C  CD2 . PHE   A  204 ? 2.0675 0.3757 1.9989 0.0300  -0.3717 -0.2391 204 PHE   A CD2 
1556  C  CE1 . PHE   A  204 ? 1.9924 0.3218 1.9909 -0.1200 -0.3443 -0.2860 204 PHE   A CE1 
1557  C  CE2 . PHE   A  204 ? 2.0448 0.3558 2.0221 0.0255  -0.3448 -0.2369 204 PHE   A CE2 
1558  C  CZ  . PHE   A  204 ? 2.0252 0.3251 2.0260 -0.0463 -0.3325 -0.2515 204 PHE   A CZ  
1559  N  N   . ASN   A  205 ? 2.0108 0.7743 1.7955 -0.0585 -0.3305 -0.2231 205 ASN   A N   
1560  C  CA  . ASN   A  205 ? 2.0358 0.8449 1.7536 0.0064  -0.3284 -0.2284 205 ASN   A CA  
1561  C  C   . ASN   A  205 ? 2.0578 0.8229 1.7393 -0.0015 -0.2581 -0.2308 205 ASN   A C   
1562  O  O   . ASN   A  205 ? 2.0387 0.6892 1.8086 0.0707  -0.2489 -0.1985 205 ASN   A O   
1563  C  CB  . ASN   A  205 ? 2.0586 0.9146 1.7420 0.0114  -0.3840 -0.3265 205 ASN   A CB  
1564  C  CG  . ASN   A  205 ? 2.0713 0.9283 1.6952 0.0347  -0.3953 -0.3931 205 ASN   A CG  
1565  O  OD1 . ASN   A  205 ? 2.0310 0.9356 1.7703 0.0206  -0.3583 -0.3818 205 ASN   A OD1 
1566  N  ND2 . ASN   A  205 ? 2.1420 1.0298 1.6565 0.0202  -0.4434 -0.4280 205 ASN   A ND2 
1567  N  N   . GLY   A  206 ? 2.0268 0.8913 1.6567 0.0152  -0.2346 -0.1556 206 GLY   A N   
1568  C  CA  . GLY   A  206 ? 1.9771 0.8305 1.6004 0.0070  -0.2105 -0.0652 206 GLY   A CA  
1569  C  C   . GLY   A  206 ? 1.9825 0.8960 1.5600 0.0365  -0.1763 -0.0211 206 GLY   A C   
1570  O  O   . GLY   A  206 ? 1.9089 0.8869 1.5414 0.0210  -0.1759 0.0381  206 GLY   A O   
1571  N  N   . ASP   A  207 ? 1.9717 0.8682 1.5672 -0.0183 -0.1768 -0.0538 207 ASP   A N   
1572  C  CA  . ASP   A  207 ? 1.9582 0.8918 1.5791 -0.0093 -0.1794 -0.0786 207 ASP   A CA  
1573  C  C   . ASP   A  207 ? 1.8768 0.9100 1.5708 -0.0540 -0.2175 -0.1106 207 ASP   A C   
1574  O  O   . ASP   A  207 ? 1.8806 0.9536 1.5883 -0.0775 -0.1912 -0.1277 207 ASP   A O   
1575  C  CB  . ASP   A  207 ? 2.0058 0.9107 1.5981 -0.0041 -0.1296 -0.1123 207 ASP   A CB  
1576  C  CG  . ASP   A  207 ? 1.9651 1.0079 1.6177 0.0237  -0.1493 -0.1178 207 ASP   A CG  
1577  O  OD1 . ASP   A  207 ? 2.0245 1.0114 1.7932 -0.0040 -0.0485 -0.0971 207 ASP   A OD1 
1578  O  OD2 . ASP   A  207 ? 1.9862 0.8675 1.5616 0.0500  -0.1124 -0.1976 207 ASP   A OD2 
1579  N  N   . THR   A  208 ? 1.8731 0.9228 1.5730 -0.0516 -0.2765 -0.0744 208 THR   A N   
1580  C  CA  . THR   A  208 ? 1.8752 0.9962 1.5091 -0.0655 -0.2990 -0.0464 208 THR   A CA  
1581  C  C   . THR   A  208 ? 1.8062 0.8553 1.4886 -0.0548 -0.3482 -0.0594 208 THR   A C   
1582  O  O   . THR   A  208 ? 1.7601 0.8055 1.4444 -0.1005 -0.3479 -0.0959 208 THR   A O   
1583  C  CB  . THR   A  208 ? 1.9114 1.0125 1.5991 -0.1140 -0.2997 -0.0330 208 THR   A CB  
1584  O  OG1 . THR   A  208 ? 1.9190 1.1316 1.6331 -0.1241 -0.2811 0.0333  208 THR   A OG1 
1585  C  CG2 . THR   A  208 ? 1.8972 1.0981 1.6098 -0.1051 -0.2817 -0.0312 208 THR   A CG2 
1586  N  N   . ILE   A  209 ? 1.8116 0.8346 1.4042 -0.0131 -0.4061 -0.0234 209 ILE   A N   
1587  C  CA  . ILE   A  209 ? 1.8304 0.8684 1.4129 0.0223  -0.3936 -0.0172 209 ILE   A CA  
1588  C  C   . ILE   A  209 ? 1.7157 0.8671 1.3888 0.0124  -0.4010 0.0250  209 ILE   A C   
1589  O  O   . ILE   A  209 ? 1.6131 1.0476 1.3112 -0.0339 -0.4411 0.0719  209 ILE   A O   
1590  C  CB  . ILE   A  209 ? 1.8553 0.8168 1.4658 0.0081  -0.3957 -0.0338 209 ILE   A CB  
1591  C  CG1 . ILE   A  209 ? 1.9684 0.8466 1.5530 -0.0125 -0.3986 -0.1015 209 ILE   A CG1 
1592  C  CG2 . ILE   A  209 ? 1.8798 0.8103 1.4823 0.0125  -0.3622 -0.0249 209 ILE   A CG2 
1593  C  CD1 . ILE   A  209 ? 1.9937 0.8830 1.6118 0.0219  -0.3851 -0.0847 209 ILE   A CD1 
1594  N  N   . GLU   A  210 ? 1.7036 0.8448 1.3907 -0.0043 -0.3785 -0.0093 210 GLU   A N   
1595  C  CA  . GLU   A  210 ? 1.7424 0.8124 1.4098 0.0207  -0.3208 -0.0057 210 GLU   A CA  
1596  C  C   . GLU   A  210 ? 1.7243 0.7537 1.4906 0.0074  -0.2602 -0.0895 210 GLU   A C   
1597  O  O   . GLU   A  210 ? 1.7128 0.7063 1.4925 -0.0068 -0.2172 -0.1125 210 GLU   A O   
1598  C  CB  . GLU   A  210 ? 1.7497 0.8348 1.4205 0.0258  -0.3437 -0.0285 210 GLU   A CB  
1599  C  CG  . GLU   A  210 ? 1.7849 0.8378 1.4810 0.0375  -0.3651 -0.0382 210 GLU   A CG  
1600  C  CD  . GLU   A  210 ? 1.7725 0.9541 1.5728 0.0932  -0.3606 -0.0690 210 GLU   A CD  
1601  O  OE1 . GLU   A  210 ? 1.8604 0.8642 1.7733 0.1264  -0.3371 -0.1113 210 GLU   A OE1 
1602  O  OE2 . GLU   A  210 ? 1.8159 1.0643 1.5120 0.1428  -0.4123 -0.1245 210 GLU   A OE2 
1603  N  N   . LEU   A  211 ? 1.7357 0.7420 1.4663 0.0108  -0.2189 -0.0236 211 LEU   A N   
1604  C  CA  . LEU   A  211 ? 1.7607 0.7563 1.5007 -0.0086 -0.1838 -0.0081 211 LEU   A CA  
1605  C  C   . LEU   A  211 ? 1.7416 0.7420 1.4882 -0.0292 -0.1646 0.0105  211 LEU   A C   
1606  O  O   . LEU   A  211 ? 1.7303 0.7166 1.5011 -0.0045 -0.1540 0.0044  211 LEU   A O   
1607  C  CB  . LEU   A  211 ? 1.7861 0.7948 1.5154 -0.0162 -0.2042 -0.0391 211 LEU   A CB  
1608  C  CG  . LEU   A  211 ? 1.8343 0.8487 1.5378 0.0101  -0.1666 -0.0350 211 LEU   A CG  
1609  C  CD1 . LEU   A  211 ? 1.8555 0.8878 1.5296 -0.0217 -0.1704 -0.0531 211 LEU   A CD1 
1610  C  CD2 . LEU   A  211 ? 1.8389 0.8703 1.5713 0.0453  -0.1746 0.0120  211 LEU   A CD2 
1611  N  N   . ALA   A  212 ? 1.7158 0.7379 1.4929 -0.0861 -0.1746 0.0149  212 ALA   A N   
1612  C  CA  . ALA   A  212 ? 1.6704 0.7646 1.4428 -0.0995 -0.1944 -0.0114 212 ALA   A CA  
1613  C  C   . ALA   A  212 ? 1.6106 0.7341 1.4391 -0.1086 -0.2110 -0.0227 212 ALA   A C   
1614  O  O   . ALA   A  212 ? 1.6013 0.7744 1.3836 -0.1315 -0.2405 -0.0111 212 ALA   A O   
1615  C  CB  . ALA   A  212 ? 1.6543 0.8354 1.4565 -0.0821 -0.2284 -0.0238 212 ALA   A CB  
1616  N  N   . ILE   A  213 ? 1.5827 0.7273 1.4236 -0.1125 -0.2035 -0.0084 213 ILE   A N   
1617  C  CA  . ILE   A  213 ? 1.5693 0.7064 1.4112 -0.0893 -0.2196 -0.0053 213 ILE   A CA  
1618  C  C   . ILE   A  213 ? 1.5197 0.6529 1.3656 -0.0667 -0.2028 0.0367  213 ILE   A C   
1619  O  O   . ILE   A  213 ? 1.4721 0.6354 1.3391 -0.0613 -0.2014 0.0085  213 ILE   A O   
1620  C  CB  . ILE   A  213 ? 1.5872 0.7399 1.4404 -0.1014 -0.2585 -0.0308 213 ILE   A CB  
1621  C  CG1 . ILE   A  213 ? 1.5871 0.7607 1.4561 -0.0614 -0.2713 -0.0286 213 ILE   A CG1 
1622  C  CG2 . ILE   A  213 ? 1.6065 0.7632 1.4677 -0.1301 -0.2878 -0.0322 213 ILE   A CG2 
1623  C  CD1 . ILE   A  213 ? 1.5760 0.8530 1.4906 -0.0566 -0.2567 -0.0345 213 ILE   A CD1 
1624  N  N   . ILE   A  214 ? 1.4847 0.6278 1.3611 -0.0535 -0.2158 0.0180  214 ILE   A N   
1625  C  CA  . ILE   A  214 ? 1.4670 0.5539 1.4413 -0.0646 -0.2031 0.0259  214 ILE   A CA  
1626  C  C   . ILE   A  214 ? 1.4908 0.6519 1.4958 -0.0257 -0.1907 -0.0066 214 ILE   A C   
1627  O  O   . ILE   A  214 ? 1.5763 0.5981 1.4968 0.0334  -0.1832 0.0122  214 ILE   A O   
1628  C  CB  . ILE   A  214 ? 1.4118 0.4647 1.4272 -0.1085 -0.1878 0.0018  214 ILE   A CB  
1629  C  CG1 . ILE   A  214 ? 1.4118 0.4429 1.4241 -0.1303 -0.1740 0.0115  214 ILE   A CG1 
1630  C  CG2 . ILE   A  214 ? 1.3701 0.4480 1.4173 -0.1048 -0.1780 0.0134  214 ILE   A CG2 
1631  C  CD1 . ILE   A  214 ? 1.4385 0.4109 1.4242 -0.1086 -0.1768 0.0283  214 ILE   A CD1 
1632  N  N   . GLY   A  215 ? 1.4760 0.7039 1.5319 -0.0229 -0.2198 0.0250  215 GLY   A N   
1633  C  CA  . GLY   A  215 ? 1.4620 0.7791 1.5983 -0.0333 -0.2380 0.0354  215 GLY   A CA  
1634  C  C   . GLY   A  215 ? 1.4502 0.7575 1.6340 -0.0738 -0.2359 0.0391  215 GLY   A C   
1635  O  O   . GLY   A  215 ? 1.3692 0.6531 1.6057 -0.0244 -0.1984 0.0493  215 GLY   A O   
1636  N  N   . ASP   A  216 ? 1.4778 0.8312 1.6650 -0.0935 -0.2523 0.1082  216 ASP   A N   
1637  C  CA  . ASP   A  216 ? 1.5168 0.8529 1.7027 -0.0784 -0.2359 0.0811  216 ASP   A CA  
1638  C  C   . ASP   A  216 ? 1.4953 0.9464 1.6959 -0.1134 -0.2600 0.0660  216 ASP   A C   
1639  O  O   . ASP   A  216 ? 1.4881 1.1054 1.6332 -0.0753 -0.3187 0.0239  216 ASP   A O   
1640  C  CB  . ASP   A  216 ? 1.4565 0.9204 1.7534 -0.1305 -0.2006 0.1268  216 ASP   A CB  
1641  C  CG  . ASP   A  216 ? 1.4664 1.0092 1.8180 -0.1561 -0.1877 0.1518  216 ASP   A CG  
1642  O  OD1 . ASP   A  216 ? 1.4575 1.1477 1.8034 -0.1340 -0.1886 0.1571  216 ASP   A OD1 
1643  O  OD2 . ASP   A  216 ? 1.4998 1.1164 1.8368 -0.1882 -0.2225 0.1788  216 ASP   A OD2 
1644  N  N   . GLU   A  217 ? 1.5270 0.9575 1.7517 -0.0775 -0.2997 0.0326  217 GLU   A N   
1645  C  CA  . GLU   A  217 ? 1.5544 0.8517 1.7668 -0.0318 -0.2908 0.0129  217 GLU   A CA  
1646  C  C   . GLU   A  217 ? 1.5242 0.7022 1.7384 -0.0605 -0.2567 -0.0293 217 GLU   A C   
1647  O  O   . GLU   A  217 ? 1.5285 0.5562 1.7971 -0.0677 -0.2742 -0.0320 217 GLU   A O   
1648  C  CB  . GLU   A  217 ? 1.5725 0.9170 1.7236 0.0506  -0.3218 -0.0038 217 GLU   A CB  
1649  C  CG  . GLU   A  217 ? 1.5641 0.9909 1.7461 0.0562  -0.3505 0.0301  217 GLU   A CG  
1650  C  CD  . GLU   A  217 ? 1.5376 1.0648 1.7381 0.0752  -0.3464 0.0254  217 GLU   A CD  
1651  O  OE1 . GLU   A  217 ? 1.4830 1.2005 1.7799 0.0944  -0.3622 0.0029  217 GLU   A OE1 
1652  O  OE2 . GLU   A  217 ? 1.5171 1.1857 1.6825 0.0346  -0.4151 0.0648  217 GLU   A OE2 
1653  N  N   . ASN   A  218 ? 1.5862 0.7062 1.7264 -0.0779 -0.2214 -0.0524 218 ASN   A N   
1654  C  CA  . ASN   A  218 ? 1.6446 0.8223 1.7285 -0.1350 -0.2202 -0.0315 218 ASN   A CA  
1655  C  C   . ASN   A  218 ? 1.6183 0.8172 1.7577 -0.1391 -0.1982 -0.0594 218 ASN   A C   
1656  O  O   . ASN   A  218 ? 1.6106 0.8826 1.7468 -0.2053 -0.2369 -0.1146 218 ASN   A O   
1657  C  CB  . ASN   A  218 ? 1.6984 0.9100 1.6721 -0.1677 -0.1850 -0.0585 218 ASN   A CB  
1658  C  CG  . ASN   A  218 ? 1.7782 0.9792 1.6779 -0.2807 -0.1655 -0.0232 218 ASN   A CG  
1659  O  OD1 . ASN   A  218 ? 1.7932 1.1673 1.6761 -0.3121 -0.2275 0.0053  218 ASN   A OD1 
1660  N  ND2 . ASN   A  218 ? 1.7786 0.9983 1.6355 -0.3277 -0.1653 -0.0457 218 ASN   A ND2 
1661  N  N   . PRO   A  219 ? 1.6141 0.7551 1.7825 -0.1669 -0.1766 -0.0308 219 PRO   A N   
1662  C  CA  . PRO   A  219 ? 1.6102 0.7127 1.7984 -0.1241 -0.1884 -0.0626 219 PRO   A CA  
1663  C  C   . PRO   A  219 ? 1.6515 0.6800 1.7802 -0.1099 -0.2100 -0.0909 219 PRO   A C   
1664  O  O   . PRO   A  219 ? 1.5063 0.7864 1.8555 -0.1054 -0.2504 -0.1179 219 PRO   A O   
1665  C  CB  . PRO   A  219 ? 1.6151 0.6769 1.7828 -0.1379 -0.1493 -0.0351 219 PRO   A CB  
1666  C  CG  . PRO   A  219 ? 1.6039 0.7199 1.7857 -0.1532 -0.1446 -0.0323 219 PRO   A CG  
1667  C  CD  . PRO   A  219 ? 1.6084 0.7599 1.7744 -0.1233 -0.1562 -0.0472 219 PRO   A CD  
1668  N  N   . ASP   A  220 ? 1.6870 0.6624 1.8471 -0.1790 -0.1878 -0.1083 220 ASP   A N   
1669  C  CA  . ASP   A  220 ? 1.7346 0.8001 1.8538 -0.1582 -0.1664 -0.1242 220 ASP   A CA  
1670  C  C   . ASP   A  220 ? 1.6963 0.6880 1.7607 -0.1881 -0.2351 -0.1266 220 ASP   A C   
1671  O  O   . ASP   A  220 ? 1.7023 0.7672 1.7276 -0.2302 -0.2335 -0.1657 220 ASP   A O   
1672  C  CB  . ASP   A  220 ? 1.8050 1.0246 1.8685 -0.1944 -0.2153 -0.1974 220 ASP   A CB  
1673  C  CG  . ASP   A  220 ? 1.9484 1.0343 1.9348 -0.1313 -0.2006 -0.2161 220 ASP   A CG  
1674  O  OD1 . ASP   A  220 ? 2.0466 1.2253 1.9601 -0.0807 -0.1788 -0.1544 220 ASP   A OD1 
1675  O  OD2 . ASP   A  220 ? 2.0294 1.2311 1.9174 -0.2042 -0.2642 -0.3445 220 ASP   A OD2 
1676  N  N   . LEU   A  221 ? 1.5954 0.6858 1.7547 -0.1761 -0.2200 -0.1404 221 LEU   A N   
1677  C  CA  . LEU   A  221 ? 1.5987 0.7323 1.7125 -0.1422 -0.2498 -0.1014 221 LEU   A CA  
1678  C  C   . LEU   A  221 ? 1.5548 0.6214 1.6686 -0.0846 -0.2461 -0.0645 221 LEU   A C   
1679  O  O   . LEU   A  221 ? 1.5269 0.6390 1.6311 -0.1468 -0.2987 -0.1089 221 LEU   A O   
1680  C  CB  . LEU   A  221 ? 1.6129 0.7814 1.7195 -0.1171 -0.2342 -0.0438 221 LEU   A CB  
1681  C  CG  . LEU   A  221 ? 1.6644 0.8469 1.7218 -0.1273 -0.2440 -0.0773 221 LEU   A CG  
1682  C  CD1 . LEU   A  221 ? 1.6549 0.8891 1.7043 -0.1266 -0.2228 -0.0473 221 LEU   A CD1 
1683  C  CD2 . LEU   A  221 ? 1.7198 0.9053 1.7270 -0.1015 -0.2282 -0.0246 221 LEU   A CD2 
1684  N  N   . LEU   A  222 ? 1.5286 0.5900 1.6558 -0.0785 -0.2305 -0.0154 222 LEU   A N   
1685  C  CA  . LEU   A  222 ? 1.4884 0.5759 1.6351 -0.0796 -0.2099 0.0015  222 LEU   A CA  
1686  C  C   . LEU   A  222 ? 1.4915 0.5569 1.6643 -0.0847 -0.2238 0.0222  222 LEU   A C   
1687  O  O   . LEU   A  222 ? 1.5200 0.3296 1.6432 -0.1430 -0.2049 0.0064  222 LEU   A O   
1688  C  CB  . LEU   A  222 ? 1.4888 0.5847 1.6327 -0.0725 -0.2294 -0.0163 222 LEU   A CB  
1689  C  CG  . LEU   A  222 ? 1.4508 0.5544 1.6428 -0.0572 -0.2396 -0.0062 222 LEU   A CG  
1690  C  CD1 . LEU   A  222 ? 1.4279 0.5899 1.6372 -0.0701 -0.2573 -0.0245 222 LEU   A CD1 
1691  C  CD2 . LEU   A  222 ? 1.4755 0.5197 1.6367 -0.0651 -0.2391 -0.0222 222 LEU   A CD2 
1692  N  N   . GLY   A  223 ? 1.5545 0.5724 1.6624 -0.0947 -0.2070 0.0673  223 GLY   A N   
1693  C  CA  . GLY   A  223 ? 1.5381 0.6920 1.6195 -0.0826 -0.2266 0.1060  223 GLY   A CA  
1694  C  C   . GLY   A  223 ? 1.5112 0.7003 1.6046 -0.0665 -0.2319 0.1071  223 GLY   A C   
1695  O  O   . GLY   A  223 ? 1.4524 0.6793 1.5875 -0.0656 -0.3172 0.1444  223 GLY   A O   
1696  N  N   . TYR   A  224 ? 1.5317 0.7164 1.6116 -0.0685 -0.2109 0.1057  224 TYR   A N   
1697  C  CA  . TYR   A  224 ? 1.5537 0.7041 1.6351 -0.0549 -0.1703 0.1221  224 TYR   A CA  
1698  C  C   . TYR   A  224 ? 1.5496 0.7259 1.6473 -0.0683 -0.1637 0.0972  224 TYR   A C   
1699  O  O   . TYR   A  224 ? 1.5820 0.7496 1.5643 -0.0089 -0.1840 0.1277  224 TYR   A O   
1700  C  CB  . TYR   A  224 ? 1.5805 0.6500 1.6412 -0.0409 -0.1734 0.0891  224 TYR   A CB  
1701  C  CG  . TYR   A  224 ? 1.6401 0.6493 1.6162 -0.0573 -0.1581 0.0687  224 TYR   A CG  
1702  C  CD1 . TYR   A  224 ? 1.6284 0.7676 1.6073 0.0149  -0.1616 0.0648  224 TYR   A CD1 
1703  C  CD2 . TYR   A  224 ? 1.6810 0.5878 1.6263 -0.0735 -0.1729 0.0405  224 TYR   A CD2 
1704  C  CE1 . TYR   A  224 ? 1.6890 0.9003 1.5410 -0.0272 -0.1589 0.0266  224 TYR   A CE1 
1705  C  CE2 . TYR   A  224 ? 1.7019 0.6904 1.5664 -0.1124 -0.1933 -0.0071 224 TYR   A CE2 
1706  C  CZ  . TYR   A  224 ? 1.6641 0.8186 1.5616 -0.0520 -0.1860 -0.0122 224 TYR   A CZ  
1707  O  OH  . TYR   A  224 ? 1.7243 1.0358 1.4209 -0.1993 -0.1535 -0.0834 224 TYR   A OH  
1708  N  N   . THR   A  225 ? 1.4911 0.7849 1.7009 -0.0505 -0.0749 0.0430  225 THR   A N   
1709  C  CA  . THR   A  225 ? 1.4784 0.9128 1.7479 -0.0829 -0.0489 0.0154  225 THR   A CA  
1710  C  C   . THR   A  225 ? 1.5297 0.9543 1.8007 -0.1166 0.0142  -0.0330 225 THR   A C   
1711  O  O   . THR   A  225 ? 1.6415 0.9575 1.8244 -0.1500 0.0645  -0.0051 225 THR   A O   
1712  C  CB  . THR   A  225 ? 1.4269 0.9398 1.7776 -0.0421 -0.0209 0.0078  225 THR   A CB  
1713  O  OG1 . THR   A  225 ? 1.3234 0.9532 1.8304 -0.0514 -0.0253 0.0379  225 THR   A OG1 
1714  C  CG2 . THR   A  225 ? 1.4243 0.9244 1.7635 -0.0195 -0.0350 0.0216  225 THR   A CG2 
1715  N  N   . GLY   A  226 ? 1.5061 1.0314 1.8531 -0.0966 0.0290  -0.0556 226 GLY   A N   
1716  C  CA  . GLY   A  226 ? 1.5081 1.0169 1.8926 -0.0363 0.0051  -0.0544 226 GLY   A CA  
1717  C  C   . GLY   A  226 ? 1.4935 1.0100 1.9146 0.0084  -0.0406 -0.0314 226 GLY   A C   
1718  O  O   . GLY   A  226 ? 1.3672 1.1965 1.9042 0.1155  -0.0072 -0.0894 226 GLY   A O   
1719  N  N   . ILE   A  227 ? 1.5596 0.9243 1.8120 -0.0530 -0.0829 -0.0534 227 ILE   A N   
1720  C  CA  . ILE   A  227 ? 1.5886 0.8202 1.8256 -0.0105 -0.1101 -0.0515 227 ILE   A CA  
1721  C  C   . ILE   A  227 ? 1.6307 0.8306 1.8041 -0.0358 -0.1583 -0.0228 227 ILE   A C   
1722  O  O   . ILE   A  227 ? 1.6936 0.8435 1.7762 -0.0214 -0.2694 -0.0438 227 ILE   A O   
1723  C  CB  . ILE   A  227 ? 1.5905 0.7716 1.7791 -0.0024 -0.0840 -0.0328 227 ILE   A CB  
1724  C  CG1 . ILE   A  227 ? 1.6221 0.6640 1.7799 0.0368  -0.0800 -0.0318 227 ILE   A CG1 
1725  C  CG2 . ILE   A  227 ? 1.5951 0.7837 1.7643 -0.0096 -0.0637 -0.0496 227 ILE   A CG2 
1726  C  CD1 . ILE   A  227 ? 1.6039 0.6463 1.7464 -0.0015 -0.0711 -0.0284 227 ILE   A CD1 
1727  N  N   . PRO   A  228 ? 1.6789 0.8467 1.8348 0.0424  -0.1475 -0.0041 228 PRO   A N   
1728  C  CA  . PRO   A  228 ? 1.6832 0.8814 1.8309 0.0397  -0.1359 0.0149  228 PRO   A CA  
1729  C  C   . PRO   A  228 ? 1.6461 0.9374 1.8304 0.0189  -0.1607 0.0600  228 PRO   A C   
1730  O  O   . PRO   A  228 ? 1.6218 0.9045 1.8379 0.0147  -0.1311 0.2008  228 PRO   A O   
1731  C  CB  . PRO   A  228 ? 1.6962 0.8938 1.8607 0.0695  -0.1288 0.0179  228 PRO   A CB  
1732  C  CG  . PRO   A  228 ? 1.6964 0.9106 1.8911 0.0678  -0.1282 0.0453  228 PRO   A CG  
1733  C  CD  . PRO   A  228 ? 1.6810 0.8427 1.8904 0.0645  -0.1428 0.0090  228 PRO   A CD  
1734  N  N   . THR   A  229 ? 1.6603 1.0073 1.8539 0.0196  -0.1811 0.0581  229 THR   A N   
1735  C  CA  . THR   A  229 ? 1.7003 1.0594 1.8167 -0.0213 -0.1816 0.1039  229 THR   A CA  
1736  C  C   . THR   A  229 ? 1.6752 1.0564 1.8245 -0.0061 -0.1527 0.1463  229 THR   A C   
1737  O  O   . THR   A  229 ? 1.6239 1.1535 1.8958 0.1429  -0.2230 0.2689  229 THR   A O   
1738  C  CB  . THR   A  229 ? 1.7571 1.1141 1.7284 0.0373  -0.2019 0.1186  229 THR   A CB  
1739  O  OG1 . THR   A  229 ? 1.7864 1.1164 1.7897 -0.0098 -0.2407 0.1259  229 THR   A OG1 
1740  C  CG2 . THR   A  229 ? 1.7180 1.1162 1.7038 0.0563  -0.1952 0.1525  229 THR   A CG2 
1741  N  N   . ASP   A  230 ? 1.6634 1.1855 1.8258 0.0148  -0.0667 0.0432  230 ASP   A N   
1742  C  CA  . ASP   A  230 ? 1.6732 1.2577 1.8101 0.0335  -0.0705 0.0165  230 ASP   A CA  
1743  C  C   . ASP   A  230 ? 1.7112 1.0358 1.7778 -0.0606 0.0151  0.0207  230 ASP   A C   
1744  O  O   . ASP   A  230 ? 1.7310 1.1963 1.8162 -0.0131 -0.0313 0.0538  230 ASP   A O   
1745  C  CB  . ASP   A  230 ? 1.5777 1.4406 1.8257 0.0547  -0.0506 -0.0305 230 ASP   A CB  
1746  C  CG  . ASP   A  230 ? 1.6010 1.5377 1.7960 0.1213  -0.0953 -0.0732 230 ASP   A CG  
1747  O  OD1 . ASP   A  230 ? 1.5830 1.6269 1.7793 0.1914  -0.1625 -0.0662 230 ASP   A OD1 
1748  O  OD2 . ASP   A  230 ? 1.5683 1.6250 1.7866 0.1621  -0.0746 -0.0619 230 ASP   A OD2 
1749  N  N   . LYS   A  231 ? 1.8116 1.0076 1.7432 -0.0434 0.0639  -0.0308 231 LYS   A N   
1750  C  CA  . LYS   A  231 ? 1.8417 0.8475 1.7096 -0.0589 0.1295  -0.0455 231 LYS   A CA  
1751  C  C   . LYS   A  231 ? 1.8151 0.7473 1.6768 -0.0807 0.0437  -0.0264 231 LYS   A C   
1752  O  O   . LYS   A  231 ? 1.8583 0.4031 1.6709 -0.1318 0.1515  -0.0500 231 LYS   A O   
1753  C  CB  . LYS   A  231 ? 1.9042 0.8571 1.7735 -0.1108 0.1602  -0.0167 231 LYS   A CB  
1754  C  CG  . LYS   A  231 ? 1.8757 0.8894 1.7730 -0.1318 0.2020  -0.0218 231 LYS   A CG  
1755  C  CD  . LYS   A  231 ? 1.8989 0.9069 1.7919 -0.1654 0.2176  -0.0186 231 LYS   A CD  
1756  C  CE  . LYS   A  231 ? 1.9367 0.9164 1.7862 -0.2029 0.2362  -0.0469 231 LYS   A CE  
1757  N  NZ  . LYS   A  231 ? 1.9661 1.0146 1.7811 -0.1834 0.2784  -0.0893 231 LYS   A NZ  
1758  N  N   . GLY   A  232 ? 1.8444 0.7137 1.6056 0.0169  -0.0058 -0.0417 232 GLY   A N   
1759  C  CA  . GLY   A  232 ? 1.7469 0.7661 1.5454 0.0222  -0.0780 -0.0546 232 GLY   A CA  
1760  C  C   . GLY   A  232 ? 1.6750 0.7735 1.4773 0.0033  -0.1248 -0.0735 232 GLY   A C   
1761  O  O   . GLY   A  232 ? 1.6255 0.8122 1.4573 -0.0795 -0.1557 -0.1044 232 GLY   A O   
1762  N  N   . PRO   A  233 ? 1.6475 0.7091 1.4275 -0.0187 -0.1571 -0.0676 233 PRO   A N   
1763  C  CA  . PRO   A  233 ? 1.6274 0.7095 1.4118 -0.0007 -0.1542 -0.0891 233 PRO   A CA  
1764  C  C   . PRO   A  233 ? 1.5815 0.7863 1.4409 0.0034  -0.1363 -0.0572 233 PRO   A C   
1765  O  O   . PRO   A  233 ? 1.5755 0.9367 1.4697 0.1171  -0.1560 0.0442  233 PRO   A O   
1766  C  CB  . PRO   A  233 ? 1.6186 0.6766 1.3894 -0.0306 -0.1623 -0.0824 233 PRO   A CB  
1767  C  CG  . PRO   A  233 ? 1.6493 0.6564 1.4102 -0.0215 -0.1562 -0.0627 233 PRO   A CG  
1768  C  CD  . PRO   A  233 ? 1.6525 0.6958 1.4285 0.0064  -0.1393 -0.0764 233 PRO   A CD  
1769  N  N   . ARG   A  234 ? 1.5833 0.8024 1.4291 -0.0206 -0.1046 -0.0537 234 ARG   A N   
1770  C  CA  . ARG   A  234 ? 1.6031 0.7803 1.4523 -0.0211 -0.0903 -0.0589 234 ARG   A CA  
1771  C  C   . ARG   A  234 ? 1.6270 0.6915 1.4433 -0.0574 -0.1108 -0.0321 234 ARG   A C   
1772  O  O   . ARG   A  234 ? 1.7488 0.6264 1.3826 -0.0469 -0.1108 -0.0821 234 ARG   A O   
1773  C  CB  . ARG   A  234 ? 1.5626 0.7544 1.4569 -0.0418 -0.0848 -0.0503 234 ARG   A CB  
1774  C  CG  . ARG   A  234 ? 1.5432 0.8057 1.4967 -0.0490 -0.0559 -0.0793 234 ARG   A CG  
1775  C  CD  . ARG   A  234 ? 1.5350 0.8225 1.5021 -0.0668 -0.0230 -0.0666 234 ARG   A CD  
1776  N  NE  . ARG   A  234 ? 1.4906 0.9457 1.5594 -0.0696 0.0348  -0.0822 234 ARG   A NE  
1777  C  CZ  . ARG   A  234 ? 1.5029 0.9495 1.6151 -0.1502 0.0251  -0.0780 234 ARG   A CZ  
1778  N  NH1 . ARG   A  234 ? 1.4689 0.9443 1.6122 -0.1513 0.0252  -0.0679 234 ARG   A NH1 
1779  N  NH2 . ARG   A  234 ? 1.4777 1.0860 1.6795 -0.0871 0.0976  -0.0536 234 ARG   A NH2 
1780  N  N   . PHE   A  235 ? 1.6131 0.6147 1.4223 -0.0155 -0.1294 -0.0334 235 PHE   A N   
1781  C  CA  . PHE   A  235 ? 1.6215 0.6641 1.4195 0.0086  -0.1260 -0.0404 235 PHE   A CA  
1782  C  C   . PHE   A  235 ? 1.6066 0.7425 1.4331 0.0166  -0.1307 -0.0263 235 PHE   A C   
1783  O  O   . PHE   A  235 ? 1.6294 0.6299 1.4331 0.0101  -0.0852 -0.1624 235 PHE   A O   
1784  C  CB  . PHE   A  235 ? 1.6353 0.7116 1.3971 -0.0118 -0.1543 -0.0336 235 PHE   A CB  
1785  C  CG  . PHE   A  235 ? 1.7085 0.7749 1.3591 -0.0149 -0.1418 -0.0489 235 PHE   A CG  
1786  C  CD1 . PHE   A  235 ? 1.7379 0.7846 1.3688 -0.0005 -0.1686 -0.0059 235 PHE   A CD1 
1787  C  CD2 . PHE   A  235 ? 1.7458 0.7349 1.3551 -0.0481 -0.1538 -0.0738 235 PHE   A CD2 
1788  C  CE1 . PHE   A  235 ? 1.7632 0.7596 1.3713 -0.0220 -0.1896 -0.0386 235 PHE   A CE1 
1789  C  CE2 . PHE   A  235 ? 1.7450 0.6706 1.3713 -0.0565 -0.1681 -0.0678 235 PHE   A CE2 
1790  C  CZ  . PHE   A  235 ? 1.7504 0.7258 1.3667 -0.0411 -0.1673 -0.0679 235 PHE   A CZ  
1791  N  N   . ARG   A  236 ? 1.6215 0.7294 1.5220 -0.0222 -0.1426 -0.0019 236 ARG   A N   
1792  C  CA  . ARG   A  236 ? 1.6865 0.8466 1.5296 -0.0090 -0.1521 0.0576  236 ARG   A CA  
1793  C  C   . ARG   A  236 ? 1.7001 0.8574 1.5143 0.0090  -0.1505 0.0602  236 ARG   A C   
1794  O  O   . ARG   A  236 ? 1.7182 0.8510 1.5507 0.0438  -0.1477 0.0781  236 ARG   A O   
1795  C  CB  . ARG   A  236 ? 1.6810 0.9714 1.6528 -0.0218 -0.1591 0.0803  236 ARG   A CB  
1796  C  CG  . ARG   A  236 ? 1.6909 1.0835 1.6772 -0.0220 -0.1946 0.1070  236 ARG   A CG  
1797  C  CD  . ARG   A  236 ? 1.6981 1.1843 1.7528 -0.0105 -0.2243 0.1065  236 ARG   A CD  
1798  N  NE  . ARG   A  236 ? 1.7468 1.2268 1.8604 -0.0289 -0.2147 0.1496  236 ARG   A NE  
1799  C  CZ  . ARG   A  236 ? 1.7751 1.4204 1.8579 0.1579  -0.3025 0.1787  236 ARG   A CZ  
1800  N  NH1 . ARG   A  236 ? 1.8179 1.4066 1.8556 0.1788  -0.2306 0.2168  236 ARG   A NH1 
1801  N  NH2 . ARG   A  236 ? 1.8364 1.4433 1.9953 0.1151  -0.2802 0.1190  236 ARG   A NH2 
1802  N  N   . LYS   A  237 ? 1.7185 0.7951 1.4610 -0.0151 -0.1842 0.0578  237 LYS   A N   
1803  C  CA  . LYS   A  237 ? 1.7260 0.7755 1.4046 -0.0651 -0.2182 0.0551  237 LYS   A CA  
1804  C  C   . LYS   A  237 ? 1.7340 0.7950 1.4240 -0.0696 -0.2287 0.0615  237 LYS   A C   
1805  O  O   . LYS   A  237 ? 1.7963 0.8520 1.3869 -0.0751 -0.2627 0.0779  237 LYS   A O   
1806  C  CB  . LYS   A  237 ? 1.7197 0.7737 1.3806 -0.0425 -0.2181 0.0247  237 LYS   A CB  
1807  C  CG  . LYS   A  237 ? 1.7901 0.7682 1.3840 -0.0295 -0.2118 -0.0052 237 LYS   A CG  
1808  C  CD  . LYS   A  237 ? 1.8168 0.8359 1.4171 -0.0438 -0.1855 -0.0116 237 LYS   A CD  
1809  C  CE  . LYS   A  237 ? 1.8631 0.8782 1.4918 -0.0081 -0.1874 0.0340  237 LYS   A CE  
1810  N  NZ  . LYS   A  237 ? 1.9357 0.9717 1.4535 -0.0295 -0.1953 0.0708  237 LYS   A NZ  
1811  N  N   . LEU   A  238 ? 1.6570 0.7978 1.4924 -0.0558 -0.2517 0.0340  238 LEU   A N   
1812  C  CA  . LEU   A  238 ? 1.6243 0.7657 1.5410 -0.0390 -0.2560 0.0033  238 LEU   A CA  
1813  C  C   . LEU   A  238 ? 1.5638 0.7319 1.5160 -0.0340 -0.3166 -0.0747 238 LEU   A C   
1814  O  O   . LEU   A  238 ? 1.5337 0.8271 1.4766 -0.0400 -0.3435 -0.1779 238 LEU   A O   
1815  C  CB  . LEU   A  238 ? 1.6489 0.7840 1.5929 -0.0447 -0.2398 0.0358  238 LEU   A CB  
1816  C  CG  . LEU   A  238 ? 1.6403 0.7316 1.6530 -0.0420 -0.1910 0.0655  238 LEU   A CG  
1817  C  CD1 . LEU   A  238 ? 1.6318 0.7926 1.7067 -0.0585 -0.1938 0.0510  238 LEU   A CD1 
1818  C  CD2 . LEU   A  238 ? 1.6164 0.7225 1.6639 -0.0467 -0.1897 0.0775  238 LEU   A CD2 
1819  N  N   . THR   A  239 ? 1.6021 0.7175 1.5388 -0.0444 -0.3404 -0.0714 239 THR   A N   
1820  C  CA  . THR   A  239 ? 1.6251 0.8259 1.5413 -0.0248 -0.3375 -0.0638 239 THR   A CA  
1821  C  C   . THR   A  239 ? 1.6466 0.9047 1.5236 0.0153  -0.3353 -0.1785 239 THR   A C   
1822  O  O   . THR   A  239 ? 1.6588 0.9157 1.5617 0.0070  -0.2918 -0.2098 239 THR   A O   
1823  C  CB  . THR   A  239 ? 1.6215 0.9045 1.5210 -0.0472 -0.3721 -0.0292 239 THR   A CB  
1824  O  OG1 . THR   A  239 ? 1.6208 0.8169 1.5090 -0.0552 -0.4254 0.0036  239 THR   A OG1 
1825  C  CG2 . THR   A  239 ? 1.6075 0.9163 1.5140 -0.0358 -0.3797 -0.0379 239 THR   A CG2 
1826  N  N   . SER   A  240 ? 1.6440 1.0347 1.5070 0.0217  -0.3486 -0.2004 240 SER   A N   
1827  C  CA  . SER   A  240 ? 1.6648 1.0534 1.5517 -0.0295 -0.3575 -0.2192 240 SER   A CA  
1828  C  C   . SER   A  240 ? 1.6705 1.0955 1.6057 -0.0344 -0.3793 -0.2205 240 SER   A C   
1829  O  O   . SER   A  240 ? 1.6233 1.1074 1.6400 -0.0398 -0.3759 -0.2762 240 SER   A O   
1830  C  CB  . SER   A  240 ? 1.6919 1.0891 1.5500 -0.0302 -0.3451 -0.2427 240 SER   A CB  
1831  O  OG  . SER   A  240 ? 1.6980 1.1665 1.5316 -0.0674 -0.3245 -0.3011 240 SER   A OG  
1832  N  N   . GLN   A  241 ? 1.6494 1.1294 1.5961 -0.0650 -0.4028 -0.1538 241 GLN   A N   
1833  C  CA  . GLN   A  241 ? 1.6594 1.1825 1.5934 -0.1182 -0.4125 -0.1410 241 GLN   A CA  
1834  C  C   . GLN   A  241 ? 1.6768 1.1824 1.5615 -0.0633 -0.4264 -0.1269 241 GLN   A C   
1835  O  O   . GLN   A  241 ? 1.6340 1.3272 1.5603 -0.0813 -0.4648 -0.1050 241 GLN   A O   
1836  C  CB  . GLN   A  241 ? 1.6818 1.1897 1.5592 -0.1415 -0.3474 -0.1168 241 GLN   A CB  
1837  C  CG  . GLN   A  241 ? 1.6621 1.2397 1.5492 -0.2018 -0.3200 -0.0997 241 GLN   A CG  
1838  C  CD  . GLN   A  241 ? 1.6615 1.2979 1.5159 -0.2614 -0.3277 -0.0929 241 GLN   A CD  
1839  O  OE1 . GLN   A  241 ? 1.7071 1.3889 1.4743 -0.3344 -0.2991 -0.0455 241 GLN   A OE1 
1840  N  NE2 . GLN   A  241 ? 1.6236 1.3909 1.5487 -0.2542 -0.3072 -0.0927 241 GLN   A NE2 
1841  N  N   . GLU   A  242 ? 1.6372 1.0958 1.6208 -0.0552 -0.4900 -0.1268 242 GLU   A N   
1842  C  CA  . GLU   A  242 ? 1.6423 1.1556 1.6628 -0.0434 -0.4751 -0.1362 242 GLU   A CA  
1843  C  C   . GLU   A  242 ? 1.6845 1.1361 1.7013 -0.0241 -0.5102 -0.1721 242 GLU   A C   
1844  O  O   . GLU   A  242 ? 1.7097 1.3298 1.6667 -0.0649 -0.4896 -0.2257 242 GLU   A O   
1845  C  CB  . GLU   A  242 ? 1.6164 1.1206 1.7112 -0.0478 -0.4980 -0.1237 242 GLU   A CB  
1846  C  CG  . GLU   A  242 ? 1.6339 1.1510 1.7392 -0.0272 -0.5023 -0.0885 242 GLU   A CG  
1847  C  CD  . GLU   A  242 ? 1.6326 1.1291 1.7432 -0.0430 -0.4896 -0.0729 242 GLU   A CD  
1848  O  OE1 . GLU   A  242 ? 1.6476 1.1823 1.7043 -0.0320 -0.4738 -0.0649 242 GLU   A OE1 
1849  O  OE2 . GLU   A  242 ? 1.6692 1.1243 1.7692 -0.0477 -0.4651 -0.0294 242 GLU   A OE2 
1850  N  N   . ILE   A  243 ? 1.7165 1.0423 1.7197 -0.0167 -0.5166 -0.1506 243 ILE   A N   
1851  C  CA  . ILE   A  243 ? 1.7382 1.0284 1.7818 -0.0340 -0.4874 -0.1299 243 ILE   A CA  
1852  C  C   . ILE   A  243 ? 1.7309 1.0066 1.7903 -0.0661 -0.5111 -0.0526 243 ILE   A C   
1853  O  O   . ILE   A  243 ? 1.6773 1.1990 1.8990 -0.0785 -0.4401 -0.0107 243 ILE   A O   
1854  C  CB  . ILE   A  243 ? 1.7475 1.0260 1.8040 -0.0223 -0.4673 -0.1178 243 ILE   A CB  
1855  C  CG1 . ILE   A  243 ? 1.7548 0.9707 1.7299 0.0404  -0.4548 -0.1127 243 ILE   A CG1 
1856  C  CG2 . ILE   A  243 ? 1.7638 1.0157 1.8527 -0.0796 -0.4835 -0.1336 243 ILE   A CG2 
1857  C  CD1 . ILE   A  243 ? 1.7760 0.9752 1.7138 0.0885  -0.4244 -0.0797 243 ILE   A CD1 
1858  N  N   . ASN   A  244 ? 1.7207 0.9805 1.7855 -0.1052 -0.5330 -0.0081 244 ASN   A N   
1859  C  CA  . ASN   A  244 ? 1.6845 1.1325 1.6756 -0.1288 -0.5372 0.0150  244 ASN   A CA  
1860  C  C   . ASN   A  244 ? 1.7052 1.1882 1.7960 -0.0022 -0.5451 -0.0181 244 ASN   A C   
1861  O  O   . ASN   A  244 ? 1.6196 1.3296 1.8743 -0.0355 -0.5950 -0.0149 244 ASN   A O   
1862  C  CB  . ASN   A  244 ? 1.6781 1.1381 1.6472 -0.1928 -0.5761 0.0332  244 ASN   A CB  
1863  C  CG  . ASN   A  244 ? 1.6537 1.1396 1.5090 -0.2671 -0.5579 0.0431  244 ASN   A CG  
1864  O  OD1 . ASN   A  244 ? 1.6227 1.1738 1.4636 -0.2478 -0.5223 0.0563  244 ASN   A OD1 
1865  N  ND2 . ASN   A  244 ? 1.6477 1.1682 1.4681 -0.3102 -0.5851 0.0204  244 ASN   A ND2 
1866  N  N   . ASP   A  245 ? 1.6832 1.1452 1.8155 -0.0647 -0.5512 -0.0518 245 ASP   A N   
1867  C  CA  . ASP   A  245 ? 1.7351 1.1957 1.8638 -0.0128 -0.4822 -0.1263 245 ASP   A CA  
1868  C  C   . ASP   A  245 ? 1.7590 1.2352 1.9028 0.0241  -0.3969 -0.1186 245 ASP   A C   
1869  O  O   . ASP   A  245 ? 1.6793 1.3962 1.9295 0.0912  -0.3209 -0.0930 245 ASP   A O   
1870  C  CB  . ASP   A  245 ? 1.7679 1.2319 1.8548 -0.0150 -0.4686 -0.1939 245 ASP   A CB  
1871  C  CG  . ASP   A  245 ? 1.8582 1.3234 1.8189 0.0037  -0.4549 -0.1859 245 ASP   A CG  
1872  O  OD1 . ASP   A  245 ? 1.9545 1.3468 1.9041 0.0094  -0.4525 -0.3045 245 ASP   A OD1 
1873  O  OD2 . ASP   A  245 ? 1.9692 1.3337 1.9010 0.0428  -0.4626 -0.2610 245 ASP   A OD2 
1874  N  N   . ARG   A  246 ? 1.7317 1.2024 1.9314 0.0045  -0.4113 -0.1687 246 ARG   A N   
1875  C  CA  . ARG   A  246 ? 1.7926 1.1846 1.9971 -0.0630 -0.3302 -0.1933 246 ARG   A CA  
1876  C  C   . ARG   A  246 ? 1.9627 1.1511 2.1625 -0.1750 -0.2838 -0.2165 246 ARG   A C   
1877  O  O   . ARG   A  246 ? 2.0526 1.0453 2.2939 -0.2790 -0.1581 -0.3374 246 ARG   A O   
1878  C  CB  . ARG   A  246 ? 1.7348 1.1098 2.0296 -0.0396 -0.3118 -0.2495 246 ARG   A CB  
1879  C  CG  . ARG   A  246 ? 1.6366 1.0906 2.0301 -0.0450 -0.3369 -0.2306 246 ARG   A CG  
1880  C  CD  . ARG   A  246 ? 1.6023 1.0660 2.0291 -0.0179 -0.3316 -0.2260 246 ARG   A CD  
1881  N  NE  . ARG   A  246 ? 1.5731 1.0976 2.0283 -0.0018 -0.3320 -0.2546 246 ARG   A NE  
1882  C  CZ  . ARG   A  246 ? 1.6073 1.1342 1.9658 0.0295  -0.3640 -0.2603 246 ARG   A CZ  
1883  N  NH1 . ARG   A  246 ? 1.5978 1.1424 1.9502 0.0765  -0.3718 -0.3138 246 ARG   A NH1 
1884  N  NH2 . ARG   A  246 ? 1.5950 1.2321 1.9557 0.0700  -0.3389 -0.2842 246 ARG   A NH2 
1885  N  N   . LEU   A  247 ? 2.0228 1.0639 2.1645 -0.2070 -0.2611 -0.2083 247 LEU   A N   
1886  C  CA  . LEU   A  247 ? 2.0577 1.0520 2.2297 -0.2042 -0.3159 -0.2014 247 LEU   A CA  
1887  C  C   . LEU   A  247 ? 2.1089 1.2343 2.2266 -0.2019 -0.3817 -0.2344 247 LEU   A C   
1888  O  O   . LEU   A  247 ? 2.0114 1.2340 2.1917 -0.2252 -0.4732 -0.2447 247 LEU   A O   
1889  C  CB  . LEU   A  247 ? 2.0372 0.9341 2.2228 -0.2602 -0.3296 -0.1757 247 LEU   A CB  
1890  C  CG  . LEU   A  247 ? 2.0397 0.8128 2.2203 -0.3197 -0.3253 -0.1806 247 LEU   A CG  
1891  C  CD1 . LEU   A  247 ? 2.0085 0.6734 2.1828 -0.3389 -0.3587 -0.1763 247 LEU   A CD1 
1892  C  CD2 . LEU   A  247 ? 2.0271 0.9350 2.1871 -0.3091 -0.3698 -0.1480 247 LEU   A CD2 
1893  N  N   . GLU   A  248 ? 2.2208 1.3388 2.2455 -0.1240 -0.3753 -0.1856 248 GLU   A N   
1894  C  CA  . GLU   A  248 ? 2.3105 1.4117 2.2669 -0.1723 -0.3960 -0.1975 248 GLU   A CA  
1895  C  C   . GLU   A  248 ? 2.4098 1.4983 2.3282 -0.2304 -0.3303 -0.2121 248 GLU   A C   
1896  O  O   . GLU   A  248 ? 2.4773 1.5321 2.5851 -0.3126 -0.3423 -0.1314 248 GLU   A O   
1897  C  CB  . GLU   A  248 ? 2.4011 1.3920 2.2251 -0.1033 -0.3165 -0.1972 248 GLU   A CB  
1898  C  CG  . GLU   A  248 ? 2.4594 1.3180 2.1763 -0.0457 -0.3368 -0.1981 248 GLU   A CG  
1899  C  CD  . GLU   A  248 ? 2.5034 1.2283 2.1064 0.0145  -0.3172 -0.2908 248 GLU   A CD  
1900  O  OE1 . GLU   A  248 ? 2.4911 1.2187 2.1119 0.0109  -0.3132 -0.2738 248 GLU   A OE1 
1901  O  OE2 . GLU   A  248 ? 2.5620 1.0240 2.0193 0.0792  -0.3014 -0.4209 248 GLU   A OE2 
1902  N  N   . ALA   A  249 ? 2.4142 1.6058 2.2322 -0.2225 -0.3103 -0.1907 249 ALA   A N   
1903  C  CA  . ALA   A  249 ? 2.4162 1.5845 2.2150 -0.2078 -0.2947 -0.2334 249 ALA   A CA  
1904  C  C   . ALA   A  249 ? 2.4288 1.5089 2.2654 -0.2172 -0.2661 -0.1787 249 ALA   A C   
1905  O  O   . ALA   A  249 ? 2.4671 1.4337 2.3777 -0.1406 -0.1833 -0.2860 249 ALA   A O   
1906  C  CB  . ALA   A  249 ? 2.3529 1.6212 2.1314 -0.1711 -0.3024 -0.1922 249 ALA   A CB  
1907  N  N   . LEU   A  250 ? 2.4231 1.4621 2.2896 -0.2522 -0.2361 -0.1380 250 LEU   A N   
1908  C  CA  . LEU   A  250 ? 2.4113 1.5071 2.2726 -0.3679 -0.1989 0.0270  250 LEU   A CA  
1909  C  C   . LEU   A  250 ? 2.3471 1.6053 2.1547 -0.3532 -0.1073 0.1091  250 LEU   A C   
1910  O  O   . LEU   A  250 ? 2.3103 1.4811 2.1574 -0.4515 -0.1044 0.2657  250 LEU   A O   
1911  C  CB  . LEU   A  250 ? 2.3687 1.5834 2.3092 -0.3870 -0.2225 0.0281  250 LEU   A CB  
1912  C  CG  . LEU   A  250 ? 2.3626 1.5431 2.3180 -0.4333 -0.2395 0.0793  250 LEU   A CG  
1913  C  CD1 . LEU   A  250 ? 2.3599 1.5714 2.3394 -0.3775 -0.2905 0.1070  250 LEU   A CD1 
1914  C  CD2 . LEU   A  250 ? 2.2248 1.5705 2.2438 -0.4901 -0.2602 0.1110  250 LEU   A CD2 
1915  O  OXT . LEU   A  250 ? 2.3470 1.4197 2.0465 -0.4611 -0.1328 0.2787  250 LEU   A OXT 
1916  N  N   . GLY   B  2   ? 1.8965 1.2912 1.2014 0.2345  -0.2372 -0.2839 1   GLY   B N   
1917  C  CA  . GLY   B  2   ? 1.9139 1.2297 1.1876 0.2028  -0.2250 -0.3009 1   GLY   B CA  
1918  C  C   . GLY   B  2   ? 1.9072 1.3156 1.2312 0.2209  -0.2034 -0.2885 1   GLY   B C   
1919  O  O   . GLY   B  2   ? 1.9370 1.4078 1.2024 0.1822  -0.2278 -0.3420 1   GLY   B O   
1920  N  N   . SER   B  3   ? 1.8800 1.1458 1.3440 0.2258  -0.2348 -0.3015 2   SER   B N   
1921  C  CA  . SER   B  3   ? 1.8471 1.2285 1.4999 0.2310  -0.2376 -0.3166 2   SER   B CA  
1922  C  C   . SER   B  3   ? 1.8960 1.2158 1.5307 0.2804  -0.2231 -0.3262 2   SER   B C   
1923  O  O   . SER   B  3   ? 1.7515 1.1590 1.5925 0.3735  -0.2218 -0.4447 2   SER   B O   
1924  C  CB  . SER   B  3   ? 1.8567 1.1903 1.4963 0.2259  -0.2342 -0.2242 2   SER   B CB  
1925  O  OG  . SER   B  3   ? 1.8540 1.2918 1.4666 0.1995  -0.2720 -0.2060 2   SER   B OG  
1926  N  N   . ARG   B  4   ? 1.9122 1.3155 1.5929 0.2517  -0.2509 -0.3074 3   ARG   B N   
1927  C  CA  . ARG   B  4   ? 1.9615 1.3257 1.6932 0.2786  -0.2302 -0.2190 3   ARG   B CA  
1928  C  C   . ARG   B  4   ? 1.9191 1.3164 1.7042 0.2772  -0.2153 -0.1282 3   ARG   B C   
1929  O  O   . ARG   B  4   ? 1.7828 1.3644 1.7710 0.2934  -0.0838 -0.2209 3   ARG   B O   
1930  C  CB  . ARG   B  4   ? 1.9568 1.5757 1.8047 0.2479  -0.2308 -0.2231 3   ARG   B CB  
1931  C  CG  . ARG   B  4   ? 2.1568 1.7121 1.8814 0.2381  -0.2674 -0.1000 3   ARG   B CG  
1932  C  CD  . ARG   B  4   ? 2.1908 2.0177 1.9875 0.1758  -0.3203 -0.1177 3   ARG   B CD  
1933  N  NE  . ARG   B  4   ? 2.3874 2.1324 2.0230 0.0871  -0.2638 -0.0770 3   ARG   B NE  
1934  C  CZ  . ARG   B  4   ? 2.6121 2.0220 2.0916 0.0726  -0.3750 -0.1246 3   ARG   B CZ  
1935  N  NH1 . ARG   B  4   ? 2.6273 2.0073 1.9594 0.0805  -0.3572 -0.0712 3   ARG   B NH1 
1936  N  NH2 . ARG   B  4   ? 2.6313 2.0804 2.1562 0.0110  -0.3553 -0.0822 3   ARG   B NH2 
1937  N  N   . ARG   B  5   ? 1.9659 1.3157 1.6352 0.2547  -0.2725 -0.0526 4   ARG   B N   
1938  C  CA  . ARG   B  5   ? 2.0090 1.3669 1.6067 0.1930  -0.2974 -0.0671 4   ARG   B CA  
1939  C  C   . ARG   B  5   ? 1.9873 1.2300 1.4525 0.1825  -0.3673 -0.0746 4   ARG   B C   
1940  O  O   . ARG   B  5   ? 2.0903 1.2939 1.5770 0.1054  -0.2972 -0.0496 4   ARG   B O   
1941  C  CB  . ARG   B  5   ? 1.9968 1.5516 1.6106 0.2052  -0.2310 -0.0494 4   ARG   B CB  
1942  C  CG  . ARG   B  5   ? 2.0200 1.5993 1.7790 0.2377  -0.1175 -0.0574 4   ARG   B CG  
1943  C  CD  . ARG   B  5   ? 2.0198 1.7074 1.7970 0.1844  -0.0119 -0.0845 4   ARG   B CD  
1944  N  NE  . ARG   B  5   ? 2.0040 1.8093 1.8814 0.1512  0.0756  -0.0579 4   ARG   B NE  
1945  C  CZ  . ARG   B  5   ? 2.0200 1.7793 1.8811 0.0983  0.1027  -0.0577 4   ARG   B CZ  
1946  N  NH1 . ARG   B  5   ? 2.0225 1.7717 1.8872 0.1083  0.0924  -0.0809 4   ARG   B NH1 
1947  N  NH2 . ARG   B  5   ? 2.0431 1.8071 1.8682 0.0560  0.1134  -0.0693 4   ARG   B NH2 
1948  N  N   . TYR   B  6   ? 2.0465 1.0012 1.2743 0.0644  -0.4184 -0.0154 5   TYR   B N   
1949  C  CA  . TYR   B  6   ? 2.0538 0.8583 1.3617 0.0352  -0.4107 -0.0145 5   TYR   B CA  
1950  C  C   . TYR   B  6   ? 1.9916 0.7170 1.4014 0.0889  -0.3985 0.0083  5   TYR   B C   
1951  O  O   . TYR   B  6   ? 1.9684 0.5156 1.4214 0.1273  -0.4437 0.0725  5   TYR   B O   
1952  C  CB  . TYR   B  6   ? 2.0595 0.8113 1.4337 -0.0051 -0.4331 0.0283  5   TYR   B CB  
1953  C  CG  . TYR   B  6   ? 2.1399 0.8690 1.4456 -0.0537 -0.4198 0.0529  5   TYR   B CG  
1954  C  CD1 . TYR   B  6   ? 2.1564 0.9774 1.4886 -0.1433 -0.4996 0.0213  5   TYR   B CD1 
1955  C  CD2 . TYR   B  6   ? 2.2153 0.8094 1.4537 -0.0488 -0.4555 0.1112  5   TYR   B CD2 
1956  C  CE1 . TYR   B  6   ? 2.1804 0.9990 1.4321 -0.1843 -0.5297 0.0865  5   TYR   B CE1 
1957  C  CE2 . TYR   B  6   ? 2.2267 0.8731 1.4083 -0.1036 -0.4695 0.1611  5   TYR   B CE2 
1958  C  CZ  . TYR   B  6   ? 2.2125 0.9837 1.3704 -0.1552 -0.5190 0.1291  5   TYR   B CZ  
1959  O  OH  . TYR   B  6   ? 2.1473 1.0277 1.3552 -0.2548 -0.5151 0.1527  5   TYR   B OH  
1960  N  N   . ASP   B  7   ? 2.0245 0.7085 1.4354 0.0863  -0.4121 -0.0393 6   ASP   B N   
1961  C  CA  . ASP   B  7   ? 2.0490 0.5989 1.4807 0.0668  -0.4091 -0.0888 6   ASP   B CA  
1962  C  C   . ASP   B  7   ? 2.0372 0.6067 1.4119 -0.0276 -0.3927 -0.1599 6   ASP   B C   
1963  O  O   . ASP   B  7   ? 2.1484 0.5682 1.4931 -0.0080 -0.4429 -0.1648 6   ASP   B O   
1964  C  CB  . ASP   B  7   ? 2.0454 0.5026 1.4939 0.0730  -0.3784 -0.0458 6   ASP   B CB  
1965  C  CG  . ASP   B  7   ? 2.0368 0.4610 1.4773 0.1221  -0.3575 0.0047  6   ASP   B CG  
1966  O  OD1 . ASP   B  7   ? 2.0942 0.3245 1.5551 0.1067  -0.3315 0.0945  6   ASP   B OD1 
1967  O  OD2 . ASP   B  7   ? 1.9549 0.4731 1.4148 0.1457  -0.3950 -0.0039 6   ASP   B OD2 
1968  N  N   . SER   B  8   ? 1.9812 0.5893 1.3958 -0.0329 -0.4360 -0.2450 7   SER   B N   
1969  C  CA  . SER   B  8   ? 1.9591 0.5804 1.4597 -0.0360 -0.4107 -0.2238 7   SER   B CA  
1970  C  C   . SER   B  8   ? 1.9739 0.7454 1.4172 0.0229  -0.3959 -0.1611 7   SER   B C   
1971  O  O   . SER   B  8   ? 2.0718 0.8121 1.4074 -0.1348 -0.4033 -0.1183 7   SER   B O   
1972  C  CB  . SER   B  8   ? 1.9613 0.4784 1.5128 -0.0707 -0.3775 -0.2187 7   SER   B CB  
1973  O  OG  . SER   B  8   ? 1.9697 0.5054 1.5540 -0.0745 -0.4012 -0.2022 7   SER   B OG  
1974  N  N   . ARG   B  9   ? 1.8937 0.7010 1.4583 0.0662  -0.3573 -0.1018 8   ARG   B N   
1975  C  CA  . ARG   B  9   ? 1.8355 0.7697 1.4417 0.0697  -0.3321 -0.1026 8   ARG   B CA  
1976  C  C   . ARG   B  9   ? 1.7230 0.6876 1.4884 0.0844  -0.3549 -0.0700 8   ARG   B C   
1977  O  O   . ARG   B  9   ? 1.7059 0.6680 1.5033 0.0988  -0.3279 -0.0778 8   ARG   B O   
1978  C  CB  . ARG   B  9   ? 1.8807 0.8718 1.5265 0.1363  -0.3074 -0.0956 8   ARG   B CB  
1979  C  CG  . ARG   B  9   ? 1.9284 1.0609 1.5790 0.1372  -0.2550 -0.0718 8   ARG   B CG  
1980  C  CD  . ARG   B  9   ? 1.9435 1.2248 1.6773 0.2481  -0.1838 -0.0887 8   ARG   B CD  
1981  N  NE  . ARG   B  9   ? 2.0273 1.3526 1.7377 0.2878  -0.2139 -0.0399 8   ARG   B NE  
1982  C  CZ  . ARG   B  9   ? 2.1829 1.3599 1.8278 0.3353  -0.2324 -0.1046 8   ARG   B CZ  
1983  N  NH1 . ARG   B  9   ? 2.2914 1.4703 1.7770 0.3518  -0.1983 -0.1617 8   ARG   B NH1 
1984  N  NH2 . ARG   B  9   ? 2.2037 1.5012 1.8950 0.3522  -0.2991 -0.1160 8   ARG   B NH2 
1985  N  N   . THR   B  10  ? 1.6265 0.7040 1.4630 0.0362  -0.3232 -0.0317 9   THR   B N   
1986  C  CA  . THR   B  10  ? 1.6243 0.6321 1.4347 0.0097  -0.3285 -0.0165 9   THR   B CA  
1987  C  C   . THR   B  10  ? 1.6175 0.5971 1.3824 0.0045  -0.2793 0.0337  9   THR   B C   
1988  O  O   . THR   B  10  ? 1.6558 0.7486 1.3239 0.0428  -0.2466 0.0483  9   THR   B O   
1989  C  CB  . THR   B  10  ? 1.5747 0.5026 1.5393 -0.0326 -0.2828 -0.0459 9   THR   B CB  
1990  O  OG1 . THR   B  10  ? 1.5649 0.4484 1.5604 0.0276  -0.3104 -0.1062 9   THR   B OG1 
1991  C  CG2 . THR   B  10  ? 1.5528 0.5487 1.5467 -0.0194 -0.2900 -0.0451 9   THR   B CG2 
1992  N  N   . THR   B  11  ? 1.6365 0.5562 1.3168 0.0307  -0.3211 -0.0046 10  THR   B N   
1993  C  CA  . THR   B  11  ? 1.6221 0.7012 1.3209 0.0130  -0.3415 -0.0083 10  THR   B CA  
1994  C  C   . THR   B  11  ? 1.6452 0.6667 1.3451 0.0376  -0.3192 -0.0135 10  THR   B C   
1995  O  O   . THR   B  11  ? 1.6927 0.6580 1.3977 0.0047  -0.2946 -0.0293 10  THR   B O   
1996  C  CB  . THR   B  11  ? 1.5810 0.7113 1.2949 0.0167  -0.3924 -0.0199 10  THR   B CB  
1997  O  OG1 . THR   B  11  ? 1.5150 0.9168 1.2517 0.0115  -0.4520 -0.0071 10  THR   B OG1 
1998  C  CG2 . THR   B  11  ? 1.5469 0.7931 1.2868 0.0301  -0.3806 -0.0504 10  THR   B CG2 
1999  N  N   . ILE   B  12  ? 1.6909 0.6647 1.3250 -0.0485 -0.2682 -0.0437 11  ILE   B N   
2000  C  CA  . ILE   B  12  ? 1.7254 0.6521 1.2972 -0.0440 -0.2487 -0.0064 11  ILE   B CA  
2001  C  C   . ILE   B  12  ? 1.6816 0.5239 1.3440 -0.0532 -0.2606 -0.0375 11  ILE   B C   
2002  O  O   . ILE   B  12  ? 1.7079 0.3290 1.3247 -0.1026 -0.2225 -0.0170 11  ILE   B O   
2003  C  CB  . ILE   B  12  ? 1.7585 0.7253 1.3176 -0.0313 -0.2347 -0.0294 11  ILE   B CB  
2004  C  CG1 . ILE   B  12  ? 1.7573 0.6908 1.3349 -0.0292 -0.2428 -0.0058 11  ILE   B CG1 
2005  C  CG2 . ILE   B  12  ? 1.7603 0.7783 1.3494 -0.0667 -0.2125 -0.0225 11  ILE   B CG2 
2006  C  CD1 . ILE   B  12  ? 1.7572 0.6863 1.3522 0.0035  -0.2618 0.0096  11  ILE   B CD1 
2007  N  N   . PHE   B  13  ? 1.7245 0.4856 1.3388 -0.0298 -0.2607 -0.0311 12  PHE   B N   
2008  C  CA  . PHE   B  13  ? 1.7597 0.5771 1.3194 -0.0322 -0.2405 -0.0107 12  PHE   B CA  
2009  C  C   . PHE   B  13  ? 1.7640 0.6638 1.3148 -0.0395 -0.2732 -0.1180 12  PHE   B C   
2010  O  O   . PHE   B  13  ? 1.7868 0.7576 1.3021 -0.0623 -0.2691 -0.1652 12  PHE   B O   
2011  C  CB  . PHE   B  13  ? 1.7773 0.5089 1.3084 -0.0044 -0.2318 -0.0306 12  PHE   B CB  
2012  C  CG  . PHE   B  13  ? 1.7578 0.4140 1.2952 -0.0230 -0.2189 0.0178  12  PHE   B CG  
2013  C  CD1 . PHE   B  13  ? 1.7545 0.3919 1.2706 -0.0132 -0.2262 0.0109  12  PHE   B CD1 
2014  C  CD2 . PHE   B  13  ? 1.7303 0.4359 1.2328 -0.0285 -0.2204 0.0171  12  PHE   B CD2 
2015  C  CE1 . PHE   B  13  ? 1.7168 0.3757 1.2263 -0.0244 -0.2285 0.0379  12  PHE   B CE1 
2016  C  CE2 . PHE   B  13  ? 1.7079 0.4375 1.2063 -0.0190 -0.2212 0.0295  12  PHE   B CE2 
2017  C  CZ  . PHE   B  13  ? 1.7067 0.3642 1.1965 -0.0127 -0.2237 0.0284  12  PHE   B CZ  
2018  N  N   . SER   B  14  ? 1.7627 0.6766 1.3962 -0.0505 -0.2891 -0.0959 13  SER   B N   
2019  C  CA  . SER   B  14  ? 1.7812 0.6931 1.4676 -0.0034 -0.2975 -0.0852 13  SER   B CA  
2020  C  C   . SER   B  14  ? 1.8508 0.6641 1.4935 0.0531  -0.3090 -0.0557 13  SER   B C   
2021  O  O   . SER   B  14  ? 1.8628 0.5684 1.5285 0.1108  -0.2682 -0.0867 13  SER   B O   
2022  C  CB  . SER   B  14  ? 1.7560 0.7450 1.4518 -0.0096 -0.3122 -0.0871 13  SER   B CB  
2023  O  OG  . SER   B  14  ? 1.7021 0.8065 1.4339 -0.0451 -0.3398 -0.0267 13  SER   B OG  
2024  N  N   . PRO   B  15  ? 1.9760 0.5450 1.5270 0.0105  -0.3048 -0.0224 14  PRO   B N   
2025  C  CA  . PRO   B  15  ? 2.0122 0.5188 1.5106 0.0074  -0.2819 0.0397  14  PRO   B CA  
2026  C  C   . PRO   B  15  ? 2.0444 0.4327 1.5266 -0.0320 -0.2560 0.0775  14  PRO   B C   
2027  O  O   . PRO   B  15  ? 2.0848 0.3379 1.4485 -0.1228 -0.2333 0.1237  14  PRO   B O   
2028  C  CB  . PRO   B  15  ? 2.0555 0.5752 1.5535 0.0351  -0.2719 -0.0073 14  PRO   B CB  
2029  C  CG  . PRO   B  15  ? 2.0063 0.6378 1.5673 0.0615  -0.2931 0.0038  14  PRO   B CG  
2030  C  CD  . PRO   B  15  ? 1.9843 0.5627 1.5294 0.0215  -0.3094 -0.0276 14  PRO   B CD  
2031  N  N   . GLU   B  16  ? 2.0294 0.4423 1.4920 -0.0227 -0.2785 0.0865  15  GLU   B N   
2032  C  CA  . GLU   B  16  ? 2.0084 0.5332 1.4752 -0.0040 -0.2958 0.0792  15  GLU   B CA  
2033  C  C   . GLU   B  16  ? 1.9271 0.4995 1.4193 0.0186  -0.3433 0.1271  15  GLU   B C   
2034  O  O   . GLU   B  16  ? 1.9170 0.3220 1.4081 0.0391  -0.3576 0.1785  15  GLU   B O   
2035  C  CB  . GLU   B  16  ? 2.0167 0.7385 1.5252 -0.0679 -0.2995 0.0331  15  GLU   B CB  
2036  C  CG  . GLU   B  16  ? 2.0758 0.7978 1.6642 -0.0798 -0.3019 -0.0611 15  GLU   B CG  
2037  C  CD  . GLU   B  16  ? 2.1284 0.9588 1.6802 -0.1222 -0.2900 -0.0678 15  GLU   B CD  
2038  O  OE1 . GLU   B  16  ? 2.0842 0.8716 1.8982 -0.1240 -0.3747 -0.1173 15  GLU   B OE1 
2039  O  OE2 . GLU   B  16  ? 2.1669 1.0487 1.7860 -0.1349 -0.2979 0.0540  15  GLU   B OE2 
2040  N  N   . GLY   B  17  ? 1.8758 0.5115 1.4061 0.0114  -0.3536 0.1273  16  GLY   B N   
2041  C  CA  . GLY   B  17  ? 1.8486 0.5147 1.4284 0.0113  -0.3543 0.1263  16  GLY   B CA  
2042  C  C   . GLY   B  17  ? 1.8502 0.4821 1.4490 0.0151  -0.3363 0.1106  16  GLY   B C   
2043  O  O   . GLY   B  17  ? 1.8080 0.3831 1.4464 0.0003  -0.4337 0.0778  16  GLY   B O   
2044  N  N   . ARG   B  18  ? 1.8856 0.4932 1.4607 -0.0115 -0.3330 0.0925  17  ARG   B N   
2045  C  CA  . ARG   B  18  ? 1.8660 0.5657 1.4874 -0.0233 -0.3181 0.0560  17  ARG   B CA  
2046  C  C   . ARG   B  18  ? 1.8736 0.6124 1.4066 0.0101  -0.3198 -0.0102 17  ARG   B C   
2047  O  O   . ARG   B  18  ? 1.8584 0.6141 1.4805 0.0179  -0.3263 -0.1147 17  ARG   B O   
2048  C  CB  . ARG   B  18  ? 1.8967 0.6546 1.5240 -0.1067 -0.3134 0.1419  17  ARG   B CB  
2049  C  CG  . ARG   B  18  ? 1.9590 0.8431 1.6448 -0.1349 -0.2657 0.2778  17  ARG   B CG  
2050  C  CD  . ARG   B  18  ? 1.9970 0.8794 1.7948 -0.2216 -0.2545 0.3761  17  ARG   B CD  
2051  N  NE  . ARG   B  18  ? 2.0490 0.9038 1.9709 -0.2569 -0.2585 0.5166  17  ARG   B NE  
2052  C  CZ  . ARG   B  18  ? 2.0197 0.9870 2.0760 -0.2687 -0.2281 0.5454  17  ARG   B CZ  
2053  N  NH1 . ARG   B  18  ? 1.9996 0.9096 2.0807 -0.3103 -0.1855 0.5588  17  ARG   B NH1 
2054  N  NH2 . ARG   B  18  ? 2.0504 1.1439 2.0658 -0.2399 -0.2460 0.5949  17  ARG   B NH2 
2055  N  N   . LEU   B  19  ? 1.8300 0.7061 1.4543 0.0414  -0.3068 -0.0580 18  LEU   B N   
2056  C  CA  . LEU   B  19  ? 1.7710 0.6734 1.4627 0.0158  -0.2981 -0.0627 18  LEU   B CA  
2057  C  C   . LEU   B  19  ? 1.7638 0.6519 1.4872 0.0123  -0.2498 -0.1380 18  LEU   B C   
2058  O  O   . LEU   B  19  ? 1.7543 0.6159 1.4740 -0.0684 -0.2530 -0.2620 18  LEU   B O   
2059  C  CB  . LEU   B  19  ? 1.7523 0.6339 1.5083 0.0192  -0.2650 0.0284  18  LEU   B CB  
2060  C  CG  . LEU   B  19  ? 1.7685 0.6117 1.4741 0.0340  -0.2857 0.0637  18  LEU   B CG  
2061  C  CD1 . LEU   B  19  ? 1.7399 0.6310 1.4061 0.0371  -0.2564 0.0737  18  LEU   B CD1 
2062  C  CD2 . LEU   B  19  ? 1.7707 0.6837 1.5335 0.0365  -0.2748 0.0766  18  LEU   B CD2 
2063  N  N   . TYR   B  20  ? 1.7816 0.5911 1.4656 0.0087  -0.2768 -0.1306 19  TYR   B N   
2064  C  CA  . TYR   B  20  ? 1.7827 0.5765 1.4400 0.0297  -0.2923 -0.1097 19  TYR   B CA  
2065  C  C   . TYR   B  20  ? 1.7872 0.5217 1.4169 0.0223  -0.2836 -0.0839 19  TYR   B C   
2066  O  O   . TYR   B  20  ? 1.8057 0.3778 1.3634 0.0285  -0.3246 -0.1262 19  TYR   B O   
2067  C  CB  . TYR   B  20  ? 1.8001 0.6342 1.4129 0.0385  -0.3172 -0.1481 19  TYR   B CB  
2068  C  CG  . TYR   B  20  ? 1.8624 0.6994 1.4286 0.1021  -0.3603 -0.1883 19  TYR   B CG  
2069  C  CD1 . TYR   B  20  ? 1.8747 0.6758 1.4242 0.0980  -0.3979 -0.2583 19  TYR   B CD1 
2070  C  CD2 . TYR   B  20  ? 1.8560 0.7186 1.4616 0.1150  -0.3743 -0.1689 19  TYR   B CD2 
2071  C  CE1 . TYR   B  20  ? 1.9191 0.7639 1.4942 0.1548  -0.4212 -0.2667 19  TYR   B CE1 
2072  C  CE2 . TYR   B  20  ? 1.8822 0.7896 1.4940 0.1587  -0.3983 -0.2108 19  TYR   B CE2 
2073  C  CZ  . TYR   B  20  ? 1.9066 0.7815 1.5309 0.1873  -0.4020 -0.2349 19  TYR   B CZ  
2074  O  OH  . TYR   B  20  ? 1.8817 1.0595 1.5826 0.2794  -0.4071 -0.2181 19  TYR   B OH  
2075  N  N   . GLN   B  21  ? 1.7606 0.5522 1.4298 0.0247  -0.2395 -0.0479 20  GLN   B N   
2076  C  CA  . GLN   B  21  ? 1.7543 0.5058 1.4505 0.0140  -0.2057 -0.0194 20  GLN   B CA  
2077  C  C   . GLN   B  21  ? 1.7878 0.5432 1.4481 0.0153  -0.1973 -0.0521 20  GLN   B C   
2078  O  O   . GLN   B  21  ? 1.7425 0.6139 1.6048 0.0671  -0.1475 -0.0350 20  GLN   B O   
2079  C  CB  . GLN   B  21  ? 1.7592 0.4641 1.4328 0.0289  -0.2184 -0.0350 20  GLN   B CB  
2080  C  CG  . GLN   B  21  ? 1.7757 0.4146 1.4378 0.0416  -0.2018 -0.0053 20  GLN   B CG  
2081  C  CD  . GLN   B  21  ? 1.7942 0.3865 1.4733 0.0170  -0.1982 -0.0367 20  GLN   B CD  
2082  O  OE1 . GLN   B  21  ? 1.8495 0.3918 1.4941 0.0560  -0.1638 -0.0658 20  GLN   B OE1 
2083  N  NE2 . GLN   B  21  ? 1.7550 0.4726 1.5135 0.0347  -0.2106 -0.0102 20  GLN   B NE2 
2084  N  N   . VAL   B  22  ? 1.7631 0.4827 1.4181 0.0168  -0.1813 -0.0312 21  VAL   B N   
2085  C  CA  . VAL   B  22  ? 1.7483 0.5120 1.3969 0.0265  -0.1885 0.0058  21  VAL   B CA  
2086  C  C   . VAL   B  22  ? 1.7612 0.5312 1.4224 0.0055  -0.1762 -0.0027 21  VAL   B C   
2087  O  O   . VAL   B  22  ? 1.7615 0.4596 1.4472 0.0768  -0.1829 0.0235  21  VAL   B O   
2088  C  CB  . VAL   B  22  ? 1.7472 0.5739 1.3645 0.0400  -0.1873 0.0256  21  VAL   B CB  
2089  C  CG1 . VAL   B  22  ? 1.7399 0.5800 1.3817 0.0495  -0.1778 0.0381  21  VAL   B CG1 
2090  C  CG2 . VAL   B  22  ? 1.7230 0.5920 1.3392 0.0274  -0.1794 0.0157  21  VAL   B CG2 
2091  N  N   . GLU   B  23  ? 1.8020 0.5277 1.4465 0.0151  -0.1632 -0.0032 22  GLU   B N   
2092  C  CA  . GLU   B  23  ? 1.8744 0.5322 1.4141 -0.0262 -0.1680 -0.0383 22  GLU   B CA  
2093  C  C   . GLU   B  23  ? 1.8491 0.3417 1.3528 -0.0087 -0.1308 -0.0393 22  GLU   B C   
2094  O  O   . GLU   B  23  ? 1.8496 0.1550 1.3287 -0.0052 -0.1371 -0.1143 22  GLU   B O   
2095  C  CB  . GLU   B  23  ? 1.9282 0.6259 1.4961 0.0358  -0.1456 -0.0616 22  GLU   B CB  
2096  C  CG  . GLU   B  23  ? 2.0254 0.8103 1.5165 0.0159  -0.1843 -0.0495 22  GLU   B CG  
2097  C  CD  . GLU   B  23  ? 2.1858 0.8895 1.5359 -0.0347 -0.1438 -0.1057 22  GLU   B CD  
2098  O  OE1 . GLU   B  23  ? 2.3329 0.8390 1.5745 -0.0660 -0.1522 -0.1044 22  GLU   B OE1 
2099  O  OE2 . GLU   B  23  ? 2.2559 1.1345 1.7837 -0.1411 -0.1202 0.0580  22  GLU   B OE2 
2100  N  N   . TYR   B  24  ? 1.7840 0.3789 1.3396 -0.0116 -0.1698 -0.0044 23  TYR   B N   
2101  C  CA  . TYR   B  24  ? 1.7635 0.5220 1.3176 -0.0363 -0.1688 0.0340  23  TYR   B CA  
2102  C  C   . TYR   B  24  ? 1.7194 0.5046 1.3063 -0.0751 -0.1816 -0.0044 23  TYR   B C   
2103  O  O   . TYR   B  24  ? 1.7377 0.5988 1.2972 -0.1368 -0.1554 -0.0268 23  TYR   B O   
2104  C  CB  . TYR   B  24  ? 1.7289 0.5894 1.3059 -0.0100 -0.1844 0.0633  23  TYR   B CB  
2105  C  CG  . TYR   B  24  ? 1.7528 0.5878 1.3146 0.0046  -0.1703 0.0824  23  TYR   B CG  
2106  C  CD1 . TYR   B  24  ? 1.7893 0.5831 1.3334 0.0009  -0.1441 0.0937  23  TYR   B CD1 
2107  C  CD2 . TYR   B  24  ? 1.7587 0.6224 1.3085 0.0138  -0.1709 0.0935  23  TYR   B CD2 
2108  C  CE1 . TYR   B  24  ? 1.8042 0.6358 1.3656 0.0320  -0.1577 0.1193  23  TYR   B CE1 
2109  C  CE2 . TYR   B  24  ? 1.7770 0.6320 1.3077 0.0294  -0.1662 0.1005  23  TYR   B CE2 
2110  C  CZ  . TYR   B  24  ? 1.7830 0.6337 1.3593 0.0553  -0.1667 0.1205  23  TYR   B CZ  
2111  O  OH  . TYR   B  24  ? 1.8301 0.6543 1.3689 0.1007  -0.1508 0.1497  23  TYR   B OH  
2112  N  N   . ALA   B  25  ? 1.7041 0.4844 1.2939 -0.0671 -0.1933 0.0227  24  ALA   B N   
2113  C  CA  . ALA   B  25  ? 1.7166 0.4546 1.2689 -0.0672 -0.2232 0.0395  24  ALA   B CA  
2114  C  C   . ALA   B  25  ? 1.7497 0.4016 1.2631 -0.0655 -0.2394 0.0793  24  ALA   B C   
2115  O  O   . ALA   B  25  ? 1.7697 0.4243 1.2881 -0.0678 -0.2846 0.0710  24  ALA   B O   
2116  C  CB  . ALA   B  25  ? 1.6903 0.4669 1.2467 -0.0781 -0.2023 0.0368  24  ALA   B CB  
2117  N  N   . LEU   B  26  ? 1.8077 0.3825 1.3049 -0.0492 -0.2647 0.1158  25  LEU   B N   
2118  C  CA  . LEU   B  26  ? 1.8644 0.4194 1.2817 -0.0303 -0.2864 0.1838  25  LEU   B CA  
2119  C  C   . LEU   B  26  ? 1.8732 0.4339 1.3023 -0.0466 -0.3042 0.2095  25  LEU   B C   
2120  O  O   . LEU   B  26  ? 1.8397 0.4076 1.3354 -0.0122 -0.3526 0.3097  25  LEU   B O   
2121  C  CB  . LEU   B  26  ? 1.8985 0.3783 1.2495 -0.0478 -0.2944 0.1415  25  LEU   B CB  
2122  C  CG  . LEU   B  26  ? 1.9157 0.3662 1.2086 -0.0241 -0.2836 0.1386  25  LEU   B CG  
2123  C  CD1 . LEU   B  26  ? 1.9213 0.3792 1.1962 -0.0350 -0.3000 0.0956  25  LEU   B CD1 
2124  C  CD2 . LEU   B  26  ? 1.9112 0.3377 1.2062 -0.0191 -0.2861 0.1637  25  LEU   B CD2 
2125  N  N   . GLU   B  27  ? 1.9235 0.5383 1.2883 0.0002  -0.2787 0.2005  26  GLU   B N   
2126  C  CA  . GLU   B  27  ? 1.9477 0.6754 1.3172 -0.0562 -0.2894 0.1301  26  GLU   B CA  
2127  C  C   . GLU   B  27  ? 1.9182 0.7688 1.3082 -0.0099 -0.2431 0.1584  26  GLU   B C   
2128  O  O   . GLU   B  27  ? 1.9010 0.9177 1.3812 -0.0347 -0.2296 0.2124  26  GLU   B O   
2129  C  CB  . GLU   B  27  ? 1.9969 0.7678 1.3362 -0.0252 -0.2830 0.0871  26  GLU   B CB  
2130  C  CG  . GLU   B  27  ? 2.0731 0.7930 1.4083 -0.0251 -0.2824 0.0348  26  GLU   B CG  
2131  C  CD  . GLU   B  27  ? 2.1315 0.7887 1.4350 -0.0566 -0.3033 0.0476  26  GLU   B CD  
2132  O  OE1 . GLU   B  27  ? 2.2298 0.8091 1.5462 -0.1315 -0.3071 -0.0305 26  GLU   B OE1 
2133  O  OE2 . GLU   B  27  ? 2.2005 0.7834 1.4712 0.0409  -0.3194 0.1353  26  GLU   B OE2 
2134  N  N   . SER   B  28  ? 1.8368 0.7404 1.2856 -0.0148 -0.1934 0.1178  27  SER   B N   
2135  C  CA  . SER   B  28  ? 1.7809 0.7798 1.2504 0.0066  -0.1479 0.1021  27  SER   B CA  
2136  C  C   . SER   B  28  ? 1.7393 0.7618 1.2588 -0.0238 -0.1383 0.1337  27  SER   B C   
2137  O  O   . SER   B  28  ? 1.6837 0.7126 1.1686 0.0440  -0.1076 0.1872  27  SER   B O   
2138  C  CB  . SER   B  28  ? 1.7765 0.8048 1.2066 -0.0093 -0.1424 0.0850  27  SER   B CB  
2139  O  OG  . SER   B  28  ? 1.7095 0.8889 1.2461 0.0210  -0.1313 0.0633  27  SER   B OG  
2140  N  N   . ILE   B  29  ? 1.7020 0.8073 1.2991 -0.0724 -0.1208 0.0983  28  ILE   B N   
2141  C  CA  . ILE   B  29  ? 1.6543 0.8837 1.3940 -0.0951 -0.1023 0.0692  28  ILE   B CA  
2142  C  C   . ILE   B  29  ? 1.6381 0.8910 1.5039 -0.1497 -0.1033 0.0323  28  ILE   B C   
2143  O  O   . ILE   B  29  ? 1.6229 0.9418 1.5396 -0.1904 -0.0963 -0.0117 28  ILE   B O   
2144  C  CB  . ILE   B  29  ? 1.6434 0.9569 1.3981 -0.1090 -0.1189 0.0613  28  ILE   B CB  
2145  C  CG1 . ILE   B  29  ? 1.5696 0.9747 1.3941 -0.1032 -0.1162 0.0718  28  ILE   B CG1 
2146  C  CG2 . ILE   B  29  ? 1.6533 1.0317 1.4103 -0.0992 -0.1098 0.0568  28  ILE   B CG2 
2147  C  CD1 . ILE   B  29  ? 1.5486 0.9618 1.4135 -0.0978 -0.1044 0.0749  28  ILE   B CD1 
2148  N  N   . SER   B  30  ? 1.6655 0.8677 1.5468 -0.1656 -0.0850 0.0546  29  SER   B N   
2149  C  CA  . SER   B  30  ? 1.6970 0.9177 1.5544 -0.2129 -0.0714 0.0573  29  SER   B CA  
2150  C  C   . SER   B  30  ? 1.7304 0.8579 1.5875 -0.1881 -0.1143 0.0488  29  SER   B C   
2151  O  O   . SER   B  30  ? 1.6891 0.9716 1.7113 -0.2393 -0.1151 0.0556  29  SER   B O   
2152  C  CB  . SER   B  30  ? 1.6829 0.9852 1.5932 -0.1921 -0.0364 0.0760  29  SER   B CB  
2153  O  OG  . SER   B  30  ? 1.6725 1.1231 1.5895 -0.2426 0.0495  0.0647  29  SER   B OG  
2154  N  N   . HIS   B  31  ? 1.6786 0.7435 1.5555 -0.2119 -0.1641 -0.0250 30  HIS   B N   
2155  C  CA  . HIS   B  31  ? 1.7330 0.7747 1.5221 -0.2285 -0.1711 -0.0609 30  HIS   B CA  
2156  C  C   . HIS   B  31  ? 1.7288 0.7056 1.5001 -0.2719 -0.1904 -0.0543 30  HIS   B C   
2157  O  O   . HIS   B  31  ? 1.8011 0.4465 1.4545 -0.3262 -0.1789 -0.1092 30  HIS   B O   
2158  C  CB  . HIS   B  31  ? 1.7330 0.8642 1.5048 -0.2050 -0.2102 -0.0927 30  HIS   B CB  
2159  C  CG  . HIS   B  31  ? 1.8203 0.8727 1.5232 -0.1573 -0.2008 -0.1273 30  HIS   B CG  
2160  N  ND1 . HIS   B  31  ? 1.8951 0.8563 1.5651 -0.1619 -0.1643 -0.1374 30  HIS   B ND1 
2161  C  CD2 . HIS   B  31  ? 1.8376 0.8678 1.4968 -0.1352 -0.1863 -0.1793 30  HIS   B CD2 
2162  C  CE1 . HIS   B  31  ? 1.9341 0.8666 1.5817 -0.1338 -0.1463 -0.1722 30  HIS   B CE1 
2163  N  NE2 . HIS   B  31  ? 1.9072 0.8483 1.5262 -0.1209 -0.1639 -0.1954 30  HIS   B NE2 
2164  N  N   . ALA   B  32  ? 1.7252 0.7236 1.4889 -0.2768 -0.2024 -0.0570 31  ALA   B N   
2165  C  CA  . ALA   B  32  ? 1.6867 0.7788 1.4848 -0.2621 -0.1885 -0.0209 31  ALA   B CA  
2166  C  C   . ALA   B  32  ? 1.7342 0.8298 1.5165 -0.2863 -0.1569 0.0189  31  ALA   B C   
2167  O  O   . ALA   B  32  ? 1.6338 0.9322 1.5149 -0.3115 -0.1365 0.0590  31  ALA   B O   
2168  C  CB  . ALA   B  32  ? 1.6759 0.7456 1.4824 -0.2304 -0.1935 -0.0260 31  ALA   B CB  
2169  N  N   . GLY   B  33  ? 1.7512 0.8288 1.5197 -0.2742 -0.1460 0.0308  32  GLY   B N   
2170  C  CA  . GLY   B  33  ? 1.8066 0.8456 1.5298 -0.2989 -0.1177 0.0643  32  GLY   B CA  
2171  C  C   . GLY   B  33  ? 1.8430 0.8403 1.5252 -0.3027 -0.1219 0.0772  32  GLY   B C   
2172  O  O   . GLY   B  33  ? 1.8028 0.9065 1.4851 -0.3487 -0.1193 0.1337  32  GLY   B O   
2173  N  N   . THR   B  34  ? 1.8880 0.8931 1.4950 -0.3037 -0.1325 0.0813  33  THR   B N   
2174  C  CA  . THR   B  34  ? 1.8621 0.9175 1.5265 -0.2952 -0.2092 0.0788  33  THR   B CA  
2175  C  C   . THR   B  34  ? 1.8192 0.8864 1.5158 -0.3315 -0.2231 0.0791  33  THR   B C   
2176  O  O   . THR   B  34  ? 1.8624 0.9212 1.5179 -0.2680 -0.2195 0.0946  33  THR   B O   
2177  C  CB  . THR   B  34  ? 1.9048 0.9372 1.5268 -0.3112 -0.2458 0.1047  33  THR   B CB  
2178  O  OG1 . THR   B  34  ? 1.9530 0.9396 1.5302 -0.2873 -0.2617 0.0959  33  THR   B OG1 
2179  C  CG2 . THR   B  34  ? 1.9109 0.9856 1.5296 -0.3097 -0.2612 0.1577  33  THR   B CG2 
2180  N  N   . ALA   B  35  ? 1.7925 0.7415 1.5685 -0.3497 -0.1865 0.0898  34  ALA   B N   
2181  C  CA  . ALA   B  35  ? 1.8002 0.7562 1.5611 -0.3333 -0.1918 0.0910  34  ALA   B CA  
2182  C  C   . ALA   B  35  ? 1.7808 0.7288 1.5590 -0.3370 -0.1890 0.0834  34  ALA   B C   
2183  O  O   . ALA   B  35  ? 1.8028 0.7037 1.5765 -0.3223 -0.2083 0.0705  34  ALA   B O   
2184  C  CB  . ALA   B  35  ? 1.8116 0.7796 1.5526 -0.3078 -0.1887 0.1305  34  ALA   B CB  
2185  N  N   . ILE   B  36  ? 1.7981 0.7278 1.5184 -0.3158 -0.2104 0.0590  35  ILE   B N   
2186  C  CA  . ILE   B  36  ? 1.8307 0.7143 1.5134 -0.2974 -0.2223 0.0660  35  ILE   B CA  
2187  C  C   . ILE   B  36  ? 1.8178 0.7189 1.4878 -0.2995 -0.2185 0.0634  35  ILE   B C   
2188  O  O   . ILE   B  36  ? 1.7775 0.7303 1.5077 -0.3138 -0.2455 0.0220  35  ILE   B O   
2189  C  CB  . ILE   B  36  ? 1.8862 0.6937 1.5137 -0.3175 -0.2435 0.0822  35  ILE   B CB  
2190  C  CG1 . ILE   B  36  ? 1.9138 0.6990 1.5751 -0.2746 -0.2631 0.1113  35  ILE   B CG1 
2191  C  CG2 . ILE   B  36  ? 1.9302 0.7095 1.5208 -0.3124 -0.2172 0.0886  35  ILE   B CG2 
2192  C  CD1 . ILE   B  36  ? 1.9162 0.7760 1.6657 -0.3067 -0.2443 0.1205  35  ILE   B CD1 
2193  N  N   . GLY   B  37  ? 1.8262 0.6168 1.4937 -0.3143 -0.1996 0.0351  36  GLY   B N   
2194  C  CA  . GLY   B  37  ? 1.8617 0.6474 1.5136 -0.2779 -0.1455 0.0246  36  GLY   B CA  
2195  C  C   . GLY   B  37  ? 1.8969 0.6971 1.5076 -0.2729 -0.0916 0.0004  36  GLY   B C   
2196  O  O   . GLY   B  37  ? 1.9010 0.6718 1.5139 -0.2771 -0.1368 -0.0568 36  GLY   B O   
2197  N  N   . ILE   B  38  ? 1.9235 0.7759 1.5551 -0.2598 -0.0418 0.0093  37  ILE   B N   
2198  C  CA  . ILE   B  38  ? 1.9534 0.7829 1.5698 -0.2812 -0.0166 0.0222  37  ILE   B CA  
2199  C  C   . ILE   B  38  ? 1.9858 0.7792 1.5584 -0.2589 -0.0387 0.0289  37  ILE   B C   
2200  O  O   . ILE   B  38  ? 2.0116 0.5762 1.5526 -0.3150 -0.0370 0.0347  37  ILE   B O   
2201  C  CB  . ILE   B  38  ? 1.9772 0.7930 1.5844 -0.2896 0.0202  0.0348  37  ILE   B CB  
2202  C  CG1 . ILE   B  38  ? 1.9786 0.7940 1.5719 -0.3049 0.0307  0.0326  37  ILE   B CG1 
2203  C  CG2 . ILE   B  38  ? 2.0029 0.8361 1.5814 -0.2676 0.0180  0.0338  37  ILE   B CG2 
2204  C  CD1 . ILE   B  38  ? 1.9987 0.8373 1.6216 -0.3354 0.0516  0.0439  37  ILE   B CD1 
2205  N  N   . MET   B  39  ? 2.0547 0.7297 1.5180 -0.2271 -0.0348 -0.0156 38  MET   B N   
2206  C  CA  . MET   B  39  ? 2.1052 0.7387 1.5088 -0.1808 -0.0085 -0.0200 38  MET   B CA  
2207  C  C   . MET   B  39  ? 2.0973 0.6228 1.5058 -0.1965 -0.0275 0.0107  38  MET   B C   
2208  O  O   . MET   B  39  ? 2.1564 0.4764 1.4045 -0.2788 -0.0389 -0.0469 38  MET   B O   
2209  C  CB  . MET   B  39  ? 2.1046 0.8824 1.4994 -0.1397 -0.0609 -0.0462 38  MET   B CB  
2210  C  CG  . MET   B  39  ? 2.1794 0.9356 1.5195 -0.1135 -0.0894 -0.1108 38  MET   B CG  
2211  S  SD  . MET   B  39  ? 2.2462 1.1556 1.5426 -0.0725 -0.1916 -0.0877 38  MET   B SD  
2212  C  CE  . MET   B  39  ? 2.2719 1.1205 1.5976 -0.0286 -0.1829 -0.0942 38  MET   B CE  
2213  N  N   . ALA   B  40  ? 2.0823 0.7100 1.5555 -0.1995 0.0283  0.0143  39  ALA   B N   
2214  C  CA  . ALA   B  40  ? 2.0782 0.8443 1.5660 -0.1812 0.0471  0.0756  39  ALA   B CA  
2215  C  C   . ALA   B  40  ? 2.1133 0.9488 1.5257 -0.0834 0.0365  -0.0198 39  ALA   B C   
2216  O  O   . ALA   B  40  ? 2.0202 1.1355 1.5362 -0.0709 0.0777  0.0367  39  ALA   B O   
2217  C  CB  . ALA   B  40  ? 2.0546 0.7739 1.5714 -0.2344 0.1015  0.0678  39  ALA   B CB  
2218  N  N   . SER   B  41  ? 2.1354 1.0655 1.5745 -0.0183 0.0973  0.0390  40  SER   B N   
2219  C  CA  . SER   B  41  ? 2.1288 1.0952 1.5930 0.0226  0.0797  0.0062  40  SER   B CA  
2220  C  C   . SER   B  41  ? 2.1154 1.0440 1.6682 0.0032  0.0449  -0.0380 40  SER   B C   
2221  O  O   . SER   B  41  ? 2.1071 1.0669 1.7174 0.0025  -0.0126 -0.0737 40  SER   B O   
2222  C  CB  . SER   B  41  ? 2.1639 1.1536 1.5942 0.0406  0.0960  0.0240  40  SER   B CB  
2223  O  OG  . SER   B  41  ? 2.1656 1.1536 1.5786 0.0394  0.1327  0.0362  40  SER   B OG  
2224  N  N   . ASP   B  42  ? 2.0962 1.0936 1.6978 0.0279  0.0379  0.0134  41  ASP   B N   
2225  C  CA  . ASP   B  42  ? 2.0285 1.1002 1.7171 -0.0030 0.0436  0.0428  41  ASP   B CA  
2226  C  C   . ASP   B  42  ? 1.9818 1.0633 1.7152 0.0013  0.0684  0.0575  41  ASP   B C   
2227  O  O   . ASP   B  42  ? 1.9424 1.1758 1.8024 0.0657  0.0919  0.0274  41  ASP   B O   
2228  C  CB  . ASP   B  42  ? 2.0005 1.0838 1.7688 -0.0202 0.0213  0.0222  41  ASP   B CB  
2229  C  CG  . ASP   B  42  ? 2.0195 1.0797 1.8028 -0.0327 0.0192  0.0155  41  ASP   B CG  
2230  O  OD1 . ASP   B  42  ? 2.0262 1.0080 1.7437 -0.0975 0.0006  -0.0047 41  ASP   B OD1 
2231  O  OD2 . ASP   B  42  ? 2.0042 0.8177 1.8697 -0.0344 0.0228  -0.0639 41  ASP   B OD2 
2232  N  N   . GLY   B  43  ? 1.9735 0.9370 1.6522 -0.0565 0.0855  0.1059  42  GLY   B N   
2233  C  CA  . GLY   B  43  ? 1.9274 0.8817 1.6502 -0.1026 0.0783  0.1209  42  GLY   B CA  
2234  C  C   . GLY   B  43  ? 1.9163 0.7844 1.5599 -0.1406 0.0514  0.1648  42  GLY   B C   
2235  O  O   . GLY   B  43  ? 1.9523 0.8255 1.5527 -0.0710 0.0607  0.1554  42  GLY   B O   
2236  N  N   . ILE   B  44  ? 1.8747 0.7624 1.5559 -0.1914 0.0271  0.1547  43  ILE   B N   
2237  C  CA  . ILE   B  44  ? 1.8388 0.7755 1.5975 -0.1719 0.0122  0.1595  43  ILE   B CA  
2238  C  C   . ILE   B  44  ? 1.8213 0.9162 1.6475 -0.1802 0.0013  0.1297  43  ILE   B C   
2239  O  O   . ILE   B  44  ? 1.8306 1.0235 1.7460 -0.1335 0.0105  0.1812  43  ILE   B O   
2240  C  CB  . ILE   B  44  ? 1.8542 0.6745 1.5528 -0.1962 -0.0281 0.1779  43  ILE   B CB  
2241  C  CG1 . ILE   B  44  ? 1.9122 0.6822 1.5581 -0.1942 -0.0504 0.1698  43  ILE   B CG1 
2242  C  CG2 . ILE   B  44  ? 1.8169 0.6553 1.4926 -0.2119 -0.0320 0.2066  43  ILE   B CG2 
2243  C  CD1 . ILE   B  44  ? 1.9013 0.7701 1.5551 -0.2089 -0.0347 0.1570  43  ILE   B CD1 
2244  N  N   . VAL   B  45  ? 1.7756 0.9249 1.6269 -0.1777 0.0014  0.1127  44  VAL   B N   
2245  C  CA  . VAL   B  45  ? 1.7571 0.9308 1.6128 -0.2035 0.0062  0.1268  44  VAL   B CA  
2246  C  C   . VAL   B  45  ? 1.7335 0.8792 1.5662 -0.1976 -0.0399 0.1045  44  VAL   B C   
2247  O  O   . VAL   B  45  ? 1.7345 0.9421 1.5419 -0.1808 -0.0519 0.0702  44  VAL   B O   
2248  C  CB  . VAL   B  45  ? 1.7739 0.9880 1.5983 -0.2360 0.0189  0.1519  44  VAL   B CB  
2249  C  CG1 . VAL   B  45  ? 1.7697 1.0261 1.5911 -0.2301 0.0245  0.1390  44  VAL   B CG1 
2250  C  CG2 . VAL   B  45  ? 1.7953 1.0335 1.6267 -0.2267 0.0372  0.1466  44  VAL   B CG2 
2251  N  N   . LEU   B  46  ? 1.7424 0.8149 1.5667 -0.1954 -0.0279 0.1174  45  LEU   B N   
2252  C  CA  . LEU   B  46  ? 1.7625 0.7473 1.5533 -0.1882 -0.0354 0.1294  45  LEU   B CA  
2253  C  C   . LEU   B  46  ? 1.7938 0.7642 1.5095 -0.2103 -0.0275 0.1397  45  LEU   B C   
2254  O  O   . LEU   B  46  ? 1.8437 0.7432 1.4759 -0.1654 -0.0122 0.1686  45  LEU   B O   
2255  C  CB  . LEU   B  46  ? 1.7663 0.6897 1.5788 -0.1731 -0.0552 0.1159  45  LEU   B CB  
2256  C  CG  . LEU   B  46  ? 1.7864 0.6066 1.5957 -0.1516 -0.0697 0.0890  45  LEU   B CG  
2257  C  CD1 . LEU   B  46  ? 1.7919 0.6579 1.5726 -0.1650 -0.0792 0.1013  45  LEU   B CD1 
2258  C  CD2 . LEU   B  46  ? 1.8059 0.5332 1.5733 -0.1671 -0.0693 0.1038  45  LEU   B CD2 
2259  N  N   . ALA   B  47  ? 1.8108 0.7863 1.5179 -0.2010 -0.0068 0.1107  46  ALA   B N   
2260  C  CA  . ALA   B  47  ? 1.8252 0.8855 1.5295 -0.2465 -0.0015 0.0784  46  ALA   B CA  
2261  C  C   . ALA   B  47  ? 1.8191 0.8547 1.4974 -0.2554 -0.0306 0.0651  46  ALA   B C   
2262  O  O   . ALA   B  47  ? 1.8120 0.8369 1.4599 -0.2676 -0.0333 0.0445  46  ALA   B O   
2263  C  CB  . ALA   B  47  ? 1.8232 0.9015 1.5614 -0.2841 0.0435  0.0540  46  ALA   B CB  
2264  N  N   . ALA   B  48  ? 1.8559 0.8740 1.5012 -0.2714 -0.0419 0.0806  47  ALA   B N   
2265  C  CA  . ALA   B  48  ? 1.8549 0.8419 1.5119 -0.2682 -0.0367 0.0964  47  ALA   B CA  
2266  C  C   . ALA   B  48  ? 1.8621 0.9637 1.5221 -0.2337 -0.1099 0.0950  47  ALA   B C   
2267  O  O   . ALA   B  48  ? 1.9172 0.9169 1.4038 -0.1832 -0.1445 0.0801  47  ALA   B O   
2268  C  CB  . ALA   B  48  ? 1.8569 0.7952 1.5291 -0.2558 -0.0532 0.0990  47  ALA   B CB  
2269  N  N   . GLU   B  49  ? 1.9463 1.0058 1.5923 -0.2306 -0.0910 0.0446  48  GLU   B N   
2270  C  CA  . GLU   B  49  ? 1.9636 1.1807 1.6739 -0.3277 -0.1399 0.0278  48  GLU   B CA  
2271  C  C   . GLU   B  49  ? 2.0085 1.2657 1.7051 -0.3147 -0.1053 0.0600  48  GLU   B C   
2272  O  O   . GLU   B  49  ? 1.9834 1.3557 1.6810 -0.3425 -0.1613 0.0598  48  GLU   B O   
2273  C  CB  . GLU   B  49  ? 2.0204 1.1850 1.7304 -0.2954 -0.1422 0.0047  48  GLU   B CB  
2274  C  CG  . GLU   B  49  ? 2.0744 1.2322 1.7727 -0.2912 -0.1484 -0.0647 48  GLU   B CG  
2275  C  CD  . GLU   B  49  ? 2.1179 1.1928 1.8446 -0.3360 -0.1293 -0.1239 48  GLU   B CD  
2276  O  OE1 . GLU   B  49  ? 2.0822 1.2429 1.9183 -0.2945 -0.1102 -0.1425 48  GLU   B OE1 
2277  O  OE2 . GLU   B  49  ? 2.1956 1.2809 1.8077 -0.3701 -0.1399 -0.1996 48  GLU   B OE2 
2278  N  N   . ARG   B  50  ? 2.0060 1.3364 1.8160 -0.2269 -0.1097 0.0811  49  ARG   B N   
2279  C  CA  . ARG   B  50  ? 2.0581 1.5238 1.8108 -0.1355 -0.0861 0.0756  49  ARG   B CA  
2280  C  C   . ARG   B  50  ? 2.1194 1.6026 1.7767 -0.1459 -0.0754 0.0181  49  ARG   B C   
2281  O  O   . ARG   B  50  ? 2.0002 1.7284 1.6357 -0.2023 0.0113  0.0474  49  ARG   B O   
2282  C  CB  . ARG   B  50  ? 2.0712 1.5563 1.9599 -0.0447 -0.0732 0.0688  49  ARG   B CB  
2283  C  CG  . ARG   B  50  ? 2.1449 1.5524 2.0740 -0.0062 -0.0445 0.0951  49  ARG   B CG  
2284  C  CD  . ARG   B  50  ? 2.1610 1.5071 2.1831 0.0401  -0.0292 0.1389  49  ARG   B CD  
2285  N  NE  . ARG   B  50  ? 2.1804 1.4492 2.1995 0.0653  0.0088  0.2752  49  ARG   B NE  
2286  C  CZ  . ARG   B  50  ? 2.1677 1.5005 2.1666 0.1585  0.0220  0.3287  49  ARG   B CZ  
2287  N  NH1 . ARG   B  50  ? 2.1804 1.4072 2.1526 0.2098  0.0198  0.3300  49  ARG   B NH1 
2288  N  NH2 . ARG   B  50  ? 2.1610 1.5246 2.1901 0.2189  0.0059  0.3531  49  ARG   B NH2 
2289  N  N   . LYS   B  51  ? 2.1500 1.8259 1.7900 -0.1435 -0.0584 -0.0301 50  LYS   B N   
2290  C  CA  . LYS   B  51  ? 2.1865 1.8064 1.9659 -0.1566 -0.1179 -0.1026 50  LYS   B CA  
2291  C  C   . LYS   B  51  ? 2.2925 1.7934 2.1732 -0.3191 -0.1240 -0.2308 50  LYS   B C   
2292  O  O   . LYS   B  51  ? 2.2814 1.7216 2.2983 -0.3446 -0.1618 -0.2475 50  LYS   B O   
2293  C  CB  . LYS   B  51  ? 2.0803 1.8386 1.9411 -0.0905 -0.1948 -0.0436 50  LYS   B CB  
2294  C  CG  . LYS   B  51  ? 1.9663 1.8271 1.8694 -0.1027 -0.2373 0.0190  50  LYS   B CG  
2295  C  CD  . LYS   B  51  ? 1.9006 1.7092 1.8967 -0.1067 -0.2097 0.0267  50  LYS   B CD  
2296  C  CE  . LYS   B  51  ? 1.9305 1.6857 1.8393 -0.0905 -0.1992 0.0584  50  LYS   B CE  
2297  N  NZ  . LYS   B  51  ? 1.9063 1.6686 1.8516 -0.0885 -0.1725 0.0851  50  LYS   B NZ  
2298  N  N   . VAL   B  52  ? 2.4110 1.7884 2.2150 -0.3053 -0.0828 -0.2763 51  VAL   B N   
2299  C  CA  . VAL   B  52  ? 2.4180 1.7253 2.1693 -0.2868 -0.0236 -0.3272 51  VAL   B CA  
2300  C  C   . VAL   B  52  ? 2.3459 1.7418 2.1793 -0.2521 -0.0117 -0.3366 51  VAL   B C   
2301  O  O   . VAL   B  52  ? 2.4689 1.6048 2.1017 -0.2434 -0.0477 -0.3547 51  VAL   B O   
2302  C  CB  . VAL   B  52  ? 2.4752 1.6905 2.1211 -0.3384 0.0527  -0.3041 51  VAL   B CB  
2303  C  CG1 . VAL   B  52  ? 2.5002 1.5815 2.1035 -0.3932 0.1313  -0.3335 51  VAL   B CG1 
2304  C  CG2 . VAL   B  52  ? 2.4933 1.5993 2.0838 -0.3608 0.0963  -0.2866 51  VAL   B CG2 
2305  N  N   . THR   B  53  ? 2.2360 1.5723 2.2258 -0.2006 -0.1881 -0.2226 52  THR   B N   
2306  C  CA  . THR   B  53  ? 2.2282 1.5165 2.2244 -0.2774 -0.2216 -0.1727 52  THR   B CA  
2307  C  C   . THR   B  53  ? 2.1637 1.5017 2.1763 -0.2915 -0.2472 -0.0789 52  THR   B C   
2308  O  O   . THR   B  53  ? 2.2150 1.4981 2.2408 -0.2240 -0.2554 -0.0377 52  THR   B O   
2309  C  CB  . THR   B  53  ? 2.2604 1.5920 2.2795 -0.2149 -0.2038 -0.1543 52  THR   B CB  
2310  O  OG1 . THR   B  53  ? 2.2403 1.6148 2.3227 -0.2701 -0.2181 -0.1036 52  THR   B OG1 
2311  C  CG2 . THR   B  53  ? 2.2661 1.5901 2.2786 -0.2566 -0.2123 -0.1996 52  THR   B CG2 
2312  N  N   . SER   B  54  ? 2.0783 1.2786 2.1666 -0.4501 -0.2038 -0.0895 53  SER   B N   
2313  C  CA  . SER   B  54  ? 2.0113 1.2579 2.1195 -0.4561 -0.1669 -0.0458 53  SER   B CA  
2314  C  C   . SER   B  54  ? 1.9520 1.1994 2.1559 -0.4911 -0.1874 -0.0060 53  SER   B C   
2315  O  O   . SER   B  54  ? 1.8538 1.0191 2.1929 -0.5140 -0.1748 0.1847  53  SER   B O   
2316  C  CB  . SER   B  54  ? 2.0213 1.1350 2.0462 -0.5012 -0.2228 -0.1026 53  SER   B CB  
2317  O  OG  . SER   B  54  ? 2.1224 1.0850 1.9537 -0.4739 -0.2297 -0.1176 53  SER   B OG  
2318  N  N   . THR   B  55  ? 1.7810 1.4494 2.1354 -0.4296 -0.1512 -0.0049 54  THR   B N   
2319  C  CA  . THR   B  55  ? 1.7338 1.5602 2.0914 -0.4735 -0.1412 -0.0363 54  THR   B CA  
2320  C  C   . THR   B  55  ? 1.7066 1.6433 2.0147 -0.4405 -0.1011 0.0113  54  THR   B C   
2321  O  O   . THR   B  55  ? 1.6209 1.7322 2.0164 -0.4838 -0.0306 0.0195  54  THR   B O   
2322  C  CB  . THR   B  55  ? 1.6705 1.6167 2.0956 -0.4465 -0.1513 -0.1134 54  THR   B CB  
2323  O  OG1 . THR   B  55  ? 1.5892 1.5704 2.1512 -0.5202 -0.1785 -0.1673 54  THR   B OG1 
2324  C  CG2 . THR   B  55  ? 1.6567 1.6659 2.0931 -0.4735 -0.1731 -0.1525 54  THR   B CG2 
2325  N  N   . LEU   B  56  ? 1.7645 1.6866 1.9428 -0.4492 -0.1324 -0.0002 55  LEU   B N   
2326  C  CA  . LEU   B  56  ? 1.7555 1.6950 1.9147 -0.3958 -0.1458 -0.0116 55  LEU   B CA  
2327  C  C   . LEU   B  56  ? 1.7478 1.5610 1.8761 -0.3328 -0.1040 0.0114  55  LEU   B C   
2328  O  O   . LEU   B  56  ? 1.6442 1.5828 1.7390 -0.3026 -0.1438 -0.0040 55  LEU   B O   
2329  C  CB  . LEU   B  56  ? 1.7763 1.7073 1.8976 -0.4114 -0.1639 0.0108  55  LEU   B CB  
2330  C  CG  . LEU   B  56  ? 1.8199 1.7690 1.8929 -0.3924 -0.1839 0.0217  55  LEU   B CG  
2331  C  CD1 . LEU   B  56  ? 1.8044 1.8789 1.9457 -0.3993 -0.1545 -0.0041 55  LEU   B CD1 
2332  C  CD2 . LEU   B  56  ? 1.8454 1.7914 1.8737 -0.4046 -0.1742 0.0323  55  LEU   B CD2 
2333  N  N   . LEU   B  57  ? 1.7672 1.5866 1.8984 -0.2761 -0.1127 -0.0245 56  LEU   B N   
2334  C  CA  . LEU   B  57  ? 1.7300 1.4722 1.9839 -0.2481 -0.0481 -0.0172 56  LEU   B CA  
2335  C  C   . LEU   B  57  ? 1.7552 1.4523 1.9923 -0.2239 -0.0552 0.0012  56  LEU   B C   
2336  O  O   . LEU   B  57  ? 1.6502 1.4575 2.0752 -0.1671 -0.0418 -0.0789 56  LEU   B O   
2337  C  CB  . LEU   B  57  ? 1.6782 1.5117 2.0639 -0.2118 -0.0413 -0.0148 56  LEU   B CB  
2338  C  CG  . LEU   B  57  ? 1.5865 1.5073 2.1083 -0.1794 0.0143  0.0091  56  LEU   B CG  
2339  C  CD1 . LEU   B  57  ? 1.6052 1.5298 2.0926 -0.1535 0.0180  0.0166  56  LEU   B CD1 
2340  C  CD2 . LEU   B  57  ? 1.5525 1.4988 2.1224 -0.1699 0.0031  0.0147  56  LEU   B CD2 
2341  N  N   . GLU   B  58  ? 1.7744 1.4363 1.9617 -0.1877 -0.0264 0.0053  57  GLU   B N   
2342  C  CA  . GLU   B  58  ? 1.8143 1.4136 2.0024 -0.1968 -0.0349 -0.0215 57  GLU   B CA  
2343  C  C   . GLU   B  58  ? 1.8923 1.2706 1.9935 -0.1832 -0.0559 0.0496  57  GLU   B C   
2344  O  O   . GLU   B  58  ? 1.9486 1.0545 1.8532 -0.2340 -0.0404 0.0954  57  GLU   B O   
2345  C  CB  . GLU   B  58  ? 1.8429 1.3468 1.9881 -0.2303 -0.0058 -0.1052 57  GLU   B CB  
2346  C  CG  . GLU   B  58  ? 1.9458 1.4045 2.0366 -0.2333 0.0562  -0.2151 57  GLU   B CG  
2347  C  CD  . GLU   B  58  ? 1.9806 1.4370 2.0999 -0.2723 0.0509  -0.3136 57  GLU   B CD  
2348  O  OE1 . GLU   B  58  ? 2.1349 1.4719 2.1362 -0.3025 0.1436  -0.3713 57  GLU   B OE1 
2349  O  OE2 . GLU   B  58  ? 2.0899 1.3087 2.0304 -0.2698 0.0985  -0.4183 57  GLU   B OE2 
2350  N  N   . GLN   B  59  ? 1.9453 1.3985 2.0289 -0.1649 -0.0202 0.0719  58  GLN   B N   
2351  C  CA  . GLN   B  59  ? 2.0998 1.5622 2.0724 -0.1412 -0.0839 0.0829  58  GLN   B CA  
2352  C  C   . GLN   B  59  ? 2.1190 1.4939 2.1503 -0.1092 -0.0409 0.1223  58  GLN   B C   
2353  O  O   . GLN   B  59  ? 2.0892 1.5845 2.2044 -0.2022 -0.0313 0.1789  58  GLN   B O   
2354  C  CB  . GLN   B  59  ? 2.1941 1.5941 2.1647 -0.1638 -0.0703 0.1321  58  GLN   B CB  
2355  C  CG  . GLN   B  59  ? 2.2969 1.5610 2.3647 -0.1190 -0.1183 0.1844  58  GLN   B CG  
2356  C  CD  . GLN   B  59  ? 2.3505 1.5453 2.3914 -0.1296 -0.1961 0.1762  58  GLN   B CD  
2357  O  OE1 . GLN   B  59  ? 2.3907 1.4402 2.5571 -0.0740 -0.3603 0.2854  58  GLN   B OE1 
2358  N  NE2 . GLN   B  59  ? 2.3542 1.6728 2.5737 -0.1552 -0.1660 0.2390  58  GLN   B NE2 
2359  N  N   . ASP   B  60  ? 2.1030 1.6433 2.1256 -0.0737 -0.1255 0.1613  59  ASP   B N   
2360  C  CA  . ASP   B  60  ? 2.0626 1.7628 2.1309 0.0007  -0.0901 0.0967  59  ASP   B CA  
2361  C  C   . ASP   B  60  ? 2.0904 1.7196 2.1100 -0.0078 -0.0814 0.0570  59  ASP   B C   
2362  O  O   . ASP   B  60  ? 2.0982 1.5041 2.1755 -0.0287 -0.0554 0.0337  59  ASP   B O   
2363  C  CB  . ASP   B  60  ? 2.0662 1.9653 2.1501 0.0653  -0.0598 0.0300  59  ASP   B CB  
2364  C  CG  . ASP   B  60  ? 2.0484 2.1016 2.1584 0.1392  -0.0682 -0.0243 59  ASP   B CG  
2365  O  OD1 . ASP   B  60  ? 2.0944 2.2718 2.2004 0.1184  -0.0330 -0.0799 59  ASP   B OD1 
2366  O  OD2 . ASP   B  60  ? 2.0453 2.1559 2.1746 0.2627  0.0629  -0.1073 59  ASP   B OD2 
2367  N  N   . THR   B  61  ? 2.0483 1.7024 2.1326 -0.0703 -0.0446 0.0646  60  THR   B N   
2368  C  CA  . THR   B  61  ? 2.0898 1.5965 2.1623 -0.0431 -0.0296 0.0587  60  THR   B CA  
2369  C  C   . THR   B  61  ? 2.0623 1.6128 2.1907 -0.0737 -0.0057 0.0464  60  THR   B C   
2370  O  O   . THR   B  61  ? 1.9825 1.1904 2.2767 -0.1437 -0.0842 -0.0263 60  THR   B O   
2371  C  CB  . THR   B  61  ? 2.0782 1.5694 2.1928 -0.0680 -0.0087 0.1104  60  THR   B CB  
2372  O  OG1 . THR   B  61  ? 2.1389 1.5242 2.2356 -0.0531 -0.0111 0.1163  60  THR   B OG1 
2373  C  CG2 . THR   B  61  ? 2.0365 1.6574 2.1754 -0.0859 0.0243  0.1216  60  THR   B CG2 
2374  N  N   . SER   B  62  ? 2.1108 1.7659 2.2015 -0.0117 -0.0027 0.1154  61  SER   B N   
2375  C  CA  . SER   B  62  ? 2.0529 1.8978 2.1923 -0.0241 0.0345  0.0530  61  SER   B CA  
2376  C  C   . SER   B  62  ? 2.0027 1.8207 2.2316 -0.1159 0.0469  -0.0052 61  SER   B C   
2377  O  O   . SER   B  62  ? 2.0595 1.9558 2.1577 -0.1700 0.0177  -0.0175 61  SER   B O   
2378  C  CB  . SER   B  62  ? 2.0301 1.8790 2.2160 0.0264  0.1395  0.0690  61  SER   B CB  
2379  O  OG  . SER   B  62  ? 2.0412 1.9794 2.1789 0.0544  0.3278  0.0506  61  SER   B OG  
2380  N  N   . THR   B  63  ? 1.9665 1.6023 2.1708 -0.1363 -0.0939 -0.0777 62  THR   B N   
2381  C  CA  . THR   B  63  ? 2.0808 1.3578 2.0714 -0.0651 -0.1052 -0.0971 62  THR   B CA  
2382  C  C   . THR   B  63  ? 2.0724 1.2142 2.0993 -0.0508 -0.1927 -0.0604 62  THR   B C   
2383  O  O   . THR   B  63  ? 2.0329 1.2469 2.1704 -0.0383 -0.1121 -0.1480 62  THR   B O   
2384  C  CB  . THR   B  63  ? 2.1371 1.2935 1.9064 0.0582  -0.1576 -0.0906 62  THR   B CB  
2385  O  OG1 . THR   B  63  ? 2.2577 0.9472 1.8007 0.0429  -0.1433 -0.0910 62  THR   B OG1 
2386  C  CG2 . THR   B  63  ? 2.1664 1.2601 1.8721 0.0909  -0.1456 -0.0797 62  THR   B CG2 
2387  N  N   . GLU   B  64  ? 2.0672 1.1523 1.9947 -0.1978 -0.1249 -0.0238 63  GLU   B N   
2388  C  CA  . GLU   B  64  ? 2.0402 1.2604 1.9185 -0.1751 -0.1409 -0.0086 63  GLU   B CA  
2389  C  C   . GLU   B  64  ? 1.9984 1.2384 1.7885 -0.2556 -0.0718 -0.0568 63  GLU   B C   
2390  O  O   . GLU   B  64  ? 1.9704 1.3449 1.8079 -0.2236 -0.1773 -0.1092 63  GLU   B O   
2391  C  CB  . GLU   B  64  ? 2.1423 1.3224 2.0468 -0.2697 -0.1287 -0.0149 63  GLU   B CB  
2392  C  CG  . GLU   B  64  ? 2.1880 1.3337 2.1542 -0.2477 -0.1155 -0.0272 63  GLU   B CG  
2393  C  CD  . GLU   B  64  ? 2.2512 1.3414 2.2046 -0.2579 -0.1672 -0.0235 63  GLU   B CD  
2394  O  OE1 . GLU   B  64  ? 2.3215 1.4421 2.2415 -0.1893 -0.1421 0.0667  63  GLU   B OE1 
2395  O  OE2 . GLU   B  64  ? 2.3420 1.4903 2.1190 -0.3332 -0.2651 -0.1032 63  GLU   B OE2 
2396  N  N   . LYS   B  65  ? 1.9247 1.0672 1.7243 -0.2328 -0.1299 -0.0483 64  LYS   B N   
2397  C  CA  . LYS   B  65  ? 1.9078 0.8388 1.7161 -0.1862 -0.1027 -0.0848 64  LYS   B CA  
2398  C  C   . LYS   B  65  ? 1.7448 0.5543 1.7630 -0.1709 -0.0927 0.0564  64  LYS   B C   
2399  O  O   . LYS   B  65  ? 1.7740 0.3159 1.7573 -0.2457 -0.1045 0.0580  64  LYS   B O   
2400  C  CB  . LYS   B  65  ? 1.9501 0.8443 1.7623 -0.1910 -0.0640 -0.1118 64  LYS   B CB  
2401  C  CG  . LYS   B  65  ? 1.9798 0.9166 1.7929 -0.1617 -0.1037 -0.1949 64  LYS   B CG  
2402  C  CD  . LYS   B  65  ? 1.9737 0.8509 1.7816 -0.1385 -0.0707 -0.2817 64  LYS   B CD  
2403  C  CE  . LYS   B  65  ? 1.9447 0.8625 1.7767 -0.1207 -0.0838 -0.2845 64  LYS   B CE  
2404  N  NZ  . LYS   B  65  ? 1.9752 0.8108 1.7389 -0.1148 -0.0944 -0.2720 64  LYS   B NZ  
2405  N  N   . LEU   B  66  ? 1.7795 0.4445 1.6786 -0.1821 -0.1046 0.0374  65  LEU   B N   
2406  C  CA  . LEU   B  66  ? 1.7361 0.5922 1.5570 -0.1529 -0.1164 0.0232  65  LEU   B CA  
2407  C  C   . LEU   B  66  ? 1.7266 0.6117 1.5195 -0.1465 -0.1573 0.0355  65  LEU   B C   
2408  O  O   . LEU   B  66  ? 1.7116 0.6494 1.5809 -0.1073 -0.1662 0.0260  65  LEU   B O   
2409  C  CB  . LEU   B  66  ? 1.7798 0.5248 1.4760 -0.1495 -0.0915 0.0002  65  LEU   B CB  
2410  C  CG  . LEU   B  66  ? 1.7955 0.4323 1.4710 -0.1398 -0.0648 -0.0322 65  LEU   B CG  
2411  C  CD1 . LEU   B  66  ? 1.8005 0.4448 1.4760 -0.1334 -0.0602 -0.0452 65  LEU   B CD1 
2412  C  CD2 . LEU   B  66  ? 1.8007 0.4838 1.4945 -0.1311 -0.0524 -0.0368 65  LEU   B CD2 
2413  N  N   . TYR   B  67  ? 1.7075 0.6016 1.4462 -0.1114 -0.2146 0.0895  66  TYR   B N   
2414  C  CA  . TYR   B  67  ? 1.7127 0.5918 1.3840 -0.0057 -0.2507 0.1395  66  TYR   B CA  
2415  C  C   . TYR   B  67  ? 1.7149 0.5578 1.3813 -0.0106 -0.2464 0.1485  66  TYR   B C   
2416  O  O   . TYR   B  67  ? 1.7469 0.2795 1.3793 0.0011  -0.2529 0.0909  66  TYR   B O   
2417  C  CB  . TYR   B  67  ? 1.7126 0.5784 1.3131 0.0033  -0.2726 0.2079  66  TYR   B CB  
2418  C  CG  . TYR   B  67  ? 1.7187 0.7079 1.2536 -0.0371 -0.3031 0.2268  66  TYR   B CG  
2419  C  CD1 . TYR   B  67  ? 1.7438 0.7367 1.2618 -0.0214 -0.3283 0.1594  66  TYR   B CD1 
2420  C  CD2 . TYR   B  67  ? 1.7191 0.6969 1.2556 -0.0402 -0.3124 0.2217  66  TYR   B CD2 
2421  C  CE1 . TYR   B  67  ? 1.7938 0.9345 1.1968 -0.0392 -0.3753 0.1655  66  TYR   B CE1 
2422  C  CE2 . TYR   B  67  ? 1.7557 0.8047 1.2252 -0.0658 -0.3442 0.2254  66  TYR   B CE2 
2423  C  CZ  . TYR   B  67  ? 1.8028 0.8497 1.2506 -0.0102 -0.3479 0.2047  66  TYR   B CZ  
2424  O  OH  . TYR   B  67  ? 1.8882 1.1384 1.1247 -0.0088 -0.3623 0.2285  66  TYR   B OH  
2425  N  N   . LYS   B  68  ? 1.6923 0.5712 1.3827 0.0166  -0.2054 0.1221  67  LYS   B N   
2426  C  CA  . LYS   B  68  ? 1.6925 0.6257 1.3698 0.0112  -0.1572 0.0975  67  LYS   B CA  
2427  C  C   . LYS   B  68  ? 1.7080 0.5090 1.3658 0.0224  -0.1972 0.0822  67  LYS   B C   
2428  O  O   . LYS   B  68  ? 1.7542 0.3659 1.3527 0.0323  -0.1977 0.0312  67  LYS   B O   
2429  C  CB  . LYS   B  68  ? 1.6634 0.6787 1.4233 0.0170  -0.1118 0.0977  67  LYS   B CB  
2430  C  CG  . LYS   B  68  ? 1.6734 0.8006 1.4176 0.0010  -0.0761 0.0677  67  LYS   B CG  
2431  C  CD  . LYS   B  68  ? 1.6312 0.9768 1.4711 0.0007  -0.0587 0.0663  67  LYS   B CD  
2432  C  CE  . LYS   B  68  ? 1.6195 1.0151 1.5186 -0.0068 -0.0320 0.0551  67  LYS   B CE  
2433  N  NZ  . LYS   B  68  ? 1.6113 1.0932 1.5735 0.0097  0.0047  0.0583  67  LYS   B NZ  
2434  N  N   . LEU   B  69  ? 1.7190 0.5320 1.3205 0.0318  -0.1854 0.1145  68  LEU   B N   
2435  C  CA  . LEU   B  69  ? 1.6937 0.6829 1.3171 0.0080  -0.1921 0.1506  68  LEU   B CA  
2436  C  C   . LEU   B  69  ? 1.7281 0.7143 1.3562 0.0116  -0.2119 0.1106  68  LEU   B C   
2437  O  O   . LEU   B  69  ? 1.6821 0.8200 1.4267 -0.0440 -0.2208 0.1528  68  LEU   B O   
2438  C  CB  . LEU   B  69  ? 1.6781 0.7391 1.2593 -0.0180 -0.1983 0.1325  68  LEU   B CB  
2439  C  CG  . LEU   B  69  ? 1.6775 0.7705 1.2440 -0.0335 -0.1947 0.0891  68  LEU   B CG  
2440  C  CD1 . LEU   B  69  ? 1.6901 0.7853 1.1991 -0.0607 -0.2116 0.0970  68  LEU   B CD1 
2441  C  CD2 . LEU   B  69  ? 1.6789 0.8176 1.2522 -0.0426 -0.1677 0.0817  68  LEU   B CD2 
2442  N  N   . ASN   B  70  ? 1.7594 0.7040 1.3441 -0.0309 -0.1945 0.1675  69  ASN   B N   
2443  C  CA  . ASN   B  70  ? 1.7884 0.6260 1.4634 -0.0643 -0.2047 0.1833  69  ASN   B CA  
2444  C  C   . ASN   B  70  ? 1.8098 0.7421 1.5119 -0.0106 -0.1511 0.2003  69  ASN   B C   
2445  O  O   . ASN   B  70  ? 1.7111 0.8021 1.5230 -0.0594 -0.1684 0.2210  69  ASN   B O   
2446  C  CB  . ASN   B  70  ? 1.8415 0.4828 1.5615 -0.0648 -0.1964 0.1587  69  ASN   B CB  
2447  C  CG  . ASN   B  70  ? 1.8775 0.3664 1.5728 -0.1175 -0.2191 0.1427  69  ASN   B CG  
2448  O  OD1 . ASN   B  70  ? 1.8875 0.4581 1.6650 -0.1878 -0.2057 0.1983  69  ASN   B OD1 
2449  N  ND2 . ASN   B  70  ? 1.9539 0.2420 1.6313 -0.1294 -0.1936 0.1057  69  ASN   B ND2 
2450  N  N   . ASP   B  71  ? 1.8780 0.7184 1.5683 -0.0115 -0.0991 0.2129  70  ASP   B N   
2451  C  CA  . ASP   B  71  ? 1.9044 0.8098 1.6173 -0.0195 -0.0753 0.2047  70  ASP   B CA  
2452  C  C   . ASP   B  71  ? 1.8634 0.8263 1.5415 -0.0527 -0.0728 0.1581  70  ASP   B C   
2453  O  O   . ASP   B  71  ? 1.9154 0.9633 1.5917 -0.1407 -0.0377 0.1334  70  ASP   B O   
2454  C  CB  . ASP   B  71  ? 1.9688 0.8252 1.7015 0.0382  -0.0876 0.2272  70  ASP   B CB  
2455  C  CG  . ASP   B  71  ? 2.0167 0.9548 1.7668 0.1127  -0.0968 0.2819  70  ASP   B CG  
2456  O  OD1 . ASP   B  71  ? 2.0162 0.8198 1.8836 0.0022  -0.1164 0.3505  70  ASP   B OD1 
2457  O  OD2 . ASP   B  71  ? 2.1332 0.9576 1.8034 0.1269  -0.0904 0.2342  70  ASP   B OD2 
2458  N  N   . LYS   B  72  ? 1.8684 0.7488 1.4356 -0.0239 -0.0536 0.1319  71  LYS   B N   
2459  C  CA  . LYS   B  72  ? 1.8671 0.7423 1.4201 -0.0532 -0.0341 0.1399  71  LYS   B CA  
2460  C  C   . LYS   B  72  ? 1.7933 0.7196 1.2985 -0.0815 -0.0522 0.1946  71  LYS   B C   
2461  O  O   . LYS   B  72  ? 1.7690 0.7938 1.2593 -0.0845 -0.1254 0.1806  71  LYS   B O   
2462  C  CB  . LYS   B  72  ? 1.9160 0.7580 1.4051 -0.0249 -0.0425 0.1082  71  LYS   B CB  
2463  C  CG  . LYS   B  72  ? 2.0231 0.7944 1.4956 -0.0063 -0.0119 0.0484  71  LYS   B CG  
2464  C  CD  . LYS   B  72  ? 2.0669 0.8499 1.5435 -0.0532 0.0241  0.0196  71  LYS   B CD  
2465  C  CE  . LYS   B  72  ? 2.1237 0.8186 1.6275 -0.0885 0.0183  -0.0522 71  LYS   B CE  
2466  N  NZ  . LYS   B  72  ? 2.2080 0.8065 1.6950 -0.1237 0.0245  -0.0937 71  LYS   B NZ  
2467  N  N   . ILE   B  73  ? 1.7351 0.6651 1.3203 -0.0827 -0.0352 0.1926  72  ILE   B N   
2468  C  CA  . ILE   B  73  ? 1.7148 0.6128 1.3254 -0.1018 -0.0810 0.1985  72  ILE   B CA  
2469  C  C   . ILE   B  73  ? 1.6943 0.6087 1.3536 -0.0862 -0.0835 0.1698  72  ILE   B C   
2470  O  O   . ILE   B  73  ? 1.6856 0.4758 1.3787 -0.1061 -0.0819 0.1402  72  ILE   B O   
2471  C  CB  . ILE   B  73  ? 1.7133 0.5925 1.3073 -0.1115 -0.1193 0.1880  72  ILE   B CB  
2472  C  CG1 . ILE   B  73  ? 1.7621 0.6128 1.2815 -0.0930 -0.1204 0.1845  72  ILE   B CG1 
2473  C  CG2 . ILE   B  73  ? 1.7091 0.5896 1.3053 -0.1272 -0.1076 0.1822  72  ILE   B CG2 
2474  C  CD1 . ILE   B  73  ? 1.7549 0.6685 1.2798 -0.1103 -0.1340 0.1795  72  ILE   B CD1 
2475  N  N   . ALA   B  74  ? 1.7005 0.6099 1.3047 -0.0751 -0.0862 0.1564  73  ALA   B N   
2476  C  CA  . ALA   B  74  ? 1.6986 0.6166 1.3051 -0.0519 -0.0775 0.1394  73  ALA   B CA  
2477  C  C   . ALA   B  74  ? 1.7352 0.5777 1.2812 -0.0586 -0.0976 0.1402  73  ALA   B C   
2478  O  O   . ALA   B  74  ? 1.7706 0.4383 1.2551 -0.0439 -0.0848 0.1137  73  ALA   B O   
2479  C  CB  . ALA   B  74  ? 1.7045 0.6170 1.3157 -0.0684 -0.0650 0.1246  73  ALA   B CB  
2480  N  N   . VAL   B  75  ? 1.7320 0.6329 1.2556 -0.0620 -0.1174 0.1494  74  VAL   B N   
2481  C  CA  . VAL   B  75  ? 1.7137 0.6566 1.3105 -0.0525 -0.1046 0.1761  74  VAL   B CA  
2482  C  C   . VAL   B  75  ? 1.7551 0.6767 1.3793 -0.0909 -0.0976 0.1716  74  VAL   B C   
2483  O  O   . VAL   B  75  ? 1.7877 0.6219 1.3932 -0.0184 -0.0524 0.2752  74  VAL   B O   
2484  C  CB  . VAL   B  75  ? 1.6768 0.6900 1.3017 -0.0740 -0.1328 0.1626  74  VAL   B CB  
2485  C  CG1 . VAL   B  75  ? 1.6693 0.6793 1.3134 -0.0864 -0.1131 0.1539  74  VAL   B CG1 
2486  C  CG2 . VAL   B  75  ? 1.6601 0.7206 1.3013 -0.0540 -0.1397 0.1591  74  VAL   B CG2 
2487  N  N   . ALA   B  76  ? 1.7970 0.6490 1.4421 -0.1272 -0.0614 0.1667  75  ALA   B N   
2488  C  CA  . ALA   B  76  ? 1.7720 0.6837 1.4813 -0.1842 -0.0381 0.1536  75  ALA   B CA  
2489  C  C   . ALA   B  76  ? 1.7624 0.6962 1.4546 -0.2071 -0.0366 0.1468  75  ALA   B C   
2490  O  O   . ALA   B  76  ? 1.7154 0.6783 1.5249 -0.2368 -0.0004 0.1623  75  ALA   B O   
2491  C  CB  . ALA   B  76  ? 1.7838 0.7343 1.4839 -0.2232 -0.0314 0.1599  75  ALA   B CB  
2492  N  N   . VAL   B  77  ? 1.6767 0.7112 1.4434 -0.1952 -0.0346 0.1453  76  VAL   B N   
2493  C  CA  . VAL   B  77  ? 1.6486 0.6749 1.4160 -0.1803 -0.0744 0.1159  76  VAL   B CA  
2494  C  C   . VAL   B  77  ? 1.6200 0.6555 1.3985 -0.1504 -0.0999 0.1649  76  VAL   B C   
2495  O  O   . VAL   B  77  ? 1.6243 0.6754 1.4017 -0.1652 -0.1107 0.2108  76  VAL   B O   
2496  C  CB  . VAL   B  77  ? 1.6179 0.6861 1.3757 -0.1826 -0.0693 0.0804  76  VAL   B CB  
2497  C  CG1 . VAL   B  77  ? 1.6275 0.7386 1.3675 -0.1995 -0.0681 0.0587  76  VAL   B CG1 
2498  C  CG2 . VAL   B  77  ? 1.5951 0.6737 1.4026 -0.1505 -0.0603 0.0835  76  VAL   B CG2 
2499  N  N   . ALA   B  78  ? 1.6707 0.5439 1.3960 -0.1232 -0.1233 0.1683  77  ALA   B N   
2500  C  CA  . ALA   B  78  ? 1.6720 0.5582 1.4359 -0.1417 -0.1143 0.1271  77  ALA   B CA  
2501  C  C   . ALA   B  78  ? 1.6670 0.4425 1.3405 -0.1263 -0.1494 0.1222  77  ALA   B C   
2502  O  O   . ALA   B  78  ? 1.6382 0.4970 1.3094 -0.1174 -0.1229 0.1109  77  ALA   B O   
2503  C  CB  . ALA   B  78  ? 1.7284 0.5567 1.4580 -0.1511 -0.1121 0.1350  77  ALA   B CB  
2504  N  N   . GLY   B  79  ? 1.6373 0.4191 1.3514 -0.1430 -0.1941 0.1292  78  GLY   B N   
2505  C  CA  . GLY   B  79  ? 1.6072 0.5093 1.3561 -0.1650 -0.2138 0.1064  78  GLY   B CA  
2506  C  C   . GLY   B  79  ? 1.5413 0.5934 1.3523 -0.1688 -0.2810 0.0574  78  GLY   B C   
2507  O  O   . GLY   B  79  ? 1.5360 0.6408 1.4014 -0.2139 -0.2810 0.0333  78  GLY   B O   
2508  N  N   . LEU   B  80  ? 1.4909 0.6436 1.3600 -0.1891 -0.2792 -0.0049 79  LEU   B N   
2509  C  CA  . LEU   B  80  ? 1.4600 0.6944 1.3563 -0.2127 -0.2900 0.0070  79  LEU   B CA  
2510  C  C   . LEU   B  80  ? 1.4450 0.6943 1.3360 -0.2399 -0.2587 -0.0033 79  LEU   B C   
2511  O  O   . LEU   B  80  ? 1.4002 0.7366 1.2664 -0.2365 -0.2673 0.0278  79  LEU   B O   
2512  C  CB  . LEU   B  80  ? 1.4513 0.7044 1.3507 -0.1849 -0.2954 0.0172  79  LEU   B CB  
2513  C  CG  . LEU   B  80  ? 1.5014 0.7498 1.4042 -0.1424 -0.3071 -0.0028 79  LEU   B CG  
2514  C  CD1 . LEU   B  80  ? 1.4790 0.8252 1.4292 -0.1645 -0.3388 -0.0405 79  LEU   B CD1 
2515  C  CD2 . LEU   B  80  ? 1.5070 0.7953 1.4431 -0.1418 -0.3313 -0.0303 79  LEU   B CD2 
2516  N  N   . THR   B  81  ? 1.4063 0.7698 1.4144 -0.2804 -0.2479 -0.0298 80  THR   B N   
2517  C  CA  . THR   B  81  ? 1.4548 0.8192 1.4768 -0.2383 -0.2046 -0.0345 80  THR   B CA  
2518  C  C   . THR   B  81  ? 1.4462 0.8504 1.4108 -0.2194 -0.1466 -0.0457 80  THR   B C   
2519  O  O   . THR   B  81  ? 1.4816 0.8078 1.5278 -0.2036 -0.1435 -0.0554 80  THR   B O   
2520  C  CB  . THR   B  81  ? 1.4613 0.8777 1.5780 -0.2408 -0.2296 -0.0192 80  THR   B CB  
2521  O  OG1 . THR   B  81  ? 1.5366 0.9863 1.6979 -0.2782 -0.1699 0.0532  80  THR   B OG1 
2522  C  CG2 . THR   B  81  ? 1.4505 0.8929 1.5885 -0.2279 -0.2219 0.0019  80  THR   B CG2 
2523  N  N   . ALA   B  82  ? 1.4874 0.9451 1.3913 -0.2035 -0.1469 -0.0158 81  ALA   B N   
2524  C  CA  . ALA   B  82  ? 1.5405 0.8848 1.3319 -0.1633 -0.1616 -0.0068 81  ALA   B CA  
2525  C  C   . ALA   B  82  ? 1.5550 0.7707 1.2888 -0.1547 -0.1417 -0.0235 81  ALA   B C   
2526  O  O   . ALA   B  82  ? 1.5414 0.7637 1.3067 -0.1336 -0.1479 0.0003  81  ALA   B O   
2527  C  CB  . ALA   B  82  ? 1.5403 0.9525 1.2943 -0.1735 -0.1763 0.0153  81  ALA   B CB  
2528  N  N   . ASP   B  83  ? 1.5711 0.8153 1.2722 -0.1174 -0.1339 -0.0330 82  ASP   B N   
2529  C  CA  . ASP   B  83  ? 1.5610 0.7926 1.2294 -0.0721 -0.1206 -0.0205 82  ASP   B CA  
2530  C  C   . ASP   B  83  ? 1.5593 0.6839 1.2561 -0.0660 -0.1190 -0.0071 82  ASP   B C   
2531  O  O   . ASP   B  83  ? 1.6009 0.5834 1.1719 -0.0227 -0.1275 0.0238  82  ASP   B O   
2532  C  CB  . ASP   B  83  ? 1.5897 0.8259 1.2493 -0.0368 -0.0834 0.0008  82  ASP   B CB  
2533  C  CG  . ASP   B  83  ? 1.6092 0.8871 1.2261 -0.0064 -0.0812 0.0170  82  ASP   B CG  
2534  O  OD1 . ASP   B  83  ? 1.6107 1.0076 1.1790 -0.0016 -0.0912 -0.0219 82  ASP   B OD1 
2535  O  OD2 . ASP   B  83  ? 1.6374 0.9351 1.3480 0.0705  -0.0023 0.0181  82  ASP   B OD2 
2536  N  N   . ALA   B  84  ? 1.5382 0.6816 1.2656 -0.0402 -0.1005 -0.0539 83  ALA   B N   
2537  C  CA  . ALA   B  84  ? 1.5482 0.6490 1.2897 -0.0573 -0.1143 -0.1040 83  ALA   B CA  
2538  C  C   . ALA   B  84  ? 1.5054 0.6612 1.2631 -0.0588 -0.1315 -0.0936 83  ALA   B C   
2539  O  O   . ALA   B  84  ? 1.4888 0.6944 1.3356 -0.1256 -0.1287 -0.1180 83  ALA   B O   
2540  C  CB  . ALA   B  84  ? 1.5755 0.6226 1.2852 -0.0592 -0.0999 -0.1122 83  ALA   B CB  
2541  N  N   . GLU   B  85  ? 1.4961 0.5848 1.2655 -0.0568 -0.1496 -0.1235 84  GLU   B N   
2542  C  CA  . GLU   B  85  ? 1.5087 0.5614 1.3125 -0.0582 -0.1547 -0.1436 84  GLU   B CA  
2543  C  C   . GLU   B  85  ? 1.4539 0.5855 1.2974 -0.0245 -0.1492 -0.0744 84  GLU   B C   
2544  O  O   . GLU   B  85  ? 1.4584 0.6085 1.3580 -0.0447 -0.1387 -0.1114 84  GLU   B O   
2545  C  CB  . GLU   B  85  ? 1.5050 0.5573 1.3760 -0.0695 -0.1949 -0.1596 84  GLU   B CB  
2546  C  CG  . GLU   B  85  ? 1.5172 0.6250 1.4744 -0.0983 -0.1966 -0.1628 84  GLU   B CG  
2547  C  CD  . GLU   B  85  ? 1.4935 0.6068 1.5481 -0.1264 -0.2172 -0.1557 84  GLU   B CD  
2548  O  OE1 . GLU   B  85  ? 1.4757 0.8096 1.6346 -0.1816 -0.2061 -0.1471 84  GLU   B OE1 
2549  O  OE2 . GLU   B  85  ? 1.5053 0.4489 1.6544 -0.0991 -0.2408 -0.2404 84  GLU   B OE2 
2550  N  N   . ILE   B  86  ? 1.4880 0.4744 1.2613 0.0228  -0.1685 -0.0728 85  ILE   B N   
2551  C  CA  . ILE   B  86  ? 1.5088 0.4819 1.2753 0.0107  -0.1551 -0.0180 85  ILE   B CA  
2552  C  C   . ILE   B  86  ? 1.5296 0.5915 1.2556 0.0218  -0.1478 0.0007  85  ILE   B C   
2553  O  O   . ILE   B  86  ? 1.6032 0.6355 1.4228 -0.0242 -0.1557 -0.0642 85  ILE   B O   
2554  C  CB  . ILE   B  86  ? 1.5340 0.4540 1.2493 0.0162  -0.1512 0.0036  85  ILE   B CB  
2555  C  CG1 . ILE   B  86  ? 1.5601 0.4649 1.2485 0.0013  -0.1536 0.0175  85  ILE   B CG1 
2556  C  CG2 . ILE   B  86  ? 1.5240 0.4532 1.2302 0.0246  -0.1470 0.0280  85  ILE   B CG2 
2557  C  CD1 . ILE   B  86  ? 1.5712 0.5015 1.2570 0.0548  -0.1528 0.0455  85  ILE   B CD1 
2558  N  N   . LEU   B  87  ? 1.5000 0.5347 1.2116 -0.0368 -0.1330 -0.0421 86  LEU   B N   
2559  C  CA  . LEU   B  87  ? 1.4657 0.5157 1.2001 -0.0516 -0.1198 -0.0515 86  LEU   B CA  
2560  C  C   . LEU   B  87  ? 1.4823 0.5549 1.1762 -0.0398 -0.1084 -0.0550 86  LEU   B C   
2561  O  O   . LEU   B  87  ? 1.4523 0.5371 1.1722 -0.0258 -0.0771 -0.0615 86  LEU   B O   
2562  C  CB  . LEU   B  87  ? 1.4515 0.4957 1.1559 -0.1016 -0.1633 -0.0701 86  LEU   B CB  
2563  C  CG  . LEU   B  87  ? 1.4365 0.4673 1.1325 -0.1053 -0.1898 -0.0610 86  LEU   B CG  
2564  C  CD1 . LEU   B  87  ? 1.4698 0.4835 1.1487 -0.1027 -0.1874 -0.0468 86  LEU   B CD1 
2565  C  CD2 . LEU   B  87  ? 1.4302 0.4748 1.0971 -0.1004 -0.1984 -0.0495 86  LEU   B CD2 
2566  N  N   . ILE   B  88  ? 1.4762 0.5781 1.1749 -0.0151 -0.1098 -0.0763 87  ILE   B N   
2567  C  CA  . ILE   B  88  ? 1.5005 0.6011 1.1960 0.0106  -0.1050 -0.0715 87  ILE   B CA  
2568  C  C   . ILE   B  88  ? 1.5052 0.6002 1.2260 0.0072  -0.1209 -0.0670 87  ILE   B C   
2569  O  O   . ILE   B  88  ? 1.4796 0.5789 1.2384 0.0404  -0.1412 -0.0634 87  ILE   B O   
2570  C  CB  . ILE   B  88  ? 1.5105 0.5677 1.1969 0.0112  -0.1063 -0.0724 87  ILE   B CB  
2571  C  CG1 . ILE   B  88  ? 1.5298 0.5216 1.2198 0.0100  -0.0860 -0.1024 87  ILE   B CG1 
2572  C  CG2 . ILE   B  88  ? 1.5242 0.6134 1.2294 0.0393  -0.0989 -0.0641 87  ILE   B CG2 
2573  C  CD1 . ILE   B  88  ? 1.5181 0.5273 1.2458 -0.0041 -0.0942 -0.0712 87  ILE   B CD1 
2574  N  N   . ASN   B  89  ? 1.5557 0.6456 1.2362 -0.0256 -0.1158 -0.0622 88  ASN   B N   
2575  C  CA  . ASN   B  89  ? 1.6018 0.6247 1.3405 -0.0667 -0.1441 -0.0854 88  ASN   B CA  
2576  C  C   . ASN   B  89  ? 1.6243 0.4559 1.3844 -0.0981 -0.0949 -0.0951 88  ASN   B C   
2577  O  O   . ASN   B  89  ? 1.6143 0.4160 1.5042 -0.1903 -0.0694 -0.0876 88  ASN   B O   
2578  C  CB  . ASN   B  89  ? 1.7049 0.7238 1.3499 -0.0186 -0.1550 -0.0353 88  ASN   B CB  
2579  C  CG  . ASN   B  89  ? 1.7185 0.7908 1.4845 0.0793  -0.1704 0.0095  88  ASN   B CG  
2580  O  OD1 . ASN   B  89  ? 1.9250 0.6302 1.4734 0.0798  -0.2063 -0.0534 88  ASN   B OD1 
2581  N  ND2 . ASN   B  89  ? 1.8196 0.8309 1.5601 0.0234  -0.1746 -0.0263 88  ASN   B ND2 
2582  N  N   . THR   B  90  ? 1.5730 0.4668 1.3592 -0.1451 -0.1288 -0.0759 89  THR   B N   
2583  C  CA  . THR   B  90  ? 1.5914 0.4556 1.3515 -0.1647 -0.1302 -0.0655 89  THR   B CA  
2584  C  C   . THR   B  90  ? 1.6018 0.4689 1.3554 -0.1574 -0.1077 -0.0554 89  THR   B C   
2585  O  O   . THR   B  90  ? 1.6001 0.5338 1.2221 -0.1344 -0.1738 -0.0929 89  THR   B O   
2586  C  CB  . THR   B  90  ? 1.5847 0.4788 1.3768 -0.1653 -0.1474 -0.0564 89  THR   B CB  
2587  O  OG1 . THR   B  90  ? 1.6429 0.4589 1.3195 -0.2616 -0.2240 -0.0456 89  THR   B OG1 
2588  C  CG2 . THR   B  90  ? 1.5997 0.4893 1.4064 -0.1421 -0.1761 -0.0640 89  THR   B CG2 
2589  N  N   . ALA   B  91  ? 1.6480 0.4760 1.3599 -0.1587 -0.0831 -0.0517 90  ALA   B N   
2590  C  CA  . ALA   B  91  ? 1.6924 0.4869 1.3518 -0.1429 -0.0939 -0.0531 90  ALA   B CA  
2591  C  C   . ALA   B  91  ? 1.6654 0.5287 1.3557 -0.1224 -0.1056 -0.0071 90  ALA   B C   
2592  O  O   . ALA   B  91  ? 1.7250 0.7100 1.2822 -0.1170 -0.0196 -0.0343 90  ALA   B O   
2593  C  CB  . ALA   B  91  ? 1.6957 0.5079 1.3557 -0.1317 -0.0938 -0.0061 90  ALA   B CB  
2594  N  N   . ARG   B  92  ? 1.6521 0.4740 1.3925 -0.0894 -0.1063 0.0461  91  ARG   B N   
2595  C  CA  . ARG   B  92  ? 1.6751 0.4925 1.3942 -0.0617 -0.0894 0.0911  91  ARG   B CA  
2596  C  C   . ARG   B  92  ? 1.6896 0.4516 1.3882 -0.0251 -0.0673 0.0635  91  ARG   B C   
2597  O  O   . ARG   B  92  ? 1.7160 0.3516 1.3315 -0.0209 -0.1009 0.1242  91  ARG   B O   
2598  C  CB  . ARG   B  92  ? 1.6459 0.5025 1.4153 -0.0040 -0.1029 0.1427  91  ARG   B CB  
2599  C  CG  . ARG   B  92  ? 1.6158 0.5055 1.4260 0.0196  -0.0847 0.1485  91  ARG   B CG  
2600  C  CD  . ARG   B  92  ? 1.6166 0.5071 1.4408 0.0500  -0.0969 0.1420  91  ARG   B CD  
2601  N  NE  . ARG   B  92  ? 1.5988 0.5415 1.4341 0.0518  -0.0699 0.1129  91  ARG   B NE  
2602  C  CZ  . ARG   B  92  ? 1.6124 0.6472 1.4116 0.0739  -0.0864 0.1357  91  ARG   B CZ  
2603  N  NH1 . ARG   B  92  ? 1.6421 0.5998 1.4263 0.1201  -0.1117 0.1613  91  ARG   B NH1 
2604  N  NH2 . ARG   B  92  ? 1.6226 0.7450 1.4350 0.0480  -0.0562 0.1681  91  ARG   B NH2 
2605  N  N   . ILE   B  93  ? 1.6836 0.4902 1.4545 -0.0306 -0.0341 0.0264  92  ILE   B N   
2606  C  CA  . ILE   B  93  ? 1.6975 0.4702 1.5239 -0.0253 -0.0127 -0.0050 92  ILE   B CA  
2607  C  C   . ILE   B  93  ? 1.6727 0.5568 1.5542 -0.0316 -0.0237 -0.0010 92  ILE   B C   
2608  O  O   . ILE   B  93  ? 1.7107 0.6070 1.6172 -0.0117 0.0202  -0.0675 92  ILE   B O   
2609  C  CB  . ILE   B  93  ? 1.7102 0.4460 1.5134 -0.0380 -0.0116 0.0224  92  ILE   B CB  
2610  C  CG1 . ILE   B  93  ? 1.7106 0.4380 1.5435 -0.0218 -0.0177 0.0729  92  ILE   B CG1 
2611  C  CG2 . ILE   B  93  ? 1.6747 0.5081 1.5021 -0.0419 -0.0117 0.0111  92  ILE   B CG2 
2612  C  CD1 . ILE   B  93  ? 1.7150 0.4621 1.5449 -0.0190 -0.0107 0.0860  92  ILE   B CD1 
2613  N  N   . HIS   B  94  ? 1.6315 0.5293 1.5910 -0.0634 -0.0425 -0.0095 93  HIS   B N   
2614  C  CA  . HIS   B  94  ? 1.6137 0.6305 1.5734 -0.1429 -0.0162 -0.0420 93  HIS   B CA  
2615  C  C   . HIS   B  94  ? 1.5712 0.5067 1.4566 -0.1985 -0.0474 0.0242  93  HIS   B C   
2616  O  O   . HIS   B  94  ? 1.4748 0.4022 1.4404 -0.2743 0.0263  0.1029  93  HIS   B O   
2617  C  CB  . HIS   B  94  ? 1.7090 0.6619 1.7632 -0.1390 -0.1227 -0.0109 93  HIS   B CB  
2618  C  CG  . HIS   B  94  ? 1.6699 1.0319 1.9696 -0.2165 -0.1173 -0.0338 93  HIS   B CG  
2619  N  ND1 . HIS   B  94  ? 1.8168 1.1612 2.1455 -0.3596 -0.1693 -0.0265 93  HIS   B ND1 
2620  C  CD2 . HIS   B  94  ? 1.7907 1.1118 2.0536 -0.1957 -0.1391 -0.1315 93  HIS   B CD2 
2621  C  CE1 . HIS   B  94  ? 1.8537 1.1878 2.1582 -0.4349 -0.0682 -0.0440 93  HIS   B CE1 
2622  N  NE2 . HIS   B  94  ? 1.8376 1.1562 2.0568 -0.2426 -0.0800 -0.1619 93  HIS   B NE2 
2623  N  N   . ALA   B  95  ? 1.5620 0.4973 1.3664 -0.1691 -0.0113 0.0409  94  ALA   B N   
2624  C  CA  . ALA   B  95  ? 1.6123 0.4997 1.3123 -0.1563 -0.0153 0.0534  94  ALA   B CA  
2625  C  C   . ALA   B  95  ? 1.6408 0.5008 1.2490 -0.1526 0.0004  0.0750  94  ALA   B C   
2626  O  O   . ALA   B  95  ? 1.6230 0.4557 1.2601 -0.1469 -0.0221 0.0781  94  ALA   B O   
2627  C  CB  . ALA   B  95  ? 1.6239 0.4731 1.3295 -0.1611 0.0088  0.0458  94  ALA   B CB  
2628  N  N   . GLN   B  96  ? 1.6616 0.5393 1.2594 -0.1357 0.0140  0.1072  95  GLN   B N   
2629  C  CA  . GLN   B  96  ? 1.6678 0.5682 1.2590 -0.0991 -0.0054 0.1286  95  GLN   B CA  
2630  C  C   . GLN   B  96  ? 1.6722 0.4834 1.2925 -0.0752 -0.0046 0.1276  95  GLN   B C   
2631  O  O   . GLN   B  96  ? 1.7742 0.4268 1.2702 -0.2112 -0.0090 0.1323  95  GLN   B O   
2632  C  CB  . GLN   B  96  ? 1.6667 0.6345 1.2604 -0.0840 -0.0100 0.1282  95  GLN   B CB  
2633  C  CG  . GLN   B  96  ? 1.6566 0.7030 1.2026 -0.0966 0.0188  0.1410  95  GLN   B CG  
2634  C  CD  . GLN   B  96  ? 1.6873 0.7299 1.1687 -0.1015 0.0343  0.1749  95  GLN   B CD  
2635  O  OE1 . GLN   B  96  ? 1.6985 0.8810 1.0462 -0.1203 0.0491  0.2249  95  GLN   B OE1 
2636  N  NE2 . GLN   B  96  ? 1.6849 0.7256 1.1463 -0.0588 0.0720  0.1944  95  GLN   B NE2 
2637  N  N   . ASN   B  97  ? 1.6527 0.4702 1.3268 -0.0351 -0.0379 0.1731  96  ASN   B N   
2638  C  CA  . ASN   B  97  ? 1.5912 0.4327 1.3589 0.0197  -0.0193 0.1908  96  ASN   B CA  
2639  C  C   . ASN   B  97  ? 1.6141 0.3836 1.3662 0.0185  -0.0281 0.1747  96  ASN   B C   
2640  O  O   . ASN   B  97  ? 1.5324 0.4174 1.3289 -0.0491 -0.0359 0.2310  96  ASN   B O   
2641  C  CB  . ASN   B  97  ? 1.5530 0.5384 1.4278 0.0467  -0.0248 0.2150  96  ASN   B CB  
2642  C  CG  . ASN   B  97  ? 1.5518 0.6554 1.4440 0.0591  -0.0206 0.2147  96  ASN   B CG  
2643  O  OD1 . ASN   B  97  ? 1.4951 0.6375 1.5685 0.1014  -0.0142 0.2022  96  ASN   B OD1 
2644  N  ND2 . ASN   B  97  ? 1.5468 0.8011 1.5179 0.0780  -0.0081 0.1287  96  ASN   B ND2 
2645  N  N   . TYR   B  98  ? 1.6626 0.3601 1.3430 0.0165  -0.0226 0.1453  97  TYR   B N   
2646  C  CA  . TYR   B  98  ? 1.7175 0.3136 1.3556 -0.0270 -0.0529 0.1068  97  TYR   B CA  
2647  C  C   . TYR   B  98  ? 1.7523 0.2866 1.3830 -0.0278 -0.0480 0.1036  97  TYR   B C   
2648  O  O   . TYR   B  98  ? 1.8130 0.2665 1.3703 -0.0091 -0.0789 0.1185  97  TYR   B O   
2649  C  CB  . TYR   B  98  ? 1.6772 0.2765 1.3879 -0.0209 -0.0517 0.0813  97  TYR   B CB  
2650  C  CG  . TYR   B  98  ? 1.6822 0.2243 1.3928 -0.0367 -0.0575 0.0702  97  TYR   B CG  
2651  C  CD1 . TYR   B  98  ? 1.6960 0.2862 1.4477 -0.0414 -0.0307 0.0608  97  TYR   B CD1 
2652  C  CD2 . TYR   B  98  ? 1.6666 0.2046 1.4325 -0.0439 -0.0368 0.0544  97  TYR   B CD2 
2653  C  CE1 . TYR   B  98  ? 1.7174 0.2714 1.4554 -0.0575 -0.0371 0.0588  97  TYR   B CE1 
2654  C  CE2 . TYR   B  98  ? 1.6902 0.1659 1.4352 -0.0645 -0.0378 0.0562  97  TYR   B CE2 
2655  C  CZ  . TYR   B  98  ? 1.7173 0.1847 1.4040 -0.0830 -0.0417 0.0447  97  TYR   B CZ  
2656  O  OH  . TYR   B  98  ? 1.7404 0.1101 1.4090 -0.1278 -0.0820 0.0521  97  TYR   B OH  
2657  N  N   . LEU   B  99  ? 1.7306 0.2786 1.4069 -0.0611 -0.0210 0.1180  98  LEU   B N   
2658  C  CA  . LEU   B  99  ? 1.7436 0.3455 1.4150 -0.0665 0.0294  0.0673  98  LEU   B CA  
2659  C  C   . LEU   B  99  ? 1.8231 0.3313 1.4289 -0.0692 0.0667  0.0322  98  LEU   B C   
2660  O  O   . LEU   B  99  ? 1.8286 0.4518 1.4424 -0.0763 0.0897  -0.0373 98  LEU   B O   
2661  C  CB  . LEU   B  99  ? 1.7225 0.2937 1.4405 -0.1077 0.0560  0.1086  98  LEU   B CB  
2662  C  CG  . LEU   B  99  ? 1.7263 0.2991 1.4429 -0.1167 0.0709  0.1024  98  LEU   B CG  
2663  C  CD1 . LEU   B  99  ? 1.7343 0.2708 1.4356 -0.1383 0.0600  0.0762  98  LEU   B CD1 
2664  C  CD2 . LEU   B  99  ? 1.7184 0.3271 1.4593 -0.1180 0.0618  0.1348  98  LEU   B CD2 
2665  N  N   . LYS   B  100 ? 1.9194 0.4109 1.4324 -0.0520 0.0841  0.0575  99  LYS   B N   
2666  C  CA  . LYS   B  100 ? 1.9933 0.3612 1.5096 -0.0426 0.0405  0.0423  99  LYS   B CA  
2667  C  C   . LYS   B  100 ? 1.9224 0.3954 1.4435 0.0437  0.0212  0.0982  99  LYS   B C   
2668  O  O   . LYS   B  100 ? 1.9623 0.4209 1.4830 0.0684  0.0178  0.0494  99  LYS   B O   
2669  C  CB  . LYS   B  100 ? 2.0797 0.3847 1.5201 -0.0784 0.0486  0.0329  99  LYS   B CB  
2670  C  CG  . LYS   B  100 ? 2.1471 0.4092 1.6054 -0.1054 0.0598  0.0669  99  LYS   B CG  
2671  C  CD  . LYS   B  100 ? 2.2105 0.4504 1.6159 -0.1145 0.0753  0.0687  99  LYS   B CD  
2672  C  CE  . LYS   B  100 ? 2.1947 0.6048 1.7475 -0.1704 0.1177  0.0615  99  LYS   B CE  
2673  N  NZ  . LYS   B  100 ? 2.2664 0.6295 1.9054 -0.1593 0.1186  -0.0161 99  LYS   B NZ  
2674  N  N   . THR   B  101 ? 1.9144 0.3174 1.3732 0.0192  0.0162  0.0691  100 THR   B N   
2675  C  CA  . THR   B  101 ? 1.8857 0.2256 1.3856 0.1040  -0.0035 0.0652  100 THR   B CA  
2676  C  C   . THR   B  101 ? 1.8788 0.3135 1.3862 0.0849  -0.0119 0.0425  100 THR   B C   
2677  O  O   . THR   B  101 ? 1.8875 0.3579 1.4453 0.0684  -0.0188 -0.0080 100 THR   B O   
2678  C  CB  . THR   B  101 ? 1.9174 0.1260 1.3522 0.0812  -0.0303 0.0657  100 THR   B CB  
2679  O  OG1 . THR   B  101 ? 1.9286 0.0972 1.3431 0.1311  -0.0604 0.0532  100 THR   B OG1 
2680  C  CG2 . THR   B  101 ? 1.9135 0.0910 1.3623 0.0795  -0.0314 0.0627  100 THR   B CG2 
2681  N  N   . TYR   B  102 ? 1.8131 0.3272 1.2959 0.0912  -0.0578 0.0309  101 TYR   B N   
2682  C  CA  . TYR   B  102 ? 1.7794 0.3615 1.2882 0.0731  -0.0758 -0.0233 101 TYR   B CA  
2683  C  C   . TYR   B  102 ? 1.7831 0.3498 1.3171 0.0705  -0.0534 -0.0301 101 TYR   B C   
2684  O  O   . TYR   B  102 ? 1.7475 0.2507 1.2912 0.1276  -0.0800 0.0433  101 TYR   B O   
2685  C  CB  . TYR   B  102 ? 1.8048 0.3530 1.1812 0.0216  -0.0763 -0.0315 101 TYR   B CB  
2686  C  CG  . TYR   B  102 ? 1.8153 0.3207 1.1157 0.0242  -0.0749 -0.0603 101 TYR   B CG  
2687  C  CD1 . TYR   B  102 ? 1.8245 0.3721 1.1155 0.0234  -0.0849 -0.0668 101 TYR   B CD1 
2688  C  CD2 . TYR   B  102 ? 1.7847 0.2895 1.0746 0.0335  -0.0822 -0.0222 101 TYR   B CD2 
2689  C  CE1 . TYR   B  102 ? 1.8421 0.3028 1.0458 0.0547  -0.0940 -0.0536 101 TYR   B CE1 
2690  C  CE2 . TYR   B  102 ? 1.7793 0.3079 1.0166 0.0367  -0.0996 0.0027  101 TYR   B CE2 
2691  C  CZ  . TYR   B  102 ? 1.8027 0.2956 0.9748 0.0585  -0.1047 -0.0195 101 TYR   B CZ  
2692  O  OH  . TYR   B  102 ? 1.8021 0.3935 0.8947 0.0779  -0.1160 0.0333  101 TYR   B OH  
2693  N  N   . ASN   B  103 ? 1.7156 0.4708 1.4065 -0.0006 -0.0769 -0.0685 102 ASN   B N   
2694  C  CA  . ASN   B  103 ? 1.7056 0.5505 1.4952 -0.0548 -0.0285 -0.0919 102 ASN   B CA  
2695  C  C   . ASN   B  103 ? 1.6824 0.6175 1.4439 -0.0711 -0.0307 -0.0921 102 ASN   B C   
2696  O  O   . ASN   B  103 ? 1.6963 0.4906 1.4300 -0.0786 -0.0511 -0.1290 102 ASN   B O   
2697  C  CB  . ASN   B  103 ? 1.7267 0.5572 1.5958 -0.0671 -0.0036 -0.1196 102 ASN   B CB  
2698  C  CG  . ASN   B  103 ? 1.7476 0.5300 1.6757 -0.0739 -0.0290 -0.1085 102 ASN   B CG  
2699  O  OD1 . ASN   B  103 ? 1.7112 0.5526 1.7183 -0.1085 0.0035  -0.1576 102 ASN   B OD1 
2700  N  ND2 . ASN   B  103 ? 1.7347 0.6170 1.7490 -0.1206 0.0108  -0.1408 102 ASN   B ND2 
2701  N  N   . GLU   B  104 ? 1.6513 0.6499 1.4587 -0.0220 -0.0681 -0.0083 103 GLU   B N   
2702  C  CA  . GLU   B  104 ? 1.6240 0.7692 1.4788 -0.0719 -0.0387 0.0182  103 GLU   B CA  
2703  C  C   . GLU   B  104 ? 1.6133 0.7462 1.5069 -0.0311 -0.0794 0.0224  103 GLU   B C   
2704  O  O   . GLU   B  104 ? 1.5091 0.6961 1.5476 -0.0585 -0.1260 -0.0330 103 GLU   B O   
2705  C  CB  . GLU   B  104 ? 1.6097 0.9193 1.4944 -0.1209 -0.0463 0.0450  103 GLU   B CB  
2706  C  CG  . GLU   B  104 ? 1.6541 0.9332 1.5776 -0.1812 0.0182  0.0228  103 GLU   B CG  
2707  C  CD  . GLU   B  104 ? 1.6418 1.0080 1.5930 -0.2412 0.0258  0.1040  103 GLU   B CD  
2708  O  OE1 . GLU   B  104 ? 1.6718 0.9705 1.5703 -0.2997 0.0920  0.1260  103 GLU   B OE1 
2709  O  OE2 . GLU   B  104 ? 1.5856 1.0695 1.6682 -0.2340 0.0596  0.2308  103 GLU   B OE2 
2710  N  N   . ASP   B  105 ? 1.6303 0.7595 1.5159 -0.0347 -0.0676 0.0720  104 ASP   B N   
2711  C  CA  . ASP   B  105 ? 1.6487 0.7188 1.4757 -0.0276 -0.0494 0.1164  104 ASP   B CA  
2712  C  C   . ASP   B  105 ? 1.6630 0.6029 1.3651 -0.0410 -0.0259 0.0807  104 ASP   B C   
2713  O  O   . ASP   B  105 ? 1.6590 0.6214 1.3578 -0.0180 -0.0136 0.1186  104 ASP   B O   
2714  C  CB  . ASP   B  105 ? 1.6642 0.8216 1.5068 -0.0491 -0.0223 0.1354  104 ASP   B CB  
2715  C  CG  . ASP   B  105 ? 1.6415 0.9118 1.5725 -0.0283 0.0105  0.1749  104 ASP   B CG  
2716  O  OD1 . ASP   B  105 ? 1.6784 0.9446 1.6514 -0.1227 -0.0195 0.2465  104 ASP   B OD1 
2717  O  OD2 . ASP   B  105 ? 1.7405 1.0674 1.5036 -0.0169 0.0777  0.2204  104 ASP   B OD2 
2718  N  N   . ILE   B  106 ? 1.6695 0.5450 1.3468 -0.0385 -0.0466 0.0905  105 ILE   B N   
2719  C  CA  . ILE   B  106 ? 1.7137 0.4930 1.3037 -0.0263 -0.0609 0.0925  105 ILE   B CA  
2720  C  C   . ILE   B  106 ? 1.7614 0.4446 1.3216 -0.0436 -0.0407 0.0611  105 ILE   B C   
2721  O  O   . ILE   B  106 ? 1.8159 0.2775 1.3127 -0.0318 -0.0172 0.0746  105 ILE   B O   
2722  C  CB  . ILE   B  106 ? 1.6900 0.4702 1.3219 0.0108  -0.0479 0.1176  105 ILE   B CB  
2723  C  CG1 . ILE   B  106 ? 1.7045 0.4044 1.3008 0.0065  -0.0784 0.1357  105 ILE   B CG1 
2724  C  CG2 . ILE   B  106 ? 1.6894 0.4490 1.3653 0.0149  -0.0461 0.1096  105 ILE   B CG2 
2725  C  CD1 . ILE   B  106 ? 1.6765 0.3817 1.3270 0.0268  -0.0751 0.1382  105 ILE   B CD1 
2726  N  N   . PRO   B  107 ? 1.7890 0.4910 1.3179 -0.0524 -0.0483 0.0437  106 PRO   B N   
2727  C  CA  . PRO   B  107 ? 1.7826 0.5224 1.2932 -0.0612 -0.0481 0.0625  106 PRO   B CA  
2728  C  C   . PRO   B  107 ? 1.8005 0.5531 1.2603 -0.0352 -0.0849 0.0557  106 PRO   B C   
2729  O  O   . PRO   B  107 ? 1.7873 0.5538 1.2500 -0.0988 -0.0980 0.1274  106 PRO   B O   
2730  C  CB  . PRO   B  107 ? 1.7812 0.5033 1.2757 -0.0646 -0.0406 0.0747  106 PRO   B CB  
2731  C  CG  . PRO   B  107 ? 1.7866 0.5149 1.3313 -0.0766 -0.0188 0.0334  106 PRO   B CG  
2732  C  CD  . PRO   B  107 ? 1.7764 0.5550 1.3397 -0.0772 -0.0355 0.0332  106 PRO   B CD  
2733  N  N   . VAL   B  108 ? 1.7685 0.5722 1.2662 -0.0384 -0.0824 0.0338  107 VAL   B N   
2734  C  CA  . VAL   B  108 ? 1.7299 0.5268 1.2953 0.0029  -0.0849 0.0465  107 VAL   B CA  
2735  C  C   . VAL   B  108 ? 1.7695 0.4428 1.3573 0.0346  -0.0921 0.0144  107 VAL   B C   
2736  O  O   . VAL   B  108 ? 1.7391 0.4491 1.3845 0.1160  -0.1187 -0.0409 107 VAL   B O   
2737  C  CB  . VAL   B  108 ? 1.7214 0.5014 1.2409 0.0301  -0.0917 0.0582  107 VAL   B CB  
2738  C  CG1 . VAL   B  108 ? 1.7034 0.4489 1.2440 0.0577  -0.1120 0.0905  107 VAL   B CG1 
2739  C  CG2 . VAL   B  108 ? 1.7052 0.5976 1.2284 0.0178  -0.0694 0.0556  107 VAL   B CG2 
2740  N  N   . GLU   B  109 ? 1.8111 0.3906 1.3576 -0.0026 -0.1020 0.0290  108 GLU   B N   
2741  C  CA  . GLU   B  109 ? 1.7822 0.4586 1.3887 -0.0339 -0.0606 0.0168  108 GLU   B CA  
2742  C  C   . GLU   B  109 ? 1.7893 0.4349 1.3557 -0.0609 -0.0744 -0.0105 108 GLU   B C   
2743  O  O   . GLU   B  109 ? 1.7782 0.4231 1.3596 -0.1004 -0.0155 0.0218  108 GLU   B O   
2744  C  CB  . GLU   B  109 ? 1.8504 0.5645 1.3909 -0.0709 -0.0785 0.0045  108 GLU   B CB  
2745  C  CG  . GLU   B  109 ? 1.9128 0.5805 1.4807 -0.0320 0.0033  -0.0456 108 GLU   B CG  
2746  C  CD  . GLU   B  109 ? 1.8893 0.6063 1.5733 0.0132  -0.0031 -0.0612 108 GLU   B CD  
2747  O  OE1 . GLU   B  109 ? 2.1743 0.7536 1.7154 -0.1244 0.1087  -0.2027 108 GLU   B OE1 
2748  O  OE2 . GLU   B  109 ? 2.0595 0.4887 1.6431 0.0653  0.1480  -0.0905 108 GLU   B OE2 
2749  N  N   . ILE   B  110 ? 1.7518 0.4341 1.3310 -0.0576 -0.0671 -0.0069 109 ILE   B N   
2750  C  CA  . ILE   B  110 ? 1.7704 0.3835 1.3128 -0.0218 -0.0770 0.0151  109 ILE   B CA  
2751  C  C   . ILE   B  110 ? 1.7353 0.2894 1.3296 0.0204  -0.0818 -0.0034 109 ILE   B C   
2752  O  O   . ILE   B  110 ? 1.8017 0.2270 1.3868 0.1476  -0.0501 -0.0146 109 ILE   B O   
2753  C  CB  . ILE   B  110 ? 1.7649 0.3960 1.3000 -0.0793 -0.0817 -0.0334 109 ILE   B CB  
2754  C  CG1 . ILE   B  110 ? 1.7582 0.3810 1.2792 -0.1012 -0.0723 0.0108  109 ILE   B CG1 
2755  C  CG2 . ILE   B  110 ? 1.7377 0.4316 1.2973 -0.1243 -0.0723 -0.0825 109 ILE   B CG2 
2756  C  CD1 . ILE   B  110 ? 1.7799 0.4021 1.3031 -0.0755 -0.0362 -0.0031 109 ILE   B CD1 
2757  N  N   . LEU   B  111 ? 1.7046 0.2539 1.3449 -0.0149 -0.0428 -0.0063 110 LEU   B N   
2758  C  CA  . LEU   B  111 ? 1.6298 0.3657 1.3734 -0.0553 -0.0665 -0.0271 110 LEU   B CA  
2759  C  C   . LEU   B  111 ? 1.6091 0.3839 1.3236 -0.0630 -0.0901 -0.0554 110 LEU   B C   
2760  O  O   . LEU   B  111 ? 1.5805 0.5754 1.3781 -0.1081 -0.0650 -0.1238 110 LEU   B O   
2761  C  CB  . LEU   B  111 ? 1.6318 0.2775 1.4002 -0.0217 -0.0610 -0.0217 110 LEU   B CB  
2762  C  CG  . LEU   B  111 ? 1.6107 0.3382 1.4373 0.0211  -0.1016 -0.0061 110 LEU   B CG  
2763  C  CD1 . LEU   B  111 ? 1.6140 0.3452 1.4792 0.0242  -0.0882 0.0015  110 LEU   B CD1 
2764  C  CD2 . LEU   B  111 ? 1.6096 0.3718 1.4845 -0.0362 -0.1079 -0.0135 110 LEU   B CD2 
2765  N  N   . VAL   B  112 ? 1.5967 0.5273 1.2400 -0.0567 -0.0754 -0.0204 111 VAL   B N   
2766  C  CA  . VAL   B  112 ? 1.6019 0.5348 1.2374 -0.0280 -0.0579 0.0031  111 VAL   B CA  
2767  C  C   . VAL   B  112 ? 1.5870 0.5527 1.2438 -0.0360 -0.1024 -0.0102 111 VAL   B C   
2768  O  O   . VAL   B  112 ? 1.5452 0.6086 1.2573 0.0140  -0.0721 0.0000  111 VAL   B O   
2769  C  CB  . VAL   B  112 ? 1.6219 0.5831 1.2240 -0.0213 -0.0443 0.0170  111 VAL   B CB  
2770  C  CG1 . VAL   B  112 ? 1.6326 0.5699 1.2136 -0.0374 -0.0286 0.0270  111 VAL   B CG1 
2771  C  CG2 . VAL   B  112 ? 1.6202 0.6148 1.2389 -0.0224 -0.0362 0.0469  111 VAL   B CG2 
2772  N  N   . ARG   B  113 ? 1.6248 0.4810 1.2673 -0.0233 -0.1110 -0.0175 112 ARG   B N   
2773  C  CA  . ARG   B  113 ? 1.6313 0.4560 1.2745 0.0040  -0.1153 -0.0038 112 ARG   B CA  
2774  C  C   . ARG   B  113 ? 1.6033 0.4507 1.2555 0.0051  -0.0982 -0.0473 112 ARG   B C   
2775  O  O   . ARG   B  113 ? 1.5528 0.4123 1.2113 -0.0295 -0.0692 0.0168  112 ARG   B O   
2776  C  CB  . ARG   B  113 ? 1.6797 0.4567 1.2871 -0.0043 -0.1633 0.0229  112 ARG   B CB  
2777  C  CG  . ARG   B  113 ? 1.7245 0.4620 1.2382 0.0530  -0.2134 0.0723  112 ARG   B CG  
2778  C  CD  . ARG   B  113 ? 1.7481 0.5551 1.1516 0.0470  -0.2579 0.0702  112 ARG   B CD  
2779  N  NE  . ARG   B  113 ? 1.8091 0.6468 1.1310 0.0719  -0.2580 0.0972  112 ARG   B NE  
2780  C  CZ  . ARG   B  113 ? 1.8490 0.6647 1.1092 0.0332  -0.2135 0.0583  112 ARG   B CZ  
2781  N  NH1 . ARG   B  113 ? 1.8316 0.7307 1.1143 0.0045  -0.2033 0.0888  112 ARG   B NH1 
2782  N  NH2 . ARG   B  113 ? 1.9063 0.5960 1.1243 -0.0385 -0.1773 0.0344  112 ARG   B NH2 
2783  N  N   . ARG   B  114 ? 1.6497 0.5075 1.3229 0.0638  -0.1284 -0.0361 113 ARG   B N   
2784  C  CA  . ARG   B  114 ? 1.7288 0.6184 1.3715 0.0724  -0.0882 -0.0128 113 ARG   B CA  
2785  C  C   . ARG   B  114 ? 1.6801 0.6715 1.4303 0.0118  -0.1024 -0.0384 113 ARG   B C   
2786  O  O   . ARG   B  114 ? 1.6439 0.9186 1.4976 0.0424  -0.0847 -0.0304 113 ARG   B O   
2787  C  CB  . ARG   B  114 ? 1.8757 0.6641 1.5511 0.1605  -0.1335 -0.0405 113 ARG   B CB  
2788  C  CG  . ARG   B  114 ? 1.9219 0.6681 1.5540 0.2114  -0.1326 -0.0148 113 ARG   B CG  
2789  C  CD  . ARG   B  114 ? 2.0549 0.6650 1.6146 0.2459  -0.1894 -0.0185 113 ARG   B CD  
2790  N  NE  . ARG   B  114 ? 2.1106 0.6910 1.6315 0.2777  -0.1371 -0.0649 113 ARG   B NE  
2791  C  CZ  . ARG   B  114 ? 2.0536 0.6824 1.7239 0.3217  -0.0306 -0.0409 113 ARG   B CZ  
2792  N  NH1 . ARG   B  114 ? 2.1230 0.5374 1.7559 0.3474  -0.0545 -0.0615 113 ARG   B NH1 
2793  N  NH2 . ARG   B  114 ? 2.0270 0.6403 1.6941 0.2841  0.0430  -0.0382 113 ARG   B NH2 
2794  N  N   . LEU   B  115 ? 1.7151 0.6387 1.3643 -0.0191 -0.0844 0.0125  114 LEU   B N   
2795  C  CA  . LEU   B  115 ? 1.7091 0.5413 1.3195 -0.0004 -0.1140 0.0790  114 LEU   B CA  
2796  C  C   . LEU   B  115 ? 1.7344 0.5009 1.2200 -0.0176 -0.1444 0.0820  114 LEU   B C   
2797  O  O   . LEU   B  115 ? 1.7101 0.4894 1.1166 0.0529  -0.2033 0.1792  114 LEU   B O   
2798  C  CB  . LEU   B  115 ? 1.7240 0.5311 1.3468 -0.0367 -0.1076 0.0732  114 LEU   B CB  
2799  C  CG  . LEU   B  115 ? 1.7100 0.5764 1.3772 -0.0376 -0.1095 0.0916  114 LEU   B CG  
2800  C  CD1 . LEU   B  115 ? 1.7472 0.5747 1.4289 -0.0606 -0.0877 0.1366  114 LEU   B CD1 
2801  C  CD2 . LEU   B  115 ? 1.6955 0.6184 1.3950 -0.0206 -0.1021 0.0787  114 LEU   B CD2 
2802  N  N   . SER   B  116 ? 1.7267 0.4655 1.2000 -0.0227 -0.1268 0.0619  115 SER   B N   
2803  C  CA  . SER   B  116 ? 1.7156 0.4263 1.1472 -0.0546 -0.1097 0.0735  115 SER   B CA  
2804  C  C   . SER   B  116 ? 1.6906 0.3678 1.1728 -0.0634 -0.1449 0.0458  115 SER   B C   
2805  O  O   . SER   B  116 ? 1.6160 0.3084 1.1913 -0.0450 -0.1942 0.1440  115 SER   B O   
2806  C  CB  . SER   B  116 ? 1.7431 0.4278 1.1491 -0.0687 -0.0953 0.0829  115 SER   B CB  
2807  O  OG  . SER   B  116 ? 1.7852 0.4813 1.1306 -0.0899 -0.0512 0.1429  115 SER   B OG  
2808  N  N   . ASP   B  117 ? 1.6865 0.3648 1.1758 -0.0628 -0.1197 0.0411  116 ASP   B N   
2809  C  CA  . ASP   B  117 ? 1.6946 0.3584 1.1436 -0.0315 -0.0845 0.0857  116 ASP   B CA  
2810  C  C   . ASP   B  117 ? 1.6372 0.2012 1.1337 -0.0213 -0.0821 0.0534  116 ASP   B C   
2811  O  O   . ASP   B  117 ? 1.6821 0.0839 1.0695 0.0196  -0.0675 0.0852  116 ASP   B O   
2812  C  CB  . ASP   B  117 ? 1.7425 0.3963 1.2688 -0.0774 -0.0939 0.0557  116 ASP   B CB  
2813  C  CG  . ASP   B  117 ? 1.7809 0.4679 1.2880 -0.0536 -0.1127 0.0944  116 ASP   B CG  
2814  O  OD1 . ASP   B  117 ? 1.7373 0.5932 1.3573 -0.0693 -0.1187 0.2485  116 ASP   B OD1 
2815  O  OD2 . ASP   B  117 ? 1.8603 0.6669 1.4020 -0.0529 -0.0877 -0.1188 116 ASP   B OD2 
2816  N  N   . ILE   B  118 ? 1.6278 0.2839 1.1138 -0.0331 -0.0898 0.0429  117 ILE   B N   
2817  C  CA  . ILE   B  118 ? 1.6083 0.4479 1.1198 -0.0364 -0.1479 0.0624  117 ILE   B CA  
2818  C  C   . ILE   B  118 ? 1.5896 0.4651 1.1403 -0.0566 -0.1514 0.0335  117 ILE   B C   
2819  O  O   . ILE   B  118 ? 1.5914 0.6181 1.1218 -0.0730 -0.1726 -0.0485 117 ILE   B O   
2820  C  CB  . ILE   B  118 ? 1.6204 0.5003 1.0936 -0.0439 -0.1632 0.0966  117 ILE   B CB  
2821  C  CG1 . ILE   B  118 ? 1.6377 0.4993 1.0869 -0.0153 -0.1648 0.1160  117 ILE   B CG1 
2822  C  CG2 . ILE   B  118 ? 1.6228 0.5038 1.0853 -0.0491 -0.1857 0.1242  117 ILE   B CG2 
2823  C  CD1 . ILE   B  118 ? 1.6215 0.5745 1.0959 -0.0156 -0.1702 0.1304  117 ILE   B CD1 
2824  N  N   . LYS   B  119 ? 1.6011 0.5203 1.1446 -0.0520 -0.1366 0.0806  118 LYS   B N   
2825  C  CA  . LYS   B  119 ? 1.6005 0.5126 1.1890 -0.0201 -0.1248 0.1050  118 LYS   B CA  
2826  C  C   . LYS   B  119 ? 1.6220 0.4820 1.1993 0.0085  -0.1409 0.0871  118 LYS   B C   
2827  O  O   . LYS   B  119 ? 1.6100 0.5667 1.1743 0.1045  -0.1237 0.1487  118 LYS   B O   
2828  C  CB  . LYS   B  119 ? 1.6213 0.5002 1.2506 -0.0422 -0.1256 0.1283  118 LYS   B CB  
2829  C  CG  . LYS   B  119 ? 1.6130 0.5288 1.3243 -0.0621 -0.1327 0.1423  118 LYS   B CG  
2830  C  CD  . LYS   B  119 ? 1.5977 0.5510 1.4198 -0.0800 -0.1162 0.1463  118 LYS   B CD  
2831  C  CE  . LYS   B  119 ? 1.6176 0.6091 1.4978 -0.0445 -0.1469 0.1532  118 LYS   B CE  
2832  N  NZ  . LYS   B  119 ? 1.6623 0.6251 1.5333 -0.0633 -0.1240 0.1570  118 LYS   B NZ  
2833  N  N   . GLN   B  120 ? 1.6415 0.3610 1.2292 -0.0212 -0.1179 0.0208  119 GLN   B N   
2834  C  CA  . GLN   B  120 ? 1.6520 0.3431 1.2742 -0.0276 -0.1369 -0.0180 119 GLN   B CA  
2835  C  C   . GLN   B  120 ? 1.6883 0.3555 1.2579 -0.0505 -0.1371 -0.0405 119 GLN   B C   
2836  O  O   . GLN   B  120 ? 1.7026 0.3549 1.3005 -0.0362 -0.1452 -0.0313 119 GLN   B O   
2837  C  CB  . GLN   B  120 ? 1.6739 0.3199 1.2722 -0.0513 -0.1025 -0.0238 119 GLN   B CB  
2838  C  CG  . GLN   B  120 ? 1.6956 0.3067 1.2851 -0.0287 -0.1071 -0.0282 119 GLN   B CG  
2839  C  CD  . GLN   B  120 ? 1.6908 0.3474 1.3013 -0.0335 -0.0963 -0.0551 119 GLN   B CD  
2840  O  OE1 . GLN   B  120 ? 1.6884 0.2239 1.3009 -0.0745 -0.1017 -0.0401 119 GLN   B OE1 
2841  N  NE2 . GLN   B  120 ? 1.6846 0.3789 1.2856 -0.0467 -0.0936 -0.0197 119 GLN   B NE2 
2842  N  N   . GLY   B  121 ? 1.7267 0.3826 1.2282 -0.0093 -0.1840 -0.0327 120 GLY   B N   
2843  C  CA  . GLY   B  121 ? 1.7244 0.4810 1.1628 -0.0114 -0.2002 -0.0631 120 GLY   B CA  
2844  C  C   . GLY   B  121 ? 1.7374 0.4560 1.1839 -0.0535 -0.2883 -0.0793 120 GLY   B C   
2845  O  O   . GLY   B  121 ? 1.7474 0.4426 1.1590 -0.0511 -0.2972 -0.0687 120 GLY   B O   
2846  N  N   . TYR   B  122 ? 1.7084 0.4126 1.2470 -0.0442 -0.2747 -0.0818 121 TYR   B N   
2847  C  CA  . TYR   B  122 ? 1.6532 0.4551 1.2895 -0.0590 -0.3081 -0.1217 121 TYR   B CA  
2848  C  C   . TYR   B  122 ? 1.6262 0.4358 1.2946 -0.0657 -0.2985 -0.1818 121 TYR   B C   
2849  O  O   . TYR   B  122 ? 1.5830 0.5462 1.3245 -0.0589 -0.3002 -0.2445 121 TYR   B O   
2850  C  CB  . TYR   B  122 ? 1.6671 0.4845 1.2412 -0.0338 -0.3382 -0.1527 121 TYR   B CB  
2851  C  CG  . TYR   B  122 ? 1.6588 0.5221 1.1897 0.0141  -0.3488 -0.1803 121 TYR   B CG  
2852  C  CD1 . TYR   B  122 ? 1.6810 0.5345 1.1790 0.1076  -0.3644 -0.1735 121 TYR   B CD1 
2853  C  CD2 . TYR   B  122 ? 1.6777 0.6160 1.1659 0.0643  -0.3331 -0.1577 121 TYR   B CD2 
2854  C  CE1 . TYR   B  122 ? 1.7179 0.5349 1.1924 0.1389  -0.3327 -0.1665 121 TYR   B CE1 
2855  C  CE2 . TYR   B  122 ? 1.7151 0.5460 1.2262 0.1153  -0.2764 -0.1802 121 TYR   B CE2 
2856  C  CZ  . TYR   B  122 ? 1.7283 0.5689 1.1766 0.1127  -0.2705 -0.2036 121 TYR   B CZ  
2857  O  OH  . TYR   B  122 ? 1.6989 0.5481 1.2526 0.1577  -0.1735 -0.1747 121 TYR   B OH  
2858  N  N   . THR   B  123 ? 1.6250 0.3986 1.2803 -0.0854 -0.2630 -0.1552 122 THR   B N   
2859  C  CA  . THR   B  123 ? 1.5836 0.3791 1.2604 -0.1093 -0.2635 -0.1590 122 THR   B CA  
2860  C  C   . THR   B  123 ? 1.5655 0.4626 1.2495 -0.0638 -0.2733 -0.1158 122 THR   B C   
2861  O  O   . THR   B  123 ? 1.4505 0.4113 1.3297 -0.1463 -0.3228 -0.0670 122 THR   B O   
2862  C  CB  . THR   B  123 ? 1.6276 0.3072 1.2332 -0.1154 -0.2540 -0.2030 122 THR   B CB  
2863  O  OG1 . THR   B  123 ? 1.6567 0.1824 1.2891 -0.1246 -0.2187 -0.2144 122 THR   B OG1 
2864  C  CG2 . THR   B  123 ? 1.6277 0.3478 1.2474 -0.1226 -0.2227 -0.1836 122 THR   B CG2 
2865  N  N   . GLN   B  124 ? 1.5594 0.4494 1.1861 -0.0379 -0.2488 -0.1243 123 GLN   B N   
2866  C  CA  . GLN   B  124 ? 1.5561 0.4967 1.1967 -0.0004 -0.2564 -0.1213 123 GLN   B CA  
2867  C  C   . GLN   B  124 ? 1.5828 0.4631 1.1726 0.0111  -0.2572 -0.1364 123 GLN   B C   
2868  O  O   . GLN   B  124 ? 1.5659 0.5884 1.1721 -0.0192 -0.2607 -0.1522 123 GLN   B O   
2869  C  CB  . GLN   B  124 ? 1.6027 0.4782 1.1857 0.0060  -0.2488 -0.1050 123 GLN   B CB  
2870  C  CG  . GLN   B  124 ? 1.6165 0.4968 1.1590 0.0327  -0.2740 -0.0499 123 GLN   B CG  
2871  C  CD  . GLN   B  124 ? 1.6511 0.5260 1.1098 0.0508  -0.2809 0.0425  123 GLN   B CD  
2872  O  OE1 . GLN   B  124 ? 1.7513 0.5099 1.0897 0.0558  -0.2473 0.1373  123 GLN   B OE1 
2873  N  NE2 . GLN   B  124 ? 1.6376 0.5959 1.0741 0.0591  -0.2469 0.0283  123 GLN   B NE2 
2874  N  N   . HIS   B  125 ? 1.5874 0.3769 1.2377 0.0206  -0.2323 -0.1320 124 HIS   B N   
2875  C  CA  . HIS   B  125 ? 1.6024 0.4633 1.2720 0.0459  -0.2124 -0.0855 124 HIS   B CA  
2876  C  C   . HIS   B  125 ? 1.5389 0.5333 1.2677 0.0789  -0.1775 -0.0755 124 HIS   B C   
2877  O  O   . HIS   B  125 ? 1.5062 0.4487 1.3225 0.1760  -0.1736 -0.0472 124 HIS   B O   
2878  C  CB  . HIS   B  125 ? 1.6586 0.4912 1.2894 0.0138  -0.2420 -0.0910 124 HIS   B CB  
2879  C  CG  . HIS   B  125 ? 1.7241 0.4067 1.2968 0.0083  -0.2343 -0.0877 124 HIS   B CG  
2880  N  ND1 . HIS   B  125 ? 1.7623 0.2831 1.3526 -0.0206 -0.2445 -0.0742 124 HIS   B ND1 
2881  C  CD2 . HIS   B  125 ? 1.7897 0.3776 1.2878 0.0074  -0.2438 -0.0550 124 HIS   B CD2 
2882  C  CE1 . HIS   B  125 ? 1.7794 0.2865 1.3164 -0.0096 -0.2410 -0.0406 124 HIS   B CE1 
2883  N  NE2 . HIS   B  125 ? 1.7949 0.3413 1.3083 -0.0044 -0.2330 -0.0244 124 HIS   B NE2 
2884  N  N   . GLY   B  126 ? 1.5513 0.6710 1.2501 0.1036  -0.1715 -0.0792 125 GLY   B N   
2885  C  CA  . GLY   B  126 ? 1.5271 0.6893 1.2797 0.0924  -0.1756 -0.0559 125 GLY   B CA  
2886  C  C   . GLY   B  126 ? 1.5320 0.6476 1.3507 0.0534  -0.1965 -0.0474 125 GLY   B C   
2887  O  O   . GLY   B  126 ? 1.5251 0.8839 1.3891 0.0514  -0.2583 -0.0429 125 GLY   B O   
2888  N  N   . GLY   B  127 ? 1.5509 0.6222 1.3511 -0.0018 -0.1924 -0.0377 126 GLY   B N   
2889  C  CA  . GLY   B  127 ? 1.5194 0.5694 1.3635 0.0290  -0.2044 -0.0096 126 GLY   B CA  
2890  C  C   . GLY   B  127 ? 1.5361 0.4982 1.3063 0.0135  -0.2152 -0.0272 126 GLY   B C   
2891  O  O   . GLY   B  127 ? 1.4730 0.5703 1.3208 -0.0099 -0.2308 -0.0632 126 GLY   B O   
2892  N  N   . LEU   B  128 ? 1.5196 0.4461 1.2885 0.0198  -0.2284 0.0136  127 LEU   B N   
2893  C  CA  . LEU   B  128 ? 1.5475 0.5201 1.2425 -0.0222 -0.2454 -0.0266 127 LEU   B CA  
2894  C  C   . LEU   B  128 ? 1.5758 0.5209 1.2209 -0.0321 -0.2466 -0.0392 127 LEU   B C   
2895  O  O   . LEU   B  128 ? 1.6021 0.7292 1.2129 -0.0487 -0.2791 -0.0969 127 LEU   B O   
2896  C  CB  . LEU   B  128 ? 1.5279 0.5392 1.2288 -0.0291 -0.2026 -0.0513 127 LEU   B CB  
2897  C  CG  . LEU   B  128 ? 1.5298 0.5564 1.1974 -0.0254 -0.1987 -0.0393 127 LEU   B CG  
2898  C  CD1 . LEU   B  128 ? 1.5295 0.5358 1.1824 -0.0278 -0.2020 0.0072  127 LEU   B CD1 
2899  C  CD2 . LEU   B  128 ? 1.5302 0.5953 1.1885 -0.0525 -0.2118 -0.0348 127 LEU   B CD2 
2900  N  N   . ARG   B  129 ? 1.5944 0.5124 1.2270 -0.0504 -0.2329 -0.0451 128 ARG   B N   
2901  C  CA  . ARG   B  129 ? 1.6434 0.4473 1.2181 -0.0297 -0.2009 -0.0720 128 ARG   B CA  
2902  C  C   . ARG   B  129 ? 1.6674 0.3664 1.1927 -0.0374 -0.2405 -0.0924 128 ARG   B C   
2903  O  O   . ARG   B  129 ? 1.6294 0.3801 1.0600 -0.0092 -0.2461 -0.1352 128 ARG   B O   
2904  C  CB  . ARG   B  129 ? 1.6128 0.4061 1.2609 -0.0290 -0.2131 -0.0344 128 ARG   B CB  
2905  C  CG  . ARG   B  129 ? 1.6320 0.3776 1.2733 -0.0096 -0.1606 0.0256  128 ARG   B CG  
2906  C  CD  . ARG   B  129 ? 1.6126 0.3556 1.2843 0.0005  -0.1566 0.0552  128 ARG   B CD  
2907  N  NE  . ARG   B  129 ? 1.6276 0.3495 1.2659 0.0030  -0.1441 0.1037  128 ARG   B NE  
2908  C  CZ  . ARG   B  129 ? 1.6321 0.3712 1.2958 0.0224  -0.1308 0.1250  128 ARG   B CZ  
2909  N  NH1 . ARG   B  129 ? 1.6958 0.3875 1.3173 0.0477  -0.0940 0.1552  128 ARG   B NH1 
2910  N  NH2 . ARG   B  129 ? 1.6040 0.4263 1.2901 0.0114  -0.1629 0.1121  128 ARG   B NH2 
2911  N  N   . PRO   B  130 ? 1.7282 0.3448 1.1616 -0.0677 -0.2399 -0.1308 129 PRO   B N   
2912  C  CA  . PRO   B  130 ? 1.7020 0.3205 1.1982 -0.0521 -0.2380 -0.1255 129 PRO   B CA  
2913  C  C   . PRO   B  130 ? 1.7089 0.3085 1.2231 -0.0957 -0.2738 -0.1386 129 PRO   B C   
2914  O  O   . PRO   B  130 ? 1.6347 0.2563 1.2532 -0.0747 -0.2635 -0.1537 129 PRO   B O   
2915  C  CB  . PRO   B  130 ? 1.7450 0.3473 1.2091 -0.0622 -0.2489 -0.1060 129 PRO   B CB  
2916  C  CG  . PRO   B  130 ? 1.7756 0.3958 1.1936 -0.0509 -0.2344 -0.1393 129 PRO   B CG  
2917  C  CD  . PRO   B  130 ? 1.7626 0.3851 1.1973 -0.0240 -0.2411 -0.1111 129 PRO   B CD  
2918  N  N   . PHE   B  131 ? 1.7235 0.3444 1.3132 -0.0361 -0.2031 -0.0687 130 PHE   B N   
2919  C  CA  . PHE   B  131 ? 1.7309 0.3829 1.2999 -0.0648 -0.2474 -0.0042 130 PHE   B CA  
2920  C  C   . PHE   B  131 ? 1.7396 0.3859 1.2317 -0.0730 -0.2560 -0.0158 130 PHE   B C   
2921  O  O   . PHE   B  131 ? 1.7910 0.3740 1.2383 -0.1105 -0.2269 0.0440  130 PHE   B O   
2922  C  CB  . PHE   B  131 ? 1.7733 0.4021 1.3467 -0.0230 -0.2142 0.0052  130 PHE   B CB  
2923  C  CG  . PHE   B  131 ? 1.8109 0.4620 1.3376 -0.0280 -0.2190 0.0644  130 PHE   B CG  
2924  C  CD1 . PHE   B  131 ? 1.8134 0.3983 1.3439 -0.0321 -0.1956 0.0937  130 PHE   B CD1 
2925  C  CD2 . PHE   B  131 ? 1.8490 0.3882 1.3299 -0.0536 -0.2039 0.0984  130 PHE   B CD2 
2926  C  CE1 . PHE   B  131 ? 1.8060 0.3310 1.3463 0.0286  -0.1993 0.0649  130 PHE   B CE1 
2927  C  CE2 . PHE   B  131 ? 1.8474 0.3243 1.3122 0.0209  -0.1971 0.0765  130 PHE   B CE2 
2928  C  CZ  . PHE   B  131 ? 1.8152 0.2568 1.3367 0.0273  -0.1837 0.0774  130 PHE   B CZ  
2929  N  N   . GLY   B  132 ? 1.7129 0.4001 1.2094 -0.0486 -0.2605 -0.0123 131 GLY   B N   
2930  C  CA  . GLY   B  132 ? 1.7048 0.4285 1.2465 -0.0640 -0.2414 -0.0102 131 GLY   B CA  
2931  C  C   . GLY   B  132 ? 1.7253 0.4346 1.2288 -0.0340 -0.2433 -0.0404 131 GLY   B C   
2932  O  O   . GLY   B  132 ? 1.6760 0.4710 1.3076 0.0103  -0.2390 -0.0232 131 GLY   B O   
2933  N  N   . VAL   B  133 ? 1.7170 0.4398 1.2194 -0.0502 -0.2371 -0.0370 132 VAL   B N   
2934  C  CA  . VAL   B  133 ? 1.7290 0.5115 1.2624 -0.0632 -0.2121 -0.0632 132 VAL   B CA  
2935  C  C   . VAL   B  133 ? 1.7360 0.4120 1.2657 -0.1012 -0.1989 -0.0556 132 VAL   B C   
2936  O  O   . VAL   B  133 ? 1.7567 0.3653 1.2971 -0.1321 -0.1875 -0.1271 132 VAL   B O   
2937  C  CB  . VAL   B  133 ? 1.7380 0.5585 1.2046 -0.0033 -0.2227 -0.0399 132 VAL   B CB  
2938  C  CG1 . VAL   B  133 ? 1.7237 0.7042 1.2511 0.0003  -0.1763 -0.0376 132 VAL   B CG1 
2939  C  CG2 . VAL   B  133 ? 1.7420 0.6353 1.1890 -0.0119 -0.2193 -0.0771 132 VAL   B CG2 
2940  N  N   . SER   B  134 ? 1.7089 0.4633 1.3526 -0.1222 -0.1862 -0.0544 133 SER   B N   
2941  C  CA  . SER   B  134 ? 1.6868 0.4965 1.3581 -0.1115 -0.1883 -0.0344 133 SER   B CA  
2942  C  C   . SER   B  134 ? 1.6498 0.4581 1.4118 -0.1301 -0.1901 0.0096  133 SER   B C   
2943  O  O   . SER   B  134 ? 1.6607 0.3646 1.4427 -0.1154 -0.2224 0.0463  133 SER   B O   
2944  C  CB  . SER   B  134 ? 1.7087 0.5268 1.3649 -0.0768 -0.2165 0.0043  133 SER   B CB  
2945  O  OG  . SER   B  134 ? 1.7524 0.5344 1.3385 -0.0274 -0.2490 -0.0073 133 SER   B OG  
2946  N  N   . PHE   B  135 ? 1.6411 0.4739 1.3848 -0.1315 -0.1670 0.0121  134 PHE   B N   
2947  C  CA  . PHE   B  135 ? 1.6191 0.5336 1.3515 -0.1172 -0.1503 0.0501  134 PHE   B CA  
2948  C  C   . PHE   B  135 ? 1.6105 0.4493 1.3739 -0.1528 -0.1295 0.0647  134 PHE   B C   
2949  O  O   . PHE   B  135 ? 1.6434 0.4908 1.3280 -0.1882 -0.1309 0.1157  134 PHE   B O   
2950  C  CB  . PHE   B  135 ? 1.5834 0.5464 1.3223 -0.1233 -0.1656 0.0558  134 PHE   B CB  
2951  C  CG  . PHE   B  135 ? 1.5286 0.6325 1.2778 -0.0868 -0.1985 0.0436  134 PHE   B CG  
2952  C  CD1 . PHE   B  135 ? 1.5418 0.6784 1.2486 -0.0886 -0.2034 0.0386  134 PHE   B CD1 
2953  C  CD2 . PHE   B  135 ? 1.5056 0.6639 1.2166 -0.0524 -0.1920 0.0268  134 PHE   B CD2 
2954  C  CE1 . PHE   B  135 ? 1.4996 0.7487 1.2234 -0.0729 -0.2141 0.0328  134 PHE   B CE1 
2955  C  CE2 . PHE   B  135 ? 1.4672 0.7074 1.1883 -0.0300 -0.1958 0.0121  134 PHE   B CE2 
2956  C  CZ  . PHE   B  135 ? 1.4816 0.7554 1.1976 -0.0454 -0.2110 0.0289  134 PHE   B CZ  
2957  N  N   . ILE   B  136 ? 1.6124 0.4054 1.3448 -0.1771 -0.1097 0.0457  135 ILE   B N   
2958  C  CA  . ILE   B  136 ? 1.6387 0.5028 1.3546 -0.1777 -0.0971 0.0147  135 ILE   B CA  
2959  C  C   . ILE   B  136 ? 1.6285 0.5138 1.3762 -0.1752 -0.0789 0.0136  135 ILE   B C   
2960  O  O   . ILE   B  136 ? 1.6056 0.6206 1.3368 -0.2546 -0.1150 0.0006  135 ILE   B O   
2961  C  CB  . ILE   B  136 ? 1.6304 0.5583 1.3765 -0.1873 -0.0825 -0.0018 135 ILE   B CB  
2962  C  CG1 . ILE   B  136 ? 1.6948 0.5912 1.3954 -0.1436 -0.0892 -0.0517 135 ILE   B CG1 
2963  C  CG2 . ILE   B  136 ? 1.6487 0.5669 1.3841 -0.1762 -0.0671 0.0121  135 ILE   B CG2 
2964  C  CD1 . ILE   B  136 ? 1.7145 0.6413 1.4218 -0.1706 -0.0781 -0.0405 135 ILE   B CD1 
2965  N  N   . TYR   B  137 ? 1.6317 0.5793 1.3541 -0.1624 -0.0901 0.0007  136 TYR   B N   
2966  C  CA  . TYR   B  137 ? 1.6057 0.5695 1.3118 -0.1737 -0.0929 -0.0086 136 TYR   B CA  
2967  C  C   . TYR   B  137 ? 1.5634 0.4428 1.3218 -0.1762 -0.0973 0.0022  136 TYR   B C   
2968  O  O   . TYR   B  137 ? 1.5322 0.4211 1.3220 -0.1749 -0.1201 -0.0253 136 TYR   B O   
2969  C  CB  . TYR   B  137 ? 1.6346 0.4863 1.2575 -0.1536 -0.1021 -0.0541 136 TYR   B CB  
2970  C  CG  . TYR   B  137 ? 1.6755 0.5337 1.2037 -0.1475 -0.1073 -0.0044 136 TYR   B CG  
2971  C  CD1 . TYR   B  137 ? 1.6671 0.6208 1.2152 -0.1100 -0.1229 0.0220  136 TYR   B CD1 
2972  C  CD2 . TYR   B  137 ? 1.6856 0.5800 1.1598 -0.0939 -0.1152 0.0092  136 TYR   B CD2 
2973  C  CE1 . TYR   B  137 ? 1.7225 0.6595 1.1661 -0.1125 -0.1153 0.0669  136 TYR   B CE1 
2974  C  CE2 . TYR   B  137 ? 1.7096 0.6702 1.1651 -0.0788 -0.1047 0.0302  136 TYR   B CE2 
2975  C  CZ  . TYR   B  137 ? 1.7650 0.6307 1.1978 -0.0825 -0.1361 0.0725  136 TYR   B CZ  
2976  O  OH  . TYR   B  137 ? 1.8066 0.6925 1.2392 -0.0874 -0.1032 0.0969  136 TYR   B OH  
2977  N  N   . ALA   B  138 ? 1.5541 0.4523 1.3545 -0.1859 -0.0904 0.0553  137 ALA   B N   
2978  C  CA  . ALA   B  138 ? 1.5667 0.5255 1.3631 -0.1553 -0.0758 0.1051  137 ALA   B CA  
2979  C  C   . ALA   B  138 ? 1.5551 0.5312 1.3804 -0.1024 -0.0816 0.1528  137 ALA   B C   
2980  O  O   . ALA   B  138 ? 1.5614 0.6237 1.4115 -0.0575 -0.0803 0.1838  137 ALA   B O   
2981  C  CB  . ALA   B  138 ? 1.5628 0.6231 1.4010 -0.1702 -0.0847 0.1066  137 ALA   B CB  
2982  N  N   . GLY   B  139 ? 1.5682 0.5138 1.3241 -0.0627 -0.1018 0.2127  138 GLY   B N   
2983  C  CA  . GLY   B  139 ? 1.5929 0.5217 1.3681 -0.0581 -0.1027 0.1775  138 GLY   B CA  
2984  C  C   . GLY   B  139 ? 1.6313 0.5151 1.3534 -0.0470 -0.1061 0.2110  138 GLY   B C   
2985  O  O   . GLY   B  139 ? 1.5831 0.3257 1.4570 -0.0309 -0.1390 0.1701  138 GLY   B O   
2986  N  N   . TYR   B  140 ? 1.6848 0.5586 1.4253 -0.0161 -0.0635 0.1259  139 TYR   B N   
2987  C  CA  . TYR   B  140 ? 1.7214 0.6443 1.3957 -0.0326 -0.0303 0.1379  139 TYR   B CA  
2988  C  C   . TYR   B  140 ? 1.7346 0.5932 1.4138 -0.0027 -0.0422 0.0702  139 TYR   B C   
2989  O  O   . TYR   B  140 ? 1.7298 0.4928 1.3909 -0.0570 0.0245  0.0140  139 TYR   B O   
2990  C  CB  . TYR   B  140 ? 1.7524 0.7301 1.4112 -0.0049 0.0237  0.1698  139 TYR   B CB  
2991  C  CG  . TYR   B  140 ? 1.8177 0.7747 1.3940 0.0236  0.0449  0.1837  139 TYR   B CG  
2992  C  CD1 . TYR   B  140 ? 1.8881 0.7826 1.4331 0.0064  0.0819  0.1779  139 TYR   B CD1 
2993  C  CD2 . TYR   B  140 ? 1.8453 0.8190 1.3946 0.0323  0.0611  0.1947  139 TYR   B CD2 
2994  C  CE1 . TYR   B  140 ? 1.9529 0.9627 1.3798 0.0235  0.1201  0.1934  139 TYR   B CE1 
2995  C  CE2 . TYR   B  140 ? 1.8983 0.8984 1.3754 0.0376  0.1066  0.2012  139 TYR   B CE2 
2996  C  CZ  . TYR   B  140 ? 1.9641 0.9112 1.4015 0.0270  0.1130  0.1998  139 TYR   B CZ  
2997  O  OH  . TYR   B  140 ? 2.0126 1.2285 1.3295 0.0212  0.1553  0.1940  139 TYR   B OH  
2998  N  N   . ASP   B  141 ? 1.7380 0.5416 1.4048 -0.0237 -0.0471 0.1091  140 ASP   B N   
2999  C  CA  . ASP   B  141 ? 1.7500 0.6149 1.4209 -0.0622 -0.0826 0.0609  140 ASP   B CA  
3000  C  C   . ASP   B  141 ? 1.7903 0.6190 1.4140 -0.0744 -0.0427 0.1022  140 ASP   B C   
3001  O  O   . ASP   B  141 ? 1.7866 0.4695 1.4354 -0.0123 -0.0730 0.0472  140 ASP   B O   
3002  C  CB  . ASP   B  141 ? 1.7343 0.6731 1.3946 -0.0773 -0.1234 0.0802  140 ASP   B CB  
3003  C  CG  . ASP   B  141 ? 1.7604 0.6102 1.3116 -0.1508 -0.1770 0.0940  140 ASP   B CG  
3004  O  OD1 . ASP   B  141 ? 1.7363 0.5523 1.3196 -0.1801 -0.2246 0.1665  140 ASP   B OD1 
3005  O  OD2 . ASP   B  141 ? 1.7430 0.5433 1.3127 -0.2345 -0.1747 0.0692  140 ASP   B OD2 
3006  N  N   . ASP   B  142 ? 1.8976 0.7523 1.4762 -0.0976 -0.0306 -0.0713 141 ASP   B N   
3007  C  CA  . ASP   B  142 ? 1.9937 0.8273 1.4789 -0.1267 0.0229  -0.0550 141 ASP   B CA  
3008  C  C   . ASP   B  142 ? 1.9895 0.7740 1.4470 -0.1238 0.0418  -0.0621 141 ASP   B C   
3009  O  O   . ASP   B  142 ? 2.0246 0.8159 1.4642 -0.1749 0.0397  -0.1046 141 ASP   B O   
3010  C  CB  . ASP   B  142 ? 2.0661 0.8310 1.5478 -0.1153 0.0279  -0.0567 141 ASP   B CB  
3011  C  CG  . ASP   B  142 ? 2.0774 0.8647 1.5866 -0.1490 0.0131  -0.0724 141 ASP   B CG  
3012  O  OD1 . ASP   B  142 ? 2.0341 0.7380 1.6536 -0.1624 -0.0118 0.0008  141 ASP   B OD1 
3013  O  OD2 . ASP   B  142 ? 2.1690 0.8991 1.6014 -0.1403 -0.0065 -0.2584 141 ASP   B OD2 
3014  N  N   . ARG   B  143 ? 1.9899 0.7061 1.4285 -0.1212 0.0293  -0.0240 142 ARG   B N   
3015  C  CA  . ARG   B  143 ? 2.0420 0.7369 1.3935 -0.1743 -0.0277 -0.0275 142 ARG   B CA  
3016  C  C   . ARG   B  143 ? 2.0908 0.8103 1.3066 -0.2040 0.0025  0.0403  142 ARG   B C   
3017  O  O   . ARG   B  143 ? 2.1846 0.9893 1.2878 -0.2229 -0.0460 -0.0015 142 ARG   B O   
3018  C  CB  . ARG   B  143 ? 1.9904 0.7013 1.4328 -0.1466 -0.0670 -0.0610 142 ARG   B CB  
3019  C  CG  . ARG   B  143 ? 2.0480 0.6818 1.4772 -0.0932 -0.0979 -0.0368 142 ARG   B CG  
3020  C  CD  . ARG   B  143 ? 2.0366 0.6577 1.5215 -0.0224 -0.1064 -0.0190 142 ARG   B CD  
3021  N  NE  . ARG   B  143 ? 2.1245 0.5728 1.5808 0.0385  -0.1202 0.0704  142 ARG   B NE  
3022  C  CZ  . ARG   B  143 ? 2.1364 0.5330 1.5995 0.1221  -0.1330 0.0914  142 ARG   B CZ  
3023  N  NH1 . ARG   B  143 ? 2.1845 0.6660 1.5689 0.1362  -0.1342 0.0515  142 ARG   B NH1 
3024  N  NH2 . ARG   B  143 ? 2.1778 0.3730 1.6580 0.1746  -0.1385 0.1132  142 ARG   B NH2 
3025  N  N   . TYR   B  144 ? 2.0673 0.7236 1.3482 -0.2074 0.0239  0.0630  143 TYR   B N   
3026  C  CA  . TYR   B  144 ? 2.0081 0.7147 1.3347 -0.2223 -0.0020 0.0627  143 TYR   B CA  
3027  C  C   . TYR   B  144 ? 2.0082 0.6380 1.3700 -0.2093 -0.0133 0.0986  143 TYR   B C   
3028  O  O   . TYR   B  144 ? 2.0881 0.6459 1.4172 -0.2100 0.0226  0.1098  143 TYR   B O   
3029  C  CB  . TYR   B  144 ? 1.9487 0.5805 1.3382 -0.2691 -0.0295 0.0680  143 TYR   B CB  
3030  C  CG  . TYR   B  144 ? 1.9579 0.5629 1.3217 -0.2652 -0.0585 0.0613  143 TYR   B CG  
3031  C  CD1 . TYR   B  144 ? 1.9269 0.5243 1.3093 -0.2775 -0.0486 0.0514  143 TYR   B CD1 
3032  C  CD2 . TYR   B  144 ? 1.8871 0.6374 1.3634 -0.2668 -0.0595 0.0417  143 TYR   B CD2 
3033  C  CE1 . TYR   B  144 ? 1.9338 0.5171 1.3204 -0.2713 -0.0765 0.0358  143 TYR   B CE1 
3034  C  CE2 . TYR   B  144 ? 1.8991 0.6749 1.3365 -0.2499 -0.1021 0.0199  143 TYR   B CE2 
3035  C  CZ  . TYR   B  144 ? 1.8682 0.5951 1.3322 -0.2768 -0.0924 0.0197  143 TYR   B CZ  
3036  O  OH  . TYR   B  144 ? 1.9019 0.6156 1.3933 -0.2742 -0.1679 -0.0693 143 TYR   B OH  
3037  N  N   . GLY   B  145 ? 2.0259 0.6428 1.3984 -0.1971 -0.0184 0.1076  144 GLY   B N   
3038  C  CA  . GLY   B  145 ? 1.9947 0.6135 1.4251 -0.1483 -0.0105 0.1305  144 GLY   B CA  
3039  C  C   . GLY   B  145 ? 1.9745 0.5365 1.4698 -0.0888 -0.0262 0.1348  144 GLY   B C   
3040  O  O   . GLY   B  145 ? 1.9783 0.4594 1.5144 0.0031  0.0396  0.1105  144 GLY   B O   
3041  N  N   . TYR   B  146 ? 1.9334 0.5105 1.4495 -0.0655 -0.0625 0.1049  145 TYR   B N   
3042  C  CA  . TYR   B  146 ? 1.8818 0.5031 1.4570 -0.1004 -0.0755 0.1081  145 TYR   B CA  
3043  C  C   . TYR   B  146 ? 1.8735 0.5260 1.3986 -0.0984 -0.0965 0.1139  145 TYR   B C   
3044  O  O   . TYR   B  146 ? 1.9055 0.5294 1.3526 -0.1343 -0.1307 0.0371  145 TYR   B O   
3045  C  CB  . TYR   B  146 ? 1.8870 0.5060 1.4839 -0.0975 -0.0510 0.1116  145 TYR   B CB  
3046  C  CG  . TYR   B  146 ? 1.8943 0.4676 1.5543 -0.1030 0.0048  0.0950  145 TYR   B CG  
3047  C  CD1 . TYR   B  146 ? 1.8991 0.4115 1.5957 -0.0902 0.0070  0.1174  145 TYR   B CD1 
3048  C  CD2 . TYR   B  146 ? 1.9194 0.4796 1.5361 -0.1188 0.0089  0.1027  145 TYR   B CD2 
3049  C  CE1 . TYR   B  146 ? 1.8886 0.4592 1.6453 -0.0881 0.0330  0.1280  145 TYR   B CE1 
3050  C  CE2 . TYR   B  146 ? 1.9197 0.4837 1.5847 -0.1203 0.0484  0.0991  145 TYR   B CE2 
3051  C  CZ  . TYR   B  146 ? 1.9015 0.4914 1.6387 -0.0856 0.0354  0.1230  145 TYR   B CZ  
3052  O  OH  . TYR   B  146 ? 1.8989 0.6087 1.7303 -0.0499 0.0597  0.1032  145 TYR   B OH  
3053  N  N   . GLN   B  147 ? 1.8443 0.5915 1.3595 -0.0856 -0.1208 0.1815  146 GLN   B N   
3054  C  CA  . GLN   B  147 ? 1.8468 0.6487 1.3465 -0.0503 -0.1500 0.1873  146 GLN   B CA  
3055  C  C   . GLN   B  147 ? 1.8321 0.6041 1.3712 -0.0955 -0.1384 0.1927  146 GLN   B C   
3056  O  O   . GLN   B  147 ? 1.7985 0.5897 1.4400 -0.0683 -0.1616 0.2026  146 GLN   B O   
3057  C  CB  . GLN   B  147 ? 1.7711 0.6805 1.3007 -0.0286 -0.1909 0.1448  146 GLN   B CB  
3058  C  CG  . GLN   B  147 ? 1.7941 0.8202 1.2693 0.0450  -0.2350 0.1094  146 GLN   B CG  
3059  C  CD  . GLN   B  147 ? 1.7258 0.8424 1.2664 0.0463  -0.2668 0.0636  146 GLN   B CD  
3060  O  OE1 . GLN   B  147 ? 1.7104 1.0048 1.1227 0.1189  -0.3582 -0.0302 146 GLN   B OE1 
3061  N  NE2 . GLN   B  147 ? 1.7779 0.8547 1.3191 0.0746  -0.2864 0.0574  146 GLN   B NE2 
3062  N  N   . LEU   B  148 ? 1.8256 0.5669 1.4100 -0.1545 -0.1197 0.1612  147 LEU   B N   
3063  C  CA  . LEU   B  148 ? 1.8141 0.5858 1.3629 -0.1354 -0.1277 0.1921  147 LEU   B CA  
3064  C  C   . LEU   B  148 ? 1.8001 0.5084 1.2963 -0.1265 -0.1734 0.2322  147 LEU   B C   
3065  O  O   . LEU   B  148 ? 1.8046 0.3826 1.3448 -0.1384 -0.1732 0.3300  147 LEU   B O   
3066  C  CB  . LEU   B  148 ? 1.8781 0.5847 1.4142 -0.1416 -0.1336 0.1975  147 LEU   B CB  
3067  C  CG  . LEU   B  148 ? 1.8890 0.6555 1.4170 -0.1396 -0.1415 0.1767  147 LEU   B CG  
3068  C  CD1 . LEU   B  148 ? 1.8968 0.6589 1.4272 -0.1690 -0.1267 0.1555  147 LEU   B CD1 
3069  C  CD2 . LEU   B  148 ? 1.9148 0.6542 1.4227 -0.1318 -0.1565 0.1805  147 LEU   B CD2 
3070  N  N   . TYR   B  149 ? 1.8184 0.5597 1.3037 -0.1047 -0.1455 0.1653  148 TYR   B N   
3071  C  CA  . TYR   B  149 ? 1.8123 0.4791 1.3096 -0.0848 -0.1816 0.1354  148 TYR   B CA  
3072  C  C   . TYR   B  149 ? 1.7831 0.3415 1.4079 -0.0785 -0.1784 0.1137  148 TYR   B C   
3073  O  O   . TYR   B  149 ? 1.8309 0.1291 1.4493 -0.0824 -0.2227 0.0720  148 TYR   B O   
3074  C  CB  . TYR   B  149 ? 1.8095 0.5006 1.2454 -0.0842 -0.1692 0.1526  148 TYR   B CB  
3075  C  CG  . TYR   B  149 ? 1.8173 0.5357 1.1596 -0.0460 -0.2026 0.1909  148 TYR   B CG  
3076  C  CD1 . TYR   B  149 ? 1.8715 0.5244 1.1167 -0.0002 -0.2069 0.2483  148 TYR   B CD1 
3077  C  CD2 . TYR   B  149 ? 1.8231 0.5920 1.1801 -0.0080 -0.1785 0.2063  148 TYR   B CD2 
3078  C  CE1 . TYR   B  149 ? 1.8841 0.5983 1.0617 0.0365  -0.2454 0.2628  148 TYR   B CE1 
3079  C  CE2 . TYR   B  149 ? 1.8341 0.6465 1.1218 0.0311  -0.2204 0.2294  148 TYR   B CE2 
3080  C  CZ  . TYR   B  149 ? 1.9005 0.6225 1.0643 0.0576  -0.2330 0.2713  148 TYR   B CZ  
3081  O  OH  . TYR   B  149 ? 1.8855 0.6366 0.9772 0.1012  -0.3221 0.3306  148 TYR   B OH  
3082  N  N   . THR   B  150 ? 1.7513 0.3024 1.3514 -0.1108 -0.2010 0.0743  149 THR   B N   
3083  C  CA  . THR   B  150 ? 1.7302 0.4027 1.3252 -0.1054 -0.1922 0.0829  149 THR   B CA  
3084  C  C   . THR   B  150 ? 1.7263 0.3906 1.2714 -0.1061 -0.2082 0.0521  149 THR   B C   
3085  O  O   . THR   B  150 ? 1.7760 0.3267 1.2808 -0.1017 -0.2354 -0.0156 149 THR   B O   
3086  C  CB  . THR   B  150 ? 1.7212 0.4113 1.3483 -0.1149 -0.2127 0.1470  149 THR   B CB  
3087  O  OG1 . THR   B  150 ? 1.7245 0.3829 1.4061 -0.0850 -0.2201 0.1841  149 THR   B OG1 
3088  C  CG2 . THR   B  150 ? 1.7237 0.4537 1.3874 -0.1248 -0.2086 0.1281  149 THR   B CG2 
3089  N  N   . SER   B  151 ? 1.7452 0.4169 1.2818 -0.0875 -0.1720 0.0732  150 SER   B N   
3090  C  CA  . SER   B  151 ? 1.7407 0.4397 1.2595 -0.0672 -0.1752 0.0743  150 SER   B CA  
3091  C  C   . SER   B  151 ? 1.6992 0.4538 1.2133 -0.0689 -0.1758 0.0940  150 SER   B C   
3092  O  O   . SER   B  151 ? 1.7560 0.4683 1.0893 -0.0810 -0.2140 0.0758  150 SER   B O   
3093  C  CB  . SER   B  151 ? 1.7124 0.4037 1.2791 -0.0533 -0.1734 0.0287  150 SER   B CB  
3094  O  OG  . SER   B  151 ? 1.7129 0.4214 1.3010 0.0114  -0.1686 0.0301  150 SER   B OG  
3095  N  N   . ASN   B  152 ? 1.7007 0.4016 1.1859 -0.0752 -0.1697 0.1048  151 ASN   B N   
3096  C  CA  . ASN   B  152 ? 1.6917 0.3982 1.1942 -0.0992 -0.1713 0.0967  151 ASN   B CA  
3097  C  C   . ASN   B  152 ? 1.6914 0.2959 1.1941 -0.0731 -0.1695 0.0956  151 ASN   B C   
3098  O  O   . ASN   B  152 ? 1.7383 0.2606 1.0923 -0.0829 -0.1367 0.1155  151 ASN   B O   
3099  C  CB  . ASN   B  152 ? 1.7201 0.4131 1.1958 -0.1317 -0.1644 0.1236  151 ASN   B CB  
3100  C  CG  . ASN   B  152 ? 1.7385 0.4850 1.1760 -0.1429 -0.1753 0.1296  151 ASN   B CG  
3101  O  OD1 . ASN   B  152 ? 1.7445 0.5822 1.1374 -0.1441 -0.1547 0.1063  151 ASN   B OD1 
3102  N  ND2 . ASN   B  152 ? 1.7959 0.5688 1.1827 -0.1347 -0.1833 0.1572  151 ASN   B ND2 
3103  N  N   . PRO   B  153 ? 1.6870 0.2788 1.2538 -0.0456 -0.1788 0.0566  152 PRO   B N   
3104  C  CA  . PRO   B  153 ? 1.6775 0.2851 1.3134 -0.0504 -0.1568 0.0385  152 PRO   B CA  
3105  C  C   . PRO   B  153 ? 1.6854 0.3003 1.3882 -0.0215 -0.1883 0.0234  152 PRO   B C   
3106  O  O   . PRO   B  153 ? 1.5995 0.4115 1.5053 -0.0845 -0.1043 -0.0937 152 PRO   B O   
3107  C  CB  . PRO   B  153 ? 1.6682 0.2881 1.3167 -0.0482 -0.1803 0.0315  152 PRO   B CB  
3108  C  CG  . PRO   B  153 ? 1.6673 0.2940 1.2987 -0.0545 -0.1871 0.0201  152 PRO   B CG  
3109  C  CD  . PRO   B  153 ? 1.6673 0.3016 1.2882 -0.0548 -0.1871 0.0455  152 PRO   B CD  
3110  N  N   . SER   B  154 ? 1.7073 0.3286 1.3941 -0.0134 -0.1515 0.0652  153 SER   B N   
3111  C  CA  . SER   B  154 ? 1.7206 0.4261 1.4063 0.0003  -0.1561 0.0421  153 SER   B CA  
3112  C  C   . SER   B  154 ? 1.7669 0.4276 1.4111 0.0199  -0.1809 0.0357  153 SER   B C   
3113  O  O   . SER   B  154 ? 1.7807 0.4894 1.4889 0.0245  -0.2533 -0.0179 153 SER   B O   
3114  C  CB  . SER   B  154 ? 1.7667 0.5250 1.3738 0.0407  -0.1236 0.0622  153 SER   B CB  
3115  O  OG  . SER   B  154 ? 1.8004 0.5828 1.4101 0.0497  -0.0897 0.0454  153 SER   B OG  
3116  N  N   . GLY   B  155 ? 1.7118 0.5551 1.4139 0.0042  -0.1665 0.0471  154 GLY   B N   
3117  C  CA  . GLY   B  155 ? 1.7582 0.6148 1.3341 -0.0204 -0.1801 0.0080  154 GLY   B CA  
3118  C  C   . GLY   B  155 ? 1.7865 0.5601 1.3350 -0.0432 -0.1992 0.1072  154 GLY   B C   
3119  O  O   . GLY   B  155 ? 1.8618 0.7588 1.1810 -0.0930 -0.2139 0.0388  154 GLY   B O   
3120  N  N   . ASN   B  156 ? 1.7924 0.5675 1.2710 -0.0184 -0.2542 0.1376  155 ASN   B N   
3121  C  CA  . ASN   B  156 ? 1.8223 0.6035 1.2633 -0.0420 -0.2405 0.0893  155 ASN   B CA  
3122  C  C   . ASN   B  156 ? 1.8020 0.4647 1.2472 -0.0584 -0.2603 0.0539  155 ASN   B C   
3123  O  O   . ASN   B  156 ? 1.7750 0.5646 1.2049 -0.0759 -0.2506 0.0791  155 ASN   B O   
3124  C  CB  . ASN   B  156 ? 1.9256 0.5848 1.3109 -0.0560 -0.2590 0.0973  155 ASN   B CB  
3125  C  CG  . ASN   B  156 ? 2.0359 0.6790 1.2985 -0.0203 -0.2807 0.0796  155 ASN   B CG  
3126  O  OD1 . ASN   B  156 ? 2.1623 0.6235 1.4213 -0.0696 -0.2740 -0.0656 155 ASN   B OD1 
3127  N  ND2 . ASN   B  156 ? 2.0659 0.5956 1.3152 -0.0493 -0.2596 0.1139  155 ASN   B ND2 
3128  N  N   . TYR   B  157 ? 1.7480 0.3317 1.2776 -0.0592 -0.2799 0.0607  156 TYR   B N   
3129  C  CA  . TYR   B  157 ? 1.7454 0.3463 1.2620 -0.0858 -0.2750 0.0591  156 TYR   B CA  
3130  C  C   . TYR   B  157 ? 1.7505 0.2916 1.2596 -0.1008 -0.2719 0.0446  156 TYR   B C   
3131  O  O   . TYR   B  157 ? 1.7351 0.3265 1.3187 -0.1167 -0.2755 0.0561  156 TYR   B O   
3132  C  CB  . TYR   B  157 ? 1.7497 0.3824 1.2344 -0.0652 -0.2986 0.1073  156 TYR   B CB  
3133  C  CG  . TYR   B  157 ? 1.7656 0.3969 1.1825 -0.0475 -0.3123 0.1083  156 TYR   B CG  
3134  C  CD1 . TYR   B  157 ? 1.7476 0.3667 1.1656 -0.0354 -0.3352 0.0976  156 TYR   B CD1 
3135  C  CD2 . TYR   B  157 ? 1.7817 0.3648 1.1803 -0.0396 -0.3147 0.1085  156 TYR   B CD2 
3136  C  CE1 . TYR   B  157 ? 1.7614 0.3766 1.1587 -0.0270 -0.3465 0.0938  156 TYR   B CE1 
3137  C  CE2 . TYR   B  157 ? 1.7922 0.3908 1.1733 -0.0429 -0.3314 0.1082  156 TYR   B CE2 
3138  C  CZ  . TYR   B  157 ? 1.7790 0.4329 1.1624 -0.0298 -0.3350 0.1002  156 TYR   B CZ  
3139  O  OH  . TYR   B  157 ? 1.8394 0.5956 1.1514 -0.0399 -0.3971 0.0380  156 TYR   B OH  
3140  N  N   . THR   B  158 ? 1.7677 0.2852 1.2806 -0.1032 -0.2412 0.0198  157 THR   B N   
3141  C  CA  . THR   B  158 ? 1.8098 0.3460 1.2921 -0.1010 -0.2051 0.0156  157 THR   B CA  
3142  C  C   . THR   B  158 ? 1.8456 0.3873 1.2967 -0.0975 -0.1470 0.0014  157 THR   B C   
3143  O  O   . THR   B  158 ? 1.8799 0.3370 1.2940 -0.1127 -0.1537 0.0578  157 THR   B O   
3144  C  CB  . THR   B  158 ? 1.8052 0.3470 1.3156 -0.0889 -0.2370 0.0031  157 THR   B CB  
3145  O  OG1 . THR   B  158 ? 1.8529 0.3146 1.3205 -0.0788 -0.2315 -0.0194 157 THR   B OG1 
3146  C  CG2 . THR   B  158 ? 1.8073 0.3293 1.3301 -0.0764 -0.2453 0.0229  157 THR   B CG2 
3147  N  N   . GLY   B  159 ? 1.8867 0.4767 1.3100 -0.0917 -0.1143 -0.0252 158 GLY   B N   
3148  C  CA  . GLY   B  159 ? 1.8838 0.5297 1.3309 -0.0978 -0.0925 0.0193  158 GLY   B CA  
3149  C  C   . GLY   B  159 ? 1.8591 0.4835 1.3222 -0.0498 -0.1140 0.0425  158 GLY   B C   
3150  O  O   . GLY   B  159 ? 2.0168 0.3085 1.3359 -0.0994 -0.1024 0.0524  158 GLY   B O   
3151  N  N   . TRP   B  160 ? 1.8463 0.5643 1.2861 -0.1286 -0.0790 0.0765  159 TRP   B N   
3152  C  CA  . TRP   B  160 ? 1.8629 0.6085 1.2449 -0.1268 -0.0703 0.1872  159 TRP   B CA  
3153  C  C   . TRP   B  160 ? 1.8525 0.7456 1.1941 -0.1845 -0.0505 0.2135  159 TRP   B C   
3154  O  O   . TRP   B  160 ? 1.7898 0.8309 1.1698 -0.1182 -0.0751 0.2340  159 TRP   B O   
3155  C  CB  . TRP   B  160 ? 1.8292 0.6503 1.2147 -0.1430 -0.0498 0.2062  159 TRP   B CB  
3156  C  CG  . TRP   B  160 ? 1.8368 0.6984 1.2505 -0.1305 -0.0267 0.2273  159 TRP   B CG  
3157  C  CD1 . TRP   B  160 ? 1.8043 0.7229 1.2570 -0.1225 0.0106  0.1943  159 TRP   B CD1 
3158  C  CD2 . TRP   B  160 ? 1.8667 0.6974 1.2339 -0.1229 0.0103  0.2498  159 TRP   B CD2 
3159  N  NE1 . TRP   B  160 ? 1.8458 0.6752 1.2275 -0.1081 0.0160  0.1956  159 TRP   B NE1 
3160  C  CE2 . TRP   B  160 ? 1.8880 0.7116 1.2179 -0.1217 0.0161  0.2231  159 TRP   B CE2 
3161  C  CE3 . TRP   B  160 ? 1.9229 0.6740 1.3329 -0.1943 0.0609  0.2645  159 TRP   B CE3 
3162  C  CZ2 . TRP   B  160 ? 1.9001 0.7064 1.2280 -0.1263 0.0324  0.2450  159 TRP   B CZ2 
3163  C  CZ3 . TRP   B  160 ? 1.9332 0.6953 1.3748 -0.1831 0.0816  0.2488  159 TRP   B CZ3 
3164  C  CH2 . TRP   B  160 ? 1.9557 0.7038 1.2898 -0.1799 0.0601  0.2608  159 TRP   B CH2 
3165  N  N   . LYS   B  161 ? 1.9109 0.7189 1.2216 -0.1503 -0.0718 0.2594  160 LYS   B N   
3166  C  CA  . LYS   B  161 ? 1.9435 0.7893 1.2858 -0.1295 -0.0256 0.2932  160 LYS   B CA  
3167  C  C   . LYS   B  161 ? 1.9730 0.7227 1.2826 -0.1129 -0.0312 0.3104  160 LYS   B C   
3168  O  O   . LYS   B  161 ? 2.0130 0.8275 1.3315 -0.0527 0.0075  0.4182  160 LYS   B O   
3169  C  CB  . LYS   B  161 ? 1.9573 0.8796 1.2752 -0.1430 -0.0083 0.3073  160 LYS   B CB  
3170  C  CG  . LYS   B  161 ? 1.9466 0.9315 1.2797 -0.1490 0.0027  0.2922  160 LYS   B CG  
3171  C  CD  . LYS   B  161 ? 1.9900 1.0206 1.2882 -0.1417 0.0060  0.3318  160 LYS   B CD  
3172  C  CE  . LYS   B  161 ? 1.9899 1.1311 1.2983 -0.1454 -0.0079 0.3186  160 LYS   B CE  
3173  N  NZ  . LYS   B  161 ? 2.0337 1.2269 1.2801 -0.1297 -0.0248 0.3384  160 LYS   B NZ  
3174  N  N   . ALA   B  162 ? 2.0014 0.6067 1.3461 -0.1439 -0.0165 0.3552  161 ALA   B N   
3175  C  CA  . ALA   B  162 ? 1.9810 0.4859 1.3906 -0.1732 0.0106  0.3287  161 ALA   B CA  
3176  C  C   . ALA   B  162 ? 1.9736 0.3879 1.3722 -0.1858 -0.0160 0.3179  161 ALA   B C   
3177  O  O   . ALA   B  162 ? 2.0120 0.3597 1.4129 -0.1677 -0.0232 0.3445  161 ALA   B O   
3178  C  CB  . ALA   B  162 ? 1.9706 0.5754 1.4478 -0.2104 0.0251  0.3195  161 ALA   B CB  
3179  N  N   . ILE   B  163 ? 1.8888 0.3809 1.3581 -0.1735 -0.0003 0.2292  162 ILE   B N   
3180  C  CA  . ILE   B  163 ? 1.8370 0.4408 1.3778 -0.1793 -0.0294 0.1688  162 ILE   B CA  
3181  C  C   . ILE   B  163 ? 1.7894 0.4621 1.4094 -0.1572 -0.0399 0.1382  162 ILE   B C   
3182  O  O   . ILE   B  163 ? 1.7552 0.5945 1.4278 -0.1426 -0.0437 0.1468  162 ILE   B O   
3183  C  CB  . ILE   B  163 ? 1.7962 0.4220 1.3361 -0.1572 -0.0272 0.1160  162 ILE   B CB  
3184  C  CG1 . ILE   B  163 ? 1.7715 0.4253 1.3378 -0.1586 -0.0446 0.1078  162 ILE   B CG1 
3185  C  CG2 . ILE   B  163 ? 1.7605 0.4123 1.3006 -0.1644 -0.0188 0.1027  162 ILE   B CG2 
3186  C  CD1 . ILE   B  163 ? 1.7809 0.4420 1.3481 -0.1480 -0.0549 0.1123  162 ILE   B CD1 
3187  N  N   . SER   B  164 ? 1.7780 0.4351 1.4483 -0.1992 -0.0778 0.0876  163 SER   B N   
3188  C  CA  . SER   B  164 ? 1.7593 0.4401 1.4872 -0.2204 -0.1125 0.0587  163 SER   B CA  
3189  C  C   . SER   B  164 ? 1.7612 0.3669 1.4363 -0.1949 -0.1345 0.0227  163 SER   B C   
3190  O  O   . SER   B  164 ? 1.7996 0.3184 1.4389 -0.1806 -0.1810 0.0104  163 SER   B O   
3191  C  CB  . SER   B  164 ? 1.7289 0.5134 1.5402 -0.2958 -0.0923 0.0532  163 SER   B CB  
3192  O  OG  . SER   B  164 ? 1.6946 0.5410 1.6084 -0.2744 -0.0907 0.0218  163 SER   B OG  
3193  N  N   . VAL   B  165 ? 1.7650 0.3365 1.4223 -0.1837 -0.1247 -0.0061 164 VAL   B N   
3194  C  CA  . VAL   B  165 ? 1.7612 0.4010 1.4418 -0.1649 -0.1098 -0.0027 164 VAL   B CA  
3195  C  C   . VAL   B  165 ? 1.7953 0.3980 1.4231 -0.1810 -0.1101 0.0272  164 VAL   B C   
3196  O  O   . VAL   B  165 ? 1.8001 0.4074 1.4814 -0.1584 -0.0959 0.0604  164 VAL   B O   
3197  C  CB  . VAL   B  165 ? 1.7022 0.4247 1.3883 -0.1906 -0.0986 -0.0301 164 VAL   B CB  
3198  C  CG1 . VAL   B  165 ? 1.6805 0.5616 1.3824 -0.1614 -0.1210 -0.0301 164 VAL   B CG1 
3199  C  CG2 . VAL   B  165 ? 1.6717 0.4895 1.3725 -0.1834 -0.1042 -0.0512 164 VAL   B CG2 
3200  N  N   . GLY   B  166 ? 1.7795 0.4495 1.4642 -0.1592 -0.0723 0.0791  165 GLY   B N   
3201  C  CA  . GLY   B  166 ? 1.8176 0.5587 1.5095 -0.1349 -0.0941 0.0188  165 GLY   B CA  
3202  C  C   . GLY   B  166 ? 1.8299 0.5553 1.6057 -0.0957 -0.1233 0.0188  165 GLY   B C   
3203  O  O   . GLY   B  166 ? 1.9153 0.5571 1.6604 0.0032  -0.1343 0.0016  165 GLY   B O   
3204  N  N   . ALA   B  167 ? 1.8376 0.6057 1.6743 -0.1450 -0.0908 -0.0015 166 ALA   B N   
3205  C  CA  . ALA   B  167 ? 1.8253 0.6152 1.6656 -0.1784 -0.0728 -0.0346 166 ALA   B CA  
3206  C  C   . ALA   B  167 ? 1.8516 0.6744 1.6981 -0.1934 -0.0471 0.0011  166 ALA   B C   
3207  O  O   . ALA   B  167 ? 1.8679 0.6493 1.7084 -0.2139 -0.0603 -0.0357 166 ALA   B O   
3208  C  CB  . ALA   B  167 ? 1.8176 0.6114 1.6739 -0.1813 -0.0632 -0.0758 166 ALA   B CB  
3209  N  N   . ASN   B  168 ? 1.8608 0.7044 1.7039 -0.1912 -0.0415 0.0572  167 ASN   B N   
3210  C  CA  . ASN   B  168 ? 1.9264 0.7729 1.7128 -0.1922 -0.0284 0.0866  167 ASN   B CA  
3211  C  C   . ASN   B  168 ? 1.8845 0.7283 1.6462 -0.2144 0.0037  0.1382  167 ASN   B C   
3212  O  O   . ASN   B  168 ? 1.9133 0.7734 1.5900 -0.2379 -0.0049 0.0894  167 ASN   B O   
3213  C  CB  . ASN   B  168 ? 1.9390 0.8893 1.8254 -0.2180 -0.0306 0.1121  167 ASN   B CB  
3214  C  CG  . ASN   B  168 ? 1.9989 0.9620 1.8438 -0.1763 -0.0298 0.0781  167 ASN   B CG  
3215  O  OD1 . ASN   B  168 ? 2.0162 1.0573 1.9736 -0.1110 0.0114  0.0820  167 ASN   B OD1 
3216  N  ND2 . ASN   B  168 ? 2.0338 1.0321 1.8888 -0.1926 -0.0671 0.1359  167 ASN   B ND2 
3217  N  N   . THR   B  169 ? 1.8723 0.7275 1.6293 -0.2054 0.0196  0.1494  168 THR   B N   
3218  C  CA  . THR   B  169 ? 1.9205 0.8505 1.5764 -0.1748 0.0325  0.1512  168 THR   B CA  
3219  C  C   . THR   B  169 ? 1.9669 0.7679 1.6726 -0.2212 0.0257  0.1914  168 THR   B C   
3220  O  O   . THR   B  169 ? 2.0050 0.7510 1.6602 -0.2767 0.0510  0.2270  168 THR   B O   
3221  C  CB  . THR   B  169 ? 1.8377 0.9278 1.5563 -0.1226 0.0771  0.1773  168 THR   B CB  
3222  O  OG1 . THR   B  169 ? 1.8354 1.0919 1.5573 -0.0887 0.1000  0.1303  168 THR   B OG1 
3223  C  CG2 . THR   B  169 ? 1.8320 0.9219 1.5611 -0.1254 0.0982  0.1880  168 THR   B CG2 
3224  N  N   . SER   B  170 ? 1.9753 0.8131 1.6547 -0.1903 -0.0068 0.1466  169 SER   B N   
3225  C  CA  . SER   B  170 ? 1.9855 0.8667 1.6549 -0.1976 -0.0454 0.1633  169 SER   B CA  
3226  C  C   . SER   B  170 ? 1.9579 0.8448 1.6997 -0.2188 -0.0815 0.1995  169 SER   B C   
3227  O  O   . SER   B  170 ? 1.9153 0.8490 1.7035 -0.2400 -0.0699 0.2098  169 SER   B O   
3228  C  CB  . SER   B  170 ? 2.0478 0.8618 1.6593 -0.2194 -0.0473 0.1118  169 SER   B CB  
3229  O  OG  . SER   B  170 ? 2.0850 0.9017 1.6370 -0.2013 -0.0889 0.0647  169 SER   B OG  
3230  N  N   . ALA   B  171 ? 1.9641 0.8487 1.6929 -0.2085 -0.0920 0.1917  170 ALA   B N   
3231  C  CA  . ALA   B  171 ? 1.9375 0.9294 1.6944 -0.2044 -0.0980 0.1350  170 ALA   B CA  
3232  C  C   . ALA   B  171 ? 1.9601 0.8869 1.6687 -0.2151 -0.1165 0.1417  170 ALA   B C   
3233  O  O   . ALA   B  171 ? 2.0182 0.9266 1.6700 -0.1915 -0.0917 0.1215  170 ALA   B O   
3234  C  CB  . ALA   B  171 ? 1.9457 0.9984 1.7138 -0.1984 -0.1107 0.1021  170 ALA   B CB  
3235  N  N   . ALA   B  172 ? 1.9022 0.8297 1.6444 -0.1890 -0.1175 0.0838  171 ALA   B N   
3236  C  CA  . ALA   B  172 ? 1.8967 0.8351 1.6388 -0.2083 -0.0859 0.0576  171 ALA   B CA  
3237  C  C   . ALA   B  172 ? 1.8961 0.7982 1.6347 -0.1878 -0.0583 0.0361  171 ALA   B C   
3238  O  O   . ALA   B  172 ? 1.9340 0.8220 1.6714 -0.1583 -0.0374 0.0218  171 ALA   B O   
3239  C  CB  . ALA   B  172 ? 1.8552 0.7356 1.6599 -0.2060 -0.0933 0.0301  171 ALA   B CB  
3240  N  N   . GLN   B  173 ? 1.8947 0.7424 1.6117 -0.2002 -0.0451 0.0416  172 GLN   B N   
3241  C  CA  . GLN   B  173 ? 1.9263 0.6909 1.5765 -0.2085 -0.0358 0.0707  172 GLN   B CA  
3242  C  C   . GLN   B  173 ? 1.9654 0.7522 1.5921 -0.2184 -0.0176 0.1018  172 GLN   B C   
3243  O  O   . GLN   B  173 ? 1.9797 0.7514 1.6344 -0.2509 0.0496  0.0830  172 GLN   B O   
3244  C  CB  . GLN   B  173 ? 1.9200 0.6485 1.5880 -0.1805 -0.0500 0.0420  172 GLN   B CB  
3245  C  CG  . GLN   B  173 ? 1.9333 0.6596 1.6044 -0.1815 -0.0620 0.0357  172 GLN   B CG  
3246  C  CD  . GLN   B  173 ? 1.9262 0.6358 1.6150 -0.2195 -0.0733 0.0276  172 GLN   B CD  
3247  O  OE1 . GLN   B  173 ? 1.9363 0.6048 1.5787 -0.2495 -0.0397 0.0560  172 GLN   B OE1 
3248  N  NE2 . GLN   B  173 ? 1.9284 0.5811 1.7049 -0.2437 -0.0668 0.0003  172 GLN   B NE2 
3249  N  N   . THR   B  174 ? 2.0080 0.7281 1.5191 -0.2438 -0.0305 0.1975  173 THR   B N   
3250  C  CA  . THR   B  174 ? 2.1123 0.7649 1.5368 -0.2391 -0.0733 0.2567  173 THR   B CA  
3251  C  C   . THR   B  174 ? 2.1475 0.6804 1.5687 -0.2436 -0.0340 0.2910  173 THR   B C   
3252  O  O   . THR   B  174 ? 2.2572 0.7247 1.5615 -0.2122 -0.0627 0.3385  173 THR   B O   
3253  C  CB  . THR   B  174 ? 2.0926 0.7756 1.4891 -0.2301 -0.0763 0.2668  173 THR   B CB  
3254  O  OG1 . THR   B  174 ? 2.0655 0.7899 1.3840 -0.2437 -0.1151 0.3545  173 THR   B OG1 
3255  C  CG2 . THR   B  174 ? 2.1518 0.8061 1.5270 -0.2409 -0.0760 0.2973  173 THR   B CG2 
3256  N  N   . LEU   B  175 ? 2.2314 0.6353 1.5558 -0.2494 -0.0667 0.2897  174 LEU   B N   
3257  C  CA  . LEU   B  175 ? 2.2463 0.6515 1.5932 -0.2288 -0.0545 0.3026  174 LEU   B CA  
3258  C  C   . LEU   B  175 ? 2.2519 0.6749 1.5973 -0.1431 -0.0519 0.2984  174 LEU   B C   
3259  O  O   . LEU   B  175 ? 2.2708 0.5329 1.5826 -0.1060 -0.0499 0.3218  174 LEU   B O   
3260  C  CB  . LEU   B  175 ? 2.2436 0.7188 1.6056 -0.2442 -0.0650 0.3464  174 LEU   B CB  
3261  C  CG  . LEU   B  175 ? 2.2767 0.7683 1.6266 -0.2912 -0.0723 0.3230  174 LEU   B CG  
3262  C  CD1 . LEU   B  175 ? 2.2769 0.7637 1.6341 -0.2729 -0.0711 0.3437  174 LEU   B CD1 
3263  C  CD2 . LEU   B  175 ? 2.3058 0.8442 1.6715 -0.3289 -0.0605 0.3520  174 LEU   B CD2 
3264  N  N   . LEU   B  176 ? 2.2104 0.6920 1.5694 -0.1494 -0.0495 0.2665  175 LEU   B N   
3265  C  CA  . LEU   B  176 ? 2.2083 0.7477 1.5343 -0.1610 -0.0373 0.2168  175 LEU   B CA  
3266  C  C   . LEU   B  176 ? 2.2081 0.7526 1.5334 -0.1749 -0.0327 0.2363  175 LEU   B C   
3267  O  O   . LEU   B  176 ? 2.1788 0.6836 1.4962 -0.2269 -0.0113 0.2945  175 LEU   B O   
3268  C  CB  . LEU   B  176 ? 2.1967 0.7420 1.4694 -0.1386 -0.0305 0.1937  175 LEU   B CB  
3269  C  CG  . LEU   B  176 ? 2.1960 0.7367 1.4506 -0.1340 -0.0162 0.1831  175 LEU   B CG  
3270  C  CD1 . LEU   B  176 ? 2.1756 0.7137 1.4149 -0.1203 -0.0133 0.1546  175 LEU   B CD1 
3271  C  CD2 . LEU   B  176 ? 2.1852 0.7762 1.4663 -0.1317 -0.0100 0.1816  175 LEU   B CD2 
3272  N  N   . GLN   B  177 ? 2.2141 0.7914 1.5337 -0.1519 -0.0229 0.1819  176 GLN   B N   
3273  C  CA  . GLN   B  177 ? 2.2298 0.8619 1.5334 -0.1019 -0.0267 0.1642  176 GLN   B CA  
3274  C  C   . GLN   B  177 ? 2.2717 0.9216 1.5257 -0.1349 -0.0222 0.1566  176 GLN   B C   
3275  O  O   . GLN   B  177 ? 2.3151 1.1497 1.5200 -0.1064 -0.0479 0.1808  176 GLN   B O   
3276  C  CB  . GLN   B  177 ? 2.2734 0.8609 1.5927 -0.0601 -0.0242 0.1649  176 GLN   B CB  
3277  C  CG  . GLN   B  177 ? 2.2618 0.9426 1.6229 0.0174  -0.0227 0.1464  176 GLN   B CG  
3278  C  CD  . GLN   B  177 ? 2.3193 1.0336 1.7163 0.0614  0.0463  0.1048  176 GLN   B CD  
3279  O  OE1 . GLN   B  177 ? 2.3493 1.2591 1.7346 0.1334  0.0411  0.1227  176 GLN   B OE1 
3280  N  NE2 . GLN   B  177 ? 2.2829 0.9989 1.7122 0.0680  0.0406  0.1092  176 GLN   B NE2 
3281  N  N   . MET   B  178 ? 2.3361 0.8288 1.5625 -0.1488 -0.0053 0.1438  177 MET   B N   
3282  C  CA  . MET   B  178 ? 2.4043 0.8813 1.6077 -0.1907 -0.0164 0.2101  177 MET   B CA  
3283  C  C   . MET   B  178 ? 2.4035 0.9403 1.5999 -0.2314 0.0416  0.1930  177 MET   B C   
3284  O  O   . MET   B  178 ? 2.4523 1.0212 1.6096 -0.2034 -0.0018 0.3007  177 MET   B O   
3285  C  CB  . MET   B  178 ? 2.3840 0.9404 1.6644 -0.2496 -0.0449 0.2203  177 MET   B CB  
3286  C  CG  . MET   B  178 ? 2.4371 0.9387 1.7593 -0.2777 -0.0742 0.2569  177 MET   B CG  
3287  S  SD  . MET   B  178 ? 2.5335 0.8523 1.8270 -0.2135 -0.1143 0.2728  177 MET   B SD  
3288  C  CE  . MET   B  178 ? 2.4905 0.9696 1.8199 -0.2167 -0.0915 0.2785  177 MET   B CE  
3289  N  N   . ASP   B  179 ? 2.3717 1.0144 1.6226 -0.2243 0.0225  0.1966  178 ASP   B N   
3290  C  CA  . ASP   B  179 ? 2.3434 1.0010 1.6401 -0.2940 0.0521  0.1300  178 ASP   B CA  
3291  C  C   . ASP   B  179 ? 2.2799 0.9927 1.6069 -0.2999 0.0954  0.1375  178 ASP   B C   
3292  O  O   . ASP   B  179 ? 2.3517 0.8125 1.6214 -0.3125 0.1031  0.0901  178 ASP   B O   
3293  C  CB  . ASP   B  179 ? 2.3259 0.8946 1.6885 -0.3373 0.0477  0.0657  178 ASP   B CB  
3294  C  CG  . ASP   B  179 ? 2.3737 0.8786 1.7237 -0.3077 0.0234  0.0334  178 ASP   B CG  
3295  O  OD1 . ASP   B  179 ? 2.4130 0.6905 1.7422 -0.3308 0.0030  -0.0465 178 ASP   B OD1 
3296  O  OD2 . ASP   B  179 ? 2.4351 0.7396 1.7233 -0.2803 0.0299  -0.0295 178 ASP   B OD2 
3297  N  N   . TYR   B  180 ? 2.2955 0.9249 1.5387 -0.3141 0.0755  0.1836  179 TYR   B N   
3298  C  CA  . TYR   B  180 ? 2.2320 0.9429 1.5609 -0.3156 0.0574  0.1711  179 TYR   B CA  
3299  C  C   . TYR   B  180 ? 2.2605 1.0549 1.5403 -0.3506 0.1163  0.2219  179 TYR   B C   
3300  O  O   . TYR   B  180 ? 2.2790 1.1379 1.6301 -0.2878 0.0928  0.2276  179 TYR   B O   
3301  C  CB  . TYR   B  180 ? 2.1426 0.9914 1.5049 -0.2877 0.0051  0.1376  179 TYR   B CB  
3302  C  CG  . TYR   B  180 ? 2.0968 0.9879 1.4633 -0.2955 -0.0287 0.1642  179 TYR   B CG  
3303  C  CD1 . TYR   B  180 ? 2.0681 0.9836 1.4199 -0.3203 -0.0121 0.1778  179 TYR   B CD1 
3304  C  CD2 . TYR   B  180 ? 2.0951 1.0083 1.4885 -0.3021 -0.0398 0.1579  179 TYR   B CD2 
3305  C  CE1 . TYR   B  180 ? 2.0323 0.9839 1.4054 -0.2675 -0.0387 0.1416  179 TYR   B CE1 
3306  C  CE2 . TYR   B  180 ? 2.0480 0.9978 1.4368 -0.2744 -0.0491 0.1656  179 TYR   B CE2 
3307  C  CZ  . TYR   B  180 ? 2.0210 0.9648 1.4101 -0.2537 -0.0345 0.1214  179 TYR   B CZ  
3308  O  OH  . TYR   B  180 ? 1.9546 0.9960 1.4024 -0.2279 -0.0452 0.0050  179 TYR   B OH  
3309  N  N   . LYS   B  181 ? 2.2722 1.1029 1.6234 -0.3686 0.1943  0.1818  180 LYS   B N   
3310  C  CA  . LYS   B  181 ? 2.3197 1.2034 1.6441 -0.3972 0.2220  0.1222  180 LYS   B CA  
3311  C  C   . LYS   B  181 ? 2.3391 1.2118 1.5943 -0.4067 0.1872  0.0444  180 LYS   B C   
3312  O  O   . LYS   B  181 ? 2.3578 1.0657 1.6779 -0.3925 0.2165  0.0962  180 LYS   B O   
3313  C  CB  . LYS   B  181 ? 2.3729 1.2709 1.7117 -0.3946 0.2709  0.1676  180 LYS   B CB  
3314  C  CG  . LYS   B  181 ? 2.3552 1.4663 1.7822 -0.3664 0.2693  0.1799  180 LYS   B CG  
3315  C  CD  . LYS   B  181 ? 2.3863 1.5702 1.8737 -0.3966 0.2999  0.2336  180 LYS   B CD  
3316  C  CE  . LYS   B  181 ? 2.4280 1.6303 1.8898 -0.3537 0.2899  0.2032  180 LYS   B CE  
3317  N  NZ  . LYS   B  181 ? 2.4354 1.6409 1.9342 -0.3548 0.2989  0.1657  180 LYS   B NZ  
3318  N  N   . ASP   B  182 ? 2.3887 1.3015 1.5807 -0.4063 0.1924  -0.0096 181 ASP   B N   
3319  C  CA  . ASP   B  182 ? 2.3217 1.2764 1.4700 -0.3678 0.1117  -0.1326 181 ASP   B CA  
3320  C  C   . ASP   B  182 ? 2.3195 1.3997 1.4778 -0.3332 0.1920  -0.1505 181 ASP   B C   
3321  O  O   . ASP   B  182 ? 2.3566 1.4435 1.3046 -0.2631 0.1324  -0.1939 181 ASP   B O   
3322  C  CB  . ASP   B  182 ? 2.3923 1.2744 1.4581 -0.4074 0.0926  -0.1815 181 ASP   B CB  
3323  C  CG  . ASP   B  182 ? 2.3766 1.1928 1.3805 -0.4411 0.0296  -0.2434 181 ASP   B CG  
3324  O  OD1 . ASP   B  182 ? 2.3434 1.0912 1.4141 -0.4981 -0.0013 -0.3148 181 ASP   B OD1 
3325  O  OD2 . ASP   B  182 ? 2.4676 1.2094 1.3654 -0.4837 -0.0144 -0.2559 181 ASP   B OD2 
3326  N  N   . ASP   B  183 ? 2.3475 1.3698 1.5558 -0.3180 0.2258  -0.0662 182 ASP   B N   
3327  C  CA  . ASP   B  183 ? 2.3038 1.4747 1.6878 -0.3116 0.2455  -0.0556 182 ASP   B CA  
3328  C  C   . ASP   B  183 ? 2.2538 1.4488 1.6060 -0.3329 0.3128  -0.0442 182 ASP   B C   
3329  O  O   . ASP   B  183 ? 2.2640 1.6354 1.6562 -0.2996 0.3875  -0.0300 182 ASP   B O   
3330  C  CB  . ASP   B  183 ? 2.3510 1.4886 1.6926 -0.3377 0.2284  -0.0503 182 ASP   B CB  
3331  C  CG  . ASP   B  183 ? 2.3787 1.4800 1.8637 -0.3661 0.1351  -0.1403 182 ASP   B CG  
3332  O  OD1 . ASP   B  183 ? 2.3325 1.4828 2.0353 -0.3992 0.0887  -0.2164 182 ASP   B OD1 
3333  O  OD2 . ASP   B  183 ? 2.4148 1.4027 1.8455 -0.3793 0.0893  -0.1891 182 ASP   B OD2 
3334  N  N   . MET   B  184 ? 2.1927 1.2762 1.6294 -0.3660 0.2954  -0.0303 183 MET   B N   
3335  C  CA  . MET   B  184 ? 2.1882 1.2511 1.7002 -0.3685 0.2515  -0.0384 183 MET   B CA  
3336  C  C   . MET   B  184 ? 2.1633 1.3590 1.6535 -0.2639 0.1982  -0.0557 183 MET   B C   
3337  O  O   . MET   B  184 ? 2.0899 1.4095 1.6846 -0.2478 0.1491  -0.0865 183 MET   B O   
3338  C  CB  . MET   B  184 ? 2.1933 1.1179 1.7274 -0.3543 0.2264  -0.0392 183 MET   B CB  
3339  C  CG  . MET   B  184 ? 2.2216 1.0458 1.7886 -0.3501 0.2182  -0.0336 183 MET   B CG  
3340  S  SD  . MET   B  184 ? 2.2448 0.9631 1.9444 -0.2533 0.2078  -0.0310 183 MET   B SD  
3341  C  CE  . MET   B  184 ? 2.2312 1.1325 1.9000 -0.2733 0.2001  -0.0656 183 MET   B CE  
3342  N  N   . LYS   B  185 ? 2.1830 1.3619 1.6634 -0.3190 0.1742  -0.0691 184 LYS   B N   
3343  C  CA  . LYS   B  185 ? 2.2355 1.3402 1.7193 -0.2964 0.1637  -0.0922 184 LYS   B CA  
3344  C  C   . LYS   B  185 ? 2.2810 1.2179 1.7110 -0.2651 0.0674  -0.0423 184 LYS   B C   
3345  O  O   . LYS   B  185 ? 2.3001 1.3566 1.7589 -0.2718 0.0828  -0.2123 184 LYS   B O   
3346  C  CB  . LYS   B  185 ? 2.2443 1.3862 1.7334 -0.3254 0.1969  -0.0922 184 LYS   B CB  
3347  C  CG  . LYS   B  185 ? 2.2805 1.5289 1.7105 -0.2828 0.2359  -0.0618 184 LYS   B CG  
3348  C  CD  . LYS   B  185 ? 2.3337 1.5228 1.7313 -0.2356 0.2464  -0.0476 184 LYS   B CD  
3349  C  CE  . LYS   B  185 ? 2.3571 1.6093 1.7022 -0.2138 0.2260  -0.0127 184 LYS   B CE  
3350  N  NZ  . LYS   B  185 ? 2.4338 1.6559 1.7121 -0.1944 0.2267  0.0228  184 LYS   B NZ  
3351  N  N   . VAL   B  186 ? 2.2912 1.2217 1.7759 -0.2302 -0.0043 -0.0259 185 VAL   B N   
3352  C  CA  . VAL   B  186 ? 2.2259 1.2099 1.7810 -0.2304 -0.0314 0.0461  185 VAL   B CA  
3353  C  C   . VAL   B  186 ? 2.1552 1.1062 1.8174 -0.2449 -0.0032 0.1777  185 VAL   B C   
3354  O  O   . VAL   B  186 ? 2.0832 1.1352 1.7379 -0.2047 -0.0102 0.2483  185 VAL   B O   
3355  C  CB  . VAL   B  186 ? 2.2341 1.2794 1.8109 -0.1996 -0.0434 0.0925  185 VAL   B CB  
3356  C  CG1 . VAL   B  186 ? 2.2267 1.3723 1.8079 -0.2002 -0.0296 0.0721  185 VAL   B CG1 
3357  C  CG2 . VAL   B  186 ? 2.2171 1.3675 1.8023 -0.2253 -0.0528 0.0772  185 VAL   B CG2 
3358  N  N   . ASP   B  187 ? 2.1851 1.0478 1.8366 -0.2871 0.0403  0.2102  186 ASP   B N   
3359  C  CA  . ASP   B  187 ? 2.1894 1.0955 1.8563 -0.3192 0.0666  0.1928  186 ASP   B CA  
3360  C  C   . ASP   B  187 ? 2.1272 1.0568 1.8345 -0.3773 0.0889  0.1679  186 ASP   B C   
3361  O  O   . ASP   B  187 ? 2.0796 0.9160 1.9114 -0.4483 0.0854  0.2169  186 ASP   B O   
3362  C  CB  . ASP   B  187 ? 2.1997 1.1668 1.8650 -0.3560 0.0822  0.1567  186 ASP   B CB  
3363  C  CG  . ASP   B  187 ? 2.2066 1.1196 1.8817 -0.4129 0.0781  0.0843  186 ASP   B CG  
3364  O  OD1 . ASP   B  187 ? 2.3264 0.9704 1.8991 -0.4760 0.2147  0.0938  186 ASP   B OD1 
3365  O  OD2 . ASP   B  187 ? 2.1762 1.2706 1.9711 -0.4533 0.0529  0.1010  186 ASP   B OD2 
3366  N  N   . ASP   B  188 ? 2.0748 0.9767 1.8171 -0.3219 0.1493  0.1863  187 ASP   B N   
3367  C  CA  . ASP   B  188 ? 2.0600 0.9566 1.7809 -0.3376 0.1582  0.1796  187 ASP   B CA  
3368  C  C   . ASP   B  188 ? 2.0121 0.9358 1.8048 -0.3327 0.1462  0.1848  187 ASP   B C   
3369  O  O   . ASP   B  188 ? 1.9569 0.9035 1.8124 -0.3367 0.2025  0.2233  187 ASP   B O   
3370  C  CB  . ASP   B  188 ? 2.0937 0.9379 1.7742 -0.2788 0.1570  0.1717  187 ASP   B CB  
3371  C  CG  . ASP   B  188 ? 2.1583 0.9703 1.7245 -0.2303 0.1497  0.1442  187 ASP   B CG  
3372  O  OD1 . ASP   B  188 ? 2.1598 0.9989 1.7758 -0.2400 0.1813  0.1077  187 ASP   B OD1 
3373  O  OD2 . ASP   B  188 ? 2.1730 0.9706 1.6796 -0.1744 0.0926  0.2029  187 ASP   B OD2 
3374  N  N   . ALA   B  189 ? 1.9477 0.9638 1.7899 -0.3346 0.1354  0.1393  188 ALA   B N   
3375  C  CA  . ALA   B  189 ? 1.9489 0.9585 1.7121 -0.3075 0.1029  0.1288  188 ALA   B CA  
3376  C  C   . ALA   B  189 ? 1.8951 0.8890 1.7082 -0.3008 0.1003  0.1358  188 ALA   B C   
3377  O  O   . ALA   B  189 ? 1.8675 0.8100 1.6468 -0.3004 0.0486  0.1654  188 ALA   B O   
3378  C  CB  . ALA   B  189 ? 1.9309 0.9862 1.7008 -0.3195 0.1155  0.1489  188 ALA   B CB  
3379  N  N   . ILE   B  190 ? 1.8963 0.9678 1.6980 -0.2928 0.0763  0.1424  189 ILE   B N   
3380  C  CA  . ILE   B  190 ? 1.9362 1.1161 1.7164 -0.2916 0.0601  0.1019  189 ILE   B CA  
3381  C  C   . ILE   B  190 ? 1.9251 1.1134 1.6982 -0.2778 0.0496  0.1283  189 ILE   B C   
3382  O  O   . ILE   B  190 ? 1.9310 1.1811 1.6575 -0.2292 0.0210  0.1553  189 ILE   B O   
3383  C  CB  . ILE   B  190 ? 1.9485 1.1951 1.8131 -0.2632 0.0761  0.0650  189 ILE   B CB  
3384  C  CG1 . ILE   B  190 ? 1.9764 1.2195 1.8323 -0.3020 0.0851  0.0563  189 ILE   B CG1 
3385  C  CG2 . ILE   B  190 ? 1.9817 1.2196 1.8306 -0.2789 0.0730  0.0399  189 ILE   B CG2 
3386  C  CD1 . ILE   B  190 ? 2.0004 1.2229 1.8509 -0.2890 0.0927  0.0338  189 ILE   B CD1 
3387  N  N   . GLU   B  191 ? 1.9129 1.1729 1.6810 -0.3014 0.0596  0.1144  190 GLU   B N   
3388  C  CA  . GLU   B  191 ? 1.9052 1.2114 1.6991 -0.3705 0.0573  0.0919  190 GLU   B CA  
3389  C  C   . GLU   B  191 ? 1.8824 1.1170 1.6673 -0.4151 0.0161  0.1102  190 GLU   B C   
3390  O  O   . GLU   B  191 ? 1.9162 1.1437 1.6547 -0.4703 -0.0100 0.1112  190 GLU   B O   
3391  C  CB  . GLU   B  191 ? 1.9311 1.3458 1.7290 -0.3615 0.0981  0.0776  190 GLU   B CB  
3392  C  CG  . GLU   B  191 ? 1.9502 1.4311 1.8133 -0.4190 0.0837  0.0705  190 GLU   B CG  
3393  C  CD  . GLU   B  191 ? 1.9835 1.6064 1.8268 -0.4012 0.1024  0.1041  190 GLU   B CD  
3394  O  OE1 . GLU   B  191 ? 1.9634 1.6658 1.8811 -0.3862 0.1132  0.0726  190 GLU   B OE1 
3395  O  OE2 . GLU   B  191 ? 2.0213 1.6474 1.8164 -0.4022 0.0528  0.1455  190 GLU   B OE2 
3396  N  N   . LEU   B  192 ? 1.8963 1.0389 1.6357 -0.4141 0.0193  0.1060  191 LEU   B N   
3397  C  CA  . LEU   B  192 ? 1.8937 0.9917 1.6270 -0.4278 0.0037  0.0970  191 LEU   B CA  
3398  C  C   . LEU   B  192 ? 1.8787 0.9775 1.6163 -0.3845 -0.0144 0.0944  191 LEU   B C   
3399  O  O   . LEU   B  192 ? 1.8845 0.9644 1.6323 -0.3748 -0.0153 0.1085  191 LEU   B O   
3400  C  CB  . LEU   B  192 ? 1.8532 0.9310 1.5895 -0.4150 0.0302  0.1120  191 LEU   B CB  
3401  C  CG  . LEU   B  192 ? 1.8623 0.8731 1.5837 -0.4228 0.0276  0.0926  191 LEU   B CG  
3402  C  CD1 . LEU   B  192 ? 1.8364 0.8938 1.5712 -0.3843 0.0123  0.0928  191 LEU   B CD1 
3403  C  CD2 . LEU   B  192 ? 1.8643 0.8582 1.5848 -0.4113 0.0069  0.0983  191 LEU   B CD2 
3404  N  N   . ALA   B  193 ? 1.8824 0.9805 1.5961 -0.3154 -0.0635 0.1160  192 ALA   B N   
3405  C  CA  . ALA   B  193 ? 1.8966 0.9698 1.5676 -0.2592 -0.0847 0.1187  192 ALA   B CA  
3406  C  C   . ALA   B  193 ? 1.9225 0.9878 1.5957 -0.2766 -0.0803 0.0924  192 ALA   B C   
3407  O  O   . ALA   B  193 ? 1.8529 1.0741 1.5369 -0.2800 -0.0866 0.0984  192 ALA   B O   
3408  C  CB  . ALA   B  193 ? 1.8854 0.9961 1.5514 -0.2143 -0.1072 0.1620  192 ALA   B CB  
3409  N  N   . LEU   B  194 ? 1.9327 1.0652 1.6822 -0.2453 -0.0505 0.0843  193 LEU   B N   
3410  C  CA  . LEU   B  194 ? 2.0356 1.1625 1.7309 -0.2807 -0.0669 0.0327  193 LEU   B CA  
3411  C  C   . LEU   B  194 ? 2.0370 1.1464 1.7611 -0.3546 -0.0620 0.0029  193 LEU   B C   
3412  O  O   . LEU   B  194 ? 2.0356 1.0017 1.7362 -0.4207 -0.0546 0.0641  193 LEU   B O   
3413  C  CB  . LEU   B  194 ? 2.0839 1.2787 1.8478 -0.2189 -0.0102 0.0156  193 LEU   B CB  
3414  C  CG  . LEU   B  194 ? 2.1532 1.2909 1.9084 -0.1569 0.0046  0.0031  193 LEU   B CG  
3415  C  CD1 . LEU   B  194 ? 2.1557 1.4098 1.9840 -0.1461 0.0244  -0.0043 193 LEU   B CD1 
3416  C  CD2 . LEU   B  194 ? 2.1375 1.3760 1.8950 -0.1288 0.0027  -0.0774 193 LEU   B CD2 
3417  N  N   . LYS   B  195 ? 2.0479 1.1843 1.7878 -0.3951 -0.0671 0.0331  194 LYS   B N   
3418  C  CA  . LYS   B  195 ? 2.0329 1.1490 1.9059 -0.4055 -0.0731 -0.0365 194 LYS   B CA  
3419  C  C   . LYS   B  195 ? 1.9855 1.1573 1.8775 -0.4180 -0.1189 -0.0556 194 LYS   B C   
3420  O  O   . LYS   B  195 ? 1.8784 1.2516 1.8722 -0.4560 -0.1491 -0.1535 194 LYS   B O   
3421  C  CB  . LYS   B  195 ? 2.0703 1.2570 1.9225 -0.4474 -0.0370 -0.0195 194 LYS   B CB  
3422  C  CG  . LYS   B  195 ? 2.0874 1.2939 1.9967 -0.5068 0.0083  0.0102  194 LYS   B CG  
3423  C  CD  . LYS   B  195 ? 2.1247 1.3261 2.0055 -0.5337 0.0353  0.0270  194 LYS   B CD  
3424  C  CE  . LYS   B  195 ? 2.2194 1.3363 2.0822 -0.5071 0.0446  0.0373  194 LYS   B CE  
3425  N  NZ  . LYS   B  195 ? 2.2046 1.4597 2.1357 -0.5164 0.0576  -0.0128 194 LYS   B NZ  
3426  N  N   . THR   B  196 ? 2.0025 0.9066 1.8201 -0.3701 -0.0876 0.0066  195 THR   B N   
3427  C  CA  . THR   B  196 ? 2.0455 0.8193 1.7850 -0.3475 -0.0664 0.0297  195 THR   B CA  
3428  C  C   . THR   B  196 ? 2.0412 0.8011 1.7584 -0.3507 -0.1061 0.0970  195 THR   B C   
3429  O  O   . THR   B  196 ? 2.0810 1.0461 1.7752 -0.1914 -0.0842 -0.0550 195 THR   B O   
3430  C  CB  . THR   B  196 ? 2.0457 0.7489 1.8124 -0.3455 -0.0574 0.0857  195 THR   B CB  
3431  O  OG1 . THR   B  196 ? 2.0977 0.8391 1.8105 -0.3266 -0.0028 0.1285  195 THR   B OG1 
3432  C  CG2 . THR   B  196 ? 2.0665 0.6842 1.8131 -0.3387 -0.0516 0.0642  195 THR   B CG2 
3433  N  N   . LEU   B  197 ? 1.9807 0.7377 1.7337 -0.3748 -0.0819 0.0685  196 LEU   B N   
3434  C  CA  . LEU   B  197 ? 1.9309 0.7703 1.7324 -0.3837 -0.0892 0.0850  196 LEU   B CA  
3435  C  C   . LEU   B  197 ? 1.9418 0.7852 1.6992 -0.4063 -0.0810 0.1004  196 LEU   B C   
3436  O  O   . LEU   B  197 ? 1.9957 0.8806 1.5802 -0.3924 -0.1247 0.1105  196 LEU   B O   
3437  C  CB  . LEU   B  197 ? 1.8541 0.7977 1.7198 -0.3667 -0.1002 0.0736  196 LEU   B CB  
3438  C  CG  . LEU   B  197 ? 1.8389 0.7361 1.6753 -0.3280 -0.0939 0.0579  196 LEU   B CG  
3439  C  CD1 . LEU   B  197 ? 1.7893 0.7532 1.6791 -0.3329 -0.1100 0.0594  196 LEU   B CD1 
3440  C  CD2 . LEU   B  197 ? 1.8278 0.6671 1.6481 -0.3498 -0.1028 0.0488  196 LEU   B CD2 
3441  N  N   . SER   B  198 ? 1.9687 0.9067 1.7584 -0.4364 -0.0460 0.1085  197 SER   B N   
3442  C  CA  . SER   B  198 ? 1.9928 0.9939 1.7947 -0.4869 -0.0235 0.0555  197 SER   B CA  
3443  C  C   . SER   B  198 ? 2.0383 0.9391 1.8375 -0.5263 -0.0041 0.0437  197 SER   B C   
3444  O  O   . SER   B  198 ? 2.0606 0.9896 1.8013 -0.5565 0.0087  0.0392  197 SER   B O   
3445  C  CB  . SER   B  198 ? 1.9793 1.0760 1.8055 -0.5597 -0.0188 0.0434  197 SER   B CB  
3446  O  OG  . SER   B  198 ? 1.9669 1.1410 1.7966 -0.5786 -0.0080 0.0285  197 SER   B OG  
3447  N  N   . LYS   B  199 ? 2.0453 0.8552 1.8577 -0.4612 0.0095  0.0931  198 LYS   B N   
3448  C  CA  . LYS   B  199 ? 2.0972 0.9301 1.8676 -0.3843 0.0226  0.1282  198 LYS   B CA  
3449  C  C   . LYS   B  199 ? 2.1141 0.9135 1.8379 -0.3083 0.0056  0.0989  198 LYS   B C   
3450  O  O   . LYS   B  199 ? 2.1354 0.9821 1.8141 -0.2246 0.0622  0.0799  198 LYS   B O   
3451  C  CB  . LYS   B  199 ? 2.1483 1.0317 1.8694 -0.3849 0.0178  0.1377  198 LYS   B CB  
3452  C  CG  . LYS   B  199 ? 2.1742 1.1969 1.8767 -0.3758 0.0353  0.1362  198 LYS   B CG  
3453  C  CD  . LYS   B  199 ? 2.2342 1.2947 1.8854 -0.3728 0.0065  0.1490  198 LYS   B CD  
3454  C  CE  . LYS   B  199 ? 2.2875 1.3147 1.9041 -0.3690 -0.0248 0.1916  198 LYS   B CE  
3455  N  NZ  . LYS   B  199 ? 2.3084 1.3343 1.9156 -0.3812 -0.0455 0.2154  198 LYS   B NZ  
3456  N  N   . THR   B  200 ? 2.0833 0.8007 1.8100 -0.2609 -0.0298 0.0092  199 THR   B N   
3457  C  CA  . THR   B  200 ? 2.1126 0.8784 1.7537 -0.1577 -0.0317 -0.0088 199 THR   B CA  
3458  C  C   . THR   B  200 ? 2.0851 0.8490 1.7559 -0.1665 -0.0558 0.0028  199 THR   B C   
3459  O  O   . THR   B  200 ? 2.0501 0.8973 1.7056 -0.1460 -0.0890 0.0677  199 THR   B O   
3460  C  CB  . THR   B  200 ? 2.1063 0.9400 1.7895 -0.1428 -0.0530 -0.0465 199 THR   B CB  
3461  O  OG1 . THR   B  200 ? 2.1029 0.9782 1.7618 -0.1294 -0.0483 0.1064  199 THR   B OG1 
3462  C  CG2 . THR   B  200 ? 2.1618 0.9933 1.8170 -0.1163 -0.0708 -0.0134 199 THR   B CG2 
3463  N  N   . THR   B  201 ? 2.1071 0.8408 1.7155 -0.1952 -0.0767 0.0473  200 THR   B N   
3464  C  CA  . THR   B  201 ? 2.1866 0.8988 1.7101 -0.2551 -0.0620 0.0735  200 THR   B CA  
3465  C  C   . THR   B  201 ? 2.2314 0.8963 1.7100 -0.2304 -0.0625 0.0911  200 THR   B C   
3466  O  O   . THR   B  201 ? 2.2594 0.9415 1.7581 -0.2563 -0.0268 0.1245  200 THR   B O   
3467  C  CB  . THR   B  201 ? 2.1621 0.8664 1.6059 -0.3110 -0.0825 0.0216  200 THR   B CB  
3468  O  OG1 . THR   B  201 ? 2.2016 0.7835 1.5423 -0.3352 -0.1349 -0.1241 200 THR   B OG1 
3469  C  CG2 . THR   B  201 ? 2.1901 0.9093 1.7042 -0.3601 -0.0743 -0.0009 200 THR   B CG2 
3470  N  N   . ASP   B  202 ? 2.2960 0.9492 1.7245 -0.2232 -0.0944 0.2512  201 ASP   B N   
3471  C  CA  . ASP   B  202 ? 2.3915 0.8981 1.7942 -0.2506 -0.1212 0.2478  201 ASP   B CA  
3472  C  C   . ASP   B  202 ? 2.4267 0.7139 1.8288 -0.3426 -0.1484 0.2445  201 ASP   B C   
3473  O  O   . ASP   B  202 ? 2.4739 0.7138 1.8046 -0.4469 -0.1765 0.2525  201 ASP   B O   
3474  C  CB  . ASP   B  202 ? 2.4238 1.0483 1.7982 -0.1781 -0.0841 0.2719  201 ASP   B CB  
3475  C  CG  . ASP   B  202 ? 2.4401 1.1438 1.7915 -0.1421 -0.0826 0.2837  201 ASP   B CG  
3476  O  OD1 . ASP   B  202 ? 2.5853 1.2524 1.8179 -0.1230 -0.0929 0.3365  201 ASP   B OD1 
3477  O  OD2 . ASP   B  202 ? 2.4416 1.1589 1.7157 -0.1100 -0.0260 0.2536  201 ASP   B OD2 
3478  N  N   . SER   B  203 ? 2.4050 0.7798 1.9257 -0.3121 -0.1789 0.2733  202 SER   B N   
3479  C  CA  . SER   B  203 ? 2.4604 0.9352 1.9575 -0.3124 -0.2451 0.2146  202 SER   B CA  
3480  C  C   . SER   B  203 ? 2.4626 0.8665 1.9368 -0.3074 -0.2436 0.1589  202 SER   B C   
3481  O  O   . SER   B  203 ? 2.4048 0.8048 1.9449 -0.2901 -0.2681 0.1217  202 SER   B O   
3482  C  CB  . SER   B  203 ? 2.4521 1.0341 2.0601 -0.2158 -0.3006 0.2576  202 SER   B CB  
3483  O  OG  . SER   B  203 ? 2.4920 1.1683 2.1065 -0.2157 -0.2911 0.3456  202 SER   B OG  
3484  N  N   . SER   B  204 ? 2.5381 1.0171 1.8627 -0.2531 -0.3064 0.1025  203 SER   B N   
3485  C  CA  . SER   B  204 ? 2.6022 1.1694 1.8772 -0.3043 -0.3051 0.1358  203 SER   B CA  
3486  C  C   . SER   B  204 ? 2.7209 1.2264 1.8971 -0.2550 -0.2915 0.1274  203 SER   B C   
3487  O  O   . SER   B  204 ? 2.9122 1.3878 1.9801 -0.3004 -0.2740 0.2392  203 SER   B O   
3488  C  CB  . SER   B  204 ? 2.6199 1.2519 1.8407 -0.2367 -0.3251 0.1164  203 SER   B CB  
3489  O  OG  . SER   B  204 ? 2.5895 1.2859 1.7167 -0.2605 -0.3574 0.1237  203 SER   B OG  
3490  N  N   . ALA   B  205 ? 2.7196 1.2371 1.9088 -0.2300 -0.3357 0.0790  204 ALA   B N   
3491  C  CA  . ALA   B  205 ? 2.7033 1.2884 1.8978 -0.2521 -0.3464 0.0385  204 ALA   B CA  
3492  C  C   . ALA   B  205 ? 2.6623 1.2812 1.8109 -0.2482 -0.3512 0.0167  204 ALA   B C   
3493  O  O   . ALA   B  205 ? 2.6189 1.1056 1.7939 -0.2535 -0.3714 -0.0293 204 ALA   B O   
3494  C  CB  . ALA   B  205 ? 2.6945 1.3831 1.9008 -0.2516 -0.3219 0.0131  204 ALA   B CB  
3495  N  N   . LEU   B  206 ? 2.6013 1.2253 1.9014 -0.2870 -0.3605 -0.0256 205 LEU   B N   
3496  C  CA  . LEU   B  206 ? 2.4563 1.2250 1.9642 -0.2847 -0.3489 0.0279  205 LEU   B CA  
3497  C  C   . LEU   B  206 ? 2.3978 1.3119 1.9191 -0.3025 -0.3686 -0.0198 205 LEU   B C   
3498  O  O   . LEU   B  206 ? 2.4131 1.3037 1.8999 -0.2098 -0.3602 0.0439  205 LEU   B O   
3499  C  CB  . LEU   B  206 ? 2.4246 1.1814 2.0096 -0.3133 -0.3650 0.0178  205 LEU   B CB  
3500  C  CG  . LEU   B  206 ? 2.3682 1.1943 2.0471 -0.2926 -0.3417 0.0213  205 LEU   B CG  
3501  C  CD1 . LEU   B  206 ? 2.3777 1.1691 2.0542 -0.2670 -0.3398 0.0043  205 LEU   B CD1 
3502  C  CD2 . LEU   B  206 ? 2.3913 1.2663 2.0213 -0.2623 -0.3226 0.0341  205 LEU   B CD2 
3503  N  N   . THR   B  207 ? 2.2703 1.3572 1.8439 -0.3725 -0.3328 -0.0487 206 THR   B N   
3504  C  CA  . THR   B  207 ? 2.1956 1.4060 1.8930 -0.3900 -0.3103 -0.0622 206 THR   B CA  
3505  C  C   . THR   B  207 ? 2.1129 1.4157 1.9207 -0.3919 -0.3207 -0.0071 206 THR   B C   
3506  O  O   . THR   B  207 ? 2.0936 1.5194 2.0322 -0.3801 -0.3773 0.0028  206 THR   B O   
3507  C  CB  . THR   B  207 ? 2.1858 1.5067 1.8808 -0.3567 -0.2879 -0.1092 206 THR   B CB  
3508  O  OG1 . THR   B  207 ? 2.1963 1.4437 1.8419 -0.3299 -0.2991 -0.1219 206 THR   B OG1 
3509  C  CG2 . THR   B  207 ? 2.1938 1.5511 1.8982 -0.4039 -0.2953 -0.1622 206 THR   B CG2 
3510  N  N   . TYR   B  208 ? 2.1005 1.3767 1.8945 -0.4135 -0.2907 0.0272  207 TYR   B N   
3511  C  CA  . TYR   B  208 ? 2.0782 1.3633 1.8122 -0.3895 -0.2420 0.0823  207 TYR   B CA  
3512  C  C   . TYR   B  208 ? 2.0618 1.1928 1.7882 -0.4150 -0.2744 0.0720  207 TYR   B C   
3513  O  O   . TYR   B  208 ? 2.0417 1.1547 1.5970 -0.4004 -0.2539 0.1230  207 TYR   B O   
3514  C  CB  . TYR   B  208 ? 2.0779 1.4245 1.8458 -0.3743 -0.2389 0.1197  207 TYR   B CB  
3515  C  CG  . TYR   B  208 ? 2.0726 1.4213 1.8447 -0.3749 -0.2339 0.1487  207 TYR   B CG  
3516  C  CD1 . TYR   B  208 ? 2.0665 1.4662 1.8846 -0.4115 -0.2085 0.1509  207 TYR   B CD1 
3517  C  CD2 . TYR   B  208 ? 2.0388 1.4065 1.8630 -0.3476 -0.2272 0.1527  207 TYR   B CD2 
3518  C  CE1 . TYR   B  208 ? 2.0330 1.4868 1.8969 -0.3948 -0.2083 0.1727  207 TYR   B CE1 
3519  C  CE2 . TYR   B  208 ? 2.0257 1.4290 1.8474 -0.3416 -0.2094 0.1719  207 TYR   B CE2 
3520  C  CZ  . TYR   B  208 ? 2.0059 1.4805 1.8687 -0.3601 -0.2116 0.1648  207 TYR   B CZ  
3521  O  OH  . TYR   B  208 ? 1.9419 1.5109 1.8623 -0.3545 -0.1853 0.2050  207 TYR   B OH  
3522  N  N   . ASP   B  209 ? 2.0695 1.1820 1.8241 -0.4561 -0.2490 0.0417  208 ASP   B N   
3523  C  CA  . ASP   B  209 ? 2.0574 1.1416 1.8699 -0.4761 -0.2420 0.0701  208 ASP   B CA  
3524  C  C   . ASP   B  209 ? 2.0744 1.1065 1.9226 -0.4248 -0.2751 0.1270  208 ASP   B C   
3525  O  O   . ASP   B  209 ? 2.0934 1.1023 1.9558 -0.4146 -0.2709 0.1517  208 ASP   B O   
3526  C  CB  . ASP   B  209 ? 2.0917 1.2370 1.8685 -0.5005 -0.2485 0.0556  208 ASP   B CB  
3527  C  CG  . ASP   B  209 ? 2.1929 1.2430 1.9206 -0.5135 -0.2372 -0.0084 208 ASP   B CG  
3528  O  OD1 . ASP   B  209 ? 2.2831 1.2341 1.9501 -0.5317 -0.1950 -0.0173 208 ASP   B OD1 
3529  O  OD2 . ASP   B  209 ? 2.2069 0.9917 1.9629 -0.5804 -0.2644 -0.0452 208 ASP   B OD2 
3530  N  N   . ARG   B  210 ? 2.0587 1.1828 1.9605 -0.3680 -0.2871 0.1459  209 ARG   B N   
3531  C  CA  . ARG   B  210 ? 2.1052 1.1297 1.9845 -0.2917 -0.2936 0.1299  209 ARG   B CA  
3532  C  C   . ARG   B  210 ? 2.0785 0.9119 1.9372 -0.2748 -0.2283 0.1565  209 ARG   B C   
3533  O  O   . ARG   B  210 ? 2.0980 0.6651 1.9659 -0.2849 -0.2461 0.1561  209 ARG   B O   
3534  C  CB  . ARG   B  210 ? 2.1841 1.1230 2.0933 -0.3141 -0.3473 0.0428  209 ARG   B CB  
3535  C  CG  . ARG   B  210 ? 2.2133 1.1734 2.1330 -0.2883 -0.3739 -0.0319 209 ARG   B CG  
3536  C  CD  . ARG   B  210 ? 2.2521 1.1625 2.2730 -0.2856 -0.4448 -0.0472 209 ARG   B CD  
3537  N  NE  . ARG   B  210 ? 2.1682 1.2886 2.3893 -0.2933 -0.4768 -0.0225 209 ARG   B NE  
3538  C  CZ  . ARG   B  210 ? 2.1236 1.4689 2.3943 -0.2310 -0.5515 -0.0446 209 ARG   B CZ  
3539  N  NH1 . ARG   B  210 ? 2.0833 1.5841 2.3865 -0.2273 -0.6125 -0.0748 209 ARG   B NH1 
3540  N  NH2 . ARG   B  210 ? 2.0451 1.3825 2.4942 -0.2661 -0.5937 -0.0847 209 ARG   B NH2 
3541  N  N   . LEU   B  211 ? 2.0271 0.9537 1.8888 -0.2985 -0.1823 0.1619  210 LEU   B N   
3542  C  CA  . LEU   B  211 ? 1.9788 1.1336 1.8365 -0.2657 -0.1443 0.1225  210 LEU   B CA  
3543  C  C   . LEU   B  211 ? 1.9388 1.1448 1.8067 -0.2522 -0.1233 0.1371  210 LEU   B C   
3544  O  O   . LEU   B  211 ? 1.8759 1.3121 1.8536 -0.2380 -0.0799 0.2033  210 LEU   B O   
3545  C  CB  . LEU   B  211 ? 1.9833 1.2230 1.8224 -0.2549 -0.1311 0.0904  210 LEU   B CB  
3546  C  CG  . LEU   B  211 ? 2.0470 1.2557 1.8252 -0.2103 -0.1514 0.0920  210 LEU   B CG  
3547  C  CD1 . LEU   B  211 ? 2.0599 1.3950 1.8521 -0.1907 -0.1202 0.0537  210 LEU   B CD1 
3548  C  CD2 . LEU   B  211 ? 2.0366 1.3144 1.8179 -0.1948 -0.1294 0.0517  210 LEU   B CD2 
3549  N  N   . GLU   B  212 ? 1.9764 1.2070 1.7580 -0.2656 -0.1205 0.0842  211 GLU   B N   
3550  C  CA  . GLU   B  212 ? 1.9756 1.2176 1.6973 -0.2430 -0.1142 0.0583  211 GLU   B CA  
3551  C  C   . GLU   B  212 ? 1.9215 1.0562 1.6758 -0.2496 -0.0558 0.1099  211 GLU   B C   
3552  O  O   . GLU   B  212 ? 1.8772 1.0365 1.5669 -0.3140 -0.0750 0.1039  211 GLU   B O   
3553  C  CB  . GLU   B  212 ? 1.9211 1.2687 1.7446 -0.2643 -0.1327 -0.0117 211 GLU   B CB  
3554  C  CG  . GLU   B  212 ? 1.9772 1.4139 1.7507 -0.2185 -0.2097 -0.0956 211 GLU   B CG  
3555  C  CD  . GLU   B  212 ? 1.9201 1.4223 1.7367 -0.2091 -0.2090 -0.1638 211 GLU   B CD  
3556  O  OE1 . GLU   B  212 ? 1.9179 1.7323 1.7502 -0.1448 -0.2152 -0.2149 211 GLU   B OE1 
3557  O  OE2 . GLU   B  212 ? 1.9358 1.4907 1.8638 -0.1557 -0.3316 -0.2892 211 GLU   B OE2 
3558  N  N   . PHE   B  213 ? 1.8939 1.0699 1.6216 -0.2123 -0.0298 0.1727  212 PHE   B N   
3559  C  CA  . PHE   B  213 ? 1.8868 1.0792 1.6038 -0.1812 -0.0593 0.2335  212 PHE   B CA  
3560  C  C   . PHE   B  213 ? 1.7965 1.0678 1.5285 -0.1507 -0.0550 0.2474  212 PHE   B C   
3561  O  O   . PHE   B  213 ? 1.7546 1.0401 1.5571 -0.1791 -0.1065 0.2211  212 PHE   B O   
3562  C  CB  . PHE   B  213 ? 1.9283 1.1522 1.6517 -0.1917 -0.0297 0.2886  212 PHE   B CB  
3563  C  CG  . PHE   B  213 ? 2.0372 1.2348 1.6731 -0.1535 -0.0512 0.3263  212 PHE   B CG  
3564  C  CD1 . PHE   B  213 ? 2.0718 1.2943 1.7048 -0.0844 -0.0546 0.3454  212 PHE   B CD1 
3565  C  CD2 . PHE   B  213 ? 2.1029 1.2441 1.7152 -0.1471 -0.0460 0.2952  212 PHE   B CD2 
3566  C  CE1 . PHE   B  213 ? 2.1502 1.3170 1.7438 -0.0738 -0.0579 0.3831  212 PHE   B CE1 
3567  C  CE2 . PHE   B  213 ? 2.1715 1.2708 1.7488 -0.1103 -0.0580 0.3263  212 PHE   B CE2 
3568  C  CZ  . PHE   B  213 ? 2.1925 1.3028 1.8440 -0.0645 -0.0488 0.3140  212 PHE   B CZ  
3569  N  N   . ALA   B  214 ? 1.7966 0.9853 1.4621 -0.0942 -0.0078 0.2460  213 ALA   B N   
3570  C  CA  . ALA   B  214 ? 1.7926 0.9635 1.4623 -0.0359 0.0065  0.2550  213 ALA   B CA  
3571  C  C   . ALA   B  214 ? 1.7945 0.9490 1.4614 -0.0401 -0.0029 0.2558  213 ALA   B C   
3572  O  O   . ALA   B  214 ? 1.6879 0.9973 1.4416 -0.0563 -0.0406 0.2328  213 ALA   B O   
3573  C  CB  . ALA   B  214 ? 1.7498 0.9347 1.4883 -0.0147 0.0179  0.2136  213 ALA   B CB  
3574  N  N   . THR   B  215 ? 1.8531 0.9632 1.4296 -0.0143 -0.0190 0.2550  214 THR   B N   
3575  C  CA  . THR   B  215 ? 1.9097 1.0060 1.4413 0.0151  -0.0252 0.2205  214 THR   B CA  
3576  C  C   . THR   B  215 ? 1.9010 0.9943 1.4469 0.0483  -0.0150 0.1793  214 THR   B C   
3577  O  O   . THR   B  215 ? 1.8565 1.0038 1.3848 0.0662  -0.0512 0.1292  214 THR   B O   
3578  C  CB  . THR   B  215 ? 1.9522 1.0418 1.4601 0.0155  0.0051  0.2413  214 THR   B CB  
3579  O  OG1 . THR   B  215 ? 1.9922 1.0266 1.4772 0.0475  0.0118  0.2381  214 THR   B OG1 
3580  C  CG2 . THR   B  215 ? 2.0203 1.0700 1.4724 -0.0287 0.0141  0.2206  214 THR   B CG2 
3581  N  N   . ILE   B  216 ? 1.9028 1.0285 1.4872 0.0379  -0.0160 0.1102  215 ILE   B N   
3582  C  CA  . ILE   B  216 ? 1.9337 1.0497 1.5598 0.0313  0.0398  0.0579  215 ILE   B CA  
3583  C  C   . ILE   B  216 ? 2.0545 1.1186 1.5359 0.0562  -0.0078 0.0474  215 ILE   B C   
3584  O  O   . ILE   B  216 ? 2.0920 1.0449 1.5633 0.1147  -0.0246 0.0004  215 ILE   B O   
3585  C  CB  . ILE   B  216 ? 1.9529 1.0838 1.5534 0.0150  0.1077  0.0329  215 ILE   B CB  
3586  C  CG1 . ILE   B  216 ? 1.9430 1.1724 1.5754 0.0013  0.1418  -0.0152 215 ILE   B CG1 
3587  C  CG2 . ILE   B  216 ? 1.9474 1.0961 1.5178 0.0276  0.1346  0.0070  215 ILE   B CG2 
3588  C  CD1 . ILE   B  216 ? 1.9416 1.2058 1.6230 -0.0015 0.1380  -0.0280 215 ILE   B CD1 
3589  N  N   . ARG   B  217 ? 2.0830 1.2145 1.6263 0.0913  0.0005  0.0250  216 ARG   B N   
3590  C  CA  . ARG   B  217 ? 2.1817 1.3516 1.6179 0.0475  0.0267  0.0439  216 ARG   B CA  
3591  C  C   . ARG   B  217 ? 2.2509 1.3736 1.7976 0.0452  -0.0111 0.0084  216 ARG   B C   
3592  O  O   . ARG   B  217 ? 2.2436 1.4888 1.7332 -0.0252 0.0146  -0.0040 216 ARG   B O   
3593  C  CB  . ARG   B  217 ? 2.1975 1.3250 1.5895 0.0030  0.0460  0.0394  216 ARG   B CB  
3594  C  CG  . ARG   B  217 ? 2.2174 1.3486 1.5843 -0.0421 0.0583  0.0521  216 ARG   B CG  
3595  C  CD  . ARG   B  217 ? 2.2101 1.4646 1.6441 -0.0106 0.0994  0.0596  216 ARG   B CD  
3596  N  NE  . ARG   B  217 ? 2.2652 1.4564 1.7363 -0.0051 0.1336  0.0592  216 ARG   B NE  
3597  C  CZ  . ARG   B  217 ? 2.3008 1.5953 1.6593 0.0408  0.1828  -0.0429 216 ARG   B CZ  
3598  N  NH1 . ARG   B  217 ? 2.2782 1.5486 1.6856 0.0246  0.1981  -0.0549 216 ARG   B NH1 
3599  N  NH2 . ARG   B  217 ? 2.3229 1.6526 1.7452 -0.0058 0.1799  -0.0346 216 ARG   B NH2 
3600  N  N   . LYS   B  218 ? 2.3383 1.5396 1.7974 0.0496  -0.0203 0.0374  217 LYS   B N   
3601  C  CA  . LYS   B  218 ? 2.3875 1.5480 1.9715 0.0975  -0.0928 -0.0031 217 LYS   B CA  
3602  C  C   . LYS   B  218 ? 2.4109 1.5988 2.1096 0.2358  -0.1172 -0.0158 217 LYS   B C   
3603  O  O   . LYS   B  218 ? 2.5657 1.5432 2.1381 0.3329  -0.1492 0.0026  217 LYS   B O   
3604  C  CB  . LYS   B  218 ? 2.3469 1.5804 1.9999 0.0339  -0.1119 0.0192  217 LYS   B CB  
3605  C  CG  . LYS   B  218 ? 2.3077 1.5915 2.0242 0.0045  -0.1978 0.0350  217 LYS   B CG  
3606  C  CD  . LYS   B  218 ? 2.3331 1.6258 2.0582 -0.0395 -0.2319 0.0439  217 LYS   B CD  
3607  C  CE  . LYS   B  218 ? 2.3270 1.5891 2.0718 -0.0654 -0.2410 0.0375  217 LYS   B CE  
3608  N  NZ  . LYS   B  218 ? 2.3755 1.5232 2.0726 -0.0604 -0.2508 0.0383  217 LYS   B NZ  
3609  N  N   . GLY   B  219 ? 2.4252 1.6916 2.2425 0.2554  -0.2196 -0.0429 218 GLY   B N   
3610  C  CA  . GLY   B  219 ? 2.4359 1.8276 2.4890 0.2060  -0.2300 -0.1046 218 GLY   B CA  
3611  C  C   . GLY   B  219 ? 2.5609 1.8006 2.7072 0.3292  -0.3148 -0.1900 218 GLY   B C   
3612  O  O   . GLY   B  219 ? 2.5637 1.6791 2.9445 0.1751  -0.2647 -0.2677 218 GLY   B O   
3613  N  N   . ALA   B  220 ? 2.5962 1.8371 2.8101 0.2685  -0.3390 -0.2970 219 ALA   B N   
3614  C  CA  . ALA   B  220 ? 2.6145 1.8852 2.7760 0.2957  -0.3278 -0.2626 219 ALA   B CA  
3615  C  C   . ALA   B  220 ? 2.6762 2.0402 2.8514 0.3505  -0.3107 -0.3411 219 ALA   B C   
3616  O  O   . ALA   B  220 ? 2.6784 1.9667 2.8238 0.3577  -0.2625 -0.4154 219 ALA   B O   
3617  C  CB  . ALA   B  220 ? 2.6236 1.8161 2.6360 0.3140  -0.3180 -0.2673 219 ALA   B CB  
3618  N  N   . ASN   B  221 ? 2.6333 2.0472 2.8117 0.3402  -0.2150 -0.2647 220 ASN   B N   
3619  C  CA  . ASN   B  221 ? 2.5056 2.2595 2.6339 0.0989  -0.1501 -0.2660 220 ASN   B CA  
3620  C  C   . ASN   B  221 ? 2.5297 1.9955 2.4698 0.0515  -0.0643 -0.1973 220 ASN   B C   
3621  O  O   . ASN   B  221 ? 2.3902 2.0558 2.3679 -0.1317 -0.1692 -0.2768 220 ASN   B O   
3622  C  CB  . ASN   B  221 ? 2.5714 2.5185 2.6785 0.2751  -0.0187 -0.1881 220 ASN   B CB  
3623  C  CG  . ASN   B  221 ? 2.5095 2.7453 2.6395 0.2566  0.0246  -0.2250 220 ASN   B CG  
3624  O  OD1 . ASN   B  221 ? 2.5936 2.7898 2.6747 0.2642  -0.0087 -0.2780 220 ASN   B OD1 
3625  N  ND2 . ASN   B  221 ? 2.5588 2.9267 2.6595 0.2998  0.0984  -0.1936 220 ASN   B ND2 
3626  N  N   . ASP   B  222 ? 2.3588 1.7877 2.3575 -0.0830 -0.0280 -0.2754 221 ASP   B N   
3627  C  CA  . ASP   B  222 ? 2.3765 1.8088 2.2440 -0.0956 -0.0084 -0.2072 221 ASP   B CA  
3628  C  C   . ASP   B  222 ? 2.3949 1.5351 2.2198 -0.0054 0.0230  -0.2653 221 ASP   B C   
3629  O  O   . ASP   B  222 ? 2.4974 1.5333 2.2390 0.0390  0.0060  -0.2470 221 ASP   B O   
3630  C  CB  . ASP   B  222 ? 2.2747 1.9037 2.1870 -0.0613 0.0758  -0.1911 221 ASP   B CB  
3631  C  CG  . ASP   B  222 ? 2.2688 2.0665 2.1868 -0.1399 0.0547  -0.0872 221 ASP   B CG  
3632  O  OD1 . ASP   B  222 ? 2.3206 2.0985 2.0839 -0.1850 0.0407  -0.0407 221 ASP   B OD1 
3633  O  OD2 . ASP   B  222 ? 2.2135 2.0275 2.1352 -0.1622 0.0745  -0.0395 221 ASP   B OD2 
3634  N  N   . GLY   B  223 ? 2.4296 1.4095 2.1182 -0.0246 0.0575  -0.2736 222 GLY   B N   
3635  C  CA  . GLY   B  223 ? 2.4142 1.3852 2.0338 0.0068  0.0552  -0.2649 222 GLY   B CA  
3636  C  C   . GLY   B  223 ? 2.3788 1.3662 2.0278 0.0434  0.0582  -0.2921 222 GLY   B C   
3637  O  O   . GLY   B  223 ? 2.3168 1.4774 1.9799 0.0514  0.0335  -0.3573 222 GLY   B O   
3638  N  N   . GLU   B  224 ? 2.3427 1.4015 1.9429 0.0878  0.0530  -0.2193 223 GLU   B N   
3639  C  CA  . GLU   B  224 ? 2.2730 1.3734 1.9418 0.1826  0.0376  -0.0720 223 GLU   B CA  
3640  C  C   . GLU   B  224 ? 2.1875 1.3328 1.8694 0.1555  0.0365  -0.0053 223 GLU   B C   
3641  O  O   . GLU   B  224 ? 2.1503 1.2174 1.8632 0.2075  0.0886  -0.0694 223 GLU   B O   
3642  C  CB  . GLU   B  224 ? 2.3136 1.4875 1.8896 0.2366  0.0660  -0.0091 223 GLU   B CB  
3643  C  CG  . GLU   B  224 ? 2.3000 1.6222 1.8596 0.2996  0.0572  0.0528  223 GLU   B CG  
3644  C  CD  . GLU   B  224 ? 2.3421 1.7187 1.8638 0.3900  0.0869  0.0570  223 GLU   B CD  
3645  O  OE1 . GLU   B  224 ? 2.2927 1.8297 1.8482 0.3437  0.1588  0.0789  223 GLU   B OE1 
3646  O  OE2 . GLU   B  224 ? 2.3469 1.9231 1.8672 0.3775  0.0900  0.0848  223 GLU   B OE2 
3647  N  N   . VAL   B  225 ? 2.1516 1.1537 1.7325 0.1306  -0.0589 0.0399  224 VAL   B N   
3648  C  CA  . VAL   B  225 ? 2.1055 1.0406 1.6968 0.0567  -0.1796 0.1419  224 VAL   B CA  
3649  C  C   . VAL   B  225 ? 2.0669 0.9713 1.7164 0.0681  -0.1978 0.2222  224 VAL   B C   
3650  O  O   . VAL   B  225 ? 2.0665 0.8988 1.6850 0.0695  -0.2568 0.1754  224 VAL   B O   
3651  C  CB  . VAL   B  225 ? 2.1002 1.0200 1.7566 0.0238  -0.1375 0.0999  224 VAL   B CB  
3652  C  CG1 . VAL   B  225 ? 2.1032 1.0840 1.6816 0.0043  -0.1393 0.0968  224 VAL   B CG1 
3653  C  CG2 . VAL   B  225 ? 2.0877 1.0411 1.7614 -0.0066 -0.1617 0.0754  224 VAL   B CG2 
3654  N  N   . TYR   B  226 ? 1.9982 1.0321 1.6653 0.0607  -0.2840 0.2788  225 TYR   B N   
3655  C  CA  . TYR   B  226 ? 1.9772 1.1082 1.7004 0.0590  -0.2996 0.2586  225 TYR   B CA  
3656  C  C   . TYR   B  226 ? 1.8842 0.9821 1.6546 -0.0489 -0.2845 0.3118  225 TYR   B C   
3657  O  O   . TYR   B  226 ? 1.8327 1.0119 1.5822 -0.0777 -0.3668 0.3064  225 TYR   B O   
3658  C  CB  . TYR   B  226 ? 1.9846 1.3077 1.8278 0.0926  -0.2996 0.2545  225 TYR   B CB  
3659  C  CG  . TYR   B  226 ? 2.0092 1.5294 1.9184 0.1231  -0.3563 0.1708  225 TYR   B CG  
3660  C  CD1 . TYR   B  226 ? 1.9931 1.6945 1.8339 0.1522  -0.3927 0.1683  225 TYR   B CD1 
3661  C  CD2 . TYR   B  226 ? 1.9470 1.5689 1.8962 0.1288  -0.3610 0.2133  225 TYR   B CD2 
3662  C  CE1 . TYR   B  226 ? 1.9255 1.8409 1.8758 0.1852  -0.4050 0.1503  225 TYR   B CE1 
3663  C  CE2 . TYR   B  226 ? 1.8676 1.7135 1.9600 0.1705  -0.3853 0.1917  225 TYR   B CE2 
3664  C  CZ  . TYR   B  226 ? 1.8404 1.8706 1.8467 0.2008  -0.4419 0.1762  225 TYR   B CZ  
3665  O  OH  . TYR   B  226 ? 1.7399 2.0438 1.9079 0.2039  -0.4346 0.1076  225 TYR   B OH  
3666  N  N   . GLN   B  227 ? 1.8399 0.8613 1.6834 -0.0600 -0.1847 0.2210  226 GLN   B N   
3667  C  CA  . GLN   B  227 ? 1.8756 0.8539 1.7442 -0.0274 -0.1050 0.2303  226 GLN   B CA  
3668  C  C   . GLN   B  227 ? 1.8613 0.9077 1.7434 -0.0211 -0.0853 0.2401  226 GLN   B C   
3669  O  O   . GLN   B  227 ? 1.9810 1.0378 1.7722 0.0636  -0.1071 0.2784  226 GLN   B O   
3670  C  CB  . GLN   B  227 ? 1.7802 0.7680 1.7712 -0.0243 -0.1199 0.1552  226 GLN   B CB  
3671  C  CG  . GLN   B  227 ? 1.7985 0.6975 1.7469 0.0106  -0.1310 0.1262  226 GLN   B CG  
3672  C  CD  . GLN   B  227 ? 1.7875 0.6773 1.7583 0.0529  -0.1071 0.0881  226 GLN   B CD  
3673  O  OE1 . GLN   B  227 ? 1.8707 0.7816 1.7376 0.0785  -0.0945 0.1521  226 GLN   B OE1 
3674  N  NE2 . GLN   B  227 ? 1.8199 0.5911 1.7353 0.0551  -0.1462 0.0827  226 GLN   B NE2 
3675  N  N   . LYS   B  228 ? 1.8656 0.8987 1.7257 -0.0142 -0.0383 0.2122  227 LYS   B N   
3676  C  CA  . LYS   B  228 ? 1.8490 0.9147 1.7117 0.0140  -0.0532 0.2016  227 LYS   B CA  
3677  C  C   . LYS   B  228 ? 1.8459 0.9602 1.6371 0.0020  -0.0523 0.2040  227 LYS   B C   
3678  O  O   . LYS   B  228 ? 1.8434 1.0080 1.6652 0.0608  -0.0529 0.2096  227 LYS   B O   
3679  C  CB  . LYS   B  228 ? 1.7996 0.9447 1.7891 -0.0019 -0.0381 0.1800  227 LYS   B CB  
3680  C  CG  . LYS   B  228 ? 1.7862 0.9994 1.8421 0.0167  -0.0440 0.1821  227 LYS   B CG  
3681  C  CD  . LYS   B  228 ? 1.7026 1.0852 1.8720 0.0073  -0.0376 0.1603  227 LYS   B CD  
3682  C  CE  . LYS   B  228 ? 1.7032 1.1352 1.9051 0.0288  -0.0304 0.1747  227 LYS   B CE  
3683  N  NZ  . LYS   B  228 ? 1.7122 1.1646 1.9066 0.0576  -0.0439 0.1700  227 LYS   B NZ  
3684  N  N   . ILE   B  229 ? 1.8522 0.9176 1.6440 0.0246  -0.0774 0.2213  228 ILE   B N   
3685  C  CA  . ILE   B  229 ? 1.8334 0.8841 1.6561 -0.0240 -0.0974 0.2069  228 ILE   B CA  
3686  C  C   . ILE   B  229 ? 1.8534 0.8758 1.6765 -0.0351 -0.1259 0.1702  228 ILE   B C   
3687  O  O   . ILE   B  229 ? 1.8775 0.7182 1.6966 -0.0797 -0.1425 0.1461  228 ILE   B O   
3688  C  CB  . ILE   B  229 ? 1.8359 0.9030 1.6040 0.0084  -0.0782 0.1562  228 ILE   B CB  
3689  C  CG1 . ILE   B  229 ? 1.8194 0.8958 1.5620 0.0184  -0.0810 0.1663  228 ILE   B CG1 
3690  C  CG2 . ILE   B  229 ? 1.8468 0.8869 1.5974 0.0091  -0.0780 0.1667  228 ILE   B CG2 
3691  C  CD1 . ILE   B  229 ? 1.8294 0.8400 1.5192 -0.0045 -0.0938 0.1560  228 ILE   B CD1 
3692  N  N   . PHE   B  230 ? 1.8165 0.8925 1.7064 -0.1126 -0.1314 0.1417  229 PHE   B N   
3693  C  CA  . PHE   B  230 ? 1.8217 1.0231 1.7489 -0.1526 -0.1362 0.1449  229 PHE   B CA  
3694  C  C   . PHE   B  230 ? 1.7927 1.0456 1.7650 -0.1586 -0.1821 0.2341  229 PHE   B C   
3695  O  O   . PHE   B  230 ? 1.6620 0.9715 1.6740 -0.1711 -0.2420 0.3113  229 PHE   B O   
3696  C  CB  . PHE   B  230 ? 1.8615 1.0045 1.7355 -0.2336 -0.0950 0.1153  229 PHE   B CB  
3697  C  CG  . PHE   B  230 ? 1.8781 1.0606 1.7369 -0.2644 -0.0785 0.0158  229 PHE   B CG  
3698  C  CD1 . PHE   B  230 ? 1.8527 1.0089 1.7180 -0.2630 -0.0582 0.0303  229 PHE   B CD1 
3699  C  CD2 . PHE   B  230 ? 1.8912 1.1784 1.7412 -0.2810 -0.0387 -0.0094 229 PHE   B CD2 
3700  C  CE1 . PHE   B  230 ? 1.8450 1.0563 1.7176 -0.2610 -0.0655 0.0281  229 PHE   B CE1 
3701  C  CE2 . PHE   B  230 ? 1.8851 1.1812 1.7415 -0.2838 -0.0392 -0.0127 229 PHE   B CE2 
3702  C  CZ  . PHE   B  230 ? 1.8688 1.1381 1.7242 -0.2783 -0.0287 0.0053  229 PHE   B CZ  
3703  N  N   . LYS   B  231 ? 1.8062 1.2099 1.8291 -0.1431 -0.2126 0.2574  230 LYS   B N   
3704  C  CA  . LYS   B  231 ? 1.8864 1.3363 1.8304 -0.1467 -0.2340 0.2677  230 LYS   B CA  
3705  C  C   . LYS   B  231 ? 1.9204 1.3283 1.8414 -0.1299 -0.2527 0.2620  230 LYS   B C   
3706  O  O   . LYS   B  231 ? 1.9618 1.2411 1.8919 -0.0677 -0.3471 0.3097  230 LYS   B O   
3707  C  CB  . LYS   B  231 ? 1.8949 1.3577 1.8551 -0.1395 -0.2297 0.3288  230 LYS   B CB  
3708  C  CG  . LYS   B  231 ? 1.9412 1.3409 1.8276 -0.1406 -0.2294 0.4022  230 LYS   B CG  
3709  C  CD  . LYS   B  231 ? 1.9327 1.4369 1.8411 -0.1267 -0.2142 0.4260  230 LYS   B CD  
3710  C  CE  . LYS   B  231 ? 1.9957 1.4515 1.8515 -0.1243 -0.1928 0.4041  230 LYS   B CE  
3711  N  NZ  . LYS   B  231 ? 2.0172 1.4805 1.8807 -0.1392 -0.1939 0.4266  230 LYS   B NZ  
3712  N  N   . PRO   B  232 ? 1.8891 1.5152 1.8629 -0.1308 -0.2155 0.1846  231 PRO   B N   
3713  C  CA  . PRO   B  232 ? 1.8792 1.5665 1.8916 -0.1832 -0.2363 0.1540  231 PRO   B CA  
3714  C  C   . PRO   B  232 ? 1.8413 1.7395 1.9739 -0.1806 -0.2127 0.1245  231 PRO   B C   
3715  O  O   . PRO   B  232 ? 1.9288 1.8278 2.0317 -0.1870 -0.3426 0.1899  231 PRO   B O   
3716  C  CB  . PRO   B  232 ? 1.8243 1.6308 1.8753 -0.1872 -0.2018 0.1306  231 PRO   B CB  
3717  C  CG  . PRO   B  232 ? 1.8122 1.5687 1.8690 -0.1495 -0.2023 0.1233  231 PRO   B CG  
3718  C  CD  . PRO   B  232 ? 1.8315 1.5065 1.8459 -0.1337 -0.1951 0.1604  231 PRO   B CD  
3719  N  N   . GLN   B  233 ? 1.9269 1.7109 1.9874 -0.1255 -0.1865 0.1230  232 GLN   B N   
3720  C  CA  . GLN   B  233 ? 1.9089 1.7623 1.9686 -0.0182 -0.1478 0.1040  232 GLN   B CA  
3721  C  C   . GLN   B  233 ? 1.9588 1.7482 1.9461 -0.0111 -0.1103 0.0960  232 GLN   B C   
3722  O  O   . GLN   B  233 ? 1.9561 1.7912 1.9249 -0.0457 -0.1290 0.0952  232 GLN   B O   
3723  C  CB  . GLN   B  233 ? 1.9022 1.8004 2.0193 0.0056  -0.1135 0.1282  232 GLN   B CB  
3724  C  CG  . GLN   B  233 ? 1.9094 1.8940 2.0687 0.0478  -0.0829 0.1487  232 GLN   B CG  
3725  C  CD  . GLN   B  233 ? 1.9411 1.8869 2.0883 0.0427  -0.0528 0.1873  232 GLN   B CD  
3726  O  OE1 . GLN   B  233 ? 1.9540 1.9223 2.1722 0.0595  0.0083  0.2408  232 GLN   B OE1 
3727  N  NE2 . GLN   B  233 ? 1.9823 1.9469 2.0715 0.0878  -0.0553 0.1968  232 GLN   B NE2 
3728  N  N   . GLU   B  234 ? 1.9835 1.6524 1.8613 0.0157  -0.0852 0.0940  233 GLU   B N   
3729  C  CA  . GLU   B  234 ? 2.0550 1.6148 1.8343 0.0047  -0.0392 0.0533  233 GLU   B CA  
3730  C  C   . GLU   B  234 ? 2.1245 1.6158 1.8417 0.0141  -0.0257 0.0758  233 GLU   B C   
3731  O  O   . GLU   B  234 ? 2.2397 1.6984 1.8221 0.0273  -0.0452 0.0788  233 GLU   B O   
3732  C  CB  . GLU   B  234 ? 2.0573 1.4985 1.7742 0.0777  -0.0187 0.0618  233 GLU   B CB  
3733  C  CG  . GLU   B  234 ? 2.0350 1.5446 1.7808 0.1034  -0.0333 0.0667  233 GLU   B CG  
3734  C  CD  . GLU   B  234 ? 2.0550 1.4767 1.7861 0.1785  -0.0372 0.0187  233 GLU   B CD  
3735  O  OE1 . GLU   B  234 ? 2.0690 1.6281 1.7845 0.1188  -0.0346 0.0294  233 GLU   B OE1 
3736  O  OE2 . GLU   B  234 ? 2.0474 1.3115 1.8785 0.1764  -0.1244 0.0749  233 GLU   B OE2 
3737  N  N   . ILE   B  235 ? 2.1463 1.5294 1.8678 -0.0035 -0.0068 0.0780  234 ILE   B N   
3738  C  CA  . ILE   B  235 ? 2.1990 1.4283 1.8579 -0.0648 -0.0024 0.0849  234 ILE   B CA  
3739  C  C   . ILE   B  235 ? 2.1931 1.3933 1.9465 -0.0494 -0.0670 0.0753  234 ILE   B C   
3740  O  O   . ILE   B  235 ? 2.1932 1.3616 1.9640 -0.0535 -0.0876 0.0604  234 ILE   B O   
3741  C  CB  . ILE   B  235 ? 2.2575 1.3263 1.8210 -0.0165 0.0029  0.0599  234 ILE   B CB  
3742  C  CG1 . ILE   B  235 ? 2.2480 1.2948 1.7947 0.0107  0.0021  -0.0139 234 ILE   B CG1 
3743  C  CG2 . ILE   B  235 ? 2.2918 1.2283 1.7827 -0.0952 0.0392  0.0720  234 ILE   B CG2 
3744  C  CD1 . ILE   B  235 ? 2.2199 1.2898 1.7970 0.0329  0.0029  -0.0463 234 ILE   B CD1 
3745  N  N   . LYS   B  236 ? 2.1696 1.4049 2.0110 -0.0935 -0.0850 0.0797  235 LYS   B N   
3746  C  CA  . LYS   B  236 ? 2.1817 1.4956 2.0625 -0.1369 -0.0907 0.0630  235 LYS   B CA  
3747  C  C   . LYS   B  236 ? 2.1700 1.5785 2.1167 -0.1799 -0.0442 0.0917  235 LYS   B C   
3748  O  O   . LYS   B  236 ? 2.1840 1.5624 2.0644 -0.1846 -0.0212 0.0587  235 LYS   B O   
3749  C  CB  . LYS   B  236 ? 2.2356 1.5303 2.1085 -0.1359 -0.1453 0.0668  235 LYS   B CB  
3750  C  CG  . LYS   B  236 ? 2.3033 1.5681 2.1525 -0.1584 -0.2089 0.0571  235 LYS   B CG  
3751  C  CD  . LYS   B  236 ? 2.3950 1.6453 2.1433 -0.1134 -0.2425 0.0840  235 LYS   B CD  
3752  C  CE  . LYS   B  236 ? 2.4385 1.6597 2.1251 -0.1229 -0.2907 0.0656  235 LYS   B CE  
3753  N  NZ  . LYS   B  236 ? 2.4747 1.6044 2.1050 -0.1225 -0.3616 0.0628  235 LYS   B NZ  
3754  N  N   . ASP   B  237 ? 2.0899 1.6349 2.1297 -0.1906 0.0138  0.0596  236 ASP   B N   
3755  C  CA  . ASP   B  237 ? 2.0106 1.6895 2.1889 -0.2248 0.0427  0.0554  236 ASP   B CA  
3756  C  C   . ASP   B  237 ? 2.0488 1.7351 2.2055 -0.2478 0.0277  0.0897  236 ASP   B C   
3757  O  O   . ASP   B  237 ? 2.0844 1.7239 2.2251 -0.2336 0.0324  0.1125  236 ASP   B O   
3758  C  CB  . ASP   B  237 ? 1.8646 1.6939 2.1575 -0.2348 0.0504  0.0425  236 ASP   B CB  
3759  C  CG  . ASP   B  237 ? 1.7478 1.6302 2.2237 -0.2324 0.0755  -0.0140 236 ASP   B CG  
3760  O  OD1 . ASP   B  237 ? 1.6395 1.7374 2.2496 -0.2746 0.0677  0.0232  236 ASP   B OD1 
3761  O  OD2 . ASP   B  237 ? 1.6461 1.5981 2.2322 -0.2231 0.0861  -0.1225 236 ASP   B OD2 
3762  N  N   . ILE   B  238 ? 2.0848 1.7424 2.3269 -0.3184 0.0821  0.0597  237 ILE   B N   
3763  C  CA  . ILE   B  238 ? 2.1519 1.6951 2.3348 -0.2906 0.0825  0.0561  237 ILE   B CA  
3764  C  C   . ILE   B  238 ? 2.1428 1.6396 2.3756 -0.3990 0.1837  0.0636  237 ILE   B C   
3765  O  O   . ILE   B  238 ? 2.0915 1.4976 2.4252 -0.4545 0.2967  0.1467  237 ILE   B O   
3766  C  CB  . ILE   B  238 ? 2.1311 1.8251 2.3269 -0.2999 0.0457  0.0106  237 ILE   B CB  
3767  C  CG1 . ILE   B  238 ? 2.1575 1.9648 2.3630 -0.2558 -0.0084 -0.0136 237 ILE   B CG1 
3768  C  CG2 . ILE   B  238 ? 2.1761 1.7836 2.2882 -0.2546 0.0242  0.0086  237 ILE   B CG2 
3769  C  CD1 . ILE   B  238 ? 2.1442 2.0517 2.3399 -0.2142 -0.0184 -0.0319 237 ILE   B CD1 
3770  N  N   . LEU   B  239 ? 2.1381 1.3803 2.4139 -0.3717 0.2134  0.0685  238 LEU   B N   
3771  C  CA  . LEU   B  239 ? 2.1739 1.3630 2.3938 -0.3734 0.1911  0.0897  238 LEU   B CA  
3772  C  C   . LEU   B  239 ? 2.1792 1.4091 2.4092 -0.3826 0.2126  0.0829  238 LEU   B C   
3773  O  O   . LEU   B  239 ? 2.2054 1.3771 2.4689 -0.4225 0.2385  0.0845  238 LEU   B O   
3774  C  CB  . LEU   B  239 ? 2.1312 1.1774 2.3825 -0.3674 0.1617  0.0975  238 LEU   B CB  
3775  C  CG  . LEU   B  239 ? 2.1344 1.0917 2.3417 -0.3976 0.1476  0.1023  238 LEU   B CG  
3776  C  CD1 . LEU   B  239 ? 2.1094 0.9576 2.3599 -0.4121 0.1746  0.1247  238 LEU   B CD1 
3777  C  CD2 . LEU   B  239 ? 2.1033 1.0335 2.3267 -0.3922 0.1335  0.1213  238 LEU   B CD2 
3778  N  N   . VAL   B  240 ? 2.1736 1.5894 2.3522 -0.3590 0.1802  0.0694  239 VAL   B N   
3779  C  CA  . VAL   B  240 ? 2.2061 1.6946 2.2939 -0.4048 0.1664  0.0849  239 VAL   B CA  
3780  C  C   . VAL   B  240 ? 2.2538 1.7081 2.2736 -0.4246 0.1767  0.1483  239 VAL   B C   
3781  O  O   . VAL   B  240 ? 2.2886 1.6945 2.2791 -0.4447 0.2160  0.1282  239 VAL   B O   
3782  C  CB  . VAL   B  240 ? 2.1972 1.7846 2.2814 -0.4030 0.1443  0.0692  239 VAL   B CB  
3783  C  CG1 . VAL   B  240 ? 2.1811 1.8050 2.3157 -0.4342 0.1376  0.0613  239 VAL   B CG1 
3784  C  CG2 . VAL   B  240 ? 2.1917 1.7981 2.2855 -0.3973 0.1123  0.0609  239 VAL   B CG2 
3785  N  N   . LYS   B  241 ? 2.2442 1.7956 2.1773 -0.4097 0.1169  0.0848  240 LYS   B N   
3786  C  CA  . LYS   B  241 ? 2.2163 1.8433 2.1397 -0.3588 0.1004  0.1497  240 LYS   B CA  
3787  C  C   . LYS   B  241 ? 2.1728 1.7844 2.0829 -0.3994 0.1562  0.1748  240 LYS   B C   
3788  O  O   . LYS   B  241 ? 2.0682 1.7276 2.1031 -0.4529 0.1228  0.2079  240 LYS   B O   
3789  C  CB  . LYS   B  241 ? 2.2768 1.8358 2.0871 -0.3142 0.0675  0.0959  240 LYS   B CB  
3790  C  CG  . LYS   B  241 ? 2.3065 1.8730 2.0505 -0.2979 0.0216  0.0844  240 LYS   B CG  
3791  C  CD  . LYS   B  241 ? 2.3176 1.8661 1.9812 -0.2506 -0.0152 0.0676  240 LYS   B CD  
3792  C  CE  . LYS   B  241 ? 2.3145 1.8361 1.9171 -0.2201 -0.0527 0.0728  240 LYS   B CE  
3793  N  NZ  . LYS   B  241 ? 2.3501 1.8521 1.9354 -0.1994 -0.0823 0.0717  240 LYS   B NZ  
3794  N  N   . THR   B  242 ? 2.1885 1.7327 2.0412 -0.3258 0.1086  0.2059  241 THR   B N   
3795  C  CA  . THR   B  242 ? 2.1653 1.7533 1.9747 -0.3130 0.1490  0.2102  241 THR   B CA  
3796  C  C   . THR   B  242 ? 2.1925 1.7374 1.9945 -0.3496 0.1616  0.2646  241 THR   B C   
3797  O  O   . THR   B  242 ? 2.1487 1.8155 1.9471 -0.4021 0.1424  0.3634  241 THR   B O   
3798  C  CB  . THR   B  242 ? 2.1200 1.7346 1.8937 -0.2197 0.1433  0.1884  241 THR   B CB  
3799  O  OG1 . THR   B  242 ? 2.0612 1.7154 1.8964 -0.2004 0.1477  0.1409  241 THR   B OG1 
3800  C  CG2 . THR   B  242 ? 2.0559 1.7328 1.8538 -0.1895 0.1474  0.1877  241 THR   B CG2 
3801  N  N   . GLY   B  243 ? 2.1906 1.7800 2.0236 -0.3962 0.1669  0.2587  242 GLY   B N   
3802  C  CA  . GLY   B  243 ? 2.2676 1.7598 2.0627 -0.4170 0.1900  0.2817  242 GLY   B CA  
3803  C  C   . GLY   B  243 ? 2.3468 1.6513 2.0706 -0.3901 0.1610  0.2877  242 GLY   B C   
3804  O  O   . GLY   B  243 ? 2.3856 1.6608 2.0294 -0.3362 0.2129  0.3667  242 GLY   B O   
3805  N  N   . ILE   B  244 ? 2.3503 1.5443 2.0616 -0.3432 0.1457  0.3014  243 ILE   B N   
3806  C  CA  . ILE   B  244 ? 2.3774 1.3908 2.0775 -0.2814 0.0734  0.3052  243 ILE   B CA  
3807  C  C   . ILE   B  244 ? 2.4947 1.3897 2.0516 -0.2270 0.0504  0.2757  243 ILE   B C   
3808  O  O   . ILE   B  244 ? 2.5873 1.5219 2.1146 -0.1923 0.0229  0.1395  243 ILE   B O   
3809  C  CB  . ILE   B  244 ? 2.3466 1.2542 2.0093 -0.2175 0.0689  0.3406  243 ILE   B CB  
3810  C  CG1 . ILE   B  244 ? 2.2973 1.1638 2.0404 -0.2576 0.0646  0.3742  243 ILE   B CG1 
3811  C  CG2 . ILE   B  244 ? 2.3382 1.1759 1.9853 -0.2118 0.0585  0.3622  243 ILE   B CG2 
3812  C  CD1 . ILE   B  244 ? 2.2801 1.1394 1.9958 -0.2393 0.0657  0.4139  243 ILE   B CD1 
3813  N  N   . THR   B  245 ? 2.5841 1.4529 1.9846 -0.2059 0.0401  0.4192  244 THR   B N   
3814  C  CA  . THR   B  245 ? 2.5448 1.4731 1.9054 -0.1554 0.0543  0.5306  244 THR   B CA  
3815  C  C   . THR   B  245 ? 2.5240 1.5223 1.9371 -0.1637 0.0751  0.6081  244 THR   B C   
3816  O  O   . THR   B  245 ? 2.3378 1.5532 1.9626 -0.0977 0.2204  0.6683  244 THR   B O   
3817  C  CB  . THR   B  245 ? 2.5508 1.5757 1.8088 -0.1235 -0.0349 0.5419  244 THR   B CB  
3818  O  OG1 . THR   B  245 ? 2.5304 1.5978 1.7008 -0.1226 -0.0625 0.5560  244 THR   B OG1 
3819  C  CG2 . THR   B  245 ? 2.5471 1.4523 1.7711 -0.1359 -0.0599 0.5364  244 THR   B CG2 
3820  N  N   . GLY   C  3   ? 1.7635 0.8746 1.4843 0.2250  -0.3992 0.3833  1   GLY   C N   
3821  C  CA  . GLY   C  3   ? 1.7199 0.9363 1.4147 0.1736  -0.4315 0.3306  1   GLY   C CA  
3822  C  C   . GLY   C  3   ? 1.6924 0.9238 1.3910 0.1157  -0.4235 0.2140  1   GLY   C C   
3823  O  O   . GLY   C  3   ? 1.7525 1.0117 1.2992 0.1092  -0.4576 0.1322  1   GLY   C O   
3824  N  N   . TYR   C  4   ? 1.6540 0.7483 1.4252 0.0458  -0.4490 0.1111  2   TYR   C N   
3825  C  CA  . TYR   C  4   ? 1.6466 0.7063 1.4345 0.0024  -0.4265 0.0499  2   TYR   C CA  
3826  C  C   . TYR   C  4   ? 1.6700 0.5550 1.4468 -0.0052 -0.4542 0.0000  2   TYR   C C   
3827  O  O   . TYR   C  4   ? 1.6901 0.4494 1.5337 -0.0085 -0.5112 -0.0316 2   TYR   C O   
3828  C  CB  . TYR   C  4   ? 1.5554 0.7763 1.4791 0.0075  -0.4184 0.0394  2   TYR   C CB  
3829  C  CG  . TYR   C  4   ? 1.5113 0.7791 1.4812 0.0133  -0.4115 0.0426  2   TYR   C CG  
3830  C  CD1 . TYR   C  4   ? 1.5038 0.7926 1.4654 -0.0129 -0.3948 0.0499  2   TYR   C CD1 
3831  C  CD2 . TYR   C  4   ? 1.5147 0.7490 1.5277 0.0396  -0.4281 0.0562  2   TYR   C CD2 
3832  C  CE1 . TYR   C  4   ? 1.5352 0.7925 1.4846 -0.0163 -0.3934 0.0626  2   TYR   C CE1 
3833  C  CE2 . TYR   C  4   ? 1.5575 0.7440 1.5725 0.0129  -0.4361 0.0396  2   TYR   C CE2 
3834  C  CZ  . TYR   C  4   ? 1.5556 0.8038 1.5178 0.0220  -0.4265 0.0485  2   TYR   C CZ  
3835  O  OH  . TYR   C  4   ? 1.5696 0.8203 1.5924 0.1032  -0.3844 -0.0723 2   TYR   C OH  
3836  N  N   . ASP   C  5   ? 1.7290 0.5917 1.4841 -0.0105 -0.4040 -0.0185 3   ASP   C N   
3837  C  CA  . ASP   C  5   ? 1.7380 0.6198 1.5504 -0.0403 -0.4067 -0.0063 3   ASP   C CA  
3838  C  C   . ASP   C  5   ? 1.7788 0.6551 1.5930 0.0301  -0.3790 -0.0164 3   ASP   C C   
3839  O  O   . ASP   C  5   ? 1.7572 0.3594 1.6221 -0.0247 -0.3537 -0.0643 3   ASP   C O   
3840  C  CB  . ASP   C  5   ? 1.8397 0.7247 1.5602 -0.0309 -0.3952 0.0297  3   ASP   C CB  
3841  C  CG  . ASP   C  5   ? 1.7954 0.8843 1.6186 -0.0077 -0.3957 0.0121  3   ASP   C CG  
3842  O  OD1 . ASP   C  5   ? 1.9164 1.1091 1.6819 0.0936  -0.3135 -0.0640 3   ASP   C OD1 
3843  O  OD2 . ASP   C  5   ? 1.9640 0.9958 1.5015 0.1720  -0.3919 0.0448  3   ASP   C OD2 
3844  N  N   . ARG   C  6   ? 1.7684 0.6408 1.6137 0.0406  -0.3567 0.0132  4   ARG   C N   
3845  C  CA  . ARG   C  6   ? 1.8193 0.6097 1.6804 0.0316  -0.2636 0.0211  4   ARG   C CA  
3846  C  C   . ARG   C  6   ? 1.7931 0.4947 1.7032 0.0580  -0.2534 0.0284  4   ARG   C C   
3847  O  O   . ARG   C  6   ? 1.7859 0.4961 1.8362 0.1067  -0.1844 -0.0378 4   ARG   C O   
3848  C  CB  . ARG   C  6   ? 1.8213 0.5688 1.7206 0.0492  -0.2759 -0.0133 4   ARG   C CB  
3849  C  CG  . ARG   C  6   ? 1.9175 0.7759 1.7048 0.0016  -0.2701 -0.0654 4   ARG   C CG  
3850  C  CD  . ARG   C  6   ? 1.9475 0.8456 1.7915 0.0534  -0.2681 -0.1034 4   ARG   C CD  
3851  N  NE  . ARG   C  6   ? 2.0314 0.9153 1.8355 0.0207  -0.2735 -0.1755 4   ARG   C NE  
3852  C  CZ  . ARG   C  6   ? 2.0943 0.9458 1.8843 0.0580  -0.2502 -0.2419 4   ARG   C CZ  
3853  N  NH1 . ARG   C  6   ? 2.0830 1.0825 1.9319 0.0316  -0.2721 -0.3083 4   ARG   C NH1 
3854  N  NH2 . ARG   C  6   ? 2.0682 1.1895 1.8303 -0.0543 -0.3054 -0.2519 4   ARG   C NH2 
3855  N  N   . ALA   C  7   ? 1.7852 0.4410 1.6777 0.0325  -0.2329 0.0436  5   ALA   C N   
3856  C  CA  . ALA   C  7   ? 1.8264 0.5699 1.6324 0.0034  -0.2496 0.0176  5   ALA   C CA  
3857  C  C   . ALA   C  7   ? 1.8517 0.6045 1.5799 -0.0416 -0.2355 -0.0053 5   ALA   C C   
3858  O  O   . ALA   C  7   ? 1.9488 0.4999 1.6193 -0.1316 -0.3388 -0.0183 5   ALA   C O   
3859  C  CB  . ALA   C  7   ? 1.8430 0.5483 1.6214 0.0057  -0.2205 0.0179  5   ALA   C CB  
3860  N  N   . LEU   C  8   ? 1.8268 0.6929 1.5914 -0.0936 -0.2245 0.0145  6   LEU   C N   
3861  C  CA  . LEU   C  8   ? 1.7834 0.6144 1.5679 -0.0829 -0.2436 -0.0436 6   LEU   C CA  
3862  C  C   . LEU   C  8   ? 1.8023 0.6970 1.5778 -0.0793 -0.2629 -0.0191 6   LEU   C C   
3863  O  O   . LEU   C  8   ? 1.8727 0.7073 1.7070 -0.1313 -0.2832 -0.0090 6   LEU   C O   
3864  C  CB  . LEU   C  8   ? 1.7892 0.6137 1.5230 -0.1173 -0.2328 -0.0645 6   LEU   C CB  
3865  C  CG  . LEU   C  8   ? 1.8523 0.6086 1.4135 -0.1361 -0.2307 -0.0472 6   LEU   C CG  
3866  C  CD1 . LEU   C  8   ? 1.8460 0.5984 1.4169 -0.0905 -0.2520 -0.0221 6   LEU   C CD1 
3867  C  CD2 . LEU   C  8   ? 1.8839 0.6412 1.3709 -0.1607 -0.2266 -0.0314 6   LEU   C CD2 
3868  N  N   . SER   C  9   ? 1.7581 0.6443 1.4666 -0.0115 -0.2868 0.0298  7   SER   C N   
3869  C  CA  . SER   C  9   ? 1.6932 0.7201 1.4948 -0.0202 -0.2694 0.0345  7   SER   C CA  
3870  C  C   . SER   C  9   ? 1.6629 0.7315 1.4879 -0.0599 -0.2898 0.0683  7   SER   C C   
3871  O  O   . SER   C  9   ? 1.6422 0.6914 1.4066 -0.0223 -0.3179 0.0546  7   SER   C O   
3872  C  CB  . SER   C  9   ? 1.7025 0.7299 1.5133 -0.0160 -0.2573 0.0187  7   SER   C CB  
3873  O  OG  . SER   C  9   ? 1.7285 0.8759 1.5584 -0.0173 -0.2184 0.0373  7   SER   C OG  
3874  N  N   . ILE   C  10  ? 1.6290 0.7177 1.5252 -0.0776 -0.2893 0.0717  8   ILE   C N   
3875  C  CA  . ILE   C  10  ? 1.6173 0.6492 1.5238 -0.0732 -0.3053 0.0762  8   ILE   C CA  
3876  C  C   . ILE   C  10  ? 1.6392 0.6274 1.5643 -0.0570 -0.3184 0.0525  8   ILE   C C   
3877  O  O   . ILE   C  10  ? 1.7019 0.6897 1.5874 -0.0962 -0.2966 0.0581  8   ILE   C O   
3878  C  CB  . ILE   C  10  ? 1.6032 0.6339 1.5307 -0.0808 -0.3183 0.0699  8   ILE   C CB  
3879  C  CG1 . ILE   C  10  ? 1.5956 0.6675 1.5910 -0.1152 -0.2981 0.1423  8   ILE   C CG1 
3880  C  CG2 . ILE   C  10  ? 1.5398 0.6184 1.5282 -0.1028 -0.3580 0.0477  8   ILE   C CG2 
3881  C  CD1 . ILE   C  10  ? 1.6243 0.7789 1.5561 -0.0849 -0.2707 0.1843  8   ILE   C CD1 
3882  N  N   . PHE   C  11  ? 1.6338 0.5774 1.5266 -0.0073 -0.3365 0.0606  9   PHE   C N   
3883  C  CA  . PHE   C  11  ? 1.6201 0.6763 1.5118 0.0325  -0.3611 0.0609  9   PHE   C CA  
3884  C  C   . PHE   C  11  ? 1.6592 0.7838 1.5203 -0.0128 -0.3895 -0.0028 9   PHE   C C   
3885  O  O   . PHE   C  11  ? 1.5398 0.9714 1.5478 -0.0455 -0.4942 -0.0166 9   PHE   C O   
3886  C  CB  . PHE   C  11  ? 1.6075 0.6083 1.4137 0.0548  -0.3985 0.0743  9   PHE   C CB  
3887  C  CG  . PHE   C  11  ? 1.5832 0.5783 1.3362 0.1046  -0.4360 0.1165  9   PHE   C CG  
3888  C  CD1 . PHE   C  11  ? 1.6300 0.5725 1.3248 0.1002  -0.4284 0.1078  9   PHE   C CD1 
3889  C  CD2 . PHE   C  11  ? 1.5500 0.5771 1.3196 0.1152  -0.4574 0.1121  9   PHE   C CD2 
3890  C  CE1 . PHE   C  11  ? 1.6355 0.5713 1.2996 0.1066  -0.4319 0.1159  9   PHE   C CE1 
3891  C  CE2 . PHE   C  11  ? 1.5629 0.6206 1.2570 0.1118  -0.4808 0.1268  9   PHE   C CE2 
3892  C  CZ  . PHE   C  11  ? 1.6163 0.5951 1.2538 0.1191  -0.4631 0.1470  9   PHE   C CZ  
3893  N  N   . SER   C  12  ? 1.7324 0.7279 1.6238 -0.0323 -0.3365 -0.0171 10  SER   C N   
3894  C  CA  . SER   C  12  ? 1.8012 0.7461 1.7096 -0.0165 -0.3232 -0.0657 10  SER   C CA  
3895  C  C   . SER   C  12  ? 1.8536 0.6038 1.7182 0.0165  -0.2415 -0.0643 10  SER   C C   
3896  O  O   . SER   C  12  ? 1.8527 0.6077 1.7955 0.0195  -0.2696 -0.0538 10  SER   C O   
3897  C  CB  . SER   C  12  ? 1.8132 0.7652 1.7613 -0.0283 -0.2797 -0.1012 10  SER   C CB  
3898  O  OG  . SER   C  12  ? 1.8279 0.9313 1.8294 0.0142  -0.2918 -0.1455 10  SER   C OG  
3899  N  N   . PRO   C  13  ? 1.9141 0.4757 1.7064 -0.0598 -0.2474 -0.0243 11  PRO   C N   
3900  C  CA  . PRO   C  13  ? 1.9635 0.4018 1.7178 -0.0200 -0.2312 -0.0241 11  PRO   C CA  
3901  C  C   . PRO   C  13  ? 2.0095 0.3753 1.7327 0.0074  -0.2482 -0.0198 11  PRO   C C   
3902  O  O   . PRO   C  13  ? 1.9795 0.3773 1.7299 0.1050  -0.2355 0.0446  11  PRO   C O   
3903  C  CB  . PRO   C  13  ? 1.9997 0.4314 1.7364 -0.0310 -0.2272 -0.0522 11  PRO   C CB  
3904  C  CG  . PRO   C  13  ? 1.9889 0.4095 1.7163 -0.0349 -0.2096 -0.0476 11  PRO   C CG  
3905  C  CD  . PRO   C  13  ? 1.9502 0.3560 1.7004 -0.0591 -0.2257 -0.0395 11  PRO   C CD  
3906  N  N   . ASP   C  14  ? 2.0446 0.4496 1.7493 -0.0836 -0.2442 -0.0321 12  ASP   C N   
3907  C  CA  . ASP   C  14  ? 2.0948 0.6950 1.7543 -0.1348 -0.2827 -0.0237 12  ASP   C CA  
3908  C  C   . ASP   C  14  ? 2.0526 0.7112 1.6775 -0.0987 -0.3104 -0.0157 12  ASP   C C   
3909  O  O   . ASP   C  14  ? 2.0661 0.7887 1.7035 -0.1482 -0.3502 -0.0548 12  ASP   C O   
3910  C  CB  . ASP   C  14  ? 2.1998 0.8682 1.8063 -0.2322 -0.2795 0.0335  12  ASP   C CB  
3911  C  CG  . ASP   C  14  ? 2.1839 0.9753 1.8818 -0.2713 -0.2863 0.0491  12  ASP   C CG  
3912  O  OD1 . ASP   C  14  ? 2.3299 0.8373 1.9488 -0.3927 -0.3091 0.0643  12  ASP   C OD1 
3913  O  OD2 . ASP   C  14  ? 2.2625 1.1571 1.9647 -0.4467 -0.3126 0.0938  12  ASP   C OD2 
3914  N  N   . GLY   C  15  ? 2.0566 0.6812 1.5824 -0.1097 -0.2958 -0.0442 13  GLY   C N   
3915  C  CA  . GLY   C  15  ? 2.0158 0.6156 1.5588 -0.1227 -0.2612 0.0274  13  GLY   C CA  
3916  C  C   . GLY   C  15  ? 2.0121 0.5860 1.5830 -0.1184 -0.2551 0.0209  13  GLY   C C   
3917  O  O   . GLY   C  15  ? 2.0554 0.4355 1.6544 -0.1917 -0.2237 0.0661  13  GLY   C O   
3918  N  N   . HIS   C  16  ? 1.9203 0.6974 1.5317 -0.0464 -0.2540 -0.0138 14  HIS   C N   
3919  C  CA  . HIS   C  16  ? 1.9127 0.7726 1.5119 0.0081  -0.2798 -0.0204 14  HIS   C CA  
3920  C  C   . HIS   C  16  ? 1.8528 0.6869 1.4383 -0.0415 -0.2731 -0.0711 14  HIS   C C   
3921  O  O   . HIS   C  16  ? 1.8881 0.7894 1.4319 -0.1186 -0.2079 -0.0303 14  HIS   C O   
3922  C  CB  . HIS   C  16  ? 1.9356 0.7864 1.5680 0.0221  -0.2178 -0.0121 14  HIS   C CB  
3923  C  CG  . HIS   C  16  ? 2.0140 0.8421 1.6336 0.1379  -0.1838 0.0032  14  HIS   C CG  
3924  N  ND1 . HIS   C  16  ? 2.0680 0.8541 1.7065 0.1380  -0.1403 -0.0524 14  HIS   C ND1 
3925  C  CD2 . HIS   C  16  ? 2.0215 0.8590 1.6724 0.1698  -0.2001 -0.0372 14  HIS   C CD2 
3926  C  CE1 . HIS   C  16  ? 2.0773 0.9892 1.7339 0.1569  -0.1644 -0.0487 14  HIS   C CE1 
3927  N  NE2 . HIS   C  16  ? 2.0299 0.9309 1.7190 0.2171  -0.2206 -0.0097 14  HIS   C NE2 
3928  N  N   . ILE   C  17  ? 1.8328 0.6129 1.4158 -0.0219 -0.3292 -0.0417 15  ILE   C N   
3929  C  CA  . ILE   C  17  ? 1.8550 0.6318 1.3798 -0.0112 -0.3364 -0.0143 15  ILE   C CA  
3930  C  C   . ILE   C  17  ? 1.8598 0.4982 1.4091 0.0147  -0.3249 -0.0078 15  ILE   C C   
3931  O  O   . ILE   C  17  ? 1.8422 0.5432 1.4341 -0.0163 -0.2549 0.0404  15  ILE   C O   
3932  C  CB  . ILE   C  17  ? 1.7856 0.6322 1.3580 0.0113  -0.4201 0.0000  15  ILE   C CB  
3933  C  CG1 . ILE   C  17  ? 1.7783 0.6375 1.3402 0.0081  -0.4501 0.0069  15  ILE   C CG1 
3934  C  CG2 . ILE   C  17  ? 1.7824 0.6780 1.3293 0.0203  -0.4142 0.0101  15  ILE   C CG2 
3935  C  CD1 . ILE   C  17  ? 1.7508 0.6116 1.3095 0.0095  -0.4736 0.0438  15  ILE   C CD1 
3936  N  N   . PHE   C  18  ? 1.8545 0.4152 1.4064 0.0823  -0.3026 -0.0248 16  PHE   C N   
3937  C  CA  . PHE   C  18  ? 1.8490 0.4748 1.4551 0.0696  -0.2864 -0.0506 16  PHE   C CA  
3938  C  C   . PHE   C  18  ? 1.8496 0.4359 1.4507 0.0595  -0.3283 -0.1011 16  PHE   C C   
3939  O  O   . PHE   C  18  ? 1.8437 0.4696 1.4659 0.0476  -0.2991 -0.1659 16  PHE   C O   
3940  C  CB  . PHE   C  18  ? 1.9006 0.4986 1.4245 0.1220  -0.3022 -0.0562 16  PHE   C CB  
3941  C  CG  . PHE   C  18  ? 2.0365 0.4080 1.4792 0.1140  -0.2606 -0.0499 16  PHE   C CG  
3942  C  CD1 . PHE   C  18  ? 2.1014 0.3063 1.5299 0.1733  -0.2544 -0.0384 16  PHE   C CD1 
3943  C  CD2 . PHE   C  18  ? 2.0886 0.3452 1.4678 0.1436  -0.2334 -0.0062 16  PHE   C CD2 
3944  C  CE1 . PHE   C  18  ? 2.1617 0.3622 1.5869 0.2312  -0.2427 -0.0428 16  PHE   C CE1 
3945  C  CE2 . PHE   C  18  ? 2.1522 0.3780 1.5481 0.1900  -0.2027 0.0153  16  PHE   C CE2 
3946  C  CZ  . PHE   C  18  ? 2.1765 0.4689 1.5529 0.2348  -0.2256 -0.0100 16  PHE   C CZ  
3947  N  N   . GLN   C  19  ? 1.8176 0.4086 1.3781 -0.0037 -0.2720 -0.1033 17  GLN   C N   
3948  C  CA  . GLN   C  19  ? 1.7840 0.4699 1.3889 -0.0143 -0.2450 -0.0902 17  GLN   C CA  
3949  C  C   . GLN   C  19  ? 1.7944 0.4757 1.3789 -0.0172 -0.2315 -0.0749 17  GLN   C C   
3950  O  O   . GLN   C  19  ? 1.8534 0.4687 1.4169 0.0007  -0.1752 -0.0324 17  GLN   C O   
3951  C  CB  . GLN   C  19  ? 1.7341 0.5383 1.2937 -0.0495 -0.2614 -0.0977 17  GLN   C CB  
3952  C  CG  . GLN   C  19  ? 1.7450 0.5601 1.2537 -0.0792 -0.2271 -0.1094 17  GLN   C CG  
3953  C  CD  . GLN   C  19  ? 1.7575 0.5294 1.2453 -0.1505 -0.2608 -0.1247 17  GLN   C CD  
3954  O  OE1 . GLN   C  19  ? 1.8050 0.4793 1.1833 -0.1259 -0.2351 -0.0885 17  GLN   C OE1 
3955  N  NE2 . GLN   C  19  ? 1.7083 0.6215 1.2676 -0.1362 -0.2590 -0.1605 17  GLN   C NE2 
3956  N  N   . VAL   C  20  ? 1.7834 0.4875 1.4273 -0.0187 -0.2268 -0.0747 18  VAL   C N   
3957  C  CA  . VAL   C  20  ? 1.8198 0.5518 1.4349 0.0001  -0.2320 -0.0994 18  VAL   C CA  
3958  C  C   . VAL   C  20  ? 1.8416 0.5492 1.4670 -0.0241 -0.2258 -0.1004 18  VAL   C C   
3959  O  O   . VAL   C  20  ? 1.8543 0.3862 1.5344 0.0526  -0.2072 -0.2335 18  VAL   C O   
3960  C  CB  . VAL   C  20  ? 1.8029 0.6441 1.4668 0.0082  -0.2133 -0.0984 18  VAL   C CB  
3961  C  CG1 . VAL   C  20  ? 1.8038 0.6899 1.4681 0.0092  -0.2036 -0.1063 18  VAL   C CG1 
3962  C  CG2 . VAL   C  20  ? 1.8061 0.6498 1.4391 0.0061  -0.2248 -0.1056 18  VAL   C CG2 
3963  N  N   . GLU   C  21  ? 1.8523 0.5427 1.5052 -0.0285 -0.2402 -0.0956 19  GLU   C N   
3964  C  CA  . GLU   C  21  ? 1.8184 0.5905 1.5303 -0.1145 -0.2663 -0.0464 19  GLU   C CA  
3965  C  C   . GLU   C  21  ? 1.8029 0.5123 1.4574 -0.0998 -0.3048 -0.0300 19  GLU   C C   
3966  O  O   . GLU   C  21  ? 1.7235 0.6254 1.4077 -0.1748 -0.3208 -0.0895 19  GLU   C O   
3967  C  CB  . GLU   C  21  ? 1.8338 0.5972 1.6020 -0.1158 -0.2811 -0.0945 19  GLU   C CB  
3968  C  CG  . GLU   C  21  ? 1.8189 0.7407 1.7459 -0.1542 -0.2913 -0.0678 19  GLU   C CG  
3969  C  CD  . GLU   C  21  ? 1.8594 0.8762 1.7907 -0.2042 -0.2531 -0.1537 19  GLU   C CD  
3970  O  OE1 . GLU   C  21  ? 1.8403 1.1004 1.7714 -0.3584 -0.3959 -0.2640 19  GLU   C OE1 
3971  O  OE2 . GLU   C  21  ? 1.9315 1.0706 1.9885 -0.2925 -0.1665 -0.0220 19  GLU   C OE2 
3972  N  N   . TYR   C  22  ? 1.7880 0.4179 1.4021 -0.0774 -0.2469 0.0644  20  TYR   C N   
3973  C  CA  . TYR   C  22  ? 1.7874 0.4597 1.4148 -0.0618 -0.2516 0.1153  20  TYR   C CA  
3974  C  C   . TYR   C  22  ? 1.8361 0.4413 1.4354 -0.0458 -0.2764 0.0978  20  TYR   C C   
3975  O  O   . TYR   C  22  ? 1.8263 0.3725 1.5287 -0.0387 -0.2570 0.0754  20  TYR   C O   
3976  C  CB  . TYR   C  22  ? 1.8113 0.5027 1.3893 -0.0353 -0.2358 0.1549  20  TYR   C CB  
3977  C  CG  . TYR   C  22  ? 1.8638 0.5194 1.4055 -0.0493 -0.2042 0.1421  20  TYR   C CG  
3978  C  CD1 . TYR   C  22  ? 1.8897 0.5837 1.4242 -0.0089 -0.2251 0.1338  20  TYR   C CD1 
3979  C  CD2 . TYR   C  22  ? 1.8863 0.5141 1.4049 -0.0679 -0.1961 0.1636  20  TYR   C CD2 
3980  C  CE1 . TYR   C  22  ? 1.9617 0.6261 1.4590 -0.0147 -0.2075 0.0825  20  TYR   C CE1 
3981  C  CE2 . TYR   C  22  ? 1.9475 0.5351 1.4242 -0.0676 -0.1844 0.1387  20  TYR   C CE2 
3982  C  CZ  . TYR   C  22  ? 1.9728 0.5798 1.4559 -0.0107 -0.1969 0.1004  20  TYR   C CZ  
3983  O  OH  . TYR   C  22  ? 2.0872 0.6987 1.4608 -0.0425 -0.1776 -0.0028 20  TYR   C OH  
3984  N  N   . ALA   C  23  ? 1.8254 0.4454 1.3904 -0.0435 -0.2824 0.0710  21  ALA   C N   
3985  C  CA  . ALA   C  23  ? 1.8005 0.5510 1.3035 -0.0207 -0.3086 0.0556  21  ALA   C CA  
3986  C  C   . ALA   C  23  ? 1.7941 0.5480 1.3052 0.0048  -0.3255 0.0548  21  ALA   C C   
3987  O  O   . ALA   C  23  ? 1.7651 0.6823 1.2607 -0.0021 -0.3551 0.0567  21  ALA   C O   
3988  C  CB  . ALA   C  23  ? 1.7759 0.5736 1.2996 -0.0355 -0.3186 0.0683  21  ALA   C CB  
3989  N  N   . LEU   C  24  ? 1.8234 0.4534 1.3176 0.0394  -0.2751 0.0485  22  LEU   C N   
3990  C  CA  . LEU   C  24  ? 1.7908 0.4498 1.3438 0.0530  -0.2652 0.0876  22  LEU   C CA  
3991  C  C   . LEU   C  24  ? 1.8244 0.4752 1.2987 0.0366  -0.2570 0.1205  22  LEU   C C   
3992  O  O   . LEU   C  24  ? 1.8727 0.4826 1.3046 0.0097  -0.2345 0.0979  22  LEU   C O   
3993  C  CB  . LEU   C  24  ? 1.7850 0.4782 1.3533 0.0522  -0.2650 0.0764  22  LEU   C CB  
3994  C  CG  . LEU   C  24  ? 1.7519 0.5350 1.3686 0.0500  -0.2884 0.0858  22  LEU   C CG  
3995  C  CD1 . LEU   C  24  ? 1.7591 0.5961 1.3883 0.0589  -0.2820 0.0549  22  LEU   C CD1 
3996  C  CD2 . LEU   C  24  ? 1.7415 0.5405 1.3640 0.0549  -0.2608 0.1590  22  LEU   C CD2 
3997  N  N   . GLU   C  25  ? 1.8086 0.5837 1.2586 0.0135  -0.2912 0.1287  23  GLU   C N   
3998  C  CA  . GLU   C  25  ? 1.7705 0.6948 1.3109 -0.0259 -0.2976 0.1171  23  GLU   C CA  
3999  C  C   . GLU   C  25  ? 1.7883 0.6674 1.3042 0.0165  -0.3333 0.1112  23  GLU   C C   
4000  O  O   . GLU   C  25  ? 1.7057 0.8669 1.3517 -0.0272 -0.2717 0.0590  23  GLU   C O   
4001  C  CB  . GLU   C  25  ? 1.7814 0.7589 1.3073 -0.0160 -0.3082 0.1035  23  GLU   C CB  
4002  C  CG  . GLU   C  25  ? 1.7785 0.7739 1.3747 -0.0034 -0.3125 0.0989  23  GLU   C CG  
4003  C  CD  . GLU   C  25  ? 1.7216 0.7516 1.4535 0.0262  -0.3331 0.0914  23  GLU   C CD  
4004  O  OE1 . GLU   C  25  ? 1.7814 0.7545 1.5123 -0.0266 -0.3080 0.0741  23  GLU   C OE1 
4005  O  OE2 . GLU   C  25  ? 1.7232 0.8596 1.5513 0.0446  -0.3588 0.0253  23  GLU   C OE2 
4006  N  N   . ALA   C  26  ? 1.7939 0.6332 1.2686 -0.0229 -0.3096 0.1112  24  ALA   C N   
4007  C  CA  . ALA   C  26  ? 1.7995 0.6294 1.2723 -0.0367 -0.2887 0.1050  24  ALA   C CA  
4008  C  C   . ALA   C  26  ? 1.7915 0.5465 1.2620 -0.0636 -0.2642 0.1275  24  ALA   C C   
4009  O  O   . ALA   C  26  ? 1.8184 0.4269 1.2512 -0.1103 -0.2509 0.1232  24  ALA   C O   
4010  C  CB  . ALA   C  26  ? 1.8089 0.6460 1.2777 -0.0297 -0.2939 0.1095  24  ALA   C CB  
4011  N  N   . VAL   C  27  ? 1.7731 0.5748 1.3280 -0.0657 -0.2577 0.1398  25  VAL   C N   
4012  C  CA  . VAL   C  27  ? 1.7935 0.6454 1.3349 -0.0514 -0.2711 0.1375  25  VAL   C CA  
4013  C  C   . VAL   C  27  ? 1.8203 0.6218 1.4372 -0.0617 -0.2662 0.1526  25  VAL   C C   
4014  O  O   . VAL   C  27  ? 1.8548 0.4205 1.4466 -0.0454 -0.2534 0.1454  25  VAL   C O   
4015  C  CB  . VAL   C  27  ? 1.7872 0.7254 1.3252 -0.0539 -0.2890 0.1466  25  VAL   C CB  
4016  C  CG1 . VAL   C  27  ? 1.8021 0.7668 1.3250 -0.0518 -0.2914 0.1523  25  VAL   C CG1 
4017  C  CG2 . VAL   C  27  ? 1.7883 0.7474 1.2806 -0.0738 -0.2860 0.1437  25  VAL   C CG2 
4018  N  N   . LYS   C  28  ? 1.8138 0.7222 1.4724 -0.0361 -0.2479 0.0751  26  LYS   C N   
4019  C  CA  . LYS   C  28  ? 1.8032 0.7450 1.4813 -0.0768 -0.2601 0.0915  26  LYS   C CA  
4020  C  C   . LYS   C  28  ? 1.8280 0.6493 1.4982 -0.1133 -0.2648 0.0898  26  LYS   C C   
4021  O  O   . LYS   C  28  ? 1.7729 0.6271 1.5189 -0.1831 -0.2398 0.0532  26  LYS   C O   
4022  C  CB  . LYS   C  28  ? 1.8404 0.8555 1.4818 -0.0455 -0.2750 0.0141  26  LYS   C CB  
4023  C  CG  . LYS   C  28  ? 1.8166 1.0987 1.5408 -0.0457 -0.2575 -0.0456 26  LYS   C CG  
4024  C  CD  . LYS   C  28  ? 1.8016 1.2131 1.5545 -0.0120 -0.2163 -0.1468 26  LYS   C CD  
4025  C  CE  . LYS   C  28  ? 1.8392 1.3968 1.5244 -0.0810 -0.2219 -0.1374 26  LYS   C CE  
4026  N  NZ  . LYS   C  28  ? 1.8684 1.4585 1.4619 -0.1308 -0.1570 -0.1377 26  LYS   C NZ  
4027  N  N   . ARG   C  29  ? 1.8345 0.6191 1.4614 -0.1261 -0.2194 0.1679  27  ARG   C N   
4028  C  CA  . ARG   C  29  ? 1.8272 0.6529 1.4949 -0.1077 -0.1916 0.2192  27  ARG   C CA  
4029  C  C   . ARG   C  29  ? 1.7957 0.6333 1.4475 -0.0457 -0.2102 0.2975  27  ARG   C C   
4030  O  O   . ARG   C  29  ? 1.7804 0.6041 1.5001 -0.0433 -0.2205 0.3081  27  ARG   C O   
4031  C  CB  . ARG   C  29  ? 1.8917 0.7665 1.4842 -0.1285 -0.1898 0.1534  27  ARG   C CB  
4032  C  CG  . ARG   C  29  ? 1.9053 0.8729 1.6258 -0.1616 -0.1290 0.0909  27  ARG   C CG  
4033  C  CD  . ARG   C  29  ? 1.9639 1.0013 1.6516 -0.1790 -0.1348 -0.0064 27  ARG   C CD  
4034  N  NE  . ARG   C  29  ? 2.0339 0.9962 1.7541 -0.2066 -0.1091 -0.0576 27  ARG   C NE  
4035  C  CZ  . ARG   C  29  ? 2.0281 1.0474 1.8051 -0.1936 -0.0998 -0.1086 27  ARG   C CZ  
4036  N  NH1 . ARG   C  29  ? 1.9909 1.1271 1.8294 -0.2221 -0.0564 -0.1165 27  ARG   C NH1 
4037  N  NH2 . ARG   C  29  ? 1.9984 1.0689 1.8650 -0.1871 -0.1044 -0.1331 27  ARG   C NH2 
4038  N  N   . GLY   C  30  ? 1.7674 0.6117 1.4270 -0.0110 -0.2289 0.3274  28  GLY   C N   
4039  C  CA  . GLY   C  30  ? 1.7926 0.6489 1.4338 0.0150  -0.2246 0.3232  28  GLY   C CA  
4040  C  C   . GLY   C  30  ? 1.8350 0.6390 1.4550 0.0424  -0.2533 0.3622  28  GLY   C C   
4041  O  O   . GLY   C  30  ? 1.8345 0.6604 1.4772 0.0536  -0.2388 0.3806  28  GLY   C O   
4042  N  N   . THR   C  31  ? 1.8421 0.6851 1.4718 0.0480  -0.2483 0.3491  29  THR   C N   
4043  C  CA  . THR   C  31  ? 1.8660 0.7104 1.4741 -0.0014 -0.2692 0.3599  29  THR   C CA  
4044  C  C   . THR   C  31  ? 1.8823 0.6273 1.4873 -0.0074 -0.2760 0.3453  29  THR   C C   
4045  O  O   . THR   C  31  ? 1.8760 0.5608 1.5003 0.0082  -0.3322 0.3280  29  THR   C O   
4046  C  CB  . THR   C  31  ? 1.8506 0.8245 1.4949 -0.0424 -0.2145 0.3506  29  THR   C CB  
4047  O  OG1 . THR   C  31  ? 1.8258 0.8434 1.4801 -0.1597 -0.2103 0.3303  29  THR   C OG1 
4048  C  CG2 . THR   C  31  ? 1.8568 0.8945 1.5388 -0.0818 -0.2066 0.3482  29  THR   C CG2 
4049  N  N   . CYS   C  32  ? 1.9223 0.6888 1.4640 0.0072  -0.3212 0.3273  30  CYS   C N   
4050  C  CA  . CYS   C  32  ? 1.9380 0.7134 1.4671 -0.0168 -0.3226 0.2769  30  CYS   C CA  
4051  C  C   . CYS   C  32  ? 1.8483 0.6789 1.4134 -0.0744 -0.3182 0.3070  30  CYS   C C   
4052  O  O   . CYS   C  32  ? 1.8192 0.5930 1.3962 -0.1243 -0.3320 0.2776  30  CYS   C O   
4053  C  CB  . CYS   C  32  ? 2.0249 0.8274 1.4746 0.0196  -0.3554 0.3277  30  CYS   C CB  
4054  S  SG  . CYS   C  32  ? 2.0778 0.9370 1.5385 0.0456  -0.4223 0.3574  30  CYS   C SG  
4055  N  N   . ALA   C  33  ? 1.8515 0.6455 1.3549 -0.0689 -0.3072 0.2714  31  ALA   C N   
4056  C  CA  . ALA   C  33  ? 1.8369 0.6799 1.3332 -0.0828 -0.2819 0.2463  31  ALA   C CA  
4057  C  C   . ALA   C  33  ? 1.8123 0.6380 1.3131 -0.0558 -0.2514 0.2307  31  ALA   C C   
4058  O  O   . ALA   C  33  ? 1.8428 0.5505 1.3437 -0.0355 -0.2477 0.2335  31  ALA   C O   
4059  C  CB  . ALA   C  33  ? 1.7950 0.6645 1.3198 -0.1060 -0.3019 0.2319  31  ALA   C CB  
4060  N  N   . VAL   C  34  ? 1.8095 0.7171 1.2838 -0.0553 -0.2436 0.2498  32  VAL   C N   
4061  C  CA  . VAL   C  34  ? 1.8117 0.6920 1.2323 -0.0328 -0.2268 0.2689  32  VAL   C CA  
4062  C  C   . VAL   C  34  ? 1.7888 0.7249 1.2378 -0.0495 -0.2295 0.2391  32  VAL   C C   
4063  O  O   . VAL   C  34  ? 1.7759 0.6058 1.2469 -0.1237 -0.2050 0.1944  32  VAL   C O   
4064  C  CB  . VAL   C  34  ? 1.7987 0.7027 1.1914 0.0080  -0.2336 0.2649  32  VAL   C CB  
4065  C  CG1 . VAL   C  34  ? 1.8307 0.7250 1.1749 0.0062  -0.2120 0.2668  32  VAL   C CG1 
4066  C  CG2 . VAL   C  34  ? 1.8106 0.6909 1.1717 0.0196  -0.2363 0.2838  32  VAL   C CG2 
4067  N  N   . GLY   C  35  ? 1.7637 0.7722 1.2673 -0.0092 -0.2352 0.2831  33  GLY   C N   
4068  C  CA  . GLY   C  35  ? 1.7722 0.7632 1.2525 0.0325  -0.2436 0.2861  33  GLY   C CA  
4069  C  C   . GLY   C  35  ? 1.8017 0.8266 1.2429 0.0523  -0.2364 0.3210  33  GLY   C C   
4070  O  O   . GLY   C  35  ? 1.7755 0.8862 1.2731 0.0741  -0.2369 0.3569  33  GLY   C O   
4071  N  N   . VAL   C  36  ? 1.8337 0.7827 1.2416 0.0695  -0.2543 0.3238  34  VAL   C N   
4072  C  CA  . VAL   C  36  ? 1.8785 0.7581 1.2790 0.0739  -0.2822 0.3642  34  VAL   C CA  
4073  C  C   . VAL   C  36  ? 1.9008 0.7216 1.2811 0.0432  -0.3141 0.4104  34  VAL   C C   
4074  O  O   . VAL   C  36  ? 1.9348 0.6301 1.2646 0.0512  -0.3134 0.4590  34  VAL   C O   
4075  C  CB  . VAL   C  36  ? 1.8831 0.7269 1.3315 0.0574  -0.2634 0.3531  34  VAL   C CB  
4076  C  CG1 . VAL   C  36  ? 1.8992 0.7485 1.3299 0.0730  -0.2627 0.3630  34  VAL   C CG1 
4077  C  CG2 . VAL   C  36  ? 1.8664 0.7190 1.3572 0.0554  -0.2619 0.3526  34  VAL   C CG2 
4078  N  N   . LYS   C  37  ? 1.8776 0.7965 1.2629 0.0663  -0.3437 0.4233  35  LYS   C N   
4079  C  CA  . LYS   C  37  ? 1.8892 0.9131 1.2491 0.0664  -0.3557 0.3438  35  LYS   C CA  
4080  C  C   . LYS   C  37  ? 1.9411 1.0691 1.2837 0.0764  -0.3982 0.3738  35  LYS   C C   
4081  O  O   . LYS   C  37  ? 1.9078 1.1244 1.3516 0.0928  -0.3957 0.3315  35  LYS   C O   
4082  C  CB  . LYS   C  37  ? 1.8274 0.9190 1.2236 0.0918  -0.3402 0.3146  35  LYS   C CB  
4083  C  CG  . LYS   C  37  ? 1.8222 0.8948 1.1964 0.0942  -0.3476 0.3197  35  LYS   C CG  
4084  C  CD  . LYS   C  37  ? 1.7605 0.8536 1.1925 0.0997  -0.3409 0.2845  35  LYS   C CD  
4085  C  CE  . LYS   C  37  ? 1.7621 0.8586 1.1855 0.0983  -0.3422 0.2918  35  LYS   C CE  
4086  N  NZ  . LYS   C  37  ? 1.7501 0.8447 1.1809 0.1124  -0.3416 0.2850  35  LYS   C NZ  
4087  N  N   . GLY   C  38  ? 1.9972 1.1015 1.2752 0.0837  -0.4006 0.3620  36  GLY   C N   
4088  C  CA  . GLY   C  38  ? 2.1020 1.0906 1.2643 0.0367  -0.4013 0.3544  36  GLY   C CA  
4089  C  C   . GLY   C  38  ? 2.2092 1.0284 1.3048 0.0194  -0.4117 0.3111  36  GLY   C C   
4090  O  O   . GLY   C  38  ? 2.2667 0.8334 1.2638 -0.0064 -0.4414 0.3187  36  GLY   C O   
4091  N  N   . LYS   C  39  ? 2.2937 1.1137 1.3481 -0.0032 -0.4089 0.2373  37  LYS   C N   
4092  C  CA  . LYS   C  39  ? 2.3249 1.1804 1.3930 -0.0059 -0.4210 0.1663  37  LYS   C CA  
4093  C  C   . LYS   C  39  ? 2.3410 1.1746 1.2825 0.0046  -0.4166 0.1415  37  LYS   C C   
4094  O  O   . LYS   C  39  ? 2.3495 1.1342 1.2149 0.0265  -0.4128 0.2418  37  LYS   C O   
4095  C  CB  . LYS   C  39  ? 2.3809 1.3040 1.3832 -0.0529 -0.4118 0.1430  37  LYS   C CB  
4096  C  CG  . LYS   C  39  ? 2.3839 1.4012 1.5146 -0.0657 -0.4375 0.1046  37  LYS   C CG  
4097  C  CD  . LYS   C  39  ? 2.3924 1.4706 1.6246 -0.0988 -0.4572 0.0103  37  LYS   C CD  
4098  C  CE  . LYS   C  39  ? 2.3975 1.6263 1.7088 -0.0951 -0.4736 -0.0299 37  LYS   C CE  
4099  N  NZ  . LYS   C  39  ? 2.4315 1.6666 1.7609 -0.1338 -0.4608 -0.1035 37  LYS   C NZ  
4100  N  N   . ASN   C  40  ? 2.3425 1.1578 1.2573 0.0421  -0.3683 0.1205  38  ASN   C N   
4101  C  CA  . ASN   C  40  ? 2.3904 1.1408 1.2268 0.0386  -0.2979 0.1215  38  ASN   C CA  
4102  C  C   . ASN   C  40  ? 2.3495 0.9799 1.2632 0.0626  -0.2795 0.1783  38  ASN   C C   
4103  O  O   . ASN   C  40  ? 2.4128 0.8762 1.1876 0.0479  -0.2887 0.1662  38  ASN   C O   
4104  C  CB  . ASN   C  40  ? 2.4362 1.2794 1.2365 0.0600  -0.2744 0.0963  38  ASN   C CB  
4105  C  CG  . ASN   C  40  ? 2.4577 1.3296 1.2025 0.0385  -0.2421 0.0583  38  ASN   C CG  
4106  O  OD1 . ASN   C  40  ? 2.5075 1.4323 1.1902 0.0861  -0.2766 0.0453  38  ASN   C OD1 
4107  N  ND2 . ASN   C  40  ? 2.4492 1.3327 1.2175 0.0244  -0.2199 0.0532  38  ASN   C ND2 
4108  N  N   . CYS   C  41  ? 2.3668 0.8920 1.3142 0.0257  -0.2146 0.1979  39  CYS   C N   
4109  C  CA  . CYS   C  41  ? 2.3062 0.8153 1.3464 0.0057  -0.1648 0.2098  39  CYS   C CA  
4110  C  C   . CYS   C  41  ? 2.2575 0.7430 1.3316 0.0345  -0.1616 0.2544  39  CYS   C C   
4111  O  O   . CYS   C  41  ? 2.2880 0.6336 1.2663 0.0208  -0.1069 0.2339  39  CYS   C O   
4112  C  CB  . CYS   C  41  ? 2.3599 0.7986 1.4566 -0.0277 -0.1149 0.2216  39  CYS   C CB  
4113  S  SG  . CYS   C  41  ? 2.3777 0.6726 1.5909 -0.1851 -0.0328 0.1770  39  CYS   C SG  
4114  N  N   . VAL   C  42  ? 2.1801 0.7005 1.3647 0.0294  -0.1626 0.2135  40  VAL   C N   
4115  C  CA  . VAL   C  42  ? 2.0888 0.6470 1.4031 0.0297  -0.1838 0.2174  40  VAL   C CA  
4116  C  C   . VAL   C  42  ? 2.0717 0.7134 1.4455 0.0380  -0.1501 0.2329  40  VAL   C C   
4117  O  O   . VAL   C  42  ? 2.0617 0.5378 1.4477 -0.0328 -0.1617 0.2912  40  VAL   C O   
4118  C  CB  . VAL   C  42  ? 2.0502 0.6609 1.3508 0.0772  -0.2076 0.1800  40  VAL   C CB  
4119  C  CG1 . VAL   C  42  ? 2.0382 0.6296 1.3574 0.1068  -0.2047 0.2058  40  VAL   C CG1 
4120  C  CG2 . VAL   C  42  ? 2.0277 0.7236 1.3335 0.0741  -0.2305 0.1703  40  VAL   C CG2 
4121  N  N   . VAL   C  43  ? 2.0964 0.7506 1.4837 -0.0023 -0.1481 0.1723  41  VAL   C N   
4122  C  CA  . VAL   C  43  ? 2.0871 0.8500 1.4657 -0.0083 -0.1425 0.1976  41  VAL   C CA  
4123  C  C   . VAL   C  43  ? 2.1173 0.9284 1.4775 0.0251  -0.1685 0.1762  41  VAL   C C   
4124  O  O   . VAL   C  43  ? 2.1190 0.9673 1.4851 0.0429  -0.1589 0.1934  41  VAL   C O   
4125  C  CB  . VAL   C  43  ? 2.1306 0.8250 1.4420 0.0038  -0.1495 0.1891  41  VAL   C CB  
4126  C  CG1 . VAL   C  43  ? 2.1406 0.7792 1.4499 -0.0029 -0.1116 0.2084  41  VAL   C CG1 
4127  C  CG2 . VAL   C  43  ? 2.1388 0.8539 1.3958 0.0050  -0.1616 0.2286  41  VAL   C CG2 
4128  N  N   . LEU   C  44  ? 2.1023 0.9522 1.5179 0.0689  -0.1560 0.1818  42  LEU   C N   
4129  C  CA  . LEU   C  44  ? 2.0202 0.8453 1.5272 0.0612  -0.1741 0.2165  42  LEU   C CA  
4130  C  C   . LEU   C  44  ? 2.0253 0.8008 1.5753 0.0621  -0.1813 0.2094  42  LEU   C C   
4131  O  O   . LEU   C  44  ? 1.9889 0.8004 1.6579 0.0113  -0.1759 0.1459  42  LEU   C O   
4132  C  CB  . LEU   C  44  ? 2.0096 0.7774 1.5813 0.0820  -0.1776 0.2079  42  LEU   C CB  
4133  C  CG  . LEU   C  44  ? 2.0386 0.6759 1.6147 0.0815  -0.1947 0.2048  42  LEU   C CG  
4134  C  CD1 . LEU   C  44  ? 2.0219 0.6809 1.6291 0.0766  -0.1981 0.2081  42  LEU   C CD1 
4135  C  CD2 . LEU   C  44  ? 2.0431 0.6127 1.5987 0.0800  -0.2084 0.2414  42  LEU   C CD2 
4136  N  N   . GLY   C  45  ? 2.0571 0.7863 1.5386 0.0907  -0.1937 0.2853  43  GLY   C N   
4137  C  CA  . GLY   C  45  ? 2.0583 0.7985 1.4997 0.0951  -0.1949 0.2466  43  GLY   C CA  
4138  C  C   . GLY   C  45  ? 2.0646 0.7778 1.5114 0.1385  -0.1993 0.2094  43  GLY   C C   
4139  O  O   . GLY   C  45  ? 2.0487 0.7847 1.4667 0.1481  -0.2261 0.1512  43  GLY   C O   
4140  N  N   . CYS   C  46  ? 2.0623 0.8139 1.5761 0.1399  -0.1948 0.2057  44  CYS   C N   
4141  C  CA  . CYS   C  46  ? 2.1278 0.9534 1.5931 0.1163  -0.2051 0.1968  44  CYS   C CA  
4142  C  C   . CYS   C  46  ? 2.0978 1.0715 1.6044 0.0809  -0.1641 0.2044  44  CYS   C C   
4143  O  O   . CYS   C  46  ? 2.1163 1.2168 1.5810 0.0908  -0.1395 0.3070  44  CYS   C O   
4144  C  CB  . CYS   C  46  ? 2.2592 0.9089 1.6771 0.1447  -0.1877 0.1909  44  CYS   C CB  
4145  S  SG  . CYS   C  46  ? 2.3608 0.9050 1.8045 0.0939  -0.1776 0.1093  44  CYS   C SG  
4146  N  N   . GLU   C  47  ? 2.1041 1.1524 1.6031 0.0193  -0.1512 0.1273  45  GLU   C N   
4147  C  CA  . GLU   C  47  ? 2.1639 1.2189 1.6715 -0.0551 -0.0693 0.0773  45  GLU   C CA  
4148  C  C   . GLU   C  47  ? 2.1467 1.3224 1.7538 0.0114  -0.0907 -0.0038 45  GLU   C C   
4149  O  O   . GLU   C  47  ? 2.0754 1.4811 1.7093 -0.0043 -0.0602 -0.0034 45  GLU   C O   
4150  C  CB  . GLU   C  47  ? 2.1625 1.1513 1.6787 -0.1561 -0.0224 0.0725  45  GLU   C CB  
4151  C  CG  . GLU   C  47  ? 2.2118 1.2332 1.6796 -0.2357 0.0250  0.0535  45  GLU   C CG  
4152  C  CD  . GLU   C  47  ? 2.2125 1.2310 1.5949 -0.3535 0.0361  0.0394  45  GLU   C CD  
4153  O  OE1 . GLU   C  47  ? 2.2984 1.2363 1.5295 -0.3707 -0.0038 0.0027  45  GLU   C OE1 
4154  O  OE2 . GLU   C  47  ? 2.3149 1.2244 1.4381 -0.4592 0.1021  0.0668  45  GLU   C OE2 
4155  N  N   . ARG   C  48  ? 2.2035 1.2718 1.7883 -0.0184 -0.0331 0.0021  46  ARG   C N   
4156  C  CA  . ARG   C  48  ? 2.2493 1.3031 1.8062 -0.0252 -0.0832 -0.0550 46  ARG   C CA  
4157  C  C   . ARG   C  48  ? 2.2535 1.3197 1.7824 -0.0350 -0.1171 -0.1053 46  ARG   C C   
4158  O  O   . ARG   C  48  ? 2.1591 1.2333 1.7251 -0.0377 -0.0597 -0.2805 46  ARG   C O   
4159  C  CB  . ARG   C  48  ? 2.2925 1.4825 1.9017 0.0601  -0.0747 -0.1215 46  ARG   C CB  
4160  C  CG  . ARG   C  48  ? 2.3899 1.4531 1.9792 0.0489  -0.0993 -0.2046 46  ARG   C CG  
4161  C  CD  . ARG   C  48  ? 2.4433 1.3952 2.0936 0.0479  -0.1504 -0.2306 46  ARG   C CD  
4162  N  NE  . ARG   C  48  ? 2.5021 1.4660 2.1128 -0.0478 -0.1254 -0.2682 46  ARG   C NE  
4163  C  CZ  . ARG   C  48  ? 2.5240 1.5808 2.0389 -0.1000 -0.1023 -0.3175 46  ARG   C CZ  
4164  N  NH1 . ARG   C  48  ? 2.5012 1.6717 2.1773 -0.1945 -0.1588 -0.2985 46  ARG   C NH1 
4165  N  NH2 . ARG   C  48  ? 2.5449 1.5578 2.0540 -0.0842 -0.0820 -0.3472 46  ARG   C NH2 
4166  N  N   . ARG   C  49  ? 2.3275 1.5261 1.6862 -0.0574 -0.1611 -0.0218 47  ARG   C N   
4167  C  CA  . ARG   C  49  ? 2.4026 1.5980 1.8043 -0.1280 -0.2099 0.0074  47  ARG   C CA  
4168  C  C   . ARG   C  49  ? 2.4034 1.6465 1.7906 -0.0656 -0.1956 0.0352  47  ARG   C C   
4169  O  O   . ARG   C  49  ? 2.4441 1.6657 1.7249 0.0107  -0.1409 -0.0338 47  ARG   C O   
4170  C  CB  . ARG   C  49  ? 2.4509 1.6967 1.7998 -0.1077 -0.2297 0.0010  47  ARG   C CB  
4171  C  CG  . ARG   C  49  ? 2.4902 1.6595 1.7861 -0.1457 -0.2456 -0.0074 47  ARG   C CG  
4172  C  CD  . ARG   C  49  ? 2.5152 1.5359 1.7731 -0.1462 -0.2455 -0.0001 47  ARG   C CD  
4173  N  NE  . ARG   C  49  ? 2.5917 1.4310 1.8695 -0.1560 -0.1736 0.0519  47  ARG   C NE  
4174  C  CZ  . ARG   C  49  ? 2.6009 1.5001 1.9979 -0.1039 -0.2472 0.0686  47  ARG   C CZ  
4175  N  NH1 . ARG   C  49  ? 2.6449 1.5247 2.0696 -0.1232 -0.2463 0.0311  47  ARG   C NH1 
4176  N  NH2 . ARG   C  49  ? 2.5554 1.4276 2.1031 -0.1229 -0.2555 0.0909  47  ARG   C NH2 
4177  N  N   . SER   C  50  ? 2.3685 1.6489 1.8779 -0.1584 -0.2132 -0.0199 48  SER   C N   
4178  C  CA  . SER   C  50  ? 2.3710 1.5396 1.8928 -0.2015 -0.2112 -0.0565 48  SER   C CA  
4179  C  C   . SER   C  50  ? 2.3182 1.4510 1.9352 -0.1651 -0.2682 0.0252  48  SER   C C   
4180  O  O   . SER   C  50  ? 2.2892 1.4934 1.9312 -0.1012 -0.2759 0.1011  48  SER   C O   
4181  C  CB  . SER   C  50  ? 2.4325 1.4937 1.7978 -0.2600 -0.2097 -0.1668 48  SER   C CB  
4182  O  OG  . SER   C  50  ? 2.4505 1.5387 1.7839 -0.3006 -0.2156 -0.3306 48  SER   C OG  
4183  N  N   . THR   C  51  ? 2.2738 1.3815 1.9957 -0.1123 -0.1726 0.0675  49  THR   C N   
4184  C  CA  . THR   C  51  ? 2.2452 1.4207 1.9768 -0.1147 -0.1176 0.0226  49  THR   C CA  
4185  C  C   . THR   C  51  ? 2.2667 1.4311 2.0330 -0.1291 -0.1501 0.0666  49  THR   C C   
4186  O  O   . THR   C  51  ? 2.2588 1.6073 2.0451 -0.1539 -0.1493 0.0298  49  THR   C O   
4187  C  CB  . THR   C  51  ? 2.1235 1.3421 2.0271 -0.0904 -0.1243 0.0198  49  THR   C CB  
4188  O  OG1 . THR   C  51  ? 2.0134 1.2628 1.9877 -0.0041 -0.0686 -0.0386 49  THR   C OG1 
4189  C  CG2 . THR   C  51  ? 2.0888 1.3137 1.9973 -0.1108 -0.1214 -0.0172 49  THR   C CG2 
4190  N  N   . LEU   C  52  ? 2.3473 1.3624 2.1154 -0.1596 -0.0912 0.1215  50  LEU   C N   
4191  C  CA  . LEU   C  52  ? 2.3845 1.2400 2.1234 -0.1999 -0.0494 0.1017  50  LEU   C CA  
4192  C  C   . LEU   C  52  ? 2.3779 1.0906 2.0897 -0.2200 -0.0871 0.0870  50  LEU   C C   
4193  O  O   . LEU   C  52  ? 2.3975 0.9799 2.0919 -0.2901 0.0131  0.0992  50  LEU   C O   
4194  C  CB  . LEU   C  52  ? 2.3836 1.1892 2.0844 -0.1563 -0.0084 0.0701  50  LEU   C CB  
4195  C  CG  . LEU   C  52  ? 2.4130 1.1252 1.9988 -0.1638 0.0047  0.0876  50  LEU   C CG  
4196  C  CD1 . LEU   C  52  ? 2.3957 1.0726 1.8696 -0.1319 0.0252  0.0471  50  LEU   C CD1 
4197  C  CD2 . LEU   C  52  ? 2.4165 1.2003 1.9346 -0.1562 0.0352  0.1332  50  LEU   C CD2 
4198  N  N   . LYS   C  53  ? 2.3061 1.1921 2.1260 -0.1709 -0.1273 0.1287  51  LYS   C N   
4199  C  CA  . LYS   C  53  ? 2.2952 1.2093 2.0987 -0.0741 -0.1922 0.1124  51  LYS   C CA  
4200  C  C   . LYS   C  53  ? 2.3018 0.9141 2.1005 -0.0880 -0.1259 0.0818  51  LYS   C C   
4201  O  O   . LYS   C  53  ? 2.3024 0.6945 2.1032 -0.0968 -0.1784 0.1615  51  LYS   C O   
4202  C  CB  . LYS   C  53  ? 2.2520 1.3795 2.1258 -0.1412 -0.1599 0.1588  51  LYS   C CB  
4203  C  CG  . LYS   C  53  ? 2.2546 1.5731 2.1560 -0.1032 -0.1992 0.0887  51  LYS   C CG  
4204  C  CD  . LYS   C  53  ? 2.2735 1.6111 2.1988 -0.0767 -0.2857 0.0420  51  LYS   C CD  
4205  C  CE  . LYS   C  53  ? 2.1359 1.5820 2.2462 -0.0583 -0.3584 0.0329  51  LYS   C CE  
4206  N  NZ  . LYS   C  53  ? 2.1154 1.5128 2.2588 -0.0139 -0.4304 0.0378  51  LYS   C NZ  
4207  N  N   . LEU   C  54  ? 2.3108 0.8415 1.9888 -0.1168 -0.1454 0.1100  52  LEU   C N   
4208  C  CA  . LEU   C  54  ? 2.2552 0.9242 1.8953 -0.1339 -0.1346 0.1592  52  LEU   C CA  
4209  C  C   . LEU   C  54  ? 2.2202 1.0063 1.7899 -0.1364 -0.1277 0.2347  52  LEU   C C   
4210  O  O   . LEU   C  54  ? 2.2369 1.0124 1.6600 -0.1838 -0.1066 0.2462  52  LEU   C O   
4211  C  CB  . LEU   C  54  ? 2.2294 0.8357 1.9123 -0.1765 -0.1282 0.1888  52  LEU   C CB  
4212  C  CG  . LEU   C  54  ? 2.2620 0.7897 1.9515 -0.2164 -0.1037 0.2159  52  LEU   C CG  
4213  C  CD1 . LEU   C  54  ? 2.2769 0.7999 1.9326 -0.2316 -0.0682 0.1928  52  LEU   C CD1 
4214  C  CD2 . LEU   C  54  ? 2.2700 0.7580 1.9486 -0.2225 -0.1183 0.2459  52  LEU   C CD2 
4215  N  N   . GLN   C  55  ? 2.1827 1.0183 1.7761 -0.1178 -0.0969 0.3359  53  GLN   C N   
4216  C  CA  . GLN   C  55  ? 2.1247 0.9928 1.7833 -0.0626 -0.0797 0.3852  53  GLN   C CA  
4217  C  C   . GLN   C  55  ? 2.1656 1.0205 1.8171 -0.1204 -0.0379 0.3278  53  GLN   C C   
4218  O  O   . GLN   C  55  ? 2.2379 0.6765 1.8276 -0.1923 -0.0696 0.3963  53  GLN   C O   
4219  C  CB  . GLN   C  55  ? 2.1597 1.0044 1.7960 0.0394  -0.0963 0.4476  53  GLN   C CB  
4220  C  CG  . GLN   C  55  ? 2.1957 0.9982 1.7934 0.1614  -0.1686 0.4380  53  GLN   C CG  
4221  C  CD  . GLN   C  55  ? 2.1252 1.0590 1.8291 0.2060  -0.1859 0.4292  53  GLN   C CD  
4222  O  OE1 . GLN   C  55  ? 2.1864 1.1047 1.8773 0.2832  -0.2640 0.4627  53  GLN   C OE1 
4223  N  NE2 . GLN   C  55  ? 2.2202 0.9253 1.8170 0.2763  -0.1767 0.4597  53  GLN   C NE2 
4224  N  N   . ASP   C  56  ? 2.1286 1.0347 1.8044 -0.1647 -0.0176 0.3116  54  ASP   C N   
4225  C  CA  . ASP   C  56  ? 2.0705 1.0604 1.7847 -0.1970 -0.0372 0.2874  54  ASP   C CA  
4226  C  C   . ASP   C  56  ? 2.0588 0.9480 1.6424 -0.1710 -0.0621 0.3535  54  ASP   C C   
4227  O  O   . ASP   C  56  ? 2.0171 0.9659 1.6168 -0.1438 -0.0694 0.3546  54  ASP   C O   
4228  C  CB  . ASP   C  56  ? 2.0441 1.1120 1.8133 -0.1546 -0.0266 0.2603  54  ASP   C CB  
4229  C  CG  . ASP   C  56  ? 2.0746 1.2692 1.9047 -0.1614 0.0179  0.1267  54  ASP   C CG  
4230  O  OD1 . ASP   C  56  ? 2.1532 1.4118 1.8833 -0.1055 0.0109  0.0676  54  ASP   C OD1 
4231  O  OD2 . ASP   C  56  ? 1.9682 1.3137 2.0469 -0.1503 0.0759  0.0121  54  ASP   C OD2 
4232  N  N   . THR   C  57  ? 1.9929 0.9743 1.6847 -0.1844 -0.1377 0.2852  55  THR   C N   
4233  C  CA  . THR   C  57  ? 2.0173 0.9333 1.6042 -0.1708 -0.1814 0.2853  55  THR   C CA  
4234  C  C   . THR   C  57  ? 1.9342 0.9419 1.6721 -0.1653 -0.1923 0.2579  55  THR   C C   
4235  O  O   . THR   C  57  ? 1.9488 1.0353 1.7194 -0.1978 -0.2115 0.2741  55  THR   C O   
4236  C  CB  . THR   C  57  ? 2.0385 0.9345 1.5568 -0.1837 -0.1966 0.2541  55  THR   C CB  
4237  O  OG1 . THR   C  57  ? 2.0619 0.8638 1.4710 -0.1476 -0.2154 0.3062  55  THR   C OG1 
4238  C  CG2 . THR   C  57  ? 2.0404 0.9133 1.4992 -0.1957 -0.2047 0.2786  55  THR   C CG2 
4239  N  N   . ARG   C  58  ? 1.9375 0.9874 1.7555 -0.1433 -0.1724 0.2213  56  ARG   C N   
4240  C  CA  . ARG   C  58  ? 1.9549 0.9937 1.7996 -0.0643 -0.1446 0.1842  56  ARG   C CA  
4241  C  C   . ARG   C  58  ? 1.9830 0.9400 1.8205 -0.0034 -0.1423 0.2287  56  ARG   C C   
4242  O  O   . ARG   C  58  ? 1.9862 0.9599 1.7276 0.0033  -0.1762 0.1905  56  ARG   C O   
4243  C  CB  . ARG   C  58  ? 1.9650 1.0094 1.8596 -0.0530 -0.1317 0.1517  56  ARG   C CB  
4244  C  CG  . ARG   C  58  ? 1.9846 1.0327 1.8664 -0.0632 -0.1126 0.1354  56  ARG   C CG  
4245  C  CD  . ARG   C  58  ? 1.9964 1.0998 1.9204 -0.0351 -0.0877 0.1452  56  ARG   C CD  
4246  N  NE  . ARG   C  58  ? 2.0007 1.0970 1.9267 -0.0206 -0.0941 0.1623  56  ARG   C NE  
4247  C  CZ  . ARG   C  58  ? 2.0171 1.1243 1.9103 -0.0274 -0.0482 0.2323  56  ARG   C CZ  
4248  N  NH1 . ARG   C  58  ? 2.0323 1.1264 1.9143 0.0210  -0.0123 0.2598  56  ARG   C NH1 
4249  N  NH2 . ARG   C  58  ? 2.0003 1.0706 1.8885 -0.0491 -0.0427 0.2802  56  ARG   C NH2 
4250  N  N   . ILE   C  59  ? 1.9891 0.9330 1.8620 0.0187  -0.1724 0.2144  57  ILE   C N   
4251  C  CA  . ILE   C  59  ? 2.0048 1.0267 1.8905 0.0832  -0.1855 0.2666  57  ILE   C CA  
4252  C  C   . ILE   C  59  ? 1.9937 1.0738 1.9630 0.0871  -0.1955 0.2284  57  ILE   C C   
4253  O  O   . ILE   C  59  ? 2.0070 1.3048 1.9486 0.1401  -0.1643 0.3156  57  ILE   C O   
4254  C  CB  . ILE   C  59  ? 1.9766 0.9783 1.9572 0.1045  -0.1809 0.2244  57  ILE   C CB  
4255  C  CG1 . ILE   C  59  ? 2.0364 0.8455 1.9524 0.1771  -0.1647 0.2803  57  ILE   C CG1 
4256  C  CG2 . ILE   C  59  ? 1.9992 1.1527 1.9883 0.1558  -0.1402 0.1683  57  ILE   C CG2 
4257  C  CD1 . ILE   C  59  ? 2.0464 0.7838 1.9693 0.1938  -0.1737 0.2695  57  ILE   C CD1 
4258  N  N   . THR   C  60  ? 1.9969 1.0402 2.0284 -0.0696 -0.2312 0.2564  58  THR   C N   
4259  C  CA  . THR   C  60  ? 1.9170 1.1455 2.0313 -0.0950 -0.2453 0.2533  58  THR   C CA  
4260  C  C   . THR   C  60  ? 1.9218 1.2568 1.9548 -0.1384 -0.2076 0.2331  58  THR   C C   
4261  O  O   . THR   C  60  ? 1.9089 1.3407 1.9388 -0.1224 -0.2113 0.2553  58  THR   C O   
4262  C  CB  . THR   C  60  ? 1.9298 1.1674 2.1242 -0.0609 -0.2997 0.3065  58  THR   C CB  
4263  O  OG1 . THR   C  60  ? 1.9904 1.1002 2.2355 -0.0885 -0.3714 0.3687  58  THR   C OG1 
4264  C  CG2 . THR   C  60  ? 1.9279 1.0286 2.1011 -0.0225 -0.3536 0.3719  58  THR   C CG2 
4265  N  N   . PRO   C  61  ? 1.9028 1.3300 1.8593 -0.1751 -0.2464 0.1448  59  PRO   C N   
4266  C  CA  . PRO   C  61  ? 1.8915 1.3337 1.8008 -0.1666 -0.2119 0.1403  59  PRO   C CA  
4267  C  C   . PRO   C  61  ? 1.9257 1.3188 1.7628 -0.1862 -0.2260 0.1202  59  PRO   C C   
4268  O  O   . PRO   C  61  ? 1.9535 1.3098 1.7852 -0.1221 -0.1358 0.2085  59  PRO   C O   
4269  C  CB  . PRO   C  61  ? 1.8944 1.2890 1.7641 -0.1751 -0.2440 0.1203  59  PRO   C CB  
4270  C  CG  . PRO   C  61  ? 1.8737 1.2976 1.7480 -0.1922 -0.2280 0.0982  59  PRO   C CG  
4271  C  CD  . PRO   C  61  ? 1.8817 1.3234 1.8340 -0.1957 -0.2011 0.1167  59  PRO   C CD  
4272  N  N   . SER   C  62  ? 1.9382 1.3870 1.6998 -0.1821 -0.2379 0.1236  60  SER   C N   
4273  C  CA  . SER   C  62  ? 1.9460 1.2863 1.6002 -0.2294 -0.2453 0.0441  60  SER   C CA  
4274  C  C   . SER   C  62  ? 1.9419 0.9528 1.6182 -0.1272 -0.3381 0.0602  60  SER   C C   
4275  O  O   . SER   C  62  ? 1.9643 1.0957 1.6026 -0.2448 -0.2778 -0.0115 60  SER   C O   
4276  C  CB  . SER   C  62  ? 1.9670 1.4780 1.4916 -0.2717 -0.2405 0.0285  60  SER   C CB  
4277  O  OG  . SER   C  62  ? 2.0198 1.5454 1.3902 -0.3405 -0.2089 0.0656  60  SER   C OG  
4278  N  N   . LYS   C  63  ? 1.9967 0.8257 1.6843 -0.0870 -0.2842 0.0236  61  LYS   C N   
4279  C  CA  . LYS   C  63  ? 1.9791 0.8964 1.6732 -0.0312 -0.3301 0.0531  61  LYS   C CA  
4280  C  C   . LYS   C  63  ? 1.9633 0.6994 1.5283 0.0177  -0.2857 0.1080  61  LYS   C C   
4281  O  O   . LYS   C  63  ? 1.9918 0.6927 1.4607 -0.0301 -0.2953 0.1776  61  LYS   C O   
4282  C  CB  . LYS   C  63  ? 2.0885 0.9454 1.7426 0.1475  -0.3541 0.0380  61  LYS   C CB  
4283  C  CG  . LYS   C  63  ? 2.1522 1.0144 1.8143 0.2745  -0.4005 -0.0035 61  LYS   C CG  
4284  C  CD  . LYS   C  63  ? 2.1509 1.0172 1.7836 0.3561  -0.4092 -0.0505 61  LYS   C CD  
4285  C  CE  . LYS   C  63  ? 2.1771 1.0385 1.7499 0.4287  -0.3996 0.0151  61  LYS   C CE  
4286  N  NZ  . LYS   C  63  ? 2.2236 1.0265 1.7002 0.4640  -0.3952 0.0362  61  LYS   C NZ  
4287  N  N   . VAL   C  64  ? 1.8372 0.7011 1.4878 0.0118  -0.2680 0.1298  62  VAL   C N   
4288  C  CA  . VAL   C  64  ? 1.8012 0.7726 1.3974 -0.0036 -0.2479 0.1193  62  VAL   C CA  
4289  C  C   . VAL   C  64  ? 1.7351 0.7431 1.3584 -0.0375 -0.2378 0.0889  62  VAL   C C   
4290  O  O   . VAL   C  64  ? 1.7481 0.7852 1.3523 -0.1004 -0.1815 0.0657  62  VAL   C O   
4291  C  CB  . VAL   C  64  ? 1.8126 0.8053 1.3875 -0.0131 -0.2243 0.1496  62  VAL   C CB  
4292  C  CG1 . VAL   C  64  ? 1.8292 0.8013 1.3674 -0.0204 -0.2362 0.1709  62  VAL   C CG1 
4293  C  CG2 . VAL   C  64  ? 1.8204 0.7985 1.3875 -0.0205 -0.2077 0.1469  62  VAL   C CG2 
4294  N  N   . SER   C  65  ? 1.7284 0.7114 1.3293 -0.0406 -0.2529 0.0664  63  SER   C N   
4295  C  CA  . SER   C  65  ? 1.7690 0.7012 1.3434 -0.0584 -0.2333 0.0740  63  SER   C CA  
4296  C  C   . SER   C  65  ? 1.7379 0.6535 1.3465 -0.0390 -0.2246 0.0939  63  SER   C C   
4297  O  O   . SER   C  65  ? 1.7246 0.6320 1.3801 -0.0546 -0.2071 0.1593  63  SER   C O   
4298  C  CB  . SER   C  65  ? 1.7995 0.6952 1.3420 -0.0797 -0.2049 0.0529  63  SER   C CB  
4299  O  OG  . SER   C  65  ? 1.8282 0.7402 1.3502 -0.1156 -0.1956 0.0404  63  SER   C OG  
4300  N  N   . LYS   C  66  ? 1.7529 0.6230 1.3367 -0.0686 -0.2180 0.0818  64  LYS   C N   
4301  C  CA  . LYS   C  66  ? 1.7545 0.5554 1.3342 -0.0281 -0.1941 0.0710  64  LYS   C CA  
4302  C  C   . LYS   C  66  ? 1.7052 0.4711 1.3225 -0.0262 -0.2245 0.0541  64  LYS   C C   
4303  O  O   . LYS   C  66  ? 1.6705 0.3831 1.3702 -0.0243 -0.2292 0.0515  64  LYS   C O   
4304  C  CB  . LYS   C  66  ? 1.7762 0.5965 1.3919 -0.0352 -0.1599 0.0406  64  LYS   C CB  
4305  C  CG  . LYS   C  66  ? 1.8138 0.6363 1.4053 -0.0352 -0.1229 0.0362  64  LYS   C CG  
4306  C  CD  . LYS   C  66  ? 1.8671 0.6775 1.4633 -0.0355 -0.0901 -0.0124 64  LYS   C CD  
4307  C  CE  . LYS   C  66  ? 1.9038 0.6907 1.4711 -0.0106 -0.0883 -0.0878 64  LYS   C CE  
4308  N  NZ  . LYS   C  66  ? 1.9493 0.7506 1.5135 0.0130  -0.0763 -0.1361 64  LYS   C NZ  
4309  N  N   . ILE   C  67  ? 1.7015 0.5235 1.2693 -0.0272 -0.2409 0.0359  65  ILE   C N   
4310  C  CA  . ILE   C  67  ? 1.6901 0.6698 1.2451 -0.0249 -0.2276 0.0568  65  ILE   C CA  
4311  C  C   . ILE   C  67  ? 1.7571 0.7333 1.2613 -0.0457 -0.2354 -0.0234 65  ILE   C C   
4312  O  O   . ILE   C  67  ? 1.7202 0.8611 1.2640 -0.0517 -0.2285 0.0394  65  ILE   C O   
4313  C  CB  . ILE   C  67  ? 1.6849 0.5556 1.2203 -0.0452 -0.2391 0.0529  65  ILE   C CB  
4314  C  CG1 . ILE   C  67  ? 1.6405 0.5298 1.2285 -0.0560 -0.2473 0.0973  65  ILE   C CG1 
4315  C  CG2 . ILE   C  67  ? 1.6617 0.5954 1.2260 -0.0600 -0.2257 0.0443  65  ILE   C CG2 
4316  C  CD1 . ILE   C  67  ? 1.6350 0.4972 1.2445 -0.0661 -0.2518 0.1034  65  ILE   C CD1 
4317  N  N   . ASP   C  68  ? 1.8554 0.8360 1.2576 -0.0343 -0.2498 -0.0143 66  ASP   C N   
4318  C  CA  . ASP   C  68  ? 1.9258 0.8184 1.3636 -0.0218 -0.2586 -0.0252 66  ASP   C CA  
4319  C  C   . ASP   C  68  ? 2.0041 0.8094 1.3583 0.0014  -0.2578 -0.0193 66  ASP   C C   
4320  O  O   . ASP   C  68  ? 2.0854 0.8367 1.4427 0.0103  -0.2326 0.0617  66  ASP   C O   
4321  C  CB  . ASP   C  68  ? 1.9145 0.8819 1.3154 -0.0312 -0.3063 -0.0211 66  ASP   C CB  
4322  C  CG  . ASP   C  68  ? 1.9525 0.8871 1.2410 -0.0098 -0.3616 -0.0050 66  ASP   C CG  
4323  O  OD1 . ASP   C  68  ? 1.9740 0.9307 1.2081 -0.0158 -0.3502 -0.0567 66  ASP   C OD1 
4324  O  OD2 . ASP   C  68  ? 1.9448 0.7224 0.9609 0.0030  -0.5116 0.0422  66  ASP   C OD2 
4325  N  N   . SER   C  69  ? 1.9787 0.8004 1.2735 0.0013  -0.2770 0.0147  67  SER   C N   
4326  C  CA  . SER   C  69  ? 1.9330 0.7591 1.2780 0.0014  -0.2738 0.0229  67  SER   C CA  
4327  C  C   . SER   C  69  ? 1.9008 0.6958 1.2594 -0.0316 -0.2672 0.0083  67  SER   C C   
4328  O  O   . SER   C  69  ? 1.8492 0.6524 1.2741 -0.0456 -0.2632 0.0011  67  SER   C O   
4329  C  CB  . SER   C  69  ? 1.9630 0.7788 1.2892 0.0366  -0.2615 0.0210  67  SER   C CB  
4330  O  OG  . SER   C  69  ? 1.9356 0.8542 1.2797 0.0392  -0.3228 0.0253  67  SER   C OG  
4331  N  N   . HIS   C  70  ? 1.8935 0.6076 1.2196 -0.0376 -0.2807 0.0207  68  HIS   C N   
4332  C  CA  . HIS   C  70  ? 1.9117 0.5937 1.1841 -0.0560 -0.2833 0.0467  68  HIS   C CA  
4333  C  C   . HIS   C  70  ? 1.8673 0.5779 1.1864 -0.0581 -0.2537 0.0839  68  HIS   C C   
4334  O  O   . HIS   C  70  ? 1.8678 0.5499 1.1733 -0.0909 -0.2664 0.0919  68  HIS   C O   
4335  C  CB  . HIS   C  70  ? 1.9321 0.5409 1.1536 -0.0392 -0.3169 0.0445  68  HIS   C CB  
4336  C  CG  . HIS   C  70  ? 1.9250 0.5056 1.1357 -0.0404 -0.3227 0.0037  68  HIS   C CG  
4337  N  ND1 . HIS   C  70  ? 1.9594 0.6589 1.1283 -0.0204 -0.3507 0.0165  68  HIS   C ND1 
4338  C  CD2 . HIS   C  70  ? 1.9072 0.3958 1.1154 -0.0120 -0.3805 -0.0076 68  HIS   C CD2 
4339  C  CE1 . HIS   C  70  ? 1.9139 0.6753 1.1386 -0.0027 -0.3614 -0.0050 68  HIS   C CE1 
4340  N  NE2 . HIS   C  70  ? 1.9388 0.4750 1.0989 -0.0208 -0.3726 -0.0169 68  HIS   C NE2 
4341  N  N   . VAL   C  71  ? 1.8335 0.6101 1.1872 -0.0893 -0.2292 0.0805  69  VAL   C N   
4342  C  CA  . VAL   C  71  ? 1.8058 0.5669 1.2524 -0.0902 -0.2215 0.0977  69  VAL   C CA  
4343  C  C   . VAL   C  71  ? 1.7735 0.5476 1.2666 -0.0745 -0.1950 0.0853  69  VAL   C C   
4344  O  O   . VAL   C  71  ? 1.8008 0.4669 1.3141 -0.0768 -0.1728 0.1314  69  VAL   C O   
4345  C  CB  . VAL   C  71  ? 1.8163 0.5995 1.2604 -0.0813 -0.2027 0.0711  69  VAL   C CB  
4346  C  CG1 . VAL   C  71  ? 1.8181 0.5628 1.2330 -0.0896 -0.2209 0.0874  69  VAL   C CG1 
4347  C  CG2 . VAL   C  71  ? 1.8443 0.6884 1.2960 -0.1231 -0.2271 0.0481  69  VAL   C CG2 
4348  N  N   . VAL   C  72  ? 1.7089 0.5481 1.2683 -0.0807 -0.2074 0.0447  70  VAL   C N   
4349  C  CA  . VAL   C  72  ? 1.6952 0.5646 1.2829 -0.0845 -0.1937 0.0246  70  VAL   C CA  
4350  C  C   . VAL   C  72  ? 1.6900 0.4888 1.2899 -0.1149 -0.2161 0.0238  70  VAL   C C   
4351  O  O   . VAL   C  72  ? 1.6830 0.3642 1.2146 -0.1538 -0.2681 -0.0104 70  VAL   C O   
4352  C  CB  . VAL   C  72  ? 1.6807 0.5783 1.3182 -0.1077 -0.1750 0.0192  70  VAL   C CB  
4353  C  CG1 . VAL   C  72  ? 1.7088 0.6223 1.3485 -0.0899 -0.1630 -0.0020 70  VAL   C CG1 
4354  C  CG2 . VAL   C  72  ? 1.6657 0.5736 1.3422 -0.1152 -0.1749 0.0314  70  VAL   C CG2 
4355  N  N   . LEU   C  73  ? 1.6920 0.4936 1.2893 -0.1108 -0.2001 0.0029  71  LEU   C N   
4356  C  CA  . LEU   C  73  ? 1.7013 0.5937 1.2722 -0.0458 -0.1775 -0.0002 71  LEU   C CA  
4357  C  C   . LEU   C  73  ? 1.6610 0.6217 1.2616 -0.0380 -0.2068 -0.0047 71  LEU   C C   
4358  O  O   . LEU   C  73  ? 1.6537 0.7803 1.2135 -0.0526 -0.2295 -0.0577 71  LEU   C O   
4359  C  CB  . LEU   C  73  ? 1.6888 0.5215 1.2832 -0.0594 -0.1450 -0.0114 71  LEU   C CB  
4360  C  CG  . LEU   C  73  ? 1.6747 0.4981 1.3362 -0.0652 -0.1479 -0.0474 71  LEU   C CG  
4361  C  CD1 . LEU   C  73  ? 1.6754 0.4783 1.3241 -0.0365 -0.1385 -0.0539 71  LEU   C CD1 
4362  C  CD2 . LEU   C  73  ? 1.6599 0.4972 1.3469 -0.0679 -0.1278 -0.0685 71  LEU   C CD2 
4363  N  N   . SER   C  74  ? 1.6859 0.6896 1.2605 0.0230  -0.2280 0.0502  72  SER   C N   
4364  C  CA  . SER   C  74  ? 1.6538 0.6994 1.2405 0.0374  -0.2459 0.0451  72  SER   C CA  
4365  C  C   . SER   C  74  ? 1.6692 0.5984 1.1610 0.0564  -0.2909 0.0945  72  SER   C C   
4366  O  O   . SER   C  74  ? 1.6616 0.5541 1.0341 0.0892  -0.2932 0.1106  72  SER   C O   
4367  C  CB  . SER   C  74  ? 1.6762 0.7794 1.2703 0.0392  -0.2255 0.0829  72  SER   C CB  
4368  O  OG  . SER   C  74  ? 1.6842 0.8493 1.3693 0.0739  -0.2405 0.0271  72  SER   C OG  
4369  N  N   . PHE   C  75  ? 1.6939 0.5517 1.1961 0.0644  -0.2977 0.1068  73  PHE   C N   
4370  C  CA  . PHE   C  75  ? 1.7191 0.5722 1.2113 0.0541  -0.2769 0.1028  73  PHE   C CA  
4371  C  C   . PHE   C  75  ? 1.7319 0.5664 1.2096 0.0521  -0.2746 0.1274  73  PHE   C C   
4372  O  O   . PHE   C  75  ? 1.7486 0.4127 1.2050 0.0042  -0.3042 0.1482  73  PHE   C O   
4373  C  CB  . PHE   C  75  ? 1.7135 0.5451 1.2118 0.0527  -0.2732 0.0931  73  PHE   C CB  
4374  C  CG  . PHE   C  75  ? 1.7113 0.5375 1.2530 0.0336  -0.2629 0.0391  73  PHE   C CG  
4375  C  CD1 . PHE   C  75  ? 1.7198 0.5774 1.2812 0.0360  -0.2414 0.0243  73  PHE   C CD1 
4376  C  CD2 . PHE   C  75  ? 1.7369 0.5626 1.2777 0.0121  -0.2560 0.0161  73  PHE   C CD2 
4377  C  CE1 . PHE   C  75  ? 1.7245 0.6064 1.2974 0.0277  -0.2437 -0.0041 73  PHE   C CE1 
4378  C  CE2 . PHE   C  75  ? 1.7362 0.5424 1.2868 0.0301  -0.2466 -0.0054 73  PHE   C CE2 
4379  C  CZ  . PHE   C  75  ? 1.7489 0.5450 1.3013 0.0470  -0.2378 0.0053  73  PHE   C CZ  
4380  N  N   . SER   C  76  ? 1.7605 0.5841 1.2387 0.0728  -0.2581 0.1237  74  SER   C N   
4381  C  CA  . SER   C  76  ? 1.7973 0.6462 1.2983 0.0128  -0.2364 0.0863  74  SER   C CA  
4382  C  C   . SER   C  76  ? 1.7514 0.5682 1.3006 0.0363  -0.2339 0.0805  74  SER   C C   
4383  O  O   . SER   C  76  ? 1.7692 0.5586 1.3006 0.0220  -0.2236 0.0709  74  SER   C O   
4384  C  CB  . SER   C  76  ? 1.8259 0.7683 1.3192 0.0709  -0.2422 0.1184  74  SER   C CB  
4385  O  OG  . SER   C  76  ? 1.8846 0.9578 1.3537 0.0464  -0.1821 0.1456  74  SER   C OG  
4386  N  N   . GLY   C  77  ? 1.7341 0.5101 1.3380 0.0563  -0.2274 0.0566  75  GLY   C N   
4387  C  CA  . GLY   C  77  ? 1.7221 0.5022 1.3380 0.0503  -0.2273 0.0648  75  GLY   C CA  
4388  C  C   . GLY   C  77  ? 1.6983 0.4852 1.4050 0.0509  -0.2153 0.0418  75  GLY   C C   
4389  O  O   . GLY   C  77  ? 1.7430 0.4929 1.3755 0.1036  -0.1793 0.0238  75  GLY   C O   
4390  N  N   . LEU   C  78  ? 1.7259 0.5202 1.4116 -0.0221 -0.2078 0.0413  76  LEU   C N   
4391  C  CA  . LEU   C  78  ? 1.7064 0.5673 1.4265 -0.0516 -0.2213 0.0434  76  LEU   C CA  
4392  C  C   . LEU   C  78  ? 1.6243 0.5979 1.4105 -0.0296 -0.2358 0.0358  76  LEU   C C   
4393  O  O   . LEU   C  78  ? 1.6006 0.5783 1.3482 -0.0051 -0.2525 0.0553  76  LEU   C O   
4394  C  CB  . LEU   C  78  ? 1.7534 0.5693 1.4413 -0.1105 -0.2154 0.0744  76  LEU   C CB  
4395  C  CG  . LEU   C  78  ? 1.7940 0.5470 1.4629 -0.1454 -0.2191 0.0677  76  LEU   C CG  
4396  C  CD1 . LEU   C  78  ? 1.7793 0.5366 1.4825 -0.1956 -0.2188 0.0745  76  LEU   C CD1 
4397  C  CD2 . LEU   C  78  ? 1.7922 0.5912 1.5147 -0.1490 -0.2549 0.0746  76  LEU   C CD2 
4398  N  N   . ASN   C  79  ? 1.6146 0.6056 1.4368 -0.0332 -0.2370 0.0199  77  ASN   C N   
4399  C  CA  . ASN   C  79  ? 1.6060 0.6304 1.4552 -0.0175 -0.1979 0.0313  77  ASN   C CA  
4400  C  C   . ASN   C  79  ? 1.6219 0.6675 1.3964 -0.0039 -0.2054 0.0408  77  ASN   C C   
4401  O  O   . ASN   C  79  ? 1.6230 0.5626 1.3661 -0.0069 -0.2316 0.1794  77  ASN   C O   
4402  C  CB  . ASN   C  79  ? 1.5975 0.6988 1.5535 -0.0114 -0.1592 -0.0206 77  ASN   C CB  
4403  C  CG  . ASN   C  79  ? 1.6019 0.7764 1.5887 0.0096  -0.1240 0.0173  77  ASN   C CG  
4404  O  OD1 . ASN   C  79  ? 1.5831 0.8877 1.7557 0.0786  -0.0585 -0.0826 77  ASN   C OD1 
4405  N  ND2 . ASN   C  79  ? 1.5658 0.9011 1.6773 0.0213  -0.1403 -0.0119 77  ASN   C ND2 
4406  N  N   . ALA   C  80  ? 1.6175 0.6095 1.3815 -0.0292 -0.1856 0.0283  78  ALA   C N   
4407  C  CA  . ALA   C  80  ? 1.6153 0.6198 1.3448 -0.0140 -0.1825 0.0146  78  ALA   C CA  
4408  C  C   . ALA   C  80  ? 1.6020 0.6911 1.3515 -0.0030 -0.1610 0.0286  78  ALA   C C   
4409  O  O   . ALA   C  80  ? 1.6117 0.7014 1.3212 -0.0829 -0.1384 0.0689  78  ALA   C O   
4410  C  CB  . ALA   C  80  ? 1.5936 0.6054 1.3477 -0.0313 -0.1824 0.0229  78  ALA   C CB  
4411  N  N   . ASP   C  81  ? 1.6285 0.6879 1.3750 0.0213  -0.1747 0.0617  79  ASP   C N   
4412  C  CA  . ASP   C  81  ? 1.6471 0.6510 1.3672 0.0007  -0.1928 0.1032  79  ASP   C CA  
4413  C  C   . ASP   C  81  ? 1.6214 0.6482 1.3751 0.0197  -0.2180 0.1073  79  ASP   C C   
4414  O  O   . ASP   C  81  ? 1.6463 0.7242 1.4594 -0.0003 -0.2126 0.2189  79  ASP   C O   
4415  C  CB  . ASP   C  81  ? 1.6763 0.6601 1.3281 0.0179  -0.1777 0.1343  79  ASP   C CB  
4416  C  CG  . ASP   C  81  ? 1.6968 0.6550 1.2871 0.0148  -0.1534 0.1934  79  ASP   C CG  
4417  O  OD1 . ASP   C  81  ? 1.6941 0.7189 1.2861 0.0070  -0.1472 0.2315  79  ASP   C OD1 
4418  O  OD2 . ASP   C  81  ? 1.7308 0.5951 1.2125 0.0129  -0.1286 0.2371  79  ASP   C OD2 
4419  N  N   . SER   C  82  ? 1.5772 0.6078 1.3537 -0.0034 -0.2514 0.0880  80  SER   C N   
4420  C  CA  . SER   C  82  ? 1.5791 0.6452 1.3623 -0.0084 -0.2727 0.0857  80  SER   C CA  
4421  C  C   . SER   C  82  ? 1.5846 0.6262 1.3357 -0.0357 -0.2902 0.0245  80  SER   C C   
4422  O  O   . SER   C  82  ? 1.5797 0.5138 1.2691 0.0200  -0.2567 0.0212  80  SER   C O   
4423  C  CB  . SER   C  82  ? 1.6083 0.7005 1.3816 -0.0764 -0.2807 0.0997  80  SER   C CB  
4424  O  OG  . SER   C  82  ? 1.6019 0.7327 1.4390 -0.1364 -0.2975 0.1282  80  SER   C OG  
4425  N  N   . ARG   C  83  ? 1.5940 0.6202 1.4117 0.0174  -0.2849 0.0165  81  ARG   C N   
4426  C  CA  . ARG   C  83  ? 1.6039 0.5859 1.4406 -0.0084 -0.2933 0.0537  81  ARG   C CA  
4427  C  C   . ARG   C  83  ? 1.5838 0.6423 1.3840 0.0012  -0.2585 0.0512  81  ARG   C C   
4428  O  O   . ARG   C  83  ? 1.5901 0.6299 1.4450 -0.0964 -0.2557 0.0877  81  ARG   C O   
4429  C  CB  . ARG   C  83  ? 1.6233 0.6237 1.4899 0.0137  -0.3334 0.0745  81  ARG   C CB  
4430  C  CG  . ARG   C  83  ? 1.6456 0.6470 1.5055 -0.0012 -0.3340 0.0923  81  ARG   C CG  
4431  C  CD  . ARG   C  83  ? 1.6624 0.6669 1.5430 0.0131  -0.3495 0.1082  81  ARG   C CD  
4432  N  NE  . ARG   C  83  ? 1.6894 0.6592 1.5630 0.0133  -0.3886 0.0976  81  ARG   C NE  
4433  C  CZ  . ARG   C  83  ? 1.7223 0.6705 1.5542 0.0460  -0.3990 0.0704  81  ARG   C CZ  
4434  N  NH1 . ARG   C  83  ? 1.7354 0.7434 1.5594 0.0277  -0.3754 0.1261  81  ARG   C NH1 
4435  N  NH2 . ARG   C  83  ? 1.7522 0.5817 1.5439 0.0473  -0.3901 0.0434  81  ARG   C NH2 
4436  N  N   . ILE   C  84  ? 1.5876 0.4437 1.3893 0.0051  -0.2797 0.0141  82  ILE   C N   
4437  C  CA  . ILE   C  84  ? 1.6060 0.4561 1.3851 0.0015  -0.2797 0.0207  82  ILE   C CA  
4438  C  C   . ILE   C  84  ? 1.6086 0.5880 1.3558 0.0480  -0.3095 0.0409  82  ILE   C C   
4439  O  O   . ILE   C  84  ? 1.6512 0.6878 1.4496 -0.0924 -0.3017 0.0376  82  ILE   C O   
4440  C  CB  . ILE   C  84  ? 1.5919 0.4060 1.3786 0.0140  -0.2988 0.0387  82  ILE   C CB  
4441  C  CG1 . ILE   C  84  ? 1.5775 0.4302 1.4004 0.0030  -0.3046 0.0460  82  ILE   C CG1 
4442  C  CG2 . ILE   C  84  ? 1.5914 0.3899 1.3600 0.0336  -0.2894 0.0362  82  ILE   C CG2 
4443  C  CD1 . ILE   C  84  ? 1.5696 0.4643 1.4189 0.0096  -0.2969 0.0438  82  ILE   C CD1 
4444  N  N   . LEU   C  85  ? 1.6011 0.5231 1.3497 0.0235  -0.2961 0.0271  83  LEU   C N   
4445  C  CA  . LEU   C  85  ? 1.5996 0.5241 1.3622 0.0168  -0.2975 0.0527  83  LEU   C CA  
4446  C  C   . LEU   C  85  ? 1.5775 0.5377 1.3472 -0.0370 -0.3225 0.0320  83  LEU   C C   
4447  O  O   . LEU   C  85  ? 1.5919 0.5223 1.3094 -0.0226 -0.3403 0.0005  83  LEU   C O   
4448  C  CB  . LEU   C  85  ? 1.6462 0.5027 1.3895 -0.0054 -0.2998 0.0769  83  LEU   C CB  
4449  C  CG  . LEU   C  85  ? 1.6601 0.4425 1.3807 0.0068  -0.3159 0.0959  83  LEU   C CG  
4450  C  CD1 . LEU   C  85  ? 1.6752 0.4926 1.3920 0.0206  -0.3361 0.1237  83  LEU   C CD1 
4451  C  CD2 . LEU   C  85  ? 1.6508 0.4481 1.3423 0.0184  -0.3245 0.1068  83  LEU   C CD2 
4452  N  N   . ILE   C  86  ? 1.5930 0.6106 1.2963 -0.0251 -0.3207 0.0263  84  ILE   C N   
4453  C  CA  . ILE   C  86  ? 1.6091 0.6193 1.2595 -0.0251 -0.3462 0.0287  84  ILE   C CA  
4454  C  C   . ILE   C  86  ? 1.6187 0.6170 1.3212 -0.0334 -0.3430 0.0395  84  ILE   C C   
4455  O  O   . ILE   C  86  ? 1.6040 0.6360 1.3063 -0.0606 -0.4049 0.0813  84  ILE   C O   
4456  C  CB  . ILE   C  86  ? 1.6019 0.6870 1.2301 -0.0303 -0.3393 0.0110  84  ILE   C CB  
4457  C  CG1 . ILE   C  86  ? 1.6746 0.6968 1.2497 -0.0293 -0.3193 0.0194  84  ILE   C CG1 
4458  C  CG2 . ILE   C  86  ? 1.5654 0.7084 1.2046 0.0102  -0.3571 0.0403  84  ILE   C CG2 
4459  C  CD1 . ILE   C  86  ? 1.6517 0.8257 1.3143 -0.0433 -0.2810 0.0140  84  ILE   C CD1 
4460  N  N   . GLU   C  87  ? 1.6247 0.5424 1.3478 -0.0028 -0.3516 0.0514  85  GLU   C N   
4461  C  CA  . GLU   C  87  ? 1.6335 0.5398 1.4321 0.0201  -0.3502 0.0553  85  GLU   C CA  
4462  C  C   . GLU   C  87  ? 1.6446 0.4472 1.3632 0.0592  -0.3400 0.1299  85  GLU   C C   
4463  O  O   . GLU   C  87  ? 1.6947 0.4076 1.3973 0.0336  -0.3329 0.1708  85  GLU   C O   
4464  C  CB  . GLU   C  87  ? 1.6013 0.6068 1.5003 0.0352  -0.3765 0.0091  85  GLU   C CB  
4465  C  CG  . GLU   C  87  ? 1.6542 0.5908 1.5669 0.0412  -0.3537 -0.0030 85  GLU   C CG  
4466  C  CD  . GLU   C  87  ? 1.7064 0.6463 1.6828 0.0442  -0.3228 -0.0828 85  GLU   C CD  
4467  O  OE1 . GLU   C  87  ? 1.6826 0.6465 1.7679 0.1205  -0.3277 -0.0137 85  GLU   C OE1 
4468  O  OE2 . GLU   C  87  ? 1.7417 0.5989 1.7069 0.0253  -0.2439 -0.1795 85  GLU   C OE2 
4469  N  N   . LYS   C  88  ? 1.6607 0.3437 1.2948 0.0553  -0.3467 0.1625  86  LYS   C N   
4470  C  CA  . LYS   C  88  ? 1.6691 0.3773 1.2677 0.0576  -0.3320 0.1780  86  LYS   C CA  
4471  C  C   . LYS   C  88  ? 1.6885 0.4722 1.2747 0.0935  -0.3300 0.1277  86  LYS   C C   
4472  O  O   . LYS   C  88  ? 1.6584 0.5822 1.3768 0.0088  -0.3064 0.0801  86  LYS   C O   
4473  C  CB  . LYS   C  88  ? 1.6651 0.3314 1.2030 0.0407  -0.3495 0.2081  86  LYS   C CB  
4474  C  CG  . LYS   C  88  ? 1.6755 0.3189 1.2023 0.0207  -0.3575 0.2305  86  LYS   C CG  
4475  C  CD  . LYS   C  88  ? 1.6662 0.3266 1.1744 0.0184  -0.3623 0.2438  86  LYS   C CD  
4476  C  CE  . LYS   C  88  ? 1.6919 0.3692 1.1812 0.0059  -0.3726 0.2483  86  LYS   C CE  
4477  N  NZ  . LYS   C  88  ? 1.7238 0.3958 1.2121 0.0055  -0.3799 0.2777  86  LYS   C NZ  
4478  N  N   . ALA   C  89  ? 1.6720 0.4701 1.2485 0.1077  -0.3325 0.1105  87  ALA   C N   
4479  C  CA  . ALA   C  89  ? 1.6625 0.5196 1.2596 0.1034  -0.3294 0.0530  87  ALA   C CA  
4480  C  C   . ALA   C  89  ? 1.6331 0.4969 1.2325 0.1018  -0.3648 0.0622  87  ALA   C C   
4481  O  O   . ALA   C  89  ? 1.6384 0.5234 1.2241 0.1236  -0.3835 0.0285  87  ALA   C O   
4482  C  CB  . ALA   C  89  ? 1.6786 0.5362 1.2605 0.1126  -0.2994 0.0622  87  ALA   C CB  
4483  N  N   . ARG   C  90  ? 1.6289 0.4661 1.2044 0.1109  -0.3694 0.0369  88  ARG   C N   
4484  C  CA  . ARG   C  90  ? 1.6415 0.4694 1.2006 0.0901  -0.3567 0.0204  88  ARG   C CA  
4485  C  C   . ARG   C  90  ? 1.6521 0.4130 1.2425 0.1119  -0.3873 -0.0123 88  ARG   C C   
4486  O  O   . ARG   C  90  ? 1.6546 0.2413 1.3951 0.1332  -0.4184 0.0386  88  ARG   C O   
4487  C  CB  . ARG   C  90  ? 1.6420 0.5616 1.1867 0.0889  -0.3254 -0.0003 88  ARG   C CB  
4488  C  CG  . ARG   C  90  ? 1.6649 0.5801 1.1490 0.0864  -0.3050 -0.0128 88  ARG   C CG  
4489  C  CD  . ARG   C  90  ? 1.6729 0.5604 1.1616 0.0722  -0.2836 -0.0445 88  ARG   C CD  
4490  N  NE  . ARG   C  90  ? 1.7079 0.5555 1.1463 0.0544  -0.2548 -0.0836 88  ARG   C NE  
4491  C  CZ  . ARG   C  90  ? 1.7028 0.5783 1.1754 0.0614  -0.2406 -0.1334 88  ARG   C CZ  
4492  N  NH1 . ARG   C  90  ? 1.7175 0.5630 1.1614 0.1018  -0.2368 -0.1570 88  ARG   C NH1 
4493  N  NH2 . ARG   C  90  ? 1.7524 0.6103 1.1766 0.0775  -0.2136 -0.1338 88  ARG   C NH2 
4494  N  N   . VAL   C  91  ? 1.6529 0.3503 1.2427 0.0929  -0.3806 0.0109  89  VAL   C N   
4495  C  CA  . VAL   C  91  ? 1.6587 0.3286 1.2677 0.0648  -0.3682 -0.0046 89  VAL   C CA  
4496  C  C   . VAL   C  91  ? 1.6508 0.3728 1.2289 0.0609  -0.3534 0.0142  89  VAL   C C   
4497  O  O   . VAL   C  91  ? 1.6967 0.3839 1.2494 0.0638  -0.3581 -0.0225 89  VAL   C O   
4498  C  CB  . VAL   C  91  ? 1.6694 0.3057 1.2646 0.0712  -0.3724 0.0299  89  VAL   C CB  
4499  C  CG1 . VAL   C  91  ? 1.6507 0.3030 1.2638 0.0659  -0.3563 0.0133  89  VAL   C CG1 
4500  C  CG2 . VAL   C  91  ? 1.6670 0.3090 1.2831 0.0885  -0.3741 0.0545  89  VAL   C CG2 
4501  N  N   . GLU   C  92  ? 1.6237 0.3017 1.2057 0.0149  -0.3374 0.0449  90  GLU   C N   
4502  C  CA  . GLU   C  92  ? 1.6318 0.3197 1.1939 -0.0218 -0.3204 0.0820  90  GLU   C CA  
4503  C  C   . GLU   C  92  ? 1.6718 0.3094 1.1878 -0.0106 -0.3133 0.0886  90  GLU   C C   
4504  O  O   . GLU   C  92  ? 1.6578 0.2978 1.1273 -0.0054 -0.3291 0.1381  90  GLU   C O   
4505  C  CB  . GLU   C  92  ? 1.6015 0.3515 1.1869 -0.0212 -0.2950 0.0912  90  GLU   C CB  
4506  C  CG  . GLU   C  92  ? 1.6064 0.4016 1.1945 -0.0478 -0.2831 0.1215  90  GLU   C CG  
4507  C  CD  . GLU   C  92  ? 1.5978 0.4416 1.2041 -0.0810 -0.2681 0.1177  90  GLU   C CD  
4508  O  OE1 . GLU   C  92  ? 1.5783 0.5829 1.2090 -0.1150 -0.2628 0.1124  90  GLU   C OE1 
4509  O  OE2 . GLU   C  92  ? 1.6123 0.4908 1.2081 -0.0488 -0.2609 0.1314  90  GLU   C OE2 
4510  N  N   . ALA   C  93  ? 1.7040 0.3413 1.1952 -0.0543 -0.2929 0.0466  91  ALA   C N   
4511  C  CA  . ALA   C  93  ? 1.7694 0.3846 1.2289 -0.0858 -0.3096 -0.0196 91  ALA   C CA  
4512  C  C   . ALA   C  93  ? 1.7455 0.3744 1.2045 -0.1075 -0.3490 -0.0265 91  ALA   C C   
4513  O  O   . ALA   C  93  ? 1.8215 0.2270 1.3227 -0.1339 -0.2762 -0.0747 91  ALA   C O   
4514  C  CB  . ALA   C  93  ? 1.8179 0.3978 1.2549 -0.1208 -0.2964 -0.0258 91  ALA   C CB  
4515  N  N   . GLN   C  94  ? 1.7357 0.4321 1.1904 -0.0963 -0.3512 -0.0379 92  GLN   C N   
4516  C  CA  . GLN   C  94  ? 1.7080 0.4430 1.2083 -0.0884 -0.3388 -0.0650 92  GLN   C CA  
4517  C  C   . GLN   C  94  ? 1.7488 0.4744 1.2196 -0.0852 -0.3334 -0.0137 92  GLN   C C   
4518  O  O   . GLN   C  94  ? 1.8093 0.4951 1.2381 -0.1534 -0.3445 -0.0037 92  GLN   C O   
4519  C  CB  . GLN   C  94  ? 1.6852 0.4752 1.2333 -0.0482 -0.3163 -0.0790 92  GLN   C CB  
4520  C  CG  . GLN   C  94  ? 1.6373 0.5426 1.2656 -0.0299 -0.3045 -0.0768 92  GLN   C CG  
4521  C  CD  . GLN   C  94  ? 1.6381 0.6236 1.2654 -0.0354 -0.3182 -0.0762 92  GLN   C CD  
4522  O  OE1 . GLN   C  94  ? 1.6045 0.6451 1.3296 -0.0394 -0.3423 -0.0306 92  GLN   C OE1 
4523  N  NE2 . GLN   C  94  ? 1.6385 0.6258 1.2926 -0.0339 -0.3329 -0.0742 92  GLN   C NE2 
4524  N  N   . SER   C  95  ? 1.7356 0.4100 1.2258 -0.0852 -0.3190 0.0067  93  SER   C N   
4525  C  CA  . SER   C  95  ? 1.7583 0.4324 1.2317 -0.0617 -0.2980 0.0428  93  SER   C CA  
4526  C  C   . SER   C  95  ? 1.7634 0.4751 1.2227 -0.0182 -0.3127 0.0468  93  SER   C C   
4527  O  O   . SER   C  95  ? 1.7278 0.5342 1.2140 -0.0541 -0.3214 0.0459  93  SER   C O   
4528  C  CB  . SER   C  95  ? 1.7634 0.4255 1.2201 -0.0880 -0.2568 0.0704  93  SER   C CB  
4529  O  OG  . SER   C  95  ? 1.7821 0.5417 1.2904 -0.1249 -0.2142 0.0762  93  SER   C OG  
4530  N  N   . HIS   C  96  ? 1.7712 0.4391 1.2709 -0.0038 -0.2894 0.0469  94  HIS   C N   
4531  C  CA  . HIS   C  96  ? 1.7731 0.4008 1.2672 0.0132  -0.2863 0.0663  94  HIS   C CA  
4532  C  C   . HIS   C  96  ? 1.8235 0.4087 1.2534 0.0093  -0.2607 0.0747  94  HIS   C C   
4533  O  O   . HIS   C  96  ? 1.8218 0.3479 1.2326 0.0279  -0.2927 0.1704  94  HIS   C O   
4534  C  CB  . HIS   C  96  ? 1.7932 0.3586 1.2966 0.0337  -0.2716 0.0233  94  HIS   C CB  
4535  C  CG  . HIS   C  96  ? 1.8070 0.3009 1.2891 0.0314  -0.2807 0.0071  94  HIS   C CG  
4536  N  ND1 . HIS   C  96  ? 1.8584 0.3277 1.2789 0.0409  -0.2720 0.0081  94  HIS   C ND1 
4537  C  CD2 . HIS   C  96  ? 1.8132 0.2765 1.2889 0.0318  -0.2804 -0.0113 94  HIS   C CD2 
4538  C  CE1 . HIS   C  96  ? 1.8537 0.3577 1.2711 0.0235  -0.2700 -0.0119 94  HIS   C CE1 
4539  N  NE2 . HIS   C  96  ? 1.8366 0.3026 1.2812 0.0306  -0.2878 -0.0271 94  HIS   C NE2 
4540  N  N   . ARG   C  97  ? 1.8590 0.4518 1.2538 0.0078  -0.2274 0.0175  95  ARG   C N   
4541  C  CA  . ARG   C  97  ? 1.9190 0.5225 1.2884 -0.0021 -0.1980 -0.0352 95  ARG   C CA  
4542  C  C   . ARG   C  97  ? 1.9413 0.5086 1.3183 -0.0162 -0.1772 -0.0483 95  ARG   C C   
4543  O  O   . ARG   C  97  ? 1.9888 0.5227 1.3677 -0.0488 -0.1535 -0.0740 95  ARG   C O   
4544  C  CB  . ARG   C  97  ? 1.9306 0.5774 1.3141 -0.0095 -0.1685 -0.1123 95  ARG   C CB  
4545  C  CG  . ARG   C  97  ? 1.9865 0.5790 1.3142 0.0023  -0.1712 -0.1145 95  ARG   C CG  
4546  C  CD  . ARG   C  97  ? 2.0032 0.6427 1.3304 0.0065  -0.1475 -0.1319 95  ARG   C CD  
4547  N  NE  . ARG   C  97  ? 2.1076 0.6628 1.3213 -0.0202 -0.1553 -0.1539 95  ARG   C NE  
4548  C  CZ  . ARG   C  97  ? 2.1507 0.6708 1.3662 -0.0553 -0.1491 -0.1181 95  ARG   C CZ  
4549  N  NH1 . ARG   C  97  ? 2.1200 0.6605 1.4143 -0.0659 -0.1153 -0.1497 95  ARG   C NH1 
4550  N  NH2 . ARG   C  97  ? 2.2364 0.7279 1.4220 -0.0939 -0.1175 -0.1770 95  ARG   C NH2 
4551  N  N   . LEU   C  98  ? 1.9130 0.4519 1.3390 0.0000  -0.2026 -0.0530 96  LEU   C N   
4552  C  CA  . LEU   C  98  ? 1.8792 0.4006 1.3930 -0.0109 -0.1994 -0.0713 96  LEU   C CA  
4553  C  C   . LEU   C  98  ? 1.8821 0.3839 1.3715 0.0054  -0.1914 0.0269  96  LEU   C C   
4554  O  O   . LEU   C  98  ? 1.9257 0.3900 1.5059 -0.0221 -0.1707 0.0224  96  LEU   C O   
4555  C  CB  . LEU   C  98  ? 1.9249 0.3754 1.3853 0.0180  -0.2103 -0.0800 96  LEU   C CB  
4556  C  CG  . LEU   C  98  ? 1.9577 0.4113 1.4104 0.0262  -0.2335 -0.0660 96  LEU   C CG  
4557  C  CD1 . LEU   C  98  ? 1.9866 0.5386 1.4229 -0.0053 -0.1901 -0.0927 96  LEU   C CD1 
4558  C  CD2 . LEU   C  98  ? 1.9514 0.4159 1.4223 0.0265  -0.2174 -0.1171 96  LEU   C CD2 
4559  N  N   . THR   C  99  ? 1.7863 0.3482 1.2874 -0.0680 -0.1908 0.0475  97  THR   C N   
4560  C  CA  . THR   C  99  ? 1.7579 0.4022 1.2554 -0.0644 -0.2170 0.0453  97  THR   C CA  
4561  C  C   . THR   C  99  ? 1.7423 0.4605 1.2789 -0.0961 -0.2317 -0.0144 97  THR   C C   
4562  O  O   . THR   C  99  ? 1.7223 0.4217 1.2841 -0.0600 -0.2760 -0.0024 97  THR   C O   
4563  C  CB  . THR   C  99  ? 1.7049 0.4219 1.2144 -0.0879 -0.2119 0.0802  97  THR   C CB  
4564  O  OG1 . THR   C  99  ? 1.6877 0.4328 1.1992 -0.1380 -0.1685 0.1198  97  THR   C OG1 
4565  C  CG2 . THR   C  99  ? 1.6879 0.4793 1.2536 -0.0654 -0.2377 0.0554  97  THR   C CG2 
4566  N  N   . LEU   C  100 ? 1.7440 0.4855 1.2681 -0.1050 -0.2667 -0.0101 98  LEU   C N   
4567  C  CA  . LEU   C  100 ? 1.7797 0.5789 1.2515 -0.1195 -0.2826 -0.0601 98  LEU   C CA  
4568  C  C   . LEU   C  100 ? 1.8221 0.5601 1.2701 -0.0999 -0.2672 -0.0723 98  LEU   C C   
4569  O  O   . LEU   C  100 ? 1.8629 0.4760 1.2128 -0.0986 -0.2541 -0.0826 98  LEU   C O   
4570  C  CB  . LEU   C  100 ? 1.7884 0.5844 1.2820 -0.1280 -0.3025 -0.0563 98  LEU   C CB  
4571  C  CG  . LEU   C  100 ? 1.7713 0.6498 1.2351 -0.1664 -0.3166 -0.0788 98  LEU   C CG  
4572  C  CD1 . LEU   C  100 ? 1.8084 0.6645 1.2391 -0.1912 -0.3023 -0.0364 98  LEU   C CD1 
4573  C  CD2 . LEU   C  100 ? 1.7740 0.6579 1.2293 -0.1440 -0.3141 -0.1004 98  LEU   C CD2 
4574  N  N   . GLU   C  101 ? 1.8322 0.6313 1.2374 -0.0763 -0.2507 -0.0955 99  GLU   C N   
4575  C  CA  . GLU   C  101 ? 1.8848 0.6789 1.2199 -0.0614 -0.2366 -0.0798 99  GLU   C CA  
4576  C  C   . GLU   C  101 ? 1.9318 0.6787 1.1948 -0.0848 -0.2298 -0.0798 99  GLU   C C   
4577  O  O   . GLU   C  101 ? 1.9855 0.5617 1.1914 -0.0616 -0.1554 -0.1170 99  GLU   C O   
4578  C  CB  . GLU   C  101 ? 1.8993 0.6820 1.1952 -0.0532 -0.2088 -0.1004 99  GLU   C CB  
4579  C  CG  . GLU   C  101 ? 1.8984 0.7422 1.1823 -0.0295 -0.1902 -0.0752 99  GLU   C CG  
4580  C  CD  . GLU   C  101 ? 1.9465 0.7862 1.1548 -0.0322 -0.1712 -0.1171 99  GLU   C CD  
4581  O  OE1 . GLU   C  101 ? 1.9487 0.7226 1.1823 -0.0185 -0.1567 -0.1582 99  GLU   C OE1 
4582  O  OE2 . GLU   C  101 ? 1.9958 0.8829 1.0920 -0.0607 -0.1310 -0.1537 99  GLU   C OE2 
4583  N  N   . ASP   C  102 ? 1.9511 0.6898 1.2680 -0.1056 -0.2527 -0.0831 100 ASP   C N   
4584  C  CA  . ASP   C  102 ? 1.9994 0.7540 1.2762 -0.0827 -0.2717 -0.0592 100 ASP   C CA  
4585  C  C   . ASP   C  102 ? 2.0160 0.6528 1.2280 -0.0059 -0.2453 -0.0566 100 ASP   C C   
4586  O  O   . ASP   C  102 ? 2.0518 0.4382 1.2374 0.0329  -0.2924 -0.0841 100 ASP   C O   
4587  C  CB  . ASP   C  102 ? 2.0031 0.8760 1.3674 -0.0648 -0.2660 -0.0265 100 ASP   C CB  
4588  C  CG  . ASP   C  102 ? 2.0357 0.9302 1.3799 -0.0436 -0.2214 0.0255  100 ASP   C CG  
4589  O  OD1 . ASP   C  102 ? 2.1331 1.0552 1.3531 -0.1343 -0.1594 0.0630  100 ASP   C OD1 
4590  O  OD2 . ASP   C  102 ? 2.1033 0.9536 1.4837 0.0757  -0.2337 -0.0049 100 ASP   C OD2 
4591  N  N   . PRO   C  103 ? 1.9865 0.6150 1.2007 -0.0116 -0.2544 -0.0912 101 PRO   C N   
4592  C  CA  . PRO   C  103 ? 1.9514 0.6304 1.1866 -0.0278 -0.2679 -0.0730 101 PRO   C CA  
4593  C  C   . PRO   C  103 ? 1.9617 0.5723 1.1320 -0.0343 -0.2969 -0.0405 101 PRO   C C   
4594  O  O   . PRO   C  103 ? 2.0419 0.5706 1.0388 -0.0465 -0.3783 0.0445  101 PRO   C O   
4595  C  CB  . PRO   C  103 ? 1.9188 0.6126 1.1905 -0.0064 -0.2667 -0.0767 101 PRO   C CB  
4596  C  CG  . PRO   C  103 ? 1.9458 0.6665 1.1845 -0.0090 -0.2593 -0.1106 101 PRO   C CG  
4597  C  CD  . PRO   C  103 ? 1.9726 0.6578 1.1948 -0.0194 -0.2564 -0.0879 101 PRO   C CD  
4598  N  N   . VAL   C  104 ? 1.9591 0.5825 1.1030 -0.0423 -0.2910 -0.0319 102 VAL   C N   
4599  C  CA  . VAL   C  104 ? 1.9019 0.6353 1.0642 -0.0138 -0.3290 -0.0173 102 VAL   C CA  
4600  C  C   . VAL   C  104 ? 1.8324 0.6808 1.0344 -0.0004 -0.3572 -0.0597 102 VAL   C C   
4601  O  O   . VAL   C  104 ? 1.7852 0.6822 1.0164 0.0323  -0.3632 -0.1100 102 VAL   C O   
4602  C  CB  . VAL   C  104 ? 1.8763 0.5877 1.0704 -0.0198 -0.3156 -0.0004 102 VAL   C CB  
4603  C  CG1 . VAL   C  104 ? 1.9104 0.6302 1.0935 -0.0100 -0.3177 0.0251  102 VAL   C CG1 
4604  C  CG2 . VAL   C  104 ? 1.8851 0.5454 1.0693 -0.0298 -0.3072 -0.0271 102 VAL   C CG2 
4605  N  N   . THR   C  105 ? 1.7984 0.6874 0.9764 -0.0332 -0.3960 -0.0685 103 THR   C N   
4606  C  CA  . THR   C  105 ? 1.7749 0.6634 0.9698 -0.0601 -0.3758 -0.0548 103 THR   C CA  
4607  C  C   . THR   C  105 ? 1.7406 0.6305 0.9850 -0.0486 -0.3464 -0.0349 103 THR   C C   
4608  O  O   . THR   C  105 ? 1.7032 0.6490 0.9982 -0.0244 -0.3556 -0.0513 103 THR   C O   
4609  C  CB  . THR   C  105 ? 1.7724 0.6224 0.9005 -0.0677 -0.3899 -0.0481 103 THR   C CB  
4610  O  OG1 . THR   C  105 ? 1.7600 0.5439 0.8753 -0.0863 -0.4098 -0.0241 103 THR   C OG1 
4611  C  CG2 . THR   C  105 ? 1.7922 0.6379 0.9606 -0.0895 -0.3951 -0.0531 103 THR   C CG2 
4612  N  N   . VAL   C  106 ? 1.7528 0.6526 1.0130 -0.0769 -0.3024 -0.0113 104 VAL   C N   
4613  C  CA  . VAL   C  106 ? 1.7349 0.6360 1.0609 -0.0855 -0.2859 0.0150  104 VAL   C CA  
4614  C  C   . VAL   C  106 ? 1.6646 0.5503 1.0534 -0.0950 -0.3050 0.0499  104 VAL   C C   
4615  O  O   . VAL   C  106 ? 1.6110 0.5292 1.0444 -0.0438 -0.3181 0.0579  104 VAL   C O   
4616  C  CB  . VAL   C  106 ? 1.7756 0.6877 1.0740 -0.1027 -0.2645 0.0306  104 VAL   C CB  
4617  C  CG1 . VAL   C  106 ? 1.7674 0.7019 1.1048 -0.0959 -0.2663 -0.0008 104 VAL   C CG1 
4618  C  CG2 . VAL   C  106 ? 1.8057 0.7135 1.1041 -0.1128 -0.2545 -0.0064 104 VAL   C CG2 
4619  N  N   . GLU   C  107 ? 1.6649 0.5265 1.1023 -0.1266 -0.2964 0.0892  105 GLU   C N   
4620  C  CA  . GLU   C  107 ? 1.6341 0.5747 1.1488 -0.1488 -0.2852 0.0748  105 GLU   C CA  
4621  C  C   . GLU   C  107 ? 1.6358 0.6196 1.1731 -0.1316 -0.3154 0.0796  105 GLU   C C   
4622  O  O   . GLU   C  107 ? 1.6793 0.6275 1.2290 -0.1427 -0.3332 0.0446  105 GLU   C O   
4623  C  CB  . GLU   C  107 ? 1.6234 0.6322 1.1652 -0.1508 -0.2832 0.1170  105 GLU   C CB  
4624  C  CG  . GLU   C  107 ? 1.6065 0.6660 1.2504 -0.1322 -0.2813 0.0916  105 GLU   C CG  
4625  C  CD  . GLU   C  107 ? 1.5888 0.8174 1.2747 -0.1273 -0.1955 0.0892  105 GLU   C CD  
4626  O  OE1 . GLU   C  107 ? 1.5187 0.7531 1.4513 -0.1304 -0.2034 -0.0206 105 GLU   C OE1 
4627  O  OE2 . GLU   C  107 ? 1.6516 0.8269 1.4691 -0.0975 -0.1246 0.0738  105 GLU   C OE2 
4628  N  N   . TYR   C  108 ? 1.6437 0.6390 1.1724 -0.0819 -0.3299 0.0589  106 TYR   C N   
4629  C  CA  . TYR   C  108 ? 1.6293 0.6887 1.1517 -0.0845 -0.3373 0.0620  106 TYR   C CA  
4630  C  C   . TYR   C  108 ? 1.6032 0.6250 1.1324 -0.0575 -0.3151 0.0432  106 TYR   C C   
4631  O  O   . TYR   C  108 ? 1.5393 0.6660 1.1414 -0.0533 -0.3421 0.0157  106 TYR   C O   
4632  C  CB  . TYR   C  108 ? 1.6531 0.6912 1.1633 -0.0797 -0.3466 0.0771  106 TYR   C CB  
4633  C  CG  . TYR   C  108 ? 1.6478 0.7478 1.1840 -0.0662 -0.3627 0.1055  106 TYR   C CG  
4634  C  CD1 . TYR   C  108 ? 1.6429 0.7712 1.2006 -0.0680 -0.3578 0.1114  106 TYR   C CD1 
4635  C  CD2 . TYR   C  108 ? 1.6523 0.7658 1.1709 -0.0576 -0.3730 0.1375  106 TYR   C CD2 
4636  C  CE1 . TYR   C  108 ? 1.6813 0.8184 1.1926 -0.0802 -0.3595 0.1226  106 TYR   C CE1 
4637  C  CE2 . TYR   C  108 ? 1.6948 0.8625 1.1424 -0.0315 -0.3725 0.1400  106 TYR   C CE2 
4638  C  CZ  . TYR   C  108 ? 1.6819 0.8826 1.1718 -0.0545 -0.3566 0.1485  106 TYR   C CZ  
4639  O  OH  . TYR   C  108 ? 1.8196 1.0206 1.2031 0.0126  -0.3970 0.1914  106 TYR   C OH  
4640  N  N   . LEU   C  109 ? 1.6417 0.5925 1.1248 -0.0363 -0.2866 0.0401  107 LEU   C N   
4641  C  CA  . LEU   C  109 ? 1.6441 0.5671 1.1634 -0.0242 -0.2951 0.0568  107 LEU   C CA  
4642  C  C   . LEU   C  109 ? 1.6629 0.5746 1.1803 -0.0262 -0.2473 0.0533  107 LEU   C C   
4643  O  O   . LEU   C  109 ? 1.6446 0.5994 1.1882 -0.0883 -0.2364 0.0345  107 LEU   C O   
4644  C  CB  . LEU   C  109 ? 1.6513 0.5067 1.1586 0.0004  -0.3009 0.0608  107 LEU   C CB  
4645  C  CG  . LEU   C  109 ? 1.6495 0.4675 1.1950 0.0223  -0.3189 0.0762  107 LEU   C CG  
4646  C  CD1 . LEU   C  109 ? 1.6364 0.4860 1.1981 -0.0115 -0.3245 0.0942  107 LEU   C CD1 
4647  C  CD2 . LEU   C  109 ? 1.6293 0.5146 1.1953 0.0422  -0.3346 0.0767  107 LEU   C CD2 
4648  N  N   . THR   C  110 ? 1.6774 0.6002 1.2077 0.0035  -0.2218 0.0731  108 THR   C N   
4649  C  CA  . THR   C  110 ? 1.6917 0.5817 1.2317 -0.0067 -0.2391 0.0814  108 THR   C CA  
4650  C  C   . THR   C  110 ? 1.6688 0.6353 1.2634 -0.0160 -0.2258 0.0527  108 THR   C C   
4651  O  O   . THR   C  110 ? 1.6167 0.6990 1.2912 -0.0262 -0.3001 0.0580  108 THR   C O   
4652  C  CB  . THR   C  110 ? 1.7068 0.5148 1.2281 -0.0218 -0.2346 0.0809  108 THR   C CB  
4653  O  OG1 . THR   C  110 ? 1.7187 0.4202 1.1911 -0.0038 -0.2588 0.1045  108 THR   C OG1 
4654  C  CG2 . THR   C  110 ? 1.6847 0.4987 1.2194 0.0034  -0.2435 0.1239  108 THR   C CG2 
4655  N  N   . ARG   C  111 ? 1.6826 0.6378 1.3211 -0.0258 -0.2289 0.0561  109 ARG   C N   
4656  C  CA  . ARG   C  111 ? 1.6890 0.6187 1.3038 0.0014  -0.2423 0.0930  109 ARG   C CA  
4657  C  C   . ARG   C  111 ? 1.6430 0.5056 1.3065 -0.0164 -0.2484 0.0658  109 ARG   C C   
4658  O  O   . ARG   C  111 ? 1.5982 0.3992 1.3219 -0.0453 -0.2420 0.0680  109 ARG   C O   
4659  C  CB  . ARG   C  111 ? 1.6804 0.6659 1.3190 0.0008  -0.2608 0.0912  109 ARG   C CB  
4660  C  CG  . ARG   C  111 ? 1.6871 0.7243 1.2863 0.0321  -0.2702 0.0972  109 ARG   C CG  
4661  C  CD  . ARG   C  111 ? 1.6987 0.7418 1.3137 0.0347  -0.2961 0.1025  109 ARG   C CD  
4662  N  NE  . ARG   C  111 ? 1.7643 0.8107 1.2877 0.0372  -0.3098 0.1096  109 ARG   C NE  
4663  C  CZ  . ARG   C  111 ? 1.8496 0.8309 1.2914 0.0210  -0.2969 0.0797  109 ARG   C CZ  
4664  N  NH1 . ARG   C  111 ? 1.8441 0.9620 1.2555 0.0417  -0.3180 0.0848  109 ARG   C NH1 
4665  N  NH2 . ARG   C  111 ? 1.9301 0.9545 1.3389 0.0339  -0.2539 0.1582  109 ARG   C NH2 
4666  N  N   . TYR   C  112 ? 1.6417 0.5278 1.2970 -0.0048 -0.2855 0.0384  110 TYR   C N   
4667  C  CA  . TYR   C  112 ? 1.6556 0.5517 1.2803 -0.0058 -0.3113 -0.0065 110 TYR   C CA  
4668  C  C   . TYR   C  112 ? 1.6887 0.5499 1.2407 -0.0142 -0.3157 0.0006  110 TYR   C C   
4669  O  O   . TYR   C  112 ? 1.6736 0.6172 1.2302 -0.0413 -0.2844 0.0044  110 TYR   C O   
4670  C  CB  . TYR   C  112 ? 1.6635 0.5320 1.2664 0.0038  -0.3404 0.0049  110 TYR   C CB  
4671  C  CG  . TYR   C  112 ? 1.6648 0.4358 1.2178 0.0015  -0.3183 0.0027  110 TYR   C CG  
4672  C  CD1 . TYR   C  112 ? 1.6506 0.4206 1.1952 0.0207  -0.3256 -0.0043 110 TYR   C CD1 
4673  C  CD2 . TYR   C  112 ? 1.6647 0.4146 1.2231 0.0109  -0.3067 0.0015  110 TYR   C CD2 
4674  C  CE1 . TYR   C  112 ? 1.6481 0.3785 1.2139 0.0601  -0.3008 0.0239  110 TYR   C CE1 
4675  C  CE2 . TYR   C  112 ? 1.6734 0.3389 1.2343 0.0373  -0.2906 0.0300  110 TYR   C CE2 
4676  C  CZ  . TYR   C  112 ? 1.6604 0.3066 1.2501 0.0536  -0.2926 0.0368  110 TYR   C CZ  
4677  O  OH  . TYR   C  112 ? 1.6567 0.2571 1.2497 0.0310  -0.2931 0.0503  110 TYR   C OH  
4678  N  N   . VAL   C  113 ? 1.7463 0.5720 1.2639 0.0140  -0.2917 0.0394  111 VAL   C N   
4679  C  CA  . VAL   C  113 ? 1.7363 0.5665 1.2483 0.0425  -0.2953 0.0039  111 VAL   C CA  
4680  C  C   . VAL   C  113 ? 1.7386 0.5260 1.2212 0.0540  -0.3383 0.0114  111 VAL   C C   
4681  O  O   . VAL   C  113 ? 1.7923 0.3732 1.2360 0.0942  -0.3326 -0.0109 111 VAL   C O   
4682  C  CB  . VAL   C  113 ? 1.7533 0.6253 1.2859 0.0217  -0.2715 0.0242  111 VAL   C CB  
4683  C  CG1 . VAL   C  113 ? 1.7493 0.6601 1.2930 -0.0113 -0.2721 0.0384  111 VAL   C CG1 
4684  C  CG2 . VAL   C  113 ? 1.7606 0.6733 1.2776 0.0407  -0.2599 0.0150  111 VAL   C CG2 
4685  N  N   . ALA   C  114 ? 1.7358 0.4774 1.1622 0.0933  -0.3024 -0.0006 112 ALA   C N   
4686  C  CA  . ALA   C  114 ? 1.7066 0.4466 1.0795 0.0920  -0.3074 0.0596  112 ALA   C CA  
4687  C  C   . ALA   C  114 ? 1.6852 0.4455 1.0868 0.0972  -0.2970 0.0754  112 ALA   C C   
4688  O  O   . ALA   C  114 ? 1.6731 0.3117 1.0003 0.1169  -0.2402 0.1869  112 ALA   C O   
4689  C  CB  . ALA   C  114 ? 1.7384 0.4727 1.0859 0.1023  -0.3285 0.0640  112 ALA   C CB  
4690  N  N   . GLY   C  115 ? 1.6364 0.4604 1.0547 0.0830  -0.3058 0.0794  113 GLY   C N   
4691  C  CA  . GLY   C  115 ? 1.6130 0.4700 1.0485 0.1031  -0.3185 0.0760  113 GLY   C CA  
4692  C  C   . GLY   C  115 ? 1.5796 0.4381 1.0923 0.0881  -0.3156 0.0144  113 GLY   C C   
4693  O  O   . GLY   C  115 ? 1.6269 0.2446 1.0723 0.0764  -0.3880 -0.0262 113 GLY   C O   
4694  N  N   . VAL   C  116 ? 1.5438 0.5106 1.0962 0.0560  -0.3401 0.0016  114 VAL   C N   
4695  C  CA  . VAL   C  116 ? 1.5489 0.5626 1.0567 0.0756  -0.3429 0.0177  114 VAL   C CA  
4696  C  C   . VAL   C  116 ? 1.5490 0.5796 1.0347 0.0705  -0.3511 0.0047  114 VAL   C C   
4697  O  O   . VAL   C  116 ? 1.5512 0.7041 1.0083 0.0770  -0.3135 0.0623  114 VAL   C O   
4698  C  CB  . VAL   C  116 ? 1.5303 0.5788 1.0561 0.0921  -0.3670 0.0164  114 VAL   C CB  
4699  C  CG1 . VAL   C  116 ? 1.5226 0.5973 1.0723 0.0864  -0.3614 0.0037  114 VAL   C CG1 
4700  C  CG2 . VAL   C  116 ? 1.5472 0.5806 1.0531 0.1132  -0.3663 0.0171  114 VAL   C CG2 
4701  N  N   . GLN   C  117 ? 1.5771 0.5234 1.0481 0.0602  -0.3610 -0.0164 115 GLN   C N   
4702  C  CA  . GLN   C  117 ? 1.5885 0.5165 1.0792 0.0552  -0.3748 -0.0142 115 GLN   C CA  
4703  C  C   . GLN   C  117 ? 1.5609 0.4084 1.0842 0.0816  -0.3908 0.0266  115 GLN   C C   
4704  O  O   . GLN   C  117 ? 1.5672 0.4977 0.9929 0.2053  -0.4221 0.0419  115 GLN   C O   
4705  C  CB  . GLN   C  117 ? 1.6306 0.5335 1.0169 -0.0034 -0.3488 -0.0530 115 GLN   C CB  
4706  C  CG  . GLN   C  117 ? 1.6351 0.5856 1.0757 -0.0430 -0.3275 -0.1126 115 GLN   C CG  
4707  C  CD  . GLN   C  117 ? 1.6861 0.6076 1.1398 -0.0518 -0.2850 -0.0569 115 GLN   C CD  
4708  O  OE1 . GLN   C  117 ? 1.7143 0.7127 1.1894 -0.0942 -0.3272 -0.0523 115 GLN   C OE1 
4709  N  NE2 . GLN   C  117 ? 1.6957 0.6062 1.1003 -0.0521 -0.2815 -0.0616 115 GLN   C NE2 
4710  N  N   . GLN   C  118 ? 1.5844 0.3054 1.1266 0.0504  -0.3960 0.0498  116 GLN   C N   
4711  C  CA  . GLN   C  118 ? 1.6068 0.3231 1.1595 0.0416  -0.3716 0.0321  116 GLN   C CA  
4712  C  C   . GLN   C  118 ? 1.5919 0.3518 1.1442 0.0106  -0.3795 0.0066  116 GLN   C C   
4713  O  O   . GLN   C  118 ? 1.5922 0.1994 1.3023 0.0517  -0.3465 -0.0241 116 GLN   C O   
4714  C  CB  . GLN   C  118 ? 1.6210 0.3477 1.1374 0.0386  -0.3943 0.0835  116 GLN   C CB  
4715  C  CG  . GLN   C  118 ? 1.6526 0.3510 1.1013 0.0434  -0.3857 0.0807  116 GLN   C CG  
4716  C  CD  . GLN   C  118 ? 1.6688 0.3474 1.0692 0.0361  -0.4190 0.0564  116 GLN   C CD  
4717  O  OE1 . GLN   C  118 ? 1.6665 0.2848 1.0162 -0.0291 -0.4744 0.0645  116 GLN   C OE1 
4718  N  NE2 . GLN   C  118 ? 1.6944 0.3566 1.0680 0.0266  -0.4240 0.1137  116 GLN   C NE2 
4719  N  N   . ARG   C  119 ? 1.5715 0.4074 1.2476 0.0590  -0.3564 0.0188  117 ARG   C N   
4720  C  CA  . ARG   C  119 ? 1.5805 0.5399 1.2274 -0.0083 -0.3363 0.0497  117 ARG   C CA  
4721  C  C   . ARG   C  119 ? 1.5195 0.5164 1.1876 0.0088  -0.3185 0.0713  117 ARG   C C   
4722  O  O   . ARG   C  119 ? 1.4298 0.5837 1.1657 -0.0360 -0.3500 0.0910  117 ARG   C O   
4723  C  CB  . ARG   C  119 ? 1.6413 0.5542 1.2959 0.0027  -0.3072 0.0306  117 ARG   C CB  
4724  C  CG  . ARG   C  119 ? 1.7273 0.6200 1.2904 -0.0490 -0.2710 0.0310  117 ARG   C CG  
4725  C  CD  . ARG   C  119 ? 1.8350 0.5789 1.3860 -0.0784 -0.2135 0.0170  117 ARG   C CD  
4726  N  NE  . ARG   C  119 ? 1.9653 0.7240 1.3899 -0.1649 -0.1866 -0.0006 117 ARG   C NE  
4727  C  CZ  . ARG   C  119 ? 2.0131 0.8210 1.4655 -0.1953 -0.1249 -0.0439 117 ARG   C CZ  
4728  N  NH1 . ARG   C  119 ? 2.0199 0.8856 1.4015 -0.1562 -0.1717 -0.0023 117 ARG   C NH1 
4729  N  NH2 . ARG   C  119 ? 2.0742 0.6756 1.5356 -0.2407 -0.0273 -0.1457 117 ARG   C NH2 
4730  N  N   . TYR   C  120 ? 1.5108 0.4695 1.2875 0.0031  -0.3250 0.0776  118 TYR   C N   
4731  C  CA  . TYR   C  120 ? 1.5096 0.5103 1.3100 -0.0029 -0.3444 0.0797  118 TYR   C CA  
4732  C  C   . TYR   C  120 ? 1.4985 0.5671 1.3539 0.0507  -0.3215 0.0885  118 TYR   C C   
4733  O  O   . TYR   C  120 ? 1.4241 0.5710 1.3663 0.0943  -0.3682 0.1214  118 TYR   C O   
4734  C  CB  . TYR   C  120 ? 1.5109 0.5185 1.3677 0.0150  -0.3199 0.0695  118 TYR   C CB  
4735  C  CG  . TYR   C  120 ? 1.5170 0.5047 1.4037 0.0099  -0.3063 0.0822  118 TYR   C CG  
4736  C  CD1 . TYR   C  120 ? 1.4910 0.4982 1.3941 -0.0002 -0.2886 0.1002  118 TYR   C CD1 
4737  C  CD2 . TYR   C  120 ? 1.5205 0.5465 1.4264 -0.0028 -0.3049 0.0837  118 TYR   C CD2 
4738  C  CE1 . TYR   C  120 ? 1.5234 0.4750 1.3787 0.0040  -0.2610 0.1167  118 TYR   C CE1 
4739  C  CE2 . TYR   C  120 ? 1.5254 0.5007 1.4013 -0.0263 -0.2971 0.0785  118 TYR   C CE2 
4740  C  CZ  . TYR   C  120 ? 1.5051 0.4197 1.3914 0.0483  -0.2609 0.1223  118 TYR   C CZ  
4741  O  OH  . TYR   C  120 ? 1.5226 0.4092 1.4077 0.0557  -0.2386 0.1534  118 TYR   C OH  
4742  N  N   . THR   C  121 ? 1.4804 0.5492 1.3440 0.0115  -0.3163 0.0419  119 THR   C N   
4743  C  CA  . THR   C  121 ? 1.6017 0.4380 1.3169 -0.0317 -0.3097 0.0726  119 THR   C CA  
4744  C  C   . THR   C  121 ? 1.6780 0.5250 1.3677 -0.0655 -0.2557 0.0508  119 THR   C C   
4745  O  O   . THR   C  121 ? 1.7478 0.4426 1.5339 -0.0557 -0.2432 0.0730  119 THR   C O   
4746  C  CB  . THR   C  121 ? 1.6119 0.3152 1.2883 -0.0583 -0.2877 0.0920  119 THR   C CB  
4747  O  OG1 . THR   C  121 ? 1.5484 0.2969 1.1973 -0.0240 -0.3160 0.1898  119 THR   C OG1 
4748  C  CG2 . THR   C  121 ? 1.6273 0.2867 1.2910 -0.0743 -0.2916 0.0890  119 THR   C CG2 
4749  N  N   . GLN   C  122 ? 1.7293 0.5053 1.3353 -0.0387 -0.3196 0.0548  120 GLN   C N   
4750  C  CA  . GLN   C  122 ? 1.7522 0.4329 1.3373 -0.0258 -0.3293 0.0615  120 GLN   C CA  
4751  C  C   . GLN   C  122 ? 1.6892 0.2975 1.3948 -0.0513 -0.3110 -0.0158 120 GLN   C C   
4752  O  O   . GLN   C  122 ? 1.7842 0.2752 1.3814 -0.0376 -0.2625 -0.0061 120 GLN   C O   
4753  C  CB  . GLN   C  122 ? 1.7706 0.4935 1.3859 -0.0672 -0.3435 0.0170  120 GLN   C CB  
4754  C  CG  . GLN   C  122 ? 1.8051 0.4790 1.4142 -0.0437 -0.3451 0.0009  120 GLN   C CG  
4755  C  CD  . GLN   C  122 ? 1.8049 0.5421 1.4584 -0.0320 -0.2951 -0.0411 120 GLN   C CD  
4756  O  OE1 . GLN   C  122 ? 1.8281 0.4906 1.4222 -0.0522 -0.2965 -0.0767 120 GLN   C OE1 
4757  N  NE2 . GLN   C  122 ? 1.8163 0.5938 1.4724 -0.0107 -0.3347 -0.0339 120 GLN   C NE2 
4758  N  N   . SER   C  123 ? 1.6824 0.2679 1.3056 -0.0126 -0.3499 0.0209  121 SER   C N   
4759  C  CA  . SER   C  123 ? 1.6872 0.3315 1.2096 -0.0093 -0.3259 0.0487  121 SER   C CA  
4760  C  C   . SER   C  123 ? 1.7397 0.4329 1.2098 0.0170  -0.3757 0.0177  121 SER   C C   
4761  O  O   . SER   C  123 ? 1.7540 0.5956 1.0964 -0.1010 -0.3679 0.0901  121 SER   C O   
4762  C  CB  . SER   C  123 ? 1.6275 0.3603 1.1436 0.0276  -0.3569 0.1070  121 SER   C CB  
4763  O  OG  . SER   C  123 ? 1.5637 0.3879 1.1382 0.0540  -0.3439 0.0834  121 SER   C OG  
4764  N  N   . GLY   C  124 ? 1.7141 0.2881 1.2144 -0.0200 -0.3601 -0.0103 122 GLY   C N   
4765  C  CA  . GLY   C  124 ? 1.6861 0.3108 1.2309 -0.0238 -0.3652 -0.0178 122 GLY   C CA  
4766  C  C   . GLY   C  124 ? 1.6907 0.2731 1.2136 0.0351  -0.3713 -0.0460 122 GLY   C C   
4767  O  O   . GLY   C  124 ? 1.6493 0.3155 1.1229 0.0087  -0.4017 -0.1065 122 GLY   C O   
4768  N  N   . GLY   C  125 ? 1.6528 0.3570 1.2553 -0.0044 -0.3675 -0.0532 123 GLY   C N   
4769  C  CA  . GLY   C  125 ? 1.6527 0.3553 1.2658 0.0590  -0.3664 -0.0211 123 GLY   C CA  
4770  C  C   . GLY   C  125 ? 1.6410 0.3400 1.2919 0.0885  -0.3384 -0.0166 123 GLY   C C   
4771  O  O   . GLY   C  125 ? 1.6573 0.2741 1.2475 0.2061  -0.3630 0.0312  123 GLY   C O   
4772  N  N   . VAL   C  126 ? 1.6901 0.3884 1.2838 0.0351  -0.3554 -0.0004 124 VAL   C N   
4773  C  CA  . VAL   C  126 ? 1.7210 0.3921 1.3034 0.0132  -0.3463 0.0178  124 VAL   C CA  
4774  C  C   . VAL   C  126 ? 1.7984 0.3808 1.3096 0.0116  -0.3371 0.0231  124 VAL   C C   
4775  O  O   . VAL   C  126 ? 1.8742 0.1472 1.3232 0.0307  -0.3223 -0.0106 124 VAL   C O   
4776  C  CB  . VAL   C  126 ? 1.7000 0.3962 1.3585 0.0189  -0.3651 0.0011  124 VAL   C CB  
4777  C  CG1 . VAL   C  126 ? 1.6947 0.4618 1.3598 0.0190  -0.3716 0.0714  124 VAL   C CG1 
4778  C  CG2 . VAL   C  126 ? 1.7005 0.3990 1.4002 0.0644  -0.3684 0.0194  124 VAL   C CG2 
4779  N  N   . ARG   C  127 ? 1.8035 0.4517 1.3145 0.0147  -0.3129 0.0308  125 ARG   C N   
4780  C  CA  . ARG   C  127 ? 1.7589 0.4540 1.2779 -0.0154 -0.2965 0.0390  125 ARG   C CA  
4781  C  C   . ARG   C  127 ? 1.7026 0.4639 1.2625 0.0252  -0.3454 0.0812  125 ARG   C C   
4782  O  O   . ARG   C  127 ? 1.6177 0.5452 1.0964 -0.0089 -0.3846 0.0133  125 ARG   C O   
4783  C  CB  . ARG   C  127 ? 1.7779 0.4780 1.3218 -0.0366 -0.2470 0.0711  125 ARG   C CB  
4784  C  CG  . ARG   C  127 ? 1.7774 0.4731 1.3369 -0.0672 -0.2194 0.0850  125 ARG   C CG  
4785  C  CD  . ARG   C  127 ? 1.8078 0.4793 1.3337 -0.0758 -0.2085 0.0899  125 ARG   C CD  
4786  N  NE  . ARG   C  127 ? 1.7967 0.4874 1.3206 -0.1143 -0.1924 0.1034  125 ARG   C NE  
4787  C  CZ  . ARG   C  127 ? 1.7914 0.4370 1.3376 -0.0890 -0.1533 0.0994  125 ARG   C CZ  
4788  N  NH1 . ARG   C  127 ? 1.8101 0.3772 1.3356 -0.0720 -0.1638 0.1071  125 ARG   C NH1 
4789  N  NH2 . ARG   C  127 ? 1.7838 0.3810 1.3367 -0.1015 -0.1531 0.0800  125 ARG   C NH2 
4790  N  N   . PRO   C  128 ? 1.7119 0.4671 1.2735 0.0517  -0.3337 0.0800  126 PRO   C N   
4791  C  CA  . PRO   C  128 ? 1.7276 0.4627 1.2686 0.0772  -0.3059 0.0803  126 PRO   C CA  
4792  C  C   . PRO   C  128 ? 1.6897 0.3861 1.3147 0.0737  -0.3102 0.0869  126 PRO   C C   
4793  O  O   . PRO   C  128 ? 1.6815 0.3072 1.3250 0.0812  -0.3141 0.1051  126 PRO   C O   
4794  C  CB  . PRO   C  128 ? 1.7184 0.5161 1.3023 0.0980  -0.3027 0.0865  126 PRO   C CB  
4795  C  CG  . PRO   C  128 ? 1.7312 0.5453 1.2832 0.0681  -0.3190 0.0690  126 PRO   C CG  
4796  C  CD  . PRO   C  128 ? 1.7229 0.5062 1.2760 0.0579  -0.3151 0.0597  126 PRO   C CD  
4797  N  N   . PHE   C  129 ? 1.7700 0.3932 1.2997 0.1125  -0.2907 0.0889  127 PHE   C N   
4798  C  CA  . PHE   C  129 ? 1.7662 0.5122 1.3059 0.0648  -0.2956 0.0287  127 PHE   C CA  
4799  C  C   . PHE   C  129 ? 1.7779 0.4665 1.3534 -0.0070 -0.2607 -0.0204 127 PHE   C C   
4800  O  O   . PHE   C  129 ? 1.7445 0.6380 1.4010 0.0160  -0.2743 -0.1128 127 PHE   C O   
4801  C  CB  . PHE   C  129 ? 1.7723 0.5078 1.3152 0.0503  -0.3440 0.0441  127 PHE   C CB  
4802  C  CG  . PHE   C  129 ? 1.7196 0.5550 1.2846 0.0590  -0.3786 0.0877  127 PHE   C CG  
4803  C  CD1 . PHE   C  129 ? 1.7051 0.5730 1.2634 0.0548  -0.4042 0.0908  127 PHE   C CD1 
4804  C  CD2 . PHE   C  129 ? 1.7307 0.5491 1.2904 0.0622  -0.3807 0.1152  127 PHE   C CD2 
4805  C  CE1 . PHE   C  129 ? 1.6750 0.5714 1.2898 0.0471  -0.4001 0.0980  127 PHE   C CE1 
4806  C  CE2 . PHE   C  129 ? 1.7067 0.5544 1.2823 0.0657  -0.3959 0.1156  127 PHE   C CE2 
4807  C  CZ  . PHE   C  129 ? 1.6859 0.5881 1.2956 0.0379  -0.4051 0.1080  127 PHE   C CZ  
4808  N  N   . GLY   C  130 ? 1.7974 0.4645 1.3635 -0.0352 -0.2463 -0.0649 128 GLY   C N   
4809  C  CA  . GLY   C  130 ? 1.8014 0.4937 1.3448 -0.0478 -0.2164 -0.0433 128 GLY   C CA  
4810  C  C   . GLY   C  130 ? 1.7668 0.3950 1.3439 -0.0687 -0.2117 -0.0460 128 GLY   C C   
4811  O  O   . GLY   C  130 ? 1.7387 0.3942 1.3667 -0.0089 -0.1578 -0.1118 128 GLY   C O   
4812  N  N   . VAL   C  131 ? 1.7174 0.4242 1.3213 -0.0804 -0.2140 0.0110  129 VAL   C N   
4813  C  CA  . VAL   C  131 ? 1.6623 0.4932 1.3073 -0.1048 -0.2491 0.0105  129 VAL   C CA  
4814  C  C   . VAL   C  131 ? 1.6766 0.4776 1.2847 -0.1178 -0.2599 0.0517  129 VAL   C C   
4815  O  O   . VAL   C  131 ? 1.6871 0.5369 1.2613 -0.1548 -0.2666 0.0249  129 VAL   C O   
4816  C  CB  . VAL   C  131 ? 1.6355 0.5068 1.3008 -0.1028 -0.2625 -0.0393 129 VAL   C CB  
4817  C  CG1 . VAL   C  131 ? 1.6263 0.5217 1.3063 -0.1193 -0.2735 -0.0471 129 VAL   C CG1 
4818  C  CG2 . VAL   C  131 ? 1.6280 0.5570 1.3312 -0.1072 -0.2502 -0.0255 129 VAL   C CG2 
4819  N  N   . SER   C  132 ? 1.6864 0.5013 1.3191 -0.1064 -0.2298 0.1109  130 SER   C N   
4820  C  CA  . SER   C  132 ? 1.6700 0.5620 1.3184 -0.0896 -0.2347 0.1441  130 SER   C CA  
4821  C  C   . SER   C  132 ? 1.6720 0.5122 1.2870 -0.0623 -0.2274 0.2037  130 SER   C C   
4822  O  O   . SER   C  132 ? 1.6725 0.4840 1.2614 -0.0387 -0.2132 0.2187  130 SER   C O   
4823  C  CB  . SER   C  132 ? 1.6477 0.6229 1.3573 -0.0562 -0.2552 0.1545  130 SER   C CB  
4824  O  OG  . SER   C  132 ? 1.6291 0.8032 1.3919 -0.0882 -0.2280 0.0979  130 SER   C OG  
4825  N  N   . THR   C  133 ? 1.6927 0.5006 1.2725 -0.0502 -0.2646 0.2263  131 THR   C N   
4826  C  CA  . THR   C  133 ? 1.7278 0.5854 1.2653 -0.0239 -0.2418 0.2251  131 THR   C CA  
4827  C  C   . THR   C  133 ? 1.7701 0.5467 1.2451 -0.0300 -0.2264 0.2875  131 THR   C C   
4828  O  O   . THR   C  133 ? 1.7943 0.4289 1.2139 0.0102  -0.1928 0.3428  131 THR   C O   
4829  C  CB  . THR   C  133 ? 1.7008 0.5930 1.2839 -0.0010 -0.2925 0.2304  131 THR   C CB  
4830  O  OG1 . THR   C  133 ? 1.7012 0.5806 1.3192 -0.0360 -0.3274 0.2170  131 THR   C OG1 
4831  C  CG2 . THR   C  133 ? 1.7018 0.6372 1.2812 0.0170  -0.2993 0.1947  131 THR   C CG2 
4832  N  N   . LEU   C  134 ? 1.7826 0.6029 1.2630 -0.0566 -0.2100 0.2532  132 LEU   C N   
4833  C  CA  . LEU   C  134 ? 1.7620 0.6265 1.3009 -0.0662 -0.2241 0.2082  132 LEU   C CA  
4834  C  C   . LEU   C  134 ? 1.7242 0.6238 1.3041 -0.1054 -0.2186 0.1669  132 LEU   C C   
4835  O  O   . LEU   C  134 ? 1.7126 0.5068 1.3443 -0.1375 -0.2233 0.1351  132 LEU   C O   
4836  C  CB  . LEU   C  134 ? 1.7649 0.6679 1.3132 -0.0733 -0.2315 0.2308  132 LEU   C CB  
4837  C  CG  . LEU   C  134 ? 1.7638 0.6588 1.3436 -0.0937 -0.2739 0.2199  132 LEU   C CG  
4838  C  CD1 . LEU   C  134 ? 1.7755 0.6722 1.3696 -0.1267 -0.2754 0.2163  132 LEU   C CD1 
4839  C  CD2 . LEU   C  134 ? 1.7640 0.6723 1.3472 -0.0908 -0.2677 0.2380  132 LEU   C CD2 
4840  N  N   . ILE   C  135 ? 1.6981 0.6707 1.3046 -0.1014 -0.2256 0.1438  133 ILE   C N   
4841  C  CA  . ILE   C  135 ? 1.6985 0.6925 1.2905 -0.0673 -0.2323 0.1134  133 ILE   C CA  
4842  C  C   . ILE   C  135 ? 1.7088 0.6594 1.2919 -0.0949 -0.2137 0.0684  133 ILE   C C   
4843  O  O   . ILE   C  135 ? 1.6878 0.6310 1.2642 -0.1477 -0.2123 0.0515  133 ILE   C O   
4844  C  CB  . ILE   C  135 ? 1.6928 0.6838 1.2525 -0.0163 -0.2480 0.1247  133 ILE   C CB  
4845  C  CG1 . ILE   C  135 ? 1.6842 0.7450 1.2669 0.0178  -0.2454 0.0804  133 ILE   C CG1 
4846  C  CG2 . ILE   C  135 ? 1.7032 0.6814 1.2219 -0.0105 -0.2663 0.1306  133 ILE   C CG2 
4847  C  CD1 . ILE   C  135 ? 1.6587 0.7687 1.2731 0.0331  -0.2143 0.0422  133 ILE   C CD1 
4848  N  N   . ALA   C  136 ? 1.7066 0.6586 1.3447 -0.0620 -0.2087 0.0543  134 ALA   C N   
4849  C  CA  . ALA   C  136 ? 1.7427 0.7214 1.3645 -0.0447 -0.2489 0.0737  134 ALA   C CA  
4850  C  C   . ALA   C  136 ? 1.7717 0.7225 1.4201 -0.0565 -0.2637 0.0458  134 ALA   C C   
4851  O  O   . ALA   C  136 ? 1.7818 0.7582 1.4843 -0.0535 -0.2972 0.0333  134 ALA   C O   
4852  C  CB  . ALA   C  136 ? 1.7543 0.7025 1.3857 -0.0344 -0.2454 0.0783  134 ALA   C CB  
4853  N  N   . GLY   C  137 ? 1.7918 0.7727 1.4184 -0.0548 -0.2952 0.0636  135 GLY   C N   
4854  C  CA  . GLY   C  137 ? 1.8553 0.8386 1.3761 -0.0197 -0.2690 0.0302  135 GLY   C CA  
4855  C  C   . GLY   C  137 ? 1.8955 0.8651 1.2981 -0.0195 -0.2935 0.0628  135 GLY   C C   
4856  O  O   . GLY   C  137 ? 1.9750 0.8562 1.1891 -0.0135 -0.3250 0.0876  135 GLY   C O   
4857  N  N   . PHE   C  138 ? 1.9435 0.8683 1.2898 -0.0457 -0.2752 0.0530  136 PHE   C N   
4858  C  CA  . PHE   C  138 ? 1.9876 0.8885 1.2648 -0.0410 -0.3000 0.0561  136 PHE   C CA  
4859  C  C   . PHE   C  138 ? 1.9997 0.8997 1.2645 -0.0522 -0.3045 0.0625  136 PHE   C C   
4860  O  O   . PHE   C  138 ? 2.0547 0.8918 1.2904 -0.0222 -0.2749 0.0888  136 PHE   C O   
4861  C  CB  . PHE   C  138 ? 2.0123 0.8873 1.2825 -0.0400 -0.2663 0.0661  136 PHE   C CB  
4862  C  CG  . PHE   C  138 ? 1.9846 0.8831 1.3339 -0.0324 -0.2750 0.0847  136 PHE   C CG  
4863  C  CD1 . PHE   C  138 ? 1.9646 0.8986 1.3737 -0.0209 -0.2636 0.1146  136 PHE   C CD1 
4864  C  CD2 . PHE   C  138 ? 2.0034 0.8815 1.3195 -0.0446 -0.2837 0.1053  136 PHE   C CD2 
4865  C  CE1 . PHE   C  138 ? 1.9771 0.9348 1.3679 -0.0163 -0.2679 0.1436  136 PHE   C CE1 
4866  C  CE2 . PHE   C  138 ? 2.0063 0.9341 1.3069 -0.0507 -0.2857 0.1365  136 PHE   C CE2 
4867  C  CZ  . PHE   C  138 ? 1.9982 0.9497 1.3201 -0.0491 -0.2739 0.1527  136 PHE   C CZ  
4868  N  N   . ASP   C  139 ? 1.9906 0.8581 1.2395 -0.0798 -0.3527 0.0756  137 ASP   C N   
4869  C  CA  . ASP   C  139 ? 1.9834 0.8644 1.2536 -0.0697 -0.3898 0.1023  137 ASP   C CA  
4870  C  C   . ASP   C  139 ? 2.0715 0.9425 1.1538 -0.0803 -0.3892 0.0672  137 ASP   C C   
4871  O  O   . ASP   C  139 ? 2.0474 0.8919 1.1421 -0.0856 -0.4259 0.0899  137 ASP   C O   
4872  C  CB  . ASP   C  139 ? 1.9711 0.9272 1.3034 -0.0653 -0.4442 0.1262  137 ASP   C CB  
4873  C  CG  . ASP   C  139 ? 1.9340 0.8670 1.3800 -0.0825 -0.4562 0.1258  137 ASP   C CG  
4874  O  OD1 . ASP   C  139 ? 1.9015 0.8387 1.5035 -0.1806 -0.4508 0.2075  137 ASP   C OD1 
4875  O  OD2 . ASP   C  139 ? 1.9378 0.8873 1.4335 -0.0510 -0.5491 0.1587  137 ASP   C OD2 
4876  N  N   . PRO   C  140 ? 2.1161 0.8859 1.2376 -0.0556 -0.3896 0.0195  138 PRO   C N   
4877  C  CA  . PRO   C  140 ? 2.1444 0.8604 1.3079 -0.0579 -0.3306 0.0302  138 PRO   C CA  
4878  C  C   . PRO   C  140 ? 2.1887 0.8467 1.3633 -0.1174 -0.3627 0.0465  138 PRO   C C   
4879  O  O   . PRO   C  140 ? 2.2193 0.8226 1.4069 -0.1317 -0.2902 0.1251  138 PRO   C O   
4880  C  CB  . PRO   C  140 ? 2.1140 0.8727 1.2522 -0.0189 -0.3861 0.0236  138 PRO   C CB  
4881  C  CG  . PRO   C  140 ? 2.1027 0.8373 1.2737 -0.0275 -0.3723 0.0108  138 PRO   C CG  
4882  C  CD  . PRO   C  140 ? 2.0818 0.8662 1.2527 -0.0134 -0.3901 0.0562  138 PRO   C CD  
4883  N  N   . ARG   C  141 ? 2.1932 0.8126 1.4164 -0.1240 -0.3082 0.0505  139 ARG   C N   
4884  C  CA  . ARG   C  141 ? 2.2556 0.9239 1.4215 -0.1453 -0.3158 0.0352  139 ARG   C CA  
4885  C  C   . ARG   C  141 ? 2.2160 0.9627 1.4937 -0.1529 -0.3401 0.0488  139 ARG   C C   
4886  O  O   . ARG   C  141 ? 2.2867 0.8929 1.5802 -0.2166 -0.3974 0.0282  139 ARG   C O   
4887  C  CB  . ARG   C  141 ? 2.2688 0.9595 1.4632 -0.1768 -0.2941 0.0250  139 ARG   C CB  
4888  C  CG  . ARG   C  141 ? 2.2961 0.8758 1.4934 -0.1956 -0.2408 0.0000  139 ARG   C CG  
4889  C  CD  . ARG   C  141 ? 2.3408 0.8828 1.5521 -0.2302 -0.2601 -0.0165 139 ARG   C CD  
4890  N  NE  . ARG   C  141 ? 2.3084 0.8972 1.6327 -0.2209 -0.2490 -0.0450 139 ARG   C NE  
4891  C  CZ  . ARG   C  141 ? 2.2747 0.8871 1.6524 -0.1671 -0.2565 -0.0660 139 ARG   C CZ  
4892  N  NH1 . ARG   C  141 ? 2.2894 0.9430 1.7158 -0.1553 -0.2947 -0.0641 139 ARG   C NH1 
4893  N  NH2 . ARG   C  141 ? 2.2857 0.7961 1.6671 -0.1385 -0.2527 -0.1130 139 ARG   C NH2 
4894  N  N   . ASP   C  142 ? 2.1716 0.9590 1.5130 -0.1557 -0.3074 0.0842  140 ASP   C N   
4895  C  CA  . ASP   C  142 ? 2.1214 1.0258 1.4046 -0.1543 -0.3054 0.1953  140 ASP   C CA  
4896  C  C   . ASP   C  142 ? 2.1257 1.0619 1.3884 -0.1484 -0.2551 0.2031  140 ASP   C C   
4897  O  O   . ASP   C  142 ? 2.0934 1.0060 1.3686 -0.1557 -0.2119 0.2665  140 ASP   C O   
4898  C  CB  . ASP   C  142 ? 2.0615 0.9917 1.3982 -0.0789 -0.3351 0.2209  140 ASP   C CB  
4899  C  CG  . ASP   C  142 ? 2.0219 1.0344 1.3201 -0.0941 -0.3793 0.2804  140 ASP   C CG  
4900  O  OD1 . ASP   C  142 ? 2.0239 1.0163 1.3661 -0.1321 -0.3828 0.2000  140 ASP   C OD1 
4901  O  OD2 . ASP   C  142 ? 2.0135 0.9427 1.2829 -0.0173 -0.2940 0.3641  140 ASP   C OD2 
4902  N  N   . ASP   C  143 ? 2.1578 1.1235 1.3355 -0.1491 -0.2408 0.2006  141 ASP   C N   
4903  C  CA  . ASP   C  143 ? 2.2077 1.1366 1.3991 -0.1691 -0.1685 0.1781  141 ASP   C CA  
4904  C  C   . ASP   C  143 ? 2.2419 1.1435 1.4104 -0.1596 -0.1648 0.1727  141 ASP   C C   
4905  O  O   . ASP   C  143 ? 2.2951 1.1507 1.4031 -0.1420 -0.1289 0.1786  141 ASP   C O   
4906  C  CB  . ASP   C  143 ? 2.2407 1.1891 1.3847 -0.1971 -0.1334 0.2131  141 ASP   C CB  
4907  C  CG  . ASP   C  143 ? 2.2513 1.2292 1.3465 -0.1997 -0.1435 0.2236  141 ASP   C CG  
4908  O  OD1 . ASP   C  143 ? 2.2029 1.2781 1.4554 -0.1488 -0.1424 0.2432  141 ASP   C OD1 
4909  O  OD2 . ASP   C  143 ? 2.3221 1.2530 1.3122 -0.2239 -0.0858 0.2423  141 ASP   C OD2 
4910  N  N   . GLU   C  144 ? 2.2086 1.1102 1.4597 -0.1556 -0.1641 0.1327  142 GLU   C N   
4911  C  CA  . GLU   C  144 ? 2.1057 1.0930 1.4850 -0.1570 -0.2190 0.1418  142 GLU   C CA  
4912  C  C   . GLU   C  144 ? 2.0608 1.0252 1.5440 -0.1295 -0.2272 0.1024  142 GLU   C C   
4913  O  O   . GLU   C  144 ? 1.9730 1.0715 1.4693 -0.1572 -0.3429 -0.0110 142 GLU   C O   
4914  C  CB  . GLU   C  144 ? 2.1287 1.1566 1.5462 -0.1299 -0.1723 0.1729  142 GLU   C CB  
4915  C  CG  . GLU   C  144 ? 2.1438 1.1901 1.5571 -0.0979 -0.1593 0.2038  142 GLU   C CG  
4916  C  CD  . GLU   C  144 ? 2.1884 1.2657 1.5311 -0.0930 -0.1433 0.1550  142 GLU   C CD  
4917  O  OE1 . GLU   C  144 ? 2.2781 1.2053 1.6218 -0.1146 -0.1376 0.1372  142 GLU   C OE1 
4918  O  OE2 . GLU   C  144 ? 2.2302 1.3602 1.5458 -0.1414 -0.2522 0.0977  142 GLU   C OE2 
4919  N  N   . PRO   C  145 ? 1.9217 0.9914 1.4527 -0.1147 -0.3217 0.0331  143 PRO   C N   
4920  C  CA  . PRO   C  145 ? 1.8782 0.8548 1.4432 -0.0848 -0.2889 0.0291  143 PRO   C CA  
4921  C  C   . PRO   C  145 ? 1.8006 0.7815 1.4274 -0.0627 -0.3266 0.0416  143 PRO   C C   
4922  O  O   . PRO   C  145 ? 1.8112 0.7710 1.5105 -0.0418 -0.3068 0.0108  143 PRO   C O   
4923  C  CB  . PRO   C  145 ? 1.8703 0.8418 1.4644 -0.1059 -0.3065 0.0164  143 PRO   C CB  
4924  C  CG  . PRO   C  145 ? 1.9134 0.8834 1.4726 -0.1137 -0.3194 0.0331  143 PRO   C CG  
4925  C  CD  . PRO   C  145 ? 1.9149 0.9435 1.4962 -0.1337 -0.3273 0.0441  143 PRO   C CD  
4926  N  N   . LYS   C  146 ? 1.7830 0.7498 1.3938 -0.0354 -0.3002 0.0956  144 LYS   C N   
4927  C  CA  . LYS   C  146 ? 1.7588 0.7207 1.3568 -0.0439 -0.3269 0.1321  144 LYS   C CA  
4928  C  C   . LYS   C  146 ? 1.7755 0.6482 1.3413 -0.0178 -0.2827 0.0914  144 LYS   C C   
4929  O  O   . LYS   C  146 ? 1.7659 0.5713 1.3556 -0.0433 -0.2735 0.0340  144 LYS   C O   
4930  C  CB  . LYS   C  146 ? 1.7497 0.7827 1.3694 -0.0594 -0.3306 0.1843  144 LYS   C CB  
4931  C  CG  . LYS   C  146 ? 1.7364 0.8204 1.3651 -0.0889 -0.3710 0.2317  144 LYS   C CG  
4932  C  CD  . LYS   C  146 ? 1.7191 0.8646 1.3995 -0.1227 -0.3897 0.3047  144 LYS   C CD  
4933  C  CE  . LYS   C  146 ? 1.7910 0.8500 1.4268 -0.1734 -0.3931 0.3498  144 LYS   C CE  
4934  N  NZ  . LYS   C  146 ? 1.8127 0.8711 1.4665 -0.1618 -0.3742 0.3860  144 LYS   C NZ  
4935  N  N   . LEU   C  147 ? 1.7847 0.6295 1.3021 -0.0539 -0.2958 0.0745  145 LEU   C N   
4936  C  CA  . LEU   C  147 ? 1.7893 0.5812 1.2714 -0.0365 -0.2714 0.0746  145 LEU   C CA  
4937  C  C   . LEU   C  147 ? 1.7734 0.5053 1.2225 -0.0488 -0.3061 0.0849  145 LEU   C C   
4938  O  O   . LEU   C  147 ? 1.7934 0.4862 1.1731 -0.0218 -0.3244 0.1082  145 LEU   C O   
4939  C  CB  . LEU   C  147 ? 1.8205 0.5395 1.2678 -0.0294 -0.2803 0.0429  145 LEU   C CB  
4940  C  CG  . LEU   C  147 ? 1.8522 0.5327 1.2823 0.0037  -0.2738 -0.0047 145 LEU   C CG  
4941  C  CD1 . LEU   C  147 ? 1.8539 0.4762 1.2812 0.0240  -0.2573 -0.0334 145 LEU   C CD1 
4942  C  CD2 . LEU   C  147 ? 1.8870 0.5300 1.3050 -0.0181 -0.2841 0.0021  145 LEU   C CD2 
4943  N  N   . TYR   C  148 ? 1.7743 0.4532 1.2167 -0.0564 -0.2975 0.1042  146 TYR   C N   
4944  C  CA  . TYR   C  148 ? 1.7806 0.4541 1.2145 -0.0328 -0.2895 0.1420  146 TYR   C CA  
4945  C  C   . TYR   C  148 ? 1.7679 0.4266 1.1955 -0.0107 -0.2959 0.1644  146 TYR   C C   
4946  O  O   . TYR   C  148 ? 1.7638 0.3593 1.1920 0.0386  -0.2914 0.2271  146 TYR   C O   
4947  C  CB  . TYR   C  148 ? 1.7593 0.4441 1.2048 -0.0724 -0.3009 0.1165  146 TYR   C CB  
4948  C  CG  . TYR   C  148 ? 1.8010 0.4325 1.2207 -0.1038 -0.3051 0.1088  146 TYR   C CG  
4949  C  CD1 . TYR   C  148 ? 1.8066 0.3811 1.2333 -0.1445 -0.3019 0.1217  146 TYR   C CD1 
4950  C  CD2 . TYR   C  148 ? 1.7926 0.3969 1.2279 -0.1373 -0.3060 0.1097  146 TYR   C CD2 
4951  C  CE1 . TYR   C  148 ? 1.8509 0.3282 1.2347 -0.1741 -0.2990 0.1297  146 TYR   C CE1 
4952  C  CE2 . TYR   C  148 ? 1.8296 0.3405 1.2249 -0.1666 -0.3011 0.1380  146 TYR   C CE2 
4953  C  CZ  . TYR   C  148 ? 1.8340 0.3181 1.2335 -0.1947 -0.3109 0.1389  146 TYR   C CZ  
4954  O  OH  . TYR   C  148 ? 1.8921 0.3397 1.2534 -0.2328 -0.3343 0.1130  146 TYR   C OH  
4955  N  N   . GLN   C  149 ? 1.8122 0.4737 1.1843 0.0042  -0.2949 0.1511  147 GLN   C N   
4956  C  CA  . GLN   C  149 ? 1.8031 0.5598 1.2069 -0.0057 -0.3033 0.1120  147 GLN   C CA  
4957  C  C   . GLN   C  149 ? 1.8130 0.4619 1.1993 0.0302  -0.3294 0.1303  147 GLN   C C   
4958  O  O   . GLN   C  149 ? 1.8066 0.3781 1.2220 0.0652  -0.3430 0.1414  147 GLN   C O   
4959  C  CB  . GLN   C  149 ? 1.8192 0.5732 1.2217 0.0139  -0.3106 0.1023  147 GLN   C CB  
4960  C  CG  . GLN   C  149 ? 1.8238 0.6889 1.2057 0.0091  -0.3215 0.0438  147 GLN   C CG  
4961  C  CD  . GLN   C  149 ? 1.8261 0.7256 1.1813 0.0517  -0.3419 0.0511  147 GLN   C CD  
4962  O  OE1 . GLN   C  149 ? 1.8840 0.9884 1.1848 0.0662  -0.2900 -0.0398 147 GLN   C OE1 
4963  N  NE2 . GLN   C  149 ? 1.8803 0.6620 1.1111 0.0345  -0.3553 0.0781  147 GLN   C NE2 
4964  N  N   . THR   C  150 ? 1.7813 0.4844 1.2143 -0.0072 -0.3226 0.1028  148 THR   C N   
4965  C  CA  . THR   C  150 ? 1.8120 0.5502 1.2292 -0.0261 -0.2899 0.1222  148 THR   C CA  
4966  C  C   . THR   C  150 ? 1.8508 0.6072 1.2286 -0.0553 -0.2777 0.0953  148 THR   C C   
4967  O  O   . THR   C  150 ? 1.8993 0.5723 1.3097 -0.0391 -0.2613 0.1528  148 THR   C O   
4968  C  CB  . THR   C  150 ? 1.7695 0.5232 1.1642 -0.0907 -0.2888 0.1320  148 THR   C CB  
4969  O  OG1 . THR   C  150 ? 1.7704 0.4763 1.0625 -0.1172 -0.2866 0.1438  148 THR   C OG1 
4970  C  CG2 . THR   C  150 ? 1.7942 0.5479 1.1768 -0.0919 -0.2667 0.1117  148 THR   C CG2 
4971  N  N   . GLU   C  151 ? 1.9132 0.7518 1.2296 -0.0160 -0.2556 0.1166  149 GLU   C N   
4972  C  CA  . GLU   C  151 ? 1.9487 0.7245 1.3241 -0.0341 -0.2362 0.1028  149 GLU   C CA  
4973  C  C   . GLU   C  151 ? 1.9566 0.6986 1.2999 -0.0572 -0.2574 0.0539  149 GLU   C C   
4974  O  O   . GLU   C  151 ? 1.9815 0.7797 1.3048 -0.0720 -0.2071 0.1093  149 GLU   C O   
4975  C  CB  . GLU   C  151 ? 1.9705 0.8274 1.3661 0.0202  -0.2340 0.1805  149 GLU   C CB  
4976  C  CG  . GLU   C  151 ? 1.9688 0.9317 1.4393 0.0354  -0.2297 0.1998  149 GLU   C CG  
4977  C  CD  . GLU   C  151 ? 2.0451 0.9532 1.5074 0.1053  -0.1954 0.1768  149 GLU   C CD  
4978  O  OE1 . GLU   C  151 ? 2.0800 0.6751 1.6053 0.1341  -0.2354 0.1826  149 GLU   C OE1 
4979  O  OE2 . GLU   C  151 ? 2.2099 1.1349 1.4896 0.1633  -0.1092 0.1625  149 GLU   C OE2 
4980  N  N   . PRO   C  152 ? 1.9543 0.6341 1.2936 -0.0720 -0.2211 0.0421  150 PRO   C N   
4981  C  CA  . PRO   C  152 ? 1.9127 0.5953 1.2835 -0.0953 -0.2203 0.0144  150 PRO   C CA  
4982  C  C   . PRO   C  152 ? 1.8764 0.5377 1.3172 -0.0914 -0.2306 -0.0127 150 PRO   C C   
4983  O  O   . PRO   C  152 ? 1.9749 0.3877 1.2970 -0.2075 -0.1278 -0.0749 150 PRO   C O   
4984  C  CB  . PRO   C  152 ? 1.9381 0.5879 1.3283 -0.1095 -0.2173 0.0203  150 PRO   C CB  
4985  C  CG  . PRO   C  152 ? 1.9582 0.6285 1.3023 -0.1099 -0.2229 0.0255  150 PRO   C CG  
4986  C  CD  . PRO   C  152 ? 1.9571 0.6505 1.2941 -0.0987 -0.2299 0.0281  150 PRO   C CD  
4987  N  N   . SER   C  153 ? 1.8579 0.5568 1.2810 -0.0931 -0.2492 0.0202  151 SER   C N   
4988  C  CA  . SER   C  153 ? 1.7975 0.5971 1.2539 -0.0504 -0.2929 0.0455  151 SER   C CA  
4989  C  C   . SER   C  153 ? 1.7373 0.5986 1.2205 -0.0615 -0.3010 0.0912  151 SER   C C   
4990  O  O   . SER   C  153 ? 1.7168 0.6549 1.1957 -0.0330 -0.3126 0.1163  151 SER   C O   
4991  C  CB  . SER   C  153 ? 1.8185 0.6488 1.2113 -0.0366 -0.3096 0.0459  151 SER   C CB  
4992  O  OG  . SER   C  153 ? 1.8616 0.6222 1.2338 -0.0573 -0.3272 -0.0008 151 SER   C OG  
4993  N  N   . GLY   C  154 ? 1.7168 0.5848 1.2198 -0.0365 -0.3252 0.0930  152 GLY   C N   
4994  C  CA  . GLY   C  154 ? 1.7068 0.5387 1.2280 0.0106  -0.3406 0.1286  152 GLY   C CA  
4995  C  C   . GLY   C  154 ? 1.7002 0.5745 1.2561 0.0470  -0.3607 0.1615  152 GLY   C C   
4996  O  O   . GLY   C  154 ? 1.6417 0.6106 1.1471 0.1080  -0.4339 0.1341  152 GLY   C O   
4997  N  N   . ILE   C  155 ? 1.7292 0.5404 1.2897 0.0060  -0.3597 0.1735  153 ILE   C N   
4998  C  CA  . ILE   C  155 ? 1.7660 0.5338 1.2679 -0.0284 -0.3536 0.1868  153 ILE   C CA  
4999  C  C   . ILE   C  155 ? 1.7596 0.4501 1.2784 -0.0600 -0.3404 0.1633  153 ILE   C C   
5000  O  O   . ILE   C  155 ? 1.7852 0.3573 1.2325 -0.1002 -0.3169 0.1331  153 ILE   C O   
5001  C  CB  . ILE   C  155 ? 1.8061 0.5784 1.3483 0.0119  -0.3811 0.2525  153 ILE   C CB  
5002  C  CG1 . ILE   C  155 ? 1.8242 0.6966 1.4586 -0.0611 -0.3771 0.2531  153 ILE   C CG1 
5003  C  CG2 . ILE   C  155 ? 1.7600 0.5216 1.3659 -0.0024 -0.3757 0.2947  153 ILE   C CG2 
5004  C  CD1 . ILE   C  155 ? 1.8477 0.7954 1.5418 0.0185  -0.3931 0.2610  153 ILE   C CD1 
5005  N  N   . TYR   C  156 ? 1.7922 0.4635 1.2259 -0.0149 -0.3281 0.1450  154 TYR   C N   
5006  C  CA  . TYR   C  156 ? 1.7873 0.5297 1.1964 -0.0432 -0.3548 0.1426  154 TYR   C CA  
5007  C  C   . TYR   C  156 ? 1.7616 0.4773 1.2528 -0.0076 -0.3628 0.1525  154 TYR   C C   
5008  O  O   . TYR   C  156 ? 1.7258 0.5342 1.2897 0.0471  -0.3834 0.1141  154 TYR   C O   
5009  C  CB  . TYR   C  156 ? 1.7709 0.5396 1.1586 -0.0467 -0.3593 0.1418  154 TYR   C CB  
5010  C  CG  . TYR   C  156 ? 1.8086 0.5872 1.1409 -0.0939 -0.3498 0.1488  154 TYR   C CG  
5011  C  CD1 . TYR   C  156 ? 1.7851 0.6181 1.1787 -0.1335 -0.3199 0.1265  154 TYR   C CD1 
5012  C  CD2 . TYR   C  156 ? 1.8209 0.5558 1.1635 -0.1532 -0.3471 0.1538  154 TYR   C CD2 
5013  C  CE1 . TYR   C  156 ? 1.7793 0.6570 1.2118 -0.1575 -0.3325 0.0733  154 TYR   C CE1 
5014  C  CE2 . TYR   C  156 ? 1.7965 0.6361 1.1704 -0.1902 -0.3664 0.1272  154 TYR   C CE2 
5015  C  CZ  . TYR   C  156 ? 1.7535 0.6804 1.1904 -0.1934 -0.3461 0.1003  154 TYR   C CZ  
5016  O  OH  . TYR   C  156 ? 1.7257 0.7712 1.3280 -0.2297 -0.3307 0.1643  154 TYR   C OH  
5017  N  N   . SER   C  157 ? 1.7913 0.4526 1.2822 -0.0134 -0.3418 0.1899  155 SER   C N   
5018  C  CA  . SER   C  157 ? 1.8380 0.5179 1.2708 0.0062  -0.3396 0.2284  155 SER   C CA  
5019  C  C   . SER   C  157 ? 1.8673 0.5596 1.2768 0.0105  -0.3257 0.2305  155 SER   C C   
5020  O  O   . SER   C  157 ? 1.8611 0.5520 1.2972 -0.0175 -0.3209 0.2205  155 SER   C O   
5021  C  CB  . SER   C  157 ? 1.8498 0.5293 1.2949 0.0250  -0.3512 0.2462  155 SER   C CB  
5022  O  OG  . SER   C  157 ? 1.8113 0.5936 1.3289 0.0138  -0.3750 0.2547  155 SER   C OG  
5023  N  N   . SER   C  158 ? 1.9368 0.5984 1.2452 0.0146  -0.3319 0.2340  156 SER   C N   
5024  C  CA  . SER   C  158 ? 1.9707 0.6406 1.2387 -0.0051 -0.3394 0.2048  156 SER   C CA  
5025  C  C   . SER   C  158 ? 1.9412 0.5901 1.2579 0.0061  -0.3338 0.1621  156 SER   C C   
5026  O  O   . SER   C  158 ? 1.9658 0.5779 1.3303 0.0271  -0.3599 0.1828  156 SER   C O   
5027  C  CB  . SER   C  158 ? 1.9935 0.6622 1.2249 -0.0532 -0.3340 0.2384  156 SER   C CB  
5028  O  OG  . SER   C  158 ? 2.0671 0.7403 1.2093 -0.0665 -0.3020 0.2817  156 SER   C OG  
5029  N  N   . TRP   C  159 ? 1.9146 0.6078 1.2473 -0.0210 -0.3436 0.0974  157 TRP   C N   
5030  C  CA  . TRP   C  159 ? 1.9006 0.6433 1.2796 -0.0341 -0.3441 0.1275  157 TRP   C CA  
5031  C  C   . TRP   C  159 ? 1.9185 0.6260 1.2806 -0.0735 -0.3511 0.1153  157 TRP   C C   
5032  O  O   . TRP   C  159 ? 1.9099 0.6944 1.3824 -0.0481 -0.3187 0.0909  157 TRP   C O   
5033  C  CB  . TRP   C  159 ? 1.8566 0.7484 1.2799 -0.0187 -0.3651 0.1246  157 TRP   C CB  
5034  C  CG  . TRP   C  159 ? 1.8599 0.7885 1.2702 -0.0007 -0.3912 0.1152  157 TRP   C CG  
5035  C  CD1 . TRP   C  159 ? 1.8569 0.7985 1.2461 0.0105  -0.3916 0.0991  157 TRP   C CD1 
5036  C  CD2 . TRP   C  159 ? 1.8692 0.7939 1.2752 0.0045  -0.4156 0.1015  157 TRP   C CD2 
5037  N  NE1 . TRP   C  159 ? 1.8788 0.7911 1.2656 0.0128  -0.3873 0.0915  157 TRP   C NE1 
5038  C  CE2 . TRP   C  159 ? 1.8802 0.8038 1.2786 0.0100  -0.4073 0.1117  157 TRP   C CE2 
5039  C  CE3 . TRP   C  159 ? 1.8729 0.8119 1.3148 0.0102  -0.4277 0.1237  157 TRP   C CE3 
5040  C  CZ2 . TRP   C  159 ? 1.8806 0.7932 1.3166 0.0323  -0.4099 0.1227  157 TRP   C CZ2 
5041  C  CZ3 . TRP   C  159 ? 1.8802 0.8079 1.3321 0.0229  -0.4286 0.1309  157 TRP   C CZ3 
5042  C  CH2 . TRP   C  159 ? 1.8921 0.8124 1.3309 0.0344  -0.4248 0.1407  157 TRP   C CH2 
5043  N  N   . SER   C  160 ? 1.9278 0.6234 1.2781 -0.1315 -0.3541 0.1525  158 SER   C N   
5044  C  CA  . SER   C  160 ? 1.9829 0.6323 1.2746 -0.1680 -0.3527 0.1994  158 SER   C CA  
5045  C  C   . SER   C  160 ? 1.9887 0.5887 1.2360 -0.1598 -0.3631 0.2579  158 SER   C C   
5046  O  O   . SER   C  160 ? 2.0302 0.3724 1.1737 -0.2290 -0.3956 0.2164  158 SER   C O   
5047  C  CB  . SER   C  160 ? 1.9855 0.6796 1.3043 -0.1672 -0.3545 0.2207  158 SER   C CB  
5048  O  OG  . SER   C  160 ? 2.0193 0.7536 1.3648 -0.2009 -0.2997 0.2138  158 SER   C OG  
5049  N  N   . ALA   C  161 ? 2.0318 0.5855 1.1920 -0.1113 -0.3986 0.2751  159 ALA   C N   
5050  C  CA  . ALA   C  161 ? 1.9877 0.6396 1.2145 -0.0740 -0.3832 0.3327  159 ALA   C CA  
5051  C  C   . ALA   C  161 ? 1.9753 0.5867 1.2383 -0.0122 -0.3722 0.3264  159 ALA   C C   
5052  O  O   . ALA   C  161 ? 1.9998 0.5347 1.2352 -0.0023 -0.3674 0.3411  159 ALA   C O   
5053  C  CB  . ALA   C  161 ? 2.0190 0.6905 1.1955 -0.0961 -0.3807 0.3372  159 ALA   C CB  
5054  N  N   . GLN   C  162 ? 1.9502 0.6137 1.2503 0.0471  -0.3524 0.3168  160 GLN   C N   
5055  C  CA  . GLN   C  162 ? 1.9247 0.6387 1.2680 0.0969  -0.3423 0.2890  160 GLN   C CA  
5056  C  C   . GLN   C  162 ? 1.9103 0.5597 1.3017 0.0933  -0.3128 0.3060  160 GLN   C C   
5057  O  O   . GLN   C  162 ? 1.8814 0.5943 1.2467 0.0617  -0.3144 0.2882  160 GLN   C O   
5058  C  CB  . GLN   C  162 ? 1.9178 0.7076 1.2578 0.1099  -0.3095 0.2839  160 GLN   C CB  
5059  C  CG  . GLN   C  162 ? 1.9369 0.7452 1.2778 0.1368  -0.2911 0.2394  160 GLN   C CG  
5060  C  CD  . GLN   C  162 ? 1.9752 0.7208 1.2863 0.1504  -0.3000 0.2638  160 GLN   C CD  
5061  O  OE1 . GLN   C  162 ? 2.0399 0.8240 1.3135 0.1316  -0.2659 0.1865  160 GLN   C OE1 
5062  N  NE2 . GLN   C  162 ? 1.9984 0.7492 1.3123 0.1343  -0.2949 0.2976  160 GLN   C NE2 
5063  N  N   . THR   C  163 ? 1.9016 0.4973 1.3785 0.0973  -0.3140 0.3118  161 THR   C N   
5064  C  CA  . THR   C  163 ? 1.8730 0.5759 1.4497 0.1240  -0.3100 0.3222  161 THR   C CA  
5065  C  C   . THR   C  163 ? 1.8608 0.5541 1.4582 0.1559  -0.2748 0.3210  161 THR   C C   
5066  O  O   . THR   C  163 ? 1.8993 0.5581 1.5369 0.1712  -0.2198 0.2701  161 THR   C O   
5067  C  CB  . THR   C  163 ? 1.9049 0.6051 1.4727 0.1259  -0.3143 0.3584  161 THR   C CB  
5068  O  OG1 . THR   C  163 ? 1.8662 0.5293 1.5186 0.1440  -0.2982 0.3633  161 THR   C OG1 
5069  C  CG2 . THR   C  163 ? 1.9185 0.6161 1.5038 0.1372  -0.3336 0.3477  161 THR   C CG2 
5070  N  N   . ILE   C  164 ? 1.8808 0.5517 1.4596 0.1467  -0.2940 0.3333  162 ILE   C N   
5071  C  CA  . ILE   C  164 ? 1.8696 0.5186 1.4597 0.1260  -0.3066 0.3227  162 ILE   C CA  
5072  C  C   . ILE   C  164 ? 1.9141 0.4466 1.4584 0.0901  -0.3108 0.2991  162 ILE   C C   
5073  O  O   . ILE   C  164 ? 1.9050 0.3872 1.4564 0.0439  -0.3113 0.2996  162 ILE   C O   
5074  C  CB  . ILE   C  164 ? 1.8715 0.5569 1.4007 0.1108  -0.2857 0.3315  162 ILE   C CB  
5075  C  CG1 . ILE   C  164 ? 1.9010 0.5855 1.4284 0.1059  -0.2776 0.2821  162 ILE   C CG1 
5076  C  CG2 . ILE   C  164 ? 1.8554 0.5706 1.3691 0.1291  -0.2968 0.3536  162 ILE   C CG2 
5077  C  CD1 . ILE   C  164 ? 1.8982 0.5677 1.4361 0.1294  -0.2702 0.2664  162 ILE   C CD1 
5078  N  N   . GLY   C  165 ? 1.9015 0.4324 1.4771 0.0769  -0.3048 0.2845  163 GLY   C N   
5079  C  CA  . GLY   C  165 ? 1.8950 0.5970 1.4932 0.0506  -0.2880 0.2294  163 GLY   C CA  
5080  C  C   . GLY   C  165 ? 1.8859 0.5975 1.5353 0.0475  -0.2647 0.1967  163 GLY   C C   
5081  O  O   . GLY   C  165 ? 1.8816 0.7465 1.5804 0.0832  -0.2708 0.1668  163 GLY   C O   
5082  N  N   . ARG   C  166 ? 1.9348 0.6553 1.5432 -0.0130 -0.2421 0.1840  164 ARG   C N   
5083  C  CA  . ARG   C  166 ? 2.0073 0.6542 1.5545 -0.0266 -0.2482 0.1932  164 ARG   C CA  
5084  C  C   . ARG   C  166 ? 2.0412 0.6192 1.5185 -0.0704 -0.2537 0.1579  164 ARG   C C   
5085  O  O   . ARG   C  166 ? 2.0434 0.5426 1.4574 -0.0240 -0.3317 0.1902  164 ARG   C O   
5086  C  CB  . ARG   C  166 ? 2.0296 0.6819 1.6143 -0.0597 -0.2480 0.1900  164 ARG   C CB  
5087  C  CG  . ARG   C  166 ? 2.0688 0.7180 1.6595 -0.0400 -0.2214 0.1754  164 ARG   C CG  
5088  C  CD  . ARG   C  166 ? 2.0987 0.7983 1.6762 -0.0475 -0.2509 0.1693  164 ARG   C CD  
5089  N  NE  . ARG   C  166 ? 2.1808 0.9424 1.6770 -0.0515 -0.2093 0.1538  164 ARG   C NE  
5090  C  CZ  . ARG   C  166 ? 2.2058 1.1148 1.6447 -0.0505 -0.2312 0.1427  164 ARG   C CZ  
5091  N  NH1 . ARG   C  166 ? 2.2704 1.2108 1.6554 -0.0346 -0.1867 0.1716  164 ARG   C NH1 
5092  N  NH2 . ARG   C  166 ? 2.2879 1.1798 1.6538 -0.0508 -0.2629 0.1354  164 ARG   C NH2 
5093  N  N   . ASN   C  167 ? 2.0779 0.5861 1.5179 -0.0889 -0.2402 0.1758  165 ASN   C N   
5094  C  CA  . ASN   C  167 ? 2.1461 0.6297 1.4794 -0.1433 -0.2340 0.1845  165 ASN   C CA  
5095  C  C   . ASN   C  167 ? 2.1449 0.6385 1.4822 -0.1587 -0.2123 0.1754  165 ASN   C C   
5096  O  O   . ASN   C  167 ? 2.1834 0.5713 1.5198 -0.1634 -0.2255 0.2549  165 ASN   C O   
5097  C  CB  . ASN   C  167 ? 2.1654 0.6464 1.4878 -0.1889 -0.2345 0.1649  165 ASN   C CB  
5098  C  CG  . ASN   C  167 ? 2.1900 0.6461 1.5097 -0.2223 -0.2203 0.1687  165 ASN   C CG  
5099  O  OD1 . ASN   C  167 ? 2.1811 0.5132 1.4930 -0.2407 -0.2077 0.1894  165 ASN   C OD1 
5100  N  ND2 . ASN   C  167 ? 2.2305 0.6455 1.5148 -0.2358 -0.2313 0.1255  165 ASN   C ND2 
5101  N  N   . SER   C  168 ? 2.0911 0.7154 1.4434 -0.1894 -0.1697 0.1550  166 SER   C N   
5102  C  CA  . SER   C  168 ? 2.0716 0.7678 1.4383 -0.1647 -0.1807 0.1066  166 SER   C CA  
5103  C  C   . SER   C  168 ? 2.0702 0.8007 1.5398 -0.1168 -0.1621 0.0618  166 SER   C C   
5104  O  O   . SER   C  168 ? 2.0850 0.9151 1.5622 -0.0965 -0.1815 0.0279  166 SER   C O   
5105  C  CB  . SER   C  168 ? 2.0573 0.7675 1.3942 -0.1567 -0.1875 0.0976  166 SER   C CB  
5106  O  OG  . SER   C  168 ? 2.0575 0.7643 1.3878 -0.1663 -0.1747 0.1206  166 SER   C OG  
5107  N  N   . LYS   C  169 ? 2.0508 0.7461 1.6320 -0.1358 -0.1810 0.0547  167 LYS   C N   
5108  C  CA  . LYS   C  169 ? 2.0756 0.6798 1.6946 -0.1200 -0.1821 0.0177  167 LYS   C CA  
5109  C  C   . LYS   C  169 ? 2.0459 0.5630 1.7178 -0.0998 -0.2272 0.0259  167 LYS   C C   
5110  O  O   . LYS   C  169 ? 2.0141 0.4040 1.7720 -0.1410 -0.2371 -0.0275 167 LYS   C O   
5111  C  CB  . LYS   C  169 ? 2.0938 0.7884 1.7252 -0.1361 -0.1528 -0.0429 167 LYS   C CB  
5112  C  CG  . LYS   C  169 ? 2.0850 0.9477 1.7709 -0.1515 -0.1311 -0.0715 167 LYS   C CG  
5113  C  CD  . LYS   C  169 ? 2.0964 1.1212 1.7963 -0.1508 -0.1035 -0.1089 167 LYS   C CD  
5114  C  CE  . LYS   C  169 ? 2.1499 1.2097 1.8120 -0.1920 -0.1007 -0.1805 167 LYS   C CE  
5115  N  NZ  . LYS   C  169 ? 2.1689 1.3208 1.8053 -0.1834 -0.0975 -0.1652 167 LYS   C NZ  
5116  N  N   . THR   C  170 ? 2.0095 0.6033 1.7612 -0.0679 -0.2548 0.0402  168 THR   C N   
5117  C  CA  . THR   C  170 ? 2.0647 0.6854 1.7549 -0.0313 -0.2934 0.0864  168 THR   C CA  
5118  C  C   . THR   C  170 ? 2.0926 0.7605 1.6740 -0.0144 -0.3287 0.0993  168 THR   C C   
5119  O  O   . THR   C  170 ? 2.1644 0.8112 1.6768 0.0217  -0.3392 0.1132  168 THR   C O   
5120  C  CB  . THR   C  170 ? 2.0721 0.6613 1.8168 -0.0409 -0.2912 0.1472  168 THR   C CB  
5121  O  OG1 . THR   C  170 ? 2.0554 0.6369 1.8780 -0.0243 -0.2813 0.1201  168 THR   C OG1 
5122  C  CG2 . THR   C  170 ? 2.0768 0.6583 1.8500 -0.0765 -0.3002 0.1842  168 THR   C CG2 
5123  N  N   . VAL   C  171 ? 2.0833 0.7702 1.5725 -0.0142 -0.3231 0.1151  169 VAL   C N   
5124  C  CA  . VAL   C  171 ? 2.0838 0.7999 1.4938 -0.0131 -0.3251 0.1392  169 VAL   C CA  
5125  C  C   . VAL   C  171 ? 2.0512 0.7747 1.3913 0.0272  -0.3463 0.1435  169 VAL   C C   
5126  O  O   . VAL   C  171 ? 2.0778 0.7921 1.4321 0.0325  -0.3789 0.1041  169 VAL   C O   
5127  C  CB  . VAL   C  171 ? 2.0956 0.8067 1.4591 -0.0084 -0.3129 0.1556  169 VAL   C CB  
5128  C  CG1 . VAL   C  171 ? 2.0863 0.8307 1.4634 -0.0020 -0.3147 0.1595  169 VAL   C CG1 
5129  C  CG2 . VAL   C  171 ? 2.0773 0.8320 1.4307 -0.0276 -0.3224 0.1449  169 VAL   C CG2 
5130  N  N   . ARG   C  172 ? 2.0161 0.7449 1.3621 0.0450  -0.3774 0.2055  170 ARG   C N   
5131  C  CA  . ARG   C  172 ? 2.0189 0.7871 1.3446 0.0314  -0.3675 0.2185  170 ARG   C CA  
5132  C  C   . ARG   C  172 ? 2.0019 0.8744 1.3798 0.0319  -0.3731 0.2613  170 ARG   C C   
5133  O  O   . ARG   C  172 ? 1.9634 0.8234 1.4004 -0.0045 -0.3459 0.2763  170 ARG   C O   
5134  C  CB  . ARG   C  172 ? 2.0380 0.8044 1.3204 0.0809  -0.3912 0.2444  170 ARG   C CB  
5135  C  CG  . ARG   C  172 ? 2.0298 0.8371 1.2795 0.0845  -0.4007 0.2534  170 ARG   C CG  
5136  C  CD  . ARG   C  172 ? 2.0532 0.8485 1.2835 0.1022  -0.3897 0.2605  170 ARG   C CD  
5137  N  NE  . ARG   C  172 ? 2.1154 0.8123 1.2546 0.1115  -0.3573 0.2946  170 ARG   C NE  
5138  C  CZ  . ARG   C  172 ? 2.1334 0.8685 1.2253 0.1240  -0.3825 0.3397  170 ARG   C CZ  
5139  N  NH1 . ARG   C  172 ? 2.1594 0.8875 1.2925 0.0921  -0.3466 0.3092  170 ARG   C NH1 
5140  N  NH2 . ARG   C  172 ? 2.1675 0.8734 1.2842 0.1624  -0.3720 0.3522  170 ARG   C NH2 
5141  N  N   . GLU   C  173 ? 2.0328 0.8916 1.4359 -0.0086 -0.3561 0.2543  171 GLU   C N   
5142  C  CA  . GLU   C  173 ? 2.0617 0.9503 1.4925 0.0126  -0.3654 0.3041  171 GLU   C CA  
5143  C  C   . GLU   C  173 ? 2.0766 0.8134 1.5030 -0.0206 -0.3430 0.3112  171 GLU   C C   
5144  O  O   . GLU   C  173 ? 2.0550 0.7455 1.5602 -0.0422 -0.3509 0.3185  171 GLU   C O   
5145  C  CB  . GLU   C  173 ? 2.0832 1.0530 1.5331 -0.0431 -0.3818 0.2352  171 GLU   C CB  
5146  C  CG  . GLU   C  173 ? 2.0999 1.2232 1.5876 0.0178  -0.4286 0.2875  171 GLU   C CG  
5147  C  CD  . GLU   C  173 ? 2.1263 1.4388 1.5541 0.0187  -0.4202 0.2522  171 GLU   C CD  
5148  O  OE1 . GLU   C  173 ? 2.1767 1.5574 1.5871 0.0399  -0.4583 0.3009  171 GLU   C OE1 
5149  O  OE2 . GLU   C  173 ? 2.1567 1.6471 1.5490 0.0361  -0.4449 0.2296  171 GLU   C OE2 
5150  N  N   . PHE   C  174 ? 2.0890 0.7502 1.5017 -0.0148 -0.3288 0.3241  172 PHE   C N   
5151  C  CA  . PHE   C  174 ? 2.1191 0.7632 1.5139 0.0020  -0.3163 0.3124  172 PHE   C CA  
5152  C  C   . PHE   C  174 ? 2.0964 0.8154 1.4721 0.0215  -0.3474 0.2668  172 PHE   C C   
5153  O  O   . PHE   C  174 ? 2.1283 0.7801 1.4098 -0.0183 -0.3003 0.2985  172 PHE   C O   
5154  C  CB  . PHE   C  174 ? 2.1289 0.7326 1.5238 0.0319  -0.2923 0.3003  172 PHE   C CB  
5155  C  CG  . PHE   C  174 ? 2.1718 0.8165 1.5316 0.0638  -0.2931 0.2736  172 PHE   C CG  
5156  C  CD1 . PHE   C  174 ? 2.1954 0.8370 1.4949 0.0564  -0.2791 0.2419  172 PHE   C CD1 
5157  C  CD2 . PHE   C  174 ? 2.2122 0.8440 1.5250 0.0848  -0.2882 0.2861  172 PHE   C CD2 
5158  C  CE1 . PHE   C  174 ? 2.2277 0.9178 1.5022 0.0442  -0.2668 0.2286  172 PHE   C CE1 
5159  C  CE2 . PHE   C  174 ? 2.2333 0.8802 1.5410 0.0868  -0.2725 0.2766  172 PHE   C CE2 
5160  C  CZ  . PHE   C  174 ? 2.2436 0.8889 1.5584 0.0669  -0.2660 0.2533  172 PHE   C CZ  
5161  N  N   . LEU   C  175 ? 2.0880 0.7633 1.4747 0.0392  -0.3735 0.2178  173 LEU   C N   
5162  C  CA  . LEU   C  175 ? 2.0942 0.8263 1.4328 0.0340  -0.3981 0.1331  173 LEU   C CA  
5163  C  C   . LEU   C  175 ? 2.0988 0.8246 1.4392 0.0339  -0.4280 0.1021  173 LEU   C C   
5164  O  O   . LEU   C  175 ? 2.1605 0.9625 1.3953 0.0540  -0.4338 0.0620  173 LEU   C O   
5165  C  CB  . LEU   C  175 ? 2.0945 0.8062 1.4061 0.0454  -0.3742 0.1127  173 LEU   C CB  
5166  C  CG  . LEU   C  175 ? 2.1053 0.7941 1.4282 0.0645  -0.3418 0.0637  173 LEU   C CG  
5167  C  CD1 . LEU   C  175 ? 2.0943 0.7889 1.4080 0.0779  -0.3382 0.0337  173 LEU   C CD1 
5168  C  CD2 . LEU   C  175 ? 2.1349 0.8227 1.3879 0.0605  -0.3369 0.0863  173 LEU   C CD2 
5169  N  N   . GLU   C  176 ? 2.1166 0.8312 1.4852 0.0344  -0.4232 0.0747  174 GLU   C N   
5170  C  CA  . GLU   C  176 ? 2.1221 0.9199 1.5794 0.0292  -0.4159 0.0723  174 GLU   C CA  
5171  C  C   . GLU   C  176 ? 2.1827 0.8946 1.5910 0.0402  -0.4064 0.0793  174 GLU   C C   
5172  O  O   . GLU   C  176 ? 2.1569 0.8351 1.6422 0.0938  -0.4003 0.0301  174 GLU   C O   
5173  C  CB  . GLU   C  176 ? 2.1237 0.9928 1.5609 0.0583  -0.4017 0.0855  174 GLU   C CB  
5174  C  CG  . GLU   C  176 ? 2.1084 1.0041 1.5996 0.0773  -0.3826 0.1128  174 GLU   C CG  
5175  C  CD  . GLU   C  176 ? 2.1111 1.0500 1.6369 0.1008  -0.3388 0.1116  174 GLU   C CD  
5176  O  OE1 . GLU   C  176 ? 2.1372 1.0911 1.6922 0.1441  -0.3712 0.1481  174 GLU   C OE1 
5177  O  OE2 . GLU   C  176 ? 2.1051 0.9676 1.6944 0.0770  -0.2639 0.1501  174 GLU   C OE2 
5178  N  N   . LYS   C  177 ? 2.2425 0.9316 1.6107 0.0165  -0.3851 0.0955  175 LYS   C N   
5179  C  CA  . LYS   C  177 ? 2.3065 1.0667 1.5808 -0.0048 -0.3882 0.1068  175 LYS   C CA  
5180  C  C   . LYS   C  177 ? 2.3085 0.9550 1.5810 -0.0169 -0.3851 0.1308  175 LYS   C C   
5181  O  O   . LYS   C  177 ? 2.3768 0.9459 1.5481 0.0367  -0.3459 0.1351  175 LYS   C O   
5182  C  CB  . LYS   C  177 ? 2.3805 1.1166 1.6762 -0.1002 -0.3671 0.0985  175 LYS   C CB  
5183  C  CG  . LYS   C  177 ? 2.3774 1.2639 1.7409 -0.0999 -0.3528 0.0269  175 LYS   C CG  
5184  C  CD  . LYS   C  177 ? 2.4611 1.2745 1.7800 -0.1444 -0.3241 0.0018  175 LYS   C CD  
5185  C  CE  . LYS   C  177 ? 2.4872 1.3138 1.8629 -0.1264 -0.3193 -0.0499 175 LYS   C CE  
5186  N  NZ  . LYS   C  177 ? 2.4642 1.3578 1.9294 -0.1616 -0.3174 -0.1145 175 LYS   C NZ  
5187  N  N   . ASN   C  178 ? 2.2489 0.9442 1.5004 -0.0641 -0.3660 0.1476  176 ASN   C N   
5188  C  CA  . ASN   C  178 ? 2.2687 1.0250 1.4122 -0.1213 -0.3444 0.1785  176 ASN   C CA  
5189  C  C   . ASN   C  178 ? 2.2147 1.0275 1.2792 -0.1090 -0.3480 0.1614  176 ASN   C C   
5190  O  O   . ASN   C  178 ? 2.2030 1.0893 1.1874 -0.1606 -0.3793 0.1554  176 ASN   C O   
5191  C  CB  . ASN   C  178 ? 2.2882 0.9579 1.4413 -0.1901 -0.3312 0.1711  176 ASN   C CB  
5192  C  CG  . ASN   C  178 ? 2.3768 0.9671 1.4681 -0.2180 -0.3364 0.1835  176 ASN   C CG  
5193  O  OD1 . ASN   C  178 ? 2.4282 0.8894 1.4532 -0.2727 -0.3648 0.2257  176 ASN   C OD1 
5194  N  ND2 . ASN   C  178 ? 2.4012 0.9654 1.5067 -0.2018 -0.3108 0.1709  176 ASN   C ND2 
5195  N  N   . TYR   C  179 ? 2.1713 0.9720 1.3351 -0.1161 -0.3880 0.2029  177 TYR   C N   
5196  C  CA  . TYR   C  179 ? 2.1630 0.9538 1.3607 -0.0919 -0.4143 0.1982  177 TYR   C CA  
5197  C  C   . TYR   C  179 ? 2.1753 0.9049 1.3553 -0.0736 -0.4361 0.2664  177 TYR   C C   
5198  O  O   . TYR   C  179 ? 2.1671 0.8341 1.4085 -0.0160 -0.4446 0.3085  177 TYR   C O   
5199  C  CB  . TYR   C  179 ? 2.1020 0.9055 1.3785 -0.1063 -0.4387 0.1863  177 TYR   C CB  
5200  C  CG  . TYR   C  179 ? 2.0581 0.9140 1.3665 -0.0984 -0.4758 0.1391  177 TYR   C CG  
5201  C  CD1 . TYR   C  179 ? 2.0509 0.8983 1.3627 -0.0964 -0.5199 0.1206  177 TYR   C CD1 
5202  C  CD2 . TYR   C  179 ? 2.0309 0.9278 1.2955 -0.1138 -0.4856 0.1169  177 TYR   C CD2 
5203  C  CE1 . TYR   C  179 ? 1.9995 0.9028 1.2894 -0.1402 -0.5436 0.1153  177 TYR   C CE1 
5204  C  CE2 . TYR   C  179 ? 1.9853 0.9312 1.2490 -0.1450 -0.5058 0.1011  177 TYR   C CE2 
5205  C  CZ  . TYR   C  179 ? 2.0213 0.7916 1.2480 -0.1649 -0.5391 0.0960  177 TYR   C CZ  
5206  O  OH  . TYR   C  179 ? 1.9581 0.7927 1.2196 -0.1636 -0.5646 0.0519  177 TYR   C OH  
5207  N  N   . ASP   C  180 ? 2.2513 0.9092 1.3387 -0.0780 -0.3994 0.2648  178 ASP   C N   
5208  C  CA  . ASP   C  180 ? 2.2619 1.0531 1.4516 -0.0690 -0.4261 0.2042  178 ASP   C CA  
5209  C  C   . ASP   C  180 ? 2.2952 1.1254 1.4110 -0.1140 -0.4093 0.2496  178 ASP   C C   
5210  O  O   . ASP   C  180 ? 2.2936 1.3095 1.4244 -0.0249 -0.3842 0.2164  178 ASP   C O   
5211  C  CB  . ASP   C  180 ? 2.3230 1.0307 1.4533 -0.0839 -0.4013 0.1635  178 ASP   C CB  
5212  C  CG  . ASP   C  180 ? 2.3255 1.0667 1.5769 -0.0533 -0.4226 0.1197  178 ASP   C CG  
5213  O  OD1 . ASP   C  180 ? 2.3508 1.0220 1.6535 -0.0584 -0.3923 0.0588  178 ASP   C OD1 
5214  O  OD2 . ASP   C  180 ? 2.3822 1.1882 1.5652 0.0247  -0.4501 0.1312  178 ASP   C OD2 
5215  N  N   . ARG   C  181 ? 2.2857 1.3053 1.4587 -0.1017 -0.3918 0.2167  179 ARG   C N   
5216  C  CA  . ARG   C  181 ? 2.2926 1.3299 1.4797 -0.1431 -0.3751 0.1901  179 ARG   C CA  
5217  C  C   . ARG   C  181 ? 2.2938 1.3801 1.5093 -0.1712 -0.3992 0.1738  179 ARG   C C   
5218  O  O   . ARG   C  181 ? 2.2700 1.3767 1.3781 -0.1832 -0.4711 0.1123  179 ARG   C O   
5219  C  CB  . ARG   C  181 ? 2.2960 1.3700 1.5095 -0.1119 -0.3637 0.2010  179 ARG   C CB  
5220  C  CG  . ARG   C  181 ? 2.2907 1.2992 1.4862 -0.1077 -0.3423 0.2188  179 ARG   C CG  
5221  C  CD  . ARG   C  181 ? 2.2599 1.2788 1.4348 -0.0682 -0.3564 0.2080  179 ARG   C CD  
5222  N  NE  . ARG   C  181 ? 2.2581 1.1896 1.4235 -0.0377 -0.3435 0.2584  179 ARG   C NE  
5223  C  CZ  . ARG   C  181 ? 2.2700 1.1532 1.5085 -0.0360 -0.3085 0.2606  179 ARG   C CZ  
5224  N  NH1 . ARG   C  181 ? 2.2631 1.2101 1.5266 -0.0517 -0.3520 0.2084  179 ARG   C NH1 
5225  N  NH2 . ARG   C  181 ? 2.3194 1.1202 1.5637 -0.0064 -0.2604 0.2216  179 ARG   C NH2 
5226  N  N   . LYS   C  182 ? 2.2722 1.4010 1.5843 -0.1647 -0.4174 0.2007  180 LYS   C N   
5227  C  CA  . LYS   C  182 ? 2.2796 1.4491 1.6547 -0.1999 -0.4226 0.1449  180 LYS   C CA  
5228  C  C   . LYS   C  182 ? 2.2801 1.4102 1.6442 -0.2269 -0.4087 0.1475  180 LYS   C C   
5229  O  O   . LYS   C  182 ? 2.1760 1.4349 1.5745 -0.2088 -0.4402 0.1627  180 LYS   C O   
5230  C  CB  . LYS   C  182 ? 2.3437 1.4820 1.7536 -0.1618 -0.4407 0.1644  180 LYS   C CB  
5231  C  CG  . LYS   C  182 ? 2.3411 1.5473 1.8386 -0.1362 -0.4544 0.1655  180 LYS   C CG  
5232  C  CD  . LYS   C  182 ? 2.3516 1.4967 1.8619 -0.1035 -0.4414 0.1759  180 LYS   C CD  
5233  C  CE  . LYS   C  182 ? 2.3638 1.5054 1.9573 -0.0796 -0.4691 0.2199  180 LYS   C CE  
5234  N  NZ  . LYS   C  182 ? 2.3828 1.4352 2.0139 -0.0581 -0.4428 0.2571  180 LYS   C NZ  
5235  N  N   . GLU   C  183 ? 2.2682 1.3911 1.6614 -0.2168 -0.3284 0.1518  181 GLU   C N   
5236  C  CA  . GLU   C  183 ? 2.3001 1.3986 1.6381 -0.1864 -0.3359 0.1248  181 GLU   C CA  
5237  C  C   . GLU   C  183 ? 2.2710 1.2542 1.5676 -0.1487 -0.3110 0.1288  181 GLU   C C   
5238  O  O   . GLU   C  183 ? 2.1215 1.2348 1.4455 -0.0863 -0.4000 0.1672  181 GLU   C O   
5239  C  CB  . GLU   C  183 ? 2.4092 1.5150 1.6530 -0.2198 -0.2758 0.1523  181 GLU   C CB  
5240  C  CG  . GLU   C  183 ? 2.4039 1.6190 1.7511 -0.2568 -0.2186 0.1209  181 GLU   C CG  
5241  C  CD  . GLU   C  183 ? 2.4092 1.7553 1.7641 -0.3478 -0.2011 0.1584  181 GLU   C CD  
5242  O  OE1 . GLU   C  183 ? 2.4158 1.7750 1.9232 -0.4183 -0.1800 0.1110  181 GLU   C OE1 
5243  O  OE2 . GLU   C  183 ? 2.4213 2.0158 1.9495 -0.3638 -0.2561 0.0974  181 GLU   C OE2 
5244  N  N   . PRO   C  184 ? 2.2245 1.2291 1.5866 -0.1524 -0.2979 0.1194  182 PRO   C N   
5245  C  CA  . PRO   C  184 ? 2.1603 1.1922 1.6389 -0.1716 -0.2399 0.1046  182 PRO   C CA  
5246  C  C   . PRO   C  184 ? 2.2208 1.1335 1.5885 -0.2095 -0.2114 0.1358  182 PRO   C C   
5247  O  O   . PRO   C  184 ? 2.2462 1.2788 1.5097 -0.2295 -0.2062 0.1840  182 PRO   C O   
5248  C  CB  . PRO   C  184 ? 2.1500 1.2143 1.6382 -0.1548 -0.2473 0.1164  182 PRO   C CB  
5249  C  CG  . PRO   C  184 ? 2.1815 1.2749 1.6404 -0.1621 -0.2771 0.0835  182 PRO   C CG  
5250  C  CD  . PRO   C  184 ? 2.1960 1.2796 1.6217 -0.1810 -0.3046 0.1006  182 PRO   C CD  
5251  N  N   . PRO   C  185 ? 2.2044 0.9616 1.5911 -0.2041 -0.1593 0.1512  183 PRO   C N   
5252  C  CA  . PRO   C  185 ? 2.2217 1.0272 1.5685 -0.2069 -0.1441 0.1819  183 PRO   C CA  
5253  C  C   . PRO   C  185 ? 2.2220 1.1252 1.5089 -0.2290 -0.1178 0.1060  183 PRO   C C   
5254  O  O   . PRO   C  185 ? 2.2352 1.2339 1.4241 -0.2286 -0.1178 0.1426  183 PRO   C O   
5255  C  CB  . PRO   C  185 ? 2.2009 0.8870 1.5708 -0.1785 -0.1332 0.1652  183 PRO   C CB  
5256  C  CG  . PRO   C  185 ? 2.1881 0.8676 1.5945 -0.1532 -0.1462 0.1695  183 PRO   C CG  
5257  C  CD  . PRO   C  185 ? 2.1932 0.8989 1.6183 -0.1805 -0.1688 0.1485  183 PRO   C CD  
5258  N  N   . ALA   C  186 ? 2.2464 1.2363 1.5050 -0.2596 -0.1134 0.1702  184 ALA   C N   
5259  C  CA  . ALA   C  186 ? 2.2814 1.2576 1.5316 -0.3177 -0.1190 0.1648  184 ALA   C CA  
5260  C  C   . ALA   C  186 ? 2.2677 1.2979 1.6106 -0.3203 -0.1047 0.1071  184 ALA   C C   
5261  O  O   . ALA   C  186 ? 2.3130 1.3362 1.7460 -0.3430 -0.1019 0.0014  184 ALA   C O   
5262  C  CB  . ALA   C  186 ? 2.2914 1.2757 1.5273 -0.3456 -0.1137 0.1956  184 ALA   C CB  
5263  N  N   . THR   C  187 ? 2.2156 1.3899 1.6348 -0.2755 -0.1224 0.1180  185 THR   C N   
5264  C  CA  . THR   C  187 ? 2.2539 1.4352 1.6385 -0.2245 -0.1280 0.1216  185 THR   C CA  
5265  C  C   . THR   C  187 ? 2.2045 1.4357 1.6754 -0.1393 -0.1545 0.1192  185 THR   C C   
5266  O  O   . THR   C  187 ? 2.1108 1.5400 1.6437 -0.0978 -0.1560 0.0997  185 THR   C O   
5267  C  CB  . THR   C  187 ? 2.2723 1.5099 1.6512 -0.1989 -0.1042 0.1355  185 THR   C CB  
5268  O  OG1 . THR   C  187 ? 2.2902 1.5283 1.6463 -0.2026 -0.0689 0.2165  185 THR   C OG1 
5269  C  CG2 . THR   C  187 ? 2.2775 1.4815 1.6489 -0.2139 -0.0993 0.1419  185 THR   C CG2 
5270  N  N   . VAL   C  188 ? 2.2428 1.4217 1.6635 -0.1187 -0.1812 0.1017  186 VAL   C N   
5271  C  CA  . VAL   C  188 ? 2.3188 1.4296 1.5913 -0.1395 -0.1753 0.0511  186 VAL   C CA  
5272  C  C   . VAL   C  188 ? 2.3379 1.3994 1.5081 -0.1223 -0.2050 0.0225  186 VAL   C C   
5273  O  O   . VAL   C  188 ? 2.3778 1.4971 1.4905 -0.1409 -0.2364 0.0086  186 VAL   C O   
5274  C  CB  . VAL   C  188 ? 2.3228 1.4777 1.6109 -0.1292 -0.1239 0.0278  186 VAL   C CB  
5275  C  CG1 . VAL   C  188 ? 2.3063 1.5022 1.5876 -0.1122 -0.1042 0.0267  186 VAL   C CG1 
5276  C  CG2 . VAL   C  188 ? 2.3569 1.4901 1.6121 -0.1566 -0.1323 0.0103  186 VAL   C CG2 
5277  N  N   . GLU   C  189 ? 2.3292 1.3414 1.5324 -0.1573 -0.2147 0.0587  187 GLU   C N   
5278  C  CA  . GLU   C  189 ? 2.3282 1.3410 1.5048 -0.1523 -0.2272 0.1095  187 GLU   C CA  
5279  C  C   . GLU   C  189 ? 2.2746 1.2589 1.5568 -0.1474 -0.2416 0.2220  187 GLU   C C   
5280  O  O   . GLU   C  189 ? 2.3149 1.2407 1.6509 -0.1912 -0.2583 0.2457  187 GLU   C O   
5281  C  CB  . GLU   C  189 ? 2.3724 1.4184 1.5077 -0.1833 -0.2345 0.1277  187 GLU   C CB  
5282  C  CG  . GLU   C  189 ? 2.3669 1.5094 1.5997 -0.1667 -0.2472 0.1000  187 GLU   C CG  
5283  C  CD  . GLU   C  189 ? 2.3775 1.6114 1.6234 -0.1704 -0.2152 0.1131  187 GLU   C CD  
5284  O  OE1 . GLU   C  189 ? 2.3713 1.7192 1.6517 -0.1382 -0.1975 0.0311  187 GLU   C OE1 
5285  O  OE2 . GLU   C  189 ? 2.3999 1.7280 1.6397 -0.1553 -0.2267 0.1496  187 GLU   C OE2 
5286  N  N   . GLU   C  190 ? 2.2889 1.2176 1.4883 -0.1472 -0.2765 0.2181  188 GLU   C N   
5287  C  CA  . GLU   C  190 ? 2.2500 1.3350 1.5290 -0.0963 -0.2790 0.2192  188 GLU   C CA  
5288  C  C   . GLU   C  190 ? 2.1758 1.3260 1.5324 -0.0368 -0.2274 0.2575  188 GLU   C C   
5289  O  O   . GLU   C  190 ? 2.0910 1.3717 1.5415 0.0402  -0.1837 0.2052  188 GLU   C O   
5290  C  CB  . GLU   C  190 ? 2.3006 1.3595 1.4527 -0.0795 -0.3288 0.2097  188 GLU   C CB  
5291  C  CG  . GLU   C  190 ? 2.3625 1.4152 1.4590 -0.0375 -0.3589 0.2195  188 GLU   C CG  
5292  C  CD  . GLU   C  190 ? 2.3775 1.3544 1.4302 0.0124  -0.4077 0.2638  188 GLU   C CD  
5293  O  OE1 . GLU   C  190 ? 2.4436 1.4017 1.4428 0.0758  -0.3967 0.2633  188 GLU   C OE1 
5294  O  OE2 . GLU   C  190 ? 2.3956 1.3944 1.4589 -0.0664 -0.4448 0.2427  188 GLU   C OE2 
5295  N  N   . CYS   C  191 ? 2.1677 1.2633 1.5694 -0.0150 -0.1937 0.2191  189 CYS   C N   
5296  C  CA  . CYS   C  191 ? 2.1550 1.2480 1.5687 0.0148  -0.1876 0.1801  189 CYS   C CA  
5297  C  C   . CYS   C  191 ? 2.1419 1.0694 1.5319 0.0297  -0.1579 0.1647  189 CYS   C C   
5298  O  O   . CYS   C  191 ? 2.0513 0.9911 1.5568 0.0459  -0.2087 0.1662  189 CYS   C O   
5299  C  CB  . CYS   C  191 ? 2.2053 1.2608 1.6872 0.0040  -0.1794 0.1871  189 CYS   C CB  
5300  S  SG  . CYS   C  191 ? 2.3116 1.3788 1.7642 -0.0015 -0.0756 0.1351  189 CYS   C SG  
5301  N  N   . VAL   C  192 ? 2.1489 1.0527 1.5067 -0.0005 -0.1459 0.1319  190 VAL   C N   
5302  C  CA  . VAL   C  192 ? 2.1788 1.0880 1.5104 -0.0279 -0.1418 0.0871  190 VAL   C CA  
5303  C  C   . VAL   C  192 ? 2.2339 1.1047 1.4669 0.0045  -0.1787 0.1918  190 VAL   C C   
5304  O  O   . VAL   C  192 ? 2.2601 1.1329 1.4409 0.0244  -0.1563 0.1839  190 VAL   C O   
5305  C  CB  . VAL   C  192 ? 2.2008 1.1794 1.5601 -0.0586 -0.0950 -0.0109 190 VAL   C CB  
5306  C  CG1 . VAL   C  192 ? 2.1818 1.1656 1.5882 -0.0517 -0.0698 -0.0364 190 VAL   C CG1 
5307  C  CG2 . VAL   C  192 ? 2.1721 1.1842 1.5665 -0.0376 -0.0597 -0.0160 190 VAL   C CG2 
5308  N  N   . LYS   C  193 ? 2.2562 1.0355 1.4730 -0.0052 -0.2213 0.1700  191 LYS   C N   
5309  C  CA  . LYS   C  193 ? 2.2330 1.0182 1.4248 0.0348  -0.2449 0.1787  191 LYS   C CA  
5310  C  C   . LYS   C  193 ? 2.2119 0.8428 1.3847 0.0307  -0.2800 0.2453  191 LYS   C C   
5311  O  O   . LYS   C  193 ? 2.1641 0.8203 1.3713 -0.0123 -0.2756 0.3141  191 LYS   C O   
5312  C  CB  . LYS   C  193 ? 2.2609 1.0317 1.4173 0.0185  -0.2490 0.1607  191 LYS   C CB  
5313  C  CG  . LYS   C  193 ? 2.2730 1.0778 1.4532 -0.0194 -0.2393 0.1809  191 LYS   C CG  
5314  C  CD  . LYS   C  193 ? 2.2824 1.2263 1.4597 -0.0164 -0.2610 0.1809  191 LYS   C CD  
5315  C  CE  . LYS   C  193 ? 2.2938 1.2773 1.4561 -0.0389 -0.2534 0.2361  191 LYS   C CE  
5316  N  NZ  . LYS   C  193 ? 2.3245 1.3985 1.4258 -0.0530 -0.2464 0.2309  191 LYS   C NZ  
5317  N  N   . LEU   C  194 ? 2.2171 0.7957 1.3256 0.0173  -0.3199 0.2577  192 LEU   C N   
5318  C  CA  . LEU   C  194 ? 2.1994 0.8329 1.3212 0.0009  -0.3236 0.2434  192 LEU   C CA  
5319  C  C   . LEU   C  194 ? 2.2236 0.8595 1.3323 0.0261  -0.3317 0.2683  192 LEU   C C   
5320  O  O   . LEU   C  194 ? 2.2781 0.9783 1.3737 0.0979  -0.3250 0.2022  192 LEU   C O   
5321  C  CB  . LEU   C  194 ? 2.2202 0.8002 1.2457 -0.0214 -0.3628 0.2464  192 LEU   C CB  
5322  C  CG  . LEU   C  194 ? 2.1914 0.8283 1.2419 -0.0471 -0.3728 0.2249  192 LEU   C CG  
5323  C  CD1 . LEU   C  194 ? 2.2227 0.8441 1.2601 -0.0387 -0.3794 0.2439  192 LEU   C CD1 
5324  C  CD2 . LEU   C  194 ? 2.2172 0.7913 1.2170 -0.0575 -0.3869 0.2281  192 LEU   C CD2 
5325  N  N   . THR   C  195 ? 2.1988 0.8001 1.3483 0.0143  -0.2837 0.2274  193 THR   C N   
5326  C  CA  . THR   C  195 ? 2.1466 0.8061 1.3387 0.0145  -0.2727 0.1763  193 THR   C CA  
5327  C  C   . THR   C  195 ? 2.1500 0.9218 1.3932 -0.0500 -0.2166 0.2235  193 THR   C C   
5328  O  O   . THR   C  195 ? 2.1495 0.9723 1.3980 -0.1106 -0.2006 0.2132  193 THR   C O   
5329  C  CB  . THR   C  195 ? 2.1137 0.8104 1.3158 0.0736  -0.2772 0.1112  193 THR   C CB  
5330  O  OG1 . THR   C  195 ? 2.1009 0.6938 1.3621 0.1265  -0.2730 0.1239  193 THR   C OG1 
5331  C  CG2 . THR   C  195 ? 2.0604 0.7217 1.3329 0.1066  -0.2957 0.1034  193 THR   C CG2 
5332  N  N   . VAL   C  196 ? 2.1776 0.9714 1.4090 -0.0886 -0.1918 0.2034  194 VAL   C N   
5333  C  CA  . VAL   C  196 ? 2.1955 1.0225 1.4703 -0.1113 -0.1781 0.2054  194 VAL   C CA  
5334  C  C   . VAL   C  196 ? 2.2150 1.0243 1.4970 -0.1025 -0.2108 0.2550  194 VAL   C C   
5335  O  O   . VAL   C  196 ? 2.2401 0.8655 1.5894 -0.1028 -0.2278 0.2970  194 VAL   C O   
5336  C  CB  . VAL   C  196 ? 2.2573 1.1074 1.4809 -0.1243 -0.1465 0.1827  194 VAL   C CB  
5337  C  CG1 . VAL   C  196 ? 2.2688 1.1634 1.4929 -0.1521 -0.1189 0.1659  194 VAL   C CG1 
5338  C  CG2 . VAL   C  196 ? 2.2654 1.0676 1.4833 -0.1594 -0.1479 0.1609  194 VAL   C CG2 
5339  N  N   . ARG   C  197 ? 2.2268 1.0030 1.4862 -0.1005 -0.2024 0.2755  195 ARG   C N   
5340  C  CA  . ARG   C  197 ? 2.2479 1.0021 1.5397 -0.0957 -0.1786 0.2338  195 ARG   C CA  
5341  C  C   . ARG   C  197 ? 2.2602 0.9875 1.5412 -0.1175 -0.1559 0.2398  195 ARG   C C   
5342  O  O   . ARG   C  197 ? 2.2935 1.1068 1.4484 -0.1439 -0.1190 0.1052  195 ARG   C O   
5343  C  CB  . ARG   C  197 ? 2.2352 1.0752 1.5840 -0.0921 -0.1934 0.2350  195 ARG   C CB  
5344  C  CG  . ARG   C  197 ? 2.2302 1.0929 1.5754 -0.0885 -0.2217 0.2695  195 ARG   C CG  
5345  C  CD  . ARG   C  197 ? 2.2561 1.0972 1.5422 -0.0844 -0.2282 0.3209  195 ARG   C CD  
5346  N  NE  . ARG   C  197 ? 2.2621 1.0900 1.5544 -0.0767 -0.2316 0.3630  195 ARG   C NE  
5347  C  CZ  . ARG   C  197 ? 2.2562 1.0815 1.5776 -0.0595 -0.2244 0.3693  195 ARG   C CZ  
5348  N  NH1 . ARG   C  197 ? 2.2440 1.1061 1.5800 -0.0862 -0.2192 0.3686  195 ARG   C NH1 
5349  N  NH2 . ARG   C  197 ? 2.2635 1.0816 1.5938 -0.0437 -0.2209 0.3977  195 ARG   C NH2 
5350  N  N   . SER   C  198 ? 2.2866 0.7998 1.5790 -0.0949 -0.2023 0.2370  196 SER   C N   
5351  C  CA  . SER   C  198 ? 2.2631 0.7307 1.5887 -0.0718 -0.2289 0.2226  196 SER   C CA  
5352  C  C   . SER   C  198 ? 2.2038 0.6951 1.6948 -0.0819 -0.2645 0.2625  196 SER   C C   
5353  O  O   . SER   C  198 ? 2.2051 0.7088 1.7338 -0.1030 -0.2763 0.2324  196 SER   C O   
5354  C  CB  . SER   C  198 ? 2.2473 0.6711 1.5832 -0.0426 -0.2351 0.1946  196 SER   C CB  
5355  O  OG  . SER   C  198 ? 2.2398 0.6721 1.5763 -0.0229 -0.2317 0.1590  196 SER   C OG  
5356  N  N   . LEU   C  199 ? 2.1835 0.6918 1.7165 -0.0955 -0.2670 0.2428  197 LEU   C N   
5357  C  CA  . LEU   C  199 ? 2.1967 0.7767 1.7466 -0.0880 -0.2842 0.2533  197 LEU   C CA  
5358  C  C   . LEU   C  199 ? 2.2416 0.8248 1.7606 -0.0999 -0.2381 0.3234  197 LEU   C C   
5359  O  O   . LEU   C  199 ? 2.2361 0.7969 1.8998 -0.1013 -0.2613 0.2546  197 LEU   C O   
5360  C  CB  . LEU   C  199 ? 2.2061 0.8034 1.7202 -0.0690 -0.2954 0.1955  197 LEU   C CB  
5361  C  CG  . LEU   C  199 ? 2.1818 0.8030 1.6921 -0.0572 -0.3117 0.1899  197 LEU   C CG  
5362  C  CD1 . LEU   C  199 ? 2.1708 0.8255 1.6831 -0.0545 -0.3123 0.1696  197 LEU   C CD1 
5363  C  CD2 . LEU   C  199 ? 2.1936 0.8113 1.6959 -0.0256 -0.2862 0.1740  197 LEU   C CD2 
5364  N  N   . LEU   C  200 ? 2.2290 0.8667 1.7398 -0.1459 -0.2523 0.3196  198 LEU   C N   
5365  C  CA  . LEU   C  200 ? 2.2353 0.8722 1.6318 -0.1443 -0.2511 0.3268  198 LEU   C CA  
5366  C  C   . LEU   C  200 ? 2.2696 0.8061 1.6170 -0.1453 -0.2771 0.3787  198 LEU   C C   
5367  O  O   . LEU   C  200 ? 2.2647 0.7459 1.6234 -0.0993 -0.2856 0.3525  198 LEU   C O   
5368  C  CB  . LEU   C  200 ? 2.2306 0.9340 1.6261 -0.2489 -0.2506 0.3445  198 LEU   C CB  
5369  C  CG  . LEU   C  200 ? 2.2113 0.9573 1.6095 -0.2833 -0.2220 0.3267  198 LEU   C CG  
5370  C  CD1 . LEU   C  200 ? 2.2102 1.0387 1.6113 -0.3104 -0.2390 0.3447  198 LEU   C CD1 
5371  C  CD2 . LEU   C  200 ? 2.2232 0.9822 1.6001 -0.3181 -0.2033 0.3206  198 LEU   C CD2 
5372  N  N   . GLU   C  201 ? 2.2709 0.7350 1.5787 -0.1167 -0.2813 0.3626  199 GLU   C N   
5373  C  CA  . GLU   C  201 ? 2.2979 0.7815 1.5771 -0.1137 -0.2775 0.3159  199 GLU   C CA  
5374  C  C   . GLU   C  201 ? 2.3627 0.7423 1.5624 -0.0796 -0.2469 0.2377  199 GLU   C C   
5375  O  O   . GLU   C  201 ? 2.4395 0.8087 1.4483 -0.0231 -0.2796 0.1655  199 GLU   C O   
5376  C  CB  . GLU   C  201 ? 2.3059 0.7913 1.6729 -0.1315 -0.2363 0.3510  199 GLU   C CB  
5377  C  CG  . GLU   C  201 ? 2.2787 0.9294 1.6924 -0.1584 -0.2162 0.3130  199 GLU   C CG  
5378  C  CD  . GLU   C  201 ? 2.2996 0.9774 1.6940 -0.1506 -0.1397 0.3467  199 GLU   C CD  
5379  O  OE1 . GLU   C  201 ? 2.3202 1.0192 1.8219 -0.1042 -0.1314 0.3197  199 GLU   C OE1 
5380  O  OE2 . GLU   C  201 ? 2.3311 1.2014 1.6975 -0.1974 -0.1194 0.3383  199 GLU   C OE2 
5381  N  N   . VAL   C  202 ? 2.2840 0.8135 1.4584 -0.0481 -0.2807 0.1724  200 VAL   C N   
5382  C  CA  . VAL   C  202 ? 2.2317 0.8425 1.4769 -0.0300 -0.2915 0.0783  200 VAL   C CA  
5383  C  C   . VAL   C  202 ? 2.2448 0.8197 1.4794 -0.0017 -0.3100 0.0639  200 VAL   C C   
5384  O  O   . VAL   C  202 ? 2.2434 0.6859 1.4922 0.0700  -0.3058 0.0557  200 VAL   C O   
5385  C  CB  . VAL   C  202 ? 2.1748 0.9031 1.4481 -0.0016 -0.2884 0.0973  200 VAL   C CB  
5386  C  CG1 . VAL   C  202 ? 2.1120 0.8707 1.4833 0.0154  -0.3043 0.1011  200 VAL   C CG1 
5387  C  CG2 . VAL   C  202 ? 2.1755 0.9673 1.4458 -0.0050 -0.2721 0.0746  200 VAL   C CG2 
5388  N  N   . VAL   C  203 ? 2.3271 0.9291 1.4816 0.0028  -0.3219 -0.0160 201 VAL   C N   
5389  C  CA  . VAL   C  203 ? 2.3320 1.0738 1.5825 0.0223  -0.3397 -0.0339 201 VAL   C CA  
5390  C  C   . VAL   C  203 ? 2.4435 1.0481 1.7472 -0.0226 -0.2608 -0.0369 201 VAL   C C   
5391  O  O   . VAL   C  203 ? 2.5408 1.1462 1.7005 0.0147  -0.2362 -0.0290 201 VAL   C O   
5392  C  CB  . VAL   C  203 ? 2.3570 1.1227 1.5780 -0.0123 -0.3780 -0.0863 201 VAL   C CB  
5393  C  CG1 . VAL   C  203 ? 2.3783 1.2004 1.5968 -0.0346 -0.3917 -0.0458 201 VAL   C CG1 
5394  C  CG2 . VAL   C  203 ? 2.3517 1.1257 1.5562 -0.0139 -0.3679 -0.0791 201 VAL   C CG2 
5395  N  N   . GLN   C  204 ? 2.4723 1.0260 1.8584 -0.0819 -0.1990 -0.0042 202 GLN   C N   
5396  C  CA  . GLN   C  204 ? 2.5336 1.1889 2.0831 -0.1734 -0.1212 -0.0358 202 GLN   C CA  
5397  C  C   . GLN   C  204 ? 2.5258 1.1907 2.0195 -0.1927 -0.1822 -0.0337 202 GLN   C C   
5398  O  O   . GLN   C  204 ? 2.4594 1.2767 2.0226 -0.2185 -0.1862 0.0002  202 GLN   C O   
5399  C  CB  . GLN   C  204 ? 2.5243 1.2660 2.1279 -0.2026 -0.1255 -0.0291 202 GLN   C CB  
5400  C  CG  . GLN   C  204 ? 2.5308 1.4990 2.3250 -0.2574 -0.0502 -0.1090 202 GLN   C CG  
5401  C  CD  . GLN   C  204 ? 2.6920 1.4954 2.5321 -0.2007 -0.0066 -0.2141 202 GLN   C CD  
5402  O  OE1 . GLN   C  204 ? 2.7319 1.6055 2.6772 -0.2041 0.0390  -0.3532 202 GLN   C OE1 
5403  N  NE2 . GLN   C  204 ? 2.7223 1.7362 2.5945 -0.2047 0.0971  -0.2685 202 GLN   C NE2 
5404  N  N   . THR   C  205 ? 2.5301 1.2191 2.1211 -0.1830 -0.1939 -0.1046 203 THR   C N   
5405  C  CA  . THR   C  205 ? 2.5310 1.4205 2.0559 -0.1683 -0.2576 -0.1457 203 THR   C CA  
5406  C  C   . THR   C  205 ? 2.6283 1.4344 2.0047 -0.1716 -0.2174 -0.1834 203 THR   C C   
5407  O  O   . THR   C  205 ? 2.6791 1.6638 1.9365 -0.1292 -0.1722 -0.1452 203 THR   C O   
5408  C  CB  . THR   C  205 ? 2.5363 1.3548 2.0472 -0.2162 -0.3530 -0.2089 203 THR   C CB  
5409  O  OG1 . THR   C  205 ? 2.3984 1.0626 2.2466 -0.2366 -0.4630 -0.2273 203 THR   C OG1 
5410  C  CG2 . THR   C  205 ? 2.4799 1.3923 1.9843 -0.2067 -0.3742 -0.2388 203 THR   C CG2 
5411  N  N   . GLY   C  206 ? 2.6565 1.5231 1.9840 -0.0974 -0.2223 -0.1669 204 GLY   C N   
5412  C  CA  . GLY   C  206 ? 2.5590 1.5075 2.0595 -0.0759 -0.2331 -0.1649 204 GLY   C CA  
5413  C  C   . GLY   C  206 ? 2.6158 1.4177 2.0620 -0.0716 -0.2507 -0.2416 204 GLY   C C   
5414  O  O   . GLY   C  206 ? 2.4856 1.3145 2.1118 -0.0243 -0.3358 -0.1983 204 GLY   C O   
5415  N  N   . ALA   C  207 ? 2.5158 1.5595 2.0901 0.0555  -0.2749 -0.0864 205 ALA   C N   
5416  C  CA  . ALA   C  207 ? 2.4730 1.5970 2.0650 0.0348  -0.2163 -0.0398 205 ALA   C CA  
5417  C  C   . ALA   C  207 ? 2.4540 1.6296 2.0703 -0.1137 -0.1019 -0.0742 205 ALA   C C   
5418  O  O   . ALA   C  207 ? 2.5292 1.6005 1.7646 -0.1472 -0.1411 -0.0874 205 ALA   C O   
5419  C  CB  . ALA   C  207 ? 2.4400 1.5712 2.0406 0.0486  -0.2227 -0.0086 205 ALA   C CB  
5420  N  N   . LYS   C  208 ? 2.4501 1.8037 2.0397 -0.0738 -0.0421 -0.0284 206 LYS   C N   
5421  C  CA  . LYS   C  208 ? 2.4505 1.7667 2.1965 -0.1245 0.0597  -0.0082 206 LYS   C CA  
5422  C  C   . LYS   C  208 ? 2.2374 1.6872 2.2793 -0.1404 0.0048  -0.0362 206 LYS   C C   
5423  O  O   . LYS   C  208 ? 2.3105 1.7520 2.2855 -0.2238 -0.0390 -0.0309 206 LYS   C O   
5424  C  CB  . LYS   C  208 ? 2.4501 1.8563 2.2296 -0.0623 0.1200  0.0155  206 LYS   C CB  
5425  C  CG  . LYS   C  208 ? 2.5266 1.8728 2.3006 -0.0560 0.2115  0.0477  206 LYS   C CG  
5426  C  CD  . LYS   C  208 ? 2.5316 1.8756 2.3371 -0.0469 0.1972  0.0891  206 LYS   C CD  
5427  C  CE  . LYS   C  208 ? 2.5328 1.7859 2.4430 -0.0121 0.2473  0.1182  206 LYS   C CE  
5428  N  NZ  . LYS   C  208 ? 2.5895 1.8422 2.4953 -0.0346 0.2927  0.1622  206 LYS   C NZ  
5429  N  N   . ASN   C  209 ? 2.1991 1.5605 2.3748 -0.1987 -0.0297 -0.0483 207 ASN   C N   
5430  C  CA  . ASN   C  209 ? 2.0328 1.4847 2.4003 -0.1421 -0.1218 -0.0110 207 ASN   C CA  
5431  C  C   . ASN   C  209 ? 2.0559 1.3211 2.1958 -0.0861 -0.2117 -0.0632 207 ASN   C C   
5432  O  O   . ASN   C  209 ? 1.9850 1.1602 2.1144 -0.1381 -0.2929 -0.0753 207 ASN   C O   
5433  C  CB  . ASN   C  209 ? 2.0575 1.5452 2.5416 -0.0507 -0.0709 0.0811  207 ASN   C CB  
5434  C  CG  . ASN   C  209 ? 1.9381 1.7300 2.6343 -0.0611 -0.0656 0.0977  207 ASN   C CG  
5435  O  OD1 . ASN   C  209 ? 1.9517 1.7563 2.6798 -0.0296 -0.0338 0.1810  207 ASN   C OD1 
5436  N  ND2 . ASN   C  209 ? 1.9580 1.7500 2.7012 -0.0281 -0.0034 0.1207  207 ASN   C ND2 
5437  N  N   . ILE   C  210 ? 2.0468 1.3127 2.1766 -0.0684 -0.2207 -0.0548 208 ILE   C N   
5438  C  CA  . ILE   C  210 ? 2.1156 1.2873 2.0205 -0.0895 -0.2466 -0.0793 208 ILE   C CA  
5439  C  C   . ILE   C  210 ? 2.0566 1.3082 1.8855 -0.0982 -0.2389 -0.1322 208 ILE   C C   
5440  O  O   . ILE   C  210 ? 2.0216 1.4719 1.9024 -0.1660 -0.2282 -0.1878 208 ILE   C O   
5441  C  CB  . ILE   C  210 ? 2.2289 1.2038 2.0299 -0.1112 -0.2690 -0.0605 208 ILE   C CB  
5442  C  CG1 . ILE   C  210 ? 2.3549 1.1915 2.1102 -0.1010 -0.2732 -0.0317 208 ILE   C CG1 
5443  C  CG2 . ILE   C  210 ? 2.2506 1.1244 2.0068 -0.0761 -0.2778 -0.0815 208 ILE   C CG2 
5444  C  CD1 . ILE   C  210 ? 2.4277 1.3329 2.0766 -0.1344 -0.3070 -0.0237 208 ILE   C CD1 
5445  N  N   . GLU   C  211 ? 2.1254 1.3011 1.7722 -0.0606 -0.2940 -0.0592 209 GLU   C N   
5446  C  CA  . GLU   C  211 ? 2.1043 1.2702 1.7550 -0.0317 -0.2890 0.0306  209 GLU   C CA  
5447  C  C   . GLU   C  211 ? 2.1079 1.0507 1.6672 -0.0631 -0.2773 0.1440  209 GLU   C C   
5448  O  O   . GLU   C  211 ? 1.9694 1.0383 1.6139 -0.1200 -0.3086 0.3142  209 GLU   C O   
5449  C  CB  . GLU   C  211 ? 2.2060 1.3618 1.7034 0.0117  -0.2859 -0.0037 209 GLU   C CB  
5450  C  CG  . GLU   C  211 ? 2.1936 1.5897 1.8498 0.0250  -0.2849 -0.1325 209 GLU   C CG  
5451  C  CD  . GLU   C  211 ? 2.2891 1.7550 1.7959 0.0103  -0.2550 -0.1606 209 GLU   C CD  
5452  O  OE1 . GLU   C  211 ? 2.3218 1.9106 1.8271 -0.0353 -0.1495 -0.2994 209 GLU   C OE1 
5453  O  OE2 . GLU   C  211 ? 2.3071 1.9982 1.9426 0.0128  -0.3237 -0.3510 209 GLU   C OE2 
5454  N  N   . ILE   C  212 ? 2.0703 0.9460 1.6844 -0.0635 -0.2509 0.1693  210 ILE   C N   
5455  C  CA  . ILE   C  212 ? 2.1033 1.0400 1.7079 -0.0966 -0.2397 0.0978  210 ILE   C CA  
5456  C  C   . ILE   C  212 ? 2.0933 1.0399 1.6642 -0.1405 -0.2263 0.1119  210 ILE   C C   
5457  O  O   . ILE   C  212 ? 2.0891 1.0915 1.6666 -0.1426 -0.2108 0.1202  210 ILE   C O   
5458  C  CB  . ILE   C  212 ? 2.1650 1.1508 1.6872 -0.1091 -0.2341 0.0719  210 ILE   C CB  
5459  C  CG1 . ILE   C  212 ? 2.2073 1.1600 1.7605 -0.1240 -0.2314 -0.0251 210 ILE   C CG1 
5460  C  CG2 . ILE   C  212 ? 2.1628 1.0751 1.7218 -0.1116 -0.2279 0.0777  210 ILE   C CG2 
5461  C  CD1 . ILE   C  212 ? 2.1878 1.2708 1.7552 -0.1326 -0.2325 -0.0356 210 ILE   C CD1 
5462  N  N   . THR   C  213 ? 2.0862 1.0386 1.6392 -0.1746 -0.2426 0.0529  211 THR   C N   
5463  C  CA  . THR   C  213 ? 2.1339 1.0449 1.6600 -0.1800 -0.2161 0.0006  211 THR   C CA  
5464  C  C   . THR   C  213 ? 2.1107 0.9755 1.6373 -0.1576 -0.1953 0.0404  211 THR   C C   
5465  O  O   . THR   C  213 ? 2.1977 0.7840 1.6396 -0.1185 -0.1880 0.1027  211 THR   C O   
5466  C  CB  . THR   C  213 ? 2.0660 1.0316 1.6316 -0.2103 -0.2655 -0.0380 211 THR   C CB  
5467  O  OG1 . THR   C  213 ? 2.0458 1.0847 1.7446 -0.2554 -0.2545 -0.0898 211 THR   C OG1 
5468  C  CG2 . THR   C  213 ? 2.0666 1.0306 1.6545 -0.1704 -0.2588 -0.0572 211 THR   C CG2 
5469  N  N   . VAL   C  214 ? 2.2056 0.9838 1.6633 -0.1845 -0.1390 0.0287  212 VAL   C N   
5470  C  CA  . VAL   C  214 ? 2.2191 0.9934 1.6125 -0.1351 -0.1554 0.0419  212 VAL   C CA  
5471  C  C   . VAL   C  214 ? 2.1796 0.9758 1.6644 -0.1035 -0.1170 0.0200  212 VAL   C C   
5472  O  O   . VAL   C  214 ? 2.2764 0.9650 1.6962 -0.0491 -0.1180 0.0877  212 VAL   C O   
5473  C  CB  . VAL   C  214 ? 2.2666 0.9271 1.5978 -0.1428 -0.1703 0.0608  212 VAL   C CB  
5474  C  CG1 . VAL   C  214 ? 2.3028 0.8968 1.5313 -0.1192 -0.1821 0.0753  212 VAL   C CG1 
5475  C  CG2 . VAL   C  214 ? 2.2456 0.9804 1.6017 -0.1860 -0.1514 0.0785  212 VAL   C CG2 
5476  N  N   . VAL   C  215 ? 2.1298 0.9834 1.6680 -0.0636 -0.1428 0.0048  213 VAL   C N   
5477  C  CA  . VAL   C  215 ? 2.0636 0.9837 1.6238 -0.0317 -0.1384 0.0337  213 VAL   C CA  
5478  C  C   . VAL   C  215 ? 2.0532 1.0779 1.6103 0.0296  -0.1563 0.0658  213 VAL   C C   
5479  O  O   . VAL   C  215 ? 2.0365 1.1653 1.5970 0.0588  -0.2029 0.0508  213 VAL   C O   
5480  C  CB  . VAL   C  215 ? 2.0807 0.9544 1.6089 0.0022  -0.1404 0.0164  213 VAL   C CB  
5481  C  CG1 . VAL   C  215 ? 2.1095 0.9071 1.5834 -0.0095 -0.1569 0.0184  213 VAL   C CG1 
5482  C  CG2 . VAL   C  215 ? 2.0990 1.0217 1.5958 -0.0545 -0.1362 0.0355  213 VAL   C CG2 
5483  N  N   . LYS   C  216 ? 2.0324 1.1309 1.5519 -0.0003 -0.1669 0.0315  214 LYS   C N   
5484  C  CA  . LYS   C  216 ? 2.0456 1.1162 1.5246 -0.0310 -0.1592 0.0514  214 LYS   C CA  
5485  C  C   . LYS   C  216 ? 2.0672 1.1229 1.5513 -0.0497 -0.1772 0.0669  214 LYS   C C   
5486  O  O   . LYS   C  216 ? 1.9712 1.0364 1.5771 -0.0711 -0.1799 0.0396  214 LYS   C O   
5487  C  CB  . LYS   C  216 ? 2.0692 1.2273 1.5485 -0.0324 -0.1422 -0.0371 214 LYS   C CB  
5488  C  CG  . LYS   C  216 ? 2.0593 1.2318 1.5631 -0.0711 -0.0956 -0.0478 214 LYS   C CG  
5489  C  CD  . LYS   C  216 ? 2.0716 1.3101 1.6352 -0.0752 -0.0532 -0.1161 214 LYS   C CD  
5490  C  CE  . LYS   C  216 ? 2.0460 1.3528 1.6870 -0.0476 -0.0132 -0.1728 214 LYS   C CE  
5491  N  NZ  . LYS   C  216 ? 2.0860 1.4628 1.7434 -0.0335 0.0323  -0.2007 214 LYS   C NZ  
5492  N  N   . PRO   C  217 ? 2.1203 1.0985 1.4992 -0.0463 -0.2428 0.1580  215 PRO   C N   
5493  C  CA  . PRO   C  217 ? 2.1617 1.0793 1.5474 -0.0619 -0.2449 0.1144  215 PRO   C CA  
5494  C  C   . PRO   C  217 ? 2.1980 1.1480 1.6407 -0.0071 -0.1824 0.0174  215 PRO   C C   
5495  O  O   . PRO   C  217 ? 2.2565 1.1493 1.6266 -0.0398 -0.1350 -0.0348 215 PRO   C O   
5496  C  CB  . PRO   C  217 ? 2.2028 1.0504 1.4839 -0.0614 -0.2550 0.1593  215 PRO   C CB  
5497  C  CG  . PRO   C  217 ? 2.1732 1.0735 1.4550 -0.0726 -0.2705 0.1877  215 PRO   C CG  
5498  C  CD  . PRO   C  217 ? 2.1588 1.0890 1.4839 -0.0673 -0.2353 0.1830  215 PRO   C CD  
5499  N  N   . ASP   C  218 ? 2.2413 1.1327 1.6880 0.0027  -0.1760 0.0228  216 ASP   C N   
5500  C  CA  . ASP   C  218 ? 2.2420 1.1424 1.7030 0.0176  -0.1408 0.0227  216 ASP   C CA  
5501  C  C   . ASP   C  218 ? 2.1765 1.0906 1.7221 0.1113  -0.0978 0.0304  216 ASP   C C   
5502  O  O   . ASP   C  218 ? 2.1980 1.1703 1.7544 0.1534  -0.0708 0.0520  216 ASP   C O   
5503  C  CB  . ASP   C  218 ? 2.3522 1.2326 1.6871 0.0043  -0.0951 0.0013  216 ASP   C CB  
5504  C  CG  . ASP   C  218 ? 2.3926 1.3303 1.7095 -0.0465 -0.1031 -0.0075 216 ASP   C CG  
5505  O  OD1 . ASP   C  218 ? 2.4233 1.3917 1.6444 -0.0903 -0.1375 -0.0387 216 ASP   C OD1 
5506  O  OD2 . ASP   C  218 ? 2.4590 1.4254 1.6205 -0.0770 0.0206  0.0955  216 ASP   C OD2 
5507  N  N   . SER   C  219 ? 2.1144 1.0181 1.7097 0.1306  -0.0947 0.0553  217 SER   C N   
5508  C  CA  . SER   C  219 ? 2.0817 0.9709 1.6567 0.1116  -0.0459 0.0611  217 SER   C CA  
5509  C  C   . SER   C  219 ? 2.0390 0.9818 1.7075 0.0973  -0.0213 0.0114  217 SER   C C   
5510  O  O   . SER   C  219 ? 2.0340 0.9005 1.6625 0.0843  0.0000  0.0809  217 SER   C O   
5511  C  CB  . SER   C  219 ? 2.0763 0.9731 1.6380 0.1076  -0.0117 0.0725  217 SER   C CB  
5512  O  OG  . SER   C  219 ? 2.1290 0.9562 1.5957 0.0938  -0.0023 0.0756  217 SER   C OG  
5513  N  N   . ASP   C  220 ? 2.1248 0.9805 1.6395 0.0200  -0.0304 0.0192  218 ASP   C N   
5514  C  CA  . ASP   C  220 ? 2.1617 1.0536 1.5792 -0.0326 -0.0026 -0.0604 218 ASP   C CA  
5515  C  C   . ASP   C  220 ? 2.1392 1.0795 1.5855 -0.0472 -0.0460 -0.0692 218 ASP   C C   
5516  O  O   . ASP   C  220 ? 2.1726 1.0809 1.7133 0.0215  -0.0430 -0.1378 218 ASP   C O   
5517  C  CB  . ASP   C  220 ? 2.2285 1.0984 1.5248 -0.0815 0.0252  -0.1449 218 ASP   C CB  
5518  C  CG  . ASP   C  220 ? 2.2350 1.1563 1.4992 -0.1052 0.0467  -0.2188 218 ASP   C CG  
5519  O  OD1 . ASP   C  220 ? 2.2201 1.0795 1.4941 -0.0989 0.0838  -0.3088 218 ASP   C OD1 
5520  O  OD2 . ASP   C  220 ? 2.2573 1.2314 1.4709 -0.1275 0.0176  -0.2597 218 ASP   C OD2 
5521  N  N   . ILE   C  221 ? 2.1292 1.0382 1.5436 -0.0074 -0.0304 -0.0623 219 ILE   C N   
5522  C  CA  . ILE   C  221 ? 2.1297 0.9992 1.5095 0.0409  -0.0240 -0.0592 219 ILE   C CA  
5523  C  C   . ILE   C  221 ? 2.1313 0.9665 1.5067 0.0478  -0.0144 -0.0962 219 ILE   C C   
5524  O  O   . ILE   C  221 ? 2.1884 1.0574 1.4752 0.0992  -0.0608 -0.0241 219 ILE   C O   
5525  C  CB  . ILE   C  221 ? 2.0971 0.9676 1.5106 0.0314  -0.0327 -0.0474 219 ILE   C CB  
5526  C  CG1 . ILE   C  221 ? 2.1000 0.9621 1.4849 0.0169  -0.0411 -0.0518 219 ILE   C CG1 
5527  C  CG2 . ILE   C  221 ? 2.0795 1.0045 1.5204 -0.0122 -0.0597 -0.0332 219 ILE   C CG2 
5528  C  CD1 . ILE   C  221 ? 2.0727 0.9693 1.4654 0.0224  -0.0424 -0.0741 219 ILE   C CD1 
5529  N  N   . VAL   C  222 ? 2.1313 0.9917 1.5175 -0.0028 -0.0035 -0.0984 220 VAL   C N   
5530  C  CA  . VAL   C  222 ? 2.1368 1.0269 1.5260 -0.0253 -0.0125 -0.1119 220 VAL   C CA  
5531  C  C   . VAL   C  222 ? 2.0774 0.9873 1.5663 -0.1004 -0.0721 -0.0345 220 VAL   C C   
5532  O  O   . VAL   C  222 ? 2.0775 0.8188 1.6398 -0.1528 -0.0568 -0.0581 220 VAL   C O   
5533  C  CB  . VAL   C  222 ? 2.1625 1.0783 1.5517 0.0027  0.0364  -0.1524 220 VAL   C CB  
5534  C  CG1 . VAL   C  222 ? 2.1773 1.0866 1.5265 -0.0027 0.0343  -0.1503 220 VAL   C CG1 
5535  C  CG2 . VAL   C  222 ? 2.1595 1.0831 1.5489 0.0169  0.0580  -0.1618 220 VAL   C CG2 
5536  N  N   . ALA   C  223 ? 2.0948 0.9926 1.5753 -0.1405 -0.0876 0.0028  221 ALA   C N   
5537  C  CA  . ALA   C  223 ? 2.0366 1.0783 1.5590 -0.1806 -0.1265 -0.0780 221 ALA   C CA  
5538  C  C   . ALA   C  223 ? 2.0155 1.1623 1.5730 -0.1470 -0.1024 -0.0578 221 ALA   C C   
5539  O  O   . ALA   C  223 ? 1.9891 1.3518 1.6183 -0.1666 -0.0438 -0.1182 221 ALA   C O   
5540  C  CB  . ALA   C  223 ? 2.0426 1.0907 1.5565 -0.1807 -0.1270 -0.0709 221 ALA   C CB  
5541  N  N   . LEU   C  224 ? 2.0139 1.1820 1.5704 -0.1415 -0.1231 -0.0147 222 LEU   C N   
5542  C  CA  . LEU   C  224 ? 2.0144 1.1483 1.6170 -0.1195 -0.1165 0.0103  222 LEU   C CA  
5543  C  C   . LEU   C  224 ? 2.0012 1.1187 1.6053 -0.1066 -0.0927 -0.0243 222 LEU   C C   
5544  O  O   . LEU   C  224 ? 1.9167 0.9772 1.6231 -0.0987 -0.0943 -0.0679 222 LEU   C O   
5545  C  CB  . LEU   C  224 ? 2.0565 1.1280 1.6231 -0.1459 -0.1514 0.0439  222 LEU   C CB  
5546  C  CG  . LEU   C  224 ? 2.0997 1.1324 1.6111 -0.1807 -0.1588 0.0519  222 LEU   C CG  
5547  C  CD1 . LEU   C  224 ? 2.0805 1.1140 1.6163 -0.1749 -0.1753 0.0186  222 LEU   C CD1 
5548  C  CD2 . LEU   C  224 ? 2.1090 1.1227 1.5787 -0.1937 -0.1795 0.0641  222 LEU   C CD2 
5549  N  N   . SER   C  225 ? 2.0446 1.1846 1.7069 -0.1313 -0.0358 -0.0004 223 SER   C N   
5550  C  CA  . SER   C  225 ? 2.0416 1.3000 1.7670 -0.1558 -0.0316 0.0077  223 SER   C CA  
5551  C  C   . SER   C  225 ? 2.0420 1.3202 1.8108 -0.0789 -0.0436 0.0369  223 SER   C C   
5552  O  O   . SER   C  225 ? 2.0477 1.4983 1.8795 0.0012  -0.0441 0.0143  223 SER   C O   
5553  C  CB  . SER   C  225 ? 2.0345 1.3296 1.7946 -0.2023 0.0174  0.0141  223 SER   C CB  
5554  O  OG  . SER   C  225 ? 2.0295 1.3850 1.7689 -0.2654 0.0515  -0.0052 223 SER   C OG  
5555  N  N   . SER   C  226 ? 2.0113 1.4142 1.7965 -0.0941 -0.0454 0.0687  224 SER   C N   
5556  C  CA  . SER   C  226 ? 1.9839 1.4196 1.7977 -0.1206 -0.0419 0.0952  224 SER   C CA  
5557  C  C   . SER   C  226 ? 2.0698 1.4681 1.8259 -0.1242 -0.0531 0.1264  224 SER   C C   
5558  O  O   . SER   C  226 ? 2.1035 1.4068 1.8277 -0.1159 -0.0323 0.0760  224 SER   C O   
5559  C  CB  . SER   C  226 ? 1.9757 1.4096 1.6644 -0.0934 -0.0528 0.1184  224 SER   C CB  
5560  O  OG  . SER   C  226 ? 1.8547 1.3710 1.6413 -0.1181 -0.0613 0.0631  224 SER   C OG  
5561  N  N   . GLU   C  227 ? 2.0947 1.5847 1.9486 -0.1311 -0.0017 0.0474  225 GLU   C N   
5562  C  CA  . GLU   C  227 ? 2.1722 1.6683 1.9571 -0.1732 -0.0438 0.0399  225 GLU   C CA  
5563  C  C   . GLU   C  227 ? 2.1972 1.6200 1.9867 -0.2677 -0.0548 0.0252  225 GLU   C C   
5564  O  O   . GLU   C  227 ? 2.1845 1.5524 1.9593 -0.3380 -0.1138 -0.0217 225 GLU   C O   
5565  C  CB  . GLU   C  227 ? 2.2432 1.7522 2.0580 -0.1309 -0.0144 -0.0140 225 GLU   C CB  
5566  C  CG  . GLU   C  227 ? 2.2665 1.7984 2.1722 -0.1604 0.0297  -0.0150 225 GLU   C CG  
5567  C  CD  . GLU   C  227 ? 2.3039 1.8313 2.1994 -0.1418 0.0136  -0.0042 225 GLU   C CD  
5568  O  OE1 . GLU   C  227 ? 2.3629 1.8242 2.2270 -0.1077 0.0282  0.0330  225 GLU   C OE1 
5569  O  OE2 . GLU   C  227 ? 2.3423 1.8251 2.3155 -0.1902 0.0734  -0.0246 225 GLU   C OE2 
5570  N  N   . GLU   C  228 ? 2.2284 1.5743 1.9458 -0.2164 -0.0824 0.0993  226 GLU   C N   
5571  C  CA  . GLU   C  228 ? 2.2463 1.4694 1.9032 -0.2279 -0.0997 0.1554  226 GLU   C CA  
5572  C  C   . GLU   C  228 ? 2.2222 1.4841 1.8216 -0.2272 -0.1076 0.1756  226 GLU   C C   
5573  O  O   . GLU   C  228 ? 2.2084 1.5368 1.8499 -0.2059 -0.1175 0.1682  226 GLU   C O   
5574  C  CB  . GLU   C  228 ? 2.2181 1.4061 1.8968 -0.1621 -0.1331 0.1355  226 GLU   C CB  
5575  C  CG  . GLU   C  228 ? 2.2384 1.3585 1.8833 -0.1349 -0.1270 0.2084  226 GLU   C CG  
5576  C  CD  . GLU   C  228 ? 2.2141 1.3200 1.8331 -0.0607 -0.1624 0.2398  226 GLU   C CD  
5577  O  OE1 . GLU   C  228 ? 2.2431 1.0129 1.7761 -0.1288 -0.1857 0.3546  226 GLU   C OE1 
5578  O  OE2 . GLU   C  228 ? 2.3330 1.1790 1.7637 -0.0527 -0.1286 0.2255  226 GLU   C OE2 
5579  N  N   . ILE   C  229 ? 2.2169 1.4455 1.8100 -0.2334 -0.0731 0.1880  227 ILE   C N   
5580  C  CA  . ILE   C  229 ? 2.2024 1.4256 1.8447 -0.2252 -0.1344 0.1658  227 ILE   C CA  
5581  C  C   . ILE   C  229 ? 2.1570 1.4390 1.8560 -0.2104 -0.1528 0.1859  227 ILE   C C   
5582  O  O   . ILE   C  229 ? 2.1575 1.4968 1.8702 -0.2208 -0.2559 0.2085  227 ILE   C O   
5583  C  CB  . ILE   C  229 ? 2.2089 1.4455 1.8495 -0.2453 -0.1717 0.1204  227 ILE   C CB  
5584  C  CG1 . ILE   C  229 ? 2.2270 1.4769 1.8145 -0.2354 -0.1785 0.1248  227 ILE   C CG1 
5585  C  CG2 . ILE   C  229 ? 2.1639 1.3792 1.8224 -0.2835 -0.1701 0.1598  227 ILE   C CG2 
5586  C  CD1 . ILE   C  229 ? 2.2114 1.5863 1.8160 -0.2058 -0.2099 0.0539  227 ILE   C CD1 
5587  N  N   . ASN   C  230 ? 2.1633 1.4960 1.8870 -0.1939 -0.0891 0.1571  228 ASN   C N   
5588  C  CA  . ASN   C  230 ? 2.1793 1.5066 1.9000 -0.1817 -0.0716 0.1845  228 ASN   C CA  
5589  C  C   . ASN   C  230 ? 2.2132 1.5463 1.8695 -0.2072 -0.0921 0.1202  228 ASN   C C   
5590  O  O   . ASN   C  230 ? 2.2677 1.5337 1.8763 -0.1829 -0.1043 0.0645  228 ASN   C O   
5591  C  CB  . ASN   C  230 ? 2.1794 1.5601 1.9422 -0.1719 -0.0216 0.1979  228 ASN   C CB  
5592  C  CG  . ASN   C  230 ? 2.1255 1.5746 1.9745 -0.1813 -0.0087 0.2227  228 ASN   C CG  
5593  O  OD1 . ASN   C  230 ? 2.1177 1.5716 2.0529 -0.1880 -0.0241 0.2425  228 ASN   C OD1 
5594  N  ND2 . ASN   C  230 ? 2.1143 1.6318 1.9471 -0.1903 0.0247  0.2144  228 ASN   C ND2 
5595  N  N   . GLN   C  231 ? 2.1940 1.5092 1.8893 -0.2281 -0.0894 0.1351  229 GLN   C N   
5596  C  CA  . GLN   C  231 ? 2.2520 1.5344 1.8967 -0.2639 -0.1206 0.0844  229 GLN   C CA  
5597  C  C   . GLN   C  231 ? 2.2363 1.5928 1.9295 -0.2951 -0.0787 0.1043  229 GLN   C C   
5598  O  O   . GLN   C  231 ? 2.3472 1.7057 1.9104 -0.2940 -0.1572 0.1086  229 GLN   C O   
5599  C  CB  . GLN   C  231 ? 2.1596 1.5476 1.9105 -0.1974 -0.1222 0.0629  229 GLN   C CB  
5600  C  CG  . GLN   C  231 ? 2.1537 1.6126 1.9411 -0.1822 -0.1318 0.0185  229 GLN   C CG  
5601  C  CD  . GLN   C  231 ? 2.1068 1.6610 1.9406 -0.1077 -0.1174 -0.0417 229 GLN   C CD  
5602  O  OE1 . GLN   C  231 ? 2.1448 1.6604 1.8767 -0.0622 -0.1487 -0.0975 229 GLN   C OE1 
5603  N  NE2 . GLN   C  231 ? 2.0880 1.7337 2.0002 -0.0830 -0.0894 -0.0722 229 GLN   C NE2 
5604  N  N   . TYR   C  232 ? 2.4049 1.5268 1.9240 -0.3269 -0.0879 0.2067  230 TYR   C N   
5605  C  CA  . TYR   C  232 ? 2.4278 1.5158 1.9509 -0.2983 -0.0788 0.2733  230 TYR   C CA  
5606  C  C   . TYR   C  232 ? 2.4499 1.5161 2.0370 -0.3392 -0.0783 0.2810  230 TYR   C C   
5607  O  O   . TYR   C  232 ? 2.4482 1.6523 2.1570 -0.2493 -0.0714 0.2731  230 TYR   C O   
5608  C  CB  . TYR   C  232 ? 2.4228 1.4433 1.9334 -0.2926 -0.1087 0.2594  230 TYR   C CB  
5609  C  CG  . TYR   C  232 ? 2.3705 1.3844 1.8685 -0.2624 -0.1232 0.3225  230 TYR   C CG  
5610  C  CD1 . TYR   C  232 ? 2.4033 1.4091 1.7926 -0.2736 -0.1459 0.3493  230 TYR   C CD1 
5611  C  CD2 . TYR   C  232 ? 2.3898 1.3452 1.8395 -0.2751 -0.0980 0.3253  230 TYR   C CD2 
5612  C  CE1 . TYR   C  232 ? 2.4242 1.3420 1.7453 -0.1970 -0.1471 0.3570  230 TYR   C CE1 
5613  C  CE2 . TYR   C  232 ? 2.4143 1.3021 1.7728 -0.2083 -0.1092 0.3215  230 TYR   C CE2 
5614  C  CZ  . TYR   C  232 ? 2.4370 1.3766 1.7517 -0.1603 -0.1262 0.3800  230 TYR   C CZ  
5615  O  OH  . TYR   C  232 ? 2.4929 1.2686 1.7341 -0.1375 -0.0746 0.4737  230 TYR   C OH  
5616  N  N   . VAL   C  233 ? 2.4209 1.4239 2.0852 -0.3488 -0.0876 0.2944  231 VAL   C N   
5617  C  CA  . VAL   C  233 ? 2.4479 1.3769 2.1675 -0.2788 -0.0825 0.2966  231 VAL   C CA  
5618  C  C   . VAL   C  233 ? 2.4370 1.2978 2.1865 -0.2949 -0.1114 0.2790  231 VAL   C C   
5619  O  O   . VAL   C  233 ? 2.4204 1.4443 2.3281 -0.2056 -0.1494 0.3596  231 VAL   C O   
5620  C  CB  . VAL   C  233 ? 2.4409 1.3818 2.1484 -0.2597 -0.0571 0.2760  231 VAL   C CB  
5621  C  CG1 . VAL   C  233 ? 2.4507 1.3628 2.1336 -0.2223 -0.0395 0.2708  231 VAL   C CG1 
5622  C  CG2 . VAL   C  233 ? 2.4282 1.4557 2.1351 -0.2677 -0.0176 0.2751  231 VAL   C CG2 
5623  N  N   . THR   C  234 ? 2.4445 1.1639 2.0856 -0.3081 -0.1649 0.2317  232 THR   C N   
5624  C  CA  . THR   C  234 ? 2.4137 1.2456 1.9495 -0.2471 -0.1684 0.1857  232 THR   C CA  
5625  C  C   . THR   C  234 ? 2.4662 1.3111 1.9023 -0.3161 -0.2168 0.1530  232 THR   C C   
5626  O  O   . THR   C  234 ? 2.5027 1.4153 1.9092 -0.2551 -0.2524 0.2446  232 THR   C O   
5627  C  CB  . THR   C  234 ? 2.4422 1.2531 1.9421 -0.2641 -0.1415 0.1446  232 THR   C CB  
5628  O  OG1 . THR   C  234 ? 2.3762 1.1793 1.9398 -0.2354 -0.0855 0.1347  232 THR   C OG1 
5629  C  CG2 . THR   C  234 ? 2.4302 1.3174 1.9135 -0.2381 -0.1213 0.1496  232 THR   C CG2 
5630  N  N   . GLN   C  235 ? 2.5117 1.1620 1.8042 -0.2710 -0.2268 0.2339  233 GLN   C N   
5631  C  CA  . GLN   C  235 ? 2.5503 1.2510 1.8210 -0.3182 -0.2591 0.2332  233 GLN   C CA  
5632  C  C   . GLN   C  235 ? 2.5483 1.3355 1.8407 -0.3465 -0.2239 0.1556  233 GLN   C C   
5633  O  O   . GLN   C  235 ? 2.6029 1.5623 1.8092 -0.2860 -0.3719 0.1017  233 GLN   C O   
5634  C  CB  . GLN   C  235 ? 2.5149 1.2515 1.8079 -0.3016 -0.2784 0.2291  233 GLN   C CB  
5635  C  CG  . GLN   C  235 ? 2.5499 1.3145 1.8306 -0.2955 -0.3074 0.2172  233 GLN   C CG  
5636  C  CD  . GLN   C  235 ? 2.5179 1.3342 1.8898 -0.2989 -0.3900 0.1282  233 GLN   C CD  
5637  O  OE1 . GLN   C  235 ? 2.5175 1.4021 1.9362 -0.2232 -0.4626 0.0442  233 GLN   C OE1 
5638  N  NE2 . GLN   C  235 ? 2.4909 1.3799 1.9333 -0.2649 -0.4115 0.1000  233 GLN   C NE2 
5639  N  N   . ILE   C  236 ? 2.5055 1.2796 1.8589 -0.3864 -0.2000 0.2542  234 ILE   C N   
5640  C  CA  . ILE   C  236 ? 2.4666 1.3713 1.9273 -0.3863 -0.1522 0.2890  234 ILE   C CA  
5641  C  C   . ILE   C  236 ? 2.5227 1.3518 2.0069 -0.3524 -0.1577 0.3396  234 ILE   C C   
5642  O  O   . ILE   C  236 ? 2.5158 1.1780 2.0385 -0.4399 -0.1729 0.4007  234 ILE   C O   
5643  C  CB  . ILE   C  236 ? 2.4348 1.3756 1.9353 -0.3391 -0.1280 0.2878  234 ILE   C CB  
5644  C  CG1 . ILE   C  236 ? 2.4366 1.3383 1.9343 -0.3033 -0.1096 0.2436  234 ILE   C CG1 
5645  C  CG2 . ILE   C  236 ? 2.4238 1.4339 1.9548 -0.3092 -0.1262 0.2860  234 ILE   C CG2 
5646  C  CD1 . ILE   C  236 ? 2.4155 1.3509 1.9229 -0.2846 -0.0690 0.2318  234 ILE   C CD1 
5647  N  N   . GLU   C  237 ? 2.5496 1.4704 2.1127 -0.3986 -0.1619 0.2973  235 GLU   C N   
5648  C  CA  . GLU   C  237 ? 2.5470 1.5411 2.1581 -0.4920 -0.1714 0.2737  235 GLU   C CA  
5649  C  C   . GLU   C  237 ? 2.5908 1.7002 2.1112 -0.5719 -0.0897 0.2751  235 GLU   C C   
5650  O  O   . GLU   C  237 ? 2.6586 1.6494 2.2128 -0.6724 -0.1203 0.2825  235 GLU   C O   
5651  C  CB  . GLU   C  237 ? 2.5515 1.5549 2.2089 -0.4694 -0.1967 0.2103  235 GLU   C CB  
5652  C  CG  . GLU   C  237 ? 2.5119 1.5344 2.1986 -0.4512 -0.2461 0.1338  235 GLU   C CG  
5653  C  CD  . GLU   C  237 ? 2.5168 1.6129 2.2342 -0.4397 -0.2538 0.0544  235 GLU   C CD  
5654  O  OE1 . GLU   C  237 ? 2.6096 1.7481 2.2464 -0.3179 -0.1826 -0.0143 235 GLU   C OE1 
5655  O  OE2 . GLU   C  237 ? 2.5180 1.6428 2.2756 -0.4792 -0.2417 -0.0008 235 GLU   C OE2 
5656  N  N   . GLN   C  238 ? 2.5624 1.8484 1.9192 -0.6099 -0.0086 0.3704  236 GLN   C N   
5657  C  CA  . GLN   C  238 ? 2.6046 2.0188 1.8338 -0.5832 -0.0045 0.3009  236 GLN   C CA  
5658  C  C   . GLN   C  238 ? 2.6088 2.1337 1.6813 -0.6057 -0.0018 0.3277  236 GLN   C C   
5659  O  O   . GLN   C  238 ? 2.6778 2.2490 1.6463 -0.5739 -0.0312 0.3705  236 GLN   C O   
5660  C  CB  . GLN   C  238 ? 2.6799 2.0112 1.8628 -0.5936 -0.0101 0.2473  236 GLN   C CB  
5661  C  CG  . GLN   C  238 ? 2.6757 2.0076 1.9292 -0.5806 0.0101  0.1754  236 GLN   C CG  
5662  C  CD  . GLN   C  238 ? 2.7220 1.9889 1.9878 -0.6395 0.0180  0.0994  236 GLN   C CD  
5663  O  OE1 . GLN   C  238 ? 2.7276 1.9122 2.0961 -0.6983 0.0337  0.1503  236 GLN   C OE1 
5664  N  NE2 . GLN   C  238 ? 2.7163 2.0989 2.0461 -0.6165 0.0254  0.0479  236 GLN   C NE2 
5665  N  N   . GLU   C  239 ? 2.5649 2.0659 1.5910 -0.5681 -0.0432 0.3157  237 GLU   C N   
5666  C  CA  . GLU   C  239 ? 2.5894 2.0575 1.6509 -0.5491 -0.1027 0.2911  237 GLU   C CA  
5667  C  C   . GLU   C  239 ? 2.5801 2.0613 1.8105 -0.4407 -0.0886 0.3252  237 GLU   C C   
5668  O  O   . GLU   C  239 ? 2.5167 2.1901 1.6860 -0.4779 -0.1155 0.3272  237 GLU   C O   
5669  C  CB  . GLU   C  239 ? 2.5515 1.9895 1.6377 -0.5314 -0.1723 0.2105  237 GLU   C CB  
5670  C  CG  . GLU   C  239 ? 2.5170 2.0050 1.6116 -0.5567 -0.1862 0.1938  237 GLU   C CG  
5671  C  CD  . GLU   C  239 ? 2.4650 1.9442 1.6311 -0.5368 -0.2313 0.1244  237 GLU   C CD  
5672  O  OE1 . GLU   C  239 ? 2.4420 1.9433 1.6471 -0.6006 -0.2904 0.0933  237 GLU   C OE1 
5673  O  OE2 . GLU   C  239 ? 2.4079 1.7949 1.6157 -0.6503 -0.2263 0.0790  237 GLU   C OE2 
5674  N  N   . LYS   C  240 ? 2.5612 1.9817 1.8765 -0.3736 -0.1428 0.3093  238 LYS   C N   
5675  C  CA  . LYS   C  240 ? 2.5560 1.8599 1.9891 -0.3165 -0.1221 0.3563  238 LYS   C CA  
5676  C  C   . LYS   C  240 ? 2.5710 1.8855 2.0560 -0.2691 -0.0464 0.4083  238 LYS   C C   
5677  O  O   . LYS   C  240 ? 2.6012 1.8946 2.2668 -0.2550 -0.0245 0.3817  238 LYS   C O   
5678  C  CB  . LYS   C  240 ? 2.5267 1.7714 1.9733 -0.3187 -0.1139 0.3124  238 LYS   C CB  
5679  C  CG  . LYS   C  240 ? 2.5449 1.7559 1.9207 -0.3130 -0.1436 0.3319  238 LYS   C CG  
5680  C  CD  . LYS   C  240 ? 2.5559 1.7726 1.9272 -0.3212 -0.1650 0.3150  238 LYS   C CD  
5681  C  CE  . LYS   C  240 ? 2.5859 1.7740 1.9368 -0.3030 -0.2146 0.2889  238 LYS   C CE  
5682  N  NZ  . LYS   C  240 ? 2.5770 1.8049 1.9741 -0.2930 -0.2604 0.2352  238 LYS   C NZ  
5683  N  N   . GLN   C  241 ? 2.6092 1.9837 1.9619 -0.1623 0.0087  0.5082  239 GLN   C N   
5684  C  CA  . GLN   C  241 ? 2.5994 2.1193 1.8891 -0.1310 0.0994  0.6205  239 GLN   C CA  
5685  C  C   . GLN   C  241 ? 2.5096 2.1634 1.8601 -0.1731 0.1437  0.6129  239 GLN   C C   
5686  O  O   . GLN   C  241 ? 2.4717 2.0109 1.8635 -0.2943 0.2190  0.6843  239 GLN   C O   
5687  C  CB  . GLN   C  241 ? 2.6131 2.1690 1.8007 -0.0379 0.1252  0.6749  239 GLN   C CB  
5688  C  CG  . GLN   C  241 ? 2.6500 2.1853 1.7579 0.0496  0.1198  0.6960  239 GLN   C CG  
5689  C  CD  . GLN   C  241 ? 2.6981 2.2242 1.7516 0.1300  0.1585  0.6768  239 GLN   C CD  
5690  O  OE1 . GLN   C  241 ? 2.7571 2.2202 1.6317 0.2556  0.0838  0.6730  239 GLN   C OE1 
5691  N  NE2 . GLN   C  241 ? 2.6843 2.2549 1.7861 0.1675  0.1544  0.6788  239 GLN   C NE2 
5692  N  N   . GLU   C  242 ? 2.4623 2.2982 1.9419 -0.1671 0.0571  0.6093  240 GLU   C N   
5693  C  CA  . GLU   C  242 ? 2.4043 2.3617 1.9933 -0.1671 0.0368  0.5482  240 GLU   C CA  
5694  C  C   . GLU   C  242 ? 2.3892 2.4290 2.0975 -0.1257 0.0429  0.5441  240 GLU   C C   
5695  O  O   . GLU   C  242 ? 2.4165 2.5389 2.1141 -0.0584 0.0673  0.5529  240 GLU   C O   
5696  C  CB  . GLU   C  242 ? 2.3759 2.3510 1.9057 -0.1492 -0.0120 0.5182  240 GLU   C CB  
5697  C  CG  . GLU   C  242 ? 2.3807 2.3847 1.9032 -0.1916 -0.0250 0.5362  240 GLU   C CG  
5698  C  CD  . GLU   C  242 ? 2.3419 2.4480 1.8513 -0.2149 -0.0238 0.5639  240 GLU   C CD  
5699  O  OE1 . GLU   C  242 ? 2.3889 2.6253 1.8479 -0.2867 0.0246  0.5164  240 GLU   C OE1 
5700  O  OE2 . GLU   C  242 ? 2.3071 2.4517 1.8334 -0.2396 -0.0228 0.5637  240 GLU   C OE2 
5701  N  N   . ASP   D  9   ? 2.2673 1.5048 2.0461 -0.2194 -0.2398 -0.1898 1   ASP   D N   
5702  C  CA  . ASP   D  9   ? 2.3197 1.3767 2.0368 -0.1987 -0.2625 -0.2087 1   ASP   D CA  
5703  C  C   . ASP   D  9   ? 2.3828 1.2970 1.9940 -0.2451 -0.3185 -0.1765 1   ASP   D C   
5704  O  O   . ASP   D  9   ? 2.5268 1.5467 1.9526 -0.1459 -0.4047 -0.2230 1   ASP   D O   
5705  C  CB  . ASP   D  9   ? 2.3293 1.1817 2.1305 -0.1818 -0.1790 -0.1522 1   ASP   D CB  
5706  C  CG  . ASP   D  9   ? 2.3052 1.0179 2.0452 -0.1087 -0.1154 -0.1365 1   ASP   D CG  
5707  O  OD1 . ASP   D  9   ? 2.2720 1.0370 2.2476 -0.0891 -0.1748 -0.0569 1   ASP   D OD1 
5708  O  OD2 . ASP   D  9   ? 2.3818 0.7377 2.0092 -0.0898 -0.0723 -0.0266 1   ASP   D OD2 
5709  N  N   . ARG   D  10  ? 2.3772 1.1949 1.9726 -0.1954 -0.3169 -0.0969 2   ARG   D N   
5710  C  CA  . ARG   D  10  ? 2.2814 1.1682 1.9415 -0.0949 -0.3373 -0.0698 2   ARG   D CA  
5711  C  C   . ARG   D  10  ? 2.1929 1.1024 1.8284 -0.0134 -0.3120 -0.0043 2   ARG   D C   
5712  O  O   . ARG   D  10  ? 2.2366 1.1202 1.9036 0.1225  -0.2776 -0.0952 2   ARG   D O   
5713  C  CB  . ARG   D  10  ? 2.3140 0.9444 1.9789 -0.1437 -0.3078 -0.1328 2   ARG   D CB  
5714  C  CG  . ARG   D  10  ? 2.3350 0.9347 1.9736 -0.1277 -0.2851 -0.1652 2   ARG   D CG  
5715  C  CD  . ARG   D  10  ? 2.3794 0.8628 2.0741 -0.1298 -0.2634 -0.1427 2   ARG   D CD  
5716  N  NE  . ARG   D  10  ? 2.4216 0.9373 2.0896 -0.1485 -0.2538 -0.1795 2   ARG   D NE  
5717  C  CZ  . ARG   D  10  ? 2.4147 1.0538 2.1597 -0.0892 -0.2596 -0.1474 2   ARG   D CZ  
5718  N  NH1 . ARG   D  10  ? 2.4009 1.1224 2.1662 -0.0689 -0.2400 -0.2216 2   ARG   D NH1 
5719  N  NH2 . ARG   D  10  ? 2.4185 1.1863 2.1789 -0.1114 -0.2538 -0.2101 2   ARG   D NH2 
5720  N  N   . GLY   D  11  ? 2.0732 1.0755 1.7358 0.0534  -0.3568 -0.0027 3   GLY   D N   
5721  C  CA  . GLY   D  11  ? 1.9577 1.0608 1.6194 0.0729  -0.3377 0.0277  3   GLY   D CA  
5722  C  C   . GLY   D  11  ? 1.9314 0.9706 1.5668 0.0947  -0.3021 0.0479  3   GLY   D C   
5723  O  O   . GLY   D  11  ? 1.9512 0.8712 1.5474 0.0285  -0.3292 0.0840  3   GLY   D O   
5724  N  N   . VAL   D  12  ? 1.8415 0.9513 1.4447 0.1402  -0.3127 0.0991  4   VAL   D N   
5725  C  CA  . VAL   D  12  ? 1.8362 0.9344 1.4002 0.1547  -0.2758 0.0501  4   VAL   D CA  
5726  C  C   . VAL   D  12  ? 1.8338 0.8698 1.3481 0.1932  -0.2407 -0.0035 4   VAL   D C   
5727  O  O   . VAL   D  12  ? 1.7937 0.9474 1.3089 0.2188  -0.2064 -0.0474 4   VAL   D O   
5728  C  CB  . VAL   D  12  ? 1.8310 1.0073 1.4087 0.1960  -0.2425 0.0630  4   VAL   D CB  
5729  C  CG1 . VAL   D  12  ? 1.8426 1.0806 1.4634 0.1693  -0.2632 0.0811  4   VAL   D CG1 
5730  C  CG2 . VAL   D  12  ? 1.7716 1.0220 1.4422 0.1704  -0.2927 0.0392  4   VAL   D CG2 
5731  N  N   . SER   D  13  ? 1.7700 0.8356 1.3580 0.2026  -0.2615 0.0000  5   SER   D N   
5732  C  CA  . SER   D  13  ? 1.7979 0.8721 1.4004 0.1637  -0.2598 0.0505  5   SER   D CA  
5733  C  C   . SER   D  13  ? 1.8552 0.8298 1.3913 0.1408  -0.2522 0.0723  5   SER   D C   
5734  O  O   . SER   D  13  ? 1.9120 1.0057 1.4673 0.0961  -0.2182 0.1442  5   SER   D O   
5735  C  CB  . SER   D  13  ? 1.7228 0.8661 1.3640 0.1765  -0.2396 0.0365  5   SER   D CB  
5736  O  OG  . SER   D  13  ? 1.6628 0.8345 1.4008 0.2227  -0.2211 0.0554  5   SER   D OG  
5737  N  N   . THR   D  14  ? 1.8447 0.8077 1.4151 0.1606  -0.2793 0.0297  6   THR   D N   
5738  C  CA  . THR   D  14  ? 1.8369 0.7066 1.4566 0.1397  -0.3095 0.0300  6   THR   D CA  
5739  C  C   . THR   D  14  ? 1.8126 0.6271 1.5304 0.1030  -0.2858 -0.0007 6   THR   D C   
5740  O  O   . THR   D  14  ? 1.8496 0.5914 1.5718 0.0609  -0.3354 -0.0375 6   THR   D O   
5741  C  CB  . THR   D  14  ? 1.8087 0.6955 1.4454 0.1611  -0.3254 -0.0078 6   THR   D CB  
5742  O  OG1 . THR   D  14  ? 1.8313 0.5698 1.4152 0.1709  -0.3440 -0.0233 6   THR   D OG1 
5743  C  CG2 . THR   D  14  ? 1.8607 0.8243 1.4224 0.1563  -0.3169 -0.0336 6   THR   D CG2 
5744  N  N   . PHE   D  15  ? 1.7830 0.6462 1.4888 0.0803  -0.3075 0.0244  7   PHE   D N   
5745  C  CA  . PHE   D  15  ? 1.7609 0.8178 1.5481 0.0979  -0.2856 -0.0011 7   PHE   D CA  
5746  C  C   . PHE   D  15  ? 1.8112 0.8251 1.6009 0.0995  -0.2854 -0.0288 7   PHE   D C   
5747  O  O   . PHE   D  15  ? 1.8443 0.9377 1.5662 0.1248  -0.3062 -0.0578 7   PHE   D O   
5748  C  CB  . PHE   D  15  ? 1.7554 0.8680 1.5485 0.1135  -0.2935 0.0253  7   PHE   D CB  
5749  C  CG  . PHE   D  15  ? 1.7528 0.8809 1.5759 0.0981  -0.2877 0.0545  7   PHE   D CG  
5750  C  CD1 . PHE   D  15  ? 1.7658 0.9589 1.6093 0.0761  -0.2966 0.0440  7   PHE   D CD1 
5751  C  CD2 . PHE   D  15  ? 1.7037 0.9733 1.5243 0.0945  -0.2969 0.1160  7   PHE   D CD2 
5752  C  CE1 . PHE   D  15  ? 1.7596 0.9526 1.5973 0.0618  -0.2795 0.1029  7   PHE   D CE1 
5753  C  CE2 . PHE   D  15  ? 1.6949 0.9721 1.5216 0.0835  -0.2777 0.1510  7   PHE   D CE2 
5754  C  CZ  . PHE   D  15  ? 1.7060 1.0031 1.5483 0.0625  -0.2889 0.1301  7   PHE   D CZ  
5755  N  N   . SER   D  16  ? 1.8576 0.7459 1.6198 0.1196  -0.2920 -0.0539 8   SER   D N   
5756  C  CA  . SER   D  16  ? 1.9184 0.7497 1.5924 0.1007  -0.2783 -0.1218 8   SER   D CA  
5757  C  C   . SER   D  16  ? 1.9510 0.6625 1.5664 0.1151  -0.2814 -0.1130 8   SER   D C   
5758  O  O   . SER   D  16  ? 1.9428 0.5353 1.4509 0.1230  -0.2978 -0.2335 8   SER   D O   
5759  C  CB  . SER   D  16  ? 1.9585 0.7110 1.6158 0.0873  -0.2946 -0.1231 8   SER   D CB  
5760  O  OG  . SER   D  16  ? 1.9829 0.6358 1.7250 0.0275  -0.2503 -0.1704 8   SER   D OG  
5761  N  N   . PRO   D  17  ? 1.9958 0.7102 1.5733 0.1729  -0.2356 -0.1668 9   PRO   D N   
5762  C  CA  . PRO   D  17  ? 2.0356 0.7646 1.5698 0.1637  -0.2072 -0.1530 9   PRO   D CA  
5763  C  C   . PRO   D  17  ? 2.0270 0.6949 1.5821 0.1298  -0.1479 -0.1101 9   PRO   D C   
5764  O  O   . PRO   D  17  ? 2.0689 0.5767 1.5907 0.1184  -0.1451 -0.0398 9   PRO   D O   
5765  C  CB  . PRO   D  17  ? 2.0479 0.8259 1.5878 0.0984  -0.2279 -0.2370 9   PRO   D CB  
5766  C  CG  . PRO   D  17  ? 2.0188 0.8493 1.5890 0.1082  -0.2485 -0.2564 9   PRO   D CG  
5767  C  CD  . PRO   D  17  ? 1.9875 0.7120 1.6249 0.1286  -0.2405 -0.2350 9   PRO   D CD  
5768  N  N   . GLU   D  18  ? 2.0529 0.7630 1.6147 0.1116  -0.1878 -0.1113 10  GLU   D N   
5769  C  CA  . GLU   D  18  ? 2.0614 0.8578 1.6917 0.1210  -0.2045 -0.0776 10  GLU   D CA  
5770  C  C   . GLU   D  18  ? 2.0529 0.8132 1.6685 0.2065  -0.2119 -0.0029 10  GLU   D C   
5771  O  O   . GLU   D  18  ? 1.9891 0.8339 1.7667 0.3017  -0.2067 0.0233  10  GLU   D O   
5772  C  CB  . GLU   D  18  ? 2.1525 0.8338 1.7352 0.0653  -0.2076 -0.0304 10  GLU   D CB  
5773  C  CG  . GLU   D  18  ? 2.2799 0.8362 1.7622 0.0384  -0.2212 -0.0206 10  GLU   D CG  
5774  C  CD  . GLU   D  18  ? 2.3232 0.8645 1.7812 -0.0053 -0.2228 0.0040  10  GLU   D CD  
5775  O  OE1 . GLU   D  18  ? 2.4551 0.9719 1.8167 -0.0647 -0.2461 -0.0358 10  GLU   D OE1 
5776  O  OE2 . GLU   D  18  ? 2.4301 0.6698 1.7293 0.0307  -0.2477 0.0007  10  GLU   D OE2 
5777  N  N   . GLY   D  19  ? 1.9928 0.9566 1.5712 0.2074  -0.2489 0.0527  11  GLY   D N   
5778  C  CA  . GLY   D  19  ? 1.9192 0.9689 1.5336 0.1763  -0.2665 0.0663  11  GLY   D CA  
5779  C  C   . GLY   D  19  ? 1.8304 0.9255 1.5411 0.1408  -0.3090 0.0598  11  GLY   D C   
5780  O  O   . GLY   D  19  ? 1.8121 0.9042 1.5364 0.1531  -0.3247 0.0954  11  GLY   D O   
5781  N  N   . ARG   D  20  ? 1.7885 0.9867 1.5086 0.1347  -0.3014 0.0080  12  ARG   D N   
5782  C  CA  . ARG   D  20  ? 1.7417 0.9695 1.5208 0.1318  -0.3031 -0.0107 12  ARG   D CA  
5783  C  C   . ARG   D  20  ? 1.7367 0.8885 1.3798 0.1258  -0.3288 -0.0450 12  ARG   D C   
5784  O  O   . ARG   D  20  ? 1.7276 0.8813 1.3333 0.1551  -0.3344 -0.0511 12  ARG   D O   
5785  C  CB  . ARG   D  20  ? 1.7516 0.9942 1.5768 0.1412  -0.3027 0.0247  12  ARG   D CB  
5786  C  CG  . ARG   D  20  ? 1.7663 1.0212 1.7002 0.1674  -0.2581 0.0321  12  ARG   D CG  
5787  C  CD  . ARG   D  20  ? 1.7364 1.0175 1.7714 0.2067  -0.2656 0.0812  12  ARG   D CD  
5788  N  NE  . ARG   D  20  ? 1.7213 1.1220 1.9386 0.2422  -0.2320 0.0722  12  ARG   D NE  
5789  C  CZ  . ARG   D  20  ? 1.8074 1.1332 2.1160 0.2194  -0.2022 0.0766  12  ARG   D CZ  
5790  N  NH1 . ARG   D  20  ? 1.7908 1.1916 2.2045 0.2285  -0.2345 0.0894  12  ARG   D NH1 
5791  N  NH2 . ARG   D  20  ? 1.8432 1.1747 2.2191 0.2472  -0.1387 0.0755  12  ARG   D NH2 
5792  N  N   . LEU   D  21  ? 1.6979 0.8833 1.3256 0.1079  -0.3409 -0.0305 13  LEU   D N   
5793  C  CA  . LEU   D  21  ? 1.6806 0.8823 1.2738 0.0820  -0.3467 -0.0275 13  LEU   D CA  
5794  C  C   . LEU   D  21  ? 1.6823 0.7786 1.3158 0.0621  -0.3637 -0.0416 13  LEU   D C   
5795  O  O   . LEU   D  21  ? 1.7181 0.7098 1.2969 0.0384  -0.3526 -0.0144 13  LEU   D O   
5796  C  CB  . LEU   D  21  ? 1.6623 0.9081 1.2526 0.0787  -0.3253 -0.0564 13  LEU   D CB  
5797  C  CG  . LEU   D  21  ? 1.6590 0.9881 1.2322 0.0543  -0.2806 -0.0665 13  LEU   D CG  
5798  C  CD1 . LEU   D  21  ? 1.6334 0.9901 1.2359 0.0554  -0.2776 -0.0720 13  LEU   D CD1 
5799  C  CD2 . LEU   D  21  ? 1.6525 1.0228 1.2390 0.0582  -0.2812 -0.0870 13  LEU   D CD2 
5800  N  N   . PHE   D  22  ? 1.6856 0.7681 1.3255 0.0605  -0.3806 -0.0141 14  PHE   D N   
5801  C  CA  . PHE   D  22  ? 1.6990 0.7851 1.3521 0.0634  -0.3757 0.0064  14  PHE   D CA  
5802  C  C   . PHE   D  22  ? 1.6856 0.7195 1.3859 0.0419  -0.3580 -0.0167 14  PHE   D C   
5803  O  O   . PHE   D  22  ? 1.7085 0.7368 1.3885 0.0676  -0.3569 -0.0347 14  PHE   D O   
5804  C  CB  . PHE   D  22  ? 1.6915 0.8392 1.3742 0.0745  -0.3885 0.0237  14  PHE   D CB  
5805  C  CG  . PHE   D  22  ? 1.7147 0.8546 1.3734 0.0992  -0.4049 0.0170  14  PHE   D CG  
5806  C  CD1 . PHE   D  22  ? 1.7359 0.8520 1.4390 0.1210  -0.4159 -0.0167 14  PHE   D CD1 
5807  C  CD2 . PHE   D  22  ? 1.7106 0.8347 1.3702 0.0948  -0.3930 0.0317  14  PHE   D CD2 
5808  C  CE1 . PHE   D  22  ? 1.7548 0.8735 1.4225 0.1312  -0.4266 -0.0169 14  PHE   D CE1 
5809  C  CE2 . PHE   D  22  ? 1.7398 0.8651 1.3761 0.0988  -0.3931 0.0137  14  PHE   D CE2 
5810  C  CZ  . PHE   D  22  ? 1.7521 0.8837 1.4173 0.1381  -0.4184 -0.0100 14  PHE   D CZ  
5811  N  N   . GLN   D  23  ? 1.6715 0.6847 1.3391 0.0241  -0.3745 0.0771  15  GLN   D N   
5812  C  CA  . GLN   D  23  ? 1.6626 0.6828 1.3345 0.0420  -0.3624 0.1040  15  GLN   D CA  
5813  C  C   . GLN   D  23  ? 1.6707 0.7212 1.3444 0.0206  -0.3633 0.1109  15  GLN   D C   
5814  O  O   . GLN   D  23  ? 1.7060 0.7849 1.3384 -0.0019 -0.3773 0.0587  15  GLN   D O   
5815  C  CB  . GLN   D  23  ? 1.6276 0.6865 1.3321 0.0317  -0.3589 0.1058  15  GLN   D CB  
5816  C  CG  . GLN   D  23  ? 1.6415 0.6799 1.3656 0.0225  -0.3708 0.0856  15  GLN   D CG  
5817  C  CD  . GLN   D  23  ? 1.6244 0.6635 1.3916 0.0086  -0.3740 0.0840  15  GLN   D CD  
5818  O  OE1 . GLN   D  23  ? 1.5867 0.6585 1.4720 0.0208  -0.4210 0.0580  15  GLN   D OE1 
5819  N  NE2 . GLN   D  23  ? 1.6333 0.6871 1.3978 0.0104  -0.3701 0.0753  15  GLN   D NE2 
5820  N  N   . VAL   D  24  ? 1.6968 0.7667 1.3363 0.0289  -0.3409 0.1363  16  VAL   D N   
5821  C  CA  . VAL   D  24  ? 1.6969 0.8159 1.3584 0.0152  -0.3353 0.1209  16  VAL   D CA  
5822  C  C   . VAL   D  24  ? 1.7184 0.8183 1.4415 0.0394  -0.3453 0.1069  16  VAL   D C   
5823  O  O   . VAL   D  24  ? 1.7459 0.8099 1.4570 0.0239  -0.3605 0.0784  16  VAL   D O   
5824  C  CB  . VAL   D  24  ? 1.7189 0.8328 1.3425 0.0432  -0.3096 0.1317  16  VAL   D CB  
5825  C  CG1 . VAL   D  24  ? 1.7152 0.8589 1.3362 0.0265  -0.2957 0.1353  16  VAL   D CG1 
5826  C  CG2 . VAL   D  24  ? 1.7030 0.8253 1.3480 0.0363  -0.2911 0.1382  16  VAL   D CG2 
5827  N  N   . GLU   D  25  ? 1.6830 0.8187 1.4730 0.0707  -0.3768 0.0957  17  GLU   D N   
5828  C  CA  . GLU   D  25  ? 1.6726 0.8437 1.5181 0.0782  -0.3846 0.1303  17  GLU   D CA  
5829  C  C   . GLU   D  25  ? 1.6313 0.7323 1.5476 0.0690  -0.3659 0.0921  17  GLU   D C   
5830  O  O   . GLU   D  25  ? 1.6506 0.7244 1.4737 -0.0533 -0.3542 0.1164  17  GLU   D O   
5831  C  CB  . GLU   D  25  ? 1.7228 0.9450 1.5462 0.0684  -0.4208 0.0859  17  GLU   D CB  
5832  C  CG  . GLU   D  25  ? 1.7840 1.0510 1.6344 0.0463  -0.3775 0.1435  17  GLU   D CG  
5833  C  CD  . GLU   D  25  ? 1.8019 1.0834 1.7334 0.0095  -0.4031 0.1835  17  GLU   D CD  
5834  O  OE1 . GLU   D  25  ? 1.9256 1.0480 1.7868 -0.0066 -0.3680 0.2431  17  GLU   D OE1 
5835  O  OE2 . GLU   D  25  ? 1.8563 1.2599 1.8907 0.1655  -0.4053 0.2386  17  GLU   D OE2 
5836  N  N   . TYR   D  26  ? 1.6369 0.6307 1.4575 0.1585  -0.3915 0.1457  18  TYR   D N   
5837  C  CA  . TYR   D  26  ? 1.6381 0.6693 1.4626 0.1936  -0.3705 0.1505  18  TYR   D CA  
5838  C  C   . TYR   D  26  ? 1.6329 0.6271 1.5214 0.1870  -0.3605 0.1209  18  TYR   D C   
5839  O  O   . TYR   D  26  ? 1.6780 0.7000 1.5048 0.1953  -0.3376 0.1104  18  TYR   D O   
5840  C  CB  . TYR   D  26  ? 1.6505 0.6764 1.4240 0.2122  -0.3854 0.1433  18  TYR   D CB  
5841  C  CG  . TYR   D  26  ? 1.6893 0.6927 1.4470 0.2051  -0.3759 0.1183  18  TYR   D CG  
5842  C  CD1 . TYR   D  26  ? 1.6913 0.7285 1.4810 0.2115  -0.3726 0.0929  18  TYR   D CD1 
5843  C  CD2 . TYR   D  26  ? 1.6836 0.7132 1.4439 0.1922  -0.3714 0.0987  18  TYR   D CD2 
5844  C  CE1 . TYR   D  26  ? 1.7149 0.7833 1.4931 0.1981  -0.3665 0.0665  18  TYR   D CE1 
5845  C  CE2 . TYR   D  26  ? 1.6997 0.7393 1.4606 0.1819  -0.3745 0.0842  18  TYR   D CE2 
5846  C  CZ  . TYR   D  26  ? 1.7213 0.7659 1.4626 0.1876  -0.3681 0.0504  18  TYR   D CZ  
5847  O  OH  . TYR   D  26  ? 1.7634 0.8116 1.4744 0.1671  -0.3342 0.0107  18  TYR   D OH  
5848  N  N   . SER   D  27  ? 1.6219 0.6411 1.4918 0.1680  -0.3402 0.1849  19  SER   D N   
5849  C  CA  . SER   D  27  ? 1.6108 0.6525 1.4942 0.1666  -0.3276 0.1784  19  SER   D CA  
5850  C  C   . SER   D  27  ? 1.6130 0.5887 1.5159 0.1784  -0.3354 0.1505  19  SER   D C   
5851  O  O   . SER   D  27  ? 1.5805 0.4382 1.5238 0.1751  -0.3673 0.1252  19  SER   D O   
5852  C  CB  . SER   D  27  ? 1.5865 0.6594 1.4805 0.1664  -0.2997 0.1914  19  SER   D CB  
5853  O  OG  . SER   D  27  ? 1.5688 0.7094 1.5514 0.1384  -0.2821 0.1712  19  SER   D OG  
5854  N  N   . LEU   D  28  ? 1.6182 0.5973 1.5598 0.1961  -0.3321 0.1319  20  LEU   D N   
5855  C  CA  . LEU   D  28  ? 1.6062 0.6722 1.5866 0.1998  -0.3374 0.0982  20  LEU   D CA  
5856  C  C   . LEU   D  28  ? 1.6692 0.7225 1.6188 0.1921  -0.3313 0.1403  20  LEU   D C   
5857  O  O   . LEU   D  28  ? 1.6305 0.7058 1.6458 0.2202  -0.3220 0.1454  20  LEU   D O   
5858  C  CB  . LEU   D  28  ? 1.6190 0.6926 1.6051 0.2165  -0.3369 0.0425  20  LEU   D CB  
5859  C  CG  . LEU   D  28  ? 1.6136 0.6710 1.6293 0.2291  -0.3235 0.0230  20  LEU   D CG  
5860  C  CD1 . LEU   D  28  ? 1.6217 0.7221 1.6395 0.2808  -0.3160 0.0167  20  LEU   D CD1 
5861  C  CD2 . LEU   D  28  ? 1.6034 0.6583 1.6361 0.2277  -0.3211 -0.0002 20  LEU   D CD2 
5862  N  N   . GLU   D  29  ? 1.7008 0.7626 1.6026 0.1621  -0.3568 0.1646  21  GLU   D N   
5863  C  CA  . GLU   D  29  ? 1.7649 0.8084 1.5977 0.1479  -0.3446 0.1929  21  GLU   D CA  
5864  C  C   . GLU   D  29  ? 1.7521 0.7921 1.6145 0.1325  -0.3555 0.1623  21  GLU   D C   
5865  O  O   . GLU   D  29  ? 1.8458 0.8927 1.5958 0.0616  -0.4093 0.1664  21  GLU   D O   
5866  C  CB  . GLU   D  29  ? 1.7713 0.8278 1.5374 0.1274  -0.3206 0.2098  21  GLU   D CB  
5867  C  CG  . GLU   D  29  ? 1.8142 0.9326 1.5378 0.1129  -0.2803 0.1958  21  GLU   D CG  
5868  C  CD  . GLU   D  29  ? 1.7939 1.0353 1.5602 0.1368  -0.2453 0.1928  21  GLU   D CD  
5869  O  OE1 . GLU   D  29  ? 1.8924 1.2069 1.5479 0.1134  -0.1958 0.1883  21  GLU   D OE1 
5870  O  OE2 . GLU   D  29  ? 1.8248 1.1008 1.5784 0.1376  -0.2716 0.2230  21  GLU   D OE2 
5871  N  N   . ALA   D  30  ? 1.6873 0.8516 1.5985 0.1410  -0.4092 0.1648  22  ALA   D N   
5872  C  CA  . ALA   D  30  ? 1.6743 0.8586 1.5933 0.1189  -0.4340 0.1407  22  ALA   D CA  
5873  C  C   . ALA   D  30  ? 1.6905 0.7784 1.6350 0.1072  -0.4396 0.1195  22  ALA   D C   
5874  O  O   . ALA   D  30  ? 1.5902 0.6003 1.6451 0.1188  -0.4631 0.1528  22  ALA   D O   
5875  C  CB  . ALA   D  30  ? 1.6790 0.8771 1.5822 0.1163  -0.4405 0.1642  22  ALA   D CB  
5876  N  N   . ILE   D  31  ? 1.7527 0.7738 1.6115 0.0743  -0.4087 0.0870  23  ILE   D N   
5877  C  CA  . ILE   D  31  ? 1.7830 0.7740 1.5895 0.0672  -0.4206 0.1069  23  ILE   D CA  
5878  C  C   . ILE   D  31  ? 1.8608 0.7360 1.5870 0.0999  -0.4390 0.0636  23  ILE   D C   
5879  O  O   . ILE   D  31  ? 1.8292 0.8687 1.6032 0.1313  -0.5121 0.1498  23  ILE   D O   
5880  C  CB  . ILE   D  31  ? 1.7748 0.8378 1.5853 0.0288  -0.3989 0.0857  23  ILE   D CB  
5881  C  CG1 . ILE   D  31  ? 1.7267 0.8798 1.4924 0.0010  -0.4064 0.1210  23  ILE   D CG1 
5882  C  CG2 . ILE   D  31  ? 1.7578 0.7811 1.6161 0.0179  -0.3840 0.0902  23  ILE   D CG2 
5883  C  CD1 . ILE   D  31  ? 1.7029 0.9365 1.4538 -0.0009 -0.4059 0.1031  23  ILE   D CD1 
5884  N  N   . LYS   D  32  ? 1.8914 0.6977 1.5709 0.1174  -0.4417 0.0886  24  LYS   D N   
5885  C  CA  . LYS   D  32  ? 1.9357 0.6115 1.5556 0.1143  -0.4152 0.0510  24  LYS   D CA  
5886  C  C   . LYS   D  32  ? 1.9507 0.4982 1.4751 0.1484  -0.4743 0.0484  24  LYS   D C   
5887  O  O   . LYS   D  32  ? 1.9049 0.5733 1.4951 0.1334  -0.5330 0.0064  24  LYS   D O   
5888  C  CB  . LYS   D  32  ? 2.0077 0.6501 1.5809 0.1795  -0.3458 0.0495  24  LYS   D CB  
5889  C  CG  . LYS   D  32  ? 2.0502 0.7101 1.6301 0.1503  -0.3127 0.0862  24  LYS   D CG  
5890  C  CD  . LYS   D  32  ? 2.0964 0.8000 1.6139 0.1689  -0.2826 0.0441  24  LYS   D CD  
5891  C  CE  . LYS   D  32  ? 2.0871 0.7917 1.6023 0.1862  -0.2524 -0.0166 24  LYS   D CE  
5892  N  NZ  . LYS   D  32  ? 2.1003 0.9144 1.5873 0.2015  -0.2425 -0.0765 24  LYS   D NZ  
5893  N  N   . LEU   D  33  ? 1.9548 0.5591 1.4482 0.1270  -0.4569 0.0653  25  LEU   D N   
5894  C  CA  . LEU   D  33  ? 1.9876 0.6363 1.4670 0.0747  -0.4571 0.0895  25  LEU   D CA  
5895  C  C   . LEU   D  33  ? 2.0033 0.6546 1.4215 0.0091  -0.4632 0.1194  25  LEU   D C   
5896  O  O   . LEU   D  33  ? 1.9521 0.6030 1.4736 -0.0882 -0.4778 0.1854  25  LEU   D O   
5897  C  CB  . LEU   D  33  ? 1.9966 0.6618 1.4281 0.0553  -0.4609 0.0368  25  LEU   D CB  
5898  C  CG  . LEU   D  33  ? 2.0162 0.6838 1.4846 0.0590  -0.4500 -0.0104 25  LEU   D CG  
5899  C  CD1 . LEU   D  33  ? 2.0070 0.6437 1.4735 0.0572  -0.4259 -0.0384 25  LEU   D CD1 
5900  C  CD2 . LEU   D  33  ? 2.0109 0.6757 1.5094 0.0895  -0.4870 -0.0363 25  LEU   D CD2 
5901  N  N   . GLY   D  34  ? 2.0125 0.6767 1.4300 -0.0087 -0.4672 0.1308  26  GLY   D N   
5902  C  CA  . GLY   D  34  ? 1.9610 0.6831 1.3665 0.0588  -0.5174 0.1553  26  GLY   D CA  
5903  C  C   . GLY   D  34  ? 1.9768 0.6272 1.3897 0.0934  -0.5176 0.2030  26  GLY   D C   
5904  O  O   . GLY   D  34  ? 2.0027 0.5425 1.2645 0.1077  -0.6036 0.3470  26  GLY   D O   
5905  N  N   . SER   D  35  ? 1.9215 0.6189 1.3659 0.1028  -0.5421 0.2203  27  SER   D N   
5906  C  CA  . SER   D  35  ? 1.8946 0.5555 1.3497 0.1102  -0.5194 0.2363  27  SER   D CA  
5907  C  C   . SER   D  35  ? 1.8655 0.5387 1.3859 0.0997  -0.5286 0.1708  27  SER   D C   
5908  O  O   . SER   D  35  ? 1.8636 0.5998 1.3309 0.0492  -0.4864 0.1720  27  SER   D O   
5909  C  CB  . SER   D  35  ? 1.9027 0.6706 1.3039 0.1340  -0.5284 0.2493  27  SER   D CB  
5910  O  OG  . SER   D  35  ? 1.8917 0.6932 1.3001 0.1838  -0.4985 0.2511  27  SER   D OG  
5911  N  N   . THR   D  36  ? 1.8075 0.4688 1.3921 0.0513  -0.5018 0.1774  28  THR   D N   
5912  C  CA  . THR   D  36  ? 1.7957 0.6082 1.4284 0.0786  -0.4794 0.1770  28  THR   D CA  
5913  C  C   . THR   D  36  ? 1.7910 0.6307 1.4167 0.0952  -0.4758 0.1443  28  THR   D C   
5914  O  O   . THR   D  36  ? 1.8336 0.7913 1.4422 0.1260  -0.4454 0.1106  28  THR   D O   
5915  C  CB  . THR   D  36  ? 1.7933 0.5806 1.4697 0.0602  -0.4751 0.2008  28  THR   D CB  
5916  O  OG1 . THR   D  36  ? 1.7676 0.5914 1.5012 0.0274  -0.4775 0.2366  28  THR   D OG1 
5917  C  CG2 . THR   D  36  ? 1.7854 0.5687 1.4860 0.0583  -0.4785 0.1774  28  THR   D CG2 
5918  N  N   . ALA   D  37  ? 1.7583 0.5921 1.4113 0.1134  -0.4948 0.1487  29  ALA   D N   
5919  C  CA  . ALA   D  37  ? 1.7659 0.5904 1.4043 0.1257  -0.5136 0.1130  29  ALA   D CA  
5920  C  C   . ALA   D  37  ? 1.7769 0.5807 1.4555 0.1341  -0.5002 0.1200  29  ALA   D C   
5921  O  O   . ALA   D  37  ? 1.8143 0.4919 1.4354 0.1266  -0.5565 0.1333  29  ALA   D O   
5922  C  CB  . ALA   D  37  ? 1.7135 0.6281 1.3829 0.1464  -0.5094 0.0751  29  ALA   D CB  
5923  N  N   . ILE   D  38  ? 1.7461 0.6537 1.5447 0.1180  -0.5069 0.1099  30  ILE   D N   
5924  C  CA  . ILE   D  38  ? 1.7511 0.6708 1.6226 0.1180  -0.4802 0.1004  30  ILE   D CA  
5925  C  C   . ILE   D  38  ? 1.7302 0.6613 1.5959 0.1404  -0.4896 0.0748  30  ILE   D C   
5926  O  O   . ILE   D  38  ? 1.6987 0.5282 1.6587 0.1642  -0.5451 0.0478  30  ILE   D O   
5927  C  CB  . ILE   D  38  ? 1.7636 0.6829 1.6578 0.1107  -0.4720 0.1354  30  ILE   D CB  
5928  C  CG1 . ILE   D  38  ? 1.7894 0.7185 1.6937 0.0536  -0.4543 0.1263  30  ILE   D CG1 
5929  C  CG2 . ILE   D  38  ? 1.7690 0.7021 1.6897 0.1131  -0.4532 0.1221  30  ILE   D CG2 
5930  C  CD1 . ILE   D  38  ? 1.8097 0.7704 1.7043 0.0614  -0.4744 0.1401  30  ILE   D CD1 
5931  N  N   . GLY   D  39  ? 1.7615 0.6524 1.5966 0.1330  -0.4863 0.0900  31  GLY   D N   
5932  C  CA  . GLY   D  39  ? 1.7999 0.6340 1.5914 0.1387  -0.4740 0.0957  31  GLY   D CA  
5933  C  C   . GLY   D  39  ? 1.7980 0.6821 1.6036 0.1441  -0.4928 0.1228  31  GLY   D C   
5934  O  O   . GLY   D  39  ? 1.8435 0.6740 1.5730 0.1437  -0.4843 0.1476  31  GLY   D O   
5935  N  N   . ILE   D  40  ? 1.8071 0.7088 1.6209 0.1622  -0.5354 0.1331  32  ILE   D N   
5936  C  CA  . ILE   D  40  ? 1.8107 0.8273 1.6935 0.1638  -0.5298 0.0832  32  ILE   D CA  
5937  C  C   . ILE   D  40  ? 1.7904 0.8250 1.6753 0.1843  -0.5301 0.0975  32  ILE   D C   
5938  O  O   . ILE   D  40  ? 1.7994 0.9148 1.6500 0.2203  -0.5488 0.0778  32  ILE   D O   
5939  C  CB  . ILE   D  40  ? 1.8424 0.8020 1.7228 0.1478  -0.5705 0.0603  32  ILE   D CB  
5940  C  CG1 . ILE   D  40  ? 1.8843 0.7788 1.7405 0.1763  -0.5687 0.0112  32  ILE   D CG1 
5941  C  CG2 . ILE   D  40  ? 1.8482 0.8557 1.7951 0.1209  -0.5507 0.0280  32  ILE   D CG2 
5942  C  CD1 . ILE   D  40  ? 1.9163 0.7696 1.7404 0.1892  -0.5918 0.0002  32  ILE   D CD1 
5943  N  N   . ALA   D  41  ? 1.7724 0.8940 1.7218 0.2045  -0.4980 0.1028  33  ALA   D N   
5944  C  CA  . ALA   D  41  ? 1.7618 0.8822 1.7313 0.2227  -0.4952 0.1232  33  ALA   D CA  
5945  C  C   . ALA   D  41  ? 1.7581 0.9177 1.7662 0.2276  -0.4940 0.1043  33  ALA   D C   
5946  O  O   . ALA   D  41  ? 1.7312 1.0308 1.8307 0.2475  -0.4571 0.0635  33  ALA   D O   
5947  C  CB  . ALA   D  41  ? 1.7626 0.8824 1.7340 0.2213  -0.4785 0.1347  33  ALA   D CB  
5948  N  N   . THR   D  42  ? 1.8053 0.8812 1.7322 0.2380  -0.4768 0.1240  34  THR   D N   
5949  C  CA  . THR   D  42  ? 1.8151 0.8233 1.6857 0.2019  -0.4680 0.1696  34  THR   D CA  
5950  C  C   . THR   D  42  ? 1.8332 0.8150 1.6935 0.2378  -0.4547 0.2240  34  THR   D C   
5951  O  O   . THR   D  42  ? 1.8477 0.7044 1.6493 0.1548  -0.4023 0.3585  34  THR   D O   
5952  C  CB  . THR   D  42  ? 1.8165 0.8618 1.6901 0.1916  -0.5204 0.1663  34  THR   D CB  
5953  O  OG1 . THR   D  42  ? 1.7915 0.9550 1.5802 0.1956  -0.5606 0.1385  34  THR   D OG1 
5954  C  CG2 . THR   D  42  ? 1.8359 0.8220 1.6702 0.2185  -0.5257 0.1481  34  THR   D CG2 
5955  N  N   . LYS   D  43  ? 1.8674 0.7394 1.6899 0.2048  -0.4543 0.2035  35  LYS   D N   
5956  C  CA  . LYS   D  43  ? 1.9140 0.7703 1.7138 0.1560  -0.4295 0.1810  35  LYS   D CA  
5957  C  C   . LYS   D  43  ? 1.9281 0.8671 1.6850 0.1512  -0.4152 0.1790  35  LYS   D C   
5958  O  O   . LYS   D  43  ? 1.9865 0.8732 1.7827 0.1253  -0.3774 0.0743  35  LYS   D O   
5959  C  CB  . LYS   D  43  ? 1.9221 0.8146 1.7412 0.1781  -0.4107 0.1229  35  LYS   D CB  
5960  C  CG  . LYS   D  43  ? 1.9918 0.8793 1.7997 0.1790  -0.3778 0.0351  35  LYS   D CG  
5961  C  CD  . LYS   D  43  ? 2.0133 1.0294 1.8480 0.1479  -0.3410 -0.0470 35  LYS   D CD  
5962  C  CE  . LYS   D  43  ? 2.0664 1.1238 1.8597 0.1452  -0.3041 -0.1072 35  LYS   D CE  
5963  N  NZ  . LYS   D  43  ? 2.1136 1.0953 1.8861 0.1845  -0.2884 -0.0754 35  LYS   D NZ  
5964  N  N   . GLU   D  44  ? 1.8926 0.7583 1.7211 0.1843  -0.4282 0.1942  36  GLU   D N   
5965  C  CA  . GLU   D  44  ? 1.8191 0.7462 1.7726 0.2033  -0.4098 0.1727  36  GLU   D CA  
5966  C  C   . GLU   D  44  ? 1.8143 0.6442 1.7373 0.2175  -0.4393 0.1669  36  GLU   D C   
5967  O  O   . GLU   D  44  ? 1.8400 0.6302 1.7945 0.2306  -0.4019 0.1650  36  GLU   D O   
5968  C  CB  . GLU   D  44  ? 1.8119 0.8208 1.7275 0.1756  -0.4076 0.1665  36  GLU   D CB  
5969  C  CG  . GLU   D  44  ? 1.7991 0.9063 1.7753 0.1577  -0.3848 0.1344  36  GLU   D CG  
5970  C  CD  . GLU   D  44  ? 1.7421 0.9502 1.7754 0.1483  -0.3965 0.1332  36  GLU   D CD  
5971  O  OE1 . GLU   D  44  ? 1.7478 0.9719 1.8148 0.1213  -0.3592 0.0785  36  GLU   D OE1 
5972  O  OE2 . GLU   D  44  ? 1.7130 1.0562 1.8750 0.1053  -0.3345 0.0852  36  GLU   D OE2 
5973  N  N   . GLY   D  45  ? 1.8145 0.6091 1.7178 0.2412  -0.4460 0.1711  37  GLY   D N   
5974  C  CA  . GLY   D  45  ? 1.8213 0.6542 1.6870 0.2534  -0.4588 0.1702  37  GLY   D CA  
5975  C  C   . GLY   D  45  ? 1.7977 0.6593 1.6830 0.2599  -0.4777 0.1800  37  GLY   D C   
5976  O  O   . GLY   D  45  ? 1.8788 0.6806 1.7074 0.3309  -0.4886 0.2362  37  GLY   D O   
5977  N  N   . VAL   D  46  ? 1.7839 0.6854 1.6750 0.2094  -0.4653 0.1673  38  VAL   D N   
5978  C  CA  . VAL   D  46  ? 1.7851 0.6884 1.6933 0.1759  -0.4363 0.1867  38  VAL   D CA  
5979  C  C   . VAL   D  46  ? 1.7873 0.6530 1.6362 0.1864  -0.4555 0.1627  38  VAL   D C   
5980  O  O   . VAL   D  46  ? 1.8387 0.5407 1.5815 0.1448  -0.4817 0.1773  38  VAL   D O   
5981  C  CB  . VAL   D  46  ? 1.7818 0.7633 1.6977 0.1592  -0.4466 0.1711  38  VAL   D CB  
5982  C  CG1 . VAL   D  46  ? 1.7916 0.7452 1.7050 0.1498  -0.4298 0.1783  38  VAL   D CG1 
5983  C  CG2 . VAL   D  46  ? 1.7749 0.8181 1.7394 0.1479  -0.4168 0.1735  38  VAL   D CG2 
5984  N  N   . VAL   D  47  ? 1.7671 0.6578 1.6380 0.1657  -0.4663 0.1556  39  VAL   D N   
5985  C  CA  . VAL   D  47  ? 1.7594 0.6198 1.5741 0.1452  -0.4935 0.1154  39  VAL   D CA  
5986  C  C   . VAL   D  47  ? 1.7776 0.5428 1.5362 0.1345  -0.4461 0.0828  39  VAL   D C   
5987  O  O   . VAL   D  47  ? 1.7829 0.5355 1.4903 0.1145  -0.4869 0.0940  39  VAL   D O   
5988  C  CB  . VAL   D  47  ? 1.7797 0.5746 1.5745 0.1220  -0.5063 0.1110  39  VAL   D CB  
5989  C  CG1 . VAL   D  47  ? 1.7871 0.4746 1.5843 0.0958  -0.5240 0.0825  39  VAL   D CG1 
5990  C  CG2 . VAL   D  47  ? 1.7835 0.6595 1.5878 0.1190  -0.5232 0.1027  39  VAL   D CG2 
5991  N  N   . LEU   D  48  ? 1.7865 0.4800 1.5131 0.1232  -0.4344 0.0610  40  LEU   D N   
5992  C  CA  . LEU   D  48  ? 1.7780 0.4151 1.4805 0.1385  -0.4146 0.0538  40  LEU   D CA  
5993  C  C   . LEU   D  48  ? 1.7931 0.4267 1.4464 0.1270  -0.4194 0.0352  40  LEU   D C   
5994  O  O   . LEU   D  48  ? 1.7978 0.2013 1.5409 0.0877  -0.4283 0.0393  40  LEU   D O   
5995  C  CB  . LEU   D  48  ? 1.7735 0.4515 1.5028 0.1807  -0.3781 0.0459  40  LEU   D CB  
5996  C  CG  . LEU   D  48  ? 1.7688 0.4824 1.5056 0.2273  -0.3537 0.0763  40  LEU   D CG  
5997  C  CD1 . LEU   D  48  ? 1.7654 0.5092 1.5683 0.2513  -0.3389 0.0856  40  LEU   D CD1 
5998  C  CD2 . LEU   D  48  ? 1.7521 0.5408 1.4672 0.2455  -0.3761 0.1069  40  LEU   D CD2 
5999  N  N   . GLY   D  49  ? 1.7975 0.4316 1.4474 0.1129  -0.4353 0.0393  41  GLY   D N   
6000  C  CA  . GLY   D  49  ? 1.8049 0.3972 1.4266 0.0925  -0.4638 0.0238  41  GLY   D CA  
6001  C  C   . GLY   D  49  ? 1.8493 0.3556 1.3709 0.0920  -0.4593 0.0059  41  GLY   D C   
6002  O  O   . GLY   D  49  ? 1.7933 0.3344 1.3840 0.0655  -0.4542 -0.0182 41  GLY   D O   
6003  N  N   . VAL   D  50  ? 1.8803 0.4215 1.3492 0.0939  -0.4597 0.0441  42  VAL   D N   
6004  C  CA  . VAL   D  50  ? 1.8813 0.5397 1.3488 0.0871  -0.4993 0.0524  42  VAL   D CA  
6005  C  C   . VAL   D  50  ? 1.9159 0.5692 1.3806 0.0936  -0.5117 0.0891  42  VAL   D C   
6006  O  O   . VAL   D  50  ? 2.0040 0.6667 1.3707 0.1357  -0.4872 0.0877  42  VAL   D O   
6007  C  CB  . VAL   D  50  ? 1.8864 0.5680 1.3159 0.0953  -0.4869 0.0736  42  VAL   D CB  
6008  C  CG1 . VAL   D  50  ? 1.9027 0.5987 1.3098 0.0681  -0.4609 0.0601  42  VAL   D CG1 
6009  C  CG2 . VAL   D  50  ? 1.8782 0.5924 1.2714 0.0741  -0.4866 0.0919  42  VAL   D CG2 
6010  N  N   . GLU   D  51  ? 1.8832 0.6026 1.4217 0.0849  -0.5408 0.0714  43  GLU   D N   
6011  C  CA  . GLU   D  51  ? 1.8704 0.6546 1.4720 0.0944  -0.5209 0.1072  43  GLU   D CA  
6012  C  C   . GLU   D  51  ? 1.8908 0.6130 1.4308 0.1172  -0.4887 0.0888  43  GLU   D C   
6013  O  O   . GLU   D  51  ? 1.8284 0.6450 1.4809 0.1854  -0.4732 0.1228  43  GLU   D O   
6014  C  CB  . GLU   D  51  ? 1.9009 0.6473 1.5620 0.1074  -0.5129 0.1024  43  GLU   D CB  
6015  C  CG  . GLU   D  51  ? 1.9049 0.6882 1.6116 0.0972  -0.5050 0.1272  43  GLU   D CG  
6016  C  CD  . GLU   D  51  ? 1.9020 0.6693 1.6471 0.0688  -0.4924 0.1330  43  GLU   D CD  
6017  O  OE1 . GLU   D  51  ? 1.9255 0.7488 1.7515 0.0003  -0.4727 0.1363  43  GLU   D OE1 
6018  O  OE2 . GLU   D  51  ? 1.8951 0.7463 1.6334 0.1370  -0.5101 0.0934  43  GLU   D OE2 
6019  N  N   . LYS   D  52  ? 1.8843 0.5809 1.3967 0.1312  -0.5229 0.0889  44  LYS   D N   
6020  C  CA  . LYS   D  52  ? 1.9088 0.6065 1.4003 0.1462  -0.4712 0.1244  44  LYS   D CA  
6021  C  C   . LYS   D  52  ? 1.9495 0.5602 1.4781 0.1328  -0.4146 0.1393  44  LYS   D C   
6022  O  O   . LYS   D  52  ? 1.9351 0.4195 1.5067 0.1686  -0.3862 0.1390  44  LYS   D O   
6023  C  CB  . LYS   D  52  ? 1.9399 0.6622 1.3831 0.1067  -0.4786 0.1371  44  LYS   D CB  
6024  C  CG  . LYS   D  52  ? 1.9747 0.6603 1.3955 0.0842  -0.4487 0.1532  44  LYS   D CG  
6025  C  CD  . LYS   D  52  ? 2.0137 0.6689 1.3829 0.0405  -0.4575 0.1270  44  LYS   D CD  
6026  C  CE  . LYS   D  52  ? 2.0183 0.7294 1.3071 0.0238  -0.4687 0.0474  44  LYS   D CE  
6027  N  NZ  . LYS   D  52  ? 2.0387 0.7791 1.2848 -0.0093 -0.4912 0.0103  44  LYS   D NZ  
6028  N  N   . ARG   D  53  ? 1.9911 0.6476 1.5301 0.1388  -0.4136 0.2451  45  ARG   D N   
6029  C  CA  . ARG   D  53  ? 1.9566 0.7271 1.5788 0.0951  -0.4142 0.2510  45  ARG   D CA  
6030  C  C   . ARG   D  53  ? 1.9326 0.7434 1.5778 0.1300  -0.4664 0.2593  45  ARG   D C   
6031  O  O   . ARG   D  53  ? 1.8394 0.6846 1.6465 0.2036  -0.4448 0.2908  45  ARG   D O   
6032  C  CB  . ARG   D  53  ? 1.9755 0.7062 1.5578 0.0771  -0.4177 0.2867  45  ARG   D CB  
6033  C  CG  . ARG   D  53  ? 1.9907 0.7119 1.5653 0.0537  -0.4193 0.3278  45  ARG   D CG  
6034  C  CD  . ARG   D  53  ? 1.9839 0.7235 1.5447 0.0544  -0.4086 0.3849  45  ARG   D CD  
6035  N  NE  . ARG   D  53  ? 1.9598 0.6676 1.5989 0.0795  -0.4198 0.4281  45  ARG   D NE  
6036  C  CZ  . ARG   D  53  ? 1.9236 0.6799 1.6176 0.0660  -0.3977 0.3831  45  ARG   D CZ  
6037  N  NH1 . ARG   D  53  ? 1.8407 0.8127 1.6703 0.0183  -0.4185 0.3248  45  ARG   D NH1 
6038  N  NH2 . ARG   D  53  ? 1.9235 0.5034 1.6632 0.1121  -0.4246 0.4403  45  ARG   D NH2 
6039  N  N   . ALA   D  54  ? 1.8755 0.8719 1.6325 0.1267  -0.3833 0.1649  46  ALA   D N   
6040  C  CA  . ALA   D  54  ? 1.8340 0.9099 1.7544 0.0914  -0.4099 0.1024  46  ALA   D CA  
6041  C  C   . ALA   D  54  ? 1.8444 0.9555 1.8079 0.0773  -0.4160 -0.0130 46  ALA   D C   
6042  O  O   . ALA   D  54  ? 1.7647 0.8774 1.9368 0.0830  -0.4483 -0.1372 46  ALA   D O   
6043  C  CB  . ALA   D  54  ? 1.8613 1.0257 1.7552 0.0938  -0.3711 0.1062  46  ALA   D CB  
6044  N  N   . THR   D  55  ? 1.8644 0.9307 1.8286 0.0563  -0.4363 0.0189  47  THR   D N   
6045  C  CA  . THR   D  55  ? 1.9156 0.9287 1.8259 0.0214  -0.4109 0.0400  47  THR   D CA  
6046  C  C   . THR   D  55  ? 1.9705 0.7780 1.8687 -0.0521 -0.3856 0.0247  47  THR   D C   
6047  O  O   . THR   D  55  ? 1.8917 0.7890 1.7866 -0.0744 -0.3676 0.0314  47  THR   D O   
6048  C  CB  . THR   D  55  ? 1.9446 1.0046 1.8610 0.0458  -0.4475 0.0171  47  THR   D CB  
6049  O  OG1 . THR   D  55  ? 1.9270 1.1210 1.8963 0.0944  -0.4389 -0.0233 47  THR   D OG1 
6050  C  CG2 . THR   D  55  ? 1.9493 1.0483 1.8449 0.0561  -0.4405 -0.0053 47  THR   D CG2 
6051  N  N   . SER   D  56  ? 2.0274 0.7294 1.7658 -0.1009 -0.3009 0.1257  48  SER   D N   
6052  C  CA  . SER   D  56  ? 2.1191 0.5962 1.7811 -0.1117 -0.3554 0.2118  48  SER   D CA  
6053  C  C   . SER   D  56  ? 2.0593 0.5869 1.6722 -0.0678 -0.3900 0.3269  48  SER   D C   
6054  O  O   . SER   D  56  ? 2.0303 0.6835 1.7725 -0.1803 -0.3460 0.2928  48  SER   D O   
6055  C  CB  . SER   D  56  ? 2.1353 0.5889 1.8092 -0.1142 -0.3206 0.2262  48  SER   D CB  
6056  O  OG  . SER   D  56  ? 2.2851 0.5727 1.7959 -0.1215 -0.3314 0.2639  48  SER   D OG  
6057  N  N   . PRO   D  57  ? 2.0328 0.4986 1.7089 -0.0456 -0.4368 0.3332  49  PRO   D N   
6058  C  CA  . PRO   D  57  ? 2.0299 0.4545 1.6715 -0.0576 -0.4244 0.3631  49  PRO   D CA  
6059  C  C   . PRO   D  57  ? 2.0288 0.4260 1.5050 -0.1011 -0.4502 0.3620  49  PRO   D C   
6060  O  O   . PRO   D  57  ? 1.9984 0.4475 1.4862 -0.1103 -0.4327 0.3564  49  PRO   D O   
6061  C  CB  . PRO   D  57  ? 2.0615 0.4755 1.6841 -0.0126 -0.4498 0.3740  49  PRO   D CB  
6062  C  CG  . PRO   D  57  ? 2.0690 0.5006 1.7395 -0.0212 -0.4470 0.3581  49  PRO   D CG  
6063  C  CD  . PRO   D  57  ? 2.0588 0.4895 1.7394 -0.0229 -0.4471 0.3468  49  PRO   D CD  
6064  N  N   . LEU   D  58  ? 2.0386 0.4402 1.4359 -0.0644 -0.4355 0.3954  50  LEU   D N   
6065  C  CA  . LEU   D  58  ? 2.0846 0.5209 1.3794 -0.0554 -0.4059 0.3480  50  LEU   D CA  
6066  C  C   . LEU   D  58  ? 2.0930 0.5571 1.3190 -0.0564 -0.4006 0.3611  50  LEU   D C   
6067  O  O   . LEU   D  58  ? 2.1091 0.5164 1.2113 -0.0827 -0.3968 0.4119  50  LEU   D O   
6068  C  CB  . LEU   D  58  ? 2.0967 0.4792 1.3900 -0.0729 -0.3802 0.3657  50  LEU   D CB  
6069  C  CG  . LEU   D  58  ? 2.1311 0.4503 1.3967 -0.0634 -0.4113 0.3836  50  LEU   D CG  
6070  C  CD1 . LEU   D  58  ? 2.1356 0.4645 1.4414 -0.0728 -0.4117 0.3832  50  LEU   D CD1 
6071  C  CD2 . LEU   D  58  ? 2.1399 0.4551 1.3740 -0.0610 -0.4344 0.3974  50  LEU   D CD2 
6072  N  N   . LEU   D  59  ? 2.0788 0.6339 1.3196 -0.0039 -0.4134 0.3519  51  LEU   D N   
6073  C  CA  . LEU   D  59  ? 2.0230 0.6367 1.3051 0.0335  -0.4542 0.3685  51  LEU   D CA  
6074  C  C   . LEU   D  59  ? 1.9735 0.7200 1.3000 0.0747  -0.5149 0.3984  51  LEU   D C   
6075  O  O   . LEU   D  59  ? 1.9552 0.7125 1.3168 0.0394  -0.6228 0.3863  51  LEU   D O   
6076  C  CB  . LEU   D  59  ? 2.0274 0.6575 1.3009 0.0377  -0.4262 0.3772  51  LEU   D CB  
6077  C  CG  . LEU   D  59  ? 2.0240 0.6955 1.2737 0.0416  -0.3960 0.3416  51  LEU   D CG  
6078  C  CD1 . LEU   D  59  ? 2.0237 0.6972 1.2425 0.0452  -0.3821 0.3108  51  LEU   D CD1 
6079  C  CD2 . LEU   D  59  ? 2.0185 0.7096 1.2919 0.0459  -0.3876 0.3211  51  LEU   D CD2 
6080  N  N   . GLU   D  60  ? 1.9869 0.7512 1.2561 0.1012  -0.4991 0.3759  52  GLU   D N   
6081  C  CA  . GLU   D  60  ? 1.9707 0.8241 1.2245 0.1084  -0.5028 0.3559  52  GLU   D CA  
6082  C  C   . GLU   D  60  ? 1.9239 0.8950 1.2483 0.1221  -0.4922 0.3222  52  GLU   D C   
6083  O  O   . GLU   D  60  ? 1.8964 0.8263 1.2371 0.0926  -0.4277 0.3142  52  GLU   D O   
6084  C  CB  . GLU   D  60  ? 2.0403 0.8113 1.2330 0.1003  -0.4868 0.3437  52  GLU   D CB  
6085  C  CG  . GLU   D  60  ? 2.0794 0.8308 1.2355 0.0852  -0.4783 0.3762  52  GLU   D CG  
6086  C  CD  . GLU   D  60  ? 2.1035 0.8762 1.2596 0.0898  -0.4690 0.3401  52  GLU   D CD  
6087  O  OE1 . GLU   D  60  ? 2.1470 0.8534 1.2555 0.0600  -0.4751 0.3964  52  GLU   D OE1 
6088  O  OE2 . GLU   D  60  ? 2.0985 0.9177 1.3309 0.0358  -0.4576 0.3559  52  GLU   D OE2 
6089  N  N   . SER   D  61  ? 1.8877 0.9954 1.2222 0.1079  -0.5120 0.3230  53  SER   D N   
6090  C  CA  . SER   D  61  ? 1.8924 1.0239 1.2598 0.0572  -0.4876 0.2921  53  SER   D CA  
6091  C  C   . SER   D  61  ? 1.8718 0.9396 1.2570 0.0996  -0.5017 0.2245  53  SER   D C   
6092  O  O   . SER   D  61  ? 1.8623 0.9200 1.2701 0.0861  -0.4950 0.2358  53  SER   D O   
6093  C  CB  . SER   D  61  ? 1.8605 1.1197 1.2869 0.0650  -0.4981 0.2881  53  SER   D CB  
6094  O  OG  . SER   D  61  ? 1.8867 1.2437 1.3700 -0.0252 -0.4653 0.1855  53  SER   D OG  
6095  N  N   . ASP   D  62  ? 1.8788 0.9293 1.2674 0.1201  -0.4796 0.2185  54  ASP   D N   
6096  C  CA  . ASP   D  62  ? 1.8426 0.9085 1.2521 0.1754  -0.4785 0.2509  54  ASP   D CA  
6097  C  C   . ASP   D  62  ? 1.8489 0.6309 1.2328 0.1198  -0.4207 0.2726  54  ASP   D C   
6098  O  O   . ASP   D  62  ? 1.8013 0.5856 1.1577 0.2003  -0.5075 0.3269  54  ASP   D O   
6099  C  CB  . ASP   D  62  ? 1.9073 1.0928 1.2889 0.1638  -0.4138 0.1529  54  ASP   D CB  
6100  C  CG  . ASP   D  62  ? 1.9499 1.3032 1.3044 0.1745  -0.3694 0.0968  54  ASP   D CG  
6101  O  OD1 . ASP   D  62  ? 1.8972 1.5021 1.3694 0.1927  -0.3229 0.0603  54  ASP   D OD1 
6102  O  OD2 . ASP   D  62  ? 2.0149 1.4687 1.3274 0.1522  -0.3971 0.0266  54  ASP   D OD2 
6103  N  N   . SER   D  63  ? 1.8400 0.5625 1.2382 0.1566  -0.4382 0.2675  55  SER   D N   
6104  C  CA  . SER   D  63  ? 1.8342 0.5195 1.2533 0.1371  -0.4329 0.2800  55  SER   D CA  
6105  C  C   . SER   D  63  ? 1.8241 0.4601 1.2850 0.1319  -0.4347 0.2499  55  SER   D C   
6106  O  O   . SER   D  63  ? 1.8283 0.5779 1.2785 0.1051  -0.4859 0.2458  55  SER   D O   
6107  C  CB  . SER   D  63  ? 1.8570 0.4909 1.2418 0.1199  -0.4005 0.2626  55  SER   D CB  
6108  O  OG  . SER   D  63  ? 1.8277 0.4674 1.2430 0.1385  -0.3883 0.2871  55  SER   D OG  
6109  N  N   . ILE   D  64  ? 1.8305 0.4412 1.3372 0.1233  -0.4545 0.2342  56  ILE   D N   
6110  C  CA  . ILE   D  64  ? 1.8180 0.4659 1.3335 0.0791  -0.4552 0.2245  56  ILE   D CA  
6111  C  C   . ILE   D  64  ? 1.8318 0.3917 1.3936 0.1006  -0.4407 0.2256  56  ILE   D C   
6112  O  O   . ILE   D  64  ? 1.8026 0.2319 1.4396 0.0527  -0.4238 0.2702  56  ILE   D O   
6113  C  CB  . ILE   D  64  ? 1.8311 0.4822 1.3333 0.1034  -0.4881 0.1797  56  ILE   D CB  
6114  C  CG1 . ILE   D  64  ? 1.8386 0.5112 1.3224 0.0893  -0.4923 0.1741  56  ILE   D CG1 
6115  C  CG2 . ILE   D  64  ? 1.8021 0.4634 1.3341 0.1021  -0.4814 0.1876  56  ILE   D CG2 
6116  C  CD1 . ILE   D  64  ? 1.8286 0.5426 1.3102 0.1129  -0.5280 0.1824  56  ILE   D CD1 
6117  N  N   . GLU   D  65  ? 1.7853 0.4079 1.4183 0.1342  -0.4290 0.2435  57  GLU   D N   
6118  C  CA  . GLU   D  65  ? 1.7700 0.4849 1.4780 0.1053  -0.4105 0.2713  57  GLU   D CA  
6119  C  C   . GLU   D  65  ? 1.7425 0.4517 1.5230 0.1165  -0.3777 0.2435  57  GLU   D C   
6120  O  O   . GLU   D  65  ? 1.7653 0.4043 1.4608 0.1017  -0.3303 0.2460  57  GLU   D O   
6121  C  CB  . GLU   D  65  ? 1.7804 0.5174 1.5726 0.1258  -0.3751 0.2576  57  GLU   D CB  
6122  C  CG  . GLU   D  65  ? 1.7829 0.5641 1.6842 0.1009  -0.3439 0.2577  57  GLU   D CG  
6123  C  CD  . GLU   D  65  ? 1.7968 0.6189 1.7213 0.1465  -0.3093 0.3014  57  GLU   D CD  
6124  O  OE1 . GLU   D  65  ? 1.8942 0.5487 1.7287 0.1941  -0.3633 0.3537  57  GLU   D OE1 
6125  O  OE2 . GLU   D  65  ? 1.7843 0.6608 1.7462 0.2111  -0.3050 0.3007  57  GLU   D OE2 
6126  N  N   . LYS   D  66  ? 1.6804 0.5435 1.5184 0.0933  -0.4108 0.2156  58  LYS   D N   
6127  C  CA  . LYS   D  66  ? 1.6978 0.6368 1.5180 0.0515  -0.4029 0.1900  58  LYS   D CA  
6128  C  C   . LYS   D  66  ? 1.6911 0.6082 1.5048 0.0582  -0.4290 0.2108  58  LYS   D C   
6129  O  O   . LYS   D  66  ? 1.6520 0.5408 1.4738 0.0256  -0.4494 0.2361  58  LYS   D O   
6130  C  CB  . LYS   D  66  ? 1.7493 0.6481 1.5689 0.0714  -0.3723 0.1505  58  LYS   D CB  
6131  C  CG  . LYS   D  66  ? 1.7614 0.7234 1.5808 0.0365  -0.3294 0.1226  58  LYS   D CG  
6132  C  CD  . LYS   D  66  ? 1.8042 0.7074 1.5647 0.0015  -0.3210 0.1021  58  LYS   D CD  
6133  C  CE  . LYS   D  66  ? 1.8071 0.7289 1.5673 -0.0010 -0.2905 0.0711  58  LYS   D CE  
6134  N  NZ  . LYS   D  66  ? 1.8424 0.7341 1.5942 0.0363  -0.3087 0.0411  58  LYS   D NZ  
6135  N  N   . ILE   D  67  ? 1.7063 0.6299 1.5295 0.0714  -0.4591 0.1984  59  ILE   D N   
6136  C  CA  . ILE   D  67  ? 1.6574 0.6541 1.5471 0.0865  -0.4695 0.1837  59  ILE   D CA  
6137  C  C   . ILE   D  67  ? 1.6258 0.6773 1.5035 0.1106  -0.4272 0.2273  59  ILE   D C   
6138  O  O   . ILE   D  67  ? 1.5669 0.9278 1.6093 0.0933  -0.3827 0.1605  59  ILE   D O   
6139  C  CB  . ILE   D  67  ? 1.7217 0.6563 1.5739 0.1067  -0.5224 0.1589  59  ILE   D CB  
6140  C  CG1 . ILE   D  67  ? 1.7960 0.6114 1.5685 0.0622  -0.5137 0.1175  59  ILE   D CG1 
6141  C  CG2 . ILE   D  67  ? 1.7050 0.6906 1.5871 0.1091  -0.5271 0.1812  59  ILE   D CG2 
6142  C  CD1 . ILE   D  67  ? 1.8267 0.5413 1.5780 0.0784  -0.5248 0.1236  59  ILE   D CD1 
6143  N  N   . VAL   D  68  ? 1.5875 0.5996 1.5022 0.1698  -0.4421 0.2214  60  VAL   D N   
6144  C  CA  . VAL   D  68  ? 1.5953 0.5906 1.4737 0.1661  -0.4358 0.2560  60  VAL   D CA  
6145  C  C   . VAL   D  68  ? 1.5862 0.5147 1.4550 0.2168  -0.4443 0.2584  60  VAL   D C   
6146  O  O   . VAL   D  68  ? 1.6104 0.3962 1.4349 0.3069  -0.4573 0.3200  60  VAL   D O   
6147  C  CB  . VAL   D  68  ? 1.5651 0.5338 1.4818 0.1752  -0.4246 0.2814  60  VAL   D CB  
6148  C  CG1 . VAL   D  68  ? 1.5868 0.5791 1.4424 0.1627  -0.4338 0.3051  60  VAL   D CG1 
6149  C  CG2 . VAL   D  68  ? 1.5900 0.4784 1.4701 0.1738  -0.4187 0.2991  60  VAL   D CG2 
6150  N  N   . GLU   D  69  ? 1.6087 0.5426 1.4255 0.1719  -0.4283 0.2121  61  GLU   D N   
6151  C  CA  . GLU   D  69  ? 1.6478 0.5170 1.4424 0.1464  -0.4064 0.1387  61  GLU   D CA  
6152  C  C   . GLU   D  69  ? 1.6818 0.3693 1.3948 0.1246  -0.3678 0.1181  61  GLU   D C   
6153  O  O   . GLU   D  69  ? 1.6791 0.2470 1.3503 0.0930  -0.3354 0.0909  61  GLU   D O   
6154  C  CB  . GLU   D  69  ? 1.6828 0.6130 1.4491 0.1358  -0.3880 0.0994  61  GLU   D CB  
6155  C  CG  . GLU   D  69  ? 1.7080 0.6960 1.4895 0.0941  -0.3462 0.1283  61  GLU   D CG  
6156  C  CD  . GLU   D  69  ? 1.7609 0.8291 1.4328 0.0792  -0.3382 0.0924  61  GLU   D CD  
6157  O  OE1 . GLU   D  69  ? 1.7600 0.7959 1.4706 0.0595  -0.3775 0.0147  61  GLU   D OE1 
6158  O  OE2 . GLU   D  69  ? 1.7766 0.9425 1.3784 0.0155  -0.3368 0.0143  61  GLU   D OE2 
6159  N  N   . ILE   D  70  ? 1.7167 0.3568 1.3898 0.1352  -0.3658 0.1460  62  ILE   D N   
6160  C  CA  . ILE   D  70  ? 1.7674 0.5365 1.3959 0.1660  -0.3808 0.1833  62  ILE   D CA  
6161  C  C   . ILE   D  70  ? 1.7977 0.5627 1.4389 0.1372  -0.3939 0.1575  62  ILE   D C   
6162  O  O   . ILE   D  70  ? 1.7716 0.6374 1.4807 0.1535  -0.3738 0.1970  62  ILE   D O   
6163  C  CB  . ILE   D  70  ? 1.8042 0.5212 1.4235 0.1822  -0.3619 0.1839  62  ILE   D CB  
6164  C  CG1 . ILE   D  70  ? 1.8226 0.5078 1.3971 0.1753  -0.3719 0.2401  62  ILE   D CG1 
6165  C  CG2 . ILE   D  70  ? 1.8066 0.5486 1.4393 0.1983  -0.3609 0.2010  62  ILE   D CG2 
6166  C  CD1 . ILE   D  70  ? 1.8245 0.5524 1.3874 0.1687  -0.3732 0.2412  62  ILE   D CD1 
6167  N  N   . ASP   D  71  ? 1.7986 0.6819 1.4400 0.1726  -0.4381 0.1869  63  ASP   D N   
6168  C  CA  . ASP   D  71  ? 1.8672 0.6512 1.4334 0.1671  -0.4242 0.2143  63  ASP   D CA  
6169  C  C   . ASP   D  71  ? 1.8486 0.6444 1.4460 0.1496  -0.4239 0.1972  63  ASP   D C   
6170  O  O   . ASP   D  71  ? 1.9170 0.7295 1.4276 0.2033  -0.3334 0.3060  63  ASP   D O   
6171  C  CB  . ASP   D  71  ? 1.9141 0.7558 1.3895 0.1231  -0.4336 0.2142  63  ASP   D CB  
6172  C  CG  . ASP   D  71  ? 2.0098 0.7612 1.4133 0.0975  -0.4223 0.2012  63  ASP   D CG  
6173  O  OD1 . ASP   D  71  ? 2.1048 0.8117 1.3710 0.1005  -0.3908 0.2558  63  ASP   D OD1 
6174  O  OD2 . ASP   D  71  ? 2.0906 0.8460 1.4038 0.1242  -0.4343 0.2169  63  ASP   D OD2 
6175  N  N   . ARG   D  72  ? 1.8167 0.5856 1.4872 0.1607  -0.4599 0.2581  64  ARG   D N   
6176  C  CA  . ARG   D  72  ? 1.8119 0.5866 1.4965 0.1381  -0.4681 0.2634  64  ARG   D CA  
6177  C  C   . ARG   D  72  ? 1.8370 0.4596 1.4660 0.1279  -0.4909 0.2392  64  ARG   D C   
6178  O  O   . ARG   D  72  ? 1.8925 0.3017 1.5302 0.1343  -0.4904 0.2559  64  ARG   D O   
6179  C  CB  . ARG   D  72  ? 1.8018 0.6322 1.5095 0.0782  -0.5026 0.2716  64  ARG   D CB  
6180  C  CG  . ARG   D  72  ? 1.8000 0.7768 1.5108 0.0564  -0.5097 0.3022  64  ARG   D CG  
6181  C  CD  . ARG   D  72  ? 1.7235 0.8710 1.5550 0.0023  -0.5126 0.3112  64  ARG   D CD  
6182  N  NE  . ARG   D  72  ? 1.7181 0.9782 1.6184 -0.0007 -0.4884 0.3513  64  ARG   D NE  
6183  C  CZ  . ARG   D  72  ? 1.6475 1.0286 1.6155 0.0008  -0.4647 0.3461  64  ARG   D CZ  
6184  N  NH1 . ARG   D  72  ? 1.6258 1.0603 1.6613 0.0175  -0.5417 0.3204  64  ARG   D NH1 
6185  N  NH2 . ARG   D  72  ? 1.6680 1.0120 1.5801 -0.0256 -0.4987 0.3990  64  ARG   D NH2 
6186  N  N   . HIS   D  73  ? 1.8046 0.4338 1.4817 0.1195  -0.4476 0.1776  65  HIS   D N   
6187  C  CA  . HIS   D  73  ? 1.8147 0.5179 1.4919 0.1677  -0.4494 0.1939  65  HIS   D CA  
6188  C  C   . HIS   D  73  ? 1.7669 0.5401 1.4000 0.2021  -0.4517 0.1970  65  HIS   D C   
6189  O  O   . HIS   D  73  ? 1.7752 0.6349 1.3610 0.2758  -0.4650 0.2605  65  HIS   D O   
6190  C  CB  . HIS   D  73  ? 1.7933 0.4625 1.5121 0.1738  -0.4456 0.1632  65  HIS   D CB  
6191  C  CG  . HIS   D  73  ? 1.7989 0.3875 1.5326 0.2380  -0.4569 0.1450  65  HIS   D CG  
6192  N  ND1 . HIS   D  73  ? 1.8342 0.4044 1.5331 0.2745  -0.4553 0.1402  65  HIS   D ND1 
6193  C  CD2 . HIS   D  73  ? 1.8236 0.3584 1.5350 0.2476  -0.4584 0.1401  65  HIS   D CD2 
6194  C  CE1 . HIS   D  73  ? 1.8221 0.4495 1.5263 0.2730  -0.4478 0.0981  65  HIS   D CE1 
6195  N  NE2 . HIS   D  73  ? 1.8068 0.3631 1.5816 0.2819  -0.4491 0.1019  65  HIS   D NE2 
6196  N  N   . ILE   D  74  ? 1.7789 0.4968 1.3557 0.1821  -0.4278 0.2187  66  ILE   D N   
6197  C  CA  . ILE   D  74  ? 1.8166 0.3888 1.3657 0.1805  -0.3910 0.2768  66  ILE   D CA  
6198  C  C   . ILE   D  74  ? 1.8560 0.3799 1.3232 0.1816  -0.4114 0.3087  66  ILE   D C   
6199  O  O   . ILE   D  74  ? 1.9292 0.2430 1.2872 0.1635  -0.4331 0.3000  66  ILE   D O   
6200  C  CB  . ILE   D  74  ? 1.7954 0.4582 1.3441 0.1397  -0.4091 0.2084  66  ILE   D CB  
6201  C  CG1 . ILE   D  74  ? 1.8061 0.4852 1.3427 0.1376  -0.4090 0.2198  66  ILE   D CG1 
6202  C  CG2 . ILE   D  74  ? 1.7624 0.4698 1.3569 0.1323  -0.4153 0.2158  66  ILE   D CG2 
6203  C  CD1 . ILE   D  74  ? 1.7926 0.4551 1.3630 0.1529  -0.4063 0.2367  66  ILE   D CD1 
6204  N  N   . GLY   D  75  ? 1.8477 0.3803 1.3744 0.1733  -0.4180 0.3191  67  GLY   D N   
6205  C  CA  . GLY   D  75  ? 1.8651 0.3898 1.3824 0.1643  -0.4515 0.3644  67  GLY   D CA  
6206  C  C   . GLY   D  75  ? 1.8650 0.3328 1.3719 0.1421  -0.4647 0.4217  67  GLY   D C   
6207  O  O   . GLY   D  75  ? 1.8336 0.3989 1.3810 0.1528  -0.4666 0.4734  67  GLY   D O   
6208  N  N   . CYS   D  76  ? 1.8956 0.3545 1.3993 0.1024  -0.4706 0.4015  68  CYS   D N   
6209  C  CA  . CYS   D  76  ? 1.9305 0.5185 1.4319 0.1075  -0.4822 0.2832  68  CYS   D CA  
6210  C  C   . CYS   D  76  ? 1.9227 0.5460 1.4909 0.0200  -0.4272 0.2404  68  CYS   D C   
6211  O  O   . CYS   D  76  ? 1.9294 0.5840 1.5870 -0.0422 -0.3558 0.1790  68  CYS   D O   
6212  C  CB  . CYS   D  76  ? 1.9750 0.4786 1.3729 0.0916  -0.4989 0.2787  68  CYS   D CB  
6213  S  SG  . CYS   D  76  ? 2.0151 0.6394 1.3885 0.0705  -0.5269 0.2109  68  CYS   D SG  
6214  N  N   . ALA   D  77  ? 1.9111 0.6153 1.4749 0.0237  -0.4210 0.1655  69  ALA   D N   
6215  C  CA  . ALA   D  77  ? 1.8882 0.6098 1.3809 0.0388  -0.4537 0.1582  69  ALA   D CA  
6216  C  C   . ALA   D  77  ? 1.8875 0.6391 1.3635 0.0372  -0.4103 0.1067  69  ALA   D C   
6217  O  O   . ALA   D  77  ? 1.8213 0.6239 1.3199 0.0708  -0.4126 0.0108  69  ALA   D O   
6218  C  CB  . ALA   D  77  ? 1.9304 0.6203 1.3884 0.0664  -0.4608 0.1862  69  ALA   D CB  
6219  N  N   . MET   D  78  ? 1.9100 0.6131 1.3012 0.0232  -0.4268 0.0856  70  MET   D N   
6220  C  CA  . MET   D  78  ? 1.9153 0.6485 1.2881 0.0280  -0.4177 0.0619  70  MET   D CA  
6221  C  C   . MET   D  78  ? 1.9021 0.6522 1.2444 0.0643  -0.4409 0.0877  70  MET   D C   
6222  O  O   . MET   D  78  ? 1.8156 0.7192 1.2630 0.1134  -0.4916 0.0673  70  MET   D O   
6223  C  CB  . MET   D  78  ? 1.9287 0.6268 1.3256 0.0308  -0.4149 0.0405  70  MET   D CB  
6224  C  CG  . MET   D  78  ? 2.0009 0.6832 1.3333 0.0009  -0.4047 0.0432  70  MET   D CG  
6225  S  SD  . MET   D  78  ? 1.9967 0.7828 1.4762 0.0101  -0.4112 -0.0006 70  MET   D SD  
6226  C  CE  . MET   D  78  ? 2.0234 0.9042 1.5144 -0.0727 -0.3978 -0.0755 70  MET   D CE  
6227  N  N   . SER   D  79  ? 1.9242 0.6324 1.2663 0.0683  -0.4180 0.0628  71  SER   D N   
6228  C  CA  . SER   D  79  ? 1.9599 0.6180 1.3080 0.0932  -0.4090 0.0407  71  SER   D CA  
6229  C  C   . SER   D  79  ? 1.9504 0.5241 1.3120 0.0566  -0.3695 0.0051  71  SER   D C   
6230  O  O   . SER   D  79  ? 2.0024 0.4596 1.3119 0.1031  -0.3488 0.0053  71  SER   D O   
6231  C  CB  . SER   D  79  ? 1.9590 0.6079 1.3189 0.0984  -0.4447 0.0599  71  SER   D CB  
6232  O  OG  . SER   D  79  ? 2.0233 0.6026 1.3561 0.1302  -0.4736 0.1248  71  SER   D OG  
6233  N  N   . GLY   D  80  ? 1.9191 0.5434 1.4003 0.0324  -0.3672 -0.0653 72  GLY   D N   
6234  C  CA  . GLY   D  80  ? 1.8911 0.5814 1.3735 0.0639  -0.3688 -0.0569 72  GLY   D CA  
6235  C  C   . GLY   D  80  ? 1.8735 0.5049 1.3466 0.0965  -0.4214 -0.0247 72  GLY   D C   
6236  O  O   . GLY   D  80  ? 1.9053 0.4815 1.3758 0.1346  -0.3541 -0.0932 72  GLY   D O   
6237  N  N   . LEU   D  81  ? 1.9162 0.4902 1.3384 0.0820  -0.4152 0.0667  73  LEU   D N   
6238  C  CA  . LEU   D  81  ? 1.8754 0.6149 1.3124 0.0719  -0.4319 0.1279  73  LEU   D CA  
6239  C  C   . LEU   D  81  ? 1.8821 0.6367 1.3035 0.0807  -0.4275 0.1042  73  LEU   D C   
6240  O  O   . LEU   D  81  ? 1.8480 0.7166 1.2926 0.1482  -0.4593 0.1323  73  LEU   D O   
6241  C  CB  . LEU   D  81  ? 1.8431 0.6605 1.3395 0.0506  -0.4413 0.1475  73  LEU   D CB  
6242  C  CG  . LEU   D  81  ? 1.8154 0.7126 1.3048 0.0385  -0.4792 0.1186  73  LEU   D CG  
6243  C  CD1 . LEU   D  81  ? 1.8006 0.7834 1.2827 0.0311  -0.4508 0.1333  73  LEU   D CD1 
6244  C  CD2 . LEU   D  81  ? 1.8021 0.7711 1.3037 0.0352  -0.4757 0.1162  73  LEU   D CD2 
6245  N  N   . THR   D  82  ? 1.8535 0.6467 1.2842 0.0518  -0.4021 0.1658  74  THR   D N   
6246  C  CA  . THR   D  82  ? 1.8068 0.6578 1.3426 0.0186  -0.3597 0.1553  74  THR   D CA  
6247  C  C   . THR   D  82  ? 1.7149 0.7109 1.3747 0.0020  -0.3511 0.1354  74  THR   D C   
6248  O  O   . THR   D  82  ? 1.7328 0.7213 1.4572 -0.0160 -0.3043 0.1368  74  THR   D O   
6249  C  CB  . THR   D  82  ? 1.8146 0.6170 1.3337 0.0237  -0.3449 0.1579  74  THR   D CB  
6250  O  OG1 . THR   D  82  ? 1.8652 0.6148 1.3138 0.0206  -0.2995 0.1262  74  THR   D OG1 
6251  C  CG2 . THR   D  82  ? 1.7927 0.6484 1.3544 0.0210  -0.3673 0.1482  74  THR   D CG2 
6252  N  N   . ALA   D  83  ? 1.7209 0.7393 1.3472 -0.0182 -0.3580 0.1324  75  ALA   D N   
6253  C  CA  . ALA   D  83  ? 1.7168 0.6974 1.2964 -0.0391 -0.3628 0.1626  75  ALA   D CA  
6254  C  C   . ALA   D  83  ? 1.6768 0.6661 1.3050 -0.0775 -0.3661 0.1583  75  ALA   D C   
6255  O  O   . ALA   D  83  ? 1.6082 0.6469 1.2477 -0.1263 -0.3588 0.1549  75  ALA   D O   
6256  C  CB  . ALA   D  83  ? 1.6895 0.7189 1.2837 -0.0149 -0.3658 0.1769  75  ALA   D CB  
6257  N  N   . ASP   D  84  ? 1.7002 0.6045 1.3477 -0.0693 -0.3698 0.1383  76  ASP   D N   
6258  C  CA  . ASP   D  84  ? 1.7114 0.6644 1.3434 -0.0621 -0.3747 0.1368  76  ASP   D CA  
6259  C  C   . ASP   D  84  ? 1.7349 0.6312 1.3700 -0.0491 -0.4050 0.1131  76  ASP   D C   
6260  O  O   . ASP   D  84  ? 1.7900 0.5186 1.4103 -0.1373 -0.3724 0.0848  76  ASP   D O   
6261  C  CB  . ASP   D  84  ? 1.6809 0.6919 1.3457 -0.0757 -0.3909 0.1153  76  ASP   D CB  
6262  C  CG  . ASP   D  84  ? 1.6345 0.7807 1.3076 -0.0774 -0.3998 0.1173  76  ASP   D CG  
6263  O  OD1 . ASP   D  84  ? 1.5323 0.8172 1.3108 -0.0732 -0.4801 0.1222  76  ASP   D OD1 
6264  O  OD2 . ASP   D  84  ? 1.6463 0.8254 1.2754 -0.1384 -0.4700 0.0835  76  ASP   D OD2 
6265  N  N   . ALA   D  85  ? 1.7212 0.6412 1.4233 -0.0133 -0.4333 0.0873  77  ALA   D N   
6266  C  CA  . ALA   D  85  ? 1.7420 0.6237 1.4421 -0.0267 -0.4244 0.1169  77  ALA   D CA  
6267  C  C   . ALA   D  85  ? 1.7692 0.6472 1.4298 -0.0093 -0.4266 0.1027  77  ALA   D C   
6268  O  O   . ALA   D  85  ? 1.7467 0.7127 1.3743 -0.0286 -0.3904 0.0813  77  ALA   D O   
6269  C  CB  . ALA   D  85  ? 1.7526 0.6019 1.4510 -0.0176 -0.4405 0.0893  77  ALA   D CB  
6270  N  N   . ARG   D  86  ? 1.7690 0.6628 1.4385 -0.0256 -0.4268 0.1248  78  ARG   D N   
6271  C  CA  . ARG   D  86  ? 1.8575 0.6395 1.4539 0.0216  -0.4767 0.1575  78  ARG   D CA  
6272  C  C   . ARG   D  86  ? 1.7839 0.6141 1.4520 0.0781  -0.4760 0.1495  78  ARG   D C   
6273  O  O   . ARG   D  86  ? 1.7452 0.5619 1.5491 0.0994  -0.4323 0.1828  78  ARG   D O   
6274  C  CB  . ARG   D  86  ? 1.8606 0.7633 1.5052 0.0075  -0.4945 0.1715  78  ARG   D CB  
6275  C  CG  . ARG   D  86  ? 1.9986 0.8274 1.5930 0.0538  -0.5080 0.2465  78  ARG   D CG  
6276  C  CD  . ARG   D  86  ? 2.0267 0.9258 1.6736 0.0953  -0.5883 0.3076  78  ARG   D CD  
6277  N  NE  . ARG   D  86  ? 2.0790 1.0001 1.8123 0.1506  -0.6110 0.3685  78  ARG   D NE  
6278  C  CZ  . ARG   D  86  ? 2.0809 1.0207 1.8924 0.1586  -0.6336 0.3876  78  ARG   D CZ  
6279  N  NH1 . ARG   D  86  ? 2.0420 1.0283 1.8950 0.1657  -0.6678 0.3609  78  ARG   D NH1 
6280  N  NH2 . ARG   D  86  ? 2.0588 1.0704 1.8638 0.1257  -0.6528 0.4490  78  ARG   D NH2 
6281  N  N   . SER   D  87  ? 1.7593 0.4661 1.4386 0.0720  -0.4686 0.1705  79  SER   D N   
6282  C  CA  . SER   D  87  ? 1.7336 0.4619 1.4390 0.0683  -0.4929 0.1721  79  SER   D CA  
6283  C  C   . SER   D  87  ? 1.7447 0.4687 1.4608 0.1113  -0.4628 0.1851  79  SER   D C   
6284  O  O   . SER   D  87  ? 1.8257 0.6386 1.4438 -0.0479 -0.4023 0.2724  79  SER   D O   
6285  C  CB  . SER   D  87  ? 1.6975 0.4405 1.4725 0.0702  -0.5093 0.2000  79  SER   D CB  
6286  O  OG  . SER   D  87  ? 1.6433 0.5097 1.4590 0.1275  -0.5379 0.1683  79  SER   D OG  
6287  N  N   . MET   D  88  ? 1.7643 0.4360 1.4506 0.1072  -0.4477 0.1595  80  MET   D N   
6288  C  CA  . MET   D  88  ? 1.7865 0.4675 1.4684 0.0908  -0.4178 0.1555  80  MET   D CA  
6289  C  C   . MET   D  88  ? 1.7803 0.3723 1.4832 0.1059  -0.3552 0.1312  80  MET   D C   
6290  O  O   . MET   D  88  ? 1.7965 0.3847 1.5120 0.1097  -0.3226 0.1323  80  MET   D O   
6291  C  CB  . MET   D  88  ? 1.8225 0.5099 1.5028 0.1334  -0.4630 0.1240  80  MET   D CB  
6292  C  CG  . MET   D  88  ? 1.8588 0.6202 1.4728 0.1381  -0.5120 0.1040  80  MET   D CG  
6293  S  SD  . MET   D  88  ? 1.9911 0.5115 1.5381 0.0818  -0.5311 0.1341  80  MET   D SD  
6294  C  CE  . MET   D  88  ? 1.9543 0.7157 1.5753 0.0469  -0.5400 0.1533  80  MET   D CE  
6295  N  N   . ILE   D  89  ? 1.7693 0.3965 1.4944 0.1004  -0.3119 0.1254  81  ILE   D N   
6296  C  CA  . ILE   D  89  ? 1.7313 0.5081 1.4584 0.1113  -0.3339 0.1293  81  ILE   D CA  
6297  C  C   . ILE   D  89  ? 1.6697 0.5337 1.4584 0.1301  -0.3118 0.1399  81  ILE   D C   
6298  O  O   . ILE   D  89  ? 1.6344 0.5104 1.4640 0.1511  -0.2778 0.1280  81  ILE   D O   
6299  C  CB  . ILE   D  89  ? 1.7442 0.5360 1.4551 0.1172  -0.3705 0.1529  81  ILE   D CB  
6300  C  CG1 . ILE   D  89  ? 1.7564 0.5489 1.5284 0.1456  -0.3435 0.0647  81  ILE   D CG1 
6301  C  CG2 . ILE   D  89  ? 1.7310 0.4784 1.3967 0.1824  -0.3923 0.1924  81  ILE   D CG2 
6302  C  CD1 . ILE   D  89  ? 1.7722 0.6758 1.5864 0.0974  -0.3012 -0.0051 81  ILE   D CD1 
6303  N  N   . GLU   D  90  ? 1.6769 0.5136 1.4103 0.1622  -0.3312 0.1616  82  GLU   D N   
6304  C  CA  . GLU   D  90  ? 1.6581 0.4834 1.4108 0.1304  -0.3229 0.1770  82  GLU   D CA  
6305  C  C   . GLU   D  90  ? 1.6346 0.4141 1.4312 0.1406  -0.3229 0.1836  82  GLU   D C   
6306  O  O   . GLU   D  90  ? 1.5469 0.4229 1.3924 0.0848  -0.3367 0.2806  82  GLU   D O   
6307  C  CB  . GLU   D  90  ? 1.6614 0.5480 1.4532 0.1198  -0.3328 0.1334  82  GLU   D CB  
6308  C  CG  . GLU   D  90  ? 1.6275 0.6130 1.5330 0.1541  -0.3309 0.1376  82  GLU   D CG  
6309  C  CD  . GLU   D  90  ? 1.6286 0.6868 1.5254 0.1020  -0.3608 0.1111  82  GLU   D CD  
6310  O  OE1 . GLU   D  90  ? 1.5814 0.7999 1.5137 0.0644  -0.3854 0.0758  82  GLU   D OE1 
6311  O  OE2 . GLU   D  90  ? 1.6508 0.5434 1.7243 0.0612  -0.2942 -0.0019 82  GLU   D OE2 
6312  N  N   . HIS   D  91  ? 1.6550 0.2921 1.4253 0.1050  -0.2676 0.2276  83  HIS   D N   
6313  C  CA  . HIS   D  91  ? 1.6662 0.2534 1.4742 0.0622  -0.2421 0.2355  83  HIS   D CA  
6314  C  C   . HIS   D  91  ? 1.6652 0.3069 1.4100 0.0586  -0.2662 0.2336  83  HIS   D C   
6315  O  O   . HIS   D  91  ? 1.6186 0.4441 1.4244 -0.1097 -0.1964 0.2552  83  HIS   D O   
6316  C  CB  . HIS   D  91  ? 1.7413 0.2463 1.4940 0.0493  -0.1971 0.2305  83  HIS   D CB  
6317  C  CG  . HIS   D  91  ? 1.7937 0.2440 1.5673 0.0474  -0.1524 0.2665  83  HIS   D CG  
6318  N  ND1 . HIS   D  91  ? 1.8010 0.2446 1.6202 0.1001  -0.1568 0.2689  83  HIS   D ND1 
6319  C  CD2 . HIS   D  91  ? 1.7923 0.2721 1.6560 0.0499  -0.1440 0.2728  83  HIS   D CD2 
6320  C  CE1 . HIS   D  91  ? 1.8196 0.3203 1.6607 0.0813  -0.1350 0.2966  83  HIS   D CE1 
6321  N  NE2 . HIS   D  91  ? 1.7780 0.3238 1.6561 0.0330  -0.1103 0.2805  83  HIS   D NE2 
6322  N  N   . ALA   D  92  ? 1.6462 0.2979 1.4105 0.0461  -0.2962 0.2111  84  ALA   D N   
6323  C  CA  . ALA   D  92  ? 1.6420 0.3688 1.4373 0.0467  -0.2927 0.2247  84  ALA   D CA  
6324  C  C   . ALA   D  92  ? 1.6111 0.3722 1.3851 0.0460  -0.2901 0.2464  84  ALA   D C   
6325  O  O   . ALA   D  92  ? 1.5802 0.5539 1.3660 0.0122  -0.2776 0.3197  84  ALA   D O   
6326  C  CB  . ALA   D  92  ? 1.6537 0.3985 1.4649 0.0838  -0.3221 0.2107  84  ALA   D CB  
6327  N  N   . ARG   D  93  ? 1.6290 0.4165 1.3688 0.0741  -0.2993 0.2120  85  ARG   D N   
6328  C  CA  . ARG   D  93  ? 1.6284 0.4461 1.3395 0.0840  -0.2936 0.2030  85  ARG   D CA  
6329  C  C   . ARG   D  93  ? 1.5995 0.4117 1.3034 0.0658  -0.2826 0.1734  85  ARG   D C   
6330  O  O   . ARG   D  93  ? 1.6211 0.3022 1.2926 0.1101  -0.2781 0.2275  85  ARG   D O   
6331  C  CB  . ARG   D  93  ? 1.6410 0.4805 1.3130 0.0876  -0.2926 0.1631  85  ARG   D CB  
6332  C  CG  . ARG   D  93  ? 1.6515 0.4658 1.3176 0.1106  -0.3101 0.1343  85  ARG   D CG  
6333  C  CD  . ARG   D  93  ? 1.6321 0.4236 1.3028 0.1156  -0.3244 0.1152  85  ARG   D CD  
6334  N  NE  . ARG   D  93  ? 1.6318 0.3426 1.3233 0.1252  -0.3579 0.0823  85  ARG   D NE  
6335  C  CZ  . ARG   D  93  ? 1.6228 0.3419 1.2688 0.1306  -0.3909 0.0674  85  ARG   D CZ  
6336  N  NH1 . ARG   D  93  ? 1.6246 0.3026 1.2738 0.1268  -0.3962 0.0537  85  ARG   D NH1 
6337  N  NH2 . ARG   D  93  ? 1.6268 0.3895 1.2713 0.1590  -0.4253 0.0356  85  ARG   D NH2 
6338  N  N   . THR   D  94  ? 1.5977 0.3813 1.2575 0.0721  -0.2644 0.1561  86  THR   D N   
6339  C  CA  . THR   D  94  ? 1.5843 0.3643 1.2396 0.0653  -0.2622 0.1401  86  THR   D CA  
6340  C  C   . THR   D  94  ? 1.6129 0.4562 1.2414 0.0926  -0.2292 0.1305  86  THR   D C   
6341  O  O   . THR   D  94  ? 1.6300 0.4664 1.2816 0.0950  -0.1961 0.1609  86  THR   D O   
6342  C  CB  . THR   D  94  ? 1.5878 0.3571 1.1910 0.0617  -0.2615 0.1356  86  THR   D CB  
6343  O  OG1 . THR   D  94  ? 1.5900 0.2953 1.1698 0.0587  -0.2748 0.1249  86  THR   D OG1 
6344  C  CG2 . THR   D  94  ? 1.5676 0.3712 1.1810 0.0681  -0.2802 0.1243  86  THR   D CG2 
6345  N  N   . ALA   D  95  ? 1.6391 0.4185 1.2430 0.0789  -0.2234 0.1414  87  ALA   D N   
6346  C  CA  . ALA   D  95  ? 1.6272 0.4556 1.2793 0.0730  -0.2165 0.1699  87  ALA   D CA  
6347  C  C   . ALA   D  95  ? 1.6188 0.4749 1.2918 0.0832  -0.2228 0.1667  87  ALA   D C   
6348  O  O   . ALA   D  95  ? 1.5423 0.6454 1.3305 0.0297  -0.1287 0.1675  87  ALA   D O   
6349  C  CB  . ALA   D  95  ? 1.6114 0.4812 1.2815 0.1174  -0.2105 0.1766  87  ALA   D CB  
6350  N  N   . ALA   D  96  ? 1.6493 0.3648 1.3334 0.0789  -0.2414 0.1957  88  ALA   D N   
6351  C  CA  . ALA   D  96  ? 1.6680 0.3934 1.3471 0.0675  -0.2548 0.1940  88  ALA   D CA  
6352  C  C   . ALA   D  96  ? 1.6327 0.4175 1.3354 0.0538  -0.2353 0.1581  88  ALA   D C   
6353  O  O   . ALA   D  96  ? 1.6933 0.3594 1.3900 0.0335  -0.1945 0.0695  88  ALA   D O   
6354  C  CB  . ALA   D  96  ? 1.6996 0.3814 1.3536 0.0865  -0.2873 0.1818  88  ALA   D CB  
6355  N  N   . VAL   D  97  ? 1.6261 0.4552 1.3037 0.0770  -0.2575 0.1582  89  VAL   D N   
6356  C  CA  . VAL   D  97  ? 1.6305 0.4336 1.3127 0.0957  -0.2751 0.1903  89  VAL   D CA  
6357  C  C   . VAL   D  97  ? 1.5875 0.4346 1.3193 0.1177  -0.2809 0.1914  89  VAL   D C   
6358  O  O   . VAL   D  97  ? 1.5647 0.3896 1.3410 0.1499  -0.2955 0.3020  89  VAL   D O   
6359  C  CB  . VAL   D  97  ? 1.6290 0.4956 1.3289 0.1088  -0.2710 0.1700  89  VAL   D CB  
6360  C  CG1 . VAL   D  97  ? 1.5968 0.5291 1.3339 0.1583  -0.2786 0.1958  89  VAL   D CG1 
6361  C  CG2 . VAL   D  97  ? 1.6866 0.5327 1.3217 0.0900  -0.2578 0.1758  89  VAL   D CG2 
6362  N  N   . THR   D  98  ? 1.5741 0.3438 1.2867 0.1156  -0.2582 0.2136  90  THR   D N   
6363  C  CA  . THR   D  98  ? 1.5752 0.3223 1.2972 0.1206  -0.2342 0.2224  90  THR   D CA  
6364  C  C   . THR   D  98  ? 1.5341 0.4368 1.3244 0.1353  -0.2450 0.1936  90  THR   D C   
6365  O  O   . THR   D  98  ? 1.5207 0.4160 1.4040 0.1121  -0.2344 0.1525  90  THR   D O   
6366  C  CB  . THR   D  98  ? 1.5545 0.2953 1.2588 0.1134  -0.2000 0.2376  90  THR   D CB  
6367  O  OG1 . THR   D  98  ? 1.5801 0.2665 1.2377 0.1388  -0.1760 0.2862  90  THR   D OG1 
6368  C  CG2 . THR   D  98  ? 1.5405 0.3154 1.2507 0.1158  -0.1977 0.2353  90  THR   D CG2 
6369  N  N   . HIS   D  99  ? 1.5642 0.4077 1.3188 0.1506  -0.3003 0.2231  91  HIS   D N   
6370  C  CA  . HIS   D  99  ? 1.5499 0.4063 1.3453 0.1676  -0.3177 0.2289  91  HIS   D CA  
6371  C  C   . HIS   D  99  ? 1.5551 0.5160 1.3315 0.1712  -0.3820 0.2129  91  HIS   D C   
6372  O  O   . HIS   D  99  ? 1.5453 0.5808 1.4368 0.1360  -0.3771 0.2283  91  HIS   D O   
6373  C  CB  . HIS   D  99  ? 1.6262 0.3407 1.3417 0.1506  -0.3344 0.2109  91  HIS   D CB  
6374  C  CG  . HIS   D  99  ? 1.6299 0.3095 1.3697 0.1561  -0.3265 0.1729  91  HIS   D CG  
6375  N  ND1 . HIS   D  99  ? 1.7063 0.3915 1.3891 0.1680  -0.3019 0.1581  91  HIS   D ND1 
6376  C  CD2 . HIS   D  99  ? 1.6883 0.3528 1.3634 0.1491  -0.3573 0.1271  91  HIS   D CD2 
6377  C  CE1 . HIS   D  99  ? 1.7111 0.5048 1.4016 0.1356  -0.3396 0.0913  91  HIS   D CE1 
6378  N  NE2 . HIS   D  99  ? 1.7096 0.4845 1.3965 0.1428  -0.3374 0.0871  91  HIS   D NE2 
6379  N  N   . ASN   D  100 ? 1.5027 0.5039 1.3253 0.1744  -0.3925 0.2245  92  ASN   D N   
6380  C  CA  . ASN   D  100 ? 1.4995 0.5620 1.3696 0.1576  -0.3808 0.1723  92  ASN   D CA  
6381  C  C   . ASN   D  100 ? 1.4370 0.5887 1.3555 0.1652  -0.4338 0.1397  92  ASN   D C   
6382  O  O   . ASN   D  100 ? 1.4266 0.6292 1.4053 0.1420  -0.4357 0.1186  92  ASN   D O   
6383  C  CB  . ASN   D  100 ? 1.5372 0.5642 1.3701 0.1544  -0.3447 0.1598  92  ASN   D CB  
6384  C  CG  . ASN   D  100 ? 1.5777 0.6048 1.3944 0.1377  -0.3382 0.1332  92  ASN   D CG  
6385  O  OD1 . ASN   D  100 ? 1.5853 0.7178 1.4638 0.1622  -0.2737 0.1645  92  ASN   D OD1 
6386  N  ND2 . ASN   D  100 ? 1.5784 0.6754 1.4254 0.1408  -0.3075 0.1362  92  ASN   D ND2 
6387  N  N   . LEU   D  101 ? 1.4515 0.5931 1.3358 0.1434  -0.4734 0.1295  93  LEU   D N   
6388  C  CA  . LEU   D  101 ? 1.4523 0.5426 1.3616 0.1066  -0.4818 0.1423  93  LEU   D CA  
6389  C  C   . LEU   D  101 ? 1.4774 0.6319 1.4001 0.1162  -0.4558 0.1846  93  LEU   D C   
6390  O  O   . LEU   D  101 ? 1.5113 0.6599 1.4034 0.0465  -0.4145 0.1590  93  LEU   D O   
6391  C  CB  . LEU   D  101 ? 1.4351 0.4358 1.3302 0.1391  -0.5047 0.1655  93  LEU   D CB  
6392  C  CG  . LEU   D  101 ? 1.4103 0.4223 1.3349 0.1150  -0.5186 0.1985  93  LEU   D CG  
6393  C  CD1 . LEU   D  101 ? 1.4032 0.4646 1.3177 0.1393  -0.5399 0.1939  93  LEU   D CD1 
6394  C  CD2 . LEU   D  101 ? 1.4016 0.3588 1.3279 0.1290  -0.5163 0.2343  93  LEU   D CD2 
6395  N  N   . TYR   D  102 ? 1.4871 0.6265 1.4402 0.1298  -0.4359 0.1748  94  TYR   D N   
6396  C  CA  . TYR   D  102 ? 1.4608 0.6909 1.4854 0.1147  -0.4217 0.2175  94  TYR   D CA  
6397  C  C   . TYR   D  102 ? 1.4660 0.6470 1.5282 0.1138  -0.3793 0.2109  94  TYR   D C   
6398  O  O   . TYR   D  102 ? 1.4747 0.7431 1.5553 0.1285  -0.3319 0.2598  94  TYR   D O   
6399  C  CB  . TYR   D  102 ? 1.4783 0.7818 1.4941 0.1221  -0.4796 0.1904  94  TYR   D CB  
6400  C  CG  . TYR   D  102 ? 1.5096 0.8997 1.4959 0.1114  -0.5511 0.1847  94  TYR   D CG  
6401  C  CD1 . TYR   D  102 ? 1.4908 0.9740 1.5522 0.1312  -0.5822 0.1455  94  TYR   D CD1 
6402  C  CD2 . TYR   D  102 ? 1.5227 0.9299 1.4140 0.1145  -0.5832 0.1974  94  TYR   D CD2 
6403  C  CE1 . TYR   D  102 ? 1.5125 1.0991 1.5233 0.0862  -0.6077 0.1321  94  TYR   D CE1 
6404  C  CE2 . TYR   D  102 ? 1.5303 1.0129 1.3837 0.1230  -0.6184 0.2447  94  TYR   D CE2 
6405  C  CZ  . TYR   D  102 ? 1.4920 1.0827 1.4316 0.1033  -0.6197 0.1723  94  TYR   D CZ  
6406  O  OH  . TYR   D  102 ? 1.5214 1.3614 1.4373 -0.0329 -0.6157 0.1853  94  TYR   D OH  
6407  N  N   . TYR   D  103 ? 1.4516 0.5432 1.5099 0.0862  -0.3604 0.2062  95  TYR   D N   
6408  C  CA  . TYR   D  103 ? 1.4590 0.5404 1.5018 0.0857  -0.3470 0.1894  95  TYR   D CA  
6409  C  C   . TYR   D  103 ? 1.4908 0.4913 1.5105 0.1065  -0.3582 0.1623  95  TYR   D C   
6410  O  O   . TYR   D  103 ? 1.4796 0.3834 1.4842 0.1202  -0.4164 0.1598  95  TYR   D O   
6411  C  CB  . TYR   D  103 ? 1.4557 0.5336 1.4712 0.0622  -0.3241 0.1938  95  TYR   D CB  
6412  C  CG  . TYR   D  103 ? 1.4276 0.5120 1.4546 0.0426  -0.2893 0.1762  95  TYR   D CG  
6413  C  CD1 . TYR   D  103 ? 1.4361 0.5567 1.4288 0.0551  -0.2834 0.1727  95  TYR   D CD1 
6414  C  CD2 . TYR   D  103 ? 1.4388 0.5074 1.4043 0.0347  -0.2649 0.1752  95  TYR   D CD2 
6415  C  CE1 . TYR   D  103 ? 1.4348 0.5873 1.4231 0.0399  -0.2691 0.1631  95  TYR   D CE1 
6416  C  CE2 . TYR   D  103 ? 1.4463 0.5566 1.3923 0.0388  -0.2599 0.1893  95  TYR   D CE2 
6417  C  CZ  . TYR   D  103 ? 1.4328 0.5866 1.3864 0.0340  -0.2601 0.1879  95  TYR   D CZ  
6418  O  OH  . TYR   D  103 ? 1.4319 0.7061 1.4052 0.0453  -0.2711 0.1446  95  TYR   D OH  
6419  N  N   . ASP   D  104 ? 1.5007 0.5112 1.5240 0.1058  -0.3455 0.1522  96  ASP   D N   
6420  C  CA  . ASP   D  104 ? 1.4819 0.6411 1.5577 0.1064  -0.3693 0.1340  96  ASP   D CA  
6421  C  C   . ASP   D  104 ? 1.4591 0.6457 1.5431 0.0955  -0.3681 0.1313  96  ASP   D C   
6422  O  O   . ASP   D  104 ? 1.4918 0.6055 1.5485 0.0763  -0.3774 0.1308  96  ASP   D O   
6423  C  CB  . ASP   D  104 ? 1.5107 0.6725 1.6446 0.0554  -0.3730 0.1211  96  ASP   D CB  
6424  C  CG  . ASP   D  104 ? 1.5474 0.7828 1.6870 0.0487  -0.4082 0.0864  96  ASP   D CG  
6425  O  OD1 . ASP   D  104 ? 1.5411 0.7599 1.7048 0.0598  -0.4230 0.1059  96  ASP   D OD1 
6426  O  OD2 . ASP   D  104 ? 1.6086 0.9039 1.8610 -0.0390 -0.3611 0.1378  96  ASP   D OD2 
6427  N  N   . GLU   D  105 ? 1.4171 0.6506 1.5018 0.1245  -0.3635 0.1060  97  GLU   D N   
6428  C  CA  . GLU   D  105 ? 1.4265 0.6913 1.5078 0.1538  -0.3597 0.0888  97  GLU   D CA  
6429  C  C   . GLU   D  105 ? 1.4137 0.6623 1.5054 0.1761  -0.3643 0.0631  97  GLU   D C   
6430  O  O   . GLU   D  105 ? 1.4091 0.5998 1.4630 0.1938  -0.3637 0.0706  97  GLU   D O   
6431  C  CB  . GLU   D  105 ? 1.4417 0.6958 1.5379 0.1581  -0.3319 0.0879  97  GLU   D CB  
6432  C  CG  . GLU   D  105 ? 1.4412 0.6610 1.5499 0.1386  -0.2923 0.0557  97  GLU   D CG  
6433  C  CD  . GLU   D  105 ? 1.4985 0.6981 1.5881 0.1564  -0.2487 0.0309  97  GLU   D CD  
6434  O  OE1 . GLU   D  105 ? 1.4607 0.6257 1.5746 0.1204  -0.1869 0.0499  97  GLU   D OE1 
6435  O  OE2 . GLU   D  105 ? 1.4733 0.7913 1.6302 0.1619  -0.2258 -0.0124 97  GLU   D OE2 
6436  N  N   . ASP   D  106 ? 1.4701 0.7380 1.5486 0.2465  -0.3446 0.0815  98  ASP   D N   
6437  C  CA  . ASP   D  106 ? 1.4891 0.7482 1.5638 0.2654  -0.3389 0.1302  98  ASP   D CA  
6438  C  C   . ASP   D  106 ? 1.4635 0.6636 1.5982 0.2428  -0.3895 0.1147  98  ASP   D C   
6439  O  O   . ASP   D  106 ? 1.4276 0.7325 1.6003 0.2341  -0.3925 0.0638  98  ASP   D O   
6440  C  CB  . ASP   D  106 ? 1.5042 0.8715 1.5385 0.3179  -0.3224 0.1345  98  ASP   D CB  
6441  C  CG  . ASP   D  106 ? 1.5070 0.9472 1.5510 0.3805  -0.3104 0.1081  98  ASP   D CG  
6442  O  OD1 . ASP   D  106 ? 1.6041 0.9971 1.5523 0.4167  -0.2308 0.0688  98  ASP   D OD1 
6443  O  OD2 . ASP   D  106 ? 1.4068 1.1460 1.5412 0.3671  -0.3439 0.1127  98  ASP   D OD2 
6444  N  N   . ILE   D  107 ? 1.4771 0.6022 1.6990 0.2486  -0.3982 0.1751  99  ILE   D N   
6445  C  CA  . ILE   D  107 ? 1.4972 0.5892 1.7432 0.2523  -0.3528 0.1501  99  ILE   D CA  
6446  C  C   . ILE   D  107 ? 1.5033 0.5422 1.7021 0.2205  -0.3635 0.1759  99  ILE   D C   
6447  O  O   . ILE   D  107 ? 1.4961 0.4593 1.6638 0.1982  -0.3958 0.1264  99  ILE   D O   
6448  C  CB  . ILE   D  107 ? 1.4862 0.4924 1.8138 0.2699  -0.3444 0.1718  99  ILE   D CB  
6449  C  CG1 . ILE   D  107 ? 1.5324 0.4890 1.8259 0.2483  -0.2994 0.1782  99  ILE   D CG1 
6450  C  CG2 . ILE   D  107 ? 1.4961 0.6110 1.7812 0.2517  -0.3220 0.1794  99  ILE   D CG2 
6451  C  CD1 . ILE   D  107 ? 1.5812 0.5472 1.8071 0.1963  -0.2810 0.1553  99  ILE   D CD1 
6452  N  N   . ASN   D  108 ? 1.5107 0.6345 1.7138 0.1676  -0.3345 0.1760  100 ASN   D N   
6453  C  CA  . ASN   D  108 ? 1.5038 0.7053 1.7016 0.2078  -0.3290 0.2263  100 ASN   D CA  
6454  C  C   . ASN   D  108 ? 1.4893 0.7405 1.6962 0.1869  -0.3335 0.2233  100 ASN   D C   
6455  O  O   . ASN   D  108 ? 1.4058 0.8239 1.7345 0.2527  -0.2569 0.1737  100 ASN   D O   
6456  C  CB  . ASN   D  108 ? 1.5373 0.7224 1.7036 0.1684  -0.3119 0.2833  100 ASN   D CB  
6457  C  CG  . ASN   D  108 ? 1.5932 0.6977 1.6672 0.1649  -0.2804 0.3039  100 ASN   D CG  
6458  O  OD1 . ASN   D  108 ? 1.6685 0.7045 1.6814 0.1363  -0.2448 0.3078  100 ASN   D OD1 
6459  N  ND2 . ASN   D  108 ? 1.6174 0.6454 1.6762 0.1688  -0.3014 0.3196  100 ASN   D ND2 
6460  N  N   . VAL   D  109 ? 1.5574 0.7256 1.6831 0.1672  -0.3570 0.2330  101 VAL   D N   
6461  C  CA  . VAL   D  109 ? 1.6059 0.7220 1.6754 0.1328  -0.3667 0.1889  101 VAL   D CA  
6462  C  C   . VAL   D  109 ? 1.6256 0.6891 1.6040 0.1462  -0.3320 0.2301  101 VAL   D C   
6463  O  O   . VAL   D  109 ? 1.6626 0.6788 1.5985 0.1223  -0.3345 0.1543  101 VAL   D O   
6464  C  CB  . VAL   D  109 ? 1.6128 0.7579 1.7496 0.1591  -0.4039 0.1639  101 VAL   D CB  
6465  C  CG1 . VAL   D  109 ? 1.6161 0.7467 1.7539 0.1667  -0.4121 0.1675  101 VAL   D CG1 
6466  C  CG2 . VAL   D  109 ? 1.6520 0.7917 1.7659 0.1395  -0.4008 0.1365  101 VAL   D CG2 
6467  N  N   . GLU   D  110 ? 1.6307 0.6441 1.5895 0.1425  -0.3331 0.2607  102 GLU   D N   
6468  C  CA  . GLU   D  110 ? 1.6522 0.7084 1.5735 0.1291  -0.3125 0.2588  102 GLU   D CA  
6469  C  C   . GLU   D  110 ? 1.6320 0.6986 1.5442 0.1240  -0.3172 0.2134  102 GLU   D C   
6470  O  O   . GLU   D  110 ? 1.6268 0.5298 1.5046 0.1799  -0.3136 0.2500  102 GLU   D O   
6471  C  CB  . GLU   D  110 ? 1.6957 0.8718 1.6283 0.0843  -0.2732 0.2958  102 GLU   D CB  
6472  C  CG  . GLU   D  110 ? 1.7595 0.9774 1.6515 0.0616  -0.2580 0.2414  102 GLU   D CG  
6473  C  CD  . GLU   D  110 ? 1.8193 1.1867 1.6574 0.0387  -0.2039 0.2403  102 GLU   D CD  
6474  O  OE1 . GLU   D  110 ? 1.8480 1.2152 1.7716 0.1147  -0.1982 0.2003  102 GLU   D OE1 
6475  O  OE2 . GLU   D  110 ? 1.8207 1.5215 1.6511 0.1073  -0.2608 0.2319  102 GLU   D OE2 
6476  N  N   . SER   D  111 ? 1.6160 0.7117 1.5518 0.1531  -0.3558 0.1725  103 SER   D N   
6477  C  CA  . SER   D  111 ? 1.6032 0.7215 1.5107 0.1340  -0.3684 0.1776  103 SER   D CA  
6478  C  C   . SER   D  111 ? 1.6131 0.5903 1.4748 0.1711  -0.3550 0.1641  103 SER   D C   
6479  O  O   . SER   D  111 ? 1.6057 0.5021 1.5209 0.1937  -0.3559 0.1347  103 SER   D O   
6480  C  CB  . SER   D  111 ? 1.5924 0.7511 1.4972 0.0728  -0.3915 0.1679  103 SER   D CB  
6481  O  OG  . SER   D  111 ? 1.6563 0.9404 1.4950 0.0117  -0.3544 0.1481  103 SER   D OG  
6482  N  N   . LEU   D  112 ? 1.5921 0.4794 1.4639 0.1441  -0.3627 0.1248  104 LEU   D N   
6483  C  CA  . LEU   D  112 ? 1.6268 0.4556 1.4361 0.1265  -0.3717 0.1606  104 LEU   D CA  
6484  C  C   . LEU   D  112 ? 1.6301 0.5022 1.4422 0.0800  -0.3821 0.1455  104 LEU   D C   
6485  O  O   . LEU   D  112 ? 1.6465 0.6504 1.4443 0.0646  -0.4218 0.1822  104 LEU   D O   
6486  C  CB  . LEU   D  112 ? 1.6409 0.2986 1.4277 0.1095  -0.3669 0.1528  104 LEU   D CB  
6487  C  CG  . LEU   D  112 ? 1.6475 0.3062 1.3999 0.1189  -0.3716 0.1528  104 LEU   D CG  
6488  C  CD1 . LEU   D  112 ? 1.6749 0.3295 1.4142 0.0755  -0.3654 0.1683  104 LEU   D CD1 
6489  C  CD2 . LEU   D  112 ? 1.6490 0.2697 1.3596 0.1138  -0.3605 0.1645  104 LEU   D CD2 
6490  N  N   . THR   D  113 ? 1.6151 0.6129 1.4712 0.1254  -0.3631 0.1584  105 THR   D N   
6491  C  CA  . THR   D  113 ? 1.6484 0.6292 1.4823 0.0914  -0.3482 0.1503  105 THR   D CA  
6492  C  C   . THR   D  113 ? 1.6682 0.6550 1.4492 0.1130  -0.3178 0.1828  105 THR   D C   
6493  O  O   . THR   D  113 ? 1.6696 0.7043 1.4812 0.0960  -0.3113 0.1589  105 THR   D O   
6494  C  CB  . THR   D  113 ? 1.6323 0.6682 1.5418 0.0858  -0.3463 0.1648  105 THR   D CB  
6495  O  OG1 . THR   D  113 ? 1.6764 0.7405 1.5177 0.0277  -0.3104 0.1516  105 THR   D OG1 
6496  C  CG2 . THR   D  113 ? 1.6580 0.6553 1.5424 0.1192  -0.3551 0.1629  105 THR   D CG2 
6497  N  N   . GLN   D  114 ? 1.6731 0.6614 1.4425 0.1509  -0.3141 0.2056  106 GLN   D N   
6498  C  CA  . GLN   D  114 ? 1.6570 0.6765 1.4374 0.1635  -0.3038 0.2165  106 GLN   D CA  
6499  C  C   . GLN   D  114 ? 1.6384 0.6409 1.3681 0.1372  -0.3472 0.2085  106 GLN   D C   
6500  O  O   . GLN   D  114 ? 1.6297 0.4510 1.3331 0.1686  -0.3243 0.2130  106 GLN   D O   
6501  C  CB  . GLN   D  114 ? 1.6746 0.7542 1.4195 0.1621  -0.2880 0.2385  106 GLN   D CB  
6502  C  CG  . GLN   D  114 ? 1.6516 0.8012 1.4010 0.1608  -0.2662 0.2274  106 GLN   D CG  
6503  C  CD  . GLN   D  114 ? 1.6164 0.8329 1.3667 0.1737  -0.2494 0.2074  106 GLN   D CD  
6504  O  OE1 . GLN   D  114 ? 1.5728 0.9258 1.3692 0.1720  -0.2501 0.2428  106 GLN   D OE1 
6505  N  NE2 . GLN   D  114 ? 1.6478 0.8970 1.3687 0.2020  -0.2202 0.2169  106 GLN   D NE2 
6506  N  N   . SER   D  115 ? 1.6824 0.7091 1.3583 0.1651  -0.3371 0.1951  107 SER   D N   
6507  C  CA  . SER   D  115 ? 1.6917 0.7439 1.3282 0.1720  -0.3597 0.1840  107 SER   D CA  
6508  C  C   . SER   D  115 ? 1.7401 0.7510 1.2748 0.1478  -0.3777 0.2063  107 SER   D C   
6509  O  O   . SER   D  115 ? 1.7714 0.6868 1.1711 0.1193  -0.3954 0.2751  107 SER   D O   
6510  C  CB  . SER   D  115 ? 1.7427 0.7773 1.3832 0.1441  -0.3793 0.1368  107 SER   D CB  
6511  O  OG  . SER   D  115 ? 1.7513 0.8232 1.4167 0.1667  -0.3694 0.0393  107 SER   D OG  
6512  N  N   . VAL   D  116 ? 1.8074 0.7666 1.2477 0.1481  -0.3423 0.2118  108 VAL   D N   
6513  C  CA  . VAL   D  116 ? 1.7922 0.7920 1.2288 0.1353  -0.3209 0.1727  108 VAL   D CA  
6514  C  C   . VAL   D  116 ? 1.7997 0.8498 1.2691 0.1387  -0.2907 0.1171  108 VAL   D C   
6515  O  O   . VAL   D  116 ? 1.7379 0.8830 1.1830 0.1970  -0.2712 0.0749  108 VAL   D O   
6516  C  CB  . VAL   D  116 ? 1.8023 0.7682 1.2557 0.1543  -0.3323 0.1906  108 VAL   D CB  
6517  C  CG1 . VAL   D  116 ? 1.8216 0.7503 1.2025 0.1654  -0.3580 0.2063  108 VAL   D CG1 
6518  C  CG2 . VAL   D  116 ? 1.7811 0.7832 1.2048 0.1564  -0.3574 0.2125  108 VAL   D CG2 
6519  N  N   . CYS   D  117 ? 1.8154 0.8415 1.3180 0.1297  -0.2741 0.0840  109 CYS   D N   
6520  C  CA  . CYS   D  117 ? 1.8223 0.7753 1.3669 0.0930  -0.2889 0.0877  109 CYS   D CA  
6521  C  C   . CYS   D  117 ? 1.8057 0.7594 1.3460 0.0538  -0.2787 0.0962  109 CYS   D C   
6522  O  O   . CYS   D  117 ? 1.8125 0.6188 1.3372 0.0542  -0.2584 0.1656  109 CYS   D O   
6523  C  CB  . CYS   D  117 ? 1.8256 0.7966 1.4173 0.0869  -0.2748 0.0424  109 CYS   D CB  
6524  S  SG  . CYS   D  117 ? 1.8495 0.8189 1.5106 0.1281  -0.3239 0.0228  109 CYS   D SG  
6525  N  N   . ASP   D  118 ? 1.7839 0.7986 1.3521 0.1055  -0.2800 0.1513  110 ASP   D N   
6526  C  CA  . ASP   D  118 ? 1.7585 0.8807 1.3333 0.0919  -0.2873 0.1336  110 ASP   D CA  
6527  C  C   . ASP   D  118 ? 1.7592 0.8295 1.3402 0.0937  -0.2922 0.1575  110 ASP   D C   
6528  O  O   . ASP   D  118 ? 1.7354 0.8443 1.3281 0.1174  -0.2772 0.1642  110 ASP   D O   
6529  C  CB  . ASP   D  118 ? 1.7858 0.8874 1.3634 0.0771  -0.2739 0.1200  110 ASP   D CB  
6530  C  CG  . ASP   D  118 ? 1.7943 0.9251 1.3831 0.0624  -0.2624 0.1049  110 ASP   D CG  
6531  O  OD1 . ASP   D  118 ? 1.8310 1.0552 1.3875 0.1064  -0.2591 0.0400  110 ASP   D OD1 
6532  O  OD2 . ASP   D  118 ? 1.7818 0.9609 1.3813 -0.0162 -0.2862 0.2571  110 ASP   D OD2 
6533  N  N   . LEU   D  119 ? 1.7648 0.8070 1.3269 0.0904  -0.3132 0.1650  111 LEU   D N   
6534  C  CA  . LEU   D  119 ? 1.7376 0.9339 1.3495 0.1204  -0.3168 0.1783  111 LEU   D CA  
6535  C  C   . LEU   D  119 ? 1.7131 0.9868 1.3968 0.1522  -0.3726 0.1190  111 LEU   D C   
6536  O  O   . LEU   D  119 ? 1.7530 1.1339 1.2185 0.1908  -0.4844 0.1803  111 LEU   D O   
6537  C  CB  . LEU   D  119 ? 1.7769 0.8396 1.3552 0.1149  -0.3076 0.1002  111 LEU   D CB  
6538  C  CG  . LEU   D  119 ? 1.7680 0.8035 1.3935 0.1631  -0.3108 0.1453  111 LEU   D CG  
6539  C  CD1 . LEU   D  119 ? 1.7907 0.8012 1.3952 0.1888  -0.2979 0.1123  111 LEU   D CD1 
6540  C  CD2 . LEU   D  119 ? 1.7413 0.8671 1.3457 0.1388  -0.3212 0.1458  111 LEU   D CD2 
6541  N  N   . ALA   D  120 ? 1.7216 1.1601 1.5843 0.2328  -0.3239 0.1019  112 ALA   D N   
6542  C  CA  . ALA   D  120 ? 1.7026 1.1832 1.6642 0.2069  -0.3438 0.0415  112 ALA   D CA  
6543  C  C   . ALA   D  120 ? 1.6014 1.3424 1.5839 0.2569  -0.3544 0.1370  112 ALA   D C   
6544  O  O   . ALA   D  120 ? 1.4585 1.6298 1.6897 0.2263  -0.4013 0.0766  112 ALA   D O   
6545  C  CB  . ALA   D  120 ? 1.6908 1.2630 1.8052 0.1989  -0.2992 0.0169  112 ALA   D CB  
6546  N  N   . LEU   D  121 ? 1.5905 1.2771 1.5521 0.2939  -0.4201 0.1957  113 LEU   D N   
6547  C  CA  . LEU   D  121 ? 1.6503 1.2382 1.4850 0.2814  -0.3767 0.2180  113 LEU   D CA  
6548  C  C   . LEU   D  121 ? 1.6972 1.1034 1.4128 0.2674  -0.3658 0.2345  113 LEU   D C   
6549  O  O   . LEU   D  121 ? 1.7243 0.9567 1.2982 0.3310  -0.3334 0.3219  113 LEU   D O   
6550  C  CB  . LEU   D  121 ? 1.6787 1.2974 1.4581 0.2761  -0.3835 0.2214  113 LEU   D CB  
6551  C  CG  . LEU   D  121 ? 1.7420 1.2298 1.4713 0.2769  -0.4238 0.2656  113 LEU   D CG  
6552  C  CD1 . LEU   D  121 ? 1.7533 1.2955 1.4915 0.2924  -0.4063 0.2611  113 LEU   D CD1 
6553  C  CD2 . LEU   D  121 ? 1.7390 1.1600 1.4451 0.3339  -0.4538 0.2689  113 LEU   D CD2 
6554  N  N   . ARG   D  122 ? 1.7493 1.0816 1.5121 0.2748  -0.2946 0.2433  114 ARG   D N   
6555  C  CA  . ARG   D  122 ? 1.7519 1.0760 1.4929 0.2597  -0.3100 0.3095  114 ARG   D CA  
6556  C  C   . ARG   D  122 ? 1.6811 0.9834 1.4682 0.3149  -0.3319 0.2710  114 ARG   D C   
6557  O  O   . ARG   D  122 ? 1.5842 0.9807 1.5286 0.3751  -0.3819 0.2845  114 ARG   D O   
6558  C  CB  . ARG   D  122 ? 1.8202 1.1245 1.5702 0.1955  -0.3086 0.2507  114 ARG   D CB  
6559  C  CG  . ARG   D  122 ? 1.8731 1.1929 1.6539 0.0497  -0.2879 0.2391  114 ARG   D CG  
6560  C  CD  . ARG   D  122 ? 1.9675 1.1628 1.8084 0.0436  -0.2436 0.2493  114 ARG   D CD  
6561  N  NE  . ARG   D  122 ? 2.0389 1.2285 1.9232 -0.0133 -0.2822 0.2605  114 ARG   D NE  
6562  C  CZ  . ARG   D  122 ? 2.1313 1.3200 1.9718 0.0198  -0.1551 0.4203  114 ARG   D CZ  
6563  N  NH1 . ARG   D  122 ? 2.2018 1.2638 1.9263 0.0917  -0.2138 0.4957  114 ARG   D NH1 
6564  N  NH2 . ARG   D  122 ? 2.1513 1.4505 2.1054 -0.0316 -0.2048 0.3974  114 ARG   D NH2 
6565  N  N   . PHE   D  123 ? 1.6709 0.9731 1.4691 0.2593  -0.3349 0.2885  115 PHE   D N   
6566  C  CA  . PHE   D  123 ? 1.6928 1.0249 1.5397 0.2325  -0.2854 0.3202  115 PHE   D CA  
6567  C  C   . PHE   D  123 ? 1.7262 1.0500 1.4975 0.1971  -0.2527 0.3686  115 PHE   D C   
6568  O  O   . PHE   D  123 ? 1.7585 0.9425 1.5898 0.1683  -0.2359 0.4734  115 PHE   D O   
6569  C  CB  . PHE   D  123 ? 1.6975 1.0230 1.5872 0.2513  -0.2832 0.3268  115 PHE   D CB  
6570  C  CG  . PHE   D  123 ? 1.7674 0.9530 1.6542 0.2615  -0.2792 0.3278  115 PHE   D CG  
6571  C  CD1 . PHE   D  123 ? 1.7693 0.9351 1.6963 0.2808  -0.2487 0.3372  115 PHE   D CD1 
6572  C  CD2 . PHE   D  123 ? 1.7289 0.8968 1.6500 0.2749  -0.2959 0.3617  115 PHE   D CD2 
6573  C  CE1 . PHE   D  123 ? 1.8000 0.8602 1.7044 0.3036  -0.2714 0.3750  115 PHE   D CE1 
6574  C  CE2 . PHE   D  123 ? 1.7895 0.8268 1.6294 0.2667  -0.3047 0.3628  115 PHE   D CE2 
6575  C  CZ  . PHE   D  123 ? 1.7847 0.8570 1.6688 0.2976  -0.2756 0.3871  115 PHE   D CZ  
6576  N  N   . GLY   D  124 ? 1.7573 1.1729 1.5429 0.1506  -0.2707 0.2947  116 GLY   D N   
6577  C  CA  . GLY   D  124 ? 1.8033 1.2613 1.5569 0.1657  -0.2643 0.2378  116 GLY   D CA  
6578  C  C   . GLY   D  124 ? 1.8012 1.2665 1.5841 0.1825  -0.2083 0.1979  116 GLY   D C   
6579  O  O   . GLY   D  124 ? 1.6841 1.1303 1.6800 0.2382  -0.2072 0.0343  116 GLY   D O   
6580  N  N   . GLU   D  125 ? 1.9179 1.3315 1.6115 0.1806  -0.2491 0.2649  117 GLU   D N   
6581  C  CA  . GLU   D  125 ? 1.9332 1.4228 1.6840 0.1872  -0.2701 0.2028  117 GLU   D CA  
6582  C  C   . GLU   D  125 ? 1.9913 1.4807 1.6784 0.2884  -0.2372 0.2120  117 GLU   D C   
6583  O  O   . GLU   D  125 ? 2.0852 1.5944 1.5625 0.4951  -0.2634 0.1651  117 GLU   D O   
6584  C  CB  . GLU   D  125 ? 2.1188 1.4418 1.7383 0.1208  -0.2816 0.1931  117 GLU   D CB  
6585  C  CG  . GLU   D  125 ? 2.1388 1.4637 1.8129 0.0469  -0.2813 0.0898  117 GLU   D CG  
6586  C  CD  . GLU   D  125 ? 2.2395 1.3482 1.9004 0.0296  -0.3272 -0.0127 117 GLU   D CD  
6587  O  OE1 . GLU   D  125 ? 2.3043 1.2420 1.9563 0.0660  -0.4184 -0.1182 117 GLU   D OE1 
6588  O  OE2 . GLU   D  125 ? 2.3186 1.2927 1.9168 0.0757  -0.3586 -0.0565 117 GLU   D OE2 
6589  N  N   . LEU   D  133 ? 1.8356 1.1137 1.4587 0.0940  -0.1771 0.3458  125 LEU   D N   
6590  C  CA  . LEU   D  133 ? 1.8616 1.1629 1.5230 0.1289  -0.2079 0.3300  125 LEU   D CA  
6591  C  C   . LEU   D  133 ? 1.7665 1.1364 1.5202 0.1149  -0.2237 0.2746  125 LEU   D C   
6592  O  O   . LEU   D  133 ? 1.7445 1.1087 1.5352 0.1562  -0.2127 0.1706  125 LEU   D O   
6593  C  CB  . LEU   D  133 ? 1.9015 1.2328 1.4572 0.1094  -0.2211 0.3436  125 LEU   D CB  
6594  C  CG  . LEU   D  133 ? 1.8954 1.2041 1.4230 0.1534  -0.2480 0.4533  125 LEU   D CG  
6595  C  CD1 . LEU   D  133 ? 1.8558 1.2788 1.4477 0.1124  -0.2802 0.4015  125 LEU   D CD1 
6596  C  CD2 . LEU   D  133 ? 1.9007 1.1586 1.3196 0.1687  -0.2975 0.4945  125 LEU   D CD2 
6597  N  N   . MET   D  134 ? 1.8162 0.9032 1.5515 0.0461  -0.2524 0.2543  126 MET   D N   
6598  C  CA  . MET   D  134 ? 1.7880 0.7858 1.5586 0.0514  -0.2896 0.2108  126 MET   D CA  
6599  C  C   . MET   D  134 ? 1.7704 0.8857 1.4852 0.0949  -0.3491 0.1541  126 MET   D C   
6600  O  O   . MET   D  134 ? 1.7818 0.9989 1.4728 0.1885  -0.3545 0.1985  126 MET   D O   
6601  C  CB  . MET   D  134 ? 1.7574 0.6277 1.5782 0.0157  -0.3079 0.1551  126 MET   D CB  
6602  C  CG  . MET   D  134 ? 1.7600 0.5488 1.5938 0.0059  -0.3174 0.1156  126 MET   D CG  
6603  S  SD  . MET   D  134 ? 1.8042 0.3642 1.6174 0.0024  -0.3010 0.0419  126 MET   D SD  
6604  C  CE  . MET   D  134 ? 1.8029 0.4473 1.6333 0.0405  -0.3045 0.0468  126 MET   D CE  
6605  N  N   . SER   D  135 ? 1.7180 0.8270 1.4006 0.1135  -0.4287 0.1443  127 SER   D N   
6606  C  CA  . SER   D  135 ? 1.6799 0.8317 1.3387 0.1254  -0.4431 0.1500  127 SER   D CA  
6607  C  C   . SER   D  135 ? 1.7182 0.7825 1.3129 0.1162  -0.4000 0.1089  127 SER   D C   
6608  O  O   . SER   D  135 ? 1.6279 0.7781 1.3201 0.1596  -0.4101 0.0962  127 SER   D O   
6609  C  CB  . SER   D  135 ? 1.6472 0.9086 1.2513 0.1319  -0.4837 0.1388  127 SER   D CB  
6610  O  OG  . SER   D  135 ? 1.6591 1.0187 1.1825 0.1539  -0.5361 0.0997  127 SER   D OG  
6611  N  N   . ARG   D  136 ? 1.7376 0.7378 1.3281 0.0992  -0.4088 0.1300  128 ARG   D N   
6612  C  CA  . ARG   D  136 ? 1.7928 0.6591 1.3855 0.0912  -0.3612 0.1112  128 ARG   D CA  
6613  C  C   . ARG   D  136 ? 1.7496 0.6488 1.4157 0.1065  -0.3394 0.1188  128 ARG   D C   
6614  O  O   . ARG   D  136 ? 1.7677 0.6381 1.4936 -0.0099 -0.3262 0.1073  128 ARG   D O   
6615  C  CB  . ARG   D  136 ? 1.8721 0.6069 1.4013 0.1122  -0.3687 0.1179  128 ARG   D CB  
6616  C  CG  . ARG   D  136 ? 1.9093 0.6001 1.3880 0.1055  -0.3578 0.1409  128 ARG   D CG  
6617  C  CD  . ARG   D  136 ? 1.9579 0.5440 1.4014 0.0626  -0.3404 0.1483  128 ARG   D CD  
6618  N  NE  . ARG   D  136 ? 1.9777 0.5032 1.4326 0.0483  -0.3321 0.0870  128 ARG   D NE  
6619  C  CZ  . ARG   D  136 ? 1.9762 0.4996 1.4346 0.0151  -0.3169 0.0635  128 ARG   D CZ  
6620  N  NH1 . ARG   D  136 ? 1.9628 0.5246 1.4571 -0.0301 -0.3161 0.0527  128 ARG   D NH1 
6621  N  NH2 . ARG   D  136 ? 2.0095 0.4737 1.4361 0.0239  -0.3380 0.0351  128 ARG   D NH2 
6622  N  N   . PRO   D  137 ? 1.7682 0.5829 1.3434 0.1250  -0.3736 0.1235  129 PRO   D N   
6623  C  CA  . PRO   D  137 ? 1.7871 0.5645 1.3302 0.1464  -0.3984 0.1157  129 PRO   D CA  
6624  C  C   . PRO   D  137 ? 1.7796 0.4947 1.3269 0.1365  -0.4483 0.0762  129 PRO   D C   
6625  O  O   . PRO   D  137 ? 1.7683 0.4547 1.3800 0.1502  -0.4316 0.0660  129 PRO   D O   
6626  C  CB  . PRO   D  137 ? 1.7942 0.5998 1.3015 0.1498  -0.3691 0.1292  129 PRO   D CB  
6627  C  CG  . PRO   D  137 ? 1.7891 0.6261 1.3096 0.1212  -0.3652 0.1282  129 PRO   D CG  
6628  C  CD  . PRO   D  137 ? 1.7827 0.5990 1.3196 0.1168  -0.3715 0.1186  129 PRO   D CD  
6629  N  N   . PHE   D  138 ? 1.7939 0.5099 1.4100 0.1374  -0.4857 0.0526  130 PHE   D N   
6630  C  CA  . PHE   D  138 ? 1.7413 0.5336 1.4156 0.1008  -0.5112 0.0259  130 PHE   D CA  
6631  C  C   . PHE   D  138 ? 1.7128 0.4715 1.3846 0.0400  -0.5040 -0.0231 130 PHE   D C   
6632  O  O   . PHE   D  138 ? 1.6980 0.4518 1.4243 0.0142  -0.5229 -0.0851 130 PHE   D O   
6633  C  CB  . PHE   D  138 ? 1.7212 0.5308 1.4518 0.1022  -0.5241 0.0567  130 PHE   D CB  
6634  C  CG  . PHE   D  138 ? 1.7194 0.5319 1.4510 0.0982  -0.4961 0.0855  130 PHE   D CG  
6635  C  CD1 . PHE   D  138 ? 1.7064 0.4934 1.4530 0.0827  -0.4893 0.0981  130 PHE   D CD1 
6636  C  CD2 . PHE   D  138 ? 1.7331 0.5399 1.4426 0.1094  -0.4822 0.0867  130 PHE   D CD2 
6637  C  CE1 . PHE   D  138 ? 1.6784 0.5177 1.4517 0.1116  -0.4999 0.1141  130 PHE   D CE1 
6638  C  CE2 . PHE   D  138 ? 1.7261 0.5719 1.4237 0.1526  -0.4789 0.1105  130 PHE   D CE2 
6639  C  CZ  . PHE   D  138 ? 1.6914 0.5745 1.4305 0.1429  -0.4861 0.1459  130 PHE   D CZ  
6640  N  N   . GLY   D  139 ? 1.7143 0.4223 1.3793 0.0312  -0.5080 -0.0252 131 GLY   D N   
6641  C  CA  . GLY   D  139 ? 1.7356 0.4410 1.3971 0.0471  -0.5058 -0.0130 131 GLY   D CA  
6642  C  C   . GLY   D  139 ? 1.7425 0.4921 1.3955 0.0495  -0.5048 -0.0290 131 GLY   D C   
6643  O  O   . GLY   D  139 ? 1.7866 0.4309 1.4135 0.0601  -0.4780 -0.0501 131 GLY   D O   
6644  N  N   . VAL   D  140 ? 1.7127 0.4859 1.3854 0.0748  -0.4840 0.0752  132 VAL   D N   
6645  C  CA  . VAL   D  140 ? 1.6935 0.5038 1.3907 0.1232  -0.4977 0.0988  132 VAL   D CA  
6646  C  C   . VAL   D  140 ? 1.6895 0.4840 1.3786 0.1621  -0.4958 0.1448  132 VAL   D C   
6647  O  O   . VAL   D  140 ? 1.6417 0.5162 1.3251 0.2610  -0.5372 0.1160  132 VAL   D O   
6648  C  CB  . VAL   D  140 ? 1.7033 0.4534 1.3831 0.1111  -0.4982 0.1141  132 VAL   D CB  
6649  C  CG1 . VAL   D  140 ? 1.6948 0.5055 1.3342 0.1226  -0.5098 0.1428  132 VAL   D CG1 
6650  C  CG2 . VAL   D  140 ? 1.7044 0.4225 1.3854 0.1270  -0.5021 0.1218  132 VAL   D CG2 
6651  N  N   . ALA   D  141 ? 1.6648 0.5005 1.4479 0.1622  -0.4817 0.1460  133 ALA   D N   
6652  C  CA  . ALA   D  141 ? 1.6975 0.4770 1.4699 0.1315  -0.4562 0.1536  133 ALA   D CA  
6653  C  C   . ALA   D  141 ? 1.6898 0.4858 1.4645 0.1219  -0.4724 0.1680  133 ALA   D C   
6654  O  O   . ALA   D  141 ? 1.6533 0.4200 1.4780 0.0930  -0.5032 0.2165  133 ALA   D O   
6655  C  CB  . ALA   D  141 ? 1.6992 0.5136 1.4937 0.1484  -0.4444 0.1368  133 ALA   D CB  
6656  N  N   . LEU   D  142 ? 1.6850 0.5461 1.4797 0.0910  -0.4462 0.1641  134 LEU   D N   
6657  C  CA  . LEU   D  142 ? 1.7538 0.5995 1.4580 0.0798  -0.4482 0.1446  134 LEU   D CA  
6658  C  C   . LEU   D  142 ? 1.7608 0.6149 1.4487 0.0828  -0.4492 0.1794  134 LEU   D C   
6659  O  O   . LEU   D  142 ? 1.8053 0.6296 1.4884 0.1220  -0.3981 0.2018  134 LEU   D O   
6660  C  CB  . LEU   D  142 ? 1.7742 0.5539 1.4308 0.0548  -0.4335 0.0892  134 LEU   D CB  
6661  C  CG  . LEU   D  142 ? 1.7778 0.5331 1.3958 0.0343  -0.4409 0.0587  134 LEU   D CG  
6662  C  CD1 . LEU   D  142 ? 1.7696 0.5417 1.3759 0.0612  -0.4553 0.0521  134 LEU   D CD1 
6663  C  CD2 . LEU   D  142 ? 1.8203 0.5646 1.3678 -0.0145 -0.4448 0.0196  134 LEU   D CD2 
6664  N  N   . LEU   D  143 ? 1.7923 0.6327 1.4560 0.0408  -0.4672 0.1659  135 LEU   D N   
6665  C  CA  . LEU   D  143 ? 1.7946 0.6623 1.4605 0.0258  -0.4583 0.1567  135 LEU   D CA  
6666  C  C   . LEU   D  143 ? 1.7688 0.6447 1.3929 0.0229  -0.4471 0.2005  135 LEU   D C   
6667  O  O   . LEU   D  143 ? 1.7599 0.8035 1.3888 0.0086  -0.4553 0.1684  135 LEU   D O   
6668  C  CB  . LEU   D  143 ? 1.8364 0.6713 1.4950 0.0286  -0.4840 0.1638  135 LEU   D CB  
6669  C  CG  . LEU   D  143 ? 1.8870 0.6852 1.4922 -0.0051 -0.4865 0.1152  135 LEU   D CG  
6670  C  CD1 . LEU   D  143 ? 1.9364 0.6786 1.5119 -0.0026 -0.4999 0.1246  135 LEU   D CD1 
6671  C  CD2 . LEU   D  143 ? 1.8897 0.6952 1.4881 -0.0195 -0.4811 0.1047  135 LEU   D CD2 
6672  N  N   . ILE   D  144 ? 1.7484 0.6032 1.3856 0.0602  -0.4413 0.1974  136 ILE   D N   
6673  C  CA  . ILE   D  144 ? 1.7074 0.5753 1.3954 0.0920  -0.4265 0.2328  136 ILE   D CA  
6674  C  C   . ILE   D  144 ? 1.7208 0.4556 1.3887 0.0997  -0.4465 0.2364  136 ILE   D C   
6675  O  O   . ILE   D  144 ? 1.7291 0.4536 1.4303 0.0875  -0.4216 0.2419  136 ILE   D O   
6676  C  CB  . ILE   D  144 ? 1.6790 0.5415 1.3882 0.0956  -0.4074 0.2217  136 ILE   D CB  
6677  C  CG1 . ILE   D  144 ? 1.6806 0.5122 1.3641 0.0599  -0.3804 0.2260  136 ILE   D CG1 
6678  C  CG2 . ILE   D  144 ? 1.6916 0.5546 1.4083 0.0828  -0.4115 0.2202  136 ILE   D CG2 
6679  C  CD1 . ILE   D  144 ? 1.6485 0.5281 1.3563 0.0637  -0.3677 0.2251  136 ILE   D CD1 
6680  N  N   . ALA   D  145 ? 1.7077 0.4363 1.3777 0.1266  -0.4626 0.2527  137 ALA   D N   
6681  C  CA  . ALA   D  145 ? 1.6976 0.5869 1.4319 0.1318  -0.4704 0.2255  137 ALA   D CA  
6682  C  C   . ALA   D  145 ? 1.6789 0.5965 1.4340 0.1140  -0.4721 0.2230  137 ALA   D C   
6683  O  O   . ALA   D  145 ? 1.6766 0.7276 1.4465 0.1424  -0.4669 0.2297  137 ALA   D O   
6684  C  CB  . ALA   D  145 ? 1.6994 0.5780 1.4412 0.1244  -0.4869 0.2216  137 ALA   D CB  
6685  N  N   . GLY   D  146 ? 1.6580 0.7151 1.4619 0.0928  -0.4442 0.2007  138 GLY   D N   
6686  C  CA  . GLY   D  146 ? 1.6342 0.7348 1.4694 0.0713  -0.4448 0.1547  138 GLY   D CA  
6687  C  C   . GLY   D  146 ? 1.6281 0.7342 1.4815 0.0608  -0.4708 0.1006  138 GLY   D C   
6688  O  O   . GLY   D  146 ? 1.5952 0.7771 1.4363 0.0517  -0.4896 0.0583  138 GLY   D O   
6689  N  N   . HIS   D  147 ? 1.5853 0.7352 1.5190 0.0689  -0.4673 0.0856  139 HIS   D N   
6690  C  CA  . HIS   D  147 ? 1.5914 0.7435 1.5902 0.0555  -0.4503 0.0525  139 HIS   D CA  
6691  C  C   . HIS   D  147 ? 1.6146 0.6800 1.6085 0.0151  -0.4173 0.0144  139 HIS   D C   
6692  O  O   . HIS   D  147 ? 1.6644 0.6045 1.6590 -0.0311 -0.3848 -0.1059 139 HIS   D O   
6693  C  CB  . HIS   D  147 ? 1.5610 0.7124 1.6016 0.0322  -0.4486 0.0561  139 HIS   D CB  
6694  C  CG  . HIS   D  147 ? 1.5658 0.7383 1.6190 0.0162  -0.4496 0.0439  139 HIS   D CG  
6695  N  ND1 . HIS   D  147 ? 1.5238 0.7388 1.5926 0.0235  -0.4329 0.0405  139 HIS   D ND1 
6696  C  CD2 . HIS   D  147 ? 1.5594 0.7543 1.6476 0.0038  -0.4485 0.0503  139 HIS   D CD2 
6697  C  CE1 . HIS   D  147 ? 1.5460 0.7875 1.6328 0.0005  -0.4037 0.0637  139 HIS   D CE1 
6698  N  NE2 . HIS   D  147 ? 1.5872 0.7582 1.6564 -0.0039 -0.4341 0.0839  139 HIS   D NE2 
6699  N  N   . ASP   D  148 ? 1.5939 0.7036 1.6441 0.0217  -0.4073 0.0256  140 ASP   D N   
6700  C  CA  . ASP   D  148 ? 1.5852 0.7276 1.6763 0.0565  -0.4349 0.0692  140 ASP   D CA  
6701  C  C   . ASP   D  148 ? 1.5667 0.7994 1.7511 0.0791  -0.4436 0.0541  140 ASP   D C   
6702  O  O   . ASP   D  148 ? 1.5476 0.8024 1.7432 0.0742  -0.5145 0.0195  140 ASP   D O   
6703  C  CB  . ASP   D  148 ? 1.5543 0.6896 1.6972 0.0899  -0.4400 0.1074  140 ASP   D CB  
6704  C  CG  . ASP   D  148 ? 1.5296 0.6653 1.7014 0.1277  -0.4376 0.1364  140 ASP   D CG  
6705  O  OD1 . ASP   D  148 ? 1.5151 0.6599 1.7260 0.1492  -0.4462 0.1209  140 ASP   D OD1 
6706  O  OD2 . ASP   D  148 ? 1.4997 0.6414 1.6856 0.1295  -0.4449 0.1934  140 ASP   D OD2 
6707  N  N   . ALA   D  149 ? 1.6075 0.8501 1.8116 0.0127  -0.3838 0.0850  141 ALA   D N   
6708  C  CA  . ALA   D  149 ? 1.5838 0.9750 1.8549 0.0155  -0.3199 0.0863  141 ALA   D CA  
6709  C  C   . ALA   D  149 ? 1.5515 1.0004 1.9044 0.0276  -0.2792 0.0988  141 ALA   D C   
6710  O  O   . ALA   D  149 ? 1.5425 1.0000 1.9515 -0.0624 -0.2505 0.1045  141 ALA   D O   
6711  C  CB  . ALA   D  149 ? 1.5748 0.9688 1.8782 -0.0494 -0.3230 0.0687  141 ALA   D CB  
6712  N  N   . ASP   D  150 ? 1.5884 1.0249 1.8577 0.0628  -0.2644 0.0951  142 ASP   D N   
6713  C  CA  . ASP   D  150 ? 1.6245 1.1042 1.8455 0.0713  -0.2502 0.1282  142 ASP   D CA  
6714  C  C   . ASP   D  150 ? 1.6733 1.0852 1.8579 0.0482  -0.2415 0.1409  142 ASP   D C   
6715  O  O   . ASP   D  150 ? 1.6925 1.1720 1.9032 0.0605  -0.2058 0.1509  142 ASP   D O   
6716  C  CB  . ASP   D  150 ? 1.6361 1.1846 1.8230 0.0808  -0.2384 0.1382  142 ASP   D CB  
6717  C  CG  . ASP   D  150 ? 1.5670 1.2274 1.8337 0.1055  -0.2421 0.1867  142 ASP   D CG  
6718  O  OD1 . ASP   D  150 ? 1.5613 1.2582 1.7288 0.1463  -0.3344 0.2235  142 ASP   D OD1 
6719  O  OD2 . ASP   D  150 ? 1.6730 1.3474 1.8747 0.0187  -0.2095 0.2591  142 ASP   D OD2 
6720  N  N   . ASP   D  151 ? 1.7144 1.0103 1.8171 0.0599  -0.2598 0.1251  143 ASP   D N   
6721  C  CA  . ASP   D  151 ? 1.7115 1.0011 1.7570 0.0588  -0.2712 0.1281  143 ASP   D CA  
6722  C  C   . ASP   D  151 ? 1.7235 0.9202 1.7330 0.0862  -0.3253 0.0873  143 ASP   D C   
6723  O  O   . ASP   D  151 ? 1.6812 0.9281 1.7458 0.0956  -0.3418 0.1449  143 ASP   D O   
6724  C  CB  . ASP   D  151 ? 1.7143 1.0204 1.7230 0.0589  -0.2342 0.0850  143 ASP   D CB  
6725  C  CG  . ASP   D  151 ? 1.7076 1.0331 1.7388 0.0212  -0.1643 0.0662  143 ASP   D CG  
6726  O  OD1 . ASP   D  151 ? 1.7193 1.0205 1.7507 -0.0036 -0.1290 0.0238  143 ASP   D OD1 
6727  O  OD2 . ASP   D  151 ? 1.7080 1.1288 1.7972 0.0395  -0.1190 -0.0200 143 ASP   D OD2 
6728  N  N   . GLY   D  152 ? 1.7367 0.7845 1.6738 0.0846  -0.4085 0.1614  144 GLY   D N   
6729  C  CA  . GLY   D  152 ? 1.7629 0.6607 1.6910 0.1174  -0.4475 0.1636  144 GLY   D CA  
6730  C  C   . GLY   D  152 ? 1.7465 0.6743 1.6130 0.1120  -0.4800 0.1601  144 GLY   D C   
6731  O  O   . GLY   D  152 ? 1.7647 0.5372 1.4732 0.0963  -0.4765 0.2141  144 GLY   D O   
6732  N  N   . TYR   D  153 ? 1.8235 0.6655 1.6639 0.1151  -0.4735 0.1730  145 TYR   D N   
6733  C  CA  . TYR   D  153 ? 1.8274 0.5928 1.6511 0.1364  -0.4873 0.1497  145 TYR   D CA  
6734  C  C   . TYR   D  153 ? 1.7887 0.5895 1.6657 0.1429  -0.4471 0.1235  145 TYR   D C   
6735  O  O   . TYR   D  153 ? 1.8050 0.5834 1.6686 0.1731  -0.4778 0.0738  145 TYR   D O   
6736  C  CB  . TYR   D  153 ? 1.8805 0.5440 1.7425 0.1894  -0.4982 0.1877  145 TYR   D CB  
6737  C  CG  . TYR   D  153 ? 1.8972 0.5134 1.7762 0.2027  -0.5370 0.1831  145 TYR   D CG  
6738  C  CD1 . TYR   D  153 ? 1.8997 0.5415 1.8002 0.2060  -0.5354 0.1625  145 TYR   D CD1 
6739  C  CD2 . TYR   D  153 ? 1.8905 0.4296 1.8408 0.2186  -0.5572 0.2029  145 TYR   D CD2 
6740  C  CE1 . TYR   D  153 ? 1.9188 0.5384 1.8484 0.1925  -0.5518 0.1346  145 TYR   D CE1 
6741  C  CE2 . TYR   D  153 ? 1.9019 0.4410 1.8725 0.1974  -0.5730 0.1874  145 TYR   D CE2 
6742  C  CZ  . TYR   D  153 ? 1.9024 0.5356 1.9297 0.2026  -0.5537 0.1829  145 TYR   D CZ  
6743  O  OH  . TYR   D  153 ? 1.9246 0.5891 1.9159 0.2456  -0.5789 0.1832  145 TYR   D OH  
6744  N  N   . GLN   D  154 ? 1.7972 0.5667 1.6727 0.1127  -0.4263 0.1259  146 GLN   D N   
6745  C  CA  . GLN   D  154 ? 1.8011 0.5985 1.6760 0.0971  -0.4229 0.1196  146 GLN   D CA  
6746  C  C   . GLN   D  154 ? 1.8577 0.5717 1.6316 0.0763  -0.4181 0.1121  146 GLN   D C   
6747  O  O   . GLN   D  154 ? 1.8729 0.4613 1.5477 0.0679  -0.4477 0.1332  146 GLN   D O   
6748  C  CB  . GLN   D  154 ? 1.7417 0.6178 1.7002 0.1212  -0.4248 0.1227  146 GLN   D CB  
6749  C  CG  . GLN   D  154 ? 1.6934 0.6822 1.7455 0.1286  -0.4201 0.1349  146 GLN   D CG  
6750  C  CD  . GLN   D  154 ? 1.6567 0.7357 1.7549 0.1270  -0.4324 0.1752  146 GLN   D CD  
6751  O  OE1 . GLN   D  154 ? 1.5742 0.7284 1.7941 0.0985  -0.4683 0.1793  146 GLN   D OE1 
6752  N  NE2 . GLN   D  154 ? 1.6754 0.8011 1.7248 0.1251  -0.4088 0.1896  146 GLN   D NE2 
6753  N  N   . LEU   D  155 ? 1.8872 0.5575 1.6764 0.0867  -0.4088 0.1147  147 LEU   D N   
6754  C  CA  . LEU   D  155 ? 1.8823 0.5294 1.6606 0.0971  -0.3988 0.0522  147 LEU   D CA  
6755  C  C   . LEU   D  155 ? 1.8289 0.5105 1.6610 0.1607  -0.3883 0.0204  147 LEU   D C   
6756  O  O   . LEU   D  155 ? 1.8739 0.5255 1.6579 0.1694  -0.3687 0.0066  147 LEU   D O   
6757  C  CB  . LEU   D  155 ? 1.9011 0.5453 1.6513 0.1012  -0.4053 0.0549  147 LEU   D CB  
6758  C  CG  . LEU   D  155 ? 1.9391 0.5122 1.6195 0.1044  -0.3969 0.0688  147 LEU   D CG  
6759  C  CD1 . LEU   D  155 ? 1.9452 0.5089 1.5666 0.0571  -0.3996 0.0588  147 LEU   D CD1 
6760  C  CD2 . LEU   D  155 ? 1.9675 0.4986 1.6420 0.0897  -0.4137 0.0915  147 LEU   D CD2 
6761  N  N   . PHE   D  156 ? 1.8296 0.5240 1.6903 0.1785  -0.4140 0.0132  148 PHE   D N   
6762  C  CA  . PHE   D  156 ? 1.8321 0.5933 1.6870 0.1545  -0.4006 0.0168  148 PHE   D CA  
6763  C  C   . PHE   D  156 ? 1.8784 0.5328 1.7092 0.1682  -0.3961 0.0335  148 PHE   D C   
6764  O  O   . PHE   D  156 ? 1.9196 0.3623 1.7390 0.2370  -0.3634 0.0469  148 PHE   D O   
6765  C  CB  . PHE   D  156 ? 1.7787 0.5875 1.6750 0.1062  -0.3870 0.0429  148 PHE   D CB  
6766  C  CG  . PHE   D  156 ? 1.7558 0.6270 1.7020 0.0768  -0.3720 0.0025  148 PHE   D CG  
6767  C  CD1 . PHE   D  156 ? 1.7374 0.6242 1.7168 0.0630  -0.3585 -0.0186 148 PHE   D CD1 
6768  C  CD2 . PHE   D  156 ? 1.7590 0.6061 1.7231 0.0751  -0.3869 0.0240  148 PHE   D CD2 
6769  C  CE1 . PHE   D  156 ? 1.7496 0.5963 1.7027 0.1002  -0.3479 0.0227  148 PHE   D CE1 
6770  C  CE2 . PHE   D  156 ? 1.7595 0.6050 1.7055 0.1173  -0.3708 0.0706  148 PHE   D CE2 
6771  C  CZ  . PHE   D  156 ? 1.7415 0.5528 1.7092 0.1160  -0.3657 0.0596  148 PHE   D CZ  
6772  N  N   . HIS   D  157 ? 1.8759 0.6199 1.6187 0.1351  -0.4167 0.0326  149 HIS   D N   
6773  C  CA  . HIS   D  157 ? 1.8825 0.7212 1.5120 0.0880  -0.4184 0.0023  149 HIS   D CA  
6774  C  C   . HIS   D  157 ? 1.8972 0.6922 1.4875 0.1053  -0.3934 0.0026  149 HIS   D C   
6775  O  O   . HIS   D  157 ? 1.9102 0.6809 1.5207 0.0968  -0.3452 -0.0186 149 HIS   D O   
6776  C  CB  . HIS   D  157 ? 1.8632 0.7524 1.4341 0.1015  -0.4203 -0.0243 149 HIS   D CB  
6777  C  CG  . HIS   D  157 ? 1.9213 0.7977 1.3972 0.0459  -0.4054 -0.0068 149 HIS   D CG  
6778  N  ND1 . HIS   D  157 ? 1.9829 0.8295 1.3819 0.0179  -0.3769 -0.0164 149 HIS   D ND1 
6779  C  CD2 . HIS   D  157 ? 1.9550 0.7916 1.3574 0.0291  -0.3904 0.0027  149 HIS   D CD2 
6780  C  CE1 . HIS   D  157 ? 1.9697 0.9094 1.3648 0.0045  -0.3727 0.0031  149 HIS   D CE1 
6781  N  NE2 . HIS   D  157 ? 1.9585 0.8386 1.3647 -0.0117 -0.3833 -0.0034 149 HIS   D NE2 
6782  N  N   . ALA   D  158 ? 1.9286 0.6732 1.4866 0.1296  -0.3666 0.0157  150 ALA   D N   
6783  C  CA  . ALA   D  158 ? 1.9369 0.7755 1.4458 0.1094  -0.3638 0.0398  150 ALA   D CA  
6784  C  C   . ALA   D  158 ? 1.9481 0.7670 1.4080 0.0924  -0.3246 0.0776  150 ALA   D C   
6785  O  O   . ALA   D  158 ? 1.9997 0.6719 1.3504 0.0779  -0.3415 0.0510  150 ALA   D O   
6786  C  CB  . ALA   D  158 ? 1.9393 0.8226 1.4496 0.1291  -0.3567 0.0230  150 ALA   D CB  
6787  N  N   . GLU   D  159 ? 1.8871 0.8704 1.3988 0.0402  -0.3112 0.0792  151 GLU   D N   
6788  C  CA  . GLU   D  159 ? 1.7955 0.9052 1.4277 0.0295  -0.3049 0.1456  151 GLU   D CA  
6789  C  C   . GLU   D  159 ? 1.7705 0.9339 1.4242 0.0364  -0.2865 0.1633  151 GLU   D C   
6790  O  O   . GLU   D  159 ? 1.5558 1.0053 1.3563 -0.0107 -0.3541 0.2238  151 GLU   D O   
6791  C  CB  . GLU   D  159 ? 1.8342 0.9384 1.4427 0.0255  -0.2474 0.1481  151 GLU   D CB  
6792  C  CG  . GLU   D  159 ? 1.8186 0.9572 1.4820 0.0443  -0.2345 0.1468  151 GLU   D CG  
6793  C  CD  . GLU   D  159 ? 1.8373 1.0854 1.4804 0.0114  -0.1786 0.0879  151 GLU   D CD  
6794  O  OE1 . GLU   D  159 ? 1.9205 1.0211 1.5784 -0.0570 -0.1687 -0.0178 151 GLU   D OE1 
6795  O  OE2 . GLU   D  159 ? 1.8282 1.1080 1.4615 0.0225  -0.1977 0.1024  151 GLU   D OE2 
6796  N  N   . PRO   D  160 ? 1.7836 0.8757 1.4191 0.0516  -0.2621 0.1399  152 PRO   D N   
6797  C  CA  . PRO   D  160 ? 1.8244 0.8234 1.3838 0.0507  -0.2744 0.1140  152 PRO   D CA  
6798  C  C   . PRO   D  160 ? 1.8552 0.7875 1.3867 0.0909  -0.2719 0.0983  152 PRO   D C   
6799  O  O   . PRO   D  160 ? 1.9629 0.6711 1.3669 0.0321  -0.3475 0.1530  152 PRO   D O   
6800  C  CB  . PRO   D  160 ? 1.8301 0.8186 1.3738 0.0337  -0.2670 0.0728  152 PRO   D CB  
6801  C  CG  . PRO   D  160 ? 1.7974 0.7926 1.4103 0.0591  -0.2831 0.0879  152 PRO   D CG  
6802  C  CD  . PRO   D  160 ? 1.7908 0.8166 1.4334 0.0801  -0.2876 0.1189  152 PRO   D CD  
6803  N  N   . SER   D  161 ? 1.8695 0.8491 1.4748 0.1214  -0.2678 0.0207  153 SER   D N   
6804  C  CA  . SER   D  161 ? 1.8111 0.9428 1.4908 0.1312  -0.2337 -0.0714 153 SER   D CA  
6805  C  C   . SER   D  161 ? 1.7565 0.9837 1.5381 0.0758  -0.1770 -0.0616 153 SER   D C   
6806  O  O   . SER   D  161 ? 1.7706 1.0955 1.4943 0.0310  -0.1023 -0.1440 153 SER   D O   
6807  C  CB  . SER   D  161 ? 1.8091 1.0202 1.4943 0.1372  -0.2190 -0.1439 153 SER   D CB  
6808  O  OG  . SER   D  161 ? 1.8190 1.0337 1.5372 0.1086  -0.1960 -0.2291 153 SER   D OG  
6809  N  N   . GLY   D  162 ? 1.6746 0.9634 1.6006 0.0512  -0.1870 -0.0634 154 GLY   D N   
6810  C  CA  . GLY   D  162 ? 1.6443 0.9534 1.6246 0.0811  -0.1755 -0.0414 154 GLY   D CA  
6811  C  C   . GLY   D  162 ? 1.6427 0.8846 1.6268 0.0699  -0.1745 -0.0052 154 GLY   D C   
6812  O  O   . GLY   D  162 ? 1.5137 0.9089 1.6256 0.0587  -0.1901 -0.0107 154 GLY   D O   
6813  N  N   . THR   D  163 ? 1.7239 0.9105 1.6281 0.0968  -0.1925 0.0243  155 THR   D N   
6814  C  CA  . THR   D  163 ? 1.7307 0.8407 1.5817 0.0833  -0.1957 0.0429  155 THR   D CA  
6815  C  C   . THR   D  163 ? 1.7980 0.6804 1.5946 0.0772  -0.2316 0.0560  155 THR   D C   
6816  O  O   . THR   D  163 ? 1.8775 0.6586 1.5582 0.0922  -0.2347 0.0683  155 THR   D O   
6817  C  CB  . THR   D  163 ? 1.7364 0.8865 1.5471 0.0877  -0.1804 0.0072  155 THR   D CB  
6818  O  OG1 . THR   D  163 ? 1.7918 0.7954 1.5380 0.0764  -0.1597 -0.0603 155 THR   D OG1 
6819  C  CG2 . THR   D  163 ? 1.7383 0.9431 1.5627 0.0962  -0.1611 0.0140  155 THR   D CG2 
6820  N  N   . PHE   D  164 ? 1.8236 0.6098 1.6067 0.0744  -0.2317 0.0764  156 PHE   D N   
6821  C  CA  . PHE   D  164 ? 1.8467 0.6589 1.6014 0.0883  -0.2375 0.1173  156 PHE   D CA  
6822  C  C   . PHE   D  164 ? 1.8662 0.6246 1.6001 0.1515  -0.2185 0.1428  156 PHE   D C   
6823  O  O   . PHE   D  164 ? 1.8481 0.7076 1.6208 0.2008  -0.1361 0.1277  156 PHE   D O   
6824  C  CB  . PHE   D  164 ? 1.8430 0.6649 1.5612 0.0737  -0.2485 0.1163  156 PHE   D CB  
6825  C  CG  . PHE   D  164 ? 1.8244 0.6612 1.5598 0.0819  -0.2713 0.1303  156 PHE   D CG  
6826  C  CD1 . PHE   D  164 ? 1.8314 0.6357 1.5504 0.0648  -0.2561 0.1555  156 PHE   D CD1 
6827  C  CD2 . PHE   D  164 ? 1.8265 0.6095 1.5520 0.0680  -0.2509 0.1852  156 PHE   D CD2 
6828  C  CE1 . PHE   D  164 ? 1.8138 0.6861 1.5838 0.0123  -0.2256 0.1633  156 PHE   D CE1 
6829  C  CE2 . PHE   D  164 ? 1.7802 0.6541 1.5707 0.0285  -0.2248 0.1898  156 PHE   D CE2 
6830  C  CZ  . PHE   D  164 ? 1.7705 0.7602 1.5628 0.0230  -0.2287 0.1748  156 PHE   D CZ  
6831  N  N   . TYR   D  165 ? 1.9166 0.6118 1.5941 0.1383  -0.2171 0.1635  157 TYR   D N   
6832  C  CA  . TYR   D  165 ? 1.9175 0.6869 1.5954 0.0994  -0.2171 0.1626  157 TYR   D CA  
6833  C  C   . TYR   D  165 ? 1.8914 0.5564 1.6521 0.1069  -0.2401 0.1576  157 TYR   D C   
6834  O  O   . TYR   D  165 ? 1.8644 0.4308 1.6129 0.1144  -0.2735 0.1265  157 TYR   D O   
6835  C  CB  . TYR   D  165 ? 2.0051 0.6866 1.5677 0.0929  -0.2026 0.1790  157 TYR   D CB  
6836  C  CG  . TYR   D  165 ? 2.0357 0.8088 1.5295 0.0257  -0.2035 0.1841  157 TYR   D CG  
6837  C  CD1 . TYR   D  165 ? 2.0533 0.8698 1.5210 0.0309  -0.1951 0.1885  157 TYR   D CD1 
6838  C  CD2 . TYR   D  165 ? 2.0534 0.8562 1.4810 -0.0173 -0.1823 0.1728  157 TYR   D CD2 
6839  C  CE1 . TYR   D  165 ? 2.0469 0.9337 1.5412 -0.0006 -0.2048 0.1505  157 TYR   D CE1 
6840  C  CE2 . TYR   D  165 ? 2.0683 0.9374 1.4715 -0.0452 -0.2183 0.1605  157 TYR   D CE2 
6841  C  CZ  . TYR   D  165 ? 2.0519 0.9963 1.5334 -0.0263 -0.2178 0.1675  157 TYR   D CZ  
6842  O  OH  . TYR   D  165 ? 2.0245 1.1248 1.5336 -0.0491 -0.3061 0.1317  157 TYR   D OH  
6843  N  N   . ARG   D  166 ? 1.8486 0.6071 1.7331 0.1396  -0.2441 0.1668  158 ARG   D N   
6844  C  CA  . ARG   D  166 ? 1.8622 0.6317 1.7830 0.1822  -0.2726 0.1329  158 ARG   D CA  
6845  C  C   . ARG   D  166 ? 1.9038 0.5601 1.8219 0.1927  -0.2193 0.0861  158 ARG   D C   
6846  O  O   . ARG   D  166 ? 1.9342 0.3114 1.9694 0.1870  -0.2071 0.1194  158 ARG   D O   
6847  C  CB  . ARG   D  166 ? 1.8594 0.6195 1.8453 0.1784  -0.2785 0.1021  158 ARG   D CB  
6848  C  CG  . ARG   D  166 ? 1.8618 0.5764 1.9312 0.1832  -0.3018 0.0522  158 ARG   D CG  
6849  C  CD  . ARG   D  166 ? 1.8399 0.5899 1.9904 0.2018  -0.2806 0.0747  158 ARG   D CD  
6850  N  NE  . ARG   D  166 ? 1.8460 0.5986 2.0336 0.2176  -0.3092 0.0601  158 ARG   D NE  
6851  C  CZ  . ARG   D  166 ? 1.8328 0.6824 2.0459 0.1774  -0.2970 0.0935  158 ARG   D CZ  
6852  N  NH1 . ARG   D  166 ? 1.8220 0.7632 2.0555 0.1611  -0.2521 0.1107  158 ARG   D NH1 
6853  N  NH2 . ARG   D  166 ? 1.8442 0.7728 2.0780 0.1816  -0.3299 0.1105  158 ARG   D NH2 
6854  N  N   . TYR   D  167 ? 1.8560 0.5978 1.8282 0.2296  -0.2887 0.1080  159 TYR   D N   
6855  C  CA  . TYR   D  167 ? 1.7440 0.6177 1.8177 0.2337  -0.3389 0.0741  159 TYR   D CA  
6856  C  C   . TYR   D  167 ? 1.7305 0.6825 1.8597 0.2127  -0.3430 0.0353  159 TYR   D C   
6857  O  O   . TYR   D  167 ? 1.6177 0.7461 1.9015 0.1852  -0.3729 -0.0402 159 TYR   D O   
6858  C  CB  . TYR   D  167 ? 1.7384 0.5732 1.8119 0.2699  -0.3539 0.1298  159 TYR   D CB  
6859  C  CG  . TYR   D  167 ? 1.7232 0.5502 1.8085 0.2884  -0.3505 0.1416  159 TYR   D CG  
6860  C  CD1 . TYR   D  167 ? 1.7341 0.5923 1.7891 0.2865  -0.3476 0.1611  159 TYR   D CD1 
6861  C  CD2 . TYR   D  167 ? 1.7332 0.5513 1.8567 0.2894  -0.3463 0.1316  159 TYR   D CD2 
6862  C  CE1 . TYR   D  167 ? 1.7643 0.5061 1.7816 0.3092  -0.3258 0.1692  159 TYR   D CE1 
6863  C  CE2 . TYR   D  167 ? 1.7485 0.5472 1.8674 0.2795  -0.3399 0.1233  159 TYR   D CE2 
6864  C  CZ  . TYR   D  167 ? 1.7712 0.4654 1.8087 0.2668  -0.3388 0.1458  159 TYR   D CZ  
6865  O  OH  . TYR   D  167 ? 1.8223 0.4679 1.8318 0.2172  -0.3043 0.1298  159 TYR   D OH  
6866  N  N   . ASN   D  168 ? 1.7093 0.6667 1.7806 0.1874  -0.3589 0.0119  160 ASN   D N   
6867  C  CA  . ASN   D  168 ? 1.7360 0.6954 1.7509 0.1817  -0.3556 0.0169  160 ASN   D CA  
6868  C  C   . ASN   D  168 ? 1.7581 0.6834 1.7602 0.1606  -0.3561 0.0123  160 ASN   D C   
6869  O  O   . ASN   D  168 ? 1.7836 0.7365 1.8214 0.0965  -0.3553 -0.0598 160 ASN   D O   
6870  C  CB  . ASN   D  168 ? 1.7391 0.7290 1.7153 0.1967  -0.3722 0.0001  160 ASN   D CB  
6871  C  CG  . ASN   D  168 ? 1.7360 0.8034 1.6820 0.2018  -0.3514 -0.0190 160 ASN   D CG  
6872  O  OD1 . ASN   D  168 ? 1.7865 0.8856 1.6606 0.1765  -0.3455 -0.0633 160 ASN   D OD1 
6873  N  ND2 . ASN   D  168 ? 1.7087 0.8077 1.6714 0.2012  -0.3497 -0.0385 160 ASN   D ND2 
6874  N  N   . ALA   D  169 ? 1.7623 0.6517 1.7557 0.1793  -0.3543 0.0259  161 ALA   D N   
6875  C  CA  . ALA   D  169 ? 1.7728 0.6308 1.7560 0.2079  -0.3745 0.0818  161 ALA   D CA  
6876  C  C   . ALA   D  169 ? 1.7520 0.6208 1.7319 0.2073  -0.3641 0.1055  161 ALA   D C   
6877  O  O   . ALA   D  169 ? 1.7518 0.6793 1.7197 0.2092  -0.3554 0.1213  161 ALA   D O   
6878  C  CB  . ALA   D  169 ? 1.8048 0.6525 1.7750 0.2046  -0.3900 0.1057  161 ALA   D CB  
6879  N  N   . LYS   D  170 ? 1.7469 0.5737 1.7130 0.2013  -0.3798 0.1241  162 LYS   D N   
6880  C  CA  . LYS   D  170 ? 1.7666 0.6063 1.7001 0.1808  -0.3832 0.1203  162 LYS   D CA  
6881  C  C   . LYS   D  170 ? 1.7576 0.5803 1.6787 0.1612  -0.4201 0.1379  162 LYS   D C   
6882  O  O   . LYS   D  170 ? 1.7139 0.5707 1.6805 0.1926  -0.4486 0.1435  162 LYS   D O   
6883  C  CB  . LYS   D  170 ? 1.7662 0.6229 1.6639 0.1839  -0.3632 0.1184  162 LYS   D CB  
6884  C  CG  . LYS   D  170 ? 1.7862 0.6451 1.6672 0.1655  -0.3557 0.0965  162 LYS   D CG  
6885  C  CD  . LYS   D  170 ? 1.8536 0.7053 1.7067 0.1604  -0.3250 0.0460  162 LYS   D CD  
6886  C  CE  . LYS   D  170 ? 1.8696 0.8227 1.7248 0.1447  -0.3298 0.0411  162 LYS   D CE  
6887  N  NZ  . LYS   D  170 ? 1.9506 0.8387 1.7654 0.1407  -0.2979 0.0210  162 LYS   D NZ  
6888  N  N   . ALA   D  171 ? 1.7907 0.5965 1.6750 0.1173  -0.4276 0.1766  163 ALA   D N   
6889  C  CA  . ALA   D  171 ? 1.8037 0.5697 1.6591 0.0849  -0.4531 0.1743  163 ALA   D CA  
6890  C  C   . ALA   D  171 ? 1.8412 0.4906 1.5566 0.0612  -0.4350 0.1577  163 ALA   D C   
6891  O  O   . ALA   D  171 ? 1.7615 0.4079 1.4947 -0.0159 -0.4831 0.2013  163 ALA   D O   
6892  C  CB  . ALA   D  171 ? 1.8350 0.5747 1.7224 0.1055  -0.4443 0.1818  163 ALA   D CB  
6893  N  N   . ILE   D  172 ? 1.8498 0.4596 1.5804 0.0716  -0.4482 0.1166  164 ILE   D N   
6894  C  CA  . ILE   D  172 ? 1.8899 0.4740 1.5807 0.0484  -0.4568 0.0763  164 ILE   D CA  
6895  C  C   . ILE   D  172 ? 1.9522 0.4364 1.6463 0.0218  -0.4177 0.0673  164 ILE   D C   
6896  O  O   . ILE   D  172 ? 1.8858 0.2940 1.6648 -0.0629 -0.4785 0.0213  164 ILE   D O   
6897  C  CB  . ILE   D  172 ? 1.8967 0.5098 1.5382 0.0791  -0.4554 0.0791  164 ILE   D CB  
6898  C  CG1 . ILE   D  172 ? 1.8971 0.5325 1.5158 0.0597  -0.4921 0.0780  164 ILE   D CG1 
6899  C  CG2 . ILE   D  172 ? 1.8853 0.5059 1.5320 0.0963  -0.4308 0.0460  164 ILE   D CG2 
6900  C  CD1 . ILE   D  172 ? 1.8805 0.5633 1.5174 0.0557  -0.4959 0.1112  164 ILE   D CD1 
6901  N  N   . GLY   D  173 ? 2.0065 0.4743 1.7317 0.0045  -0.3930 -0.0148 165 GLY   D N   
6902  C  CA  . GLY   D  173 ? 2.0323 0.5274 1.7370 0.0330  -0.3428 -0.0044 165 GLY   D CA  
6903  C  C   . GLY   D  173 ? 2.0794 0.5287 1.7097 0.0556  -0.3191 0.0417  165 GLY   D C   
6904  O  O   . GLY   D  173 ? 2.1265 0.2567 1.8329 0.1730  -0.3160 0.0744  165 GLY   D O   
6905  N  N   . SER   D  174 ? 2.0925 0.6113 1.6283 0.0738  -0.3485 0.0807  166 SER   D N   
6906  C  CA  . SER   D  174 ? 2.1029 0.6269 1.6396 0.1242  -0.3820 0.1136  166 SER   D CA  
6907  C  C   . SER   D  174 ? 2.0208 0.8346 1.6215 0.0150  -0.4701 0.1472  166 SER   D C   
6908  O  O   . SER   D  174 ? 2.1656 0.9013 1.7122 0.1554  -0.3472 0.1825  166 SER   D O   
6909  C  CB  . SER   D  174 ? 2.1144 0.7427 1.5258 0.1817  -0.3880 0.0868  166 SER   D CB  
6910  O  OG  . SER   D  174 ? 2.1433 0.6008 1.5442 0.2471  -0.3915 0.0915  166 SER   D OG  
6911  N  N   . GLY   D  175 ? 1.9352 0.7313 1.6343 -0.0149 -0.4650 0.2057  167 GLY   D N   
6912  C  CA  . GLY   D  175 ? 1.9343 0.7362 1.6733 -0.0686 -0.5722 0.1823  167 GLY   D CA  
6913  C  C   . GLY   D  175 ? 1.8910 0.7197 1.7331 -0.0677 -0.5851 0.1774  167 GLY   D C   
6914  O  O   . GLY   D  175 ? 1.9137 0.7473 1.8086 0.0099  -0.5869 0.2669  167 GLY   D O   
6915  N  N   . SER   D  176 ? 1.8660 0.7219 1.7313 -0.0474 -0.6742 0.1084  168 SER   D N   
6916  C  CA  . SER   D  176 ? 1.8016 0.7095 1.7999 0.0000  -0.6336 0.0993  168 SER   D CA  
6917  C  C   . SER   D  176 ? 1.8491 0.7817 1.8834 0.0517  -0.6243 0.0299  168 SER   D C   
6918  O  O   . SER   D  176 ? 1.8264 0.7270 1.9466 0.0385  -0.5396 0.1063  168 SER   D O   
6919  C  CB  . SER   D  176 ? 1.8014 0.6931 1.8086 -0.0301 -0.6507 0.1090  168 SER   D CB  
6920  O  OG  . SER   D  176 ? 1.7988 0.5480 1.8819 -0.0411 -0.6780 0.1513  168 SER   D OG  
6921  N  N   . GLU   D  177 ? 1.7724 0.9004 1.8931 0.1763  -0.5861 -0.1033 169 GLU   D N   
6922  C  CA  . GLU   D  177 ? 1.8375 0.9724 1.9209 0.2266  -0.5744 -0.1443 169 GLU   D CA  
6923  C  C   . GLU   D  177 ? 1.8298 0.8804 1.9879 0.3154  -0.5428 -0.1784 169 GLU   D C   
6924  O  O   . GLU   D  177 ? 1.8258 0.8265 2.0621 0.3866  -0.5248 -0.2015 169 GLU   D O   
6925  C  CB  . GLU   D  177 ? 1.8403 1.0993 1.8794 0.2180  -0.5605 -0.1976 169 GLU   D CB  
6926  C  CG  . GLU   D  177 ? 1.8733 1.1651 1.8801 0.1940  -0.5612 -0.1497 169 GLU   D CG  
6927  C  CD  . GLU   D  177 ? 1.8800 1.3069 1.8335 0.2030  -0.5617 -0.2058 169 GLU   D CD  
6928  O  OE1 . GLU   D  177 ? 1.8867 1.5574 1.8269 0.2207  -0.5574 -0.1460 169 GLU   D OE1 
6929  O  OE2 . GLU   D  177 ? 1.8929 1.2794 1.8342 0.1942  -0.5646 -0.2212 169 GLU   D OE2 
6930  N  N   . GLY   D  178 ? 1.8497 0.7858 1.9893 0.3599  -0.5298 -0.1902 170 GLY   D N   
6931  C  CA  . GLY   D  178 ? 1.8316 0.7259 2.0297 0.3994  -0.5196 -0.1857 170 GLY   D CA  
6932  C  C   . GLY   D  178 ? 1.7577 0.7718 1.9894 0.3937  -0.5533 -0.1521 170 GLY   D C   
6933  O  O   . GLY   D  178 ? 1.7823 0.5890 1.9719 0.5212  -0.5440 -0.2183 170 GLY   D O   
6934  N  N   . ALA   D  179 ? 1.7939 0.7323 1.9534 0.3830  -0.5293 -0.1029 171 ALA   D N   
6935  C  CA  . ALA   D  179 ? 1.8186 0.7243 1.9210 0.3184  -0.5542 -0.0279 171 ALA   D CA  
6936  C  C   . ALA   D  179 ? 1.8604 0.7407 1.8981 0.3494  -0.5470 0.0157  171 ALA   D C   
6937  O  O   . ALA   D  179 ? 1.8383 0.7987 2.0243 0.3297  -0.5382 0.0130  171 ALA   D O   
6938  C  CB  . ALA   D  179 ? 1.8047 0.7027 1.8745 0.2901  -0.5533 -0.0359 171 ALA   D CB  
6939  N  N   . GLN   D  180 ? 1.9036 0.7172 1.8845 0.3565  -0.5318 0.1086  172 GLN   D N   
6940  C  CA  . GLN   D  180 ? 2.0019 0.7760 1.8575 0.3481  -0.5185 0.1349  172 GLN   D CA  
6941  C  C   . GLN   D  180 ? 1.9624 0.8486 1.8243 0.3329  -0.5480 0.1301  172 GLN   D C   
6942  O  O   . GLN   D  180 ? 1.9462 0.7902 1.7616 0.3498  -0.5618 0.0904  172 GLN   D O   
6943  C  CB  . GLN   D  180 ? 2.0780 0.8052 1.8031 0.3168  -0.4766 0.1850  172 GLN   D CB  
6944  C  CG  . GLN   D  180 ? 2.1628 0.7642 1.8073 0.3278  -0.4805 0.2166  172 GLN   D CG  
6945  C  CD  . GLN   D  180 ? 2.1963 0.7201 1.7218 0.2924  -0.4909 0.3116  172 GLN   D CD  
6946  O  OE1 . GLN   D  180 ? 2.2159 0.4678 1.6712 0.3301  -0.4960 0.4229  172 GLN   D OE1 
6947  N  NE2 . GLN   D  180 ? 2.1982 0.7235 1.7121 0.2731  -0.5103 0.3075  172 GLN   D NE2 
6948  N  N   . ALA   D  181 ? 2.0560 0.8556 1.8720 0.2629  -0.5671 0.1284  173 ALA   D N   
6949  C  CA  . ALA   D  181 ? 2.0313 0.9129 1.8970 0.2630  -0.5985 0.1293  173 ALA   D CA  
6950  C  C   . ALA   D  181 ? 2.0414 0.8894 1.9085 0.2073  -0.6136 0.1720  173 ALA   D C   
6951  O  O   . ALA   D  181 ? 2.0227 0.8450 1.8570 0.1077  -0.6418 0.1989  173 ALA   D O   
6952  C  CB  . ALA   D  181 ? 2.0817 0.9409 1.9449 0.2283  -0.5990 0.1198  173 ALA   D CB  
6953  N  N   . GLU   D  182 ? 2.0203 0.9139 1.8991 0.2301  -0.6199 0.2018  174 GLU   D N   
6954  C  CA  . GLU   D  182 ? 1.9987 0.9320 1.9183 0.2094  -0.6212 0.1972  174 GLU   D CA  
6955  C  C   . GLU   D  182 ? 1.9212 0.8743 1.8698 0.2741  -0.5978 0.1858  174 GLU   D C   
6956  O  O   . GLU   D  182 ? 1.9297 0.8196 1.8606 0.2689  -0.6076 0.1800  174 GLU   D O   
6957  C  CB  . GLU   D  182 ? 2.0374 1.0922 1.9321 0.2100  -0.6000 0.1905  174 GLU   D CB  
6958  C  CG  . GLU   D  182 ? 2.1080 1.2449 1.9454 0.1902  -0.6369 0.2059  174 GLU   D CG  
6959  C  CD  . GLU   D  182 ? 2.1961 1.3038 2.0191 0.2463  -0.6425 0.2777  174 GLU   D CD  
6960  O  OE1 . GLU   D  182 ? 2.1579 1.7082 2.1050 0.1785  -0.6577 0.2283  174 GLU   D OE1 
6961  O  OE2 . GLU   D  182 ? 2.2061 1.4881 1.9874 0.1720  -0.7336 0.2889  174 GLU   D OE2 
6962  N  N   . LEU   D  183 ? 1.8693 0.7224 1.8655 0.2144  -0.5295 0.1521  175 LEU   D N   
6963  C  CA  . LEU   D  183 ? 1.8219 0.7172 1.8500 0.2291  -0.5061 0.1586  175 LEU   D CA  
6964  C  C   . LEU   D  183 ? 1.8613 0.7943 1.8687 0.1600  -0.4773 0.1479  175 LEU   D C   
6965  O  O   . LEU   D  183 ? 1.8646 0.8585 1.8537 0.1204  -0.5107 0.1679  175 LEU   D O   
6966  C  CB  . LEU   D  183 ? 1.8385 0.5574 1.8426 0.2171  -0.4705 0.1350  175 LEU   D CB  
6967  C  CG  . LEU   D  183 ? 1.8214 0.3937 1.8301 0.2479  -0.5022 0.1271  175 LEU   D CG  
6968  C  CD1 . LEU   D  183 ? 1.7945 0.3652 1.8236 0.2543  -0.4730 0.0860  175 LEU   D CD1 
6969  C  CD2 . LEU   D  183 ? 1.7973 0.3482 1.8128 0.2669  -0.5070 0.1503  175 LEU   D CD2 
6970  N  N   . LEU   D  184 ? 1.8762 0.8651 1.8508 0.1481  -0.4308 0.1249  176 LEU   D N   
6971  C  CA  . LEU   D  184 ? 1.8251 0.9277 1.8694 0.1440  -0.4446 0.1268  176 LEU   D CA  
6972  C  C   . LEU   D  184 ? 1.7734 0.9002 1.8534 0.1150  -0.4134 0.1169  176 LEU   D C   
6973  O  O   . LEU   D  184 ? 1.7261 0.8426 1.7929 0.1230  -0.4652 0.0759  176 LEU   D O   
6974  C  CB  . LEU   D  184 ? 1.8463 0.9881 1.8546 0.1383  -0.4597 0.1080  176 LEU   D CB  
6975  C  CG  . LEU   D  184 ? 1.8396 1.0372 1.8423 0.1258  -0.4618 0.0908  176 LEU   D CG  
6976  C  CD1 . LEU   D  184 ? 1.7990 1.0314 1.8390 0.1605  -0.4745 0.0954  176 LEU   D CD1 
6977  C  CD2 . LEU   D  184 ? 1.8290 1.0605 1.7950 0.1127  -0.4572 0.0938  176 LEU   D CD2 
6978  N  N   . ASN   D  185 ? 1.7549 0.9925 1.8431 0.1388  -0.4299 0.1481  177 ASN   D N   
6979  C  CA  . ASN   D  185 ? 1.7090 1.0852 1.9541 0.1561  -0.4161 0.1676  177 ASN   D CA  
6980  C  C   . ASN   D  185 ? 1.6755 1.1143 1.9803 0.1282  -0.4726 0.1879  177 ASN   D C   
6981  O  O   . ASN   D  185 ? 1.6410 1.3602 2.0547 0.2017  -0.5208 0.2366  177 ASN   D O   
6982  C  CB  . ASN   D  185 ? 1.7325 1.0624 1.9676 0.2121  -0.3783 0.1618  177 ASN   D CB  
6983  C  CG  . ASN   D  185 ? 1.7597 1.0747 1.9777 0.2545  -0.2894 0.1417  177 ASN   D CG  
6984  O  OD1 . ASN   D  185 ? 1.7814 1.0718 2.0168 0.3109  -0.2537 0.1377  177 ASN   D OD1 
6985  N  ND2 . ASN   D  185 ? 1.7989 1.0978 2.0055 0.2239  -0.2678 0.1219  177 ASN   D ND2 
6986  N  N   . GLU   D  186 ? 1.7024 1.0523 1.9798 0.1363  -0.4562 0.2334  178 GLU   D N   
6987  C  CA  . GLU   D  186 ? 1.7546 1.0388 1.9580 0.1351  -0.4784 0.2592  178 GLU   D CA  
6988  C  C   . GLU   D  186 ? 1.8244 1.0253 1.9553 0.1340  -0.4897 0.2456  178 GLU   D C   
6989  O  O   . GLU   D  186 ? 1.8600 0.9428 1.9204 0.0957  -0.5055 0.3317  178 GLU   D O   
6990  C  CB  . GLU   D  186 ? 1.7678 1.0756 1.9558 0.0993  -0.4691 0.2466  178 GLU   D CB  
6991  C  CG  . GLU   D  186 ? 1.7740 1.1104 2.0219 0.0435  -0.4446 0.2412  178 GLU   D CG  
6992  C  CD  . GLU   D  186 ? 1.7555 1.1534 2.0522 0.0230  -0.4508 0.2726  178 GLU   D CD  
6993  O  OE1 . GLU   D  186 ? 1.7776 1.0899 2.1246 0.0548  -0.4669 0.3371  178 GLU   D OE1 
6994  O  OE2 . GLU   D  186 ? 1.7778 1.2598 2.1277 -0.0445 -0.4223 0.2096  178 GLU   D OE2 
6995  N  N   . TRP   D  187 ? 1.8865 0.9750 1.9407 0.1744  -0.4826 0.2141  179 TRP   D N   
6996  C  CA  . TRP   D  187 ? 1.8643 0.9146 1.9297 0.2426  -0.4844 0.1314  179 TRP   D CA  
6997  C  C   . TRP   D  187 ? 1.8306 0.8858 1.9871 0.2526  -0.5053 0.0965  179 TRP   D C   
6998  O  O   . TRP   D  187 ? 1.8114 1.1063 2.0597 0.2938  -0.4224 0.0411  179 TRP   D O   
6999  C  CB  . TRP   D  187 ? 1.9109 0.8552 1.8920 0.2739  -0.4712 0.1221  179 TRP   D CB  
7000  C  CG  . TRP   D  187 ? 1.9449 0.8517 1.8200 0.2922  -0.4643 0.1074  179 TRP   D CG  
7001  C  CD1 . TRP   D  187 ? 1.9621 0.8159 1.7512 0.2757  -0.4821 0.1175  179 TRP   D CD1 
7002  C  CD2 . TRP   D  187 ? 1.9619 0.8284 1.8038 0.3442  -0.4454 0.1185  179 TRP   D CD2 
7003  N  NE1 . TRP   D  187 ? 1.9790 0.7626 1.7028 0.3418  -0.4836 0.1007  179 TRP   D NE1 
7004  C  CE2 . TRP   D  187 ? 1.9758 0.8068 1.7512 0.3212  -0.4515 0.1393  179 TRP   D CE2 
7005  C  CE3 . TRP   D  187 ? 1.9547 0.8793 1.8320 0.3601  -0.4148 0.1496  179 TRP   D CE3 
7006  C  CZ2 . TRP   D  187 ? 1.9806 0.7524 1.7801 0.3244  -0.4190 0.1026  179 TRP   D CZ2 
7007  C  CZ3 . TRP   D  187 ? 1.9492 0.8236 1.8177 0.4060  -0.3924 0.1400  179 TRP   D CZ3 
7008  C  CH2 . TRP   D  187 ? 1.9671 0.7965 1.7981 0.3350  -0.3943 0.1384  179 TRP   D CH2 
7009  N  N   . HIS   D  188 ? 1.7652 0.8580 2.0078 0.2623  -0.4916 0.1157  180 HIS   D N   
7010  C  CA  . HIS   D  188 ? 1.7470 0.9470 2.0761 0.2468  -0.4726 0.0991  180 HIS   D CA  
7011  C  C   . HIS   D  188 ? 1.7368 0.9358 2.1275 0.1555  -0.4082 0.1074  180 HIS   D C   
7012  O  O   . HIS   D  188 ? 1.7890 0.9055 2.1805 0.1480  -0.3958 0.0313  180 HIS   D O   
7013  C  CB  . HIS   D  188 ? 1.7254 0.9561 2.1255 0.2453  -0.4803 0.0775  180 HIS   D CB  
7014  C  CG  . HIS   D  188 ? 1.6993 0.9758 2.1271 0.2465  -0.5145 0.0797  180 HIS   D CG  
7015  N  ND1 . HIS   D  188 ? 1.7044 1.0103 2.0985 0.2398  -0.5111 0.0560  180 HIS   D ND1 
7016  C  CD2 . HIS   D  188 ? 1.6717 0.9567 2.0637 0.2798  -0.5661 0.0843  180 HIS   D CD2 
7017  C  CE1 . HIS   D  188 ? 1.6856 0.9495 2.0797 0.2565  -0.5697 0.0798  180 HIS   D CE1 
7018  N  NE2 . HIS   D  188 ? 1.6625 0.9200 2.0288 0.2995  -0.5826 0.1229  180 HIS   D NE2 
7019  N  N   . SER   D  189 ? 1.7390 0.9250 2.1875 0.1349  -0.3904 0.1015  181 SER   D N   
7020  C  CA  . SER   D  189 ? 1.6731 0.9352 2.1166 0.1046  -0.3856 0.1441  181 SER   D CA  
7021  C  C   . SER   D  189 ? 1.7028 0.9456 2.0872 0.0381  -0.4411 0.2064  181 SER   D C   
7022  O  O   . SER   D  189 ? 1.6814 0.9410 2.0352 0.0044  -0.4861 0.1621  181 SER   D O   
7023  C  CB  . SER   D  189 ? 1.5964 0.9958 2.1447 0.1627  -0.3458 0.1116  181 SER   D CB  
7024  O  OG  . SER   D  189 ? 1.5748 1.0265 2.1957 0.1812  -0.2692 0.0622  181 SER   D OG  
7025  N  N   . SER   D  190 ? 1.7161 0.8886 2.0968 0.0085  -0.4729 0.1969  182 SER   D N   
7026  C  CA  . SER   D  190 ? 1.7373 0.8084 2.1252 0.0082  -0.4947 0.2006  182 SER   D CA  
7027  C  C   . SER   D  190 ? 1.7523 0.6773 2.0647 0.0156  -0.5469 0.2054  182 SER   D C   
7028  O  O   . SER   D  190 ? 1.7285 0.5659 2.1247 0.0355  -0.6177 0.2153  182 SER   D O   
7029  C  CB  . SER   D  190 ? 1.7220 0.8583 2.1620 -0.0045 -0.4660 0.1923  182 SER   D CB  
7030  O  OG  . SER   D  190 ? 1.7402 0.9180 2.2085 -0.0072 -0.4194 0.1905  182 SER   D OG  
7031  N  N   . LEU   D  191 ? 1.7648 0.6536 2.0437 -0.0012 -0.5234 0.2301  183 LEU   D N   
7032  C  CA  . LEU   D  191 ? 1.8674 0.6046 1.9794 0.0036  -0.5194 0.2280  183 LEU   D CA  
7033  C  C   . LEU   D  191 ? 1.8899 0.5728 1.9400 -0.0758 -0.5097 0.2261  183 LEU   D C   
7034  O  O   . LEU   D  191 ? 1.9255 0.4485 2.0292 -0.1118 -0.4899 0.1758  183 LEU   D O   
7035  C  CB  . LEU   D  191 ? 1.8658 0.6760 1.9390 0.0128  -0.5390 0.2401  183 LEU   D CB  
7036  C  CG  . LEU   D  191 ? 1.9145 0.6944 1.9365 0.0123  -0.5382 0.2046  183 LEU   D CG  
7037  C  CD1 . LEU   D  191 ? 1.9069 0.7147 1.9056 0.0304  -0.5335 0.2213  183 LEU   D CD1 
7038  C  CD2 . LEU   D  191 ? 1.9355 0.7285 1.9231 -0.0064 -0.5650 0.2064  183 LEU   D CD2 
7039  N  N   . THR   D  192 ? 1.8981 0.5018 1.9307 -0.0566 -0.5063 0.2686  184 THR   D N   
7040  C  CA  . THR   D  192 ? 1.8756 0.6025 1.8483 -0.0228 -0.4960 0.2668  184 THR   D CA  
7041  C  C   . THR   D  192 ? 1.8749 0.6370 1.8222 -0.0438 -0.5004 0.2863  184 THR   D C   
7042  O  O   . THR   D  192 ? 1.8141 0.5375 1.7201 0.0434  -0.4849 0.3222  184 THR   D O   
7043  C  CB  . THR   D  192 ? 1.9020 0.6176 1.8626 -0.0294 -0.5172 0.2510  184 THR   D CB  
7044  O  OG1 . THR   D  192 ? 1.9137 0.5746 1.9119 -0.0491 -0.5068 0.2133  184 THR   D OG1 
7045  C  CG2 . THR   D  192 ? 1.9041 0.6344 1.8778 -0.0182 -0.5045 0.2449  184 THR   D CG2 
7046  N  N   . LEU   D  193 ? 1.8647 0.8224 1.8638 0.0269  -0.4697 0.2200  185 LEU   D N   
7047  C  CA  . LEU   D  193 ? 1.8642 0.9661 1.8927 -0.0163 -0.4764 0.1932  185 LEU   D CA  
7048  C  C   . LEU   D  193 ? 1.9050 0.9959 1.9217 -0.0244 -0.5109 0.2336  185 LEU   D C   
7049  O  O   . LEU   D  193 ? 1.9003 1.0828 1.9316 -0.0316 -0.5470 0.2233  185 LEU   D O   
7050  C  CB  . LEU   D  193 ? 1.8305 1.0319 1.8847 0.0047  -0.4669 0.1224  185 LEU   D CB  
7051  C  CG  . LEU   D  193 ? 1.8278 1.0891 1.8760 0.0012  -0.4395 0.0756  185 LEU   D CG  
7052  C  CD1 . LEU   D  193 ? 1.8179 1.1292 1.8493 0.0119  -0.4023 0.0554  185 LEU   D CD1 
7053  C  CD2 . LEU   D  193 ? 1.8270 1.1578 1.8305 -0.0392 -0.4487 0.0383  185 LEU   D CD2 
7054  N  N   . LYS   D  194 ? 1.9184 1.0476 1.9620 -0.0183 -0.5483 0.2262  186 LYS   D N   
7055  C  CA  . LYS   D  194 ? 1.9542 1.0670 1.9374 -0.0254 -0.5295 0.2154  186 LYS   D CA  
7056  C  C   . LYS   D  194 ? 1.9012 1.0118 2.0183 -0.0036 -0.5636 0.2515  186 LYS   D C   
7057  O  O   . LYS   D  194 ? 1.9177 0.8778 1.9957 0.0976  -0.5239 0.2944  186 LYS   D O   
7058  C  CB  . LYS   D  194 ? 2.0282 1.2138 1.8699 -0.0464 -0.5182 0.2337  186 LYS   D CB  
7059  C  CG  . LYS   D  194 ? 2.0957 1.2808 1.7706 -0.0291 -0.4745 0.2570  186 LYS   D CG  
7060  C  CD  . LYS   D  194 ? 2.1391 1.3403 1.7289 -0.0105 -0.4811 0.3072  186 LYS   D CD  
7061  C  CE  . LYS   D  194 ? 2.1920 1.3248 1.7332 0.0124  -0.4762 0.3150  186 LYS   D CE  
7062  N  NZ  . LYS   D  194 ? 2.2452 1.3806 1.7326 0.0087  -0.4515 0.3496  186 LYS   D NZ  
7063  N  N   . GLU   D  195 ? 1.8535 0.8595 2.0644 0.0492  -0.6088 0.1664  187 GLU   D N   
7064  C  CA  . GLU   D  195 ? 1.8702 0.8116 2.1177 0.0401  -0.6506 0.1804  187 GLU   D CA  
7065  C  C   . GLU   D  195 ? 1.8817 0.7770 2.1347 0.0593  -0.6569 0.1325  187 GLU   D C   
7066  O  O   . GLU   D  195 ? 1.8142 0.8083 2.1998 0.0317  -0.7323 0.1562  187 GLU   D O   
7067  C  CB  . GLU   D  195 ? 1.8859 0.8529 2.1372 -0.0169 -0.6334 0.1824  187 GLU   D CB  
7068  C  CG  . GLU   D  195 ? 1.9010 0.9857 2.1508 -0.0886 -0.6663 0.1736  187 GLU   D CG  
7069  C  CD  . GLU   D  195 ? 1.9330 1.1331 2.2072 -0.0981 -0.6236 0.1738  187 GLU   D CD  
7070  O  OE1 . GLU   D  195 ? 1.8825 1.1444 2.2185 -0.1511 -0.6089 0.1586  187 GLU   D OE1 
7071  O  OE2 . GLU   D  195 ? 1.8981 1.2753 2.2688 -0.1642 -0.5995 0.1755  187 GLU   D OE2 
7072  N  N   . ALA   D  196 ? 1.8769 0.7620 2.0840 0.0700  -0.6480 0.0946  188 ALA   D N   
7073  C  CA  . ALA   D  196 ? 1.8370 0.7638 2.0587 0.0248  -0.6012 0.0636  188 ALA   D CA  
7074  C  C   . ALA   D  196 ? 1.8746 0.7589 1.9632 0.0441  -0.5816 0.0251  188 ALA   D C   
7075  O  O   . ALA   D  196 ? 1.8406 0.7147 2.0507 0.0687  -0.5834 0.0579  188 ALA   D O   
7076  C  CB  . ALA   D  196 ? 1.8601 0.8039 2.0360 0.0331  -0.5820 0.0817  188 ALA   D CB  
7077  N  N   . GLU   D  197 ? 1.8914 0.7091 1.9433 -0.0729 -0.6048 0.0092  189 GLU   D N   
7078  C  CA  . GLU   D  197 ? 1.9624 0.6993 1.8819 -0.0640 -0.5804 -0.0196 189 GLU   D CA  
7079  C  C   . GLU   D  197 ? 1.9618 0.6969 1.8847 0.0234  -0.5827 -0.0034 189 GLU   D C   
7080  O  O   . GLU   D  197 ? 1.9629 0.6301 1.9563 0.0249  -0.5377 0.0407  189 GLU   D O   
7081  C  CB  . GLU   D  197 ? 2.0299 0.7357 1.9049 -0.1045 -0.5657 -0.0459 189 GLU   D CB  
7082  C  CG  . GLU   D  197 ? 2.0716 0.7361 1.8875 -0.0928 -0.5380 -0.0630 189 GLU   D CG  
7083  C  CD  . GLU   D  197 ? 2.1478 0.7370 1.9328 -0.1226 -0.5277 -0.0952 189 GLU   D CD  
7084  O  OE1 . GLU   D  197 ? 2.1888 0.6672 1.9183 -0.2268 -0.5807 -0.2380 189 GLU   D OE1 
7085  O  OE2 . GLU   D  197 ? 2.1949 0.7659 1.8718 -0.1305 -0.5208 -0.1177 189 GLU   D OE2 
7086  N  N   . LEU   D  198 ? 1.9765 0.6618 1.8563 0.0575  -0.5569 0.0000  190 LEU   D N   
7087  C  CA  . LEU   D  198 ? 1.9539 0.7107 1.8538 0.0930  -0.5433 0.0667  190 LEU   D CA  
7088  C  C   . LEU   D  198 ? 1.9627 0.6464 1.8481 0.1087  -0.5009 0.0864  190 LEU   D C   
7089  O  O   . LEU   D  198 ? 1.9842 0.6230 1.8216 0.1034  -0.5014 0.0488  190 LEU   D O   
7090  C  CB  . LEU   D  198 ? 1.9383 0.7413 1.8887 0.0978  -0.5385 0.0630  190 LEU   D CB  
7091  C  CG  . LEU   D  198 ? 1.9587 0.7743 1.8947 0.1098  -0.5318 0.0583  190 LEU   D CG  
7092  C  CD1 . LEU   D  198 ? 1.9611 0.7896 1.8851 0.1299  -0.5256 0.0780  190 LEU   D CD1 
7093  C  CD2 . LEU   D  198 ? 1.9546 0.8078 1.9400 0.1131  -0.5284 0.0550  190 LEU   D CD2 
7094  N  N   . LEU   D  199 ? 1.9580 0.6412 1.8475 0.1623  -0.5013 0.0997  191 LEU   D N   
7095  C  CA  . LEU   D  199 ? 1.9156 0.5655 1.8561 0.1675  -0.5530 0.1210  191 LEU   D CA  
7096  C  C   . LEU   D  199 ? 1.9182 0.4704 1.8136 0.1251  -0.5479 0.1281  191 LEU   D C   
7097  O  O   . LEU   D  199 ? 1.9656 0.5158 1.8343 0.0641  -0.5574 0.1152  191 LEU   D O   
7098  C  CB  . LEU   D  199 ? 1.9486 0.5571 1.8257 0.2490  -0.5371 0.1429  191 LEU   D CB  
7099  C  CG  . LEU   D  199 ? 2.0039 0.5797 1.8578 0.2910  -0.5242 0.1405  191 LEU   D CG  
7100  C  CD1 . LEU   D  199 ? 2.0565 0.6235 1.8949 0.3173  -0.5413 0.1528  191 LEU   D CD1 
7101  C  CD2 . LEU   D  199 ? 1.9903 0.5118 1.8494 0.3436  -0.5427 0.1618  191 LEU   D CD2 
7102  N  N   . VAL   D  200 ? 1.8518 0.4358 1.7588 0.0779  -0.5565 0.1053  192 VAL   D N   
7103  C  CA  . VAL   D  200 ? 1.8471 0.3632 1.7248 0.0779  -0.5524 0.1112  192 VAL   D CA  
7104  C  C   . VAL   D  200 ? 1.8876 0.2621 1.7237 0.1290  -0.5747 0.1383  192 VAL   D C   
7105  O  O   . VAL   D  200 ? 1.8906 0.2019 1.7268 0.1436  -0.5954 0.1984  192 VAL   D O   
7106  C  CB  . VAL   D  200 ? 1.8062 0.3318 1.6827 0.0295  -0.5535 0.1258  192 VAL   D CB  
7107  C  CG1 . VAL   D  200 ? 1.8072 0.3575 1.6541 -0.0067 -0.5312 0.1296  192 VAL   D CG1 
7108  C  CG2 . VAL   D  200 ? 1.7718 0.3284 1.6702 0.0266  -0.5605 0.1135  192 VAL   D CG2 
7109  N  N   . LEU   D  201 ? 1.9194 0.2987 1.7305 0.1561  -0.5904 0.1290  193 LEU   D N   
7110  C  CA  . LEU   D  201 ? 1.9379 0.4510 1.7396 0.1482  -0.5681 0.1644  193 LEU   D CA  
7111  C  C   . LEU   D  201 ? 1.9453 0.4656 1.8257 0.1697  -0.5807 0.1522  193 LEU   D C   
7112  O  O   . LEU   D  201 ? 1.8993 0.5199 1.8765 0.1729  -0.5801 0.2079  193 LEU   D O   
7113  C  CB  . LEU   D  201 ? 1.9665 0.4513 1.7204 0.1810  -0.5867 0.1989  193 LEU   D CB  
7114  C  CG  . LEU   D  201 ? 1.9834 0.4310 1.6812 0.1970  -0.5886 0.2364  193 LEU   D CG  
7115  C  CD1 . LEU   D  201 ? 1.9989 0.4192 1.6783 0.2163  -0.5641 0.2633  193 LEU   D CD1 
7116  C  CD2 . LEU   D  201 ? 2.0023 0.3976 1.6662 0.2118  -0.5851 0.2264  193 LEU   D CD2 
7117  N  N   . LYS   D  202 ? 1.9484 0.5980 1.9019 0.1689  -0.5698 0.1438  194 LYS   D N   
7118  C  CA  . LYS   D  202 ? 1.9880 0.5710 1.9347 0.1448  -0.5833 0.1346  194 LYS   D CA  
7119  C  C   . LYS   D  202 ? 1.9961 0.5996 1.9216 0.1513  -0.5655 0.1096  194 LYS   D C   
7120  O  O   . LYS   D  202 ? 2.0059 0.6901 2.0878 0.0691  -0.5501 0.1523  194 LYS   D O   
7121  C  CB  . LYS   D  202 ? 1.9900 0.5765 1.9643 0.1675  -0.5743 0.1411  194 LYS   D CB  
7122  C  CG  . LYS   D  202 ? 2.0530 0.5554 1.9953 0.1568  -0.5379 0.1470  194 LYS   D CG  
7123  C  CD  . LYS   D  202 ? 2.0633 0.5511 2.0388 0.1671  -0.5055 0.1601  194 LYS   D CD  
7124  C  CE  . LYS   D  202 ? 2.0896 0.5599 2.1165 0.2226  -0.4868 0.2168  194 LYS   D CE  
7125  N  NZ  . LYS   D  202 ? 2.1135 0.5886 2.1143 0.2418  -0.4662 0.2408  194 LYS   D NZ  
7126  N  N   . ILE   D  203 ? 1.9110 0.4510 1.8894 0.1408  -0.5730 0.0588  195 ILE   D N   
7127  C  CA  . ILE   D  203 ? 1.8434 0.5056 1.8375 0.1595  -0.5908 0.1124  195 ILE   D CA  
7128  C  C   . ILE   D  203 ? 1.8330 0.5416 1.7501 0.2245  -0.6095 0.0940  195 ILE   D C   
7129  O  O   . ILE   D  203 ? 1.8042 0.7061 1.7543 0.1686  -0.6366 0.0409  195 ILE   D O   
7130  C  CB  . ILE   D  203 ? 1.8153 0.4966 1.8553 0.1516  -0.5813 0.1167  195 ILE   D CB  
7131  C  CG1 . ILE   D  203 ? 1.8276 0.5727 1.9193 0.1845  -0.5590 0.1310  195 ILE   D CG1 
7132  C  CG2 . ILE   D  203 ? 1.7854 0.4834 1.8483 0.1436  -0.5732 0.1332  195 ILE   D CG2 
7133  C  CD1 . ILE   D  203 ? 1.8423 0.6625 1.9120 0.1996  -0.5205 0.1375  195 ILE   D CD1 
7134  N  N   . LEU   D  204 ? 1.8724 0.5119 1.6735 0.1914  -0.6407 0.0735  196 LEU   D N   
7135  C  CA  . LEU   D  204 ? 1.8959 0.5597 1.6379 0.1867  -0.6055 0.1036  196 LEU   D CA  
7136  C  C   . LEU   D  204 ? 1.9717 0.5504 1.6172 0.2675  -0.6363 0.1355  196 LEU   D C   
7137  O  O   . LEU   D  204 ? 1.9517 0.5152 1.5076 0.2778  -0.6552 0.2543  196 LEU   D O   
7138  C  CB  . LEU   D  204 ? 1.8869 0.6087 1.6390 0.1757  -0.5741 0.0652  196 LEU   D CB  
7139  C  CG  . LEU   D  204 ? 1.8814 0.5940 1.6576 0.1924  -0.5275 0.0655  196 LEU   D CG  
7140  C  CD1 . LEU   D  204 ? 1.8883 0.6380 1.6787 0.1522  -0.5015 0.0160  196 LEU   D CD1 
7141  C  CD2 . LEU   D  204 ? 1.8731 0.6451 1.6422 0.1889  -0.5070 0.0429  196 LEU   D CD2 
7142  N  N   . LYS   D  205 ? 1.9965 0.5902 1.6516 0.2762  -0.6630 0.1289  197 LYS   D N   
7143  C  CA  . LYS   D  205 ? 2.0739 0.6028 1.6940 0.2641  -0.6477 0.1456  197 LYS   D CA  
7144  C  C   . LYS   D  205 ? 2.1043 0.4682 1.7842 0.2154  -0.7003 0.2271  197 LYS   D C   
7145  O  O   . LYS   D  205 ? 2.2340 0.2697 1.7649 0.2829  -0.8312 0.2925  197 LYS   D O   
7146  C  CB  . LYS   D  205 ? 2.0704 0.6634 1.6693 0.3238  -0.6413 0.1638  197 LYS   D CB  
7147  C  CG  . LYS   D  205 ? 2.1064 0.7172 1.6549 0.3252  -0.6087 0.1616  197 LYS   D CG  
7148  C  CD  . LYS   D  205 ? 2.1718 0.8102 1.6486 0.2472  -0.5726 0.0987  197 LYS   D CD  
7149  C  CE  . LYS   D  205 ? 2.1519 0.8859 1.6662 0.2477  -0.5589 0.0992  197 LYS   D CE  
7150  N  NZ  . LYS   D  205 ? 2.1582 0.9150 1.7145 0.1981  -0.5300 0.0303  197 LYS   D NZ  
7151  N  N   . GLN   D  206 ? 2.0825 0.5453 1.8184 0.1419  -0.6853 0.2203  198 GLN   D N   
7152  C  CA  . GLN   D  206 ? 2.0592 0.6503 1.7755 0.0870  -0.6358 0.1584  198 GLN   D CA  
7153  C  C   . GLN   D  206 ? 2.1116 0.7081 1.7973 0.0006  -0.6382 0.1548  198 GLN   D C   
7154  O  O   . GLN   D  206 ? 2.2779 0.7649 1.9762 -0.1222 -0.5824 0.1986  198 GLN   D O   
7155  C  CB  . GLN   D  206 ? 2.0346 0.7774 1.7553 0.1043  -0.6435 0.1685  198 GLN   D CB  
7156  C  CG  . GLN   D  206 ? 2.0220 0.9433 1.7591 0.1091  -0.6265 0.1643  198 GLN   D CG  
7157  C  CD  . GLN   D  206 ? 2.0710 1.0847 1.7713 0.1280  -0.5788 0.1467  198 GLN   D CD  
7158  O  OE1 . GLN   D  206 ? 2.1052 1.2080 1.7833 0.0777  -0.5606 0.0795  198 GLN   D OE1 
7159  N  NE2 . GLN   D  206 ? 2.0272 1.1549 1.7594 0.1507  -0.6008 0.1662  198 GLN   D NE2 
7160  N  N   . VAL   D  207 ? 2.0890 0.5200 1.7657 -0.0753 -0.5755 0.1226  199 VAL   D N   
7161  C  CA  . VAL   D  207 ? 2.0359 0.5607 1.7895 -0.0790 -0.5599 0.1278  199 VAL   D CA  
7162  C  C   . VAL   D  207 ? 2.0653 0.5518 1.8083 -0.1013 -0.5216 0.1504  199 VAL   D C   
7163  O  O   . VAL   D  207 ? 2.0534 0.6225 1.8791 -0.1696 -0.5203 0.2039  199 VAL   D O   
7164  C  CB  . VAL   D  207 ? 1.9590 0.6086 1.7159 -0.1061 -0.5461 0.0908  199 VAL   D CB  
7165  C  CG1 . VAL   D  207 ? 1.9424 0.6362 1.7296 -0.1137 -0.5558 0.0830  199 VAL   D CG1 
7166  C  CG2 . VAL   D  207 ? 1.9222 0.6305 1.6748 -0.1065 -0.5522 0.0600  199 VAL   D CG2 
7167  N  N   . MET   D  208 ? 2.0939 0.5580 1.8149 -0.1154 -0.5303 0.1372  200 MET   D N   
7168  C  CA  . MET   D  208 ? 2.1276 0.6801 1.8392 -0.0904 -0.4937 0.1468  200 MET   D CA  
7169  C  C   . MET   D  208 ? 2.0938 0.7124 1.9333 -0.0819 -0.4512 0.1883  200 MET   D C   
7170  O  O   . MET   D  208 ? 2.0743 0.8099 2.0738 -0.0169 -0.4205 0.2282  200 MET   D O   
7171  C  CB  . MET   D  208 ? 2.1774 0.7089 1.7717 -0.0433 -0.4967 0.1764  200 MET   D CB  
7172  C  CG  . MET   D  208 ? 2.2104 0.7385 1.7043 0.0077  -0.4869 0.2044  200 MET   D CG  
7173  S  SD  . MET   D  208 ? 2.2919 0.8043 1.6048 0.0431  -0.4876 0.2413  200 MET   D SD  
7174  C  CE  . MET   D  208 ? 2.3311 0.7715 1.5410 0.0055  -0.4982 0.2808  200 MET   D CE  
7175  N  N   . GLU   D  209 ? 2.1134 0.8681 1.9957 -0.1408 -0.3691 0.1918  201 GLU   D N   
7176  C  CA  . GLU   D  209 ? 2.1772 0.8405 1.9802 -0.1205 -0.3952 0.2242  201 GLU   D CA  
7177  C  C   . GLU   D  209 ? 2.2160 0.6709 1.9733 -0.0723 -0.4528 0.3101  201 GLU   D C   
7178  O  O   . GLU   D  209 ? 2.2812 0.3829 1.9879 -0.1169 -0.3796 0.2745  201 GLU   D O   
7179  C  CB  . GLU   D  209 ? 2.1404 0.9216 2.1312 -0.2319 -0.3267 0.1601  201 GLU   D CB  
7180  C  CG  . GLU   D  209 ? 2.1380 0.9212 2.1946 -0.2827 -0.2828 0.0759  201 GLU   D CG  
7181  C  CD  . GLU   D  209 ? 2.1374 0.9055 2.3023 -0.3105 -0.3024 0.0738  201 GLU   D CD  
7182  O  OE1 . GLU   D  209 ? 2.1562 0.8795 2.2989 -0.3627 -0.3499 0.0623  201 GLU   D OE1 
7183  O  OE2 . GLU   D  209 ? 2.0370 0.9018 2.4238 -0.3261 -0.2901 0.0314  201 GLU   D OE2 
7184  N  N   . GLU   D  210 ? 2.2474 0.7272 1.8211 -0.0221 -0.5071 0.3326  202 GLU   D N   
7185  C  CA  . GLU   D  210 ? 2.2671 0.7876 1.8137 0.0052  -0.5616 0.3945  202 GLU   D CA  
7186  C  C   . GLU   D  210 ? 2.2943 0.6137 1.7384 -0.0052 -0.5659 0.4743  202 GLU   D C   
7187  O  O   . GLU   D  210 ? 2.4050 0.2867 1.6625 0.0372  -0.7039 0.4560  202 GLU   D O   
7188  C  CB  . GLU   D  210 ? 2.2416 0.9464 1.9202 0.0131  -0.5352 0.3257  202 GLU   D CB  
7189  C  CG  . GLU   D  210 ? 2.2540 1.0125 1.9454 0.0065  -0.5398 0.3537  202 GLU   D CG  
7190  C  CD  . GLU   D  210 ? 2.2437 1.1217 2.0584 0.0002  -0.5223 0.2639  202 GLU   D CD  
7191  O  OE1 . GLU   D  210 ? 2.0917 1.1006 1.9816 0.0583  -0.5727 0.2067  202 GLU   D OE1 
7192  O  OE2 . GLU   D  210 ? 2.3503 1.4869 2.1024 -0.1584 -0.4494 0.2213  202 GLU   D OE2 
7193  N  N   . LYS   D  211 ? 2.2293 0.7117 1.7728 0.0120  -0.6333 0.4288  203 LYS   D N   
7194  C  CA  . LYS   D  211 ? 2.1881 0.7101 1.8023 0.0234  -0.6083 0.4097  203 LYS   D CA  
7195  C  C   . LYS   D  211 ? 2.1369 0.7083 1.7647 -0.0246 -0.6055 0.4566  203 LYS   D C   
7196  O  O   . LYS   D  211 ? 2.1108 0.7995 1.7200 -0.0583 -0.5714 0.4826  203 LYS   D O   
7197  C  CB  . LYS   D  211 ? 2.1629 0.7586 1.7572 0.0232  -0.6328 0.3556  203 LYS   D CB  
7198  C  CG  . LYS   D  211 ? 2.1532 0.7509 1.7803 0.0129  -0.6143 0.3005  203 LYS   D CG  
7199  C  CD  . LYS   D  211 ? 2.1509 0.7650 1.7779 0.0410  -0.6187 0.2957  203 LYS   D CD  
7200  C  CE  . LYS   D  211 ? 2.1318 0.7540 1.7582 0.0518  -0.6090 0.3112  203 LYS   D CE  
7201  N  NZ  . LYS   D  211 ? 2.1777 0.7311 1.7628 0.0915  -0.6086 0.3337  203 LYS   D NZ  
7202  N  N   . LEU   D  212 ? 2.1209 0.8519 1.7454 -0.0106 -0.5743 0.4754  204 LEU   D N   
7203  C  CA  . LEU   D  212 ? 2.1539 0.8423 1.6796 0.0086  -0.5508 0.3880  204 LEU   D CA  
7204  C  C   . LEU   D  212 ? 2.1359 0.8380 1.6235 0.0183  -0.6088 0.4464  204 LEU   D C   
7205  O  O   . LEU   D  212 ? 2.1422 1.0361 1.5893 0.0158  -0.6631 0.4140  204 LEU   D O   
7206  C  CB  . LEU   D  212 ? 2.1682 0.8050 1.7730 0.0135  -0.4984 0.3450  204 LEU   D CB  
7207  C  CG  . LEU   D  212 ? 2.1259 0.7735 1.7510 0.0381  -0.4862 0.2840  204 LEU   D CG  
7208  C  CD1 . LEU   D  212 ? 2.1277 0.7143 1.7809 0.0520  -0.4408 0.2851  204 LEU   D CD1 
7209  C  CD2 . LEU   D  212 ? 2.1054 0.7373 1.7592 0.0583  -0.5050 0.2981  204 LEU   D CD2 
7210  N  N   . ASP   D  213 ? 2.1234 0.7803 1.5706 -0.0324 -0.6287 0.4238  205 ASP   D N   
7211  C  CA  . ASP   D  213 ? 2.1221 0.7659 1.5883 -0.0810 -0.6358 0.4211  205 ASP   D CA  
7212  C  C   . ASP   D  213 ? 2.0779 0.7413 1.6211 -0.0898 -0.6013 0.3794  205 ASP   D C   
7213  O  O   . ASP   D  213 ? 2.0225 0.6315 1.6034 -0.1103 -0.5417 0.3673  205 ASP   D O   
7214  C  CB  . ASP   D  213 ? 2.2000 0.6734 1.5736 -0.0801 -0.6467 0.4517  205 ASP   D CB  
7215  C  CG  . ASP   D  213 ? 2.2004 0.6359 1.5174 -0.0872 -0.6185 0.4771  205 ASP   D CG  
7216  O  OD1 . ASP   D  213 ? 2.2460 0.6543 1.5592 0.0199  -0.6349 0.4492  205 ASP   D OD1 
7217  O  OD2 . ASP   D  213 ? 2.2503 0.6965 1.4820 -0.1111 -0.5945 0.4677  205 ASP   D OD2 
7218  N  N   . GLU   D  214 ? 2.1009 0.7938 1.6229 -0.0943 -0.5707 0.3607  206 GLU   D N   
7219  C  CA  . GLU   D  214 ? 2.1024 0.8062 1.6299 -0.0790 -0.5373 0.3881  206 GLU   D CA  
7220  C  C   . GLU   D  214 ? 2.0880 0.8016 1.6109 -0.0798 -0.5126 0.3958  206 GLU   D C   
7221  O  O   . GLU   D  214 ? 2.0252 0.8398 1.6263 -0.0183 -0.5250 0.3995  206 GLU   D O   
7222  C  CB  . GLU   D  214 ? 2.1510 0.9063 1.6216 -0.0903 -0.5104 0.3548  206 GLU   D CB  
7223  C  CG  . GLU   D  214 ? 2.1907 0.9713 1.6218 -0.0964 -0.4902 0.3505  206 GLU   D CG  
7224  C  CD  . GLU   D  214 ? 2.2264 1.0831 1.5604 -0.0930 -0.5252 0.3551  206 GLU   D CD  
7225  O  OE1 . GLU   D  214 ? 2.2365 1.2090 1.5828 -0.0838 -0.5335 0.2332  206 GLU   D OE1 
7226  O  OE2 . GLU   D  214 ? 2.2058 1.1752 1.5662 -0.0673 -0.5441 0.3072  206 GLU   D OE2 
7227  N  N   . ASN   D  215 ? 2.1180 0.7530 1.6173 -0.0578 -0.4775 0.4342  207 ASN   D N   
7228  C  CA  . ASN   D  215 ? 2.1274 0.7656 1.5721 -0.0017 -0.4388 0.4507  207 ASN   D CA  
7229  C  C   . ASN   D  215 ? 2.1214 0.6874 1.5422 0.0832  -0.4711 0.5080  207 ASN   D C   
7230  O  O   . ASN   D  215 ? 2.1134 0.7686 1.5001 0.1164  -0.4498 0.4900  207 ASN   D O   
7231  C  CB  . ASN   D  215 ? 2.1649 0.9111 1.5794 -0.0409 -0.3437 0.3814  207 ASN   D CB  
7232  C  CG  . ASN   D  215 ? 2.1860 0.9547 1.6387 -0.1014 -0.3102 0.3156  207 ASN   D CG  
7233  O  OD1 . ASN   D  215 ? 2.1832 0.9434 1.5946 -0.1099 -0.2408 0.3167  207 ASN   D OD1 
7234  N  ND2 . ASN   D  215 ? 2.2104 1.1073 1.6883 -0.1151 -0.2643 0.3261  207 ASN   D ND2 
7235  N  N   . ASN   D  216 ? 2.1601 0.6535 1.5141 0.0951  -0.5263 0.4901  208 ASN   D N   
7236  C  CA  . ASN   D  216 ? 2.1568 0.7235 1.5690 0.1103  -0.5471 0.4267  208 ASN   D CA  
7237  C  C   . ASN   D  216 ? 2.0780 0.6671 1.5904 0.1106  -0.5526 0.3490  208 ASN   D C   
7238  O  O   . ASN   D  216 ? 2.1502 0.6901 1.6282 0.1744  -0.5390 0.2921  208 ASN   D O   
7239  C  CB  . ASN   D  216 ? 2.1778 0.7370 1.6816 0.0695  -0.5520 0.4235  208 ASN   D CB  
7240  C  CG  . ASN   D  216 ? 2.1760 0.8305 1.7982 0.0827  -0.6003 0.3816  208 ASN   D CG  
7241  O  OD1 . ASN   D  216 ? 2.1690 1.0125 1.8101 0.0470  -0.5975 0.3700  208 ASN   D OD1 
7242  N  ND2 . ASN   D  216 ? 2.2144 0.8154 1.9145 0.0187  -0.6145 0.3505  208 ASN   D ND2 
7243  N  N   . ALA   D  217 ? 2.0746 0.6818 1.4943 0.1421  -0.5899 0.2521  209 ALA   D N   
7244  C  CA  . ALA   D  217 ? 2.0033 0.6538 1.4475 0.1151  -0.6220 0.1871  209 ALA   D CA  
7245  C  C   . ALA   D  217 ? 2.0045 0.6912 1.3977 0.0641  -0.6160 0.1518  209 ALA   D C   
7246  O  O   . ALA   D  217 ? 2.0654 0.8335 1.4085 0.0188  -0.5887 0.1225  209 ALA   D O   
7247  C  CB  . ALA   D  217 ? 2.0180 0.6262 1.4647 0.1267  -0.6464 0.1916  209 ALA   D CB  
7248  N  N   . GLN   D  218 ? 1.9508 0.6059 1.3610 0.1076  -0.6254 0.1098  210 GLN   D N   
7249  C  CA  . GLN   D  218 ? 1.9437 0.5747 1.3663 0.1673  -0.5999 0.1411  210 GLN   D CA  
7250  C  C   . GLN   D  218 ? 1.9465 0.5512 1.3884 0.1711  -0.6046 0.1683  210 GLN   D C   
7251  O  O   . GLN   D  218 ? 1.9546 0.4495 1.3391 0.1981  -0.6263 0.2436  210 GLN   D O   
7252  C  CB  . GLN   D  218 ? 1.8973 0.5346 1.3404 0.1610  -0.5617 0.0824  210 GLN   D CB  
7253  C  CG  . GLN   D  218 ? 1.8718 0.5326 1.3438 0.1922  -0.5236 0.0743  210 GLN   D CG  
7254  C  CD  . GLN   D  218 ? 1.8761 0.3867 1.3432 0.1938  -0.4463 0.0034  210 GLN   D CD  
7255  O  OE1 . GLN   D  218 ? 1.9255 0.2617 1.3555 0.1891  -0.4487 -0.0191 210 GLN   D OE1 
7256  N  NE2 . GLN   D  218 ? 1.8443 0.4198 1.3348 0.1801  -0.4244 -0.0076 210 GLN   D NE2 
7257  N  N   . LEU   D  219 ? 1.9524 0.6476 1.4880 0.1206  -0.6339 0.1647  211 LEU   D N   
7258  C  CA  . LEU   D  219 ? 1.9580 0.7356 1.5462 0.0821  -0.6263 0.1563  211 LEU   D CA  
7259  C  C   . LEU   D  219 ? 1.9672 0.7258 1.5250 0.0340  -0.6503 0.1583  211 LEU   D C   
7260  O  O   . LEU   D  219 ? 2.0031 0.7704 1.5417 0.0348  -0.6224 0.1410  211 LEU   D O   
7261  C  CB  . LEU   D  219 ? 1.9617 0.7453 1.6274 0.0965  -0.6430 0.1756  211 LEU   D CB  
7262  C  CG  . LEU   D  219 ? 2.0197 0.7350 1.6802 0.0992  -0.6088 0.2013  211 LEU   D CG  
7263  C  CD1 . LEU   D  219 ? 2.0418 0.7757 1.7250 0.0778  -0.6376 0.2067  211 LEU   D CD1 
7264  C  CD2 . LEU   D  219 ? 2.0101 0.7581 1.6559 0.0828  -0.6185 0.2294  211 LEU   D CD2 
7265  N  N   . SER   D  220 ? 1.9188 0.8474 1.5081 -0.0382 -0.6620 0.1179  212 SER   D N   
7266  C  CA  . SER   D  220 ? 1.8987 0.8354 1.5328 -0.0628 -0.6899 0.0837  212 SER   D CA  
7267  C  C   . SER   D  220 ? 1.9071 0.8547 1.5606 -0.0211 -0.6576 0.0587  212 SER   D C   
7268  O  O   . SER   D  220 ? 1.8799 0.9482 1.4824 -0.0027 -0.6962 -0.0037 212 SER   D O   
7269  C  CB  . SER   D  220 ? 1.8437 0.8391 1.5555 -0.1033 -0.6843 0.0769  212 SER   D CB  
7270  O  OG  . SER   D  220 ? 1.8333 0.9388 1.5602 -0.0994 -0.6255 0.0922  212 SER   D OG  
7271  N  N   . CYS   D  221 ? 1.9647 0.8414 1.6237 0.0094  -0.6176 0.0997  213 CYS   D N   
7272  C  CA  . CYS   D  221 ? 1.9662 0.7943 1.6530 0.0369  -0.5918 0.0869  213 CYS   D CA  
7273  C  C   . CYS   D  221 ? 1.9770 0.7654 1.6487 0.0484  -0.5400 0.0443  213 CYS   D C   
7274  O  O   . CYS   D  221 ? 2.0828 0.6572 1.6922 0.0143  -0.5301 -0.0316 213 CYS   D O   
7275  C  CB  . CYS   D  221 ? 1.9856 0.7554 1.6777 0.0428  -0.6173 0.0685  213 CYS   D CB  
7276  S  SG  . CYS   D  221 ? 2.0783 0.5976 1.7745 0.0595  -0.6004 0.0935  213 CYS   D SG  
7277  N  N   . ILE   D  222 ? 1.9728 0.7669 1.6498 0.0404  -0.5363 0.0362  214 ILE   D N   
7278  C  CA  . ILE   D  222 ? 1.9687 0.7509 1.6726 0.0350  -0.5243 0.0168  214 ILE   D CA  
7279  C  C   . ILE   D  222 ? 1.9329 0.7700 1.6637 0.0995  -0.5548 0.0705  214 ILE   D C   
7280  O  O   . ILE   D  222 ? 1.9125 0.7581 1.5960 0.0688  -0.6115 0.0136  214 ILE   D O   
7281  C  CB  . ILE   D  222 ? 2.0070 0.7969 1.6898 0.0641  -0.5329 0.0166  214 ILE   D CB  
7282  C  CG1 . ILE   D  222 ? 2.0121 0.8521 1.7624 0.0458  -0.4731 -0.0049 214 ILE   D CG1 
7283  C  CG2 . ILE   D  222 ? 2.0239 0.8016 1.7055 0.0565  -0.5180 0.0113  214 ILE   D CG2 
7284  C  CD1 . ILE   D  222 ? 2.0475 0.8927 1.7895 0.0786  -0.4815 -0.0683 214 ILE   D CD1 
7285  N  N   . THR   D  223 ? 1.9021 0.7364 1.6816 0.0897  -0.5693 0.1106  215 THR   D N   
7286  C  CA  . THR   D  223 ? 1.8765 0.7974 1.6624 0.1013  -0.5831 0.1648  215 THR   D CA  
7287  C  C   . THR   D  223 ? 1.8619 0.7838 1.7219 0.0305  -0.5537 0.1557  215 THR   D C   
7288  O  O   . THR   D  223 ? 1.8137 0.7379 1.6622 -0.0045 -0.5910 0.1537  215 THR   D O   
7289  C  CB  . THR   D  223 ? 1.8604 0.7722 1.6729 0.1659  -0.5947 0.1674  215 THR   D CB  
7290  O  OG1 . THR   D  223 ? 1.9170 0.6067 1.5877 0.1858  -0.6567 0.2043  215 THR   D OG1 
7291  C  CG2 . THR   D  223 ? 1.8686 0.7943 1.6458 0.1486  -0.6100 0.1855  215 THR   D CG2 
7292  N  N   . LYS   D  224 ? 1.8623 0.8004 1.7702 0.0002  -0.5463 0.1394  216 LYS   D N   
7293  C  CA  . LYS   D  224 ? 1.8000 0.8020 1.6961 -0.0266 -0.5559 0.1378  216 LYS   D CA  
7294  C  C   . LYS   D  224 ? 1.8579 0.7250 1.7383 -0.0585 -0.5751 0.1149  216 LYS   D C   
7295  O  O   . LYS   D  224 ? 1.8096 0.6536 1.6583 -0.1099 -0.5907 0.0215  216 LYS   D O   
7296  C  CB  . LYS   D  224 ? 1.7871 0.8754 1.6793 -0.0188 -0.5623 0.1725  216 LYS   D CB  
7297  C  CG  . LYS   D  224 ? 1.7428 0.9108 1.6715 -0.0802 -0.5209 0.1933  216 LYS   D CG  
7298  C  CD  . LYS   D  224 ? 1.7266 1.0872 1.7235 -0.1196 -0.5054 0.1766  216 LYS   D CD  
7299  C  CE  . LYS   D  224 ? 1.7287 1.1178 1.7580 -0.1856 -0.4629 0.1878  216 LYS   D CE  
7300  N  NZ  . LYS   D  224 ? 1.7355 1.2459 1.7833 -0.1835 -0.4499 0.2204  216 LYS   D NZ  
7301  N  N   . GLN   D  225 ? 1.8829 0.7293 1.7612 -0.0527 -0.5895 0.1294  217 GLN   D N   
7302  C  CA  . GLN   D  225 ? 1.9188 0.7292 1.7549 -0.0380 -0.6046 0.1353  217 GLN   D CA  
7303  C  C   . GLN   D  225 ? 1.9604 0.5924 1.7380 -0.0274 -0.5640 0.1601  217 GLN   D C   
7304  O  O   . GLN   D  225 ? 2.1218 0.5418 1.7078 -0.0679 -0.4952 0.1075  217 GLN   D O   
7305  C  CB  . GLN   D  225 ? 1.9088 0.9372 1.7633 -0.0886 -0.6432 0.1315  217 GLN   D CB  
7306  C  CG  . GLN   D  225 ? 1.9020 1.0521 1.8273 -0.1326 -0.6522 0.0659  217 GLN   D CG  
7307  C  CD  . GLN   D  225 ? 1.9009 1.1740 1.8221 -0.2066 -0.7062 0.0422  217 GLN   D CD  
7308  O  OE1 . GLN   D  225 ? 1.9089 1.2336 1.8206 -0.2872 -0.7383 0.0391  217 GLN   D OE1 
7309  N  NE2 . GLN   D  225 ? 1.9028 1.2385 1.8913 -0.2427 -0.6914 0.0108  217 GLN   D NE2 
7310  N  N   . ASP   D  226 ? 1.9608 0.5841 1.7573 0.0246  -0.5429 0.2246  218 ASP   D N   
7311  C  CA  . ASP   D  226 ? 1.9755 0.6126 1.7742 0.0454  -0.5216 0.2018  218 ASP   D CA  
7312  C  C   . ASP   D  226 ? 1.9204 0.5242 1.7268 0.0356  -0.4583 0.2136  218 ASP   D C   
7313  O  O   . ASP   D  226 ? 1.9555 0.3621 1.8269 0.0040  -0.3885 0.1625  218 ASP   D O   
7314  C  CB  . ASP   D  226 ? 2.0346 0.7023 1.7505 0.0320  -0.5622 0.2199  218 ASP   D CB  
7315  C  CG  . ASP   D  226 ? 2.0655 0.7805 1.8268 0.0330  -0.6003 0.1689  218 ASP   D CG  
7316  O  OD1 . ASP   D  226 ? 2.1125 0.7428 1.9023 0.0691  -0.5272 0.1920  218 ASP   D OD1 
7317  O  OD2 . ASP   D  226 ? 2.1418 0.8180 1.8411 0.0402  -0.7031 0.2391  218 ASP   D OD2 
7318  N  N   . GLY   D  227 ? 1.9040 0.5138 1.6954 0.0262  -0.4893 0.2453  219 GLY   D N   
7319  C  CA  . GLY   D  227 ? 1.8923 0.6431 1.6447 0.0512  -0.4778 0.2495  219 GLY   D CA  
7320  C  C   . GLY   D  227 ? 1.8655 0.6717 1.6172 0.0621  -0.4616 0.3009  219 GLY   D C   
7321  O  O   . GLY   D  227 ? 1.9488 0.7160 1.6555 0.1438  -0.4307 0.3179  219 GLY   D O   
7322  N  N   . PHE   D  228 ? 1.8704 0.6522 1.5872 0.0134  -0.4409 0.3006  220 PHE   D N   
7323  C  CA  . PHE   D  228 ? 1.9217 0.5736 1.5607 0.0540  -0.4789 0.2982  220 PHE   D CA  
7324  C  C   . PHE   D  228 ? 1.9243 0.5010 1.5537 -0.0214 -0.4767 0.2017  220 PHE   D C   
7325  O  O   . PHE   D  228 ? 1.9742 0.2825 1.5148 -0.1169 -0.4709 0.2427  220 PHE   D O   
7326  C  CB  . PHE   D  228 ? 1.9216 0.5988 1.5520 0.0129  -0.4670 0.3247  220 PHE   D CB  
7327  C  CG  . PHE   D  228 ? 1.9574 0.6396 1.5692 -0.0101 -0.4596 0.3925  220 PHE   D CG  
7328  C  CD1 . PHE   D  228 ? 1.9344 0.6721 1.5693 0.0141  -0.4715 0.3751  220 PHE   D CD1 
7329  C  CD2 . PHE   D  228 ? 1.9757 0.6897 1.5832 0.0000  -0.4489 0.3935  220 PHE   D CD2 
7330  C  CE1 . PHE   D  228 ? 1.9643 0.6761 1.5750 -0.0044 -0.4962 0.3550  220 PHE   D CE1 
7331  C  CE2 . PHE   D  228 ? 1.9941 0.7020 1.5836 -0.0259 -0.4748 0.3632  220 PHE   D CE2 
7332  C  CZ  . PHE   D  228 ? 1.9744 0.7158 1.5742 -0.0183 -0.4883 0.3545  220 PHE   D CZ  
7333  N  N   . LYS   D  229 ? 1.9699 0.5596 1.5585 0.0363  -0.5199 0.2068  221 LYS   D N   
7334  C  CA  . LYS   D  229 ? 2.0399 0.6743 1.5572 -0.0034 -0.4542 0.1164  221 LYS   D CA  
7335  C  C   . LYS   D  229 ? 1.9394 0.6817 1.4902 -0.0137 -0.4616 0.0936  221 LYS   D C   
7336  O  O   . LYS   D  229 ? 2.0278 0.6107 1.4857 0.0066  -0.4725 0.1038  221 LYS   D O   
7337  C  CB  . LYS   D  229 ? 2.0926 0.7834 1.6170 0.0036  -0.4888 0.0540  221 LYS   D CB  
7338  C  CG  . LYS   D  229 ? 2.1548 0.7718 1.6920 0.0343  -0.4797 0.0461  221 LYS   D CG  
7339  C  CD  . LYS   D  229 ? 2.2026 0.8426 1.7129 0.0662  -0.4506 0.0654  221 LYS   D CD  
7340  C  CE  . LYS   D  229 ? 2.2442 0.8679 1.7406 0.0613  -0.4722 0.0473  221 LYS   D CE  
7341  N  NZ  . LYS   D  229 ? 2.2868 0.8778 1.7712 0.0649  -0.4574 0.0643  221 LYS   D NZ  
7342  N  N   . ILE   D  230 ? 1.9065 0.6627 1.4407 -0.0190 -0.4977 0.0667  222 ILE   D N   
7343  C  CA  . ILE   D  230 ? 1.9019 0.6228 1.4416 0.0229  -0.4971 0.0535  222 ILE   D CA  
7344  C  C   . ILE   D  230 ? 1.8572 0.5471 1.4528 0.0002  -0.5279 0.0287  222 ILE   D C   
7345  O  O   . ILE   D  230 ? 1.8747 0.6642 1.4135 0.0591  -0.5251 0.0099  222 ILE   D O   
7346  C  CB  . ILE   D  230 ? 1.8994 0.5809 1.4362 0.0326  -0.4481 0.0683  222 ILE   D CB  
7347  C  CG1 . ILE   D  230 ? 1.8919 0.6191 1.4116 0.0449  -0.4305 0.0291  222 ILE   D CG1 
7348  C  CG2 . ILE   D  230 ? 1.9509 0.6022 1.4438 0.0314  -0.4355 0.1036  222 ILE   D CG2 
7349  C  CD1 . ILE   D  230 ? 1.8873 0.6140 1.3791 0.0204  -0.4195 0.0089  222 ILE   D CD1 
7350  N  N   . TYR   D  231 ? 1.8468 0.5123 1.5063 -0.0294 -0.5261 0.0262  223 TYR   D N   
7351  C  CA  . TYR   D  231 ? 1.8774 0.5144 1.5435 0.0237  -0.5438 0.0627  223 TYR   D CA  
7352  C  C   . TYR   D  231 ? 1.8780 0.5937 1.5702 0.0259  -0.5340 0.0634  223 TYR   D C   
7353  O  O   . TYR   D  231 ? 1.8073 0.6469 1.5393 0.0791  -0.5555 0.1041  223 TYR   D O   
7354  C  CB  . TYR   D  231 ? 1.8969 0.5058 1.5480 0.0408  -0.5660 0.1170  223 TYR   D CB  
7355  C  CG  . TYR   D  231 ? 1.8868 0.5107 1.5846 0.0665  -0.5621 0.1398  223 TYR   D CG  
7356  C  CD1 . TYR   D  231 ? 1.8954 0.5046 1.6360 0.0553  -0.5442 0.1188  223 TYR   D CD1 
7357  C  CD2 . TYR   D  231 ? 1.9066 0.5360 1.6199 0.0982  -0.5594 0.1866  223 TYR   D CD2 
7358  C  CE1 . TYR   D  231 ? 1.8808 0.5712 1.6893 0.0961  -0.5224 0.0946  223 TYR   D CE1 
7359  C  CE2 . TYR   D  231 ? 1.9104 0.5181 1.6605 0.0946  -0.5492 0.1875  223 TYR   D CE2 
7360  C  CZ  . TYR   D  231 ? 1.9084 0.4832 1.7001 0.0808  -0.5449 0.1332  223 TYR   D CZ  
7361  O  OH  . TYR   D  231 ? 1.8671 0.4277 1.7671 0.0901  -0.5489 0.1035  223 TYR   D OH  
7362  N  N   . ASP   D  232 ? 1.9460 0.7189 1.6041 0.0233  -0.5584 0.0054  224 ASP   D N   
7363  C  CA  . ASP   D  232 ? 1.9856 0.8379 1.7199 -0.0002 -0.4815 0.0132  224 ASP   D CA  
7364  C  C   . ASP   D  232 ? 2.0106 0.8350 1.6910 -0.0182 -0.4875 0.0155  224 ASP   D C   
7365  O  O   . ASP   D  232 ? 1.9967 0.8488 1.7169 -0.0006 -0.5055 0.0198  224 ASP   D O   
7366  C  CB  . ASP   D  232 ? 2.0200 1.0887 1.7748 0.0216  -0.4838 -0.0951 224 ASP   D CB  
7367  C  CG  . ASP   D  232 ? 1.9819 1.1242 1.9324 0.0002  -0.4686 -0.1098 224 ASP   D CG  
7368  O  OD1 . ASP   D  232 ? 1.9456 1.4389 2.0030 0.0885  -0.4448 -0.1805 224 ASP   D OD1 
7369  O  OD2 . ASP   D  232 ? 1.8688 1.4068 2.0188 -0.0117 -0.4692 -0.1779 224 ASP   D OD2 
7370  N  N   . ASN   D  233 ? 2.0708 0.8016 1.6654 -0.0196 -0.4962 0.0769  225 ASN   D N   
7371  C  CA  . ASN   D  233 ? 2.1007 0.8255 1.6894 -0.0429 -0.4495 0.1518  225 ASN   D CA  
7372  C  C   . ASN   D  233 ? 2.1394 0.8365 1.7420 -0.0681 -0.4859 0.1424  225 ASN   D C   
7373  O  O   . ASN   D  233 ? 2.1836 0.8723 1.8605 -0.0266 -0.4878 0.0694  225 ASN   D O   
7374  C  CB  . ASN   D  233 ? 2.0889 0.8147 1.6307 -0.0256 -0.4640 0.1896  225 ASN   D CB  
7375  C  CG  . ASN   D  233 ? 2.0508 0.7687 1.5884 -0.0612 -0.4191 0.2099  225 ASN   D CG  
7376  O  OD1 . ASN   D  233 ? 2.1009 0.8198 1.5933 -0.1179 -0.3462 0.1992  225 ASN   D OD1 
7377  N  ND2 . ASN   D  233 ? 2.0501 0.7220 1.6026 -0.0710 -0.3967 0.2044  225 ASN   D ND2 
7378  N  N   . GLU   D  234 ? 2.1636 0.7570 1.8191 -0.0799 -0.4342 0.1421  226 GLU   D N   
7379  C  CA  . GLU   D  234 ? 2.1359 0.7530 1.9231 -0.0756 -0.4681 0.1723  226 GLU   D CA  
7380  C  C   . GLU   D  234 ? 2.1127 0.6753 1.8513 -0.0925 -0.5052 0.1563  226 GLU   D C   
7381  O  O   . GLU   D  234 ? 2.0496 0.7908 1.8369 -0.0999 -0.5332 0.1467  226 GLU   D O   
7382  C  CB  . GLU   D  234 ? 2.2088 0.7260 2.0610 -0.0921 -0.4586 0.1370  226 GLU   D CB  
7383  C  CG  . GLU   D  234 ? 2.2688 0.8511 2.1436 -0.0869 -0.4000 0.1415  226 GLU   D CG  
7384  C  CD  . GLU   D  234 ? 2.2547 0.9437 2.2804 -0.1114 -0.4041 0.0960  226 GLU   D CD  
7385  O  OE1 . GLU   D  234 ? 2.3291 0.9561 2.4198 -0.1347 -0.3361 0.1311  226 GLU   D OE1 
7386  O  OE2 . GLU   D  234 ? 2.3177 1.0076 2.3002 -0.0779 -0.4293 0.1327  226 GLU   D OE2 
7387  N  N   . LYS   D  235 ? 2.0811 0.6713 1.8031 -0.1067 -0.5289 0.1217  227 LYS   D N   
7388  C  CA  . LYS   D  235 ? 2.0479 0.7063 1.8181 -0.0983 -0.5630 0.1634  227 LYS   D CA  
7389  C  C   . LYS   D  235 ? 2.0046 0.6640 1.8349 -0.0120 -0.5714 0.2291  227 LYS   D C   
7390  O  O   . LYS   D  235 ? 2.0146 0.6439 1.8584 -0.0049 -0.6180 0.3631  227 LYS   D O   
7391  C  CB  . LYS   D  235 ? 2.0541 0.7303 1.7667 -0.1384 -0.5777 0.1619  227 LYS   D CB  
7392  C  CG  . LYS   D  235 ? 2.0366 0.8325 1.8289 -0.1570 -0.5865 0.1506  227 LYS   D CG  
7393  C  CD  . LYS   D  235 ? 2.0327 0.9456 1.8581 -0.1740 -0.5386 0.2140  227 LYS   D CD  
7394  C  CE  . LYS   D  235 ? 1.9909 1.1135 1.9316 -0.1451 -0.5408 0.1970  227 LYS   D CE  
7395  N  NZ  . LYS   D  235 ? 1.9410 1.1515 1.9261 -0.1274 -0.5401 0.2162  227 LYS   D NZ  
7396  N  N   . THR   D  236 ? 1.9761 0.6137 1.8266 0.0089  -0.5468 0.2156  228 THR   D N   
7397  C  CA  . THR   D  236 ? 1.9434 0.6067 1.8610 0.0239  -0.5335 0.2084  228 THR   D CA  
7398  C  C   . THR   D  236 ? 2.0023 0.6837 1.8237 -0.0094 -0.5207 0.2574  228 THR   D C   
7399  O  O   . THR   D  236 ? 2.0177 0.7975 1.9526 0.0344  -0.4510 0.2588  228 THR   D O   
7400  C  CB  . THR   D  236 ? 1.8983 0.5658 1.8589 0.0260  -0.5085 0.2170  228 THR   D CB  
7401  O  OG1 . THR   D  236 ? 1.8975 0.4719 1.8677 0.0060  -0.4842 0.1663  228 THR   D OG1 
7402  C  CG2 . THR   D  236 ? 1.8547 0.6222 1.8426 0.0188  -0.5138 0.1847  228 THR   D CG2 
7403  N  N   . ALA   D  237 ? 2.0000 0.6060 1.7721 0.0061  -0.5560 0.2344  229 ALA   D N   
7404  C  CA  . ALA   D  237 ? 2.0199 0.6393 1.7446 0.0432  -0.5883 0.2441  229 ALA   D CA  
7405  C  C   . ALA   D  237 ? 2.0448 0.7114 1.7476 0.0254  -0.6296 0.3002  229 ALA   D C   
7406  O  O   . ALA   D  237 ? 2.0807 0.7971 1.7973 0.1088  -0.5907 0.3621  229 ALA   D O   
7407  C  CB  . ALA   D  237 ? 2.0453 0.5223 1.6600 0.0385  -0.6208 0.2697  229 ALA   D CB  
7408  N  N   . GLU   D  238 ? 2.0358 0.5938 1.7800 0.1212  -0.6413 0.2824  230 GLU   D N   
7409  C  CA  . GLU   D  238 ? 2.0441 0.6289 1.8472 0.1054  -0.6705 0.2520  230 GLU   D CA  
7410  C  C   . GLU   D  238 ? 2.0112 0.5600 1.8706 0.0895  -0.6871 0.2237  230 GLU   D C   
7411  O  O   . GLU   D  238 ? 1.9987 0.6876 1.8974 0.0846  -0.7334 0.2533  230 GLU   D O   
7412  C  CB  . GLU   D  238 ? 2.0369 0.7189 1.8561 0.0754  -0.6634 0.1559  230 GLU   D CB  
7413  C  CG  . GLU   D  238 ? 2.0879 0.9514 1.8696 0.0876  -0.6283 0.1468  230 GLU   D CG  
7414  C  CD  . GLU   D  238 ? 2.1137 1.0552 1.9624 0.0154  -0.6182 0.0720  230 GLU   D CD  
7415  O  OE1 . GLU   D  238 ? 2.1965 1.1482 2.0802 0.0615  -0.5347 0.0370  230 GLU   D OE1 
7416  O  OE2 . GLU   D  238 ? 2.0998 1.1863 2.0289 0.0269  -0.6038 0.0481  230 GLU   D OE2 
7417  N  N   . LEU   D  239 ? 1.9641 0.5358 1.8624 0.0951  -0.7130 0.1596  231 LEU   D N   
7418  C  CA  . LEU   D  239 ? 1.9578 0.5887 1.8858 0.0948  -0.7021 0.1440  231 LEU   D CA  
7419  C  C   . LEU   D  239 ? 1.9632 0.5897 1.9532 0.0770  -0.6961 0.1517  231 LEU   D C   
7420  O  O   . LEU   D  239 ? 2.0193 0.5373 2.0069 0.0602  -0.6853 0.0699  231 LEU   D O   
7421  C  CB  . LEU   D  239 ? 1.9554 0.4830 1.8508 0.0681  -0.6760 0.1094  231 LEU   D CB  
7422  C  CG  . LEU   D  239 ? 1.9841 0.4664 1.7875 0.0851  -0.6842 0.0496  231 LEU   D CG  
7423  C  CD1 . LEU   D  239 ? 1.9793 0.4456 1.7912 0.0986  -0.6665 0.0456  231 LEU   D CD1 
7424  C  CD2 . LEU   D  239 ? 1.9768 0.4182 1.7800 0.0893  -0.7005 0.0293  231 LEU   D CD2 
7425  N  N   . ILE   D  240 ? 1.9726 0.6231 1.9590 0.0609  -0.6944 0.1658  232 ILE   D N   
7426  C  CA  . ILE   D  240 ? 1.9652 0.6282 1.9601 0.0431  -0.7016 0.2093  232 ILE   D CA  
7427  C  C   . ILE   D  240 ? 2.0421 0.5998 1.9870 0.0242  -0.7168 0.2638  232 ILE   D C   
7428  O  O   . ILE   D  240 ? 1.9994 0.5025 2.0374 -0.0311 -0.7667 0.3136  232 ILE   D O   
7429  C  CB  . ILE   D  240 ? 1.9879 0.6162 1.9868 0.0051  -0.6483 0.1929  232 ILE   D CB  
7430  C  CG1 . ILE   D  240 ? 1.9449 0.7129 1.9676 -0.0086 -0.6359 0.1602  232 ILE   D CG1 
7431  C  CG2 . ILE   D  240 ? 1.9743 0.6141 1.9730 0.0322  -0.6615 0.2198  232 ILE   D CG2 
7432  C  CD1 . ILE   D  240 ? 1.9575 0.7292 1.9930 -0.0453 -0.5882 0.1369  232 ILE   D CD1 
7433  N  N   . LYS   D  241 ? 2.0987 0.6598 1.9400 0.0423  -0.7216 0.2998  233 LYS   D N   
7434  C  CA  . LYS   D  241 ? 2.1828 0.8478 1.8806 0.0186  -0.7535 0.3058  233 LYS   D CA  
7435  C  C   . LYS   D  241 ? 2.1754 0.9264 1.8688 0.0094  -0.7830 0.3175  233 LYS   D C   
7436  O  O   . LYS   D  241 ? 2.1547 1.0977 1.8718 0.0928  -0.8191 0.3700  233 LYS   D O   
7437  C  CB  . LYS   D  241 ? 2.2139 0.9234 1.9437 -0.0405 -0.7098 0.2274  233 LYS   D CB  
7438  C  CG  . LYS   D  241 ? 2.2533 1.0786 1.9238 -0.0583 -0.7551 0.1903  233 LYS   D CG  
7439  C  CD  . LYS   D  241 ? 2.2663 1.2382 1.9955 -0.0994 -0.6981 0.1413  233 LYS   D CD  
7440  C  CE  . LYS   D  241 ? 2.2626 1.2828 2.0137 -0.1388 -0.6786 0.1016  233 LYS   D CE  
7441  N  NZ  . LYS   D  241 ? 2.2972 1.3349 2.0089 -0.1507 -0.7102 0.0899  233 LYS   D NZ  
7442  N  N   . GLU   D  242 ? 2.1630 0.8989 1.8346 0.0062  -0.8199 0.2884  234 GLU   D N   
7443  C  CA  . GLU   D  242 ? 2.1484 1.0114 1.8616 0.0131  -0.8326 0.2531  234 GLU   D CA  
7444  C  C   . GLU   D  242 ? 2.1908 0.9612 1.9106 0.0393  -0.7763 0.2744  234 GLU   D C   
7445  O  O   . GLU   D  242 ? 2.1662 0.8994 1.9093 0.0161  -0.8553 0.3467  234 GLU   D O   
7446  C  CB  . GLU   D  242 ? 2.1522 1.0345 1.8226 0.0118  -0.8589 0.2712  234 GLU   D CB  
7447  C  CG  . GLU   D  242 ? 2.1590 1.1516 1.8527 0.0054  -0.8526 0.2538  234 GLU   D CG  
7448  C  CD  . GLU   D  242 ? 2.2072 1.1580 1.8746 -0.0008 -0.8471 0.2510  234 GLU   D CD  
7449  O  OE1 . GLU   D  242 ? 2.1749 1.2051 1.8955 0.0019  -0.8609 0.2042  234 GLU   D OE1 
7450  O  OE2 . GLU   D  242 ? 2.2405 1.3441 1.9403 -0.0545 -0.7894 0.1782  234 GLU   D OE2 
7451  N  N   . LEU   D  243 ? 2.2232 0.9188 1.8591 0.0747  -0.7542 0.2283  235 LEU   D N   
7452  C  CA  . LEU   D  243 ? 2.2853 0.9083 1.8835 0.1574  -0.6996 0.2346  235 LEU   D CA  
7453  C  C   . LEU   D  243 ? 2.4085 0.9168 1.9065 0.1902  -0.6547 0.2418  235 LEU   D C   
7454  O  O   . LEU   D  243 ? 2.4229 0.9035 1.9361 0.2160  -0.6674 0.2541  235 LEU   D O   
7455  C  CB  . LEU   D  243 ? 2.2575 0.7820 1.8385 0.1981  -0.6696 0.2404  235 LEU   D CB  
7456  C  CG  . LEU   D  243 ? 2.1992 0.7226 1.8676 0.2117  -0.6818 0.2289  235 LEU   D CG  
7457  C  CD1 . LEU   D  243 ? 2.1418 0.7822 1.8849 0.1811  -0.6742 0.2228  235 LEU   D CD1 
7458  C  CD2 . LEU   D  243 ? 2.2043 0.7249 1.8723 0.2066  -0.6798 0.2240  235 LEU   D CD2 
7459  N  N   . LYS   D  244 ? 2.4858 1.0907 1.8794 0.2064  -0.5971 0.2205  236 LYS   D N   
7460  C  CA  . LYS   D  244 ? 2.4993 1.1472 1.8301 0.2234  -0.6202 0.2703  236 LYS   D CA  
7461  C  C   . LYS   D  244 ? 2.5322 1.1892 1.7824 0.1769  -0.6819 0.2269  236 LYS   D C   
7462  O  O   . LYS   D  244 ? 2.4542 1.3044 1.7048 0.2860  -0.7759 0.2601  236 LYS   D O   
7463  C  CB  . LYS   D  244 ? 2.6110 1.3230 1.8225 0.2529  -0.5417 0.2987  236 LYS   D CB  
7464  C  CG  . LYS   D  244 ? 2.6489 1.3706 1.7936 0.2204  -0.5072 0.2961  236 LYS   D CG  
7465  C  CD  . LYS   D  244 ? 2.7130 1.4647 1.8034 0.2811  -0.5306 0.3610  236 LYS   D CD  
7466  C  CE  . LYS   D  244 ? 2.7586 1.4894 1.7650 0.3451  -0.5467 0.3700  236 LYS   D CE  
7467  N  NZ  . LYS   D  244 ? 2.7286 1.5010 1.6879 0.4245  -0.5845 0.3717  236 LYS   D NZ  
7468  N  N   . GLU   D  245 ? 2.4249 1.1612 1.7764 0.2113  -0.6950 0.2367  237 GLU   D N   
7469  C  CA  . GLU   D  245 ? 2.3640 1.1418 1.8284 0.2191  -0.6658 0.2382  237 GLU   D CA  
7470  C  C   . GLU   D  245 ? 2.3849 1.0397 1.8567 0.2445  -0.6401 0.2509  237 GLU   D C   
7471  O  O   . GLU   D  245 ? 2.3906 1.0554 1.9609 0.3255  -0.6076 0.1136  237 GLU   D O   
7472  C  CB  . GLU   D  245 ? 2.2993 1.2267 1.7771 0.1793  -0.6938 0.2115  237 GLU   D CB  
7473  C  CG  . GLU   D  245 ? 2.3008 1.2969 1.7367 0.1155  -0.7182 0.1792  237 GLU   D CG  
7474  C  CD  . GLU   D  245 ? 2.2741 1.3315 1.6735 0.0179  -0.7349 0.1523  237 GLU   D CD  
7475  O  OE1 . GLU   D  245 ? 2.2384 1.3331 1.6482 0.0120  -0.7640 0.1283  237 GLU   D OE1 
7476  O  OE2 . GLU   D  245 ? 2.3112 1.3820 1.6245 -0.0027 -0.7426 0.0981  237 GLU   D OE2 
7477  N  N   . LYS   D  246 ? 2.3648 1.0070 1.8740 0.2044  -0.5337 0.2641  238 LYS   D N   
7478  C  CA  . LYS   D  246 ? 2.3688 1.0183 1.9524 0.2025  -0.4987 0.2911  238 LYS   D CA  
7479  C  C   . LYS   D  246 ? 2.3613 0.9354 1.9029 0.1856  -0.5487 0.3770  238 LYS   D C   
7480  O  O   . LYS   D  246 ? 2.3634 1.0192 1.9238 0.2021  -0.4968 0.5701  238 LYS   D O   
7481  C  CB  . LYS   D  246 ? 2.3369 1.0244 1.9762 0.2212  -0.4572 0.3013  238 LYS   D CB  
7482  C  CG  . LYS   D  246 ? 2.3269 1.0073 2.0215 0.2264  -0.4450 0.3169  238 LYS   D CG  
7483  C  CD  . LYS   D  246 ? 2.3057 1.0150 2.0206 0.2130  -0.4005 0.3222  238 LYS   D CD  
7484  C  CE  . LYS   D  246 ? 2.3220 1.1179 2.0514 0.1389  -0.4017 0.2833  238 LYS   D CE  
7485  N  NZ  . LYS   D  246 ? 2.3125 1.1452 2.0300 0.1118  -0.3912 0.2926  238 LYS   D NZ  
7486  N  N   . GLU   D  247 ? 2.3733 0.9280 1.8215 0.1929  -0.5889 0.3602  239 GLU   D N   
7487  C  CA  . GLU   D  247 ? 2.3927 0.9297 1.7842 0.1816  -0.6565 0.3612  239 GLU   D CA  
7488  C  C   . GLU   D  247 ? 2.4905 0.7841 1.8254 0.1391  -0.6858 0.3174  239 GLU   D C   
7489  O  O   . GLU   D  247 ? 2.5459 0.7159 1.7879 0.1517  -0.7109 0.3559  239 GLU   D O   
7490  C  CB  . GLU   D  247 ? 2.4008 1.0598 1.7592 0.1411  -0.6266 0.2332  239 GLU   D CB  
7491  C  CG  . GLU   D  247 ? 2.4128 1.1341 1.6538 0.1381  -0.6413 0.1863  239 GLU   D CG  
7492  C  CD  . GLU   D  247 ? 2.5033 1.1971 1.6335 0.1199  -0.6198 0.0860  239 GLU   D CD  
7493  O  OE1 . GLU   D  247 ? 2.4481 1.3061 1.6068 0.0925  -0.7098 -0.0197 239 GLU   D OE1 
7494  O  OE2 . GLU   D  247 ? 2.5313 1.1416 1.4256 0.0744  -0.6537 0.0648  239 GLU   D OE2 
7495  N  N   . ALA   D  248 ? 2.4818 0.5632 1.7605 0.1696  -0.7901 0.4080  240 ALA   D N   
7496  C  CA  . ALA   D  248 ? 2.5238 0.5564 1.8062 0.1871  -0.8068 0.4220  240 ALA   D CA  
7497  C  C   . ALA   D  248 ? 2.5456 0.7508 1.9189 0.0902  -0.7411 0.4105  240 ALA   D C   
7498  O  O   . ALA   D  248 ? 2.6075 0.8588 2.1009 0.2792  -0.6924 0.3050  240 ALA   D O   
7499  C  CB  . ALA   D  248 ? 2.4613 0.4721 1.7377 0.2125  -0.8733 0.4536  240 ALA   D CB  
7500  N  N   . ALA   D  249 ? 2.5432 0.6854 1.9364 0.2345  -0.7363 0.5764  241 ALA   D N   
7501  C  CA  . ALA   D  249 ? 2.5369 0.8687 2.0711 0.1637  -0.6726 0.5481  241 ALA   D CA  
7502  C  C   . ALA   D  249 ? 2.6155 0.9731 2.1524 0.0902  -0.5797 0.4714  241 ALA   D C   
7503  O  O   . ALA   D  249 ? 2.6520 1.0288 2.2765 0.0449  -0.5482 0.4828  241 ALA   D O   
7504  C  CB  . ALA   D  249 ? 2.5011 0.8860 2.0866 0.1558  -0.6842 0.4967  241 ALA   D CB  
7505  N  N   . GLU   D  250 ? 2.6515 1.1721 2.1408 -0.0572 -0.4871 0.3784  242 GLU   D N   
7506  C  CA  . GLU   D  250 ? 2.6582 1.4047 2.1122 -0.1199 -0.4108 0.3144  242 GLU   D CA  
7507  C  C   . GLU   D  250 ? 2.6387 1.5261 2.0525 -0.1982 -0.4137 0.3304  242 GLU   D C   
7508  O  O   . GLU   D  250 ? 2.7200 1.5256 2.2356 -0.2305 -0.2583 0.4150  242 GLU   D O   
7509  C  CB  . GLU   D  250 ? 2.6244 1.4221 2.0254 -0.1633 -0.4345 0.2548  242 GLU   D CB  
7510  C  CG  . GLU   D  250 ? 2.6039 1.5513 2.0229 -0.2175 -0.4309 0.2276  242 GLU   D CG  
7511  C  CD  . GLU   D  250 ? 2.5645 1.6557 1.9915 -0.2558 -0.4248 0.1310  242 GLU   D CD  
7512  O  OE1 . GLU   D  250 ? 2.5170 1.7065 1.9641 -0.3055 -0.4697 0.1403  242 GLU   D OE1 
7513  O  OE2 . GLU   D  250 ? 2.5858 1.6628 2.0567 -0.2962 -0.4260 0.1364  242 GLU   D OE2 
7514  N  N   . ASN   E  4   ? 1.8561 0.8356 1.6383 -0.3466 -0.3623 -0.2402 3   ASN   E N   
7515  C  CA  . ASN   E  4   ? 1.9372 0.8879 1.7083 -0.3391 -0.3441 -0.1606 3   ASN   E CA  
7516  C  C   . ASN   E  4   ? 1.9999 0.8013 1.6558 -0.3050 -0.3318 -0.1506 3   ASN   E C   
7517  O  O   . ASN   E  4   ? 2.0500 0.7258 1.6610 -0.3975 -0.3470 -0.1788 3   ASN   E O   
7518  C  CB  . ASN   E  4   ? 1.9867 1.0461 1.6953 -0.3227 -0.3430 -0.2526 3   ASN   E CB  
7519  C  CG  . ASN   E  4   ? 1.9941 1.2157 1.7942 -0.4125 -0.3540 -0.2011 3   ASN   E CG  
7520  O  OD1 . ASN   E  4   ? 1.9528 1.3774 1.9009 -0.3170 -0.4711 -0.1498 3   ASN   E OD1 
7521  N  ND2 . ASN   E  4   ? 2.0761 1.2942 1.7565 -0.4774 -0.3570 -0.2504 3   ASN   E ND2 
7522  N  N   . ASN   E  5   ? 2.0155 0.7961 1.6452 -0.1883 -0.3113 -0.0724 4   ASN   E N   
7523  C  CA  . ASN   E  5   ? 2.0279 0.8700 1.6279 -0.1585 -0.2861 -0.0945 4   ASN   E CA  
7524  C  C   . ASN   E  5   ? 1.9269 0.8597 1.6127 -0.1023 -0.2491 -0.1314 4   ASN   E C   
7525  O  O   . ASN   E  5   ? 1.8597 0.9717 1.6118 -0.1294 -0.2353 -0.1768 4   ASN   E O   
7526  C  CB  . ASN   E  5   ? 2.0620 0.8524 1.5931 -0.1352 -0.2987 -0.1281 4   ASN   E CB  
7527  C  CG  . ASN   E  5   ? 2.1261 0.8766 1.6181 -0.1788 -0.2889 -0.1481 4   ASN   E CG  
7528  O  OD1 . ASN   E  5   ? 2.2053 1.0226 1.6020 -0.1459 -0.3266 -0.3475 4   ASN   E OD1 
7529  N  ND2 . ASN   E  5   ? 2.1532 0.9280 1.6701 -0.1457 -0.2662 -0.1868 4   ASN   E ND2 
7530  N  N   . TYR   E  6   ? 1.9411 0.7708 1.5833 -0.0926 -0.2784 -0.0702 5   TYR   E N   
7531  C  CA  . TYR   E  6   ? 1.9088 0.8201 1.5850 -0.0363 -0.2667 -0.0075 5   TYR   E CA  
7532  C  C   . TYR   E  6   ? 1.8721 0.9035 1.5785 0.0335  -0.3122 -0.0706 5   TYR   E C   
7533  O  O   . TYR   E  6   ? 1.8059 0.8566 1.5675 0.0674  -0.2527 -0.1564 5   TYR   E O   
7534  C  CB  . TYR   E  6   ? 1.8920 0.8306 1.5883 -0.0518 -0.2486 0.0199  5   TYR   E CB  
7535  C  CG  . TYR   E  6   ? 1.8815 0.8137 1.6286 -0.0929 -0.2435 0.0808  5   TYR   E CG  
7536  C  CD1 . TYR   E  6   ? 1.9013 0.8428 1.6664 -0.0341 -0.2431 0.0971  5   TYR   E CD1 
7537  C  CD2 . TYR   E  6   ? 1.8248 0.8829 1.6616 -0.1082 -0.2129 0.0819  5   TYR   E CD2 
7538  C  CE1 . TYR   E  6   ? 1.8710 0.9537 1.6668 -0.0702 -0.2556 0.0954  5   TYR   E CE1 
7539  C  CE2 . TYR   E  6   ? 1.8212 0.9139 1.6368 -0.1159 -0.2249 0.0975  5   TYR   E CE2 
7540  C  CZ  . TYR   E  6   ? 1.8462 0.9170 1.6075 -0.1073 -0.2474 0.0815  5   TYR   E CZ  
7541  O  OH  . TYR   E  6   ? 1.8893 1.0422 1.4365 -0.0895 -0.2833 0.0355  5   TYR   E OH  
7542  N  N   . ASP   E  7   ? 1.8653 0.7775 1.6388 0.0350  -0.3172 0.0167  6   ASP   E N   
7543  C  CA  . ASP   E  7   ? 1.8068 0.7222 1.7574 0.0400  -0.3107 0.0269  6   ASP   E CA  
7544  C  C   . ASP   E  7   ? 1.7892 0.7076 1.7793 0.0034  -0.2870 0.0196  6   ASP   E C   
7545  O  O   . ASP   E  7   ? 1.6848 0.7854 1.9176 -0.0283 -0.2622 -0.0684 6   ASP   E O   
7546  C  CB  . ASP   E  7   ? 1.8727 0.6668 1.8698 0.0707  -0.3156 -0.0079 6   ASP   E CB  
7547  C  CG  . ASP   E  7   ? 1.9542 0.6382 1.9134 0.1531  -0.3750 0.0352  6   ASP   E CG  
7548  O  OD1 . ASP   E  7   ? 1.9387 0.5929 2.0304 0.1799  -0.4098 0.0900  6   ASP   E OD1 
7549  O  OD2 . ASP   E  7   ? 1.9883 0.7206 1.9206 0.2462  -0.3627 -0.0198 6   ASP   E OD2 
7550  N  N   . GLY   E  8   ? 1.7988 0.7028 1.7285 -0.0258 -0.2538 0.0708  7   GLY   E N   
7551  C  CA  . GLY   E  8   ? 1.8309 0.7104 1.6927 -0.0914 -0.2418 0.0757  7   GLY   E CA  
7552  C  C   . GLY   E  8   ? 1.8079 0.7299 1.5597 -0.1278 -0.2327 0.0181  7   GLY   E C   
7553  O  O   . GLY   E  8   ? 1.7691 0.6309 1.5574 -0.1149 -0.1684 0.0125  7   GLY   E O   
7554  N  N   . ASP   E  9   ? 1.8307 0.7506 1.5815 -0.1771 -0.2305 0.0292  8   ASP   E N   
7555  C  CA  . ASP   E  9   ? 1.8096 0.7422 1.6119 -0.1618 -0.2474 0.0052  8   ASP   E CA  
7556  C  C   . ASP   E  9   ? 1.8617 0.6166 1.6293 -0.1766 -0.3280 0.1383  8   ASP   E C   
7557  O  O   . ASP   E  9   ? 1.9030 0.2457 1.5518 -0.1962 -0.4935 0.3442  8   ASP   E O   
7558  C  CB  . ASP   E  9   ? 1.7705 0.9288 1.6340 -0.1838 -0.1817 -0.0562 8   ASP   E CB  
7559  C  CG  . ASP   E  9   ? 1.7214 1.0602 1.6423 -0.1946 -0.1206 -0.1249 8   ASP   E CG  
7560  O  OD1 . ASP   E  9   ? 1.7740 1.1525 1.6477 -0.0931 -0.0613 -0.1367 8   ASP   E OD1 
7561  O  OD2 . ASP   E  9   ? 1.7971 1.2645 1.6773 -0.1982 -0.0325 -0.1312 8   ASP   E OD2 
7562  N  N   . THR   E  10  ? 1.8519 0.6566 1.5588 -0.2272 -0.3079 0.1503  9   THR   E N   
7563  C  CA  . THR   E  10  ? 1.8338 0.7051 1.5804 -0.1956 -0.2720 0.1557  9   THR   E CA  
7564  C  C   . THR   E  10  ? 1.8245 0.5656 1.5564 -0.1097 -0.2287 0.1612  9   THR   E C   
7565  O  O   . THR   E  10  ? 1.8994 0.4993 1.5989 -0.0896 -0.1931 0.3194  9   THR   E O   
7566  C  CB  . THR   E  10  ? 1.7870 0.7344 1.6761 -0.2455 -0.2336 0.2081  9   THR   E CB  
7567  O  OG1 . THR   E  10  ? 1.8244 0.8042 1.6589 -0.2892 -0.1348 0.2471  9   THR   E OG1 
7568  C  CG2 . THR   E  10  ? 1.8022 0.7857 1.6124 -0.2246 -0.2355 0.2200  9   THR   E CG2 
7569  N  N   . VAL   E  11  ? 1.8408 0.4209 1.5560 -0.0328 -0.2051 0.0848  10  VAL   E N   
7570  C  CA  . VAL   E  11  ? 1.7706 0.4102 1.5714 -0.0089 -0.1783 0.0420  10  VAL   E CA  
7571  C  C   . VAL   E  11  ? 1.7934 0.4603 1.5573 -0.0298 -0.1478 0.0137  10  VAL   E C   
7572  O  O   . VAL   E  11  ? 1.7913 0.3627 1.4835 0.0317  -0.1080 -0.0634 10  VAL   E O   
7573  C  CB  . VAL   E  11  ? 1.7548 0.4519 1.5613 -0.0264 -0.1895 0.0087  10  VAL   E CB  
7574  C  CG1 . VAL   E  11  ? 1.7551 0.3967 1.5676 0.0056  -0.1949 0.0321  10  VAL   E CG1 
7575  C  CG2 . VAL   E  11  ? 1.7659 0.5414 1.5594 -0.0143 -0.2068 0.0406  10  VAL   E CG2 
7576  N  N   . THR   E  12  ? 1.8139 0.4173 1.5414 -0.0636 -0.1215 -0.0112 11  THR   E N   
7577  C  CA  . THR   E  12  ? 1.7774 0.4302 1.4719 -0.0871 -0.0835 -0.0034 11  THR   E CA  
7578  C  C   . THR   E  12  ? 1.8158 0.3625 1.4030 -0.1138 -0.0775 -0.0175 11  THR   E C   
7579  O  O   . THR   E  12  ? 1.7454 0.3814 1.4128 -0.1668 0.0144  -0.0556 11  THR   E O   
7580  C  CB  . THR   E  12  ? 1.8136 0.3652 1.5016 -0.1242 -0.1050 -0.0377 11  THR   E CB  
7581  O  OG1 . THR   E  12  ? 1.7685 0.3621 1.5300 -0.1087 -0.1081 -0.0295 11  THR   E OG1 
7582  C  CG2 . THR   E  12  ? 1.8310 0.3914 1.5069 -0.1434 -0.1053 -0.0457 11  THR   E CG2 
7583  N  N   . PHE   E  13  ? 1.6999 0.3257 1.3976 -0.0798 -0.0862 0.0116  12  PHE   E N   
7584  C  CA  . PHE   E  13  ? 1.6529 0.5163 1.3452 -0.0655 -0.1235 -0.0075 12  PHE   E CA  
7585  C  C   . PHE   E  13  ? 1.7184 0.5253 1.4457 -0.0591 -0.0871 0.0261  12  PHE   E C   
7586  O  O   . PHE   E  13  ? 1.7117 0.7031 1.4615 -0.0571 -0.0534 0.0460  12  PHE   E O   
7587  C  CB  . PHE   E  13  ? 1.5792 0.5322 1.3328 -0.0601 -0.1844 -0.0805 12  PHE   E CB  
7588  C  CG  . PHE   E  13  ? 1.5009 0.5415 1.2510 -0.0330 -0.2202 -0.0714 12  PHE   E CG  
7589  C  CD1 . PHE   E  13  ? 1.5034 0.6010 1.2870 -0.0188 -0.2319 -0.0692 12  PHE   E CD1 
7590  C  CD2 . PHE   E  13  ? 1.4452 0.5848 1.1612 -0.0189 -0.2324 -0.0612 12  PHE   E CD2 
7591  C  CE1 . PHE   E  13  ? 1.4915 0.5762 1.2596 0.0213  -0.2532 -0.0400 12  PHE   E CE1 
7592  C  CE2 . PHE   E  13  ? 1.4439 0.5647 1.1539 -0.0066 -0.2444 -0.0644 12  PHE   E CE2 
7593  C  CZ  . PHE   E  13  ? 1.4455 0.5657 1.1920 0.0081  -0.2504 -0.0604 12  PHE   E CZ  
7594  N  N   . SER   E  14  ? 1.6971 0.6336 1.5199 -0.0413 -0.0613 0.0452  13  SER   E N   
7595  C  CA  . SER   E  14  ? 1.7267 0.6435 1.5352 -0.0291 -0.1015 0.0224  13  SER   E CA  
7596  C  C   . SER   E  14  ? 1.7293 0.5965 1.5422 -0.0669 -0.1149 0.0279  13  SER   E C   
7597  O  O   . SER   E  14  ? 1.6197 0.7051 1.5396 -0.0417 -0.1222 0.0851  13  SER   E O   
7598  C  CB  . SER   E  14  ? 1.7302 0.6826 1.5590 0.0015  -0.0899 0.0155  13  SER   E CB  
7599  O  OG  . SER   E  14  ? 1.6552 0.6198 1.5449 0.0669  -0.1129 0.0196  13  SER   E OG  
7600  N  N   . PRO   E  15  ? 1.7816 0.6043 1.5549 -0.0346 -0.1624 -0.0513 14  PRO   E N   
7601  C  CA  . PRO   E  15  ? 1.7857 0.5555 1.5589 -0.0414 -0.1692 -0.0526 14  PRO   E CA  
7602  C  C   . PRO   E  15  ? 1.7468 0.5161 1.5623 -0.0491 -0.1819 -0.0723 14  PRO   E C   
7603  O  O   . PRO   E  15  ? 1.7442 0.5458 1.5789 -0.0099 -0.1848 -0.0382 14  PRO   E O   
7604  C  CB  . PRO   E  15  ? 1.8500 0.5561 1.6197 -0.0480 -0.1743 -0.0578 14  PRO   E CB  
7605  C  CG  . PRO   E  15  ? 1.8459 0.5819 1.6121 -0.0641 -0.1788 -0.0906 14  PRO   E CG  
7606  C  CD  . PRO   E  15  ? 1.8381 0.5162 1.5957 -0.0390 -0.1675 -0.0833 14  PRO   E CD  
7607  N  N   . THR   E  16  ? 1.7478 0.4976 1.5105 -0.0623 -0.1726 -0.1112 15  THR   E N   
7608  C  CA  . THR   E  16  ? 1.7516 0.5696 1.4923 -0.0243 -0.1543 -0.1445 15  THR   E CA  
7609  C  C   . THR   E  16  ? 1.7145 0.5845 1.4904 -0.0377 -0.1410 -0.1057 15  THR   E C   
7610  O  O   . THR   E  16  ? 1.7396 0.7196 1.4529 -0.0047 -0.1063 -0.0859 15  THR   E O   
7611  C  CB  . THR   E  16  ? 1.7878 0.4579 1.4941 -0.0191 -0.1262 -0.2007 15  THR   E CB  
7612  O  OG1 . THR   E  16  ? 1.7616 0.3521 1.5181 -0.0286 -0.1443 -0.2021 15  THR   E OG1 
7613  C  CG2 . THR   E  16  ? 1.8299 0.4723 1.5273 -0.0406 -0.1178 -0.2133 15  THR   E CG2 
7614  N  N   . GLY   E  17  ? 1.6765 0.6507 1.5153 0.0150  -0.1676 -0.0958 16  GLY   E N   
7615  C  CA  . GLY   E  17  ? 1.5915 0.6609 1.5259 -0.0086 -0.2373 -0.0742 16  GLY   E CA  
7616  C  C   . GLY   E  17  ? 1.5391 0.6512 1.5748 0.0044  -0.2394 -0.0783 16  GLY   E C   
7617  O  O   . GLY   E  17  ? 1.3583 0.5806 1.4715 0.0218  -0.3376 -0.2152 16  GLY   E O   
7618  N  N   . ARG   E  18  ? 1.5500 0.7021 1.5908 0.0114  -0.2825 -0.0628 17  ARG   E N   
7619  C  CA  . ARG   E  18  ? 1.5792 0.6794 1.6404 0.0267  -0.3323 -0.0225 17  ARG   E CA  
7620  C  C   . ARG   E  18  ? 1.6302 0.5310 1.6899 0.0812  -0.3680 -0.0294 17  ARG   E C   
7621  O  O   . ARG   E  18  ? 1.5869 0.5563 1.8631 0.1006  -0.4460 -0.0105 17  ARG   E O   
7622  C  CB  . ARG   E  18  ? 1.6484 0.6961 1.7076 0.0461  -0.3265 0.0100  17  ARG   E CB  
7623  C  CG  . ARG   E  18  ? 1.7163 0.7565 1.7132 0.0051  -0.3008 -0.0150 17  ARG   E CG  
7624  C  CD  . ARG   E  18  ? 1.7990 0.7898 1.8183 0.0100  -0.3492 0.0256  17  ARG   E CD  
7625  N  NE  . ARG   E  18  ? 1.8347 0.8621 1.8676 0.0058  -0.3941 0.0195  17  ARG   E NE  
7626  C  CZ  . ARG   E  18  ? 1.8543 0.9499 1.9325 0.0503  -0.4679 0.0380  17  ARG   E CZ  
7627  N  NH1 . ARG   E  18  ? 1.9526 1.0273 1.9979 -0.0182 -0.4599 -0.0714 17  ARG   E NH1 
7628  N  NH2 . ARG   E  18  ? 1.8082 1.0813 2.0492 -0.0128 -0.4623 -0.0039 17  ARG   E NH2 
7629  N  N   . LEU   E  19  ? 1.6711 0.3942 1.6568 0.1227  -0.3421 -0.0242 18  LEU   E N   
7630  C  CA  . LEU   E  19  ? 1.6869 0.4023 1.6802 0.1059  -0.3479 -0.0699 18  LEU   E CA  
7631  C  C   . LEU   E  19  ? 1.7808 0.3459 1.6812 0.1193  -0.3405 -0.0286 18  LEU   E C   
7632  O  O   . LEU   E  19  ? 1.8100 0.1907 1.8097 0.1002  -0.3139 0.0071  18  LEU   E O   
7633  C  CB  . LEU   E  19  ? 1.6039 0.4072 1.6408 0.0832  -0.3124 -0.0846 18  LEU   E CB  
7634  C  CG  . LEU   E  19  ? 1.5543 0.4351 1.5650 0.0860  -0.2928 -0.1368 18  LEU   E CG  
7635  C  CD1 . LEU   E  19  ? 1.5375 0.4536 1.6054 0.0720  -0.2553 -0.1096 18  LEU   E CD1 
7636  C  CD2 . LEU   E  19  ? 1.5544 0.3954 1.5036 0.0628  -0.3153 -0.1558 18  LEU   E CD2 
7637  N  N   . PHE   E  20  ? 1.8626 0.4499 1.6188 0.0636  -0.2711 -0.0367 19  PHE   E N   
7638  C  CA  . PHE   E  20  ? 1.8297 0.5197 1.6138 0.0952  -0.2497 -0.0397 19  PHE   E CA  
7639  C  C   . PHE   E  20  ? 1.8080 0.4384 1.6270 0.0980  -0.1839 -0.0524 19  PHE   E C   
7640  O  O   . PHE   E  20  ? 1.8156 0.4849 1.6105 0.0673  -0.2041 -0.0813 19  PHE   E O   
7641  C  CB  . PHE   E  20  ? 1.8175 0.5050 1.6069 0.0785  -0.2600 -0.1009 19  PHE   E CB  
7642  C  CG  . PHE   E  20  ? 1.7859 0.5056 1.6172 0.1386  -0.2751 -0.1026 19  PHE   E CG  
7643  C  CD1 . PHE   E  20  ? 1.7863 0.5627 1.6373 0.1434  -0.2254 -0.1398 19  PHE   E CD1 
7644  C  CD2 . PHE   E  20  ? 1.7882 0.5307 1.5825 0.1846  -0.2852 -0.1170 19  PHE   E CD2 
7645  C  CE1 . PHE   E  20  ? 1.7737 0.6971 1.5899 0.1450  -0.2276 -0.1997 19  PHE   E CE1 
7646  C  CE2 . PHE   E  20  ? 1.7994 0.5889 1.5594 0.1785  -0.2809 -0.1444 19  PHE   E CE2 
7647  C  CZ  . PHE   E  20  ? 1.7767 0.6761 1.5723 0.1697  -0.2380 -0.1964 19  PHE   E CZ  
7648  N  N   . GLN   E  21  ? 1.8215 0.3860 1.6209 0.0614  -0.1425 -0.0525 20  GLN   E N   
7649  C  CA  . GLN   E  21  ? 1.7913 0.3613 1.6465 0.0541  -0.1690 -0.0405 20  GLN   E CA  
7650  C  C   . GLN   E  21  ? 1.7955 0.3124 1.5873 0.1001  -0.1364 -0.0044 20  GLN   E C   
7651  O  O   . GLN   E  21  ? 1.8100 0.1808 1.7329 0.1399  -0.1925 -0.0650 20  GLN   E O   
7652  C  CB  . GLN   E  21  ? 1.7745 0.3668 1.7040 0.0402  -0.1613 -0.0381 20  GLN   E CB  
7653  C  CG  . GLN   E  21  ? 1.8100 0.3973 1.7166 0.0081  -0.1729 -0.0225 20  GLN   E CG  
7654  C  CD  . GLN   E  21  ? 1.8750 0.3875 1.7324 0.0299  -0.1783 0.0118  20  GLN   E CD  
7655  O  OE1 . GLN   E  21  ? 1.9397 0.3803 1.7628 0.0427  -0.2016 -0.0068 20  GLN   E OE1 
7656  N  NE2 . GLN   E  21  ? 1.9189 0.4158 1.7482 -0.0060 -0.1533 0.0723  20  GLN   E NE2 
7657  N  N   . VAL   E  22  ? 1.7382 0.3631 1.5525 0.1061  -0.1598 -0.0148 21  VAL   E N   
7658  C  CA  . VAL   E  22  ? 1.6842 0.4490 1.5180 0.1146  -0.1735 0.0026  21  VAL   E CA  
7659  C  C   . VAL   E  22  ? 1.6278 0.4213 1.5015 0.0763  -0.2148 0.0616  21  VAL   E C   
7660  O  O   . VAL   E  22  ? 1.6393 0.2350 1.4516 0.0979  -0.2163 0.0600  21  VAL   E O   
7661  C  CB  . VAL   E  22  ? 1.6858 0.5543 1.5026 0.1041  -0.1682 0.0054  21  VAL   E CB  
7662  C  CG1 . VAL   E  22  ? 1.6787 0.5844 1.5414 0.0880  -0.1820 0.0344  21  VAL   E CG1 
7663  C  CG2 . VAL   E  22  ? 1.6927 0.5912 1.4637 0.1228  -0.1574 -0.0220 21  VAL   E CG2 
7664  N  N   . GLU   E  23  ? 1.6467 0.4316 1.5463 0.0164  -0.2405 0.0708  22  GLU   E N   
7665  C  CA  . GLU   E  23  ? 1.6292 0.4794 1.6194 0.0223  -0.2374 0.0597  22  GLU   E CA  
7666  C  C   . GLU   E  23  ? 1.6242 0.4060 1.6291 -0.0117 -0.2554 0.0555  22  GLU   E C   
7667  O  O   . GLU   E  23  ? 1.6403 0.3285 1.6550 -0.0067 -0.2872 0.1091  22  GLU   E O   
7668  C  CB  . GLU   E  23  ? 1.6791 0.5526 1.6031 0.0052  -0.2459 0.0206  22  GLU   E CB  
7669  C  CG  . GLU   E  23  ? 1.6907 0.6783 1.6037 0.0202  -0.2338 0.0441  22  GLU   E CG  
7670  C  CD  . GLU   E  23  ? 1.7519 0.7309 1.6306 0.0014  -0.2365 0.0082  22  GLU   E CD  
7671  O  OE1 . GLU   E  23  ? 1.8164 0.6822 1.6439 0.0293  -0.2761 -0.0437 22  GLU   E OE1 
7672  O  OE2 . GLU   E  23  ? 1.7381 0.9772 1.6142 -0.0498 -0.2041 0.0318  22  GLU   E OE2 
7673  N  N   . TYR   E  24  ? 1.6143 0.4127 1.6375 -0.0022 -0.2523 0.0545  23  TYR   E N   
7674  C  CA  . TYR   E  24  ? 1.6285 0.4749 1.6596 0.0589  -0.2630 0.0776  23  TYR   E CA  
7675  C  C   . TYR   E  24  ? 1.6080 0.5312 1.6528 0.0596  -0.2936 0.0587  23  TYR   E C   
7676  O  O   . TYR   E  24  ? 1.5824 0.6499 1.7085 0.1069  -0.3113 -0.0056 23  TYR   E O   
7677  C  CB  . TYR   E  24  ? 1.6460 0.4183 1.6751 0.0569  -0.2575 0.1050  23  TYR   E CB  
7678  C  CG  . TYR   E  24  ? 1.6804 0.3216 1.6828 0.0878  -0.2349 0.1666  23  TYR   E CG  
7679  C  CD1 . TYR   E  24  ? 1.6942 0.2669 1.6801 0.0678  -0.2247 0.1867  23  TYR   E CD1 
7680  C  CD2 . TYR   E  24  ? 1.6809 0.2418 1.6916 0.1067  -0.2349 0.2116  23  TYR   E CD2 
7681  C  CE1 . TYR   E  24  ? 1.7550 0.2076 1.6959 0.0999  -0.2088 0.1587  23  TYR   E CE1 
7682  C  CE2 . TYR   E  24  ? 1.7048 0.2516 1.6918 0.1012  -0.2315 0.1932  23  TYR   E CE2 
7683  C  CZ  . TYR   E  24  ? 1.7477 0.2462 1.7203 0.0828  -0.2237 0.1562  23  TYR   E CZ  
7684  O  OH  . TYR   E  24  ? 1.7640 0.2918 1.7374 0.0546  -0.2217 0.1318  23  TYR   E OH  
7685  N  N   . ALA   E  25  ? 1.6138 0.5160 1.6448 0.0563  -0.2794 0.0464  24  ALA   E N   
7686  C  CA  . ALA   E  25  ? 1.6423 0.5132 1.6467 0.0568  -0.2695 0.0280  24  ALA   E CA  
7687  C  C   . ALA   E  25  ? 1.6604 0.4678 1.6272 0.0737  -0.2627 0.0103  24  ALA   E C   
7688  O  O   . ALA   E  25  ? 1.6403 0.4678 1.6087 0.0662  -0.2590 0.1030  24  ALA   E O   
7689  C  CB  . ALA   E  25  ? 1.5941 0.5992 1.6647 0.0987  -0.2547 0.0479  24  ALA   E CB  
7690  N  N   . LEU   E  26  ? 1.7672 0.4346 1.6794 0.0609  -0.2637 -0.1012 25  LEU   E N   
7691  C  CA  . LEU   E  26  ? 1.7883 0.4947 1.7330 0.1219  -0.2667 -0.1578 25  LEU   E CA  
7692  C  C   . LEU   E  26  ? 1.8033 0.4895 1.7527 0.1254  -0.3027 -0.1740 25  LEU   E C   
7693  O  O   . LEU   E  26  ? 1.7932 0.3323 1.7524 0.1789  -0.2952 -0.2339 25  LEU   E O   
7694  C  CB  . LEU   E  26  ? 1.8825 0.6038 1.7480 0.1301  -0.2366 -0.2120 25  LEU   E CB  
7695  C  CG  . LEU   E  26  ? 1.9067 0.6542 1.7193 0.1593  -0.2110 -0.2166 25  LEU   E CG  
7696  C  CD1 . LEU   E  26  ? 1.9080 0.6619 1.7580 0.1957  -0.1928 -0.1846 25  LEU   E CD1 
7697  C  CD2 . LEU   E  26  ? 1.9192 0.7854 1.6956 0.1777  -0.2096 -0.2352 25  LEU   E CD2 
7698  N  N   . GLU   E  27  ? 1.8054 0.6355 1.8020 0.0717  -0.2740 -0.1220 26  GLU   E N   
7699  C  CA  . GLU   E  27  ? 1.8298 0.7459 1.8871 0.1430  -0.3016 -0.1129 26  GLU   E CA  
7700  C  C   . GLU   E  27  ? 1.7144 0.7270 1.9325 0.1255  -0.2704 -0.1622 26  GLU   E C   
7701  O  O   . GLU   E  27  ? 1.6831 0.7587 1.9080 0.1242  -0.2907 -0.2409 26  GLU   E O   
7702  C  CB  . GLU   E  27  ? 1.9248 0.7834 1.9398 0.0988  -0.2867 -0.0920 26  GLU   E CB  
7703  C  CG  . GLU   E  27  ? 2.0487 0.7974 1.9670 0.1277  -0.3154 -0.0622 26  GLU   E CG  
7704  C  CD  . GLU   E  27  ? 2.1401 0.9151 1.9082 0.1464  -0.2867 -0.0243 26  GLU   E CD  
7705  O  OE1 . GLU   E  27  ? 2.2325 1.0170 1.8797 0.1748  -0.3900 0.0475  26  GLU   E OE1 
7706  O  OE2 . GLU   E  27  ? 2.2052 1.1292 1.8458 0.1648  -0.1946 0.0112  26  GLU   E OE2 
7707  N  N   . ALA   E  28  ? 1.7503 0.6891 1.8922 0.0603  -0.2510 -0.1718 27  ALA   E N   
7708  C  CA  . ALA   E  28  ? 1.7478 0.6787 1.8502 0.0362  -0.2845 -0.0861 27  ALA   E CA  
7709  C  C   . ALA   E  28  ? 1.7909 0.5796 1.8849 0.0353  -0.2673 -0.0338 27  ALA   E C   
7710  O  O   . ALA   E  28  ? 1.8093 0.4825 1.8451 0.0217  -0.2529 -0.0252 27  ALA   E O   
7711  C  CB  . ALA   E  28  ? 1.7284 0.6304 1.8234 0.0220  -0.2892 -0.0578 27  ALA   E CB  
7712  N  N   . ILE   E  29  ? 1.8030 0.5395 1.8912 0.0632  -0.3226 -0.0160 28  ILE   E N   
7713  C  CA  . ILE   E  29  ? 1.7547 0.6039 1.9020 0.0780  -0.3419 -0.0294 28  ILE   E CA  
7714  C  C   . ILE   E  29  ? 1.7637 0.6380 1.9739 0.1012  -0.3717 -0.0594 28  ILE   E C   
7715  O  O   . ILE   E  29  ? 1.7794 0.3885 2.0437 0.1024  -0.3804 -0.1294 28  ILE   E O   
7716  C  CB  . ILE   E  29  ? 1.7171 0.7146 1.8802 0.0374  -0.3220 -0.0006 28  ILE   E CB  
7717  C  CG1 . ILE   E  29  ? 1.7462 0.6984 1.8915 0.0443  -0.3343 0.0534  28  ILE   E CG1 
7718  C  CG2 . ILE   E  29  ? 1.6928 0.7625 1.8051 0.0590  -0.3128 0.0085  28  ILE   E CG2 
7719  C  CD1 . ILE   E  29  ? 1.7473 0.6536 1.9010 0.0392  -0.3174 0.0713  28  ILE   E CD1 
7720  N  N   . LYS   E  30  ? 1.8852 0.7422 1.9173 0.0429  -0.4015 -0.1138 29  LYS   E N   
7721  C  CA  . LYS   E  30  ? 1.8748 0.8696 1.8962 0.1112  -0.3834 -0.0640 29  LYS   E CA  
7722  C  C   . LYS   E  30  ? 1.8423 0.8183 1.9431 0.0725  -0.4466 -0.0716 29  LYS   E C   
7723  O  O   . LYS   E  30  ? 1.8100 0.8328 1.8627 0.0285  -0.4248 -0.1442 29  LYS   E O   
7724  C  CB  . LYS   E  30  ? 1.9080 1.0083 1.8226 0.0541  -0.3913 -0.0869 29  LYS   E CB  
7725  C  CG  . LYS   E  30  ? 1.9405 1.1032 1.8019 0.0508  -0.3760 -0.0272 29  LYS   E CG  
7726  C  CD  . LYS   E  30  ? 1.9630 1.0987 1.7227 0.0054  -0.3491 -0.0185 29  LYS   E CD  
7727  C  CE  . LYS   E  30  ? 1.9920 1.0516 1.6148 -0.0542 -0.3598 -0.0279 29  LYS   E CE  
7728  N  NZ  . LYS   E  30  ? 2.0327 1.1146 1.5878 -0.1086 -0.3674 -0.0476 29  LYS   E NZ  
7729  N  N   . GLN   E  31  ? 1.8606 0.7961 1.9071 0.0462  -0.4699 0.0257  30  GLN   E N   
7730  C  CA  . GLN   E  31  ? 1.8640 0.7977 1.9586 0.0325  -0.5176 0.0642  30  GLN   E CA  
7731  C  C   . GLN   E  31  ? 1.8365 0.7440 1.9097 0.0694  -0.5278 0.0940  30  GLN   E C   
7732  O  O   . GLN   E  31  ? 1.9175 0.5495 1.8991 0.0139  -0.5452 0.1382  30  GLN   E O   
7733  C  CB  . GLN   E  31  ? 1.8918 0.8208 2.0039 -0.0082 -0.4894 0.0471  30  GLN   E CB  
7734  C  CG  . GLN   E  31  ? 1.9556 0.7731 2.0689 -0.0737 -0.4504 0.0367  30  GLN   E CG  
7735  C  CD  . GLN   E  31  ? 1.9774 0.7157 2.1618 -0.1217 -0.4646 0.0480  30  GLN   E CD  
7736  O  OE1 . GLN   E  31  ? 1.9775 0.5659 2.2188 -0.1460 -0.4913 0.0391  30  GLN   E OE1 
7737  N  NE2 . GLN   E  31  ? 2.0732 0.6391 2.1748 -0.1622 -0.4458 -0.0016 30  GLN   E NE2 
7738  N  N   . GLY   E  32  ? 1.7928 0.7818 1.8458 0.1370  -0.5115 0.1056  31  GLY   E N   
7739  C  CA  . GLY   E  32  ? 1.7253 0.8293 1.7842 0.1654  -0.5243 0.0754  31  GLY   E CA  
7740  C  C   . GLY   E  32  ? 1.7254 0.8835 1.7669 0.2309  -0.5426 0.0898  31  GLY   E C   
7741  O  O   . GLY   E  32  ? 1.7133 0.9249 1.7108 0.2452  -0.5663 0.0986  31  GLY   E O   
7742  N  N   . SER   E  33  ? 1.6574 0.8769 1.7542 0.2717  -0.5149 0.0665  32  SER   E N   
7743  C  CA  . SER   E  33  ? 1.6533 0.8845 1.8016 0.3283  -0.4783 0.0384  32  SER   E CA  
7744  C  C   . SER   E  33  ? 1.6345 0.8836 1.7990 0.3489  -0.4532 0.0232  32  SER   E C   
7745  O  O   . SER   E  33  ? 1.6297 0.8594 1.7800 0.3261  -0.4642 0.0168  32  SER   E O   
7746  C  CB  . SER   E  33  ? 1.5836 0.9089 1.8157 0.3282  -0.4710 0.0272  32  SER   E CB  
7747  O  OG  . SER   E  33  ? 1.5816 0.9371 1.8419 0.3247  -0.4839 0.0163  32  SER   E OG  
7748  N  N   . VAL   E  34  ? 1.6876 0.9530 1.8110 0.3729  -0.4224 0.0125  33  VAL   E N   
7749  C  CA  . VAL   E  34  ? 1.7536 0.9705 1.8165 0.3446  -0.4373 0.0363  33  VAL   E CA  
7750  C  C   . VAL   E  34  ? 1.7451 0.9507 1.8085 0.3680  -0.4176 0.0094  33  VAL   E C   
7751  O  O   . VAL   E  34  ? 1.8078 0.8813 1.7756 0.3684  -0.4236 0.0410  33  VAL   E O   
7752  C  CB  . VAL   E  34  ? 1.7433 1.1563 1.8656 0.3939  -0.4193 0.0508  33  VAL   E CB  
7753  C  CG1 . VAL   E  34  ? 1.7556 1.2327 1.9140 0.3731  -0.4415 0.0492  33  VAL   E CG1 
7754  C  CG2 . VAL   E  34  ? 1.7418 1.2163 1.8693 0.3891  -0.4240 0.0721  33  VAL   E CG2 
7755  N  N   . THR   E  35  ? 1.7193 0.8989 1.8007 0.3587  -0.4019 -0.0114 34  THR   E N   
7756  C  CA  . THR   E  35  ? 1.7003 0.9261 1.8172 0.3202  -0.3439 -0.0456 34  THR   E CA  
7757  C  C   . THR   E  35  ? 1.6850 0.8550 1.8203 0.3254  -0.2886 -0.1102 34  THR   E C   
7758  O  O   . THR   E  35  ? 1.6720 0.8827 1.7658 0.3380  -0.2465 -0.1450 34  THR   E O   
7759  C  CB  . THR   E  35  ? 1.6472 0.9294 1.8381 0.3139  -0.3615 -0.0218 34  THR   E CB  
7760  O  OG1 . THR   E  35  ? 1.6079 0.9375 1.8479 0.3079  -0.3732 -0.0176 34  THR   E OG1 
7761  C  CG2 . THR   E  35  ? 1.6498 0.9103 1.8319 0.3098  -0.3665 0.0064  34  THR   E CG2 
7762  N  N   . VAL   E  36  ? 1.7219 0.8348 1.7759 0.3497  -0.2075 -0.0971 35  VAL   E N   
7763  C  CA  . VAL   E  36  ? 1.7457 0.9054 1.7676 0.3702  -0.1912 -0.1369 35  VAL   E CA  
7764  C  C   . VAL   E  36  ? 1.8154 0.9093 1.7140 0.2942  -0.1897 -0.1377 35  VAL   E C   
7765  O  O   . VAL   E  36  ? 1.8150 0.9142 1.8099 0.2021  -0.2077 -0.1738 35  VAL   E O   
7766  C  CB  . VAL   E  36  ? 1.7557 0.9524 1.8060 0.3993  -0.1835 -0.1239 35  VAL   E CB  
7767  C  CG1 . VAL   E  36  ? 1.7149 0.9216 1.8340 0.4228  -0.1727 -0.0968 35  VAL   E CG1 
7768  C  CG2 . VAL   E  36  ? 1.7788 0.9720 1.8444 0.3873  -0.2034 -0.0937 35  VAL   E CG2 
7769  N  N   . GLY   E  37  ? 1.8444 0.9088 1.7067 0.2718  -0.1818 -0.1303 36  GLY   E N   
7770  C  CA  . GLY   E  37  ? 1.7691 0.8508 1.7277 0.2699  -0.2063 -0.1763 36  GLY   E CA  
7771  C  C   . GLY   E  37  ? 1.6722 0.8073 1.8185 0.2180  -0.1615 -0.0933 36  GLY   E C   
7772  O  O   . GLY   E  37  ? 1.7504 0.9051 1.8115 0.3120  -0.1460 -0.1667 36  GLY   E O   
7773  N  N   . LEU   E  38  ? 1.6516 0.7381 1.8003 0.2286  -0.1762 -0.1456 37  LEU   E N   
7774  C  CA  . LEU   E  38  ? 1.6094 0.8451 1.8336 0.2002  -0.1622 -0.1313 37  LEU   E CA  
7775  C  C   . LEU   E  38  ? 1.5950 0.9028 1.8386 0.1497  -0.1353 -0.0897 37  LEU   E C   
7776  O  O   . LEU   E  38  ? 1.5397 1.1777 1.7740 0.1589  -0.1597 -0.1442 37  LEU   E O   
7777  C  CB  . LEU   E  38  ? 1.6069 0.7755 1.8574 0.1729  -0.1863 -0.0916 37  LEU   E CB  
7778  C  CG  . LEU   E  38  ? 1.6274 0.7773 1.8657 0.1456  -0.1923 -0.0729 37  LEU   E CG  
7779  C  CD1 . LEU   E  38  ? 1.6187 0.8108 1.8995 0.1484  -0.1899 -0.0612 37  LEU   E CD1 
7780  C  CD2 . LEU   E  38  ? 1.6305 0.7351 1.8703 0.1577  -0.1685 -0.0824 37  LEU   E CD2 
7781  N  N   . ARG   E  39  ? 1.6123 0.9181 1.8712 0.1562  -0.1109 -0.0539 38  ARG   E N   
7782  C  CA  . ARG   E  39  ? 1.6078 0.8695 1.8980 0.1974  -0.1043 -0.0769 38  ARG   E CA  
7783  C  C   . ARG   E  39  ? 1.6014 0.8357 1.9558 0.1937  -0.0824 0.0173  38  ARG   E C   
7784  O  O   . ARG   E  39  ? 1.5811 0.7986 1.9262 0.1719  -0.0453 0.0606  38  ARG   E O   
7785  C  CB  . ARG   E  39  ? 1.6283 0.7227 1.8505 0.1800  -0.0893 -0.1209 38  ARG   E CB  
7786  C  CG  . ARG   E  39  ? 1.6900 0.7299 1.8430 0.1559  -0.0772 -0.1559 38  ARG   E CG  
7787  C  CD  . ARG   E  39  ? 1.7125 0.6975 1.7866 0.1693  -0.0820 -0.2276 38  ARG   E CD  
7788  N  NE  . ARG   E  39  ? 1.7446 0.6424 1.7973 0.1512  -0.0967 -0.2546 38  ARG   E NE  
7789  C  CZ  . ARG   E  39  ? 1.7846 0.6218 1.7999 0.1405  -0.0994 -0.2496 38  ARG   E CZ  
7790  N  NH1 . ARG   E  39  ? 1.7976 0.5995 1.8184 0.1430  -0.0929 -0.2219 38  ARG   E NH1 
7791  N  NH2 . ARG   E  39  ? 1.7628 0.6322 1.8285 0.0917  -0.1085 -0.2649 38  ARG   E NH2 
7792  N  N   . SER   E  40  ? 1.6037 0.8248 1.9749 0.2024  -0.0774 -0.0378 39  SER   E N   
7793  C  CA  . SER   E  40  ? 1.6464 0.8874 1.9975 0.2084  -0.0301 -0.0600 39  SER   E CA  
7794  C  C   . SER   E  40  ? 1.5616 0.8443 1.9710 0.1663  -0.0134 -0.0800 39  SER   E C   
7795  O  O   . SER   E  40  ? 1.5501 0.7850 1.9254 0.1746  -0.0333 -0.1826 39  SER   E O   
7796  C  CB  . SER   E  40  ? 1.6397 0.8586 2.0243 0.2405  -0.0390 -0.0598 39  SER   E CB  
7797  O  OG  . SER   E  40  ? 1.6916 0.8058 2.0614 0.2435  0.0075  -0.0239 39  SER   E OG  
7798  N  N   . ASN   E  41  ? 1.6309 0.8632 1.9692 0.1562  -0.0187 -0.0407 40  ASN   E N   
7799  C  CA  . ASN   E  41  ? 1.6013 0.8464 1.9785 0.1048  -0.0284 -0.0061 40  ASN   E CA  
7800  C  C   . ASN   E  41  ? 1.6404 0.6785 2.0826 0.0711  -0.0261 0.0528  40  ASN   E C   
7801  O  O   . ASN   E  41  ? 1.5871 0.7290 2.0499 0.0309  -0.0839 0.1587  40  ASN   E O   
7802  C  CB  . ASN   E  41  ? 1.6084 0.9441 1.9939 0.1083  -0.0464 0.0782  40  ASN   E CB  
7803  C  CG  . ASN   E  41  ? 1.5746 1.1587 1.9528 0.0732  -0.1252 0.0897  40  ASN   E CG  
7804  O  OD1 . ASN   E  41  ? 1.4959 1.2779 2.0451 0.0576  -0.0567 0.1668  40  ASN   E OD1 
7805  N  ND2 . ASN   E  41  ? 1.6253 1.2835 1.9837 0.1563  -0.0962 0.1221  40  ASN   E ND2 
7806  N  N   . THR   E  42  ? 1.6642 0.6564 2.1303 0.1084  -0.0585 0.0245  41  THR   E N   
7807  C  CA  . THR   E  42  ? 1.6563 0.7483 2.1240 0.1206  -0.0267 -0.0332 41  THR   E CA  
7808  C  C   . THR   E  42  ? 1.6598 0.7669 2.1063 0.1458  -0.0358 -0.0094 41  THR   E C   
7809  O  O   . THR   E  42  ? 1.6475 0.8942 2.0796 0.1626  0.0702  -0.0211 41  THR   E O   
7810  C  CB  . THR   E  42  ? 1.6535 0.8152 2.2416 0.1184  -0.0426 -0.0849 41  THR   E CB  
7811  O  OG1 . THR   E  42  ? 1.6392 0.7218 2.2637 0.0700  -0.0210 -0.1223 41  THR   E OG1 
7812  C  CG2 . THR   E  42  ? 1.5967 0.8977 2.2377 0.1143  -0.0280 -0.1116 41  THR   E CG2 
7813  N  N   . HIS   E  43  ? 1.6452 0.7715 1.9908 0.1711  -0.0739 -0.0264 42  HIS   E N   
7814  C  CA  . HIS   E  43  ? 1.6469 0.8536 1.9422 0.1925  -0.1226 -0.0390 42  HIS   E CA  
7815  C  C   . HIS   E  43  ? 1.5795 0.8369 1.9215 0.2281  -0.1152 -0.0019 42  HIS   E C   
7816  O  O   . HIS   E  43  ? 1.6106 1.0153 1.8358 0.2500  -0.1403 -0.0150 42  HIS   E O   
7817  C  CB  . HIS   E  43  ? 1.7452 0.8977 1.9237 0.1432  -0.1976 -0.0401 42  HIS   E CB  
7818  C  CG  . HIS   E  43  ? 1.8103 0.9351 1.8472 0.1001  -0.2019 -0.0554 42  HIS   E CG  
7819  N  ND1 . HIS   E  43  ? 1.8182 0.9730 1.8532 0.0664  -0.2160 -0.0197 42  HIS   E ND1 
7820  C  CD2 . HIS   E  43  ? 1.8503 0.9219 1.8402 0.0949  -0.2288 -0.0479 42  HIS   E CD2 
7821  C  CE1 . HIS   E  43  ? 1.7902 0.9768 1.7969 0.0962  -0.2088 -0.0379 42  HIS   E CE1 
7822  N  NE2 . HIS   E  43  ? 1.8268 0.9159 1.8025 0.1159  -0.2123 -0.0636 42  HIS   E NE2 
7823  N  N   . ALA   E  44  ? 1.5590 0.7353 1.8816 0.2911  -0.1279 -0.0209 43  ALA   E N   
7824  C  CA  . ALA   E  44  ? 1.5185 0.7674 1.8358 0.2796  -0.1606 -0.0106 43  ALA   E CA  
7825  C  C   . ALA   E  44  ? 1.5531 0.6915 1.8507 0.2685  -0.1801 -0.0068 43  ALA   E C   
7826  O  O   . ALA   E  44  ? 1.6179 0.5375 1.8700 0.3564  -0.2015 0.0444  43  ALA   E O   
7827  C  CB  . ALA   E  44  ? 1.5077 0.7355 1.7855 0.2556  -0.1646 -0.0221 43  ALA   E CB  
7828  N  N   . VAL   E  45  ? 1.5428 0.6512 1.9236 0.1661  -0.1818 -0.0593 44  VAL   E N   
7829  C  CA  . VAL   E  45  ? 1.5214 0.5691 1.9137 0.1029  -0.1972 -0.0897 44  VAL   E CA  
7830  C  C   . VAL   E  45  ? 1.5959 0.5502 1.9196 0.0911  -0.1713 -0.0770 44  VAL   E C   
7831  O  O   . VAL   E  45  ? 1.6033 0.7085 1.8598 0.0436  -0.1878 -0.0928 44  VAL   E O   
7832  C  CB  . VAL   E  45  ? 1.4822 0.5461 1.9264 0.0724  -0.2518 -0.0990 44  VAL   E CB  
7833  C  CG1 . VAL   E  45  ? 1.4288 0.4968 1.9370 0.0885  -0.2766 -0.1186 44  VAL   E CG1 
7834  C  CG2 . VAL   E  45  ? 1.4162 0.6873 1.9759 0.0293  -0.2439 -0.0865 44  VAL   E CG2 
7835  N  N   . LEU   E  46  ? 1.6145 0.4570 1.8920 0.0830  -0.1984 -0.1122 45  LEU   E N   
7836  C  CA  . LEU   E  46  ? 1.5945 0.5031 1.8801 0.0893  -0.1737 -0.0964 45  LEU   E CA  
7837  C  C   . LEU   E  46  ? 1.6613 0.6180 1.9515 0.1153  -0.2119 -0.0487 45  LEU   E C   
7838  O  O   . LEU   E  46  ? 1.6717 0.5729 2.0054 0.1025  -0.2345 -0.0143 45  LEU   E O   
7839  C  CB  . LEU   E  46  ? 1.5722 0.4203 1.8319 0.0805  -0.2017 -0.1062 45  LEU   E CB  
7840  C  CG  . LEU   E  46  ? 1.5554 0.4109 1.8027 0.0707  -0.1775 -0.0906 45  LEU   E CG  
7841  C  CD1 . LEU   E  46  ? 1.5449 0.4545 1.7665 0.0425  -0.1784 -0.0993 45  LEU   E CD1 
7842  C  CD2 . LEU   E  46  ? 1.5363 0.4257 1.7999 0.0713  -0.1619 -0.1000 45  LEU   E CD2 
7843  N  N   . VAL   E  47  ? 1.7019 0.6169 2.0329 0.1309  -0.1769 -0.0524 46  VAL   E N   
7844  C  CA  . VAL   E  47  ? 1.7019 0.5787 2.0816 0.1098  -0.1777 -0.0272 46  VAL   E CA  
7845  C  C   . VAL   E  47  ? 1.6923 0.5479 2.0220 0.1298  -0.1754 -0.0303 46  VAL   E C   
7846  O  O   . VAL   E  47  ? 1.5808 0.5709 2.0393 0.0869  -0.1610 0.0220  46  VAL   E O   
7847  C  CB  . VAL   E  47  ? 1.7077 0.6386 2.1687 0.1562  -0.1842 0.0016  46  VAL   E CB  
7848  C  CG1 . VAL   E  47  ? 1.7450 0.6680 2.2058 0.1472  -0.2214 0.0230  46  VAL   E CG1 
7849  C  CG2 . VAL   E  47  ? 1.6957 0.6668 2.2077 0.1258  -0.1811 -0.0108 46  VAL   E CG2 
7850  N  N   . ALA   E  48  ? 1.7133 0.4893 2.0065 0.0926  -0.2068 -0.0564 47  ALA   E N   
7851  C  CA  . ALA   E  48  ? 1.7472 0.5137 2.0197 0.0509  -0.2113 -0.0745 47  ALA   E CA  
7852  C  C   . ALA   E  48  ? 1.7707 0.6218 2.0180 0.0495  -0.2791 -0.0874 47  ALA   E C   
7853  O  O   . ALA   E  48  ? 1.8709 0.3321 2.1413 -0.0394 -0.2463 -0.1298 47  ALA   E O   
7854  C  CB  . ALA   E  48  ? 1.7834 0.4122 2.0082 0.0490  -0.2350 -0.0820 47  ALA   E CB  
7855  N  N   . LEU   E  49  ? 1.8039 0.6330 2.0207 0.0301  -0.2474 -0.0930 48  LEU   E N   
7856  C  CA  . LEU   E  49  ? 1.8576 0.7765 1.9759 0.0215  -0.2766 -0.0645 48  LEU   E CA  
7857  C  C   . LEU   E  49  ? 1.9025 0.6955 1.9261 0.0206  -0.2784 -0.0566 48  LEU   E C   
7858  O  O   . LEU   E  49  ? 1.9721 0.4142 1.8022 -0.0474 -0.2981 -0.1028 48  LEU   E O   
7859  C  CB  . LEU   E  49  ? 1.9007 0.8107 1.9934 -0.0071 -0.2815 -0.1059 48  LEU   E CB  
7860  C  CG  . LEU   E  49  ? 1.9500 1.0435 1.9246 -0.0150 -0.3347 -0.0467 48  LEU   E CG  
7861  C  CD1 . LEU   E  49  ? 1.9620 1.1613 1.9565 -0.0474 -0.3566 -0.0715 48  LEU   E CD1 
7862  C  CD2 . LEU   E  49  ? 1.9868 1.0915 1.9410 -0.0353 -0.3367 -0.1033 48  LEU   E CD2 
7863  N  N   . LYS   E  50  ? 1.9204 0.7980 1.9055 0.0775  -0.3093 -0.0303 49  LYS   E N   
7864  C  CA  . LYS   E  50  ? 1.8915 0.8058 1.9536 0.1245  -0.3066 -0.0415 49  LYS   E CA  
7865  C  C   . LYS   E  50  ? 1.8863 0.7674 2.0354 0.1679  -0.2630 -0.0499 49  LYS   E C   
7866  O  O   . LYS   E  50  ? 2.0130 0.7445 2.2273 0.2405  -0.3026 -0.1437 49  LYS   E O   
7867  C  CB  . LYS   E  50  ? 1.8494 0.7552 1.9141 0.1572  -0.3460 0.0056  49  LYS   E CB  
7868  C  CG  . LYS   E  50  ? 1.7808 0.7727 1.8892 0.1878  -0.3689 0.0155  49  LYS   E CG  
7869  C  CD  . LYS   E  50  ? 1.7757 0.7791 1.8465 0.1921  -0.3902 0.0377  49  LYS   E CD  
7870  C  CE  . LYS   E  50  ? 1.7700 0.8129 1.8522 0.2001  -0.4057 0.0356  49  LYS   E CE  
7871  N  NZ  . LYS   E  50  ? 1.7107 0.9065 1.8233 0.1327  -0.4475 0.0277  49  LYS   E NZ  
7872  N  N   . ARG   E  51  ? 1.9111 0.8590 2.0158 0.1525  -0.2280 -0.0741 50  ARG   E N   
7873  C  CA  . ARG   E  51  ? 1.9295 0.9220 1.9520 0.1291  -0.1967 -0.0484 50  ARG   E CA  
7874  C  C   . ARG   E  51  ? 1.9811 0.8775 1.9385 0.1221  -0.2245 -0.0591 50  ARG   E C   
7875  O  O   . ARG   E  51  ? 2.0282 0.8848 1.8604 0.1508  -0.2247 -0.0085 50  ARG   E O   
7876  C  CB  . ARG   E  51  ? 1.9528 1.0545 1.9264 0.0542  -0.1695 -0.0556 50  ARG   E CB  
7877  C  CG  . ARG   E  51  ? 2.0018 1.1336 1.9249 -0.0359 -0.1318 -0.0561 50  ARG   E CG  
7878  C  CD  . ARG   E  51  ? 2.0317 1.2134 1.8848 -0.0651 -0.1018 -0.1079 50  ARG   E CD  
7879  N  NE  . ARG   E  51  ? 2.0656 1.2184 1.9465 -0.0682 -0.0342 -0.1324 50  ARG   E NE  
7880  C  CZ  . ARG   E  51  ? 2.0727 1.1524 1.9859 -0.1367 -0.0284 -0.1223 50  ARG   E CZ  
7881  N  NH1 . ARG   E  51  ? 2.0842 1.0876 1.9642 -0.1306 0.0551  -0.1592 50  ARG   E NH1 
7882  N  NH2 . ARG   E  51  ? 2.0650 1.0862 2.0061 -0.1587 -0.0104 -0.1105 50  ARG   E NH2 
7883  N  N   . ASN   E  52  ? 1.9656 0.8526 1.9962 0.1452  -0.2678 -0.0833 51  ASN   E N   
7884  C  CA  . ASN   E  52  ? 1.9281 0.8827 1.9799 0.1298  -0.3193 -0.0869 51  ASN   E CA  
7885  C  C   . ASN   E  52  ? 1.9834 0.9504 1.9872 0.1161  -0.2507 -0.0357 51  ASN   E C   
7886  O  O   . ASN   E  52  ? 1.9620 1.0366 2.0006 0.0294  -0.2767 -0.0563 51  ASN   E O   
7887  C  CB  . ASN   E  52  ? 1.9527 0.8734 1.9969 0.1323  -0.3570 -0.0995 51  ASN   E CB  
7888  C  CG  . ASN   E  52  ? 1.9311 0.9087 2.0277 0.1642  -0.4102 -0.0963 51  ASN   E CG  
7889  O  OD1 . ASN   E  52  ? 1.9656 0.9696 2.0326 0.2259  -0.4350 -0.1264 51  ASN   E OD1 
7890  N  ND2 . ASN   E  52  ? 1.9194 0.8428 1.9906 0.1711  -0.4090 -0.1705 51  ASN   E ND2 
7891  N  N   . ALA   E  53  ? 2.0530 0.9063 1.9403 0.0956  -0.2791 -0.0806 52  ALA   E N   
7892  C  CA  . ALA   E  53  ? 2.0905 0.8596 1.9023 0.1046  -0.2755 -0.0970 52  ALA   E CA  
7893  C  C   . ALA   E  53  ? 2.1354 0.7588 1.9466 0.1208  -0.2553 -0.1259 52  ALA   E C   
7894  O  O   . ALA   E  53  ? 2.2036 0.7597 1.9696 0.0663  -0.2790 -0.0342 52  ALA   E O   
7895  C  CB  . ALA   E  53  ? 2.0871 0.8991 1.8442 0.0726  -0.2668 -0.0800 52  ALA   E CB  
7896  N  N   . ASP   E  54  ? 2.0988 0.6686 2.0280 0.1411  -0.2299 -0.1955 53  ASP   E N   
7897  C  CA  . ASP   E  54  ? 2.1042 0.6481 2.1496 0.1827  -0.2009 -0.2074 53  ASP   E CA  
7898  C  C   . ASP   E  54  ? 2.0544 0.7298 2.2444 0.2022  -0.2193 -0.2365 53  ASP   E C   
7899  O  O   . ASP   E  54  ? 2.0180 0.8959 2.2035 0.2062  -0.2303 -0.0808 53  ASP   E O   
7900  C  CB  . ASP   E  54  ? 2.1289 0.6624 2.1632 0.1589  -0.1570 -0.2284 53  ASP   E CB  
7901  C  CG  . ASP   E  54  ? 2.1667 0.5713 2.1638 0.0917  -0.1074 -0.2025 53  ASP   E CG  
7902  O  OD1 . ASP   E  54  ? 2.1815 0.6688 2.2201 -0.0228 -0.1010 -0.2595 53  ASP   E OD1 
7903  O  OD2 . ASP   E  54  ? 2.2410 0.4563 2.1374 0.0569  -0.0963 -0.2298 53  ASP   E OD2 
7904  N  N   . GLU   E  55  ? 2.1495 0.7178 2.3145 0.2701  -0.2331 -0.1792 54  GLU   E N   
7905  C  CA  . GLU   E  55  ? 2.1162 0.8905 2.2992 0.2868  -0.2876 -0.1389 54  GLU   E CA  
7906  C  C   . GLU   E  55  ? 2.0764 0.9558 2.2228 0.2188  -0.3314 -0.1551 54  GLU   E C   
7907  O  O   . GLU   E  55  ? 2.1533 0.9548 2.2236 0.1984  -0.4181 -0.2648 54  GLU   E O   
7908  C  CB  . GLU   E  55  ? 2.1613 1.0136 2.3085 0.3440  -0.3062 -0.1029 54  GLU   E CB  
7909  C  CG  . GLU   E  55  ? 2.1690 1.1284 2.3997 0.3892  -0.2696 -0.0852 54  GLU   E CG  
7910  C  CD  . GLU   E  55  ? 2.2392 1.1598 2.3772 0.4644  -0.1972 -0.0777 54  GLU   E CD  
7911  O  OE1 . GLU   E  55  ? 2.1924 1.1825 2.4545 0.4743  -0.1545 -0.0513 54  GLU   E OE1 
7912  O  OE2 . GLU   E  55  ? 2.3329 1.0524 2.4815 0.5054  -0.0899 -0.1134 54  GLU   E OE2 
7913  N  N   . LEU   E  56  ? 2.1222 0.9920 2.1518 0.2572  -0.3114 -0.0867 55  LEU   E N   
7914  C  CA  . LEU   E  56  ? 2.1237 0.8482 2.0912 0.2279  -0.3603 -0.0055 55  LEU   E CA  
7915  C  C   . LEU   E  56  ? 2.1261 0.7505 2.1446 0.1327  -0.3837 0.0228  55  LEU   E C   
7916  O  O   . LEU   E  56  ? 2.0499 0.6646 2.1264 0.0818  -0.4147 0.1093  55  LEU   E O   
7917  C  CB  . LEU   E  56  ? 2.1661 0.9004 2.0231 0.2794  -0.3730 0.0320  55  LEU   E CB  
7918  C  CG  . LEU   E  56  ? 2.1365 0.8976 2.0496 0.3403  -0.3713 0.0481  55  LEU   E CG  
7919  C  CD1 . LEU   E  56  ? 2.1425 0.8834 2.0524 0.3709  -0.3881 0.0620  55  LEU   E CD1 
7920  C  CD2 . LEU   E  56  ? 2.1830 0.9219 2.0355 0.3360  -0.3762 0.0717  55  LEU   E CD2 
7921  N  N   . SER   E  57  ? 2.1484 0.5022 2.1370 0.1742  -0.4002 0.0647  56  SER   E N   
7922  C  CA  . SER   E  57  ? 2.1064 0.5349 2.0815 0.1492  -0.4116 0.0569  56  SER   E CA  
7923  C  C   . SER   E  57  ? 2.0060 0.7251 2.0589 0.0883  -0.3743 0.0101  56  SER   E C   
7924  O  O   . SER   E  57  ? 1.9190 0.8734 2.0422 -0.0080 -0.3838 -0.1000 56  SER   E O   
7925  C  CB  . SER   E  57  ? 2.1385 0.2885 2.1042 0.1951  -0.4000 0.0203  56  SER   E CB  
7926  O  OG  . SER   E  57  ? 2.1189 0.2887 2.2026 0.2298  -0.4151 -0.0141 56  SER   E OG  
7927  N  N   . SER   E  58  ? 2.0627 0.6795 1.9411 0.0235  -0.3459 0.0604  57  SER   E N   
7928  C  CA  . SER   E  58  ? 2.0260 0.7129 1.8610 0.0804  -0.3611 0.0656  57  SER   E CA  
7929  C  C   . SER   E  58  ? 2.0120 0.7954 1.7877 0.0624  -0.3429 0.1176  57  SER   E C   
7930  O  O   . SER   E  58  ? 2.0342 0.8018 1.5732 0.0477  -0.3604 0.1753  57  SER   E O   
7931  C  CB  . SER   E  58  ? 2.0298 0.7195 1.8391 0.0915  -0.3570 0.0752  57  SER   E CB  
7932  O  OG  . SER   E  58  ? 2.0361 0.6301 1.8359 0.0957  -0.4091 0.0445  57  SER   E OG  
7933  N  N   . TYR   E  59  ? 1.9312 0.8603 1.8412 0.0625  -0.3093 0.1341  58  TYR   E N   
7934  C  CA  . TYR   E  59  ? 1.8433 0.8652 1.8722 0.1333  -0.3557 0.1101  58  TYR   E CA  
7935  C  C   . TYR   E  59  ? 1.7621 0.7969 1.9683 0.1210  -0.3441 0.0923  58  TYR   E C   
7936  O  O   . TYR   E  59  ? 1.7473 0.7372 2.0324 0.2003  -0.3831 0.0547  58  TYR   E O   
7937  C  CB  . TYR   E  59  ? 1.8558 0.8893 1.8853 0.1987  -0.3435 0.1127  58  TYR   E CB  
7938  C  CG  . TYR   E  59  ? 1.8834 0.8740 1.8459 0.2150  -0.3337 0.0979  58  TYR   E CG  
7939  C  CD1 . TYR   E  59  ? 1.8863 0.8350 1.8388 0.2491  -0.3301 0.1408  58  TYR   E CD1 
7940  C  CD2 . TYR   E  59  ? 1.8892 0.9037 1.8203 0.3149  -0.2947 0.0945  58  TYR   E CD2 
7941  C  CE1 . TYR   E  59  ? 1.8852 0.9299 1.8097 0.3240  -0.3331 0.1207  58  TYR   E CE1 
7942  C  CE2 . TYR   E  59  ? 1.8710 1.0091 1.8072 0.3872  -0.2908 0.0933  58  TYR   E CE2 
7943  C  CZ  . TYR   E  59  ? 1.9005 1.0138 1.8049 0.3898  -0.2991 0.0767  58  TYR   E CZ  
7944  O  OH  . TYR   E  59  ? 2.0138 1.0390 1.8401 0.4613  -0.2772 0.0655  58  TYR   E OH  
7945  N  N   . GLN   E  60  ? 1.6806 0.8905 1.9706 0.1875  -0.3729 0.1212  59  GLN   E N   
7946  C  CA  . GLN   E  60  ? 1.6594 0.9955 1.9469 0.1958  -0.3681 0.1275  59  GLN   E CA  
7947  C  C   . GLN   E  60  ? 1.5671 1.0809 1.9086 0.1880  -0.3585 0.1107  59  GLN   E C   
7948  O  O   . GLN   E  60  ? 1.5719 1.1303 1.8614 0.1934  -0.3514 0.1428  59  GLN   E O   
7949  C  CB  . GLN   E  60  ? 1.7196 1.0199 1.9840 0.1734  -0.3824 0.1131  59  GLN   E CB  
7950  C  CG  . GLN   E  60  ? 1.7504 1.0887 2.0025 0.1727  -0.4326 0.1039  59  GLN   E CG  
7951  C  CD  . GLN   E  60  ? 1.8825 1.1167 1.9775 0.1511  -0.3967 0.0665  59  GLN   E CD  
7952  O  OE1 . GLN   E  60  ? 1.9956 1.0593 2.0083 0.1380  -0.4772 0.0994  59  GLN   E OE1 
7953  N  NE2 . GLN   E  60  ? 1.8882 1.1700 1.9542 0.1573  -0.3988 0.0245  59  GLN   E NE2 
7954  N  N   . LYS   E  61  ? 1.4861 1.0904 1.9102 0.2029  -0.3571 0.1055  60  LYS   E N   
7955  C  CA  . LYS   E  61  ? 1.4618 1.0789 1.9390 0.2385  -0.3250 0.1147  60  LYS   E CA  
7956  C  C   . LYS   E  61  ? 1.4992 1.0721 1.8718 0.2670  -0.2885 0.1282  60  LYS   E C   
7957  O  O   . LYS   E  61  ? 1.4931 1.1742 1.8989 0.2941  -0.3109 0.2321  60  LYS   E O   
7958  C  CB  . LYS   E  61  ? 1.4489 1.0656 2.0015 0.2536  -0.2670 0.1296  60  LYS   E CB  
7959  C  CG  . LYS   E  61  ? 1.4826 1.1150 2.0426 0.2461  -0.2141 0.1342  60  LYS   E CG  
7960  C  CD  . LYS   E  61  ? 1.4993 1.1645 2.1120 0.1947  -0.1849 0.0931  60  LYS   E CD  
7961  C  CE  . LYS   E  61  ? 1.4669 1.2016 2.1455 0.1915  -0.1785 0.1186  60  LYS   E CE  
7962  N  NZ  . LYS   E  61  ? 1.4667 1.1772 2.1685 0.2023  -0.1856 0.1172  60  LYS   E NZ  
7963  N  N   . LYS   E  62  ? 1.5278 1.0217 1.8449 0.2593  -0.3044 0.0747  61  LYS   E N   
7964  C  CA  . LYS   E  62  ? 1.5447 0.9792 1.8673 0.2071  -0.3286 0.0728  61  LYS   E CA  
7965  C  C   . LYS   E  62  ? 1.4198 0.8563 1.8141 0.1376  -0.3132 -0.0072 61  LYS   E C   
7966  O  O   . LYS   E  62  ? 1.3774 0.7683 1.8331 0.1279  -0.3145 0.0854  61  LYS   E O   
7967  C  CB  . LYS   E  62  ? 1.6363 1.0031 1.9098 0.1822  -0.3570 -0.0531 61  LYS   E CB  
7968  C  CG  . LYS   E  62  ? 1.7520 0.9971 1.9118 0.1678  -0.4003 -0.0734 61  LYS   E CG  
7969  C  CD  . LYS   E  62  ? 1.7483 1.0906 1.9163 0.1495  -0.4210 -0.1478 61  LYS   E CD  
7970  C  CE  . LYS   E  62  ? 1.7670 1.0465 1.9702 0.1950  -0.4131 -0.1773 61  LYS   E CE  
7971  N  NZ  . LYS   E  62  ? 1.7998 0.9193 1.9562 0.2246  -0.4202 -0.2062 61  LYS   E NZ  
7972  N  N   . ILE   E  63  ? 1.4644 0.7678 1.6713 0.1782  -0.2860 -0.0144 62  ILE   E N   
7973  C  CA  . ILE   E  63  ? 1.4408 0.7649 1.6185 0.1488  -0.2715 -0.0393 62  ILE   E CA  
7974  C  C   . ILE   E  63  ? 1.4571 0.7509 1.5815 0.1060  -0.2557 -0.0552 62  ILE   E C   
7975  O  O   . ILE   E  63  ? 1.4884 0.7434 1.5756 0.1239  -0.3205 0.0250  62  ILE   E O   
7976  C  CB  . ILE   E  63  ? 1.4415 0.7261 1.6248 0.1526  -0.2645 -0.0397 62  ILE   E CB  
7977  C  CG1 . ILE   E  63  ? 1.4595 0.7018 1.6777 0.1932  -0.2619 -0.0061 62  ILE   E CG1 
7978  C  CG2 . ILE   E  63  ? 1.4163 0.7095 1.6178 0.1298  -0.2600 -0.0617 62  ILE   E CG2 
7979  C  CD1 . ILE   E  63  ? 1.4580 0.7020 1.7209 0.2053  -0.2739 0.0025  62  ILE   E CD1 
7980  N  N   . ILE   E  64  ? 1.4348 0.7115 1.5390 0.0854  -0.2347 -0.0747 63  ILE   E N   
7981  C  CA  . ILE   E  64  ? 1.4663 0.7377 1.5571 0.0752  -0.1881 -0.1124 63  ILE   E CA  
7982  C  C   . ILE   E  64  ? 1.4512 0.7835 1.5827 0.0622  -0.1779 -0.0873 63  ILE   E C   
7983  O  O   . ILE   E  64  ? 1.4352 0.8031 1.6137 0.0240  -0.1690 -0.1659 63  ILE   E O   
7984  C  CB  . ILE   E  64  ? 1.4880 0.7116 1.5093 0.0483  -0.1524 -0.1277 63  ILE   E CB  
7985  C  CG1 . ILE   E  64  ? 1.5213 0.6739 1.5453 0.0445  -0.1432 -0.1514 63  ILE   E CG1 
7986  C  CG2 . ILE   E  64  ? 1.5043 0.7165 1.4721 0.0704  -0.1324 -0.0844 63  ILE   E CG2 
7987  C  CD1 . ILE   E  64  ? 1.5151 0.7354 1.5653 0.0521  -0.1424 -0.1762 63  ILE   E CD1 
7988  N  N   . LYS   E  65  ? 1.4801 0.7682 1.6679 0.0782  -0.1653 -0.0957 64  LYS   E N   
7989  C  CA  . LYS   E  65  ? 1.5536 0.7256 1.7099 0.0284  -0.1509 -0.1234 64  LYS   E CA  
7990  C  C   . LYS   E  65  ? 1.6332 0.6804 1.7446 0.0492  -0.2147 -0.0432 64  LYS   E C   
7991  O  O   . LYS   E  65  ? 1.7355 0.6785 1.7058 0.0216  -0.2005 -0.0329 64  LYS   E O   
7992  C  CB  . LYS   E  65  ? 1.5041 0.7873 1.7273 0.0006  -0.1376 -0.1281 64  LYS   E CB  
7993  C  CG  . LYS   E  65  ? 1.4898 0.8904 1.7078 -0.0129 -0.1154 -0.0631 64  LYS   E CG  
7994  C  CD  . LYS   E  65  ? 1.4607 0.9371 1.7188 -0.0053 -0.1126 -0.0917 64  LYS   E CD  
7995  C  CE  . LYS   E  65  ? 1.4000 0.8652 1.7165 0.0141  -0.0951 -0.1645 64  LYS   E CE  
7996  N  NZ  . LYS   E  65  ? 1.3875 0.8713 1.7174 0.0492  -0.1031 -0.1828 64  LYS   E NZ  
7997  N  N   . CYS   E  66  ? 1.7621 0.6992 1.7499 0.0024  -0.2001 -0.0054 65  CYS   E N   
7998  C  CA  . CYS   E  66  ? 1.7617 0.8668 1.7556 -0.0076 -0.2606 -0.0410 65  CYS   E CA  
7999  C  C   . CYS   E  66  ? 1.8396 0.8788 1.7508 0.0026  -0.2714 -0.0550 65  CYS   E C   
8000  O  O   . CYS   E  66  ? 1.7295 1.2404 1.6111 0.0245  -0.2657 -0.0964 65  CYS   E O   
8001  C  CB  . CYS   E  66  ? 1.7446 0.6802 1.8191 -0.0639 -0.2652 -0.0330 65  CYS   E CB  
8002  S  SG  . CYS   E  66  ? 1.7011 0.6030 1.9352 0.0454  -0.2402 -0.0505 65  CYS   E SG  
8003  N  N   . ASP   E  67  ? 1.8052 0.8848 1.7597 0.0376  -0.2647 -0.0926 66  ASP   E N   
8004  C  CA  . ASP   E  67  ? 1.8118 0.8480 1.7744 0.0726  -0.2916 -0.0956 66  ASP   E CA  
8005  C  C   . ASP   E  67  ? 1.8014 0.7035 1.7215 0.0668  -0.2481 -0.0396 66  ASP   E C   
8006  O  O   . ASP   E  67  ? 1.6729 0.7881 1.6705 0.0850  -0.3017 -0.0831 66  ASP   E O   
8007  C  CB  . ASP   E  67  ? 1.8679 0.8950 1.8201 0.1010  -0.3540 -0.1126 66  ASP   E CB  
8008  C  CG  . ASP   E  67  ? 1.9595 0.9360 1.9452 0.1511  -0.3851 -0.2832 66  ASP   E CG  
8009  O  OD1 . ASP   E  67  ? 1.9495 1.0843 1.9910 0.2363  -0.4724 -0.3473 66  ASP   E OD1 
8010  O  OD2 . ASP   E  67  ? 2.0722 1.1302 1.9985 0.2374  -0.4523 -0.3089 66  ASP   E OD2 
8011  N  N   . GLU   E  68  ? 1.7942 0.7606 1.7437 0.0557  -0.1730 0.0203  67  GLU   E N   
8012  C  CA  . GLU   E  68  ? 1.7977 0.8067 1.7734 0.0797  -0.1321 0.0339  67  GLU   E CA  
8013  C  C   . GLU   E  68  ? 1.7535 0.6068 1.8401 0.1348  -0.1314 0.0701  67  GLU   E C   
8014  O  O   . GLU   E  68  ? 1.8029 0.4046 1.7929 0.2253  -0.1237 0.1582  67  GLU   E O   
8015  C  CB  . GLU   E  68  ? 1.8783 0.8545 1.8583 -0.0331 -0.1259 0.0394  67  GLU   E CB  
8016  C  CG  . GLU   E  68  ? 1.9470 0.9527 1.7837 -0.0439 -0.1432 0.0619  67  GLU   E CG  
8017  C  CD  . GLU   E  68  ? 2.0388 1.0346 1.8229 -0.0461 -0.1746 0.1256  67  GLU   E CD  
8018  O  OE1 . GLU   E  68  ? 2.0227 1.1278 1.7995 -0.0565 -0.2498 0.2275  67  GLU   E OE1 
8019  O  OE2 . GLU   E  68  ? 2.1475 1.0822 1.8092 0.0040  -0.1465 0.1461  67  GLU   E OE2 
8020  N  N   . HIS   E  69  ? 1.6323 0.5748 1.9214 0.1379  -0.1189 0.0412  68  HIS   E N   
8021  C  CA  . HIS   E  69  ? 1.5465 0.6337 1.9270 0.1368  -0.1212 0.0359  68  HIS   E CA  
8022  C  C   . HIS   E  69  ? 1.5054 0.6471 1.8873 0.1305  -0.1011 0.0246  68  HIS   E C   
8023  O  O   . HIS   E  69  ? 1.4933 0.5639 1.9287 0.1205  -0.0893 -0.0046 68  HIS   E O   
8024  C  CB  . HIS   E  69  ? 1.4890 0.7024 1.9332 0.1654  -0.1236 0.0533  68  HIS   E CB  
8025  C  CG  . HIS   E  69  ? 1.4909 0.6414 1.9460 0.1925  -0.1369 0.0795  68  HIS   E CG  
8026  N  ND1 . HIS   E  69  ? 1.4647 0.5021 1.9878 0.1524  -0.1204 0.0950  68  HIS   E ND1 
8027  C  CD2 . HIS   E  69  ? 1.4983 0.6730 1.9544 0.2241  -0.1396 0.0932  68  HIS   E CD2 
8028  C  CE1 . HIS   E  69  ? 1.4654 0.4089 1.9832 0.1477  -0.1424 0.0915  68  HIS   E CE1 
8029  N  NE2 . HIS   E  69  ? 1.5102 0.5243 1.9619 0.1963  -0.1308 0.0831  68  HIS   E NE2 
8030  N  N   . MET   E  70  ? 1.4602 0.6881 1.8534 0.1047  -0.1321 0.0054  69  MET   E N   
8031  C  CA  . MET   E  70  ? 1.4198 0.6468 1.7657 0.1580  -0.1893 -0.0094 69  MET   E CA  
8032  C  C   . MET   E  70  ? 1.4296 0.5032 1.8044 0.1798  -0.2346 -0.0072 69  MET   E C   
8033  O  O   . MET   E  70  ? 1.4521 0.4252 1.8251 0.2803  -0.2208 -0.0043 69  MET   E O   
8034  C  CB  . MET   E  70  ? 1.4140 0.6464 1.7502 0.1322  -0.1991 -0.0168 69  MET   E CB  
8035  C  CG  . MET   E  70  ? 1.4167 0.6034 1.7673 0.1333  -0.1926 0.0064  69  MET   E CG  
8036  S  SD  . MET   E  70  ? 1.4108 0.5497 1.7952 0.1270  -0.1962 0.0093  69  MET   E SD  
8037  C  CE  . MET   E  70  ? 1.3942 0.6201 1.7610 0.1259  -0.1565 0.0339  69  MET   E CE  
8038  N  N   . GLY   E  71  ? 1.4291 0.5084 1.7146 0.1405  -0.2673 0.0112  70  GLY   E N   
8039  C  CA  . GLY   E  71  ? 1.4526 0.6100 1.6910 0.0965  -0.2547 0.0312  70  GLY   E CA  
8040  C  C   . GLY   E  71  ? 1.4647 0.5666 1.6626 0.1061  -0.2314 0.0912  70  GLY   E C   
8041  O  O   . GLY   E  71  ? 1.5259 0.5149 1.6573 0.0971  -0.2345 0.1020  70  GLY   E O   
8042  N  N   . LEU   E  72  ? 1.4248 0.5405 1.6624 0.1169  -0.2059 0.0708  71  LEU   E N   
8043  C  CA  . LEU   E  72  ? 1.4091 0.5546 1.6619 0.0854  -0.1785 0.0611  71  LEU   E CA  
8044  C  C   . LEU   E  72  ? 1.3542 0.5819 1.6447 0.0551  -0.1590 0.0823  71  LEU   E C   
8045  O  O   . LEU   E  72  ? 1.3138 0.5966 1.6206 0.0261  -0.1541 0.1194  71  LEU   E O   
8046  C  CB  . LEU   E  72  ? 1.4105 0.5298 1.6532 0.1212  -0.1955 0.0876  71  LEU   E CB  
8047  C  CG  . LEU   E  72  ? 1.4463 0.4505 1.6174 0.1523  -0.1986 0.0932  71  LEU   E CG  
8048  C  CD1 . LEU   E  72  ? 1.4441 0.4762 1.6116 0.1756  -0.2188 0.1021  71  LEU   E CD1 
8049  C  CD2 . LEU   E  72  ? 1.4759 0.4875 1.5946 0.1041  -0.1972 0.0723  71  LEU   E CD2 
8050  N  N   . SER   E  73  ? 1.3328 0.5736 1.6699 0.0731  -0.1193 0.0978  72  SER   E N   
8051  C  CA  . SER   E  73  ? 1.3828 0.5569 1.6833 0.0627  -0.1317 0.0935  72  SER   E CA  
8052  C  C   . SER   E  73  ? 1.4077 0.5201 1.6930 0.0642  -0.1187 0.1036  72  SER   E C   
8053  O  O   . SER   E  73  ? 1.3812 0.4570 1.7065 0.1367  -0.1126 0.1099  72  SER   E O   
8054  C  CB  . SER   E  73  ? 1.3270 0.5623 1.7115 0.0255  -0.1483 0.1028  72  SER   E CB  
8055  O  OG  . SER   E  73  ? 1.3485 0.5084 1.7350 -0.0196 -0.1472 0.1113  72  SER   E OG  
8056  N  N   . LEU   E  74  ? 1.4856 0.5896 1.6475 0.0591  -0.1369 0.1057  73  LEU   E N   
8057  C  CA  . LEU   E  74  ? 1.4858 0.5332 1.6512 0.0645  -0.1691 0.0751  73  LEU   E CA  
8058  C  C   . LEU   E  74  ? 1.5371 0.5171 1.6560 0.0617  -0.1837 0.0524  73  LEU   E C   
8059  O  O   . LEU   E  74  ? 1.5436 0.3095 1.6617 0.0797  -0.1666 0.0823  73  LEU   E O   
8060  C  CB  . LEU   E  74  ? 1.4799 0.5652 1.6357 0.0576  -0.1915 0.0464  73  LEU   E CB  
8061  C  CG  . LEU   E  74  ? 1.5323 0.5633 1.6182 0.0547  -0.1808 0.0453  73  LEU   E CG  
8062  C  CD1 . LEU   E  74  ? 1.5883 0.5114 1.6129 0.0696  -0.1876 0.0319  73  LEU   E CD1 
8063  C  CD2 . LEU   E  74  ? 1.5237 0.5494 1.6162 0.0805  -0.1785 0.0632  73  LEU   E CD2 
8064  N  N   . ALA   E  75  ? 1.5958 0.4820 1.6631 0.0704  -0.1901 0.0215  74  ALA   E N   
8065  C  CA  . ALA   E  75  ? 1.6943 0.4869 1.7042 0.0433  -0.1911 0.0411  74  ALA   E CA  
8066  C  C   . ALA   E  75  ? 1.7420 0.3418 1.7124 0.0098  -0.1819 0.0525  74  ALA   E C   
8067  O  O   . ALA   E  75  ? 1.7767 0.1554 1.7255 0.0298  -0.1876 0.1304  74  ALA   E O   
8068  C  CB  . ALA   E  75  ? 1.6916 0.5271 1.7207 0.0471  -0.1796 0.0339  74  ALA   E CB  
8069  N  N   . GLY   E  76  ? 1.8656 0.3429 1.6818 0.0159  -0.1908 0.0341  75  GLY   E N   
8070  C  CA  . GLY   E  76  ? 1.8467 0.4223 1.6789 0.0305  -0.2182 0.0453  75  GLY   E CA  
8071  C  C   . GLY   E  76  ? 1.8714 0.3540 1.6910 0.0825  -0.2251 0.0699  75  GLY   E C   
8072  O  O   . GLY   E  76  ? 1.9767 0.2018 1.7312 0.0608  -0.2656 0.0771  75  GLY   E O   
8073  N  N   . LEU   E  77  ? 1.8341 0.4631 1.6418 0.0550  -0.3219 0.1018  76  LEU   E N   
8074  C  CA  . LEU   E  77  ? 1.7927 0.6430 1.6149 0.0611  -0.3093 0.1131  76  LEU   E CA  
8075  C  C   . LEU   E  77  ? 1.7885 0.6426 1.6308 0.0836  -0.3129 0.0722  76  LEU   E C   
8076  O  O   . LEU   E  77  ? 1.8106 0.6094 1.6217 0.1241  -0.2546 0.0590  76  LEU   E O   
8077  C  CB  . LEU   E  77  ? 1.7974 0.6888 1.6190 -0.0095 -0.3227 0.1510  76  LEU   E CB  
8078  C  CG  . LEU   E  77  ? 1.8343 0.7361 1.6524 -0.0331 -0.3245 0.1888  76  LEU   E CG  
8079  C  CD1 . LEU   E  77  ? 1.8251 0.8015 1.6590 -0.0692 -0.3027 0.1938  76  LEU   E CD1 
8080  C  CD2 . LEU   E  77  ? 1.8220 0.7248 1.6586 -0.0115 -0.3405 0.1876  76  LEU   E CD2 
8081  N  N   . ALA   E  78  ? 1.7651 0.6887 1.6729 0.0928  -0.3272 0.0363  77  ALA   E N   
8082  C  CA  . ALA   E  78  ? 1.7003 0.6947 1.6889 0.0789  -0.3274 0.0888  77  ALA   E CA  
8083  C  C   . ALA   E  78  ? 1.6707 0.6716 1.6388 0.0514  -0.2984 0.1188  77  ALA   E C   
8084  O  O   . ALA   E  78  ? 1.7135 0.6471 1.6320 0.1344  -0.2834 0.1315  77  ALA   E O   
8085  C  CB  . ALA   E  78  ? 1.6698 0.7274 1.7376 0.0943  -0.3376 0.1055  77  ALA   E CB  
8086  N  N   . PRO   E  79  ? 1.6343 0.7159 1.6087 0.0702  -0.3109 0.0699  78  PRO   E N   
8087  C  CA  . PRO   E  79  ? 1.6191 0.6885 1.5927 0.0478  -0.2958 0.0575  78  PRO   E CA  
8088  C  C   . PRO   E  79  ? 1.6315 0.7186 1.5729 0.0228  -0.3044 0.0343  78  PRO   E C   
8089  O  O   . PRO   E  79  ? 1.6841 0.7402 1.6216 0.0684  -0.2564 0.0153  78  PRO   E O   
8090  C  CB  . PRO   E  79  ? 1.6170 0.6948 1.5497 0.0481  -0.3025 0.0500  78  PRO   E CB  
8091  C  CG  . PRO   E  79  ? 1.6388 0.7056 1.5701 0.0427  -0.3058 0.0714  78  PRO   E CG  
8092  C  CD  . PRO   E  79  ? 1.6468 0.7388 1.5908 0.0395  -0.2928 0.0656  78  PRO   E CD  
8093  N  N   . ASP   E  80  ? 1.5957 0.7825 1.5737 0.0087  -0.3145 0.0143  79  ASP   E N   
8094  C  CA  . ASP   E  80  ? 1.5113 0.8300 1.5921 0.0080  -0.2998 0.0513  79  ASP   E CA  
8095  C  C   . ASP   E  80  ? 1.4387 0.7852 1.5918 0.0458  -0.2707 -0.0050 79  ASP   E C   
8096  O  O   . ASP   E  80  ? 1.3492 0.7108 1.6301 0.1084  -0.2137 -0.0531 79  ASP   E O   
8097  C  CB  . ASP   E  80  ? 1.4611 0.8641 1.5704 -0.0196 -0.3653 0.0648  79  ASP   E CB  
8098  C  CG  . ASP   E  80  ? 1.4269 0.8836 1.5680 -0.0326 -0.4171 0.0556  79  ASP   E CG  
8099  O  OD1 . ASP   E  80  ? 1.2995 1.0811 1.5935 -0.0638 -0.3870 0.0692  79  ASP   E OD1 
8100  O  OD2 . ASP   E  80  ? 1.4040 0.8679 1.5124 -0.0074 -0.4755 0.0930  79  ASP   E OD2 
8101  N  N   . ALA   E  81  ? 1.4343 0.8056 1.6082 0.0309  -0.2879 -0.0403 80  ALA   E N   
8102  C  CA  . ALA   E  81  ? 1.4547 0.8282 1.6143 0.0408  -0.2614 -0.0226 80  ALA   E CA  
8103  C  C   . ALA   E  81  ? 1.4471 0.8282 1.5566 0.1101  -0.2252 -0.0032 80  ALA   E C   
8104  O  O   . ALA   E  81  ? 1.4552 0.8159 1.5755 0.1308  -0.2597 0.0099  80  ALA   E O   
8105  C  CB  . ALA   E  81  ? 1.4631 0.8514 1.6497 0.0481  -0.2606 -0.0296 80  ALA   E CB  
8106  N  N   . ARG   E  82  ? 1.4433 0.7576 1.5568 0.1201  -0.2042 0.0279  81  ARG   E N   
8107  C  CA  . ARG   E  82  ? 1.4073 0.6963 1.4977 0.1048  -0.1916 0.0855  81  ARG   E CA  
8108  C  C   . ARG   E  82  ? 1.3581 0.7008 1.5086 0.1089  -0.1817 0.0249  81  ARG   E C   
8109  O  O   . ARG   E  82  ? 1.2910 0.7255 1.6022 0.0953  -0.2001 0.0650  81  ARG   E O   
8110  C  CB  . ARG   E  82  ? 1.4214 0.6964 1.5006 0.1064  -0.2009 0.1255  81  ARG   E CB  
8111  C  CG  . ARG   E  82  ? 1.4312 0.7102 1.3977 0.1087  -0.1783 0.1649  81  ARG   E CG  
8112  C  CD  . ARG   E  82  ? 1.4525 0.7565 1.4239 0.0992  -0.2154 0.2232  81  ARG   E CD  
8113  N  NE  . ARG   E  82  ? 1.5049 0.7313 1.3993 0.0678  -0.2148 0.2206  81  ARG   E NE  
8114  C  CZ  . ARG   E  82  ? 1.5243 0.7663 1.4158 0.0193  -0.2200 0.2429  81  ARG   E CZ  
8115  N  NH1 . ARG   E  82  ? 1.5239 0.8397 1.3989 0.0284  -0.2159 0.2635  81  ARG   E NH1 
8116  N  NH2 . ARG   E  82  ? 1.5267 0.9114 1.4196 0.0707  -0.1909 0.2400  81  ARG   E NH2 
8117  N  N   . VAL   E  83  ? 1.3873 0.5286 1.4032 0.1212  -0.1498 0.0114  82  VAL   E N   
8118  C  CA  . VAL   E  83  ? 1.3828 0.4880 1.3268 0.1059  -0.1377 -0.0015 82  VAL   E CA  
8119  C  C   . VAL   E  83  ? 1.4222 0.5535 1.3090 0.1173  -0.1403 0.0010  82  VAL   E C   
8120  O  O   . VAL   E  83  ? 1.4402 0.6215 1.1904 0.1414  -0.1036 0.1266  82  VAL   E O   
8121  C  CB  . VAL   E  83  ? 1.3542 0.4780 1.2843 0.1255  -0.1337 -0.0192 82  VAL   E CB  
8122  C  CG1 . VAL   E  83  ? 1.3271 0.4405 1.2889 0.1329  -0.1116 -0.0229 82  VAL   E CG1 
8123  C  CG2 . VAL   E  83  ? 1.3771 0.5606 1.2669 0.1116  -0.1353 -0.0357 82  VAL   E CG2 
8124  N  N   . LEU   E  84  ? 1.4317 0.5336 1.3401 0.1186  -0.1572 -0.0133 83  LEU   E N   
8125  C  CA  . LEU   E  84  ? 1.4373 0.5905 1.3468 0.1154  -0.1848 0.0251  83  LEU   E CA  
8126  C  C   . LEU   E  84  ? 1.4515 0.5934 1.4099 0.1075  -0.1931 -0.0153 83  LEU   E C   
8127  O  O   . LEU   E  84  ? 1.4072 0.6066 1.3433 0.1022  -0.2120 -0.0490 83  LEU   E O   
8128  C  CB  . LEU   E  84  ? 1.4413 0.6252 1.3385 0.1333  -0.1779 0.0131  83  LEU   E CB  
8129  C  CG  . LEU   E  84  ? 1.4460 0.6732 1.3303 0.1254  -0.1831 0.0102  83  LEU   E CG  
8130  C  CD1 . LEU   E  84  ? 1.4758 0.6830 1.3294 0.1563  -0.1865 0.0240  83  LEU   E CD1 
8131  C  CD2 . LEU   E  84  ? 1.4621 0.6836 1.3320 0.1402  -0.1732 0.0257  83  LEU   E CD2 
8132  N  N   . SER   E  85  ? 1.5074 0.6040 1.4214 0.1214  -0.2247 0.0184  84  SER   E N   
8133  C  CA  . SER   E  85  ? 1.4967 0.6697 1.4244 0.1032  -0.2293 0.0232  84  SER   E CA  
8134  C  C   . SER   E  85  ? 1.4634 0.7200 1.4166 0.1250  -0.2371 -0.0163 84  SER   E C   
8135  O  O   . SER   E  85  ? 1.4416 0.7302 1.3988 0.1288  -0.2194 -0.0203 84  SER   E O   
8136  C  CB  . SER   E  85  ? 1.5394 0.6468 1.4327 0.1129  -0.2284 0.0776  84  SER   E CB  
8137  O  OG  . SER   E  85  ? 1.6140 0.6148 1.4622 0.1191  -0.2063 0.1481  84  SER   E OG  
8138  N  N   . ASN   E  86  ? 1.4488 0.6879 1.4134 0.1427  -0.2414 -0.0406 85  ASN   E N   
8139  C  CA  . ASN   E  86  ? 1.4554 0.7061 1.4219 0.1455  -0.1859 -0.0389 85  ASN   E CA  
8140  C  C   . ASN   E  86  ? 1.4675 0.6582 1.4507 0.1535  -0.1879 -0.0335 85  ASN   E C   
8141  O  O   . ASN   E  86  ? 1.5149 0.6582 1.4357 0.1577  -0.1270 -0.0169 85  ASN   E O   
8142  C  CB  . ASN   E  86  ? 1.4282 0.7029 1.4645 0.1375  -0.1618 -0.0448 85  ASN   E CB  
8143  C  CG  . ASN   E  86  ? 1.4222 0.7418 1.5001 0.1645  -0.1208 -0.0491 85  ASN   E CG  
8144  O  OD1 . ASN   E  86  ? 1.3829 0.7902 1.5192 0.1290  -0.1266 -0.0151 85  ASN   E OD1 
8145  N  ND2 . ASN   E  86  ? 1.4824 0.6921 1.5169 0.1458  -0.1141 -0.0877 85  ASN   E ND2 
8146  N  N   . TYR   E  87  ? 1.4482 0.6213 1.4635 0.1686  -0.2428 0.0224  86  TYR   E N   
8147  C  CA  . TYR   E  87  ? 1.4786 0.5639 1.4882 0.1838  -0.2288 0.0834  86  TYR   E CA  
8148  C  C   . TYR   E  87  ? 1.4734 0.5296 1.4113 0.2297  -0.2824 0.1272  86  TYR   E C   
8149  O  O   . TYR   E  87  ? 1.4841 0.5559 1.4517 0.2791  -0.3066 0.1261  86  TYR   E O   
8150  C  CB  . TYR   E  87  ? 1.4659 0.5525 1.4849 0.1825  -0.2450 0.1110  86  TYR   E CB  
8151  C  CG  . TYR   E  87  ? 1.4213 0.4750 1.5254 0.2030  -0.2295 0.1502  86  TYR   E CG  
8152  C  CD1 . TYR   E  87  ? 1.4342 0.4313 1.5289 0.1997  -0.2118 0.1423  86  TYR   E CD1 
8153  C  CD2 . TYR   E  87  ? 1.4115 0.5008 1.5204 0.1835  -0.2180 0.1754  86  TYR   E CD2 
8154  C  CE1 . TYR   E  87  ? 1.4020 0.4763 1.5352 0.2157  -0.2121 0.1334  86  TYR   E CE1 
8155  C  CE2 . TYR   E  87  ? 1.3746 0.5120 1.5385 0.1861  -0.2136 0.1908  86  TYR   E CE2 
8156  C  CZ  . TYR   E  87  ? 1.3943 0.5225 1.5439 0.1998  -0.1919 0.1472  86  TYR   E CZ  
8157  O  OH  . TYR   E  87  ? 1.3810 0.6462 1.5831 0.2174  -0.1980 0.1946  86  TYR   E OH  
8158  N  N   . LEU   E  88  ? 1.4921 0.6000 1.3859 0.2600  -0.2834 0.1112  87  LEU   E N   
8159  C  CA  . LEU   E  88  ? 1.5042 0.6261 1.3831 0.2662  -0.2717 0.1070  87  LEU   E CA  
8160  C  C   . LEU   E  88  ? 1.4875 0.6768 1.4228 0.2354  -0.2497 0.0670  87  LEU   E C   
8161  O  O   . LEU   E  88  ? 1.4021 0.9135 1.2663 0.2101  -0.2432 0.1288  87  LEU   E O   
8162  C  CB  . LEU   E  88  ? 1.5454 0.6948 1.4262 0.3209  -0.2932 0.1076  87  LEU   E CB  
8163  C  CG  . LEU   E  88  ? 1.6201 0.7597 1.4057 0.3534  -0.2715 0.1416  87  LEU   E CG  
8164  C  CD1 . LEU   E  88  ? 1.6435 0.8318 1.4492 0.4030  -0.3034 0.1829  87  LEU   E CD1 
8165  C  CD2 . LEU   E  88  ? 1.6154 0.6749 1.4793 0.3618  -0.2465 0.1309  87  LEU   E CD2 
8166  N  N   . ARG   E  89  ? 1.5475 0.5434 1.4213 0.1830  -0.2319 0.0157  88  ARG   E N   
8167  C  CA  . ARG   E  89  ? 1.5855 0.5385 1.4897 0.1724  -0.2398 0.0000  88  ARG   E CA  
8168  C  C   . ARG   E  89  ? 1.6118 0.3893 1.4925 0.1019  -0.2195 -0.0086 88  ARG   E C   
8169  O  O   . ARG   E  89  ? 1.7484 0.1945 1.5445 0.2743  -0.2235 0.0164  88  ARG   E O   
8170  C  CB  . ARG   E  89  ? 1.5905 0.4985 1.4941 0.1431  -0.2807 -0.0121 88  ARG   E CB  
8171  C  CG  . ARG   E  89  ? 1.6059 0.4143 1.5650 0.1360  -0.2843 -0.0312 88  ARG   E CG  
8172  C  CD  . ARG   E  89  ? 1.6632 0.3528 1.5801 0.1295  -0.2819 -0.0234 88  ARG   E CD  
8173  N  NE  . ARG   E  89  ? 1.6849 0.3108 1.6002 0.1368  -0.2800 0.0187  88  ARG   E NE  
8174  C  CZ  . ARG   E  89  ? 1.7306 0.3618 1.5991 0.0670  -0.2676 0.0493  88  ARG   E CZ  
8175  N  NH1 . ARG   E  89  ? 1.7456 0.2581 1.6404 0.0510  -0.2349 0.0678  88  ARG   E NH1 
8176  N  NH2 . ARG   E  89  ? 1.6808 0.5108 1.6677 0.0285  -0.2721 -0.0043 88  ARG   E NH2 
8177  N  N   . GLN   E  90  ? 1.5937 0.4223 1.4397 0.1028  -0.2440 -0.0448 89  GLN   E N   
8178  C  CA  . GLN   E  90  ? 1.5523 0.3978 1.4317 0.0781  -0.1971 -0.0496 89  GLN   E CA  
8179  C  C   . GLN   E  90  ? 1.5666 0.4970 1.4255 0.0588  -0.1599 -0.0534 89  GLN   E C   
8180  O  O   . GLN   E  90  ? 1.6154 0.5306 1.4837 0.0576  -0.1571 0.0119  89  GLN   E O   
8181  C  CB  . GLN   E  90  ? 1.5570 0.4591 1.3534 0.0555  -0.2040 -0.0485 89  GLN   E CB  
8182  C  CG  . GLN   E  90  ? 1.5526 0.5584 1.3499 0.0384  -0.2197 -0.0040 89  GLN   E CG  
8183  C  CD  . GLN   E  90  ? 1.5341 0.7204 1.3527 0.0090  -0.2241 0.0133  89  GLN   E CD  
8184  O  OE1 . GLN   E  90  ? 1.5348 0.9161 1.2375 0.0032  -0.1959 0.0084  89  GLN   E OE1 
8185  N  NE2 . GLN   E  90  ? 1.5858 0.8330 1.3595 0.0057  -0.2311 0.0401  89  GLN   E NE2 
8186  N  N   . GLN   E  91  ? 1.5249 0.4412 1.4097 0.0875  -0.1026 -0.0095 90  GLN   E N   
8187  C  CA  . GLN   E  91  ? 1.4495 0.4655 1.4146 0.0994  -0.0706 0.0224  90  GLN   E CA  
8188  C  C   . GLN   E  91  ? 1.4735 0.5012 1.4432 0.0774  -0.0289 0.0130  90  GLN   E C   
8189  O  O   . GLN   E  91  ? 1.4400 0.5192 1.4410 0.0491  0.0455  0.0413  90  GLN   E O   
8190  C  CB  . GLN   E  91  ? 1.3980 0.4876 1.3614 0.1327  -0.1151 0.0190  90  GLN   E CB  
8191  C  CG  . GLN   E  91  ? 1.3616 0.5101 1.3252 0.1566  -0.1501 0.0019  90  GLN   E CG  
8192  C  CD  . GLN   E  91  ? 1.3373 0.5467 1.3407 0.1636  -0.1579 -0.0284 90  GLN   E CD  
8193  O  OE1 . GLN   E  91  ? 1.3484 0.6271 1.2656 0.1682  -0.0973 -0.0659 90  GLN   E OE1 
8194  N  NE2 . GLN   E  91  ? 1.3104 0.5335 1.3279 0.1448  -0.1798 -0.0245 90  GLN   E NE2 
8195  N  N   . CYS   E  92  ? 1.4922 0.4397 1.4532 0.0914  -0.0373 0.0306  91  CYS   E N   
8196  C  CA  . CYS   E  92  ? 1.4830 0.5244 1.4861 0.0789  -0.0615 0.0139  91  CYS   E CA  
8197  C  C   . CYS   E  92  ? 1.4854 0.5143 1.4491 0.0870  -0.0409 0.0388  91  CYS   E C   
8198  O  O   . CYS   E  92  ? 1.4849 0.4210 1.5701 0.0480  -0.0515 -0.0091 91  CYS   E O   
8199  C  CB  . CYS   E  92  ? 1.5428 0.5679 1.5550 0.0827  -0.1226 0.0338  91  CYS   E CB  
8200  S  SG  . CYS   E  92  ? 1.6326 0.7351 1.6047 0.1603  -0.0987 -0.0431 91  CYS   E SG  
8201  N  N   . ASN   E  93  ? 1.4899 0.4812 1.4426 0.0969  -0.0488 0.0030  92  ASN   E N   
8202  C  CA  . ASN   E  93  ? 1.5029 0.4160 1.4558 0.0305  -0.0721 0.0243  92  ASN   E CA  
8203  C  C   . ASN   E  93  ? 1.5114 0.4381 1.5122 0.0711  -0.1036 -0.0305 92  ASN   E C   
8204  O  O   . ASN   E  93  ? 1.5056 0.4427 1.5760 0.0797  -0.1177 -0.0156 92  ASN   E O   
8205  C  CB  . ASN   E  93  ? 1.4937 0.3782 1.4191 0.0230  -0.0942 -0.0185 92  ASN   E CB  
8206  C  CG  . ASN   E  93  ? 1.4785 0.4738 1.3071 0.0002  -0.0598 -0.0266 92  ASN   E CG  
8207  O  OD1 . ASN   E  93  ? 1.5421 0.5566 1.2568 0.0035  -0.0808 -0.0883 92  ASN   E OD1 
8208  N  ND2 . ASN   E  93  ? 1.4399 0.6449 1.3152 -0.0207 -0.0510 0.0091  92  ASN   E ND2 
8209  N  N   . TYR   E  94  ? 1.4857 0.3868 1.5158 0.1003  -0.1176 0.0184  93  TYR   E N   
8210  C  CA  . TYR   E  94  ? 1.5056 0.3937 1.4975 0.1407  -0.0878 0.0271  93  TYR   E CA  
8211  C  C   . TYR   E  94  ? 1.4526 0.4844 1.4542 0.1428  -0.1235 0.0369  93  TYR   E C   
8212  O  O   . TYR   E  94  ? 1.4437 0.5258 1.4474 0.2337  -0.1164 0.0367  93  TYR   E O   
8213  C  CB  . TYR   E  94  ? 1.5020 0.4045 1.5274 0.1439  -0.0905 0.0501  93  TYR   E CB  
8214  C  CG  . TYR   E  94  ? 1.5631 0.3727 1.5774 0.2109  -0.0560 0.0902  93  TYR   E CG  
8215  C  CD1 . TYR   E  94  ? 1.6397 0.3218 1.5202 0.1949  -0.0412 0.0494  93  TYR   E CD1 
8216  C  CD2 . TYR   E  94  ? 1.5769 0.3594 1.5853 0.2434  -0.0414 0.1354  93  TYR   E CD2 
8217  C  CE1 . TYR   E  94  ? 1.6470 0.2682 1.5602 0.2162  -0.0343 0.0278  93  TYR   E CE1 
8218  C  CE2 . TYR   E  94  ? 1.5694 0.3929 1.5935 0.2271  -0.0714 0.1117  93  TYR   E CE2 
8219  C  CZ  . TYR   E  94  ? 1.6598 0.3392 1.5712 0.2020  -0.0497 0.0302  93  TYR   E CZ  
8220  O  OH  . TYR   E  94  ? 1.6746 0.1697 1.7030 0.3107  0.0080  -0.1331 93  TYR   E OH  
8221  N  N   . SER   E  95  ? 1.3902 0.4955 1.4004 0.1447  -0.1310 0.0901  94  SER   E N   
8222  C  CA  . SER   E  95  ? 1.3937 0.5547 1.4037 0.1469  -0.1283 0.1115  94  SER   E CA  
8223  C  C   . SER   E  95  ? 1.4061 0.6255 1.4373 0.1088  -0.1168 0.0868  94  SER   E C   
8224  O  O   . SER   E  95  ? 1.4458 0.7157 1.3996 0.0880  -0.0714 0.1270  94  SER   E O   
8225  C  CB  . SER   E  95  ? 1.3623 0.5077 1.3920 0.1411  -0.1600 0.1379  94  SER   E CB  
8226  O  OG  . SER   E  95  ? 1.3494 0.5456 1.4119 0.1507  -0.1299 0.1251  94  SER   E OG  
8227  N  N   . SER   E  96  ? 1.4325 0.6324 1.4480 0.1212  -0.1288 0.1240  95  SER   E N   
8228  C  CA  . SER   E  96  ? 1.4634 0.6405 1.4866 0.0877  -0.1161 0.1329  95  SER   E CA  
8229  C  C   . SER   E  96  ? 1.4753 0.5894 1.4989 0.0373  -0.0844 0.1242  95  SER   E C   
8230  O  O   . SER   E  96  ? 1.4827 0.5675 1.5150 0.0851  -0.0670 0.1399  95  SER   E O   
8231  C  CB  . SER   E  96  ? 1.4983 0.6588 1.5183 0.0914  -0.1329 0.1678  95  SER   E CB  
8232  O  OG  . SER   E  96  ? 1.5082 0.7591 1.5422 0.1281  -0.1328 0.1355  95  SER   E OG  
8233  N  N   . LEU   E  97  ? 1.4911 0.5619 1.4828 0.0133  -0.0800 0.0809  96  LEU   E N   
8234  C  CA  . LEU   E  97  ? 1.5367 0.5236 1.5051 0.0081  -0.0934 0.0790  96  LEU   E CA  
8235  C  C   . LEU   E  97  ? 1.5057 0.5944 1.4670 0.0180  -0.0944 0.0494  96  LEU   E C   
8236  O  O   . LEU   E  97  ? 1.5487 0.6175 1.4536 -0.0358 -0.1061 0.1083  96  LEU   E O   
8237  C  CB  . LEU   E  97  ? 1.5545 0.5372 1.5268 -0.0432 -0.0974 0.0870  96  LEU   E CB  
8238  C  CG  . LEU   E  97  ? 1.5750 0.6625 1.5198 -0.0632 -0.1299 0.0742  96  LEU   E CG  
8239  C  CD1 . LEU   E  97  ? 1.5505 0.7240 1.5421 -0.0947 -0.1120 0.0191  96  LEU   E CD1 
8240  C  CD2 . LEU   E  97  ? 1.5907 0.6662 1.5540 -0.0850 -0.1391 0.1001  96  LEU   E CD2 
8241  N  N   . VAL   E  98  ? 1.4897 0.3916 1.4846 0.0452  -0.0389 0.0512  97  VAL   E N   
8242  C  CA  . VAL   E  98  ? 1.5043 0.4100 1.4331 0.0496  -0.0296 0.0438  97  VAL   E CA  
8243  C  C   . VAL   E  98  ? 1.4516 0.4855 1.4233 0.0574  -0.0188 0.0112  97  VAL   E C   
8244  O  O   . VAL   E  98  ? 1.4953 0.6243 1.3823 0.0788  -0.0845 0.1042  97  VAL   E O   
8245  C  CB  . VAL   E  98  ? 1.5010 0.3784 1.4134 0.0784  -0.0489 0.0461  97  VAL   E CB  
8246  C  CG1 . VAL   E  98  ? 1.5264 0.4149 1.3875 0.0902  -0.0258 0.0823  97  VAL   E CG1 
8247  C  CG2 . VAL   E  98  ? 1.5284 0.4154 1.3937 0.1192  -0.0389 0.0334  97  VAL   E CG2 
8248  N  N   . PHE   E  99  ? 1.4560 0.3850 1.4689 0.0598  -0.0527 0.0019  98  PHE   E N   
8249  C  CA  . PHE   E  99  ? 1.4460 0.4482 1.5022 0.0822  -0.0215 -0.0018 98  PHE   E CA  
8250  C  C   . PHE   E  99  ? 1.4519 0.4678 1.5253 0.0922  -0.0250 -0.0351 98  PHE   E C   
8251  O  O   . PHE   E  99  ? 1.4965 0.4754 1.5728 0.0948  0.0291  -0.0318 98  PHE   E O   
8252  C  CB  . PHE   E  99  ? 1.3693 0.4629 1.5187 0.0204  -0.0552 0.0056  98  PHE   E CB  
8253  C  CG  . PHE   E  99  ? 1.3603 0.4496 1.5315 -0.0092 -0.0263 0.0386  98  PHE   E CG  
8254  C  CD1 . PHE   E  99  ? 1.3333 0.3836 1.5278 0.0069  -0.0212 -0.0047 98  PHE   E CD1 
8255  C  CD2 . PHE   E  99  ? 1.3623 0.4388 1.5172 -0.0164 -0.0580 0.0451  98  PHE   E CD2 
8256  C  CE1 . PHE   E  99  ? 1.3453 0.3230 1.4793 -0.0004 -0.0329 -0.0307 98  PHE   E CE1 
8257  C  CE2 . PHE   E  99  ? 1.3808 0.4013 1.4758 -0.0374 -0.0698 0.0173  98  PHE   E CE2 
8258  C  CZ  . PHE   E  99  ? 1.3370 0.3698 1.4564 -0.0299 -0.0604 -0.0187 98  PHE   E CZ  
8259  N  N   . ASN   E  100 ? 1.4628 0.5545 1.5461 0.1198  -0.0509 -0.0352 99  ASN   E N   
8260  C  CA  . ASN   E  100 ? 1.4596 0.6335 1.5967 0.1046  -0.0505 -0.0119 99  ASN   E CA  
8261  C  C   . ASN   E  100 ? 1.4550 0.6669 1.5607 0.0742  -0.0413 -0.0222 99  ASN   E C   
8262  O  O   . ASN   E  100 ? 1.4912 0.7182 1.5365 0.0407  -0.0536 0.0151  99  ASN   E O   
8263  C  CB  . ASN   E  100 ? 1.4596 0.6420 1.6586 0.0981  -0.0373 0.0078  99  ASN   E CB  
8264  C  CG  . ASN   E  100 ? 1.4725 0.7459 1.7353 0.1196  -0.0700 -0.0305 99  ASN   E CG  
8265  O  OD1 . ASN   E  100 ? 1.5699 0.8483 1.8020 0.0630  -0.0175 0.0145  99  ASN   E OD1 
8266  N  ND2 . ASN   E  100 ? 1.4990 0.6802 1.7814 0.1059  -0.0470 -0.0079 99  ASN   E ND2 
8267  N  N   . ARG   E  101 ? 1.4921 0.6870 1.5721 0.0423  -0.0643 -0.0339 100 ARG   E N   
8268  C  CA  . ARG   E  101 ? 1.4948 0.6439 1.5780 0.0505  -0.0643 -0.0147 100 ARG   E CA  
8269  C  C   . ARG   E  101 ? 1.4756 0.6067 1.5841 0.0766  -0.0549 -0.0480 100 ARG   E C   
8270  O  O   . ARG   E  101 ? 1.4614 0.4725 1.5528 0.1549  -0.0799 0.0008  100 ARG   E O   
8271  C  CB  . ARG   E  101 ? 1.4977 0.6122 1.5680 0.0518  -0.0623 -0.0130 100 ARG   E CB  
8272  C  CG  . ARG   E  101 ? 1.4744 0.5504 1.5466 0.0294  -0.1189 -0.0069 100 ARG   E CG  
8273  C  CD  . ARG   E  101 ? 1.4880 0.4895 1.5772 0.0515  -0.1508 0.0280  100 ARG   E CD  
8274  N  NE  . ARG   E  101 ? 1.4636 0.4849 1.5746 0.0763  -0.2039 0.0205  100 ARG   E NE  
8275  C  CZ  . ARG   E  101 ? 1.4138 0.5299 1.6325 0.1309  -0.2386 0.0399  100 ARG   E CZ  
8276  N  NH1 . ARG   E  101 ? 1.3958 0.4444 1.6189 0.0984  -0.2714 0.0327  100 ARG   E NH1 
8277  N  NH2 . ARG   E  101 ? 1.3959 0.6530 1.6285 0.1690  -0.2435 0.0241  100 ARG   E NH2 
8278  N  N   . LYS   E  102 ? 1.4481 0.7022 1.5952 0.0488  -0.0204 -0.0791 101 LYS   E N   
8279  C  CA  . LYS   E  102 ? 1.4546 0.7285 1.5972 0.0406  -0.0298 -0.0646 101 LYS   E CA  
8280  C  C   . LYS   E  102 ? 1.4803 0.7772 1.5046 0.0330  -0.0201 -0.0772 101 LYS   E C   
8281  O  O   . LYS   E  102 ? 1.5341 0.8957 1.4972 0.0918  -0.0362 -0.1872 101 LYS   E O   
8282  C  CB  . LYS   E  102 ? 1.4299 0.8095 1.6478 -0.0286 -0.0246 -0.1076 101 LYS   E CB  
8283  C  CG  . LYS   E  102 ? 1.4367 0.8678 1.7034 -0.0659 -0.0292 -0.1422 101 LYS   E CG  
8284  C  CD  . LYS   E  102 ? 1.4297 1.0094 1.7502 -0.0980 -0.0549 -0.1692 101 LYS   E CD  
8285  C  CE  . LYS   E  102 ? 1.4838 1.2130 1.7615 -0.0947 -0.0919 -0.1781 101 LYS   E CE  
8286  N  NZ  . LYS   E  102 ? 1.4929 1.3635 1.8335 -0.0897 -0.0623 -0.1551 101 LYS   E NZ  
8287  N  N   . LEU   E  103 ? 1.4495 0.7075 1.5157 0.0213  -0.0586 -0.0895 102 LEU   E N   
8288  C  CA  . LEU   E  103 ? 1.4187 0.6593 1.5111 0.0101  -0.0510 -0.0155 102 LEU   E CA  
8289  C  C   . LEU   E  103 ? 1.4452 0.6551 1.5713 0.0351  -0.0567 -0.0142 102 LEU   E C   
8290  O  O   . LEU   E  103 ? 1.5269 0.5884 1.5623 0.0127  -0.1175 0.0208  102 LEU   E O   
8291  C  CB  . LEU   E  103 ? 1.3864 0.5969 1.4917 0.0513  -0.0414 -0.0415 102 LEU   E CB  
8292  C  CG  . LEU   E  103 ? 1.3630 0.5014 1.4667 0.0863  -0.0303 -0.0145 102 LEU   E CG  
8293  C  CD1 . LEU   E  103 ? 1.3375 0.4691 1.4340 0.0699  -0.0111 -0.0033 102 LEU   E CD1 
8294  C  CD2 . LEU   E  103 ? 1.3497 0.4731 1.4680 0.0560  -0.0490 -0.0269 102 LEU   E CD2 
8295  N  N   . ALA   E  104 ? 1.5058 0.7486 1.5897 0.0012  -0.0908 0.0067  103 ALA   E N   
8296  C  CA  . ALA   E  104 ? 1.4865 0.7515 1.6408 0.0613  -0.0716 0.0554  103 ALA   E CA  
8297  C  C   . ALA   E  104 ? 1.4479 0.7413 1.6665 0.0946  -0.1264 0.0745  103 ALA   E C   
8298  O  O   . ALA   E  104 ? 1.4393 0.5491 1.5685 0.1062  -0.1850 0.1422  103 ALA   E O   
8299  C  CB  . ALA   E  104 ? 1.5046 0.8738 1.6269 0.0326  -0.0586 0.0660  103 ALA   E CB  
8300  N  N   . VAL   E  105 ? 1.4678 0.6806 1.7336 0.0858  -0.1485 0.0607  104 VAL   E N   
8301  C  CA  . VAL   E  105 ? 1.4681 0.6102 1.7805 0.0587  -0.1635 -0.0210 104 VAL   E CA  
8302  C  C   . VAL   E  105 ? 1.4697 0.5670 1.7579 0.0721  -0.1715 -0.0023 104 VAL   E C   
8303  O  O   . VAL   E  105 ? 1.4221 0.4613 1.8397 0.0567  -0.2154 -0.0605 104 VAL   E O   
8304  C  CB  . VAL   E  105 ? 1.4825 0.5959 1.8098 0.0708  -0.1570 -0.0393 104 VAL   E CB  
8305  C  CG1 . VAL   E  105 ? 1.5179 0.6203 1.8321 0.0686  -0.1739 -0.0044 104 VAL   E CG1 
8306  C  CG2 . VAL   E  105 ? 1.4696 0.6160 1.8205 0.0664  -0.1451 -0.0505 104 VAL   E CG2 
8307  N  N   . GLU   E  106 ? 1.4726 0.6249 1.7499 0.0605  -0.1463 0.0205  105 GLU   E N   
8308  C  CA  . GLU   E  106 ? 1.4789 0.6628 1.7393 0.0346  -0.1206 0.0044  105 GLU   E CA  
8309  C  C   . GLU   E  106 ? 1.4461 0.6908 1.7406 0.0538  -0.1486 0.0084  105 GLU   E C   
8310  O  O   . GLU   E  106 ? 1.2277 0.7490 1.7116 0.0871  -0.2033 -0.0448 105 GLU   E O   
8311  C  CB  . GLU   E  106 ? 1.6247 0.7427 1.7641 -0.0045 -0.1129 0.0447  105 GLU   E CB  
8312  C  CG  . GLU   E  106 ? 1.7220 0.8658 1.8167 -0.0837 -0.1760 0.0308  105 GLU   E CG  
8313  C  CD  . GLU   E  106 ? 1.8545 1.0585 1.8341 -0.0839 -0.2268 0.1032  105 GLU   E CD  
8314  O  OE1 . GLU   E  106 ? 1.8092 1.1989 1.8460 -0.0390 -0.2179 0.1834  105 GLU   E OE1 
8315  O  OE2 . GLU   E  106 ? 1.9308 1.2665 2.0167 -0.2317 -0.1935 0.0203  105 GLU   E OE2 
8316  N  N   . ARG   E  107 ? 1.3686 0.7509 1.7272 0.0999  -0.0956 -0.0156 106 ARG   E N   
8317  C  CA  . ARG   E  107 ? 1.3724 0.8160 1.6586 0.0829  -0.0981 -0.0434 106 ARG   E CA  
8318  C  C   . ARG   E  107 ? 1.3560 0.7014 1.6106 0.0954  -0.1266 -0.1007 106 ARG   E C   
8319  O  O   . ARG   E  107 ? 1.3142 0.6911 1.5110 0.0993  -0.1868 -0.1730 106 ARG   E O   
8320  C  CB  . ARG   E  107 ? 1.3678 0.8267 1.6965 0.1163  -0.0931 -0.0302 106 ARG   E CB  
8321  C  CG  . ARG   E  107 ? 1.3581 0.8881 1.7048 0.1523  -0.0947 -0.0182 106 ARG   E CG  
8322  C  CD  . ARG   E  107 ? 1.3394 0.9373 1.7001 0.1648  -0.0748 -0.0523 106 ARG   E CD  
8323  N  NE  . ARG   E  107 ? 1.3376 1.0347 1.7238 0.1056  -0.0977 -0.0348 106 ARG   E NE  
8324  C  CZ  . ARG   E  107 ? 1.2760 1.1234 1.6944 0.0797  -0.0801 0.0386  106 ARG   E CZ  
8325  N  NH1 . ARG   E  107 ? 1.3257 1.2505 1.6174 0.0736  -0.0788 0.0603  106 ARG   E NH1 
8326  N  NH2 . ARG   E  107 ? 1.2783 1.1033 1.6583 0.0911  -0.0534 0.0543  106 ARG   E NH2 
8327  N  N   . ALA   E  108 ? 1.3832 0.6391 1.5522 0.0907  -0.1211 -0.0879 107 ALA   E N   
8328  C  CA  . ALA   E  108 ? 1.4466 0.6479 1.5525 0.0648  -0.1044 -0.0811 107 ALA   E CA  
8329  C  C   . ALA   E  108 ? 1.5003 0.6432 1.5324 0.0575  -0.0782 -0.0625 107 ALA   E C   
8330  O  O   . ALA   E  108 ? 1.5477 0.6400 1.4717 0.0924  -0.0462 -0.0772 107 ALA   E O   
8331  C  CB  . ALA   E  108 ? 1.4491 0.6544 1.5534 0.0477  -0.1048 -0.0679 107 ALA   E CB  
8332  N  N   . GLY   E  109 ? 1.5006 0.6030 1.5553 0.0411  -0.0902 -0.0791 108 GLY   E N   
8333  C  CA  . GLY   E  109 ? 1.4751 0.5728 1.6019 0.0266  -0.1205 -0.0233 108 GLY   E CA  
8334  C  C   . GLY   E  109 ? 1.4846 0.5044 1.6348 0.0159  -0.1419 -0.0287 108 GLY   E C   
8335  O  O   . GLY   E  109 ? 1.4547 0.5375 1.6021 0.0758  -0.1339 0.0273  108 GLY   E O   
8336  N  N   . HIS   E  110 ? 1.4932 0.4640 1.6684 -0.0081 -0.1117 -0.0042 109 HIS   E N   
8337  C  CA  . HIS   E  110 ? 1.4851 0.4845 1.6626 0.0126  -0.0956 -0.0334 109 HIS   E CA  
8338  C  C   . HIS   E  110 ? 1.4937 0.4191 1.6307 0.0066  -0.1142 -0.0604 109 HIS   E C   
8339  O  O   . HIS   E  110 ? 1.4486 0.4747 1.6749 0.0381  -0.1453 -0.1098 109 HIS   E O   
8340  C  CB  . HIS   E  110 ? 1.5068 0.5641 1.6568 0.0456  -0.0948 -0.0034 109 HIS   E CB  
8341  C  CG  . HIS   E  110 ? 1.5631 0.7194 1.6541 0.0901  -0.0926 -0.0273 109 HIS   E CG  
8342  N  ND1 . HIS   E  110 ? 1.5567 0.6976 1.6212 0.0459  -0.1218 0.0069  109 HIS   E ND1 
8343  C  CD2 . HIS   E  110 ? 1.5910 0.8377 1.6376 0.0903  -0.0503 0.0086  109 HIS   E CD2 
8344  C  CE1 . HIS   E  110 ? 1.5895 0.8609 1.6005 0.0776  -0.1172 0.0072  109 HIS   E CE1 
8345  N  NE2 . HIS   E  110 ? 1.5833 0.8542 1.6186 0.0929  -0.0728 0.0091  109 HIS   E NE2 
8346  N  N   . LEU   E  111 ? 1.5285 0.4651 1.6031 -0.0182 -0.1427 -0.0466 110 LEU   E N   
8347  C  CA  . LEU   E  111 ? 1.5589 0.5807 1.5149 -0.0478 -0.1959 -0.0695 110 LEU   E CA  
8348  C  C   . LEU   E  111 ? 1.5336 0.5978 1.4464 -0.0520 -0.2436 -0.0782 110 LEU   E C   
8349  O  O   . LEU   E  111 ? 1.5248 0.6898 1.3783 -0.1025 -0.2658 -0.0913 110 LEU   E O   
8350  C  CB  . LEU   E  111 ? 1.5395 0.6634 1.5601 -0.0809 -0.2069 -0.1090 110 LEU   E CB  
8351  C  CG  . LEU   E  111 ? 1.5035 0.6509 1.6194 -0.0855 -0.1786 -0.1080 110 LEU   E CG  
8352  C  CD1 . LEU   E  111 ? 1.4853 0.6980 1.6965 -0.1062 -0.1725 -0.1242 110 LEU   E CD1 
8353  C  CD2 . LEU   E  111 ? 1.4881 0.6792 1.6313 -0.1038 -0.1753 -0.1271 110 LEU   E CD2 
8354  N  N   . LEU   E  112 ? 1.5941 0.6316 1.4265 -0.0011 -0.2807 -0.0824 111 LEU   E N   
8355  C  CA  . LEU   E  112 ? 1.6330 0.6348 1.4685 0.0360  -0.2516 -0.0654 111 LEU   E CA  
8356  C  C   . LEU   E  112 ? 1.7023 0.6051 1.4681 0.0034  -0.2584 -0.0240 111 LEU   E C   
8357  O  O   . LEU   E  112 ? 1.7586 0.6923 1.4436 -0.0023 -0.2367 0.0017  111 LEU   E O   
8358  C  CB  . LEU   E  112 ? 1.6364 0.6388 1.4997 0.0726  -0.2169 -0.0964 111 LEU   E CB  
8359  C  CG  . LEU   E  112 ? 1.5822 0.6541 1.4980 0.1051  -0.2103 -0.1061 111 LEU   E CG  
8360  C  CD1 . LEU   E  112 ? 1.5925 0.6521 1.5307 0.1280  -0.1998 -0.1019 111 LEU   E CD1 
8361  C  CD2 . LEU   E  112 ? 1.6228 0.6760 1.4885 0.1097  -0.2113 -0.1019 111 LEU   E CD2 
8362  N  N   . CYS   E  113 ? 1.7335 0.6410 1.4626 0.0169  -0.1977 0.0610  112 CYS   E N   
8363  C  CA  . CYS   E  113 ? 1.7573 0.5921 1.5016 0.0113  -0.1621 0.0416  112 CYS   E CA  
8364  C  C   . CYS   E  113 ? 1.7749 0.5704 1.5251 0.0662  -0.1197 0.0533  112 CYS   E C   
8365  O  O   . CYS   E  113 ? 1.8165 0.4237 1.5465 0.1285  -0.1168 -0.0169 112 CYS   E O   
8366  C  CB  . CYS   E  113 ? 1.7866 0.6014 1.5258 -0.0290 -0.1106 0.0356  112 CYS   E CB  
8367  S  SG  . CYS   E  113 ? 1.9236 0.4309 1.5537 -0.0702 -0.0857 -0.0061 112 CYS   E SG  
8368  N  N   . ASP   E  114 ? 1.6850 0.5936 1.5498 0.0979  -0.0621 0.0240  113 ASP   E N   
8369  C  CA  . ASP   E  114 ? 1.6918 0.6080 1.5989 0.1052  -0.0280 -0.0049 113 ASP   E CA  
8370  C  C   . ASP   E  114 ? 1.6769 0.3562 1.5698 0.1134  -0.0691 -0.0208 113 ASP   E C   
8371  O  O   . ASP   E  114 ? 1.7091 0.1686 1.6154 0.0880  -0.0493 -0.0092 113 ASP   E O   
8372  C  CB  . ASP   E  114 ? 1.7109 0.6680 1.6745 0.0977  -0.0377 0.0710  113 ASP   E CB  
8373  C  CG  . ASP   E  114 ? 1.7074 0.8309 1.6942 0.0778  -0.0380 0.0957  113 ASP   E CG  
8374  O  OD1 . ASP   E  114 ? 1.7559 0.8877 1.8680 0.1752  -0.0836 0.0070  113 ASP   E OD1 
8375  O  OD2 . ASP   E  114 ? 1.5827 0.8375 1.7827 0.0524  -0.0959 0.1336  113 ASP   E OD2 
8376  N  N   . LYS   E  115 ? 1.6130 0.3521 1.5663 0.1346  -0.0527 -0.0197 114 LYS   E N   
8377  C  CA  . LYS   E  115 ? 1.5783 0.4971 1.5617 0.1204  -0.0752 0.0278  114 LYS   E CA  
8378  C  C   . LYS   E  115 ? 1.5617 0.4943 1.5462 0.1280  -0.0935 0.0249  114 LYS   E C   
8379  O  O   . LYS   E  115 ? 1.5614 0.4616 1.5450 0.1525  -0.0849 0.0192  114 LYS   E O   
8380  C  CB  . LYS   E  115 ? 1.5433 0.6283 1.5891 0.0989  -0.1100 0.0786  114 LYS   E CB  
8381  C  CG  . LYS   E  115 ? 1.5300 0.7744 1.5595 0.0423  -0.0959 0.0896  114 LYS   E CG  
8382  C  CD  . LYS   E  115 ? 1.5083 0.8546 1.6491 0.0247  -0.1436 0.1224  114 LYS   E CD  
8383  C  CE  . LYS   E  115 ? 1.5179 0.9181 1.6893 0.0109  -0.1167 0.0971  114 LYS   E CE  
8384  N  NZ  . LYS   E  115 ? 1.5311 0.9688 1.7231 0.0001  -0.1045 0.1083  114 LYS   E NZ  
8385  N  N   . ALA   E  116 ? 1.5407 0.5941 1.5230 0.1209  -0.0448 0.0120  115 ALA   E N   
8386  C  CA  . ALA   E  116 ? 1.5866 0.5841 1.5294 0.0775  -0.0358 -0.0321 115 ALA   E CA  
8387  C  C   . ALA   E  116 ? 1.6243 0.5614 1.5151 0.0788  -0.0628 -0.0432 115 ALA   E C   
8388  O  O   . ALA   E  116 ? 1.5896 0.6918 1.6161 -0.1289 -0.0449 -0.1735 115 ALA   E O   
8389  C  CB  . ALA   E  116 ? 1.5893 0.6388 1.5204 0.0712  0.0043  -0.0248 115 ALA   E CB  
8390  N  N   . GLN   E  117 ? 1.5814 0.4727 1.5506 0.1131  -0.0447 -0.0017 116 GLN   E N   
8391  C  CA  . GLN   E  117 ? 1.6041 0.5518 1.5492 0.1078  -0.0971 0.0810  116 GLN   E CA  
8392  C  C   . GLN   E  117 ? 1.6668 0.5136 1.5438 0.1741  -0.0487 0.0813  116 GLN   E C   
8393  O  O   . GLN   E  117 ? 1.7118 0.5093 1.4993 0.1610  -0.0377 0.1333  116 GLN   E O   
8394  C  CB  . GLN   E  117 ? 1.5963 0.6106 1.6058 0.0979  -0.0846 0.1437  116 GLN   E CB  
8395  C  CG  . GLN   E  117 ? 1.6483 0.6806 1.6142 0.0495  -0.1335 0.2148  116 GLN   E CG  
8396  C  CD  . GLN   E  117 ? 1.6373 0.6650 1.6228 0.0082  -0.1512 0.2513  116 GLN   E CD  
8397  O  OE1 . GLN   E  117 ? 1.6959 0.6564 1.7009 -0.0480 -0.1808 0.3649  116 GLN   E OE1 
8398  N  NE2 . GLN   E  117 ? 1.6860 0.7141 1.5445 0.0389  -0.1510 0.2056  116 GLN   E NE2 
8399  N  N   . LYS   E  118 ? 1.7372 0.5269 1.6043 0.1655  -0.0620 0.0423  117 LYS   E N   
8400  C  CA  . LYS   E  118 ? 1.7472 0.5710 1.6229 0.1822  -0.0563 0.0507  117 LYS   E CA  
8401  C  C   . LYS   E  118 ? 1.7602 0.5482 1.5237 0.2354  -0.1595 0.0380  117 LYS   E C   
8402  O  O   . LYS   E  118 ? 1.7536 0.6145 1.5766 0.2732  -0.1052 0.0226  117 LYS   E O   
8403  C  CB  . LYS   E  118 ? 1.7715 0.6060 1.6681 0.1925  -0.0226 -0.0058 117 LYS   E CB  
8404  C  CG  . LYS   E  118 ? 1.8264 0.5925 1.7083 0.2026  0.0213  0.0045  117 LYS   E CG  
8405  C  CD  . LYS   E  118 ? 1.8867 0.6218 1.7199 0.2174  0.0200  -0.0317 117 LYS   E CD  
8406  C  CE  . LYS   E  118 ? 1.9077 0.6429 1.7477 0.2585  0.0258  -0.0162 117 LYS   E CE  
8407  N  NZ  . LYS   E  118 ? 1.8952 0.6390 1.7515 0.2146  -0.0250 -0.0104 117 LYS   E NZ  
8408  N  N   . ASN   E  119 ? 1.8333 0.4070 1.4010 0.2082  -0.2010 0.0045  118 ASN   E N   
8409  C  CA  . ASN   E  119 ? 1.8669 0.4673 1.3726 0.2050  -0.2429 0.0236  118 ASN   E CA  
8410  C  C   . ASN   E  119 ? 1.9278 0.4618 1.3540 0.1036  -0.2658 0.0841  118 ASN   E C   
8411  O  O   . ASN   E  119 ? 1.9881 0.5161 1.2472 0.0992  -0.3393 0.0903  118 ASN   E O   
8412  C  CB  . ASN   E  119 ? 1.8788 0.3754 1.3442 0.2258  -0.2456 -0.0137 118 ASN   E CB  
8413  C  CG  . ASN   E  119 ? 1.8532 0.4021 1.3352 0.2710  -0.2595 -0.0250 118 ASN   E CG  
8414  O  OD1 . ASN   E  119 ? 1.8876 0.1472 1.3096 0.2730  -0.2304 -0.0905 118 ASN   E OD1 
8415  N  ND2 . ASN   E  119 ? 1.8530 0.4161 1.3409 0.3004  -0.2469 -0.0234 118 ASN   E ND2 
8416  N  N   . THR   E  120 ? 1.9277 0.5451 1.3631 0.0652  -0.2295 0.0868  119 THR   E N   
8417  C  CA  . THR   E  120 ? 1.8797 0.4811 1.4432 0.0722  -0.2162 0.1244  119 THR   E CA  
8418  C  C   . THR   E  120 ? 1.8699 0.4826 1.4476 0.0233  -0.2176 0.1141  119 THR   E C   
8419  O  O   . THR   E  120 ? 1.7336 0.4955 1.4189 0.0199  -0.2812 0.1203  119 THR   E O   
8420  C  CB  . THR   E  120 ? 1.9420 0.4010 1.4072 0.1134  -0.1894 0.1579  119 THR   E CB  
8421  O  OG1 . THR   E  120 ? 1.9730 0.5067 1.2427 0.1457  -0.1735 0.1035  119 THR   E OG1 
8422  C  CG2 . THR   E  120 ? 1.9243 0.3359 1.4391 0.1341  -0.1875 0.1671  119 THR   E CG2 
8423  N  N   . GLN   E  121 ? 1.8037 0.5715 1.4452 0.0481  -0.2025 0.1495  120 GLN   E N   
8424  C  CA  . GLN   E  121 ? 1.8059 0.6202 1.4497 0.0394  -0.1922 0.1179  120 GLN   E CA  
8425  C  C   . GLN   E  121 ? 1.8512 0.5815 1.5220 -0.0013 -0.1306 0.1303  120 GLN   E C   
8426  O  O   . GLN   E  121 ? 1.8982 0.3244 1.3855 -0.1173 -0.1029 0.0536  120 GLN   E O   
8427  C  CB  . GLN   E  121 ? 1.7837 0.6552 1.4756 0.0566  -0.1550 0.1417  120 GLN   E CB  
8428  C  CG  . GLN   E  121 ? 1.7725 0.6238 1.4851 0.0609  -0.1605 0.1450  120 GLN   E CG  
8429  C  CD  . GLN   E  121 ? 1.7356 0.5942 1.4674 0.0958  -0.1977 0.1455  120 GLN   E CD  
8430  O  OE1 . GLN   E  121 ? 1.7256 0.4137 1.4705 0.0157  -0.1564 0.0859  120 GLN   E OE1 
8431  N  NE2 . GLN   E  121 ? 1.6702 0.6308 1.4913 0.1126  -0.2047 0.1863  120 GLN   E NE2 
8432  N  N   . SER   E  122 ? 1.9386 0.6254 1.5403 -0.0096 -0.1480 0.1337  121 SER   E N   
8433  C  CA  . SER   E  122 ? 1.9143 0.5790 1.6525 -0.0587 -0.1131 0.1321  121 SER   E CA  
8434  C  C   . SER   E  122 ? 1.9717 0.6562 1.6474 -0.0545 -0.1862 0.1761  121 SER   E C   
8435  O  O   . SER   E  122 ? 1.9851 0.6665 1.5957 -0.0818 -0.2421 0.1546  121 SER   E O   
8436  C  CB  . SER   E  122 ? 1.9068 0.5423 1.7251 -0.0582 -0.1054 0.1420  121 SER   E CB  
8437  O  OG  . SER   E  122 ? 1.8553 0.2320 1.8610 -0.0708 -0.1240 0.0558  121 SER   E OG  
8438  N  N   . TYR   E  123 ? 1.9840 0.7565 1.6440 -0.0691 -0.1890 0.1640  122 TYR   E N   
8439  C  CA  . TYR   E  123 ? 2.1658 0.8572 1.5645 -0.1344 -0.2064 0.1542  122 TYR   E CA  
8440  C  C   . TYR   E  123 ? 2.0784 0.8157 1.6680 -0.1383 -0.2202 0.0633  122 TYR   E C   
8441  O  O   . TYR   E  123 ? 2.1224 0.8783 1.6535 0.0790  -0.2699 -0.0883 122 TYR   E O   
8442  C  CB  . TYR   E  123 ? 2.2209 1.0131 1.6383 -0.2097 -0.1482 0.3054  122 TYR   E CB  
8443  C  CG  . TYR   E  123 ? 2.4956 1.2236 1.6842 -0.2599 -0.1058 0.3889  122 TYR   E CG  
8444  C  CD1 . TYR   E  123 ? 2.6374 1.2450 1.7398 -0.2426 -0.0650 0.5123  122 TYR   E CD1 
8445  C  CD2 . TYR   E  123 ? 2.5806 1.2388 1.7440 -0.2721 -0.0658 0.3337  122 TYR   E CD2 
8446  C  CE1 . TYR   E  123 ? 2.7302 1.1668 1.8317 -0.1785 -0.0780 0.6037  122 TYR   E CE1 
8447  C  CE2 . TYR   E  123 ? 2.6430 1.2931 1.8186 -0.2730 0.0005  0.3819  122 TYR   E CE2 
8448  C  CZ  . TYR   E  123 ? 2.7517 1.3527 1.8115 -0.2305 -0.0311 0.5598  122 TYR   E CZ  
8449  O  OH  . TYR   E  123 ? 2.7255 1.7167 1.5758 -0.0767 0.0623  0.4748  122 TYR   E OH  
8450  N  N   . GLY   E  124 ? 2.0098 0.8305 1.6934 -0.1979 -0.2486 0.0842  123 GLY   E N   
8451  C  CA  . GLY   E  124 ? 2.0036 0.7580 1.7045 -0.1838 -0.2441 0.0800  123 GLY   E CA  
8452  C  C   . GLY   E  124 ? 1.9919 0.6966 1.7212 -0.1744 -0.1832 0.0557  123 GLY   E C   
8453  O  O   . GLY   E  124 ? 2.0954 0.7857 1.7730 -0.2044 -0.3075 -0.0137 123 GLY   E O   
8454  N  N   . GLY   E  125 ? 1.8112 0.6295 1.6978 -0.1324 -0.1686 -0.0154 124 GLY   E N   
8455  C  CA  . GLY   E  125 ? 1.7834 0.5251 1.6252 -0.0860 -0.1542 -0.0365 124 GLY   E CA  
8456  C  C   . GLY   E  125 ? 1.7626 0.4621 1.5697 -0.1239 -0.1692 -0.0152 124 GLY   E C   
8457  O  O   . GLY   E  125 ? 1.7970 0.4355 1.5795 -0.1294 -0.1372 0.0420  124 GLY   E O   
8458  N  N   . ARG   E  126 ? 1.7390 0.2695 1.4812 -0.0335 -0.1820 -0.0397 125 ARG   E N   
8459  C  CA  . ARG   E  126 ? 1.7671 0.2196 1.4683 -0.0211 -0.2022 -0.0163 125 ARG   E CA  
8460  C  C   . ARG   E  126 ? 1.7049 0.2646 1.4399 0.0042  -0.2154 -0.0407 125 ARG   E C   
8461  O  O   . ARG   E  126 ? 1.6484 0.3366 1.4095 -0.0773 -0.2182 -0.1506 125 ARG   E O   
8462  C  CB  . ARG   E  126 ? 1.7905 0.1725 1.4859 -0.0132 -0.2072 -0.0202 125 ARG   E CB  
8463  C  CG  . ARG   E  126 ? 1.8096 0.0975 1.5454 -0.0359 -0.1817 -0.0239 125 ARG   E CG  
8464  C  CD  . ARG   E  126 ? 1.8230 0.1733 1.5482 -0.0681 -0.1907 0.0154  125 ARG   E CD  
8465  N  NE  . ARG   E  126 ? 1.7968 0.1596 1.5515 -0.1333 -0.1746 0.0648  125 ARG   E NE  
8466  C  CZ  . ARG   E  126 ? 1.8162 0.1154 1.5469 -0.1255 -0.1889 0.0397  125 ARG   E CZ  
8467  N  NH1 . ARG   E  126 ? 1.7885 0.1161 1.5952 -0.1147 -0.1510 0.0784  125 ARG   E NH1 
8468  N  NH2 . ARG   E  126 ? 1.8474 0.1095 1.5446 -0.0999 -0.1434 0.0228  125 ARG   E NH2 
8469  N  N   . PRO   E  127 ? 1.6676 0.3028 1.4398 0.0318  -0.2254 -0.0241 126 PRO   E N   
8470  C  CA  . PRO   E  127 ? 1.6189 0.2905 1.4773 0.0210  -0.2448 -0.0694 126 PRO   E CA  
8471  C  C   . PRO   E  127 ? 1.6223 0.2527 1.4449 0.0608  -0.2437 -0.0712 126 PRO   E C   
8472  O  O   . PRO   E  127 ? 1.5902 0.1062 1.4873 -0.0247 -0.2590 -0.0726 126 PRO   E O   
8473  C  CB  . PRO   E  127 ? 1.6449 0.3065 1.4652 0.0471  -0.2344 -0.0561 126 PRO   E CB  
8474  C  CG  . PRO   E  127 ? 1.6588 0.3517 1.4682 0.0251  -0.2407 -0.0287 126 PRO   E CG  
8475  C  CD  . PRO   E  127 ? 1.6990 0.3221 1.4397 0.0188  -0.2548 -0.0431 126 PRO   E CD  
8476  N  N   . TYR   E  128 ? 1.5607 0.2966 1.5259 0.0639  -0.2017 -0.1208 127 TYR   E N   
8477  C  CA  . TYR   E  128 ? 1.5794 0.3809 1.5281 0.1092  -0.2358 -0.1026 127 TYR   E CA  
8478  C  C   . TYR   E  128 ? 1.6379 0.3388 1.5296 0.1060  -0.2542 -0.0659 127 TYR   E C   
8479  O  O   . TYR   E  128 ? 1.6481 0.2474 1.5255 0.1236  -0.2671 -0.0359 127 TYR   E O   
8480  C  CB  . TYR   E  128 ? 1.5622 0.4492 1.5353 0.1158  -0.1960 -0.0472 127 TYR   E CB  
8481  C  CG  . TYR   E  128 ? 1.5260 0.5249 1.5427 0.1684  -0.1980 -0.0273 127 TYR   E CG  
8482  C  CD1 . TYR   E  128 ? 1.5219 0.4976 1.5759 0.1616  -0.2037 -0.0450 127 TYR   E CD1 
8483  C  CD2 . TYR   E  128 ? 1.5010 0.5988 1.5485 0.1881  -0.1763 -0.0084 127 TYR   E CD2 
8484  C  CE1 . TYR   E  128 ? 1.4505 0.5324 1.5772 0.1581  -0.1891 -0.0619 127 TYR   E CE1 
8485  C  CE2 . TYR   E  128 ? 1.4777 0.5882 1.5397 0.1590  -0.1391 -0.0450 127 TYR   E CE2 
8486  C  CZ  . TYR   E  128 ? 1.4101 0.5176 1.5734 0.1774  -0.1512 -0.0517 127 TYR   E CZ  
8487  O  OH  . TYR   E  128 ? 1.4217 0.4620 1.6489 0.1500  -0.1336 -0.0118 127 TYR   E OH  
8488  N  N   . GLY   E  129 ? 1.6574 0.3135 1.5382 0.1145  -0.2603 -0.0595 128 GLY   E N   
8489  C  CA  . GLY   E  129 ? 1.6716 0.3050 1.5401 0.1100  -0.2913 -0.0543 128 GLY   E CA  
8490  C  C   . GLY   E  129 ? 1.6796 0.3428 1.5575 0.1001  -0.2939 -0.0681 128 GLY   E C   
8491  O  O   . GLY   E  129 ? 1.7450 0.3121 1.5869 0.1037  -0.3222 -0.0752 128 GLY   E O   
8492  N  N   . VAL   E  130 ? 1.6543 0.3997 1.5299 0.1271  -0.2984 -0.0388 129 VAL   E N   
8493  C  CA  . VAL   E  130 ? 1.6428 0.4395 1.5329 0.1486  -0.3079 -0.0573 129 VAL   E CA  
8494  C  C   . VAL   E  130 ? 1.6503 0.4265 1.5557 0.1789  -0.2862 -0.0346 129 VAL   E C   
8495  O  O   . VAL   E  130 ? 1.6153 0.2322 1.6276 0.1924  -0.2714 -0.0487 129 VAL   E O   
8496  C  CB  . VAL   E  130 ? 1.6393 0.4400 1.5137 0.1754  -0.3297 -0.0546 129 VAL   E CB  
8497  C  CG1 . VAL   E  130 ? 1.6130 0.4241 1.4872 0.1950  -0.3304 -0.1080 129 VAL   E CG1 
8498  C  CG2 . VAL   E  130 ? 1.6385 0.4835 1.5674 0.1471  -0.3124 -0.0720 129 VAL   E CG2 
8499  N  N   . GLY   E  131 ? 1.6585 0.5215 1.5625 0.1547  -0.2568 -0.0271 130 GLY   E N   
8500  C  CA  . GLY   E  131 ? 1.6930 0.5238 1.5518 0.1359  -0.2575 -0.0235 130 GLY   E CA  
8501  C  C   . GLY   E  131 ? 1.6678 0.5462 1.5300 0.1350  -0.2767 -0.0036 130 GLY   E C   
8502  O  O   . GLY   E  131 ? 1.7006 0.4618 1.5091 0.1373  -0.2701 0.0224  130 GLY   E O   
8503  N  N   . LEU   E  132 ? 1.6264 0.5917 1.5166 0.1024  -0.2685 0.0097  131 LEU   E N   
8504  C  CA  . LEU   E  132 ? 1.6228 0.6031 1.5111 0.0946  -0.2875 0.0122  131 LEU   E CA  
8505  C  C   . LEU   E  132 ? 1.5680 0.6025 1.5936 0.0731  -0.2732 0.0385  131 LEU   E C   
8506  O  O   . LEU   E  132 ? 1.5386 0.5780 1.6159 0.0656  -0.2879 0.0444  131 LEU   E O   
8507  C  CB  . LEU   E  132 ? 1.6384 0.5774 1.4286 0.0852  -0.3106 0.0221  131 LEU   E CB  
8508  C  CG  . LEU   E  132 ? 1.6549 0.6264 1.4257 0.0886  -0.3121 0.0418  131 LEU   E CG  
8509  C  CD1 . LEU   E  132 ? 1.5999 0.7150 1.3652 0.1107  -0.3466 0.0813  131 LEU   E CD1 
8510  C  CD2 . LEU   E  132 ? 1.7070 0.6661 1.4344 0.0679  -0.3267 0.0478  131 LEU   E CD2 
8511  N  N   . LEU   E  133 ? 1.5853 0.6527 1.6519 0.0913  -0.3455 0.0059  132 LEU   E N   
8512  C  CA  . LEU   E  133 ? 1.5962 0.6986 1.6961 0.0760  -0.3259 -0.0185 132 LEU   E CA  
8513  C  C   . LEU   E  133 ? 1.5614 0.7036 1.7504 0.1035  -0.3334 -0.0715 132 LEU   E C   
8514  O  O   . LEU   E  133 ? 1.5280 0.6067 1.7526 0.1780  -0.3338 -0.0886 132 LEU   E O   
8515  C  CB  . LEU   E  133 ? 1.6169 0.7549 1.7173 0.0930  -0.3549 -0.0411 132 LEU   E CB  
8516  C  CG  . LEU   E  133 ? 1.6777 0.7640 1.7087 0.0715  -0.3471 -0.0738 132 LEU   E CG  
8517  C  CD1 . LEU   E  133 ? 1.6518 0.8451 1.6967 0.0667  -0.3609 -0.1043 132 LEU   E CD1 
8518  C  CD2 . LEU   E  133 ? 1.6875 0.8023 1.6854 0.0775  -0.3340 -0.0656 132 LEU   E CD2 
8519  N  N   . ILE   E  134 ? 1.5693 0.6850 1.7814 0.0760  -0.2748 -0.0209 133 ILE   E N   
8520  C  CA  . ILE   E  134 ? 1.5764 0.6846 1.8003 0.0559  -0.1898 -0.0120 133 ILE   E CA  
8521  C  C   . ILE   E  134 ? 1.5981 0.6521 1.7955 0.0688  -0.1690 -0.0102 133 ILE   E C   
8522  O  O   . ILE   E  134 ? 1.6924 0.7660 1.8092 0.0800  -0.1244 -0.0414 133 ILE   E O   
8523  C  CB  . ILE   E  134 ? 1.5574 0.6284 1.8559 0.0463  -0.1638 -0.0141 133 ILE   E CB  
8524  C  CG1 . ILE   E  134 ? 1.5345 0.6829 1.8877 0.0500  -0.1598 -0.0357 133 ILE   E CG1 
8525  C  CG2 . ILE   E  134 ? 1.5887 0.6271 1.8697 0.0491  -0.1349 0.0137  133 ILE   E CG2 
8526  C  CD1 . ILE   E  134 ? 1.5329 0.7707 1.9425 0.0207  -0.1827 -0.0586 133 ILE   E CD1 
8527  N  N   . ILE   E  135 ? 1.5377 0.5926 1.7515 0.0828  -0.1222 0.0128  134 ILE   E N   
8528  C  CA  . ILE   E  135 ? 1.5221 0.7149 1.7269 0.0782  -0.0998 0.0007  134 ILE   E CA  
8529  C  C   . ILE   E  135 ? 1.5161 0.7277 1.6980 0.0482  -0.0725 -0.0647 134 ILE   E C   
8530  O  O   . ILE   E  135 ? 1.4705 0.8467 1.6887 -0.0354 -0.0187 -0.0377 134 ILE   E O   
8531  C  CB  . ILE   E  135 ? 1.5667 0.6448 1.7033 0.1142  -0.1034 0.0268  134 ILE   E CB  
8532  C  CG1 . ILE   E  135 ? 1.5770 0.5501 1.7019 0.1221  -0.1154 0.0306  134 ILE   E CG1 
8533  C  CG2 . ILE   E  135 ? 1.6049 0.6549 1.7125 0.1003  -0.0904 -0.0007 134 ILE   E CG2 
8534  C  CD1 . ILE   E  135 ? 1.5821 0.5513 1.7078 0.1043  -0.1237 0.0098  134 ILE   E CD1 
8535  N  N   . GLY   E  136 ? 1.5394 0.7799 1.6836 0.0295  -0.0791 -0.0607 135 GLY   E N   
8536  C  CA  . GLY   E  136 ? 1.5663 0.7904 1.7369 0.0817  -0.1059 -0.0850 135 GLY   E CA  
8537  C  C   . GLY   E  136 ? 1.5886 0.8457 1.7518 0.0789  -0.0954 -0.0733 135 GLY   E C   
8538  O  O   . GLY   E  136 ? 1.6334 0.8465 1.8257 0.1271  -0.1213 -0.1236 135 GLY   E O   
8539  N  N   . TYR   E  137 ? 1.6018 0.8360 1.7671 0.0839  -0.1037 -0.0554 136 TYR   E N   
8540  C  CA  . TYR   E  137 ? 1.6067 0.7588 1.7837 0.1272  -0.0914 -0.0511 136 TYR   E CA  
8541  C  C   . TYR   E  137 ? 1.6440 0.6762 1.7656 0.0975  -0.0688 -0.0898 136 TYR   E C   
8542  O  O   . TYR   E  137 ? 1.7111 0.6266 1.7122 0.0950  -0.0875 -0.0435 136 TYR   E O   
8543  C  CB  . TYR   E  137 ? 1.5942 0.8055 1.8113 0.1276  -0.0725 -0.0341 136 TYR   E CB  
8544  C  CG  . TYR   E  137 ? 1.6139 0.8037 1.8359 0.1538  -0.0656 0.0137  136 TYR   E CG  
8545  C  CD1 . TYR   E  137 ? 1.5783 0.8049 1.8313 0.1439  -0.0403 0.0220  136 TYR   E CD1 
8546  C  CD2 . TYR   E  137 ? 1.5892 0.9172 1.8639 0.1801  -0.0361 0.0179  136 TYR   E CD2 
8547  C  CE1 . TYR   E  137 ? 1.5696 0.8414 1.8679 0.1247  -0.0158 0.0084  136 TYR   E CE1 
8548  C  CE2 . TYR   E  137 ? 1.5647 0.8683 1.8895 0.1846  -0.0494 0.0541  136 TYR   E CE2 
8549  C  CZ  . TYR   E  137 ? 1.5449 0.8542 1.8562 0.1311  -0.0026 0.0322  136 TYR   E CZ  
8550  O  OH  . TYR   E  137 ? 1.4904 0.9935 1.8669 0.1493  0.0758  -0.0627 136 TYR   E OH  
8551  N  N   . ASP   E  138 ? 1.6293 0.7148 1.7436 0.0980  -0.0474 -0.1377 137 ASP   E N   
8552  C  CA  . ASP   E  138 ? 1.5858 0.7916 1.7722 0.1470  -0.0110 -0.1564 137 ASP   E CA  
8553  C  C   . ASP   E  138 ? 1.5916 0.8586 1.7655 0.1706  -0.0031 -0.1322 137 ASP   E C   
8554  O  O   . ASP   E  138 ? 1.5788 0.9058 1.7486 0.1666  -0.0277 -0.1280 137 ASP   E O   
8555  C  CB  . ASP   E  138 ? 1.5711 0.8073 1.8382 0.1492  0.0138  -0.1496 137 ASP   E CB  
8556  C  CG  . ASP   E  138 ? 1.5405 0.8949 1.8197 0.1451  0.0247  -0.1746 137 ASP   E CG  
8557  O  OD1 . ASP   E  138 ? 1.5477 0.9982 1.8924 0.1344  0.0676  -0.1585 137 ASP   E OD1 
8558  O  OD2 . ASP   E  138 ? 1.4383 1.0969 1.8463 0.1614  0.0902  -0.0775 137 ASP   E OD2 
8559  N  N   . LYS   E  139 ? 1.6022 0.8697 1.7546 0.1694  0.0266  -0.0857 138 LYS   E N   
8560  C  CA  . LYS   E  139 ? 1.5820 0.9042 1.8287 0.1550  -0.0068 -0.0187 138 LYS   E CA  
8561  C  C   . LYS   E  139 ? 1.5351 0.9449 1.8084 0.1495  -0.0283 -0.0169 138 LYS   E C   
8562  O  O   . LYS   E  139 ? 1.4426 0.9976 1.9103 0.0957  -0.0221 0.0117  138 LYS   E O   
8563  C  CB  . LYS   E  139 ? 1.5579 0.9483 1.8543 0.1858  0.0042  -0.0798 138 LYS   E CB  
8564  C  CG  . LYS   E  139 ? 1.5943 0.9525 1.8819 0.2287  0.0072  -0.0871 138 LYS   E CG  
8565  C  CD  . LYS   E  139 ? 1.6081 0.9227 1.9458 0.2699  0.0017  -0.1057 138 LYS   E CD  
8566  C  CE  . LYS   E  139 ? 1.6463 0.8861 1.9705 0.2834  -0.0263 -0.0762 138 LYS   E CE  
8567  N  NZ  . LYS   E  139 ? 1.6831 0.9415 1.9724 0.2422  -0.0399 -0.0324 138 LYS   E NZ  
8568  N  N   . SER   E  140 ? 1.5520 0.9456 1.7964 0.1563  -0.0864 0.0337  139 SER   E N   
8569  C  CA  . SER   E  140 ? 1.5547 1.0284 1.7619 0.1661  -0.0960 0.0170  139 SER   E CA  
8570  C  C   . SER   E  140 ? 1.6214 1.0968 1.7588 0.2076  -0.1427 0.0098  139 SER   E C   
8571  O  O   . SER   E  140 ? 1.6667 1.1811 1.6999 0.2030  -0.1271 -0.0563 139 SER   E O   
8572  C  CB  . SER   E  140 ? 1.4833 1.0640 1.7625 0.1791  -0.0887 0.0654  139 SER   E CB  
8573  O  OG  . SER   E  140 ? 1.3757 1.1849 1.7874 0.1446  -0.1065 0.0943  139 SER   E OG  
8574  N  N   . GLY   E  141 ? 1.6705 1.1117 1.8060 0.2145  -0.1786 -0.0264 140 GLY   E N   
8575  C  CA  . GLY   E  141 ? 1.6527 1.1056 1.8382 0.1956  -0.1883 -0.0244 140 GLY   E CA  
8576  C  C   . GLY   E  141 ? 1.6627 1.0185 1.8742 0.2145  -0.2389 -0.0109 140 GLY   E C   
8577  O  O   . GLY   E  141 ? 1.5963 1.0129 1.8975 0.1695  -0.2476 0.0276  140 GLY   E O   
8578  N  N   . ALA   E  142 ? 1.7406 0.9317 1.8294 0.1823  -0.2183 0.0093  141 ALA   E N   
8579  C  CA  . ALA   E  142 ? 1.7133 0.8713 1.8313 0.1613  -0.2002 -0.0224 141 ALA   E CA  
8580  C  C   . ALA   E  142 ? 1.7214 0.7624 1.7739 0.1552  -0.1459 0.0188  141 ALA   E C   
8581  O  O   . ALA   E  142 ? 1.5999 0.5698 1.7931 0.0808  -0.1174 -0.0274 141 ALA   E O   
8582  C  CB  . ALA   E  142 ? 1.7552 0.9199 1.8415 0.2160  -0.1907 -0.0145 141 ALA   E CB  
8583  N  N   . HIS   E  143 ? 1.7203 0.7238 1.7928 0.1217  -0.1546 0.0061  142 HIS   E N   
8584  C  CA  . HIS   E  143 ? 1.6876 0.8367 1.8080 0.1051  -0.1624 -0.0309 142 HIS   E CA  
8585  C  C   . HIS   E  143 ? 1.6703 0.7932 1.8639 0.0663  -0.1649 -0.0312 142 HIS   E C   
8586  O  O   . HIS   E  143 ? 1.7350 0.9507 1.8537 0.1068  -0.1277 -0.0884 142 HIS   E O   
8587  C  CB  . HIS   E  143 ? 1.6695 0.8125 1.7887 0.0822  -0.1277 -0.0337 142 HIS   E CB  
8588  C  CG  . HIS   E  143 ? 1.7419 0.8367 1.8182 0.0324  -0.0832 -0.0037 142 HIS   E CG  
8589  N  ND1 . HIS   E  143 ? 1.7976 0.8644 1.8188 0.0106  -0.0457 -0.0465 142 HIS   E ND1 
8590  C  CD2 . HIS   E  143 ? 1.7761 0.8600 1.8421 -0.0247 -0.0669 -0.0360 142 HIS   E CD2 
8591  C  CE1 . HIS   E  143 ? 1.7771 0.8628 1.8522 -0.0104 -0.0107 -0.0354 142 HIS   E CE1 
8592  N  NE2 . HIS   E  143 ? 1.7706 0.8737 1.8467 -0.0251 -0.0439 -0.0195 142 HIS   E NE2 
8593  N  N   . LEU   E  144 ? 1.6096 0.7466 1.8247 0.1062  -0.1940 0.0093  143 LEU   E N   
8594  C  CA  . LEU   E  144 ? 1.5866 0.7208 1.7800 0.1153  -0.2064 -0.0210 143 LEU   E CA  
8595  C  C   . LEU   E  144 ? 1.5841 0.6728 1.6452 0.1704  -0.2292 -0.0560 143 LEU   E C   
8596  O  O   . LEU   E  144 ? 1.5155 0.5917 1.6213 0.2420  -0.3202 0.0281  143 LEU   E O   
8597  C  CB  . LEU   E  144 ? 1.6105 0.7180 1.8190 0.1198  -0.1997 -0.0082 143 LEU   E CB  
8598  C  CG  . LEU   E  144 ? 1.6481 0.7277 1.8099 0.1028  -0.2144 0.0117  143 LEU   E CG  
8599  C  CD1 . LEU   E  144 ? 1.6328 0.6538 1.8075 0.0800  -0.2066 0.0229  143 LEU   E CD1 
8600  C  CD2 . LEU   E  144 ? 1.6884 0.6948 1.8334 0.1179  -0.2087 0.0544  143 LEU   E CD2 
8601  N  N   . LEU   E  145 ? 1.5989 0.7005 1.6545 0.1537  -0.2150 -0.0862 144 LEU   E N   
8602  C  CA  . LEU   E  145 ? 1.6382 0.7013 1.6174 0.1123  -0.2164 -0.0589 144 LEU   E CA  
8603  C  C   . LEU   E  145 ? 1.6576 0.7213 1.5831 0.1435  -0.2334 -0.0454 144 LEU   E C   
8604  O  O   . LEU   E  145 ? 1.7274 0.6492 1.4896 0.1794  -0.1777 -0.0382 144 LEU   E O   
8605  C  CB  . LEU   E  145 ? 1.6418 0.7211 1.6252 0.0958  -0.1755 -0.0605 144 LEU   E CB  
8606  C  CG  . LEU   E  145 ? 1.6733 0.7043 1.6031 0.0569  -0.1511 -0.0470 144 LEU   E CG  
8607  C  CD1 . LEU   E  145 ? 1.6989 0.8055 1.6426 0.0299  -0.1040 -0.0909 144 LEU   E CD1 
8608  C  CD2 . LEU   E  145 ? 1.6689 0.6537 1.6179 0.0237  -0.1248 -0.0434 144 LEU   E CD2 
8609  N  N   . GLU   E  146 ? 1.6577 0.7087 1.6207 0.1167  -0.2522 0.0214  145 GLU   E N   
8610  C  CA  . GLU   E  146 ? 1.6819 0.6833 1.6770 0.1288  -0.2697 0.0405  145 GLU   E CA  
8611  C  C   . GLU   E  146 ? 1.6791 0.6022 1.6354 0.1297  -0.2417 0.0443  145 GLU   E C   
8612  O  O   . GLU   E  146 ? 1.6436 0.5631 1.6832 0.0766  -0.2616 0.0794  145 GLU   E O   
8613  C  CB  . GLU   E  146 ? 1.7603 0.7143 1.7624 0.1441  -0.2560 0.0005  145 GLU   E CB  
8614  C  CG  . GLU   E  146 ? 1.8658 0.7220 1.7997 0.1229  -0.2550 0.0125  145 GLU   E CG  
8615  C  CD  . GLU   E  146 ? 1.9858 0.7066 1.9049 0.1846  -0.2567 0.0248  145 GLU   E CD  
8616  O  OE1 . GLU   E  146 ? 1.9463 0.6740 2.0537 0.1218  -0.1982 0.0931  145 GLU   E OE1 
8617  O  OE2 . GLU   E  146 ? 2.1066 0.7396 1.9397 0.1280  -0.3244 0.0965  145 GLU   E OE2 
8618  N  N   . PHE   E  147 ? 1.6310 0.5847 1.6308 0.1453  -0.2520 0.0316  146 PHE   E N   
8619  C  CA  . PHE   E  147 ? 1.6293 0.6514 1.6581 0.1286  -0.2594 0.0448  146 PHE   E CA  
8620  C  C   . PHE   E  147 ? 1.6576 0.6146 1.6562 0.1888  -0.2520 0.0285  146 PHE   E C   
8621  O  O   . PHE   E  147 ? 1.6789 0.5352 1.7674 0.3879  -0.2629 -0.0261 146 PHE   E O   
8622  C  CB  . PHE   E  147 ? 1.5676 0.5887 1.6523 0.1007  -0.2521 0.0875  146 PHE   E CB  
8623  C  CG  . PHE   E  147 ? 1.5039 0.5485 1.6618 0.0941  -0.3144 0.1454  146 PHE   E CG  
8624  C  CD1 . PHE   E  147 ? 1.5099 0.5359 1.5997 0.0387  -0.3446 0.1692  146 PHE   E CD1 
8625  C  CD2 . PHE   E  147 ? 1.5146 0.5906 1.6834 0.0829  -0.2959 0.1674  146 PHE   E CD2 
8626  C  CE1 . PHE   E  147 ? 1.5176 0.5194 1.5757 0.0095  -0.3611 0.1675  146 PHE   E CE1 
8627  C  CE2 . PHE   E  147 ? 1.5076 0.5659 1.6438 0.0489  -0.3215 0.1681  146 PHE   E CE2 
8628  C  CZ  . PHE   E  147 ? 1.5298 0.5231 1.5728 0.0049  -0.3541 0.1637  146 PHE   E CZ  
8629  N  N   . GLN   E  148 ? 1.6206 0.7387 1.7035 0.1242  -0.1954 0.0196  147 GLN   E N   
8630  C  CA  . GLN   E  148 ? 1.6735 0.6833 1.7375 0.1401  -0.1727 0.0201  147 GLN   E CA  
8631  C  C   . GLN   E  148 ? 1.6851 0.6033 1.7083 0.1083  -0.1362 0.0546  147 GLN   E C   
8632  O  O   . GLN   E  148 ? 1.6950 0.7577 1.7322 0.2100  -0.1602 0.0281  147 GLN   E O   
8633  C  CB  . GLN   E  148 ? 1.6929 0.6438 1.8282 0.0801  -0.0959 -0.0091 147 GLN   E CB  
8634  C  CG  . GLN   E  148 ? 1.6657 0.8141 1.9581 0.1128  -0.0485 -0.0110 147 GLN   E CG  
8635  C  CD  . GLN   E  148 ? 1.7964 1.0217 2.0023 0.1479  0.0471  -0.0941 147 GLN   E CD  
8636  O  OE1 . GLN   E  148 ? 1.6896 1.3106 2.2392 0.0987  0.1032  0.0705  147 GLN   E OE1 
8637  N  NE2 . GLN   E  148 ? 1.7244 1.1648 2.0640 0.1927  0.0631  -0.0929 147 GLN   E NE2 
8638  N  N   . PRO   E  149 ? 1.7688 0.4500 1.7043 0.1223  -0.1909 0.0903  148 PRO   E N   
8639  C  CA  . PRO   E  149 ? 1.7323 0.4467 1.6898 0.0596  -0.2040 0.0915  148 PRO   E CA  
8640  C  C   . PRO   E  149 ? 1.7953 0.3760 1.6111 -0.0263 -0.1811 0.1066  148 PRO   E C   
8641  O  O   . PRO   E  149 ? 1.7314 0.3910 1.6322 -0.1226 -0.1954 0.2555  148 PRO   E O   
8642  C  CB  . PRO   E  149 ? 1.7495 0.4129 1.7072 0.0994  -0.2004 0.0930  148 PRO   E CB  
8643  C  CG  . PRO   E  149 ? 1.7781 0.4215 1.7684 0.1134  -0.2200 0.0627  148 PRO   E CG  
8644  C  CD  . PRO   E  149 ? 1.7668 0.4608 1.7626 0.1414  -0.2227 0.0799  148 PRO   E CD  
8645  N  N   . SER   E  150 ? 1.7350 0.3105 1.6353 -0.0625 -0.1773 0.0885  149 SER   E N   
8646  C  CA  . SER   E  150 ? 1.7383 0.4623 1.6227 -0.1236 -0.1532 0.0387  149 SER   E CA  
8647  C  C   . SER   E  150 ? 1.7242 0.5624 1.5543 -0.0889 -0.1700 0.0834  149 SER   E C   
8648  O  O   . SER   E  150 ? 1.7297 0.8924 1.5845 -0.1249 -0.1842 0.0855  149 SER   E O   
8649  C  CB  . SER   E  150 ? 1.7080 0.5070 1.6005 -0.1640 -0.1270 0.0355  149 SER   E CB  
8650  O  OG  . SER   E  150 ? 1.7544 0.3953 1.6074 -0.1857 -0.1269 0.0498  149 SER   E OG  
8651  N  N   . GLY   E  151 ? 1.7112 0.5911 1.5384 -0.0910 -0.1485 0.0146  150 GLY   E N   
8652  C  CA  . GLY   E  151 ? 1.7175 0.5819 1.5388 -0.0053 -0.1076 -0.0014 150 GLY   E CA  
8653  C  C   . GLY   E  151 ? 1.7402 0.6668 1.5094 0.0846  -0.0785 -0.0285 150 GLY   E C   
8654  O  O   . GLY   E  151 ? 1.6964 0.7547 1.4825 0.1058  0.0007  0.0777  150 GLY   E O   
8655  N  N   . ASN   E  152 ? 1.7086 0.6329 1.4650 0.0736  -0.0813 0.0103  151 ASN   E N   
8656  C  CA  . ASN   E  152 ? 1.6339 0.6075 1.4915 0.1021  -0.0987 0.0396  151 ASN   E CA  
8657  C  C   . ASN   E  152 ? 1.5866 0.6519 1.4814 0.1411  -0.1347 0.0626  151 ASN   E C   
8658  O  O   . ASN   E  152 ? 1.5358 0.6063 1.5295 0.1152  -0.1139 0.1189  151 ASN   E O   
8659  C  CB  . ASN   E  152 ? 1.6878 0.6346 1.5166 0.1614  -0.0623 0.0369  151 ASN   E CB  
8660  C  CG  . ASN   E  152 ? 1.7172 0.6332 1.4992 0.1823  -0.0828 0.0404  151 ASN   E CG  
8661  O  OD1 . ASN   E  152 ? 1.7234 0.6293 1.5066 0.2406  -0.0303 0.0680  151 ASN   E OD1 
8662  N  ND2 . ASN   E  152 ? 1.8209 0.6541 1.5446 0.1468  -0.0782 0.0620  151 ASN   E ND2 
8663  N  N   . VAL   E  153 ? 1.5651 0.7097 1.4799 0.0646  -0.1415 0.0648  152 VAL   E N   
8664  C  CA  . VAL   E  153 ? 1.5799 0.7489 1.5292 0.0449  -0.1579 0.0531  152 VAL   E CA  
8665  C  C   . VAL   E  153 ? 1.5011 0.7195 1.5298 0.0445  -0.1836 0.0422  152 VAL   E C   
8666  O  O   . VAL   E  153 ? 1.5432 0.7420 1.5006 0.0415  -0.1614 0.0413  152 VAL   E O   
8667  C  CB  . VAL   E  153 ? 1.6388 0.7085 1.5721 -0.0050 -0.1328 0.0902  152 VAL   E CB  
8668  C  CG1 . VAL   E  153 ? 1.6127 0.7938 1.6215 -0.0161 -0.1035 0.1342  152 VAL   E CG1 
8669  C  CG2 . VAL   E  153 ? 1.6560 0.7427 1.5983 -0.0497 -0.1099 0.0867  152 VAL   E CG2 
8670  N  N   . THR   E  154 ? 1.4997 0.6909 1.6053 0.0291  -0.2583 0.0337  153 THR   E N   
8671  C  CA  . THR   E  154 ? 1.4659 0.6917 1.6789 0.0546  -0.2511 0.0160  153 THR   E CA  
8672  C  C   . THR   E  154 ? 1.5288 0.5935 1.7976 0.0303  -0.2250 0.0161  153 THR   E C   
8673  O  O   . THR   E  154 ? 1.6683 0.7042 1.7750 0.0139  -0.2326 0.0049  153 THR   E O   
8674  C  CB  . THR   E  154 ? 1.4050 0.7003 1.7410 0.0327  -0.2609 -0.0458 153 THR   E CB  
8675  O  OG1 . THR   E  154 ? 1.3559 0.7688 1.7939 0.0655  -0.3038 -0.0043 153 THR   E OG1 
8676  C  CG2 . THR   E  154 ? 1.4228 0.7294 1.7558 0.0189  -0.2401 -0.0584 153 THR   E CG2 
8677  N  N   . GLU   E  155 ? 1.6157 0.5372 1.7945 0.0681  -0.2137 0.0121  154 GLU   E N   
8678  C  CA  . GLU   E  155 ? 1.6643 0.5705 1.8820 0.0180  -0.1640 -0.0265 154 GLU   E CA  
8679  C  C   . GLU   E  155 ? 1.7690 0.3903 1.8339 -0.0064 -0.1961 -0.1212 154 GLU   E C   
8680  O  O   . GLU   E  155 ? 1.7943 0.2625 1.8748 0.0549  -0.1782 -0.1504 154 GLU   E O   
8681  C  CB  . GLU   E  155 ? 1.7597 0.7080 1.9117 -0.0409 -0.1298 0.0922  154 GLU   E CB  
8682  C  CG  . GLU   E  155 ? 1.8030 0.8516 1.9683 -0.1177 -0.0982 0.1382  154 GLU   E CG  
8683  C  CD  . GLU   E  155 ? 1.8718 0.8442 1.9716 -0.2460 -0.1049 0.1692  154 GLU   E CD  
8684  O  OE1 . GLU   E  155 ? 2.0228 0.6624 1.9250 -0.2947 -0.0579 0.2119  154 GLU   E OE1 
8685  O  OE2 . GLU   E  155 ? 1.9348 1.0587 2.0393 -0.1424 -0.1057 0.2552  154 GLU   E OE2 
8686  N  N   . LEU   E  156 ? 1.7333 0.4501 1.8654 0.0169  -0.1807 -0.1460 155 LEU   E N   
8687  C  CA  . LEU   E  156 ? 1.7108 0.6367 1.8934 0.0480  -0.1265 -0.1911 155 LEU   E CA  
8688  C  C   . LEU   E  156 ? 1.6644 0.7285 1.8696 0.0467  -0.0562 -0.1563 155 LEU   E C   
8689  O  O   . LEU   E  156 ? 1.7141 0.7241 1.8208 -0.0217 -0.0665 -0.1249 155 LEU   E O   
8690  C  CB  . LEU   E  156 ? 1.8068 0.7241 1.9360 0.0176  -0.1465 -0.1314 155 LEU   E CB  
8691  C  CG  . LEU   E  156 ? 1.8072 0.7576 1.9681 0.0121  -0.1571 -0.1309 155 LEU   E CG  
8692  C  CD1 . LEU   E  156 ? 1.8243 0.7834 1.9811 0.0083  -0.1609 -0.0833 155 LEU   E CD1 
8693  C  CD2 . LEU   E  156 ? 1.8327 0.6926 2.0362 -0.0204 -0.1761 -0.1304 155 LEU   E CD2 
8694  N  N   . TYR   E  157 ? 1.6822 0.8733 1.8514 0.0972  -0.0474 -0.1687 156 TYR   E N   
8695  C  CA  . TYR   E  157 ? 1.6334 0.9170 1.9168 0.1819  -0.0491 -0.1464 156 TYR   E CA  
8696  C  C   . TYR   E  157 ? 1.6385 0.8995 1.9630 0.2156  -0.0512 -0.1181 156 TYR   E C   
8697  O  O   . TYR   E  157 ? 1.6678 0.7352 2.1394 0.2526  -0.0067 -0.2221 156 TYR   E O   
8698  C  CB  . TYR   E  157 ? 1.6485 0.9791 1.8608 0.2109  -0.0493 -0.0879 156 TYR   E CB  
8699  C  CG  . TYR   E  157 ? 1.6290 0.9141 1.9143 0.1883  0.0003  -0.0241 156 TYR   E CG  
8700  C  CD1 . TYR   E  157 ? 1.6025 0.8599 1.8558 0.2793  -0.0036 -0.0205 156 TYR   E CD1 
8701  C  CD2 . TYR   E  157 ? 1.5836 1.0283 1.8522 0.1924  -0.0242 0.0092  156 TYR   E CD2 
8702  C  CE1 . TYR   E  157 ? 1.5791 0.8140 1.8867 0.3160  0.0128  0.0084  156 TYR   E CE1 
8703  C  CE2 . TYR   E  157 ? 1.5459 0.9276 1.9079 0.1939  -0.0159 0.0600  156 TYR   E CE2 
8704  C  CZ  . TYR   E  157 ? 1.5613 0.8844 1.8636 0.2605  -0.0067 0.0488  156 TYR   E CZ  
8705  O  OH  . TYR   E  157 ? 1.6120 1.0003 1.8766 0.2667  0.0366  0.0976  156 TYR   E OH  
8706  N  N   . GLY   E  158 ? 1.6248 0.9201 1.9967 0.1854  -0.0492 -0.1136 157 GLY   E N   
8707  C  CA  . GLY   E  158 ? 1.6321 0.9017 1.9983 0.1637  -0.0470 -0.1086 157 GLY   E CA  
8708  C  C   . GLY   E  158 ? 1.6233 0.8430 1.9532 0.1892  -0.0649 -0.1212 157 GLY   E C   
8709  O  O   . GLY   E  158 ? 1.5856 0.9133 1.9170 0.2578  -0.0926 -0.0770 157 GLY   E O   
8710  N  N   . THR   E  159 ? 1.5861 0.7523 1.9371 0.1664  -0.0719 -0.1598 158 THR   E N   
8711  C  CA  . THR   E  159 ? 1.5741 0.7216 1.9105 0.1777  -0.0976 -0.1519 158 THR   E CA  
8712  C  C   . THR   E  159 ? 1.5684 0.6272 1.9099 0.1534  -0.1113 -0.1534 158 THR   E C   
8713  O  O   . THR   E  159 ? 1.5953 0.6442 1.9383 0.1398  -0.1361 -0.1484 158 THR   E O   
8714  C  CB  . THR   E  159 ? 1.5455 0.6547 1.9110 0.1288  -0.0866 -0.1472 158 THR   E CB  
8715  O  OG1 . THR   E  159 ? 1.5796 0.5886 1.9051 0.1517  -0.1253 -0.1452 158 THR   E OG1 
8716  C  CG2 . THR   E  159 ? 1.5542 0.6887 1.8807 0.1237  -0.0798 -0.1543 158 THR   E CG2 
8717  N  N   . ALA   E  160 ? 1.5948 0.5472 1.8510 0.1802  -0.1338 -0.1738 159 ALA   E N   
8718  C  CA  . ALA   E  160 ? 1.6499 0.5667 1.8485 0.2047  -0.1607 -0.1710 159 ALA   E CA  
8719  C  C   . ALA   E  160 ? 1.7010 0.4767 1.8107 0.1705  -0.1871 -0.1624 159 ALA   E C   
8720  O  O   . ALA   E  160 ? 1.7441 0.4369 1.7915 0.1309  -0.2014 -0.1100 159 ALA   E O   
8721  C  CB  . ALA   E  160 ? 1.6676 0.6181 1.8859 0.2332  -0.1726 -0.1791 159 ALA   E CB  
8722  N  N   . ILE   E  161 ? 1.7423 0.4846 1.7894 0.1410  -0.1867 -0.1108 160 ILE   E N   
8723  C  CA  . ILE   E  161 ? 1.7716 0.4986 1.8183 0.1036  -0.2025 -0.0878 160 ILE   E CA  
8724  C  C   . ILE   E  161 ? 1.8550 0.5497 1.8458 0.1262  -0.2410 -0.0729 160 ILE   E C   
8725  O  O   . ILE   E  161 ? 1.8430 0.4089 1.9515 0.0876  -0.2272 -0.0572 160 ILE   E O   
8726  C  CB  . ILE   E  161 ? 1.7102 0.5929 1.7664 0.1028  -0.2097 -0.0421 160 ILE   E CB  
8727  C  CG1 . ILE   E  161 ? 1.7398 0.6185 1.7424 0.0778  -0.2088 -0.0401 160 ILE   E CG1 
8728  C  CG2 . ILE   E  161 ? 1.6789 0.6289 1.7398 0.0710  -0.2004 -0.0873 160 ILE   E CG2 
8729  C  CD1 . ILE   E  161 ? 1.7147 0.6708 1.7117 0.0783  -0.2008 -0.0078 160 ILE   E CD1 
8730  N  N   . GLY   E  162 ? 1.9096 0.6066 1.8457 0.0838  -0.2520 -0.0441 161 GLY   E N   
8731  C  CA  . GLY   E  162 ? 1.9409 0.6757 1.8694 0.0912  -0.2681 -0.0058 161 GLY   E CA  
8732  C  C   . GLY   E  162 ? 1.9835 0.6849 1.9017 0.0995  -0.2943 -0.0298 161 GLY   E C   
8733  O  O   . GLY   E  162 ? 2.0171 0.7111 1.8856 0.0374  -0.3783 -0.0389 161 GLY   E O   
8734  N  N   . ALA   E  163 ? 1.9805 0.7513 2.0050 0.1397  -0.3006 0.0524  162 ALA   E N   
8735  C  CA  . ALA   E  163 ? 1.9482 0.7901 2.0505 0.1997  -0.3117 0.1023  162 ALA   E CA  
8736  C  C   . ALA   E  163 ? 1.9585 0.7671 2.0896 0.2546  -0.3002 0.0756  162 ALA   E C   
8737  O  O   . ALA   E  163 ? 1.9572 0.6554 2.1960 0.2801  -0.3086 0.1053  162 ALA   E O   
8738  C  CB  . ALA   E  163 ? 1.9398 0.8266 2.0703 0.2210  -0.2938 0.1420  162 ALA   E CB  
8739  N  N   . ARG   E  164 ? 1.9693 0.8340 2.0917 0.2477  -0.2763 0.0419  163 ARG   E N   
8740  C  CA  . ARG   E  164 ? 2.0074 0.9785 2.1459 0.2438  -0.2301 0.0069  163 ARG   E CA  
8741  C  C   . ARG   E  164 ? 1.9231 0.9036 2.1909 0.3712  -0.2596 0.0348  163 ARG   E C   
8742  O  O   . ARG   E  164 ? 1.9436 0.9592 2.2947 0.3513  -0.2252 0.0322  163 ARG   E O   
8743  C  CB  . ARG   E  164 ? 2.0365 1.2257 2.1077 0.2206  -0.2634 0.0026  163 ARG   E CB  
8744  C  CG  . ARG   E  164 ? 2.1730 1.2823 2.1357 0.0937  -0.2212 0.0226  163 ARG   E CG  
8745  C  CD  . ARG   E  164 ? 2.2622 1.5295 2.1072 0.0438  -0.2565 -0.0089 163 ARG   E CD  
8746  N  NE  . ARG   E  164 ? 2.3574 1.6102 2.0990 -0.0255 -0.2308 -0.0416 163 ARG   E NE  
8747  C  CZ  . ARG   E  164 ? 2.4042 1.6534 2.0677 -0.0060 -0.1892 -0.0759 163 ARG   E CZ  
8748  N  NH1 . ARG   E  164 ? 2.3772 1.7506 2.0767 0.0397  -0.2436 -0.0769 163 ARG   E NH1 
8749  N  NH2 . ARG   E  164 ? 2.4879 1.5919 2.0200 -0.0132 -0.1884 -0.1201 163 ARG   E NH2 
8750  N  N   . SER   E  165 ? 1.8436 0.9215 2.1768 0.3692  -0.2396 -0.0035 164 SER   E N   
8751  C  CA  . SER   E  165 ? 1.7084 0.8083 2.1315 0.4258  -0.2562 -0.0804 164 SER   E CA  
8752  C  C   . SER   E  165 ? 1.7610 0.9077 2.1017 0.3662  -0.2572 -0.0840 164 SER   E C   
8753  O  O   . SER   E  165 ? 1.8296 0.7916 2.1155 0.3080  -0.2389 -0.1994 164 SER   E O   
8754  C  CB  . SER   E  165 ? 1.7144 0.7061 2.1342 0.4057  -0.2438 -0.0824 164 SER   E CB  
8755  O  OG  . SER   E  165 ? 1.5467 0.4681 2.2118 0.5884  -0.2334 -0.0863 164 SER   E OG  
8756  N  N   . GLN   E  166 ? 1.7325 0.8721 2.0238 0.3964  -0.2779 -0.0405 165 GLN   E N   
8757  C  CA  . GLN   E  166 ? 1.7648 0.7998 2.0491 0.3666  -0.2718 -0.0634 165 GLN   E CA  
8758  C  C   . GLN   E  166 ? 1.7652 0.6585 2.0713 0.3685  -0.2920 -0.0757 165 GLN   E C   
8759  O  O   . GLN   E  166 ? 1.8062 0.6578 2.0976 0.3365  -0.2462 -0.1318 165 GLN   E O   
8760  C  CB  . GLN   E  166 ? 1.7413 0.8865 2.0850 0.2658  -0.2962 0.0048  165 GLN   E CB  
8761  C  CG  . GLN   E  166 ? 1.7683 1.1364 2.0565 0.2136  -0.2934 0.0042  165 GLN   E CG  
8762  C  CD  . GLN   E  166 ? 1.7131 1.2280 2.0366 0.2061  -0.3229 0.0084  165 GLN   E CD  
8763  O  OE1 . GLN   E  166 ? 1.7018 1.2518 1.9954 0.1452  -0.3844 -0.0291 165 GLN   E OE1 
8764  N  NE2 . GLN   E  166 ? 1.7026 1.2933 2.0116 0.1853  -0.2936 0.0420  165 GLN   E NE2 
8765  N  N   . GLY   E  167 ? 1.7625 0.6068 2.0352 0.3487  -0.2671 -0.0660 166 GLY   E N   
8766  C  CA  . GLY   E  167 ? 1.7570 0.7748 2.0654 0.3274  -0.2612 -0.0800 166 GLY   E CA  
8767  C  C   . GLY   E  167 ? 1.6728 0.8695 2.0510 0.2481  -0.2373 -0.0930 166 GLY   E C   
8768  O  O   . GLY   E  167 ? 1.7274 1.1480 2.0237 0.2266  -0.2342 -0.0993 166 GLY   E O   
8769  N  N   . ALA   E  168 ? 1.5756 0.8725 2.0540 0.2164  -0.2396 -0.1049 167 ALA   E N   
8770  C  CA  . ALA   E  168 ? 1.4970 0.8708 2.0637 0.2375  -0.2488 -0.0655 167 ALA   E CA  
8771  C  C   . ALA   E  168 ? 1.4794 0.8608 2.0444 0.2172  -0.2399 -0.0839 167 ALA   E C   
8772  O  O   . ALA   E  168 ? 1.4138 1.0219 1.9943 0.1794  -0.2486 -0.1084 167 ALA   E O   
8773  C  CB  . ALA   E  168 ? 1.4416 0.8399 2.0377 0.2455  -0.2462 -0.0245 167 ALA   E CB  
8774  N  N   . LYS   E  169 ? 1.4881 0.8866 2.1213 0.1757  -0.2038 -0.1289 168 LYS   E N   
8775  C  CA  . LYS   E  169 ? 1.5300 1.0760 2.1131 0.1865  -0.1987 -0.1245 168 LYS   E CA  
8776  C  C   . LYS   E  169 ? 1.5333 1.0811 2.2129 0.1953  -0.1251 -0.1336 168 LYS   E C   
8777  O  O   . LYS   E  169 ? 1.5181 1.1675 2.1873 0.1633  -0.0555 -0.1418 168 LYS   E O   
8778  C  CB  . LYS   E  169 ? 1.5219 1.1631 2.1574 0.1924  -0.1990 -0.1373 168 LYS   E CB  
8779  C  CG  . LYS   E  169 ? 1.4233 1.3241 2.1669 0.2328  -0.1985 -0.1628 168 LYS   E CG  
8780  C  CD  . LYS   E  169 ? 1.4170 1.4086 2.1616 0.2588  -0.1868 -0.1475 168 LYS   E CD  
8781  C  CE  . LYS   E  169 ? 1.3650 1.4745 2.1544 0.2451  -0.1671 -0.1100 168 LYS   E CE  
8782  N  NZ  . LYS   E  169 ? 1.3636 1.5365 2.1288 0.2068  -0.1867 -0.0648 168 LYS   E NZ  
8783  N  N   . THR   E  170 ? 1.5862 1.0833 2.2566 0.1880  -0.1321 -0.0478 169 THR   E N   
8784  C  CA  . THR   E  170 ? 1.7081 1.1236 2.2236 0.1589  -0.1258 -0.0920 169 THR   E CA  
8785  C  C   . THR   E  170 ? 1.7030 1.2334 2.2981 0.1432  -0.1395 -0.0419 169 THR   E C   
8786  O  O   . THR   E  170 ? 1.7211 1.3600 2.2314 0.1358  -0.1936 -0.0680 169 THR   E O   
8787  C  CB  . THR   E  170 ? 1.7403 1.0678 2.2514 0.0738  -0.1223 -0.1465 169 THR   E CB  
8788  O  OG1 . THR   E  170 ? 1.7727 1.0395 2.2754 0.0424  -0.1080 -0.2194 169 THR   E OG1 
8789  C  CG2 . THR   E  170 ? 1.7732 1.0327 2.2491 0.1077  -0.1247 -0.1274 169 THR   E CG2 
8790  N  N   . TYR   E  171 ? 1.7715 1.2259 2.3182 0.2211  -0.1886 -0.0353 170 TYR   E N   
8791  C  CA  . TYR   E  171 ? 1.7411 1.1461 2.3188 0.2825  -0.1947 -0.0841 170 TYR   E CA  
8792  C  C   . TYR   E  171 ? 1.7961 1.1570 2.2974 0.3014  -0.1641 -0.0823 170 TYR   E C   
8793  O  O   . TYR   E  171 ? 1.7557 1.1925 2.2960 0.3147  -0.1761 -0.0805 170 TYR   E O   
8794  C  CB  . TYR   E  171 ? 1.7286 1.1367 2.3119 0.3596  -0.1915 -0.0924 170 TYR   E CB  
8795  C  CG  . TYR   E  171 ? 1.6178 1.1911 2.3318 0.4097  -0.1771 -0.1121 170 TYR   E CG  
8796  C  CD1 . TYR   E  171 ? 1.6156 1.2035 2.3209 0.3862  -0.1672 -0.1693 170 TYR   E CD1 
8797  C  CD2 . TYR   E  171 ? 1.6227 1.2417 2.3438 0.4344  -0.1626 -0.1085 170 TYR   E CD2 
8798  C  CE1 . TYR   E  171 ? 1.5437 1.2579 2.3309 0.4113  -0.1675 -0.2064 170 TYR   E CE1 
8799  C  CE2 . TYR   E  171 ? 1.5503 1.2091 2.3389 0.4961  -0.1516 -0.1677 170 TYR   E CE2 
8800  C  CZ  . TYR   E  171 ? 1.5463 1.1844 2.3628 0.4146  -0.1632 -0.2007 170 TYR   E CZ  
8801  O  OH  . TYR   E  171 ? 1.4793 1.1190 2.4358 0.4622  -0.1133 -0.1991 170 TYR   E OH  
8802  N  N   . LEU   E  172 ? 1.8716 1.1184 2.2222 0.3129  -0.1245 -0.0539 171 LEU   E N   
8803  C  CA  . LEU   E  172 ? 1.9233 1.1102 2.1361 0.2442  -0.0802 -0.0346 171 LEU   E CA  
8804  C  C   . LEU   E  172 ? 1.8991 1.0711 2.1182 0.2816  -0.0400 0.0179  171 LEU   E C   
8805  O  O   . LEU   E  172 ? 1.8305 1.2040 2.1345 0.1895  0.0389  -0.0127 171 LEU   E O   
8806  C  CB  . LEU   E  172 ? 1.9496 1.0480 1.9962 0.2145  -0.0988 -0.0525 171 LEU   E CB  
8807  C  CG  . LEU   E  172 ? 1.9784 1.0978 1.9828 0.2280  -0.0600 -0.0754 171 LEU   E CG  
8808  C  CD1 . LEU   E  172 ? 1.9110 1.0627 1.9211 0.2080  -0.1123 -0.0652 171 LEU   E CD1 
8809  C  CD2 . LEU   E  172 ? 2.0249 1.1868 1.9673 0.1710  -0.0375 -0.0816 171 LEU   E CD2 
8810  N  N   . GLU   E  173 ? 1.8988 1.0016 2.1400 0.3188  -0.0334 0.0418  172 GLU   E N   
8811  C  CA  . GLU   E  173 ? 1.9142 1.0416 2.1364 0.3505  -0.0283 0.0527  172 GLU   E CA  
8812  C  C   . GLU   E  173 ? 1.9237 1.1289 2.1787 0.3489  -0.0080 0.0411  172 GLU   E C   
8813  O  O   . GLU   E  173 ? 1.9975 1.1148 2.1189 0.3298  0.0487  -0.0535 172 GLU   E O   
8814  C  CB  . GLU   E  173 ? 1.9403 1.0726 2.1919 0.3209  -0.0586 0.1006  172 GLU   E CB  
8815  C  CG  . GLU   E  173 ? 1.9839 1.1367 2.2113 0.3689  -0.0772 0.1546  172 GLU   E CG  
8816  C  CD  . GLU   E  173 ? 1.9934 1.2465 2.2815 0.3421  -0.0554 0.1976  172 GLU   E CD  
8817  O  OE1 . GLU   E  173 ? 1.9977 1.1907 2.3445 0.4214  -0.0627 0.2267  172 GLU   E OE1 
8818  O  OE2 . GLU   E  173 ? 2.0559 1.5211 2.2200 0.3766  -0.1019 0.2959  172 GLU   E OE2 
8819  N  N   . ARG   E  174 ? 1.9072 1.2084 2.2254 0.3945  0.0125  0.0623  173 ARG   E N   
8820  C  CA  . ARG   E  174 ? 1.9025 1.2715 2.2737 0.4637  -0.0018 0.0485  173 ARG   E CA  
8821  C  C   . ARG   E  174 ? 1.7862 1.3048 2.2834 0.4627  0.0546  0.1551  173 ARG   E C   
8822  O  O   . ARG   E  174 ? 1.7351 1.3458 2.3589 0.4841  0.1006  0.1470  173 ARG   E O   
8823  C  CB  . ARG   E  174 ? 1.9254 1.4068 2.2741 0.5950  -0.0481 -0.0099 173 ARG   E CB  
8824  C  CG  . ARG   E  174 ? 1.9907 1.5027 2.2901 0.5848  -0.0658 -0.2028 173 ARG   E CG  
8825  C  CD  . ARG   E  174 ? 2.0995 1.5287 2.2988 0.6793  -0.0731 -0.2473 173 ARG   E CD  
8826  N  NE  . ARG   E  174 ? 2.1128 1.6806 2.3490 0.6554  -0.0491 -0.3180 173 ARG   E NE  
8827  C  CZ  . ARG   E  174 ? 2.0788 1.6725 2.3713 0.6279  -0.0506 -0.3138 173 ARG   E CZ  
8828  N  NH1 . ARG   E  174 ? 2.1060 1.5412 2.3266 0.5868  -0.1155 -0.3540 173 ARG   E NH1 
8829  N  NH2 . ARG   E  174 ? 2.0717 1.7354 2.3326 0.5866  -0.0828 -0.3116 173 ARG   E NH2 
8830  N  N   . THR   E  175 ? 1.8086 1.2607 2.2824 0.4313  0.0040  0.1736  174 THR   E N   
8831  C  CA  . THR   E  175 ? 1.7539 1.3388 2.3362 0.3901  -0.0148 0.2041  174 THR   E CA  
8832  C  C   . THR   E  175 ? 1.6701 1.2917 2.3362 0.3419  -0.0067 0.1836  174 THR   E C   
8833  O  O   . THR   E  175 ? 1.5982 1.2615 2.3905 0.3649  0.0250  0.2370  174 THR   E O   
8834  C  CB  . THR   E  175 ? 1.7405 1.2706 2.3079 0.4074  -0.0882 0.3491  174 THR   E CB  
8835  O  OG1 . THR   E  175 ? 1.7908 1.2381 2.3323 0.5460  -0.1130 0.3357  174 THR   E OG1 
8836  C  CG2 . THR   E  175 ? 1.6921 1.4258 2.3365 0.4085  -0.1243 0.3620  174 THR   E CG2 
8837  N  N   . LEU   E  176 ? 1.7257 1.2543 2.2757 0.3166  -0.0260 0.1175  175 LEU   E N   
8838  C  CA  . LEU   E  176 ? 1.7291 1.1244 2.1938 0.2551  -0.0293 0.0416  175 LEU   E CA  
8839  C  C   . LEU   E  176 ? 1.6976 1.2314 2.1525 0.2319  0.0258  -0.0034 175 LEU   E C   
8840  O  O   . LEU   E  176 ? 1.7780 1.2582 2.2109 0.1864  0.0213  -0.0532 175 LEU   E O   
8841  C  CB  . LEU   E  176 ? 1.7255 1.0175 2.1982 0.2688  -0.0305 0.0385  175 LEU   E CB  
8842  C  CG  . LEU   E  176 ? 1.7101 0.9028 2.1883 0.2360  -0.0116 -0.0001 175 LEU   E CG  
8843  C  CD1 . LEU   E  176 ? 1.7035 0.9669 2.1198 0.2311  -0.0113 0.0147  175 LEU   E CD1 
8844  C  CD2 . LEU   E  176 ? 1.7222 0.7868 2.1732 0.2576  -0.0057 -0.0185 175 LEU   E CD2 
8845  N  N   . ASP   E  177 ? 1.6662 1.3222 2.0932 0.2060  0.0048  -0.0161 176 ASP   E N   
8846  C  CA  . ASP   E  177 ? 1.6227 1.3495 2.0508 0.1853  -0.0138 -0.0449 176 ASP   E CA  
8847  C  C   . ASP   E  177 ? 1.6432 1.2863 2.0823 0.1280  0.0632  -0.1135 176 ASP   E C   
8848  O  O   . ASP   E  177 ? 1.6213 1.3576 2.0460 0.0464  0.0885  -0.1181 176 ASP   E O   
8849  C  CB  . ASP   E  177 ? 1.6019 1.4034 2.0204 0.2461  -0.0356 -0.0149 176 ASP   E CB  
8850  C  CG  . ASP   E  177 ? 1.6136 1.4475 2.0071 0.2690  -0.0773 0.0314  176 ASP   E CG  
8851  O  OD1 . ASP   E  177 ? 1.7225 1.3872 2.0240 0.2847  -0.0914 0.0451  176 ASP   E OD1 
8852  O  OD2 . ASP   E  177 ? 1.5426 1.4353 1.9508 0.2839  -0.1249 0.0827  176 ASP   E OD2 
8853  N  N   . THR   E  178 ? 1.6814 1.1887 2.0678 0.1589  0.0918  -0.1473 177 THR   E N   
8854  C  CA  . THR   E  178 ? 1.6675 1.2271 2.0763 0.1753  0.0977  -0.1728 177 THR   E CA  
8855  C  C   . THR   E  178 ? 1.7209 1.3444 2.0248 0.2157  0.1045  -0.1973 177 THR   E C   
8856  O  O   . THR   E  178 ? 1.7424 1.3847 1.9080 0.1819  0.1341  -0.1394 177 THR   E O   
8857  C  CB  . THR   E  178 ? 1.6054 1.1146 2.1054 0.2016  0.1231  -0.2409 177 THR   E CB  
8858  O  OG1 . THR   E  178 ? 1.5813 1.2166 2.1270 0.2049  0.1717  -0.2840 177 THR   E OG1 
8859  C  CG2 . THR   E  178 ? 1.5851 1.0760 2.1101 0.2254  0.1316  -0.2623 177 THR   E CG2 
8860  N  N   . PHE   E  179 ? 1.6922 1.3961 2.0596 0.2074  0.0955  -0.2039 178 PHE   E N   
8861  C  CA  . PHE   E  179 ? 1.6824 1.3107 2.1293 0.2438  0.0666  -0.2163 178 PHE   E CA  
8862  C  C   . PHE   E  179 ? 1.7049 1.2815 2.1294 0.2313  0.0689  -0.2018 178 PHE   E C   
8863  O  O   . PHE   E  179 ? 1.6423 1.1981 2.1960 0.2045  0.0810  -0.1595 178 PHE   E O   
8864  C  CB  . PHE   E  179 ? 1.6667 1.3141 2.1158 0.2110  0.0814  -0.2705 178 PHE   E CB  
8865  C  CG  . PHE   E  179 ? 1.7178 1.2094 2.0699 0.1478  0.0707  -0.3207 178 PHE   E CG  
8866  C  CD1 . PHE   E  179 ? 1.7118 1.1844 2.0519 0.1289  0.0650  -0.3792 178 PHE   E CD1 
8867  C  CD2 . PHE   E  179 ? 1.7845 1.1604 2.1005 0.1598  0.0787  -0.2562 178 PHE   E CD2 
8868  C  CE1 . PHE   E  179 ? 1.6947 1.1851 2.0327 0.1511  0.0722  -0.3765 178 PHE   E CE1 
8869  C  CE2 . PHE   E  179 ? 1.7885 1.1621 2.0976 0.1894  0.0549  -0.2378 178 PHE   E CE2 
8870  C  CZ  . PHE   E  179 ? 1.7545 1.1531 2.0459 0.1674  0.0705  -0.3257 178 PHE   E CZ  
8871  N  N   . ILE   E  180 ? 1.7678 1.1436 2.1346 0.3093  0.0370  -0.2028 179 ILE   E N   
8872  C  CA  . ILE   E  180 ? 1.7812 1.1913 2.1353 0.3285  -0.0047 -0.1948 179 ILE   E CA  
8873  C  C   . ILE   E  180 ? 1.7416 1.2760 2.2283 0.3063  -0.0145 -0.1270 179 ILE   E C   
8874  O  O   . ILE   E  180 ? 1.7620 1.2581 2.2810 0.2879  -0.0143 -0.1399 179 ILE   E O   
8875  C  CB  . ILE   E  180 ? 1.8264 1.1743 2.1234 0.3660  -0.0099 -0.2301 179 ILE   E CB  
8876  C  CG1 . ILE   E  180 ? 1.7419 1.3091 2.0798 0.3826  -0.0169 -0.2476 179 ILE   E CG1 
8877  C  CG2 . ILE   E  180 ? 1.8368 1.1486 2.0818 0.3951  -0.0388 -0.2141 179 ILE   E CG2 
8878  C  CD1 . ILE   E  180 ? 1.7162 1.3869 2.1040 0.3458  -0.0002 -0.2644 179 ILE   E CD1 
8879  N  N   . LYS   E  181 ? 1.7145 1.2588 2.2731 0.2527  -0.0005 -0.0397 180 LYS   E N   
8880  C  CA  . LYS   E  181 ? 1.7562 1.2785 2.2812 0.2400  0.0026  0.0290  180 LYS   E CA  
8881  C  C   . LYS   E  181 ? 1.6752 1.2529 2.3247 0.2081  0.0050  0.0553  180 LYS   E C   
8882  O  O   . LYS   E  181 ? 1.7065 1.1593 2.3341 0.2127  0.0288  0.0799  180 LYS   E O   
8883  C  CB  . LYS   E  181 ? 1.8456 1.2443 2.2297 0.2218  -0.0037 0.0318  180 LYS   E CB  
8884  C  CG  . LYS   E  181 ? 1.9069 1.2195 2.1908 0.2033  0.0050  0.0092  180 LYS   E CG  
8885  C  CD  . LYS   E  181 ? 1.9796 1.2228 2.1572 0.2123  -0.0038 -0.0014 180 LYS   E CD  
8886  C  CE  . LYS   E  181 ? 2.0289 1.2884 2.1968 0.2431  -0.0299 0.0619  180 LYS   E CE  
8887  N  NZ  . LYS   E  181 ? 2.1183 1.4404 2.1501 0.1954  -0.0282 0.0523  180 LYS   E NZ  
8888  N  N   . ILE   E  182 ? 1.6286 1.2730 2.3301 0.1934  -0.0080 0.0669  181 ILE   E N   
8889  C  CA  . ILE   E  182 ? 1.5939 1.3205 2.3869 0.1710  -0.0496 0.0732  181 ILE   E CA  
8890  C  C   . ILE   E  182 ? 1.5308 1.2762 2.3609 0.1368  -0.0580 0.1561  181 ILE   E C   
8891  O  O   . ILE   E  182 ? 1.4155 1.2431 2.3576 0.0779  -0.0893 0.2655  181 ILE   E O   
8892  C  CB  . ILE   E  182 ? 1.6147 1.2808 2.4129 0.2308  -0.0728 0.0725  181 ILE   E CB  
8893  C  CG1 . ILE   E  182 ? 1.6007 1.3052 2.4787 0.2650  -0.0909 0.0522  181 ILE   E CG1 
8894  C  CG2 . ILE   E  182 ? 1.6073 1.3353 2.4420 0.2404  -0.0987 0.0629  181 ILE   E CG2 
8895  C  CD1 . ILE   E  182 ? 1.6109 1.2450 2.4941 0.2921  -0.1084 0.0401  181 ILE   E CD1 
8896  N  N   . ASP   E  183 ? 1.4642 1.2869 2.3465 0.1505  -0.0374 0.1467  182 ASP   E N   
8897  C  CA  . ASP   E  183 ? 1.4146 1.2917 2.3232 0.1417  -0.0116 0.0712  182 ASP   E CA  
8898  C  C   . ASP   E  183 ? 1.3467 1.2690 2.3110 0.2043  0.0035  0.0412  182 ASP   E C   
8899  O  O   . ASP   E  183 ? 1.3746 1.1663 2.3084 0.3096  -0.0441 0.0200  182 ASP   E O   
8900  C  CB  . ASP   E  183 ? 1.4233 1.3206 2.3073 0.0883  0.0203  0.0737  182 ASP   E CB  
8901  C  CG  . ASP   E  183 ? 1.4237 1.3244 2.2851 0.0326  0.0606  0.0973  182 ASP   E CG  
8902  O  OD1 . ASP   E  183 ? 1.3652 1.3533 2.3182 0.0013  0.0476  0.0221  182 ASP   E OD1 
8903  O  OD2 . ASP   E  183 ? 1.5410 1.3618 2.2849 0.0200  0.0703  0.1655  182 ASP   E OD2 
8904  N  N   . GLY   E  184 ? 1.3992 1.3728 2.2659 0.1862  0.0226  0.0051  183 GLY   E N   
8905  C  CA  . GLY   E  184 ? 1.4267 1.4680 2.2706 0.1383  0.0393  -0.0228 183 GLY   E CA  
8906  C  C   . GLY   E  184 ? 1.4970 1.4005 2.2854 0.1311  0.0581  0.0097  183 GLY   E C   
8907  O  O   . GLY   E  184 ? 1.5446 1.5470 2.3555 0.0627  0.0742  -0.0773 183 GLY   E O   
8908  N  N   . ASN   E  185 ? 1.5626 1.3760 2.3091 0.0994  0.0603  -0.0222 184 ASN   E N   
8909  C  CA  . ASN   E  185 ? 1.6055 1.3505 2.2992 0.0160  0.0626  0.0248  184 ASN   E CA  
8910  C  C   . ASN   E  185 ? 1.6726 1.2859 2.2976 -0.0826 0.0577  -0.0476 184 ASN   E C   
8911  O  O   . ASN   E  185 ? 1.6480 1.3478 2.2129 -0.1872 0.1279  -0.0273 184 ASN   E O   
8912  C  CB  . ASN   E  185 ? 1.6012 1.3532 2.3215 0.0486  0.0581  0.0575  184 ASN   E CB  
8913  C  CG  . ASN   E  185 ? 1.5821 1.3006 2.3903 0.1005  0.0784  0.0708  184 ASN   E CG  
8914  O  OD1 . ASN   E  185 ? 1.5181 1.1926 2.3893 0.0455  0.0865  0.1142  184 ASN   E OD1 
8915  N  ND2 . ASN   E  185 ? 1.6209 1.3525 2.3793 0.1142  0.0027  0.0958  184 ASN   E ND2 
8916  N  N   . PRO   E  186 ? 1.7406 1.1785 2.3419 -0.0816 0.0078  -0.1051 185 PRO   E N   
8917  C  CA  . PRO   E  186 ? 1.7065 1.2001 2.3218 -0.1042 -0.0161 -0.1521 185 PRO   E CA  
8918  C  C   . PRO   E  186 ? 1.7437 1.2317 2.3952 -0.0295 -0.1307 -0.2150 185 PRO   E C   
8919  O  O   . PRO   E  186 ? 1.7820 1.1779 2.3445 0.0091  -0.2074 -0.3339 185 PRO   E O   
8920  C  CB  . PRO   E  186 ? 1.6983 1.0836 2.3599 -0.0758 -0.0424 -0.1244 185 PRO   E CB  
8921  C  CG  . PRO   E  186 ? 1.6851 1.1410 2.3210 -0.0692 -0.0150 -0.0871 185 PRO   E CG  
8922  C  CD  . PRO   E  186 ? 1.7185 1.1715 2.3338 -0.0702 0.0084  -0.0996 185 PRO   E CD  
8923  N  N   . ASP   E  187 ? 1.7580 1.3106 2.4392 0.0727  -0.1590 -0.2508 186 ASP   E N   
8924  C  CA  . ASP   E  187 ? 1.7358 1.3664 2.4374 0.0862  -0.2191 -0.2470 186 ASP   E CA  
8925  C  C   . ASP   E  187 ? 1.8161 1.5069 2.3541 0.0410  -0.2174 -0.3080 186 ASP   E C   
8926  O  O   . ASP   E  187 ? 1.9427 1.6260 2.4746 -0.1019 -0.2683 -0.2144 186 ASP   E O   
8927  C  CB  . ASP   E  187 ? 1.7512 1.2723 2.4015 0.1168  -0.2240 -0.3551 186 ASP   E CB  
8928  C  CG  . ASP   E  187 ? 1.7226 1.2465 2.4314 0.1382  -0.2706 -0.3747 186 ASP   E CG  
8929  O  OD1 . ASP   E  187 ? 1.6914 1.2529 2.3775 0.1298  -0.3418 -0.3824 186 ASP   E OD1 
8930  O  OD2 . ASP   E  187 ? 1.7081 1.2742 2.4557 0.2169  -0.2679 -0.4384 186 ASP   E OD2 
8931  N  N   . GLU   E  188 ? 1.7657 1.5226 2.3666 0.0157  -0.2161 -0.2282 187 GLU   E N   
8932  C  CA  . GLU   E  188 ? 1.7347 1.4751 2.3577 0.0280  -0.2088 -0.2000 187 GLU   E CA  
8933  C  C   . GLU   E  188 ? 1.7340 1.2932 2.2829 0.0633  -0.2025 -0.1925 187 GLU   E C   
8934  O  O   . GLU   E  188 ? 1.8013 1.2859 2.2881 0.1309  -0.1076 -0.2462 187 GLU   E O   
8935  C  CB  . GLU   E  188 ? 1.6746 1.4933 2.3513 0.0362  -0.2115 -0.2358 187 GLU   E CB  
8936  C  CG  . GLU   E  188 ? 1.6764 1.4853 2.3652 0.0668  -0.2475 -0.2456 187 GLU   E CG  
8937  C  CD  . GLU   E  188 ? 1.6462 1.4253 2.3578 0.0320  -0.2952 -0.3118 187 GLU   E CD  
8938  O  OE1 . GLU   E  188 ? 1.7340 1.5013 2.4102 0.0911  -0.3478 -0.2236 187 GLU   E OE1 
8939  O  OE2 . GLU   E  188 ? 1.5621 1.4013 2.3369 0.0568  -0.3213 -0.2838 187 GLU   E OE2 
8940  N  N   . LEU   E  189 ? 1.7339 1.3188 2.2174 0.0633  -0.2686 -0.1366 188 LEU   E N   
8941  C  CA  . LEU   E  189 ? 1.7628 1.2152 2.1269 0.0732  -0.3231 -0.1504 188 LEU   E CA  
8942  C  C   . LEU   E  189 ? 1.7403 1.2235 2.1331 0.0178  -0.3684 -0.1381 188 LEU   E C   
8943  O  O   . LEU   E  189 ? 1.7829 1.3100 2.1616 -0.0289 -0.4469 -0.1546 188 LEU   E O   
8944  C  CB  . LEU   E  189 ? 1.7630 1.2302 2.0559 0.1020  -0.3228 -0.1896 188 LEU   E CB  
8945  C  CG  . LEU   E  189 ? 1.7475 1.1575 2.0314 0.1094  -0.3036 -0.2101 188 LEU   E CG  
8946  C  CD1 . LEU   E  189 ? 1.7456 1.2281 1.9668 0.1412  -0.2950 -0.2490 188 LEU   E CD1 
8947  C  CD2 . LEU   E  189 ? 1.7539 1.1109 2.0229 0.1395  -0.3226 -0.1708 188 LEU   E CD2 
8948  N  N   . ILE   E  190 ? 1.7099 1.2721 2.0490 0.0494  -0.3276 -0.0501 189 ILE   E N   
8949  C  CA  . ILE   E  190 ? 1.6758 1.2754 2.0465 0.0413  -0.3184 -0.0532 189 ILE   E CA  
8950  C  C   . ILE   E  190 ? 1.6796 1.2830 2.0299 0.0478  -0.2752 -0.0458 189 ILE   E C   
8951  O  O   . ILE   E  190 ? 1.6712 1.2702 1.9346 0.0224  -0.2738 -0.1623 189 ILE   E O   
8952  C  CB  . ILE   E  190 ? 1.6685 1.2309 2.0360 0.0522  -0.3510 -0.0223 189 ILE   E CB  
8953  C  CG1 . ILE   E  190 ? 1.6297 1.2085 1.9905 0.0329  -0.3991 -0.0350 189 ILE   E CG1 
8954  C  CG2 . ILE   E  190 ? 1.7089 1.2452 2.0313 0.0555  -0.3735 -0.0119 189 ILE   E CG2 
8955  C  CD1 . ILE   E  190 ? 1.6433 1.1947 1.9965 0.0456  -0.4032 -0.0392 189 ILE   E CD1 
8956  N  N   . LYS   E  191 ? 1.6819 1.3480 2.1013 0.0697  -0.2667 0.0206  190 LYS   E N   
8957  C  CA  . LYS   E  191 ? 1.6286 1.4074 2.1691 0.1086  -0.2962 0.1004  190 LYS   E CA  
8958  C  C   . LYS   E  191 ? 1.6271 1.3086 2.2895 0.1186  -0.2738 0.0809  190 LYS   E C   
8959  O  O   . LYS   E  191 ? 1.6507 1.3112 2.2826 0.1220  -0.3112 0.0929  190 LYS   E O   
8960  C  CB  . LYS   E  191 ? 1.6191 1.4902 2.1535 0.0772  -0.3230 0.1356  190 LYS   E CB  
8961  C  CG  . LYS   E  191 ? 1.5599 1.5792 2.1735 0.0018  -0.3036 0.1713  190 LYS   E CG  
8962  C  CD  . LYS   E  191 ? 1.5672 1.7081 2.1565 -0.0277 -0.2997 0.1922  190 LYS   E CD  
8963  C  CE  . LYS   E  191 ? 1.5604 1.8076 2.1414 -0.0588 -0.2958 0.2053  190 LYS   E CE  
8964  N  NZ  . LYS   E  191 ? 1.5512 1.8521 2.1276 -0.0740 -0.3184 0.2097  190 LYS   E NZ  
8965  N  N   . ALA   E  192 ? 1.5923 1.3327 2.3295 0.1494  -0.2386 0.1322  191 ALA   E N   
8966  C  CA  . ALA   E  192 ? 1.5429 1.2503 2.3794 0.1662  -0.2130 0.1295  191 ALA   E CA  
8967  C  C   . ALA   E  192 ? 1.5827 1.0451 2.3657 0.1460  -0.2240 0.1503  191 ALA   E C   
8968  O  O   . ALA   E  192 ? 1.5919 0.9634 2.5256 0.1549  -0.2375 0.2709  191 ALA   E O   
8969  C  CB  . ALA   E  192 ? 1.4873 1.3441 2.3679 0.1948  -0.1851 0.1507  191 ALA   E CB  
8970  N  N   . GLY   E  193 ? 1.5866 1.0497 2.2438 0.1185  -0.2485 0.1398  192 GLY   E N   
8971  C  CA  . GLY   E  193 ? 1.5630 0.9212 2.1181 0.1514  -0.2717 0.0674  192 GLY   E CA  
8972  C  C   . GLY   E  193 ? 1.5945 0.8412 2.0845 0.1441  -0.2568 0.0191  192 GLY   E C   
8973  O  O   . GLY   E  193 ? 1.5618 0.7505 2.0202 0.1672  -0.2773 -0.0767 192 GLY   E O   
8974  N  N   . VAL   E  194 ? 1.6361 0.8677 2.0445 0.1883  -0.2845 0.0439  193 VAL   E N   
8975  C  CA  . VAL   E  194 ? 1.6225 0.9070 2.0447 0.1995  -0.3112 0.0483  193 VAL   E CA  
8976  C  C   . VAL   E  194 ? 1.6497 0.9499 2.0595 0.2939  -0.3148 0.0699  193 VAL   E C   
8977  O  O   . VAL   E  194 ? 1.6773 0.9404 2.1118 0.3394  -0.2886 0.0941  193 VAL   E O   
8978  C  CB  . VAL   E  194 ? 1.6458 0.8540 2.0338 0.1709  -0.2933 0.0354  193 VAL   E CB  
8979  C  CG1 . VAL   E  194 ? 1.6629 0.8965 2.0067 0.1525  -0.3192 0.0355  193 VAL   E CG1 
8980  C  CG2 . VAL   E  194 ? 1.6260 0.8284 1.9939 0.1056  -0.3072 0.0156  193 VAL   E CG2 
8981  N  N   . GLU   E  195 ? 1.6426 0.9841 2.0568 0.3359  -0.3257 0.0621  194 GLU   E N   
8982  C  CA  . GLU   E  195 ? 1.6845 0.9615 2.1349 0.3670  -0.3299 0.0617  194 GLU   E CA  
8983  C  C   . GLU   E  195 ? 1.6779 0.8644 2.1547 0.3976  -0.3078 0.0214  194 GLU   E C   
8984  O  O   . GLU   E  195 ? 1.7105 0.8670 2.2047 0.4003  -0.3005 0.0035  194 GLU   E O   
8985  C  CB  . GLU   E  195 ? 1.7089 1.0746 2.1520 0.3439  -0.3067 0.0404  194 GLU   E CB  
8986  C  CG  . GLU   E  195 ? 1.7909 1.2040 2.1501 0.3277  -0.2758 -0.0700 194 GLU   E CG  
8987  C  CD  . GLU   E  195 ? 1.8273 1.4593 2.1916 0.2354  -0.2592 -0.0638 194 GLU   E CD  
8988  O  OE1 . GLU   E  195 ? 1.9602 1.6764 2.2074 0.1640  -0.2413 -0.1211 194 GLU   E OE1 
8989  O  OE2 . GLU   E  195 ? 1.8749 1.6621 2.2163 0.1912  -0.3138 -0.0284 194 GLU   E OE2 
8990  N  N   . ALA   E  196 ? 1.6052 0.8281 2.1751 0.3722  -0.2796 -0.0180 195 ALA   E N   
8991  C  CA  . ALA   E  196 ? 1.5949 0.7652 2.1544 0.3494  -0.2317 -0.0511 195 ALA   E CA  
8992  C  C   . ALA   E  196 ? 1.6138 0.7769 2.1380 0.3511  -0.2152 -0.0650 195 ALA   E C   
8993  O  O   . ALA   E  196 ? 1.6234 0.7244 2.1005 0.3827  -0.2382 0.0204  195 ALA   E O   
8994  C  CB  . ALA   E  196 ? 1.5180 0.7848 2.1410 0.3457  -0.2358 -0.0639 195 ALA   E CB  
8995  N  N   . ILE   E  197 ? 1.6295 0.8382 2.1543 0.3161  -0.1770 -0.0901 196 ILE   E N   
8996  C  CA  . ILE   E  197 ? 1.6743 0.8974 2.1633 0.2854  -0.1529 -0.1113 196 ILE   E CA  
8997  C  C   . ILE   E  197 ? 1.6601 0.9700 2.2038 0.3465  -0.1692 -0.1236 196 ILE   E C   
8998  O  O   . ILE   E  197 ? 1.6474 1.0746 2.1694 0.3102  -0.1429 -0.1466 196 ILE   E O   
8999  C  CB  . ILE   E  197 ? 1.6945 0.9396 2.1451 0.2539  -0.1727 -0.1407 196 ILE   E CB  
9000  C  CG1 . ILE   E  197 ? 1.8126 0.9199 2.1071 0.1981  -0.1341 -0.1376 196 ILE   E CG1 
9001  C  CG2 . ILE   E  197 ? 1.6601 0.9527 2.1646 0.2779  -0.1728 -0.1531 196 ILE   E CG2 
9002  C  CD1 . ILE   E  197 ? 1.8260 0.9598 2.0640 0.1743  -0.1217 -0.1618 196 ILE   E CD1 
9003  N  N   . SER   E  198 ? 1.6671 1.0292 2.2373 0.3060  -0.1145 -0.1369 197 SER   E N   
9004  C  CA  . SER   E  198 ? 1.7335 1.0200 2.2766 0.3105  -0.0975 -0.0925 197 SER   E CA  
9005  C  C   . SER   E  198 ? 1.7818 0.9394 2.3017 0.3298  -0.0459 -0.0513 197 SER   E C   
9006  O  O   . SER   E  198 ? 1.8677 0.9984 2.2254 0.2777  -0.0715 0.0151  197 SER   E O   
9007  C  CB  . SER   E  198 ? 1.7347 1.0806 2.3343 0.2984  -0.1087 -0.0823 197 SER   E CB  
9008  O  OG  . SER   E  198 ? 1.7242 1.1640 2.3503 0.2467  -0.1336 -0.1066 197 SER   E OG  
9009  N  N   . GLN   E  199 ? 1.7798 0.8931 2.2812 0.3461  -0.0057 -0.0186 198 GLN   E N   
9010  C  CA  . GLN   E  199 ? 1.8202 0.8258 2.2890 0.3473  0.0429  0.0037  198 GLN   E CA  
9011  C  C   . GLN   E  199 ? 1.8229 0.7648 2.3145 0.3504  0.0607  -0.0344 198 GLN   E C   
9012  O  O   . GLN   E  199 ? 1.8092 0.8815 2.3179 0.3216  0.0893  -0.1205 198 GLN   E O   
9013  C  CB  . GLN   E  199 ? 1.8493 0.8591 2.2890 0.3270  0.0527  0.0289  198 GLN   E CB  
9014  C  CG  . GLN   E  199 ? 1.8936 0.9448 2.2703 0.2987  0.0699  0.0649  198 GLN   E CG  
9015  C  CD  . GLN   E  199 ? 1.9541 0.9024 2.2954 0.3329  0.0760  0.1055  198 GLN   E CD  
9016  O  OE1 . GLN   E  199 ? 1.9793 0.8909 2.2596 0.2578  0.1555  0.0874  198 GLN   E OE1 
9017  N  NE2 . GLN   E  199 ? 1.9535 1.0027 2.3200 0.3134  0.0331  0.1407  198 GLN   E NE2 
9018  N  N   . SER   E  200 ? 1.8080 0.7994 2.3092 0.3387  0.0788  -0.0214 199 SER   E N   
9019  C  CA  . SER   E  200 ? 1.8000 0.8364 2.2749 0.3342  0.0669  -0.0411 199 SER   E CA  
9020  C  C   . SER   E  200 ? 1.8224 0.9346 2.2566 0.3232  0.0756  -0.0435 199 SER   E C   
9021  O  O   . SER   E  200 ? 1.8671 0.8204 2.1968 0.3538  0.1089  -0.0529 199 SER   E O   
9022  C  CB  . SER   E  200 ? 1.7714 0.8034 2.2187 0.3063  0.0702  -0.0556 199 SER   E CB  
9023  O  OG  . SER   E  200 ? 1.7411 0.8105 2.2069 0.2818  0.0760  -0.0660 199 SER   E OG  
9024  N  N   . LEU   E  201 ? 1.8785 1.1045 2.2581 0.3152  0.0046  -0.0486 200 LEU   E N   
9025  C  CA  . LEU   E  201 ? 1.9906 1.2270 2.2542 0.2861  -0.0011 -0.0306 200 LEU   E CA  
9026  C  C   . LEU   E  201 ? 2.0379 1.2397 2.2331 0.2563  0.0344  0.0263  200 LEU   E C   
9027  O  O   . LEU   E  201 ? 2.0507 1.3851 2.1783 0.2623  0.0992  0.0760  200 LEU   E O   
9028  C  CB  . LEU   E  201 ? 2.0486 1.1037 2.3073 0.3262  -0.0446 -0.1123 200 LEU   E CB  
9029  C  CG  . LEU   E  201 ? 2.0720 1.0928 2.2951 0.4125  -0.0488 -0.1682 200 LEU   E CG  
9030  C  CD1 . LEU   E  201 ? 2.0727 0.9828 2.3024 0.4349  -0.0415 -0.2103 200 LEU   E CD1 
9031  C  CD2 . LEU   E  201 ? 2.0247 1.0576 2.2795 0.4098  -0.0663 -0.1426 200 LEU   E CD2 
9032  N  N   . ARG   E  202 ? 2.0918 1.4496 2.2616 0.2247  0.0363  0.0990  201 ARG   E N   
9033  C  CA  . ARG   E  202 ? 2.0981 1.4509 2.3114 0.2630  -0.0168 0.1026  201 ARG   E CA  
9034  C  C   . ARG   E  202 ? 2.1490 1.3906 2.3608 0.3109  -0.0571 0.2643  201 ARG   E C   
9035  O  O   . ARG   E  202 ? 2.0057 1.2605 2.3474 0.3990  -0.1034 0.4746  201 ARG   E O   
9036  C  CB  . ARG   E  202 ? 2.1814 1.4789 2.3125 0.2007  0.0011  -0.0136 201 ARG   E CB  
9037  C  CG  . ARG   E  202 ? 2.1813 1.6910 2.3350 0.1313  0.0058  -0.0862 201 ARG   E CG  
9038  C  CD  . ARG   E  202 ? 2.2037 1.8007 2.3968 0.1567  0.0132  -0.1876 201 ARG   E CD  
9039  N  NE  . ARG   E  202 ? 2.1999 2.0950 2.3861 0.0424  -0.0334 -0.1865 201 ARG   E NE  
9040  C  CZ  . ARG   E  202 ? 2.1522 2.1756 2.3655 -0.0865 0.0063  -0.2409 201 ARG   E CZ  
9041  N  NH1 . ARG   E  202 ? 2.1075 2.2165 2.2449 -0.0650 -0.0363 -0.3097 201 ARG   E NH1 
9042  N  NH2 . ARG   E  202 ? 2.1351 2.2364 2.3704 -0.1214 -0.0516 -0.2384 201 ARG   E NH2 
9043  N  N   . ASP   E  203 ? 2.1656 1.4581 2.3659 0.3112  -0.0736 0.2685  202 ASP   E N   
9044  C  CA  . ASP   E  203 ? 2.3245 1.5907 2.3362 0.2569  -0.0989 0.2299  202 ASP   E CA  
9045  C  C   . ASP   E  203 ? 2.3422 1.5552 2.3163 0.3160  -0.1415 0.2543  202 ASP   E C   
9046  O  O   . ASP   E  203 ? 2.4048 1.6923 2.2785 0.3082  -0.1356 0.3394  202 ASP   E O   
9047  C  CB  . ASP   E  203 ? 2.3667 1.6420 2.3097 0.1973  -0.0761 0.1739  202 ASP   E CB  
9048  C  CG  . ASP   E  203 ? 2.4327 1.6788 2.2656 0.1703  -0.0419 0.1321  202 ASP   E CG  
9049  O  OD1 . ASP   E  203 ? 2.4402 1.7044 2.2366 0.1164  0.0560  -0.0837 202 ASP   E OD1 
9050  O  OD2 . ASP   E  203 ? 2.5230 1.5304 2.3354 0.1071  0.0342  0.1197  202 ASP   E OD2 
9051  N  N   . GLU   E  204 ? 2.3243 1.5239 2.3219 0.3391  -0.2030 0.1570  203 GLU   E N   
9052  C  CA  . GLU   E  204 ? 2.2787 1.5195 2.3216 0.4134  -0.2246 0.1212  203 GLU   E CA  
9053  C  C   . GLU   E  204 ? 2.2800 1.3653 2.2391 0.4132  -0.2721 0.0561  203 GLU   E C   
9054  O  O   . GLU   E  204 ? 2.3242 1.2595 2.2178 0.4181  -0.2266 0.0868  203 GLU   E O   
9055  C  CB  . GLU   E  204 ? 2.2170 1.7045 2.3610 0.3892  -0.2099 0.0833  203 GLU   E CB  
9056  C  CG  . GLU   E  204 ? 2.1663 1.8884 2.3101 0.3535  -0.1895 0.0165  203 GLU   E CG  
9057  C  CD  . GLU   E  204 ? 2.0948 2.0383 2.2926 0.3186  -0.1333 0.0402  203 GLU   E CD  
9058  O  OE1 . GLU   E  204 ? 2.0292 2.0856 2.1416 0.2862  -0.1952 0.1151  203 GLU   E OE1 
9059  O  OE2 . GLU   E  204 ? 2.0079 2.1301 2.4095 0.2439  -0.1296 0.0458  203 GLU   E OE2 
9060  N  N   . SER   E  205 ? 2.2655 1.3930 2.2266 0.4279  -0.3304 0.0691  204 SER   E N   
9061  C  CA  . SER   E  205 ? 2.2184 1.4183 2.1981 0.3893  -0.3815 0.0531  204 SER   E CA  
9062  C  C   . SER   E  205 ? 2.2231 1.3773 2.1427 0.3036  -0.4404 0.0666  204 SER   E C   
9063  O  O   . SER   E  205 ? 2.2525 1.5283 2.0925 0.2219  -0.4796 0.0229  204 SER   E O   
9064  C  CB  . SER   E  205 ? 2.2323 1.3838 2.2052 0.4320  -0.3723 0.0322  204 SER   E CB  
9065  O  OG  . SER   E  205 ? 2.2672 1.3592 2.2081 0.4569  -0.3669 0.0604  204 SER   E OG  
9066  N  N   . LEU   E  206 ? 2.1836 1.3300 2.1516 0.2819  -0.4743 0.0478  205 LEU   E N   
9067  C  CA  . LEU   E  206 ? 2.1271 1.3291 2.1493 0.2635  -0.4585 0.0285  205 LEU   E CA  
9068  C  C   . LEU   E  206 ? 2.1350 1.4006 2.0731 0.2455  -0.4264 0.0495  205 LEU   E C   
9069  O  O   . LEU   E  206 ? 2.1403 1.6090 2.0737 0.2667  -0.4261 0.0210  205 LEU   E O   
9070  C  CB  . LEU   E  206 ? 2.1100 1.2840 2.2058 0.3256  -0.3803 0.0326  205 LEU   E CB  
9071  C  CG  . LEU   E  206 ? 2.1064 1.1125 2.1968 0.3384  -0.3426 0.0016  205 LEU   E CG  
9072  C  CD1 . LEU   E  206 ? 2.0464 1.0991 2.1707 0.3927  -0.3320 -0.0023 205 LEU   E CD1 
9073  C  CD2 . LEU   E  206 ? 2.1113 1.0143 2.2221 0.3324  -0.3370 -0.0232 205 LEU   E CD2 
9074  N  N   . THR   E  207 ? 2.0124 1.3035 2.0491 0.1610  -0.4433 0.0658  206 THR   E N   
9075  C  CA  . THR   E  207 ? 1.9473 1.3141 2.0055 0.1081  -0.3805 0.0834  206 THR   E CA  
9076  C  C   . THR   E  207 ? 1.8770 1.3271 2.0211 0.1270  -0.4194 0.1124  206 THR   E C   
9077  O  O   . THR   E  207 ? 1.6977 1.3000 2.0634 0.1261  -0.4503 0.0456  206 THR   E O   
9078  C  CB  . THR   E  207 ? 1.8822 1.2349 1.9992 0.0901  -0.3706 0.0501  206 THR   E CB  
9079  O  OG1 . THR   E  207 ? 1.8263 1.1827 1.8862 0.0007  -0.3578 0.0503  206 THR   E OG1 
9080  C  CG2 . THR   E  207 ? 1.9211 1.2411 1.9655 0.0450  -0.3630 0.0662  206 THR   E CG2 
9081  N  N   . VAL   E  208 ? 1.9521 1.2688 2.0416 0.0733  -0.3639 0.0994  207 VAL   E N   
9082  C  CA  . VAL   E  208 ? 1.8840 1.2468 2.0305 0.0960  -0.3731 0.1786  207 VAL   E CA  
9083  C  C   . VAL   E  208 ? 1.8906 1.1530 2.0003 0.1121  -0.3650 0.2517  207 VAL   E C   
9084  O  O   . VAL   E  208 ? 1.8840 1.0708 2.0702 -0.0011 -0.2756 0.2470  207 VAL   E O   
9085  C  CB  . VAL   E  208 ? 1.9721 1.2878 2.0451 0.0404  -0.3858 0.1310  207 VAL   E CB  
9086  C  CG1 . VAL   E  208 ? 1.9785 1.3299 2.0490 -0.0157 -0.3734 0.1139  207 VAL   E CG1 
9087  C  CG2 . VAL   E  208 ? 1.9985 1.2484 2.0563 0.0810  -0.4173 0.1328  207 VAL   E CG2 
9088  N  N   . ASP   E  209 ? 1.9633 1.1001 1.9564 0.1502  -0.3792 0.2940  208 ASP   E N   
9089  C  CA  . ASP   E  209 ? 2.0021 1.0722 1.8961 0.1104  -0.3417 0.2656  208 ASP   E CA  
9090  C  C   . ASP   E  209 ? 1.9932 1.1510 1.8698 0.0940  -0.3120 0.2298  208 ASP   E C   
9091  O  O   . ASP   E  209 ? 1.9649 1.3775 1.8374 0.1298  -0.3329 0.2179  208 ASP   E O   
9092  C  CB  . ASP   E  209 ? 2.0508 0.9056 1.8820 0.1489  -0.4256 0.2831  208 ASP   E CB  
9093  C  CG  . ASP   E  209 ? 2.1439 0.8339 1.8780 0.1332  -0.4496 0.2821  208 ASP   E CG  
9094  O  OD1 . ASP   E  209 ? 2.2326 0.8085 1.8891 0.1875  -0.4457 0.3093  208 ASP   E OD1 
9095  O  OD2 . ASP   E  209 ? 2.2312 0.5083 1.8736 0.1520  -0.4658 0.2551  208 ASP   E OD2 
9096  N  N   . ASN   E  210 ? 2.0214 1.0963 1.9257 0.1146  -0.3244 0.1747  209 ASN   E N   
9097  C  CA  . ASN   E  210 ? 1.9935 1.0944 2.0035 0.1206  -0.3272 0.1414  209 ASN   E CA  
9098  C  C   . ASN   E  210 ? 1.8439 0.9245 2.0426 0.2316  -0.3185 0.1135  209 ASN   E C   
9099  O  O   . ASN   E  210 ? 1.7770 0.7405 2.0810 0.3011  -0.2872 0.0468  209 ASN   E O   
9100  C  CB  . ASN   E  210 ? 2.0030 1.1204 2.0163 0.1093  -0.3437 0.0839  209 ASN   E CB  
9101  C  CG  . ASN   E  210 ? 2.0457 1.2418 1.9950 0.0911  -0.3450 0.0182  209 ASN   E CG  
9102  O  OD1 . ASN   E  210 ? 2.0528 1.4394 2.0726 0.0036  -0.3723 -0.0476 209 ASN   E OD1 
9103  N  ND2 . ASN   E  210 ? 1.9886 1.2921 1.9941 0.1374  -0.3788 0.0222  209 ASN   E ND2 
9104  N  N   . LEU   E  211 ? 1.8258 0.9341 2.0325 0.2906  -0.2716 0.1702  210 LEU   E N   
9105  C  CA  . LEU   E  211 ? 1.7692 0.9897 2.0307 0.3119  -0.2446 0.1875  210 LEU   E CA  
9106  C  C   . LEU   E  211 ? 1.6636 0.9857 1.9341 0.2833  -0.2530 0.2261  210 LEU   E C   
9107  O  O   . LEU   E  211 ? 1.6243 0.8695 1.9108 0.2577  -0.2518 0.2871  210 LEU   E O   
9108  C  CB  . LEU   E  211 ? 1.7788 0.9435 2.0922 0.3747  -0.2254 0.1701  210 LEU   E CB  
9109  C  CG  . LEU   E  211 ? 1.8150 0.9190 2.1053 0.3963  -0.2260 0.1758  210 LEU   E CG  
9110  C  CD1 . LEU   E  211 ? 1.8028 0.8403 2.1357 0.4254  -0.2239 0.1565  210 LEU   E CD1 
9111  C  CD2 . LEU   E  211 ? 1.8094 0.9718 2.1780 0.4184  -0.2441 0.1681  210 LEU   E CD2 
9112  N  N   . SER   E  212 ? 1.6074 1.0593 1.9248 0.2793  -0.2262 0.2335  211 SER   E N   
9113  C  CA  . SER   E  212 ? 1.6096 1.0037 1.8795 0.2311  -0.1939 0.2055  211 SER   E CA  
9114  C  C   . SER   E  212 ? 1.5722 1.0424 1.9061 0.2367  -0.1661 0.2355  211 SER   E C   
9115  O  O   . SER   E  212 ? 1.6049 0.9617 1.8634 0.2743  -0.1643 0.2976  211 SER   E O   
9116  C  CB  . SER   E  212 ? 1.6450 0.9797 1.7824 0.2216  -0.1428 0.2085  211 SER   E CB  
9117  O  OG  . SER   E  212 ? 1.6926 0.9006 1.6845 0.1379  -0.1473 0.2391  211 SER   E OG  
9118  N  N   . ILE   E  213 ? 1.5076 1.0633 1.9886 0.1737  -0.1974 0.0573  212 ILE   E N   
9119  C  CA  . ILE   E  213 ? 1.5242 1.0965 1.9630 0.1845  -0.1762 0.0119  212 ILE   E CA  
9120  C  C   . ILE   E  213 ? 1.4280 1.1067 1.8866 0.1807  -0.1875 -0.0342 212 ILE   E C   
9121  O  O   . ILE   E  213 ? 1.4454 1.2529 1.8858 0.2081  -0.1108 -0.0953 212 ILE   E O   
9122  C  CB  . ILE   E  213 ? 1.5138 1.1805 2.0903 0.2455  -0.2077 0.0164  212 ILE   E CB  
9123  C  CG1 . ILE   E  213 ? 1.5898 1.2139 2.1448 0.2935  -0.2509 0.0797  212 ILE   E CG1 
9124  C  CG2 . ILE   E  213 ? 1.5444 1.1828 2.0746 0.2494  -0.2069 0.0052  212 ILE   E CG2 
9125  C  CD1 . ILE   E  213 ? 1.5921 1.2657 2.1871 0.3012  -0.2357 0.0974  212 ILE   E CD1 
9126  N  N   . ALA   E  214 ? 1.3980 1.0346 1.8179 0.1466  -0.1703 -0.0969 213 ALA   E N   
9127  C  CA  . ALA   E  214 ? 1.4348 1.0032 1.7786 0.1156  -0.1757 -0.1092 213 ALA   E CA  
9128  C  C   . ALA   E  214 ? 1.5019 1.0287 1.7697 0.1092  -0.1806 -0.1100 213 ALA   E C   
9129  O  O   . ALA   E  214 ? 1.5588 1.0515 1.7784 0.1092  -0.1961 -0.1278 213 ALA   E O   
9130  C  CB  . ALA   E  214 ? 1.4338 0.9194 1.7261 0.1129  -0.1662 -0.1206 213 ALA   E CB  
9131  N  N   . ILE   E  215 ? 1.5728 1.0228 1.8184 0.1192  -0.1865 -0.1224 214 ILE   E N   
9132  C  CA  . ILE   E  215 ? 1.5700 1.0191 1.8302 0.1331  -0.1653 -0.1242 214 ILE   E CA  
9133  C  C   . ILE   E  215 ? 1.6119 1.0219 1.7815 0.1489  -0.1799 -0.1296 214 ILE   E C   
9134  O  O   . ILE   E  215 ? 1.6432 0.9655 1.7805 0.1867  -0.2593 -0.1250 214 ILE   E O   
9135  C  CB  . ILE   E  215 ? 1.5671 1.0376 1.8810 0.1213  -0.1401 -0.1412 214 ILE   E CB  
9136  C  CG1 . ILE   E  215 ? 1.5867 1.0360 1.9141 0.1165  -0.0977 -0.1458 214 ILE   E CG1 
9137  C  CG2 . ILE   E  215 ? 1.5268 1.0496 1.8816 0.0951  -0.1404 -0.1325 214 ILE   E CG2 
9138  C  CD1 . ILE   E  215 ? 1.6110 0.9974 1.9507 0.1640  -0.1012 -0.1761 214 ILE   E CD1 
9139  N  N   . VAL   E  216 ? 1.5901 0.9689 1.7897 0.1730  -0.1507 -0.0917 215 VAL   E N   
9140  C  CA  . VAL   E  216 ? 1.5476 0.9329 1.7683 0.1329  -0.0915 -0.0883 215 VAL   E CA  
9141  C  C   . VAL   E  216 ? 1.5610 0.9854 1.7871 0.1001  -0.0761 -0.0741 215 VAL   E C   
9142  O  O   . VAL   E  216 ? 1.5750 0.9526 1.7068 0.0259  -0.0936 -0.0546 215 VAL   E O   
9143  C  CB  . VAL   E  216 ? 1.5456 0.8763 1.7241 0.1571  -0.0849 -0.0896 215 VAL   E CB  
9144  C  CG1 . VAL   E  216 ? 1.5186 0.8569 1.6987 0.1992  -0.0796 -0.0895 215 VAL   E CG1 
9145  C  CG2 . VAL   E  216 ? 1.5225 0.8741 1.7197 0.1396  -0.0666 -0.0648 215 VAL   E CG2 
9146  N  N   . GLY   E  217 ? 1.5405 1.0271 1.8386 0.0870  -0.0281 -0.0336 216 GLY   E N   
9147  C  CA  . GLY   E  217 ? 1.5163 1.1543 1.8753 0.1102  0.0069  -0.0133 216 GLY   E CA  
9148  C  C   . GLY   E  217 ? 1.5259 1.1568 1.9602 0.1551  0.0225  0.0194  216 GLY   E C   
9149  O  O   . GLY   E  217 ? 1.5242 1.1731 1.9149 0.1296  0.1353  0.0877  216 GLY   E O   
9150  N  N   . LYS   E  218 ? 1.5351 1.1984 2.0106 0.1347  0.0113  0.0912  217 LYS   E N   
9151  C  CA  . LYS   E  218 ? 1.5787 1.2253 2.0699 0.1142  -0.0316 0.1384  217 LYS   E CA  
9152  C  C   . LYS   E  218 ? 1.6293 1.2813 2.0911 0.1036  -0.0978 0.1323  217 LYS   E C   
9153  O  O   . LYS   E  218 ? 1.6481 1.4245 2.1066 0.2112  -0.1441 0.1224  217 LYS   E O   
9154  C  CB  . LYS   E  218 ? 1.5800 1.3319 2.0842 0.0456  -0.0205 0.0793  217 LYS   E CB  
9155  C  CG  . LYS   E  218 ? 1.5921 1.3832 2.0530 -0.0427 0.0239  0.0929  217 LYS   E CG  
9156  C  CD  . LYS   E  218 ? 1.5938 1.4807 2.1011 -0.1508 0.0281  0.0628  217 LYS   E CD  
9157  C  CE  . LYS   E  218 ? 1.6306 1.4948 2.1136 -0.2052 0.0331  0.0815  217 LYS   E CE  
9158  N  NZ  . LYS   E  218 ? 1.6432 1.6215 2.1812 -0.2521 0.0404  0.0673  217 LYS   E NZ  
9159  N  N   . ASP   E  219 ? 1.6963 1.2614 2.1403 0.0815  -0.1451 0.1958  218 ASP   E N   
9160  C  CA  . ASP   E  219 ? 1.9103 1.2769 2.1202 0.0379  -0.0926 0.1854  218 ASP   E CA  
9161  C  C   . ASP   E  219 ? 1.8626 1.2048 2.1340 0.0078  -0.0443 0.1739  218 ASP   E C   
9162  O  O   . ASP   E  219 ? 2.0065 1.2826 2.1586 -0.0432 -0.1268 0.1750  218 ASP   E O   
9163  C  CB  . ASP   E  219 ? 2.0426 1.3121 2.1940 -0.0323 -0.0091 0.2749  218 ASP   E CB  
9164  C  CG  . ASP   E  219 ? 2.1583 1.3595 2.2153 -0.0379 0.0676  0.3154  218 ASP   E CG  
9165  O  OD1 . ASP   E  219 ? 2.1975 1.2770 2.1585 -0.0391 0.0285  0.3808  218 ASP   E OD1 
9166  O  OD2 . ASP   E  219 ? 2.3569 1.4020 2.2089 -0.0853 0.1804  0.4563  218 ASP   E OD2 
9167  N  N   . THR   E  220 ? 1.6911 1.0826 2.0416 0.0985  -0.1606 0.0862  219 THR   E N   
9168  C  CA  . THR   E  220 ? 1.6528 1.0936 2.0255 0.0499  -0.1850 0.0768  219 THR   E CA  
9169  C  C   . THR   E  220 ? 1.6213 0.9167 1.9015 0.0939  -0.2534 0.0895  219 THR   E C   
9170  O  O   . THR   E  220 ? 1.6406 1.0183 1.8486 0.1826  -0.3372 0.0859  219 THR   E O   
9171  C  CB  . THR   E  220 ? 1.7489 1.1475 2.0837 0.0937  -0.1553 0.0191  219 THR   E CB  
9172  O  OG1 . THR   E  220 ? 1.8991 1.2926 2.0860 0.0497  -0.0591 -0.0177 219 THR   E OG1 
9173  C  CG2 . THR   E  220 ? 1.7639 1.2116 2.0829 0.0785  -0.1247 0.0524  219 THR   E CG2 
9174  N  N   . PRO   E  221 ? 1.6227 0.7740 1.8727 0.0486  -0.2679 0.1194  220 PRO   E N   
9175  C  CA  . PRO   E  221 ? 1.6097 0.8427 1.8449 0.0708  -0.2652 0.0746  220 PRO   E CA  
9176  C  C   . PRO   E  221 ? 1.5456 0.8500 1.8904 0.0289  -0.2101 0.0514  220 PRO   E C   
9177  O  O   . PRO   E  221 ? 1.5624 0.8554 1.9791 0.0876  -0.1880 0.0236  220 PRO   E O   
9178  C  CB  . PRO   E  221 ? 1.6316 0.7198 1.8313 0.0704  -0.2718 0.1266  220 PRO   E CB  
9179  C  CG  . PRO   E  221 ? 1.6296 0.7970 1.8444 0.0488  -0.2656 0.1526  220 PRO   E CG  
9180  C  CD  . PRO   E  221 ? 1.6369 0.7705 1.8709 0.0440  -0.2717 0.1288  220 PRO   E CD  
9181  N  N   . PHE   E  222 ? 1.5163 0.9581 1.8853 0.0362  -0.1697 -0.0111 221 PHE   E N   
9182  C  CA  . PHE   E  222 ? 1.5617 0.9307 1.8832 0.0978  -0.1776 -0.0126 221 PHE   E CA  
9183  C  C   . PHE   E  222 ? 1.4810 0.9533 1.8782 0.1353  -0.1850 -0.0741 221 PHE   E C   
9184  O  O   . PHE   E  222 ? 1.5459 0.8492 1.8487 0.1428  -0.2755 -0.1185 221 PHE   E O   
9185  C  CB  . PHE   E  222 ? 1.5717 0.8867 1.9119 0.0930  -0.1808 0.0084  221 PHE   E CB  
9186  C  CG  . PHE   E  222 ? 1.6040 0.8804 1.9385 0.1122  -0.2131 0.0485  221 PHE   E CG  
9187  C  CD1 . PHE   E  222 ? 1.6084 0.8437 1.9289 0.1307  -0.2727 0.0746  221 PHE   E CD1 
9188  C  CD2 . PHE   E  222 ? 1.5971 0.8448 1.9413 0.1659  -0.1883 0.0584  221 PHE   E CD2 
9189  C  CE1 . PHE   E  222 ? 1.5993 0.8492 1.9031 0.1780  -0.2758 0.1181  221 PHE   E CE1 
9190  C  CE2 . PHE   E  222 ? 1.5892 0.8306 1.9381 0.2157  -0.2213 0.0837  221 PHE   E CE2 
9191  C  CZ  . PHE   E  222 ? 1.5987 0.8578 1.9287 0.2109  -0.2568 0.0931  221 PHE   E CZ  
9192  N  N   . THR   E  223 ? 1.3782 1.0822 1.9032 0.1213  -0.1882 -0.0817 222 THR   E N   
9193  C  CA  . THR   E  223 ? 1.4510 1.1372 1.8526 0.0236  -0.1727 -0.1337 222 THR   E CA  
9194  C  C   . THR   E  223 ? 1.4508 1.1306 1.7992 0.0051  -0.1804 -0.1191 222 THR   E C   
9195  O  O   . THR   E  223 ? 1.4122 1.0585 1.8374 -0.0240 -0.1910 -0.1349 222 THR   E O   
9196  C  CB  . THR   E  223 ? 1.4735 1.2458 1.9006 -0.0199 -0.1501 -0.2161 222 THR   E CB  
9197  O  OG1 . THR   E  223 ? 1.4798 1.3669 1.9627 -0.0755 -0.1019 -0.2569 222 THR   E OG1 
9198  C  CG2 . THR   E  223 ? 1.4529 1.2661 1.8849 0.0457  -0.1343 -0.2155 222 THR   E CG2 
9199  N  N   . ILE   E  224 ? 1.4827 0.9490 1.8183 -0.0026 -0.2293 -0.0882 223 ILE   E N   
9200  C  CA  . ILE   E  224 ? 1.5507 0.9112 1.8115 -0.0388 -0.2502 -0.1229 223 ILE   E CA  
9201  C  C   . ILE   E  224 ? 1.5646 0.8742 1.8052 -0.0572 -0.2546 -0.0727 223 ILE   E C   
9202  O  O   . ILE   E  224 ? 1.5978 0.9799 1.7216 -0.0484 -0.2480 -0.0917 223 ILE   E O   
9203  C  CB  . ILE   E  224 ? 1.5889 0.8527 1.7632 -0.0134 -0.2327 -0.1207 223 ILE   E CB  
9204  C  CG1 . ILE   E  224 ? 1.6121 0.7575 1.7102 0.0098  -0.2255 -0.1283 223 ILE   E CG1 
9205  C  CG2 . ILE   E  224 ? 1.6740 0.8963 1.8011 0.0405  -0.2247 -0.0471 223 ILE   E CG2 
9206  C  CD1 . ILE   E  224 ? 1.6145 0.7564 1.6485 0.0152  -0.2400 -0.1367 223 ILE   E CD1 
9207  N  N   . TYR   E  225 ? 1.5477 0.9233 1.8266 -0.0017 -0.2775 0.0038  224 TYR   E N   
9208  C  CA  . TYR   E  225 ? 1.5953 1.1442 1.8840 0.0335  -0.3167 0.0447  224 TYR   E CA  
9209  C  C   . TYR   E  225 ? 1.5862 1.2041 1.9761 0.0801  -0.2815 0.1193  224 TYR   E C   
9210  O  O   . TYR   E  225 ? 1.5603 1.2201 1.9069 0.1898  -0.3144 0.0857  224 TYR   E O   
9211  C  CB  . TYR   E  225 ? 1.6492 1.1324 1.8589 0.0072  -0.2867 0.0955  224 TYR   E CB  
9212  C  CG  . TYR   E  225 ? 1.7623 1.0800 1.8568 0.0310  -0.2901 0.0800  224 TYR   E CG  
9213  C  CD1 . TYR   E  225 ? 1.8267 1.0599 1.8394 0.0374  -0.2685 0.0792  224 TYR   E CD1 
9214  C  CD2 . TYR   E  225 ? 1.8191 1.0982 1.8594 0.0058  -0.2330 0.0798  224 TYR   E CD2 
9215  C  CE1 . TYR   E  225 ? 1.8655 1.0692 1.8666 -0.0515 -0.2143 0.0299  224 TYR   E CE1 
9216  C  CE2 . TYR   E  225 ? 1.8673 1.0846 1.9044 -0.0457 -0.1623 0.0322  224 TYR   E CE2 
9217  C  CZ  . TYR   E  225 ? 1.8918 1.1000 1.8713 -0.0745 -0.1658 0.0394  224 TYR   E CZ  
9218  O  OH  . TYR   E  225 ? 1.9562 1.0784 1.9521 -0.1300 -0.1584 0.0156  224 TYR   E OH  
9219  N  N   . ASP   E  226 ? 1.6150 1.2705 1.9895 0.1406  -0.2941 0.1248  225 ASP   E N   
9220  C  CA  . ASP   E  226 ? 1.6331 1.2043 2.0625 0.2055  -0.3457 0.1346  225 ASP   E CA  
9221  C  C   . ASP   E  226 ? 1.7302 1.0824 2.0280 0.2235  -0.4052 0.1407  225 ASP   E C   
9222  O  O   . ASP   E  226 ? 1.7159 1.1680 1.9466 0.1761  -0.5027 0.1062  225 ASP   E O   
9223  C  CB  . ASP   E  226 ? 1.7080 1.2333 2.1134 0.2199  -0.2706 0.1691  225 ASP   E CB  
9224  C  CG  . ASP   E  226 ? 1.6943 1.2315 2.1500 0.1921  -0.2571 0.1477  225 ASP   E CG  
9225  O  OD1 . ASP   E  226 ? 1.6631 1.0357 2.2556 0.1393  -0.2528 0.2243  225 ASP   E OD1 
9226  O  OD2 . ASP   E  226 ? 1.6749 1.4990 2.2382 0.2975  -0.1696 0.1207  225 ASP   E OD2 
9227  N  N   . GLY   E  227 ? 1.7620 0.9559 2.0831 0.2267  -0.4488 0.0813  226 GLY   E N   
9228  C  CA  . GLY   E  227 ? 1.7893 0.8938 2.0765 0.2149  -0.4610 0.0763  226 GLY   E CA  
9229  C  C   . GLY   E  227 ? 1.7751 0.8181 2.0953 0.2375  -0.4580 0.0587  226 GLY   E C   
9230  O  O   . GLY   E  227 ? 1.6718 0.6445 2.1051 0.2733  -0.4640 0.0933  226 GLY   E O   
9231  N  N   . GLU   E  228 ? 1.7578 0.9377 2.1084 0.2130  -0.4576 0.0360  227 GLU   E N   
9232  C  CA  . GLU   E  228 ? 1.7657 1.1404 2.1248 0.2292  -0.4422 0.0151  227 GLU   E CA  
9233  C  C   . GLU   E  228 ? 1.7524 1.2381 2.0868 0.1950  -0.4201 -0.0157 227 GLU   E C   
9234  O  O   . GLU   E  228 ? 1.6975 1.3235 2.0541 0.1918  -0.4787 -0.0117 227 GLU   E O   
9235  C  CB  . GLU   E  228 ? 1.8571 1.2759 2.1037 0.2222  -0.4656 -0.0099 227 GLU   E CB  
9236  C  CG  . GLU   E  228 ? 1.8931 1.3114 2.1615 0.2736  -0.4636 -0.0230 227 GLU   E CG  
9237  C  CD  . GLU   E  228 ? 1.9914 1.2940 2.2005 0.3189  -0.4877 -0.0549 227 GLU   E CD  
9238  O  OE1 . GLU   E  228 ? 2.0532 1.2020 2.1563 0.3400  -0.4588 -0.1104 227 GLU   E OE1 
9239  O  OE2 . GLU   E  228 ? 1.9546 1.4348 2.2477 0.3667  -0.4846 -0.0324 227 GLU   E OE2 
9240  N  N   . ALA   E  229 ? 1.7307 1.2306 2.0359 0.1671  -0.4084 -0.0200 228 ALA   E N   
9241  C  CA  . ALA   E  229 ? 1.7668 1.1555 2.0870 0.0983  -0.3619 -0.0106 228 ALA   E CA  
9242  C  C   . ALA   E  229 ? 1.8431 1.2036 2.1396 0.0969  -0.3381 -0.0476 228 ALA   E C   
9243  O  O   . ALA   E  229 ? 1.9576 1.3228 2.2518 0.0326  -0.2896 0.0624  228 ALA   E O   
9244  C  CB  . ALA   E  229 ? 1.7345 1.0351 2.0087 0.0371  -0.3646 -0.0820 228 ALA   E CB  
9245  N  N   . VAL   E  230 ? 1.8298 1.2098 2.2120 0.1229  -0.3166 0.0283  229 VAL   E N   
9246  C  CA  . VAL   E  230 ? 1.7840 1.0979 2.2350 0.1732  -0.2994 0.0692  229 VAL   E CA  
9247  C  C   . VAL   E  230 ? 1.7797 1.0626 2.1837 0.1730  -0.2676 0.0682  229 VAL   E C   
9248  O  O   . VAL   E  230 ? 1.7190 0.9475 2.2039 0.2108  -0.1938 0.1260  229 VAL   E O   
9249  C  CB  . VAL   E  230 ? 1.8345 1.1034 2.2277 0.1352  -0.3109 0.0774  229 VAL   E CB  
9250  C  CG1 . VAL   E  230 ? 1.8478 1.0910 2.2609 0.1464  -0.2877 0.0293  229 VAL   E CG1 
9251  C  CG2 . VAL   E  230 ? 1.8720 1.1207 2.2109 0.2051  -0.3471 0.1036  229 VAL   E CG2 
9252  N  N   . ALA   E  231 ? 1.7101 1.1416 2.2145 0.2174  -0.2751 0.0775  230 ALA   E N   
9253  C  CA  . ALA   E  231 ? 1.6506 1.2856 2.2468 0.2386  -0.2977 0.0225  230 ALA   E CA  
9254  C  C   . ALA   E  231 ? 1.6473 1.3750 2.2570 0.2296  -0.3022 0.0350  230 ALA   E C   
9255  O  O   . ALA   E  231 ? 1.7155 1.4037 2.3069 0.2611  -0.3522 -0.0159 230 ALA   E O   
9256  C  CB  . ALA   E  231 ? 1.5951 1.3003 2.2389 0.2477  -0.2721 0.0017  230 ALA   E CB  
9257  N  N   . LYS   E  232 ? 1.6850 1.3413 2.3052 0.2110  -0.3366 0.0169  231 LYS   E N   
9258  C  CA  . LYS   E  232 ? 1.7333 1.4457 2.3157 0.1979  -0.3169 0.0018  231 LYS   E CA  
9259  C  C   . LYS   E  232 ? 1.7105 1.4840 2.3375 0.1847  -0.3175 -0.0196 231 LYS   E C   
9260  O  O   . LYS   E  232 ? 1.7795 1.6329 2.3742 0.2075  -0.2477 0.0120  231 LYS   E O   
9261  C  CB  . LYS   E  232 ? 1.7557 1.4326 2.2832 0.1766  -0.3431 -0.0158 231 LYS   E CB  
9262  C  CG  . LYS   E  232 ? 1.7538 1.4881 2.2718 0.1586  -0.3347 -0.0400 231 LYS   E CG  
9263  C  CD  . LYS   E  232 ? 1.7237 1.5259 2.2237 0.1284  -0.3430 -0.0316 231 LYS   E CD  
9264  C  CE  . LYS   E  232 ? 1.6895 1.5500 2.1891 0.1180  -0.3401 -0.0441 231 LYS   E CE  
9265  N  NZ  . LYS   E  232 ? 1.6709 1.5249 2.1714 0.1300  -0.3539 -0.0590 231 LYS   E NZ  
9266  N  N   . TYR   E  233 ? 1.7185 1.4756 2.3386 0.1831  -0.3528 -0.0374 232 TYR   E N   
9267  C  CA  . TYR   E  233 ? 1.7322 1.4387 2.3130 0.2438  -0.3420 -0.0457 232 TYR   E CA  
9268  C  C   . TYR   E  233 ? 1.7437 1.3877 2.2985 0.3552  -0.3070 -0.1251 232 TYR   E C   
9269  O  O   . TYR   E  233 ? 1.6866 1.2117 2.2770 0.4633  -0.2466 -0.1518 232 TYR   E O   
9270  C  CB  . TYR   E  233 ? 1.7325 1.4330 2.2531 0.1880  -0.4026 -0.0476 232 TYR   E CB  
9271  C  CG  . TYR   E  233 ? 1.7145 1.4301 2.2514 0.1094  -0.4122 -0.0538 232 TYR   E CG  
9272  C  CD1 . TYR   E  233 ? 1.6785 1.4674 2.2700 0.0661  -0.3846 -0.0739 232 TYR   E CD1 
9273  C  CD2 . TYR   E  233 ? 1.7470 1.4721 2.2255 0.0763  -0.4097 -0.0876 232 TYR   E CD2 
9274  C  CE1 . TYR   E  233 ? 1.7049 1.4932 2.2462 0.0642  -0.3658 -0.0487 232 TYR   E CE1 
9275  C  CE2 . TYR   E  233 ? 1.7581 1.4901 2.2323 0.0585  -0.3945 -0.0675 232 TYR   E CE2 
9276  C  CZ  . TYR   E  233 ? 1.7313 1.5220 2.2423 0.0738  -0.3804 -0.0672 232 TYR   E CZ  
9277  O  OH  . TYR   E  233 ? 1.7165 1.5046 2.2658 0.1008  -0.4082 -0.0851 232 TYR   E OH  
9278  N  N   . ILE   E  234 ? 1.7587 1.4327 2.3241 0.4012  -0.2910 -0.0915 233 ILE   E N   
9279  C  CA  . ILE   E  234 ? 1.9070 1.4496 2.3170 0.2745  -0.2343 -0.0612 233 ILE   E CA  
9280  C  C   . ILE   E  234 ? 1.9603 1.4947 2.4047 0.3090  -0.1741 -0.0699 233 ILE   E C   
9281  O  O   . ILE   E  234 ? 2.0337 1.7431 2.4883 0.2012  -0.2176 -0.0429 233 ILE   E O   
9282  C  CB  . ILE   E  234 ? 1.8258 1.4661 2.3274 0.2798  -0.2113 -0.0702 233 ILE   E CB  
9283  C  CG1 . ILE   E  234 ? 1.8314 1.4209 2.2497 0.2870  -0.1789 -0.0135 233 ILE   E CG1 
9284  C  CG2 . ILE   E  234 ? 1.8536 1.4555 2.2917 0.2099  -0.2269 -0.0972 233 ILE   E CG2 
9285  C  CD1 . ILE   E  234 ? 1.8071 1.4506 2.2440 0.2959  -0.1702 0.0253  233 ILE   E CD1 
9286  O  OXT . ILE   E  234 ? 2.0176 1.2523 2.4873 0.2483  -0.2302 0.0419  233 ILE   E OXT 
9287  N  N   . THR   F  6   ? 2.1145 0.7647 2.3316 -0.1413 -0.0949 -0.1147 2   THR   F N   
9288  C  CA  . THR   F  6   ? 2.0105 0.8971 2.2532 -0.1369 -0.1240 -0.0696 2   THR   F CA  
9289  C  C   . THR   F  6   ? 1.8853 0.9611 2.1169 -0.1620 -0.1433 -0.0013 2   THR   F C   
9290  O  O   . THR   F  6   ? 1.7732 1.0544 2.0452 -0.2050 -0.2106 0.0119  2   THR   F O   
9291  C  CB  . THR   F  6   ? 2.0423 0.9594 2.3638 -0.0754 -0.1026 -0.0939 2   THR   F CB  
9292  O  OG1 . THR   F  6   ? 1.9705 0.7749 2.4981 -0.1446 -0.1471 -0.1442 2   THR   F OG1 
9293  C  CG2 . THR   F  6   ? 2.0609 0.9564 2.3267 -0.0614 -0.0918 -0.0765 2   THR   F CG2 
9294  N  N   . GLY   F  7   ? 1.8854 0.8953 2.0540 -0.1586 -0.1941 0.0451  3   GLY   F N   
9295  C  CA  . GLY   F  7   ? 1.7823 0.9943 1.9457 -0.1279 -0.2481 0.0455  3   GLY   F CA  
9296  C  C   . GLY   F  7   ? 1.6881 1.1274 1.9040 -0.0002 -0.2600 0.1003  3   GLY   F C   
9297  O  O   . GLY   F  7   ? 1.6338 1.1424 2.0326 0.0174  -0.2372 0.0535  3   GLY   F O   
9298  N  N   . TYR   F  8   ? 1.6314 0.9519 1.8779 0.0627  -0.2397 0.1000  4   TYR   F N   
9299  C  CA  . TYR   F  8   ? 1.6243 0.8968 1.7344 0.0335  -0.2115 0.0509  4   TYR   F CA  
9300  C  C   . TYR   F  8   ? 1.6337 0.9034 1.7035 0.0468  -0.1624 0.0372  4   TYR   F C   
9301  O  O   . TYR   F  8   ? 1.3204 0.8267 1.8999 0.1028  -0.0538 -0.1414 4   TYR   F O   
9302  C  CB  . TYR   F  8   ? 1.6931 0.7604 1.6667 0.0486  -0.1961 0.0599  4   TYR   F CB  
9303  C  CG  . TYR   F  8   ? 1.7208 0.6806 1.5570 0.0071  -0.2737 0.0342  4   TYR   F CG  
9304  C  CD1 . TYR   F  8   ? 1.7221 0.7198 1.5190 0.0373  -0.2973 0.0907  4   TYR   F CD1 
9305  C  CD2 . TYR   F  8   ? 1.7730 0.6753 1.4909 0.0203  -0.2750 -0.0016 4   TYR   F CD2 
9306  C  CE1 . TYR   F  8   ? 1.7678 0.6047 1.4752 0.0265  -0.2949 0.0967  4   TYR   F CE1 
9307  C  CE2 . TYR   F  8   ? 1.8112 0.6208 1.4594 0.0168  -0.2571 0.0769  4   TYR   F CE2 
9308  C  CZ  . TYR   F  8   ? 1.8098 0.5940 1.4460 0.0204  -0.2746 0.1065  4   TYR   F CZ  
9309  O  OH  . TYR   F  8   ? 1.8775 0.3251 1.4228 0.0033  -0.2978 0.1534  4   TYR   F OH  
9310  N  N   . ASP   F  9   ? 1.7128 0.6893 1.5069 0.0685  -0.2155 0.0768  5   ASP   F N   
9311  C  CA  . ASP   F  9   ? 1.8171 0.5759 1.3997 0.0032  -0.2168 0.0513  5   ASP   F CA  
9312  C  C   . ASP   F  9   ? 1.9469 0.5460 1.3498 0.0183  -0.2791 0.1180  5   ASP   F C   
9313  O  O   . ASP   F  9   ? 1.9379 0.7275 1.4047 0.0236  -0.2430 0.1225  5   ASP   F O   
9314  C  CB  . ASP   F  9   ? 1.8923 0.6053 1.3901 -0.0448 -0.1967 -0.0538 5   ASP   F CB  
9315  C  CG  . ASP   F  9   ? 1.9238 0.6366 1.3655 0.0308  -0.1891 -0.1093 5   ASP   F CG  
9316  O  OD1 . ASP   F  9   ? 2.0018 0.8676 1.3529 0.0158  -0.0961 -0.2052 5   ASP   F OD1 
9317  O  OD2 . ASP   F  9   ? 1.9763 0.6400 1.3392 0.0014  -0.1011 -0.2496 5   ASP   F OD2 
9318  N  N   . LEU   F  10  ? 1.9513 0.4013 1.3010 -0.0353 -0.3365 0.0991  6   LEU   F N   
9319  C  CA  . LEU   F  10  ? 1.9894 0.5617 1.3286 -0.0201 -0.3703 0.0580  6   LEU   F CA  
9320  C  C   . LEU   F  10  ? 1.9492 0.5939 1.3358 0.0764  -0.3788 0.0831  6   LEU   F C   
9321  O  O   . LEU   F  10  ? 2.0077 0.6276 1.4204 0.0290  -0.3950 0.0456  6   LEU   F O   
9322  C  CB  . LEU   F  10  ? 2.0215 0.5132 1.3209 -0.0682 -0.4129 0.0391  6   LEU   F CB  
9323  C  CG  . LEU   F  10  ? 2.0776 0.4804 1.3006 -0.1256 -0.4549 0.0635  6   LEU   F CG  
9324  C  CD1 . LEU   F  10  ? 2.0455 0.5635 1.2984 -0.2029 -0.4487 0.0326  6   LEU   F CD1 
9325  C  CD2 . LEU   F  10  ? 2.0945 0.5179 1.3358 -0.1247 -0.4255 0.0745  6   LEU   F CD2 
9326  N  N   . SER   F  11  ? 1.8995 0.6341 1.3251 0.1134  -0.3422 0.0346  7   SER   F N   
9327  C  CA  . SER   F  11  ? 1.8271 0.5910 1.3032 0.0205  -0.3304 -0.0212 7   SER   F CA  
9328  C  C   . SER   F  11  ? 1.7990 0.5443 1.3340 0.0792  -0.2703 -0.0060 7   SER   F C   
9329  O  O   . SER   F  11  ? 1.7141 0.3867 1.4953 0.0354  -0.3302 0.0970  7   SER   F O   
9330  C  CB  . SER   F  11  ? 1.8561 0.5995 1.2347 0.0202  -0.3363 -0.0520 7   SER   F CB  
9331  O  OG  . SER   F  11  ? 1.8606 0.5888 1.1865 0.0164  -0.3425 -0.0161 7   SER   F OG  
9332  N  N   . ASN   F  12  ? 1.7265 0.5676 1.2039 0.0655  -0.2698 -0.0736 8   ASN   F N   
9333  C  CA  . ASN   F  12  ? 1.7654 0.5562 1.1701 0.0672  -0.2355 -0.0879 8   ASN   F CA  
9334  C  C   . ASN   F  12  ? 1.7614 0.5101 1.1790 0.0546  -0.2396 -0.0205 8   ASN   F C   
9335  O  O   . ASN   F  12  ? 1.8107 0.4621 1.1395 0.0353  -0.2565 0.0309  8   ASN   F O   
9336  C  CB  . ASN   F  12  ? 1.7557 0.5945 1.1682 0.0524  -0.2371 -0.1554 8   ASN   F CB  
9337  C  CG  . ASN   F  12  ? 1.7516 0.6910 1.0870 0.0896  -0.2617 -0.1867 8   ASN   F CG  
9338  O  OD1 . ASN   F  12  ? 1.7587 0.7286 1.0849 0.1391  -0.2314 -0.2625 8   ASN   F OD1 
9339  N  ND2 . ASN   F  12  ? 1.7596 0.6752 1.1693 0.1094  -0.2510 -0.1647 8   ASN   F ND2 
9340  N  N   . SER   F  13  ? 1.7586 0.4820 1.1617 0.0594  -0.2196 -0.0038 9   SER   F N   
9341  C  CA  . SER   F  13  ? 1.7709 0.5068 1.1810 0.0745  -0.2324 -0.0268 9   SER   F CA  
9342  C  C   . SER   F  13  ? 1.8486 0.5298 1.2820 0.0426  -0.2314 0.0735  9   SER   F C   
9343  O  O   . SER   F  13  ? 1.9118 0.3633 1.3657 0.1020  -0.2384 0.1461  9   SER   F O   
9344  C  CB  . SER   F  13  ? 1.7453 0.5568 1.2398 0.0849  -0.2369 -0.0846 9   SER   F CB  
9345  O  OG  . SER   F  13  ? 1.6602 0.4498 1.2061 0.1498  -0.2231 -0.1744 9   SER   F OG  
9346  N  N   . VAL   F  14  ? 1.8261 0.5708 1.2984 0.1079  -0.2459 0.0629  10  VAL   F N   
9347  C  CA  . VAL   F  14  ? 1.8343 0.5504 1.2607 0.1094  -0.2411 -0.0059 10  VAL   F CA  
9348  C  C   . VAL   F  14  ? 1.8880 0.5074 1.2123 0.0985  -0.2925 0.0641  10  VAL   F C   
9349  O  O   . VAL   F  14  ? 1.8840 0.6224 0.9762 -0.0471 -0.2416 0.1871  10  VAL   F O   
9350  C  CB  . VAL   F  14  ? 1.8254 0.5316 1.3361 0.1262  -0.2406 0.0035  10  VAL   F CB  
9351  C  CG1 . VAL   F  14  ? 1.8072 0.6280 1.3528 0.0690  -0.2237 -0.0573 10  VAL   F CG1 
9352  C  CG2 . VAL   F  14  ? 1.8092 0.5241 1.3546 0.1336  -0.2421 -0.0090 10  VAL   F CG2 
9353  N  N   . PHE   F  15  ? 1.8526 0.4392 1.1867 0.1779  -0.2551 0.0191  11  PHE   F N   
9354  C  CA  . PHE   F  15  ? 1.8486 0.5602 1.1848 0.1420  -0.2495 -0.0097 11  PHE   F CA  
9355  C  C   . PHE   F  15  ? 1.9013 0.5759 1.1775 0.1754  -0.2295 0.0068  11  PHE   F C   
9356  O  O   . PHE   F  15  ? 1.9481 0.8043 1.2046 0.1402  -0.1862 0.0266  11  PHE   F O   
9357  C  CB  . PHE   F  15  ? 1.8526 0.5294 1.1387 0.1093  -0.2862 -0.0549 11  PHE   F CB  
9358  C  CG  . PHE   F  15  ? 1.8523 0.5671 1.0705 0.0977  -0.2732 -0.0335 11  PHE   F CG  
9359  C  CD1 . PHE   F  15  ? 1.8355 0.5747 1.0789 0.0933  -0.2530 -0.0608 11  PHE   F CD1 
9360  C  CD2 . PHE   F  15  ? 1.8539 0.5483 1.0746 0.1337  -0.2737 0.0216  11  PHE   F CD2 
9361  C  CE1 . PHE   F  15  ? 1.8126 0.5703 1.0710 0.1563  -0.2468 -0.0737 11  PHE   F CE1 
9362  C  CE2 . PHE   F  15  ? 1.8489 0.5199 1.0827 0.1417  -0.2840 -0.0011 11  PHE   F CE2 
9363  C  CZ  . PHE   F  15  ? 1.8292 0.5021 1.0778 0.1739  -0.2779 -0.0342 11  PHE   F CZ  
9364  N  N   . SER   F  16  ? 1.8917 0.6052 1.2001 0.1856  -0.1748 0.0373  12  SER   F N   
9365  C  CA  . SER   F  16  ? 1.7936 0.6040 1.2660 0.1584  -0.1548 0.0297  12  SER   F CA  
9366  C  C   . SER   F  16  ? 1.7859 0.5548 1.2781 0.1678  -0.1742 0.0944  12  SER   F C   
9367  O  O   . SER   F  16  ? 1.7637 0.5551 1.2404 0.1341  -0.2048 0.0894  12  SER   F O   
9368  C  CB  . SER   F  16  ? 1.8124 0.5879 1.2915 0.1344  -0.1321 -0.0063 12  SER   F CB  
9369  O  OG  . SER   F  16  ? 1.7761 0.5957 1.2734 0.1219  -0.1808 -0.0582 12  SER   F OG  
9370  N  N   . PRO   F  17  ? 1.7760 0.5411 1.3514 0.1924  -0.1812 0.0938  13  PRO   F N   
9371  C  CA  . PRO   F  17  ? 1.7941 0.4747 1.3284 0.1798  -0.1826 0.0936  13  PRO   F CA  
9372  C  C   . PRO   F  17  ? 1.7996 0.3695 1.3344 0.1483  -0.1698 0.1079  13  PRO   F C   
9373  O  O   . PRO   F  17  ? 1.8085 0.2141 1.2645 0.0829  -0.1718 0.1539  13  PRO   F O   
9374  C  CB  . PRO   F  17  ? 1.8057 0.4782 1.3902 0.1768  -0.1963 0.1061  13  PRO   F CB  
9375  C  CG  . PRO   F  17  ? 1.8091 0.5327 1.4233 0.1724  -0.2150 0.1076  13  PRO   F CG  
9376  C  CD  . PRO   F  17  ? 1.7966 0.5294 1.4338 0.1947  -0.1870 0.1134  13  PRO   F CD  
9377  N  N   . ASP   F  18  ? 1.8255 0.4192 1.4437 0.1889  -0.1160 0.1030  14  ASP   F N   
9378  C  CA  . ASP   F  18  ? 1.9346 0.6382 1.4168 0.1911  -0.0884 0.0361  14  ASP   F CA  
9379  C  C   . ASP   F  18  ? 1.9320 0.6618 1.3616 0.2315  -0.0736 0.0116  14  ASP   F C   
9380  O  O   . ASP   F  18  ? 1.9395 0.7468 1.2821 0.2443  -0.0038 0.0199  14  ASP   F O   
9381  C  CB  . ASP   F  18  ? 1.9697 0.6396 1.5073 0.2453  -0.0461 -0.0245 14  ASP   F CB  
9382  C  CG  . ASP   F  18  ? 2.0813 0.5352 1.6050 0.2970  -0.0043 -0.1146 14  ASP   F CG  
9383  O  OD1 . ASP   F  18  ? 2.1405 0.7334 1.6565 0.2837  0.0547  -0.2638 14  ASP   F OD1 
9384  O  OD2 . ASP   F  18  ? 2.2433 0.6425 1.6490 0.2601  -0.0569 -0.2600 14  ASP   F OD2 
9385  N  N   . GLY   F  19  ? 1.9517 0.6083 1.4101 0.1821  -0.0691 0.0141  15  GLY   F N   
9386  C  CA  . GLY   F  19  ? 1.9255 0.5908 1.3416 0.0629  -0.0808 0.0578  15  GLY   F CA  
9387  C  C   . GLY   F  19  ? 1.9142 0.6834 1.3289 0.0513  -0.0762 0.0613  15  GLY   F C   
9388  O  O   . GLY   F  19  ? 1.9287 0.8029 1.2951 -0.0028 -0.0674 0.1448  15  GLY   F O   
9389  N  N   . ARG   F  20  ? 1.9566 0.4887 1.3535 0.0628  -0.0631 0.0467  16  ARG   F N   
9390  C  CA  . ARG   F  20  ? 1.9817 0.4762 1.3959 0.0318  -0.0701 0.0064  16  ARG   F CA  
9391  C  C   . ARG   F  20  ? 2.0350 0.3536 1.5661 -0.0573 -0.1459 -0.0991 16  ARG   F C   
9392  O  O   . ARG   F  20  ? 2.1318 0.0759 1.7312 -0.1606 -0.0435 -0.1481 16  ARG   F O   
9393  C  CB  . ARG   F  20  ? 1.9706 0.5085 1.3558 0.0341  -0.0592 0.0142  16  ARG   F CB  
9394  C  CG  . ARG   F  20  ? 1.9613 0.5899 1.3687 0.0060  -0.1022 0.0197  16  ARG   F CG  
9395  C  CD  . ARG   F  20  ? 1.8887 0.6121 1.3734 0.0376  -0.1211 -0.0006 16  ARG   F CD  
9396  N  NE  . ARG   F  20  ? 1.8808 0.6259 1.3808 0.0586  -0.1179 -0.0436 16  ARG   F NE  
9397  C  CZ  . ARG   F  20  ? 1.8007 0.6895 1.4377 0.1279  -0.1415 -0.1150 16  ARG   F CZ  
9398  N  NH1 . ARG   F  20  ? 1.8135 0.8144 1.4460 0.0463  -0.1662 -0.1223 16  ARG   F NH1 
9399  N  NH2 . ARG   F  20  ? 1.7925 0.7733 1.5183 0.1719  -0.0930 -0.1299 16  ARG   F NH2 
9400  N  N   . ASN   F  21  ? 2.0225 0.3956 1.5629 -0.0741 -0.2181 -0.0978 17  ASN   F N   
9401  C  CA  . ASN   F  21  ? 1.9335 0.5196 1.5829 0.0047  -0.2730 -0.1000 17  ASN   F CA  
9402  C  C   . ASN   F  21  ? 1.9800 0.2731 1.5195 0.0593  -0.3636 -0.0498 17  ASN   F C   
9403  O  O   . ASN   F  21  ? 1.8198 0.5099 1.4706 0.1273  -0.3313 -0.0470 17  ASN   F O   
9404  C  CB  . ASN   F  21  ? 2.0146 0.5202 1.4777 -0.0206 -0.3071 -0.1862 17  ASN   F CB  
9405  C  CG  . ASN   F  21  ? 2.0683 0.6084 1.5477 -0.0287 -0.2885 -0.3044 17  ASN   F CG  
9406  O  OD1 . ASN   F  21  ? 2.1003 0.6434 1.5070 -0.0817 -0.3559 -0.3478 17  ASN   F OD1 
9407  N  ND2 . ASN   F  21  ? 2.0721 0.6076 1.6731 0.0092  -0.2561 -0.2541 17  ASN   F ND2 
9408  N  N   . PHE   F  22  ? 1.9562 0.1790 1.5477 0.0657  -0.4512 -0.1409 18  PHE   F N   
9409  C  CA  . PHE   F  22  ? 1.9659 0.2484 1.4832 0.0625  -0.4026 -0.1197 18  PHE   F CA  
9410  C  C   . PHE   F  22  ? 2.0336 0.1132 1.4421 0.0447  -0.3624 -0.0918 18  PHE   F C   
9411  O  O   . PHE   F  22  ? 2.1078 0.0828 1.4057 0.0187  -0.3043 -0.1074 18  PHE   F O   
9412  C  CB  . PHE   F  22  ? 1.9578 0.3421 1.4791 -0.0040 -0.4257 -0.0587 18  PHE   F CB  
9413  C  CG  . PHE   F  22  ? 1.8845 0.2526 1.5320 0.0785  -0.4390 -0.0462 18  PHE   F CG  
9414  C  CD1 . PHE   F  22  ? 1.8918 0.1972 1.5495 0.0717  -0.4590 -0.0489 18  PHE   F CD1 
9415  C  CD2 . PHE   F  22  ? 1.8970 0.2825 1.5330 0.0299  -0.4763 -0.0498 18  PHE   F CD2 
9416  C  CE1 . PHE   F  22  ? 1.8737 0.2481 1.5235 0.0825  -0.4459 -0.0899 18  PHE   F CE1 
9417  C  CE2 . PHE   F  22  ? 1.8770 0.1701 1.5432 0.0785  -0.4443 -0.0225 18  PHE   F CE2 
9418  C  CZ  . PHE   F  22  ? 1.8692 0.2499 1.5239 0.1035  -0.4337 -0.0423 18  PHE   F CZ  
9419  N  N   . GLN   F  23  ? 2.0747 0.0403 1.4425 0.1281  -0.3274 -0.0423 19  GLN   F N   
9420  C  CA  . GLN   F  23  ? 2.0319 0.1510 1.3532 0.1126  -0.2663 -0.0732 19  GLN   F CA  
9421  C  C   . GLN   F  23  ? 2.0311 0.1496 1.3244 0.1540  -0.2541 -0.0683 19  GLN   F C   
9422  O  O   . GLN   F  23  ? 2.0161 0.0622 1.2586 0.2217  -0.2396 -0.0246 19  GLN   F O   
9423  C  CB  . GLN   F  23  ? 2.0469 0.3409 1.3079 0.1609  -0.2025 -0.0405 19  GLN   F CB  
9424  C  CG  . GLN   F  23  ? 2.0362 0.3714 1.3171 0.1183  -0.1773 -0.0084 19  GLN   F CG  
9425  C  CD  . GLN   F  23  ? 2.0196 0.3052 1.2777 0.1472  -0.1621 0.0062  19  GLN   F CD  
9426  O  OE1 . GLN   F  23  ? 1.9310 0.2688 1.2492 0.1316  -0.1000 -0.0239 19  GLN   F OE1 
9427  N  NE2 . GLN   F  23  ? 1.9332 0.5479 1.2692 -0.0400 -0.1621 -0.0351 19  GLN   F NE2 
9428  N  N   . VAL   F  24  ? 1.9299 0.1607 1.3120 0.0866  -0.2337 -0.0579 20  VAL   F N   
9429  C  CA  . VAL   F  24  ? 1.8859 0.1833 1.3854 0.0290  -0.2127 -0.0320 20  VAL   F CA  
9430  C  C   . VAL   F  24  ? 1.8989 0.1128 1.4632 0.0352  -0.2021 -0.0288 20  VAL   F C   
9431  O  O   . VAL   F  24  ? 1.9980 0.0445 1.5111 -0.0677 -0.2392 -0.0553 20  VAL   F O   
9432  C  CB  . VAL   F  24  ? 1.8105 0.3570 1.3444 0.0065  -0.1961 -0.0177 20  VAL   F CB  
9433  C  CG1 . VAL   F  24  ? 1.8024 0.4640 1.3549 0.0046  -0.1739 -0.0026 20  VAL   F CG1 
9434  C  CG2 . VAL   F  24  ? 1.7913 0.4423 1.2704 0.0102  -0.1835 -0.0191 20  VAL   F CG2 
9435  N  N   . GLU   F  25  ? 1.8982 0.1848 1.5243 0.0219  -0.2809 -0.0824 21  GLU   F N   
9436  C  CA  . GLU   F  25  ? 1.8614 0.2083 1.5462 0.1104  -0.2610 -0.0180 21  GLU   F CA  
9437  C  C   . GLU   F  25  ? 1.8299 0.1869 1.4787 0.1147  -0.2123 -0.0440 21  GLU   F C   
9438  O  O   . GLU   F  25  ? 1.8258 0.1509 1.5419 0.1034  -0.1640 -0.0163 21  GLU   F O   
9439  C  CB  . GLU   F  25  ? 1.8418 0.1706 1.6251 0.1338  -0.3166 0.0629  21  GLU   F CB  
9440  C  CG  . GLU   F  25  ? 1.8664 0.3769 1.6980 0.1730  -0.3455 0.1020  21  GLU   F CG  
9441  C  CD  . GLU   F  25  ? 1.7891 0.5939 1.7782 0.0964  -0.4103 0.0872  21  GLU   F CD  
9442  O  OE1 . GLU   F  25  ? 1.8024 0.6587 1.8236 0.1760  -0.4214 0.0495  21  GLU   F OE1 
9443  O  OE2 . GLU   F  25  ? 1.8054 0.9257 1.8924 0.0968  -0.4894 0.1136  21  GLU   F OE2 
9444  N  N   . TYR   F  26  ? 1.8220 0.2855 1.4770 0.0785  -0.2372 -0.0438 22  TYR   F N   
9445  C  CA  . TYR   F  26  ? 1.8149 0.4223 1.4857 0.0981  -0.2338 -0.0642 22  TYR   F CA  
9446  C  C   . TYR   F  26  ? 1.7356 0.4420 1.4555 0.1387  -0.2206 -0.0206 22  TYR   F C   
9447  O  O   . TYR   F  26  ? 1.7772 0.5694 1.4857 0.2363  -0.1886 -0.0782 22  TYR   F O   
9448  C  CB  . TYR   F  26  ? 1.8637 0.4900 1.5114 0.0328  -0.1970 -0.0605 22  TYR   F CB  
9449  C  CG  . TYR   F  26  ? 1.9015 0.5091 1.5333 0.0067  -0.1688 -0.0724 22  TYR   F CG  
9450  C  CD1 . TYR   F  26  ? 1.9185 0.4752 1.5145 0.0329  -0.1465 -0.0764 22  TYR   F CD1 
9451  C  CD2 . TYR   F  26  ? 1.9228 0.5645 1.5674 0.0002  -0.1454 -0.0208 22  TYR   F CD2 
9452  C  CE1 . TYR   F  26  ? 1.9671 0.4582 1.5338 0.0256  -0.1432 -0.0894 22  TYR   F CE1 
9453  C  CE2 . TYR   F  26  ? 1.9633 0.5152 1.5299 0.0238  -0.1522 -0.0558 22  TYR   F CE2 
9454  C  CZ  . TYR   F  26  ? 1.9863 0.4535 1.5539 0.0099  -0.1346 -0.0617 22  TYR   F CZ  
9455  O  OH  . TYR   F  26  ? 2.0655 0.4765 1.5071 0.0307  -0.1487 0.0771  22  TYR   F OH  
9456  N  N   . ALA   F  27  ? 1.7564 0.4200 1.4065 0.1256  -0.2633 0.0153  23  ALA   F N   
9457  C  CA  . ALA   F  27  ? 1.7422 0.4329 1.3547 0.1114  -0.2789 -0.0234 23  ALA   F CA  
9458  C  C   . ALA   F  27  ? 1.7440 0.3494 1.3482 0.1134  -0.2729 -0.0523 23  ALA   F C   
9459  O  O   . ALA   F  27  ? 1.7003 0.4040 1.2213 0.1386  -0.3068 -0.0889 23  ALA   F O   
9460  C  CB  . ALA   F  27  ? 1.7012 0.5556 1.3649 0.1865  -0.3001 -0.0339 23  ALA   F CB  
9461  N  N   . VAL   F  28  ? 1.8054 0.2292 1.3121 0.0846  -0.2325 -0.0735 24  VAL   F N   
9462  C  CA  . VAL   F  28  ? 1.8257 0.2789 1.3253 0.0324  -0.2064 -0.0736 24  VAL   F CA  
9463  C  C   . VAL   F  28  ? 1.7931 0.3460 1.4007 0.0210  -0.1673 -0.0567 24  VAL   F C   
9464  O  O   . VAL   F  28  ? 1.8681 0.2707 1.4109 -0.0785 -0.1757 0.0333  24  VAL   F O   
9465  C  CB  . VAL   F  28  ? 1.8063 0.2916 1.3336 0.0422  -0.2070 -0.0747 24  VAL   F CB  
9466  C  CG1 . VAL   F  28  ? 1.8041 0.3618 1.3454 0.0853  -0.1756 -0.0522 24  VAL   F CG1 
9467  C  CG2 . VAL   F  28  ? 1.7637 0.2931 1.2882 0.0178  -0.2182 -0.1379 24  VAL   F CG2 
9468  N  N   . LYS   F  29  ? 1.8711 0.4931 1.3838 0.0236  -0.2046 0.0178  25  LYS   F N   
9469  C  CA  . LYS   F  29  ? 1.8256 0.6701 1.4459 0.0639  -0.1904 -0.0532 25  LYS   F CA  
9470  C  C   . LYS   F  29  ? 1.8335 0.6015 1.3968 0.0404  -0.1351 -0.0355 25  LYS   F C   
9471  O  O   . LYS   F  29  ? 1.8013 0.6950 1.3818 -0.0048 -0.1227 -0.0226 25  LYS   F O   
9472  C  CB  . LYS   F  29  ? 1.8970 0.7339 1.4633 0.0669  -0.1669 -0.0233 25  LYS   F CB  
9473  C  CG  . LYS   F  29  ? 1.9170 0.7582 1.4987 0.0772  -0.1736 -0.1034 25  LYS   F CG  
9474  C  CD  . LYS   F  29  ? 1.9955 0.8044 1.5548 0.1373  -0.1898 -0.1561 25  LYS   F CD  
9475  C  CE  . LYS   F  29  ? 2.0073 0.8598 1.5994 0.1281  -0.1984 -0.1996 25  LYS   F CE  
9476  N  NZ  . LYS   F  29  ? 2.0739 0.9765 1.6452 0.2411  -0.1427 -0.2239 25  LYS   F NZ  
9477  N  N   . ALA   F  30  ? 1.8624 0.5683 1.4097 0.0150  -0.1312 -0.0296 26  ALA   F N   
9478  C  CA  . ALA   F  30  ? 1.8136 0.6255 1.4994 0.0352  -0.1218 -0.0473 26  ALA   F CA  
9479  C  C   . ALA   F  30  ? 1.8160 0.6668 1.4432 0.0815  -0.1254 -0.0542 26  ALA   F C   
9480  O  O   . ALA   F  30  ? 1.7966 0.6350 1.4819 0.1554  -0.0844 0.0150  26  ALA   F O   
9481  C  CB  . ALA   F  30  ? 1.8293 0.5999 1.5197 0.0655  -0.0990 -0.0329 26  ALA   F CB  
9482  N  N   . VAL   F  31  ? 1.8054 0.6987 1.4254 0.0783  -0.1638 -0.1546 27  VAL   F N   
9483  C  CA  . VAL   F  31  ? 1.8015 0.7218 1.4515 0.0366  -0.1097 -0.1712 27  VAL   F CA  
9484  C  C   . VAL   F  31  ? 1.7612 0.7186 1.5708 0.0501  -0.0734 -0.1816 27  VAL   F C   
9485  O  O   . VAL   F  31  ? 1.7775 0.8133 1.6417 0.0450  -0.0276 -0.1778 27  VAL   F O   
9486  C  CB  . VAL   F  31  ? 1.8036 0.8165 1.4305 0.0359  -0.1392 -0.2128 27  VAL   F CB  
9487  C  CG1 . VAL   F  31  ? 1.8222 0.8619 1.4231 0.0375  -0.1028 -0.2151 27  VAL   F CG1 
9488  C  CG2 . VAL   F  31  ? 1.8212 0.8831 1.3878 0.0075  -0.1339 -0.2309 27  VAL   F CG2 
9489  N  N   . GLU   F  32  ? 1.7680 0.6563 1.6174 0.0994  -0.0641 -0.1714 28  GLU   F N   
9490  C  CA  . GLU   F  32  ? 1.7886 0.5634 1.6283 0.1211  -0.0698 -0.1318 28  GLU   F CA  
9491  C  C   . GLU   F  32  ? 1.7744 0.4504 1.5539 0.0999  -0.0446 -0.1370 28  GLU   F C   
9492  O  O   . GLU   F  32  ? 1.7689 0.4748 1.5104 0.0557  -0.0382 -0.0666 28  GLU   F O   
9493  C  CB  . GLU   F  32  ? 1.8229 0.6017 1.7481 0.0852  -0.0533 -0.0987 28  GLU   F CB  
9494  C  CG  . GLU   F  32  ? 1.8516 0.6564 1.8192 0.1315  -0.0693 -0.0821 28  GLU   F CG  
9495  C  CD  . GLU   F  32  ? 1.8472 0.8834 1.9863 -0.0001 -0.0968 -0.1967 28  GLU   F CD  
9496  O  OE1 . GLU   F  32  ? 2.0256 0.9827 2.0944 0.0258  -0.1309 -0.1263 28  GLU   F OE1 
9497  O  OE2 . GLU   F  32  ? 1.9548 0.6604 1.9666 0.0743  -0.1925 -0.1673 28  GLU   F OE2 
9498  N  N   . ASN   F  33  ? 1.8109 0.5104 1.5699 0.0769  -0.0779 -0.1933 29  ASN   F N   
9499  C  CA  . ASN   F  33  ? 1.8173 0.7390 1.6046 0.0878  -0.1025 -0.2380 29  ASN   F CA  
9500  C  C   . ASN   F  33  ? 1.8504 0.7591 1.5640 0.0849  -0.0717 -0.2316 29  ASN   F C   
9501  O  O   . ASN   F  33  ? 1.8591 0.9989 1.5965 0.1429  -0.1228 -0.2551 29  ASN   F O   
9502  C  CB  . ASN   F  33  ? 1.8347 0.7832 1.6098 0.0856  -0.1129 -0.2255 29  ASN   F CB  
9503  C  CG  . ASN   F  33  ? 1.8709 0.8619 1.6683 0.1180  -0.1333 -0.1860 29  ASN   F CG  
9504  O  OD1 . ASN   F  33  ? 1.8754 0.8828 1.6239 0.1171  -0.1578 -0.1361 29  ASN   F OD1 
9505  N  ND2 . ASN   F  33  ? 1.9273 0.9128 1.7283 0.1332  -0.1422 -0.2661 29  ASN   F ND2 
9506  N  N   . GLY   F  34  ? 1.8439 0.7656 1.4963 0.0937  -0.0648 -0.2418 30  GLY   F N   
9507  C  CA  . GLY   F  34  ? 1.8496 0.8243 1.4921 0.0521  -0.0162 -0.2558 30  GLY   F CA  
9508  C  C   . GLY   F  34  ? 1.8724 0.9048 1.5232 0.0658  0.0256  -0.2756 30  GLY   F C   
9509  O  O   . GLY   F  34  ? 1.8183 0.8617 1.5637 -0.0323 -0.0019 -0.2183 30  GLY   F O   
9510  N  N   . THR   F  35  ? 1.8485 0.9403 1.5675 0.0846  0.0895  -0.2626 31  THR   F N   
9511  C  CA  . THR   F  35  ? 1.8660 0.9039 1.5859 0.1355  0.1021  -0.2097 31  THR   F CA  
9512  C  C   . THR   F  35  ? 1.9160 0.7860 1.6195 0.1156  0.0848  -0.1677 31  THR   F C   
9513  O  O   . THR   F  35  ? 1.9311 0.6767 1.4758 0.1131  0.0732  -0.1374 31  THR   F O   
9514  C  CB  . THR   F  35  ? 1.8173 0.8871 1.6160 0.1576  0.1881  -0.2017 31  THR   F CB  
9515  O  OG1 . THR   F  35  ? 1.7738 0.8875 1.5306 0.1313  0.2121  -0.2701 31  THR   F OG1 
9516  C  CG2 . THR   F  35  ? 1.8158 0.9843 1.6267 0.1666  0.1859  -0.1952 31  THR   F CG2 
9517  N  N   . THR   F  36  ? 1.9432 0.7882 1.6220 0.0945  0.0783  -0.1548 32  THR   F N   
9518  C  CA  . THR   F  36  ? 1.9139 0.8401 1.7151 0.1080  0.0242  -0.1647 32  THR   F CA  
9519  C  C   . THR   F  36  ? 1.8157 0.8448 1.7437 0.1472  0.0437  -0.1033 32  THR   F C   
9520  O  O   . THR   F  36  ? 1.8191 0.7457 1.8700 0.1536  0.0634  -0.0513 32  THR   F O   
9521  C  CB  . THR   F  36  ? 1.9604 0.9948 1.7019 0.0598  -0.0076 -0.2342 32  THR   F CB  
9522  O  OG1 . THR   F  36  ? 2.0327 1.0063 1.7629 0.0478  -0.0604 -0.2449 32  THR   F OG1 
9523  C  CG2 . THR   F  36  ? 1.9930 0.9039 1.6441 0.0672  -0.0010 -0.2633 32  THR   F CG2 
9524  N  N   . SER   F  37  ? 1.8636 0.7135 1.6846 0.1678  0.0885  -0.0498 33  SER   F N   
9525  C  CA  . SER   F  37  ? 1.8750 0.6840 1.6316 0.1505  0.1637  -0.0859 33  SER   F CA  
9526  C  C   . SER   F  37  ? 1.9173 0.7325 1.6178 0.1789  0.1559  -0.1390 33  SER   F C   
9527  O  O   . SER   F  37  ? 1.9746 0.6739 1.6286 0.1777  0.2141  -0.1420 33  SER   F O   
9528  C  CB  . SER   F  37  ? 1.8485 0.5586 1.6060 0.1612  0.1590  -0.0287 33  SER   F CB  
9529  O  OG  . SER   F  37  ? 1.8897 0.3624 1.5298 0.2228  0.1944  0.0071  33  SER   F OG  
9530  N  N   . ILE   F  38  ? 1.8545 0.7817 1.5374 0.1850  0.1161  -0.1463 34  ILE   F N   
9531  C  CA  . ILE   F  38  ? 1.8560 0.7955 1.5162 0.1823  0.1095  -0.2135 34  ILE   F CA  
9532  C  C   . ILE   F  38  ? 1.8436 0.8157 1.5049 0.2065  0.1008  -0.1941 34  ILE   F C   
9533  O  O   . ILE   F  38  ? 1.8384 0.7705 1.5263 0.2336  0.1292  -0.2195 34  ILE   F O   
9534  C  CB  . ILE   F  38  ? 1.8482 0.7943 1.4841 0.1413  0.0831  -0.2404 34  ILE   F CB  
9535  C  CG1 . ILE   F  38  ? 1.8668 0.7670 1.4350 0.1158  0.0875  -0.2484 34  ILE   F CG1 
9536  C  CG2 . ILE   F  38  ? 1.9068 0.7981 1.5116 0.1592  0.0939  -0.2619 34  ILE   F CG2 
9537  C  CD1 . ILE   F  38  ? 1.8620 0.7593 1.4231 0.1006  0.0756  -0.2557 34  ILE   F CD1 
9538  N  N   . GLY   F  39  ? 1.8380 0.8840 1.4403 0.1618  0.1061  -0.2294 35  GLY   F N   
9539  C  CA  . GLY   F  39  ? 1.7680 0.9098 1.3655 0.1307  0.0998  -0.2020 35  GLY   F CA  
9540  C  C   . GLY   F  39  ? 1.7180 0.8816 1.3770 0.0792  0.0806  -0.2344 35  GLY   F C   
9541  O  O   . GLY   F  39  ? 1.6854 0.8497 1.3254 0.1141  0.0955  -0.2658 35  GLY   F O   
9542  N  N   . ILE   F  40  ? 1.7391 0.8745 1.4081 0.0638  0.0349  -0.1891 36  ILE   F N   
9543  C  CA  . ILE   F  40  ? 1.7508 0.8683 1.4121 0.0332  0.0287  -0.1714 36  ILE   F CA  
9544  C  C   . ILE   F  40  ? 1.7351 0.8558 1.3795 0.0204  0.0307  -0.2031 36  ILE   F C   
9545  O  O   . ILE   F  40  ? 1.7219 0.8113 1.3574 0.0737  0.0318  -0.2780 36  ILE   F O   
9546  C  CB  . ILE   F  40  ? 1.7371 0.8937 1.4658 0.0154  0.0514  -0.1161 36  ILE   F CB  
9547  C  CG1 . ILE   F  40  ? 1.7395 0.9774 1.5484 0.0381  0.0272  -0.0531 36  ILE   F CG1 
9548  C  CG2 . ILE   F  40  ? 1.7415 0.8231 1.4729 -0.0054 0.0370  -0.0797 36  ILE   F CG2 
9549  C  CD1 . ILE   F  40  ? 1.7579 1.0911 1.6054 0.0094  0.0676  -0.0366 36  ILE   F CD1 
9550  N  N   . LYS   F  41  ? 1.7455 0.8927 1.3558 0.0249  0.0291  -0.2004 37  LYS   F N   
9551  C  CA  . LYS   F  41  ? 1.8376 0.8165 1.3356 -0.0043 0.0274  -0.2092 37  LYS   F CA  
9552  C  C   . LYS   F  41  ? 1.9209 0.8268 1.3407 0.0179  0.0154  -0.1486 37  LYS   F C   
9553  O  O   . LYS   F  41  ? 2.0023 0.7489 1.4243 0.0239  0.0750  -0.1039 37  LYS   F O   
9554  C  CB  . LYS   F  41  ? 1.8275 0.8130 1.3281 0.0302  -0.0074 -0.1714 37  LYS   F CB  
9555  C  CG  . LYS   F  41  ? 1.8451 0.8235 1.3167 0.0322  -0.0362 -0.1536 37  LYS   F CG  
9556  C  CD  . LYS   F  41  ? 1.8505 0.9218 1.3713 0.0428  -0.0613 -0.1538 37  LYS   F CD  
9557  C  CE  . LYS   F  41  ? 1.8927 0.9415 1.3923 0.0698  -0.0648 -0.1741 37  LYS   F CE  
9558  N  NZ  . LYS   F  41  ? 1.9032 1.0648 1.4159 0.0497  -0.0675 -0.1749 37  LYS   F NZ  
9559  N  N   . CYS   F  42  ? 1.9799 0.7272 1.3659 0.0176  -0.0456 -0.3201 38  CYS   F N   
9560  C  CA  . CYS   F  42  ? 2.0383 0.8242 1.3900 0.0655  -0.0065 -0.3008 38  CYS   F CA  
9561  C  C   . CYS   F  42  ? 2.0283 0.8918 1.3374 0.0401  -0.0745 -0.2642 38  CYS   F C   
9562  O  O   . CYS   F  42  ? 1.9487 0.8592 1.2239 -0.0229 -0.1522 -0.2853 38  CYS   F O   
9563  C  CB  . CYS   F  42  ? 2.0069 0.9497 1.4628 0.1231  0.0375  -0.2627 38  CYS   F CB  
9564  S  SG  . CYS   F  42  ? 2.1083 0.8800 1.4738 0.1335  0.0505  -0.1979 38  CYS   F SG  
9565  N  N   . ASN   F  43  ? 2.0956 1.0876 1.3088 0.1061  -0.0279 -0.2509 39  ASN   F N   
9566  C  CA  . ASN   F  43  ? 2.1403 1.1855 1.3034 0.1560  -0.0121 -0.2177 39  ASN   F CA  
9567  C  C   . ASN   F  43  ? 2.0634 1.0266 1.4165 0.1335  -0.0688 -0.2011 39  ASN   F C   
9568  O  O   . ASN   F  43  ? 2.0701 0.8376 1.4601 0.1403  -0.1306 -0.2124 39  ASN   F O   
9569  C  CB  . ASN   F  43  ? 2.2171 1.3472 1.2222 0.2029  0.0439  -0.2189 39  ASN   F CB  
9570  C  CG  . ASN   F  43  ? 2.3204 1.5044 1.1826 0.2239  0.0133  -0.2494 39  ASN   F CG  
9571  O  OD1 . ASN   F  43  ? 2.2817 1.5914 1.0267 0.2218  -0.0219 -0.2066 39  ASN   F OD1 
9572  N  ND2 . ASN   F  43  ? 2.3475 1.6662 1.2588 0.2347  0.0419  -0.2032 39  ASN   F ND2 
9573  N  N   . ASP   F  44  ? 2.1387 0.9692 1.4428 0.0591  -0.0641 -0.1745 40  ASP   F N   
9574  C  CA  . ASP   F  44  ? 2.1624 1.0719 1.3585 0.0810  -0.0075 -0.1983 40  ASP   F CA  
9575  C  C   . ASP   F  44  ? 2.2338 0.9962 1.3382 0.0391  0.0467  -0.1256 40  ASP   F C   
9576  O  O   . ASP   F  44  ? 2.3586 0.9527 1.3899 -0.0095 0.0558  -0.0891 40  ASP   F O   
9577  C  CB  . ASP   F  44  ? 2.1329 1.1722 1.3576 0.0282  0.0391  -0.2093 40  ASP   F CB  
9578  C  CG  . ASP   F  44  ? 2.1310 1.2340 1.3965 0.0160  0.0854  -0.2446 40  ASP   F CG  
9579  O  OD1 . ASP   F  44  ? 2.1057 1.3435 1.5394 0.0837  0.1141  -0.1651 40  ASP   F OD1 
9580  O  OD2 . ASP   F  44  ? 2.1761 1.1319 1.3385 0.0687  0.1397  -0.3191 40  ASP   F OD2 
9581  N  N   . GLY   F  45  ? 2.1906 0.9214 1.3631 0.0179  0.0683  -0.2043 41  GLY   F N   
9582  C  CA  . GLY   F  45  ? 2.0971 0.8795 1.4012 0.0642  0.0248  -0.2112 41  GLY   F CA  
9583  C  C   . GLY   F  45  ? 2.0543 0.8797 1.3469 0.1218  0.0227  -0.2161 41  GLY   F C   
9584  O  O   . GLY   F  45  ? 2.0158 0.8504 1.3761 0.1834  0.0121  -0.2242 41  GLY   F O   
9585  N  N   . VAL   F  46  ? 1.9651 0.8193 1.3042 0.0408  0.0341  -0.2680 42  VAL   F N   
9586  C  CA  . VAL   F  46  ? 1.9252 0.8491 1.2928 0.0145  0.0240  -0.2358 42  VAL   F CA  
9587  C  C   . VAL   F  46  ? 1.9112 0.8761 1.3761 -0.0068 0.0332  -0.2020 42  VAL   F C   
9588  O  O   . VAL   F  46  ? 1.8870 0.8742 1.4922 -0.0234 0.0768  -0.1624 42  VAL   F O   
9589  C  CB  . VAL   F  46  ? 1.9199 0.8840 1.2793 0.0145  0.0141  -0.2375 42  VAL   F CB  
9590  C  CG1 . VAL   F  46  ? 1.9169 0.9029 1.2589 0.0131  0.0230  -0.2491 42  VAL   F CG1 
9591  C  CG2 . VAL   F  46  ? 1.9477 0.8927 1.2622 0.0162  0.0131  -0.2269 42  VAL   F CG2 
9592  N  N   . VAL   F  47  ? 1.9241 0.8882 1.4288 0.0081  0.0370  -0.1768 43  VAL   F N   
9593  C  CA  . VAL   F  47  ? 1.9220 0.8776 1.4671 0.0078  0.0422  -0.1852 43  VAL   F CA  
9594  C  C   . VAL   F  47  ? 1.9251 0.8774 1.5157 -0.0194 0.0242  -0.1654 43  VAL   F C   
9595  O  O   . VAL   F  47  ? 1.9894 0.8636 1.5238 -0.0329 0.0296  -0.1973 43  VAL   F O   
9596  C  CB  . VAL   F  47  ? 1.9814 0.8670 1.4284 0.0039  0.0472  -0.1765 43  VAL   F CB  
9597  C  CG1 . VAL   F  47  ? 1.9569 0.8957 1.4624 0.0170  0.0676  -0.2233 43  VAL   F CG1 
9598  C  CG2 . VAL   F  47  ? 1.9906 0.8582 1.3941 -0.0250 0.0497  -0.1942 43  VAL   F CG2 
9599  N  N   . PHE   F  48  ? 1.8580 0.8092 1.5585 -0.0486 0.0137  -0.1429 44  PHE   F N   
9600  C  CA  . PHE   F  48  ? 1.7851 0.6665 1.5385 -0.0056 0.0153  -0.2105 44  PHE   F CA  
9601  C  C   . PHE   F  48  ? 1.7840 0.5710 1.5261 -0.0196 0.0292  -0.1795 44  PHE   F C   
9602  O  O   . PHE   F  48  ? 1.8484 0.3759 1.5665 -0.0024 -0.0153 -0.1693 44  PHE   F O   
9603  C  CB  . PHE   F  48  ? 1.6986 0.5546 1.5856 0.0027  -0.0310 -0.2588 44  PHE   F CB  
9604  C  CG  . PHE   F  48  ? 1.7185 0.4795 1.5619 0.0136  -0.0264 -0.3878 44  PHE   F CG  
9605  C  CD1 . PHE   F  48  ? 1.6740 0.5578 1.6161 0.0476  -0.0085 -0.3921 44  PHE   F CD1 
9606  C  CD2 . PHE   F  48  ? 1.6492 0.4611 1.5242 0.0015  -0.0599 -0.4499 44  PHE   F CD2 
9607  C  CE1 . PHE   F  48  ? 1.7112 0.4716 1.5867 0.0498  -0.0176 -0.4043 44  PHE   F CE1 
9608  C  CE2 . PHE   F  48  ? 1.6648 0.5044 1.5173 0.0160  -0.0960 -0.4244 44  PHE   F CE2 
9609  C  CZ  . PHE   F  48  ? 1.6858 0.4710 1.5339 0.0148  -0.0623 -0.4045 44  PHE   F CZ  
9610  N  N   . ALA   F  49  ? 1.8409 0.5630 1.4834 0.0328  0.0382  -0.2230 45  ALA   F N   
9611  C  CA  . ALA   F  49  ? 1.8678 0.5395 1.4940 0.0223  -0.0023 -0.1758 45  ALA   F CA  
9612  C  C   . ALA   F  49  ? 1.9034 0.5127 1.4999 -0.0047 -0.0120 -0.1861 45  ALA   F C   
9613  O  O   . ALA   F  49  ? 1.8955 0.4108 1.4208 0.0100  -0.0178 -0.2129 45  ALA   F O   
9614  C  CB  . ALA   F  49  ? 1.8924 0.5675 1.5109 0.0039  0.0220  -0.1858 45  ALA   F CB  
9615  N  N   . VAL   F  50  ? 1.9367 0.6058 1.5421 0.0185  -0.0265 -0.1455 46  VAL   F N   
9616  C  CA  . VAL   F  50  ? 1.9126 0.6697 1.5441 0.1283  -0.0321 -0.1068 46  VAL   F CA  
9617  C  C   . VAL   F  50  ? 1.9261 0.7098 1.6041 0.1627  -0.0247 -0.0523 46  VAL   F C   
9618  O  O   . VAL   F  50  ? 1.8410 0.5999 1.5440 0.2614  -0.0380 -0.0395 46  VAL   F O   
9619  C  CB  . VAL   F  50  ? 1.9477 0.7245 1.5436 0.1111  -0.0057 -0.1151 46  VAL   F CB  
9620  C  CG1 . VAL   F  50  ? 1.9281 0.7456 1.6086 0.0894  -0.0058 -0.0928 46  VAL   F CG1 
9621  C  CG2 . VAL   F  50  ? 2.0040 0.7989 1.5175 0.1471  0.0378  -0.1008 46  VAL   F CG2 
9622  N  N   . GLU   F  51  ? 1.9295 0.6873 1.7245 0.2160  -0.0498 -0.0550 47  GLU   F N   
9623  C  CA  . GLU   F  51  ? 1.9582 0.6929 1.7413 0.2311  -0.0693 -0.0413 47  GLU   F CA  
9624  C  C   . GLU   F  51  ? 1.9219 0.4582 1.7538 0.2044  -0.0790 -0.0842 47  GLU   F C   
9625  O  O   . GLU   F  51  ? 2.0337 0.1792 1.5797 0.2404  -0.0809 -0.2207 47  GLU   F O   
9626  C  CB  . GLU   F  51  ? 1.9317 0.7000 1.7903 0.2578  -0.1106 -0.0452 47  GLU   F CB  
9627  C  CG  . GLU   F  51  ? 1.9633 0.7822 1.8534 0.3193  -0.0915 -0.0094 47  GLU   F CG  
9628  C  CD  . GLU   F  51  ? 1.9488 0.7713 1.8793 0.3358  -0.1250 0.0161  47  GLU   F CD  
9629  O  OE1 . GLU   F  51  ? 2.0298 0.9316 1.9970 0.4543  -0.0644 0.0574  47  GLU   F OE1 
9630  O  OE2 . GLU   F  51  ? 1.9095 0.8033 1.8202 0.4613  -0.1974 0.0874  47  GLU   F OE2 
9631  N  N   . LYS   F  52  ? 1.9388 0.4844 1.7254 0.1571  -0.0885 -0.0800 48  LYS   F N   
9632  C  CA  . LYS   F  52  ? 1.9032 0.6236 1.7517 0.1442  -0.1156 -0.0548 48  LYS   F CA  
9633  C  C   . LYS   F  52  ? 1.8843 0.5316 1.7986 0.0763  -0.1711 -0.0282 48  LYS   F C   
9634  O  O   . LYS   F  52  ? 1.8758 0.4448 1.8672 0.0519  -0.1849 0.0151  48  LYS   F O   
9635  C  CB  . LYS   F  52  ? 1.9440 0.6894 1.7719 0.0737  -0.1106 -0.0143 48  LYS   F CB  
9636  C  CG  . LYS   F  52  ? 1.9752 0.8154 1.7801 0.1575  -0.0937 0.0315  48  LYS   F CG  
9637  C  CD  . LYS   F  52  ? 1.9911 0.8775 1.8136 0.0982  -0.0764 -0.0003 48  LYS   F CD  
9638  C  CE  . LYS   F  52  ? 1.9714 0.9416 1.7908 0.1263  -0.0620 -0.0159 48  LYS   F CE  
9639  N  NZ  . LYS   F  52  ? 1.9541 0.9925 1.7794 0.0924  -0.0149 0.0229  48  LYS   F NZ  
9640  N  N   . LEU   F  53  ? 1.9029 0.6070 1.7968 0.0379  -0.1945 0.0215  49  LEU   F N   
9641  C  CA  . LEU   F  53  ? 1.9548 0.6000 1.7750 0.0521  -0.1634 0.0329  49  LEU   F CA  
9642  C  C   . LEU   F  53  ? 1.9443 0.5827 1.6747 0.0581  -0.1293 0.0380  49  LEU   F C   
9643  O  O   . LEU   F  53  ? 2.0497 0.2038 1.6147 -0.0334 -0.2076 0.1191  49  LEU   F O   
9644  C  CB  . LEU   F  53  ? 1.9863 0.5388 1.7472 0.0467  -0.1622 -0.0197 49  LEU   F CB  
9645  C  CG  . LEU   F  53  ? 2.0218 0.4413 1.7430 0.0960  -0.1604 -0.1023 49  LEU   F CG  
9646  C  CD1 . LEU   F  53  ? 2.0543 0.4296 1.7366 0.0960  -0.1301 -0.1202 49  LEU   F CD1 
9647  C  CD2 . LEU   F  53  ? 2.0466 0.5210 1.7476 0.1249  -0.1460 -0.1045 49  LEU   F CD2 
9648  N  N   . ILE   F  54  ? 1.9260 0.7061 1.7477 0.1327  -0.1363 0.0390  50  ILE   F N   
9649  C  CA  . ILE   F  54  ? 1.8468 0.8408 1.7966 0.1549  -0.0810 -0.0387 50  ILE   F CA  
9650  C  C   . ILE   F  54  ? 1.8525 0.9439 1.7817 0.1757  -0.0362 0.0122  50  ILE   F C   
9651  O  O   . ILE   F  54  ? 1.8971 0.9653 1.7821 0.1327  0.0296  -0.0452 50  ILE   F O   
9652  C  CB  . ILE   F  54  ? 1.8205 0.7600 1.8364 0.1713  -0.0854 -0.0219 50  ILE   F CB  
9653  C  CG1 . ILE   F  54  ? 1.7436 0.7855 1.8037 0.1483  -0.0923 -0.0244 50  ILE   F CG1 
9654  C  CG2 . ILE   F  54  ? 1.8111 0.7272 1.8676 0.1707  -0.0797 -0.0221 50  ILE   F CG2 
9655  C  CD1 . ILE   F  54  ? 1.7131 0.8306 1.8303 0.1329  -0.0856 -0.0382 50  ILE   F CD1 
9656  N  N   . THR   F  55  ? 1.7898 1.0914 1.8262 0.1954  -0.0003 0.0004  51  THR   F N   
9657  C  CA  . THR   F  55  ? 1.7353 1.0544 1.9008 0.2396  -0.0328 0.0130  51  THR   F CA  
9658  C  C   . THR   F  55  ? 1.7583 0.9843 1.9110 0.3032  -0.0464 0.0336  51  THR   F C   
9659  O  O   . THR   F  55  ? 1.7892 1.0123 1.9454 0.3158  -0.0680 0.1187  51  THR   F O   
9660  C  CB  . THR   F  55  ? 1.6844 1.1375 1.8516 0.2037  -0.0536 0.0542  51  THR   F CB  
9661  O  OG1 . THR   F  55  ? 1.6005 1.3384 1.8702 0.1269  -0.0566 0.0708  51  THR   F OG1 
9662  C  CG2 . THR   F  55  ? 1.6604 1.0643 1.8566 0.2175  -0.0708 0.0135  51  THR   F CG2 
9663  N  N   . SER   F  56  ? 1.7092 1.0219 1.9069 0.3066  -0.0905 -0.0245 52  SER   F N   
9664  C  CA  . SER   F  56  ? 1.7309 1.0282 1.9201 0.3077  -0.1312 -0.0698 52  SER   F CA  
9665  C  C   . SER   F  56  ? 1.7903 0.9828 1.8629 0.2861  -0.1373 -0.1276 52  SER   F C   
9666  O  O   . SER   F  56  ? 1.7175 0.9635 1.8944 0.2667  -0.1662 -0.1574 52  SER   F O   
9667  C  CB  . SER   F  56  ? 1.7223 1.0376 1.9182 0.2923  -0.1461 -0.0219 52  SER   F CB  
9668  O  OG  . SER   F  56  ? 1.7425 1.1135 2.0109 0.2444  -0.1672 -0.0079 52  SER   F OG  
9669  N  N   . LYS   F  57  ? 1.7967 0.9787 1.8356 0.2436  -0.0970 -0.1803 53  LYS   F N   
9670  C  CA  . LYS   F  57  ? 1.9193 0.9594 1.8477 0.2310  -0.0416 -0.1516 53  LYS   F CA  
9671  C  C   . LYS   F  57  ? 1.9349 0.9938 1.8929 0.3092  -0.0344 -0.1867 53  LYS   F C   
9672  O  O   . LYS   F  57  ? 1.9344 0.8116 1.8137 0.4224  0.0288  -0.3383 53  LYS   F O   
9673  C  CB  . LYS   F  57  ? 1.9085 0.9871 1.8654 0.2113  -0.0296 -0.0928 53  LYS   F CB  
9674  C  CG  . LYS   F  57  ? 1.9179 1.0235 1.8660 0.2038  0.0198  -0.0733 53  LYS   F CG  
9675  C  CD  . LYS   F  57  ? 1.9355 1.1072 1.9240 0.1825  0.0317  -0.0193 53  LYS   F CD  
9676  C  CE  . LYS   F  57  ? 1.9414 1.1677 1.9014 0.1908  0.0755  0.0277  53  LYS   F CE  
9677  N  NZ  . LYS   F  57  ? 1.9872 1.2785 1.9035 0.1633  0.0766  0.0697  53  LYS   F NZ  
9678  N  N   . LEU   F  58  ? 1.9560 0.8976 1.8866 0.2946  -0.0502 -0.1864 54  LEU   F N   
9679  C  CA  . LEU   F  58  ? 1.9726 0.9112 1.9089 0.2229  -0.0911 -0.1968 54  LEU   F CA  
9680  C  C   . LEU   F  58  ? 1.9570 0.9097 1.8502 0.2022  -0.0980 -0.1709 54  LEU   F C   
9681  O  O   . LEU   F  58  ? 1.9734 0.9088 1.8123 0.1708  -0.0239 -0.1602 54  LEU   F O   
9682  C  CB  . LEU   F  58  ? 1.9467 0.8607 1.9372 0.2180  -0.0975 -0.1804 54  LEU   F CB  
9683  C  CG  . LEU   F  58  ? 1.9607 0.8262 2.0128 0.2242  -0.0992 -0.1963 54  LEU   F CG  
9684  C  CD1 . LEU   F  58  ? 1.9387 0.8466 2.0073 0.2007  -0.1048 -0.2016 54  LEU   F CD1 
9685  C  CD2 . LEU   F  58  ? 1.9707 0.8069 2.0519 0.2177  -0.1009 -0.1671 54  LEU   F CD2 
9686  N  N   . LEU   F  59  ? 1.9762 0.9324 1.8326 0.1516  -0.0846 -0.1895 55  LEU   F N   
9687  C  CA  . LEU   F  59  ? 1.9518 0.9191 1.7766 0.1431  -0.0758 -0.2169 55  LEU   F CA  
9688  C  C   . LEU   F  59  ? 2.0057 0.8996 1.8105 0.1029  -0.1318 -0.2144 55  LEU   F C   
9689  O  O   . LEU   F  59  ? 2.1128 1.1120 1.7613 0.0444  -0.1158 -0.2434 55  LEU   F O   
9690  C  CB  . LEU   F  59  ? 1.9149 0.8968 1.7483 0.1437  -0.0338 -0.2098 55  LEU   F CB  
9691  C  CG  . LEU   F  59  ? 1.9384 0.9350 1.6894 0.1778  0.0229  -0.2055 55  LEU   F CG  
9692  C  CD1 . LEU   F  59  ? 1.9327 0.9462 1.7230 0.1638  0.0178  -0.2098 55  LEU   F CD1 
9693  C  CD2 . LEU   F  59  ? 1.9609 0.8754 1.6302 0.1710  0.0122  -0.1776 55  LEU   F CD2 
9694  N  N   . VAL   F  60  ? 1.9950 0.8799 1.8210 0.1107  -0.1470 -0.1891 56  VAL   F N   
9695  C  CA  . VAL   F  60  ? 2.0058 0.7655 1.8017 0.1163  -0.1880 -0.2518 56  VAL   F CA  
9696  C  C   . VAL   F  60  ? 2.0008 0.7495 1.7563 0.1384  -0.1471 -0.1942 56  VAL   F C   
9697  O  O   . VAL   F  60  ? 2.0040 0.6733 1.7474 0.1936  -0.2115 -0.1833 56  VAL   F O   
9698  C  CB  . VAL   F  60  ? 1.9934 0.7807 1.7935 0.0056  -0.2307 -0.2719 56  VAL   F CB  
9699  C  CG1 . VAL   F  60  ? 1.9719 0.8111 1.7782 -0.0140 -0.2274 -0.2662 56  VAL   F CG1 
9700  C  CG2 . VAL   F  60  ? 2.0004 0.7203 1.8028 -0.0224 -0.2562 -0.3346 56  VAL   F CG2 
9701  N  N   . PRO   F  61  ? 1.9804 0.7485 1.7356 0.1125  -0.1549 -0.1407 57  PRO   F N   
9702  C  CA  . PRO   F  61  ? 1.9801 0.8478 1.7108 0.1024  -0.1397 -0.1472 57  PRO   F CA  
9703  C  C   . PRO   F  61  ? 2.0017 0.8808 1.6746 0.1379  -0.1525 -0.1710 57  PRO   F C   
9704  O  O   . PRO   F  61  ? 1.9605 0.9296 1.6475 0.1070  -0.2330 -0.1268 57  PRO   F O   
9705  C  CB  . PRO   F  61  ? 1.9594 0.8425 1.7464 0.0760  -0.1147 -0.0843 57  PRO   F CB  
9706  C  CG  . PRO   F  61  ? 1.9633 0.8075 1.7597 0.0660  -0.1060 -0.0626 57  PRO   F CG  
9707  C  CD  . PRO   F  61  ? 1.9671 0.7447 1.7736 0.0663  -0.1253 -0.0754 57  PRO   F CD  
9708  N  N   . GLN   F  62  ? 2.0222 1.0390 1.6750 0.1821  -0.1583 -0.1954 58  GLN   F N   
9709  C  CA  . GLN   F  62  ? 2.0618 1.1136 1.6968 0.2539  -0.1587 -0.2076 58  GLN   F CA  
9710  C  C   . GLN   F  62  ? 2.0944 1.0248 1.6999 0.2558  -0.1221 -0.1668 58  GLN   F C   
9711  O  O   . GLN   F  62  ? 2.1059 1.0562 1.8157 0.2804  -0.1071 -0.1847 58  GLN   F O   
9712  C  CB  . GLN   F  62  ? 2.0114 1.2289 1.7044 0.2303  -0.1475 -0.2132 58  GLN   F CB  
9713  C  CG  . GLN   F  62  ? 2.0036 1.4294 1.7058 0.2467  -0.1515 -0.2222 58  GLN   F CG  
9714  C  CD  . GLN   F  62  ? 1.9816 1.5459 1.7032 0.3573  -0.1207 -0.2324 58  GLN   F CD  
9715  O  OE1 . GLN   F  62  ? 1.9553 1.7621 1.7778 0.3650  -0.1559 -0.1891 58  GLN   F OE1 
9716  N  NE2 . GLN   F  62  ? 1.9638 1.6912 1.6798 0.3393  -0.1056 -0.2334 58  GLN   F NE2 
9717  N  N   . LYS   F  63  ? 2.1036 0.9849 1.7477 0.2489  -0.1061 -0.1160 59  LYS   F N   
9718  C  CA  . LYS   F  63  ? 2.0920 1.0270 1.6899 0.1560  -0.1312 -0.0895 59  LYS   F CA  
9719  C  C   . LYS   F  63  ? 2.0449 0.9079 1.7472 0.1170  -0.1581 -0.1543 59  LYS   F C   
9720  O  O   . LYS   F  63  ? 2.1647 1.2050 1.7135 0.1243  -0.1700 -0.1334 59  LYS   F O   
9721  C  CB  . LYS   F  63  ? 2.0996 1.1520 1.7717 0.0727  -0.1502 -0.0381 59  LYS   F CB  
9722  C  CG  . LYS   F  63  ? 2.1891 1.2810 1.7956 -0.0281 -0.1599 0.0325  59  LYS   F CG  
9723  C  CD  . LYS   F  63  ? 2.2030 1.3170 1.8464 -0.0351 -0.1655 0.0340  59  LYS   F CD  
9724  C  CE  . LYS   F  63  ? 2.2586 1.4363 1.8850 -0.1502 -0.1708 0.0076  59  LYS   F CE  
9725  N  NZ  . LYS   F  63  ? 2.3406 1.4614 1.9320 -0.2086 -0.1866 0.0338  59  LYS   F NZ  
9726  N  N   . ASN   F  64  ? 1.9805 0.7363 1.7178 0.1574  -0.0437 -0.1613 60  ASN   F N   
9727  C  CA  . ASN   F  64  ? 1.9446 0.5872 1.6712 0.1106  -0.0963 -0.2411 60  ASN   F CA  
9728  C  C   . ASN   F  64  ? 1.9204 0.6404 1.6219 0.1437  -0.0530 -0.1970 60  ASN   F C   
9729  O  O   . ASN   F  64  ? 1.9004 0.8419 1.6046 0.0463  -0.1114 -0.2420 60  ASN   F O   
9730  C  CB  . ASN   F  64  ? 1.9632 0.5734 1.6980 0.1121  -0.0706 -0.2533 60  ASN   F CB  
9731  C  CG  . ASN   F  64  ? 1.9665 0.4033 1.7007 0.0984  -0.0746 -0.3081 60  ASN   F CG  
9732  O  OD1 . ASN   F  64  ? 2.0159 0.2962 1.7876 0.0564  -0.0585 -0.3852 60  ASN   F OD1 
9733  N  ND2 . ASN   F  64  ? 1.9766 0.4152 1.8010 0.1083  -0.0630 -0.3119 60  ASN   F ND2 
9734  N  N   . VAL   F  65  ? 1.8744 0.6464 1.6367 0.1334  -0.0319 -0.1747 61  VAL   F N   
9735  C  CA  . VAL   F  65  ? 1.8538 0.7460 1.6598 0.1820  -0.0189 -0.1847 61  VAL   F CA  
9736  C  C   . VAL   F  65  ? 1.8806 0.6484 1.6460 0.2055  0.0159  -0.1734 61  VAL   F C   
9737  O  O   . VAL   F  65  ? 1.9093 0.7025 1.6378 0.3043  -0.0096 -0.2075 61  VAL   F O   
9738  C  CB  . VAL   F  65  ? 1.8045 0.7567 1.6724 0.2482  -0.0100 -0.1703 61  VAL   F CB  
9739  C  CG1 . VAL   F  65  ? 1.7641 0.8250 1.6647 0.2363  -0.0097 -0.1886 61  VAL   F CG1 
9740  C  CG2 . VAL   F  65  ? 1.7838 0.7613 1.7046 0.2858  0.0186  -0.1760 61  VAL   F CG2 
9741  N  N   . LYS   F  66  ? 1.9100 0.6100 1.6592 0.1946  -0.0172 -0.1287 62  LYS   F N   
9742  C  CA  . LYS   F  66  ? 1.8981 0.7378 1.7019 0.1885  -0.0129 -0.0647 62  LYS   F CA  
9743  C  C   . LYS   F  66  ? 1.8496 0.7073 1.6552 0.1872  0.0348  -0.0900 62  LYS   F C   
9744  O  O   . LYS   F  66  ? 1.8670 0.8095 1.6758 0.1598  0.0508  -0.1331 62  LYS   F O   
9745  C  CB  . LYS   F  66  ? 2.0219 0.7771 1.7548 0.1454  0.0088  -0.1261 62  LYS   F CB  
9746  C  CG  . LYS   F  66  ? 2.0194 0.8335 1.8637 0.1437  -0.0238 -0.1014 62  LYS   F CG  
9747  C  CD  . LYS   F  66  ? 2.1065 0.8480 1.9181 0.1218  -0.0434 -0.1168 62  LYS   F CD  
9748  C  CE  . LYS   F  66  ? 2.0946 1.1462 1.9208 0.0590  -0.0488 -0.1003 62  LYS   F CE  
9749  N  NZ  . LYS   F  66  ? 2.1667 1.2000 1.9253 0.0409  -0.0725 -0.2036 62  LYS   F NZ  
9750  N  N   . ILE   F  67  ? 1.7478 0.6914 1.6841 0.1587  0.0902  -0.0773 63  ILE   F N   
9751  C  CA  . ILE   F  67  ? 1.7364 0.6971 1.5897 0.0972  0.1100  0.0122  63  ILE   F CA  
9752  C  C   . ILE   F  67  ? 1.6552 0.7221 1.5269 0.0888  0.0544  0.0040  63  ILE   F C   
9753  O  O   . ILE   F  67  ? 1.6744 0.7984 1.4985 0.0507  0.0612  0.0049  63  ILE   F O   
9754  C  CB  . ILE   F  67  ? 1.7319 0.7306 1.6118 0.1089  0.1463  0.0393  63  ILE   F CB  
9755  C  CG1 . ILE   F  67  ? 1.7367 0.7064 1.5810 0.0817  0.1460  0.0626  63  ILE   F CG1 
9756  C  CG2 . ILE   F  67  ? 1.7092 0.8485 1.6181 0.1193  0.1349  0.0571  63  ILE   F CG2 
9757  C  CD1 . ILE   F  67  ? 1.7410 0.7938 1.5892 0.0674  0.1544  0.0642  63  ILE   F CD1 
9758  N  N   . GLN   F  68  ? 1.6662 0.6304 1.4863 0.1002  0.0153  -0.0769 64  GLN   F N   
9759  C  CA  . GLN   F  68  ? 1.6876 0.5694 1.5217 0.0627  -0.0438 -0.0810 64  GLN   F CA  
9760  C  C   . GLN   F  68  ? 1.7244 0.5251 1.5444 0.0340  -0.0571 -0.0594 64  GLN   F C   
9761  O  O   . GLN   F  68  ? 1.7419 0.4675 1.6078 0.0246  -0.0831 -0.0569 64  GLN   F O   
9762  C  CB  . GLN   F  68  ? 1.7050 0.5209 1.5081 0.0737  -0.0203 -0.1403 64  GLN   F CB  
9763  C  CG  . GLN   F  68  ? 1.6974 0.4199 1.5498 0.1092  -0.0118 -0.1556 64  GLN   F CG  
9764  C  CD  . GLN   F  68  ? 1.7115 0.3921 1.5639 0.1040  0.0077  -0.1862 64  GLN   F CD  
9765  O  OE1 . GLN   F  68  ? 1.6863 0.4077 1.6241 0.0981  0.0542  -0.2072 64  GLN   F OE1 
9766  N  NE2 . GLN   F  68  ? 1.7202 0.4339 1.5575 0.0930  -0.0448 -0.1992 64  GLN   F NE2 
9767  N  N   . VAL   F  69  ? 1.7176 0.5387 1.4796 0.0490  -0.0946 -0.0853 65  VAL   F N   
9768  C  CA  . VAL   F  69  ? 1.7091 0.5207 1.4420 0.0151  -0.1020 -0.0694 65  VAL   F CA  
9769  C  C   . VAL   F  69  ? 1.7258 0.5815 1.3456 0.0771  -0.1365 -0.0249 65  VAL   F C   
9770  O  O   . VAL   F  69  ? 1.7630 0.6917 1.3204 0.1305  -0.1126 0.0276  65  VAL   F O   
9771  C  CB  . VAL   F  69  ? 1.7276 0.4858 1.4932 0.0009  -0.1576 -0.0547 65  VAL   F CB  
9772  C  CG1 . VAL   F  69  ? 1.6848 0.4272 1.5176 -0.0233 -0.1804 -0.0082 65  VAL   F CG1 
9773  C  CG2 . VAL   F  69  ? 1.6980 0.5681 1.4323 -0.0603 -0.1828 -0.0112 65  VAL   F CG2 
9774  N  N   . VAL   F  70  ? 1.7092 0.5562 1.2882 0.0643  -0.1177 -0.0427 66  VAL   F N   
9775  C  CA  . VAL   F  70  ? 1.6857 0.5784 1.2310 0.0184  -0.1253 -0.0837 66  VAL   F CA  
9776  C  C   . VAL   F  70  ? 1.7451 0.5927 1.2346 0.0280  -0.1133 -0.0707 66  VAL   F C   
9777  O  O   . VAL   F  70  ? 1.7392 0.7840 1.2448 0.0816  -0.1071 -0.0256 66  VAL   F O   
9778  C  CB  . VAL   F  70  ? 1.6987 0.4967 1.1932 0.0242  -0.1357 -0.1123 66  VAL   F CB  
9779  C  CG1 . VAL   F  70  ? 1.6942 0.4372 1.1476 -0.0171 -0.1471 -0.1666 66  VAL   F CG1 
9780  C  CG2 . VAL   F  70  ? 1.6627 0.5535 1.1741 0.0323  -0.1493 -0.0814 66  VAL   F CG2 
9781  N  N   . ASP   F  71  ? 1.8177 0.4795 1.2181 -0.0324 -0.1232 -0.0092 67  ASP   F N   
9782  C  CA  . ASP   F  71  ? 1.8962 0.4853 1.2724 -0.0194 -0.1328 0.0067  67  ASP   F CA  
9783  C  C   . ASP   F  71  ? 1.8696 0.4786 1.3230 -0.0119 -0.1392 0.0413  67  ASP   F C   
9784  O  O   . ASP   F  71  ? 1.8856 0.3224 1.4047 0.0965  -0.1015 0.1210  67  ASP   F O   
9785  C  CB  . ASP   F  71  ? 1.9498 0.4535 1.2922 -0.0286 -0.1744 0.0067  67  ASP   F CB  
9786  C  CG  . ASP   F  71  ? 2.1038 0.4354 1.3512 -0.0427 -0.1485 0.0383  67  ASP   F CG  
9787  O  OD1 . ASP   F  71  ? 2.1826 0.5162 1.4606 -0.1784 -0.1489 0.0202  67  ASP   F OD1 
9788  O  OD2 . ASP   F  71  ? 2.2642 0.1967 1.2940 0.0484  -0.0893 0.0167  67  ASP   F OD2 
9789  N  N   . ARG   F  72  ? 1.8113 0.5150 1.3026 -0.0456 -0.1182 0.0342  68  ARG   F N   
9790  C  CA  . ARG   F  72  ? 1.7882 0.5937 1.3382 -0.0646 -0.1185 0.0171  68  ARG   F CA  
9791  C  C   . ARG   F  72  ? 1.7950 0.5672 1.3531 -0.0833 -0.0779 0.0047  68  ARG   F C   
9792  O  O   . ARG   F  72  ? 1.7153 0.6317 1.5089 -0.1001 -0.0444 -0.0380 68  ARG   F O   
9793  C  CB  . ARG   F  72  ? 1.7889 0.5758 1.3902 0.0123  -0.0913 0.0274  68  ARG   F CB  
9794  C  CG  . ARG   F  72  ? 1.8152 0.5917 1.4004 0.0279  -0.1028 0.0168  68  ARG   F CG  
9795  C  CD  . ARG   F  72  ? 1.8668 0.6351 1.3810 -0.0008 -0.1153 -0.0206 68  ARG   F CD  
9796  N  NE  . ARG   F  72  ? 1.9443 0.6557 1.3915 -0.0497 -0.1094 -0.0174 68  ARG   F NE  
9797  C  CZ  . ARG   F  72  ? 1.9924 0.6411 1.3551 -0.0175 -0.1054 -0.0070 68  ARG   F CZ  
9798  N  NH1 . ARG   F  72  ? 2.0020 0.5510 1.3509 0.0033  -0.0856 -0.0816 68  ARG   F NH1 
9799  N  NH2 . ARG   F  72  ? 2.0067 0.7009 1.3882 -0.0695 -0.1250 0.0357  68  ARG   F NH2 
9800  N  N   . HIS   F  73  ? 1.8479 0.4601 1.3857 -0.0993 -0.0979 0.0359  69  HIS   F N   
9801  C  CA  . HIS   F  73  ? 1.8361 0.4954 1.4063 -0.0674 -0.1113 0.0015  69  HIS   F CA  
9802  C  C   . HIS   F  73  ? 1.8384 0.4715 1.4105 -0.0103 -0.1077 -0.0541 69  HIS   F C   
9803  O  O   . HIS   F  73  ? 1.8531 0.5869 1.4768 0.1097  -0.1528 -0.1503 69  HIS   F O   
9804  C  CB  . HIS   F  73  ? 1.7984 0.4834 1.3563 -0.1197 -0.1216 0.0232  69  HIS   F CB  
9805  C  CG  . HIS   F  73  ? 1.7845 0.3950 1.3118 -0.1512 -0.1490 0.0757  69  HIS   F CG  
9806  N  ND1 . HIS   F  73  ? 1.8145 0.3351 1.3010 -0.1692 -0.1394 0.1074  69  HIS   F ND1 
9807  C  CD2 . HIS   F  73  ? 1.7824 0.4081 1.2631 -0.1366 -0.1784 0.1115  69  HIS   F CD2 
9808  C  CE1 . HIS   F  73  ? 1.7973 0.3454 1.2930 -0.1821 -0.1880 0.1187  69  HIS   F CE1 
9809  N  NE2 . HIS   F  73  ? 1.7871 0.4126 1.2512 -0.1466 -0.1940 0.1310  69  HIS   F NE2 
9810  N  N   . ILE   F  74  ? 1.7789 0.5583 1.3125 0.0213  -0.1126 -0.1081 70  ILE   F N   
9811  C  CA  . ILE   F  74  ? 1.7218 0.5707 1.2431 -0.0009 -0.0759 -0.0990 70  ILE   F CA  
9812  C  C   . ILE   F  74  ? 1.7270 0.5204 1.2985 -0.0204 -0.0855 -0.0890 70  ILE   F C   
9813  O  O   . ILE   F  74  ? 1.7902 0.5176 1.3020 -0.0327 -0.0936 -0.1024 70  ILE   F O   
9814  C  CB  . ILE   F  74  ? 1.6978 0.4979 1.2092 0.0076  -0.0885 -0.1360 70  ILE   F CB  
9815  C  CG1 . ILE   F  74  ? 1.6874 0.5035 1.1383 0.0000  -0.0782 -0.1223 70  ILE   F CG1 
9816  C  CG2 . ILE   F  74  ? 1.6953 0.4909 1.2481 0.0169  -0.0744 -0.1702 70  ILE   F CG2 
9817  C  CD1 . ILE   F  74  ? 1.6759 0.4831 1.1190 0.0089  -0.0950 -0.1218 70  ILE   F CD1 
9818  N  N   . GLY   F  75  ? 1.7001 0.5542 1.3015 0.0095  -0.0749 -0.1110 71  GLY   F N   
9819  C  CA  . GLY   F  75  ? 1.6942 0.6749 1.3063 0.0536  -0.0907 -0.0942 71  GLY   F CA  
9820  C  C   . GLY   F  75  ? 1.6606 0.6908 1.3254 0.0808  -0.0948 -0.0499 71  GLY   F C   
9821  O  O   . GLY   F  75  ? 1.5984 0.6800 1.3288 0.1134  -0.0839 -0.0086 71  GLY   F O   
9822  N  N   . CYS   F  76  ? 1.6497 0.7407 1.3520 0.0841  -0.1290 -0.0468 72  CYS   F N   
9823  C  CA  . CYS   F  76  ? 1.5947 0.7557 1.3423 0.0931  -0.1474 -0.0215 72  CYS   F CA  
9824  C  C   . CYS   F  76  ? 1.6947 0.6203 1.3709 0.0832  -0.1844 -0.0050 72  CYS   F C   
9825  O  O   . CYS   F  76  ? 1.7022 0.5755 1.4355 0.1065  -0.2349 0.0510  72  CYS   F O   
9826  C  CB  . CYS   F  76  ? 1.5473 0.8556 1.3197 0.0231  -0.1467 0.0143  72  CYS   F CB  
9827  S  SG  . CYS   F  76  ? 1.4021 1.0169 1.3939 -0.0002 -0.1143 0.0100  72  CYS   F SG  
9828  N  N   . VAL   F  77  ? 1.6762 0.5979 1.3402 0.1466  -0.1877 -0.0203 73  VAL   F N   
9829  C  CA  . VAL   F  77  ? 1.6870 0.6024 1.2759 0.1855  -0.1359 -0.0934 73  VAL   F CA  
9830  C  C   . VAL   F  77  ? 1.6949 0.4936 1.3033 0.2153  -0.1752 -0.1395 73  VAL   F C   
9831  O  O   . VAL   F  77  ? 1.7395 0.2817 1.1581 0.2601  -0.2245 -0.1622 73  VAL   F O   
9832  C  CB  . VAL   F  77  ? 1.6563 0.6315 1.2962 0.2036  -0.1099 -0.0844 73  VAL   F CB  
9833  C  CG1 . VAL   F  77  ? 1.6199 0.6557 1.2763 0.2069  -0.0903 -0.0815 73  VAL   F CG1 
9834  C  CG2 . VAL   F  77  ? 1.6284 0.6480 1.3343 0.2063  -0.0731 -0.0866 73  VAL   F CG2 
9835  N  N   . TYR   F  78  ? 1.7600 0.4636 1.3558 0.2398  -0.1364 -0.1132 74  TYR   F N   
9836  C  CA  . TYR   F  78  ? 1.7279 0.5613 1.3828 0.2116  -0.1342 -0.0774 74  TYR   F CA  
9837  C  C   . TYR   F  78  ? 1.6954 0.6078 1.4477 0.2195  -0.1507 -0.0483 74  TYR   F C   
9838  O  O   . TYR   F  78  ? 1.6723 0.8624 1.5669 0.2128  -0.0768 -0.0496 74  TYR   F O   
9839  C  CB  . TYR   F  78  ? 1.6836 0.5750 1.4013 0.2542  -0.1331 -0.0567 74  TYR   F CB  
9840  C  CG  . TYR   F  78  ? 1.6366 0.5421 1.4555 0.2704  -0.1938 -0.0016 74  TYR   F CG  
9841  C  CD1 . TYR   F  78  ? 1.6079 0.5779 1.5191 0.2630  -0.2157 -0.0057 74  TYR   F CD1 
9842  C  CD2 . TYR   F  78  ? 1.6224 0.5487 1.4613 0.2900  -0.1919 -0.0092 74  TYR   F CD2 
9843  C  CE1 . TYR   F  78  ? 1.5504 0.5349 1.5441 0.2680  -0.2278 0.0303  74  TYR   F CE1 
9844  C  CE2 . TYR   F  78  ? 1.5389 0.5840 1.4968 0.2998  -0.2249 0.0097  74  TYR   F CE2 
9845  C  CZ  . TYR   F  78  ? 1.5407 0.5418 1.5444 0.2894  -0.2272 0.0448  74  TYR   F CZ  
9846  O  OH  . TYR   F  78  ? 1.5598 0.4869 1.5863 0.2755  -0.2592 0.0945  74  TYR   F OH  
9847  N  N   . SER   F  79  ? 1.7443 0.5420 1.4067 0.2642  -0.1607 0.0076  75  SER   F N   
9848  C  CA  . SER   F  79  ? 1.7754 0.4909 1.3442 0.2242  -0.1198 0.0171  75  SER   F CA  
9849  C  C   . SER   F  79  ? 1.8005 0.3521 1.3260 0.2102  -0.1332 -0.0120 75  SER   F C   
9850  O  O   . SER   F  79  ? 1.7868 0.2709 1.2160 0.2206  -0.1799 0.0358  75  SER   F O   
9851  C  CB  . SER   F  79  ? 1.7661 0.4921 1.3075 0.2608  -0.1199 0.0371  75  SER   F CB  
9852  O  OG  . SER   F  79  ? 1.7582 0.5855 1.2823 0.3008  -0.1158 0.0392  75  SER   F OG  
9853  N  N   . GLY   F  80  ? 1.7996 0.3211 1.3372 0.1934  -0.1734 -0.0533 76  GLY   F N   
9854  C  CA  . GLY   F  80  ? 1.8065 0.3674 1.3607 0.1598  -0.1669 -0.0492 76  GLY   F CA  
9855  C  C   . GLY   F  80  ? 1.7864 0.3143 1.4304 0.1350  -0.1767 -0.0759 76  GLY   F C   
9856  O  O   . GLY   F  80  ? 1.8063 0.2181 1.5176 0.0998  -0.1506 -0.0213 76  GLY   F O   
9857  N  N   . LEU   F  81  ? 1.7749 0.3033 1.4275 0.1338  -0.1850 -0.1095 77  LEU   F N   
9858  C  CA  . LEU   F  81  ? 1.7625 0.4140 1.3815 0.1299  -0.1609 -0.1001 77  LEU   F CA  
9859  C  C   . LEU   F  81  ? 1.6950 0.4442 1.3772 0.1470  -0.1650 -0.0020 77  LEU   F C   
9860  O  O   . LEU   F  81  ? 1.7128 0.4395 1.3613 0.1541  -0.1480 0.0747  77  LEU   F O   
9861  C  CB  . LEU   F  81  ? 1.7599 0.4076 1.3732 0.0720  -0.1675 -0.1046 77  LEU   F CB  
9862  C  CG  . LEU   F  81  ? 1.7401 0.4265 1.3797 0.0365  -0.1630 -0.1309 77  LEU   F CG  
9863  C  CD1 . LEU   F  81  ? 1.7276 0.4853 1.3792 0.0437  -0.1741 -0.1641 77  LEU   F CD1 
9864  C  CD2 . LEU   F  81  ? 1.7114 0.4981 1.4159 0.0442  -0.1551 -0.1074 77  LEU   F CD2 
9865  N  N   . ILE   F  82  ? 1.7059 0.5167 1.3944 0.1210  -0.1387 0.0190  78  ILE   F N   
9866  C  CA  . ILE   F  82  ? 1.7707 0.4781 1.4335 0.1790  -0.1307 0.0220  78  ILE   F CA  
9867  C  C   . ILE   F  82  ? 1.8215 0.4653 1.4448 0.1491  -0.1252 0.0028  78  ILE   F C   
9868  O  O   . ILE   F  82  ? 1.7771 0.5048 1.5661 0.2151  -0.1538 -0.0462 78  ILE   F O   
9869  C  CB  . ILE   F  82  ? 1.7744 0.5532 1.4605 0.1959  -0.1129 0.0253  78  ILE   F CB  
9870  C  CG1 . ILE   F  82  ? 1.7911 0.7410 1.4391 0.2056  -0.0780 -0.0126 78  ILE   F CG1 
9871  C  CG2 . ILE   F  82  ? 1.7753 0.5722 1.4448 0.1635  -0.1130 0.0345  78  ILE   F CG2 
9872  C  CD1 . ILE   F  82  ? 1.7784 0.7737 1.4385 0.2207  -0.0634 -0.0097 78  ILE   F CD1 
9873  N  N   . PRO   F  83  ? 1.8794 0.2684 1.4444 0.1346  -0.0809 0.0285  79  PRO   F N   
9874  C  CA  . PRO   F  83  ? 1.8745 0.2735 1.4497 0.1196  -0.0954 -0.0040 79  PRO   F CA  
9875  C  C   . PRO   F  83  ? 1.8510 0.4677 1.4017 0.0631  -0.1045 -0.0545 79  PRO   F C   
9876  O  O   . PRO   F  83  ? 1.8997 0.5754 1.4930 0.1523  -0.0658 -0.2104 79  PRO   F O   
9877  C  CB  . PRO   F  83  ? 1.8992 0.1327 1.4517 0.1004  -0.0813 -0.0353 79  PRO   F CB  
9878  C  CG  . PRO   F  83  ? 1.9030 0.1195 1.5256 0.1083  -0.0919 0.0166  79  PRO   F CG  
9879  C  CD  . PRO   F  83  ? 1.9172 0.2443 1.4863 0.1249  -0.0684 0.0538  79  PRO   F CD  
9880  N  N   . ASP   F  84  ? 1.8723 0.4391 1.3565 0.0639  -0.1131 -0.0298 80  ASP   F N   
9881  C  CA  . ASP   F  84  ? 1.8889 0.5748 1.3145 0.1158  -0.1086 -0.0277 80  ASP   F CA  
9882  C  C   . ASP   F  84  ? 1.8126 0.4517 1.2973 0.1706  -0.1168 -0.0999 80  ASP   F C   
9883  O  O   . ASP   F  84  ? 1.8281 0.5969 1.2806 0.2336  -0.1378 -0.1635 80  ASP   F O   
9884  C  CB  . ASP   F  84  ? 1.8901 0.7002 1.2300 -0.0086 -0.1159 0.0371  80  ASP   F CB  
9885  C  CG  . ASP   F  84  ? 1.8907 0.9087 1.2426 -0.0318 -0.1269 0.1116  80  ASP   F CG  
9886  O  OD1 . ASP   F  84  ? 1.9992 1.1017 1.1218 -0.0166 -0.0763 0.1858  80  ASP   F OD1 
9887  O  OD2 . ASP   F  84  ? 1.8847 0.9897 1.1442 -0.0620 -0.2251 0.1898  80  ASP   F OD2 
9888  N  N   . GLY   F  85  ? 1.7472 0.4053 1.3283 0.2094  -0.1271 -0.0785 81  GLY   F N   
9889  C  CA  . GLY   F  85  ? 1.7217 0.4187 1.3374 0.2575  -0.1386 -0.0663 81  GLY   F CA  
9890  C  C   . GLY   F  85  ? 1.7138 0.4280 1.3244 0.2438  -0.1474 -0.0726 81  GLY   F C   
9891  O  O   . GLY   F  85  ? 1.7049 0.4371 1.2910 0.2625  -0.1490 -0.1154 81  GLY   F O   
9892  N  N   . ARG   F  86  ? 1.6848 0.2983 1.3580 0.2865  -0.1613 -0.0489 82  ARG   F N   
9893  C  CA  . ARG   F  86  ? 1.7135 0.3152 1.4317 0.2815  -0.1667 -0.0812 82  ARG   F CA  
9894  C  C   . ARG   F  86  ? 1.6946 0.4652 1.4082 0.2301  -0.1411 -0.1273 82  ARG   F C   
9895  O  O   . ARG   F  86  ? 1.6538 0.4918 1.4493 0.3536  -0.1810 -0.2169 82  ARG   F O   
9896  C  CB  . ARG   F  86  ? 1.7217 0.2300 1.4813 0.3193  -0.1830 -0.0311 82  ARG   F CB  
9897  C  CG  . ARG   F  86  ? 1.7630 0.2534 1.5244 0.3183  -0.1416 -0.0340 82  ARG   F CG  
9898  C  CD  . ARG   F  86  ? 1.8044 0.2859 1.5653 0.2620  -0.1589 -0.0215 82  ARG   F CD  
9899  N  NE  . ARG   F  86  ? 1.8796 0.2565 1.5539 0.2025  -0.1623 -0.0073 82  ARG   F NE  
9900  C  CZ  . ARG   F  86  ? 1.9837 0.2973 1.5680 0.1334  -0.1397 0.0282  82  ARG   F CZ  
9901  N  NH1 . ARG   F  86  ? 2.0160 0.3413 1.5886 0.0862  -0.1382 0.0845  82  ARG   F NH1 
9902  N  NH2 . ARG   F  86  ? 2.0174 0.1993 1.6004 0.1769  -0.1230 0.0796  82  ARG   F NH2 
9903  N  N   . HIS   F  87  ? 1.7331 0.3449 1.3993 0.2195  -0.1658 -0.1378 83  HIS   F N   
9904  C  CA  . HIS   F  87  ? 1.7473 0.4122 1.3905 0.1817  -0.1323 -0.1631 83  HIS   F CA  
9905  C  C   . HIS   F  87  ? 1.7232 0.5373 1.3549 0.0921  -0.1442 -0.1459 83  HIS   F C   
9906  O  O   . HIS   F  87  ? 1.7978 0.6273 1.4228 0.1287  -0.0105 -0.1853 83  HIS   F O   
9907  C  CB  . HIS   F  87  ? 1.7554 0.3592 1.3755 0.2127  -0.1628 -0.1740 83  HIS   F CB  
9908  C  CG  . HIS   F  87  ? 1.7747 0.4606 1.4052 0.2163  -0.1464 -0.1817 83  HIS   F CG  
9909  N  ND1 . HIS   F  87  ? 1.8368 0.6137 1.3745 0.2100  -0.1601 -0.1309 83  HIS   F ND1 
9910  C  CD2 . HIS   F  87  ? 1.8027 0.5341 1.3676 0.1480  -0.1868 -0.2144 83  HIS   F CD2 
9911  C  CE1 . HIS   F  87  ? 1.8385 0.7132 1.3532 0.1849  -0.1380 -0.1259 83  HIS   F CE1 
9912  N  NE2 . HIS   F  87  ? 1.8417 0.6583 1.3740 0.1467  -0.1376 -0.1805 83  HIS   F NE2 
9913  N  N   . LEU   F  88  ? 1.6928 0.4849 1.3864 0.0235  -0.1704 -0.1337 84  LEU   F N   
9914  C  CA  . LEU   F  88  ? 1.6912 0.5735 1.4510 -0.0284 -0.2132 -0.1007 84  LEU   F CA  
9915  C  C   . LEU   F  88  ? 1.6525 0.5309 1.4192 0.0203  -0.3075 -0.0901 84  LEU   F C   
9916  O  O   . LEU   F  88  ? 1.7216 0.3976 1.3857 -0.0199 -0.3731 -0.0515 84  LEU   F O   
9917  C  CB  . LEU   F  88  ? 1.6724 0.5944 1.5520 -0.0661 -0.1941 -0.1492 84  LEU   F CB  
9918  C  CG  . LEU   F  88  ? 1.6522 0.6523 1.6142 -0.1304 -0.2032 -0.1641 84  LEU   F CG  
9919  C  CD1 . LEU   F  88  ? 1.6565 0.6362 1.6158 -0.1843 -0.1864 -0.1671 84  LEU   F CD1 
9920  C  CD2 . LEU   F  88  ? 1.6879 0.6305 1.6863 -0.1073 -0.1597 -0.1690 84  LEU   F CD2 
9921  N  N   . VAL   F  89  ? 1.6820 0.4622 1.3498 -0.0358 -0.2919 -0.0470 85  VAL   F N   
9922  C  CA  . VAL   F  89  ? 1.6294 0.5099 1.3223 -0.0285 -0.2571 -0.0254 85  VAL   F CA  
9923  C  C   . VAL   F  89  ? 1.6909 0.5813 1.2894 -0.0069 -0.2518 -0.0473 85  VAL   F C   
9924  O  O   . VAL   F  89  ? 1.6972 0.6736 1.1639 0.0380  -0.2740 -0.0161 85  VAL   F O   
9925  C  CB  . VAL   F  89  ? 1.6150 0.4808 1.3365 -0.0107 -0.2647 -0.0276 85  VAL   F CB  
9926  C  CG1 . VAL   F  89  ? 1.5741 0.5589 1.3644 -0.0413 -0.2593 0.0253  85  VAL   F CG1 
9927  C  CG2 . VAL   F  89  ? 1.5896 0.4340 1.3555 -0.0032 -0.2536 -0.0191 85  VAL   F CG2 
9928  N  N   . ASN   F  90  ? 1.7083 0.5190 1.2857 -0.0399 -0.2520 -0.0821 86  ASN   F N   
9929  C  CA  . ASN   F  90  ? 1.6797 0.4261 1.4072 -0.0514 -0.2699 -0.1093 86  ASN   F CA  
9930  C  C   . ASN   F  90  ? 1.7044 0.4539 1.3818 -0.0067 -0.2550 -0.1552 86  ASN   F C   
9931  O  O   . ASN   F  90  ? 1.6614 0.5149 1.5014 0.1450  -0.2600 -0.2114 86  ASN   F O   
9932  C  CB  . ASN   F  90  ? 1.7229 0.3568 1.4023 -0.0985 -0.2671 -0.1019 86  ASN   F CB  
9933  C  CG  . ASN   F  90  ? 1.7391 0.3580 1.4730 -0.0649 -0.2639 -0.0409 86  ASN   F CG  
9934  O  OD1 . ASN   F  90  ? 1.9526 0.1327 1.5733 -0.1622 -0.1868 -0.0242 86  ASN   F OD1 
9935  N  ND2 . ASN   F  90  ? 1.7407 0.5279 1.5469 -0.1171 -0.1828 -0.0065 86  ASN   F ND2 
9936  N  N   . ARG   F  91  ? 1.6495 0.4483 1.2942 0.0197  -0.2254 -0.1063 87  ARG   F N   
9937  C  CA  . ARG   F  91  ? 1.6561 0.4752 1.2281 0.0397  -0.2006 -0.1478 87  ARG   F CA  
9938  C  C   . ARG   F  91  ? 1.6878 0.4420 1.2111 -0.0097 -0.1626 -0.1587 87  ARG   F C   
9939  O  O   . ARG   F  91  ? 1.7108 0.3669 1.2176 -0.0650 -0.1528 -0.2454 87  ARG   F O   
9940  C  CB  . ARG   F  91  ? 1.6637 0.4628 1.1423 0.0564  -0.2039 -0.1242 87  ARG   F CB  
9941  C  CG  . ARG   F  91  ? 1.6760 0.4728 1.0783 0.0975  -0.1820 -0.1731 87  ARG   F CG  
9942  C  CD  . ARG   F  91  ? 1.7280 0.5185 1.0583 0.1233  -0.1812 -0.1779 87  ARG   F CD  
9943  N  NE  . ARG   F  91  ? 1.7297 0.4945 1.0193 0.1508  -0.1404 -0.2338 87  ARG   F NE  
9944  C  CZ  . ARG   F  91  ? 1.7781 0.4926 1.0050 0.1316  -0.1254 -0.2347 87  ARG   F CZ  
9945  N  NH1 . ARG   F  91  ? 1.7931 0.5217 1.0224 0.1170  -0.1518 -0.1805 87  ARG   F NH1 
9946  N  NH2 . ARG   F  91  ? 1.7761 0.5559 1.0138 0.0942  -0.1476 -0.2495 87  ARG   F NH2 
9947  N  N   . GLY   F  92  ? 1.7089 0.5205 1.2564 -0.0070 -0.1114 -0.1776 88  GLY   F N   
9948  C  CA  . GLY   F  92  ? 1.7152 0.4739 1.2967 -0.0090 -0.1155 -0.1438 88  GLY   F CA  
9949  C  C   . GLY   F  92  ? 1.7319 0.4562 1.3174 0.0097  -0.1105 -0.1498 88  GLY   F C   
9950  O  O   . GLY   F  92  ? 1.8111 0.3280 1.3431 -0.0552 -0.1150 -0.1250 88  GLY   F O   
9951  N  N   . ARG   F  93  ? 1.6831 0.4983 1.2911 0.0425  -0.1081 -0.0835 89  ARG   F N   
9952  C  CA  . ARG   F  93  ? 1.6329 0.5225 1.2415 0.0321  -0.1333 -0.0784 89  ARG   F CA  
9953  C  C   . ARG   F  93  ? 1.6362 0.4702 1.1696 0.0048  -0.1501 -0.0809 89  ARG   F C   
9954  O  O   . ARG   F  93  ? 1.6228 0.4526 1.2342 0.1578  -0.1329 -0.1677 89  ARG   F O   
9955  C  CB  . ARG   F  93  ? 1.6523 0.6406 1.2576 0.0833  -0.1548 -0.0495 89  ARG   F CB  
9956  C  CG  . ARG   F  93  ? 1.6508 0.7468 1.2987 0.1259  -0.1267 -0.0045 89  ARG   F CG  
9957  C  CD  . ARG   F  93  ? 1.6794 0.7190 1.3256 0.1532  -0.1322 0.0464  89  ARG   F CD  
9958  N  NE  . ARG   F  93  ? 1.6868 0.6359 1.3565 0.2068  -0.1288 0.0477  89  ARG   F NE  
9959  C  CZ  . ARG   F  93  ? 1.6879 0.5656 1.3518 0.1807  -0.1549 0.1238  89  ARG   F CZ  
9960  N  NH1 . ARG   F  93  ? 1.6993 0.5019 1.3502 0.1492  -0.1395 0.1847  89  ARG   F NH1 
9961  N  NH2 . ARG   F  93  ? 1.6624 0.5868 1.3989 0.1484  -0.1344 0.1182  89  ARG   F NH2 
9962  N  N   . GLU   F  94  ? 1.6515 0.4045 1.1473 -0.0232 -0.1865 -0.0720 90  GLU   F N   
9963  C  CA  . GLU   F  94  ? 1.6958 0.4094 1.1840 -0.0176 -0.1795 -0.1040 90  GLU   F CA  
9964  C  C   . GLU   F  94  ? 1.7089 0.5225 1.1330 -0.0743 -0.1773 -0.0437 90  GLU   F C   
9965  O  O   . GLU   F  94  ? 1.6749 0.5657 1.1464 -0.0569 -0.1605 -0.0311 90  GLU   F O   
9966  C  CB  . GLU   F  94  ? 1.7288 0.4473 1.1993 -0.0404 -0.1904 -0.0947 90  GLU   F CB  
9967  C  CG  . GLU   F  94  ? 1.7468 0.5604 1.2882 -0.0635 -0.2339 -0.1644 90  GLU   F CG  
9968  C  CD  . GLU   F  94  ? 1.7807 0.7482 1.2704 -0.0967 -0.2316 -0.1141 90  GLU   F CD  
9969  O  OE1 . GLU   F  94  ? 1.7758 1.0651 1.3685 -0.1509 -0.2379 -0.1160 90  GLU   F OE1 
9970  O  OE2 . GLU   F  94  ? 1.7945 0.9066 1.3843 -0.0576 -0.3128 -0.2055 90  GLU   F OE2 
9971  N  N   . GLU   F  95  ? 1.7349 0.4890 1.1257 -0.0221 -0.1459 -0.0653 91  GLU   F N   
9972  C  CA  . GLU   F  95  ? 1.7397 0.5184 1.1590 -0.0256 -0.1539 -0.0646 91  GLU   F CA  
9973  C  C   . GLU   F  95  ? 1.6817 0.4360 1.1795 -0.0158 -0.1462 -0.0986 91  GLU   F C   
9974  O  O   . GLU   F  95  ? 1.7328 0.2704 1.0820 -0.0464 -0.1308 -0.1562 91  GLU   F O   
9975  C  CB  . GLU   F  95  ? 1.7918 0.4820 1.1751 -0.0096 -0.1502 -0.0463 91  GLU   F CB  
9976  C  CG  . GLU   F  95  ? 1.8800 0.5183 1.1344 -0.0096 -0.1831 -0.0255 91  GLU   F CG  
9977  C  CD  . GLU   F  95  ? 1.8931 0.5655 1.0665 -0.0212 -0.1973 0.0261  91  GLU   F CD  
9978  O  OE1 . GLU   F  95  ? 2.0238 0.5470 1.1014 -0.0020 -0.2786 0.0064  91  GLU   F OE1 
9979  O  OE2 . GLU   F  95  ? 1.9225 0.7389 0.8405 -0.0444 -0.2639 0.1298  91  GLU   F OE2 
9980  N  N   . ALA   F  96  ? 1.6529 0.4177 1.2303 -0.0350 -0.1506 -0.1171 92  ALA   F N   
9981  C  CA  . ALA   F  96  ? 1.6088 0.3675 1.2266 -0.0330 -0.1552 -0.1383 92  ALA   F CA  
9982  C  C   . ALA   F  96  ? 1.6313 0.3618 1.3223 -0.0160 -0.1537 -0.1521 92  ALA   F C   
9983  O  O   . ALA   F  96  ? 1.5838 0.1996 1.4307 -0.0549 -0.1873 -0.2027 92  ALA   F O   
9984  C  CB  . ALA   F  96  ? 1.5981 0.3609 1.2012 -0.0207 -0.1741 -0.1387 92  ALA   F CB  
9985  N  N   . ALA   F  97  ? 1.6462 0.3204 1.3018 -0.0008 -0.1332 -0.1332 93  ALA   F N   
9986  C  CA  . ALA   F  97  ? 1.6362 0.3282 1.2942 -0.0373 -0.1346 -0.1284 93  ALA   F CA  
9987  C  C   . ALA   F  97  ? 1.6423 0.4165 1.3098 -0.0439 -0.0902 -0.1558 93  ALA   F C   
9988  O  O   . ALA   F  97  ? 1.6657 0.4421 1.2898 0.0661  -0.0715 -0.1567 93  ALA   F O   
9989  C  CB  . ALA   F  97  ? 1.5957 0.2341 1.3070 -0.0470 -0.1433 -0.1376 93  ALA   F CB  
9990  N  N   . SER   F  98  ? 1.6195 0.4398 1.3281 -0.0369 -0.0901 -0.1410 94  SER   F N   
9991  C  CA  . SER   F  98  ? 1.6188 0.4380 1.3223 -0.0270 -0.0672 -0.0929 94  SER   F CA  
9992  C  C   . SER   F  98  ? 1.6063 0.5115 1.3853 0.0286  -0.0868 -0.0792 94  SER   F C   
9993  O  O   . SER   F  98  ? 1.5160 0.5095 1.5275 -0.0181 -0.0377 -0.0447 94  SER   F O   
9994  C  CB  . SER   F  98  ? 1.6680 0.4575 1.3003 0.0328  -0.0095 -0.0668 94  SER   F CB  
9995  O  OG  . SER   F  98  ? 1.7101 0.4556 1.2886 -0.0089 0.0347  -0.0526 94  SER   F OG  
9996  N  N   . PHE   F  99  ? 1.6378 0.6049 1.3285 0.0896  -0.1325 -0.0715 95  PHE   F N   
9997  C  CA  . PHE   F  99  ? 1.6344 0.6187 1.3045 0.1042  -0.1195 -0.0709 95  PHE   F CA  
9998  C  C   . PHE   F  99  ? 1.6278 0.6906 1.2706 0.0382  -0.1038 -0.0613 95  PHE   F C   
9999  O  O   . PHE   F  99  ? 1.5993 0.7906 1.3113 0.0606  -0.0862 -0.0324 95  PHE   F O   
10000 C  CB  . PHE   F  99  ? 1.6301 0.6662 1.2661 0.1243  -0.1449 -0.0836 95  PHE   F CB  
10001 C  CG  . PHE   F  99  ? 1.6462 0.6739 1.2244 0.1464  -0.1294 -0.1037 95  PHE   F CG  
10002 C  CD1 . PHE   F  99  ? 1.6030 0.7305 1.1763 0.0991  -0.1140 -0.1472 95  PHE   F CD1 
10003 C  CD2 . PHE   F  99  ? 1.6569 0.6793 1.1389 0.1490  -0.1454 -0.1470 95  PHE   F CD2 
10004 C  CE1 . PHE   F  99  ? 1.6535 0.7818 1.1301 0.1041  -0.0993 -0.1977 95  PHE   F CE1 
10005 C  CE2 . PHE   F  99  ? 1.7067 0.7175 1.1262 0.1457  -0.1513 -0.1804 95  PHE   F CE2 
10006 C  CZ  . PHE   F  99  ? 1.6838 0.7594 1.1593 0.0990  -0.0833 -0.2047 95  PHE   F CZ  
10007 N  N   . LYS   F  100 ? 1.6058 0.6057 1.2295 0.0877  -0.1503 -0.0295 96  LYS   F N   
10008 C  CA  . LYS   F  100 ? 1.5850 0.5829 1.2344 0.1022  -0.1470 -0.0390 96  LYS   F CA  
10009 C  C   . LYS   F  100 ? 1.6740 0.4955 1.2060 -0.0137 -0.1390 -0.0187 96  LYS   F C   
10010 O  O   . LYS   F  100 ? 1.6871 0.4085 1.0902 -0.0182 -0.1360 -0.1303 96  LYS   F O   
10011 C  CB  . LYS   F  100 ? 1.5899 0.5841 1.2682 0.1639  -0.1714 -0.0101 96  LYS   F CB  
10012 C  CG  . LYS   F  100 ? 1.5873 0.5551 1.3448 0.1800  -0.2185 -0.0015 96  LYS   F CG  
10013 C  CD  . LYS   F  100 ? 1.6207 0.6612 1.3823 0.1861  -0.1996 0.0129  96  LYS   F CD  
10014 C  CE  . LYS   F  100 ? 1.6092 0.7163 1.4645 0.2034  -0.2350 0.0557  96  LYS   F CE  
10015 N  NZ  . LYS   F  100 ? 1.6149 0.7714 1.5363 0.1888  -0.2440 0.0347  96  LYS   F NZ  
10016 N  N   . LYS   F  101 ? 1.6970 0.5096 1.2149 -0.0346 -0.0915 -0.0393 97  LYS   F N   
10017 C  CA  . LYS   F  101 ? 1.6913 0.4220 1.2836 -0.0077 -0.0874 -0.0197 97  LYS   F CA  
10018 C  C   . LYS   F  101 ? 1.6777 0.4904 1.2630 -0.0060 -0.0967 -0.0133 97  LYS   F C   
10019 O  O   . LYS   F  101 ? 1.5960 0.5170 1.1946 0.0998  -0.1381 -0.0208 97  LYS   F O   
10020 C  CB  . LYS   F  101 ? 1.7384 0.5033 1.2718 0.0176  -0.0713 -0.0231 97  LYS   F CB  
10021 C  CG  . LYS   F  101 ? 1.7856 0.5152 1.3593 0.0565  -0.0117 -0.0564 97  LYS   F CG  
10022 C  CD  . LYS   F  101 ? 1.8145 0.6896 1.3867 0.1022  0.0189  -0.0112 97  LYS   F CD  
10023 C  CE  . LYS   F  101 ? 1.8505 0.6965 1.4291 0.0896  0.0120  -0.0291 97  LYS   F CE  
10024 N  NZ  . LYS   F  101 ? 1.8904 0.6701 1.4516 0.1071  0.0220  0.0003  97  LYS   F NZ  
10025 N  N   . LEU   F  102 ? 1.6718 0.4542 1.2982 0.0200  -0.1197 -0.0102 98  LEU   F N   
10026 C  CA  . LEU   F  102 ? 1.6743 0.4986 1.3197 0.0170  -0.1101 0.0020  98  LEU   F CA  
10027 C  C   . LEU   F  102 ? 1.7445 0.5794 1.2604 -0.0581 -0.0752 -0.0468 98  LEU   F C   
10028 O  O   . LEU   F  102 ? 1.7255 0.5833 1.3437 -0.0633 -0.0618 -0.0767 98  LEU   F O   
10029 C  CB  . LEU   F  102 ? 1.7152 0.5048 1.3742 0.0226  -0.0871 0.0485  98  LEU   F CB  
10030 C  CG  . LEU   F  102 ? 1.7180 0.5434 1.4180 0.0072  -0.0563 0.0936  98  LEU   F CG  
10031 C  CD1 . LEU   F  102 ? 1.7549 0.5448 1.4022 -0.0367 -0.0515 0.0652  98  LEU   F CD1 
10032 C  CD2 . LEU   F  102 ? 1.7868 0.5289 1.4081 0.0416  -0.0554 0.1636  98  LEU   F CD2 
10033 N  N   . TYR   F  103 ? 1.7365 0.6128 1.1483 -0.0398 -0.1550 -0.0396 99  TYR   F N   
10034 C  CA  . TYR   F  103 ? 1.6985 0.6410 1.1327 -0.0677 -0.1525 -0.0516 99  TYR   F CA  
10035 C  C   . TYR   F  103 ? 1.6381 0.6300 1.0493 -0.0671 -0.2044 -0.0619 99  TYR   F C   
10036 O  O   . TYR   F  103 ? 1.6265 0.5830 1.0570 -0.1037 -0.0837 0.0997  99  TYR   F O   
10037 C  CB  . TYR   F  103 ? 1.7171 0.6537 1.0966 -0.0921 -0.2128 -0.0303 99  TYR   F CB  
10038 C  CG  . TYR   F  103 ? 1.7169 0.6320 1.0885 -0.1099 -0.2431 -0.0245 99  TYR   F CG  
10039 C  CD1 . TYR   F  103 ? 1.7380 0.6169 1.0764 -0.0890 -0.2638 -0.0474 99  TYR   F CD1 
10040 C  CD2 . TYR   F  103 ? 1.7366 0.6652 1.0995 -0.0947 -0.2755 0.0073  99  TYR   F CD2 
10041 C  CE1 . TYR   F  103 ? 1.7707 0.5948 1.0336 -0.0878 -0.2730 -0.0400 99  TYR   F CE1 
10042 C  CE2 . TYR   F  103 ? 1.7516 0.6920 1.0979 -0.1172 -0.2776 0.0062  99  TYR   F CE2 
10043 C  CZ  . TYR   F  103 ? 1.7416 0.5894 1.0247 -0.1654 -0.2539 -0.0136 99  TYR   F CZ  
10044 O  OH  . TYR   F  103 ? 1.7744 0.5654 0.8921 -0.2785 -0.3096 -0.1063 99  TYR   F OH  
10045 N  N   . LYS   F  104 ? 1.6420 0.6378 1.0481 -0.0367 -0.2128 -0.1341 100 LYS   F N   
10046 C  CA  . LYS   F  104 ? 1.6292 0.7091 1.1012 -0.0551 -0.2468 -0.0934 100 LYS   F CA  
10047 C  C   . LYS   F  104 ? 1.7024 0.7753 1.0704 -0.0095 -0.2711 -0.0966 100 LYS   F C   
10048 O  O   . LYS   F  104 ? 1.7078 0.8720 1.1158 -0.0680 -0.2976 -0.0824 100 LYS   F O   
10049 C  CB  . LYS   F  104 ? 1.6101 0.7143 1.1508 -0.0467 -0.2672 -0.0953 100 LYS   F CB  
10050 C  CG  . LYS   F  104 ? 1.5910 0.8169 1.2894 -0.0451 -0.2231 -0.0464 100 LYS   F CG  
10051 C  CD  . LYS   F  104 ? 1.5844 0.8784 1.3604 -0.1004 -0.2298 -0.0635 100 LYS   F CD  
10052 C  CE  . LYS   F  104 ? 1.6252 0.9359 1.4593 -0.1379 -0.1990 -0.0155 100 LYS   F CE  
10053 N  NZ  . LYS   F  104 ? 1.6378 0.8642 1.5345 -0.1730 -0.1455 0.0211  100 LYS   F NZ  
10054 N  N   . THR   F  105 ? 1.6866 0.7912 1.0590 0.0047  -0.2868 -0.0715 101 THR   F N   
10055 C  CA  . THR   F  105 ? 1.7200 0.7525 1.1033 -0.0061 -0.2322 -0.0605 101 THR   F CA  
10056 C  C   . THR   F  105 ? 1.6730 0.7334 1.0924 -0.0380 -0.2316 -0.0460 101 THR   F C   
10057 O  O   . THR   F  105 ? 1.7288 0.6402 1.0047 0.0417  -0.3026 -0.0146 101 THR   F O   
10058 C  CB  . THR   F  105 ? 1.7666 0.8134 1.0840 -0.0204 -0.2216 -0.1190 101 THR   F CB  
10059 O  OG1 . THR   F  105 ? 1.8645 0.9456 1.1044 -0.0153 -0.1961 -0.1903 101 THR   F OG1 
10060 C  CG2 . THR   F  105 ? 1.7531 0.8681 1.0652 0.0032  -0.1933 -0.1224 101 THR   F CG2 
10061 N  N   . PRO   F  106 ? 1.6352 0.6943 1.1549 -0.0277 -0.2445 0.0143  102 PRO   F N   
10062 C  CA  . PRO   F  106 ? 1.6460 0.7169 1.2093 0.0047  -0.2272 0.0126  102 PRO   F CA  
10063 C  C   . PRO   F  106 ? 1.6748 0.7299 1.2610 -0.0051 -0.2202 -0.0167 102 PRO   F C   
10064 O  O   . PRO   F  106 ? 1.7336 0.8188 1.2971 -0.0039 -0.2677 -0.0136 102 PRO   F O   
10065 C  CB  . PRO   F  106 ? 1.6285 0.7185 1.2114 -0.0150 -0.2319 0.0352  102 PRO   F CB  
10066 C  CG  . PRO   F  106 ? 1.6316 0.7258 1.1933 -0.0135 -0.2311 0.0435  102 PRO   F CG  
10067 C  CD  . PRO   F  106 ? 1.6262 0.7254 1.1828 -0.0134 -0.2254 0.0190  102 PRO   F CD  
10068 N  N   . ILE   F  107 ? 1.7054 0.6783 1.3262 0.0558  -0.1487 -0.0136 103 ILE   F N   
10069 C  CA  . ILE   F  107 ? 1.6864 0.6159 1.2484 0.0955  -0.1241 0.0399  103 ILE   F CA  
10070 C  C   . ILE   F  107 ? 1.6505 0.5097 1.2614 0.1022  -0.1364 0.0583  103 ILE   F C   
10071 O  O   . ILE   F  107 ? 1.6372 0.5294 1.2350 0.1038  -0.1140 0.1674  103 ILE   F O   
10072 C  CB  . ILE   F  107 ? 1.6881 0.6902 1.1783 0.0940  -0.0874 0.0223  103 ILE   F CB  
10073 C  CG1 . ILE   F  107 ? 1.6416 0.7743 1.1435 0.0781  -0.0589 -0.0443 103 ILE   F CG1 
10074 C  CG2 . ILE   F  107 ? 1.6720 0.7856 1.2304 0.0973  -0.0939 0.0107  103 ILE   F CG2 
10075 C  CD1 . ILE   F  107 ? 1.6327 0.8116 1.1183 0.0601  -0.0180 -0.0878 103 ILE   F CD1 
10076 N  N   . PRO   F  108 ? 1.6174 0.4480 1.3157 0.1246  -0.1310 0.0004  104 PRO   F N   
10077 C  CA  . PRO   F  108 ? 1.6440 0.5442 1.2846 0.0849  -0.1621 -0.0126 104 PRO   F CA  
10078 C  C   . PRO   F  108 ? 1.6465 0.5391 1.1768 0.0633  -0.1838 -0.0214 104 PRO   F C   
10079 O  O   . PRO   F  108 ? 1.6432 0.6015 1.1511 0.0702  -0.2431 0.0037  104 PRO   F O   
10080 C  CB  . PRO   F  108 ? 1.6439 0.5330 1.3253 0.1624  -0.1474 -0.0211 104 PRO   F CB  
10081 C  CG  . PRO   F  108 ? 1.6173 0.5586 1.3411 0.1548  -0.1427 -0.0602 104 PRO   F CG  
10082 C  CD  . PRO   F  108 ? 1.5991 0.5295 1.3486 0.1364  -0.1444 -0.0156 104 PRO   F CD  
10083 N  N   . ILE   F  109 ? 1.6510 0.4817 1.1567 0.0010  -0.1740 -0.0269 105 ILE   F N   
10084 C  CA  . ILE   F  109 ? 1.6778 0.4285 1.1692 -0.0565 -0.1793 -0.0636 105 ILE   F CA  
10085 C  C   . ILE   F  109 ? 1.7202 0.3494 1.1491 -0.0669 -0.2041 -0.0763 105 ILE   F C   
10086 O  O   . ILE   F  109 ? 1.6918 0.1705 1.1489 -0.1147 -0.2806 -0.1428 105 ILE   F O   
10087 C  CB  . ILE   F  109 ? 1.6730 0.4520 1.1863 -0.0885 -0.1472 -0.0580 105 ILE   F CB  
10088 C  CG1 . ILE   F  109 ? 1.6887 0.5337 1.1769 -0.1100 -0.1414 -0.0221 105 ILE   F CG1 
10089 C  CG2 . ILE   F  109 ? 1.6547 0.4594 1.1999 -0.0742 -0.1442 -0.0705 105 ILE   F CG2 
10090 C  CD1 . ILE   F  109 ? 1.6882 0.5927 1.1715 -0.1102 -0.1510 -0.0226 105 ILE   F CD1 
10091 N  N   . PRO   F  110 ? 1.6867 0.3805 1.2141 -0.0513 -0.1895 -0.0859 106 PRO   F N   
10092 C  CA  . PRO   F  110 ? 1.7061 0.3907 1.1798 -0.0382 -0.1384 -0.0498 106 PRO   F CA  
10093 C  C   . PRO   F  110 ? 1.6864 0.3229 1.2046 -0.0319 -0.1209 -0.0844 106 PRO   F C   
10094 O  O   . PRO   F  110 ? 1.7159 0.4771 1.1741 -0.0509 -0.0311 -0.0488 106 PRO   F O   
10095 C  CB  . PRO   F  110 ? 1.6968 0.3816 1.2357 -0.0282 -0.1571 -0.0379 106 PRO   F CB  
10096 C  CG  . PRO   F  110 ? 1.7063 0.4523 1.2215 -0.0333 -0.1703 -0.0314 106 PRO   F CG  
10097 C  CD  . PRO   F  110 ? 1.7147 0.4433 1.2249 -0.0229 -0.1753 -0.0578 106 PRO   F CD  
10098 N  N   . ALA   F  111 ? 1.6615 0.3181 1.1506 0.0072  -0.1286 -0.0601 107 ALA   F N   
10099 C  CA  . ALA   F  111 ? 1.6497 0.3813 1.1324 0.0043  -0.1415 -0.0542 107 ALA   F CA  
10100 C  C   . ALA   F  111 ? 1.6703 0.2509 1.1411 -0.0055 -0.1293 -0.0439 107 ALA   F C   
10101 O  O   . ALA   F  111 ? 1.6852 0.1402 1.1651 -0.0455 -0.1337 -0.0561 107 ALA   F O   
10102 C  CB  . ALA   F  111 ? 1.6262 0.3857 1.1350 0.0065  -0.1603 -0.0886 107 ALA   F CB  
10103 N  N   . PHE   F  112 ? 1.6812 0.2910 1.1115 0.0117  -0.0968 -0.0691 108 PHE   F N   
10104 C  CA  . PHE   F  112 ? 1.6860 0.4080 1.0540 0.0367  -0.0997 -0.1115 108 PHE   F CA  
10105 C  C   . PHE   F  112 ? 1.7251 0.4143 1.0698 0.0501  -0.1114 -0.0952 108 PHE   F C   
10106 O  O   . PHE   F  112 ? 1.8314 0.5639 1.0434 0.0951  -0.1327 -0.1079 108 PHE   F O   
10107 C  CB  . PHE   F  112 ? 1.6976 0.3926 1.0121 0.0341  -0.0799 -0.1690 108 PHE   F CB  
10108 C  CG  . PHE   F  112 ? 1.6796 0.4187 0.9912 0.0394  -0.0759 -0.2108 108 PHE   F CG  
10109 C  CD1 . PHE   F  112 ? 1.7100 0.5185 0.9840 0.0323  -0.0761 -0.2051 108 PHE   F CD1 
10110 C  CD2 . PHE   F  112 ? 1.7044 0.4123 0.9470 0.0105  -0.0709 -0.2541 108 PHE   F CD2 
10111 C  CE1 . PHE   F  112 ? 1.6843 0.5247 1.0183 0.0699  -0.0531 -0.2257 108 PHE   F CE1 
10112 C  CE2 . PHE   F  112 ? 1.6944 0.3442 0.9782 0.0348  -0.0585 -0.2754 108 PHE   F CE2 
10113 C  CZ  . PHE   F  112 ? 1.7062 0.4191 0.9826 0.0082  -0.0925 -0.2644 108 PHE   F CZ  
10114 N  N   . ALA   F  113 ? 1.7019 0.4868 1.0336 0.0289  -0.1224 -0.0760 109 ALA   F N   
10115 C  CA  . ALA   F  113 ? 1.7094 0.4712 1.0568 0.0534  -0.1272 0.0283  109 ALA   F CA  
10116 C  C   . ALA   F  113 ? 1.6557 0.4835 1.0841 0.0906  -0.1227 0.0021  109 ALA   F C   
10117 O  O   . ALA   F  113 ? 1.7013 0.5181 1.1410 0.1821  -0.1750 -0.0025 109 ALA   F O   
10118 C  CB  . ALA   F  113 ? 1.7164 0.4111 1.0370 0.0453  -0.0905 0.0567  109 ALA   F CB  
10119 N  N   . ASP   F  114 ? 1.6704 0.4974 1.0346 0.1165  -0.1243 0.0561  110 ASP   F N   
10120 C  CA  . ASP   F  114 ? 1.6264 0.5920 1.0335 0.1526  -0.1236 0.0197  110 ASP   F CA  
10121 C  C   . ASP   F  114 ? 1.6793 0.6617 1.0920 0.1155  -0.1761 -0.0722 110 ASP   F C   
10122 O  O   . ASP   F  114 ? 1.7688 0.8229 0.9526 0.0773  -0.1540 -0.1232 110 ASP   F O   
10123 C  CB  . ASP   F  114 ? 1.6106 0.6147 1.0454 0.1572  -0.1002 0.0392  110 ASP   F CB  
10124 C  CG  . ASP   F  114 ? 1.5528 0.6815 1.0947 0.1891  -0.0778 0.0193  110 ASP   F CG  
10125 O  OD1 . ASP   F  114 ? 1.5372 0.7085 1.1700 0.1035  -0.0976 -0.0004 110 ASP   F OD1 
10126 O  OD2 . ASP   F  114 ? 1.5445 0.7469 1.1877 0.1572  0.0091  -0.0032 110 ASP   F OD2 
10127 N  N   . ARG   F  115 ? 1.6691 0.6706 1.1390 0.0845  -0.1677 -0.0175 111 ARG   F N   
10128 C  CA  . ARG   F  115 ? 1.6946 0.7153 1.1683 0.0886  -0.2029 -0.0099 111 ARG   F CA  
10129 C  C   . ARG   F  115 ? 1.6996 0.6564 1.0892 0.0641  -0.1596 -0.0163 111 ARG   F C   
10130 O  O   . ARG   F  115 ? 1.6666 0.7494 1.0873 0.0866  -0.2895 0.1228  111 ARG   F O   
10131 C  CB  . ARG   F  115 ? 1.6719 0.7045 1.2834 0.1151  -0.1866 0.0077  111 ARG   F CB  
10132 C  CG  . ARG   F  115 ? 1.6810 0.6783 1.2986 0.1324  -0.1546 -0.0276 111 ARG   F CG  
10133 C  CD  . ARG   F  115 ? 1.6906 0.7671 1.2859 0.1187  -0.1570 -0.0771 111 ARG   F CD  
10134 N  NE  . ARG   F  115 ? 1.6686 0.8383 1.3263 0.1706  -0.1737 -0.1065 111 ARG   F NE  
10135 C  CZ  . ARG   F  115 ? 1.6696 0.8938 1.3335 0.1898  -0.1386 -0.1991 111 ARG   F CZ  
10136 N  NH1 . ARG   F  115 ? 1.6666 0.9886 1.3420 0.2016  -0.1454 -0.1987 111 ARG   F NH1 
10137 N  NH2 . ARG   F  115 ? 1.6655 0.8050 1.3616 0.1587  -0.0996 -0.2127 111 ARG   F NH2 
10138 N  N   . LEU   F  116 ? 1.7801 0.5900 0.9939 0.0705  -0.1699 -0.0631 112 LEU   F N   
10139 C  CA  . LEU   F  116 ? 1.7823 0.5937 0.9307 0.0877  -0.1688 -0.1014 112 LEU   F CA  
10140 C  C   . LEU   F  116 ? 1.8310 0.5271 0.9263 0.1054  -0.1578 -0.1189 112 LEU   F C   
10141 O  O   . LEU   F  116 ? 1.8873 0.5318 0.9597 0.0762  -0.1622 -0.0921 112 LEU   F O   
10142 C  CB  . LEU   F  116 ? 1.7883 0.6761 0.9105 0.0697  -0.1695 -0.1201 112 LEU   F CB  
10143 C  CG  . LEU   F  116 ? 1.7986 0.7447 0.9145 0.0368  -0.2056 -0.1302 112 LEU   F CG  
10144 C  CD1 . LEU   F  116 ? 1.7979 0.7970 0.9687 0.0267  -0.1794 -0.1209 112 LEU   F CD1 
10145 C  CD2 . LEU   F  116 ? 1.8314 0.7572 0.9098 0.0433  -0.1856 -0.1689 112 LEU   F CD2 
10146 N  N   . GLY   F  117 ? 1.8009 0.4306 0.9045 0.1185  -0.1261 -0.1609 113 GLY   F N   
10147 C  CA  . GLY   F  117 ? 1.8060 0.4549 0.9571 0.1016  -0.0911 -0.1616 113 GLY   F CA  
10148 C  C   . GLY   F  117 ? 1.7946 0.4535 0.9808 0.1412  -0.0753 -0.1867 113 GLY   F C   
10149 O  O   . GLY   F  117 ? 1.8432 0.4242 0.9789 0.1047  -0.0316 -0.2274 113 GLY   F O   
10150 N  N   . GLN   F  118 ? 1.7358 0.4145 1.0375 0.1438  -0.1226 -0.1256 114 GLN   F N   
10151 C  CA  . GLN   F  118 ? 1.6636 0.4739 1.0540 0.1215  -0.1498 -0.1031 114 GLN   F CA  
10152 C  C   . GLN   F  118 ? 1.6076 0.3977 1.1267 0.1083  -0.2036 -0.1184 114 GLN   F C   
10153 O  O   . GLN   F  118 ? 1.6426 0.3019 1.1372 0.0842  -0.2390 -0.1254 114 GLN   F O   
10154 C  CB  . GLN   F  118 ? 1.6455 0.4924 1.0785 0.1359  -0.1688 -0.0788 114 GLN   F CB  
10155 C  CG  . GLN   F  118 ? 1.6487 0.5971 1.0811 0.1292  -0.1783 -0.0825 114 GLN   F CG  
10156 C  CD  . GLN   F  118 ? 1.6585 0.6770 1.0677 0.1067  -0.2188 -0.0644 114 GLN   F CD  
10157 O  OE1 . GLN   F  118 ? 1.6995 0.8305 1.1703 0.0956  -0.2719 0.0935  114 GLN   F OE1 
10158 N  NE2 . GLN   F  118 ? 1.7210 0.7344 1.0045 0.1290  -0.1954 -0.1023 114 GLN   F NE2 
10159 N  N   . TYR   F  119 ? 1.5962 0.3616 1.1581 0.1088  -0.1896 -0.0948 115 TYR   F N   
10160 C  CA  . TYR   F  119 ? 1.5491 0.4424 1.1686 0.0707  -0.1891 -0.0998 115 TYR   F CA  
10161 C  C   . TYR   F  119 ? 1.5416 0.4655 1.1216 0.0894  -0.1961 -0.0694 115 TYR   F C   
10162 O  O   . TYR   F  119 ? 1.4793 0.6234 1.1095 0.0713  -0.2586 -0.0278 115 TYR   F O   
10163 C  CB  . TYR   F  119 ? 1.5588 0.3853 1.1601 0.0755  -0.2048 -0.1208 115 TYR   F CB  
10164 C  CG  . TYR   F  119 ? 1.5480 0.4214 1.1493 0.0863  -0.1974 -0.1412 115 TYR   F CG  
10165 C  CD1 . TYR   F  119 ? 1.5249 0.5191 1.0871 0.0862  -0.2152 -0.1331 115 TYR   F CD1 
10166 C  CD2 . TYR   F  119 ? 1.5417 0.3910 1.1473 0.0729  -0.2221 -0.1622 115 TYR   F CD2 
10167 C  CE1 . TYR   F  119 ? 1.5296 0.5477 1.0831 0.0844  -0.2145 -0.1519 115 TYR   F CE1 
10168 C  CE2 . TYR   F  119 ? 1.5313 0.4169 1.1313 0.0952  -0.2105 -0.1705 115 TYR   F CE2 
10169 C  CZ  . TYR   F  119 ? 1.5506 0.4974 1.1036 0.0966  -0.1982 -0.1656 115 TYR   F CZ  
10170 O  OH  . TYR   F  119 ? 1.5471 0.4829 1.1129 0.1233  -0.1997 -0.1642 115 TYR   F OH  
10171 N  N   . VAL   F  120 ? 1.5500 0.4312 1.1159 0.0737  -0.1866 -0.0678 116 VAL   F N   
10172 C  CA  . VAL   F  120 ? 1.5737 0.4191 1.0898 0.0619  -0.2095 -0.0430 116 VAL   F CA  
10173 C  C   . VAL   F  120 ? 1.5973 0.3600 1.0743 0.0698  -0.1927 -0.0662 116 VAL   F C   
10174 O  O   . VAL   F  120 ? 1.6071 0.4039 1.0526 -0.0041 -0.2156 -0.0474 116 VAL   F O   
10175 C  CB  . VAL   F  120 ? 1.5556 0.4218 1.1121 0.0529  -0.2003 -0.0395 116 VAL   F CB  
10176 C  CG1 . VAL   F  120 ? 1.5552 0.4199 1.1408 0.0543  -0.2074 -0.0239 116 VAL   F CG1 
10177 C  CG2 . VAL   F  120 ? 1.5649 0.4402 1.1623 0.0384  -0.2094 -0.0481 116 VAL   F CG2 
10178 N  N   . GLN   F  121 ? 1.6396 0.3003 1.0348 0.1076  -0.1872 -0.0714 117 GLN   F N   
10179 C  CA  . GLN   F  121 ? 1.6869 0.2276 1.0794 0.0899  -0.1864 -0.0468 117 GLN   F CA  
10180 C  C   . GLN   F  121 ? 1.6999 0.1655 1.0818 0.0718  -0.1791 -0.0025 117 GLN   F C   
10181 O  O   . GLN   F  121 ? 1.7051 0.0472 1.0801 0.0617  -0.2723 -0.1558 117 GLN   F O   
10182 C  CB  . GLN   F  121 ? 1.7243 0.2976 1.0704 0.1133  -0.1792 -0.0151 117 GLN   F CB  
10183 C  CG  . GLN   F  121 ? 1.7684 0.2255 1.1168 0.0976  -0.1776 0.0855  117 GLN   F CG  
10184 C  CD  . GLN   F  121 ? 1.8104 0.1499 1.1102 0.1097  -0.1744 0.0923  117 GLN   F CD  
10185 O  OE1 . GLN   F  121 ? 1.8492 0.1620 1.2148 0.1813  -0.1994 0.2155  117 GLN   F OE1 
10186 N  NE2 . GLN   F  121 ? 1.8482 0.2892 1.1277 0.1088  -0.1783 -0.0518 117 GLN   F NE2 
10187 N  N   . ALA   F  122 ? 1.7812 0.3002 1.1160 0.0525  -0.2379 -0.0926 118 ALA   F N   
10188 C  CA  . ALA   F  122 ? 1.8198 0.4056 1.1135 0.0713  -0.2166 -0.0443 118 ALA   F CA  
10189 C  C   . ALA   F  122 ? 1.8477 0.4668 1.2375 0.1001  -0.2445 0.0097  118 ALA   F C   
10190 O  O   . ALA   F  122 ? 1.9660 0.5933 1.3526 0.0728  -0.1515 0.0782  118 ALA   F O   
10191 C  CB  . ALA   F  122 ? 1.8142 0.4149 1.1266 0.0588  -0.2105 -0.0663 118 ALA   F CB  
10192 N  N   . HIS   F  123 ? 1.8047 0.4601 1.2191 0.0793  -0.2639 0.0062  119 HIS   F N   
10193 C  CA  . HIS   F  123 ? 1.7447 0.5269 1.2490 0.0354  -0.3320 0.0189  119 HIS   F CA  
10194 C  C   . HIS   F  123 ? 1.7310 0.5428 1.2616 0.0060  -0.3614 0.0287  119 HIS   F C   
10195 O  O   . HIS   F  123 ? 1.7334 0.4465 1.3493 -0.0159 -0.3431 0.0009  119 HIS   F O   
10196 C  CB  . HIS   F  123 ? 1.7592 0.5990 1.2197 -0.0040 -0.3344 0.0569  119 HIS   F CB  
10197 C  CG  . HIS   F  123 ? 1.7595 0.5822 1.1922 -0.0219 -0.3241 0.0787  119 HIS   F CG  
10198 N  ND1 . HIS   F  123 ? 1.7604 0.6199 1.1333 -0.0264 -0.3134 0.1207  119 HIS   F ND1 
10199 C  CD2 . HIS   F  123 ? 1.7399 0.6551 1.2213 -0.0512 -0.3336 0.0601  119 HIS   F CD2 
10200 C  CE1 . HIS   F  123 ? 1.7594 0.7671 1.1394 -0.0318 -0.3760 0.0892  119 HIS   F CE1 
10201 N  NE2 . HIS   F  123 ? 1.7629 0.6552 1.1823 -0.0417 -0.3528 0.1064  119 HIS   F NE2 
10202 N  N   . THR   F  124 ? 1.7244 0.4194 1.2188 -0.0391 -0.3234 -0.0163 120 THR   F N   
10203 C  CA  . THR   F  124 ? 1.7065 0.3425 1.2401 0.0158  -0.2757 0.0161  120 THR   F CA  
10204 C  C   . THR   F  124 ? 1.7022 0.2963 1.1634 -0.0191 -0.2885 0.0031  120 THR   F C   
10205 O  O   . THR   F  124 ? 1.6925 0.2243 1.1186 0.0460  -0.3014 -0.0718 120 THR   F O   
10206 C  CB  . THR   F  124 ? 1.7002 0.1989 1.2830 -0.0154 -0.2695 -0.0205 120 THR   F CB  
10207 O  OG1 . THR   F  124 ? 1.7016 0.0834 1.4102 -0.0267 -0.2380 0.0034  120 THR   F OG1 
10208 C  CG2 . THR   F  124 ? 1.6902 0.1973 1.3390 0.0229  -0.2499 -0.0415 120 THR   F CG2 
10209 N  N   . LEU   F  125 ? 1.7370 0.4051 1.1367 0.0146  -0.2476 -0.0410 121 LEU   F N   
10210 C  CA  . LEU   F  125 ? 1.7697 0.5048 1.1429 0.0038  -0.2279 -0.0490 121 LEU   F CA  
10211 C  C   . LEU   F  125 ? 1.7816 0.6315 1.1266 -0.0148 -0.2544 -0.0522 121 LEU   F C   
10212 O  O   . LEU   F  125 ? 1.8568 0.8186 1.0563 -0.0836 -0.2085 -0.0436 121 LEU   F O   
10213 C  CB  . LEU   F  125 ? 1.8048 0.5263 1.1529 0.0617  -0.2279 -0.0852 121 LEU   F CB  
10214 C  CG  . LEU   F  125 ? 1.7913 0.4070 1.1463 0.0935  -0.2172 -0.1195 121 LEU   F CG  
10215 C  CD1 . LEU   F  125 ? 1.8103 0.3876 1.1515 0.0539  -0.1814 -0.0703 121 LEU   F CD1 
10216 C  CD2 . LEU   F  125 ? 1.8031 0.4132 1.1320 0.0986  -0.2203 -0.1655 121 LEU   F CD2 
10217 N  N   . TYR   F  126 ? 1.7571 0.6398 1.1397 0.0341  -0.2430 -0.0687 122 TYR   F N   
10218 C  CA  . TYR   F  126 ? 1.7044 0.6034 1.1392 0.0884  -0.2478 -0.0723 122 TYR   F CA  
10219 C  C   . TYR   F  126 ? 1.6695 0.5449 1.1490 0.0651  -0.2131 -0.1010 122 TYR   F C   
10220 O  O   . TYR   F  126 ? 1.6607 0.3893 1.1395 0.1199  -0.2256 -0.0893 122 TYR   F O   
10221 C  CB  . TYR   F  126 ? 1.7167 0.6404 1.0776 0.1155  -0.2562 -0.0976 122 TYR   F CB  
10222 C  CG  . TYR   F  126 ? 1.7496 0.6398 1.0842 0.1274  -0.2616 -0.0967 122 TYR   F CG  
10223 C  CD1 . TYR   F  126 ? 1.7428 0.6107 1.0892 0.1338  -0.2668 -0.0578 122 TYR   F CD1 
10224 C  CD2 . TYR   F  126 ? 1.7446 0.6325 1.0745 0.1580  -0.2429 -0.1070 122 TYR   F CD2 
10225 C  CE1 . TYR   F  126 ? 1.7280 0.6576 1.1320 0.1893  -0.2715 -0.0780 122 TYR   F CE1 
10226 C  CE2 . TYR   F  126 ? 1.7753 0.6853 1.0908 0.2056  -0.2404 -0.0934 122 TYR   F CE2 
10227 C  CZ  . TYR   F  126 ? 1.7451 0.7475 1.1101 0.1953  -0.2565 -0.0686 122 TYR   F CZ  
10228 O  OH  . TYR   F  126 ? 1.6971 0.8749 1.0746 0.2726  -0.3179 -0.0723 122 TYR   F OH  
10229 N  N   . ASN   F  127 ? 1.6692 0.5534 1.1673 0.0667  -0.2040 -0.0917 123 ASN   F N   
10230 C  CA  . ASN   F  127 ? 1.6429 0.5660 1.2063 0.0756  -0.2112 -0.1128 123 ASN   F CA  
10231 C  C   . ASN   F  127 ? 1.6046 0.5692 1.1867 0.1451  -0.2518 -0.0816 123 ASN   F C   
10232 O  O   . ASN   F  127 ? 1.5547 0.5421 1.2401 0.0988  -0.2914 -0.0776 123 ASN   F O   
10233 C  CB  . ASN   F  127 ? 1.7307 0.5673 1.2694 0.0747  -0.1453 -0.1057 123 ASN   F CB  
10234 C  CG  . ASN   F  127 ? 1.8120 0.6269 1.2901 0.0382  -0.0974 -0.1156 123 ASN   F CG  
10235 O  OD1 . ASN   F  127 ? 1.9175 0.5472 1.4354 0.0452  -0.0354 -0.1121 123 ASN   F OD1 
10236 N  ND2 . ASN   F  127 ? 1.8636 0.6840 1.2944 -0.0756 -0.1243 -0.1555 123 ASN   F ND2 
10237 N  N   . SER   F  128 ? 1.6017 0.5829 1.1180 0.1222  -0.3162 -0.1004 124 SER   F N   
10238 C  CA  . SER   F  128 ? 1.6280 0.5823 1.1086 0.1527  -0.3646 -0.0869 124 SER   F CA  
10239 C  C   . SER   F  128 ? 1.6561 0.5389 1.1026 0.1515  -0.3562 -0.0954 124 SER   F C   
10240 O  O   . SER   F  128 ? 1.7063 0.5789 1.0861 0.1568  -0.3912 -0.1197 124 SER   F O   
10241 C  CB  . SER   F  128 ? 1.5804 0.5187 1.1109 0.1535  -0.4312 -0.0812 124 SER   F CB  
10242 O  OG  . SER   F  128 ? 1.5277 0.5453 1.1379 0.1993  -0.4695 -0.1448 124 SER   F OG  
10243 N  N   . VAL   F  129 ? 1.7460 0.5323 1.0950 0.1815  -0.2743 -0.0406 125 VAL   F N   
10244 C  CA  . VAL   F  129 ? 1.7891 0.5298 1.2339 0.1486  -0.2111 -0.0499 125 VAL   F CA  
10245 C  C   . VAL   F  129 ? 1.8023 0.4509 1.2233 0.0936  -0.2064 -0.0127 125 VAL   F C   
10246 O  O   . VAL   F  129 ? 1.9021 0.3796 1.1889 0.0857  -0.2542 -0.0477 125 VAL   F O   
10247 C  CB  . VAL   F  129 ? 1.8449 0.4646 1.3226 0.1336  -0.1785 -0.0636 125 VAL   F CB  
10248 C  CG1 . VAL   F  129 ? 1.8597 0.4765 1.3738 0.1128  -0.1774 -0.0842 125 VAL   F CG1 
10249 C  CG2 . VAL   F  129 ? 1.8422 0.5273 1.3142 0.1415  -0.1730 -0.0727 125 VAL   F CG2 
10250 N  N   . ARG   F  130 ? 1.8545 0.4762 1.1620 0.0864  -0.1531 -0.0073 126 ARG   F N   
10251 C  CA  . ARG   F  130 ? 1.8402 0.4041 1.2046 0.0356  -0.1760 -0.0450 126 ARG   F CA  
10252 C  C   . ARG   F  130 ? 1.8967 0.5207 1.1788 0.0190  -0.1603 -0.0581 126 ARG   F C   
10253 O  O   . ARG   F  130 ? 2.0273 0.5669 1.2367 -0.0049 -0.1431 0.0441  126 ARG   F O   
10254 C  CB  . ARG   F  130 ? 1.8369 0.2822 1.1234 0.0688  -0.1471 -0.0712 126 ARG   F CB  
10255 C  CG  . ARG   F  130 ? 1.8458 0.2746 1.1420 0.0461  -0.1397 -0.0912 126 ARG   F CG  
10256 C  CD  . ARG   F  130 ? 1.8418 0.2163 1.1636 0.0176  -0.1417 -0.1088 126 ARG   F CD  
10257 N  NE  . ARG   F  130 ? 1.8997 0.1085 1.1676 0.0609  -0.0882 -0.1113 126 ARG   F NE  
10258 C  CZ  . ARG   F  130 ? 1.8814 0.0739 1.2074 -0.0089 -0.0651 -0.1695 126 ARG   F CZ  
10259 N  NH1 . ARG   F  130 ? 1.8877 0.0928 1.2143 -0.0415 -0.0763 -0.1776 126 ARG   F NH1 
10260 N  NH2 . ARG   F  130 ? 1.8451 0.1794 1.2710 -0.0708 -0.0367 -0.2023 126 ARG   F NH2 
10261 N  N   . PRO   F  131 ? 1.8466 0.5085 1.2660 -0.0147 -0.1813 -0.0799 127 PRO   F N   
10262 C  CA  . PRO   F  131 ? 1.7787 0.5168 1.2539 -0.0498 -0.1444 -0.1111 127 PRO   F CA  
10263 C  C   . PRO   F  131 ? 1.7390 0.4933 1.3070 0.0084  -0.1342 -0.1417 127 PRO   F C   
10264 O  O   . PRO   F  131 ? 1.7274 0.3054 1.3844 0.0856  -0.0393 -0.0276 127 PRO   F O   
10265 C  CB  . PRO   F  131 ? 1.7958 0.5226 1.2154 -0.0019 -0.1696 -0.1186 127 PRO   F CB  
10266 C  CG  . PRO   F  131 ? 1.8169 0.5169 1.2473 0.0009  -0.1861 -0.0703 127 PRO   F CG  
10267 C  CD  . PRO   F  131 ? 1.8234 0.5146 1.2695 -0.0065 -0.1961 -0.0708 127 PRO   F CD  
10268 N  N   . PHE   F  132 ? 1.8250 0.5415 1.2483 -0.0252 -0.0679 -0.1852 128 PHE   F N   
10269 C  CA  . PHE   F  132 ? 1.7720 0.5151 1.2594 0.0505  -0.0657 -0.2321 128 PHE   F CA  
10270 C  C   . PHE   F  132 ? 1.7923 0.5274 1.2744 0.0089  -0.0935 -0.3198 128 PHE   F C   
10271 O  O   . PHE   F  132 ? 1.7841 0.4942 1.3302 0.0208  -0.0488 -0.3993 128 PHE   F O   
10272 C  CB  . PHE   F  132 ? 1.7665 0.6070 1.2381 0.0688  -0.1010 -0.1771 128 PHE   F CB  
10273 C  CG  . PHE   F  132 ? 1.7246 0.5915 1.2525 0.1141  -0.1140 -0.1618 128 PHE   F CG  
10274 C  CD1 . PHE   F  132 ? 1.7099 0.6165 1.2828 0.1232  -0.1453 -0.1626 128 PHE   F CD1 
10275 C  CD2 . PHE   F  132 ? 1.7319 0.5600 1.2868 0.1122  -0.1056 -0.1720 128 PHE   F CD2 
10276 C  CE1 . PHE   F  132 ? 1.7356 0.6449 1.2977 0.0890  -0.1657 -0.1982 128 PHE   F CE1 
10277 C  CE2 . PHE   F  132 ? 1.7437 0.5845 1.3217 0.0974  -0.1195 -0.2009 128 PHE   F CE2 
10278 C  CZ  . PHE   F  132 ? 1.7061 0.7066 1.3157 0.0769  -0.1523 -0.1769 128 PHE   F CZ  
10279 N  N   . GLY   F  133 ? 1.8051 0.4423 1.3016 0.0858  -0.0491 -0.3253 129 GLY   F N   
10280 C  CA  . GLY   F  133 ? 1.8189 0.3735 1.3577 0.0950  -0.0485 -0.2769 129 GLY   F CA  
10281 C  C   . GLY   F  133 ? 1.8032 0.3383 1.3936 0.1032  -0.0463 -0.2415 129 GLY   F C   
10282 O  O   . GLY   F  133 ? 1.8098 0.1837 1.4406 0.0857  0.0307  -0.2204 129 GLY   F O   
10283 N  N   . VAL   F  134 ? 1.8117 0.4182 1.3720 0.0834  -0.0696 -0.2132 130 VAL   F N   
10284 C  CA  . VAL   F  134 ? 1.8263 0.5298 1.3507 0.1258  -0.0734 -0.1881 130 VAL   F CA  
10285 C  C   . VAL   F  134 ? 1.8491 0.6054 1.3452 0.1275  -0.0742 -0.2079 130 VAL   F C   
10286 O  O   . VAL   F  134 ? 1.8598 0.6940 1.3386 0.1306  -0.0487 -0.2736 130 VAL   F O   
10287 C  CB  . VAL   F  134 ? 1.7697 0.5282 1.3251 0.1367  -0.1061 -0.1492 130 VAL   F CB  
10288 C  CG1 . VAL   F  134 ? 1.7725 0.5485 1.3443 0.1424  -0.1084 -0.1329 130 VAL   F CG1 
10289 C  CG2 . VAL   F  134 ? 1.7547 0.5805 1.2766 0.1579  -0.1183 -0.1410 130 VAL   F CG2 
10290 N  N   . SER   F  135 ? 1.9107 0.6905 1.3303 0.1112  -0.0472 -0.1344 131 SER   F N   
10291 C  CA  . SER   F  135 ? 1.8380 0.6639 1.4702 0.0949  -0.0697 -0.0018 131 SER   F CA  
10292 C  C   . SER   F  135 ? 1.8524 0.5765 1.3770 0.1664  -0.0439 -0.0078 131 SER   F C   
10293 O  O   . SER   F  135 ? 1.8573 0.5320 1.4089 0.1442  0.0453  0.0511  131 SER   F O   
10294 C  CB  . SER   F  135 ? 1.7987 0.6664 1.4641 0.0317  -0.1213 0.0240  131 SER   F CB  
10295 O  OG  . SER   F  135 ? 1.8146 0.6365 1.6757 0.0281  -0.1939 0.1247  131 SER   F OG  
10296 N  N   . THR   F  136 ? 1.8242 0.6257 1.3268 0.2096  -0.0655 -0.0546 132 THR   F N   
10297 C  CA  . THR   F  136 ? 1.8416 0.6133 1.2114 0.2149  -0.0861 -0.0528 132 THR   F CA  
10298 C  C   . THR   F  136 ? 1.7384 0.5128 1.1838 0.2547  -0.0452 -0.0870 132 THR   F C   
10299 O  O   . THR   F  136 ? 1.7486 0.3885 0.9917 0.3232  -0.0265 -0.0727 132 THR   F O   
10300 C  CB  . THR   F  136 ? 1.9042 0.5730 1.2214 0.2051  -0.1424 -0.0513 132 THR   F CB  
10301 O  OG1 . THR   F  136 ? 1.9823 0.6106 1.2381 0.2335  -0.1610 -0.0290 132 THR   F OG1 
10302 C  CG2 . THR   F  136 ? 1.8889 0.6642 1.2442 0.1612  -0.1538 -0.0092 132 THR   F CG2 
10303 N  N   . ILE   F  137 ? 1.7535 0.5785 1.2151 0.2126  -0.0336 -0.1012 133 ILE   F N   
10304 C  CA  . ILE   F  137 ? 1.7450 0.6954 1.1885 0.1922  -0.0793 -0.1218 133 ILE   F CA  
10305 C  C   . ILE   F  137 ? 1.7581 0.6856 1.2055 0.2065  -0.0651 -0.1452 133 ILE   F C   
10306 O  O   . ILE   F  137 ? 1.7558 0.6234 1.2476 0.2668  -0.0827 -0.2023 133 ILE   F O   
10307 C  CB  . ILE   F  137 ? 1.7489 0.8132 1.1704 0.2065  -0.0598 -0.1197 133 ILE   F CB  
10308 C  CG1 . ILE   F  137 ? 1.7925 0.8038 1.2207 0.2253  -0.0678 -0.1272 133 ILE   F CG1 
10309 C  CG2 . ILE   F  137 ? 1.7361 0.8739 1.1430 0.1917  -0.0542 -0.1246 133 ILE   F CG2 
10310 C  CD1 . ILE   F  137 ? 1.7934 0.8518 1.2676 0.2234  -0.0432 -0.1451 133 ILE   F CD1 
10311 N  N   . PHE   F  138 ? 1.7192 0.6613 1.1757 0.1499  -0.0605 -0.1160 134 PHE   F N   
10312 C  CA  . PHE   F  138 ? 1.7126 0.6963 1.1788 0.0298  -0.0452 -0.1325 134 PHE   F CA  
10313 C  C   . PHE   F  138 ? 1.7207 0.7197 1.1568 0.0181  -0.0375 -0.1149 134 PHE   F C   
10314 O  O   . PHE   F  138 ? 1.6543 0.7249 1.0786 0.0289  -0.0410 -0.0318 134 PHE   F O   
10315 C  CB  . PHE   F  138 ? 1.6337 0.6649 1.1967 -0.0433 -0.0477 -0.1661 134 PHE   F CB  
10316 C  CG  . PHE   F  138 ? 1.6259 0.6012 1.2080 -0.0911 -0.0818 -0.1733 134 PHE   F CG  
10317 C  CD1 . PHE   F  138 ? 1.5655 0.6813 1.2325 -0.1293 -0.0799 -0.1208 134 PHE   F CD1 
10318 C  CD2 . PHE   F  138 ? 1.5549 0.5169 1.1646 -0.1581 -0.1054 -0.2033 134 PHE   F CD2 
10319 C  CE1 . PHE   F  138 ? 1.5564 0.7056 1.2072 -0.1131 -0.0967 -0.1259 134 PHE   F CE1 
10320 C  CE2 . PHE   F  138 ? 1.5404 0.5095 1.1226 -0.1471 -0.1398 -0.1966 134 PHE   F CE2 
10321 C  CZ  . PHE   F  138 ? 1.5323 0.6095 1.1370 -0.1776 -0.0914 -0.1300 134 PHE   F CZ  
10322 N  N   . GLY   F  139 ? 1.7738 0.7063 1.1362 0.0489  -0.0394 -0.0981 135 GLY   F N   
10323 C  CA  . GLY   F  139 ? 1.7801 0.8252 1.1244 0.0742  -0.0896 -0.1157 135 GLY   F CA  
10324 C  C   . GLY   F  139 ? 1.8302 0.8314 1.1744 0.0513  -0.1019 -0.1360 135 GLY   F C   
10325 O  O   . GLY   F  139 ? 1.8761 0.8976 1.0954 0.0676  -0.1004 -0.1686 135 GLY   F O   
10326 N  N   . GLY   F  140 ? 1.9020 0.7539 1.2389 0.0453  -0.1251 -0.1251 136 GLY   F N   
10327 C  CA  . GLY   F  140 ? 1.9478 0.7065 1.3094 0.0366  -0.1506 -0.1832 136 GLY   F CA  
10328 C  C   . GLY   F  140 ? 1.9918 0.6992 1.3380 0.0682  -0.1446 -0.1688 136 GLY   F C   
10329 O  O   . GLY   F  140 ? 2.0536 0.7232 1.4574 0.0316  -0.1775 -0.1935 136 GLY   F O   
10330 N  N   . VAL   F  141 ? 1.9885 0.6931 1.3604 0.0580  -0.0805 -0.2207 137 VAL   F N   
10331 C  CA  . VAL   F  141 ? 1.9301 0.6108 1.3565 0.0512  -0.0276 -0.2177 137 VAL   F CA  
10332 C  C   . VAL   F  141 ? 1.8994 0.5551 1.3358 0.0682  -0.0588 -0.1573 137 VAL   F C   
10333 O  O   . VAL   F  141 ? 1.9426 0.5676 1.3753 0.1024  -0.0781 -0.1929 137 VAL   F O   
10334 C  CB  . VAL   F  141 ? 1.9209 0.5923 1.4161 0.0385  -0.0143 -0.2188 137 VAL   F CB  
10335 C  CG1 . VAL   F  141 ? 1.8904 0.5507 1.4442 0.0266  -0.0258 -0.2332 137 VAL   F CG1 
10336 C  CG2 . VAL   F  141 ? 1.9221 0.6794 1.4300 0.0259  0.0346  -0.2611 137 VAL   F CG2 
10337 N  N   . ASP   F  142 ? 1.8917 0.5222 1.2465 0.0438  -0.0479 -0.1502 138 ASP   F N   
10338 C  CA  . ASP   F  142 ? 1.9167 0.5394 1.2650 0.0551  -0.0378 -0.1571 138 ASP   F CA  
10339 C  C   . ASP   F  142 ? 1.8748 0.6512 1.1937 0.0035  0.0009  -0.1449 138 ASP   F C   
10340 O  O   . ASP   F  142 ? 1.7264 0.5474 1.2416 -0.0556 0.0298  -0.1498 138 ASP   F O   
10341 C  CB  . ASP   F  142 ? 2.0120 0.4663 1.2320 0.0511  -0.0353 -0.1224 138 ASP   F CB  
10342 C  CG  . ASP   F  142 ? 2.0527 0.4159 1.2213 0.0669  -0.0542 -0.1094 138 ASP   F CG  
10343 O  OD1 . ASP   F  142 ? 2.0612 0.4002 1.2330 0.0647  -0.0769 -0.0627 138 ASP   F OD1 
10344 O  OD2 . ASP   F  142 ? 2.1018 0.4981 1.1943 0.0953  0.0334  -0.1151 138 ASP   F OD2 
10345 N  N   . LYS   F  143 ? 1.8513 0.7948 1.2727 0.0613  -0.0179 -0.0707 139 LYS   F N   
10346 C  CA  . LYS   F  143 ? 1.8407 0.8697 1.2735 0.0827  0.0062  -0.0357 139 LYS   F CA  
10347 C  C   . LYS   F  143 ? 1.8202 0.8454 1.1773 0.1186  0.0525  -0.0239 139 LYS   F C   
10348 O  O   . LYS   F  143 ? 1.7809 0.9272 1.0741 0.1096  0.0823  -0.0963 139 LYS   F O   
10349 C  CB  . LYS   F  143 ? 1.8543 0.9652 1.3840 0.1310  0.0681  -0.0002 139 LYS   F CB  
10350 C  CG  . LYS   F  143 ? 1.8487 1.1098 1.4413 0.1416  0.0657  0.0280  139 LYS   F CG  
10351 C  CD  . LYS   F  143 ? 1.8697 1.1680 1.3900 0.1482  0.1272  0.0479  139 LYS   F CD  
10352 C  CE  . LYS   F  143 ? 1.8741 1.1894 1.3083 0.1525  0.1320  0.1218  139 LYS   F CE  
10353 N  NZ  . LYS   F  143 ? 1.8772 1.1660 1.2232 0.1683  0.1312  0.1474  139 LYS   F NZ  
10354 N  N   . ASN   F  144 ? 1.7899 0.8303 1.1280 0.1148  0.0300  -0.0523 140 ASN   F N   
10355 C  CA  . ASN   F  144 ? 1.7559 0.7074 1.1401 0.1028  0.0501  -0.0073 140 ASN   F CA  
10356 C  C   . ASN   F  144 ? 1.7667 0.6109 1.1904 0.0084  0.0544  -0.1220 140 ASN   F C   
10357 O  O   . ASN   F  144 ? 1.8066 0.7035 1.3054 -0.1257 0.1354  -0.1785 140 ASN   F O   
10358 C  CB  . ASN   F  144 ? 1.7291 0.7015 1.0951 0.1652  0.0622  0.0386  140 ASN   F CB  
10359 C  CG  . ASN   F  144 ? 1.6819 0.7824 1.1160 0.2033  0.0466  0.1546  140 ASN   F CG  
10360 O  OD1 . ASN   F  144 ? 1.6697 0.7988 1.1095 0.2474  0.0268  0.2142  140 ASN   F OD1 
10361 N  ND2 . ASN   F  144 ? 1.6886 0.9504 1.0637 0.1917  0.0757  0.1992  140 ASN   F ND2 
10362 N  N   . GLY   F  145 ? 1.7893 0.6388 1.1631 -0.0194 0.0204  -0.2184 141 GLY   F N   
10363 C  CA  . GLY   F  145 ? 1.7665 0.6868 1.1318 -0.0371 0.0088  -0.2501 141 GLY   F CA  
10364 C  C   . GLY   F  145 ? 1.7718 0.6467 1.1545 -0.0542 -0.0295 -0.2626 141 GLY   F C   
10365 O  O   . GLY   F  145 ? 1.7617 0.5420 1.1402 -0.0342 -0.0519 -0.2304 141 GLY   F O   
10366 N  N   . ALA   F  146 ? 1.7751 0.6549 1.1881 -0.0607 -0.0526 -0.2986 142 ALA   F N   
10367 C  CA  . ALA   F  146 ? 1.7423 0.6770 1.1751 -0.0667 -0.0652 -0.3163 142 ALA   F CA  
10368 C  C   . ALA   F  146 ? 1.7995 0.6454 1.1890 -0.0676 -0.0611 -0.2885 142 ALA   F C   
10369 O  O   . ALA   F  146 ? 1.8003 0.7470 1.1644 -0.0925 -0.0698 -0.2121 142 ALA   F O   
10370 C  CB  . ALA   F  146 ? 1.7323 0.7520 1.2197 -0.0754 -0.0600 -0.3680 142 ALA   F CB  
10371 N  N   . HIS   F  147 ? 1.7790 0.5399 1.2337 -0.0722 -0.0678 -0.2672 143 HIS   F N   
10372 C  CA  . HIS   F  147 ? 1.7743 0.5674 1.2979 -0.0551 -0.0455 -0.2286 143 HIS   F CA  
10373 C  C   . HIS   F  147 ? 1.7613 0.5795 1.3629 -0.0570 -0.0706 -0.2205 143 HIS   F C   
10374 O  O   . HIS   F  147 ? 1.7985 0.3891 1.3174 -0.0319 -0.0311 -0.2738 143 HIS   F O   
10375 C  CB  . HIS   F  147 ? 1.7908 0.5808 1.2752 -0.0528 -0.0531 -0.2443 143 HIS   F CB  
10376 C  CG  . HIS   F  147 ? 1.7200 0.6677 1.2714 -0.0621 -0.0810 -0.2338 143 HIS   F CG  
10377 N  ND1 . HIS   F  147 ? 1.7209 0.7085 1.2948 -0.1278 -0.0418 -0.2118 143 HIS   F ND1 
10378 C  CD2 . HIS   F  147 ? 1.7259 0.7539 1.2665 -0.1036 -0.0849 -0.2847 143 HIS   F CD2 
10379 C  CE1 . HIS   F  147 ? 1.7291 0.6881 1.2369 -0.1611 -0.0486 -0.1886 143 HIS   F CE1 
10380 N  NE2 . HIS   F  147 ? 1.7343 0.7497 1.2252 -0.1783 -0.0642 -0.2301 143 HIS   F NE2 
10381 N  N   . LEU   F  148 ? 1.7970 0.5509 1.4738 -0.0361 -0.0595 -0.1481 144 LEU   F N   
10382 C  CA  . LEU   F  148 ? 1.8089 0.3705 1.5039 -0.0745 -0.0636 -0.2158 144 LEU   F CA  
10383 C  C   . LEU   F  148 ? 1.7878 0.3360 1.4584 -0.0831 -0.1112 -0.2207 144 LEU   F C   
10384 O  O   . LEU   F  148 ? 1.8135 0.4104 1.5515 -0.1553 -0.1076 -0.3169 144 LEU   F O   
10385 C  CB  . LEU   F  148 ? 1.8368 0.3645 1.4667 -0.0653 -0.0845 -0.2196 144 LEU   F CB  
10386 C  CG  . LEU   F  148 ? 1.8613 0.4868 1.4497 -0.0336 -0.1250 -0.1621 144 LEU   F CG  
10387 C  CD1 . LEU   F  148 ? 1.8673 0.4292 1.4725 -0.0414 -0.1332 -0.1555 144 LEU   F CD1 
10388 C  CD2 . LEU   F  148 ? 1.8944 0.5235 1.4227 -0.0014 -0.1097 -0.1479 144 LEU   F CD2 
10389 N  N   . TYR   F  149 ? 1.7873 0.3805 1.4500 -0.0415 -0.0924 -0.2092 145 TYR   F N   
10390 C  CA  . TYR   F  149 ? 1.7447 0.4353 1.4440 -0.0248 -0.0901 -0.2083 145 TYR   F CA  
10391 C  C   . TYR   F  149 ? 1.7892 0.4993 1.4801 0.0205  -0.0730 -0.1589 145 TYR   F C   
10392 O  O   . TYR   F  149 ? 1.7685 0.4322 1.4955 0.1071  -0.0768 -0.0933 145 TYR   F O   
10393 C  CB  . TYR   F  149 ? 1.7287 0.4266 1.4513 -0.0518 -0.1215 -0.2491 145 TYR   F CB  
10394 C  CG  . TYR   F  149 ? 1.6951 0.4073 1.4376 -0.1046 -0.1496 -0.2448 145 TYR   F CG  
10395 C  CD1 . TYR   F  149 ? 1.6966 0.4182 1.4326 -0.1095 -0.1560 -0.2685 145 TYR   F CD1 
10396 C  CD2 . TYR   F  149 ? 1.7212 0.4244 1.4367 -0.1111 -0.1411 -0.2287 145 TYR   F CD2 
10397 C  CE1 . TYR   F  149 ? 1.6648 0.4212 1.4273 -0.1236 -0.1401 -0.2604 145 TYR   F CE1 
10398 C  CE2 . TYR   F  149 ? 1.6699 0.4859 1.4140 -0.1095 -0.1568 -0.2815 145 TYR   F CE2 
10399 C  CZ  . TYR   F  149 ? 1.6643 0.4056 1.4086 -0.0926 -0.1504 -0.2696 145 TYR   F CZ  
10400 O  OH  . TYR   F  149 ? 1.6344 0.4701 1.4258 0.0000  -0.1337 -0.3956 145 TYR   F OH  
10401 N  N   . MET   F  150 ? 1.7805 0.5124 1.4462 0.0139  -0.0904 -0.1519 146 MET   F N   
10402 C  CA  . MET   F  150 ? 1.8427 0.4853 1.4265 -0.0035 -0.0770 -0.1609 146 MET   F CA  
10403 C  C   . MET   F  150 ? 1.8322 0.3640 1.3709 -0.0045 -0.0899 -0.2099 146 MET   F C   
10404 O  O   . MET   F  150 ? 1.8660 0.1082 1.2824 -0.0403 -0.0854 -0.3018 146 MET   F O   
10405 C  CB  . MET   F  150 ? 1.9249 0.5134 1.4358 0.0164  -0.1190 -0.1881 146 MET   F CB  
10406 C  CG  . MET   F  150 ? 1.9819 0.5792 1.4928 0.0278  -0.1391 -0.1204 146 MET   F CG  
10407 S  SD  . MET   F  150 ? 2.0701 0.6702 1.5121 0.0562  -0.1356 -0.1586 146 MET   F SD  
10408 C  CE  . MET   F  150 ? 2.1355 0.7597 1.5090 -0.0041 -0.1524 -0.1369 146 MET   F CE  
10409 N  N   . LEU   F  151 ? 1.8633 0.3844 1.3332 0.0355  -0.0469 -0.1154 147 LEU   F N   
10410 C  CA  . LEU   F  151 ? 1.8608 0.5105 1.3323 0.0362  -0.0503 -0.0936 147 LEU   F CA  
10411 C  C   . LEU   F  151 ? 1.8596 0.5478 1.3874 0.0266  -0.0594 -0.0538 147 LEU   F C   
10412 O  O   . LEU   F  151 ? 1.8158 0.6940 1.6089 -0.0437 -0.0169 -0.0762 147 LEU   F O   
10413 C  CB  . LEU   F  151 ? 1.8518 0.5338 1.2205 0.0323  -0.0422 -0.0766 147 LEU   F CB  
10414 C  CG  . LEU   F  151 ? 1.8879 0.5299 1.1758 0.0462  -0.0726 -0.0866 147 LEU   F CG  
10415 C  CD1 . LEU   F  151 ? 1.8873 0.5622 1.1221 0.0877  -0.0751 -0.0839 147 LEU   F CD1 
10416 C  CD2 . LEU   F  151 ? 1.8763 0.5169 1.1783 0.0072  -0.0945 -0.0500 147 LEU   F CD2 
10417 N  N   . GLU   F  152 ? 1.8141 0.5867 1.3467 0.0176  -0.1126 -0.0438 148 GLU   F N   
10418 C  CA  . GLU   F  152 ? 1.7899 0.5847 1.3370 0.0395  -0.1033 -0.0445 148 GLU   F CA  
10419 C  C   . GLU   F  152 ? 1.7232 0.3979 1.3017 0.0510  -0.1357 0.0092  148 GLU   F C   
10420 O  O   . GLU   F  152 ? 1.6493 0.3703 1.1265 -0.0168 -0.1303 -0.0021 148 GLU   F O   
10421 C  CB  . GLU   F  152 ? 1.8709 0.6129 1.4293 0.0544  -0.2012 -0.0625 148 GLU   F CB  
10422 C  CG  . GLU   F  152 ? 1.9166 0.7796 1.4433 0.0730  -0.2004 -0.0814 148 GLU   F CG  
10423 C  CD  . GLU   F  152 ? 2.0292 1.0048 1.4990 0.0576  -0.3024 -0.1348 148 GLU   F CD  
10424 O  OE1 . GLU   F  152 ? 2.0389 1.2885 1.6246 0.0069  -0.3824 -0.2312 148 GLU   F OE1 
10425 O  OE2 . GLU   F  152 ? 2.0377 1.0276 1.6505 0.1946  -0.2301 -0.0222 148 GLU   F OE2 
10426 N  N   . PRO   F  153 ? 1.7180 0.3876 1.3198 0.0972  -0.0808 0.0227  149 PRO   F N   
10427 C  CA  . PRO   F  153 ? 1.7157 0.3641 1.3406 0.1225  -0.0706 0.0766  149 PRO   F CA  
10428 C  C   . PRO   F  153 ? 1.7055 0.3239 1.4221 0.1021  -0.0879 0.0993  149 PRO   F C   
10429 O  O   . PRO   F  153 ? 1.7446 0.1697 1.4455 0.1477  0.0012  0.2108  149 PRO   F O   
10430 C  CB  . PRO   F  153 ? 1.6980 0.3879 1.3681 0.1343  -0.0768 0.0967  149 PRO   F CB  
10431 C  CG  . PRO   F  153 ? 1.7207 0.4230 1.3218 0.1458  -0.0784 0.0652  149 PRO   F CG  
10432 C  CD  . PRO   F  153 ? 1.7361 0.4242 1.2807 0.1293  -0.0717 0.0345  149 PRO   F CD  
10433 N  N   . SER   F  154 ? 1.7227 0.3887 1.3398 0.0959  -0.0610 0.0745  150 SER   F N   
10434 C  CA  . SER   F  154 ? 1.7141 0.4563 1.2725 0.0990  -0.1044 0.0537  150 SER   F CA  
10435 C  C   . SER   F  154 ? 1.7093 0.4607 1.1967 0.1167  -0.1349 -0.0373 150 SER   F C   
10436 O  O   . SER   F  154 ? 1.6915 0.4386 1.1381 0.1573  -0.1909 -0.1183 150 SER   F O   
10437 C  CB  . SER   F  154 ? 1.6836 0.5291 1.1899 0.1148  -0.1103 0.0848  150 SER   F CB  
10438 O  OG  . SER   F  154 ? 1.6345 0.5196 1.2479 0.1311  -0.0948 0.1604  150 SER   F OG  
10439 N  N   . GLY   F  155 ? 1.7775 0.4916 1.1487 0.0783  -0.1224 -0.0640 151 GLY   F N   
10440 C  CA  . GLY   F  155 ? 1.8104 0.4744 1.1976 0.1042  -0.1180 -0.1280 151 GLY   F CA  
10441 C  C   . GLY   F  155 ? 1.8461 0.5221 1.1781 0.0888  -0.1044 -0.2019 151 GLY   F C   
10442 O  O   . GLY   F  155 ? 1.8965 0.4169 1.1426 0.0104  -0.0394 -0.2652 151 GLY   F O   
10443 N  N   . SER   F  156 ? 1.8206 0.4999 1.1833 0.0972  -0.0969 -0.1879 152 SER   F N   
10444 C  CA  . SER   F  156 ? 1.7968 0.5120 1.1944 0.0873  -0.1340 -0.0988 152 SER   F CA  
10445 C  C   . SER   F  156 ? 1.7974 0.4336 1.2307 0.1137  -0.1025 -0.1395 152 SER   F C   
10446 O  O   . SER   F  156 ? 1.7997 0.4373 1.2195 0.1322  -0.0983 -0.1762 152 SER   F O   
10447 C  CB  . SER   F  156 ? 1.7590 0.4887 1.2155 0.0080  -0.1714 -0.0311 152 SER   F CB  
10448 O  OG  . SER   F  156 ? 1.7506 0.4274 1.1995 0.0317  -0.1767 0.0680  152 SER   F OG  
10449 N  N   . TYR   F  157 ? 1.7942 0.3635 1.2423 0.1115  -0.1288 -0.1774 153 TYR   F N   
10450 C  CA  . TYR   F  157 ? 1.7806 0.4033 1.2332 0.1090  -0.1021 -0.2212 153 TYR   F CA  
10451 C  C   . TYR   F  157 ? 1.7599 0.3634 1.2069 0.0836  -0.0763 -0.2375 153 TYR   F C   
10452 O  O   . TYR   F  157 ? 1.7519 0.2686 1.1605 0.0684  -0.0730 -0.2587 153 TYR   F O   
10453 C  CB  . TYR   F  157 ? 1.7329 0.4510 1.2021 0.1252  -0.1650 -0.2423 153 TYR   F CB  
10454 C  CG  . TYR   F  157 ? 1.7678 0.4107 1.1918 0.1236  -0.1764 -0.2784 153 TYR   F CG  
10455 C  CD1 . TYR   F  157 ? 1.7711 0.4408 1.1883 0.1000  -0.1563 -0.2639 153 TYR   F CD1 
10456 C  CD2 . TYR   F  157 ? 1.7720 0.4374 1.1137 0.1374  -0.2462 -0.2979 153 TYR   F CD2 
10457 C  CE1 . TYR   F  157 ? 1.7232 0.5402 1.1581 0.1258  -0.1725 -0.2744 153 TYR   F CE1 
10458 C  CE2 . TYR   F  157 ? 1.7095 0.5122 1.1574 0.1421  -0.2238 -0.3049 153 TYR   F CE2 
10459 C  CZ  . TYR   F  157 ? 1.6653 0.4888 1.1762 0.1743  -0.1905 -0.3004 153 TYR   F CZ  
10460 O  OH  . TYR   F  157 ? 1.6331 0.4834 1.1519 0.1632  -0.1569 -0.3315 153 TYR   F OH  
10461 N  N   . TRP   F  158 ? 1.7956 0.4042 1.2451 0.0671  -0.0405 -0.1985 154 TRP   F N   
10462 C  CA  . TRP   F  158 ? 1.8084 0.5097 1.2666 0.0926  -0.0551 -0.1772 154 TRP   F CA  
10463 C  C   . TRP   F  158 ? 1.8030 0.5767 1.2809 0.1103  -0.0216 -0.1527 154 TRP   F C   
10464 O  O   . TRP   F  158 ? 1.7903 0.6483 1.3596 0.1371  -0.0138 -0.2064 154 TRP   F O   
10465 C  CB  . TRP   F  158 ? 1.8439 0.5736 1.2404 0.0804  -0.0521 -0.2148 154 TRP   F CB  
10466 C  CG  . TRP   F  158 ? 1.8301 0.5736 1.2553 0.0885  -0.0462 -0.2229 154 TRP   F CG  
10467 C  CD1 . TRP   F  158 ? 1.8902 0.5078 1.3647 0.1159  -0.0346 -0.2989 154 TRP   F CD1 
10468 C  CD2 . TRP   F  158 ? 1.8200 0.6354 1.2394 0.1121  -0.0807 -0.2450 154 TRP   F CD2 
10469 N  NE1 . TRP   F  158 ? 1.8555 0.5363 1.4173 0.1304  -0.0464 -0.3012 154 TRP   F NE1 
10470 C  CE2 . TRP   F  158 ? 1.8328 0.5702 1.2859 0.1226  -0.0843 -0.2935 154 TRP   F CE2 
10471 C  CE3 . TRP   F  158 ? 1.8393 0.6168 1.2006 0.1058  -0.0730 -0.2221 154 TRP   F CE3 
10472 C  CZ2 . TRP   F  158 ? 1.8410 0.6330 1.2324 0.1287  -0.0754 -0.3211 154 TRP   F CZ2 
10473 C  CZ3 . TRP   F  158 ? 1.8426 0.6481 1.1829 0.1373  -0.0612 -0.2393 154 TRP   F CZ3 
10474 C  CH2 . TRP   F  158 ? 1.8652 0.6367 1.1676 0.1262  -0.0558 -0.2707 154 TRP   F CH2 
10475 N  N   . GLY   F  159 ? 1.7779 0.6357 1.2424 0.0782  0.0008  -0.1324 155 GLY   F N   
10476 C  CA  . GLY   F  159 ? 1.7733 0.6378 1.2242 0.0614  -0.0304 -0.1164 155 GLY   F CA  
10477 C  C   . GLY   F  159 ? 1.7859 0.5152 1.2299 0.0285  -0.0852 -0.1117 155 GLY   F C   
10478 O  O   . GLY   F  159 ? 1.7471 0.5640 1.1606 0.0505  -0.1291 -0.1668 155 GLY   F O   
10479 N  N   . TYR   F  160 ? 1.8081 0.5454 1.2492 0.0346  -0.0519 -0.0681 156 TYR   F N   
10480 C  CA  . TYR   F  160 ? 1.8522 0.6563 1.2293 0.0339  -0.0242 -0.1153 156 TYR   F CA  
10481 C  C   . TYR   F  160 ? 1.8607 0.7762 1.2094 0.0215  -0.0263 -0.1033 156 TYR   F C   
10482 O  O   . TYR   F  160 ? 1.8419 0.8502 1.1956 -0.0680 -0.0073 -0.1413 156 TYR   F O   
10483 C  CB  . TYR   F  160 ? 1.8694 0.6947 1.2619 0.0199  -0.0298 -0.0694 156 TYR   F CB  
10484 C  CG  . TYR   F  160 ? 1.8951 0.5291 1.3113 0.0212  -0.0612 -0.1121 156 TYR   F CG  
10485 C  CD1 . TYR   F  160 ? 1.8894 0.5791 1.2850 0.0159  -0.0295 -0.0126 156 TYR   F CD1 
10486 C  CD2 . TYR   F  160 ? 1.8585 0.4946 1.2935 -0.0077 -0.0702 -0.0663 156 TYR   F CD2 
10487 C  CE1 . TYR   F  160 ? 1.8794 0.4093 1.3215 0.0116  -0.0886 -0.0601 156 TYR   F CE1 
10488 C  CE2 . TYR   F  160 ? 1.8527 0.4401 1.3050 -0.0206 -0.1020 -0.0858 156 TYR   F CE2 
10489 C  CZ  . TYR   F  160 ? 1.8517 0.4137 1.3064 -0.0374 -0.0960 -0.0703 156 TYR   F CZ  
10490 O  OH  . TYR   F  160 ? 1.8922 0.3919 1.4446 -0.0852 -0.0974 -0.0444 156 TYR   F OH  
10491 N  N   . LYS   F  161 ? 1.8553 0.7799 1.2403 0.0475  -0.0304 -0.1204 157 LYS   F N   
10492 C  CA  . LYS   F  161 ? 1.8699 0.7747 1.2526 0.0404  -0.0144 -0.1456 157 LYS   F CA  
10493 C  C   . LYS   F  161 ? 1.8686 0.7559 1.2778 0.0596  0.0075  -0.1175 157 LYS   F C   
10494 O  O   . LYS   F  161 ? 1.8604 0.7428 1.1415 0.0744  0.0317  -0.1419 157 LYS   F O   
10495 C  CB  . LYS   F  161 ? 1.9145 0.7570 1.3069 0.0319  -0.0213 -0.1911 157 LYS   F CB  
10496 C  CG  . LYS   F  161 ? 1.9240 0.8077 1.2829 0.0371  -0.0500 -0.2643 157 LYS   F CG  
10497 C  CD  . LYS   F  161 ? 1.9975 0.8410 1.3325 0.0019  -0.0456 -0.3001 157 LYS   F CD  
10498 C  CE  . LYS   F  161 ? 1.9786 0.9067 1.3427 -0.0465 -0.0829 -0.3288 157 LYS   F CE  
10499 N  NZ  . LYS   F  161 ? 2.0112 0.9711 1.3772 -0.1246 -0.0730 -0.3286 157 LYS   F NZ  
10500 N  N   . GLY   F  162 ? 1.8675 0.7310 1.3293 0.0868  -0.0184 -0.1419 158 GLY   F N   
10501 C  CA  . GLY   F  162 ? 1.8572 0.7155 1.3433 0.1047  -0.0165 -0.1770 158 GLY   F CA  
10502 C  C   . GLY   F  162 ? 1.8496 0.6577 1.3420 0.1405  -0.0181 -0.1873 158 GLY   F C   
10503 O  O   . GLY   F  162 ? 1.8814 0.5725 1.3147 0.1201  -0.0464 -0.2033 158 GLY   F O   
10504 N  N   . ALA   F  163 ? 1.8348 0.6727 1.3209 0.2156  0.0077  -0.1709 159 ALA   F N   
10505 C  CA  . ALA   F  163 ? 1.8301 0.6499 1.3653 0.2242  0.0681  -0.1512 159 ALA   F CA  
10506 C  C   . ALA   F  163 ? 1.8027 0.6860 1.3597 0.2115  0.0804  -0.1499 159 ALA   F C   
10507 O  O   . ALA   F  163 ? 1.7979 0.8219 1.3907 0.1688  0.0582  -0.1534 159 ALA   F O   
10508 C  CB  . ALA   F  163 ? 1.8395 0.5881 1.4015 0.2455  0.0681  -0.1245 159 ALA   F CB  
10509 N  N   . ALA   F  164 ? 1.7328 0.6328 1.3298 0.2433  0.0660  -0.1938 160 ALA   F N   
10510 C  CA  . ALA   F  164 ? 1.7061 0.6520 1.3167 0.2154  0.0483  -0.1785 160 ALA   F CA  
10511 C  C   . ALA   F  164 ? 1.6655 0.6133 1.2968 0.2289  0.0327  -0.1944 160 ALA   F C   
10512 O  O   . ALA   F  164 ? 1.6035 0.6060 1.2589 0.3327  0.0556  -0.2090 160 ALA   F O   
10513 C  CB  . ALA   F  164 ? 1.6998 0.7137 1.3081 0.2300  0.0526  -0.1897 160 ALA   F CB  
10514 N  N   . THR   F  165 ? 1.6951 0.6162 1.2998 0.1427  0.0070  -0.2036 161 THR   F N   
10515 C  CA  . THR   F  165 ? 1.7569 0.6050 1.3098 0.1305  -0.0193 -0.1855 161 THR   F CA  
10516 C  C   . THR   F  165 ? 1.7446 0.5736 1.3772 0.1060  -0.0239 -0.1523 161 THR   F C   
10517 O  O   . THR   F  165 ? 1.7785 0.5118 1.3882 0.1040  -0.0070 -0.1141 161 THR   F O   
10518 C  CB  . THR   F  165 ? 1.7501 0.5680 1.2603 0.1470  -0.0424 -0.1502 161 THR   F CB  
10519 O  OG1 . THR   F  165 ? 1.8429 0.6046 1.2523 0.1528  -0.0530 -0.1206 161 THR   F OG1 
10520 C  CG2 . THR   F  165 ? 1.7142 0.5658 1.2732 0.1570  -0.0321 -0.1542 161 THR   F CG2 
10521 N  N   . GLY   F  166 ? 1.8482 0.5810 1.4545 0.1296  -0.0480 -0.1202 162 GLY   F N   
10522 C  CA  . GLY   F  166 ? 1.8710 0.6105 1.5538 0.1184  -0.0895 -0.1026 162 GLY   F CA  
10523 C  C   . GLY   F  166 ? 1.9550 0.5528 1.6152 0.0158  -0.1088 -0.0883 162 GLY   F C   
10524 O  O   . GLY   F  166 ? 1.9873 0.3635 1.6914 -0.0714 -0.0689 -0.0164 162 GLY   F O   
10525 N  N   . LYS   F  167 ? 2.0162 0.5415 1.6361 0.0807  -0.0878 -0.0478 163 LYS   F N   
10526 C  CA  . LYS   F  167 ? 2.0551 0.5997 1.6278 0.1676  -0.0775 -0.0803 163 LYS   F CA  
10527 C  C   . LYS   F  167 ? 2.0532 0.5418 1.6063 0.1406  -0.0286 -0.0240 163 LYS   F C   
10528 O  O   . LYS   F  167 ? 2.0033 0.6424 1.6010 0.0344  -0.0701 -0.0684 163 LYS   F O   
10529 C  CB  . LYS   F  167 ? 2.0687 0.9102 1.6729 0.2002  -0.1237 -0.1376 163 LYS   F CB  
10530 C  CG  . LYS   F  167 ? 2.1127 0.9444 1.7334 0.2573  -0.1796 -0.1411 163 LYS   F CG  
10531 C  CD  . LYS   F  167 ? 2.1201 1.1162 1.7477 0.2179  -0.2473 -0.1416 163 LYS   F CD  
10532 C  CE  . LYS   F  167 ? 2.1429 1.2473 1.7965 0.1597  -0.2801 -0.1058 163 LYS   F CE  
10533 N  NZ  . LYS   F  167 ? 2.1277 1.2833 1.8086 0.1385  -0.2914 -0.0352 163 LYS   F NZ  
10534 N  N   . GLY   F  168 ? 2.0819 0.3944 1.6499 0.1495  -0.0139 -0.0911 164 GLY   F N   
10535 C  CA  . GLY   F  168 ? 2.0857 0.3894 1.6549 0.1241  0.0270  -0.0793 164 GLY   F CA  
10536 C  C   . GLY   F  168 ? 2.0745 0.3301 1.5983 0.0819  0.0304  -0.0890 164 GLY   F C   
10537 O  O   . GLY   F  168 ? 2.1105 0.2541 1.5993 0.0524  0.0390  -0.1106 164 GLY   F O   
10538 N  N   . ARG   F  169 ? 2.0540 0.3650 1.5903 0.0505  0.0100  -0.1113 165 ARG   F N   
10539 C  CA  . ARG   F  169 ? 2.0168 0.4763 1.5162 0.0548  0.0014  -0.1407 165 ARG   F CA  
10540 C  C   . ARG   F  169 ? 1.9918 0.5941 1.5103 0.0184  0.0175  -0.1577 165 ARG   F C   
10541 O  O   . ARG   F  169 ? 1.9208 0.6388 1.4053 -0.0144 0.0240  -0.1986 165 ARG   F O   
10542 C  CB  . ARG   F  169 ? 2.0339 0.4682 1.4509 0.0985  -0.0256 -0.1724 165 ARG   F CB  
10543 C  CG  . ARG   F  169 ? 2.0691 0.4205 1.4139 0.1153  -0.0495 -0.2115 165 ARG   F CG  
10544 C  CD  . ARG   F  169 ? 2.1195 0.4610 1.3885 0.1040  -0.0480 -0.2612 165 ARG   F CD  
10545 N  NE  . ARG   F  169 ? 2.1430 0.6105 1.3993 0.1107  -0.0855 -0.2952 165 ARG   F NE  
10546 C  CZ  . ARG   F  169 ? 2.1764 0.6150 1.4772 0.0410  -0.0754 -0.2816 165 ARG   F CZ  
10547 N  NH1 . ARG   F  169 ? 2.1427 0.7435 1.5370 -0.0252 -0.0970 -0.2392 165 ARG   F NH1 
10548 N  NH2 . ARG   F  169 ? 2.1734 0.6647 1.4983 0.0532  -0.0798 -0.2766 165 ARG   F NH2 
10549 N  N   . GLN   F  170 ? 2.0098 0.5918 1.5646 0.0163  0.0106  -0.1239 166 GLN   F N   
10550 C  CA  . GLN   F  170 ? 1.9948 0.6724 1.5982 0.0253  -0.0098 -0.1552 166 GLN   F CA  
10551 C  C   . GLN   F  170 ? 1.9491 0.5633 1.6306 0.0877  0.0189  -0.1968 166 GLN   F C   
10552 O  O   . GLN   F  170 ? 1.9752 0.3749 1.6043 0.2389  0.0803  -0.2356 166 GLN   F O   
10553 C  CB  . GLN   F  170 ? 2.0525 0.7175 1.7854 -0.0403 -0.1016 -0.0717 166 GLN   F CB  
10554 C  CG  . GLN   F  170 ? 1.9924 0.9986 1.8720 -0.0959 -0.1181 -0.0653 166 GLN   F CG  
10555 C  CD  . GLN   F  170 ? 2.0548 1.0793 2.0571 -0.1768 -0.1593 0.0781  166 GLN   F CD  
10556 O  OE1 . GLN   F  170 ? 1.9882 1.3965 2.2056 -0.2509 -0.2485 0.1731  166 GLN   F OE1 
10557 N  NE2 . GLN   F  170 ? 2.0241 1.2494 2.0947 -0.1957 -0.1938 0.1330  166 GLN   F NE2 
10558 N  N   . SER   F  171 ? 1.9182 0.6050 1.5841 0.0575  0.0544  -0.2108 167 SER   F N   
10559 C  CA  . SER   F  171 ? 1.8573 0.7315 1.6040 0.0368  0.0347  -0.2103 167 SER   F CA  
10560 C  C   . SER   F  171 ? 1.8082 0.7270 1.5727 0.0341  0.0568  -0.2216 167 SER   F C   
10561 O  O   . SER   F  171 ? 1.7253 0.7278 1.5515 0.0557  0.0794  -0.2905 167 SER   F O   
10562 C  CB  . SER   F  171 ? 1.8501 0.7890 1.6459 0.0429  0.0395  -0.1593 167 SER   F CB  
10563 O  OG  . SER   F  171 ? 1.8645 0.9598 1.6764 0.0317  0.0363  -0.0817 167 SER   F OG  
10564 N  N   . ALA   F  172 ? 1.8487 0.6784 1.5706 0.0040  0.0362  -0.1909 168 ALA   F N   
10565 C  CA  . ALA   F  172 ? 1.8852 0.7244 1.5860 -0.0154 0.0112  -0.0726 168 ALA   F CA  
10566 C  C   . ALA   F  172 ? 1.9547 0.6633 1.5707 -0.0205 -0.0416 -0.0673 168 ALA   F C   
10567 O  O   . ALA   F  172 ? 1.9576 0.9007 1.4996 -0.0342 -0.0659 -0.0174 168 ALA   F O   
10568 C  CB  . ALA   F  172 ? 1.8579 0.7389 1.5624 -0.0058 0.0122  -0.0567 168 ALA   F CB  
10569 N  N   . LYS   F  173 ? 2.0481 0.4885 1.5459 -0.0300 -0.0204 -0.0548 169 LYS   F N   
10570 C  CA  . LYS   F  173 ? 2.0730 0.4728 1.5297 0.0477  -0.0063 -0.0676 169 LYS   F CA  
10571 C  C   . LYS   F  173 ? 2.1351 0.5715 1.5317 0.0337  -0.0271 -0.0810 169 LYS   F C   
10572 O  O   . LYS   F  173 ? 2.1145 0.4590 1.5781 0.0963  -0.0845 -0.1789 169 LYS   F O   
10573 C  CB  . LYS   F  173 ? 2.1137 0.4489 1.5289 0.0644  0.0548  -0.1012 169 LYS   F CB  
10574 C  CG  . LYS   F  173 ? 2.1517 0.5025 1.5335 0.1170  0.0623  -0.0896 169 LYS   F CG  
10575 C  CD  . LYS   F  173 ? 2.1671 0.6287 1.5682 0.0900  0.0503  -0.0797 169 LYS   F CD  
10576 C  CE  . LYS   F  173 ? 2.2259 0.7706 1.5037 0.0906  0.0717  -0.0261 169 LYS   F CE  
10577 N  NZ  . LYS   F  173 ? 2.2717 0.8640 1.5099 0.1013  0.0956  0.0344  169 LYS   F NZ  
10578 N  N   . ALA   F  174 ? 2.0855 0.6808 1.5283 0.1121  0.0150  -0.0998 170 ALA   F N   
10579 C  CA  . ALA   F  174 ? 2.0650 0.7592 1.5434 0.1277  0.0244  -0.1298 170 ALA   F CA  
10580 C  C   . ALA   F  174 ? 2.0544 0.8898 1.5635 0.1221  0.0778  -0.1041 170 ALA   F C   
10581 O  O   . ALA   F  174 ? 2.1041 1.0568 1.5663 0.1733  0.0850  -0.0595 170 ALA   F O   
10582 C  CB  . ALA   F  174 ? 2.0622 0.7227 1.5390 0.0972  -0.0003 -0.1485 170 ALA   F CB  
10583 N  N   . GLU   F  175 ? 2.0186 0.8991 1.6223 0.1079  0.1262  -0.1328 171 GLU   F N   
10584 C  CA  . GLU   F  175 ? 2.0028 0.9961 1.6378 0.0866  0.1765  -0.1455 171 GLU   F CA  
10585 C  C   . GLU   F  175 ? 1.9587 1.0271 1.5591 0.0850  0.1656  -0.1124 171 GLU   F C   
10586 O  O   . GLU   F  175 ? 1.8176 0.9376 1.6299 0.0548  0.1939  -0.0812 171 GLU   F O   
10587 C  CB  . GLU   F  175 ? 1.9834 1.0450 1.6445 0.0751  0.1952  -0.1301 171 GLU   F CB  
10588 C  CG  . GLU   F  175 ? 2.0618 1.1121 1.6724 0.0757  0.2570  -0.0922 171 GLU   F CG  
10589 C  CD  . GLU   F  175 ? 2.0962 1.0326 1.7088 0.0580  0.3063  -0.0438 171 GLU   F CD  
10590 O  OE1 . GLU   F  175 ? 2.0830 1.0535 1.7615 0.0408  0.2778  -0.0076 171 GLU   F OE1 
10591 O  OE2 . GLU   F  175 ? 2.1813 1.1785 1.7599 0.0510  0.3586  0.0191  171 GLU   F OE2 
10592 N  N   . LEU   F  176 ? 1.9929 1.0088 1.5346 0.1104  0.1318  -0.1487 172 LEU   F N   
10593 C  CA  . LEU   F  176 ? 2.0169 0.9293 1.4696 0.0701  0.1250  -0.1758 172 LEU   F CA  
10594 C  C   . LEU   F  176 ? 2.0629 0.8853 1.4290 0.0690  0.1356  -0.2287 172 LEU   F C   
10595 O  O   . LEU   F  176 ? 2.0534 0.8657 1.3847 0.1053  0.1530  -0.2660 172 LEU   F O   
10596 C  CB  . LEU   F  176 ? 1.9691 0.9346 1.4664 0.0470  0.1169  -0.1537 172 LEU   F CB  
10597 C  CG  . LEU   F  176 ? 1.8980 0.9823 1.4747 -0.0272 0.0977  -0.1332 172 LEU   F CG  
10598 C  CD1 . LEU   F  176 ? 1.8994 0.9966 1.4924 -0.0478 0.0945  -0.1450 172 LEU   F CD1 
10599 C  CD2 . LEU   F  176 ? 1.9055 0.9478 1.4765 -0.0412 0.1032  -0.1388 172 LEU   F CD2 
10600 N  N   . GLU   F  177 ? 2.1006 0.8798 1.3774 0.0600  0.1189  -0.2342 173 GLU   F N   
10601 C  CA  . GLU   F  177 ? 2.1649 0.8375 1.3579 0.0547  0.0938  -0.2444 173 GLU   F CA  
10602 C  C   . GLU   F  177 ? 2.2001 0.6378 1.3005 0.0449  0.0138  -0.2052 173 GLU   F C   
10603 O  O   . GLU   F  177 ? 2.2809 0.2775 1.2594 0.0059  -0.0083 -0.2815 173 GLU   F O   
10604 C  CB  . GLU   F  177 ? 2.1350 0.9340 1.3604 -0.0260 0.1226  -0.2232 173 GLU   F CB  
10605 C  CG  . GLU   F  177 ? 2.1004 1.0489 1.4009 -0.0315 0.1383  -0.2644 173 GLU   F CG  
10606 C  CD  . GLU   F  177 ? 2.0717 1.1813 1.4348 -0.1261 0.1490  -0.1988 173 GLU   F CD  
10607 O  OE1 . GLU   F  177 ? 2.0583 1.4007 1.4965 -0.1262 0.2035  -0.0741 173 GLU   F OE1 
10608 O  OE2 . GLU   F  177 ? 2.1567 1.3887 1.4714 -0.1426 0.1084  -0.2660 173 GLU   F OE2 
10609 N  N   . LYS   F  178 ? 2.2162 0.7217 1.4047 0.0613  0.0586  -0.1471 174 LYS   F N   
10610 C  CA  . LYS   F  178 ? 2.2212 0.9060 1.4465 0.0642  0.0907  -0.0576 174 LYS   F CA  
10611 C  C   . LYS   F  178 ? 2.2352 0.9013 1.4297 0.0198  0.0796  -0.0854 174 LYS   F C   
10612 O  O   . LYS   F  178 ? 2.2412 1.0305 1.4024 -0.0221 0.0986  -0.1054 174 LYS   F O   
10613 C  CB  . LYS   F  178 ? 2.2151 1.0114 1.5617 0.0913  0.1344  0.0089  174 LYS   F CB  
10614 C  CG  . LYS   F  178 ? 2.2284 1.0129 1.6379 0.1456  0.1439  0.0049  174 LYS   F CG  
10615 C  CD  . LYS   F  178 ? 2.2219 1.0868 1.7395 0.1798  0.1430  0.0408  174 LYS   F CD  
10616 C  CE  . LYS   F  178 ? 2.2128 1.0972 1.7619 0.1633  0.0953  0.0954  174 LYS   F CE  
10617 N  NZ  . LYS   F  178 ? 2.2407 1.0774 1.7957 0.1468  0.1113  0.1640  174 LYS   F NZ  
10618 N  N   . LEU   F  179 ? 2.2301 0.9468 1.4042 0.0198  0.0519  -0.0822 175 LEU   F N   
10619 C  CA  . LEU   F  179 ? 2.2179 0.9457 1.3907 0.0831  0.0433  -0.0507 175 LEU   F CA  
10620 C  C   . LEU   F  179 ? 2.1972 0.8726 1.3479 0.0535  0.0449  -0.0875 175 LEU   F C   
10621 O  O   . LEU   F  179 ? 2.2424 0.9201 1.1698 0.0761  0.0654  -0.1866 175 LEU   F O   
10622 C  CB  . LEU   F  179 ? 2.2060 0.9176 1.3622 0.1261  0.0354  -0.0261 175 LEU   F CB  
10623 C  CG  . LEU   F  179 ? 2.2076 0.9439 1.4024 0.1441  0.0595  -0.0157 175 LEU   F CG  
10624 C  CD1 . LEU   F  179 ? 2.2195 0.9039 1.3998 0.1508  0.0647  -0.0073 175 LEU   F CD1 
10625 C  CD2 . LEU   F  179 ? 2.2202 0.9343 1.4348 0.1419  0.0867  -0.0190 175 LEU   F CD2 
10626 N  N   . VAL   F  180 ? 2.1963 0.8269 1.3348 0.0077  0.0086  -0.0457 176 VAL   F N   
10627 C  CA  . VAL   F  180 ? 2.2055 0.8852 1.3346 0.0053  -0.0123 -0.0017 176 VAL   F CA  
10628 C  C   . VAL   F  180 ? 2.2642 1.0506 1.3774 -0.0178 -0.0486 -0.0474 176 VAL   F C   
10629 O  O   . VAL   F  180 ? 2.2069 1.0827 1.3919 -0.0165 -0.0853 -0.0727 176 VAL   F O   
10630 C  CB  . VAL   F  180 ? 2.2518 0.8967 1.2570 0.0257  -0.0326 0.0239  176 VAL   F CB  
10631 C  CG1 . VAL   F  180 ? 2.2800 0.8545 1.1847 0.0412  -0.0552 0.0507  176 VAL   F CG1 
10632 C  CG2 . VAL   F  180 ? 2.2062 0.9371 1.2391 0.0241  -0.0420 0.0519  176 VAL   F CG2 
10633 N  N   . ASP   F  181 ? 2.3267 1.0751 1.4792 0.0709  -0.0619 -0.0283 177 ASP   F N   
10634 C  CA  . ASP   F  181 ? 2.3796 1.2149 1.4780 0.0819  -0.1079 -0.0409 177 ASP   F CA  
10635 C  C   . ASP   F  181 ? 2.3913 1.2735 1.4181 0.1246  -0.0706 -0.0951 177 ASP   F C   
10636 O  O   . ASP   F  181 ? 2.3894 1.4665 1.4226 0.2100  -0.1323 -0.2132 177 ASP   F O   
10637 C  CB  . ASP   F  181 ? 2.4484 1.2083 1.5848 0.0130  -0.1734 -0.0456 177 ASP   F CB  
10638 C  CG  . ASP   F  181 ? 2.4496 1.2829 1.7118 -0.0942 -0.2106 -0.0322 177 ASP   F CG  
10639 O  OD1 . ASP   F  181 ? 2.3886 1.1334 1.7754 -0.1221 -0.4024 0.0421  177 ASP   F OD1 
10640 O  OD2 . ASP   F  181 ? 2.6189 1.2638 1.9289 -0.0577 -0.2357 -0.0301 177 ASP   F OD2 
10641 N  N   . HIS   F  182 ? 2.3807 1.2847 1.4426 0.1285  -0.0266 -0.1048 178 HIS   F N   
10642 C  CA  . HIS   F  182 ? 2.4798 1.2521 1.4328 0.1263  0.0208  -0.1196 178 HIS   F CA  
10643 C  C   . HIS   F  182 ? 2.4296 1.2604 1.2093 0.0534  0.0817  -0.0127 178 HIS   F C   
10644 O  O   . HIS   F  182 ? 2.5692 0.9860 1.2365 -0.0082 0.0491  0.0316  178 HIS   F O   
10645 C  CB  . HIS   F  182 ? 2.4729 1.3950 1.5502 0.1838  0.0729  -0.1639 178 HIS   F CB  
10646 C  CG  . HIS   F  182 ? 2.5656 1.4046 1.6790 0.1194  0.1122  -0.2497 178 HIS   F CG  
10647 N  ND1 . HIS   F  182 ? 2.5716 1.4178 1.8224 0.1433  0.0915  -0.2500 178 HIS   F ND1 
10648 C  CD2 . HIS   F  182 ? 2.5854 1.4244 1.6532 0.1126  0.1193  -0.2658 178 HIS   F CD2 
10649 C  CE1 . HIS   F  182 ? 2.6063 1.4367 1.8222 0.1036  0.1074  -0.2968 178 HIS   F CE1 
10650 N  NE2 . HIS   F  182 ? 2.6354 1.3488 1.7484 0.0715  0.1329  -0.3337 178 HIS   F NE2 
10651 N  N   . HIS   F  183 ? 2.4040 1.0979 1.3431 0.1231  0.0045  -0.0324 179 HIS   F N   
10652 C  CA  . HIS   F  183 ? 2.4025 1.1000 1.3502 0.1468  0.0041  -0.0158 179 HIS   F CA  
10653 C  C   . HIS   F  183 ? 2.3829 1.1386 1.3849 0.1517  -0.0700 -0.1119 179 HIS   F C   
10654 O  O   . HIS   F  183 ? 2.3803 1.2598 1.3794 0.1710  -0.0946 -0.1530 179 HIS   F O   
10655 C  CB  . HIS   F  183 ? 2.4261 1.0339 1.2824 0.1510  0.0176  0.0262  179 HIS   F CB  
10656 C  CG  . HIS   F  183 ? 2.4732 0.9615 1.2637 0.1795  0.0712  0.0959  179 HIS   F CG  
10657 N  ND1 . HIS   F  183 ? 2.5525 0.9841 1.1638 0.2116  0.0787  0.1105  179 HIS   F ND1 
10658 C  CD2 . HIS   F  183 ? 2.5001 0.9412 1.3084 0.1963  0.0752  0.0886  179 HIS   F CD2 
10659 C  CE1 . HIS   F  183 ? 2.5598 0.9620 1.1457 0.2318  0.1115  0.1046  179 HIS   F CE1 
10660 N  NE2 . HIS   F  183 ? 2.5085 0.9114 1.2541 0.2716  0.0814  0.1336  179 HIS   F NE2 
10661 N  N   . PRO   F  184 ? 2.3524 1.1620 1.4883 0.1701  -0.1086 -0.1360 180 PRO   F N   
10662 C  CA  . PRO   F  184 ? 2.3473 1.1205 1.4603 0.1798  -0.1220 -0.1203 180 PRO   F CA  
10663 C  C   . PRO   F  184 ? 2.2538 1.1150 1.3864 0.1842  -0.1026 -0.0971 180 PRO   F C   
10664 O  O   . PRO   F  184 ? 2.2081 0.8406 1.3028 0.2238  -0.1805 0.0141  180 PRO   F O   
10665 C  CB  . PRO   F  184 ? 2.3470 1.1953 1.4816 0.1834  -0.1415 -0.1256 180 PRO   F CB  
10666 C  CG  . PRO   F  184 ? 2.3950 1.2030 1.5002 0.1904  -0.1019 -0.1078 180 PRO   F CG  
10667 C  CD  . PRO   F  184 ? 2.3700 1.1818 1.4843 0.1700  -0.0883 -0.1320 180 PRO   F CD  
10668 N  N   . GLU   F  185 ? 2.2654 1.1815 1.4554 0.1691  -0.0562 -0.1060 181 GLU   F N   
10669 C  CA  . GLU   F  185 ? 2.2543 1.1781 1.5209 0.1752  -0.0261 -0.1544 181 GLU   F CA  
10670 C  C   . GLU   F  185 ? 2.2264 0.9918 1.5907 0.1885  -0.0211 -0.1923 181 GLU   F C   
10671 O  O   . GLU   F  185 ? 2.2855 0.7725 1.7060 0.1307  -0.0424 -0.1106 181 GLU   F O   
10672 C  CB  . GLU   F  185 ? 2.2555 1.3133 1.5557 0.1503  -0.0030 -0.1298 181 GLU   F CB  
10673 C  CG  . GLU   F  185 ? 2.2226 1.4400 1.5952 0.1611  0.0347  -0.1636 181 GLU   F CG  
10674 C  CD  . GLU   F  185 ? 2.1721 1.4878 1.6197 0.1488  0.0450  -0.1822 181 GLU   F CD  
10675 O  OE1 . GLU   F  185 ? 2.1869 1.5423 1.6388 0.2335  0.0636  -0.2212 181 GLU   F OE1 
10676 O  OE2 . GLU   F  185 ? 2.1032 1.5393 1.6115 0.0565  0.0922  -0.1515 181 GLU   F OE2 
10677 N  N   . GLY   F  186 ? 2.2208 1.0132 1.5759 0.1768  -0.0341 -0.1998 182 GLY   F N   
10678 C  CA  . GLY   F  186 ? 2.2043 0.9962 1.5569 0.1980  -0.0438 -0.1713 182 GLY   F CA  
10679 C  C   . GLY   F  186 ? 2.2120 0.9774 1.5344 0.2120  -0.0734 -0.1781 182 GLY   F C   
10680 O  O   . GLY   F  186 ? 2.2130 1.0190 1.5755 0.2257  -0.0398 -0.1796 182 GLY   F O   
10681 N  N   . LEU   F  187 ? 2.2358 0.9520 1.5728 0.2224  -0.1242 -0.1701 183 LEU   F N   
10682 C  CA  . LEU   F  187 ? 2.2594 0.9343 1.5714 0.2384  -0.1623 -0.1162 183 LEU   F CA  
10683 C  C   . LEU   F  187 ? 2.1696 0.9290 1.4820 0.2007  -0.2119 -0.0133 183 LEU   F C   
10684 O  O   . LEU   F  187 ? 2.1187 0.7768 1.3237 0.2100  -0.2591 0.1213  183 LEU   F O   
10685 C  CB  . LEU   F  187 ? 2.4174 0.7865 1.6123 0.2495  -0.1678 -0.1702 183 LEU   F CB  
10686 C  CG  . LEU   F  187 ? 2.4351 0.8598 1.7316 0.2706  -0.1594 -0.1804 183 LEU   F CG  
10687 C  CD1 . LEU   F  187 ? 2.4832 0.9586 1.7203 0.2762  -0.1124 -0.1628 183 LEU   F CD1 
10688 C  CD2 . LEU   F  187 ? 2.4761 0.8498 1.6721 0.2843  -0.1661 -0.2286 183 LEU   F CD2 
10689 N  N   . SER   F  188 ? 2.1321 1.0091 1.4960 0.2093  -0.2521 0.0230  184 SER   F N   
10690 C  CA  . SER   F  188 ? 2.0495 1.0496 1.4680 0.1873  -0.2654 0.0247  184 SER   F CA  
10691 C  C   . SER   F  188 ? 2.0745 1.0973 1.4514 0.1437  -0.2797 -0.0686 184 SER   F C   
10692 O  O   . SER   F  188 ? 1.9901 1.1387 1.3408 0.1818  -0.3281 -0.1116 184 SER   F O   
10693 C  CB  . SER   F  188 ? 1.9299 1.0600 1.4706 0.1937  -0.3199 0.0660  184 SER   F CB  
10694 O  OG  . SER   F  188 ? 1.8290 1.0445 1.5021 0.1093  -0.3207 0.1149  184 SER   F OG  
10695 N  N   . ALA   F  189 ? 2.1357 1.0110 1.5872 0.1494  -0.2142 -0.0594 185 ALA   F N   
10696 C  CA  . ALA   F  189 ? 2.2060 1.0229 1.5496 0.1426  -0.1663 -0.0340 185 ALA   F CA  
10697 C  C   . ALA   F  189 ? 2.1629 1.1648 1.6610 0.1256  0.0086  -0.1047 185 ALA   F C   
10698 O  O   . ALA   F  189 ? 2.3354 1.2538 1.5795 0.0932  0.0485  -0.0945 185 ALA   F O   
10699 C  CB  . ALA   F  189 ? 2.1599 1.0317 1.5360 0.1762  -0.1948 -0.0436 185 ALA   F CB  
10700 N  N   . ARG   F  190 ? 2.2343 1.2431 1.7136 0.0916  0.0799  -0.1068 186 ARG   F N   
10701 C  CA  . ARG   F  190 ? 2.1792 1.3248 1.7145 0.0090  0.1364  -0.0924 186 ARG   F CA  
10702 C  C   . ARG   F  190 ? 2.1772 1.3148 1.7764 0.0644  0.1783  -0.0674 186 ARG   F C   
10703 O  O   . ARG   F  190 ? 2.1690 1.2949 1.8830 0.0783  0.2217  0.0012  186 ARG   F O   
10704 C  CB  . ARG   F  190 ? 2.2252 1.4011 1.6679 -0.0532 0.1179  -0.0974 186 ARG   F CB  
10705 C  CG  . ARG   F  190 ? 2.2216 1.4399 1.5841 -0.0894 0.1096  -0.1167 186 ARG   F CG  
10706 C  CD  . ARG   F  190 ? 2.1876 1.6222 1.5825 -0.0987 0.1283  -0.0878 186 ARG   F CD  
10707 N  NE  . ARG   F  190 ? 2.0654 1.7537 1.5570 -0.1150 0.1113  -0.0918 186 ARG   F NE  
10708 C  CZ  . ARG   F  190 ? 1.9946 1.8185 1.5784 -0.0886 0.1756  -0.1226 186 ARG   F CZ  
10709 N  NH1 . ARG   F  190 ? 1.8688 1.8068 1.5945 -0.1155 0.1883  -0.1212 186 ARG   F NH1 
10710 N  NH2 . ARG   F  190 ? 1.9454 1.8541 1.5408 -0.0751 0.1759  -0.1492 186 ARG   F NH2 
10711 N  N   . GLU   F  191 ? 2.1893 1.2565 1.7601 0.0639  0.2236  -0.1410 187 GLU   F N   
10712 C  CA  . GLU   F  191 ? 2.1852 1.2515 1.8006 0.1203  0.2472  -0.1677 187 GLU   F CA  
10713 C  C   . GLU   F  191 ? 2.1513 1.0982 1.7729 0.0837  0.1809  -0.2131 187 GLU   F C   
10714 O  O   . GLU   F  191 ? 2.2337 1.0952 1.7937 0.0695  0.1397  -0.1709 187 GLU   F O   
10715 C  CB  . GLU   F  191 ? 2.1140 1.3576 1.7963 0.1689  0.2960  -0.2277 187 GLU   F CB  
10716 C  CG  . GLU   F  191 ? 2.1355 1.4761 1.8944 0.1797  0.4009  -0.2555 187 GLU   F CG  
10717 C  CD  . GLU   F  191 ? 2.0802 1.5553 1.9486 0.2185  0.5346  -0.3214 187 GLU   F CD  
10718 O  OE1 . GLU   F  191 ? 2.1189 1.6143 1.9384 0.1701  0.6208  -0.2911 187 GLU   F OE1 
10719 O  OE2 . GLU   F  191 ? 2.1379 1.5405 2.0600 0.2764  0.6836  -0.4528 187 GLU   F OE2 
10720 N  N   . ALA   F  192 ? 2.0542 0.8434 1.7088 0.0304  0.1110  -0.1745 188 ALA   F N   
10721 C  CA  . ALA   F  192 ? 1.9948 0.7652 1.7373 -0.0002 0.0676  -0.1628 188 ALA   F CA  
10722 C  C   . ALA   F  192 ? 2.0349 0.8001 1.7545 0.0418  0.0565  -0.1210 188 ALA   F C   
10723 O  O   . ALA   F  192 ? 1.9960 0.7894 1.8508 -0.0195 0.0389  -0.1031 188 ALA   F O   
10724 C  CB  . ALA   F  192 ? 1.9527 0.6755 1.7052 -0.0447 0.0325  -0.1664 188 ALA   F CB  
10725 N  N   . VAL   F  193 ? 2.0392 0.7856 1.7029 0.0495  0.0500  -0.0863 189 VAL   F N   
10726 C  CA  . VAL   F  193 ? 2.0940 0.7636 1.6505 0.0385  0.0415  -0.1184 189 VAL   F CA  
10727 C  C   . VAL   F  193 ? 2.1286 0.8474 1.7129 0.0814  0.0809  -0.1494 189 VAL   F C   
10728 O  O   . VAL   F  193 ? 2.1801 0.8948 1.7427 0.1009  -0.0122 -0.1643 189 VAL   F O   
10729 C  CB  . VAL   F  193 ? 2.1339 0.6244 1.5907 0.1285  0.0585  -0.1538 189 VAL   F CB  
10730 C  CG1 . VAL   F  193 ? 2.1134 0.5250 1.5825 0.1226  0.0736  -0.1812 189 VAL   F CG1 
10731 C  CG2 . VAL   F  193 ? 2.0958 0.6056 1.5877 0.1294  0.0384  -0.1307 189 VAL   F CG2 
10732 N  N   . LYS   F  194 ? 2.1387 0.9270 1.7213 0.0636  0.1285  -0.0944 190 LYS   F N   
10733 C  CA  . LYS   F  194 ? 2.1575 0.9667 1.7455 0.0854  0.1725  -0.0865 190 LYS   F CA  
10734 C  C   . LYS   F  194 ? 2.1325 0.9566 1.7790 0.0924  0.1709  -0.1118 190 LYS   F C   
10735 O  O   . LYS   F  194 ? 2.1879 0.9175 1.9622 0.0908  0.1942  -0.0660 190 LYS   F O   
10736 C  CB  . LYS   F  194 ? 2.1881 1.0868 1.7512 0.1073  0.1828  -0.0585 190 LYS   F CB  
10737 C  CG  . LYS   F  194 ? 2.1924 1.1475 1.6723 0.0848  0.2013  -0.0187 190 LYS   F CG  
10738 C  CD  . LYS   F  194 ? 2.2076 1.2600 1.6682 0.0887  0.2402  0.0003  190 LYS   F CD  
10739 C  CE  . LYS   F  194 ? 2.2256 1.3430 1.6743 0.1088  0.2581  0.0076  190 LYS   F CE  
10740 N  NZ  . LYS   F  194 ? 2.2396 1.4321 1.6560 0.1206  0.2538  0.0097  190 LYS   F NZ  
10741 N  N   . GLN   F  195 ? 2.1476 0.8611 1.6522 0.0841  0.1471  -0.1347 191 GLN   F N   
10742 C  CA  . GLN   F  195 ? 2.1018 0.8959 1.6052 0.0696  0.1101  -0.1526 191 GLN   F CA  
10743 C  C   . GLN   F  195 ? 2.0903 0.9772 1.5846 0.0271  0.1694  -0.1941 191 GLN   F C   
10744 O  O   . GLN   F  195 ? 2.1272 0.9994 1.5542 -0.0654 0.1694  -0.1365 191 GLN   F O   
10745 C  CB  . GLN   F  195 ? 2.1109 0.8835 1.6022 0.1021  0.1062  -0.1508 191 GLN   F CB  
10746 C  CG  . GLN   F  195 ? 2.1238 0.9583 1.6052 0.1126  0.1419  -0.1692 191 GLN   F CG  
10747 C  CD  . GLN   F  195 ? 2.1505 0.9821 1.5493 0.0623  0.1836  -0.2089 191 GLN   F CD  
10748 O  OE1 . GLN   F  195 ? 2.1678 1.0477 1.5908 0.0968  0.2510  -0.3161 191 GLN   F OE1 
10749 N  NE2 . GLN   F  195 ? 2.2010 0.9799 1.5164 0.0104  0.1346  -0.2583 191 GLN   F NE2 
10750 N  N   . ALA   F  196 ? 2.0119 0.9047 1.5198 0.0439  0.1972  -0.1110 192 ALA   F N   
10751 C  CA  . ALA   F  196 ? 1.9533 0.8620 1.5122 0.0429  0.1308  -0.0845 192 ALA   F CA  
10752 C  C   . ALA   F  196 ? 1.9709 0.8834 1.4977 0.0431  0.1055  -0.0621 192 ALA   F C   
10753 O  O   . ALA   F  196 ? 1.9428 0.8774 1.5121 0.0618  0.0801  -0.0572 192 ALA   F O   
10754 C  CB  . ALA   F  196 ? 1.9181 0.8683 1.4110 -0.0051 0.1217  -0.0819 192 ALA   F CB  
10755 N  N   . ALA   F  197 ? 1.9786 0.8104 1.4993 0.0327  0.0717  -0.0160 193 ALA   F N   
10756 C  CA  . ALA   F  197 ? 2.0168 0.8173 1.5400 0.0498  0.0393  -0.0129 193 ALA   F CA  
10757 C  C   . ALA   F  197 ? 2.0680 0.8456 1.6091 0.0358  0.0592  -0.0580 193 ALA   F C   
10758 O  O   . ALA   F  197 ? 2.1084 0.7932 1.5844 0.0394  0.0461  -0.1021 193 ALA   F O   
10759 C  CB  . ALA   F  197 ? 2.0634 0.7253 1.5420 0.0400  0.0287  -0.0231 193 ALA   F CB  
10760 N  N   . LYS   F  198 ? 2.0647 0.8727 1.6490 0.0132  0.0258  -0.0618 194 LYS   F N   
10761 C  CA  . LYS   F  198 ? 2.1129 0.8633 1.7778 -0.0116 0.0478  -0.0783 194 LYS   F CA  
10762 C  C   . LYS   F  198 ? 2.0441 0.8275 1.7977 0.0434  0.0594  -0.0696 194 LYS   F C   
10763 O  O   . LYS   F  198 ? 2.1263 0.8118 1.8743 -0.0531 0.0313  0.0985  194 LYS   F O   
10764 C  CB  . LYS   F  198 ? 2.1489 0.9712 1.7872 -0.0233 0.0282  -0.1013 194 LYS   F CB  
10765 C  CG  . LYS   F  198 ? 2.1813 1.0264 1.8397 -0.0776 0.0095  -0.1543 194 LYS   F CG  
10766 C  CD  . LYS   F  198 ? 2.1579 1.0511 1.8477 -0.0952 -0.0002 -0.1342 194 LYS   F CD  
10767 C  CE  . LYS   F  198 ? 2.1530 0.9950 1.8612 -0.0934 -0.0032 -0.1403 194 LYS   F CE  
10768 N  NZ  . LYS   F  198 ? 2.1664 0.9618 1.9011 -0.0879 -0.0284 -0.1783 194 LYS   F NZ  
10769 N  N   . ILE   F  199 ? 2.0376 0.6844 1.7686 0.0222  0.0533  -0.1255 195 ILE   F N   
10770 C  CA  . ILE   F  199 ? 1.9967 0.5789 1.7865 0.0318  0.0316  -0.1775 195 ILE   F CA  
10771 C  C   . ILE   F  199 ? 1.9317 0.6001 1.7843 0.0497  0.0108  -0.2381 195 ILE   F C   
10772 O  O   . ILE   F  199 ? 1.8920 0.6647 1.9064 -0.0181 0.0113  -0.1775 195 ILE   F O   
10773 C  CB  . ILE   F  199 ? 2.0158 0.5449 1.7170 0.0388  0.0154  -0.1539 195 ILE   F CB  
10774 C  CG1 . ILE   F  199 ? 2.0882 0.6351 1.7107 0.0580  0.0273  -0.1249 195 ILE   F CG1 
10775 C  CG2 . ILE   F  199 ? 2.0267 0.4722 1.6869 0.0337  0.0038  -0.1765 195 ILE   F CG2 
10776 C  CD1 . ILE   F  199 ? 2.0645 0.7537 1.6973 0.1072  0.0261  -0.1023 195 ILE   F CD1 
10777 N  N   . ILE   F  200 ? 1.8911 0.6293 1.7413 0.0710  0.0008  -0.2377 196 ILE   F N   
10778 C  CA  . ILE   F  200 ? 1.8911 0.6335 1.7396 0.0778  -0.0031 -0.2412 196 ILE   F CA  
10779 C  C   . ILE   F  200 ? 1.9447 0.6971 1.7736 0.1348  -0.0469 -0.2567 196 ILE   F C   
10780 O  O   . ILE   F  200 ? 2.0547 0.7389 1.7022 0.1342  -0.0690 -0.2781 196 ILE   F O   
10781 C  CB  . ILE   F  200 ? 1.8268 0.6003 1.7710 0.0600  0.0419  -0.2169 196 ILE   F CB  
10782 C  CG1 . ILE   F  200 ? 1.8125 0.5544 1.7593 0.0354  0.0315  -0.2353 196 ILE   F CG1 
10783 C  CG2 . ILE   F  200 ? 1.8012 0.5452 1.8017 0.0472  0.0352  -0.1988 196 ILE   F CG2 
10784 C  CD1 . ILE   F  200 ? 1.7956 0.4979 1.7620 0.0521  0.0348  -0.2525 196 ILE   F CD1 
10785 N  N   . TYR   F  201 ? 1.9659 0.7984 1.7641 0.1252  -0.0588 -0.1574 197 TYR   F N   
10786 C  CA  . TYR   F  201 ? 1.9738 0.8707 1.8797 0.1900  -0.1042 -0.0854 197 TYR   F CA  
10787 C  C   . TYR   F  201 ? 2.0040 0.8395 1.9131 0.2198  -0.0917 -0.0961 197 TYR   F C   
10788 O  O   . TYR   F  201 ? 2.1219 0.7763 2.0366 0.2393  -0.1341 -0.1456 197 TYR   F O   
10789 C  CB  . TYR   F  201 ? 1.9643 0.9680 1.9289 0.1680  -0.1252 -0.0150 197 TYR   F CB  
10790 C  CG  . TYR   F  201 ? 1.9296 0.9933 1.9733 0.1776  -0.1565 0.0346  197 TYR   F CG  
10791 C  CD1 . TYR   F  201 ? 1.9014 0.9788 1.9494 0.1467  -0.1672 0.0647  197 TYR   F CD1 
10792 C  CD2 . TYR   F  201 ? 1.8933 1.0674 2.0570 0.1591  -0.1544 0.0739  197 TYR   F CD2 
10793 C  CE1 . TYR   F  201 ? 1.8409 1.0041 1.9822 0.1486  -0.1607 0.1244  197 TYR   F CE1 
10794 C  CE2 . TYR   F  201 ? 1.8558 1.0513 2.1079 0.1603  -0.1326 0.0920  197 TYR   F CE2 
10795 C  CZ  . TYR   F  201 ? 1.8055 1.0367 2.0704 0.1369  -0.1466 0.1241  197 TYR   F CZ  
10796 O  OH  . TYR   F  201 ? 1.6958 1.1379 2.1640 0.1008  -0.1241 0.2539  197 TYR   F OH  
10797 N  N   . LEU   F  202 ? 1.9409 0.7679 1.9172 0.1792  -0.0492 -0.1086 198 LEU   F N   
10798 C  CA  . LEU   F  202 ? 1.9823 0.7152 1.9637 0.1460  0.0030  -0.0484 198 LEU   F CA  
10799 C  C   . LEU   F  202 ? 1.9774 0.8017 2.0091 0.1581  0.0219  -0.0097 198 LEU   F C   
10800 O  O   . LEU   F  202 ? 2.0550 0.8353 2.1494 0.1456  0.0091  0.1113  198 LEU   F O   
10801 C  CB  . LEU   F  202 ? 1.9781 0.7004 1.8680 0.0630  0.0207  -0.1213 198 LEU   F CB  
10802 C  CG  . LEU   F  202 ? 2.0596 0.7934 1.8315 0.0184  0.0002  -0.1419 198 LEU   F CG  
10803 C  CD1 . LEU   F  202 ? 2.0734 0.8630 1.8074 0.0118  0.0199  -0.1556 198 LEU   F CD1 
10804 C  CD2 . LEU   F  202 ? 2.0310 0.8194 1.8161 -0.0099 0.0155  -0.1264 198 LEU   F CD2 
10805 N  N   . ALA   F  203 ? 2.0170 0.6256 2.0667 0.2182  -0.0044 0.0630  199 ALA   F N   
10806 C  CA  . ALA   F  203 ? 2.0455 0.6569 2.0860 0.2481  0.0026  0.1023  199 ALA   F CA  
10807 C  C   . ALA   F  203 ? 2.0235 0.6252 2.1733 0.2314  -0.0394 0.1117  199 ALA   F C   
10808 O  O   . ALA   F  203 ? 2.0728 0.3845 2.2436 0.3181  -0.0562 0.1649  199 ALA   F O   
10809 C  CB  . ALA   F  203 ? 2.0033 0.7515 2.0514 0.2898  0.0185  0.1316  199 ALA   F CB  
10810 N  N   . HIS   F  204 ? 2.0695 0.6992 2.1308 0.1186  0.0135  0.1247  200 HIS   F N   
10811 C  CA  . HIS   F  204 ? 2.0446 0.9355 2.0774 0.0671  0.0250  0.1270  200 HIS   F CA  
10812 C  C   . HIS   F  204 ? 2.0663 0.9548 2.1555 0.0569  0.0793  0.0495  200 HIS   F C   
10813 O  O   . HIS   F  204 ? 2.0146 1.2290 2.2163 -0.0098 0.0069  0.1048  200 HIS   F O   
10814 C  CB  . HIS   F  204 ? 2.0427 0.8937 2.0028 0.0946  0.0500  0.1418  200 HIS   F CB  
10815 C  CG  . HIS   F  204 ? 2.0593 0.9154 1.9930 0.1067  0.0376  0.1088  200 HIS   F CG  
10816 N  ND1 . HIS   F  204 ? 2.0361 0.9347 2.0022 0.1056  0.0401  0.0812  200 HIS   F ND1 
10817 C  CD2 . HIS   F  204 ? 2.0681 0.9663 2.0256 0.1204  0.0504  0.0746  200 HIS   F CD2 
10818 C  CE1 . HIS   F  204 ? 2.0480 0.9710 2.0281 0.1148  0.0212  0.0632  200 HIS   F CE1 
10819 N  NE2 . HIS   F  204 ? 2.0710 1.0190 2.0372 0.1093  0.0406  0.0538  200 HIS   F NE2 
10820 N  N   . GLU   F  205 ? 2.1233 1.2113 2.1127 0.0649  0.1425  -0.0424 201 GLU   F N   
10821 C  CA  . GLU   F  205 ? 2.2007 1.2561 2.2031 0.1012  0.1925  -0.1742 201 GLU   F CA  
10822 C  C   . GLU   F  205 ? 2.3336 1.2239 2.1997 -0.0601 0.1790  -0.2515 201 GLU   F C   
10823 O  O   . GLU   F  205 ? 2.1232 1.1805 2.2266 0.0105  0.3111  -0.4135 201 GLU   F O   
10824 C  CB  . GLU   F  205 ? 2.1969 1.3181 2.1430 0.1401  0.2008  -0.1071 201 GLU   F CB  
10825 C  CG  . GLU   F  205 ? 2.2311 1.3700 2.1631 0.1666  0.2123  -0.0473 201 GLU   F CG  
10826 C  CD  . GLU   F  205 ? 2.2438 1.3958 2.2203 0.1901  0.2102  0.0295  201 GLU   F CD  
10827 O  OE1 . GLU   F  205 ? 2.3302 1.3912 2.2821 0.1439  0.1264  0.0318  201 GLU   F OE1 
10828 O  OE2 . GLU   F  205 ? 2.3094 1.4505 2.2963 0.2910  0.3107  0.0691  201 GLU   F OE2 
10829 N  N   . ASP   F  206 ? 2.3533 1.3311 2.2320 -0.1435 0.1756  -0.4168 202 ASP   F N   
10830 C  CA  . ASP   F  206 ? 2.5745 1.4459 2.2457 -0.3261 0.1357  -0.3733 202 ASP   F CA  
10831 C  C   . ASP   F  206 ? 2.6525 1.6437 2.2432 -0.2682 0.0713  -0.3019 202 ASP   F C   
10832 O  O   . ASP   F  206 ? 2.6917 1.8215 2.4072 -0.2186 0.1479  -0.1252 202 ASP   F O   
10833 C  CB  . ASP   F  206 ? 2.5474 1.3953 2.2095 -0.3997 0.0889  -0.4654 202 ASP   F CB  
10834 C  CG  . ASP   F  206 ? 2.5898 1.4199 2.2482 -0.4960 0.0342  -0.4033 202 ASP   F CG  
10835 O  OD1 . ASP   F  206 ? 2.6884 1.6421 2.2153 -0.3997 0.1276  -0.3509 202 ASP   F OD1 
10836 O  OD2 . ASP   F  206 ? 2.5101 0.8815 2.0766 -0.6186 0.1081  -0.5955 202 ASP   F OD2 
10837 N  N   . ASN   F  207 ? 2.6449 1.6633 2.2669 -0.2615 0.0838  -0.2975 203 ASN   F N   
10838 C  CA  . ASN   F  207 ? 2.6346 1.4694 2.2702 -0.1889 0.1413  -0.3913 203 ASN   F CA  
10839 C  C   . ASN   F  207 ? 2.5886 1.3941 2.1795 -0.0602 0.0502  -0.4047 203 ASN   F C   
10840 O  O   . ASN   F  207 ? 2.4921 1.4172 2.0232 0.0188  0.1108  -0.4803 203 ASN   F O   
10841 C  CB  . ASN   F  207 ? 2.8407 1.3701 2.2034 -0.3222 0.1659  -0.4712 203 ASN   F CB  
10842 C  CG  . ASN   F  207 ? 2.8969 1.3193 2.2503 -0.3595 0.2659  -0.3747 203 ASN   F CG  
10843 O  OD1 . ASN   F  207 ? 2.9866 0.8238 2.3166 -0.4200 0.3285  -0.2286 203 ASN   F OD1 
10844 N  ND2 . ASN   F  207 ? 2.9416 1.4106 2.2919 -0.3561 0.2902  -0.2770 203 ASN   F ND2 
10845 N  N   . LYS   F  208 ? 2.4475 1.4026 2.2541 0.0854  0.0616  -0.2737 204 LYS   F N   
10846 C  CA  . LYS   F  208 ? 2.4212 1.3295 2.1770 0.1571  0.0499  -0.3089 204 LYS   F CA  
10847 C  C   . LYS   F  208 ? 2.1111 1.3110 2.3371 0.1119  0.1500  -0.3150 204 LYS   F C   
10848 O  O   . LYS   F  208 ? 2.1194 1.1581 2.2693 0.0400  0.1708  -0.3219 204 LYS   F O   
10849 C  CB  . LYS   F  208 ? 2.4854 1.4086 2.1085 0.2500  0.0546  -0.2845 204 LYS   F CB  
10850 C  CG  . LYS   F  208 ? 2.5637 1.4144 2.0381 0.2836  -0.0122 -0.2953 204 LYS   F CG  
10851 C  CD  . LYS   F  208 ? 2.5959 1.4388 1.9859 0.2975  0.0042  -0.2848 204 LYS   F CD  
10852 C  CE  . LYS   F  208 ? 2.6295 1.3478 1.9571 0.3412  0.0211  -0.3218 204 LYS   F CE  
10853 N  NZ  . LYS   F  208 ? 2.6566 1.2299 2.0136 0.3190  0.0867  -0.3313 204 LYS   F NZ  
10854 N  N   . GLU   F  209 ? 2.1268 1.4190 2.3707 0.0741  0.1268  -0.2608 205 GLU   F N   
10855 C  CA  . GLU   F  209 ? 2.0269 1.4913 2.4542 0.0464  0.1420  -0.2165 205 GLU   F CA  
10856 C  C   . GLU   F  209 ? 1.9804 1.4132 2.4456 0.0869  0.1511  -0.1536 205 GLU   F C   
10857 O  O   . GLU   F  209 ? 1.9880 1.2685 2.4868 0.0458  0.1868  -0.0869 205 GLU   F O   
10858 C  CB  . GLU   F  209 ? 1.9906 1.7139 2.4694 0.0352  0.1754  -0.2002 205 GLU   F CB  
10859 C  CG  . GLU   F  209 ? 1.9415 1.7881 2.5401 -0.0324 0.2415  -0.1878 205 GLU   F CG  
10860 C  CD  . GLU   F  209 ? 1.9312 1.9857 2.5804 -0.1510 0.2932  -0.1657 205 GLU   F CD  
10861 O  OE1 . GLU   F  209 ? 2.0222 1.9716 2.6209 -0.1728 0.2819  -0.1515 205 GLU   F OE1 
10862 O  OE2 . GLU   F  209 ? 1.9086 2.0676 2.5880 -0.2224 0.3068  -0.0492 205 GLU   F OE2 
10863 N  N   . LYS   F  210 ? 2.0661 1.3491 2.3821 0.0981  0.0489  -0.1527 206 LYS   F N   
10864 C  CA  . LYS   F  210 ? 2.1151 1.3009 2.3003 0.1680  -0.0063 -0.1859 206 LYS   F CA  
10865 C  C   . LYS   F  210 ? 2.0612 1.2051 2.2843 0.1818  -0.0189 -0.2262 206 LYS   F C   
10866 O  O   . LYS   F  210 ? 2.1018 1.1871 2.2790 0.2116  -0.0535 -0.2119 206 LYS   F O   
10867 C  CB  . LYS   F  210 ? 2.1594 1.3451 2.2205 0.2309  -0.0211 -0.1249 206 LYS   F CB  
10868 C  CG  . LYS   F  210 ? 2.2138 1.3251 2.2445 0.2565  0.0041  -0.0958 206 LYS   F CG  
10869 C  CD  . LYS   F  210 ? 2.2311 1.3160 2.2143 0.2964  -0.0155 -0.0540 206 LYS   F CD  
10870 C  CE  . LYS   F  210 ? 2.2823 1.3006 2.2783 0.3239  -0.0168 -0.0648 206 LYS   F CE  
10871 N  NZ  . LYS   F  210 ? 2.2602 1.2611 2.3162 0.3254  -0.0017 -0.0996 206 LYS   F NZ  
10872 N  N   . ASP   F  211 ? 2.0606 1.1266 2.2719 0.1652  -0.0358 -0.2940 207 ASP   F N   
10873 C  CA  . ASP   F  211 ? 2.0474 1.1486 2.2183 0.1035  0.0051  -0.3171 207 ASP   F CA  
10874 C  C   . ASP   F  211 ? 2.0709 1.0452 2.1524 0.0950  -0.0783 -0.2482 207 ASP   F C   
10875 O  O   . ASP   F  211 ? 2.0334 1.0164 2.1419 0.0411  -0.1458 -0.2821 207 ASP   F O   
10876 C  CB  . ASP   F  211 ? 2.0926 1.2612 2.2733 0.1020  0.0851  -0.3772 207 ASP   F CB  
10877 C  CG  . ASP   F  211 ? 1.9498 1.3392 2.3748 0.0423  0.1566  -0.3661 207 ASP   F CG  
10878 O  OD1 . ASP   F  211 ? 2.1166 1.3993 2.3969 0.1086  0.2064  -0.3488 207 ASP   F OD1 
10879 O  OD2 . ASP   F  211 ? 1.9527 1.4836 2.4345 0.0446  0.2727  -0.4188 207 ASP   F OD2 
10880 N  N   . PHE   F  212 ? 2.0884 0.9899 2.1163 0.1255  -0.0134 -0.2676 208 PHE   F N   
10881 C  CA  . PHE   F  212 ? 2.1116 0.9968 1.9523 0.1450  0.0000  -0.2443 208 PHE   F CA  
10882 C  C   . PHE   F  212 ? 2.0258 0.9594 1.8635 0.2319  0.0790  -0.2611 208 PHE   F C   
10883 O  O   . PHE   F  212 ? 2.0966 0.9867 1.8871 0.2888  0.1504  -0.2846 208 PHE   F O   
10884 C  CB  . PHE   F  212 ? 2.1349 0.9287 1.9104 0.1527  -0.0201 -0.2343 208 PHE   F CB  
10885 C  CG  . PHE   F  212 ? 2.2441 0.8911 1.9070 0.1419  0.0162  -0.2167 208 PHE   F CG  
10886 C  CD1 . PHE   F  212 ? 2.2858 0.8860 1.8526 0.1238  0.0200  -0.2121 208 PHE   F CD1 
10887 C  CD2 . PHE   F  212 ? 2.3297 0.8660 1.8662 0.1060  0.0301  -0.1705 208 PHE   F CD2 
10888 C  CE1 . PHE   F  212 ? 2.3114 0.8511 1.8257 0.1278  0.0669  -0.2662 208 PHE   F CE1 
10889 C  CE2 . PHE   F  212 ? 2.3526 0.8322 1.8382 0.0806  0.0696  -0.2329 208 PHE   F CE2 
10890 C  CZ  . PHE   F  212 ? 2.3505 0.8088 1.8311 0.0782  0.0532  -0.2400 208 PHE   F CZ  
10891 N  N   . GLU   F  213 ? 1.9996 0.9232 1.8383 0.2331  0.0460  -0.2136 209 GLU   F N   
10892 C  CA  . GLU   F  213 ? 1.9593 0.9419 1.8803 0.2232  0.0743  -0.1887 209 GLU   F CA  
10893 C  C   . GLU   F  213 ? 1.9266 0.7954 1.8196 0.2139  0.1156  -0.2367 209 GLU   F C   
10894 O  O   . GLU   F  213 ? 1.8995 0.7258 1.8481 0.2838  0.1283  -0.3415 209 GLU   F O   
10895 C  CB  . GLU   F  213 ? 1.9942 0.9580 1.8672 0.2572  0.0585  -0.1903 209 GLU   F CB  
10896 C  CG  . GLU   F  213 ? 2.0428 0.9749 1.9392 0.2520  0.0502  -0.1677 209 GLU   F CG  
10897 C  CD  . GLU   F  213 ? 2.0774 1.2022 1.9202 0.2245  -0.0538 -0.1217 209 GLU   F CD  
10898 O  OE1 . GLU   F  213 ? 2.1671 1.1928 1.9241 0.2305  -0.0361 -0.0182 209 GLU   F OE1 
10899 O  OE2 . GLU   F  213 ? 2.0792 1.2424 2.0565 0.2984  -0.0670 -0.0970 209 GLU   F OE2 
10900 N  N   . LEU   F  214 ? 1.8783 0.6953 1.8229 0.1848  0.1191  -0.2465 210 LEU   F N   
10901 C  CA  . LEU   F  214 ? 1.8752 0.7139 1.7393 0.1453  0.1351  -0.2038 210 LEU   F CA  
10902 C  C   . LEU   F  214 ? 1.8469 0.7112 1.6829 0.1437  0.1073  -0.1853 210 LEU   F C   
10903 O  O   . LEU   F  214 ? 1.8813 0.7848 1.6989 0.0992  0.0481  -0.1285 210 LEU   F O   
10904 C  CB  . LEU   F  214 ? 1.9061 0.6613 1.7690 0.1409  0.1981  -0.2547 210 LEU   F CB  
10905 C  CG  . LEU   F  214 ? 1.8732 0.6583 1.8033 0.1535  0.2122  -0.2706 210 LEU   F CG  
10906 C  CD1 . LEU   F  214 ? 1.8984 0.6221 1.7945 0.1365  0.2323  -0.2959 210 LEU   F CD1 
10907 C  CD2 . LEU   F  214 ? 1.9209 0.6934 1.8229 0.1440  0.2355  -0.2430 210 LEU   F CD2 
10908 N  N   . GLU   F  215 ? 1.8236 0.8178 1.6324 0.1188  0.1109  -0.1916 211 GLU   F N   
10909 C  CA  . GLU   F  215 ? 1.7800 0.8584 1.6276 0.1198  0.1363  -0.2471 211 GLU   F CA  
10910 C  C   . GLU   F  215 ? 1.7786 0.7423 1.6094 0.1153  0.1363  -0.2731 211 GLU   F C   
10911 O  O   . GLU   F  215 ? 1.8044 0.7591 1.6172 0.0864  0.1431  -0.3314 211 GLU   F O   
10912 C  CB  . GLU   F  215 ? 1.7668 0.9917 1.6264 0.1046  0.1418  -0.1986 211 GLU   F CB  
10913 C  CG  . GLU   F  215 ? 1.7407 1.0612 1.6883 0.1408  0.1480  -0.2659 211 GLU   F CG  
10914 C  CD  . GLU   F  215 ? 1.7332 1.1515 1.6991 0.1522  0.1637  -0.2752 211 GLU   F CD  
10915 O  OE1 . GLU   F  215 ? 1.7516 1.2123 1.7266 0.1438  0.1808  -0.3534 211 GLU   F OE1 
10916 O  OE2 . GLU   F  215 ? 1.7337 1.1629 1.7205 0.2156  0.1919  -0.2357 211 GLU   F OE2 
10917 N  N   . ILE   F  216 ? 1.7538 0.7850 1.5675 0.1970  0.0905  -0.2297 212 ILE   F N   
10918 C  CA  . ILE   F  216 ? 1.8022 0.8232 1.4840 0.1657  0.0905  -0.1844 212 ILE   F CA  
10919 C  C   . ILE   F  216 ? 1.8168 0.8100 1.4882 0.1467  0.0427  -0.1685 212 ILE   F C   
10920 O  O   . ILE   F  216 ? 1.8363 0.7882 1.5630 0.1171  0.0437  -0.1453 212 ILE   F O   
10921 C  CB  . ILE   F  216 ? 1.8085 0.7145 1.4942 0.2049  0.1113  -0.1936 212 ILE   F CB  
10922 C  CG1 . ILE   F  216 ? 1.8188 0.7373 1.4853 0.2498  0.1309  -0.1556 212 ILE   F CG1 
10923 C  CG2 . ILE   F  216 ? 1.8137 0.7051 1.4476 0.1873  0.1157  -0.2302 212 ILE   F CG2 
10924 C  CD1 . ILE   F  216 ? 1.8362 0.8085 1.4931 0.2734  0.1481  -0.1323 212 ILE   F CD1 
10925 N  N   . SER   F  217 ? 1.8219 0.8921 1.4724 0.1462  0.0077  -0.1751 213 SER   F N   
10926 C  CA  . SER   F  217 ? 1.8731 0.8541 1.4502 0.1029  0.0174  -0.2041 213 SER   F CA  
10927 C  C   . SER   F  217 ? 1.9110 0.8207 1.4665 0.1088  0.0016  -0.1827 213 SER   F C   
10928 O  O   . SER   F  217 ? 1.9884 0.8660 1.4744 0.1011  -0.0342 -0.2047 213 SER   F O   
10929 C  CB  . SER   F  217 ? 1.8685 0.8837 1.3909 0.0989  -0.0219 -0.1758 213 SER   F CB  
10930 O  OG  . SER   F  217 ? 1.8373 0.9110 1.2625 0.1288  -0.0106 -0.1908 213 SER   F OG  
10931 N  N   . TRP   F  218 ? 1.9077 0.7901 1.4947 0.0444  0.0045  -0.1544 214 TRP   F N   
10932 C  CA  . TRP   F  218 ? 1.9144 0.7317 1.4620 -0.0185 -0.0006 -0.1675 214 TRP   F CA  
10933 C  C   . TRP   F  218 ? 1.9243 0.6436 1.4863 -0.0811 0.0010  -0.0906 214 TRP   F C   
10934 O  O   . TRP   F  218 ? 1.8557 0.4243 1.5374 -0.0827 0.0638  0.0292  214 TRP   F O   
10935 C  CB  . TRP   F  218 ? 1.9104 0.6823 1.4685 -0.0268 0.0036  -0.1838 214 TRP   F CB  
10936 C  CG  . TRP   F  218 ? 1.9542 0.5792 1.4918 -0.0016 0.0057  -0.1136 214 TRP   F CG  
10937 C  CD1 . TRP   F  218 ? 1.9472 0.5749 1.5179 0.0230  -0.0175 -0.1059 214 TRP   F CD1 
10938 C  CD2 . TRP   F  218 ? 2.0160 0.5277 1.4758 0.0208  -0.0331 -0.0596 214 TRP   F CD2 
10939 N  NE1 . TRP   F  218 ? 1.9561 0.5673 1.5108 0.0528  -0.0194 -0.0642 214 TRP   F NE1 
10940 C  CE2 . TRP   F  218 ? 1.9802 0.5965 1.5112 0.0287  -0.0541 -0.0482 214 TRP   F CE2 
10941 C  CE3 . TRP   F  218 ? 2.0303 0.4896 1.4878 0.0058  -0.0527 -0.0457 214 TRP   F CE3 
10942 C  CZ2 . TRP   F  218 ? 1.9888 0.6887 1.5039 0.0202  -0.0451 -0.0549 214 TRP   F CZ2 
10943 C  CZ3 . TRP   F  218 ? 2.0551 0.6254 1.5147 0.0147  -0.0157 -0.0327 214 TRP   F CZ3 
10944 C  CH2 . TRP   F  218 ? 2.0279 0.7286 1.5087 0.0130  -0.0424 -0.0752 214 TRP   F CH2 
10945 N  N   . CYS   F  219 ? 1.9474 0.8193 1.4499 -0.1224 -0.0301 -0.1238 215 CYS   F N   
10946 C  CA  . CYS   F  219 ? 1.9796 0.8965 1.4651 -0.0803 -0.0409 -0.0925 215 CYS   F CA  
10947 C  C   . CYS   F  219 ? 1.9509 0.9110 1.4843 -0.0839 -0.0835 -0.1521 215 CYS   F C   
10948 O  O   . CYS   F  219 ? 1.9688 0.8047 1.5089 -0.0693 -0.0489 -0.1036 215 CYS   F O   
10949 C  CB  . CYS   F  219 ? 2.0106 1.1431 1.5777 -0.1240 0.0134  -0.1650 215 CYS   F CB  
10950 S  SG  . CYS   F  219 ? 2.2742 1.5864 1.5680 -0.1337 0.0364  -0.2158 215 CYS   F SG  
10951 N  N   . SER   F  220 ? 1.9002 0.9595 1.4526 -0.0659 -0.0965 -0.1217 216 SER   F N   
10952 C  CA  . SER   F  220 ? 1.8642 0.9702 1.4255 -0.0743 -0.0808 -0.1531 216 SER   F CA  
10953 C  C   . SER   F  220 ? 1.8554 0.9480 1.3615 -0.1306 -0.1280 -0.1735 216 SER   F C   
10954 O  O   . SER   F  220 ? 1.8931 0.8515 1.3839 -0.1384 -0.0889 -0.1601 216 SER   F O   
10955 C  CB  . SER   F  220 ? 1.8589 1.0263 1.4102 -0.0752 -0.0595 -0.1143 216 SER   F CB  
10956 O  OG  . SER   F  220 ? 1.8208 1.1102 1.3946 -0.0716 -0.0451 -0.1267 216 SER   F OG  
10957 N  N   . LEU   F  221 ? 1.8881 0.8960 1.3775 -0.1172 -0.1533 -0.1818 217 LEU   F N   
10958 C  CA  . LEU   F  221 ? 1.8849 0.8426 1.3786 -0.1720 -0.1398 -0.1869 217 LEU   F CA  
10959 C  C   . LEU   F  221 ? 1.8609 0.8759 1.3689 -0.1597 -0.1230 -0.1930 217 LEU   F C   
10960 O  O   . LEU   F  221 ? 1.9283 0.8705 1.4385 -0.0823 -0.0936 -0.1909 217 LEU   F O   
10961 C  CB  . LEU   F  221 ? 1.9142 0.8702 1.4075 -0.0882 -0.1759 -0.1295 217 LEU   F CB  
10962 C  CG  . LEU   F  221 ? 1.9195 0.9001 1.4577 -0.0784 -0.1871 -0.0903 217 LEU   F CG  
10963 C  CD1 . LEU   F  221 ? 1.8408 0.8980 1.3903 -0.1295 -0.2475 -0.0760 217 LEU   F CD1 
10964 C  CD2 . LEU   F  221 ? 1.9063 1.0182 1.4656 -0.0294 -0.1897 -0.0609 217 LEU   F CD2 
10965 N  N   . SER   F  222 ? 1.8354 0.7731 1.3577 -0.2361 -0.0922 -0.1778 218 SER   F N   
10966 C  CA  . SER   F  222 ? 1.8727 0.8528 1.4148 -0.2155 -0.0198 -0.1708 218 SER   F CA  
10967 C  C   . SER   F  222 ? 1.8838 0.9012 1.5044 -0.1263 -0.0015 -0.0863 218 SER   F C   
10968 O  O   . SER   F  222 ? 1.8596 1.0991 1.6980 -0.2234 0.0460  -0.0915 218 SER   F O   
10969 C  CB  . SER   F  222 ? 1.8561 0.9001 1.3648 -0.1987 0.0265  -0.1259 218 SER   F CB  
10970 O  OG  . SER   F  222 ? 1.8679 0.8997 1.3452 -0.1947 0.0760  -0.0327 218 SER   F OG  
10971 N  N   . GLU   F  223 ? 1.8695 0.8403 1.5979 -0.2054 0.0750  -0.0546 219 GLU   F N   
10972 C  CA  . GLU   F  223 ? 1.8575 0.9079 1.6461 -0.1927 0.1162  0.0370  219 GLU   F CA  
10973 C  C   . GLU   F  223 ? 1.8372 0.8220 1.6129 -0.1772 0.1313  0.0958  219 GLU   F C   
10974 O  O   . GLU   F  223 ? 1.8353 0.9352 1.7246 -0.2017 0.1197  0.1571  219 GLU   F O   
10975 C  CB  . GLU   F  223 ? 1.8983 0.9329 1.6585 -0.1241 0.1357  0.0641  219 GLU   F CB  
10976 C  CG  . GLU   F  223 ? 1.9083 1.1040 1.6125 -0.1100 0.1736  0.1030  219 GLU   F CG  
10977 C  CD  . GLU   F  223 ? 1.9091 1.1489 1.6424 -0.0988 0.1822  0.1432  219 GLU   F CD  
10978 O  OE1 . GLU   F  223 ? 1.9372 1.3615 1.6313 -0.0749 0.1860  0.0861  219 GLU   F OE1 
10979 O  OE2 . GLU   F  223 ? 1.8275 0.9191 1.7297 -0.1006 0.2263  0.1754  219 GLU   F OE2 
10980 N  N   . THR   F  224 ? 1.8494 0.7996 1.5617 -0.1074 0.1178  0.0893  220 THR   F N   
10981 C  CA  . THR   F  224 ? 1.8775 0.8290 1.5956 -0.0678 0.0821  0.0358  220 THR   F CA  
10982 C  C   . THR   F  224 ? 1.8721 0.8362 1.5333 -0.0730 0.0468  0.0188  220 THR   F C   
10983 O  O   . THR   F  224 ? 1.9107 0.8440 1.5035 -0.1478 -0.0385 0.0667  220 THR   F O   
10984 C  CB  . THR   F  224 ? 1.8979 0.7636 1.5938 0.0255  0.0504  0.0137  220 THR   F CB  
10985 O  OG1 . THR   F  224 ? 1.8889 0.6236 1.6467 0.0636  0.0351  -0.0488 220 THR   F OG1 
10986 C  CG2 . THR   F  224 ? 1.8879 0.8311 1.6241 0.0605  0.0561  0.0211  220 THR   F CG2 
10987 N  N   . ASN   F  225 ? 1.8554 1.0050 1.4821 -0.0599 0.0171  -0.0485 221 ASN   F N   
10988 C  CA  . ASN   F  225 ? 1.8296 1.0333 1.4569 -0.0754 0.0215  -0.1522 221 ASN   F CA  
10989 C  C   . ASN   F  225 ? 1.8200 0.9772 1.2989 0.0050  0.0150  -0.2480 221 ASN   F C   
10990 O  O   . ASN   F  225 ? 1.7927 0.9541 1.1531 -0.0966 0.0021  -0.2830 221 ASN   F O   
10991 C  CB  . ASN   F  225 ? 1.8410 1.0331 1.5524 -0.0965 0.0365  -0.1609 221 ASN   F CB  
10992 C  CG  . ASN   F  225 ? 1.8538 1.0638 1.5952 -0.1788 0.0453  -0.0919 221 ASN   F CG  
10993 O  OD1 . ASN   F  225 ? 1.6868 1.3200 1.6783 -0.2322 0.0772  -0.1630 221 ASN   F OD1 
10994 N  ND2 . ASN   F  225 ? 1.8386 1.2451 1.5866 -0.1908 0.0990  -0.0993 221 ASN   F ND2 
10995 N  N   . GLY   F  226 ? 1.8153 1.0074 1.3070 -0.0176 -0.0144 -0.1619 222 GLY   F N   
10996 C  CA  . GLY   F  226 ? 1.7874 1.0395 1.2473 0.0148  -0.0338 -0.1834 222 GLY   F CA  
10997 C  C   . GLY   F  226 ? 1.7983 1.0170 1.2367 0.0211  -0.0549 -0.2202 222 GLY   F C   
10998 O  O   . GLY   F  226 ? 1.8001 1.0963 1.1849 0.0484  -0.0237 -0.2438 222 GLY   F O   
10999 N  N   . LEU   F  227 ? 1.8482 0.9546 1.2129 0.0259  -0.1279 -0.2219 223 LEU   F N   
11000 C  CA  . LEU   F  227 ? 1.9086 0.9260 1.2456 0.0238  -0.1693 -0.1728 223 LEU   F CA  
11001 C  C   . LEU   F  227 ? 1.9577 0.8901 1.2781 -0.0152 -0.1922 -0.1124 223 LEU   F C   
11002 O  O   . LEU   F  227 ? 1.9915 0.9035 1.2433 0.0059  -0.1034 0.0440  223 LEU   F O   
11003 C  CB  . LEU   F  227 ? 1.8695 0.9923 1.2917 0.0157  -0.2286 -0.1399 223 LEU   F CB  
11004 C  CG  . LEU   F  227 ? 1.8666 0.9932 1.3428 0.0018  -0.2693 -0.1168 223 LEU   F CG  
11005 C  CD1 . LEU   F  227 ? 1.8277 1.0274 1.3717 0.0020  -0.2893 -0.0940 223 LEU   F CD1 
11006 C  CD2 . LEU   F  227 ? 1.8848 1.0001 1.3053 -0.0119 -0.2699 -0.1362 223 LEU   F CD2 
11007 N  N   . HIS   F  228 ? 1.9592 0.9028 1.2246 -0.0905 -0.2155 -0.1632 224 HIS   F N   
11008 C  CA  . HIS   F  228 ? 1.9067 0.9508 1.1941 -0.0884 -0.2313 -0.1108 224 HIS   F CA  
11009 C  C   . HIS   F  228 ? 1.8969 0.9164 1.2097 -0.0817 -0.1904 -0.1158 224 HIS   F C   
11010 O  O   . HIS   F  228 ? 1.9409 0.8692 1.2057 -0.1313 -0.1503 -0.0834 224 HIS   F O   
11011 C  CB  . HIS   F  228 ? 1.8828 0.9823 1.1641 -0.0740 -0.2694 -0.0962 224 HIS   F CB  
11012 C  CG  . HIS   F  228 ? 1.8929 1.0395 1.2592 -0.0043 -0.2734 -0.0674 224 HIS   F CG  
11013 N  ND1 . HIS   F  228 ? 1.8758 1.0668 1.3569 0.0047  -0.2873 -0.0026 224 HIS   F ND1 
11014 C  CD2 . HIS   F  228 ? 1.8948 1.0665 1.2117 0.0035  -0.3140 -0.0809 224 HIS   F CD2 
11015 C  CE1 . HIS   F  228 ? 1.9133 1.0802 1.3419 0.0164  -0.3167 -0.0095 224 HIS   F CE1 
11016 N  NE2 . HIS   F  228 ? 1.9327 1.1133 1.2756 0.0280  -0.3074 -0.0270 224 HIS   F NE2 
11017 N  N   . LYS   F  229 ? 1.9033 0.9500 1.3089 -0.0586 -0.1317 -0.0889 225 LYS   F N   
11018 C  CA  . LYS   F  229 ? 1.9110 0.9287 1.4794 -0.0518 -0.1394 -0.1073 225 LYS   F CA  
11019 C  C   . LYS   F  229 ? 1.9169 0.8807 1.3786 -0.0951 -0.0940 -0.0335 225 LYS   F C   
11020 O  O   . LYS   F  229 ? 1.8903 0.6538 1.3742 -0.0467 -0.0691 0.0435  225 LYS   F O   
11021 C  CB  . LYS   F  229 ? 1.9585 0.9420 1.5626 -0.1072 -0.1053 -0.1169 225 LYS   F CB  
11022 C  CG  . LYS   F  229 ? 2.0150 0.9639 1.7568 -0.0633 -0.1703 -0.2113 225 LYS   F CG  
11023 C  CD  . LYS   F  229 ? 2.0505 1.0193 1.8358 -0.0882 -0.1273 -0.2151 225 LYS   F CD  
11024 C  CE  . LYS   F  229 ? 2.0699 1.0143 1.9013 -0.0600 -0.1906 -0.3034 225 LYS   F CE  
11025 N  NZ  . LYS   F  229 ? 2.0873 1.0112 2.0387 -0.1130 -0.2326 -0.3917 225 LYS   F NZ  
11026 N  N   . PHE   F  230 ? 1.9179 0.9461 1.3897 -0.0327 -0.0565 0.0369  226 PHE   F N   
11027 C  CA  . PHE   F  230 ? 1.9504 0.9265 1.4560 -0.0523 0.0301  -0.0043 226 PHE   F CA  
11028 C  C   . PHE   F  230 ? 2.0083 0.9302 1.4459 -0.0692 0.0459  0.0484  226 PHE   F C   
11029 O  O   . PHE   F  230 ? 2.0472 0.9887 1.4289 -0.0666 0.0326  0.1867  226 PHE   F O   
11030 C  CB  . PHE   F  230 ? 1.9080 0.9601 1.4101 -0.0645 0.0842  0.0074  226 PHE   F CB  
11031 C  CG  . PHE   F  230 ? 1.8659 0.8973 1.4802 -0.1211 0.0997  0.0385  226 PHE   F CG  
11032 C  CD1 . PHE   F  230 ? 1.8372 1.0135 1.4369 -0.1082 0.1794  0.0528  226 PHE   F CD1 
11033 C  CD2 . PHE   F  230 ? 1.7553 0.9205 1.4517 -0.1711 0.1534  0.0387  226 PHE   F CD2 
11034 C  CE1 . PHE   F  230 ? 1.8344 0.8917 1.4754 -0.1765 0.1711  0.0675  226 PHE   F CE1 
11035 C  CE2 . PHE   F  230 ? 1.7512 0.8883 1.4800 -0.1983 0.1621  0.0304  226 PHE   F CE2 
11036 C  CZ  . PHE   F  230 ? 1.8085 0.8623 1.5069 -0.1876 0.1443  0.0174  226 PHE   F CZ  
11037 N  N   . VAL   F  231 ? 2.0339 0.9379 1.4990 -0.0883 0.0473  0.0189  227 VAL   F N   
11038 C  CA  . VAL   F  231 ? 2.0208 0.9152 1.5883 -0.0515 0.0666  -0.0475 227 VAL   F CA  
11039 C  C   . VAL   F  231 ? 2.0089 0.8918 1.6250 -0.0080 0.0791  -0.0950 227 VAL   F C   
11040 O  O   . VAL   F  231 ? 1.9819 0.8475 1.5298 0.0667  0.1026  -0.1626 227 VAL   F O   
11041 C  CB  . VAL   F  231 ? 2.0664 0.8757 1.6963 -0.0908 0.0639  -0.0492 227 VAL   F CB  
11042 C  CG1 . VAL   F  231 ? 2.0568 0.9483 1.7373 -0.1028 0.0961  -0.0184 227 VAL   F CG1 
11043 C  CG2 . VAL   F  231 ? 2.0652 0.8313 1.7263 -0.0906 0.0650  -0.0441 227 VAL   F CG2 
11044 N  N   . LYS   F  232 ? 1.9235 1.0082 1.7675 -0.0326 0.0687  -0.1832 228 LYS   F N   
11045 C  CA  . LYS   F  232 ? 1.9212 1.0978 1.8928 -0.0429 0.0487  -0.1847 228 LYS   F CA  
11046 C  C   . LYS   F  232 ? 1.8776 1.0755 1.9515 -0.0446 0.0652  -0.2020 228 LYS   F C   
11047 O  O   . LYS   F  232 ? 1.8799 0.9790 1.9388 -0.0980 0.1171  -0.1787 228 LYS   F O   
11048 C  CB  . LYS   F  232 ? 1.9862 1.1789 1.9267 -0.0546 -0.0363 -0.2107 228 LYS   F CB  
11049 C  CG  . LYS   F  232 ? 1.9417 1.2599 1.9859 -0.0614 -0.0383 -0.1483 228 LYS   F CG  
11050 C  CD  . LYS   F  232 ? 1.9925 1.2740 2.0716 -0.0516 -0.0724 -0.1780 228 LYS   F CD  
11051 C  CE  . LYS   F  232 ? 2.0577 1.3326 2.1019 -0.0764 -0.1000 -0.1442 228 LYS   F CE  
11052 N  NZ  . LYS   F  232 ? 2.0591 1.3468 2.1653 -0.0834 -0.1163 -0.1637 228 LYS   F NZ  
11053 N  N   . GLY   F  233 ? 1.8537 1.1074 2.0088 -0.0491 0.0868  -0.1898 229 GLY   F N   
11054 C  CA  . GLY   F  233 ? 1.8777 1.1344 2.0005 -0.0862 0.0833  -0.1683 229 GLY   F CA  
11055 C  C   . GLY   F  233 ? 1.8876 1.1272 1.9954 -0.1207 0.0912  -0.1686 229 GLY   F C   
11056 O  O   . GLY   F  233 ? 1.7535 1.2115 1.9620 -0.2408 0.0426  -0.2782 229 GLY   F O   
11057 N  N   . ASP   F  234 ? 1.9147 1.0980 2.0186 -0.1299 0.1297  -0.1661 230 ASP   F N   
11058 C  CA  . ASP   F  234 ? 1.9249 1.1246 2.0066 -0.0989 0.2065  -0.1187 230 ASP   F CA  
11059 C  C   . ASP   F  234 ? 1.9201 1.1340 2.0298 -0.1188 0.2046  -0.0511 230 ASP   F C   
11060 O  O   . ASP   F  234 ? 2.0215 1.1537 2.0423 -0.1733 0.2480  -0.0656 230 ASP   F O   
11061 C  CB  . ASP   F  234 ? 1.8823 1.1848 1.9812 -0.0796 0.2341  -0.0909 230 ASP   F CB  
11062 C  CG  . ASP   F  234 ? 1.8344 1.3214 2.0283 -0.0333 0.2669  -0.0453 230 ASP   F CG  
11063 O  OD1 . ASP   F  234 ? 1.7819 1.3885 2.0662 0.0257  0.2932  -0.0466 230 ASP   F OD1 
11064 O  OD2 . ASP   F  234 ? 1.9124 1.4426 1.9748 0.1009  0.2433  0.0841  230 ASP   F OD2 
11065 N  N   . LEU   F  235 ? 1.9575 0.9686 2.0144 -0.0903 0.1896  -0.0462 231 LEU   F N   
11066 C  CA  . LEU   F  235 ? 1.9549 1.0207 2.0206 -0.0808 0.1907  -0.1012 231 LEU   F CA  
11067 C  C   . LEU   F  235 ? 2.0282 0.9995 1.9601 -0.0563 0.1644  -0.1338 231 LEU   F C   
11068 O  O   . LEU   F  235 ? 2.1057 0.9988 2.1294 -0.0693 0.1727  -0.2230 231 LEU   F O   
11069 C  CB  . LEU   F  235 ? 1.9024 0.9636 2.0238 -0.1445 0.1921  -0.1186 231 LEU   F CB  
11070 C  CG  . LEU   F  235 ? 1.9301 1.0037 2.0249 -0.1974 0.1937  -0.1663 231 LEU   F CG  
11071 C  CD1 . LEU   F  235 ? 1.8735 1.0635 2.0312 -0.2399 0.2468  -0.1310 231 LEU   F CD1 
11072 C  CD2 . LEU   F  235 ? 1.9787 0.8956 1.9834 -0.2231 0.1494  -0.2364 231 LEU   F CD2 
11073 N  N   . LEU   F  236 ? 2.1097 0.9930 1.9211 -0.0203 0.2191  -0.0806 232 LEU   F N   
11074 C  CA  . LEU   F  236 ? 2.1093 0.9249 1.8712 -0.0346 0.2243  -0.1380 232 LEU   F CA  
11075 C  C   . LEU   F  236 ? 2.1029 0.8161 1.8333 -0.0685 0.2003  -0.0893 232 LEU   F C   
11076 O  O   . LEU   F  236 ? 2.2224 0.8927 1.9351 -0.1586 0.1147  -0.1031 232 LEU   F O   
11077 C  CB  . LEU   F  236 ? 2.0759 0.8395 1.8327 0.0360  0.2997  -0.1025 232 LEU   F CB  
11078 C  CG  . LEU   F  236 ? 2.0385 0.7478 1.8398 0.0868  0.3321  -0.1562 232 LEU   F CG  
11079 C  CD1 . LEU   F  236 ? 2.0130 0.6821 1.8061 0.1406  0.3411  -0.1851 232 LEU   F CD1 
11080 C  CD2 . LEU   F  236 ? 2.0078 0.7346 1.8393 0.0899  0.3253  -0.1399 232 LEU   F CD2 
11081 N  N   . GLN   F  237 ? 2.0930 0.8533 1.8069 -0.0639 0.1975  -0.0218 233 GLN   F N   
11082 C  CA  . GLN   F  237 ? 2.0335 0.9426 1.7859 -0.0475 0.2108  0.0211  233 GLN   F CA  
11083 C  C   . GLN   F  237 ? 2.0193 0.9226 1.7728 -0.0907 0.2241  0.0425  233 GLN   F C   
11084 O  O   . GLN   F  237 ? 1.9580 0.9278 1.7559 -0.0920 0.2195  0.0341  233 GLN   F O   
11085 C  CB  . GLN   F  237 ? 1.9991 1.0463 1.8066 -0.0226 0.2150  0.0329  233 GLN   F CB  
11086 C  CG  . GLN   F  237 ? 2.0209 1.1844 1.8642 0.0425  0.2298  0.0151  233 GLN   F CG  
11087 C  CD  . GLN   F  237 ? 2.0290 1.2636 1.8288 0.0895  0.2149  0.0311  233 GLN   F CD  
11088 O  OE1 . GLN   F  237 ? 2.0738 1.4301 1.8664 0.1101  0.2334  -0.0927 233 GLN   F OE1 
11089 N  NE2 . GLN   F  237 ? 2.0244 1.3491 1.8655 0.1033  0.1964  -0.0720 233 GLN   F NE2 
11090 N  N   . GLU   F  238 ? 2.0650 1.0245 1.7360 -0.0443 0.2019  0.0446  234 GLU   F N   
11091 C  CA  . GLU   F  238 ? 2.1370 1.1185 1.7465 -0.0140 0.1848  -0.0015 234 GLU   F CA  
11092 C  C   . GLU   F  238 ? 2.1216 0.9924 1.7005 0.0455  0.2062  -0.0244 234 GLU   F C   
11093 O  O   . GLU   F  238 ? 2.1858 1.0093 1.7355 0.0033  0.1489  -0.0464 234 GLU   F O   
11094 C  CB  . GLU   F  238 ? 2.1945 1.2409 1.6461 0.0811  0.1039  -0.0073 234 GLU   F CB  
11095 C  CG  . GLU   F  238 ? 2.2583 1.3452 1.6516 0.1107  0.0761  -0.0203 234 GLU   F CG  
11096 C  CD  . GLU   F  238 ? 2.2942 1.2871 1.5970 0.0798  0.0308  -0.0609 234 GLU   F CD  
11097 O  OE1 . GLU   F  238 ? 2.2898 1.4152 1.6049 0.1495  0.0094  -0.0301 234 GLU   F OE1 
11098 O  OE2 . GLU   F  238 ? 2.3009 1.3309 1.5523 0.0468  -0.0378 -0.0879 234 GLU   F OE2 
11099 N  N   . ALA   F  239 ? 2.0543 0.9201 1.6906 0.0872  0.1691  -0.0923 235 ALA   F N   
11100 C  CA  . ALA   F  239 ? 2.0192 0.9742 1.6326 0.0783  0.1723  -0.1578 235 ALA   F CA  
11101 C  C   . ALA   F  239 ? 2.0114 0.8988 1.6487 0.0398  0.2194  -0.2177 235 ALA   F C   
11102 O  O   . ALA   F  239 ? 1.9878 0.8225 1.6764 0.0604  0.2177  -0.1674 235 ALA   F O   
11103 C  CB  . ALA   F  239 ? 1.9762 0.9769 1.5904 0.0778  0.1579  -0.1018 235 ALA   F CB  
11104 N  N   . ILE   F  240 ? 1.9950 0.9510 1.6679 0.0836  0.2334  -0.2192 236 ILE   F N   
11105 C  CA  . ILE   F  240 ? 2.0323 0.9039 1.7741 0.0746  0.2616  -0.2168 236 ILE   F CA  
11106 C  C   . ILE   F  240 ? 2.0700 1.1075 1.8332 0.0617  0.3784  -0.2349 236 ILE   F C   
11107 O  O   . ILE   F  240 ? 2.1376 1.1808 1.9430 -0.0521 0.3874  -0.3178 236 ILE   F O   
11108 C  CB  . ILE   F  240 ? 2.0114 0.9136 1.7923 0.1131  0.2336  -0.1669 236 ILE   F CB  
11109 C  CG1 . ILE   F  240 ? 1.9378 1.0091 1.7670 0.1073  0.2200  -0.1264 236 ILE   F CG1 
11110 C  CG2 . ILE   F  240 ? 2.0282 0.8949 1.7807 0.1146  0.2151  -0.1849 236 ILE   F CG2 
11111 C  CD1 . ILE   F  240 ? 1.9201 1.0693 1.8095 0.1057  0.1803  -0.1023 236 ILE   F CD1 
11112 N  N   . ASP   F  241 ? 2.0793 1.0811 1.9260 0.0651  0.4373  -0.2418 237 ASP   F N   
11113 C  CA  . ASP   F  241 ? 2.1032 1.2281 1.9664 0.0580  0.4927  -0.2589 237 ASP   F CA  
11114 C  C   . ASP   F  241 ? 2.0786 1.3321 1.9744 0.0465  0.4362  -0.1766 237 ASP   F C   
11115 O  O   . ASP   F  241 ? 2.2439 1.3244 2.0316 -0.0645 0.4641  -0.2153 237 ASP   F O   
11116 C  CB  . ASP   F  241 ? 2.1041 1.3037 2.0100 0.0758  0.5897  -0.2507 237 ASP   F CB  
11117 C  CG  . ASP   F  241 ? 2.0637 1.3332 2.0581 0.0536  0.6284  -0.2513 237 ASP   F CG  
11118 O  OD1 . ASP   F  241 ? 2.1726 1.4784 2.1050 0.1398  0.6014  -0.2172 237 ASP   F OD1 
11119 O  OD2 . ASP   F  241 ? 2.0477 1.3136 2.0320 0.0964  0.7878  -0.2588 237 ASP   F OD2 
11120 N  N   . PHE   F  242 ? 2.0996 1.1902 1.9229 0.0391  0.4011  -0.2276 238 PHE   F N   
11121 C  CA  . PHE   F  242 ? 2.1084 1.2323 1.9278 0.1196  0.3351  -0.2314 238 PHE   F CA  
11122 C  C   . PHE   F  242 ? 2.0580 1.3107 1.9551 0.0887  0.2935  -0.1823 238 PHE   F C   
11123 O  O   . PHE   F  242 ? 2.0456 1.4349 2.0125 0.1044  0.2269  -0.2544 238 PHE   F O   
11124 C  CB  . PHE   F  242 ? 2.1671 1.0467 1.8340 0.0619  0.2950  -0.2117 238 PHE   F CB  
11125 C  CG  . PHE   F  242 ? 2.2785 0.9120 1.7744 0.0504  0.2507  -0.2083 238 PHE   F CG  
11126 C  CD1 . PHE   F  242 ? 2.3223 0.9530 1.7922 0.0247  0.2519  -0.1353 238 PHE   F CD1 
11127 C  CD2 . PHE   F  242 ? 2.3092 0.8115 1.7146 0.0513  0.2361  -0.2256 238 PHE   F CD2 
11128 C  CE1 . PHE   F  242 ? 2.3432 0.9898 1.8017 0.0257  0.2135  -0.0804 238 PHE   F CE1 
11129 C  CE2 . PHE   F  242 ? 2.3298 0.8571 1.7606 0.0497  0.1884  -0.1804 238 PHE   F CE2 
11130 C  CZ  . PHE   F  242 ? 2.3467 0.9564 1.7916 0.0292  0.1979  -0.0723 238 PHE   F CZ  
11131 N  N   . ALA   F  243 ? 2.0441 1.4454 1.9205 0.1473  0.2237  -0.2500 239 ALA   F N   
11132 C  CA  . ALA   F  243 ? 2.0651 1.3863 1.9570 0.1601  0.1735  -0.2546 239 ALA   F CA  
11133 C  C   . ALA   F  243 ? 2.1493 1.3619 2.0272 0.1911  0.1072  -0.2297 239 ALA   F C   
11134 O  O   . ALA   F  243 ? 2.2299 1.3158 2.0575 0.2434  0.0343  -0.2080 239 ALA   F O   
11135 C  CB  . ALA   F  243 ? 2.0234 1.4503 1.9424 0.1248  0.1717  -0.2266 239 ALA   F CB  
11136 N  N   . GLN   F  244 ? 2.1791 1.3345 2.0897 0.1782  0.0340  -0.2097 240 GLN   F N   
11137 C  CA  . GLN   F  244 ? 2.1586 1.4278 2.1299 0.2034  -0.0093 -0.2228 240 GLN   F CA  
11138 C  C   . GLN   F  244 ? 2.1115 1.4898 2.1301 0.1386  0.0050  -0.2427 240 GLN   F C   
11139 O  O   . GLN   F  244 ? 2.0704 1.4887 2.2287 0.0939  0.0065  -0.2957 240 GLN   F O   
11140 C  CB  . GLN   F  244 ? 2.1702 1.4830 2.1120 0.2122  -0.0499 -0.2249 240 GLN   F CB  
11141 C  CG  . GLN   F  244 ? 2.2052 1.5913 2.1167 0.2129  -0.0642 -0.2704 240 GLN   F CG  
11142 C  CD  . GLN   F  244 ? 2.2600 1.6796 1.9975 0.2580  -0.0666 -0.2499 240 GLN   F CD  
11143 O  OE1 . GLN   F  244 ? 2.2411 1.8600 1.9895 0.1997  -0.0825 -0.2756 240 GLN   F OE1 
11144 N  NE2 . GLN   F  244 ? 2.3210 1.7584 2.0382 0.3186  -0.0446 -0.3036 240 GLN   F NE2 
11145 N  N   . LYS   F  245 ? 2.0702 1.4931 2.0534 0.0968  0.0339  -0.2780 241 LYS   F N   
11146 C  CA  . LYS   F  245 ? 2.0828 1.6083 2.0449 0.0544  0.0518  -0.2889 241 LYS   F CA  
11147 C  C   . LYS   F  245 ? 2.1483 1.6543 2.0401 0.0137  0.0391  -0.3235 241 LYS   F C   
11148 O  O   . LYS   F  245 ? 2.1531 1.8164 1.9449 -0.0316 0.0441  -0.3805 241 LYS   F O   
11149 C  CB  . LYS   F  245 ? 2.0374 1.6810 2.0028 0.0270  0.0272  -0.2621 241 LYS   F CB  
11150 C  CG  . LYS   F  245 ? 2.0426 1.8430 1.9624 0.0048  -0.0085 -0.2393 241 LYS   F CG  
11151 C  CD  . LYS   F  245 ? 2.0513 1.9429 1.9300 0.0009  -0.0485 -0.1855 241 LYS   F CD  
11152 C  CE  . LYS   F  245 ? 2.1010 2.0761 1.9376 -0.0033 -0.0154 -0.1529 241 LYS   F CE  
11153 N  NZ  . LYS   F  245 ? 2.1303 2.1407 1.9250 -0.0087 -0.0107 -0.1195 241 LYS   F NZ  
11154 N  N   . GLU   F  246 ? 2.1590 1.5846 2.0776 0.0178  0.0427  -0.3628 242 GLU   F N   
11155 C  CA  . GLU   F  246 ? 2.2121 1.5810 2.1434 -0.0046 0.0043  -0.3790 242 GLU   F CA  
11156 C  C   . GLU   F  246 ? 2.2266 1.5598 2.3127 -0.0671 -0.0245 -0.3594 242 GLU   F C   
11157 O  O   . GLU   F  246 ? 2.1319 1.5914 2.3692 -0.1482 -0.0020 -0.3105 242 GLU   F O   
11158 C  CB  . GLU   F  246 ? 2.2305 1.5267 2.0766 -0.0107 -0.0038 -0.3980 242 GLU   F CB  
11159 C  CG  . GLU   F  246 ? 2.2490 1.5092 2.0310 -0.0244 0.0288  -0.4200 242 GLU   F CG  
11160 C  CD  . GLU   F  246 ? 2.3029 1.5795 1.9989 -0.0751 0.0858  -0.3921 242 GLU   F CD  
11161 O  OE1 . GLU   F  246 ? 2.3545 1.5695 2.0765 -0.1192 0.0964  -0.3006 242 GLU   F OE1 
11162 O  OE2 . GLU   F  246 ? 2.3451 1.6678 2.1128 -0.1336 0.0641  -0.4007 242 GLU   F OE2 
11163 N  N   . ILE   F  247 ? 2.2692 1.4411 2.3790 -0.0508 -0.0659 -0.2500 243 ILE   F N   
11164 C  CA  . ILE   F  247 ? 2.3178 1.3396 2.5171 -0.0925 0.0240  -0.2761 243 ILE   F CA  
11165 C  C   . ILE   F  247 ? 2.4154 1.4880 2.5770 -0.0495 0.1139  -0.3076 243 ILE   F C   
11166 O  O   . ILE   F  247 ? 2.4702 1.5488 2.7990 -0.2019 0.1166  -0.2768 243 ILE   F O   
11167 C  CB  . ILE   F  247 ? 2.2996 1.1775 2.4796 -0.0554 0.0901  -0.2366 243 ILE   F CB  
11168 C  CG1 . ILE   F  247 ? 2.2878 1.2591 2.5226 -0.0058 0.0307  -0.1865 243 ILE   F CG1 
11169 C  CG2 . ILE   F  247 ? 2.1565 1.1571 2.3498 -0.1404 0.1063  -0.2075 243 ILE   F CG2 
11170 C  CD1 . ILE   F  247 ? 2.2814 1.2558 2.5266 0.0498  0.0362  -0.1655 243 ILE   F CD1 
11171 N  N   . ASN   F  248 ? 2.4786 1.4373 2.4737 0.0364  0.2067  -0.3555 244 ASN   F N   
11172 C  CA  . ASN   F  248 ? 2.4320 1.5672 2.4290 0.0000  0.2514  -0.3695 244 ASN   F CA  
11173 C  C   . ASN   F  248 ? 2.5140 1.5394 2.3434 0.1100  0.4267  -0.3823 244 ASN   F C   
11174 O  O   . ASN   F  248 ? 2.5553 1.3892 2.3609 0.1753  0.4236  -0.3235 244 ASN   F O   
11175 C  CB  . ASN   F  248 ? 2.4187 1.5693 2.4333 -0.0018 0.2553  -0.4188 244 ASN   F CB  
11176 C  CG  . ASN   F  248 ? 2.1889 1.5429 2.5212 -0.0879 0.1368  -0.5063 244 ASN   F CG  
11177 O  OD1 . ASN   F  248 ? 2.1075 1.5380 2.4802 -0.1409 0.0331  -0.5399 244 ASN   F OD1 
11178 N  ND2 . ASN   F  248 ? 2.0883 1.5073 2.5172 -0.0996 0.1772  -0.4049 244 ASN   F ND2 
11179 N  N   . GLY   G  11  ? 2.0988 0.7795 1.7453 0.3365  -0.0980 0.1326  2   GLY   G N   
11180 C  CA  . GLY   G  11  ? 2.0472 0.8725 1.7026 0.2761  -0.1419 0.0956  2   GLY   G CA  
11181 C  C   . GLY   G  11  ? 2.0436 0.8762 1.7384 0.1713  -0.1816 0.0357  2   GLY   G C   
11182 O  O   . GLY   G  11  ? 2.0204 0.9999 1.6763 0.1058  -0.1881 -0.1077 2   GLY   G O   
11183 N  N   . TYR   G  12  ? 2.0561 0.8071 1.8485 0.1214  -0.2376 0.0486  3   TYR   G N   
11184 C  CA  . TYR   G  12  ? 2.1157 0.7736 1.9646 0.1679  -0.2552 0.0757  3   TYR   G CA  
11185 C  C   . TYR   G  12  ? 2.1037 0.5790 1.8044 0.1058  -0.2075 0.0662  3   TYR   G C   
11186 O  O   . TYR   G  12  ? 2.0983 0.5297 1.7840 0.1059  -0.2541 0.0109  3   TYR   G O   
11187 C  CB  . TYR   G  12  ? 2.2005 0.6798 2.1195 0.1503  -0.3373 0.0513  3   TYR   G CB  
11188 C  CG  . TYR   G  12  ? 2.2602 0.8126 2.4224 0.2064  -0.4153 0.0735  3   TYR   G CG  
11189 C  CD1 . TYR   G  12  ? 2.2881 0.9366 2.4789 0.2004  -0.4033 0.0494  3   TYR   G CD1 
11190 C  CD2 . TYR   G  12  ? 2.3069 0.9530 2.4264 0.1881  -0.4481 0.0490  3   TYR   G CD2 
11191 C  CE1 . TYR   G  12  ? 2.2943 1.1247 2.6088 0.2083  -0.4823 0.0599  3   TYR   G CE1 
11192 C  CE2 . TYR   G  12  ? 2.3195 1.1117 2.4969 0.1922  -0.5462 0.0277  3   TYR   G CE2 
11193 C  CZ  . TYR   G  12  ? 2.1457 1.1986 2.6463 0.2581  -0.5472 0.0405  3   TYR   G CZ  
11194 O  OH  . TYR   G  12  ? 2.1344 1.4100 2.6714 0.2577  -0.5920 -0.0134 3   TYR   G OH  
11195 N  N   . ASP   G  13  ? 2.1747 0.5843 1.6960 0.0588  -0.1099 0.0701  4   ASP   G N   
11196 C  CA  . ASP   G  13  ? 2.1700 0.5784 1.6074 0.0451  -0.0927 0.0317  4   ASP   G CA  
11197 C  C   . ASP   G  13  ? 2.2640 0.6276 1.5956 -0.0402 0.0005  -0.0314 4   ASP   G C   
11198 O  O   . ASP   G  13  ? 2.2575 0.6045 1.5215 -0.0421 0.0385  -0.1061 4   ASP   G O   
11199 C  CB  . ASP   G  13  ? 2.2148 0.6153 1.5934 -0.0032 -0.0904 0.0173  4   ASP   G CB  
11200 C  CG  . ASP   G  13  ? 2.1998 0.6427 1.6370 -0.0531 -0.0960 -0.0219 4   ASP   G CG  
11201 O  OD1 . ASP   G  13  ? 2.1540 0.7899 1.6555 -0.0458 -0.0636 -0.0909 4   ASP   G OD1 
11202 O  OD2 . ASP   G  13  ? 2.2004 0.8137 1.6396 -0.0634 -0.1261 -0.0220 4   ASP   G OD2 
11203 N  N   . ARG   G  14  ? 2.1974 0.5563 1.5675 0.0176  -0.0902 0.0160  5   ARG   G N   
11204 C  CA  . ARG   G  14  ? 2.1329 0.5795 1.5739 -0.0066 -0.1057 0.0591  5   ARG   G CA  
11205 C  C   . ARG   G  14  ? 2.1295 0.4717 1.4963 0.0265  -0.1451 0.0488  5   ARG   G C   
11206 O  O   . ARG   G  14  ? 2.2450 0.4109 1.4618 -0.0886 -0.1347 -0.0661 5   ARG   G O   
11207 C  CB  . ARG   G  14  ? 2.1222 0.5748 1.6971 0.0626  -0.1127 0.1010  5   ARG   G CB  
11208 C  CG  . ARG   G  14  ? 2.1221 0.6455 1.7700 0.0377  -0.1124 0.1485  5   ARG   G CG  
11209 C  CD  . ARG   G  14  ? 2.1105 0.6708 1.8369 0.0354  -0.0924 0.0966  5   ARG   G CD  
11210 N  NE  . ARG   G  14  ? 2.1689 0.6566 1.9114 0.0092  -0.0717 0.1093  5   ARG   G NE  
11211 C  CZ  . ARG   G  14  ? 2.1549 0.8166 1.9248 -0.0619 -0.1169 0.1516  5   ARG   G CZ  
11212 N  NH1 . ARG   G  14  ? 2.1199 0.9171 1.9498 -0.0502 -0.0719 0.1488  5   ARG   G NH1 
11213 N  NH2 . ARG   G  14  ? 2.1966 0.9919 1.9403 -0.0886 -0.1070 0.2803  5   ARG   G NH2 
11214 N  N   . HIS   G  15  ? 2.0166 0.5542 1.4076 0.0619  -0.1673 0.1607  6   HIS   G N   
11215 C  CA  . HIS   G  15  ? 1.9367 0.5326 1.3878 0.1219  -0.1655 0.1794  6   HIS   G CA  
11216 C  C   . HIS   G  15  ? 1.8472 0.4702 1.3067 0.0334  -0.1611 0.1876  6   HIS   G C   
11217 O  O   . HIS   G  15  ? 1.8300 0.2023 1.4384 0.1502  -0.2130 0.1437  6   HIS   G O   
11218 C  CB  . HIS   G  15  ? 1.9291 0.7093 1.3892 0.1135  -0.1615 0.2114  6   HIS   G CB  
11219 C  CG  . HIS   G  15  ? 1.9483 0.7833 1.4585 0.1943  -0.1317 0.2250  6   HIS   G CG  
11220 N  ND1 . HIS   G  15  ? 1.9342 0.9155 1.4882 0.1534  -0.1296 0.2522  6   HIS   G ND1 
11221 C  CD2 . HIS   G  15  ? 1.9715 0.8666 1.4750 0.1294  -0.1536 0.2040  6   HIS   G CD2 
11222 C  CE1 . HIS   G  15  ? 1.9373 0.9560 1.5074 0.2001  -0.1010 0.2383  6   HIS   G CE1 
11223 N  NE2 . HIS   G  15  ? 1.9593 0.9933 1.4723 0.1765  -0.1310 0.2488  6   HIS   G NE2 
11224 N  N   . ILE   G  16  ? 1.8161 0.4075 1.2743 0.0686  -0.2146 0.1474  7   ILE   G N   
11225 C  CA  . ILE   G  16  ? 1.7541 0.4581 1.2961 0.0962  -0.2031 0.1114  7   ILE   G CA  
11226 C  C   . ILE   G  16  ? 1.7501 0.5436 1.3154 0.0639  -0.1807 0.0800  7   ILE   G C   
11227 O  O   . ILE   G  16  ? 1.7943 0.4039 1.4252 0.1585  -0.0950 0.2171  7   ILE   G O   
11228 C  CB  . ILE   G  16  ? 1.7408 0.4693 1.2926 0.1058  -0.2151 0.1313  7   ILE   G CB  
11229 C  CG1 . ILE   G  16  ? 1.7341 0.4334 1.2877 0.1338  -0.2078 0.1227  7   ILE   G CG1 
11230 C  CG2 . ILE   G  16  ? 1.7354 0.5402 1.3410 0.1178  -0.2208 0.1243  7   ILE   G CG2 
11231 C  CD1 . ILE   G  16  ? 1.7154 0.4211 1.2705 0.1376  -0.2170 0.1285  7   ILE   G CD1 
11232 N  N   . THR   G  17  ? 1.7078 0.5839 1.2702 0.0978  -0.2032 -0.0123 8   THR   G N   
11233 C  CA  . THR   G  17  ? 1.6940 0.6757 1.1863 0.0632  -0.1774 -0.0367 8   THR   G CA  
11234 C  C   . THR   G  17  ? 1.7274 0.6808 1.1223 0.0704  -0.2098 -0.0375 8   THR   G C   
11235 O  O   . THR   G  17  ? 1.7347 0.6452 0.9787 0.0402  -0.1616 0.0217  8   THR   G O   
11236 C  CB  . THR   G  17  ? 1.7257 0.6425 1.1907 0.0086  -0.2003 -0.0596 8   THR   G CB  
11237 O  OG1 . THR   G  17  ? 1.7328 0.7347 1.2298 0.0098  -0.2018 -0.1458 8   THR   G OG1 
11238 C  CG2 . THR   G  17  ? 1.7339 0.6817 1.2255 -0.0101 -0.1541 -0.0802 8   THR   G CG2 
11239 N  N   . ILE   G  18  ? 1.7116 0.6479 1.0779 0.0935  -0.2384 -0.0796 9   ILE   G N   
11240 C  CA  . ILE   G  18  ? 1.7162 0.6285 1.1069 0.1048  -0.2293 -0.0722 9   ILE   G CA  
11241 C  C   . ILE   G  18  ? 1.7130 0.6316 1.1802 0.0936  -0.2756 -0.0269 9   ILE   G C   
11242 O  O   . ILE   G  18  ? 1.6631 0.7009 1.1680 0.1878  -0.2729 0.0267  9   ILE   G O   
11243 C  CB  . ILE   G  18  ? 1.7356 0.5893 1.1160 0.1140  -0.2354 -0.0728 9   ILE   G CB  
11244 C  CG1 . ILE   G  18  ? 1.7482 0.5740 1.1026 0.1070  -0.2259 -0.0686 9   ILE   G CG1 
11245 C  CG2 . ILE   G  18  ? 1.7302 0.6554 1.1114 0.0954  -0.2615 -0.0940 9   ILE   G CG2 
11246 C  CD1 . ILE   G  18  ? 1.7838 0.6411 1.0624 0.0902  -0.2215 -0.0746 9   ILE   G CD1 
11247 N  N   . PHE   G  19  ? 1.7360 0.5960 1.1669 0.0721  -0.2600 -0.0595 10  PHE   G N   
11248 C  CA  . PHE   G  19  ? 1.7598 0.6491 1.2171 0.0344  -0.2562 -0.0792 10  PHE   G CA  
11249 C  C   . PHE   G  19  ? 1.7327 0.6744 1.2547 0.0733  -0.2549 -0.1270 10  PHE   G C   
11250 O  O   . PHE   G  19  ? 1.6862 0.8125 1.1943 0.0475  -0.2518 -0.2291 10  PHE   G O   
11251 C  CB  . PHE   G  19  ? 1.7808 0.6141 1.1867 0.0477  -0.2572 -0.0732 10  PHE   G CB  
11252 C  CG  . PHE   G  19  ? 1.7842 0.5952 1.2060 0.0347  -0.2808 -0.0768 10  PHE   G CG  
11253 C  CD1 . PHE   G  19  ? 1.7899 0.5919 1.2172 0.0308  -0.2983 -0.0917 10  PHE   G CD1 
11254 C  CD2 . PHE   G  19  ? 1.7791 0.6429 1.1637 0.0411  -0.2596 -0.0710 10  PHE   G CD2 
11255 C  CE1 . PHE   G  19  ? 1.8004 0.6015 1.2370 0.0306  -0.2958 -0.0787 10  PHE   G CE1 
11256 C  CE2 . PHE   G  19  ? 1.7645 0.6684 1.1939 0.0362  -0.2699 -0.0441 10  PHE   G CE2 
11257 C  CZ  . PHE   G  19  ? 1.7847 0.6636 1.1940 0.0162  -0.2829 -0.0871 10  PHE   G CZ  
11258 N  N   . SER   G  20  ? 1.7629 0.5958 1.3629 0.0834  -0.1990 -0.1647 11  SER   G N   
11259 C  CA  . SER   G  20  ? 1.7775 0.6001 1.4326 0.0615  -0.1404 -0.0847 11  SER   G CA  
11260 C  C   . SER   G  20  ? 1.8263 0.4629 1.4821 0.0361  -0.1458 -0.0333 11  SER   G C   
11261 O  O   . SER   G  20  ? 1.8208 0.4523 1.5281 0.0254  -0.0998 0.0148  11  SER   G O   
11262 C  CB  . SER   G  20  ? 1.8146 0.6319 1.4551 0.0894  -0.1076 -0.1028 11  SER   G CB  
11263 O  OG  . SER   G  20  ? 1.7791 0.6663 1.4961 0.0441  -0.0776 -0.1394 11  SER   G OG  
11264 N  N   . PRO   G  21  ? 1.8021 0.3445 1.5186 -0.0288 -0.1332 -0.1246 12  PRO   G N   
11265 C  CA  . PRO   G  21  ? 1.8930 0.2133 1.5246 -0.0708 -0.1274 -0.1205 12  PRO   G CA  
11266 C  C   . PRO   G  21  ? 1.9206 0.1971 1.5430 -0.0865 -0.1451 -0.1100 12  PRO   G C   
11267 O  O   . PRO   G  21  ? 1.9534 0.2193 1.5937 -0.1413 -0.1134 -0.1004 12  PRO   G O   
11268 C  CB  . PRO   G  21  ? 1.8814 0.2441 1.5428 -0.0427 -0.1172 -0.0989 12  PRO   G CB  
11269 C  CG  . PRO   G  21  ? 1.8874 0.2404 1.5229 -0.0786 -0.1339 -0.1089 12  PRO   G CG  
11270 C  CD  . PRO   G  21  ? 1.8314 0.2160 1.5087 -0.0508 -0.1443 -0.1187 12  PRO   G CD  
11271 N  N   . GLU   G  22  ? 1.9629 0.2733 1.5375 -0.0626 -0.1576 -0.1234 13  GLU   G N   
11272 C  CA  . GLU   G  22  ? 1.9949 0.4572 1.5566 -0.0200 -0.1858 -0.0920 13  GLU   G CA  
11273 C  C   . GLU   G  22  ? 1.9900 0.4939 1.4860 0.0125  -0.2459 -0.0802 13  GLU   G C   
11274 O  O   . GLU   G  22  ? 2.0345 0.5267 1.5134 0.0452  -0.2710 -0.0304 13  GLU   G O   
11275 C  CB  . GLU   G  22  ? 2.0419 0.5816 1.5958 0.0073  -0.1614 -0.1435 13  GLU   G CB  
11276 C  CG  . GLU   G  22  ? 2.0080 0.6366 1.6434 0.0696  -0.1806 -0.1245 13  GLU   G CG  
11277 C  CD  . GLU   G  22  ? 2.0841 0.5465 1.6459 0.1152  -0.1762 -0.1451 13  GLU   G CD  
11278 O  OE1 . GLU   G  22  ? 2.1168 0.4112 1.6133 0.0616  -0.1625 -0.2669 13  GLU   G OE1 
11279 O  OE2 . GLU   G  22  ? 2.0249 0.4701 1.6284 0.1989  -0.2075 -0.1960 13  GLU   G OE2 
11280 N  N   . GLY   G  23  ? 1.9804 0.5299 1.3897 0.0201  -0.2850 -0.0587 14  GLY   G N   
11281 C  CA  . GLY   G  23  ? 1.9822 0.5329 1.2784 0.0137  -0.2819 -0.0291 14  GLY   G CA  
11282 C  C   . GLY   G  23  ? 1.9498 0.4881 1.2584 0.0556  -0.3003 -0.0182 14  GLY   G C   
11283 O  O   . GLY   G  23  ? 1.9828 0.5239 1.2791 0.0336  -0.3424 0.0267  14  GLY   G O   
11284 N  N   . ARG   G  24  ? 1.9705 0.4951 1.1978 0.0678  -0.2570 0.0214  15  ARG   G N   
11285 C  CA  . ARG   G  24  ? 1.9570 0.4794 1.2433 0.0863  -0.1967 0.0109  15  ARG   G CA  
11286 C  C   . ARG   G  24  ? 1.9560 0.3399 1.1683 0.1263  -0.1915 0.0182  15  ARG   G C   
11287 O  O   . ARG   G  24  ? 2.0437 0.1574 1.1106 0.1325  -0.1558 0.0363  15  ARG   G O   
11288 C  CB  . ARG   G  24  ? 2.0192 0.5748 1.2624 0.1012  -0.1336 -0.0329 15  ARG   G CB  
11289 C  CG  . ARG   G  24  ? 2.0059 0.6225 1.3717 0.0488  -0.0930 -0.0236 15  ARG   G CG  
11290 C  CD  . ARG   G  24  ? 2.0731 0.5836 1.4650 0.0696  -0.0724 0.0095  15  ARG   G CD  
11291 N  NE  . ARG   G  24  ? 2.0711 0.6282 1.5131 0.0963  -0.0551 0.0253  15  ARG   G NE  
11292 C  CZ  . ARG   G  24  ? 2.0514 0.7691 1.5303 0.2204  -0.0505 0.0037  15  ARG   G CZ  
11293 N  NH1 . ARG   G  24  ? 2.0281 0.7921 1.5853 0.2458  -0.0714 0.0828  15  ARG   G NH1 
11294 N  NH2 . ARG   G  24  ? 2.0514 0.8615 1.5410 0.1858  -0.0558 0.0574  15  ARG   G NH2 
11295 N  N   . LEU   G  25  ? 1.8934 0.3414 1.1736 0.1329  -0.1910 0.0193  16  LEU   G N   
11296 C  CA  . LEU   G  25  ? 1.8658 0.4412 1.1652 0.1253  -0.2052 0.0048  16  LEU   G CA  
11297 C  C   . LEU   G  25  ? 1.8568 0.4534 1.2561 0.1358  -0.1742 -0.0416 16  LEU   G C   
11298 O  O   . LEU   G  25  ? 1.8885 0.4960 1.2447 0.2119  -0.1502 -0.0610 16  LEU   G O   
11299 C  CB  . LEU   G  25  ? 1.8195 0.4256 1.1423 0.0801  -0.2410 0.0007  16  LEU   G CB  
11300 C  CG  . LEU   G  25  ? 1.8036 0.3790 1.1072 0.0581  -0.2619 0.0131  16  LEU   G CG  
11301 C  CD1 . LEU   G  25  ? 1.7912 0.3719 1.1234 0.0373  -0.2536 0.0245  16  LEU   G CD1 
11302 C  CD2 . LEU   G  25  ? 1.8116 0.3989 1.1203 0.0706  -0.2790 0.0176  16  LEU   G CD2 
11303 N  N   . TYR   G  26  ? 1.8133 0.4429 1.2621 0.0967  -0.1979 -0.0181 17  TYR   G N   
11304 C  CA  . TYR   G  26  ? 1.7777 0.4722 1.2723 0.0519  -0.2075 -0.0518 17  TYR   G CA  
11305 C  C   . TYR   G  26  ? 1.7365 0.4104 1.3325 0.0280  -0.2375 -0.1005 17  TYR   G C   
11306 O  O   . TYR   G  26  ? 1.7623 0.4609 1.3515 0.0127  -0.1897 -0.1042 17  TYR   G O   
11307 C  CB  . TYR   G  26  ? 1.7998 0.5571 1.2648 0.0621  -0.2471 -0.0028 17  TYR   G CB  
11308 C  CG  . TYR   G  26  ? 1.8650 0.6129 1.3220 -0.0038 -0.2378 -0.0473 17  TYR   G CG  
11309 C  CD1 . TYR   G  26  ? 1.8941 0.5956 1.3292 -0.0181 -0.2156 -0.0600 17  TYR   G CD1 
11310 C  CD2 . TYR   G  26  ? 1.9192 0.7101 1.3440 -0.0028 -0.2005 -0.0513 17  TYR   G CD2 
11311 C  CE1 . TYR   G  26  ? 1.9418 0.5622 1.3616 -0.0407 -0.2542 -0.1345 17  TYR   G CE1 
11312 C  CE2 . TYR   G  26  ? 1.9659 0.6498 1.3232 -0.0055 -0.2297 -0.1326 17  TYR   G CE2 
11313 C  CZ  . TYR   G  26  ? 1.9517 0.5331 1.3885 -0.0437 -0.2292 -0.1270 17  TYR   G CZ  
11314 O  OH  . TYR   G  26  ? 1.9527 0.4928 1.3670 -0.0183 -0.2355 -0.1293 17  TYR   G OH  
11315 N  N   . GLN   G  27  ? 1.7299 0.3019 1.3027 0.0565  -0.1967 -0.0665 18  GLN   G N   
11316 C  CA  . GLN   G  27  ? 1.7683 0.1701 1.2089 0.0525  -0.2346 -0.1330 18  GLN   G CA  
11317 C  C   . GLN   G  27  ? 1.7377 0.2113 1.2078 0.0464  -0.2281 -0.1209 18  GLN   G C   
11318 O  O   . GLN   G  27  ? 1.7000 0.2218 1.2546 0.0443  -0.1799 -0.1817 18  GLN   G O   
11319 C  CB  . GLN   G  27  ? 1.7517 0.1734 1.1779 0.0341  -0.2411 -0.0993 18  GLN   G CB  
11320 C  CG  . GLN   G  27  ? 1.7985 0.1478 1.1369 0.0616  -0.2271 -0.0787 18  GLN   G CG  
11321 C  CD  . GLN   G  27  ? 1.8189 0.1654 1.1002 0.0957  -0.2349 -0.0884 18  GLN   G CD  
11322 O  OE1 . GLN   G  27  ? 1.8378 0.3213 1.0384 0.0856  -0.1522 -0.0386 18  GLN   G OE1 
11323 N  NE2 . GLN   G  27  ? 1.8006 0.1579 1.0813 0.1009  -0.2069 -0.0384 18  GLN   G NE2 
11324 N  N   . VAL   G  28  ? 1.7469 0.3147 1.1570 0.0508  -0.1954 -0.0733 19  VAL   G N   
11325 C  CA  . VAL   G  28  ? 1.7691 0.4036 1.1198 0.0679  -0.1960 -0.0723 19  VAL   G CA  
11326 C  C   . VAL   G  28  ? 1.8101 0.4089 1.1188 0.0125  -0.2593 -0.0557 19  VAL   G C   
11327 O  O   . VAL   G  28  ? 1.8452 0.1681 1.1353 -0.0886 -0.2930 -0.0897 19  VAL   G O   
11328 C  CB  . VAL   G  28  ? 1.7914 0.4731 1.1038 0.1169  -0.1781 -0.0481 19  VAL   G CB  
11329 C  CG1 . VAL   G  28  ? 1.7265 0.5291 1.1136 0.1328  -0.1836 -0.0866 19  VAL   G CG1 
11330 C  CG2 . VAL   G  28  ? 1.7930 0.4999 1.0659 0.1482  -0.1526 -0.0486 19  VAL   G CG2 
11331 N  N   . GLU   G  29  ? 1.8075 0.4363 1.0522 0.0163  -0.2803 0.0056  20  GLU   G N   
11332 C  CA  . GLU   G  29  ? 1.7877 0.4647 1.0243 0.0674  -0.2687 -0.0081 20  GLU   G CA  
11333 C  C   . GLU   G  29  ? 1.7695 0.4168 1.0758 0.1113  -0.2707 -0.0426 20  GLU   G C   
11334 O  O   . GLU   G  29  ? 1.8332 0.4905 1.0716 0.1648  -0.2286 -0.0568 20  GLU   G O   
11335 C  CB  . GLU   G  29  ? 1.7962 0.5075 1.0091 0.0500  -0.2858 0.0288  20  GLU   G CB  
11336 C  CG  . GLU   G  29  ? 1.7910 0.6162 1.0265 0.0468  -0.2935 0.0480  20  GLU   G CG  
11337 C  CD  . GLU   G  29  ? 1.8409 0.7003 1.0551 0.0056  -0.2570 0.1207  20  GLU   G CD  
11338 O  OE1 . GLU   G  29  ? 1.8540 0.8979 1.0322 0.0018  -0.2590 0.1856  20  GLU   G OE1 
11339 O  OE2 . GLU   G  29  ? 1.9014 0.7203 1.1700 0.0310  -0.2210 0.1123  20  GLU   G OE2 
11340 N  N   . TYR   G  30  ? 1.7727 0.3946 1.0406 0.0973  -0.2708 -0.0748 21  TYR   G N   
11341 C  CA  . TYR   G  30  ? 1.7690 0.4664 1.1015 0.0535  -0.2560 -0.0925 21  TYR   G CA  
11342 C  C   . TYR   G  30  ? 1.7297 0.4610 1.1256 0.0208  -0.2683 -0.1066 21  TYR   G C   
11343 O  O   . TYR   G  30  ? 1.7405 0.4583 1.1708 -0.0532 -0.2324 -0.1506 21  TYR   G O   
11344 C  CB  . TYR   G  30  ? 1.7823 0.5223 1.1369 0.0564  -0.2686 -0.0744 21  TYR   G CB  
11345 C  CG  . TYR   G  30  ? 1.8501 0.5906 1.1670 0.0835  -0.2321 -0.0108 21  TYR   G CG  
11346 C  CD1 . TYR   G  30  ? 1.8667 0.6150 1.2111 0.0600  -0.2301 0.0025  21  TYR   G CD1 
11347 C  CD2 . TYR   G  30  ? 1.8605 0.6473 1.1638 0.0918  -0.2431 -0.0304 21  TYR   G CD2 
11348 C  CE1 . TYR   G  30  ? 1.9199 0.6118 1.2630 0.0541  -0.2076 0.0119  21  TYR   G CE1 
11349 C  CE2 . TYR   G  30  ? 1.9067 0.6841 1.1833 0.0871  -0.2381 -0.0028 21  TYR   G CE2 
11350 C  CZ  . TYR   G  30  ? 1.9319 0.6692 1.2673 0.0631  -0.2160 0.0046  21  TYR   G CZ  
11351 O  OH  . TYR   G  30  ? 1.9966 0.6488 1.3267 0.1110  -0.1994 0.0159  21  TYR   G OH  
11352 N  N   . ALA   G  31  ? 1.6745 0.4939 1.1082 0.0563  -0.2450 -0.1034 22  ALA   G N   
11353 C  CA  . ALA   G  31  ? 1.6634 0.5070 1.1406 0.0625  -0.2281 -0.0837 22  ALA   G CA  
11354 C  C   . ALA   G  31  ? 1.6608 0.4676 1.1277 0.0530  -0.2165 -0.1062 22  ALA   G C   
11355 O  O   . ALA   G  31  ? 1.6277 0.6127 1.0887 0.0835  -0.1841 -0.1216 22  ALA   G O   
11356 C  CB  . ALA   G  31  ? 1.6590 0.5732 1.1233 0.0363  -0.2124 -0.1154 22  ALA   G CB  
11357 N  N   . PHE   G  32  ? 1.7292 0.3453 1.0963 0.0187  -0.2304 -0.0988 23  PHE   G N   
11358 C  CA  . PHE   G  32  ? 1.7711 0.4116 1.1007 -0.0150 -0.2465 -0.0936 23  PHE   G CA  
11359 C  C   . PHE   G  32  ? 1.7790 0.5206 1.1522 0.0014  -0.1995 -0.1042 23  PHE   G C   
11360 O  O   . PHE   G  32  ? 1.7991 0.6050 1.1669 -0.0428 -0.2257 -0.1006 23  PHE   G O   
11361 C  CB  . PHE   G  32  ? 1.7706 0.4193 1.0764 0.0020  -0.2357 -0.0814 23  PHE   G CB  
11362 C  CG  . PHE   G  32  ? 1.7770 0.3735 1.1063 -0.0134 -0.2539 -0.1066 23  PHE   G CG  
11363 C  CD1 . PHE   G  32  ? 1.7866 0.3920 1.0827 -0.0368 -0.2719 -0.1254 23  PHE   G CD1 
11364 C  CD2 . PHE   G  32  ? 1.8037 0.3526 1.0932 -0.0390 -0.2751 -0.0979 23  PHE   G CD2 
11365 C  CE1 . PHE   G  32  ? 1.7487 0.4205 1.1000 -0.0428 -0.3093 -0.1096 23  PHE   G CE1 
11366 C  CE2 . PHE   G  32  ? 1.7881 0.3987 1.1269 -0.0422 -0.2770 -0.1119 23  PHE   G CE2 
11367 C  CZ  . PHE   G  32  ? 1.7874 0.4422 1.1051 -0.0824 -0.3077 -0.1298 23  PHE   G CZ  
11368 N  N   . LYS   G  33  ? 1.8189 0.6183 1.1104 0.0202  -0.2046 -0.0066 24  LYS   G N   
11369 C  CA  . LYS   G  33  ? 1.8851 0.6385 1.1622 0.0139  -0.1765 -0.0424 24  LYS   G CA  
11370 C  C   . LYS   G  33  ? 1.8856 0.5801 1.2278 -0.0300 -0.1923 -0.1222 24  LYS   G C   
11371 O  O   . LYS   G  33  ? 1.9716 0.6681 1.2685 -0.0901 -0.1718 -0.2340 24  LYS   G O   
11372 C  CB  . LYS   G  33  ? 1.9422 0.7349 1.1752 0.0231  -0.1755 0.0538  24  LYS   G CB  
11373 C  CG  . LYS   G  33  ? 1.9362 0.7851 1.2603 -0.0312 -0.1926 0.1452  24  LYS   G CG  
11374 C  CD  . LYS   G  33  ? 1.9727 0.8439 1.3571 -0.0322 -0.1982 0.2252  24  LYS   G CD  
11375 C  CE  . LYS   G  33  ? 1.9492 0.8384 1.3791 -0.0661 -0.1934 0.2522  24  LYS   G CE  
11376 N  NZ  . LYS   G  33  ? 1.9708 0.8688 1.3725 -0.0906 -0.1888 0.3010  24  LYS   G NZ  
11377 N  N   . ALA   G  34  ? 1.8854 0.5130 1.2503 -0.0094 -0.1878 -0.1116 25  ALA   G N   
11378 C  CA  . ALA   G  34  ? 1.8889 0.4088 1.2238 0.0515  -0.1900 -0.0693 25  ALA   G CA  
11379 C  C   . ALA   G  34  ? 1.8471 0.3315 1.1990 0.0177  -0.1350 -0.0560 25  ALA   G C   
11380 O  O   . ALA   G  34  ? 1.8332 0.1463 1.1627 0.0249  -0.1572 -0.0823 25  ALA   G O   
11381 C  CB  . ALA   G  34  ? 1.8848 0.3909 1.2736 0.0313  -0.1986 -0.0778 25  ALA   G CB  
11382 N  N   . THR   G  35  ? 1.8498 0.4017 1.1966 0.0362  -0.1306 -0.0181 26  THR   G N   
11383 C  CA  . THR   G  35  ? 1.8152 0.5195 1.2443 0.0827  -0.1322 0.0035  26  THR   G CA  
11384 C  C   . THR   G  35  ? 1.8942 0.4795 1.3315 0.1155  -0.1245 -0.0871 26  THR   G C   
11385 O  O   . THR   G  35  ? 1.9290 0.4210 1.4794 0.1106  -0.0528 -0.0664 26  THR   G O   
11386 C  CB  . THR   G  35  ? 1.8258 0.6288 1.2582 0.0875  -0.0753 0.0240  26  THR   G CB  
11387 O  OG1 . THR   G  35  ? 1.7878 0.7224 1.1505 0.0753  -0.0919 0.0212  26  THR   G OG1 
11388 C  CG2 . THR   G  35  ? 1.7989 0.6925 1.2777 0.0801  -0.0730 0.0109  26  THR   G CG2 
11389 N  N   . ASN   G  36  ? 1.8799 0.4436 1.2450 0.1160  -0.1645 0.0160  27  ASN   G N   
11390 C  CA  . ASN   G  36  ? 1.8605 0.4027 1.2359 0.1378  -0.1848 0.0227  27  ASN   G CA  
11391 C  C   . ASN   G  36  ? 1.8617 0.3801 1.1976 0.1509  -0.1960 -0.0083 27  ASN   G C   
11392 O  O   . ASN   G  36  ? 1.9497 0.5621 1.1418 0.1374  -0.2240 -0.0123 27  ASN   G O   
11393 C  CB  . ASN   G  36  ? 1.8333 0.4822 1.2223 0.0848  -0.1889 0.0667  27  ASN   G CB  
11394 C  CG  . ASN   G  36  ? 1.8354 0.5311 1.2335 0.1126  -0.2310 0.0859  27  ASN   G CG  
11395 O  OD1 . ASN   G  36  ? 1.7470 0.5220 1.1934 0.0387  -0.2323 0.1209  27  ASN   G OD1 
11396 N  ND2 . ASN   G  36  ? 1.8315 0.6962 1.2406 0.0234  -0.1939 0.0666  27  ASN   G ND2 
11397 N  N   . GLN   G  37  ? 1.8309 0.4236 1.2995 0.1517  -0.2197 -0.0255 28  GLN   G N   
11398 C  CA  . GLN   G  37  ? 1.8341 0.6209 1.4223 0.1323  -0.1620 -0.0271 28  GLN   G CA  
11399 C  C   . GLN   G  37  ? 1.8333 0.6040 1.3900 0.0977  -0.1956 -0.0371 28  GLN   G C   
11400 O  O   . GLN   G  37  ? 1.8055 0.5175 1.3961 0.0528  -0.1676 0.0292  28  GLN   G O   
11401 C  CB  . GLN   G  37  ? 1.8594 0.8010 1.5475 0.1079  -0.2117 -0.0914 28  GLN   G CB  
11402 C  CG  . GLN   G  37  ? 1.8672 1.0229 1.7409 0.1619  -0.2080 -0.0931 28  GLN   G CG  
11403 C  CD  . GLN   G  37  ? 1.9174 1.0323 1.8780 0.1133  -0.1900 -0.1307 28  GLN   G CD  
11404 O  OE1 . GLN   G  37  ? 1.8918 0.9105 1.9948 0.3040  -0.2523 -0.0886 28  GLN   G OE1 
11405 N  NE2 . GLN   G  37  ? 1.9581 1.3559 1.8782 0.1661  -0.1375 -0.1390 28  GLN   G NE2 
11406 N  N   . THR   G  38  ? 1.7943 0.6145 1.3541 0.1200  -0.1677 -0.0617 29  THR   G N   
11407 C  CA  . THR   G  38  ? 1.7844 0.7340 1.3152 0.0965  -0.1717 -0.0769 29  THR   G CA  
11408 C  C   . THR   G  38  ? 1.7580 0.6199 1.3099 0.0951  -0.1332 -0.0707 29  THR   G C   
11409 O  O   . THR   G  38  ? 1.6731 0.5802 1.2618 0.1185  -0.1480 -0.1546 29  THR   G O   
11410 C  CB  . THR   G  38  ? 1.8069 0.7548 1.3233 0.1106  -0.2213 -0.0748 29  THR   G CB  
11411 O  OG1 . THR   G  38  ? 1.7933 0.9390 1.2172 0.0790  -0.3237 -0.0918 29  THR   G OG1 
11412 C  CG2 . THR   G  38  ? 1.7915 0.8642 1.3185 0.0862  -0.2270 -0.0836 29  THR   G CG2 
11413 N  N   . ASN   G  39  ? 1.8243 0.6127 1.3391 0.0771  -0.0909 -0.0249 30  ASN   G N   
11414 C  CA  . ASN   G  39  ? 1.9122 0.7158 1.2938 0.0928  -0.0926 -0.0438 30  ASN   G CA  
11415 C  C   . ASN   G  39  ? 1.8982 0.7478 1.3250 0.1077  -0.0991 -0.0243 30  ASN   G C   
11416 O  O   . ASN   G  39  ? 1.8666 0.6788 1.3304 0.0773  -0.1283 -0.0699 30  ASN   G O   
11417 C  CB  . ASN   G  39  ? 1.9650 0.8054 1.3090 0.0935  -0.0444 -0.1104 30  ASN   G CB  
11418 C  CG  . ASN   G  39  ? 2.0308 0.8221 1.2921 0.1094  -0.0422 -0.1440 30  ASN   G CG  
11419 O  OD1 . ASN   G  39  ? 2.0586 0.8750 1.2312 0.1764  -0.0754 -0.0367 30  ASN   G OD1 
11420 N  ND2 . ASN   G  39  ? 2.0564 0.7875 1.3503 0.0753  -0.0437 -0.1745 30  ASN   G ND2 
11421 N  N   . ILE   G  40  ? 1.8856 0.7854 1.4167 0.1247  -0.0791 -0.0284 31  ILE   G N   
11422 C  CA  . ILE   G  40  ? 1.9272 0.8843 1.4458 0.1429  -0.0768 0.0435  31  ILE   G CA  
11423 C  C   . ILE   G  40  ? 1.8993 0.6631 1.4400 0.0795  -0.1334 -0.0431 31  ILE   G C   
11424 O  O   . ILE   G  40  ? 1.8670 0.6110 1.4982 0.1241  -0.0480 -0.1067 31  ILE   G O   
11425 C  CB  . ILE   G  40  ? 1.9334 0.9121 1.4893 0.1247  -0.0725 0.1683  31  ILE   G CB  
11426 C  CG1 . ILE   G  40  ? 1.9624 1.0545 1.4840 0.2192  -0.0235 0.2045  31  ILE   G CG1 
11427 C  CG2 . ILE   G  40  ? 1.9760 1.0451 1.5575 0.1766  -0.1006 0.2354  31  ILE   G CG2 
11428 C  CD1 . ILE   G  40  ? 1.9598 1.0790 1.4997 0.2458  0.0090  0.1851  31  ILE   G CD1 
11429 N  N   . ASN   G  41  ? 1.9310 0.6308 1.3934 0.0506  -0.1284 -0.1182 32  ASN   G N   
11430 C  CA  . ASN   G  41  ? 1.9137 0.7303 1.3397 0.0072  -0.1584 -0.2164 32  ASN   G CA  
11431 C  C   . ASN   G  41  ? 1.9050 0.6711 1.2587 -0.0683 -0.2153 -0.2942 32  ASN   G C   
11432 O  O   . ASN   G  41  ? 1.8852 0.7063 1.1859 -0.1264 -0.2234 -0.3707 32  ASN   G O   
11433 C  CB  . ASN   G  41  ? 1.8668 0.8308 1.3169 0.0056  -0.1516 -0.2516 32  ASN   G CB  
11434 C  CG  . ASN   G  41  ? 1.8860 0.8240 1.3749 0.0223  -0.0838 -0.2806 32  ASN   G CG  
11435 O  OD1 . ASN   G  41  ? 1.8848 1.0283 1.4554 0.0130  0.0054  -0.3052 32  ASN   G OD1 
11436 N  ND2 . ASN   G  41  ? 1.9299 0.9705 1.3522 0.0136  -0.0141 -0.3249 32  ASN   G ND2 
11437 N  N   . SER   G  42  ? 1.9278 0.6095 1.2589 -0.0728 -0.2594 -0.3462 33  SER   G N   
11438 C  CA  . SER   G  42  ? 1.9779 0.5728 1.2382 -0.1304 -0.3287 -0.2728 33  SER   G CA  
11439 C  C   . SER   G  42  ? 1.9785 0.4681 1.1916 -0.1061 -0.3860 -0.2835 33  SER   G C   
11440 O  O   . SER   G  42  ? 1.9229 0.4593 1.0662 -0.1942 -0.4054 -0.4797 33  SER   G O   
11441 C  CB  . SER   G  42  ? 2.0987 0.4661 1.2720 -0.1360 -0.3679 -0.2388 33  SER   G CB  
11442 O  OG  . SER   G  42  ? 2.1876 0.4268 1.2018 -0.1838 -0.3965 -0.3032 33  SER   G OG  
11443 N  N   . LEU   G  43  ? 1.9000 0.5019 1.1990 -0.1373 -0.3648 -0.2216 34  LEU   G N   
11444 C  CA  . LEU   G  43  ? 1.8850 0.5195 1.1936 -0.1469 -0.3506 -0.2081 34  LEU   G CA  
11445 C  C   . LEU   G  43  ? 1.8129 0.5665 1.1462 -0.0876 -0.3276 -0.2032 34  LEU   G C   
11446 O  O   . LEU   G  43  ? 1.8125 0.5785 1.1268 -0.1119 -0.3461 -0.2140 34  LEU   G O   
11447 C  CB  . LEU   G  43  ? 1.9056 0.4760 1.1904 -0.1650 -0.3348 -0.1888 34  LEU   G CB  
11448 C  CG  . LEU   G  43  ? 1.8951 0.5347 1.2375 -0.1602 -0.3247 -0.1227 34  LEU   G CG  
11449 C  CD1 . LEU   G  43  ? 1.9300 0.6440 1.1605 -0.1369 -0.3320 -0.1416 34  LEU   G CD1 
11450 C  CD2 . LEU   G  43  ? 1.8848 0.5355 1.2480 -0.1500 -0.3216 -0.1227 34  LEU   G CD2 
11451 N  N   . ALA   G  44  ? 1.7968 0.6415 1.1508 -0.0789 -0.3290 -0.1814 35  ALA   G N   
11452 C  CA  . ALA   G  44  ? 1.7863 0.6285 1.1260 -0.0847 -0.3489 -0.1561 35  ALA   G CA  
11453 C  C   . ALA   G  44  ? 1.8176 0.5678 1.1136 -0.0162 -0.4078 -0.1561 35  ALA   G C   
11454 O  O   . ALA   G  44  ? 1.8096 0.6198 0.9974 -0.0732 -0.4807 -0.1804 35  ALA   G O   
11455 C  CB  . ALA   G  44  ? 1.7185 0.5723 1.1464 -0.1037 -0.3140 -0.1700 35  ALA   G CB  
11456 N  N   . VAL   G  45  ? 1.8777 0.4981 1.1857 0.0073  -0.3911 -0.1594 36  VAL   G N   
11457 C  CA  . VAL   G  45  ? 1.8780 0.5169 1.2729 -0.0117 -0.4021 -0.1704 36  VAL   G CA  
11458 C  C   . VAL   G  45  ? 1.8385 0.5244 1.2878 -0.0033 -0.4600 -0.1301 36  VAL   G C   
11459 O  O   . VAL   G  45  ? 1.9118 0.2545 1.2973 0.0740  -0.4951 -0.0979 36  VAL   G O   
11460 C  CB  . VAL   G  45  ? 1.9237 0.5224 1.2736 -0.0390 -0.3698 -0.1776 36  VAL   G CB  
11461 C  CG1 . VAL   G  45  ? 1.9548 0.5284 1.3625 -0.1254 -0.3401 -0.1736 36  VAL   G CG1 
11462 C  CG2 . VAL   G  45  ? 1.9429 0.5506 1.2495 -0.0084 -0.3604 -0.1600 36  VAL   G CG2 
11463 N  N   . ARG   G  46  ? 1.8580 0.4981 1.3182 0.0417  -0.4713 -0.1192 37  ARG   G N   
11464 C  CA  . ARG   G  46  ? 1.9148 0.4494 1.3658 -0.0043 -0.4050 -0.1472 37  ARG   G CA  
11465 C  C   . ARG   G  46  ? 1.9670 0.5475 1.4212 0.0315  -0.4613 -0.1653 37  ARG   G C   
11466 O  O   . ARG   G  46  ? 1.9676 0.3638 1.4115 0.0593  -0.4043 -0.0770 37  ARG   G O   
11467 C  CB  . ARG   G  46  ? 1.8925 0.4422 1.3985 -0.0534 -0.3830 -0.1726 37  ARG   G CB  
11468 C  CG  . ARG   G  46  ? 1.8220 0.4154 1.3984 -0.0631 -0.3409 -0.1533 37  ARG   G CG  
11469 C  CD  . ARG   G  46  ? 1.7653 0.4264 1.4921 -0.1116 -0.2919 -0.1478 37  ARG   G CD  
11470 N  NE  . ARG   G  46  ? 1.7631 0.3581 1.4997 -0.1149 -0.2469 -0.1687 37  ARG   G NE  
11471 C  CZ  . ARG   G  46  ? 1.7440 0.4073 1.5621 -0.1242 -0.2305 -0.1933 37  ARG   G CZ  
11472 N  NH1 . ARG   G  46  ? 1.6747 0.4961 1.5423 -0.1460 -0.1852 -0.2239 37  ARG   G NH1 
11473 N  NH2 . ARG   G  46  ? 1.7065 0.4545 1.5913 -0.1078 -0.2105 -0.1959 37  ARG   G NH2 
11474 N  N   . GLY   G  47  ? 2.0222 0.6342 1.4093 0.0693  -0.4987 -0.0831 38  GLY   G N   
11475 C  CA  . GLY   G  47  ? 2.0363 0.8004 1.4359 0.1227  -0.5479 -0.1292 38  GLY   G CA  
11476 C  C   . GLY   G  47  ? 2.0361 0.8086 1.5019 0.1505  -0.5883 -0.1518 38  GLY   G C   
11477 O  O   . GLY   G  47  ? 1.9236 0.8379 1.4822 0.1695  -0.6460 -0.2135 38  GLY   G O   
11478 N  N   . LYS   G  48  ? 2.0758 0.7723 1.5439 0.1382  -0.6070 -0.1380 39  LYS   G N   
11479 C  CA  . LYS   G  48  ? 2.0902 0.7214 1.6002 0.1144  -0.5744 -0.1045 39  LYS   G CA  
11480 C  C   . LYS   G  48  ? 2.0465 0.7464 1.5124 0.1200  -0.5936 -0.0719 39  LYS   G C   
11481 O  O   . LYS   G  48  ? 2.0590 0.8103 1.4068 0.1719  -0.6279 0.0034  39  LYS   G O   
11482 C  CB  . LYS   G  48  ? 2.1610 0.7041 1.6222 0.0960  -0.5964 -0.0865 39  LYS   G CB  
11483 C  CG  . LYS   G  48  ? 2.1844 0.7613 1.7820 0.0447  -0.5561 -0.1146 39  LYS   G CG  
11484 C  CD  . LYS   G  48  ? 2.2395 0.7855 1.7956 0.0774  -0.5576 -0.1154 39  LYS   G CD  
11485 C  CE  . LYS   G  48  ? 2.2870 0.7518 1.8866 0.0712  -0.5404 -0.1400 39  LYS   G CE  
11486 N  NZ  . LYS   G  48  ? 2.2870 0.8506 1.9602 0.0095  -0.5115 -0.1678 39  LYS   G NZ  
11487 N  N   . ASP   G  49  ? 2.0188 0.7807 1.5625 0.0855  -0.6152 -0.0774 40  ASP   G N   
11488 C  CA  . ASP   G  49  ? 2.0580 0.7412 1.5374 0.1086  -0.5929 -0.1321 40  ASP   G CA  
11489 C  C   . ASP   G  49  ? 2.0299 0.6225 1.4549 0.0989  -0.5570 -0.1815 40  ASP   G C   
11490 O  O   . ASP   G  49  ? 1.9677 0.6682 1.3933 0.1105  -0.5962 -0.1536 40  ASP   G O   
11491 C  CB  . ASP   G  49  ? 2.1433 0.8069 1.5454 0.0183  -0.5749 -0.1264 40  ASP   G CB  
11492 C  CG  . ASP   G  49  ? 2.1607 0.9786 1.6106 0.0590  -0.6021 -0.0755 40  ASP   G CG  
11493 O  OD1 . ASP   G  49  ? 2.2307 1.0037 1.6344 -0.0536 -0.5649 -0.0463 40  ASP   G OD1 
11494 O  OD2 . ASP   G  49  ? 2.2549 1.2511 1.6611 -0.0416 -0.4766 0.0196  40  ASP   G OD2 
11495 N  N   . CYS   G  50  ? 2.0100 0.5986 1.4319 0.0619  -0.5306 -0.1773 41  CYS   G N   
11496 C  CA  . CYS   G  50  ? 1.9827 0.4481 1.3391 0.0295  -0.4779 -0.1899 41  CYS   G CA  
11497 C  C   . CYS   G  50  ? 1.9423 0.4144 1.3751 -0.0408 -0.4564 -0.1975 41  CYS   G C   
11498 O  O   . CYS   G  50  ? 2.0196 0.3251 1.5005 -0.0579 -0.3696 -0.1224 41  CYS   G O   
11499 C  CB  . CYS   G  50  ? 2.0209 0.4275 1.3315 0.0519  -0.4660 -0.2254 41  CYS   G CB  
11500 S  SG  . CYS   G  50  ? 2.0667 0.3451 1.2920 0.1540  -0.3605 -0.2693 41  CYS   G SG  
11501 N  N   . THR   G  51  ? 1.9505 0.2778 1.2688 -0.0324 -0.4262 -0.1575 42  THR   G N   
11502 C  CA  . THR   G  51  ? 1.8929 0.3242 1.2496 -0.0117 -0.4060 -0.1254 42  THR   G CA  
11503 C  C   . THR   G  51  ? 1.8722 0.3783 1.1867 -0.0367 -0.3986 -0.0958 42  THR   G C   
11504 O  O   . THR   G  51  ? 1.9047 0.2154 1.0669 0.0006  -0.4027 -0.0953 42  THR   G O   
11505 C  CB  . THR   G  51  ? 1.9041 0.3296 1.2626 -0.0113 -0.3813 -0.1451 42  THR   G CB  
11506 O  OG1 . THR   G  51  ? 1.9185 0.1967 1.3051 0.0147  -0.4123 -0.0978 42  THR   G OG1 
11507 C  CG2 . THR   G  51  ? 1.8993 0.3703 1.3071 -0.0067 -0.3678 -0.0988 42  THR   G CG2 
11508 N  N   . VAL   G  52  ? 1.8800 0.4202 1.1924 0.0027  -0.3704 -0.1281 43  VAL   G N   
11509 C  CA  . VAL   G  52  ? 1.8951 0.4257 1.2215 -0.0069 -0.3457 -0.1487 43  VAL   G CA  
11510 C  C   . VAL   G  52  ? 1.8663 0.3866 1.2914 -0.0132 -0.3159 -0.1336 43  VAL   G C   
11511 O  O   . VAL   G  52  ? 1.7710 0.4791 1.4195 -0.0610 -0.3225 -0.1822 43  VAL   G O   
11512 C  CB  . VAL   G  52  ? 1.9229 0.4415 1.2375 0.0052  -0.3551 -0.1722 43  VAL   G CB  
11513 C  CG1 . VAL   G  52  ? 1.9089 0.4495 1.2456 0.0011  -0.3535 -0.1611 43  VAL   G CG1 
11514 C  CG2 . VAL   G  52  ? 1.9597 0.4340 1.2807 0.0405  -0.3721 -0.1818 43  VAL   G CG2 
11515 N  N   . VAL   G  53  ? 1.8541 0.3861 1.3079 0.0074  -0.2797 -0.1208 44  VAL   G N   
11516 C  CA  . VAL   G  53  ? 1.8986 0.3888 1.2830 0.0149  -0.2540 -0.1039 44  VAL   G CA  
11517 C  C   . VAL   G  53  ? 1.9077 0.4659 1.2352 -0.0543 -0.2245 -0.0864 44  VAL   G C   
11518 O  O   . VAL   G  53  ? 1.9445 0.3242 1.1738 -0.0624 -0.2891 -0.1422 44  VAL   G O   
11519 C  CB  . VAL   G  53  ? 1.8821 0.3496 1.2687 0.0181  -0.2099 -0.1288 44  VAL   G CB  
11520 C  CG1 . VAL   G  53  ? 1.8773 0.3124 1.2171 0.0327  -0.1953 -0.1201 44  VAL   G CG1 
11521 C  CG2 . VAL   G  53  ? 1.8902 0.4192 1.2794 0.0517  -0.2164 -0.0981 44  VAL   G CG2 
11522 N  N   . ILE   G  54  ? 1.9449 0.4794 1.2628 -0.0664 -0.2511 -0.1297 45  ILE   G N   
11523 C  CA  . ILE   G  54  ? 1.9373 0.4419 1.2989 -0.0852 -0.2387 -0.1284 45  ILE   G CA  
11524 C  C   . ILE   G  54  ? 1.9085 0.3519 1.3850 -0.0718 -0.2048 -0.1478 45  ILE   G C   
11525 O  O   . ILE   G  54  ? 1.8711 0.4562 1.4366 -0.0897 -0.1689 -0.1605 45  ILE   G O   
11526 C  CB  . ILE   G  54  ? 2.0252 0.4386 1.3253 -0.1015 -0.2588 -0.1519 45  ILE   G CB  
11527 C  CG1 . ILE   G  54  ? 1.9989 0.4897 1.3762 -0.1201 -0.2564 -0.1887 45  ILE   G CG1 
11528 C  CG2 . ILE   G  54  ? 2.0567 0.5042 1.3075 -0.1297 -0.2809 -0.1083 45  ILE   G CG2 
11529 C  CD1 . ILE   G  54  ? 2.0508 0.6546 1.3390 -0.0820 -0.2850 -0.2117 45  ILE   G CD1 
11530 N  N   . SER   G  55  ? 1.9201 0.3256 1.3797 -0.0987 -0.1321 -0.1285 46  SER   G N   
11531 C  CA  . SER   G  55  ? 1.9198 0.4154 1.3780 -0.0702 -0.1545 -0.1305 46  SER   G CA  
11532 C  C   . SER   G  55  ? 1.9438 0.3951 1.2786 -0.1149 -0.1487 -0.0974 46  SER   G C   
11533 O  O   . SER   G  55  ? 2.0422 0.4270 1.3480 -0.2303 -0.1238 -0.0943 46  SER   G O   
11534 C  CB  . SER   G  55  ? 1.8920 0.4249 1.4236 -0.0196 -0.1733 -0.1682 46  SER   G CB  
11535 O  OG  . SER   G  55  ? 1.8702 0.4259 1.5766 0.0409  -0.1638 -0.1997 46  SER   G OG  
11536 N  N   . GLN   G  56  ? 1.9388 0.4518 1.2262 -0.0329 -0.1839 -0.0767 47  GLN   G N   
11537 C  CA  . GLN   G  56  ? 1.9421 0.5706 1.1842 -0.0316 -0.1581 -0.0483 47  GLN   G CA  
11538 C  C   . GLN   G  56  ? 1.9579 0.4812 1.1343 -0.0551 -0.1253 0.0017  47  GLN   G C   
11539 O  O   . GLN   G  56  ? 2.0109 0.3267 1.1464 -0.0505 -0.0851 0.0104  47  GLN   G O   
11540 C  CB  . GLN   G  56  ? 1.9323 0.5706 1.2053 -0.0148 -0.1800 -0.0613 47  GLN   G CB  
11541 C  CG  . GLN   G  56  ? 1.9498 0.5832 1.1699 0.0016  -0.2134 -0.1233 47  GLN   G CG  
11542 C  CD  . GLN   G  56  ? 1.9615 0.5905 1.1622 0.0633  -0.2272 -0.1586 47  GLN   G CD  
11543 O  OE1 . GLN   G  56  ? 1.9870 0.5875 1.1454 0.1183  -0.2258 -0.1462 47  GLN   G OE1 
11544 N  NE2 . GLN   G  56  ? 1.9855 0.7922 1.1003 0.0497  -0.1856 -0.1710 47  GLN   G NE2 
11545 N  N   . LYS   G  57  ? 1.9745 0.5414 1.1152 -0.0794 -0.1296 0.0497  48  LYS   G N   
11546 C  CA  . LYS   G  57  ? 1.9426 0.6577 1.1432 -0.0711 -0.1092 0.0937  48  LYS   G CA  
11547 C  C   . LYS   G  57  ? 1.9438 0.6897 1.1093 -0.0398 -0.0853 0.1588  48  LYS   G C   
11548 O  O   . LYS   G  57  ? 1.9206 0.7138 1.1065 -0.0384 -0.0574 0.2144  48  LYS   G O   
11549 C  CB  . LYS   G  57  ? 1.9341 0.6616 1.2049 -0.0564 -0.1250 0.1163  48  LYS   G CB  
11550 C  CG  . LYS   G  57  ? 1.9319 0.7014 1.3182 -0.0636 -0.1191 0.1278  48  LYS   G CG  
11551 C  CD  . LYS   G  57  ? 1.9454 0.7314 1.4264 -0.0557 -0.1242 0.1870  48  LYS   G CD  
11552 C  CE  . LYS   G  57  ? 1.9353 0.7693 1.5082 -0.0612 -0.1027 0.2159  48  LYS   G CE  
11553 N  NZ  . LYS   G  57  ? 1.9572 0.7633 1.5517 -0.0823 -0.1066 0.2158  48  LYS   G NZ  
11554 N  N   . LYS   G  58  ? 1.9648 0.8239 1.0665 -0.0222 -0.0904 0.1749  49  LYS   G N   
11555 C  CA  . LYS   G  58  ? 1.9323 0.9132 1.1053 -0.0201 -0.0883 0.1263  49  LYS   G CA  
11556 C  C   . LYS   G  58  ? 1.9690 0.9316 1.1000 -0.0602 -0.1166 0.1301  49  LYS   G C   
11557 O  O   . LYS   G  58  ? 1.8641 1.0115 1.1352 -0.1598 -0.1354 0.0843  49  LYS   G O   
11558 C  CB  . LYS   G  58  ? 1.9564 0.9020 1.1600 -0.0622 -0.0728 0.1081  49  LYS   G CB  
11559 C  CG  . LYS   G  58  ? 1.9541 0.9025 1.2085 -0.0584 -0.0852 0.1087  49  LYS   G CG  
11560 C  CD  . LYS   G  58  ? 1.9664 0.8913 1.2906 -0.0487 -0.0650 0.1241  49  LYS   G CD  
11561 C  CE  . LYS   G  58  ? 1.9493 0.8504 1.3618 -0.0412 -0.0601 0.1490  49  LYS   G CE  
11562 N  NZ  . LYS   G  58  ? 1.9526 0.8297 1.4696 -0.0504 -0.0053 0.1420  49  LYS   G NZ  
11563 N  N   . VAL   G  59  ? 1.9784 0.8483 1.1342 -0.0717 -0.1074 0.1376  50  VAL   G N   
11564 C  CA  . VAL   G  59  ? 1.9702 0.8808 1.2280 -0.0159 -0.1518 0.0220  50  VAL   G CA  
11565 C  C   . VAL   G  59  ? 2.0224 0.9014 1.2371 0.0277  -0.1064 0.0609  50  VAL   G C   
11566 O  O   . VAL   G  59  ? 2.1112 0.9661 1.2851 0.0211  -0.0227 0.0037  50  VAL   G O   
11567 C  CB  . VAL   G  59  ? 1.9912 0.8181 1.2733 -0.0341 -0.2050 -0.0236 50  VAL   G CB  
11568 C  CG1 . VAL   G  59  ? 1.9993 0.8240 1.3107 -0.0405 -0.2188 -0.0568 50  VAL   G CG1 
11569 C  CG2 . VAL   G  59  ? 1.9877 0.8250 1.2773 -0.0260 -0.2529 -0.0557 50  VAL   G CG2 
11570 N  N   . PRO   G  60  ? 1.9771 0.8794 1.2512 0.1126  -0.0762 0.0323  51  PRO   G N   
11571 C  CA  . PRO   G  60  ? 2.0087 0.8475 1.2410 0.1132  -0.0762 0.0533  51  PRO   G CA  
11572 C  C   . PRO   G  60  ? 2.0143 0.8656 1.2486 0.1032  -0.0715 0.0425  51  PRO   G C   
11573 O  O   . PRO   G  60  ? 2.0547 0.9590 1.1812 0.0866  -0.0447 0.0924  51  PRO   G O   
11574 C  CB  . PRO   G  60  ? 1.9895 0.8486 1.2618 0.1156  -0.0617 0.0648  51  PRO   G CB  
11575 C  CG  . PRO   G  60  ? 1.9558 0.8038 1.2970 0.1402  -0.0691 0.0616  51  PRO   G CG  
11576 C  CD  . PRO   G  60  ? 1.9404 0.8253 1.2529 0.1518  -0.0750 0.0457  51  PRO   G CD  
11577 N  N   . ASP   G  61  ? 1.9985 0.8312 1.3025 0.1135  -0.0475 0.0106  52  ASP   G N   
11578 C  CA  . ASP   G  61  ? 2.0002 0.8747 1.3402 0.1023  -0.0381 -0.0887 52  ASP   G CA  
11579 C  C   . ASP   G  61  ? 2.0201 0.8488 1.3195 0.1054  -0.0680 -0.1161 52  ASP   G C   
11580 O  O   . ASP   G  61  ? 1.9720 0.8582 1.1588 0.1036  -0.0723 -0.2727 52  ASP   G O   
11581 C  CB  . ASP   G  61  ? 2.0557 0.8496 1.2933 0.1039  -0.0103 -0.0758 52  ASP   G CB  
11582 C  CG  . ASP   G  61  ? 2.0665 0.9317 1.3031 0.0785  0.0168  -0.0980 52  ASP   G CG  
11583 O  OD1 . ASP   G  61  ? 2.1615 1.1705 1.3318 0.0403  0.0649  -0.1397 52  ASP   G OD1 
11584 O  OD2 . ASP   G  61  ? 2.1147 0.8236 1.2013 0.0682  0.1098  -0.0767 52  ASP   G OD2 
11585 N  N   . LYS   G  62  ? 2.0200 0.8648 1.3766 0.0902  -0.0521 -0.1338 53  LYS   G N   
11586 C  CA  . LYS   G  62  ? 2.0687 0.8088 1.4290 0.0385  -0.0549 -0.1270 53  LYS   G CA  
11587 C  C   . LYS   G  62  ? 2.1049 0.7899 1.4856 0.0317  -0.0491 -0.1308 53  LYS   G C   
11588 O  O   . LYS   G  62  ? 2.1728 0.7527 1.5010 0.0161  -0.0968 -0.1528 53  LYS   G O   
11589 C  CB  . LYS   G  62  ? 2.1121 0.8914 1.4648 0.0464  -0.0240 -0.1653 53  LYS   G CB  
11590 C  CG  . LYS   G  62  ? 2.1232 0.9838 1.4698 0.0606  -0.0283 -0.1904 53  LYS   G CG  
11591 C  CD  . LYS   G  62  ? 2.1314 1.1142 1.5801 0.0826  0.0338  -0.1855 53  LYS   G CD  
11592 C  CE  . LYS   G  62  ? 2.1692 1.1063 1.6811 0.0792  0.0565  -0.2038 53  LYS   G CE  
11593 N  NZ  . LYS   G  62  ? 2.2069 1.1343 1.7594 0.0413  0.1114  -0.2283 53  LYS   G NZ  
11594 N  N   . LEU   G  63  ? 2.0294 0.6234 1.4857 0.0252  -0.0283 -0.1076 54  LEU   G N   
11595 C  CA  . LEU   G  63  ? 1.9405 0.6543 1.4909 0.0218  -0.0160 -0.0953 54  LEU   G CA  
11596 C  C   . LEU   G  63  ? 1.9014 0.6888 1.4840 -0.0029 -0.0066 -0.1269 54  LEU   G C   
11597 O  O   . LEU   G  63  ? 1.7647 0.6767 1.4639 0.0697  0.0236  -0.2140 54  LEU   G O   
11598 C  CB  . LEU   G  63  ? 1.9144 0.5649 1.5103 0.0127  -0.0057 -0.0820 54  LEU   G CB  
11599 C  CG  . LEU   G  63  ? 1.9040 0.5501 1.5311 0.0094  0.0016  -0.0660 54  LEU   G CG  
11600 C  CD1 . LEU   G  63  ? 1.8809 0.6048 1.5338 -0.0091 -0.0059 -0.0790 54  LEU   G CD1 
11601 C  CD2 . LEU   G  63  ? 1.9197 0.5399 1.5550 0.0014  0.0031  -0.0472 54  LEU   G CD2 
11602 N  N   . LEU   G  64  ? 1.9067 0.7435 1.4532 0.0156  0.0145  -0.1139 55  LEU   G N   
11603 C  CA  . LEU   G  64  ? 1.9742 0.6956 1.4080 0.0127  -0.0288 -0.1565 55  LEU   G CA  
11604 C  C   . LEU   G  64  ? 1.9916 0.6894 1.4344 -0.0369 -0.0488 -0.1403 55  LEU   G C   
11605 O  O   . LEU   G  64  ? 1.9927 0.6661 1.4485 -0.0692 -0.0667 -0.1807 55  LEU   G O   
11606 C  CB  . LEU   G  64  ? 1.9566 0.7297 1.3291 0.0198  -0.0478 -0.1699 55  LEU   G CB  
11607 C  CG  . LEU   G  64  ? 1.9590 0.7973 1.2806 0.0697  -0.0612 -0.1869 55  LEU   G CG  
11608 C  CD1 . LEU   G  64  ? 1.9396 0.8249 1.1991 0.0689  -0.0612 -0.1917 55  LEU   G CD1 
11609 C  CD2 . LEU   G  64  ? 1.9512 0.7681 1.2981 0.1028  -0.0504 -0.1893 55  LEU   G CD2 
11610 N  N   . ASP   G  65  ? 1.9645 0.6289 1.4639 0.0017  -0.0498 -0.0595 56  ASP   G N   
11611 C  CA  . ASP   G  65  ? 1.9092 0.6089 1.4664 -0.0188 -0.0480 -0.0591 56  ASP   G CA  
11612 C  C   . ASP   G  65  ? 1.9003 0.5963 1.3526 -0.0225 -0.0625 -0.0489 56  ASP   G C   
11613 O  O   . ASP   G  65  ? 1.8220 0.5713 1.2484 -0.0324 -0.1726 -0.0687 56  ASP   G O   
11614 C  CB  . ASP   G  65  ? 1.9558 0.5408 1.5377 0.0365  -0.0400 -0.0471 56  ASP   G CB  
11615 C  CG  . ASP   G  65  ? 2.0406 0.4684 1.6595 0.0359  -0.0283 -0.0454 56  ASP   G CG  
11616 O  OD1 . ASP   G  65  ? 2.0605 0.2283 1.6867 0.0177  -0.0351 -0.0445 56  ASP   G OD1 
11617 O  OD2 . ASP   G  65  ? 2.0650 0.4672 1.7699 0.0282  -0.0488 -0.0531 56  ASP   G OD2 
11618 N  N   . PRO   G  66  ? 1.9045 0.6235 1.3788 -0.0691 -0.0565 -0.0552 57  PRO   G N   
11619 C  CA  . PRO   G  66  ? 1.9051 0.5633 1.3761 -0.0630 -0.0555 -0.0605 57  PRO   G CA  
11620 C  C   . PRO   G  66  ? 1.8943 0.5713 1.3598 -0.0512 -0.0781 -0.0600 57  PRO   G C   
11621 O  O   . PRO   G  66  ? 1.8964 0.3476 1.2582 -0.0260 -0.1027 -0.0479 57  PRO   G O   
11622 C  CB  . PRO   G  66  ? 1.9221 0.5914 1.3821 -0.0799 -0.0417 -0.0930 57  PRO   G CB  
11623 C  CG  . PRO   G  66  ? 1.9443 0.6598 1.3683 -0.0910 -0.0178 -0.1091 57  PRO   G CG  
11624 C  CD  . PRO   G  66  ? 1.9365 0.6693 1.4028 -0.0782 -0.0211 -0.0947 57  PRO   G CD  
11625 N  N   . THR   G  67  ? 1.9028 0.5620 1.3785 -0.0494 -0.0936 -0.0807 58  THR   G N   
11626 C  CA  . THR   G  67  ? 1.9008 0.5230 1.3338 -0.0600 -0.1155 -0.0357 58  THR   G CA  
11627 C  C   . THR   G  67  ? 1.8717 0.5058 1.3438 -0.0068 -0.1145 -0.0663 58  THR   G C   
11628 O  O   . THR   G  67  ? 1.9331 0.3077 1.4229 -0.0228 -0.1118 -0.0584 58  THR   G O   
11629 C  CB  . THR   G  67  ? 1.9176 0.5722 1.3142 -0.0805 -0.1499 0.0093  58  THR   G CB  
11630 O  OG1 . THR   G  67  ? 1.9238 0.5992 1.3309 -0.0773 -0.1670 0.0352  58  THR   G OG1 
11631 C  CG2 . THR   G  67  ? 1.9512 0.6687 1.3165 -0.0898 -0.1535 0.0158  58  THR   G CG2 
11632 N  N   . THR   G  68  ? 1.8642 0.5775 1.3551 0.0584  -0.1025 -0.0848 59  THR   G N   
11633 C  CA  . THR   G  68  ? 1.8153 0.6071 1.3540 0.1310  -0.1359 -0.0974 59  THR   G CA  
11634 C  C   . THR   G  68  ? 1.8519 0.5822 1.3052 0.1776  -0.1598 -0.0645 59  THR   G C   
11635 O  O   . THR   G  68  ? 1.8621 0.6045 1.2873 0.2443  -0.2210 -0.0782 59  THR   G O   
11636 C  CB  . THR   G  68  ? 1.7762 0.6233 1.3585 0.1471  -0.0919 -0.0853 59  THR   G CB  
11637 O  OG1 . THR   G  68  ? 1.7172 0.6595 1.3903 0.1496  -0.0931 -0.1241 59  THR   G OG1 
11638 C  CG2 . THR   G  68  ? 1.7863 0.6058 1.3819 0.1671  -0.0837 -0.0657 59  THR   G CG2 
11639 N  N   . VAL   G  69  ? 1.8901 0.5622 1.3328 0.1758  -0.2139 -0.0371 60  VAL   G N   
11640 C  CA  . VAL   G  69  ? 1.8875 0.5691 1.3103 0.1902  -0.2426 0.0054  60  VAL   G CA  
11641 C  C   . VAL   G  69  ? 1.8950 0.5477 1.2691 0.2077  -0.2570 -0.0107 60  VAL   G C   
11642 O  O   . VAL   G  69  ? 1.9274 0.5032 1.3116 0.2158  -0.2982 -0.1106 60  VAL   G O   
11643 C  CB  . VAL   G  69  ? 1.9278 0.5182 1.3232 0.1679  -0.2338 0.0389  60  VAL   G CB  
11644 C  CG1 . VAL   G  69  ? 1.8944 0.6070 1.3505 0.1399  -0.2292 0.0747  60  VAL   G CG1 
11645 C  CG2 . VAL   G  69  ? 1.9213 0.5605 1.3432 0.1469  -0.2265 0.0486  60  VAL   G CG2 
11646 N  N   . SER   G  70  ? 1.8533 0.5383 1.2079 0.1934  -0.3019 0.0146  61  SER   G N   
11647 C  CA  . SER   G  70  ? 1.8154 0.6210 1.2249 0.1444  -0.3490 -0.0247 61  SER   G CA  
11648 C  C   . SER   G  70  ? 1.7799 0.4660 1.2818 0.1413  -0.3555 0.0312  61  SER   G C   
11649 O  O   . SER   G  70  ? 1.8066 0.3819 1.3328 0.1697  -0.4042 0.0607  61  SER   G O   
11650 C  CB  . SER   G  70  ? 1.8304 0.6061 1.2481 0.0881  -0.3553 -0.0767 61  SER   G CB  
11651 O  OG  . SER   G  70  ? 1.8056 0.7006 1.2610 0.0610  -0.3721 -0.1458 61  SER   G OG  
11652 N  N   . TYR   G  71  ? 1.7866 0.4261 1.2531 0.1308  -0.4239 -0.0309 62  TYR   G N   
11653 C  CA  . TYR   G  71  ? 1.7524 0.4970 1.2496 0.1236  -0.4147 -0.1073 62  TYR   G CA  
11654 C  C   . TYR   G  71  ? 1.7459 0.4161 1.2324 0.0916  -0.4084 -0.1271 62  TYR   G C   
11655 O  O   . TYR   G  71  ? 1.7538 0.2865 1.1027 0.1314  -0.4472 -0.1297 62  TYR   G O   
11656 C  CB  . TYR   G  71  ? 1.7875 0.5116 1.2536 0.0956  -0.4105 -0.1933 62  TYR   G CB  
11657 C  CG  . TYR   G  71  ? 1.7968 0.6361 1.2061 0.1590  -0.4155 -0.2511 62  TYR   G CG  
11658 C  CD1 . TYR   G  71  ? 1.8388 0.7674 1.2394 0.1969  -0.3788 -0.2443 62  TYR   G CD1 
11659 C  CD2 . TYR   G  71  ? 1.7886 0.6309 1.2080 0.1872  -0.4147 -0.2495 62  TYR   G CD2 
11660 C  CE1 . TYR   G  71  ? 1.8343 0.8052 1.2393 0.1849  -0.3835 -0.1669 62  TYR   G CE1 
11661 C  CE2 . TYR   G  71  ? 1.8030 0.6035 1.2480 0.1840  -0.4103 -0.2278 62  TYR   G CE2 
11662 C  CZ  . TYR   G  71  ? 1.7958 0.6601 1.2404 0.1669  -0.3887 -0.1892 62  TYR   G CZ  
11663 O  OH  . TYR   G  71  ? 1.7574 0.4535 1.4276 0.0868  -0.3232 -0.1327 62  TYR   G OH  
11664 N  N   . ILE   G  72  ? 1.7925 0.4580 1.2476 0.0255  -0.3770 -0.0934 63  ILE   G N   
11665 C  CA  . ILE   G  72  ? 1.8063 0.4104 1.2615 0.0048  -0.3494 -0.0822 63  ILE   G CA  
11666 C  C   . ILE   G  72  ? 1.8443 0.3272 1.2784 0.0250  -0.2495 -0.0663 63  ILE   G C   
11667 O  O   . ILE   G  72  ? 1.9077 0.0914 1.3386 0.0297  -0.1871 -0.0544 63  ILE   G O   
11668 C  CB  . ILE   G  72  ? 1.8388 0.4522 1.2648 0.0291  -0.3592 -0.0566 63  ILE   G CB  
11669 C  CG1 . ILE   G  72  ? 1.8528 0.5084 1.1801 0.0212  -0.3900 -0.0994 63  ILE   G CG1 
11670 C  CG2 . ILE   G  72  ? 1.8607 0.3639 1.2577 -0.0086 -0.3908 -0.0243 63  ILE   G CG2 
11671 C  CD1 . ILE   G  72  ? 1.8839 0.5603 1.1743 0.0482  -0.3968 -0.0784 63  ILE   G CD1 
11672 N  N   . PHE   G  73  ? 1.8256 0.3630 1.2699 -0.0113 -0.2345 -0.0800 64  PHE   G N   
11673 C  CA  . PHE   G  73  ? 1.7761 0.4639 1.2307 -0.0558 -0.2853 -0.1019 64  PHE   G CA  
11674 C  C   . PHE   G  73  ? 1.8148 0.3992 1.2285 -0.0699 -0.2817 -0.0916 64  PHE   G C   
11675 O  O   . PHE   G  73  ? 1.7921 0.4022 1.1916 -0.0597 -0.3295 -0.0969 64  PHE   G O   
11676 C  CB  . PHE   G  73  ? 1.6868 0.5065 1.2214 -0.0596 -0.3079 -0.1287 64  PHE   G CB  
11677 C  CG  . PHE   G  73  ? 1.6350 0.5543 1.2027 -0.0657 -0.3257 -0.1386 64  PHE   G CG  
11678 C  CD1 . PHE   G  73  ? 1.6355 0.5956 1.2405 -0.0796 -0.3024 -0.1490 64  PHE   G CD1 
11679 C  CD2 . PHE   G  73  ? 1.5984 0.5638 1.2028 -0.0812 -0.3245 -0.1851 64  PHE   G CD2 
11680 C  CE1 . PHE   G  73  ? 1.6119 0.5910 1.2565 -0.0805 -0.2913 -0.1919 64  PHE   G CE1 
11681 C  CE2 . PHE   G  73  ? 1.6003 0.5994 1.2335 -0.0580 -0.2929 -0.1849 64  PHE   G CE2 
11682 C  CZ  . PHE   G  73  ? 1.6061 0.5866 1.2502 -0.0686 -0.2830 -0.1965 64  PHE   G CZ  
11683 N  N   . CYS   G  74  ? 1.9088 0.3944 1.1994 -0.0722 -0.2676 -0.0738 65  CYS   G N   
11684 C  CA  . CYS   G  74  ? 1.8858 0.3275 1.2136 -0.1316 -0.2482 -0.0916 65  CYS   G CA  
11685 C  C   . CYS   G  74  ? 1.8626 0.2891 1.2222 -0.0907 -0.2427 -0.0994 65  CYS   G C   
11686 O  O   . CYS   G  74  ? 1.7346 0.5386 1.2320 -0.0874 -0.2489 -0.0660 65  CYS   G O   
11687 C  CB  . CYS   G  74  ? 1.9027 0.4140 1.2713 -0.1720 -0.2114 -0.0548 65  CYS   G CB  
11688 S  SG  . CYS   G  74  ? 1.9025 0.4786 1.2367 -0.2693 -0.1346 0.0024  65  CYS   G SG  
11689 N  N   . ILE   G  75  ? 1.8131 0.1414 1.1994 -0.1118 -0.2784 -0.1574 66  ILE   G N   
11690 C  CA  . ILE   G  75  ? 1.7952 0.3221 1.1946 -0.1108 -0.3174 -0.1761 66  ILE   G CA  
11691 C  C   . ILE   G  75  ? 1.7856 0.3422 1.1795 -0.0783 -0.3684 -0.2474 66  ILE   G C   
11692 O  O   . ILE   G  75  ? 1.8036 0.2893 1.2602 -0.0975 -0.3431 -0.2863 66  ILE   G O   
11693 C  CB  . ILE   G  75  ? 1.7614 0.3120 1.1789 -0.1045 -0.3455 -0.1648 66  ILE   G CB  
11694 C  CG1 . ILE   G  75  ? 1.7309 0.3366 1.2039 -0.0388 -0.3646 -0.1558 66  ILE   G CG1 
11695 C  CG2 . ILE   G  75  ? 1.7355 0.2780 1.1512 -0.0914 -0.3258 -0.1142 66  ILE   G CG2 
11696 C  CD1 . ILE   G  75  ? 1.7425 0.4379 1.2002 -0.0274 -0.3832 -0.1376 66  ILE   G CD1 
11697 N  N   . SER   G  76  ? 1.8264 0.3176 1.1546 -0.0483 -0.3702 -0.2485 67  SER   G N   
11698 C  CA  . SER   G  76  ? 1.8639 0.2597 1.2386 -0.1396 -0.3939 -0.2931 67  SER   G CA  
11699 C  C   . SER   G  76  ? 1.8930 0.3119 1.2391 -0.1150 -0.3755 -0.3042 67  SER   G C   
11700 O  O   . SER   G  76  ? 1.9403 0.3631 1.3348 0.0080  -0.3072 -0.3389 67  SER   G O   
11701 C  CB  . SER   G  76  ? 1.8036 0.2146 1.2082 -0.1546 -0.4450 -0.2736 67  SER   G CB  
11702 O  OG  . SER   G  76  ? 1.8397 0.1456 1.2591 -0.1281 -0.4698 -0.2383 67  SER   G OG  
11703 N  N   . ARG   G  77  ? 1.9028 0.3502 1.2736 -0.0862 -0.3735 -0.2657 68  ARG   G N   
11704 C  CA  . ARG   G  77  ? 1.8949 0.4035 1.2843 -0.0871 -0.3743 -0.2487 68  ARG   G CA  
11705 C  C   . ARG   G  77  ? 1.8830 0.2990 1.2704 -0.0490 -0.3594 -0.2573 68  ARG   G C   
11706 O  O   . ARG   G  77  ? 1.8973 0.2659 1.3090 -0.0984 -0.3582 -0.3275 68  ARG   G O   
11707 C  CB  . ARG   G  77  ? 1.9516 0.4182 1.3971 -0.0541 -0.3606 -0.2852 68  ARG   G CB  
11708 C  CG  . ARG   G  77  ? 2.0499 0.5371 1.4406 -0.0742 -0.3481 -0.2350 68  ARG   G CG  
11709 C  CD  . ARG   G  77  ? 2.1736 0.5328 1.5845 -0.0651 -0.3574 -0.2437 68  ARG   G CD  
11710 N  NE  . ARG   G  77  ? 2.1502 0.6465 1.7413 -0.0991 -0.3603 -0.1602 68  ARG   G NE  
11711 C  CZ  . ARG   G  77  ? 2.3149 0.6383 1.9264 -0.1672 -0.2847 -0.1595 68  ARG   G CZ  
11712 N  NH1 . ARG   G  77  ? 2.2246 0.9169 1.9990 -0.1204 -0.2614 -0.1046 68  ARG   G NH1 
11713 N  NH2 . ARG   G  77  ? 2.2923 0.7768 2.0544 -0.2158 -0.2625 -0.0657 68  ARG   G NH2 
11714 N  N   . THR   G  78  ? 1.8830 0.3371 1.2434 0.0193  -0.3559 -0.2200 69  THR   G N   
11715 C  CA  . THR   G  78  ? 1.8417 0.3548 1.2540 0.0440  -0.3306 -0.1885 69  THR   G CA  
11716 C  C   . THR   G  78  ? 1.8285 0.3841 1.2558 0.0708  -0.3394 -0.1168 69  THR   G C   
11717 O  O   . THR   G  78  ? 1.8504 0.2132 1.4127 0.0547  -0.3164 -0.0994 69  THR   G O   
11718 C  CB  . THR   G  78  ? 1.8650 0.3168 1.2435 0.0660  -0.3383 -0.1940 69  THR   G CB  
11719 O  OG1 . THR   G  78  ? 1.8514 0.3295 1.2277 0.1307  -0.3111 -0.1916 69  THR   G OG1 
11720 C  CG2 . THR   G  78  ? 1.8965 0.3216 1.2943 0.0808  -0.3229 -0.1835 69  THR   G CG2 
11721 N  N   . ILE   G  79  ? 1.7987 0.3892 1.1955 0.0730  -0.3021 -0.1183 70  ILE   G N   
11722 C  CA  . ILE   G  79  ? 1.7708 0.4011 1.1812 0.0993  -0.3011 -0.1063 70  ILE   G CA  
11723 C  C   . ILE   G  79  ? 1.7366 0.3731 1.1994 0.0559  -0.2863 -0.0939 70  ILE   G C   
11724 O  O   . ILE   G  79  ? 1.8409 0.1055 1.1797 -0.0007 -0.3017 -0.1223 70  ILE   G O   
11725 C  CB  . ILE   G  79  ? 1.7403 0.4452 1.1832 0.1738  -0.3131 -0.0708 70  ILE   G CB  
11726 C  CG1 . ILE   G  79  ? 1.7457 0.5560 1.1686 0.2064  -0.3153 -0.0492 70  ILE   G CG1 
11727 C  CG2 . ILE   G  79  ? 1.7284 0.4623 1.1699 0.1888  -0.3202 -0.0591 70  ILE   G CG2 
11728 C  CD1 . ILE   G  79  ? 1.7140 0.6057 1.1514 0.2320  -0.3438 0.0191  70  ILE   G CD1 
11729 N  N   . GLY   G  80  ? 1.7748 0.4054 1.1925 0.0516  -0.2832 -0.1227 71  GLY   G N   
11730 C  CA  . GLY   G  80  ? 1.7331 0.5059 1.1513 0.0814  -0.2730 -0.0875 71  GLY   G CA  
11731 C  C   . GLY   G  80  ? 1.6873 0.5809 1.0807 0.0842  -0.2877 -0.0475 71  GLY   G C   
11732 O  O   . GLY   G  80  ? 1.6625 0.6446 0.9516 0.1096  -0.3191 -0.0184 71  GLY   G O   
11733 N  N   . MET   G  81  ? 1.7024 0.5268 1.1068 0.0737  -0.2923 -0.0325 72  MET   G N   
11734 C  CA  . MET   G  81  ? 1.7233 0.4203 1.1866 0.0061  -0.2730 -0.0787 72  MET   G CA  
11735 C  C   . MET   G  81  ? 1.7380 0.4499 1.1992 -0.0131 -0.2771 -0.1334 72  MET   G C   
11736 O  O   . MET   G  81  ? 1.7862 0.3544 1.3267 -0.0570 -0.2393 -0.1440 72  MET   G O   
11737 C  CB  . MET   G  81  ? 1.6995 0.3600 1.1899 0.0101  -0.2589 -0.0865 72  MET   G CB  
11738 C  CG  . MET   G  81  ? 1.6821 0.3566 1.2252 -0.0221 -0.2597 -0.0727 72  MET   G CG  
11739 S  SD  . MET   G  81  ? 1.6681 0.2867 1.2323 -0.0682 -0.2498 -0.0625 72  MET   G SD  
11740 C  CE  . MET   G  81  ? 1.6498 0.3568 1.2943 -0.0434 -0.2544 -0.0623 72  MET   G CE  
11741 N  N   . VAL   G  82  ? 1.7675 0.4876 1.1657 -0.0414 -0.3131 -0.1460 73  VAL   G N   
11742 C  CA  . VAL   G  82  ? 1.8280 0.3643 1.1403 -0.0648 -0.3327 -0.0859 73  VAL   G CA  
11743 C  C   . VAL   G  82  ? 1.8445 0.3981 1.1689 -0.0742 -0.3298 -0.0507 73  VAL   G C   
11744 O  O   . VAL   G  82  ? 1.8718 0.4417 1.2360 -0.0614 -0.2826 -0.0467 73  VAL   G O   
11745 C  CB  . VAL   G  82  ? 1.8485 0.2244 1.2044 -0.0902 -0.3108 -0.1134 73  VAL   G CB  
11746 C  CG1 . VAL   G  82  ? 1.8386 0.1927 1.1681 -0.0916 -0.3257 -0.1208 73  VAL   G CG1 
11747 C  CG2 . VAL   G  82  ? 1.8487 0.2846 1.2255 -0.0638 -0.2990 -0.1054 73  VAL   G CG2 
11748 N  N   . VAL   G  83  ? 1.8207 0.4871 1.1417 -0.0806 -0.3523 -0.0281 74  VAL   G N   
11749 C  CA  . VAL   G  83  ? 1.8121 0.6023 1.1618 -0.0692 -0.3651 0.0259  74  VAL   G CA  
11750 C  C   . VAL   G  83  ? 1.8841 0.6102 1.0588 -0.0942 -0.3925 0.0335  74  VAL   G C   
11751 O  O   . VAL   G  83  ? 1.9172 0.9162 1.0390 -0.1507 -0.3728 0.0973  74  VAL   G O   
11752 C  CB  . VAL   G  83  ? 1.7585 0.5657 1.1692 -0.0379 -0.3521 0.0659  74  VAL   G CB  
11753 C  CG1 . VAL   G  83  ? 1.7646 0.5968 1.1805 -0.0113 -0.3266 0.0840  74  VAL   G CG1 
11754 C  CG2 . VAL   G  83  ? 1.7320 0.5760 1.1150 -0.0547 -0.3649 0.0412  74  VAL   G CG2 
11755 N  N   . ASN   G  84  ? 1.8961 0.6064 1.1246 -0.1214 -0.3994 0.0410  75  ASN   G N   
11756 C  CA  . ASN   G  84  ? 1.8734 0.6100 1.2631 -0.1067 -0.4069 0.0002  75  ASN   G CA  
11757 C  C   . ASN   G  84  ? 1.7459 0.4786 1.3634 -0.0138 -0.3759 0.0083  75  ASN   G C   
11758 O  O   . ASN   G  84  ? 1.7918 0.3523 1.3569 0.0872  -0.3610 0.0375  75  ASN   G O   
11759 C  CB  . ASN   G  84  ? 1.9352 0.6539 1.1802 -0.1499 -0.4865 -0.0555 75  ASN   G CB  
11760 C  CG  . ASN   G  84  ? 2.0425 0.6975 1.1502 -0.2034 -0.4956 -0.1201 75  ASN   G CG  
11761 O  OD1 . ASN   G  84  ? 2.0022 0.6753 1.0847 -0.2981 -0.6319 -0.1230 75  ASN   G OD1 
11762 N  ND2 . ASN   G  84  ? 2.1309 0.7472 1.1688 -0.1779 -0.4420 -0.1562 75  ASN   G ND2 
11763 N  N   . GLY   G  85  ? 1.7546 0.4748 1.4617 -0.0223 -0.2995 -0.0389 76  GLY   G N   
11764 C  CA  . GLY   G  85  ? 1.6574 0.4562 1.4188 -0.0419 -0.2477 -0.0640 76  GLY   G CA  
11765 C  C   . GLY   G  85  ? 1.6494 0.3759 1.3732 -0.0182 -0.2177 -0.1132 76  GLY   G C   
11766 O  O   . GLY   G  85  ? 1.6467 0.2554 1.3748 -0.0361 -0.1702 -0.1765 76  GLY   G O   
11767 N  N   . PRO   G  86  ? 1.6064 0.2922 1.3237 -0.0102 -0.1706 -0.1142 77  PRO   G N   
11768 C  CA  . PRO   G  86  ? 1.5747 0.4144 1.3120 0.0259  -0.1688 -0.1021 77  PRO   G CA  
11769 C  C   . PRO   G  86  ? 1.5855 0.4208 1.2865 0.0435  -0.1362 -0.0470 77  PRO   G C   
11770 O  O   . PRO   G  86  ? 1.6006 0.4456 1.2263 0.0641  -0.1610 -0.0443 77  PRO   G O   
11771 C  CB  . PRO   G  86  ? 1.5572 0.2854 1.3295 0.0245  -0.1581 -0.1019 77  PRO   G CB  
11772 C  CG  . PRO   G  86  ? 1.5674 0.2993 1.3293 0.0112  -0.1651 -0.0991 77  PRO   G CG  
11773 C  CD  . PRO   G  86  ? 1.5799 0.2519 1.3360 0.0148  -0.1787 -0.1075 77  PRO   G CD  
11774 N  N   . ILE   G  87  ? 1.6030 0.5669 1.2866 0.0836  -0.1091 0.0121  78  ILE   G N   
11775 C  CA  . ILE   G  87  ? 1.6502 0.5325 1.2869 0.1050  -0.1275 -0.0492 78  ILE   G CA  
11776 C  C   . ILE   G  87  ? 1.6327 0.5990 1.2293 0.0852  -0.1653 0.0117  78  ILE   G C   
11777 O  O   . ILE   G  87  ? 1.6264 0.6670 1.3777 0.1607  -0.1436 0.0112  78  ILE   G O   
11778 C  CB  . ILE   G  87  ? 1.6911 0.6133 1.2969 0.1027  -0.1128 -0.0594 78  ILE   G CB  
11779 C  CG1 . ILE   G  87  ? 1.7105 0.6144 1.2815 0.1465  -0.1513 -0.0827 78  ILE   G CG1 
11780 C  CG2 . ILE   G  87  ? 1.6990 0.6360 1.3472 0.1006  -0.1295 -0.0235 78  ILE   G CG2 
11781 C  CD1 . ILE   G  87  ? 1.7175 0.6440 1.2642 0.1444  -0.1634 -0.0992 78  ILE   G CD1 
11782 N  N   . PRO   G  88  ? 1.6621 0.5184 1.2156 0.1210  -0.1472 0.0108  79  PRO   G N   
11783 C  CA  . PRO   G  88  ? 1.6448 0.5889 1.1692 0.1241  -0.1758 0.0284  79  PRO   G CA  
11784 C  C   . PRO   G  88  ? 1.6189 0.6559 1.0907 0.0894  -0.1972 0.0311  79  PRO   G C   
11785 O  O   . PRO   G  88  ? 1.6474 0.6990 1.0058 0.1881  -0.2338 0.0346  79  PRO   G O   
11786 C  CB  . PRO   G  88  ? 1.6521 0.5623 1.1723 0.1385  -0.1736 0.0025  79  PRO   G CB  
11787 C  CG  . PRO   G  88  ? 1.6756 0.5702 1.2256 0.1492  -0.1637 -0.0254 79  PRO   G CG  
11788 C  CD  . PRO   G  88  ? 1.6695 0.5342 1.2009 0.1458  -0.1496 -0.0416 79  PRO   G CD  
11789 N  N   . ASP   G  89  ? 1.6047 0.6338 1.1170 0.0911  -0.1956 0.0032  80  ASP   G N   
11790 C  CA  . ASP   G  89  ? 1.5918 0.6530 1.1381 0.0618  -0.1942 -0.0151 80  ASP   G CA  
11791 C  C   . ASP   G  89  ? 1.5673 0.6150 1.1485 0.0225  -0.1729 0.0181  80  ASP   G C   
11792 O  O   . ASP   G  89  ? 1.5094 0.5999 1.1499 -0.0281 -0.1623 0.0101  80  ASP   G O   
11793 C  CB  . ASP   G  89  ? 1.5933 0.6651 1.1403 0.0545  -0.2020 -0.0162 80  ASP   G CB  
11794 C  CG  . ASP   G  89  ? 1.5924 0.7740 1.1255 0.0260  -0.2558 -0.0262 80  ASP   G CG  
11795 O  OD1 . ASP   G  89  ? 1.6260 0.7892 1.1212 0.0023  -0.2789 -0.0511 80  ASP   G OD1 
11796 O  OD2 . ASP   G  89  ? 1.6207 0.9019 1.1057 -0.0268 -0.2423 0.0358  80  ASP   G OD2 
11797 N  N   . ALA   G  90  ? 1.5951 0.5775 1.1510 0.0204  -0.1402 0.0108  81  ALA   G N   
11798 C  CA  . ALA   G  90  ? 1.6006 0.5253 1.1961 0.0127  -0.1613 -0.0011 81  ALA   G CA  
11799 C  C   . ALA   G  90  ? 1.5881 0.5082 1.2042 0.0550  -0.1549 -0.0338 81  ALA   G C   
11800 O  O   . ALA   G  90  ? 1.5978 0.3927 1.2193 0.0211  -0.1573 -0.0261 81  ALA   G O   
11801 C  CB  . ALA   G  90  ? 1.6149 0.5436 1.2112 -0.0246 -0.1721 -0.0251 81  ALA   G CB  
11802 N  N   . ARG   G  91  ? 1.6154 0.4356 1.2183 0.0257  -0.1702 -0.0619 82  ARG   G N   
11803 C  CA  . ARG   G  91  ? 1.6727 0.4191 1.2107 0.0391  -0.1537 -0.0674 82  ARG   G CA  
11804 C  C   . ARG   G  91  ? 1.7066 0.4721 1.2169 0.0079  -0.1940 -0.1150 82  ARG   G C   
11805 O  O   . ARG   G  91  ? 1.6790 0.4863 1.1799 0.0010  -0.1834 -0.2063 82  ARG   G O   
11806 C  CB  . ARG   G  91  ? 1.6831 0.3833 1.2591 0.0326  -0.1272 -0.0223 82  ARG   G CB  
11807 C  CG  . ARG   G  91  ? 1.6655 0.3997 1.2711 0.0280  -0.0885 -0.0192 82  ARG   G CG  
11808 C  CD  . ARG   G  91  ? 1.6578 0.4445 1.2929 0.0206  -0.0843 -0.0224 82  ARG   G CD  
11809 N  NE  . ARG   G  91  ? 1.6692 0.5252 1.2937 0.0125  -0.0888 -0.0479 82  ARG   G NE  
11810 C  CZ  . ARG   G  91  ? 1.6290 0.5959 1.3435 0.0132  -0.0873 -0.0306 82  ARG   G CZ  
11811 N  NH1 . ARG   G  91  ? 1.6134 0.5507 1.3733 -0.0184 -0.1073 -0.0316 82  ARG   G NH1 
11812 N  NH2 . ARG   G  91  ? 1.6902 0.7315 1.3503 -0.0068 -0.0656 -0.0145 82  ARG   G NH2 
11813 N  N   . ASN   G  92  ? 1.7445 0.4023 1.1919 0.0166  -0.2249 -0.1683 83  ASN   G N   
11814 C  CA  . ASN   G  92  ? 1.6965 0.4536 1.1859 -0.0063 -0.2911 -0.2062 83  ASN   G CA  
11815 C  C   . ASN   G  92  ? 1.6886 0.4706 1.2082 0.0055  -0.3135 -0.1730 83  ASN   G C   
11816 O  O   . ASN   G  92  ? 1.6993 0.4690 1.2050 0.0268  -0.2858 -0.1592 83  ASN   G O   
11817 C  CB  . ASN   G  92  ? 1.7115 0.3999 1.2003 -0.0123 -0.3298 -0.2449 83  ASN   G CB  
11818 C  CG  . ASN   G  92  ? 1.6781 0.4009 1.2038 -0.0640 -0.3742 -0.3115 83  ASN   G CG  
11819 O  OD1 . ASN   G  92  ? 1.6566 0.6190 1.2200 -0.0128 -0.3850 -0.3057 83  ASN   G OD1 
11820 N  ND2 . ASN   G  92  ? 1.6864 0.2700 1.2250 -0.0846 -0.3569 -0.3571 83  ASN   G ND2 
11821 N  N   . ALA   G  93  ? 1.5855 0.5083 1.2586 0.0317  -0.3171 -0.1461 84  ALA   G N   
11822 C  CA  . ALA   G  93  ? 1.5843 0.4939 1.2745 0.0363  -0.3037 -0.1382 84  ALA   G CA  
11823 C  C   . ALA   G  93  ? 1.5645 0.4639 1.2962 0.0415  -0.2757 -0.1439 84  ALA   G C   
11824 O  O   . ALA   G  93  ? 1.5847 0.3598 1.3091 0.0295  -0.3022 -0.1281 84  ALA   G O   
11825 C  CB  . ALA   G  93  ? 1.5474 0.4927 1.2934 0.0626  -0.2962 -0.1717 84  ALA   G CB  
11826 N  N   . ALA   G  94  ? 1.5902 0.4295 1.2571 0.0604  -0.3040 -0.0998 85  ALA   G N   
11827 C  CA  . ALA   G  94  ? 1.5798 0.4621 1.2513 0.0981  -0.3339 -0.0932 85  ALA   G CA  
11828 C  C   . ALA   G  94  ? 1.5763 0.4839 1.2490 0.0591  -0.3540 -0.0753 85  ALA   G C   
11829 O  O   . ALA   G  94  ? 1.4852 0.4830 1.2849 0.0293  -0.3849 -0.1179 85  ALA   G O   
11830 C  CB  . ALA   G  94  ? 1.5998 0.4152 1.2540 0.1216  -0.3382 -0.1087 85  ALA   G CB  
11831 N  N   . LEU   G  95  ? 1.5707 0.4713 1.2004 0.0640  -0.3335 -0.0501 86  LEU   G N   
11832 C  CA  . LEU   G  95  ? 1.5885 0.4280 1.1508 0.1155  -0.2904 -0.0653 86  LEU   G CA  
11833 C  C   . LEU   G  95  ? 1.6266 0.5252 1.1092 0.0544  -0.2511 -0.0291 86  LEU   G C   
11834 O  O   . LEU   G  95  ? 1.6924 0.5892 1.1818 0.1617  -0.2488 -0.0214 86  LEU   G O   
11835 C  CB  . LEU   G  95  ? 1.5886 0.4047 1.0983 0.1307  -0.2817 -0.0667 86  LEU   G CB  
11836 C  CG  . LEU   G  95  ? 1.6068 0.3840 1.1217 0.1498  -0.2631 -0.0896 86  LEU   G CG  
11837 C  CD1 . LEU   G  95  ? 1.5912 0.4142 1.1128 0.1112  -0.2770 -0.0754 86  LEU   G CD1 
11838 C  CD2 . LEU   G  95  ? 1.6001 0.3396 1.1420 0.1473  -0.2473 -0.1047 86  LEU   G CD2 
11839 N  N   . ARG   G  96  ? 1.5884 0.3963 1.1201 0.0716  -0.2557 -0.0821 87  ARG   G N   
11840 C  CA  . ARG   G  96  ? 1.5837 0.3883 1.1171 0.0600  -0.2606 -0.1082 87  ARG   G CA  
11841 C  C   . ARG   G  96  ? 1.5815 0.3518 1.0936 0.0493  -0.2594 -0.0990 87  ARG   G C   
11842 O  O   . ARG   G  96  ? 1.5340 0.5019 0.9902 0.1487  -0.2664 -0.1099 87  ARG   G O   
11843 C  CB  . ARG   G  96  ? 1.5861 0.4134 1.1163 0.0398  -0.2228 -0.1090 87  ARG   G CB  
11844 C  CG  . ARG   G  96  ? 1.5931 0.4468 1.1385 0.0492  -0.2110 -0.1308 87  ARG   G CG  
11845 C  CD  . ARG   G  96  ? 1.5944 0.4869 1.1503 0.0232  -0.2438 -0.1300 87  ARG   G CD  
11846 N  NE  . ARG   G  96  ? 1.6071 0.5361 1.1164 0.0174  -0.2640 -0.1043 87  ARG   G NE  
11847 C  CZ  . ARG   G  96  ? 1.5864 0.4919 1.1473 0.0461  -0.2630 -0.0911 87  ARG   G CZ  
11848 N  NH1 . ARG   G  96  ? 1.5716 0.5198 1.1783 0.0500  -0.2548 -0.0451 87  ARG   G NH1 
11849 N  NH2 . ARG   G  96  ? 1.6272 0.5114 1.1467 0.0330  -0.2544 -0.1076 87  ARG   G NH2 
11850 N  N   . ALA   G  97  ? 1.5845 0.3538 1.1094 0.0265  -0.2652 -0.0938 88  ALA   G N   
11851 C  CA  . ALA   G  97  ? 1.5827 0.4475 1.1235 0.0451  -0.2539 -0.0982 88  ALA   G CA  
11852 C  C   . ALA   G  97  ? 1.6015 0.4577 1.1461 -0.0137 -0.2297 -0.1055 88  ALA   G C   
11853 O  O   . ALA   G  97  ? 1.5352 0.6194 1.2146 0.0057  -0.2212 -0.1224 88  ALA   G O   
11854 C  CB  . ALA   G  97  ? 1.6125 0.4585 1.1103 0.0447  -0.2418 -0.0983 88  ALA   G CB  
11855 N  N   . LYS   G  98  ? 1.6269 0.5003 1.1457 -0.0364 -0.2171 -0.0980 89  LYS   G N   
11856 C  CA  . LYS   G  98  ? 1.6979 0.4984 1.1410 0.0105  -0.2047 -0.0698 89  LYS   G CA  
11857 C  C   . LYS   G  98  ? 1.7361 0.5275 1.1266 0.0192  -0.2467 -0.0805 89  LYS   G C   
11858 O  O   . LYS   G  98  ? 1.7212 0.6117 1.1392 0.0954  -0.1953 -0.2412 89  LYS   G O   
11859 C  CB  . LYS   G  98  ? 1.7117 0.5204 1.1753 0.0141  -0.1804 -0.0112 89  LYS   G CB  
11860 C  CG  . LYS   G  98  ? 1.7176 0.4709 1.1753 -0.0086 -0.1563 0.0027  89  LYS   G CG  
11861 C  CD  . LYS   G  98  ? 1.7512 0.4412 1.1726 -0.0264 -0.1063 0.0238  89  LYS   G CD  
11862 C  CE  . LYS   G  98  ? 1.7958 0.4241 1.1544 -0.0245 -0.0644 0.0526  89  LYS   G CE  
11863 N  NZ  . LYS   G  98  ? 1.8050 0.4665 1.2338 -0.0421 -0.0270 0.1243  89  LYS   G NZ  
11864 N  N   . ALA   G  99  ? 1.7592 0.3808 1.0935 0.0002  -0.2569 -0.1241 90  ALA   G N   
11865 C  CA  . ALA   G  99  ? 1.7421 0.4575 1.0457 0.0103  -0.3183 -0.1086 90  ALA   G CA  
11866 C  C   . ALA   G  99  ? 1.7213 0.5110 1.0627 -0.0367 -0.3193 -0.0824 90  ALA   G C   
11867 O  O   . ALA   G  99  ? 1.7732 0.6197 1.1110 0.1056  -0.2728 -0.1077 90  ALA   G O   
11868 C  CB  . ALA   G  99  ? 1.7424 0.4455 1.0730 0.0158  -0.3090 -0.0733 90  ALA   G CB  
11869 N  N   . GLU   G  100 ? 1.7676 0.3937 1.0298 0.0029  -0.3333 -0.1413 91  GLU   G N   
11870 C  CA  . GLU   G  100 ? 1.7871 0.4858 1.0488 0.0233  -0.3163 -0.1752 91  GLU   G CA  
11871 C  C   . GLU   G  100 ? 1.7920 0.4445 1.1134 0.0352  -0.3532 -0.2238 91  GLU   G C   
11872 O  O   . GLU   G  100 ? 1.8181 0.6625 1.0147 -0.0046 -0.3782 -0.4171 91  GLU   G O   
11873 C  CB  . GLU   G  100 ? 1.7529 0.5718 1.0829 -0.0405 -0.2689 -0.1219 91  GLU   G CB  
11874 C  CG  . GLU   G  100 ? 1.7087 0.6635 1.1326 -0.0075 -0.2454 -0.0702 91  GLU   G CG  
11875 C  CD  . GLU   G  100 ? 1.7145 0.6958 1.1494 -0.0075 -0.2072 -0.0736 91  GLU   G CD  
11876 O  OE1 . GLU   G  100 ? 1.7317 0.6990 1.3595 -0.0227 -0.1080 -0.0885 91  GLU   G OE1 
11877 O  OE2 . GLU   G  100 ? 1.6603 0.7381 1.1632 0.0416  -0.1501 -0.0136 91  GLU   G OE2 
11878 N  N   . ALA   G  101 ? 1.8141 0.3958 1.1210 0.0482  -0.3299 -0.2237 92  ALA   G N   
11879 C  CA  . ALA   G  101 ? 1.8093 0.3532 1.1873 0.0366  -0.3349 -0.1946 92  ALA   G CA  
11880 C  C   . ALA   G  101 ? 1.7703 0.3167 1.2450 0.1039  -0.3675 -0.1200 92  ALA   G C   
11881 O  O   . ALA   G  101 ? 1.8929 0.0670 1.3153 0.0453  -0.3374 -0.1110 92  ALA   G O   
11882 C  CB  . ALA   G  101 ? 1.8111 0.4140 1.2048 0.0416  -0.3490 -0.2347 92  ALA   G CB  
11883 N  N   . ALA   G  102 ? 1.7984 0.2480 1.2267 0.0417  -0.3675 -0.0873 93  ALA   G N   
11884 C  CA  . ALA   G  102 ? 1.7874 0.2626 1.2010 0.0284  -0.3530 -0.1085 93  ALA   G CA  
11885 C  C   . ALA   G  102 ? 1.7950 0.2662 1.2253 -0.0015 -0.3452 -0.1433 93  ALA   G C   
11886 O  O   . ALA   G  102 ? 1.7968 0.2048 1.1713 -0.0503 -0.3397 -0.2475 93  ALA   G O   
11887 C  CB  . ALA   G  102 ? 1.7829 0.3007 1.1896 0.0371  -0.3658 -0.0781 93  ALA   G CB  
11888 N  N   . GLU   G  103 ? 1.7622 0.2473 1.2351 0.0000  -0.3228 -0.1411 94  GLU   G N   
11889 C  CA  . GLU   G  103 ? 1.7803 0.2860 1.2657 0.0044  -0.3207 -0.1804 94  GLU   G CA  
11890 C  C   . GLU   G  103 ? 1.7772 0.3361 1.2882 -0.0125 -0.3364 -0.1647 94  GLU   G C   
11891 O  O   . GLU   G  103 ? 1.7984 0.3922 1.3591 0.0384  -0.3106 -0.1841 94  GLU   G O   
11892 C  CB  . GLU   G  103 ? 1.7574 0.3477 1.3136 0.0194  -0.3401 -0.1427 94  GLU   G CB  
11893 C  CG  . GLU   G  103 ? 1.7863 0.4602 1.3601 0.0569  -0.2937 -0.1634 94  GLU   G CG  
11894 C  CD  . GLU   G  103 ? 1.8314 0.5939 1.4243 0.0515  -0.2605 -0.0769 94  GLU   G CD  
11895 O  OE1 . GLU   G  103 ? 1.7481 0.9153 1.5576 0.0574  -0.2458 -0.0516 94  GLU   G OE1 
11896 O  OE2 . GLU   G  103 ? 1.8472 0.6012 1.5323 0.1133  -0.1796 -0.1312 94  GLU   G OE2 
11897 N  N   . PHE   G  104 ? 1.7456 0.3068 1.2477 0.0153  -0.3435 -0.1393 95  PHE   G N   
11898 C  CA  . PHE   G  104 ? 1.7481 0.3307 1.2027 0.0315  -0.3320 -0.1405 95  PHE   G CA  
11899 C  C   . PHE   G  104 ? 1.7969 0.2934 1.1839 0.0292  -0.3050 -0.1705 95  PHE   G C   
11900 O  O   . PHE   G  104 ? 1.8054 0.3468 1.1980 0.0227  -0.2855 -0.2031 95  PHE   G O   
11901 C  CB  . PHE   G  104 ? 1.7126 0.2953 1.1938 0.0366  -0.3365 -0.1062 95  PHE   G CB  
11902 C  CG  . PHE   G  104 ? 1.7141 0.2856 1.1807 0.0054  -0.3225 -0.0991 95  PHE   G CG  
11903 C  CD1 . PHE   G  104 ? 1.7285 0.3184 1.2013 0.0068  -0.3356 -0.0874 95  PHE   G CD1 
11904 C  CD2 . PHE   G  104 ? 1.7314 0.2630 1.1421 0.0306  -0.3349 -0.0927 95  PHE   G CD2 
11905 C  CE1 . PHE   G  104 ? 1.7312 0.3299 1.2164 0.0241  -0.3271 -0.0869 95  PHE   G CE1 
11906 C  CE2 . PHE   G  104 ? 1.7345 0.2889 1.1447 0.0244  -0.3295 -0.0951 95  PHE   G CE2 
11907 C  CZ  . PHE   G  104 ? 1.7326 0.3112 1.1914 0.0327  -0.3445 -0.0869 95  PHE   G CZ  
11908 N  N   . ARG   G  105 ? 1.8226 0.2816 1.1864 0.0272  -0.2877 -0.1733 96  ARG   G N   
11909 C  CA  . ARG   G  105 ? 1.8496 0.3272 1.2032 0.0339  -0.2699 -0.1293 96  ARG   G CA  
11910 C  C   . ARG   G  105 ? 1.8016 0.3205 1.1844 0.0528  -0.2959 -0.1119 96  ARG   G C   
11911 O  O   . ARG   G  105 ? 1.8444 0.2617 1.1801 0.0452  -0.3023 -0.1235 96  ARG   G O   
11912 C  CB  . ARG   G  105 ? 1.8884 0.3565 1.2152 0.0340  -0.2495 -0.1307 96  ARG   G CB  
11913 C  CG  . ARG   G  105 ? 1.9651 0.4569 1.1913 0.0576  -0.2488 -0.0759 96  ARG   G CG  
11914 C  CD  . ARG   G  105 ? 1.9789 0.5422 1.2139 0.0865  -0.2541 -0.0978 96  ARG   G CD  
11915 N  NE  . ARG   G  105 ? 2.0763 0.5529 1.2308 0.0952  -0.2424 -0.0800 96  ARG   G NE  
11916 C  CZ  . ARG   G  105 ? 2.1598 0.5579 1.1627 0.0587  -0.2517 -0.0631 96  ARG   G CZ  
11917 N  NH1 . ARG   G  105 ? 2.1675 0.5917 1.1690 0.0397  -0.2504 -0.1327 96  ARG   G NH1 
11918 N  NH2 . ARG   G  105 ? 2.1906 0.6326 1.1154 0.0349  -0.2412 -0.0081 96  ARG   G NH2 
11919 N  N   . TYR   G  106 ? 1.7956 0.3576 1.1732 0.0205  -0.2886 -0.0865 97  TYR   G N   
11920 C  CA  . TYR   G  106 ? 1.7897 0.3209 1.1722 0.0509  -0.2650 -0.0941 97  TYR   G CA  
11921 C  C   . TYR   G  106 ? 1.8136 0.3441 1.1896 0.0430  -0.2456 -0.1100 97  TYR   G C   
11922 O  O   . TYR   G  106 ? 1.8188 0.3767 1.2557 0.0626  -0.2153 -0.1386 97  TYR   G O   
11923 C  CB  . TYR   G  106 ? 1.7966 0.3551 1.1264 0.0379  -0.2875 -0.0796 97  TYR   G CB  
11924 C  CG  . TYR   G  106 ? 1.7542 0.4812 1.0632 0.0483  -0.3365 -0.0905 97  TYR   G CG  
11925 C  CD1 . TYR   G  106 ? 1.7675 0.4935 1.1031 0.0274  -0.3224 -0.0862 97  TYR   G CD1 
11926 C  CD2 . TYR   G  106 ? 1.7316 0.5080 1.0800 0.0609  -0.3356 -0.0458 97  TYR   G CD2 
11927 C  CE1 . TYR   G  106 ? 1.7858 0.5291 1.0857 0.0331  -0.3386 -0.0963 97  TYR   G CE1 
11928 C  CE2 . TYR   G  106 ? 1.7365 0.5471 1.0658 0.0579  -0.3421 -0.0604 97  TYR   G CE2 
11929 C  CZ  . TYR   G  106 ? 1.7587 0.5155 1.0769 0.0280  -0.3606 -0.1193 97  TYR   G CZ  
11930 O  OH  . TYR   G  106 ? 1.7861 0.6744 1.0490 -0.0112 -0.3756 -0.1718 97  TYR   G OH  
11931 N  N   . LYS   G  107 ? 1.7989 0.2392 1.1825 0.1189  -0.2564 -0.1468 98  LYS   G N   
11932 C  CA  . LYS   G  107 ? 1.7969 0.2612 1.1776 0.1275  -0.2644 -0.1375 98  LYS   G CA  
11933 C  C   . LYS   G  107 ? 1.8008 0.2584 1.2075 0.1133  -0.2709 -0.0665 98  LYS   G C   
11934 O  O   . LYS   G  107 ? 1.7982 0.2911 1.1730 0.1775  -0.2451 0.0058  98  LYS   G O   
11935 C  CB  . LYS   G  107 ? 1.7817 0.2148 1.2003 0.1350  -0.2739 -0.1764 98  LYS   G CB  
11936 C  CG  . LYS   G  107 ? 1.7834 0.2735 1.2525 0.1347  -0.2990 -0.2002 98  LYS   G CG  
11937 C  CD  . LYS   G  107 ? 1.7944 0.3195 1.2809 0.1454  -0.3257 -0.1540 98  LYS   G CD  
11938 C  CE  . LYS   G  107 ? 1.8477 0.5065 1.3127 0.0823  -0.3528 -0.1706 98  LYS   G CE  
11939 N  NZ  . LYS   G  107 ? 1.7887 0.6377 1.4083 0.1216  -0.3757 -0.1721 98  LYS   G NZ  
11940 N  N   . TYR   G  108 ? 1.8036 0.2117 1.2269 0.0761  -0.2511 -0.0735 99  TYR   G N   
11941 C  CA  . TYR   G  108 ? 1.8103 0.3322 1.2211 0.0799  -0.2616 -0.0470 99  TYR   G CA  
11942 C  C   . TYR   G  108 ? 1.7959 0.2960 1.2113 0.0418  -0.2981 -0.0720 99  TYR   G C   
11943 O  O   . TYR   G  108 ? 1.7888 0.2634 1.2163 0.0160  -0.3035 -0.1053 99  TYR   G O   
11944 C  CB  . TYR   G  108 ? 1.7893 0.3743 1.2329 0.0319  -0.2397 -0.0146 99  TYR   G CB  
11945 C  CG  . TYR   G  108 ? 1.7718 0.4729 1.2363 0.0755  -0.2021 0.0269  99  TYR   G CG  
11946 C  CD1 . TYR   G  108 ? 1.7792 0.5142 1.2112 0.0776  -0.1850 0.0809  99  TYR   G CD1 
11947 C  CD2 . TYR   G  108 ? 1.7731 0.4184 1.2253 0.0492  -0.1990 0.0795  99  TYR   G CD2 
11948 C  CE1 . TYR   G  108 ? 1.7867 0.4900 1.2069 0.0590  -0.1263 0.1034  99  TYR   G CE1 
11949 C  CE2 . TYR   G  108 ? 1.7817 0.4395 1.2126 0.0147  -0.1403 0.1091  99  TYR   G CE2 
11950 C  CZ  . TYR   G  108 ? 1.7892 0.4773 1.2589 0.0468  -0.1014 0.0919  99  TYR   G CZ  
11951 O  OH  . TYR   G  108 ? 1.8271 0.6459 1.2267 0.0640  -0.1145 0.1058  99  TYR   G OH  
11952 N  N   . GLY   G  109 ? 1.7947 0.4015 1.1955 0.0228  -0.2942 -0.0841 100 GLY   G N   
11953 C  CA  . GLY   G  109 ? 1.7870 0.4725 1.1520 0.0217  -0.3333 -0.0864 100 GLY   G CA  
11954 C  C   . GLY   G  109 ? 1.7288 0.4758 1.1361 0.0495  -0.3600 -0.0563 100 GLY   G C   
11955 O  O   . GLY   G  109 ? 1.6568 0.3688 1.1685 0.0599  -0.3862 -0.1082 100 GLY   G O   
11956 N  N   . TYR   G  110 ? 1.7222 0.4927 1.1303 0.0146  -0.3627 -0.0987 101 TYR   G N   
11957 C  CA  . TYR   G  110 ? 1.7601 0.5045 1.1251 0.0485  -0.3726 -0.1036 101 TYR   G CA  
11958 C  C   . TYR   G  110 ? 1.7774 0.4473 1.1388 0.0372  -0.3986 -0.0344 101 TYR   G C   
11959 O  O   . TYR   G  110 ? 1.7730 0.3829 1.0965 0.0686  -0.3808 -0.0899 101 TYR   G O   
11960 C  CB  . TYR   G  110 ? 1.7666 0.5444 1.1326 0.0355  -0.3529 -0.0931 101 TYR   G CB  
11961 C  CG  . TYR   G  110 ? 1.7548 0.4876 1.1518 0.0654  -0.3613 -0.0929 101 TYR   G CG  
11962 C  CD1 . TYR   G  110 ? 1.7581 0.4857 1.1651 0.0723  -0.3499 -0.0936 101 TYR   G CD1 
11963 C  CD2 . TYR   G  110 ? 1.7456 0.4879 1.1133 0.1048  -0.3457 -0.1121 101 TYR   G CD2 
11964 C  CE1 . TYR   G  110 ? 1.7328 0.4691 1.2121 0.0815  -0.3335 -0.0946 101 TYR   G CE1 
11965 C  CE2 . TYR   G  110 ? 1.7461 0.4795 1.1593 0.1012  -0.3374 -0.1061 101 TYR   G CE2 
11966 C  CZ  . TYR   G  110 ? 1.7368 0.4563 1.1811 0.1065  -0.2907 -0.1001 101 TYR   G CZ  
11967 O  OH  . TYR   G  110 ? 1.7165 0.3436 1.3003 0.0805  -0.2323 -0.1614 101 TYR   G OH  
11968 N  N   . ASP   G  111 ? 1.8142 0.4664 1.1484 0.0122  -0.3950 -0.0399 102 ASP   G N   
11969 C  CA  . ASP   G  111 ? 1.7863 0.5491 1.1824 0.0305  -0.3695 -0.0669 102 ASP   G CA  
11970 C  C   . ASP   G  111 ? 1.7917 0.5477 1.1313 0.0677  -0.3885 -0.0490 102 ASP   G C   
11971 O  O   . ASP   G  111 ? 1.7862 0.5916 1.1304 0.0980  -0.3677 -0.0271 102 ASP   G O   
11972 C  CB  . ASP   G  111 ? 1.8136 0.6298 1.1917 -0.0301 -0.3439 -0.0777 102 ASP   G CB  
11973 C  CG  . ASP   G  111 ? 1.8790 0.6757 1.2899 -0.0953 -0.3071 -0.0697 102 ASP   G CG  
11974 O  OD1 . ASP   G  111 ? 1.8897 0.8243 1.3490 -0.1467 -0.2837 -0.1428 102 ASP   G OD1 
11975 O  OD2 . ASP   G  111 ? 1.9453 0.7422 1.3519 -0.0809 -0.3800 -0.0554 102 ASP   G OD2 
11976 N  N   . MET   G  112 ? 1.7958 0.4875 1.1355 0.0560  -0.3685 -0.0400 103 MET   G N   
11977 C  CA  . MET   G  112 ? 1.7961 0.4359 1.1765 0.0468  -0.3736 -0.0783 103 MET   G CA  
11978 C  C   . MET   G  112 ? 1.7745 0.3864 1.1342 0.0983  -0.3756 -0.0686 103 MET   G C   
11979 O  O   . MET   G  112 ? 1.7345 0.1494 1.0911 0.1019  -0.4153 -0.0480 103 MET   G O   
11980 C  CB  . MET   G  112 ? 1.7858 0.4457 1.2427 0.0607  -0.3552 -0.1023 103 MET   G CB  
11981 C  CG  . MET   G  112 ? 1.8602 0.4244 1.2577 0.0100  -0.3120 -0.1384 103 MET   G CG  
11982 S  SD  . MET   G  112 ? 1.8551 0.3918 1.2747 0.0193  -0.3053 -0.1950 103 MET   G SD  
11983 C  CE  . MET   G  112 ? 1.9052 0.3069 1.2657 0.0656  -0.3198 -0.1408 103 MET   G CE  
11984 N  N   . PRO   G  113 ? 1.7633 0.4846 1.2068 0.1229  -0.3626 -0.0580 104 PRO   G N   
11985 C  CA  . PRO   G  113 ? 1.7630 0.4940 1.2379 0.1132  -0.3472 -0.0769 104 PRO   G CA  
11986 C  C   . PRO   G  113 ? 1.7275 0.4859 1.2573 0.0934  -0.3594 -0.0828 104 PRO   G C   
11987 O  O   . PRO   G  113 ? 1.6744 0.5177 1.3053 0.1136  -0.3698 -0.0701 104 PRO   G O   
11988 C  CB  . PRO   G  113 ? 1.7554 0.5103 1.2415 0.1099  -0.3481 -0.0515 104 PRO   G CB  
11989 C  CG  . PRO   G  113 ? 1.7639 0.5383 1.2297 0.1473  -0.3401 -0.0551 104 PRO   G CG  
11990 C  CD  . PRO   G  113 ? 1.7829 0.5328 1.1972 0.1338  -0.3574 -0.0594 104 PRO   G CD  
11991 N  N   . CYS   G  114 ? 1.7385 0.4349 1.3082 0.0991  -0.3260 -0.1080 105 CYS   G N   
11992 C  CA  . CYS   G  114 ? 1.7430 0.3872 1.3096 0.0574  -0.3095 -0.1006 105 CYS   G CA  
11993 C  C   . CYS   G  114 ? 1.7108 0.1977 1.2947 0.0371  -0.3045 -0.1912 105 CYS   G C   
11994 O  O   . CYS   G  114 ? 1.7044 0.0925 1.2822 0.0126  -0.2660 -0.1922 105 CYS   G O   
11995 C  CB  . CYS   G  114 ? 1.7690 0.5090 1.3111 0.0387  -0.3244 -0.0969 105 CYS   G CB  
11996 S  SG  . CYS   G  114 ? 1.7128 0.6183 1.4960 0.1473  -0.2529 -0.1243 105 CYS   G SG  
11997 N  N   . ASP   G  115 ? 1.7051 0.1591 1.2707 0.0157  -0.3189 -0.1944 106 ASP   G N   
11998 C  CA  . ASP   G  115 ? 1.7040 0.2699 1.2387 0.0010  -0.3362 -0.1617 106 ASP   G CA  
11999 C  C   . ASP   G  115 ? 1.7304 0.3628 1.2260 0.0108  -0.3367 -0.1643 106 ASP   G C   
12000 O  O   . ASP   G  115 ? 1.7341 0.4008 1.1430 0.0111  -0.3371 -0.1858 106 ASP   G O   
12001 C  CB  . ASP   G  115 ? 1.7027 0.2344 1.2804 0.0140  -0.3319 -0.1548 106 ASP   G CB  
12002 C  CG  . ASP   G  115 ? 1.7189 0.2100 1.3213 -0.0065 -0.3225 -0.1631 106 ASP   G CG  
12003 O  OD1 . ASP   G  115 ? 1.7030 0.2263 1.4529 -0.0272 -0.3172 -0.1034 106 ASP   G OD1 
12004 O  OD2 . ASP   G  115 ? 1.7798 0.1648 1.2868 -0.0686 -0.2924 -0.1099 106 ASP   G OD2 
12005 N  N   . VAL   G  116 ? 1.7090 0.3671 1.1136 -0.0007 -0.3794 -0.1366 107 VAL   G N   
12006 C  CA  . VAL   G  116 ? 1.6790 0.4516 1.0727 -0.0057 -0.3813 -0.0921 107 VAL   G CA  
12007 C  C   . VAL   G  116 ? 1.6706 0.4688 1.0251 -0.0116 -0.3771 -0.0791 107 VAL   G C   
12008 O  O   . VAL   G  116 ? 1.6446 0.4993 1.0592 0.0056  -0.3774 -0.0449 107 VAL   G O   
12009 C  CB  . VAL   G  116 ? 1.6966 0.4453 1.0614 -0.0157 -0.3867 -0.0749 107 VAL   G CB  
12010 C  CG1 . VAL   G  116 ? 1.7230 0.4534 1.0516 -0.0205 -0.3816 -0.0686 107 VAL   G CG1 
12011 C  CG2 . VAL   G  116 ? 1.6864 0.4703 1.0542 -0.0400 -0.4150 -0.0709 107 VAL   G CG2 
12012 N  N   . LEU   G  117 ? 1.6739 0.4725 0.9910 -0.0029 -0.3879 -0.0884 108 LEU   G N   
12013 C  CA  . LEU   G  117 ? 1.6705 0.4968 0.9767 -0.0081 -0.3722 -0.1098 108 LEU   G CA  
12014 C  C   . LEU   G  117 ? 1.7324 0.4965 1.0426 -0.0336 -0.3445 -0.1095 108 LEU   G C   
12015 O  O   . LEU   G  117 ? 1.6691 0.5369 1.0586 -0.0735 -0.3615 -0.1549 108 LEU   G O   
12016 C  CB  . LEU   G  117 ? 1.6491 0.4791 0.9429 0.0029  -0.3930 -0.1292 108 LEU   G CB  
12017 C  CG  . LEU   G  117 ? 1.6431 0.4858 0.9421 -0.0093 -0.3836 -0.1466 108 LEU   G CG  
12018 C  CD1 . LEU   G  117 ? 1.6509 0.5092 0.9259 -0.0245 -0.3801 -0.1288 108 LEU   G CD1 
12019 C  CD2 . LEU   G  117 ? 1.6321 0.4923 0.9419 -0.0010 -0.3864 -0.1514 108 LEU   G CD2 
12020 N  N   . ALA   G  118 ? 1.7383 0.5470 1.0578 -0.0517 -0.3732 -0.0846 109 ALA   G N   
12021 C  CA  . ALA   G  118 ? 1.7813 0.5499 1.0900 0.0200  -0.3265 -0.0048 109 ALA   G CA  
12022 C  C   . ALA   G  118 ? 1.7630 0.4388 1.1139 0.0705  -0.3021 0.0258  109 ALA   G C   
12023 O  O   . ALA   G  118 ? 1.8151 0.4507 1.1219 0.0934  -0.2654 0.0890  109 ALA   G O   
12024 C  CB  . ALA   G  118 ? 1.7805 0.6010 1.1012 0.0120  -0.3325 0.0037  109 ALA   G CB  
12025 N  N   . LYS   G  119 ? 1.7872 0.3779 1.1102 0.0605  -0.2882 0.0098  110 LYS   G N   
12026 C  CA  . LYS   G  119 ? 1.7339 0.3148 1.1168 0.1013  -0.2780 0.0075  110 LYS   G CA  
12027 C  C   . LYS   G  119 ? 1.7563 0.2381 1.1045 0.1253  -0.3003 0.0078  110 LYS   G C   
12028 O  O   . LYS   G  119 ? 1.6856 0.0870 1.1843 0.0503  -0.3018 -0.0374 110 LYS   G O   
12029 C  CB  . LYS   G  119 ? 1.7399 0.3660 1.1617 0.1264  -0.2562 0.0222  110 LYS   G CB  
12030 C  CG  . LYS   G  119 ? 1.7431 0.4052 1.1964 0.1452  -0.2259 0.0621  110 LYS   G CG  
12031 C  CD  . LYS   G  119 ? 1.7338 0.5013 1.2404 0.1722  -0.1838 0.0620  110 LYS   G CD  
12032 C  CE  . LYS   G  119 ? 1.7417 0.5689 1.2767 0.1597  -0.1558 0.1158  110 LYS   G CE  
12033 N  NZ  . LYS   G  119 ? 1.7374 0.6077 1.3476 0.1883  -0.1264 0.1729  110 LYS   G NZ  
12034 N  N   . ARG   G  120 ? 1.7136 0.2858 1.0959 0.1094  -0.3110 0.0041  111 ARG   G N   
12035 C  CA  . ARG   G  120 ? 1.7030 0.3654 1.0740 0.1566  -0.3285 0.0144  111 ARG   G CA  
12036 C  C   . ARG   G  120 ? 1.6852 0.3940 1.0616 0.1521  -0.3068 -0.0306 111 ARG   G C   
12037 O  O   . ARG   G  120 ? 1.6810 0.3938 1.0729 0.2018  -0.2861 -0.0134 111 ARG   G O   
12038 C  CB  . ARG   G  120 ? 1.7286 0.3204 1.0911 0.1950  -0.3347 -0.0022 111 ARG   G CB  
12039 C  CG  . ARG   G  120 ? 1.7394 0.3100 1.0818 0.2304  -0.3460 -0.0377 111 ARG   G CG  
12040 C  CD  . ARG   G  120 ? 1.8098 0.3421 1.0867 0.2877  -0.3121 -0.0963 111 ARG   G CD  
12041 N  NE  . ARG   G  120 ? 1.8257 0.4487 1.0869 0.2940  -0.3226 -0.1138 111 ARG   G NE  
12042 C  CZ  . ARG   G  120 ? 1.9286 0.4760 1.0537 0.3154  -0.2894 -0.1142 111 ARG   G CZ  
12043 N  NH1 . ARG   G  120 ? 2.0226 0.2388 1.0605 0.4072  -0.2357 -0.1470 111 ARG   G NH1 
12044 N  NH2 . ARG   G  120 ? 1.9456 0.6723 1.1413 0.2466  -0.2878 -0.1329 111 ARG   G NH2 
12045 N  N   . MET   G  121 ? 1.6686 0.4056 1.0347 0.0821  -0.3304 -0.0373 112 MET   G N   
12046 C  CA  . MET   G  121 ? 1.6151 0.4250 1.0253 0.0491  -0.3307 -0.0467 112 MET   G CA  
12047 C  C   . MET   G  121 ? 1.5752 0.4360 1.0225 0.0335  -0.3452 -0.0442 112 MET   G C   
12048 O  O   . MET   G  121 ? 1.6048 0.3079 0.9341 0.0079  -0.3415 -0.0543 112 MET   G O   
12049 C  CB  . MET   G  121 ? 1.6341 0.4478 1.0167 0.0280  -0.3416 -0.0251 112 MET   G CB  
12050 C  CG  . MET   G  121 ? 1.6631 0.4355 1.0432 0.0150  -0.3552 -0.0306 112 MET   G CG  
12051 S  SD  . MET   G  121 ? 1.6268 0.4862 1.1030 0.0517  -0.3762 0.0348  112 MET   G SD  
12052 C  CE  . MET   G  121 ? 1.6335 0.4679 1.0531 0.0297  -0.3815 -0.0098 112 MET   G CE  
12053 N  N   . ALA   G  122 ? 1.5975 0.4904 1.0783 -0.0160 -0.3237 -0.0493 113 ALA   G N   
12054 C  CA  . ALA   G  122 ? 1.6084 0.4566 1.1331 0.0125  -0.3335 -0.0329 113 ALA   G CA  
12055 C  C   . ALA   G  122 ? 1.5966 0.4238 1.1281 0.0387  -0.3240 0.0371  113 ALA   G C   
12056 O  O   . ALA   G  122 ? 1.6056 0.3531 1.1305 0.0012  -0.2680 0.0142  113 ALA   G O   
12057 C  CB  . ALA   G  122 ? 1.6142 0.4699 1.1934 -0.0252 -0.3320 -0.0444 113 ALA   G CB  
12058 N  N   . ASN   G  123 ? 1.5824 0.4754 1.1727 0.0371  -0.2934 -0.0012 114 ASN   G N   
12059 C  CA  . ASN   G  123 ? 1.5384 0.4311 1.1709 0.0153  -0.2702 0.0120  114 ASN   G CA  
12060 C  C   . ASN   G  123 ? 1.5416 0.3626 1.1681 0.0481  -0.2655 0.0209  114 ASN   G C   
12061 O  O   . ASN   G  123 ? 1.4305 0.1868 1.2018 0.0391  -0.2414 0.0159  114 ASN   G O   
12062 C  CB  . ASN   G  123 ? 1.5466 0.4312 1.1865 0.0346  -0.2620 0.0347  114 ASN   G CB  
12063 C  CG  . ASN   G  123 ? 1.5456 0.4491 1.1875 0.0283  -0.2551 0.0912  114 ASN   G CG  
12064 O  OD1 . ASN   G  123 ? 1.5736 0.5641 1.3234 0.1432  -0.2207 0.2436  114 ASN   G OD1 
12065 N  ND2 . ASN   G  123 ? 1.5426 0.4724 1.1224 0.0224  -0.2294 0.0966  114 ASN   G ND2 
12066 N  N   . LEU   G  124 ? 1.5346 0.4587 1.2424 0.0394  -0.2075 -0.0321 115 LEU   G N   
12067 C  CA  . LEU   G  124 ? 1.5509 0.5911 1.2486 0.0540  -0.2263 -0.0367 115 LEU   G CA  
12068 C  C   . LEU   G  124 ? 1.6146 0.5937 1.2725 0.0343  -0.2109 -0.0701 115 LEU   G C   
12069 O  O   . LEU   G  124 ? 1.6630 0.8005 1.2028 -0.0363 -0.2146 -0.0184 115 LEU   G O   
12070 C  CB  . LEU   G  124 ? 1.5837 0.5827 1.2585 0.0537  -0.2037 -0.0410 115 LEU   G CB  
12071 C  CG  . LEU   G  124 ? 1.5645 0.5939 1.2291 0.0569  -0.1858 -0.0665 115 LEU   G CG  
12072 C  CD1 . LEU   G  124 ? 1.5901 0.6239 1.2400 0.0713  -0.1851 -0.0847 115 LEU   G CD1 
12073 C  CD2 . LEU   G  124 ? 1.5476 0.5355 1.2496 0.0571  -0.1762 -0.0704 115 LEU   G CD2 
12074 N  N   . SER   G  125 ? 1.5942 0.6484 1.2741 0.0220  -0.1909 -0.0950 116 SER   G N   
12075 C  CA  . SER   G  125 ? 1.5334 0.6330 1.2310 0.0455  -0.1572 -0.0408 116 SER   G CA  
12076 C  C   . SER   G  125 ? 1.4771 0.5087 1.1935 0.0934  -0.2000 -0.0613 116 SER   G C   
12077 O  O   . SER   G  125 ? 1.4847 0.6236 1.2374 0.0783  -0.2382 0.0512  116 SER   G O   
12078 C  CB  . SER   G  125 ? 1.5276 0.6691 1.2181 0.0241  -0.1016 -0.0803 116 SER   G CB  
12079 O  OG  . SER   G  125 ? 1.5387 0.8166 1.2672 0.0291  -0.0034 -0.1125 116 SER   G OG  
12080 N  N   . GLN   G  126 ? 1.4685 0.4148 1.0683 0.0850  -0.2308 -0.0589 117 GLN   G N   
12081 C  CA  . GLN   G  126 ? 1.4885 0.3309 1.0524 0.1089  -0.2410 -0.0529 117 GLN   G CA  
12082 C  C   . GLN   G  126 ? 1.5276 0.3249 1.0348 0.0746  -0.2391 -0.0297 117 GLN   G C   
12083 O  O   . GLN   G  126 ? 1.5467 0.2591 1.0269 0.0505  -0.2088 -0.0719 117 GLN   G O   
12084 C  CB  . GLN   G  126 ? 1.4961 0.3593 1.0153 0.1209  -0.2417 -0.0630 117 GLN   G CB  
12085 C  CG  . GLN   G  126 ? 1.4987 0.3113 0.9956 0.1594  -0.2447 -0.0565 117 GLN   G CG  
12086 C  CD  . GLN   G  126 ? 1.4946 0.3203 0.9860 0.1996  -0.2366 -0.0589 117 GLN   G CD  
12087 O  OE1 . GLN   G  126 ? 1.4720 0.2929 0.9436 0.2353  -0.2534 -0.0905 117 GLN   G OE1 
12088 N  NE2 . GLN   G  126 ? 1.4872 0.3444 0.9705 0.1766  -0.2257 -0.0639 117 GLN   G NE2 
12089 N  N   . ILE   G  127 ? 1.5654 0.4130 1.0594 -0.0043 -0.2699 -0.0364 118 ILE   G N   
12090 C  CA  . ILE   G  127 ? 1.6223 0.4504 1.0269 -0.0152 -0.2780 -0.0131 118 ILE   G CA  
12091 C  C   . ILE   G  127 ? 1.6389 0.4320 1.0113 -0.0164 -0.2916 -0.0122 118 ILE   G C   
12092 O  O   . ILE   G  127 ? 1.6789 0.5350 0.9912 -0.0230 -0.2375 0.0202  118 ILE   G O   
12093 C  CB  . ILE   G  127 ? 1.6295 0.4668 1.0320 -0.0378 -0.2861 -0.0548 118 ILE   G CB  
12094 C  CG1 . ILE   G  127 ? 1.6159 0.4919 1.0681 -0.0443 -0.2517 -0.0662 118 ILE   G CG1 
12095 C  CG2 . ILE   G  127 ? 1.6504 0.4637 1.0345 -0.0571 -0.2969 -0.0557 118 ILE   G CG2 
12096 C  CD1 . ILE   G  127 ? 1.6317 0.4967 1.1032 -0.0456 -0.2361 -0.0621 118 ILE   G CD1 
12097 N  N   . TYR   G  128 ? 1.6643 0.3930 1.0058 -0.0443 -0.3152 -0.0601 119 TYR   G N   
12098 C  CA  . TYR   G  128 ? 1.6483 0.4711 1.0689 -0.0359 -0.3353 -0.0798 119 TYR   G CA  
12099 C  C   . TYR   G  128 ? 1.6455 0.5146 1.0988 -0.0633 -0.2991 -0.0481 119 TYR   G C   
12100 O  O   . TYR   G  128 ? 1.6416 0.5374 1.0852 -0.0692 -0.3377 -0.0536 119 TYR   G O   
12101 C  CB  . TYR   G  128 ? 1.6746 0.4952 1.0735 -0.0748 -0.3349 -0.0638 119 TYR   G CB  
12102 C  CG  . TYR   G  128 ? 1.7125 0.4577 1.1710 -0.0981 -0.3588 -0.0914 119 TYR   G CG  
12103 C  CD1 . TYR   G  128 ? 1.7138 0.5217 1.1721 -0.1271 -0.4275 -0.0871 119 TYR   G CD1 
12104 C  CD2 . TYR   G  128 ? 1.7545 0.4492 1.1707 -0.1133 -0.3238 -0.0981 119 TYR   G CD2 
12105 C  CE1 . TYR   G  128 ? 1.7327 0.5665 1.2558 -0.1772 -0.4036 -0.0482 119 TYR   G CE1 
12106 C  CE2 . TYR   G  128 ? 1.7775 0.4921 1.2305 -0.1617 -0.2916 -0.0713 119 TYR   G CE2 
12107 C  CZ  . TYR   G  128 ? 1.7685 0.5755 1.2366 -0.2234 -0.3339 -0.0768 119 TYR   G CZ  
12108 O  OH  . TYR   G  128 ? 1.7503 0.6164 1.4621 -0.2843 -0.2473 -0.0160 119 TYR   G OH  
12109 N  N   . THR   G  129 ? 1.6280 0.4553 1.1351 -0.0645 -0.2429 -0.0356 120 THR   G N   
12110 C  CA  . THR   G  129 ? 1.6562 0.3712 1.1315 -0.0008 -0.2288 -0.0592 120 THR   G CA  
12111 C  C   . THR   G  129 ? 1.6657 0.3615 1.1508 -0.0242 -0.1934 -0.0329 120 THR   G C   
12112 O  O   . THR   G  129 ? 1.6100 0.2854 1.1569 -0.0437 -0.1798 -0.1403 120 THR   G O   
12113 C  CB  . THR   G  129 ? 1.6499 0.2545 1.1398 0.0001  -0.2227 -0.0751 120 THR   G CB  
12114 O  OG1 . THR   G  129 ? 1.6548 0.2407 1.1101 0.0168  -0.2309 -0.0405 120 THR   G OG1 
12115 C  CG2 . THR   G  129 ? 1.6425 0.2515 1.1321 0.0205  -0.2353 -0.1176 120 THR   G CG2 
12116 N  N   . GLN   G  130 ? 1.6632 0.3183 1.1693 -0.0304 -0.1910 -0.0043 121 GLN   G N   
12117 C  CA  . GLN   G  130 ? 1.6836 0.3062 1.1781 -0.0377 -0.1665 0.0282  121 GLN   G CA  
12118 C  C   . GLN   G  130 ? 1.7234 0.3237 1.1984 -0.0261 -0.1952 0.0010  121 GLN   G C   
12119 O  O   . GLN   G  130 ? 1.7317 0.4155 1.0873 -0.1416 -0.1245 -0.0467 121 GLN   G O   
12120 C  CB  . GLN   G  130 ? 1.6639 0.2941 1.1808 -0.0531 -0.1682 0.0344  121 GLN   G CB  
12121 C  CG  . GLN   G  130 ? 1.6860 0.2955 1.1584 -0.0636 -0.1950 0.0533  121 GLN   G CG  
12122 C  CD  . GLN   G  130 ? 1.6572 0.3627 1.1597 -0.0976 -0.1801 0.0345  121 GLN   G CD  
12123 O  OE1 . GLN   G  130 ? 1.6496 0.2556 1.0620 -0.0723 -0.2552 0.0686  121 GLN   G OE1 
12124 N  NE2 . GLN   G  130 ? 1.6325 0.4375 1.1882 -0.0709 -0.2180 0.0450  121 GLN   G NE2 
12125 N  N   . ARG   G  131 ? 1.7429 0.3677 1.2847 -0.0395 -0.1653 0.0120  122 ARG   G N   
12126 C  CA  . ARG   G  131 ? 1.7796 0.5707 1.3322 -0.0097 -0.2166 -0.0653 122 ARG   G CA  
12127 C  C   . ARG   G  131 ? 1.7933 0.5381 1.2653 0.0038  -0.2607 -0.0593 122 ARG   G C   
12128 O  O   . ARG   G  131 ? 1.7978 0.6000 1.2465 0.0556  -0.1800 -0.0264 122 ARG   G O   
12129 C  CB  . ARG   G  131 ? 1.8254 0.6376 1.5328 -0.0741 -0.1551 -0.0072 122 ARG   G CB  
12130 C  CG  . ARG   G  131 ? 1.8952 0.7329 1.5811 -0.0285 -0.1165 -0.0941 122 ARG   G CG  
12131 C  CD  . ARG   G  131 ? 1.9515 0.8094 1.7509 0.0321  -0.0269 -0.0758 122 ARG   G CD  
12132 N  NE  . ARG   G  131 ? 2.0476 0.8352 1.8624 0.0557  0.0416  -0.0421 122 ARG   G NE  
12133 C  CZ  . ARG   G  131 ? 2.0451 0.8848 1.9496 0.0428  0.1326  -0.0920 122 ARG   G CZ  
12134 N  NH1 . ARG   G  131 ? 2.0961 1.1571 2.0019 0.0187  0.1988  -0.1581 122 ARG   G NH1 
12135 N  NH2 . ARG   G  131 ? 2.1209 0.7310 2.0460 0.0000  0.1096  -0.1800 122 ARG   G NH2 
12136 N  N   . ALA   G  132 ? 1.8497 0.5750 1.1740 0.0204  -0.2586 -0.0892 123 ALA   G N   
12137 C  CA  . ALA   G  132 ? 1.9012 0.5613 1.1275 0.0346  -0.2730 -0.0692 123 ALA   G CA  
12138 C  C   . ALA   G  132 ? 1.9103 0.6253 1.1474 0.0243  -0.2648 -0.0806 123 ALA   G C   
12139 O  O   . ALA   G  132 ? 1.9705 0.7020 1.0631 0.0096  -0.2263 -0.0765 123 ALA   G O   
12140 C  CB  . ALA   G  132 ? 1.9488 0.5645 1.1147 0.0311  -0.2514 -0.0728 123 ALA   G CB  
12141 N  N   . TYR   G  133 ? 1.9565 0.5922 1.2390 0.0477  -0.2897 -0.0738 124 TYR   G N   
12142 C  CA  . TYR   G  133 ? 1.9500 0.5900 1.2909 0.0551  -0.3006 -0.0424 124 TYR   G CA  
12143 C  C   . TYR   G  133 ? 1.9148 0.4221 1.2733 0.0339  -0.3298 -0.1152 124 TYR   G C   
12144 O  O   . TYR   G  133 ? 1.9175 0.3205 1.3153 -0.0116 -0.3247 -0.2307 124 TYR   G O   
12145 C  CB  . TYR   G  133 ? 1.9554 0.6550 1.2799 0.0600  -0.3449 -0.0601 124 TYR   G CB  
12146 C  CG  . TYR   G  133 ? 1.9970 0.7136 1.3207 0.0951  -0.3413 0.0072  124 TYR   G CG  
12147 C  CD1 . TYR   G  133 ? 1.9906 0.7845 1.3649 0.0853  -0.3261 0.0508  124 TYR   G CD1 
12148 C  CD2 . TYR   G  133 ? 1.9810 0.7324 1.3454 0.1149  -0.3441 0.0516  124 TYR   G CD2 
12149 C  CE1 . TYR   G  133 ? 2.0548 0.7842 1.4512 0.0595  -0.2927 0.1108  124 TYR   G CE1 
12150 C  CE2 . TYR   G  133 ? 2.0861 0.7679 1.3877 0.1011  -0.3319 0.1373  124 TYR   G CE2 
12151 C  CZ  . TYR   G  133 ? 2.1040 0.7215 1.4507 0.1012  -0.2921 0.1640  124 TYR   G CZ  
12152 O  OH  . TYR   G  133 ? 2.2388 0.6879 1.5602 0.1900  -0.2717 0.0721  124 TYR   G OH  
12153 N  N   . MET   G  134 ? 1.8825 0.3959 1.3628 0.0494  -0.3246 -0.1122 125 MET   G N   
12154 C  CA  . MET   G  134 ? 1.8385 0.5244 1.4052 0.0750  -0.3524 -0.0461 125 MET   G CA  
12155 C  C   . MET   G  134 ? 1.7398 0.4739 1.3143 0.1015  -0.3080 0.0058  125 MET   G C   
12156 O  O   . MET   G  134 ? 1.7599 0.4390 1.3427 0.1458  -0.3138 0.1582  125 MET   G O   
12157 C  CB  . MET   G  134 ? 1.8661 0.5596 1.5294 0.0986  -0.3490 -0.0244 125 MET   G CB  
12158 C  CG  . MET   G  134 ? 1.9344 0.5826 1.6005 0.0722  -0.3603 -0.0469 125 MET   G CG  
12159 S  SD  . MET   G  134 ? 2.0111 0.4888 1.8161 0.1429  -0.2965 0.0104  125 MET   G SD  
12160 C  CE  . MET   G  134 ? 2.0288 0.7017 1.8571 0.1119  -0.1805 0.0016  125 MET   G CE  
12161 N  N   . ARG   G  135 ? 1.7257 0.4202 1.2876 0.0990  -0.3276 -0.0025 126 ARG   G N   
12162 C  CA  . ARG   G  135 ? 1.7354 0.3062 1.3241 0.0844  -0.2631 0.0159  126 ARG   G CA  
12163 C  C   . ARG   G  135 ? 1.6914 0.4684 1.2628 0.0294  -0.3088 -0.0416 126 ARG   G C   
12164 O  O   . ARG   G  135 ? 1.7258 0.5455 1.2216 0.0734  -0.3292 0.1047  126 ARG   G O   
12165 C  CB  . ARG   G  135 ? 1.7389 0.2775 1.3324 0.0658  -0.2444 0.0138  126 ARG   G CB  
12166 C  CG  . ARG   G  135 ? 1.7134 0.2439 1.3331 0.0727  -0.2180 -0.0203 126 ARG   G CG  
12167 C  CD  . ARG   G  135 ? 1.7033 0.2878 1.3420 0.0777  -0.2131 -0.0320 126 ARG   G CD  
12168 N  NE  . ARG   G  135 ? 1.7009 0.3345 1.3243 0.0877  -0.1944 -0.0480 126 ARG   G NE  
12169 C  CZ  . ARG   G  135 ? 1.6867 0.3593 1.2909 0.0557  -0.1914 -0.0945 126 ARG   G CZ  
12170 N  NH1 . ARG   G  135 ? 1.6939 0.3499 1.2890 0.0193  -0.1806 -0.1125 126 ARG   G NH1 
12171 N  NH2 . ARG   G  135 ? 1.7055 0.3183 1.2862 0.0398  -0.1924 -0.1123 126 ARG   G NH2 
12172 N  N   . PRO   G  136 ? 1.7653 0.4001 1.2019 0.0030  -0.2709 -0.0711 127 PRO   G N   
12173 C  CA  . PRO   G  136 ? 1.7990 0.3171 1.1490 -0.0578 -0.2796 -0.1111 127 PRO   G CA  
12174 C  C   . PRO   G  136 ? 1.8007 0.1626 1.1585 -0.0717 -0.2772 -0.1316 127 PRO   G C   
12175 O  O   . PRO   G  136 ? 1.8598 0.1444 1.2333 -0.0539 -0.2361 -0.1403 127 PRO   G O   
12176 C  CB  . PRO   G  136 ? 1.7185 0.4680 1.1199 -0.1063 -0.2836 -0.0949 127 PRO   G CB  
12177 C  CG  . PRO   G  136 ? 1.7314 0.5009 1.1392 -0.0393 -0.2774 -0.0651 127 PRO   G CG  
12178 C  CD  . PRO   G  136 ? 1.7187 0.4560 1.1628 -0.0161 -0.2700 -0.0278 127 PRO   G CD  
12179 N  N   . LEU   G  137 ? 1.8181 0.2794 1.1177 -0.0597 -0.3392 -0.1329 128 LEU   G N   
12180 C  CA  . LEU   G  137 ? 1.7953 0.3878 1.1266 -0.0309 -0.3387 -0.1151 128 LEU   G CA  
12181 C  C   . LEU   G  137 ? 1.7615 0.3583 1.1309 0.0101  -0.3268 -0.1265 128 LEU   G C   
12182 O  O   . LEU   G  137 ? 1.7624 0.4706 1.1501 -0.0112 -0.3141 -0.1250 128 LEU   G O   
12183 C  CB  . LEU   G  137 ? 1.8002 0.4142 1.1615 -0.0266 -0.3305 -0.0782 128 LEU   G CB  
12184 C  CG  . LEU   G  137 ? 1.8031 0.4474 1.1728 -0.0325 -0.3302 -0.1018 128 LEU   G CG  
12185 C  CD1 . LEU   G  137 ? 1.7691 0.5104 1.2279 0.0033  -0.3385 -0.0727 128 LEU   G CD1 
12186 C  CD2 . LEU   G  137 ? 1.8047 0.4355 1.1720 0.0148  -0.3209 -0.0338 128 LEU   G CD2 
12187 N  N   . GLY   G  138 ? 1.7631 0.3479 1.1291 0.0165  -0.3277 -0.1196 129 GLY   G N   
12188 C  CA  . GLY   G  138 ? 1.7924 0.3463 1.1432 0.0097  -0.2952 -0.1382 129 GLY   G CA  
12189 C  C   . GLY   G  138 ? 1.7448 0.3305 1.1003 0.0113  -0.2896 -0.1970 129 GLY   G C   
12190 O  O   . GLY   G  138 ? 1.7997 0.2347 1.0767 -0.0329 -0.3220 -0.2746 129 GLY   G O   
12191 N  N   . VAL   G  139 ? 1.6886 0.4022 1.1281 0.0036  -0.2868 -0.1787 130 VAL   G N   
12192 C  CA  . VAL   G  139 ? 1.6701 0.4712 1.1553 0.0043  -0.2874 -0.1433 130 VAL   G CA  
12193 C  C   . VAL   G  139 ? 1.6702 0.4244 1.1934 -0.0141 -0.2785 -0.1200 130 VAL   G C   
12194 O  O   . VAL   G  139 ? 1.6703 0.3724 1.1484 -0.0087 -0.3184 -0.0958 130 VAL   G O   
12195 C  CB  . VAL   G  139 ? 1.6631 0.4981 1.1948 -0.0075 -0.2564 -0.1278 130 VAL   G CB  
12196 C  CG1 . VAL   G  139 ? 1.6774 0.5950 1.1940 0.0394  -0.2396 -0.1301 130 VAL   G CG1 
12197 C  CG2 . VAL   G  139 ? 1.6319 0.5311 1.2005 0.0166  -0.2685 -0.1405 130 VAL   G CG2 
12198 N  N   . ILE   G  140 ? 1.6813 0.4579 1.1954 0.0127  -0.2770 -0.0372 131 ILE   G N   
12199 C  CA  . ILE   G  140 ? 1.6729 0.4241 1.2612 0.0061  -0.2491 -0.0211 131 ILE   G CA  
12200 C  C   . ILE   G  140 ? 1.6982 0.2885 1.3914 -0.0112 -0.2283 -0.0773 131 ILE   G C   
12201 O  O   . ILE   G  140 ? 1.6601 0.0681 1.5166 -0.0325 -0.1132 -0.0950 131 ILE   G O   
12202 C  CB  . ILE   G  140 ? 1.6592 0.4620 1.2574 -0.0292 -0.2425 -0.0096 131 ILE   G CB  
12203 C  CG1 . ILE   G  140 ? 1.6193 0.4802 1.2532 0.0222  -0.2426 0.0051  131 ILE   G CG1 
12204 C  CG2 . ILE   G  140 ? 1.6368 0.4907 1.2864 -0.0445 -0.2327 -0.0126 131 ILE   G CG2 
12205 C  CD1 . ILE   G  140 ? 1.6197 0.4988 1.2439 0.0486  -0.2344 -0.0311 131 ILE   G CD1 
12206 N  N   . LEU   G  141 ? 1.6967 0.2689 1.3790 0.0225  -0.2556 -0.0260 132 LEU   G N   
12207 C  CA  . LEU   G  141 ? 1.7213 0.2797 1.3698 0.0188  -0.2826 -0.0180 132 LEU   G CA  
12208 C  C   . LEU   G  141 ? 1.7272 0.3369 1.3641 0.0346  -0.2785 -0.0278 132 LEU   G C   
12209 O  O   . LEU   G  141 ? 1.7466 0.2318 1.4992 0.0518  -0.2152 -0.0422 132 LEU   G O   
12210 C  CB  . LEU   G  141 ? 1.6907 0.2178 1.3438 0.0322  -0.3231 0.0234  132 LEU   G CB  
12211 C  CG  . LEU   G  141 ? 1.7407 0.2096 1.2627 0.0218  -0.3246 0.0235  132 LEU   G CG  
12212 C  CD1 . LEU   G  141 ? 1.7899 0.2356 1.2223 0.0445  -0.2833 0.0302  132 LEU   G CD1 
12213 C  CD2 . LEU   G  141 ? 1.7483 0.2267 1.2914 0.0221  -0.3208 0.0097  132 LEU   G CD2 
12214 N  N   . THR   G  142 ? 1.6984 0.4474 1.3318 0.0207  -0.3030 -0.0625 133 THR   G N   
12215 C  CA  . THR   G  142 ? 1.7252 0.6203 1.2384 0.0026  -0.3185 -0.0343 133 THR   G CA  
12216 C  C   . THR   G  142 ? 1.6965 0.6590 1.1110 0.0450  -0.3285 0.0158  133 THR   G C   
12217 O  O   . THR   G  142 ? 1.6717 1.0215 1.0667 0.0275  -0.3378 0.0371  133 THR   G O   
12218 C  CB  . THR   G  142 ? 1.7236 0.6976 1.2438 -0.0696 -0.3270 -0.0407 133 THR   G CB  
12219 O  OG1 . THR   G  142 ? 1.7671 0.7842 1.3012 -0.0341 -0.2752 0.1023  133 THR   G OG1 
12220 C  CG2 . THR   G  142 ? 1.7140 0.6281 1.3119 -0.0354 -0.3220 0.0208  133 THR   G CG2 
12221 N  N   . PHE   G  143 ? 1.7033 0.6688 1.0479 0.0613  -0.3605 -0.0098 134 PHE   G N   
12222 C  CA  . PHE   G  143 ? 1.6519 0.6257 1.0537 0.0797  -0.3456 -0.1160 134 PHE   G CA  
12223 C  C   . PHE   G  143 ? 1.6495 0.6053 1.0901 0.1002  -0.3533 -0.1329 134 PHE   G C   
12224 O  O   . PHE   G  143 ? 1.6456 0.6498 1.1787 0.1076  -0.2448 -0.1518 134 PHE   G O   
12225 C  CB  . PHE   G  143 ? 1.6014 0.5714 1.0259 0.0970  -0.3566 -0.0731 134 PHE   G CB  
12226 C  CG  . PHE   G  143 ? 1.6009 0.5030 0.9727 0.0869  -0.3324 -0.0495 134 PHE   G CG  
12227 C  CD1 . PHE   G  143 ? 1.5893 0.5530 0.8989 0.0706  -0.3733 -0.0726 134 PHE   G CD1 
12228 C  CD2 . PHE   G  143 ? 1.5683 0.4390 0.9504 0.1084  -0.3591 -0.0846 134 PHE   G CD2 
12229 C  CE1 . PHE   G  143 ? 1.5986 0.4875 0.8698 0.0642  -0.3699 -0.0838 134 PHE   G CE1 
12230 C  CE2 . PHE   G  143 ? 1.5746 0.4541 0.9290 0.0703  -0.3607 -0.1104 134 PHE   G CE2 
12231 C  CZ  . PHE   G  143 ? 1.5895 0.4370 0.9102 0.0668  -0.3713 -0.0887 134 PHE   G CZ  
12232 N  N   . VAL   G  144 ? 1.6776 0.6272 1.1241 0.0469  -0.3481 -0.1246 135 VAL   G N   
12233 C  CA  . VAL   G  144 ? 1.6752 0.6844 1.1209 0.0389  -0.3581 -0.1291 135 VAL   G CA  
12234 C  C   . VAL   G  144 ? 1.6149 0.6995 1.1971 0.0105  -0.4151 -0.0532 135 VAL   G C   
12235 O  O   . VAL   G  144 ? 1.5710 0.7533 1.2612 0.0085  -0.4104 -0.0089 135 VAL   G O   
12236 C  CB  . VAL   G  144 ? 1.6953 0.6768 1.0847 0.0122  -0.3671 -0.1237 135 VAL   G CB  
12237 C  CG1 . VAL   G  144 ? 1.7172 0.6890 1.0896 -0.0107 -0.3568 -0.1337 135 VAL   G CG1 
12238 C  CG2 . VAL   G  144 ? 1.7137 0.6047 1.0014 -0.0158 -0.3614 -0.1352 135 VAL   G CG2 
12239 N  N   . SER   G  145 ? 1.6208 0.7528 1.2280 0.0281  -0.4166 -0.0488 136 SER   G N   
12240 C  CA  . SER   G  145 ? 1.5894 0.7477 1.2063 0.0328  -0.4107 -0.0700 136 SER   G CA  
12241 C  C   . SER   G  145 ? 1.5811 0.6902 1.2016 0.0332  -0.4057 -0.0950 136 SER   G C   
12242 O  O   . SER   G  145 ? 1.5582 0.6041 1.2132 0.1049  -0.4059 -0.1262 136 SER   G O   
12243 C  CB  . SER   G  145 ? 1.5477 0.7908 1.2073 0.0177  -0.4279 -0.0812 136 SER   G CB  
12244 O  OG  . SER   G  145 ? 1.5049 0.8893 1.2500 0.0263  -0.4560 -0.0842 136 SER   G OG  
12245 N  N   . VAL   G  146 ? 1.6135 0.6860 1.1428 0.0089  -0.4230 -0.0902 137 VAL   G N   
12246 C  CA  . VAL   G  146 ? 1.6202 0.6018 1.0534 -0.0206 -0.4577 -0.1294 137 VAL   G CA  
12247 C  C   . VAL   G  146 ? 1.6251 0.5730 1.0329 -0.0379 -0.4668 -0.1170 137 VAL   G C   
12248 O  O   . VAL   G  146 ? 1.5713 0.5789 0.9347 -0.0812 -0.5032 -0.1802 137 VAL   G O   
12249 C  CB  . VAL   G  146 ? 1.6149 0.5724 0.9878 -0.0352 -0.5093 -0.2219 137 VAL   G CB  
12250 C  CG1 . VAL   G  146 ? 1.6202 0.5677 0.9650 -0.0328 -0.5360 -0.2816 137 VAL   G CG1 
12251 C  CG2 . VAL   G  146 ? 1.6320 0.5836 0.9592 -0.0576 -0.5308 -0.2369 137 VAL   G CG2 
12252 N  N   . ASP   G  147 ? 1.6796 0.5948 1.0550 -0.0587 -0.4553 -0.0977 138 ASP   G N   
12253 C  CA  . ASP   G  147 ? 1.7561 0.6356 1.1003 -0.0841 -0.4357 -0.1359 138 ASP   G CA  
12254 C  C   . ASP   G  147 ? 1.7985 0.6764 1.1304 -0.0721 -0.4416 -0.0706 138 ASP   G C   
12255 O  O   . ASP   G  147 ? 1.8457 0.6598 1.0920 -0.0979 -0.4520 -0.0450 138 ASP   G O   
12256 C  CB  . ASP   G  147 ? 1.7974 0.6924 1.1418 -0.1067 -0.4198 -0.1108 138 ASP   G CB  
12257 C  CG  . ASP   G  147 ? 1.8130 0.7195 1.1357 -0.1405 -0.4652 -0.1138 138 ASP   G CG  
12258 O  OD1 . ASP   G  147 ? 1.8453 0.6682 1.1570 -0.1959 -0.4818 -0.0703 138 ASP   G OD1 
12259 O  OD2 . ASP   G  147 ? 1.8718 0.7229 1.2116 -0.1086 -0.3979 -0.0681 138 ASP   G OD2 
12260 N  N   . GLU   G  148 ? 1.8398 0.6940 1.2322 -0.0716 -0.3799 -0.1145 139 GLU   G N   
12261 C  CA  . GLU   G  148 ? 1.8088 0.8104 1.3320 -0.0107 -0.3911 -0.1323 139 GLU   G CA  
12262 C  C   . GLU   G  148 ? 1.8025 0.9145 1.3244 -0.0276 -0.4013 -0.1227 139 GLU   G C   
12263 O  O   . GLU   G  148 ? 1.7974 0.9543 1.3913 -0.0141 -0.3813 -0.0898 139 GLU   G O   
12264 C  CB  . GLU   G  148 ? 1.8544 0.8161 1.4004 -0.0130 -0.3665 -0.1744 139 GLU   G CB  
12265 C  CG  . GLU   G  148 ? 1.8756 0.8058 1.3987 0.0117  -0.3321 -0.1749 139 GLU   G CG  
12266 C  CD  . GLU   G  148 ? 1.8714 0.7194 1.4241 0.0794  -0.3481 -0.1163 139 GLU   G CD  
12267 O  OE1 . GLU   G  148 ? 1.9039 0.5843 1.3869 0.0371  -0.3480 -0.1394 139 GLU   G OE1 
12268 O  OE2 . GLU   G  148 ? 1.9014 0.6432 1.5896 0.1702  -0.2516 -0.1420 139 GLU   G OE2 
12269 N  N   . GLU   G  149 ? 1.7415 0.9248 1.2783 -0.0017 -0.4674 -0.1243 140 GLU   G N   
12270 C  CA  . GLU   G  149 ? 1.6977 0.9194 1.2894 -0.0372 -0.5342 -0.1377 140 GLU   G CA  
12271 C  C   . GLU   G  149 ? 1.6610 0.8792 1.2655 0.0065  -0.5695 -0.1049 140 GLU   G C   
12272 O  O   . GLU   G  149 ? 1.6182 1.0320 1.3987 0.0562  -0.5567 -0.0955 140 GLU   G O   
12273 C  CB  . GLU   G  149 ? 1.7299 0.9695 1.2900 -0.0685 -0.5076 -0.1352 140 GLU   G CB  
12274 C  CG  . GLU   G  149 ? 1.7867 1.0065 1.2698 -0.1233 -0.5284 -0.1748 140 GLU   G CG  
12275 C  CD  . GLU   G  149 ? 1.7963 0.9930 1.2579 -0.1583 -0.5593 -0.1591 140 GLU   G CD  
12276 O  OE1 . GLU   G  149 ? 1.7930 0.9357 1.2192 -0.2344 -0.6336 -0.2298 140 GLU   G OE1 
12277 O  OE2 . GLU   G  149 ? 1.7037 1.1697 1.3188 -0.1807 -0.6366 -0.0006 140 GLU   G OE2 
12278 N  N   . LEU   G  150 ? 1.6857 0.8021 1.2327 -0.0424 -0.5830 -0.0738 141 LEU   G N   
12279 C  CA  . LEU   G  150 ? 1.7222 0.8134 1.2501 -0.0702 -0.5725 -0.1006 141 LEU   G CA  
12280 C  C   . LEU   G  150 ? 1.6839 0.6978 1.2513 -0.0526 -0.5733 -0.0847 141 LEU   G C   
12281 O  O   . LEU   G  150 ? 1.6461 0.6939 1.3209 -0.0701 -0.5621 -0.0494 141 LEU   G O   
12282 C  CB  . LEU   G  150 ? 1.7692 0.7437 1.2257 -0.0959 -0.5716 -0.1244 141 LEU   G CB  
12283 C  CG  . LEU   G  150 ? 1.8237 0.8013 1.2342 -0.1526 -0.5507 -0.1602 141 LEU   G CG  
12284 C  CD1 . LEU   G  150 ? 1.8504 0.7545 1.2046 -0.1798 -0.5593 -0.1696 141 LEU   G CD1 
12285 C  CD2 . LEU   G  150 ? 1.8172 0.7983 1.2435 -0.1853 -0.5605 -0.1817 141 LEU   G CD2 
12286 N  N   . GLY   G  151 ? 1.6596 0.6396 1.2753 -0.0450 -0.5599 -0.1269 142 GLY   G N   
12287 C  CA  . GLY   G  151 ? 1.6662 0.5821 1.2868 -0.0107 -0.5674 -0.1387 142 GLY   G CA  
12288 C  C   . GLY   G  151 ? 1.6872 0.5352 1.2958 -0.0064 -0.5862 -0.0868 142 GLY   G C   
12289 O  O   . GLY   G  151 ? 1.6630 0.4631 1.2939 -0.0729 -0.5895 -0.0972 142 GLY   G O   
12290 N  N   . PRO   G  152 ? 1.7321 0.4337 1.3071 0.0681  -0.5522 -0.0547 143 PRO   G N   
12291 C  CA  . PRO   G  152 ? 1.7418 0.4038 1.3007 0.0448  -0.5124 -0.0936 143 PRO   G CA  
12292 C  C   . PRO   G  152 ? 1.7318 0.4312 1.3200 0.0374  -0.4423 -0.0738 143 PRO   G C   
12293 O  O   . PRO   G  152 ? 1.7646 0.3489 1.3826 0.0004  -0.4389 -0.1190 143 PRO   G O   
12294 C  CB  . PRO   G  152 ? 1.7528 0.3713 1.3080 0.0465  -0.5359 -0.0822 143 PRO   G CB  
12295 C  CG  . PRO   G  152 ? 1.7824 0.3419 1.3531 0.0609  -0.5459 -0.0932 143 PRO   G CG  
12296 C  CD  . PRO   G  152 ? 1.7520 0.4391 1.3124 0.0800  -0.5608 -0.0826 143 PRO   G CD  
12297 N  N   . SER   G  153 ? 1.7020 0.4910 1.2794 0.0688  -0.3911 -0.0539 144 SER   G N   
12298 C  CA  . SER   G  153 ? 1.6840 0.5232 1.2707 0.0708  -0.3504 -0.0423 144 SER   G CA  
12299 C  C   . SER   G  153 ? 1.6936 0.4542 1.1456 0.0492  -0.3385 -0.0729 144 SER   G C   
12300 O  O   . SER   G  153 ? 1.7008 0.3974 1.1315 0.0432  -0.3495 -0.0647 144 SER   G O   
12301 C  CB  . SER   G  153 ? 1.6742 0.4809 1.2953 0.1208  -0.3215 -0.0393 144 SER   G CB  
12302 O  OG  . SER   G  153 ? 1.7056 0.5074 1.4208 0.1555  -0.2674 0.0045  144 SER   G OG  
12303 N  N   . ILE   G  154 ? 1.7007 0.4579 1.0824 -0.0038 -0.3413 -0.1071 145 ILE   G N   
12304 C  CA  . ILE   G  154 ? 1.6543 0.4614 1.0687 -0.0389 -0.3469 -0.1035 145 ILE   G CA  
12305 C  C   . ILE   G  154 ? 1.6396 0.4315 1.0777 -0.1056 -0.3184 -0.1089 145 ILE   G C   
12306 O  O   . ILE   G  154 ? 1.7286 0.3311 1.0458 -0.2100 -0.3256 -0.1646 145 ILE   G O   
12307 C  CB  . ILE   G  154 ? 1.6364 0.4423 1.0926 -0.0252 -0.3588 -0.1008 145 ILE   G CB  
12308 C  CG1 . ILE   G  154 ? 1.6508 0.4717 1.0939 -0.0174 -0.3880 -0.0998 145 ILE   G CG1 
12309 C  CG2 . ILE   G  154 ? 1.6561 0.4152 1.0845 -0.0249 -0.3570 -0.0799 145 ILE   G CG2 
12310 C  CD1 . ILE   G  154 ? 1.6663 0.4967 1.0934 -0.0067 -0.4048 -0.1126 145 ILE   G CD1 
12311 N  N   . TYR   G  155 ? 1.6362 0.4777 1.0695 -0.0672 -0.3296 -0.0638 146 TYR   G N   
12312 C  CA  . TYR   G  155 ? 1.6198 0.5345 1.0850 -0.0317 -0.3510 -0.0339 146 TYR   G CA  
12313 C  C   . TYR   G  155 ? 1.6204 0.5643 1.0964 -0.0275 -0.3725 -0.0757 146 TYR   G C   
12314 O  O   . TYR   G  155 ? 1.6192 0.6784 1.0407 -0.0290 -0.3914 -0.0034 146 TYR   G O   
12315 C  CB  . TYR   G  155 ? 1.5975 0.5225 1.0839 -0.0169 -0.3378 -0.0183 146 TYR   G CB  
12316 C  CG  . TYR   G  155 ? 1.6210 0.5228 1.1350 0.0104  -0.3435 -0.0311 146 TYR   G CG  
12317 C  CD1 . TYR   G  155 ? 1.6013 0.4827 1.1478 0.0019  -0.3357 -0.0302 146 TYR   G CD1 
12318 C  CD2 . TYR   G  155 ? 1.6191 0.5626 1.1570 0.0292  -0.3316 -0.0412 146 TYR   G CD2 
12319 C  CE1 . TYR   G  155 ? 1.5923 0.5326 1.1870 0.0050  -0.3938 -0.0447 146 TYR   G CE1 
12320 C  CE2 . TYR   G  155 ? 1.6072 0.5573 1.2019 0.0255  -0.3870 -0.0467 146 TYR   G CE2 
12321 C  CZ  . TYR   G  155 ? 1.5617 0.5587 1.2043 0.0078  -0.3994 -0.0483 146 TYR   G CZ  
12322 O  OH  . TYR   G  155 ? 1.5347 0.6279 1.2900 -0.0061 -0.4768 -0.0538 146 TYR   G OH  
12323 N  N   . LYS   G  156 ? 1.6962 0.4703 1.1339 -0.0192 -0.3923 -0.1429 147 LYS   G N   
12324 C  CA  . LYS   G  156 ? 1.7256 0.4629 1.2004 0.0010  -0.3842 -0.1551 147 LYS   G CA  
12325 C  C   . LYS   G  156 ? 1.7396 0.3727 1.2235 0.0284  -0.4023 -0.1486 147 LYS   G C   
12326 O  O   . LYS   G  156 ? 1.7592 0.1928 1.3258 0.0254  -0.3696 -0.1251 147 LYS   G O   
12327 C  CB  . LYS   G  156 ? 1.7472 0.5026 1.1678 -0.0250 -0.3944 -0.1625 147 LYS   G CB  
12328 C  CG  . LYS   G  156 ? 1.7585 0.5154 1.1824 -0.0179 -0.3720 -0.1174 147 LYS   G CG  
12329 C  CD  . LYS   G  156 ? 1.8135 0.4764 1.2083 -0.0572 -0.3503 -0.1155 147 LYS   G CD  
12330 C  CE  . LYS   G  156 ? 1.8517 0.4983 1.1935 -0.0867 -0.3290 -0.1292 147 LYS   G CE  
12331 N  NZ  . LYS   G  156 ? 1.8763 0.5655 1.1968 -0.0898 -0.3215 -0.1583 147 LYS   G NZ  
12332 N  N   . THR   G  157 ? 1.7319 0.3864 1.1996 0.0223  -0.3945 -0.1657 148 THR   G N   
12333 C  CA  . THR   G  157 ? 1.7463 0.4646 1.1767 -0.0006 -0.3899 -0.1700 148 THR   G CA  
12334 C  C   . THR   G  157 ? 1.7026 0.4444 1.1628 -0.0351 -0.3770 -0.1520 148 THR   G C   
12335 O  O   . THR   G  157 ? 1.6715 0.4448 1.1526 -0.0887 -0.3556 -0.0712 148 THR   G O   
12336 C  CB  . THR   G  157 ? 1.7620 0.4609 1.1632 0.0218  -0.4195 -0.1821 148 THR   G CB  
12337 O  OG1 . THR   G  157 ? 1.8378 0.4199 1.0766 0.0361  -0.4473 -0.1765 148 THR   G OG1 
12338 C  CG2 . THR   G  157 ? 1.7727 0.5058 1.1601 -0.0052 -0.4128 -0.1611 148 THR   G CG2 
12339 N  N   . ASP   G  158 ? 1.7175 0.6021 1.0995 -0.0618 -0.3353 -0.1538 149 ASP   G N   
12340 C  CA  . ASP   G  158 ? 1.6773 0.7405 1.1498 0.0257  -0.3141 -0.1541 149 ASP   G CA  
12341 C  C   . ASP   G  158 ? 1.6066 0.6964 1.1680 0.0871  -0.3205 -0.1439 149 ASP   G C   
12342 O  O   . ASP   G  158 ? 1.6831 0.8699 1.1357 0.1443  -0.3630 -0.2116 149 ASP   G O   
12343 C  CB  . ASP   G  158 ? 1.6952 0.7867 1.2306 -0.0160 -0.2598 -0.1384 149 ASP   G CB  
12344 C  CG  . ASP   G  158 ? 1.7351 0.9202 1.2460 -0.0271 -0.2303 -0.0960 149 ASP   G CG  
12345 O  OD1 . ASP   G  158 ? 1.7266 0.9659 1.1731 -0.0892 -0.1983 -0.0364 149 ASP   G OD1 
12346 O  OD2 . ASP   G  158 ? 1.6782 1.0131 1.3668 -0.0407 -0.1896 -0.1243 149 ASP   G OD2 
12347 N  N   . PRO   G  159 ? 1.6039 0.5444 1.1058 0.0397  -0.2709 -0.1671 150 PRO   G N   
12348 C  CA  . PRO   G  159 ? 1.5760 0.5119 1.1055 0.0958  -0.2554 -0.0918 150 PRO   G CA  
12349 C  C   . PRO   G  159 ? 1.5641 0.5149 1.1680 0.1358  -0.2259 -0.0137 150 PRO   G C   
12350 O  O   . PRO   G  159 ? 1.5554 0.4964 1.0840 0.2750  -0.2123 0.0775  150 PRO   G O   
12351 C  CB  . PRO   G  159 ? 1.5964 0.4089 1.0727 0.0458  -0.2785 -0.1195 150 PRO   G CB  
12352 C  CG  . PRO   G  159 ? 1.6021 0.3898 1.0847 0.0238  -0.2624 -0.1401 150 PRO   G CG  
12353 C  CD  . PRO   G  159 ? 1.5966 0.4523 1.1277 0.0178  -0.2668 -0.1385 150 PRO   G CD  
12354 N  N   . ALA   G  160 ? 1.5839 0.4625 1.1649 0.1180  -0.2322 -0.0479 151 ALA   G N   
12355 C  CA  . ALA   G  160 ? 1.5747 0.4914 1.1836 0.1057  -0.2265 -0.0556 151 ALA   G CA  
12356 C  C   . ALA   G  160 ? 1.5406 0.5583 1.1794 0.1019  -0.2184 -0.1366 151 ALA   G C   
12357 O  O   . ALA   G  160 ? 1.4960 0.5180 1.1763 0.0516  -0.2196 -0.1593 151 ALA   G O   
12358 C  CB  . ALA   G  160 ? 1.5989 0.4696 1.1765 0.1038  -0.2265 -0.0520 151 ALA   G CB  
12359 N  N   . GLY   G  161 ? 1.5439 0.5469 1.1939 0.1294  -0.2444 -0.1459 152 GLY   G N   
12360 C  CA  . GLY   G  161 ? 1.5548 0.5931 1.2187 0.1574  -0.2718 -0.2296 152 GLY   G CA  
12361 C  C   . GLY   G  161 ? 1.5737 0.6488 1.2719 0.1654  -0.3039 -0.2414 152 GLY   G C   
12362 O  O   . GLY   G  161 ? 1.5968 0.7377 1.3055 0.2035  -0.2960 -0.2981 152 GLY   G O   
12363 N  N   . TYR   G  162 ? 1.6096 0.6282 1.2951 0.1659  -0.3166 -0.2300 153 TYR   G N   
12364 C  CA  . TYR   G  162 ? 1.6371 0.6538 1.2762 0.1735  -0.3405 -0.2106 153 TYR   G CA  
12365 C  C   . TYR   G  162 ? 1.6165 0.5912 1.2301 0.1424  -0.4064 -0.2613 153 TYR   G C   
12366 O  O   . TYR   G  162 ? 1.5894 0.5569 1.1900 0.1219  -0.4317 -0.3184 153 TYR   G O   
12367 C  CB  . TYR   G  162 ? 1.6201 0.6424 1.3002 0.1866  -0.3173 -0.2066 153 TYR   G CB  
12368 C  CG  . TYR   G  162 ? 1.5586 0.6845 1.4016 0.2373  -0.3179 -0.1181 153 TYR   G CG  
12369 C  CD1 . TYR   G  162 ? 1.5833 0.7152 1.4171 0.2742  -0.2745 -0.0771 153 TYR   G CD1 
12370 C  CD2 . TYR   G  162 ? 1.6179 0.7701 1.4416 0.2689  -0.2448 -0.0552 153 TYR   G CD2 
12371 C  CE1 . TYR   G  162 ? 1.6050 0.8123 1.4692 0.2583  -0.3032 -0.0792 153 TYR   G CE1 
12372 C  CE2 . TYR   G  162 ? 1.6379 0.8273 1.4770 0.2414  -0.2623 -0.0309 153 TYR   G CE2 
12373 C  CZ  . TYR   G  162 ? 1.6281 0.8237 1.4730 0.2200  -0.3003 -0.0483 153 TYR   G CZ  
12374 O  OH  . TYR   G  162 ? 1.6346 0.7862 1.5411 0.1506  -0.3276 0.0226  153 TYR   G OH  
12375 N  N   . TYR   G  163 ? 1.6427 0.4510 1.2057 0.1117  -0.4281 -0.2502 154 TYR   G N   
12376 C  CA  . TYR   G  163 ? 1.6873 0.4743 1.1967 0.0733  -0.3901 -0.2245 154 TYR   G CA  
12377 C  C   . TYR   G  163 ? 1.7156 0.3692 1.1501 0.0143  -0.4281 -0.1974 154 TYR   G C   
12378 O  O   . TYR   G  163 ? 1.7769 0.4274 1.1522 -0.0218 -0.4091 -0.2546 154 TYR   G O   
12379 C  CB  . TYR   G  163 ? 1.6469 0.5224 1.1577 0.0291  -0.4137 -0.1960 154 TYR   G CB  
12380 C  CG  . TYR   G  163 ? 1.6517 0.6106 1.1618 0.0569  -0.3880 -0.2240 154 TYR   G CG  
12381 C  CD1 . TYR   G  163 ? 1.6307 0.6505 1.1690 0.0597  -0.3693 -0.2183 154 TYR   G CD1 
12382 C  CD2 . TYR   G  163 ? 1.6510 0.6656 1.1741 0.0773  -0.4094 -0.2282 154 TYR   G CD2 
12383 C  CE1 . TYR   G  163 ? 1.5925 0.7310 1.1978 0.0804  -0.3399 -0.2016 154 TYR   G CE1 
12384 C  CE2 . TYR   G  163 ? 1.5931 0.7370 1.2065 0.0706  -0.3700 -0.2570 154 TYR   G CE2 
12385 C  CZ  . TYR   G  163 ? 1.5293 0.7204 1.2242 0.1156  -0.3433 -0.2275 154 TYR   G CZ  
12386 O  OH  . TYR   G  163 ? 1.5163 0.7181 1.3715 0.0902  -0.2826 -0.2603 154 TYR   G OH  
12387 N  N   . VAL   G  164 ? 1.7468 0.3534 1.1285 -0.0280 -0.3691 -0.1668 155 VAL   G N   
12388 C  CA  . VAL   G  164 ? 1.7287 0.3992 1.1692 -0.0513 -0.3456 -0.1421 155 VAL   G CA  
12389 C  C   . VAL   G  164 ? 1.7102 0.3912 1.1688 -0.0432 -0.3373 -0.1390 155 VAL   G C   
12390 O  O   . VAL   G  164 ? 1.7349 0.3260 1.1080 -0.0779 -0.3225 -0.1489 155 VAL   G O   
12391 C  CB  . VAL   G  164 ? 1.7450 0.3976 1.1816 -0.0574 -0.3171 -0.1036 155 VAL   G CB  
12392 C  CG1 . VAL   G  164 ? 1.7573 0.3655 1.1734 -0.0588 -0.2956 -0.0760 155 VAL   G CG1 
12393 C  CG2 . VAL   G  164 ? 1.7411 0.4347 1.2182 -0.0685 -0.3241 -0.1060 155 VAL   G CG2 
12394 N  N   . GLY   G  165 ? 1.7207 0.4213 1.1825 -0.0384 -0.3465 -0.1053 156 GLY   G N   
12395 C  CA  . GLY   G  165 ? 1.7432 0.4614 1.1824 -0.0325 -0.3299 -0.1044 156 GLY   G CA  
12396 C  C   . GLY   G  165 ? 1.7589 0.3777 1.2324 -0.0234 -0.3059 -0.0903 156 GLY   G C   
12397 O  O   . GLY   G  165 ? 1.8169 0.2222 1.2025 0.0265  -0.3089 -0.1654 156 GLY   G O   
12398 N  N   . TYR   G  166 ? 1.7620 0.4838 1.2251 -0.0069 -0.3202 -0.1016 157 TYR   G N   
12399 C  CA  . TYR   G  166 ? 1.7502 0.4598 1.2691 -0.0405 -0.3482 -0.0980 157 TYR   G CA  
12400 C  C   . TYR   G  166 ? 1.7616 0.5742 1.3015 -0.0603 -0.3792 -0.0552 157 TYR   G C   
12401 O  O   . TYR   G  166 ? 1.7916 0.7120 1.2544 -0.1487 -0.3896 0.1050  157 TYR   G O   
12402 C  CB  . TYR   G  166 ? 1.7565 0.5020 1.2545 -0.0455 -0.3294 -0.1256 157 TYR   G CB  
12403 C  CG  . TYR   G  166 ? 1.7540 0.5253 1.2529 -0.0457 -0.3227 -0.1127 157 TYR   G CG  
12404 C  CD1 . TYR   G  166 ? 1.6940 0.5472 1.2988 -0.0731 -0.3337 -0.0738 157 TYR   G CD1 
12405 C  CD2 . TYR   G  166 ? 1.7785 0.4956 1.2463 0.0130  -0.2867 -0.1487 157 TYR   G CD2 
12406 C  CE1 . TYR   G  166 ? 1.6813 0.5091 1.3473 -0.0409 -0.3155 -0.0728 157 TYR   G CE1 
12407 C  CE2 . TYR   G  166 ? 1.7331 0.4373 1.2609 0.0144  -0.2701 -0.1615 157 TYR   G CE2 
12408 C  CZ  . TYR   G  166 ? 1.6702 0.4674 1.2880 0.0416  -0.3151 -0.0909 157 TYR   G CZ  
12409 O  OH  . TYR   G  166 ? 1.6194 0.3522 1.4107 0.1155  -0.2553 -0.0784 157 TYR   G OH  
12410 N  N   . LYS   G  167 ? 1.7639 0.4845 1.3445 -0.0849 -0.3739 -0.0032 158 LYS   G N   
12411 C  CA  . LYS   G  167 ? 1.7478 0.5009 1.3362 -0.1273 -0.3765 -0.0062 158 LYS   G CA  
12412 C  C   . LYS   G  167 ? 1.7458 0.4203 1.2803 -0.1218 -0.4044 -0.0751 158 LYS   G C   
12413 O  O   . LYS   G  167 ? 1.6997 0.4588 1.2374 -0.1508 -0.3548 -0.1031 158 LYS   G O   
12414 C  CB  . LYS   G  167 ? 1.7629 0.5977 1.4086 -0.1772 -0.4166 0.0303  158 LYS   G CB  
12415 C  CG  . LYS   G  167 ? 1.7585 0.7629 1.5261 -0.1770 -0.3925 0.0517  158 LYS   G CG  
12416 C  CD  . LYS   G  167 ? 1.7455 0.8814 1.6767 -0.2440 -0.3962 0.0498  158 LYS   G CD  
12417 C  CE  . LYS   G  167 ? 1.6922 0.9694 1.7796 -0.2537 -0.3863 0.0792  158 LYS   G CE  
12418 N  NZ  . LYS   G  167 ? 1.6911 0.9386 1.8147 -0.2319 -0.3870 0.0980  158 LYS   G NZ  
12419 N  N   . ALA   G  168 ? 1.7221 0.4196 1.1779 -0.1388 -0.4216 -0.0693 159 ALA   G N   
12420 C  CA  . ALA   G  168 ? 1.7272 0.4584 1.1366 -0.1796 -0.4175 -0.1274 159 ALA   G CA  
12421 C  C   . ALA   G  168 ? 1.7145 0.4101 1.2221 -0.1590 -0.4336 -0.1590 159 ALA   G C   
12422 O  O   . ALA   G  168 ? 1.6869 0.4043 1.2667 -0.1914 -0.4428 -0.1701 159 ALA   G O   
12423 C  CB  . ALA   G  168 ? 1.7432 0.4966 1.1019 -0.1680 -0.4227 -0.0986 159 ALA   G CB  
12424 N  N   . THR   G  169 ? 1.7298 0.3013 1.2450 -0.1625 -0.3836 -0.1651 160 THR   G N   
12425 C  CA  . THR   G  169 ? 1.7784 0.2663 1.3146 -0.1398 -0.3677 -0.1396 160 THR   G CA  
12426 C  C   . THR   G  169 ? 1.7942 0.2626 1.2779 -0.1679 -0.3666 -0.1905 160 THR   G C   
12427 O  O   . THR   G  169 ? 1.8068 0.1370 1.2648 -0.1375 -0.4516 -0.1909 160 THR   G O   
12428 C  CB  . THR   G  169 ? 1.8015 0.2555 1.3173 -0.1716 -0.3657 -0.1219 160 THR   G CB  
12429 O  OG1 . THR   G  169 ? 1.8498 0.3727 1.3857 -0.1248 -0.3797 -0.0555 160 THR   G OG1 
12430 C  CG2 . THR   G  169 ? 1.8267 0.2586 1.3102 -0.1861 -0.3808 -0.1198 160 THR   G CG2 
12431 N  N   . ALA   G  170 ? 1.7413 0.3238 1.3064 -0.0875 -0.3771 -0.2383 161 ALA   G N   
12432 C  CA  . ALA   G  170 ? 1.7383 0.3528 1.2765 -0.0935 -0.3670 -0.2574 161 ALA   G CA  
12433 C  C   . ALA   G  170 ? 1.7150 0.3098 1.2631 -0.0755 -0.3182 -0.2160 161 ALA   G C   
12434 O  O   . ALA   G  170 ? 1.7261 0.1856 1.2035 -0.0443 -0.3486 -0.2276 161 ALA   G O   
12435 C  CB  . ALA   G  170 ? 1.7618 0.3677 1.3064 -0.0860 -0.3539 -0.2850 161 ALA   G CB  
12436 N  N   . THR   G  171 ? 1.7180 0.3508 1.2642 -0.0586 -0.2877 -0.1617 162 THR   G N   
12437 C  CA  . THR   G  171 ? 1.7084 0.4726 1.2841 -0.0631 -0.2833 -0.1287 162 THR   G CA  
12438 C  C   . THR   G  171 ? 1.7313 0.4880 1.2906 -0.0672 -0.2331 -0.0815 162 THR   G C   
12439 O  O   . THR   G  171 ? 1.7799 0.3654 1.3099 -0.0821 -0.2945 0.0022  162 THR   G O   
12440 C  CB  . THR   G  171 ? 1.6835 0.5860 1.2880 -0.1201 -0.2735 -0.1713 162 THR   G CB  
12441 O  OG1 . THR   G  171 ? 1.5939 0.6767 1.3129 -0.1556 -0.2590 -0.2187 162 THR   G OG1 
12442 C  CG2 . THR   G  171 ? 1.6711 0.7019 1.2698 -0.1289 -0.2830 -0.1933 162 THR   G CG2 
12443 N  N   . GLY   G  172 ? 1.7379 0.5005 1.3806 -0.0206 -0.2058 -0.0600 163 GLY   G N   
12444 C  CA  . GLY   G  172 ? 1.7729 0.4837 1.3130 0.0148  -0.2032 -0.0265 163 GLY   G CA  
12445 C  C   . GLY   G  172 ? 1.7953 0.4798 1.2538 0.0294  -0.1802 -0.0496 163 GLY   G C   
12446 O  O   . GLY   G  172 ? 1.8228 0.4561 1.2076 0.0193  -0.1524 -0.0820 163 GLY   G O   
12447 N  N   . PRO   G  173 ? 1.8237 0.4680 1.2226 0.0557  -0.1907 -0.0281 164 PRO   G N   
12448 C  CA  . PRO   G  173 ? 1.8469 0.4649 1.2284 0.0774  -0.1883 -0.0243 164 PRO   G CA  
12449 C  C   . PRO   G  173 ? 1.8890 0.5031 1.2000 0.1127  -0.2379 -0.0345 164 PRO   G C   
12450 O  O   . PRO   G  173 ? 1.9177 0.5459 1.1950 0.1002  -0.1777 -0.0692 164 PRO   G O   
12451 C  CB  . PRO   G  173 ? 1.8505 0.4571 1.2174 0.0644  -0.1784 -0.0294 164 PRO   G CB  
12452 C  CG  . PRO   G  173 ? 1.8053 0.4649 1.1959 0.0762  -0.1880 -0.0303 164 PRO   G CG  
12453 C  CD  . PRO   G  173 ? 1.8163 0.4385 1.1883 0.0600  -0.2011 -0.0235 164 PRO   G CD  
12454 N  N   . LYS   G  174 ? 1.9098 0.5133 1.2403 0.0849  -0.2309 0.0273  165 LYS   G N   
12455 C  CA  . LYS   G  174 ? 1.9586 0.6384 1.2353 0.0917  -0.2840 0.0615  165 LYS   G CA  
12456 C  C   . LYS   G  174 ? 1.9656 0.5386 1.1612 0.0582  -0.3480 0.1324  165 LYS   G C   
12457 O  O   . LYS   G  174 ? 2.0208 0.5278 1.1471 0.0612  -0.3610 0.1192  165 LYS   G O   
12458 C  CB  . LYS   G  174 ? 1.9914 0.8297 1.2211 0.0999  -0.2774 0.1064  165 LYS   G CB  
12459 C  CG  . LYS   G  174 ? 1.9681 1.0137 1.3362 0.2056  -0.2310 0.1238  165 LYS   G CG  
12460 C  CD  . LYS   G  174 ? 2.0096 1.2073 1.3355 0.1750  -0.2081 0.1183  165 LYS   G CD  
12461 C  CE  . LYS   G  174 ? 2.0095 1.2585 1.4352 0.1799  -0.1990 0.2105  165 LYS   G CE  
12462 N  NZ  . LYS   G  174 ? 1.9959 1.3489 1.4628 0.1859  -0.1865 0.2446  165 LYS   G NZ  
12463 N  N   . GLN   G  175 ? 1.9706 0.4886 1.2396 0.0043  -0.2775 0.0901  166 GLN   G N   
12464 C  CA  . GLN   G  175 ? 1.9355 0.4805 1.2907 -0.0234 -0.2759 0.0663  166 GLN   G CA  
12465 C  C   . GLN   G  175 ? 1.9700 0.5295 1.3353 -0.0774 -0.2573 0.0238  166 GLN   G C   
12466 O  O   . GLN   G  175 ? 1.8943 0.3790 1.3457 -0.1467 -0.2641 -0.0447 166 GLN   G O   
12467 C  CB  . GLN   G  175 ? 1.9398 0.5626 1.2613 -0.0297 -0.2677 0.0879  166 GLN   G CB  
12468 C  CG  . GLN   G  175 ? 1.9136 0.6540 1.2894 -0.0558 -0.2580 0.1284  166 GLN   G CG  
12469 C  CD  . GLN   G  175 ? 1.9157 0.6769 1.3376 -0.0962 -0.2250 0.1444  166 GLN   G CD  
12470 O  OE1 . GLN   G  175 ? 1.9526 0.6705 1.2746 -0.1311 -0.2633 -0.0236 166 GLN   G OE1 
12471 N  NE2 . GLN   G  175 ? 1.8826 0.7909 1.4021 -0.0724 -0.2317 0.1683  166 GLN   G NE2 
12472 N  N   . GLN   G  176 ? 2.0244 0.5689 1.3830 -0.1253 -0.1991 0.0481  167 GLN   G N   
12473 C  CA  . GLN   G  176 ? 2.0593 0.6145 1.4007 -0.1542 -0.1793 -0.0320 167 GLN   G CA  
12474 C  C   . GLN   G  176 ? 2.1615 0.6048 1.4129 -0.1058 -0.2012 -0.1078 167 GLN   G C   
12475 O  O   . GLN   G  176 ? 2.1892 0.5460 1.4231 -0.0627 -0.2359 -0.1607 167 GLN   G O   
12476 C  CB  . GLN   G  176 ? 2.1050 0.5793 1.4159 -0.1782 -0.0981 -0.0535 167 GLN   G CB  
12477 C  CG  . GLN   G  176 ? 2.1596 0.5635 1.4439 -0.2252 -0.0633 -0.0283 167 GLN   G CG  
12478 C  CD  . GLN   G  176 ? 2.1180 0.6085 1.4859 -0.2376 -0.0329 -0.0243 167 GLN   G CD  
12479 O  OE1 . GLN   G  176 ? 2.1700 0.7877 1.4198 -0.2318 0.0341  -0.0045 167 GLN   G OE1 
12480 N  NE2 . GLN   G  176 ? 2.0892 0.5945 1.4620 -0.2649 -0.0373 -0.0793 167 GLN   G NE2 
12481 N  N   . GLU   G  177 ? 2.1325 0.5922 1.4468 -0.0753 -0.2207 -0.1417 168 GLU   G N   
12482 C  CA  . GLU   G  177 ? 2.1262 0.7169 1.4677 -0.0555 -0.2685 -0.1516 168 GLU   G CA  
12483 C  C   . GLU   G  177 ? 2.0557 0.7179 1.3890 -0.0852 -0.3300 -0.1717 168 GLU   G C   
12484 O  O   . GLU   G  177 ? 2.1068 0.8145 1.3680 -0.1198 -0.3608 -0.1637 168 GLU   G O   
12485 C  CB  . GLU   G  177 ? 2.1455 1.0382 1.4887 -0.0118 -0.2327 -0.1531 168 GLU   G CB  
12486 C  CG  . GLU   G  177 ? 2.2279 1.1384 1.6206 0.1645  -0.1519 -0.1629 168 GLU   G CG  
12487 C  CD  . GLU   G  177 ? 2.2129 1.4507 1.7106 0.2457  -0.1627 -0.1774 168 GLU   G CD  
12488 O  OE1 . GLU   G  177 ? 2.5180 1.3379 1.8012 0.2393  0.0017  -0.3536 168 GLU   G OE1 
12489 O  OE2 . GLU   G  177 ? 2.3428 1.8842 1.6240 0.2088  -0.1745 -0.1555 168 GLU   G OE2 
12490 N  N   . ILE   G  178 ? 1.9528 0.5837 1.3513 0.0483  -0.3491 -0.1545 169 ILE   G N   
12491 C  CA  . ILE   G  178 ? 1.8623 0.5429 1.2863 0.0501  -0.3528 -0.2117 169 ILE   G CA  
12492 C  C   . ILE   G  178 ? 1.8614 0.4542 1.3427 0.0810  -0.3546 -0.1870 169 ILE   G C   
12493 O  O   . ILE   G  178 ? 1.8430 0.6155 1.3241 0.0753  -0.3736 -0.1733 169 ILE   G O   
12494 C  CB  . ILE   G  178 ? 1.8065 0.4907 1.2047 0.1025  -0.3681 -0.1906 169 ILE   G CB  
12495 C  CG1 . ILE   G  178 ? 1.8121 0.4338 1.2103 0.1091  -0.3571 -0.1663 169 ILE   G CG1 
12496 C  CG2 . ILE   G  178 ? 1.7877 0.4826 1.1428 0.0697  -0.3819 -0.2016 169 ILE   G CG2 
12497 C  CD1 . ILE   G  178 ? 1.7598 0.4023 1.2558 0.1013  -0.3104 -0.1523 169 ILE   G CD1 
12498 N  N   . THR   G  179 ? 1.8578 0.4282 1.3638 0.0687  -0.3177 -0.1815 170 THR   G N   
12499 C  CA  . THR   G  179 ? 1.8369 0.5252 1.4394 0.0493  -0.3072 -0.2164 170 THR   G CA  
12500 C  C   . THR   G  179 ? 1.8421 0.5282 1.4547 0.0564  -0.3398 -0.2001 170 THR   G C   
12501 O  O   . THR   G  179 ? 1.8161 0.4278 1.3966 0.0037  -0.3659 -0.2482 170 THR   G O   
12502 C  CB  . THR   G  179 ? 1.8721 0.6253 1.4213 0.0323  -0.2695 -0.2375 170 THR   G CB  
12503 O  OG1 . THR   G  179 ? 1.8399 0.7594 1.4254 0.0075  -0.2244 -0.2688 170 THR   G OG1 
12504 C  CG2 . THR   G  179 ? 1.8575 0.6902 1.4790 0.0415  -0.2553 -0.2362 170 THR   G CG2 
12505 N  N   . THR   G  180 ? 1.8693 0.5485 1.5463 0.0666  -0.3021 -0.2491 171 THR   G N   
12506 C  CA  . THR   G  180 ? 1.8430 0.6112 1.5797 0.0786  -0.2949 -0.2477 171 THR   G CA  
12507 C  C   . THR   G  180 ? 1.9432 0.6504 1.5328 0.0376  -0.2506 -0.2558 171 THR   G C   
12508 O  O   . THR   G  180 ? 1.9707 0.7536 1.5691 -0.0300 -0.3284 -0.2587 171 THR   G O   
12509 C  CB  . THR   G  180 ? 1.8039 0.6334 1.6529 0.1827  -0.2123 -0.2804 171 THR   G CB  
12510 O  OG1 . THR   G  180 ? 1.8652 0.4553 1.6546 0.2824  -0.1681 -0.3463 171 THR   G OG1 
12511 C  CG2 . THR   G  180 ? 1.8472 0.6415 1.6822 0.1791  -0.2092 -0.2439 171 THR   G CG2 
12512 N  N   . ASN   G  181 ? 1.9582 0.5497 1.3773 0.0656  -0.2777 -0.2717 172 ASN   G N   
12513 C  CA  . ASN   G  181 ? 2.0033 0.5013 1.3676 0.0358  -0.3084 -0.2900 172 ASN   G CA  
12514 C  C   . ASN   G  181 ? 1.9858 0.5167 1.3621 0.0471  -0.3501 -0.2484 172 ASN   G C   
12515 O  O   . ASN   G  181 ? 2.0494 0.3628 1.3047 0.0551  -0.3665 -0.2885 172 ASN   G O   
12516 C  CB  . ASN   G  181 ? 2.0063 0.4420 1.3149 0.0227  -0.3275 -0.2567 172 ASN   G CB  
12517 C  CG  . ASN   G  181 ? 2.0300 0.4662 1.3311 -0.0119 -0.3752 -0.2294 172 ASN   G CG  
12518 O  OD1 . ASN   G  181 ? 1.9814 0.4860 1.2222 -0.0017 -0.4088 -0.1825 172 ASN   G OD1 
12519 N  ND2 . ASN   G  181 ? 2.0771 0.5290 1.2852 0.0260  -0.3882 -0.2173 172 ASN   G ND2 
12520 N  N   . LEU   G  182 ? 1.9512 0.5693 1.3900 0.0259  -0.3700 -0.2652 173 LEU   G N   
12521 C  CA  . LEU   G  182 ? 1.9325 0.5412 1.4499 0.0217  -0.4131 -0.2158 173 LEU   G CA  
12522 C  C   . LEU   G  182 ? 1.9335 0.5840 1.5092 0.0211  -0.4101 -0.2340 173 LEU   G C   
12523 O  O   . LEU   G  182 ? 1.9626 0.4508 1.5721 -0.0180 -0.4715 -0.2843 173 LEU   G O   
12524 C  CB  . LEU   G  182 ? 1.8591 0.4864 1.4931 0.0075  -0.4106 -0.1778 173 LEU   G CB  
12525 C  CG  . LEU   G  182 ? 1.8644 0.4998 1.4841 0.0017  -0.4133 -0.1564 173 LEU   G CG  
12526 C  CD1 . LEU   G  182 ? 1.8157 0.5301 1.5128 -0.0006 -0.4108 -0.1431 173 LEU   G CD1 
12527 C  CD2 . LEU   G  182 ? 1.8421 0.5450 1.4169 -0.0233 -0.4484 -0.1522 173 LEU   G CD2 
12528 N  N   . GLU   G  183 ? 1.9551 0.6612 1.5259 0.0183  -0.3707 -0.2025 174 GLU   G N   
12529 C  CA  . GLU   G  183 ? 1.9696 0.7150 1.5514 -0.0115 -0.3673 -0.1719 174 GLU   G CA  
12530 C  C   . GLU   G  183 ? 1.9667 0.6952 1.6080 -0.0271 -0.4164 -0.1224 174 GLU   G C   
12531 O  O   . GLU   G  183 ? 1.9659 0.7281 1.5993 -0.0236 -0.4272 -0.1065 174 GLU   G O   
12532 C  CB  . GLU   G  183 ? 2.0299 0.7278 1.5576 -0.0204 -0.2912 -0.1579 174 GLU   G CB  
12533 C  CG  . GLU   G  183 ? 2.0645 0.8159 1.5460 -0.0433 -0.2757 -0.1592 174 GLU   G CG  
12534 C  CD  . GLU   G  183 ? 2.1265 0.9231 1.5127 0.0011  -0.2490 -0.1076 174 GLU   G CD  
12535 O  OE1 . GLU   G  183 ? 2.1774 0.9917 1.4677 -0.0183 -0.2146 -0.2260 174 GLU   G OE1 
12536 O  OE2 . GLU   G  183 ? 2.0593 0.9982 1.5561 -0.0686 -0.2416 -0.0797 174 GLU   G OE2 
12537 N  N   . ASN   G  184 ? 1.9554 0.6586 1.6421 -0.0132 -0.4390 -0.1230 175 ASN   G N   
12538 C  CA  . ASN   G  184 ? 1.9947 0.8486 1.6855 -0.0551 -0.4824 -0.1189 175 ASN   G CA  
12539 C  C   . ASN   G  184 ? 2.0618 0.7765 1.7640 -0.1084 -0.4631 -0.1012 175 ASN   G C   
12540 O  O   . ASN   G  184 ? 2.0510 0.9038 1.9843 -0.0319 -0.4912 -0.0283 175 ASN   G O   
12541 C  CB  . ASN   G  184 ? 2.0076 0.9063 1.7104 0.0214  -0.4184 -0.0463 175 ASN   G CB  
12542 C  CG  . ASN   G  184 ? 2.0033 0.8672 1.7514 0.0027  -0.3677 -0.0440 175 ASN   G CG  
12543 O  OD1 . ASN   G  184 ? 2.1067 0.7627 1.7714 0.0508  -0.2604 -0.1903 175 ASN   G OD1 
12544 N  ND2 . ASN   G  184 ? 2.0191 0.9481 1.8316 -0.0510 -0.3584 0.0031  175 ASN   G ND2 
12545 N  N   . HIS   G  185 ? 1.9789 0.9070 1.7054 -0.1545 -0.4954 -0.1203 176 HIS   G N   
12546 C  CA  . HIS   G  185 ? 1.9435 0.9688 1.7105 -0.1410 -0.4880 -0.0781 176 HIS   G CA  
12547 C  C   . HIS   G  185 ? 1.9436 0.9710 1.7763 -0.1107 -0.5197 -0.0957 176 HIS   G C   
12548 O  O   . HIS   G  185 ? 1.8514 1.0384 1.9136 -0.0741 -0.5250 -0.1442 176 HIS   G O   
12549 C  CB  . HIS   G  185 ? 1.9363 0.9802 1.6277 -0.1327 -0.4677 -0.0642 176 HIS   G CB  
12550 C  CG  . HIS   G  185 ? 1.9313 1.0046 1.5846 -0.1755 -0.4552 -0.0396 176 HIS   G CG  
12551 N  ND1 . HIS   G  185 ? 1.9090 1.0189 1.5204 -0.1817 -0.4392 -0.0180 176 HIS   G ND1 
12552 C  CD2 . HIS   G  185 ? 1.9457 0.9828 1.5906 -0.1813 -0.4524 -0.0032 176 HIS   G CD2 
12553 C  CE1 . HIS   G  185 ? 1.8928 1.1237 1.5060 -0.1860 -0.4770 0.0293  176 HIS   G CE1 
12554 N  NE2 . HIS   G  185 ? 1.9126 1.0251 1.4837 -0.1524 -0.4889 0.0846  176 HIS   G NE2 
12555 N  N   . PHE   G  186 ? 1.9289 0.9879 1.7731 -0.1046 -0.5781 -0.0633 177 PHE   G N   
12556 C  CA  . PHE   G  186 ? 1.8962 1.0764 1.8591 -0.0674 -0.5769 -0.0564 177 PHE   G CA  
12557 C  C   . PHE   G  186 ? 1.9040 1.0959 1.8661 -0.0696 -0.5656 -0.0533 177 PHE   G C   
12558 O  O   . PHE   G  186 ? 1.9193 1.2502 1.8601 -0.0140 -0.5306 -0.0523 177 PHE   G O   
12559 C  CB  . PHE   G  186 ? 1.8639 1.1326 1.8866 -0.0730 -0.6198 -0.0307 177 PHE   G CB  
12560 C  CG  . PHE   G  186 ? 1.8590 1.0986 1.9049 -0.0579 -0.6796 0.0070  177 PHE   G CG  
12561 C  CD1 . PHE   G  186 ? 1.8742 1.0413 1.9487 -0.0822 -0.6938 -0.0210 177 PHE   G CD1 
12562 C  CD2 . PHE   G  186 ? 1.8281 1.0419 1.9074 -0.1401 -0.6821 -0.0277 177 PHE   G CD2 
12563 C  CE1 . PHE   G  186 ? 1.8085 1.0404 1.8723 -0.0620 -0.7624 -0.0370 177 PHE   G CE1 
12564 C  CE2 . PHE   G  186 ? 1.8495 0.9649 1.8761 -0.1364 -0.7176 -0.0580 177 PHE   G CE2 
12565 C  CZ  . PHE   G  186 ? 1.7994 1.0381 1.8391 -0.0731 -0.7525 -0.0390 177 PHE   G CZ  
12566 N  N   . LYS   G  187 ? 1.9285 1.0836 1.8491 -0.0262 -0.5355 -0.1298 178 LYS   G N   
12567 C  CA  . LYS   G  187 ? 1.9631 0.9988 1.8576 -0.0306 -0.5170 -0.1719 178 LYS   G CA  
12568 C  C   . LYS   G  187 ? 1.9717 0.7799 1.9128 -0.0706 -0.5652 -0.1641 178 LYS   G C   
12569 O  O   . LYS   G  187 ? 1.9542 0.3924 1.8725 -0.1395 -0.6160 -0.2034 178 LYS   G O   
12570 C  CB  . LYS   G  187 ? 1.9590 1.0453 1.8634 0.0632  -0.4500 -0.1204 178 LYS   G CB  
12571 C  CG  . LYS   G  187 ? 1.9618 1.2061 1.8807 0.1320  -0.3753 -0.0779 178 LYS   G CG  
12572 C  CD  . LYS   G  187 ? 2.0230 1.2265 1.9786 0.1464  -0.3210 -0.1231 178 LYS   G CD  
12573 C  CE  . LYS   G  187 ? 2.0904 1.3502 1.9858 0.2050  -0.2343 -0.0959 178 LYS   G CE  
12574 N  NZ  . LYS   G  187 ? 2.0822 1.3777 2.0261 0.2616  -0.1876 -0.1383 178 LYS   G NZ  
12575 N  N   . LYS   G  188 ? 2.0227 0.8275 1.9445 -0.0336 -0.5391 -0.1015 179 LYS   G N   
12576 C  CA  . LYS   G  188 ? 2.0616 1.0429 1.9620 0.0120  -0.5608 -0.0801 179 LYS   G CA  
12577 C  C   . LYS   G  188 ? 2.0480 1.0827 1.9942 0.0506  -0.6254 -0.0601 179 LYS   G C   
12578 O  O   . LYS   G  188 ? 2.0253 1.1369 2.1424 0.0772  -0.6046 0.0079  179 LYS   G O   
12579 C  CB  . LYS   G  188 ? 2.1388 1.0724 1.9309 0.0473  -0.5310 -0.0767 179 LYS   G CB  
12580 C  CG  . LYS   G  188 ? 2.1740 1.1392 1.9048 0.0692  -0.4519 -0.1263 179 LYS   G CG  
12581 C  CD  . LYS   G  188 ? 2.2374 1.1724 1.9444 0.0885  -0.3841 -0.1005 179 LYS   G CD  
12582 C  CE  . LYS   G  188 ? 2.2824 1.1748 1.9902 0.0830  -0.3328 -0.1299 179 LYS   G CE  
12583 N  NZ  . LYS   G  188 ? 2.3257 1.2169 2.0061 0.0921  -0.2876 -0.1130 179 LYS   G NZ  
12584 N  N   . SER   G  189 ? 2.0554 1.0977 1.9363 0.0583  -0.6464 -0.0766 180 SER   G N   
12585 C  CA  . SER   G  189 ? 2.0269 1.1112 1.8995 0.1020  -0.6240 -0.0697 180 SER   G CA  
12586 C  C   . SER   G  189 ? 1.9987 1.0361 1.8845 0.0744  -0.6302 -0.0714 180 SER   G C   
12587 O  O   . SER   G  189 ? 2.0053 1.0119 1.9478 0.1071  -0.6495 -0.1449 180 SER   G O   
12588 C  CB  . SER   G  189 ? 2.0090 1.1565 1.8848 0.0998  -0.5871 -0.0261 180 SER   G CB  
12589 O  OG  . SER   G  189 ? 1.9901 1.1602 1.8836 0.1855  -0.6059 -0.0079 180 SER   G OG  
12590 N  N   . LYS   G  190 ? 1.9829 0.9930 1.8906 0.0421  -0.4999 -0.1079 181 LYS   G N   
12591 C  CA  . LYS   G  190 ? 2.0507 1.0223 1.8980 -0.0135 -0.4262 -0.0875 181 LYS   G CA  
12592 C  C   . LYS   G  190 ? 2.0018 1.0197 1.8490 -0.0092 -0.3841 -0.0790 181 LYS   G C   
12593 O  O   . LYS   G  190 ? 1.9902 0.9311 1.8289 -0.0652 -0.3593 -0.0800 181 LYS   G O   
12594 C  CB  . LYS   G  190 ? 2.0650 1.0882 1.9204 -0.0112 -0.4280 -0.1037 181 LYS   G CB  
12595 C  CG  . LYS   G  190 ? 2.1476 1.1458 1.9591 0.0065  -0.3376 -0.1201 181 LYS   G CG  
12596 C  CD  . LYS   G  190 ? 2.2039 1.1810 2.0218 -0.0342 -0.2833 -0.1612 181 LYS   G CD  
12597 C  CE  . LYS   G  190 ? 2.2052 1.1250 1.9994 -0.0215 -0.2157 -0.1974 181 LYS   G CE  
12598 N  NZ  . LYS   G  190 ? 2.2105 1.1088 2.0047 -0.0036 -0.1691 -0.2127 181 LYS   G NZ  
12599 N  N   . ILE   G  191 ? 2.0465 0.9853 1.8301 -0.0475 -0.3899 -0.0905 182 ILE   G N   
12600 C  CA  . ILE   G  191 ? 2.0433 0.9821 1.7640 -0.0203 -0.3857 -0.1049 182 ILE   G CA  
12601 C  C   . ILE   G  191 ? 2.0245 1.0800 1.7480 -0.0529 -0.3740 -0.1481 182 ILE   G C   
12602 O  O   . ILE   G  191 ? 2.0335 0.9833 1.6854 -0.1294 -0.3374 -0.2402 182 ILE   G O   
12603 C  CB  . ILE   G  191 ? 2.0757 0.8797 1.8234 -0.0184 -0.4117 -0.1053 182 ILE   G CB  
12604 C  CG1 . ILE   G  191 ? 2.0475 0.8325 1.8353 -0.0465 -0.3809 -0.0399 182 ILE   G CG1 
12605 C  CG2 . ILE   G  191 ? 2.0904 0.8456 1.8004 0.0019  -0.4078 -0.1258 182 ILE   G CG2 
12606 C  CD1 . ILE   G  191 ? 2.0389 0.8354 1.8847 -0.0436 -0.3790 -0.0137 182 ILE   G CD1 
12607 N  N   . ASP   G  192 ? 1.9904 1.1500 1.7378 -0.0710 -0.3775 -0.1725 183 ASP   G N   
12608 C  CA  . ASP   G  192 ? 1.9452 1.1969 1.7359 -0.0683 -0.3549 -0.1684 183 ASP   G CA  
12609 C  C   . ASP   G  192 ? 1.9681 1.1307 1.7377 -0.1394 -0.4115 -0.0755 183 ASP   G C   
12610 O  O   . ASP   G  192 ? 2.0578 1.1003 1.7213 -0.2612 -0.4592 -0.0635 183 ASP   G O   
12611 C  CB  . ASP   G  192 ? 1.8876 1.2450 1.7851 -0.0397 -0.3709 -0.2249 183 ASP   G CB  
12612 C  CG  . ASP   G  192 ? 1.8762 1.3187 1.7725 0.0133  -0.3110 -0.2963 183 ASP   G CG  
12613 O  OD1 . ASP   G  192 ? 1.9551 1.2718 1.8457 0.0918  -0.2982 -0.2923 183 ASP   G OD1 
12614 O  OD2 . ASP   G  192 ? 1.8624 1.4930 1.7847 0.0118  -0.3736 -0.4036 183 ASP   G OD2 
12615 N  N   . HIS   G  193 ? 1.9809 1.0567 1.7435 -0.0933 -0.4531 -0.0541 184 HIS   G N   
12616 C  CA  . HIS   G  193 ? 1.9594 1.0211 1.6715 -0.0378 -0.4611 -0.0366 184 HIS   G CA  
12617 C  C   . HIS   G  193 ? 2.0000 0.9403 1.6749 0.0174  -0.4937 -0.0589 184 HIS   G C   
12618 O  O   . HIS   G  193 ? 1.9821 0.9876 1.6532 0.0630  -0.5498 -0.0337 184 HIS   G O   
12619 C  CB  . HIS   G  193 ? 1.9657 1.0013 1.7278 -0.0095 -0.4474 0.0512  184 HIS   G CB  
12620 C  CG  . HIS   G  193 ? 1.9249 1.0645 1.7491 -0.0355 -0.4302 0.1001  184 HIS   G CG  
12621 N  ND1 . HIS   G  193 ? 1.9820 1.0555 1.7835 -0.0501 -0.4130 0.1350  184 HIS   G ND1 
12622 C  CD2 . HIS   G  193 ? 1.9193 1.1018 1.8042 -0.0475 -0.4158 0.0932  184 HIS   G CD2 
12623 C  CE1 . HIS   G  193 ? 1.9655 0.9886 1.8329 -0.0611 -0.3684 0.1485  184 HIS   G CE1 
12624 N  NE2 . HIS   G  193 ? 1.9232 1.0114 1.8318 -0.0519 -0.3723 0.1282  184 HIS   G NE2 
12625 N  N   . ILE   G  194 ? 1.9582 0.8355 1.5817 0.0103  -0.5525 -0.1012 185 ILE   G N   
12626 C  CA  . ILE   G  194 ? 1.9844 0.8897 1.5810 -0.0282 -0.5761 -0.1729 185 ILE   G CA  
12627 C  C   . ILE   G  194 ? 2.0427 0.9994 1.5863 0.0291  -0.6166 -0.1524 185 ILE   G C   
12628 O  O   . ILE   G  194 ? 2.0184 1.0565 1.6656 -0.0076 -0.6311 -0.1926 185 ILE   G O   
12629 C  CB  . ILE   G  194 ? 1.9930 0.8245 1.5361 -0.0353 -0.5590 -0.2355 185 ILE   G CB  
12630 C  CG1 . ILE   G  194 ? 1.9685 0.8255 1.5989 -0.0201 -0.5469 -0.2375 185 ILE   G CG1 
12631 C  CG2 . ILE   G  194 ? 1.9900 0.8109 1.5261 -0.0454 -0.5826 -0.2520 185 ILE   G CG2 
12632 C  CD1 . ILE   G  194 ? 1.9634 0.8770 1.6773 -0.0654 -0.5031 -0.2421 185 ILE   G CD1 
12633 N  N   . ASN   G  195 ? 2.0848 1.0808 1.5579 0.0148  -0.6330 -0.1657 186 ASN   G N   
12634 C  CA  . ASN   G  195 ? 2.1542 1.1390 1.4675 0.0463  -0.5602 -0.0792 186 ASN   G CA  
12635 C  C   . ASN   G  195 ? 2.1868 1.0561 1.4260 0.0698  -0.6052 -0.0262 186 ASN   G C   
12636 O  O   . ASN   G  195 ? 2.2150 1.1291 1.3198 0.0723  -0.5555 0.0924  186 ASN   G O   
12637 C  CB  . ASN   G  195 ? 2.1063 1.2774 1.4878 0.1119  -0.5835 -0.0564 186 ASN   G CB  
12638 C  CG  . ASN   G  195 ? 2.1788 1.2881 1.4726 0.1542  -0.5662 -0.0577 186 ASN   G CG  
12639 O  OD1 . ASN   G  195 ? 2.2782 1.5569 1.4648 0.1803  -0.5852 -0.0552 186 ASN   G OD1 
12640 N  ND2 . ASN   G  195 ? 2.1406 1.1816 1.5134 0.0873  -0.6034 -0.0450 186 ASN   G ND2 
12641 N  N   . GLU   G  196 ? 2.1709 0.9774 1.4449 0.0734  -0.5124 0.0334  187 GLU   G N   
12642 C  CA  . GLU   G  196 ? 2.1852 1.0945 1.4964 0.1181  -0.4477 0.0440  187 GLU   G CA  
12643 C  C   . GLU   G  196 ? 2.1674 1.1106 1.5620 0.1124  -0.4073 0.0450  187 GLU   G C   
12644 O  O   . GLU   G  196 ? 2.0905 1.1855 1.5708 0.1466  -0.3349 -0.0070 187 GLU   G O   
12645 C  CB  . GLU   G  196 ? 2.2228 0.9787 1.5357 0.1105  -0.4368 0.0335  187 GLU   G CB  
12646 C  CG  . GLU   G  196 ? 2.2677 0.9732 1.5689 0.1361  -0.4032 0.0856  187 GLU   G CG  
12647 C  CD  . GLU   G  196 ? 2.2655 1.0018 1.6474 0.1375  -0.4422 0.0814  187 GLU   G CD  
12648 O  OE1 . GLU   G  196 ? 2.2472 0.9948 1.7408 0.1593  -0.4380 0.0892  187 GLU   G OE1 
12649 O  OE2 . GLU   G  196 ? 2.3445 1.0639 1.7354 0.1770  -0.3954 0.1873  187 GLU   G OE2 
12650 N  N   . GLU   G  197 ? 2.1871 1.1987 1.5864 0.1188  -0.3882 0.0951  188 GLU   G N   
12651 C  CA  . GLU   G  197 ? 2.1691 1.1938 1.5856 0.1130  -0.3993 0.0845  188 GLU   G CA  
12652 C  C   . GLU   G  197 ? 2.1783 0.9930 1.4042 0.1233  -0.4160 0.1478  188 GLU   G C   
12653 O  O   . GLU   G  197 ? 2.2000 0.9720 1.3959 0.1358  -0.3623 0.1436  188 GLU   G O   
12654 C  CB  . GLU   G  197 ? 2.2447 1.3173 1.6297 0.1535  -0.3805 0.1416  188 GLU   G CB  
12655 C  CG  . GLU   G  197 ? 2.2529 1.4926 1.8125 0.1192  -0.3781 0.1030  188 GLU   G CG  
12656 C  CD  . GLU   G  197 ? 2.3205 1.5452 1.9053 0.1095  -0.3370 0.0309  188 GLU   G CD  
12657 O  OE1 . GLU   G  197 ? 2.3381 1.6605 2.0053 0.0273  -0.4280 0.1011  188 GLU   G OE1 
12658 O  OE2 . GLU   G  197 ? 2.4252 1.6395 1.9132 0.0102  -0.3178 -0.0163 188 GLU   G OE2 
12659 N  N   . SER   G  198 ? 2.1075 0.9115 1.3467 0.1192  -0.4719 0.1882  189 SER   G N   
12660 C  CA  . SER   G  198 ? 2.1162 0.9289 1.3982 0.0877  -0.4810 0.1744  189 SER   G CA  
12661 C  C   . SER   G  198 ? 2.0510 0.9539 1.3912 0.0757  -0.5208 0.1417  189 SER   G C   
12662 O  O   . SER   G  198 ? 2.1095 1.0099 1.5365 0.0117  -0.5161 0.2051  189 SER   G O   
12663 C  CB  . SER   G  198 ? 2.0892 0.9329 1.3911 0.1006  -0.4964 0.2257  189 SER   G CB  
12664 O  OG  . SER   G  198 ? 2.0541 0.9509 1.3966 0.0732  -0.4817 0.2021  189 SER   G OG  
12665 N  N   . TRP   G  199 ? 2.0336 0.8688 1.3890 0.0690  -0.4750 0.0881  190 TRP   G N   
12666 C  CA  . TRP   G  199 ? 1.9999 0.7747 1.3693 0.0518  -0.4708 0.0429  190 TRP   G CA  
12667 C  C   . TRP   G  199 ? 2.0222 0.9139 1.3403 0.0179  -0.3952 0.0137  190 TRP   G C   
12668 O  O   . TRP   G  199 ? 2.0483 0.9714 1.4023 0.0119  -0.4016 0.0737  190 TRP   G O   
12669 C  CB  . TRP   G  199 ? 1.9531 0.6880 1.3525 0.0977  -0.4645 0.0546  190 TRP   G CB  
12670 C  CG  . TRP   G  199 ? 1.9779 0.5454 1.3391 0.1075  -0.5047 0.0338  190 TRP   G CG  
12671 C  CD1 . TRP   G  199 ? 2.0018 0.5049 1.3322 0.0673  -0.5101 -0.0507 190 TRP   G CD1 
12672 C  CD2 . TRP   G  199 ? 1.9835 0.5334 1.3645 0.0933  -0.4865 0.0472  190 TRP   G CD2 
12673 N  NE1 . TRP   G  199 ? 2.0236 0.4258 1.3613 0.0633  -0.4967 -0.0698 190 TRP   G NE1 
12674 C  CE2 . TRP   G  199 ? 2.0129 0.4767 1.3595 0.1004  -0.4886 0.0032  190 TRP   G CE2 
12675 C  CE3 . TRP   G  199 ? 2.0114 0.5262 1.4083 0.0818  -0.4391 -0.0342 190 TRP   G CE3 
12676 C  CZ2 . TRP   G  199 ? 2.0467 0.4942 1.3559 0.0892  -0.4523 0.0380  190 TRP   G CZ2 
12677 C  CZ3 . TRP   G  199 ? 2.0490 0.4936 1.3836 0.0632  -0.4060 -0.0367 190 TRP   G CZ3 
12678 C  CH2 . TRP   G  199 ? 2.0312 0.5248 1.3455 0.1052  -0.4220 0.0386  190 TRP   G CH2 
12679 N  N   . GLU   G  200 ? 2.0625 0.8402 1.3675 0.0239  -0.3884 0.0612  191 GLU   G N   
12680 C  CA  . GLU   G  200 ? 2.0807 0.8586 1.2988 -0.0531 -0.3559 0.0548  191 GLU   G CA  
12681 C  C   . GLU   G  200 ? 2.0973 0.8275 1.3017 -0.0234 -0.3343 -0.0194 191 GLU   G C   
12682 O  O   . GLU   G  200 ? 2.0831 0.6250 1.4318 -0.1598 -0.2821 -0.1518 191 GLU   G O   
12683 C  CB  . GLU   G  200 ? 2.1201 1.0002 1.2626 -0.0493 -0.3783 0.0662  191 GLU   G CB  
12684 C  CG  . GLU   G  200 ? 2.1193 1.0935 1.2514 -0.1056 -0.3359 0.1448  191 GLU   G CG  
12685 C  CD  . GLU   G  200 ? 2.1397 1.0972 1.2057 -0.1148 -0.3228 0.1974  191 GLU   G CD  
12686 O  OE1 . GLU   G  200 ? 2.1656 1.2125 0.9985 -0.1157 -0.3431 0.3138  191 GLU   G OE1 
12687 O  OE2 . GLU   G  200 ? 2.1463 1.4054 1.2649 -0.1154 -0.3089 0.1243  191 GLU   G OE2 
12688 N  N   . LYS   G  201 ? 2.1066 0.7663 1.2188 -0.0223 -0.3749 -0.0558 192 LYS   G N   
12689 C  CA  . LYS   G  201 ? 2.1081 0.8257 1.2790 -0.0599 -0.3633 -0.0795 192 LYS   G CA  
12690 C  C   . LYS   G  201 ? 2.0989 0.8456 1.2227 -0.1129 -0.3409 -0.1369 192 LYS   G C   
12691 O  O   . LYS   G  201 ? 2.1501 0.8689 1.3795 -0.2430 -0.3417 -0.0862 192 LYS   G O   
12692 C  CB  . LYS   G  201 ? 2.1095 0.9610 1.3273 0.0177  -0.3399 -0.0423 192 LYS   G CB  
12693 C  CG  . LYS   G  201 ? 2.1904 1.1050 1.3399 0.0399  -0.2551 -0.0237 192 LYS   G CG  
12694 C  CD  . LYS   G  201 ? 2.2004 1.2707 1.3075 0.0549  -0.2624 -0.0246 192 LYS   G CD  
12695 C  CE  . LYS   G  201 ? 2.2653 1.3059 1.2916 0.1032  -0.1539 0.0354  192 LYS   G CE  
12696 N  NZ  . LYS   G  201 ? 2.3277 1.3918 1.2908 0.1451  -0.1151 0.0698  192 LYS   G NZ  
12697 N  N   . VAL   G  202 ? 2.0506 0.6165 1.2348 -0.0911 -0.3193 -0.0895 193 VAL   G N   
12698 C  CA  . VAL   G  202 ? 1.9708 0.5669 1.2221 -0.0463 -0.3432 -0.0947 193 VAL   G CA  
12699 C  C   . VAL   G  202 ? 1.9758 0.6460 1.1374 -0.0420 -0.3870 -0.0768 193 VAL   G C   
12700 O  O   . VAL   G  202 ? 1.9410 0.7715 1.0734 -0.0438 -0.4140 0.0180  193 VAL   G O   
12701 C  CB  . VAL   G  202 ? 1.9210 0.5226 1.1986 -0.0450 -0.3245 -0.0499 193 VAL   G CB  
12702 C  CG1 . VAL   G  202 ? 1.8605 0.4832 1.2165 -0.0391 -0.3256 -0.0435 193 VAL   G CG1 
12703 C  CG2 . VAL   G  202 ? 1.9277 0.5809 1.2371 -0.0246 -0.3212 -0.0425 193 VAL   G CG2 
12704 N  N   . VAL   G  203 ? 2.0052 0.5602 1.0974 -0.0498 -0.4107 -0.0691 194 VAL   G N   
12705 C  CA  . VAL   G  203 ? 2.0176 0.6210 1.1345 -0.0322 -0.3553 -0.0838 194 VAL   G CA  
12706 C  C   . VAL   G  203 ? 2.0833 0.7046 1.0835 -0.0436 -0.3588 -0.1232 194 VAL   G C   
12707 O  O   . VAL   G  203 ? 2.1206 0.6717 0.9938 -0.0140 -0.3801 -0.2216 194 VAL   G O   
12708 C  CB  . VAL   G  203 ? 2.0697 0.6152 1.1944 -0.0238 -0.3127 -0.0242 194 VAL   G CB  
12709 C  CG1 . VAL   G  203 ? 2.0717 0.6863 1.2373 -0.0134 -0.2809 -0.0452 194 VAL   G CG1 
12710 C  CG2 . VAL   G  203 ? 2.0495 0.5734 1.1686 -0.0051 -0.2947 0.0152  194 VAL   G CG2 
12711 N  N   . GLU   G  204 ? 2.1089 0.6838 1.0684 -0.0055 -0.3492 -0.1353 195 GLU   G N   
12712 C  CA  . GLU   G  204 ? 2.1570 0.6982 1.0846 -0.0113 -0.3257 -0.1531 195 GLU   G CA  
12713 C  C   . GLU   G  204 ? 2.1157 0.6782 1.1404 -0.0469 -0.3492 -0.2056 195 GLU   G C   
12714 O  O   . GLU   G  204 ? 2.1585 0.5854 1.1933 -0.2019 -0.3347 -0.2908 195 GLU   G O   
12715 C  CB  . GLU   G  204 ? 2.2558 0.7695 1.0621 0.0439  -0.3234 -0.1705 195 GLU   G CB  
12716 C  CG  . GLU   G  204 ? 2.3335 0.7871 1.0808 0.0332  -0.2903 -0.1631 195 GLU   G CG  
12717 C  CD  . GLU   G  204 ? 2.4590 0.8201 1.0896 0.0355  -0.2654 -0.1033 195 GLU   G CD  
12718 O  OE1 . GLU   G  204 ? 2.5525 0.7644 1.0591 0.0365  -0.2529 -0.1246 195 GLU   G OE1 
12719 O  OE2 . GLU   G  204 ? 2.4817 0.9059 1.0874 0.0520  -0.3221 -0.0761 195 GLU   G OE2 
12720 N  N   . PHE   G  205 ? 2.0651 0.5711 1.1582 -0.0416 -0.3832 -0.1964 196 PHE   G N   
12721 C  CA  . PHE   G  205 ? 2.0411 0.5915 1.1731 -0.0509 -0.3626 -0.2157 196 PHE   G CA  
12722 C  C   . PHE   G  205 ? 2.0156 0.6170 1.2123 -0.0864 -0.3641 -0.1705 196 PHE   G C   
12723 O  O   . PHE   G  205 ? 2.0626 0.6169 1.2299 -0.0134 -0.3461 -0.0961 196 PHE   G O   
12724 C  CB  . PHE   G  205 ? 2.0478 0.6008 1.1512 -0.0228 -0.3943 -0.2407 196 PHE   G CB  
12725 C  CG  . PHE   G  205 ? 2.0294 0.6504 1.1755 -0.0678 -0.3501 -0.3057 196 PHE   G CG  
12726 C  CD1 . PHE   G  205 ? 2.0529 0.7080 1.1574 -0.0559 -0.3147 -0.3236 196 PHE   G CD1 
12727 C  CD2 . PHE   G  205 ? 2.0645 0.7671 1.1315 -0.0698 -0.3944 -0.3437 196 PHE   G CD2 
12728 C  CE1 . PHE   G  205 ? 2.0456 0.7424 1.1736 -0.0837 -0.3141 -0.3287 196 PHE   G CE1 
12729 C  CE2 . PHE   G  205 ? 2.0512 0.8842 1.1721 -0.1086 -0.3718 -0.3301 196 PHE   G CE2 
12730 C  CZ  . PHE   G  205 ? 2.0531 0.8458 1.1720 -0.0976 -0.3473 -0.3158 196 PHE   G CZ  
12731 N  N   . ALA   G  206 ? 1.9419 0.5268 1.2696 -0.0948 -0.3740 -0.1268 197 ALA   G N   
12732 C  CA  . ALA   G  206 ? 1.9300 0.4743 1.3208 -0.0917 -0.3727 -0.0869 197 ALA   G CA  
12733 C  C   . ALA   G  206 ? 1.8806 0.5220 1.3713 -0.0941 -0.3819 -0.0932 197 ALA   G C   
12734 O  O   . ALA   G  206 ? 1.9252 0.4728 1.5118 -0.2024 -0.3613 -0.0845 197 ALA   G O   
12735 C  CB  . ALA   G  206 ? 1.9433 0.3939 1.3001 -0.0631 -0.3292 -0.0696 197 ALA   G CB  
12736 N  N   . ILE   G  207 ? 1.8689 0.4920 1.3127 -0.0881 -0.4440 -0.0521 198 ILE   G N   
12737 C  CA  . ILE   G  207 ? 1.9114 0.5475 1.2936 -0.0779 -0.4092 -0.0727 198 ILE   G CA  
12738 C  C   . ILE   G  207 ? 1.9341 0.7339 1.3533 -0.1500 -0.4675 -0.1522 198 ILE   G C   
12739 O  O   . ILE   G  207 ? 1.9584 0.8317 1.5269 -0.0739 -0.4364 -0.1043 198 ILE   G O   
12740 C  CB  . ILE   G  207 ? 1.9384 0.5202 1.2589 -0.0397 -0.4086 -0.0502 198 ILE   G CB  
12741 C  CG1 . ILE   G  207 ? 1.9467 0.5883 1.2455 -0.0777 -0.3913 -0.0554 198 ILE   G CG1 
12742 C  CG2 . ILE   G  207 ? 1.9400 0.4545 1.2303 -0.0826 -0.4148 -0.0789 198 ILE   G CG2 
12743 C  CD1 . ILE   G  207 ? 1.9789 0.6390 1.2258 -0.0633 -0.3689 -0.0340 198 ILE   G CD1 
12744 N  N   . THR   G  208 ? 1.9579 0.6356 1.3855 -0.0945 -0.4814 -0.1530 199 THR   G N   
12745 C  CA  . THR   G  208 ? 2.0062 0.6186 1.3858 -0.0613 -0.4819 -0.2107 199 THR   G CA  
12746 C  C   . THR   G  208 ? 2.0375 0.5924 1.4002 -0.0937 -0.4578 -0.2420 199 THR   G C   
12747 O  O   . THR   G  208 ? 2.1428 0.5906 1.4437 -0.0352 -0.4129 -0.1865 199 THR   G O   
12748 C  CB  . THR   G  208 ? 2.0108 0.4750 1.3318 -0.0904 -0.4962 -0.2575 199 THR   G CB  
12749 O  OG1 . THR   G  208 ? 1.9652 0.3043 1.2718 -0.0911 -0.5498 -0.3204 199 THR   G OG1 
12750 C  CG2 . THR   G  208 ? 1.9889 0.5837 1.3656 -0.1163 -0.5152 -0.2905 199 THR   G CG2 
12751 N  N   . HIS   G  209 ? 2.0159 0.6492 1.4423 -0.1006 -0.4089 -0.2196 200 HIS   G N   
12752 C  CA  . HIS   G  209 ? 1.9946 0.5945 1.5058 -0.0865 -0.4244 -0.1936 200 HIS   G CA  
12753 C  C   . HIS   G  209 ? 2.0582 0.6411 1.5475 -0.0130 -0.4188 -0.1444 200 HIS   G C   
12754 O  O   . HIS   G  209 ? 1.9591 0.8256 1.5023 0.0330  -0.4483 0.0254  200 HIS   G O   
12755 C  CB  . HIS   G  209 ? 1.9674 0.6003 1.5288 -0.1425 -0.4168 -0.2427 200 HIS   G CB  
12756 C  CG  . HIS   G  209 ? 1.9997 0.5914 1.4630 -0.1540 -0.4367 -0.2791 200 HIS   G CG  
12757 N  ND1 . HIS   G  209 ? 1.9579 0.7382 1.4969 -0.1533 -0.4122 -0.2796 200 HIS   G ND1 
12758 C  CD2 . HIS   G  209 ? 2.0039 0.4893 1.4303 -0.1632 -0.4302 -0.3180 200 HIS   G CD2 
12759 C  CE1 . HIS   G  209 ? 1.9874 0.7724 1.4544 -0.1365 -0.4052 -0.2437 200 HIS   G CE1 
12760 N  NE2 . HIS   G  209 ? 1.9961 0.5678 1.4601 -0.1503 -0.4299 -0.3179 200 HIS   G NE2 
12761 N  N   . MET   G  210 ? 2.0835 0.5286 1.5431 0.0029  -0.4284 -0.0911 201 MET   G N   
12762 C  CA  . MET   G  210 ? 2.1287 0.5906 1.5706 0.0668  -0.4255 -0.0967 201 MET   G CA  
12763 C  C   . MET   G  210 ? 2.1891 0.7808 1.4273 -0.0197 -0.4241 -0.2194 201 MET   G C   
12764 O  O   . MET   G  210 ? 2.2751 0.7466 1.5846 0.0647  -0.4115 -0.2861 201 MET   G O   
12765 C  CB  . MET   G  210 ? 2.1795 0.5332 1.5788 0.0586  -0.3897 -0.0756 201 MET   G CB  
12766 C  CG  . MET   G  210 ? 2.1616 0.6233 1.6414 0.0924  -0.3430 -0.0706 201 MET   G CG  
12767 S  SD  . MET   G  210 ? 2.2457 0.5809 1.5993 0.0438  -0.3008 -0.0203 201 MET   G SD  
12768 C  CE  . MET   G  210 ? 2.2446 0.8771 1.6029 0.1408  -0.2794 0.0282  201 MET   G CE  
12769 N  N   . ILE   G  211 ? 2.1199 0.6526 1.3843 -0.0219 -0.4608 -0.2781 202 ILE   G N   
12770 C  CA  . ILE   G  211 ? 2.1326 0.6842 1.4136 -0.0129 -0.4074 -0.2740 202 ILE   G CA  
12771 C  C   . ILE   G  211 ? 2.1837 0.7218 1.4891 -0.0615 -0.3920 -0.3341 202 ILE   G C   
12772 O  O   . ILE   G  211 ? 2.1931 0.6483 1.5225 -0.1317 -0.3821 -0.4197 202 ILE   G O   
12773 C  CB  . ILE   G  211 ? 2.1128 0.6466 1.3843 -0.0210 -0.4189 -0.3135 202 ILE   G CB  
12774 C  CG1 . ILE   G  211 ? 2.1009 0.5876 1.3562 0.0029  -0.4312 -0.3108 202 ILE   G CG1 
12775 C  CG2 . ILE   G  211 ? 2.1753 0.6262 1.3924 -0.0374 -0.4265 -0.3176 202 ILE   G CG2 
12776 C  CD1 . ILE   G  211 ? 2.0961 0.4865 1.3437 -0.0092 -0.4504 -0.3532 202 ILE   G CD1 
12777 N  N   . ASP   G  212 ? 2.1841 0.7080 1.5469 -0.0472 -0.3832 -0.3841 203 ASP   G N   
12778 C  CA  . ASP   G  212 ? 2.1934 0.7986 1.6078 -0.1011 -0.3064 -0.4262 203 ASP   G CA  
12779 C  C   . ASP   G  212 ? 2.2278 0.9360 1.5896 -0.1960 -0.2444 -0.3769 203 ASP   G C   
12780 O  O   . ASP   G  212 ? 2.3404 0.9607 1.7183 -0.1948 -0.1608 -0.4164 203 ASP   G O   
12781 C  CB  . ASP   G  212 ? 2.1999 0.9361 1.6909 -0.0501 -0.2840 -0.5456 203 ASP   G CB  
12782 C  CG  . ASP   G  212 ? 2.2196 1.0789 1.5827 -0.0194 -0.2856 -0.6473 203 ASP   G CG  
12783 O  OD1 . ASP   G  212 ? 2.3228 1.2052 1.5748 0.0395  -0.2458 -0.9451 203 ASP   G OD1 
12784 O  OD2 . ASP   G  212 ? 2.1810 1.2068 1.7971 -0.0057 -0.3201 -0.8339 203 ASP   G OD2 
12785 N  N   . ALA   G  213 ? 2.1703 0.6207 1.6112 -0.2671 -0.2172 -0.3206 204 ALA   G N   
12786 C  CA  . ALA   G  213 ? 2.1585 0.5954 1.6540 -0.1985 -0.2207 -0.2796 204 ALA   G CA  
12787 C  C   . ALA   G  213 ? 2.1580 0.6332 1.6446 -0.1727 -0.1897 -0.2511 204 ALA   G C   
12788 O  O   . ALA   G  213 ? 2.2562 0.7289 1.9143 -0.0589 -0.1480 -0.1026 204 ALA   G O   
12789 C  CB  . ALA   G  213 ? 2.1439 0.4767 1.6892 -0.2342 -0.2025 -0.2462 204 ALA   G CB  
12790 N  N   . LEU   G  214 ? 2.1681 0.3573 1.4354 -0.0991 -0.2363 -0.1689 205 LEU   G N   
12791 C  CA  . LEU   G  214 ? 2.1428 0.3868 1.4138 -0.1121 -0.1923 -0.1763 205 LEU   G CA  
12792 C  C   . LEU   G  214 ? 2.1940 0.5097 1.4379 -0.1093 -0.1531 -0.2296 205 LEU   G C   
12793 O  O   . LEU   G  214 ? 2.1957 0.5279 1.4625 -0.0359 -0.0491 -0.3881 205 LEU   G O   
12794 C  CB  . LEU   G  214 ? 2.1504 0.3028 1.4265 -0.0802 -0.2036 -0.0368 205 LEU   G CB  
12795 C  CG  . LEU   G  214 ? 2.1450 0.2478 1.4352 -0.0994 -0.2303 -0.0194 205 LEU   G CG  
12796 C  CD1 . LEU   G  214 ? 2.1625 0.1922 1.4093 -0.0951 -0.2515 0.0070  205 LEU   G CD1 
12797 C  CD2 . LEU   G  214 ? 2.1497 0.3418 1.4209 -0.1343 -0.1815 -0.0137 205 LEU   G CD2 
12798 N  N   . GLY   G  215 ? 2.1926 0.5559 1.4754 -0.0522 -0.1794 -0.2098 206 GLY   G N   
12799 C  CA  . GLY   G  215 ? 2.2569 0.6872 1.4536 -0.0838 -0.2464 -0.2671 206 GLY   G CA  
12800 C  C   . GLY   G  215 ? 2.2902 0.7381 1.4109 -0.1340 -0.2460 -0.2720 206 GLY   G C   
12801 O  O   . GLY   G  215 ? 2.3957 0.8451 1.1311 -0.2434 -0.3617 -0.3949 206 GLY   G O   
12802 N  N   . THR   G  216 ? 2.2620 0.7413 1.4463 -0.1343 -0.2311 -0.2679 207 THR   G N   
12803 C  CA  . THR   G  216 ? 2.2427 0.8591 1.4240 -0.1288 -0.2251 -0.2898 207 THR   G CA  
12804 C  C   . THR   G  216 ? 2.1964 0.8637 1.4456 -0.1340 -0.2043 -0.2815 207 THR   G C   
12805 O  O   . THR   G  216 ? 2.1595 0.8199 1.3816 -0.1740 -0.1960 -0.3090 207 THR   G O   
12806 C  CB  . THR   G  216 ? 2.2273 0.8572 1.4490 -0.1436 -0.2277 -0.3237 207 THR   G CB  
12807 O  OG1 . THR   G  216 ? 2.1880 0.9560 1.3839 -0.1495 -0.2961 -0.3385 207 THR   G OG1 
12808 C  CG2 . THR   G  216 ? 2.1982 0.8907 1.4148 -0.1252 -0.2375 -0.3400 207 THR   G CG2 
12809 N  N   . GLU   G  217 ? 2.2075 0.9806 1.5184 -0.1674 -0.1838 -0.2367 208 GLU   G N   
12810 C  CA  . GLU   G  217 ? 2.2410 0.9895 1.6036 -0.0934 -0.2772 -0.1838 208 GLU   G CA  
12811 C  C   . GLU   G  217 ? 2.2861 0.8515 1.5065 -0.0272 -0.2218 -0.2628 208 GLU   G C   
12812 O  O   . GLU   G  217 ? 2.2904 1.0138 1.5626 -0.0249 -0.3099 -0.3533 208 GLU   G O   
12813 C  CB  . GLU   G  217 ? 2.2604 1.0682 1.6054 -0.1101 -0.2552 -0.1254 208 GLU   G CB  
12814 C  CG  . GLU   G  217 ? 2.2396 1.0067 1.7663 -0.1322 -0.2818 -0.0595 208 GLU   G CG  
12815 C  CD  . GLU   G  217 ? 2.2921 0.8892 1.8840 -0.2319 -0.2729 -0.0594 208 GLU   G CD  
12816 O  OE1 . GLU   G  217 ? 2.2730 0.9442 1.8955 -0.2960 -0.2929 -0.1025 208 GLU   G OE1 
12817 O  OE2 . GLU   G  217 ? 2.2364 0.7693 2.0756 -0.3093 -0.2390 -0.0080 208 GLU   G OE2 
12818 N  N   . PHE   G  218 ? 2.2122 0.8762 1.4281 0.0092  -0.2156 -0.1892 209 PHE   G N   
12819 C  CA  . PHE   G  218 ? 2.1881 0.7840 1.4039 0.0544  -0.1674 -0.1898 209 PHE   G CA  
12820 C  C   . PHE   G  218 ? 2.1689 0.7644 1.3139 0.1421  -0.2057 -0.1814 209 PHE   G C   
12821 O  O   . PHE   G  218 ? 2.1887 0.4537 1.3740 0.3132  -0.1437 -0.2207 209 PHE   G O   
12822 C  CB  . PHE   G  218 ? 2.1929 0.6804 1.4291 0.0393  -0.1757 -0.1851 209 PHE   G CB  
12823 C  CG  . PHE   G  218 ? 2.2289 0.7335 1.4545 -0.0022 -0.1505 -0.1811 209 PHE   G CG  
12824 C  CD1 . PHE   G  218 ? 2.2170 0.8834 1.4681 -0.0119 -0.1708 -0.1696 209 PHE   G CD1 
12825 C  CD2 . PHE   G  218 ? 2.2076 0.7056 1.4781 0.0430  -0.2065 -0.1603 209 PHE   G CD2 
12826 C  CE1 . PHE   G  218 ? 2.2511 0.9629 1.5247 -0.0292 -0.1418 -0.1285 209 PHE   G CE1 
12827 C  CE2 . PHE   G  218 ? 2.2171 0.8757 1.5095 -0.0154 -0.1645 -0.1475 209 PHE   G CE2 
12828 C  CZ  . PHE   G  218 ? 2.2389 0.9758 1.5083 -0.0297 -0.1769 -0.1216 209 PHE   G CZ  
12829 N  N   . SER   G  219 ? 2.1852 0.8792 1.3297 0.0788  -0.1862 -0.2224 210 SER   G N   
12830 C  CA  . SER   G  219 ? 2.1662 0.9677 1.3188 0.0503  -0.2019 -0.1748 210 SER   G CA  
12831 C  C   . SER   G  219 ? 2.1469 0.8094 1.4078 -0.0081 -0.1914 -0.0797 210 SER   G C   
12832 O  O   . SER   G  219 ? 2.1718 0.9543 1.4944 0.0393  -0.1258 0.0613  210 SER   G O   
12833 C  CB  . SER   G  219 ? 2.1359 1.1176 1.3082 -0.0027 -0.1861 -0.2017 210 SER   G CB  
12834 O  OG  . SER   G  219 ? 2.0183 1.2668 1.3839 0.0008  -0.1995 -0.2357 210 SER   G OG  
12835 N  N   . LYS   G  220 ? 2.1336 0.8206 1.3909 -0.0559 -0.1423 -0.1174 211 LYS   G N   
12836 C  CA  . LYS   G  220 ? 2.1090 0.8232 1.3360 -0.0622 -0.1005 -0.1258 211 LYS   G CA  
12837 C  C   . LYS   G  220 ? 2.0722 0.8076 1.3232 -0.0628 -0.0817 -0.1748 211 LYS   G C   
12838 O  O   . LYS   G  220 ? 1.9918 0.7944 1.3585 -0.0686 -0.0629 -0.1545 211 LYS   G O   
12839 C  CB  . LYS   G  220 ? 2.1872 0.6762 1.3918 -0.0803 -0.1005 -0.1873 211 LYS   G CB  
12840 C  CG  . LYS   G  220 ? 2.2089 0.6663 1.4455 -0.1472 -0.0600 -0.1543 211 LYS   G CG  
12841 C  CD  . LYS   G  220 ? 2.3284 0.6480 1.4375 -0.1915 -0.0773 -0.1676 211 LYS   G CD  
12842 C  CE  . LYS   G  220 ? 2.3456 0.5819 1.4169 -0.2568 -0.0393 -0.1045 211 LYS   G CE  
12843 N  NZ  . LYS   G  220 ? 2.3671 0.5010 1.4536 -0.3052 -0.0626 -0.1376 211 LYS   G NZ  
12844 N  N   . ASN   G  221 ? 2.0788 0.7761 1.1969 -0.0607 -0.0760 -0.2385 212 ASN   G N   
12845 C  CA  . ASN   G  221 ? 2.0892 0.7581 1.1858 -0.0393 -0.0694 -0.2034 212 ASN   G CA  
12846 C  C   . ASN   G  221 ? 2.1192 0.6928 1.2015 -0.0521 -0.1010 -0.2137 212 ASN   G C   
12847 O  O   . ASN   G  221 ? 2.1490 0.6917 1.1629 -0.0310 -0.0770 -0.2341 212 ASN   G O   
12848 C  CB  . ASN   G  221 ? 2.1120 0.8334 1.1708 -0.0394 -0.0317 -0.1968 212 ASN   G CB  
12849 C  CG  . ASN   G  221 ? 2.1281 0.8019 1.1344 -0.0379 -0.0320 -0.2287 212 ASN   G CG  
12850 O  OD1 . ASN   G  221 ? 2.0738 0.7701 1.0555 0.0394  0.0169  -0.2207 212 ASN   G OD1 
12851 N  ND2 . ASN   G  221 ? 2.1388 1.0067 1.0726 -0.0446 -0.0351 -0.2241 212 ASN   G ND2 
12852 N  N   . ASP   G  222 ? 2.1395 0.7931 1.2137 -0.0723 -0.1844 -0.2227 213 ASP   G N   
12853 C  CA  . ASP   G  222 ? 2.1032 0.8889 1.2475 -0.0930 -0.1500 -0.1974 213 ASP   G CA  
12854 C  C   . ASP   G  222 ? 1.9953 0.7843 1.2408 -0.1045 -0.2311 -0.2270 213 ASP   G C   
12855 O  O   . ASP   G  222 ? 1.9247 1.0572 1.2087 -0.1546 -0.1728 -0.2252 213 ASP   G O   
12856 C  CB  . ASP   G  222 ? 2.2165 0.8493 1.3331 -0.1048 -0.2026 -0.1732 213 ASP   G CB  
12857 C  CG  . ASP   G  222 ? 2.3112 0.8174 1.3148 -0.0810 -0.1839 -0.1570 213 ASP   G CG  
12858 O  OD1 . ASP   G  222 ? 2.2878 0.7973 1.4833 -0.0802 -0.1380 -0.0551 213 ASP   G OD1 
12859 O  OD2 . ASP   G  222 ? 2.4024 0.7981 1.2735 -0.0874 -0.2645 -0.0805 213 ASP   G OD2 
12860 N  N   . LEU   G  223 ? 1.9554 0.7303 1.1440 -0.1789 -0.2455 -0.2081 214 LEU   G N   
12861 C  CA  . LEU   G  223 ? 1.9401 0.7397 1.1472 -0.1449 -0.2467 -0.1308 214 LEU   G CA  
12862 C  C   . LEU   G  223 ? 1.9292 0.6692 1.1407 -0.1036 -0.2177 -0.0822 214 LEU   G C   
12863 O  O   . LEU   G  223 ? 1.9601 0.6031 1.1587 -0.1297 -0.2309 -0.0915 214 LEU   G O   
12864 C  CB  . LEU   G  223 ? 1.9868 0.7402 1.1290 -0.1362 -0.2645 -0.1085 214 LEU   G CB  
12865 C  CG  . LEU   G  223 ? 1.9555 0.8162 1.1651 -0.1471 -0.3032 -0.1485 214 LEU   G CG  
12866 C  CD1 . LEU   G  223 ? 1.9772 0.7862 1.1745 -0.1048 -0.3055 -0.1364 214 LEU   G CD1 
12867 C  CD2 . LEU   G  223 ? 1.9750 0.9361 1.1667 -0.1297 -0.2673 -0.1551 214 LEU   G CD2 
12868 N  N   . GLU   G  224 ? 1.9368 0.5887 1.1369 -0.0336 -0.2418 -0.0513 215 GLU   G N   
12869 C  CA  . GLU   G  224 ? 1.9499 0.5994 1.1543 -0.0666 -0.2839 -0.0580 215 GLU   G CA  
12870 C  C   . GLU   G  224 ? 1.9604 0.6353 1.0334 -0.0316 -0.3464 -0.0236 215 GLU   G C   
12871 O  O   . GLU   G  224 ? 1.9839 0.7089 1.0604 -0.0223 -0.3272 0.0434  215 GLU   G O   
12872 C  CB  . GLU   G  224 ? 1.9254 0.5826 1.2170 -0.0289 -0.3291 -0.0872 215 GLU   G CB  
12873 C  CG  . GLU   G  224 ? 1.9928 0.6049 1.3315 -0.0308 -0.3163 -0.1476 215 GLU   G CG  
12874 C  CD  . GLU   G  224 ? 1.9923 0.5913 1.3964 -0.0365 -0.3722 -0.2222 215 GLU   G CD  
12875 O  OE1 . GLU   G  224 ? 2.1039 0.5220 1.4840 0.1419  -0.2836 -0.2945 215 GLU   G OE1 
12876 O  OE2 . GLU   G  224 ? 1.9806 0.7663 1.6035 -0.1818 -0.3807 -0.2282 215 GLU   G OE2 
12877 N  N   . VAL   G  225 ? 1.9514 0.6316 0.9334 -0.0570 -0.3515 -0.0234 216 VAL   G N   
12878 C  CA  . VAL   G  225 ? 1.9362 0.5949 0.9886 -0.0920 -0.3265 -0.0158 216 VAL   G CA  
12879 C  C   . VAL   G  225 ? 1.9445 0.5477 0.9586 -0.1465 -0.3226 0.0304  216 VAL   G C   
12880 O  O   . VAL   G  225 ? 2.0504 0.4712 0.9243 -0.1585 -0.3093 0.0169  216 VAL   G O   
12881 C  CB  . VAL   G  225 ? 1.9134 0.5964 1.0002 -0.1068 -0.3220 0.0194  216 VAL   G CB  
12882 C  CG1 . VAL   G  225 ? 1.9102 0.5761 1.0219 -0.1056 -0.3331 0.0393  216 VAL   G CG1 
12883 C  CG2 . VAL   G  225 ? 1.9138 0.6338 1.0213 -0.1042 -0.3062 -0.0111 216 VAL   G CG2 
12884 N  N   . GLY   G  226 ? 1.9359 0.6067 1.0042 -0.0577 -0.3212 -0.0051 217 GLY   G N   
12885 C  CA  . GLY   G  226 ? 1.9152 0.5819 1.0853 -0.0189 -0.3702 0.0113  217 GLY   G CA  
12886 C  C   . GLY   G  226 ? 1.9252 0.6755 1.0921 -0.0421 -0.4366 0.0062  217 GLY   G C   
12887 O  O   . GLY   G  226 ? 1.9074 0.6241 1.0261 0.0013  -0.5292 0.0033  217 GLY   G O   
12888 N  N   . VAL   G  227 ? 1.9008 0.6984 1.1011 -0.0130 -0.4221 0.0284  218 VAL   G N   
12889 C  CA  . VAL   G  227 ? 1.8923 0.6245 1.0609 -0.0190 -0.4026 -0.0003 218 VAL   G CA  
12890 C  C   . VAL   G  227 ? 1.8591 0.5758 1.1192 -0.0351 -0.3582 0.0138  218 VAL   G C   
12891 O  O   . VAL   G  227 ? 1.8844 0.5876 1.1166 -0.0572 -0.3506 -0.0010 218 VAL   G O   
12892 C  CB  . VAL   G  227 ? 1.9015 0.6192 1.0723 -0.0438 -0.4008 0.0257  218 VAL   G CB  
12893 C  CG1 . VAL   G  227 ? 1.9038 0.5974 1.0671 -0.0380 -0.4013 0.0147  218 VAL   G CG1 
12894 C  CG2 . VAL   G  227 ? 1.9185 0.6678 1.0852 -0.0187 -0.3554 0.0391  218 VAL   G CG2 
12895 N  N   . ALA   G  228 ? 1.8423 0.5955 1.1106 -0.0169 -0.3602 -0.0401 219 ALA   G N   
12896 C  CA  . ALA   G  228 ? 1.7915 0.6111 1.1027 -0.0513 -0.3636 -0.0721 219 ALA   G CA  
12897 C  C   . ALA   G  228 ? 1.7310 0.6580 1.1080 -0.0707 -0.3740 -0.1165 219 ALA   G C   
12898 O  O   . ALA   G  228 ? 1.6851 0.6447 1.1644 -0.0564 -0.3686 -0.0780 219 ALA   G O   
12899 C  CB  . ALA   G  228 ? 1.7822 0.5993 1.1177 -0.0454 -0.3415 -0.0774 219 ALA   G CB  
12900 N  N   . THR   G  229 ? 1.8050 0.6727 1.1318 -0.0693 -0.3378 -0.1061 220 THR   G N   
12901 C  CA  . THR   G  229 ? 1.8310 0.7063 1.1929 -0.0405 -0.3398 -0.1140 220 THR   G CA  
12902 C  C   . THR   G  229 ? 1.9018 0.6024 1.2845 0.0321  -0.2863 -0.0686 220 THR   G C   
12903 O  O   . THR   G  229 ? 1.8605 0.6471 1.3133 -0.0189 -0.2695 -0.1251 220 THR   G O   
12904 C  CB  . THR   G  229 ? 1.8642 0.7494 1.1982 -0.0570 -0.3334 -0.1077 220 THR   G CB  
12905 O  OG1 . THR   G  229 ? 1.9137 0.6937 1.1980 -0.0760 -0.3221 -0.1730 220 THR   G OG1 
12906 C  CG2 . THR   G  229 ? 1.8902 0.8106 1.2019 -0.0638 -0.3166 -0.1326 220 THR   G CG2 
12907 N  N   . LYS   G  230 ? 2.0041 0.5821 1.3223 0.0651  -0.3331 0.0100  221 LYS   G N   
12908 C  CA  . LYS   G  230 ? 2.0405 0.6176 1.3979 0.1578  -0.3349 -0.0067 221 LYS   G CA  
12909 C  C   . LYS   G  230 ? 2.1194 0.5455 1.4108 0.1461  -0.3687 -0.0482 221 LYS   G C   
12910 O  O   . LYS   G  230 ? 2.1902 0.4687 1.4597 0.1127  -0.2824 -0.1083 221 LYS   G O   
12911 C  CB  . LYS   G  230 ? 1.9744 0.7041 1.5015 0.1708  -0.3348 -0.0614 221 LYS   G CB  
12912 C  CG  . LYS   G  230 ? 1.9186 0.7884 1.5557 0.1833  -0.3045 -0.0846 221 LYS   G CG  
12913 C  CD  . LYS   G  230 ? 1.8937 0.8706 1.6230 0.2040  -0.3130 -0.0325 221 LYS   G CD  
12914 C  CE  . LYS   G  230 ? 1.8437 0.8783 1.6402 0.2554  -0.2829 -0.0071 221 LYS   G CE  
12915 N  NZ  . LYS   G  230 ? 1.8553 0.9268 1.6839 0.2734  -0.2864 0.0312  221 LYS   G NZ  
12916 N  N   . ASP   G  231 ? 2.1904 0.5869 1.3776 0.2055  -0.3871 0.0106  222 ASP   G N   
12917 C  CA  . ASP   G  231 ? 2.1976 0.7580 1.4873 0.1313  -0.3620 -0.0014 222 ASP   G CA  
12918 C  C   . ASP   G  231 ? 2.2585 0.6363 1.4659 0.1600  -0.3101 0.0297  222 ASP   G C   
12919 O  O   . ASP   G  231 ? 2.2003 0.7810 1.5957 0.1263  -0.3070 0.1560  222 ASP   G O   
12920 C  CB  . ASP   G  231 ? 2.3387 0.8086 1.5486 0.2375  -0.3710 -0.0042 222 ASP   G CB  
12921 C  CG  . ASP   G  231 ? 2.4645 1.0853 1.5002 0.2262  -0.2849 -0.1786 222 ASP   G CG  
12922 O  OD1 . ASP   G  231 ? 2.5374 1.2631 1.4930 0.2193  -0.1936 -0.2325 222 ASP   G OD1 
12923 O  OD2 . ASP   G  231 ? 2.5483 1.1866 1.6965 0.2895  -0.4063 -0.2235 222 ASP   G OD2 
12924 N  N   . LYS   G  232 ? 2.2381 0.6071 1.4233 -0.0134 -0.3397 -0.0111 223 LYS   G N   
12925 C  CA  . LYS   G  232 ? 2.2258 0.5321 1.4118 -0.0569 -0.3388 -0.0715 223 LYS   G CA  
12926 C  C   . LYS   G  232 ? 2.0707 0.5578 1.3723 -0.0331 -0.4437 -0.1659 223 LYS   G C   
12927 O  O   . LYS   G  232 ? 2.1108 0.5150 1.4231 -0.0589 -0.4403 -0.2172 223 LYS   G O   
12928 C  CB  . LYS   G  232 ? 2.3246 0.5933 1.4605 -0.1446 -0.2811 -0.0914 223 LYS   G CB  
12929 C  CG  . LYS   G  232 ? 2.3603 0.7199 1.4340 -0.2012 -0.2322 -0.1495 223 LYS   G CG  
12930 C  CD  . LYS   G  232 ? 2.3856 0.8799 1.4841 -0.2268 -0.1228 -0.1687 223 LYS   G CD  
12931 C  CE  . LYS   G  232 ? 2.4041 1.0246 1.5606 -0.1998 -0.0738 -0.1896 223 LYS   G CE  
12932 N  NZ  . LYS   G  232 ? 2.4196 1.1655 1.5949 -0.2183 -0.0133 -0.1671 223 LYS   G NZ  
12933 N  N   . PHE   G  233 ? 2.0110 0.4157 1.3839 -0.0405 -0.3976 -0.2037 224 PHE   G N   
12934 C  CA  . PHE   G  233 ? 1.9163 0.3616 1.3470 -0.0758 -0.4046 -0.0990 224 PHE   G CA  
12935 C  C   . PHE   G  233 ? 1.9199 0.1528 1.3400 -0.0844 -0.3966 -0.0607 224 PHE   G C   
12936 O  O   . PHE   G  233 ? 1.9044 0.0978 1.3916 -0.1069 -0.3892 -0.0102 224 PHE   G O   
12937 C  CB  . PHE   G  233 ? 1.8469 0.4366 1.3219 -0.0732 -0.4095 -0.0961 224 PHE   G CB  
12938 C  CG  . PHE   G  233 ? 1.7998 0.4565 1.3183 -0.0648 -0.4041 -0.0560 224 PHE   G CG  
12939 C  CD1 . PHE   G  233 ? 1.7480 0.5100 1.3009 -0.0872 -0.4183 -0.0595 224 PHE   G CD1 
12940 C  CD2 . PHE   G  233 ? 1.8076 0.5187 1.3152 -0.0468 -0.4059 -0.0198 224 PHE   G CD2 
12941 C  CE1 . PHE   G  233 ? 1.7383 0.5375 1.2568 -0.0799 -0.4325 -0.1118 224 PHE   G CE1 
12942 C  CE2 . PHE   G  233 ? 1.7934 0.5109 1.3020 -0.0582 -0.4060 -0.0242 224 PHE   G CE2 
12943 C  CZ  . PHE   G  233 ? 1.7420 0.5863 1.2633 -0.0636 -0.4220 -0.0804 224 PHE   G CZ  
12944 N  N   . PHE   G  234 ? 1.9430 0.2017 1.3071 0.0002  -0.3219 -0.0210 225 PHE   G N   
12945 C  CA  . PHE   G  234 ? 1.9610 0.2666 1.3210 0.0032  -0.2929 0.0050  225 PHE   G CA  
12946 C  C   . PHE   G  234 ? 1.9418 0.3054 1.3081 0.0488  -0.2950 -0.0269 225 PHE   G C   
12947 O  O   . PHE   G  234 ? 1.9966 0.1491 1.3162 0.0713  -0.3233 -0.0415 225 PHE   G O   
12948 C  CB  . PHE   G  234 ? 1.9488 0.2312 1.3282 -0.0285 -0.2411 -0.0004 225 PHE   G CB  
12949 C  CG  . PHE   G  234 ? 1.9190 0.2118 1.3554 0.0107  -0.2454 0.0182  225 PHE   G CG  
12950 C  CD1 . PHE   G  234 ? 1.9396 0.1577 1.3395 0.0343  -0.2616 0.0264  225 PHE   G CD1 
12951 C  CD2 . PHE   G  234 ? 1.9500 0.2635 1.3646 0.0265  -0.2148 0.0063  225 PHE   G CD2 
12952 C  CE1 . PHE   G  234 ? 1.8997 0.1615 1.3740 0.0792  -0.2638 0.0704  225 PHE   G CE1 
12953 C  CE2 . PHE   G  234 ? 1.9327 0.2446 1.3939 0.0648  -0.2262 0.0266  225 PHE   G CE2 
12954 C  CZ  . PHE   G  234 ? 1.9352 0.1872 1.3703 0.0818  -0.2612 0.0707  225 PHE   G CZ  
12955 N  N   . THR   G  235 ? 1.9302 0.4514 1.2902 0.0444  -0.2920 -0.0032 226 THR   G N   
12956 C  CA  . THR   G  235 ? 1.9334 0.4056 1.1867 -0.0028 -0.3326 0.0092  226 THR   G CA  
12957 C  C   . THR   G  235 ? 1.9960 0.3996 1.1872 -0.0033 -0.3338 0.0690  226 THR   G C   
12958 O  O   . THR   G  235 ? 2.0187 0.4296 0.9403 -0.1083 -0.3720 -0.0070 226 THR   G O   
12959 C  CB  . THR   G  235 ? 1.9048 0.4097 1.2322 -0.0089 -0.3292 0.0147  226 THR   G CB  
12960 O  OG1 . THR   G  235 ? 1.9043 0.3840 1.3553 0.0145  -0.3289 0.0894  226 THR   G OG1 
12961 C  CG2 . THR   G  235 ? 1.8632 0.4629 1.2427 -0.0086 -0.3274 0.0577  226 THR   G CG2 
12962 N  N   . LEU   G  236 ? 2.0101 0.4375 1.0809 0.0686  -0.3265 0.0799  227 LEU   G N   
12963 C  CA  . LEU   G  236 ? 2.0361 0.4545 1.0767 0.0438  -0.3157 0.1185  227 LEU   G CA  
12964 C  C   . LEU   G  236 ? 2.0636 0.5004 1.0650 0.0389  -0.2555 0.1311  227 LEU   G C   
12965 O  O   . LEU   G  236 ? 2.0781 0.6420 0.9485 0.0861  -0.2755 0.1087  227 LEU   G O   
12966 C  CB  . LEU   G  236 ? 2.0331 0.4527 1.0962 0.0587  -0.3074 0.0789  227 LEU   G CB  
12967 C  CG  . LEU   G  236 ? 2.0332 0.4655 1.1366 0.0681  -0.3165 0.0680  227 LEU   G CG  
12968 C  CD1 . LEU   G  236 ? 2.0084 0.5623 1.1485 0.0724  -0.3574 0.0551  227 LEU   G CD1 
12969 C  CD2 . LEU   G  236 ? 2.0344 0.4793 1.1303 0.0620  -0.3192 0.1000  227 LEU   G CD2 
12970 N  N   . SER   G  237 ? 2.1313 0.5008 1.1099 0.0299  -0.2455 0.1715  228 SER   G N   
12971 C  CA  . SER   G  237 ? 2.1518 0.5263 1.1888 0.0436  -0.2146 0.1894  228 SER   G CA  
12972 C  C   . SER   G  237 ? 2.1940 0.4728 1.2684 0.0477  -0.2140 0.2188  228 SER   G C   
12973 O  O   . SER   G  237 ? 2.1537 0.3894 1.3009 0.0882  -0.2125 0.3444  228 SER   G O   
12974 C  CB  . SER   G  237 ? 2.1763 0.6114 1.1734 0.0016  -0.1837 0.1952  228 SER   G CB  
12975 O  OG  . SER   G  237 ? 2.1886 0.6650 1.2053 -0.0024 -0.2086 0.2375  228 SER   G OG  
12976 N  N   . ALA   G  238 ? 2.2057 0.5919 1.3489 0.0565  -0.1902 0.1738  229 ALA   G N   
12977 C  CA  . ALA   G  238 ? 2.2947 0.7139 1.3697 -0.0084 -0.2155 0.0632  229 ALA   G CA  
12978 C  C   . ALA   G  238 ? 2.3639 0.7660 1.3481 -0.0093 -0.2118 0.0793  229 ALA   G C   
12979 O  O   . ALA   G  238 ? 2.4198 0.8439 1.4240 -0.1020 -0.2624 0.1608  229 ALA   G O   
12980 C  CB  . ALA   G  238 ? 2.2898 0.7375 1.3962 -0.0257 -0.2130 0.0191  229 ALA   G CB  
12981 N  N   . GLU   G  239 ? 2.3338 0.7501 1.3308 -0.0358 -0.1686 0.0408  230 GLU   G N   
12982 C  CA  . GLU   G  239 ? 2.3228 0.8177 1.3738 -0.0039 -0.2119 0.0141  230 GLU   G CA  
12983 C  C   . GLU   G  239 ? 2.3318 0.6651 1.2860 -0.0120 -0.1821 -0.0661 230 GLU   G C   
12984 O  O   . GLU   G  239 ? 2.2756 0.6301 1.4712 -0.0411 -0.2622 -0.0803 230 GLU   G O   
12985 C  CB  . GLU   G  239 ? 2.3451 0.8986 1.4688 -0.0119 -0.1653 0.0754  230 GLU   G CB  
12986 C  CG  . GLU   G  239 ? 2.3919 1.0883 1.5392 -0.0374 -0.0881 0.0722  230 GLU   G CG  
12987 C  CD  . GLU   G  239 ? 2.3616 1.1510 1.6395 0.0000  -0.0644 0.0466  230 GLU   G CD  
12988 O  OE1 . GLU   G  239 ? 2.3937 1.3835 1.7129 -0.1218 -0.1090 0.0576  230 GLU   G OE1 
12989 O  OE2 . GLU   G  239 ? 2.4105 1.3616 1.6151 -0.0208 0.0637  -0.1359 230 GLU   G OE2 
12990 N  N   . ASN   G  240 ? 2.3266 0.6124 1.2449 -0.0393 -0.2279 -0.0711 231 ASN   G N   
12991 C  CA  . ASN   G  240 ? 2.3149 0.6988 1.2188 -0.0448 -0.2598 -0.0536 231 ASN   G CA  
12992 C  C   . ASN   G  240 ? 2.2429 0.7764 1.1781 -0.1027 -0.3065 -0.0877 231 ASN   G C   
12993 O  O   . ASN   G  240 ? 2.3023 0.9911 1.0529 -0.0069 -0.3887 0.0171  231 ASN   G O   
12994 C  CB  . ASN   G  240 ? 2.3241 0.6814 1.2228 -0.0120 -0.2005 -0.0225 231 ASN   G CB  
12995 C  CG  . ASN   G  240 ? 2.3224 0.6848 1.2204 -0.0112 -0.1740 0.0099  231 ASN   G CG  
12996 O  OD1 . ASN   G  240 ? 2.2758 0.5633 1.1542 -0.0394 -0.1286 0.0664  231 ASN   G OD1 
12997 N  ND2 . ASN   G  240 ? 2.3554 0.6917 1.2449 0.0334  -0.1654 0.0191  231 ASN   G ND2 
12998 N  N   . ILE   G  241 ? 2.2168 0.7388 1.2344 -0.0820 -0.2857 -0.1266 232 ILE   G N   
12999 C  CA  . ILE   G  241 ? 2.2203 0.7620 1.2839 -0.1364 -0.2407 -0.2288 232 ILE   G CA  
13000 C  C   . ILE   G  241 ? 2.2137 0.7890 1.2847 -0.1287 -0.2254 -0.2403 232 ILE   G C   
13001 O  O   . ILE   G  241 ? 2.1583 0.9018 1.2730 -0.0992 -0.2267 -0.3238 232 ILE   G O   
13002 C  CB  . ILE   G  241 ? 2.2196 0.7416 1.2201 -0.1796 -0.2332 -0.2503 232 ILE   G CB  
13003 C  CG1 . ILE   G  241 ? 2.2176 0.6650 1.2456 -0.2771 -0.2618 -0.2961 232 ILE   G CG1 
13004 C  CG2 . ILE   G  241 ? 2.2374 0.7484 1.2682 -0.1911 -0.2394 -0.2160 232 ILE   G CG2 
13005 C  CD1 . ILE   G  241 ? 2.2046 0.6263 1.2329 -0.3133 -0.2567 -0.3008 232 ILE   G CD1 
13006 N  N   . GLU   G  242 ? 2.2697 0.7764 1.3375 -0.1696 -0.1984 -0.1357 233 GLU   G N   
13007 C  CA  . GLU   G  242 ? 2.3251 0.8298 1.3232 -0.1494 -0.1567 -0.0940 233 GLU   G CA  
13008 C  C   . GLU   G  242 ? 2.2823 0.7703 1.3955 -0.1439 -0.1457 -0.0440 233 GLU   G C   
13009 O  O   . GLU   G  242 ? 2.2213 0.9004 1.2675 -0.1542 -0.1730 -0.0207 233 GLU   G O   
13010 C  CB  . GLU   G  242 ? 2.3896 0.8312 1.3507 -0.1652 -0.0873 -0.1049 233 GLU   G CB  
13011 C  CG  . GLU   G  242 ? 2.4810 0.8946 1.3753 -0.1182 -0.0634 -0.1396 233 GLU   G CG  
13012 C  CD  . GLU   G  242 ? 2.5326 0.9360 1.3598 -0.0745 -0.0672 -0.2876 233 GLU   G CD  
13013 O  OE1 . GLU   G  242 ? 2.5689 1.1512 1.2592 0.0233  -0.1274 -0.1858 233 GLU   G OE1 
13014 O  OE2 . GLU   G  242 ? 2.5453 1.0439 1.3495 -0.0083 -0.0910 -0.3197 233 GLU   G OE2 
13015 N  N   . GLU   G  243 ? 2.2128 0.8208 1.4266 -0.0544 -0.1674 -0.0633 234 GLU   G N   
13016 C  CA  . GLU   G  243 ? 2.2365 0.9498 1.3833 -0.0218 -0.1915 -0.0898 234 GLU   G CA  
13017 C  C   . GLU   G  243 ? 2.2566 0.6862 1.3102 -0.0151 -0.2512 -0.1730 234 GLU   G C   
13018 O  O   . GLU   G  243 ? 2.3485 0.7222 1.2832 -0.0131 -0.2841 -0.1958 234 GLU   G O   
13019 C  CB  . GLU   G  243 ? 2.2144 0.9475 1.4227 0.0230  -0.1982 -0.0404 234 GLU   G CB  
13020 C  CG  . GLU   G  243 ? 2.2116 1.2129 1.4154 -0.0088 -0.2370 0.0539  234 GLU   G CG  
13021 C  CD  . GLU   G  243 ? 2.1075 1.2341 1.4223 0.0047  -0.2532 0.0636  234 GLU   G CD  
13022 O  OE1 . GLU   G  243 ? 2.1106 1.3257 1.4828 0.0449  -0.2260 0.1102  234 GLU   G OE1 
13023 O  OE2 . GLU   G  243 ? 2.0741 1.4522 1.4120 -0.0800 -0.2051 0.0667  234 GLU   G OE2 
13024 N  N   . ARG   G  244 ? 2.2843 0.6155 1.3294 0.0377  -0.1851 -0.1725 235 ARG   G N   
13025 C  CA  . ARG   G  244 ? 2.2498 0.7609 1.3389 0.0559  -0.1603 -0.1684 235 ARG   G CA  
13026 C  C   . ARG   G  244 ? 2.2365 0.8287 1.3057 0.0010  -0.2281 -0.2588 235 ARG   G C   
13027 O  O   . ARG   G  244 ? 2.1645 0.9335 1.2868 0.0339  -0.2187 -0.2286 235 ARG   G O   
13028 C  CB  . ARG   G  244 ? 2.2303 0.8178 1.3381 0.0860  -0.1140 -0.1049 235 ARG   G CB  
13029 C  CG  . ARG   G  244 ? 2.2276 0.8612 1.3804 0.1167  -0.1068 -0.0504 235 ARG   G CG  
13030 C  CD  . ARG   G  244 ? 2.2088 0.8532 1.3260 0.1198  -0.1009 -0.0106 235 ARG   G CD  
13031 N  NE  . ARG   G  244 ? 2.2200 0.9399 1.3244 0.1436  -0.0837 0.0399  235 ARG   G NE  
13032 C  CZ  . ARG   G  244 ? 2.1920 1.1171 1.2843 0.1738  -0.1253 0.1062  235 ARG   G CZ  
13033 N  NH1 . ARG   G  244 ? 2.1958 1.1903 1.3502 0.1670  -0.0956 0.0990  235 ARG   G NH1 
13034 N  NH2 . ARG   G  244 ? 2.2156 1.2431 1.3396 0.1995  -0.1549 0.1425  235 ARG   G NH2 
13035 N  N   . LEU   G  245 ? 2.2918 0.8291 1.3272 0.0392  -0.2658 -0.3607 236 LEU   G N   
13036 C  CA  . LEU   G  245 ? 2.3752 0.8511 1.3421 0.0452  -0.2965 -0.4107 236 LEU   G CA  
13037 C  C   . LEU   G  245 ? 2.3950 1.0034 1.3227 0.0217  -0.3073 -0.2563 236 LEU   G C   
13038 O  O   . LEU   G  245 ? 2.4414 1.1307 1.3738 -0.0725 -0.4133 -0.2362 236 LEU   G O   
13039 C  CB  . LEU   G  245 ? 2.4252 0.6399 1.2774 0.1039  -0.3045 -0.5317 236 LEU   G CB  
13040 C  CG  . LEU   G  245 ? 2.4693 0.5903 1.2479 0.1167  -0.2981 -0.5786 236 LEU   G CG  
13041 C  CD1 . LEU   G  245 ? 2.4415 0.5127 1.2825 0.1776  -0.3216 -0.6234 236 LEU   G CD1 
13042 C  CD2 . LEU   G  245 ? 2.4611 0.6221 1.3127 0.0865  -0.2772 -0.5894 236 LEU   G CD2 
13043 N  N   . VAL   G  246 ? 2.3622 1.0583 1.3185 0.0469  -0.2773 -0.2091 237 VAL   G N   
13044 C  CA  . VAL   G  246 ? 2.3229 1.0372 1.3074 0.0607  -0.2309 -0.1251 237 VAL   G CA  
13045 C  C   . VAL   G  246 ? 2.3318 0.9973 1.2749 0.1058  -0.2749 -0.1038 237 VAL   G C   
13046 O  O   . VAL   G  246 ? 2.2740 1.1258 1.1833 0.0930  -0.3721 -0.0140 237 VAL   G O   
13047 C  CB  . VAL   G  246 ? 2.3776 0.9980 1.3597 0.0950  -0.1886 -0.1118 237 VAL   G CB  
13048 C  CG1 . VAL   G  246 ? 2.3762 0.9732 1.3811 0.0943  -0.2149 -0.1104 237 VAL   G CG1 
13049 C  CG2 . VAL   G  246 ? 2.3836 1.0690 1.3871 0.0973  -0.1513 -0.0931 237 VAL   G CG2 
13050 N  N   . ALA   G  247 ? 2.2720 0.8908 1.3340 0.1143  -0.3167 -0.0863 238 ALA   G N   
13051 C  CA  . ALA   G  247 ? 2.2724 0.9428 1.3675 0.1151  -0.3370 -0.0999 238 ALA   G CA  
13052 C  C   . ALA   G  247 ? 2.2293 0.9531 1.4435 0.1053  -0.3075 -0.1499 238 ALA   G C   
13053 O  O   . ALA   G  247 ? 2.1975 0.8692 1.4149 0.1740  -0.3145 -0.0872 238 ALA   G O   
13054 C  CB  . ALA   G  247 ? 2.2519 0.9621 1.3819 0.1237  -0.3189 -0.1000 238 ALA   G CB  
13055 N  N   . ILE   G  248 ? 2.1730 0.9324 1.4244 0.0434  -0.3003 -0.1632 239 ILE   G N   
13056 C  CA  . ILE   G  248 ? 2.1682 1.0045 1.5519 -0.0723 -0.2648 -0.2273 239 ILE   G CA  
13057 C  C   . ILE   G  248 ? 2.2603 1.1388 1.4984 -0.1734 -0.2886 -0.2663 239 ILE   G C   
13058 O  O   . ILE   G  248 ? 2.3207 1.2612 1.4863 -0.2597 -0.2690 -0.3141 239 ILE   G O   
13059 C  CB  . ILE   G  248 ? 2.0950 0.8965 1.5286 -0.0800 -0.2386 -0.2792 239 ILE   G CB  
13060 C  CG1 . ILE   G  248 ? 2.0741 0.7731 1.6101 -0.0520 -0.2109 -0.2745 239 ILE   G CG1 
13061 C  CG2 . ILE   G  248 ? 2.0600 0.9280 1.5810 -0.1347 -0.2533 -0.2863 239 ILE   G CG2 
13062 C  CD1 . ILE   G  248 ? 2.0610 0.6757 1.5727 -0.0308 -0.1756 -0.2980 239 ILE   G CD1 
13063 N  N   . ALA   G  249 ? 2.2920 1.3259 1.5568 -0.1703 -0.2436 -0.1911 240 ALA   G N   
13064 C  CA  . ALA   G  249 ? 2.3526 1.3879 1.5466 -0.1683 -0.2276 -0.2020 240 ALA   G CA  
13065 C  C   . ALA   G  249 ? 2.4215 1.4392 1.6015 -0.1974 -0.2625 -0.0972 240 ALA   G C   
13066 O  O   . ALA   G  249 ? 2.4101 1.4521 1.6857 -0.3276 -0.2305 -0.0711 240 ALA   G O   
13067 C  CB  . ALA   G  249 ? 2.3617 1.4719 1.5202 -0.1342 -0.1903 -0.1847 240 ALA   G CB  
13068 N  N   . GLU   G  250 ? 2.5402 1.5043 1.6511 -0.1428 -0.2924 -0.0100 241 GLU   G N   
13069 C  CA  . GLU   G  250 ? 2.5579 1.6272 1.7071 -0.0802 -0.3262 0.0033  241 GLU   G CA  
13070 C  C   . GLU   G  250 ? 2.5114 1.6200 1.6965 0.0096  -0.4277 0.0462  241 GLU   G C   
13071 O  O   . GLU   G  250 ? 2.4378 1.5877 1.5989 0.0204  -0.3915 -0.0233 241 GLU   G O   
13072 C  CB  . GLU   G  250 ? 2.6972 1.6145 1.7731 -0.0411 -0.2827 0.0272  241 GLU   G CB  
13073 C  CG  . GLU   G  250 ? 2.7653 1.6948 1.8473 -0.0020 -0.1847 0.0069  241 GLU   G CG  
13074 C  CD  . GLU   G  250 ? 2.8144 1.6570 1.8801 0.0467  -0.1575 -0.0013 241 GLU   G CD  
13075 O  OE1 . GLU   G  250 ? 2.8333 1.6086 1.9019 0.0576  -0.0880 -0.0504 241 GLU   G OE1 
13076 O  OE2 . GLU   G  250 ? 2.8343 1.6790 1.8885 0.0685  -0.1832 -0.0156 241 GLU   G OE2 
13077 N  N   . GLN   G  251 ? 2.4547 1.6653 1.7628 0.0552  -0.4550 0.1274  242 GLN   G N   
13078 C  CA  . GLN   G  251 ? 2.3950 1.8857 1.8735 0.1552  -0.5164 0.1193  242 GLN   G CA  
13079 C  C   . GLN   G  251 ? 2.4056 2.0022 1.8616 0.1217  -0.5860 0.2508  242 GLN   G C   
13080 O  O   . GLN   G  251 ? 2.4274 2.2412 1.9908 0.0584  -0.5731 0.1225  242 GLN   G O   
13081 C  CB  . GLN   G  251 ? 2.3729 1.7991 1.9434 0.2086  -0.5218 0.1421  242 GLN   G CB  
13082 C  CG  . GLN   G  251 ? 2.3732 1.8259 2.0048 0.2387  -0.4846 0.1134  242 GLN   G CG  
13083 C  CD  . GLN   G  251 ? 2.4052 1.8771 1.9799 0.2618  -0.4644 0.1635  242 GLN   G CD  
13084 O  OE1 . GLN   G  251 ? 2.4202 1.8331 1.9461 0.3035  -0.5531 0.2340  242 GLN   G OE1 
13085 N  NE2 . GLN   G  251 ? 2.4134 1.9686 2.0968 0.2787  -0.4324 0.1553  242 GLN   G NE2 
13086 N  N   . THR   H  1   ? 1.7599 1.0958 1.2987 0.1167  -0.2665 -0.0676 2   THR   H N   
13087 C  CA  . THR   H  1   ? 1.4531 0.8196 1.3171 0.1300  -0.2953 -0.0389 2   THR   H CA  
13088 C  C   . THR   H  1   ? 1.4436 0.7803 1.2666 0.1129  -0.3198 0.0183  2   THR   H C   
13089 O  O   . THR   H  1   ? 1.3862 0.7765 1.2606 0.1344  -0.3956 0.0686  2   THR   H O   
13090 C  CB  . THR   H  1   ? 1.4225 0.8281 1.3025 0.1238  -0.2929 -0.0567 2   THR   H CB  
13091 O  OG1 . THR   H  1   ? 1.4435 0.8345 1.3158 0.1201  -0.2888 -0.0714 2   THR   H OG1 
13092 C  CG2 . THR   H  1   ? 1.4303 0.8442 1.3144 0.1312  -0.2970 -0.0379 2   THR   H CG2 
13093 N  N   . ILE   H  2   ? 1.5055 0.6976 1.2366 0.0810  -0.3194 -0.0224 3   ILE   H N   
13094 C  CA  . ILE   H  2   ? 1.5731 0.6892 1.2943 0.0757  -0.2690 -0.0473 3   ILE   H CA  
13095 C  C   . ILE   H  2   ? 1.5408 0.6271 1.3028 0.0794  -0.2337 -0.0637 3   ILE   H C   
13096 O  O   . ILE   H  2   ? 1.5178 0.7327 1.3619 0.0891  -0.1765 -0.0706 3   ILE   H O   
13097 C  CB  . ILE   H  2   ? 1.6706 0.6377 1.2676 0.0828  -0.3239 -0.0937 3   ILE   H CB  
13098 C  CG1 . ILE   H  2   ? 1.7164 0.6430 1.2601 0.0666  -0.3198 -0.1359 3   ILE   H CG1 
13099 C  CG2 . ILE   H  2   ? 1.7651 0.7018 1.2789 0.0862  -0.2922 -0.1361 3   ILE   H CG2 
13100 C  CD1 . ILE   H  2   ? 1.7115 0.6564 1.3465 0.0782  -0.3283 -0.1369 3   ILE   H CD1 
13101 N  N   . VAL   H  3   ? 1.4724 0.5976 1.3255 0.0541  -0.1974 -0.0518 4   VAL   H N   
13102 C  CA  . VAL   H  3   ? 1.4340 0.6057 1.3246 0.0418  -0.2188 -0.0393 4   VAL   H CA  
13103 C  C   . VAL   H  3   ? 1.4523 0.6223 1.3080 -0.0043 -0.2036 -0.0376 4   VAL   H C   
13104 O  O   . VAL   H  3   ? 1.4198 0.5853 1.2799 0.0038  -0.2184 -0.0616 4   VAL   H O   
13105 C  CB  . VAL   H  3   ? 1.3986 0.6257 1.3523 0.0360  -0.2213 -0.0227 4   VAL   H CB  
13106 C  CG1 . VAL   H  3   ? 1.3949 0.6436 1.3534 0.0367  -0.2423 -0.0336 4   VAL   H CG1 
13107 C  CG2 . VAL   H  3   ? 1.3863 0.6197 1.3551 0.0515  -0.2216 -0.0192 4   VAL   H CG2 
13108 N  N   . GLY   H  4   ? 1.4771 0.6185 1.2935 -0.0203 -0.2179 -0.0485 5   GLY   H N   
13109 C  CA  . GLY   H  4   ? 1.4652 0.5971 1.2824 -0.0215 -0.2327 -0.0264 5   GLY   H CA  
13110 C  C   . GLY   H  4   ? 1.4560 0.6065 1.2863 -0.0175 -0.2528 -0.0275 5   GLY   H C   
13111 O  O   . GLY   H  4   ? 1.4643 0.6171 1.2674 0.0335  -0.2171 0.0241  5   GLY   H O   
13112 N  N   . VAL   H  5   ? 1.4705 0.6269 1.2593 -0.0241 -0.2607 -0.0269 6   VAL   H N   
13113 C  CA  . VAL   H  5   ? 1.5212 0.6956 1.2693 -0.0386 -0.2825 -0.0052 6   VAL   H CA  
13114 C  C   . VAL   H  5   ? 1.5412 0.6978 1.2427 0.0066  -0.2885 -0.0054 6   VAL   H C   
13115 O  O   . VAL   H  5   ? 1.5065 0.6671 1.3387 0.0060  -0.3070 -0.0157 6   VAL   H O   
13116 C  CB  . VAL   H  5   ? 1.5156 0.6837 1.2780 -0.0582 -0.2976 -0.0073 6   VAL   H CB  
13117 C  CG1 . VAL   H  5   ? 1.5755 0.7194 1.2913 -0.0544 -0.2993 0.0311  6   VAL   H CG1 
13118 C  CG2 . VAL   H  5   ? 1.5104 0.6795 1.2989 -0.0969 -0.3015 0.0097  6   VAL   H CG2 
13119 N  N   . LYS   H  6   ? 1.5910 0.7339 1.2003 -0.0065 -0.3209 -0.0316 7   LYS   H N   
13120 C  CA  . LYS   H  6   ? 1.6533 0.7863 1.1730 -0.0366 -0.3305 -0.0499 7   LYS   H CA  
13121 C  C   . LYS   H  6   ? 1.6655 0.8470 1.1625 -0.0417 -0.3431 -0.0827 7   LYS   H C   
13122 O  O   . LYS   H  6   ? 1.7103 0.8049 1.0301 -0.0684 -0.3560 -0.1682 7   LYS   H O   
13123 C  CB  . LYS   H  6   ? 1.6851 0.7815 1.1462 -0.0418 -0.3210 -0.0842 7   LYS   H CB  
13124 C  CG  . LYS   H  6   ? 1.6932 0.7953 1.1509 -0.0292 -0.3149 -0.0964 7   LYS   H CG  
13125 C  CD  . LYS   H  6   ? 1.7648 0.8493 1.1893 -0.0263 -0.2879 -0.1541 7   LYS   H CD  
13126 C  CE  . LYS   H  6   ? 1.7775 0.8928 1.2193 -0.0394 -0.2600 -0.1683 7   LYS   H CE  
13127 N  NZ  . LYS   H  6   ? 1.7761 0.9371 1.2680 -0.0388 -0.2468 -0.2337 7   LYS   H NZ  
13128 N  N   . PHE   H  7   ? 1.6801 0.8131 1.2277 -0.0335 -0.3361 -0.0817 8   PHE   H N   
13129 C  CA  . PHE   H  7   ? 1.6763 0.8257 1.2737 0.0012  -0.3564 -0.1150 8   PHE   H CA  
13130 C  C   . PHE   H  7   ? 1.7098 0.8454 1.2738 0.0170  -0.3701 -0.1251 8   PHE   H C   
13131 O  O   . PHE   H  7   ? 1.6707 0.9508 1.2258 0.0213  -0.3252 -0.1495 8   PHE   H O   
13132 C  CB  . PHE   H  7   ? 1.6827 0.8697 1.2940 0.0299  -0.3450 -0.1736 8   PHE   H CB  
13133 C  CG  . PHE   H  7   ? 1.6894 0.8705 1.3031 0.0224  -0.2930 -0.2046 8   PHE   H CG  
13134 C  CD1 . PHE   H  7   ? 1.6838 1.0094 1.3718 -0.0301 -0.3289 -0.2279 8   PHE   H CD1 
13135 C  CD2 . PHE   H  7   ? 1.6728 0.8958 1.2801 0.0151  -0.2839 -0.2860 8   PHE   H CD2 
13136 C  CE1 . PHE   H  7   ? 1.6994 1.0657 1.3742 -0.0500 -0.3026 -0.2069 8   PHE   H CE1 
13137 C  CE2 . PHE   H  7   ? 1.6946 0.9455 1.3104 -0.0106 -0.2533 -0.2688 8   PHE   H CE2 
13138 C  CZ  . PHE   H  7   ? 1.6948 1.0335 1.3458 -0.0530 -0.2799 -0.2713 8   PHE   H CZ  
13139 N  N   . ASN   H  8   ? 1.7377 0.9207 1.3340 0.0467  -0.4195 -0.1146 9   ASN   H N   
13140 C  CA  . ASN   H  8   ? 1.7567 0.9889 1.3785 -0.0095 -0.4701 -0.1849 9   ASN   H CA  
13141 C  C   . ASN   H  8   ? 1.7853 0.9813 1.4139 -0.0490 -0.4985 -0.1833 9   ASN   H C   
13142 O  O   . ASN   H  8   ? 1.8050 0.9709 1.4234 -0.0360 -0.5038 -0.1933 9   ASN   H O   
13143 C  CB  . ASN   H  8   ? 1.7779 1.0106 1.4269 -0.0538 -0.5001 -0.2258 9   ASN   H CB  
13144 C  CG  . ASN   H  8   ? 1.8010 1.0427 1.4617 -0.0247 -0.5167 -0.2769 9   ASN   H CG  
13145 O  OD1 . ASN   H  8   ? 1.8308 1.1454 1.4886 -0.1053 -0.4769 -0.2658 9   ASN   H OD1 
13146 N  ND2 . ASN   H  8   ? 1.8041 0.9952 1.4875 -0.0967 -0.5370 -0.3143 9   ASN   H ND2 
13147 N  N   . ASN   H  9   ? 1.7926 0.9761 1.4250 -0.0662 -0.5169 -0.1582 10  ASN   H N   
13148 C  CA  . ASN   H  9   ? 1.8385 0.9917 1.5027 -0.0242 -0.5225 -0.1014 10  ASN   H CA  
13149 C  C   . ASN   H  9   ? 1.7991 0.9755 1.5299 0.0212  -0.5397 -0.1287 10  ASN   H C   
13150 O  O   . ASN   H  9   ? 1.8485 1.0261 1.6788 0.0817  -0.5210 -0.0363 10  ASN   H O   
13151 C  CB  . ASN   H  9   ? 1.8520 1.0691 1.5110 -0.0517 -0.5436 -0.1454 10  ASN   H CB  
13152 C  CG  . ASN   H  9   ? 1.9115 1.1138 1.4985 -0.0876 -0.5272 -0.2278 10  ASN   H CG  
13153 O  OD1 . ASN   H  9   ? 1.9952 1.2164 1.4269 -0.0636 -0.5320 -0.2627 10  ASN   H OD1 
13154 N  ND2 . ASN   H  9   ? 1.9405 1.1255 1.5421 -0.1054 -0.5032 -0.2256 10  ASN   H ND2 
13155 N  N   . GLY   H  10  ? 1.7360 0.7795 1.4382 0.0960  -0.5244 -0.0302 11  GLY   H N   
13156 C  CA  . GLY   H  10  ? 1.7000 0.7652 1.4366 0.1320  -0.4938 0.0134  11  GLY   H CA  
13157 C  C   . GLY   H  10  ? 1.6855 0.7219 1.3438 0.1553  -0.4968 0.0702  11  GLY   H C   
13158 O  O   . GLY   H  10  ? 1.7248 0.7657 1.3210 0.1811  -0.5037 0.1044  11  GLY   H O   
13159 N  N   . VAL   H  11  ? 1.6442 0.6924 1.3322 0.1425  -0.4677 0.0809  12  VAL   H N   
13160 C  CA  . VAL   H  11  ? 1.5829 0.6531 1.3057 0.1135  -0.4277 0.1170  12  VAL   H CA  
13161 C  C   . VAL   H  11  ? 1.5977 0.6423 1.3012 0.1272  -0.4240 0.1078  12  VAL   H C   
13162 O  O   . VAL   H  11  ? 1.6169 0.6738 1.2728 0.1310  -0.4058 0.1240  12  VAL   H O   
13163 C  CB  . VAL   H  11  ? 1.5533 0.6718 1.2937 0.0650  -0.4206 0.1109  12  VAL   H CB  
13164 C  CG1 . VAL   H  11  ? 1.5594 0.6670 1.2996 0.0682  -0.4140 0.1063  12  VAL   H CG1 
13165 C  CG2 . VAL   H  11  ? 1.5319 0.6621 1.2653 0.0650  -0.4257 0.1443  12  VAL   H CG2 
13166 N  N   . VAL   H  12  ? 1.5618 0.6501 1.2859 0.0773  -0.3536 0.0994  13  VAL   H N   
13167 C  CA  . VAL   H  12  ? 1.5688 0.6618 1.3264 0.0469  -0.3205 0.0680  13  VAL   H CA  
13168 C  C   . VAL   H  12  ? 1.5829 0.5928 1.3360 0.0203  -0.2880 0.0648  13  VAL   H C   
13169 O  O   . VAL   H  12  ? 1.6297 0.6261 1.2651 -0.0182 -0.2776 0.0349  13  VAL   H O   
13170 C  CB  . VAL   H  12  ? 1.5570 0.7097 1.3647 0.0659  -0.2941 0.0562  13  VAL   H CB  
13171 C  CG1 . VAL   H  12  ? 1.5767 0.6969 1.3481 0.0566  -0.2991 0.0419  13  VAL   H CG1 
13172 C  CG2 . VAL   H  12  ? 1.5595 0.7364 1.3929 0.0704  -0.2744 0.0485  13  VAL   H CG2 
13173 N  N   . ILE   H  13  ? 1.5818 0.5305 1.3352 0.0129  -0.2735 0.0452  14  ILE   H N   
13174 C  CA  . ILE   H  13  ? 1.5781 0.5023 1.3726 -0.0110 -0.2531 0.0319  14  ILE   H CA  
13175 C  C   . ILE   H  13  ? 1.5675 0.4966 1.3800 0.0061  -0.2628 0.0305  14  ILE   H C   
13176 O  O   . ILE   H  13  ? 1.6083 0.3782 1.3819 0.0117  -0.2525 0.0242  14  ILE   H O   
13177 C  CB  . ILE   H  13  ? 1.5600 0.4989 1.3704 -0.0317 -0.2570 0.0314  14  ILE   H CB  
13178 C  CG1 . ILE   H  13  ? 1.6079 0.6254 1.3850 -0.0673 -0.2046 0.0616  14  ILE   H CG1 
13179 C  CG2 . ILE   H  13  ? 1.5658 0.4701 1.3596 -0.0828 -0.2396 0.0260  14  ILE   H CG2 
13180 C  CD1 . ILE   H  13  ? 1.5615 0.7345 1.4381 -0.0552 -0.2291 0.0383  14  ILE   H CD1 
13181 N  N   . ALA   H  14  ? 1.5507 0.5294 1.3572 0.0200  -0.3118 0.0129  15  ALA   H N   
13182 C  CA  . ALA   H  14  ? 1.5115 0.4972 1.3618 0.0367  -0.3262 0.0354  15  ALA   H CA  
13183 C  C   . ALA   H  14  ? 1.4664 0.3864 1.3506 0.0374  -0.3041 0.0692  15  ALA   H C   
13184 O  O   . ALA   H  14  ? 1.4345 0.3001 1.3664 0.0637  -0.3309 0.0773  15  ALA   H O   
13185 C  CB  . ALA   H  14  ? 1.5139 0.5017 1.4072 0.0510  -0.3307 0.0256  15  ALA   H CB  
13186 N  N   . ALA   H  15  ? 1.4508 0.3810 1.3405 0.0167  -0.3154 0.0624  16  ALA   H N   
13187 C  CA  . ALA   H  15  ? 1.4346 0.4577 1.3417 0.0026  -0.3204 0.0604  16  ALA   H CA  
13188 C  C   . ALA   H  15  ? 1.3748 0.5493 1.3669 -0.0203 -0.2982 0.0849  16  ALA   H C   
13189 O  O   . ALA   H  15  ? 1.3894 0.5933 1.3626 -0.0640 -0.3103 0.0840  16  ALA   H O   
13190 C  CB  . ALA   H  15  ? 1.4256 0.4346 1.3252 0.0251  -0.3189 0.0072  16  ALA   H CB  
13191 N  N   . ASP   H  16  ? 1.3871 0.5641 1.3835 -0.0080 -0.2922 0.0652  17  ASP   H N   
13192 C  CA  . ASP   H  16  ? 1.3557 0.6483 1.4884 0.0065  -0.2775 0.0145  17  ASP   H CA  
13193 C  C   . ASP   H  16  ? 1.3656 0.7204 1.4935 0.0130  -0.2639 0.0328  17  ASP   H C   
13194 O  O   . ASP   H  16  ? 1.2791 0.8275 1.5212 0.1042  -0.2174 0.0435  17  ASP   H O   
13195 C  CB  . ASP   H  16  ? 1.3539 0.6601 1.5144 -0.0191 -0.3160 0.0377  17  ASP   H CB  
13196 C  CG  . ASP   H  16  ? 1.3369 0.6799 1.5672 0.0022  -0.3327 0.0423  17  ASP   H CG  
13197 O  OD1 . ASP   H  16  ? 1.3234 0.6592 1.5758 -0.0135 -0.3560 -0.0405 17  ASP   H OD1 
13198 O  OD2 . ASP   H  16  ? 1.3341 0.7793 1.5696 -0.0001 -0.3443 -0.0105 17  ASP   H OD2 
13199 N  N   . THR   H  17  ? 1.4125 0.7745 1.4824 -0.0167 -0.2787 0.0041  18  THR   H N   
13200 C  CA  . THR   H  17  ? 1.4834 0.7159 1.5296 -0.0323 -0.3357 0.0447  18  THR   H CA  
13201 C  C   . THR   H  17  ? 1.5270 0.7734 1.5155 -0.0301 -0.3272 0.0281  18  THR   H C   
13202 O  O   . THR   H  17  ? 1.4807 0.5954 1.5760 -0.1191 -0.2762 -0.0148 18  THR   H O   
13203 C  CB  . THR   H  17  ? 1.4950 0.7555 1.5735 -0.0640 -0.3285 0.0575  18  THR   H CB  
13204 O  OG1 . THR   H  17  ? 1.5273 0.7742 1.6326 -0.0851 -0.3541 0.0880  18  THR   H OG1 
13205 C  CG2 . THR   H  17  ? 1.4873 0.7436 1.5509 -0.0470 -0.3619 0.0779  18  THR   H CG2 
13206 N  N   . ARG   H  18  ? 1.5208 0.8456 1.5014 -0.0621 -0.3239 0.0008  19  ARG   H N   
13207 C  CA  . ARG   H  18  ? 1.5692 0.9070 1.4515 0.0311  -0.2955 -0.0461 19  ARG   H CA  
13208 C  C   . ARG   H  18  ? 1.5593 0.8425 1.3659 0.0546  -0.2532 -0.0627 19  ARG   H C   
13209 O  O   . ARG   H  18  ? 1.4952 0.8481 1.4096 0.0385  -0.2572 -0.0243 19  ARG   H O   
13210 C  CB  . ARG   H  18  ? 1.6533 0.9072 1.4346 0.0200  -0.3197 -0.0713 19  ARG   H CB  
13211 C  CG  . ARG   H  18  ? 1.6612 1.0292 1.3851 0.0478  -0.3229 -0.1030 19  ARG   H CG  
13212 C  CD  . ARG   H  18  ? 1.6456 1.0142 1.3661 0.0543  -0.3455 -0.1427 19  ARG   H CD  
13213 N  NE  . ARG   H  18  ? 1.6474 1.1429 1.3461 0.1019  -0.3439 -0.1406 19  ARG   H NE  
13214 C  CZ  . ARG   H  18  ? 1.6639 1.1756 1.4204 0.1570  -0.3203 -0.1196 19  ARG   H CZ  
13215 N  NH1 . ARG   H  18  ? 1.6410 1.2636 1.4919 0.1090  -0.2883 -0.1176 19  ARG   H NH1 
13216 N  NH2 . ARG   H  18  ? 1.7358 1.2084 1.3934 0.1818  -0.2556 -0.1315 19  ARG   H NH2 
13217 N  N   . SER   H  19  ? 1.5122 0.7805 1.3392 0.0994  -0.2716 -0.1363 20  SER   H N   
13218 C  CA  . SER   H  19  ? 1.5134 0.7404 1.3019 0.1096  -0.2575 -0.1348 20  SER   H CA  
13219 C  C   . SER   H  19  ? 1.4833 0.6358 1.3066 0.1378  -0.2059 -0.1174 20  SER   H C   
13220 O  O   . SER   H  19  ? 1.5671 0.6372 1.3196 0.1296  -0.1480 -0.0936 20  SER   H O   
13221 C  CB  . SER   H  19  ? 1.5209 0.7500 1.2394 0.1220  -0.2807 -0.1377 20  SER   H CB  
13222 O  OG  . SER   H  19  ? 1.5519 0.7994 1.2327 0.1080  -0.2639 -0.1456 20  SER   H OG  
13223 N  N   . THR   H  20  ? 1.4547 0.6178 1.3413 0.1683  -0.2500 -0.1008 21  THR   H N   
13224 C  CA  . THR   H  20  ? 1.4487 0.7136 1.3281 0.1419  -0.3110 -0.1108 21  THR   H CA  
13225 C  C   . THR   H  20  ? 1.4527 0.7135 1.3428 0.1563  -0.3127 -0.1202 21  THR   H C   
13226 O  O   . THR   H  20  ? 1.5059 0.5668 1.2424 0.1217  -0.3664 -0.1616 21  THR   H O   
13227 C  CB  . THR   H  20  ? 1.4669 0.7226 1.3928 0.1077  -0.3255 -0.0892 21  THR   H CB  
13228 O  OG1 . THR   H  20  ? 1.3963 0.6236 1.3960 0.0966  -0.3541 -0.0655 21  THR   H OG1 
13229 C  CG2 . THR   H  20  ? 1.4750 0.6851 1.4722 0.1299  -0.3193 -0.0653 21  THR   H CG2 
13230 N  N   . GLN   H  21  ? 1.4858 0.8557 1.3333 0.1260  -0.3118 -0.1189 22  GLN   H N   
13231 C  CA  . GLN   H  21  ? 1.4971 0.9493 1.3427 0.1204  -0.3241 -0.0818 22  GLN   H CA  
13232 C  C   . GLN   H  21  ? 1.4439 0.9624 1.2979 0.0807  -0.3338 -0.0615 22  GLN   H C   
13233 O  O   . GLN   H  21  ? 1.3830 0.9100 1.3104 0.0755  -0.3446 -0.0476 22  GLN   H O   
13234 C  CB  . GLN   H  21  ? 1.5630 1.0202 1.3611 0.1119  -0.3165 -0.0488 22  GLN   H CB  
13235 C  CG  . GLN   H  21  ? 1.5785 1.1015 1.4482 0.1505  -0.3128 -0.0244 22  GLN   H CG  
13236 C  CD  . GLN   H  21  ? 1.6527 1.1728 1.5542 0.0703  -0.2379 0.0210  22  GLN   H CD  
13237 O  OE1 . GLN   H  21  ? 1.6734 1.1150 1.5510 0.0577  -0.2654 -0.1089 22  GLN   H OE1 
13238 N  NE2 . GLN   H  21  ? 1.6785 1.3563 1.5965 0.0741  -0.2666 0.0474  22  GLN   H NE2 
13239 N  N   . GLY   H  22  ? 1.4403 0.9477 1.2800 0.0723  -0.3462 -0.0669 23  GLY   H N   
13240 C  CA  . GLY   H  22  ? 1.4137 0.9301 1.3129 0.1202  -0.3378 -0.0382 23  GLY   H CA  
13241 C  C   . GLY   H  22  ? 1.3967 0.8828 1.3276 0.0988  -0.3257 -0.0177 23  GLY   H C   
13242 O  O   . GLY   H  22  ? 1.2913 0.7753 1.3223 0.1229  -0.3542 0.0573  23  GLY   H O   
13243 N  N   . PRO   H  23  ? 1.3988 0.8732 1.3523 0.0929  -0.3101 -0.0178 24  PRO   H N   
13244 C  CA  . PRO   H  23  ? 1.3743 0.8672 1.3944 0.0800  -0.3033 -0.0271 24  PRO   H CA  
13245 C  C   . PRO   H  23  ? 1.3782 0.8505 1.4138 0.0786  -0.2831 -0.0532 24  PRO   H C   
13246 O  O   . PRO   H  23  ? 1.3622 0.7357 1.3851 0.0432  -0.2452 -0.0421 24  PRO   H O   
13247 C  CB  . PRO   H  23  ? 1.3834 0.9090 1.3971 0.0558  -0.3173 -0.0600 24  PRO   H CB  
13248 C  CG  . PRO   H  23  ? 1.4041 0.8975 1.3707 0.0621  -0.2965 -0.0671 24  PRO   H CG  
13249 C  CD  . PRO   H  23  ? 1.4119 0.8966 1.3501 0.0811  -0.3043 -0.0294 24  PRO   H CD  
13250 N  N   . ILE   H  24  ? 1.3848 0.8610 1.4125 0.1013  -0.2695 -0.0493 25  ILE   H N   
13251 C  CA  . ILE   H  24  ? 1.3547 0.8866 1.4111 0.1241  -0.2636 -0.0698 25  ILE   H CA  
13252 C  C   . ILE   H  24  ? 1.3428 0.8084 1.4918 0.1391  -0.2599 -0.0719 25  ILE   H C   
13253 O  O   . ILE   H  24  ? 1.3502 0.6935 1.5205 0.0871  -0.2687 -0.1165 25  ILE   H O   
13254 C  CB  . ILE   H  24  ? 1.3809 0.9566 1.4140 0.1539  -0.2733 -0.0608 25  ILE   H CB  
13255 C  CG1 . ILE   H  24  ? 1.3525 0.9852 1.4073 0.1383  -0.3018 -0.0736 25  ILE   H CG1 
13256 C  CG2 . ILE   H  24  ? 1.3917 0.9557 1.4064 0.1477  -0.2834 -0.0606 25  ILE   H CG2 
13257 C  CD1 . ILE   H  24  ? 1.3523 1.0224 1.4194 0.1532  -0.3126 -0.0662 25  ILE   H CD1 
13258 N  N   . VAL   H  25  ? 1.3515 0.7898 1.5582 0.1176  -0.2744 -0.0718 26  VAL   H N   
13259 C  CA  . VAL   H  25  ? 1.3823 0.7973 1.5901 0.1217  -0.2722 -0.0919 26  VAL   H CA  
13260 C  C   . VAL   H  25  ? 1.4681 0.8662 1.5661 0.0713  -0.2241 -0.0736 26  VAL   H C   
13261 O  O   . VAL   H  25  ? 1.4496 0.8535 1.6079 0.1395  -0.2084 -0.1194 26  VAL   H O   
13262 C  CB  . VAL   H  25  ? 1.3608 0.8342 1.6548 0.0983  -0.2825 -0.0876 26  VAL   H CB  
13263 C  CG1 . VAL   H  25  ? 1.3708 0.7777 1.6777 0.1072  -0.2757 -0.0710 26  VAL   H CG1 
13264 C  CG2 . VAL   H  25  ? 1.3403 0.8576 1.6905 0.0655  -0.2796 -0.0688 26  VAL   H CG2 
13265 N  N   . ALA   H  26  ? 1.5217 0.8602 1.5750 0.0772  -0.2272 -0.0926 27  ALA   H N   
13266 C  CA  . ALA   H  26  ? 1.5334 0.8687 1.5471 0.0653  -0.2070 -0.0910 27  ALA   H CA  
13267 C  C   . ALA   H  26  ? 1.6028 0.8307 1.5425 -0.0018 -0.1660 -0.0752 27  ALA   H C   
13268 O  O   . ALA   H  26  ? 1.6333 0.8534 1.5163 -0.0069 -0.1167 -0.1485 27  ALA   H O   
13269 C  CB  . ALA   H  26  ? 1.5529 0.8897 1.5413 0.0950  -0.2006 -0.0790 27  ALA   H CB  
13270 N  N   . ASP   H  27  ? 1.6195 0.7826 1.5699 -0.0687 -0.2022 -0.1046 28  ASP   H N   
13271 C  CA  . ASP   H  27  ? 1.6297 0.8481 1.5853 -0.0824 -0.2185 -0.1195 28  ASP   H CA  
13272 C  C   . ASP   H  27  ? 1.6176 0.7781 1.5308 -0.0694 -0.1672 -0.1396 28  ASP   H C   
13273 O  O   . ASP   H  27  ? 1.5928 0.7459 1.4591 -0.0495 -0.1981 -0.1817 28  ASP   H O   
13274 C  CB  . ASP   H  27  ? 1.6892 0.9246 1.6250 -0.0959 -0.2201 -0.2102 28  ASP   H CB  
13275 C  CG  . ASP   H  27  ? 1.6577 1.1410 1.7001 -0.1877 -0.2566 -0.2114 28  ASP   H CG  
13276 O  OD1 . ASP   H  27  ? 1.7376 1.0866 1.7193 -0.2729 -0.2977 -0.2176 28  ASP   H OD1 
13277 O  OD2 . ASP   H  27  ? 1.5989 1.1840 1.6590 -0.2577 -0.2662 -0.2765 28  ASP   H OD2 
13278 N  N   . LYS   H  28  ? 1.6319 0.8131 1.5144 -0.0501 -0.1471 -0.1293 29  LYS   H N   
13279 C  CA  . LYS   H  28  ? 1.6018 0.7772 1.5096 -0.0532 -0.1344 -0.1426 29  LYS   H CA  
13280 C  C   . LYS   H  28  ? 1.6597 0.6919 1.5724 -0.1061 -0.1541 -0.1432 29  LYS   H C   
13281 O  O   . LYS   H  28  ? 1.7211 0.5360 1.6090 -0.0805 -0.1816 -0.1724 29  LYS   H O   
13282 C  CB  . LYS   H  28  ? 1.5849 0.8023 1.5362 -0.0093 -0.1376 -0.1110 29  LYS   H CB  
13283 C  CG  . LYS   H  28  ? 1.5568 0.7842 1.5515 0.0185  -0.1022 -0.1203 29  LYS   H CG  
13284 C  CD  . LYS   H  28  ? 1.5875 0.8183 1.5609 0.0145  -0.0737 -0.1665 29  LYS   H CD  
13285 C  CE  . LYS   H  28  ? 1.6099 0.8630 1.5531 0.0483  -0.0368 -0.1692 29  LYS   H CE  
13286 N  NZ  . LYS   H  28  ? 1.6358 0.9471 1.5675 0.0317  0.0003  -0.2037 29  LYS   H NZ  
13287 N  N   . ASN   H  29  ? 1.6217 0.7014 1.5528 -0.1386 -0.1744 -0.1037 30  ASN   H N   
13288 C  CA  . ASN   H  29  ? 1.5665 0.6635 1.5303 -0.1227 -0.1930 -0.0681 30  ASN   H CA  
13289 C  C   . ASN   H  29  ? 1.5614 0.6856 1.5191 -0.1123 -0.2034 -0.0572 30  ASN   H C   
13290 O  O   . ASN   H  29  ? 1.5772 0.6584 1.6145 -0.1406 -0.2087 -0.0575 30  ASN   H O   
13291 C  CB  . ASN   H  29  ? 1.5447 0.5973 1.4789 -0.0995 -0.2348 -0.1189 30  ASN   H CB  
13292 C  CG  . ASN   H  29  ? 1.4804 0.4868 1.5342 -0.1026 -0.2312 -0.1355 30  ASN   H CG  
13293 O  OD1 . ASN   H  29  ? 1.4088 0.3710 1.5866 -0.1429 -0.1986 -0.2381 30  ASN   H OD1 
13294 N  ND2 . ASN   H  29  ? 1.5151 0.4832 1.4986 -0.0904 -0.2317 -0.1192 30  ASN   H ND2 
13295 N  N   . CYS   H  30  ? 1.5838 0.6226 1.4135 -0.1423 -0.2144 0.0001  31  CYS   H N   
13296 C  CA  . CYS   H  30  ? 1.6536 0.5673 1.5084 -0.1532 -0.2056 -0.0549 31  CYS   H CA  
13297 C  C   . CYS   H  30  ? 1.6541 0.5868 1.5297 -0.1828 -0.2195 -0.0672 31  CYS   H C   
13298 O  O   . CYS   H  30  ? 1.6878 0.4323 1.7524 -0.1254 -0.2858 -0.0734 31  CYS   H O   
13299 C  CB  . CYS   H  30  ? 1.7074 0.7175 1.4974 -0.1113 -0.2575 -0.1302 31  CYS   H CB  
13300 S  SG  . CYS   H  30  ? 1.7819 0.8665 1.4219 -0.1351 -0.2543 -0.1276 31  CYS   H SG  
13301 N  N   . ALA   H  31  ? 1.6846 0.5993 1.6300 -0.1648 -0.1617 -0.0762 32  ALA   H N   
13302 C  CA  . ALA   H  31  ? 1.6618 0.6603 1.6427 -0.1217 -0.1575 -0.0987 32  ALA   H CA  
13303 C  C   . ALA   H  31  ? 1.6510 0.6199 1.5557 -0.0831 -0.1648 -0.0727 32  ALA   H C   
13304 O  O   . ALA   H  31  ? 1.5595 0.6799 1.6776 -0.0209 -0.1567 -0.0892 32  ALA   H O   
13305 C  CB  . ALA   H  31  ? 1.6976 0.6585 1.6801 -0.1186 -0.1386 -0.1377 32  ALA   H CB  
13306 N  N   . LYS   H  32  ? 1.6842 0.5809 1.4921 -0.0687 -0.2144 -0.0898 33  LYS   H N   
13307 C  CA  . LYS   H  32  ? 1.6850 0.5924 1.4124 -0.0264 -0.2480 -0.0722 33  LYS   H CA  
13308 C  C   . LYS   H  32  ? 1.7567 0.4637 1.4296 -0.0097 -0.3058 -0.0471 33  LYS   H C   
13309 O  O   . LYS   H  32  ? 1.7370 0.3444 1.4124 0.0140  -0.3304 -0.0411 33  LYS   H O   
13310 C  CB  . LYS   H  32  ? 1.7119 0.5937 1.4037 0.0008  -0.2661 -0.0466 33  LYS   H CB  
13311 C  CG  . LYS   H  32  ? 1.6886 0.6535 1.4070 0.0289  -0.2698 -0.0625 33  LYS   H CG  
13312 C  CD  . LYS   H  32  ? 1.6853 0.6605 1.4120 -0.0011 -0.2922 -0.0782 33  LYS   H CD  
13313 C  CE  . LYS   H  32  ? 1.6741 0.6790 1.4561 0.0239  -0.2700 -0.1050 33  LYS   H CE  
13314 N  NZ  . LYS   H  32  ? 1.6826 0.6951 1.5057 0.0231  -0.2592 -0.0742 33  LYS   H NZ  
13315 N  N   . LEU   H  33  ? 1.7674 0.5169 1.4548 -0.0214 -0.3360 -0.0401 34  LEU   H N   
13316 C  CA  . LEU   H  33  ? 1.7645 0.5583 1.4653 0.0018  -0.3875 -0.0647 34  LEU   H CA  
13317 C  C   . LEU   H  33  ? 1.8067 0.5117 1.4604 0.0491  -0.3147 -0.1275 34  LEU   H C   
13318 O  O   . LEU   H  33  ? 1.8878 0.2761 1.4910 0.0542  -0.2796 -0.1531 34  LEU   H O   
13319 C  CB  . LEU   H  33  ? 1.7750 0.5993 1.4731 -0.0161 -0.4181 -0.1116 34  LEU   H CB  
13320 C  CG  . LEU   H  33  ? 1.7160 0.5513 1.4666 -0.0090 -0.4505 -0.1371 34  LEU   H CG  
13321 C  CD1 . LEU   H  33  ? 1.6885 0.5334 1.4842 0.0011  -0.4535 -0.0938 34  LEU   H CD1 
13322 C  CD2 . LEU   H  33  ? 1.7269 0.5372 1.4819 0.0297  -0.4463 -0.1424 34  LEU   H CD2 
13323 N  N   . HIS   H  34  ? 1.7964 0.6451 1.4331 0.0788  -0.3030 -0.1207 35  HIS   H N   
13324 C  CA  . HIS   H  34  ? 1.7626 0.7240 1.4532 0.1283  -0.2919 -0.0501 35  HIS   H CA  
13325 C  C   . HIS   H  34  ? 1.6709 0.6836 1.4155 0.0672  -0.3160 -0.0075 35  HIS   H C   
13326 O  O   . HIS   H  34  ? 1.7349 0.5909 1.4480 0.1438  -0.3003 0.0439  35  HIS   H O   
13327 C  CB  . HIS   H  34  ? 1.7602 0.8419 1.5217 0.1657  -0.2905 -0.0837 35  HIS   H CB  
13328 C  CG  . HIS   H  34  ? 1.8532 0.8557 1.4914 0.1896  -0.2869 -0.0918 35  HIS   H CG  
13329 N  ND1 . HIS   H  34  ? 1.8992 0.9290 1.4926 0.2039  -0.2758 -0.0171 35  HIS   H ND1 
13330 C  CD2 . HIS   H  34  ? 1.8901 0.8343 1.5461 0.2544  -0.2718 -0.0242 35  HIS   H CD2 
13331 C  CE1 . HIS   H  34  ? 1.9268 0.8725 1.5012 0.2997  -0.2460 -0.0324 35  HIS   H CE1 
13332 N  NE2 . HIS   H  34  ? 1.9187 0.9421 1.4881 0.3053  -0.2535 -0.0116 35  HIS   H NE2 
13333 N  N   . ARG   H  35  ? 1.5957 0.7453 1.4132 0.0007  -0.3065 0.0214  36  ARG   H N   
13334 C  CA  . ARG   H  35  ? 1.5007 0.7517 1.3370 0.0648  -0.2782 0.0495  36  ARG   H CA  
13335 C  C   . ARG   H  35  ? 1.4830 0.6525 1.2665 0.0453  -0.2192 0.0744  36  ARG   H C   
13336 O  O   . ARG   H  35  ? 1.3945 0.6636 1.2558 0.1305  -0.1858 0.0555  36  ARG   H O   
13337 C  CB  . ARG   H  35  ? 1.5303 0.8590 1.3307 0.0026  -0.3127 0.0609  36  ARG   H CB  
13338 C  CG  . ARG   H  35  ? 1.5343 0.8933 1.3059 -0.0273 -0.3178 0.0475  36  ARG   H CG  
13339 C  CD  . ARG   H  35  ? 1.5610 1.0014 1.3025 -0.0621 -0.3046 0.1098  36  ARG   H CD  
13340 N  NE  . ARG   H  35  ? 1.5367 1.0480 1.3165 -0.0774 -0.3411 0.1304  36  ARG   H NE  
13341 C  CZ  . ARG   H  35  ? 1.6064 1.1692 1.2678 -0.0562 -0.3237 0.1527  36  ARG   H CZ  
13342 N  NH1 . ARG   H  35  ? 1.6044 1.2089 1.3707 -0.0347 -0.3039 0.1231  36  ARG   H NH1 
13343 N  NH2 . ARG   H  35  ? 1.6015 1.3377 1.2417 -0.0310 -0.3994 0.1092  36  ARG   H NH2 
13344 N  N   . ILE   H  36  ? 1.4171 0.5946 1.2438 0.0429  -0.2538 0.0892  37  ILE   H N   
13345 C  CA  . ILE   H  36  ? 1.3912 0.6968 1.2497 0.0485  -0.2194 0.0952  37  ILE   H CA  
13346 C  C   . ILE   H  36  ? 1.3987 0.7239 1.3159 0.0206  -0.1947 0.0769  37  ILE   H C   
13347 O  O   . ILE   H  36  ? 1.3801 0.7040 1.3215 0.0276  -0.1705 0.0602  37  ILE   H O   
13348 C  CB  . ILE   H  36  ? 1.4305 0.6701 1.1992 0.0235  -0.2477 0.1025  37  ILE   H CB  
13349 C  CG1 . ILE   H  36  ? 1.4563 0.6740 1.1539 0.0531  -0.2599 0.0844  37  ILE   H CG1 
13350 C  CG2 . ILE   H  36  ? 1.4094 0.7094 1.2130 0.0237  -0.2421 0.0932  37  ILE   H CG2 
13351 C  CD1 . ILE   H  36  ? 1.4563 0.7357 1.1262 0.0569  -0.2606 0.0869  37  ILE   H CD1 
13352 N  N   . SER   H  37  ? 1.3688 0.6936 1.3656 0.0383  -0.2021 0.1052  38  SER   H N   
13353 C  CA  . SER   H  37  ? 1.4087 0.6410 1.4286 0.0565  -0.1630 0.0836  38  SER   H CA  
13354 C  C   . SER   H  37  ? 1.3986 0.6374 1.4677 0.0475  -0.1648 0.0499  38  SER   H C   
13355 O  O   . SER   H  37  ? 1.4420 0.6080 1.5231 -0.0001 -0.1253 0.1150  38  SER   H O   
13356 C  CB  . SER   H  37  ? 1.4178 0.6214 1.4114 0.0588  -0.1579 0.1107  38  SER   H CB  
13357 O  OG  . SER   H  37  ? 1.4795 0.5386 1.4389 0.0601  -0.1275 0.1843  38  SER   H OG  
13358 N  N   . PRO   H  38  ? 1.3518 0.6811 1.5030 0.0645  -0.1857 0.0093  39  PRO   H N   
13359 C  CA  . PRO   H  38  ? 1.3537 0.7362 1.4900 0.0547  -0.1988 0.0038  39  PRO   H CA  
13360 C  C   . PRO   H  38  ? 1.3918 0.6883 1.4721 0.0013  -0.2065 -0.0236 39  PRO   H C   
13361 O  O   . PRO   H  38  ? 1.4375 0.5765 1.4249 -0.0421 -0.2184 -0.0595 39  PRO   H O   
13362 C  CB  . PRO   H  38  ? 1.3536 0.7238 1.5192 0.0999  -0.1955 -0.0183 39  PRO   H CB  
13363 C  CG  . PRO   H  38  ? 1.3334 0.7480 1.5523 0.1325  -0.1809 -0.0211 39  PRO   H CG  
13364 C  CD  . PRO   H  38  ? 1.3685 0.6997 1.5401 0.1045  -0.1768 0.0031  39  PRO   H CD  
13365 N  N   . LYS   H  39  ? 1.4067 0.7340 1.4547 -0.0350 -0.2090 -0.0064 40  LYS   H N   
13366 C  CA  . LYS   H  39  ? 1.4376 0.7641 1.4548 -0.0038 -0.2460 0.0006  40  LYS   H CA  
13367 C  C   . LYS   H  39  ? 1.4069 0.7552 1.3682 0.0190  -0.2738 -0.0113 40  LYS   H C   
13368 O  O   . LYS   H  39  ? 1.3801 0.7515 1.3567 0.0409  -0.2855 -0.0097 40  LYS   H O   
13369 C  CB  . LYS   H  39  ? 1.4642 0.7801 1.4582 -0.0077 -0.2641 -0.0038 40  LYS   H CB  
13370 C  CG  . LYS   H  39  ? 1.4343 0.8496 1.5136 0.0029  -0.2849 0.0114  40  LYS   H CG  
13371 C  CD  . LYS   H  39  ? 1.4684 0.9336 1.5320 -0.0097 -0.2996 0.0299  40  LYS   H CD  
13372 C  CE  . LYS   H  39  ? 1.5163 0.9534 1.6374 -0.0599 -0.2637 0.0169  40  LYS   H CE  
13373 N  NZ  . LYS   H  39  ? 1.4977 0.9958 1.6443 -0.1021 -0.3099 0.0120  40  LYS   H NZ  
13374 N  N   . ILE   H  40  ? 1.4167 0.7569 1.3426 0.0131  -0.2551 -0.0647 41  ILE   H N   
13375 C  CA  . ILE   H  40  ? 1.4513 0.7575 1.3517 -0.0189 -0.2210 -0.0182 41  ILE   H CA  
13376 C  C   . ILE   H  40  ? 1.4765 0.6435 1.4195 -0.0300 -0.2179 -0.0334 41  ILE   H C   
13377 O  O   . ILE   H  40  ? 1.5553 0.7655 1.4857 -0.0500 -0.2073 0.0476  41  ILE   H O   
13378 C  CB  . ILE   H  40  ? 1.4132 0.8075 1.3196 -0.0527 -0.2072 -0.0703 41  ILE   H CB  
13379 C  CG1 . ILE   H  40  ? 1.4734 0.8729 1.3376 -0.0925 -0.2028 -0.1100 41  ILE   H CG1 
13380 C  CG2 . ILE   H  40  ? 1.4041 0.7792 1.2904 -0.0342 -0.2269 -0.0603 41  ILE   H CG2 
13381 C  CD1 . ILE   H  40  ? 1.4617 0.8935 1.3321 -0.1117 -0.2119 -0.1300 41  ILE   H CD1 
13382 N  N   . TRP   H  41  ? 1.4674 0.6375 1.3446 -0.0454 -0.2664 -0.0146 42  TRP   H N   
13383 C  CA  . TRP   H  41  ? 1.4661 0.6613 1.3286 -0.0169 -0.2853 -0.0207 42  TRP   H CA  
13384 C  C   . TRP   H  41  ? 1.4971 0.5830 1.3020 0.0064  -0.3047 -0.1020 42  TRP   H C   
13385 O  O   . TRP   H  41  ? 1.5113 0.5503 1.3094 -0.0090 -0.2823 -0.1311 42  TRP   H O   
13386 C  CB  . TRP   H  41  ? 1.4510 0.6896 1.2931 -0.0377 -0.2565 -0.0226 42  TRP   H CB  
13387 C  CG  . TRP   H  41  ? 1.4793 0.6768 1.2828 -0.0367 -0.2348 -0.0023 42  TRP   H CG  
13388 C  CD1 . TRP   H  41  ? 1.4603 0.6753 1.3025 -0.0436 -0.2473 0.0052  42  TRP   H CD1 
13389 C  CD2 . TRP   H  41  ? 1.4896 0.6685 1.2628 -0.0564 -0.2409 -0.0166 42  TRP   H CD2 
13390 N  NE1 . TRP   H  41  ? 1.4368 0.7354 1.2847 -0.0398 -0.2446 0.0067  42  TRP   H NE1 
13391 C  CE2 . TRP   H  41  ? 1.4526 0.7048 1.2976 -0.0642 -0.2465 -0.0144 42  TRP   H CE2 
13392 C  CE3 . TRP   H  41  ? 1.4951 0.6833 1.2835 -0.0707 -0.2182 -0.0334 42  TRP   H CE3 
13393 C  CZ2 . TRP   H  41  ? 1.4347 0.7488 1.3189 -0.0680 -0.2243 -0.0718 42  TRP   H CZ2 
13394 C  CZ3 . TRP   H  41  ? 1.4690 0.7148 1.3422 -0.0804 -0.1949 -0.0539 42  TRP   H CZ3 
13395 C  CH2 . TRP   H  41  ? 1.4439 0.7294 1.3649 -0.0710 -0.2224 -0.0971 42  TRP   H CH2 
13396 N  N   . CYS   H  42  ? 1.5340 0.4817 1.3624 -0.0164 -0.2906 -0.1547 43  CYS   H N   
13397 C  CA  . CYS   H  42  ? 1.5442 0.5255 1.4289 -0.0428 -0.3179 -0.1358 43  CYS   H CA  
13398 C  C   . CYS   H  42  ? 1.5512 0.4617 1.4129 -0.0702 -0.3566 -0.1335 43  CYS   H C   
13399 O  O   . CYS   H  42  ? 1.5501 0.3299 1.4283 -0.1744 -0.3431 -0.2213 43  CYS   H O   
13400 C  CB  . CYS   H  42  ? 1.5777 0.5113 1.5151 0.0191  -0.2942 -0.1410 43  CYS   H CB  
13401 S  SG  . CYS   H  42  ? 1.6559 0.6705 1.6066 0.0000  -0.3857 -0.1777 43  CYS   H SG  
13402 N  N   . ALA   H  43  ? 1.5834 0.4659 1.4028 -0.0074 -0.4046 -0.0648 44  ALA   H N   
13403 C  CA  . ALA   H  43  ? 1.5925 0.4860 1.3902 0.0081  -0.3782 -0.0485 44  ALA   H CA  
13404 C  C   . ALA   H  43  ? 1.5966 0.3953 1.3252 -0.0043 -0.3625 -0.0118 44  ALA   H C   
13405 O  O   . ALA   H  43  ? 1.5937 0.2462 1.4108 -0.0608 -0.3463 -0.0146 44  ALA   H O   
13406 C  CB  . ALA   H  43  ? 1.6591 0.4957 1.4220 0.0221  -0.3804 -0.0151 44  ALA   H CB  
13407 N  N   . GLY   H  44  ? 1.5446 0.3929 1.3007 0.0220  -0.3733 0.0281  45  GLY   H N   
13408 C  CA  . GLY   H  44  ? 1.5187 0.5003 1.2392 0.0481  -0.3708 0.0949  45  GLY   H CA  
13409 C  C   . GLY   H  44  ? 1.4879 0.5163 1.1749 0.0625  -0.3545 0.1148  45  GLY   H C   
13410 O  O   . GLY   H  44  ? 1.4952 0.5795 1.0635 0.0806  -0.3675 0.2156  45  GLY   H O   
13411 N  N   . ALA   H  45  ? 1.4997 0.5295 1.1900 0.0472  -0.3670 0.0789  46  ALA   H N   
13412 C  CA  . ALA   H  45  ? 1.5279 0.5618 1.2214 0.1026  -0.3408 0.0195  46  ALA   H CA  
13413 C  C   . ALA   H  45  ? 1.5408 0.5983 1.2259 0.0616  -0.3554 -0.0160 46  ALA   H C   
13414 O  O   . ALA   H  45  ? 1.5100 0.6934 1.2160 0.0865  -0.3390 -0.0021 46  ALA   H O   
13415 C  CB  . ALA   H  45  ? 1.5179 0.5419 1.2264 0.0963  -0.3412 0.0093  46  ALA   H CB  
13416 N  N   . GLY   H  46  ? 1.5309 0.5486 1.2928 0.0761  -0.2708 -0.0555 47  GLY   H N   
13417 C  CA  . GLY   H  46  ? 1.5095 0.5178 1.3387 0.0715  -0.2663 -0.0725 47  GLY   H CA  
13418 C  C   . GLY   H  46  ? 1.5211 0.4420 1.3967 0.0808  -0.2336 -0.0518 47  GLY   H C   
13419 O  O   . GLY   H  46  ? 1.5178 0.3505 1.5122 0.1310  -0.2232 -0.0074 47  GLY   H O   
13420 N  N   . THR   H  47  ? 1.5088 0.4941 1.4137 0.0893  -0.2415 -0.0689 48  THR   H N   
13421 C  CA  . THR   H  47  ? 1.5142 0.5534 1.3944 0.0731  -0.2147 -0.0901 48  THR   H CA  
13422 C  C   . THR   H  47  ? 1.5244 0.5077 1.3908 0.0876  -0.1662 -0.1195 48  THR   H C   
13423 O  O   . THR   H  47  ? 1.4950 0.4504 1.3331 0.1123  -0.1332 -0.0427 48  THR   H O   
13424 C  CB  . THR   H  47  ? 1.5579 0.4951 1.4262 0.1112  -0.2283 -0.0940 48  THR   H CB  
13425 O  OG1 . THR   H  47  ? 1.6104 0.6610 1.4187 -0.0026 -0.2274 -0.1052 48  THR   H OG1 
13426 C  CG2 . THR   H  47  ? 1.5718 0.4124 1.4456 0.1800  -0.2457 -0.0676 48  THR   H CG2 
13427 N  N   . ALA   H  48  ? 1.5390 0.5712 1.4598 0.0666  -0.1320 -0.1356 49  ALA   H N   
13428 C  CA  . ALA   H  48  ? 1.4905 0.6880 1.4623 0.0598  -0.1243 -0.1287 49  ALA   H CA  
13429 C  C   . ALA   H  48  ? 1.4797 0.7428 1.4070 0.1213  -0.1514 -0.1071 49  ALA   H C   
13430 O  O   . ALA   H  48  ? 1.4763 0.8405 1.3555 0.1714  -0.1322 -0.1865 49  ALA   H O   
13431 C  CB  . ALA   H  48  ? 1.5089 0.6179 1.4674 0.0758  -0.1326 -0.1567 49  ALA   H CB  
13432 N  N   . ALA   H  49  ? 1.4678 0.8206 1.4215 0.1339  -0.1286 -0.0058 50  ALA   H N   
13433 C  CA  . ALA   H  49  ? 1.4940 0.7147 1.3349 0.0353  -0.1167 -0.0528 50  ALA   H CA  
13434 C  C   . ALA   H  49  ? 1.5535 0.6472 1.3360 0.0525  -0.1116 -0.0500 50  ALA   H C   
13435 O  O   . ALA   H  49  ? 1.5948 0.6833 1.3704 -0.0366 -0.0040 -0.0745 50  ALA   H O   
13436 C  CB  . ALA   H  49  ? 1.4687 0.7757 1.3411 0.0478  -0.1254 -0.0116 50  ALA   H CB  
13437 N  N   . ASP   H  50  ? 1.5692 0.5243 1.3053 0.0529  -0.1648 -0.0807 51  ASP   H N   
13438 C  CA  . ASP   H  50  ? 1.5518 0.4838 1.2892 0.0581  -0.1906 -0.0588 51  ASP   H CA  
13439 C  C   . ASP   H  50  ? 1.5778 0.4207 1.3140 0.0279  -0.2113 -0.0452 51  ASP   H C   
13440 O  O   . ASP   H  50  ? 1.6153 0.4169 1.3073 0.0411  -0.2112 -0.0369 51  ASP   H O   
13441 C  CB  . ASP   H  50  ? 1.5250 0.5298 1.2739 0.0346  -0.2332 -0.0692 51  ASP   H CB  
13442 C  CG  . ASP   H  50  ? 1.5600 0.5772 1.2641 0.0623  -0.2501 -0.0788 51  ASP   H CG  
13443 O  OD1 . ASP   H  50  ? 1.5544 0.5810 1.3348 0.0490  -0.2821 -0.0557 51  ASP   H OD1 
13444 O  OD2 . ASP   H  50  ? 1.6075 0.6827 1.2839 -0.0380 -0.2222 -0.1010 51  ASP   H OD2 
13445 N  N   . THR   H  51  ? 1.5319 0.4915 1.2909 0.0094  -0.2546 -0.0677 52  THR   H N   
13446 C  CA  . THR   H  51  ? 1.5731 0.5413 1.2667 -0.0297 -0.2305 -0.0954 52  THR   H CA  
13447 C  C   . THR   H  51  ? 1.5128 0.5339 1.3092 -0.0037 -0.2513 -0.0727 52  THR   H C   
13448 O  O   . THR   H  51  ? 1.5120 0.5584 1.3444 0.0106  -0.2455 -0.1008 52  THR   H O   
13449 C  CB  . THR   H  51  ? 1.6306 0.5054 1.2133 -0.0404 -0.2337 -0.0986 52  THR   H CB  
13450 O  OG1 . THR   H  51  ? 1.6734 0.5314 1.2515 -0.1016 -0.1774 -0.0891 52  THR   H OG1 
13451 C  CG2 . THR   H  51  ? 1.6469 0.4733 1.1840 -0.0306 -0.2583 -0.1282 52  THR   H CG2 
13452 N  N   . GLU   H  52  ? 1.4232 0.5818 1.3423 -0.0271 -0.2610 -0.0347 53  GLU   H N   
13453 C  CA  . GLU   H  52  ? 1.3633 0.6695 1.4095 -0.0692 -0.2577 -0.0108 53  GLU   H CA  
13454 C  C   . GLU   H  52  ? 1.3354 0.6492 1.3673 -0.0862 -0.2318 0.0007  53  GLU   H C   
13455 O  O   . GLU   H  52  ? 1.3747 0.6152 1.3623 -0.0246 -0.1886 -0.0084 53  GLU   H O   
13456 C  CB  . GLU   H  52  ? 1.3691 0.8493 1.4455 -0.0658 -0.2419 -0.0040 53  GLU   H CB  
13457 C  CG  . GLU   H  52  ? 1.3978 0.9305 1.5787 -0.0902 -0.2242 0.0710  53  GLU   H CG  
13458 C  CD  . GLU   H  52  ? 1.3967 1.0187 1.7119 -0.0836 -0.2535 0.0846  53  GLU   H CD  
13459 O  OE1 . GLU   H  52  ? 1.4607 1.1760 1.7580 0.0975  -0.2383 0.0782  53  GLU   H OE1 
13460 O  OE2 . GLU   H  52  ? 1.2085 1.1112 1.8481 -0.1949 -0.2508 0.1620  53  GLU   H OE2 
13461 N  N   . ALA   H  53  ? 1.3483 0.5407 1.3472 -0.0826 -0.2302 -0.0344 54  ALA   H N   
13462 C  CA  . ALA   H  53  ? 1.3877 0.5465 1.3212 -0.0543 -0.2156 -0.0444 54  ALA   H CA  
13463 C  C   . ALA   H  53  ? 1.4063 0.5614 1.3117 -0.0359 -0.2290 -0.0710 54  ALA   H C   
13464 O  O   . ALA   H  53  ? 1.3897 0.5974 1.2660 0.0294  -0.2047 -0.1811 54  ALA   H O   
13465 C  CB  . ALA   H  53  ? 1.3677 0.4989 1.3434 -0.0564 -0.2263 -0.0038 54  ALA   H CB  
13466 N  N   . VAL   H  54  ? 1.4145 0.5114 1.2702 -0.0235 -0.2200 -0.1096 55  VAL   H N   
13467 C  CA  . VAL   H  54  ? 1.4246 0.5038 1.2908 0.0200  -0.2218 -0.1228 55  VAL   H CA  
13468 C  C   . VAL   H  54  ? 1.4021 0.4623 1.3542 -0.0050 -0.2373 -0.0915 55  VAL   H C   
13469 O  O   . VAL   H  54  ? 1.3487 0.4823 1.3283 0.0002  -0.2559 -0.0919 55  VAL   H O   
13470 C  CB  . VAL   H  54  ? 1.4232 0.5665 1.2605 0.0157  -0.1957 -0.1133 55  VAL   H CB  
13471 C  CG1 . VAL   H  54  ? 1.4535 0.5736 1.2796 0.0172  -0.2076 -0.0915 55  VAL   H CG1 
13472 C  CG2 . VAL   H  54  ? 1.4223 0.6294 1.2767 0.0347  -0.1807 -0.1054 55  VAL   H CG2 
13473 N  N   . THR   H  55  ? 1.3897 0.4909 1.3682 -0.0208 -0.2891 -0.1212 56  THR   H N   
13474 C  CA  . THR   H  55  ? 1.4744 0.5998 1.3385 -0.0174 -0.3309 -0.1629 56  THR   H CA  
13475 C  C   . THR   H  55  ? 1.5160 0.6207 1.3254 0.0160  -0.2655 -0.1196 56  THR   H C   
13476 O  O   . THR   H  55  ? 1.5887 0.6886 1.3626 0.0109  -0.2477 -0.1716 56  THR   H O   
13477 C  CB  . THR   H  55  ? 1.4420 0.5954 1.3342 -0.0360 -0.4113 -0.1729 56  THR   H CB  
13478 O  OG1 . THR   H  55  ? 1.3992 0.5553 1.2751 -0.1098 -0.4686 -0.2292 56  THR   H OG1 
13479 C  CG2 . THR   H  55  ? 1.4101 0.6864 1.3887 -0.0382 -0.4258 -0.1420 56  THR   H CG2 
13480 N  N   . GLN   H  56  ? 1.5374 0.5980 1.3430 0.0281  -0.1978 -0.0973 57  GLN   H N   
13481 C  CA  . GLN   H  56  ? 1.5272 0.5986 1.3514 0.0481  -0.1457 -0.0855 57  GLN   H CA  
13482 C  C   . GLN   H  56  ? 1.4912 0.5025 1.2528 -0.0126 -0.1664 -0.1124 57  GLN   H C   
13483 O  O   . GLN   H  56  ? 1.5035 0.5270 1.2801 0.0226  -0.1379 -0.1904 57  GLN   H O   
13484 C  CB  . GLN   H  56  ? 1.5692 0.6444 1.3887 0.0764  -0.0537 -0.0198 57  GLN   H CB  
13485 C  CG  . GLN   H  56  ? 1.6007 0.6560 1.5120 0.1228  -0.0318 0.0188  57  GLN   H CG  
13486 C  CD  . GLN   H  56  ? 1.6619 0.7070 1.5662 0.1857  0.0694  0.0119  57  GLN   H CD  
13487 O  OE1 . GLN   H  56  ? 1.6893 0.6836 1.5983 0.2536  0.0396  0.0434  57  GLN   H OE1 
13488 N  NE2 . GLN   H  56  ? 1.6906 0.8068 1.6289 0.2667  0.0854  0.0252  57  GLN   H NE2 
13489 N  N   . LEU   H  57  ? 1.4568 0.4659 1.2089 0.0330  -0.1627 -0.0773 58  LEU   H N   
13490 C  CA  . LEU   H  57  ? 1.4615 0.4468 1.2212 0.0361  -0.1845 -0.0938 58  LEU   H CA  
13491 C  C   . LEU   H  57  ? 1.4639 0.5442 1.2168 0.0324  -0.2075 -0.0979 58  LEU   H C   
13492 O  O   . LEU   H  57  ? 1.4867 0.5688 1.3128 0.0940  -0.2248 -0.1170 58  LEU   H O   
13493 C  CB  . LEU   H  57  ? 1.4342 0.4164 1.1846 0.0634  -0.1854 -0.0664 58  LEU   H CB  
13494 C  CG  . LEU   H  57  ? 1.4512 0.4057 1.1822 0.0755  -0.1854 -0.0780 58  LEU   H CG  
13495 C  CD1 . LEU   H  57  ? 1.4493 0.4319 1.1743 0.0865  -0.1724 -0.0625 58  LEU   H CD1 
13496 C  CD2 . LEU   H  57  ? 1.4221 0.4210 1.1792 0.0930  -0.1859 -0.0769 58  LEU   H CD2 
13497 N  N   . ILE   H  58  ? 1.4368 0.4580 1.2280 0.0357  -0.2099 -0.1358 59  ILE   H N   
13498 C  CA  . ILE   H  58  ? 1.4432 0.4957 1.2328 0.0602  -0.1839 -0.1371 59  ILE   H CA  
13499 C  C   . ILE   H  58  ? 1.4391 0.5530 1.2756 0.0407  -0.1707 -0.1300 59  ILE   H C   
13500 O  O   . ILE   H  58  ? 1.4592 0.6113 1.2631 0.0154  -0.1652 -0.1627 59  ILE   H O   
13501 C  CB  . ILE   H  58  ? 1.4150 0.4857 1.2189 0.0788  -0.2158 -0.1383 59  ILE   H CB  
13502 C  CG1 . ILE   H  58  ? 1.4014 0.5363 1.2123 0.0999  -0.2104 -0.1285 59  ILE   H CG1 
13503 C  CG2 . ILE   H  58  ? 1.4249 0.4689 1.2236 0.0739  -0.2243 -0.1407 59  ILE   H CG2 
13504 C  CD1 . ILE   H  58  ? 1.4024 0.6277 1.1895 0.1176  -0.1891 -0.1257 59  ILE   H CD1 
13505 N  N   . GLY   H  59  ? 1.4573 0.5718 1.3191 0.0444  -0.1440 -0.1263 60  GLY   H N   
13506 C  CA  . GLY   H  59  ? 1.4721 0.6034 1.3427 0.0294  -0.1463 -0.1573 60  GLY   H CA  
13507 C  C   . GLY   H  59  ? 1.4744 0.5722 1.3259 0.0199  -0.1402 -0.2167 60  GLY   H C   
13508 O  O   . GLY   H  59  ? 1.5044 0.5278 1.4015 0.0174  -0.0448 -0.2882 60  GLY   H O   
13509 N  N   . SER   H  60  ? 1.4664 0.4987 1.3494 0.0550  -0.1426 -0.1853 61  SER   H N   
13510 C  CA  . SER   H  60  ? 1.4762 0.4545 1.3788 0.0275  -0.1623 -0.2127 61  SER   H CA  
13511 C  C   . SER   H  60  ? 1.4795 0.4684 1.3414 0.0347  -0.1497 -0.1663 61  SER   H C   
13512 O  O   . SER   H  60  ? 1.4293 0.5228 1.3875 0.0046  -0.1618 -0.2075 61  SER   H O   
13513 C  CB  . SER   H  60  ? 1.4709 0.4088 1.3795 0.0519  -0.1606 -0.2040 61  SER   H CB  
13514 O  OG  . SER   H  60  ? 1.4889 0.3784 1.4103 -0.0139 -0.1949 -0.1878 61  SER   H OG  
13515 N  N   . ASN   H  61  ? 1.5026 0.4375 1.2984 0.0384  -0.1471 -0.1307 62  ASN   H N   
13516 C  CA  . ASN   H  61  ? 1.5207 0.4437 1.3103 0.0429  -0.1281 -0.1235 62  ASN   H CA  
13517 C  C   . ASN   H  61  ? 1.5479 0.4264 1.3104 0.0581  -0.1384 -0.1003 62  ASN   H C   
13518 O  O   . ASN   H  61  ? 1.6312 0.4817 1.2994 0.0030  -0.0714 -0.1474 62  ASN   H O   
13519 C  CB  . ASN   H  61  ? 1.5151 0.4861 1.3111 0.0341  -0.1249 -0.1387 62  ASN   H CB  
13520 C  CG  . ASN   H  61  ? 1.5180 0.5667 1.3308 0.0359  -0.1300 -0.1448 62  ASN   H CG  
13521 O  OD1 . ASN   H  61  ? 1.5364 0.5691 1.3798 -0.0297 -0.0806 -0.1263 62  ASN   H OD1 
13522 N  ND2 . ASN   H  61  ? 1.5231 0.5988 1.4079 0.0165  -0.1172 -0.1749 62  ASN   H ND2 
13523 N  N   . ILE   H  62  ? 1.5411 0.5037 1.2993 0.0705  -0.1799 -0.0984 63  ILE   H N   
13524 C  CA  . ILE   H  62  ? 1.5461 0.5189 1.3026 0.0295  -0.1852 -0.1312 63  ILE   H CA  
13525 C  C   . ILE   H  62  ? 1.5229 0.4596 1.2955 0.0702  -0.1973 -0.1429 63  ILE   H C   
13526 O  O   . ILE   H  62  ? 1.5056 0.4988 1.2859 0.1341  -0.1844 -0.1514 63  ILE   H O   
13527 C  CB  . ILE   H  62  ? 1.5433 0.5684 1.2601 0.0358  -0.2309 -0.0930 63  ILE   H CB  
13528 C  CG1 . ILE   H  62  ? 1.5749 0.5645 1.2394 0.0300  -0.2205 -0.0948 63  ILE   H CG1 
13529 C  CG2 . ILE   H  62  ? 1.5520 0.5776 1.2576 0.0307  -0.2400 -0.1072 63  ILE   H CG2 
13530 C  CD1 . ILE   H  62  ? 1.5809 0.5607 1.2329 0.0165  -0.2275 -0.1106 63  ILE   H CD1 
13531 N  N   . GLU   H  63  ? 1.5149 0.4631 1.2765 0.0464  -0.2137 -0.1468 64  GLU   H N   
13532 C  CA  . GLU   H  63  ? 1.4943 0.5477 1.3168 0.0098  -0.2167 -0.1301 64  GLU   H CA  
13533 C  C   . GLU   H  63  ? 1.4723 0.5226 1.2812 -0.0222 -0.2119 -0.1460 64  GLU   H C   
13534 O  O   . GLU   H  63  ? 1.4495 0.5042 1.2722 0.0024  -0.1951 -0.1570 64  GLU   H O   
13535 C  CB  . GLU   H  63  ? 1.5094 0.6033 1.3557 0.0027  -0.1846 -0.1304 64  GLU   H CB  
13536 C  CG  . GLU   H  63  ? 1.5579 0.6463 1.5003 -0.0372 -0.1846 -0.1028 64  GLU   H CG  
13537 C  CD  . GLU   H  63  ? 1.6071 0.7721 1.5821 -0.0415 -0.1283 -0.1316 64  GLU   H CD  
13538 O  OE1 . GLU   H  63  ? 1.6984 0.8588 1.7353 -0.0459 -0.0547 -0.0469 64  GLU   H OE1 
13539 O  OE2 . GLU   H  63  ? 1.6484 0.6981 1.6595 -0.1047 -0.1655 -0.0988 64  GLU   H OE2 
13540 N  N   . LEU   H  64  ? 1.4659 0.5250 1.2965 -0.0141 -0.2037 -0.1245 65  LEU   H N   
13541 C  CA  . LEU   H  64  ? 1.4898 0.4965 1.3114 -0.0229 -0.2072 -0.1529 65  LEU   H CA  
13542 C  C   . LEU   H  64  ? 1.5019 0.5394 1.2916 -0.0257 -0.2160 -0.1148 65  LEU   H C   
13543 O  O   . LEU   H  64  ? 1.5349 0.6520 1.2312 -0.0741 -0.2836 -0.2300 65  LEU   H O   
13544 C  CB  . LEU   H  64  ? 1.4755 0.4659 1.3016 -0.0483 -0.1927 -0.1630 65  LEU   H CB  
13545 C  CG  . LEU   H  64  ? 1.4548 0.5194 1.2944 -0.0726 -0.2066 -0.1290 65  LEU   H CG  
13546 C  CD1 . LEU   H  64  ? 1.4569 0.5677 1.2915 -0.0755 -0.2098 -0.0816 65  LEU   H CD1 
13547 C  CD2 . LEU   H  64  ? 1.4582 0.5264 1.3004 -0.0675 -0.1867 -0.1217 65  LEU   H CD2 
13548 N  N   . HIS   H  65  ? 1.4960 0.4849 1.2963 0.0051  -0.1985 -0.1395 66  HIS   H N   
13549 C  CA  . HIS   H  65  ? 1.4810 0.5366 1.3200 0.0280  -0.1798 -0.1794 66  HIS   H CA  
13550 C  C   . HIS   H  65  ? 1.4889 0.4461 1.3380 -0.0149 -0.1701 -0.1667 66  HIS   H C   
13551 O  O   . HIS   H  65  ? 1.4813 0.4712 1.3098 -0.0232 -0.1347 -0.1568 66  HIS   H O   
13552 C  CB  . HIS   H  65  ? 1.4723 0.5498 1.3339 0.0415  -0.1539 -0.1740 66  HIS   H CB  
13553 C  CG  . HIS   H  65  ? 1.4709 0.5850 1.3411 0.1344  -0.1457 -0.2119 66  HIS   H CG  
13554 N  ND1 . HIS   H  65  ? 1.4485 0.5375 1.3727 0.1719  -0.1676 -0.2266 66  HIS   H ND1 
13555 C  CD2 . HIS   H  65  ? 1.4985 0.6164 1.3683 0.1834  -0.1321 -0.2470 66  HIS   H CD2 
13556 C  CE1 . HIS   H  65  ? 1.4748 0.5078 1.3823 0.1907  -0.1514 -0.2443 66  HIS   H CE1 
13557 N  NE2 . HIS   H  65  ? 1.4769 0.5679 1.3746 0.2185  -0.1299 -0.2345 66  HIS   H NE2 
13558 N  N   . SER   H  66  ? 1.4507 0.4591 1.3577 -0.0408 -0.2307 -0.1341 67  SER   H N   
13559 C  CA  . SER   H  66  ? 1.4830 0.5454 1.3501 -0.0232 -0.2743 -0.1108 67  SER   H CA  
13560 C  C   . SER   H  66  ? 1.5139 0.5388 1.3376 0.0005  -0.2515 -0.1139 67  SER   H C   
13561 O  O   . SER   H  66  ? 1.5484 0.5565 1.3456 0.0023  -0.2367 -0.1337 67  SER   H O   
13562 C  CB  . SER   H  66  ? 1.4594 0.5224 1.3462 -0.0092 -0.3419 -0.0963 67  SER   H CB  
13563 O  OG  . SER   H  66  ? 1.4848 0.5857 1.3740 0.0392  -0.4005 -0.0446 67  SER   H OG  
13564 N  N   . LEU   H  67  ? 1.5022 0.5087 1.3785 -0.0010 -0.2303 -0.0650 68  LEU   H N   
13565 C  CA  . LEU   H  67  ? 1.4852 0.5131 1.3756 -0.0337 -0.2105 -0.0681 68  LEU   H CA  
13566 C  C   . LEU   H  67  ? 1.5314 0.4090 1.3370 -0.0647 -0.1957 -0.0743 68  LEU   H C   
13567 O  O   . LEU   H  67  ? 1.5051 0.4088 1.3648 -0.0383 -0.1850 -0.0973 68  LEU   H O   
13568 C  CB  . LEU   H  67  ? 1.4597 0.5350 1.3930 -0.0146 -0.1569 -0.0234 68  LEU   H CB  
13569 C  CG  . LEU   H  67  ? 1.4506 0.5803 1.4361 0.0183  -0.1498 -0.0134 68  LEU   H CG  
13570 C  CD1 . LEU   H  67  ? 1.4522 0.5954 1.4032 0.0060  -0.1712 -0.0250 68  LEU   H CD1 
13571 C  CD2 . LEU   H  67  ? 1.4435 0.6135 1.4239 0.0337  -0.1212 0.0069  68  LEU   H CD2 
13572 N  N   . TYR   H  68  ? 1.5730 0.3485 1.3125 -0.1055 -0.1658 -0.0602 69  TYR   H N   
13573 C  CA  . TYR   H  68  ? 1.6202 0.2938 1.2771 -0.1231 -0.1438 -0.0990 69  TYR   H CA  
13574 C  C   . TYR   H  68  ? 1.6274 0.3328 1.2670 -0.1259 -0.1894 -0.0744 69  TYR   H C   
13575 O  O   . TYR   H  68  ? 1.6619 0.3433 1.2056 -0.0423 -0.1695 -0.0067 69  TYR   H O   
13576 C  CB  . TYR   H  68  ? 1.6720 0.2439 1.2994 -0.1699 -0.1078 -0.0949 69  TYR   H CB  
13577 C  CG  . TYR   H  68  ? 1.7387 0.2554 1.3028 -0.1883 -0.0508 -0.1540 69  TYR   H CG  
13578 C  CD1 . TYR   H  68  ? 1.7854 0.2616 1.2984 -0.2117 -0.0381 -0.1708 69  TYR   H CD1 
13579 C  CD2 . TYR   H  68  ? 1.7828 0.2624 1.3000 -0.1779 -0.0614 -0.1717 69  TYR   H CD2 
13580 C  CE1 . TYR   H  68  ? 1.8000 0.2756 1.3298 -0.2402 0.0003  -0.2009 69  TYR   H CE1 
13581 C  CE2 . TYR   H  68  ? 1.8134 0.2796 1.3371 -0.2130 -0.0073 -0.2042 69  TYR   H CE2 
13582 C  CZ  . TYR   H  68  ? 1.8227 0.2849 1.3446 -0.2499 0.0064  -0.2096 69  TYR   H CZ  
13583 O  OH  . TYR   H  68  ? 1.9157 0.3316 1.5124 -0.3237 0.1507  -0.3054 69  TYR   H OH  
13584 N  N   . THR   H  69  ? 1.5937 0.3236 1.2470 -0.0927 -0.2195 -0.1182 70  THR   H N   
13585 C  CA  . THR   H  69  ? 1.5821 0.3777 1.2498 -0.0727 -0.2205 -0.1166 70  THR   H CA  
13586 C  C   . THR   H  69  ? 1.5826 0.4180 1.2378 -0.0543 -0.2294 -0.1317 70  THR   H C   
13587 O  O   . THR   H  69  ? 1.5842 0.4163 1.2328 -0.0207 -0.2499 -0.1147 70  THR   H O   
13588 C  CB  . THR   H  69  ? 1.5705 0.4155 1.2187 -0.0741 -0.2450 -0.0573 70  THR   H CB  
13589 O  OG1 . THR   H  69  ? 1.5028 0.4543 1.2458 -0.0646 -0.2792 -0.0044 70  THR   H OG1 
13590 C  CG2 . THR   H  69  ? 1.5367 0.4421 1.2005 -0.0457 -0.2298 -0.0344 70  THR   H CG2 
13591 N  N   . SER   H  70  ? 1.5557 0.4604 1.2997 -0.0845 -0.2252 -0.1536 71  SER   H N   
13592 C  CA  . SER   H  70  ? 1.5777 0.5111 1.3069 -0.1344 -0.2322 -0.1669 71  SER   H CA  
13593 C  C   . SER   H  70  ? 1.5742 0.4881 1.2865 -0.1479 -0.2287 -0.1813 71  SER   H C   
13594 O  O   . SER   H  70  ? 1.5634 0.3435 1.2997 -0.2356 -0.1971 -0.1749 71  SER   H O   
13595 C  CB  . SER   H  70  ? 1.5890 0.5171 1.3188 -0.1456 -0.2438 -0.1720 71  SER   H CB  
13596 O  OG  . SER   H  70  ? 1.6182 0.5762 1.3178 -0.1687 -0.2360 -0.1196 71  SER   H OG  
13597 N  N   . ARG   H  71  ? 1.6035 0.4705 1.3377 -0.1198 -0.2223 -0.1726 72  ARG   H N   
13598 C  CA  . ARG   H  71  ? 1.6111 0.5778 1.3267 -0.0694 -0.2474 -0.1294 72  ARG   H CA  
13599 C  C   . ARG   H  71  ? 1.6695 0.5897 1.3459 -0.0348 -0.2250 -0.1198 72  ARG   H C   
13600 O  O   . ARG   H  71  ? 1.6579 0.5334 1.3174 0.0525  -0.1649 -0.1684 72  ARG   H O   
13601 C  CB  . ARG   H  71  ? 1.6021 0.5759 1.2814 -0.0643 -0.2602 -0.1239 72  ARG   H CB  
13602 C  CG  . ARG   H  71  ? 1.5944 0.5312 1.2908 -0.0846 -0.2918 -0.1440 72  ARG   H CG  
13603 C  CD  . ARG   H  71  ? 1.5968 0.5385 1.2902 -0.0921 -0.2995 -0.1320 72  ARG   H CD  
13604 N  NE  . ARG   H  71  ? 1.6251 0.5995 1.3046 -0.1108 -0.3068 -0.1565 72  ARG   H NE  
13605 C  CZ  . ARG   H  71  ? 1.6654 0.6244 1.3814 -0.0747 -0.2936 -0.1817 72  ARG   H CZ  
13606 N  NH1 . ARG   H  71  ? 1.6682 0.6986 1.3904 -0.0555 -0.2794 -0.1512 72  ARG   H NH1 
13607 N  NH2 . ARG   H  71  ? 1.7099 0.6961 1.3812 -0.0888 -0.3050 -0.2029 72  ARG   H NH2 
13608 N  N   . GLU   H  72  ? 1.7207 0.6198 1.2989 -0.0693 -0.2790 -0.0958 73  GLU   H N   
13609 C  CA  . GLU   H  72  ? 1.7117 0.5782 1.3049 -0.0707 -0.2914 -0.0518 73  GLU   H CA  
13610 C  C   . GLU   H  72  ? 1.7132 0.5367 1.2599 -0.0599 -0.3281 -0.0511 73  GLU   H C   
13611 O  O   . GLU   H  72  ? 1.6775 0.4660 1.3258 -0.1357 -0.3222 0.0053  73  GLU   H O   
13612 C  CB  . GLU   H  72  ? 1.7672 0.6849 1.3342 -0.0430 -0.3244 -0.0304 73  GLU   H CB  
13613 C  CG  . GLU   H  72  ? 1.8775 0.7753 1.4369 -0.1340 -0.2975 0.0032  73  GLU   H CG  
13614 C  CD  . GLU   H  72  ? 1.9358 0.9872 1.5337 -0.1036 -0.2297 0.0055  73  GLU   H CD  
13615 O  OE1 . GLU   H  72  ? 2.1374 1.0425 1.5692 -0.1818 -0.2336 0.1070  73  GLU   H OE1 
13616 O  OE2 . GLU   H  72  ? 2.1863 1.1445 1.5718 -0.1899 -0.2298 0.1552  73  GLU   H OE2 
13617 N  N   . PRO   H  73  ? 1.6568 0.5290 1.2683 -0.0753 -0.3360 -0.0589 74  PRO   H N   
13618 C  CA  . PRO   H  73  ? 1.7000 0.5188 1.2575 -0.0948 -0.3203 -0.1190 74  PRO   H CA  
13619 C  C   . PRO   H  73  ? 1.6753 0.4626 1.2194 -0.1768 -0.3170 -0.1713 74  PRO   H C   
13620 O  O   . PRO   H  73  ? 1.6639 0.4311 1.1941 -0.2285 -0.3915 -0.3002 74  PRO   H O   
13621 C  CB  . PRO   H  73  ? 1.6907 0.5517 1.2494 -0.0749 -0.3022 -0.0893 74  PRO   H CB  
13622 C  CG  . PRO   H  73  ? 1.6698 0.5662 1.2848 -0.0642 -0.3264 -0.0903 74  PRO   H CG  
13623 C  CD  . PRO   H  73  ? 1.6275 0.5675 1.2816 -0.0643 -0.3387 -0.0843 74  PRO   H CD  
13624 N  N   . ARG   H  74  ? 1.6753 0.4734 1.2545 -0.1834 -0.2995 -0.1729 75  ARG   H N   
13625 C  CA  . ARG   H  74  ? 1.6341 0.5499 1.2836 -0.1078 -0.2908 -0.0942 75  ARG   H CA  
13626 C  C   . ARG   H  74  ? 1.5982 0.5193 1.3526 -0.0605 -0.2835 -0.1086 75  ARG   H C   
13627 O  O   . ARG   H  74  ? 1.5782 0.4393 1.3884 0.0351  -0.2919 -0.1057 75  ARG   H O   
13628 C  CB  . ARG   H  74  ? 1.6561 0.4915 1.2168 -0.1355 -0.2855 -0.0340 75  ARG   H CB  
13629 C  CG  . ARG   H  74  ? 1.6713 0.4584 1.2483 -0.1346 -0.2764 -0.0206 75  ARG   H CG  
13630 C  CD  . ARG   H  74  ? 1.6772 0.4847 1.2442 -0.1264 -0.2718 0.0042  75  ARG   H CD  
13631 N  NE  . ARG   H  74  ? 1.6928 0.5403 1.2516 -0.1335 -0.2791 -0.0344 75  ARG   H NE  
13632 C  CZ  . ARG   H  74  ? 1.6570 0.5570 1.2523 -0.1602 -0.2798 -0.0252 75  ARG   H CZ  
13633 N  NH1 . ARG   H  74  ? 1.6775 0.5224 1.2612 -0.1486 -0.2772 0.0155  75  ARG   H NH1 
13634 N  NH2 . ARG   H  74  ? 1.6522 0.6576 1.2685 -0.1966 -0.3345 -0.0655 75  ARG   H NH2 
13635 N  N   . VAL   H  75  ? 1.5367 0.5505 1.3799 -0.0642 -0.3052 -0.0849 76  VAL   H N   
13636 C  CA  . VAL   H  75  ? 1.4826 0.5157 1.3772 -0.1159 -0.2848 -0.0376 76  VAL   H CA  
13637 C  C   . VAL   H  75  ? 1.4751 0.5069 1.3672 -0.1101 -0.2123 -0.0405 76  VAL   H C   
13638 O  O   . VAL   H  75  ? 1.4625 0.5288 1.4203 -0.1106 -0.2211 -0.0736 76  VAL   H O   
13639 C  CB  . VAL   H  75  ? 1.4997 0.5430 1.3570 -0.1398 -0.3030 0.0062  76  VAL   H CB  
13640 C  CG1 . VAL   H  75  ? 1.4842 0.5801 1.3181 -0.1529 -0.3288 -0.0093 76  VAL   H CG1 
13641 C  CG2 . VAL   H  75  ? 1.5026 0.5355 1.3848 -0.1389 -0.2858 0.0071  76  VAL   H CG2 
13642 N  N   . VAL   H  76  ? 1.5016 0.4682 1.2811 -0.1230 -0.2363 -0.0217 77  VAL   H N   
13643 C  CA  . VAL   H  76  ? 1.4955 0.5011 1.1537 -0.0803 -0.1942 -0.0466 77  VAL   H CA  
13644 C  C   . VAL   H  76  ? 1.4911 0.4721 1.2036 -0.0552 -0.2038 -0.0611 77  VAL   H C   
13645 O  O   . VAL   H  76  ? 1.5074 0.4296 1.2433 -0.0524 -0.2038 -0.1077 77  VAL   H O   
13646 C  CB  . VAL   H  76  ? 1.5127 0.4803 1.1190 -0.0818 -0.2230 -0.0549 77  VAL   H CB  
13647 C  CG1 . VAL   H  76  ? 1.5442 0.5621 1.1181 -0.0187 -0.2324 -0.0524 77  VAL   H CG1 
13648 C  CG2 . VAL   H  76  ? 1.4962 0.4994 1.0630 -0.1302 -0.2186 -0.0457 77  VAL   H CG2 
13649 N  N   . SER   H  77  ? 1.4716 0.4931 1.1771 -0.0680 -0.2075 -0.0578 78  SER   H N   
13650 C  CA  . SER   H  77  ? 1.4502 0.5866 1.1127 -0.0558 -0.2043 -0.0700 78  SER   H CA  
13651 C  C   . SER   H  77  ? 1.4207 0.5660 1.0927 -0.0596 -0.2216 -0.0560 78  SER   H C   
13652 O  O   . SER   H  77  ? 1.4195 0.5739 1.0275 -0.0644 -0.1973 -0.0824 78  SER   H O   
13653 C  CB  . SER   H  77  ? 1.4441 0.5793 1.1320 -0.0424 -0.2001 -0.0671 78  SER   H CB  
13654 O  OG  . SER   H  77  ? 1.4430 0.5555 1.1336 0.0288  -0.1757 -0.0443 78  SER   H OG  
13655 N  N   . ALA   H  78  ? 1.4316 0.5515 1.0283 -0.0537 -0.2297 -0.0722 79  ALA   H N   
13656 C  CA  . ALA   H  78  ? 1.4221 0.5796 0.9995 -0.0447 -0.2568 -0.0689 79  ALA   H CA  
13657 C  C   . ALA   H  78  ? 1.4501 0.5934 1.0015 -0.0606 -0.2568 -0.0737 79  ALA   H C   
13658 O  O   . ALA   H  78  ? 1.4361 0.6387 0.9678 -0.0753 -0.2564 -0.0228 79  ALA   H O   
13659 C  CB  . ALA   H  78  ? 1.4144 0.5580 0.9890 -0.0415 -0.2788 -0.0764 79  ALA   H CB  
13660 N  N   . LEU   H  79  ? 1.4922 0.6188 0.9545 -0.0442 -0.2903 -0.1090 80  LEU   H N   
13661 C  CA  . LEU   H  79  ? 1.5237 0.5869 0.9864 -0.0413 -0.3173 -0.1378 80  LEU   H CA  
13662 C  C   . LEU   H  79  ? 1.5304 0.5943 1.0605 0.0130  -0.2673 -0.1101 80  LEU   H C   
13663 O  O   . LEU   H  79  ? 1.4873 0.6483 1.0987 0.0054  -0.3116 -0.0907 80  LEU   H O   
13664 C  CB  . LEU   H  79  ? 1.5371 0.6351 0.9623 -0.0374 -0.3670 -0.1822 80  LEU   H CB  
13665 C  CG  . LEU   H  79  ? 1.5569 0.6487 0.9317 -0.0526 -0.3933 -0.1765 80  LEU   H CG  
13666 C  CD1 . LEU   H  79  ? 1.5742 0.6415 0.9777 -0.0259 -0.3979 -0.1585 80  LEU   H CD1 
13667 C  CD2 . LEU   H  79  ? 1.5746 0.6982 0.9416 -0.0648 -0.3786 -0.1520 80  LEU   H CD2 
13668 N  N   . GLN   H  80  ? 1.5378 0.5721 1.0998 0.0240  -0.2529 -0.0832 81  GLN   H N   
13669 C  CA  . GLN   H  80  ? 1.5391 0.5422 1.1531 0.0344  -0.2255 -0.0481 81  GLN   H CA  
13670 C  C   . GLN   H  80  ? 1.5371 0.5223 1.1409 0.0009  -0.2393 -0.0941 81  GLN   H C   
13671 O  O   . GLN   H  80  ? 1.5369 0.4093 1.2304 -0.0398 -0.2160 -0.0557 81  GLN   H O   
13672 C  CB  . GLN   H  80  ? 1.5413 0.5475 1.1813 0.0842  -0.1637 -0.0221 81  GLN   H CB  
13673 C  CG  . GLN   H  80  ? 1.5564 0.5738 1.1801 0.0957  -0.1077 0.0254  81  GLN   H CG  
13674 C  CD  . GLN   H  80  ? 1.5784 0.5698 1.1944 0.1381  -0.0945 0.0540  81  GLN   H CD  
13675 O  OE1 . GLN   H  80  ? 1.5237 0.6643 1.2047 0.2315  -0.0620 0.0421  81  GLN   H OE1 
13676 N  NE2 . GLN   H  80  ? 1.5922 0.5192 1.1720 0.1577  -0.1013 0.0706  81  GLN   H NE2 
13677 N  N   . MET   H  81  ? 1.5551 0.5885 1.1564 -0.0401 -0.2318 -0.1058 82  MET   H N   
13678 C  CA  . MET   H  81  ? 1.5846 0.6272 1.1761 -0.0094 -0.2835 -0.0994 82  MET   H CA  
13679 C  C   . MET   H  81  ? 1.5481 0.5985 1.2011 0.0457  -0.2933 -0.0895 82  MET   H C   
13680 O  O   . MET   H  81  ? 1.5510 0.7285 1.2107 0.0567  -0.3007 -0.1248 82  MET   H O   
13681 C  CB  . MET   H  81  ? 1.6234 0.6318 1.1925 -0.0244 -0.2865 -0.0925 82  MET   H CB  
13682 C  CG  . MET   H  81  ? 1.6550 0.6668 1.1683 0.0041  -0.2750 -0.1109 82  MET   H CG  
13683 S  SD  . MET   H  81  ? 1.6948 0.6498 1.1795 -0.0133 -0.2623 -0.1562 82  MET   H SD  
13684 C  CE  . MET   H  81  ? 1.6863 0.6243 1.1804 0.0103  -0.2326 -0.1622 82  MET   H CE  
13685 N  N   . LEU   H  82  ? 1.5736 0.5131 1.1907 0.0278  -0.2724 -0.0937 83  LEU   H N   
13686 C  CA  . LEU   H  82  ? 1.5070 0.4341 1.1625 0.0180  -0.2868 -0.0331 83  LEU   H CA  
13687 C  C   . LEU   H  82  ? 1.5521 0.3290 1.1154 0.0132  -0.3088 -0.0427 83  LEU   H C   
13688 O  O   . LEU   H  82  ? 1.5438 0.3909 1.1048 0.0264  -0.3364 -0.0021 83  LEU   H O   
13689 C  CB  . LEU   H  82  ? 1.5068 0.3669 1.1487 0.0195  -0.2591 -0.0282 83  LEU   H CB  
13690 C  CG  . LEU   H  82  ? 1.4548 0.3786 1.1659 0.0534  -0.2760 -0.0312 83  LEU   H CG  
13691 C  CD1 . LEU   H  82  ? 1.4545 0.3518 1.1582 0.0500  -0.2700 -0.0229 83  LEU   H CD1 
13692 C  CD2 . LEU   H  82  ? 1.4546 0.3911 1.1739 0.0581  -0.2885 -0.0601 83  LEU   H CD2 
13693 N  N   . LYS   H  83  ? 1.5593 0.2672 1.1152 0.0064  -0.2943 -0.0680 84  LYS   H N   
13694 C  CA  . LYS   H  83  ? 1.5566 0.3104 1.1442 -0.0068 -0.2852 -0.0678 84  LYS   H CA  
13695 C  C   . LYS   H  83  ? 1.5697 0.3441 1.0977 0.0015  -0.2831 -0.0305 84  LYS   H C   
13696 O  O   . LYS   H  83  ? 1.5443 0.2323 1.2323 -0.0027 -0.2984 0.0947  84  LYS   H O   
13697 C  CB  . LYS   H  83  ? 1.6033 0.3383 1.1346 -0.0215 -0.2763 -0.1007 84  LYS   H CB  
13698 C  CG  . LYS   H  83  ? 1.6226 0.3687 1.1624 0.0070  -0.2357 -0.0798 84  LYS   H CG  
13699 C  CD  . LYS   H  83  ? 1.6380 0.4010 1.2102 -0.0294 -0.2442 -0.0318 84  LYS   H CD  
13700 C  CE  . LYS   H  83  ? 1.6532 0.4477 1.2570 -0.0112 -0.2550 -0.0039 84  LYS   H CE  
13701 N  NZ  . LYS   H  83  ? 1.6528 0.5074 1.2833 -0.0246 -0.2503 0.0085  84  LYS   H NZ  
13702 N  N   . GLN   H  84  ? 1.5823 0.3535 1.0104 0.0156  -0.2502 -0.0550 85  GLN   H N   
13703 C  CA  . GLN   H  84  ? 1.5614 0.4289 1.0072 0.0087  -0.2219 -0.0193 85  GLN   H CA  
13704 C  C   . GLN   H  84  ? 1.5523 0.4000 1.0146 -0.0030 -0.2507 0.0120  85  GLN   H C   
13705 O  O   . GLN   H  84  ? 1.5504 0.2947 1.0595 -0.0308 -0.2612 0.0245  85  GLN   H O   
13706 C  CB  . GLN   H  84  ? 1.5680 0.4377 0.9714 0.0288  -0.1747 -0.0087 85  GLN   H CB  
13707 C  CG  . GLN   H  84  ? 1.5784 0.5328 0.9803 0.0422  -0.1541 -0.0084 85  GLN   H CG  
13708 C  CD  . GLN   H  84  ? 1.6002 0.6172 0.8848 0.0509  -0.1169 -0.0666 85  GLN   H CD  
13709 O  OE1 . GLN   H  84  ? 1.6300 0.6713 0.8461 0.0759  -0.0823 -0.0389 85  GLN   H OE1 
13710 N  NE2 . GLN   H  84  ? 1.6202 0.6559 0.8900 0.0341  -0.0973 -0.0922 85  GLN   H NE2 
13711 N  N   . HIS   H  85  ? 1.5505 0.4382 1.0606 -0.0087 -0.2451 0.0141  86  HIS   H N   
13712 C  CA  . HIS   H  85  ? 1.5436 0.5210 1.0579 -0.0144 -0.2472 0.0161  86  HIS   H CA  
13713 C  C   . HIS   H  85  ? 1.5020 0.5406 1.0372 -0.0334 -0.2849 0.0143  86  HIS   H C   
13714 O  O   . HIS   H  85  ? 1.4798 0.6662 1.0725 -0.0443 -0.2904 0.0032  86  HIS   H O   
13715 C  CB  . HIS   H  85  ? 1.5597 0.5142 1.0664 -0.0043 -0.2114 0.0138  86  HIS   H CB  
13716 C  CG  . HIS   H  85  ? 1.5780 0.5821 1.0744 0.0087  -0.1864 0.0306  86  HIS   H CG  
13717 N  ND1 . HIS   H  85  ? 1.5696 0.5922 1.0557 -0.0016 -0.1648 0.0509  86  HIS   H ND1 
13718 C  CD2 . HIS   H  85  ? 1.5636 0.6739 1.0900 0.0517  -0.1464 0.0628  86  HIS   H CD2 
13719 C  CE1 . HIS   H  85  ? 1.5711 0.6239 1.0611 0.0063  -0.1318 0.1053  86  HIS   H CE1 
13720 N  NE2 . HIS   H  85  ? 1.5677 0.6839 1.1090 0.0439  -0.1388 0.0926  86  HIS   H NE2 
13721 N  N   . LEU   H  86  ? 1.4735 0.4903 0.9725 -0.0938 -0.3212 -0.0098 87  LEU   H N   
13722 C  CA  . LEU   H  86  ? 1.4612 0.4703 0.9188 -0.0926 -0.3324 0.0234  87  LEU   H CA  
13723 C  C   . LEU   H  86  ? 1.4648 0.4296 0.9597 -0.0706 -0.3254 0.0768  87  LEU   H C   
13724 O  O   . LEU   H  86  ? 1.4387 0.5255 0.9056 -0.1096 -0.4062 0.1731  87  LEU   H O   
13725 C  CB  . LEU   H  86  ? 1.4280 0.4696 0.9046 -0.1000 -0.3373 -0.0177 87  LEU   H CB  
13726 C  CG  . LEU   H  86  ? 1.4545 0.5151 0.8945 -0.1171 -0.3078 -0.0378 87  LEU   H CG  
13727 C  CD1 . LEU   H  86  ? 1.4510 0.5385 0.9443 -0.1107 -0.3306 -0.0466 87  LEU   H CD1 
13728 C  CD2 . LEU   H  86  ? 1.4545 0.5772 0.8751 -0.1086 -0.2923 -0.0055 87  LEU   H CD2 
13729 N  N   . PHE   H  87  ? 1.4732 0.3559 0.9667 -0.0556 -0.3587 0.0135  88  PHE   H N   
13730 C  CA  . PHE   H  87  ? 1.4557 0.4213 1.0446 -0.0366 -0.3356 -0.0364 88  PHE   H CA  
13731 C  C   . PHE   H  87  ? 1.4955 0.4172 1.1027 0.0112  -0.3418 -0.0160 88  PHE   H C   
13732 O  O   . PHE   H  87  ? 1.4317 0.5287 1.2901 -0.0133 -0.3367 0.0243  88  PHE   H O   
13733 C  CB  . PHE   H  87  ? 1.3996 0.4125 1.0553 -0.0064 -0.3332 -0.0261 88  PHE   H CB  
13734 C  CG  . PHE   H  87  ? 1.3628 0.4066 1.0482 0.0290  -0.3379 -0.0299 88  PHE   H CG  
13735 C  CD1 . PHE   H  87  ? 1.3731 0.4469 1.0758 -0.0287 -0.2992 -0.0068 88  PHE   H CD1 
13736 C  CD2 . PHE   H  87  ? 1.3460 0.3838 0.9965 0.0112  -0.3415 -0.0026 88  PHE   H CD2 
13737 C  CE1 . PHE   H  87  ? 1.3189 0.4900 1.0797 0.0136  -0.3265 -0.0297 88  PHE   H CE1 
13738 C  CE2 . PHE   H  87  ? 1.3216 0.3816 0.9927 0.0285  -0.3578 -0.0046 88  PHE   H CE2 
13739 C  CZ  . PHE   H  87  ? 1.3433 0.3917 1.0201 -0.0053 -0.3418 -0.0029 88  PHE   H CZ  
13740 N  N   . LYS   H  88  ? 1.5631 0.4168 1.1865 -0.0904 -0.2826 -0.0499 89  LYS   H N   
13741 C  CA  . LYS   H  88  ? 1.5743 0.5270 1.1777 -0.0816 -0.3043 -0.0556 89  LYS   H CA  
13742 C  C   . LYS   H  88  ? 1.5286 0.4454 1.1774 -0.0749 -0.3378 -0.0372 89  LYS   H C   
13743 O  O   . LYS   H  88  ? 1.5514 0.2703 1.1687 -0.0937 -0.3569 0.0329  89  LYS   H O   
13744 C  CB  . LYS   H  88  ? 1.6257 0.5772 1.2944 -0.1369 -0.2405 -0.0310 89  LYS   H CB  
13745 C  CG  . LYS   H  88  ? 1.6149 0.6940 1.3586 -0.1037 -0.2499 -0.0138 89  LYS   H CG  
13746 C  CD  . LYS   H  88  ? 1.7219 0.7562 1.5179 -0.2071 -0.2064 -0.0414 89  LYS   H CD  
13747 C  CE  . LYS   H  88  ? 1.7982 0.8431 1.6401 -0.2437 -0.1259 -0.0701 89  LYS   H CE  
13748 N  NZ  . LYS   H  88  ? 1.9505 0.8241 1.7760 -0.2865 -0.0699 -0.0465 89  LYS   H NZ  
13749 N  N   . TYR   H  89  ? 1.5643 0.5451 1.1328 -0.0455 -0.3119 -0.1041 90  TYR   H N   
13750 C  CA  . TYR   H  89  ? 1.5569 0.7276 1.0948 -0.0231 -0.2958 -0.1250 90  TYR   H CA  
13751 C  C   . TYR   H  89  ? 1.6663 0.7149 1.0857 -0.0056 -0.2764 -0.1567 90  TYR   H C   
13752 O  O   . TYR   H  89  ? 1.7098 0.7493 1.0849 0.0200  -0.2369 -0.1487 90  TYR   H O   
13753 C  CB  . TYR   H  89  ? 1.5279 0.7419 1.0523 -0.0400 -0.3240 -0.1512 90  TYR   H CB  
13754 C  CG  . TYR   H  89  ? 1.4802 0.6717 1.0727 -0.0268 -0.3252 -0.1992 90  TYR   H CG  
13755 C  CD1 . TYR   H  89  ? 1.4892 0.7302 1.0772 -0.0319 -0.3192 -0.1918 90  TYR   H CD1 
13756 C  CD2 . TYR   H  89  ? 1.5020 0.6735 1.0662 -0.0249 -0.2976 -0.2101 90  TYR   H CD2 
13757 C  CE1 . TYR   H  89  ? 1.4898 0.6989 1.1129 -0.0544 -0.3132 -0.2038 90  TYR   H CE1 
13758 C  CE2 . TYR   H  89  ? 1.5452 0.6985 1.0791 -0.0400 -0.2815 -0.1906 90  TYR   H CE2 
13759 C  CZ  . TYR   H  89  ? 1.5371 0.6621 1.0880 -0.0397 -0.3036 -0.1750 90  TYR   H CZ  
13760 O  OH  . TYR   H  89  ? 1.5986 0.7363 1.1799 -0.0069 -0.2886 -0.0841 90  TYR   H OH  
13761 N  N   . GLN   H  90  ? 1.6761 0.7578 1.0716 0.0288  -0.2585 -0.1769 91  GLN   H N   
13762 C  CA  . GLN   H  90  ? 1.5670 0.7605 1.1186 0.0521  -0.2412 -0.2046 91  GLN   H CA  
13763 C  C   . GLN   H  90  ? 1.5588 0.8153 1.0847 0.0910  -0.2634 -0.2102 91  GLN   H C   
13764 O  O   . GLN   H  90  ? 1.5844 0.8421 0.9980 0.2202  -0.2971 -0.3150 91  GLN   H O   
13765 C  CB  . GLN   H  90  ? 1.5517 0.8857 1.1248 0.1443  -0.2466 -0.2290 91  GLN   H CB  
13766 C  CG  . GLN   H  90  ? 1.5926 0.8418 1.2210 0.1930  -0.2867 -0.2722 91  GLN   H CG  
13767 C  CD  . GLN   H  90  ? 1.5992 0.9738 1.2092 0.2563  -0.2201 -0.3361 91  GLN   H CD  
13768 O  OE1 . GLN   H  90  ? 1.6288 1.0580 1.3189 0.1873  -0.1862 -0.2516 91  GLN   H OE1 
13769 N  NE2 . GLN   H  90  ? 1.5607 0.8573 1.3152 0.2570  -0.2364 -0.3375 91  GLN   H NE2 
13770 N  N   . GLY   H  91  ? 1.5398 0.8241 1.0727 0.1129  -0.2269 -0.1470 92  GLY   H N   
13771 C  CA  . GLY   H  91  ? 1.4985 0.8398 1.0415 0.0730  -0.1807 -0.1686 92  GLY   H CA  
13772 C  C   . GLY   H  91  ? 1.4935 0.7751 1.0219 -0.0041 -0.2008 -0.1455 92  GLY   H C   
13773 O  O   . GLY   H  91  ? 1.4469 0.7486 0.9214 -0.0435 -0.1963 -0.1032 92  GLY   H O   
13774 N  N   . HIS   H  92  ? 1.4374 0.7356 1.0241 -0.0074 -0.2095 -0.1866 93  HIS   H N   
13775 C  CA  . HIS   H  92  ? 1.4523 0.8010 1.0299 -0.0028 -0.2032 -0.2215 93  HIS   H CA  
13776 C  C   . HIS   H  92  ? 1.4793 0.8293 1.1063 -0.0407 -0.2373 -0.1848 93  HIS   H C   
13777 O  O   . HIS   H  92  ? 1.4969 1.0786 1.0837 -0.0772 -0.1869 -0.1423 93  HIS   H O   
13778 C  CB  . HIS   H  92  ? 1.4426 0.7754 1.0244 0.0340  -0.1638 -0.2294 93  HIS   H CB  
13779 C  CG  . HIS   H  92  ? 1.4094 0.8592 1.0451 0.0443  -0.1409 -0.2430 93  HIS   H CG  
13780 N  ND1 . HIS   H  92  ? 1.4404 0.9948 1.0079 0.0220  -0.1869 -0.3125 93  HIS   H ND1 
13781 C  CD2 . HIS   H  92  ? 1.4357 0.8702 1.0583 0.0958  -0.1343 -0.2782 93  HIS   H CD2 
13782 C  CE1 . HIS   H  92  ? 1.4153 1.0022 1.0052 0.0503  -0.1961 -0.3675 93  HIS   H CE1 
13783 N  NE2 . HIS   H  92  ? 1.4246 0.9932 1.0160 0.0944  -0.1976 -0.3408 93  HIS   H NE2 
13784 N  N   . ILE   H  93  ? 1.5050 0.7097 1.1883 -0.0537 -0.2948 -0.1299 94  ILE   H N   
13785 C  CA  . ILE   H  93  ? 1.5513 0.6738 1.1806 -0.1152 -0.3220 -0.1419 94  ILE   H CA  
13786 C  C   . ILE   H  93  ? 1.5924 0.6604 1.1653 -0.1626 -0.3203 -0.1188 94  ILE   H C   
13787 O  O   . ILE   H  93  ? 1.7471 0.6568 1.1549 -0.3327 -0.3527 -0.1698 94  ILE   H O   
13788 C  CB  . ILE   H  93  ? 1.5497 0.6898 1.1116 -0.0605 -0.3660 -0.1650 94  ILE   H CB  
13789 C  CG1 . ILE   H  93  ? 1.5732 0.7609 1.0754 -0.0895 -0.3677 -0.1355 94  ILE   H CG1 
13790 C  CG2 . ILE   H  93  ? 1.5478 0.6673 1.0855 -0.0438 -0.3774 -0.1508 94  ILE   H CG2 
13791 C  CD1 . ILE   H  93  ? 1.5987 0.7306 1.1180 -0.1385 -0.3481 -0.0912 94  ILE   H CD1 
13792 N  N   . GLY   H  94  ? 1.5690 0.6388 1.2342 -0.1551 -0.2738 -0.0789 95  GLY   H N   
13793 C  CA  . GLY   H  94  ? 1.4689 0.6234 1.2620 -0.1688 -0.2607 -0.0871 95  GLY   H CA  
13794 C  C   . GLY   H  94  ? 1.4370 0.5304 1.2476 -0.1653 -0.2240 -0.1021 95  GLY   H C   
13795 O  O   . GLY   H  94  ? 1.3316 0.5808 1.2823 -0.2264 -0.2238 -0.0680 95  GLY   H O   
13796 N  N   . ALA   H  95  ? 1.4350 0.4716 1.2622 -0.1050 -0.2112 -0.0874 96  ALA   H N   
13797 C  CA  . ALA   H  95  ? 1.4733 0.4581 1.2251 -0.0604 -0.2255 -0.1321 96  ALA   H CA  
13798 C  C   . ALA   H  95  ? 1.4954 0.3403 1.2518 0.0097  -0.2302 -0.1257 96  ALA   H C   
13799 O  O   . ALA   H  95  ? 1.5399 0.3231 1.2488 -0.0048 -0.1977 -0.1367 96  ALA   H O   
13800 C  CB  . ALA   H  95  ? 1.4769 0.4567 1.2467 -0.0473 -0.2313 -0.1199 96  ALA   H CB  
13801 N  N   . TYR   H  96  ? 1.5167 0.3599 1.2803 0.0335  -0.2461 -0.1247 97  TYR   H N   
13802 C  CA  . TYR   H  96  ? 1.5283 0.3914 1.3213 0.0548  -0.2759 -0.0904 97  TYR   H CA  
13803 C  C   . TYR   H  96  ? 1.5214 0.4217 1.3511 0.0590  -0.2670 -0.1095 97  TYR   H C   
13804 O  O   . TYR   H  96  ? 1.5509 0.5989 1.3755 0.0202  -0.2030 -0.0722 97  TYR   H O   
13805 C  CB  . TYR   H  96  ? 1.5178 0.3872 1.3529 0.0264  -0.3010 -0.0565 97  TYR   H CB  
13806 C  CG  . TYR   H  96  ? 1.5279 0.2553 1.3818 0.0271  -0.2937 -0.0274 97  TYR   H CG  
13807 C  CD1 . TYR   H  96  ? 1.5547 0.2691 1.3946 -0.0020 -0.2770 -0.0614 97  TYR   H CD1 
13808 C  CD2 . TYR   H  96  ? 1.5236 0.2271 1.3768 0.0521  -0.2909 -0.0252 97  TYR   H CD2 
13809 C  CE1 . TYR   H  96  ? 1.5655 0.2380 1.4535 -0.0305 -0.2388 -0.0870 97  TYR   H CE1 
13810 C  CE2 . TYR   H  96  ? 1.5382 0.2223 1.4125 0.0191  -0.2550 -0.0613 97  TYR   H CE2 
13811 C  CZ  . TYR   H  96  ? 1.5357 0.2338 1.4348 -0.0388 -0.2599 -0.1044 97  TYR   H CZ  
13812 O  OH  . TYR   H  96  ? 1.4957 0.2471 1.5585 -0.0895 -0.1720 -0.1251 97  TYR   H OH  
13813 N  N   . LEU   H  97  ? 1.5545 0.3012 1.3919 0.0836  -0.2836 -0.0943 98  LEU   H N   
13814 C  CA  . LEU   H  97  ? 1.5497 0.4170 1.3621 0.0679  -0.3089 -0.1198 98  LEU   H CA  
13815 C  C   . LEU   H  97  ? 1.5248 0.2438 1.3834 0.0925  -0.3210 -0.1151 98  LEU   H C   
13816 O  O   . LEU   H  97  ? 1.5219 0.2333 1.4299 0.0497  -0.3264 -0.1022 98  LEU   H O   
13817 C  CB  . LEU   H  97  ? 1.5706 0.4697 1.3299 0.1287  -0.3319 -0.0679 98  LEU   H CB  
13818 C  CG  . LEU   H  97  ? 1.5505 0.6115 1.3011 0.1388  -0.3288 -0.0889 98  LEU   H CG  
13819 C  CD1 . LEU   H  97  ? 1.5543 0.6263 1.2953 0.1542  -0.3258 -0.0912 98  LEU   H CD1 
13820 C  CD2 . LEU   H  97  ? 1.5446 0.6672 1.2625 0.1388  -0.3407 -0.1093 98  LEU   H CD2 
13821 N  N   . ILE   H  98  ? 1.5334 0.3060 1.3856 0.1041  -0.3327 -0.1376 99  ILE   H N   
13822 C  CA  . ILE   H  98  ? 1.5618 0.5002 1.3936 0.0896  -0.3589 -0.1161 99  ILE   H CA  
13823 C  C   . ILE   H  98  ? 1.5235 0.5440 1.4076 0.0361  -0.3680 -0.1143 99  ILE   H C   
13824 O  O   . ILE   H  98  ? 1.4636 0.6793 1.4654 0.0288  -0.3870 -0.0871 99  ILE   H O   
13825 C  CB  . ILE   H  98  ? 1.5744 0.5369 1.3877 0.1217  -0.3456 -0.1347 99  ILE   H CB  
13826 C  CG1 . ILE   H  98  ? 1.5936 0.5724 1.3689 0.0862  -0.3284 -0.1175 99  ILE   H CG1 
13827 C  CG2 . ILE   H  98  ? 1.5778 0.5834 1.4133 0.1138  -0.3586 -0.1447 99  ILE   H CG2 
13828 C  CD1 . ILE   H  98  ? 1.6207 0.5973 1.3819 0.1011  -0.3131 -0.0847 99  ILE   H CD1 
13829 N  N   . VAL   H  99  ? 1.5356 0.5434 1.3737 0.0199  -0.3647 -0.1184 100 VAL   H N   
13830 C  CA  . VAL   H  99  ? 1.5335 0.5638 1.3219 -0.0151 -0.3606 -0.1441 100 VAL   H CA  
13831 C  C   . VAL   H  99  ? 1.5682 0.4811 1.2930 -0.0601 -0.3405 -0.1704 100 VAL   H C   
13832 O  O   . VAL   H  99  ? 1.5828 0.3440 1.2952 -0.1476 -0.3255 -0.2571 100 VAL   H O   
13833 C  CB  . VAL   H  99  ? 1.5267 0.5676 1.3552 -0.0237 -0.3633 -0.1446 100 VAL   H CB  
13834 C  CG1 . VAL   H  99  ? 1.5394 0.5841 1.3503 -0.0643 -0.3728 -0.1669 100 VAL   H CG1 
13835 C  CG2 . VAL   H  99  ? 1.5035 0.5898 1.3734 -0.0259 -0.3661 -0.1334 100 VAL   H CG2 
13836 N  N   . ALA   H  100 ? 1.5567 0.5426 1.3255 -0.0575 -0.3109 -0.0917 101 ALA   H N   
13837 C  CA  . ALA   H  100 ? 1.5580 0.5929 1.3220 -0.0092 -0.3345 -0.0252 101 ALA   H CA  
13838 C  C   . ALA   H  100 ? 1.5532 0.6272 1.2533 -0.0521 -0.3542 -0.0592 101 ALA   H C   
13839 O  O   . ALA   H  100 ? 1.5840 0.6476 1.2243 -0.1198 -0.2746 -0.0995 101 ALA   H O   
13840 C  CB  . ALA   H  100 ? 1.5698 0.6599 1.3569 0.0352  -0.3496 -0.0040 101 ALA   H CB  
13841 N  N   . GLY   H  101 ? 1.5304 0.6032 1.2077 -0.0412 -0.3688 0.0113  102 GLY   H N   
13842 C  CA  . GLY   H  101 ? 1.5390 0.6265 1.2266 -0.0589 -0.3574 -0.0023 102 GLY   H CA  
13843 C  C   . GLY   H  101 ? 1.5608 0.6235 1.2209 -0.1027 -0.3621 0.0016  102 GLY   H C   
13844 O  O   . GLY   H  101 ? 1.5879 0.5387 1.1697 -0.0834 -0.4101 0.0237  102 GLY   H O   
13845 N  N   . VAL   H  102 ? 1.5651 0.6989 1.2575 -0.1461 -0.3698 -0.0675 103 VAL   H N   
13846 C  CA  . VAL   H  102 ? 1.5763 0.7141 1.2489 -0.1079 -0.3739 -0.0710 103 VAL   H CA  
13847 C  C   . VAL   H  102 ? 1.5589 0.7137 1.3193 -0.0820 -0.3761 -0.1168 103 VAL   H C   
13848 O  O   . VAL   H  102 ? 1.5273 0.5957 1.3070 -0.0811 -0.3808 -0.1697 103 VAL   H O   
13849 C  CB  . VAL   H  102 ? 1.5793 0.7412 1.2398 -0.1293 -0.3730 -0.0899 103 VAL   H CB  
13850 C  CG1 . VAL   H  102 ? 1.5779 0.7538 1.2296 -0.1057 -0.3584 -0.0802 103 VAL   H CG1 
13851 C  CG2 . VAL   H  102 ? 1.5579 0.7623 1.2621 -0.1705 -0.3701 -0.1274 103 VAL   H CG2 
13852 N  N   . ASP   H  103 ? 1.5703 0.7120 1.2992 -0.0376 -0.3551 -0.0512 104 ASP   H N   
13853 C  CA  . ASP   H  103 ? 1.6491 0.7428 1.3822 0.0075  -0.2991 -0.1046 104 ASP   H CA  
13854 C  C   . ASP   H  103 ? 1.6634 0.8458 1.3440 -0.0017 -0.3465 -0.0680 104 ASP   H C   
13855 O  O   . ASP   H  103 ? 1.6234 0.6392 1.4367 -0.0375 -0.3417 -0.0634 104 ASP   H O   
13856 C  CB  . ASP   H  103 ? 1.6562 0.7019 1.3887 -0.0105 -0.2921 -0.1156 104 ASP   H CB  
13857 C  CG  . ASP   H  103 ? 1.7409 0.6474 1.3154 0.0625  -0.2782 -0.0518 104 ASP   H CG  
13858 O  OD1 . ASP   H  103 ? 1.6768 0.3858 1.3010 0.1202  -0.3804 0.0149  104 ASP   H OD1 
13859 O  OD2 . ASP   H  103 ? 1.8003 0.6703 1.3770 0.0427  -0.2755 -0.0773 104 ASP   H OD2 
13860 N  N   . PRO   H  104 ? 1.7337 0.8779 1.4561 -0.0211 -0.2794 -0.1637 105 PRO   H N   
13861 C  CA  . PRO   H  104 ? 1.7093 1.0332 1.4071 -0.0246 -0.2950 -0.1380 105 PRO   H CA  
13862 C  C   . PRO   H  104 ? 1.6671 1.0772 1.3315 -0.0141 -0.3319 -0.1373 105 PRO   H C   
13863 O  O   . PRO   H  104 ? 1.6975 1.1867 1.3228 -0.0399 -0.3329 -0.1051 105 PRO   H O   
13864 C  CB  . PRO   H  104 ? 1.7666 1.0125 1.4848 -0.0132 -0.2249 -0.1261 105 PRO   H CB  
13865 C  CG  . PRO   H  104 ? 1.7897 0.9506 1.5020 -0.0100 -0.1867 -0.1347 105 PRO   H CG  
13866 C  CD  . PRO   H  104 ? 1.7875 0.9074 1.4668 -0.0624 -0.2310 -0.1088 105 PRO   H CD  
13867 N  N   . THR   H  105 ? 1.6340 1.0566 1.3111 0.0107  -0.3349 -0.1147 106 THR   H N   
13868 C  CA  . THR   H  105 ? 1.6441 1.1150 1.2898 0.0197  -0.3220 -0.1077 106 THR   H CA  
13869 C  C   . THR   H  105 ? 1.6013 1.1640 1.1733 0.0158  -0.3553 -0.1062 106 THR   H C   
13870 O  O   . THR   H  105 ? 1.5909 1.1497 1.1318 0.0106  -0.3974 -0.1222 106 THR   H O   
13871 C  CB  . THR   H  105 ? 1.6509 1.1692 1.3654 -0.0238 -0.3153 -0.1056 106 THR   H CB  
13872 O  OG1 . THR   H  105 ? 1.7164 1.1830 1.4543 0.0045  -0.2653 -0.1752 106 THR   H OG1 
13873 C  CG2 . THR   H  105 ? 1.6539 1.1593 1.3796 0.0183  -0.3055 -0.0723 106 THR   H CG2 
13874 N  N   . GLY   H  106 ? 1.5707 1.2019 1.2668 0.0312  -0.3513 -0.1327 107 GLY   H N   
13875 C  CA  . GLY   H  106 ? 1.5800 1.1772 1.3497 -0.0052 -0.3764 -0.0497 107 GLY   H CA  
13876 C  C   . GLY   H  106 ? 1.5692 1.0751 1.4825 -0.0281 -0.3467 -0.1050 107 GLY   H C   
13877 O  O   . GLY   H  106 ? 1.5057 1.1219 1.5405 0.0016  -0.3541 -0.0739 107 GLY   H O   
13878 N  N   . SER   H  107 ? 1.6278 1.0719 1.4619 -0.0818 -0.3425 0.0525  108 SER   H N   
13879 C  CA  . SER   H  107 ? 1.6307 1.0120 1.4529 -0.1086 -0.3173 0.0963  108 SER   H CA  
13880 C  C   . SER   H  107 ? 1.6924 0.8966 1.2964 -0.1178 -0.3194 0.1157  108 SER   H C   
13881 O  O   . SER   H  107 ? 1.6474 0.6299 1.3675 -0.2025 -0.3721 0.1910  108 SER   H O   
13882 C  CB  . SER   H  107 ? 1.6659 1.0571 1.4844 -0.0711 -0.2772 0.1895  108 SER   H CB  
13883 O  OG  . SER   H  107 ? 1.7554 1.1159 1.5519 -0.1159 -0.2118 0.2393  108 SER   H OG  
13884 N  N   . HIS   H  108 ? 1.6923 0.8272 1.3456 -0.1379 -0.3391 0.0506  109 HIS   H N   
13885 C  CA  . HIS   H  108 ? 1.6618 0.8372 1.2924 -0.1071 -0.3535 0.0729  109 HIS   H CA  
13886 C  C   . HIS   H  108 ? 1.6126 0.7877 1.3431 -0.1279 -0.3724 0.0582  109 HIS   H C   
13887 O  O   . HIS   H  108 ? 1.6487 0.7348 1.3423 -0.1240 -0.3534 0.0401  109 HIS   H O   
13888 C  CB  . HIS   H  108 ? 1.6682 0.9426 1.2798 -0.0846 -0.3899 0.1047  109 HIS   H CB  
13889 C  CG  . HIS   H  108 ? 1.7474 1.1160 1.2104 -0.0885 -0.3800 0.0408  109 HIS   H CG  
13890 N  ND1 . HIS   H  108 ? 1.7772 1.1534 1.2405 -0.1548 -0.3773 0.1921  109 HIS   H ND1 
13891 C  CD2 . HIS   H  108 ? 1.8541 1.1872 1.3752 -0.1819 -0.3929 0.0419  109 HIS   H CD2 
13892 C  CE1 . HIS   H  108 ? 1.8954 1.2763 1.3417 -0.1630 -0.3324 0.0921  109 HIS   H CE1 
13893 N  NE2 . HIS   H  108 ? 1.9034 1.3537 1.4044 -0.1990 -0.2853 0.0715  109 HIS   H NE2 
13894 N  N   . LEU   H  109 ? 1.5286 0.7843 1.3033 -0.1062 -0.3836 -0.0300 110 LEU   H N   
13895 C  CA  . LEU   H  109 ? 1.5185 0.8087 1.2911 -0.0669 -0.3749 -0.0413 110 LEU   H CA  
13896 C  C   . LEU   H  109 ? 1.5061 0.6746 1.2129 -0.0309 -0.3835 -0.0314 110 LEU   H C   
13897 O  O   . LEU   H  109 ? 1.4373 0.6161 1.1672 -0.0188 -0.4456 -0.0142 110 LEU   H O   
13898 C  CB  . LEU   H  109 ? 1.5466 0.8090 1.2864 -0.0479 -0.3690 -0.0790 110 LEU   H CB  
13899 C  CG  . LEU   H  109 ? 1.5590 0.8267 1.2468 -0.0863 -0.3816 -0.0873 110 LEU   H CG  
13900 C  CD1 . LEU   H  109 ? 1.5689 0.8603 1.2086 -0.0983 -0.3807 -0.1469 110 LEU   H CD1 
13901 C  CD2 . LEU   H  109 ? 1.5680 0.7782 1.2314 -0.0944 -0.3856 -0.1097 110 LEU   H CD2 
13902 N  N   . PHE   H  110 ? 1.4784 0.5608 1.2162 -0.0600 -0.3848 -0.0565 111 PHE   H N   
13903 C  CA  . PHE   H  110 ? 1.4566 0.5492 1.2671 -0.0758 -0.3568 -0.0016 111 PHE   H CA  
13904 C  C   . PHE   H  110 ? 1.4410 0.4611 1.3195 -0.0503 -0.3629 -0.0042 111 PHE   H C   
13905 O  O   . PHE   H  110 ? 1.4313 0.4827 1.3957 -0.0542 -0.3429 0.0068  111 PHE   H O   
13906 C  CB  . PHE   H  110 ? 1.4605 0.5557 1.2133 -0.0806 -0.3669 0.0128  111 PHE   H CB  
13907 C  CG  . PHE   H  110 ? 1.5330 0.5972 1.2006 -0.0809 -0.3340 0.0162  111 PHE   H CG  
13908 C  CD1 . PHE   H  110 ? 1.5926 0.6008 1.2287 -0.1209 -0.3336 0.0721  111 PHE   H CD1 
13909 C  CD2 . PHE   H  110 ? 1.5656 0.6150 1.2644 -0.0992 -0.3012 0.0574  111 PHE   H CD2 
13910 C  CE1 . PHE   H  110 ? 1.6624 0.6569 1.1899 -0.1183 -0.3228 0.0775  111 PHE   H CE1 
13911 C  CE2 . PHE   H  110 ? 1.6396 0.6425 1.2486 -0.1320 -0.2979 0.0524  111 PHE   H CE2 
13912 C  CZ  . PHE   H  110 ? 1.6975 0.6498 1.2278 -0.1187 -0.3083 0.0913  111 PHE   H CZ  
13913 N  N   . SER   H  111 ? 1.4856 0.3808 1.3901 -0.0545 -0.3870 -0.0057 112 SER   H N   
13914 C  CA  . SER   H  111 ? 1.5657 0.4429 1.3698 -0.0359 -0.3983 -0.0024 112 SER   H CA  
13915 C  C   . SER   H  111 ? 1.5952 0.2934 1.3422 -0.0375 -0.4048 0.0330  112 SER   H C   
13916 O  O   . SER   H  111 ? 1.5908 0.2362 1.2480 -0.0588 -0.4349 0.0360  112 SER   H O   
13917 C  CB  . SER   H  111 ? 1.6201 0.4376 1.4374 -0.0182 -0.3934 -0.0225 112 SER   H CB  
13918 O  OG  . SER   H  111 ? 1.6208 0.4454 1.4686 -0.0303 -0.3844 -0.0549 112 SER   H OG  
13919 N  N   . ILE   H  112 ? 1.6027 0.3079 1.3500 -0.0315 -0.4168 0.0284  113 ILE   H N   
13920 C  CA  . ILE   H  112 ? 1.5993 0.4384 1.3905 -0.0175 -0.4322 0.0061  113 ILE   H CA  
13921 C  C   . ILE   H  112 ? 1.6066 0.4818 1.3279 0.0420  -0.4272 0.0039  113 ILE   H C   
13922 O  O   . ILE   H  112 ? 1.4905 0.5466 1.2937 0.0573  -0.4803 0.0330  113 ILE   H O   
13923 C  CB  . ILE   H  112 ? 1.6384 0.4665 1.3903 -0.0486 -0.4343 0.0365  113 ILE   H CB  
13924 C  CG1 . ILE   H  112 ? 1.6599 0.5732 1.4180 -0.0694 -0.4522 -0.0028 113 ILE   H CG1 
13925 C  CG2 . ILE   H  112 ? 1.6517 0.4375 1.2893 -0.0710 -0.4662 0.0159  113 ILE   H CG2 
13926 C  CD1 . ILE   H  112 ? 1.6852 0.5768 1.4280 -0.0659 -0.4337 -0.0024 113 ILE   H CD1 
13927 N  N   . HIS   H  113 ? 1.6367 0.5688 1.3900 0.0075  -0.3990 0.0423  114 HIS   H N   
13928 C  CA  . HIS   H  113 ? 1.7530 0.5903 1.4091 -0.0050 -0.3599 0.0000  114 HIS   H CA  
13929 C  C   . HIS   H  113 ? 1.6924 0.4740 1.3385 -0.0703 -0.3080 -0.0130 114 HIS   H C   
13930 O  O   . HIS   H  113 ? 1.6310 0.3811 1.4360 -0.1311 -0.2461 0.0809  114 HIS   H O   
13931 C  CB  . HIS   H  113 ? 1.8744 0.6551 1.4848 0.0035  -0.2765 0.0705  114 HIS   H CB  
13932 C  CG  . HIS   H  113 ? 1.9363 0.7498 1.6554 0.1134  -0.2459 0.0941  114 HIS   H CG  
13933 N  ND1 . HIS   H  113 ? 1.9717 0.8058 1.7410 0.0632  -0.2729 0.0012  114 HIS   H ND1 
13934 C  CD2 . HIS   H  113 ? 1.9809 0.7803 1.7577 0.1206  -0.2022 0.0251  114 HIS   H CD2 
13935 C  CE1 . HIS   H  113 ? 2.0160 0.8484 1.8154 0.1157  -0.2355 0.0352  114 HIS   H CE1 
13936 N  NE2 . HIS   H  113 ? 2.0556 0.6385 1.8422 0.1558  -0.1804 0.0975  114 HIS   H NE2 
13937 N  N   . ALA   H  114 ? 1.6573 0.4741 1.2986 -0.0677 -0.3112 0.0173  115 ALA   H N   
13938 C  CA  . ALA   H  114 ? 1.6082 0.4055 1.2311 -0.0667 -0.2688 -0.0212 115 ALA   H CA  
13939 C  C   . ALA   H  114 ? 1.5965 0.3494 1.1788 -0.0774 -0.2727 -0.0243 115 ALA   H C   
13940 O  O   . ALA   H  114 ? 1.5334 0.2495 1.2362 -0.1313 -0.2234 -0.0974 115 ALA   H O   
13941 C  CB  . ALA   H  114 ? 1.6179 0.4967 1.1779 -0.0427 -0.2832 -0.0251 115 ALA   H CB  
13942 N  N   . HIS   H  115 ? 1.5835 0.3818 1.1541 -0.0379 -0.2592 -0.0118 116 HIS   H N   
13943 C  CA  . HIS   H  115 ? 1.5962 0.3208 1.1489 -0.0295 -0.2571 0.0105  116 HIS   H CA  
13944 C  C   . HIS   H  115 ? 1.5933 0.2841 1.1918 0.0163  -0.2634 0.0212  116 HIS   H C   
13945 O  O   . HIS   H  115 ? 1.6339 0.2318 1.2370 0.0427  -0.2627 0.0821  116 HIS   H O   
13946 C  CB  . HIS   H  115 ? 1.6300 0.2757 1.1371 -0.0281 -0.2548 -0.0326 116 HIS   H CB  
13947 C  CG  . HIS   H  115 ? 1.6183 0.2216 1.0943 -0.0174 -0.2423 0.0050  116 HIS   H CG  
13948 N  ND1 . HIS   H  115 ? 1.6060 0.2322 1.0364 -0.0458 -0.2139 0.0100  116 HIS   H ND1 
13949 C  CD2 . HIS   H  115 ? 1.6487 0.3300 1.0715 0.0125  -0.2341 -0.1182 116 HIS   H CD2 
13950 C  CE1 . HIS   H  115 ? 1.6079 0.2304 1.0339 -0.0146 -0.2009 -0.0130 116 HIS   H CE1 
13951 N  NE2 . HIS   H  115 ? 1.6076 0.2576 1.0691 0.0548  -0.2261 -0.1139 116 HIS   H NE2 
13952 N  N   . GLY   H  116 ? 1.5990 0.2837 1.2225 -0.0277 -0.2614 0.0182  117 GLY   H N   
13953 C  CA  . GLY   H  116 ? 1.6182 0.2600 1.1912 -0.0287 -0.2481 0.0436  117 GLY   H CA  
13954 C  C   . GLY   H  116 ? 1.6432 0.3597 1.1773 -0.0396 -0.2448 0.0152  117 GLY   H C   
13955 O  O   . GLY   H  116 ? 1.7125 0.2487 1.1844 -0.1106 -0.2260 0.0857  117 GLY   H O   
13956 N  N   . SER   H  117 ? 1.5959 0.3486 1.1905 0.0006  -0.2692 -0.0147 118 SER   H N   
13957 C  CA  . SER   H  117 ? 1.5814 0.3323 1.2058 0.0158  -0.2777 0.0011  118 SER   H CA  
13958 C  C   . SER   H  117 ? 1.5835 0.2675 1.2268 0.0184  -0.2775 0.0046  118 SER   H C   
13959 O  O   . SER   H  117 ? 1.5681 0.2268 1.2243 0.0349  -0.2804 0.0538  118 SER   H O   
13960 C  CB  . SER   H  117 ? 1.5575 0.3539 1.2309 -0.0537 -0.2773 -0.0323 118 SER   H CB  
13961 O  OG  . SER   H  117 ? 1.5602 0.3188 1.3385 -0.0720 -0.2370 -0.0548 118 SER   H OG  
13962 N  N   . THR   H  118 ? 1.5917 0.2614 1.2594 -0.0024 -0.2852 -0.0469 119 THR   H N   
13963 C  CA  . THR   H  118 ? 1.5923 0.4447 1.3229 -0.0212 -0.2947 -0.0853 119 THR   H CA  
13964 C  C   . THR   H  118 ? 1.5842 0.4075 1.3112 -0.0415 -0.2930 -0.1152 119 THR   H C   
13965 O  O   . THR   H  118 ? 1.5147 0.3652 1.3142 -0.0659 -0.3172 -0.1765 119 THR   H O   
13966 C  CB  . THR   H  118 ? 1.6112 0.4438 1.3324 -0.0566 -0.3130 -0.0588 119 THR   H CB  
13967 O  OG1 . THR   H  118 ? 1.6196 0.5121 1.3106 -0.0277 -0.3171 -0.0240 119 THR   H OG1 
13968 C  CG2 . THR   H  118 ? 1.6262 0.5592 1.3042 -0.0618 -0.2950 -0.0413 119 THR   H CG2 
13969 N  N   . ASP   H  119 ? 1.5894 0.4889 1.4055 -0.0249 -0.2850 -0.1502 120 ASP   H N   
13970 C  CA  . ASP   H  119 ? 1.6712 0.6232 1.4130 -0.0371 -0.2979 -0.0949 120 ASP   H CA  
13971 C  C   . ASP   H  119 ? 1.6785 0.6153 1.3536 -0.0032 -0.3205 -0.0981 120 ASP   H C   
13972 O  O   . ASP   H  119 ? 1.7023 0.6724 1.3161 -0.0213 -0.3172 -0.1012 120 ASP   H O   
13973 C  CB  . ASP   H  119 ? 1.7363 0.7321 1.5634 0.0594  -0.2178 -0.1065 120 ASP   H CB  
13974 C  CG  . ASP   H  119 ? 1.7963 0.8472 1.6663 -0.0010 -0.2137 -0.1562 120 ASP   H CG  
13975 O  OD1 . ASP   H  119 ? 1.8235 1.0570 1.7910 0.0857  -0.1688 -0.0598 120 ASP   H OD1 
13976 O  OD2 . ASP   H  119 ? 1.9624 0.8488 1.8299 0.0551  -0.0968 -0.1384 120 ASP   H OD2 
13977 N  N   . VAL   H  120 ? 1.6254 0.6735 1.3640 -0.0254 -0.3353 -0.0677 121 VAL   H N   
13978 C  CA  . VAL   H  120 ? 1.6324 0.7477 1.3528 -0.0354 -0.3339 -0.1067 121 VAL   H CA  
13979 C  C   . VAL   H  120 ? 1.5505 0.8222 1.3669 -0.0131 -0.3704 -0.1403 121 VAL   H C   
13980 O  O   . VAL   H  120 ? 1.5782 0.9598 1.4327 -0.0350 -0.2941 -0.0246 121 VAL   H O   
13981 C  CB  . VAL   H  120 ? 1.6059 0.7635 1.3128 -0.0100 -0.3879 -0.1070 121 VAL   H CB  
13982 C  CG1 . VAL   H  120 ? 1.5511 0.8081 1.3501 0.0169  -0.3980 -0.0941 121 VAL   H CG1 
13983 C  CG2 . VAL   H  120 ? 1.5932 0.7899 1.2862 0.0000  -0.3679 -0.1263 121 VAL   H CG2 
13984 N  N   . GLY   H  121 ? 1.5679 0.6782 1.3074 -0.1547 -0.3581 -0.2513 122 GLY   H N   
13985 C  CA  . GLY   H  121 ? 1.5791 0.6760 1.3186 -0.1550 -0.3408 -0.2348 122 GLY   H CA  
13986 C  C   . GLY   H  121 ? 1.5901 0.6652 1.3309 -0.1727 -0.3257 -0.2518 122 GLY   H C   
13987 O  O   . GLY   H  121 ? 1.6107 0.6872 1.3769 -0.1401 -0.2760 -0.2185 122 GLY   H O   
13988 N  N   . TYR   H  122 ? 1.6344 0.6656 1.3197 -0.1608 -0.2983 -0.2107 123 TYR   H N   
13989 C  CA  . TYR   H  122 ? 1.6301 0.7378 1.3457 -0.1326 -0.2831 -0.1606 123 TYR   H CA  
13990 C  C   . TYR   H  122 ? 1.6903 0.5892 1.3051 -0.1133 -0.3072 -0.1159 123 TYR   H C   
13991 O  O   . TYR   H  122 ? 1.6970 0.6560 1.3656 -0.1400 -0.3273 -0.0882 123 TYR   H O   
13992 C  CB  . TYR   H  122 ? 1.6642 0.8184 1.3213 -0.1238 -0.2710 -0.1723 123 TYR   H CB  
13993 C  CG  . TYR   H  122 ? 1.6476 1.0171 1.3071 -0.1571 -0.2556 -0.2221 123 TYR   H CG  
13994 C  CD1 . TYR   H  122 ? 1.6906 1.0957 1.2937 -0.1743 -0.2510 -0.3026 123 TYR   H CD1 
13995 C  CD2 . TYR   H  122 ? 1.6496 1.0950 1.2973 -0.1546 -0.2405 -0.2292 123 TYR   H CD2 
13996 C  CE1 . TYR   H  122 ? 1.7452 1.1575 1.3501 -0.1698 -0.1892 -0.3350 123 TYR   H CE1 
13997 C  CE2 . TYR   H  122 ? 1.6527 1.1681 1.3130 -0.2045 -0.2319 -0.2825 123 TYR   H CE2 
13998 C  CZ  . TYR   H  122 ? 1.7246 1.1693 1.4212 -0.2155 -0.2112 -0.3408 123 TYR   H CZ  
13999 O  OH  . TYR   H  122 ? 1.8063 1.2772 1.5453 -0.1330 -0.0387 -0.3313 123 TYR   H OH  
14000 N  N   . TYR   H  123 ? 1.6610 0.5018 1.2807 -0.0943 -0.3132 -0.0383 124 TYR   H N   
14001 C  CA  . TYR   H  123 ? 1.6465 0.5287 1.2894 -0.0855 -0.2952 -0.0316 124 TYR   H CA  
14002 C  C   . TYR   H  123 ? 1.6485 0.3953 1.2613 -0.0657 -0.2970 -0.0193 124 TYR   H C   
14003 O  O   . TYR   H  123 ? 1.6506 0.3893 1.2736 -0.0754 -0.2939 -0.0502 124 TYR   H O   
14004 C  CB  . TYR   H  123 ? 1.6473 0.5647 1.2845 -0.0680 -0.2989 -0.0316 124 TYR   H CB  
14005 C  CG  . TYR   H  123 ? 1.6519 0.5285 1.2911 -0.0909 -0.3222 -0.0583 124 TYR   H CG  
14006 C  CD1 . TYR   H  123 ? 1.6716 0.5660 1.2998 -0.0982 -0.3085 -0.0615 124 TYR   H CD1 
14007 C  CD2 . TYR   H  123 ? 1.6353 0.5411 1.2692 -0.0826 -0.3386 -0.0619 124 TYR   H CD2 
14008 C  CE1 . TYR   H  123 ? 1.6671 0.5574 1.3066 -0.1027 -0.3135 -0.0615 124 TYR   H CE1 
14009 C  CE2 . TYR   H  123 ? 1.6332 0.5874 1.2784 -0.1078 -0.3271 -0.0625 124 TYR   H CE2 
14010 C  CZ  . TYR   H  123 ? 1.6540 0.5807 1.2845 -0.1169 -0.3080 -0.0663 124 TYR   H CZ  
14011 O  OH  . TYR   H  123 ? 1.6733 0.6342 1.2665 -0.1335 -0.2940 -0.0580 124 TYR   H OH  
14012 N  N   . LEU   H  124 ? 1.6425 0.3073 1.2718 -0.0638 -0.2828 -0.0043 125 LEU   H N   
14013 C  CA  . LEU   H  124 ? 1.6620 0.3598 1.2598 -0.0625 -0.2871 0.0207  125 LEU   H CA  
14014 C  C   . LEU   H  124 ? 1.6339 0.2851 1.2712 -0.0486 -0.2636 0.0819  125 LEU   H C   
14015 O  O   . LEU   H  124 ? 1.6615 0.2901 1.3001 -0.0683 -0.2613 0.0764  125 LEU   H O   
14016 C  CB  . LEU   H  124 ? 1.6536 0.4385 1.2379 -0.0049 -0.3117 -0.0145 125 LEU   H CB  
14017 C  CG  . LEU   H  124 ? 1.7144 0.5725 1.2354 -0.0210 -0.3197 -0.0740 125 LEU   H CG  
14018 C  CD1 . LEU   H  124 ? 1.7385 0.5949 1.2320 -0.0179 -0.3401 -0.0362 125 LEU   H CD1 
14019 C  CD2 . LEU   H  124 ? 1.7223 0.5680 1.2433 -0.0414 -0.3438 -0.0776 125 LEU   H CD2 
14020 N  N   . SER   H  125 ? 1.5993 0.3078 1.2782 -0.0588 -0.2998 0.1106  126 SER   H N   
14021 C  CA  . SER   H  125 ? 1.5501 0.3613 1.2969 -0.0392 -0.2860 0.1226  126 SER   H CA  
14022 C  C   . SER   H  125 ? 1.5446 0.4145 1.3035 -0.0574 -0.2875 0.1472  126 SER   H C   
14023 O  O   . SER   H  125 ? 1.5443 0.5907 1.4126 -0.0821 -0.2520 0.1623  126 SER   H O   
14024 C  CB  . SER   H  125 ? 1.5465 0.3197 1.3427 -0.0684 -0.2891 0.1109  126 SER   H CB  
14025 O  OG  . SER   H  125 ? 1.5852 0.2649 1.3474 -0.0113 -0.3170 0.0635  126 SER   H OG  
14026 N  N   . LEU   H  126 ? 1.5426 0.4378 1.2535 0.0013  -0.3213 0.1030  127 LEU   H N   
14027 C  CA  . LEU   H  126 ? 1.5933 0.4489 1.2056 0.0256  -0.3270 0.0748  127 LEU   H CA  
14028 C  C   . LEU   H  126 ? 1.5630 0.3780 1.2131 0.0408  -0.3165 0.1159  127 LEU   H C   
14029 O  O   . LEU   H  126 ? 1.5514 0.3247 1.2297 0.0588  -0.3805 0.1375  127 LEU   H O   
14030 C  CB  . LEU   H  126 ? 1.6260 0.4925 1.1571 0.1129  -0.3595 0.0122  127 LEU   H CB  
14031 C  CG  . LEU   H  126 ? 1.6408 0.5302 1.1715 0.1235  -0.3527 0.0054  127 LEU   H CG  
14032 C  CD1 . LEU   H  126 ? 1.6260 0.4346 1.2299 0.1207  -0.3314 0.0399  127 LEU   H CD1 
14033 C  CD2 . LEU   H  126 ? 1.7041 0.5315 1.2063 0.1460  -0.3494 0.0487  127 LEU   H CD2 
14034 N  N   . GLY   H  127 ? 1.5793 0.3908 1.1986 0.0199  -0.3054 0.1291  128 GLY   H N   
14035 C  CA  . GLY   H  127 ? 1.5801 0.5136 1.2093 -0.0168 -0.2930 0.0918  128 GLY   H CA  
14036 C  C   . GLY   H  127 ? 1.5281 0.5263 1.2427 -0.0539 -0.2800 0.0180  128 GLY   H C   
14037 O  O   . GLY   H  127 ? 1.4842 0.5862 1.2260 -0.0912 -0.3255 0.0312  128 GLY   H O   
14038 N  N   . SER   H  128 ? 1.4672 0.6389 1.2939 -0.0350 -0.2264 -0.0303 129 SER   H N   
14039 C  CA  . SER   H  128 ? 1.4279 0.6461 1.3411 -0.0533 -0.2072 -0.0491 129 SER   H CA  
14040 C  C   . SER   H  128 ? 1.3789 0.6983 1.3184 -0.0869 -0.2483 -0.1002 129 SER   H C   
14041 O  O   . SER   H  128 ? 1.3846 0.7228 1.3779 -0.1364 -0.1921 -0.1063 129 SER   H O   
14042 C  CB  . SER   H  128 ? 1.4144 0.6911 1.3450 -0.0375 -0.1930 -0.0457 129 SER   H CB  
14043 O  OG  . SER   H  128 ? 1.3958 0.8036 1.3797 0.0081  -0.1515 -0.0396 129 SER   H OG  
14044 N  N   . GLY   H  129 ? 1.4131 0.6751 1.2885 -0.0804 -0.2722 -0.1285 130 GLY   H N   
14045 C  CA  . GLY   H  129 ? 1.4309 0.6417 1.3260 -0.0759 -0.2980 -0.1500 130 GLY   H CA  
14046 C  C   . GLY   H  129 ? 1.4363 0.5934 1.3116 -0.0751 -0.3753 -0.1451 130 GLY   H C   
14047 O  O   . GLY   H  129 ? 1.4490 0.4909 1.3077 -0.0764 -0.3903 -0.1491 130 GLY   H O   
14048 N  N   . SER   H  130 ? 1.4349 0.5857 1.3418 -0.0969 -0.3686 -0.1697 131 SER   H N   
14049 C  CA  . SER   H  130 ? 1.4573 0.5971 1.2979 -0.1083 -0.4096 -0.1225 131 SER   H CA  
14050 C  C   . SER   H  130 ? 1.4303 0.5123 1.3868 -0.0610 -0.4193 -0.1320 131 SER   H C   
14051 O  O   . SER   H  130 ? 1.4528 0.3769 1.4134 -0.0515 -0.4558 -0.1265 131 SER   H O   
14052 C  CB  . SER   H  130 ? 1.3873 0.6414 1.3159 -0.1586 -0.4480 -0.1156 131 SER   H CB  
14053 O  OG  . SER   H  130 ? 1.4360 0.6815 1.3002 -0.1970 -0.5218 -0.1489 131 SER   H OG  
14054 N  N   . LEU   H  131 ? 1.4055 0.4776 1.3580 -0.0279 -0.4171 -0.1069 132 LEU   H N   
14055 C  CA  . LEU   H  131 ? 1.4595 0.5010 1.3872 0.0110  -0.3972 -0.0804 132 LEU   H CA  
14056 C  C   . LEU   H  131 ? 1.4639 0.4315 1.3885 0.0203  -0.3541 -0.0691 132 LEU   H C   
14057 O  O   . LEU   H  131 ? 1.5528 0.3939 1.4197 0.1017  -0.3615 -0.0555 132 LEU   H O   
14058 C  CB  . LEU   H  131 ? 1.4176 0.4888 1.4442 0.0248  -0.3923 -0.0853 132 LEU   H CB  
14059 C  CG  . LEU   H  131 ? 1.4310 0.5351 1.4763 0.0335  -0.3566 -0.0589 132 LEU   H CG  
14060 C  CD1 . LEU   H  131 ? 1.4546 0.5650 1.4560 0.0293  -0.3437 -0.0330 132 LEU   H CD1 
14061 C  CD2 . LEU   H  131 ? 1.4041 0.5345 1.5033 0.0397  -0.3672 -0.0447 132 LEU   H CD2 
14062 N  N   . ALA   H  132 ? 1.4844 0.3855 1.3701 -0.0177 -0.3437 -0.0498 133 ALA   H N   
14063 C  CA  . ALA   H  132 ? 1.4943 0.4122 1.3996 0.0023  -0.3259 -0.0053 133 ALA   H CA  
14064 C  C   . ALA   H  132 ? 1.5253 0.4959 1.3843 -0.0058 -0.3511 -0.0190 133 ALA   H C   
14065 O  O   . ALA   H  132 ? 1.5519 0.4090 1.4768 0.0301  -0.3332 0.0813  133 ALA   H O   
14066 C  CB  . ALA   H  132 ? 1.4953 0.3866 1.3951 -0.0099 -0.3309 -0.0331 133 ALA   H CB  
14067 N  N   . ALA   H  133 ? 1.5404 0.5202 1.3788 0.0608  -0.3328 -0.0378 134 ALA   H N   
14068 C  CA  . ALA   H  133 ? 1.5257 0.5663 1.3346 0.0740  -0.3399 -0.0584 134 ALA   H CA  
14069 C  C   . ALA   H  133 ? 1.5311 0.5700 1.3247 0.0876  -0.3457 -0.0701 134 ALA   H C   
14070 O  O   . ALA   H  133 ? 1.5525 0.6418 1.3077 0.0860  -0.3444 -0.0977 134 ALA   H O   
14071 C  CB  . ALA   H  133 ? 1.5196 0.5723 1.3090 0.0546  -0.3236 -0.0441 134 ALA   H CB  
14072 N  N   . MET   H  134 ? 1.5326 0.5122 1.2739 0.0890  -0.3355 -0.0368 135 MET   H N   
14073 C  CA  . MET   H  134 ? 1.5622 0.5414 1.2669 0.0584  -0.3302 -0.0015 135 MET   H CA  
14074 C  C   . MET   H  134 ? 1.5348 0.5392 1.2946 0.0377  -0.3537 -0.0015 135 MET   H C   
14075 O  O   . MET   H  134 ? 1.5508 0.6643 1.3096 0.0037  -0.3385 -0.0596 135 MET   H O   
14076 C  CB  . MET   H  134 ? 1.5631 0.4570 1.2217 0.0856  -0.3253 0.0545  135 MET   H CB  
14077 C  CG  . MET   H  134 ? 1.5921 0.5098 1.2184 0.1157  -0.3220 0.1121  135 MET   H CG  
14078 S  SD  . MET   H  134 ? 1.6618 0.6342 1.1414 0.1445  -0.3632 0.0630  135 MET   H SD  
14079 C  CE  . MET   H  134 ? 1.6676 0.5994 1.1306 0.1069  -0.3304 0.0715  135 MET   H CE  
14080 N  N   . ALA   H  135 ? 1.5198 0.5926 1.3327 0.0300  -0.3558 -0.0601 136 ALA   H N   
14081 C  CA  . ALA   H  135 ? 1.5605 0.6295 1.3737 0.0348  -0.3650 -0.0160 136 ALA   H CA  
14082 C  C   . ALA   H  135 ? 1.5872 0.6101 1.3380 0.0101  -0.3666 -0.0061 136 ALA   H C   
14083 O  O   . ALA   H  135 ? 1.7005 0.6408 1.3494 0.0064  -0.3567 0.0293  136 ALA   H O   
14084 C  CB  . ALA   H  135 ? 1.5530 0.6799 1.3856 0.0518  -0.3528 -0.0416 136 ALA   H CB  
14085 N  N   . VAL   H  136 ? 1.5814 0.5941 1.3582 0.0114  -0.3569 -0.0144 137 VAL   H N   
14086 C  CA  . VAL   H  136 ? 1.5740 0.5922 1.3553 0.0056  -0.3543 0.0124  137 VAL   H CA  
14087 C  C   . VAL   H  136 ? 1.5612 0.5944 1.3000 0.0165  -0.4120 0.0334  137 VAL   H C   
14088 O  O   . VAL   H  136 ? 1.5867 0.5554 1.3267 -0.0104 -0.4392 0.0850  137 VAL   H O   
14089 C  CB  . VAL   H  136 ? 1.5582 0.5700 1.3562 -0.0030 -0.3385 -0.0272 137 VAL   H CB  
14090 C  CG1 . VAL   H  136 ? 1.5360 0.6438 1.3449 0.0046  -0.3537 -0.0391 137 VAL   H CG1 
14091 C  CG2 . VAL   H  136 ? 1.5750 0.5461 1.3842 -0.0043 -0.3155 -0.0189 137 VAL   H CG2 
14092 N  N   . LEU   H  137 ? 1.5493 0.6763 1.3341 0.0554  -0.3961 0.0531  138 LEU   H N   
14093 C  CA  . LEU   H  137 ? 1.5536 0.7262 1.2771 0.0759  -0.4008 0.0610  138 LEU   H CA  
14094 C  C   . LEU   H  137 ? 1.5529 0.7463 1.2789 0.0643  -0.4316 0.0938  138 LEU   H C   
14095 O  O   . LEU   H  137 ? 1.5463 0.7827 1.2280 0.1136  -0.4627 0.1968  138 LEU   H O   
14096 C  CB  . LEU   H  137 ? 1.5950 0.6839 1.2675 0.0855  -0.3715 0.0788  138 LEU   H CB  
14097 C  CG  . LEU   H  137 ? 1.5712 0.5882 1.2970 0.1119  -0.3742 0.0754  138 LEU   H CG  
14098 C  CD1 . LEU   H  137 ? 1.5793 0.5960 1.3073 0.1373  -0.3472 0.0791  138 LEU   H CD1 
14099 C  CD2 . LEU   H  137 ? 1.5455 0.5786 1.2579 0.1315  -0.3987 0.0874  138 LEU   H CD2 
14100 N  N   . GLU   H  138 ? 1.5710 0.7334 1.2853 0.0578  -0.4305 0.0770  139 GLU   H N   
14101 C  CA  . GLU   H  138 ? 1.5798 0.7421 1.3206 0.0387  -0.4103 0.0752  139 GLU   H CA  
14102 C  C   . GLU   H  138 ? 1.5870 0.7106 1.3774 0.0487  -0.4139 0.0646  139 GLU   H C   
14103 O  O   . GLU   H  138 ? 1.6494 0.7245 1.4393 0.0572  -0.3511 0.1590  139 GLU   H O   
14104 C  CB  . GLU   H  138 ? 1.5681 0.7601 1.3926 0.0192  -0.3792 0.0788  139 GLU   H CB  
14105 C  CG  . GLU   H  138 ? 1.5446 0.8198 1.4213 0.0209  -0.3664 0.0714  139 GLU   H CG  
14106 C  CD  . GLU   H  138 ? 1.5960 0.8250 1.4082 -0.0168 -0.3763 0.0178  139 GLU   H CD  
14107 O  OE1 . GLU   H  138 ? 1.5916 0.8464 1.5681 -0.0173 -0.3307 0.0134  139 GLU   H OE1 
14108 O  OE2 . GLU   H  138 ? 1.5842 0.8430 1.4305 -0.0262 -0.3873 -0.0034 139 GLU   H OE2 
14109 N  N   . SER   H  139 ? 1.5770 0.7356 1.3807 0.0170  -0.4205 0.0169  140 SER   H N   
14110 C  CA  . SER   H  139 ? 1.5946 0.7631 1.3934 0.0186  -0.4456 0.0361  140 SER   H CA  
14111 C  C   . SER   H  139 ? 1.6042 0.8562 1.3209 0.0175  -0.4840 0.0613  140 SER   H C   
14112 O  O   . SER   H  139 ? 1.6112 0.8842 1.2880 0.0077  -0.4826 0.0410  140 SER   H O   
14113 C  CB  . SER   H  139 ? 1.5591 0.7198 1.4677 0.0660  -0.4422 0.0421  140 SER   H CB  
14114 O  OG  . SER   H  139 ? 1.5479 0.7109 1.5288 0.0882  -0.4406 0.0199  140 SER   H OG  
14115 N  N   . HIS   H  140 ? 1.6348 0.8737 1.3187 -0.0092 -0.4907 0.0614  141 HIS   H N   
14116 C  CA  . HIS   H  140 ? 1.6428 0.9128 1.3193 -0.0078 -0.5239 0.0685  141 HIS   H CA  
14117 C  C   . HIS   H  140 ? 1.5904 0.9063 1.3037 -0.0384 -0.5375 0.0628  141 HIS   H C   
14118 O  O   . HIS   H  140 ? 1.6454 0.8708 1.3187 -0.0777 -0.5537 0.0992  141 HIS   H O   
14119 C  CB  . HIS   H  140 ? 1.6587 0.8987 1.3352 0.0239  -0.5084 0.0696  141 HIS   H CB  
14120 C  CG  . HIS   H  140 ? 1.7032 0.8763 1.4114 0.0603  -0.5131 0.1158  141 HIS   H CG  
14121 N  ND1 . HIS   H  140 ? 1.7365 0.8938 1.4198 0.0556  -0.5185 0.1336  141 HIS   H ND1 
14122 C  CD2 . HIS   H  140 ? 1.7426 0.8649 1.4391 0.0744  -0.4773 0.1121  141 HIS   H CD2 
14123 C  CE1 . HIS   H  140 ? 1.7661 0.8922 1.4774 0.0702  -0.5025 0.1336  141 HIS   H CE1 
14124 N  NE2 . HIS   H  140 ? 1.7684 0.8766 1.4869 0.0858  -0.4869 0.1449  141 HIS   H NE2 
14125 N  N   . TRP   H  141 ? 1.5958 0.8749 1.3080 -0.0209 -0.5089 0.0410  142 TRP   H N   
14126 C  CA  . TRP   H  141 ? 1.5927 0.8940 1.3429 -0.0302 -0.4895 0.0061  142 TRP   H CA  
14127 C  C   . TRP   H  141 ? 1.6395 0.8843 1.3512 -0.0048 -0.4825 0.0422  142 TRP   H C   
14128 O  O   . TRP   H  141 ? 1.6382 0.8708 1.4329 -0.0106 -0.4872 0.0479  142 TRP   H O   
14129 C  CB  . TRP   H  141 ? 1.5682 0.9812 1.2958 -0.0248 -0.4647 -0.0300 142 TRP   H CB  
14130 C  CG  . TRP   H  141 ? 1.5549 1.0599 1.2527 -0.0065 -0.4280 -0.0880 142 TRP   H CG  
14131 C  CD1 . TRP   H  141 ? 1.5294 1.0632 1.2736 -0.0249 -0.4097 -0.1012 142 TRP   H CD1 
14132 C  CD2 . TRP   H  141 ? 1.5609 1.1354 1.2362 -0.0044 -0.4390 -0.1036 142 TRP   H CD2 
14133 N  NE1 . TRP   H  141 ? 1.5076 1.1106 1.2247 -0.0491 -0.4243 -0.1296 142 TRP   H NE1 
14134 C  CE2 . TRP   H  141 ? 1.5346 1.1358 1.1806 -0.0280 -0.4347 -0.1318 142 TRP   H CE2 
14135 C  CE3 . TRP   H  141 ? 1.5584 1.1690 1.2281 -0.0112 -0.4241 -0.1134 142 TRP   H CE3 
14136 C  CZ2 . TRP   H  141 ? 1.5558 1.1530 1.1836 -0.0473 -0.4432 -0.1681 142 TRP   H CZ2 
14137 C  CZ3 . TRP   H  141 ? 1.5775 1.1830 1.2284 -0.0131 -0.4179 -0.1178 142 TRP   H CZ3 
14138 C  CH2 . TRP   H  141 ? 1.5906 1.1796 1.2159 -0.0271 -0.4135 -0.1427 142 TRP   H CH2 
14139 N  N   . LYS   H  142 ? 1.7086 0.9281 1.4346 -0.0058 -0.4614 -0.0233 143 LYS   H N   
14140 C  CA  . LYS   H  142 ? 1.7703 0.9256 1.4435 0.0311  -0.4519 -0.0370 143 LYS   H CA  
14141 C  C   . LYS   H  142 ? 1.8480 0.9585 1.4767 0.0558  -0.4740 -0.1268 143 LYS   H C   
14142 O  O   . LYS   H  142 ? 1.8577 0.7086 1.5352 0.1456  -0.4197 -0.2003 143 LYS   H O   
14143 C  CB  . LYS   H  142 ? 1.7581 0.9233 1.4515 0.0000  -0.4537 -0.0039 143 LYS   H CB  
14144 C  CG  . LYS   H  142 ? 1.7834 0.9078 1.5015 -0.0489 -0.4585 -0.0075 143 LYS   H CG  
14145 C  CD  . LYS   H  142 ? 1.8017 0.9368 1.5276 -0.0666 -0.4780 0.0145  143 LYS   H CD  
14146 C  CE  . LYS   H  142 ? 1.7851 1.0141 1.5912 -0.0687 -0.4881 0.0241  143 LYS   H CE  
14147 N  NZ  . LYS   H  142 ? 1.7819 1.0372 1.6207 -0.0982 -0.4887 0.0035  143 LYS   H NZ  
14148 N  N   . GLN   H  143 ? 1.9380 1.0925 1.4327 0.0957  -0.5217 -0.1484 144 GLN   H N   
14149 C  CA  . GLN   H  143 ? 2.0178 1.1696 1.4943 0.1598  -0.5054 -0.2274 144 GLN   H CA  
14150 C  C   . GLN   H  143 ? 2.0575 1.1131 1.5664 0.1219  -0.5069 -0.2355 144 GLN   H C   
14151 O  O   . GLN   H  143 ? 2.1035 1.1156 1.7233 0.1989  -0.4514 -0.2384 144 GLN   H O   
14152 C  CB  . GLN   H  143 ? 2.0148 1.4095 1.5123 0.1604  -0.4936 -0.1589 144 GLN   H CB  
14153 C  CG  . GLN   H  143 ? 2.0484 1.4909 1.5230 0.1706  -0.4412 -0.2371 144 GLN   H CG  
14154 C  CD  . GLN   H  143 ? 2.0545 1.5576 1.4872 0.1373  -0.4499 -0.2285 144 GLN   H CD  
14155 O  OE1 . GLN   H  143 ? 2.1325 1.6379 1.5176 0.0055  -0.3559 -0.2686 144 GLN   H OE1 
14156 N  NE2 . GLN   H  143 ? 2.0976 1.4980 1.4307 0.1414  -0.4684 -0.2709 144 GLN   H NE2 
14157 N  N   . ASP   H  144 ? 2.0775 1.1236 1.5105 0.0007  -0.4855 -0.2766 145 ASP   H N   
14158 C  CA  . ASP   H  144 ? 2.0561 1.1040 1.4662 0.0006  -0.4260 -0.2664 145 ASP   H CA  
14159 C  C   . ASP   H  144 ? 1.9353 0.9302 1.4551 0.0001  -0.4920 -0.2534 145 ASP   H C   
14160 O  O   . ASP   H  144 ? 1.9072 0.9055 1.4861 0.0299  -0.4597 -0.2643 145 ASP   H O   
14161 C  CB  . ASP   H  144 ? 2.2391 1.2572 1.4791 -0.0630 -0.4826 -0.2687 145 ASP   H CB  
14162 C  CG  . ASP   H  144 ? 2.4216 1.2311 1.4556 -0.0632 -0.4642 -0.3360 145 ASP   H CG  
14163 O  OD1 . ASP   H  144 ? 2.5944 1.0881 1.2700 -0.1945 -0.4903 -0.4754 145 ASP   H OD1 
14164 O  OD2 . ASP   H  144 ? 2.6191 1.5961 1.5459 -0.2031 -0.3614 -0.2574 145 ASP   H OD2 
14165 N  N   . LEU   H  145 ? 1.8746 0.8121 1.4380 -0.0279 -0.4604 -0.3313 146 LEU   H N   
14166 C  CA  . LEU   H  145 ? 1.8165 0.7675 1.5579 -0.0467 -0.4414 -0.3699 146 LEU   H CA  
14167 C  C   . LEU   H  145 ? 1.7312 0.8077 1.4906 -0.0655 -0.4655 -0.4497 146 LEU   H C   
14168 O  O   . LEU   H  145 ? 1.8284 0.8200 1.4660 -0.1548 -0.4875 -0.5196 146 LEU   H O   
14169 C  CB  . LEU   H  145 ? 1.8203 0.7426 1.5932 -0.0487 -0.4575 -0.3886 146 LEU   H CB  
14170 C  CG  . LEU   H  145 ? 1.8085 0.6886 1.6331 0.0105  -0.4481 -0.3536 146 LEU   H CG  
14171 C  CD1 . LEU   H  145 ? 1.8214 0.7316 1.6069 0.0055  -0.4493 -0.3578 146 LEU   H CD1 
14172 C  CD2 . LEU   H  145 ? 1.8519 0.6422 1.6607 0.0280  -0.4529 -0.3510 146 LEU   H CD2 
14173 N  N   . THR   H  146 ? 1.6990 0.7018 1.4924 -0.1108 -0.4665 -0.4223 147 THR   H N   
14174 C  CA  . THR   H  146 ? 1.6463 0.7620 1.5026 -0.1109 -0.4417 -0.3875 147 THR   H CA  
14175 C  C   . THR   H  146 ? 1.6164 0.8163 1.5169 -0.1260 -0.4158 -0.3364 147 THR   H C   
14176 O  O   . THR   H  146 ? 1.5371 0.6099 1.5332 -0.1124 -0.3913 -0.2229 147 THR   H O   
14177 C  CB  . THR   H  146 ? 1.6450 0.7522 1.4842 -0.1173 -0.4471 -0.3986 147 THR   H CB  
14178 O  OG1 . THR   H  146 ? 1.6325 0.7012 1.5747 -0.2027 -0.4571 -0.4032 147 THR   H OG1 
14179 C  CG2 . THR   H  146 ? 1.6578 0.8242 1.4851 -0.1029 -0.4343 -0.3749 147 THR   H CG2 
14180 N  N   . LYS   H  147 ? 1.6276 0.9398 1.5451 -0.1659 -0.3494 -0.2740 148 LYS   H N   
14181 C  CA  . LYS   H  147 ? 1.6069 1.0435 1.5510 -0.1399 -0.3522 -0.2507 148 LYS   H CA  
14182 C  C   . LYS   H  147 ? 1.6144 1.0688 1.5931 -0.1055 -0.3525 -0.2530 148 LYS   H C   
14183 O  O   . LYS   H  147 ? 1.6221 1.1250 1.6298 -0.1324 -0.3315 -0.3165 148 LYS   H O   
14184 C  CB  . LYS   H  147 ? 1.5939 1.0006 1.5504 -0.0842 -0.3152 -0.1958 148 LYS   H CB  
14185 C  CG  . LYS   H  147 ? 1.5633 0.9888 1.6076 -0.0635 -0.3031 -0.1165 148 LYS   H CG  
14186 C  CD  . LYS   H  147 ? 1.5460 1.0648 1.6900 -0.0770 -0.2758 -0.0471 148 LYS   H CD  
14187 C  CE  . LYS   H  147 ? 1.5483 1.0979 1.7409 -0.1017 -0.2278 0.0049  148 LYS   H CE  
14188 N  NZ  . LYS   H  147 ? 1.5874 1.0980 1.8410 -0.1208 -0.2155 -0.0045 148 LYS   H NZ  
14189 N  N   . GLU   H  148 ? 1.6578 0.9938 1.6229 -0.0984 -0.3890 -0.2031 149 GLU   H N   
14190 C  CA  . GLU   H  148 ? 1.6771 0.9012 1.6121 -0.1012 -0.4108 -0.1711 149 GLU   H CA  
14191 C  C   . GLU   H  148 ? 1.6865 0.8586 1.4940 -0.0550 -0.4114 -0.1364 149 GLU   H C   
14192 O  O   . GLU   H  148 ? 1.6537 0.6599 1.5537 -0.0909 -0.4189 -0.0991 149 GLU   H O   
14193 C  CB  . GLU   H  148 ? 1.6815 1.0201 1.7174 -0.0835 -0.4237 -0.1627 149 GLU   H CB  
14194 C  CG  . GLU   H  148 ? 1.7288 1.0962 1.8395 -0.1184 -0.3611 -0.1349 149 GLU   H CG  
14195 C  CD  . GLU   H  148 ? 1.7982 1.1498 1.9123 -0.1566 -0.3412 -0.2051 149 GLU   H CD  
14196 O  OE1 . GLU   H  148 ? 1.8505 1.2085 2.0876 -0.2789 -0.2481 -0.2084 149 GLU   H OE1 
14197 O  OE2 . GLU   H  148 ? 1.8220 1.2130 1.8120 -0.1673 -0.4442 -0.2350 149 GLU   H OE2 
14198 N  N   . GLU   H  149 ? 1.7133 0.8182 1.4480 -0.0394 -0.4373 -0.1180 150 GLU   H N   
14199 C  CA  . GLU   H  149 ? 1.7422 0.7399 1.4400 0.0125  -0.4412 -0.1098 150 GLU   H CA  
14200 C  C   . GLU   H  149 ? 1.7405 0.7461 1.4335 0.0420  -0.4323 -0.0600 150 GLU   H C   
14201 O  O   . GLU   H  149 ? 1.7640 0.6673 1.4124 0.0146  -0.4644 0.0296  150 GLU   H O   
14202 C  CB  . GLU   H  149 ? 1.7682 0.7337 1.4518 0.0064  -0.4317 -0.0907 150 GLU   H CB  
14203 C  CG  . GLU   H  149 ? 1.7708 0.8154 1.5247 0.0342  -0.4315 -0.0518 150 GLU   H CG  
14204 C  CD  . GLU   H  149 ? 1.8297 0.9406 1.5494 0.0272  -0.3937 -0.0082 150 GLU   H CD  
14205 O  OE1 . GLU   H  149 ? 1.8827 0.9278 1.5144 0.0713  -0.3561 0.0765  150 GLU   H OE1 
14206 O  OE2 . GLU   H  149 ? 1.8195 1.0555 1.5329 0.0288  -0.4179 0.0599  150 GLU   H OE2 
14207 N  N   . ALA   H  150 ? 1.7029 0.8021 1.3822 0.0717  -0.4523 -0.0974 151 ALA   H N   
14208 C  CA  . ALA   H  150 ? 1.6846 0.8126 1.3671 0.0431  -0.4484 -0.1421 151 ALA   H CA  
14209 C  C   . ALA   H  150 ? 1.6065 0.7651 1.3744 0.0297  -0.4351 -0.1830 151 ALA   H C   
14210 O  O   . ALA   H  150 ? 1.7139 0.6338 1.3178 0.0574  -0.4060 -0.2560 151 ALA   H O   
14211 C  CB  . ALA   H  150 ? 1.7013 0.8113 1.3693 0.0364  -0.4577 -0.1599 151 ALA   H CB  
14212 N  N   . ILE   H  151 ? 1.5676 0.8286 1.3595 0.0406  -0.4383 -0.1694 152 ILE   H N   
14213 C  CA  . ILE   H  151 ? 1.5097 0.8389 1.3536 0.0380  -0.4487 -0.1262 152 ILE   H CA  
14214 C  C   . ILE   H  151 ? 1.4788 0.8107 1.4246 0.0475  -0.4456 -0.0659 152 ILE   H C   
14215 O  O   . ILE   H  151 ? 1.4091 0.8347 1.3842 0.1008  -0.4978 0.0336  152 ILE   H O   
14216 C  CB  . ILE   H  151 ? 1.5137 0.8683 1.3454 0.0288  -0.4441 -0.1260 152 ILE   H CB  
14217 C  CG1 . ILE   H  151 ? 1.5575 0.8743 1.3175 0.0580  -0.4279 -0.1029 152 ILE   H CG1 
14218 C  CG2 . ILE   H  151 ? 1.4891 0.8693 1.3633 0.0170  -0.4308 -0.1331 152 ILE   H CG2 
14219 C  CD1 . ILE   H  151 ? 1.5574 0.9013 1.3312 0.0493  -0.4025 -0.0868 152 ILE   H CD1 
14220 N  N   . LYS   H  152 ? 1.4751 0.7323 1.4463 0.0427  -0.4420 -0.0836 153 LYS   H N   
14221 C  CA  . LYS   H  152 ? 1.4651 0.7150 1.4742 0.0037  -0.4206 -0.1060 153 LYS   H CA  
14222 C  C   . LYS   H  152 ? 1.4783 0.5679 1.5012 0.0294  -0.3628 -0.0988 153 LYS   H C   
14223 O  O   . LYS   H  152 ? 1.4854 0.4938 1.5515 -0.0366 -0.3361 -0.0980 153 LYS   H O   
14224 C  CB  . LYS   H  152 ? 1.4967 0.7179 1.4826 -0.0064 -0.4473 -0.1065 153 LYS   H CB  
14225 C  CG  . LYS   H  152 ? 1.4970 0.7752 1.5297 -0.0021 -0.4425 -0.1260 153 LYS   H CG  
14226 C  CD  . LYS   H  152 ? 1.5293 0.7948 1.5831 -0.0267 -0.4432 -0.1437 153 LYS   H CD  
14227 C  CE  . LYS   H  152 ? 1.5467 0.8275 1.6391 0.0155  -0.4304 -0.1275 153 LYS   H CE  
14228 N  NZ  . LYS   H  152 ? 1.5789 0.8107 1.6879 0.0323  -0.4213 -0.0727 153 LYS   H NZ  
14229 N  N   . LEU   H  153 ? 1.4719 0.5400 1.4802 0.0596  -0.3759 -0.0793 154 LEU   H N   
14230 C  CA  . LEU   H  153 ? 1.4412 0.5578 1.4683 0.0815  -0.3858 -0.0709 154 LEU   H CA  
14231 C  C   . LEU   H  153 ? 1.4183 0.5442 1.4707 0.0790  -0.3783 -0.0676 154 LEU   H C   
14232 O  O   . LEU   H  153 ? 1.3900 0.5634 1.4681 0.1121  -0.3982 -0.0835 154 LEU   H O   
14233 C  CB  . LEU   H  153 ? 1.4520 0.6098 1.4524 0.1115  -0.3914 -0.0492 154 LEU   H CB  
14234 C  CG  . LEU   H  153 ? 1.4462 0.6484 1.4710 0.1151  -0.3937 -0.0597 154 LEU   H CG  
14235 C  CD1 . LEU   H  153 ? 1.4676 0.6505 1.4987 0.1262  -0.3968 -0.0718 154 LEU   H CD1 
14236 C  CD2 . LEU   H  153 ? 1.4642 0.7250 1.4457 0.1279  -0.3989 -0.0407 154 LEU   H CD2 
14237 N  N   . ALA   H  154 ? 1.4077 0.5518 1.4255 0.0200  -0.4018 -0.0403 155 ALA   H N   
14238 C  CA  . ALA   H  154 ? 1.3713 0.5744 1.4087 0.0061  -0.3887 -0.0401 155 ALA   H CA  
14239 C  C   . ALA   H  154 ? 1.3778 0.5030 1.4249 0.0237  -0.3689 -0.0123 155 ALA   H C   
14240 O  O   . ALA   H  154 ? 1.3313 0.4626 1.4697 -0.0049 -0.3563 0.0307  155 ALA   H O   
14241 C  CB  . ALA   H  154 ? 1.3526 0.5746 1.4126 0.0297  -0.3828 -0.0544 155 ALA   H CB  
14242 N  N   . SER   H  155 ? 1.3648 0.5061 1.4113 0.0637  -0.3942 -0.0238 156 SER   H N   
14243 C  CA  . SER   H  155 ? 1.3589 0.6294 1.4220 0.0976  -0.3851 -0.0257 156 SER   H CA  
14244 C  C   . SER   H  155 ? 1.4389 0.6395 1.4205 0.0948  -0.3528 -0.0650 156 SER   H C   
14245 O  O   . SER   H  155 ? 1.5463 0.7832 1.4205 0.1098  -0.2432 -0.1201 156 SER   H O   
14246 C  CB  . SER   H  155 ? 1.3266 0.6085 1.4215 0.1289  -0.4229 -0.0031 156 SER   H CB  
14247 O  OG  . SER   H  155 ? 1.3092 0.7009 1.4690 0.1121  -0.4558 0.0204  156 SER   H OG  
14248 N  N   . ASP   H  156 ? 1.4679 0.7606 1.4148 0.0811  -0.3699 -0.0391 157 ASP   H N   
14249 C  CA  . ASP   H  156 ? 1.4421 0.7522 1.5143 0.0530  -0.3703 -0.1151 157 ASP   H CA  
14250 C  C   . ASP   H  156 ? 1.4315 0.7141 1.4737 0.0494  -0.3643 -0.0714 157 ASP   H C   
14251 O  O   . ASP   H  156 ? 1.4106 0.7827 1.5060 -0.0076 -0.3854 -0.1096 157 ASP   H O   
14252 C  CB  . ASP   H  156 ? 1.5079 0.8201 1.5230 0.0481  -0.3542 -0.1007 157 ASP   H CB  
14253 C  CG  . ASP   H  156 ? 1.4996 0.9265 1.6507 0.0263  -0.3520 -0.1478 157 ASP   H CG  
14254 O  OD1 . ASP   H  156 ? 1.5182 1.0691 1.6679 0.0207  -0.2754 -0.2459 157 ASP   H OD1 
14255 O  OD2 . ASP   H  156 ? 1.4964 0.9340 1.7216 -0.0282 -0.3941 -0.0853 157 ASP   H OD2 
14256 N  N   . ALA   H  157 ? 1.4337 0.6336 1.4154 0.0243  -0.3800 -0.0831 158 ALA   H N   
14257 C  CA  . ALA   H  157 ? 1.4244 0.6532 1.3974 0.0299  -0.3490 -0.0531 158 ALA   H CA  
14258 C  C   . ALA   H  157 ? 1.4387 0.6867 1.3871 0.0601  -0.3205 -0.0421 158 ALA   H C   
14259 O  O   . ALA   H  157 ? 1.4193 0.5968 1.2600 0.1064  -0.3346 0.0229  158 ALA   H O   
14260 C  CB  . ALA   H  157 ? 1.4519 0.6332 1.4030 0.0121  -0.3388 -0.0647 158 ALA   H CB  
14261 N  N   . ILE   H  158 ? 1.4081 0.7661 1.3666 0.0382  -0.2919 -0.0399 159 ILE   H N   
14262 C  CA  . ILE   H  158 ? 1.3951 0.8345 1.3658 0.0331  -0.2782 -0.0490 159 ILE   H CA  
14263 C  C   . ILE   H  158 ? 1.3496 0.8681 1.3951 0.0666  -0.2892 -0.0451 159 ILE   H C   
14264 O  O   . ILE   H  158 ? 1.3668 0.9232 1.4024 0.0282  -0.2488 -0.0918 159 ILE   H O   
14265 C  CB  . ILE   H  158 ? 1.3774 0.8447 1.3905 0.0170  -0.2603 -0.0646 159 ILE   H CB  
14266 C  CG1 . ILE   H  158 ? 1.4162 0.8550 1.3714 0.0244  -0.2675 -0.0765 159 ILE   H CG1 
14267 C  CG2 . ILE   H  158 ? 1.3474 0.8592 1.3934 0.0071  -0.2299 -0.0849 159 ILE   H CG2 
14268 C  CD1 . ILE   H  158 ? 1.4213 0.8606 1.3757 0.0104  -0.2748 -0.0632 159 ILE   H CD1 
14269 N  N   . GLN   H  159 ? 1.3502 0.8721 1.4111 0.0365  -0.3140 -0.0091 160 GLN   H N   
14270 C  CA  . GLN   H  159 ? 1.3832 0.8274 1.4187 0.0323  -0.3172 0.0111  160 GLN   H CA  
14271 C  C   . GLN   H  159 ? 1.3817 0.8304 1.3776 0.0315  -0.3031 -0.0034 160 GLN   H C   
14272 O  O   . GLN   H  159 ? 1.3238 0.8734 1.4307 0.0085  -0.2759 -0.0564 160 GLN   H O   
14273 C  CB  . GLN   H  159 ? 1.3980 0.7685 1.4869 0.0341  -0.3378 0.0828  160 GLN   H CB  
14274 C  CG  . GLN   H  159 ? 1.4046 0.7550 1.5369 0.0451  -0.3485 0.1320  160 GLN   H CG  
14275 C  CD  . GLN   H  159 ? 1.4239 0.7080 1.5624 0.0426  -0.3583 0.1965  160 GLN   H CD  
14276 O  OE1 . GLN   H  159 ? 1.5139 0.6146 1.6080 -0.0512 -0.3398 0.1584  160 GLN   H OE1 
14277 N  NE2 . GLN   H  159 ? 1.4298 0.7101 1.5392 0.0155  -0.3894 0.2565  160 GLN   H NE2 
14278 N  N   . ALA   H  160 ? 1.4489 0.8242 1.3175 0.0562  -0.3248 0.0219  161 ALA   H N   
14279 C  CA  . ALA   H  160 ? 1.5154 0.7247 1.3478 0.0966  -0.3423 0.0465  161 ALA   H CA  
14280 C  C   . ALA   H  160 ? 1.5460 0.6546 1.3410 0.1053  -0.3416 -0.0159 161 ALA   H C   
14281 O  O   . ALA   H  160 ? 1.5949 0.5524 1.4236 0.1285  -0.3229 0.0341  161 ALA   H O   
14282 C  CB  . ALA   H  160 ? 1.5175 0.7392 1.3326 0.1088  -0.3548 0.0715  161 ALA   H CB  
14283 N  N   . GLY   H  161 ? 1.5803 0.6737 1.3899 0.1177  -0.3231 0.0245  162 GLY   H N   
14284 C  CA  . GLY   H  161 ? 1.5610 0.5763 1.3758 0.0961  -0.3142 0.0162  162 GLY   H CA  
14285 C  C   . GLY   H  161 ? 1.4971 0.4882 1.4035 0.0869  -0.3124 0.0086  162 GLY   H C   
14286 O  O   . GLY   H  161 ? 1.5034 0.2912 1.5132 0.0490  -0.3016 0.0474  162 GLY   H O   
14287 N  N   . ILE   H  162 ? 1.4632 0.5242 1.4013 0.1009  -0.2911 -0.0203 163 ILE   H N   
14288 C  CA  . ILE   H  162 ? 1.4169 0.5328 1.4411 0.1034  -0.2785 -0.0542 163 ILE   H CA  
14289 C  C   . ILE   H  162 ? 1.4181 0.5183 1.5089 0.1111  -0.2223 -0.0258 163 ILE   H C   
14290 O  O   . ILE   H  162 ? 1.4086 0.3120 1.4930 0.1680  -0.1440 -0.0151 163 ILE   H O   
14291 C  CB  . ILE   H  162 ? 1.4063 0.6458 1.4503 0.0913  -0.3186 -0.0824 163 ILE   H CB  
14292 C  CG1 . ILE   H  162 ? 1.4411 0.6587 1.5060 0.1205  -0.3193 -0.0658 163 ILE   H CG1 
14293 C  CG2 . ILE   H  162 ? 1.3903 0.6676 1.4309 0.0849  -0.3351 -0.0980 163 ILE   H CG2 
14294 C  CD1 . ILE   H  162 ? 1.4439 0.6868 1.5704 0.0993  -0.3250 -0.0491 163 ILE   H CD1 
14295 N  N   . TRP   H  163 ? 1.4015 0.5028 1.4916 0.0781  -0.2466 -0.0461 164 TRP   H N   
14296 C  CA  . TRP   H  163 ? 1.3812 0.5085 1.5429 0.0741  -0.2528 -0.0732 164 TRP   H CA  
14297 C  C   . TRP   H  163 ? 1.4115 0.4606 1.6056 0.0667  -0.2228 -0.0843 164 TRP   H C   
14298 O  O   . TRP   H  163 ? 1.3765 0.2991 1.7329 0.0275  -0.1558 -0.0659 164 TRP   H O   
14299 C  CB  . TRP   H  163 ? 1.3712 0.5323 1.5444 0.0495  -0.2626 -0.0649 164 TRP   H CB  
14300 C  CG  . TRP   H  163 ? 1.3882 0.5230 1.5145 0.0331  -0.2603 -0.0613 164 TRP   H CG  
14301 C  CD1 . TRP   H  163 ? 1.3704 0.5418 1.5276 -0.0066 -0.2834 -0.0568 164 TRP   H CD1 
14302 C  CD2 . TRP   H  163 ? 1.3580 0.5398 1.5310 0.0008  -0.2678 -0.0727 164 TRP   H CD2 
14303 N  NE1 . TRP   H  163 ? 1.3283 0.6465 1.5051 -0.0107 -0.2964 -0.0583 164 TRP   H NE1 
14304 C  CE2 . TRP   H  163 ? 1.3354 0.6099 1.5095 -0.0055 -0.2850 -0.0604 164 TRP   H CE2 
14305 C  CE3 . TRP   H  163 ? 1.3457 0.5490 1.5329 -0.0051 -0.2474 -0.0688 164 TRP   H CE3 
14306 C  CZ2 . TRP   H  163 ? 1.3442 0.6516 1.5051 -0.0039 -0.2774 -0.0437 164 TRP   H CZ2 
14307 C  CZ3 . TRP   H  163 ? 1.3395 0.5750 1.5321 -0.0092 -0.2480 -0.0739 164 TRP   H CZ3 
14308 C  CH2 . TRP   H  163 ? 1.3410 0.6143 1.5213 -0.0083 -0.2627 -0.0740 164 TRP   H CH2 
14309 N  N   . ASN   H  164 ? 1.4393 0.5058 1.5294 0.0380  -0.2351 -0.1089 165 ASN   H N   
14310 C  CA  . ASN   H  164 ? 1.4740 0.5170 1.4970 -0.0020 -0.3077 -0.1547 165 ASN   H CA  
14311 C  C   . ASN   H  164 ? 1.4948 0.5651 1.4751 -0.0281 -0.3324 -0.1321 165 ASN   H C   
14312 O  O   . ASN   H  164 ? 1.4133 0.6065 1.3976 0.0059  -0.3835 -0.1174 165 ASN   H O   
14313 C  CB  . ASN   H  164 ? 1.5070 0.5931 1.4601 -0.0146 -0.3412 -0.2085 165 ASN   H CB  
14314 C  CG  . ASN   H  164 ? 1.5341 0.5897 1.4623 0.0383  -0.3356 -0.2108 165 ASN   H CG  
14315 O  OD1 . ASN   H  164 ? 1.5796 0.8458 1.4266 -0.0178 -0.3932 -0.2183 165 ASN   H OD1 
14316 N  ND2 . ASN   H  164 ? 1.5388 0.5817 1.4069 0.0336  -0.3500 -0.2162 165 ASN   H ND2 
14317 N  N   . ASP   H  165 ? 1.5029 0.6168 1.4419 0.0511  -0.3939 -0.1027 166 ASP   H N   
14318 C  CA  . ASP   H  165 ? 1.5284 0.7629 1.3735 0.0302  -0.4263 -0.1258 166 ASP   H CA  
14319 C  C   . ASP   H  165 ? 1.5660 0.6915 1.3609 0.0361  -0.4338 -0.1309 166 ASP   H C   
14320 O  O   . ASP   H  165 ? 1.6495 0.4781 1.2151 0.0295  -0.5017 -0.0349 166 ASP   H O   
14321 C  CB  . ASP   H  165 ? 1.5432 0.7945 1.3761 0.0414  -0.4118 -0.1304 166 ASP   H CB  
14322 C  CG  . ASP   H  165 ? 1.5545 0.8609 1.3434 0.0218  -0.4161 -0.0970 166 ASP   H CG  
14323 O  OD1 . ASP   H  165 ? 1.5207 0.9712 1.3639 0.0151  -0.3988 -0.1693 166 ASP   H OD1 
14324 O  OD2 . ASP   H  165 ? 1.5741 0.8381 1.3057 -0.0373 -0.4209 -0.0433 166 ASP   H OD2 
14325 N  N   . LEU   H  166 ? 1.5880 0.6550 1.3836 0.0397  -0.4177 -0.1772 167 LEU   H N   
14326 C  CA  . LEU   H  166 ? 1.5702 0.6471 1.3875 0.0424  -0.4070 -0.1942 167 LEU   H CA  
14327 C  C   . LEU   H  166 ? 1.5872 0.5921 1.4151 -0.0011 -0.4040 -0.2420 167 LEU   H C   
14328 O  O   . LEU   H  166 ? 1.5834 0.4100 1.4333 -0.0049 -0.3919 -0.2778 167 LEU   H O   
14329 C  CB  . LEU   H  166 ? 1.5399 0.6259 1.4053 0.0571  -0.4080 -0.1899 167 LEU   H CB  
14330 C  CG  . LEU   H  166 ? 1.5150 0.6425 1.4286 0.1137  -0.3883 -0.1989 167 LEU   H CG  
14331 C  CD1 . LEU   H  166 ? 1.4966 0.6134 1.4442 0.1435  -0.3759 -0.2193 167 LEU   H CD1 
14332 C  CD2 . LEU   H  166 ? 1.5134 0.6605 1.4194 0.1072  -0.3673 -0.2136 167 LEU   H CD2 
14333 N  N   . GLY   H  167 ? 1.5577 0.6284 1.4322 -0.0321 -0.3946 -0.2492 168 GLY   H N   
14334 C  CA  . GLY   H  167 ? 1.5290 0.6210 1.4325 -0.0664 -0.3990 -0.2218 168 GLY   H CA  
14335 C  C   . GLY   H  167 ? 1.5472 0.5648 1.4509 -0.0858 -0.3686 -0.1641 168 GLY   H C   
14336 O  O   . GLY   H  167 ? 1.4769 0.4809 1.4645 -0.1948 -0.4153 -0.2353 168 GLY   H O   
14337 N  N   . SER   H  168 ? 1.5056 0.6033 1.4792 -0.0697 -0.3582 -0.1673 169 SER   H N   
14338 C  CA  . SER   H  168 ? 1.4906 0.5623 1.4563 -0.0644 -0.3535 -0.1290 169 SER   H CA  
14339 C  C   . SER   H  168 ? 1.4654 0.7900 1.4751 -0.0572 -0.3605 -0.1421 169 SER   H C   
14340 O  O   . SER   H  168 ? 1.4537 0.8116 1.4563 -0.0719 -0.3841 -0.1552 169 SER   H O   
14341 C  CB  . SER   H  168 ? 1.5418 0.5193 1.4556 -0.0688 -0.3515 -0.0650 169 SER   H CB  
14342 O  OG  . SER   H  168 ? 1.5576 0.5009 1.4689 -0.1005 -0.3400 -0.0404 169 SER   H OG  
14343 N  N   . GLY   H  169 ? 1.4791 0.6596 1.5111 -0.0006 -0.3692 -0.1483 170 GLY   H N   
14344 C  CA  . GLY   H  169 ? 1.4753 0.7032 1.5655 -0.0022 -0.3773 -0.1542 170 GLY   H CA  
14345 C  C   . GLY   H  169 ? 1.4804 0.6594 1.5770 0.0216  -0.3913 -0.1823 170 GLY   H C   
14346 O  O   . GLY   H  169 ? 1.3732 0.5675 1.5749 -0.0857 -0.4101 -0.1651 170 GLY   H O   
14347 N  N   . SER   H  170 ? 1.4863 0.7302 1.5774 0.0397  -0.4006 -0.1690 171 SER   H N   
14348 C  CA  . SER   H  170 ? 1.5332 0.7042 1.5804 0.0467  -0.3819 -0.1501 171 SER   H CA  
14349 C  C   . SER   H  170 ? 1.5984 0.6926 1.5878 0.0906  -0.3956 -0.1614 171 SER   H C   
14350 O  O   . SER   H  170 ? 1.6985 0.7005 1.7229 0.1283  -0.4175 -0.1180 171 SER   H O   
14351 C  CB  . SER   H  170 ? 1.5619 0.7391 1.5216 0.0923  -0.3661 -0.1690 171 SER   H CB  
14352 O  OG  . SER   H  170 ? 1.6260 0.7928 1.4936 0.1195  -0.3248 -0.1684 171 SER   H OG  
14353 N  N   . ASN   H  171 ? 1.5540 0.6610 1.5225 0.1058  -0.3990 -0.0826 172 ASN   H N   
14354 C  CA  . ASN   H  171 ? 1.5644 0.5648 1.4888 0.0764  -0.3777 -0.0385 172 ASN   H CA  
14355 C  C   . ASN   H  171 ? 1.5366 0.5720 1.4414 0.0573  -0.3964 0.0082  172 ASN   H C   
14356 O  O   . ASN   H  171 ? 1.5388 0.5467 1.3303 0.0867  -0.4850 0.0904  172 ASN   H O   
14357 C  CB  . ASN   H  171 ? 1.5689 0.5852 1.4433 0.0529  -0.3421 -0.0697 172 ASN   H CB  
14358 C  CG  . ASN   H  171 ? 1.5757 0.5652 1.4642 0.0523  -0.3191 -0.0851 172 ASN   H CG  
14359 O  OD1 . ASN   H  171 ? 1.6008 0.6507 1.4138 0.0340  -0.2616 -0.0716 172 ASN   H OD1 
14360 N  ND2 . ASN   H  171 ? 1.5629 0.5530 1.4535 0.0402  -0.3148 -0.0634 172 ASN   H ND2 
14361 N  N   . VAL   H  172 ? 1.5543 0.6200 1.4383 0.0325  -0.3721 -0.0112 173 VAL   H N   
14362 C  CA  . VAL   H  172 ? 1.5437 0.7487 1.4471 0.0425  -0.3621 -0.0318 173 VAL   H CA  
14363 C  C   . VAL   H  172 ? 1.5299 0.7676 1.5002 0.0278  -0.3312 -0.0932 173 VAL   H C   
14364 O  O   . VAL   H  172 ? 1.5183 0.8712 1.5463 0.0243  -0.3358 -0.1321 173 VAL   H O   
14365 C  CB  . VAL   H  172 ? 1.5139 0.7791 1.4315 0.0338  -0.3936 -0.0577 173 VAL   H CB  
14366 C  CG1 . VAL   H  172 ? 1.5266 0.7732 1.4154 0.0378  -0.4082 -0.0685 173 VAL   H CG1 
14367 C  CG2 . VAL   H  172 ? 1.5018 0.7803 1.4441 0.0620  -0.4093 -0.0555 173 VAL   H CG2 
14368 N  N   . ASP   H  173 ? 1.5284 0.8100 1.5155 0.0442  -0.3109 -0.1152 174 ASP   H N   
14369 C  CA  . ASP   H  173 ? 1.5154 0.8123 1.4813 -0.0155 -0.2990 -0.1381 174 ASP   H CA  
14370 C  C   . ASP   H  173 ? 1.4770 0.7409 1.4672 0.0127  -0.3254 -0.1332 174 ASP   H C   
14371 O  O   . ASP   H  173 ? 1.4264 0.6801 1.3565 0.0635  -0.3553 -0.1416 174 ASP   H O   
14372 C  CB  . ASP   H  173 ? 1.5627 0.8088 1.4692 -0.0070 -0.2873 -0.1284 174 ASP   H CB  
14373 C  CG  . ASP   H  173 ? 1.6172 0.8589 1.4886 -0.0389 -0.2528 -0.1349 174 ASP   H CG  
14374 O  OD1 . ASP   H  173 ? 1.5489 0.8327 1.5226 -0.1314 -0.2701 -0.1550 174 ASP   H OD1 
14375 O  OD2 . ASP   H  173 ? 1.6954 0.8804 1.4861 0.0189  -0.2517 -0.1083 174 ASP   H OD2 
14376 N  N   . VAL   H  174 ? 1.4978 0.7891 1.4826 -0.0058 -0.3298 -0.1519 175 VAL   H N   
14377 C  CA  . VAL   H  174 ? 1.5787 0.8283 1.4851 0.0032  -0.2879 -0.1222 175 VAL   H CA  
14378 C  C   . VAL   H  174 ? 1.5820 0.8379 1.5003 0.0563  -0.2920 -0.1400 175 VAL   H C   
14379 O  O   . VAL   H  174 ? 1.6436 0.7038 1.5891 0.0704  -0.2792 -0.1207 175 VAL   H O   
14380 C  CB  . VAL   H  174 ? 1.5762 0.8534 1.4805 -0.0298 -0.2818 -0.0941 175 VAL   H CB  
14381 C  CG1 . VAL   H  174 ? 1.6372 0.9467 1.4546 -0.0527 -0.2678 -0.0680 175 VAL   H CG1 
14382 C  CG2 . VAL   H  174 ? 1.5445 0.8436 1.4916 -0.0565 -0.2616 -0.0904 175 VAL   H CG2 
14383 N  N   . CYS   H  175 ? 1.5692 0.7858 1.5146 0.0869  -0.3216 -0.1659 176 CYS   H N   
14384 C  CA  . CYS   H  175 ? 1.5448 0.7978 1.5217 0.0949  -0.3072 -0.1878 176 CYS   H CA  
14385 C  C   . CYS   H  175 ? 1.4984 0.7319 1.5199 0.0800  -0.3172 -0.1883 176 CYS   H C   
14386 O  O   . CYS   H  175 ? 1.4527 0.5669 1.5125 0.1430  -0.3203 -0.1979 176 CYS   H O   
14387 C  CB  . CYS   H  175 ? 1.5072 0.8025 1.5452 0.1010  -0.2788 -0.2040 176 CYS   H CB  
14388 S  SG  . CYS   H  175 ? 1.5624 0.7863 1.6263 0.0679  -0.2116 -0.1622 176 CYS   H SG  
14389 N  N   . VAL   H  176 ? 1.5582 0.8197 1.5289 0.0527  -0.3596 -0.2032 177 VAL   H N   
14390 C  CA  . VAL   H  176 ? 1.5665 0.8146 1.5193 -0.0142 -0.4122 -0.1842 177 VAL   H CA  
14391 C  C   . VAL   H  176 ? 1.5811 0.8672 1.4857 0.0049  -0.4106 -0.2523 177 VAL   H C   
14392 O  O   . VAL   H  176 ? 1.5753 0.9061 1.5215 0.0189  -0.4510 -0.1805 177 VAL   H O   
14393 C  CB  . VAL   H  176 ? 1.5955 0.7061 1.4658 -0.0418 -0.4381 -0.1495 177 VAL   H CB  
14394 C  CG1 . VAL   H  176 ? 1.6445 0.6676 1.4686 -0.0671 -0.4299 -0.1225 177 VAL   H CG1 
14395 C  CG2 . VAL   H  176 ? 1.5762 0.6587 1.4658 -0.0433 -0.4434 -0.0966 177 VAL   H CG2 
14396 N  N   . MET   H  177 ? 1.6378 0.8537 1.4354 -0.0626 -0.3683 -0.2230 178 MET   H N   
14397 C  CA  . MET   H  177 ? 1.7093 0.8494 1.4208 -0.0282 -0.3284 -0.1788 178 MET   H CA  
14398 C  C   . MET   H  177 ? 1.7152 0.8899 1.4129 -0.0474 -0.2875 -0.1292 178 MET   H C   
14399 O  O   . MET   H  177 ? 1.7707 0.7936 1.4747 -0.0888 -0.2746 -0.1627 178 MET   H O   
14400 C  CB  . MET   H  177 ? 1.7331 0.7935 1.3543 -0.0373 -0.3715 -0.1742 178 MET   H CB  
14401 C  CG  . MET   H  177 ? 1.8328 0.8139 1.3578 0.0120  -0.3494 -0.1599 178 MET   H CG  
14402 S  SD  . MET   H  177 ? 1.8985 0.8323 1.3238 0.0224  -0.3756 -0.1839 178 MET   H SD  
14403 C  CE  . MET   H  177 ? 1.9195 0.8156 1.3236 0.0299  -0.3778 -0.1069 178 MET   H CE  
14404 N  N   . GLU   H  178 ? 1.6773 0.9402 1.4589 -0.0397 -0.3210 -0.1039 179 GLU   H N   
14405 C  CA  . GLU   H  178 ? 1.6653 0.9915 1.4626 -0.0184 -0.3440 -0.0501 179 GLU   H CA  
14406 C  C   . GLU   H  178 ? 1.6671 1.0213 1.4451 0.0248  -0.3182 -0.0454 179 GLU   H C   
14407 O  O   . GLU   H  178 ? 1.7465 1.0662 1.5192 0.1200  -0.2009 0.0080  179 GLU   H O   
14408 C  CB  . GLU   H  178 ? 1.6587 1.0800 1.5419 -0.0337 -0.3310 -0.0280 179 GLU   H CB  
14409 C  CG  . GLU   H  178 ? 1.7207 1.1902 1.5396 -0.0503 -0.3224 -0.0063 179 GLU   H CG  
14410 C  CD  . GLU   H  178 ? 1.7417 1.2425 1.5622 -0.0232 -0.3100 0.0514  179 GLU   H CD  
14411 O  OE1 . GLU   H  178 ? 1.7697 1.2586 1.6310 -0.0108 -0.3415 0.1295  179 GLU   H OE1 
14412 O  OE2 . GLU   H  178 ? 1.7445 1.3548 1.6437 -0.0188 -0.2623 0.0010  179 GLU   H OE2 
14413 N  N   . ILE   H  179 ? 1.6186 0.9760 1.3967 0.0554  -0.3857 -0.0250 180 ILE   H N   
14414 C  CA  . ILE   H  179 ? 1.6172 0.9956 1.3492 0.0470  -0.4219 -0.0572 180 ILE   H CA  
14415 C  C   . ILE   H  179 ? 1.5902 0.9638 1.3656 0.0804  -0.4527 -0.0925 180 ILE   H C   
14416 O  O   . ILE   H  179 ? 1.6012 0.9664 1.4209 0.1278  -0.4583 -0.1250 180 ILE   H O   
14417 C  CB  . ILE   H  179 ? 1.6505 0.9871 1.2829 0.0574  -0.4641 -0.0697 180 ILE   H CB  
14418 C  CG1 . ILE   H  179 ? 1.6441 0.9799 1.2660 0.0666  -0.4560 -0.0572 180 ILE   H CG1 
14419 C  CG2 . ILE   H  179 ? 1.6718 0.9917 1.2652 0.0472  -0.4858 -0.0846 180 ILE   H CG2 
14420 C  CD1 . ILE   H  179 ? 1.6525 1.0072 1.2243 0.0846  -0.4590 -0.0790 180 ILE   H CD1 
14421 N  N   . GLY   H  180 ? 1.6087 0.9189 1.4313 -0.0228 -0.3848 -0.1162 181 GLY   H N   
14422 C  CA  . GLY   H  180 ? 1.6115 0.9890 1.5222 -0.0619 -0.3674 -0.1103 181 GLY   H CA  
14423 C  C   . GLY   H  180 ? 1.6306 1.0158 1.5731 -0.0499 -0.3377 -0.1327 181 GLY   H C   
14424 O  O   . GLY   H  180 ? 1.7089 1.0520 1.6856 -0.1002 -0.3500 -0.1746 181 GLY   H O   
14425 N  N   . LYS   H  181 ? 1.5524 0.9248 1.6054 -0.0767 -0.3488 -0.1055 182 LYS   H N   
14426 C  CA  . LYS   H  181 ? 1.5300 0.9346 1.6297 -0.0541 -0.3461 -0.0810 182 LYS   H CA  
14427 C  C   . LYS   H  181 ? 1.4763 0.8018 1.6047 -0.0712 -0.3099 -0.0731 182 LYS   H C   
14428 O  O   . LYS   H  181 ? 1.4601 0.6689 1.6249 -0.0255 -0.3021 -0.0097 182 LYS   H O   
14429 C  CB  . LYS   H  181 ? 1.5280 0.9755 1.6717 -0.0371 -0.3527 -0.0469 182 LYS   H CB  
14430 C  CG  . LYS   H  181 ? 1.5829 1.1354 1.6671 -0.0284 -0.3609 0.0255  182 LYS   H CG  
14431 C  CD  . LYS   H  181 ? 1.5597 1.2386 1.7135 0.0191  -0.3797 0.0882  182 LYS   H CD  
14432 C  CE  . LYS   H  181 ? 1.5859 1.4217 1.7565 0.0210  -0.4089 0.0599  182 LYS   H CE  
14433 N  NZ  . LYS   H  181 ? 1.6003 1.5323 1.8658 0.0440  -0.3681 0.0286  182 LYS   H NZ  
14434 N  N   . ASP   H  182 ? 1.4813 0.9190 1.5676 -0.0655 -0.2974 -0.1050 183 ASP   H N   
14435 C  CA  . ASP   H  182 ? 1.4677 1.0579 1.5578 -0.0902 -0.2860 -0.0966 183 ASP   H CA  
14436 C  C   . ASP   H  182 ? 1.4257 1.0607 1.4726 -0.0848 -0.3097 -0.0767 183 ASP   H C   
14437 O  O   . ASP   H  182 ? 1.4850 1.1856 1.4453 -0.0339 -0.2961 0.0197  183 ASP   H O   
14438 C  CB  . ASP   H  182 ? 1.4884 1.1800 1.5555 -0.1138 -0.2605 -0.1097 183 ASP   H CB  
14439 C  CG  . ASP   H  182 ? 1.5472 1.2142 1.5889 -0.2192 -0.2461 -0.1274 183 ASP   H CG  
14440 O  OD1 . ASP   H  182 ? 1.5239 1.3037 1.5478 -0.2170 -0.2974 -0.1635 183 ASP   H OD1 
14441 O  OD2 . ASP   H  182 ? 1.5484 1.4108 1.5927 -0.2065 -0.1133 -0.2345 183 ASP   H OD2 
14442 N  N   . ALA   H  183 ? 1.4511 1.0577 1.4477 -0.1216 -0.2980 -0.1274 184 ALA   H N   
14443 C  CA  . ALA   H  183 ? 1.4410 1.0521 1.4636 -0.1570 -0.3208 -0.1087 184 ALA   H CA  
14444 C  C   . ALA   H  183 ? 1.3925 0.9290 1.5005 -0.1292 -0.3587 -0.1200 184 ALA   H C   
14445 O  O   . ALA   H  183 ? 1.4388 0.9726 1.5313 -0.1664 -0.3159 -0.1230 184 ALA   H O   
14446 C  CB  . ALA   H  183 ? 1.4406 1.0728 1.4494 -0.1775 -0.3145 -0.1422 184 ALA   H CB  
14447 N  N   . GLU   H  184 ? 1.4188 0.8811 1.4618 -0.1795 -0.3945 -0.0386 185 GLU   H N   
14448 C  CA  . GLU   H  184 ? 1.4490 0.7899 1.4985 -0.1285 -0.3897 -0.0060 185 GLU   H CA  
14449 C  C   . GLU   H  184 ? 1.5027 0.6293 1.5391 -0.1152 -0.3340 0.0401  185 GLU   H C   
14450 O  O   . GLU   H  184 ? 1.4735 0.6758 1.5181 -0.0762 -0.3046 0.0966  185 GLU   H O   
14451 C  CB  . GLU   H  184 ? 1.4756 0.7950 1.5100 -0.1280 -0.4174 0.0129  185 GLU   H CB  
14452 C  CG  . GLU   H  184 ? 1.4687 0.8142 1.4976 -0.1351 -0.4275 0.0164  185 GLU   H CG  
14453 C  CD  . GLU   H  184 ? 1.4664 0.9117 1.5157 -0.1530 -0.4539 0.0098  185 GLU   H CD  
14454 O  OE1 . GLU   H  184 ? 1.3735 1.0768 1.5278 -0.0856 -0.5924 0.0009  185 GLU   H OE1 
14455 O  OE2 . GLU   H  184 ? 1.3809 0.9031 1.5778 -0.2260 -0.4735 0.0353  185 GLU   H OE2 
14456 N  N   . TYR   H  185 ? 1.5514 0.5965 1.5141 -0.1041 -0.3216 -0.0267 186 TYR   H N   
14457 C  CA  . TYR   H  185 ? 1.5300 0.4828 1.5744 -0.1208 -0.3040 -0.0217 186 TYR   H CA  
14458 C  C   . TYR   H  185 ? 1.4932 0.5324 1.6083 -0.1640 -0.2745 -0.0667 186 TYR   H C   
14459 O  O   . TYR   H  185 ? 1.5336 0.3210 1.6929 -0.1346 -0.2671 -0.0275 186 TYR   H O   
14460 C  CB  . TYR   H  185 ? 1.5724 0.5008 1.5319 -0.1203 -0.3037 -0.0364 186 TYR   H CB  
14461 C  CG  . TYR   H  185 ? 1.6272 0.4553 1.5007 -0.0864 -0.2878 -0.0230 186 TYR   H CG  
14462 C  CD1 . TYR   H  185 ? 1.6261 0.4481 1.4705 -0.0822 -0.2934 -0.0369 186 TYR   H CD1 
14463 C  CD2 . TYR   H  185 ? 1.6365 0.4890 1.5045 -0.0946 -0.2538 -0.0407 186 TYR   H CD2 
14464 C  CE1 . TYR   H  185 ? 1.6427 0.4696 1.4745 -0.0856 -0.2744 -0.0602 186 TYR   H CE1 
14465 C  CE2 . TYR   H  185 ? 1.6334 0.4199 1.5038 -0.0666 -0.2365 -0.0377 186 TYR   H CE2 
14466 C  CZ  . TYR   H  185 ? 1.6352 0.4190 1.4636 -0.0824 -0.2707 -0.0840 186 TYR   H CZ  
14467 O  OH  . TYR   H  185 ? 1.6287 0.5260 1.4364 -0.0898 -0.2813 -0.0963 186 TYR   H OH  
14468 N  N   . LEU   H  186 ? 1.5089 0.5373 1.5884 -0.1346 -0.2566 -0.0625 187 LEU   H N   
14469 C  CA  . LEU   H  186 ? 1.4898 0.5975 1.5713 -0.1274 -0.2303 -0.0495 187 LEU   H CA  
14470 C  C   . LEU   H  186 ? 1.5042 0.5882 1.5501 -0.1443 -0.2018 -0.0369 187 LEU   H C   
14471 O  O   . LEU   H  186 ? 1.5511 0.5855 1.5900 -0.1569 -0.1998 -0.0538 187 LEU   H O   
14472 C  CB  . LEU   H  186 ? 1.4782 0.5865 1.5527 -0.1318 -0.2471 -0.0712 187 LEU   H CB  
14473 C  CG  . LEU   H  186 ? 1.4765 0.6035 1.5759 -0.1285 -0.2433 -0.1017 187 LEU   H CG  
14474 C  CD1 . LEU   H  186 ? 1.4792 0.6108 1.5724 -0.1267 -0.2725 -0.1036 187 LEU   H CD1 
14475 C  CD2 . LEU   H  186 ? 1.4838 0.6377 1.5921 -0.1175 -0.2007 -0.0973 187 LEU   H CD2 
14476 N  N   . ARG   H  187 ? 1.4931 0.6986 1.5146 -0.1444 -0.1969 -0.0429 188 ARG   H N   
14477 C  CA  . ARG   H  187 ? 1.4716 0.6377 1.5387 -0.1437 -0.2166 -0.0568 188 ARG   H CA  
14478 C  C   . ARG   H  187 ? 1.4543 0.6223 1.4932 -0.1585 -0.2127 -0.0577 188 ARG   H C   
14479 O  O   . ARG   H  187 ? 1.4629 0.4653 1.5297 -0.1574 -0.1959 -0.1042 188 ARG   H O   
14480 C  CB  . ARG   H  187 ? 1.4915 0.7679 1.4923 -0.1083 -0.2573 -0.0239 188 ARG   H CB  
14481 C  CG  . ARG   H  187 ? 1.5106 0.8002 1.5050 -0.0754 -0.2678 -0.0418 188 ARG   H CG  
14482 C  CD  . ARG   H  187 ? 1.4842 0.8108 1.5021 -0.0474 -0.2967 -0.0208 188 ARG   H CD  
14483 N  NE  . ARG   H  187 ? 1.5036 0.8593 1.4992 0.0186  -0.3069 -0.0175 188 ARG   H NE  
14484 C  CZ  . ARG   H  187 ? 1.4835 0.8182 1.5117 0.0524  -0.3181 0.0042  188 ARG   H CZ  
14485 N  NH1 . ARG   H  187 ? 1.4807 0.7283 1.4620 0.1197  -0.3379 0.0405  188 ARG   H NH1 
14486 N  NH2 . ARG   H  187 ? 1.5314 0.9399 1.5170 0.0963  -0.2848 0.0140  188 ARG   H NH2 
14487 N  N   . ASN   H  188 ? 1.4688 0.6065 1.4659 -0.1298 -0.2093 -0.0762 189 ASN   H N   
14488 C  CA  . ASN   H  188 ? 1.5114 0.5637 1.4825 -0.1365 -0.2258 -0.0701 189 ASN   H CA  
14489 C  C   . ASN   H  188 ? 1.4950 0.5260 1.5535 -0.1051 -0.2575 -0.0781 189 ASN   H C   
14490 O  O   . ASN   H  188 ? 1.4927 0.4308 1.5760 -0.1292 -0.2520 -0.0729 189 ASN   H O   
14491 C  CB  . ASN   H  188 ? 1.5373 0.5565 1.4966 -0.1414 -0.2050 -0.0625 189 ASN   H CB  
14492 C  CG  . ASN   H  188 ? 1.5575 0.5775 1.4603 -0.1388 -0.1870 -0.0338 189 ASN   H CG  
14493 O  OD1 . ASN   H  188 ? 1.5533 0.5627 1.4544 -0.1392 -0.1801 -0.0108 189 ASN   H OD1 
14494 N  ND2 . ASN   H  188 ? 1.6170 0.6183 1.4610 -0.1364 -0.1698 -0.0194 189 ASN   H ND2 
14495 N  N   . TYR   H  189 ? 1.4843 0.5767 1.5680 -0.0516 -0.2476 -0.0873 190 TYR   H N   
14496 C  CA  . TYR   H  189 ? 1.5105 0.6671 1.5940 -0.0211 -0.2642 -0.0632 190 TYR   H CA  
14497 C  C   . TYR   H  189 ? 1.4692 0.7034 1.6214 0.0062  -0.2687 -0.0237 190 TYR   H C   
14498 O  O   . TYR   H  189 ? 1.4786 0.7602 1.6436 -0.0055 -0.2928 -0.0034 190 TYR   H O   
14499 C  CB  . TYR   H  189 ? 1.5253 0.6873 1.5851 0.0050  -0.2693 -0.0423 190 TYR   H CB  
14500 C  CG  . TYR   H  189 ? 1.5335 0.6780 1.6231 0.0149  -0.3089 -0.0363 190 TYR   H CG  
14501 C  CD1 . TYR   H  189 ? 1.4943 0.7259 1.6020 0.0301  -0.3334 -0.0353 190 TYR   H CD1 
14502 C  CD2 . TYR   H  189 ? 1.5325 0.6526 1.6196 0.0446  -0.3191 -0.0436 190 TYR   H CD2 
14503 C  CE1 . TYR   H  189 ? 1.4343 0.7145 1.6143 0.0488  -0.3503 -0.0645 190 TYR   H CE1 
14504 C  CE2 . TYR   H  189 ? 1.4801 0.6803 1.6280 0.0779  -0.3452 -0.0808 190 TYR   H CE2 
14505 C  CZ  . TYR   H  189 ? 1.4360 0.7018 1.6196 0.0834  -0.3556 -0.0580 190 TYR   H CZ  
14506 O  OH  . TYR   H  189 ? 1.3876 0.7789 1.6517 0.1501  -0.3769 -0.0741 190 TYR   H OH  
14507 N  N   . LEU   H  190 ? 1.4329 0.7864 1.6417 -0.0458 -0.2761 -0.0031 191 LEU   H N   
14508 C  CA  . LEU   H  190 ? 1.4016 0.8250 1.6642 -0.0031 -0.2880 -0.0017 191 LEU   H CA  
14509 C  C   . LEU   H  190 ? 1.3144 0.7545 1.6801 -0.0511 -0.2939 -0.0286 191 LEU   H C   
14510 O  O   . LEU   H  190 ? 1.3047 0.6462 1.6362 -0.1075 -0.3153 -0.0342 191 LEU   H O   
14511 C  CB  . LEU   H  190 ? 1.3728 0.8665 1.6539 0.0393  -0.3170 0.0571  191 LEU   H CB  
14512 C  CG  . LEU   H  190 ? 1.3649 0.9190 1.7000 0.1099  -0.3853 0.0943  191 LEU   H CG  
14513 C  CD1 . LEU   H  190 ? 1.3237 0.9025 1.7055 0.1236  -0.4314 0.1273  191 LEU   H CD1 
14514 C  CD2 . LEU   H  190 ? 1.3694 0.9755 1.7376 0.1270  -0.3700 0.0866  191 LEU   H CD2 
14515 N  N   . THR   H  191 ? 1.3817 0.7432 1.6782 -0.0705 -0.2671 -0.0885 192 THR   H N   
14516 C  CA  . THR   H  191 ? 1.4065 0.8494 1.6700 -0.0602 -0.2793 -0.0949 192 THR   H CA  
14517 C  C   . THR   H  191 ? 1.4123 0.9019 1.6902 0.0029  -0.2838 -0.0998 192 THR   H C   
14518 O  O   . THR   H  191 ? 1.4187 1.0902 1.7111 -0.0255 -0.2406 -0.0920 192 THR   H O   
14519 C  CB  . THR   H  191 ? 1.4360 0.7886 1.6500 -0.0372 -0.2880 -0.0958 192 THR   H CB  
14520 O  OG1 . THR   H  191 ? 1.4325 0.7909 1.6706 -0.0370 -0.2825 -0.1178 192 THR   H OG1 
14521 C  CG2 . THR   H  191 ? 1.4211 0.8164 1.6207 -0.0151 -0.2801 -0.0415 192 THR   H CG2 
14522 N  N   . PRO   H  192 ? 1.3666 0.8848 1.6316 0.0311  -0.3063 -0.1070 193 PRO   H N   
14523 C  CA  . PRO   H  192 ? 1.3668 0.9078 1.6428 0.0851  -0.3244 -0.1166 193 PRO   H CA  
14524 C  C   . PRO   H  192 ? 1.3577 0.9021 1.6205 0.1371  -0.2886 -0.1194 193 PRO   H C   
14525 O  O   . PRO   H  192 ? 1.3065 0.9050 1.6778 0.1906  -0.2847 -0.1332 193 PRO   H O   
14526 C  CB  . PRO   H  192 ? 1.3740 0.8874 1.6067 0.0947  -0.3407 -0.1323 193 PRO   H CB  
14527 C  CG  . PRO   H  192 ? 1.3620 0.8983 1.5814 0.0873  -0.3322 -0.1373 193 PRO   H CG  
14528 C  CD  . PRO   H  192 ? 1.3694 0.9246 1.5933 0.0582  -0.3192 -0.1263 193 PRO   H CD  
14529 N  N   . ASN   H  193 ? 1.3856 0.9145 1.5873 0.1168  -0.2317 -0.1136 194 ASN   H N   
14530 C  CA  . ASN   H  193 ? 1.3911 0.8737 1.5835 0.1019  -0.2183 -0.1067 194 ASN   H CA  
14531 C  C   . ASN   H  193 ? 1.4193 0.8183 1.6215 0.0850  -0.2510 -0.0376 194 ASN   H C   
14532 O  O   . ASN   H  193 ? 1.4474 0.7976 1.6293 0.0509  -0.2395 0.0808  194 ASN   H O   
14533 C  CB  . ASN   H  193 ? 1.3921 0.9074 1.5503 0.1186  -0.2133 -0.1632 194 ASN   H CB  
14534 C  CG  . ASN   H  193 ? 1.3988 0.9161 1.5582 0.1118  -0.2200 -0.1652 194 ASN   H CG  
14535 O  OD1 . ASN   H  193 ? 1.3801 0.9465 1.5617 0.1601  -0.2015 -0.2125 194 ASN   H OD1 
14536 N  ND2 . ASN   H  193 ? 1.4154 0.9409 1.5615 0.1295  -0.2312 -0.1755 194 ASN   H ND2 
14537 N  N   . VAL   H  194 ? 1.4383 0.7852 1.7030 0.0130  -0.1799 -0.0318 195 VAL   H N   
14538 C  CA  . VAL   H  194 ? 1.5068 0.8140 1.7141 -0.0306 -0.1489 -0.0542 195 VAL   H CA  
14539 C  C   . VAL   H  194 ? 1.5387 0.8038 1.7377 -0.0253 -0.0924 -0.0478 195 VAL   H C   
14540 O  O   . VAL   H  194 ? 1.5987 0.8036 1.7817 -0.0656 -0.0524 -0.0168 195 VAL   H O   
14541 C  CB  . VAL   H  194 ? 1.5637 0.8091 1.7423 -0.1038 -0.1557 -0.1176 195 VAL   H CB  
14542 C  CG1 . VAL   H  194 ? 1.5470 0.7949 1.7165 -0.1398 -0.1598 -0.1860 195 VAL   H CG1 
14543 C  CG2 . VAL   H  194 ? 1.5919 0.8594 1.7303 -0.0936 -0.1550 -0.1316 195 VAL   H CG2 
14544 N  N   . ARG   H  195 ? 1.5048 0.7829 1.7677 0.0061  -0.1040 -0.0099 196 ARG   H N   
14545 C  CA  . ARG   H  195 ? 1.4976 0.7164 1.8245 -0.0322 -0.0777 -0.0222 196 ARG   H CA  
14546 C  C   . ARG   H  195 ? 1.4979 0.8557 1.8243 -0.0228 -0.0441 -0.0288 196 ARG   H C   
14547 O  O   . ARG   H  195 ? 1.4865 0.7844 1.8662 0.0238  0.0197  0.0061  196 ARG   H O   
14548 C  CB  . ARG   H  195 ? 1.5183 0.7130 1.7937 -0.0393 -0.0313 -0.0180 196 ARG   H CB  
14549 C  CG  . ARG   H  195 ? 1.5158 0.7095 1.8186 -0.0374 -0.0028 -0.0438 196 ARG   H CG  
14550 C  CD  . ARG   H  195 ? 1.5414 0.7730 1.8997 -0.0204 0.0657  -0.0658 196 ARG   H CD  
14551 N  NE  . ARG   H  195 ? 1.5468 0.7723 1.9286 -0.0093 0.0609  -0.0938 196 ARG   H NE  
14552 C  CZ  . ARG   H  195 ? 1.5629 0.8246 2.0054 0.0291  0.0913  -0.1757 196 ARG   H CZ  
14553 N  NH1 . ARG   H  195 ? 1.5974 0.8795 2.0533 0.0770  0.1310  -0.2351 196 ARG   H NH1 
14554 N  NH2 . ARG   H  195 ? 1.5309 0.7584 2.0041 0.0372  0.0951  -0.1899 196 ARG   H NH2 
14555 N  N   . GLU   H  196 ? 1.5020 0.8722 1.8448 -0.0122 -0.0349 -0.0384 197 GLU   H N   
14556 C  CA  . GLU   H  196 ? 1.5125 1.0175 1.8932 0.0227  -0.0396 -0.0572 197 GLU   H CA  
14557 C  C   . GLU   H  196 ? 1.5570 1.0857 1.8637 0.0417  -0.0897 -0.0253 197 GLU   H C   
14558 O  O   . GLU   H  196 ? 1.5821 1.1706 1.8606 0.0317  -0.1050 -0.0038 197 GLU   H O   
14559 C  CB  . GLU   H  196 ? 1.5377 1.0037 1.9067 0.0351  -0.0136 -0.1274 197 GLU   H CB  
14560 C  CG  . GLU   H  196 ? 1.5551 1.0769 1.9146 0.0200  0.0000  -0.1710 197 GLU   H CG  
14561 C  CD  . GLU   H  196 ? 1.6034 1.0723 1.9163 0.0126  0.0137  -0.2141 197 GLU   H CD  
14562 O  OE1 . GLU   H  196 ? 1.6251 1.0768 1.9918 0.0746  0.0129  -0.2683 197 GLU   H OE1 
14563 O  OE2 . GLU   H  196 ? 1.6304 1.1531 1.9863 -0.0726 0.0458  -0.1469 197 GLU   H OE2 
14564 N  N   . GLU   H  197 ? 1.5518 1.1810 1.9338 0.0321  -0.1190 -0.0365 198 GLU   H N   
14565 C  CA  . GLU   H  197 ? 1.5960 1.2749 1.9108 -0.0201 -0.1453 -0.0358 198 GLU   H CA  
14566 C  C   . GLU   H  197 ? 1.5411 1.2955 1.9031 0.0123  -0.1761 -0.0374 198 GLU   H C   
14567 O  O   . GLU   H  197 ? 1.5691 1.3232 1.8936 -0.0350 -0.2235 -0.0133 198 GLU   H O   
14568 C  CB  . GLU   H  197 ? 1.5951 1.4334 2.0396 -0.0615 -0.1677 -0.0194 198 GLU   H CB  
14569 C  CG  . GLU   H  197 ? 1.7040 1.4937 2.1136 -0.1315 -0.2229 0.0091  198 GLU   H CG  
14570 C  CD  . GLU   H  197 ? 1.6777 1.6538 2.2493 -0.1320 -0.2404 0.0324  198 GLU   H CD  
14571 O  OE1 . GLU   H  197 ? 1.8654 1.6544 2.2516 -0.1403 -0.2688 0.0564  198 GLU   H OE1 
14572 O  OE2 . GLU   H  197 ? 1.8386 1.8287 2.3128 -0.1525 -0.3676 -0.0256 198 GLU   H OE2 
14573 N  N   . LYS   H  198 ? 1.4832 1.1831 1.8911 0.0011  -0.1677 -0.0683 199 LYS   H N   
14574 C  CA  . LYS   H  198 ? 1.4599 1.1761 1.8906 0.0129  -0.1288 -0.0956 199 LYS   H CA  
14575 C  C   . LYS   H  198 ? 1.4610 1.1174 1.8417 -0.0103 -0.1216 -0.1000 199 LYS   H C   
14576 O  O   . LYS   H  198 ? 1.4635 1.0728 1.8117 -0.0135 -0.0846 -0.0270 199 LYS   H O   
14577 C  CB  . LYS   H  198 ? 1.5035 1.1909 1.8627 0.0271  -0.1360 -0.1181 199 LYS   H CB  
14578 C  CG  . LYS   H  198 ? 1.5288 1.1658 1.8384 0.0406  -0.1195 -0.1642 199 LYS   H CG  
14579 C  CD  . LYS   H  198 ? 1.5448 1.1521 1.7933 0.0557  -0.1068 -0.2046 199 LYS   H CD  
14580 C  CE  . LYS   H  198 ? 1.5565 1.1188 1.7324 0.1137  -0.0966 -0.2340 199 LYS   H CE  
14581 N  NZ  . LYS   H  198 ? 1.5742 1.1480 1.7053 0.1403  -0.0877 -0.2128 199 LYS   H NZ  
14582 N  N   . GLN   H  199 ? 1.4642 1.1380 1.8184 0.0386  -0.0861 -0.1618 200 GLN   H N   
14583 C  CA  . GLN   H  199 ? 1.5080 1.1325 1.8390 0.0191  -0.0881 -0.2309 200 GLN   H CA  
14584 C  C   . GLN   H  199 ? 1.5491 1.1286 1.8788 -0.0010 -0.1027 -0.1754 200 GLN   H C   
14585 O  O   . GLN   H  199 ? 1.5614 1.2077 2.0319 -0.0122 -0.0635 -0.2255 200 GLN   H O   
14586 C  CB  . GLN   H  199 ? 1.5278 1.1229 1.7562 0.0351  -0.0734 -0.2645 200 GLN   H CB  
14587 C  CG  . GLN   H  199 ? 1.5391 1.0486 1.7270 0.0606  -0.0712 -0.2962 200 GLN   H CG  
14588 C  CD  . GLN   H  199 ? 1.5586 1.0079 1.7377 0.0824  -0.0697 -0.3011 200 GLN   H CD  
14589 O  OE1 . GLN   H  199 ? 1.5753 0.9499 1.7413 0.1162  -0.0189 -0.3231 200 GLN   H OE1 
14590 N  NE2 . GLN   H  199 ? 1.5609 1.0802 1.7763 0.1071  -0.0486 -0.3011 200 GLN   H NE2 
14591 N  N   . LYS   H  200 ? 1.5359 1.1159 1.8826 0.0082  -0.1041 -0.1879 201 LYS   H N   
14592 C  CA  . LYS   H  200 ? 1.5593 1.1796 1.8625 0.0155  -0.0959 -0.2160 201 LYS   H CA  
14593 C  C   . LYS   H  200 ? 1.5445 1.1839 1.7991 0.0223  -0.0586 -0.2420 201 LYS   H C   
14594 O  O   . LYS   H  200 ? 1.5522 1.2582 1.7680 0.0389  -0.0798 -0.3072 201 LYS   H O   
14595 C  CB  . LYS   H  200 ? 1.5695 1.0628 1.8998 0.0298  -0.0738 -0.2168 201 LYS   H CB  
14596 C  CG  . LYS   H  200 ? 1.6183 1.0864 1.9091 0.0567  -0.0567 -0.2286 201 LYS   H CG  
14597 C  CD  . LYS   H  200 ? 1.6470 1.1646 1.9338 0.0454  -0.0846 -0.2463 201 LYS   H CD  
14598 C  CE  . LYS   H  200 ? 1.6873 1.2269 1.9436 0.0586  -0.0692 -0.2150 201 LYS   H CE  
14599 N  NZ  . LYS   H  200 ? 1.6794 1.2144 1.9532 0.0528  -0.0689 -0.2167 201 LYS   H NZ  
14600 N  N   . SER   H  201 ? 1.6112 1.1256 1.8014 -0.0231 -0.0618 -0.2681 202 SER   H N   
14601 C  CA  . SER   H  201 ? 1.6059 1.0962 1.7920 -0.0154 -0.0096 -0.2888 202 SER   H CA  
14602 C  C   . SER   H  201 ? 1.5598 1.0913 1.7922 0.0238  -0.0036 -0.2683 202 SER   H C   
14603 O  O   . SER   H  201 ? 1.5781 1.1209 1.7918 0.0337  0.0535  -0.2355 202 SER   H O   
14604 C  CB  . SER   H  201 ? 1.6438 1.1025 1.7606 -0.0393 0.0039  -0.2981 202 SER   H CB  
14605 O  OG  . SER   H  201 ? 1.6704 1.0880 1.7093 -0.0326 0.0326  -0.3172 202 SER   H OG  
14606 N  N   . TYR   H  202 ? 1.5801 1.1365 1.8179 0.0574  0.0085  -0.2622 203 TYR   H N   
14607 C  CA  . TYR   H  202 ? 1.5844 1.1726 1.8349 0.0634  -0.0008 -0.2746 203 TYR   H CA  
14608 C  C   . TYR   H  202 ? 1.5126 1.1362 1.8321 0.1101  0.0004  -0.2989 203 TYR   H C   
14609 O  O   . TYR   H  202 ? 1.4612 1.1099 1.8459 0.1568  0.0220  -0.3428 203 TYR   H O   
14610 C  CB  . TYR   H  202 ? 1.5768 1.2043 1.8265 0.0579  -0.0217 -0.2434 203 TYR   H CB  
14611 C  CG  . TYR   H  202 ? 1.6417 1.2663 1.8718 0.0156  -0.0222 -0.1739 203 TYR   H CG  
14612 C  CD1 . TYR   H  202 ? 1.6918 1.2934 1.8996 -0.0461 -0.0247 -0.1945 203 TYR   H CD1 
14613 C  CD2 . TYR   H  202 ? 1.7095 1.2748 1.8711 0.0008  -0.0062 -0.1884 203 TYR   H CD2 
14614 C  CE1 . TYR   H  202 ? 1.7772 1.3043 1.9729 -0.0956 -0.0397 -0.1755 203 TYR   H CE1 
14615 C  CE2 . TYR   H  202 ? 1.8168 1.2882 1.9423 -0.0515 -0.0239 -0.1700 203 TYR   H CE2 
14616 C  CZ  . TYR   H  202 ? 1.8567 1.2969 1.9772 -0.0803 -0.0607 -0.1836 203 TYR   H CZ  
14617 O  OH  . TYR   H  202 ? 1.9689 1.3169 2.0997 -0.0573 -0.1013 -0.1261 203 TYR   H OH  
14618 N  N   . LYS   H  203 ? 1.5773 1.0745 1.8961 0.0793  0.0092  -0.3408 204 LYS   H N   
14619 C  CA  . LYS   H  203 ? 1.6180 1.0325 1.9179 0.0394  -0.0163 -0.3647 204 LYS   H CA  
14620 C  C   . LYS   H  203 ? 1.6697 1.1299 1.8904 0.0345  -0.0068 -0.3514 204 LYS   H C   
14621 O  O   . LYS   H  203 ? 1.7085 1.1907 1.9283 0.0615  0.0240  -0.3744 204 LYS   H O   
14622 C  CB  . LYS   H  203 ? 1.6756 1.0540 2.0009 -0.0079 -0.0647 -0.3604 204 LYS   H CB  
14623 C  CG  . LYS   H  203 ? 1.7118 1.0711 2.0258 -0.0392 -0.1010 -0.3443 204 LYS   H CG  
14624 C  CD  . LYS   H  203 ? 1.7784 0.9307 2.0705 -0.0917 -0.0936 -0.3243 204 LYS   H CD  
14625 C  CE  . LYS   H  203 ? 1.8386 0.8307 2.0836 -0.1438 -0.1218 -0.3415 204 LYS   H CE  
14626 N  NZ  . LYS   H  203 ? 1.8771 0.8012 2.0995 -0.1621 -0.1365 -0.3319 204 LYS   H NZ  
14627 N  N   . PHE   H  204 ? 1.6337 1.1530 1.8115 0.0891  0.0658  -0.3571 205 PHE   H N   
14628 C  CA  . PHE   H  204 ? 1.6452 1.3109 1.7607 0.0879  0.0570  -0.3014 205 PHE   H CA  
14629 C  C   . PHE   H  204 ? 1.6642 1.3490 1.8334 0.0544  0.0437  -0.2489 205 PHE   H C   
14630 O  O   . PHE   H  204 ? 1.5533 1.3134 1.7765 0.1592  0.0357  -0.2930 205 PHE   H O   
14631 C  CB  . PHE   H  204 ? 1.6314 1.3348 1.6742 0.0859  0.0913  -0.2779 205 PHE   H CB  
14632 C  CG  . PHE   H  204 ? 1.6024 1.4343 1.6013 0.0915  0.1012  -0.2730 205 PHE   H CG  
14633 C  CD1 . PHE   H  204 ? 1.5720 1.5114 1.5817 0.0164  0.0836  -0.2894 205 PHE   H CD1 
14634 C  CD2 . PHE   H  204 ? 1.5469 1.3493 1.6145 0.0832  0.0900  -0.2633 205 PHE   H CD2 
14635 C  CE1 . PHE   H  204 ? 1.5112 1.5939 1.5892 0.0302  0.0888  -0.2984 205 PHE   H CE1 
14636 C  CE2 . PHE   H  204 ? 1.4810 1.4286 1.6483 0.0790  0.0695  -0.2635 205 PHE   H CE2 
14637 C  CZ  . PHE   H  204 ? 1.4973 1.5021 1.6225 0.0618  0.0592  -0.3261 205 PHE   H CZ  
14638 N  N   . PRO   H  205 ? 1.7478 1.5096 1.8407 0.0922  0.0714  -0.2764 206 PRO   H N   
14639 C  CA  . PRO   H  205 ? 1.7933 1.5350 1.8754 0.0906  0.0627  -0.2150 206 PRO   H CA  
14640 C  C   . PRO   H  205 ? 1.8092 1.5214 1.8677 0.1017  0.0529  -0.2333 206 PRO   H C   
14641 O  O   . PRO   H  205 ? 1.7642 1.5229 1.8357 0.1874  0.0572  -0.2114 206 PRO   H O   
14642 C  CB  . PRO   H  205 ? 1.7742 1.5879 1.9323 0.0921  0.0739  -0.2602 206 PRO   H CB  
14643 C  CG  . PRO   H  205 ? 1.7328 1.5823 1.9280 0.0804  0.0537  -0.2694 206 PRO   H CG  
14644 C  CD  . PRO   H  205 ? 1.7479 1.5166 1.8883 0.0639  0.0448  -0.2884 206 PRO   H CD  
14645 N  N   . ARG   H  206 ? 1.7869 1.4885 1.8309 0.1186  -0.0019 -0.2688 207 ARG   H N   
14646 C  CA  . ARG   H  206 ? 1.7260 1.5052 1.7722 0.0750  0.0007  -0.2342 207 ARG   H CA  
14647 C  C   . ARG   H  206 ? 1.6506 1.4965 1.7294 0.1234  0.0498  -0.1916 207 ARG   H C   
14648 O  O   . ARG   H  206 ? 1.6751 1.5092 1.7377 0.0652  0.1288  -0.1090 207 ARG   H O   
14649 C  CB  . ARG   H  206 ? 1.7537 1.5755 1.8344 0.0145  -0.0260 -0.1929 207 ARG   H CB  
14650 C  CG  . ARG   H  206 ? 1.7904 1.5822 1.8679 -0.0345 -0.0606 -0.2137 207 ARG   H CG  
14651 C  CD  . ARG   H  206 ? 1.7949 1.5802 1.8985 -0.0412 -0.0641 -0.2039 207 ARG   H CD  
14652 N  NE  . ARG   H  206 ? 1.7640 1.5072 1.9531 -0.1027 -0.0968 -0.2201 207 ARG   H NE  
14653 C  CZ  . ARG   H  206 ? 1.7080 1.4976 1.9451 -0.0958 -0.1320 -0.1886 207 ARG   H CZ  
14654 N  NH1 . ARG   H  206 ? 1.6536 1.4571 1.9368 -0.0931 -0.1231 -0.2110 207 ARG   H NH1 
14655 N  NH2 . ARG   H  206 ? 1.7001 1.4542 1.9716 -0.1120 -0.1520 -0.2102 207 ARG   H NH2 
14656 N  N   . GLY   H  207 ? 1.6694 1.5222 1.6401 0.1962  0.0420  -0.1816 208 GLY   H N   
14657 C  CA  . GLY   H  207 ? 1.6278 1.6607 1.6478 0.2194  -0.0117 -0.1557 208 GLY   H CA  
14658 C  C   . GLY   H  207 ? 1.5646 1.7782 1.6328 0.1663  -0.0940 -0.1843 208 GLY   H C   
14659 O  O   . GLY   H  207 ? 1.6045 1.9330 1.6589 0.1655  -0.2087 -0.0660 208 GLY   H O   
14660 N  N   . THR   H  208 ? 1.5092 1.8766 1.6035 0.1654  -0.0486 -0.1982 209 THR   H N   
14661 C  CA  . THR   H  208 ? 1.4568 1.9695 1.6573 0.1375  -0.0023 -0.1707 209 THR   H CA  
14662 C  C   . THR   H  208 ? 1.4727 2.0575 1.6267 0.2593  0.0441  -0.1562 209 THR   H C   
14663 O  O   . THR   H  208 ? 1.4563 2.1625 1.6396 0.2555  -0.0394 -0.1345 209 THR   H O   
14664 C  CB  . THR   H  208 ? 1.4645 2.0427 1.6389 0.1552  -0.0010 -0.1913 209 THR   H CB  
14665 O  OG1 . THR   H  208 ? 1.3976 2.0117 1.6902 0.0408  0.0390  -0.2007 209 THR   H OG1 
14666 C  CG2 . THR   H  208 ? 1.4680 2.0884 1.6959 0.1372  0.0054  -0.2007 209 THR   H CG2 
14667 N  N   . THR   H  209 ? 1.5286 1.9974 1.5407 0.1655  0.0398  -0.2372 210 THR   H N   
14668 C  CA  . THR   H  209 ? 1.5275 1.9864 1.5067 0.1601  0.0350  -0.2723 210 THR   H CA  
14669 C  C   . THR   H  209 ? 1.5695 1.9466 1.5164 0.1107  0.0596  -0.2578 210 THR   H C   
14670 O  O   . THR   H  209 ? 1.6155 1.8027 1.4288 0.1117  0.0064  -0.3881 210 THR   H O   
14671 C  CB  . THR   H  209 ? 1.4284 1.9263 1.5707 0.1788  0.0306  -0.2578 210 THR   H CB  
14672 O  OG1 . THR   H  209 ? 1.4110 1.9631 1.5502 0.1494  0.0078  -0.2980 210 THR   H OG1 
14673 C  CG2 . THR   H  209 ? 1.4450 1.8954 1.5369 0.2420  0.0202  -0.2512 210 THR   H CG2 
14674 N  N   . ALA   H  210 ? 1.5813 2.0725 1.5771 0.1209  0.0127  -0.2762 211 ALA   H N   
14675 C  CA  . ALA   H  210 ? 1.5715 2.0841 1.6188 0.1497  0.0169  -0.2243 211 ALA   H CA  
14676 C  C   . ALA   H  210 ? 1.5452 2.0468 1.5733 0.1170  0.0281  -0.2465 211 ALA   H C   
14677 O  O   . ALA   H  210 ? 1.5673 1.8910 1.5100 0.0693  0.0274  -0.2225 211 ALA   H O   
14678 C  CB  . ALA   H  210 ? 1.5516 2.1728 1.6336 0.1313  -0.0108 -0.2445 211 ALA   H CB  
14679 N  N   . VAL   H  211 ? 1.5706 2.0208 1.5787 0.1095  -0.0255 -0.2545 212 VAL   H N   
14680 C  CA  . VAL   H  211 ? 1.5084 2.0000 1.6033 0.0731  -0.0463 -0.2760 212 VAL   H CA  
14681 C  C   . VAL   H  211 ? 1.5572 2.0614 1.6059 0.0496  -0.0330 -0.2401 212 VAL   H C   
14682 O  O   . VAL   H  211 ? 1.4759 2.1308 1.6670 -0.0106 0.0204  -0.1558 212 VAL   H O   
14683 C  CB  . VAL   H  211 ? 1.4936 1.9143 1.5628 0.0959  -0.0272 -0.2357 212 VAL   H CB  
14684 C  CG1 . VAL   H  211 ? 1.4169 1.9316 1.5248 0.1163  -0.0149 -0.2034 212 VAL   H CG1 
14685 C  CG2 . VAL   H  211 ? 1.5348 1.9351 1.5678 0.0692  -0.0533 -0.2615 212 VAL   H CG2 
14686 N  N   . LEU   H  212 ? 1.5979 2.0127 1.7057 0.0726  -0.0227 -0.2868 213 LEU   H N   
14687 C  CA  . LEU   H  212 ? 1.6520 2.0428 1.7087 0.0540  -0.0206 -0.2460 213 LEU   H CA  
14688 C  C   . LEU   H  212 ? 1.6257 2.0529 1.6321 0.0336  0.0003  -0.2296 213 LEU   H C   
14689 O  O   . LEU   H  212 ? 1.6081 1.9753 1.6032 0.0465  0.0470  -0.3164 213 LEU   H O   
14690 C  CB  . LEU   H  212 ? 1.6294 2.1728 1.8117 0.0908  -0.0702 -0.2406 213 LEU   H CB  
14691 C  CG  . LEU   H  212 ? 1.6624 2.2250 1.9104 0.0109  -0.1122 -0.2503 213 LEU   H CG  
14692 C  CD1 . LEU   H  212 ? 1.6560 2.2625 1.9556 0.0163  -0.1548 -0.2553 213 LEU   H CD1 
14693 C  CD2 . LEU   H  212 ? 1.6223 2.3308 1.8970 -0.0136 -0.0993 -0.2794 213 LEU   H CD2 
14694 N  N   . LYS   H  213 ? 1.6405 1.9372 1.6748 -0.0216 -0.0686 -0.2132 214 LYS   H N   
14695 C  CA  . LYS   H  213 ? 1.6457 1.9627 1.7426 -0.0260 -0.0701 -0.0369 214 LYS   H CA  
14696 C  C   . LYS   H  213 ? 1.6578 1.8155 1.7950 -0.0747 -0.0419 -0.0472 214 LYS   H C   
14697 O  O   . LYS   H  213 ? 1.6796 1.8892 1.7630 -0.1229 -0.0304 -0.0764 214 LYS   H O   
14698 C  CB  . LYS   H  213 ? 1.6968 1.8750 1.7261 0.0025  -0.1333 0.0187  214 LYS   H CB  
14699 C  CG  . LYS   H  213 ? 1.8061 1.9480 1.7303 0.0055  -0.1795 0.0477  214 LYS   H CG  
14700 C  CD  . LYS   H  213 ? 1.8434 1.9633 1.7906 0.0429  -0.1985 0.0455  214 LYS   H CD  
14701 C  CE  . LYS   H  213 ? 1.8601 2.0539 1.8322 0.0553  -0.2347 0.0427  214 LYS   H CE  
14702 N  NZ  . LYS   H  213 ? 1.8597 2.0549 1.8555 0.0588  -0.2281 0.0383  214 LYS   H NZ  
14703 N  N   . GLU   H  214 ? 1.7363 1.7615 1.7144 0.0104  0.0263  0.0612  215 GLU   H N   
14704 C  CA  . GLU   H  214 ? 1.7114 1.7608 1.6853 -0.0138 0.0631  0.0712  215 GLU   H CA  
14705 C  C   . GLU   H  214 ? 1.6929 1.8019 1.5641 0.0117  0.0782  0.1094  215 GLU   H C   
14706 O  O   . GLU   H  214 ? 1.6642 1.9749 1.5368 0.0513  0.1178  0.1125  215 GLU   H O   
14707 C  CB  . GLU   H  214 ? 1.7096 1.7436 1.7717 -0.0961 0.0735  0.0814  215 GLU   H CB  
14708 C  CG  . GLU   H  214 ? 1.6962 1.7241 1.8445 -0.1314 0.0434  0.0807  215 GLU   H CG  
14709 C  CD  . GLU   H  214 ? 1.7291 1.6898 1.8918 -0.2589 0.0260  0.0634  215 GLU   H CD  
14710 O  OE1 . GLU   H  214 ? 1.7556 1.6583 1.8693 -0.2464 0.0257  0.0854  215 GLU   H OE1 
14711 O  OE2 . GLU   H  214 ? 1.6840 1.8185 1.9642 -0.1939 0.0038  0.0952  215 GLU   H OE2 
14712 N  N   . SER   H  215 ? 1.6992 1.7131 1.6083 -0.0397 0.0541  0.1095  216 SER   H N   
14713 C  CA  . SER   H  215 ? 1.7126 1.7011 1.6438 -0.0636 0.0439  0.1727  216 SER   H CA  
14714 C  C   . SER   H  215 ? 1.7272 1.5841 1.7101 -0.0544 0.0490  0.1522  216 SER   H C   
14715 O  O   . SER   H  215 ? 1.7259 1.4594 1.7508 -0.0913 0.0932  0.1375  216 SER   H O   
14716 C  CB  . SER   H  215 ? 1.7373 1.7023 1.5736 -0.0518 0.0045  0.1586  216 SER   H CB  
14717 O  OG  . SER   H  215 ? 1.6514 1.7244 1.5553 -0.0530 -0.0172 0.1256  216 SER   H OG  
14718 N  N   . ILE   H  216 ? 1.7441 1.5592 1.7421 0.0166  0.0504  0.2497  217 ILE   H N   
14719 C  CA  . ILE   H  216 ? 1.7108 1.4373 1.7410 0.0409  0.0527  0.2922  217 ILE   H CA  
14720 C  C   . ILE   H  216 ? 1.7393 1.3681 1.7276 0.1325  -0.0038 0.3127  217 ILE   H C   
14721 O  O   . ILE   H  216 ? 1.7473 1.2710 1.7104 0.2222  0.0925  0.3645  217 ILE   H O   
14722 C  CB  . ILE   H  216 ? 1.7650 1.4040 1.7278 0.0431  0.0326  0.3366  217 ILE   H CB  
14723 C  CG1 . ILE   H  216 ? 1.7450 1.4213 1.7698 0.0033  0.0496  0.3319  217 ILE   H CG1 
14724 C  CG2 . ILE   H  216 ? 1.7196 1.3015 1.7200 0.0312  0.0446  0.3776  217 ILE   H CG2 
14725 C  CD1 . ILE   H  216 ? 1.7099 1.4127 1.7831 -0.0076 0.0237  0.2983  217 ILE   H CD1 
14726 N  N   . VAL   H  217 ? 1.7861 1.3566 1.7356 0.1185  0.0126  0.2161  218 VAL   H N   
14727 C  CA  . VAL   H  217 ? 1.7971 1.4069 1.8092 0.1594  -0.0055 0.2094  218 VAL   H CA  
14728 C  C   . VAL   H  217 ? 1.8423 1.4699 1.8523 0.0745  -0.0370 0.1811  218 VAL   H C   
14729 O  O   . VAL   H  217 ? 1.8267 1.5474 1.9493 0.1211  -0.0754 0.1970  218 VAL   H O   
14730 C  CB  . VAL   H  217 ? 1.8612 1.3323 1.8210 0.1352  -0.0063 0.1847  218 VAL   H CB  
14731 C  CG1 . VAL   H  217 ? 1.8862 1.2245 1.7754 0.1588  0.0027  0.2074  218 VAL   H CG1 
14732 C  CG2 . VAL   H  217 ? 1.9058 1.3734 1.8549 0.1336  -0.0092 0.1196  218 VAL   H CG2 
14733 N  N   . ASN   H  218 ? 1.7997 1.5800 1.8351 0.0841  -0.0381 0.2344  219 ASN   H N   
14734 C  CA  . ASN   H  218 ? 1.8201 1.5852 1.8539 0.0709  -0.0378 0.2284  219 ASN   H CA  
14735 C  C   . ASN   H  218 ? 1.8697 1.5913 1.8703 0.0291  0.0001  0.2326  219 ASN   H C   
14736 O  O   . ASN   H  218 ? 1.8684 1.5552 1.7536 0.0135  -0.1185 0.2828  219 ASN   H O   
14737 C  CB  . ASN   H  218 ? 1.7813 1.6408 1.9045 0.1280  -0.0792 0.2247  219 ASN   H CB  
14738 C  CG  . ASN   H  218 ? 1.7588 1.6588 1.9557 0.1043  -0.1155 0.2097  219 ASN   H CG  
14739 O  OD1 . ASN   H  218 ? 1.7483 1.5964 1.9696 0.1267  -0.1597 0.2142  219 ASN   H OD1 
14740 N  ND2 . ASN   H  218 ? 1.7404 1.7261 1.9704 0.1049  -0.1066 0.1738  219 ASN   H ND2 
14741 N  N   . ILE   H  219 ? 1.9442 1.6245 1.8547 -0.0016 0.0411  0.1334  220 ILE   H N   
14742 C  CA  . ILE   H  219 ? 1.9981 1.6523 1.9316 0.0270  0.1265  0.0908  220 ILE   H CA  
14743 C  C   . ILE   H  219 ? 1.9757 1.6643 2.0191 0.0395  0.1803  0.0773  220 ILE   H C   
14744 O  O   . ILE   H  219 ? 1.9400 1.7322 2.0229 0.0105  0.2254  0.1339  220 ILE   H O   
14745 C  CB  . ILE   H  219 ? 2.0636 1.5027 1.8542 0.0439  0.1707  0.0523  220 ILE   H CB  
14746 C  CG1 . ILE   H  219 ? 2.0620 1.3873 1.7904 0.0513  0.1788  0.0328  220 ILE   H CG1 
14747 C  CG2 . ILE   H  219 ? 2.0885 1.5055 1.8312 0.0389  0.1647  0.0991  220 ILE   H CG2 
14748 C  CD1 . ILE   H  219 ? 2.0437 1.2766 1.7386 0.0332  0.2050  0.0021  220 ILE   H CD1 
14749 N  N   . CYS   H  220 ? 1.9103 1.9405 2.1523 0.0042  0.2003  0.1802  221 CYS   H N   
14750 C  CA  . CYS   H  220 ? 1.8611 1.9792 2.3205 0.0152  0.1775  0.0868  221 CYS   H CA  
14751 C  C   . CYS   H  220 ? 1.8249 2.2062 2.4084 0.0550  0.1512  0.0150  221 CYS   H C   
14752 O  O   . CYS   H  220 ? 1.8079 2.3543 2.4881 0.0431  0.1607  -0.0964 221 CYS   H O   
14753 C  CB  . CYS   H  220 ? 1.7790 2.1103 2.3847 0.0133  0.1437  0.1079  221 CYS   H CB  
14754 S  SG  . CYS   H  220 ? 1.5956 2.3031 2.3827 -0.2044 0.1138  0.0888  221 CYS   H SG  
14755 N  N   . ASP   H  221 ? 1.8810 2.2183 2.4612 0.0240  0.1789  -0.0208 222 ASP   H N   
14756 C  CA  . ASP   H  221 ? 1.8823 2.2764 2.2798 -0.0111 0.1829  0.0791  222 ASP   H CA  
14757 C  C   . ASP   H  221 ? 1.8481 2.1418 2.2680 0.0032  0.1046  0.1573  222 ASP   H C   
14758 O  O   . ASP   H  221 ? 1.8304 2.1473 1.8515 0.0855  0.0750  0.2807  222 ASP   H O   
14759 C  CB  . ASP   H  221 ? 1.8801 2.2619 2.5024 -0.0165 0.1652  0.0009  222 ASP   H CB  
14760 C  CG  . ASP   H  221 ? 1.8531 2.3552 2.5419 -0.0407 0.2226  -0.0475 222 ASP   H CG  
14761 O  OD1 . ASP   H  221 ? 1.6974 2.5214 2.5719 0.0006  0.1728  -0.1673 222 ASP   H OD1 
14762 O  OD2 . ASP   H  221 ? 1.9354 2.3576 2.6749 -0.1138 0.2002  -0.1458 222 ASP   H OD2 
14763 N  N   . SER   I  2   ? 2.0480 1.3550 1.9016 0.4575  -0.3924 -0.3969 1   SER   I N   
14764 C  CA  . SER   I  2   ? 1.9665 1.2935 1.9171 0.4189  -0.3411 -0.3460 1   SER   I CA  
14765 C  C   . SER   I  2   ? 1.9637 1.2793 1.8750 0.3404  -0.3036 -0.2611 1   SER   I C   
14766 O  O   . SER   I  2   ? 1.9397 1.4932 1.9920 0.4092  -0.1107 -0.0872 1   SER   I O   
14767 C  CB  . SER   I  2   ? 1.9331 1.2271 1.8783 0.4309  -0.3944 -0.4269 1   SER   I CB  
14768 O  OG  . SER   I  2   ? 1.8530 1.2999 1.9245 0.4150  -0.4061 -0.4964 1   SER   I OG  
14769 N  N   . ASP   I  3   ? 1.9624 1.1031 1.9204 0.2622  -0.1989 -0.1831 2   ASP   I N   
14770 C  CA  . ASP   I  3   ? 1.9092 0.9582 1.7651 0.2144  -0.1237 -0.0511 2   ASP   I CA  
14771 C  C   . ASP   I  3   ? 1.9239 0.8650 1.6733 0.2607  -0.1151 -0.0923 2   ASP   I C   
14772 O  O   . ASP   I  3   ? 1.9041 0.8084 1.7040 0.3398  -0.0804 0.1128  2   ASP   I O   
14773 C  CB  . ASP   I  3   ? 1.8971 1.0086 1.6732 0.2293  -0.1009 -0.0450 2   ASP   I CB  
14774 C  CG  . ASP   I  3   ? 1.9617 0.9211 1.5442 0.2156  -0.0302 -0.0955 2   ASP   I CG  
14775 O  OD1 . ASP   I  3   ? 2.0487 0.7775 1.5998 0.1686  -0.0400 -0.1113 2   ASP   I OD1 
14776 O  OD2 . ASP   I  3   ? 1.9117 1.0806 1.4746 0.1168  -0.0318 -0.0519 2   ASP   I OD2 
14777 N  N   . PRO   I  4   ? 1.8914 0.8225 1.4868 0.1462  -0.1138 -0.0991 3   PRO   I N   
14778 C  CA  . PRO   I  4   ? 1.8122 0.7585 1.4615 0.1196  -0.1467 -0.1640 3   PRO   I CA  
14779 C  C   . PRO   I  4   ? 1.7906 0.6624 1.3642 0.1186  -0.1880 -0.1440 3   PRO   I C   
14780 O  O   . PRO   I  4   ? 1.8106 0.4573 1.2828 0.1111  -0.2476 -0.2353 3   PRO   I O   
14781 C  CB  . PRO   I  4   ? 1.8320 0.8186 1.4538 0.1179  -0.1071 -0.1748 3   PRO   I CB  
14782 C  CG  . PRO   I  4   ? 1.8551 0.7996 1.5194 0.1236  -0.1113 -0.1045 3   PRO   I CG  
14783 C  CD  . PRO   I  4   ? 1.8951 0.8075 1.5062 0.1570  -0.0994 -0.1150 3   PRO   I CD  
14784 N  N   . SER   I  5   ? 1.7563 0.7474 1.4007 0.1104  -0.1587 -0.0480 4   SER   I N   
14785 C  CA  . SER   I  5   ? 1.7505 0.8236 1.3179 0.1304  -0.1500 0.0132  4   SER   I CA  
14786 C  C   . SER   I  5   ? 1.7109 0.7638 1.3190 0.1001  -0.1836 -0.0030 4   SER   I C   
14787 O  O   . SER   I  5   ? 1.7028 0.6702 1.3120 0.1726  -0.1628 -0.1213 4   SER   I O   
14788 C  CB  . SER   I  5   ? 1.7560 0.9481 1.3170 0.1178  -0.1410 0.0830  4   SER   I CB  
14789 O  OG  . SER   I  5   ? 1.8425 0.9872 1.2852 0.1214  -0.1148 0.1115  4   SER   I OG  
14790 N  N   . SER   I  6   ? 1.7030 0.7391 1.3190 0.0726  -0.1948 0.0603  5   SER   I N   
14791 C  CA  . SER   I  6   ? 1.7253 0.8152 1.3174 0.0302  -0.1937 0.0045  5   SER   I CA  
14792 C  C   . SER   I  6   ? 1.6983 0.7952 1.3284 0.0697  -0.2036 0.0424  5   SER   I C   
14793 O  O   . SER   I  6   ? 1.7681 0.8605 1.3207 0.1405  -0.1904 -0.0074 5   SER   I O   
14794 C  CB  . SER   I  6   ? 1.8104 0.8458 1.3769 0.0797  -0.1893 0.0273  5   SER   I CB  
14795 O  OG  . SER   I  6   ? 1.8668 1.0443 1.4671 0.0365  -0.1243 0.0167  5   SER   I OG  
14796 N  N   . ILE   I  7   ? 1.5727 0.6938 1.2384 -0.0029 -0.2351 -0.0579 6   ILE   I N   
14797 C  CA  . ILE   I  7   ? 1.5440 0.6613 1.2399 0.0255  -0.2351 -0.0585 6   ILE   I CA  
14798 C  C   . ILE   I  7   ? 1.5108 0.6119 1.2330 0.0617  -0.2663 -0.0024 6   ILE   I C   
14799 O  O   . ILE   I  7   ? 1.4611 0.5138 1.2512 -0.0120 -0.3215 0.0359  6   ILE   I O   
14800 C  CB  . ILE   I  7   ? 1.4880 0.7557 1.1783 0.0240  -0.2593 -0.0817 6   ILE   I CB  
14801 C  CG1 . ILE   I  7   ? 1.4670 0.8126 1.2081 0.0194  -0.2460 -0.1010 6   ILE   I CG1 
14802 C  CG2 . ILE   I  7   ? 1.5178 0.8046 1.1698 0.0195  -0.2592 -0.0844 6   ILE   I CG2 
14803 C  CD1 . ILE   I  7   ? 1.4995 0.7932 1.2350 0.0271  -0.2470 -0.0965 6   ILE   I CD1 
14804 N  N   . ASN   I  8   ? 1.5011 0.5749 1.2392 0.0935  -0.2441 0.0054  7   ASN   I N   
14805 C  CA  . ASN   I  8   ? 1.5394 0.6188 1.2629 0.1400  -0.2016 0.0263  7   ASN   I CA  
14806 C  C   . ASN   I  8   ? 1.5592 0.5806 1.2858 0.1573  -0.1581 0.0892  7   ASN   I C   
14807 O  O   . ASN   I  8   ? 1.5766 0.5957 1.2606 0.1567  -0.1451 0.2308  7   ASN   I O   
14808 C  CB  . ASN   I  8   ? 1.5304 0.6214 1.2889 0.1307  -0.1999 0.0142  7   ASN   I CB  
14809 C  CG  . ASN   I  8   ? 1.5377 0.6128 1.3231 0.1381  -0.2211 -0.0233 7   ASN   I CG  
14810 O  OD1 . ASN   I  8   ? 1.4986 0.6092 1.3267 0.0805  -0.2285 -0.0404 7   ASN   I OD1 
14811 N  ND2 . ASN   I  8   ? 1.5834 0.5896 1.3561 0.1607  -0.2452 -0.0829 7   ASN   I ND2 
14812 N  N   . GLY   I  9   ? 1.5598 0.5560 1.3128 0.1611  -0.1736 0.0998  8   GLY   I N   
14813 C  CA  . GLY   I  9   ? 1.5167 0.5773 1.3574 0.1212  -0.1533 0.0538  8   GLY   I CA  
14814 C  C   . GLY   I  9   ? 1.5441 0.5514 1.3447 0.1189  -0.1402 0.0699  8   GLY   I C   
14815 O  O   . GLY   I  9   ? 1.6448 0.5880 1.3830 0.1599  -0.1393 0.1271  8   GLY   I O   
14816 N  N   . GLY   I  10  ? 1.5001 0.5853 1.3358 0.0606  -0.1122 0.0248  9   GLY   I N   
14817 C  CA  . GLY   I  10  ? 1.5243 0.5980 1.3101 0.0388  -0.0973 0.0198  9   GLY   I CA  
14818 C  C   . GLY   I  10  ? 1.5232 0.5572 1.3000 -0.0312 -0.0918 0.0060  9   GLY   I C   
14819 O  O   . GLY   I  10  ? 1.5381 0.4912 1.2737 -0.0404 -0.1134 -0.0103 9   GLY   I O   
14820 N  N   . ILE   I  11  ? 1.5212 0.5955 1.2941 -0.0385 -0.1044 -0.0140 10  ILE   I N   
14821 C  CA  . ILE   I  11  ? 1.5040 0.6482 1.3135 0.0221  -0.1106 -0.0123 10  ILE   I CA  
14822 C  C   . ILE   I  11  ? 1.5026 0.6395 1.3502 0.0338  -0.1005 -0.0120 10  ILE   I C   
14823 O  O   . ILE   I  11  ? 1.4420 0.6032 1.3205 0.0483  -0.0297 -0.0653 10  ILE   I O   
14824 C  CB  . ILE   I  11  ? 1.4579 0.6592 1.3138 0.0141  -0.1114 -0.0410 10  ILE   I CB  
14825 C  CG1 . ILE   I  11  ? 1.4589 0.7037 1.3165 0.0353  -0.1042 -0.0530 10  ILE   I CG1 
14826 C  CG2 . ILE   I  11  ? 1.4449 0.6855 1.3609 -0.0179 -0.1228 -0.0415 10  ILE   I CG2 
14827 C  CD1 . ILE   I  11  ? 1.4363 0.7767 1.3373 0.0494  -0.0884 -0.0673 10  ILE   I CD1 
14828 N  N   . VAL   I  12  ? 1.5126 0.6069 1.3943 0.0528  -0.1519 0.0005  11  VAL   I N   
14829 C  CA  . VAL   I  12  ? 1.5550 0.6588 1.4711 0.0010  -0.1466 0.0432  11  VAL   I CA  
14830 C  C   . VAL   I  12  ? 1.5543 0.5529 1.4804 0.0444  -0.1147 0.0361  11  VAL   I C   
14831 O  O   . VAL   I  12  ? 1.6267 0.4866 1.4893 0.0188  -0.0812 -0.0075 11  VAL   I O   
14832 C  CB  . VAL   I  12  ? 1.5810 0.7442 1.4976 0.0765  -0.1825 0.0385  11  VAL   I CB  
14833 C  CG1 . VAL   I  12  ? 1.5658 0.8081 1.5025 0.0510  -0.2053 0.0651  11  VAL   I CG1 
14834 C  CG2 . VAL   I  12  ? 1.6149 0.8717 1.5140 0.0563  -0.2206 0.0572  11  VAL   I CG2 
14835 N  N   . VAL   I  13  ? 1.5733 0.5773 1.4724 0.0453  -0.0534 0.0495  12  VAL   I N   
14836 C  CA  . VAL   I  13  ? 1.6156 0.5899 1.4388 0.0326  -0.0629 0.0750  12  VAL   I CA  
14837 C  C   . VAL   I  13  ? 1.6302 0.6119 1.4366 0.0142  -0.0748 0.0616  12  VAL   I C   
14838 O  O   . VAL   I  13  ? 1.6287 0.5705 1.4628 0.0011  -0.0279 0.0556  12  VAL   I O   
14839 C  CB  . VAL   I  13  ? 1.6692 0.5669 1.4177 0.0357  -0.0329 0.1097  12  VAL   I CB  
14840 C  CG1 . VAL   I  13  ? 1.6964 0.5976 1.4261 0.0765  -0.0095 0.0868  12  VAL   I CG1 
14841 C  CG2 . VAL   I  13  ? 1.6722 0.5633 1.4705 0.0272  -0.0547 0.1256  12  VAL   I CG2 
14842 N  N   . ALA   I  14  ? 1.6192 0.6463 1.4679 -0.0142 -0.0807 0.0266  13  ALA   I N   
14843 C  CA  . ALA   I  14  ? 1.5965 0.6361 1.4506 0.0050  -0.0682 -0.0263 13  ALA   I CA  
14844 C  C   . ALA   I  14  ? 1.5769 0.6973 1.4717 -0.0005 -0.0761 -0.0350 13  ALA   I C   
14845 O  O   . ALA   I  14  ? 1.5024 0.7152 1.3712 0.0364  -0.1141 -0.0628 13  ALA   I O   
14846 C  CB  . ALA   I  14  ? 1.5775 0.5888 1.4360 -0.0322 -0.0979 -0.0362 13  ALA   I CB  
14847 N  N   . MET   I  15  ? 1.6013 0.7586 1.5398 -0.0072 -0.0352 -0.0298 14  MET   I N   
14848 C  CA  . MET   I  15  ? 1.6749 0.8448 1.5922 -0.0020 -0.0788 0.0625  14  MET   I CA  
14849 C  C   . MET   I  15  ? 1.6910 0.8568 1.5952 -0.0083 -0.0959 0.0493  14  MET   I C   
14850 O  O   . MET   I  15  ? 1.7059 0.7854 1.7246 -0.0080 -0.0206 0.0702  14  MET   I O   
14851 C  CB  . MET   I  15  ? 1.7585 0.8231 1.6341 0.0104  -0.0319 0.0895  14  MET   I CB  
14852 C  CG  . MET   I  15  ? 1.8200 0.8191 1.6346 0.0430  -0.0138 0.1452  14  MET   I CG  
14853 S  SD  . MET   I  15  ? 1.9082 0.8751 1.6659 0.1043  0.0266  0.1649  14  MET   I SD  
14854 C  CE  . MET   I  15  ? 1.9142 0.9192 1.7148 0.0866  0.0130  0.2183  14  MET   I CE  
14855 N  N   . THR   I  16  ? 1.7150 0.8806 1.5524 -0.0193 -0.0914 0.0904  15  THR   I N   
14856 C  CA  . THR   I  16  ? 1.6672 0.8960 1.5076 -0.0045 -0.1334 0.1291  15  THR   I CA  
14857 C  C   . THR   I  16  ? 1.6282 0.9760 1.5584 -0.0156 -0.1483 0.1347  15  THR   I C   
14858 O  O   . THR   I  16  ? 1.6363 0.9587 1.5842 -0.0133 -0.1655 0.0842  15  THR   I O   
14859 C  CB  . THR   I  16  ? 1.6829 0.8676 1.4937 -0.0075 -0.1349 0.1551  15  THR   I CB  
14860 O  OG1 . THR   I  16  ? 1.7727 0.8810 1.5347 -0.0190 -0.1269 0.1923  15  THR   I OG1 
14861 C  CG2 . THR   I  16  ? 1.6780 0.8378 1.4079 -0.0081 -0.1461 0.1675  15  THR   I CG2 
14862 N  N   . GLY   I  17  ? 1.5733 1.0622 1.5927 -0.0001 -0.1267 0.1670  16  GLY   I N   
14863 C  CA  . GLY   I  17  ? 1.5764 1.1337 1.6858 0.0183  -0.1209 0.1879  16  GLY   I CA  
14864 C  C   . GLY   I  17  ? 1.5806 1.1246 1.7342 0.0322  -0.1519 0.1874  16  GLY   I C   
14865 O  O   . GLY   I  17  ? 1.5277 0.9710 1.6720 0.0433  -0.2156 0.2507  16  GLY   I O   
14866 N  N   . LYS   I  18  ? 1.5675 1.2004 1.8846 -0.0084 -0.1577 0.1862  17  LYS   I N   
14867 C  CA  . LYS   I  18  ? 1.6466 1.2076 1.9501 -0.0317 -0.1625 0.1372  17  LYS   I CA  
14868 C  C   . LYS   I  18  ? 1.6089 1.1778 1.9377 -0.0001 -0.1236 0.0967  17  LYS   I C   
14869 O  O   . LYS   I  18  ? 1.5454 1.0966 1.9627 0.0709  -0.0793 0.1063  17  LYS   I O   
14870 C  CB  . LYS   I  18  ? 1.6285 1.3573 2.0673 -0.0479 -0.1690 0.1424  17  LYS   I CB  
14871 C  CG  . LYS   I  18  ? 1.7302 1.4554 2.1298 -0.1143 -0.1881 0.0780  17  LYS   I CG  
14872 C  CD  . LYS   I  18  ? 1.6821 1.5642 2.2325 -0.1259 -0.1938 0.0226  17  LYS   I CD  
14873 C  CE  . LYS   I  18  ? 1.7483 1.6238 2.3166 -0.2006 -0.1733 -0.0332 17  LYS   I CE  
14874 N  NZ  . LYS   I  18  ? 1.8137 1.6876 2.3092 -0.2399 -0.1818 -0.0825 17  LYS   I NZ  
14875 N  N   . ASP   I  19  ? 1.6143 1.1928 1.8826 -0.0103 -0.1449 0.0920  18  ASP   I N   
14876 C  CA  . ASP   I  19  ? 1.6322 1.1985 1.8980 0.0212  -0.1008 0.0971  18  ASP   I CA  
14877 C  C   . ASP   I  19  ? 1.6035 1.1425 1.8552 -0.0074 -0.0468 0.0305  18  ASP   I C   
14878 O  O   . ASP   I  19  ? 1.6815 1.2035 1.8526 0.0784  0.0755  0.0442  18  ASP   I O   
14879 C  CB  . ASP   I  19  ? 1.6031 1.2283 1.9218 0.0210  -0.1400 0.1261  18  ASP   I CB  
14880 C  CG  . ASP   I  19  ? 1.5576 1.2581 2.0165 -0.0193 -0.1756 0.1590  18  ASP   I CG  
14881 O  OD1 . ASP   I  19  ? 1.6093 1.2739 2.0200 0.0532  -0.1886 0.1564  18  ASP   I OD1 
14882 O  OD2 . ASP   I  19  ? 1.5675 1.3501 2.0615 -0.0833 -0.1057 0.1973  18  ASP   I OD2 
14883 N  N   . CYS   I  20  ? 1.6599 1.0474 1.8278 0.0072  0.0270  0.0654  19  CYS   I N   
14884 C  CA  . CYS   I  20  ? 1.6379 0.9461 1.8131 0.0126  0.0464  0.0580  19  CYS   I CA  
14885 C  C   . CYS   I  20  ? 1.6160 0.8710 1.6963 0.0336  0.0118  0.0288  19  CYS   I C   
14886 O  O   . CYS   I  20  ? 1.5574 0.8647 1.6358 -0.0326 0.0247  -0.0015 19  CYS   I O   
14887 C  CB  . CYS   I  20  ? 1.6789 0.9242 1.8556 0.0147  0.0891  0.0623  19  CYS   I CB  
14888 S  SG  . CYS   I  20  ? 1.7695 0.8862 1.9559 0.0206  0.1140  -0.0044 19  CYS   I SG  
14889 N  N   . VAL   I  21  ? 1.6494 0.7750 1.6314 0.0810  0.0107  0.0066  20  VAL   I N   
14890 C  CA  . VAL   I  21  ? 1.6727 0.7145 1.5319 0.0911  0.0005  0.0153  20  VAL   I CA  
14891 C  C   . VAL   I  21  ? 1.6370 0.7101 1.5441 0.0962  -0.0062 0.0028  20  VAL   I C   
14892 O  O   . VAL   I  21  ? 1.5973 0.7119 1.5285 0.1679  -0.0014 -0.0016 20  VAL   I O   
14893 C  CB  . VAL   I  21  ? 1.7037 0.7261 1.4873 0.1009  0.0093  0.0322  20  VAL   I CB  
14894 C  CG1 . VAL   I  21  ? 1.7251 0.7040 1.4955 0.0882  -0.0126 0.0513  20  VAL   I CG1 
14895 C  CG2 . VAL   I  21  ? 1.7200 0.7178 1.5311 0.1150  0.0011  0.0091  20  VAL   I CG2 
14896 N  N   . ALA   I  22  ? 1.5793 0.7690 1.4588 0.0507  -0.0323 0.0020  21  ALA   I N   
14897 C  CA  . ALA   I  22  ? 1.5401 0.7178 1.4668 0.0362  0.0066  -0.0186 21  ALA   I CA  
14898 C  C   . ALA   I  22  ? 1.5247 0.6522 1.3709 0.0414  -0.0130 -0.0149 21  ALA   I C   
14899 O  O   . ALA   I  22  ? 1.4781 0.6182 1.3242 0.0306  -0.0373 -0.0603 21  ALA   I O   
14900 C  CB  . ALA   I  22  ? 1.5853 0.7048 1.5058 0.0292  0.0111  -0.0419 21  ALA   I CB  
14901 N  N   . ILE   I  23  ? 1.5132 0.5920 1.3796 0.0555  -0.0014 -0.0041 22  ILE   I N   
14902 C  CA  . ILE   I  23  ? 1.5107 0.5464 1.3523 0.0684  -0.0216 0.0058  22  ILE   I CA  
14903 C  C   . ILE   I  23  ? 1.5251 0.5341 1.3527 0.1000  -0.0370 0.0125  22  ILE   I C   
14904 O  O   . ILE   I  23  ? 1.5104 0.4733 1.3990 0.1148  -0.0151 0.0270  22  ILE   I O   
14905 C  CB  . ILE   I  23  ? 1.5081 0.5410 1.2750 0.0553  -0.0273 -0.0005 22  ILE   I CB  
14906 C  CG1 . ILE   I  23  ? 1.5031 0.5386 1.2100 0.0465  -0.0509 -0.0044 22  ILE   I CG1 
14907 C  CG2 . ILE   I  23  ? 1.5484 0.5880 1.2680 0.0497  -0.0184 0.0226  22  ILE   I CG2 
14908 C  CD1 . ILE   I  23  ? 1.4732 0.5668 1.1899 0.0306  -0.0572 -0.0098 22  ILE   I CD1 
14909 N  N   . ALA   I  24  ? 1.5319 0.5203 1.4256 0.1148  -0.0686 -0.0236 23  ALA   I N   
14910 C  CA  . ALA   I  24  ? 1.5298 0.4856 1.4643 0.1370  -0.0828 -0.0407 23  ALA   I CA  
14911 C  C   . ALA   I  24  ? 1.5123 0.4178 1.4470 0.1669  -0.0972 -0.0451 23  ALA   I C   
14912 O  O   . ALA   I  24  ? 1.4273 0.3499 1.4174 0.2169  -0.1160 -0.0856 23  ALA   I O   
14913 C  CB  . ALA   I  24  ? 1.5368 0.4805 1.5080 0.1296  -0.0570 -0.0616 23  ALA   I CB  
14914 N  N   . CYS   I  25  ? 1.5572 0.4280 1.4561 0.1841  -0.1199 -0.0435 24  CYS   I N   
14915 C  CA  . CYS   I  25  ? 1.5723 0.5126 1.4832 0.1621  -0.1282 -0.0399 24  CYS   I CA  
14916 C  C   . CYS   I  25  ? 1.5973 0.6245 1.4558 0.1624  -0.1197 -0.0424 24  CYS   I C   
14917 O  O   . CYS   I  25  ? 1.5793 0.6790 1.5547 0.1668  -0.0785 0.0316  24  CYS   I O   
14918 C  CB  . CYS   I  25  ? 1.6048 0.5166 1.4590 0.1741  -0.1233 -0.0518 24  CYS   I CB  
14919 S  SG  . CYS   I  25  ? 1.6991 0.5413 1.4747 0.1298  -0.1353 -0.0301 24  CYS   I SG  
14920 N  N   . ASP   I  26  ? 1.5961 0.7524 1.4785 0.1082  -0.1368 -0.0796 25  ASP   I N   
14921 C  CA  . ASP   I  26  ? 1.6255 0.8143 1.5037 0.1129  -0.1087 -0.1495 25  ASP   I CA  
14922 C  C   . ASP   I  26  ? 1.6153 0.8634 1.4459 0.1009  -0.1261 -0.1492 25  ASP   I C   
14923 O  O   . ASP   I  26  ? 1.5697 0.8994 1.5805 0.1689  -0.1174 -0.1748 25  ASP   I O   
14924 C  CB  . ASP   I  26  ? 1.6304 0.8286 1.4988 0.0709  -0.1050 -0.2138 25  ASP   I CB  
14925 C  CG  . ASP   I  26  ? 1.6223 0.8486 1.4847 0.0744  -0.1244 -0.2482 25  ASP   I CG  
14926 O  OD1 . ASP   I  26  ? 1.6223 0.8690 1.4405 0.1151  -0.1352 -0.2347 25  ASP   I OD1 
14927 O  OD2 . ASP   I  26  ? 1.6402 0.9572 1.5044 0.0498  -0.1495 -0.3305 25  ASP   I OD2 
14928 N  N   . LEU   I  27  ? 1.6380 0.8339 1.3918 0.1044  -0.0726 -0.1550 26  LEU   I N   
14929 C  CA  . LEU   I  27  ? 1.6692 0.8364 1.3129 0.1005  -0.0485 -0.1544 26  LEU   I CA  
14930 C  C   . LEU   I  27  ? 1.6570 0.7530 1.2774 0.1404  -0.0831 -0.1423 26  LEU   I C   
14931 O  O   . LEU   I  27  ? 1.7152 0.4961 1.3263 0.2182  -0.0543 -0.2395 26  LEU   I O   
14932 C  CB  . LEU   I  27  ? 1.7418 0.9471 1.3416 0.0890  -0.0058 -0.1312 26  LEU   I CB  
14933 C  CG  . LEU   I  27  ? 1.7657 0.9409 1.3713 0.0776  -0.0074 -0.1098 26  LEU   I CG  
14934 C  CD1 . LEU   I  27  ? 1.8844 1.0494 1.4037 0.0602  0.0228  -0.0357 26  LEU   I CD1 
14935 C  CD2 . LEU   I  27  ? 1.6971 0.9116 1.2765 0.0665  -0.0200 -0.0715 26  LEU   I CD2 
14936 N  N   . ARG   I  28  ? 1.6056 0.8270 1.2683 0.0676  -0.0771 -0.1107 27  ARG   I N   
14937 C  CA  . ARG   I  28  ? 1.5637 0.8472 1.2240 0.0873  -0.0774 -0.0938 27  ARG   I CA  
14938 C  C   . ARG   I  28  ? 1.5220 0.7535 1.1463 0.0341  -0.0889 -0.0965 27  ARG   I C   
14939 O  O   . ARG   I  28  ? 1.4514 0.7077 1.1534 0.0085  -0.0496 -0.1079 27  ARG   I O   
14940 C  CB  . ARG   I  28  ? 1.5617 0.8824 1.2667 0.0769  -0.1339 -0.0392 27  ARG   I CB  
14941 C  CG  . ARG   I  28  ? 1.5837 0.9547 1.3011 0.0639  -0.1962 -0.0263 27  ARG   I CG  
14942 C  CD  . ARG   I  28  ? 1.6594 0.9628 1.3684 0.0093  -0.2217 0.0045  27  ARG   I CD  
14943 N  NE  . ARG   I  28  ? 1.7234 1.0591 1.4248 -0.0228 -0.3323 0.0254  27  ARG   I NE  
14944 C  CZ  . ARG   I  28  ? 1.6834 1.0925 1.4243 -0.0117 -0.3857 0.0114  27  ARG   I CZ  
14945 N  NH1 . ARG   I  28  ? 1.7473 1.0653 1.4370 -0.0066 -0.3691 0.0046  27  ARG   I NH1 
14946 N  NH2 . ARG   I  28  ? 1.7224 1.1334 1.4619 0.0201  -0.5157 0.0035  27  ARG   I NH2 
14947 N  N   . LEU   I  29  ? 1.5073 0.6674 1.1500 0.1017  -0.0650 -0.0989 28  LEU   I N   
14948 C  CA  . LEU   I  29  ? 1.5241 0.6673 1.1673 0.1314  -0.0581 -0.1193 28  LEU   I CA  
14949 C  C   . LEU   I  29  ? 1.5193 0.6843 1.1806 0.1731  -0.0803 -0.1644 28  LEU   I C   
14950 O  O   . LEU   I  29  ? 1.5519 0.6860 1.1783 0.2122  -0.0757 -0.1692 28  LEU   I O   
14951 C  CB  . LEU   I  29  ? 1.5351 0.6434 1.1742 0.0953  -0.0469 -0.1246 28  LEU   I CB  
14952 C  CG  . LEU   I  29  ? 1.5125 0.6610 1.1825 0.0838  -0.0583 -0.1201 28  LEU   I CG  
14953 C  CD1 . LEU   I  29  ? 1.4881 0.6337 1.2000 0.0998  -0.0515 -0.0866 28  LEU   I CD1 
14954 C  CD2 . LEU   I  29  ? 1.5087 0.6733 1.1944 0.1101  -0.0680 -0.1194 28  LEU   I CD2 
14955 N  N   . GLY   I  30  ? 1.4757 0.7195 1.1809 0.1599  -0.0393 -0.2058 29  GLY   I N   
14956 C  CA  . GLY   I  30  ? 1.4835 0.7328 1.1965 0.1716  -0.0286 -0.2700 29  GLY   I CA  
14957 C  C   . GLY   I  30  ? 1.4839 0.7018 1.2064 0.1888  -0.0265 -0.2804 29  GLY   I C   
14958 O  O   . GLY   I  30  ? 1.4163 0.6928 1.1993 0.2878  0.0123  -0.2424 29  GLY   I O   
14959 N  N   . SER   I  31  ? 1.5006 0.7216 1.2546 0.1773  -0.0351 -0.3057 30  SER   I N   
14960 C  CA  . SER   I  31  ? 1.4631 0.7151 1.3343 0.1481  -0.0629 -0.3063 30  SER   I CA  
14961 C  C   . SER   I  31  ? 1.5196 0.7248 1.3860 0.1308  -0.0908 -0.2955 30  SER   I C   
14962 O  O   . SER   I  31  ? 1.5390 0.6679 1.4975 0.1323  -0.0731 -0.3503 30  SER   I O   
14963 C  CB  . SER   I  31  ? 1.4948 0.6753 1.3737 0.1505  -0.0945 -0.3102 30  SER   I CB  
14964 O  OG  . SER   I  31  ? 1.4620 0.6316 1.4534 0.1375  -0.1000 -0.2936 30  SER   I OG  
14965 N  N   . GLN   I  32  ? 1.5734 0.7289 1.4273 0.1474  -0.1034 -0.2295 31  GLN   I N   
14966 C  CA  . GLN   I  32  ? 1.5859 0.7261 1.5024 0.1358  -0.1250 -0.2091 31  GLN   I CA  
14967 C  C   . GLN   I  32  ? 1.5874 0.7776 1.4495 0.1161  -0.1319 -0.2009 31  GLN   I C   
14968 O  O   . GLN   I  32  ? 1.6017 0.7826 1.3706 0.0910  -0.1357 -0.1428 31  GLN   I O   
14969 C  CB  . GLN   I  32  ? 1.5848 0.7408 1.5600 0.1422  -0.1197 -0.1567 31  GLN   I CB  
14970 C  CG  . GLN   I  32  ? 1.6165 0.7383 1.5507 0.1414  -0.0900 -0.1007 31  GLN   I CG  
14971 C  CD  . GLN   I  32  ? 1.5990 0.8534 1.6188 0.1747  -0.0934 -0.0576 31  GLN   I CD  
14972 O  OE1 . GLN   I  32  ? 1.6902 1.0666 1.6114 0.2421  -0.0564 0.0259  31  GLN   I OE1 
14973 N  NE2 . GLN   I  32  ? 1.6860 0.8240 1.6459 0.2103  -0.1040 -0.0085 31  GLN   I NE2 
14974 N  N   . SER   I  33  ? 1.6573 0.8430 1.4634 0.0745  -0.1940 -0.1946 32  SER   I N   
14975 C  CA  . SER   I  33  ? 1.6542 0.7409 1.4500 0.0095  -0.2271 -0.2209 32  SER   I CA  
14976 C  C   . SER   I  33  ? 1.6547 0.7855 1.4293 0.0563  -0.2159 -0.2113 32  SER   I C   
14977 O  O   . SER   I  33  ? 1.6698 0.7678 1.3699 0.0169  -0.1989 -0.2576 32  SER   I O   
14978 C  CB  . SER   I  33  ? 1.6665 0.7661 1.4780 -0.0071 -0.2997 -0.2191 32  SER   I CB  
14979 O  OG  . SER   I  33  ? 1.6440 0.5912 1.5371 -0.1288 -0.3572 -0.2407 32  SER   I OG  
14980 N  N   . LEU   I  34  ? 1.6610 0.7752 1.4263 0.0667  -0.1977 -0.2047 33  LEU   I N   
14981 C  CA  . LEU   I  34  ? 1.6721 0.7340 1.4062 0.1073  -0.1795 -0.2294 33  LEU   I CA  
14982 C  C   . LEU   I  34  ? 1.7125 0.6797 1.3200 0.1150  -0.1398 -0.2546 33  LEU   I C   
14983 O  O   . LEU   I  34  ? 1.7142 0.6327 1.3304 0.1066  -0.1290 -0.2380 33  LEU   I O   
14984 C  CB  . LEU   I  34  ? 1.6856 0.6962 1.4431 0.1193  -0.1759 -0.2121 33  LEU   I CB  
14985 C  CG  . LEU   I  34  ? 1.6787 0.6513 1.4434 0.1467  -0.1719 -0.2277 33  LEU   I CG  
14986 C  CD1 . LEU   I  34  ? 1.6883 0.6944 1.4364 0.1581  -0.1766 -0.2383 33  LEU   I CD1 
14987 C  CD2 . LEU   I  34  ? 1.6993 0.6187 1.4680 0.1454  -0.2042 -0.2023 33  LEU   I CD2 
14988 N  N   . GLY   I  35  ? 1.7798 0.7227 1.2900 0.1569  -0.1018 -0.2757 34  GLY   I N   
14989 C  CA  . GLY   I  35  ? 1.7634 0.6915 1.2828 0.1889  -0.0592 -0.2879 34  GLY   I CA  
14990 C  C   . GLY   I  35  ? 1.7860 0.7221 1.2904 0.2323  -0.0629 -0.2925 34  GLY   I C   
14991 O  O   . GLY   I  35  ? 1.8431 0.6036 1.2846 0.3079  -0.0543 -0.3491 34  GLY   I O   
14992 N  N   . VAL   I  36  ? 1.7369 0.6643 1.3355 0.2390  -0.0550 -0.2084 35  VAL   I N   
14993 C  CA  . VAL   I  36  ? 1.7274 0.7087 1.3622 0.2426  -0.0743 -0.1799 35  VAL   I CA  
14994 C  C   . VAL   I  36  ? 1.7692 0.6841 1.3524 0.2639  -0.0400 -0.1559 35  VAL   I C   
14995 O  O   . VAL   I  36  ? 1.7532 0.5556 1.3648 0.3053  -0.0105 -0.1513 35  VAL   I O   
14996 C  CB  . VAL   I  36  ? 1.6567 0.6312 1.3697 0.2730  -0.1297 -0.1448 35  VAL   I CB  
14997 C  CG1 . VAL   I  36  ? 1.6635 0.6129 1.4002 0.2733  -0.1298 -0.1506 35  VAL   I CG1 
14998 C  CG2 . VAL   I  36  ? 1.6380 0.6441 1.4084 0.2613  -0.1590 -0.1507 35  VAL   I CG2 
14999 N  N   . SER   I  37  ? 1.7856 0.6650 1.3334 0.2502  -0.0202 -0.1659 36  SER   I N   
15000 C  CA  . SER   I  37  ? 1.8177 0.6655 1.3125 0.2531  0.0065  -0.1372 36  SER   I CA  
15001 C  C   . SER   I  37  ? 1.8140 0.6687 1.3732 0.2425  -0.0056 -0.1580 36  SER   I C   
15002 O  O   . SER   I  37  ? 1.7139 0.5978 1.3474 0.2293  0.0233  -0.2000 36  SER   I O   
15003 C  CB  . SER   I  37  ? 1.7721 0.6552 1.2656 0.2784  -0.0073 -0.1024 36  SER   I CB  
15004 O  OG  . SER   I  37  ? 1.7473 0.7114 1.2608 0.2891  0.0036  -0.0580 36  SER   I OG  
15005 N  N   . ASN   I  38  ? 1.9456 0.7628 1.3779 0.2044  0.0427  -0.1278 37  ASN   I N   
15006 C  CA  . ASN   I  38  ? 1.9543 0.8938 1.4611 0.1627  0.0217  -0.1094 37  ASN   I CA  
15007 C  C   . ASN   I  38  ? 1.9370 0.9149 1.4849 0.1486  0.0367  -0.0332 37  ASN   I C   
15008 O  O   . ASN   I  38  ? 1.9011 1.0323 1.5855 0.0473  0.0036  0.0656  37  ASN   I O   
15009 C  CB  . ASN   I  38  ? 2.1870 1.1101 1.4504 0.1841  0.0872  -0.1974 37  ASN   I CB  
15010 C  CG  . ASN   I  38  ? 2.3256 1.2563 1.3496 0.2876  0.1336  -0.1346 37  ASN   I CG  
15011 O  OD1 . ASN   I  38  ? 2.4933 1.5221 1.4153 0.1504  0.1892  -0.3658 37  ASN   I OD1 
15012 N  ND2 . ASN   I  38  ? 2.3171 1.1980 1.3005 0.3153  0.1933  -0.1853 37  ASN   I ND2 
15013 N  N   . LYS   I  39  ? 1.8741 0.8419 1.4089 0.0804  0.0374  -0.0043 38  LYS   I N   
15014 C  CA  . LYS   I  39  ? 1.8627 0.8686 1.4228 0.0490  0.0612  0.0075  38  LYS   I CA  
15015 C  C   . LYS   I  39  ? 1.8015 0.7784 1.3802 0.0580  0.0619  0.0792  38  LYS   I C   
15016 O  O   . LYS   I  39  ? 1.8471 0.7262 1.3959 0.1455  0.0982  0.0971  38  LYS   I O   
15017 C  CB  . LYS   I  39  ? 1.9126 0.9013 1.4096 0.0395  0.0668  0.0141  38  LYS   I CB  
15018 C  CG  . LYS   I  39  ? 1.9829 0.9793 1.4751 0.0419  0.1438  -0.0235 38  LYS   I CG  
15019 C  CD  . LYS   I  39  ? 1.9911 1.0149 1.4845 0.0632  0.1523  -0.0073 38  LYS   I CD  
15020 C  CE  . LYS   I  39  ? 2.0391 1.0819 1.5469 0.0694  0.2266  0.0043  38  LYS   I CE  
15021 N  NZ  . LYS   I  39  ? 2.0641 1.1020 1.6174 0.0606  0.2766  -0.0375 38  LYS   I NZ  
15022 N  N   . PHE   I  40  ? 1.7692 0.7280 1.3656 0.0350  0.0420  0.0494  39  PHE   I N   
15023 C  CA  . PHE   I  40  ? 1.7567 0.6134 1.3717 0.0455  0.0134  0.0368  39  PHE   I CA  
15024 C  C   . PHE   I  40  ? 1.7531 0.6625 1.3638 0.0587  0.0235  0.0049  39  PHE   I C   
15025 O  O   . PHE   I  40  ? 1.7442 0.6734 1.3513 -0.0179 -0.0257 0.0171  39  PHE   I O   
15026 C  CB  . PHE   I  40  ? 1.7293 0.6132 1.3344 0.0460  -0.0004 -0.0041 39  PHE   I CB  
15027 C  CG  . PHE   I  40  ? 1.7476 0.5126 1.2794 0.0386  -0.0474 0.0041  39  PHE   I CG  
15028 C  CD1 . PHE   I  40  ? 1.7577 0.5017 1.2461 0.0193  -0.0587 0.0301  39  PHE   I CD1 
15029 C  CD2 . PHE   I  40  ? 1.7379 0.5315 1.2635 0.0519  -0.0724 -0.0348 39  PHE   I CD2 
15030 C  CE1 . PHE   I  40  ? 1.7707 0.4686 1.2232 -0.0041 -0.0819 0.0032  39  PHE   I CE1 
15031 C  CE2 . PHE   I  40  ? 1.7425 0.4929 1.2113 0.0468  -0.0996 -0.0147 39  PHE   I CE2 
15032 C  CZ  . PHE   I  40  ? 1.7364 0.4589 1.2219 0.0267  -0.0974 -0.0182 39  PHE   I CZ  
15033 N  N   . GLU   I  41  ? 1.7462 0.6672 1.3799 0.0654  0.0397  0.0269  40  GLU   I N   
15034 C  CA  . GLU   I  41  ? 1.7270 0.7151 1.3739 0.0946  0.0541  0.0265  40  GLU   I CA  
15035 C  C   . GLU   I  41  ? 1.7144 0.6905 1.3895 0.1261  0.0352  -0.0319 40  GLU   I C   
15036 O  O   . GLU   I  41  ? 1.7857 0.5676 1.3382 0.1345  0.0711  -0.1289 40  GLU   I O   
15037 C  CB  . GLU   I  41  ? 1.8029 0.6663 1.4301 0.1212  0.0698  0.0751  40  GLU   I CB  
15038 C  CG  . GLU   I  41  ? 1.8910 0.6949 1.4260 0.1323  0.0992  0.1146  40  GLU   I CG  
15039 C  CD  . GLU   I  41  ? 1.9796 0.6428 1.4459 0.1311  0.1353  0.1588  40  GLU   I CD  
15040 O  OE1 . GLU   I  41  ? 2.0734 0.6249 1.3831 0.1300  0.1035  0.2488  40  GLU   I OE1 
15041 O  OE2 . GLU   I  41  ? 2.0618 0.5670 1.5017 0.1521  0.2010  0.1089  40  GLU   I OE2 
15042 N  N   . LYS   I  42  ? 1.7064 0.7337 1.3578 0.0772  0.0075  -0.0665 41  LYS   I N   
15043 C  CA  . LYS   I  42  ? 1.6687 0.6588 1.3225 0.0224  -0.0632 -0.1222 41  LYS   I CA  
15044 C  C   . LYS   I  42  ? 1.6765 0.5286 1.3752 0.0025  -0.0482 -0.0851 41  LYS   I C   
15045 O  O   . LYS   I  42  ? 1.6876 0.3519 1.3751 -0.0856 -0.0680 -0.1146 41  LYS   I O   
15046 C  CB  . LYS   I  42  ? 1.6740 0.6754 1.3583 0.0406  -0.0796 -0.0976 41  LYS   I CB  
15047 C  CG  . LYS   I  42  ? 1.6780 0.6934 1.3988 0.0651  -0.1031 -0.1390 41  LYS   I CG  
15048 C  CD  . LYS   I  42  ? 1.7014 0.6908 1.4187 0.1048  -0.1358 -0.1604 41  LYS   I CD  
15049 C  CE  . LYS   I  42  ? 1.7160 0.6538 1.4661 0.0839  -0.1366 -0.1611 41  LYS   I CE  
15050 N  NZ  . LYS   I  42  ? 1.7529 0.6962 1.4886 0.0717  -0.1026 -0.1395 41  LYS   I NZ  
15051 N  N   . ILE   I  43  ? 1.6271 0.5440 1.3155 0.0109  -0.0836 -0.0972 42  ILE   I N   
15052 C  CA  . ILE   I  43  ? 1.5992 0.5905 1.3059 0.0231  -0.1316 -0.0763 42  ILE   I CA  
15053 C  C   . ILE   I  43  ? 1.6082 0.6195 1.2468 -0.0266 -0.1659 -0.0242 42  ILE   I C   
15054 O  O   . ILE   I  43  ? 1.6120 0.3780 1.2202 -0.0915 -0.1761 -0.0803 42  ILE   I O   
15055 C  CB  . ILE   I  43  ? 1.6024 0.6463 1.3254 0.0442  -0.1437 -0.1119 42  ILE   I CB  
15056 C  CG1 . ILE   I  43  ? 1.6122 0.6619 1.3201 0.0687  -0.1688 -0.1138 42  ILE   I CG1 
15057 C  CG2 . ILE   I  43  ? 1.5774 0.6344 1.3695 0.0449  -0.1401 -0.0999 42  ILE   I CG2 
15058 C  CD1 . ILE   I  43  ? 1.6157 0.7155 1.3286 0.0640  -0.1487 -0.1294 42  ILE   I CD1 
15059 N  N   . PHE   I  44  ? 1.6035 0.5773 1.2828 -0.0004 -0.1763 -0.0082 43  PHE   I N   
15060 C  CA  . PHE   I  44  ? 1.6204 0.6162 1.3177 0.0436  -0.2001 0.0619  43  PHE   I CA  
15061 C  C   . PHE   I  44  ? 1.6205 0.6561 1.3323 0.0432  -0.2130 0.0463  43  PHE   I C   
15062 O  O   . PHE   I  44  ? 1.6125 0.6158 1.2871 0.0117  -0.2147 0.0078  43  PHE   I O   
15063 C  CB  . PHE   I  44  ? 1.6223 0.5773 1.3442 0.0381  -0.1888 0.0769  43  PHE   I CB  
15064 C  CG  . PHE   I  44  ? 1.6596 0.4903 1.3915 0.0319  -0.1651 0.0929  43  PHE   I CG  
15065 C  CD1 . PHE   I  44  ? 1.6909 0.4382 1.3725 0.0069  -0.1530 0.0877  43  PHE   I CD1 
15066 C  CD2 . PHE   I  44  ? 1.6622 0.4514 1.3921 0.0225  -0.1680 0.0604  43  PHE   I CD2 
15067 C  CE1 . PHE   I  44  ? 1.7292 0.3812 1.3687 0.0396  -0.1495 0.0205  43  PHE   I CE1 
15068 C  CE2 . PHE   I  44  ? 1.6978 0.4705 1.4020 0.0271  -0.1791 0.0005  43  PHE   I CE2 
15069 C  CZ  . PHE   I  44  ? 1.7203 0.3939 1.3797 0.0254  -0.1560 0.0227  43  PHE   I CZ  
15070 N  N   . HIS   I  45  ? 1.6184 0.6873 1.3522 0.0778  -0.2195 0.1315  44  HIS   I N   
15071 C  CA  . HIS   I  45  ? 1.6253 0.7105 1.3313 0.0709  -0.2130 0.1460  44  HIS   I CA  
15072 C  C   . HIS   I  45  ? 1.6143 0.6987 1.3663 0.0616  -0.1965 0.1552  44  HIS   I C   
15073 O  O   . HIS   I  45  ? 1.5840 0.6099 1.4232 0.0729  -0.2267 0.1257  44  HIS   I O   
15074 C  CB  . HIS   I  45  ? 1.6856 0.8501 1.3012 0.0808  -0.1463 0.2115  44  HIS   I CB  
15075 C  CG  . HIS   I  45  ? 1.7668 0.9613 1.2978 0.0879  -0.1483 0.2340  44  HIS   I CG  
15076 N  ND1 . HIS   I  45  ? 1.8417 0.9899 1.2652 0.0326  -0.1309 0.2449  44  HIS   I ND1 
15077 C  CD2 . HIS   I  45  ? 1.8016 1.0296 1.2502 0.1005  -0.1812 0.2646  44  HIS   I CD2 
15078 C  CE1 . HIS   I  45  ? 1.8770 1.1225 1.2687 0.0171  -0.1243 0.2622  44  HIS   I CE1 
15079 N  NE2 . HIS   I  45  ? 1.8650 1.1082 1.2612 0.0293  -0.1545 0.2861  44  HIS   I NE2 
15080 N  N   . TYR   I  46  ? 1.5990 0.5754 1.3853 0.0791  -0.1420 0.1462  45  TYR   I N   
15081 C  CA  . TYR   I  46  ? 1.5596 0.5736 1.4061 0.0776  -0.0955 0.1583  45  TYR   I CA  
15082 C  C   . TYR   I  46  ? 1.5720 0.4658 1.4599 0.0598  -0.0417 0.1705  45  TYR   I C   
15083 O  O   . TYR   I  46  ? 1.5443 0.3538 1.4531 0.1216  -0.0152 0.1990  45  TYR   I O   
15084 C  CB  . TYR   I  46  ? 1.5292 0.5556 1.3690 0.0767  -0.1246 0.1481  45  TYR   I CB  
15085 C  CG  . TYR   I  46  ? 1.5130 0.5994 1.3469 0.0662  -0.1428 0.1302  45  TYR   I CG  
15086 C  CD1 . TYR   I  46  ? 1.5210 0.5732 1.3496 0.0727  -0.1439 0.1589  45  TYR   I CD1 
15087 C  CD2 . TYR   I  46  ? 1.5207 0.5941 1.3559 0.0627  -0.1589 0.1226  45  TYR   I CD2 
15088 C  CE1 . TYR   I  46  ? 1.5269 0.5896 1.3449 0.0771  -0.1704 0.1172  45  TYR   I CE1 
15089 C  CE2 . TYR   I  46  ? 1.5353 0.6073 1.3634 0.0583  -0.1955 0.0991  45  TYR   I CE2 
15090 C  CZ  . TYR   I  46  ? 1.5472 0.5776 1.3371 0.0365  -0.1954 0.1076  45  TYR   I CZ  
15091 O  OH  . TYR   I  46  ? 1.5647 0.5995 1.3183 0.0097  -0.2110 0.1451  45  TYR   I OH  
15092 N  N   . GLY   I  47  ? 1.5755 0.4718 1.5535 0.0031  0.0042  0.1596  46  GLY   I N   
15093 C  CA  . GLY   I  47  ? 1.5859 0.5394 1.6273 -0.0249 -0.0159 0.1502  46  GLY   I CA  
15094 C  C   . GLY   I  47  ? 1.5985 0.4839 1.6345 -0.0562 -0.0408 0.1759  46  GLY   I C   
15095 O  O   . GLY   I  47  ? 1.6287 0.4317 1.6378 -0.0328 -0.0800 0.2020  46  GLY   I O   
15096 N  N   . HIS   I  48  ? 1.6456 0.5375 1.5801 -0.1360 -0.0411 0.1507  47  HIS   I N   
15097 C  CA  . HIS   I  48  ? 1.6482 0.5927 1.5709 -0.1049 -0.0130 0.0926  47  HIS   I CA  
15098 C  C   . HIS   I  48  ? 1.6572 0.5997 1.5104 -0.1494 -0.0266 0.0530  47  HIS   I C   
15099 O  O   . HIS   I  48  ? 1.6727 0.5425 1.5402 -0.1765 -0.0478 0.0506  47  HIS   I O   
15100 C  CB  . HIS   I  48  ? 1.6320 0.6639 1.5614 -0.1170 0.0089  0.1165  47  HIS   I CB  
15101 C  CG  . HIS   I  48  ? 1.6716 0.7144 1.5535 -0.1151 0.0501  0.1217  47  HIS   I CG  
15102 N  ND1 . HIS   I  48  ? 1.6852 0.7114 1.5352 -0.1491 0.0747  0.0950  47  HIS   I ND1 
15103 C  CD2 . HIS   I  48  ? 1.6762 0.7573 1.5242 -0.0911 0.0666  0.1052  47  HIS   I CD2 
15104 C  CE1 . HIS   I  48  ? 1.6814 0.7242 1.5367 -0.1471 0.0773  0.0974  47  HIS   I CE1 
15105 N  NE2 . HIS   I  48  ? 1.6703 0.7257 1.5408 -0.1418 0.0615  0.0940  47  HIS   I NE2 
15106 N  N   . VAL   I  49  ? 1.6697 0.6983 1.4733 -0.1104 -0.0314 -0.0205 48  VAL   I N   
15107 C  CA  . VAL   I  49  ? 1.6983 0.7347 1.4087 -0.0794 -0.0677 0.0191  48  VAL   I CA  
15108 C  C   . VAL   I  49  ? 1.6675 0.7685 1.4438 -0.0619 -0.0959 0.0116  48  VAL   I C   
15109 O  O   . VAL   I  49  ? 1.6705 0.8881 1.5307 -0.0651 -0.1578 -0.0055 48  VAL   I O   
15110 C  CB  . VAL   I  49  ? 1.7406 0.7510 1.3704 -0.0722 -0.1129 -0.0279 48  VAL   I CB  
15111 C  CG1 . VAL   I  49  ? 1.7506 0.7263 1.3434 -0.0512 -0.1249 -0.0321 48  VAL   I CG1 
15112 C  CG2 . VAL   I  49  ? 1.7348 0.7754 1.4325 -0.1117 -0.1416 -0.0075 48  VAL   I CG2 
15113 N  N   . PHE   I  50  ? 1.5900 0.7778 1.4176 -0.0398 -0.1011 0.0525  49  PHE   I N   
15114 C  CA  . PHE   I  50  ? 1.5360 0.7124 1.3826 -0.0003 -0.0754 0.0673  49  PHE   I CA  
15115 C  C   . PHE   I  50  ? 1.4864 0.6548 1.3714 0.0152  -0.0951 0.0436  49  PHE   I C   
15116 O  O   . PHE   I  50  ? 1.4811 0.6420 1.3554 0.0014  -0.0790 0.0270  49  PHE   I O   
15117 C  CB  . PHE   I  50  ? 1.5274 0.7625 1.3775 -0.0071 -0.0615 0.0511  49  PHE   I CB  
15118 C  CG  . PHE   I  50  ? 1.5475 0.8357 1.3969 -0.0009 -0.0458 0.0741  49  PHE   I CG  
15119 C  CD1 . PHE   I  50  ? 1.5544 0.8474 1.4130 -0.0032 -0.0645 0.0641  49  PHE   I CD1 
15120 C  CD2 . PHE   I  50  ? 1.5647 0.8723 1.3951 -0.0058 -0.0705 0.1029  49  PHE   I CD2 
15121 C  CE1 . PHE   I  50  ? 1.5903 0.8256 1.4419 -0.0016 -0.0759 0.1163  49  PHE   I CE1 
15122 C  CE2 . PHE   I  50  ? 1.6137 0.9072 1.4159 0.0048  -0.0694 0.1545  49  PHE   I CE2 
15123 C  CZ  . PHE   I  50  ? 1.6188 0.8945 1.4145 0.0060  -0.0685 0.1505  49  PHE   I CZ  
15124 N  N   . LEU   I  51  ? 1.4743 0.6154 1.3048 0.0298  -0.0827 0.0682  50  LEU   I N   
15125 C  CA  . LEU   I  51  ? 1.5014 0.6193 1.2830 0.0075  -0.1006 0.0910  50  LEU   I CA  
15126 C  C   . LEU   I  51  ? 1.4774 0.6465 1.2815 -0.0180 -0.0986 0.0940  50  LEU   I C   
15127 O  O   . LEU   I  51  ? 1.4912 0.6019 1.2797 -0.0432 -0.0668 0.1294  50  LEU   I O   
15128 C  CB  . LEU   I  51  ? 1.5310 0.6087 1.2534 -0.0006 -0.0849 0.0684  50  LEU   I CB  
15129 C  CG  . LEU   I  51  ? 1.5609 0.5937 1.2514 -0.0186 -0.0933 0.0718  50  LEU   I CG  
15130 C  CD1 . LEU   I  51  ? 1.5889 0.6024 1.2665 -0.0195 -0.1034 0.0837  50  LEU   I CD1 
15131 C  CD2 . LEU   I  51  ? 1.5569 0.6156 1.2328 -0.0052 -0.1250 0.0774  50  LEU   I CD2 
15132 N  N   . GLY   I  52  ? 1.4803 0.6808 1.2935 -0.0068 -0.1250 0.1393  51  GLY   I N   
15133 C  CA  . GLY   I  52  ? 1.4678 0.6890 1.2939 -0.0240 -0.1116 0.1418  51  GLY   I CA  
15134 C  C   . GLY   I  52  ? 1.4459 0.6854 1.2701 -0.0523 -0.1446 0.1263  51  GLY   I C   
15135 O  O   . GLY   I  52  ? 1.5294 0.7451 1.2647 -0.0822 -0.0505 0.1216  51  GLY   I O   
15136 N  N   . ILE   I  53  ? 1.4252 0.6734 1.2970 -0.0567 -0.1291 0.0861  52  ILE   I N   
15137 C  CA  . ILE   I  53  ? 1.3912 0.7124 1.3272 -0.0468 -0.1378 0.0541  52  ILE   I CA  
15138 C  C   . ILE   I  53  ? 1.3917 0.6946 1.3108 0.0112  -0.1220 0.0350  52  ILE   I C   
15139 O  O   . ILE   I  53  ? 1.3394 0.9010 1.2992 0.0302  -0.0898 -0.0336 52  ILE   I O   
15140 C  CB  . ILE   I  53  ? 1.3967 0.6863 1.3841 -0.0616 -0.1437 0.0446  52  ILE   I CB  
15141 C  CG1 . ILE   I  53  ? 1.4182 0.6958 1.4318 -0.1062 -0.1321 0.0878  52  ILE   I CG1 
15142 C  CG2 . ILE   I  53  ? 1.3960 0.6942 1.3450 -0.0622 -0.1530 0.0177  52  ILE   I CG2 
15143 C  CD1 . ILE   I  53  ? 1.4371 0.7302 1.4715 -0.0883 -0.1450 0.1254  52  ILE   I CD1 
15144 N  N   . THR   I  54  ? 1.3878 0.5848 1.3089 0.0501  -0.1476 -0.0230 53  THR   I N   
15145 C  CA  . THR   I  54  ? 1.3983 0.4962 1.3103 0.1011  -0.1351 0.0003  53  THR   I CA  
15146 C  C   . THR   I  54  ? 1.3893 0.3695 1.3115 0.1039  -0.1418 -0.0120 53  THR   I C   
15147 O  O   . THR   I  54  ? 1.3578 0.3863 1.2431 0.1070  -0.1500 0.0200  53  THR   I O   
15148 C  CB  . THR   I  54  ? 1.3916 0.4570 1.3006 0.0827  -0.1415 -0.0290 53  THR   I CB  
15149 O  OG1 . THR   I  54  ? 1.4359 0.4115 1.2966 0.0924  -0.1433 -0.0507 53  THR   I OG1 
15150 C  CG2 . THR   I  54  ? 1.4127 0.4713 1.3073 0.0788  -0.1087 -0.0169 53  THR   I CG2 
15151 N  N   . GLY   I  55  ? 1.3699 0.3611 1.3623 0.1116  -0.1256 -0.0244 54  GLY   I N   
15152 C  CA  . GLY   I  55  ? 1.3695 0.4320 1.3686 0.1468  -0.1008 -0.0296 54  GLY   I CA  
15153 C  C   . GLY   I  55  ? 1.4059 0.4669 1.3640 0.1448  -0.1210 -0.0466 54  GLY   I C   
15154 O  O   . GLY   I  55  ? 1.3433 0.5295 1.3911 0.1948  -0.1004 -0.0767 54  GLY   I O   
15155 N  N   . LEU   I  56  ? 1.4377 0.4431 1.2944 0.1060  -0.0778 -0.0815 55  LEU   I N   
15156 C  CA  . LEU   I  56  ? 1.4661 0.4704 1.2675 0.0901  -0.1010 -0.1033 55  LEU   I CA  
15157 C  C   . LEU   I  56  ? 1.5189 0.5730 1.1976 0.0515  -0.0836 -0.0819 55  LEU   I C   
15158 O  O   . LEU   I  56  ? 1.5244 0.7258 1.1687 0.0261  -0.0995 -0.1888 55  LEU   I O   
15159 C  CB  . LEU   I  56  ? 1.4449 0.3478 1.2733 0.0783  -0.1063 -0.0775 55  LEU   I CB  
15160 C  CG  . LEU   I  56  ? 1.4377 0.3511 1.3301 0.0607  -0.1086 -0.0847 55  LEU   I CG  
15161 C  CD1 . LEU   I  56  ? 1.4579 0.3996 1.3578 0.0457  -0.1191 -0.1287 55  LEU   I CD1 
15162 C  CD2 . LEU   I  56  ? 1.4324 0.3619 1.3323 0.0357  -0.0966 -0.0751 55  LEU   I CD2 
15163 N  N   . ALA   I  57  ? 1.5974 0.6812 1.1998 0.0039  -0.0855 -0.1001 56  ALA   I N   
15164 C  CA  . ALA   I  57  ? 1.5806 0.6616 1.1611 0.0223  -0.1287 -0.0864 56  ALA   I CA  
15165 C  C   . ALA   I  57  ? 1.4921 0.6580 1.0832 0.0070  -0.1614 -0.0699 56  ALA   I C   
15166 O  O   . ALA   I  57  ? 1.4905 0.6864 1.0847 -0.0191 -0.1672 -0.0983 56  ALA   I O   
15167 C  CB  . ALA   I  57  ? 1.6205 0.6919 1.1345 0.0237  -0.1220 -0.0618 56  ALA   I CB  
15168 N  N   . THR   I  58  ? 1.4651 0.5650 1.0900 -0.0042 -0.1976 -0.0545 57  THR   I N   
15169 C  CA  . THR   I  58  ? 1.4362 0.5546 1.1497 -0.0226 -0.1988 -0.0661 57  THR   I CA  
15170 C  C   . THR   I  58  ? 1.4277 0.5598 1.1426 -0.0314 -0.2228 -0.0455 57  THR   I C   
15171 O  O   . THR   I  58  ? 1.3912 0.5516 1.1121 -0.0776 -0.2865 -0.0744 57  THR   I O   
15172 C  CB  . THR   I  58  ? 1.4360 0.4711 1.2063 -0.0168 -0.1722 -0.0516 57  THR   I CB  
15173 O  OG1 . THR   I  58  ? 1.4210 0.5128 1.2680 0.0331  -0.1346 0.0374  57  THR   I OG1 
15174 C  CG2 . THR   I  58  ? 1.4090 0.4322 1.2212 -0.0181 -0.1718 -0.0555 57  THR   I CG2 
15175 N  N   . ASP   I  59  ? 1.4288 0.5697 1.0949 -0.0381 -0.2268 -0.0799 58  ASP   I N   
15176 C  CA  . ASP   I  59  ? 1.4129 0.5394 1.1220 -0.0570 -0.2125 -0.1037 58  ASP   I CA  
15177 C  C   . ASP   I  59  ? 1.4056 0.6169 1.0739 -0.0271 -0.1851 -0.0560 58  ASP   I C   
15178 O  O   . ASP   I  59  ? 1.4651 0.6703 1.1002 -0.0700 -0.1936 -0.0732 58  ASP   I O   
15179 C  CB  . ASP   I  59  ? 1.3693 0.4979 1.1114 -0.0559 -0.2149 -0.1315 58  ASP   I CB  
15180 C  CG  . ASP   I  59  ? 1.3366 0.5119 1.1757 -0.0136 -0.2340 -0.1665 58  ASP   I CG  
15181 O  OD1 . ASP   I  59  ? 1.2773 0.5538 1.1889 -0.0190 -0.2263 -0.1707 58  ASP   I OD1 
15182 O  OD2 . ASP   I  59  ? 1.3873 0.4788 1.1739 0.0203  -0.2339 -0.1782 58  ASP   I OD2 
15183 N  N   . VAL   I  60  ? 1.3805 0.5700 1.0468 -0.0444 -0.2107 -0.0550 59  VAL   I N   
15184 C  CA  . VAL   I  60  ? 1.3905 0.6210 1.0776 -0.0354 -0.1950 -0.0294 59  VAL   I CA  
15185 C  C   . VAL   I  60  ? 1.4086 0.6023 1.1178 -0.0632 -0.1827 -0.0330 59  VAL   I C   
15186 O  O   . VAL   I  60  ? 1.4653 0.6003 1.1449 -0.1380 -0.1437 0.0275  59  VAL   I O   
15187 C  CB  . VAL   I  60  ? 1.4024 0.6605 1.0744 -0.0217 -0.1866 -0.0355 59  VAL   I CB  
15188 C  CG1 . VAL   I  60  ? 1.4340 0.6970 1.0667 -0.0148 -0.1540 -0.0083 59  VAL   I CG1 
15189 C  CG2 . VAL   I  60  ? 1.3986 0.6694 1.0756 -0.0179 -0.1861 -0.0328 59  VAL   I CG2 
15190 N  N   . THR   I  61  ? 1.4030 0.5803 1.1460 -0.0246 -0.1884 -0.0105 60  THR   I N   
15191 C  CA  . THR   I  61  ? 1.3892 0.5587 1.1610 -0.0031 -0.1680 -0.0227 60  THR   I CA  
15192 C  C   . THR   I  61  ? 1.3814 0.5193 1.2083 0.0100  -0.1316 -0.0086 60  THR   I C   
15193 O  O   . THR   I  61  ? 1.3935 0.4340 1.3139 0.0782  -0.1123 -0.0714 60  THR   I O   
15194 C  CB  . THR   I  61  ? 1.4212 0.6066 1.1436 0.0095  -0.1844 0.0051  60  THR   I CB  
15195 O  OG1 . THR   I  61  ? 1.4118 0.6213 1.0871 0.0562  -0.2006 0.0220  60  THR   I OG1 
15196 C  CG2 . THR   I  61  ? 1.4378 0.6563 1.1246 -0.0138 -0.1965 0.0367  60  THR   I CG2 
15197 N  N   . THR   I  62  ? 1.4038 0.4125 1.1839 0.0156  -0.1161 -0.0286 61  THR   I N   
15198 C  CA  . THR   I  62  ? 1.4135 0.4026 1.1954 0.0053  -0.0894 -0.0235 61  THR   I CA  
15199 C  C   . THR   I  62  ? 1.4296 0.5102 1.1385 0.0669  -0.1149 -0.0339 61  THR   I C   
15200 O  O   . THR   I  62  ? 1.4601 0.5233 1.1358 0.0530  -0.1089 -0.0641 61  THR   I O   
15201 C  CB  . THR   I  62  ? 1.4036 0.3731 1.2049 -0.0002 -0.0838 -0.0450 61  THR   I CB  
15202 O  OG1 . THR   I  62  ? 1.3468 0.5199 1.2410 0.0167  -0.0836 -0.0046 61  THR   I OG1 
15203 C  CG2 . THR   I  62  ? 1.4041 0.3265 1.2061 -0.0558 -0.0800 -0.0529 61  THR   I CG2 
15204 N  N   . LEU   I  63  ? 1.4920 0.4259 1.1391 0.0710  -0.1118 -0.0546 62  LEU   I N   
15205 C  CA  . LEU   I  63  ? 1.5249 0.4506 1.1356 0.0619  -0.1106 -0.0812 62  LEU   I CA  
15206 C  C   . LEU   I  63  ? 1.5085 0.4816 1.1130 0.1004  -0.0979 -0.0413 62  LEU   I C   
15207 O  O   . LEU   I  63  ? 1.4966 0.5054 1.1187 0.0730  -0.0991 -0.0292 62  LEU   I O   
15208 C  CB  . LEU   I  63  ? 1.5876 0.4301 1.1447 0.0482  -0.1075 -0.0792 62  LEU   I CB  
15209 C  CG  . LEU   I  63  ? 1.6217 0.4009 1.1454 0.0533  -0.1046 -0.0760 62  LEU   I CG  
15210 C  CD1 . LEU   I  63  ? 1.6440 0.3992 1.1817 0.0590  -0.1263 -0.0722 62  LEU   I CD1 
15211 C  CD2 . LEU   I  63  ? 1.6257 0.4599 1.1534 0.0679  -0.0682 -0.0925 62  LEU   I CD2 
15212 N  N   . ASN   I  64  ? 1.4937 0.4853 1.1045 0.0989  -0.1170 -0.0446 63  ASN   I N   
15213 C  CA  . ASN   I  64  ? 1.5129 0.5306 1.1756 0.0555  -0.1219 -0.0235 63  ASN   I CA  
15214 C  C   . ASN   I  64  ? 1.5320 0.5065 1.2143 0.0162  -0.1044 0.0000  63  ASN   I C   
15215 O  O   . ASN   I  64  ? 1.5594 0.4684 1.2236 0.0062  -0.0819 0.0355  63  ASN   I O   
15216 C  CB  . ASN   I  64  ? 1.5332 0.5852 1.1576 0.0984  -0.1400 -0.0169 63  ASN   I CB  
15217 C  CG  . ASN   I  64  ? 1.5659 0.6265 1.1371 0.1497  -0.1373 0.0384  63  ASN   I CG  
15218 O  OD1 . ASN   I  64  ? 1.5547 0.7318 1.1343 0.1950  -0.1876 -0.0257 63  ASN   I OD1 
15219 N  ND2 . ASN   I  64  ? 1.6003 0.6827 1.1768 0.2082  -0.2039 0.0594  63  ASN   I ND2 
15220 N  N   . GLU   I  65  ? 1.5217 0.5122 1.2630 -0.0822 -0.1278 -0.0171 64  GLU   I N   
15221 C  CA  . GLU   I  65  ? 1.6018 0.5067 1.3403 -0.0664 -0.1072 -0.0264 64  GLU   I CA  
15222 C  C   . GLU   I  65  ? 1.6154 0.6505 1.3257 -0.0941 -0.0921 -0.0612 64  GLU   I C   
15223 O  O   . GLU   I  65  ? 1.6957 0.6543 1.4234 -0.1860 -0.1407 -0.3312 64  GLU   I O   
15224 C  CB  . GLU   I  65  ? 1.6494 0.4887 1.4112 -0.1350 -0.1462 0.0157  64  GLU   I CB  
15225 C  CG  . GLU   I  65  ? 1.7342 0.4802 1.3893 -0.1393 -0.1489 0.0624  64  GLU   I CG  
15226 C  CD  . GLU   I  65  ? 1.7664 0.4826 1.4796 -0.1728 -0.2003 0.1526  64  GLU   I CD  
15227 O  OE1 . GLU   I  65  ? 1.8711 0.4724 1.4415 -0.2094 -0.1734 0.2149  64  GLU   I OE1 
15228 O  OE2 . GLU   I  65  ? 1.7470 0.3366 1.4870 -0.2135 -0.2010 0.2053  64  GLU   I OE2 
15229 N  N   . MET   I  66  ? 1.6141 0.6054 1.3029 0.0013  -0.0603 -0.0725 65  MET   I N   
15230 C  CA  . MET   I  66  ? 1.6087 0.5895 1.3288 0.0321  -0.0082 -0.0805 65  MET   I CA  
15231 C  C   . MET   I  66  ? 1.5917 0.6049 1.2862 0.0106  0.0062  -0.0532 65  MET   I C   
15232 O  O   . MET   I  66  ? 1.6028 0.6655 1.2741 -0.0547 0.0163  -0.1033 65  MET   I O   
15233 C  CB  . MET   I  66  ? 1.6735 0.5356 1.3317 0.1385  0.0547  -0.0725 65  MET   I CB  
15234 C  CG  . MET   I  66  ? 1.7188 0.6271 1.3917 0.1959  0.0886  -0.1033 65  MET   I CG  
15235 S  SD  . MET   I  66  ? 1.7381 0.5623 1.4336 0.2856  0.1394  -0.1165 65  MET   I SD  
15236 C  CE  . MET   I  66  ? 1.7141 0.6331 1.4081 0.2398  0.1296  -0.1194 65  MET   I CE  
15237 N  N   . PHE   I  67  ? 1.5487 0.5409 1.2285 -0.0338 -0.0367 -0.0479 66  PHE   I N   
15238 C  CA  . PHE   I  67  ? 1.5646 0.6161 1.2178 -0.0456 -0.0494 -0.0391 66  PHE   I CA  
15239 C  C   . PHE   I  67  ? 1.5742 0.6651 1.2535 -0.0203 -0.0359 0.0144  66  PHE   I C   
15240 O  O   . PHE   I  67  ? 1.5534 0.7267 1.3078 -0.0362 -0.0781 0.0352  66  PHE   I O   
15241 C  CB  . PHE   I  67  ? 1.5749 0.5790 1.1935 -0.0647 -0.0503 -0.0582 66  PHE   I CB  
15242 C  CG  . PHE   I  67  ? 1.5914 0.6174 1.1520 -0.0469 -0.0507 -0.0646 66  PHE   I CG  
15243 C  CD1 . PHE   I  67  ? 1.6164 0.6220 1.1522 -0.0424 -0.0438 -0.0582 66  PHE   I CD1 
15244 C  CD2 . PHE   I  67  ? 1.5903 0.6138 1.1159 -0.0140 -0.0579 -0.0675 66  PHE   I CD2 
15245 C  CE1 . PHE   I  67  ? 1.6230 0.6207 1.1331 -0.0078 -0.0754 -0.0390 66  PHE   I CE1 
15246 C  CE2 . PHE   I  67  ? 1.5942 0.6347 1.0803 0.0092  -0.0831 -0.0518 66  PHE   I CE2 
15247 C  CZ  . PHE   I  67  ? 1.6032 0.6189 1.0784 0.0033  -0.0824 -0.0474 66  PHE   I CZ  
15248 N  N   . ARG   I  68  ? 1.5310 0.6161 1.2503 -0.0344 -0.0193 0.0554  67  ARG   I N   
15249 C  CA  . ARG   I  68  ? 1.4997 0.5348 1.3319 -0.0478 -0.0167 0.0385  67  ARG   I CA  
15250 C  C   . ARG   I  68  ? 1.4759 0.4504 1.3178 -0.1006 -0.0085 0.0908  67  ARG   I C   
15251 O  O   . ARG   I  68  ? 1.4863 0.4586 1.3440 -0.1057 0.0037  0.0664  67  ARG   I O   
15252 C  CB  . ARG   I  68  ? 1.5095 0.4955 1.3231 -0.0648 -0.0228 0.0720  67  ARG   I CB  
15253 C  CG  . ARG   I  68  ? 1.5435 0.4438 1.3734 -0.0549 -0.0412 0.0845  67  ARG   I CG  
15254 C  CD  . ARG   I  68  ? 1.5797 0.4591 1.3866 -0.0628 -0.0663 0.0858  67  ARG   I CD  
15255 N  NE  . ARG   I  68  ? 1.5859 0.4447 1.4552 -0.0662 -0.0766 0.1070  67  ARG   I NE  
15256 C  CZ  . ARG   I  68  ? 1.5856 0.5419 1.4983 -0.0704 -0.1036 0.0952  67  ARG   I CZ  
15257 N  NH1 . ARG   I  68  ? 1.6350 0.6268 1.5424 -0.0679 -0.0603 0.0785  67  ARG   I NH1 
15258 N  NH2 . ARG   I  68  ? 1.5768 0.5221 1.5609 -0.0635 -0.0942 0.1109  67  ARG   I NH2 
15259 N  N   . TYR   I  69  ? 1.4716 0.4194 1.3038 -0.0996 -0.0223 0.0833  68  TYR   I N   
15260 C  CA  . TYR   I  69  ? 1.4897 0.4040 1.2884 -0.0909 -0.0621 0.0716  68  TYR   I CA  
15261 C  C   . TYR   I  69  ? 1.5086 0.4633 1.2803 -0.0855 -0.0598 0.0510  68  TYR   I C   
15262 O  O   . TYR   I  69  ? 1.5412 0.4600 1.2782 -0.0204 -0.0727 -0.0023 68  TYR   I O   
15263 C  CB  . TYR   I  69  ? 1.4639 0.4046 1.2815 -0.0539 -0.0733 0.0788  68  TYR   I CB  
15264 C  CG  . TYR   I  69  ? 1.4761 0.3625 1.2359 -0.0722 -0.0729 0.0769  68  TYR   I CG  
15265 C  CD1 . TYR   I  69  ? 1.4582 0.3364 1.2123 -0.0814 -0.0695 0.0983  68  TYR   I CD1 
15266 C  CD2 . TYR   I  69  ? 1.4745 0.3644 1.2868 -0.0491 -0.0751 0.0724  68  TYR   I CD2 
15267 C  CE1 . TYR   I  69  ? 1.4628 0.3580 1.2183 -0.0748 -0.0646 0.1009  68  TYR   I CE1 
15268 C  CE2 . TYR   I  69  ? 1.4773 0.3786 1.2936 -0.0507 -0.0620 0.0635  68  TYR   I CE2 
15269 C  CZ  . TYR   I  69  ? 1.4612 0.3813 1.2758 -0.0585 -0.0754 0.0886  68  TYR   I CZ  
15270 O  OH  . TYR   I  69  ? 1.4789 0.3831 1.3541 -0.0696 -0.0420 0.0671  68  TYR   I OH  
15271 N  N   . LYS   I  70  ? 1.5170 0.4825 1.1779 -0.0859 -0.0847 -0.0057 69  LYS   I N   
15272 C  CA  . LYS   I  70  ? 1.5109 0.5109 1.1839 -0.0642 -0.0859 -0.0413 69  LYS   I CA  
15273 C  C   . LYS   I  70  ? 1.4875 0.5649 1.1754 -0.0356 -0.1232 -0.0306 69  LYS   I C   
15274 O  O   . LYS   I  70  ? 1.5130 0.5863 1.1982 0.0041  -0.1517 -0.0533 69  LYS   I O   
15275 C  CB  . LYS   I  70  ? 1.5131 0.5347 1.0894 -0.0405 -0.0873 -0.0595 69  LYS   I CB  
15276 C  CG  . LYS   I  70  ? 1.5304 0.5623 1.0998 -0.0246 -0.0589 -0.0594 69  LYS   I CG  
15277 C  CD  . LYS   I  70  ? 1.5480 0.5500 1.1324 0.0034  -0.0519 -0.0450 69  LYS   I CD  
15278 C  CE  . LYS   I  70  ? 1.5669 0.5408 1.1608 0.0048  -0.0175 0.0020  69  LYS   I CE  
15279 N  NZ  . LYS   I  70  ? 1.5869 0.5194 1.1937 0.0207  -0.0001 0.0183  69  LYS   I NZ  
15280 N  N   . THR   I  71  ? 1.5030 0.5254 1.1573 -0.0201 -0.1544 -0.0507 70  THR   I N   
15281 C  CA  . THR   I  71  ? 1.5022 0.5652 1.1853 -0.0026 -0.1532 -0.0423 70  THR   I CA  
15282 C  C   . THR   I  71  ? 1.5554 0.6164 1.2163 -0.0039 -0.1391 0.0072  70  THR   I C   
15283 O  O   . THR   I  71  ? 1.6035 0.6581 1.2143 -0.0572 -0.0954 -0.0231 70  THR   I O   
15284 C  CB  . THR   I  71  ? 1.5371 0.5208 1.1879 -0.0089 -0.1597 -0.0453 70  THR   I CB  
15285 O  OG1 . THR   I  71  ? 1.5035 0.5339 1.1793 0.0165  -0.1621 -0.0300 70  THR   I OG1 
15286 C  CG2 . THR   I  71  ? 1.5369 0.4866 1.1683 -0.0277 -0.1550 -0.0673 70  THR   I CG2 
15287 N  N   . ASN   I  72  ? 1.5517 0.5505 1.2337 -0.0013 -0.1368 0.0391  71  ASN   I N   
15288 C  CA  . ASN   I  72  ? 1.5549 0.4801 1.2636 0.0224  -0.1240 -0.0015 71  ASN   I CA  
15289 C  C   . ASN   I  72  ? 1.5485 0.4368 1.2737 -0.0007 -0.1640 -0.0049 71  ASN   I C   
15290 O  O   . ASN   I  72  ? 1.5348 0.3869 1.2677 0.0192  -0.1994 -0.1574 71  ASN   I O   
15291 C  CB  . ASN   I  72  ? 1.5595 0.4395 1.2262 0.0145  -0.1051 0.0652  71  ASN   I CB  
15292 C  CG  . ASN   I  72  ? 1.5620 0.3827 1.2408 0.0317  -0.0838 0.0896  71  ASN   I CG  
15293 O  OD1 . ASN   I  72  ? 1.5490 0.4213 1.2004 0.0426  -0.0602 0.0913  71  ASN   I OD1 
15294 N  ND2 . ASN   I  72  ? 1.5836 0.4133 1.2445 0.0005  -0.0958 0.0813  71  ASN   I ND2 
15295 N  N   . LEU   I  73  ? 1.5441 0.3926 1.2646 -0.0294 -0.1726 0.0088  72  LEU   I N   
15296 C  CA  . LEU   I  73  ? 1.5593 0.4552 1.2818 -0.0442 -0.1449 -0.0176 72  LEU   I CA  
15297 C  C   . LEU   I  73  ? 1.5528 0.5093 1.3075 -0.0602 -0.1565 0.0189  72  LEU   I C   
15298 O  O   . LEU   I  73  ? 1.5370 0.5315 1.2881 -0.0343 -0.1983 -0.0070 72  LEU   I O   
15299 C  CB  . LEU   I  73  ? 1.5874 0.4820 1.2566 -0.0786 -0.1363 -0.0399 72  LEU   I CB  
15300 C  CG  . LEU   I  73  ? 1.6046 0.5599 1.2492 -0.0994 -0.1491 -0.0991 72  LEU   I CG  
15301 C  CD1 . LEU   I  73  ? 1.6305 0.5518 1.1972 -0.0829 -0.1246 -0.1451 72  LEU   I CD1 
15302 C  CD2 . LEU   I  73  ? 1.6207 0.5591 1.3221 -0.1137 -0.1407 -0.0890 72  LEU   I CD2 
15303 N  N   . TYR   I  74  ? 1.5544 0.4887 1.3469 -0.0661 -0.1202 0.0194  73  TYR   I N   
15304 C  CA  . TYR   I  74  ? 1.5583 0.5070 1.3746 -0.0865 -0.1286 -0.0136 73  TYR   I CA  
15305 C  C   . TYR   I  74  ? 1.6154 0.4887 1.4422 -0.1122 -0.1113 -0.0198 73  TYR   I C   
15306 O  O   . TYR   I  74  ? 1.7456 0.4674 1.5428 -0.1531 -0.1276 -0.0450 73  TYR   I O   
15307 C  CB  . TYR   I  74  ? 1.5411 0.4785 1.3555 -0.1122 -0.1127 -0.0391 73  TYR   I CB  
15308 C  CG  . TYR   I  74  ? 1.5353 0.4294 1.3614 -0.1198 -0.1127 -0.0491 73  TYR   I CG  
15309 C  CD1 . TYR   I  74  ? 1.5339 0.4353 1.3944 -0.1216 -0.1172 -0.0377 73  TYR   I CD1 
15310 C  CD2 . TYR   I  74  ? 1.5181 0.4065 1.3485 -0.1240 -0.1215 -0.0708 73  TYR   I CD2 
15311 C  CE1 . TYR   I  74  ? 1.5530 0.3985 1.3816 -0.1240 -0.1260 -0.0511 73  TYR   I CE1 
15312 C  CE2 . TYR   I  74  ? 1.5514 0.3869 1.3358 -0.1245 -0.1359 -0.0804 73  TYR   I CE2 
15313 C  CZ  . TYR   I  74  ? 1.5558 0.3708 1.3627 -0.1393 -0.1368 -0.0878 73  TYR   I CZ  
15314 O  OH  . TYR   I  74  ? 1.5947 0.3635 1.3227 -0.1950 -0.1577 -0.1439 73  TYR   I OH  
15315 N  N   . LYS   I  75  ? 1.6126 0.5776 1.4674 -0.0840 -0.0672 0.0057  74  LYS   I N   
15316 C  CA  . LYS   I  75  ? 1.5849 0.6402 1.5008 -0.0908 -0.0497 -0.0201 74  LYS   I CA  
15317 C  C   . LYS   I  75  ? 1.5653 0.6358 1.5057 -0.1134 -0.0758 -0.0119 74  LYS   I C   
15318 O  O   . LYS   I  75  ? 1.5740 0.6696 1.4665 -0.1208 -0.1045 -0.0367 74  LYS   I O   
15319 C  CB  . LYS   I  75  ? 1.5924 0.6615 1.5290 -0.0739 -0.0235 -0.0449 74  LYS   I CB  
15320 C  CG  . LYS   I  75  ? 1.5960 0.7011 1.5473 -0.0801 -0.0035 -0.0794 74  LYS   I CG  
15321 C  CD  . LYS   I  75  ? 1.6368 0.7595 1.5525 -0.0776 -0.0034 -0.1027 74  LYS   I CD  
15322 C  CE  . LYS   I  75  ? 1.6436 0.8520 1.6330 -0.0935 0.0092  -0.1070 74  LYS   I CE  
15323 N  NZ  . LYS   I  75  ? 1.6562 0.9929 1.6274 -0.0661 0.0551  -0.1106 74  LYS   I NZ  
15324 N  N   . LEU   I  76  ? 1.5770 0.5952 1.5228 -0.1060 -0.0831 0.0221  75  LEU   I N   
15325 C  CA  . LEU   I  76  ? 1.5809 0.5865 1.5730 -0.1214 -0.0934 0.0399  75  LEU   I CA  
15326 C  C   . LEU   I  76  ? 1.6125 0.6549 1.5763 -0.1064 -0.0791 0.0209  75  LEU   I C   
15327 O  O   . LEU   I  76  ? 1.6386 0.7058 1.6384 -0.1751 -0.1090 -0.0133 75  LEU   I O   
15328 C  CB  . LEU   I  76  ? 1.6046 0.5191 1.4794 -0.1368 -0.1184 0.0737  75  LEU   I CB  
15329 C  CG  . LEU   I  76  ? 1.6012 0.5061 1.4582 -0.1278 -0.1480 0.1544  75  LEU   I CG  
15330 C  CD1 . LEU   I  76  ? 1.6000 0.5143 1.3965 -0.1283 -0.1420 0.1854  75  LEU   I CD1 
15331 C  CD2 . LEU   I  76  ? 1.5907 0.5064 1.5033 -0.1567 -0.1595 0.1599  75  LEU   I CD2 
15332 N  N   . LYS   I  77  ? 1.5869 0.5669 1.5859 -0.0566 -0.0635 0.0130  76  LYS   I N   
15333 C  CA  . LYS   I  77  ? 1.6043 0.5502 1.6034 -0.0554 -0.0407 -0.0081 76  LYS   I CA  
15334 C  C   . LYS   I  77  ? 1.6245 0.5289 1.6154 -0.0268 -0.0596 -0.0074 76  LYS   I C   
15335 O  O   . LYS   I  77  ? 1.6309 0.6002 1.6169 -0.0124 -0.0815 -0.0481 76  LYS   I O   
15336 C  CB  . LYS   I  77  ? 1.6682 0.5757 1.5494 -0.0336 -0.0064 0.0149  76  LYS   I CB  
15337 C  CG  . LYS   I  77  ? 1.6626 0.6787 1.5569 -0.0608 0.0254  0.0425  76  LYS   I CG  
15338 C  CD  . LYS   I  77  ? 1.7203 0.7576 1.5200 -0.0730 0.0542  0.1056  76  LYS   I CD  
15339 C  CE  . LYS   I  77  ? 1.7422 0.8761 1.5103 -0.0931 0.0740  0.1226  76  LYS   I CE  
15340 N  NZ  . LYS   I  77  ? 1.6957 0.9986 1.5325 -0.1399 0.0715  0.1012  76  LYS   I NZ  
15341 N  N   . GLU   I  78  ? 1.6242 0.5106 1.6105 -0.0482 -0.0836 -0.0393 77  GLU   I N   
15342 C  CA  . GLU   I  78  ? 1.6413 0.6329 1.6370 -0.0832 -0.1282 -0.0570 77  GLU   I CA  
15343 C  C   . GLU   I  78  ? 1.6328 0.5624 1.7158 -0.1198 -0.1521 -0.0636 77  GLU   I C   
15344 O  O   . GLU   I  78  ? 1.6525 0.4657 1.7737 -0.1207 -0.1625 -0.1516 77  GLU   I O   
15345 C  CB  . GLU   I  78  ? 1.6413 0.6679 1.6112 -0.0166 -0.1283 -0.0127 77  GLU   I CB  
15346 C  CG  . GLU   I  78  ? 1.6638 0.6878 1.5899 0.0253  -0.0842 -0.0377 77  GLU   I CG  
15347 C  CD  . GLU   I  78  ? 1.6794 0.7066 1.5655 0.0683  -0.0459 -0.0656 77  GLU   I CD  
15348 O  OE1 . GLU   I  78  ? 1.6539 0.7968 1.6423 0.1015  -0.0722 -0.0742 77  GLU   I OE1 
15349 O  OE2 . GLU   I  78  ? 1.7005 0.6025 1.5120 0.1343  0.0063  -0.1187 77  GLU   I OE2 
15350 N  N   . GLU   I  79  ? 1.6551 0.5950 1.7425 -0.1413 -0.1595 0.0008  78  GLU   I N   
15351 C  CA  . GLU   I  79  ? 1.6490 0.7175 1.7916 -0.1416 -0.1509 0.0586  78  GLU   I CA  
15352 C  C   . GLU   I  79  ? 1.5802 0.7313 1.7329 -0.1791 -0.1268 0.0458  78  GLU   I C   
15353 O  O   . GLU   I  79  ? 1.5937 0.6416 1.7323 -0.1702 -0.1103 0.1079  78  GLU   I O   
15354 C  CB  . GLU   I  79  ? 1.6990 0.7408 1.8866 -0.1496 -0.1843 0.0264  78  GLU   I CB  
15355 C  CG  . GLU   I  79  ? 1.7605 0.8016 1.9436 -0.1114 -0.1966 0.0735  78  GLU   I CG  
15356 C  CD  . GLU   I  79  ? 1.8304 0.8123 2.0630 -0.1507 -0.2206 0.0840  78  GLU   I CD  
15357 O  OE1 . GLU   I  79  ? 1.8702 0.9201 2.0297 -0.0990 -0.2421 0.1851  78  GLU   I OE1 
15358 O  OE2 . GLU   I  79  ? 1.9257 0.9746 2.1343 -0.1303 -0.2261 0.1953  78  GLU   I OE2 
15359 N  N   . ARG   I  80  ? 1.6069 0.7301 1.6644 -0.1765 -0.1075 -0.0084 79  ARG   I N   
15360 C  CA  . ARG   I  80  ? 1.5966 0.7856 1.6620 -0.1665 -0.0760 -0.0007 79  ARG   I CA  
15361 C  C   . ARG   I  80  ? 1.6347 0.7366 1.6544 -0.1469 -0.0463 0.0357  79  ARG   I C   
15362 O  O   . ARG   I  80  ? 1.6441 0.7773 1.6895 -0.2104 -0.0717 0.0957  79  ARG   I O   
15363 C  CB  . ARG   I  80  ? 1.6142 0.8285 1.6645 -0.2131 -0.0916 -0.0521 79  ARG   I CB  
15364 C  CG  . ARG   I  80  ? 1.6493 0.8290 1.6189 -0.2230 -0.1033 -0.0799 79  ARG   I CG  
15365 C  CD  . ARG   I  80  ? 1.6697 0.8752 1.6253 -0.2198 -0.1193 -0.0556 79  ARG   I CD  
15366 N  NE  . ARG   I  80  ? 1.6873 0.8903 1.5945 -0.2227 -0.1531 -0.0379 79  ARG   I NE  
15367 C  CZ  . ARG   I  80  ? 1.6609 0.8863 1.5515 -0.2147 -0.1581 -0.0544 79  ARG   I CZ  
15368 N  NH1 . ARG   I  80  ? 1.6317 0.9328 1.5318 -0.1785 -0.1595 -0.0491 79  ARG   I NH1 
15369 N  NH2 . ARG   I  80  ? 1.6814 0.9937 1.5397 -0.2488 -0.1597 -0.0747 79  ARG   I NH2 
15370 N  N   . ALA   I  81  ? 1.6492 0.7307 1.6882 -0.1145 -0.0068 0.0790  80  ALA   I N   
15371 C  CA  . ALA   I  81  ? 1.6080 0.7155 1.6422 -0.0821 0.0213  0.0649  80  ALA   I CA  
15372 C  C   . ALA   I  81  ? 1.5724 0.6403 1.6057 -0.0913 0.0509  0.0133  80  ALA   I C   
15373 O  O   . ALA   I  81  ? 1.5817 0.5519 1.5458 -0.0919 0.0862  0.0193  80  ALA   I O   
15374 C  CB  . ALA   I  81  ? 1.6092 0.7501 1.6727 -0.1005 0.0577  0.0759  80  ALA   I CB  
15375 N  N   . ILE   I  82  ? 1.5145 0.6824 1.5056 -0.0779 0.0254  0.0115  81  ILE   I N   
15376 C  CA  . ILE   I  82  ? 1.5122 0.7109 1.4877 -0.0453 -0.0063 0.0201  81  ILE   I CA  
15377 C  C   . ILE   I  82  ? 1.5016 0.7243 1.5576 -0.0410 -0.0011 0.0131  81  ILE   I C   
15378 O  O   . ILE   I  82  ? 1.4877 0.6395 1.5748 0.0126  -0.0212 0.0166  81  ILE   I O   
15379 C  CB  . ILE   I  82  ? 1.5192 0.6897 1.4446 -0.0387 -0.0416 0.0485  81  ILE   I CB  
15380 C  CG1 . ILE   I  82  ? 1.5501 0.6018 1.4526 -0.0336 -0.0802 0.0681  81  ILE   I CG1 
15381 C  CG2 . ILE   I  82  ? 1.5347 0.6736 1.4294 -0.0269 -0.0279 0.0634  81  ILE   I CG2 
15382 C  CD1 . ILE   I  82  ? 1.5303 0.5583 1.4088 -0.0062 -0.1151 0.0926  81  ILE   I CD1 
15383 N  N   . GLU   I  83  ? 1.5104 0.7535 1.5376 -0.0529 0.0154  0.0022  82  GLU   I N   
15384 C  CA  . GLU   I  83  ? 1.4936 0.7682 1.5381 -0.0549 0.0235  -0.0178 82  GLU   I CA  
15385 C  C   . GLU   I  83  ? 1.4675 0.7776 1.5262 -0.0567 0.0469  -0.0246 82  GLU   I C   
15386 O  O   . GLU   I  83  ? 1.4517 0.7699 1.5199 0.0018  0.0468  -0.0459 82  GLU   I O   
15387 C  CB  . GLU   I  83  ? 1.5062 0.8112 1.5232 -0.0930 0.0362  -0.0258 82  GLU   I CB  
15388 C  CG  . GLU   I  83  ? 1.5129 0.8241 1.5412 -0.1006 0.0586  -0.0026 82  GLU   I CG  
15389 C  CD  . GLU   I  83  ? 1.4980 0.7660 1.5957 -0.1460 0.0834  0.0692  82  GLU   I CD  
15390 O  OE1 . GLU   I  83  ? 1.4671 0.8139 1.6133 -0.0891 0.1253  0.0805  82  GLU   I OE1 
15391 O  OE2 . GLU   I  83  ? 1.4944 0.7800 1.6422 -0.2029 0.1022  0.0425  82  GLU   I OE2 
15392 N  N   . PRO   I  84  ? 1.5095 0.7108 1.5298 -0.0792 0.0012  -0.0034 83  PRO   I N   
15393 C  CA  . PRO   I  84  ? 1.5117 0.6760 1.4922 -0.0490 -0.0273 -0.0190 83  PRO   I CA  
15394 C  C   . PRO   I  84  ? 1.4994 0.6792 1.4604 -0.0550 -0.0490 -0.0734 83  PRO   I C   
15395 O  O   . PRO   I  84  ? 1.4885 0.7065 1.4885 -0.0514 -0.0217 -0.0568 83  PRO   I O   
15396 C  CB  . PRO   I  84  ? 1.5046 0.6422 1.4892 -0.0547 -0.0350 0.0200  83  PRO   I CB  
15397 C  CG  . PRO   I  84  ? 1.4656 0.6625 1.5556 -0.0694 -0.0357 0.0307  83  PRO   I CG  
15398 C  CD  . PRO   I  84  ? 1.4846 0.6891 1.5740 -0.0703 -0.0237 -0.0023 83  PRO   I CD  
15399 N  N   . GLU   I  85  ? 1.5015 0.6991 1.5194 -0.0358 -0.0714 -0.1426 84  GLU   I N   
15400 C  CA  . GLU   I  85  ? 1.5225 0.7039 1.4856 -0.0364 -0.0927 -0.1864 84  GLU   I CA  
15401 C  C   . GLU   I  85  ? 1.5193 0.6727 1.4782 -0.0498 -0.1250 -0.2107 84  GLU   I C   
15402 O  O   . GLU   I  85  ? 1.5976 0.4781 1.4487 -0.1161 -0.1398 -0.3269 84  GLU   I O   
15403 C  CB  . GLU   I  85  ? 1.5211 0.7752 1.4817 0.0060  -0.1117 -0.1905 84  GLU   I CB  
15404 C  CG  . GLU   I  85  ? 1.5607 0.8266 1.5191 0.0478  -0.1340 -0.1700 84  GLU   I CG  
15405 C  CD  . GLU   I  85  ? 1.5663 0.8803 1.6037 0.0473  -0.1024 -0.1628 84  GLU   I CD  
15406 O  OE1 . GLU   I  85  ? 1.6009 0.8876 1.6640 0.0762  -0.1093 -0.1320 84  GLU   I OE1 
15407 O  OE2 . GLU   I  85  ? 1.5880 0.9635 1.6094 0.0633  -0.1438 -0.1534 84  GLU   I OE2 
15408 N  N   . THR   I  86  ? 1.5037 0.7208 1.5319 -0.0564 -0.1796 -0.1368 85  THR   I N   
15409 C  CA  . THR   I  86  ? 1.5136 0.7091 1.5519 -0.0467 -0.1906 -0.0956 85  THR   I CA  
15410 C  C   . THR   I  86  ? 1.5098 0.6437 1.4570 -0.0240 -0.1806 -0.0357 85  THR   I C   
15411 O  O   . THR   I  86  ? 1.5418 0.6517 1.3928 0.0002  -0.1531 0.0428  85  THR   I O   
15412 C  CB  . THR   I  86  ? 1.4503 0.6766 1.6417 -0.1154 -0.2318 -0.1876 85  THR   I CB  
15413 O  OG1 . THR   I  86  ? 1.4528 0.7465 1.7397 -0.1348 -0.2460 -0.2420 85  THR   I OG1 
15414 C  CG2 . THR   I  86  ? 1.4727 0.6563 1.6481 -0.1137 -0.2169 -0.2216 85  THR   I CG2 
15415 N  N   . PHE   I  87  ? 1.5794 0.5274 1.4534 0.0036  -0.1739 -0.0088 86  PHE   I N   
15416 C  CA  . PHE   I  87  ? 1.5880 0.4635 1.4568 -0.0203 -0.1540 -0.0062 86  PHE   I CA  
15417 C  C   . PHE   I  87  ? 1.5706 0.4900 1.4089 -0.0318 -0.1370 -0.0105 86  PHE   I C   
15418 O  O   . PHE   I  87  ? 1.5552 0.4721 1.4500 0.0173  -0.1272 -0.0038 86  PHE   I O   
15419 C  CB  . PHE   I  87  ? 1.6070 0.4340 1.4505 -0.0044 -0.1461 0.0384  86  PHE   I CB  
15420 C  CG  . PHE   I  87  ? 1.6308 0.3996 1.4160 -0.0034 -0.1698 0.0962  86  PHE   I CG  
15421 C  CD1 . PHE   I  87  ? 1.6909 0.4091 1.4135 0.0107  -0.1796 0.1351  86  PHE   I CD1 
15422 C  CD2 . PHE   I  87  ? 1.6506 0.3975 1.4265 -0.0018 -0.1639 0.0976  86  PHE   I CD2 
15423 C  CE1 . PHE   I  87  ? 1.7010 0.3435 1.4373 0.0062  -0.1810 0.1465  86  PHE   I CE1 
15424 C  CE2 . PHE   I  87  ? 1.6679 0.4037 1.4189 0.0189  -0.1758 0.1093  86  PHE   I CE2 
15425 C  CZ  . PHE   I  87  ? 1.7260 0.3294 1.4417 0.0074  -0.1561 0.1669  86  PHE   I CZ  
15426 N  N   . THR   I  88  ? 1.5250 0.5545 1.3370 -0.0309 -0.1625 -0.0592 87  THR   I N   
15427 C  CA  . THR   I  88  ? 1.5461 0.5328 1.2766 -0.0580 -0.1457 -0.1177 87  THR   I CA  
15428 C  C   . THR   I  88  ? 1.5509 0.5368 1.2669 -0.0491 -0.1503 -0.1391 87  THR   I C   
15429 O  O   . THR   I  88  ? 1.5419 0.4992 1.2513 -0.0254 -0.1102 -0.0927 87  THR   I O   
15430 C  CB  . THR   I  88  ? 1.5614 0.5275 1.2245 -0.0937 -0.1827 -0.1286 87  THR   I CB  
15431 O  OG1 . THR   I  88  ? 1.5651 0.5117 1.2532 -0.1220 -0.1689 -0.1513 87  THR   I OG1 
15432 C  CG2 . THR   I  88  ? 1.5771 0.5508 1.1737 -0.0998 -0.1847 -0.1303 87  THR   I CG2 
15433 N  N   . GLN   I  89  ? 1.5629 0.5537 1.2618 -0.0091 -0.1274 -0.1620 88  GLN   I N   
15434 C  CA  . GLN   I  89  ? 1.6036 0.4988 1.2217 -0.0102 -0.1252 -0.1483 88  GLN   I CA  
15435 C  C   . GLN   I  89  ? 1.5779 0.4297 1.2141 -0.0178 -0.0920 -0.1336 88  GLN   I C   
15436 O  O   . GLN   I  89  ? 1.5942 0.2782 1.1669 -0.0111 -0.0981 -0.1105 88  GLN   I O   
15437 C  CB  . GLN   I  89  ? 1.6363 0.5261 1.2406 -0.0120 -0.1469 -0.1648 88  GLN   I CB  
15438 C  CG  . GLN   I  89  ? 1.6658 0.5401 1.2639 0.0068  -0.1626 -0.1561 88  GLN   I CG  
15439 C  CD  . GLN   I  89  ? 1.7128 0.4989 1.2549 0.0597  -0.1908 -0.1329 88  GLN   I CD  
15440 O  OE1 . GLN   I  89  ? 1.7321 0.5251 1.2038 0.1272  -0.2020 -0.2577 88  GLN   I OE1 
15441 N  NE2 . GLN   I  89  ? 1.7273 0.5910 1.2710 0.0381  -0.1694 -0.1118 88  GLN   I NE2 
15442 N  N   . LEU   I  90  ? 1.6448 0.4754 1.2228 -0.0253 -0.0890 -0.1159 89  LEU   I N   
15443 C  CA  . LEU   I  90  ? 1.6259 0.5096 1.2174 -0.0735 -0.0929 -0.1183 89  LEU   I CA  
15444 C  C   . LEU   I  90  ? 1.5519 0.4614 1.1989 -0.0696 -0.0221 -0.0838 89  LEU   I C   
15445 O  O   . LEU   I  90  ? 1.5461 0.4198 1.1615 -0.1398 0.0016  -0.0773 89  LEU   I O   
15446 C  CB  . LEU   I  90  ? 1.6962 0.4783 1.2319 -0.0572 -0.0955 -0.1108 89  LEU   I CB  
15447 C  CG  . LEU   I  90  ? 1.7282 0.4109 1.2240 -0.0271 -0.0899 -0.1113 89  LEU   I CG  
15448 C  CD1 . LEU   I  90  ? 1.7593 0.3961 1.2237 -0.0236 -0.0991 -0.1360 89  LEU   I CD1 
15449 C  CD2 . LEU   I  90  ? 1.7419 0.4334 1.2336 -0.0455 -0.0605 -0.1291 89  LEU   I CD2 
15450 N  N   . VAL   I  91  ? 1.5107 0.4755 1.1988 -0.0559 -0.0118 -0.0537 90  VAL   I N   
15451 C  CA  . VAL   I  91  ? 1.4779 0.5230 1.1893 -0.0621 -0.0232 -0.0732 90  VAL   I CA  
15452 C  C   . VAL   I  91  ? 1.4578 0.5311 1.1913 -0.0676 -0.0351 -0.0671 90  VAL   I C   
15453 O  O   . VAL   I  91  ? 1.4867 0.4217 1.1609 -0.1081 -0.0175 -0.0567 90  VAL   I O   
15454 C  CB  . VAL   I  91  ? 1.4888 0.5403 1.2054 -0.0298 -0.0272 -0.0633 90  VAL   I CB  
15455 C  CG1 . VAL   I  91  ? 1.4758 0.5221 1.1838 -0.0098 -0.0391 -0.0460 90  VAL   I CG1 
15456 C  CG2 . VAL   I  91  ? 1.4886 0.5640 1.2219 -0.0306 -0.0042 -0.0634 90  VAL   I CG2 
15457 N  N   . SER   I  92  ? 1.4499 0.5240 1.2109 -0.0423 -0.0498 -0.0707 91  SER   I N   
15458 C  CA  . SER   I  92  ? 1.4499 0.4874 1.2185 -0.0475 -0.0806 -0.0515 91  SER   I CA  
15459 C  C   . SER   I  92  ? 1.4565 0.5320 1.2113 -0.0210 -0.0992 -0.0274 91  SER   I C   
15460 O  O   . SER   I  92  ? 1.4718 0.4760 1.1922 -0.0144 -0.1341 -0.0234 91  SER   I O   
15461 C  CB  . SER   I  92  ? 1.4121 0.5366 1.2926 -0.0326 -0.0972 -0.0843 91  SER   I CB  
15462 O  OG  . SER   I  92  ? 1.3728 0.4899 1.4036 -0.0887 -0.0456 -0.0970 91  SER   I OG  
15463 N  N   . SER   I  93  ? 1.5012 0.5281 1.2382 -0.0128 -0.1167 -0.0188 92  SER   I N   
15464 C  CA  . SER   I  93  ? 1.5251 0.5394 1.2500 0.0054  -0.1059 -0.0156 92  SER   I CA  
15465 C  C   . SER   I  93  ? 1.4812 0.3621 1.2732 0.0108  -0.0921 0.0310  92  SER   I C   
15466 O  O   . SER   I  93  ? 1.5072 0.3032 1.3007 0.0464  -0.0743 0.1072  92  SER   I O   
15467 C  CB  . SER   I  93  ? 1.5528 0.5785 1.2759 -0.0594 -0.1212 -0.0673 92  SER   I CB  
15468 O  OG  . SER   I  93  ? 1.5773 0.7358 1.3013 -0.0837 -0.1445 -0.0701 92  SER   I OG  
15469 N  N   . SER   I  94  ? 1.5076 0.4589 1.2707 -0.0074 -0.0761 -0.0085 93  SER   I N   
15470 C  CA  . SER   I  94  ? 1.5351 0.5918 1.2597 -0.0449 -0.0716 -0.0362 93  SER   I CA  
15471 C  C   . SER   I  94  ? 1.5577 0.5693 1.2295 -0.0292 -0.0617 0.0145  93  SER   I C   
15472 O  O   . SER   I  94  ? 1.5378 0.6684 1.2579 -0.1164 0.0074  0.0175  93  SER   I O   
15473 C  CB  . SER   I  94  ? 1.5331 0.6415 1.3124 -0.0590 -0.0254 -0.0259 93  SER   I CB  
15474 O  OG  . SER   I  94  ? 1.5390 0.6764 1.3389 -0.0937 -0.0123 -0.0071 93  SER   I OG  
15475 N  N   . LEU   I  95  ? 1.5642 0.5776 1.1563 -0.0217 -0.0870 0.0089  94  LEU   I N   
15476 C  CA  . LEU   I  95  ? 1.5331 0.5844 1.1538 -0.0190 -0.0791 -0.0058 94  LEU   I CA  
15477 C  C   . LEU   I  95  ? 1.5131 0.5071 1.1444 -0.0454 -0.1003 0.0009  94  LEU   I C   
15478 O  O   . LEU   I  95  ? 1.4674 0.5795 1.2006 -0.0402 -0.0935 0.1558  94  LEU   I O   
15479 C  CB  . LEU   I  95  ? 1.5553 0.6338 1.1226 0.0191  -0.0947 0.0027  94  LEU   I CB  
15480 C  CG  . LEU   I  95  ? 1.5326 0.6247 1.1493 0.0538  -0.0823 -0.0359 94  LEU   I CG  
15481 C  CD1 . LEU   I  95  ? 1.5167 0.5629 1.1093 0.0280  -0.0759 -0.0488 94  LEU   I CD1 
15482 C  CD2 . LEU   I  95  ? 1.5685 0.6289 1.1487 0.0785  -0.0866 -0.0768 94  LEU   I CD2 
15483 N  N   . TYR   I  96  ? 1.4983 0.3431 1.1838 -0.0744 -0.0787 -0.0597 95  TYR   I N   
15484 C  CA  . TYR   I  96  ? 1.5263 0.3673 1.1544 -0.0929 -0.0895 -0.0914 95  TYR   I CA  
15485 C  C   . TYR   I  96  ? 1.5285 0.3606 1.2373 -0.1076 -0.0770 -0.1008 95  TYR   I C   
15486 O  O   . TYR   I  96  ? 1.6144 0.2852 1.2859 -0.1719 -0.1011 -0.0530 95  TYR   I O   
15487 C  CB  . TYR   I  96  ? 1.5146 0.3956 1.1450 -0.0743 -0.0869 -0.1102 95  TYR   I CB  
15488 C  CG  . TYR   I  96  ? 1.5499 0.4534 1.1040 -0.0788 -0.1053 -0.1180 95  TYR   I CG  
15489 C  CD1 . TYR   I  96  ? 1.5626 0.4857 1.0751 -0.0076 -0.1061 -0.1149 95  TYR   I CD1 
15490 C  CD2 . TYR   I  96  ? 1.5904 0.4803 1.0911 -0.0663 -0.1019 -0.1132 95  TYR   I CD2 
15491 C  CE1 . TYR   I  96  ? 1.6254 0.5547 1.0412 0.0044  -0.1227 -0.1017 95  TYR   I CE1 
15492 C  CE2 . TYR   I  96  ? 1.6611 0.5623 1.0767 -0.0501 -0.1092 -0.0882 95  TYR   I CE2 
15493 C  CZ  . TYR   I  96  ? 1.6655 0.5831 1.0574 0.0220  -0.1212 -0.1143 95  TYR   I CZ  
15494 O  OH  . TYR   I  96  ? 1.7329 0.5523 1.0474 0.0494  -0.1490 -0.0841 95  TYR   I OH  
15495 N  N   . GLU   I  97  ? 1.5698 0.4494 1.2612 -0.0831 -0.1075 -0.0333 96  GLU   I N   
15496 C  CA  . GLU   I  97  ? 1.5783 0.5490 1.3554 -0.0412 -0.0871 -0.0362 96  GLU   I CA  
15497 C  C   . GLU   I  97  ? 1.5445 0.5527 1.3626 -0.0296 -0.0564 -0.0571 96  GLU   I C   
15498 O  O   . GLU   I  97  ? 1.5389 0.6178 1.4290 -0.0994 0.0344  -0.0687 96  GLU   I O   
15499 C  CB  . GLU   I  97  ? 1.6190 0.6004 1.4219 -0.0614 -0.0630 0.0073  96  GLU   I CB  
15500 C  CG  . GLU   I  97  ? 1.6744 0.5969 1.4909 -0.0342 -0.0246 0.0370  96  GLU   I CG  
15501 C  CD  . GLU   I  97  ? 1.7523 0.5850 1.5321 -0.0073 0.0224  0.0477  96  GLU   I CD  
15502 O  OE1 . GLU   I  97  ? 1.8419 0.6167 1.6027 0.0138  0.0631  0.0182  96  GLU   I OE1 
15503 O  OE2 . GLU   I  97  ? 1.7742 0.5928 1.5575 0.0087  0.0526  0.0746  96  GLU   I OE2 
15504 N  N   . ARG   I  98  ? 1.6007 0.5678 1.3703 0.0422  -0.0823 -0.0542 97  ARG   I N   
15505 C  CA  . ARG   I  98  ? 1.6277 0.5604 1.4002 0.0678  -0.1277 -0.0687 97  ARG   I CA  
15506 C  C   . ARG   I  98  ? 1.6307 0.6799 1.1831 0.0744  -0.1768 -0.0342 97  ARG   I C   
15507 O  O   . ARG   I  98  ? 1.6168 0.6742 1.2634 0.1458  -0.2619 -0.0456 97  ARG   I O   
15508 C  CB  . ARG   I  98  ? 1.6879 0.5669 1.4176 0.1287  -0.0983 -0.0566 97  ARG   I CB  
15509 C  CG  . ARG   I  98  ? 1.7795 0.6264 1.5002 0.1937  -0.1063 -0.0128 97  ARG   I CG  
15510 C  CD  . ARG   I  98  ? 1.8022 0.7789 1.5983 0.1981  -0.1313 -0.0192 97  ARG   I CD  
15511 N  NE  . ARG   I  98  ? 1.9551 0.8804 1.6678 0.3158  -0.1492 0.0204  97  ARG   I NE  
15512 C  CZ  . ARG   I  98  ? 2.0905 0.9949 1.6835 0.2664  -0.1217 -0.0970 97  ARG   I CZ  
15513 N  NH1 . ARG   I  98  ? 2.0509 0.9184 1.6581 0.2865  -0.1439 -0.1294 97  ARG   I NH1 
15514 N  NH2 . ARG   I  98  ? 2.1890 0.8734 1.7565 0.2216  -0.0956 -0.1521 97  ARG   I NH2 
15515 N  N   . ARG   I  99  ? 1.6513 0.6859 1.1740 0.0473  -0.1640 -0.0548 98  ARG   I N   
15516 C  CA  . ARG   I  99  ? 1.6124 0.6113 1.1909 0.0254  -0.1511 -0.0866 98  ARG   I CA  
15517 C  C   . ARG   I  99  ? 1.5839 0.5343 1.1592 0.0598  -0.1330 -0.0623 98  ARG   I C   
15518 O  O   . ARG   I  99  ? 1.5071 0.5253 1.2104 0.0305  -0.1107 -0.0351 98  ARG   I O   
15519 C  CB  . ARG   I  99  ? 1.6829 0.6820 1.1637 0.0236  -0.1922 -0.0268 98  ARG   I CB  
15520 C  CG  . ARG   I  99  ? 1.7345 0.6762 1.2036 0.0174  -0.2206 -0.0090 98  ARG   I CG  
15521 C  CD  . ARG   I  99  ? 1.7070 0.7111 1.1452 0.0143  -0.2541 0.0078  98  ARG   I CD  
15522 N  NE  . ARG   I  99  ? 1.7473 0.7320 1.1530 -0.0113 -0.3117 0.0278  98  ARG   I NE  
15523 C  CZ  . ARG   I  99  ? 1.7371 0.6731 1.1450 0.0253  -0.3453 0.1076  98  ARG   I CZ  
15524 N  NH1 . ARG   I  99  ? 1.7268 0.7490 1.1607 0.0330  -0.3624 0.1481  98  ARG   I NH1 
15525 N  NH2 . ARG   I  99  ? 1.7335 0.6134 1.1347 -0.0038 -0.3401 0.1433  98  ARG   I NH2 
15526 N  N   . PHE   I  100 ? 1.5531 0.4785 1.1701 0.0043  -0.1377 -0.0820 99  PHE   I N   
15527 C  CA  . PHE   I  100 ? 1.5602 0.4829 1.2692 -0.0055 -0.1209 -0.0405 99  PHE   I CA  
15528 C  C   . PHE   I  100 ? 1.5401 0.5145 1.2831 -0.0317 -0.1238 -0.0202 99  PHE   I C   
15529 O  O   . PHE   I  100 ? 1.5612 0.5990 1.3706 -0.0797 -0.1216 -0.0438 99  PHE   I O   
15530 C  CB  . PHE   I  100 ? 1.6020 0.5045 1.2773 -0.0138 -0.1056 -0.0611 99  PHE   I CB  
15531 C  CG  . PHE   I  100 ? 1.6608 0.6134 1.2846 -0.0305 -0.1252 -0.0740 99  PHE   I CG  
15532 C  CD1 . PHE   I  100 ? 1.7042 0.6287 1.2948 -0.0023 -0.1097 -0.0737 99  PHE   I CD1 
15533 C  CD2 . PHE   I  100 ? 1.7017 0.6127 1.2867 -0.0426 -0.1150 -0.0724 99  PHE   I CD2 
15534 C  CE1 . PHE   I  100 ? 1.7456 0.7063 1.2746 -0.0360 -0.1001 -0.0816 99  PHE   I CE1 
15535 C  CE2 . PHE   I  100 ? 1.7609 0.7005 1.2476 -0.0523 -0.0897 -0.0832 99  PHE   I CE2 
15536 C  CZ  . PHE   I  100 ? 1.7647 0.7185 1.2412 -0.0419 -0.0914 -0.0780 99  PHE   I CZ  
15537 N  N   . GLY   I  101 ? 1.5105 0.5767 1.3023 -0.0511 -0.1180 -0.0365 100 GLY   I N   
15538 C  CA  . GLY   I  101 ? 1.5093 0.6111 1.3357 -0.0449 -0.1706 -0.0811 100 GLY   I CA  
15539 C  C   . GLY   I  101 ? 1.4550 0.6149 1.3336 0.0060  -0.1999 -0.1113 100 GLY   I C   
15540 O  O   . GLY   I  101 ? 1.4705 0.7171 1.2444 -0.0567 -0.2890 -0.1037 100 GLY   I O   
15541 N  N   . PRO   I  102 ? 1.5273 0.5160 1.3035 0.0205  -0.1739 -0.0800 101 PRO   I N   
15542 C  CA  . PRO   I  102 ? 1.5309 0.5135 1.2145 0.0628  -0.1569 -0.0692 101 PRO   I CA  
15543 C  C   . PRO   I  102 ? 1.5630 0.4905 1.1974 0.0896  -0.1540 -0.0134 101 PRO   I C   
15544 O  O   . PRO   I  102 ? 1.5579 0.3806 1.1373 0.1263  -0.1356 0.0182  101 PRO   I O   
15545 C  CB  . PRO   I  102 ? 1.4804 0.4952 1.2524 0.0466  -0.1655 -0.0836 101 PRO   I CB  
15546 C  CG  . PRO   I  102 ? 1.5124 0.4609 1.2823 0.0533  -0.1677 -0.0720 101 PRO   I CG  
15547 C  CD  . PRO   I  102 ? 1.4979 0.4971 1.3204 0.0312  -0.1599 -0.0873 101 PRO   I CD  
15548 N  N   . TYR   I  103 ? 1.5715 0.5140 1.1849 0.0807  -0.1713 0.0024  102 TYR   I N   
15549 C  CA  . TYR   I  103 ? 1.5825 0.5515 1.1776 0.1370  -0.2135 -0.0336 102 TYR   I CA  
15550 C  C   . TYR   I  103 ? 1.5067 0.5244 1.0796 0.0912  -0.2575 -0.0129 102 TYR   I C   
15551 O  O   . TYR   I  103 ? 1.5345 0.4978 1.0362 0.0827  -0.2530 -0.0256 102 TYR   I O   
15552 C  CB  . TYR   I  103 ? 1.5993 0.6134 1.2312 0.1080  -0.2218 -0.0238 102 TYR   I CB  
15553 C  CG  . TYR   I  103 ? 1.7115 0.6282 1.2768 0.1478  -0.2790 -0.0196 102 TYR   I CG  
15554 C  CD1 . TYR   I  103 ? 1.7595 0.6520 1.3652 0.1948  -0.3331 -0.0076 102 TYR   I CD1 
15555 C  CD2 . TYR   I  103 ? 1.7212 0.5817 1.3106 0.1345  -0.2985 -0.0003 102 TYR   I CD2 
15556 C  CE1 . TYR   I  103 ? 1.7903 0.6614 1.4532 0.2190  -0.3432 -0.0673 102 TYR   I CE1 
15557 C  CE2 . TYR   I  103 ? 1.7436 0.6210 1.4035 0.1831  -0.2915 -0.0151 102 TYR   I CE2 
15558 C  CZ  . TYR   I  103 ? 1.7641 0.6773 1.4301 0.2168  -0.3215 -0.0643 102 TYR   I CZ  
15559 O  OH  . TYR   I  103 ? 1.7312 0.7957 1.5650 0.3363  -0.2021 0.0155  102 TYR   I OH  
15560 N  N   . PHE   I  104 ? 1.5148 0.4958 1.1051 0.0944  -0.2199 -0.0245 103 PHE   I N   
15561 C  CA  . PHE   I  104 ? 1.4900 0.4788 1.0896 0.0725  -0.2058 -0.0363 103 PHE   I CA  
15562 C  C   . PHE   I  104 ? 1.5049 0.4257 1.1005 0.0970  -0.1851 -0.0067 103 PHE   I C   
15563 O  O   . PHE   I  104 ? 1.5168 0.3946 1.0900 0.0940  -0.2185 0.0066  103 PHE   I O   
15564 C  CB  . PHE   I  104 ? 1.5248 0.4203 1.1157 0.0749  -0.1850 -0.0689 103 PHE   I CB  
15565 C  CG  . PHE   I  104 ? 1.5297 0.3901 1.1242 0.0571  -0.1808 -0.1030 103 PHE   I CG  
15566 C  CD1 . PHE   I  104 ? 1.5292 0.4307 1.0870 0.0676  -0.2085 -0.1208 103 PHE   I CD1 
15567 C  CD2 . PHE   I  104 ? 1.5200 0.4359 1.1646 0.0542  -0.1839 -0.0968 103 PHE   I CD2 
15568 C  CE1 . PHE   I  104 ? 1.5301 0.4710 1.1008 0.0739  -0.2031 -0.1131 103 PHE   I CE1 
15569 C  CE2 . PHE   I  104 ? 1.5202 0.4771 1.1867 0.0481  -0.1806 -0.0917 103 PHE   I CE2 
15570 C  CZ  . PHE   I  104 ? 1.5059 0.4857 1.1578 0.0664  -0.1945 -0.1086 103 PHE   I CZ  
15571 N  N   . VAL   I  105 ? 1.4608 0.4000 1.1214 0.0649  -0.1317 0.0053  104 VAL   I N   
15572 C  CA  . VAL   I  105 ? 1.4755 0.4627 1.1522 0.0801  -0.0830 -0.0101 104 VAL   I CA  
15573 C  C   . VAL   I  105 ? 1.4131 0.4059 1.1591 0.0767  -0.0385 -0.0153 104 VAL   I C   
15574 O  O   . VAL   I  105 ? 1.3644 0.3522 1.1436 0.0864  0.0150  -0.0970 104 VAL   I O   
15575 C  CB  . VAL   I  105 ? 1.5222 0.4660 1.1535 0.0828  -0.0855 -0.0029 104 VAL   I CB  
15576 C  CG1 . VAL   I  105 ? 1.5398 0.5004 1.1514 0.0868  -0.0991 -0.0229 104 VAL   I CG1 
15577 C  CG2 . VAL   I  105 ? 1.5412 0.4471 1.1367 0.0691  -0.0985 0.0097  104 VAL   I CG2 
15578 N  N   . GLY   I  106 ? 1.4183 0.4513 1.2214 0.0558  -0.0147 -0.0051 105 GLY   I N   
15579 C  CA  . GLY   I  106 ? 1.4266 0.5128 1.2256 0.0379  -0.0324 -0.0072 105 GLY   I CA  
15580 C  C   . GLY   I  106 ? 1.4231 0.5511 1.2111 0.0285  -0.0251 -0.0070 105 GLY   I C   
15581 O  O   . GLY   I  106 ? 1.3687 0.6064 1.2636 0.0387  -0.0263 0.0068  105 GLY   I O   
15582 N  N   . PRO   I  107 ? 1.4423 0.5498 1.1554 0.0028  -0.0221 -0.0003 106 PRO   I N   
15583 C  CA  . PRO   I  107 ? 1.4333 0.5535 1.1806 -0.0098 -0.0441 -0.0061 106 PRO   I CA  
15584 C  C   . PRO   I  107 ? 1.4825 0.4978 1.1635 0.0121  -0.1022 0.0240  106 PRO   I C   
15585 O  O   . PRO   I  107 ? 1.4482 0.3601 1.1823 0.0278  -0.0878 0.0112  106 PRO   I O   
15586 C  CB  . PRO   I  107 ? 1.4410 0.5878 1.1456 0.0008  -0.0128 -0.0180 106 PRO   I CB  
15587 C  CG  . PRO   I  107 ? 1.4691 0.5713 1.1145 -0.0103 -0.0252 -0.0080 106 PRO   I CG  
15588 C  CD  . PRO   I  107 ? 1.4694 0.5653 1.1096 -0.0016 -0.0307 -0.0156 106 PRO   I CD  
15589 N  N   . VAL   I  108 ? 1.4136 0.5767 1.2428 -0.0237 -0.1295 0.0007  107 VAL   I N   
15590 C  CA  . VAL   I  108 ? 1.4295 0.6613 1.2986 -0.0291 -0.1716 0.0060  107 VAL   I CA  
15591 C  C   . VAL   I  108 ? 1.4497 0.7050 1.2835 -0.0428 -0.1479 0.0466  107 VAL   I C   
15592 O  O   . VAL   I  108 ? 1.4715 0.8273 1.2715 -0.0238 -0.1335 0.0475  107 VAL   I O   
15593 C  CB  . VAL   I  108 ? 1.4271 0.5761 1.3581 -0.0603 -0.1815 0.0164  107 VAL   I CB  
15594 C  CG1 . VAL   I  108 ? 1.4245 0.5516 1.3866 -0.0957 -0.1788 0.0362  107 VAL   I CG1 
15595 C  CG2 . VAL   I  108 ? 1.4570 0.5953 1.3952 -0.0737 -0.1887 0.0403  107 VAL   I CG2 
15596 N  N   . VAL   I  109 ? 1.4901 0.7597 1.2723 -0.0159 -0.1565 0.0204  108 VAL   I N   
15597 C  CA  . VAL   I  109 ? 1.4586 0.7576 1.2839 -0.0106 -0.1463 -0.0033 108 VAL   I CA  
15598 C  C   . VAL   I  109 ? 1.4507 0.7848 1.2385 -0.0251 -0.1262 -0.0312 108 VAL   I C   
15599 O  O   . VAL   I  109 ? 1.3648 0.8032 1.1662 -0.0358 -0.1324 -0.0665 108 VAL   I O   
15600 C  CB  . VAL   I  109 ? 1.5161 0.8096 1.3061 -0.0301 -0.1482 -0.0345 108 VAL   I CB  
15601 C  CG1 . VAL   I  109 ? 1.4936 0.8895 1.3675 -0.0640 -0.1448 -0.0038 108 VAL   I CG1 
15602 C  CG2 . VAL   I  109 ? 1.5020 0.9076 1.3446 -0.0449 -0.1345 -0.0344 108 VAL   I CG2 
15603 N  N   . ALA   I  110 ? 1.4860 0.7417 1.2665 0.0031  -0.1126 -0.0084 109 ALA   I N   
15604 C  CA  . ALA   I  110 ? 1.4871 0.7697 1.3761 -0.0065 -0.1358 -0.0035 109 ALA   I CA  
15605 C  C   . ALA   I  110 ? 1.4692 0.7330 1.4487 -0.0004 -0.1509 -0.0433 109 ALA   I C   
15606 O  O   . ALA   I  110 ? 1.4480 0.6384 1.5304 0.0557  -0.1268 -0.0825 109 ALA   I O   
15607 C  CB  . ALA   I  110 ? 1.5695 0.7320 1.4013 -0.0108 -0.1361 0.0026  109 ALA   I CB  
15608 N  N   . GLY   I  111 ? 1.4649 0.8284 1.4616 0.0166  -0.1683 -0.0619 110 GLY   I N   
15609 C  CA  . GLY   I  111 ? 1.4919 0.8378 1.4968 0.0409  -0.0986 -0.0378 110 GLY   I CA  
15610 C  C   . GLY   I  111 ? 1.4862 0.8393 1.5391 0.0204  -0.0882 -0.0693 110 GLY   I C   
15611 O  O   . GLY   I  111 ? 1.5325 0.8882 1.5581 0.0569  -0.0597 -0.0369 110 GLY   I O   
15612 N  N   . ILE   I  112 ? 1.5255 0.8107 1.5754 0.0221  -0.0417 -0.1022 111 ILE   I N   
15613 C  CA  . ILE   I  112 ? 1.4619 0.8760 1.6010 0.0172  -0.0234 -0.0539 111 ILE   I CA  
15614 C  C   . ILE   I  112 ? 1.5438 0.8934 1.6756 0.0384  -0.0417 -0.0748 111 ILE   I C   
15615 O  O   . ILE   I  112 ? 1.5635 1.0483 1.5839 0.0308  -0.0158 -0.0158 111 ILE   I O   
15616 C  CB  . ILE   I  112 ? 1.4101 0.8046 1.6201 0.0080  -0.0382 -0.0332 111 ILE   I CB  
15617 C  CG1 . ILE   I  112 ? 1.3692 0.8187 1.6145 0.0232  -0.0184 -0.0244 111 ILE   I CG1 
15618 C  CG2 . ILE   I  112 ? 1.3899 0.7715 1.6331 0.0097  -0.0207 -0.0393 111 ILE   I CG2 
15619 C  CD1 . ILE   I  112 ? 1.3719 0.8755 1.6465 0.0188  0.0076  0.0022  111 ILE   I CD1 
15620 N  N   . ASN   I  113 ? 1.5739 0.9902 1.6845 0.0439  -0.0713 -0.0671 112 ASN   I N   
15621 C  CA  . ASN   I  113 ? 1.5644 0.9430 1.7579 0.0824  -0.0518 -0.0352 112 ASN   I CA  
15622 C  C   . ASN   I  113 ? 1.6076 0.8573 1.8830 0.0747  -0.0892 0.0111  112 ASN   I C   
15623 O  O   . ASN   I  113 ? 1.6564 0.7500 1.8967 0.1244  -0.1496 0.1008  112 ASN   I O   
15624 C  CB  . ASN   I  113 ? 1.5294 0.9774 1.7330 0.1259  0.0018  -0.0951 112 ASN   I CB  
15625 C  CG  . ASN   I  113 ? 1.5095 0.9892 1.7170 0.1160  0.0419  -0.0995 112 ASN   I CG  
15626 O  OD1 . ASN   I  113 ? 1.4174 0.9380 1.6763 0.1623  0.1110  -0.1751 112 ASN   I OD1 
15627 N  ND2 . ASN   I  113 ? 1.5679 1.0405 1.6709 0.1562  0.0697  -0.1388 112 ASN   I ND2 
15628 N  N   . SER   I  114 ? 1.6256 0.7752 1.9476 0.0220  -0.0882 -0.0072 113 SER   I N   
15629 C  CA  . SER   I  114 ? 1.6395 0.6523 1.9404 0.0036  -0.1233 -0.0688 113 SER   I CA  
15630 C  C   . SER   I  114 ? 1.6994 0.7145 1.9512 -0.0085 -0.1557 -0.0962 113 SER   I C   
15631 O  O   . SER   I  114 ? 1.7641 0.6645 1.9368 -0.0926 -0.1702 -0.0974 113 SER   I O   
15632 C  CB  . SER   I  114 ? 1.6230 0.4956 1.9673 0.0153  -0.0619 -0.1020 113 SER   I CB  
15633 O  OG  . SER   I  114 ? 1.6660 0.3380 2.0244 -0.0108 -0.0975 -0.1309 113 SER   I OG  
15634 N  N   . LYS   I  115 ? 1.6961 0.8114 1.8966 0.0148  -0.2626 -0.1765 114 LYS   I N   
15635 C  CA  . LYS   I  115 ? 1.6798 0.9502 1.9289 0.0109  -0.3354 -0.1652 114 LYS   I CA  
15636 C  C   . LYS   I  115 ? 1.6899 0.9417 1.9253 -0.0142 -0.3953 -0.1841 114 LYS   I C   
15637 O  O   . LYS   I  115 ? 1.7035 0.9123 1.9369 -0.0276 -0.4267 -0.1906 114 LYS   I O   
15638 C  CB  . LYS   I  115 ? 1.6687 1.0174 1.8839 0.0140  -0.3790 -0.2014 114 LYS   I CB  
15639 C  CG  . LYS   I  115 ? 1.6617 1.0451 1.9066 0.0050  -0.4108 -0.2264 114 LYS   I CG  
15640 C  CD  . LYS   I  115 ? 1.7008 1.0219 1.9037 0.0050  -0.4030 -0.2506 114 LYS   I CD  
15641 C  CE  . LYS   I  115 ? 1.7261 1.0805 1.9740 -0.0100 -0.4333 -0.3017 114 LYS   I CE  
15642 N  NZ  . LYS   I  115 ? 1.7388 1.1052 1.9675 -0.0007 -0.4691 -0.3358 114 LYS   I NZ  
15643 N  N   . SER   I  116 ? 1.7058 0.9663 1.8747 -0.0307 -0.4207 -0.1592 115 SER   I N   
15644 C  CA  . SER   I  116 ? 1.6721 1.0544 1.8289 -0.0803 -0.4574 -0.1139 115 SER   I CA  
15645 C  C   . SER   I  116 ? 1.5807 1.0891 1.8449 -0.0647 -0.4330 -0.0738 115 SER   I C   
15646 O  O   . SER   I  116 ? 1.5931 1.1947 1.8226 -0.0792 -0.4833 -0.0362 115 SER   I O   
15647 C  CB  . SER   I  116 ? 1.6972 1.1055 1.7368 -0.1106 -0.4829 -0.1368 115 SER   I CB  
15648 O  OG  . SER   I  116 ? 1.6987 1.1326 1.7085 -0.1580 -0.4725 -0.0979 115 SER   I OG  
15649 N  N   . GLY   I  117 ? 1.5457 1.0485 1.7898 -0.0532 -0.3509 -0.1054 116 GLY   I N   
15650 C  CA  . GLY   I  117 ? 1.5247 1.0569 1.7809 -0.0073 -0.3140 -0.0517 116 GLY   I CA  
15651 C  C   . GLY   I  117 ? 1.5238 1.0193 1.7321 0.0969  -0.3267 -0.0504 116 GLY   I C   
15652 O  O   . GLY   I  117 ? 1.4614 0.9188 1.6750 0.0838  -0.3208 0.0337  116 GLY   I O   
15653 N  N   . LYS   I  118 ? 1.5719 1.0212 1.7020 0.0986  -0.3433 -0.0319 117 LYS   I N   
15654 C  CA  . LYS   I  118 ? 1.6201 1.0072 1.7207 0.0909  -0.3655 -0.0535 117 LYS   I CA  
15655 C  C   . LYS   I  118 ? 1.6209 0.8935 1.7173 0.0715  -0.2998 -0.0902 117 LYS   I C   
15656 O  O   . LYS   I  118 ? 1.5819 0.8683 1.7669 0.0651  -0.2568 -0.1227 117 LYS   I O   
15657 C  CB  . LYS   I  118 ? 1.7061 1.1381 1.6995 0.1399  -0.3870 -0.0547 117 LYS   I CB  
15658 C  CG  . LYS   I  118 ? 1.7789 1.2656 1.7417 0.1646  -0.4508 -0.0254 117 LYS   I CG  
15659 C  CD  . LYS   I  118 ? 1.8420 1.3408 1.6943 0.1720  -0.4942 -0.0280 117 LYS   I CD  
15660 C  CE  . LYS   I  118 ? 1.8910 1.3889 1.7192 0.1513  -0.5278 -0.0424 117 LYS   I CE  
15661 N  NZ  . LYS   I  118 ? 1.8757 1.4288 1.7219 0.1606  -0.5595 -0.0295 117 LYS   I NZ  
15662 N  N   . PRO   I  119 ? 1.5787 0.8159 1.7279 0.0461  -0.2960 -0.0066 118 PRO   I N   
15663 C  CA  . PRO   I  119 ? 1.5632 0.6918 1.6767 0.0245  -0.2141 0.0215  118 PRO   I CA  
15664 C  C   . PRO   I  119 ? 1.6250 0.6196 1.5515 0.0212  -0.2237 0.0374  118 PRO   I C   
15665 O  O   . PRO   I  119 ? 1.5536 0.6231 1.5238 0.0103  -0.1884 0.0375  118 PRO   I O   
15666 C  CB  . PRO   I  119 ? 1.5770 0.7242 1.7592 0.0568  -0.2372 0.0000  118 PRO   I CB  
15667 C  CG  . PRO   I  119 ? 1.5955 0.7609 1.8095 0.0287  -0.2689 -0.0099 118 PRO   I CG  
15668 C  CD  . PRO   I  119 ? 1.5996 0.7674 1.7931 0.0505  -0.3045 -0.0026 118 PRO   I CD  
15669 N  N   . PHE   I  120 ? 1.5728 0.6059 1.5546 -0.0404 -0.1419 0.0550  119 PHE   I N   
15670 C  CA  . PHE   I  120 ? 1.6207 0.5627 1.5513 -0.0854 -0.1286 0.0892  119 PHE   I CA  
15671 C  C   . PHE   I  120 ? 1.6141 0.6063 1.5758 -0.1037 -0.0931 0.0377  119 PHE   I C   
15672 O  O   . PHE   I  120 ? 1.6273 0.4792 1.6021 -0.1916 -0.0542 0.1077  119 PHE   I O   
15673 C  CB  . PHE   I  120 ? 1.6299 0.5018 1.5585 -0.1018 -0.1242 0.1471  119 PHE   I CB  
15674 C  CG  . PHE   I  120 ? 1.6452 0.4136 1.5497 -0.1250 -0.1374 0.2377  119 PHE   I CG  
15675 C  CD1 . PHE   I  120 ? 1.6346 0.4011 1.5260 -0.1213 -0.1260 0.2488  119 PHE   I CD1 
15676 C  CD2 . PHE   I  120 ? 1.6652 0.4361 1.5633 -0.1521 -0.1690 0.2545  119 PHE   I CD2 
15677 C  CE1 . PHE   I  120 ? 1.6086 0.3961 1.5363 -0.1380 -0.1475 0.2387  119 PHE   I CE1 
15678 C  CE2 . PHE   I  120 ? 1.6571 0.4339 1.5702 -0.1503 -0.1677 0.2331  119 PHE   I CE2 
15679 C  CZ  . PHE   I  120 ? 1.6442 0.4078 1.5335 -0.1418 -0.1496 0.2312  119 PHE   I CZ  
15680 N  N   . ILE   I  121 ? 1.5468 0.5894 1.5091 -0.0875 -0.1123 0.0092  120 ILE   I N   
15681 C  CA  . ILE   I  121 ? 1.4994 0.6272 1.4798 -0.0495 -0.1102 -0.0374 120 ILE   I CA  
15682 C  C   . ILE   I  121 ? 1.4847 0.5424 1.4677 -0.0022 -0.1056 -0.0643 120 ILE   I C   
15683 O  O   . ILE   I  121 ? 1.4177 0.5632 1.4939 0.0350  -0.1160 -0.0561 120 ILE   I O   
15684 C  CB  . ILE   I  121 ? 1.4815 0.6150 1.4852 -0.0970 -0.1484 -0.0691 120 ILE   I CB  
15685 C  CG1 . ILE   I  121 ? 1.4874 0.6249 1.5201 -0.1199 -0.1836 -0.0564 120 ILE   I CG1 
15686 C  CG2 . ILE   I  121 ? 1.4976 0.7253 1.4932 -0.1119 -0.1352 -0.0967 120 ILE   I CG2 
15687 C  CD1 . ILE   I  121 ? 1.4997 0.6263 1.5739 -0.1013 -0.1739 -0.0537 120 ILE   I CD1 
15688 N  N   . ALA   I  122 ? 1.4973 0.4663 1.4383 0.0343  -0.1268 -0.1216 121 ALA   I N   
15689 C  CA  . ALA   I  122 ? 1.5562 0.5496 1.4211 0.0255  -0.1101 -0.1272 121 ALA   I CA  
15690 C  C   . ALA   I  122 ? 1.5704 0.5634 1.3780 0.0475  -0.1057 -0.1568 121 ALA   I C   
15691 O  O   . ALA   I  122 ? 1.6658 0.5876 1.3826 0.0943  -0.0752 -0.1105 121 ALA   I O   
15692 C  CB  . ALA   I  122 ? 1.6031 0.5907 1.4200 0.0214  -0.1221 -0.1760 121 ALA   I CB  
15693 N  N   . GLY   I  123 ? 1.5462 0.6294 1.3432 0.0259  -0.0860 -0.1849 122 GLY   I N   
15694 C  CA  . GLY   I  123 ? 1.5538 0.6569 1.3130 0.0377  -0.1018 -0.2434 122 GLY   I CA  
15695 C  C   . GLY   I  123 ? 1.5064 0.6616 1.2855 0.0449  -0.1406 -0.2570 122 GLY   I C   
15696 O  O   . GLY   I  123 ? 1.5241 0.7562 1.2706 0.0740  -0.1285 -0.2533 122 GLY   I O   
15697 N  N   . PHE   I  124 ? 1.5053 0.6346 1.2907 0.0615  -0.1507 -0.2407 123 PHE   I N   
15698 C  CA  . PHE   I  124 ? 1.4976 0.7077 1.2989 -0.0055 -0.1426 -0.1867 123 PHE   I CA  
15699 C  C   . PHE   I  124 ? 1.5265 0.5989 1.3332 0.0392  -0.1330 -0.1633 123 PHE   I C   
15700 O  O   . PHE   I  124 ? 1.5187 0.5977 1.3540 0.0918  -0.0755 -0.1648 123 PHE   I O   
15701 C  CB  . PHE   I  124 ? 1.5263 0.7218 1.3360 -0.0268 -0.1777 -0.1484 123 PHE   I CB  
15702 C  CG  . PHE   I  124 ? 1.5777 0.7526 1.3750 -0.0687 -0.1811 -0.1463 123 PHE   I CG  
15703 C  CD1 . PHE   I  124 ? 1.5570 0.7769 1.3922 -0.0745 -0.1668 -0.1655 123 PHE   I CD1 
15704 C  CD2 . PHE   I  124 ? 1.6222 0.8780 1.3378 -0.0913 -0.1957 -0.1822 123 PHE   I CD2 
15705 C  CE1 . PHE   I  124 ? 1.5131 0.8931 1.4159 -0.1233 -0.1399 -0.1517 123 PHE   I CE1 
15706 C  CE2 . PHE   I  124 ? 1.5989 1.0353 1.3780 -0.1775 -0.1895 -0.1556 123 PHE   I CE2 
15707 C  CZ  . PHE   I  124 ? 1.5662 0.9990 1.3936 -0.1713 -0.1767 -0.1824 123 PHE   I CZ  
15708 N  N   . ASP   I  125 ? 1.5733 0.6187 1.3079 0.0182  -0.1307 -0.1668 124 ASP   I N   
15709 C  CA  . ASP   I  125 ? 1.5748 0.6816 1.3941 -0.0017 -0.1513 -0.1456 124 ASP   I CA  
15710 C  C   . ASP   I  125 ? 1.5394 0.6642 1.3406 -0.0475 -0.1497 -0.1170 124 ASP   I C   
15711 O  O   . ASP   I  125 ? 1.5358 0.6517 1.2695 -0.0267 -0.1497 -0.0750 124 ASP   I O   
15712 C  CB  . ASP   I  125 ? 1.6450 0.6259 1.4958 -0.0251 -0.1628 -0.0889 124 ASP   I CB  
15713 C  CG  . ASP   I  125 ? 1.6940 0.6413 1.5823 -0.0513 -0.1998 -0.1640 124 ASP   I CG  
15714 O  OD1 . ASP   I  125 ? 1.7947 0.6306 1.7160 -0.0790 -0.2068 -0.1973 124 ASP   I OD1 
15715 O  OD2 . ASP   I  125 ? 1.6219 0.2937 1.7696 -0.0907 -0.3144 -0.0460 124 ASP   I OD2 
15716 N  N   . LEU   I  126 ? 1.4940 0.7961 1.3859 -0.0485 -0.1537 -0.1029 125 LEU   I N   
15717 C  CA  . LEU   I  126 ? 1.4523 0.7491 1.4093 -0.0763 -0.1347 -0.1080 125 LEU   I CA  
15718 C  C   . LEU   I  126 ? 1.5305 0.8153 1.3259 -0.1502 -0.1327 -0.1559 125 LEU   I C   
15719 O  O   . LEU   I  126 ? 1.5126 0.8731 1.3713 -0.1657 -0.1835 -0.1880 125 LEU   I O   
15720 C  CB  . LEU   I  126 ? 1.4397 0.6813 1.4348 -0.0874 -0.0608 -0.0963 125 LEU   I CB  
15721 C  CG  . LEU   I  126 ? 1.4371 0.6017 1.4531 -0.0944 -0.0495 -0.0967 125 LEU   I CG  
15722 C  CD1 . LEU   I  126 ? 1.3971 0.6834 1.4735 -0.0838 -0.0391 -0.0964 125 LEU   I CD1 
15723 C  CD2 . LEU   I  126 ? 1.4063 0.5541 1.4387 -0.0997 -0.0326 -0.1128 125 LEU   I CD2 
15724 N  N   . ILE   I  127 ? 1.4580 0.6969 1.3539 -0.0907 -0.1676 -0.0830 126 ILE   I N   
15725 C  CA  . ILE   I  127 ? 1.4702 0.7308 1.3850 -0.0311 -0.1708 -0.0881 126 ILE   I CA  
15726 C  C   . ILE   I  127 ? 1.4680 0.6895 1.3178 -0.0271 -0.1901 -0.0082 126 ILE   I C   
15727 O  O   . ILE   I  127 ? 1.5758 0.7213 1.2166 -0.0085 -0.1574 0.0664  126 ILE   I O   
15728 C  CB  . ILE   I  127 ? 1.4248 0.7521 1.3988 -0.0451 -0.1709 -0.1121 126 ILE   I CB  
15729 C  CG1 . ILE   I  127 ? 1.4571 0.8661 1.4925 -0.0290 -0.1170 -0.1316 126 ILE   I CG1 
15730 C  CG2 . ILE   I  127 ? 1.4592 0.7528 1.3559 -0.0643 -0.1889 -0.1656 126 ILE   I CG2 
15731 C  CD1 . ILE   I  127 ? 1.4581 0.8919 1.5230 -0.0286 -0.1234 -0.1259 126 ILE   I CD1 
15732 N  N   . GLY   I  128 ? 1.4487 0.6568 1.3362 0.0039  -0.2074 0.0085  127 GLY   I N   
15733 C  CA  . GLY   I  128 ? 1.4566 0.6710 1.3572 -0.0070 -0.2250 -0.0092 127 GLY   I CA  
15734 C  C   . GLY   I  128 ? 1.4837 0.6621 1.3398 -0.0005 -0.2361 0.0035  127 GLY   I C   
15735 O  O   . GLY   I  128 ? 1.4165 0.7195 1.3415 0.0076  -0.2783 0.0500  127 GLY   I O   
15736 N  N   . CYS   I  129 ? 1.4842 0.6479 1.3284 -0.0354 -0.2117 -0.0088 128 CYS   I N   
15737 C  CA  . CYS   I  129 ? 1.4629 0.7428 1.3120 -0.0208 -0.1928 -0.0171 128 CYS   I CA  
15738 C  C   . CYS   I  129 ? 1.4943 0.7496 1.3054 -0.0369 -0.1531 0.0032  128 CYS   I C   
15739 O  O   . CYS   I  129 ? 1.3535 0.6746 1.3316 -0.0926 -0.1325 0.0164  128 CYS   I O   
15740 C  CB  . CYS   I  129 ? 1.5083 0.7269 1.3440 0.0349  -0.2130 -0.0150 128 CYS   I CB  
15741 S  SG  . CYS   I  129 ? 1.4993 0.7325 1.4318 0.1505  -0.2179 -0.0358 128 CYS   I SG  
15742 N  N   . ILE   I  130 ? 1.4998 0.7942 1.3031 -0.0606 -0.1489 0.0085  129 ILE   I N   
15743 C  CA  . ILE   I  130 ? 1.5000 0.7997 1.3264 -0.0390 -0.1449 -0.0077 129 ILE   I CA  
15744 C  C   . ILE   I  130 ? 1.6141 0.7897 1.3146 -0.0061 -0.1329 0.0211  129 ILE   I C   
15745 O  O   . ILE   I  130 ? 1.6745 0.7122 1.2995 -0.0332 -0.1431 -0.0057 129 ILE   I O   
15746 C  CB  . ILE   I  130 ? 1.4852 0.8390 1.3331 -0.0739 -0.1733 -0.0169 129 ILE   I CB  
15747 C  CG1 . ILE   I  130 ? 1.4495 0.8581 1.3602 -0.0721 -0.1555 -0.0283 129 ILE   I CG1 
15748 C  CG2 . ILE   I  130 ? 1.4650 0.7803 1.3478 -0.0878 -0.1977 -0.0070 129 ILE   I CG2 
15749 C  CD1 . ILE   I  130 ? 1.4525 0.9420 1.3626 -0.1111 -0.1705 -0.0721 129 ILE   I CD1 
15750 N  N   . ASP   I  131 ? 1.6681 0.7532 1.4440 0.0862  -0.0899 0.0136  130 ASP   I N   
15751 C  CA  . ASP   I  131 ? 1.6924 0.8623 1.5610 0.1519  -0.0798 0.0470  130 ASP   I CA  
15752 C  C   . ASP   I  131 ? 1.5843 0.7508 1.5980 0.1571  -0.1623 -0.0388 130 ASP   I C   
15753 O  O   . ASP   I  131 ? 1.4732 0.5880 1.6196 0.2460  -0.0682 -0.0352 130 ASP   I O   
15754 C  CB  . ASP   I  131 ? 1.7960 0.8888 1.6127 0.1359  -0.0662 0.0327  130 ASP   I CB  
15755 C  CG  . ASP   I  131 ? 1.8755 0.9183 1.6198 0.2145  -0.0704 0.1295  130 ASP   I CG  
15756 O  OD1 . ASP   I  131 ? 2.0270 0.8946 1.4764 0.2409  -0.1204 0.3694  130 ASP   I OD1 
15757 O  OD2 . ASP   I  131 ? 2.0135 0.7896 1.6972 0.1787  -0.0191 0.1212  130 ASP   I OD2 
15758 N  N   . GLU   I  132 ? 1.5949 0.8903 1.5997 0.1695  -0.2118 -0.0225 131 GLU   I N   
15759 C  CA  . GLU   I  132 ? 1.6104 1.0568 1.6194 0.1037  -0.2437 0.0050  131 GLU   I CA  
15760 C  C   . GLU   I  132 ? 1.5317 1.1226 1.5195 0.0938  -0.2814 -0.0064 131 GLU   I C   
15761 O  O   . GLU   I  132 ? 1.6634 1.2389 1.5538 0.0500  -0.2996 0.0570  131 GLU   I O   
15762 C  CB  . GLU   I  132 ? 1.6117 1.1226 1.7131 0.1022  -0.2895 -0.0471 131 GLU   I CB  
15763 C  CG  . GLU   I  132 ? 1.5935 1.2981 1.8618 0.1052  -0.2303 0.0846  131 GLU   I CG  
15764 C  CD  . GLU   I  132 ? 1.7029 1.3389 2.0162 0.1505  -0.2191 -0.0042 131 GLU   I CD  
15765 O  OE1 . GLU   I  132 ? 1.7348 1.2970 2.1549 0.1770  -0.2123 0.0516  131 GLU   I OE1 
15766 O  OE2 . GLU   I  132 ? 1.6882 1.7382 2.3480 0.2054  -0.2324 0.1157  131 GLU   I OE2 
15767 N  N   . ALA   I  133 ? 1.5186 1.1276 1.4378 -0.0326 -0.3235 0.0244  132 ALA   I N   
15768 C  CA  . ALA   I  133 ? 1.4949 1.1234 1.4277 -0.0452 -0.3010 0.0500  132 ALA   I CA  
15769 C  C   . ALA   I  133 ? 1.5547 1.0868 1.4683 -0.0807 -0.2757 0.0741  132 ALA   I C   
15770 O  O   . ALA   I  133 ? 1.6073 1.1030 1.4937 -0.1240 -0.2465 0.0972  132 ALA   I O   
15771 C  CB  . ALA   I  133 ? 1.4677 1.1593 1.4114 -0.0286 -0.3104 0.0448  132 ALA   I CB  
15772 N  N   . LYS   I  134 ? 1.5969 1.1007 1.5357 -0.0517 -0.2928 0.0948  133 LYS   I N   
15773 C  CA  . LYS   I  134 ? 1.6100 1.1856 1.6057 -0.0797 -0.2835 0.0867  133 LYS   I CA  
15774 C  C   . LYS   I  134 ? 1.5931 1.0721 1.6453 -0.0599 -0.2387 0.0792  133 LYS   I C   
15775 O  O   . LYS   I  134 ? 1.6480 1.0469 1.6655 0.0085  -0.1629 0.0820  133 LYS   I O   
15776 C  CB  . LYS   I  134 ? 1.6539 1.3990 1.6450 -0.1242 -0.3855 0.0855  133 LYS   I CB  
15777 C  CG  . LYS   I  134 ? 1.7278 1.5917 1.6596 -0.1668 -0.4314 0.0311  133 LYS   I CG  
15778 C  CD  . LYS   I  134 ? 1.7218 1.7413 1.7232 -0.2198 -0.5160 0.0275  133 LYS   I CD  
15779 C  CE  . LYS   I  134 ? 1.6939 1.7908 1.7461 -0.2349 -0.5833 -0.0005 133 LYS   I CE  
15780 N  NZ  . LYS   I  134 ? 1.6977 1.8359 1.8436 -0.2290 -0.6031 -0.0226 133 LYS   I NZ  
15781 N  N   . ASP   I  135 ? 1.5730 1.0365 1.6020 -0.0171 -0.2128 0.0529  134 ASP   I N   
15782 C  CA  . ASP   I  135 ? 1.5384 1.0079 1.6569 -0.0192 -0.2009 0.0261  134 ASP   I CA  
15783 C  C   . ASP   I  135 ? 1.4870 0.7902 1.6228 0.0696  -0.1515 -0.0262 134 ASP   I C   
15784 O  O   . ASP   I  135 ? 1.4433 0.6218 1.6807 0.0738  -0.1000 -0.0621 134 ASP   I O   
15785 C  CB  . ASP   I  135 ? 1.5754 1.0572 1.6461 -0.0313 -0.2564 0.0809  134 ASP   I CB  
15786 C  CG  . ASP   I  135 ? 1.5758 1.1240 1.6087 -0.0810 -0.2994 0.0858  134 ASP   I CG  
15787 O  OD1 . ASP   I  135 ? 1.5246 1.1529 1.5487 -0.1259 -0.2963 0.0533  134 ASP   I OD1 
15788 O  OD2 . ASP   I  135 ? 1.7116 1.1019 1.5630 -0.1677 -0.3581 0.0942  134 ASP   I OD2 
15789 N  N   . PHE   I  136 ? 1.4595 0.7439 1.6051 0.1141  -0.1068 -0.0717 135 PHE   I N   
15790 C  CA  . PHE   I  136 ? 1.4345 0.7033 1.5722 0.0896  -0.0685 -0.1179 135 PHE   I CA  
15791 C  C   . PHE   I  136 ? 1.4105 0.6932 1.5539 0.0409  -0.1032 -0.1110 135 PHE   I C   
15792 O  O   . PHE   I  136 ? 1.4512 0.6027 1.5443 0.0368  -0.1284 -0.1322 135 PHE   I O   
15793 C  CB  . PHE   I  136 ? 1.4473 0.7143 1.5699 0.0859  -0.0268 -0.1210 135 PHE   I CB  
15794 C  CG  . PHE   I  136 ? 1.4687 0.6778 1.5806 0.1233  -0.0110 -0.1423 135 PHE   I CG  
15795 C  CD1 . PHE   I  136 ? 1.4491 0.6829 1.5572 0.1501  0.0094  -0.1614 135 PHE   I CD1 
15796 C  CD2 . PHE   I  136 ? 1.4713 0.6362 1.6354 0.1462  -0.0027 -0.1555 135 PHE   I CD2 
15797 C  CE1 . PHE   I  136 ? 1.4630 0.6741 1.5892 0.1726  0.0080  -0.1634 135 PHE   I CE1 
15798 C  CE2 . PHE   I  136 ? 1.4674 0.6824 1.6687 0.1861  -0.0087 -0.1238 135 PHE   I CE2 
15799 C  CZ  . PHE   I  136 ? 1.4608 0.7196 1.6604 0.1772  -0.0016 -0.1434 135 PHE   I CZ  
15800 N  N   . ILE   I  137 ? 1.4100 0.7406 1.5158 -0.0015 -0.1191 -0.0970 136 ILE   I N   
15801 C  CA  . ILE   I  137 ? 1.4076 0.7824 1.4670 -0.0016 -0.1420 -0.0834 136 ILE   I CA  
15802 C  C   . ILE   I  137 ? 1.3937 0.6330 1.4724 0.0121  -0.0734 -0.0990 136 ILE   I C   
15803 O  O   . ILE   I  137 ? 1.4223 0.6090 1.5042 0.0303  0.0014  -0.1556 136 ILE   I O   
15804 C  CB  . ILE   I  137 ? 1.4345 0.7662 1.4301 -0.0233 -0.1776 -0.0863 136 ILE   I CB  
15805 C  CG1 . ILE   I  137 ? 1.4782 0.8353 1.3994 -0.0450 -0.2140 -0.0500 136 ILE   I CG1 
15806 C  CG2 . ILE   I  137 ? 1.4361 0.8490 1.4093 -0.0230 -0.1611 -0.0878 136 ILE   I CG2 
15807 C  CD1 . ILE   I  137 ? 1.4926 0.8884 1.4066 -0.0638 -0.2156 -0.0357 136 ILE   I CD1 
15808 N  N   . VAL   I  138 ? 1.4073 0.5646 1.5000 0.0286  -0.0668 -0.0864 137 VAL   I N   
15809 C  CA  . VAL   I  138 ? 1.3666 0.6313 1.4758 -0.0144 -0.0510 -0.0669 137 VAL   I CA  
15810 C  C   . VAL   I  138 ? 1.3648 0.5921 1.4252 -0.0097 -0.0680 -0.0646 137 VAL   I C   
15811 O  O   . VAL   I  138 ? 1.3858 0.6447 1.4470 0.0355  -0.0415 -0.0658 137 VAL   I O   
15812 C  CB  . VAL   I  138 ? 1.4001 0.6069 1.5094 -0.0721 -0.0341 -0.0785 137 VAL   I CB  
15813 C  CG1 . VAL   I  138 ? 1.4015 0.6521 1.5147 -0.0862 0.0018  -0.0642 137 VAL   I CG1 
15814 C  CG2 . VAL   I  138 ? 1.4016 0.6706 1.5101 -0.1005 -0.0430 -0.0739 137 VAL   I CG2 
15815 N  N   . SER   I  139 ? 1.3323 0.5879 1.4422 -0.0270 -0.0722 -0.0749 138 SER   I N   
15816 C  CA  . SER   I  139 ? 1.3315 0.6383 1.4309 -0.0242 -0.1063 -0.0756 138 SER   I CA  
15817 C  C   . SER   I  139 ? 1.3345 0.6146 1.4321 -0.0059 -0.1131 -0.0683 138 SER   I C   
15818 O  O   . SER   I  139 ? 1.2772 0.6397 1.4599 0.0346  -0.1063 -0.0374 138 SER   I O   
15819 C  CB  . SER   I  139 ? 1.2937 0.6369 1.4047 -0.0396 -0.1238 -0.0753 138 SER   I CB  
15820 O  OG  . SER   I  139 ? 1.2872 0.7144 1.3924 -0.0305 -0.1476 -0.0729 138 SER   I OG  
15821 N  N   . GLY   I  140 ? 1.3663 0.5761 1.4912 -0.0411 -0.1169 -0.0582 139 GLY   I N   
15822 C  CA  . GLY   I  140 ? 1.3898 0.6072 1.5019 -0.0421 -0.1008 -0.1109 139 GLY   I CA  
15823 C  C   . GLY   I  140 ? 1.3775 0.6000 1.5188 -0.0325 -0.0936 -0.1373 139 GLY   I C   
15824 O  O   . GLY   I  140 ? 1.3882 0.5300 1.5571 0.0082  -0.0933 -0.1256 139 GLY   I O   
15825 N  N   . THR   I  141 ? 1.3501 0.5810 1.5162 -0.0240 -0.0683 -0.1530 140 THR   I N   
15826 C  CA  . THR   I  141 ? 1.3847 0.5404 1.5102 0.0173  -0.0681 -0.1885 140 THR   I CA  
15827 C  C   . THR   I  141 ? 1.3573 0.5626 1.5288 0.0119  -0.0753 -0.1798 140 THR   I C   
15828 O  O   . THR   I  141 ? 1.3898 0.5706 1.6278 0.0374  -0.0883 -0.1217 140 THR   I O   
15829 C  CB  . THR   I  141 ? 1.4448 0.5068 1.4552 0.0214  -0.0403 -0.2269 140 THR   I CB  
15830 O  OG1 . THR   I  141 ? 1.4183 0.4460 1.4321 0.0175  -0.0255 -0.2797 140 THR   I OG1 
15831 C  CG2 . THR   I  141 ? 1.4781 0.4657 1.4391 0.0482  -0.0540 -0.2442 140 THR   I CG2 
15832 N  N   . ALA   I  142 ? 1.4009 0.5239 1.4623 -0.0357 -0.0574 -0.1653 141 ALA   I N   
15833 C  CA  . ALA   I  142 ? 1.3887 0.5560 1.4818 -0.0299 -0.0443 -0.1740 141 ALA   I CA  
15834 C  C   . ALA   I  142 ? 1.3880 0.5187 1.4874 -0.0507 -0.0460 -0.1502 141 ALA   I C   
15835 O  O   . ALA   I  142 ? 1.3966 0.3839 1.5356 -0.0212 -0.0204 -0.1491 141 ALA   I O   
15836 C  CB  . ALA   I  142 ? 1.4097 0.6044 1.4815 0.0024  -0.0382 -0.1616 141 ALA   I CB  
15837 N  N   . SER   I  143 ? 1.3882 0.5889 1.4231 -0.1194 -0.0587 -0.1271 142 SER   I N   
15838 C  CA  . SER   I  143 ? 1.4083 0.5215 1.4252 -0.1817 -0.0436 -0.1113 142 SER   I CA  
15839 C  C   . SER   I  143 ? 1.3888 0.6263 1.4721 -0.1348 -0.0732 -0.0919 142 SER   I C   
15840 O  O   . SER   I  143 ? 1.4133 0.4568 1.4713 -0.2031 -0.0746 -0.0678 142 SER   I O   
15841 C  CB  . SER   I  143 ? 1.4307 0.4162 1.3708 -0.2476 -0.0571 -0.1341 142 SER   I CB  
15842 O  OG  . SER   I  143 ? 1.5013 0.4770 1.3623 -0.2999 -0.0357 -0.1418 142 SER   I OG  
15843 N  N   . ASP   I  144 ? 1.3854 0.6422 1.5191 -0.1301 -0.0408 -0.0575 143 ASP   I N   
15844 C  CA  . ASP   I  144 ? 1.4038 0.7242 1.5723 -0.0927 -0.0582 -0.0228 143 ASP   I CA  
15845 C  C   . ASP   I  144 ? 1.4210 0.7197 1.5469 -0.0925 -0.0571 -0.0435 143 ASP   I C   
15846 O  O   . ASP   I  144 ? 1.3618 0.7585 1.6753 -0.0750 -0.0392 -0.0733 143 ASP   I O   
15847 C  CB  . ASP   I  144 ? 1.3676 0.8455 1.6620 -0.1485 -0.0579 -0.0169 143 ASP   I CB  
15848 C  CG  . ASP   I  144 ? 1.3986 0.9179 1.6851 -0.1183 -0.0392 -0.0397 143 ASP   I CG  
15849 O  OD1 . ASP   I  144 ? 1.3985 0.8148 1.7034 -0.1228 -0.1234 0.0223  143 ASP   I OD1 
15850 O  OD2 . ASP   I  144 ? 1.4299 1.0604 1.8635 -0.2096 -0.0250 0.0658  143 ASP   I OD2 
15851 N  N   . GLN   I  145 ? 1.3987 0.6881 1.5367 -0.0773 -0.0551 -0.0448 144 GLN   I N   
15852 C  CA  . GLN   I  145 ? 1.3771 0.6983 1.5186 -0.0754 -0.0732 -0.0662 144 GLN   I CA  
15853 C  C   . GLN   I  145 ? 1.3253 0.7424 1.5067 -0.0691 -0.1150 -0.0421 144 GLN   I C   
15854 O  O   . GLN   I  145 ? 1.3610 0.7721 1.5085 0.0009  -0.0941 0.0039  144 GLN   I O   
15855 C  CB  . GLN   I  145 ? 1.3700 0.6307 1.4872 -0.1099 -0.0105 -0.1418 144 GLN   I CB  
15856 C  CG  . GLN   I  145 ? 1.3677 0.6241 1.4950 -0.1054 0.0198  -0.1739 144 GLN   I CG  
15857 C  CD  . GLN   I  145 ? 1.3383 0.5235 1.4655 -0.1577 0.0072  -0.1996 144 GLN   I CD  
15858 O  OE1 . GLN   I  145 ? 1.2394 0.4888 1.4610 -0.1490 0.0627  -0.1364 144 GLN   I OE1 
15859 N  NE2 . GLN   I  145 ? 1.3298 0.5378 1.4808 -0.1652 0.0229  -0.2305 144 GLN   I NE2 
15860 N  N   . LEU   I  146 ? 1.3651 0.7575 1.5121 -0.0460 -0.1607 -0.0654 145 LEU   I N   
15861 C  CA  . LEU   I  146 ? 1.4032 0.7479 1.5007 -0.0429 -0.1875 -0.0967 145 LEU   I CA  
15862 C  C   . LEU   I  146 ? 1.3526 0.6817 1.5177 -0.0613 -0.1922 -0.0969 145 LEU   I C   
15863 O  O   . LEU   I  146 ? 1.3333 0.6544 1.5940 -0.0365 -0.2256 -0.1222 145 LEU   I O   
15864 C  CB  . LEU   I  146 ? 1.3990 0.8011 1.4687 -0.0055 -0.2029 -0.0714 145 LEU   I CB  
15865 C  CG  . LEU   I  146 ? 1.4051 0.8448 1.4579 -0.0142 -0.1879 -0.0631 145 LEU   I CG  
15866 C  CD1 . LEU   I  146 ? 1.4284 0.8540 1.4556 -0.0066 -0.1982 -0.0468 145 LEU   I CD1 
15867 C  CD2 . LEU   I  146 ? 1.4003 0.8366 1.4370 -0.0002 -0.1792 -0.0751 145 LEU   I CD2 
15868 N  N   . PHE   I  147 ? 1.3892 0.6160 1.4779 -0.0731 -0.2136 -0.0870 146 PHE   I N   
15869 C  CA  . PHE   I  147 ? 1.3687 0.6418 1.4692 -0.0945 -0.2024 -0.0588 146 PHE   I CA  
15870 C  C   . PHE   I  147 ? 1.3702 0.7035 1.5063 -0.0710 -0.1808 -0.0375 146 PHE   I C   
15871 O  O   . PHE   I  147 ? 1.4049 0.6008 1.5083 -0.1805 -0.1483 -0.0862 146 PHE   I O   
15872 C  CB  . PHE   I  147 ? 1.3380 0.6483 1.4224 -0.0951 -0.2429 -0.0510 146 PHE   I CB  
15873 C  CG  . PHE   I  147 ? 1.3257 0.6736 1.3543 -0.1131 -0.2681 -0.0692 146 PHE   I CG  
15874 C  CD1 . PHE   I  147 ? 1.3273 0.7013 1.3259 -0.1060 -0.2896 -0.0713 146 PHE   I CD1 
15875 C  CD2 . PHE   I  147 ? 1.3268 0.6913 1.3436 -0.1190 -0.2563 -0.0763 146 PHE   I CD2 
15876 C  CE1 . PHE   I  147 ? 1.3427 0.7204 1.3014 -0.1292 -0.3053 -0.1063 146 PHE   I CE1 
15877 C  CE2 . PHE   I  147 ? 1.3110 0.7047 1.2895 -0.1462 -0.2742 -0.0977 146 PHE   I CE2 
15878 C  CZ  . PHE   I  147 ? 1.3359 0.7369 1.2775 -0.1532 -0.2946 -0.1047 146 PHE   I CZ  
15879 N  N   . GLY   I  148 ? 1.4043 0.7670 1.5063 -0.0621 -0.1795 -0.0885 147 GLY   I N   
15880 C  CA  . GLY   I  148 ? 1.4244 0.8305 1.5730 -0.0160 -0.1502 -0.0542 147 GLY   I CA  
15881 C  C   . GLY   I  148 ? 1.4551 0.8841 1.5946 -0.0067 -0.1084 -0.0511 147 GLY   I C   
15882 O  O   . GLY   I  148 ? 1.3985 0.9134 1.6342 -0.0321 -0.0444 -0.0104 147 GLY   I O   
15883 N  N   . MET   I  149 ? 1.5037 0.9950 1.5273 -0.0043 -0.0804 -0.0650 148 MET   I N   
15884 C  CA  . MET   I  149 ? 1.5292 1.0680 1.5322 0.0200  -0.0498 -0.0651 148 MET   I CA  
15885 C  C   . MET   I  149 ? 1.5228 1.0562 1.5953 0.0154  -0.0316 -0.0737 148 MET   I C   
15886 O  O   . MET   I  149 ? 1.5519 1.0255 1.6368 0.1155  0.0311  -0.0904 148 MET   I O   
15887 C  CB  . MET   I  149 ? 1.5728 1.1534 1.5019 0.0176  -0.0430 -0.0424 148 MET   I CB  
15888 C  CG  . MET   I  149 ? 1.6196 1.2470 1.4406 0.0342  -0.0882 -0.0469 148 MET   I CG  
15889 S  SD  . MET   I  149 ? 1.6360 1.4167 1.4309 0.1230  -0.0591 -0.0206 148 MET   I SD  
15890 C  CE  . MET   I  149 ? 1.7037 1.3259 1.4371 0.0752  -0.0743 -0.0040 148 MET   I CE  
15891 N  N   . CYS   I  150 ? 1.5537 1.0371 1.5909 0.0253  -0.0473 -0.0592 149 CYS   I N   
15892 C  CA  . CYS   I  150 ? 1.4995 1.0767 1.5744 0.0150  -0.0901 -0.0338 149 CYS   I CA  
15893 C  C   . CYS   I  150 ? 1.5170 1.0956 1.5890 -0.0247 -0.1251 -0.0321 149 CYS   I C   
15894 O  O   . CYS   I  150 ? 1.4976 1.1287 1.6394 -0.0073 -0.0928 0.0327  149 CYS   I O   
15895 C  CB  . CYS   I  150 ? 1.4620 1.0843 1.5253 0.0368  -0.1285 -0.0021 149 CYS   I CB  
15896 S  SG  . CYS   I  150 ? 1.4290 1.0203 1.5887 0.1375  -0.1174 -0.0231 149 CYS   I SG  
15897 N  N   . GLU   I  151 ? 1.5150 1.0903 1.5313 -0.0413 -0.1592 -0.0553 150 GLU   I N   
15898 C  CA  . GLU   I  151 ? 1.5089 1.0717 1.5295 -0.0652 -0.1623 -0.0504 150 GLU   I CA  
15899 C  C   . GLU   I  151 ? 1.5522 1.0519 1.5317 -0.0550 -0.1731 -0.1425 150 GLU   I C   
15900 O  O   . GLU   I  151 ? 1.5744 1.0962 1.5638 -0.1044 -0.1978 -0.1906 150 GLU   I O   
15901 C  CB  . GLU   I  151 ? 1.5053 1.0319 1.5694 -0.0627 -0.1773 -0.0113 150 GLU   I CB  
15902 C  CG  . GLU   I  151 ? 1.5247 1.0487 1.5836 -0.0977 -0.1516 0.0725  150 GLU   I CG  
15903 C  CD  . GLU   I  151 ? 1.5544 1.0550 1.6211 -0.1070 -0.1182 0.0576  150 GLU   I CD  
15904 O  OE1 . GLU   I  151 ? 1.4448 1.1227 1.5848 -0.1345 -0.1898 0.1163  150 GLU   I OE1 
15905 O  OE2 . GLU   I  151 ? 1.5708 1.1376 1.6494 -0.1234 -0.1207 0.0183  150 GLU   I OE2 
15906 N  N   . SER   I  152 ? 1.5514 1.0641 1.5759 -0.0260 -0.1187 -0.1768 151 SER   I N   
15907 C  CA  . SER   I  152 ? 1.5014 1.1428 1.6301 -0.0291 -0.0835 -0.1429 151 SER   I CA  
15908 C  C   . SER   I  152 ? 1.4956 1.0811 1.6851 -0.0110 -0.0689 -0.1386 151 SER   I C   
15909 O  O   . SER   I  152 ? 1.5184 1.0746 1.7355 -0.0099 -0.1070 -0.0866 151 SER   I O   
15910 C  CB  . SER   I  152 ? 1.5217 1.1788 1.6342 -0.0061 -0.0496 -0.2017 151 SER   I CB  
15911 O  OG  . SER   I  152 ? 1.5524 1.2776 1.5466 -0.0394 -0.0496 -0.2701 151 SER   I OG  
15912 N  N   . LEU   I  153 ? 1.4629 1.0106 1.7027 0.0139  -0.0322 -0.1395 152 LEU   I N   
15913 C  CA  . LEU   I  153 ? 1.5029 0.9921 1.7200 0.0615  -0.0177 -0.0859 152 LEU   I CA  
15914 C  C   . LEU   I  153 ? 1.5470 1.0003 1.7292 0.0400  -0.0158 -0.0830 152 LEU   I C   
15915 O  O   . LEU   I  153 ? 1.6067 1.0179 1.7522 0.0035  0.0713  -0.1270 152 LEU   I O   
15916 C  CB  . LEU   I  153 ? 1.4963 0.9749 1.7224 0.1060  0.0116  -0.0553 152 LEU   I CB  
15917 C  CG  . LEU   I  153 ? 1.5137 0.9955 1.6926 0.1368  0.0098  -0.0641 152 LEU   I CG  
15918 C  CD1 . LEU   I  153 ? 1.5425 1.0072 1.6775 0.1610  0.0230  -0.0680 152 LEU   I CD1 
15919 C  CD2 . LEU   I  153 ? 1.5328 1.0588 1.7643 0.1675  0.0580  -0.0551 152 LEU   I CD2 
15920 N  N   . TYR   I  154 ? 1.5183 0.9992 1.7084 0.0545  -0.0526 -0.0744 153 TYR   I N   
15921 C  CA  . TYR   I  154 ? 1.5220 0.9954 1.7302 0.0300  -0.0994 -0.0502 153 TYR   I CA  
15922 C  C   . TYR   I  154 ? 1.5513 0.9597 1.7763 -0.0229 -0.1422 -0.0445 153 TYR   I C   
15923 O  O   . TYR   I  154 ? 1.5714 1.0208 1.7869 -0.0825 -0.2425 -0.0099 153 TYR   I O   
15924 C  CB  . TYR   I  154 ? 1.5330 0.9800 1.6807 0.0118  -0.1134 -0.0766 153 TYR   I CB  
15925 C  CG  . TYR   I  154 ? 1.6037 1.0074 1.7348 0.0122  -0.0980 -0.1339 153 TYR   I CG  
15926 C  CD1 . TYR   I  154 ? 1.6375 1.0384 1.6937 0.0642  -0.0926 -0.1585 153 TYR   I CD1 
15927 C  CD2 . TYR   I  154 ? 1.6685 0.9821 1.7131 0.0588  -0.1016 -0.1084 153 TYR   I CD2 
15928 C  CE1 . TYR   I  154 ? 1.6937 1.0513 1.7145 0.0733  -0.0658 -0.1999 153 TYR   I CE1 
15929 C  CE2 . TYR   I  154 ? 1.7372 1.0322 1.7209 0.0799  -0.0807 -0.2158 153 TYR   I CE2 
15930 C  CZ  . TYR   I  154 ? 1.7574 1.0618 1.7083 0.0748  -0.0727 -0.2071 153 TYR   I CZ  
15931 O  OH  . TYR   I  154 ? 1.8293 1.0474 1.6849 0.0884  -0.0606 -0.2095 153 TYR   I OH  
15932 N  N   . GLU   I  155 ? 1.5711 0.9347 1.8227 -0.0131 -0.1298 -0.0259 154 GLU   I N   
15933 C  CA  . GLU   I  155 ? 1.5674 1.0303 1.8923 -0.0101 -0.1627 -0.0034 154 GLU   I CA  
15934 C  C   . GLU   I  155 ? 1.5940 1.0400 1.9181 -0.0107 -0.1683 -0.0416 154 GLU   I C   
15935 O  O   . GLU   I  155 ? 1.5487 1.0512 1.9389 0.0288  -0.1702 -0.0458 154 GLU   I O   
15936 C  CB  . GLU   I  155 ? 1.5598 1.0199 1.9953 -0.0093 -0.1532 0.0007  154 GLU   I CB  
15937 C  CG  . GLU   I  155 ? 1.5375 1.0397 2.0114 0.0003  -0.1266 -0.0091 154 GLU   I CG  
15938 C  CD  . GLU   I  155 ? 1.4933 1.0731 2.1799 0.0044  -0.1476 0.0095  154 GLU   I CD  
15939 O  OE1 . GLU   I  155 ? 1.5093 0.9910 2.2283 0.0320  -0.1726 -0.0377 154 GLU   I OE1 
15940 O  OE2 . GLU   I  155 ? 1.4820 1.1178 2.2114 0.0813  -0.1016 -0.0279 154 GLU   I OE2 
15941 N  N   . PRO   I  156 ? 1.6367 1.0311 1.9298 -0.0425 -0.1590 -0.0577 155 PRO   I N   
15942 C  CA  . PRO   I  156 ? 1.6290 1.0375 1.9027 -0.0359 -0.1296 -0.0686 155 PRO   I CA  
15943 C  C   . PRO   I  156 ? 1.6450 1.1328 1.9226 -0.0038 -0.0746 -0.0503 155 PRO   I C   
15944 O  O   . PRO   I  156 ? 1.7394 1.1675 1.9934 0.0720  -0.0224 -0.0081 155 PRO   I O   
15945 C  CB  . PRO   I  156 ? 1.6526 1.0298 1.9152 -0.0573 -0.1579 -0.0533 155 PRO   I CB  
15946 C  CG  . PRO   I  156 ? 1.6693 1.0201 1.9161 -0.0626 -0.1749 -0.0580 155 PRO   I CG  
15947 C  CD  . PRO   I  156 ? 1.6737 0.9936 1.9370 -0.0662 -0.1704 -0.0572 155 PRO   I CD  
15948 N  N   . ASN   I  157 ? 1.5875 1.1250 1.8950 -0.0033 -0.0760 -0.0787 156 ASN   I N   
15949 C  CA  . ASN   I  157 ? 1.5332 1.1339 1.9697 -0.0223 -0.1025 -0.0859 156 ASN   I CA  
15950 C  C   . ASN   I  157 ? 1.5277 1.1317 1.9853 -0.0205 -0.0655 -0.0737 156 ASN   I C   
15951 O  O   . ASN   I  157 ? 1.5224 1.1685 2.0597 -0.1442 -0.0662 -0.0992 156 ASN   I O   
15952 C  CB  . ASN   I  157 ? 1.5091 1.2228 2.0261 -0.0353 -0.1085 -0.0782 156 ASN   I CB  
15953 C  CG  . ASN   I  157 ? 1.4744 1.2840 2.0071 -0.0276 -0.1390 -0.0825 156 ASN   I CG  
15954 O  OD1 . ASN   I  157 ? 1.4151 1.3397 2.0503 -0.0885 -0.1519 -0.0268 156 ASN   I OD1 
15955 N  ND2 . ASN   I  157 ? 1.4703 1.3079 1.9861 -0.0004 -0.1273 -0.1037 156 ASN   I ND2 
15956 N  N   . LEU   I  158 ? 1.5453 1.1817 1.9343 0.0328  -0.0968 -0.0371 157 LEU   I N   
15957 C  CA  . LEU   I  158 ? 1.5325 1.2148 1.9450 0.0371  -0.0891 -0.0551 157 LEU   I CA  
15958 C  C   . LEU   I  158 ? 1.5512 1.1464 1.9996 0.0941  -0.0677 -0.0924 157 LEU   I C   
15959 O  O   . LEU   I  158 ? 1.5981 1.1465 1.9759 0.0857  -0.0984 -0.1781 157 LEU   I O   
15960 C  CB  . LEU   I  158 ? 1.5302 1.1614 1.8902 0.0357  -0.0696 -0.0376 157 LEU   I CB  
15961 C  CG  . LEU   I  158 ? 1.5004 1.1608 1.8860 0.0430  -0.0888 -0.0308 157 LEU   I CG  
15962 C  CD1 . LEU   I  158 ? 1.4713 1.1742 1.8331 0.0718  -0.0567 -0.0312 157 LEU   I CD1 
15963 C  CD2 . LEU   I  158 ? 1.4653 1.1926 1.9342 0.0475  -0.0847 -0.0153 157 LEU   I CD2 
15964 N  N   . GLU   I  159 ? 1.5652 1.2060 2.0381 0.0153  -0.0447 0.0142  158 GLU   I N   
15965 C  CA  . GLU   I  159 ? 1.6414 1.1424 2.1488 0.0153  -0.0635 0.0393  158 GLU   I CA  
15966 C  C   . GLU   I  159 ? 1.6149 1.1042 2.0905 0.0633  -0.0159 0.0719  158 GLU   I C   
15967 O  O   . GLU   I  159 ? 1.6576 1.1441 2.1880 0.0265  -0.0281 0.0735  158 GLU   I O   
15968 C  CB  . GLU   I  159 ? 1.6780 1.1844 2.2130 0.0173  -0.0261 0.0843  158 GLU   I CB  
15969 C  CG  . GLU   I  159 ? 1.7229 1.1725 2.3055 0.0518  -0.0948 0.0948  158 GLU   I CG  
15970 C  CD  . GLU   I  159 ? 1.7492 1.1490 2.3273 0.1164  -0.1373 0.0998  158 GLU   I CD  
15971 O  OE1 . GLU   I  159 ? 1.7910 0.9783 2.4354 0.1932  -0.0521 0.0170  158 GLU   I OE1 
15972 O  OE2 . GLU   I  159 ? 1.7046 1.1825 2.3756 0.1030  -0.1782 0.0449  158 GLU   I OE2 
15973 N  N   . PRO   I  160 ? 1.6199 1.0704 2.0121 0.0278  0.0101  0.0527  159 PRO   I N   
15974 C  CA  . PRO   I  160 ? 1.6432 1.0739 1.8929 0.0189  0.0345  0.0692  159 PRO   I CA  
15975 C  C   . PRO   I  160 ? 1.6438 1.0026 1.8385 0.0569  0.0575  0.1222  159 PRO   I C   
15976 O  O   . PRO   I  160 ? 1.6442 0.8813 1.7281 0.0912  0.0333  0.1631  159 PRO   I O   
15977 C  CB  . PRO   I  160 ? 1.6427 1.0576 1.9075 0.0163  0.0498  0.0503  159 PRO   I CB  
15978 C  CG  . PRO   I  160 ? 1.6486 1.0539 1.9609 0.0122  0.0327  0.0358  159 PRO   I CG  
15979 C  CD  . PRO   I  160 ? 1.6251 1.0947 2.0149 0.0079  0.0040  0.0460  159 PRO   I CD  
15980 N  N   . GLU   I  161 ? 1.6331 0.9979 1.8976 0.0365  0.0894  0.1444  160 GLU   I N   
15981 C  CA  . GLU   I  161 ? 1.6566 1.0738 1.9411 0.0228  0.1395  0.0874  160 GLU   I CA  
15982 C  C   . GLU   I  161 ? 1.6153 1.0652 1.8897 0.0108  0.1409  0.0569  160 GLU   I C   
15983 O  O   . GLU   I  161 ? 1.6048 1.0711 1.8796 -0.0031 0.1548  0.0600  160 GLU   I O   
15984 C  CB  . GLU   I  161 ? 1.6929 1.1654 2.0672 0.0058  0.2025  0.0774  160 GLU   I CB  
15985 C  CG  . GLU   I  161 ? 1.7741 1.2057 2.1236 0.0024  0.2448  0.1166  160 GLU   I CG  
15986 C  CD  . GLU   I  161 ? 1.7975 1.2324 2.2339 -0.0396 0.2232  0.1077  160 GLU   I CD  
15987 O  OE1 . GLU   I  161 ? 1.8157 1.3051 2.2700 0.0534  0.1589  0.1634  160 GLU   I OE1 
15988 O  OE2 . GLU   I  161 ? 1.8918 1.2933 2.2794 -0.0899 0.2785  0.1339  160 GLU   I OE2 
15989 N  N   . ASP   I  162 ? 1.5814 0.9641 1.8854 -0.0138 0.1502  0.0439  161 ASP   I N   
15990 C  CA  . ASP   I  162 ? 1.5218 0.9074 1.9431 -0.0455 0.1618  0.0014  161 ASP   I CA  
15991 C  C   . ASP   I  162 ? 1.4853 0.8343 1.8997 -0.0518 0.1093  0.0364  161 ASP   I C   
15992 O  O   . ASP   I  162 ? 1.4400 0.9063 1.8809 -0.0687 0.0531  0.0122  161 ASP   I O   
15993 C  CB  . ASP   I  162 ? 1.5100 0.8911 1.9623 -0.0631 0.1569  -0.0214 161 ASP   I CB  
15994 C  CG  . ASP   I  162 ? 1.5305 0.9558 2.0136 -0.0708 0.1948  -0.0554 161 ASP   I CG  
15995 O  OD1 . ASP   I  162 ? 1.6015 1.0327 2.0322 -0.0962 0.2786  -0.0699 161 ASP   I OD1 
15996 O  OD2 . ASP   I  162 ? 1.4988 1.0056 2.0083 -0.0516 0.2007  -0.0836 161 ASP   I OD2 
15997 N  N   . LEU   I  163 ? 1.4319 0.8179 1.9004 -0.1003 0.1148  0.0286  162 LEU   I N   
15998 C  CA  . LEU   I  163 ? 1.4413 0.8378 1.8553 -0.1168 0.1168  0.0124  162 LEU   I CA  
15999 C  C   . LEU   I  163 ? 1.4573 0.8254 1.8013 -0.1317 0.1385  0.0039  162 LEU   I C   
16000 O  O   . LEU   I  163 ? 1.4295 0.8035 1.7804 -0.1195 0.1229  -0.0282 162 LEU   I O   
16001 C  CB  . LEU   I  163 ? 1.4221 0.8703 1.8616 -0.0836 0.1323  -0.0092 162 LEU   I CB  
16002 C  CG  . LEU   I  163 ? 1.4078 0.8818 1.8263 -0.0756 0.1109  -0.0043 162 LEU   I CG  
16003 C  CD1 . LEU   I  163 ? 1.3809 0.8701 1.8136 -0.0658 0.1031  -0.0111 162 LEU   I CD1 
16004 C  CD2 . LEU   I  163 ? 1.3999 0.8971 1.8273 -0.0479 0.1115  -0.0158 162 LEU   I CD2 
16005 N  N   . PHE   I  164 ? 1.4840 0.8755 1.7890 -0.1328 0.1353  0.0025  163 PHE   I N   
16006 C  CA  . PHE   I  164 ? 1.4830 0.9024 1.7652 -0.1199 0.1496  -0.0019 163 PHE   I CA  
16007 C  C   . PHE   I  164 ? 1.4897 0.8925 1.7797 -0.1478 0.1716  0.0373  163 PHE   I C   
16008 O  O   . PHE   I  164 ? 1.4711 0.8852 1.7808 -0.1393 0.1815  0.0737  163 PHE   I O   
16009 C  CB  . PHE   I  164 ? 1.4934 0.9030 1.7403 -0.1151 0.1668  -0.0336 163 PHE   I CB  
16010 C  CG  . PHE   I  164 ? 1.5242 0.9421 1.7322 -0.0965 0.1763  -0.0796 163 PHE   I CG  
16011 C  CD1 . PHE   I  164 ? 1.5272 0.9117 1.6544 -0.0965 0.1636  -0.1155 163 PHE   I CD1 
16012 C  CD2 . PHE   I  164 ? 1.5701 1.0509 1.7218 -0.1016 0.1849  -0.1254 163 PHE   I CD2 
16013 C  CE1 . PHE   I  164 ? 1.5525 0.9648 1.6475 -0.0856 0.1694  -0.1426 163 PHE   I CE1 
16014 C  CE2 . PHE   I  164 ? 1.5892 1.1271 1.7165 -0.0874 0.1877  -0.1512 163 PHE   I CE2 
16015 C  CZ  . PHE   I  164 ? 1.5908 1.0592 1.6784 -0.0735 0.2053  -0.1723 163 PHE   I CZ  
16016 N  N   . GLU   I  165 ? 1.5338 0.9071 1.8327 -0.1168 0.1982  0.0647  164 GLU   I N   
16017 C  CA  . GLU   I  165 ? 1.6009 0.9266 1.8630 -0.1358 0.2015  0.0164  164 GLU   I CA  
16018 C  C   . GLU   I  165 ? 1.5534 0.8698 1.8310 -0.1494 0.1510  -0.0078 164 GLU   I C   
16019 O  O   . GLU   I  165 ? 1.6038 0.8853 1.8686 -0.1502 0.1160  -0.0458 164 GLU   I O   
16020 C  CB  . GLU   I  165 ? 1.6349 0.9589 1.9030 -0.1085 0.2567  0.0170  164 GLU   I CB  
16021 C  CG  . GLU   I  165 ? 1.7184 0.9914 1.9358 -0.1109 0.3032  0.0310  164 GLU   I CG  
16022 C  CD  . GLU   I  165 ? 1.7996 1.0242 1.9138 -0.1206 0.3231  0.0329  164 GLU   I CD  
16023 O  OE1 . GLU   I  165 ? 1.8216 0.9921 1.9752 -0.1764 0.3356  0.0334  164 GLU   I OE1 
16024 O  OE2 . GLU   I  165 ? 1.8346 1.1086 1.9933 -0.1906 0.3164  0.0778  164 GLU   I OE2 
16025 N  N   . THR   I  166 ? 1.4964 0.7896 1.8436 -0.1728 0.1272  -0.0129 165 THR   I N   
16026 C  CA  . THR   I  166 ? 1.4409 0.7300 1.7754 -0.1729 0.0720  -0.0442 165 THR   I CA  
16027 C  C   . THR   I  166 ? 1.4677 0.7210 1.7370 -0.0833 0.0870  -0.0590 165 THR   I C   
16028 O  O   . THR   I  166 ? 1.4845 0.6609 1.7925 -0.0503 0.0588  -0.0507 165 THR   I O   
16029 C  CB  . THR   I  166 ? 1.3942 0.6846 1.7792 -0.2260 0.0678  -0.0125 165 THR   I CB  
16030 O  OG1 . THR   I  166 ? 1.3827 0.6463 1.7787 -0.2403 0.0246  -0.0056 165 THR   I OG1 
16031 C  CG2 . THR   I  166 ? 1.3661 0.6768 1.7477 -0.2478 0.0390  -0.0329 165 THR   I CG2 
16032 N  N   . ILE   I  167 ? 1.4608 0.7598 1.6698 -0.0332 0.0860  -0.0770 166 ILE   I N   
16033 C  CA  . ILE   I  167 ? 1.4692 0.7487 1.5844 -0.0077 0.0425  -0.0936 166 ILE   I CA  
16034 C  C   . ILE   I  167 ? 1.4727 0.8136 1.5467 0.0485  0.0533  -0.1181 166 ILE   I C   
16035 O  O   . ILE   I  167 ? 1.4270 0.8027 1.4973 0.1071  0.0724  -0.2063 166 ILE   I O   
16036 C  CB  . ILE   I  167 ? 1.4636 0.7302 1.5142 -0.0390 0.0087  -0.0961 166 ILE   I CB  
16037 C  CG1 . ILE   I  167 ? 1.4492 0.6488 1.4723 -0.0527 -0.0209 -0.1233 166 ILE   I CG1 
16038 C  CG2 . ILE   I  167 ? 1.5034 0.6960 1.5048 -0.0197 0.0170  -0.1083 166 ILE   I CG2 
16039 C  CD1 . ILE   I  167 ? 1.4511 0.6653 1.4546 -0.0503 -0.0233 -0.1319 166 ILE   I CD1 
16040 N  N   . SER   I  168 ? 1.5183 0.8739 1.5690 0.0876  0.0822  -0.0761 167 SER   I N   
16041 C  CA  . SER   I  168 ? 1.5693 0.9676 1.5753 0.1040  0.0345  -0.0581 167 SER   I CA  
16042 C  C   . SER   I  168 ? 1.6090 0.9750 1.6556 0.0970  0.0435  -0.0424 167 SER   I C   
16043 O  O   . SER   I  168 ? 1.6341 1.0952 1.7166 0.0708  0.0305  -0.1188 167 SER   I O   
16044 C  CB  . SER   I  168 ? 1.5890 1.0400 1.5707 0.1326  0.0425  -0.0485 167 SER   I CB  
16045 O  OG  . SER   I  168 ? 1.5667 1.0423 1.5120 0.1358  0.0264  -0.0404 167 SER   I OG  
16046 N  N   . GLN   I  169 ? 1.6434 0.9601 1.6951 0.1150  0.0581  0.0008  168 GLN   I N   
16047 C  CA  . GLN   I  169 ? 1.7139 0.9620 1.7036 0.1007  0.0718  0.0235  168 GLN   I CA  
16048 C  C   . GLN   I  169 ? 1.5662 0.8967 1.6671 0.1206  -0.0108 0.0349  168 GLN   I C   
16049 O  O   . GLN   I  169 ? 1.5014 0.9758 1.6646 0.0698  -0.0431 -0.0151 168 GLN   I O   
16050 C  CB  . GLN   I  169 ? 1.7275 0.9505 1.7788 0.1091  0.1408  0.0528  168 GLN   I CB  
16051 C  CG  . GLN   I  169 ? 1.8574 0.9518 1.8330 0.0943  0.2293  0.0730  168 GLN   I CG  
16052 C  CD  . GLN   I  169 ? 1.9078 0.9935 1.8125 0.1369  0.2484  0.0445  168 GLN   I CD  
16053 O  OE1 . GLN   I  169 ? 1.9423 1.0336 1.9641 0.1082  0.2802  0.0820  168 GLN   I OE1 
16054 N  NE2 . GLN   I  169 ? 1.9296 0.9094 1.8608 0.1320  0.2717  0.0871  168 GLN   I NE2 
16055 N  N   . ALA   I  170 ? 1.4863 0.8942 1.6236 0.1352  -0.0357 0.0621  169 ALA   I N   
16056 C  CA  . ALA   I  170 ? 1.4030 0.9106 1.6410 0.1426  -0.0604 0.0381  169 ALA   I CA  
16057 C  C   . ALA   I  170 ? 1.4217 0.9028 1.6347 0.1423  -0.0883 -0.0088 169 ALA   I C   
16058 O  O   . ALA   I  170 ? 1.4118 0.9117 1.6321 0.1295  -0.1448 0.0056  169 ALA   I O   
16059 C  CB  . ALA   I  170 ? 1.3968 0.8810 1.6221 0.1631  -0.0453 0.0570  169 ALA   I CB  
16060 N  N   . LEU   I  171 ? 1.4935 0.8623 1.6239 0.1412  -0.0535 -0.0314 170 LEU   I N   
16061 C  CA  . LEU   I  171 ? 1.4983 0.8928 1.6511 0.1375  -0.0720 -0.1210 170 LEU   I CA  
16062 C  C   . LEU   I  171 ? 1.5002 0.8561 1.6726 0.1283  -0.0122 -0.1311 170 LEU   I C   
16063 O  O   . LEU   I  171 ? 1.4671 0.7569 1.7135 0.1670  -0.0616 -0.1832 170 LEU   I O   
16064 C  CB  . LEU   I  171 ? 1.5551 0.8908 1.6362 0.1511  -0.0911 -0.1324 170 LEU   I CB  
16065 C  CG  . LEU   I  171 ? 1.5915 0.9130 1.5663 0.1547  -0.1415 -0.1701 170 LEU   I CG  
16066 C  CD1 . LEU   I  171 ? 1.5922 0.9145 1.5895 0.1836  -0.1564 -0.1422 170 LEU   I CD1 
16067 C  CD2 . LEU   I  171 ? 1.6184 0.9714 1.5575 0.1604  -0.1286 -0.1822 170 LEU   I CD2 
16068 N  N   . LEU   I  172 ? 1.5462 0.9045 1.6683 0.0847  0.0232  -0.1333 171 LEU   I N   
16069 C  CA  . LEU   I  172 ? 1.5602 1.0132 1.6172 0.0716  0.0272  -0.1389 171 LEU   I CA  
16070 C  C   . LEU   I  172 ? 1.5929 1.0187 1.6144 0.0902  -0.0161 -0.1112 171 LEU   I C   
16071 O  O   . LEU   I  172 ? 1.5888 0.9969 1.5967 0.1576  -0.0714 -0.1253 171 LEU   I O   
16072 C  CB  . LEU   I  172 ? 1.5752 1.0612 1.6968 0.0415  0.0676  -0.1325 171 LEU   I CB  
16073 C  CG  . LEU   I  172 ? 1.5553 1.0099 1.7028 0.0472  0.1058  -0.1434 171 LEU   I CG  
16074 C  CD1 . LEU   I  172 ? 1.5465 0.9683 1.6805 0.0280  0.1012  -0.1141 171 LEU   I CD1 
16075 C  CD2 . LEU   I  172 ? 1.5872 1.0120 1.7306 0.0234  0.1397  -0.1214 171 LEU   I CD2 
16076 N  N   . ASN   I  173 ? 1.6164 1.0498 1.6172 0.1077  -0.0178 -0.1026 172 ASN   I N   
16077 C  CA  . ASN   I  173 ? 1.5833 1.0385 1.5833 0.1169  -0.0205 -0.1192 172 ASN   I CA  
16078 C  C   . ASN   I  173 ? 1.5993 1.0293 1.5849 0.0815  -0.0127 -0.1166 172 ASN   I C   
16079 O  O   . ASN   I  173 ? 1.5855 1.1197 1.5910 0.0044  -0.0030 -0.1190 172 ASN   I O   
16080 C  CB  . ASN   I  173 ? 1.5754 1.0126 1.5855 0.1650  0.0161  -0.1229 172 ASN   I CB  
16081 C  CG  . ASN   I  173 ? 1.6249 0.9751 1.5653 0.2179  0.0267  -0.1535 172 ASN   I CG  
16082 O  OD1 . ASN   I  173 ? 1.6556 1.0139 1.5793 0.2775  0.0060  -0.1816 172 ASN   I OD1 
16083 N  ND2 . ASN   I  173 ? 1.6557 0.9798 1.5418 0.2072  0.0705  -0.1303 172 ASN   I ND2 
16084 N  N   . ALA   I  174 ? 1.5635 0.9638 1.6201 0.0770  -0.0114 -0.0835 173 ALA   I N   
16085 C  CA  . ALA   I  174 ? 1.5178 0.9138 1.6567 0.0849  -0.0382 -0.1145 173 ALA   I CA  
16086 C  C   . ALA   I  174 ? 1.5773 0.8893 1.6361 0.1055  -0.0705 -0.1830 173 ALA   I C   
16087 O  O   . ALA   I  174 ? 1.6246 0.6757 1.6190 0.1461  -0.1103 -0.2141 173 ALA   I O   
16088 C  CB  . ALA   I  174 ? 1.4805 0.9273 1.6254 0.0639  -0.0605 -0.1060 173 ALA   I CB  
16089 N  N   . ALA   I  175 ? 1.6031 0.9144 1.6145 0.0486  0.0121  -0.1939 174 ALA   I N   
16090 C  CA  . ALA   I  175 ? 1.5834 0.9042 1.6265 0.0652  0.0234  -0.2326 174 ALA   I CA  
16091 C  C   . ALA   I  175 ? 1.6505 0.8870 1.7218 0.0821  0.0688  -0.2772 174 ALA   I C   
16092 O  O   . ALA   I  175 ? 1.7228 0.6869 1.7810 0.0391  -0.0133 -0.3534 174 ALA   I O   
16093 C  CB  . ALA   I  175 ? 1.5682 0.9234 1.6025 0.0745  0.0564  -0.2351 174 ALA   I CB  
16094 N  N   . ASP   I  176 ? 1.6784 0.8812 1.6658 0.0648  0.1293  -0.3523 175 ASP   I N   
16095 C  CA  . ASP   I  176 ? 1.7375 0.9569 1.6715 0.0717  0.1226  -0.4100 175 ASP   I CA  
16096 C  C   . ASP   I  176 ? 1.7175 0.9306 1.6845 0.0941  0.1235  -0.4189 175 ASP   I C   
16097 O  O   . ASP   I  176 ? 1.7619 1.0156 1.8401 0.0665  0.1128  -0.5104 175 ASP   I O   
16098 C  CB  . ASP   I  176 ? 1.7510 1.0349 1.6833 0.0242  0.1650  -0.3991 175 ASP   I CB  
16099 C  CG  . ASP   I  176 ? 1.8255 1.0353 1.6476 0.0276  0.1483  -0.4037 175 ASP   I CG  
16100 O  OD1 . ASP   I  176 ? 1.8983 0.8024 1.5678 -0.0597 0.1325  -0.4305 175 ASP   I OD1 
16101 O  OD2 . ASP   I  176 ? 1.8787 1.2253 1.6130 -0.0198 0.2131  -0.4541 175 ASP   I OD2 
16102 N  N   . ARG   I  177 ? 1.6570 0.8776 1.6773 0.0958  0.0499  -0.4279 176 ARG   I N   
16103 C  CA  . ARG   I  177 ? 1.6028 0.9199 1.6572 0.1130  -0.0060 -0.3758 176 ARG   I CA  
16104 C  C   . ARG   I  177 ? 1.5818 0.9289 1.7150 0.1465  -0.0681 -0.3524 176 ARG   I C   
16105 O  O   . ARG   I  177 ? 1.6241 1.1060 1.7155 0.1442  -0.0001 -0.3633 176 ARG   I O   
16106 C  CB  . ARG   I  177 ? 1.5815 0.9078 1.6901 0.1295  -0.0167 -0.3518 176 ARG   I CB  
16107 C  CG  . ARG   I  177 ? 1.5723 0.9845 1.6787 0.1700  -0.0273 -0.3313 176 ARG   I CG  
16108 C  CD  . ARG   I  177 ? 1.5884 0.9728 1.6818 0.1896  -0.0163 -0.3325 176 ARG   I CD  
16109 N  NE  . ARG   I  177 ? 1.6007 1.0141 1.6545 0.2139  0.0149  -0.3058 176 ARG   I NE  
16110 C  CZ  . ARG   I  177 ? 1.6245 1.0061 1.6389 0.2454  0.0351  -0.3048 176 ARG   I CZ  
16111 N  NH1 . ARG   I  177 ? 1.5991 1.0355 1.6671 0.2693  0.0056  -0.2656 176 ARG   I NH1 
16112 N  NH2 . ARG   I  177 ? 1.6244 1.1220 1.6394 0.2479  0.0975  -0.3131 176 ARG   I NH2 
16113 N  N   . ASP   I  178 ? 1.5424 0.9243 1.7179 0.0730  -0.0712 -0.2932 177 ASP   I N   
16114 C  CA  . ASP   I  178 ? 1.5399 0.8454 1.7123 0.0793  -0.1272 -0.2861 177 ASP   I CA  
16115 C  C   . ASP   I  178 ? 1.5092 0.7562 1.7434 0.0948  -0.1596 -0.3194 177 ASP   I C   
16116 O  O   . ASP   I  178 ? 1.3949 0.6488 1.7069 0.1438  -0.1954 -0.3396 177 ASP   I O   
16117 C  CB  . ASP   I  178 ? 1.5486 0.8198 1.6905 0.0128  -0.1026 -0.2507 177 ASP   I CB  
16118 C  CG  . ASP   I  178 ? 1.5571 0.8295 1.6677 0.0148  -0.0987 -0.2278 177 ASP   I CG  
16119 O  OD1 . ASP   I  178 ? 1.5119 0.9978 1.7678 -0.0232 -0.0824 -0.2538 177 ASP   I OD1 
16120 O  OD2 . ASP   I  178 ? 1.5207 0.7724 1.5476 -0.0644 -0.0814 -0.0913 177 ASP   I OD2 
16121 N  N   . ALA   I  179 ? 1.5172 0.6974 1.7626 0.1072  -0.2389 -0.3180 178 ALA   I N   
16122 C  CA  . ALA   I  179 ? 1.5841 0.7213 1.7569 0.1230  -0.2579 -0.2678 178 ALA   I CA  
16123 C  C   . ALA   I  179 ? 1.6047 0.6972 1.6723 0.0670  -0.2676 -0.2584 178 ALA   I C   
16124 O  O   . ALA   I  179 ? 1.6307 0.6080 1.6738 0.0188  -0.3022 -0.2731 178 ALA   I O   
16125 C  CB  . ALA   I  179 ? 1.5705 0.7402 1.8034 0.1319  -0.2650 -0.2377 178 ALA   I CB  
16126 N  N   . LEU   I  180 ? 1.5542 0.6957 1.5582 0.0605  -0.2592 -0.1876 179 LEU   I N   
16127 C  CA  . LEU   I  180 ? 1.5424 0.7160 1.4128 0.0797  -0.2593 -0.1513 179 LEU   I CA  
16128 C  C   . LEU   I  180 ? 1.4857 0.7045 1.3402 0.1233  -0.2531 -0.1251 179 LEU   I C   
16129 O  O   . LEU   I  180 ? 1.4812 0.7090 1.2579 0.0850  -0.2579 -0.0854 179 LEU   I O   
16130 C  CB  . LEU   I  180 ? 1.5667 0.6565 1.3905 0.0383  -0.2495 -0.1239 179 LEU   I CB  
16131 C  CG  . LEU   I  180 ? 1.5968 0.7111 1.4324 -0.0034 -0.2657 -0.1290 179 LEU   I CG  
16132 C  CD1 . LEU   I  180 ? 1.6091 0.6884 1.4832 0.0143  -0.2506 -0.1380 179 LEU   I CD1 
16133 C  CD2 . LEU   I  180 ? 1.6323 0.7512 1.4272 0.0086  -0.2833 -0.1082 179 LEU   I CD2 
16134 N  N   . SER   I  181 ? 1.4791 0.8024 1.3813 0.1476  -0.2062 -0.1185 180 SER   I N   
16135 C  CA  . SER   I  181 ? 1.5113 0.7958 1.3579 0.1510  -0.1398 -0.0743 180 SER   I CA  
16136 C  C   . SER   I  181 ? 1.5651 0.9173 1.3501 0.1520  -0.1190 -0.0484 180 SER   I C   
16137 O  O   . SER   I  181 ? 1.5687 0.9977 1.2407 0.0294  -0.1081 -0.0787 180 SER   I O   
16138 C  CB  . SER   I  181 ? 1.5164 0.8247 1.3569 0.1383  -0.1396 -0.1290 180 SER   I CB  
16139 O  OG  . SER   I  181 ? 1.5142 0.7756 1.4009 0.1658  -0.1604 -0.2013 180 SER   I OG  
16140 N  N   . GLY   I  182 ? 1.5724 0.9116 1.3913 0.1677  -0.0847 -0.0554 181 GLY   I N   
16141 C  CA  . GLY   I  182 ? 1.5817 1.0540 1.4691 0.1719  -0.0423 -0.1340 181 GLY   I CA  
16142 C  C   . GLY   I  182 ? 1.5568 1.1313 1.4709 0.1697  -0.0692 -0.1283 181 GLY   I C   
16143 O  O   . GLY   I  182 ? 1.4624 1.1484 1.4345 0.1389  -0.0467 -0.1883 181 GLY   I O   
16144 N  N   . TRP   I  183 ? 1.5737 1.2384 1.5421 0.1584  -0.0800 -0.2153 182 TRP   I N   
16145 C  CA  . TRP   I  183 ? 1.6183 1.1509 1.5792 0.1526  -0.1047 -0.2227 182 TRP   I CA  
16146 C  C   . TRP   I  183 ? 1.6148 1.0913 1.5959 0.2101  -0.0939 -0.1838 182 TRP   I C   
16147 O  O   . TRP   I  183 ? 1.5023 1.0539 1.6635 0.2846  -0.0867 -0.2597 182 TRP   I O   
16148 C  CB  . TRP   I  183 ? 1.6113 1.0393 1.5806 0.1164  -0.1592 -0.2837 182 TRP   I CB  
16149 C  CG  . TRP   I  183 ? 1.7404 1.0193 1.6156 0.0996  -0.1510 -0.3549 182 TRP   I CG  
16150 C  CD1 . TRP   I  183 ? 1.7802 1.1049 1.6116 0.0946  -0.1384 -0.4977 182 TRP   I CD1 
16151 C  CD2 . TRP   I  183 ? 1.8000 0.8750 1.5210 0.0564  -0.2046 -0.3560 182 TRP   I CD2 
16152 N  NE1 . TRP   I  183 ? 1.8240 1.1787 1.5815 0.1483  -0.1913 -0.4956 182 TRP   I NE1 
16153 C  CE2 . TRP   I  183 ? 1.8655 1.0184 1.4997 0.0896  -0.2185 -0.4720 182 TRP   I CE2 
16154 C  CE3 . TRP   I  183 ? 1.7927 0.8119 1.4672 0.0048  -0.1942 -0.3284 182 TRP   I CE3 
16155 C  CZ2 . TRP   I  183 ? 1.8787 1.0157 1.5082 0.1210  -0.2341 -0.4429 182 TRP   I CZ2 
16156 C  CZ3 . TRP   I  183 ? 1.8128 0.8535 1.4485 -0.0061 -0.2028 -0.3707 182 TRP   I CZ3 
16157 C  CH2 . TRP   I  183 ? 1.8779 0.8987 1.4595 0.0367  -0.2307 -0.4262 182 TRP   I CH2 
16158 N  N   . GLY   I  184 ? 1.6201 1.0765 1.6189 0.1340  -0.0983 -0.1875 183 GLY   I N   
16159 C  CA  . GLY   I  184 ? 1.6944 1.0334 1.6373 0.1324  -0.0828 -0.1494 183 GLY   I CA  
16160 C  C   . GLY   I  184 ? 1.6813 0.9413 1.6534 0.0861  -0.1024 -0.1172 183 GLY   I C   
16161 O  O   . GLY   I  184 ? 1.6823 1.0346 1.7265 0.0312  -0.0667 -0.1124 183 GLY   I O   
16162 N  N   . ALA   I  185 ? 1.7074 0.8681 1.6627 0.0961  -0.1038 -0.0858 184 ALA   I N   
16163 C  CA  . ALA   I  185 ? 1.7029 0.8199 1.6625 0.0480  -0.0902 -0.0740 184 ALA   I CA  
16164 C  C   . ALA   I  185 ? 1.7200 0.8088 1.5876 0.0681  -0.0916 -0.0346 184 ALA   I C   
16165 O  O   . ALA   I  185 ? 1.7112 0.7819 1.6214 0.0714  -0.0631 0.0282  184 ALA   I O   
16166 C  CB  . ALA   I  185 ? 1.6848 0.7924 1.6938 0.0456  -0.0826 -0.0916 184 ALA   I CB  
16167 N  N   . VAL   I  186 ? 1.7291 0.7678 1.5957 0.0459  -0.1096 -0.0185 185 VAL   I N   
16168 C  CA  . VAL   I  186 ? 1.7114 0.7903 1.5558 0.0301  -0.1111 -0.0193 185 VAL   I CA  
16169 C  C   . VAL   I  186 ? 1.6540 0.7288 1.5637 -0.0288 -0.0937 -0.0712 185 VAL   I C   
16170 O  O   . VAL   I  186 ? 1.6549 0.6374 1.4835 -0.0465 -0.1301 -0.1618 185 VAL   I O   
16171 C  CB  . VAL   I  186 ? 1.7317 0.7596 1.5118 0.0142  -0.1336 0.0047  185 VAL   I CB  
16172 C  CG1 . VAL   I  186 ? 1.7225 0.7831 1.4555 -0.0036 -0.1417 0.0011  185 VAL   I CG1 
16173 C  CG2 . VAL   I  186 ? 1.7869 0.8442 1.5066 0.0515  -0.1384 0.0156  185 VAL   I CG2 
16174 N  N   . VAL   I  187 ? 1.6412 0.7655 1.5660 -0.0090 -0.0669 -0.0603 186 VAL   I N   
16175 C  CA  . VAL   I  187 ? 1.6159 0.7883 1.5575 0.0344  -0.0672 -0.0346 186 VAL   I CA  
16176 C  C   . VAL   I  187 ? 1.6076 0.7897 1.5304 0.0353  -0.0470 -0.0313 186 VAL   I C   
16177 O  O   . VAL   I  187 ? 1.6185 0.8341 1.5405 0.0219  -0.0042 -0.0523 186 VAL   I O   
16178 C  CB  . VAL   I  187 ? 1.6282 0.7800 1.6056 0.0385  -0.0574 -0.0231 186 VAL   I CB  
16179 C  CG1 . VAL   I  187 ? 1.6192 0.8037 1.6209 0.0415  -0.0672 -0.0197 186 VAL   I CG1 
16180 C  CG2 . VAL   I  187 ? 1.6340 0.7946 1.6232 0.0119  -0.0629 -0.0431 186 VAL   I CG2 
16181 N  N   . TYR   I  188 ? 1.5834 0.7929 1.5169 0.0330  -0.0761 -0.0254 187 TYR   I N   
16182 C  CA  . TYR   I  188 ? 1.5690 0.7968 1.5290 0.0254  -0.0638 -0.0214 187 TYR   I CA  
16183 C  C   . TYR   I  188 ? 1.5677 0.7973 1.5248 0.0302  -0.0569 0.0380  187 TYR   I C   
16184 O  O   . TYR   I  188 ? 1.5194 0.7264 1.5227 0.0391  -0.1232 0.0453  187 TYR   I O   
16185 C  CB  . TYR   I  188 ? 1.5845 0.7359 1.4868 0.0118  -0.1084 -0.0556 187 TYR   I CB  
16186 C  CG  . TYR   I  188 ? 1.6473 0.6437 1.4353 0.0005  -0.1386 -0.0724 187 TYR   I CG  
16187 C  CD1 . TYR   I  188 ? 1.6346 0.6701 1.4020 0.0185  -0.1834 -0.1224 187 TYR   I CD1 
16188 C  CD2 . TYR   I  188 ? 1.6207 0.6594 1.4090 0.0120  -0.1483 -0.0549 187 TYR   I CD2 
16189 C  CE1 . TYR   I  188 ? 1.6407 0.5790 1.4225 0.0553  -0.1545 -0.0850 187 TYR   I CE1 
16190 C  CE2 . TYR   I  188 ? 1.6330 0.6061 1.3996 0.0345  -0.1293 -0.0329 187 TYR   I CE2 
16191 C  CZ  . TYR   I  188 ? 1.6015 0.5942 1.4141 0.0751  -0.1621 -0.0647 187 TYR   I CZ  
16192 O  OH  . TYR   I  188 ? 1.6149 0.5918 1.4521 0.1268  -0.1421 -0.0131 187 TYR   I OH  
16193 N  N   . ILE   I  189 ? 1.5854 0.8816 1.5923 0.0495  -0.0020 0.0464  188 ILE   I N   
16194 C  CA  . ILE   I  189 ? 1.5647 0.8739 1.6373 0.0664  -0.0003 0.0487  188 ILE   I CA  
16195 C  C   . ILE   I  189 ? 1.5682 0.8670 1.6705 0.0919  0.0370  0.0460  188 ILE   I C   
16196 O  O   . ILE   I  189 ? 1.5986 0.8357 1.6380 0.1181  0.0762  0.0120  188 ILE   I O   
16197 C  CB  . ILE   I  189 ? 1.6242 0.9319 1.7099 0.0765  0.0648  0.0459  188 ILE   I CB  
16198 C  CG1 . ILE   I  189 ? 1.6467 0.9668 1.7007 0.0493  0.0739  -0.0156 188 ILE   I CG1 
16199 C  CG2 . ILE   I  189 ? 1.6199 0.9631 1.7600 0.0661  0.0606  0.0660  188 ILE   I CG2 
16200 C  CD1 . ILE   I  189 ? 1.6380 1.0002 1.6867 -0.0088 0.0865  -0.0257 188 ILE   I CD1 
16201 N  N   . ILE   I  190 ? 1.5568 0.7837 1.6671 0.0684  0.0402  0.0725  189 ILE   I N   
16202 C  CA  . ILE   I  190 ? 1.5921 0.7796 1.6823 0.0234  0.0722  0.0695  189 ILE   I CA  
16203 C  C   . ILE   I  190 ? 1.6459 0.8034 1.6904 -0.0319 0.0527  0.0627  189 ILE   I C   
16204 O  O   . ILE   I  190 ? 1.7100 0.6897 1.5971 -0.0990 0.0837  -0.0004 189 ILE   I O   
16205 C  CB  . ILE   I  190 ? 1.5947 0.7093 1.6229 0.0132  0.0610  0.0803  189 ILE   I CB  
16206 C  CG1 . ILE   I  190 ? 1.5901 0.6273 1.5944 0.0230  0.0749  0.0934  189 ILE   I CG1 
16207 C  CG2 . ILE   I  190 ? 1.5887 0.7468 1.6250 0.0059  0.0545  0.0301  189 ILE   I CG2 
16208 C  CD1 . ILE   I  190 ? 1.5749 0.5748 1.5510 0.0415  0.0499  0.0942  189 ILE   I CD1 
16209 N  N   . LYS   I  191 ? 1.7302 0.9241 1.7871 -0.0814 0.1543  0.1093  190 LYS   I N   
16210 C  CA  . LYS   I  191 ? 1.7206 0.9551 1.8446 -0.1518 0.2018  0.1485  190 LYS   I CA  
16211 C  C   . LYS   I  191 ? 1.7408 0.9477 1.8881 -0.1810 0.1836  0.1206  190 LYS   I C   
16212 O  O   . LYS   I  191 ? 1.6534 0.8737 1.8673 -0.2632 0.2326  0.1415  190 LYS   I O   
16213 C  CB  . LYS   I  191 ? 1.7932 0.9847 1.9029 -0.1108 0.2736  0.2010  190 LYS   I CB  
16214 C  CG  . LYS   I  191 ? 1.7889 0.9788 1.8892 -0.0749 0.3501  0.2471  190 LYS   I CG  
16215 C  CD  . LYS   I  191 ? 1.8299 1.0209 1.9474 -0.0499 0.4046  0.2490  190 LYS   I CD  
16216 C  CE  . LYS   I  191 ? 1.8358 1.0803 1.9891 -0.0772 0.4078  0.2244  190 LYS   I CE  
16217 N  NZ  . LYS   I  191 ? 1.8890 1.1936 2.0445 -0.0664 0.4553  0.2024  190 LYS   I NZ  
16218 N  N   . LYS   I  192 ? 1.8582 1.0385 1.9963 -0.2039 0.1156  0.0472  191 LYS   I N   
16219 C  CA  . LYS   I  192 ? 1.9355 1.0774 2.0919 -0.1919 0.0912  -0.0083 191 LYS   I CA  
16220 C  C   . LYS   I  192 ? 1.9121 1.0814 2.0336 -0.2521 0.1295  0.0059  191 LYS   I C   
16221 O  O   . LYS   I  192 ? 1.8664 1.1176 1.9939 -0.3279 0.2358  -0.0336 191 LYS   I O   
16222 C  CB  . LYS   I  192 ? 1.9486 1.1556 2.2276 -0.1260 -0.0335 0.0123  191 LYS   I CB  
16223 C  CG  . LYS   I  192 ? 1.9428 1.2605 2.2750 -0.0144 -0.1298 -0.0556 191 LYS   I CG  
16224 C  CD  . LYS   I  192 ? 1.8783 1.2875 2.4170 -0.0067 -0.1667 -0.0742 191 LYS   I CD  
16225 C  CE  . LYS   I  192 ? 1.8584 1.3431 2.4919 0.0921  -0.2032 -0.1147 191 LYS   I CE  
16226 N  NZ  . LYS   I  192 ? 1.8676 1.3927 2.4554 0.1153  -0.1917 -0.1588 191 LYS   I NZ  
16227 N  N   . ASP   I  193 ? 1.9685 1.1525 2.0428 -0.3549 0.1444  0.0119  192 ASP   I N   
16228 C  CA  . ASP   I  193 ? 1.9189 1.2057 2.1375 -0.3276 0.1252  0.0520  192 ASP   I CA  
16229 C  C   . ASP   I  193 ? 1.8551 1.2562 2.1323 -0.3082 0.1253  0.0609  192 ASP   I C   
16230 O  O   . ASP   I  193 ? 1.8502 1.3136 2.2139 -0.4007 0.1270  0.0915  192 ASP   I O   
16231 C  CB  . ASP   I  193 ? 1.9666 1.1745 2.2591 -0.3159 0.1931  0.0533  192 ASP   I CB  
16232 C  CG  . ASP   I  193 ? 1.9616 1.1269 2.3595 -0.3783 0.1850  -0.0042 192 ASP   I CG  
16233 O  OD1 . ASP   I  193 ? 1.9695 1.4367 2.5194 -0.2070 0.2723  -0.0131 192 ASP   I OD1 
16234 O  OD2 . ASP   I  193 ? 1.9161 0.7377 2.5819 -0.3916 0.2888  0.0882  192 ASP   I OD2 
16235 N  N   . GLU   I  194 ? 1.7556 1.1894 2.1004 -0.2000 0.1107  0.1455  193 GLU   I N   
16236 C  CA  . GLU   I  194 ? 1.6246 1.1225 2.0668 -0.1269 0.1267  0.1718  193 GLU   I CA  
16237 C  C   . GLU   I  194 ? 1.5426 1.0960 1.9676 -0.0952 0.0631  0.1582  193 GLU   I C   
16238 O  O   . GLU   I  194 ? 1.3782 1.1504 1.9292 -0.1296 0.0065  0.1328  193 GLU   I O   
16239 C  CB  . GLU   I  194 ? 1.6776 1.1555 2.1332 -0.0766 0.1861  0.2061  193 GLU   I CB  
16240 C  CG  . GLU   I  194 ? 1.6847 1.1941 2.1386 -0.0310 0.2484  0.2138  193 GLU   I CG  
16241 C  CD  . GLU   I  194 ? 1.6788 1.2568 2.1771 0.0325  0.2862  0.2590  193 GLU   I CD  
16242 O  OE1 . GLU   I  194 ? 1.7027 1.2473 2.1147 0.0252  0.3889  0.3070  193 GLU   I OE1 
16243 O  OE2 . GLU   I  194 ? 1.7012 1.3751 2.2613 0.1185  0.3282  0.2265  193 GLU   I OE2 
16244 N  N   . VAL   I  195 ? 1.5413 1.0352 1.9132 -0.0863 0.0868  0.1606  194 VAL   I N   
16245 C  CA  . VAL   I  195 ? 1.5251 0.9741 1.7805 -0.0469 0.1158  0.1102  194 VAL   I CA  
16246 C  C   . VAL   I  195 ? 1.5142 0.9201 1.7811 -0.0497 0.1306  0.1082  194 VAL   I C   
16247 O  O   . VAL   I  195 ? 1.4843 0.8561 1.7041 -0.0940 0.1387  0.0520  194 VAL   I O   
16248 C  CB  . VAL   I  195 ? 1.5243 0.9500 1.7028 -0.0423 0.1067  0.1208  194 VAL   I CB  
16249 C  CG1 . VAL   I  195 ? 1.5177 0.9705 1.6463 -0.0510 0.0805  0.0855  194 VAL   I CG1 
16250 C  CG2 . VAL   I  195 ? 1.4859 0.9073 1.6916 -0.0271 0.1000  0.1369  194 VAL   I CG2 
16251 N  N   . VAL   I  196 ? 1.5486 0.9353 1.7868 -0.0220 0.1676  0.0358  195 VAL   I N   
16252 C  CA  . VAL   I  196 ? 1.6865 0.9258 1.8021 -0.0224 0.1875  0.0251  195 VAL   I CA  
16253 C  C   . VAL   I  196 ? 1.7044 0.7904 1.7627 0.0240  0.1578  0.0252  195 VAL   I C   
16254 O  O   . VAL   I  196 ? 1.8154 0.8320 1.7160 -0.0030 0.1533  0.0046  195 VAL   I O   
16255 C  CB  . VAL   I  196 ? 1.7113 1.0089 1.8715 -0.0154 0.2470  -0.0064 195 VAL   I CB  
16256 C  CG1 . VAL   I  196 ? 1.7643 1.1014 1.8546 -0.0267 0.2786  -0.0080 195 VAL   I CG1 
16257 C  CG2 . VAL   I  196 ? 1.7572 1.0239 1.9158 -0.0482 0.2629  -0.0132 195 VAL   I CG2 
16258 N  N   . LYS   I  197 ? 1.7304 0.7133 1.7597 0.0541  0.1445  0.0589  196 LYS   I N   
16259 C  CA  . LYS   I  197 ? 1.7498 0.7006 1.7551 0.0415  0.1159  0.0923  196 LYS   I CA  
16260 C  C   . LYS   I  197 ? 1.8231 0.8064 1.6870 -0.0045 0.1633  0.0853  196 LYS   I C   
16261 O  O   . LYS   I  197 ? 1.9341 0.8085 1.7682 -0.0727 0.1867  0.1886  196 LYS   I O   
16262 C  CB  . LYS   I  197 ? 1.7595 0.5998 1.7713 0.0263  0.1104  0.0650  196 LYS   I CB  
16263 C  CG  . LYS   I  197 ? 1.7443 0.5805 1.7779 0.0488  0.0787  0.0826  196 LYS   I CG  
16264 C  CD  . LYS   I  197 ? 1.7596 0.6294 1.7651 0.0589  0.0386  0.0862  196 LYS   I CD  
16265 C  CE  . LYS   I  197 ? 1.7345 0.6833 1.7584 0.0833  -0.0002 0.0879  196 LYS   I CE  
16266 N  NZ  . LYS   I  197 ? 1.7312 0.7655 1.7561 0.1174  -0.0089 0.0672  196 LYS   I NZ  
16267 N  N   . ARG   I  198 ? 1.8270 0.8050 1.6823 0.0322  0.1780  0.0801  197 ARG   I N   
16268 C  CA  . ARG   I  198 ? 1.8146 0.8411 1.6857 0.0563  0.2317  0.0723  197 ARG   I CA  
16269 C  C   . ARG   I  198 ? 1.8196 0.7405 1.6598 0.0901  0.1925  0.0499  197 ARG   I C   
16270 O  O   . ARG   I  198 ? 1.7625 0.6581 1.6753 0.0638  0.2111  -0.0170 197 ARG   I O   
16271 C  CB  . ARG   I  198 ? 1.7439 0.9432 1.6760 0.0443  0.2641  0.0530  197 ARG   I CB  
16272 C  CG  . ARG   I  198 ? 1.7792 1.0458 1.6571 -0.0205 0.2969  0.0572  197 ARG   I CG  
16273 C  CD  . ARG   I  198 ? 1.7050 1.1654 1.6653 -0.0538 0.3352  0.0441  197 ARG   I CD  
16274 N  NE  . ARG   I  198 ? 1.7217 1.2489 1.6686 -0.1034 0.3794  0.0409  197 ARG   I NE  
16275 C  CZ  . ARG   I  198 ? 1.6925 1.2557 1.6732 -0.1509 0.3942  0.0461  197 ARG   I CZ  
16276 N  NH1 . ARG   I  198 ? 1.6979 1.2821 1.6481 -0.1733 0.3571  0.0666  197 ARG   I NH1 
16277 N  NH2 . ARG   I  198 ? 1.6865 1.2788 1.7170 -0.1549 0.4601  0.0422  197 ARG   I NH2 
16278 N  N   . TYR   I  199 ? 1.8198 0.7907 1.6328 0.0824  0.1932  0.0804  198 TYR   I N   
16279 C  CA  . TYR   I  199 ? 1.8348 0.9611 1.6690 -0.0073 0.1829  0.0835  198 TYR   I CA  
16280 C  C   . TYR   I  199 ? 1.9046 0.9466 1.6353 -0.0072 0.1870  0.1082  198 TYR   I C   
16281 O  O   . TYR   I  199 ? 1.9788 0.9485 1.6195 -0.0607 0.2265  0.0968  198 TYR   I O   
16282 C  CB  . TYR   I  199 ? 1.8205 1.0304 1.6863 0.0251  0.1950  0.0863  198 TYR   I CB  
16283 C  CG  . TYR   I  199 ? 1.7681 1.0449 1.7665 0.0073  0.2234  0.0602  198 TYR   I CG  
16284 C  CD1 . TYR   I  199 ? 1.7573 1.0590 1.8045 -0.0045 0.2170  0.0818  198 TYR   I CD1 
16285 C  CD2 . TYR   I  199 ? 1.7621 1.0760 1.7867 0.0125  0.2121  0.0428  198 TYR   I CD2 
16286 C  CE1 . TYR   I  199 ? 1.7262 1.0974 1.7662 0.0214  0.2016  0.1236  198 TYR   I CE1 
16287 C  CE2 . TYR   I  199 ? 1.7436 1.0438 1.7414 -0.0060 0.2000  0.0896  198 TYR   I CE2 
16288 C  CZ  . TYR   I  199 ? 1.7261 1.0229 1.7162 0.0221  0.1981  0.1206  198 TYR   I CZ  
16289 O  OH  . TYR   I  199 ? 1.7480 1.0306 1.6265 0.0262  0.2065  0.0719  198 TYR   I OH  
16290 N  N   . LEU   I  200 ? 2.0013 1.0024 1.6136 -0.0899 0.1666  0.1135  199 LEU   I N   
16291 C  CA  . LEU   I  200 ? 2.0508 1.0047 1.6419 -0.0903 0.1984  0.1185  199 LEU   I CA  
16292 C  C   . LEU   I  200 ? 2.1101 1.0305 1.4743 -0.0649 0.2708  0.1350  199 LEU   I C   
16293 O  O   . LEU   I  200 ? 2.1312 1.1368 1.4158 -0.0961 0.2568  0.2832  199 LEU   I O   
16294 C  CB  . LEU   I  200 ? 2.0361 1.0569 1.5790 -0.1409 0.1166  0.0615  199 LEU   I CB  
16295 C  CG  . LEU   I  200 ? 2.0048 1.0862 1.6264 -0.1698 0.1183  0.0272  199 LEU   I CG  
16296 C  CD1 . LEU   I  200 ? 1.9750 1.0971 1.5393 -0.1518 0.1050  -0.0398 199 LEU   I CD1 
16297 C  CD2 . LEU   I  200 ? 2.0322 1.1181 1.6976 -0.2153 0.1216  0.0608  199 LEU   I CD2 
16298 N  N   . LYS   I  201 ? 2.0996 1.0622 1.5157 -0.0032 0.3094  0.1682  200 LYS   I N   
16299 C  CA  . LYS   I  201 ? 2.0877 1.0834 1.6168 0.1277  0.2940  0.0406  200 LYS   I CA  
16300 C  C   . LYS   I  201 ? 1.9361 1.0118 1.6980 0.1238  0.3012  0.0108  200 LYS   I C   
16301 O  O   . LYS   I  201 ? 1.9504 0.9910 1.7858 0.1491  0.3285  0.0659  200 LYS   I O   
16302 C  CB  . LYS   I  201 ? 2.1470 1.1341 1.6906 0.1435  0.3242  -0.0266 200 LYS   I CB  
16303 C  CG  . LYS   I  201 ? 2.2198 1.2393 1.7455 0.1359  0.3150  -0.1161 200 LYS   I CG  
16304 C  CD  . LYS   I  201 ? 2.3015 1.2835 1.7858 0.1239  0.3697  -0.1763 200 LYS   I CD  
16305 C  CE  . LYS   I  201 ? 2.3507 1.2949 1.8260 0.1965  0.3900  -0.2574 200 LYS   I CE  
16306 N  NZ  . LYS   I  201 ? 2.4016 1.3508 1.8743 0.2287  0.4171  -0.2743 200 LYS   I NZ  
16307 N  N   . MET   I  202 ? 1.8867 0.9523 1.6950 0.1804  0.1924  -0.0096 201 MET   I N   
16308 C  CA  . MET   I  202 ? 1.7766 0.9405 1.7269 0.1848  0.1292  0.0040  201 MET   I CA  
16309 C  C   . MET   I  202 ? 1.7878 1.0986 1.6385 0.2209  0.0748  -0.0281 201 MET   I C   
16310 O  O   . MET   I  202 ? 1.8129 1.2143 1.5505 0.2808  0.1311  -0.0288 201 MET   I O   
16311 C  CB  . MET   I  202 ? 1.7123 0.8044 1.7541 0.2628  0.0972  0.0128  201 MET   I CB  
16312 C  CG  . MET   I  202 ? 1.7615 0.7275 1.7506 0.3001  0.0341  0.0127  201 MET   I CG  
16313 S  SD  . MET   I  202 ? 1.7119 0.6678 1.7413 0.3614  -0.0253 0.0094  201 MET   I SD  
16314 C  CE  . MET   I  202 ? 1.7237 0.6767 1.7894 0.3839  0.0138  0.0266  201 MET   I CE  
16315 N  N   . ARG   I  203 ? 1.7451 1.0583 1.7248 0.1459  0.0380  -0.1241 202 ARG   I N   
16316 C  CA  . ARG   I  203 ? 1.8356 1.0189 1.7536 0.1467  -0.0118 -0.1382 202 ARG   I CA  
16317 C  C   . ARG   I  203 ? 1.7867 0.9594 1.7611 0.0866  -0.1478 -0.0591 202 ARG   I C   
16318 O  O   . ARG   I  203 ? 1.8472 0.8070 1.7822 -0.0125 -0.2200 -0.0762 202 ARG   I O   
16319 C  CB  . ARG   I  203 ? 1.7739 1.0178 1.7790 0.2108  -0.0480 -0.1427 202 ARG   I CB  
16320 C  CG  . ARG   I  203 ? 1.7204 0.9837 1.7780 0.2056  -0.0743 -0.1078 202 ARG   I CG  
16321 C  CD  . ARG   I  203 ? 1.7038 0.9571 1.8282 0.1349  -0.0606 -0.1101 202 ARG   I CD  
16322 N  NE  . ARG   I  203 ? 1.7066 0.9560 1.8565 0.1328  -0.0356 -0.1416 202 ARG   I NE  
16323 C  CZ  . ARG   I  203 ? 1.7105 1.0167 1.8506 0.1499  -0.0068 -0.1561 202 ARG   I CZ  
16324 N  NH1 . ARG   I  203 ? 1.7124 0.9735 1.8438 0.1506  0.0315  -0.1397 202 ARG   I NH1 
16325 N  NH2 . ARG   I  203 ? 1.7091 1.1283 1.8184 0.1665  -0.0309 -0.2051 202 ARG   I NH2 
16326 N  N   . GLN   I  204 ? 1.8412 0.9494 1.6947 0.1343  -0.1401 -0.0319 203 GLN   I N   
16327 C  CA  . GLN   I  204 ? 1.8664 1.0629 1.6015 0.1716  -0.1866 -0.0011 203 GLN   I CA  
16328 C  C   . GLN   I  204 ? 1.8039 1.1285 1.7267 0.1832  -0.2214 -0.0208 203 GLN   I C   
16329 O  O   . GLN   I  204 ? 1.8692 1.1802 1.6668 0.2350  -0.2371 -0.0878 203 GLN   I O   
16330 C  CB  . GLN   I  204 ? 1.8999 1.2163 1.4877 0.2016  -0.1959 -0.0658 203 GLN   I CB  
16331 C  CG  . GLN   I  204 ? 1.8961 1.2810 1.3839 0.1974  -0.1761 0.0040  203 GLN   I CG  
16332 C  CD  . GLN   I  204 ? 1.9170 1.2690 1.3256 0.2775  -0.1729 0.0646  203 GLN   I CD  
16333 O  OE1 . GLN   I  204 ? 1.9371 1.2708 1.1720 0.2583  -0.2957 0.1629  203 GLN   I OE1 
16334 N  NE2 . GLN   I  204 ? 1.9445 1.3394 1.3279 0.2675  -0.1699 0.0261  203 GLN   I NE2 
16335 N  N   . ASP   I  205 ? 1.8108 1.1567 1.8878 0.1582  -0.1258 0.0826  204 ASP   I N   
16336 C  CA  . ASP   I  205 ? 1.8683 1.1167 2.0555 0.1462  -0.0896 0.1044  204 ASP   I CA  
16337 C  C   . ASP   I  205 ? 1.8945 1.2054 2.0976 0.0950  -0.0292 0.1561  204 ASP   I C   
16338 O  O   . ASP   I  205 ? 2.0027 1.2837 2.2515 -0.0063 0.0270  0.1621  204 ASP   I O   
16339 C  CB  . ASP   I  205 ? 1.8611 1.1461 2.1531 0.1599  -0.0114 0.0675  204 ASP   I CB  
16340 C  CG  . ASP   I  205 ? 1.8474 1.0416 2.2296 0.2085  0.0217  0.0715  204 ASP   I CG  
16341 O  OD1 . ASP   I  205 ? 1.7596 0.8060 2.3108 0.1706  0.0753  0.1992  204 ASP   I OD1 
16342 O  OD2 . ASP   I  205 ? 1.9059 1.1011 2.3206 0.3678  -0.0127 0.1089  204 ASP   I OD2 
16343 O  OXT . ASP   I  205 ? 1.9195 1.1633 2.0876 0.0598  0.0014  0.2135  204 ASP   I OXT 
16344 N  N   . MET   J  1   ? 2.1255 1.0066 2.0312 -0.1144 -0.2681 -0.0705 1   MET   J N   
16345 C  CA  . MET   J  1   ? 2.1376 0.8907 2.0396 -0.1356 -0.2758 -0.0744 1   MET   J CA  
16346 C  C   . MET   J  1   ? 1.9366 0.9408 2.0508 -0.1067 -0.3117 -0.0124 1   MET   J C   
16347 O  O   . MET   J  1   ? 2.2195 0.9996 2.1314 -0.1283 -0.3304 -0.1207 1   MET   J O   
16348 C  CB  . MET   J  1   ? 2.1725 1.0413 2.0502 -0.2369 -0.3196 -0.0488 1   MET   J CB  
16349 C  CG  . MET   J  1   ? 2.2820 1.1503 2.1320 -0.1599 -0.3275 -0.1317 1   MET   J CG  
16350 S  SD  . MET   J  1   ? 2.5290 1.2856 2.2012 -0.1884 -0.2591 -0.0765 1   MET   J SD  
16351 C  CE  . MET   J  1   ? 2.5257 1.1564 2.1593 -0.2170 -0.2825 -0.1078 1   MET   J CE  
16352 N  N   . ASP   J  2   ? 1.8821 0.6690 1.9907 -0.0225 -0.2278 -0.0170 2   ASP   J N   
16353 C  CA  . ASP   J  2   ? 1.7689 0.7454 1.9590 -0.0034 -0.2067 0.0319  2   ASP   J CA  
16354 C  C   . ASP   J  2   ? 1.8026 0.6423 1.7269 0.0105  -0.2566 0.0709  2   ASP   J C   
16355 O  O   . ASP   J  2   ? 1.7486 0.5583 1.8127 0.0791  -0.2957 0.2242  2   ASP   J O   
16356 C  CB  . ASP   J  2   ? 1.7814 0.6726 2.0578 0.0603  -0.1361 -0.0249 2   ASP   J CB  
16357 C  CG  . ASP   J  2   ? 1.7347 0.6414 2.1922 0.1118  -0.0187 -0.0374 2   ASP   J CG  
16358 O  OD1 . ASP   J  2   ? 1.7703 0.4384 2.2672 0.2327  0.0524  -0.1155 2   ASP   J OD1 
16359 O  OD2 . ASP   J  2   ? 1.7730 0.6674 2.2925 0.1151  0.0710  -0.0288 2   ASP   J OD2 
16360 N  N   . ILE   J  3   ? 1.7789 0.6047 1.7045 -0.0273 -0.3286 0.0165  3   ILE   J N   
16361 C  CA  . ILE   J  3   ? 1.8187 0.6242 1.5997 -0.0402 -0.3416 -0.0098 3   ILE   J CA  
16362 C  C   . ILE   J  3   ? 1.8087 0.6593 1.4578 -0.0474 -0.3713 0.0416  3   ILE   J C   
16363 O  O   . ILE   J  3   ? 1.7971 0.6247 1.3803 -0.1285 -0.4137 0.0129  3   ILE   J O   
16364 C  CB  . ILE   J  3   ? 1.8403 0.7252 1.6087 -0.0519 -0.3299 -0.0473 3   ILE   J CB  
16365 C  CG1 . ILE   J  3   ? 1.9117 0.7394 1.6765 -0.1239 -0.3405 -0.0539 3   ILE   J CG1 
16366 C  CG2 . ILE   J  3   ? 1.8664 0.6602 1.5514 -0.0470 -0.3270 -0.0187 3   ILE   J CG2 
16367 C  CD1 . ILE   J  3   ? 1.9777 0.8010 1.6773 -0.1437 -0.3300 -0.0814 3   ILE   J CD1 
16368 N  N   . ILE   J  4   ? 1.8065 0.7143 1.3613 -0.0802 -0.3295 0.0723  4   ILE   J N   
16369 C  CA  . ILE   J  4   ? 1.8397 0.7110 1.2770 -0.0540 -0.3075 0.0766  4   ILE   J CA  
16370 C  C   . ILE   J  4   ? 1.8552 0.6612 1.2082 -0.0468 -0.2931 0.0391  4   ILE   J C   
16371 O  O   . ILE   J  4   ? 1.8100 0.5843 1.1052 -0.0306 -0.2155 0.0090  4   ILE   J O   
16372 C  CB  . ILE   J  4   ? 1.8018 0.7427 1.2352 -0.0498 -0.3481 0.0718  4   ILE   J CB  
16373 C  CG1 . ILE   J  4   ? 1.8197 0.7385 1.2337 -0.0459 -0.3242 0.1303  4   ILE   J CG1 
16374 C  CG2 . ILE   J  4   ? 1.7886 0.8177 1.3004 -0.0707 -0.3691 0.0641  4   ILE   J CG2 
16375 C  CD1 . ILE   J  4   ? 1.8180 0.7424 1.2046 -0.0534 -0.3159 0.1466  4   ILE   J CD1 
16376 N  N   . LEU   J  5   ? 1.9347 0.6908 1.1960 -0.0794 -0.2754 -0.0089 5   LEU   J N   
16377 C  CA  . LEU   J  5   ? 1.9313 0.6963 1.1943 -0.0511 -0.2955 -0.0218 5   LEU   J CA  
16378 C  C   . LEU   J  5   ? 1.9137 0.7238 1.1552 -0.0768 -0.2753 -0.0248 5   LEU   J C   
16379 O  O   . LEU   J  5   ? 1.9741 0.6625 1.0973 -0.1318 -0.3601 0.0731  5   LEU   J O   
16380 C  CB  . LEU   J  5   ? 2.0325 0.7259 1.1908 -0.0252 -0.3425 -0.0332 5   LEU   J CB  
16381 C  CG  . LEU   J  5   ? 2.1200 0.6700 1.2060 0.0499  -0.4078 0.0071  5   LEU   J CG  
16382 C  CD1 . LEU   J  5   ? 2.2187 0.7002 1.2158 0.0866  -0.3869 -0.0163 5   LEU   J CD1 
16383 C  CD2 . LEU   J  5   ? 2.1303 0.7138 1.2451 0.1002  -0.4307 -0.0141 5   LEU   J CD2 
16384 N  N   . GLY   J  6   ? 1.9033 0.6751 1.1262 -0.0379 -0.2338 -0.0556 6   GLY   J N   
16385 C  CA  . GLY   J  6   ? 1.9005 0.6592 1.1123 -0.0219 -0.2096 -0.0623 6   GLY   J CA  
16386 C  C   . GLY   J  6   ? 1.9284 0.6693 1.1084 -0.0375 -0.1744 -0.0503 6   GLY   J C   
16387 O  O   . GLY   J  6   ? 1.9239 0.7336 1.1586 -0.0153 -0.1940 -0.0505 6   GLY   J O   
16388 N  N   . ILE   J  7   ? 1.9511 0.6821 1.1358 -0.0579 -0.1725 -0.0188 7   ILE   J N   
16389 C  CA  . ILE   J  7   ? 1.9727 0.6986 1.1934 -0.0650 -0.1307 0.0076  7   ILE   J CA  
16390 C  C   . ILE   J  7   ? 1.9378 0.7033 1.1961 -0.0402 -0.1214 0.0296  7   ILE   J C   
16391 O  O   . ILE   J  7   ? 1.9751 0.6097 1.2216 -0.0309 -0.1130 0.0333  7   ILE   J O   
16392 C  CB  . ILE   J  7   ? 2.0287 0.6952 1.2203 -0.0407 -0.0791 -0.0139 7   ILE   J CB  
16393 C  CG1 . ILE   J  7   ? 2.0947 0.6912 1.2686 0.0045  -0.0893 0.0074  7   ILE   J CG1 
16394 C  CG2 . ILE   J  7   ? 2.0499 0.6115 1.2303 -0.0601 -0.0511 0.0094  7   ILE   J CG2 
16395 C  CD1 . ILE   J  7   ? 2.1569 0.7918 1.2854 0.0064  -0.0957 -0.0415 7   ILE   J CD1 
16396 N  N   . ARG   J  8   ? 1.8982 0.6796 1.2676 -0.0719 -0.0548 0.0323  8   ARG   J N   
16397 C  CA  . ARG   J  8   ? 1.9285 0.6533 1.2987 -0.0346 -0.0015 0.0637  8   ARG   J CA  
16398 C  C   . ARG   J  8   ? 1.9616 0.6508 1.3672 -0.0415 0.0490  0.0333  8   ARG   J C   
16399 O  O   . ARG   J  8   ? 1.9456 0.7344 1.3756 0.0055  0.0994  0.0428  8   ARG   J O   
16400 C  CB  . ARG   J  8   ? 1.9000 0.6131 1.3507 -0.0807 -0.0133 0.0870  8   ARG   J CB  
16401 C  CG  . ARG   J  8   ? 1.9148 0.6578 1.4218 -0.0927 0.0009  0.1261  8   ARG   J CG  
16402 C  CD  . ARG   J  8   ? 1.8661 0.6429 1.4722 -0.1135 -0.0249 0.1509  8   ARG   J CD  
16403 N  NE  . ARG   J  8   ? 1.8347 0.5650 1.5310 -0.1288 0.0107  0.1848  8   ARG   J NE  
16404 C  CZ  . ARG   J  8   ? 1.8152 0.5829 1.5142 -0.1472 0.0350  0.2090  8   ARG   J CZ  
16405 N  NH1 . ARG   J  8   ? 1.7998 0.6165 1.5509 -0.1348 0.0892  0.1571  8   ARG   J NH1 
16406 N  NH2 . ARG   J  8   ? 1.7848 0.6329 1.5298 -0.1458 0.0174  0.2187  8   ARG   J NH2 
16407 N  N   . VAL   J  9   ? 1.9600 0.6881 1.3233 0.0005  0.0706  0.0002  9   VAL   J N   
16408 C  CA  . VAL   J  9   ? 1.9913 0.7929 1.3682 -0.0275 0.1060  -0.0461 9   VAL   J CA  
16409 C  C   . VAL   J  9   ? 1.9739 0.7950 1.3246 -0.0392 0.1250  -0.1001 9   VAL   J C   
16410 O  O   . VAL   J  9   ? 1.8705 0.6949 1.4008 -0.0871 0.1408  -0.0921 9   VAL   J O   
16411 C  CB  . VAL   J  9   ? 2.0064 0.8424 1.4082 -0.0470 0.0561  -0.0096 9   VAL   J CB  
16412 C  CG1 . VAL   J  9   ? 2.0475 0.8816 1.4728 -0.1094 0.0371  0.0128  9   VAL   J CG1 
16413 C  CG2 . VAL   J  9   ? 2.0188 0.8443 1.3881 -0.0264 0.0597  -0.0231 9   VAL   J CG2 
16414 N  N   . GLN   J  10  ? 2.0398 0.8771 1.3189 -0.0822 0.1340  -0.0868 10  GLN   J N   
16415 C  CA  . GLN   J  10  ? 2.0500 0.9503 1.3427 -0.1225 0.1409  -0.0732 10  GLN   J CA  
16416 C  C   . GLN   J  10  ? 2.0453 0.9749 1.3207 -0.1052 0.1235  -0.0847 10  GLN   J C   
16417 O  O   . GLN   J  10  ? 2.0230 0.9630 1.3180 -0.1197 0.1232  -0.0592 10  GLN   J O   
16418 C  CB  . GLN   J  10  ? 2.1400 1.0898 1.3481 -0.1224 0.1610  -0.0496 10  GLN   J CB  
16419 C  CG  . GLN   J  10  ? 2.1848 1.1528 1.3435 -0.1236 0.1924  0.0204  10  GLN   J CG  
16420 C  CD  . GLN   J  10  ? 2.1612 1.2596 1.3545 -0.1587 0.2412  0.0532  10  GLN   J CD  
16421 O  OE1 . GLN   J  10  ? 2.1906 1.3569 1.3631 -0.1610 0.2252  0.0243  10  GLN   J OE1 
16422 N  NE2 . GLN   J  10  ? 2.2079 1.3280 1.3559 -0.1829 0.2722  0.1024  10  GLN   J NE2 
16423 N  N   . ASP   J  11  ? 2.0607 0.9562 1.3368 -0.1026 0.1058  -0.1221 11  ASP   J N   
16424 C  CA  . ASP   J  11  ? 2.1277 0.9150 1.3868 -0.1082 0.0957  -0.1625 11  ASP   J CA  
16425 C  C   . ASP   J  11  ? 2.0971 0.7771 1.2792 -0.0782 0.0365  -0.1650 11  ASP   J C   
16426 O  O   . ASP   J  11  ? 2.1070 0.7433 1.2182 -0.1036 0.0091  -0.1928 11  ASP   J O   
16427 C  CB  . ASP   J  11  ? 2.2533 0.9547 1.4028 -0.0869 0.0723  -0.1681 11  ASP   J CB  
16428 C  CG  . ASP   J  11  ? 2.2674 1.0891 1.5917 -0.1372 0.1126  -0.1855 11  ASP   J CG  
16429 O  OD1 . ASP   J  11  ? 2.3714 0.9915 1.7002 -0.1538 0.1121  -0.2487 11  ASP   J OD1 
16430 O  OD2 . ASP   J  11  ? 2.4740 1.3626 1.5837 -0.1218 0.0834  -0.2557 11  ASP   J OD2 
16431 N  N   . SER   J  12  ? 2.0723 0.7814 1.2234 -0.0756 0.0170  -0.1717 12  SER   J N   
16432 C  CA  . SER   J  12  ? 2.0480 0.7736 1.1909 -0.0439 -0.0126 -0.1580 12  SER   J CA  
16433 C  C   . SER   J  12  ? 2.0175 0.7394 1.1715 -0.0499 -0.0346 -0.1846 12  SER   J C   
16434 O  O   . SER   J  12  ? 1.9620 0.8578 1.1937 -0.0360 -0.0886 -0.1865 12  SER   J O   
16435 C  CB  . SER   J  12  ? 2.0726 0.8430 1.1976 -0.0444 -0.0451 -0.0945 12  SER   J CB  
16436 O  OG  . SER   J  12  ? 2.1540 0.8608 1.2662 -0.0358 -0.0278 -0.1124 12  SER   J OG  
16437 N  N   . VAL   J  13  ? 1.9876 0.6864 1.1884 -0.0170 -0.0523 -0.1506 13  VAL   J N   
16438 C  CA  . VAL   J  13  ? 2.0073 0.7418 1.2200 -0.0219 -0.0568 -0.1013 13  VAL   J CA  
16439 C  C   . VAL   J  13  ? 2.0071 0.6733 1.2084 0.0152  -0.0805 -0.0986 13  VAL   J C   
16440 O  O   . VAL   J  13  ? 2.0679 0.5344 1.2719 0.0090  -0.0898 -0.1192 13  VAL   J O   
16441 C  CB  . VAL   J  13  ? 1.9786 0.8137 1.1692 -0.0491 -0.0383 -0.0504 13  VAL   J CB  
16442 C  CG1 . VAL   J  13  ? 1.9838 0.8831 1.2011 -0.0518 -0.0234 -0.0146 13  VAL   J CG1 
16443 C  CG2 . VAL   J  13  ? 1.9607 0.8067 1.1990 -0.0640 -0.0196 0.0052  13  VAL   J CG2 
16444 N  N   . ILE   J  14  ? 2.0606 0.6830 1.2447 -0.0370 -0.0606 -0.0783 14  ILE   J N   
16445 C  CA  . ILE   J  14  ? 2.0596 0.6621 1.2203 -0.0319 -0.0690 -0.0438 14  ILE   J CA  
16446 C  C   . ILE   J  14  ? 2.0444 0.5915 1.2163 0.0062  -0.0878 -0.0283 14  ILE   J C   
16447 O  O   . ILE   J  14  ? 2.0172 0.5832 1.1842 0.0083  -0.0641 -0.0399 14  ILE   J O   
16448 C  CB  . ILE   J  14  ? 2.1146 0.6906 1.2328 -0.0447 -0.0582 -0.0676 14  ILE   J CB  
16449 C  CG1 . ILE   J  14  ? 2.1436 0.7268 1.2239 -0.0375 -0.0340 -0.0765 14  ILE   J CG1 
16450 C  CG2 . ILE   J  14  ? 2.1461 0.6706 1.2402 -0.0636 -0.0695 -0.0751 14  ILE   J CG2 
16451 C  CD1 . ILE   J  14  ? 2.1708 0.7699 1.2434 -0.0072 -0.0153 -0.0779 14  ILE   J CD1 
16452 N  N   . LEU   J  15  ? 2.0446 0.5637 1.1850 0.0361  -0.1149 -0.0003 15  LEU   J N   
16453 C  CA  . LEU   J  15  ? 2.0468 0.5550 1.2014 0.0201  -0.1581 0.0438  15  LEU   J CA  
16454 C  C   . LEU   J  15  ? 2.0209 0.6127 1.2004 0.0300  -0.1985 0.0631  15  LEU   J C   
16455 O  O   . LEU   J  15  ? 2.0590 0.4890 1.2955 -0.0320 -0.2598 0.1016  15  LEU   J O   
16456 C  CB  . LEU   J  15  ? 2.0652 0.5882 1.2231 0.0602  -0.1465 0.0541  15  LEU   J CB  
16457 C  CG  . LEU   J  15  ? 2.0502 0.6246 1.2969 0.0323  -0.1448 0.0652  15  LEU   J CG  
16458 C  CD1 . LEU   J  15  ? 2.0358 0.6469 1.3023 0.0383  -0.1353 0.0692  15  LEU   J CD1 
16459 C  CD2 . LEU   J  15  ? 2.0755 0.5922 1.3612 0.0671  -0.1186 0.0947  15  LEU   J CD2 
16460 N  N   . ALA   J  16  ? 2.0171 0.6165 1.1933 0.0241  -0.1502 0.0614  16  ALA   J N   
16461 C  CA  . ALA   J  16  ? 2.0260 0.5871 1.1455 0.0377  -0.1361 0.0338  16  ALA   J CA  
16462 C  C   . ALA   J  16  ? 1.9958 0.5293 1.1404 0.0717  -0.1265 0.0064  16  ALA   J C   
16463 O  O   . ALA   J  16  ? 1.9746 0.5599 1.1644 0.0870  -0.1125 0.0684  16  ALA   J O   
16464 C  CB  . ALA   J  16  ? 2.0546 0.5814 1.1530 0.0391  -0.1245 0.0425  16  ALA   J CB  
16465 N  N   . SER   J  17  ? 1.9955 0.5091 1.1092 0.0703  -0.1298 -0.0604 17  SER   J N   
16466 C  CA  . SER   J  17  ? 1.9969 0.5512 1.1083 0.0374  -0.1253 -0.0999 17  SER   J CA  
16467 C  C   . SER   J  17  ? 1.9634 0.5328 1.0782 0.0809  -0.1606 -0.0949 17  SER   J C   
16468 O  O   . SER   J  17  ? 1.9869 0.6434 1.0733 0.0630  -0.1777 -0.0754 17  SER   J O   
16469 C  CB  . SER   J  17  ? 2.0952 0.6249 1.1132 0.0187  -0.0723 -0.1883 17  SER   J CB  
16470 O  OG  . SER   J  17  ? 2.1970 0.6085 1.1928 -0.0307 0.0351  -0.3437 17  SER   J OG  
16471 N  N   . SER   J  18  ? 1.9205 0.4951 1.0914 0.0772  -0.1585 -0.1251 18  SER   J N   
16472 C  CA  . SER   J  18  ? 1.9410 0.4820 1.0985 0.0752  -0.1861 -0.1412 18  SER   J CA  
16473 C  C   . SER   J  18  ? 1.9140 0.4816 1.1213 0.0518  -0.2236 -0.0869 18  SER   J C   
16474 O  O   . SER   J  18  ? 1.9193 0.5184 1.0770 0.0830  -0.2019 -0.0824 18  SER   J O   
16475 C  CB  . SER   J  18  ? 1.9286 0.4339 1.0846 0.0714  -0.1844 -0.1740 18  SER   J CB  
16476 O  OG  . SER   J  18  ? 1.8990 0.4558 1.0519 0.1052  -0.1399 -0.1217 18  SER   J OG  
16477 N  N   . LYS   J  19  ? 1.9317 0.4542 1.1526 0.0331  -0.2421 -0.0699 19  LYS   J N   
16478 C  CA  . LYS   J  19  ? 1.9122 0.4786 1.1735 0.0059  -0.2619 -0.0361 19  LYS   J CA  
16479 C  C   . LYS   J  19  ? 1.9147 0.4498 1.1915 0.0103  -0.2808 0.0079  19  LYS   J C   
16480 O  O   . LYS   J  19  ? 1.9280 0.4090 1.2158 0.0141  -0.2878 0.0620  19  LYS   J O   
16481 C  CB  . LYS   J  19  ? 1.9488 0.5423 1.1734 -0.0433 -0.2557 -0.0792 19  LYS   J CB  
16482 C  CG  . LYS   J  19  ? 1.9566 0.6068 1.1513 -0.0655 -0.2481 -0.0884 19  LYS   J CG  
16483 C  CD  . LYS   J  19  ? 1.9786 0.6897 1.1653 -0.0888 -0.2726 -0.0833 19  LYS   J CD  
16484 C  CE  . LYS   J  19  ? 2.0091 0.7966 1.1413 -0.0871 -0.2591 -0.1326 19  LYS   J CE  
16485 N  NZ  . LYS   J  19  ? 2.0449 0.9386 1.1341 -0.0981 -0.2707 -0.1264 19  LYS   J NZ  
16486 N  N   . ALA   J  20  ? 1.9075 0.4621 1.1943 0.0083  -0.2788 0.0187  20  ALA   J N   
16487 C  CA  . ALA   J  20  ? 1.8860 0.4729 1.2248 -0.0044 -0.2972 0.0266  20  ALA   J CA  
16488 C  C   . ALA   J  20  ? 1.8185 0.4523 1.2074 -0.0126 -0.2907 0.0520  20  ALA   J C   
16489 O  O   . ALA   J  20  ? 1.8492 0.4440 1.1737 -0.0270 -0.2878 0.0408  20  ALA   J O   
16490 C  CB  . ALA   J  20  ? 1.9087 0.4769 1.2504 0.0059  -0.2940 0.0263  20  ALA   J CB  
16491 N  N   . VAL   J  21  ? 1.7793 0.4400 1.2327 -0.0362 -0.3235 0.0893  21  VAL   J N   
16492 C  CA  . VAL   J  21  ? 1.7237 0.4132 1.2528 -0.0355 -0.2939 0.1109  21  VAL   J CA  
16493 C  C   . VAL   J  21  ? 1.7554 0.4597 1.3385 -0.0774 -0.2894 0.1205  21  VAL   J C   
16494 O  O   . VAL   J  21  ? 1.7873 0.4911 1.3124 -0.0738 -0.3321 0.1066  21  VAL   J O   
16495 C  CB  . VAL   J  21  ? 1.6861 0.4123 1.2565 -0.0376 -0.3162 0.1190  21  VAL   J CB  
16496 C  CG1 . VAL   J  21  ? 1.6502 0.3413 1.2713 -0.0302 -0.3022 0.1272  21  VAL   J CG1 
16497 C  CG2 . VAL   J  21  ? 1.6685 0.4206 1.2144 -0.0208 -0.2931 0.1204  21  VAL   J CG2 
16498 N  N   . THR   J  22  ? 1.7729 0.4410 1.3829 -0.0997 -0.2611 0.1677  22  THR   J N   
16499 C  CA  . THR   J  22  ? 1.8257 0.5070 1.3913 -0.1413 -0.2709 0.2261  22  THR   J CA  
16500 C  C   . THR   J  22  ? 1.8045 0.4979 1.3744 -0.1644 -0.2779 0.2511  22  THR   J C   
16501 O  O   . THR   J  22  ? 1.7845 0.4611 1.2800 -0.1543 -0.2401 0.2716  22  THR   J O   
16502 C  CB  . THR   J  22  ? 1.8564 0.4952 1.4471 -0.1436 -0.2528 0.2384  22  THR   J CB  
16503 O  OG1 . THR   J  22  ? 1.8880 0.3913 1.4291 -0.1787 -0.2570 0.3076  22  THR   J OG1 
16504 C  CG2 . THR   J  22  ? 1.8887 0.5273 1.5078 -0.1791 -0.2407 0.2406  22  THR   J CG2 
16505 N  N   . ARG   J  23  ? 1.8029 0.6350 1.4767 -0.1987 -0.2940 0.2562  23  ARG   J N   
16506 C  CA  . ARG   J  23  ? 1.8204 0.7813 1.5014 -0.2377 -0.2753 0.2508  23  ARG   J CA  
16507 C  C   . ARG   J  23  ? 1.8196 0.8592 1.5616 -0.3030 -0.2680 0.2705  23  ARG   J C   
16508 O  O   . ARG   J  23  ? 1.8017 1.0044 1.6011 -0.3735 -0.2533 0.2675  23  ARG   J O   
16509 C  CB  . ARG   J  23  ? 1.7837 0.8146 1.5671 -0.2223 -0.2950 0.2747  23  ARG   J CB  
16510 C  CG  . ARG   J  23  ? 1.7664 0.8526 1.5806 -0.2801 -0.2863 0.2783  23  ARG   J CG  
16511 C  CD  . ARG   J  23  ? 1.8082 0.8494 1.6069 -0.2914 -0.3061 0.3023  23  ARG   J CD  
16512 N  NE  . ARG   J  23  ? 1.8135 0.7953 1.6704 -0.3263 -0.2899 0.3096  23  ARG   J NE  
16513 C  CZ  . ARG   J  23  ? 1.8491 0.7764 1.7186 -0.3398 -0.2860 0.2803  23  ARG   J CZ  
16514 N  NH1 . ARG   J  23  ? 1.8799 0.7916 1.7568 -0.3316 -0.2370 0.2499  23  ARG   J NH1 
16515 N  NH2 . ARG   J  23  ? 1.8369 0.8376 1.7222 -0.2307 -0.3171 0.3318  23  ARG   J NH2 
16516 N  N   . GLY   J  24  ? 1.8697 0.8343 1.5545 -0.2939 -0.2326 0.2787  24  GLY   J N   
16517 C  CA  . GLY   J  24  ? 1.9329 0.7661 1.5539 -0.2588 -0.2406 0.1857  24  GLY   J CA  
16518 C  C   . GLY   J  24  ? 1.9539 0.7309 1.5719 -0.2662 -0.2941 0.1652  24  GLY   J C   
16519 O  O   . GLY   J  24  ? 1.9649 0.7047 1.5376 -0.2286 -0.2878 0.1577  24  GLY   J O   
16520 N  N   . ILE   J  25  ? 1.9948 0.7150 1.5695 -0.2598 -0.3224 0.1261  25  ILE   J N   
16521 C  CA  . ILE   J  25  ? 2.0050 0.6705 1.5987 -0.2310 -0.3545 0.1178  25  ILE   J CA  
16522 C  C   . ILE   J  25  ? 1.9786 0.6340 1.5939 -0.1971 -0.3690 0.0773  25  ILE   J C   
16523 O  O   . ILE   J  25  ? 1.9538 0.7177 1.5728 -0.1489 -0.4550 0.0977  25  ILE   J O   
16524 C  CB  . ILE   J  25  ? 2.0560 0.6375 1.6525 -0.2326 -0.3640 0.1026  25  ILE   J CB  
16525 C  CG1 . ILE   J  25  ? 2.0333 0.6375 1.6645 -0.2645 -0.3904 0.1110  25  ILE   J CG1 
16526 C  CG2 . ILE   J  25  ? 2.0575 0.5944 1.6709 -0.2085 -0.3444 0.1031  25  ILE   J CG2 
16527 C  CD1 . ILE   J  25  ? 2.0442 0.6872 1.7153 -0.2987 -0.4132 0.1101  25  ILE   J CD1 
16528 N  N   . SER   J  26  ? 1.9255 0.6277 1.5153 -0.1987 -0.3406 0.0303  26  SER   J N   
16529 C  CA  . SER   J  26  ? 1.9137 0.5545 1.4750 -0.1967 -0.3327 -0.0232 26  SER   J CA  
16530 C  C   . SER   J  26  ? 1.8854 0.5493 1.4286 -0.1664 -0.3163 -0.0158 26  SER   J C   
16531 O  O   . SER   J  26  ? 1.8498 0.5369 1.3975 -0.1525 -0.2992 -0.0030 26  SER   J O   
16532 C  CB  . SER   J  26  ? 1.9058 0.5154 1.4662 -0.2124 -0.3391 -0.0327 26  SER   J CB  
16533 O  OG  . SER   J  26  ? 2.0110 0.3580 1.4463 -0.2243 -0.3783 -0.0915 26  SER   J OG  
16534 N  N   . VAL   J  27  ? 1.8903 0.5432 1.4004 -0.1482 -0.3625 -0.0402 27  VAL   J N   
16535 C  CA  . VAL   J  27  ? 1.8788 0.5823 1.3528 -0.1441 -0.3558 -0.0317 27  VAL   J CA  
16536 C  C   . VAL   J  27  ? 1.8528 0.6949 1.3670 -0.1151 -0.4058 -0.0071 27  VAL   J C   
16537 O  O   . VAL   J  27  ? 1.8727 0.7220 1.4019 -0.1493 -0.4242 -0.0556 27  VAL   J O   
16538 C  CB  . VAL   J  27  ? 1.9140 0.5599 1.3480 -0.1601 -0.3651 -0.0659 27  VAL   J CB  
16539 C  CG1 . VAL   J  27  ? 1.8933 0.5822 1.3244 -0.1476 -0.3378 -0.0716 27  VAL   J CG1 
16540 C  CG2 . VAL   J  27  ? 1.9445 0.5219 1.3504 -0.1743 -0.3530 -0.0612 27  VAL   J CG2 
16541 N  N   . LEU   J  28  ? 1.8551 0.6933 1.3601 -0.0823 -0.3867 0.0017  28  LEU   J N   
16542 C  CA  . LEU   J  28  ? 1.8612 0.7078 1.4049 -0.0748 -0.3957 0.0225  28  LEU   J CA  
16543 C  C   . LEU   J  28  ? 1.8545 0.6296 1.4174 -0.0474 -0.4169 0.0099  28  LEU   J C   
16544 O  O   . LEU   J  28  ? 1.9295 0.6387 1.3969 -0.0116 -0.4482 0.0119  28  LEU   J O   
16545 C  CB  . LEU   J  28  ? 1.8544 0.7536 1.3606 -0.0850 -0.3730 0.0445  28  LEU   J CB  
16546 C  CG  . LEU   J  28  ? 1.8844 0.8841 1.3901 -0.1099 -0.3250 0.0623  28  LEU   J CG  
16547 C  CD1 . LEU   J  28  ? 1.8655 0.8899 1.4124 -0.1088 -0.2974 0.0458  28  LEU   J CD1 
16548 C  CD2 . LEU   J  28  ? 1.8971 0.9519 1.4189 -0.1251 -0.3551 0.0371  28  LEU   J CD2 
16549 N  N   . LYS   J  29  ? 1.8756 0.5689 1.4306 -0.0404 -0.3766 -0.0014 29  LYS   J N   
16550 C  CA  . LYS   J  29  ? 1.9185 0.6059 1.4160 0.0041  -0.3720 0.0318  29  LYS   J CA  
16551 C  C   . LYS   J  29  ? 1.9835 0.4617 1.3724 -0.0001 -0.3530 -0.0122 29  LYS   J C   
16552 O  O   . LYS   J  29  ? 1.9790 0.3968 1.3623 0.0292  -0.3140 -0.0363 29  LYS   J O   
16553 C  CB  . LYS   J  29  ? 1.9394 0.6291 1.4613 0.0108  -0.3445 0.0007  29  LYS   J CB  
16554 C  CG  . LYS   J  29  ? 1.9919 0.6865 1.5052 0.0296  -0.3380 0.0381  29  LYS   J CG  
16555 C  CD  . LYS   J  29  ? 1.9994 0.6908 1.5728 0.0365  -0.3040 0.0168  29  LYS   J CD  
16556 C  CE  . LYS   J  29  ? 2.0604 0.7227 1.6046 0.0458  -0.2805 0.0438  29  LYS   J CE  
16557 N  NZ  . LYS   J  29  ? 2.0939 0.7869 1.6363 0.0637  -0.2547 -0.0294 29  LYS   J NZ  
16558 N  N   . ASP   J  30  ? 2.0100 0.4736 1.3599 0.0047  -0.4050 -0.0255 30  ASP   J N   
16559 C  CA  . ASP   J  30  ? 2.0165 0.5598 1.3803 0.0151  -0.4058 -0.0514 30  ASP   J CA  
16560 C  C   . ASP   J  30  ? 2.0140 0.6589 1.2959 0.0149  -0.3977 -0.0176 30  ASP   J C   
16561 O  O   . ASP   J  30  ? 2.0109 0.7673 1.2558 0.0593  -0.4047 0.0475  30  ASP   J O   
16562 C  CB  . ASP   J  30  ? 2.0839 0.6270 1.4770 -0.0249 -0.4346 -0.1063 30  ASP   J CB  
16563 C  CG  . ASP   J  30  ? 2.1317 0.6363 1.5136 -0.0249 -0.4770 -0.1178 30  ASP   J CG  
16564 O  OD1 . ASP   J  30  ? 2.1233 0.6259 1.5803 -0.0448 -0.4729 -0.1544 30  ASP   J OD1 
16565 O  OD2 . ASP   J  30  ? 2.2214 0.7865 1.5474 -0.0576 -0.4920 -0.1978 30  ASP   J OD2 
16566 N  N   . SER   J  31  ? 2.0035 0.6228 1.2510 -0.0342 -0.3986 0.0208  31  SER   J N   
16567 C  CA  . SER   J  31  ? 2.0410 0.6103 1.2498 -0.0244 -0.3913 0.0299  31  SER   J CA  
16568 C  C   . SER   J  31  ? 2.0504 0.5525 1.2588 -0.0126 -0.3606 0.0382  31  SER   J C   
16569 O  O   . SER   J  31  ? 2.0657 0.5164 1.2901 -0.0439 -0.3629 -0.0211 31  SER   J O   
16570 C  CB  . SER   J  31  ? 2.0336 0.6589 1.2883 -0.0433 -0.4162 0.0312  31  SER   J CB  
16571 O  OG  . SER   J  31  ? 2.0341 0.6884 1.2866 -0.0754 -0.4003 0.0206  31  SER   J OG  
16572 N  N   . ASP   J  32  ? 2.0839 0.4581 1.2724 -0.0123 -0.3297 0.0718  32  ASP   J N   
16573 C  CA  . ASP   J  32  ? 2.1252 0.3847 1.3301 -0.0426 -0.3084 0.0673  32  ASP   J CA  
16574 C  C   . ASP   J  32  ? 2.1221 0.4451 1.2193 -0.0212 -0.2724 0.0964  32  ASP   J C   
16575 O  O   . ASP   J  32  ? 2.2918 0.2039 1.1381 -0.0623 -0.2821 0.0773  32  ASP   J O   
16576 C  CB  . ASP   J  32  ? 2.1295 0.3798 1.3723 -0.0329 -0.2820 0.0898  32  ASP   J CB  
16577 C  CG  . ASP   J  32  ? 2.1515 0.2909 1.4840 -0.0468 -0.2713 0.0586  32  ASP   J CG  
16578 O  OD1 . ASP   J  32  ? 2.1778 0.3222 1.6282 -0.0203 -0.1856 0.0039  32  ASP   J OD1 
16579 O  OD2 . ASP   J  32  ? 2.1335 0.1795 1.5071 -0.0249 -0.2652 0.0442  32  ASP   J OD2 
16580 N  N   . ASP   J  33  ? 2.1618 0.4719 1.2307 -0.1370 -0.3125 0.1024  33  ASP   J N   
16581 C  CA  . ASP   J  33  ? 2.1217 0.6577 1.3039 -0.1476 -0.2935 0.1328  33  ASP   J CA  
16582 C  C   . ASP   J  33  ? 1.9843 0.5950 1.3492 -0.0796 -0.3242 0.1488  33  ASP   J C   
16583 O  O   . ASP   J  33  ? 1.9617 0.3447 1.4900 -0.1050 -0.3434 0.2404  33  ASP   J O   
16584 C  CB  . ASP   J  33  ? 2.1908 0.6598 1.3097 -0.1700 -0.2935 0.1383  33  ASP   J CB  
16585 C  CG  . ASP   J  33  ? 2.2449 0.8406 1.3444 -0.2588 -0.2553 0.0758  33  ASP   J CG  
16586 O  OD1 . ASP   J  33  ? 2.2117 0.8759 1.3030 -0.2885 -0.2667 -0.0035 33  ASP   J OD1 
16587 O  OD2 . ASP   J  33  ? 2.2944 0.9954 1.3243 -0.2821 -0.2672 0.2539  33  ASP   J OD2 
16588 N  N   . LYS   J  34  ? 1.8832 0.7992 1.4044 -0.0746 -0.3575 0.1563  34  LYS   J N   
16589 C  CA  . LYS   J  34  ? 1.7761 0.7185 1.3750 -0.0966 -0.3053 0.1245  34  LYS   J CA  
16590 C  C   . LYS   J  34  ? 1.7583 0.6356 1.3114 -0.0597 -0.2813 0.0798  34  LYS   J C   
16591 O  O   . LYS   J  34  ? 1.7095 0.5010 1.2486 -0.1150 -0.2365 0.0737  34  LYS   J O   
16592 C  CB  . LYS   J  34  ? 1.7560 0.7378 1.3966 -0.0742 -0.3157 0.1294  34  LYS   J CB  
16593 C  CG  . LYS   J  34  ? 1.7578 0.7589 1.4471 -0.0950 -0.3329 0.1091  34  LYS   J CG  
16594 C  CD  . LYS   J  34  ? 1.7569 0.7868 1.4475 -0.0621 -0.3352 0.0931  34  LYS   J CD  
16595 C  CE  . LYS   J  34  ? 1.8017 0.7977 1.4945 -0.0843 -0.3354 0.1203  34  LYS   J CE  
16596 N  NZ  . LYS   J  34  ? 1.8121 0.8434 1.5486 -0.0631 -0.3561 0.1389  34  LYS   J NZ  
16597 N  N   . THR   J  35  ? 1.7344 0.6775 1.2548 -0.0341 -0.2995 0.1054  35  THR   J N   
16598 C  CA  . THR   J  35  ? 1.6827 0.7239 1.1646 -0.0228 -0.2685 0.0889  35  THR   J CA  
16599 C  C   . THR   J  35  ? 1.6870 0.6667 1.1120 -0.0627 -0.3262 0.0684  35  THR   J C   
16600 O  O   . THR   J  35  ? 1.7303 0.4323 1.0897 0.0099  -0.3816 0.0162  35  THR   J O   
16601 C  CB  . THR   J  35  ? 1.7056 0.9192 1.1517 -0.0336 -0.2650 0.0846  35  THR   J CB  
16602 O  OG1 . THR   J  35  ? 1.6986 1.0012 1.0844 -0.0448 -0.2415 0.0950  35  THR   J OG1 
16603 C  CG2 . THR   J  35  ? 1.6756 0.9644 1.1417 -0.0338 -0.2683 0.0798  35  THR   J CG2 
16604 N  N   . ARG   J  36  ? 1.6920 0.5492 1.0705 -0.0214 -0.2778 0.0777  36  ARG   J N   
16605 C  CA  . ARG   J  36  ? 1.6947 0.5541 1.0187 -0.0087 -0.2827 0.0714  36  ARG   J CA  
16606 C  C   . ARG   J  36  ? 1.7442 0.4680 1.0184 0.0031  -0.2435 0.0363  36  ARG   J C   
16607 O  O   . ARG   J  36  ? 1.7903 0.4042 0.9851 0.0534  -0.2506 0.0440  36  ARG   J O   
16608 C  CB  . ARG   J  36  ? 1.6370 0.5639 0.9967 -0.0187 -0.2825 0.1042  36  ARG   J CB  
16609 C  CG  . ARG   J  36  ? 1.5989 0.6257 0.9851 -0.0082 -0.3159 0.1362  36  ARG   J CG  
16610 C  CD  . ARG   J  36  ? 1.6338 0.7214 0.9736 0.0270  -0.3240 0.1783  36  ARG   J CD  
16611 N  NE  . ARG   J  36  ? 1.6092 0.7551 0.9730 0.0318  -0.3408 0.2286  36  ARG   J NE  
16612 C  CZ  . ARG   J  36  ? 1.6150 0.7860 0.9776 0.0367  -0.3346 0.2457  36  ARG   J CZ  
16613 N  NH1 . ARG   J  36  ? 1.6437 0.8446 0.9685 0.0557  -0.3236 0.2130  36  ARG   J NH1 
16614 N  NH2 . ARG   J  36  ? 1.6144 0.7651 0.9490 0.0423  -0.3441 0.2400  36  ARG   J NH2 
16615 N  N   . GLN   J  37  ? 1.7640 0.4095 1.0304 0.0260  -0.2296 -0.0029 37  GLN   J N   
16616 C  CA  . GLN   J  37  ? 1.7634 0.3853 1.0904 0.0559  -0.2224 0.0426  37  GLN   J CA  
16617 C  C   . GLN   J  37  ? 1.7274 0.3369 1.1231 0.0079  -0.2671 0.0605  37  GLN   J C   
16618 O  O   . GLN   J  37  ? 1.6400 0.3927 1.1786 -0.0283 -0.2995 0.0512  37  GLN   J O   
16619 C  CB  . GLN   J  37  ? 1.7771 0.4246 1.0990 0.0859  -0.2341 0.0385  37  GLN   J CB  
16620 C  CG  . GLN   J  37  ? 1.7946 0.5010 1.1474 0.0573  -0.2144 0.0711  37  GLN   J CG  
16621 C  CD  . GLN   J  37  ? 1.8505 0.5976 1.1796 0.0551  -0.2410 0.1145  37  GLN   J CD  
16622 O  OE1 . GLN   J  37  ? 1.9448 0.6076 1.3619 0.0937  -0.2520 0.1773  37  GLN   J OE1 
16623 N  NE2 . GLN   J  37  ? 1.8660 0.5829 1.2154 0.0458  -0.2457 0.1027  37  GLN   J NE2 
16624 N  N   . LEU   J  38  ? 1.7278 0.3615 1.1391 -0.0244 -0.2658 0.0447  38  LEU   J N   
16625 C  CA  . LEU   J  38  ? 1.7801 0.5400 1.1583 -0.0495 -0.2566 -0.0365 38  LEU   J CA  
16626 C  C   . LEU   J  38  ? 1.8442 0.6297 1.2007 -0.1320 -0.2017 -0.0051 38  LEU   J C   
16627 O  O   . LEU   J  38  ? 1.9465 0.7611 1.3051 -0.0888 -0.2345 -0.1407 38  LEU   J O   
16628 C  CB  . LEU   J  38  ? 1.7470 0.5351 1.1492 -0.0669 -0.2419 -0.0472 38  LEU   J CB  
16629 C  CG  . LEU   J  38  ? 1.7148 0.5252 1.1398 -0.1344 -0.2189 -0.0952 38  LEU   J CG  
16630 C  CD1 . LEU   J  38  ? 1.7047 0.5200 1.1337 -0.1132 -0.1949 -0.0809 38  LEU   J CD1 
16631 C  CD2 . LEU   J  38  ? 1.6965 0.5118 1.1182 -0.1717 -0.2434 -0.1265 38  LEU   J CD2 
16632 N  N   . SER   J  39  ? 1.8818 0.6890 1.2066 -0.1878 -0.1728 -0.0402 39  SER   J N   
16633 C  CA  . SER   J  39  ? 1.8849 0.6203 1.2493 -0.1919 -0.1922 -0.0635 39  SER   J CA  
16634 C  C   . SER   J  39  ? 1.9268 0.7154 1.2324 -0.1924 -0.2062 -0.0341 39  SER   J C   
16635 O  O   . SER   J  39  ? 1.9369 0.7357 1.3012 -0.2199 -0.2206 -0.0687 39  SER   J O   
16636 C  CB  . SER   J  39  ? 1.9224 0.5236 1.2328 -0.2166 -0.1838 -0.0606 39  SER   J CB  
16637 O  OG  . SER   J  39  ? 1.9483 0.4608 1.2460 -0.2217 -0.1999 -0.0967 39  SER   J OG  
16638 N  N   . PRO   J  40  ? 1.9312 0.6734 1.2512 -0.1251 -0.2305 -0.0382 40  PRO   J N   
16639 C  CA  . PRO   J  40  ? 1.9148 0.6910 1.2477 -0.1008 -0.2353 -0.0293 40  PRO   J CA  
16640 C  C   . PRO   J  40  ? 1.9293 0.6677 1.2405 -0.1225 -0.1836 -0.0437 40  PRO   J C   
16641 O  O   . PRO   J  40  ? 1.8687 0.6238 1.2300 -0.0858 -0.1762 -0.0294 40  PRO   J O   
16642 C  CB  . PRO   J  40  ? 1.9605 0.6926 1.2308 -0.0846 -0.2446 -0.0138 40  PRO   J CB  
16643 C  CG  . PRO   J  40  ? 1.9502 0.7072 1.2568 -0.0685 -0.2557 -0.0291 40  PRO   J CG  
16644 C  CD  . PRO   J  40  ? 1.9295 0.6791 1.2488 -0.0676 -0.2322 -0.0452 40  PRO   J CD  
16645 N  N   . HIS   J  41  ? 1.8920 0.6710 1.2252 -0.1251 -0.1458 -0.0320 41  HIS   J N   
16646 C  CA  . HIS   J  41  ? 1.8674 0.6845 1.1935 -0.1348 -0.1353 0.0028  41  HIS   J CA  
16647 C  C   . HIS   J  41  ? 1.8211 0.7174 1.1884 -0.1189 -0.1237 0.0154  41  HIS   J C   
16648 O  O   . HIS   J  41  ? 1.8120 0.8255 1.2382 -0.0989 -0.1131 0.0455  41  HIS   J O   
16649 C  CB  . HIS   J  41  ? 1.8890 0.7081 1.1879 -0.1582 -0.1331 0.0153  41  HIS   J CB  
16650 C  CG  . HIS   J  41  ? 1.9361 0.6835 1.1850 -0.1662 -0.1388 0.0082  41  HIS   J CG  
16651 N  ND1 . HIS   J  41  ? 1.9339 0.6632 1.1615 -0.1796 -0.1381 0.0501  41  HIS   J ND1 
16652 C  CD2 . HIS   J  41  ? 1.9912 0.7254 1.1668 -0.1656 -0.1653 0.0601  41  HIS   J CD2 
16653 C  CE1 . HIS   J  41  ? 1.9598 0.6802 1.1629 -0.1696 -0.1931 0.0455  41  HIS   J CE1 
16654 N  NE2 . HIS   J  41  ? 2.0009 0.6873 1.1924 -0.1623 -0.1935 0.0290  41  HIS   J NE2 
16655 N  N   . THR   J  42  ? 1.8399 0.6216 1.1514 -0.1198 -0.1390 0.0545  42  THR   J N   
16656 C  CA  . THR   J  42  ? 1.8466 0.6206 1.1157 -0.1090 -0.1574 0.0385  42  THR   J CA  
16657 C  C   . THR   J  42  ? 1.8170 0.6232 1.1265 -0.0776 -0.1477 0.0619  42  THR   J C   
16658 O  O   . THR   J  42  ? 1.8531 0.6207 1.1046 -0.0388 -0.1481 0.0927  42  THR   J O   
16659 C  CB  . THR   J  42  ? 1.8335 0.5541 1.1185 -0.1407 -0.1606 0.0528  42  THR   J CB  
16660 O  OG1 . THR   J  42  ? 1.8387 0.5409 1.1205 -0.1360 -0.1464 0.0693  42  THR   J OG1 
16661 C  CG2 . THR   J  42  ? 1.8139 0.5908 1.0901 -0.1446 -0.1483 0.0451  42  THR   J CG2 
16662 N  N   . LEU   J  43  ? 1.7861 0.6225 1.1045 -0.0619 -0.1272 0.0581  43  LEU   J N   
16663 C  CA  . LEU   J  43  ? 1.7510 0.5373 1.0738 -0.0060 -0.1141 0.0876  43  LEU   J CA  
16664 C  C   . LEU   J  43  ? 1.7252 0.5283 1.0269 0.0058  -0.1079 0.0523  43  LEU   J C   
16665 O  O   . LEU   J  43  ? 1.7319 0.5299 0.9821 0.0313  -0.1013 -0.0193 43  LEU   J O   
16666 C  CB  . LEU   J  43  ? 1.7430 0.4903 1.0802 0.0060  -0.1069 0.0973  43  LEU   J CB  
16667 C  CG  . LEU   J  43  ? 1.7437 0.4569 1.0842 0.0163  -0.1037 0.1108  43  LEU   J CG  
16668 C  CD1 . LEU   J  43  ? 1.7529 0.4553 1.1002 0.0214  -0.1117 0.1200  43  LEU   J CD1 
16669 C  CD2 . LEU   J  43  ? 1.7709 0.4721 1.0760 0.0139  -0.0926 0.1137  43  LEU   J CD2 
16670 N  N   . MET   J  44  ? 1.7162 0.5239 1.0377 0.0062  -0.1095 0.0427  44  MET   J N   
16671 C  CA  . MET   J  44  ? 1.7264 0.4452 1.0849 0.0209  -0.1319 0.0383  44  MET   J CA  
16672 C  C   . MET   J  44  ? 1.7256 0.4644 1.0423 0.0084  -0.1482 0.0383  44  MET   J C   
16673 O  O   . MET   J  44  ? 1.7094 0.3113 1.0055 -0.0404 -0.1671 -0.0003 44  MET   J O   
16674 C  CB  . MET   J  44  ? 1.7622 0.4110 1.0805 0.0309  -0.1457 0.0531  44  MET   J CB  
16675 C  CG  . MET   J  44  ? 1.7902 0.3314 1.1439 0.0441  -0.1422 0.0645  44  MET   J CG  
16676 S  SD  . MET   J  44  ? 1.8125 0.2082 1.2188 0.0006  -0.1267 0.0303  44  MET   J SD  
16677 C  CE  . MET   J  44  ? 1.8157 0.2168 1.1890 0.0099  -0.1190 0.0371  44  MET   J CE  
16678 N  N   . SER   J  45  ? 1.7267 0.4702 1.0670 0.0111  -0.1394 0.0587  45  SER   J N   
16679 C  CA  . SER   J  45  ? 1.7522 0.5354 1.1337 -0.0345 -0.1385 0.0928  45  SER   J CA  
16680 C  C   . SER   J  45  ? 1.7346 0.5230 1.1026 -0.0648 -0.1360 0.0389  45  SER   J C   
16681 O  O   . SER   J  45  ? 1.7408 0.4302 1.1289 -0.0815 -0.1229 -0.0233 45  SER   J O   
16682 C  CB  . SER   J  45  ? 1.7817 0.5567 1.1303 0.0146  -0.1269 0.1184  45  SER   J CB  
16683 O  OG  . SER   J  45  ? 1.8125 0.5803 1.1956 0.0535  -0.1044 0.2573  45  SER   J OG  
16684 N  N   . PHE   J  46  ? 1.7481 0.5136 1.1011 -0.0953 -0.1553 0.0111  46  PHE   J N   
16685 C  CA  . PHE   J  46  ? 1.7174 0.4771 1.0738 -0.0858 -0.1993 -0.0094 46  PHE   J CA  
16686 C  C   . PHE   J  46  ? 1.7160 0.4323 1.0938 -0.0455 -0.2239 -0.0150 46  PHE   J C   
16687 O  O   . PHE   J  46  ? 1.7781 0.3783 1.0673 -0.0202 -0.2439 -0.0130 46  PHE   J O   
16688 C  CB  . PHE   J  46  ? 1.7065 0.4882 1.0381 -0.0957 -0.2186 -0.0228 46  PHE   J CB  
16689 C  CG  . PHE   J  46  ? 1.7172 0.4402 1.0666 -0.1046 -0.2419 -0.0213 46  PHE   J CG  
16690 C  CD1 . PHE   J  46  ? 1.7175 0.4770 1.0909 -0.1121 -0.2643 -0.0228 46  PHE   J CD1 
16691 C  CD2 . PHE   J  46  ? 1.7218 0.4333 1.0783 -0.1050 -0.2409 -0.0262 46  PHE   J CD2 
16692 C  CE1 . PHE   J  46  ? 1.7292 0.4590 1.1362 -0.1172 -0.2777 -0.0119 46  PHE   J CE1 
16693 C  CE2 . PHE   J  46  ? 1.7238 0.4768 1.0931 -0.1235 -0.2639 -0.0379 46  PHE   J CE2 
16694 C  CZ  . PHE   J  46  ? 1.7550 0.4424 1.1355 -0.1458 -0.2613 -0.0315 46  PHE   J CZ  
16695 N  N   . ALA   J  47  ? 1.6431 0.3802 1.1149 -0.0640 -0.2258 -0.0238 47  ALA   J N   
16696 C  CA  . ALA   J  47  ? 1.6327 0.3776 1.1544 -0.0841 -0.2312 -0.0657 47  ALA   J CA  
16697 C  C   . ALA   J  47  ? 1.6061 0.2759 1.1459 -0.0888 -0.2218 -0.0961 47  ALA   J C   
16698 O  O   . ALA   J  47  ? 1.5553 0.3807 1.1381 -0.1015 -0.1982 -0.0587 47  ALA   J O   
16699 C  CB  . ALA   J  47  ? 1.6324 0.4006 1.1790 -0.0725 -0.2159 -0.0628 47  ALA   J CB  
16700 N  N   . GLY   J  48  ? 1.5998 0.1936 1.1676 -0.0915 -0.2466 -0.1213 48  GLY   J N   
16701 C  CA  . GLY   J  48  ? 1.5829 0.1977 1.1760 -0.1000 -0.2426 -0.1136 48  GLY   J CA  
16702 C  C   . GLY   J  48  ? 1.5729 0.1991 1.2516 -0.1113 -0.2475 -0.1087 48  GLY   J C   
16703 O  O   . GLY   J  48  ? 1.5837 0.2059 1.2804 -0.1426 -0.2336 -0.1129 48  GLY   J O   
16704 N  N   . GLU   J  49  ? 1.5747 0.2583 1.2464 -0.0895 -0.2374 -0.0984 49  GLU   J N   
16705 C  CA  . GLU   J  49  ? 1.5880 0.3762 1.3315 -0.0842 -0.2129 -0.0367 49  GLU   J CA  
16706 C  C   . GLU   J  49  ? 1.6089 0.4109 1.2727 -0.0830 -0.2355 -0.0593 49  GLU   J C   
16707 O  O   . GLU   J  49  ? 1.5936 0.4310 1.2323 -0.0746 -0.2230 -0.0452 49  GLU   J O   
16708 C  CB  . GLU   J  49  ? 1.6299 0.4899 1.3208 -0.0413 -0.1998 -0.0067 49  GLU   J CB  
16709 C  CG  . GLU   J  49  ? 1.6515 0.6292 1.4334 0.0192  -0.1546 0.0440  49  GLU   J CG  
16710 C  CD  . GLU   J  49  ? 1.7733 0.7007 1.5230 -0.0474 -0.1353 0.0701  49  GLU   J CD  
16711 O  OE1 . GLU   J  49  ? 1.7614 0.9114 1.5854 0.0883  -0.1452 0.0194  49  GLU   J OE1 
16712 O  OE2 . GLU   J  49  ? 1.7669 0.8561 1.5957 0.1715  -0.1137 0.1090  49  GLU   J OE2 
16713 N  N   . ALA   J  50  ? 1.6265 0.3973 1.2850 -0.0971 -0.2516 -0.0203 50  ALA   J N   
16714 C  CA  . ALA   J  50  ? 1.6862 0.4493 1.2833 -0.0843 -0.2858 0.0314  50  ALA   J CA  
16715 C  C   . ALA   J  50  ? 1.6854 0.5388 1.2347 -0.0364 -0.2694 0.0039  50  ALA   J C   
16716 O  O   . ALA   J  50  ? 1.6762 0.6057 1.2381 -0.0169 -0.2773 0.1043  50  ALA   J O   
16717 C  CB  . ALA   J  50  ? 1.6984 0.4547 1.3035 -0.0913 -0.3078 0.0268  50  ALA   J CB  
16718 N  N   . GLY   J  51  ? 1.7190 0.5616 1.2311 -0.0349 -0.2636 0.0198  51  GLY   J N   
16719 C  CA  . GLY   J  51  ? 1.6808 0.5445 1.2481 -0.0426 -0.2576 0.0330  51  GLY   J CA  
16720 C  C   . GLY   J  51  ? 1.6629 0.5248 1.2609 -0.0294 -0.2289 0.0137  51  GLY   J C   
16721 O  O   . GLY   J  51  ? 1.6235 0.4775 1.2830 -0.0384 -0.2366 -0.0271 51  GLY   J O   
16722 N  N   . ASP   J  52  ? 1.6565 0.5771 1.2633 -0.0008 -0.2000 0.0338  52  ASP   J N   
16723 C  CA  . ASP   J  52  ? 1.6516 0.6229 1.2204 -0.0113 -0.1694 0.0287  52  ASP   J CA  
16724 C  C   . ASP   J  52  ? 1.6687 0.5755 1.2213 0.0174  -0.1678 0.0528  52  ASP   J C   
16725 O  O   . ASP   J  52  ? 1.6407 0.5581 1.2058 0.0342  -0.1003 0.1287  52  ASP   J O   
16726 C  CB  . ASP   J  52  ? 1.6589 0.7021 1.1735 -0.0015 -0.1847 0.0319  52  ASP   J CB  
16727 C  CG  . ASP   J  52  ? 1.6792 0.8104 1.1743 -0.0087 -0.1593 -0.0076 52  ASP   J CG  
16728 O  OD1 . ASP   J  52  ? 1.6519 0.8170 1.1714 -0.0013 -0.1656 0.0383  52  ASP   J OD1 
16729 O  OD2 . ASP   J  52  ? 1.6730 0.9429 1.0744 0.0327  -0.1733 -0.0408 52  ASP   J OD2 
16730 N  N   . THR   J  53  ? 1.6813 0.5825 1.2048 -0.0168 -0.2034 0.0540  53  THR   J N   
16731 C  CA  . THR   J  53  ? 1.6483 0.5435 1.2016 -0.0414 -0.2260 0.0373  53  THR   J CA  
16732 C  C   . THR   J  53  ? 1.6153 0.4834 1.2299 -0.0643 -0.2539 -0.0119 53  THR   J C   
16733 O  O   . THR   J  53  ? 1.6265 0.4636 1.2075 -0.0585 -0.2272 0.0010  53  THR   J O   
16734 C  CB  . THR   J  53  ? 1.6756 0.5428 1.2472 -0.0445 -0.2479 0.0212  53  THR   J CB  
16735 O  OG1 . THR   J  53  ? 1.6828 0.5622 1.3655 -0.0663 -0.2441 0.0308  53  THR   J OG1 
16736 C  CG2 . THR   J  53  ? 1.6762 0.5449 1.2182 -0.0382 -0.2542 0.0120  53  THR   J CG2 
16737 N  N   . VAL   J  54  ? 1.6472 0.4444 1.2242 -0.0480 -0.2937 0.0213  54  VAL   J N   
16738 C  CA  . VAL   J  54  ? 1.6417 0.4828 1.2178 -0.0756 -0.2870 0.0738  54  VAL   J CA  
16739 C  C   . VAL   J  54  ? 1.6311 0.5113 1.1430 -0.0436 -0.2525 0.0885  54  VAL   J C   
16740 O  O   . VAL   J  54  ? 1.6863 0.5863 1.1815 -0.0884 -0.1826 0.1175  54  VAL   J O   
16741 C  CB  . VAL   J  54  ? 1.6659 0.5036 1.2603 -0.0932 -0.3149 0.0476  54  VAL   J CB  
16742 C  CG1 . VAL   J  54  ? 1.6555 0.4841 1.2642 -0.1402 -0.3330 0.0574  54  VAL   J CG1 
16743 C  CG2 . VAL   J  54  ? 1.6994 0.5138 1.2687 -0.0635 -0.3133 0.0399  54  VAL   J CG2 
16744 N  N   . GLN   J  55  ? 1.5653 0.4553 1.1485 -0.0276 -0.2568 0.1224  55  GLN   J N   
16745 C  CA  . GLN   J  55  ? 1.5179 0.4292 1.1609 -0.0400 -0.2447 0.1251  55  GLN   J CA  
16746 C  C   . GLN   J  55  ? 1.4878 0.4724 1.1529 -0.0138 -0.2394 0.0923  55  GLN   J C   
16747 O  O   . GLN   J  55  ? 1.4845 0.4826 1.1810 -0.0385 -0.1944 0.0726  55  GLN   J O   
16748 C  CB  . GLN   J  55  ? 1.4810 0.4301 1.1477 -0.0440 -0.2499 0.1089  55  GLN   J CB  
16749 C  CG  . GLN   J  55  ? 1.4773 0.4614 1.1614 -0.0467 -0.2543 0.0986  55  GLN   J CG  
16750 C  CD  . GLN   J  55  ? 1.4361 0.4575 1.1553 -0.0659 -0.2525 0.0680  55  GLN   J CD  
16751 O  OE1 . GLN   J  55  ? 1.4367 0.4909 1.2036 -0.0070 -0.2422 0.0727  55  GLN   J OE1 
16752 N  NE2 . GLN   J  55  ? 1.4056 0.4987 1.1313 -0.0821 -0.2632 0.0572  55  GLN   J NE2 
16753 N  N   . PHE   J  56  ? 1.5291 0.3787 1.1486 -0.0183 -0.2326 0.0574  56  PHE   J N   
16754 C  CA  . PHE   J  56  ? 1.5295 0.3588 1.1181 -0.0021 -0.2403 0.0357  56  PHE   J CA  
16755 C  C   . PHE   J  56  ? 1.5553 0.3872 1.1056 0.0077  -0.2747 0.0588  56  PHE   J C   
16756 O  O   . PHE   J  56  ? 1.5143 0.4426 1.1672 -0.0326 -0.2901 0.1333  56  PHE   J O   
16757 C  CB  . PHE   J  56  ? 1.5550 0.3178 1.0657 0.0057  -0.2040 0.0078  56  PHE   J CB  
16758 C  CG  . PHE   J  56  ? 1.5461 0.2818 1.0251 0.0304  -0.1891 0.0020  56  PHE   J CG  
16759 C  CD1 . PHE   J  56  ? 1.5397 0.2948 0.9737 0.0335  -0.1760 0.0293  56  PHE   J CD1 
16760 C  CD2 . PHE   J  56  ? 1.5700 0.2780 1.0547 0.0349  -0.1712 -0.0107 56  PHE   J CD2 
16761 C  CE1 . PHE   J  56  ? 1.5531 0.2454 0.9669 0.0171  -0.1747 0.0366  56  PHE   J CE1 
16762 C  CE2 . PHE   J  56  ? 1.5793 0.2346 1.0259 0.0281  -0.1808 -0.0182 56  PHE   J CE2 
16763 C  CZ  . PHE   J  56  ? 1.5628 0.2132 0.9896 0.0293  -0.1729 0.0106  56  PHE   J CZ  
16764 N  N   . ALA   J  57  ? 1.5708 0.3729 1.1178 -0.0003 -0.3014 0.0579  57  ALA   J N   
16765 C  CA  . ALA   J  57  ? 1.5912 0.4380 1.1311 -0.0472 -0.2802 0.0514  57  ALA   J CA  
16766 C  C   . ALA   J  57  ? 1.6329 0.4372 1.1482 -0.0533 -0.2832 0.0636  57  ALA   J C   
16767 O  O   . ALA   J  57  ? 1.6009 0.5619 1.1353 -0.0851 -0.2544 0.0794  57  ALA   J O   
16768 C  CB  . ALA   J  57  ? 1.5978 0.4592 1.1547 -0.0203 -0.2933 0.0247  57  ALA   J CB  
16769 N  N   . GLU   J  58  ? 1.6324 0.4106 1.1775 -0.0720 -0.2841 0.0813  58  GLU   J N   
16770 C  CA  . GLU   J  58  ? 1.6961 0.4238 1.2375 -0.0508 -0.2811 0.1177  58  GLU   J CA  
16771 C  C   . GLU   J  58  ? 1.7270 0.3808 1.2084 -0.0256 -0.2611 0.1331  58  GLU   J C   
16772 O  O   . GLU   J  58  ? 1.7446 0.3435 1.3154 -0.0519 -0.2014 0.0828  58  GLU   J O   
16773 C  CB  . GLU   J  58  ? 1.7008 0.4245 1.3061 -0.0703 -0.2830 0.1386  58  GLU   J CB  
16774 C  CG  . GLU   J  58  ? 1.7340 0.4597 1.3277 -0.0937 -0.3008 0.1417  58  GLU   J CG  
16775 C  CD  . GLU   J  58  ? 1.7343 0.5022 1.3958 -0.0672 -0.2537 0.1759  58  GLU   J CD  
16776 O  OE1 . GLU   J  58  ? 1.7307 0.3141 1.4343 -0.0868 -0.2534 0.1960  58  GLU   J OE1 
16777 O  OE2 . GLU   J  58  ? 1.8156 0.6079 1.3934 -0.0961 -0.2807 0.1553  58  GLU   J OE2 
16778 N  N   . TYR   J  59  ? 1.7425 0.3654 1.1963 -0.0092 -0.2597 0.1135  59  TYR   J N   
16779 C  CA  . TYR   J  59  ? 1.7115 0.3250 1.1873 -0.0108 -0.2391 0.1189  59  TYR   J CA  
16780 C  C   . TYR   J  59  ? 1.6998 0.4211 1.1171 -0.0017 -0.2041 0.0922  59  TYR   J C   
16781 O  O   . TYR   J  59  ? 1.6871 0.4591 1.1329 -0.0437 -0.1701 0.0138  59  TYR   J O   
16782 C  CB  . TYR   J  59  ? 1.7361 0.3399 1.1916 0.0121  -0.2617 0.1257  59  TYR   J CB  
16783 C  CG  . TYR   J  59  ? 1.7728 0.3306 1.2048 0.0089  -0.2751 0.1346  59  TYR   J CG  
16784 C  CD1 . TYR   J  59  ? 1.7709 0.3297 1.2280 0.0259  -0.2734 0.1496  59  TYR   J CD1 
16785 C  CD2 . TYR   J  59  ? 1.7474 0.3999 1.2511 0.0195  -0.2648 0.0910  59  TYR   J CD2 
16786 C  CE1 . TYR   J  59  ? 1.7554 0.4326 1.2609 -0.0205 -0.2779 0.1384  59  TYR   J CE1 
16787 C  CE2 . TYR   J  59  ? 1.7386 0.3786 1.2940 -0.0246 -0.2641 0.0980  59  TYR   J CE2 
16788 C  CZ  . TYR   J  59  ? 1.7517 0.3605 1.3153 -0.0170 -0.2591 0.1271  59  TYR   J CZ  
16789 O  OH  . TYR   J  59  ? 1.7401 0.5487 1.3563 -0.0473 -0.2954 0.1245  59  TYR   J OH  
16790 N  N   . ILE   J  60  ? 1.6869 0.3682 1.0256 -0.0393 -0.1915 0.1125  60  ILE   J N   
16791 C  CA  . ILE   J  60  ? 1.6976 0.4294 0.9976 -0.0423 -0.1797 0.1006  60  ILE   J CA  
16792 C  C   . ILE   J  60  ? 1.7146 0.4553 0.9968 0.0008  -0.1675 0.1028  60  ILE   J C   
16793 O  O   . ILE   J  60  ? 1.7024 0.4672 0.9451 -0.0089 -0.1654 0.0654  60  ILE   J O   
16794 C  CB  . ILE   J  60  ? 1.6943 0.4119 0.9508 -0.0497 -0.1838 0.1356  60  ILE   J CB  
16795 C  CG1 . ILE   J  60  ? 1.6871 0.4598 0.9409 -0.0579 -0.1834 0.1479  60  ILE   J CG1 
16796 C  CG2 . ILE   J  60  ? 1.6894 0.4425 0.9647 -0.0707 -0.1904 0.1247  60  ILE   J CG2 
16797 C  CD1 . ILE   J  60  ? 1.6748 0.4329 0.9453 -0.0724 -0.1856 0.1684  60  ILE   J CD1 
16798 N  N   . GLN   J  61  ? 1.6909 0.5106 1.0361 0.0049  -0.1860 0.1279  61  GLN   J N   
16799 C  CA  . GLN   J  61  ? 1.7372 0.5162 1.0732 -0.0100 -0.1470 0.1810  61  GLN   J CA  
16800 C  C   . GLN   J  61  ? 1.7257 0.5033 1.1359 -0.0340 -0.1257 0.1764  61  GLN   J C   
16801 O  O   . GLN   J  61  ? 1.7482 0.5224 1.2376 -0.0629 -0.0742 0.1742  61  GLN   J O   
16802 C  CB  . GLN   J  61  ? 1.7712 0.5383 1.0069 -0.0063 -0.1771 0.2180  61  GLN   J CB  
16803 C  CG  . GLN   J  61  ? 1.8212 0.5682 1.0345 0.0153  -0.1783 0.2540  61  GLN   J CG  
16804 C  CD  . GLN   J  61  ? 1.8369 0.6103 1.0325 0.0351  -0.2359 0.3112  61  GLN   J CD  
16805 O  OE1 . GLN   J  61  ? 1.8404 0.6217 0.9964 0.1547  -0.1829 0.3435  61  GLN   J OE1 
16806 N  NE2 . GLN   J  61  ? 1.8923 0.7084 1.0110 0.0336  -0.1869 0.4190  61  GLN   J NE2 
16807 N  N   . ALA   J  62  ? 1.6919 0.4404 1.1617 -0.0543 -0.1295 0.1449  62  ALA   J N   
16808 C  CA  . ALA   J  62  ? 1.7424 0.4243 1.1772 -0.0900 -0.1419 0.1035  62  ALA   J CA  
16809 C  C   . ALA   J  62  ? 1.7086 0.4850 1.2113 -0.0515 -0.1795 0.0792  62  ALA   J C   
16810 O  O   . ALA   J  62  ? 1.8223 0.4905 1.3348 -0.0851 -0.1452 0.0884  62  ALA   J O   
16811 C  CB  . ALA   J  62  ? 1.7411 0.3667 1.1573 -0.1000 -0.1438 0.0569  62  ALA   J CB  
16812 N  N   . ASN   J  63  ? 1.7007 0.4486 1.2206 -0.0426 -0.1746 0.0802  63  ASN   J N   
16813 C  CA  . ASN   J  63  ? 1.7141 0.4609 1.2289 -0.0350 -0.1970 0.0635  63  ASN   J CA  
16814 C  C   . ASN   J  63  ? 1.6820 0.5425 1.1867 -0.0224 -0.2195 0.0599  63  ASN   J C   
16815 O  O   . ASN   J  63  ? 1.6437 0.5877 1.2145 -0.0531 -0.2481 0.0437  63  ASN   J O   
16816 C  CB  . ASN   J  63  ? 1.7319 0.4194 1.2642 -0.0359 -0.1996 0.0651  63  ASN   J CB  
16817 C  CG  . ASN   J  63  ? 1.7584 0.4050 1.2961 -0.0370 -0.1701 0.0535  63  ASN   J CG  
16818 O  OD1 . ASN   J  63  ? 1.7907 0.4497 1.3059 -0.0924 -0.1863 0.0615  63  ASN   J OD1 
16819 N  ND2 . ASN   J  63  ? 1.8275 0.4347 1.3445 0.0187  -0.1771 0.0060  63  ASN   J ND2 
16820 N  N   . ILE   J  64  ? 1.6569 0.5429 1.1515 -0.0356 -0.2196 0.0752  64  ILE   J N   
16821 C  CA  . ILE   J  64  ? 1.6577 0.5752 1.1702 -0.0425 -0.2052 0.0696  64  ILE   J CA  
16822 C  C   . ILE   J  64  ? 1.6506 0.5207 1.2332 -0.0429 -0.1829 0.0662  64  ILE   J C   
16823 O  O   . ILE   J  64  ? 1.7033 0.5257 1.2910 -0.0782 -0.1512 0.0317  64  ILE   J O   
16824 C  CB  . ILE   J  64  ? 1.6458 0.5762 1.1569 -0.0141 -0.2221 0.0894  64  ILE   J CB  
16825 C  CG1 . ILE   J  64  ? 1.6126 0.6148 1.1366 -0.0046 -0.2397 0.0760  64  ILE   J CG1 
16826 C  CG2 . ILE   J  64  ? 1.6666 0.6052 1.1827 -0.0312 -0.2147 0.1153  64  ILE   J CG2 
16827 C  CD1 . ILE   J  64  ? 1.6119 0.6493 1.1224 -0.0007 -0.2336 0.0586  64  ILE   J CD1 
16828 N  N   . GLN   J  65  ? 1.6498 0.4936 1.2459 -0.0194 -0.1982 0.0912  65  GLN   J N   
16829 C  CA  . GLN   J  65  ? 1.6967 0.5266 1.2248 -0.0379 -0.2090 0.1356  65  GLN   J CA  
16830 C  C   . GLN   J  65  ? 1.6945 0.5213 1.2257 -0.0534 -0.1810 0.1394  65  GLN   J C   
16831 O  O   . GLN   J  65  ? 1.7360 0.4699 1.3517 -0.0950 -0.1274 0.1227  65  GLN   J O   
16832 C  CB  . GLN   J  65  ? 1.7120 0.5447 1.1573 -0.0182 -0.2606 0.1395  65  GLN   J CB  
16833 C  CG  . GLN   J  65  ? 1.7271 0.5730 1.0925 0.0109  -0.2833 0.1564  65  GLN   J CG  
16834 C  CD  . GLN   J  65  ? 1.7363 0.6167 1.0861 0.0043  -0.3051 0.1650  65  GLN   J CD  
16835 O  OE1 . GLN   J  65  ? 1.7561 0.6302 1.0619 0.0061  -0.3066 0.1469  65  GLN   J OE1 
16836 N  NE2 . GLN   J  65  ? 1.7609 0.6107 1.0839 0.0399  -0.2858 0.1708  65  GLN   J NE2 
16837 N  N   . LEU   J  66  ? 1.6527 0.4407 1.2206 -0.0485 -0.1801 0.1282  66  LEU   J N   
16838 C  CA  . LEU   J  66  ? 1.6169 0.4030 1.2276 -0.0537 -0.1705 0.1451  66  LEU   J CA  
16839 C  C   . LEU   J  66  ? 1.6048 0.4063 1.2734 -0.0466 -0.1801 0.0920  66  LEU   J C   
16840 O  O   . LEU   J  66  ? 1.6431 0.3975 1.3790 -0.0545 -0.1618 0.0073  66  LEU   J O   
16841 C  CB  . LEU   J  66  ? 1.6002 0.3748 1.2018 -0.0457 -0.1857 0.1263  66  LEU   J CB  
16842 C  CG  . LEU   J  66  ? 1.6000 0.3521 1.2102 -0.0724 -0.1910 0.1329  66  LEU   J CG  
16843 C  CD1 . LEU   J  66  ? 1.6194 0.3656 1.2134 -0.0640 -0.2011 0.1335  66  LEU   J CD1 
16844 C  CD2 . LEU   J  66  ? 1.5761 0.3945 1.2031 -0.0648 -0.1733 0.1104  66  LEU   J CD2 
16845 N  N   . TYR   J  67  ? 1.6320 0.3795 1.2206 -0.0367 -0.1920 0.0933  67  TYR   J N   
16846 C  CA  . TYR   J  67  ? 1.6351 0.3632 1.1955 -0.0338 -0.2061 0.0635  67  TYR   J CA  
16847 C  C   . TYR   J  67  ? 1.6560 0.3899 1.2227 -0.0021 -0.2344 0.1091  67  TYR   J C   
16848 O  O   . TYR   J  67  ? 1.6295 0.4251 1.2050 -0.0355 -0.2587 0.0607  67  TYR   J O   
16849 C  CB  . TYR   J  67  ? 1.6224 0.3336 1.1450 -0.0548 -0.1875 0.0668  67  TYR   J CB  
16850 C  CG  . TYR   J  67  ? 1.6446 0.2690 1.1507 -0.0856 -0.1737 0.0323  67  TYR   J CG  
16851 C  CD1 . TYR   J  67  ? 1.6559 0.3163 1.1825 -0.1267 -0.1607 0.0227  67  TYR   J CD1 
16852 C  CD2 . TYR   J  67  ? 1.6233 0.2206 1.1370 -0.0793 -0.1496 0.0309  67  TYR   J CD2 
16853 C  CE1 . TYR   J  67  ? 1.6465 0.3822 1.2269 -0.1250 -0.1502 0.0194  67  TYR   J CE1 
16854 C  CE2 . TYR   J  67  ? 1.6172 0.2672 1.1938 -0.0825 -0.1359 0.0397  67  TYR   J CE2 
16855 C  CZ  . TYR   J  67  ? 1.6424 0.3559 1.2084 -0.1091 -0.1230 0.0432  67  TYR   J CZ  
16856 O  OH  . TYR   J  67  ? 1.6536 0.4259 1.2943 -0.1453 -0.0987 0.0042  67  TYR   J OH  
16857 N  N   . SER   J  68  ? 1.6795 0.4792 1.1707 0.0317  -0.2971 0.1531  68  SER   J N   
16858 C  CA  . SER   J  68  ? 1.7314 0.5893 1.1867 0.0034  -0.3048 0.1938  68  SER   J CA  
16859 C  C   . SER   J  68  ? 1.7497 0.5912 1.2218 -0.0044 -0.3235 0.2406  68  SER   J C   
16860 O  O   . SER   J  68  ? 1.7806 0.5587 1.1878 0.0028  -0.3809 0.2862  68  SER   J O   
16861 C  CB  . SER   J  68  ? 1.7642 0.6334 1.1867 -0.0206 -0.3164 0.1916  68  SER   J CB  
16862 O  OG  . SER   J  68  ? 1.7259 0.7380 1.1763 0.0615  -0.3968 0.2667  68  SER   J OG  
16863 N  N   . ILE   J  69  ? 1.7395 0.6585 1.2794 0.0350  -0.3487 0.2084  69  ILE   J N   
16864 C  CA  . ILE   J  69  ? 1.8319 0.6060 1.3802 0.0295  -0.3434 0.1569  69  ILE   J CA  
16865 C  C   . ILE   J  69  ? 1.7820 0.6247 1.3834 -0.0027 -0.3094 0.1634  69  ILE   J C   
16866 O  O   . ILE   J  69  ? 1.8466 0.6355 1.5611 -0.0327 -0.2968 0.1973  69  ILE   J O   
16867 C  CB  . ILE   J  69  ? 1.8221 0.6901 1.4772 0.0497  -0.3607 0.0994  69  ILE   J CB  
16868 C  CG1 . ILE   J  69  ? 1.8722 0.8490 1.5255 0.0504  -0.4323 0.0976  69  ILE   J CG1 
16869 C  CG2 . ILE   J  69  ? 1.8428 0.7060 1.5227 0.0564  -0.3601 0.0723  69  ILE   J CG2 
16870 C  CD1 . ILE   J  69  ? 1.8853 0.8495 1.5835 0.0660  -0.4416 0.1327  69  ILE   J CD1 
16871 N  N   . ARG   J  70  ? 1.7283 0.4815 1.3454 -0.0202 -0.2571 0.1540  70  ARG   J N   
16872 C  CA  . ARG   J  70  ? 1.7636 0.4819 1.3600 -0.0279 -0.2210 0.1131  70  ARG   J CA  
16873 C  C   . ARG   J  70  ? 1.7720 0.5538 1.4015 -0.0433 -0.2036 0.0965  70  ARG   J C   
16874 O  O   . ARG   J  70  ? 1.8770 0.5697 1.4720 -0.0769 -0.2090 0.0498  70  ARG   J O   
16875 C  CB  . ARG   J  70  ? 1.7261 0.4498 1.2953 -0.0405 -0.2183 0.0419  70  ARG   J CB  
16876 C  CG  . ARG   J  70  ? 1.7632 0.5085 1.3054 -0.0626 -0.2197 0.0182  70  ARG   J CG  
16877 C  CD  . ARG   J  70  ? 1.7823 0.5452 1.2549 -0.0608 -0.2081 -0.0193 70  ARG   J CD  
16878 N  NE  . ARG   J  70  ? 1.7909 0.5334 1.1910 -0.0511 -0.1916 -0.0642 70  ARG   J NE  
16879 C  CZ  . ARG   J  70  ? 1.8102 0.5026 1.0949 0.0048  -0.1972 -0.1101 70  ARG   J CZ  
16880 N  NH1 . ARG   J  70  ? 1.8221 0.5267 1.0506 0.0226  -0.2016 -0.1108 70  ARG   J NH1 
16881 N  NH2 . ARG   J  70  ? 1.8074 0.5102 1.0532 0.0219  -0.1921 -0.1283 70  ARG   J NH2 
16882 N  N   . GLU   J  71  ? 1.7961 0.4834 1.4563 -0.0425 -0.2046 0.1146  71  GLU   J N   
16883 C  CA  . GLU   J  71  ? 1.8278 0.5112 1.4929 -0.1034 -0.1901 0.0836  71  GLU   J CA  
16884 C  C   . GLU   J  71  ? 1.7979 0.3875 1.5080 -0.0840 -0.1669 0.1052  71  GLU   J C   
16885 O  O   . GLU   J  71  ? 1.7634 0.2423 1.5494 -0.0365 -0.1760 0.1226  71  GLU   J O   
16886 C  CB  . GLU   J  71  ? 1.7565 0.5776 1.4567 -0.1135 -0.1812 0.0703  71  GLU   J CB  
16887 C  CG  . GLU   J  71  ? 1.7772 0.6558 1.4466 -0.1567 -0.1709 0.0616  71  GLU   J CG  
16888 C  CD  . GLU   J  71  ? 1.8086 0.7761 1.4195 -0.1580 -0.1443 0.0105  71  GLU   J CD  
16889 O  OE1 . GLU   J  71  ? 1.8242 0.9066 1.4201 -0.0836 -0.1275 0.0195  71  GLU   J OE1 
16890 O  OE2 . GLU   J  71  ? 1.8005 0.8411 1.4993 -0.1921 -0.0834 0.0189  71  GLU   J OE2 
16891 N  N   . ASP   J  72  ? 1.8456 0.4477 1.5495 -0.0808 -0.2032 0.0544  72  ASP   J N   
16892 C  CA  . ASP   J  72  ? 1.8794 0.4763 1.5554 -0.0902 -0.2161 0.0692  72  ASP   J CA  
16893 C  C   . ASP   J  72  ? 1.8670 0.5876 1.5839 -0.0783 -0.1808 0.0712  72  ASP   J C   
16894 O  O   . ASP   J  72  ? 1.8418 0.4632 1.6479 -0.0689 -0.1881 0.0860  72  ASP   J O   
16895 C  CB  . ASP   J  72  ? 1.9305 0.4817 1.5838 -0.1133 -0.2663 0.0863  72  ASP   J CB  
16896 C  CG  . ASP   J  72  ? 1.9729 0.4787 1.6083 -0.1161 -0.3322 0.0770  72  ASP   J CG  
16897 O  OD1 . ASP   J  72  ? 2.0243 0.2915 1.6176 -0.1132 -0.3249 0.1429  72  ASP   J OD1 
16898 O  OD2 . ASP   J  72  ? 1.9957 0.6315 1.6394 -0.1507 -0.3012 0.1188  72  ASP   J OD2 
16899 N  N   . TYR   J  73  ? 1.8642 0.6148 1.5468 -0.0535 -0.1729 0.0920  73  TYR   J N   
16900 C  CA  . TYR   J  73  ? 1.8708 0.6714 1.5030 -0.0323 -0.1785 0.0911  73  TYR   J CA  
16901 C  C   . TYR   J  73  ? 1.8943 0.6863 1.4458 -0.0471 -0.2111 0.0961  73  TYR   J C   
16902 O  O   . TYR   J  73  ? 1.9494 0.8281 1.2934 -0.0127 -0.2597 0.1108  73  TYR   J O   
16903 C  CB  . TYR   J  73  ? 1.8190 0.6588 1.5090 0.0037  -0.1584 0.0735  73  TYR   J CB  
16904 C  CG  . TYR   J  73  ? 1.8578 0.6462 1.5638 0.0718  -0.1470 0.0195  73  TYR   J CG  
16905 C  CD1 . TYR   J  73  ? 1.8310 0.7645 1.5784 0.1193  -0.0928 -0.0028 73  TYR   J CD1 
16906 C  CD2 . TYR   J  73  ? 1.8117 0.6118 1.5287 0.0915  -0.0996 -0.0177 73  TYR   J CD2 
16907 C  CE1 . TYR   J  73  ? 1.8315 0.8221 1.6602 0.1357  -0.0941 -0.0372 73  TYR   J CE1 
16908 C  CE2 . TYR   J  73  ? 1.7911 0.6981 1.5894 0.0767  -0.1029 -0.0265 73  TYR   J CE2 
16909 C  CZ  . TYR   J  73  ? 1.7986 0.7772 1.6238 0.0838  -0.0719 -0.0183 73  TYR   J CZ  
16910 O  OH  . TYR   J  73  ? 1.7798 0.9379 1.7489 0.1075  -0.0978 -0.0816 73  TYR   J OH  
16911 N  N   . GLU   J  74  ? 1.8986 0.7455 1.4284 -0.0240 -0.2057 0.0954  74  GLU   J N   
16912 C  CA  . GLU   J  74  ? 1.9223 0.7483 1.2824 -0.0825 -0.1830 0.1349  74  GLU   J CA  
16913 C  C   . GLU   J  74  ? 1.8716 0.6256 1.2391 -0.1308 -0.1413 0.1409  74  GLU   J C   
16914 O  O   . GLU   J  74  ? 1.9224 0.6421 1.1579 -0.1007 -0.0692 0.1876  74  GLU   J O   
16915 C  CB  . GLU   J  74  ? 2.0035 0.7776 1.2911 -0.1119 -0.2058 0.1201  74  GLU   J CB  
16916 C  CG  . GLU   J  74  ? 2.0625 0.7928 1.2643 -0.1333 -0.1992 0.1683  74  GLU   J CG  
16917 C  CD  . GLU   J  74  ? 2.1408 0.8802 1.2708 -0.1442 -0.2155 0.1428  74  GLU   J CD  
16918 O  OE1 . GLU   J  74  ? 2.1308 0.8815 1.1552 -0.1349 -0.2544 0.0190  74  GLU   J OE1 
16919 O  OE2 . GLU   J  74  ? 2.2626 0.9835 1.2483 -0.1358 -0.1786 0.1533  74  GLU   J OE2 
16920 N  N   . LEU   J  75  ? 1.8294 0.5835 1.2150 -0.1498 -0.1626 0.1033  75  LEU   J N   
16921 C  CA  . LEU   J  75  ? 1.8156 0.5206 1.2233 -0.1384 -0.1359 0.1011  75  LEU   J CA  
16922 C  C   . LEU   J  75  ? 1.7990 0.4739 1.2493 -0.1207 -0.1484 0.1330  75  LEU   J C   
16923 O  O   . LEU   J  75  ? 1.7697 0.5028 1.2057 -0.0400 -0.2287 0.1965  75  LEU   J O   
16924 C  CB  . LEU   J  75  ? 1.8191 0.4964 1.2347 -0.1235 -0.1261 0.1109  75  LEU   J CB  
16925 C  CG  . LEU   J  75  ? 1.8001 0.5641 1.2227 -0.1112 -0.0982 0.1083  75  LEU   J CG  
16926 C  CD1 . LEU   J  75  ? 1.7922 0.5990 1.2164 -0.1506 -0.0908 0.1193  75  LEU   J CD1 
16927 C  CD2 . LEU   J  75  ? 1.8068 0.5797 1.2409 -0.0898 -0.0802 0.0828  75  LEU   J CD2 
16928 N  N   . SER   J  76  ? 1.7750 0.4991 1.2936 -0.1978 -0.1513 0.1413  76  SER   J N   
16929 C  CA  . SER   J  76  ? 1.8060 0.5956 1.3027 -0.1767 -0.1094 0.1146  76  SER   J CA  
16930 C  C   . SER   J  76  ? 1.8680 0.5681 1.2607 -0.1237 -0.0775 0.1305  76  SER   J C   
16931 O  O   . SER   J  76  ? 1.8524 0.7014 1.2524 -0.0424 -0.0662 0.1147  76  SER   J O   
16932 C  CB  . SER   J  76  ? 1.7961 0.5955 1.3303 -0.2485 -0.0838 0.1420  76  SER   J CB  
16933 O  OG  . SER   J  76  ? 1.7473 0.5535 1.3426 -0.3049 -0.0761 0.1696  76  SER   J OG  
16934 N  N   . PRO   J  77  ? 1.9449 0.5538 1.2806 -0.0632 -0.0680 0.1371  77  PRO   J N   
16935 C  CA  . PRO   J  77  ? 1.8989 0.5327 1.2721 -0.0167 -0.0689 0.1434  77  PRO   J CA  
16936 C  C   . PRO   J  77  ? 1.7785 0.3996 1.2988 -0.0200 -0.0494 0.1574  77  PRO   J C   
16937 O  O   . PRO   J  77  ? 1.7723 0.3790 1.2693 0.0487  -0.0571 0.2164  77  PRO   J O   
16938 C  CB  . PRO   J  77  ? 1.9424 0.6039 1.2744 -0.0104 -0.0392 0.1276  77  PRO   J CB  
16939 C  CG  . PRO   J  77  ? 1.9886 0.6055 1.2585 -0.0254 -0.0165 0.1109  77  PRO   J CG  
16940 C  CD  . PRO   J  77  ? 1.9791 0.5995 1.3073 -0.0548 -0.0166 0.1222  77  PRO   J CD  
16941 N  N   . GLN   J  78  ? 1.7688 0.3369 1.3408 0.0241  -0.0908 0.1046  78  GLN   J N   
16942 C  CA  . GLN   J  78  ? 1.7085 0.3646 1.3191 0.0214  -0.0654 0.0878  78  GLN   J CA  
16943 C  C   . GLN   J  78  ? 1.6655 0.3601 1.3060 0.0135  -0.0592 0.1132  78  GLN   J C   
16944 O  O   . GLN   J  78  ? 1.6078 0.1930 1.3462 0.0546  -0.0331 0.0610  78  GLN   J O   
16945 C  CB  . GLN   J  78  ? 1.7255 0.4332 1.3780 -0.0123 -0.0530 0.0560  78  GLN   J CB  
16946 C  CG  . GLN   J  78  ? 1.7089 0.4952 1.3661 -0.0591 -0.0680 0.0614  78  GLN   J CG  
16947 C  CD  . GLN   J  78  ? 1.7038 0.4624 1.3660 -0.0992 -0.0626 0.0632  78  GLN   J CD  
16948 O  OE1 . GLN   J  78  ? 1.6905 0.5169 1.3486 -0.1366 -0.0649 0.0741  78  GLN   J OE1 
16949 N  NE2 . GLN   J  78  ? 1.7187 0.4750 1.3966 -0.0979 -0.0802 0.0312  78  GLN   J NE2 
16950 N  N   . ALA   J  79  ? 1.6466 0.3786 1.3085 0.0394  -0.0726 0.1186  79  ALA   J N   
16951 C  CA  . ALA   J  79  ? 1.6469 0.4310 1.2702 0.0109  -0.0916 0.0932  79  ALA   J CA  
16952 C  C   . ALA   J  79  ? 1.6627 0.4144 1.1914 0.0025  -0.1156 0.1269  79  ALA   J C   
16953 O  O   . ALA   J  79  ? 1.6903 0.3646 1.1535 0.0212  -0.1597 0.1095  79  ALA   J O   
16954 C  CB  . ALA   J  79  ? 1.6528 0.4107 1.3130 -0.0325 -0.0895 0.0768  79  ALA   J CB  
16955 N  N   . VAL   J  80  ? 1.7205 0.4574 1.2137 -0.0009 -0.1425 0.1031  80  VAL   J N   
16956 C  CA  . VAL   J  80  ? 1.7107 0.4707 1.1617 0.0056  -0.1644 0.0482  80  VAL   J CA  
16957 C  C   . VAL   J  80  ? 1.7051 0.4733 1.1436 0.0239  -0.1278 0.0442  80  VAL   J C   
16958 O  O   . VAL   J  80  ? 1.6886 0.4233 1.1600 0.0085  -0.1012 -0.0173 80  VAL   J O   
16959 C  CB  . VAL   J  80  ? 1.7554 0.4614 1.1687 -0.0051 -0.1778 -0.0155 80  VAL   J CB  
16960 C  CG1 . VAL   J  80  ? 1.7259 0.4308 1.1070 0.0179  -0.2088 -0.0341 80  VAL   J CG1 
16961 C  CG2 . VAL   J  80  ? 1.7857 0.4823 1.1672 -0.0191 -0.1896 0.0084  80  VAL   J CG2 
16962 N  N   . SER   J  81  ? 1.6801 0.5476 1.1650 0.0664  -0.1430 0.0846  81  SER   J N   
16963 C  CA  . SER   J  81  ? 1.6616 0.6292 1.1052 0.0244  -0.1451 0.1892  81  SER   J CA  
16964 C  C   . SER   J  81  ? 1.6442 0.5135 1.0914 0.0143  -0.1404 0.2138  81  SER   J C   
16965 O  O   . SER   J  81  ? 1.7091 0.5309 1.1139 0.0198  -0.1255 0.2390  81  SER   J O   
16966 C  CB  . SER   J  81  ? 1.6433 0.6739 1.1845 0.0494  -0.1302 0.2160  81  SER   J CB  
16967 O  OG  . SER   J  81  ? 1.6320 0.7950 1.2773 0.0491  -0.1625 0.2366  81  SER   J OG  
16968 N  N   . SER   J  82  ? 1.6166 0.5119 0.9997 0.0474  -0.1681 0.1974  82  SER   J N   
16969 C  CA  . SER   J  82  ? 1.5833 0.5023 1.0068 0.0652  -0.1783 0.1887  82  SER   J CA  
16970 C  C   . SER   J  82  ? 1.5746 0.4248 0.9661 0.0225  -0.1897 0.1533  82  SER   J C   
16971 O  O   . SER   J  82  ? 1.5535 0.3253 0.9536 -0.0129 -0.1645 0.1118  82  SER   J O   
16972 C  CB  . SER   J  82  ? 1.5665 0.5059 0.9948 0.0825  -0.2068 0.1909  82  SER   J CB  
16973 O  OG  . SER   J  82  ? 1.5983 0.5104 1.0043 0.1419  -0.2135 0.2027  82  SER   J OG  
16974 N  N   . PHE   J  83  ? 1.5453 0.4509 1.0144 0.0336  -0.2101 0.1170  83  PHE   J N   
16975 C  CA  . PHE   J  83  ? 1.5487 0.4850 1.0214 0.0027  -0.2102 0.0726  83  PHE   J CA  
16976 C  C   . PHE   J  83  ? 1.5978 0.4710 1.0353 0.0034  -0.1929 0.0978  83  PHE   J C   
16977 O  O   . PHE   J  83  ? 1.5826 0.4031 0.9994 -0.0276 -0.2411 0.0972  83  PHE   J O   
16978 C  CB  . PHE   J  83  ? 1.5294 0.4997 1.0230 0.0139  -0.2563 0.0327  83  PHE   J CB  
16979 C  CG  . PHE   J  83  ? 1.5012 0.5078 0.9719 0.0304  -0.3119 0.0016  83  PHE   J CG  
16980 C  CD1 . PHE   J  83  ? 1.4955 0.6069 0.9276 0.0484  -0.3164 0.0015  83  PHE   J CD1 
16981 C  CD2 . PHE   J  83  ? 1.5025 0.5064 1.0125 0.0116  -0.3048 -0.0172 83  PHE   J CD2 
16982 C  CE1 . PHE   J  83  ? 1.4916 0.6293 0.8782 0.0290  -0.3242 -0.0202 83  PHE   J CE1 
16983 C  CE2 . PHE   J  83  ? 1.5109 0.5302 0.9865 -0.0054 -0.2954 -0.0471 83  PHE   J CE2 
16984 C  CZ  . PHE   J  83  ? 1.4993 0.5753 0.9265 -0.0057 -0.3132 -0.0245 83  PHE   J CZ  
16985 N  N   . VAL   J  84  ? 1.6373 0.4618 1.0867 0.0382  -0.1772 0.0629  84  VAL   J N   
16986 C  CA  . VAL   J  84  ? 1.6292 0.4767 1.1275 0.0390  -0.1558 0.0656  84  VAL   J CA  
16987 C  C   . VAL   J  84  ? 1.6173 0.4636 1.1711 0.0518  -0.1386 0.0793  84  VAL   J C   
16988 O  O   . VAL   J  84  ? 1.6568 0.3860 1.2765 0.0505  -0.0847 0.0726  84  VAL   J O   
16989 C  CB  . VAL   J  84  ? 1.6728 0.4965 1.1443 0.0597  -0.1496 0.0386  84  VAL   J CB  
16990 C  CG1 . VAL   J  84  ? 1.6697 0.4475 1.1262 0.1128  -0.1527 0.0761  84  VAL   J CG1 
16991 C  CG2 . VAL   J  84  ? 1.7028 0.5109 1.1654 0.0697  -0.1579 0.0431  84  VAL   J CG2 
16992 N  N   . ARG   J  85  ? 1.6033 0.5268 1.1643 0.0135  -0.1336 0.0544  85  ARG   J N   
16993 C  CA  . ARG   J  85  ? 1.6135 0.5300 1.1125 -0.0089 -0.1513 0.0375  85  ARG   J CA  
16994 C  C   . ARG   J  85  ? 1.5894 0.5159 1.0634 -0.0305 -0.1644 0.0959  85  ARG   J C   
16995 O  O   . ARG   J  85  ? 1.5925 0.5143 0.9909 -0.0637 -0.1925 0.0630  85  ARG   J O   
16996 C  CB  . ARG   J  85  ? 1.6193 0.5701 1.1439 0.0108  -0.1545 0.0256  85  ARG   J CB  
16997 C  CG  . ARG   J  85  ? 1.6672 0.5461 1.1424 -0.0126 -0.1438 0.0457  85  ARG   J CG  
16998 C  CD  . ARG   J  85  ? 1.6684 0.5805 1.1335 0.0085  -0.1524 0.0449  85  ARG   J CD  
16999 N  NE  . ARG   J  85  ? 1.7127 0.5995 1.1025 0.0391  -0.1285 0.0561  85  ARG   J NE  
17000 C  CZ  . ARG   J  85  ? 1.7140 0.4970 1.1521 0.0513  -0.1446 0.1077  85  ARG   J CZ  
17001 N  NH1 . ARG   J  85  ? 1.7034 0.5085 1.1680 0.0165  -0.1390 0.1087  85  ARG   J NH1 
17002 N  NH2 . ARG   J  85  ? 1.7333 0.5237 1.0943 0.0554  -0.1724 0.1397  85  ARG   J NH2 
17003 N  N   . GLN   J  86  ? 1.6184 0.5223 1.0906 0.0013  -0.1660 0.0613  86  GLN   J N   
17004 C  CA  . GLN   J  86  ? 1.6360 0.5031 1.0888 0.0198  -0.1751 0.0658  86  GLN   J CA  
17005 C  C   . GLN   J  86  ? 1.6562 0.3787 1.0268 0.0117  -0.1607 0.0960  86  GLN   J C   
17006 O  O   . GLN   J  86  ? 1.6595 0.2239 1.0303 0.0824  -0.1970 0.1449  86  GLN   J O   
17007 C  CB  . GLN   J  86  ? 1.6701 0.5321 1.1913 -0.0202 -0.1802 0.0274  86  GLN   J CB  
17008 C  CG  . GLN   J  86  ? 1.6893 0.6157 1.2097 -0.0102 -0.1874 -0.0028 86  GLN   J CG  
17009 C  CD  . GLN   J  86  ? 1.6938 0.6173 1.3071 -0.0027 -0.1676 -0.0501 86  GLN   J CD  
17010 O  OE1 . GLN   J  86  ? 1.6090 0.7079 1.3106 0.0186  -0.1933 -0.0686 86  GLN   J OE1 
17011 N  NE2 . GLN   J  86  ? 1.6776 0.7087 1.3403 -0.0175 -0.1662 -0.0458 86  GLN   J NE2 
17012 N  N   . GLU   J  87  ? 1.6704 0.4378 1.0587 -0.0175 -0.1857 0.0579  87  GLU   J N   
17013 C  CA  . GLU   J  87  ? 1.6887 0.4681 1.0816 -0.0549 -0.1650 0.0339  87  GLU   J CA  
17014 C  C   . GLU   J  87  ? 1.6387 0.4855 1.0236 -0.0867 -0.1713 0.0346  87  GLU   J C   
17015 O  O   . GLU   J  87  ? 1.6249 0.4472 0.9206 -0.1058 -0.2393 0.0413  87  GLU   J O   
17016 C  CB  . GLU   J  87  ? 1.7233 0.5649 1.0855 -0.0494 -0.1892 0.0162  87  GLU   J CB  
17017 C  CG  . GLU   J  87  ? 1.8051 0.5623 1.1949 -0.0524 -0.1649 -0.0150 87  GLU   J CG  
17018 C  CD  . GLU   J  87  ? 1.8309 0.6089 1.2312 -0.0824 -0.1182 -0.0328 87  GLU   J CD  
17019 O  OE1 . GLU   J  87  ? 1.8928 0.6371 1.2353 -0.0988 -0.0528 0.1103  87  GLU   J OE1 
17020 O  OE2 . GLU   J  87  ? 1.9545 0.6426 1.3638 -0.1168 -0.1517 -0.0996 87  GLU   J OE2 
17021 N  N   . LEU   J  88  ? 1.6333 0.4723 1.0638 -0.0941 -0.1746 0.0217  88  LEU   J N   
17022 C  CA  . LEU   J  88  ? 1.6245 0.4759 1.0784 -0.0873 -0.1591 0.0361  88  LEU   J CA  
17023 C  C   . LEU   J  88  ? 1.6399 0.4597 1.0772 -0.0853 -0.1523 0.0564  88  LEU   J C   
17024 O  O   . LEU   J  88  ? 1.6672 0.4377 1.1054 -0.0565 -0.1372 0.0730  88  LEU   J O   
17025 C  CB  . LEU   J  88  ? 1.6087 0.4182 1.1117 -0.1142 -0.1636 0.0214  88  LEU   J CB  
17026 C  CG  . LEU   J  88  ? 1.6011 0.3597 1.1246 -0.1457 -0.1675 -0.0056 88  LEU   J CG  
17027 C  CD1 . LEU   J  88  ? 1.5828 0.3240 1.1043 -0.1747 -0.1777 -0.0023 88  LEU   J CD1 
17028 C  CD2 . LEU   J  88  ? 1.5952 0.3611 1.1347 -0.1391 -0.1681 -0.0046 88  LEU   J CD2 
17029 N  N   . ALA   J  89  ? 1.6255 0.5139 1.0731 -0.0823 -0.1503 0.0669  89  ALA   J N   
17030 C  CA  . ALA   J  89  ? 1.6614 0.5542 1.0975 -0.0320 -0.1570 0.1442  89  ALA   J CA  
17031 C  C   . ALA   J  89  ? 1.6524 0.6337 1.0945 -0.0515 -0.1292 0.1753  89  ALA   J C   
17032 O  O   . ALA   J  89  ? 1.6744 0.5041 1.1369 -0.1110 -0.0968 0.1827  89  ALA   J O   
17033 C  CB  . ALA   J  89  ? 1.6310 0.5855 1.0737 -0.0059 -0.1673 0.1331  89  ALA   J CB  
17034 N  N   . LYS   J  90  ? 1.6449 0.7175 1.1544 0.0046  -0.1082 0.1767  90  LYS   J N   
17035 C  CA  . LYS   J  90  ? 1.6629 0.7859 1.1072 -0.0198 -0.1134 0.1632  90  LYS   J CA  
17036 C  C   . LYS   J  90  ? 1.6257 0.8485 1.0759 -0.0327 -0.1246 0.1877  90  LYS   J C   
17037 O  O   . LYS   J  90  ? 1.5225 0.8790 1.0441 -0.0614 -0.1560 0.1580  90  LYS   J O   
17038 C  CB  . LYS   J  90  ? 1.7350 0.7835 1.1822 0.0301  -0.0743 0.1459  90  LYS   J CB  
17039 C  CG  . LYS   J  90  ? 1.7974 0.7729 1.2063 0.0341  -0.0706 0.1229  90  LYS   J CG  
17040 C  CD  . LYS   J  90  ? 1.8309 0.7927 1.2219 0.0595  -0.0549 0.1351  90  LYS   J CD  
17041 C  CE  . LYS   J  90  ? 1.8604 0.7680 1.2373 0.0914  -0.0576 0.1878  90  LYS   J CE  
17042 N  NZ  . LYS   J  90  ? 1.8395 0.8183 1.2885 0.1395  -0.0388 0.1851  90  LYS   J NZ  
17043 N  N   . SER   J  91  ? 1.6121 0.8711 1.1959 -0.0692 -0.1572 0.1213  91  SER   J N   
17044 C  CA  . SER   J  91  ? 1.6406 0.7831 1.2299 -0.0521 -0.1650 0.1187  91  SER   J CA  
17045 C  C   . SER   J  91  ? 1.6405 0.7541 1.2380 0.0150  -0.1983 0.0811  91  SER   J C   
17046 O  O   . SER   J  91  ? 1.6566 0.6880 1.2066 0.0273  -0.2185 0.1028  91  SER   J O   
17047 C  CB  . SER   J  91  ? 1.6485 0.8182 1.2514 -0.0909 -0.1611 0.0637  91  SER   J CB  
17048 O  OG  . SER   J  91  ? 1.6952 0.8646 1.2505 -0.1370 -0.1999 0.0028  91  SER   J OG  
17049 N  N   . ILE   J  92  ? 1.6573 0.6454 1.2173 0.0125  -0.2015 0.1025  92  ILE   J N   
17050 C  CA  . ILE   J  92  ? 1.6971 0.6279 1.1889 0.0003  -0.2008 0.0881  92  ILE   J CA  
17051 C  C   . ILE   J  92  ? 1.7019 0.5654 1.1701 0.0166  -0.2379 0.1044  92  ILE   J C   
17052 O  O   . ILE   J  92  ? 1.7256 0.5645 1.0742 0.0941  -0.3197 0.1354  92  ILE   J O   
17053 C  CB  . ILE   J  92  ? 1.6692 0.5937 1.2324 -0.0081 -0.2240 0.0992  92  ILE   J CB  
17054 C  CG1 . ILE   J  92  ? 1.7069 0.6049 1.2500 0.0495  -0.2272 0.1248  92  ILE   J CG1 
17055 C  CG2 . ILE   J  92  ? 1.6665 0.5502 1.1986 0.0106  -0.2435 0.1234  92  ILE   J CG2 
17056 C  CD1 . ILE   J  92  ? 1.7189 0.6476 1.2840 0.0099  -0.2046 0.0980  92  ILE   J CD1 
17057 N  N   . ARG   J  93  ? 1.6801 0.6036 1.1465 -0.0287 -0.2014 0.0858  93  ARG   J N   
17058 C  CA  . ARG   J  93  ? 1.6941 0.6279 1.1499 -0.0735 -0.1944 0.0464  93  ARG   J CA  
17059 C  C   . ARG   J  93  ? 1.7584 0.6827 1.0915 -0.0627 -0.1168 0.0427  93  ARG   J C   
17060 O  O   . ARG   J  93  ? 1.7630 0.7156 1.0761 -0.1272 -0.1553 0.0297  93  ARG   J O   
17061 C  CB  . ARG   J  93  ? 1.7088 0.6450 1.1626 -0.0724 -0.1911 -0.0269 93  ARG   J CB  
17062 C  CG  . ARG   J  93  ? 1.7037 0.6274 1.2270 -0.0833 -0.2127 -0.0531 93  ARG   J CG  
17063 C  CD  . ARG   J  93  ? 1.7169 0.7289 1.2566 -0.0975 -0.2350 -0.0890 93  ARG   J CD  
17064 N  NE  . ARG   J  93  ? 1.6579 0.8020 1.2871 -0.1248 -0.2410 -0.0925 93  ARG   J NE  
17065 C  CZ  . ARG   J  93  ? 1.6172 0.8324 1.2111 -0.1893 -0.2562 -0.0465 93  ARG   J CZ  
17066 N  NH1 . ARG   J  93  ? 1.6351 0.8617 1.2520 -0.2671 -0.2574 -0.0290 93  ARG   J NH1 
17067 N  NH2 . ARG   J  93  ? 1.6175 0.8133 1.1650 -0.1735 -0.2923 -0.0761 93  ARG   J NH2 
17068 N  N   . SER   J  94  ? 1.7937 0.7558 1.1511 -0.0221 -0.1308 0.1073  94  SER   J N   
17069 C  CA  . SER   J  94  ? 1.8125 0.8706 1.2124 0.0034  -0.0948 0.0951  94  SER   J CA  
17070 C  C   . SER   J  94  ? 1.7840 0.8802 1.1724 -0.0189 -0.1515 0.0885  94  SER   J C   
17071 O  O   . SER   J  94  ? 1.7846 0.8672 1.1157 -0.0298 -0.1394 0.0383  94  SER   J O   
17072 C  CB  . SER   J  94  ? 1.8749 0.9594 1.2471 0.0434  -0.1212 0.1032  94  SER   J CB  
17073 O  OG  . SER   J  94  ? 1.9489 1.1080 1.3240 0.0417  -0.0147 0.1231  94  SER   J OG  
17074 N  N   . ARG   J  95  ? 1.7484 0.9627 1.2024 -0.0227 -0.1960 0.0609  95  ARG   J N   
17075 C  CA  . ARG   J  95  ? 1.7868 0.9653 1.2693 -0.0582 -0.2146 0.0708  95  ARG   J CA  
17076 C  C   . ARG   J  95  ? 1.7623 0.8729 1.2912 -0.0448 -0.1767 0.0824  95  ARG   J C   
17077 O  O   . ARG   J  95  ? 1.6597 0.8373 1.3395 0.0194  -0.1720 0.0479  95  ARG   J O   
17078 C  CB  . ARG   J  95  ? 1.7946 1.0444 1.3863 -0.0345 -0.2347 0.0063  95  ARG   J CB  
17079 C  CG  . ARG   J  95  ? 1.8492 1.0772 1.5171 -0.1209 -0.2520 0.0169  95  ARG   J CG  
17080 C  CD  . ARG   J  95  ? 1.8826 1.1484 1.6217 -0.0980 -0.2393 -0.0213 95  ARG   J CD  
17081 N  NE  . ARG   J  95  ? 1.9742 1.1893 1.6576 -0.1320 -0.2951 0.0134  95  ARG   J NE  
17082 C  CZ  . ARG   J  95  ? 2.0263 1.1149 1.6921 -0.1297 -0.3401 0.0401  95  ARG   J CZ  
17083 N  NH1 . ARG   J  95  ? 2.0936 1.1065 1.7921 -0.1108 -0.3219 -0.0023 95  ARG   J NH1 
17084 N  NH2 . ARG   J  95  ? 2.0311 1.1948 1.7007 -0.1169 -0.3498 0.0626  95  ARG   J NH2 
17085 N  N   . ARG   J  96  ? 1.8337 0.8931 1.2971 -0.0396 -0.1373 0.1078  96  ARG   J N   
17086 C  CA  . ARG   J  96  ? 1.8241 0.8398 1.2860 -0.0315 -0.1116 0.1268  96  ARG   J CA  
17087 C  C   . ARG   J  96  ? 1.7686 0.8040 1.2699 0.0165  -0.1278 0.1368  96  ARG   J C   
17088 O  O   . ARG   J  96  ? 1.7586 0.9526 1.1469 0.0324  -0.1263 0.1912  96  ARG   J O   
17089 C  CB  . ARG   J  96  ? 1.8158 0.9040 1.3387 -0.0130 -0.0979 0.1499  96  ARG   J CB  
17090 C  CG  . ARG   J  96  ? 1.8298 0.9648 1.3613 -0.0044 -0.1039 0.1078  96  ARG   J CG  
17091 C  CD  . ARG   J  96  ? 1.8154 1.0489 1.4090 0.0164  -0.0691 0.1029  96  ARG   J CD  
17092 N  NE  . ARG   J  96  ? 1.8632 0.9692 1.4303 -0.0370 -0.0206 0.0962  96  ARG   J NE  
17093 C  CZ  . ARG   J  96  ? 1.8490 0.9525 1.4171 -0.0659 -0.0210 0.0443  96  ARG   J CZ  
17094 N  NH1 . ARG   J  96  ? 1.8356 0.9573 1.3994 -0.0546 -0.0117 0.0683  96  ARG   J NH1 
17095 N  NH2 . ARG   J  96  ? 1.8351 0.9432 1.4341 -0.0643 -0.0630 0.0125  96  ARG   J NH2 
17096 N  N   . PRO   J  97  ? 1.7591 0.7013 1.2675 0.0027  -0.1614 0.1757  97  PRO   J N   
17097 C  CA  . PRO   J  97  ? 1.7452 0.6477 1.2917 0.0186  -0.1478 0.1579  97  PRO   J CA  
17098 C  C   . PRO   J  97  ? 1.8047 0.6341 1.2993 0.0108  -0.1408 0.1250  97  PRO   J C   
17099 O  O   . PRO   J  97  ? 1.7921 0.6796 1.4082 -0.0197 -0.1033 0.1067  97  PRO   J O   
17100 C  CB  . PRO   J  97  ? 1.7587 0.6225 1.2794 0.0161  -0.1659 0.1656  97  PRO   J CB  
17101 C  CG  . PRO   J  97  ? 1.7713 0.6824 1.2868 0.0264  -0.1388 0.1788  97  PRO   J CG  
17102 C  CD  . PRO   J  97  ? 1.7607 0.7270 1.2840 0.0225  -0.1569 0.1911  97  PRO   J CD  
17103 N  N   . TYR   J  98  ? 1.8620 0.6676 1.2623 0.0133  -0.1012 0.1071  98  TYR   J N   
17104 C  CA  . TYR   J  98  ? 1.8647 0.6128 1.2778 0.0638  -0.1010 0.0413  98  TYR   J CA  
17105 C  C   . TYR   J  98  ? 1.8741 0.5551 1.2537 0.0502  -0.0827 0.1067  98  TYR   J C   
17106 O  O   . TYR   J  98  ? 1.8622 0.3177 1.2737 0.1282  -0.0231 0.1401  98  TYR   J O   
17107 C  CB  . TYR   J  98  ? 1.8878 0.6433 1.2448 0.0544  -0.1407 0.0567  98  TYR   J CB  
17108 C  CG  . TYR   J  98  ? 1.8862 0.6633 1.2857 0.0724  -0.2022 0.0324  98  TYR   J CG  
17109 C  CD1 . TYR   J  98  ? 1.8884 0.7063 1.3573 0.0479  -0.2264 -0.0027 98  TYR   J CD1 
17110 C  CD2 . TYR   J  98  ? 1.8881 0.7643 1.2460 0.0581  -0.2455 -0.0365 98  TYR   J CD2 
17111 C  CE1 . TYR   J  98  ? 1.8518 0.7752 1.3965 0.0776  -0.2436 -0.0585 98  TYR   J CE1 
17112 C  CE2 . TYR   J  98  ? 1.8811 0.8447 1.2479 0.1106  -0.2672 -0.1329 98  TYR   J CE2 
17113 C  CZ  . TYR   J  98  ? 1.8597 0.8203 1.2918 0.1417  -0.2527 -0.1337 98  TYR   J CZ  
17114 O  OH  . TYR   J  98  ? 1.8427 0.8388 1.1238 0.1575  -0.2548 -0.2122 98  TYR   J OH  
17115 N  N   . GLN   J  99  ? 1.8083 0.5762 1.2371 0.0433  -0.0702 0.1262  99  GLN   J N   
17116 C  CA  . GLN   J  99  ? 1.7903 0.5759 1.1913 0.0090  -0.0736 0.1042  99  GLN   J CA  
17117 C  C   . GLN   J  99  ? 1.7037 0.4309 1.1811 -0.0218 -0.1116 0.0806  99  GLN   J C   
17118 O  O   . GLN   J  99  ? 1.7163 0.4221 1.1339 -0.0125 -0.1081 0.0768  99  GLN   J O   
17119 C  CB  . GLN   J  99  ? 1.8306 0.6663 1.1659 -0.0258 -0.0405 0.1505  99  GLN   J CB  
17120 C  CG  . GLN   J  99  ? 1.8957 0.7933 1.1547 -0.0021 -0.0177 0.1689  99  GLN   J CG  
17121 C  CD  . GLN   J  99  ? 1.9579 0.9542 1.1220 -0.0661 0.0097  0.2681  99  GLN   J CD  
17122 O  OE1 . GLN   J  99  ? 2.0492 1.0457 1.1620 -0.0130 0.0353  0.2072  99  GLN   J OE1 
17123 N  NE2 . GLN   J  99  ? 2.0359 1.0574 1.1025 -0.0114 0.0117  0.2069  99  GLN   J NE2 
17124 N  N   . VAL   J  100 ? 1.6831 0.4374 1.1595 -0.0146 -0.1279 0.0971  100 VAL   J N   
17125 C  CA  . VAL   J  100 ? 1.6543 0.4313 1.1604 -0.0672 -0.1500 0.0970  100 VAL   J CA  
17126 C  C   . VAL   J  100 ? 1.6622 0.3142 1.1639 -0.0193 -0.1486 0.0686  100 VAL   J C   
17127 O  O   . VAL   J  100 ? 1.6418 0.1881 1.2703 -0.0257 -0.1746 0.1230  100 VAL   J O   
17128 C  CB  . VAL   J  100 ? 1.6209 0.4523 1.1209 -0.0711 -0.1427 0.1265  100 VAL   J CB  
17129 C  CG1 . VAL   J  100 ? 1.6393 0.5351 1.1160 -0.0951 -0.1519 0.1295  100 VAL   J CG1 
17130 C  CG2 . VAL   J  100 ? 1.6180 0.4870 1.1221 -0.0973 -0.1371 0.1159  100 VAL   J CG2 
17131 N  N   . ASN   J  101 ? 1.6613 0.3200 1.1855 -0.0251 -0.1802 0.0244  101 ASN   J N   
17132 C  CA  . ASN   J  101 ? 1.6589 0.4208 1.2233 -0.0322 -0.1804 0.0063  101 ASN   J CA  
17133 C  C   . ASN   J  101 ? 1.6864 0.3297 1.2380 -0.0126 -0.1725 -0.0144 101 ASN   J C   
17134 O  O   . ASN   J  101 ? 1.6963 0.3031 1.3053 0.0034  -0.1961 -0.0352 101 ASN   J O   
17135 C  CB  . ASN   J  101 ? 1.6827 0.4286 1.2941 -0.0092 -0.1811 0.0268  101 ASN   J CB  
17136 C  CG  . ASN   J  101 ? 1.6826 0.4894 1.2944 -0.0188 -0.1814 0.0377  101 ASN   J CG  
17137 O  OD1 . ASN   J  101 ? 1.6732 0.3539 1.3082 -0.0521 -0.1198 -0.0076 101 ASN   J OD1 
17138 N  ND2 . ASN   J  101 ? 1.6829 0.5559 1.4523 -0.0801 -0.1720 0.0138  101 ASN   J ND2 
17139 N  N   . VAL   J  102 ? 1.6406 0.3837 1.1767 -0.0121 -0.1710 -0.0337 102 VAL   J N   
17140 C  CA  . VAL   J  102 ? 1.6753 0.4963 1.1302 0.0081  -0.1710 -0.0154 102 VAL   J CA  
17141 C  C   . VAL   J  102 ? 1.7224 0.5464 1.0896 0.0236  -0.1539 -0.0249 102 VAL   J C   
17142 O  O   . VAL   J  102 ? 1.7903 0.5886 1.0212 0.0548  -0.1813 -0.0299 102 VAL   J O   
17143 C  CB  . VAL   J  102 ? 1.6407 0.4760 1.1216 0.0393  -0.1780 0.0435  102 VAL   J CB  
17144 C  CG1 . VAL   J  102 ? 1.6130 0.5154 1.1321 0.0133  -0.1854 0.0851  102 VAL   J CG1 
17145 C  CG2 . VAL   J  102 ? 1.6326 0.5184 1.1453 0.0306  -0.1804 0.0440  102 VAL   J CG2 
17146 N  N   . LEU   J  103 ? 1.7473 0.5734 1.1056 0.0236  -0.1663 0.0196  103 LEU   J N   
17147 C  CA  . LEU   J  103 ? 1.7520 0.6413 1.1177 0.0366  -0.1575 0.0489  103 LEU   J CA  
17148 C  C   . LEU   J  103 ? 1.7602 0.6586 1.1135 0.0470  -0.1613 0.0639  103 LEU   J C   
17149 O  O   . LEU   J  103 ? 1.7425 0.8881 1.1043 0.0540  -0.1541 0.0221  103 LEU   J O   
17150 C  CB  . LEU   J  103 ? 1.7649 0.6396 1.0984 0.0395  -0.1628 0.0609  103 LEU   J CB  
17151 C  CG  . LEU   J  103 ? 1.7647 0.6601 1.1164 0.0906  -0.1586 0.0830  103 LEU   J CG  
17152 C  CD1 . LEU   J  103 ? 1.8004 0.7184 1.1056 0.1025  -0.1494 0.0688  103 LEU   J CD1 
17153 C  CD2 . LEU   J  103 ? 1.7583 0.6209 1.1275 0.1022  -0.1465 0.1008  103 LEU   J CD2 
17154 N  N   . ILE   J  104 ? 1.7368 0.6541 1.0837 0.0554  -0.1784 0.0394  104 ILE   J N   
17155 C  CA  . ILE   J  104 ? 1.7423 0.6278 1.0680 0.0134  -0.1578 0.0154  104 ILE   J CA  
17156 C  C   . ILE   J  104 ? 1.7150 0.5705 1.0682 -0.0207 -0.1664 -0.0463 104 ILE   J C   
17157 O  O   . ILE   J  104 ? 1.7171 0.5317 1.0280 -0.0360 -0.2005 -0.0817 104 ILE   J O   
17158 C  CB  . ILE   J  104 ? 1.7432 0.5778 1.0385 0.0351  -0.1414 0.0489  104 ILE   J CB  
17159 C  CG1 . ILE   J  104 ? 1.7505 0.5714 1.0545 0.0619  -0.1331 0.0589  104 ILE   J CG1 
17160 C  CG2 . ILE   J  104 ? 1.7446 0.6147 1.0760 0.0089  -0.1141 0.0763  104 ILE   J CG2 
17161 C  CD1 . ILE   J  104 ? 1.7529 0.5524 1.0579 0.0718  -0.1312 0.0571  104 ILE   J CD1 
17162 N  N   . GLY   J  105 ? 1.7685 0.5838 1.0747 -0.0368 -0.1839 -0.0484 105 GLY   J N   
17163 C  CA  . GLY   J  105 ? 1.7841 0.5411 1.1134 -0.0532 -0.1683 -0.0111 105 GLY   J CA  
17164 C  C   . GLY   J  105 ? 1.7490 0.5383 1.1130 -0.0714 -0.1990 -0.0086 105 GLY   J C   
17165 O  O   . GLY   J  105 ? 1.7473 0.4380 1.1102 -0.0906 -0.2138 -0.0286 105 GLY   J O   
17166 N  N   . GLY   J  106 ? 1.7601 0.5704 1.1244 -0.0811 -0.1892 0.0144  106 GLY   J N   
17167 C  CA  . GLY   J  106 ? 1.7839 0.5859 1.1477 -0.0753 -0.1645 0.0584  106 GLY   J CA  
17168 C  C   . GLY   J  106 ? 1.8022 0.6147 1.1853 -0.0624 -0.1403 0.0756  106 GLY   J C   
17169 O  O   . GLY   J  106 ? 1.8598 0.5500 1.1779 -0.0420 -0.1626 0.1448  106 GLY   J O   
17170 N  N   . TYR   J  107 ? 1.7899 0.6581 1.2152 -0.0414 -0.1311 0.1147  107 TYR   J N   
17171 C  CA  . TYR   J  107 ? 1.7932 0.6212 1.2230 -0.0439 -0.1351 0.1349  107 TYR   J CA  
17172 C  C   . TYR   J  107 ? 1.7726 0.5294 1.2872 -0.0461 -0.0996 0.2134  107 TYR   J C   
17173 O  O   . TYR   J  107 ? 1.7222 0.5364 1.3200 -0.0631 -0.1007 0.2637  107 TYR   J O   
17174 C  CB  . TYR   J  107 ? 1.8127 0.6222 1.2201 -0.0141 -0.1434 0.1319  107 TYR   J CB  
17175 C  CG  . TYR   J  107 ? 1.8375 0.6523 1.2057 -0.0158 -0.1439 0.1453  107 TYR   J CG  
17176 C  CD1 . TYR   J  107 ? 1.8456 0.6362 1.2065 0.0004  -0.1310 0.1305  107 TYR   J CD1 
17177 C  CD2 . TYR   J  107 ? 1.8383 0.7508 1.2300 0.0296  -0.1061 0.1404  107 TYR   J CD2 
17178 C  CE1 . TYR   J  107 ? 1.8600 0.7162 1.2497 0.0003  -0.0996 0.1300  107 TYR   J CE1 
17179 C  CE2 . TYR   J  107 ? 1.8622 0.7596 1.2770 0.0051  -0.0824 0.1724  107 TYR   J CE2 
17180 C  CZ  . TYR   J  107 ? 1.8603 0.7399 1.2824 0.0208  -0.0642 0.1483  107 TYR   J CZ  
17181 O  OH  . TYR   J  107 ? 1.8904 0.8235 1.3685 0.0187  -0.0129 0.1655  107 TYR   J OH  
17182 N  N   . ASP   J  108 ? 1.7848 0.5770 1.3084 -0.0935 -0.1040 0.1923  108 ASP   J N   
17183 C  CA  . ASP   J  108 ? 1.8309 0.6291 1.3225 -0.1124 -0.1011 0.1365  108 ASP   J CA  
17184 C  C   . ASP   J  108 ? 1.8698 0.6914 1.3591 -0.1466 -0.0751 0.1638  108 ASP   J C   
17185 O  O   . ASP   J  108 ? 1.8605 0.7192 1.4038 -0.1537 -0.0233 0.2473  108 ASP   J O   
17186 C  CB  . ASP   J  108 ? 1.8297 0.6213 1.3041 -0.1316 -0.1096 0.1144  108 ASP   J CB  
17187 C  CG  . ASP   J  108 ? 1.8035 0.7093 1.3056 -0.1910 -0.1488 0.1110  108 ASP   J CG  
17188 O  OD1 . ASP   J  108 ? 1.8019 0.6947 1.3574 -0.2674 -0.1642 0.1211  108 ASP   J OD1 
17189 O  OD2 . ASP   J  108 ? 1.8073 0.6422 1.3503 -0.1732 -0.1653 0.1696  108 ASP   J OD2 
17190 N  N   . LYS   J  109 ? 1.8835 0.6518 1.4038 -0.1622 -0.0701 0.1075  109 LYS   J N   
17191 C  CA  . LYS   J  109 ? 1.9308 0.6606 1.4417 -0.1844 -0.0473 0.1132  109 LYS   J CA  
17192 C  C   . LYS   J  109 ? 1.9506 0.6976 1.5220 -0.2112 -0.0201 0.0598  109 LYS   J C   
17193 O  O   . LYS   J  109 ? 2.0289 0.7184 1.5619 -0.2429 0.0042  0.0946  109 LYS   J O   
17194 C  CB  . LYS   J  109 ? 1.9340 0.6788 1.4522 -0.1763 -0.0853 0.1007  109 LYS   J CB  
17195 C  CG  . LYS   J  109 ? 1.9269 0.6736 1.4406 -0.1587 -0.1088 0.1191  109 LYS   J CG  
17196 C  CD  . LYS   J  109 ? 1.9838 0.7289 1.4327 -0.1723 -0.0984 0.1234  109 LYS   J CD  
17197 C  CE  . LYS   J  109 ? 2.0290 0.7761 1.3654 -0.2132 -0.0914 0.1525  109 LYS   J CE  
17198 N  NZ  . LYS   J  109 ? 2.0776 0.8052 1.3725 -0.2409 -0.0850 0.1234  109 LYS   J NZ  
17199 N  N   . LYS   J  110 ? 1.8990 0.7035 1.5171 -0.2085 0.0070  0.0331  110 LYS   J N   
17200 C  CA  . LYS   J  110 ? 1.8798 0.7408 1.5981 -0.2213 0.0322  0.0357  110 LYS   J CA  
17201 C  C   . LYS   J  110 ? 1.8713 0.7626 1.6186 -0.2192 0.0311  0.0290  110 LYS   J C   
17202 O  O   . LYS   J  110 ? 1.9024 0.6567 1.7823 -0.2786 0.0042  -0.0085 110 LYS   J O   
17203 C  CB  . LYS   J  110 ? 1.8530 0.7715 1.6094 -0.2269 0.0238  0.0243  110 LYS   J CB  
17204 C  CG  . LYS   J  110 ? 1.8751 0.8202 1.6921 -0.2013 0.0260  -0.0117 110 LYS   J CG  
17205 C  CD  . LYS   J  110 ? 1.8792 0.9419 1.7532 -0.1611 0.0143  -0.1135 110 LYS   J CD  
17206 C  CE  . LYS   J  110 ? 1.9046 1.0076 1.8367 -0.2113 0.0621  -0.1170 110 LYS   J CE  
17207 N  NZ  . LYS   J  110 ? 1.9240 1.0946 1.9154 -0.2359 0.0236  -0.1985 110 LYS   J NZ  
17208 N  N   . LYS   J  111 ? 1.8757 0.7696 1.5681 -0.2074 0.0292  0.0463  111 LYS   J N   
17209 C  CA  . LYS   J  111 ? 1.8844 0.8210 1.5775 -0.1850 0.0460  0.0373  111 LYS   J CA  
17210 C  C   . LYS   J  111 ? 1.8570 0.8131 1.6053 -0.1448 0.0861  -0.0049 111 LYS   J C   
17211 O  O   . LYS   J  111 ? 1.9016 0.7862 1.7147 -0.1208 0.1200  -0.0220 111 LYS   J O   
17212 C  CB  . LYS   J  111 ? 1.8960 0.7877 1.5867 -0.1504 0.0211  0.0313  111 LYS   J CB  
17213 C  CG  . LYS   J  111 ? 1.9003 0.8230 1.5798 -0.1226 0.0064  0.0510  111 LYS   J CG  
17214 C  CD  . LYS   J  111 ? 1.9040 0.8817 1.5785 -0.0906 0.0136  0.0807  111 LYS   J CD  
17215 C  CE  . LYS   J  111 ? 1.8911 1.0053 1.6258 -0.1066 0.0005  0.0466  111 LYS   J CE  
17216 N  NZ  . LYS   J  111 ? 1.9186 1.0675 1.6332 -0.1228 0.0087  0.0786  111 LYS   J NZ  
17217 N  N   . ASN   J  112 ? 1.9061 0.8515 1.5552 -0.1591 0.0459  -0.0025 112 ASN   J N   
17218 C  CA  . ASN   J  112 ? 1.9393 0.8728 1.5314 -0.1444 0.0234  0.0109  112 ASN   J CA  
17219 C  C   . ASN   J  112 ? 1.9308 0.8546 1.4677 -0.1504 0.0310  -0.0639 112 ASN   J C   
17220 O  O   . ASN   J  112 ? 1.9574 0.8707 1.4292 -0.1952 0.0451  -0.0714 112 ASN   J O   
17221 C  CB  . ASN   J  112 ? 1.9721 0.9345 1.5384 -0.1555 0.0046  0.0577  112 ASN   J CB  
17222 C  CG  . ASN   J  112 ? 2.0068 0.9802 1.5718 -0.1549 -0.0468 0.1269  112 ASN   J CG  
17223 O  OD1 . ASN   J  112 ? 2.0829 0.9629 1.5067 -0.1348 -0.1118 0.1801  112 ASN   J OD1 
17224 N  ND2 . ASN   J  112 ? 1.9632 1.0162 1.6515 -0.1637 -0.0563 0.1509  112 ASN   J ND2 
17225 N  N   . LYS   J  113 ? 1.8911 0.8188 1.4428 -0.1386 0.0264  -0.1001 113 LYS   J N   
17226 C  CA  . LYS   J  113 ? 1.8429 0.8149 1.4723 -0.1408 0.0061  -0.1039 113 LYS   J CA  
17227 C  C   . LYS   J  113 ? 1.7838 0.7245 1.3982 -0.0954 -0.0422 -0.1080 113 LYS   J C   
17228 O  O   . LYS   J  113 ? 1.7374 0.5747 1.4025 -0.1478 -0.1191 -0.1796 113 LYS   J O   
17229 C  CB  . LYS   J  113 ? 1.8224 0.8906 1.5329 -0.1472 -0.0058 -0.0858 113 LYS   J CB  
17230 C  CG  . LYS   J  113 ? 1.8220 1.0302 1.6426 -0.2146 0.0542  -0.0502 113 LYS   J CG  
17231 C  CD  . LYS   J  113 ? 1.7799 1.1395 1.6997 -0.2340 0.0544  -0.0100 113 LYS   J CD  
17232 C  CE  . LYS   J  113 ? 1.8291 1.2316 1.7639 -0.1884 0.1035  -0.0010 113 LYS   J CE  
17233 N  NZ  . LYS   J  113 ? 1.9656 1.3097 1.7863 -0.1658 0.1572  0.0404  113 LYS   J NZ  
17234 N  N   . PRO   J  114 ? 1.8051 0.6837 1.4333 -0.1428 -0.0704 -0.0051 114 PRO   J N   
17235 C  CA  . PRO   J  114 ? 1.8114 0.6698 1.4057 -0.1251 -0.0671 0.0130  114 PRO   J CA  
17236 C  C   . PRO   J  114 ? 1.7657 0.6278 1.3676 -0.1426 -0.0566 -0.0330 114 PRO   J C   
17237 O  O   . PRO   J  114 ? 1.7588 0.5245 1.3949 -0.1733 -0.0646 -0.0199 114 PRO   J O   
17238 C  CB  . PRO   J  114 ? 1.8492 0.6783 1.4327 -0.1304 -0.0595 -0.0010 114 PRO   J CB  
17239 C  CG  . PRO   J  114 ? 1.8713 0.7023 1.4556 -0.1221 -0.0325 -0.0053 114 PRO   J CG  
17240 C  CD  . PRO   J  114 ? 1.8457 0.7176 1.4531 -0.1313 -0.0257 0.0111  114 PRO   J CD  
17241 N  N   . GLU   J  115 ? 1.7742 0.6256 1.2776 -0.1304 -0.0889 -0.0504 115 GLU   J N   
17242 C  CA  . GLU   J  115 ? 1.7466 0.6245 1.2965 -0.1217 -0.1197 -0.0334 115 GLU   J CA  
17243 C  C   . GLU   J  115 ? 1.7723 0.5282 1.2470 -0.1074 -0.1147 -0.0567 115 GLU   J C   
17244 O  O   . GLU   J  115 ? 1.7801 0.3892 1.2247 -0.1211 -0.1100 -0.0568 115 GLU   J O   
17245 C  CB  . GLU   J  115 ? 1.7200 0.6831 1.2875 -0.1626 -0.1826 -0.0383 115 GLU   J CB  
17246 C  CG  . GLU   J  115 ? 1.6921 0.8085 1.3335 -0.1524 -0.1942 0.0277  115 GLU   J CG  
17247 C  CD  . GLU   J  115 ? 1.6528 0.8117 1.3005 -0.1568 -0.2507 0.0552  115 GLU   J CD  
17248 O  OE1 . GLU   J  115 ? 1.6501 0.8374 1.2958 -0.1285 -0.3094 0.0792  115 GLU   J OE1 
17249 O  OE2 . GLU   J  115 ? 1.6286 0.8127 1.2175 -0.1588 -0.2511 0.1249  115 GLU   J OE2 
17250 N  N   . LEU   J  116 ? 1.7512 0.5484 1.2290 -0.0968 -0.0979 -0.0469 116 LEU   J N   
17251 C  CA  . LEU   J  116 ? 1.7455 0.5493 1.2126 -0.0764 -0.0866 -0.0291 116 LEU   J CA  
17252 C  C   . LEU   J  116 ? 1.6869 0.4898 1.2152 -0.0579 -0.0865 -0.0262 116 LEU   J C   
17253 O  O   . LEU   J  116 ? 1.6928 0.4567 1.2239 -0.0481 -0.0842 -0.0131 116 LEU   J O   
17254 C  CB  . LEU   J  116 ? 1.7718 0.5184 1.2385 -0.0837 -0.0743 -0.0135 116 LEU   J CB  
17255 C  CG  . LEU   J  116 ? 1.7696 0.5436 1.2484 -0.0888 -0.0717 0.0081  116 LEU   J CG  
17256 C  CD1 . LEU   J  116 ? 1.7663 0.4728 1.2214 -0.0981 -0.0737 0.0077  116 LEU   J CD1 
17257 C  CD2 . LEU   J  116 ? 1.8059 0.5690 1.2747 -0.0615 -0.0523 0.0027  116 LEU   J CD2 
17258 N  N   . TYR   J  117 ? 1.7213 0.4576 1.1979 -0.0797 -0.0749 -0.0358 117 TYR   J N   
17259 C  CA  . TYR   J  117 ? 1.7461 0.4691 1.2080 -0.0675 -0.0942 -0.0284 117 TYR   J CA  
17260 C  C   . TYR   J  117 ? 1.7640 0.3647 1.2030 -0.0430 -0.1154 -0.0587 117 TYR   J C   
17261 O  O   . TYR   J  117 ? 1.7755 0.2050 1.2342 -0.0321 -0.1405 -0.1391 117 TYR   J O   
17262 C  CB  . TYR   J  117 ? 1.7472 0.4835 1.2060 -0.0983 -0.0602 -0.0360 117 TYR   J CB  
17263 C  CG  . TYR   J  117 ? 1.7745 0.4884 1.2404 -0.1078 -0.0587 -0.0030 117 TYR   J CG  
17264 C  CD1 . TYR   J  117 ? 1.7686 0.4702 1.2243 -0.1113 -0.0533 -0.0221 117 TYR   J CD1 
17265 C  CD2 . TYR   J  117 ? 1.8103 0.4208 1.2988 -0.1078 -0.0596 -0.0076 117 TYR   J CD2 
17266 C  CE1 . TYR   J  117 ? 1.7588 0.4320 1.2605 -0.0997 -0.0532 -0.0615 117 TYR   J CE1 
17267 C  CE2 . TYR   J  117 ? 1.8133 0.4156 1.3295 -0.1206 -0.0556 -0.0509 117 TYR   J CE2 
17268 C  CZ  . TYR   J  117 ? 1.7993 0.3952 1.3100 -0.0979 -0.0416 -0.0559 117 TYR   J CZ  
17269 O  OH  . TYR   J  117 ? 1.7661 0.4974 1.3856 -0.1385 0.0150  -0.1177 117 TYR   J OH  
17270 N  N   . GLN   J  118 ? 1.7633 0.4902 1.1817 -0.0150 -0.1113 0.0126  118 GLN   J N   
17271 C  CA  . GLN   J  118 ? 1.7512 0.5691 1.1283 -0.0260 -0.1022 0.0399  118 GLN   J CA  
17272 C  C   . GLN   J  118 ? 1.6953 0.4565 1.1498 0.0092  -0.0610 0.0174  118 GLN   J C   
17273 O  O   . GLN   J  118 ? 1.7309 0.3230 1.0818 0.0109  -0.0556 -0.0467 118 GLN   J O   
17274 C  CB  . GLN   J  118 ? 1.7680 0.5734 1.1217 -0.0266 -0.1176 0.0388  118 GLN   J CB  
17275 C  CG  . GLN   J  118 ? 1.7771 0.6690 1.0789 -0.0512 -0.1288 0.1006  118 GLN   J CG  
17276 C  CD  . GLN   J  118 ? 1.8373 0.6600 1.0842 0.0002  -0.1303 0.2144  118 GLN   J CD  
17277 O  OE1 . GLN   J  118 ? 1.8678 0.8342 1.0899 -0.0445 -0.1359 0.3099  118 GLN   J OE1 
17278 N  NE2 . GLN   J  118 ? 1.8650 0.7907 1.1343 0.0145  -0.0861 0.1926  118 GLN   J NE2 
17279 N  N   . ILE   J  119 ? 1.6655 0.4380 1.1655 -0.0024 -0.0822 0.0282  119 ILE   J N   
17280 C  CA  . ILE   J  119 ? 1.6647 0.5466 1.1542 0.0100  -0.0935 0.0446  119 ILE   J CA  
17281 C  C   . ILE   J  119 ? 1.6751 0.5558 1.1819 -0.0079 -0.1210 0.0433  119 ILE   J C   
17282 O  O   . ILE   J  119 ? 1.7357 0.5654 1.1886 0.0853  -0.1728 0.0492  119 ILE   J O   
17283 C  CB  . ILE   J  119 ? 1.6286 0.5615 1.1439 0.0178  -0.0551 0.0463  119 ILE   J CB  
17284 C  CG1 . ILE   J  119 ? 1.6128 0.6458 1.1796 0.0010  -0.0181 0.0521  119 ILE   J CG1 
17285 C  CG2 . ILE   J  119 ? 1.6299 0.5959 1.1402 0.0146  -0.0718 0.0409  119 ILE   J CG2 
17286 C  CD1 . ILE   J  119 ? 1.5841 0.6409 1.1894 -0.0096 -0.0048 0.0035  119 ILE   J CD1 
17287 N  N   . ASP   J  120 ? 1.6637 0.6220 1.1842 -0.0414 -0.1613 0.0596  120 ASP   J N   
17288 C  CA  . ASP   J  120 ? 1.7014 0.5467 1.2045 -0.0501 -0.1780 0.0602  120 ASP   J CA  
17289 C  C   . ASP   J  120 ? 1.6856 0.4705 1.1732 -0.0508 -0.1982 0.0819  120 ASP   J C   
17290 O  O   . ASP   J  120 ? 1.7039 0.4456 1.1954 0.0344  -0.1775 0.0123  120 ASP   J O   
17291 C  CB  . ASP   J  120 ? 1.7129 0.5581 1.3126 -0.0550 -0.1869 0.0964  120 ASP   J CB  
17292 C  CG  . ASP   J  120 ? 1.6707 0.6286 1.3759 -0.0893 -0.2075 0.0918  120 ASP   J CG  
17293 O  OD1 . ASP   J  120 ? 1.6540 0.6001 1.4385 -0.1541 -0.1428 0.1204  120 ASP   J OD1 
17294 O  OD2 . ASP   J  120 ? 1.6475 0.7808 1.4681 -0.0075 -0.2085 0.1842  120 ASP   J OD2 
17295 N  N   . TYR   J  121 ? 1.6901 0.4104 1.1013 -0.0439 -0.2177 0.0729  121 TYR   J N   
17296 C  CA  . TYR   J  121 ? 1.7087 0.3448 1.0879 -0.0312 -0.2309 0.0783  121 TYR   J CA  
17297 C  C   . TYR   J  121 ? 1.6621 0.2346 1.1102 -0.0637 -0.2323 0.1090  121 TYR   J C   
17298 O  O   . TYR   J  121 ? 1.6698 0.1667 1.0747 -0.0886 -0.3188 0.1508  121 TYR   J O   
17299 C  CB  . TYR   J  121 ? 1.6865 0.4303 1.0622 -0.0458 -0.2386 0.0548  121 TYR   J CB  
17300 C  CG  . TYR   J  121 ? 1.7560 0.4827 1.0148 0.0229  -0.2562 0.0487  121 TYR   J CG  
17301 C  CD1 . TYR   J  121 ? 1.7806 0.4946 1.0432 0.0846  -0.2686 0.0782  121 TYR   J CD1 
17302 C  CD2 . TYR   J  121 ? 1.7912 0.5097 1.0050 0.0376  -0.2678 0.0752  121 TYR   J CD2 
17303 C  CE1 . TYR   J  121 ? 1.8171 0.5548 1.0241 0.1247  -0.2712 0.1048  121 TYR   J CE1 
17304 C  CE2 . TYR   J  121 ? 1.8065 0.5417 0.9998 0.0847  -0.2552 0.0824  121 TYR   J CE2 
17305 C  CZ  . TYR   J  121 ? 1.8191 0.6178 1.0211 0.1166  -0.2560 0.0413  121 TYR   J CZ  
17306 O  OH  . TYR   J  121 ? 1.8650 0.6754 0.9769 0.0682  -0.2942 0.0803  121 TYR   J OH  
17307 N  N   . LEU   J  122 ? 1.6304 0.2912 1.1203 -0.0506 -0.1891 0.0588  122 LEU   J N   
17308 C  CA  . LEU   J  122 ? 1.6233 0.3356 1.1096 -0.0130 -0.1766 0.0224  122 LEU   J CA  
17309 C  C   . LEU   J  122 ? 1.6185 0.3089 1.1388 0.0058  -0.1720 -0.0102 122 LEU   J C   
17310 O  O   . LEU   J  122 ? 1.6167 0.2880 1.2251 0.0319  -0.1859 -0.0780 122 LEU   J O   
17311 C  CB  . LEU   J  122 ? 1.6346 0.3337 1.1002 -0.0076 -0.1570 0.0333  122 LEU   J CB  
17312 C  CG  . LEU   J  122 ? 1.6548 0.3255 1.1009 0.0112  -0.1281 0.0455  122 LEU   J CG  
17313 C  CD1 . LEU   J  122 ? 1.6548 0.3668 1.1389 0.0245  -0.1163 0.0586  122 LEU   J CD1 
17314 C  CD2 . LEU   J  122 ? 1.6528 0.3198 1.0974 0.0147  -0.1292 0.0470  122 LEU   J CD2 
17315 N  N   . GLY   J  123 ? 1.6154 0.3190 1.1426 0.0097  -0.1692 -0.0041 123 GLY   J N   
17316 C  CA  . GLY   J  123 ? 1.6047 0.3495 1.1952 -0.0249 -0.1765 -0.0208 123 GLY   J CA  
17317 C  C   . GLY   J  123 ? 1.6152 0.3373 1.2427 -0.0047 -0.1846 -0.0556 123 GLY   J C   
17318 O  O   . GLY   J  123 ? 1.6282 0.5450 1.2486 -0.0160 -0.2574 -0.1057 123 GLY   J O   
17319 N  N   . THR   J  124 ? 1.6000 0.3470 1.2552 0.0150  -0.1646 -0.0606 124 THR   J N   
17320 C  CA  . THR   J  124 ? 1.6078 0.4530 1.2195 0.0220  -0.1433 -0.0769 124 THR   J CA  
17321 C  C   . THR   J  124 ? 1.6257 0.4041 1.2621 0.0193  -0.0844 -0.0363 124 THR   J C   
17322 O  O   . THR   J  124 ? 1.6413 0.5543 1.2356 -0.0220 -0.1079 -0.0032 124 THR   J O   
17323 C  CB  . THR   J  124 ? 1.6106 0.4610 1.2450 0.0612  -0.1418 -0.0817 124 THR   J CB  
17324 O  OG1 . THR   J  124 ? 1.6038 0.3984 1.2146 0.0966  -0.1416 -0.1195 124 THR   J OG1 
17325 C  CG2 . THR   J  124 ? 1.5946 0.5256 1.2777 0.0439  -0.1343 -0.0967 124 THR   J CG2 
17326 N  N   . LYS   J  125 ? 1.6176 0.4232 1.2320 0.0171  -0.0660 -0.0304 125 LYS   J N   
17327 C  CA  . LYS   J  125 ? 1.6553 0.5086 1.2634 0.0111  -0.0512 0.0102  125 LYS   J CA  
17328 C  C   . LYS   J  125 ? 1.6764 0.4649 1.2813 0.0395  -0.0547 0.0340  125 LYS   J C   
17329 O  O   . LYS   J  125 ? 1.7183 0.2909 1.2969 0.0718  -0.0887 0.0596  125 LYS   J O   
17330 C  CB  . LYS   J  125 ? 1.6255 0.5109 1.2989 0.0204  -0.0479 -0.0150 125 LYS   J CB  
17331 C  CG  . LYS   J  125 ? 1.6209 0.5685 1.3225 0.0120  -0.0641 0.0181  125 LYS   J CG  
17332 C  CD  . LYS   J  125 ? 1.5991 0.5814 1.3725 -0.0556 -0.0603 0.0309  125 LYS   J CD  
17333 C  CE  . LYS   J  125 ? 1.6077 0.5930 1.4281 -0.0789 -0.0718 0.0435  125 LYS   J CE  
17334 N  NZ  . LYS   J  125 ? 1.6315 0.5884 1.4549 -0.1004 -0.0842 0.0256  125 LYS   J NZ  
17335 N  N   . VAL   J  126 ? 1.7359 0.5040 1.2829 0.0134  -0.0167 0.0178  126 VAL   J N   
17336 C  CA  . VAL   J  126 ? 1.7611 0.5986 1.2712 0.0164  -0.0041 0.0029  126 VAL   J CA  
17337 C  C   . VAL   J  126 ? 1.7512 0.6343 1.2446 -0.0750 0.0112  -0.0176 126 VAL   J C   
17338 O  O   . VAL   J  126 ? 1.7983 0.6044 1.3247 -0.1347 -0.0420 -0.1451 126 VAL   J O   
17339 C  CB  . VAL   J  126 ? 1.7472 0.6063 1.2346 0.0410  -0.0162 0.0783  126 VAL   J CB  
17340 C  CG1 . VAL   J  126 ? 1.7626 0.6752 1.2583 0.0988  -0.0181 0.0816  126 VAL   J CG1 
17341 C  CG2 . VAL   J  126 ? 1.7410 0.6101 1.2364 0.0053  -0.0040 0.0828  126 VAL   J CG2 
17342 N  N   . GLU   J  127 ? 1.7712 0.7335 1.2818 -0.1073 0.0340  0.0103  127 GLU   J N   
17343 C  CA  . GLU   J  127 ? 1.7271 0.8050 1.2925 -0.1072 0.0489  0.0585  127 GLU   J CA  
17344 C  C   . GLU   J  127 ? 1.6804 0.7352 1.2907 -0.1240 0.0526  0.1086  127 GLU   J C   
17345 O  O   . GLU   J  127 ? 1.6108 0.6249 1.3253 -0.1692 0.0942  0.0889  127 GLU   J O   
17346 C  CB  . GLU   J  127 ? 1.7254 0.8844 1.3186 -0.1350 0.0674  0.1092  127 GLU   J CB  
17347 C  CG  . GLU   J  127 ? 1.7861 1.0061 1.3371 -0.1233 0.0821  0.1552  127 GLU   J CG  
17348 C  CD  . GLU   J  127 ? 1.8264 1.1050 1.3948 -0.1281 0.1658  0.1404  127 GLU   J CD  
17349 O  OE1 . GLU   J  127 ? 1.8061 1.1834 1.4392 -0.1458 0.2171  0.1657  127 GLU   J OE1 
17350 O  OE2 . GLU   J  127 ? 1.8838 1.1435 1.3274 -0.1755 0.1918  0.1288  127 GLU   J OE2 
17351 N  N   . LEU   J  128 ? 1.7329 0.6805 1.2582 -0.0929 0.0517  0.1117  128 LEU   J N   
17352 C  CA  . LEU   J  128 ? 1.7538 0.6690 1.2500 -0.0592 0.0415  0.1268  128 LEU   J CA  
17353 C  C   . LEU   J  128 ? 1.7447 0.5652 1.2360 -0.0797 0.0934  0.1174  128 LEU   J C   
17354 O  O   . LEU   J  128 ? 1.7006 0.6686 1.1700 -0.0979 0.0702  0.1450  128 LEU   J O   
17355 C  CB  . LEU   J  128 ? 1.7389 0.7118 1.2783 -0.0770 0.0373  0.1182  128 LEU   J CB  
17356 C  CG  . LEU   J  128 ? 1.7640 0.8242 1.2780 -0.0695 0.0370  0.1295  128 LEU   J CG  
17357 C  CD1 . LEU   J  128 ? 1.7064 0.9122 1.3118 -0.0753 0.0162  0.1242  128 LEU   J CD1 
17358 C  CD2 . LEU   J  128 ? 1.7630 0.9165 1.3281 -0.0468 0.0539  0.1165  128 LEU   J CD2 
17359 N  N   . PRO   J  129 ? 1.7950 0.4660 1.2352 -0.0597 0.0780  0.1263  129 PRO   J N   
17360 C  CA  . PRO   J  129 ? 1.8213 0.5004 1.2465 -0.0272 0.0608  0.0782  129 PRO   J CA  
17361 C  C   . PRO   J  129 ? 1.8085 0.4817 1.2514 0.0098  0.0453  0.0406  129 PRO   J C   
17362 O  O   . PRO   J  129 ? 1.8531 0.4728 1.3026 0.0679  0.0697  0.1204  129 PRO   J O   
17363 C  CB  . PRO   J  129 ? 1.8302 0.5570 1.2866 -0.0203 0.0870  0.0810  129 PRO   J CB  
17364 C  CG  . PRO   J  129 ? 1.8428 0.6183 1.2583 -0.0348 0.0974  0.0890  129 PRO   J CG  
17365 C  CD  . PRO   J  129 ? 1.7946 0.5198 1.2596 -0.0435 0.0878  0.1176  129 PRO   J CD  
17366 N  N   . TYR   J  130 ? 1.7861 0.4772 1.1747 -0.0131 0.0231  -0.0010 130 TYR   J N   
17367 C  CA  . TYR   J  130 ? 1.8176 0.4637 1.1936 -0.0292 -0.0142 -0.0496 130 TYR   J CA  
17368 C  C   . TYR   J  130 ? 1.8161 0.3725 1.1639 -0.0507 -0.0427 -0.0874 130 TYR   J C   
17369 O  O   . TYR   J  130 ? 1.7640 0.2849 1.1650 -0.1240 -0.0596 -0.1267 130 TYR   J O   
17370 C  CB  . TYR   J  130 ? 1.8403 0.4777 1.2157 -0.0262 -0.0204 -0.0676 130 TYR   J CB  
17371 C  CG  . TYR   J  130 ? 1.8810 0.4318 1.2511 -0.0064 -0.0422 -0.0694 130 TYR   J CG  
17372 C  CD1 . TYR   J  130 ? 1.8699 0.4103 1.2525 0.0116  -0.0627 -0.0850 130 TYR   J CD1 
17373 C  CD2 . TYR   J  130 ? 1.8794 0.4734 1.3030 -0.0022 -0.0293 -0.0773 130 TYR   J CD2 
17374 C  CE1 . TYR   J  130 ? 1.8736 0.4617 1.3186 0.0197  -0.0911 -0.0800 130 TYR   J CE1 
17375 C  CE2 . TYR   J  130 ? 1.9040 0.4840 1.3384 0.0151  -0.0515 -0.0588 130 TYR   J CE2 
17376 C  CZ  . TYR   J  130 ? 1.8977 0.4991 1.3427 0.0094  -0.0827 -0.0510 130 TYR   J CZ  
17377 O  OH  . TYR   J  130 ? 1.8871 0.6272 1.4444 0.0349  -0.1287 -0.0897 130 TYR   J OH  
17378 N  N   . GLY   J  131 ? 1.8189 0.3513 1.1490 -0.0218 -0.0686 -0.1201 131 GLY   J N   
17379 C  CA  . GLY   J  131 ? 1.8549 0.3992 1.1138 0.0080  -0.0916 -0.1265 131 GLY   J CA  
17380 C  C   . GLY   J  131 ? 1.8816 0.3962 1.1550 -0.0025 -0.1150 -0.1286 131 GLY   J C   
17381 O  O   . GLY   J  131 ? 1.9472 0.4568 1.1833 0.0299  -0.1442 -0.1079 131 GLY   J O   
17382 N  N   . ALA   J  132 ? 1.9162 0.4186 1.1219 -0.0014 -0.1630 -0.1148 132 ALA   J N   
17383 C  CA  . ALA   J  132 ? 1.9134 0.5204 1.1451 -0.0285 -0.1903 -0.1237 132 ALA   J CA  
17384 C  C   . ALA   J  132 ? 1.8664 0.5820 1.1475 0.0019  -0.1907 -0.1277 132 ALA   J C   
17385 O  O   . ALA   J  132 ? 1.8658 0.6920 1.1081 -0.0090 -0.1639 -0.1631 132 ALA   J O   
17386 C  CB  . ALA   J  132 ? 2.0003 0.5324 1.2116 -0.0378 -0.2306 -0.1621 132 ALA   J CB  
17387 N  N   . HIS   J  133 ? 1.8443 0.6000 1.1927 0.0042  -0.2444 -0.0752 133 HIS   J N   
17388 C  CA  . HIS   J  133 ? 1.8497 0.6066 1.1947 -0.0455 -0.2788 0.0050  133 HIS   J CA  
17389 C  C   . HIS   J  133 ? 1.8908 0.6056 1.2708 -0.0583 -0.2631 0.0507  133 HIS   J C   
17390 O  O   . HIS   J  133 ? 1.8666 0.6288 1.3928 -0.1509 -0.2942 0.0193  133 HIS   J O   
17391 C  CB  . HIS   J  133 ? 1.8491 0.6194 1.1385 -0.0055 -0.3210 0.0614  133 HIS   J CB  
17392 C  CG  . HIS   J  133 ? 1.8441 0.6230 1.0702 -0.0217 -0.3312 0.1088  133 HIS   J CG  
17393 N  ND1 . HIS   J  133 ? 1.8310 0.6384 1.0696 -0.0272 -0.3301 0.1028  133 HIS   J ND1 
17394 C  CD2 . HIS   J  133 ? 1.8231 0.6463 1.0298 -0.0893 -0.3097 0.1176  133 HIS   J CD2 
17395 C  CE1 . HIS   J  133 ? 1.8318 0.6026 1.0607 -0.0336 -0.3007 0.1430  133 HIS   J CE1 
17396 N  NE2 . HIS   J  133 ? 1.8275 0.6388 0.9873 -0.0739 -0.3107 0.1386  133 HIS   J NE2 
17397 N  N   . GLY   J  134 ? 1.8381 0.6295 1.2688 -0.0204 -0.2714 0.0649  134 GLY   J N   
17398 C  CA  . GLY   J  134 ? 1.8522 0.6066 1.2093 0.0147  -0.2535 0.1044  134 GLY   J CA  
17399 C  C   . GLY   J  134 ? 1.9551 0.5826 1.2523 0.0058  -0.2388 0.0753  134 GLY   J C   
17400 O  O   . GLY   J  134 ? 1.9532 0.5682 1.2483 -0.0057 -0.2649 0.0323  134 GLY   J O   
17401 N  N   . TYR   J  135 ? 2.0118 0.5796 1.2818 -0.0066 -0.1938 0.0280  135 TYR   J N   
17402 C  CA  . TYR   J  135 ? 2.0454 0.6294 1.2937 -0.0013 -0.1343 -0.0228 135 TYR   J CA  
17403 C  C   . TYR   J  135 ? 2.0281 0.6114 1.2804 0.0048  -0.1584 0.0060  135 TYR   J C   
17404 O  O   . TYR   J  135 ? 2.0334 0.6410 1.3754 -0.0021 -0.1028 0.0057  135 TYR   J O   
17405 C  CB  . TYR   J  135 ? 2.0827 0.5796 1.2627 0.0040  -0.0856 -0.0420 135 TYR   J CB  
17406 C  CG  . TYR   J  135 ? 2.0763 0.5369 1.2725 0.0180  -0.0690 -0.0353 135 TYR   J CG  
17407 C  CD1 . TYR   J  135 ? 2.0777 0.5135 1.2337 0.0157  -0.0550 -0.0386 135 TYR   J CD1 
17408 C  CD2 . TYR   J  135 ? 2.0807 0.5639 1.2551 0.0272  -0.0549 -0.0065 135 TYR   J CD2 
17409 C  CE1 . TYR   J  135 ? 2.0937 0.5077 1.2458 0.0126  -0.0763 0.0061  135 TYR   J CE1 
17410 C  CE2 . TYR   J  135 ? 2.0851 0.5404 1.2727 0.0318  -0.0644 0.0299  135 TYR   J CE2 
17411 C  CZ  . TYR   J  135 ? 2.0994 0.5140 1.2731 0.0122  -0.0680 0.0509  135 TYR   J CZ  
17412 O  OH  . TYR   J  135 ? 2.1618 0.5270 1.3104 0.0072  -0.1013 0.1582  135 TYR   J OH  
17413 N  N   . SER   J  136 ? 1.9474 0.6246 1.2614 0.0423  -0.1839 -0.0164 136 SER   J N   
17414 C  CA  . SER   J  136 ? 1.9394 0.6835 1.2756 0.0416  -0.1552 -0.0324 136 SER   J CA  
17415 C  C   . SER   J  136 ? 1.9324 0.6054 1.2687 0.0314  -0.1899 -0.0179 136 SER   J C   
17416 O  O   . SER   J  136 ? 1.9675 0.8117 1.2765 0.0184  -0.1605 -0.0658 136 SER   J O   
17417 C  CB  . SER   J  136 ? 1.9620 0.7295 1.2800 0.0151  -0.1639 0.0449  136 SER   J CB  
17418 O  OG  . SER   J  136 ? 1.9518 0.9805 1.3515 -0.0055 -0.1919 0.0997  136 SER   J OG  
17419 N  N   . GLY   J  137 ? 1.8845 0.5066 1.2497 0.0411  -0.1780 0.0337  137 GLY   J N   
17420 C  CA  . GLY   J  137 ? 1.8896 0.5709 1.2640 0.0198  -0.1589 0.0529  137 GLY   J CA  
17421 C  C   . GLY   J  137 ? 1.9101 0.5997 1.2462 0.0179  -0.1390 -0.0473 137 GLY   J C   
17422 O  O   . GLY   J  137 ? 1.9394 0.5436 1.0886 -0.0272 -0.1701 -0.1105 137 GLY   J O   
17423 N  N   . PHE   J  138 ? 1.9299 0.5369 1.3080 0.0159  -0.1354 -0.0803 138 PHE   J N   
17424 C  CA  . PHE   J  138 ? 1.9577 0.5483 1.3839 0.0401  -0.0931 -0.0597 138 PHE   J CA  
17425 C  C   . PHE   J  138 ? 2.0633 0.6230 1.3723 0.0243  -0.0889 -0.0577 138 PHE   J C   
17426 O  O   . PHE   J  138 ? 2.0781 0.7621 1.4675 0.0874  -0.0606 -0.0925 138 PHE   J O   
17427 C  CB  . PHE   J  138 ? 1.9400 0.5506 1.3658 0.0582  -0.0979 -0.0497 138 PHE   J CB  
17428 C  CG  . PHE   J  138 ? 1.9314 0.5156 1.3659 0.0579  -0.0950 -0.0549 138 PHE   J CG  
17429 C  CD1 . PHE   J  138 ? 1.9336 0.4619 1.3350 0.0510  -0.1134 -0.0297 138 PHE   J CD1 
17430 C  CD2 . PHE   J  138 ? 1.9136 0.5974 1.3907 0.0814  -0.1105 -0.0816 138 PHE   J CD2 
17431 C  CE1 . PHE   J  138 ? 1.9314 0.4946 1.3396 0.0644  -0.1175 -0.0362 138 PHE   J CE1 
17432 C  CE2 . PHE   J  138 ? 1.9308 0.6352 1.3913 0.0893  -0.1012 -0.0977 138 PHE   J CE2 
17433 C  CZ  . PHE   J  138 ? 1.9178 0.5561 1.3683 0.0866  -0.1280 -0.0508 138 PHE   J CZ  
17434 N  N   . TYR   J  139 ? 2.1027 0.4781 1.3853 0.0475  -0.0588 -0.0149 139 TYR   J N   
17435 C  CA  . TYR   J  139 ? 2.1775 0.5296 1.3983 0.0186  -0.0613 -0.0513 139 TYR   J CA  
17436 C  C   . TYR   J  139 ? 2.1740 0.5911 1.3819 0.0554  0.0075  -0.0477 139 TYR   J C   
17437 O  O   . TYR   J  139 ? 2.2354 0.5859 1.3285 0.0192  -0.0010 -0.0950 139 TYR   J O   
17438 C  CB  . TYR   J  139 ? 2.2297 0.6397 1.3716 -0.0072 -0.1050 -0.0754 139 TYR   J CB  
17439 C  CG  . TYR   J  139 ? 2.2936 0.7827 1.4223 -0.1299 -0.1013 -0.0441 139 TYR   J CG  
17440 C  CD1 . TYR   J  139 ? 2.3812 0.8564 1.4615 -0.1202 -0.0950 -0.1506 139 TYR   J CD1 
17441 C  CD2 . TYR   J  139 ? 2.2837 0.8679 1.4338 -0.1124 -0.1047 -0.0795 139 TYR   J CD2 
17442 C  CE1 . TYR   J  139 ? 2.4126 0.9414 1.5028 -0.1849 -0.0946 -0.1091 139 TYR   J CE1 
17443 C  CE2 . TYR   J  139 ? 2.3243 0.9489 1.4823 -0.2057 -0.1017 -0.0707 139 TYR   J CE2 
17444 C  CZ  . TYR   J  139 ? 2.3879 0.9936 1.5175 -0.1922 -0.1042 -0.1208 139 TYR   J CZ  
17445 O  OH  . TYR   J  139 ? 2.3664 1.1159 1.5719 -0.2733 -0.1140 -0.0731 139 TYR   J OH  
17446 N  N   . THR   J  140 ? 2.1215 0.5845 1.4148 0.1007  0.0502  0.0386  140 THR   J N   
17447 C  CA  . THR   J  140 ? 2.1212 0.5410 1.3903 0.1601  0.0019  0.0638  140 THR   J CA  
17448 C  C   . THR   J  140 ? 2.1119 0.4569 1.3862 0.1329  0.0862  0.0745  140 THR   J C   
17449 O  O   . THR   J  140 ? 2.2213 0.3581 1.3090 0.1474  0.0937  -0.0338 140 THR   J O   
17450 C  CB  . THR   J  140 ? 2.0393 0.6408 1.3709 0.2105  -0.0747 0.1518  140 THR   J CB  
17451 O  OG1 . THR   J  140 ? 2.0197 0.7184 1.3588 0.2973  -0.1539 0.1622  140 THR   J OG1 
17452 C  CG2 . THR   J  140 ? 2.0836 0.6465 1.3431 0.1532  -0.0996 0.1556  140 THR   J CG2 
17453 N  N   . PHE   J  141 ? 2.1213 0.5151 1.4099 0.1200  0.0405  0.1464  141 PHE   J N   
17454 C  CA  . PHE   J  141 ? 2.0811 0.6202 1.4305 0.1447  0.0404  0.2126  141 PHE   J CA  
17455 C  C   . PHE   J  141 ? 2.1129 0.5354 1.4344 0.1562  -0.0049 0.1813  141 PHE   J C   
17456 O  O   . PHE   J  141 ? 2.0351 0.4129 1.3475 0.2875  -0.0161 0.1852  141 PHE   J O   
17457 C  CB  . PHE   J  141 ? 2.0773 0.6827 1.4201 0.1482  0.0638  0.2686  141 PHE   J CB  
17458 C  CG  . PHE   J  141 ? 2.1018 0.6867 1.4600 0.1341  0.0870  0.2505  141 PHE   J CG  
17459 C  CD1 . PHE   J  141 ? 2.1265 0.7783 1.5210 0.1045  0.1816  0.3179  141 PHE   J CD1 
17460 C  CD2 . PHE   J  141 ? 2.0700 0.7303 1.5189 0.1075  0.0928  0.3310  141 PHE   J CD2 
17461 C  CE1 . PHE   J  141 ? 2.1386 0.7664 1.6344 0.2117  0.2113  0.3986  141 PHE   J CE1 
17462 C  CE2 . PHE   J  141 ? 2.0776 0.7455 1.5794 0.1796  0.1117  0.3738  141 PHE   J CE2 
17463 C  CZ  . PHE   J  141 ? 2.0885 0.7930 1.6512 0.1902  0.1897  0.4448  141 PHE   J CZ  
17464 N  N   . SER   J  142 ? 2.1960 0.5445 1.5038 0.0412  -0.0304 0.1532  142 SER   J N   
17465 C  CA  . SER   J  142 ? 2.2320 0.6181 1.5041 0.0137  0.0159  0.1094  142 SER   J CA  
17466 C  C   . SER   J  142 ? 2.1830 0.6316 1.4954 -0.0469 -0.0202 0.1152  142 SER   J C   
17467 O  O   . SER   J  142 ? 2.2643 0.4597 1.3817 -0.1704 0.0467  0.1109  142 SER   J O   
17468 C  CB  . SER   J  142 ? 2.3007 0.5937 1.6373 -0.0089 0.0089  0.0768  142 SER   J CB  
17469 O  OG  . SER   J  142 ? 2.3513 0.5146 1.6775 -0.0635 0.0000  0.0089  142 SER   J OG  
17470 N  N   . LEU   J  143 ? 2.2020 0.7081 1.3865 -0.0610 -0.0503 0.0832  143 LEU   J N   
17471 C  CA  . LEU   J  143 ? 2.1686 0.7865 1.3720 -0.0269 -0.0606 0.0132  143 LEU   J CA  
17472 C  C   . LEU   J  143 ? 2.0689 0.8476 1.2834 -0.0464 -0.0164 -0.0249 143 LEU   J C   
17473 O  O   . LEU   J  143 ? 2.0849 0.8727 1.2118 0.0093  -0.0605 -0.1710 143 LEU   J O   
17474 C  CB  . LEU   J  143 ? 2.1853 0.7628 1.3278 -0.0366 -0.1012 0.0709  143 LEU   J CB  
17475 C  CG  . LEU   J  143 ? 2.2027 0.8019 1.3113 -0.0183 -0.0822 0.0603  143 LEU   J CG  
17476 C  CD1 . LEU   J  143 ? 2.2235 0.7125 1.2697 -0.0298 -0.1266 0.0627  143 LEU   J CD1 
17477 C  CD2 . LEU   J  143 ? 2.2221 0.8779 1.2472 -0.0204 -0.0564 0.1031  143 LEU   J CD2 
17478 N  N   . LEU   J  144 ? 2.0673 0.8243 1.3555 -0.0479 -0.0544 -0.0293 144 LEU   J N   
17479 C  CA  . LEU   J  144 ? 2.0567 0.8535 1.3295 -0.0424 -0.0444 0.0386  144 LEU   J CA  
17480 C  C   . LEU   J  144 ? 2.0311 0.8069 1.3068 -0.0062 0.0220  0.0220  144 LEU   J C   
17481 O  O   . LEU   J  144 ? 2.1052 0.8630 1.1970 0.0693  0.0316  0.0842  144 LEU   J O   
17482 C  CB  . LEU   J  144 ? 2.0127 0.8624 1.3417 -0.0574 -0.0682 0.0311  144 LEU   J CB  
17483 C  CG  . LEU   J  144 ? 1.9887 0.9431 1.3746 -0.0873 -0.1106 0.0362  144 LEU   J CG  
17484 C  CD1 . LEU   J  144 ? 2.0174 0.9956 1.3817 -0.1151 -0.1093 0.0269  144 LEU   J CD1 
17485 C  CD2 . LEU   J  144 ? 1.9545 0.9041 1.3753 -0.1108 -0.1291 0.0259  144 LEU   J CD2 
17486 N  N   . ASP   J  145 ? 1.9958 0.7854 1.3586 0.0643  -0.0343 -0.0203 145 ASP   J N   
17487 C  CA  . ASP   J  145 ? 1.9888 0.8811 1.4505 0.0781  -0.0226 -0.0807 145 ASP   J CA  
17488 C  C   . ASP   J  145 ? 2.0290 0.9078 1.4568 0.0901  -0.0432 -0.1342 145 ASP   J C   
17489 O  O   . ASP   J  145 ? 2.0379 0.8970 1.4751 0.0801  -0.0401 -0.1401 145 ASP   J O   
17490 C  CB  . ASP   J  145 ? 2.0268 0.9677 1.4504 0.0866  -0.0089 -0.0514 145 ASP   J CB  
17491 C  CG  . ASP   J  145 ? 2.0147 0.9577 1.4695 0.0925  0.0132  -0.0640 145 ASP   J CG  
17492 O  OD1 . ASP   J  145 ? 1.9514 0.9298 1.4084 0.0401  -0.0204 0.0292  145 ASP   J OD1 
17493 O  OD2 . ASP   J  145 ? 2.0620 1.1852 1.4194 0.1018  0.0645  -0.0155 145 ASP   J OD2 
17494 N  N   . HIS   J  146 ? 2.0729 1.0205 1.5129 0.1173  -0.1037 -0.2157 146 HIS   J N   
17495 C  CA  . HIS   J  146 ? 2.1388 1.0980 1.5462 0.1336  -0.1310 -0.2854 146 HIS   J CA  
17496 C  C   . HIS   J  146 ? 2.1582 1.0925 1.5999 0.0908  -0.1124 -0.2403 146 HIS   J C   
17497 O  O   . HIS   J  146 ? 2.1836 1.0820 1.5968 0.1065  -0.0889 -0.1795 146 HIS   J O   
17498 C  CB  . HIS   J  146 ? 2.1508 1.1510 1.6038 0.1327  -0.1656 -0.4158 146 HIS   J CB  
17499 C  CG  . HIS   J  146 ? 2.1802 1.2315 1.6391 0.1389  -0.1980 -0.5060 146 HIS   J CG  
17500 N  ND1 . HIS   J  146 ? 2.1992 1.2625 1.6325 0.1479  -0.1142 -0.6215 146 HIS   J ND1 
17501 C  CD2 . HIS   J  146 ? 2.2463 1.2436 1.5812 0.2134  -0.1600 -0.5682 146 HIS   J CD2 
17502 C  CE1 . HIS   J  146 ? 2.2255 1.2975 1.6192 0.1526  -0.1118 -0.6250 146 HIS   J CE1 
17503 N  NE2 . HIS   J  146 ? 2.2620 1.3000 1.5515 0.1828  -0.1486 -0.6135 146 HIS   J NE2 
17504 N  N   . HIS   J  147 ? 2.1711 1.0852 1.6248 0.0894  -0.1316 -0.2454 147 HIS   J N   
17505 C  CA  . HIS   J  147 ? 2.1872 1.1795 1.6022 0.0970  -0.1137 -0.2396 147 HIS   J CA  
17506 C  C   . HIS   J  147 ? 2.1336 1.1862 1.4862 0.0763  -0.0735 -0.2138 147 HIS   J C   
17507 O  O   . HIS   J  147 ? 2.0638 1.2369 1.3532 0.0839  -0.1694 -0.2920 147 HIS   J O   
17508 C  CB  . HIS   J  147 ? 2.1980 1.2486 1.6284 0.1266  -0.1641 -0.2424 147 HIS   J CB  
17509 C  CG  . HIS   J  147 ? 2.2979 1.3343 1.6180 0.2311  -0.1760 -0.4422 147 HIS   J CG  
17510 N  ND1 . HIS   J  147 ? 2.2866 1.4690 1.7313 0.1982  -0.1807 -0.4131 147 HIS   J ND1 
17511 C  CD2 . HIS   J  147 ? 2.3680 1.5922 1.5403 0.2532  -0.1457 -0.4816 147 HIS   J CD2 
17512 C  CE1 . HIS   J  147 ? 2.3264 1.6004 1.6205 0.2197  -0.1395 -0.5289 147 HIS   J CE1 
17513 N  NE2 . HIS   J  147 ? 2.3911 1.6059 1.5699 0.2585  -0.1307 -0.5581 147 HIS   J NE2 
17514 N  N   . TYR   J  148 ? 2.1251 1.1760 1.5003 0.0591  0.0128  -0.2064 148 TYR   J N   
17515 C  CA  . TYR   J  148 ? 2.0832 1.1592 1.5271 0.0131  0.0590  -0.0960 148 TYR   J CA  
17516 C  C   . TYR   J  148 ? 2.1141 1.1937 1.5617 0.0018  0.1467  -0.1251 148 TYR   J C   
17517 O  O   . TYR   J  148 ? 2.0229 1.2275 1.5868 0.0048  0.2225  -0.1405 148 TYR   J O   
17518 C  CB  . TYR   J  148 ? 2.0573 1.0079 1.5129 0.0103  0.0195  -0.0755 148 TYR   J CB  
17519 C  CG  . TYR   J  148 ? 2.0129 0.9809 1.4719 -0.0068 -0.0001 0.0314  148 TYR   J CG  
17520 C  CD1 . TYR   J  148 ? 2.0355 0.9288 1.4586 -0.0475 -0.0207 0.0754  148 TYR   J CD1 
17521 C  CD2 . TYR   J  148 ? 1.9830 0.9400 1.4606 -0.0039 0.0188  0.0683  148 TYR   J CD2 
17522 C  CE1 . TYR   J  148 ? 2.0342 0.9349 1.4609 -0.0409 -0.0273 0.0395  148 TYR   J CE1 
17523 C  CE2 . TYR   J  148 ? 1.9614 0.9426 1.4256 -0.0241 0.0156  0.0763  148 TYR   J CE2 
17524 C  CZ  . TYR   J  148 ? 1.9760 0.9667 1.4709 -0.0067 -0.0100 0.0444  148 TYR   J CZ  
17525 O  OH  . TYR   J  148 ? 1.9626 1.0010 1.6255 -0.0903 -0.0384 0.0044  148 TYR   J OH  
17526 N  N   . ARG   J  149 ? 2.1259 1.1799 1.5998 0.0143  0.1403  -0.1266 149 ARG   J N   
17527 C  CA  . ARG   J  149 ? 2.1181 1.2399 1.7145 -0.0093 0.1603  -0.1990 149 ARG   J CA  
17528 C  C   . ARG   J  149 ? 2.1496 1.2058 1.6979 -0.0543 0.1349  -0.1587 149 ARG   J C   
17529 O  O   . ARG   J  149 ? 2.0926 1.1451 1.5631 -0.1701 0.1062  -0.1392 149 ARG   J O   
17530 C  CB  . ARG   J  149 ? 2.1212 1.2817 1.7818 0.0146  0.2392  -0.2353 149 ARG   J CB  
17531 C  CG  . ARG   J  149 ? 2.1893 1.3211 1.8215 0.0410  0.3001  -0.2872 149 ARG   J CG  
17532 C  CD  . ARG   J  149 ? 2.1603 1.2841 1.8715 0.0713  0.3410  -0.3036 149 ARG   J CD  
17533 N  NE  . ARG   J  149 ? 2.1997 1.3185 1.8844 0.0955  0.3980  -0.3349 149 ARG   J NE  
17534 C  CZ  . ARG   J  149 ? 2.2484 1.1857 1.9278 0.1278  0.3780  -0.4130 149 ARG   J CZ  
17535 N  NH1 . ARG   J  149 ? 2.2324 1.2076 1.9372 0.0884  0.3715  -0.3794 149 ARG   J NH1 
17536 N  NH2 . ARG   J  149 ? 2.2750 1.1933 1.9008 0.1085  0.4145  -0.4298 149 ARG   J NH2 
17537 N  N   . PRO   J  150 ? 2.1361 1.2139 1.7419 -0.0470 0.1087  -0.1309 150 PRO   J N   
17538 C  CA  . PRO   J  150 ? 2.1222 1.1880 1.6607 0.0072  0.1288  -0.0613 150 PRO   J CA  
17539 C  C   . PRO   J  150 ? 2.1476 1.0972 1.5914 0.0450  0.1613  -0.1339 150 PRO   J C   
17540 O  O   . PRO   J  150 ? 2.0737 1.1131 1.5277 0.0004  0.1348  -0.2135 150 PRO   J O   
17541 C  CB  . PRO   J  150 ? 2.1173 1.1826 1.7564 -0.0132 0.1204  -0.0921 150 PRO   J CB  
17542 C  CG  . PRO   J  150 ? 2.0978 1.3114 1.8581 0.0000  0.1480  -0.1084 150 PRO   J CG  
17543 C  CD  . PRO   J  150 ? 2.1392 1.3237 1.8439 -0.0017 0.1424  -0.1414 150 PRO   J CD  
17544 N  N   . ASP   J  151 ? 2.2078 1.0788 1.5266 0.0351  0.1768  -0.0175 151 ASP   J N   
17545 C  CA  . ASP   J  151 ? 2.1358 0.9989 1.4917 0.0254  0.2171  -0.0466 151 ASP   J CA  
17546 C  C   . ASP   J  151 ? 2.2094 0.8144 1.3479 0.0657  0.1911  0.0440  151 ASP   J C   
17547 O  O   . ASP   J  151 ? 2.2199 0.7182 1.4192 0.0768  0.2130  0.1391  151 ASP   J O   
17548 C  CB  . ASP   J  151 ? 2.1738 1.0741 1.4831 -0.0048 0.2589  -0.0083 151 ASP   J CB  
17549 C  CG  . ASP   J  151 ? 2.1531 1.1371 1.5272 0.0122  0.3079  -0.0600 151 ASP   J CG  
17550 O  OD1 . ASP   J  151 ? 2.1366 1.1115 1.5281 0.0502  0.3346  -0.0743 151 ASP   J OD1 
17551 O  OD2 . ASP   J  151 ? 2.1293 1.1218 1.5671 -0.0435 0.3295  -0.0440 151 ASP   J OD2 
17552 N  N   . MET   J  152 ? 2.1719 0.7649 1.4044 0.0342  0.1388  -0.0408 152 MET   J N   
17553 C  CA  . MET   J  152 ? 2.2208 0.7507 1.4349 0.0136  0.1071  -0.0322 152 MET   J CA  
17554 C  C   . MET   J  152 ? 2.2720 0.6036 1.3555 -0.0345 0.1375  -0.0712 152 MET   J C   
17555 O  O   . MET   J  152 ? 2.2902 0.6097 1.2476 -0.0360 0.1408  -0.0324 152 MET   J O   
17556 C  CB  . MET   J  152 ? 2.2070 0.8678 1.4928 -0.0533 0.0834  0.0059  152 MET   J CB  
17557 C  CG  . MET   J  152 ? 2.2297 0.8755 1.5748 -0.0587 0.0563  0.0804  152 MET   J CG  
17558 S  SD  . MET   J  152 ? 2.1328 1.0936 1.6049 -0.1727 0.0686  0.0745  152 MET   J SD  
17559 C  CE  . MET   J  152 ? 2.1023 1.0960 1.6311 -0.1949 0.0518  0.1147  152 MET   J CE  
17560 N  N   . THR   J  153 ? 2.2773 0.5512 1.3556 -0.0083 0.1352  -0.0776 153 THR   J N   
17561 C  CA  . THR   J  153 ? 2.2890 0.5926 1.3575 0.0187  0.1250  -0.0837 153 THR   J CA  
17562 C  C   . THR   J  153 ? 2.2636 0.5517 1.3729 0.0341  0.0990  -0.0686 153 THR   J C   
17563 O  O   . THR   J  153 ? 2.2790 0.4830 1.4322 0.1211  0.1381  -0.1274 153 THR   J O   
17564 C  CB  . THR   J  153 ? 2.3430 0.6538 1.3533 0.0269  0.1335  -0.0650 153 THR   J CB  
17565 O  OG1 . THR   J  153 ? 2.3866 0.6810 1.4008 -0.0433 0.1364  -0.0662 153 THR   J OG1 
17566 C  CG2 . THR   J  153 ? 2.3505 0.6962 1.3624 0.0281  0.1450  -0.0642 153 THR   J CG2 
17567 N  N   . THR   J  154 ? 2.2406 0.6813 1.3889 0.0732  0.0193  -0.0264 154 THR   J N   
17568 C  CA  . THR   J  154 ? 2.2081 0.7357 1.3532 0.0753  -0.0313 -0.0393 154 THR   J CA  
17569 C  C   . THR   J  154 ? 2.2487 0.7953 1.3421 0.1176  -0.0775 -0.1210 154 THR   J C   
17570 O  O   . THR   J  154 ? 2.1838 0.7070 1.3349 0.1256  -0.1057 -0.1739 154 THR   J O   
17571 C  CB  . THR   J  154 ? 2.1870 0.7422 1.3212 0.0704  -0.0472 -0.0383 154 THR   J CB  
17572 O  OG1 . THR   J  154 ? 2.1431 0.8215 1.2719 0.0623  -0.0446 -0.0685 154 THR   J OG1 
17573 C  CG2 . THR   J  154 ? 2.1655 0.6614 1.2853 0.0631  -0.0877 -0.0215 154 THR   J CG2 
17574 N  N   . GLU   J  155 ? 2.3186 0.9255 1.3508 0.1701  -0.0685 -0.1461 155 GLU   J N   
17575 C  CA  . GLU   J  155 ? 2.3667 1.0376 1.3615 0.1571  -0.1058 -0.2005 155 GLU   J CA  
17576 C  C   . GLU   J  155 ? 2.3431 1.0199 1.3280 0.1226  -0.0633 -0.1783 155 GLU   J C   
17577 O  O   . GLU   J  155 ? 2.3879 0.9041 1.2985 0.1719  -0.0402 -0.1884 155 GLU   J O   
17578 C  CB  . GLU   J  155 ? 2.4561 1.2420 1.3658 0.2016  -0.0988 -0.1960 155 GLU   J CB  
17579 C  CG  . GLU   J  155 ? 2.5241 1.3555 1.4110 0.2460  -0.1451 -0.1838 155 GLU   J CG  
17580 C  CD  . GLU   J  155 ? 2.5267 1.5040 1.5049 0.2143  -0.2136 -0.1852 155 GLU   J CD  
17581 O  OE1 . GLU   J  155 ? 2.5740 1.5166 1.6457 0.2686  -0.1952 -0.1950 155 GLU   J OE1 
17582 O  OE2 . GLU   J  155 ? 2.5448 1.5808 1.5178 0.2882  -0.3055 -0.1723 155 GLU   J OE2 
17583 N  N   . GLU   J  156 ? 2.3340 1.0067 1.2978 0.0731  -0.0511 -0.1930 156 GLU   J N   
17584 C  CA  . GLU   J  156 ? 2.2838 0.9459 1.3086 0.0467  -0.0348 -0.2219 156 GLU   J CA  
17585 C  C   . GLU   J  156 ? 2.2717 0.9254 1.3209 0.0090  -0.0520 -0.1750 156 GLU   J C   
17586 O  O   . GLU   J  156 ? 2.3314 0.9668 1.3229 -0.0298 -0.0967 -0.1294 156 GLU   J O   
17587 C  CB  . GLU   J  156 ? 2.2671 0.9452 1.3286 0.0769  -0.0032 -0.2703 156 GLU   J CB  
17588 C  CG  . GLU   J  156 ? 2.2607 0.9968 1.3703 0.0884  0.0219  -0.3126 156 GLU   J CG  
17589 C  CD  . GLU   J  156 ? 2.2492 1.0127 1.4272 0.0997  0.0613  -0.3266 156 GLU   J CD  
17590 O  OE1 . GLU   J  156 ? 2.1886 1.1363 1.5311 0.1090  0.1087  -0.3827 156 GLU   J OE1 
17591 O  OE2 . GLU   J  156 ? 2.1624 0.9760 1.4103 0.1357  0.0754  -0.2642 156 GLU   J OE2 
17592 N  N   . GLY   J  157 ? 2.2281 0.8824 1.2902 -0.0429 -0.0051 -0.1366 157 GLY   J N   
17593 C  CA  . GLY   J  157 ? 2.1698 0.8418 1.2940 -0.0489 -0.0100 -0.0984 157 GLY   J CA  
17594 C  C   . GLY   J  157 ? 2.1394 0.8444 1.2507 -0.0176 -0.0478 -0.0720 157 GLY   J C   
17595 O  O   . GLY   J  157 ? 2.1222 0.7590 1.3395 0.0167  -0.0152 -0.0628 157 GLY   J O   
17596 N  N   . LEU   J  158 ? 2.1534 0.9242 1.2220 -0.0336 -0.0450 -0.0510 158 LEU   J N   
17597 C  CA  . LEU   J  158 ? 2.1645 0.9273 1.2111 -0.0446 -0.0736 -0.0367 158 LEU   J CA  
17598 C  C   . LEU   J  158 ? 2.1913 0.9506 1.2187 -0.0151 -0.0473 -0.0835 158 LEU   J C   
17599 O  O   . LEU   J  158 ? 2.1904 1.0506 1.2034 -0.0555 -0.0607 -0.0895 158 LEU   J O   
17600 C  CB  . LEU   J  158 ? 2.1769 0.9581 1.2328 -0.0675 -0.1129 -0.0272 158 LEU   J CB  
17601 C  CG  . LEU   J  158 ? 2.1389 0.9219 1.2085 -0.1142 -0.1426 -0.0184 158 LEU   J CG  
17602 C  CD1 . LEU   J  158 ? 2.1820 0.9057 1.2313 -0.1194 -0.1617 -0.0155 158 LEU   J CD1 
17603 C  CD2 . LEU   J  158 ? 2.0982 0.8733 1.1569 -0.1251 -0.1837 -0.0076 158 LEU   J CD2 
17604 N  N   . ASP   J  159 ? 2.2164 0.9908 1.2607 -0.0252 -0.0027 -0.0904 159 ASP   J N   
17605 C  CA  . ASP   J  159 ? 2.2494 1.0080 1.2853 0.0125  0.0227  -0.1060 159 ASP   J CA  
17606 C  C   . ASP   J  159 ? 2.2153 0.8255 1.3124 0.0194  0.0316  -0.1387 159 ASP   J C   
17607 O  O   . ASP   J  159 ? 2.2337 0.7864 1.3674 0.0737  0.0224  -0.0994 159 ASP   J O   
17608 C  CB  . ASP   J  159 ? 2.2985 1.1065 1.3373 0.0224  0.0680  -0.1516 159 ASP   J CB  
17609 C  CG  . ASP   J  159 ? 2.3349 1.1670 1.3135 0.0189  0.0947  -0.1455 159 ASP   J CG  
17610 O  OD1 . ASP   J  159 ? 2.3554 1.2087 1.3790 0.0381  0.0330  -0.1508 159 ASP   J OD1 
17611 O  OD2 . ASP   J  159 ? 2.3697 1.2124 1.3678 0.0197  0.1592  -0.1785 159 ASP   J OD2 
17612 N  N   . LEU   J  160 ? 2.2094 0.7385 1.2407 0.0334  0.0552  -0.1251 160 LEU   J N   
17613 C  CA  . LEU   J  160 ? 2.2005 0.6555 1.2550 0.0337  0.0467  -0.1302 160 LEU   J CA  
17614 C  C   . LEU   J  160 ? 2.1896 0.6206 1.2366 0.0259  0.0212  -0.0921 160 LEU   J C   
17615 O  O   . LEU   J  160 ? 2.2224 0.4903 1.2051 0.0477  0.0389  -0.1895 160 LEU   J O   
17616 C  CB  . LEU   J  160 ? 2.1627 0.7274 1.2467 0.0219  0.0564  -0.1214 160 LEU   J CB  
17617 C  CG  . LEU   J  160 ? 2.1689 0.7237 1.2440 0.0575  0.0761  -0.1183 160 LEU   J CG  
17618 C  CD1 . LEU   J  160 ? 2.2276 0.6964 1.2201 0.0310  0.0773  -0.1823 160 LEU   J CD1 
17619 C  CD2 . LEU   J  160 ? 2.1523 0.7915 1.2430 0.0402  0.0478  -0.1168 160 LEU   J CD2 
17620 N  N   . LEU   J  161 ? 2.1825 0.6855 1.2474 0.0478  -0.0334 0.0193  161 LEU   J N   
17621 C  CA  . LEU   J  161 ? 2.1677 0.7164 1.2422 0.0658  -0.0489 0.0898  161 LEU   J CA  
17622 C  C   . LEU   J  161 ? 2.1937 0.8248 1.2941 0.0514  -0.1146 0.0351  161 LEU   J C   
17623 O  O   . LEU   J  161 ? 2.1791 0.9288 1.2341 0.0956  -0.1391 0.0682  161 LEU   J O   
17624 C  CB  . LEU   J  161 ? 2.1824 0.7093 1.2554 0.0644  -0.0609 0.1008  161 LEU   J CB  
17625 C  CG  . LEU   J  161 ? 2.1631 0.6637 1.2388 0.0691  -0.0703 0.1432  161 LEU   J CG  
17626 C  CD1 . LEU   J  161 ? 2.0978 0.5737 1.2351 0.0827  -0.0650 0.2019  161 LEU   J CD1 
17627 C  CD2 . LEU   J  161 ? 2.1425 0.7468 1.2891 0.1207  -0.1075 0.1461  161 LEU   J CD2 
17628 N  N   . LYS   J  162 ? 2.2312 0.8887 1.2902 0.0430  -0.0917 0.0251  162 LYS   J N   
17629 C  CA  . LYS   J  162 ? 2.2424 0.9330 1.3309 0.0590  -0.1199 -0.0203 162 LYS   J CA  
17630 C  C   . LYS   J  162 ? 2.1932 0.8960 1.4302 0.0415  -0.1133 -0.0357 162 LYS   J C   
17631 O  O   . LYS   J  162 ? 2.2560 0.7218 1.5433 0.0652  -0.1562 -0.0368 162 LYS   J O   
17632 C  CB  . LYS   J  162 ? 2.3065 1.0863 1.3244 0.0593  -0.0914 -0.0613 162 LYS   J CB  
17633 C  CG  . LYS   J  162 ? 2.3024 1.1758 1.2499 0.0579  -0.1374 -0.0606 162 LYS   J CG  
17634 C  CD  . LYS   J  162 ? 2.3645 1.3478 1.2597 0.0729  -0.1595 -0.1191 162 LYS   J CD  
17635 C  CE  . LYS   J  162 ? 2.3654 1.4124 1.3387 0.0373  -0.1914 -0.1011 162 LYS   J CE  
17636 N  NZ  . LYS   J  162 ? 2.4405 1.5512 1.3473 0.0470  -0.1771 -0.1134 162 LYS   J NZ  
17637 N  N   . LEU   J  163 ? 2.1948 0.8914 1.4076 0.0680  -0.1005 -0.0376 163 LEU   J N   
17638 C  CA  . LEU   J  163 ? 2.1600 0.8778 1.4406 0.0711  -0.0794 -0.0566 163 LEU   J CA  
17639 C  C   . LEU   J  163 ? 2.1128 0.8340 1.4611 0.0902  -0.0731 -0.0362 163 LEU   J C   
17640 O  O   . LEU   J  163 ? 2.1340 0.8709 1.5629 0.0755  -0.0676 0.0237  163 LEU   J O   
17641 C  CB  . LEU   J  163 ? 2.1733 0.9114 1.3700 0.0672  -0.0113 -0.0932 163 LEU   J CB  
17642 C  CG  . LEU   J  163 ? 2.2277 0.9662 1.3315 0.0634  0.0204  -0.1453 163 LEU   J CG  
17643 C  CD1 . LEU   J  163 ? 2.2518 0.9758 1.3526 0.0507  0.0093  -0.1677 163 LEU   J CD1 
17644 C  CD2 . LEU   J  163 ? 2.2283 0.9774 1.3176 0.0816  0.0479  -0.1704 163 LEU   J CD2 
17645 N  N   . CYS   J  164 ? 2.0533 0.7660 1.4683 0.0997  -0.0700 -0.0003 164 CYS   J N   
17646 C  CA  . CYS   J  164 ? 1.9947 0.7256 1.4706 0.0852  -0.0879 0.0234  164 CYS   J CA  
17647 C  C   . CYS   J  164 ? 1.9912 0.6562 1.4613 0.0667  -0.1443 0.0034  164 CYS   J C   
17648 O  O   . CYS   J  164 ? 1.9866 0.5295 1.5697 0.0658  -0.1581 -0.0160 164 CYS   J O   
17649 C  CB  . CYS   J  164 ? 1.9673 0.7249 1.4757 0.0490  -0.1063 0.0552  164 CYS   J CB  
17650 S  SG  . CYS   J  164 ? 1.9507 0.7621 1.5151 0.0825  -0.1115 0.1126  164 CYS   J SG  
17651 N  N   . VAL   J  165 ? 1.9735 0.7313 1.3765 0.0327  -0.1629 -0.0023 165 VAL   J N   
17652 C  CA  . VAL   J  165 ? 1.9622 0.7622 1.3358 0.0535  -0.2071 0.0163  165 VAL   J CA  
17653 C  C   . VAL   J  165 ? 1.9786 0.7620 1.3001 0.0956  -0.2013 -0.0053 165 VAL   J C   
17654 O  O   . VAL   J  165 ? 1.9186 0.7690 1.3520 0.0856  -0.2421 0.0074  165 VAL   J O   
17655 C  CB  . VAL   J  165 ? 1.9819 0.7465 1.3268 0.0219  -0.2112 0.0379  165 VAL   J CB  
17656 C  CG1 . VAL   J  165 ? 1.9879 0.8007 1.3559 0.0186  -0.2362 0.0306  165 VAL   J CG1 
17657 C  CG2 . VAL   J  165 ? 1.9382 0.7108 1.3085 0.0087  -0.1994 0.0870  165 VAL   J CG2 
17658 N  N   . GLN   J  166 ? 2.0454 0.8130 1.2761 0.1088  -0.1977 -0.0212 166 GLN   J N   
17659 C  CA  . GLN   J  166 ? 2.1081 0.8410 1.3175 0.1070  -0.1734 -0.0682 166 GLN   J CA  
17660 C  C   . GLN   J  166 ? 2.1101 0.7229 1.3234 0.0658  -0.1384 -0.0986 166 GLN   J C   
17661 O  O   . GLN   J  166 ? 2.1253 0.6732 1.3386 0.0772  -0.1507 -0.1307 166 GLN   J O   
17662 C  CB  . GLN   J  166 ? 2.1608 0.9213 1.3400 0.1648  -0.1544 -0.0945 166 GLN   J CB  
17663 C  CG  . GLN   J  166 ? 2.1958 1.0246 1.3721 0.1898  -0.2046 -0.1081 166 GLN   J CG  
17664 C  CD  . GLN   J  166 ? 2.2605 1.1189 1.3711 0.1971  -0.1835 -0.0901 166 GLN   J CD  
17665 O  OE1 . GLN   J  166 ? 2.3196 1.1634 1.4869 0.2633  -0.1738 -0.1000 166 GLN   J OE1 
17666 N  NE2 . GLN   J  166 ? 2.2739 1.2016 1.3573 0.1751  -0.2051 -0.0628 166 GLN   J NE2 
17667 N  N   . GLU   J  167 ? 2.0907 0.7003 1.3151 0.0206  -0.1023 -0.1176 167 GLU   J N   
17668 C  CA  . GLU   J  167 ? 2.1018 0.6810 1.3198 -0.0116 -0.0917 -0.1011 167 GLU   J CA  
17669 C  C   . GLU   J  167 ? 2.0908 0.6794 1.2979 -0.0760 -0.1137 -0.1008 167 GLU   J C   
17670 O  O   . GLU   J  167 ? 2.0936 0.6865 1.3045 -0.0647 -0.1304 -0.0861 167 GLU   J O   
17671 C  CB  . GLU   J  167 ? 2.0647 0.7158 1.3093 0.0030  -0.0549 -0.0945 167 GLU   J CB  
17672 C  CG  . GLU   J  167 ? 2.0691 0.7583 1.3456 0.0202  -0.0335 -0.0503 167 GLU   J CG  
17673 C  CD  . GLU   J  167 ? 2.1191 0.7863 1.3823 0.0473  -0.0245 -0.0769 167 GLU   J CD  
17674 O  OE1 . GLU   J  167 ? 2.1138 0.9140 1.4431 0.0933  -0.0237 -0.0024 167 GLU   J OE1 
17675 O  OE2 . GLU   J  167 ? 2.1590 0.8882 1.3567 0.0569  -0.0242 -0.0536 167 GLU   J OE2 
17676 N  N   . LEU   J  168 ? 2.0954 0.6400 1.2773 -0.1106 -0.1266 -0.0820 168 LEU   J N   
17677 C  CA  . LEU   J  168 ? 2.0790 0.6644 1.2833 -0.1637 -0.1280 -0.0631 168 LEU   J CA  
17678 C  C   . LEU   J  168 ? 2.1269 0.6008 1.2773 -0.1653 -0.1616 -0.0909 168 LEU   J C   
17679 O  O   . LEU   J  168 ? 2.1269 0.5199 1.3551 -0.2078 -0.1053 -0.1565 168 LEU   J O   
17680 C  CB  . LEU   J  168 ? 2.0727 0.6498 1.2611 -0.1890 -0.1454 -0.0417 168 LEU   J CB  
17681 C  CG  . LEU   J  168 ? 2.0738 0.6432 1.2639 -0.2000 -0.1412 -0.0310 168 LEU   J CG  
17682 C  CD1 . LEU   J  168 ? 2.0451 0.6440 1.2619 -0.1999 -0.1492 -0.0005 168 LEU   J CD1 
17683 C  CD2 . LEU   J  168 ? 2.0684 0.6812 1.2602 -0.2405 -0.1584 -0.0328 168 LEU   J CD2 
17684 N  N   . GLU   J  169 ? 2.1055 0.6246 1.3015 -0.1812 -0.2025 -0.0792 169 GLU   J N   
17685 C  CA  . GLU   J  169 ? 2.1183 0.7256 1.3427 -0.2075 -0.2328 -0.0666 169 GLU   J CA  
17686 C  C   . GLU   J  169 ? 2.1213 0.7287 1.2918 -0.2221 -0.2642 -0.0928 169 GLU   J C   
17687 O  O   . GLU   J  169 ? 2.1497 0.7656 1.2680 -0.2505 -0.2928 -0.1006 169 GLU   J O   
17688 C  CB  . GLU   J  169 ? 2.1556 0.8466 1.3669 -0.2219 -0.2456 -0.0247 169 GLU   J CB  
17689 C  CG  . GLU   J  169 ? 2.1055 0.9093 1.4205 -0.1925 -0.2375 0.0203  169 GLU   J CG  
17690 C  CD  . GLU   J  169 ? 2.1360 1.0547 1.4190 -0.2199 -0.2272 0.0691  169 GLU   J CD  
17691 O  OE1 . GLU   J  169 ? 2.0476 1.0725 1.5258 -0.2451 -0.2592 0.0914  169 GLU   J OE1 
17692 O  OE2 . GLU   J  169 ? 2.2152 1.1537 1.4185 -0.2142 -0.1680 0.0899  169 GLU   J OE2 
17693 N  N   . LYS   J  170 ? 2.1271 0.7343 1.2863 -0.2113 -0.2467 -0.1299 170 LYS   J N   
17694 C  CA  . LYS   J  170 ? 2.1674 0.7420 1.3391 -0.1936 -0.2200 -0.1750 170 LYS   J CA  
17695 C  C   . LYS   J  170 ? 2.1423 0.6945 1.3398 -0.1916 -0.2046 -0.1900 170 LYS   J C   
17696 O  O   . LYS   J  170 ? 2.1671 0.6700 1.3970 -0.1708 -0.1506 -0.1957 170 LYS   J O   
17697 C  CB  . LYS   J  170 ? 2.2179 0.7541 1.3307 -0.1696 -0.1848 -0.1681 170 LYS   J CB  
17698 C  CG  . LYS   J  170 ? 2.2943 0.7679 1.3806 -0.1485 -0.1654 -0.1730 170 LYS   J CG  
17699 C  CD  . LYS   J  170 ? 2.3617 0.7711 1.3754 -0.1277 -0.1426 -0.1959 170 LYS   J CD  
17700 C  CE  . LYS   J  170 ? 2.4201 0.7627 1.4212 -0.1252 -0.1372 -0.2160 170 LYS   J CE  
17701 N  NZ  . LYS   J  170 ? 2.4555 0.7526 1.4606 -0.1281 -0.1713 -0.2239 170 LYS   J NZ  
17702 N  N   . ARG   J  171 ? 2.0999 0.7270 1.3331 -0.2060 -0.2140 -0.1656 171 ARG   J N   
17703 C  CA  . ARG   J  171 ? 2.0760 0.7279 1.3539 -0.2283 -0.2377 -0.1508 171 ARG   J CA  
17704 C  C   . ARG   J  171 ? 2.0566 0.7586 1.3571 -0.2137 -0.2137 -0.0924 171 ARG   J C   
17705 O  O   . ARG   J  171 ? 2.0863 0.7999 1.4550 -0.2462 -0.2234 -0.0118 171 ARG   J O   
17706 C  CB  . ARG   J  171 ? 2.0633 0.7143 1.3316 -0.2152 -0.2043 -0.1800 171 ARG   J CB  
17707 C  CG  . ARG   J  171 ? 2.0830 0.6965 1.3356 -0.2290 -0.2257 -0.2346 171 ARG   J CG  
17708 C  CD  . ARG   J  171 ? 2.0968 0.7011 1.3746 -0.2390 -0.2387 -0.2487 171 ARG   J CD  
17709 N  NE  . ARG   J  171 ? 2.1184 0.6983 1.4216 -0.2335 -0.2416 -0.2865 171 ARG   J NE  
17710 C  CZ  . ARG   J  171 ? 2.1758 0.7054 1.4653 -0.2492 -0.2586 -0.3335 171 ARG   J CZ  
17711 N  NH1 . ARG   J  171 ? 2.1769 0.7075 1.4759 -0.2544 -0.2612 -0.3342 171 ARG   J NH1 
17712 N  NH2 . ARG   J  171 ? 2.2197 0.6906 1.4921 -0.2514 -0.2491 -0.3729 171 ARG   J NH2 
17713 N  N   . MET   J  172 ? 2.0817 0.7683 1.3225 -0.1942 -0.2240 -0.0669 172 MET   J N   
17714 C  CA  . MET   J  172 ? 2.0837 0.7708 1.3295 -0.1869 -0.2191 -0.0674 172 MET   J CA  
17715 C  C   . MET   J  172 ? 2.0692 0.5852 1.3628 -0.1553 -0.3133 -0.1371 172 MET   J C   
17716 O  O   . MET   J  172 ? 2.0783 0.4203 1.3249 -0.1242 -0.2973 -0.1243 172 MET   J O   
17717 C  CB  . MET   J  172 ? 2.1032 0.7842 1.3017 -0.2377 -0.1820 -0.0137 172 MET   J CB  
17718 C  CG  . MET   J  172 ? 2.1254 0.9078 1.3286 -0.3124 -0.1517 -0.0102 172 MET   J CG  
17719 S  SD  . MET   J  172 ? 2.2094 1.1099 1.3391 -0.3819 -0.0305 -0.0248 172 MET   J SD  
17720 C  CE  . MET   J  172 ? 2.1907 1.1614 1.3636 -0.3247 -0.0702 0.0041  172 MET   J CE  
17721 N  N   . PRO   J  173 ? 2.0918 0.6302 1.4121 -0.1450 -0.2814 -0.1034 173 PRO   J N   
17722 C  CA  . PRO   J  173 ? 2.1042 0.6158 1.5153 -0.1906 -0.3852 -0.1218 173 PRO   J CA  
17723 C  C   . PRO   J  173 ? 2.1327 0.6286 1.5530 -0.2128 -0.4758 -0.0992 173 PRO   J C   
17724 O  O   . PRO   J  173 ? 2.2069 0.4301 1.6153 -0.1987 -0.5021 -0.0809 173 PRO   J O   
17725 C  CB  . PRO   J  173 ? 2.1199 0.6499 1.5316 -0.1973 -0.3497 -0.0809 173 PRO   J CB  
17726 C  CG  . PRO   J  173 ? 2.0836 0.6918 1.5302 -0.1546 -0.3163 -0.0540 173 PRO   J CG  
17727 C  CD  . PRO   J  173 ? 2.0650 0.7184 1.4419 -0.1394 -0.3125 -0.0757 173 PRO   J CD  
17728 N  N   . MET   J  174 ? 2.1352 0.6291 1.6355 -0.1725 -0.5174 -0.0566 174 MET   J N   
17729 C  CA  . MET   J  174 ? 2.1179 0.7139 1.6536 -0.1603 -0.5062 -0.0485 174 MET   J CA  
17730 C  C   . MET   J  174 ? 2.0827 0.5949 1.6194 -0.1323 -0.4656 -0.0942 174 MET   J C   
17731 O  O   . MET   J  174 ? 2.0772 0.4012 1.5514 -0.1505 -0.4993 -0.1001 174 MET   J O   
17732 C  CB  . MET   J  174 ? 2.1418 0.7848 1.6742 -0.1519 -0.5521 -0.0941 174 MET   J CB  
17733 C  CG  . MET   J  174 ? 2.2256 0.8731 1.7229 -0.2187 -0.5538 -0.0473 174 MET   J CG  
17734 S  SD  . MET   J  174 ? 2.2840 1.0331 1.8831 -0.1132 -0.5746 0.0160  174 MET   J SD  
17735 C  CE  . MET   J  174 ? 2.2013 1.1271 1.8013 -0.2355 -0.5898 0.0196  174 MET   J CE  
17736 N  N   . ASP   J  175 ? 2.0775 0.5452 1.5033 -0.0924 -0.4153 -0.0817 175 ASP   J N   
17737 C  CA  . ASP   J  175 ? 2.0625 0.5738 1.4164 -0.0924 -0.3487 -0.1226 175 ASP   J CA  
17738 C  C   . ASP   J  175 ? 1.9866 0.5579 1.3312 -0.0863 -0.3125 -0.0815 175 ASP   J C   
17739 O  O   . ASP   J  175 ? 2.0119 0.3656 1.2987 -0.0531 -0.3457 -0.0782 175 ASP   J O   
17740 C  CB  . ASP   J  175 ? 2.0714 0.6261 1.4286 -0.1207 -0.3363 -0.1513 175 ASP   J CB  
17741 C  CG  . ASP   J  175 ? 2.0891 0.6439 1.4072 -0.1102 -0.3037 -0.1723 175 ASP   J CG  
17742 O  OD1 . ASP   J  175 ? 2.0584 0.5621 1.3867 -0.0406 -0.2787 -0.2050 175 ASP   J OD1 
17743 O  OD2 . ASP   J  175 ? 2.1125 0.7729 1.3982 -0.1456 -0.3057 -0.1985 175 ASP   J OD2 
17744 N  N   . PHE   J  176 ? 1.9666 0.5353 1.2628 -0.0470 -0.2796 -0.0838 176 PHE   J N   
17745 C  CA  . PHE   J  176 ? 1.9425 0.5393 1.2378 -0.0451 -0.2225 -0.0905 176 PHE   J CA  
17746 C  C   . PHE   J  176 ? 1.9340 0.6185 1.1584 -0.0952 -0.2407 -0.1088 176 PHE   J C   
17747 O  O   . PHE   J  176 ? 1.9061 0.6229 1.1594 -0.1415 -0.2161 0.0109  176 PHE   J O   
17748 C  CB  . PHE   J  176 ? 1.8998 0.5479 1.2545 -0.0035 -0.1755 -0.0599 176 PHE   J CB  
17749 C  CG  . PHE   J  176 ? 1.9677 0.5562 1.2457 -0.0054 -0.1381 -0.0317 176 PHE   J CG  
17750 C  CD1 . PHE   J  176 ? 1.9657 0.5689 1.2296 0.0109  -0.1214 -0.0275 176 PHE   J CD1 
17751 C  CD2 . PHE   J  176 ? 2.0056 0.5855 1.2856 0.0263  -0.1071 -0.0186 176 PHE   J CD2 
17752 C  CE1 . PHE   J  176 ? 2.0039 0.5840 1.2174 0.0104  -0.1068 -0.0176 176 PHE   J CE1 
17753 C  CE2 . PHE   J  176 ? 2.0550 0.6102 1.2590 0.0164  -0.0879 -0.0120 176 PHE   J CE2 
17754 C  CZ  . PHE   J  176 ? 2.0469 0.5802 1.2411 0.0152  -0.0889 -0.0340 176 PHE   J CZ  
17755 N  N   . LYS   J  177 ? 1.9681 0.6271 1.1830 -0.1082 -0.2421 -0.1350 177 LYS   J N   
17756 C  CA  . LYS   J  177 ? 1.9939 0.6194 1.1707 -0.1194 -0.2608 -0.1437 177 LYS   J CA  
17757 C  C   . LYS   J  177 ? 1.9693 0.6366 1.1338 -0.0961 -0.2356 -0.1560 177 LYS   J C   
17758 O  O   . LYS   J  177 ? 1.9566 0.6159 1.1193 -0.0832 -0.2107 -0.1916 177 LYS   J O   
17759 C  CB  . LYS   J  177 ? 1.9713 0.6155 1.1675 -0.1208 -0.2833 -0.1253 177 LYS   J CB  
17760 C  CG  . LYS   J  177 ? 1.9876 0.6547 1.2031 -0.1504 -0.2939 -0.1051 177 LYS   J CG  
17761 C  CD  . LYS   J  177 ? 2.0251 0.7489 1.2391 -0.1745 -0.3385 -0.1416 177 LYS   J CD  
17762 C  CE  . LYS   J  177 ? 1.9947 0.8077 1.3144 -0.2152 -0.3446 -0.1562 177 LYS   J CE  
17763 N  NZ  . LYS   J  177 ? 2.0428 0.8252 1.3534 -0.1960 -0.3709 -0.1862 177 LYS   J NZ  
17764 N  N   . GLY   J  178 ? 1.9822 0.6692 1.1379 -0.0678 -0.2242 -0.1217 178 GLY   J N   
17765 C  CA  . GLY   J  178 ? 2.0026 0.7040 1.1251 -0.0340 -0.2174 -0.0634 178 GLY   J CA  
17766 C  C   . GLY   J  178 ? 1.9777 0.6447 1.1083 -0.0238 -0.2148 -0.0058 178 GLY   J C   
17767 O  O   . GLY   J  178 ? 1.9720 0.7081 1.1031 -0.0182 -0.2024 0.0536  178 GLY   J O   
17768 N  N   . VAL   J  179 ? 1.9839 0.6703 1.1193 -0.0054 -0.2166 0.0379  179 VAL   J N   
17769 C  CA  . VAL   J  179 ? 1.9510 0.6365 1.1257 0.0369  -0.2290 0.0414  179 VAL   J CA  
17770 C  C   . VAL   J  179 ? 1.9353 0.6080 1.1232 0.0317  -0.2308 0.0250  179 VAL   J C   
17771 O  O   . VAL   J  179 ? 1.9859 0.4568 1.1255 0.0394  -0.2526 0.0502  179 VAL   J O   
17772 C  CB  . VAL   J  179 ? 1.9516 0.6751 1.1378 0.0628  -0.2143 0.0311  179 VAL   J CB  
17773 C  CG1 . VAL   J  179 ? 1.9519 0.6515 1.1491 0.0600  -0.1954 0.0333  179 VAL   J CG1 
17774 C  CG2 . VAL   J  179 ? 1.9715 0.6891 1.1508 0.0813  -0.2082 0.0049  179 VAL   J CG2 
17775 N  N   . ILE   J  180 ? 1.8642 0.5480 1.1191 0.0287  -0.2293 0.0765  180 ILE   J N   
17776 C  CA  . ILE   J  180 ? 1.8630 0.5398 1.1553 0.0029  -0.2395 0.0774  180 ILE   J CA  
17777 C  C   . ILE   J  180 ? 1.8443 0.5496 1.1940 0.0289  -0.2363 0.1287  180 ILE   J C   
17778 O  O   . ILE   J  180 ? 1.8154 0.6458 1.2091 0.0087  -0.2681 0.2876  180 ILE   J O   
17779 C  CB  . ILE   J  180 ? 1.8533 0.4824 1.2232 -0.0204 -0.2274 0.0768  180 ILE   J CB  
17780 C  CG1 . ILE   J  180 ? 1.8775 0.4243 1.2207 -0.0581 -0.2345 0.0329  180 ILE   J CG1 
17781 C  CG2 . ILE   J  180 ? 1.8648 0.5007 1.2444 -0.0213 -0.1854 0.1076  180 ILE   J CG2 
17782 C  CD1 . ILE   J  180 ? 1.8443 0.3981 1.2377 -0.0791 -0.2346 0.0324  180 ILE   J CD1 
17783 N  N   . VAL   J  181 ? 1.8930 0.5802 1.1460 0.0575  -0.2563 0.1095  181 VAL   J N   
17784 C  CA  . VAL   J  181 ? 1.8870 0.7010 1.1857 0.0624  -0.2447 0.1143  181 VAL   J CA  
17785 C  C   . VAL   J  181 ? 1.8878 0.7112 1.1760 0.0560  -0.2621 0.1294  181 VAL   J C   
17786 O  O   . VAL   J  181 ? 1.8818 0.8066 1.2480 0.0778  -0.2963 0.1423  181 VAL   J O   
17787 C  CB  . VAL   J  181 ? 1.9445 0.7065 1.2440 0.0995  -0.2307 0.0960  181 VAL   J CB  
17788 C  CG1 . VAL   J  181 ? 1.9339 0.6958 1.2613 0.1175  -0.2260 0.0946  181 VAL   J CG1 
17789 C  CG2 . VAL   J  181 ? 1.9615 0.7193 1.2988 0.1184  -0.2259 0.1199  181 VAL   J CG2 
17790 N  N   . LYS   J  182 ? 1.8760 0.7973 1.1478 0.0277  -0.2547 0.1267  182 LYS   J N   
17791 C  CA  . LYS   J  182 ? 1.8758 0.8156 1.1522 0.0010  -0.2552 0.1428  182 LYS   J CA  
17792 C  C   . LYS   J  182 ? 1.8745 0.9047 1.1606 0.0047  -0.2339 0.1077  182 LYS   J C   
17793 O  O   . LYS   J  182 ? 1.8790 0.9138 1.1808 0.0595  -0.1763 0.1337  182 LYS   J O   
17794 C  CB  . LYS   J  182 ? 1.7894 0.8206 1.1435 -0.0076 -0.2549 0.1664  182 LYS   J CB  
17795 C  CG  . LYS   J  182 ? 1.7670 0.8178 1.1556 0.0153  -0.2856 0.1685  182 LYS   J CG  
17796 C  CD  . LYS   J  182 ? 1.7350 0.7636 1.1978 0.0327  -0.3143 0.1970  182 LYS   J CD  
17797 C  CE  . LYS   J  182 ? 1.7390 0.7837 1.2573 0.0262  -0.3400 0.1936  182 LYS   J CE  
17798 N  NZ  . LYS   J  182 ? 1.7397 0.7842 1.3223 0.0219  -0.3280 0.1938  182 LYS   J NZ  
17799 N  N   . ILE   J  183 ? 1.9294 0.9011 1.1104 -0.0328 -0.2583 0.0809  183 ILE   J N   
17800 C  CA  . ILE   J  183 ? 1.9491 0.9140 1.0997 -0.0503 -0.2398 0.0907  183 ILE   J CA  
17801 C  C   . ILE   J  183 ? 1.9666 0.9065 1.1781 -0.0658 -0.2312 0.1091  183 ILE   J C   
17802 O  O   . ILE   J  183 ? 1.9881 0.9790 1.2557 -0.0206 -0.1867 0.1800  183 ILE   J O   
17803 C  CB  . ILE   J  183 ? 1.9864 0.8837 1.0751 -0.0437 -0.2763 0.0759  183 ILE   J CB  
17804 C  CG1 . ILE   J  183 ? 2.0256 0.9027 1.0431 -0.0252 -0.2958 0.0578  183 ILE   J CG1 
17805 C  CG2 . ILE   J  183 ? 1.9851 0.8613 1.0605 -0.0293 -0.2526 0.0538  183 ILE   J CG2 
17806 C  CD1 . ILE   J  183 ? 2.0876 0.9259 1.0429 -0.0326 -0.2892 0.0385  183 ILE   J CD1 
17807 N  N   . VAL   J  184 ? 1.9969 0.9202 1.1995 -0.1099 -0.2381 0.0552  184 VAL   J N   
17808 C  CA  . VAL   J  184 ? 2.0320 0.8814 1.2310 -0.0741 -0.2106 0.0378  184 VAL   J CA  
17809 C  C   . VAL   J  184 ? 2.1213 0.8205 1.1490 -0.1542 -0.1965 0.0283  184 VAL   J C   
17810 O  O   . VAL   J  184 ? 2.1272 0.8377 1.0982 -0.1638 -0.2291 0.0680  184 VAL   J O   
17811 C  CB  . VAL   J  184 ? 1.9564 0.8729 1.2358 -0.0524 -0.1700 0.0142  184 VAL   J CB  
17812 C  CG1 . VAL   J  184 ? 1.9254 0.8282 1.2950 -0.0307 -0.1702 0.0497  184 VAL   J CG1 
17813 C  CG2 . VAL   J  184 ? 1.9230 0.8477 1.2541 -0.0566 -0.1763 -0.0258 184 VAL   J CG2 
17814 N  N   . ASP   J  185 ? 2.1762 0.7970 1.2002 -0.1574 -0.1890 0.0202  185 ASP   J N   
17815 C  CA  . ASP   J  185 ? 2.1952 0.8837 1.2181 -0.1536 -0.1542 0.0046  185 ASP   J CA  
17816 C  C   . ASP   J  185 ? 2.1951 0.8796 1.3252 -0.1324 -0.1003 0.1156  185 ASP   J C   
17817 O  O   . ASP   J  185 ? 2.2150 0.7280 1.4659 -0.1352 -0.0388 0.1323  185 ASP   J O   
17818 C  CB  . ASP   J  185 ? 2.2398 0.9207 1.1945 -0.1403 -0.2006 0.0060  185 ASP   J CB  
17819 C  CG  . ASP   J  185 ? 2.3224 0.9154 1.1092 -0.1119 -0.2080 0.0395  185 ASP   J CG  
17820 O  OD1 . ASP   J  185 ? 2.3063 0.8453 1.0200 -0.1413 -0.2680 0.0805  185 ASP   J OD1 
17821 O  OD2 . ASP   J  185 ? 2.3425 1.1483 0.9385 -0.0929 -0.2659 0.0729  185 ASP   J OD2 
17822 N  N   . LYS   J  186 ? 2.2110 0.9025 1.3265 -0.1200 -0.0973 0.1529  186 LYS   J N   
17823 C  CA  . LYS   J  186 ? 2.1244 0.8926 1.2842 -0.0894 -0.0855 0.1353  186 LYS   J CA  
17824 C  C   . LYS   J  186 ? 2.1467 0.7979 1.2280 -0.0931 -0.1013 0.1373  186 LYS   J C   
17825 O  O   . LYS   J  186 ? 2.1535 0.7361 1.2274 -0.0512 -0.0613 0.2601  186 LYS   J O   
17826 C  CB  . LYS   J  186 ? 2.1713 1.0138 1.2767 -0.1374 -0.0680 0.1270  186 LYS   J CB  
17827 C  CG  . LYS   J  186 ? 2.2132 1.1512 1.3018 -0.1677 -0.1049 0.0800  186 LYS   J CG  
17828 C  CD  . LYS   J  186 ? 2.2191 1.3040 1.3439 -0.1870 -0.0852 0.0527  186 LYS   J CD  
17829 C  CE  . LYS   J  186 ? 2.2803 1.4545 1.3425 -0.1843 -0.0960 0.0258  186 LYS   J CE  
17830 N  NZ  . LYS   J  186 ? 2.3143 1.5332 1.4058 -0.1695 -0.1187 0.0631  186 LYS   J NZ  
17831 N  N   . ASP   J  187 ? 2.1122 0.7121 1.1934 -0.0005 -0.0908 0.0793  187 ASP   J N   
17832 C  CA  . ASP   J  187 ? 2.0817 0.6735 1.1800 -0.0052 -0.0685 0.0479  187 ASP   J CA  
17833 C  C   . ASP   J  187 ? 2.0159 0.5860 1.1005 0.0022  -0.1284 0.0391  187 ASP   J C   
17834 O  O   . ASP   J  187 ? 1.9878 0.5693 1.0868 -0.0210 -0.0931 0.0550  187 ASP   J O   
17835 C  CB  . ASP   J  187 ? 2.1370 0.7366 1.1867 0.0331  -0.0542 0.0152  187 ASP   J CB  
17836 C  CG  . ASP   J  187 ? 2.1789 0.7976 1.2554 0.0392  0.0048  0.0074  187 ASP   J CG  
17837 O  OD1 . ASP   J  187 ? 2.1845 0.7780 1.2931 0.0665  0.0015  -0.0065 187 ASP   J OD1 
17838 O  OD2 . ASP   J  187 ? 2.2235 0.9839 1.2948 0.0484  0.0718  -0.0961 187 ASP   J OD2 
17839 N  N   . GLY   J  188 ? 1.9456 0.5815 1.0801 -0.0074 -0.1478 0.0154  188 GLY   J N   
17840 C  CA  . GLY   J  188 ? 1.9150 0.6481 1.0658 0.0066  -0.1806 0.0496  188 GLY   J CA  
17841 C  C   . GLY   J  188 ? 1.9344 0.6877 1.0796 -0.0463 -0.2035 0.0688  188 GLY   J C   
17842 O  O   . GLY   J  188 ? 1.9011 0.8192 1.1004 -0.0110 -0.1881 0.0407  188 GLY   J O   
17843 N  N   . ILE   J  189 ? 1.9201 0.7213 1.0932 -0.0271 -0.2229 0.0965  189 ILE   J N   
17844 C  CA  . ILE   J  189 ? 1.9594 0.7331 1.1250 -0.0439 -0.2182 0.1028  189 ILE   J CA  
17845 C  C   . ILE   J  189 ? 1.9837 0.7480 1.1870 -0.0234 -0.2698 0.1155  189 ILE   J C   
17846 O  O   . ILE   J  189 ? 2.0229 0.7870 1.2242 0.0091  -0.2970 0.1194  189 ILE   J O   
17847 C  CB  . ILE   J  189 ? 1.9410 0.6811 1.1179 -0.0810 -0.2249 0.1295  189 ILE   J CB  
17848 C  CG1 . ILE   J  189 ? 1.9061 0.6854 1.1028 -0.0847 -0.2012 0.1603  189 ILE   J CG1 
17849 C  CG2 . ILE   J  189 ? 1.9432 0.6702 1.0847 -0.0904 -0.2472 0.0947  189 ILE   J CG2 
17850 C  CD1 . ILE   J  189 ? 1.8838 0.6418 1.0930 -0.0955 -0.1950 0.1841  189 ILE   J CD1 
17851 N  N   . ARG   J  190 ? 2.0116 0.7273 1.2636 -0.0274 -0.2338 0.1189  190 ARG   J N   
17852 C  CA  . ARG   J  190 ? 2.0390 0.7312 1.2619 -0.0135 -0.2371 0.0952  190 ARG   J CA  
17853 C  C   . ARG   J  190 ? 2.0524 0.7094 1.3152 0.0174  -0.2219 0.0416  190 ARG   J C   
17854 O  O   . ARG   J  190 ? 2.0451 0.7122 1.3719 0.0641  -0.2136 -0.0195 190 ARG   J O   
17855 C  CB  . ARG   J  190 ? 2.0692 0.7243 1.2732 -0.0167 -0.2173 0.0994  190 ARG   J CB  
17856 C  CG  . ARG   J  190 ? 2.0897 0.7192 1.3094 -0.0099 -0.1942 0.1005  190 ARG   J CG  
17857 C  CD  . ARG   J  190 ? 2.1692 0.7986 1.3273 -0.0181 -0.1761 0.1087  190 ARG   J CD  
17858 N  NE  . ARG   J  190 ? 2.2076 0.8195 1.3913 0.0138  -0.1539 0.1317  190 ARG   J NE  
17859 C  CZ  . ARG   J  190 ? 2.1920 0.8021 1.4196 0.0011  -0.1144 0.1406  190 ARG   J CZ  
17860 N  NH1 . ARG   J  190 ? 2.1744 0.8094 1.4330 -0.0245 -0.1085 0.1412  190 ARG   J NH1 
17861 N  NH2 . ARG   J  190 ? 2.2128 0.8550 1.4542 0.0375  -0.0579 0.1803  190 ARG   J NH2 
17862 N  N   . GLN   J  191 ? 2.0568 0.7993 1.3009 0.0142  -0.2423 0.0510  191 GLN   J N   
17863 C  CA  . GLN   J  191 ? 2.0852 0.7844 1.2996 0.0447  -0.2321 0.0911  191 GLN   J CA  
17864 C  C   . GLN   J  191 ? 2.1894 0.8073 1.2814 -0.0006 -0.2107 0.1006  191 GLN   J C   
17865 O  O   . GLN   J  191 ? 2.2875 0.8041 1.3073 0.0875  -0.1866 0.1255  191 GLN   J O   
17866 C  CB  . GLN   J  191 ? 2.0680 0.7281 1.2824 0.0403  -0.2540 0.1085  191 GLN   J CB  
17867 C  CG  . GLN   J  191 ? 2.0406 0.7040 1.2570 0.0501  -0.2839 0.0804  191 GLN   J CG  
17868 C  CD  . GLN   J  191 ? 2.0077 0.7373 1.2663 0.0439  -0.3415 0.0727  191 GLN   J CD  
17869 O  OE1 . GLN   J  191 ? 1.9825 0.8443 1.1986 0.0545  -0.4347 0.0302  191 GLN   J OE1 
17870 N  NE2 . GLN   J  191 ? 1.9956 0.7118 1.3104 0.0567  -0.3272 0.0886  191 GLN   J NE2 
17871 N  N   . VAL   J  192 ? 2.1778 0.7972 1.3078 -0.0222 -0.1785 0.1332  192 VAL   J N   
17872 C  CA  . VAL   J  192 ? 2.2135 0.8740 1.3247 -0.0351 -0.1588 0.0915  192 VAL   J CA  
17873 C  C   . VAL   J  192 ? 2.2517 0.9879 1.4053 -0.0964 -0.2297 0.0465  192 VAL   J C   
17874 O  O   . VAL   J  192 ? 2.2924 0.8995 1.2965 -0.1082 -0.2685 -0.0506 192 VAL   J O   
17875 C  CB  . VAL   J  192 ? 2.1447 0.8259 1.3056 -0.0802 -0.0739 0.0946  192 VAL   J CB  
17876 C  CG1 . VAL   J  192 ? 2.1795 0.8655 1.2854 -0.0600 -0.0595 0.0924  192 VAL   J CG1 
17877 C  CG2 . VAL   J  192 ? 2.1375 0.7916 1.2830 -0.0745 -0.0115 0.1180  192 VAL   J CG2 
17878 N  N   . ASP   J  193 ? 2.3854 1.2104 1.4390 -0.0714 -0.2911 0.0872  193 ASP   J N   
17879 C  CA  . ASP   J  193 ? 2.3797 1.3256 1.5341 -0.0743 -0.2929 0.1251  193 ASP   J CA  
17880 C  C   . ASP   J  193 ? 2.3961 1.3547 1.4978 -0.0711 -0.2549 0.0896  193 ASP   J C   
17881 O  O   . ASP   J  193 ? 2.3910 1.5910 1.5358 -0.1615 -0.2690 0.0804  193 ASP   J O   
17882 C  CB  . ASP   J  193 ? 2.4132 1.3802 1.6057 -0.0363 -0.3174 0.1412  193 ASP   J CB  
17883 C  CG  . ASP   J  193 ? 2.4706 1.3075 1.6020 0.0251  -0.3289 0.1872  193 ASP   J CG  
17884 O  OD1 . ASP   J  193 ? 2.5245 1.4949 1.6821 -0.0009 -0.2157 0.0262  193 ASP   J OD1 
17885 O  OD2 . ASP   J  193 ? 2.5628 1.1584 1.6436 0.0028  -0.3298 0.1520  193 ASP   J OD2 
17886 N  N   . ASP   J  194 ? 2.4701 1.3272 1.4553 -0.0247 -0.2382 0.1055  194 ASP   J N   
17887 C  CA  . ASP   J  194 ? 2.4796 1.2943 1.5558 0.0324  -0.1963 0.1305  194 ASP   J CA  
17888 C  C   . ASP   J  194 ? 2.4921 1.1774 1.5264 0.0189  -0.1817 0.0992  194 ASP   J C   
17889 O  O   . ASP   J  194 ? 2.5453 1.3456 1.5869 0.0107  -0.1170 0.0755  194 ASP   J O   
17890 C  CB  . ASP   J  194 ? 2.5121 1.3515 1.5616 0.0521  -0.1930 0.2264  194 ASP   J CB  
17891 C  CG  . ASP   J  194 ? 2.5319 1.4122 1.6035 0.0354  -0.1507 0.2489  194 ASP   J CG  
17892 O  OD1 . ASP   J  194 ? 2.5004 1.0998 1.5745 0.0147  -0.1266 0.3751  194 ASP   J OD1 
17893 O  OD2 . ASP   J  194 ? 2.5554 1.6901 1.5233 -0.0063 -0.1403 0.2495  194 ASP   J OD2 
17894 N  N   . PHE   J  195 ? 2.3830 0.9828 1.5330 -0.0298 -0.2039 0.0414  195 PHE   J N   
17895 C  CA  . PHE   J  195 ? 2.2869 0.9643 1.5521 -0.0632 -0.2198 -0.0042 195 PHE   J CA  
17896 C  C   . PHE   J  195 ? 2.2564 0.8444 1.6813 -0.0138 -0.2347 -0.0990 195 PHE   J C   
17897 O  O   . PHE   J  195 ? 2.1828 0.4421 1.9008 -0.0584 -0.2417 0.1236  195 PHE   J O   
17898 C  CB  . PHE   J  195 ? 2.2664 0.9762 1.5430 -0.0224 -0.1868 -0.0548 195 PHE   J CB  
17899 C  CG  . PHE   J  195 ? 2.2778 1.0190 1.4924 0.0139  -0.1788 -0.1005 195 PHE   J CG  
17900 C  CD1 . PHE   J  195 ? 2.2339 1.0339 1.4620 0.0871  -0.1797 -0.1108 195 PHE   J CD1 
17901 C  CD2 . PHE   J  195 ? 2.2809 0.9708 1.4453 0.0324  -0.1597 -0.1385 195 PHE   J CD2 
17902 C  CE1 . PHE   J  195 ? 2.2659 0.9471 1.4146 0.1300  -0.1575 -0.1085 195 PHE   J CE1 
17903 C  CE2 . PHE   J  195 ? 2.2929 0.9520 1.4050 0.0771  -0.1257 -0.1580 195 PHE   J CE2 
17904 C  CZ  . PHE   J  195 ? 2.2581 0.9517 1.4266 0.1302  -0.1329 -0.1564 195 PHE   J CZ  
17905 N  N   . THR   K  1   ? 1.7049 0.6230 1.3302 -0.1297 -0.4291 -0.1069 2   THR   K N   
17906 C  CA  . THR   K  1   ? 1.7221 0.6385 1.2784 -0.1193 -0.4612 -0.1556 2   THR   K CA  
17907 C  C   . THR   K  1   ? 1.7322 0.6589 1.2357 -0.1132 -0.4470 -0.1397 2   THR   K C   
17908 O  O   . THR   K  1   ? 1.7081 0.6610 1.1112 -0.1714 -0.5025 -0.2231 2   THR   K O   
17909 C  CB  . THR   K  1   ? 1.7482 0.6728 1.2115 -0.0951 -0.4661 -0.1628 2   THR   K CB  
17910 O  OG1 . THR   K  1   ? 1.7517 0.6695 1.1597 -0.1102 -0.4837 -0.1834 2   THR   K OG1 
17911 C  CG2 . THR   K  1   ? 1.7606 0.6530 1.1776 -0.0901 -0.4888 -0.1913 2   THR   K CG2 
17912 N  N   . THR   K  2   ? 1.7231 0.6630 1.2534 -0.0728 -0.3975 -0.1056 3   THR   K N   
17913 C  CA  . THR   K  2   ? 1.7014 0.6714 1.2816 -0.0571 -0.3742 -0.0823 3   THR   K CA  
17914 C  C   . THR   K  2   ? 1.7152 0.5999 1.2723 -0.0711 -0.3721 -0.1036 3   THR   K C   
17915 O  O   . THR   K  2   ? 1.6977 0.6256 1.2913 -0.0840 -0.3577 -0.1254 3   THR   K O   
17916 C  CB  . THR   K  2   ? 1.6539 0.5899 1.2757 -0.0187 -0.3779 -0.0379 3   THR   K CB  
17917 O  OG1 . THR   K  2   ? 1.6369 0.6207 1.2772 0.0195  -0.3717 0.0339  3   THR   K OG1 
17918 C  CG2 . THR   K  2   ? 1.6526 0.5692 1.2746 -0.0034 -0.3801 -0.0224 3   THR   K CG2 
17919 N  N   . LEU   K  3   ? 1.7194 0.5888 1.2658 -0.0773 -0.3654 -0.1062 4   LEU   K N   
17920 C  CA  . LEU   K  3   ? 1.7344 0.7304 1.2972 -0.0886 -0.3429 -0.0831 4   LEU   K CA  
17921 C  C   . LEU   K  3   ? 1.7016 0.7370 1.2359 -0.0793 -0.3812 -0.1196 4   LEU   K C   
17922 O  O   . LEU   K  3   ? 1.6669 0.7911 1.1880 -0.0849 -0.4290 -0.1063 4   LEU   K O   
17923 C  CB  . LEU   K  3   ? 1.7957 0.7875 1.3221 -0.0829 -0.2860 -0.1111 4   LEU   K CB  
17924 C  CG  . LEU   K  3   ? 1.7564 0.9192 1.3910 -0.0698 -0.3137 -0.0101 4   LEU   K CG  
17925 C  CD1 . LEU   K  3   ? 1.7601 0.9745 1.4006 -0.0509 -0.2945 0.0036  4   LEU   K CD1 
17926 C  CD2 . LEU   K  3   ? 1.7491 0.9541 1.3992 -0.0614 -0.3162 0.0195  4   LEU   K CD2 
17927 N  N   . ALA   K  4   ? 1.7241 0.7232 1.2022 -0.1010 -0.4117 -0.1164 5   ALA   K N   
17928 C  CA  . ALA   K  4   ? 1.7645 0.7319 1.2144 -0.1052 -0.4647 -0.1150 5   ALA   K CA  
17929 C  C   . ALA   K  4   ? 1.8099 0.7196 1.1963 -0.1308 -0.4628 -0.1041 5   ALA   K C   
17930 O  O   . ALA   K  4   ? 1.7917 0.7876 1.1761 -0.1625 -0.4931 -0.1004 5   ALA   K O   
17931 C  CB  . ALA   K  4   ? 1.7722 0.7385 1.2009 -0.0942 -0.4590 -0.1186 5   ALA   K CB  
17932 N  N   . PHE   K  5   ? 1.8547 0.6751 1.2462 -0.1222 -0.4871 -0.0663 6   PHE   K N   
17933 C  CA  . PHE   K  5   ? 1.8998 0.7506 1.2846 -0.1223 -0.4507 -0.0627 6   PHE   K CA  
17934 C  C   . PHE   K  5   ? 1.9435 0.7471 1.2864 -0.1133 -0.4717 -0.0816 6   PHE   K C   
17935 O  O   . PHE   K  5   ? 1.9431 0.7384 1.2871 -0.1095 -0.4968 -0.1585 6   PHE   K O   
17936 C  CB  . PHE   K  5   ? 1.8925 0.6898 1.3425 -0.1061 -0.4653 -0.0219 6   PHE   K CB  
17937 C  CG  . PHE   K  5   ? 1.8891 0.7120 1.4250 -0.0879 -0.5067 0.0295  6   PHE   K CG  
17938 C  CD1 . PHE   K  5   ? 1.9262 0.8266 1.4506 -0.1230 -0.5477 0.0724  6   PHE   K CD1 
17939 C  CD2 . PHE   K  5   ? 1.8599 0.6406 1.4517 -0.0304 -0.5161 0.0399  6   PHE   K CD2 
17940 C  CE1 . PHE   K  5   ? 1.9429 0.8714 1.4820 -0.1289 -0.5714 0.0782  6   PHE   K CE1 
17941 C  CE2 . PHE   K  5   ? 1.8610 0.6749 1.5017 -0.0192 -0.5369 0.0600  6   PHE   K CE2 
17942 C  CZ  . PHE   K  5   ? 1.9249 0.7975 1.4756 -0.0742 -0.5805 0.0808  6   PHE   K CZ  
17943 N  N   . ARG   K  6   ? 2.0072 0.8246 1.3069 -0.1458 -0.4449 -0.0625 7   ARG   K N   
17944 C  CA  . ARG   K  6   ? 2.0452 0.8932 1.3637 -0.1300 -0.4525 0.0053  7   ARG   K CA  
17945 C  C   . ARG   K  6   ? 2.0832 1.0028 1.3329 -0.1595 -0.5076 0.0615  7   ARG   K C   
17946 O  O   . ARG   K  6   ? 2.0534 1.0540 1.2234 -0.1000 -0.5184 0.1211  7   ARG   K O   
17947 C  CB  . ARG   K  6   ? 2.0639 0.8508 1.3631 -0.1277 -0.3964 -0.0168 7   ARG   K CB  
17948 C  CG  . ARG   K  6   ? 2.0650 0.8453 1.3980 -0.0866 -0.3477 -0.0080 7   ARG   K CG  
17949 C  CD  . ARG   K  6   ? 2.0603 0.8220 1.3899 -0.0908 -0.2823 -0.0376 7   ARG   K CD  
17950 N  NE  . ARG   K  6   ? 2.1125 0.8670 1.4068 -0.1347 -0.2475 -0.0653 7   ARG   K NE  
17951 C  CZ  . ARG   K  6   ? 2.1632 0.9359 1.3536 -0.1303 -0.2188 -0.0411 7   ARG   K CZ  
17952 N  NH1 . ARG   K  6   ? 2.1594 0.9315 1.3741 -0.0854 -0.2490 -0.0061 7   ARG   K NH1 
17953 N  NH2 . ARG   K  6   ? 2.2551 0.9784 1.3612 -0.1396 -0.1879 -0.0599 7   ARG   K NH2 
17954 N  N   . PHE   K  7   ? 2.0902 0.9814 1.4914 -0.1340 -0.5172 0.1074  8   PHE   K N   
17955 C  CA  . PHE   K  7   ? 2.1222 1.0314 1.4937 -0.1543 -0.5513 0.1624  8   PHE   K CA  
17956 C  C   . PHE   K  7   ? 2.1272 1.0138 1.5335 -0.1662 -0.6013 0.1498  8   PHE   K C   
17957 O  O   . PHE   K  7   ? 2.1024 0.9388 1.5299 -0.1669 -0.6161 0.2079  8   PHE   K O   
17958 C  CB  . PHE   K  7   ? 2.1361 1.0320 1.5936 -0.1642 -0.5450 0.2010  8   PHE   K CB  
17959 C  CG  . PHE   K  7   ? 2.1574 0.9398 1.6205 -0.1221 -0.5366 0.2603  8   PHE   K CG  
17960 C  CD1 . PHE   K  7   ? 2.1276 0.7907 1.6385 -0.0908 -0.5247 0.2631  8   PHE   K CD1 
17961 C  CD2 . PHE   K  7   ? 2.2203 0.9450 1.6462 -0.1434 -0.5760 0.3178  8   PHE   K CD2 
17962 C  CE1 . PHE   K  7   ? 2.1383 0.7013 1.6381 -0.0742 -0.5209 0.2988  8   PHE   K CE1 
17963 C  CE2 . PHE   K  7   ? 2.2405 0.8602 1.6578 -0.1191 -0.5548 0.3378  8   PHE   K CE2 
17964 C  CZ  . PHE   K  7   ? 2.1839 0.7292 1.6670 -0.0847 -0.5599 0.3324  8   PHE   K CZ  
17965 N  N   . GLN   K  8   ? 2.1912 1.1586 1.5422 -0.2002 -0.6291 0.1974  9   GLN   K N   
17966 C  CA  . GLN   K  8   ? 2.2866 1.1492 1.5677 -0.2531 -0.6359 0.2418  9   GLN   K CA  
17967 C  C   . GLN   K  8   ? 2.2846 1.0470 1.6084 -0.2374 -0.6591 0.2593  9   GLN   K C   
17968 O  O   . GLN   K  8   ? 2.2493 1.0484 1.5971 -0.2910 -0.6898 0.2731  9   GLN   K O   
17969 C  CB  . GLN   K  8   ? 2.3500 1.3284 1.5695 -0.2907 -0.6583 0.2288  9   GLN   K CB  
17970 C  CG  . GLN   K  8   ? 2.3663 1.4334 1.6514 -0.2986 -0.7380 0.2245  9   GLN   K CG  
17971 C  CD  . GLN   K  8   ? 2.3182 1.4877 1.7053 -0.2841 -0.7758 0.2185  9   GLN   K CD  
17972 O  OE1 . GLN   K  8   ? 2.2622 1.4813 1.6715 -0.2524 -0.8592 0.2057  9   GLN   K OE1 
17973 N  NE2 . GLN   K  8   ? 2.4008 1.5349 1.7689 -0.2726 -0.7378 0.1551  9   GLN   K NE2 
17974 N  N   . GLY   K  9   ? 2.2368 0.9984 1.6557 -0.1826 -0.6341 0.2473  10  GLY   K N   
17975 C  CA  . GLY   K  9   ? 2.2082 0.8793 1.6666 -0.1433 -0.6950 0.2532  10  GLY   K CA  
17976 C  C   . GLY   K  9   ? 2.1305 0.7634 1.6643 -0.0875 -0.6897 0.2674  10  GLY   K C   
17977 O  O   . GLY   K  9   ? 2.1291 0.7789 1.6969 -0.0502 -0.7448 0.2697  10  GLY   K O   
17978 N  N   . GLY   K  10  ? 2.1037 0.7836 1.5926 -0.1088 -0.6673 0.2335  11  GLY   K N   
17979 C  CA  . GLY   K  10  ? 2.0712 0.7770 1.6086 -0.0848 -0.6304 0.1946  11  GLY   K CA  
17980 C  C   . GLY   K  10  ? 2.0169 0.8061 1.5297 -0.0644 -0.6248 0.1439  11  GLY   K C   
17981 O  O   . GLY   K  10  ? 1.9997 0.8680 1.5877 -0.0519 -0.6186 0.1486  11  GLY   K O   
17982 N  N   . ILE   K  11  ? 1.9623 0.7644 1.5006 -0.0343 -0.6542 0.0897  12  ILE   K N   
17983 C  CA  . ILE   K  11  ? 1.9339 0.7108 1.5051 -0.0292 -0.6137 0.0822  12  ILE   K CA  
17984 C  C   . ILE   K  11  ? 1.9039 0.6879 1.4579 -0.0339 -0.6373 0.0250  12  ILE   K C   
17985 O  O   . ILE   K  11  ? 1.9457 0.4568 1.4106 -0.0409 -0.6882 0.0666  12  ILE   K O   
17986 C  CB  . ILE   K  11  ? 1.8985 0.7370 1.5492 -0.0214 -0.6108 0.0578  12  ILE   K CB  
17987 C  CG1 . ILE   K  11  ? 1.9242 0.8345 1.5741 -0.0255 -0.5660 0.1157  12  ILE   K CG1 
17988 C  CG2 . ILE   K  11  ? 1.8665 0.6997 1.5510 -0.0067 -0.5720 0.0502  12  ILE   K CG2 
17989 C  CD1 . ILE   K  11  ? 1.8959 0.8498 1.5652 0.0020  -0.5707 0.1047  12  ILE   K CD1 
17990 N  N   . ILE   K  12  ? 1.9340 0.6793 1.4333 -0.0643 -0.6311 0.0138  13  ILE   K N   
17991 C  CA  . ILE   K  12  ? 1.9136 0.7211 1.4277 -0.0378 -0.6096 0.0390  13  ILE   K CA  
17992 C  C   . ILE   K  12  ? 1.8899 0.5831 1.3736 -0.0463 -0.5584 -0.0023 13  ILE   K C   
17993 O  O   . ILE   K  12  ? 1.8722 0.5164 1.3551 -0.0940 -0.5591 -0.0187 13  ILE   K O   
17994 C  CB  . ILE   K  12  ? 1.9502 0.7575 1.4416 -0.0275 -0.6127 0.0125  13  ILE   K CB  
17995 C  CG1 . ILE   K  12  ? 1.9782 0.8926 1.4851 -0.0297 -0.6458 0.0348  13  ILE   K CG1 
17996 C  CG2 . ILE   K  12  ? 1.9140 0.7753 1.4473 -0.0212 -0.5934 0.0230  13  ILE   K CG2 
17997 C  CD1 . ILE   K  12  ? 1.9761 0.9108 1.5211 -0.0197 -0.6430 0.0445  13  ILE   K CD1 
17998 N  N   . VAL   K  13  ? 1.8529 0.5450 1.3866 -0.0386 -0.5576 -0.0085 14  VAL   K N   
17999 C  CA  . VAL   K  13  ? 1.8251 0.5890 1.3547 -0.0323 -0.5280 -0.0424 14  VAL   K CA  
18000 C  C   . VAL   K  13  ? 1.8216 0.5967 1.3574 -0.0477 -0.5161 -0.1008 14  VAL   K C   
18001 O  O   . VAL   K  13  ? 1.8335 0.6950 1.4281 -0.0111 -0.5453 -0.1501 14  VAL   K O   
18002 C  CB  . VAL   K  13  ? 1.7733 0.5368 1.3469 -0.0409 -0.5326 -0.0054 14  VAL   K CB  
18003 C  CG1 . VAL   K  13  ? 1.7232 0.5340 1.3514 -0.0361 -0.5144 0.0145  14  VAL   K CG1 
18004 C  CG2 . VAL   K  13  ? 1.7729 0.5576 1.3481 -0.0452 -0.5292 0.0009  14  VAL   K CG2 
18005 N  N   . ALA   K  14  ? 1.8474 0.5696 1.2769 -0.0795 -0.5079 -0.1064 15  ALA   K N   
18006 C  CA  . ALA   K  14  ? 1.8409 0.5755 1.2712 -0.0942 -0.5008 -0.1250 15  ALA   K CA  
18007 C  C   . ALA   K  14  ? 1.8130 0.4898 1.2381 -0.1024 -0.4572 -0.1431 15  ALA   K C   
18008 O  O   . ALA   K  14  ? 1.8113 0.3812 1.2494 -0.1216 -0.4411 -0.1849 15  ALA   K O   
18009 C  CB  . ALA   K  14  ? 1.8569 0.5937 1.2568 -0.1282 -0.5255 -0.1259 15  ALA   K CB  
18010 N  N   . VAL   K  15  ? 1.7635 0.4917 1.2830 -0.0844 -0.4436 -0.1368 16  VAL   K N   
18011 C  CA  . VAL   K  15  ? 1.7185 0.5049 1.2848 -0.0348 -0.4165 -0.1243 16  VAL   K CA  
18012 C  C   . VAL   K  15  ? 1.6688 0.5098 1.3077 -0.0136 -0.4023 -0.1366 16  VAL   K C   
18013 O  O   . VAL   K  15  ? 1.6613 0.5715 1.3209 0.0541  -0.3916 -0.1314 16  VAL   K O   
18014 C  CB  . VAL   K  15  ? 1.7233 0.4587 1.2579 -0.0078 -0.4022 -0.0892 16  VAL   K CB  
18015 C  CG1 . VAL   K  15  ? 1.7347 0.4816 1.2497 -0.0017 -0.3984 -0.0527 16  VAL   K CG1 
18016 C  CG2 . VAL   K  15  ? 1.7155 0.4174 1.2745 -0.0109 -0.4067 -0.0868 16  VAL   K CG2 
18017 N  N   . ASP   K  16  ? 1.6116 0.5270 1.3083 0.0061  -0.4409 -0.1590 17  ASP   K N   
18018 C  CA  . ASP   K  16  ? 1.6066 0.5757 1.3755 -0.0177 -0.4653 -0.1257 17  ASP   K CA  
18019 C  C   . ASP   K  16  ? 1.5851 0.6621 1.3619 0.0168  -0.4670 -0.1126 17  ASP   K C   
18020 O  O   . ASP   K  16  ? 1.5137 0.7386 1.3716 -0.0835 -0.5345 -0.1050 17  ASP   K O   
18021 C  CB  . ASP   K  16  ? 1.6015 0.5599 1.4143 -0.0517 -0.4678 -0.0807 17  ASP   K CB  
18022 C  CG  . ASP   K  16  ? 1.5719 0.5012 1.4558 -0.0873 -0.4900 -0.1134 17  ASP   K CG  
18023 O  OD1 . ASP   K  16  ? 1.5901 0.4964 1.4712 -0.0867 -0.4866 -0.1503 17  ASP   K OD1 
18024 O  OD2 . ASP   K  16  ? 1.5386 0.5401 1.5604 -0.1334 -0.4616 -0.0754 17  ASP   K OD2 
18025 N  N   . SER   K  17  ? 1.6146 0.5536 1.4130 0.0063  -0.4838 -0.0960 18  SER   K N   
18026 C  CA  . SER   K  17  ? 1.6060 0.6082 1.4376 0.0074  -0.4491 -0.0769 18  SER   K CA  
18027 C  C   . SER   K  17  ? 1.6507 0.5716 1.4806 0.0024  -0.4288 -0.0640 18  SER   K C   
18028 O  O   . SER   K  17  ? 1.6617 0.6376 1.5440 0.0238  -0.3989 -0.0049 18  SER   K O   
18029 C  CB  . SER   K  17  ? 1.5856 0.6183 1.4624 -0.0529 -0.4801 -0.0881 18  SER   K CB  
18030 O  OG  . SER   K  17  ? 1.6212 0.4988 1.4569 0.0172  -0.5054 -0.1257 18  SER   K OG  
18031 N  N   . ARG   K  18  ? 1.6280 0.5683 1.4788 0.0037  -0.4101 -0.1577 19  ARG   K N   
18032 C  CA  . ARG   K  18  ? 1.6210 0.6283 1.4464 -0.0039 -0.4176 -0.1552 19  ARG   K CA  
18033 C  C   . ARG   K  18  ? 1.6295 0.5338 1.4242 0.0122  -0.3988 -0.1994 19  ARG   K C   
18034 O  O   . ARG   K  18  ? 1.6080 0.4626 1.4063 0.0600  -0.4029 -0.2307 19  ARG   K O   
18035 C  CB  . ARG   K  18  ? 1.6213 0.6519 1.4526 0.0014  -0.3783 -0.1713 19  ARG   K CB  
18036 C  CG  . ARG   K  18  ? 1.6204 0.7354 1.4504 -0.0321 -0.3476 -0.1404 19  ARG   K CG  
18037 C  CD  . ARG   K  18  ? 1.6451 0.7362 1.4893 -0.0509 -0.3149 -0.1592 19  ARG   K CD  
18038 N  NE  . ARG   K  18  ? 1.6229 0.8300 1.5528 -0.0838 -0.2682 -0.1228 19  ARG   K NE  
18039 C  CZ  . ARG   K  18  ? 1.6481 0.9168 1.5739 -0.1310 -0.2567 -0.1970 19  ARG   K CZ  
18040 N  NH1 . ARG   K  18  ? 1.6501 0.9813 1.5973 -0.1295 -0.2386 -0.2010 19  ARG   K NH1 
18041 N  NH2 . ARG   K  18  ? 1.6246 1.0151 1.5785 -0.1303 -0.2675 -0.2199 19  ARG   K NH2 
18042 N  N   . ALA   K  19  ? 1.6516 0.5754 1.4240 -0.0051 -0.3961 -0.2087 20  ALA   K N   
18043 C  CA  . ALA   K  19  ? 1.6515 0.6570 1.4264 0.0080  -0.4068 -0.1911 20  ALA   K CA  
18044 C  C   . ALA   K  19  ? 1.6349 0.5943 1.4206 -0.0049 -0.4306 -0.2350 20  ALA   K C   
18045 O  O   . ALA   K  19  ? 1.6421 0.4477 1.3987 -0.0059 -0.4777 -0.2956 20  ALA   K O   
18046 C  CB  . ALA   K  19  ? 1.6656 0.6927 1.4512 0.0183  -0.3756 -0.2046 20  ALA   K CB  
18047 N  N   . THR   K  20  ? 1.6358 0.7464 1.4405 0.0365  -0.4097 -0.2225 21  THR   K N   
18048 C  CA  . THR   K  20  ? 1.6775 0.8889 1.4538 0.0700  -0.3674 -0.1319 21  THR   K CA  
18049 C  C   . THR   K  20  ? 1.7220 1.0865 1.4222 0.0577  -0.3910 -0.0647 21  THR   K C   
18050 O  O   . THR   K  20  ? 1.6697 1.1947 1.2757 0.0349  -0.4307 0.0028  21  THR   K O   
18051 C  CB  . THR   K  20  ? 1.6249 0.9592 1.5060 0.1183  -0.3507 -0.1281 21  THR   K CB  
18052 O  OG1 . THR   K  20  ? 1.5455 0.9506 1.5494 0.2118  -0.3103 -0.1860 21  THR   K OG1 
18053 C  CG2 . THR   K  20  ? 1.6136 0.9725 1.4956 0.1229  -0.3449 -0.1271 21  THR   K CG2 
18054 N  N   . ALA   K  21  ? 1.8132 1.1857 1.4948 0.0810  -0.3657 0.0215  22  ALA   K N   
18055 C  CA  . ALA   K  21  ? 1.8225 1.2566 1.5237 0.1154  -0.3781 0.0348  22  ALA   K CA  
18056 C  C   . ALA   K  21  ? 1.8599 1.2621 1.6509 0.1542  -0.3359 0.0071  22  ALA   K C   
18057 O  O   . ALA   K  21  ? 1.8046 1.3182 1.6593 0.1341  -0.3190 -0.0486 22  ALA   K O   
18058 C  CB  . ALA   K  21  ? 1.8887 1.3196 1.5065 0.0796  -0.3391 0.0340  22  ALA   K CB  
18059 N  N   . GLY   K  22  ? 1.8672 1.2502 1.7071 0.1528  -0.3205 0.0042  23  GLY   K N   
18060 C  CA  . GLY   K  22  ? 1.9384 1.2027 1.6912 0.1244  -0.3955 0.0621  23  GLY   K CA  
18061 C  C   . GLY   K  22  ? 1.9414 1.0877 1.7096 0.1466  -0.4162 0.0804  23  GLY   K C   
18062 O  O   . GLY   K  22  ? 2.0363 1.1538 1.6419 0.0990  -0.4391 0.0215  23  GLY   K O   
18063 N  N   . ASN   K  23  ? 1.8901 1.0628 1.7218 0.1564  -0.4607 0.0681  24  ASN   K N   
18064 C  CA  . ASN   K  23  ? 1.8497 1.1227 1.7007 0.1650  -0.4763 0.0783  24  ASN   K CA  
18065 C  C   . ASN   K  23  ? 1.8279 0.9710 1.6120 0.1275  -0.5203 0.0661  24  ASN   K C   
18066 O  O   . ASN   K  23  ? 1.7796 1.0284 1.5707 0.1171  -0.5105 0.0629  24  ASN   K O   
18067 C  CB  . ASN   K  23  ? 1.9594 1.1397 1.7678 0.1828  -0.4817 0.0966  24  ASN   K CB  
18068 C  CG  . ASN   K  23  ? 1.9853 1.2378 1.7883 0.1727  -0.4356 0.0964  24  ASN   K CG  
18069 O  OD1 . ASN   K  23  ? 2.0441 1.2923 1.7231 0.1339  -0.4883 0.0764  24  ASN   K OD1 
18070 N  ND2 . ASN   K  23  ? 2.0622 1.2731 1.8285 0.1772  -0.4477 0.1549  24  ASN   K ND2 
18071 N  N   . TRP   K  24  ? 1.7976 0.8781 1.6162 0.1304  -0.5165 0.1263  25  TRP   K N   
18072 C  CA  . TRP   K  24  ? 1.7769 0.8308 1.6081 0.1036  -0.5386 0.1118  25  TRP   K CA  
18073 C  C   . TRP   K  24  ? 1.7362 0.8210 1.6002 0.1347  -0.5714 0.0754  25  TRP   K C   
18074 O  O   . TRP   K  24  ? 1.7199 0.8348 1.6754 0.1458  -0.5501 0.1030  25  TRP   K O   
18075 C  CB  . TRP   K  24  ? 1.7644 0.8257 1.5991 0.0966  -0.5097 0.1448  25  TRP   K CB  
18076 C  CG  . TRP   K  24  ? 1.7097 0.8880 1.5759 0.0876  -0.4950 0.1166  25  TRP   K CG  
18077 C  CD1 . TRP   K  24  ? 1.7186 0.9036 1.5564 0.0872  -0.4855 0.0412  25  TRP   K CD1 
18078 C  CD2 . TRP   K  24  ? 1.7195 0.8531 1.5895 0.0456  -0.4911 0.1167  25  TRP   K CD2 
18079 N  NE1 . TRP   K  24  ? 1.6943 0.9491 1.5760 0.0513  -0.4561 -0.0004 25  TRP   K NE1 
18080 C  CE2 . TRP   K  24  ? 1.7053 0.9046 1.6071 0.0577  -0.4657 0.0330  25  TRP   K CE2 
18081 C  CE3 . TRP   K  24  ? 1.7374 0.8128 1.5994 0.0693  -0.5098 0.1191  25  TRP   K CE3 
18082 C  CZ2 . TRP   K  24  ? 1.7049 0.9009 1.6501 0.0212  -0.4475 0.0317  25  TRP   K CZ2 
18083 C  CZ3 . TRP   K  24  ? 1.7403 0.8597 1.6277 0.0321  -0.4926 0.0856  25  TRP   K CZ3 
18084 C  CH2 . TRP   K  24  ? 1.7497 0.8694 1.6584 0.0291  -0.4512 0.0602  25  TRP   K CH2 
18085 N  N   . VAL   K  25  ? 1.7407 0.6988 1.5802 0.0711  -0.5549 0.0361  26  VAL   K N   
18086 C  CA  . VAL   K  25  ? 1.6935 0.6901 1.5075 0.0540  -0.5460 0.0152  26  VAL   K CA  
18087 C  C   . VAL   K  25  ? 1.6699 0.6832 1.4904 0.0551  -0.5177 0.0596  26  VAL   K C   
18088 O  O   . VAL   K  25  ? 1.6477 0.7119 1.4703 0.0749  -0.5354 0.0934  26  VAL   K O   
18089 C  CB  . VAL   K  25  ? 1.6816 0.6802 1.4879 0.0739  -0.5568 0.0362  26  VAL   K CB  
18090 C  CG1 . VAL   K  25  ? 1.6610 0.6435 1.4798 0.0593  -0.5614 0.0113  26  VAL   K CG1 
18091 C  CG2 . VAL   K  25  ? 1.6731 0.7183 1.4752 0.1058  -0.5603 0.0549  26  VAL   K CG2 
18092 N  N   . ALA   K  26  ? 1.7013 0.6494 1.4689 0.0750  -0.4695 0.0366  27  ALA   K N   
18093 C  CA  . ALA   K  26  ? 1.7328 0.6497 1.4809 0.0377  -0.4259 0.0181  27  ALA   K CA  
18094 C  C   . ALA   K  26  ? 1.7003 0.5978 1.4457 0.0132  -0.4151 -0.0134 27  ALA   K C   
18095 O  O   . ALA   K  26  ? 1.7062 0.5137 1.4964 -0.0662 -0.3854 -0.0720 27  ALA   K O   
18096 C  CB  . ALA   K  26  ? 1.7206 0.6713 1.4936 0.0386  -0.3964 0.0087  27  ALA   K CB  
18097 N  N   . SER   K  27  ? 1.7330 0.5761 1.4368 0.0443  -0.4334 -0.0014 28  SER   K N   
18098 C  CA  . SER   K  27  ? 1.7532 0.6326 1.4029 0.0487  -0.4358 0.0158  28  SER   K CA  
18099 C  C   . SER   K  27  ? 1.7579 0.4643 1.3932 0.0497  -0.4842 0.0342  28  SER   K C   
18100 O  O   . SER   K  27  ? 1.7732 0.2763 1.3162 0.0781  -0.5401 0.0266  28  SER   K O   
18101 C  CB  . SER   K  27  ? 1.7332 0.6382 1.4059 0.0552  -0.4257 0.0168  28  SER   K CB  
18102 O  OG  . SER   K  27  ? 1.7062 0.7678 1.4480 0.0946  -0.4316 0.0385  28  SER   K OG  
18103 N  N   . GLN   K  28  ? 1.7698 0.4812 1.4011 0.0018  -0.4978 0.0388  29  GLN   K N   
18104 C  CA  . GLN   K  28  ? 1.8216 0.5629 1.4029 -0.0055 -0.4656 0.0273  29  GLN   K CA  
18105 C  C   . GLN   K  28  ? 1.7724 0.6209 1.3487 -0.0160 -0.5075 0.0460  29  GLN   K C   
18106 O  O   . GLN   K  28  ? 1.7730 0.5441 1.3552 0.0041  -0.5382 0.0665  29  GLN   K O   
18107 C  CB  . GLN   K  28  ? 1.8469 0.5998 1.4475 -0.0403 -0.4469 0.0402  29  GLN   K CB  
18108 C  CG  . GLN   K  28  ? 1.8953 0.6338 1.4655 -0.0261 -0.4091 0.0896  29  GLN   K CG  
18109 C  CD  . GLN   K  28  ? 1.9628 0.5505 1.4833 -0.0462 -0.4149 0.0821  29  GLN   K CD  
18110 O  OE1 . GLN   K  28  ? 2.0065 0.6618 1.5007 -0.0400 -0.3769 0.1139  29  GLN   K OE1 
18111 N  NE2 . GLN   K  28  ? 1.9892 0.5758 1.4828 -0.0701 -0.4362 0.0486  29  GLN   K NE2 
18112 N  N   . THR   K  29  ? 1.7406 0.6519 1.3555 -0.0312 -0.4777 0.0225  30  THR   K N   
18113 C  CA  . THR   K  29  ? 1.7047 0.6532 1.3815 -0.0380 -0.4821 0.0177  30  THR   K CA  
18114 C  C   . THR   K  29  ? 1.6556 0.7230 1.4075 -0.0607 -0.4618 -0.0190 30  THR   K C   
18115 O  O   . THR   K  29  ? 1.6906 0.6689 1.4906 -0.1226 -0.4295 -0.0225 30  THR   K O   
18116 C  CB  . THR   K  29  ? 1.6799 0.6993 1.4027 -0.0983 -0.4790 0.0115  30  THR   K CB  
18117 O  OG1 . THR   K  29  ? 1.7357 0.7343 1.3795 -0.0926 -0.4981 0.0373  30  THR   K OG1 
18118 C  CG2 . THR   K  29  ? 1.6607 0.7214 1.3961 -0.1114 -0.4864 0.0170  30  THR   K CG2 
18119 N  N   . VAL   K  30  ? 1.6588 0.6743 1.3889 -0.0258 -0.4514 -0.0113 31  VAL   K N   
18120 C  CA  . VAL   K  30  ? 1.6202 0.6893 1.4594 -0.0200 -0.4338 0.0044  31  VAL   K CA  
18121 C  C   . VAL   K  30  ? 1.6409 0.6341 1.4134 0.0271  -0.4589 -0.0318 31  VAL   K C   
18122 O  O   . VAL   K  30  ? 1.6134 0.2539 1.4903 0.0691  -0.4868 -0.0015 31  VAL   K O   
18123 C  CB  . VAL   K  30  ? 1.6194 0.7647 1.4949 0.0025  -0.3996 0.0604  31  VAL   K CB  
18124 C  CG1 . VAL   K  30  ? 1.6263 0.8229 1.5524 -0.0197 -0.4074 0.0363  31  VAL   K CG1 
18125 C  CG2 . VAL   K  30  ? 1.5899 0.7146 1.5266 -0.0126 -0.3916 0.0720  31  VAL   K CG2 
18126 N  N   . LYS   K  31  ? 1.6752 0.6534 1.4487 -0.0176 -0.4423 -0.1014 32  LYS   K N   
18127 C  CA  . LYS   K  31  ? 1.7120 0.6356 1.4299 -0.0169 -0.4314 -0.1284 32  LYS   K CA  
18128 C  C   . LYS   K  31  ? 1.7037 0.6340 1.4279 0.0211  -0.4176 -0.1861 32  LYS   K C   
18129 O  O   . LYS   K  31  ? 1.7308 0.6978 1.3962 0.1148  -0.3827 -0.2533 32  LYS   K O   
18130 C  CB  . LYS   K  31  ? 1.7559 0.6982 1.4974 0.0623  -0.4077 -0.0819 32  LYS   K CB  
18131 C  CG  . LYS   K  31  ? 1.7615 0.8440 1.5981 0.0321  -0.4066 -0.0475 32  LYS   K CG  
18132 C  CD  . LYS   K  31  ? 1.8723 0.8943 1.7274 0.0933  -0.3589 0.0198  32  LYS   K CD  
18133 C  CE  . LYS   K  31  ? 1.9252 0.9064 1.8088 0.0977  -0.3155 0.0551  32  LYS   K CE  
18134 N  NZ  . LYS   K  31  ? 1.9418 0.9147 1.9252 0.1239  -0.2975 0.0142  32  LYS   K NZ  
18135 N  N   . LYS   K  32  ? 1.6303 0.6689 1.3702 -0.0018 -0.4865 -0.2131 33  LYS   K N   
18136 C  CA  . LYS   K  32  ? 1.6249 0.6683 1.3529 0.0079  -0.5055 -0.1716 33  LYS   K CA  
18137 C  C   . LYS   K  32  ? 1.5839 0.6429 1.3555 0.0498  -0.5341 -0.1492 33  LYS   K C   
18138 O  O   . LYS   K  32  ? 1.5637 0.6124 1.3306 0.0724  -0.5722 -0.1469 33  LYS   K O   
18139 C  CB  . LYS   K  32  ? 1.6450 0.6637 1.3620 0.0125  -0.5032 -0.1595 33  LYS   K CB  
18140 C  CG  . LYS   K  32  ? 1.6738 0.7110 1.3724 0.0075  -0.4688 -0.1354 33  LYS   K CG  
18141 C  CD  . LYS   K  32  ? 1.6968 0.7265 1.3814 0.0207  -0.4584 -0.1431 33  LYS   K CD  
18142 C  CE  . LYS   K  32  ? 1.7240 0.7689 1.3871 0.0154  -0.4313 -0.1300 33  LYS   K CE  
18143 N  NZ  . LYS   K  32  ? 1.7484 0.7921 1.3911 0.0365  -0.4087 -0.1352 33  LYS   K NZ  
18144 N  N   . VAL   K  33  ? 1.6112 0.6061 1.3963 0.0657  -0.4965 -0.1114 34  VAL   K N   
18145 C  CA  . VAL   K  33  ? 1.6248 0.6257 1.4426 0.0604  -0.4651 -0.0878 34  VAL   K CA  
18146 C  C   . VAL   K  33  ? 1.5960 0.5659 1.4957 0.0639  -0.4820 -0.0646 34  VAL   K C   
18147 O  O   . VAL   K  33  ? 1.5997 0.4660 1.4852 0.0601  -0.4895 0.0043  34  VAL   K O   
18148 C  CB  . VAL   K  33  ? 1.6810 0.5899 1.4093 0.0596  -0.4345 -0.1031 34  VAL   K CB  
18149 C  CG1 . VAL   K  33  ? 1.7051 0.6072 1.4240 0.0716  -0.4359 -0.0767 34  VAL   K CG1 
18150 C  CG2 . VAL   K  33  ? 1.7210 0.5843 1.3902 0.0030  -0.4338 -0.1365 34  VAL   K CG2 
18151 N  N   . ILE   K  34  ? 1.5373 0.6375 1.5946 0.0508  -0.5024 -0.0705 35  ILE   K N   
18152 C  CA  . ILE   K  34  ? 1.5685 0.7686 1.7168 0.0921  -0.4622 -0.1830 35  ILE   K CA  
18153 C  C   . ILE   K  34  ? 1.6157 0.8198 1.7509 0.0945  -0.5271 -0.1550 35  ILE   K C   
18154 O  O   . ILE   K  34  ? 1.5475 0.8170 1.6855 0.1130  -0.5965 -0.1354 35  ILE   K O   
18155 C  CB  . ILE   K  34  ? 1.5686 0.8252 1.6860 0.0990  -0.4433 -0.1752 35  ILE   K CB  
18156 C  CG1 . ILE   K  34  ? 1.6052 0.9287 1.7175 0.0529  -0.3972 -0.2791 35  ILE   K CG1 
18157 C  CG2 . ILE   K  34  ? 1.5702 0.8122 1.6787 0.1420  -0.4504 -0.1467 35  ILE   K CG2 
18158 C  CD1 . ILE   K  34  ? 1.6480 0.9342 1.7696 0.0256  -0.3970 -0.2747 35  ILE   K CD1 
18159 N  N   . GLU   K  35  ? 1.6577 0.8223 1.8954 0.1317  -0.4967 -0.1995 36  GLU   K N   
18160 C  CA  . GLU   K  35  ? 1.6833 0.7691 1.9817 0.1327  -0.4992 -0.2241 36  GLU   K CA  
18161 C  C   . GLU   K  35  ? 1.6614 0.7587 1.9924 0.1009  -0.4391 -0.2198 36  GLU   K C   
18162 O  O   . GLU   K  35  ? 1.7660 0.6797 2.0383 0.0481  -0.3971 -0.2622 36  GLU   K O   
18163 C  CB  . GLU   K  35  ? 1.6725 0.8437 2.1292 0.1611  -0.4879 -0.3335 36  GLU   K CB  
18164 C  CG  . GLU   K  35  ? 1.6969 0.7995 2.1669 0.2001  -0.4698 -0.3733 36  GLU   K CG  
18165 C  CD  . GLU   K  35  ? 1.6740 0.8045 2.2494 0.2099  -0.4797 -0.4627 36  GLU   K CD  
18166 O  OE1 . GLU   K  35  ? 1.6363 0.9568 2.3106 0.3112  -0.4111 -0.4619 36  GLU   K OE1 
18167 O  OE2 . GLU   K  35  ? 1.7842 0.7790 2.3201 0.1554  -0.4919 -0.4643 36  GLU   K OE2 
18168 N  N   . ILE   K  36  ? 1.6521 0.6941 1.9089 0.0601  -0.4901 -0.1800 37  ILE   K N   
18169 C  CA  . ILE   K  36  ? 1.5939 0.7877 1.8516 -0.0088 -0.4701 -0.1514 37  ILE   K CA  
18170 C  C   . ILE   K  36  ? 1.6393 0.8379 1.8800 0.0112  -0.4878 -0.1289 37  ILE   K C   
18171 O  O   . ILE   K  36  ? 1.6205 0.8725 1.9310 -0.0346 -0.4578 -0.1802 37  ILE   K O   
18172 C  CB  . ILE   K  36  ? 1.6003 0.7755 1.7550 -0.0025 -0.4730 -0.1129 37  ILE   K CB  
18173 C  CG1 . ILE   K  36  ? 1.5759 0.7436 1.6393 -0.0670 -0.4448 -0.1063 37  ILE   K CG1 
18174 C  CG2 . ILE   K  36  ? 1.6092 0.7862 1.7673 -0.0056 -0.4743 -0.1368 37  ILE   K CG2 
18175 C  CD1 . ILE   K  36  ? 1.5654 0.7241 1.5746 -0.0798 -0.4518 -0.0872 37  ILE   K CD1 
18176 N  N   . ASN   K  37  ? 1.7171 0.8633 1.8974 0.0438  -0.5232 0.0001  38  ASN   K N   
18177 C  CA  . ASN   K  37  ? 1.7860 0.7578 2.0774 0.0679  -0.4998 -0.0109 38  ASN   K CA  
18178 C  C   . ASN   K  37  ? 1.7322 0.7588 2.0953 0.0891  -0.6024 0.0944  38  ASN   K C   
18179 O  O   . ASN   K  37  ? 1.7733 0.8514 2.0769 0.0423  -0.5913 -0.0662 38  ASN   K O   
18180 C  CB  . ASN   K  37  ? 1.8068 0.7201 2.1287 0.0875  -0.4849 -0.0250 38  ASN   K CB  
18181 C  CG  . ASN   K  37  ? 1.8255 0.7824 2.1755 0.0880  -0.4543 -0.0266 38  ASN   K CG  
18182 O  OD1 . ASN   K  37  ? 1.9425 0.6886 2.2120 0.0613  -0.4583 -0.0309 38  ASN   K OD1 
18183 N  ND2 . ASN   K  37  ? 1.8133 0.8889 2.1225 0.0896  -0.4858 -0.0745 38  ASN   K ND2 
18184 N  N   . PRO   K  38  ? 1.7712 0.6375 2.2201 0.1023  -0.5963 0.1191  39  PRO   K N   
18185 C  CA  . PRO   K  38  ? 1.8544 0.6069 2.2048 0.1407  -0.6332 0.1807  39  PRO   K CA  
18186 C  C   . PRO   K  38  ? 1.8802 0.4788 2.1487 0.2052  -0.6302 0.3279  39  PRO   K C   
18187 O  O   . PRO   K  38  ? 1.9909 0.4317 2.1305 0.1901  -0.6960 0.4256  39  PRO   K O   
18188 C  CB  . PRO   K  38  ? 1.8453 0.6614 2.3062 0.1896  -0.6692 0.1676  39  PRO   K CB  
18189 C  CG  . PRO   K  38  ? 1.7931 0.7731 2.3467 0.1214  -0.6540 0.0889  39  PRO   K CG  
18190 C  CD  . PRO   K  38  ? 1.7578 0.6774 2.2593 0.1247  -0.6091 0.0635  39  PRO   K CD  
18191 N  N   . PHE   K  39  ? 1.8727 0.5424 2.0232 0.1997  -0.6413 0.3451  40  PHE   K N   
18192 C  CA  . PHE   K  39  ? 1.9118 0.6866 1.9446 0.1846  -0.6295 0.3617  40  PHE   K CA  
18193 C  C   . PHE   K  39  ? 1.8135 0.6899 1.8632 0.2127  -0.5727 0.2660  40  PHE   K C   
18194 O  O   . PHE   K  39  ? 1.8213 0.8016 1.8589 0.2609  -0.5744 0.2677  40  PHE   K O   
18195 C  CB  . PHE   K  39  ? 1.9644 0.7742 1.9120 0.1523  -0.6165 0.4154  40  PHE   K CB  
18196 C  CG  . PHE   K  39  ? 2.0627 0.8907 1.9742 0.2047  -0.6361 0.4722  40  PHE   K CG  
18197 C  CD1 . PHE   K  39  ? 2.1718 1.0189 1.9545 0.2068  -0.5890 0.5359  40  PHE   K CD1 
18198 C  CD2 . PHE   K  39  ? 2.0854 0.8464 2.0043 0.2087  -0.6364 0.5121  40  PHE   K CD2 
18199 C  CE1 . PHE   K  39  ? 2.2205 0.9200 2.0401 0.2331  -0.5541 0.6411  40  PHE   K CE1 
18200 C  CE2 . PHE   K  39  ? 2.0964 0.8369 2.0980 0.2573  -0.6174 0.5937  40  PHE   K CE2 
18201 C  CZ  . PHE   K  39  ? 2.1740 0.9213 2.0166 0.2463  -0.6292 0.7007  40  PHE   K CZ  
18202 N  N   . LEU   K  40  ? 1.7731 0.6916 1.8346 0.1724  -0.5393 0.1842  41  LEU   K N   
18203 C  CA  . LEU   K  40  ? 1.7337 0.6353 1.7316 0.1157  -0.5214 0.1686  41  LEU   K CA  
18204 C  C   . LEU   K  40  ? 1.7714 0.6204 1.6998 0.1233  -0.5016 0.1578  41  LEU   K C   
18205 O  O   . LEU   K  40  ? 1.7977 0.3918 1.6721 0.1305  -0.4896 0.1850  41  LEU   K O   
18206 C  CB  . LEU   K  40  ? 1.6726 0.6849 1.7169 0.0987  -0.4916 0.1572  41  LEU   K CB  
18207 C  CG  . LEU   K  40  ? 1.6649 0.6727 1.6474 0.0570  -0.5324 0.1569  41  LEU   K CG  
18208 C  CD1 . LEU   K  40  ? 1.5969 0.6188 1.6142 0.0543  -0.4945 0.1769  41  LEU   K CD1 
18209 C  CD2 . LEU   K  40  ? 1.6796 0.7107 1.6010 0.0538  -0.5302 0.1521  41  LEU   K CD2 
18210 N  N   . LEU   K  41  ? 1.8133 0.5889 1.6236 0.1153  -0.5266 0.1922  42  LEU   K N   
18211 C  CA  . LEU   K  41  ? 1.8067 0.5606 1.5535 0.1417  -0.5336 0.1698  42  LEU   K CA  
18212 C  C   . LEU   K  41  ? 1.8210 0.5090 1.3986 0.1378  -0.5014 0.1546  42  LEU   K C   
18213 O  O   . LEU   K  41  ? 1.8381 0.3910 1.3601 0.1502  -0.4917 0.1683  42  LEU   K O   
18214 C  CB  . LEU   K  41  ? 1.8680 0.5427 1.6022 0.1197  -0.5477 0.1601  42  LEU   K CB  
18215 C  CG  . LEU   K  41  ? 1.8854 0.5980 1.6835 0.1096  -0.5626 0.1419  42  LEU   K CG  
18216 C  CD1 . LEU   K  41  ? 1.9251 0.6227 1.6902 0.1330  -0.5752 0.1123  42  LEU   K CD1 
18217 C  CD2 . LEU   K  41  ? 1.9006 0.6088 1.6842 0.1185  -0.5528 0.1226  42  LEU   K CD2 
18218 N  N   . GLY   K  42  ? 1.8034 0.6218 1.2898 0.1392  -0.5004 0.0973  43  GLY   K N   
18219 C  CA  . GLY   K  42  ? 1.7952 0.6991 1.2166 0.1664  -0.4896 0.0659  43  GLY   K CA  
18220 C  C   . GLY   K  42  ? 1.8165 0.6914 1.1692 0.2104  -0.5117 0.0976  43  GLY   K C   
18221 O  O   . GLY   K  42  ? 1.8005 0.6650 1.0815 0.2845  -0.5232 0.1105  43  GLY   K O   
18222 N  N   . THR   K  43  ? 1.7786 0.8339 1.1791 0.2403  -0.4756 0.0789  44  THR   K N   
18223 C  CA  . THR   K  43  ? 1.8021 0.8509 1.2646 0.1466  -0.4288 0.0777  44  THR   K CA  
18224 C  C   . THR   K  43  ? 1.7371 0.7408 1.2807 0.1054  -0.4203 0.0950  44  THR   K C   
18225 O  O   . THR   K  43  ? 1.7051 0.8058 1.2567 0.1055  -0.4375 0.1367  44  THR   K O   
18226 C  CB  . THR   K  43  ? 1.8468 0.9660 1.2364 0.1262  -0.4144 0.0399  44  THR   K CB  
18227 O  OG1 . THR   K  43  ? 1.8494 1.1030 1.3302 0.0901  -0.3719 -0.0378 44  THR   K OG1 
18228 C  CG2 . THR   K  43  ? 1.8240 1.0280 1.2807 0.0899  -0.4613 0.0578  44  THR   K CG2 
18229 N  N   . MET   K  44  ? 1.7113 0.6675 1.4121 0.0891  -0.4248 0.0738  45  MET   K N   
18230 C  CA  . MET   K  44  ? 1.6114 0.6737 1.4067 0.1122  -0.4409 0.0267  45  MET   K CA  
18231 C  C   . MET   K  44  ? 1.5837 0.6658 1.5213 0.0971  -0.4697 -0.0025 45  MET   K C   
18232 O  O   . MET   K  44  ? 1.6507 0.4344 1.6713 0.1685  -0.4787 -0.0038 45  MET   K O   
18233 C  CB  . MET   K  44  ? 1.6308 0.6856 1.3589 0.1195  -0.4425 0.0142  45  MET   K CB  
18234 C  CG  . MET   K  44  ? 1.6554 0.6928 1.3309 0.1359  -0.4169 0.0316  45  MET   K CG  
18235 S  SD  . MET   K  44  ? 1.7145 0.7794 1.3789 0.1495  -0.3618 0.0563  45  MET   K SD  
18236 C  CE  . MET   K  44  ? 1.7159 0.8149 1.4337 0.1892  -0.3271 0.0497  45  MET   K CE  
18237 N  N   . ALA   K  45  ? 1.5508 0.5795 1.5017 0.1413  -0.4032 -0.0184 46  ALA   K N   
18238 C  CA  . ALA   K  45  ? 1.5992 0.4925 1.4642 0.0759  -0.3361 -0.0470 46  ALA   K CA  
18239 C  C   . ALA   K  45  ? 1.5900 0.4444 1.4471 0.1119  -0.3136 -0.0181 46  ALA   K C   
18240 O  O   . ALA   K  45  ? 1.5430 0.5533 1.5072 0.0314  -0.3154 -0.0715 46  ALA   K O   
18241 C  CB  . ALA   K  45  ? 1.6103 0.4529 1.4845 0.0590  -0.3204 -0.0581 46  ALA   K CB  
18242 N  N   . GLY   K  46  ? 1.5767 0.4588 1.4197 0.1504  -0.3269 -0.0235 47  GLY   K N   
18243 C  CA  . GLY   K  46  ? 1.5371 0.5169 1.4273 0.1270  -0.3423 -0.0249 47  GLY   K CA  
18244 C  C   . GLY   K  46  ? 1.5015 0.5521 1.3563 0.0908  -0.3792 -0.0122 47  GLY   K C   
18245 O  O   . GLY   K  46  ? 1.4903 0.6352 1.4499 0.0989  -0.3533 0.0082  47  GLY   K O   
18246 N  N   . GLY   K  47  ? 1.4597 0.5960 1.3115 0.0530  -0.3775 0.0361  48  GLY   K N   
18247 C  CA  . GLY   K  47  ? 1.4482 0.5891 1.2677 0.0322  -0.3812 0.0745  48  GLY   K CA  
18248 C  C   . GLY   K  47  ? 1.4217 0.5831 1.2391 0.0208  -0.3871 0.0441  48  GLY   K C   
18249 O  O   . GLY   K  47  ? 1.4287 0.6128 1.1384 -0.0214 -0.3899 0.0131  48  GLY   K O   
18250 N  N   . ALA   K  48  ? 1.4464 0.5833 1.2499 -0.0151 -0.3799 0.0738  49  ALA   K N   
18251 C  CA  . ALA   K  48  ? 1.4472 0.6288 1.2672 -0.0018 -0.3777 0.0753  49  ALA   K CA  
18252 C  C   . ALA   K  48  ? 1.4439 0.6520 1.2081 0.0051  -0.3847 0.0659  49  ALA   K C   
18253 O  O   . ALA   K  48  ? 1.4979 0.6155 1.2760 0.0218  -0.3645 0.0630  49  ALA   K O   
18254 C  CB  . ALA   K  48  ? 1.4650 0.6525 1.3094 -0.0123 -0.3656 0.0905  49  ALA   K CB  
18255 N  N   . ALA   K  49  ? 1.4512 0.6675 1.1984 -0.0029 -0.3720 0.0426  50  ALA   K N   
18256 C  CA  . ALA   K  49  ? 1.4473 0.6007 1.2088 0.0049  -0.3630 0.0792  50  ALA   K CA  
18257 C  C   . ALA   K  49  ? 1.4499 0.5160 1.1684 0.0213  -0.3639 0.0360  50  ALA   K C   
18258 O  O   . ALA   K  49  ? 1.4711 0.5050 1.2804 0.0228  -0.3396 -0.0141 50  ALA   K O   
18259 C  CB  . ALA   K  49  ? 1.4791 0.6894 1.1770 -0.0440 -0.3505 0.0384  50  ALA   K CB  
18260 N  N   . ASP   K  50  ? 1.4682 0.4636 1.1195 0.0235  -0.3542 0.0376  51  ASP   K N   
18261 C  CA  . ASP   K  50  ? 1.4743 0.4874 1.1313 0.0055  -0.3387 -0.0024 51  ASP   K CA  
18262 C  C   . ASP   K  50  ? 1.4957 0.5965 1.1366 0.0526  -0.3631 -0.0099 51  ASP   K C   
18263 O  O   . ASP   K  50  ? 1.5278 0.6033 1.1858 0.0133  -0.3381 -0.0292 51  ASP   K O   
18264 C  CB  . ASP   K  50  ? 1.4583 0.5134 1.0710 -0.0018 -0.3437 0.0140  51  ASP   K CB  
18265 C  CG  . ASP   K  50  ? 1.4870 0.5919 1.0266 -0.0388 -0.3331 0.0083  51  ASP   K CG  
18266 O  OD1 . ASP   K  50  ? 1.4720 0.6193 1.0335 -0.0544 -0.3113 0.0130  51  ASP   K OD1 
18267 O  OD2 . ASP   K  50  ? 1.5025 0.6466 0.9997 -0.0064 -0.3494 0.0171  51  ASP   K OD2 
18268 N  N   . CYS   K  51  ? 1.5172 0.5705 1.1704 0.0705  -0.3892 -0.0167 52  CYS   K N   
18269 C  CA  . CYS   K  51  ? 1.5488 0.5787 1.1741 0.0898  -0.3971 -0.0117 52  CYS   K CA  
18270 C  C   . CYS   K  51  ? 1.5391 0.5979 1.1692 0.0966  -0.4114 0.0043  52  CYS   K C   
18271 O  O   . CYS   K  51  ? 1.5655 0.6098 1.2616 0.1365  -0.4164 0.0409  52  CYS   K O   
18272 C  CB  . CYS   K  51  ? 1.5661 0.5855 1.1745 0.1106  -0.3823 -0.0327 52  CYS   K CB  
18273 S  SG  . CYS   K  51  ? 1.6121 0.6408 1.2308 0.1479  -0.3323 -0.0463 52  CYS   K SG  
18274 N  N   . GLN   K  52  ? 1.5726 0.5269 1.1233 0.0595  -0.4314 0.0387  53  GLN   K N   
18275 C  CA  . GLN   K  52  ? 1.5474 0.5707 1.1596 0.0409  -0.4161 0.0378  53  GLN   K CA  
18276 C  C   . GLN   K  52  ? 1.5624 0.5319 1.1557 0.0605  -0.4207 0.0709  53  GLN   K C   
18277 O  O   . GLN   K  52  ? 1.6805 0.4940 1.2580 0.1318  -0.3605 0.0416  53  GLN   K O   
18278 C  CB  . GLN   K  52  ? 1.5591 0.6323 1.1468 -0.0252 -0.4299 0.0025  53  GLN   K CB  
18279 C  CG  . GLN   K  52  ? 1.5368 0.7261 1.1719 -0.0602 -0.4082 -0.0633 53  GLN   K CG  
18280 C  CD  . GLN   K  52  ? 1.5902 0.7353 1.1487 -0.0918 -0.3947 -0.0862 53  GLN   K CD  
18281 O  OE1 . GLN   K  52  ? 1.6616 0.8601 1.1274 -0.1482 -0.3766 -0.1366 53  GLN   K OE1 
18282 N  NE2 . GLN   K  52  ? 1.5955 0.6766 1.1537 -0.0884 -0.4028 -0.0307 53  GLN   K NE2 
18283 N  N   . PHE   K  53  ? 1.5186 0.4178 1.1512 0.0495  -0.4084 0.0983  54  PHE   K N   
18284 C  CA  . PHE   K  53  ? 1.4931 0.3893 1.1712 0.0458  -0.3977 0.1053  54  PHE   K CA  
18285 C  C   . PHE   K  53  ? 1.4540 0.3986 1.2012 0.0289  -0.3847 0.0748  54  PHE   K C   
18286 O  O   . PHE   K  53  ? 1.3971 0.4265 1.2861 0.0403  -0.3753 0.1620  54  PHE   K O   
18287 C  CB  . PHE   K  53  ? 1.5300 0.3305 1.1313 0.0064  -0.3786 0.1163  54  PHE   K CB  
18288 C  CG  . PHE   K  53  ? 1.5361 0.3622 1.0980 -0.0396 -0.3769 0.1262  54  PHE   K CG  
18289 C  CD1 . PHE   K  53  ? 1.5422 0.3795 1.0759 -0.0683 -0.3813 0.1170  54  PHE   K CD1 
18290 C  CD2 . PHE   K  53  ? 1.5409 0.3690 1.0766 -0.0562 -0.3836 0.1063  54  PHE   K CD2 
18291 C  CE1 . PHE   K  53  ? 1.5285 0.3895 1.0488 -0.0807 -0.3789 0.1229  54  PHE   K CE1 
18292 C  CE2 . PHE   K  53  ? 1.5308 0.3899 1.0603 -0.0678 -0.3853 0.1006  54  PHE   K CE2 
18293 C  CZ  . PHE   K  53  ? 1.5250 0.3889 1.0491 -0.0822 -0.3840 0.1153  54  PHE   K CZ  
18294 N  N   . TRP   K  54  ? 1.4639 0.3496 1.2096 0.0027  -0.3846 0.0144  55  TRP   K N   
18295 C  CA  . TRP   K  54  ? 1.5021 0.3125 1.2287 -0.0243 -0.3834 -0.0076 55  TRP   K CA  
18296 C  C   . TRP   K  54  ? 1.5398 0.2822 1.2367 -0.0085 -0.3792 0.0007  55  TRP   K C   
18297 O  O   . TRP   K  54  ? 1.5749 0.3340 1.2549 -0.0546 -0.3462 0.0126  55  TRP   K O   
18298 C  CB  . TRP   K  54  ? 1.4874 0.3377 1.1967 -0.0412 -0.3844 -0.0397 55  TRP   K CB  
18299 C  CG  . TRP   K  54  ? 1.4917 0.3797 1.1910 -0.0650 -0.3805 -0.0489 55  TRP   K CG  
18300 C  CD1 . TRP   K  54  ? 1.4795 0.4083 1.1626 -0.0881 -0.3920 -0.0341 55  TRP   K CD1 
18301 C  CD2 . TRP   K  54  ? 1.4776 0.4304 1.1479 -0.0805 -0.3730 -0.0601 55  TRP   K CD2 
18302 N  NE1 . TRP   K  54  ? 1.4767 0.4413 1.1479 -0.1120 -0.3613 -0.0607 55  TRP   K NE1 
18303 C  CE2 . TRP   K  54  ? 1.4643 0.4386 1.1235 -0.0927 -0.3679 -0.0718 55  TRP   K CE2 
18304 C  CE3 . TRP   K  54  ? 1.4593 0.4186 1.1283 -0.1136 -0.3565 -0.1098 55  TRP   K CE3 
18305 C  CZ2 . TRP   K  54  ? 1.4454 0.4241 1.1078 -0.1057 -0.3338 -0.0710 55  TRP   K CZ2 
18306 C  CZ3 . TRP   K  54  ? 1.4413 0.4127 1.1284 -0.1220 -0.3312 -0.1180 55  TRP   K CZ3 
18307 C  CH2 . TRP   K  54  ? 1.4253 0.4100 1.1193 -0.1254 -0.3199 -0.1158 55  TRP   K CH2 
18308 N  N   . GLU   K  55  ? 1.5382 0.3023 1.2502 -0.0114 -0.4064 0.0233  56  GLU   K N   
18309 C  CA  . GLU   K  55  ? 1.5778 0.3309 1.2865 0.0423  -0.3961 0.0891  56  GLU   K CA  
18310 C  C   . GLU   K  55  ? 1.5909 0.2614 1.3185 0.0130  -0.3704 0.0731  56  GLU   K C   
18311 O  O   . GLU   K  55  ? 1.6571 0.2955 1.3554 0.0142  -0.3885 0.1054  56  GLU   K O   
18312 C  CB  . GLU   K  55  ? 1.5776 0.3659 1.2613 0.0948  -0.4226 0.0606  56  GLU   K CB  
18313 C  CG  . GLU   K  55  ? 1.5766 0.4084 1.2574 0.1480  -0.4475 0.1012  56  GLU   K CG  
18314 C  CD  . GLU   K  55  ? 1.5686 0.4319 1.2691 0.1860  -0.4875 0.0941  56  GLU   K CD  
18315 O  OE1 . GLU   K  55  ? 1.5732 0.4316 1.3681 0.2062  -0.5112 0.1163  56  GLU   K OE1 
18316 O  OE2 . GLU   K  55  ? 1.5293 0.5420 1.2972 0.2269  -0.4946 0.0863  56  GLU   K OE2 
18317 N  N   . THR   K  56  ? 1.6115 0.2661 1.3086 -0.0099 -0.3601 0.0787  57  THR   K N   
18318 C  CA  . THR   K  56  ? 1.6378 0.3227 1.3498 0.0285  -0.3384 0.0815  57  THR   K CA  
18319 C  C   . THR   K  56  ? 1.5760 0.4232 1.3363 0.0055  -0.3261 0.0170  57  THR   K C   
18320 O  O   . THR   K  56  ? 1.5772 0.3816 1.4356 0.0240  -0.2888 -0.0691 57  THR   K O   
18321 C  CB  . THR   K  56  ? 1.6624 0.3253 1.3609 0.0409  -0.3222 0.0881  57  THR   K CB  
18322 O  OG1 . THR   K  56  ? 1.6926 0.3697 1.3660 0.0192  -0.3279 0.1058  57  THR   K OG1 
18323 C  CG2 . THR   K  56  ? 1.6737 0.3962 1.3624 0.0077  -0.3466 0.0298  57  THR   K CG2 
18324 N  N   . TRP   K  57  ? 1.5747 0.4396 1.2800 0.0137  -0.3049 0.0510  58  TRP   K N   
18325 C  CA  . TRP   K  57  ? 1.6000 0.3995 1.3066 0.0066  -0.2736 0.0587  58  TRP   K CA  
18326 C  C   . TRP   K  57  ? 1.5727 0.4366 1.3016 -0.0139 -0.2922 0.0583  58  TRP   K C   
18327 O  O   . TRP   K  57  ? 1.5778 0.4470 1.4303 -0.0797 -0.2758 0.0954  58  TRP   K O   
18328 C  CB  . TRP   K  57  ? 1.5821 0.3716 1.2229 -0.0285 -0.2409 0.0444  58  TRP   K CB  
18329 C  CG  . TRP   K  57  ? 1.6205 0.3003 1.1793 -0.0357 -0.2055 0.0930  58  TRP   K CG  
18330 C  CD1 . TRP   K  57  ? 1.6424 0.2782 1.1687 -0.0306 -0.1846 0.1089  58  TRP   K CD1 
18331 C  CD2 . TRP   K  57  ? 1.6446 0.2424 1.1425 -0.0292 -0.1944 0.1305  58  TRP   K CD2 
18332 N  NE1 . TRP   K  57  ? 1.6479 0.2601 1.1299 -0.0199 -0.1844 0.1088  58  TRP   K NE1 
18333 C  CE2 . TRP   K  57  ? 1.6273 0.2584 1.1024 -0.0206 -0.1884 0.1370  58  TRP   K CE2 
18334 C  CE3 . TRP   K  57  ? 1.6478 0.2251 1.1524 -0.0389 -0.1944 0.1277  58  TRP   K CE3 
18335 C  CZ2 . TRP   K  57  ? 1.6150 0.2455 1.0844 -0.0275 -0.2158 0.1338  58  TRP   K CZ2 
18336 C  CZ3 . TRP   K  57  ? 1.6405 0.2301 1.1243 -0.0135 -0.1992 0.1554  58  TRP   K CZ3 
18337 C  CH2 . TRP   K  57  ? 1.6163 0.2401 1.0817 -0.0022 -0.2128 0.1558  58  TRP   K CH2 
18338 N  N   . LEU   K  58  ? 1.5599 0.3976 1.2798 0.0240  -0.3379 0.0817  59  LEU   K N   
18339 C  CA  . LEU   K  58  ? 1.5741 0.3681 1.2933 0.0238  -0.3377 0.0988  59  LEU   K CA  
18340 C  C   . LEU   K  58  ? 1.6141 0.3654 1.2990 0.0301  -0.3825 0.0676  59  LEU   K C   
18341 O  O   . LEU   K  58  ? 1.6153 0.3036 1.2559 0.0247  -0.4224 0.0089  59  LEU   K O   
18342 C  CB  . LEU   K  58  ? 1.5507 0.3865 1.3013 0.0773  -0.3251 0.1140  59  LEU   K CB  
18343 C  CG  . LEU   K  58  ? 1.5698 0.3625 1.3205 0.0783  -0.3345 0.1685  59  LEU   K CG  
18344 C  CD1 . LEU   K  58  ? 1.5769 0.3678 1.3266 0.0707  -0.3300 0.1963  59  LEU   K CD1 
18345 C  CD2 . LEU   K  58  ? 1.5915 0.4133 1.3206 0.0910  -0.3478 0.1283  59  LEU   K CD2 
18346 N  N   . GLY   K  59  ? 1.6214 0.4068 1.3337 0.0231  -0.3875 0.0700  60  GLY   K N   
18347 C  CA  . GLY   K  59  ? 1.6277 0.4904 1.4025 0.0565  -0.4070 0.0544  60  GLY   K CA  
18348 C  C   . GLY   K  59  ? 1.6613 0.5346 1.4151 0.0221  -0.3802 -0.0115 60  GLY   K C   
18349 O  O   . GLY   K  59  ? 1.7112 0.5494 1.4397 0.0440  -0.4175 -0.0122 60  GLY   K O   
18350 N  N   . SER   K  60  ? 1.6283 0.5730 1.3914 0.0202  -0.3336 0.0133  61  SER   K N   
18351 C  CA  . SER   K  60  ? 1.6214 0.5501 1.4729 0.0066  -0.3187 0.0116  61  SER   K CA  
18352 C  C   . SER   K  60  ? 1.6262 0.5175 1.3980 0.0223  -0.3276 0.0148  61  SER   K C   
18353 O  O   . SER   K  60  ? 1.6650 0.5347 1.4080 0.0443  -0.3504 0.0557  61  SER   K O   
18354 C  CB  . SER   K  60  ? 1.6095 0.5295 1.4677 -0.0180 -0.3088 -0.0317 61  SER   K CB  
18355 O  OG  . SER   K  60  ? 1.5935 0.6599 1.5982 -0.0237 -0.2682 -0.0198 61  SER   K OG  
18356 N  N   . GLN   K  61  ? 1.6142 0.5707 1.3276 0.0306  -0.3315 0.0618  62  GLN   K N   
18357 C  CA  . GLN   K  61  ? 1.6531 0.6016 1.3231 0.0101  -0.3168 0.0981  62  GLN   K CA  
18358 C  C   . GLN   K  61  ? 1.6803 0.5474 1.3665 0.0532  -0.3360 0.1335  62  GLN   K C   
18359 O  O   . GLN   K  61  ? 1.7041 0.4346 1.4638 0.1280  -0.3092 0.0475  62  GLN   K O   
18360 C  CB  . GLN   K  61  ? 1.6286 0.6258 1.2359 -0.0132 -0.2969 0.1773  62  GLN   K CB  
18361 C  CG  . GLN   K  61  ? 1.6529 0.6883 1.2348 -0.0349 -0.2567 0.2215  62  GLN   K CG  
18362 C  CD  . GLN   K  61  ? 1.6503 0.7303 1.2169 -0.0722 -0.2205 0.2189  62  GLN   K CD  
18363 O  OE1 . GLN   K  61  ? 1.6629 0.8283 1.1658 -0.1013 -0.1807 0.2972  62  GLN   K OE1 
18364 N  NE2 . GLN   K  61  ? 1.6536 0.8346 1.2619 -0.0432 -0.1906 0.2485  62  GLN   K NE2 
18365 N  N   . CYS   K  62  ? 1.7116 0.6798 1.3669 0.0429  -0.4153 0.1306  63  CYS   K N   
18366 C  CA  . CYS   K  62  ? 1.7455 0.7084 1.4044 0.0599  -0.4802 0.1649  63  CYS   K CA  
18367 C  C   . CYS   K  62  ? 1.6739 0.7715 1.4198 0.0670  -0.4966 0.1316  63  CYS   K C   
18368 O  O   . CYS   K  62  ? 1.7120 0.8635 1.4954 -0.0742 -0.4518 0.1687  63  CYS   K O   
18369 C  CB  . CYS   K  62  ? 1.8066 0.6994 1.3853 0.0704  -0.5044 0.1745  63  CYS   K CB  
18370 S  SG  . CYS   K  62  ? 1.9004 0.6685 1.3554 0.1003  -0.4854 0.2528  63  CYS   K SG  
18371 N  N   . ARG   K  63  ? 1.6356 0.7360 1.3878 0.0785  -0.5206 0.1506  64  ARG   K N   
18372 C  CA  . ARG   K  63  ? 1.6169 0.7185 1.4668 0.0650  -0.5054 0.1567  64  ARG   K CA  
18373 C  C   . ARG   K  63  ? 1.6288 0.5839 1.4762 0.1421  -0.4908 0.1966  64  ARG   K C   
18374 O  O   . ARG   K  63  ? 1.6455 0.5205 1.6360 0.1579  -0.4997 0.1684  64  ARG   K O   
18375 C  CB  . ARG   K  63  ? 1.5944 0.7790 1.5044 0.0755  -0.4875 0.1484  64  ARG   K CB  
18376 C  CG  . ARG   K  63  ? 1.6125 0.7784 1.6364 0.0778  -0.4335 0.1342  64  ARG   K CG  
18377 C  CD  . ARG   K  63  ? 1.6453 0.8441 1.6865 0.0759  -0.4678 0.1512  64  ARG   K CD  
18378 N  NE  . ARG   K  63  ? 1.6706 0.8829 1.8281 0.0832  -0.4166 0.1088  64  ARG   K NE  
18379 C  CZ  . ARG   K  63  ? 1.6973 0.9146 1.8507 0.0812  -0.4278 0.1332  64  ARG   K CZ  
18380 N  NH1 . ARG   K  63  ? 1.7118 0.9886 1.8295 0.0573  -0.4443 0.1566  64  ARG   K NH1 
18381 N  NH2 . ARG   K  63  ? 1.7182 0.9362 1.9392 0.0859  -0.3989 0.0824  64  ARG   K NH2 
18382 N  N   . LEU   K  64  ? 1.5936 0.5387 1.4197 0.1008  -0.4516 0.1318  65  LEU   K N   
18383 C  CA  . LEU   K  64  ? 1.6095 0.4810 1.4689 0.1244  -0.4151 0.1122  65  LEU   K CA  
18384 C  C   . LEU   K  64  ? 1.6505 0.5384 1.4492 0.1177  -0.4153 0.1164  65  LEU   K C   
18385 O  O   . LEU   K  64  ? 1.7041 0.5693 1.5240 0.0542  -0.4276 0.0813  65  LEU   K O   
18386 C  CB  . LEU   K  64  ? 1.5361 0.4888 1.4342 0.1100  -0.3909 0.0671  65  LEU   K CB  
18387 C  CG  . LEU   K  64  ? 1.5104 0.5057 1.4458 0.0995  -0.3882 0.0238  65  LEU   K CG  
18388 C  CD1 . LEU   K  64  ? 1.4938 0.5471 1.3659 0.0754  -0.3690 -0.0060 65  LEU   K CD1 
18389 C  CD2 . LEU   K  64  ? 1.5083 0.4923 1.5073 0.0884  -0.3930 0.0272  65  LEU   K CD2 
18390 N  N   . HIS   K  65  ? 1.6906 0.5311 1.4310 0.0914  -0.4095 0.1119  66  HIS   K N   
18391 C  CA  . HIS   K  65  ? 1.7177 0.5798 1.4620 0.0286  -0.3897 0.1031  66  HIS   K CA  
18392 C  C   . HIS   K  65  ? 1.7326 0.6389 1.4654 0.0416  -0.4084 0.1052  66  HIS   K C   
18393 O  O   . HIS   K  65  ? 1.7897 0.6532 1.4517 0.0010  -0.4162 0.0874  66  HIS   K O   
18394 C  CB  . HIS   K  65  ? 1.7034 0.5875 1.4620 0.0076  -0.3853 0.0896  66  HIS   K CB  
18395 C  CG  . HIS   K  65  ? 1.6616 0.5705 1.5673 -0.0739 -0.3425 0.1030  66  HIS   K CG  
18396 N  ND1 . HIS   K  65  ? 1.6671 0.4830 1.5725 -0.1245 -0.3566 0.0685  66  HIS   K ND1 
18397 C  CD2 . HIS   K  65  ? 1.7069 0.6156 1.6085 -0.0817 -0.3725 0.1393  66  HIS   K CD2 
18398 C  CE1 . HIS   K  65  ? 1.6558 0.5631 1.5950 -0.1483 -0.3296 0.0786  66  HIS   K CE1 
18399 N  NE2 . HIS   K  65  ? 1.7000 0.6078 1.6376 -0.1180 -0.3714 0.1310  66  HIS   K NE2 
18400 N  N   . GLU   K  66  ? 1.7092 0.7181 1.4850 0.0559  -0.4130 0.1185  67  GLU   K N   
18401 C  CA  . GLU   K  66  ? 1.7426 0.7375 1.5720 0.0571  -0.4500 0.1564  67  GLU   K CA  
18402 C  C   . GLU   K  66  ? 1.7162 0.7229 1.6366 0.0561  -0.4728 0.1421  67  GLU   K C   
18403 O  O   . GLU   K  66  ? 1.7644 0.7157 1.7631 0.0909  -0.4930 0.1648  67  GLU   K O   
18404 C  CB  . GLU   K  66  ? 1.7944 0.8213 1.6278 -0.0004 -0.4730 0.1579  67  GLU   K CB  
18405 C  CG  . GLU   K  66  ? 1.8109 0.8237 1.6505 -0.0241 -0.4663 0.1480  67  GLU   K CG  
18406 C  CD  . GLU   K  66  ? 1.8986 0.7976 1.6640 -0.0456 -0.5028 0.1624  67  GLU   K CD  
18407 O  OE1 . GLU   K  66  ? 1.8988 0.7342 1.5088 -0.0280 -0.5412 0.2814  67  GLU   K OE1 
18408 O  OE2 . GLU   K  66  ? 1.8919 0.8214 1.7701 -0.0563 -0.5203 0.0777  67  GLU   K OE2 
18409 N  N   . LEU   K  67  ? 1.6304 0.5551 1.6242 0.0961  -0.5085 0.1562  68  LEU   K N   
18410 C  CA  . LEU   K  67  ? 1.6217 0.5540 1.6572 0.1013  -0.5202 0.1417  68  LEU   K CA  
18411 C  C   . LEU   K  67  ? 1.6539 0.5333 1.6395 0.0937  -0.4980 0.1510  68  LEU   K C   
18412 O  O   . LEU   K  67  ? 1.6636 0.5417 1.7018 0.0988  -0.5231 0.1661  68  LEU   K O   
18413 C  CB  . LEU   K  67  ? 1.5623 0.5003 1.6497 0.1044  -0.4981 0.0720  68  LEU   K CB  
18414 C  CG  . LEU   K  67  ? 1.5480 0.4991 1.7033 0.1186  -0.5022 0.0446  68  LEU   K CG  
18415 C  CD1 . LEU   K  67  ? 1.5073 0.5174 1.6688 0.1102  -0.4689 -0.0126 68  LEU   K CD1 
18416 C  CD2 . LEU   K  67  ? 1.5630 0.5164 1.7911 0.1332  -0.5158 0.0505  68  LEU   K CD2 
18417 N  N   . ARG   K  68  ? 1.6593 0.5255 1.6015 0.1180  -0.4451 0.1577  69  ARG   K N   
18418 C  CA  . ARG   K  68  ? 1.7041 0.5182 1.6311 0.0867  -0.3918 0.1690  69  ARG   K CA  
18419 C  C   . ARG   K  68  ? 1.7572 0.5199 1.6428 0.0632  -0.4026 0.2164  69  ARG   K C   
18420 O  O   . ARG   K  68  ? 1.7477 0.5889 1.6672 -0.0018 -0.3896 0.2665  69  ARG   K O   
18421 C  CB  . ARG   K  68  ? 1.6932 0.5229 1.6005 0.1197  -0.3585 0.1498  69  ARG   K CB  
18422 C  CG  . ARG   K  68  ? 1.6941 0.5569 1.6195 0.1434  -0.3140 0.1295  69  ARG   K CG  
18423 C  CD  . ARG   K  68  ? 1.6755 0.6418 1.5923 0.1521  -0.2947 0.1201  69  ARG   K CD  
18424 N  NE  . ARG   K  68  ? 1.7086 0.6561 1.5608 0.1804  -0.2910 0.1480  69  ARG   K NE  
18425 C  CZ  . ARG   K  68  ? 1.7223 0.7132 1.5106 0.2266  -0.2871 0.1356  69  ARG   K CZ  
18426 N  NH1 . ARG   K  68  ? 1.7126 0.7709 1.5216 0.2339  -0.2801 0.1163  69  ARG   K NH1 
18427 N  NH2 . ARG   K  68  ? 1.7570 0.7136 1.4916 0.2285  -0.2863 0.1214  69  ARG   K NH2 
18428 N  N   . GLU   K  69  ? 1.7858 0.4950 1.6260 0.0349  -0.3952 0.2375  70  GLU   K N   
18429 C  CA  . GLU   K  69  ? 1.8581 0.5107 1.6276 -0.0187 -0.3868 0.2577  70  GLU   K CA  
18430 C  C   . GLU   K  69  ? 1.8958 0.4351 1.6619 0.0268  -0.3996 0.2825  70  GLU   K C   
18431 O  O   . GLU   K  69  ? 1.9139 0.3431 1.6633 0.0315  -0.4042 0.2983  70  GLU   K O   
18432 C  CB  . GLU   K  69  ? 1.8411 0.5550 1.5554 -0.0357 -0.3595 0.2230  70  GLU   K CB  
18433 C  CG  . GLU   K  69  ? 1.8275 0.6196 1.5252 -0.0935 -0.3511 0.2278  70  GLU   K CG  
18434 C  CD  . GLU   K  69  ? 1.8742 0.6387 1.6125 -0.1469 -0.3116 0.2346  70  GLU   K CD  
18435 O  OE1 . GLU   K  69  ? 1.9571 0.5407 1.6932 -0.0855 -0.3692 0.2869  70  GLU   K OE1 
18436 O  OE2 . GLU   K  69  ? 1.9021 0.7588 1.6146 -0.2125 -0.2906 0.1505  70  GLU   K OE2 
18437 N  N   . LYS   K  70  ? 1.8901 0.4632 1.7220 0.0571  -0.4123 0.2923  71  LYS   K N   
18438 C  CA  . LYS   K  70  ? 1.9574 0.6021 1.7756 0.0672  -0.4715 0.3213  71  LYS   K CA  
18439 C  C   . LYS   K  70  ? 1.9936 0.6293 1.7417 0.0661  -0.5133 0.3290  71  LYS   K C   
18440 O  O   . LYS   K  70  ? 2.0503 0.6360 1.7514 0.0716  -0.5488 0.3348  71  LYS   K O   
18441 C  CB  . LYS   K  70  ? 2.0149 0.6197 1.8743 0.0488  -0.4716 0.3604  71  LYS   K CB  
18442 C  CG  . LYS   K  70  ? 2.0245 0.6545 1.9520 0.0531  -0.4400 0.3178  71  LYS   K CG  
18443 C  CD  . LYS   K  70  ? 2.1156 0.6548 2.0709 0.0315  -0.4409 0.3221  71  LYS   K CD  
18444 C  CE  . LYS   K  70  ? 2.1432 0.7175 2.1522 0.0182  -0.3986 0.2747  71  LYS   K CE  
18445 N  NZ  . LYS   K  70  ? 2.2167 0.7217 2.2343 -0.0213 -0.4311 0.3052  71  LYS   K NZ  
18446 N  N   . GLU   K  71  ? 2.0037 0.6406 1.6900 0.0678  -0.5143 0.3497  72  GLU   K N   
18447 C  CA  . GLU   K  71  ? 2.0897 0.7658 1.6739 0.0529  -0.5150 0.2992  72  GLU   K CA  
18448 C  C   . GLU   K  71  ? 2.1087 0.7376 1.6184 0.0545  -0.5016 0.2499  72  GLU   K C   
18449 O  O   . GLU   K  71  ? 2.1646 0.8044 1.5703 0.0473  -0.4906 0.1882  72  GLU   K O   
18450 C  CB  . GLU   K  71  ? 2.1191 0.8149 1.7277 0.0035  -0.4999 0.3159  72  GLU   K CB  
18451 C  CG  . GLU   K  71  ? 2.2004 0.8655 1.7645 -0.0074 -0.4844 0.2754  72  GLU   K CG  
18452 C  CD  . GLU   K  71  ? 2.2535 0.9198 1.8098 -0.0495 -0.4418 0.2636  72  GLU   K CD  
18453 O  OE1 . GLU   K  71  ? 2.3547 0.9625 1.8684 -0.1265 -0.4468 0.2968  72  GLU   K OE1 
18454 O  OE2 . GLU   K  71  ? 2.2887 0.9938 1.8764 -0.0008 -0.3903 0.1655  72  GLU   K OE2 
18455 N  N   . ARG   K  72  ? 2.1029 0.7227 1.6380 0.0679  -0.5270 0.2563  73  ARG   K N   
18456 C  CA  . ARG   K  72  ? 2.0124 0.6985 1.6331 0.1275  -0.4981 0.2319  73  ARG   K CA  
18457 C  C   . ARG   K  72  ? 2.0011 0.5317 1.4845 0.1077  -0.4913 0.1859  73  ARG   K C   
18458 O  O   . ARG   K  72  ? 1.9843 0.3999 1.5035 0.1700  -0.4641 0.1620  73  ARG   K O   
18459 C  CB  . ARG   K  72  ? 2.0902 0.7511 1.6420 0.0891  -0.5463 0.2702  73  ARG   K CB  
18460 C  CG  . ARG   K  72  ? 2.1067 0.8267 1.7283 0.1132  -0.5119 0.2965  73  ARG   K CG  
18461 C  CD  . ARG   K  72  ? 2.1715 0.9545 1.7289 0.0939  -0.5746 0.3491  73  ARG   K CD  
18462 N  NE  . ARG   K  72  ? 2.2507 1.0587 1.7250 0.1586  -0.5191 0.3691  73  ARG   K NE  
18463 C  CZ  . ARG   K  72  ? 2.3693 1.2646 1.7525 0.1246  -0.4537 0.3721  73  ARG   K CZ  
18464 N  NH1 . ARG   K  72  ? 2.4682 1.2513 1.9120 0.0983  -0.4553 0.3980  73  ARG   K NH1 
18465 N  NH2 . ARG   K  72  ? 2.3760 1.2609 1.7104 0.1454  -0.4616 0.3984  73  ARG   K NH2 
18466 N  N   . ILE   K  73  ? 1.8179 0.4829 1.4246 0.1289  -0.4957 0.1159  74  ILE   K N   
18467 C  CA  . ILE   K  73  ? 1.7841 0.4838 1.3724 0.1086  -0.4623 0.1232  74  ILE   K CA  
18468 C  C   . ILE   K  73  ? 1.7661 0.4979 1.2805 0.1015  -0.4743 0.1652  74  ILE   K C   
18469 O  O   . ILE   K  73  ? 1.7526 0.4546 1.2779 0.1101  -0.5035 0.2272  74  ILE   K O   
18470 C  CB  . ILE   K  73  ? 1.7295 0.4382 1.3533 0.1005  -0.4253 0.0882  74  ILE   K CB  
18471 C  CG1 . ILE   K  73  ? 1.7078 0.4840 1.3187 0.0694  -0.4141 0.0515  74  ILE   K CG1 
18472 C  CG2 . ILE   K  73  ? 1.6944 0.4597 1.3816 0.1019  -0.4256 0.0970  74  ILE   K CG2 
18473 C  CD1 . ILE   K  73  ? 1.6876 0.4717 1.2985 0.0472  -0.3989 0.0065  74  ILE   K CD1 
18474 N  N   . SER   K  74  ? 1.7927 0.4978 1.2387 0.1011  -0.4424 0.1717  75  SER   K N   
18475 C  CA  . SER   K  74  ? 1.8106 0.4818 1.2544 0.0688  -0.4440 0.1450  75  SER   K CA  
18476 C  C   . SER   K  74  ? 1.7884 0.4861 1.2160 0.0458  -0.4012 0.1373  75  SER   K C   
18477 O  O   . SER   K  74  ? 1.7289 0.3802 1.1986 -0.0148 -0.3835 0.0274  75  SER   K O   
18478 C  CB  . SER   K  74  ? 1.8076 0.4030 1.2048 0.1019  -0.4381 0.1541  75  SER   K CB  
18479 O  OG  . SER   K  74  ? 1.7446 0.3191 1.1750 0.1632  -0.3953 0.1671  75  SER   K OG  
18480 N  N   . VAL   K  75  ? 1.8103 0.5835 1.2214 0.0406  -0.3733 0.0695  76  VAL   K N   
18481 C  CA  . VAL   K  75  ? 1.7684 0.5764 1.2216 0.0901  -0.3402 0.0566  76  VAL   K CA  
18482 C  C   . VAL   K  75  ? 1.7269 0.5388 1.1550 0.0713  -0.2955 0.0165  76  VAL   K C   
18483 O  O   . VAL   K  75  ? 1.6529 0.5315 1.1558 0.0772  -0.2398 0.0225  76  VAL   K O   
18484 C  CB  . VAL   K  75  ? 1.8096 0.6746 1.2386 0.0644  -0.3703 0.0266  76  VAL   K CB  
18485 C  CG1 . VAL   K  75  ? 1.8013 0.7028 1.2433 0.0612  -0.3580 0.0650  76  VAL   K CG1 
18486 C  CG2 . VAL   K  75  ? 1.8198 0.7394 1.3108 0.0733  -0.3873 0.0461  76  VAL   K CG2 
18487 N  N   . ALA   K  76  ? 1.7621 0.5574 1.1488 0.0228  -0.2968 -0.0104 77  ALA   K N   
18488 C  CA  . ALA   K  76  ? 1.7716 0.6124 1.1252 0.0027  -0.3036 -0.0165 77  ALA   K CA  
18489 C  C   . ALA   K  76  ? 1.7577 0.6248 1.0980 0.0230  -0.2936 0.0125  77  ALA   K C   
18490 O  O   . ALA   K  76  ? 1.7321 0.6600 1.0810 0.0075  -0.2809 0.0323  77  ALA   K O   
18491 C  CB  . ALA   K  76  ? 1.8210 0.6352 1.0937 -0.0220 -0.3004 -0.0246 77  ALA   K CB  
18492 N  N   . ALA   K  77  ? 1.7513 0.6344 1.1223 0.0359  -0.2955 0.0195  78  ALA   K N   
18493 C  CA  . ALA   K  77  ? 1.6733 0.6240 1.1117 0.0415  -0.2995 0.0299  78  ALA   K CA  
18494 C  C   . ALA   K  77  ? 1.6165 0.5729 1.1170 0.0397  -0.3163 0.0141  78  ALA   K C   
18495 O  O   . ALA   K  77  ? 1.6167 0.5907 1.0759 0.0297  -0.2705 -0.0062 78  ALA   K O   
18496 C  CB  . ALA   K  77  ? 1.6591 0.6412 1.1653 0.0679  -0.3127 0.0405  78  ALA   K CB  
18497 N  N   . ALA   K  78  ? 1.6160 0.5373 1.1167 0.0533  -0.3526 0.0568  79  ALA   K N   
18498 C  CA  . ALA   K  78  ? 1.5825 0.5623 1.1137 0.0411  -0.3703 0.0508  79  ALA   K CA  
18499 C  C   . ALA   K  78  ? 1.5777 0.5780 1.1066 0.0534  -0.3554 0.0509  79  ALA   K C   
18500 O  O   . ALA   K  78  ? 1.5489 0.4823 1.0762 0.0829  -0.3316 -0.0291 79  ALA   K O   
18501 C  CB  . ALA   K  78  ? 1.6047 0.5616 1.1198 0.0596  -0.4100 0.0794  79  ALA   K CB  
18502 N  N   . SER   K  79  ? 1.5716 0.5933 1.1216 0.0513  -0.3442 0.0493  80  SER   K N   
18503 C  CA  . SER   K  79  ? 1.5615 0.6293 1.1035 0.0342  -0.3668 0.1452  80  SER   K CA  
18504 C  C   . SER   K  79  ? 1.5558 0.6193 1.1170 -0.0077 -0.3568 0.1522  80  SER   K C   
18505 O  O   . SER   K  79  ? 1.5490 0.6868 1.1170 -0.0633 -0.3296 0.2007  80  SER   K O   
18506 C  CB  . SER   K  79  ? 1.5703 0.6698 1.1052 0.0386  -0.3663 0.1369  80  SER   K CB  
18507 O  OG  . SER   K  79  ? 1.5820 0.7231 1.1445 0.0146  -0.3400 0.1272  80  SER   K OG  
18508 N  N   . LYS   K  80  ? 1.6042 0.5670 1.0882 0.0274  -0.3787 0.2056  81  LYS   K N   
18509 C  CA  . LYS   K  80  ? 1.5954 0.5116 1.0536 0.0435  -0.3579 0.1899  81  LYS   K CA  
18510 C  C   . LYS   K  80  ? 1.5746 0.4568 1.0890 0.0722  -0.3643 0.1488  81  LYS   K C   
18511 O  O   . LYS   K  80  ? 1.5673 0.3391 1.1037 0.0952  -0.3672 0.1192  81  LYS   K O   
18512 C  CB  . LYS   K  80  ? 1.6122 0.5284 1.0726 0.0398  -0.3480 0.2080  81  LYS   K CB  
18513 C  CG  . LYS   K  80  ? 1.6100 0.5155 1.0672 0.0667  -0.3436 0.2087  81  LYS   K CG  
18514 C  CD  . LYS   K  80  ? 1.6061 0.5792 1.1027 0.0520  -0.3157 0.1822  81  LYS   K CD  
18515 C  CE  . LYS   K  80  ? 1.6255 0.5712 1.1397 0.0804  -0.3340 0.1636  81  LYS   K CE  
18516 N  NZ  . LYS   K  80  ? 1.6345 0.6608 1.1618 0.0442  -0.2951 0.1097  81  LYS   K NZ  
18517 N  N   . ILE   K  81  ? 1.5595 0.5183 1.0689 0.0790  -0.3681 0.1359  82  ILE   K N   
18518 C  CA  . ILE   K  81  ? 1.5433 0.5722 1.0669 0.0621  -0.3717 0.1200  82  ILE   K CA  
18519 C  C   . ILE   K  81  ? 1.5421 0.5696 1.0508 0.0765  -0.3587 0.1151  82  ILE   K C   
18520 O  O   . ILE   K  81  ? 1.5355 0.6647 1.0359 0.0934  -0.3402 0.1458  82  ILE   K O   
18521 C  CB  . ILE   K  81  ? 1.5481 0.5941 1.0580 0.0672  -0.4028 0.0902  82  ILE   K CB  
18522 C  CG1 . ILE   K  81  ? 1.5758 0.5610 1.0744 0.0478  -0.4147 0.0312  82  ILE   K CG1 
18523 C  CG2 . ILE   K  81  ? 1.5628 0.6355 1.0510 0.0613  -0.4004 0.0713  82  ILE   K CG2 
18524 C  CD1 . ILE   K  81  ? 1.6011 0.5560 1.1508 0.0652  -0.4149 0.0141  82  ILE   K CD1 
18525 N  N   . LEU   K  82  ? 1.5925 0.5334 1.0435 0.0851  -0.3545 0.1088  83  LEU   K N   
18526 C  CA  . LEU   K  82  ? 1.5967 0.5036 1.0125 0.1033  -0.3611 0.0873  83  LEU   K CA  
18527 C  C   . LEU   K  82  ? 1.5840 0.4065 0.9325 0.0700  -0.3405 0.1041  83  LEU   K C   
18528 O  O   . LEU   K  82  ? 1.5807 0.4116 0.9137 0.0909  -0.3179 0.0915  83  LEU   K O   
18529 C  CB  . LEU   K  82  ? 1.6295 0.4618 1.0204 0.0995  -0.3800 0.1164  83  LEU   K CB  
18530 C  CG  . LEU   K  82  ? 1.6727 0.4822 1.0458 0.1028  -0.3501 0.1410  83  LEU   K CG  
18531 C  CD1 . LEU   K  82  ? 1.6600 0.4867 1.0595 0.1104  -0.3492 0.1050  83  LEU   K CD1 
18532 C  CD2 . LEU   K  82  ? 1.7026 0.4858 1.0629 0.0976  -0.3775 0.1578  83  LEU   K CD2 
18533 N  N   . SER   K  83  ? 1.5644 0.4143 0.9550 0.0224  -0.3301 0.0945  84  SER   K N   
18534 C  CA  . SER   K  83  ? 1.5238 0.4629 0.9515 -0.0026 -0.2999 0.0948  84  SER   K CA  
18535 C  C   . SER   K  83  ? 1.5069 0.5008 0.9589 -0.0285 -0.2947 0.1113  84  SER   K C   
18536 O  O   . SER   K  83  ? 1.4959 0.4822 0.9673 -0.0577 -0.2759 0.1470  84  SER   K O   
18537 C  CB  . SER   K  83  ? 1.5349 0.4790 0.9559 -0.0230 -0.2911 0.0776  84  SER   K CB  
18538 O  OG  . SER   K  83  ? 1.5563 0.4449 0.9439 -0.0157 -0.2843 0.0369  84  SER   K OG  
18539 N  N   . ASN   K  84  ? 1.5022 0.5063 1.0083 -0.0034 -0.2922 0.0800  85  ASN   K N   
18540 C  CA  . ASN   K  84  ? 1.4862 0.5382 1.0098 0.0147  -0.2925 0.0540  85  ASN   K CA  
18541 C  C   . ASN   K  84  ? 1.4475 0.5189 1.0085 0.0217  -0.3063 0.0615  85  ASN   K C   
18542 O  O   . ASN   K  84  ? 1.4556 0.5324 1.0030 0.0642  -0.3037 0.0953  85  ASN   K O   
18543 C  CB  . ASN   K  84  ? 1.5112 0.5245 1.0421 0.0047  -0.3022 0.0309  85  ASN   K CB  
18544 C  CG  . ASN   K  84  ? 1.5269 0.5298 1.0818 0.0001  -0.2837 0.0375  85  ASN   K CG  
18545 O  OD1 . ASN   K  84  ? 1.5390 0.5274 1.1521 -0.0209 -0.3236 0.0469  85  ASN   K OD1 
18546 N  ND2 . ASN   K  84  ? 1.5399 0.5826 1.1355 0.0237  -0.2702 0.0171  85  ASN   K ND2 
18547 N  N   . LEU   K  85  ? 1.4379 0.5000 1.0308 0.0112  -0.3382 0.0779  86  LEU   K N   
18548 C  CA  . LEU   K  85  ? 1.4305 0.5565 1.0304 -0.0294 -0.3420 0.0722  86  LEU   K CA  
18549 C  C   . LEU   K  85  ? 1.4161 0.6091 0.9989 -0.0162 -0.3691 0.0979  86  LEU   K C   
18550 O  O   . LEU   K  85  ? 1.4368 0.7323 0.9444 -0.0806 -0.3178 0.0420  86  LEU   K O   
18551 C  CB  . LEU   K  85  ? 1.4381 0.5121 1.0382 -0.0245 -0.3408 0.0936  86  LEU   K CB  
18552 C  CG  . LEU   K  85  ? 1.4707 0.5453 1.0001 -0.0156 -0.3528 0.0784  86  LEU   K CG  
18553 C  CD1 . LEU   K  85  ? 1.4754 0.5629 0.9686 -0.0076 -0.3668 0.1088  86  LEU   K CD1 
18554 C  CD2 . LEU   K  85  ? 1.4530 0.5360 0.9612 -0.0121 -0.3417 0.1019  86  LEU   K CD2 
18555 N  N   . VAL   K  86  ? 1.4540 0.6113 1.0606 -0.0070 -0.3741 0.0804  87  VAL   K N   
18556 C  CA  . VAL   K  86  ? 1.4611 0.6325 1.0635 -0.0212 -0.3760 0.1373  87  VAL   K CA  
18557 C  C   . VAL   K  86  ? 1.4668 0.6055 1.0685 0.0000  -0.3843 0.1223  87  VAL   K C   
18558 O  O   . VAL   K  86  ? 1.4791 0.7381 0.9512 -0.0011 -0.4040 0.1127  87  VAL   K O   
18559 C  CB  . VAL   K  86  ? 1.4997 0.5952 1.0754 -0.0347 -0.3747 0.1559  87  VAL   K CB  
18560 C  CG1 . VAL   K  86  ? 1.4963 0.6033 1.0992 -0.0439 -0.3556 0.1610  87  VAL   K CG1 
18561 C  CG2 . VAL   K  86  ? 1.5326 0.5849 1.0864 -0.0459 -0.3572 0.1589  87  VAL   K CG2 
18562 N  N   . TYR   K  87  ? 1.4269 0.5504 1.0843 0.0307  -0.3797 0.1039  88  TYR   K N   
18563 C  CA  . TYR   K  87  ? 1.4241 0.4977 1.1193 0.0135  -0.3760 0.0666  88  TYR   K CA  
18564 C  C   . TYR   K  87  ? 1.4048 0.4681 1.1476 -0.0035 -0.3963 0.0629  88  TYR   K C   
18565 O  O   . TYR   K  87  ? 1.4091 0.4282 1.1858 -0.0095 -0.4161 0.0504  88  TYR   K O   
18566 C  CB  . TYR   K  87  ? 1.4218 0.4599 1.1336 0.0021  -0.3515 0.0313  88  TYR   K CB  
18567 C  CG  . TYR   K  87  ? 1.4193 0.4631 1.1475 0.0023  -0.3462 0.0241  88  TYR   K CG  
18568 C  CD1 . TYR   K  87  ? 1.4176 0.4663 1.1790 0.0129  -0.3499 0.0366  88  TYR   K CD1 
18569 C  CD2 . TYR   K  87  ? 1.4242 0.4416 1.1636 0.0175  -0.3318 -0.0002 88  TYR   K CD2 
18570 C  CE1 . TYR   K  87  ? 1.4172 0.5238 1.2071 0.0074  -0.3436 0.0413  88  TYR   K CE1 
18571 C  CE2 . TYR   K  87  ? 1.4301 0.4996 1.1756 0.0253  -0.3365 0.0028  88  TYR   K CE2 
18572 C  CZ  . TYR   K  87  ? 1.4770 0.5026 1.1956 0.0221  -0.3294 -0.0095 88  TYR   K CZ  
18573 O  OH  . TYR   K  87  ? 1.4887 0.6431 1.2331 0.0376  -0.3363 0.0009  88  TYR   K OH  
18574 N  N   . GLN   K  88  ? 1.3993 0.5103 1.1775 -0.0103 -0.3693 0.0340  89  GLN   K N   
18575 C  CA  . GLN   K  88  ? 1.4173 0.6317 1.1600 -0.0471 -0.3821 0.0438  89  GLN   K CA  
18576 C  C   . GLN   K  88  ? 1.3942 0.6091 1.1705 -0.0260 -0.3916 0.0482  89  GLN   K C   
18577 O  O   . GLN   K  88  ? 1.4309 0.7292 1.1661 0.0094  -0.3998 0.0899  89  GLN   K O   
18578 C  CB  . GLN   K  88  ? 1.4573 0.6592 1.2447 -0.0428 -0.3651 -0.0299 89  GLN   K CB  
18579 C  CG  . GLN   K  88  ? 1.5359 0.6654 1.3710 -0.1324 -0.3487 -0.0716 89  GLN   K CG  
18580 C  CD  . GLN   K  88  ? 1.6340 0.7736 1.4803 -0.2093 -0.3205 -0.1974 89  GLN   K CD  
18581 O  OE1 . GLN   K  88  ? 1.6240 0.8454 1.6876 -0.2476 -0.2779 -0.3034 89  GLN   K OE1 
18582 N  NE2 . GLN   K  88  ? 1.6405 0.9815 1.5334 -0.2543 -0.3581 -0.1850 89  GLN   K NE2 
18583 N  N   . TYR   K  89  ? 1.3893 0.5451 1.1785 -0.0127 -0.3652 0.0949  90  TYR   K N   
18584 C  CA  . TYR   K  89  ? 1.4148 0.5984 1.1612 0.0168  -0.3322 0.1235  90  TYR   K CA  
18585 C  C   . TYR   K  89  ? 1.3893 0.6042 1.1683 0.0374  -0.3201 0.1817  90  TYR   K C   
18586 O  O   . TYR   K  89  ? 1.3648 0.5432 1.1176 0.1206  -0.3362 0.1620  90  TYR   K O   
18587 C  CB  . TYR   K  89  ? 1.4167 0.5701 1.1505 0.0215  -0.2777 0.1549  90  TYR   K CB  
18588 C  CG  . TYR   K  89  ? 1.4533 0.4899 1.0846 -0.0035 -0.2696 0.1792  90  TYR   K CG  
18589 C  CD1 . TYR   K  89  ? 1.4403 0.4759 1.0666 -0.0163 -0.2841 0.1607  90  TYR   K CD1 
18590 C  CD2 . TYR   K  89  ? 1.4589 0.4281 1.1292 0.0112  -0.2402 0.1386  90  TYR   K CD2 
18591 C  CE1 . TYR   K  89  ? 1.4320 0.4478 1.0622 -0.0488 -0.2732 0.1548  90  TYR   K CE1 
18592 C  CE2 . TYR   K  89  ? 1.4788 0.4335 1.1009 -0.0187 -0.2196 0.1132  90  TYR   K CE2 
18593 C  CZ  . TYR   K  89  ? 1.4572 0.4144 1.0928 -0.0354 -0.2434 0.1388  90  TYR   K CZ  
18594 O  OH  . TYR   K  89  ? 1.4873 0.4893 1.1187 -0.0338 -0.1984 0.0998  90  TYR   K OH  
18595 N  N   . LYS   K  90  ? 1.4188 0.6561 1.2110 0.0557  -0.2854 0.1552  91  LYS   K N   
18596 C  CA  . LYS   K  90  ? 1.4625 0.6215 1.2190 0.0487  -0.2703 0.1829  91  LYS   K CA  
18597 C  C   . LYS   K  90  ? 1.4366 0.6702 1.2317 0.0352  -0.3309 0.1561  91  LYS   K C   
18598 O  O   . LYS   K  90  ? 1.4281 0.6596 1.2308 0.0150  -0.3108 0.1438  91  LYS   K O   
18599 C  CB  . LYS   K  90  ? 1.4952 0.6442 1.2394 0.0339  -0.2400 0.1745  91  LYS   K CB  
18600 C  CG  . LYS   K  90  ? 1.5195 0.6056 1.2690 0.0236  -0.2361 0.1890  91  LYS   K CG  
18601 C  CD  . LYS   K  90  ? 1.5394 0.6266 1.2805 0.0083  -0.2232 0.1695  91  LYS   K CD  
18602 C  CE  . LYS   K  90  ? 1.5469 0.5916 1.3038 -0.0167 -0.2393 0.1613  91  LYS   K CE  
18603 N  NZ  . LYS   K  90  ? 1.5486 0.6535 1.3421 -0.0486 -0.2529 0.1607  91  LYS   K NZ  
18604 N  N   . GLY   K  91  ? 1.4787 0.6647 1.2544 0.1015  -0.3264 0.2376  92  GLY   K N   
18605 C  CA  . GLY   K  91  ? 1.4996 0.6986 1.2464 0.1210  -0.3554 0.2268  92  GLY   K CA  
18606 C  C   . GLY   K  91  ? 1.5021 0.6520 1.1862 0.1283  -0.3905 0.2540  92  GLY   K C   
18607 O  O   . GLY   K  91  ? 1.5161 0.7070 1.1842 0.1061  -0.3948 0.2917  92  GLY   K O   
18608 N  N   . ALA   K  92  ? 1.5064 0.6497 1.1441 0.1158  -0.3758 0.1824  93  ALA   K N   
18609 C  CA  . ALA   K  92  ? 1.5524 0.5957 1.0871 0.1023  -0.3814 0.1880  93  ALA   K CA  
18610 C  C   . ALA   K  92  ? 1.5813 0.5299 1.0984 0.1282  -0.3759 0.2349  93  ALA   K C   
18611 O  O   . ALA   K  92  ? 1.6174 0.5399 0.9905 0.2144  -0.4214 0.2324  93  ALA   K O   
18612 C  CB  . ALA   K  92  ? 1.5301 0.5586 1.0867 0.0675  -0.3634 0.1215  93  ALA   K CB  
18613 N  N   . GLY   K  93  ? 1.6127 0.4700 1.1889 0.1160  -0.3913 0.1710  94  GLY   K N   
18614 C  CA  . GLY   K  93  ? 1.6054 0.5431 1.2936 0.0715  -0.4082 0.1655  94  GLY   K CA  
18615 C  C   . GLY   K  93  ? 1.5876 0.5687 1.3348 0.0823  -0.4063 0.1368  94  GLY   K C   
18616 O  O   . GLY   K  93  ? 1.5738 0.6779 1.4471 0.0373  -0.3918 0.1774  94  GLY   K O   
18617 N  N   . LEU   K  94  ? 1.6361 0.5183 1.2935 0.0409  -0.3640 0.0897  95  LEU   K N   
18618 C  CA  . LEU   K  94  ? 1.6341 0.5336 1.2526 0.0356  -0.3592 0.0099  95  LEU   K CA  
18619 C  C   . LEU   K  94  ? 1.6496 0.4154 1.3196 -0.0153 -0.3407 0.0176  95  LEU   K C   
18620 O  O   . LEU   K  94  ? 1.6729 0.2336 1.3361 -0.0557 -0.3183 -0.0322 95  LEU   K O   
18621 C  CB  . LEU   K  94  ? 1.6358 0.5648 1.2429 0.0394  -0.3571 0.0352  95  LEU   K CB  
18622 C  CG  . LEU   K  94  ? 1.6062 0.6061 1.2035 0.0127  -0.3778 0.0081  95  LEU   K CG  
18623 C  CD1 . LEU   K  94  ? 1.5409 0.6107 1.1705 0.0189  -0.4153 0.0198  95  LEU   K CD1 
18624 C  CD2 . LEU   K  94  ? 1.6054 0.6872 1.2090 0.0154  -0.3819 0.0073  95  LEU   K CD2 
18625 N  N   . SER   K  95  ? 1.6392 0.4737 1.2902 -0.0127 -0.3267 -0.0362 96  SER   K N   
18626 C  CA  . SER   K  95  ? 1.6399 0.5258 1.2934 -0.0344 -0.3093 -0.0601 96  SER   K CA  
18627 C  C   . SER   K  95  ? 1.6258 0.4908 1.2823 -0.0154 -0.3042 -0.0977 96  SER   K C   
18628 O  O   . SER   K  95  ? 1.6165 0.4569 1.3083 -0.0160 -0.3202 -0.1046 96  SER   K O   
18629 C  CB  . SER   K  95  ? 1.6917 0.5647 1.2745 -0.0728 -0.3025 -0.0266 96  SER   K CB  
18630 O  OG  . SER   K  95  ? 1.7639 0.5434 1.2685 -0.0705 -0.2592 -0.0498 96  SER   K OG  
18631 N  N   . MET   K  96  ? 1.5793 0.4861 1.2514 -0.0208 -0.2956 -0.1447 97  MET   K N   
18632 C  CA  . MET   K  96  ? 1.5519 0.5582 1.2973 -0.0229 -0.3103 -0.1449 97  MET   K CA  
18633 C  C   . MET   K  96  ? 1.5267 0.5773 1.3509 -0.0070 -0.2673 -0.1307 97  MET   K C   
18634 O  O   . MET   K  96  ? 1.5364 0.4366 1.3417 -0.0550 -0.3433 -0.1719 97  MET   K O   
18635 C  CB  . MET   K  96  ? 1.5675 0.5498 1.2993 -0.0365 -0.2783 -0.1284 97  MET   K CB  
18636 C  CG  . MET   K  96  ? 1.6138 0.6290 1.2588 -0.0407 -0.2610 -0.1124 97  MET   K CG  
18637 S  SD  . MET   K  96  ? 1.6748 0.6369 1.3139 -0.0675 -0.1825 -0.0836 97  MET   K SD  
18638 C  CE  . MET   K  96  ? 1.5771 0.5940 1.2729 -0.0478 -0.2475 -0.0812 97  MET   K CE  
18639 N  N   . GLY   K  97  ? 1.5151 0.6404 1.3542 0.0373  -0.2913 -0.1165 98  GLY   K N   
18640 C  CA  . GLY   K  97  ? 1.5496 0.5865 1.3651 0.0442  -0.2770 -0.0894 98  GLY   K CA  
18641 C  C   . GLY   K  97  ? 1.5980 0.5257 1.3922 0.0772  -0.2572 -0.0651 98  GLY   K C   
18642 O  O   . GLY   K  97  ? 1.6049 0.5309 1.5144 0.0699  -0.1304 -0.0721 98  GLY   K O   
18643 N  N   . THR   K  98  ? 1.6144 0.5391 1.3553 0.0972  -0.2774 -0.0467 99  THR   K N   
18644 C  CA  . THR   K  98  ? 1.6804 0.5778 1.3121 0.0993  -0.3160 -0.0211 99  THR   K CA  
18645 C  C   . THR   K  98  ? 1.6773 0.5519 1.2706 0.1059  -0.3847 -0.0063 99  THR   K C   
18646 O  O   . THR   K  98  ? 1.6597 0.4872 1.2184 0.1435  -0.4212 0.0364  99  THR   K O   
18647 C  CB  . THR   K  98  ? 1.6878 0.5720 1.3394 0.1129  -0.3112 -0.0151 99  THR   K CB  
18648 O  OG1 . THR   K  98  ? 1.7434 0.4423 1.3191 0.0995  -0.2699 -0.0492 99  THR   K OG1 
18649 C  CG2 . THR   K  98  ? 1.6960 0.5869 1.3723 0.1202  -0.2863 0.0042  99  THR   K CG2 
18650 N  N   . MET   K  99  ? 1.7069 0.5954 1.2618 0.0395  -0.4303 -0.0057 100 MET   K N   
18651 C  CA  . MET   K  99  ? 1.7601 0.6027 1.2850 0.0276  -0.4421 0.0256  100 MET   K CA  
18652 C  C   . MET   K  99  ? 1.7417 0.5518 1.2379 -0.0215 -0.5028 0.0826  100 MET   K C   
18653 O  O   . MET   K  99  ? 1.7131 0.4060 1.1632 -0.0175 -0.5545 0.1620  100 MET   K O   
18654 C  CB  . MET   K  99  ? 1.8092 0.7111 1.3081 0.0268  -0.4443 -0.0372 100 MET   K CB  
18655 C  CG  . MET   K  99  ? 1.8565 0.7140 1.3434 0.0840  -0.4200 -0.0243 100 MET   K CG  
18656 S  SD  . MET   K  99  ? 1.9701 0.8040 1.3763 0.0972  -0.4296 -0.0805 100 MET   K SD  
18657 C  CE  . MET   K  99  ? 1.9657 0.7938 1.3552 0.0718  -0.4545 -0.0626 100 MET   K CE  
18658 N  N   . ILE   K  100 ? 1.7733 0.5182 1.2587 -0.0257 -0.5250 0.0643  101 ILE   K N   
18659 C  CA  . ILE   K  100 ? 1.7919 0.4790 1.3288 -0.0638 -0.5197 0.0804  101 ILE   K CA  
18660 C  C   . ILE   K  100 ? 1.8393 0.4267 1.3450 -0.0863 -0.5498 0.1168  101 ILE   K C   
18661 O  O   . ILE   K  100 ? 1.8165 0.3734 1.3215 -0.1311 -0.5741 0.1914  101 ILE   K O   
18662 C  CB  . ILE   K  100 ? 1.7828 0.4672 1.3644 -0.0656 -0.4888 0.0698  101 ILE   K CB  
18663 C  CG1 . ILE   K  100 ? 1.7341 0.4456 1.3445 -0.0582 -0.4573 0.0491  101 ILE   K CG1 
18664 C  CG2 . ILE   K  100 ? 1.8003 0.5010 1.4320 -0.0328 -0.4982 0.0794  101 ILE   K CG2 
18665 C  CD1 . ILE   K  100 ? 1.7112 0.4559 1.3633 -0.0640 -0.4556 0.0272  101 ILE   K CD1 
18666 N  N   . CYS   K  101 ? 1.8609 0.4483 1.4033 -0.0504 -0.5754 0.1026  102 CYS   K N   
18667 C  CA  . CYS   K  101 ? 1.9483 0.5610 1.4096 -0.0237 -0.5973 0.0585  102 CYS   K CA  
18668 C  C   . CYS   K  101 ? 1.9510 0.5943 1.4379 0.0150  -0.5732 0.0472  102 CYS   K C   
18669 O  O   . CYS   K  101 ? 1.9128 0.5926 1.4698 0.0694  -0.5836 0.0605  102 CYS   K O   
18670 C  CB  . CYS   K  101 ? 1.9895 0.5991 1.4513 -0.0472 -0.6299 0.0289  102 CYS   K CB  
18671 S  SG  . CYS   K  101 ? 2.0061 0.5540 1.4908 0.0087  -0.6825 -0.0551 102 CYS   K SG  
18672 N  N   . GLY   K  102 ? 2.0142 0.6495 1.4372 -0.0260 -0.5250 0.0381  103 GLY   K N   
18673 C  CA  . GLY   K  102 ? 2.0058 0.6907 1.4520 -0.0238 -0.5293 0.0840  103 GLY   K CA  
18674 C  C   . GLY   K  102 ? 2.0481 0.7715 1.4540 -0.0689 -0.5328 0.1054  103 GLY   K C   
18675 O  O   . GLY   K  102 ? 2.0581 0.6607 1.3790 -0.1071 -0.5191 0.1295  103 GLY   K O   
18676 N  N   . TYR   K  103 ? 2.0640 0.8697 1.5508 -0.0348 -0.5556 0.1533  104 TYR   K N   
18677 C  CA  . TYR   K  103 ? 2.1352 1.0383 1.5467 0.0032  -0.5407 0.1951  104 TYR   K CA  
18678 C  C   . TYR   K  103 ? 2.0555 1.0649 1.5381 0.0424  -0.5587 0.1193  104 TYR   K C   
18679 O  O   . TYR   K  103 ? 1.9671 0.9753 1.5717 0.0835  -0.6725 0.0656  104 TYR   K O   
18680 C  CB  . TYR   K  103 ? 2.1882 1.2109 1.6198 0.0609  -0.6104 0.2799  104 TYR   K CB  
18681 C  CG  . TYR   K  103 ? 2.3545 1.5287 1.6570 0.0393  -0.5698 0.4027  104 TYR   K CG  
18682 C  CD1 . TYR   K  103 ? 2.4769 1.5778 1.7922 0.0968  -0.5257 0.3094  104 TYR   K CD1 
18683 C  CD2 . TYR   K  103 ? 2.3877 1.6168 1.7406 0.0941  -0.5252 0.3608  104 TYR   K CD2 
18684 C  CE1 . TYR   K  103 ? 2.5594 1.7552 1.8105 0.0752  -0.5314 0.3839  104 TYR   K CE1 
18685 C  CE2 . TYR   K  103 ? 2.5191 1.9258 1.6924 0.0392  -0.5158 0.4265  104 TYR   K CE2 
18686 C  CZ  . TYR   K  103 ? 2.5818 1.9057 1.6581 0.0191  -0.5259 0.5057  104 TYR   K CZ  
18687 O  OH  . TYR   K  103 ? 2.5937 2.0782 1.5578 0.0007  -0.6489 0.5388  104 TYR   K OH  
18688 N  N   . THR   K  104 ? 2.1025 1.0302 1.4912 0.0044  -0.5378 0.0643  105 THR   K N   
18689 C  CA  . THR   K  104 ? 2.0906 1.0385 1.5090 -0.0169 -0.5042 0.0386  105 THR   K CA  
18690 C  C   . THR   K  104 ? 2.1105 1.0470 1.4702 -0.0494 -0.5229 -0.0098 105 THR   K C   
18691 O  O   . THR   K  104 ? 2.0946 1.1279 1.3698 -0.1580 -0.5778 -0.0811 105 THR   K O   
18692 C  CB  . THR   K  104 ? 2.0499 1.1073 1.5057 -0.0083 -0.4770 0.0180  105 THR   K CB  
18693 O  OG1 . THR   K  104 ? 2.0655 1.0547 1.4528 -0.0147 -0.4672 0.0121  105 THR   K OG1 
18694 C  CG2 . THR   K  104 ? 2.0086 1.0899 1.5340 0.0051  -0.4442 0.0285  105 THR   K CG2 
18695 N  N   . ARG   K  105 ? 2.1501 1.0953 1.5014 -0.0479 -0.4916 0.1095  106 ARG   K N   
18696 C  CA  . ARG   K  105 ? 2.2474 1.1108 1.5259 -0.0704 -0.4899 0.1460  106 ARG   K CA  
18697 C  C   . ARG   K  105 ? 2.2616 1.0168 1.4312 -0.0758 -0.4631 0.1791  106 ARG   K C   
18698 O  O   . ARG   K  105 ? 2.3648 1.0535 1.4692 -0.1718 -0.4303 0.1118  106 ARG   K O   
18699 C  CB  . ARG   K  105 ? 2.2683 1.1535 1.6475 -0.0059 -0.4988 0.1720  106 ARG   K CB  
18700 C  CG  . ARG   K  105 ? 2.3115 1.2789 1.7328 0.0013  -0.5534 0.1981  106 ARG   K CG  
18701 C  CD  . ARG   K  105 ? 2.4021 1.4499 1.7532 -0.0306 -0.5191 0.1640  106 ARG   K CD  
18702 N  NE  . ARG   K  105 ? 2.4650 1.5587 1.8986 0.0085  -0.5709 0.2118  106 ARG   K NE  
18703 C  CZ  . ARG   K  105 ? 2.4938 1.5872 2.0360 -0.0303 -0.5423 0.1846  106 ARG   K CZ  
18704 N  NH1 . ARG   K  105 ? 2.4732 1.6095 2.0389 -0.0605 -0.5114 0.1584  106 ARG   K NH1 
18705 N  NH2 . ARG   K  105 ? 2.5497 1.5789 2.1365 -0.0265 -0.5484 0.2341  106 ARG   K NH2 
18706 N  N   . LYS   K  106 ? 2.2228 0.9416 1.4090 -0.0144 -0.4944 0.2830  107 LYS   K N   
18707 C  CA  . LYS   K  106 ? 2.2193 0.9908 1.4096 0.0130  -0.5053 0.2751  107 LYS   K CA  
18708 C  C   . LYS   K  106 ? 2.1459 1.0168 1.3129 0.0230  -0.4527 0.2147  107 LYS   K C   
18709 O  O   . LYS   K  106 ? 2.1953 1.0835 1.2435 0.0461  -0.4402 0.2161  107 LYS   K O   
18710 C  CB  . LYS   K  106 ? 2.2212 0.9758 1.5520 0.0060  -0.5388 0.2310  107 LYS   K CB  
18711 C  CG  . LYS   K  106 ? 2.2012 0.9733 1.5730 0.0339  -0.5202 0.2290  107 LYS   K CG  
18712 C  CD  . LYS   K  106 ? 2.1961 1.0245 1.6760 0.0398  -0.5375 0.1734  107 LYS   K CD  
18713 C  CE  . LYS   K  106 ? 2.1937 1.0881 1.7186 0.0495  -0.5522 0.1172  107 LYS   K CE  
18714 N  NZ  . LYS   K  106 ? 2.1896 1.0719 1.7077 0.0742  -0.5483 0.0769  107 LYS   K NZ  
18715 N  N   . GLU   K  107 ? 2.0571 0.9925 1.3426 0.0456  -0.4298 0.1832  108 GLU   K N   
18716 C  CA  . GLU   K  107 ? 2.0309 0.9923 1.3092 0.0385  -0.4120 0.2168  108 GLU   K CA  
18717 C  C   . GLU   K  107 ? 2.0206 0.9574 1.3104 0.0418  -0.4302 0.2496  108 GLU   K C   
18718 O  O   . GLU   K  107 ? 2.1064 0.8917 1.2902 0.0522  -0.4024 0.3082  108 GLU   K O   
18719 C  CB  . GLU   K  107 ? 1.9926 0.9647 1.3092 0.0710  -0.3761 0.1948  108 GLU   K CB  
18720 C  CG  . GLU   K  107 ? 1.9882 0.9592 1.3244 0.0962  -0.3422 0.1348  108 GLU   K CG  
18721 C  CD  . GLU   K  107 ? 1.9455 0.9567 1.3164 0.1348  -0.3187 0.1032  108 GLU   K CD  
18722 O  OE1 . GLU   K  107 ? 1.9298 0.9933 1.3002 0.1404  -0.2957 0.1345  108 GLU   K OE1 
18723 O  OE2 . GLU   K  107 ? 1.9757 0.9202 1.3497 0.1396  -0.2747 0.0581  108 GLU   K OE2 
18724 N  N   . GLY   K  108 ? 2.0202 0.9972 1.3800 0.0274  -0.4629 0.2613  109 GLY   K N   
18725 C  CA  . GLY   K  108 ? 2.0115 1.0279 1.3853 0.0230  -0.4802 0.2547  109 GLY   K CA  
18726 C  C   . GLY   K  108 ? 1.9357 0.9856 1.3552 0.0253  -0.4876 0.2168  109 GLY   K C   
18727 O  O   . GLY   K  108 ? 1.9108 1.0470 1.3664 0.0672  -0.4762 0.1574  109 GLY   K O   
18728 N  N   . PRO   K  109 ? 1.9062 1.0165 1.3456 0.0024  -0.4856 0.2083  110 PRO   K N   
18729 C  CA  . PRO   K  109 ? 1.8250 0.9477 1.3639 0.0179  -0.4581 0.1752  110 PRO   K CA  
18730 C  C   . PRO   K  109 ? 1.7881 0.8190 1.2984 -0.0058 -0.4179 0.1374  110 PRO   K C   
18731 O  O   . PRO   K  109 ? 1.8052 0.8487 1.3369 -0.0389 -0.3841 0.1190  110 PRO   K O   
18732 C  CB  . PRO   K  109 ? 1.8245 0.9840 1.3408 0.0046  -0.4817 0.1966  110 PRO   K CB  
18733 C  CG  . PRO   K  109 ? 1.8933 1.0903 1.3346 -0.0223 -0.4938 0.2110  110 PRO   K CG  
18734 C  CD  . PRO   K  109 ? 1.9523 1.0925 1.3465 -0.0342 -0.4975 0.2219  110 PRO   K CD  
18735 N  N   . THR   K  110 ? 1.7400 0.7395 1.2959 -0.0017 -0.4165 0.1255  111 THR   K N   
18736 C  CA  . THR   K  110 ? 1.7129 0.7468 1.2879 -0.0057 -0.4118 0.0756  111 THR   K CA  
18737 C  C   . THR   K  110 ? 1.6770 0.7436 1.2774 -0.0198 -0.4524 0.0692  111 THR   K C   
18738 O  O   . THR   K  110 ? 1.6398 0.7442 1.2592 0.0025  -0.5006 0.0481  111 THR   K O   
18739 C  CB  . THR   K  110 ? 1.7041 0.7052 1.2607 0.0251  -0.3897 0.0802  111 THR   K CB  
18740 O  OG1 . THR   K  110 ? 1.7625 0.7359 1.2553 0.0583  -0.3911 0.0948  111 THR   K OG1 
18741 C  CG2 . THR   K  110 ? 1.6814 0.7053 1.2262 0.0405  -0.3508 0.0756  111 THR   K CG2 
18742 N  N   . ILE   K  111 ? 1.6589 0.7396 1.3083 -0.0228 -0.4719 0.0259  112 ILE   K N   
18743 C  CA  . ILE   K  111 ? 1.6689 0.6919 1.3185 -0.0254 -0.4492 0.0108  112 ILE   K CA  
18744 C  C   . ILE   K  111 ? 1.6703 0.5453 1.2447 -0.0706 -0.4271 -0.0182 112 ILE   K C   
18745 O  O   . ILE   K  111 ? 1.7198 0.5538 1.2146 -0.1022 -0.3925 -0.0295 112 ILE   K O   
18746 C  CB  . ILE   K  111 ? 1.6688 0.7176 1.3627 -0.0249 -0.4708 -0.0234 112 ILE   K CB  
18747 C  CG1 . ILE   K  111 ? 1.7026 0.7995 1.4064 -0.0081 -0.5086 -0.0208 112 ILE   K CG1 
18748 C  CG2 . ILE   K  111 ? 1.6273 0.7403 1.3645 -0.0083 -0.4416 -0.0226 112 ILE   K CG2 
18749 C  CD1 . ILE   K  111 ? 1.7249 0.8514 1.4187 -0.0212 -0.5056 -0.0640 112 ILE   K CD1 
18750 N  N   . TYR   K  112 ? 1.6654 0.4620 1.2454 -0.0911 -0.4207 -0.0160 113 TYR   K N   
18751 C  CA  . TYR   K  112 ? 1.6446 0.5186 1.2661 -0.0864 -0.4123 -0.0099 113 TYR   K CA  
18752 C  C   . TYR   K  112 ? 1.6192 0.4799 1.2369 -0.0922 -0.4462 -0.0412 113 TYR   K C   
18753 O  O   . TYR   K  112 ? 1.5751 0.4279 1.2344 -0.0904 -0.4786 -0.0585 113 TYR   K O   
18754 C  CB  . TYR   K  112 ? 1.6635 0.5279 1.2620 -0.0966 -0.3859 -0.0150 113 TYR   K CB  
18755 C  CG  . TYR   K  112 ? 1.6984 0.5898 1.3118 -0.1143 -0.3451 0.0011  113 TYR   K CG  
18756 C  CD1 . TYR   K  112 ? 1.6959 0.5739 1.3122 -0.1102 -0.3165 -0.0088 113 TYR   K CD1 
18757 C  CD2 . TYR   K  112 ? 1.7118 0.5684 1.3315 -0.1187 -0.3506 0.0009  113 TYR   K CD2 
18758 C  CE1 . TYR   K  112 ? 1.7021 0.6067 1.3050 -0.1231 -0.2961 -0.0218 113 TYR   K CE1 
18759 C  CE2 . TYR   K  112 ? 1.7483 0.5598 1.3067 -0.0976 -0.3344 0.0125  113 TYR   K CE2 
18760 C  CZ  . TYR   K  112 ? 1.7434 0.6150 1.2962 -0.1212 -0.2864 -0.0010 113 TYR   K CZ  
18761 O  OH  . TYR   K  112 ? 1.7601 0.6062 1.2770 -0.0889 -0.2649 0.0123  113 TYR   K OH  
18762 N  N   . TYR   K  113 ? 1.6355 0.5226 1.2426 -0.0673 -0.4624 -0.0464 114 TYR   K N   
18763 C  CA  . TYR   K  113 ? 1.6553 0.5567 1.3020 -0.0725 -0.4618 0.0021  114 TYR   K CA  
18764 C  C   . TYR   K  113 ? 1.6735 0.4716 1.2340 0.0173  -0.4243 0.0015  114 TYR   K C   
18765 O  O   . TYR   K  113 ? 1.6355 0.3771 1.3420 0.0964  -0.4036 0.0339  114 TYR   K O   
18766 C  CB  . TYR   K  113 ? 1.6369 0.5364 1.3214 -0.1288 -0.4738 -0.0317 114 TYR   K CB  
18767 C  CG  . TYR   K  113 ? 1.5916 0.6085 1.3083 -0.2253 -0.5209 0.0020  114 TYR   K CG  
18768 C  CD1 . TYR   K  113 ? 1.5793 0.6868 1.3300 -0.2530 -0.5309 0.0360  114 TYR   K CD1 
18769 C  CD2 . TYR   K  113 ? 1.5936 0.6448 1.3103 -0.2461 -0.5253 -0.0047 114 TYR   K CD2 
18770 C  CE1 . TYR   K  113 ? 1.5527 0.6568 1.3501 -0.2844 -0.5407 0.0422  114 TYR   K CE1 
18771 C  CE2 . TYR   K  113 ? 1.5677 0.6430 1.2995 -0.3061 -0.5250 0.0023  114 TYR   K CE2 
18772 C  CZ  . TYR   K  113 ? 1.5747 0.6208 1.3092 -0.3076 -0.5482 0.0105  114 TYR   K CZ  
18773 O  OH  . TYR   K  113 ? 1.6099 0.5708 1.2326 -0.3777 -0.5273 -0.0248 114 TYR   K OH  
18774 N  N   . VAL   K  114 ? 1.6836 0.4524 1.2343 0.0280  -0.4090 0.0358  115 VAL   K N   
18775 C  CA  . VAL   K  114 ? 1.6849 0.4906 1.1971 0.0037  -0.3695 0.0318  115 VAL   K CA  
18776 C  C   . VAL   K  114 ? 1.6368 0.4087 1.2170 -0.0133 -0.3724 0.0036  115 VAL   K C   
18777 O  O   . VAL   K  114 ? 1.6389 0.3858 1.2453 -0.0089 -0.3525 0.0039  115 VAL   K O   
18778 C  CB  . VAL   K  114 ? 1.6861 0.5455 1.1794 0.0495  -0.3648 0.0300  115 VAL   K CB  
18779 C  CG1 . VAL   K  114 ? 1.6638 0.6124 1.2136 0.0248  -0.3726 0.0020  115 VAL   K CG1 
18780 C  CG2 . VAL   K  114 ? 1.7089 0.5975 1.1277 0.0295  -0.3749 0.0330  115 VAL   K CG2 
18781 N  N   . ASP   K  115 ? 1.6186 0.4293 1.1850 -0.0476 -0.3709 0.0276  116 ASP   K N   
18782 C  CA  . ASP   K  115 ? 1.5910 0.5518 1.1755 -0.0680 -0.3776 0.0802  116 ASP   K CA  
18783 C  C   . ASP   K  115 ? 1.5849 0.4687 1.1332 -0.0352 -0.3482 0.0900  116 ASP   K C   
18784 O  O   . ASP   K  115 ? 1.5368 0.4485 1.1759 -0.0114 -0.3460 0.0239  116 ASP   K O   
18785 C  CB  . ASP   K  115 ? 1.5930 0.5218 1.2054 -0.0666 -0.3735 0.1517  116 ASP   K CB  
18786 C  CG  . ASP   K  115 ? 1.5835 0.6787 1.2262 -0.1373 -0.4039 0.2241  116 ASP   K CG  
18787 O  OD1 . ASP   K  115 ? 1.6007 0.7109 1.2189 -0.1131 -0.4265 0.1669  116 ASP   K OD1 
18788 O  OD2 . ASP   K  115 ? 1.6006 0.5533 1.2052 -0.2114 -0.3988 0.3030  116 ASP   K OD2 
18789 N  N   . SER   K  116 ? 1.6291 0.4877 1.0916 -0.0354 -0.3524 0.0672  117 SER   K N   
18790 C  CA  . SER   K  116 ? 1.6455 0.4715 1.1145 -0.0661 -0.3480 0.0252  117 SER   K CA  
18791 C  C   . SER   K  116 ? 1.6449 0.4988 1.1237 -0.0554 -0.3603 0.0460  117 SER   K C   
18792 O  O   . SER   K  116 ? 1.7122 0.4256 1.1403 -0.0356 -0.3940 0.0785  117 SER   K O   
18793 C  CB  . SER   K  116 ? 1.6765 0.4732 1.0523 -0.0497 -0.3237 -0.0189 117 SER   K CB  
18794 O  OG  . SER   K  116 ? 1.7559 0.4504 1.0381 -0.0240 -0.2819 0.0588  117 SER   K OG  
18795 N  N   . ASP   K  117 ? 1.5921 0.5475 1.1119 -0.0737 -0.3965 0.0024  118 ASP   K N   
18796 C  CA  . ASP   K  117 ? 1.6002 0.7114 1.1651 -0.1027 -0.3936 0.0570  118 ASP   K CA  
18797 C  C   . ASP   K  117 ? 1.5897 0.6494 1.1588 -0.0444 -0.3880 0.0511  118 ASP   K C   
18798 O  O   . ASP   K  117 ? 1.5794 0.6178 1.1718 -0.0094 -0.4130 0.1314  118 ASP   K O   
18799 C  CB  . ASP   K  117 ? 1.6526 0.7925 1.3210 -0.0600 -0.3621 0.0185  118 ASP   K CB  
18800 C  CG  . ASP   K  117 ? 1.7336 0.8174 1.4276 -0.1473 -0.3461 0.0205  118 ASP   K CG  
18801 O  OD1 . ASP   K  117 ? 1.8042 1.0404 1.4635 -0.0582 -0.2621 0.1745  118 ASP   K OD1 
18802 O  OD2 . ASP   K  117 ? 1.9124 0.8370 1.5979 0.0173  -0.2627 0.1978  118 ASP   K OD2 
18803 N  N   . GLY   K  118 ? 1.5798 0.6560 1.1398 -0.0449 -0.3895 0.0260  119 GLY   K N   
18804 C  CA  . GLY   K  118 ? 1.6210 0.6913 1.0808 -0.0817 -0.3607 0.0253  119 GLY   K CA  
18805 C  C   . GLY   K  118 ? 1.6460 0.7051 1.0807 -0.1007 -0.3521 0.0187  119 GLY   K C   
18806 O  O   . GLY   K  118 ? 1.7377 0.7839 1.1446 -0.1373 -0.3148 0.0686  119 GLY   K O   
18807 N  N   . THR   K  119 ? 1.5989 0.6701 1.0398 -0.0888 -0.3256 0.0437  120 THR   K N   
18808 C  CA  . THR   K  119 ? 1.6014 0.7013 1.0553 -0.0926 -0.3087 -0.0217 120 THR   K CA  
18809 C  C   . THR   K  119 ? 1.6146 0.6781 1.0545 -0.0666 -0.3113 -0.0802 120 THR   K C   
18810 O  O   . THR   K  119 ? 1.6336 0.7055 1.0335 -0.1055 -0.2877 -0.1003 120 THR   K O   
18811 C  CB  . THR   K  119 ? 1.5853 0.7147 1.0587 -0.1173 -0.3111 -0.0216 120 THR   K CB  
18812 O  OG1 . THR   K  119 ? 1.4959 0.9282 1.0549 -0.0915 -0.3313 -0.0255 120 THR   K OG1 
18813 C  CG2 . THR   K  119 ? 1.6058 0.7640 1.0718 -0.1291 -0.2889 -0.0312 120 THR   K CG2 
18814 N  N   . ARG   K  120 ? 1.6188 0.5670 1.0754 -0.0374 -0.3083 -0.1012 121 ARG   K N   
18815 C  CA  . ARG   K  120 ? 1.6241 0.5547 1.0957 -0.0250 -0.3097 -0.0918 121 ARG   K CA  
18816 C  C   . ARG   K  120 ? 1.6315 0.4810 1.0870 -0.0086 -0.3103 -0.0643 121 ARG   K C   
18817 O  O   . ARG   K  120 ? 1.6309 0.4137 1.0164 -0.0258 -0.3367 -0.1068 121 ARG   K O   
18818 C  CB  . ARG   K  120 ? 1.6202 0.5657 1.1458 -0.0005 -0.3139 -0.1180 121 ARG   K CB  
18819 C  CG  . ARG   K  120 ? 1.6432 0.6213 1.1657 0.0146  -0.3205 -0.0923 121 ARG   K CG  
18820 C  CD  . ARG   K  120 ? 1.6560 0.6124 1.1866 0.0282  -0.2863 -0.0839 121 ARG   K CD  
18821 N  NE  . ARG   K  120 ? 1.6649 0.5727 1.2187 0.0514  -0.2586 -0.0907 121 ARG   K NE  
18822 C  CZ  . ARG   K  120 ? 1.6830 0.5127 1.2652 0.0373  -0.2217 -0.1330 121 ARG   K CZ  
18823 N  NH1 . ARG   K  120 ? 1.6811 0.3764 1.3159 0.0320  -0.2316 -0.1789 121 ARG   K NH1 
18824 N  NH2 . ARG   K  120 ? 1.6835 0.6245 1.2986 0.0053  -0.1849 -0.1760 121 ARG   K NH2 
18825 N  N   . LEU   K  121 ? 1.6000 0.4628 1.1358 -0.0174 -0.3173 -0.0344 122 LEU   K N   
18826 C  CA  . LEU   K  121 ? 1.6279 0.5354 1.1468 -0.0388 -0.3203 -0.0625 122 LEU   K CA  
18827 C  C   . LEU   K  121 ? 1.6378 0.5510 1.1998 -0.0412 -0.3490 -0.0652 122 LEU   K C   
18828 O  O   . LEU   K  121 ? 1.6640 0.4480 1.2200 -0.0915 -0.3384 -0.0590 122 LEU   K O   
18829 C  CB  . LEU   K  121 ? 1.6010 0.5354 1.1522 -0.0303 -0.3287 -0.0468 122 LEU   K CB  
18830 C  CG  . LEU   K  121 ? 1.5941 0.5026 1.1399 -0.0100 -0.3019 -0.0439 122 LEU   K CG  
18831 C  CD1 . LEU   K  121 ? 1.5783 0.5009 1.1593 0.0035  -0.3133 -0.0409 122 LEU   K CD1 
18832 C  CD2 . LEU   K  121 ? 1.5901 0.4811 1.1343 -0.0096 -0.3050 -0.0588 122 LEU   K CD2 
18833 N  N   . LYS   K  122 ? 1.7019 0.6482 1.1993 -0.0376 -0.3240 -0.0514 123 LYS   K N   
18834 C  CA  . LYS   K  122 ? 1.7333 0.7321 1.2559 -0.0346 -0.3573 0.0008  123 LYS   K CA  
18835 C  C   . LYS   K  122 ? 1.7278 0.7720 1.2603 -0.0628 -0.4074 -0.0192 123 LYS   K C   
18836 O  O   . LYS   K  122 ? 1.6784 0.9113 1.3188 -0.0665 -0.4041 -0.0220 123 LYS   K O   
18837 C  CB  . LYS   K  122 ? 1.7960 0.7207 1.3015 -0.0604 -0.3080 -0.0156 123 LYS   K CB  
18838 C  CG  . LYS   K  122 ? 1.8010 0.7849 1.3473 -0.0617 -0.3120 0.0122  123 LYS   K CG  
18839 C  CD  . LYS   K  122 ? 1.8377 0.8053 1.4099 -0.0664 -0.2656 0.0385  123 LYS   K CD  
18840 C  CE  . LYS   K  122 ? 1.8674 0.8656 1.4406 -0.0922 -0.2356 0.0376  123 LYS   K CE  
18841 N  NZ  . LYS   K  122 ? 1.8651 0.8998 1.4515 -0.0948 -0.2332 0.1094  123 LYS   K NZ  
18842 N  N   . GLY   K  123 ? 1.7349 0.7422 1.3222 -0.0680 -0.4440 0.0524  124 GLY   K N   
18843 C  CA  . GLY   K  123 ? 1.7807 0.7527 1.3523 -0.0787 -0.4450 0.0371  124 GLY   K CA  
18844 C  C   . GLY   K  123 ? 1.8261 0.7814 1.3395 -0.0852 -0.4880 0.0164  124 GLY   K C   
18845 O  O   . GLY   K  123 ? 1.7559 0.7962 1.3572 -0.1218 -0.5200 -0.0224 124 GLY   K O   
18846 N  N   . ASP   K  124 ? 1.8849 0.7909 1.3494 -0.0370 -0.4293 -0.0159 125 ASP   K N   
18847 C  CA  . ASP   K  124 ? 1.8919 0.8281 1.3410 -0.0442 -0.4159 -0.0259 125 ASP   K CA  
18848 C  C   . ASP   K  124 ? 1.8455 0.7850 1.3264 -0.0144 -0.4383 -0.0241 125 ASP   K C   
18849 O  O   . ASP   K  124 ? 1.8380 0.5951 1.2879 -0.0230 -0.4797 -0.0306 125 ASP   K O   
18850 C  CB  . ASP   K  124 ? 1.9839 0.9325 1.3815 -0.0705 -0.3289 -0.0548 125 ASP   K CB  
18851 C  CG  . ASP   K  124 ? 2.0328 0.9779 1.4120 -0.1035 -0.2774 -0.0605 125 ASP   K CG  
18852 O  OD1 . ASP   K  124 ? 1.9817 0.9450 1.3680 -0.0997 -0.2278 -0.0041 125 ASP   K OD1 
18853 O  OD2 . ASP   K  124 ? 2.1015 1.0641 1.4565 -0.1524 -0.2198 -0.0939 125 ASP   K OD2 
18854 N  N   . ILE   K  125 ? 1.8383 0.8054 1.2809 -0.0427 -0.4411 0.0125  126 ILE   K N   
18855 C  CA  . ILE   K  125 ? 1.8046 0.8243 1.2320 -0.0613 -0.4675 0.0068  126 ILE   K CA  
18856 C  C   . ILE   K  125 ? 1.7717 0.7354 1.2136 -0.0408 -0.4200 0.0389  126 ILE   K C   
18857 O  O   . ILE   K  125 ? 1.7670 0.8152 1.2064 -0.0318 -0.3621 0.0707  126 ILE   K O   
18858 C  CB  . ILE   K  125 ? 1.8337 0.8551 1.2736 -0.1101 -0.4768 -0.0302 126 ILE   K CB  
18859 C  CG1 . ILE   K  125 ? 1.8992 0.9594 1.2839 -0.1306 -0.4830 -0.0178 126 ILE   K CG1 
18860 C  CG2 . ILE   K  125 ? 1.8063 0.8920 1.2091 -0.0975 -0.4983 0.0040  126 ILE   K CG2 
18861 C  CD1 . ILE   K  125 ? 1.9431 1.0529 1.3159 -0.1394 -0.4343 -0.0657 126 ILE   K CD1 
18862 N  N   . PHE   K  126 ? 1.7213 0.6621 1.2164 -0.0371 -0.4345 0.0121  127 PHE   K N   
18863 C  CA  . PHE   K  126 ? 1.6825 0.6797 1.2006 -0.0512 -0.4628 -0.0252 127 PHE   K CA  
18864 C  C   . PHE   K  126 ? 1.6669 0.5665 1.2098 -0.0630 -0.4879 -0.0988 127 PHE   K C   
18865 O  O   . PHE   K  126 ? 1.6500 0.4537 1.2894 -0.0758 -0.4782 -0.1929 127 PHE   K O   
18866 C  CB  . PHE   K  126 ? 1.6553 0.6609 1.1352 -0.0168 -0.4799 0.0153  127 PHE   K CB  
18867 C  CG  . PHE   K  126 ? 1.6900 0.6420 1.0788 -0.0267 -0.4864 0.0770  127 PHE   K CG  
18868 C  CD1 . PHE   K  126 ? 1.6669 0.6891 1.0774 -0.0591 -0.4858 0.0776  127 PHE   K CD1 
18869 C  CD2 . PHE   K  126 ? 1.6765 0.6630 1.0458 -0.0274 -0.5008 0.1024  127 PHE   K CD2 
18870 C  CE1 . PHE   K  126 ? 1.7039 0.6672 1.0438 -0.0695 -0.4840 0.1013  127 PHE   K CE1 
18871 C  CE2 . PHE   K  126 ? 1.6868 0.7206 1.0472 -0.0506 -0.5023 0.0876  127 PHE   K CE2 
18872 C  CZ  . PHE   K  126 ? 1.7101 0.6793 1.0361 -0.0374 -0.5035 0.1015  127 PHE   K CZ  
18873 N  N   . CYS   K  127 ? 1.6850 0.5313 1.2126 -0.0743 -0.4687 -0.1063 128 CYS   K N   
18874 C  CA  . CYS   K  127 ? 1.6875 0.5181 1.2541 -0.0556 -0.4465 -0.0959 128 CYS   K CA  
18875 C  C   . CYS   K  127 ? 1.6923 0.4823 1.2319 -0.0223 -0.4100 -0.0836 128 CYS   K C   
18876 O  O   . CYS   K  127 ? 1.7123 0.4085 1.2351 0.0136  -0.3964 -0.0728 128 CYS   K O   
18877 C  CB  . CYS   K  127 ? 1.6919 0.5249 1.3255 -0.0663 -0.4581 -0.1152 128 CYS   K CB  
18878 S  SG  . CYS   K  127 ? 1.7530 0.4822 1.3492 -0.0717 -0.4872 -0.1099 128 CYS   K SG  
18879 N  N   . VAL   K  128 ? 1.6861 0.4930 1.2016 -0.0348 -0.4207 -0.0779 129 VAL   K N   
18880 C  CA  . VAL   K  128 ? 1.6557 0.5505 1.1931 -0.0128 -0.4134 -0.0528 129 VAL   K CA  
18881 C  C   . VAL   K  128 ? 1.6113 0.5608 1.1833 -0.0122 -0.4257 -0.0732 129 VAL   K C   
18882 O  O   . VAL   K  128 ? 1.6293 0.5483 1.1443 -0.0067 -0.4601 -0.1075 129 VAL   K O   
18883 C  CB  . VAL   K  128 ? 1.6625 0.5484 1.1660 -0.0427 -0.4020 -0.0348 129 VAL   K CB  
18884 C  CG1 . VAL   K  128 ? 1.6133 0.5441 1.1633 -0.0176 -0.3888 -0.0057 129 VAL   K CG1 
18885 C  CG2 . VAL   K  128 ? 1.7114 0.6030 1.1654 -0.0754 -0.3831 -0.0347 129 VAL   K CG2 
18886 N  N   . GLY   K  129 ? 1.6237 0.6283 1.2072 0.0180  -0.4128 -0.0408 130 GLY   K N   
18887 C  CA  . GLY   K  129 ? 1.6143 0.6742 1.2693 0.0107  -0.3848 -0.0273 130 GLY   K CA  
18888 C  C   . GLY   K  129 ? 1.5905 0.6816 1.3093 0.0179  -0.3928 -0.0378 130 GLY   K C   
18889 O  O   . GLY   K  129 ? 1.5944 0.7269 1.2163 -0.0351 -0.4523 -0.1205 130 GLY   K O   
18890 N  N   . SER   K  130 ? 1.5627 0.6949 1.3974 0.0302  -0.3973 0.0201  131 SER   K N   
18891 C  CA  . SER   K  130 ? 1.5530 0.7221 1.4196 0.0820  -0.4110 0.0457  131 SER   K CA  
18892 C  C   . SER   K  130 ? 1.5511 0.6315 1.4222 0.1400  -0.3942 0.0407  131 SER   K C   
18893 O  O   . SER   K  130 ? 1.4957 0.6775 1.4557 0.1941  -0.4359 0.0814  131 SER   K O   
18894 C  CB  . SER   K  130 ? 1.5522 0.8009 1.4632 0.0904  -0.4062 0.1033  131 SER   K CB  
18895 O  OG  . SER   K  130 ? 1.5246 0.9136 1.4863 0.0320  -0.3977 0.1433  131 SER   K OG  
18896 N  N   . GLY   K  131 ? 1.5770 0.6601 1.3303 0.0923  -0.4190 0.0075  132 GLY   K N   
18897 C  CA  . GLY   K  131 ? 1.6205 0.5699 1.3897 0.0519  -0.3778 -0.0613 132 GLY   K CA  
18898 C  C   . GLY   K  131 ? 1.6421 0.5574 1.2824 0.0663  -0.3984 -0.1287 132 GLY   K C   
18899 O  O   . GLY   K  131 ? 1.5544 0.3726 1.3096 0.0526  -0.3970 -0.1477 132 GLY   K O   
18900 N  N   . GLN   K  132 ? 1.6253 0.6064 1.3781 0.0457  -0.3365 -0.0517 133 GLN   K N   
18901 C  CA  . GLN   K  132 ? 1.6722 0.6476 1.3470 0.0837  -0.3284 -0.0327 133 GLN   K CA  
18902 C  C   . GLN   K  132 ? 1.7049 0.5962 1.3690 0.0994  -0.3440 -0.0362 133 GLN   K C   
18903 O  O   . GLN   K  132 ? 1.6655 0.6420 1.3178 0.0657  -0.3842 -0.1277 133 GLN   K O   
18904 C  CB  . GLN   K  132 ? 1.6188 0.6832 1.3736 0.0842  -0.3402 0.0113  133 GLN   K CB  
18905 C  CG  . GLN   K  132 ? 1.6180 0.7263 1.4369 0.1193  -0.3235 0.0217  133 GLN   K CG  
18906 C  CD  . GLN   K  132 ? 1.5771 0.7858 1.4944 0.1320  -0.3387 0.0330  133 GLN   K CD  
18907 O  OE1 . GLN   K  132 ? 1.6036 0.8608 1.5305 0.1911  -0.2589 0.0295  133 GLN   K OE1 
18908 N  NE2 . GLN   K  132 ? 1.6360 0.8571 1.5016 0.2125  -0.2807 0.0258  133 GLN   K NE2 
18909 N  N   . THR   K  133 ? 1.7315 0.5918 1.4557 0.0975  -0.3373 -0.0068 134 THR   K N   
18910 C  CA  . THR   K  133 ? 1.7291 0.5575 1.4953 0.0664  -0.3140 -0.0114 134 THR   K CA  
18911 C  C   . THR   K  133 ? 1.7514 0.4364 1.4149 0.1121  -0.2965 -0.0298 134 THR   K C   
18912 O  O   . THR   K  133 ? 1.7483 0.3467 1.4227 0.1295  -0.3091 -0.0891 134 THR   K O   
18913 C  CB  . THR   K  133 ? 1.7254 0.5504 1.5908 0.0536  -0.3099 0.0250  134 THR   K CB  
18914 O  OG1 . THR   K  133 ? 1.7271 0.4599 1.6771 0.0277  -0.3683 0.1025  134 THR   K OG1 
18915 C  CG2 . THR   K  133 ? 1.7221 0.6437 1.6401 0.0290  -0.3046 0.0138  134 THR   K CG2 
18916 N  N   . PHE   K  134 ? 1.7381 0.4923 1.4469 0.0950  -0.3118 -0.0251 135 PHE   K N   
18917 C  CA  . PHE   K  134 ? 1.7694 0.5689 1.4254 0.0974  -0.3321 -0.0718 135 PHE   K CA  
18918 C  C   . PHE   K  134 ? 1.7387 0.6068 1.3316 0.0659  -0.3311 -0.0823 135 PHE   K C   
18919 O  O   . PHE   K  134 ? 1.7480 0.5056 1.3380 0.0871  -0.2959 -0.1189 135 PHE   K O   
18920 C  CB  . PHE   K  134 ? 1.7641 0.6251 1.4845 0.0875  -0.3209 -0.0580 135 PHE   K CB  
18921 C  CG  . PHE   K  134 ? 1.7881 0.5917 1.6148 0.1214  -0.3065 -0.0182 135 PHE   K CG  
18922 C  CD1 . PHE   K  134 ? 1.7995 0.6012 1.6548 0.1084  -0.3039 -0.0506 135 PHE   K CD1 
18923 C  CD2 . PHE   K  134 ? 1.7966 0.6224 1.6015 0.1512  -0.2949 0.0158  135 PHE   K CD2 
18924 C  CE1 . PHE   K  134 ? 1.8302 0.6074 1.7327 0.1216  -0.2919 -0.0089 135 PHE   K CE1 
18925 C  CE2 . PHE   K  134 ? 1.7978 0.5747 1.6997 0.1511  -0.2892 0.0416  135 PHE   K CE2 
18926 C  CZ  . PHE   K  134 ? 1.8335 0.5841 1.7259 0.1344  -0.2804 0.0122  135 PHE   K CZ  
18927 N  N   . ALA   K  135 ? 1.7238 0.6187 1.3362 0.1206  -0.3171 -0.0721 136 ALA   K N   
18928 C  CA  . ALA   K  135 ? 1.6985 0.7425 1.2743 0.1255  -0.3656 -0.0311 136 ALA   K CA  
18929 C  C   . ALA   K  135 ? 1.7174 0.7310 1.1396 0.1354  -0.4359 -0.0230 136 ALA   K C   
18930 O  O   . ALA   K  135 ? 1.6810 0.6541 1.1478 0.1159  -0.4430 -0.0183 136 ALA   K O   
18931 C  CB  . ALA   K  135 ? 1.6926 0.6696 1.3210 0.1538  -0.3507 0.0161  136 ALA   K CB  
18932 N  N   . TYR   K  136 ? 1.7104 0.8151 1.2423 0.1021  -0.3989 -0.0370 137 TYR   K N   
18933 C  CA  . TYR   K  136 ? 1.7640 0.9122 1.2533 0.0491  -0.3788 -0.0378 137 TYR   K CA  
18934 C  C   . TYR   K  136 ? 1.7763 1.0316 1.2251 0.0234  -0.4259 -0.0694 137 TYR   K C   
18935 O  O   . TYR   K  136 ? 1.7590 1.0873 1.2813 0.0323  -0.4684 0.0384  137 TYR   K O   
18936 C  CB  . TYR   K  136 ? 1.7411 0.9274 1.3498 0.0236  -0.3745 -0.0914 137 TYR   K CB  
18937 C  CG  . TYR   K  136 ? 1.7698 0.8602 1.4281 0.0457  -0.3432 -0.0722 137 TYR   K CG  
18938 C  CD1 . TYR   K  136 ? 1.7660 0.8886 1.3556 0.0349  -0.3605 -0.0754 137 TYR   K CD1 
18939 C  CD2 . TYR   K  136 ? 1.7627 0.8263 1.4553 0.0307  -0.3487 -0.1319 137 TYR   K CD2 
18940 C  CE1 . TYR   K  136 ? 1.7661 0.8644 1.4034 0.0529  -0.3420 -0.0850 137 TYR   K CE1 
18941 C  CE2 . TYR   K  136 ? 1.7820 0.7959 1.4700 0.0429  -0.3177 -0.1299 137 TYR   K CE2 
18942 C  CZ  . TYR   K  136 ? 1.7668 0.8268 1.4172 0.0539  -0.3417 -0.1249 137 TYR   K CZ  
18943 O  OH  . TYR   K  136 ? 1.7551 0.7421 1.5420 0.0981  -0.2869 -0.1215 137 TYR   K OH  
18944 N  N   . GLY   K  137 ? 1.7948 0.9940 1.3623 -0.0008 -0.4045 -0.1214 138 GLY   K N   
18945 C  CA  . GLY   K  137 ? 1.8092 1.0983 1.3773 -0.0094 -0.4033 -0.1845 138 GLY   K CA  
18946 C  C   . GLY   K  137 ? 1.8500 1.1604 1.3320 -0.0116 -0.3973 -0.1756 138 GLY   K C   
18947 O  O   . GLY   K  137 ? 1.8423 1.2467 1.2702 0.0042  -0.4442 -0.1178 138 GLY   K O   
18948 N  N   . VAL   K  138 ? 1.8478 1.1031 1.3500 -0.0231 -0.4113 -0.1874 139 VAL   K N   
18949 C  CA  . VAL   K  138 ? 1.9035 1.0658 1.2714 -0.1023 -0.4345 -0.2251 139 VAL   K CA  
18950 C  C   . VAL   K  138 ? 1.9316 1.0569 1.2081 -0.1218 -0.4368 -0.2469 139 VAL   K C   
18951 O  O   . VAL   K  138 ? 1.8987 1.0495 1.2068 -0.1588 -0.4561 -0.2989 139 VAL   K O   
18952 C  CB  . VAL   K  138 ? 1.8702 1.0881 1.3050 -0.1148 -0.4597 -0.2531 139 VAL   K CB  
18953 C  CG1 . VAL   K  138 ? 1.8745 1.1302 1.2561 -0.1452 -0.4735 -0.2545 139 VAL   K CG1 
18954 C  CG2 . VAL   K  138 ? 1.8762 1.0899 1.3976 -0.1360 -0.4464 -0.2573 139 VAL   K CG2 
18955 N  N   . LEU   K  139 ? 1.9598 0.8817 1.2757 -0.1003 -0.4207 -0.1563 140 LEU   K N   
18956 C  CA  . LEU   K  139 ? 1.9950 0.9148 1.2525 -0.0408 -0.4609 -0.0914 140 LEU   K CA  
18957 C  C   . LEU   K  139 ? 2.0272 0.8253 1.1310 -0.0578 -0.4984 -0.0881 140 LEU   K C   
18958 O  O   . LEU   K  139 ? 2.0060 0.7420 1.1087 -0.0795 -0.5365 -0.1472 140 LEU   K O   
18959 C  CB  . LEU   K  139 ? 2.0134 0.7863 1.2394 -0.0268 -0.4485 -0.0352 140 LEU   K CB  
18960 C  CG  . LEU   K  139 ? 2.0358 0.8199 1.2037 -0.0008 -0.4668 0.0510  140 LEU   K CG  
18961 C  CD1 . LEU   K  139 ? 2.0667 0.8224 1.2196 -0.0009 -0.4823 0.0821  140 LEU   K CD1 
18962 C  CD2 . LEU   K  139 ? 2.0289 0.7552 1.1727 0.0268  -0.4574 0.0931  140 LEU   K CD2 
18963 N  N   . ASP   K  140 ? 1.9579 0.8875 1.2780 -0.0864 -0.4525 -0.1559 141 ASP   K N   
18964 C  CA  . ASP   K  140 ? 1.9836 0.9849 1.2961 -0.1939 -0.4278 -0.1795 141 ASP   K CA  
18965 C  C   . ASP   K  140 ? 1.9855 1.1800 1.1948 -0.1753 -0.4545 -0.1461 141 ASP   K C   
18966 O  O   . ASP   K  140 ? 1.9179 1.0650 1.2320 -0.2017 -0.5123 -0.0955 141 ASP   K O   
18967 C  CB  . ASP   K  140 ? 1.9337 0.9694 1.3784 -0.2167 -0.4332 -0.2250 141 ASP   K CB  
18968 C  CG  . ASP   K  140 ? 1.9432 0.9577 1.4241 -0.2476 -0.4420 -0.2197 141 ASP   K CG  
18969 O  OD1 . ASP   K  140 ? 2.0155 1.0147 1.3661 -0.2688 -0.4080 -0.1433 141 ASP   K OD1 
18970 O  OD2 . ASP   K  140 ? 1.8906 0.8285 1.5604 -0.2404 -0.5059 -0.1731 141 ASP   K OD2 
18971 N  N   . SER   K  141 ? 1.9731 1.2623 1.3766 -0.2433 -0.4437 -0.2269 142 SER   K N   
18972 C  CA  . SER   K  141 ? 2.0402 1.4625 1.4030 -0.2271 -0.3918 -0.3450 142 SER   K CA  
18973 C  C   . SER   K  141 ? 2.0617 1.5536 1.3313 -0.2936 -0.4275 -0.3720 142 SER   K C   
18974 O  O   . SER   K  141 ? 2.0587 1.7339 1.3091 -0.2853 -0.3883 -0.4500 142 SER   K O   
18975 C  CB  . SER   K  141 ? 2.0581 1.4615 1.5200 -0.2010 -0.3448 -0.3381 142 SER   K CB  
18976 O  OG  . SER   K  141 ? 2.0593 1.5132 1.6071 -0.1450 -0.3113 -0.2959 142 SER   K OG  
18977 N  N   . ASN   K  142 ? 2.0802 1.5137 1.3970 -0.2881 -0.4594 -0.2886 143 ASN   K N   
18978 C  CA  . ASN   K  142 ? 2.1335 1.6213 1.3295 -0.3569 -0.5313 -0.2762 143 ASN   K CA  
18979 C  C   . ASN   K  142 ? 2.1638 1.6640 1.2776 -0.3017 -0.5561 -0.1417 143 ASN   K C   
18980 O  O   . ASN   K  142 ? 2.0420 1.6459 1.2526 -0.4277 -0.6570 -0.2595 143 ASN   K O   
18981 C  CB  . ASN   K  142 ? 2.1002 1.7261 1.3637 -0.3176 -0.5443 -0.2939 143 ASN   K CB  
18982 C  CG  . ASN   K  142 ? 2.1522 1.7709 1.4598 -0.3518 -0.5372 -0.3987 143 ASN   K CG  
18983 O  OD1 . ASN   K  142 ? 2.1692 1.8869 1.4446 -0.3760 -0.5082 -0.3945 143 ASN   K OD1 
18984 N  ND2 . ASN   K  142 ? 2.1882 1.9122 1.4085 -0.3422 -0.5552 -0.3629 143 ASN   K ND2 
18985 N  N   . TYR   K  143 ? 2.1587 1.6191 1.4189 -0.3938 -0.4634 -0.1263 144 TYR   K N   
18986 C  CA  . TYR   K  143 ? 2.2748 1.6100 1.4246 -0.2919 -0.4286 -0.0045 144 TYR   K CA  
18987 C  C   . TYR   K  143 ? 2.3091 1.7560 1.4498 -0.2615 -0.4243 0.0730  144 TYR   K C   
18988 O  O   . TYR   K  143 ? 2.3696 1.8728 1.4909 -0.1421 -0.3819 0.1981  144 TYR   K O   
18989 C  CB  . TYR   K  143 ? 2.3151 1.4555 1.3924 -0.3056 -0.3825 -0.0310 144 TYR   K CB  
18990 C  CG  . TYR   K  143 ? 2.3676 1.4363 1.3446 -0.2609 -0.4006 0.0536  144 TYR   K CG  
18991 C  CD1 . TYR   K  143 ? 2.3845 1.3260 1.2458 -0.2473 -0.4452 0.1369  144 TYR   K CD1 
18992 C  CD2 . TYR   K  143 ? 2.3938 1.3890 1.3402 -0.2675 -0.3973 0.0708  144 TYR   K CD2 
18993 C  CE1 . TYR   K  143 ? 2.3885 1.3096 1.1817 -0.2110 -0.4987 0.1314  144 TYR   K CE1 
18994 C  CE2 . TYR   K  143 ? 2.4102 1.3762 1.2377 -0.2295 -0.4337 0.1055  144 TYR   K CE2 
18995 C  CZ  . TYR   K  143 ? 2.4162 1.2584 1.1747 -0.2414 -0.5028 0.1330  144 TYR   K CZ  
18996 O  OH  . TYR   K  143 ? 2.3948 1.2489 1.0027 -0.2132 -0.5815 0.1845  144 TYR   K OH  
18997 N  N   . LYS   K  144 ? 2.2625 1.7809 1.5500 -0.2724 -0.4534 0.0899  145 LYS   K N   
18998 C  CA  . LYS   K  144 ? 2.2879 1.7211 1.6050 -0.4294 -0.4029 0.0071  145 LYS   K CA  
18999 C  C   . LYS   K  144 ? 2.2923 1.6329 1.5669 -0.4973 -0.4747 0.1003  145 LYS   K C   
19000 O  O   . LYS   K  144 ? 2.2459 1.2577 1.5112 -0.5959 -0.4923 0.1669  145 LYS   K O   
19001 C  CB  . LYS   K  144 ? 2.3286 1.8853 1.6163 -0.4737 -0.3678 -0.0755 145 LYS   K CB  
19002 C  CG  . LYS   K  144 ? 2.3427 1.9546 1.6463 -0.5077 -0.3212 -0.2160 145 LYS   K CG  
19003 C  CD  . LYS   K  144 ? 2.3958 1.9997 1.6768 -0.5643 -0.3056 -0.2744 145 LYS   K CD  
19004 C  CE  . LYS   K  144 ? 2.3944 2.0068 1.7036 -0.6116 -0.2801 -0.3187 145 LYS   K CE  
19005 N  NZ  . LYS   K  144 ? 2.4087 2.0483 1.7245 -0.6588 -0.2840 -0.3092 145 LYS   K NZ  
19006 N  N   . TRP   K  145 ? 2.2943 1.6539 1.5513 -0.5130 -0.5036 0.1082  146 TRP   K N   
19007 C  CA  . TRP   K  145 ? 2.3329 1.6654 1.5174 -0.4803 -0.5576 0.1183  146 TRP   K CA  
19008 C  C   . TRP   K  145 ? 2.3409 1.6787 1.5713 -0.4850 -0.5824 0.1270  146 TRP   K C   
19009 O  O   . TRP   K  145 ? 2.2824 1.5553 1.4956 -0.5451 -0.6562 0.1213  146 TRP   K O   
19010 C  CB  . TRP   K  145 ? 2.3985 1.7066 1.4626 -0.5013 -0.5274 0.1331  146 TRP   K CB  
19011 C  CG  . TRP   K  145 ? 2.4681 1.7250 1.4091 -0.4488 -0.5537 0.1654  146 TRP   K CG  
19012 C  CD1 . TRP   K  145 ? 2.5266 1.7921 1.3974 -0.4484 -0.5819 0.1811  146 TRP   K CD1 
19013 C  CD2 . TRP   K  145 ? 2.4886 1.7007 1.4204 -0.3998 -0.4982 0.1550  146 TRP   K CD2 
19014 N  NE1 . TRP   K  145 ? 2.5102 1.7361 1.3670 -0.4252 -0.6058 0.2663  146 TRP   K NE1 
19015 C  CE2 . TRP   K  145 ? 2.4941 1.7256 1.3456 -0.4179 -0.5567 0.2168  146 TRP   K CE2 
19016 C  CE3 . TRP   K  145 ? 2.4598 1.7068 1.4118 -0.3745 -0.4627 0.1584  146 TRP   K CE3 
19017 C  CZ2 . TRP   K  145 ? 2.4821 1.5565 1.4508 -0.3877 -0.5062 0.2668  146 TRP   K CZ2 
19018 C  CZ3 . TRP   K  145 ? 2.4160 1.6156 1.4487 -0.3732 -0.4688 0.1910  146 TRP   K CZ3 
19019 C  CH2 . TRP   K  145 ? 2.4261 1.5814 1.4236 -0.4043 -0.4954 0.1836  146 TRP   K CH2 
19020 N  N   . ASP   K  146 ? 2.4040 1.7652 1.5604 -0.5019 -0.6076 0.1304  147 ASP   K N   
19021 C  CA  . ASP   K  146 ? 2.4716 1.7445 1.5300 -0.4822 -0.5960 0.2253  147 ASP   K CA  
19022 C  C   . ASP   K  146 ? 2.3567 1.7365 1.4976 -0.4058 -0.6940 0.2636  147 ASP   K C   
19023 O  O   . ASP   K  146 ? 2.4427 1.6656 1.4894 -0.3329 -0.7153 0.4341  147 ASP   K O   
19024 C  CB  . ASP   K  146 ? 2.5457 1.7930 1.5392 -0.5339 -0.5599 0.2131  147 ASP   K CB  
19025 C  CG  . ASP   K  146 ? 2.6137 1.7705 1.5916 -0.5712 -0.4865 0.1799  147 ASP   K CG  
19026 O  OD1 . ASP   K  146 ? 2.6264 1.7642 1.6530 -0.5599 -0.5231 0.1307  147 ASP   K OD1 
19027 O  OD2 . ASP   K  146 ? 2.6902 1.7384 1.6614 -0.5890 -0.3772 0.1592  147 ASP   K OD2 
19028 N  N   . LEU   K  147 ? 2.3316 1.7355 1.4961 -0.3933 -0.5849 0.2396  148 LEU   K N   
19029 C  CA  . LEU   K  147 ? 2.2622 1.6628 1.4405 -0.2727 -0.5881 0.2466  148 LEU   K CA  
19030 C  C   . LEU   K  147 ? 2.3204 1.5135 1.2836 -0.3146 -0.6411 0.3104  148 LEU   K C   
19031 O  O   . LEU   K  147 ? 2.2533 1.3725 1.1093 -0.2051 -0.6759 0.4574  148 LEU   K O   
19032 C  CB  . LEU   K  147 ? 2.2606 1.7333 1.4056 -0.2470 -0.5762 0.2068  148 LEU   K CB  
19033 C  CG  . LEU   K  147 ? 2.3157 1.7391 1.5085 -0.2524 -0.5269 0.1714  148 LEU   K CG  
19034 C  CD1 . LEU   K  147 ? 2.3384 1.9113 1.5373 -0.2728 -0.4875 0.1384  148 LEU   K CD1 
19035 C  CD2 . LEU   K  147 ? 2.2932 1.7919 1.4338 -0.2615 -0.4622 0.0674  148 LEU   K CD2 
19036 N  N   . SER   K  148 ? 2.2618 1.5856 1.2463 -0.1744 -0.6816 0.3692  149 SER   K N   
19037 C  CA  . SER   K  148 ? 2.3124 1.5589 1.2881 -0.1430 -0.7048 0.3963  149 SER   K CA  
19038 C  C   . SER   K  148 ? 2.2442 1.4844 1.3456 -0.0874 -0.6798 0.2926  149 SER   K C   
19039 O  O   . SER   K  148 ? 2.2318 1.5247 1.3192 -0.0207 -0.6814 0.2540  149 SER   K O   
19040 C  CB  . SER   K  148 ? 2.3102 1.6662 1.3439 -0.1552 -0.7135 0.3721  149 SER   K CB  
19041 O  OG  . SER   K  148 ? 2.2372 1.7031 1.3066 -0.1853 -0.6947 0.3534  149 SER   K OG  
19042 N  N   . VAL   K  149 ? 2.2412 1.3906 1.3618 -0.0708 -0.7717 0.4250  150 VAL   K N   
19043 C  CA  . VAL   K  149 ? 2.1877 1.3686 1.4382 -0.0222 -0.7265 0.3891  150 VAL   K CA  
19044 C  C   . VAL   K  149 ? 2.1643 1.4017 1.5224 -0.0969 -0.6989 0.2908  150 VAL   K C   
19045 O  O   . VAL   K  149 ? 2.1993 1.5278 1.4392 -0.1364 -0.5841 0.2280  150 VAL   K O   
19046 C  CB  . VAL   K  149 ? 2.1960 1.3989 1.5241 0.0044  -0.7423 0.4419  150 VAL   K CB  
19047 C  CG1 . VAL   K  149 ? 2.1556 1.3593 1.5528 0.0666  -0.7377 0.4723  150 VAL   K CG1 
19048 C  CG2 . VAL   K  149 ? 2.1911 1.4297 1.5422 -0.0155 -0.7437 0.4419  150 VAL   K CG2 
19049 N  N   . GLU   K  150 ? 2.1569 1.4378 1.6000 -0.1460 -0.7118 0.2836  151 GLU   K N   
19050 C  CA  . GLU   K  150 ? 2.1157 1.4289 1.6369 -0.1497 -0.6993 0.2422  151 GLU   K CA  
19051 C  C   . GLU   K  150 ? 2.1047 1.2869 1.6076 -0.2348 -0.6670 0.2248  151 GLU   K C   
19052 O  O   . GLU   K  150 ? 2.0544 1.1630 1.5695 -0.2021 -0.6459 0.1550  151 GLU   K O   
19053 C  CB  . GLU   K  150 ? 2.1223 1.5032 1.6589 -0.1679 -0.7137 0.2512  151 GLU   K CB  
19054 C  CG  . GLU   K  150 ? 2.0965 1.5333 1.6889 -0.1467 -0.6784 0.2508  151 GLU   K CG  
19055 C  CD  . GLU   K  150 ? 2.1452 1.6448 1.6813 -0.1529 -0.6926 0.2397  151 GLU   K CD  
19056 O  OE1 . GLU   K  150 ? 2.1197 1.7041 1.7283 -0.1121 -0.7128 0.2398  151 GLU   K OE1 
19057 O  OE2 . GLU   K  150 ? 2.2087 1.7071 1.6489 -0.1929 -0.6997 0.2273  151 GLU   K OE2 
19058 N  N   . ASP   K  151 ? 2.0904 1.3394 1.6220 -0.3020 -0.6556 0.2000  152 ASP   K N   
19059 C  CA  . ASP   K  151 ? 2.0054 1.4208 1.5767 -0.2827 -0.6650 0.1457  152 ASP   K CA  
19060 C  C   . ASP   K  151 ? 1.9517 1.3570 1.6130 -0.2703 -0.6633 0.0907  152 ASP   K C   
19061 O  O   . ASP   K  151 ? 1.9255 1.3833 1.6416 -0.2302 -0.6603 0.1019  152 ASP   K O   
19062 C  CB  . ASP   K  151 ? 2.0473 1.5540 1.5648 -0.3698 -0.6351 0.1423  152 ASP   K CB  
19063 C  CG  . ASP   K  151 ? 2.0840 1.6531 1.5292 -0.4076 -0.6459 0.1747  152 ASP   K CG  
19064 O  OD1 . ASP   K  151 ? 2.0493 1.7383 1.5810 -0.4449 -0.7153 0.1058  152 ASP   K OD1 
19065 O  OD2 . ASP   K  151 ? 2.1053 1.6561 1.4634 -0.4421 -0.7470 0.2544  152 ASP   K OD2 
19066 N  N   . ALA   K  152 ? 1.9151 1.2629 1.5046 -0.1816 -0.7176 0.1515  153 ALA   K N   
19067 C  CA  . ALA   K  152 ? 1.8672 1.1448 1.4937 -0.1617 -0.6719 0.1014  153 ALA   K CA  
19068 C  C   . ALA   K  152 ? 1.8127 1.1279 1.5257 -0.1328 -0.6329 0.0210  153 ALA   K C   
19069 O  O   . ALA   K  152 ? 1.8178 1.2015 1.4378 -0.1872 -0.6120 0.0140  153 ALA   K O   
19070 C  CB  . ALA   K  152 ? 1.8829 1.1016 1.4532 -0.1029 -0.7117 0.1423  153 ALA   K CB  
19071 N  N   . LEU   K  153 ? 1.8504 1.0418 1.4763 -0.0833 -0.6665 0.0273  154 LEU   K N   
19072 C  CA  . LEU   K  153 ? 1.8542 1.0186 1.4595 -0.0488 -0.6706 0.0307  154 LEU   K CA  
19073 C  C   . LEU   K  153 ? 1.8757 1.0150 1.3981 -0.0520 -0.6396 0.0137  154 LEU   K C   
19074 O  O   . LEU   K  153 ? 1.9372 0.9940 1.3416 -0.0550 -0.5175 -0.0253 154 LEU   K O   
19075 C  CB  . LEU   K  153 ? 1.8559 1.0713 1.5373 -0.0483 -0.7020 0.0428  154 LEU   K CB  
19076 C  CG  . LEU   K  153 ? 1.8721 1.0700 1.5742 -0.0564 -0.7050 0.0452  154 LEU   K CG  
19077 C  CD1 . LEU   K  153 ? 1.9105 1.1033 1.6436 -0.0331 -0.7328 0.0605  154 LEU   K CD1 
19078 C  CD2 . LEU   K  153 ? 1.7979 1.0062 1.5651 -0.0269 -0.6932 0.0692  154 LEU   K CD2 
19079 N  N   . TYR   K  154 ? 1.8904 0.9887 1.3812 -0.0794 -0.6945 0.0627  155 TYR   K N   
19080 C  CA  . TYR   K  154 ? 1.8853 0.9789 1.4074 -0.0663 -0.6964 0.0499  155 TYR   K CA  
19081 C  C   . TYR   K  154 ? 1.8815 0.8705 1.4302 -0.0357 -0.6635 -0.0223 155 TYR   K C   
19082 O  O   . TYR   K  154 ? 1.8686 0.8687 1.4008 0.0508  -0.6674 -0.0429 155 TYR   K O   
19083 C  CB  . TYR   K  154 ? 1.8753 1.0446 1.3947 -0.1039 -0.7470 0.0953  155 TYR   K CB  
19084 C  CG  . TYR   K  154 ? 1.8471 1.0626 1.4211 -0.1466 -0.7504 0.0985  155 TYR   K CG  
19085 C  CD1 . TYR   K  154 ? 1.8298 1.0489 1.4670 -0.1374 -0.7488 0.1044  155 TYR   K CD1 
19086 C  CD2 . TYR   K  154 ? 1.8497 1.0503 1.4240 -0.1851 -0.7299 0.0633  155 TYR   K CD2 
19087 C  CE1 . TYR   K  154 ? 1.8500 1.0534 1.5280 -0.1638 -0.7056 0.0722  155 TYR   K CE1 
19088 C  CE2 . TYR   K  154 ? 1.8886 1.0463 1.4917 -0.2022 -0.6898 0.0126  155 TYR   K CE2 
19089 C  CZ  . TYR   K  154 ? 1.8902 1.0926 1.5484 -0.1816 -0.6589 0.0140  155 TYR   K CZ  
19090 O  OH  . TYR   K  154 ? 1.9582 1.1022 1.6359 -0.2361 -0.5911 -0.0503 155 TYR   K OH  
19091 N  N   . LEU   K  155 ? 1.9235 0.8065 1.4217 -0.0834 -0.6462 -0.0403 156 LEU   K N   
19092 C  CA  . LEU   K  155 ? 1.8837 0.8727 1.4358 -0.0951 -0.6181 -0.0505 156 LEU   K CA  
19093 C  C   . LEU   K  155 ? 1.8836 0.7899 1.4519 -0.0962 -0.5885 -0.1171 156 LEU   K C   
19094 O  O   . LEU   K  155 ? 1.9224 0.9299 1.3563 -0.0702 -0.5980 -0.0914 156 LEU   K O   
19095 C  CB  . LEU   K  155 ? 1.9554 0.9287 1.4508 -0.1514 -0.6005 -0.0275 156 LEU   K CB  
19096 C  CG  . LEU   K  155 ? 1.9079 1.0539 1.5251 -0.1716 -0.5504 -0.0344 156 LEU   K CG  
19097 C  CD1 . LEU   K  155 ? 1.9610 1.0586 1.6130 -0.1898 -0.5082 -0.0866 156 LEU   K CD1 
19098 C  CD2 . LEU   K  155 ? 1.9434 1.0655 1.5188 -0.2097 -0.5630 -0.0092 156 LEU   K CD2 
19099 N  N   . GLY   K  156 ? 1.8476 0.7427 1.4078 -0.0749 -0.6225 -0.0356 157 GLY   K N   
19100 C  CA  . GLY   K  156 ? 1.8556 0.6919 1.3918 -0.0419 -0.5756 -0.0190 157 GLY   K CA  
19101 C  C   . GLY   K  156 ? 1.8254 0.5955 1.4534 -0.0273 -0.5830 -0.0128 157 GLY   K C   
19102 O  O   . GLY   K  156 ? 1.9334 0.4714 1.4923 0.0291  -0.5389 0.0414  157 GLY   K O   
19103 N  N   . LYS   K  157 ? 1.8338 0.6206 1.4090 -0.0224 -0.6171 0.0141  158 LYS   K N   
19104 C  CA  . LYS   K  157 ? 1.8172 0.7296 1.4129 -0.0292 -0.6130 0.0446  158 LYS   K CA  
19105 C  C   . LYS   K  157 ? 1.8175 0.7357 1.3752 -0.0265 -0.5550 0.0295  158 LYS   K C   
19106 O  O   . LYS   K  157 ? 1.8204 0.8625 1.3961 -0.0293 -0.5006 0.0739  158 LYS   K O   
19107 C  CB  . LYS   K  157 ? 1.8519 0.7156 1.4516 -0.0203 -0.6548 0.0742  158 LYS   K CB  
19108 C  CG  . LYS   K  157 ? 1.8291 0.6857 1.4930 -0.0287 -0.6748 0.0924  158 LYS   K CG  
19109 C  CD  . LYS   K  157 ? 1.8558 0.7958 1.5491 -0.0529 -0.7052 0.0765  158 LYS   K CD  
19110 C  CE  . LYS   K  157 ? 1.8698 0.8522 1.6171 -0.0165 -0.7438 0.0793  158 LYS   K CE  
19111 N  NZ  . LYS   K  157 ? 1.8990 0.9835 1.6685 -0.0314 -0.7747 0.0591  158 LYS   K NZ  
19112 N  N   . ARG   K  158 ? 1.8621 0.8092 1.3500 -0.0807 -0.5468 0.0132  159 ARG   K N   
19113 C  CA  . ARG   K  158 ? 1.8803 0.8004 1.3634 -0.0999 -0.5494 -0.0090 159 ARG   K CA  
19114 C  C   . ARG   K  158 ? 1.8411 0.8174 1.3254 -0.1016 -0.5302 -0.0833 159 ARG   K C   
19115 O  O   . ARG   K  158 ? 1.8784 0.8273 1.3106 -0.0976 -0.5240 -0.0927 159 ARG   K O   
19116 C  CB  . ARG   K  158 ? 1.9535 0.8801 1.3624 -0.1327 -0.5428 -0.0114 159 ARG   K CB  
19117 C  CG  . ARG   K  158 ? 1.9936 0.9214 1.4322 -0.1240 -0.5218 -0.0942 159 ARG   K CG  
19118 C  CD  . ARG   K  158 ? 1.9816 0.9691 1.5103 -0.1610 -0.5292 -0.1285 159 ARG   K CD  
19119 N  NE  . ARG   K  158 ? 2.0261 0.9722 1.5483 -0.1683 -0.5274 -0.1631 159 ARG   K NE  
19120 C  CZ  . ARG   K  158 ? 2.0484 0.9486 1.5752 -0.1161 -0.4963 -0.1754 159 ARG   K CZ  
19121 N  NH1 . ARG   K  158 ? 2.0450 0.9172 1.5908 -0.1731 -0.5155 -0.1101 159 ARG   K NH1 
19122 N  NH2 . ARG   K  158 ? 2.0663 1.0120 1.5758 -0.0587 -0.4478 -0.2850 159 ARG   K NH2 
19123 N  N   . SER   K  159 ? 1.8237 0.6947 1.2318 -0.0424 -0.5400 -0.0266 160 SER   K N   
19124 C  CA  . SER   K  159 ? 1.8074 0.6635 1.1903 -0.0325 -0.5135 -0.0479 160 SER   K CA  
19125 C  C   . SER   K  159 ? 1.7986 0.6073 1.1830 -0.0366 -0.5202 -0.0549 160 SER   K C   
19126 O  O   . SER   K  159 ? 1.8349 0.5409 1.0358 -0.0455 -0.5140 -0.1205 160 SER   K O   
19127 C  CB  . SER   K  159 ? 1.7820 0.6795 1.1701 -0.0197 -0.5183 -0.0279 160 SER   K CB  
19128 O  OG  . SER   K  159 ? 1.7616 0.7326 1.1509 0.0011  -0.5691 0.0048  160 SER   K OG  
19129 N  N   . ILE   K  160 ? 1.7462 0.6564 1.1565 -0.0267 -0.5202 -0.0065 161 ILE   K N   
19130 C  CA  . ILE   K  160 ? 1.7134 0.6784 1.1722 -0.0328 -0.5024 0.0304  161 ILE   K CA  
19131 C  C   . ILE   K  160 ? 1.7320 0.6858 1.2332 -0.0573 -0.4881 0.0015  161 ILE   K C   
19132 O  O   . ILE   K  160 ? 1.7458 0.7321 1.2098 -0.0688 -0.4421 0.0278  161 ILE   K O   
19133 C  CB  . ILE   K  160 ? 1.6853 0.6906 1.1685 -0.0248 -0.5179 0.0418  161 ILE   K CB  
19134 C  CG1 . ILE   K  160 ? 1.6699 0.7059 1.1685 -0.0333 -0.5033 0.0577  161 ILE   K CG1 
19135 C  CG2 . ILE   K  160 ? 1.6722 0.6699 1.1927 -0.0273 -0.4968 0.0332  161 ILE   K CG2 
19136 C  CD1 . ILE   K  160 ? 1.6232 0.7093 1.1904 -0.0455 -0.4867 0.0717  161 ILE   K CD1 
19137 N  N   . LEU   K  161 ? 1.7493 0.6733 1.2586 -0.0476 -0.5267 0.0411  162 LEU   K N   
19138 C  CA  . LEU   K  161 ? 1.7611 0.6642 1.3578 -0.0399 -0.5108 0.0585  162 LEU   K CA  
19139 C  C   . LEU   K  161 ? 1.7664 0.5996 1.4196 -0.0660 -0.4630 0.0008  162 LEU   K C   
19140 O  O   . LEU   K  161 ? 1.7878 0.4371 1.5998 -0.0271 -0.4123 -0.0082 162 LEU   K O   
19141 C  CB  . LEU   K  161 ? 1.8062 0.7229 1.3728 -0.0710 -0.5339 0.0646  162 LEU   K CB  
19142 C  CG  . LEU   K  161 ? 1.8665 0.6463 1.4000 -0.0354 -0.5372 0.0509  162 LEU   K CG  
19143 C  CD1 . LEU   K  161 ? 1.8590 0.6155 1.4185 -0.0317 -0.5327 0.0888  162 LEU   K CD1 
19144 C  CD2 . LEU   K  161 ? 1.9034 0.6555 1.3882 -0.0474 -0.5452 0.0303  162 LEU   K CD2 
19145 N  N   . ALA   K  162 ? 1.7595 0.4976 1.3596 -0.0636 -0.4819 -0.0326 163 ALA   K N   
19146 C  CA  . ALA   K  162 ? 1.7196 0.5332 1.3671 -0.0722 -0.4588 -0.0614 163 ALA   K CA  
19147 C  C   . ALA   K  162 ? 1.6911 0.5537 1.4054 -0.0200 -0.4639 0.0093  163 ALA   K C   
19148 O  O   . ALA   K  162 ? 1.6597 0.5994 1.4237 0.0543  -0.5004 0.0468  163 ALA   K O   
19149 C  CB  . ALA   K  162 ? 1.7218 0.5165 1.3329 -0.1043 -0.4679 -0.1058 163 ALA   K CB  
19150 N  N   . ALA   K  163 ? 1.6932 0.5190 1.4085 -0.0192 -0.4504 0.0397  164 ALA   K N   
19151 C  CA  . ALA   K  163 ? 1.7088 0.5253 1.3950 0.0137  -0.4393 0.0944  164 ALA   K CA  
19152 C  C   . ALA   K  163 ? 1.7204 0.5292 1.4780 0.0150  -0.3981 0.1054  164 ALA   K C   
19153 O  O   . ALA   K  163 ? 1.7813 0.4867 1.5495 0.0460  -0.3922 0.1053  164 ALA   K O   
19154 C  CB  . ALA   K  163 ? 1.6996 0.5390 1.3818 -0.0084 -0.4157 0.1202  164 ALA   K CB  
19155 N  N   . ALA   K  164 ? 1.7279 0.5497 1.4638 0.0300  -0.4374 0.1913  165 ALA   K N   
19156 C  CA  . ALA   K  164 ? 1.7256 0.5535 1.5145 -0.0132 -0.4366 0.2476  165 ALA   K CA  
19157 C  C   . ALA   K  164 ? 1.7087 0.5603 1.5370 -0.0667 -0.4151 0.1872  165 ALA   K C   
19158 O  O   . ALA   K  164 ? 1.7108 0.5439 1.6171 -0.0984 -0.3083 0.2268  165 ALA   K O   
19159 C  CB  . ALA   K  164 ? 1.7225 0.5921 1.4851 -0.0319 -0.4738 0.2507  165 ALA   K CB  
19160 N  N   . HIS   K  165 ? 1.6862 0.5960 1.4590 -0.0987 -0.4671 0.2229  166 HIS   K N   
19161 C  CA  . HIS   K  165 ? 1.7249 0.6019 1.5169 -0.1200 -0.4564 0.2244  166 HIS   K CA  
19162 C  C   . HIS   K  165 ? 1.6430 0.6167 1.5607 -0.1463 -0.4570 0.1711  166 HIS   K C   
19163 O  O   . HIS   K  165 ? 1.6451 0.5644 1.6468 -0.1705 -0.4610 0.1794  166 HIS   K O   
19164 C  CB  . HIS   K  165 ? 1.7991 0.6275 1.4865 -0.0734 -0.4619 0.2785  166 HIS   K CB  
19165 C  CG  . HIS   K  165 ? 1.8803 0.6198 1.5489 -0.0255 -0.4403 0.3042  166 HIS   K CG  
19166 N  ND1 . HIS   K  165 ? 1.9317 0.6024 1.6415 -0.0169 -0.4248 0.3274  166 HIS   K ND1 
19167 C  CD2 . HIS   K  165 ? 1.9289 0.6454 1.5657 -0.0171 -0.4208 0.2887  166 HIS   K CD2 
19168 C  CE1 . HIS   K  165 ? 1.9632 0.6004 1.6437 -0.0360 -0.3994 0.2974  166 HIS   K CE1 
19169 N  NE2 . HIS   K  165 ? 1.9722 0.6225 1.6013 -0.0314 -0.4187 0.2681  166 HIS   K NE2 
19170 N  N   . ARG   K  166 ? 1.6469 0.6188 1.5498 -0.1461 -0.4360 0.1254  167 ARG   K N   
19171 C  CA  . ARG   K  166 ? 1.6391 0.5994 1.5542 -0.1311 -0.4199 0.0792  167 ARG   K CA  
19172 C  C   . ARG   K  166 ? 1.6249 0.6420 1.5865 -0.1160 -0.4688 0.0787  167 ARG   K C   
19173 O  O   . ARG   K  166 ? 1.5656 0.6499 1.6148 -0.1052 -0.5314 0.0694  167 ARG   K O   
19174 C  CB  . ARG   K  166 ? 1.6418 0.5637 1.5376 -0.1218 -0.4144 0.0362  167 ARG   K CB  
19175 C  CG  . ARG   K  166 ? 1.6377 0.5552 1.5661 -0.1484 -0.3945 0.0199  167 ARG   K CG  
19176 C  CD  . ARG   K  166 ? 1.6365 0.5255 1.5961 -0.1727 -0.4015 -0.0245 167 ARG   K CD  
19177 N  NE  . ARG   K  166 ? 1.6350 0.5370 1.6357 -0.1912 -0.4068 -0.0579 167 ARG   K NE  
19178 C  CZ  . ARG   K  166 ? 1.6450 0.5246 1.6830 -0.2087 -0.3903 -0.1501 167 ARG   K CZ  
19179 N  NH1 . ARG   K  166 ? 1.6450 0.4092 1.7103 -0.1940 -0.3954 -0.1722 167 ARG   K NH1 
19180 N  NH2 . ARG   K  166 ? 1.6481 0.4984 1.7014 -0.2073 -0.3794 -0.1595 167 ARG   K NH2 
19181 N  N   . ASP   K  167 ? 1.6458 0.6279 1.5369 -0.1032 -0.4770 0.1027  168 ASP   K N   
19182 C  CA  . ASP   K  167 ? 1.6963 0.6430 1.5163 -0.0900 -0.4669 0.1030  168 ASP   K CA  
19183 C  C   . ASP   K  167 ? 1.6785 0.5799 1.5024 -0.0896 -0.4841 0.0911  168 ASP   K C   
19184 O  O   . ASP   K  167 ? 1.6621 0.5057 1.5257 -0.1169 -0.4733 0.0825  168 ASP   K O   
19185 C  CB  . ASP   K  167 ? 1.7202 0.6953 1.4897 -0.1427 -0.4472 0.1476  168 ASP   K CB  
19186 C  CG  . ASP   K  167 ? 1.7518 0.7114 1.4634 -0.1575 -0.4599 0.1860  168 ASP   K CG  
19187 O  OD1 . ASP   K  167 ? 1.7931 0.8801 1.5153 -0.1796 -0.4677 0.2933  168 ASP   K OD1 
19188 O  OD2 . ASP   K  167 ? 1.7489 0.6992 1.4410 -0.1405 -0.4340 0.1763  168 ASP   K OD2 
19189 N  N   . ALA   K  168 ? 1.6924 0.6352 1.4768 -0.0511 -0.5150 0.0616  169 ALA   K N   
19190 C  CA  . ALA   K  168 ? 1.7023 0.6849 1.4785 -0.0383 -0.5094 0.0651  169 ALA   K CA  
19191 C  C   . ALA   K  168 ? 1.7076 0.7000 1.4680 0.0326  -0.4969 0.0944  169 ALA   K C   
19192 O  O   . ALA   K  168 ? 1.6832 0.8221 1.4487 0.1260  -0.5381 0.1618  169 ALA   K O   
19193 C  CB  . ALA   K  168 ? 1.7133 0.6826 1.5201 -0.0512 -0.5065 0.0937  169 ALA   K CB  
19194 N  N   . TYR   K  169 ? 1.7564 0.5915 1.4588 0.0613  -0.4783 0.0402  170 TYR   K N   
19195 C  CA  . TYR   K  169 ? 1.7763 0.5791 1.4586 0.0244  -0.4949 0.0330  170 TYR   K CA  
19196 C  C   . TYR   K  169 ? 1.7508 0.5624 1.3543 0.0007  -0.5123 -0.0224 170 TYR   K C   
19197 O  O   . TYR   K  169 ? 1.7918 0.5943 1.3398 0.1352  -0.4936 0.0090  170 TYR   K O   
19198 C  CB  . TYR   K  169 ? 1.7918 0.5762 1.4163 0.0707  -0.5222 0.0197  170 TYR   K CB  
19199 C  CG  . TYR   K  169 ? 1.8052 0.6143 1.4139 0.1092  -0.5197 0.0170  170 TYR   K CG  
19200 C  CD1 . TYR   K  169 ? 1.8288 0.6847 1.4532 0.0749  -0.5077 0.0393  170 TYR   K CD1 
19201 C  CD2 . TYR   K  169 ? 1.8293 0.6396 1.4119 0.1442  -0.4987 -0.0120 170 TYR   K CD2 
19202 C  CE1 . TYR   K  169 ? 1.8204 0.6801 1.5406 0.1174  -0.4898 0.0550  170 TYR   K CE1 
19203 C  CE2 . TYR   K  169 ? 1.7959 0.6741 1.4805 0.1864  -0.4902 0.0120  170 TYR   K CE2 
19204 C  CZ  . TYR   K  169 ? 1.8325 0.6814 1.5380 0.1433  -0.4901 0.0480  170 TYR   K CZ  
19205 O  OH  . TYR   K  169 ? 1.8113 0.7441 1.5560 0.1410  -0.5481 0.0557  170 TYR   K OH  
19206 N  N   . SER   K  170 ? 1.7042 0.4027 1.3932 -0.0448 -0.4754 -0.0882 171 SER   K N   
19207 C  CA  . SER   K  170 ? 1.6817 0.3893 1.3325 -0.0510 -0.4501 -0.1131 171 SER   K CA  
19208 C  C   . SER   K  170 ? 1.6690 0.4502 1.3236 -0.0390 -0.4609 -0.1246 171 SER   K C   
19209 O  O   . SER   K  170 ? 1.6654 0.4480 1.3026 -0.0421 -0.4526 -0.1637 171 SER   K O   
19210 C  CB  . SER   K  170 ? 1.7258 0.3601 1.3066 -0.0491 -0.4562 -0.1602 171 SER   K CB  
19211 O  OG  . SER   K  170 ? 1.7164 0.3342 1.3183 -0.0322 -0.4251 -0.1787 171 SER   K OG  
19212 N  N   . GLY   K  171 ? 1.6519 0.4751 1.3074 -0.0512 -0.4773 -0.0984 172 GLY   K N   
19213 C  CA  . GLY   K  171 ? 1.6614 0.5761 1.3605 -0.0751 -0.4758 -0.1044 172 GLY   K CA  
19214 C  C   . GLY   K  171 ? 1.6293 0.7058 1.4051 -0.0251 -0.4695 -0.1090 172 GLY   K C   
19215 O  O   . GLY   K  171 ? 1.6179 0.7644 1.4971 -0.0877 -0.4720 -0.0836 172 GLY   K O   
19216 N  N   . GLY   K  172 ? 1.6193 0.7194 1.4196 -0.0528 -0.5103 -0.1240 173 GLY   K N   
19217 C  CA  . GLY   K  172 ? 1.5757 0.7429 1.3810 -0.0491 -0.5594 -0.1045 173 GLY   K CA  
19218 C  C   . GLY   K  172 ? 1.5383 0.7351 1.3817 -0.0732 -0.6103 -0.1649 173 GLY   K C   
19219 O  O   . GLY   K  172 ? 1.5428 0.6359 1.3231 -0.0165 -0.6319 -0.1511 173 GLY   K O   
19220 N  N   . SER   K  173 ? 1.5639 0.7653 1.3683 -0.0493 -0.6191 -0.1128 174 SER   K N   
19221 C  CA  . SER   K  173 ? 1.5883 0.8119 1.3647 -0.0521 -0.6415 -0.1214 174 SER   K CA  
19222 C  C   . SER   K  173 ? 1.5986 0.8273 1.3732 -0.0288 -0.6111 -0.1070 174 SER   K C   
19223 O  O   . SER   K  173 ? 1.5251 0.7765 1.4169 0.0186  -0.5702 -0.0711 174 SER   K O   
19224 C  CB  . SER   K  173 ? 1.5931 0.8434 1.4062 -0.0429 -0.6402 -0.1447 174 SER   K CB  
19225 O  OG  . SER   K  173 ? 1.6444 0.8906 1.3678 -0.0047 -0.6122 -0.1848 174 SER   K OG  
19226 N  N   . VAL   K  174 ? 1.6576 0.8643 1.3676 -0.0456 -0.5879 -0.0895 175 VAL   K N   
19227 C  CA  . VAL   K  174 ? 1.6946 0.8669 1.3627 -0.0337 -0.5806 -0.0588 175 VAL   K CA  
19228 C  C   . VAL   K  174 ? 1.7319 0.8674 1.3762 -0.0333 -0.6228 -0.0292 175 VAL   K C   
19229 O  O   . VAL   K  174 ? 1.7299 0.9655 1.4498 -0.0444 -0.6193 0.0172  175 VAL   K O   
19230 C  CB  . VAL   K  174 ? 1.7238 0.8662 1.3830 -0.0147 -0.5454 -0.0687 175 VAL   K CB  
19231 C  CG1 . VAL   K  174 ? 1.7103 0.8921 1.3872 0.0024  -0.5497 -0.0431 175 VAL   K CG1 
19232 C  CG2 . VAL   K  174 ? 1.7318 0.8652 1.3735 -0.0223 -0.5170 -0.1014 175 VAL   K CG2 
19233 N  N   . ASN   K  175 ? 1.7346 0.8052 1.3863 -0.0020 -0.6283 -0.0158 176 ASN   K N   
19234 C  CA  . ASN   K  175 ? 1.7346 0.7697 1.4100 -0.0309 -0.5891 -0.0644 176 ASN   K CA  
19235 C  C   . ASN   K  175 ? 1.7297 0.7599 1.4241 -0.0445 -0.5931 -0.0484 176 ASN   K C   
19236 O  O   . ASN   K  175 ? 1.7225 0.6256 1.3873 -0.0643 -0.5717 -0.0897 176 ASN   K O   
19237 C  CB  . ASN   K  175 ? 1.7105 0.7154 1.4071 -0.0170 -0.5533 -0.0614 176 ASN   K CB  
19238 C  CG  . ASN   K  175 ? 1.7187 0.6778 1.4111 0.0001  -0.5372 -0.0736 176 ASN   K CG  
19239 O  OD1 . ASN   K  175 ? 1.6679 0.4164 1.4257 0.0279  -0.4803 -0.1373 176 ASN   K OD1 
19240 N  ND2 . ASN   K  175 ? 1.7004 0.7820 1.4251 -0.0061 -0.5481 -0.0655 176 ASN   K ND2 
19241 N  N   . LEU   K  176 ? 1.7391 0.8273 1.4445 -0.0390 -0.5956 -0.0050 177 LEU   K N   
19242 C  CA  . LEU   K  176 ? 1.7417 0.8602 1.4670 -0.0171 -0.5987 0.0404  177 LEU   K CA  
19243 C  C   . LEU   K  176 ? 1.7012 0.8570 1.4756 0.0226  -0.6022 0.0531  177 LEU   K C   
19244 O  O   . LEU   K  176 ? 1.6749 0.7746 1.4668 0.0384  -0.6388 0.0789  177 LEU   K O   
19245 C  CB  . LEU   K  176 ? 1.7735 0.9232 1.5126 -0.0236 -0.6380 0.0280  177 LEU   K CB  
19246 C  CG  . LEU   K  176 ? 1.8201 0.9116 1.5592 -0.0027 -0.6099 0.0528  177 LEU   K CG  
19247 C  CD1 . LEU   K  176 ? 1.8427 0.9629 1.6172 -0.0116 -0.6451 0.0520  177 LEU   K CD1 
19248 C  CD2 . LEU   K  176 ? 1.8095 0.9218 1.5328 -0.0207 -0.6327 0.0522  177 LEU   K CD2 
19249 N  N   . TYR   K  177 ? 1.7367 0.8924 1.4905 0.0147  -0.5817 0.0730  178 TYR   K N   
19250 C  CA  . TYR   K  177 ? 1.7747 0.9057 1.5437 0.0050  -0.5526 0.0990  178 TYR   K CA  
19251 C  C   . TYR   K  177 ? 1.8169 0.9462 1.4915 -0.0075 -0.6029 0.1204  178 TYR   K C   
19252 O  O   . TYR   K  177 ? 1.8301 0.9811 1.4385 -0.0344 -0.5854 0.0190  178 TYR   K O   
19253 C  CB  . TYR   K  177 ? 1.7451 0.8950 1.4921 0.0062  -0.4933 0.0980  178 TYR   K CB  
19254 C  CG  . TYR   K  177 ? 1.7392 0.8989 1.5356 0.0211  -0.4435 0.1385  178 TYR   K CG  
19255 C  CD1 . TYR   K  177 ? 1.6726 0.8597 1.5142 0.0497  -0.4005 0.1135  178 TYR   K CD1 
19256 C  CD2 . TYR   K  177 ? 1.7625 0.9273 1.5771 0.0369  -0.3913 0.1391  178 TYR   K CD2 
19257 C  CE1 . TYR   K  177 ? 1.6466 0.8837 1.5170 0.0396  -0.3939 0.1332  178 TYR   K CE1 
19258 C  CE2 . TYR   K  177 ? 1.7304 0.9254 1.5976 0.0290  -0.3750 0.1414  178 TYR   K CE2 
19259 C  CZ  . TYR   K  177 ? 1.6456 0.9257 1.5228 0.0465  -0.3522 0.1061  178 TYR   K CZ  
19260 O  OH  . TYR   K  177 ? 1.6378 1.0033 1.5041 0.0357  -0.3727 0.0821  178 TYR   K OH  
19261 N  N   . HIS   K  178 ? 1.8319 0.9895 1.5723 0.0092  -0.6312 0.1706  179 HIS   K N   
19262 C  CA  . HIS   K  178 ? 1.8803 0.8804 1.6875 0.0101  -0.6053 0.2796  179 HIS   K CA  
19263 C  C   . HIS   K  178 ? 1.7827 0.8467 1.7633 0.0631  -0.6061 0.2893  179 HIS   K C   
19264 O  O   . HIS   K  178 ? 1.7354 0.7648 1.8944 0.0412  -0.6062 0.3189  179 HIS   K O   
19265 C  CB  . HIS   K  178 ? 1.9530 0.9986 1.7126 0.0305  -0.6458 0.3498  179 HIS   K CB  
19266 C  CG  . HIS   K  178 ? 2.0398 0.9895 1.7517 0.0552  -0.6848 0.5073  179 HIS   K CG  
19267 N  ND1 . HIS   K  178 ? 2.0959 0.8626 1.8923 0.1269  -0.6676 0.5978  179 HIS   K ND1 
19268 C  CD2 . HIS   K  178 ? 2.0727 1.0281 1.7746 -0.0160 -0.6256 0.5401  179 HIS   K CD2 
19269 C  CE1 . HIS   K  178 ? 2.1541 0.8791 1.8481 0.0955  -0.7041 0.6420  179 HIS   K CE1 
19270 N  NE2 . HIS   K  178 ? 2.0879 0.9870 1.8325 0.0372  -0.6866 0.6055  179 HIS   K NE2 
19271 N  N   . VAL   K  179 ? 1.8158 0.8586 1.8141 0.0093  -0.6023 0.2966  180 VAL   K N   
19272 C  CA  . VAL   K  179 ? 1.8806 0.8550 1.9355 0.0048  -0.5832 0.2509  180 VAL   K CA  
19273 C  C   . VAL   K  179 ? 1.9792 0.9096 1.9829 -0.0785 -0.6014 0.3002  180 VAL   K C   
19274 O  O   . VAL   K  179 ? 1.9793 0.8733 1.9975 -0.0800 -0.5998 0.3181  180 VAL   K O   
19275 C  CB  . VAL   K  179 ? 1.8475 0.8051 1.8572 -0.0276 -0.5234 0.2279  180 VAL   K CB  
19276 C  CG1 . VAL   K  179 ? 1.8754 0.8106 1.9013 -0.0158 -0.4925 0.1908  180 VAL   K CG1 
19277 C  CG2 . VAL   K  179 ? 1.8187 0.7858 1.8323 -0.0435 -0.4739 0.1927  180 VAL   K CG2 
19278 N  N   . THR   K  180 ? 2.0603 0.8511 2.1842 -0.0673 -0.6125 0.2577  181 THR   K N   
19279 C  CA  . THR   K  180 ? 2.1897 0.8027 2.2481 -0.0983 -0.6062 0.2784  181 THR   K CA  
19280 C  C   . THR   K  180 ? 2.2663 0.7339 2.3215 -0.0377 -0.5959 0.2844  181 THR   K C   
19281 O  O   . THR   K  180 ? 2.2564 0.5018 2.3033 -0.0015 -0.6062 0.3467  181 THR   K O   
19282 C  CB  . THR   K  180 ? 2.1913 0.8314 2.3701 -0.1306 -0.6455 0.2396  181 THR   K CB  
19283 O  OG1 . THR   K  180 ? 2.1136 0.5810 2.5007 -0.2068 -0.6972 0.2327  181 THR   K OG1 
19284 C  CG2 . THR   K  180 ? 2.1845 0.9374 2.3481 -0.2131 -0.6554 0.1667  181 THR   K CG2 
19285 N  N   . GLU   K  181 ? 2.3241 1.0461 2.2417 -0.0530 -0.5942 0.3267  182 GLU   K N   
19286 C  CA  . GLU   K  181 ? 2.2498 1.0904 2.2477 -0.1009 -0.5888 0.3095  182 GLU   K CA  
19287 C  C   . GLU   K  181 ? 2.2208 1.1669 2.3683 -0.0415 -0.5813 0.3216  182 GLU   K C   
19288 O  O   . GLU   K  181 ? 2.2143 1.2150 2.4317 0.0206  -0.6839 0.2375  182 GLU   K O   
19289 C  CB  . GLU   K  181 ? 2.3207 1.3005 2.1689 -0.0852 -0.6000 0.2613  182 GLU   K CB  
19290 C  CG  . GLU   K  181 ? 2.3794 1.3628 2.1113 -0.0856 -0.6184 0.2438  182 GLU   K CG  
19291 C  CD  . GLU   K  181 ? 2.4038 1.4458 2.0927 -0.0965 -0.6252 0.2459  182 GLU   K CD  
19292 O  OE1 . GLU   K  181 ? 2.4721 1.5604 2.0446 -0.0375 -0.6535 0.2808  182 GLU   K OE1 
19293 O  OE2 . GLU   K  181 ? 2.4347 1.4296 1.9458 -0.1181 -0.5989 0.2081  182 GLU   K OE2 
19294 N  N   . ASP   K  182 ? 2.2042 1.2844 2.3741 -0.0227 -0.4912 0.3769  183 ASP   K N   
19295 C  CA  . ASP   K  182 ? 2.1189 1.3460 2.2618 -0.0558 -0.5081 0.4158  183 ASP   K CA  
19296 C  C   . ASP   K  182 ? 1.9789 1.1619 2.1961 -0.0106 -0.4614 0.3070  183 ASP   K C   
19297 O  O   . ASP   K  182 ? 1.9593 1.0561 2.1531 -0.0872 -0.4980 0.2529  183 ASP   K O   
19298 C  CB  . ASP   K  182 ? 2.0848 1.4700 2.3559 0.0065  -0.5537 0.4506  183 ASP   K CB  
19299 C  CG  . ASP   K  182 ? 2.0994 1.5462 2.3778 -0.0005 -0.6284 0.4920  183 ASP   K CG  
19300 O  OD1 . ASP   K  182 ? 2.0886 1.5084 2.5150 0.0080  -0.6495 0.4703  183 ASP   K OD1 
19301 O  OD2 . ASP   K  182 ? 2.1179 1.6556 2.4382 -0.0257 -0.6629 0.4387  183 ASP   K OD2 
19302 N  N   . GLY   K  183 ? 2.0018 1.1483 1.9704 -0.0587 -0.5000 0.3121  184 GLY   K N   
19303 C  CA  . GLY   K  183 ? 1.9638 0.9744 1.9694 -0.0630 -0.4929 0.2766  184 GLY   K CA  
19304 C  C   . GLY   K  183 ? 1.9697 0.9522 1.9378 -0.0123 -0.4940 0.2913  184 GLY   K C   
19305 O  O   . GLY   K  183 ? 2.0130 0.7948 1.9056 -0.0217 -0.4507 0.3649  184 GLY   K O   
19306 N  N   . TRP   K  184 ? 1.9431 0.9009 1.8897 0.0030  -0.5123 0.2360  185 TRP   K N   
19307 C  CA  . TRP   K  184 ? 1.9601 0.8999 1.9113 -0.0268 -0.4953 0.1796  185 TRP   K CA  
19308 C  C   . TRP   K  184 ? 1.9579 0.9774 1.8819 0.0103  -0.5483 0.2224  185 TRP   K C   
19309 O  O   . TRP   K  184 ? 2.0054 0.9418 1.8608 0.0954  -0.6117 0.3416  185 TRP   K O   
19310 C  CB  . TRP   K  184 ? 1.8905 0.6901 1.8931 0.0110  -0.4341 0.1233  185 TRP   K CB  
19311 C  CG  . TRP   K  184 ? 1.8437 0.5095 2.0711 0.0221  -0.3788 0.0539  185 TRP   K CG  
19312 C  CD1 . TRP   K  184 ? 1.8223 0.5365 2.0912 0.0478  -0.3693 0.0057  185 TRP   K CD1 
19313 C  CD2 . TRP   K  184 ? 1.8883 0.3850 2.1314 0.0241  -0.3110 0.0315  185 TRP   K CD2 
19314 N  NE1 . TRP   K  184 ? 1.8044 0.6237 2.1164 -0.0031 -0.3352 -0.0027 185 TRP   K NE1 
19315 C  CE2 . TRP   K  184 ? 1.8649 0.5078 2.1211 -0.0374 -0.2988 -0.0042 185 TRP   K CE2 
19316 C  CE3 . TRP   K  184 ? 1.9165 0.3628 2.1504 0.0322  -0.2910 0.0456  185 TRP   K CE3 
19317 C  CZ2 . TRP   K  184 ? 1.8947 0.5511 2.1466 -0.0678 -0.2650 -0.0005 185 TRP   K CZ2 
19318 C  CZ3 . TRP   K  184 ? 1.9264 0.3563 2.1995 0.0262  -0.2668 0.0407  185 TRP   K CZ3 
19319 C  CH2 . TRP   K  184 ? 1.8993 0.4687 2.1775 -0.0357 -0.2717 -0.0085 185 TRP   K CH2 
19320 N  N   . ILE   K  185 ? 1.9335 1.0781 1.8047 -0.0964 -0.6114 0.2254  186 ILE   K N   
19321 C  CA  . ILE   K  185 ? 1.8961 1.1177 1.8194 -0.0526 -0.6468 0.2819  186 ILE   K CA  
19322 C  C   . ILE   K  185 ? 1.8100 1.0951 1.6987 -0.0548 -0.6504 0.2355  186 ILE   K C   
19323 O  O   . ILE   K  185 ? 1.8375 0.9592 1.5272 -0.0480 -0.7411 0.3231  186 ILE   K O   
19324 C  CB  . ILE   K  185 ? 1.8664 1.2470 1.8529 -0.0270 -0.7142 0.3286  186 ILE   K CB  
19325 C  CG1 . ILE   K  185 ? 1.9221 1.2611 1.9237 -0.0272 -0.7124 0.3556  186 ILE   K CG1 
19326 C  CG2 . ILE   K  185 ? 1.8496 1.2183 1.8744 -0.0035 -0.7296 0.3607  186 ILE   K CG2 
19327 C  CD1 . ILE   K  185 ? 1.9955 1.3743 1.9465 -0.0692 -0.6665 0.3459  186 ILE   K CD1 
19328 N  N   . TYR   K  186 ? 1.7449 1.0872 1.7161 -0.0466 -0.6642 0.1968  187 TYR   K N   
19329 C  CA  . TYR   K  186 ? 1.6926 1.0420 1.7288 0.0143  -0.6203 0.1716  187 TYR   K CA  
19330 C  C   . TYR   K  186 ? 1.7082 1.0565 1.7631 0.0088  -0.6208 0.1633  187 TYR   K C   
19331 O  O   . TYR   K  186 ? 1.7183 1.0857 1.9038 0.0537  -0.6213 0.2296  187 TYR   K O   
19332 C  CB  . TYR   K  186 ? 1.6240 1.0291 1.7471 0.0096  -0.6506 0.1005  187 TYR   K CB  
19333 C  CG  . TYR   K  186 ? 1.5758 0.9946 1.7391 0.0072  -0.6557 0.0675  187 TYR   K CG  
19334 C  CD1 . TYR   K  186 ? 1.5271 1.0326 1.6681 -0.0212 -0.6684 0.0572  187 TYR   K CD1 
19335 C  CD2 . TYR   K  186 ? 1.5609 1.0073 1.7905 0.0188  -0.6563 0.0386  187 TYR   K CD2 
19336 C  CE1 . TYR   K  186 ? 1.4971 1.0113 1.6571 -0.0160 -0.6626 0.0437  187 TYR   K CE1 
19337 C  CE2 . TYR   K  186 ? 1.5067 1.0315 1.7509 0.0089  -0.6580 0.0375  187 TYR   K CE2 
19338 C  CZ  . TYR   K  186 ? 1.4924 1.0178 1.6859 -0.0079 -0.6545 0.0380  187 TYR   K CZ  
19339 O  OH  . TYR   K  186 ? 1.3899 1.0065 1.6645 0.0019  -0.6397 0.0166  187 TYR   K OH  
19340 N  N   . HIS   K  187 ? 1.7533 1.0813 1.7475 0.0339  -0.5506 0.1201  188 HIS   K N   
19341 C  CA  . HIS   K  187 ? 1.8136 1.0630 1.7353 0.0259  -0.5490 0.1244  188 HIS   K CA  
19342 C  C   . HIS   K  187 ? 1.7739 0.9642 1.7059 0.0841  -0.5301 0.0773  188 HIS   K C   
19343 O  O   . HIS   K  187 ? 1.8161 0.9200 1.7313 0.0792  -0.4773 0.1479  188 HIS   K O   
19344 C  CB  . HIS   K  187 ? 1.8820 1.1427 1.6657 0.0130  -0.5465 0.1445  188 HIS   K CB  
19345 C  CG  . HIS   K  187 ? 1.9337 1.2300 1.6555 0.0070  -0.6138 0.1858  188 HIS   K CG  
19346 N  ND1 . HIS   K  187 ? 1.9304 1.2851 1.7049 0.0335  -0.6577 0.2511  188 HIS   K ND1 
19347 C  CD2 . HIS   K  187 ? 1.9617 1.2149 1.6237 0.0158  -0.6238 0.2190  188 HIS   K CD2 
19348 C  CE1 . HIS   K  187 ? 1.9470 1.2914 1.7056 0.0443  -0.6981 0.2699  188 HIS   K CE1 
19349 N  NE2 . HIS   K  187 ? 1.9694 1.2723 1.6761 0.0528  -0.6921 0.2383  188 HIS   K NE2 
19350 N  N   . GLY   K  188 ? 1.7461 0.7906 1.6983 0.0964  -0.5701 0.0411  189 GLY   K N   
19351 C  CA  . GLY   K  188 ? 1.7389 0.8017 1.6791 0.0681  -0.5622 -0.0102 189 GLY   K CA  
19352 C  C   . GLY   K  188 ? 1.7228 0.8717 1.5919 0.0393  -0.5832 -0.0313 189 GLY   K C   
19353 O  O   . GLY   K  188 ? 1.7038 0.9741 1.4928 -0.0044 -0.6142 -0.0681 189 GLY   K O   
19354 N  N   . ASN   K  189 ? 1.7421 0.8822 1.6157 0.0162  -0.5695 -0.0351 190 ASN   K N   
19355 C  CA  . ASN   K  189 ? 1.7149 0.8398 1.6407 0.0246  -0.5450 -0.0416 190 ASN   K CA  
19356 C  C   . ASN   K  189 ? 1.7211 0.8115 1.6755 0.0119  -0.5296 -0.0157 190 ASN   K C   
19357 O  O   . ASN   K  189 ? 1.7186 0.6948 1.7958 -0.0072 -0.5260 -0.0379 190 ASN   K O   
19358 C  CB  . ASN   K  189 ? 1.7112 0.8247 1.6329 0.0597  -0.5566 -0.0244 190 ASN   K CB  
19359 C  CG  . ASN   K  189 ? 1.7077 0.7971 1.6341 0.0606  -0.5600 -0.0387 190 ASN   K CG  
19360 O  OD1 . ASN   K  189 ? 1.7260 0.8179 1.6591 0.0310  -0.5645 -0.0614 190 ASN   K OD1 
19361 N  ND2 . ASN   K  189 ? 1.7047 0.7900 1.6298 0.0919  -0.5568 -0.0336 190 ASN   K ND2 
19362 N  N   . HIS   K  190 ? 1.6797 0.7851 1.6129 -0.0289 -0.5108 -0.0270 191 HIS   K N   
19363 C  CA  . HIS   K  190 ? 1.7052 0.8394 1.5854 -0.0702 -0.5195 -0.0536 191 HIS   K CA  
19364 C  C   . HIS   K  190 ? 1.7266 0.8516 1.5624 -0.0363 -0.4877 -0.0633 191 HIS   K C   
19365 O  O   . HIS   K  190 ? 1.7082 0.9138 1.5357 -0.0467 -0.4752 -0.1084 191 HIS   K O   
19366 C  CB  . HIS   K  190 ? 1.6949 0.7898 1.5606 -0.1046 -0.5390 -0.0420 191 HIS   K CB  
19367 C  CG  . HIS   K  190 ? 1.6895 0.7663 1.5679 -0.1591 -0.5521 -0.0432 191 HIS   K CG  
19368 N  ND1 . HIS   K  190 ? 1.7196 0.7688 1.5791 -0.1607 -0.5725 -0.0221 191 HIS   K ND1 
19369 C  CD2 . HIS   K  190 ? 1.6744 0.7159 1.5421 -0.1155 -0.5656 -0.0509 191 HIS   K CD2 
19370 C  CE1 . HIS   K  190 ? 1.7108 0.7167 1.6088 -0.1395 -0.6020 -0.0557 191 HIS   K CE1 
19371 N  NE2 . HIS   K  190 ? 1.7047 0.6421 1.5834 -0.1205 -0.5814 -0.0544 191 HIS   K NE2 
19372 N  N   . ASP   K  191 ? 1.7711 0.8715 1.5746 -0.0203 -0.4359 -0.0687 192 ASP   K N   
19373 C  CA  . ASP   K  191 ? 1.8209 0.8239 1.5614 0.0390  -0.4227 -0.1018 192 ASP   K CA  
19374 C  C   . ASP   K  191 ? 1.8171 0.7582 1.4919 0.0213  -0.4492 -0.0594 192 ASP   K C   
19375 O  O   . ASP   K  191 ? 1.8584 0.7092 1.5267 0.0337  -0.4640 -0.1102 192 ASP   K O   
19376 C  CB  . ASP   K  191 ? 1.8558 0.8285 1.6484 0.0377  -0.3758 -0.1060 192 ASP   K CB  
19377 C  CG  . ASP   K  191 ? 1.9188 0.7186 1.7262 0.0797  -0.3135 -0.0979 192 ASP   K CG  
19378 O  OD1 . ASP   K  191 ? 2.0169 0.8353 1.8466 0.0280  -0.1956 -0.1352 192 ASP   K OD1 
19379 O  OD2 . ASP   K  191 ? 1.9776 0.7101 1.7721 0.0965  -0.2012 -0.1745 192 ASP   K OD2 
19380 N  N   . VAL   K  192 ? 1.8047 0.7577 1.4401 -0.0042 -0.4300 -0.0224 193 VAL   K N   
19381 C  CA  . VAL   K  192 ? 1.7778 0.7921 1.4024 0.0057  -0.4136 -0.0165 193 VAL   K CA  
19382 C  C   . VAL   K  192 ? 1.7941 0.7605 1.3721 0.0123  -0.4443 -0.0328 193 VAL   K C   
19383 O  O   . VAL   K  192 ? 1.7532 0.7011 1.3810 0.0724  -0.4337 -0.0083 193 VAL   K O   
19384 C  CB  . VAL   K  192 ? 1.7309 0.8157 1.4312 0.0158  -0.3694 -0.0196 193 VAL   K CB  
19385 C  CG1 . VAL   K  192 ? 1.7660 0.8600 1.4523 0.0064  -0.3361 -0.0826 193 VAL   K CG1 
19386 C  CG2 . VAL   K  192 ? 1.7333 0.7993 1.4218 0.0248  -0.3483 0.0164  193 VAL   K CG2 
19387 N  N   . GLY   K  193 ? 1.7963 0.7870 1.3889 -0.0554 -0.4416 0.0212  194 GLY   K N   
19388 C  CA  . GLY   K  193 ? 1.8066 0.8341 1.4297 -0.0799 -0.4417 0.0334  194 GLY   K CA  
19389 C  C   . GLY   K  193 ? 1.8321 0.8614 1.4256 -0.0837 -0.4486 0.0486  194 GLY   K C   
19390 O  O   . GLY   K  193 ? 1.8186 0.9207 1.3998 -0.1166 -0.4259 -0.0388 194 GLY   K O   
19391 N  N   . GLU   K  194 ? 1.8528 0.8563 1.4450 -0.1013 -0.4529 0.0640  195 GLU   K N   
19392 C  CA  . GLU   K  194 ? 1.8689 0.8109 1.4628 -0.1180 -0.4790 0.0623  195 GLU   K CA  
19393 C  C   . GLU   K  194 ? 1.8422 0.6539 1.4231 -0.1108 -0.5145 0.0768  195 GLU   K C   
19394 O  O   . GLU   K  194 ? 1.8358 0.5674 1.4081 -0.0941 -0.5204 0.1144  195 GLU   K O   
19395 C  CB  . GLU   K  194 ? 1.8801 0.8840 1.4574 -0.0861 -0.5147 0.0826  195 GLU   K CB  
19396 C  CG  . GLU   K  194 ? 1.9205 0.9954 1.5243 -0.0961 -0.4683 0.1017  195 GLU   K CG  
19397 C  CD  . GLU   K  194 ? 2.0091 1.0849 1.5680 -0.0663 -0.3645 0.0469  195 GLU   K CD  
19398 O  OE1 . GLU   K  194 ? 2.1142 1.1780 1.5990 -0.0002 -0.2475 0.1330  195 GLU   K OE1 
19399 O  OE2 . GLU   K  194 ? 2.0652 1.1297 1.6068 -0.0215 -0.3309 0.1637  195 GLU   K OE2 
19400 N  N   . LEU   K  195 ? 1.8444 0.6355 1.4696 -0.1066 -0.4893 0.0923  196 LEU   K N   
19401 C  CA  . LEU   K  195 ? 1.8469 0.6567 1.4712 -0.0863 -0.4787 0.0784  196 LEU   K CA  
19402 C  C   . LEU   K  195 ? 1.8608 0.6418 1.4960 -0.1015 -0.4685 0.0599  196 LEU   K C   
19403 O  O   . LEU   K  195 ? 1.8469 0.5915 1.4944 -0.0843 -0.4990 0.0481  196 LEU   K O   
19404 C  CB  . LEU   K  195 ? 1.8354 0.6320 1.4891 -0.0867 -0.4657 0.1090  196 LEU   K CB  
19405 C  CG  . LEU   K  195 ? 1.8492 0.5519 1.4639 -0.0910 -0.4851 0.1320  196 LEU   K CG  
19406 C  CD1 . LEU   K  195 ? 1.8859 0.5580 1.4530 -0.1092 -0.4925 0.1358  196 LEU   K CD1 
19407 C  CD2 . LEU   K  195 ? 1.8507 0.4866 1.4780 -0.0900 -0.4674 0.1654  196 LEU   K CD2 
19408 N  N   . PHE   K  196 ? 1.8304 0.6648 1.5475 -0.0675 -0.4558 0.0819  197 PHE   K N   
19409 C  CA  . PHE   K  196 ? 1.7871 0.7542 1.6201 -0.0395 -0.4238 0.0488  197 PHE   K CA  
19410 C  C   . PHE   K  196 ? 1.8067 0.7986 1.6236 -0.0695 -0.4141 0.0370  197 PHE   K C   
19411 O  O   . PHE   K  196 ? 1.7576 0.7096 1.6162 -0.1037 -0.3998 0.0687  197 PHE   K O   
19412 C  CB  . PHE   K  196 ? 1.7532 0.7504 1.6702 -0.0124 -0.4360 0.0665  197 PHE   K CB  
19413 C  CG  . PHE   K  196 ? 1.7771 0.7022 1.7456 -0.0389 -0.4190 0.0697  197 PHE   K CG  
19414 C  CD1 . PHE   K  196 ? 1.7929 0.7380 1.8151 -0.0391 -0.3456 0.0764  197 PHE   K CD1 
19415 C  CD2 . PHE   K  196 ? 1.7514 0.6952 1.7560 -0.0322 -0.4223 0.0758  197 PHE   K CD2 
19416 C  CE1 . PHE   K  196 ? 1.8399 0.6695 1.8639 -0.1021 -0.3087 0.0201  197 PHE   K CE1 
19417 C  CE2 . PHE   K  196 ? 1.8319 0.6479 1.7993 -0.0723 -0.3723 0.0126  197 PHE   K CE2 
19418 C  CZ  . PHE   K  196 ? 1.8416 0.6322 1.8652 -0.0647 -0.3067 -0.0080 197 PHE   K CZ  
19419 N  N   . TRP   K  197 ? 1.7987 0.8927 1.7048 -0.0650 -0.4112 0.0358  198 TRP   K N   
19420 C  CA  . TRP   K  197 ? 1.8531 0.9317 1.6886 -0.0418 -0.4439 -0.0062 198 TRP   K CA  
19421 C  C   . TRP   K  197 ? 1.8645 0.8858 1.6997 -0.0554 -0.4888 -0.0201 198 TRP   K C   
19422 O  O   . TRP   K  197 ? 1.8665 0.8568 1.7074 -0.0327 -0.5018 -0.0195 198 TRP   K O   
19423 C  CB  . TRP   K  197 ? 1.8581 0.9841 1.7567 -0.0377 -0.4107 -0.0028 198 TRP   K CB  
19424 C  CG  . TRP   K  197 ? 1.8687 0.9307 1.8214 0.0102  -0.3485 0.0566  198 TRP   K CG  
19425 C  CD1 . TRP   K  197 ? 1.8947 0.9787 1.8187 0.0457  -0.2890 0.1006  198 TRP   K CD1 
19426 C  CD2 . TRP   K  197 ? 1.8988 0.8819 1.8172 -0.0042 -0.3069 -0.0306 198 TRP   K CD2 
19427 N  NE1 . TRP   K  197 ? 1.9119 0.9216 1.8846 0.0816  -0.2433 0.1118  198 TRP   K NE1 
19428 C  CE2 . TRP   K  197 ? 1.9180 0.9265 1.8553 0.0243  -0.2683 0.0550  198 TRP   K CE2 
19429 C  CE3 . TRP   K  197 ? 1.9176 0.8881 1.7839 -0.0374 -0.3353 -0.0606 198 TRP   K CE3 
19430 C  CZ2 . TRP   K  197 ? 1.9282 0.8342 1.8939 0.0230  -0.2358 -0.0338 198 TRP   K CZ2 
19431 C  CZ3 . TRP   K  197 ? 1.9264 0.8791 1.8550 -0.0015 -0.2972 -0.0824 198 TRP   K CZ3 
19432 C  CH2 . TRP   K  197 ? 1.9567 0.8910 1.8588 -0.0227 -0.2499 -0.0812 198 TRP   K CH2 
19433 N  N   . LYS   K  198 ? 1.8393 0.8895 1.6198 -0.0560 -0.5782 0.0766  199 LYS   K N   
19434 C  CA  . LYS   K  198 ? 1.8313 0.8931 1.6181 -0.0781 -0.6416 0.0560  199 LYS   K CA  
19435 C  C   . LYS   K  198 ? 1.8562 0.7748 1.4700 -0.0852 -0.6830 0.0562  199 LYS   K C   
19436 O  O   . LYS   K  198 ? 1.8284 0.7276 1.4863 -0.1313 -0.7190 0.0480  199 LYS   K O   
19437 C  CB  . LYS   K  198 ? 1.8419 0.9048 1.6535 -0.0241 -0.6400 0.0916  199 LYS   K CB  
19438 C  CG  . LYS   K  198 ? 1.8737 1.0499 1.6465 -0.0241 -0.6626 0.1394  199 LYS   K CG  
19439 C  CD  . LYS   K  198 ? 1.8611 1.0406 1.6835 0.0253  -0.6687 0.1990  199 LYS   K CD  
19440 C  CE  . LYS   K  198 ? 1.8750 1.0481 1.6895 0.0193  -0.6891 0.2122  199 LYS   K CE  
19441 N  NZ  . LYS   K  198 ? 1.9055 1.1117 1.7156 0.0060  -0.7225 0.2215  199 LYS   K NZ  
19442 N  N   . VAL   K  199 ? 1.8286 0.7397 1.5118 -0.0711 -0.6581 0.0886  200 VAL   K N   
19443 C  CA  . VAL   K  199 ? 1.8798 0.8176 1.4967 -0.0912 -0.6282 0.0981  200 VAL   K CA  
19444 C  C   . VAL   K  199 ? 1.9310 0.9096 1.5170 -0.1186 -0.6194 -0.0441 200 VAL   K C   
19445 O  O   . VAL   K  199 ? 1.9447 1.0373 1.4535 -0.1536 -0.7091 0.0035  200 VAL   K O   
19446 C  CB  . VAL   K  199 ? 1.8375 0.7705 1.4930 -0.0772 -0.6043 0.1283  200 VAL   K CB  
19447 C  CG1 . VAL   K  199 ? 1.8659 0.7589 1.4895 -0.0949 -0.5676 0.1023  200 VAL   K CG1 
19448 C  CG2 . VAL   K  199 ? 1.8464 0.7674 1.4784 -0.0526 -0.6281 0.1809  200 VAL   K CG2 
19449 N  N   . LYS   K  200 ? 1.9728 0.9425 1.5902 -0.1799 -0.5899 -0.0046 201 LYS   K N   
19450 C  CA  . LYS   K  200 ? 1.9863 0.9772 1.6618 -0.1928 -0.5971 -0.1004 201 LYS   K CA  
19451 C  C   . LYS   K  200 ? 2.0236 1.0425 1.6534 -0.2143 -0.6062 -0.1052 201 LYS   K C   
19452 O  O   . LYS   K  200 ? 2.0051 1.0909 1.6803 -0.2590 -0.5836 -0.1409 201 LYS   K O   
19453 C  CB  . LYS   K  200 ? 1.9731 1.0050 1.6857 -0.1817 -0.5720 -0.0867 201 LYS   K CB  
19454 C  CG  . LYS   K  200 ? 1.9774 1.0219 1.7605 -0.2117 -0.5655 -0.1702 201 LYS   K CG  
19455 C  CD  . LYS   K  200 ? 1.9563 0.9554 1.7875 -0.2769 -0.5386 -0.1936 201 LYS   K CD  
19456 C  CE  . LYS   K  200 ? 1.9670 1.0259 1.7983 -0.3486 -0.5387 -0.3416 201 LYS   K CE  
19457 N  NZ  . LYS   K  200 ? 2.0284 0.9753 1.7643 -0.3968 -0.5419 -0.4415 201 LYS   K NZ  
19458 N  N   . GLU   K  201 ? 2.0252 1.0478 1.6163 -0.1857 -0.6647 -0.0851 202 GLU   K N   
19459 C  CA  . GLU   K  201 ? 2.0611 1.0913 1.6040 -0.1732 -0.6846 -0.0823 202 GLU   K CA  
19460 C  C   . GLU   K  201 ? 2.1181 1.0908 1.5587 -0.1769 -0.7286 -0.0995 202 GLU   K C   
19461 O  O   . GLU   K  201 ? 2.1514 0.9985 1.4478 -0.2461 -0.7724 -0.0155 202 GLU   K O   
19462 C  CB  . GLU   K  201 ? 2.0429 1.1446 1.6305 -0.1500 -0.7066 -0.0716 202 GLU   K CB  
19463 C  CG  . GLU   K  201 ? 2.0667 1.2524 1.6133 -0.1310 -0.7248 -0.0590 202 GLU   K CG  
19464 C  CD  . GLU   K  201 ? 2.0408 1.3059 1.6090 -0.0979 -0.7611 -0.0372 202 GLU   K CD  
19465 O  OE1 . GLU   K  201 ? 2.0481 1.3576 1.6123 -0.1448 -0.7269 -0.0416 202 GLU   K OE1 
19466 O  OE2 . GLU   K  201 ? 2.0772 1.3229 1.5692 -0.0921 -0.7779 -0.0034 202 GLU   K OE2 
19467 N  N   . GLU   K  202 ? 2.1406 1.0861 1.5847 -0.0947 -0.7424 -0.0797 203 GLU   K N   
19468 C  CA  . GLU   K  202 ? 2.1378 1.1907 1.5250 -0.0764 -0.7872 -0.0812 203 GLU   K CA  
19469 C  C   . GLU   K  202 ? 2.1707 1.1382 1.4369 -0.0883 -0.7563 -0.1121 203 GLU   K C   
19470 O  O   . GLU   K  202 ? 2.1155 1.0285 1.4299 -0.0998 -0.7807 -0.1103 203 GLU   K O   
19471 C  CB  . GLU   K  202 ? 2.1804 1.1728 1.5812 -0.0451 -0.8373 -0.0293 203 GLU   K CB  
19472 C  CG  . GLU   K  202 ? 2.1703 1.2500 1.6691 -0.0210 -0.8722 0.0039  203 GLU   K CG  
19473 C  CD  . GLU   K  202 ? 2.1768 1.2323 1.7284 -0.0220 -0.9274 0.0308  203 GLU   K CD  
19474 O  OE1 . GLU   K  202 ? 2.2092 1.2271 1.7002 -0.0570 -1.0115 0.0542  203 GLU   K OE1 
19475 O  OE2 . GLU   K  202 ? 2.1564 1.3060 1.8537 0.0287  -0.9490 0.0249  203 GLU   K OE2 
19476 N  N   . GLU   K  203 ? 2.0808 1.1528 1.5002 -0.0726 -0.7131 -0.1229 204 GLU   K N   
19477 C  CA  . GLU   K  203 ? 2.1221 1.2154 1.4635 -0.1071 -0.6639 -0.1353 204 GLU   K CA  
19478 C  C   . GLU   K  203 ? 2.0890 1.2860 1.3725 -0.1058 -0.6361 -0.2482 204 GLU   K C   
19479 O  O   . GLU   K  203 ? 2.1268 1.4029 1.1519 -0.1761 -0.7555 -0.3114 204 GLU   K O   
19480 C  CB  . GLU   K  203 ? 2.1082 1.1090 1.4679 -0.0979 -0.6561 -0.1096 204 GLU   K CB  
19481 C  CG  . GLU   K  203 ? 2.1658 1.1332 1.4616 -0.0954 -0.6035 -0.0696 204 GLU   K CG  
19482 C  CD  . GLU   K  203 ? 2.1645 1.1228 1.4655 -0.0888 -0.6097 -0.0552 204 GLU   K CD  
19483 O  OE1 . GLU   K  203 ? 2.1827 1.1608 1.4025 -0.0891 -0.5855 -0.0180 204 GLU   K OE1 
19484 O  OE2 . GLU   K  203 ? 2.2326 1.1197 1.5172 -0.0516 -0.5869 0.0173  204 GLU   K OE2 
19485 N  N   . GLY   K  204 ? 2.0854 1.2613 1.4681 -0.1098 -0.6233 -0.2350 205 GLY   K N   
19486 C  CA  . GLY   K  204 ? 2.0880 1.2706 1.5272 -0.1174 -0.5845 -0.2855 205 GLY   K CA  
19487 C  C   . GLY   K  204 ? 2.0608 1.2722 1.5747 -0.0903 -0.5518 -0.2585 205 GLY   K C   
19488 O  O   . GLY   K  204 ? 2.0539 1.3196 1.6105 -0.0711 -0.5187 -0.3076 205 GLY   K O   
19489 N  N   . SER   K  205 ? 2.0393 1.1733 1.5560 -0.0842 -0.5634 -0.1934 206 SER   K N   
19490 C  CA  . SER   K  205 ? 2.0294 1.1181 1.5861 -0.0954 -0.5687 -0.1967 206 SER   K CA  
19491 C  C   . SER   K  205 ? 2.0161 1.0634 1.6434 -0.1022 -0.5572 -0.1646 206 SER   K C   
19492 O  O   . SER   K  205 ? 2.0024 1.1491 1.5773 -0.1177 -0.6079 -0.1927 206 SER   K O   
19493 C  CB  . SER   K  205 ? 2.0239 1.0933 1.5824 -0.0877 -0.5555 -0.1131 206 SER   K CB  
19494 O  OG  . SER   K  205 ? 2.0207 1.1001 1.6104 -0.0084 -0.5711 -0.0027 206 SER   K OG  
19495 N  N   . PHE   K  206 ? 1.9886 1.0086 1.7687 -0.0400 -0.5795 -0.1108 207 PHE   K N   
19496 C  CA  . PHE   K  206 ? 1.9776 0.9667 1.7915 0.0061  -0.5485 -0.1137 207 PHE   K CA  
19497 C  C   . PHE   K  206 ? 1.9842 0.9800 1.9885 0.0175  -0.5649 -0.1973 207 PHE   K C   
19498 O  O   . PHE   K  206 ? 1.8000 1.0877 2.1840 0.0849  -0.6363 -0.2222 207 PHE   K O   
19499 C  CB  . PHE   K  206 ? 1.9724 0.8462 1.7504 -0.0117 -0.5830 -0.0983 207 PHE   K CB  
19500 C  CG  . PHE   K  206 ? 1.9960 0.8156 1.6651 0.0170  -0.5345 -0.1227 207 PHE   K CG  
19501 C  CD1 . PHE   K  206 ? 1.9406 0.7700 1.7164 0.0289  -0.4949 -0.1487 207 PHE   K CD1 
19502 C  CD2 . PHE   K  206 ? 1.9744 0.8120 1.5898 -0.0047 -0.5586 -0.1281 207 PHE   K CD2 
19503 C  CE1 . PHE   K  206 ? 1.9877 0.7306 1.6919 0.0400  -0.4485 -0.1308 207 PHE   K CE1 
19504 C  CE2 . PHE   K  206 ? 2.0016 0.8035 1.5787 -0.0343 -0.5165 -0.0996 207 PHE   K CE2 
19505 C  CZ  . PHE   K  206 ? 1.9769 0.7586 1.6167 0.0080  -0.4953 -0.0700 207 PHE   K CZ  
19506 N  N   . ASN   K  207 ? 2.1128 0.8631 2.0014 -0.0521 -0.5681 -0.2794 208 ASN   K N   
19507 C  CA  . ASN   K  207 ? 2.1133 0.8857 2.0651 -0.1013 -0.5219 -0.3091 208 ASN   K CA  
19508 C  C   . ASN   K  207 ? 2.1727 0.6369 2.1362 -0.1530 -0.4928 -0.3106 208 ASN   K C   
19509 O  O   . ASN   K  207 ? 2.1027 0.7122 2.1848 -0.2023 -0.5269 -0.2501 208 ASN   K O   
19510 C  CB  . ASN   K  207 ? 2.1177 0.9829 2.0680 -0.0767 -0.4650 -0.2419 208 ASN   K CB  
19511 C  CG  . ASN   K  207 ? 2.1001 0.9839 2.0591 -0.0996 -0.4175 -0.1946 208 ASN   K CG  
19512 O  OD1 . ASN   K  207 ? 2.1689 0.8895 2.0229 0.0091  -0.3897 -0.1488 208 ASN   K OD1 
19513 N  ND2 . ASN   K  207 ? 2.0955 1.0963 2.0309 -0.0960 -0.4362 -0.1853 208 ASN   K ND2 
19514 N  N   . ASN   K  208 ? 2.1687 0.6317 2.2116 -0.1622 -0.5089 -0.2890 209 ASN   K N   
19515 C  CA  . ASN   K  208 ? 2.1800 0.5754 2.3374 -0.1475 -0.4659 -0.1586 209 ASN   K CA  
19516 C  C   . ASN   K  208 ? 2.2061 0.5405 2.4769 -0.1488 -0.3997 -0.1387 209 ASN   K C   
19517 O  O   . ASN   K  208 ? 2.2499 0.4219 2.6414 -0.1244 -0.3817 -0.1729 209 ASN   K O   
19518 C  CB  . ASN   K  208 ? 2.1269 0.6992 2.3287 -0.1511 -0.5110 -0.1018 209 ASN   K CB  
19519 C  CG  . ASN   K  208 ? 2.0978 0.6790 2.2380 -0.1131 -0.5874 -0.0222 209 ASN   K CG  
19520 O  OD1 . ASN   K  208 ? 2.1585 0.5444 2.2414 -0.1491 -0.6021 0.0042  209 ASN   K OD1 
19521 N  ND2 . ASN   K  208 ? 2.1299 0.6645 2.2152 -0.1187 -0.5845 -0.0031 209 ASN   K ND2 
19522 N  N   . VAL   K  209 ? 2.1459 0.6209 2.4691 -0.1437 -0.3474 -0.0097 210 VAL   K N   
19523 C  CA  . VAL   K  209 ? 2.0118 0.4848 2.5211 -0.1353 -0.3950 0.0045  210 VAL   K CA  
19524 C  C   . VAL   K  209 ? 2.0546 0.4792 2.5144 -0.1780 -0.3953 -0.0006 210 VAL   K C   
19525 O  O   . VAL   K  209 ? 1.9390 0.4568 2.5094 -0.2815 -0.4643 -0.0970 210 VAL   K O   
19526 C  CB  . VAL   K  209 ? 1.9753 0.5387 2.4536 0.0084  -0.3728 0.1656  210 VAL   K CB  
19527 C  CG1 . VAL   K  209 ? 1.9049 0.5495 2.4719 0.0609  -0.4294 0.1879  210 VAL   K CG1 
19528 C  CG2 . VAL   K  209 ? 1.9597 0.4705 2.4342 0.0352  -0.3640 0.1964  210 VAL   K CG2 
19529 N  N   . ILE   K  210 ? 2.0416 0.5476 2.6475 -0.1993 -0.3286 0.0308  211 ILE   K N   
19530 C  CA  . ILE   K  210 ? 1.9231 0.6796 2.6835 -0.1524 -0.3185 0.0349  211 ILE   K CA  
19531 C  C   . ILE   K  210 ? 1.9385 0.6555 2.6373 -0.1066 -0.2698 -0.0094 211 ILE   K C   
19532 O  O   . ILE   K  210 ? 1.7218 0.4596 2.8464 -0.0873 -0.2926 0.0983  211 ILE   K O   
19533 C  CB  . ILE   K  210 ? 2.0553 0.7466 2.7123 -0.1780 -0.3036 0.0741  211 ILE   K CB  
19534 C  CG1 . ILE   K  210 ? 2.1034 0.6554 2.6586 -0.1908 -0.2935 0.0449  211 ILE   K CG1 
19535 C  CG2 . ILE   K  210 ? 2.0711 0.6965 2.7527 -0.1881 -0.3115 0.0792  211 ILE   K CG2 
19536 C  CD1 . ILE   K  210 ? 2.1262 0.6693 2.6285 -0.1948 -0.3156 0.0355  211 ILE   K CD1 
19537 N  N   . GLY   K  211 ? 1.9273 0.8087 2.6318 -0.0825 -0.2631 -0.0909 212 GLY   K N   
19538 C  CA  . GLY   K  211 ? 1.9592 0.8761 2.5603 -0.0716 -0.3230 -0.1436 212 GLY   K CA  
19539 C  C   . GLY   K  211 ? 1.9499 0.9987 2.5991 -0.0741 -0.3226 -0.2400 212 GLY   K C   
19540 O  O   . GLY   K  211 ? 2.0646 1.0185 2.6366 -0.0790 -0.3625 -0.2095 212 GLY   K O   
19541 O  OXT . GLY   K  211 ? 2.0615 0.7930 2.5358 -0.1246 -0.3630 -0.2789 212 GLY   K OXT 
19542 N  N   . GLN   L  1   ? 1.6774 0.7745 1.3086 0.0825  -0.4526 -0.0272 1   GLN   L N   
19543 C  CA  . GLN   L  1   ? 1.6833 0.7614 1.3594 0.0696  -0.3881 -0.0251 1   GLN   L CA  
19544 C  C   . GLN   L  1   ? 1.7086 0.6387 1.4053 0.0960  -0.3415 -0.0660 1   GLN   L C   
19545 O  O   . GLN   L  1   ? 1.7065 0.5207 1.5401 0.1345  -0.3385 0.0087  1   GLN   L O   
19546 C  CB  . GLN   L  1   ? 1.7716 0.8861 1.3869 0.0615  -0.3295 -0.0622 1   GLN   L CB  
19547 C  CG  . GLN   L  1   ? 1.8235 1.0397 1.4045 -0.0225 -0.2336 -0.0386 1   GLN   L CG  
19548 C  CD  . GLN   L  1   ? 1.9067 1.1403 1.4275 0.0518  -0.1732 0.0108  1   GLN   L CD  
19549 O  OE1 . GLN   L  1   ? 2.0109 1.3870 1.4192 -0.0318 0.0120  0.0211  1   GLN   L OE1 
19550 N  NE2 . GLN   L  1   ? 1.9983 1.1772 1.4039 0.0002  -0.1364 -0.0510 1   GLN   L NE2 
19551 N  N   . PHE   L  2   ? 1.5877 0.6362 1.4123 0.0711  -0.2761 -0.0676 2   PHE   L N   
19552 C  CA  . PHE   L  2   ? 1.5412 0.5631 1.3407 0.0140  -0.3026 -0.1103 2   PHE   L CA  
19553 C  C   . PHE   L  2   ? 1.4929 0.4331 1.3313 0.0047  -0.2947 -0.1627 2   PHE   L C   
19554 O  O   . PHE   L  2   ? 1.4790 0.3578 1.2884 0.0905  -0.2951 -0.1812 2   PHE   L O   
19555 C  CB  . PHE   L  2   ? 1.4466 0.5640 1.3589 0.0105  -0.3177 -0.1156 2   PHE   L CB  
19556 C  CG  . PHE   L  2   ? 1.4414 0.5470 1.3129 0.0098  -0.3570 -0.0573 2   PHE   L CG  
19557 C  CD1 . PHE   L  2   ? 1.4526 0.5425 1.3409 -0.0086 -0.3731 -0.0146 2   PHE   L CD1 
19558 C  CD2 . PHE   L  2   ? 1.4219 0.5542 1.2795 0.0092  -0.3865 -0.0620 2   PHE   L CD2 
19559 C  CE1 . PHE   L  2   ? 1.4494 0.5401 1.3254 -0.0108 -0.3968 0.0159  2   PHE   L CE1 
19560 C  CE2 . PHE   L  2   ? 1.4296 0.5248 1.3145 0.0123  -0.3869 -0.0351 2   PHE   L CE2 
19561 C  CZ  . PHE   L  2   ? 1.4379 0.5300 1.3059 0.0190  -0.3919 -0.0042 2   PHE   L CZ  
19562 N  N   . ASN   L  3   ? 1.5098 0.4575 1.2892 -0.0188 -0.2974 -0.2058 3   ASN   L N   
19563 C  CA  . ASN   L  3   ? 1.4828 0.5507 1.2827 -0.0024 -0.2810 -0.1517 3   ASN   L CA  
19564 C  C   . ASN   L  3   ? 1.4675 0.4885 1.2364 -0.0422 -0.2619 -0.1477 3   ASN   L C   
19565 O  O   . ASN   L  3   ? 1.5080 0.4955 1.1875 -0.0446 -0.2637 -0.1370 3   ASN   L O   
19566 C  CB  . ASN   L  3   ? 1.4951 0.6629 1.2865 -0.1158 -0.3001 -0.2060 3   ASN   L CB  
19567 C  CG  . ASN   L  3   ? 1.5187 0.7717 1.2539 -0.0906 -0.2931 -0.2175 3   ASN   L CG  
19568 O  OD1 . ASN   L  3   ? 1.5478 0.8932 1.4690 -0.1995 -0.1891 -0.1772 3   ASN   L OD1 
19569 N  ND2 . ASN   L  3   ? 1.4494 0.6191 1.2464 -0.1202 -0.2873 -0.2910 3   ASN   L ND2 
19570 N  N   . PRO   L  4   ? 1.4359 0.4753 1.1858 -0.0251 -0.2727 -0.1734 4   PRO   L N   
19571 C  CA  . PRO   L  4   ? 1.4473 0.4302 1.1562 -0.0159 -0.2846 -0.1265 4   PRO   L CA  
19572 C  C   . PRO   L  4   ? 1.4475 0.4379 1.1910 0.0041  -0.3047 -0.0989 4   PRO   L C   
19573 O  O   . PRO   L  4   ? 1.4836 0.4388 1.1604 0.0043  -0.2951 -0.1003 4   PRO   L O   
19574 C  CB  . PRO   L  4   ? 1.4114 0.4306 1.1391 -0.0106 -0.2738 -0.1339 4   PRO   L CB  
19575 C  CG  . PRO   L  4   ? 1.4460 0.4014 1.1472 -0.0276 -0.2755 -0.1589 4   PRO   L CG  
19576 C  CD  . PRO   L  4   ? 1.4560 0.4309 1.1275 -0.0206 -0.3006 -0.1592 4   PRO   L CD  
19577 N  N   . TYR   L  5   ? 1.4756 0.4596 1.1876 0.0284  -0.2934 -0.1199 5   TYR   L N   
19578 C  CA  . TYR   L  5   ? 1.4737 0.5005 1.2058 0.0426  -0.2945 -0.1331 5   TYR   L CA  
19579 C  C   . TYR   L  5   ? 1.4826 0.5390 1.2598 0.0810  -0.3033 -0.0580 5   TYR   L C   
19580 O  O   . TYR   L  5   ? 1.5805 0.4676 1.3312 0.1184  -0.3069 -0.0713 5   TYR   L O   
19581 C  CB  . TYR   L  5   ? 1.4960 0.5011 1.2185 0.0442  -0.2684 -0.1504 5   TYR   L CB  
19582 C  CG  . TYR   L  5   ? 1.4877 0.4143 1.2092 0.0821  -0.2876 -0.1895 5   TYR   L CG  
19583 C  CD1 . TYR   L  5   ? 1.4730 0.3779 1.1570 0.0610  -0.3041 -0.2388 5   TYR   L CD1 
19584 C  CD2 . TYR   L  5   ? 1.4967 0.3909 1.2028 0.0610  -0.2807 -0.1996 5   TYR   L CD2 
19585 C  CE1 . TYR   L  5   ? 1.4843 0.3903 1.1422 0.0193  -0.2864 -0.2560 5   TYR   L CE1 
19586 C  CE2 . TYR   L  5   ? 1.4876 0.3602 1.1653 0.0370  -0.2912 -0.2359 5   TYR   L CE2 
19587 C  CZ  . TYR   L  5   ? 1.4748 0.3903 1.1635 0.0474  -0.2924 -0.2855 5   TYR   L CZ  
19588 O  OH  . TYR   L  5   ? 1.5442 0.4437 1.1182 -0.0294 -0.2721 -0.3196 5   TYR   L OH  
19589 N  N   . GLY   L  6   ? 1.4706 0.5516 1.2790 0.1027  -0.3200 0.0210  6   GLY   L N   
19590 C  CA  . GLY   L  6   ? 1.4650 0.5362 1.3181 0.1248  -0.3470 0.0782  6   GLY   L CA  
19591 C  C   . GLY   L  6   ? 1.4646 0.5169 1.3386 0.1312  -0.3635 0.1331  6   GLY   L C   
19592 O  O   . GLY   L  6   ? 1.4650 0.6105 1.3604 0.1314  -0.3889 0.1782  6   GLY   L O   
19593 N  N   . ASP   L  7   ? 1.4879 0.4913 1.3740 0.1498  -0.3428 0.1320  7   ASP   L N   
19594 C  CA  . ASP   L  7   ? 1.4609 0.5319 1.3672 0.1538  -0.3368 0.1781  7   ASP   L CA  
19595 C  C   . ASP   L  7   ? 1.4651 0.5013 1.3798 0.1404  -0.3180 0.1048  7   ASP   L C   
19596 O  O   . ASP   L  7   ? 1.4746 0.6124 1.2889 0.0991  -0.2519 0.1252  7   ASP   L O   
19597 C  CB  . ASP   L  7   ? 1.4714 0.5996 1.3923 0.1677  -0.3212 0.1440  7   ASP   L CB  
19598 C  CG  . ASP   L  7   ? 1.4782 0.6660 1.4472 0.1345  -0.3348 0.1566  7   ASP   L CG  
19599 O  OD1 . ASP   L  7   ? 1.4890 0.7032 1.5613 0.1564  -0.2512 0.1306  7   ASP   L OD1 
19600 O  OD2 . ASP   L  7   ? 1.4921 0.5101 1.5370 0.1490  -0.3383 0.2353  7   ASP   L OD2 
19601 N  N   . ASN   L  8   ? 1.5326 0.3633 1.3327 0.1189  -0.3171 0.1531  8   ASN   L N   
19602 C  CA  . ASN   L  8   ? 1.5671 0.3741 1.3634 0.0893  -0.2931 0.1253  8   ASN   L CA  
19603 C  C   . ASN   L  8   ? 1.5603 0.2525 1.4410 0.1110  -0.2837 0.1213  8   ASN   L C   
19604 O  O   . ASN   L  8   ? 1.6149 0.1766 1.4552 0.1324  -0.2280 0.1071  8   ASN   L O   
19605 C  CB  . ASN   L  8   ? 1.5960 0.3896 1.3491 0.0422  -0.3036 0.0703  8   ASN   L CB  
19606 C  CG  . ASN   L  8   ? 1.6469 0.3924 1.3713 -0.0249 -0.3008 0.0593  8   ASN   L CG  
19607 O  OD1 . ASN   L  8   ? 1.6607 0.3944 1.3654 -0.0442 -0.3345 0.0689  8   ASN   L OD1 
19608 N  ND2 . ASN   L  8   ? 1.6928 0.3796 1.3444 -0.0649 -0.3032 0.0318  8   ASN   L ND2 
19609 N  N   . GLY   L  9   ? 1.5601 0.3668 1.4319 0.1494  -0.2868 0.1102  9   GLY   L N   
19610 C  CA  . GLY   L  9   ? 1.5174 0.4919 1.4420 0.1454  -0.3279 0.1101  9   GLY   L CA  
19611 C  C   . GLY   L  9   ? 1.4667 0.5848 1.4666 0.1376  -0.3319 0.0956  9   GLY   L C   
19612 O  O   . GLY   L  9   ? 1.4712 0.6152 1.4466 0.1246  -0.3254 0.1319  9   GLY   L O   
19613 N  N   . GLY   L  10  ? 1.4548 0.5862 1.4931 0.1436  -0.3095 0.0958  10  GLY   L N   
19614 C  CA  . GLY   L  10  ? 1.4261 0.6067 1.4897 0.1644  -0.2512 0.0719  10  GLY   L CA  
19615 C  C   . GLY   L  10  ? 1.4317 0.5962 1.4774 0.1675  -0.2242 0.0681  10  GLY   L C   
19616 O  O   . GLY   L  10  ? 1.4609 0.5377 1.3850 0.2078  -0.2377 0.0413  10  GLY   L O   
19617 N  N   . THR   L  11  ? 1.4293 0.6263 1.4379 0.1108  -0.2325 0.0935  11  THR   L N   
19618 C  CA  . THR   L  11  ? 1.5220 0.6297 1.4319 0.0833  -0.2018 0.1117  11  THR   L CA  
19619 C  C   . THR   L  11  ? 1.5596 0.5997 1.4760 0.0877  -0.2232 0.1267  11  THR   L C   
19620 O  O   . THR   L  11  ? 1.5413 0.5553 1.4480 0.1075  -0.2288 0.2279  11  THR   L O   
19621 C  CB  . THR   L  11  ? 1.5936 0.6564 1.4346 0.0197  -0.1643 0.1060  11  THR   L CB  
19622 O  OG1 . THR   L  11  ? 1.6180 0.7056 1.4337 0.0513  -0.1421 0.0967  11  THR   L OG1 
19623 C  CG2 . THR   L  11  ? 1.6310 0.6483 1.4823 -0.0330 -0.1636 0.1116  11  THR   L CG2 
19624 N  N   . ILE   L  12  ? 1.5451 0.5704 1.4854 0.1212  -0.2518 0.1182  12  ILE   L N   
19625 C  CA  . ILE   L  12  ? 1.5054 0.5431 1.5222 0.0978  -0.2782 0.0789  12  ILE   L CA  
19626 C  C   . ILE   L  12  ? 1.4436 0.5866 1.5414 0.1383  -0.3323 0.1078  12  ILE   L C   
19627 O  O   . ILE   L  12  ? 1.3952 0.5921 1.4491 0.0769  -0.3948 0.0638  12  ILE   L O   
19628 C  CB  . ILE   L  12  ? 1.5557 0.4540 1.5699 0.1592  -0.2296 0.0918  12  ILE   L CB  
19629 C  CG1 . ILE   L  12  ? 1.5653 0.4219 1.5273 0.1662  -0.2331 0.1002  12  ILE   L CG1 
19630 C  CG2 . ILE   L  12  ? 1.5656 0.4301 1.5766 0.1623  -0.1924 0.0725  12  ILE   L CG2 
19631 C  CD1 . ILE   L  12  ? 1.5563 0.4484 1.5085 0.1595  -0.2403 0.1702  12  ILE   L CD1 
19632 N  N   . LEU   L  13  ? 1.4752 0.6223 1.5490 0.1589  -0.3567 0.1294  13  LEU   L N   
19633 C  CA  . LEU   L  13  ? 1.5077 0.6758 1.5704 0.1616  -0.3745 0.1294  13  LEU   L CA  
19634 C  C   . LEU   L  13  ? 1.5364 0.6650 1.5432 0.1749  -0.3466 0.1158  13  LEU   L C   
19635 O  O   . LEU   L  13  ? 1.6006 0.6638 1.5838 0.1728  -0.3463 0.0317  13  LEU   L O   
19636 C  CB  . LEU   L  13  ? 1.5184 0.6311 1.6293 0.1800  -0.4172 0.1284  13  LEU   L CB  
19637 C  CG  . LEU   L  13  ? 1.5550 0.6153 1.6125 0.1487  -0.4501 0.1005  13  LEU   L CG  
19638 C  CD1 . LEU   L  13  ? 1.5502 0.6054 1.5981 0.1545  -0.4643 0.0443  13  LEU   L CD1 
19639 C  CD2 . LEU   L  13  ? 1.5705 0.6108 1.6486 0.1384  -0.4525 0.0929  13  LEU   L CD2 
19640 N  N   . GLY   L  14  ? 1.5073 0.5794 1.5643 0.1814  -0.3276 0.1238  14  GLY   L N   
19641 C  CA  . GLY   L  14  ? 1.5050 0.5349 1.5447 0.1297  -0.3067 0.1563  14  GLY   L CA  
19642 C  C   . GLY   L  14  ? 1.4913 0.5143 1.5392 0.1484  -0.3112 0.1816  14  GLY   L C   
19643 O  O   . GLY   L  14  ? 1.4845 0.4653 1.5231 0.1001  -0.2640 0.2665  14  GLY   L O   
19644 N  N   . ILE   L  15  ? 1.4925 0.5480 1.5916 0.1684  -0.3718 0.1526  15  ILE   L N   
19645 C  CA  . ILE   L  15  ? 1.5149 0.6070 1.6456 0.1406  -0.4006 0.0721  15  ILE   L CA  
19646 C  C   . ILE   L  15  ? 1.5269 0.5415 1.6852 0.0969  -0.4171 0.0160  15  ILE   L C   
19647 O  O   . ILE   L  15  ? 1.4895 0.4332 1.7760 0.0536  -0.4072 -0.0143 15  ILE   L O   
19648 C  CB  . ILE   L  15  ? 1.5165 0.6143 1.6392 0.1337  -0.4195 0.0745  15  ILE   L CB  
19649 C  CG1 . ILE   L  15  ? 1.5063 0.6845 1.6532 0.1903  -0.4232 0.0663  15  ILE   L CG1 
19650 C  CG2 . ILE   L  15  ? 1.5630 0.5900 1.6260 0.1503  -0.4387 0.0882  15  ILE   L CG2 
19651 C  CD1 . ILE   L  15  ? 1.4804 0.8021 1.6775 0.1443  -0.4039 0.0637  15  ILE   L CD1 
19652 N  N   . ALA   L  16  ? 1.5668 0.4913 1.6395 0.0763  -0.4292 -0.0679 16  ALA   L N   
19653 C  CA  . ALA   L  16  ? 1.5902 0.4799 1.6331 0.0684  -0.4379 -0.0744 16  ALA   L CA  
19654 C  C   . ALA   L  16  ? 1.6582 0.5192 1.6684 0.0524  -0.4831 -0.1477 16  ALA   L C   
19655 O  O   . ALA   L  16  ? 1.6779 0.5133 1.7330 0.0996  -0.4432 -0.1852 16  ALA   L O   
19656 C  CB  . ALA   L  16  ? 1.5750 0.5107 1.6041 0.0686  -0.4367 -0.0760 16  ALA   L CB  
19657 N  N   . GLY   L  17  ? 1.6408 0.5994 1.7309 0.0586  -0.4850 -0.1420 17  GLY   L N   
19658 C  CA  . GLY   L  17  ? 1.6481 0.7240 1.8300 0.0514  -0.5097 -0.1698 17  GLY   L CA  
19659 C  C   . GLY   L  17  ? 1.7199 0.8093 1.8400 0.0320  -0.4963 -0.1221 17  GLY   L C   
19660 O  O   . GLY   L  17  ? 1.7099 0.9529 1.9162 -0.0185 -0.4476 -0.1940 17  GLY   L O   
19661 N  N   . GLU   L  18  ? 1.7649 0.9287 1.8415 0.0582  -0.5288 -0.0867 18  GLU   L N   
19662 C  CA  . GLU   L  18  ? 1.8349 0.9514 1.8813 0.0637  -0.4960 -0.0242 18  GLU   L CA  
19663 C  C   . GLU   L  18  ? 1.7753 0.8682 1.8851 0.0396  -0.5012 0.0492  18  GLU   L C   
19664 O  O   . GLU   L  18  ? 1.8197 0.9799 1.9297 -0.0325 -0.4738 0.0869  18  GLU   L O   
19665 C  CB  . GLU   L  18  ? 1.8642 1.0127 1.8724 0.0959  -0.5315 -0.0085 18  GLU   L CB  
19666 C  CG  . GLU   L  18  ? 1.9827 1.1185 1.8511 0.0833  -0.5174 0.0248  18  GLU   L CG  
19667 C  CD  . GLU   L  18  ? 2.0104 1.2204 1.8922 0.0612  -0.5359 0.0233  18  GLU   L CD  
19668 O  OE1 . GLU   L  18  ? 2.0837 1.2819 1.9135 -0.0208 -0.4810 -0.0374 18  GLU   L OE1 
19669 O  OE2 . GLU   L  18  ? 2.1305 1.2044 1.9876 0.1277  -0.4897 0.0621  18  GLU   L OE2 
19670 N  N   . ASP   L  19  ? 1.6892 0.8283 1.9207 0.0311  -0.4777 0.1021  19  ASP   L N   
19671 C  CA  . ASP   L  19  ? 1.6248 0.9069 1.9071 0.0440  -0.4524 0.0604  19  ASP   L CA  
19672 C  C   . ASP   L  19  ? 1.5391 0.8520 1.9240 0.0645  -0.4495 0.0969  19  ASP   L C   
19673 O  O   . ASP   L  19  ? 1.4882 1.0117 1.8730 -0.0154 -0.4260 0.0366  19  ASP   L O   
19674 C  CB  . ASP   L  19  ? 1.6049 1.0176 1.9989 0.0399  -0.4540 0.0459  19  ASP   L CB  
19675 C  CG  . ASP   L  19  ? 1.5523 0.9659 2.0515 0.0447  -0.4552 -0.0043 19  ASP   L CG  
19676 O  OD1 . ASP   L  19  ? 1.5546 0.9616 2.1053 0.1062  -0.4629 0.0755  19  ASP   L OD1 
19677 O  OD2 . ASP   L  19  ? 1.5567 1.1484 2.1181 0.0910  -0.4560 -0.0587 19  ASP   L OD2 
19678 N  N   . PHE   L  20  ? 1.5193 0.8113 1.7891 0.0249  -0.4662 0.1041  20  PHE   L N   
19679 C  CA  . PHE   L  20  ? 1.4937 0.8098 1.7661 0.0440  -0.4337 0.1105  20  PHE   L CA  
19680 C  C   . PHE   L  20  ? 1.4774 0.7641 1.6309 0.0375  -0.4684 0.1109  20  PHE   L C   
19681 O  O   . PHE   L  20  ? 1.3442 0.7008 1.5696 0.1108  -0.5383 0.1752  20  PHE   L O   
19682 C  CB  . PHE   L  20  ? 1.5306 0.8546 1.8085 0.0290  -0.4155 0.1372  20  PHE   L CB  
19683 C  CG  . PHE   L  20  ? 1.5674 0.8100 1.8323 0.0977  -0.4250 0.1903  20  PHE   L CG  
19684 C  CD1 . PHE   L  20  ? 1.5992 0.7692 1.8110 0.1230  -0.4337 0.2067  20  PHE   L CD1 
19685 C  CD2 . PHE   L  20  ? 1.5810 0.8106 1.8560 0.1100  -0.4207 0.1934  20  PHE   L CD2 
19686 C  CE1 . PHE   L  20  ? 1.6361 0.7799 1.8178 0.0902  -0.4371 0.1901  20  PHE   L CE1 
19687 C  CE2 . PHE   L  20  ? 1.6043 0.8493 1.8763 0.0824  -0.4440 0.1460  20  PHE   L CE2 
19688 C  CZ  . PHE   L  20  ? 1.6125 0.8651 1.8465 0.1186  -0.4590 0.1974  20  PHE   L CZ  
19689 N  N   . ALA   L  21  ? 1.4740 0.7347 1.6067 0.0458  -0.4560 0.0651  21  ALA   L N   
19690 C  CA  . ALA   L  21  ? 1.4806 0.6941 1.5616 0.0320  -0.4455 0.0416  21  ALA   L CA  
19691 C  C   . ALA   L  21  ? 1.4891 0.6614 1.5677 0.0299  -0.4408 0.0425  21  ALA   L C   
19692 O  O   . ALA   L  21  ? 1.5497 0.6709 1.6279 0.0452  -0.3987 0.0214  21  ALA   L O   
19693 C  CB  . ALA   L  21  ? 1.4999 0.7118 1.5016 0.0135  -0.4519 0.0548  21  ALA   L CB  
19694 N  N   . VAL   L  22  ? 1.4485 0.6652 1.5647 0.0341  -0.4408 0.0325  22  VAL   L N   
19695 C  CA  . VAL   L  22  ? 1.4754 0.6305 1.5829 0.0485  -0.4236 0.0477  22  VAL   L CA  
19696 C  C   . VAL   L  22  ? 1.4946 0.5461 1.5817 0.0712  -0.4214 0.0552  22  VAL   L C   
19697 O  O   . VAL   L  22  ? 1.5635 0.3958 1.5518 0.1076  -0.4634 0.0200  22  VAL   L O   
19698 C  CB  . VAL   L  22  ? 1.4713 0.6402 1.5852 0.0512  -0.4056 0.0608  22  VAL   L CB  
19699 C  CG1 . VAL   L  22  ? 1.4972 0.6541 1.6162 0.1101  -0.3920 0.0579  22  VAL   L CG1 
19700 C  CG2 . VAL   L  22  ? 1.4803 0.6925 1.5721 0.0739  -0.4113 0.0523  22  VAL   L CG2 
19701 N  N   . LEU   L  23  ? 1.5086 0.5110 1.5720 0.0836  -0.4241 0.0973  23  LEU   L N   
19702 C  CA  . LEU   L  23  ? 1.5061 0.4287 1.5591 0.0864  -0.4147 0.1026  23  LEU   L CA  
19703 C  C   . LEU   L  23  ? 1.5244 0.4288 1.5262 0.0637  -0.4010 0.0720  23  LEU   L C   
19704 O  O   . LEU   L  23  ? 1.5349 0.3224 1.5648 0.0598  -0.4212 0.0440  23  LEU   L O   
19705 C  CB  . LEU   L  23  ? 1.4628 0.4431 1.5682 0.0800  -0.4033 0.1343  23  LEU   L CB  
19706 C  CG  . LEU   L  23  ? 1.4745 0.4492 1.5898 0.1449  -0.3858 0.1526  23  LEU   L CG  
19707 C  CD1 . LEU   L  23  ? 1.4336 0.5664 1.5926 0.1167  -0.3929 0.1283  23  LEU   L CD1 
19708 C  CD2 . LEU   L  23  ? 1.4443 0.4204 1.5965 0.1181  -0.3684 0.1420  23  LEU   L CD2 
19709 N  N   . ALA   L  24  ? 1.5548 0.4126 1.5273 -0.0039 -0.3895 0.0511  24  ALA   L N   
19710 C  CA  . ALA   L  24  ? 1.5546 0.4205 1.5097 0.0143  -0.4055 0.0548  24  ALA   L CA  
19711 C  C   . ALA   L  24  ? 1.5627 0.2587 1.4227 -0.0125 -0.4120 0.0598  24  ALA   L C   
19712 O  O   . ALA   L  24  ? 1.5423 0.2009 1.3297 -0.0166 -0.4650 0.0903  24  ALA   L O   
19713 C  CB  . ALA   L  24  ? 1.5613 0.4455 1.5376 -0.0038 -0.4123 0.0629  24  ALA   L CB  
19714 N  N   . GLY   L  25  ? 1.5919 0.3499 1.3952 -0.0007 -0.3742 0.0287  25  GLY   L N   
19715 C  CA  . GLY   L  25  ? 1.5926 0.4503 1.3980 0.0496  -0.3490 0.0255  25  GLY   L CA  
19716 C  C   . GLY   L  25  ? 1.6169 0.5393 1.4123 0.0925  -0.3303 0.0652  25  GLY   L C   
19717 O  O   . GLY   L  25  ? 1.6047 0.6882 1.4482 0.1479  -0.2836 0.1442  25  GLY   L O   
19718 N  N   . ASP   L  26  ? 1.6443 0.4767 1.4663 0.0720  -0.2888 -0.0070 26  ASP   L N   
19719 C  CA  . ASP   L  26  ? 1.6343 0.5603 1.5053 0.0199  -0.2564 0.0367  26  ASP   L CA  
19720 C  C   . ASP   L  26  ? 1.5756 0.5266 1.4872 0.0614  -0.2355 0.0359  26  ASP   L C   
19721 O  O   . ASP   L  26  ? 1.5751 0.6525 1.5030 0.0198  -0.1911 0.0316  26  ASP   L O   
19722 C  CB  . ASP   L  26  ? 1.6786 0.5642 1.5556 0.0258  -0.2709 0.0699  26  ASP   L CB  
19723 C  CG  . ASP   L  26  ? 1.6912 0.7040 1.5918 -0.0603 -0.2571 0.0837  26  ASP   L CG  
19724 O  OD1 . ASP   L  26  ? 1.7521 0.7206 1.6072 -0.0998 -0.2802 0.0941  26  ASP   L OD1 
19725 O  OD2 . ASP   L  26  ? 1.7167 0.6355 1.6315 -0.0852 -0.2194 0.1023  26  ASP   L OD2 
19726 N  N   . THR   L  27  ? 1.4799 0.5231 1.5191 0.0398  -0.2154 0.0555  27  THR   L N   
19727 C  CA  . THR   L  27  ? 1.4417 0.6129 1.5034 0.0191  -0.2273 0.0582  27  THR   L CA  
19728 C  C   . THR   L  27  ? 1.4699 0.5747 1.5176 0.0301  -0.2322 0.0703  27  THR   L C   
19729 O  O   . THR   L  27  ? 1.4173 0.5994 1.5080 0.0562  -0.2862 0.1139  27  THR   L O   
19730 C  CB  . THR   L  27  ? 1.4075 0.6841 1.5497 -0.0505 -0.2020 0.0580  27  THR   L CB  
19731 O  OG1 . THR   L  27  ? 1.3882 0.6749 1.5526 -0.0669 -0.2183 0.0311  27  THR   L OG1 
19732 C  CG2 . THR   L  27  ? 1.3866 0.6860 1.5528 -0.0535 -0.2094 0.0400  27  THR   L CG2 
19733 N  N   . ARG   L  28  ? 1.4625 0.5492 1.5077 0.0318  -0.2591 0.0947  28  ARG   L N   
19734 C  CA  . ARG   L  28  ? 1.4402 0.6090 1.5321 0.0310  -0.2570 0.1182  28  ARG   L CA  
19735 C  C   . ARG   L  28  ? 1.4697 0.4805 1.4729 0.0277  -0.2677 0.1468  28  ARG   L C   
19736 O  O   . ARG   L  28  ? 1.4129 0.3795 1.4889 0.0086  -0.3658 0.2508  28  ARG   L O   
19737 C  CB  . ARG   L  28  ? 1.4826 0.6412 1.5866 0.0605  -0.2311 0.0701  28  ARG   L CB  
19738 C  CG  . ARG   L  28  ? 1.4910 0.7739 1.5708 0.0923  -0.2354 0.1031  28  ARG   L CG  
19739 C  CD  . ARG   L  28  ? 1.4887 0.7755 1.5706 0.1229  -0.2309 0.1005  28  ARG   L CD  
19740 N  NE  . ARG   L  28  ? 1.4913 0.8161 1.5808 0.1190  -0.2102 0.1050  28  ARG   L NE  
19741 C  CZ  . ARG   L  28  ? 1.5679 0.8796 1.6165 0.0806  -0.2089 0.0221  28  ARG   L CZ  
19742 N  NH1 . ARG   L  28  ? 1.5926 1.0557 1.5862 0.0942  -0.1608 0.0267  28  ARG   L NH1 
19743 N  NH2 . ARG   L  28  ? 1.5555 1.0808 1.6054 0.0945  -0.1660 0.0202  28  ARG   L NH2 
19744 N  N   . ASN   L  29  ? 1.5030 0.4632 1.4714 0.0134  -0.2632 0.0672  29  ASN   L N   
19745 C  CA  . ASN   L  29  ? 1.5015 0.4471 1.4182 0.0254  -0.2952 0.0739  29  ASN   L CA  
19746 C  C   . ASN   L  29  ? 1.5382 0.4125 1.2843 -0.0082 -0.3127 0.0636  29  ASN   L C   
19747 O  O   . ASN   L  29  ? 1.5506 0.2627 1.2519 0.0268  -0.3859 0.0837  29  ASN   L O   
19748 C  CB  . ASN   L  29  ? 1.5495 0.4757 1.4443 0.0415  -0.2713 0.0409  29  ASN   L CB  
19749 C  CG  . ASN   L  29  ? 1.5004 0.5337 1.4779 0.0829  -0.3142 0.0654  29  ASN   L CG  
19750 O  OD1 . ASN   L  29  ? 1.6006 0.3945 1.4475 0.1161  -0.3028 0.1417  29  ASN   L OD1 
19751 N  ND2 . ASN   L  29  ? 1.6062 0.5335 1.5235 -0.0050 -0.2782 0.0557  29  ASN   L ND2 
19752 N  N   . ILE   L  30  ? 1.5439 0.4206 1.2997 -0.0181 -0.3080 0.0390  30  ILE   L N   
19753 C  CA  . ILE   L  30  ? 1.5576 0.4238 1.3184 -0.0150 -0.2595 0.0786  30  ILE   L CA  
19754 C  C   . ILE   L  30  ? 1.5466 0.4854 1.3259 -0.0299 -0.2805 -0.0117 30  ILE   L C   
19755 O  O   . ILE   L  30  ? 1.5232 0.4832 1.2989 -0.0257 -0.2702 -0.0352 30  ILE   L O   
19756 C  CB  . ILE   L  30  ? 1.6195 0.4016 1.3102 -0.0036 -0.2316 0.0875  30  ILE   L CB  
19757 C  CG1 . ILE   L  30  ? 1.6619 0.3882 1.3008 0.0404  -0.2371 0.1095  30  ILE   L CG1 
19758 C  CG2 . ILE   L  30  ? 1.6072 0.4274 1.3533 -0.0065 -0.2566 0.1013  30  ILE   L CG2 
19759 C  CD1 . ILE   L  30  ? 1.6796 0.3842 1.2875 0.0527  -0.2333 0.0869  30  ILE   L CD1 
19760 N  N   . THR   L  31  ? 1.5509 0.5827 1.2684 -0.0480 -0.2970 0.0105  31  THR   L N   
19761 C  CA  . THR   L  31  ? 1.5741 0.6472 1.2585 -0.0467 -0.2878 -0.0530 31  THR   L CA  
19762 C  C   . THR   L  31  ? 1.6661 0.6452 1.2418 -0.0372 -0.2666 -0.0395 31  THR   L C   
19763 O  O   . THR   L  31  ? 1.6960 0.4964 1.2098 -0.0094 -0.2390 -0.1047 31  THR   L O   
19764 C  CB  . THR   L  31  ? 1.5736 0.7339 1.2152 -0.0725 -0.2903 -0.0552 31  THR   L CB  
19765 O  OG1 . THR   L  31  ? 1.5817 0.7806 1.2227 -0.1839 -0.2687 -0.0995 31  THR   L OG1 
19766 C  CG2 . THR   L  31  ? 1.4951 0.7163 1.2119 -0.0623 -0.3463 -0.1034 31  THR   L CG2 
19767 N  N   . ASP   L  32  ? 1.6569 0.6503 1.3009 -0.0064 -0.2763 -0.0752 32  ASP   L N   
19768 C  CA  . ASP   L  32  ? 1.6299 0.6663 1.3047 0.0254  -0.2978 -0.0277 32  ASP   L CA  
19769 C  C   . ASP   L  32  ? 1.6555 0.6762 1.3331 0.0000  -0.2992 -0.0039 32  ASP   L C   
19770 O  O   . ASP   L  32  ? 1.6018 0.5827 1.3537 0.0171  -0.2574 0.0677  32  ASP   L O   
19771 C  CB  . ASP   L  32  ? 1.6749 0.7558 1.3076 0.0969  -0.3085 -0.0449 32  ASP   L CB  
19772 C  CG  . ASP   L  32  ? 1.6699 0.7562 1.3104 0.1355  -0.2562 -0.0387 32  ASP   L CG  
19773 O  OD1 . ASP   L  32  ? 1.6953 0.6671 1.2193 0.2384  -0.3484 -0.0943 32  ASP   L OD1 
19774 O  OD2 . ASP   L  32  ? 1.7295 0.9103 1.3428 0.1932  -0.2795 -0.1183 32  ASP   L OD2 
19775 N  N   . TYR   L  33  ? 1.6253 0.6805 1.3186 -0.0002 -0.3288 -0.0074 33  TYR   L N   
19776 C  CA  . TYR   L  33  ? 1.6117 0.7284 1.2853 -0.0062 -0.3211 0.0019  33  TYR   L CA  
19777 C  C   . TYR   L  33  ? 1.6128 0.6356 1.2318 -0.0400 -0.3257 0.0473  33  TYR   L C   
19778 O  O   . TYR   L  33  ? 1.6037 0.7521 1.2672 -0.1270 -0.3218 0.0095  33  TYR   L O   
19779 C  CB  . TYR   L  33  ? 1.6102 0.7725 1.3235 0.0462  -0.3389 -0.0204 33  TYR   L CB  
19780 C  CG  . TYR   L  33  ? 1.6235 0.8104 1.3685 0.0501  -0.3776 -0.0931 33  TYR   L CG  
19781 C  CD1 . TYR   L  33  ? 1.5920 0.7381 1.4015 0.0442  -0.3446 -0.1099 33  TYR   L CD1 
19782 C  CD2 . TYR   L  33  ? 1.6398 0.8872 1.3857 0.1019  -0.3606 -0.1556 33  TYR   L CD2 
19783 C  CE1 . TYR   L  33  ? 1.6204 0.7246 1.4320 0.0289  -0.3932 -0.1756 33  TYR   L CE1 
19784 C  CE2 . TYR   L  33  ? 1.6232 0.8735 1.4038 0.0680  -0.3948 -0.2016 33  TYR   L CE2 
19785 C  CZ  . TYR   L  33  ? 1.6433 0.7960 1.4298 0.0388  -0.3671 -0.2219 33  TYR   L CZ  
19786 O  OH  . TYR   L  33  ? 1.6755 0.9072 1.4412 -0.0293 -0.3698 -0.2875 33  TYR   L OH  
19787 N  N   . SER   L  34  ? 1.5628 0.6171 1.2000 -0.0365 -0.3281 0.0770  34  SER   L N   
19788 C  CA  . SER   L  34  ? 1.5400 0.5243 1.2075 -0.0574 -0.3312 0.0823  34  SER   L CA  
19789 C  C   . SER   L  34  ? 1.5123 0.5476 1.2223 -0.0312 -0.3299 0.0313  34  SER   L C   
19790 O  O   . SER   L  34  ? 1.5548 0.5170 1.1436 -0.0117 -0.4215 0.0106  34  SER   L O   
19791 C  CB  . SER   L  34  ? 1.5215 0.4731 1.2042 -0.0906 -0.2964 0.0861  34  SER   L CB  
19792 O  OG  . SER   L  34  ? 1.4967 0.4811 1.2146 -0.1410 -0.2784 0.1249  34  SER   L OG  
19793 N  N   . ILE   L  35  ? 1.5197 0.5805 1.2630 -0.0319 -0.2963 0.0561  35  ILE   L N   
19794 C  CA  . ILE   L  35  ? 1.5067 0.6010 1.3057 -0.0238 -0.2688 0.0981  35  ILE   L CA  
19795 C  C   . ILE   L  35  ? 1.4724 0.5560 1.2945 -0.0120 -0.2533 0.1207  35  ILE   L C   
19796 O  O   . ILE   L  35  ? 1.4513 0.5079 1.2679 -0.0314 -0.2258 0.0622  35  ILE   L O   
19797 C  CB  . ILE   L  35  ? 1.5176 0.6609 1.3915 -0.0360 -0.2577 0.1242  35  ILE   L CB  
19798 C  CG1 . ILE   L  35  ? 1.5430 0.5989 1.4350 -0.0171 -0.2472 0.1300  35  ILE   L CG1 
19799 C  CG2 . ILE   L  35  ? 1.5067 0.7434 1.4359 0.0048  -0.2341 0.0905  35  ILE   L CG2 
19800 C  CD1 . ILE   L  35  ? 1.5479 0.6639 1.4801 -0.0403 -0.2481 0.1376  35  ILE   L CD1 
19801 N  N   . ASN   L  36  ? 1.4917 0.5045 1.3449 0.0010  -0.2468 0.0768  36  ASN   L N   
19802 C  CA  . ASN   L  36  ? 1.5010 0.4489 1.3581 0.0098  -0.2414 0.1124  36  ASN   L CA  
19803 C  C   . ASN   L  36  ? 1.5139 0.3681 1.3632 -0.0215 -0.1995 0.1161  36  ASN   L C   
19804 O  O   . ASN   L  36  ? 1.5177 0.2716 1.3893 -0.0577 -0.1456 0.0782  36  ASN   L O   
19805 C  CB  . ASN   L  36  ? 1.4854 0.4677 1.3431 0.0192  -0.2393 0.1178  36  ASN   L CB  
19806 C  CG  . ASN   L  36  ? 1.5012 0.4108 1.3201 0.0766  -0.2857 0.1403  36  ASN   L CG  
19807 O  OD1 . ASN   L  36  ? 1.5089 0.3751 1.3898 0.1136  -0.2861 0.1235  36  ASN   L OD1 
19808 N  ND2 . ASN   L  36  ? 1.5358 0.5121 1.2844 0.0674  -0.2556 0.0781  36  ASN   L ND2 
19809 N  N   . SER   L  37  ? 1.4775 0.3590 1.4491 -0.0097 -0.2213 0.1524  37  SER   L N   
19810 C  CA  . SER   L  37  ? 1.4384 0.4855 1.4468 -0.0301 -0.2352 0.1302  37  SER   L CA  
19811 C  C   . SER   L  37  ? 1.4694 0.3920 1.4564 -0.0438 -0.2481 0.1542  37  SER   L C   
19812 O  O   . SER   L  37  ? 1.4265 0.3735 1.4421 -0.1043 -0.2909 0.1093  37  SER   L O   
19813 C  CB  . SER   L  37  ? 1.4718 0.4881 1.4786 0.0004  -0.1917 0.1326  37  SER   L CB  
19814 O  OG  . SER   L  37  ? 1.4802 0.5643 1.5107 0.0170  -0.1688 0.1290  37  SER   L OG  
19815 N  N   . ARG   L  38  ? 1.4472 0.4063 1.4316 -0.0226 -0.2685 0.1388  38  ARG   L N   
19816 C  CA  . ARG   L  38  ? 1.4656 0.5021 1.4502 0.0065  -0.2835 0.0562  38  ARG   L CA  
19817 C  C   . ARG   L  38  ? 1.4695 0.5093 1.4679 0.0693  -0.2783 -0.0029 38  ARG   L C   
19818 O  O   . ARG   L  38  ? 1.4576 0.2893 1.5325 0.1397  -0.3146 -0.0463 38  ARG   L O   
19819 C  CB  . ARG   L  38  ? 1.4391 0.5990 1.4483 -0.0151 -0.2822 0.0578  38  ARG   L CB  
19820 C  CG  . ARG   L  38  ? 1.4338 0.6315 1.4390 -0.0050 -0.3098 0.0562  38  ARG   L CG  
19821 C  CD  . ARG   L  38  ? 1.4527 0.6588 1.4770 -0.0102 -0.2900 0.0756  38  ARG   L CD  
19822 N  NE  . ARG   L  38  ? 1.4616 0.7230 1.4959 0.0229  -0.3282 0.0867  38  ARG   L NE  
19823 C  CZ  . ARG   L  38  ? 1.4659 0.7048 1.5401 0.0582  -0.3489 0.1122  38  ARG   L CZ  
19824 N  NH1 . ARG   L  38  ? 1.5003 0.6786 1.5433 0.0958  -0.3454 0.1174  38  ARG   L NH1 
19825 N  NH2 . ARG   L  38  ? 1.4479 0.6886 1.5412 0.0254  -0.3541 0.1171  38  ARG   L NH2 
19826 N  N   . TYR   L  39  ? 1.4849 0.5997 1.4315 0.0523  -0.2589 -0.0867 39  TYR   L N   
19827 C  CA  . TYR   L  39  ? 1.4984 0.6313 1.4152 0.0744  -0.2802 -0.0966 39  TYR   L CA  
19828 C  C   . TYR   L  39  ? 1.4764 0.6656 1.4011 0.0673  -0.2325 -0.1184 39  TYR   L C   
19829 O  O   . TYR   L  39  ? 1.4744 0.7677 1.4424 0.1069  -0.1999 -0.1828 39  TYR   L O   
19830 C  CB  . TYR   L  39  ? 1.5128 0.6702 1.4145 0.0608  -0.2766 -0.1303 39  TYR   L CB  
19831 C  CG  . TYR   L  39  ? 1.5528 0.6828 1.4195 0.0781  -0.2846 -0.1320 39  TYR   L CG  
19832 C  CD1 . TYR   L  39  ? 1.5705 0.7182 1.4429 0.0870  -0.3100 -0.1237 39  TYR   L CD1 
19833 C  CD2 . TYR   L  39  ? 1.5425 0.6833 1.3983 0.0851  -0.2569 -0.1289 39  TYR   L CD2 
19834 C  CE1 . TYR   L  39  ? 1.5441 0.6948 1.4671 0.0982  -0.3087 -0.1568 39  TYR   L CE1 
19835 C  CE2 . TYR   L  39  ? 1.5199 0.6858 1.4217 0.0875  -0.2690 -0.1383 39  TYR   L CE2 
19836 C  CZ  . TYR   L  39  ? 1.5100 0.6973 1.4636 0.0930  -0.3020 -0.1608 39  TYR   L CZ  
19837 O  OH  . TYR   L  39  ? 1.4620 0.8164 1.4674 0.1200  -0.3924 -0.1575 39  TYR   L OH  
19838 N  N   . GLU   L  40  ? 1.5334 0.6175 1.3644 0.0694  -0.2344 -0.0950 40  GLU   L N   
19839 C  CA  . GLU   L  40  ? 1.6193 0.5669 1.3771 0.0803  -0.2062 -0.0571 40  GLU   L CA  
19840 C  C   . GLU   L  40  ? 1.5614 0.5915 1.3626 0.0901  -0.1718 -0.0588 40  GLU   L C   
19841 O  O   . GLU   L  40  ? 1.5774 0.6056 1.3742 0.0417  -0.1436 -0.0786 40  GLU   L O   
19842 C  CB  . GLU   L  40  ? 1.6499 0.5314 1.4124 0.1006  -0.2096 -0.0538 40  GLU   L CB  
19843 C  CG  . GLU   L  40  ? 1.7375 0.5551 1.4675 0.0650  -0.1767 -0.0468 40  GLU   L CG  
19844 C  CD  . GLU   L  40  ? 1.8768 0.6621 1.4555 0.0530  -0.1587 -0.0857 40  GLU   L CD  
19845 O  OE1 . GLU   L  40  ? 2.0301 0.5748 1.4197 0.0595  -0.1994 -0.0814 40  GLU   L OE1 
19846 O  OE2 . GLU   L  40  ? 1.9453 0.6764 1.5901 -0.0650 -0.1777 -0.1444 40  GLU   L OE2 
19847 N  N   . PRO   L  41  ? 1.5498 0.6821 1.3984 0.1276  -0.1288 0.0442  41  PRO   L N   
19848 C  CA  . PRO   L  41  ? 1.5467 0.6097 1.4268 0.1281  -0.1091 0.1051  41  PRO   L CA  
19849 C  C   . PRO   L  41  ? 1.5341 0.5732 1.3924 0.1482  -0.1509 0.1677  41  PRO   L C   
19850 O  O   . PRO   L  41  ? 1.4973 0.6542 1.4126 0.0999  -0.1508 0.2122  41  PRO   L O   
19851 C  CB  . PRO   L  41  ? 1.5628 0.6459 1.4344 0.1567  -0.0791 0.1392  41  PRO   L CB  
19852 C  CG  . PRO   L  41  ? 1.5730 0.7313 1.4469 0.1655  -0.0545 0.1365  41  PRO   L CG  
19853 C  CD  . PRO   L  41  ? 1.5426 0.7747 1.4200 0.1536  -0.0720 0.0619  41  PRO   L CD  
19854 N  N   . LYS   L  42  ? 1.5200 0.5374 1.3946 0.1820  -0.1979 0.1578  42  LYS   L N   
19855 C  CA  . LYS   L  42  ? 1.4686 0.5623 1.3949 0.2221  -0.1896 0.1222  42  LYS   L CA  
19856 C  C   . LYS   L  42  ? 1.4856 0.5405 1.4085 0.2296  -0.1927 0.1272  42  LYS   L C   
19857 O  O   . LYS   L  42  ? 1.5803 0.3668 1.3524 0.2555  -0.1910 0.1377  42  LYS   L O   
19858 C  CB  . LYS   L  42  ? 1.4440 0.5364 1.4046 0.2272  -0.2239 0.1676  42  LYS   L CB  
19859 C  CG  . LYS   L  42  ? 1.4672 0.5609 1.4432 0.1791  -0.2471 0.1786  42  LYS   L CG  
19860 C  CD  . LYS   L  42  ? 1.4618 0.5748 1.4929 0.1944  -0.2293 0.1108  42  LYS   L CD  
19861 C  CE  . LYS   L  42  ? 1.4789 0.6268 1.5332 0.1728  -0.2343 0.0810  42  LYS   L CE  
19862 N  NZ  . LYS   L  42  ? 1.4935 0.6115 1.5701 0.1811  -0.2244 0.0902  42  LYS   L NZ  
19863 N  N   . VAL   L  43  ? 1.4753 0.5458 1.4029 0.2261  -0.2557 0.1584  43  VAL   L N   
19864 C  CA  . VAL   L  43  ? 1.4166 0.6051 1.4215 0.1768  -0.2850 0.1851  43  VAL   L CA  
19865 C  C   . VAL   L  43  ? 1.4023 0.5997 1.4093 0.1575  -0.2838 0.1963  43  VAL   L C   
19866 O  O   . VAL   L  43  ? 1.3898 0.6872 1.4420 0.0748  -0.2904 0.3304  43  VAL   L O   
19867 C  CB  . VAL   L  43  ? 1.3997 0.5719 1.4337 0.2214  -0.3056 0.1710  43  VAL   L CB  
19868 C  CG1 . VAL   L  43  ? 1.4335 0.5991 1.4478 0.1979  -0.3126 0.2032  43  VAL   L CG1 
19869 C  CG2 . VAL   L  43  ? 1.4071 0.5828 1.4492 0.2471  -0.3143 0.1699  43  VAL   L CG2 
19870 N  N   . PHE   L  44  ? 1.4231 0.5657 1.4307 0.1263  -0.3015 0.1483  44  PHE   L N   
19871 C  CA  . PHE   L  44  ? 1.4225 0.5808 1.4564 0.1126  -0.2834 0.1091  44  PHE   L CA  
19872 C  C   . PHE   L  44  ? 1.3852 0.4640 1.4891 0.1033  -0.2830 0.0625  44  PHE   L C   
19873 O  O   . PHE   L  44  ? 1.3567 0.2453 1.4636 0.1084  -0.3280 0.0693  44  PHE   L O   
19874 C  CB  . PHE   L  44  ? 1.4491 0.5663 1.3860 0.1006  -0.2684 0.0843  44  PHE   L CB  
19875 C  CG  . PHE   L  44  ? 1.4686 0.6005 1.3313 0.1307  -0.2639 0.0509  44  PHE   L CG  
19876 C  CD1 . PHE   L  44  ? 1.5039 0.6553 1.3394 0.1361  -0.2442 0.0311  44  PHE   L CD1 
19877 C  CD2 . PHE   L  44  ? 1.4601 0.6226 1.2960 0.1152  -0.2529 0.0163  44  PHE   L CD2 
19878 C  CE1 . PHE   L  44  ? 1.4888 0.6539 1.2760 0.1237  -0.2283 0.0169  44  PHE   L CE1 
19879 C  CE2 . PHE   L  44  ? 1.4493 0.6050 1.2686 0.1110  -0.2418 0.0054  44  PHE   L CE2 
19880 C  CZ  . PHE   L  44  ? 1.4689 0.5907 1.2533 0.1164  -0.2607 0.0326  44  PHE   L CZ  
19881 N  N   . ASP   L  45  ? 1.3982 0.5715 1.5456 0.0952  -0.2378 -0.0039 45  ASP   L N   
19882 C  CA  . ASP   L  45  ? 1.3848 0.5333 1.5692 0.1036  -0.2491 -0.0506 45  ASP   L CA  
19883 C  C   . ASP   L  45  ? 1.4186 0.4303 1.5083 0.1447  -0.2429 -0.1136 45  ASP   L C   
19884 O  O   . ASP   L  45  ? 1.3921 0.3355 1.5393 0.0798  -0.2212 -0.1615 45  ASP   L O   
19885 C  CB  . ASP   L  45  ? 1.3882 0.6650 1.6497 0.1101  -0.2254 -0.0714 45  ASP   L CB  
19886 C  CG  . ASP   L  45  ? 1.3317 0.7915 1.7553 0.1778  -0.2191 -0.0589 45  ASP   L CG  
19887 O  OD1 . ASP   L  45  ? 1.3954 1.0146 1.8222 0.1070  -0.1443 -0.0445 45  ASP   L OD1 
19888 O  OD2 . ASP   L  45  ? 1.3704 1.0418 1.8316 0.0547  -0.0752 -0.0649 45  ASP   L OD2 
19889 N  N   . CYS   L  46  ? 1.3884 0.4234 1.5358 0.1269  -0.2324 -0.1160 46  CYS   L N   
19890 C  CA  . CYS   L  46  ? 1.3719 0.5334 1.5755 0.0872  -0.2349 -0.0928 46  CYS   L CA  
19891 C  C   . CYS   L  46  ? 1.3896 0.5122 1.6533 0.0837  -0.2133 -0.1077 46  CYS   L C   
19892 O  O   . CYS   L  46  ? 1.3911 0.4235 1.6993 0.1058  -0.2205 -0.1801 46  CYS   L O   
19893 C  CB  . CYS   L  46  ? 1.3812 0.5446 1.5474 0.1041  -0.2507 -0.0844 46  CYS   L CB  
19894 S  SG  . CYS   L  46  ? 1.4155 0.5950 1.4821 0.1156  -0.3102 -0.0246 46  CYS   L SG  
19895 N  N   . GLY   L  47  ? 1.3925 0.5375 1.7045 0.0914  -0.2113 -0.1059 47  GLY   L N   
19896 C  CA  . GLY   L  47  ? 1.3876 0.5866 1.7542 0.1289  -0.2360 -0.1103 47  GLY   L CA  
19897 C  C   . GLY   L  47  ? 1.4177 0.6759 1.7709 0.1563  -0.2663 -0.0940 47  GLY   L C   
19898 O  O   . GLY   L  47  ? 1.4268 0.6890 1.8103 0.2592  -0.2860 -0.0451 47  GLY   L O   
19899 N  N   . ASP   L  48  ? 1.4070 0.6738 1.8850 0.1774  -0.2498 -0.1069 48  ASP   L N   
19900 C  CA  . ASP   L  48  ? 1.4736 0.6703 1.8968 0.1464  -0.2490 -0.0748 48  ASP   L CA  
19901 C  C   . ASP   L  48  ? 1.4584 0.6988 1.9163 0.1603  -0.2635 -0.1126 48  ASP   L C   
19902 O  O   . ASP   L  48  ? 1.4510 0.6488 1.9000 0.1199  -0.3210 -0.1879 48  ASP   L O   
19903 C  CB  . ASP   L  48  ? 1.5431 0.6772 1.9005 0.1241  -0.2357 -0.0113 48  ASP   L CB  
19904 C  CG  . ASP   L  48  ? 1.6007 0.6804 1.9072 0.0870  -0.1994 -0.0002 48  ASP   L CG  
19905 O  OD1 . ASP   L  48  ? 1.6459 0.6881 1.9203 0.0927  -0.1074 0.0722  48  ASP   L OD1 
19906 O  OD2 . ASP   L  48  ? 1.6514 0.8240 2.0027 0.0174  -0.1992 0.0686  48  ASP   L OD2 
19907 N  N   . ASN   L  49  ? 1.4302 0.6096 1.9472 0.1684  -0.2723 -0.1497 49  ASN   L N   
19908 C  CA  . ASN   L  49  ? 1.4368 0.5743 1.9809 0.1472  -0.2828 -0.0911 49  ASN   L CA  
19909 C  C   . ASN   L  49  ? 1.4666 0.5235 1.8724 0.1428  -0.2955 -0.0697 49  ASN   L C   
19910 O  O   . ASN   L  49  ? 1.4874 0.3970 1.9227 0.1040  -0.3220 -0.0709 49  ASN   L O   
19911 C  CB  . ASN   L  49  ? 1.3693 0.5900 2.0815 0.1471  -0.3002 -0.1288 49  ASN   L CB  
19912 C  CG  . ASN   L  49  ? 1.4001 0.6203 2.1659 0.0978  -0.2589 -0.1748 49  ASN   L CG  
19913 O  OD1 . ASN   L  49  ? 1.5633 0.6561 2.2129 0.0409  -0.3000 -0.2627 49  ASN   L OD1 
19914 N  ND2 . ASN   L  49  ? 1.3736 0.6520 2.1837 0.0533  -0.2534 -0.2089 49  ASN   L ND2 
19915 N  N   . ILE   L  50  ? 1.4869 0.5618 1.7868 0.1121  -0.2941 -0.0189 50  ILE   L N   
19916 C  CA  . ILE   L  50  ? 1.4584 0.5495 1.6552 0.0929  -0.2970 0.0259  50  ILE   L CA  
19917 C  C   . ILE   L  50  ? 1.4890 0.5538 1.6218 0.1012  -0.3079 0.0165  50  ILE   L C   
19918 O  O   . ILE   L  50  ? 1.5150 0.4285 1.5615 0.1730  -0.2696 0.0802  50  ILE   L O   
19919 C  CB  . ILE   L  50  ? 1.4749 0.5442 1.6361 0.0780  -0.2929 0.0426  50  ILE   L CB  
19920 C  CG1 . ILE   L  50  ? 1.4915 0.5523 1.6771 0.1042  -0.2903 0.0740  50  ILE   L CG1 
19921 C  CG2 . ILE   L  50  ? 1.4400 0.5401 1.5952 0.0634  -0.3017 0.0464  50  ILE   L CG2 
19922 C  CD1 . ILE   L  50  ? 1.5026 0.5494 1.6656 0.1066  -0.2677 0.1323  50  ILE   L CD1 
19923 N  N   . VAL   L  51  ? 1.4740 0.5678 1.5874 0.0562  -0.3293 0.0062  51  VAL   L N   
19924 C  CA  . VAL   L  51  ? 1.4433 0.5379 1.5736 0.0296  -0.3148 -0.0121 51  VAL   L CA  
19925 C  C   . VAL   L  51  ? 1.4302 0.4871 1.5517 0.0422  -0.3518 0.0026  51  VAL   L C   
19926 O  O   . VAL   L  51  ? 1.4105 0.4672 1.5589 0.0063  -0.3418 -0.0393 51  VAL   L O   
19927 C  CB  . VAL   L  51  ? 1.4381 0.5991 1.6039 0.0012  -0.2922 -0.0486 51  VAL   L CB  
19928 C  CG1 . VAL   L  51  ? 1.4175 0.6702 1.6258 -0.0167 -0.2757 -0.0540 51  VAL   L CG1 
19929 C  CG2 . VAL   L  51  ? 1.4734 0.6126 1.6179 0.0116  -0.3028 -0.0647 51  VAL   L CG2 
19930 N  N   . MET   L  52  ? 1.4727 0.4712 1.5644 0.0799  -0.3459 0.0496  52  MET   L N   
19931 C  CA  . MET   L  52  ? 1.4749 0.5370 1.5258 0.1004  -0.3768 0.0620  52  MET   L CA  
19932 C  C   . MET   L  52  ? 1.4790 0.5549 1.4475 0.1183  -0.3825 0.0312  52  MET   L C   
19933 O  O   . MET   L  52  ? 1.4617 0.6563 1.4287 0.1523  -0.3922 0.0127  52  MET   L O   
19934 C  CB  . MET   L  52  ? 1.5008 0.4817 1.4996 0.1148  -0.4145 0.1239  52  MET   L CB  
19935 C  CG  . MET   L  52  ? 1.5227 0.5594 1.4769 0.1805  -0.4533 0.1481  52  MET   L CG  
19936 S  SD  . MET   L  52  ? 1.5456 0.6457 1.5357 0.1281  -0.4930 0.2168  52  MET   L SD  
19937 C  CE  . MET   L  52  ? 1.5910 0.4357 1.5162 0.1575  -0.4463 0.1974  52  MET   L CE  
19938 N  N   . SER   L  53  ? 1.4851 0.5248 1.5023 0.0941  -0.4067 -0.0114 53  SER   L N   
19939 C  CA  . SER   L  53  ? 1.4454 0.5642 1.4708 0.0769  -0.4239 -0.0085 53  SER   L CA  
19940 C  C   . SER   L  53  ? 1.4218 0.6123 1.5101 0.0704  -0.4412 -0.0805 53  SER   L C   
19941 O  O   . SER   L  53  ? 1.3263 0.6223 1.4993 0.0909  -0.4770 -0.0817 53  SER   L O   
19942 C  CB  . SER   L  53  ? 1.5247 0.5181 1.4369 0.0849  -0.4138 0.0601  53  SER   L CB  
19943 O  OG  . SER   L  53  ? 1.5437 0.4389 1.3813 0.0391  -0.3773 0.0488  53  SER   L OG  
19944 N  N   . ALA   L  54  ? 1.4184 0.6013 1.4681 0.0770  -0.4211 -0.1250 54  ALA   L N   
19945 C  CA  . ALA   L  54  ? 1.4370 0.6021 1.4094 0.0609  -0.3791 -0.1114 54  ALA   L CA  
19946 C  C   . ALA   L  54  ? 1.4717 0.6627 1.3027 0.0304  -0.3688 -0.0635 54  ALA   L C   
19947 O  O   . ALA   L  54  ? 1.4637 0.6363 1.2695 -0.0006 -0.3115 -0.0750 54  ALA   L O   
19948 C  CB  . ALA   L  54  ? 1.4464 0.5711 1.3906 0.0888  -0.3637 -0.1557 54  ALA   L CB  
19949 N  N   . ASN   L  55  ? 1.4765 0.6303 1.3292 0.0228  -0.3483 -0.0446 55  ASN   L N   
19950 C  CA  . ASN   L  55  ? 1.4464 0.6740 1.3293 0.0582  -0.3006 0.0013  55  ASN   L CA  
19951 C  C   . ASN   L  55  ? 1.4525 0.5897 1.2657 0.0592  -0.2695 0.0393  55  ASN   L C   
19952 O  O   . ASN   L  55  ? 1.4237 0.7237 1.3150 0.1065  -0.2201 0.0867  55  ASN   L O   
19953 C  CB  . ASN   L  55  ? 1.4829 0.7654 1.4273 0.0055  -0.3345 0.0098  55  ASN   L CB  
19954 C  CG  . ASN   L  55  ? 1.5245 0.8071 1.4507 -0.0048 -0.3127 0.0362  55  ASN   L CG  
19955 O  OD1 . ASN   L  55  ? 1.5200 0.9085 1.5640 0.0751  -0.3363 -0.0711 55  ASN   L OD1 
19956 N  ND2 . ASN   L  55  ? 1.5394 0.8793 1.4666 -0.0476 -0.2877 -0.0507 55  ASN   L ND2 
19957 N  N   . GLY   L  56  ? 1.4076 0.4495 1.2564 0.0722  -0.2328 0.0122  56  GLY   L N   
19958 C  CA  . GLY   L  56  ? 1.4116 0.4545 1.2658 0.0765  -0.2314 0.0728  56  GLY   L CA  
19959 C  C   . GLY   L  56  ? 1.4192 0.4161 1.2423 0.1166  -0.2224 0.1398  56  GLY   L C   
19960 O  O   . GLY   L  56  ? 1.4447 0.4741 1.3139 0.1667  -0.1905 0.2118  56  GLY   L O   
19961 N  N   . PHE   L  57  ? 1.4125 0.4095 1.2706 0.1167  -0.1863 0.1762  57  PHE   L N   
19962 C  CA  . PHE   L  57  ? 1.4435 0.4317 1.2776 0.0955  -0.1949 0.1687  57  PHE   L CA  
19963 C  C   . PHE   L  57  ? 1.4125 0.4974 1.2885 0.0631  -0.1495 0.1197  57  PHE   L C   
19964 O  O   . PHE   L  57  ? 1.5010 0.5214 1.3504 0.0155  -0.1530 0.1399  57  PHE   L O   
19965 C  CB  . PHE   L  57  ? 1.4572 0.4241 1.2695 0.1015  -0.1836 0.1682  57  PHE   L CB  
19966 C  CG  . PHE   L  57  ? 1.5005 0.4366 1.2818 0.0789  -0.1831 0.1450  57  PHE   L CG  
19967 C  CD1 . PHE   L  57  ? 1.5461 0.5561 1.2628 0.0708  -0.1512 0.1470  57  PHE   L CD1 
19968 C  CD2 . PHE   L  57  ? 1.4836 0.4396 1.2863 0.0858  -0.1491 0.1650  57  PHE   L CD2 
19969 C  CE1 . PHE   L  57  ? 1.5110 0.5600 1.3048 0.0420  -0.1405 0.1225  57  PHE   L CE1 
19970 C  CE2 . PHE   L  57  ? 1.4692 0.4481 1.2887 0.0820  -0.1354 0.1512  57  PHE   L CE2 
19971 C  CZ  . PHE   L  57  ? 1.5040 0.4820 1.2686 0.0872  -0.1337 0.1399  57  PHE   L CZ  
19972 N  N   . ALA   L  58  ? 1.4206 0.4993 1.3353 -0.0003 -0.1421 0.1577  58  ALA   L N   
19973 C  CA  . ALA   L  58  ? 1.4427 0.5237 1.4217 0.0151  -0.1158 0.1423  58  ALA   L CA  
19974 C  C   . ALA   L  58  ? 1.3920 0.5701 1.4367 0.0321  -0.1159 0.0677  58  ALA   L C   
19975 O  O   . ALA   L  58  ? 1.3817 0.7081 1.5310 0.1493  -0.0904 -0.0590 58  ALA   L O   
19976 C  CB  . ALA   L  58  ? 1.4209 0.5704 1.4326 -0.0064 -0.1014 0.1298  58  ALA   L CB  
19977 N  N   . ALA   L  59  ? 1.3959 0.5349 1.3898 0.0443  -0.1241 0.0706  59  ALA   L N   
19978 C  CA  . ALA   L  59  ? 1.3656 0.5159 1.4023 0.0754  -0.1202 0.0460  59  ALA   L CA  
19979 C  C   . ALA   L  59  ? 1.3865 0.4350 1.4128 0.0650  -0.1126 0.0183  59  ALA   L C   
19980 O  O   . ALA   L  59  ? 1.4058 0.4494 1.4833 0.1433  -0.1041 0.0678  59  ALA   L O   
19981 C  CB  . ALA   L  59  ? 1.3777 0.5203 1.3745 0.0702  -0.1305 0.0668  59  ALA   L CB  
19982 N  N   . ASP   L  60  ? 1.4017 0.3111 1.4030 0.0253  -0.1574 0.0010  60  ASP   L N   
19983 C  CA  . ASP   L  60  ? 1.3941 0.2874 1.3636 0.0532  -0.1872 -0.0283 60  ASP   L CA  
19984 C  C   . ASP   L  60  ? 1.3559 0.3587 1.3839 0.0091  -0.1880 -0.0595 60  ASP   L C   
19985 O  O   . ASP   L  60  ? 1.3246 0.4133 1.3852 0.0692  -0.2024 -0.0382 60  ASP   L O   
19986 C  CB  . ASP   L  60  ? 1.4299 0.2820 1.3553 0.0513  -0.1983 -0.0429 60  ASP   L CB  
19987 C  CG  . ASP   L  60  ? 1.4328 0.2216 1.3100 0.0601  -0.2122 -0.0866 60  ASP   L CG  
19988 O  OD1 . ASP   L  60  ? 1.3973 0.1455 1.3577 0.0138  -0.2211 -0.0687 60  ASP   L OD1 
19989 O  OD2 . ASP   L  60  ? 1.4362 0.3113 1.3220 0.1065  -0.2000 -0.0807 60  ASP   L OD2 
19990 N  N   . GLY   L  61  ? 1.3969 0.3235 1.3839 0.0147  -0.1966 0.0060  61  GLY   L N   
19991 C  CA  . GLY   L  61  ? 1.4099 0.4435 1.4346 0.0112  -0.2071 0.0265  61  GLY   L CA  
19992 C  C   . GLY   L  61  ? 1.4678 0.5165 1.3821 -0.0347 -0.1910 -0.0491 61  GLY   L C   
19993 O  O   . GLY   L  61  ? 1.4695 0.6597 1.4654 0.0004  -0.2424 -0.0160 61  GLY   L O   
19994 N  N   . ASP   L  62  ? 1.4508 0.5444 1.3710 -0.0284 -0.2037 0.0074  62  ASP   L N   
19995 C  CA  . ASP   L  62  ? 1.4424 0.6059 1.3700 -0.0114 -0.1741 0.0014  62  ASP   L CA  
19996 C  C   . ASP   L  62  ? 1.4290 0.4850 1.3850 0.0729  -0.2035 -0.0387 62  ASP   L C   
19997 O  O   . ASP   L  62  ? 1.4201 0.4145 1.3948 0.0346  -0.1674 -0.0702 62  ASP   L O   
19998 C  CB  . ASP   L  62  ? 1.5121 0.7463 1.3665 0.0220  -0.1877 -0.0012 62  ASP   L CB  
19999 C  CG  . ASP   L  62  ? 1.5689 0.8163 1.3988 -0.0091 -0.1811 0.0418  62  ASP   L CG  
20000 O  OD1 . ASP   L  62  ? 1.6039 0.8611 1.4948 -0.0027 -0.2338 0.0121  62  ASP   L OD1 
20001 O  OD2 . ASP   L  62  ? 1.7177 1.0672 1.3403 0.0200  -0.1952 0.0346  62  ASP   L OD2 
20002 N  N   . ALA   L  63  ? 1.4233 0.4461 1.3976 0.0270  -0.2306 -0.0311 63  ALA   L N   
20003 C  CA  . ALA   L  63  ? 1.4653 0.4122 1.4237 0.0328  -0.2488 -0.0198 63  ALA   L CA  
20004 C  C   . ALA   L  63  ? 1.4792 0.4143 1.4484 0.0543  -0.2414 0.0029  63  ALA   L C   
20005 O  O   . ALA   L  63  ? 1.5355 0.4329 1.5593 0.1114  -0.2241 0.1369  63  ALA   L O   
20006 C  CB  . ALA   L  63  ? 1.4534 0.4085 1.3896 0.0026  -0.2665 -0.0433 63  ALA   L CB  
20007 N  N   . LEU   L  64  ? 1.4777 0.3965 1.4081 0.0474  -0.2563 0.0396  64  LEU   L N   
20008 C  CA  . LEU   L  64  ? 1.4889 0.3866 1.4239 0.0359  -0.2584 0.0797  64  LEU   L CA  
20009 C  C   . LEU   L  64  ? 1.4619 0.4894 1.3813 0.0140  -0.2619 0.0388  64  LEU   L C   
20010 O  O   . LEU   L  64  ? 1.5378 0.5172 1.4157 -0.0669 -0.2891 0.0932  64  LEU   L O   
20011 C  CB  . LEU   L  64  ? 1.4987 0.4249 1.3970 0.0078  -0.2397 0.0781  64  LEU   L CB  
20012 C  CG  . LEU   L  64  ? 1.5118 0.4766 1.4307 -0.0105 -0.2109 0.1467  64  LEU   L CG  
20013 C  CD1 . LEU   L  64  ? 1.4896 0.4900 1.5200 -0.0169 -0.1905 0.1264  64  LEU   L CD1 
20014 C  CD2 . LEU   L  64  ? 1.5330 0.5233 1.4398 -0.0438 -0.2266 0.1285  64  LEU   L CD2 
20015 N  N   . VAL   L  65  ? 1.4808 0.4485 1.3275 0.0370  -0.2631 0.0516  65  VAL   L N   
20016 C  CA  . VAL   L  65  ? 1.4894 0.5722 1.3555 0.0433  -0.2498 0.0337  65  VAL   L CA  
20017 C  C   . VAL   L  65  ? 1.4755 0.5713 1.3881 0.0266  -0.2286 0.0292  65  VAL   L C   
20018 O  O   . VAL   L  65  ? 1.4613 0.6438 1.5347 0.0951  -0.2119 -0.0038 65  VAL   L O   
20019 C  CB  . VAL   L  65  ? 1.5430 0.5774 1.3077 0.0388  -0.2480 0.0245  65  VAL   L CB  
20020 C  CG1 . VAL   L  65  ? 1.5301 0.6774 1.3079 0.0449  -0.2481 0.0307  65  VAL   L CG1 
20021 C  CG2 . VAL   L  65  ? 1.5805 0.5671 1.3209 0.0740  -0.2565 0.0155  65  VAL   L CG2 
20022 N  N   . LYS   L  66  ? 1.4343 0.5305 1.3725 0.0247  -0.1992 -0.0038 66  LYS   L N   
20023 C  CA  . LYS   L  66  ? 1.4307 0.5215 1.3994 0.0878  -0.1501 -0.0367 66  LYS   L CA  
20024 C  C   . LYS   L  66  ? 1.4600 0.4536 1.4004 0.0656  -0.1651 -0.0872 66  LYS   L C   
20025 O  O   . LYS   L  66  ? 1.4618 0.4095 1.5080 0.0474  -0.1309 0.0113  66  LYS   L O   
20026 C  CB  . LYS   L  66  ? 1.4371 0.5612 1.3826 0.1094  -0.1369 -0.0352 66  LYS   L CB  
20027 C  CG  . LYS   L  66  ? 1.4719 0.6481 1.3700 0.1467  -0.1130 -0.0550 66  LYS   L CG  
20028 C  CD  . LYS   L  66  ? 1.5176 0.6919 1.3955 0.1677  -0.0884 -0.0007 66  LYS   L CD  
20029 C  CE  . LYS   L  66  ? 1.5804 0.7328 1.3829 0.1849  -0.0586 -0.0028 66  LYS   L CE  
20030 N  NZ  . LYS   L  66  ? 1.6126 0.7333 1.4023 0.1958  -0.0340 0.0320  66  LYS   L NZ  
20031 N  N   . ARG   L  67  ? 1.4814 0.3334 1.3528 0.0653  -0.1905 -0.1416 67  ARG   L N   
20032 C  CA  . ARG   L  67  ? 1.5005 0.3179 1.3720 0.0223  -0.2080 -0.1554 67  ARG   L CA  
20033 C  C   . ARG   L  67  ? 1.5043 0.4224 1.4155 0.0413  -0.2214 -0.1410 67  ARG   L C   
20034 O  O   . ARG   L  67  ? 1.4895 0.4176 1.4352 0.1037  -0.2221 -0.1904 67  ARG   L O   
20035 C  CB  . ARG   L  67  ? 1.5079 0.2998 1.3445 0.0025  -0.2076 -0.1623 67  ARG   L CB  
20036 C  CG  . ARG   L  67  ? 1.5522 0.3017 1.3265 -0.0144 -0.2218 -0.1844 67  ARG   L CG  
20037 C  CD  . ARG   L  67  ? 1.5999 0.4385 1.3353 0.0004  -0.1727 -0.1382 67  ARG   L CD  
20038 N  NE  . ARG   L  67  ? 1.6853 0.5016 1.2699 -0.0301 -0.2072 -0.1637 67  ARG   L NE  
20039 C  CZ  . ARG   L  67  ? 1.7432 0.6293 1.2574 -0.0195 -0.1994 -0.1214 67  ARG   L CZ  
20040 N  NH1 . ARG   L  67  ? 1.7525 0.6593 1.3017 -0.0495 -0.1995 -0.0395 67  ARG   L NH1 
20041 N  NH2 . ARG   L  67  ? 1.7455 0.6759 1.2335 -0.0113 -0.1972 -0.1267 67  ARG   L NH2 
20042 N  N   . PHE   L  68  ? 1.4663 0.3862 1.4664 0.0508  -0.2506 -0.0995 68  PHE   L N   
20043 C  CA  . PHE   L  68  ? 1.4701 0.4286 1.4915 0.0561  -0.2650 -0.0972 68  PHE   L CA  
20044 C  C   . PHE   L  68  ? 1.4913 0.4773 1.5323 0.0723  -0.1981 -0.0371 68  PHE   L C   
20045 O  O   . PHE   L  68  ? 1.5848 0.5305 1.6449 0.1360  -0.1764 0.0113  68  PHE   L O   
20046 C  CB  . PHE   L  68  ? 1.4641 0.4791 1.4461 0.0821  -0.2820 -0.1440 68  PHE   L CB  
20047 C  CG  . PHE   L  68  ? 1.4543 0.5396 1.4585 0.0241  -0.3196 -0.2066 68  PHE   L CG  
20048 C  CD1 . PHE   L  68  ? 1.4513 0.5576 1.4645 -0.0242 -0.3409 -0.1995 68  PHE   L CD1 
20049 C  CD2 . PHE   L  68  ? 1.4384 0.6049 1.4440 0.0311  -0.3294 -0.2276 68  PHE   L CD2 
20050 C  CE1 . PHE   L  68  ? 1.4480 0.5951 1.4956 -0.0252 -0.3504 -0.1823 68  PHE   L CE1 
20051 C  CE2 . PHE   L  68  ? 1.4304 0.6894 1.4811 0.0445  -0.3382 -0.2180 68  PHE   L CE2 
20052 C  CZ  . PHE   L  68  ? 1.4221 0.6729 1.5224 0.0158  -0.3481 -0.1878 68  PHE   L CZ  
20053 N  N   . LYS   L  69  ? 1.4669 0.4633 1.5293 0.0839  -0.2227 0.0073  69  LYS   L N   
20054 C  CA  . LYS   L  69  ? 1.4454 0.5747 1.5247 0.0820  -0.1989 0.0213  69  LYS   L CA  
20055 C  C   . LYS   L  69  ? 1.4031 0.6079 1.5441 0.0343  -0.2285 0.0371  69  LYS   L C   
20056 O  O   . LYS   L  69  ? 1.4515 0.5662 1.6155 0.0413  -0.2251 0.0225  69  LYS   L O   
20057 C  CB  . LYS   L  69  ? 1.4728 0.6136 1.5248 0.0937  -0.1745 0.0225  69  LYS   L CB  
20058 C  CG  . LYS   L  69  ? 1.4609 0.7238 1.5881 0.0469  -0.1384 0.0167  69  LYS   L CG  
20059 C  CD  . LYS   L  69  ? 1.5020 0.8863 1.6008 0.0769  -0.0930 0.0225  69  LYS   L CD  
20060 C  CE  . LYS   L  69  ? 1.4862 0.9266 1.6292 0.0788  -0.0466 0.0528  69  LYS   L CE  
20061 N  NZ  . LYS   L  69  ? 1.5076 0.9626 1.6360 0.1435  -0.0420 0.0983  69  LYS   L NZ  
20062 N  N   . ASN   L  70  ? 1.4011 0.5925 1.5483 0.0201  -0.2282 0.0536  70  ASN   L N   
20063 C  CA  . ASN   L  70  ? 1.3941 0.5578 1.5812 0.0539  -0.2269 0.0409  70  ASN   L CA  
20064 C  C   . ASN   L  70  ? 1.4848 0.5221 1.5760 0.0191  -0.2192 0.0234  70  ASN   L C   
20065 O  O   . ASN   L  70  ? 1.5876 0.5172 1.5835 0.0120  -0.2230 0.0610  70  ASN   L O   
20066 C  CB  . ASN   L  70  ? 1.3731 0.4970 1.5881 0.0294  -0.2259 0.0193  70  ASN   L CB  
20067 C  CG  . ASN   L  70  ? 1.2975 0.5072 1.6416 0.0289  -0.2310 0.0086  70  ASN   L CG  
20068 O  OD1 . ASN   L  70  ? 1.3107 0.5627 1.6979 0.0082  -0.1934 -0.0243 70  ASN   L OD1 
20069 N  ND2 . ASN   L  70  ? 1.2238 0.6478 1.6731 0.0348  -0.2209 0.0007  70  ASN   L ND2 
20070 N  N   . SER   L  71  ? 1.5159 0.5086 1.5465 -0.0096 -0.2389 0.0332  71  SER   L N   
20071 C  CA  . SER   L  71  ? 1.4924 0.4770 1.5295 0.0068  -0.2318 0.0150  71  SER   L CA  
20072 C  C   . SER   L  71  ? 1.5392 0.4308 1.5135 0.0574  -0.2482 0.0329  71  SER   L C   
20073 O  O   . SER   L  71  ? 1.4237 0.4502 1.4480 0.0850  -0.3017 0.0349  71  SER   L O   
20074 C  CB  . SER   L  71  ? 1.5550 0.5102 1.5042 -0.0402 -0.1743 0.0109  71  SER   L CB  
20075 O  OG  . SER   L  71  ? 1.6151 0.5454 1.5592 -0.0864 -0.0944 0.0317  71  SER   L OG  
20076 N  N   . VAL   L  72  ? 1.4735 0.4374 1.5264 0.0991  -0.2773 0.0430  72  VAL   L N   
20077 C  CA  . VAL   L  72  ? 1.4931 0.5281 1.5472 0.1106  -0.3182 0.0821  72  VAL   L CA  
20078 C  C   . VAL   L  72  ? 1.5302 0.5743 1.5398 0.0900  -0.2755 0.0546  72  VAL   L C   
20079 O  O   . VAL   L  72  ? 1.5038 0.6480 1.5498 0.0917  -0.3252 0.0619  72  VAL   L O   
20080 C  CB  . VAL   L  72  ? 1.4613 0.5637 1.5446 0.1073  -0.3323 0.0791  72  VAL   L CB  
20081 C  CG1 . VAL   L  72  ? 1.4677 0.5497 1.5649 0.1134  -0.3193 0.0638  72  VAL   L CG1 
20082 C  CG2 . VAL   L  72  ? 1.4777 0.6132 1.5203 0.1333  -0.3394 0.0662  72  VAL   L CG2 
20083 N  N   . LYS   L  73  ? 1.5424 0.5423 1.5119 0.0945  -0.2378 0.0609  73  LYS   L N   
20084 C  CA  . LYS   L  73  ? 1.5770 0.5256 1.5607 0.1251  -0.2331 0.0540  73  LYS   L CA  
20085 C  C   . LYS   L  73  ? 1.5646 0.4702 1.5805 0.1507  -0.2536 0.0292  73  LYS   L C   
20086 O  O   . LYS   L  73  ? 1.5873 0.4586 1.6128 0.1456  -0.3077 0.0766  73  LYS   L O   
20087 C  CB  . LYS   L  73  ? 1.5907 0.5168 1.5516 0.1386  -0.2116 0.0835  73  LYS   L CB  
20088 C  CG  . LYS   L  73  ? 1.6717 0.5847 1.5511 0.1413  -0.2002 0.0607  73  LYS   L CG  
20089 C  CD  . LYS   L  73  ? 1.7202 0.6226 1.5717 0.1791  -0.2201 0.0951  73  LYS   L CD  
20090 C  CE  . LYS   L  73  ? 1.7942 0.7737 1.5507 0.1665  -0.1917 0.0589  73  LYS   L CE  
20091 N  NZ  . LYS   L  73  ? 1.8026 0.8615 1.5657 0.1678  -0.2055 0.0846  73  LYS   L NZ  
20092 N  N   . TRP   L  74  ? 1.5599 0.3841 1.5972 0.1601  -0.2642 -0.0221 74  TRP   L N   
20093 C  CA  . TRP   L  74  ? 1.6202 0.3125 1.6481 0.1636  -0.2690 -0.0368 74  TRP   L CA  
20094 C  C   . TRP   L  74  ? 1.6538 0.3592 1.6521 0.1423  -0.2638 -0.0121 74  TRP   L C   
20095 O  O   . TRP   L  74  ? 1.7704 0.3907 1.6884 0.0701  -0.2787 0.0265  74  TRP   L O   
20096 C  CB  . TRP   L  74  ? 1.6397 0.3243 1.6623 0.2131  -0.2484 -0.0624 74  TRP   L CB  
20097 C  CG  . TRP   L  74  ? 1.6545 0.3851 1.6873 0.2526  -0.2743 -0.0707 74  TRP   L CG  
20098 C  CD1 . TRP   L  74  ? 1.6781 0.3912 1.6994 0.2584  -0.2991 -0.0735 74  TRP   L CD1 
20099 C  CD2 . TRP   L  74  ? 1.6605 0.3971 1.7220 0.2354  -0.2800 -0.0782 74  TRP   L CD2 
20100 N  NE1 . TRP   L  74  ? 1.6861 0.4094 1.7346 0.2651  -0.2804 -0.1328 74  TRP   L NE1 
20101 C  CE2 . TRP   L  74  ? 1.6561 0.4172 1.7197 0.2588  -0.2868 -0.1092 74  TRP   L CE2 
20102 C  CE3 . TRP   L  74  ? 1.7093 0.3969 1.7858 0.2115  -0.2623 -0.0661 74  TRP   L CE3 
20103 C  CZ2 . TRP   L  74  ? 1.6800 0.4127 1.7494 0.2495  -0.2820 -0.1174 74  TRP   L CZ2 
20104 C  CZ3 . TRP   L  74  ? 1.7524 0.4945 1.7558 0.2171  -0.2870 -0.0986 74  TRP   L CZ3 
20105 C  CH2 . TRP   L  74  ? 1.7306 0.4672 1.7832 0.2608  -0.2757 -0.0411 74  TRP   L CH2 
20106 N  N   . TYR   L  75  ? 1.6143 0.3060 1.6404 0.1322  -0.2485 0.0330  75  TYR   L N   
20107 C  CA  . TYR   L  75  ? 1.5881 0.2386 1.6903 0.1476  -0.2639 0.1005  75  TYR   L CA  
20108 C  C   . TYR   L  75  ? 1.5161 0.3919 1.7345 0.1724  -0.2543 0.0843  75  TYR   L C   
20109 O  O   . TYR   L  75  ? 1.5066 0.4469 1.7668 0.1539  -0.2356 0.1238  75  TYR   L O   
20110 C  CB  . TYR   L  75  ? 1.5903 0.1947 1.6876 0.1571  -0.2670 0.1571  75  TYR   L CB  
20111 C  CG  . TYR   L  75  ? 1.6129 0.1990 1.7035 0.1793  -0.2813 0.1646  75  TYR   L CG  
20112 C  CD1 . TYR   L  75  ? 1.6166 0.2069 1.7093 0.2072  -0.2728 0.1572  75  TYR   L CD1 
20113 C  CD2 . TYR   L  75  ? 1.6252 0.2134 1.7501 0.2159  -0.2758 0.1775  75  TYR   L CD2 
20114 C  CE1 . TYR   L  75  ? 1.6526 0.2630 1.7223 0.2545  -0.2794 0.1680  75  TYR   L CE1 
20115 C  CE2 . TYR   L  75  ? 1.6600 0.2365 1.7615 0.2664  -0.2859 0.1867  75  TYR   L CE2 
20116 C  CZ  . TYR   L  75  ? 1.6669 0.2872 1.7481 0.2965  -0.2876 0.1820  75  TYR   L CZ  
20117 O  OH  . TYR   L  75  ? 1.7279 0.4186 1.7324 0.3278  -0.2918 0.1589  75  TYR   L OH  
20118 N  N   . HIS   L  76  ? 1.5419 0.4869 1.7130 0.1131  -0.2699 0.1357  76  HIS   L N   
20119 C  CA  . HIS   L  76  ? 1.5287 0.5691 1.7886 0.0968  -0.2334 0.0869  76  HIS   L CA  
20120 C  C   . HIS   L  76  ? 1.5437 0.6122 1.8032 0.0733  -0.2347 0.0356  76  HIS   L C   
20121 O  O   . HIS   L  76  ? 1.5852 0.5131 1.9630 0.1369  -0.1933 -0.0621 76  HIS   L O   
20122 C  CB  . HIS   L  76  ? 1.5326 0.6295 1.8100 0.0570  -0.2303 0.0837  76  HIS   L CB  
20123 C  CG  . HIS   L  76  ? 1.5630 0.6351 1.8930 0.0255  -0.2232 0.1018  76  HIS   L CG  
20124 N  ND1 . HIS   L  76  ? 1.5994 0.6520 1.9139 0.0018  -0.2497 0.1270  76  HIS   L ND1 
20125 C  CD2 . HIS   L  76  ? 1.5290 0.6763 1.8769 0.0045  -0.1978 0.1088  76  HIS   L CD2 
20126 C  CE1 . HIS   L  76  ? 1.5260 0.7055 1.9081 -0.0268 -0.2478 0.1027  76  HIS   L CE1 
20127 N  NE2 . HIS   L  76  ? 1.4934 0.7358 1.8928 -0.0088 -0.2109 0.1081  76  HIS   L NE2 
20128 N  N   . PHE   L  77  ? 1.5239 0.6653 1.7678 0.0727  -0.2136 0.0323  77  PHE   L N   
20129 C  CA  . PHE   L  77  ? 1.5257 0.6659 1.7942 0.0614  -0.1770 0.0227  77  PHE   L CA  
20130 C  C   . PHE   L  77  ? 1.5192 0.6792 1.7837 0.0322  -0.2198 0.0389  77  PHE   L C   
20131 O  O   . PHE   L  77  ? 1.5602 0.6918 1.7815 0.0084  -0.1926 -0.0369 77  PHE   L O   
20132 C  CB  . PHE   L  77  ? 1.4795 0.7102 1.7642 0.0643  -0.1398 -0.0128 77  PHE   L CB  
20133 C  CG  . PHE   L  77  ? 1.4674 0.7707 1.7796 0.0730  -0.0704 -0.0641 77  PHE   L CG  
20134 C  CD1 . PHE   L  77  ? 1.4732 0.7797 1.8179 0.0800  -0.0594 -0.0688 77  PHE   L CD1 
20135 C  CD2 . PHE   L  77  ? 1.4446 0.7635 1.7534 0.0999  -0.0462 -0.0938 77  PHE   L CD2 
20136 C  CE1 . PHE   L  77  ? 1.4685 0.8597 1.8066 0.0847  -0.0383 -0.1084 77  PHE   L CE1 
20137 C  CE2 . PHE   L  77  ? 1.4583 0.7786 1.7548 0.1097  -0.0205 -0.1215 77  PHE   L CE2 
20138 C  CZ  . PHE   L  77  ? 1.4517 0.8701 1.7692 0.1066  -0.0122 -0.1303 77  PHE   L CZ  
20139 N  N   . ASP   L  78  ? 1.5031 0.5236 1.7708 0.0363  -0.2573 0.0673  78  ASP   L N   
20140 C  CA  . ASP   L  78  ? 1.5239 0.5375 1.7877 0.0205  -0.2484 0.0646  78  ASP   L CA  
20141 C  C   . ASP   L  78  ? 1.6065 0.5324 1.7686 0.0082  -0.2637 0.0684  78  ASP   L C   
20142 O  O   . ASP   L  78  ? 1.5962 0.7292 1.7270 0.0508  -0.2890 0.1780  78  ASP   L O   
20143 C  CB  . ASP   L  78  ? 1.5024 0.5616 1.8068 0.0213  -0.2595 0.0621  78  ASP   L CB  
20144 C  CG  . ASP   L  78  ? 1.4533 0.7274 1.8314 -0.0036 -0.2521 0.0285  78  ASP   L CG  
20145 O  OD1 . ASP   L  78  ? 1.4678 0.7205 1.8473 0.0884  -0.2551 -0.0121 78  ASP   L OD1 
20146 O  OD2 . ASP   L  78  ? 1.3677 0.7587 1.8777 0.0040  -0.1883 0.0463  78  ASP   L OD2 
20147 N  N   . HIS   L  79  ? 1.6497 0.4415 1.6672 -0.0039 -0.2766 0.0478  79  HIS   L N   
20148 C  CA  . HIS   L  79  ? 1.6949 0.5169 1.6528 -0.0013 -0.2847 0.0569  79  HIS   L CA  
20149 C  C   . HIS   L  79  ? 1.6829 0.5300 1.6109 -0.0231 -0.3037 0.0481  79  HIS   L C   
20150 O  O   . HIS   L  79  ? 1.6355 0.6807 1.5986 -0.0697 -0.3217 0.1012  79  HIS   L O   
20151 C  CB  . HIS   L  79  ? 1.7385 0.5815 1.6345 0.0397  -0.2539 0.0376  79  HIS   L CB  
20152 C  CG  . HIS   L  79  ? 1.7851 0.6792 1.6537 0.0137  -0.1578 -0.0395 79  HIS   L CG  
20153 N  ND1 . HIS   L  79  ? 1.8268 0.8030 1.5782 0.0293  -0.1561 -0.0419 79  HIS   L ND1 
20154 C  CD2 . HIS   L  79  ? 1.8618 0.5745 1.6864 -0.0012 -0.1318 -0.0334 79  HIS   L CD2 
20155 C  CE1 . HIS   L  79  ? 1.8609 0.8145 1.5700 -0.0097 -0.1105 -0.0880 79  HIS   L CE1 
20156 N  NE2 . HIS   L  79  ? 1.8189 0.6811 1.6379 -0.0374 -0.0908 -0.0905 79  HIS   L NE2 
20157 N  N   . ASN   L  80  ? 1.7278 0.5747 1.6345 -0.0169 -0.3074 0.0123  80  ASN   L N   
20158 C  CA  . ASN   L  80  ? 1.7605 0.6253 1.6990 0.0262  -0.3254 -0.0114 80  ASN   L CA  
20159 C  C   . ASN   L  80  ? 1.7795 0.6127 1.7008 0.0137  -0.3300 -0.0472 80  ASN   L C   
20160 O  O   . ASN   L  80  ? 1.7748 0.4833 1.7609 0.0671  -0.3271 0.0429  80  ASN   L O   
20161 C  CB  . ASN   L  80  ? 1.8413 0.6851 1.7150 0.0806  -0.3640 -0.0085 80  ASN   L CB  
20162 C  CG  . ASN   L  80  ? 1.9307 0.6265 1.7726 0.0859  -0.3395 -0.0489 80  ASN   L CG  
20163 O  OD1 . ASN   L  80  ? 1.9917 0.5999 1.7402 0.0767  -0.3671 -0.0721 80  ASN   L OD1 
20164 N  ND2 . ASN   L  80  ? 1.9499 0.5574 1.8029 0.0707  -0.3332 -0.0627 80  ASN   L ND2 
20165 N  N   . ASP   L  81  ? 1.7692 0.6942 1.6561 0.0826  -0.3488 -0.0595 81  ASP   L N   
20166 C  CA  . ASP   L  81  ? 1.7874 0.7264 1.6771 0.1020  -0.3023 -0.0224 81  ASP   L CA  
20167 C  C   . ASP   L  81  ? 1.8017 0.6726 1.6745 0.1086  -0.2839 -0.0145 81  ASP   L C   
20168 O  O   . ASP   L  81  ? 1.7835 0.6844 1.6656 0.1043  -0.2784 -0.0634 81  ASP   L O   
20169 C  CB  . ASP   L  81  ? 1.8001 0.8549 1.6890 0.1271  -0.3053 -0.0562 81  ASP   L CB  
20170 C  CG  . ASP   L  81  ? 1.8175 0.9364 1.6951 0.1487  -0.3425 -0.0161 81  ASP   L CG  
20171 O  OD1 . ASP   L  81  ? 1.8619 0.9013 1.5826 0.1719  -0.3379 -0.0710 81  ASP   L OD1 
20172 O  OD2 . ASP   L  81  ? 1.8652 1.1134 1.7396 0.1737  -0.2466 -0.0751 81  ASP   L OD2 
20173 N  N   . LYS   L  82  ? 1.8259 0.6736 1.7070 0.1255  -0.2541 0.0524  82  LYS   L N   
20174 C  CA  . LYS   L  82  ? 1.8037 0.7331 1.6734 0.1326  -0.2509 0.0626  82  LYS   L CA  
20175 C  C   . LYS   L  82  ? 1.6930 0.7199 1.6929 0.1173  -0.2643 0.0256  82  LYS   L C   
20176 O  O   . LYS   L  82  ? 1.6660 0.7313 1.6417 0.1230  -0.2428 0.0040  82  LYS   L O   
20177 C  CB  . LYS   L  82  ? 1.8514 0.7258 1.6857 0.1464  -0.2317 0.1227  82  LYS   L CB  
20178 C  CG  . LYS   L  82  ? 1.8685 0.7417 1.6447 0.1549  -0.2098 0.1392  82  LYS   L CG  
20179 C  CD  . LYS   L  82  ? 1.8761 0.7834 1.6349 0.1320  -0.2178 0.1440  82  LYS   L CD  
20180 C  CE  . LYS   L  82  ? 1.8886 0.8256 1.5686 0.1002  -0.2439 0.1788  82  LYS   L CE  
20181 N  NZ  . LYS   L  82  ? 1.9018 0.8650 1.5653 0.0726  -0.2545 0.1923  82  LYS   L NZ  
20182 N  N   . LYS   L  83  ? 1.6522 0.7433 1.7405 0.1186  -0.2529 0.0073  83  LYS   L N   
20183 C  CA  . LYS   L  83  ? 1.5661 0.7425 1.6788 0.1397  -0.3134 0.0238  83  LYS   L CA  
20184 C  C   . LYS   L  83  ? 1.5658 0.6928 1.6226 0.1501  -0.3389 0.0472  83  LYS   L C   
20185 O  O   . LYS   L  83  ? 1.6187 0.7003 1.5859 0.1345  -0.3725 0.0022  83  LYS   L O   
20186 C  CB  . LYS   L  83  ? 1.5773 0.7924 1.7324 0.1274  -0.3417 0.0202  83  LYS   L CB  
20187 C  CG  . LYS   L  83  ? 1.5430 0.8268 1.7441 0.1064  -0.3603 0.0514  83  LYS   L CG  
20188 C  CD  . LYS   L  83  ? 1.5515 0.9250 1.7840 0.1103  -0.3907 0.0186  83  LYS   L CD  
20189 C  CE  . LYS   L  83  ? 1.5426 0.8931 1.7797 0.0878  -0.4158 -0.0345 83  LYS   L CE  
20190 N  NZ  . LYS   L  83  ? 1.5451 0.9744 1.8193 0.0812  -0.4432 -0.0438 83  LYS   L NZ  
20191 N  N   . LEU   L  84  ? 1.4990 0.6761 1.5835 0.1477  -0.2908 0.0334  84  LEU   L N   
20192 C  CA  . LEU   L  84  ? 1.5005 0.6123 1.5666 0.1611  -0.2992 0.0812  84  LEU   L CA  
20193 C  C   . LEU   L  84  ? 1.4694 0.5713 1.5666 0.1679  -0.2901 0.1107  84  LEU   L C   
20194 O  O   . LEU   L  84  ? 1.4613 0.4559 1.5980 0.2982  -0.2959 0.1559  84  LEU   L O   
20195 C  CB  . LEU   L  84  ? 1.5471 0.4910 1.5242 0.1649  -0.2693 0.1156  84  LEU   L CB  
20196 C  CG  . LEU   L  84  ? 1.5719 0.4747 1.5126 0.1966  -0.2767 0.1713  84  LEU   L CG  
20197 C  CD1 . LEU   L  84  ? 1.5642 0.4942 1.5078 0.2063  -0.2791 0.1785  84  LEU   L CD1 
20198 C  CD2 . LEU   L  84  ? 1.5883 0.5572 1.4795 0.1805  -0.2742 0.1693  84  LEU   L CD2 
20199 N  N   . SER   L  85  ? 1.4684 0.6579 1.5600 0.1661  -0.3430 0.0715  85  SER   L N   
20200 C  CA  . SER   L  85  ? 1.5007 0.7248 1.5326 0.1468  -0.3452 0.0509  85  SER   L CA  
20201 C  C   . SER   L  85  ? 1.4713 0.7492 1.4744 0.1466  -0.3696 0.0720  85  SER   L C   
20202 O  O   . SER   L  85  ? 1.4656 0.7669 1.4313 0.1254  -0.3433 0.0720  85  SER   L O   
20203 C  CB  . SER   L  85  ? 1.5212 0.7595 1.5272 0.1424  -0.3281 0.0444  85  SER   L CB  
20204 O  OG  . SER   L  85  ? 1.5218 0.8378 1.5093 0.1249  -0.3041 -0.0014 85  SER   L OG  
20205 N  N   . ILE   L  86  ? 1.4826 0.7596 1.4705 0.1242  -0.3671 0.0891  86  ILE   L N   
20206 C  CA  . ILE   L  86  ? 1.4953 0.7240 1.4254 0.0941  -0.3630 0.0804  86  ILE   L CA  
20207 C  C   . ILE   L  86  ? 1.5231 0.6306 1.3929 0.0756  -0.3557 0.0949  86  ILE   L C   
20208 O  O   . ILE   L  86  ? 1.5458 0.5706 1.2755 0.0581  -0.3737 0.0706  86  ILE   L O   
20209 C  CB  . ILE   L  86  ? 1.4566 0.8282 1.4531 0.0640  -0.3708 0.0627  86  ILE   L CB  
20210 C  CG1 . ILE   L  86  ? 1.4724 0.8503 1.4024 0.0663  -0.3755 0.0691  86  ILE   L CG1 
20211 C  CG2 . ILE   L  86  ? 1.4635 0.8519 1.4637 0.0710  -0.3949 0.0669  86  ILE   L CG2 
20212 C  CD1 . ILE   L  86  ? 1.4656 0.8997 1.4061 0.0405  -0.3411 0.0409  86  ILE   L CD1 
20213 N  N   . ASN   L  87  ? 1.5847 0.6393 1.4271 0.0629  -0.3413 0.1379  87  ASN   L N   
20214 C  CA  . ASN   L  87  ? 1.5754 0.6360 1.4244 0.0249  -0.3468 0.1495  87  ASN   L CA  
20215 C  C   . ASN   L  87  ? 1.5685 0.6483 1.4272 0.0214  -0.3506 0.1384  87  ASN   L C   
20216 O  O   . ASN   L  87  ? 1.5157 0.5155 1.3478 -0.0148 -0.4366 0.1390  87  ASN   L O   
20217 C  CB  . ASN   L  87  ? 1.6307 0.6362 1.4349 0.0621  -0.3207 0.1812  87  ASN   L CB  
20218 C  CG  . ASN   L  87  ? 1.6481 0.6244 1.4626 0.0478  -0.2684 0.1834  87  ASN   L CG  
20219 O  OD1 . ASN   L  87  ? 1.6999 0.4459 1.4921 0.0372  -0.2320 0.1864  87  ASN   L OD1 
20220 N  ND2 . ASN   L  87  ? 1.6800 0.5821 1.4794 0.0498  -0.2543 0.1779  87  ASN   L ND2 
20221 N  N   . SER   L  88  ? 1.5441 0.6247 1.4726 -0.0122 -0.3577 0.1322  88  SER   L N   
20222 C  CA  . SER   L  88  ? 1.5265 0.5997 1.4544 0.0074  -0.3638 0.1484  88  SER   L CA  
20223 C  C   . SER   L  88  ? 1.4624 0.5442 1.4645 -0.0070 -0.3593 0.1493  88  SER   L C   
20224 O  O   . SER   L  88  ? 1.4936 0.4416 1.4562 -0.0338 -0.4378 0.1217  88  SER   L O   
20225 C  CB  . SER   L  88  ? 1.5330 0.6067 1.4351 0.0132  -0.3576 0.1435  88  SER   L CB  
20226 O  OG  . SER   L  88  ? 1.5705 0.5801 1.4560 0.0055  -0.3596 0.1674  88  SER   L OG  
20227 N  N   . ALA   L  89  ? 1.4060 0.5785 1.4518 0.0317  -0.3584 0.1668  89  ALA   L N   
20228 C  CA  . ALA   L  89  ? 1.3817 0.6027 1.4315 0.0352  -0.3436 0.1630  89  ALA   L CA  
20229 C  C   . ALA   L  89  ? 1.3876 0.6170 1.4158 0.0576  -0.3581 0.1932  89  ALA   L C   
20230 O  O   . ALA   L  89  ? 1.3965 0.6363 1.4487 0.0419  -0.3817 0.1827  89  ALA   L O   
20231 C  CB  . ALA   L  89  ? 1.3633 0.5797 1.4466 0.0557  -0.3388 0.1549  89  ALA   L CB  
20232 N  N   . ALA   L  90  ? 1.4568 0.6542 1.4055 0.0343  -0.3563 0.1926  90  ALA   L N   
20233 C  CA  . ALA   L  90  ? 1.4690 0.6936 1.3888 0.0614  -0.3546 0.2033  90  ALA   L CA  
20234 C  C   . ALA   L  90  ? 1.4779 0.6523 1.3598 0.0686  -0.3361 0.2181  90  ALA   L C   
20235 O  O   . ALA   L  90  ? 1.4642 0.5672 1.3256 0.0572  -0.2933 0.2321  90  ALA   L O   
20236 C  CB  . ALA   L  90  ? 1.5207 0.7955 1.3958 0.0506  -0.3900 0.2059  90  ALA   L CB  
20237 N  N   . ARG   L  91  ? 1.4989 0.6424 1.3935 0.0462  -0.2757 0.2144  91  ARG   L N   
20238 C  CA  . ARG   L  91  ? 1.4975 0.6207 1.3666 0.0515  -0.2760 0.1990  91  ARG   L CA  
20239 C  C   . ARG   L  91  ? 1.4788 0.6420 1.3965 0.0267  -0.2567 0.1462  91  ARG   L C   
20240 O  O   . ARG   L  91  ? 1.4821 0.6548 1.3814 0.0404  -0.2112 0.0822  91  ARG   L O   
20241 C  CB  . ARG   L  91  ? 1.5349 0.5832 1.3959 0.0425  -0.2572 0.2046  91  ARG   L CB  
20242 C  CG  . ARG   L  91  ? 1.5692 0.5296 1.3707 0.0416  -0.2565 0.2337  91  ARG   L CG  
20243 C  CD  . ARG   L  91  ? 1.6067 0.5321 1.3580 0.0520  -0.2317 0.2531  91  ARG   L CD  
20244 N  NE  . ARG   L  91  ? 1.6450 0.5950 1.3537 0.0532  -0.2456 0.2804  91  ARG   L NE  
20245 C  CZ  . ARG   L  91  ? 1.6982 0.6667 1.3715 0.0198  -0.2492 0.3139  91  ARG   L CZ  
20246 N  NH1 . ARG   L  91  ? 1.6796 0.7401 1.4137 -0.0334 -0.2260 0.2628  91  ARG   L NH1 
20247 N  NH2 . ARG   L  91  ? 1.7650 0.7310 1.3915 -0.0159 -0.2843 0.3188  91  ARG   L NH2 
20248 N  N   . ASN   L  92  ? 1.4717 0.6531 1.3912 -0.0032 -0.2569 0.1456  92  ASN   L N   
20249 C  CA  . ASN   L  92  ? 1.4695 0.6725 1.4349 -0.0587 -0.2709 0.1368  92  ASN   L CA  
20250 C  C   . ASN   L  92  ? 1.3992 0.6860 1.4737 -0.0452 -0.3277 0.0968  92  ASN   L C   
20251 O  O   . ASN   L  92  ? 1.4434 0.6126 1.4768 -0.1090 -0.3713 0.0371  92  ASN   L O   
20252 C  CB  . ASN   L  92  ? 1.4683 0.7375 1.4165 -0.0935 -0.2379 0.1282  92  ASN   L CB  
20253 C  CG  . ASN   L  92  ? 1.4878 0.8280 1.3813 -0.1334 -0.1715 0.0846  92  ASN   L CG  
20254 O  OD1 . ASN   L  92  ? 1.5157 0.9086 1.3949 -0.2082 -0.1284 -0.0094 92  ASN   L OD1 
20255 N  ND2 . ASN   L  92  ? 1.4734 0.9205 1.3999 -0.1349 -0.1186 0.1057  92  ASN   L ND2 
20256 N  N   . ILE   L  93  ? 1.3768 0.6264 1.4720 0.0083  -0.3511 0.1139  93  ILE   L N   
20257 C  CA  . ILE   L  93  ? 1.3104 0.5986 1.3653 0.0139  -0.3373 0.0674  93  ILE   L CA  
20258 C  C   . ILE   L  93  ? 1.3439 0.5266 1.3292 0.0415  -0.3512 0.0573  93  ILE   L C   
20259 O  O   . ILE   L  93  ? 1.2765 0.6237 1.3535 0.0246  -0.3842 -0.0092 93  ILE   L O   
20260 C  CB  . ILE   L  93  ? 1.2847 0.6113 1.3269 0.0256  -0.3361 0.0955  93  ILE   L CB  
20261 C  CG1 . ILE   L  93  ? 1.3071 0.5902 1.2969 0.0378  -0.3301 0.1132  93  ILE   L CG1 
20262 C  CG2 . ILE   L  93  ? 1.2398 0.6016 1.3525 0.0142  -0.3384 0.0785  93  ILE   L CG2 
20263 C  CD1 . ILE   L  93  ? 1.3038 0.5884 1.3064 0.0462  -0.3047 0.1184  93  ILE   L CD1 
20264 N  N   . GLN   L  94  ? 1.3554 0.4893 1.3273 0.0622  -0.3230 0.0544  94  GLN   L N   
20265 C  CA  . GLN   L  94  ? 1.3571 0.5256 1.3025 0.0522  -0.3066 0.0886  94  GLN   L CA  
20266 C  C   . GLN   L  94  ? 1.3582 0.4752 1.2863 0.0438  -0.2733 0.0699  94  GLN   L C   
20267 O  O   . GLN   L  94  ? 1.3437 0.3193 1.2631 -0.0099 -0.2756 -0.0171 94  GLN   L O   
20268 C  CB  . GLN   L  94  ? 1.4486 0.5881 1.3216 0.0655  -0.2853 0.1598  94  GLN   L CB  
20269 C  CG  . GLN   L  94  ? 1.4801 0.6562 1.3095 0.0692  -0.2609 0.1945  94  GLN   L CG  
20270 C  CD  . GLN   L  94  ? 1.5777 0.7811 1.3122 0.0642  -0.2556 0.2110  94  GLN   L CD  
20271 O  OE1 . GLN   L  94  ? 1.6401 0.8245 1.3595 0.0678  -0.1937 0.2645  94  GLN   L OE1 
20272 N  NE2 . GLN   L  94  ? 1.6167 0.7866 1.3056 0.0889  -0.2664 0.2100  94  GLN   L NE2 
20273 N  N   . HIS   L  95  ? 1.3006 0.4738 1.3001 0.0921  -0.2510 0.1022  95  HIS   L N   
20274 C  CA  . HIS   L  95  ? 1.2849 0.4520 1.3116 0.0885  -0.2100 0.1063  95  HIS   L CA  
20275 C  C   . HIS   L  95  ? 1.3238 0.4634 1.3010 0.0531  -0.2043 0.1085  95  HIS   L C   
20276 O  O   . HIS   L  95  ? 1.3477 0.4666 1.1528 0.0410  -0.2264 0.1607  95  HIS   L O   
20277 C  CB  . HIS   L  95  ? 1.2680 0.4608 1.3443 0.1248  -0.1695 0.1039  95  HIS   L CB  
20278 C  CG  . HIS   L  95  ? 1.2940 0.4418 1.4005 0.1417  -0.0816 0.1498  95  HIS   L CG  
20279 N  ND1 . HIS   L  95  ? 1.2908 0.4491 1.4595 0.1389  -0.0908 0.1737  95  HIS   L ND1 
20280 C  CD2 . HIS   L  95  ? 1.2799 0.4402 1.4507 0.1607  -0.0619 0.1584  95  HIS   L CD2 
20281 C  CE1 . HIS   L  95  ? 1.3090 0.4609 1.5143 0.1644  -0.0534 0.2254  95  HIS   L CE1 
20282 N  NE2 . HIS   L  95  ? 1.3028 0.4712 1.4680 0.1627  -0.0272 0.2101  95  HIS   L NE2 
20283 N  N   . LEU   L  96  ? 1.3012 0.4850 1.3148 0.0521  -0.2178 0.1157  96  LEU   L N   
20284 C  CA  . LEU   L  96  ? 1.3137 0.5537 1.3040 0.0138  -0.2581 0.0904  96  LEU   L CA  
20285 C  C   . LEU   L  96  ? 1.3093 0.5969 1.3036 0.0326  -0.2866 0.0811  96  LEU   L C   
20286 O  O   . LEU   L  96  ? 1.2567 0.6231 1.4037 -0.0736 -0.2927 0.0940  96  LEU   L O   
20287 C  CB  . LEU   L  96  ? 1.2935 0.4891 1.3251 0.0461  -0.2611 0.0857  96  LEU   L CB  
20288 C  CG  . LEU   L  96  ? 1.3433 0.4155 1.3710 0.0107  -0.2758 0.0799  96  LEU   L CG  
20289 C  CD1 . LEU   L  96  ? 1.3647 0.4448 1.3959 -0.0034 -0.2626 0.0860  96  LEU   L CD1 
20290 C  CD2 . LEU   L  96  ? 1.3281 0.3584 1.3871 0.0271  -0.2639 0.0807  96  LEU   L CD2 
20291 N  N   . LEU   L  97  ? 1.3637 0.7059 1.2377 0.0583  -0.2951 0.0280  97  LEU   L N   
20292 C  CA  . LEU   L  97  ? 1.3430 0.7234 1.1760 0.0691  -0.2589 -0.0183 97  LEU   L CA  
20293 C  C   . LEU   L  97  ? 1.3166 0.6916 1.1238 0.0365  -0.2917 -0.0591 97  LEU   L C   
20294 O  O   . LEU   L  97  ? 1.2249 0.7668 1.0423 -0.0328 -0.3116 -0.1721 97  LEU   L O   
20295 C  CB  . LEU   L  97  ? 1.3643 0.7752 1.1889 0.0501  -0.2986 0.0017  97  LEU   L CB  
20296 C  CG  . LEU   L  97  ? 1.3739 0.9155 1.2061 0.0592  -0.2721 0.0138  97  LEU   L CG  
20297 C  CD1 . LEU   L  97  ? 1.3956 1.0166 1.1663 0.0853  -0.3161 0.0343  97  LEU   L CD1 
20298 C  CD2 . LEU   L  97  ? 1.4275 1.0121 1.1474 0.0539  -0.2508 0.0306  97  LEU   L CD2 
20299 N  N   . TYR   L  98  ? 1.3076 0.6681 1.1646 0.0351  -0.2731 -0.0287 98  TYR   L N   
20300 C  CA  . TYR   L  98  ? 1.3336 0.6514 1.1330 0.0178  -0.2691 0.0042  98  TYR   L CA  
20301 C  C   . TYR   L  98  ? 1.3588 0.6035 1.2131 0.0120  -0.2554 -0.0298 98  TYR   L C   
20302 O  O   . TYR   L  98  ? 1.3552 0.5832 1.2514 0.0209  -0.2626 -0.0908 98  TYR   L O   
20303 C  CB  . TYR   L  98  ? 1.3322 0.6351 1.1439 0.0276  -0.2516 0.0426  98  TYR   L CB  
20304 C  CG  . TYR   L  98  ? 1.3411 0.6860 1.0416 0.0005  -0.2486 0.1058  98  TYR   L CG  
20305 C  CD1 . TYR   L  98  ? 1.3857 0.7222 1.0194 0.0008  -0.2483 0.0893  98  TYR   L CD1 
20306 C  CD2 . TYR   L  98  ? 1.3493 0.6366 1.0141 0.0024  -0.2571 0.0931  98  TYR   L CD2 
20307 C  CE1 . TYR   L  98  ? 1.3635 0.7467 1.0186 -0.0003 -0.2486 0.1222  98  TYR   L CE1 
20308 C  CE2 . TYR   L  98  ? 1.3079 0.7127 1.0138 -0.0226 -0.2637 0.1091  98  TYR   L CE2 
20309 C  CZ  . TYR   L  98  ? 1.3366 0.7336 0.9842 0.0126  -0.2594 0.1037  98  TYR   L CZ  
20310 O  OH  . TYR   L  98  ? 1.2827 0.7406 0.9584 0.0425  -0.3005 0.1315  98  TYR   L OH  
20311 N  N   . GLY   L  99  ? 1.3870 0.5920 1.2268 0.0243  -0.2156 -0.0053 99  GLY   L N   
20312 C  CA  . GLY   L  99  ? 1.3785 0.5729 1.2441 0.0113  -0.2083 0.0095  99  GLY   L CA  
20313 C  C   . GLY   L  99  ? 1.3510 0.5672 1.2290 -0.0052 -0.2071 0.0130  99  GLY   L C   
20314 O  O   . GLY   L  99  ? 1.3620 0.5880 1.1704 -0.0068 -0.2327 0.0196  99  GLY   L O   
20315 N  N   . LYS   L  100 ? 1.4238 0.5469 1.2378 0.0544  -0.1893 0.0661  100 LYS   L N   
20316 C  CA  . LYS   L  100 ? 1.4657 0.5404 1.2270 0.0604  -0.1942 0.0674  100 LYS   L CA  
20317 C  C   . LYS   L  100 ? 1.5124 0.5387 1.2104 0.0452  -0.1995 0.0662  100 LYS   L C   
20318 O  O   . LYS   L  100 ? 1.6143 0.5012 1.2303 0.0809  -0.2602 0.0339  100 LYS   L O   
20319 C  CB  . LYS   L  100 ? 1.4726 0.5540 1.2196 0.0816  -0.1952 0.0847  100 LYS   L CB  
20320 C  CG  . LYS   L  100 ? 1.4476 0.5248 1.2574 0.0801  -0.1819 0.0708  100 LYS   L CG  
20321 C  CD  . LYS   L  100 ? 1.4179 0.6089 1.3016 0.0477  -0.1634 0.0538  100 LYS   L CD  
20322 C  CE  . LYS   L  100 ? 1.3700 0.6368 1.3036 0.0406  -0.1868 0.0725  100 LYS   L CE  
20323 N  NZ  . LYS   L  100 ? 1.3690 0.6879 1.2923 0.0350  -0.1980 0.0742  100 LYS   L NZ  
20324 N  N   . ARG   L  101 ? 1.5007 0.4440 1.2102 0.0294  -0.1860 0.0465  101 ARG   L N   
20325 C  CA  . ARG   L  101 ? 1.4862 0.4046 1.2063 0.0536  -0.2073 0.0627  101 ARG   L CA  
20326 C  C   . ARG   L  101 ? 1.4847 0.4731 1.2158 0.1118  -0.2092 0.0213  101 ARG   L C   
20327 O  O   . ARG   L  101 ? 1.3981 0.4943 1.2845 0.1754  -0.2711 -0.0483 101 ARG   L O   
20328 C  CB  . ARG   L  101 ? 1.5537 0.4203 1.2091 0.0205  -0.1865 0.0522  101 ARG   L CB  
20329 C  CG  . ARG   L  101 ? 1.5994 0.4568 1.1756 0.0295  -0.1815 0.0540  101 ARG   L CG  
20330 C  CD  . ARG   L  101 ? 1.6071 0.4953 1.1176 0.0206  -0.2211 0.0584  101 ARG   L CD  
20331 N  NE  . ARG   L  101 ? 1.6295 0.4969 1.0966 0.0343  -0.2541 0.0524  101 ARG   L NE  
20332 C  CZ  . ARG   L  101 ? 1.6420 0.4794 1.0794 0.0301  -0.2655 0.0651  101 ARG   L CZ  
20333 N  NH1 . ARG   L  101 ? 1.6914 0.5369 1.0379 -0.0176 -0.2473 0.0652  101 ARG   L NH1 
20334 N  NH2 . ARG   L  101 ? 1.6474 0.4839 1.0746 0.0303  -0.2656 0.0669  101 ARG   L NH2 
20335 N  N   . PHE   L  102 ? 1.4695 0.3919 1.2097 0.1493  -0.1990 0.0216  102 PHE   L N   
20336 C  CA  . PHE   L  102 ? 1.4628 0.4710 1.2095 0.1723  -0.1675 0.0295  102 PHE   L CA  
20337 C  C   . PHE   L  102 ? 1.4739 0.5723 1.1950 0.1635  -0.1468 0.0203  102 PHE   L C   
20338 O  O   . PHE   L  102 ? 1.5806 0.6582 1.1023 0.1710  -0.1858 0.1358  102 PHE   L O   
20339 C  CB  . PHE   L  102 ? 1.4884 0.3921 1.1969 0.1921  -0.1448 0.0663  102 PHE   L CB  
20340 C  CG  . PHE   L  102 ? 1.4995 0.3970 1.2150 0.2146  -0.1545 0.1244  102 PHE   L CG  
20341 C  CD1 . PHE   L  102 ? 1.5390 0.4151 1.1881 0.2069  -0.1695 0.1235  102 PHE   L CD1 
20342 C  CD2 . PHE   L  102 ? 1.4955 0.4177 1.2295 0.2286  -0.1440 0.1502  102 PHE   L CD2 
20343 C  CE1 . PHE   L  102 ? 1.5686 0.4197 1.1995 0.2140  -0.1715 0.1442  102 PHE   L CE1 
20344 C  CE2 . PHE   L  102 ? 1.5160 0.4560 1.2284 0.2166  -0.1372 0.1468  102 PHE   L CE2 
20345 C  CZ  . PHE   L  102 ? 1.5450 0.4251 1.2165 0.2097  -0.1584 0.1581  102 PHE   L CZ  
20346 N  N   . PHE   L  103 ? 1.4771 0.5560 1.1864 0.1277  -0.1272 0.0251  103 PHE   L N   
20347 C  CA  . PHE   L  103 ? 1.4388 0.5184 1.1845 0.0947  -0.1370 0.0117  103 PHE   L CA  
20348 C  C   . PHE   L  103 ? 1.4432 0.4728 1.1719 0.0715  -0.1620 0.0372  103 PHE   L C   
20349 O  O   . PHE   L  103 ? 1.4288 0.4514 1.2000 0.0912  -0.1415 0.0681  103 PHE   L O   
20350 C  CB  . PHE   L  103 ? 1.4371 0.4872 1.2052 0.0596  -0.0882 -0.0136 103 PHE   L CB  
20351 C  CG  . PHE   L  103 ? 1.4480 0.4933 1.1920 0.0283  -0.0553 -0.0331 103 PHE   L CG  
20352 C  CD1 . PHE   L  103 ? 1.4626 0.5021 1.1954 0.0264  -0.0453 -0.0125 103 PHE   L CD1 
20353 C  CD2 . PHE   L  103 ? 1.4175 0.5167 1.1775 -0.0237 -0.0533 -0.0215 103 PHE   L CD2 
20354 C  CE1 . PHE   L  103 ? 1.4423 0.5198 1.1560 0.0418  -0.0733 -0.0423 103 PHE   L CE1 
20355 C  CE2 . PHE   L  103 ? 1.3789 0.5030 1.1569 -0.0269 -0.0737 -0.0413 103 PHE   L CE2 
20356 C  CZ  . PHE   L  103 ? 1.3911 0.4843 1.1341 0.0426  -0.0730 -0.0222 103 PHE   L CZ  
20357 N  N   . PRO   L  104 ? 1.4982 0.4048 1.1768 0.0651  -0.1866 0.0670  104 PRO   L N   
20358 C  CA  . PRO   L  104 ? 1.5155 0.4248 1.2039 0.0381  -0.2160 0.0627  104 PRO   L CA  
20359 C  C   . PRO   L  104 ? 1.4785 0.3647 1.2249 0.0128  -0.2226 0.0401  104 PRO   L C   
20360 O  O   . PRO   L  104 ? 1.5103 0.3203 1.2859 -0.0293 -0.2675 0.0573  104 PRO   L O   
20361 C  CB  . PRO   L  104 ? 1.5485 0.4280 1.1886 0.0753  -0.2091 0.0664  104 PRO   L CB  
20362 C  CG  . PRO   L  104 ? 1.5398 0.4471 1.1742 0.0842  -0.2241 0.0893  104 PRO   L CG  
20363 C  CD  . PRO   L  104 ? 1.5055 0.3677 1.1826 0.0719  -0.2123 0.0743  104 PRO   L CD  
20364 N  N   . TYR   L  105 ? 1.4831 0.3772 1.2718 0.0297  -0.2589 0.0051  105 TYR   L N   
20365 C  CA  . TYR   L  105 ? 1.5027 0.4904 1.2699 0.0311  -0.2539 0.0409  105 TYR   L CA  
20366 C  C   . TYR   L  105 ? 1.5553 0.5679 1.2630 0.0137  -0.2847 -0.0429 105 TYR   L C   
20367 O  O   . TYR   L  105 ? 1.6169 0.6859 1.2751 0.0477  -0.3365 0.0505  105 TYR   L O   
20368 C  CB  . TYR   L  105 ? 1.4857 0.5420 1.3533 0.0207  -0.2692 0.0481  105 TYR   L CB  
20369 C  CG  . TYR   L  105 ? 1.5401 0.5389 1.3470 -0.0380 -0.2973 0.0699  105 TYR   L CG  
20370 C  CD1 . TYR   L  105 ? 1.5097 0.5364 1.3453 -0.0605 -0.2805 0.0605  105 TYR   L CD1 
20371 C  CD2 . TYR   L  105 ? 1.6002 0.5432 1.4115 0.0353  -0.3467 0.0912  105 TYR   L CD2 
20372 C  CE1 . TYR   L  105 ? 1.5375 0.5206 1.3645 -0.0022 -0.2750 0.0674  105 TYR   L CE1 
20373 C  CE2 . TYR   L  105 ? 1.6181 0.5477 1.3538 0.0492  -0.3672 0.0962  105 TYR   L CE2 
20374 C  CZ  . TYR   L  105 ? 1.5943 0.4848 1.3611 0.0343  -0.3191 0.0421  105 TYR   L CZ  
20375 O  OH  . TYR   L  105 ? 1.6122 0.4089 1.4271 0.0624  -0.2607 0.1083  105 TYR   L OH  
20376 N  N   . TYR   L  106 ? 1.6110 0.6172 1.1840 -0.0005 -0.2559 -0.0457 106 TYR   L N   
20377 C  CA  . TYR   L  106 ? 1.6228 0.6284 1.1846 -0.0084 -0.2150 -0.0903 106 TYR   L CA  
20378 C  C   . TYR   L  106 ? 1.6278 0.4533 1.1552 -0.0506 -0.2172 -0.1048 106 TYR   L C   
20379 O  O   . TYR   L  106 ? 1.6550 0.4918 1.1069 -0.0442 -0.2135 -0.1231 106 TYR   L O   
20380 C  CB  . TYR   L  106 ? 1.6407 0.6700 1.2233 0.0637  -0.1854 -0.1034 106 TYR   L CB  
20381 C  CG  . TYR   L  106 ? 1.7743 0.7928 1.3140 0.1258  -0.1175 -0.1713 106 TYR   L CG  
20382 C  CD1 . TYR   L  106 ? 1.7962 0.7850 1.3745 0.1332  -0.0676 -0.2012 106 TYR   L CD1 
20383 C  CD2 . TYR   L  106 ? 1.8248 0.7816 1.3925 0.2369  -0.0330 -0.1103 106 TYR   L CD2 
20384 C  CE1 . TYR   L  106 ? 1.8465 0.9000 1.4644 0.2080  -0.0446 -0.2231 106 TYR   L CE1 
20385 C  CE2 . TYR   L  106 ? 1.9023 0.9401 1.4835 0.3228  0.0128  -0.1162 106 TYR   L CE2 
20386 C  CZ  . TYR   L  106 ? 1.8844 0.9036 1.5464 0.3004  0.0003  -0.1687 106 TYR   L CZ  
20387 O  OH  . TYR   L  106 ? 1.8252 1.3472 1.6290 0.3693  0.0791  -0.1446 106 TYR   L OH  
20388 N  N   . VAL   L  107 ? 1.5835 0.3697 1.2066 -0.0564 -0.2015 -0.1032 107 VAL   L N   
20389 C  CA  . VAL   L  107 ? 1.5856 0.3953 1.2671 -0.0528 -0.2148 -0.0869 107 VAL   L CA  
20390 C  C   . VAL   L  107 ? 1.6362 0.3604 1.2885 -0.0354 -0.2495 -0.0807 107 VAL   L C   
20391 O  O   . VAL   L  107 ? 1.5608 0.2672 1.3086 -0.0895 -0.2780 -0.1324 107 VAL   L O   
20392 C  CB  . VAL   L  107 ? 1.5607 0.4481 1.2484 -0.0291 -0.1978 -0.0828 107 VAL   L CB  
20393 C  CG1 . VAL   L  107 ? 1.5540 0.4778 1.2433 -0.0343 -0.1912 -0.0495 107 VAL   L CG1 
20394 C  CG2 . VAL   L  107 ? 1.5616 0.4583 1.2986 -0.0679 -0.1881 -0.0909 107 VAL   L CG2 
20395 N  N   . HIS   L  108 ? 1.6475 0.4878 1.3336 -0.0706 -0.2706 -0.0489 108 HIS   L N   
20396 C  CA  . HIS   L  108 ? 1.7556 0.6418 1.2991 -0.0321 -0.2777 -0.0493 108 HIS   L CA  
20397 C  C   . HIS   L  108 ? 1.7353 0.5613 1.2126 -0.0512 -0.2972 -0.0123 108 HIS   L C   
20398 O  O   . HIS   L  108 ? 1.6901 0.5405 1.1602 -0.0028 -0.3092 -0.0463 108 HIS   L O   
20399 C  CB  . HIS   L  108 ? 1.9455 0.7619 1.3781 -0.1635 -0.2453 -0.1884 108 HIS   L CB  
20400 C  CG  . HIS   L  108 ? 2.1644 1.1615 1.4219 -0.2154 -0.0943 -0.2644 108 HIS   L CG  
20401 N  ND1 . HIS   L  108 ? 2.3538 1.2121 1.6018 -0.2231 -0.0657 -0.3567 108 HIS   L ND1 
20402 C  CD2 . HIS   L  108 ? 2.2736 1.0564 1.5835 -0.3989 -0.0381 -0.2461 108 HIS   L CD2 
20403 C  CE1 . HIS   L  108 ? 2.3670 1.3135 1.6573 -0.1560 0.0328  -0.3084 108 HIS   L CE1 
20404 N  NE2 . HIS   L  108 ? 2.4284 1.3578 1.5583 -0.2668 0.0418  -0.3711 108 HIS   L NE2 
20405 N  N   . THR   L  109 ? 1.7051 0.4787 1.2581 0.0100  -0.3576 -0.0598 109 THR   L N   
20406 C  CA  . THR   L  109 ? 1.6809 0.4113 1.2851 -0.0062 -0.3708 0.0266  109 THR   L CA  
20407 C  C   . THR   L  109 ? 1.6289 0.3953 1.3267 0.0336  -0.3586 0.0347  109 THR   L C   
20408 O  O   . THR   L  109 ? 1.6687 0.2991 1.3314 0.0487  -0.3482 0.0259  109 THR   L O   
20409 C  CB  . THR   L  109 ? 1.6634 0.4213 1.2630 -0.0131 -0.3977 0.0364  109 THR   L CB  
20410 O  OG1 . THR   L  109 ? 1.7076 0.2397 1.2258 -0.0304 -0.4261 0.1488  109 THR   L OG1 
20411 C  CG2 . THR   L  109 ? 1.6248 0.4558 1.2741 -0.0084 -0.3935 0.0312  109 THR   L CG2 
20412 N  N   . ILE   L  110 ? 1.6132 0.4317 1.3536 0.0561  -0.3587 0.0499  110 ILE   L N   
20413 C  CA  . ILE   L  110 ? 1.6175 0.5752 1.3762 0.0593  -0.3756 0.0323  110 ILE   L CA  
20414 C  C   . ILE   L  110 ? 1.5861 0.6059 1.3734 0.0380  -0.3547 0.0122  110 ILE   L C   
20415 O  O   . ILE   L  110 ? 1.5500 0.7023 1.3699 -0.0024 -0.3344 0.0569  110 ILE   L O   
20416 C  CB  . ILE   L  110 ? 1.6382 0.5670 1.3920 0.0644  -0.3869 0.0530  110 ILE   L CB  
20417 C  CG1 . ILE   L  110 ? 1.6367 0.6813 1.3831 0.1160  -0.3792 0.0224  110 ILE   L CG1 
20418 C  CG2 . ILE   L  110 ? 1.6450 0.5969 1.4447 0.0772  -0.4042 0.0344  110 ILE   L CG2 
20419 C  CD1 . ILE   L  110 ? 1.6702 0.6955 1.3981 0.0920  -0.3655 -0.0057 110 ILE   L CD1 
20420 N  N   . ILE   L  111 ? 1.6101 0.5628 1.4209 0.0203  -0.3685 0.0181  111 ILE   L N   
20421 C  CA  . ILE   L  111 ? 1.6004 0.5643 1.4219 0.0055  -0.3668 -0.0088 111 ILE   L CA  
20422 C  C   . ILE   L  111 ? 1.5800 0.5311 1.4449 -0.0094 -0.3661 0.0120  111 ILE   L C   
20423 O  O   . ILE   L  111 ? 1.5495 0.4809 1.4622 -0.0219 -0.4036 -0.0088 111 ILE   L O   
20424 C  CB  . ILE   L  111 ? 1.6526 0.5434 1.3840 0.0033  -0.3684 -0.0723 111 ILE   L CB  
20425 C  CG1 . ILE   L  111 ? 1.7237 0.5243 1.3986 0.0189  -0.3513 -0.0431 111 ILE   L CG1 
20426 C  CG2 . ILE   L  111 ? 1.6275 0.5430 1.3935 0.0204  -0.3564 -0.1192 111 ILE   L CG2 
20427 C  CD1 . ILE   L  111 ? 1.7523 0.5112 1.4165 0.0258  -0.3345 -0.0657 111 ILE   L CD1 
20428 N  N   . ALA   L  112 ? 1.5640 0.5087 1.4336 -0.0141 -0.3736 0.0245  112 ALA   L N   
20429 C  CA  . ALA   L  112 ? 1.5666 0.5090 1.4728 0.0348  -0.3855 0.0152  112 ALA   L CA  
20430 C  C   . ALA   L  112 ? 1.5891 0.4739 1.4943 0.0076  -0.3829 -0.0170 112 ALA   L C   
20431 O  O   . ALA   L  112 ? 1.5730 0.3353 1.4985 0.0314  -0.3710 0.0121  112 ALA   L O   
20432 C  CB  . ALA   L  112 ? 1.5894 0.5584 1.4633 0.0197  -0.3718 0.0437  112 ALA   L CB  
20433 N  N   . GLY   L  113 ? 1.5984 0.5001 1.5489 0.0576  -0.4035 -0.0371 113 GLY   L N   
20434 C  CA  . GLY   L  113 ? 1.6049 0.5606 1.5642 0.1012  -0.4113 -0.0358 113 GLY   L CA  
20435 C  C   . GLY   L  113 ? 1.6414 0.6459 1.5495 0.0889  -0.4258 -0.0784 113 GLY   L C   
20436 O  O   . GLY   L  113 ? 1.6746 0.5555 1.5977 0.1484  -0.4562 -0.0475 113 GLY   L O   
20437 N  N   . LEU   L  114 ? 1.6000 0.7175 1.5488 0.1102  -0.4213 0.0177  114 LEU   L N   
20438 C  CA  . LEU   L  114 ? 1.5503 0.7944 1.5717 0.1192  -0.4257 0.0292  114 LEU   L CA  
20439 C  C   . LEU   L  114 ? 1.5705 0.8067 1.5879 0.1299  -0.4189 0.0522  114 LEU   L C   
20440 O  O   . LEU   L  114 ? 1.5348 0.7949 1.5334 0.1915  -0.4714 0.0667  114 LEU   L O   
20441 C  CB  . LEU   L  114 ? 1.5064 0.8038 1.6295 0.0820  -0.4095 0.0377  114 LEU   L CB  
20442 C  CG  . LEU   L  114 ? 1.4691 0.8474 1.6659 0.0695  -0.4020 0.0385  114 LEU   L CG  
20443 C  CD1 . LEU   L  114 ? 1.4667 0.8135 1.6952 0.0403  -0.3867 0.0254  114 LEU   L CD1 
20444 C  CD2 . LEU   L  114 ? 1.4907 0.8553 1.6969 0.0901  -0.3937 0.0087  114 LEU   L CD2 
20445 N  N   . ASP   L  115 ? 1.6140 0.8734 1.5922 0.1252  -0.3817 0.0607  115 ASP   L N   
20446 C  CA  . ASP   L  115 ? 1.6265 0.9388 1.5916 0.1068  -0.3253 0.0453  115 ASP   L CA  
20447 C  C   . ASP   L  115 ? 1.6477 0.9137 1.6535 0.0846  -0.3583 0.0751  115 ASP   L C   
20448 O  O   . ASP   L  115 ? 1.6058 0.9821 1.6549 0.1100  -0.3982 -0.0044 115 ASP   L O   
20449 C  CB  . ASP   L  115 ? 1.6249 0.9672 1.5806 0.1116  -0.2714 0.0635  115 ASP   L CB  
20450 C  CG  . ASP   L  115 ? 1.6616 0.9591 1.5124 0.1196  -0.2574 -0.0006 115 ASP   L CG  
20451 O  OD1 . ASP   L  115 ? 1.6629 1.0137 1.5818 0.1562  -0.2552 0.0417  115 ASP   L OD1 
20452 O  OD2 . ASP   L  115 ? 1.6689 0.9561 1.5660 0.1144  -0.1824 -0.0368 115 ASP   L OD2 
20453 N  N   . GLU   L  116 ? 1.6562 0.8797 1.7016 0.0803  -0.3826 0.0924  116 GLU   L N   
20454 C  CA  . GLU   L  116 ? 1.6637 0.8955 1.7457 0.0999  -0.3643 0.1372  116 GLU   L CA  
20455 C  C   . GLU   L  116 ? 1.6463 0.7910 1.7997 0.1559  -0.3699 0.1526  116 GLU   L C   
20456 O  O   . GLU   L  116 ? 1.6524 0.7625 1.8929 0.1362  -0.3182 0.0485  116 GLU   L O   
20457 C  CB  . GLU   L  116 ? 1.6820 1.0377 1.7712 0.1024  -0.2969 0.2048  116 GLU   L CB  
20458 C  CG  . GLU   L  116 ? 1.6618 1.1729 1.7408 0.0634  -0.2627 0.2148  116 GLU   L CG  
20459 C  CD  . GLU   L  116 ? 1.7198 1.2974 1.7653 0.0326  -0.2056 0.2571  116 GLU   L CD  
20460 O  OE1 . GLU   L  116 ? 1.6879 1.3325 1.8154 -0.0610 -0.1285 0.2449  116 GLU   L OE1 
20461 O  OE2 . GLU   L  116 ? 1.7039 1.4646 1.6585 0.0389  -0.1533 0.3160  116 GLU   L OE2 
20462 N  N   . ASP   L  117 ? 1.7160 0.8107 1.7935 0.1678  -0.3857 0.1374  117 ASP   L N   
20463 C  CA  . ASP   L  117 ? 1.7151 0.8805 1.8121 0.2044  -0.4080 0.1392  117 ASP   L CA  
20464 C  C   . ASP   L  117 ? 1.6320 0.8253 1.7739 0.2321  -0.4411 0.1095  117 ASP   L C   
20465 O  O   . ASP   L  117 ? 1.6035 0.7182 1.7378 0.3530  -0.4853 0.1422  117 ASP   L O   
20466 C  CB  . ASP   L  117 ? 1.7797 1.0100 1.8032 0.1794  -0.4154 0.1033  117 ASP   L CB  
20467 C  CG  . ASP   L  117 ? 1.8471 1.0970 1.8295 0.1611  -0.3710 0.1135  117 ASP   L CG  
20468 O  OD1 . ASP   L  117 ? 1.9043 1.1062 1.9078 0.1686  -0.3488 0.0698  117 ASP   L OD1 
20469 O  OD2 . ASP   L  117 ? 1.8956 1.2150 1.8852 0.1791  -0.3535 0.0471  117 ASP   L OD2 
20470 N  N   . GLY   L  118 ? 1.6355 0.8507 1.7461 0.1960  -0.4150 0.0900  118 GLY   L N   
20471 C  CA  . GLY   L  118 ? 1.6065 0.9041 1.7515 0.1453  -0.4412 0.0853  118 GLY   L CA  
20472 C  C   . GLY   L  118 ? 1.5771 0.9054 1.7003 0.1153  -0.4828 0.1109  118 GLY   L C   
20473 O  O   . GLY   L  118 ? 1.5623 0.8936 1.6107 0.0886  -0.5633 0.1115  118 GLY   L O   
20474 N  N   . LYS   L  119 ? 1.5610 0.9377 1.6863 0.1221  -0.4936 0.1152  119 LYS   L N   
20475 C  CA  . LYS   L  119 ? 1.5865 0.9408 1.6673 0.1249  -0.4615 0.0999  119 LYS   L CA  
20476 C  C   . LYS   L  119 ? 1.5704 0.8351 1.6631 0.1152  -0.4249 0.1195  119 LYS   L C   
20477 O  O   . LYS   L  119 ? 1.6121 0.8022 1.7440 0.0908  -0.3904 0.0726  119 LYS   L O   
20478 C  CB  . LYS   L  119 ? 1.6496 1.0731 1.6628 0.1382  -0.4472 0.0951  119 LYS   L CB  
20479 C  CG  . LYS   L  119 ? 1.7210 1.2134 1.6485 0.1643  -0.4744 0.0578  119 LYS   L CG  
20480 C  CD  . LYS   L  119 ? 1.8293 1.3349 1.6569 0.1757  -0.4782 0.0140  119 LYS   L CD  
20481 C  CE  . LYS   L  119 ? 1.8810 1.4085 1.6654 0.2097  -0.5131 -0.0399 119 LYS   L CE  
20482 N  NZ  . LYS   L  119 ? 1.9778 1.4622 1.6748 0.2070  -0.4642 -0.0585 119 LYS   L NZ  
20483 N  N   . GLY   L  120 ? 1.5754 0.8569 1.6065 0.1748  -0.4172 0.1746  120 GLY   L N   
20484 C  CA  . GLY   L  120 ? 1.5414 0.8068 1.5531 0.1839  -0.3636 0.1685  120 GLY   L CA  
20485 C  C   . GLY   L  120 ? 1.5515 0.7103 1.4580 0.2214  -0.3644 0.2114  120 GLY   L C   
20486 O  O   . GLY   L  120 ? 1.5210 0.6635 1.4388 0.2565  -0.3253 0.2886  120 GLY   L O   
20487 N  N   . ALA   L  121 ? 1.5357 0.6659 1.4573 0.2165  -0.3464 0.1843  121 ALA   L N   
20488 C  CA  . ALA   L  121 ? 1.5452 0.6520 1.4488 0.1994  -0.3340 0.1473  121 ALA   L CA  
20489 C  C   . ALA   L  121 ? 1.5248 0.6937 1.3859 0.1962  -0.3546 0.0890  121 ALA   L C   
20490 O  O   . ALA   L  121 ? 1.4715 0.7269 1.3518 0.1885  -0.4317 0.0775  121 ALA   L O   
20491 C  CB  . ALA   L  121 ? 1.5565 0.6335 1.4544 0.2287  -0.3401 0.1828  121 ALA   L CB  
20492 N  N   . VAL   L  122 ? 1.5376 0.6907 1.4419 0.2085  -0.3609 0.0831  122 VAL   L N   
20493 C  CA  . VAL   L  122 ? 1.5456 0.7206 1.3955 0.1974  -0.3800 0.0636  122 VAL   L CA  
20494 C  C   . VAL   L  122 ? 1.5255 0.6197 1.4052 0.1738  -0.4156 0.0569  122 VAL   L C   
20495 O  O   . VAL   L  122 ? 1.5669 0.5563 1.3895 0.2300  -0.4503 0.1076  122 VAL   L O   
20496 C  CB  . VAL   L  122 ? 1.5842 0.7345 1.4401 0.1858  -0.3304 0.0717  122 VAL   L CB  
20497 C  CG1 . VAL   L  122 ? 1.5846 0.7294 1.4355 0.1895  -0.3288 0.0745  122 VAL   L CG1 
20498 C  CG2 . VAL   L  122 ? 1.6274 0.8135 1.4752 0.1853  -0.2827 0.0425  122 VAL   L CG2 
20499 N  N   . TYR   L  123 ? 1.5558 0.5891 1.3803 0.1322  -0.3870 0.0307  123 TYR   L N   
20500 C  CA  . TYR   L  123 ? 1.5609 0.6965 1.3495 0.0988  -0.3887 0.0117  123 TYR   L CA  
20501 C  C   . TYR   L  123 ? 1.5223 0.6501 1.2495 0.0360  -0.3838 -0.0096 123 TYR   L C   
20502 O  O   . TYR   L  123 ? 1.4687 0.5117 1.2376 0.0154  -0.4079 -0.0307 123 TYR   L O   
20503 C  CB  . TYR   L  123 ? 1.5774 0.7451 1.3496 0.0540  -0.3997 -0.0304 123 TYR   L CB  
20504 C  CG  . TYR   L  123 ? 1.6144 0.9181 1.3218 0.0990  -0.4369 -0.0146 123 TYR   L CG  
20505 C  CD1 . TYR   L  123 ? 1.6325 0.9183 1.3366 0.1195  -0.4246 -0.0428 123 TYR   L CD1 
20506 C  CD2 . TYR   L  123 ? 1.6410 0.9638 1.2997 0.0891  -0.4288 -0.0421 123 TYR   L CD2 
20507 C  CE1 . TYR   L  123 ? 1.6726 0.8781 1.3527 0.1282  -0.4421 -0.0571 123 TYR   L CE1 
20508 C  CE2 . TYR   L  123 ? 1.6609 0.9055 1.3201 0.0955  -0.4444 -0.0617 123 TYR   L CE2 
20509 C  CZ  . TYR   L  123 ? 1.6781 0.9091 1.3372 0.1137  -0.4551 -0.0627 123 TYR   L CZ  
20510 O  OH  . TYR   L  123 ? 1.7590 0.9739 1.3303 0.0986  -0.4728 -0.0331 123 TYR   L OH  
20511 N  N   . SER   L  124 ? 1.4830 0.7202 1.2653 0.0375  -0.3843 -0.0043 124 SER   L N   
20512 C  CA  . SER   L  124 ? 1.4236 0.7892 1.2512 0.0120  -0.4103 0.0053  124 SER   L CA  
20513 C  C   . SER   L  124 ? 1.4231 0.7061 1.2082 0.0033  -0.4195 0.0046  124 SER   L C   
20514 O  O   . SER   L  124 ? 1.2873 0.7133 1.1542 0.0073  -0.5153 -0.0030 124 SER   L O   
20515 C  CB  . SER   L  124 ? 1.4960 0.8097 1.3274 -0.0113 -0.3907 -0.0248 124 SER   L CB  
20516 O  OG  . SER   L  124 ? 1.6115 0.9302 1.3432 -0.0086 -0.2919 -0.0193 124 SER   L OG  
20517 N  N   . PHE   L  125 ? 1.4319 0.6408 1.2045 0.0227  -0.4143 0.0156  125 PHE   L N   
20518 C  CA  . PHE   L  125 ? 1.4337 0.6339 1.2206 0.0257  -0.4005 0.0413  125 PHE   L CA  
20519 C  C   . PHE   L  125 ? 1.4411 0.6401 1.2402 0.0310  -0.3996 0.0487  125 PHE   L C   
20520 O  O   . PHE   L  125 ? 1.4210 0.7959 1.1888 0.0706  -0.3301 0.0569  125 PHE   L O   
20521 C  CB  . PHE   L  125 ? 1.4271 0.6375 1.2259 -0.0265 -0.4236 0.0586  125 PHE   L CB  
20522 C  CG  . PHE   L  125 ? 1.4785 0.6419 1.2351 -0.0170 -0.4322 0.1032  125 PHE   L CG  
20523 C  CD1 . PHE   L  125 ? 1.5071 0.6638 1.2335 -0.0266 -0.4064 0.1158  125 PHE   L CD1 
20524 C  CD2 . PHE   L  125 ? 1.4919 0.6409 1.2292 -0.0131 -0.4518 0.1164  125 PHE   L CD2 
20525 C  CE1 . PHE   L  125 ? 1.5145 0.6440 1.1870 -0.0472 -0.4386 0.1477  125 PHE   L CE1 
20526 C  CE2 . PHE   L  125 ? 1.5475 0.5908 1.2221 -0.0286 -0.4523 0.1473  125 PHE   L CE2 
20527 C  CZ  . PHE   L  125 ? 1.5432 0.6076 1.1941 -0.0333 -0.4628 0.1444  125 PHE   L CZ  
20528 N  N   . ASP   L  126 ? 1.4268 0.5860 1.2687 0.0514  -0.4148 0.1079  126 ASP   L N   
20529 C  CA  . ASP   L  126 ? 1.5308 0.5222 1.3022 0.0776  -0.4066 0.1669  126 ASP   L CA  
20530 C  C   . ASP   L  126 ? 1.5394 0.4321 1.2517 0.1345  -0.4252 0.2191  126 ASP   L C   
20531 O  O   . ASP   L  126 ? 1.5443 0.3994 1.2927 0.1750  -0.4719 0.2800  126 ASP   L O   
20532 C  CB  . ASP   L  126 ? 1.5388 0.5299 1.3321 0.1090  -0.3978 0.1620  126 ASP   L CB  
20533 C  CG  . ASP   L  126 ? 1.5592 0.5495 1.3594 0.1121  -0.3566 0.1625  126 ASP   L CG  
20534 O  OD1 . ASP   L  126 ? 1.6042 0.5828 1.4233 0.0745  -0.2807 0.0940  126 ASP   L OD1 
20535 O  OD2 . ASP   L  126 ? 1.6213 0.3779 1.3391 0.2268  -0.4092 0.1494  126 ASP   L OD2 
20536 N  N   . PRO   L  127 ? 1.5720 0.4420 1.2016 0.1612  -0.4050 0.2264  127 PRO   L N   
20537 C  CA  . PRO   L  127 ? 1.5984 0.4148 1.1556 0.2092  -0.3917 0.2235  127 PRO   L CA  
20538 C  C   . PRO   L  127 ? 1.6721 0.4244 1.2123 0.2080  -0.3487 0.2596  127 PRO   L C   
20539 O  O   . PRO   L  127 ? 1.7529 0.3486 1.2147 0.2667  -0.3677 0.2913  127 PRO   L O   
20540 C  CB  . PRO   L  127 ? 1.6257 0.3868 1.1171 0.2116  -0.3609 0.2424  127 PRO   L CB  
20541 C  CG  . PRO   L  127 ? 1.5831 0.4408 1.1284 0.1953  -0.4027 0.2486  127 PRO   L CG  
20542 C  CD  . PRO   L  127 ? 1.5547 0.4682 1.1604 0.2123  -0.4245 0.2482  127 PRO   L CD  
20543 N  N   . VAL   L  128 ? 1.6229 0.4115 1.2011 0.2175  -0.3167 0.1713  128 VAL   L N   
20544 C  CA  . VAL   L  128 ? 1.5630 0.4333 1.2653 0.1920  -0.2703 0.0786  128 VAL   L CA  
20545 C  C   . VAL   L  128 ? 1.5632 0.4550 1.2632 0.1911  -0.2661 0.0877  128 VAL   L C   
20546 O  O   . VAL   L  128 ? 1.6123 0.4555 1.3293 0.1412  -0.2078 0.0311  128 VAL   L O   
20547 C  CB  . VAL   L  128 ? 1.5317 0.4210 1.2838 0.2143  -0.3077 0.0591  128 VAL   L CB  
20548 C  CG1 . VAL   L  128 ? 1.5161 0.3340 1.2668 0.1957  -0.3082 0.0094  128 VAL   L CG1 
20549 C  CG2 . VAL   L  128 ? 1.5327 0.4066 1.3242 0.2367  -0.3021 0.0560  128 VAL   L CG2 
20550 N  N   . GLY   L  129 ? 1.5613 0.5330 1.2951 0.1808  -0.2539 0.0669  129 GLY   L N   
20551 C  CA  . GLY   L  129 ? 1.6013 0.5449 1.2075 0.1659  -0.2831 0.1013  129 GLY   L CA  
20552 C  C   . GLY   L  129 ? 1.6515 0.5520 1.1960 0.1731  -0.2908 0.0973  129 GLY   L C   
20553 O  O   . GLY   L  129 ? 1.7152 0.6029 1.0894 0.1553  -0.3234 0.1286  129 GLY   L O   
20554 N  N   . SER   L  130 ? 1.6057 0.5728 1.1355 0.1941  -0.3418 0.0877  130 SER   L N   
20555 C  CA  . SER   L  130 ? 1.5924 0.6205 1.1781 0.1602  -0.3550 0.0533  130 SER   L CA  
20556 C  C   . SER   L  130 ? 1.5917 0.5009 1.2125 0.1421  -0.3542 0.0525  130 SER   L C   
20557 O  O   . SER   L  130 ? 1.6024 0.5669 1.2457 0.1049  -0.3359 0.0823  130 SER   L O   
20558 C  CB  . SER   L  130 ? 1.5512 0.7220 1.1640 0.2249  -0.3667 0.0299  130 SER   L CB  
20559 O  OG  . SER   L  130 ? 1.5800 0.8976 1.1823 0.2468  -0.3815 -0.0327 130 SER   L OG  
20560 N  N   . TYR   L  131 ? 1.5755 0.3996 1.2711 0.1276  -0.3522 0.0341  131 TYR   L N   
20561 C  CA  . TYR   L  131 ? 1.5671 0.4680 1.3125 0.1078  -0.3760 0.0840  131 TYR   L CA  
20562 C  C   . TYR   L  131 ? 1.6021 0.4125 1.3220 0.1259  -0.3978 0.1211  131 TYR   L C   
20563 O  O   . TYR   L  131 ? 1.5758 0.3149 1.3266 0.1414  -0.4323 0.1755  131 TYR   L O   
20564 C  CB  . TYR   L  131 ? 1.5403 0.5585 1.3184 0.1083  -0.3382 0.0485  131 TYR   L CB  
20565 C  CG  . TYR   L  131 ? 1.5253 0.6155 1.3678 0.0970  -0.3656 0.1094  131 TYR   L CG  
20566 C  CD1 . TYR   L  131 ? 1.5094 0.6693 1.4051 0.0824  -0.3410 0.1014  131 TYR   L CD1 
20567 C  CD2 . TYR   L  131 ? 1.5377 0.6747 1.4059 0.0878  -0.4059 0.0949  131 TYR   L CD2 
20568 C  CE1 . TYR   L  131 ? 1.5295 0.6903 1.4639 0.0967  -0.3479 0.1340  131 TYR   L CE1 
20569 C  CE2 . TYR   L  131 ? 1.5947 0.6680 1.4848 0.0845  -0.3842 0.1111  131 TYR   L CE2 
20570 C  CZ  . TYR   L  131 ? 1.5345 0.7908 1.5132 0.0732  -0.3788 0.1260  131 TYR   L CZ  
20571 O  OH  . TYR   L  131 ? 1.7156 0.8481 1.5605 -0.0059 -0.3277 0.2068  131 TYR   L OH  
20572 N  N   . GLU   L  132 ? 1.6150 0.5191 1.3723 0.1024  -0.4100 0.1599  132 GLU   L N   
20573 C  CA  . GLU   L  132 ? 1.6769 0.7144 1.3819 0.0656  -0.4457 0.1690  132 GLU   L CA  
20574 C  C   . GLU   L  132 ? 1.6493 0.7413 1.3744 0.0553  -0.4676 0.1683  132 GLU   L C   
20575 O  O   . GLU   L  132 ? 1.6350 0.8712 1.3803 0.0357  -0.3884 0.1709  132 GLU   L O   
20576 C  CB  . GLU   L  132 ? 1.7535 0.7532 1.3848 0.0577  -0.4753 0.0986  132 GLU   L CB  
20577 C  CG  . GLU   L  132 ? 1.8466 0.9699 1.3499 0.0467  -0.5005 0.0902  132 GLU   L CG  
20578 C  CD  . GLU   L  132 ? 1.9160 1.0402 1.4060 0.0606  -0.4819 -0.0386 132 GLU   L CD  
20579 O  OE1 . GLU   L  132 ? 1.8349 1.2395 1.3685 0.0900  -0.5824 -0.0424 132 GLU   L OE1 
20580 O  OE2 . GLU   L  132 ? 1.9763 1.3455 1.2922 0.0702  -0.4877 0.0715  132 GLU   L OE2 
20581 N  N   . ARG   L  133 ? 1.5929 0.7978 1.3801 0.0345  -0.5032 0.0925  133 ARG   L N   
20582 C  CA  . ARG   L  133 ? 1.6058 0.9017 1.3846 0.0490  -0.4883 0.0805  133 ARG   L CA  
20583 C  C   . ARG   L  133 ? 1.6759 0.9022 1.3606 0.0558  -0.5003 0.0812  133 ARG   L C   
20584 O  O   . ARG   L  133 ? 1.7443 0.8868 1.3358 0.0690  -0.5094 0.1064  133 ARG   L O   
20585 C  CB  . ARG   L  133 ? 1.6292 0.8391 1.3842 0.0064  -0.5371 0.0435  133 ARG   L CB  
20586 C  CG  . ARG   L  133 ? 1.6101 0.8985 1.4279 -0.0196 -0.5593 0.0213  133 ARG   L CG  
20587 C  CD  . ARG   L  133 ? 1.6190 0.9129 1.4612 -0.0289 -0.5846 0.0408  133 ARG   L CD  
20588 N  NE  . ARG   L  133 ? 1.6040 0.9384 1.5245 -0.0101 -0.6019 0.0355  133 ARG   L NE  
20589 C  CZ  . ARG   L  133 ? 1.6484 0.9540 1.5244 -0.0036 -0.6192 0.0768  133 ARG   L CZ  
20590 N  NH1 . ARG   L  133 ? 1.6683 0.9696 1.5128 0.0056  -0.6454 0.0978  133 ARG   L NH1 
20591 N  NH2 . ARG   L  133 ? 1.6430 0.9966 1.5695 0.0158  -0.6113 0.0470  133 ARG   L NH2 
20592 N  N   . GLU   L  134 ? 1.7203 1.0384 1.4041 0.1108  -0.4156 0.1386  134 GLU   L N   
20593 C  CA  . GLU   L  134 ? 1.7065 1.0810 1.5205 0.1104  -0.4264 0.1083  134 GLU   L CA  
20594 C  C   . GLU   L  134 ? 1.6636 1.1434 1.5659 0.1067  -0.4642 0.1094  134 GLU   L C   
20595 O  O   . GLU   L  134 ? 1.6983 1.3026 1.5090 0.0629  -0.4988 0.0339  134 GLU   L O   
20596 C  CB  . GLU   L  134 ? 1.7672 1.2022 1.5960 0.1818  -0.4156 0.1825  134 GLU   L CB  
20597 C  CG  . GLU   L  134 ? 1.7683 1.3771 1.6132 0.1459  -0.3995 0.2047  134 GLU   L CG  
20598 C  CD  . GLU   L  134 ? 1.7749 1.5044 1.4073 0.0750  -0.5316 0.1490  134 GLU   L CD  
20599 O  OE1 . GLU   L  134 ? 1.9186 1.5632 1.6271 0.3029  -0.4827 0.1549  134 GLU   L OE1 
20600 O  OE2 . GLU   L  134 ? 1.6706 1.5364 1.3054 -0.0070 -0.5077 0.2673  134 GLU   L OE2 
20601 N  N   . GLN   L  135 ? 1.6167 1.0884 1.6437 0.1036  -0.4812 0.1820  135 GLN   L N   
20602 C  CA  . GLN   L  135 ? 1.6382 1.0852 1.7435 0.0709  -0.4767 0.2511  135 GLN   L CA  
20603 C  C   . GLN   L  135 ? 1.5762 0.9664 1.7428 0.0497  -0.4687 0.2168  135 GLN   L C   
20604 O  O   . GLN   L  135 ? 1.5331 1.0056 1.7657 0.0055  -0.4782 0.2095  135 GLN   L O   
20605 C  CB  . GLN   L  135 ? 1.6632 1.1656 1.7732 0.0478  -0.4970 0.2445  135 GLN   L CB  
20606 C  CG  . GLN   L  135 ? 1.7313 1.3186 1.7770 0.0102  -0.5378 0.2984  135 GLN   L CG  
20607 C  CD  . GLN   L  135 ? 1.7666 1.2942 1.8822 0.0112  -0.5145 0.3162  135 GLN   L CD  
20608 O  OE1 . GLN   L  135 ? 1.8216 1.3347 1.8327 0.0765  -0.6231 0.3927  135 GLN   L OE1 
20609 N  NE2 . GLN   L  135 ? 1.8295 1.4393 1.9170 -0.0664 -0.4801 0.3070  135 GLN   L NE2 
20610 N  N   . CYS   L  136 ? 1.5779 0.8985 1.6974 0.0282  -0.4868 0.2157  136 CYS   L N   
20611 C  CA  . CYS   L  136 ? 1.6276 0.8709 1.7023 -0.0238 -0.4491 0.2213  136 CYS   L CA  
20612 C  C   . CYS   L  136 ? 1.6392 0.6507 1.5521 0.0169  -0.4304 0.2185  136 CYS   L C   
20613 O  O   . CYS   L  136 ? 1.6556 0.5523 1.5505 0.0068  -0.4193 0.2953  136 CYS   L O   
20614 C  CB  . CYS   L  136 ? 1.6894 0.8542 1.7764 -0.0368 -0.4759 0.2243  136 CYS   L CB  
20615 S  SG  . CYS   L  136 ? 1.7380 0.9771 1.9277 -0.0835 -0.4070 0.2607  136 CYS   L SG  
20616 N  N   . ARG   L  137 ? 1.6294 0.5119 1.5217 0.0798  -0.3855 0.1758  137 ARG   L N   
20617 C  CA  . ARG   L  137 ? 1.6110 0.4688 1.4302 0.0799  -0.3615 0.1050  137 ARG   L CA  
20618 C  C   . ARG   L  137 ? 1.6164 0.5461 1.3893 0.0635  -0.3470 0.0636  137 ARG   L C   
20619 O  O   . ARG   L  137 ? 1.5852 0.6719 1.3767 0.0711  -0.3110 0.0806  137 ARG   L O   
20620 C  CB  . ARG   L  137 ? 1.5993 0.4549 1.3962 0.0910  -0.3706 0.0995  137 ARG   L CB  
20621 C  CG  . ARG   L  137 ? 1.5958 0.5027 1.3596 0.0936  -0.3622 0.0812  137 ARG   L CG  
20622 C  CD  . ARG   L  137 ? 1.6120 0.5690 1.3426 0.0669  -0.3449 0.0255  137 ARG   L CD  
20623 N  NE  . ARG   L  137 ? 1.6701 0.6666 1.3813 0.0616  -0.3064 0.0685  137 ARG   L NE  
20624 C  CZ  . ARG   L  137 ? 1.6863 0.8206 1.4029 0.1054  -0.2014 0.0895  137 ARG   L CZ  
20625 N  NH1 . ARG   L  137 ? 1.6385 0.8339 1.4590 0.1019  -0.2110 0.1393  137 ARG   L NH1 
20626 N  NH2 . ARG   L  137 ? 1.7368 0.9504 1.4604 0.1083  -0.1678 0.1607  137 ARG   L NH2 
20627 N  N   . ALA   L  138 ? 1.6148 0.5282 1.3891 0.0464  -0.3609 0.0462  138 ALA   L N   
20628 C  CA  . ALA   L  138 ? 1.5706 0.5277 1.3823 0.0014  -0.3521 0.0439  138 ALA   L CA  
20629 C  C   . ALA   L  138 ? 1.5591 0.3962 1.3732 -0.0318 -0.3109 0.0179  138 ALA   L C   
20630 O  O   . ALA   L  138 ? 1.4829 0.2835 1.3937 -0.0717 -0.3234 0.0210  138 ALA   L O   
20631 C  CB  . ALA   L  138 ? 1.6199 0.5413 1.4185 -0.0301 -0.3540 0.0255  138 ALA   L CB  
20632 N  N   . GLY   L  139 ? 1.5103 0.3637 1.3816 -0.0362 -0.3113 0.0088  139 GLY   L N   
20633 C  CA  . GLY   L  139 ? 1.4848 0.4173 1.3906 -0.0042 -0.2879 0.0248  139 GLY   L CA  
20634 C  C   . GLY   L  139 ? 1.4753 0.3967 1.4157 0.0564  -0.2905 0.0270  139 GLY   L C   
20635 O  O   . GLY   L  139 ? 1.4619 0.3687 1.4827 0.0587  -0.2726 0.0215  139 GLY   L O   
20636 N  N   . GLY   L  140 ? 1.4952 0.4479 1.4063 0.1087  -0.2979 0.0299  140 GLY   L N   
20637 C  CA  . GLY   L  140 ? 1.4733 0.5915 1.3941 0.1004  -0.2948 0.0480  140 GLY   L CA  
20638 C  C   . GLY   L  140 ? 1.5031 0.5777 1.3705 0.0464  -0.2774 0.0536  140 GLY   L C   
20639 O  O   . GLY   L  140 ? 1.4638 0.6214 1.3230 -0.0035 -0.3000 0.0790  140 GLY   L O   
20640 N  N   . ALA   L  141 ? 1.5474 0.5941 1.4387 0.0556  -0.2532 0.1122  141 ALA   L N   
20641 C  CA  . ALA   L  141 ? 1.5148 0.6164 1.4859 0.1070  -0.2549 0.0556  141 ALA   L CA  
20642 C  C   . ALA   L  141 ? 1.4564 0.6063 1.4985 0.1011  -0.2392 0.0529  141 ALA   L C   
20643 O  O   . ALA   L  141 ? 1.3997 0.6059 1.4653 0.0316  -0.2693 -0.0171 141 ALA   L O   
20644 C  CB  . ALA   L  141 ? 1.5563 0.6231 1.5073 0.1483  -0.2376 0.0881  141 ALA   L CB  
20645 N  N   . ALA   L  142 ? 1.4387 0.6082 1.5292 0.0090  -0.2615 0.0851  142 ALA   L N   
20646 C  CA  . ALA   L  142 ? 1.4900 0.5889 1.5350 0.0080  -0.2447 0.0585  142 ALA   L CA  
20647 C  C   . ALA   L  142 ? 1.5125 0.4897 1.5302 -0.0167 -0.2322 0.0478  142 ALA   L C   
20648 O  O   . ALA   L  142 ? 1.6032 0.2806 1.5716 -0.0333 -0.1987 -0.0851 142 ALA   L O   
20649 C  CB  . ALA   L  142 ? 1.5126 0.6905 1.5489 0.0222  -0.2274 0.0952  142 ALA   L CB  
20650 N  N   . ALA   L  143 ? 1.5432 0.5463 1.5364 -0.0073 -0.1890 0.1022  143 ALA   L N   
20651 C  CA  . ALA   L  143 ? 1.5514 0.5843 1.5045 0.0365  -0.2061 0.0628  143 ALA   L CA  
20652 C  C   . ALA   L  143 ? 1.5044 0.5109 1.4849 0.0843  -0.2741 0.0955  143 ALA   L C   
20653 O  O   . ALA   L  143 ? 1.4730 0.3025 1.4876 0.1434  -0.2756 0.0797  143 ALA   L O   
20654 C  CB  . ALA   L  143 ? 1.5389 0.6728 1.5229 0.0086  -0.1741 0.0939  143 ALA   L CB  
20655 N  N   . SER   L  144 ? 1.5498 0.4915 1.4951 0.0941  -0.2671 0.1177  144 SER   L N   
20656 C  CA  . SER   L  144 ? 1.5792 0.5686 1.4181 0.0549  -0.3166 0.1091  144 SER   L CA  
20657 C  C   . SER   L  144 ? 1.6024 0.5170 1.3222 0.0583  -0.4045 0.0598  144 SER   L C   
20658 O  O   . SER   L  144 ? 1.6181 0.3848 1.3067 0.0829  -0.4233 0.0982  144 SER   L O   
20659 C  CB  . SER   L  144 ? 1.5863 0.6397 1.4559 0.0818  -0.2758 0.1456  144 SER   L CB  
20660 O  OG  . SER   L  144 ? 1.6195 0.6947 1.4836 0.0433  -0.2354 0.1845  144 SER   L OG  
20661 N  N   . LEU   L  145 ? 1.6082 0.6020 1.3371 0.0657  -0.3997 0.0701  145 LEU   L N   
20662 C  CA  . LEU   L  145 ? 1.6171 0.5536 1.3794 0.0624  -0.4776 0.0402  145 LEU   L CA  
20663 C  C   . LEU   L  145 ? 1.6123 0.5599 1.3510 0.0377  -0.5393 0.0100  145 LEU   L C   
20664 O  O   . LEU   L  145 ? 1.6247 0.4150 1.3756 0.0693  -0.5828 0.0641  145 LEU   L O   
20665 C  CB  . LEU   L  145 ? 1.6666 0.5766 1.4222 0.0296  -0.4238 0.0896  145 LEU   L CB  
20666 C  CG  . LEU   L  145 ? 1.6830 0.5457 1.4603 0.0345  -0.3864 0.1010  145 LEU   L CG  
20667 C  CD1 . LEU   L  145 ? 1.6406 0.5805 1.4880 0.0561  -0.3696 0.1411  145 LEU   L CD1 
20668 C  CD2 . LEU   L  145 ? 1.7095 0.5108 1.5093 0.0169  -0.3611 0.1070  145 LEU   L CD2 
20669 N  N   . ILE   L  146 ? 1.5549 0.5675 1.3851 0.1299  -0.5120 0.0470  146 ILE   L N   
20670 C  CA  . ILE   L  146 ? 1.4980 0.5752 1.4677 0.0918  -0.4807 0.0600  146 ILE   L CA  
20671 C  C   . ILE   L  146 ? 1.4527 0.5058 1.4909 0.0465  -0.4815 0.0675  146 ILE   L C   
20672 O  O   . ILE   L  146 ? 1.4402 0.4091 1.5598 -0.0204 -0.4929 0.0635  146 ILE   L O   
20673 C  CB  . ILE   L  146 ? 1.5063 0.5793 1.4222 0.1150  -0.4449 0.0868  146 ILE   L CB  
20674 C  CG1 . ILE   L  146 ? 1.5016 0.6472 1.4193 0.1235  -0.4272 0.0895  146 ILE   L CG1 
20675 C  CG2 . ILE   L  146 ? 1.4979 0.5716 1.4324 0.1159  -0.4300 0.0777  146 ILE   L CG2 
20676 C  CD1 . ILE   L  146 ? 1.5095 0.6201 1.4352 0.1183  -0.4063 0.0953  146 ILE   L CD1 
20677 N  N   . MET   L  147 ? 1.4757 0.5167 1.5849 0.0658  -0.4130 0.0549  147 MET   L N   
20678 C  CA  . MET   L  147 ? 1.4706 0.5961 1.5949 0.1107  -0.4288 0.0852  147 MET   L CA  
20679 C  C   . MET   L  147 ? 1.4440 0.5528 1.6286 0.1517  -0.4526 0.0817  147 MET   L C   
20680 O  O   . MET   L  147 ? 1.3990 0.6029 1.6585 0.1840  -0.4391 0.0759  147 MET   L O   
20681 C  CB  . MET   L  147 ? 1.4792 0.6331 1.6112 0.0974  -0.4072 0.0664  147 MET   L CB  
20682 C  CG  . MET   L  147 ? 1.4521 0.6006 1.6259 0.1428  -0.3996 0.0588  147 MET   L CG  
20683 S  SD  . MET   L  147 ? 1.5153 0.5020 1.6860 0.0875  -0.3677 0.0338  147 MET   L SD  
20684 C  CE  . MET   L  147 ? 1.5562 0.6679 1.6151 0.0850  -0.3837 -0.0048 147 MET   L CE  
20685 N  N   . PRO   L  148 ? 1.4981 0.5475 1.7058 0.1393  -0.4289 0.0645  148 PRO   L N   
20686 C  CA  . PRO   L  148 ? 1.4979 0.5590 1.6794 0.1554  -0.4582 0.0748  148 PRO   L CA  
20687 C  C   . PRO   L  148 ? 1.4962 0.4791 1.6457 0.1762  -0.4595 0.0560  148 PRO   L C   
20688 O  O   . PRO   L  148 ? 1.5348 0.3435 1.6236 0.2214  -0.4583 0.0644  148 PRO   L O   
20689 C  CB  . PRO   L  148 ? 1.5174 0.5284 1.7273 0.1430  -0.4578 0.0143  148 PRO   L CB  
20690 C  CG  . PRO   L  148 ? 1.5292 0.5839 1.7394 0.1384  -0.4395 0.0530  148 PRO   L CG  
20691 C  CD  . PRO   L  148 ? 1.5127 0.5719 1.7418 0.1387  -0.4324 0.0841  148 PRO   L CD  
20692 N  N   . PHE   L  149 ? 1.5137 0.5268 1.6712 0.1635  -0.4299 0.0525  149 PHE   L N   
20693 C  CA  . PHE   L  149 ? 1.5190 0.5786 1.7262 0.1171  -0.4305 0.0252  149 PHE   L CA  
20694 C  C   . PHE   L  149 ? 1.4918 0.6608 1.6356 0.1107  -0.4871 0.0825  149 PHE   L C   
20695 O  O   . PHE   L  149 ? 1.5120 0.7454 1.6149 0.0725  -0.5022 0.0602  149 PHE   L O   
20696 C  CB  . PHE   L  149 ? 1.4708 0.5796 1.7566 0.1203  -0.3716 0.0065  149 PHE   L CB  
20697 C  CG  . PHE   L  149 ? 1.4474 0.6021 1.8537 0.1131  -0.3927 0.0057  149 PHE   L CG  
20698 C  CD1 . PHE   L  149 ? 1.4108 0.5753 1.8434 0.1587  -0.4043 -0.0204 149 PHE   L CD1 
20699 C  CD2 . PHE   L  149 ? 1.4073 0.6730 1.8882 0.1402  -0.3258 0.0109  149 PHE   L CD2 
20700 C  CE1 . PHE   L  149 ? 1.3959 0.5976 1.8556 0.1264  -0.4224 0.0040  149 PHE   L CE1 
20701 C  CE2 . PHE   L  149 ? 1.3833 0.6982 1.9217 0.1174  -0.3585 0.0076  149 PHE   L CE2 
20702 C  CZ  . PHE   L  149 ? 1.3871 0.6435 1.8918 0.1504  -0.3760 0.0023  149 PHE   L CZ  
20703 N  N   . LEU   L  150 ? 1.6121 0.6712 1.6456 0.0380  -0.4353 0.1167  150 LEU   L N   
20704 C  CA  . LEU   L  150 ? 1.6200 0.6585 1.6334 0.0281  -0.4362 0.1151  150 LEU   L CA  
20705 C  C   . LEU   L  150 ? 1.5789 0.6399 1.6267 0.0564  -0.4604 0.0713  150 LEU   L C   
20706 O  O   . LEU   L  150 ? 1.5705 0.5909 1.7057 -0.0139 -0.5360 0.0283  150 LEU   L O   
20707 C  CB  . LEU   L  150 ? 1.6860 0.5958 1.5737 0.0416  -0.3854 0.0923  150 LEU   L CB  
20708 C  CG  . LEU   L  150 ? 1.7276 0.5685 1.5847 0.0163  -0.3367 0.1055  150 LEU   L CG  
20709 C  CD1 . LEU   L  150 ? 1.7386 0.5339 1.5978 0.0033  -0.3244 0.0754  150 LEU   L CD1 
20710 C  CD2 . LEU   L  150 ? 1.7213 0.6756 1.5938 0.0158  -0.3387 0.1093  150 LEU   L CD2 
20711 N  N   . ASP   L  151 ? 1.6109 0.7199 1.5737 0.0889  -0.4575 0.0340  151 ASP   L N   
20712 C  CA  . ASP   L  151 ? 1.6299 0.8204 1.5774 0.1720  -0.3938 0.0428  151 ASP   L CA  
20713 C  C   . ASP   L  151 ? 1.6491 0.8275 1.5283 0.1963  -0.4080 0.0371  151 ASP   L C   
20714 O  O   . ASP   L  151 ? 1.7899 0.8068 1.4932 0.2492  -0.3586 0.0611  151 ASP   L O   
20715 C  CB  . ASP   L  151 ? 1.6527 0.9285 1.5920 0.1675  -0.3260 0.0174  151 ASP   L CB  
20716 C  CG  . ASP   L  151 ? 1.6277 0.9874 1.6271 0.1462  -0.2389 0.0270  151 ASP   L CG  
20717 O  OD1 . ASP   L  151 ? 1.6907 1.0093 1.6368 0.2221  -0.1533 0.1354  151 ASP   L OD1 
20718 O  OD2 . ASP   L  151 ? 1.6330 1.1580 1.6888 0.2522  -0.1760 0.0285  151 ASP   L OD2 
20719 N  N   . ASN   L  152 ? 1.6287 0.8637 1.5224 0.1711  -0.3799 0.0332  152 ASN   L N   
20720 C  CA  . ASN   L  152 ? 1.6106 0.9204 1.5025 0.1741  -0.4023 0.0179  152 ASN   L CA  
20721 C  C   . ASN   L  152 ? 1.5851 0.9075 1.5616 0.1914  -0.4752 0.0552  152 ASN   L C   
20722 O  O   . ASN   L  152 ? 1.5983 0.8776 1.5179 0.2050  -0.4537 -0.0105 152 ASN   L O   
20723 C  CB  . ASN   L  152 ? 1.6096 0.9378 1.5130 0.1323  -0.3727 0.0468  152 ASN   L CB  
20724 C  CG  . ASN   L  152 ? 1.5693 1.0485 1.4835 0.1173  -0.3964 0.0312  152 ASN   L CG  
20725 O  OD1 . ASN   L  152 ? 1.5044 1.0159 1.5570 0.0633  -0.3912 -0.0300 152 ASN   L OD1 
20726 N  ND2 . ASN   L  152 ? 1.5307 1.0561 1.4871 0.1182  -0.4478 0.0417  152 ASN   L ND2 
20727 N  N   . GLN   L  153 ? 1.6025 0.9489 1.5985 0.2262  -0.4548 0.0404  153 GLN   L N   
20728 C  CA  . GLN   L  153 ? 1.5505 1.0003 1.7825 0.2432  -0.4967 0.0821  153 GLN   L CA  
20729 C  C   . GLN   L  153 ? 1.5043 1.0265 1.8270 0.2935  -0.4998 0.1113  153 GLN   L C   
20730 O  O   . GLN   L  153 ? 1.5152 1.0527 1.8735 0.3194  -0.5586 0.0683  153 GLN   L O   
20731 C  CB  . GLN   L  153 ? 1.5550 1.0171 1.8188 0.2186  -0.4724 0.1160  153 GLN   L CB  
20732 C  CG  . GLN   L  153 ? 1.5244 1.0163 1.8739 0.2234  -0.5136 0.1120  153 GLN   L CG  
20733 C  CD  . GLN   L  153 ? 1.4638 1.1316 1.8713 0.2851  -0.5898 0.1545  153 GLN   L CD  
20734 O  OE1 . GLN   L  153 ? 1.4156 1.1939 1.7687 0.2760  -0.7360 0.2523  153 GLN   L OE1 
20735 N  NE2 . GLN   L  153 ? 1.4807 1.1654 1.8417 0.2794  -0.6443 0.1227  153 GLN   L NE2 
20736 N  N   . VAL   L  154 ? 1.5038 1.0007 1.8780 0.3037  -0.4624 0.1291  154 VAL   L N   
20737 C  CA  . VAL   L  154 ? 1.4867 1.0031 1.8786 0.2767  -0.4415 0.1689  154 VAL   L CA  
20738 C  C   . VAL   L  154 ? 1.4509 0.9489 1.8820 0.3219  -0.4437 0.1871  154 VAL   L C   
20739 O  O   . VAL   L  154 ? 1.4620 0.9818 1.8772 0.2502  -0.5290 0.1988  154 VAL   L O   
20740 C  CB  . VAL   L  154 ? 1.4981 1.0287 1.8943 0.2529  -0.4210 0.1533  154 VAL   L CB  
20741 C  CG1 . VAL   L  154 ? 1.5657 1.0511 1.8995 0.3042  -0.4161 0.1846  154 VAL   L CG1 
20742 C  CG2 . VAL   L  154 ? 1.4804 1.0807 1.9069 0.2011  -0.3401 0.1243  154 VAL   L CG2 
20743 N  N   . ASN   L  155 ? 1.5005 0.9569 1.8760 0.3624  -0.4251 0.1702  155 ASN   L N   
20744 C  CA  . ASN   L  155 ? 1.5372 1.0654 1.8636 0.3690  -0.4362 0.1662  155 ASN   L CA  
20745 C  C   . ASN   L  155 ? 1.5266 1.1314 1.7387 0.3497  -0.5109 0.2164  155 ASN   L C   
20746 O  O   . ASN   L  155 ? 1.5323 1.1501 1.6952 0.3856  -0.6024 0.2510  155 ASN   L O   
20747 C  CB  . ASN   L  155 ? 1.5627 1.1026 1.9634 0.3461  -0.3588 0.1665  155 ASN   L CB  
20748 C  CG  . ASN   L  155 ? 1.5772 1.1201 2.0409 0.3274  -0.2909 0.1379  155 ASN   L CG  
20749 O  OD1 . ASN   L  155 ? 1.4748 1.3487 2.0825 0.4385  -0.3027 0.3157  155 ASN   L OD1 
20750 N  ND2 . ASN   L  155 ? 1.5417 1.1142 2.0847 0.2833  -0.2564 0.1426  155 ASN   L ND2 
20751 N  N   . PHE   L  156 ? 1.5492 1.1854 1.7146 0.2999  -0.5178 0.2209  156 PHE   L N   
20752 C  CA  . PHE   L  156 ? 1.6470 1.2196 1.6681 0.2962  -0.4878 0.1931  156 PHE   L CA  
20753 C  C   . PHE   L  156 ? 1.7235 1.1414 1.5955 0.2805  -0.4937 0.1629  156 PHE   L C   
20754 O  O   . PHE   L  156 ? 1.6758 1.0467 1.6044 0.2778  -0.4798 0.1278  156 PHE   L O   
20755 C  CB  . PHE   L  156 ? 1.7212 1.3436 1.6587 0.3094  -0.5361 0.2271  156 PHE   L CB  
20756 C  CG  . PHE   L  156 ? 1.7954 1.4541 1.7010 0.2993  -0.4532 0.2292  156 PHE   L CG  
20757 C  CD1 . PHE   L  156 ? 1.8446 1.4339 1.7721 0.3026  -0.4596 0.3006  156 PHE   L CD1 
20758 C  CD2 . PHE   L  156 ? 1.8923 1.4777 1.7142 0.2783  -0.4939 0.2998  156 PHE   L CD2 
20759 C  CE1 . PHE   L  156 ? 1.8681 1.5368 1.7988 0.2600  -0.3912 0.3030  156 PHE   L CE1 
20760 C  CE2 . PHE   L  156 ? 1.8638 1.5657 1.7627 0.2398  -0.4554 0.3008  156 PHE   L CE2 
20761 C  CZ  . PHE   L  156 ? 1.8613 1.5656 1.8121 0.2515  -0.4230 0.3302  156 PHE   L CZ  
20762 N  N   . LYS   L  157 ? 1.6898 1.0998 1.7195 0.2622  -0.4676 0.1216  157 LYS   L N   
20763 C  CA  . LYS   L  157 ? 1.7978 1.2066 1.7574 0.2041  -0.3655 0.0442  157 LYS   L CA  
20764 C  C   . LYS   L  157 ? 1.8225 1.2369 1.7366 0.1720  -0.4118 0.0075  157 LYS   L C   
20765 O  O   . LYS   L  157 ? 1.8306 1.3902 1.8607 0.0861  -0.3143 0.0184  157 LYS   L O   
20766 C  CB  . LYS   L  157 ? 1.7766 1.2060 1.8839 0.0843  -0.3013 -0.0390 157 LYS   L CB  
20767 C  CG  . LYS   L  157 ? 1.7945 1.2149 1.9520 0.0668  -0.2214 -0.0609 157 LYS   L CG  
20768 C  CD  . LYS   L  157 ? 1.8185 1.3514 1.9209 0.0478  -0.2052 -0.0868 157 LYS   L CD  
20769 C  CE  . LYS   L  157 ? 1.8875 1.3686 1.9981 0.0168  -0.1456 -0.0628 157 LYS   L CE  
20770 N  NZ  . LYS   L  157 ? 1.8973 1.4822 2.0571 -0.0153 -0.1379 -0.0903 157 LYS   L NZ  
20771 N  N   . ASN   L  158 ? 1.7689 1.0748 1.6755 0.1719  -0.5049 0.0526  158 ASN   L N   
20772 C  CA  . ASN   L  158 ? 1.7420 1.0201 1.6369 0.1734  -0.5422 0.1256  158 ASN   L CA  
20773 C  C   . ASN   L  158 ? 1.7135 1.0011 1.6384 0.2345  -0.5589 0.1796  158 ASN   L C   
20774 O  O   . ASN   L  158 ? 1.7262 0.9666 1.6021 0.2529  -0.5917 0.2658  158 ASN   L O   
20775 C  CB  . ASN   L  158 ? 1.7063 0.8428 1.6612 0.1167  -0.5302 0.1013  158 ASN   L CB  
20776 C  CG  . ASN   L  158 ? 1.7072 0.7712 1.6355 0.1537  -0.5043 0.1108  158 ASN   L CG  
20777 O  OD1 . ASN   L  158 ? 1.6741 0.9344 1.6337 0.1868  -0.5516 0.1770  158 ASN   L OD1 
20778 N  ND2 . ASN   L  158 ? 1.7283 0.6050 1.6058 0.1424  -0.5617 0.0679  158 ASN   L ND2 
20779 N  N   . GLN   L  159 ? 1.7684 1.0675 1.6436 0.2954  -0.5530 0.1850  159 GLN   L N   
20780 C  CA  . GLN   L  159 ? 1.7789 1.1052 1.6828 0.2895  -0.5729 0.1629  159 GLN   L CA  
20781 C  C   . GLN   L  159 ? 1.7947 1.1493 1.6797 0.2681  -0.6197 0.1105  159 GLN   L C   
20782 O  O   . GLN   L  159 ? 1.8501 1.2106 1.6878 0.2674  -0.6194 0.2210  159 GLN   L O   
20783 C  CB  . GLN   L  159 ? 1.8095 1.1867 1.7069 0.3230  -0.5323 0.1739  159 GLN   L CB  
20784 C  CG  . GLN   L  159 ? 1.8215 1.1231 1.7206 0.3290  -0.5077 0.1887  159 GLN   L CG  
20785 C  CD  . GLN   L  159 ? 1.7675 1.1261 1.8027 0.2969  -0.4803 0.2173  159 GLN   L CD  
20786 O  OE1 . GLN   L  159 ? 1.9061 1.2937 1.7789 0.3257  -0.4310 0.1609  159 GLN   L OE1 
20787 N  NE2 . GLN   L  159 ? 1.8023 0.9422 1.7916 0.2720  -0.4748 0.1789  159 GLN   L NE2 
20788 N  N   . TYR   L  160 ? 1.7853 1.0855 1.7105 0.2903  -0.6391 0.1244  160 TYR   L N   
20789 C  CA  . TYR   L  160 ? 1.7882 1.0793 1.7104 0.2935  -0.6638 0.0806  160 TYR   L CA  
20790 C  C   . TYR   L  160 ? 1.7951 1.1345 1.7568 0.2464  -0.6981 0.0341  160 TYR   L C   
20791 O  O   . TYR   L  160 ? 1.6291 0.9494 1.6834 0.2918  -0.8254 -0.0123 160 TYR   L O   
20792 C  CB  . TYR   L  160 ? 1.8132 1.0846 1.6437 0.2788  -0.7018 0.0638  160 TYR   L CB  
20793 C  CG  . TYR   L  160 ? 1.8417 1.1090 1.5897 0.2692  -0.6632 0.0590  160 TYR   L CG  
20794 C  CD1 . TYR   L  160 ? 1.8197 1.1413 1.6004 0.2459  -0.6640 0.0654  160 TYR   L CD1 
20795 C  CD2 . TYR   L  160 ? 1.8455 1.1518 1.5472 0.3011  -0.6830 0.0699  160 TYR   L CD2 
20796 C  CE1 . TYR   L  160 ? 1.8555 1.1945 1.5703 0.2128  -0.6380 0.0989  160 TYR   L CE1 
20797 C  CE2 . TYR   L  160 ? 1.8682 1.2354 1.5500 0.2714  -0.6644 0.0817  160 TYR   L CE2 
20798 C  CZ  . TYR   L  160 ? 1.8813 1.2421 1.5428 0.2490  -0.6667 0.1258  160 TYR   L CZ  
20799 O  OH  . TYR   L  160 ? 1.9366 1.2952 1.5264 0.2010  -0.6313 0.2279  160 TYR   L OH  
20800 N  N   . GLU   L  161 ? 1.8681 1.3115 1.7493 0.2602  -0.7225 0.0723  161 GLU   L N   
20801 C  CA  . GLU   L  161 ? 1.8736 1.4938 1.8891 0.2496  -0.6552 0.0470  161 GLU   L CA  
20802 C  C   . GLU   L  161 ? 1.9123 1.5022 1.8860 0.2553  -0.6559 0.0368  161 GLU   L C   
20803 O  O   . GLU   L  161 ? 2.0226 1.5324 1.8852 0.2790  -0.6562 0.0067  161 GLU   L O   
20804 C  CB  . GLU   L  161 ? 1.9782 1.5849 1.8981 0.2842  -0.6333 0.0994  161 GLU   L CB  
20805 C  CG  . GLU   L  161 ? 1.9684 1.7349 1.9899 0.2851  -0.5903 0.1490  161 GLU   L CG  
20806 C  CD  . GLU   L  161 ? 2.0296 1.7822 1.9596 0.3124  -0.4638 0.1681  161 GLU   L CD  
20807 O  OE1 . GLU   L  161 ? 2.1747 1.8791 2.0027 0.2403  -0.3529 0.2989  161 GLU   L OE1 
20808 O  OE2 . GLU   L  161 ? 1.9627 1.9924 2.0519 0.3348  -0.4509 0.2493  161 GLU   L OE2 
20809 N  N   . PRO   L  162 ? 1.7989 1.5877 1.9269 0.2471  -0.6873 0.0666  162 PRO   L N   
20810 C  CA  . PRO   L  162 ? 1.6705 1.6236 1.9277 0.2476  -0.7516 0.0240  162 PRO   L CA  
20811 C  C   . PRO   L  162 ? 1.6135 1.6858 1.9855 0.3045  -0.8175 0.0188  162 PRO   L C   
20812 O  O   . PRO   L  162 ? 1.6339 1.7535 2.0272 0.3371  -0.7941 0.0836  162 PRO   L O   
20813 C  CB  . PRO   L  162 ? 1.6318 1.6315 1.9919 0.2319  -0.7436 0.0353  162 PRO   L CB  
20814 C  CG  . PRO   L  162 ? 1.6767 1.5796 1.9770 0.2101  -0.6556 0.0489  162 PRO   L CG  
20815 C  CD  . PRO   L  162 ? 1.7513 1.5820 1.9466 0.2182  -0.6599 0.0697  162 PRO   L CD  
20816 N  N   . GLY   L  163 ? 1.6347 1.7260 1.9540 0.2625  -0.8928 -0.0656 163 GLY   L N   
20817 C  CA  . GLY   L  163 ? 1.6411 1.7266 2.0596 0.2574  -1.0014 -0.1370 163 GLY   L CA  
20818 C  C   . GLY   L  163 ? 1.6843 1.8430 1.9024 0.2911  -1.0598 -0.1546 163 GLY   L C   
20819 O  O   . GLY   L  163 ? 1.6777 1.7382 2.0082 0.2579  -1.1325 -0.2521 163 GLY   L O   
20820 N  N   . THR   L  164 ? 1.7229 1.8806 2.0363 0.2540  -1.0037 -0.1278 164 THR   L N   
20821 C  CA  . THR   L  164 ? 1.8498 2.0054 2.0015 0.3553  -0.9326 -0.0671 164 THR   L CA  
20822 C  C   . THR   L  164 ? 1.9731 2.0104 2.0576 0.4064  -0.8439 -0.1233 164 THR   L C   
20823 O  O   . THR   L  164 ? 2.0385 2.0516 1.9666 0.5222  -0.8526 -0.0476 164 THR   L O   
20824 C  CB  . THR   L  164 ? 1.8862 2.0150 1.9716 0.3933  -0.9144 -0.0674 164 THR   L CB  
20825 O  OG1 . THR   L  164 ? 1.9974 2.0553 1.9162 0.2996  -0.9318 -0.1670 164 THR   L OG1 
20826 C  CG2 . THR   L  164 ? 1.8339 2.0545 1.9260 0.3959  -0.9562 -0.0197 164 THR   L CG2 
20827 N  N   . ASN   L  165 ? 1.9603 1.9344 2.1322 0.4377  -0.7478 -0.2085 165 ASN   L N   
20828 C  CA  . ASN   L  165 ? 1.9148 1.9925 2.1334 0.3878  -0.7378 -0.2533 165 ASN   L CA  
20829 C  C   . ASN   L  165 ? 1.9089 1.9692 2.0649 0.4080  -0.7719 -0.2035 165 ASN   L C   
20830 O  O   . ASN   L  165 ? 1.8290 2.0788 1.9043 0.3582  -0.8906 -0.2777 165 ASN   L O   
20831 C  CB  . ASN   L  165 ? 1.9777 2.1276 2.1339 0.3585  -0.7473 -0.2524 165 ASN   L CB  
20832 C  CG  . ASN   L  165 ? 2.0012 2.2058 2.1714 0.3562  -0.6687 -0.2567 165 ASN   L CG  
20833 O  OD1 . ASN   L  165 ? 2.1274 2.3892 2.1613 0.3469  -0.6617 -0.1952 165 ASN   L OD1 
20834 N  ND2 . ASN   L  165 ? 2.0188 2.1893 2.2803 0.3359  -0.6309 -0.2299 165 ASN   L ND2 
20835 N  N   . GLY   L  166 ? 1.8672 1.8301 2.0268 0.4312  -0.7128 -0.1141 166 GLY   L N   
20836 C  CA  . GLY   L  166 ? 1.9250 1.6773 2.0828 0.3481  -0.6235 -0.0554 166 GLY   L CA  
20837 C  C   . GLY   L  166 ? 2.0437 1.6782 2.1186 0.3794  -0.5706 -0.0284 166 GLY   L C   
20838 O  O   . GLY   L  166 ? 2.0695 1.6782 2.2533 0.3341  -0.5157 0.0228  166 GLY   L O   
20839 N  N   . LYS   L  167 ? 2.0617 1.6093 2.0219 0.3529  -0.5215 0.0076  167 LYS   L N   
20840 C  CA  . LYS   L  167 ? 2.1531 1.6450 1.9541 0.3418  -0.4649 -0.0129 167 LYS   L CA  
20841 C  C   . LYS   L  167 ? 2.2161 1.6159 1.8972 0.3673  -0.4144 0.0640  167 LYS   L C   
20842 O  O   . LYS   L  167 ? 2.3188 1.6323 1.8250 0.4004  -0.3310 0.1136  167 LYS   L O   
20843 C  CB  . LYS   L  167 ? 2.1168 1.6739 1.9530 0.3394  -0.4744 0.0137  167 LYS   L CB  
20844 C  CG  . LYS   L  167 ? 2.1657 1.6907 1.9444 0.3456  -0.4545 -0.0201 167 LYS   L CG  
20845 C  CD  . LYS   L  167 ? 2.2394 1.7198 1.9492 0.2974  -0.3899 -0.0978 167 LYS   L CD  
20846 C  CE  . LYS   L  167 ? 2.2085 1.7246 1.9404 0.2722  -0.3550 -0.1150 167 LYS   L CE  
20847 N  NZ  . LYS   L  167 ? 2.2921 1.7870 1.9514 0.2218  -0.3060 -0.1844 167 LYS   L NZ  
20848 N  N   . VAL   L  168 ? 2.1754 1.5436 1.8958 0.3427  -0.4411 0.0612  168 VAL   L N   
20849 C  CA  . VAL   L  168 ? 2.1414 1.5157 1.8348 0.3431  -0.4848 0.0896  168 VAL   L CA  
20850 C  C   . VAL   L  168 ? 2.0953 1.4510 1.8406 0.2946  -0.5148 0.0460  168 VAL   L C   
20851 O  O   . VAL   L  168 ? 2.0833 1.6575 1.7904 0.2440  -0.4821 0.1105  168 VAL   L O   
20852 C  CB  . VAL   L  168 ? 2.1482 1.5000 1.7862 0.3282  -0.5236 0.0769  168 VAL   L CB  
20853 C  CG1 . VAL   L  168 ? 2.1365 1.5297 1.8285 0.3512  -0.4556 0.1079  168 VAL   L CG1 
20854 C  CG2 . VAL   L  168 ? 2.1363 1.4945 1.7781 0.2984  -0.5670 -0.0024 168 VAL   L CG2 
20855 N  N   . LYS   L  169 ? 2.1211 1.3755 1.7549 0.3257  -0.5003 0.0252  169 LYS   L N   
20856 C  CA  . LYS   L  169 ? 2.0690 1.2687 1.7504 0.3093  -0.4590 -0.0456 169 LYS   L CA  
20857 C  C   . LYS   L  169 ? 2.0228 1.1281 1.7483 0.3613  -0.5180 -0.0219 169 LYS   L C   
20858 O  O   . LYS   L  169 ? 1.9044 1.1770 1.6978 0.2780  -0.5662 -0.0944 169 LYS   L O   
20859 C  CB  . LYS   L  169 ? 2.0589 1.3908 1.7400 0.2616  -0.4311 -0.1058 169 LYS   L CB  
20860 C  CG  . LYS   L  169 ? 2.0562 1.5440 1.7707 0.1856  -0.4065 -0.1837 169 LYS   L CG  
20861 C  CD  . LYS   L  169 ? 2.0840 1.6244 1.8574 0.1293  -0.3347 -0.2419 169 LYS   L CD  
20862 C  CE  . LYS   L  169 ? 2.1540 1.7174 1.8239 0.1443  -0.2984 -0.2622 169 LYS   L CE  
20863 N  NZ  . LYS   L  169 ? 2.1901 1.7528 1.8802 0.1218  -0.2618 -0.2947 169 LYS   L NZ  
20864 N  N   . LYS   L  170 ? 2.0446 1.0514 1.7877 0.3959  -0.4545 0.0241  170 LYS   L N   
20865 C  CA  . LYS   L  170 ? 2.0133 1.1539 1.8393 0.4035  -0.3946 0.1082  170 LYS   L CA  
20866 C  C   . LYS   L  170 ? 2.0021 1.1599 1.8409 0.3914  -0.4381 0.1344  170 LYS   L C   
20867 O  O   . LYS   L  170 ? 2.0429 1.1442 1.9319 0.3204  -0.4023 0.1103  170 LYS   L O   
20868 C  CB  . LYS   L  170 ? 2.0702 1.1157 1.8782 0.3820  -0.2735 0.1699  170 LYS   L CB  
20869 C  CG  . LYS   L  170 ? 2.0835 1.1623 1.9494 0.3765  -0.2211 0.1935  170 LYS   L CG  
20870 C  CD  . LYS   L  170 ? 2.1016 1.2166 1.9207 0.3894  -0.1811 0.1946  170 LYS   L CD  
20871 C  CE  . LYS   L  170 ? 2.1256 1.2539 1.8900 0.3652  -0.1725 0.2152  170 LYS   L CE  
20872 N  NZ  . LYS   L  170 ? 2.1597 1.2057 1.8478 0.3554  -0.1458 0.2648  170 LYS   L NZ  
20873 N  N   . PRO   L  171 ? 1.9724 1.2407 1.8187 0.3855  -0.4913 0.1643  171 PRO   L N   
20874 C  CA  . PRO   L  171 ? 1.9745 1.2455 1.8057 0.4237  -0.5125 0.2267  171 PRO   L CA  
20875 C  C   . PRO   L  171 ? 2.0580 1.2987 1.7945 0.3921  -0.4783 0.2206  171 PRO   L C   
20876 O  O   . PRO   L  171 ? 2.0959 1.4079 1.9154 0.3656  -0.4006 0.2850  171 PRO   L O   
20877 C  CB  . PRO   L  171 ? 1.9554 1.2937 1.7878 0.4162  -0.5218 0.2223  171 PRO   L CB  
20878 C  CG  . PRO   L  171 ? 1.8998 1.2286 1.7910 0.4477  -0.5516 0.2183  171 PRO   L CG  
20879 C  CD  . PRO   L  171 ? 1.9503 1.1818 1.8148 0.4134  -0.5178 0.1698  171 PRO   L CD  
20880 N  N   . LEU   L  172 ? 2.1209 1.2351 1.7839 0.4048  -0.5289 0.1533  172 LEU   L N   
20881 C  CA  . LEU   L  172 ? 2.0847 1.2906 1.7967 0.3999  -0.5482 0.1316  172 LEU   L CA  
20882 C  C   . LEU   L  172 ? 2.0614 1.3415 1.7632 0.3872  -0.5493 0.1315  172 LEU   L C   
20883 O  O   . LEU   L  172 ? 2.0986 1.6050 1.7522 0.3953  -0.6267 0.1213  172 LEU   L O   
20884 C  CB  . LEU   L  172 ? 2.0113 1.3330 1.7697 0.4313  -0.5455 0.1155  172 LEU   L CB  
20885 C  CG  . LEU   L  172 ? 2.0485 1.3226 1.7781 0.4212  -0.5037 0.0657  172 LEU   L CG  
20886 C  CD1 . LEU   L  172 ? 2.0215 1.3593 1.6699 0.4478  -0.4844 0.1348  172 LEU   L CD1 
20887 C  CD2 . LEU   L  172 ? 2.0583 1.1871 1.8084 0.4247  -0.4559 0.0373  172 LEU   L CD2 
20888 N  N   . LYS   L  173 ? 2.0765 1.3033 1.8001 0.2826  -0.4625 0.1548  173 LYS   L N   
20889 C  CA  . LYS   L  173 ? 1.9950 1.2687 1.9084 0.2158  -0.4121 0.1858  173 LYS   L CA  
20890 C  C   . LYS   L  173 ? 2.0193 1.2277 1.8545 0.1514  -0.3320 0.2570  173 LYS   L C   
20891 O  O   . LYS   L  173 ? 2.0642 1.1246 1.9147 0.1346  -0.1996 0.3389  173 LYS   L O   
20892 C  CB  . LYS   L  173 ? 2.0040 1.2119 1.8963 0.2137  -0.4670 0.1488  173 LYS   L CB  
20893 C  CG  . LYS   L  173 ? 1.9873 1.1290 1.9178 0.1853  -0.4757 0.0855  173 LYS   L CG  
20894 C  CD  . LYS   L  173 ? 1.9622 1.1948 2.0001 0.2378  -0.4965 0.0200  173 LYS   L CD  
20895 C  CE  . LYS   L  173 ? 2.0221 1.2371 2.0439 0.2498  -0.4759 0.0567  173 LYS   L CE  
20896 N  NZ  . LYS   L  173 ? 2.1087 1.3903 2.0863 0.3160  -0.4421 -0.0318 173 LYS   L NZ  
20897 N  N   . TYR   L  174 ? 1.9494 1.2608 1.9279 0.1240  -0.2622 0.2181  174 TYR   L N   
20898 C  CA  . TYR   L  174 ? 1.8663 1.2378 1.8994 0.0533  -0.2091 0.2746  174 TYR   L CA  
20899 C  C   . TYR   L  174 ? 1.7632 1.0516 1.8919 0.0974  -0.2932 0.2581  174 TYR   L C   
20900 O  O   . TYR   L  174 ? 1.7264 0.7390 1.9609 0.1220  -0.2251 0.2573  174 TYR   L O   
20901 C  CB  . TYR   L  174 ? 1.8605 1.2395 1.9975 0.0543  -0.1621 0.3178  174 TYR   L CB  
20902 C  CG  . TYR   L  174 ? 1.9936 1.3158 1.9779 0.0557  -0.1096 0.4434  174 TYR   L CG  
20903 C  CD1 . TYR   L  174 ? 1.9685 1.3574 1.9878 -0.0512 -0.0296 0.4964  174 TYR   L CD1 
20904 C  CD2 . TYR   L  174 ? 1.9067 1.3918 2.0160 0.0502  -0.1133 0.5034  174 TYR   L CD2 
20905 C  CE1 . TYR   L  174 ? 1.9660 1.5259 1.9454 -0.0543 0.0163  0.5978  174 TYR   L CE1 
20906 C  CE2 . TYR   L  174 ? 1.9501 1.5229 1.9428 0.0665  -0.0600 0.6151  174 TYR   L CE2 
20907 C  CZ  . TYR   L  174 ? 1.9207 1.6159 1.9650 -0.0173 0.0071  0.6292  174 TYR   L CZ  
20908 O  OH  . TYR   L  174 ? 1.9586 1.6865 1.8409 0.0422  0.0346  0.7716  174 TYR   L OH  
20909 N  N   . LEU   L  175 ? 1.7137 1.0013 1.9069 0.0998  -0.3318 0.2297  175 LEU   L N   
20910 C  CA  . LEU   L  175 ? 1.6369 1.0051 1.8335 0.1296  -0.3729 0.2114  175 LEU   L CA  
20911 C  C   . LEU   L  175 ? 1.5488 0.9985 1.8290 0.1811  -0.4185 0.2328  175 LEU   L C   
20912 O  O   . LEU   L  175 ? 1.4604 0.9898 1.8050 0.2360  -0.4086 0.1902  175 LEU   L O   
20913 C  CB  . LEU   L  175 ? 1.6470 1.0581 1.8711 0.1404  -0.3812 0.2276  175 LEU   L CB  
20914 C  CG  . LEU   L  175 ? 1.7163 1.1444 1.8945 0.1475  -0.3670 0.1745  175 LEU   L CG  
20915 C  CD1 . LEU   L  175 ? 1.7464 1.2169 1.8530 0.1353  -0.3698 0.1899  175 LEU   L CD1 
20916 C  CD2 . LEU   L  175 ? 1.7322 1.1864 1.9406 0.1656  -0.3795 0.2020  175 LEU   L CD2 
20917 N  N   . SER   L  176 ? 1.4980 0.9817 1.8136 0.2003  -0.4544 0.2038  176 SER   L N   
20918 C  CA  . SER   L  176 ? 1.5276 1.0002 1.9112 0.1865  -0.4014 0.1552  176 SER   L CA  
20919 C  C   . SER   L  176 ? 1.5340 0.9803 1.9173 0.1408  -0.4042 0.1024  176 SER   L C   
20920 O  O   . SER   L  176 ? 1.5955 0.9561 2.0185 0.1617  -0.2979 0.0358  176 SER   L O   
20921 C  CB  . SER   L  176 ? 1.4876 1.0453 1.8554 0.2165  -0.4683 0.1612  176 SER   L CB  
20922 O  OG  . SER   L  176 ? 1.4544 1.0549 1.8001 0.2366  -0.5267 0.1788  176 SER   L OG  
20923 N  N   . VAL   L  177 ? 1.5740 1.0534 2.0439 0.0904  -0.3353 0.0109  177 VAL   L N   
20924 C  CA  . VAL   L  177 ? 1.5669 1.0445 2.0328 0.0930  -0.3185 0.0560  177 VAL   L CA  
20925 C  C   . VAL   L  177 ? 1.5704 0.9843 2.1004 0.1048  -0.3283 0.0398  177 VAL   L C   
20926 O  O   . VAL   L  177 ? 1.5886 0.9005 2.1489 0.1279  -0.3226 0.0394  177 VAL   L O   
20927 C  CB  . VAL   L  177 ? 1.5518 1.1520 2.0028 0.1167  -0.2930 0.0026  177 VAL   L CB  
20928 C  CG1 . VAL   L  177 ? 1.5773 1.1920 2.0117 0.1133  -0.2606 -0.0055 177 VAL   L CG1 
20929 C  CG2 . VAL   L  177 ? 1.4984 1.1302 1.9672 0.1031  -0.2548 -0.0026 177 VAL   L CG2 
20930 N  N   . GLU   L  178 ? 1.5542 0.9899 2.1784 0.1179  -0.3196 0.0424  178 GLU   L N   
20931 C  CA  . GLU   L  178 ? 1.5680 0.9862 2.2475 0.1061  -0.2905 0.0383  178 GLU   L CA  
20932 C  C   . GLU   L  178 ? 1.4930 0.9441 2.2024 0.0558  -0.3041 0.0484  178 GLU   L C   
20933 O  O   . GLU   L  178 ? 1.3561 0.8004 2.2559 0.0339  -0.2767 0.0152  178 GLU   L O   
20934 C  CB  . GLU   L  178 ? 1.5501 1.0276 2.3254 0.1584  -0.2767 0.0738  178 GLU   L CB  
20935 C  CG  . GLU   L  178 ? 1.5704 1.1248 2.3217 0.1791  -0.2347 0.0815  178 GLU   L CG  
20936 C  CD  . GLU   L  178 ? 1.6126 1.1703 2.2875 0.2094  -0.2342 0.1135  178 GLU   L CD  
20937 O  OE1 . GLU   L  178 ? 1.5495 1.0992 2.2774 0.2250  -0.2871 0.1370  178 GLU   L OE1 
20938 O  OE2 . GLU   L  178 ? 1.7081 1.2829 2.3413 0.1899  -0.2407 0.2939  178 GLU   L OE2 
20939 N  N   . GLU   L  179 ? 1.5356 0.9720 2.1954 0.0189  -0.2881 0.0469  179 GLU   L N   
20940 C  CA  . GLU   L  179 ? 1.5547 1.0254 2.0239 -0.0005 -0.3177 0.0233  179 GLU   L CA  
20941 C  C   . GLU   L  179 ? 1.5693 0.9643 1.9629 -0.0599 -0.3393 0.0126  179 GLU   L C   
20942 O  O   . GLU   L  179 ? 1.4967 1.0403 2.0068 -0.0410 -0.3490 0.0441  179 GLU   L O   
20943 C  CB  . GLU   L  179 ? 1.6628 1.1109 2.0076 -0.0252 -0.2925 0.0239  179 GLU   L CB  
20944 C  CG  . GLU   L  179 ? 1.6776 1.2984 1.9397 -0.0597 -0.3482 0.0155  179 GLU   L CG  
20945 C  CD  . GLU   L  179 ? 1.7602 1.3293 1.9239 -0.0761 -0.3378 0.1142  179 GLU   L CD  
20946 O  OE1 . GLU   L  179 ? 1.7960 1.3965 1.9499 -0.0932 -0.3286 0.1693  179 GLU   L OE1 
20947 O  OE2 . GLU   L  179 ? 1.8321 1.4160 1.8754 0.0392  -0.3546 0.1533  179 GLU   L OE2 
20948 N  N   . VAL   L  180 ? 1.4349 0.9314 1.8297 0.0096  -0.4125 -0.0009 180 VAL   L N   
20949 C  CA  . VAL   L  180 ? 1.4371 0.8216 1.7791 0.0146  -0.4272 -0.0232 180 VAL   L CA  
20950 C  C   . VAL   L  180 ? 1.4253 0.8273 1.7698 0.0175  -0.4242 -0.0479 180 VAL   L C   
20951 O  O   . VAL   L  180 ? 1.4548 0.7754 1.8691 0.0252  -0.4167 -0.1018 180 VAL   L O   
20952 C  CB  . VAL   L  180 ? 1.3874 0.8312 1.6865 0.0070  -0.4417 0.0119  180 VAL   L CB  
20953 C  CG1 . VAL   L  180 ? 1.3724 0.7691 1.6769 0.0222  -0.4265 0.0195  180 VAL   L CG1 
20954 C  CG2 . VAL   L  180 ? 1.4002 0.8448 1.6799 -0.0103 -0.4477 0.0055  180 VAL   L CG2 
20955 N  N   . ILE   L  181 ? 1.4418 0.8242 1.7613 0.0490  -0.4266 -0.0434 181 ILE   L N   
20956 C  CA  . ILE   L  181 ? 1.4966 0.7612 1.7514 0.0361  -0.4133 -0.0475 181 ILE   L CA  
20957 C  C   . ILE   L  181 ? 1.4679 0.7474 1.7527 0.0372  -0.4537 -0.0785 181 ILE   L C   
20958 O  O   . ILE   L  181 ? 1.4657 0.7020 1.7980 0.0648  -0.4425 -0.0649 181 ILE   L O   
20959 C  CB  . ILE   L  181 ? 1.5707 0.7910 1.7292 0.0262  -0.3957 -0.0720 181 ILE   L CB  
20960 C  CG1 . ILE   L  181 ? 1.5928 0.7858 1.6497 0.0145  -0.4088 -0.0612 181 ILE   L CG1 
20961 C  CG2 . ILE   L  181 ? 1.5941 0.8253 1.7316 0.0151  -0.3622 -0.0710 181 ILE   L CG2 
20962 C  CD1 . ILE   L  181 ? 1.5914 0.7446 1.6596 -0.0096 -0.4052 -0.0639 181 ILE   L CD1 
20963 N  N   . LYS   L  182 ? 1.4833 0.6837 1.7849 0.0454  -0.4885 -0.0547 182 LYS   L N   
20964 C  CA  . LYS   L  182 ? 1.4620 0.6803 1.8005 0.0295  -0.5021 -0.0728 182 LYS   L CA  
20965 C  C   . LYS   L  182 ? 1.4737 0.4544 1.7041 -0.0112 -0.5041 -0.1053 182 LYS   L C   
20966 O  O   . LYS   L  182 ? 1.4135 0.3494 1.7168 -0.0110 -0.4959 -0.1887 182 LYS   L O   
20967 C  CB  . LYS   L  182 ? 1.4658 0.7142 1.8680 0.0163  -0.5258 -0.0704 182 LYS   L CB  
20968 C  CG  . LYS   L  182 ? 1.4743 0.8169 1.9405 -0.0037 -0.4961 -0.0747 182 LYS   L CG  
20969 C  CD  . LYS   L  182 ? 1.4758 0.9174 1.9810 -0.0183 -0.5190 -0.0911 182 LYS   L CD  
20970 C  CE  . LYS   L  182 ? 1.4702 1.0125 2.0171 -0.0337 -0.5106 -0.1012 182 LYS   L CE  
20971 N  NZ  . LYS   L  182 ? 1.4683 1.0841 2.0603 -0.0241 -0.5291 -0.1206 182 LYS   L NZ  
20972 N  N   . LEU   L  183 ? 1.5088 0.4184 1.6843 0.0145  -0.5209 -0.0707 183 LEU   L N   
20973 C  CA  . LEU   L  183 ? 1.5488 0.4545 1.6599 0.0329  -0.4796 -0.0150 183 LEU   L CA  
20974 C  C   . LEU   L  183 ? 1.5257 0.5226 1.6645 0.0384  -0.4759 0.0267  183 LEU   L C   
20975 O  O   . LEU   L  183 ? 1.5173 0.4508 1.7649 0.0143  -0.4428 -0.0435 183 LEU   L O   
20976 C  CB  . LEU   L  183 ? 1.6011 0.4979 1.6529 0.0248  -0.4858 -0.0062 183 LEU   L CB  
20977 C  CG  . LEU   L  183 ? 1.6031 0.5315 1.6884 0.0032  -0.5081 0.0044  183 LEU   L CG  
20978 C  CD1 . LEU   L  183 ? 1.6420 0.5466 1.6837 0.0201  -0.5268 0.0207  183 LEU   L CD1 
20979 C  CD2 . LEU   L  183 ? 1.6049 0.5345 1.6749 0.0257  -0.5166 0.0110  183 LEU   L CD2 
20980 N  N   . VAL   L  184 ? 1.5251 0.5136 1.6400 0.0921  -0.4357 0.0501  184 VAL   L N   
20981 C  CA  . VAL   L  184 ? 1.5117 0.5627 1.6236 0.0903  -0.4174 0.0485  184 VAL   L CA  
20982 C  C   . VAL   L  184 ? 1.5612 0.6362 1.6140 0.0554  -0.3989 0.0709  184 VAL   L C   
20983 O  O   . VAL   L  184 ? 1.6340 0.5386 1.6001 0.1034  -0.3902 0.0907  184 VAL   L O   
20984 C  CB  . VAL   L  184 ? 1.4983 0.5256 1.6469 0.1240  -0.3739 0.1126  184 VAL   L CB  
20985 C  CG1 . VAL   L  184 ? 1.4574 0.4557 1.6310 0.1437  -0.3492 0.1205  184 VAL   L CG1 
20986 C  CG2 . VAL   L  184 ? 1.4906 0.6102 1.5978 0.1009  -0.3682 0.1210  184 VAL   L CG2 
20987 N  N   . ARG   L  185 ? 1.5624 0.6999 1.6257 0.0152  -0.4145 0.0783  185 ARG   L N   
20988 C  CA  . ARG   L  185 ? 1.5650 0.7254 1.6774 -0.0220 -0.3949 0.1140  185 ARG   L CA  
20989 C  C   . ARG   L  185 ? 1.5934 0.7444 1.6743 -0.0156 -0.3994 0.1018  185 ARG   L C   
20990 O  O   . ARG   L  185 ? 1.6169 0.8357 1.6991 -0.0130 -0.4292 0.1242  185 ARG   L O   
20991 C  CB  . ARG   L  185 ? 1.5686 0.7409 1.7110 -0.0409 -0.3769 0.1204  185 ARG   L CB  
20992 C  CG  . ARG   L  185 ? 1.5680 0.8036 1.7151 -0.0323 -0.3268 0.0957  185 ARG   L CG  
20993 C  CD  . ARG   L  185 ? 1.5801 0.8599 1.7811 -0.0248 -0.2969 0.0876  185 ARG   L CD  
20994 N  NE  . ARG   L  185 ? 1.6416 0.8646 1.8017 -0.0219 -0.2782 0.0965  185 ARG   L NE  
20995 C  CZ  . ARG   L  185 ? 1.6311 0.9225 1.8534 -0.0006 -0.2532 0.0731  185 ARG   L CZ  
20996 N  NH1 . ARG   L  185 ? 1.6328 0.9333 1.8752 0.0030  -0.2876 0.0498  185 ARG   L NH1 
20997 N  NH2 . ARG   L  185 ? 1.7455 0.9287 1.8840 -0.0101 -0.2191 0.0959  185 ARG   L NH2 
20998 N  N   . ASP   L  186 ? 1.5849 0.7517 1.6425 -0.0065 -0.4349 0.1633  186 ASP   L N   
20999 C  CA  . ASP   L  186 ? 1.5725 0.7028 1.6826 -0.0010 -0.4569 0.2036  186 ASP   L CA  
21000 C  C   . ASP   L  186 ? 1.5607 0.7007 1.6695 -0.0054 -0.4821 0.1868  186 ASP   L C   
21001 O  O   . ASP   L  186 ? 1.5728 0.6843 1.7717 -0.0052 -0.4804 0.1547  186 ASP   L O   
21002 C  CB  . ASP   L  186 ? 1.6262 0.6615 1.6572 0.0256  -0.4530 0.2015  186 ASP   L CB  
21003 C  CG  . ASP   L  186 ? 1.6365 0.6877 1.6984 0.0357  -0.4184 0.2178  186 ASP   L CG  
21004 O  OD1 . ASP   L  186 ? 1.6741 0.7635 1.7367 0.0725  -0.3560 0.2571  186 ASP   L OD1 
21005 O  OD2 . ASP   L  186 ? 1.6692 0.6181 1.6584 0.0374  -0.4140 0.2138  186 ASP   L OD2 
21006 N  N   . SER   L  187 ? 1.4807 0.7489 1.6347 -0.0085 -0.5000 0.2114  187 SER   L N   
21007 C  CA  . SER   L  187 ? 1.4895 0.7425 1.6324 -0.0342 -0.4764 0.1861  187 SER   L CA  
21008 C  C   . SER   L  187 ? 1.4297 0.7650 1.6733 -0.0274 -0.4845 0.1849  187 SER   L C   
21009 O  O   . SER   L  187 ? 1.4446 0.5802 1.7217 -0.0697 -0.4837 0.2197  187 SER   L O   
21010 C  CB  . SER   L  187 ? 1.4668 0.7595 1.5563 -0.0304 -0.4723 0.1910  187 SER   L CB  
21011 O  OG  . SER   L  187 ? 1.5187 0.7160 1.5035 -0.1113 -0.4168 0.1106  187 SER   L OG  
21012 N  N   . PHE   L  188 ? 1.4491 0.8634 1.6971 -0.0258 -0.4610 0.1524  188 PHE   L N   
21013 C  CA  . PHE   L  188 ? 1.4602 0.8487 1.6728 -0.0073 -0.4407 0.1325  188 PHE   L CA  
21014 C  C   . PHE   L  188 ? 1.4690 0.8286 1.7108 -0.0310 -0.4087 0.1102  188 PHE   L C   
21015 O  O   . PHE   L  188 ? 1.5054 0.8750 1.7750 0.0627  -0.4116 0.0656  188 PHE   L O   
21016 C  CB  . PHE   L  188 ? 1.4558 0.7932 1.7027 -0.0447 -0.4421 0.1346  188 PHE   L CB  
21017 C  CG  . PHE   L  188 ? 1.4953 0.7586 1.6650 -0.0430 -0.4572 0.1165  188 PHE   L CG  
21018 C  CD1 . PHE   L  188 ? 1.4817 0.7880 1.6631 -0.0655 -0.4935 0.1326  188 PHE   L CD1 
21019 C  CD2 . PHE   L  188 ? 1.5036 0.7940 1.6615 -0.0437 -0.4564 0.0942  188 PHE   L CD2 
21020 C  CE1 . PHE   L  188 ? 1.5340 0.7833 1.6321 -0.0614 -0.4613 0.1862  188 PHE   L CE1 
21021 C  CE2 . PHE   L  188 ? 1.5234 0.8063 1.6223 -0.0376 -0.4547 0.1809  188 PHE   L CE2 
21022 C  CZ  . PHE   L  188 ? 1.5266 0.7823 1.6398 -0.0644 -0.4532 0.1926  188 PHE   L CZ  
21023 N  N   . THR   L  189 ? 1.4546 0.7534 1.6316 -0.0050 -0.4294 0.1075  189 THR   L N   
21024 C  CA  . THR   L  189 ? 1.4381 0.7419 1.6385 0.0128  -0.4190 0.1099  189 THR   L CA  
21025 C  C   . THR   L  189 ? 1.4894 0.6636 1.6459 -0.0164 -0.4240 0.1004  189 THR   L C   
21026 O  O   . THR   L  189 ? 1.5123 0.5692 1.7525 -0.0314 -0.4212 0.0770  189 THR   L O   
21027 C  CB  . THR   L  189 ? 1.4432 0.8335 1.6173 -0.0131 -0.4403 0.1427  189 THR   L CB  
21028 O  OG1 . THR   L  189 ? 1.4814 0.9743 1.5946 -0.0335 -0.4271 0.1379  189 THR   L OG1 
21029 C  CG2 . THR   L  189 ? 1.4327 0.8468 1.5837 -0.0463 -0.4332 0.1428  189 THR   L CG2 
21030 N  N   . SER   L  190 ? 1.4591 0.4697 1.6268 0.0653  -0.4610 0.1113  190 SER   L N   
21031 C  CA  . SER   L  190 ? 1.4789 0.4074 1.6648 0.0688  -0.4718 0.1037  190 SER   L CA  
21032 C  C   . SER   L  190 ? 1.4722 0.4308 1.5730 0.0718  -0.4505 0.0895  190 SER   L C   
21033 O  O   . SER   L  190 ? 1.3900 0.3821 1.6188 0.0330  -0.4583 0.0268  190 SER   L O   
21034 C  CB  . SER   L  190 ? 1.4518 0.3997 1.6736 0.1049  -0.4965 0.0723  190 SER   L CB  
21035 O  OG  . SER   L  190 ? 1.4348 0.3006 1.7697 0.1431  -0.5127 0.0507  190 SER   L OG  
21036 N  N   . ALA   L  191 ? 1.5109 0.4571 1.5495 0.0354  -0.4122 0.0989  191 ALA   L N   
21037 C  CA  . ALA   L  191 ? 1.4889 0.5466 1.5467 0.0716  -0.3884 0.1184  191 ALA   L CA  
21038 C  C   . ALA   L  191 ? 1.5789 0.5235 1.5416 0.0781  -0.3250 0.1482  191 ALA   L C   
21039 O  O   . ALA   L  191 ? 1.6704 0.3861 1.4944 0.1634  -0.2828 0.0802  191 ALA   L O   
21040 C  CB  . ALA   L  191 ? 1.5063 0.5511 1.5562 0.0664  -0.3746 0.1389  191 ALA   L CB  
21041 N  N   . THR   L  192 ? 1.6044 0.5939 1.5125 0.0373  -0.3088 0.1911  192 THR   L N   
21042 C  CA  . THR   L  192 ? 1.6736 0.6046 1.5015 0.0380  -0.2872 0.1809  192 THR   L CA  
21043 C  C   . THR   L  192 ? 1.6635 0.5977 1.5306 0.0231  -0.2890 0.1912  192 THR   L C   
21044 O  O   . THR   L  192 ? 1.6669 0.3778 1.5150 0.0414  -0.2354 0.2244  192 THR   L O   
21045 C  CB  . THR   L  192 ? 1.7289 0.6591 1.4941 0.0698  -0.2712 0.1613  192 THR   L CB  
21046 O  OG1 . THR   L  192 ? 1.7542 0.6902 1.3911 0.1239  -0.2996 0.2949  192 THR   L OG1 
21047 C  CG2 . THR   L  192 ? 1.7767 0.6998 1.5014 0.0570  -0.2401 0.1821  192 THR   L CG2 
21048 N  N   . GLU   L  193 ? 1.6334 0.6681 1.5433 -0.0042 -0.3393 0.2206  193 GLU   L N   
21049 C  CA  . GLU   L  193 ? 1.6016 0.6727 1.5799 -0.0385 -0.3749 0.2102  193 GLU   L CA  
21050 C  C   . GLU   L  193 ? 1.5718 0.6809 1.5721 -0.0611 -0.3997 0.1971  193 GLU   L C   
21051 O  O   . GLU   L  193 ? 1.5051 0.7085 1.5206 -0.0835 -0.4789 0.1592  193 GLU   L O   
21052 C  CB  . GLU   L  193 ? 1.6382 0.7894 1.5851 -0.0435 -0.3992 0.1908  193 GLU   L CB  
21053 C  CG  . GLU   L  193 ? 1.6500 0.8856 1.6633 -0.0496 -0.3793 0.1600  193 GLU   L CG  
21054 C  CD  . GLU   L  193 ? 1.6980 0.9013 1.7019 -0.0911 -0.3582 0.1621  193 GLU   L CD  
21055 O  OE1 . GLU   L  193 ? 1.7429 1.0030 1.7788 -0.0556 -0.3449 0.0846  193 GLU   L OE1 
21056 O  OE2 . GLU   L  193 ? 1.6733 0.9137 1.6984 -0.0573 -0.3950 0.1264  193 GLU   L OE2 
21057 N  N   . ARG   L  194 ? 1.5607 0.6160 1.5533 -0.0162 -0.4427 0.2422  194 ARG   L N   
21058 C  CA  . ARG   L  194 ? 1.5957 0.6237 1.5680 0.0093  -0.4256 0.2421  194 ARG   L CA  
21059 C  C   . ARG   L  194 ? 1.5414 0.6348 1.5684 0.0412  -0.3939 0.2487  194 ARG   L C   
21060 O  O   . ARG   L  194 ? 1.5867 0.8345 1.6160 0.0515  -0.2832 0.3074  194 ARG   L O   
21061 C  CB  . ARG   L  194 ? 1.6533 0.6371 1.5738 0.0193  -0.4371 0.2315  194 ARG   L CB  
21062 C  CG  . ARG   L  194 ? 1.6889 0.7341 1.7004 -0.0345 -0.4239 0.2070  194 ARG   L CG  
21063 C  CD  . ARG   L  194 ? 1.7195 0.7555 1.7663 0.0186  -0.4215 0.1701  194 ARG   L CD  
21064 N  NE  . ARG   L  194 ? 1.7791 0.8112 1.8312 -0.0146 -0.4028 0.0626  194 ARG   L NE  
21065 C  CZ  . ARG   L  194 ? 1.8241 0.8033 1.9284 -0.0395 -0.4112 -0.0297 194 ARG   L CZ  
21066 N  NH1 . ARG   L  194 ? 1.7759 0.9478 1.9493 -0.1038 -0.4436 -0.0772 194 ARG   L NH1 
21067 N  NH2 . ARG   L  194 ? 1.7804 1.0965 1.9819 -0.1171 -0.4501 -0.0817 194 ARG   L NH2 
21068 N  N   . HIS   L  195 ? 1.5089 0.6248 1.5776 0.0349  -0.4301 0.2335  195 HIS   L N   
21069 C  CA  . HIS   L  195 ? 1.5621 0.5290 1.5348 0.0331  -0.4037 0.1822  195 HIS   L CA  
21070 C  C   . HIS   L  195 ? 1.5573 0.4399 1.5385 -0.0142 -0.4083 0.1840  195 HIS   L C   
21071 O  O   . HIS   L  195 ? 1.5185 0.3331 1.5703 -0.0339 -0.4440 0.1586  195 HIS   L O   
21072 C  CB  . HIS   L  195 ? 1.5784 0.5858 1.4550 0.0617  -0.3986 0.2074  195 HIS   L CB  
21073 C  CG  . HIS   L  195 ? 1.5729 0.6465 1.4639 0.0910  -0.3390 0.2486  195 HIS   L CG  
21074 N  ND1 . HIS   L  195 ? 1.6323 0.6599 1.4133 0.1566  -0.3514 0.1477  195 HIS   L ND1 
21075 C  CD2 . HIS   L  195 ? 1.6057 0.6817 1.4400 0.0908  -0.3524 0.2782  195 HIS   L CD2 
21076 C  CE1 . HIS   L  195 ? 1.6130 0.6348 1.4702 0.1548  -0.3337 0.1967  195 HIS   L CE1 
21077 N  NE2 . HIS   L  195 ? 1.5827 0.6377 1.4546 0.1181  -0.3485 0.2502  195 HIS   L NE2 
21078 N  N   . ILE   L  196 ? 1.5593 0.4207 1.5022 -0.0112 -0.3918 0.2146  196 ILE   L N   
21079 C  CA  . ILE   L  196 ? 1.5682 0.5934 1.5006 -0.0172 -0.3677 0.2156  196 ILE   L CA  
21080 C  C   . ILE   L  196 ? 1.6007 0.6641 1.5071 0.0572  -0.3482 0.1462  196 ILE   L C   
21081 O  O   . ILE   L  196 ? 1.6295 0.8381 1.5319 0.0878  -0.2869 0.2482  196 ILE   L O   
21082 C  CB  . ILE   L  196 ? 1.5120 0.5971 1.4987 -0.0378 -0.3637 0.1531  196 ILE   L CB  
21083 C  CG1 . ILE   L  196 ? 1.5141 0.6312 1.4911 -0.0360 -0.3487 0.1657  196 ILE   L CG1 
21084 C  CG2 . ILE   L  196 ? 1.5154 0.6090 1.4972 -0.0367 -0.3825 0.1308  196 ILE   L CG2 
21085 C  CD1 . ILE   L  196 ? 1.5225 0.6557 1.4986 -0.0216 -0.3479 0.1702  196 ILE   L CD1 
21086 N  N   . GLN   L  197 ? 1.5797 0.7819 1.4569 0.0403  -0.3007 0.1516  197 GLN   L N   
21087 C  CA  . GLN   L  197 ? 1.5346 0.7549 1.4645 0.0829  -0.2765 0.1737  197 GLN   L CA  
21088 C  C   . GLN   L  197 ? 1.5360 0.7723 1.4630 0.0866  -0.2993 0.1895  197 GLN   L C   
21089 O  O   . GLN   L  197 ? 1.6206 0.8590 1.4923 0.1673  -0.1977 0.1049  197 GLN   L O   
21090 C  CB  . GLN   L  197 ? 1.4621 0.7920 1.4234 0.1186  -0.2812 0.1542  197 GLN   L CB  
21091 C  CG  . GLN   L  197 ? 1.4525 0.8200 1.3870 0.1259  -0.2861 0.1210  197 GLN   L CG  
21092 C  CD  . GLN   L  197 ? 1.4023 0.8775 1.2992 0.1904  -0.2821 0.0940  197 GLN   L CD  
21093 O  OE1 . GLN   L  197 ? 1.3766 0.9988 1.1548 0.1945  -0.3233 0.0066  197 GLN   L OE1 
21094 N  NE2 . GLN   L  197 ? 1.3719 0.9444 1.3426 0.2119  -0.2277 0.0516  197 GLN   L NE2 
21095 N  N   . VAL   L  198 ? 1.5621 0.6488 1.4073 0.1002  -0.2987 0.1886  198 VAL   L N   
21096 C  CA  . VAL   L  198 ? 1.5393 0.7252 1.4051 0.0859  -0.3140 0.1651  198 VAL   L CA  
21097 C  C   . VAL   L  198 ? 1.5545 0.8103 1.4200 0.0597  -0.3217 0.1902  198 VAL   L C   
21098 O  O   . VAL   L  198 ? 1.5527 0.8237 1.4177 0.0726  -0.3864 0.1876  198 VAL   L O   
21099 C  CB  . VAL   L  198 ? 1.5737 0.7468 1.4104 0.0943  -0.3026 0.1095  198 VAL   L CB  
21100 C  CG1 . VAL   L  198 ? 1.5471 0.7698 1.4381 0.0843  -0.2745 0.1059  198 VAL   L CG1 
21101 C  CG2 . VAL   L  198 ? 1.5521 0.7830 1.3833 0.1092  -0.2955 0.0702  198 VAL   L CG2 
21102 N  N   . GLY   L  199 ? 1.5468 0.7324 1.4370 0.0237  -0.3253 0.1920  199 GLY   L N   
21103 C  CA  . GLY   L  199 ? 1.5627 0.7177 1.4566 -0.0059 -0.3162 0.1846  199 GLY   L CA  
21104 C  C   . GLY   L  199 ? 1.5667 0.6739 1.4711 -0.0262 -0.3180 0.1899  199 GLY   L C   
21105 O  O   . GLY   L  199 ? 1.5252 0.6710 1.3455 0.0206  -0.3181 0.2226  199 GLY   L O   
21106 N  N   . ASP   L  200 ? 1.5977 0.7057 1.5039 -0.0654 -0.3042 0.1827  200 ASP   L N   
21107 C  CA  . ASP   L  200 ? 1.6351 0.6268 1.5736 -0.0404 -0.3430 0.1355  200 ASP   L CA  
21108 C  C   . ASP   L  200 ? 1.6446 0.4964 1.5867 -0.0488 -0.3479 0.0671  200 ASP   L C   
21109 O  O   . ASP   L  200 ? 1.6154 0.3211 1.5641 -0.0557 -0.3765 -0.0169 200 ASP   L O   
21110 C  CB  . ASP   L  200 ? 1.6459 0.7471 1.5670 -0.0889 -0.3470 0.1604  200 ASP   L CB  
21111 C  CG  . ASP   L  200 ? 1.7242 0.8177 1.5531 -0.0753 -0.3503 0.2521  200 ASP   L CG  
21112 O  OD1 . ASP   L  200 ? 1.7942 0.8574 1.5220 -0.1164 -0.4117 0.2814  200 ASP   L OD1 
21113 O  OD2 . ASP   L  200 ? 1.6892 0.9922 1.4979 -0.0198 -0.3385 0.3292  200 ASP   L OD2 
21114 N  N   . GLY   L  201 ? 1.6283 0.4745 1.6017 0.0512  -0.3386 0.0779  201 GLY   L N   
21115 C  CA  . GLY   L  201 ? 1.6469 0.5013 1.6718 0.1025  -0.3080 0.0470  201 GLY   L CA  
21116 C  C   . GLY   L  201 ? 1.6339 0.4232 1.6659 0.1738  -0.3191 0.0403  201 GLY   L C   
21117 O  O   . GLY   L  201 ? 1.6560 0.3064 1.6355 0.2935  -0.2657 -0.0045 201 GLY   L O   
21118 N  N   . LEU   L  202 ? 1.6537 0.4610 1.6886 0.1623  -0.3546 0.0558  202 LEU   L N   
21119 C  CA  . LEU   L  202 ? 1.6778 0.5488 1.6548 0.0930  -0.3405 0.0443  202 LEU   L CA  
21120 C  C   . LEU   L  202 ? 1.6884 0.5272 1.6924 0.0726  -0.3474 0.0507  202 LEU   L C   
21121 O  O   . LEU   L  202 ? 1.6797 0.3726 1.7161 0.0002  -0.3554 0.1127  202 LEU   L O   
21122 C  CB  . LEU   L  202 ? 1.6851 0.4976 1.6522 0.1406  -0.3213 0.0185  202 LEU   L CB  
21123 C  CG  . LEU   L  202 ? 1.6663 0.5058 1.6572 0.1353  -0.3068 0.0348  202 LEU   L CG  
21124 C  CD1 . LEU   L  202 ? 1.6741 0.4656 1.6327 0.1745  -0.2777 0.0441  202 LEU   L CD1 
21125 C  CD2 . LEU   L  202 ? 1.6484 0.5272 1.6701 0.1353  -0.3344 0.0419  202 LEU   L CD2 
21126 N  N   . GLU   L  203 ? 1.6617 0.6191 1.6779 0.0269  -0.3107 0.0467  203 GLU   L N   
21127 C  CA  . GLU   L  203 ? 1.6534 0.6419 1.6674 0.0449  -0.2878 -0.0040 203 GLU   L CA  
21128 C  C   . GLU   L  203 ? 1.6040 0.6394 1.6803 0.0215  -0.3119 0.0212  203 GLU   L C   
21129 O  O   . GLU   L  203 ? 1.5947 0.5680 1.6415 0.1153  -0.3049 0.0146  203 GLU   L O   
21130 C  CB  . GLU   L  203 ? 1.6560 0.7262 1.6741 0.0292  -0.2519 -0.0699 203 GLU   L CB  
21131 C  CG  . GLU   L  203 ? 1.6950 0.7661 1.6699 0.0320  -0.2161 -0.1403 203 GLU   L CG  
21132 C  CD  . GLU   L  203 ? 1.7182 0.8261 1.6724 0.0623  -0.1775 -0.1962 203 GLU   L CD  
21133 O  OE1 . GLU   L  203 ? 1.7054 0.9404 1.6605 0.0690  -0.1828 -0.3308 203 GLU   L OE1 
21134 O  OE2 . GLU   L  203 ? 1.7232 0.7162 1.6279 0.0729  -0.1512 -0.1858 203 GLU   L OE2 
21135 N  N   . ILE   L  204 ? 1.6195 0.6728 1.6863 -0.0386 -0.3668 0.0603  204 ILE   L N   
21136 C  CA  . ILE   L  204 ? 1.6706 0.7379 1.6987 -0.0216 -0.3708 0.0826  204 ILE   L CA  
21137 C  C   . ILE   L  204 ? 1.5987 0.7014 1.6975 -0.0825 -0.3982 0.1103  204 ILE   L C   
21138 O  O   . ILE   L  204 ? 1.5975 0.6076 1.7004 -0.1397 -0.3789 0.1200  204 ILE   L O   
21139 C  CB  . ILE   L  204 ? 1.7308 0.8173 1.7324 -0.0333 -0.4103 0.0661  204 ILE   L CB  
21140 C  CG1 . ILE   L  204 ? 1.8057 0.8233 1.7377 -0.0251 -0.3753 0.0843  204 ILE   L CG1 
21141 C  CG2 . ILE   L  204 ? 1.7649 0.8496 1.7591 0.0459  -0.4240 0.1044  204 ILE   L CG2 
21142 C  CD1 . ILE   L  204 ? 1.8344 0.8758 1.7812 -0.0554 -0.3785 0.0589  204 ILE   L CD1 
21143 N  N   . LEU   L  205 ? 1.5419 0.7740 1.6741 -0.0661 -0.3886 0.1371  205 LEU   L N   
21144 C  CA  . LEU   L  205 ? 1.5341 0.7910 1.6862 -0.0523 -0.3206 0.1854  205 LEU   L CA  
21145 C  C   . LEU   L  205 ? 1.5664 0.8003 1.6414 -0.0526 -0.2612 0.2061  205 LEU   L C   
21146 O  O   . LEU   L  205 ? 1.5432 0.7773 1.6479 -0.0729 -0.2326 0.2464  205 LEU   L O   
21147 C  CB  . LEU   L  205 ? 1.5019 0.7593 1.6820 -0.0361 -0.2941 0.2273  205 LEU   L CB  
21148 C  CG  . LEU   L  205 ? 1.4901 0.7381 1.6835 -0.0172 -0.2754 0.2231  205 LEU   L CG  
21149 C  CD1 . LEU   L  205 ? 1.4996 0.8045 1.6982 0.0322  -0.2940 0.2327  205 LEU   L CD1 
21150 C  CD2 . LEU   L  205 ? 1.4708 0.7021 1.6515 0.0103  -0.2757 0.2254  205 LEU   L CD2 
21151 N  N   . ILE   L  206 ? 1.6027 0.7719 1.7009 -0.0173 -0.2684 0.1856  206 ILE   L N   
21152 C  CA  . ILE   L  206 ? 1.6697 0.7937 1.6801 0.0174  -0.2907 0.1086  206 ILE   L CA  
21153 C  C   . ILE   L  206 ? 1.6459 0.7859 1.6793 0.0481  -0.2959 0.0656  206 ILE   L C   
21154 O  O   . ILE   L  206 ? 1.6644 0.9283 1.7182 0.0689  -0.2798 -0.0003 206 ILE   L O   
21155 C  CB  . ILE   L  206 ? 1.6609 0.8583 1.7277 0.0332  -0.2672 0.0782  206 ILE   L CB  
21156 C  CG1 . ILE   L  206 ? 1.7444 0.8699 1.7362 0.0582  -0.2432 0.0847  206 ILE   L CG1 
21157 C  CG2 . ILE   L  206 ? 1.6878 0.8272 1.7522 0.0829  -0.2894 0.0616  206 ILE   L CG2 
21158 C  CD1 . ILE   L  206 ? 1.7632 0.9364 1.7524 0.0306  -0.1797 0.0592  206 ILE   L CD1 
21159 N  N   . VAL   L  207 ? 1.6284 0.6716 1.6788 0.0560  -0.3208 0.0643  207 VAL   L N   
21160 C  CA  . VAL   L  207 ? 1.5934 0.6478 1.7391 -0.0013 -0.3105 0.0260  207 VAL   L CA  
21161 C  C   . VAL   L  207 ? 1.6254 0.5112 1.7715 -0.0208 -0.3298 0.0261  207 VAL   L C   
21162 O  O   . VAL   L  207 ? 1.7209 0.3669 1.7896 -0.0405 -0.3104 0.0307  207 VAL   L O   
21163 C  CB  . VAL   L  207 ? 1.5692 0.6299 1.6909 0.0200  -0.3378 0.0614  207 VAL   L CB  
21164 C  CG1 . VAL   L  207 ? 1.5734 0.6738 1.7116 0.0478  -0.3418 0.1504  207 VAL   L CG1 
21165 C  CG2 . VAL   L  207 ? 1.5577 0.5745 1.6545 0.0290  -0.3055 0.0655  207 VAL   L CG2 
21166 N  N   . THR   L  208 ? 1.5817 0.6195 1.8543 -0.0186 -0.2922 0.0226  208 THR   L N   
21167 C  CA  . THR   L  208 ? 1.5417 0.7768 1.8704 -0.0073 -0.3045 0.0241  208 THR   L CA  
21168 C  C   . THR   L  208 ? 1.5523 0.7799 1.9061 0.0106  -0.2751 0.0028  208 THR   L C   
21169 O  O   . THR   L  208 ? 1.5591 0.6496 1.8989 0.0237  -0.2808 0.0281  208 THR   L O   
21170 C  CB  . THR   L  208 ? 1.5271 0.8612 1.9138 -0.0175 -0.3178 -0.0266 208 THR   L CB  
21171 O  OG1 . THR   L  208 ? 1.5709 1.0061 1.9355 -0.0457 -0.2804 -0.0658 208 THR   L OG1 
21172 C  CG2 . THR   L  208 ? 1.5068 0.8520 1.9296 0.0369  -0.3249 -0.0054 208 THR   L CG2 
21173 N  N   . LYS   L  209 ? 1.5500 0.8511 1.9509 0.0787  -0.2699 -0.0133 209 LYS   L N   
21174 C  CA  . LYS   L  209 ? 1.5496 0.8500 1.9623 0.0937  -0.2481 -0.0183 209 LYS   L CA  
21175 C  C   . LYS   L  209 ? 1.5583 0.8710 1.9949 0.0990  -0.1935 -0.0130 209 LYS   L C   
21176 O  O   . LYS   L  209 ? 1.6427 0.8141 2.0039 0.1813  -0.1721 0.0273  209 LYS   L O   
21177 C  CB  . LYS   L  209 ? 1.5645 0.8182 1.9886 0.0847  -0.2572 0.0071  209 LYS   L CB  
21178 C  CG  . LYS   L  209 ? 1.5925 0.9007 2.0340 0.0223  -0.2410 -0.0237 209 LYS   L CG  
21179 C  CD  . LYS   L  209 ? 1.5587 0.9928 2.0220 -0.0359 -0.2768 -0.0229 209 LYS   L CD  
21180 C  CE  . LYS   L  209 ? 1.5685 1.1251 2.0738 -0.0804 -0.2755 -0.0243 209 LYS   L CE  
21181 N  NZ  . LYS   L  209 ? 1.5611 1.1846 2.1095 -0.1333 -0.2557 -0.0141 209 LYS   L NZ  
21182 N  N   . ASP   L  210 ? 1.5682 0.9184 2.0099 0.0434  -0.1743 -0.0299 210 ASP   L N   
21183 C  CA  . ASP   L  210 ? 1.5927 0.9759 1.9881 -0.0168 -0.1522 0.0226  210 ASP   L CA  
21184 C  C   . ASP   L  210 ? 1.4888 0.8852 2.0054 -0.0082 -0.1041 0.0880  210 ASP   L C   
21185 O  O   . ASP   L  210 ? 1.4718 0.9704 1.9598 -0.0668 -0.0702 0.1515  210 ASP   L O   
21186 C  CB  . ASP   L  210 ? 1.6433 1.0719 2.0082 -0.0880 -0.1658 0.0144  210 ASP   L CB  
21187 C  CG  . ASP   L  210 ? 1.7539 1.2698 2.0004 -0.1169 -0.2460 -0.0015 210 ASP   L CG  
21188 O  OD1 . ASP   L  210 ? 1.7975 1.3109 2.0144 -0.2254 -0.2472 0.0042  210 ASP   L OD1 
21189 O  OD2 . ASP   L  210 ? 1.8322 1.4418 1.9361 -0.2050 -0.2071 -0.0210 210 ASP   L OD2 
21190 N  N   . GLY   L  211 ? 1.5194 0.7899 1.9530 -0.0008 -0.0977 0.0822  211 GLY   L N   
21191 C  CA  . GLY   L  211 ? 1.5698 0.7805 1.9048 0.0462  -0.0949 0.0559  211 GLY   L CA  
21192 C  C   . GLY   L  211 ? 1.5930 0.8073 1.8214 0.0875  -0.1172 0.0010  211 GLY   L C   
21193 O  O   . GLY   L  211 ? 1.6284 0.8338 1.8442 0.0864  -0.1267 -0.0292 211 GLY   L O   
21194 N  N   . VAL   L  212 ? 1.5410 0.7684 1.8087 0.1349  -0.1055 -0.0308 212 VAL   L N   
21195 C  CA  . VAL   L  212 ? 1.4993 0.7262 1.7535 0.1142  -0.1098 -0.0832 212 VAL   L CA  
21196 C  C   . VAL   L  212 ? 1.4548 0.7725 1.7719 0.1056  -0.1005 -0.0925 212 VAL   L C   
21197 O  O   . VAL   L  212 ? 1.4682 0.6393 1.8520 0.0449  -0.0867 -0.1507 212 VAL   L O   
21198 C  CB  . VAL   L  212 ? 1.5096 0.6830 1.6773 0.1419  -0.1180 -0.1062 212 VAL   L CB  
21199 C  CG1 . VAL   L  212 ? 1.5262 0.7522 1.6798 0.1883  -0.1211 -0.0800 212 VAL   L CG1 
21200 C  CG2 . VAL   L  212 ? 1.5095 0.6259 1.6477 0.1386  -0.1407 -0.1291 212 VAL   L CG2 
21201 N  N   . ARG   L  213 ? 1.4528 0.8063 1.8374 0.0663  -0.1333 -0.0837 213 ARG   L N   
21202 C  CA  . ARG   L  213 ? 1.4550 0.7572 1.9035 0.0441  -0.1683 -0.0557 213 ARG   L CA  
21203 C  C   . ARG   L  213 ? 1.4376 0.7061 1.8593 -0.0210 -0.1897 -0.0200 213 ARG   L C   
21204 O  O   . ARG   L  213 ? 1.4666 0.5877 1.7469 -0.0440 -0.2092 0.0131  213 ARG   L O   
21205 C  CB  . ARG   L  213 ? 1.4267 0.7543 1.9965 0.0648  -0.1734 -0.0775 213 ARG   L CB  
21206 C  CG  . ARG   L  213 ? 1.4324 0.8441 2.0198 0.0733  -0.1240 -0.0859 213 ARG   L CG  
21207 C  CD  . ARG   L  213 ? 1.4716 0.9501 2.0810 0.0574  -0.1467 -0.1576 213 ARG   L CD  
21208 N  NE  . ARG   L  213 ? 1.4997 1.0397 2.0975 0.0596  -0.1171 -0.2120 213 ARG   L NE  
21209 C  CZ  . ARG   L  213 ? 1.5080 1.0153 2.1027 0.0924  -0.1135 -0.1733 213 ARG   L CZ  
21210 N  NH1 . ARG   L  213 ? 1.5012 0.9700 2.0828 0.1905  -0.0933 -0.1958 213 ARG   L NH1 
21211 N  NH2 . ARG   L  213 ? 1.4972 1.1118 2.0735 0.0439  -0.1245 -0.2265 213 ARG   L NH2 
21212 N  N   . LYS   L  214 ? 1.4487 0.8566 1.8601 -0.0941 -0.2138 0.0050  214 LYS   L N   
21213 C  CA  . LYS   L  214 ? 1.4501 0.9206 1.8147 -0.0540 -0.2418 0.0085  214 LYS   L CA  
21214 C  C   . LYS   L  214 ? 1.5515 0.8569 1.8159 -0.0332 -0.2385 0.0856  214 LYS   L C   
21215 O  O   . LYS   L  214 ? 1.7157 0.7506 1.8253 0.0310  -0.0684 0.1151  214 LYS   L O   
21216 C  CB  . LYS   L  214 ? 1.4667 0.9615 1.7952 -0.0441 -0.2346 -0.0094 214 LYS   L CB  
21217 C  CG  . LYS   L  214 ? 1.4105 1.0900 1.7456 -0.0489 -0.2759 -0.0843 214 LYS   L CG  
21218 C  CD  . LYS   L  214 ? 1.3869 1.1961 1.7463 -0.0280 -0.2884 -0.0868 214 LYS   L CD  
21219 C  CE  . LYS   L  214 ? 1.3201 1.2632 1.7181 -0.0603 -0.3189 -0.1170 214 LYS   L CE  
21220 N  NZ  . LYS   L  214 ? 1.3473 1.2871 1.7245 -0.0623 -0.3010 -0.1388 214 LYS   L NZ  
21221 N  N   . GLU   L  215 ? 1.5112 0.9306 1.7737 0.0158  -0.2963 0.0348  215 GLU   L N   
21222 C  CA  . GLU   L  215 ? 1.5243 0.9968 1.7951 -0.0286 -0.3156 0.0713  215 GLU   L CA  
21223 C  C   . GLU   L  215 ? 1.5447 0.9510 1.6538 -0.0458 -0.3125 0.0601  215 GLU   L C   
21224 O  O   . GLU   L  215 ? 1.4906 0.9463 1.5734 -0.0123 -0.3849 -0.0132 215 GLU   L O   
21225 C  CB  . GLU   L  215 ? 1.5806 1.1260 1.8327 -0.0831 -0.3581 0.0673  215 GLU   L CB  
21226 C  CG  . GLU   L  215 ? 1.5411 1.2085 1.8751 -0.1313 -0.3824 0.0932  215 GLU   L CG  
21227 C  CD  . GLU   L  215 ? 1.5190 1.1683 1.9368 -0.1675 -0.3907 0.0879  215 GLU   L CD  
21228 O  OE1 . GLU   L  215 ? 1.3260 1.3220 2.0925 -0.1416 -0.3777 0.0969  215 GLU   L OE1 
21229 O  OE2 . GLU   L  215 ? 1.6647 1.1271 1.9760 -0.2457 -0.3465 0.0888  215 GLU   L OE2 
21230 N  N   . PHE   L  216 ? 1.5439 0.9334 1.6588 -0.0454 -0.3123 0.0672  216 PHE   L N   
21231 C  CA  . PHE   L  216 ? 1.4921 0.8893 1.6740 -0.0632 -0.2567 0.0897  216 PHE   L CA  
21232 C  C   . PHE   L  216 ? 1.5191 0.8150 1.6578 0.0066  -0.2658 0.0870  216 PHE   L C   
21233 O  O   . PHE   L  216 ? 1.5568 0.9048 1.6657 -0.0764 -0.2160 0.0327  216 PHE   L O   
21234 C  CB  . PHE   L  216 ? 1.4491 0.9362 1.6483 -0.0370 -0.2303 0.1241  216 PHE   L CB  
21235 C  CG  . PHE   L  216 ? 1.4310 0.9268 1.6791 -0.0169 -0.1837 0.1476  216 PHE   L CG  
21236 C  CD1 . PHE   L  216 ? 1.4286 0.9167 1.6367 -0.0044 -0.1848 0.1672  216 PHE   L CD1 
21237 C  CD2 . PHE   L  216 ? 1.4294 0.9493 1.6732 -0.0170 -0.1774 0.1515  216 PHE   L CD2 
21238 C  CE1 . PHE   L  216 ? 1.3950 0.9335 1.6094 -0.0088 -0.1887 0.1560  216 PHE   L CE1 
21239 C  CE2 . PHE   L  216 ? 1.4193 0.9814 1.6451 -0.0099 -0.1808 0.1425  216 PHE   L CE2 
21240 C  CZ  . PHE   L  216 ? 1.4125 0.9525 1.6074 -0.0042 -0.1914 0.1664  216 PHE   L CZ  
21241 N  N   . TYR   L  217 ? 1.5017 0.7114 1.6810 -0.0395 -0.2833 0.1361  217 TYR   L N   
21242 C  CA  . TYR   L  217 ? 1.5422 0.7060 1.7323 -0.0477 -0.2894 0.1314  217 TYR   L CA  
21243 C  C   . TYR   L  217 ? 1.5570 0.5707 1.7389 -0.0438 -0.2622 0.1035  217 TYR   L C   
21244 O  O   . TYR   L  217 ? 1.5347 0.3885 1.6476 0.0220  -0.2698 0.1636  217 TYR   L O   
21245 C  CB  . TYR   L  217 ? 1.5447 0.6417 1.7482 -0.0647 -0.3170 0.1384  217 TYR   L CB  
21246 C  CG  . TYR   L  217 ? 1.5680 0.5630 1.7994 -0.0756 -0.3338 0.1563  217 TYR   L CG  
21247 C  CD1 . TYR   L  217 ? 1.5685 0.5466 1.8464 -0.0949 -0.3539 0.1769  217 TYR   L CD1 
21248 C  CD2 . TYR   L  217 ? 1.5487 0.5869 1.7979 -0.0890 -0.3371 0.1621  217 TYR   L CD2 
21249 C  CE1 . TYR   L  217 ? 1.5593 0.6067 1.8873 -0.1033 -0.3713 0.1920  217 TYR   L CE1 
21250 C  CE2 . TYR   L  217 ? 1.5581 0.6400 1.8511 -0.0992 -0.3648 0.1970  217 TYR   L CE2 
21251 C  CZ  . TYR   L  217 ? 1.5499 0.6246 1.9086 -0.0852 -0.3771 0.2211  217 TYR   L CZ  
21252 O  OH  . TYR   L  217 ? 1.6087 0.6021 1.9636 -0.0630 -0.3507 0.3149  217 TYR   L OH  
21253 N  N   . GLU   L  218 ? 1.6239 0.4940 1.7975 -0.0071 -0.2339 0.0977  218 GLU   L N   
21254 C  CA  . GLU   L  218 ? 1.6512 0.4629 1.8168 -0.0161 -0.2123 0.1226  218 GLU   L CA  
21255 C  C   . GLU   L  218 ? 1.6455 0.4461 1.8091 0.0002  -0.2032 0.1618  218 GLU   L C   
21256 O  O   . GLU   L  218 ? 1.7034 0.3584 1.8082 -0.0586 -0.2179 0.2278  218 GLU   L O   
21257 C  CB  . GLU   L  218 ? 1.6737 0.5376 1.8231 -0.0356 -0.1394 0.0780  218 GLU   L CB  
21258 C  CG  . GLU   L  218 ? 1.7051 0.5862 1.8661 -0.0484 -0.0927 0.0486  218 GLU   L CG  
21259 C  CD  . GLU   L  218 ? 1.7151 0.6621 1.8527 -0.0420 -0.0770 0.0199  218 GLU   L CD  
21260 O  OE1 . GLU   L  218 ? 1.7542 0.6721 1.8626 0.0000  -0.0345 0.0110  218 GLU   L OE1 
21261 O  OE2 . GLU   L  218 ? 1.7700 0.6921 1.8989 -0.0326 -0.0188 -0.0426 218 GLU   L OE2 
21262 N  N   . LEU   L  219 ? 1.6664 0.5250 1.7916 0.0166  -0.2535 0.1983  219 LEU   L N   
21263 C  CA  . LEU   L  219 ? 1.6573 0.6301 1.7798 0.0348  -0.2568 0.1506  219 LEU   L CA  
21264 C  C   . LEU   L  219 ? 1.6812 0.6633 1.7853 0.0698  -0.2531 0.1549  219 LEU   L C   
21265 O  O   . LEU   L  219 ? 1.6921 0.8251 1.7717 0.0601  -0.2406 0.1933  219 LEU   L O   
21266 C  CB  . LEU   L  219 ? 1.6273 0.5506 1.7228 0.0752  -0.2807 0.1642  219 LEU   L CB  
21267 C  CG  . LEU   L  219 ? 1.5864 0.5617 1.7093 0.0829  -0.2861 0.1513  219 LEU   L CG  
21268 C  CD1 . LEU   L  219 ? 1.5279 0.5683 1.7015 0.1163  -0.2943 0.1169  219 LEU   L CD1 
21269 C  CD2 . LEU   L  219 ? 1.6000 0.5372 1.7264 0.0794  -0.2872 0.1357  219 LEU   L CD2 
21270 N  N   . LYS   L  220 ? 1.6853 0.6002 1.7518 0.0415  -0.2341 0.2071  220 LYS   L N   
21271 C  CA  . LYS   L  220 ? 1.6685 0.5692 1.7018 -0.0028 -0.2105 0.2013  220 LYS   L CA  
21272 C  C   . LYS   L  220 ? 1.6758 0.4737 1.6559 -0.0246 -0.1838 0.2062  220 LYS   L C   
21273 O  O   . LYS   L  220 ? 1.6713 0.2999 1.5864 -0.0006 -0.2159 0.1743  220 LYS   L O   
21274 C  CB  . LYS   L  220 ? 1.6502 0.6200 1.7235 0.0095  -0.2305 0.1577  220 LYS   L CB  
21275 C  CG  . LYS   L  220 ? 1.6465 0.7120 1.7744 -0.0093 -0.2352 0.1554  220 LYS   L CG  
21276 C  CD  . LYS   L  220 ? 1.6690 0.7392 1.7747 0.0091  -0.2467 0.1441  220 LYS   L CD  
21277 C  CE  . LYS   L  220 ? 1.6857 0.7096 1.7844 0.0059  -0.2423 0.1297  220 LYS   L CE  
21278 N  NZ  . LYS   L  220 ? 1.7344 0.7214 1.8161 -0.0225 -0.2502 0.1070  220 LYS   L NZ  
21279 N  N   . ARG   L  221 ? 1.7287 0.5410 1.6495 -0.0486 -0.1511 0.2067  221 ARG   L N   
21280 C  CA  . ARG   L  221 ? 1.7672 0.6005 1.6158 -0.0857 -0.1371 0.1981  221 ARG   L CA  
21281 C  C   . ARG   L  221 ? 1.7834 0.6482 1.5815 -0.0678 -0.1724 0.1703  221 ARG   L C   
21282 O  O   . ARG   L  221 ? 1.8434 0.5953 1.5401 -0.1468 -0.1585 0.1740  221 ARG   L O   
21283 C  CB  . ARG   L  221 ? 1.7662 0.6848 1.6535 -0.1044 -0.0803 0.2226  221 ARG   L CB  
21284 C  CG  . ARG   L  221 ? 1.7306 0.7403 1.7028 -0.0901 -0.0333 0.2263  221 ARG   L CG  
21285 C  CD  . ARG   L  221 ? 1.7279 0.8344 1.7997 -0.1177 0.0127  0.2216  221 ARG   L CD  
21286 N  NE  . ARG   L  221 ? 1.7117 0.8661 1.8129 -0.1478 0.0350  0.1943  221 ARG   L NE  
21287 C  CZ  . ARG   L  221 ? 1.6109 0.8500 1.8292 -0.1727 0.0539  0.2158  221 ARG   L CZ  
21288 N  NH1 . ARG   L  221 ? 1.6145 0.8194 1.8462 -0.1789 0.0675  0.2167  221 ARG   L NH1 
21289 N  NH2 . ARG   L  221 ? 1.5507 0.9101 1.8282 -0.2217 0.0749  0.1848  221 ARG   L NH2 
21290 N  N   . ASP   L  222 ? 1.8627 0.7297 1.6182 -0.0585 -0.1772 0.1025  222 ASP   L N   
21291 C  CA  . ASP   L  222 ? 1.8250 0.8070 1.6771 -0.0560 -0.2065 0.1581  222 ASP   L CA  
21292 C  C   . ASP   L  222 ? 1.7719 0.8219 1.7079 -0.0891 -0.2479 0.1589  222 ASP   L C   
21293 O  O   . ASP   L  222 ? 1.7117 0.6251 1.8921 -0.1626 -0.2811 0.0708  222 ASP   L O   
21294 C  CB  . ASP   L  222 ? 1.8625 0.7637 1.6700 -0.0447 -0.1855 0.2095  222 ASP   L CB  
21295 C  CG  . ASP   L  222 ? 1.8617 0.7171 1.6647 -0.0221 -0.1668 0.1594  222 ASP   L CG  
21296 O  OD1 . ASP   L  222 ? 1.8834 0.8469 1.6050 -0.0299 -0.2178 0.2135  222 ASP   L OD1 
21297 O  OD2 . ASP   L  222 ? 1.8330 0.6284 1.5600 0.0940  -0.1852 0.2773  222 ASP   L OD2 
21298 O  OXT . ASP   L  222 ? 1.7558 0.8738 1.7679 -0.0817 -0.2846 0.0193  222 ASP   L OXT 
21299 N  N   . THR   M  14  ? 1.8974 0.6783 1.8495 -0.2453 -0.2238 -0.1237 1   THR   M N   
21300 C  CA  . THR   M  14  ? 1.9245 0.6778 1.7882 -0.2479 -0.2507 -0.1262 1   THR   M CA  
21301 C  C   . THR   M  14  ? 1.7053 0.5213 1.7110 -0.2856 -0.1972 -0.2188 1   THR   M C   
21302 O  O   . THR   M  14  ? 1.7769 0.3820 1.7944 -0.3160 -0.2216 -0.3700 1   THR   M O   
21303 C  CB  . THR   M  14  ? 2.0651 0.9607 1.8290 -0.2033 -0.1442 -0.1387 1   THR   M CB  
21304 O  OG1 . THR   M  14  ? 2.2676 0.9658 1.6948 -0.2229 -0.0724 0.0913  1   THR   M OG1 
21305 C  CG2 . THR   M  14  ? 2.0420 0.9821 1.8891 -0.1276 -0.2276 -0.1413 1   THR   M CG2 
21306 N  N   . GLN   M  15  ? 1.7107 0.5477 1.5188 -0.1289 -0.2410 -0.1029 2   GLN   M N   
21307 C  CA  . GLN   M  15  ? 1.6360 0.4037 1.5459 0.0120  -0.2025 -0.0410 2   GLN   M CA  
21308 C  C   . GLN   M  15  ? 1.5910 0.3740 1.4940 0.0534  -0.2323 -0.1492 2   GLN   M C   
21309 O  O   . GLN   M  15  ? 1.5168 0.0919 1.6450 0.0589  -0.2381 -0.1443 2   GLN   M O   
21310 C  CB  . GLN   M  15  ? 1.6524 0.3789 1.5340 0.0498  -0.2062 -0.0082 2   GLN   M CB  
21311 C  CG  . GLN   M  15  ? 1.5838 0.3588 1.5835 0.1625  -0.2080 0.0473  2   GLN   M CG  
21312 C  CD  . GLN   M  15  ? 1.5119 0.3227 1.5860 0.2251  -0.2396 0.1074  2   GLN   M CD  
21313 O  OE1 . GLN   M  15  ? 1.4121 0.1683 1.6304 0.2651  -0.3283 0.0818  2   GLN   M OE1 
21314 N  NE2 . GLN   M  15  ? 1.5368 0.3225 1.6389 0.2286  -0.2795 0.0922  2   GLN   M NE2 
21315 N  N   . GLN   M  16  ? 1.6259 0.3373 1.4764 -0.0061 -0.1708 -0.1109 3   GLN   M N   
21316 C  CA  . GLN   M  16  ? 1.6084 0.3579 1.4040 -0.0122 -0.1617 -0.0998 3   GLN   M CA  
21317 C  C   . GLN   M  16  ? 1.5556 0.2235 1.3909 -0.0042 -0.1335 -0.0389 3   GLN   M C   
21318 O  O   . GLN   M  16  ? 1.5507 0.2727 1.3380 -0.0172 -0.1480 0.0152  3   GLN   M O   
21319 C  CB  . GLN   M  16  ? 1.6113 0.4595 1.4904 0.0437  -0.1431 -0.0512 3   GLN   M CB  
21320 C  CG  . GLN   M  16  ? 1.6556 0.5721 1.5352 -0.0370 -0.1542 -0.0854 3   GLN   M CG  
21321 C  CD  . GLN   M  16  ? 1.6947 0.7332 1.6334 0.0542  -0.1652 -0.0592 3   GLN   M CD  
21322 O  OE1 . GLN   M  16  ? 1.7946 0.8553 1.7219 -0.0955 -0.1499 -0.0346 3   GLN   M OE1 
21323 N  NE2 . GLN   M  16  ? 1.7423 0.8498 1.6734 -0.0779 -0.1756 -0.0561 3   GLN   M NE2 
21324 N  N   . PRO   M  17  ? 1.4884 0.2029 1.3194 0.0235  -0.1784 -0.0598 4   PRO   M N   
21325 C  CA  . PRO   M  17  ? 1.4623 0.2380 1.3214 0.0267  -0.1788 -0.0329 4   PRO   M CA  
21326 C  C   . PRO   M  17  ? 1.5061 0.2412 1.3159 0.0076  -0.2074 -0.0241 4   PRO   M C   
21327 O  O   . PRO   M  17  ? 1.5251 0.2851 1.4646 0.0586  -0.1707 -0.0346 4   PRO   M O   
21328 C  CB  . PRO   M  17  ? 1.4626 0.2177 1.2948 0.0282  -0.1808 -0.0329 4   PRO   M CB  
21329 C  CG  . PRO   M  17  ? 1.4692 0.2713 1.2657 0.0328  -0.1798 -0.0463 4   PRO   M CG  
21330 C  CD  . PRO   M  17  ? 1.4721 0.2485 1.2749 0.0179  -0.1776 -0.0503 4   PRO   M CD  
21331 N  N   . ILE   M  18  ? 1.5062 0.1788 1.2838 0.0380  -0.1924 -0.0107 5   ILE   M N   
21332 C  CA  . ILE   M  18  ? 1.5100 0.2272 1.2255 0.0371  -0.2020 -0.0432 5   ILE   M CA  
21333 C  C   . ILE   M  18  ? 1.5033 0.3339 1.1697 0.0406  -0.2357 -0.0533 5   ILE   M C   
21334 O  O   . ILE   M  18  ? 1.4872 0.3661 1.1119 -0.0074 -0.2777 -0.0265 5   ILE   M O   
21335 C  CB  . ILE   M  18  ? 1.4805 0.2263 1.2353 0.0452  -0.1931 -0.0116 5   ILE   M CB  
21336 C  CG1 . ILE   M  18  ? 1.4770 0.2142 1.2440 0.0702  -0.1769 -0.0155 5   ILE   M CG1 
21337 C  CG2 . ILE   M  18  ? 1.4863 0.2661 1.2687 0.0588  -0.2016 -0.0083 5   ILE   M CG2 
21338 C  CD1 . ILE   M  18  ? 1.4761 0.1182 1.2667 0.0544  -0.1780 0.0221  5   ILE   M CD1 
21339 N  N   . VAL   M  19  ? 1.4970 0.3839 1.1661 0.0668  -0.2181 -0.0601 6   VAL   M N   
21340 C  CA  . VAL   M  19  ? 1.4972 0.4333 1.1824 0.0578  -0.2215 0.0021  6   VAL   M CA  
21341 C  C   . VAL   M  19  ? 1.4925 0.4399 1.1279 0.0210  -0.2249 -0.0154 6   VAL   M C   
21342 O  O   . VAL   M  19  ? 1.4509 0.5887 1.1357 0.0625  -0.2697 0.0664  6   VAL   M O   
21343 C  CB  . VAL   M  19  ? 1.5457 0.5110 1.1732 0.0326  -0.2050 -0.0193 6   VAL   M CB  
21344 C  CG1 . VAL   M  19  ? 1.5780 0.5121 1.1836 -0.0007 -0.2124 0.0266  6   VAL   M CG1 
21345 C  CG2 . VAL   M  19  ? 1.5473 0.5132 1.1806 0.0741  -0.2275 -0.0264 6   VAL   M CG2 
21346 N  N   . THR   M  20  ? 1.5126 0.3558 1.0840 0.0639  -0.2489 -0.0050 7   THR   M N   
21347 C  CA  . THR   M  20  ? 1.5145 0.3779 1.1093 0.0790  -0.2546 0.0256  7   THR   M CA  
21348 C  C   . THR   M  20  ? 1.4882 0.2630 1.1214 0.0962  -0.2726 0.0566  7   THR   M C   
21349 O  O   . THR   M  20  ? 1.5225 0.1899 1.1619 0.0853  -0.2730 0.0855  7   THR   M O   
21350 C  CB  . THR   M  20  ? 1.5298 0.4543 1.0834 0.0625  -0.2662 0.0100  7   THR   M CB  
21351 O  OG1 . THR   M  20  ? 1.5295 0.4971 1.0572 0.0654  -0.3222 0.0284  7   THR   M OG1 
21352 C  CG2 . THR   M  20  ? 1.5268 0.5115 1.1143 0.0850  -0.2570 0.0529  7   THR   M CG2 
21353 N  N   . GLY   M  21  ? 1.4941 0.2403 1.1651 0.1146  -0.2721 0.0689  8   GLY   M N   
21354 C  CA  . GLY   M  21  ? 1.5322 0.2894 1.1711 0.1385  -0.2399 0.1149  8   GLY   M CA  
21355 C  C   . GLY   M  21  ? 1.5318 0.3691 1.1502 0.1473  -0.2566 0.1166  8   GLY   M C   
21356 O  O   . GLY   M  21  ? 1.5947 0.3717 1.1833 0.2131  -0.2472 0.1883  8   GLY   M O   
21357 N  N   . THR   M  22  ? 1.4945 0.4582 1.2167 0.0784  -0.2018 0.0816  9   THR   M N   
21358 C  CA  . THR   M  22  ? 1.4766 0.5206 1.2038 0.1116  -0.2253 0.0242  9   THR   M CA  
21359 C  C   . THR   M  22  ? 1.4601 0.4993 1.1934 0.0904  -0.2010 -0.0030 9   THR   M C   
21360 O  O   . THR   M  22  ? 1.4337 0.4954 1.1724 0.0886  -0.1953 0.0589  9   THR   M O   
21361 C  CB  . THR   M  22  ? 1.4896 0.5389 1.2212 0.1616  -0.2608 0.0318  9   THR   M CB  
21362 O  OG1 . THR   M  22  ? 1.4716 0.5775 1.2792 0.1935  -0.2990 -0.0006 9   THR   M OG1 
21363 C  CG2 . THR   M  22  ? 1.5408 0.5937 1.1871 0.1950  -0.2867 0.0131  9   THR   M CG2 
21364 N  N   . SER   M  23  ? 1.4468 0.5409 1.2523 0.0757  -0.1484 -0.0205 10  SER   M N   
21365 C  CA  . SER   M  23  ? 1.4361 0.5841 1.2805 0.0580  -0.1484 -0.0560 10  SER   M CA  
21366 C  C   . SER   M  23  ? 1.4695 0.5646 1.2568 0.0211  -0.1641 -0.0649 10  SER   M C   
21367 O  O   . SER   M  23  ? 1.4020 0.6082 1.2605 -0.0228 -0.1448 -0.1112 10  SER   M O   
21368 C  CB  . SER   M  23  ? 1.4232 0.6105 1.3563 0.0314  -0.1095 -0.1104 10  SER   M CB  
21369 O  OG  . SER   M  23  ? 1.3930 0.7282 1.4688 -0.0043 -0.0591 -0.2692 10  SER   M OG  
21370 N  N   . VAL   M  24  ? 1.5226 0.5129 1.2243 -0.0091 -0.1890 -0.0599 11  VAL   M N   
21371 C  CA  . VAL   M  24  ? 1.5391 0.5312 1.1733 0.0067  -0.1874 -0.0458 11  VAL   M CA  
21372 C  C   . VAL   M  24  ? 1.5330 0.3981 1.1955 -0.0096 -0.1584 -0.0007 11  VAL   M C   
21373 O  O   . VAL   M  24  ? 1.5059 0.2781 1.2014 -0.0251 -0.1503 0.0506  11  VAL   M O   
21374 C  CB  . VAL   M  24  ? 1.5449 0.5506 1.1387 0.0100  -0.2263 -0.0336 11  VAL   M CB  
21375 C  CG1 . VAL   M  24  ? 1.5126 0.6328 1.1211 0.0222  -0.2196 -0.0415 11  VAL   M CG1 
21376 C  CG2 . VAL   M  24  ? 1.5505 0.6303 1.1395 0.0186  -0.2479 -0.0760 11  VAL   M CG2 
21377 N  N   . ILE   M  25  ? 1.6198 0.4181 1.1724 0.0183  -0.1278 0.0021  12  ILE   M N   
21378 C  CA  . ILE   M  25  ? 1.6496 0.4610 1.2407 0.0069  -0.1473 -0.0029 12  ILE   M CA  
21379 C  C   . ILE   M  25  ? 1.6701 0.3614 1.3103 0.0022  -0.1566 0.0306  12  ILE   M C   
21380 O  O   . ILE   M  25  ? 1.7566 0.1861 1.3706 -0.0031 -0.1880 0.0604  12  ILE   M O   
21381 C  CB  . ILE   M  25  ? 1.7525 0.4507 1.2253 0.0219  -0.1322 -0.0164 12  ILE   M CB  
21382 C  CG1 . ILE   M  25  ? 1.8000 0.5250 1.2228 0.0083  -0.0996 0.0079  12  ILE   M CG1 
21383 C  CG2 . ILE   M  25  ? 1.7842 0.4349 1.2318 0.0287  -0.1487 -0.0395 12  ILE   M CG2 
21384 C  CD1 . ILE   M  25  ? 1.8035 0.5524 1.2526 -0.0204 -0.0766 0.0074  12  ILE   M CD1 
21385 N  N   . SER   M  26  ? 1.6193 0.4218 1.3723 -0.0624 -0.1363 0.0588  13  SER   M N   
21386 C  CA  . SER   M  26  ? 1.5475 0.5640 1.3763 -0.0351 -0.1197 0.0811  13  SER   M CA  
21387 C  C   . SER   M  26  ? 1.5485 0.5259 1.3942 -0.0607 -0.1107 0.0964  13  SER   M C   
21388 O  O   . SER   M  26  ? 1.5878 0.6121 1.3547 -0.0864 -0.1217 0.0957  13  SER   M O   
21389 C  CB  . SER   M  26  ? 1.5573 0.6360 1.3724 0.0003  -0.1256 0.1841  13  SER   M CB  
21390 O  OG  . SER   M  26  ? 1.5422 0.8438 1.3721 0.0557  -0.1835 0.1060  13  SER   M OG  
21391 N  N   . MET   M  27  ? 1.5534 0.5951 1.4163 -0.0314 -0.1120 0.0940  14  MET   M N   
21392 C  CA  . MET   M  27  ? 1.5590 0.7083 1.4354 -0.0153 -0.1285 0.0986  14  MET   M CA  
21393 C  C   . MET   M  27  ? 1.5925 0.7423 1.4141 0.0073  -0.1235 0.1009  14  MET   M C   
21394 O  O   . MET   M  27  ? 1.7117 0.7103 1.4350 0.0110  -0.1148 0.0770  14  MET   M O   
21395 C  CB  . MET   M  27  ? 1.5034 0.7279 1.4937 -0.0342 -0.1051 0.0859  14  MET   M CB  
21396 C  CG  . MET   M  27  ? 1.4866 0.7554 1.5139 -0.0431 -0.0856 0.1506  14  MET   M CG  
21397 S  SD  . MET   M  27  ? 1.4418 0.7899 1.6039 -0.0711 -0.0990 0.1794  14  MET   M SD  
21398 C  CE  . MET   M  27  ? 1.4390 0.8118 1.6021 -0.0966 -0.0996 0.1938  14  MET   M CE  
21399 N  N   . LYS   M  28  ? 1.5696 0.7894 1.3961 0.0082  -0.1086 0.0868  15  LYS   M N   
21400 C  CA  . LYS   M  28  ? 1.5638 0.7905 1.3993 -0.0044 -0.0960 0.0583  15  LYS   M CA  
21401 C  C   . LYS   M  28  ? 1.5540 0.8482 1.4206 -0.0181 -0.0769 0.0413  15  LYS   M C   
21402 O  O   . LYS   M  28  ? 1.5523 0.9028 1.4539 -0.0257 -0.0845 -0.0467 15  LYS   M O   
21403 C  CB  . LYS   M  28  ? 1.5695 0.8093 1.3985 0.0101  -0.0781 0.0743  15  LYS   M CB  
21404 C  CG  . LYS   M  28  ? 1.5676 0.8156 1.3667 0.0045  -0.0713 0.0507  15  LYS   M CG  
21405 C  CD  . LYS   M  28  ? 1.5961 0.8261 1.3437 0.0000  -0.0427 0.0830  15  LYS   M CD  
21406 C  CE  . LYS   M  28  ? 1.6108 0.8267 1.2865 0.0111  -0.0624 0.0951  15  LYS   M CE  
21407 N  NZ  . LYS   M  28  ? 1.6452 0.8803 1.2952 0.0321  -0.0646 0.1253  15  LYS   M NZ  
21408 N  N   . TYR   M  29  ? 1.5979 0.7509 1.4627 -0.0219 -0.0994 0.0039  16  TYR   M N   
21409 C  CA  . TYR   M  29  ? 1.5815 0.7799 1.5386 0.0186  -0.0613 -0.0046 16  TYR   M CA  
21410 C  C   . TYR   M  29  ? 1.5505 0.7637 1.5207 -0.0012 -0.0325 0.0067  16  TYR   M C   
21411 O  O   . TYR   M  29  ? 1.4877 0.7840 1.4001 -0.0204 -0.0581 -0.0187 16  TYR   M O   
21412 C  CB  . TYR   M  29  ? 1.6265 0.8249 1.5733 0.0661  -0.0752 0.0275  16  TYR   M CB  
21413 C  CG  . TYR   M  29  ? 1.6513 0.7698 1.6449 0.0826  -0.0982 0.0372  16  TYR   M CG  
21414 C  CD1 . TYR   M  29  ? 1.6268 0.7550 1.6333 0.1344  -0.1284 0.0888  16  TYR   M CD1 
21415 C  CD2 . TYR   M  29  ? 1.6641 0.8356 1.7000 0.0973  -0.0533 0.0519  16  TYR   M CD2 
21416 C  CE1 . TYR   M  29  ? 1.6401 0.7761 1.6220 0.1250  -0.1393 0.0896  16  TYR   M CE1 
21417 C  CE2 . TYR   M  29  ? 1.6867 0.8831 1.6702 0.0850  -0.0872 0.0578  16  TYR   M CE2 
21418 C  CZ  . TYR   M  29  ? 1.6733 0.8509 1.6301 0.1070  -0.1062 0.0695  16  TYR   M CZ  
21419 O  OH  . TYR   M  29  ? 1.6541 0.8759 1.6459 0.0544  -0.1333 0.0930  16  TYR   M OH  
21420 N  N   . ASP   M  30  ? 1.5839 0.7943 1.6234 -0.0201 0.0184  0.0264  17  ASP   M N   
21421 C  CA  . ASP   M  30  ? 1.5878 0.8419 1.7200 -0.0003 0.0758  0.0668  17  ASP   M CA  
21422 C  C   . ASP   M  30  ? 1.6089 0.8092 1.7114 0.0106  0.1106  0.1393  17  ASP   M C   
21423 O  O   . ASP   M  30  ? 1.5943 0.8665 1.7786 0.0176  0.1871  0.2446  17  ASP   M O   
21424 C  CB  . ASP   M  30  ? 1.6034 0.8761 1.8010 -0.0128 0.1184  0.0550  17  ASP   M CB  
21425 C  CG  . ASP   M  30  ? 1.6032 0.9166 1.7894 -0.0203 0.1563  0.0674  17  ASP   M CG  
21426 O  OD1 . ASP   M  30  ? 1.5734 0.9773 1.8119 -0.0028 0.1522  0.0720  17  ASP   M OD1 
21427 O  OD2 . ASP   M  30  ? 1.5639 0.9525 1.8798 -0.0611 0.1763  0.0405  17  ASP   M OD2 
21428 N  N   . ASN   M  31  ? 1.6646 0.7639 1.6805 -0.0063 0.1295  0.1019  18  ASN   M N   
21429 C  CA  . ASN   M  31  ? 1.7351 0.7529 1.6199 0.0051  0.1773  0.0966  18  ASN   M CA  
21430 C  C   . ASN   M  31  ? 1.7292 0.7311 1.6149 0.0236  0.1623  0.1334  18  ASN   M C   
21431 O  O   . ASN   M  31  ? 1.7525 0.7816 1.6755 -0.0031 0.1721  0.0455  18  ASN   M O   
21432 C  CB  . ASN   M  31  ? 1.7735 0.7527 1.6304 -0.0081 0.2236  0.0406  18  ASN   M CB  
21433 C  CG  . ASN   M  31  ? 1.8000 0.8169 1.5889 -0.0294 0.2612  0.0028  18  ASN   M CG  
21434 O  OD1 . ASN   M  31  ? 1.9055 0.9924 1.5737 -0.0043 0.3141  -0.0180 18  ASN   M OD1 
21435 N  ND2 . ASN   M  31  ? 1.8046 0.8029 1.5874 -0.0418 0.2481  -0.0342 18  ASN   M ND2 
21436 N  N   . GLY   M  32  ? 1.7085 0.6433 1.5704 0.0166  0.1128  0.1778  19  GLY   M N   
21437 C  CA  . GLY   M  32  ? 1.6992 0.6358 1.5542 -0.0158 0.0411  0.1629  19  GLY   M CA  
21438 C  C   . GLY   M  32  ? 1.6689 0.6532 1.5442 0.0062  0.0002  0.1727  19  GLY   M C   
21439 O  O   . GLY   M  32  ? 1.6921 0.7148 1.5425 0.0193  -0.0475 0.1687  19  GLY   M O   
21440 N  N   . VAL   M  33  ? 1.7009 0.6333 1.4822 -0.0962 -0.0528 0.1075  20  VAL   M N   
21441 C  CA  . VAL   M  33  ? 1.7097 0.6602 1.4084 -0.1263 -0.0490 0.0723  20  VAL   M CA  
21442 C  C   . VAL   M  33  ? 1.7285 0.6606 1.4108 -0.1286 -0.0720 0.0436  20  VAL   M C   
21443 O  O   . VAL   M  33  ? 1.7553 0.6267 1.4562 -0.2233 -0.1034 0.0544  20  VAL   M O   
21444 C  CB  . VAL   M  33  ? 1.7293 0.6083 1.3342 -0.1245 -0.1057 0.0787  20  VAL   M CB  
21445 C  CG1 . VAL   M  33  ? 1.7310 0.6077 1.3403 -0.1112 -0.0968 0.1181  20  VAL   M CG1 
21446 C  CG2 . VAL   M  33  ? 1.7342 0.5841 1.3250 -0.1085 -0.1024 0.0867  20  VAL   M CG2 
21447 N  N   . ILE   M  34  ? 1.6963 0.7226 1.4179 -0.0836 -0.0055 0.0076  21  ILE   M N   
21448 C  CA  . ILE   M  34  ? 1.5920 0.8036 1.3704 -0.0738 0.0522  -0.0446 21  ILE   M CA  
21449 C  C   . ILE   M  34  ? 1.5505 0.7586 1.3681 -0.1150 0.0347  -0.0930 21  ILE   M C   
21450 O  O   . ILE   M  34  ? 1.4852 0.7925 1.3455 -0.1086 0.0845  -0.0870 21  ILE   M O   
21451 C  CB  . ILE   M  34  ? 1.6155 0.8456 1.3940 -0.0681 0.0709  -0.0017 21  ILE   M CB  
21452 C  CG1 . ILE   M  34  ? 1.6386 0.9640 1.4439 -0.0905 0.1188  0.0348  21  ILE   M CG1 
21453 C  CG2 . ILE   M  34  ? 1.6284 0.7987 1.3471 -0.0645 0.0739  -0.0202 21  ILE   M CG2 
21454 C  CD1 . ILE   M  34  ? 1.7205 0.9868 1.4523 -0.0693 0.1129  0.0874  21  ILE   M CD1 
21455 N  N   . ILE   M  35  ? 1.5367 0.6711 1.3137 -0.1227 0.0659  -0.1411 22  ILE   M N   
21456 C  CA  . ILE   M  35  ? 1.5326 0.5790 1.2812 -0.0852 0.0321  -0.1545 22  ILE   M CA  
21457 C  C   . ILE   M  35  ? 1.5495 0.5789 1.2563 -0.0896 0.0302  -0.1490 22  ILE   M C   
21458 O  O   . ILE   M  35  ? 1.5157 0.6634 1.2166 -0.0599 0.0652  -0.1232 22  ILE   M O   
21459 C  CB  . ILE   M  35  ? 1.5477 0.5126 1.2814 -0.0662 0.0204  -0.1845 22  ILE   M CB  
21460 C  CG1 . ILE   M  35  ? 1.5338 0.4679 1.2741 -0.0594 0.0058  -0.1799 22  ILE   M CG1 
21461 C  CG2 . ILE   M  35  ? 1.5722 0.5697 1.2709 -0.0935 0.0079  -0.2117 22  ILE   M CG2 
21462 C  CD1 . ILE   M  35  ? 1.5147 0.5063 1.2520 -0.0384 0.0206  -0.1769 22  ILE   M CD1 
21463 N  N   . ALA   M  36  ? 1.5501 0.4609 1.2897 -0.1160 -0.0030 -0.0909 23  ALA   M N   
21464 C  CA  . ALA   M  36  ? 1.5455 0.3999 1.3220 -0.1512 -0.0066 -0.0636 23  ALA   M CA  
21465 C  C   . ALA   M  36  ? 1.5331 0.3102 1.3245 -0.1133 -0.0257 -0.0567 23  ALA   M C   
21466 O  O   . ALA   M  36  ? 1.4665 0.2508 1.3373 -0.0625 -0.0083 -0.0735 23  ALA   M O   
21467 C  CB  . ALA   M  36  ? 1.5693 0.4577 1.3670 -0.1886 0.0021  -0.0289 23  ALA   M CB  
21468 N  N   . ALA   M  37  ? 1.5657 0.2778 1.2505 -0.0778 -0.0289 -0.0616 24  ALA   M N   
21469 C  CA  . ALA   M  37  ? 1.5755 0.3533 1.2386 -0.0339 -0.0363 -0.0355 24  ALA   M CA  
21470 C  C   . ALA   M  37  ? 1.5950 0.4828 1.2396 -0.0044 -0.0413 -0.0214 24  ALA   M C   
21471 O  O   . ALA   M  37  ? 1.5897 0.6119 1.1461 0.1289  -0.0200 0.0072  24  ALA   M O   
21472 C  CB  . ALA   M  37  ? 1.5960 0.3668 1.2510 -0.0243 -0.0229 -0.0173 24  ALA   M CB  
21473 N  N   . ASP   M  38  ? 1.5944 0.5318 1.2917 0.0207  -0.0287 -0.0370 25  ASP   M N   
21474 C  CA  . ASP   M  38  ? 1.6541 0.6621 1.2879 -0.0215 -0.0602 -0.0133 25  ASP   M CA  
21475 C  C   . ASP   M  38  ? 1.6978 0.6033 1.2863 -0.0333 -0.0603 0.0027  25  ASP   M C   
21476 O  O   . ASP   M  38  ? 1.6444 0.7272 1.3194 -0.1803 -0.0252 0.0558  25  ASP   M O   
21477 C  CB  . ASP   M  38  ? 1.7153 0.7543 1.3450 0.0802  -0.0275 -0.0650 25  ASP   M CB  
21478 C  CG  . ASP   M  38  ? 1.7732 0.9165 1.3675 0.1645  -0.0012 -0.0696 25  ASP   M CG  
21479 O  OD1 . ASP   M  38  ? 1.7302 0.8116 1.2886 0.1852  -0.1244 -0.1405 25  ASP   M OD1 
21480 O  OD2 . ASP   M  38  ? 1.9169 1.0150 1.3640 0.3073  0.1181  -0.1852 25  ASP   M OD2 
21481 N  N   . ASN   M  39  ? 1.6942 0.4419 1.2559 -0.0700 -0.0489 0.0442  26  ASN   M N   
21482 C  CA  . ASN   M  39  ? 1.6943 0.5009 1.2071 -0.0682 -0.1023 0.0509  26  ASN   M CA  
21483 C  C   . ASN   M  39  ? 1.7099 0.3880 1.1588 -0.0256 -0.1518 0.1110  26  ASN   M C   
21484 O  O   . ASN   M  39  ? 1.7578 0.4028 1.1240 -0.0406 -0.1713 0.2030  26  ASN   M O   
21485 C  CB  . ASN   M  39  ? 1.7236 0.6058 1.2264 -0.0905 -0.0734 0.0019  26  ASN   M CB  
21486 C  CG  . ASN   M  39  ? 1.7317 0.7235 1.3189 -0.1509 -0.0115 -0.1143 26  ASN   M CG  
21487 O  OD1 . ASN   M  39  ? 1.7062 0.7749 1.2979 -0.1412 -0.0120 -0.1478 26  ASN   M OD1 
21488 N  ND2 . ASN   M  39  ? 1.7915 0.6769 1.3181 -0.1977 -0.0356 -0.1127 26  ASN   M ND2 
21489 N  N   . LEU   M  40  ? 1.7030 0.3991 1.1436 -0.0115 -0.1834 0.1156  27  LEU   M N   
21490 C  CA  . LEU   M  40  ? 1.6763 0.5628 1.1578 0.0130  -0.2116 0.1030  27  LEU   M CA  
21491 C  C   . LEU   M  40  ? 1.6089 0.5700 1.1581 -0.0077 -0.2181 0.0833  27  LEU   M C   
21492 O  O   . LEU   M  40  ? 1.6552 0.6644 1.2071 0.0680  -0.2132 0.1236  27  LEU   M O   
21493 C  CB  . LEU   M  40  ? 1.6957 0.6030 1.2079 0.0247  -0.2058 0.0331  27  LEU   M CB  
21494 C  CG  . LEU   M  40  ? 1.6905 0.7040 1.2470 0.0549  -0.2253 0.0028  27  LEU   M CG  
21495 C  CD1 . LEU   M  40  ? 1.7126 0.7633 1.2535 0.0293  -0.2380 -0.0163 27  LEU   M CD1 
21496 C  CD2 . LEU   M  40  ? 1.7014 0.7082 1.2712 0.0555  -0.2223 -0.0062 27  LEU   M CD2 
21497 N  N   . GLY   M  41  ? 1.5943 0.6016 1.0351 0.0403  -0.2816 0.1047  28  GLY   M N   
21498 C  CA  . GLY   M  41  ? 1.5854 0.6770 1.0353 0.0417  -0.2823 0.1158  28  GLY   M CA  
21499 C  C   . GLY   M  41  ? 1.5907 0.6995 1.0185 0.0595  -0.2999 0.1327  28  GLY   M C   
21500 O  O   . GLY   M  41  ? 1.7045 0.8744 1.0260 0.1035  -0.3704 0.2404  28  GLY   M O   
21501 N  N   . SER   M  42  ? 1.5561 0.6558 1.0855 -0.0011 -0.2392 0.0957  29  SER   M N   
21502 C  CA  . SER   M  42  ? 1.5572 0.5550 1.1346 -0.0272 -0.2185 0.1410  29  SER   M CA  
21503 C  C   . SER   M  42  ? 1.4532 0.6534 1.1771 0.0429  -0.1918 0.0722  29  SER   M C   
21504 O  O   . SER   M  42  ? 1.5419 0.6339 1.2368 -0.0377 -0.1389 0.0801  29  SER   M O   
21505 C  CB  . SER   M  42  ? 1.5485 0.4141 1.1648 -0.0629 -0.1440 0.1571  29  SER   M CB  
21506 O  OG  . SER   M  42  ? 1.5964 0.3362 1.1579 -0.1006 -0.1531 0.1589  29  SER   M OG  
21507 N  N   . TYR   M  43  ? 1.4855 0.5870 1.0878 0.0547  -0.2325 0.1643  30  TYR   M N   
21508 C  CA  . TYR   M  43  ? 1.4619 0.5914 1.1386 0.0833  -0.2244 0.1686  30  TYR   M CA  
21509 C  C   . TYR   M  43  ? 1.4376 0.5838 1.1610 0.0859  -0.2263 0.1725  30  TYR   M C   
21510 O  O   . TYR   M  43  ? 1.4224 0.5796 1.2089 0.0837  -0.1784 0.2177  30  TYR   M O   
21511 C  CB  . TYR   M  43  ? 1.4901 0.5930 1.1280 0.0632  -0.2238 0.1709  30  TYR   M CB  
21512 C  CG  . TYR   M  43  ? 1.4991 0.6425 1.1685 0.0596  -0.1960 0.1393  30  TYR   M CG  
21513 C  CD1 . TYR   M  43  ? 1.5016 0.6600 1.2044 0.0399  -0.1592 0.1374  30  TYR   M CD1 
21514 C  CD2 . TYR   M  43  ? 1.5152 0.5908 1.1498 0.0478  -0.2022 0.1367  30  TYR   M CD2 
21515 C  CE1 . TYR   M  43  ? 1.4998 0.7459 1.2057 0.0333  -0.1485 0.1167  30  TYR   M CE1 
21516 C  CE2 . TYR   M  43  ? 1.4949 0.6485 1.1519 0.0468  -0.2119 0.1265  30  TYR   M CE2 
21517 C  CZ  . TYR   M  43  ? 1.4731 0.6891 1.1638 0.0009  -0.1666 0.1425  30  TYR   M CZ  
21518 O  OH  . TYR   M  43  ? 1.4484 0.8697 1.1389 -0.0078 -0.1741 0.1142  30  TYR   M OH  
21519 N  N   . GLY   M  44  ? 1.4296 0.5547 1.1835 0.0768  -0.2322 0.1397  31  GLY   M N   
21520 C  CA  . GLY   M  44  ? 1.4468 0.5535 1.2025 0.0567  -0.2485 0.1281  31  GLY   M CA  
21521 C  C   . GLY   M  44  ? 1.5107 0.5468 1.1863 0.0257  -0.2778 0.1197  31  GLY   M C   
21522 O  O   . GLY   M  44  ? 1.5189 0.4701 1.1728 0.0704  -0.2973 0.0866  31  GLY   M O   
21523 N  N   . SER   M  45  ? 1.5378 0.5687 1.2166 0.0525  -0.3070 0.0950  32  SER   M N   
21524 C  CA  . SER   M  45  ? 1.5850 0.5284 1.2520 0.0754  -0.2694 0.0840  32  SER   M CA  
21525 C  C   . SER   M  45  ? 1.6428 0.4970 1.2198 0.0426  -0.2025 0.1229  32  SER   M C   
21526 O  O   . SER   M  45  ? 1.6797 0.3908 1.1754 0.0806  -0.1873 0.0887  32  SER   M O   
21527 C  CB  . SER   M  45  ? 1.5787 0.5730 1.3273 0.1134  -0.2647 0.0684  32  SER   M CB  
21528 O  OG  . SER   M  45  ? 1.5799 0.6493 1.4435 0.1504  -0.2718 0.0557  32  SER   M OG  
21529 N  N   . LEU   M  46  ? 1.6840 0.5540 1.2265 0.0042  -0.2019 0.1046  33  LEU   M N   
21530 C  CA  . LEU   M  46  ? 1.7089 0.5452 1.2139 -0.0002 -0.2068 0.1204  33  LEU   M CA  
21531 C  C   . LEU   M  46  ? 1.6890 0.5648 1.2405 -0.0507 -0.1765 0.0344  33  LEU   M C   
21532 O  O   . LEU   M  46  ? 1.6708 0.4743 1.2871 -0.0982 -0.1419 -0.0177 33  LEU   M O   
21533 C  CB  . LEU   M  46  ? 1.7360 0.5396 1.1761 -0.0114 -0.2444 0.1074  33  LEU   M CB  
21534 C  CG  . LEU   M  46  ? 1.8299 0.5927 1.1321 0.0128  -0.2388 0.1235  33  LEU   M CG  
21535 C  CD1 . LEU   M  46  ? 1.8825 0.5982 1.1586 0.0000  -0.2217 0.1431  33  LEU   M CD1 
21536 C  CD2 . LEU   M  46  ? 1.8246 0.6215 1.1350 0.0067  -0.2300 0.1196  33  LEU   M CD2 
21537 N  N   . LEU   M  47  ? 1.6954 0.5239 1.2178 -0.0225 -0.2123 0.0754  34  LEU   M N   
21538 C  CA  . LEU   M  47  ? 1.6903 0.6275 1.2146 -0.0174 -0.2179 0.0385  34  LEU   M CA  
21539 C  C   . LEU   M  47  ? 1.6855 0.7187 1.2324 -0.0788 -0.2595 0.0429  34  LEU   M C   
21540 O  O   . LEU   M  47  ? 1.6664 0.7415 1.2485 -0.1021 -0.2739 0.0706  34  LEU   M O   
21541 C  CB  . LEU   M  47  ? 1.6957 0.6611 1.2146 0.0148  -0.1986 0.0791  34  LEU   M CB  
21542 C  CG  . LEU   M  47  ? 1.7016 0.6283 1.2766 0.0179  -0.1699 0.0896  34  LEU   M CG  
21543 C  CD1 . LEU   M  47  ? 1.7125 0.6619 1.2610 0.0337  -0.1662 0.1225  34  LEU   M CD1 
21544 C  CD2 . LEU   M  47  ? 1.7149 0.6961 1.3108 0.0713  -0.1713 0.1107  34  LEU   M CD2 
21545 N  N   . ARG   M  48  ? 1.6738 0.7313 1.2006 -0.0896 -0.2686 0.0391  35  ARG   M N   
21546 C  CA  . ARG   M  48  ? 1.6870 0.7821 1.2071 -0.0551 -0.3250 -0.0022 35  ARG   M CA  
21547 C  C   . ARG   M  48  ? 1.6998 0.7591 1.1420 -0.0828 -0.3324 0.0209  35  ARG   M C   
21548 O  O   . ARG   M  48  ? 1.7917 0.8346 1.0919 -0.1394 -0.3039 -0.0602 35  ARG   M O   
21549 C  CB  . ARG   M  48  ? 1.6516 0.7831 1.2619 -0.0565 -0.2957 -0.0127 35  ARG   M CB  
21550 C  CG  . ARG   M  48  ? 1.6735 0.8292 1.3548 -0.0720 -0.2996 -0.0619 35  ARG   M CG  
21551 C  CD  . ARG   M  48  ? 1.6819 0.8616 1.4623 -0.0123 -0.2687 -0.0543 35  ARG   M CD  
21552 N  NE  . ARG   M  48  ? 1.7508 0.8834 1.5197 -0.0563 -0.2096 -0.1199 35  ARG   M NE  
21553 C  CZ  . ARG   M  48  ? 1.7639 0.8419 1.4797 -0.0877 -0.1780 -0.0534 35  ARG   M CZ  
21554 N  NH1 . ARG   M  48  ? 1.8283 0.8974 1.3841 -0.0441 -0.1415 -0.0023 35  ARG   M NH1 
21555 N  NH2 . ARG   M  48  ? 1.7836 0.7719 1.4271 -0.0802 -0.1395 -0.0687 35  ARG   M NH2 
21556 N  N   . PHE   M  49  ? 1.6859 0.6644 1.1036 -0.1078 -0.3146 0.0062  36  PHE   M N   
21557 C  CA  . PHE   M  49  ? 1.6984 0.5725 1.1481 -0.1480 -0.3165 0.0045  36  PHE   M CA  
21558 C  C   . PHE   M  49  ? 1.7234 0.5727 1.2105 -0.1090 -0.2460 -0.0005 36  PHE   M C   
21559 O  O   . PHE   M  49  ? 1.7249 0.4271 1.2253 -0.0955 -0.2121 -0.0340 36  PHE   M O   
21560 C  CB  . PHE   M  49  ? 1.6706 0.5738 1.1377 -0.2193 -0.2969 0.0098  36  PHE   M CB  
21561 C  CG  . PHE   M  49  ? 1.6710 0.5333 1.1575 -0.2275 -0.3081 0.0452  36  PHE   M CG  
21562 C  CD1 . PHE   M  49  ? 1.6720 0.5192 1.1730 -0.2540 -0.3206 0.0699  36  PHE   M CD1 
21563 C  CD2 . PHE   M  49  ? 1.6637 0.4988 1.1817 -0.2542 -0.2681 0.0524  36  PHE   M CD2 
21564 C  CE1 . PHE   M  49  ? 1.6733 0.5055 1.1929 -0.2875 -0.3527 0.0764  36  PHE   M CE1 
21565 C  CE2 . PHE   M  49  ? 1.6467 0.4708 1.2007 -0.2861 -0.3138 0.0490  36  PHE   M CE2 
21566 C  CZ  . PHE   M  49  ? 1.6354 0.4910 1.2047 -0.3038 -0.3196 0.0701  36  PHE   M CZ  
21567 N  N   . ASN   M  50  ? 1.7748 0.6433 1.2048 -0.1249 -0.2752 -0.0312 37  ASN   M N   
21568 C  CA  . ASN   M  50  ? 1.8071 0.7754 1.3148 -0.1843 -0.2442 -0.0542 37  ASN   M CA  
21569 C  C   . ASN   M  50  ? 1.8165 0.8353 1.2659 -0.1853 -0.2458 -0.0971 37  ASN   M C   
21570 O  O   . ASN   M  50  ? 1.8298 1.0671 1.2551 -0.1525 -0.1888 -0.1310 37  ASN   M O   
21571 C  CB  . ASN   M  50  ? 1.8825 0.8963 1.3767 -0.1724 -0.2818 0.0117  37  ASN   M CB  
21572 C  CG  . ASN   M  50  ? 1.9960 0.9544 1.4744 -0.2238 -0.2553 -0.0564 37  ASN   M CG  
21573 O  OD1 . ASN   M  50  ? 1.9815 1.0306 1.5160 -0.2045 -0.2593 -0.0326 37  ASN   M OD1 
21574 N  ND2 . ASN   M  50  ? 1.9965 1.0649 1.4953 -0.2505 -0.2553 -0.0337 37  ASN   M ND2 
21575 N  N   . GLY   M  51  ? 1.8009 0.8089 1.2078 -0.1551 -0.2644 -0.1299 38  GLY   M N   
21576 C  CA  . GLY   M  51  ? 1.8332 0.8174 1.1428 -0.1193 -0.2710 -0.1041 38  GLY   M CA  
21577 C  C   . GLY   M  51  ? 1.8413 0.8937 1.1048 -0.0756 -0.2803 -0.1094 38  GLY   M C   
21578 O  O   . GLY   M  51  ? 1.9033 0.9277 1.1180 0.0147  -0.2556 -0.1359 38  GLY   M O   
21579 N  N   . VAL   M  52  ? 1.7913 0.6514 1.1468 -0.0695 -0.2822 -0.1160 39  VAL   M N   
21580 C  CA  . VAL   M  52  ? 1.7464 0.6177 1.1412 -0.0284 -0.2567 -0.1261 39  VAL   M CA  
21581 C  C   . VAL   M  52  ? 1.7294 0.5964 1.1232 -0.0720 -0.2249 -0.0953 39  VAL   M C   
21582 O  O   . VAL   M  52  ? 1.8069 0.4563 1.2083 -0.0274 -0.1756 -0.0146 39  VAL   M O   
21583 C  CB  . VAL   M  52  ? 1.7297 0.5673 1.1594 0.0224  -0.2548 -0.1087 39  VAL   M CB  
21584 C  CG1 . VAL   M  52  ? 1.7312 0.5919 1.1696 0.0676  -0.2621 -0.1127 39  VAL   M CG1 
21585 C  CG2 . VAL   M  52  ? 1.7340 0.5462 1.1641 0.0241  -0.2732 -0.1139 39  VAL   M CG2 
21586 N  N   . GLU   M  53  ? 1.6921 0.6566 1.0844 -0.0047 -0.1888 -0.1057 40  GLU   M N   
21587 C  CA  . GLU   M  53  ? 1.6806 0.7274 1.0984 -0.0044 -0.1724 -0.0560 40  GLU   M CA  
21588 C  C   . GLU   M  53  ? 1.6612 0.7031 1.1098 0.0584  -0.1581 -0.0462 40  GLU   M C   
21589 O  O   . GLU   M  53  ? 1.6661 0.6960 1.1136 0.1259  -0.1268 0.0038  40  GLU   M O   
21590 C  CB  . GLU   M  53  ? 1.6987 0.7635 1.0876 0.0238  -0.1483 -0.0495 40  GLU   M CB  
21591 C  CG  . GLU   M  53  ? 1.6822 0.8167 1.1209 -0.0033 -0.1316 -0.0213 40  GLU   M CG  
21592 C  CD  . GLU   M  53  ? 1.7472 0.8127 1.1846 -0.0174 -0.1236 0.0260  40  GLU   M CD  
21593 O  OE1 . GLU   M  53  ? 1.7541 0.9804 1.1166 -0.0031 -0.0971 0.0188  40  GLU   M OE1 
21594 O  OE2 . GLU   M  53  ? 1.8020 0.8400 1.2060 -0.0725 -0.1627 0.0712  40  GLU   M OE2 
21595 N  N   . ARG   M  54  ? 1.6325 0.7721 1.0933 0.0309  -0.1534 -0.0251 41  ARG   M N   
21596 C  CA  . ARG   M  54  ? 1.5888 0.7228 1.1044 0.0267  -0.1728 0.0154  41  ARG   M CA  
21597 C  C   . ARG   M  54  ? 1.5774 0.6665 1.1106 0.0195  -0.1360 0.0186  41  ARG   M C   
21598 O  O   . ARG   M  54  ? 1.6201 0.6658 1.1422 -0.0220 -0.1809 0.0298  41  ARG   M O   
21599 C  CB  . ARG   M  54  ? 1.5491 0.7194 1.1339 0.0008  -0.1939 0.0013  41  ARG   M CB  
21600 C  CG  . ARG   M  54  ? 1.5639 0.7086 1.1631 -0.0002 -0.2204 0.0173  41  ARG   M CG  
21601 C  CD  . ARG   M  54  ? 1.5522 0.6882 1.1862 -0.0006 -0.2224 0.0268  41  ARG   M CD  
21602 N  NE  . ARG   M  54  ? 1.5353 0.7281 1.2165 -0.0236 -0.2409 0.0549  41  ARG   M NE  
21603 C  CZ  . ARG   M  54  ? 1.5002 0.6714 1.2496 -0.0031 -0.2266 0.0326  41  ARG   M CZ  
21604 N  NH1 . ARG   M  54  ? 1.4082 0.6618 1.2377 0.0118  -0.2251 0.0114  41  ARG   M NH1 
21605 N  NH2 . ARG   M  54  ? 1.5622 0.6860 1.2798 -0.0136 -0.1873 0.0465  41  ARG   M NH2 
21606 N  N   . LEU   M  55  ? 1.5641 0.6195 1.0615 0.0394  -0.1698 0.0285  42  LEU   M N   
21607 C  CA  . LEU   M  55  ? 1.5805 0.6669 1.1102 0.0663  -0.1757 0.0168  42  LEU   M CA  
21608 C  C   . LEU   M  55  ? 1.5691 0.7003 1.1359 0.0335  -0.1855 0.0072  42  LEU   M C   
21609 O  O   . LEU   M  55  ? 1.5422 0.8096 1.1055 0.0502  -0.1852 0.1361  42  LEU   M O   
21610 C  CB  . LEU   M  55  ? 1.6310 0.5896 1.0778 0.0593  -0.1755 -0.0120 42  LEU   M CB  
21611 C  CG  . LEU   M  55  ? 1.7063 0.5575 1.1182 0.1081  -0.1588 -0.0292 42  LEU   M CG  
21612 C  CD1 . LEU   M  55  ? 1.7595 0.5323 1.0648 0.0931  -0.1576 -0.0479 42  LEU   M CD1 
21613 C  CD2 . LEU   M  55  ? 1.7137 0.5467 1.1333 0.1671  -0.1695 -0.0251 42  LEU   M CD2 
21614 N  N   . ILE   M  56  ? 1.5957 0.6988 1.1939 0.0442  -0.1651 0.0271  43  ILE   M N   
21615 C  CA  . ILE   M  56  ? 1.5890 0.7031 1.2417 0.0680  -0.1656 -0.0139 43  ILE   M CA  
21616 C  C   . ILE   M  56  ? 1.6569 0.5719 1.2740 0.1040  -0.1023 -0.0290 43  ILE   M C   
21617 O  O   . ILE   M  56  ? 1.5926 0.3908 1.2513 0.1754  -0.0507 0.0026  43  ILE   M O   
21618 C  CB  . ILE   M  56  ? 1.6026 0.7443 1.1817 0.0045  -0.2087 -0.0286 43  ILE   M CB  
21619 C  CG1 . ILE   M  56  ? 1.6463 0.7756 1.1740 0.0299  -0.1829 0.0134  43  ILE   M CG1 
21620 C  CG2 . ILE   M  56  ? 1.5767 0.7584 1.2152 -0.0175 -0.2255 -0.0542 43  ILE   M CG2 
21621 C  CD1 . ILE   M  56  ? 1.6302 0.8208 1.2491 0.0714  -0.1598 0.0617  43  ILE   M CD1 
21622 N  N   . PRO   M  57  ? 1.6769 0.6146 1.3049 0.1337  -0.0712 -0.0342 44  PRO   M N   
21623 C  CA  . PRO   M  57  ? 1.6758 0.6795 1.3292 0.1526  -0.0570 -0.0164 44  PRO   M CA  
21624 C  C   . PRO   M  57  ? 1.6556 0.6745 1.4013 0.1203  -0.0733 -0.0276 44  PRO   M C   
21625 O  O   . PRO   M  57  ? 1.7036 0.4516 1.4209 0.1102  -0.0292 -0.1099 44  PRO   M O   
21626 C  CB  . PRO   M  57  ? 1.7139 0.7265 1.3411 0.1544  -0.0265 -0.0161 44  PRO   M CB  
21627 C  CG  . PRO   M  57  ? 1.6999 0.6834 1.3166 0.1230  -0.0367 -0.0270 44  PRO   M CG  
21628 C  CD  . PRO   M  57  ? 1.6566 0.6699 1.3029 0.1356  -0.0749 -0.0337 44  PRO   M CD  
21629 N  N   . VAL   M  58  ? 1.6998 0.6645 1.4404 0.1314  -0.0783 0.0196  45  VAL   M N   
21630 C  CA  . VAL   M  58  ? 1.6978 0.6755 1.3750 0.1295  -0.0880 0.0355  45  VAL   M CA  
21631 C  C   . VAL   M  58  ? 1.7373 0.6533 1.3657 0.1356  -0.0550 0.0413  45  VAL   M C   
21632 O  O   . VAL   M  58  ? 1.7428 0.5304 1.3147 0.1204  -0.0358 0.0411  45  VAL   M O   
21633 C  CB  . VAL   M  58  ? 1.6327 0.6626 1.3806 0.1523  -0.0748 0.0786  45  VAL   M CB  
21634 C  CG1 . VAL   M  58  ? 1.6567 0.7096 1.3982 0.1108  -0.0601 0.1304  45  VAL   M CG1 
21635 C  CG2 . VAL   M  58  ? 1.5822 0.6570 1.3287 0.1477  -0.1106 0.0972  45  VAL   M CG2 
21636 N  N   . GLY   M  59  ? 1.7885 0.7622 1.3391 0.1636  -0.0116 0.0031  46  GLY   M N   
21637 C  CA  . GLY   M  59  ? 1.7704 0.8184 1.4466 0.1384  0.0243  -0.0199 46  GLY   M CA  
21638 C  C   . GLY   M  59  ? 1.7334 0.8419 1.5354 0.0838  0.0478  -0.0519 46  GLY   M C   
21639 O  O   . GLY   M  59  ? 1.8050 0.6081 1.6079 0.0111  0.0585  -0.1290 46  GLY   M O   
21640 N  N   . ASP   M  60  ? 1.7365 0.8909 1.6177 0.0770  0.0922  -0.0860 47  ASP   M N   
21641 C  CA  . ASP   M  60  ? 1.7705 0.8768 1.6604 0.0422  0.1159  -0.1137 47  ASP   M CA  
21642 C  C   . ASP   M  60  ? 1.7411 0.7236 1.5879 0.0545  0.1663  -0.0700 47  ASP   M C   
21643 O  O   . ASP   M  60  ? 1.7501 0.7384 1.7553 0.0523  0.2270  -0.0678 47  ASP   M O   
21644 C  CB  . ASP   M  60  ? 1.8703 1.1465 1.6909 0.0455  0.2230  -0.1592 47  ASP   M CB  
21645 C  CG  . ASP   M  60  ? 1.8970 1.3477 1.7820 0.0975  0.2065  -0.0775 47  ASP   M CG  
21646 O  OD1 . ASP   M  60  ? 2.0398 1.5703 1.8004 0.0570  0.2285  -0.0355 47  ASP   M OD1 
21647 O  OD2 . ASP   M  60  ? 1.9433 1.7342 1.7714 0.0419  0.3409  -0.0410 47  ASP   M OD2 
21648 N  N   . ASN   M  61  ? 1.6565 0.6376 1.5461 0.0262  0.0737  -0.0461 48  ASN   M N   
21649 C  CA  . ASN   M  61  ? 1.6634 0.6628 1.4352 0.0007  0.1008  -0.0223 48  ASN   M CA  
21650 C  C   . ASN   M  61  ? 1.6263 0.6253 1.3018 -0.0803 0.0008  -0.0452 48  ASN   M C   
21651 O  O   . ASN   M  61  ? 1.5754 0.6484 1.3347 -0.1607 0.0026  0.0130  48  ASN   M O   
21652 C  CB  . ASN   M  61  ? 1.6569 0.7168 1.4683 0.0246  0.0825  -0.0222 48  ASN   M CB  
21653 C  CG  . ASN   M  61  ? 1.6556 0.7776 1.4786 0.0204  0.1201  -0.0310 48  ASN   M CG  
21654 O  OD1 . ASN   M  61  ? 1.6647 0.9058 1.5029 0.0467  0.0473  -0.0532 48  ASN   M OD1 
21655 N  ND2 . ASN   M  61  ? 1.6514 0.7506 1.4535 0.0859  0.1081  -0.0508 48  ASN   M ND2 
21656 N  N   . THR   M  62  ? 1.6471 0.6198 1.2564 -0.0409 -0.0333 -0.1143 49  THR   M N   
21657 C  CA  . THR   M  62  ? 1.7128 0.5476 1.2888 -0.0330 -0.0767 -0.1753 49  THR   M CA  
21658 C  C   . THR   M  62  ? 1.7376 0.5163 1.2881 -0.0125 -0.0837 -0.2253 49  THR   M C   
21659 O  O   . THR   M  62  ? 1.8270 0.3674 1.4782 -0.0807 -0.0431 -0.3987 49  THR   M O   
21660 C  CB  . THR   M  62  ? 1.7370 0.4555 1.3017 -0.0197 -0.0776 -0.1909 49  THR   M CB  
21661 O  OG1 . THR   M  62  ? 1.7630 0.4348 1.4095 -0.0470 -0.0688 -0.1109 49  THR   M OG1 
21662 C  CG2 . THR   M  62  ? 1.7069 0.4834 1.2944 0.0109  -0.0844 -0.1818 49  THR   M CG2 
21663 N  N   . VAL   M  63  ? 1.7280 0.5023 1.2065 -0.0530 -0.1113 -0.2154 50  VAL   M N   
21664 C  CA  . VAL   M  63  ? 1.7135 0.4728 1.2134 -0.0564 -0.0921 -0.2424 50  VAL   M CA  
21665 C  C   . VAL   M  63  ? 1.5842 0.3861 1.1872 -0.0883 -0.1105 -0.2033 50  VAL   M C   
21666 O  O   . VAL   M  63  ? 1.5317 0.4100 1.2757 -0.1535 -0.0890 -0.2055 50  VAL   M O   
21667 C  CB  . VAL   M  63  ? 1.7293 0.4254 1.2778 -0.0473 -0.0732 -0.2541 50  VAL   M CB  
21668 C  CG1 . VAL   M  63  ? 1.7313 0.3329 1.3009 -0.0768 -0.0920 -0.2976 50  VAL   M CG1 
21669 C  CG2 . VAL   M  63  ? 1.7506 0.6046 1.2893 -0.0113 -0.0016 -0.2324 50  VAL   M CG2 
21670 N  N   . VAL   M  64  ? 1.5623 0.3871 1.1318 -0.0701 -0.1385 -0.1755 51  VAL   M N   
21671 C  CA  . VAL   M  64  ? 1.5475 0.4390 1.1341 -0.0829 -0.1450 -0.1861 51  VAL   M CA  
21672 C  C   . VAL   M  64  ? 1.5670 0.4710 1.1311 -0.0935 -0.1891 -0.1527 51  VAL   M C   
21673 O  O   . VAL   M  64  ? 1.5759 0.3573 1.1851 -0.2398 -0.1889 -0.2555 51  VAL   M O   
21674 C  CB  . VAL   M  64  ? 1.4869 0.4596 1.1525 -0.0817 -0.1759 -0.1823 51  VAL   M CB  
21675 C  CG1 . VAL   M  64  ? 1.4818 0.4653 1.1700 -0.0928 -0.1649 -0.1882 51  VAL   M CG1 
21676 C  CG2 . VAL   M  64  ? 1.4874 0.4669 1.1823 -0.0585 -0.1466 -0.1873 51  VAL   M CG2 
21677 N  N   . GLY   M  65  ? 1.6139 0.4554 1.1891 -0.0923 -0.1406 -0.1655 52  GLY   M N   
21678 C  CA  . GLY   M  65  ? 1.6071 0.4705 1.2306 -0.0879 -0.1491 -0.1211 52  GLY   M CA  
21679 C  C   . GLY   M  65  ? 1.5305 0.4350 1.2727 -0.0635 -0.1566 -0.0802 52  GLY   M C   
21680 O  O   . GLY   M  65  ? 1.4766 0.4077 1.2766 -0.1241 -0.1664 -0.1149 52  GLY   M O   
21681 N  N   . ILE   M  66  ? 1.5562 0.4342 1.2277 -0.0327 -0.1735 -0.0266 53  ILE   M N   
21682 C  CA  . ILE   M  66  ? 1.5960 0.4676 1.1751 0.0125  -0.1799 -0.0195 53  ILE   M CA  
21683 C  C   . ILE   M  66  ? 1.6367 0.4776 1.1014 0.0301  -0.1617 -0.0213 53  ILE   M C   
21684 O  O   . ILE   M  66  ? 1.6878 0.4847 1.0739 0.0057  -0.1607 -0.0355 53  ILE   M O   
21685 C  CB  . ILE   M  66  ? 1.5595 0.5037 1.2026 0.0114  -0.2271 0.0027  53  ILE   M CB  
21686 C  CG1 . ILE   M  66  ? 1.5628 0.4931 1.2254 0.0082  -0.2448 -0.0518 53  ILE   M CG1 
21687 C  CG2 . ILE   M  66  ? 1.5215 0.4917 1.1981 0.0598  -0.2509 0.0039  53  ILE   M CG2 
21688 C  CD1 . ILE   M  66  ? 1.6014 0.4213 1.1881 0.0492  -0.2754 -0.1333 53  ILE   M CD1 
21689 N  N   . SER   M  67  ? 1.6313 0.4883 1.0675 0.0578  -0.1607 0.0011  54  SER   M N   
21690 C  CA  . SER   M  67  ? 1.5980 0.4751 1.0194 0.0527  -0.1593 0.0530  54  SER   M CA  
21691 C  C   . SER   M  67  ? 1.5304 0.3840 1.0186 0.0287  -0.1791 0.0041  54  SER   M C   
21692 O  O   . SER   M  67  ? 1.4536 0.3417 0.9948 -0.0525 -0.1236 -0.0284 54  SER   M O   
21693 C  CB  . SER   M  67  ? 1.5745 0.4858 1.0038 0.0778  -0.2087 0.0617  54  SER   M CB  
21694 O  OG  . SER   M  67  ? 1.5800 0.5292 1.0124 0.0799  -0.2187 0.0700  54  SER   M OG  
21695 N  N   . GLY   M  68  ? 1.5199 0.3195 0.9839 0.0032  -0.1856 0.0701  55  GLY   M N   
21696 C  CA  . GLY   M  68  ? 1.5344 0.3274 1.0009 0.0109  -0.1802 0.0633  55  GLY   M CA  
21697 C  C   . GLY   M  68  ? 1.5766 0.2921 1.0702 -0.0131 -0.1926 0.0524  55  GLY   M C   
21698 O  O   . GLY   M  68  ? 1.6471 0.3596 1.0731 -0.0804 -0.1812 0.0885  55  GLY   M O   
21699 N  N   . ASP   M  69  ? 1.5979 0.2728 1.1001 0.0268  -0.1577 0.0830  56  ASP   M N   
21700 C  CA  . ASP   M  69  ? 1.5647 0.3965 1.1649 0.0210  -0.1409 0.0923  56  ASP   M CA  
21701 C  C   . ASP   M  69  ? 1.6051 0.4323 1.1474 0.0327  -0.1632 0.0833  56  ASP   M C   
21702 O  O   . ASP   M  69  ? 1.5741 0.4756 1.1460 0.0428  -0.1831 0.0473  56  ASP   M O   
21703 C  CB  . ASP   M  69  ? 1.5945 0.4572 1.1911 0.0610  -0.0624 0.0787  56  ASP   M CB  
21704 C  CG  . ASP   M  69  ? 1.5695 0.4882 1.3026 0.0565  -0.0230 0.0765  56  ASP   M CG  
21705 O  OD1 . ASP   M  69  ? 1.6902 0.4681 1.3308 0.1419  -0.0036 0.1161  56  ASP   M OD1 
21706 O  OD2 . ASP   M  69  ? 1.6439 0.5922 1.4162 -0.1093 0.0076  -0.0246 56  ASP   M OD2 
21707 N  N   . ILE   M  70  ? 1.6697 0.4770 1.1119 0.0094  -0.1660 0.0381  57  ILE   M N   
21708 C  CA  . ILE   M  70  ? 1.6490 0.5040 1.1411 -0.0117 -0.1689 0.0032  57  ILE   M CA  
21709 C  C   . ILE   M  70  ? 1.6140 0.4881 1.0986 0.0185  -0.1776 0.0245  57  ILE   M C   
21710 O  O   . ILE   M  70  ? 1.6551 0.5433 1.1289 0.0939  -0.2295 0.0066  57  ILE   M O   
21711 C  CB  . ILE   M  70  ? 1.6294 0.4869 1.1736 -0.0181 -0.1815 0.0081  57  ILE   M CB  
21712 C  CG1 . ILE   M  70  ? 1.6081 0.4727 1.1903 -0.0043 -0.1602 0.0010  57  ILE   M CG1 
21713 C  CG2 . ILE   M  70  ? 1.6672 0.5403 1.1898 -0.0150 -0.1564 -0.0199 57  ILE   M CG2 
21714 C  CD1 . ILE   M  70  ? 1.6162 0.4825 1.1916 -0.0189 -0.1208 -0.0061 57  ILE   M CD1 
21715 N  N   . SER   M  71  ? 1.6294 0.4431 1.0693 -0.0292 -0.1689 0.0488  58  SER   M N   
21716 C  CA  . SER   M  71  ? 1.6621 0.3617 1.1033 0.0347  -0.1428 0.0432  58  SER   M CA  
21717 C  C   . SER   M  71  ? 1.5738 0.4786 1.0939 -0.0101 -0.1686 0.0711  58  SER   M C   
21718 O  O   . SER   M  71  ? 1.5913 0.5247 1.1092 0.1155  -0.1872 0.0361  58  SER   M O   
21719 C  CB  . SER   M  71  ? 1.6865 0.2247 1.1119 0.0492  -0.1221 0.0612  58  SER   M CB  
21720 O  OG  . SER   M  71  ? 1.7303 0.1760 1.1029 0.0350  -0.0883 0.0858  58  SER   M OG  
21721 N  N   . ASP   M  72  ? 1.5397 0.4043 1.1365 -0.0501 -0.1482 0.0677  59  ASP   M N   
21722 C  CA  . ASP   M  72  ? 1.5468 0.4543 1.1927 -0.0349 -0.1610 0.0844  59  ASP   M CA  
21723 C  C   . ASP   M  72  ? 1.5676 0.5380 1.2048 -0.0961 -0.1267 0.0437  59  ASP   M C   
21724 O  O   . ASP   M  72  ? 1.4997 0.6077 1.3174 -0.0513 -0.1165 0.0036  59  ASP   M O   
21725 C  CB  . ASP   M  72  ? 1.6070 0.4629 1.1677 -0.0111 -0.1882 0.1127  59  ASP   M CB  
21726 C  CG  . ASP   M  72  ? 1.5960 0.4916 1.1828 -0.0153 -0.2036 0.1672  59  ASP   M CG  
21727 O  OD1 . ASP   M  72  ? 1.5679 0.5569 1.1819 -0.0409 -0.2523 0.1699  59  ASP   M OD1 
21728 O  OD2 . ASP   M  72  ? 1.7312 0.4657 1.1059 0.0487  -0.2832 0.2190  59  ASP   M OD2 
21729 N  N   . MET   M  73  ? 1.5733 0.5188 1.1565 -0.0614 -0.1169 0.0182  60  MET   M N   
21730 C  CA  . MET   M  73  ? 1.5723 0.5097 1.1902 -0.0588 -0.1157 -0.0613 60  MET   M CA  
21731 C  C   . MET   M  73  ? 1.5182 0.4629 1.2220 -0.0719 -0.1386 -0.0325 60  MET   M C   
21732 O  O   . MET   M  73  ? 1.4900 0.5208 1.3098 -0.0705 -0.1397 -0.0603 60  MET   M O   
21733 C  CB  . MET   M  73  ? 1.6050 0.5167 1.1488 -0.0978 -0.1067 -0.0845 60  MET   M CB  
21734 C  CG  . MET   M  73  ? 1.6638 0.5373 1.0894 -0.0816 -0.0925 -0.1310 60  MET   M CG  
21735 S  SD  . MET   M  73  ? 1.7516 0.5419 1.0774 -0.0448 -0.1048 -0.1322 60  MET   M SD  
21736 C  CE  . MET   M  73  ? 1.7103 0.5498 1.1776 -0.0513 -0.1702 -0.1198 60  MET   M CE  
21737 N  N   . GLN   M  74  ? 1.5134 0.3426 1.1941 -0.0653 -0.1321 -0.0447 61  GLN   M N   
21738 C  CA  . GLN   M  74  ? 1.5426 0.4031 1.1613 -0.0484 -0.1315 -0.0784 61  GLN   M CA  
21739 C  C   . GLN   M  74  ? 1.5965 0.3670 1.1869 -0.0037 -0.1230 -0.1049 61  GLN   M C   
21740 O  O   . GLN   M  74  ? 1.6508 0.3235 1.2489 0.0447  -0.0962 -0.0663 61  GLN   M O   
21741 C  CB  . GLN   M  74  ? 1.5384 0.3772 1.1415 -0.0699 -0.1396 -0.0880 61  GLN   M CB  
21742 C  CG  . GLN   M  74  ? 1.5259 0.3757 1.1285 -0.0860 -0.1523 -0.0933 61  GLN   M CG  
21743 C  CD  . GLN   M  74  ? 1.5414 0.3671 1.1172 -0.0906 -0.1627 -0.0592 61  GLN   M CD  
21744 O  OE1 . GLN   M  74  ? 1.5149 0.4058 1.1700 -0.0916 -0.1730 -0.0448 61  GLN   M OE1 
21745 N  NE2 . GLN   M  74  ? 1.5838 0.4182 1.0775 -0.0860 -0.1496 -0.0561 61  GLN   M NE2 
21746 N  N   . HIS   M  75  ? 1.6182 0.4117 1.1922 0.0294  -0.1121 -0.0890 62  HIS   M N   
21747 C  CA  . HIS   M  75  ? 1.5691 0.4001 1.1914 0.0568  -0.1105 -0.0953 62  HIS   M CA  
21748 C  C   . HIS   M  75  ? 1.5512 0.5120 1.2146 0.0350  -0.1552 -0.0602 62  HIS   M C   
21749 O  O   . HIS   M  75  ? 1.5809 0.5981 1.3284 0.1915  -0.1767 -0.1047 62  HIS   M O   
21750 C  CB  . HIS   M  75  ? 1.5544 0.4281 1.1880 0.0288  -0.0984 -0.0858 62  HIS   M CB  
21751 C  CG  . HIS   M  75  ? 1.5515 0.4771 1.1534 -0.0003 -0.0669 -0.0693 62  HIS   M CG  
21752 N  ND1 . HIS   M  75  ? 1.5207 0.5246 1.1470 -0.0440 -0.0587 -0.0585 62  HIS   M ND1 
21753 C  CD2 . HIS   M  75  ? 1.5795 0.5326 1.1312 -0.0372 -0.0523 -0.0551 62  HIS   M CD2 
21754 C  CE1 . HIS   M  75  ? 1.5637 0.5357 1.1546 -0.0517 -0.0437 -0.0404 62  HIS   M CE1 
21755 N  NE2 . HIS   M  75  ? 1.6013 0.5125 1.1760 -0.0825 -0.0023 -0.0809 62  HIS   M NE2 
21756 N  N   . ILE   M  76  ? 1.5374 0.3959 1.1816 0.0734  -0.1394 0.0014  63  ILE   M N   
21757 C  CA  . ILE   M  76  ? 1.5311 0.4508 1.2006 0.0625  -0.1088 0.0126  63  ILE   M CA  
21758 C  C   . ILE   M  76  ? 1.5873 0.4726 1.1863 0.0098  -0.0947 0.0088  63  ILE   M C   
21759 O  O   . ILE   M  76  ? 1.5436 0.6115 1.2266 0.0395  -0.0983 0.0230  63  ILE   M O   
21760 C  CB  . ILE   M  76  ? 1.4977 0.4968 1.2026 0.0536  -0.1211 0.0076  63  ILE   M CB  
21761 C  CG1 . ILE   M  76  ? 1.5057 0.5336 1.2186 0.0880  -0.1286 -0.0239 63  ILE   M CG1 
21762 C  CG2 . ILE   M  76  ? 1.4950 0.5360 1.2054 0.0615  -0.1121 0.0365  63  ILE   M CG2 
21763 C  CD1 . ILE   M  76  ? 1.4953 0.5477 1.2320 0.0942  -0.1522 -0.0532 63  ILE   M CD1 
21764 N  N   . GLU   M  77  ? 1.5783 0.4787 1.2022 0.0220  -0.1081 0.0091  64  GLU   M N   
21765 C  CA  . GLU   M  77  ? 1.5965 0.6245 1.1976 0.0040  -0.0944 -0.0047 64  GLU   M CA  
21766 C  C   . GLU   M  77  ? 1.5584 0.6199 1.1816 0.0365  -0.0661 -0.0353 64  GLU   M C   
21767 O  O   . GLU   M  77  ? 1.5885 0.5929 1.0901 0.0025  -0.0344 -0.0778 64  GLU   M O   
21768 C  CB  . GLU   M  77  ? 1.6411 0.6881 1.2288 -0.0110 -0.1449 0.0013  64  GLU   M CB  
21769 C  CG  . GLU   M  77  ? 1.6899 0.7227 1.3072 -0.0647 -0.1265 -0.0070 64  GLU   M CG  
21770 C  CD  . GLU   M  77  ? 1.7338 0.7880 1.3173 -0.1085 -0.1805 -0.0359 64  GLU   M CD  
21771 O  OE1 . GLU   M  77  ? 1.8088 0.7339 1.4158 -0.1373 -0.1611 -0.1476 64  GLU   M OE1 
21772 O  OE2 . GLU   M  77  ? 1.7475 0.7971 1.2741 -0.2470 -0.2301 -0.0314 64  GLU   M OE2 
21773 N  N   . ARG   M  78  ? 1.5694 0.6236 1.2403 0.0275  -0.0516 -0.0471 65  ARG   M N   
21774 C  CA  . ARG   M  78  ? 1.6264 0.6030 1.3234 0.0382  -0.0441 -0.1124 65  ARG   M CA  
21775 C  C   . ARG   M  78  ? 1.5943 0.6013 1.3163 0.0099  -0.0561 -0.1149 65  ARG   M C   
21776 O  O   . ARG   M  78  ? 1.5627 0.6878 1.3334 0.2054  -0.0379 -0.0741 65  ARG   M O   
21777 C  CB  . ARG   M  78  ? 1.6405 0.7209 1.4189 0.0640  -0.0053 -0.0845 65  ARG   M CB  
21778 C  CG  . ARG   M  78  ? 1.6510 0.9677 1.4797 -0.0475 -0.0548 -0.1078 65  ARG   M CG  
21779 C  CD  . ARG   M  78  ? 1.7183 1.1807 1.5763 -0.0056 0.0478  -0.0473 65  ARG   M CD  
21780 N  NE  . ARG   M  78  ? 1.7475 1.3578 1.5852 -0.0214 0.1306  0.0397  65  ARG   M NE  
21781 C  CZ  . ARG   M  78  ? 1.7551 1.3903 1.6341 0.0318  0.1592  0.0004  65  ARG   M CZ  
21782 N  NH1 . ARG   M  78  ? 1.8312 1.3258 1.7154 0.0400  0.1905  -0.0307 65  ARG   M NH1 
21783 N  NH2 . ARG   M  78  ? 1.7225 1.3965 1.6849 0.0414  0.1135  0.0216  65  ARG   M NH2 
21784 N  N   . LEU   M  79  ? 1.5698 0.3765 1.3534 0.0215  -0.0386 -0.1229 66  LEU   M N   
21785 C  CA  . LEU   M  79  ? 1.5325 0.3902 1.3922 0.0211  -0.0337 -0.1099 66  LEU   M CA  
21786 C  C   . LEU   M  79  ? 1.5274 0.4170 1.3454 0.0007  -0.0493 -0.2019 66  LEU   M C   
21787 O  O   . LEU   M  79  ? 1.4088 0.3793 1.3661 -0.0070 -0.0315 -0.3307 66  LEU   M O   
21788 C  CB  . LEU   M  79  ? 1.5710 0.3392 1.3866 0.0298  -0.0175 -0.0786 66  LEU   M CB  
21789 C  CG  . LEU   M  79  ? 1.5859 0.3532 1.4082 0.0385  -0.0034 -0.0481 66  LEU   M CG  
21790 C  CD1 . LEU   M  79  ? 1.5782 0.3178 1.4004 0.0068  -0.0241 -0.0239 66  LEU   M CD1 
21791 C  CD2 . LEU   M  79  ? 1.6046 0.4109 1.4395 0.0310  0.0279  0.0119  66  LEU   M CD2 
21792 N  N   . LEU   M  80  ? 1.5825 0.4596 1.3123 0.0191  -0.0855 -0.1356 67  LEU   M N   
21793 C  CA  . LEU   M  80  ? 1.5688 0.5486 1.3401 0.0092  -0.1118 -0.1039 67  LEU   M CA  
21794 C  C   . LEU   M  80  ? 1.6094 0.5832 1.3719 -0.0328 -0.2197 -0.1234 67  LEU   M C   
21795 O  O   . LEU   M  80  ? 1.6682 0.5567 1.3953 -0.0115 -0.2208 -0.1245 67  LEU   M O   
21796 C  CB  . LEU   M  80  ? 1.6170 0.5480 1.2812 -0.0041 -0.1340 -0.1043 67  LEU   M CB  
21797 C  CG  . LEU   M  80  ? 1.6118 0.5884 1.2626 -0.0489 -0.1507 -0.0891 67  LEU   M CG  
21798 C  CD1 . LEU   M  80  ? 1.6476 0.6444 1.1880 -0.0246 -0.1628 -0.0277 67  LEU   M CD1 
21799 C  CD2 . LEU   M  80  ? 1.5978 0.5758 1.3294 -0.0476 -0.1498 -0.0797 67  LEU   M CD2 
21800 N  N   . LYS   M  81  ? 1.6454 0.6916 1.4165 -0.0975 -0.2800 -0.1725 68  LYS   M N   
21801 C  CA  . LYS   M  81  ? 1.7090 0.7606 1.4594 -0.0735 -0.2615 -0.2399 68  LYS   M CA  
21802 C  C   . LYS   M  81  ? 1.6441 0.7108 1.4209 -0.0533 -0.2226 -0.3106 68  LYS   M C   
21803 O  O   . LYS   M  81  ? 1.5417 0.7136 1.5274 -0.0434 -0.2052 -0.3007 68  LYS   M O   
21804 C  CB  . LYS   M  81  ? 1.7876 0.9295 1.5159 -0.0516 -0.3427 -0.2196 68  LYS   M CB  
21805 C  CG  . LYS   M  81  ? 1.9278 1.0079 1.5214 -0.0312 -0.4039 -0.2612 68  LYS   M CG  
21806 C  CD  . LYS   M  81  ? 1.9832 1.1265 1.5465 0.0034  -0.4421 -0.2301 68  LYS   M CD  
21807 C  CE  . LYS   M  81  ? 1.9933 1.0720 1.6134 -0.0184 -0.4347 -0.1773 68  LYS   M CE  
21808 N  NZ  . LYS   M  81  ? 2.0407 1.0618 1.5818 -0.0082 -0.4152 -0.1387 68  LYS   M NZ  
21809 N  N   . ASP   M  82  ? 1.6736 0.5507 1.4110 -0.0740 -0.2179 -0.3089 69  ASP   M N   
21810 C  CA  . ASP   M  82  ? 1.6304 0.5253 1.5035 -0.0706 -0.1725 -0.3029 69  ASP   M CA  
21811 C  C   . ASP   M  82  ? 1.5840 0.4593 1.4791 -0.0742 -0.0971 -0.2219 69  ASP   M C   
21812 O  O   . ASP   M  82  ? 1.4567 0.5406 1.6155 0.0621  -0.0683 -0.1977 69  ASP   M O   
21813 C  CB  . ASP   M  82  ? 1.6737 0.7413 1.5707 -0.1106 -0.1333 -0.3899 69  ASP   M CB  
21814 C  CG  . ASP   M  82  ? 1.7921 0.8998 1.7278 -0.1459 -0.0401 -0.2685 69  ASP   M CG  
21815 O  OD1 . ASP   M  82  ? 1.8182 1.3292 1.8756 -0.1940 -0.0975 -0.4655 69  ASP   M OD1 
21816 O  OD2 . ASP   M  82  ? 1.8583 1.4009 1.6565 -0.2101 -0.1525 -0.4771 69  ASP   M OD2 
21817 N  N   . LEU   M  83  ? 1.5337 0.2894 1.4241 -0.0075 -0.1113 -0.1202 70  LEU   M N   
21818 C  CA  . LEU   M  83  ? 1.5906 0.2620 1.4442 0.0687  -0.1170 -0.0106 70  LEU   M CA  
21819 C  C   . LEU   M  83  ? 1.6280 0.2642 1.3820 -0.0011 -0.0938 0.0120  70  LEU   M C   
21820 O  O   . LEU   M  83  ? 1.5901 0.4174 1.5027 0.0491  -0.1544 0.0274  70  LEU   M O   
21821 C  CB  . LEU   M  83  ? 1.5870 0.3044 1.4519 0.0491  -0.1615 -0.0054 70  LEU   M CB  
21822 C  CG  . LEU   M  83  ? 1.5936 0.3506 1.4972 0.0823  -0.1881 0.0121  70  LEU   M CG  
21823 C  CD1 . LEU   M  83  ? 1.5874 0.4400 1.4896 0.0384  -0.2094 -0.0152 70  LEU   M CD1 
21824 C  CD2 . LEU   M  83  ? 1.6088 0.3454 1.5537 0.0834  -0.1601 0.0274  70  LEU   M CD2 
21825 N  N   . VAL   M  84  ? 1.6211 0.3276 1.3638 0.0299  -0.0660 0.0118  71  VAL   M N   
21826 C  CA  . VAL   M  84  ? 1.6106 0.4314 1.3566 0.0405  -0.0549 0.0194  71  VAL   M CA  
21827 C  C   . VAL   M  84  ? 1.6046 0.4581 1.3113 0.0382  -0.0373 -0.0318 71  VAL   M C   
21828 O  O   . VAL   M  84  ? 1.6249 0.4863 1.2361 0.0563  -0.0156 -0.0374 71  VAL   M O   
21829 C  CB  . VAL   M  84  ? 1.6169 0.5185 1.3136 0.0848  -0.0432 0.0195  71  VAL   M CB  
21830 C  CG1 . VAL   M  84  ? 1.5997 0.4654 1.3324 0.0936  -0.0503 -0.0031 71  VAL   M CG1 
21831 C  CG2 . VAL   M  84  ? 1.6358 0.5235 1.2911 0.0698  -0.0552 0.0396  71  VAL   M CG2 
21832 N  N   . THR   M  85  ? 1.6071 0.5279 1.3258 0.0320  -0.0552 -0.0814 72  THR   M N   
21833 C  CA  . THR   M  85  ? 1.6252 0.5524 1.4289 0.0232  -0.0595 -0.1336 72  THR   M CA  
21834 C  C   . THR   M  85  ? 1.6300 0.5727 1.4330 0.0208  -0.0851 -0.1398 72  THR   M C   
21835 O  O   . THR   M  85  ? 1.6361 0.6731 1.6724 0.1262  -0.0332 -0.1524 72  THR   M O   
21836 C  CB  . THR   M  85  ? 1.6290 0.5812 1.4123 0.0586  -0.0786 -0.1036 72  THR   M CB  
21837 O  OG1 . THR   M  85  ? 1.6395 0.6226 1.3386 0.0393  -0.0906 -0.1009 72  THR   M OG1 
21838 C  CG2 . THR   M  85  ? 1.6140 0.6135 1.4528 0.0358  -0.0842 -0.1130 72  THR   M CG2 
21839 N  N   . GLU   M  86  ? 1.5946 0.4167 1.4333 -0.0011 -0.1048 -0.1619 73  GLU   M N   
21840 C  CA  . GLU   M  86  ? 1.5852 0.4879 1.4208 -0.0168 -0.0853 -0.1287 73  GLU   M CA  
21841 C  C   . GLU   M  86  ? 1.5885 0.5195 1.3540 -0.0029 -0.0795 -0.1111 73  GLU   M C   
21842 O  O   . GLU   M  86  ? 1.6234 0.4858 1.4306 0.0423  -0.1350 -0.2170 73  GLU   M O   
21843 C  CB  . GLU   M  86  ? 1.5762 0.4895 1.4579 -0.0451 -0.0418 -0.1293 73  GLU   M CB  
21844 C  CG  . GLU   M  86  ? 1.5534 0.5940 1.5275 -0.1231 0.0051  -0.1284 73  GLU   M CG  
21845 C  CD  . GLU   M  86  ? 1.5910 0.5164 1.6035 -0.1834 0.0097  -0.1609 73  GLU   M CD  
21846 O  OE1 . GLU   M  86  ? 1.7707 0.4562 1.7021 -0.1739 0.0490  -0.2307 73  GLU   M OE1 
21847 O  OE2 . GLU   M  86  ? 1.5282 0.5843 1.5595 -0.2102 0.0121  -0.0993 73  GLU   M OE2 
21848 N  N   . ASN   M  87  ? 1.6204 0.4448 1.2730 0.0439  -0.0575 -0.0694 74  ASN   M N   
21849 C  CA  . ASN   M  87  ? 1.6170 0.5152 1.2479 0.0375  -0.0161 -0.0688 74  ASN   M CA  
21850 C  C   . ASN   M  87  ? 1.6360 0.5770 1.2645 0.0279  0.0166  -0.0948 74  ASN   M C   
21851 O  O   . ASN   M  87  ? 1.5710 0.6718 1.2878 0.0244  0.0238  -0.0881 74  ASN   M O   
21852 C  CB  . ASN   M  87  ? 1.6169 0.5169 1.1848 0.0349  0.0006  -0.0951 74  ASN   M CB  
21853 C  CG  . ASN   M  87  ? 1.6177 0.5513 1.1491 0.0346  0.0560  -0.1085 74  ASN   M CG  
21854 O  OD1 . ASN   M  87  ? 1.6395 0.6408 1.1741 0.0422  0.0371  -0.0945 74  ASN   M OD1 
21855 N  ND2 . ASN   M  87  ? 1.6728 0.5857 1.1374 0.0324  0.0696  -0.1314 74  ASN   M ND2 
21856 N  N   . ALA   M  88  ? 1.6482 0.5913 1.2800 0.0157  0.0025  -0.1087 75  ALA   M N   
21857 C  CA  . ALA   M  88  ? 1.6863 0.5916 1.3230 0.0004  0.0609  -0.1222 75  ALA   M CA  
21858 C  C   . ALA   M  88  ? 1.7065 0.5843 1.4007 -0.0197 0.0608  -0.1490 75  ALA   M C   
21859 O  O   . ALA   M  88  ? 1.7615 0.5128 1.4535 -0.1156 0.1224  -0.1852 75  ALA   M O   
21860 C  CB  . ALA   M  88  ? 1.7071 0.6548 1.2836 -0.0018 0.0796  -0.1201 75  ALA   M CB  
21861 N  N   . TYR   M  89  ? 1.6660 0.5983 1.3855 -0.0003 0.0312  -0.1379 76  TYR   M N   
21862 C  CA  . TYR   M  89  ? 1.6419 0.5800 1.4309 0.0147  0.0151  -0.1469 76  TYR   M CA  
21863 C  C   . TYR   M  89  ? 1.6519 0.6381 1.5129 0.0350  0.0156  -0.1099 76  TYR   M C   
21864 O  O   . TYR   M  89  ? 1.6363 0.6604 1.5590 0.0565  0.0076  -0.1626 76  TYR   M O   
21865 C  CB  . TYR   M  89  ? 1.6093 0.5538 1.3885 0.0531  -0.0196 -0.1346 76  TYR   M CB  
21866 C  CG  . TYR   M  89  ? 1.6340 0.5434 1.3656 0.0766  -0.0505 -0.1302 76  TYR   M CG  
21867 C  CD1 . TYR   M  89  ? 1.6375 0.5145 1.3737 0.0792  -0.0672 -0.1300 76  TYR   M CD1 
21868 C  CD2 . TYR   M  89  ? 1.6208 0.4947 1.3426 0.1198  -0.0833 -0.1146 76  TYR   M CD2 
21869 C  CE1 . TYR   M  89  ? 1.6527 0.4665 1.3458 0.0757  -0.0966 -0.1454 76  TYR   M CE1 
21870 C  CE2 . TYR   M  89  ? 1.6277 0.4203 1.3069 0.1204  -0.0921 -0.1323 76  TYR   M CE2 
21871 C  CZ  . TYR   M  89  ? 1.6064 0.4208 1.3322 0.1076  -0.1450 -0.1366 76  TYR   M CZ  
21872 O  OH  . TYR   M  89  ? 1.6019 0.4374 1.2943 0.0799  -0.1702 -0.1690 76  TYR   M OH  
21873 N  N   . ASP   M  90  ? 1.6291 0.6100 1.5651 0.0426  0.0410  -0.0787 77  ASP   M N   
21874 C  CA  . ASP   M  90  ? 1.5663 0.6648 1.6054 0.0347  0.0665  -0.0280 77  ASP   M CA  
21875 C  C   . ASP   M  90  ? 1.5623 0.6836 1.6404 0.0237  0.0535  0.0056  77  ASP   M C   
21876 O  O   . ASP   M  90  ? 1.4972 0.6694 1.7092 -0.0145 0.0376  0.0569  77  ASP   M O   
21877 C  CB  . ASP   M  90  ? 1.5617 0.7030 1.6285 0.0906  0.1007  0.0019  77  ASP   M CB  
21878 C  CG  . ASP   M  90  ? 1.5396 0.6928 1.5971 0.1187  0.1289  0.0208  77  ASP   M CG  
21879 O  OD1 . ASP   M  90  ? 1.5289 0.7185 1.5871 0.1433  0.1255  0.0338  77  ASP   M OD1 
21880 O  OD2 . ASP   M  90  ? 1.4825 0.7035 1.6567 0.1489  0.1585  0.0814  77  ASP   M OD2 
21881 N  N   . ASN   M  91  ? 1.5436 0.7370 1.5715 -0.0067 0.0151  -0.0048 78  ASN   M N   
21882 C  CA  . ASN   M  91  ? 1.5781 0.7181 1.5502 -0.0257 0.0325  0.0127  78  ASN   M CA  
21883 C  C   . ASN   M  91  ? 1.6220 0.6679 1.5288 -0.0161 0.0244  -0.0105 78  ASN   M C   
21884 O  O   . ASN   M  91  ? 1.5700 0.4383 1.5185 -0.0372 0.0104  -0.1203 78  ASN   M O   
21885 C  CB  . ASN   M  91  ? 1.5791 0.6824 1.5178 -0.0457 0.0185  0.0660  78  ASN   M CB  
21886 C  CG  . ASN   M  91  ? 1.5599 0.7939 1.5559 -0.0813 0.0193  0.1222  78  ASN   M CG  
21887 O  OD1 . ASN   M  91  ? 1.5539 0.7464 1.6024 -0.1054 0.0090  0.1767  78  ASN   M OD1 
21888 N  ND2 . ASN   M  91  ? 1.5904 0.8186 1.5774 -0.0379 0.0378  0.1049  78  ASN   M ND2 
21889 N  N   . PRO   M  92  ? 1.6703 0.7289 1.5977 0.0144  0.0818  -0.0464 79  PRO   M N   
21890 C  CA  . PRO   M  92  ? 1.7252 0.7457 1.6071 0.0146  0.1036  -0.0704 79  PRO   M CA  
21891 C  C   . PRO   M  92  ? 1.7508 0.7472 1.6234 0.0212  0.1159  -0.0245 79  PRO   M C   
21892 O  O   . PRO   M  92  ? 1.7607 0.7206 1.5966 0.0042  0.1159  -0.0891 79  PRO   M O   
21893 C  CB  . PRO   M  92  ? 1.7528 0.7265 1.6544 0.0164  0.1603  -0.0835 79  PRO   M CB  
21894 C  CG  . PRO   M  92  ? 1.7587 0.7295 1.6696 0.0061  0.1544  -0.0714 79  PRO   M CG  
21895 C  CD  . PRO   M  92  ? 1.7080 0.6924 1.6409 0.0224  0.1222  -0.0389 79  PRO   M CD  
21896 N  N   . LEU   M  93  ? 1.7927 0.7777 1.6614 0.0763  0.0618  -0.0487 80  LEU   M N   
21897 C  CA  . LEU   M  93  ? 1.7714 0.8394 1.7256 0.0628  0.0648  -0.0319 80  LEU   M CA  
21898 C  C   . LEU   M  93  ? 1.6692 1.0001 1.7070 0.1683  0.0100  0.0045  80  LEU   M C   
21899 O  O   . LEU   M  93  ? 1.6854 0.9778 1.7425 0.1692  -0.0075 0.0373  80  LEU   M O   
21900 C  CB  . LEU   M  93  ? 1.7768 0.7277 1.7670 0.2000  0.0737  0.0400  80  LEU   M CB  
21901 C  CG  . LEU   M  93  ? 1.8213 0.7028 1.7934 0.2013  0.1281  0.0476  80  LEU   M CG  
21902 C  CD1 . LEU   M  93  ? 1.8079 0.7290 1.8275 0.2171  0.1190  0.0747  80  LEU   M CD1 
21903 C  CD2 . LEU   M  93  ? 1.8417 0.6191 1.7796 0.2315  0.1315  0.0454  80  LEU   M CD2 
21904 N  N   . ALA   M  94  ? 1.6787 1.0826 1.6635 0.1117  -0.0059 -0.0212 81  ALA   M N   
21905 C  CA  . ALA   M  94  ? 1.6873 1.0239 1.5953 0.0722  -0.0064 -0.0486 81  ALA   M CA  
21906 C  C   . ALA   M  94  ? 1.6753 0.9607 1.5647 0.0731  0.0330  -0.1151 81  ALA   M C   
21907 O  O   . ALA   M  94  ? 1.5877 0.9844 1.4734 0.0713  0.0688  -0.1174 81  ALA   M O   
21908 C  CB  . ALA   M  94  ? 1.7132 1.1074 1.6123 0.0598  -0.0505 -0.0605 81  ALA   M CB  
21909 N  N   . ASP   M  95  ? 1.7405 0.9275 1.5655 0.0430  0.0777  -0.0688 82  ASP   M N   
21910 C  CA  . ASP   M  95  ? 1.8129 0.8529 1.5667 0.0839  0.0776  -0.0670 82  ASP   M CA  
21911 C  C   . ASP   M  95  ? 1.8017 0.7622 1.5884 0.0664  0.1615  -0.0490 82  ASP   M C   
21912 O  O   . ASP   M  95  ? 1.8605 0.7546 1.5734 0.1120  0.1927  -0.0393 82  ASP   M O   
21913 C  CB  . ASP   M  95  ? 1.8627 0.9268 1.5556 0.0829  0.0648  -0.0370 82  ASP   M CB  
21914 C  CG  . ASP   M  95  ? 1.9278 0.9889 1.6011 0.1266  0.0592  -0.0819 82  ASP   M CG  
21915 O  OD1 . ASP   M  95  ? 1.9628 1.0494 1.6211 0.2037  0.0441  -0.0662 82  ASP   M OD1 
21916 O  OD2 . ASP   M  95  ? 1.9496 1.1318 1.5870 0.1193  0.0371  -0.0383 82  ASP   M OD2 
21917 N  N   . ALA   M  96  ? 1.8020 0.7541 1.6083 0.0979  0.1604  -0.0525 83  ALA   M N   
21918 C  CA  . ALA   M  96  ? 1.7966 0.7965 1.6653 0.1246  0.1724  -0.0609 83  ALA   M CA  
21919 C  C   . ALA   M  96  ? 1.8103 0.8121 1.7193 0.1096  0.0945  -0.1030 83  ALA   M C   
21920 O  O   . ALA   M  96  ? 1.9176 0.8502 1.8096 0.1915  0.0425  -0.1142 83  ALA   M O   
21921 C  CB  . ALA   M  96  ? 1.7950 0.8230 1.6666 0.1412  0.2247  -0.0496 83  ALA   M CB  
21922 N  N   . GLU   M  97  ? 1.7425 0.7756 1.8344 0.1175  0.0888  -0.1068 84  GLU   M N   
21923 C  CA  . GLU   M  97  ? 1.6727 0.8369 1.8445 0.1028  0.0939  -0.1015 84  GLU   M CA  
21924 C  C   . GLU   M  97  ? 1.6579 0.6888 1.8035 0.0901  0.0793  -0.0694 84  GLU   M C   
21925 O  O   . GLU   M  97  ? 1.6415 0.6263 1.7433 0.1082  0.0745  -0.0079 84  GLU   M O   
21926 C  CB  . GLU   M  97  ? 1.6087 0.9318 1.9182 0.1275  0.0678  -0.0978 84  GLU   M CB  
21927 C  CG  . GLU   M  97  ? 1.5996 1.0348 2.0028 0.1170  0.0798  -0.1598 84  GLU   M CG  
21928 C  CD  . GLU   M  97  ? 1.6276 1.1163 2.0354 0.1232  0.0956  -0.2110 84  GLU   M CD  
21929 O  OE1 . GLU   M  97  ? 1.5948 1.1807 2.1361 0.0973  0.1212  -0.2357 84  GLU   M OE1 
21930 O  OE2 . GLU   M  97  ? 1.5726 1.2033 2.0385 0.2030  0.1088  -0.2139 84  GLU   M OE2 
21931 N  N   . GLU   M  98  ? 1.7186 0.6401 1.7389 0.0629  0.0684  -0.1420 85  GLU   M N   
21932 C  CA  . GLU   M  98  ? 1.6693 0.5986 1.6792 0.0408  0.0108  -0.1364 85  GLU   M CA  
21933 C  C   . GLU   M  98  ? 1.6720 0.6477 1.6292 0.0241  -0.0042 -0.0883 85  GLU   M C   
21934 O  O   . GLU   M  98  ? 1.6223 0.5926 1.5391 0.0917  -0.0678 -0.0276 85  GLU   M O   
21935 C  CB  . GLU   M  98  ? 1.7313 0.5561 1.6782 0.0295  0.0116  -0.2279 85  GLU   M CB  
21936 C  CG  . GLU   M  98  ? 1.7428 0.5014 1.6893 0.0134  0.0133  -0.2277 85  GLU   M CG  
21937 C  CD  . GLU   M  98  ? 1.7932 0.3903 1.6992 0.0597  0.0859  -0.2832 85  GLU   M CD  
21938 O  OE1 . GLU   M  98  ? 1.8072 0.4370 1.6952 0.0638  0.1012  -0.2599 85  GLU   M OE1 
21939 O  OE2 . GLU   M  98  ? 1.8074 0.3755 1.6164 0.0946  0.0158  -0.2952 85  GLU   M OE2 
21940 N  N   . ALA   M  99  ? 1.6658 0.6972 1.6140 0.0324  -0.0140 -0.0568 86  ALA   M N   
21941 C  CA  . ALA   M  99  ? 1.6758 0.7416 1.5818 0.0775  -0.0165 -0.1013 86  ALA   M CA  
21942 C  C   . ALA   M  99  ? 1.6679 0.7503 1.5548 0.0889  -0.0171 -0.0876 86  ALA   M C   
21943 O  O   . ALA   M  99  ? 1.7078 0.8491 1.5711 0.1091  -0.0386 -0.1563 86  ALA   M O   
21944 C  CB  . ALA   M  99  ? 1.7088 0.7760 1.5638 0.1209  -0.0037 -0.0882 86  ALA   M CB  
21945 N  N   . LEU   M  100 ? 1.6604 0.6421 1.4275 0.0526  -0.0341 -0.0542 87  LEU   M N   
21946 C  CA  . LEU   M  100 ? 1.6312 0.6084 1.3815 0.0282  -0.0684 -0.0398 87  LEU   M CA  
21947 C  C   . LEU   M  100 ? 1.6233 0.6279 1.3823 0.0221  -0.0939 -0.0922 87  LEU   M C   
21948 O  O   . LEU   M  100 ? 1.6680 0.6878 1.2701 -0.0501 -0.0762 -0.1726 87  LEU   M O   
21949 C  CB  . LEU   M  100 ? 1.6299 0.5699 1.3284 0.0035  -0.0755 -0.0153 87  LEU   M CB  
21950 C  CG  . LEU   M  100 ? 1.6689 0.5495 1.3435 -0.0170 -0.0978 -0.0021 87  LEU   M CG  
21951 C  CD1 . LEU   M  100 ? 1.6856 0.5096 1.3227 -0.0210 -0.1185 -0.0225 87  LEU   M CD1 
21952 C  CD2 . LEU   M  100 ? 1.6719 0.5885 1.3492 -0.0069 -0.1209 0.0149  87  LEU   M CD2 
21953 N  N   . GLU   M  101 ? 1.5705 0.6704 1.4517 0.0373  -0.1387 -0.0873 88  GLU   M N   
21954 C  CA  . GLU   M  101 ? 1.5322 0.6554 1.5218 0.0477  -0.1017 -0.0757 88  GLU   M CA  
21955 C  C   . GLU   M  101 ? 1.4746 0.5839 1.4576 -0.0086 -0.1216 -0.0698 88  GLU   M C   
21956 O  O   . GLU   M  101 ? 1.4000 0.6456 1.4113 0.0193  -0.1710 -0.1020 88  GLU   M O   
21957 C  CB  . GLU   M  101 ? 1.4959 0.7177 1.5664 0.0661  -0.1009 -0.0647 88  GLU   M CB  
21958 C  CG  . GLU   M  101 ? 1.4737 0.7633 1.6267 0.0601  -0.0668 -0.0841 88  GLU   M CG  
21959 C  CD  . GLU   M  101 ? 1.4899 0.7493 1.6350 0.0380  -0.0678 -0.0971 88  GLU   M CD  
21960 O  OE1 . GLU   M  101 ? 1.4843 0.7114 1.6481 0.0882  -0.0621 -0.1033 88  GLU   M OE1 
21961 O  OE2 . GLU   M  101 ? 1.5156 0.7553 1.6415 -0.0373 -0.1063 -0.1187 88  GLU   M OE2 
21962 N  N   . PRO   M  102 ? 1.4806 0.4934 1.4125 0.0661  -0.1114 -0.1388 89  PRO   M N   
21963 C  CA  . PRO   M  102 ? 1.4908 0.3886 1.3872 0.0249  -0.1464 -0.1006 89  PRO   M CA  
21964 C  C   . PRO   M  102 ? 1.4787 0.2841 1.3882 0.0425  -0.1533 -0.0698 89  PRO   M C   
21965 O  O   . PRO   M  102 ? 1.4707 0.1921 1.4291 0.0516  -0.1652 -0.0446 89  PRO   M O   
21966 C  CB  . PRO   M  102 ? 1.4814 0.4003 1.3856 0.0260  -0.1202 -0.1214 89  PRO   M CB  
21967 C  CG  . PRO   M  102 ? 1.5089 0.4452 1.3885 0.0220  -0.1023 -0.1285 89  PRO   M CG  
21968 C  CD  . PRO   M  102 ? 1.5202 0.4479 1.4331 0.0276  -0.0958 -0.1187 89  PRO   M CD  
21969 N  N   . SER   M  103 ? 1.4821 0.2890 1.3465 0.0252  -0.1481 -0.0541 90  SER   M N   
21970 C  CA  . SER   M  103 ? 1.4227 0.3342 1.3397 0.0299  -0.1875 -0.0343 90  SER   M CA  
21971 C  C   . SER   M  103 ? 1.4106 0.3938 1.2671 0.0563  -0.1508 0.0169  90  SER   M C   
21972 O  O   . SER   M  103 ? 1.3880 0.2881 1.2006 -0.0192 -0.1863 0.0237  90  SER   M O   
21973 C  CB  . SER   M  103 ? 1.4271 0.3697 1.3809 0.0373  -0.2033 -0.0335 90  SER   M CB  
21974 O  OG  . SER   M  103 ? 1.4200 0.4029 1.4253 0.0537  -0.2158 -0.0792 90  SER   M OG  
21975 N  N   . TYR   M  104 ? 1.4059 0.3791 1.2976 0.0591  -0.1381 0.0214  91  TYR   M N   
21976 C  CA  . TYR   M  104 ? 1.3878 0.4591 1.3205 0.0695  -0.1017 0.0694  91  TYR   M CA  
21977 C  C   . TYR   M  104 ? 1.4046 0.4751 1.2744 0.1022  -0.0708 0.0440  91  TYR   M C   
21978 O  O   . TYR   M  104 ? 1.4061 0.4238 1.1592 0.1605  -0.1232 0.0869  91  TYR   M O   
21979 C  CB  . TYR   M  104 ? 1.4124 0.4615 1.3884 0.0530  -0.0967 0.0480  91  TYR   M CB  
21980 C  CG  . TYR   M  104 ? 1.4127 0.4558 1.4946 0.0433  -0.0606 0.0479  91  TYR   M CG  
21981 C  CD1 . TYR   M  104 ? 1.4301 0.5105 1.5417 0.0528  -0.0866 0.0509  91  TYR   M CD1 
21982 C  CD2 . TYR   M  104 ? 1.4094 0.3696 1.5369 -0.0057 -0.0547 0.0544  91  TYR   M CD2 
21983 C  CE1 . TYR   M  104 ? 1.4753 0.4564 1.6133 0.0777  -0.0728 0.0700  91  TYR   M CE1 
21984 C  CE2 . TYR   M  104 ? 1.4474 0.3676 1.6017 0.0242  -0.0325 0.0754  91  TYR   M CE2 
21985 C  CZ  . TYR   M  104 ? 1.4741 0.4286 1.6248 0.0453  -0.0563 0.0751  91  TYR   M CZ  
21986 O  OH  . TYR   M  104 ? 1.4332 0.5722 1.7165 0.0408  0.0117  0.1086  91  TYR   M OH  
21987 N  N   . ILE   M  105 ? 1.4449 0.5098 1.2665 0.0844  -0.0326 0.0553  92  ILE   M N   
21988 C  CA  . ILE   M  105 ? 1.4346 0.5352 1.2522 0.0684  -0.0319 0.0718  92  ILE   M CA  
21989 C  C   . ILE   M  105 ? 1.5136 0.5078 1.2385 -0.0206 -0.0509 0.0557  92  ILE   M C   
21990 O  O   . ILE   M  105 ? 1.4962 0.5119 1.2546 -0.0543 -0.0753 0.0503  92  ILE   M O   
21991 C  CB  . ILE   M  105 ? 1.4259 0.5521 1.2519 0.0877  -0.0203 0.0763  92  ILE   M CB  
21992 C  CG1 . ILE   M  105 ? 1.4304 0.5863 1.2687 0.0690  -0.0187 0.0478  92  ILE   M CG1 
21993 C  CG2 . ILE   M  105 ? 1.4370 0.5727 1.2650 0.0869  -0.0500 0.1113  92  ILE   M CG2 
21994 C  CD1 . ILE   M  105 ? 1.4483 0.6322 1.2796 0.0407  -0.0155 0.0536  92  ILE   M CD1 
21995 N  N   . PHE   M  106 ? 1.5694 0.4439 1.2245 -0.0539 -0.0298 0.0561  93  PHE   M N   
21996 C  CA  . PHE   M  106 ? 1.6188 0.4941 1.2114 -0.0479 -0.0851 0.0294  93  PHE   M CA  
21997 C  C   . PHE   M  106 ? 1.6542 0.4605 1.2377 -0.0752 -0.0956 0.0447  93  PHE   M C   
21998 O  O   . PHE   M  106 ? 1.7006 0.3955 1.2533 -0.0406 -0.0546 0.1193  93  PHE   M O   
21999 C  CB  . PHE   M  106 ? 1.6095 0.5514 1.1500 -0.0498 -0.1083 0.0343  93  PHE   M CB  
22000 C  CG  . PHE   M  106 ? 1.6812 0.5729 1.1002 -0.0604 -0.1799 0.0290  93  PHE   M CG  
22001 C  CD1 . PHE   M  106 ? 1.6946 0.6091 1.0618 -0.0294 -0.2173 0.0322  93  PHE   M CD1 
22002 C  CD2 . PHE   M  106 ? 1.7046 0.5552 1.1086 -0.0346 -0.2435 -0.0040 93  PHE   M CD2 
22003 C  CE1 . PHE   M  106 ? 1.6873 0.6968 1.0128 -0.0114 -0.2657 0.0042  93  PHE   M CE1 
22004 C  CE2 . PHE   M  106 ? 1.7255 0.6392 1.0647 -0.0490 -0.2579 -0.0291 93  PHE   M CE2 
22005 C  CZ  . PHE   M  106 ? 1.7091 0.6773 1.0148 -0.0349 -0.2789 -0.0043 93  PHE   M CZ  
22006 N  N   . GLU   M  107 ? 1.5631 0.4569 1.3114 -0.0708 -0.1411 -0.0376 94  GLU   M N   
22007 C  CA  . GLU   M  107 ? 1.5655 0.4909 1.3018 -0.0854 -0.1387 -0.0521 94  GLU   M CA  
22008 C  C   . GLU   M  107 ? 1.5467 0.4500 1.3760 -0.0553 -0.1754 -0.0101 94  GLU   M C   
22009 O  O   . GLU   M  107 ? 1.5534 0.3980 1.2823 -0.1384 -0.2540 -0.0727 94  GLU   M O   
22010 C  CB  . GLU   M  107 ? 1.5452 0.5140 1.3674 -0.0647 -0.1093 -0.1160 94  GLU   M CB  
22011 C  CG  . GLU   M  107 ? 1.6190 0.6005 1.3524 -0.1130 -0.0877 -0.1717 94  GLU   M CG  
22012 C  CD  . GLU   M  107 ? 1.6729 0.6802 1.3678 -0.1625 -0.0919 -0.2108 94  GLU   M CD  
22013 O  OE1 . GLU   M  107 ? 1.7533 0.7922 1.3725 -0.2198 -0.0493 -0.2232 94  GLU   M OE1 
22014 O  OE2 . GLU   M  107 ? 1.7082 0.6503 1.3013 -0.1721 -0.0772 -0.2538 94  GLU   M OE2 
22015 N  N   . TYR   M  108 ? 1.5141 0.4493 1.3634 -0.0078 -0.1990 0.0195  95  TYR   M N   
22016 C  CA  . TYR   M  108 ? 1.4822 0.4802 1.4378 0.0284  -0.1850 0.0541  95  TYR   M CA  
22017 C  C   . TYR   M  108 ? 1.4918 0.5025 1.4163 0.0450  -0.1547 0.0960  95  TYR   M C   
22018 O  O   . TYR   M  108 ? 1.4901 0.5013 1.4694 0.0667  -0.1231 0.1637  95  TYR   M O   
22019 C  CB  . TYR   M  108 ? 1.4394 0.4650 1.4506 0.0618  -0.1941 0.0395  95  TYR   M CB  
22020 C  CG  . TYR   M  108 ? 1.4045 0.5088 1.4818 0.1220  -0.2161 0.0423  95  TYR   M CG  
22021 C  CD1 . TYR   M  108 ? 1.3506 0.5311 1.5345 0.1267  -0.2164 0.0631  95  TYR   M CD1 
22022 C  CD2 . TYR   M  108 ? 1.3331 0.5078 1.5084 0.1282  -0.2169 0.0326  95  TYR   M CD2 
22023 C  CE1 . TYR   M  108 ? 1.3276 0.4845 1.5543 0.1831  -0.2352 0.0575  95  TYR   M CE1 
22024 C  CE2 . TYR   M  108 ? 1.3219 0.5770 1.5274 0.1506  -0.2324 0.0188  95  TYR   M CE2 
22025 C  CZ  . TYR   M  108 ? 1.2845 0.5438 1.5516 0.1857  -0.2509 0.0345  95  TYR   M CZ  
22026 O  OH  . TYR   M  108 ? 1.2687 0.5932 1.6305 0.2126  -0.2580 -0.0021 95  TYR   M OH  
22027 N  N   . LEU   M  109 ? 1.4231 0.4656 1.3510 0.0281  -0.1523 0.0471  96  LEU   M N   
22028 C  CA  . LEU   M  109 ? 1.3911 0.3467 1.2508 -0.0547 -0.1689 0.0704  96  LEU   M CA  
22029 C  C   . LEU   M  109 ? 1.3791 0.3530 1.2353 -0.0372 -0.1798 0.0842  96  LEU   M C   
22030 O  O   . LEU   M  109 ? 1.3478 0.3163 1.2052 -0.0026 -0.2275 0.0957  96  LEU   M O   
22031 C  CB  . LEU   M  109 ? 1.3529 0.3641 1.2175 -0.1045 -0.1743 0.0427  96  LEU   M CB  
22032 C  CG  . LEU   M  109 ? 1.3466 0.4077 1.2307 -0.1421 -0.1836 0.0270  96  LEU   M CG  
22033 C  CD1 . LEU   M  109 ? 1.3354 0.5339 1.1914 -0.1710 -0.1673 0.0493  96  LEU   M CD1 
22034 C  CD2 . LEU   M  109 ? 1.3574 0.3857 1.2316 -0.1662 -0.1813 0.0325  96  LEU   M CD2 
22035 N  N   . ALA   M  110 ? 1.3769 0.4453 1.2246 -0.0513 -0.1671 0.0845  97  ALA   M N   
22036 C  CA  . ALA   M  110 ? 1.4257 0.5376 1.2293 -0.0654 -0.1388 0.0510  97  ALA   M CA  
22037 C  C   . ALA   M  110 ? 1.4316 0.5536 1.2302 -0.0481 -0.1325 0.0689  97  ALA   M C   
22038 O  O   . ALA   M  110 ? 1.4680 0.6299 1.1791 -0.0845 -0.1110 0.0627  97  ALA   M O   
22039 C  CB  . ALA   M  110 ? 1.4250 0.5294 1.2648 -0.0712 -0.1378 0.0200  97  ALA   M CB  
22040 N  N   . THR   M  111 ? 1.3773 0.5484 1.2039 -0.0259 -0.1365 0.0939  98  THR   M N   
22041 C  CA  . THR   M  111 ? 1.3620 0.5433 1.2400 -0.0428 -0.1438 0.0949  98  THR   M CA  
22042 C  C   . THR   M  111 ? 1.3714 0.4944 1.2396 -0.0378 -0.2042 0.0785  98  THR   M C   
22043 O  O   . THR   M  111 ? 1.3435 0.5059 1.2172 -0.0454 -0.2293 0.0934  98  THR   M O   
22044 C  CB  . THR   M  111 ? 1.3649 0.5563 1.2674 -0.0206 -0.1211 0.1023  98  THR   M CB  
22045 O  OG1 . THR   M  111 ? 1.3546 0.5250 1.3057 -0.0202 -0.0761 0.1448  98  THR   M OG1 
22046 C  CG2 . THR   M  111 ? 1.3568 0.5890 1.2703 -0.0168 -0.1206 0.1188  98  THR   M CG2 
22047 N  N   . VAL   M  112 ? 1.4019 0.4522 1.2268 -0.0572 -0.1947 0.0414  99  VAL   M N   
22048 C  CA  . VAL   M  112 ? 1.4055 0.4504 1.2445 -0.0637 -0.1904 0.0207  99  VAL   M CA  
22049 C  C   . VAL   M  112 ? 1.4540 0.3991 1.2059 -0.1299 -0.1926 0.0219  99  VAL   M C   
22050 O  O   . VAL   M  112 ? 1.4357 0.1720 1.2240 -0.1465 -0.1975 -0.0336 99  VAL   M O   
22051 C  CB  . VAL   M  112 ? 1.4286 0.4965 1.2471 -0.0492 -0.1921 0.0218  99  VAL   M CB  
22052 C  CG1 . VAL   M  112 ? 1.4204 0.5556 1.2831 -0.0526 -0.1963 0.0253  99  VAL   M CG1 
22053 C  CG2 . VAL   M  112 ? 1.4451 0.4898 1.2602 -0.0208 -0.1933 0.0398  99  VAL   M CG2 
22054 N  N   . MET   M  113 ? 1.5133 0.3842 1.1905 -0.1356 -0.1896 0.0231  100 MET   M N   
22055 C  CA  . MET   M  113 ? 1.5767 0.4305 1.2025 -0.1026 -0.1655 -0.0301 100 MET   M CA  
22056 C  C   . MET   M  113 ? 1.5399 0.4262 1.1988 -0.1551 -0.1728 -0.0384 100 MET   M C   
22057 O  O   . MET   M  113 ? 1.4845 0.3530 1.2217 -0.3169 -0.1311 -0.1787 100 MET   M O   
22058 C  CB  . MET   M  113 ? 1.6370 0.4103 1.2528 -0.0918 -0.1570 0.0248  100 MET   M CB  
22059 C  CG  . MET   M  113 ? 1.6594 0.3634 1.2646 -0.0481 -0.1601 0.0671  100 MET   M CG  
22060 S  SD  . MET   M  113 ? 1.7363 0.2448 1.3408 -0.0407 -0.2265 0.1563  100 MET   M SD  
22061 C  CE  . MET   M  113 ? 1.8042 0.2693 1.4068 -0.0409 -0.1786 0.0493  100 MET   M CE  
22062 N  N   . TYR   M  114 ? 1.5224 0.4161 1.1607 -0.1357 -0.1399 -0.0275 101 TYR   M N   
22063 C  CA  . TYR   M  114 ? 1.5071 0.4502 1.1512 -0.0973 -0.1447 0.0199  101 TYR   M CA  
22064 C  C   . TYR   M  114 ? 1.4943 0.4760 1.1548 -0.0777 -0.1541 0.0649  101 TYR   M C   
22065 O  O   . TYR   M  114 ? 1.5117 0.4668 1.1901 -0.1045 -0.1317 0.0379  101 TYR   M O   
22066 C  CB  . TYR   M  114 ? 1.4958 0.4216 1.1637 -0.0743 -0.1150 0.0333  101 TYR   M CB  
22067 C  CG  . TYR   M  114 ? 1.4983 0.5055 1.1614 -0.0609 -0.1248 0.0552  101 TYR   M CG  
22068 C  CD1 . TYR   M  114 ? 1.5198 0.5682 1.1377 -0.0725 -0.1330 0.0049  101 TYR   M CD1 
22069 C  CD2 . TYR   M  114 ? 1.4800 0.4676 1.1691 -0.0406 -0.1184 0.0351  101 TYR   M CD2 
22070 C  CE1 . TYR   M  114 ? 1.5233 0.6379 1.1231 -0.0689 -0.1030 0.0418  101 TYR   M CE1 
22071 C  CE2 . TYR   M  114 ? 1.4791 0.5324 1.1638 -0.0153 -0.0971 0.0490  101 TYR   M CE2 
22072 C  CZ  . TYR   M  114 ? 1.4984 0.5701 1.1672 -0.0420 -0.0704 0.0148  101 TYR   M CZ  
22073 O  OH  . TYR   M  114 ? 1.4591 0.6606 1.1643 -0.0230 -0.0329 0.0195  101 TYR   M OH  
22074 N  N   . GLN   M  115 ? 1.5014 0.4755 1.1172 -0.0117 -0.2048 0.0597  102 GLN   M N   
22075 C  CA  . GLN   M  115 ? 1.5091 0.5025 1.1658 -0.0047 -0.2086 0.1079  102 GLN   M CA  
22076 C  C   . GLN   M  115 ? 1.5537 0.4035 1.1697 0.0155  -0.2366 0.1104  102 GLN   M C   
22077 O  O   . GLN   M  115 ? 1.5549 0.4316 1.1829 0.0362  -0.2404 0.1514  102 GLN   M O   
22078 C  CB  . GLN   M  115 ? 1.5889 0.5460 1.1967 0.0182  -0.2136 0.0714  102 GLN   M CB  
22079 C  CG  . GLN   M  115 ? 1.6170 0.6667 1.2892 0.0388  -0.2350 0.1470  102 GLN   M CG  
22080 C  CD  . GLN   M  115 ? 1.7152 0.6974 1.3528 -0.0351 -0.2507 0.1245  102 GLN   M CD  
22081 O  OE1 . GLN   M  115 ? 1.7904 0.6196 1.5600 -0.0549 -0.2040 0.1750  102 GLN   M OE1 
22082 N  NE2 . GLN   M  115 ? 1.7354 0.8898 1.3678 -0.0678 -0.2762 0.1603  102 GLN   M NE2 
22083 N  N   . ARG   M  116 ? 1.4811 0.2971 1.1824 0.0541  -0.2212 0.0841  103 ARG   M N   
22084 C  CA  . ARG   M  116 ? 1.4863 0.2944 1.2045 0.0635  -0.2074 0.0970  103 ARG   M CA  
22085 C  C   . ARG   M  116 ? 1.4835 0.3010 1.1748 0.0624  -0.1951 0.1072  103 ARG   M C   
22086 O  O   . ARG   M  116 ? 1.4847 0.2286 1.1610 0.0642  -0.1821 0.1338  103 ARG   M O   
22087 C  CB  . ARG   M  116 ? 1.4841 0.2277 1.1889 0.0751  -0.2018 0.0509  103 ARG   M CB  
22088 C  CG  . ARG   M  116 ? 1.4698 0.1182 1.2872 0.1373  -0.1901 0.0566  103 ARG   M CG  
22089 C  CD  . ARG   M  116 ? 1.4284 0.1132 1.2947 0.1829  -0.2155 -0.0057 103 ARG   M CD  
22090 N  NE  . ARG   M  116 ? 1.4036 0.1469 1.2992 0.1818  -0.2456 -0.0326 103 ARG   M NE  
22091 C  CZ  . ARG   M  116 ? 1.4095 0.2075 1.2848 0.1873  -0.2427 -0.0821 103 ARG   M CZ  
22092 N  NH1 . ARG   M  116 ? 1.3955 0.1795 1.3377 0.2295  -0.2190 -0.0824 103 ARG   M NH1 
22093 N  NH2 . ARG   M  116 ? 1.3805 0.3394 1.3187 0.2119  -0.2746 -0.0297 103 ARG   M NH2 
22094 N  N   . ARG   M  117 ? 1.4765 0.3029 1.1790 0.0599  -0.2026 0.1374  104 ARG   M N   
22095 C  CA  . ARG   M  117 ? 1.4914 0.3740 1.1619 0.0808  -0.1782 0.1119  104 ARG   M CA  
22096 C  C   . ARG   M  117 ? 1.5146 0.4179 1.1744 0.0493  -0.1493 0.1108  104 ARG   M C   
22097 O  O   . ARG   M  117 ? 1.5069 0.3580 1.2047 0.1032  -0.1505 0.1813  104 ARG   M O   
22098 C  CB  . ARG   M  117 ? 1.4376 0.4991 1.1700 0.0815  -0.1757 0.1360  104 ARG   M CB  
22099 C  CG  . ARG   M  117 ? 1.4193 0.5098 1.1923 0.0732  -0.1816 0.1269  104 ARG   M CG  
22100 C  CD  . ARG   M  117 ? 1.4394 0.4832 1.2140 0.0573  -0.1676 0.1192  104 ARG   M CD  
22101 N  NE  . ARG   M  117 ? 1.4820 0.4633 1.2585 0.0520  -0.1683 0.1541  104 ARG   M NE  
22102 C  CZ  . ARG   M  117 ? 1.5440 0.4373 1.2734 0.0610  -0.2142 0.1693  104 ARG   M CZ  
22103 N  NH1 . ARG   M  117 ? 1.5670 0.4634 1.3140 0.0473  -0.2328 0.0898  104 ARG   M NH1 
22104 N  NH2 . ARG   M  117 ? 1.5948 0.4018 1.3502 0.0819  -0.1903 0.2096  104 ARG   M NH2 
22105 N  N   . SER   M  118 ? 1.5084 0.3887 1.2178 0.0520  -0.1463 0.0495  105 SER   M N   
22106 C  CA  . SER   M  118 ? 1.5419 0.4138 1.2085 0.0030  -0.1238 0.0303  105 SER   M CA  
22107 C  C   . SER   M  118 ? 1.5571 0.4479 1.2350 -0.0284 -0.1191 -0.0028 105 SER   M C   
22108 O  O   . SER   M  118 ? 1.6204 0.4159 1.2151 -0.0598 -0.0984 -0.1084 105 SER   M O   
22109 C  CB  . SER   M  118 ? 1.5979 0.3585 1.2351 0.0039  -0.1214 0.0290  105 SER   M CB  
22110 O  OG  . SER   M  118 ? 1.6189 0.4004 1.2154 -0.0245 -0.1262 -0.0034 105 SER   M OG  
22111 N  N   . LYS   M  119 ? 1.5352 0.5513 1.2319 -0.0502 -0.1070 -0.0112 106 LYS   M N   
22112 C  CA  . LYS   M  119 ? 1.5190 0.6013 1.2293 -0.0394 -0.1268 -0.0373 106 LYS   M CA  
22113 C  C   . LYS   M  119 ? 1.4375 0.6403 1.2246 -0.0384 -0.1476 -0.0293 106 LYS   M C   
22114 O  O   . LYS   M  119 ? 1.4289 0.6043 1.1848 -0.0287 -0.1544 -0.0141 106 LYS   M O   
22115 C  CB  . LYS   M  119 ? 1.5330 0.7941 1.2451 -0.0842 -0.1039 -0.1377 106 LYS   M CB  
22116 C  CG  . LYS   M  119 ? 1.5770 0.8216 1.2825 -0.0358 -0.1060 -0.1653 106 LYS   M CG  
22117 C  CD  . LYS   M  119 ? 1.6330 0.9747 1.3487 -0.0362 -0.0682 -0.2553 106 LYS   M CD  
22118 C  CE  . LYS   M  119 ? 1.6620 1.0979 1.4158 -0.0708 -0.0808 -0.3319 106 LYS   M CE  
22119 N  NZ  . LYS   M  119 ? 1.6848 1.1718 1.4348 -0.0617 -0.0806 -0.3679 106 LYS   M NZ  
22120 N  N   . MET   M  120 ? 1.4846 0.5908 1.2487 0.0095  -0.1462 -0.0214 107 MET   M N   
22121 C  CA  . MET   M  120 ? 1.5126 0.5938 1.2374 0.0164  -0.1400 0.0179  107 MET   M CA  
22122 C  C   . MET   M  120 ? 1.4863 0.4912 1.2511 0.0377  -0.1483 0.0091  107 MET   M C   
22123 O  O   . MET   M  120 ? 1.4592 0.6177 1.3190 0.0577  -0.2067 0.0054  107 MET   M O   
22124 C  CB  . MET   M  120 ? 1.5405 0.6215 1.2777 0.0338  -0.1011 0.0275  107 MET   M CB  
22125 C  CG  . MET   M  120 ? 1.6028 0.6793 1.2519 0.0464  -0.0858 -0.0020 107 MET   M CG  
22126 S  SD  . MET   M  120 ? 1.6122 0.7142 1.3101 0.0278  -0.1029 -0.1169 107 MET   M SD  
22127 C  CE  . MET   M  120 ? 1.5825 0.8624 1.3954 0.0754  -0.0711 -0.0539 107 MET   M CE  
22128 N  N   . ASN   M  121 ? 1.5182 0.4341 1.2160 0.0072  -0.1422 0.0349  108 ASN   M N   
22129 C  CA  . ASN   M  121 ? 1.5253 0.4410 1.2011 0.0311  -0.1247 0.0618  108 ASN   M CA  
22130 C  C   . ASN   M  121 ? 1.5187 0.3777 1.2084 0.0081  -0.1177 0.0305  108 ASN   M C   
22131 O  O   . ASN   M  121 ? 1.4614 0.4047 1.1904 0.0201  -0.1030 0.0247  108 ASN   M O   
22132 C  CB  . ASN   M  121 ? 1.5547 0.4483 1.2013 0.0281  -0.1564 0.0552  108 ASN   M CB  
22133 C  CG  . ASN   M  121 ? 1.5848 0.5808 1.2313 0.0457  -0.1893 0.0122  108 ASN   M CG  
22134 O  OD1 . ASN   M  121 ? 1.6283 0.4699 1.2082 0.1260  -0.1720 0.1103  108 ASN   M OD1 
22135 N  ND2 . ASN   M  121 ? 1.6256 0.4750 1.2842 -0.0110 -0.1968 -0.0602 108 ASN   M ND2 
22136 N  N   . PRO   M  122 ? 1.5173 0.4648 1.2109 -0.0621 -0.0760 0.0560  109 PRO   M N   
22137 C  CA  . PRO   M  122 ? 1.5307 0.4204 1.1896 -0.1117 -0.0774 0.0762  109 PRO   M CA  
22138 C  C   . PRO   M  122 ? 1.5095 0.4100 1.1772 -0.1257 -0.0227 0.0687  109 PRO   M C   
22139 O  O   . PRO   M  122 ? 1.4593 0.5791 1.2222 -0.2154 -0.0531 0.1216  109 PRO   M O   
22140 C  CB  . PRO   M  122 ? 1.5239 0.4346 1.1617 -0.1248 -0.0806 0.0767  109 PRO   M CB  
22141 C  CG  . PRO   M  122 ? 1.5617 0.3838 1.1889 -0.1212 -0.0554 0.0379  109 PRO   M CG  
22142 C  CD  . PRO   M  122 ? 1.5330 0.4271 1.2040 -0.1245 -0.0542 0.0421  109 PRO   M CD  
22143 N  N   . LEU   M  123 ? 1.5169 0.2981 1.2360 -0.0853 -0.0297 0.0363  110 LEU   M N   
22144 C  CA  . LEU   M  123 ? 1.4625 0.4450 1.2133 -0.0588 -0.0700 0.0025  110 LEU   M CA  
22145 C  C   . LEU   M  123 ? 1.3986 0.4594 1.2165 -0.0614 -0.1063 0.0249  110 LEU   M C   
22146 O  O   . LEU   M  123 ? 1.3636 0.6722 1.3029 -0.1014 -0.0614 -0.0039 110 LEU   M O   
22147 C  CB  . LEU   M  123 ? 1.4125 0.4488 1.2454 -0.0377 -0.0850 0.0333  110 LEU   M CB  
22148 C  CG  . LEU   M  123 ? 1.3605 0.4389 1.2433 -0.0137 -0.0981 0.0263  110 LEU   M CG  
22149 C  CD1 . LEU   M  123 ? 1.3481 0.4227 1.2271 -0.0240 -0.1141 0.0122  110 LEU   M CD1 
22150 C  CD2 . LEU   M  123 ? 1.3614 0.4191 1.2597 -0.0401 -0.0970 0.0089  110 LEU   M CD2 
22151 N  N   . TRP   M  124 ? 1.4614 0.4553 1.1733 -0.0521 -0.1224 0.0533  111 TRP   M N   
22152 C  CA  . TRP   M  124 ? 1.4732 0.4384 1.1303 0.0099  -0.1666 0.0392  111 TRP   M CA  
22153 C  C   . TRP   M  124 ? 1.3994 0.3738 1.1677 0.0212  -0.1742 0.0093  111 TRP   M C   
22154 O  O   . TRP   M  124 ? 1.4184 0.2203 1.1441 -0.0711 -0.1220 -0.0025 111 TRP   M O   
22155 C  CB  . TRP   M  124 ? 1.4869 0.4698 1.1120 0.0234  -0.1785 0.0232  111 TRP   M CB  
22156 C  CG  . TRP   M  124 ? 1.5366 0.4787 1.0497 -0.0241 -0.2057 0.0288  111 TRP   M CG  
22157 C  CD1 . TRP   M  124 ? 1.5331 0.4548 1.0473 -0.0435 -0.2127 -0.0179 111 TRP   M CD1 
22158 C  CD2 . TRP   M  124 ? 1.5747 0.4497 1.0266 -0.0077 -0.2347 0.0146  111 TRP   M CD2 
22159 N  NE1 . TRP   M  124 ? 1.5359 0.4529 1.0370 -0.0512 -0.2158 -0.0134 111 TRP   M NE1 
22160 C  CE2 . TRP   M  124 ? 1.5619 0.4527 1.0191 -0.0244 -0.2296 0.0148  111 TRP   M CE2 
22161 C  CE3 . TRP   M  124 ? 1.5729 0.5098 1.0475 -0.0142 -0.2196 0.0278  111 TRP   M CE3 
22162 C  CZ2 . TRP   M  124 ? 1.6006 0.4765 1.0210 -0.0211 -0.2389 -0.0015 111 TRP   M CZ2 
22163 C  CZ3 . TRP   M  124 ? 1.5833 0.4420 1.0969 -0.0039 -0.2156 -0.0035 111 TRP   M CZ3 
22164 C  CH2 . TRP   M  124 ? 1.5869 0.4535 1.0515 -0.0119 -0.2193 -0.0163 111 TRP   M CH2 
22165 N  N   . ASN   M  125 ? 1.4312 0.3217 1.1486 0.0503  -0.2377 0.0263  112 ASN   M N   
22166 C  CA  . ASN   M  125 ? 1.4380 0.3296 1.1397 0.0687  -0.2478 0.0588  112 ASN   M CA  
22167 C  C   . ASN   M  125 ? 1.4574 0.2598 1.1454 0.0440  -0.2371 0.0451  112 ASN   M C   
22168 O  O   . ASN   M  125 ? 1.5320 0.2534 1.1158 0.0012  -0.2549 -0.0082 112 ASN   M O   
22169 C  CB  . ASN   M  125 ? 1.4638 0.3823 1.1650 0.1231  -0.2556 0.0247  112 ASN   M CB  
22170 C  CG  . ASN   M  125 ? 1.4524 0.3993 1.2367 0.1514  -0.2890 0.0549  112 ASN   M CG  
22171 O  OD1 . ASN   M  125 ? 1.4962 0.3521 1.2629 0.1817  -0.2840 0.0705  112 ASN   M OD1 
22172 N  ND2 . ASN   M  125 ? 1.4833 0.4703 1.2679 0.1719  -0.2939 0.0939  112 ASN   M ND2 
22173 N  N   . ALA   M  126 ? 1.4362 0.3137 1.0979 0.0778  -0.2327 0.0735  113 ALA   M N   
22174 C  CA  . ALA   M  126 ? 1.4337 0.4603 1.1291 0.0925  -0.2436 0.0647  113 ALA   M CA  
22175 C  C   . ALA   M  126 ? 1.4416 0.5113 1.1242 0.0552  -0.2588 0.0267  113 ALA   M C   
22176 O  O   . ALA   M  126 ? 1.4461 0.5841 1.1823 0.0560  -0.3493 0.0033  113 ALA   M O   
22177 C  CB  . ALA   M  126 ? 1.4559 0.4595 1.1479 0.1022  -0.2397 0.0266  113 ALA   M CB  
22178 N  N   . ILE   M  127 ? 1.4261 0.5052 1.1233 0.0319  -0.2637 0.0503  114 ILE   M N   
22179 C  CA  . ILE   M  127 ? 1.4294 0.6624 1.1247 0.0196  -0.2256 -0.0042 114 ILE   M CA  
22180 C  C   . ILE   M  127 ? 1.4281 0.5792 1.1532 0.0102  -0.1363 -0.0069 114 ILE   M C   
22181 O  O   . ILE   M  127 ? 1.3978 0.4700 1.1763 0.0244  -0.1429 -0.0270 114 ILE   M O   
22182 C  CB  . ILE   M  127 ? 1.3981 0.7241 1.1133 -0.0358 -0.2385 -0.0037 114 ILE   M CB  
22183 C  CG1 . ILE   M  127 ? 1.4025 0.8855 1.1041 -0.0411 -0.2812 -0.0082 114 ILE   M CG1 
22184 C  CG2 . ILE   M  127 ? 1.3997 0.8426 1.0499 -0.0108 -0.2489 -0.0374 114 ILE   M CG2 
22185 C  CD1 . ILE   M  127 ? 1.3785 0.8933 1.1295 -0.0732 -0.2753 -0.0254 114 ILE   M CD1 
22186 N  N   . ILE   M  128 ? 1.4808 0.6349 1.1483 0.0162  -0.1191 -0.0205 115 ILE   M N   
22187 C  CA  . ILE   M  128 ? 1.4819 0.6244 1.2385 -0.0243 -0.1335 0.0053  115 ILE   M CA  
22188 C  C   . ILE   M  128 ? 1.5013 0.5699 1.2672 -0.0661 -0.1906 -0.0025 115 ILE   M C   
22189 O  O   . ILE   M  128 ? 1.4605 0.4469 1.3223 -0.1104 -0.2227 -0.0915 115 ILE   M O   
22190 C  CB  . ILE   M  128 ? 1.5331 0.5894 1.3268 -0.0239 -0.1041 -0.0103 115 ILE   M CB  
22191 C  CG1 . ILE   M  128 ? 1.5210 0.6999 1.3274 0.0242  -0.0516 -0.0509 115 ILE   M CG1 
22192 C  CG2 . ILE   M  128 ? 1.5290 0.5104 1.3644 -0.0375 -0.0987 0.0173  115 ILE   M CG2 
22193 C  CD1 . ILE   M  128 ? 1.5290 0.7599 1.3733 0.0251  -0.0275 0.0050  115 ILE   M CD1 
22194 N  N   . VAL   M  129 ? 1.5014 0.5097 1.2314 -0.1244 -0.1884 0.0365  116 VAL   M N   
22195 C  CA  . VAL   M  129 ? 1.4915 0.5896 1.2480 -0.1301 -0.1597 -0.0105 116 VAL   M CA  
22196 C  C   . VAL   M  129 ? 1.4991 0.5766 1.2496 -0.1466 -0.1712 0.0729  116 VAL   M C   
22197 O  O   . VAL   M  129 ? 1.4385 0.5666 1.2992 -0.1331 -0.1663 0.1766  116 VAL   M O   
22198 C  CB  . VAL   M  129 ? 1.5504 0.5816 1.2560 -0.1053 -0.1489 -0.0277 116 VAL   M CB  
22199 C  CG1 . VAL   M  129 ? 1.5401 0.6560 1.2811 -0.0939 -0.1283 -0.0842 116 VAL   M CG1 
22200 C  CG2 . VAL   M  129 ? 1.5573 0.6334 1.2801 -0.1310 -0.1539 -0.0639 116 VAL   M CG2 
22201 N  N   . ALA   M  130 ? 1.5156 0.6332 1.2317 -0.1271 -0.1945 0.0254  117 ALA   M N   
22202 C  CA  . ALA   M  130 ? 1.4870 0.6202 1.3497 -0.0892 -0.1819 0.0131  117 ALA   M CA  
22203 C  C   . ALA   M  130 ? 1.4838 0.5540 1.4609 -0.0432 -0.1644 0.0576  117 ALA   M C   
22204 O  O   . ALA   M  130 ? 1.4541 0.4259 1.6488 -0.0819 -0.1819 0.0664  117 ALA   M O   
22205 C  CB  . ALA   M  130 ? 1.5278 0.6034 1.3622 -0.1055 -0.1805 0.0072  117 ALA   M CB  
22206 N  N   . GLY   M  131 ? 1.4899 0.5007 1.4258 -0.0447 -0.1511 0.0944  118 GLY   M N   
22207 C  CA  . GLY   M  131 ? 1.5271 0.4991 1.4449 -0.0541 -0.1034 0.0921  118 GLY   M CA  
22208 C  C   . GLY   M  131 ? 1.5237 0.4977 1.4618 -0.0528 -0.0883 0.0921  118 GLY   M C   
22209 O  O   . GLY   M  131 ? 1.5083 0.4884 1.3978 -0.0669 -0.0803 0.1373  118 GLY   M O   
22210 N  N   . VAL   M  132 ? 1.5281 0.5916 1.5170 0.0028  -0.0585 0.0634  119 VAL   M N   
22211 C  CA  . VAL   M  132 ? 1.5284 0.6807 1.5396 0.0354  -0.0054 0.0386  119 VAL   M CA  
22212 C  C   . VAL   M  132 ? 1.5489 0.7017 1.5730 0.0739  0.0106  0.0710  119 VAL   M C   
22213 O  O   . VAL   M  132 ? 1.5242 0.6244 1.5729 0.0828  0.0626  0.0800  119 VAL   M O   
22214 C  CB  . VAL   M  132 ? 1.5752 0.6658 1.5286 0.0466  0.0133  -0.0065 119 VAL   M CB  
22215 C  CG1 . VAL   M  132 ? 1.5706 0.7535 1.5529 0.0587  0.0317  -0.0349 119 VAL   M CG1 
22216 C  CG2 . VAL   M  132 ? 1.5822 0.6700 1.5150 0.0683  0.0113  0.0076  119 VAL   M CG2 
22217 N  N   . GLN   M  133 ? 1.5761 0.7712 1.6044 0.1056  -0.0028 0.0989  120 GLN   M N   
22218 C  CA  . GLN   M  133 ? 1.6045 0.7669 1.6692 0.1163  -0.0087 0.1046  120 GLN   M CA  
22219 C  C   . GLN   M  133 ? 1.6302 0.9225 1.7003 0.1233  0.0706  0.0993  120 GLN   M C   
22220 O  O   . GLN   M  133 ? 1.7242 0.9412 1.7201 0.1679  0.0820  0.1640  120 GLN   M O   
22221 C  CB  . GLN   M  133 ? 1.5899 0.7295 1.6956 0.1099  -0.0347 0.1126  120 GLN   M CB  
22222 C  CG  . GLN   M  133 ? 1.5216 0.6746 1.6565 0.0993  -0.0595 0.1633  120 GLN   M CG  
22223 C  CD  . GLN   M  133 ? 1.5635 0.4197 1.6020 0.1151  -0.1149 0.1936  120 GLN   M CD  
22224 O  OE1 . GLN   M  133 ? 1.5051 0.3317 1.6515 0.0235  -0.1214 0.1250  120 GLN   M OE1 
22225 N  NE2 . GLN   M  133 ? 1.5782 0.2782 1.6414 0.0624  -0.0933 0.1532  120 GLN   M NE2 
22226 N  N   . SER   M  134 ? 1.5991 0.9164 1.7600 0.1078  0.0781  0.0835  121 SER   M N   
22227 C  CA  . SER   M  134 ? 1.5262 1.0094 1.7161 0.0785  0.0633  0.0251  121 SER   M CA  
22228 C  C   . SER   M  134 ? 1.5120 0.9734 1.6933 0.1121  0.1028  0.0643  121 SER   M C   
22229 O  O   . SER   M  134 ? 1.5324 1.0397 1.7010 0.0987  0.1386  0.0772  121 SER   M O   
22230 C  CB  . SER   M  134 ? 1.5050 1.0250 1.7030 0.0368  0.0298  0.0093  121 SER   M CB  
22231 O  OG  . SER   M  134 ? 1.4957 1.1713 1.7337 0.0187  0.0001  0.0345  121 SER   M OG  
22232 N  N   . ASN   M  135 ? 1.4245 0.9219 1.7554 0.1215  0.0417  0.0863  122 ASN   M N   
22233 C  CA  . ASN   M  135 ? 1.4426 0.9394 1.7467 0.1049  -0.0034 0.0501  122 ASN   M CA  
22234 C  C   . ASN   M  135 ? 1.4405 0.9163 1.8185 0.0899  0.0325  0.0189  122 ASN   M C   
22235 O  O   . ASN   M  135 ? 1.4101 0.8800 1.8612 0.1041  0.0798  0.0416  122 ASN   M O   
22236 C  CB  . ASN   M  135 ? 1.4307 0.9661 1.7686 0.1301  -0.0609 0.0212  122 ASN   M CB  
22237 C  CG  . ASN   M  135 ? 1.3869 0.9822 1.7027 0.2096  -0.1366 0.0550  122 ASN   M CG  
22238 O  OD1 . ASN   M  135 ? 1.3761 1.0048 1.6435 0.2033  -0.1583 0.0157  122 ASN   M OD1 
22239 N  ND2 . ASN   M  135 ? 1.4147 1.0729 1.7043 0.2369  -0.1487 0.0609  122 ASN   M ND2 
22240 N  N   . GLY   M  136 ? 1.4183 0.9114 1.7894 0.0544  0.0143  -0.0063 123 GLY   M N   
22241 C  CA  . GLY   M  136 ? 1.4432 0.9621 1.7799 0.0097  0.0213  0.0190  123 GLY   M CA  
22242 C  C   . GLY   M  136 ? 1.4512 0.9421 1.8212 -0.0270 -0.0313 -0.0066 123 GLY   M C   
22243 O  O   . GLY   M  136 ? 1.3402 0.9212 1.8148 -0.1026 -0.0406 -0.0176 123 GLY   M O   
22244 N  N   . ASP   M  137 ? 1.4980 0.9605 1.8245 -0.0309 -0.0633 0.0275  124 ASP   M N   
22245 C  CA  . ASP   M  137 ? 1.5145 0.9258 1.8298 0.0007  -0.0930 0.0421  124 ASP   M CA  
22246 C  C   . ASP   M  137 ? 1.5328 0.8754 1.7426 -0.0055 -0.1135 0.0288  124 ASP   M C   
22247 O  O   . ASP   M  137 ? 1.5718 0.7478 1.7551 0.0091  -0.1058 0.0095  124 ASP   M O   
22248 C  CB  . ASP   M  137 ? 1.5957 0.9601 1.8533 -0.0233 -0.0755 0.0727  124 ASP   M CB  
22249 C  CG  . ASP   M  137 ? 1.6397 1.0764 1.9638 -0.0033 -0.1250 0.0897  124 ASP   M CG  
22250 O  OD1 . ASP   M  137 ? 1.7732 1.1729 2.0258 -0.0392 -0.0384 0.1560  124 ASP   M OD1 
22251 O  OD2 . ASP   M  137 ? 1.7472 1.0757 2.0102 -0.0885 -0.0479 0.1250  124 ASP   M OD2 
22252 N  N   . GLN   M  138 ? 1.5094 0.8662 1.6449 0.0315  -0.1436 0.0855  125 GLN   M N   
22253 C  CA  . GLN   M  138 ? 1.5107 0.7575 1.4881 0.0036  -0.1243 0.0875  125 GLN   M CA  
22254 C  C   . GLN   M  138 ? 1.5010 0.6734 1.4064 0.0261  -0.1639 0.0804  125 GLN   M C   
22255 O  O   . GLN   M  138 ? 1.5465 0.6501 1.3653 0.0342  -0.1270 0.0771  125 GLN   M O   
22256 C  CB  . GLN   M  138 ? 1.4648 0.7544 1.4703 0.0085  -0.1267 0.0702  125 GLN   M CB  
22257 C  CG  . GLN   M  138 ? 1.4397 0.7676 1.5139 -0.0181 -0.1172 0.0875  125 GLN   M CG  
22258 C  CD  . GLN   M  138 ? 1.4289 0.7710 1.5347 -0.0292 -0.1064 0.1106  125 GLN   M CD  
22259 O  OE1 . GLN   M  138 ? 1.3865 0.7630 1.5415 -0.1105 -0.1079 0.1599  125 GLN   M OE1 
22260 N  NE2 . GLN   M  138 ? 1.4376 0.7462 1.5810 -0.0251 -0.0851 0.0903  125 GLN   M NE2 
22261 N  N   . PHE   M  139 ? 1.5053 0.6283 1.3857 -0.0032 -0.1465 0.0894  126 PHE   M N   
22262 C  CA  . PHE   M  139 ? 1.5539 0.6457 1.3674 -0.0401 -0.1397 0.0612  126 PHE   M CA  
22263 C  C   . PHE   M  139 ? 1.5835 0.5387 1.3976 -0.0705 -0.0909 0.0312  126 PHE   M C   
22264 O  O   . PHE   M  139 ? 1.6112 0.5333 1.3727 -0.1111 -0.0642 0.0292  126 PHE   M O   
22265 C  CB  . PHE   M  139 ? 1.6141 0.6743 1.4095 -0.0782 -0.1612 0.0399  126 PHE   M CB  
22266 C  CG  . PHE   M  139 ? 1.6369 0.7261 1.3800 -0.0693 -0.1653 -0.0014 126 PHE   M CG  
22267 C  CD1 . PHE   M  139 ? 1.6617 0.6676 1.3821 -0.0241 -0.1711 -0.0278 126 PHE   M CD1 
22268 C  CD2 . PHE   M  139 ? 1.6692 0.7779 1.4248 -0.0903 -0.2442 -0.0071 126 PHE   M CD2 
22269 C  CE1 . PHE   M  139 ? 1.6171 0.6531 1.4300 -0.0117 -0.1658 -0.0406 126 PHE   M CE1 
22270 C  CE2 . PHE   M  139 ? 1.6140 0.7429 1.4579 -0.0723 -0.2466 -0.0064 126 PHE   M CE2 
22271 C  CZ  . PHE   M  139 ? 1.6258 0.6608 1.4739 -0.0371 -0.2217 -0.0279 126 PHE   M CZ  
22272 N  N   . LEU   M  140 ? 1.5414 0.5689 1.3318 -0.0459 -0.1248 0.0550  127 LEU   M N   
22273 C  CA  . LEU   M  140 ? 1.5692 0.6238 1.2868 0.0035  -0.1402 0.0636  127 LEU   M CA  
22274 C  C   . LEU   M  140 ? 1.5078 0.5744 1.2478 0.0508  -0.1858 0.1070  127 LEU   M C   
22275 O  O   . LEU   M  140 ? 1.4649 0.6389 1.2464 0.1390  -0.2211 0.1136  127 LEU   M O   
22276 C  CB  . LEU   M  140 ? 1.6273 0.6146 1.3587 0.0025  -0.1299 0.0703  127 LEU   M CB  
22277 C  CG  . LEU   M  140 ? 1.6935 0.5891 1.3522 0.0018  -0.1727 0.0721  127 LEU   M CG  
22278 C  CD1 . LEU   M  140 ? 1.7181 0.5706 1.3531 -0.0003 -0.1891 0.0904  127 LEU   M CD1 
22279 C  CD2 . LEU   M  140 ? 1.7047 0.6120 1.3935 -0.0228 -0.1767 0.0503  127 LEU   M CD2 
22280 N  N   . ARG   M  141 ? 1.5085 0.4937 1.1391 0.0518  -0.1956 0.1189  128 ARG   M N   
22281 C  CA  . ARG   M  141 ? 1.4895 0.5231 1.1430 0.0461  -0.1954 0.1089  128 ARG   M CA  
22282 C  C   . ARG   M  141 ? 1.4777 0.4170 1.0858 0.0221  -0.2286 0.1125  128 ARG   M C   
22283 O  O   . ARG   M  141 ? 1.4342 0.3750 1.1457 -0.0420 -0.2363 0.1352  128 ARG   M O   
22284 C  CB  . ARG   M  141 ? 1.5495 0.5378 1.1722 0.0716  -0.1746 0.1237  128 ARG   M CB  
22285 C  CG  . ARG   M  141 ? 1.5785 0.6291 1.1757 0.0966  -0.1836 0.1309  128 ARG   M CG  
22286 C  CD  . ARG   M  141 ? 1.5549 0.6753 1.2646 0.1315  -0.2202 0.1596  128 ARG   M CD  
22287 N  NE  . ARG   M  141 ? 1.5607 0.6896 1.2562 0.1153  -0.2571 0.1524  128 ARG   M NE  
22288 C  CZ  . ARG   M  141 ? 1.5713 0.6134 1.2588 0.1023  -0.2489 0.1698  128 ARG   M CZ  
22289 N  NH1 . ARG   M  141 ? 1.5697 0.5397 1.3502 0.0921  -0.2607 0.1427  128 ARG   M NH1 
22290 N  NH2 . ARG   M  141 ? 1.5909 0.6133 1.2469 0.1090  -0.2478 0.2089  128 ARG   M NH2 
22291 N  N   . TYR   M  142 ? 1.4339 0.4010 1.1098 0.0577  -0.2262 0.1236  129 TYR   M N   
22292 C  CA  . TYR   M  142 ? 1.4234 0.4625 1.1496 0.0527  -0.2123 0.0967  129 TYR   M CA  
22293 C  C   . TYR   M  142 ? 1.4104 0.3164 1.1871 0.0300  -0.2502 0.0893  129 TYR   M C   
22294 O  O   . TYR   M  142 ? 1.3834 0.3403 1.2704 0.0616  -0.2531 0.1402  129 TYR   M O   
22295 C  CB  . TYR   M  142 ? 1.4396 0.5002 1.1949 0.0720  -0.1785 0.0255  129 TYR   M CB  
22296 C  CG  . TYR   M  142 ? 1.4648 0.5307 1.1781 0.0846  -0.1571 -0.0082 129 TYR   M CG  
22297 C  CD1 . TYR   M  142 ? 1.4435 0.5643 1.1884 0.0934  -0.1433 -0.0056 129 TYR   M CD1 
22298 C  CD2 . TYR   M  142 ? 1.4460 0.4979 1.1713 0.0949  -0.1487 -0.0337 129 TYR   M CD2 
22299 C  CE1 . TYR   M  142 ? 1.4189 0.5914 1.2019 0.0750  -0.1259 -0.0052 129 TYR   M CE1 
22300 C  CE2 . TYR   M  142 ? 1.4310 0.5854 1.1962 0.0858  -0.1181 -0.0474 129 TYR   M CE2 
22301 C  CZ  . TYR   M  142 ? 1.4017 0.5961 1.2172 0.0973  -0.1098 -0.0097 129 TYR   M CZ  
22302 O  OH  . TYR   M  142 ? 1.3906 0.7750 1.2603 0.0705  -0.0049 -0.0694 129 TYR   M OH  
22303 N  N   . VAL   M  143 ? 1.4176 0.2580 1.1461 0.0128  -0.2654 0.0614  130 VAL   M N   
22304 C  CA  . VAL   M  143 ? 1.4392 0.4025 1.1235 0.0215  -0.2350 0.0319  130 VAL   M CA  
22305 C  C   . VAL   M  143 ? 1.4680 0.2606 1.1446 0.0304  -0.2234 -0.0120 130 VAL   M C   
22306 O  O   . VAL   M  143 ? 1.5668 0.2045 1.1342 -0.0204 -0.2025 -0.0106 130 VAL   M O   
22307 C  CB  . VAL   M  143 ? 1.4721 0.4087 1.1303 0.0229  -0.2106 0.0410  130 VAL   M CB  
22308 C  CG1 . VAL   M  143 ? 1.4854 0.4482 1.1185 0.0105  -0.1794 0.0188  130 VAL   M CG1 
22309 C  CG2 . VAL   M  143 ? 1.4694 0.4984 1.1256 0.0412  -0.2070 0.0577  130 VAL   M CG2 
22310 N  N   . ASN   M  144 ? 1.4846 0.2543 1.0894 0.0340  -0.2545 -0.0334 131 ASN   M N   
22311 C  CA  . ASN   M  144 ? 1.4546 0.3610 1.1032 0.0392  -0.2529 -0.0281 131 ASN   M CA  
22312 C  C   . ASN   M  144 ? 1.4034 0.2877 1.1089 0.0333  -0.2933 -0.0291 131 ASN   M C   
22313 O  O   . ASN   M  144 ? 1.3300 0.3634 1.0094 0.0094  -0.3391 0.0035  131 ASN   M O   
22314 C  CB  . ASN   M  144 ? 1.4953 0.3833 1.1100 0.0694  -0.2752 -0.0735 131 ASN   M CB  
22315 C  CG  . ASN   M  144 ? 1.5307 0.4391 1.1015 0.1152  -0.2959 -0.0384 131 ASN   M CG  
22316 O  OD1 . ASN   M  144 ? 1.4916 0.4456 1.0530 0.1597  -0.3186 -0.0511 131 ASN   M OD1 
22317 N  ND2 . ASN   M  144 ? 1.5720 0.4521 1.1508 0.1182  -0.3188 -0.0583 131 ASN   M ND2 
22318 N  N   . LEU   M  145 ? 1.3981 0.2918 1.1413 0.0278  -0.2729 -0.0177 132 LEU   M N   
22319 C  CA  . LEU   M  145 ? 1.4087 0.3111 1.1659 0.0591  -0.2474 0.0094  132 LEU   M CA  
22320 C  C   . LEU   M  145 ? 1.4235 0.3148 1.1718 0.0648  -0.2192 0.0519  132 LEU   M C   
22321 O  O   . LEU   M  145 ? 1.4640 0.3243 1.2209 0.1473  -0.1780 0.1808  132 LEU   M O   
22322 C  CB  . LEU   M  145 ? 1.4123 0.3168 1.2163 0.0594  -0.2688 0.0257  132 LEU   M CB  
22323 C  CG  . LEU   M  145 ? 1.4241 0.3552 1.2081 0.0633  -0.2980 0.0035  132 LEU   M CG  
22324 C  CD1 . LEU   M  145 ? 1.3903 0.4108 1.2662 0.0439  -0.2502 -0.0188 132 LEU   M CD1 
22325 C  CD2 . LEU   M  145 ? 1.3957 0.3715 1.1961 0.0600  -0.3348 -0.0007 132 LEU   M CD2 
22326 N  N   . LEU   M  146 ? 1.4050 0.3937 1.1995 0.0695  -0.2238 0.0182  133 LEU   M N   
22327 C  CA  . LEU   M  146 ? 1.4127 0.4717 1.1901 0.0758  -0.2045 0.0117  133 LEU   M CA  
22328 C  C   . LEU   M  146 ? 1.4020 0.4578 1.1728 0.0649  -0.1949 0.0080  133 LEU   M C   
22329 O  O   . LEU   M  146 ? 1.4314 0.5129 1.1311 0.0456  -0.1320 0.0058  133 LEU   M O   
22330 C  CB  . LEU   M  146 ? 1.4138 0.5244 1.2022 0.0497  -0.2189 -0.0116 133 LEU   M CB  
22331 C  CG  . LEU   M  146 ? 1.4221 0.5679 1.2168 0.0702  -0.2098 -0.0625 133 LEU   M CG  
22332 C  CD1 . LEU   M  146 ? 1.4105 0.7083 1.2291 0.0382  -0.2577 -0.1443 133 LEU   M CD1 
22333 C  CD2 . LEU   M  146 ? 1.4508 0.5187 1.2019 0.0581  -0.2029 -0.0272 133 LEU   M CD2 
22334 N  N   . GLY   M  147 ? 1.3811 0.4531 1.2417 0.0593  -0.1745 -0.0228 134 GLY   M N   
22335 C  CA  . GLY   M  147 ? 1.3766 0.4665 1.2953 0.0619  -0.2070 0.0220  134 GLY   M CA  
22336 C  C   . GLY   M  147 ? 1.3411 0.4583 1.2704 0.1120  -0.2270 0.0292  134 GLY   M C   
22337 O  O   . GLY   M  147 ? 1.2971 0.3815 1.3188 0.0792  -0.2103 0.0200  134 GLY   M O   
22338 N  N   . VAL   M  148 ? 1.4040 0.4760 1.2251 0.0482  -0.2110 0.0213  135 VAL   M N   
22339 C  CA  . VAL   M  148 ? 1.3730 0.5717 1.1797 0.0601  -0.2193 0.0259  135 VAL   M CA  
22340 C  C   . VAL   M  148 ? 1.3644 0.5693 1.2343 0.0942  -0.1863 0.0381  135 VAL   M C   
22341 O  O   . VAL   M  148 ? 1.3761 0.6063 1.2357 0.1246  -0.1292 0.1021  135 VAL   M O   
22342 C  CB  . VAL   M  148 ? 1.4130 0.5584 1.1893 0.0130  -0.2368 0.0303  135 VAL   M CB  
22343 C  CG1 . VAL   M  148 ? 1.3896 0.6005 1.1912 0.0153  -0.2525 0.0458  135 VAL   M CG1 
22344 C  CG2 . VAL   M  148 ? 1.4713 0.6062 1.1796 0.0175  -0.2213 0.0458  135 VAL   M CG2 
22345 N  N   . THR   M  149 ? 1.3771 0.5701 1.1668 0.0712  -0.2618 0.0367  136 THR   M N   
22346 C  CA  . THR   M  149 ? 1.4318 0.5513 1.1455 0.0343  -0.2547 0.0105  136 THR   M CA  
22347 C  C   . THR   M  149 ? 1.5207 0.4487 1.1835 0.0022  -0.2462 0.0372  136 THR   M C   
22348 O  O   . THR   M  149 ? 1.6648 0.3466 1.2226 -0.0173 -0.2973 0.0142  136 THR   M O   
22349 C  CB  . THR   M  149 ? 1.3876 0.5585 1.0996 0.0378  -0.2634 -0.0079 136 THR   M CB  
22350 O  OG1 . THR   M  149 ? 1.3547 0.5434 1.1264 0.0744  -0.2750 -0.0166 136 THR   M OG1 
22351 C  CG2 . THR   M  149 ? 1.3996 0.5656 1.1208 0.0217  -0.2241 -0.0116 136 THR   M CG2 
22352 N  N   . TYR   M  150 ? 1.5241 0.3797 1.1495 -0.0010 -0.2462 0.0012  137 TYR   M N   
22353 C  CA  . TYR   M  150 ? 1.5055 0.4935 1.1604 -0.0122 -0.2337 0.0256  137 TYR   M CA  
22354 C  C   . TYR   M  150 ? 1.4893 0.4391 1.1545 -0.0269 -0.2491 -0.0009 137 TYR   M C   
22355 O  O   . TYR   M  150 ? 1.5111 0.2390 1.1992 -0.1050 -0.2543 -0.0221 137 TYR   M O   
22356 C  CB  . TYR   M  150 ? 1.5325 0.5356 1.1308 0.0086  -0.2402 -0.0121 137 TYR   M CB  
22357 C  CG  . TYR   M  150 ? 1.5694 0.5387 1.1028 0.0345  -0.2229 0.0151  137 TYR   M CG  
22358 C  CD1 . TYR   M  150 ? 1.5824 0.5310 1.1132 0.0339  -0.2150 0.0290  137 TYR   M CD1 
22359 C  CD2 . TYR   M  150 ? 1.6020 0.5705 1.0803 0.0403  -0.2121 -0.0037 137 TYR   M CD2 
22360 C  CE1 . TYR   M  150 ? 1.5934 0.5991 1.0712 0.0268  -0.2305 0.0597  137 TYR   M CE1 
22361 C  CE2 . TYR   M  150 ? 1.6058 0.6212 1.0400 0.0249  -0.2262 0.0193  137 TYR   M CE2 
22362 C  CZ  . TYR   M  150 ? 1.6016 0.6077 1.0522 0.0343  -0.2412 0.0380  137 TYR   M CZ  
22363 O  OH  . TYR   M  150 ? 1.6299 0.5613 1.0822 0.0513  -0.2719 -0.0071 137 TYR   M OH  
22364 N  N   . SER   M  151 ? 1.4852 0.5806 1.2011 -0.0160 -0.2400 0.0219  138 SER   M N   
22365 C  CA  . SER   M  151 ? 1.5330 0.7226 1.1918 -0.0437 -0.2284 0.0143  138 SER   M CA  
22366 C  C   . SER   M  151 ? 1.6048 0.7712 1.2393 -0.1053 -0.2240 0.0183  138 SER   M C   
22367 O  O   . SER   M  151 ? 1.6689 0.7360 1.2822 -0.1692 -0.2415 0.0009  138 SER   M O   
22368 C  CB  . SER   M  151 ? 1.5203 0.7829 1.1246 -0.0055 -0.2042 -0.0049 138 SER   M CB  
22369 O  OG  . SER   M  151 ? 1.5005 0.8897 1.1403 0.0106  -0.2130 -0.0651 138 SER   M OG  
22370 N  N   . SER   M  152 ? 1.5945 0.7504 1.2755 -0.1570 -0.1909 0.0265  139 SER   M N   
22371 C  CA  . SER   M  152 ? 1.5766 0.7514 1.3556 -0.1555 -0.1789 0.0108  139 SER   M CA  
22372 C  C   . SER   M  152 ? 1.5416 0.6749 1.3678 -0.1540 -0.1595 0.0162  139 SER   M C   
22373 O  O   . SER   M  152 ? 1.5829 0.8020 1.3288 -0.1709 -0.1795 0.0226  139 SER   M O   
22374 C  CB  . SER   M  152 ? 1.5589 0.7720 1.4415 -0.1459 -0.1679 0.0301  139 SER   M CB  
22375 O  OG  . SER   M  152 ? 1.5870 0.8396 1.5378 -0.2164 -0.1562 -0.0105 139 SER   M OG  
22376 N  N   . PRO   M  153 ? 1.5103 0.5889 1.3852 -0.1234 -0.1799 0.0187  140 PRO   M N   
22377 C  CA  . PRO   M  153 ? 1.5324 0.6121 1.4210 -0.1423 -0.1114 -0.0183 140 PRO   M CA  
22378 C  C   . PRO   M  153 ? 1.5750 0.6043 1.3846 -0.1059 -0.1031 -0.0644 140 PRO   M C   
22379 O  O   . PRO   M  153 ? 1.6454 0.6276 1.4034 -0.1431 -0.0218 -0.1073 140 PRO   M O   
22380 C  CB  . PRO   M  153 ? 1.4695 0.6818 1.4391 -0.1302 -0.1406 0.0048  140 PRO   M CB  
22381 C  CG  . PRO   M  153 ? 1.4904 0.6522 1.4535 -0.1263 -0.1501 0.0338  140 PRO   M CG  
22382 C  CD  . PRO   M  153 ? 1.4666 0.6074 1.4174 -0.1290 -0.1794 0.0316  140 PRO   M CD  
22383 N  N   . THR   M  154 ? 1.6334 0.6213 1.4115 -0.0655 -0.0774 -0.0434 141 THR   M N   
22384 C  CA  . THR   M  154 ? 1.6322 0.5358 1.3327 -0.0492 -0.0162 0.0062  141 THR   M CA  
22385 C  C   . THR   M  154 ? 1.6064 0.4881 1.2985 -0.0335 -0.0374 0.0119  141 THR   M C   
22386 O  O   . THR   M  154 ? 1.5984 0.5099 1.2443 -0.0479 -0.0269 0.1560  141 THR   M O   
22387 C  CB  . THR   M  154 ? 1.6620 0.5314 1.2937 -0.0355 0.0334  -0.0013 141 THR   M CB  
22388 O  OG1 . THR   M  154 ? 1.6245 0.3078 1.4275 0.0137  0.1251  -0.0250 141 THR   M OG1 
22389 C  CG2 . THR   M  154 ? 1.6799 0.5838 1.3071 -0.0551 0.0372  0.0298  141 THR   M CG2 
22390 N  N   . LEU   M  155 ? 1.5919 0.3887 1.3100 -0.0117 -0.0169 -0.0097 142 LEU   M N   
22391 C  CA  . LEU   M  155 ? 1.5842 0.4374 1.2927 0.0417  -0.0089 -0.0426 142 LEU   M CA  
22392 C  C   . LEU   M  155 ? 1.6147 0.2924 1.2961 0.0245  -0.0204 -0.0390 142 LEU   M C   
22393 O  O   . LEU   M  155 ? 1.5420 0.2139 1.2850 0.0081  -0.0297 -0.0124 142 LEU   M O   
22394 C  CB  . LEU   M  155 ? 1.6192 0.4278 1.3266 0.0484  0.0347  -0.0836 142 LEU   M CB  
22395 C  CG  . LEU   M  155 ? 1.6509 0.5439 1.3419 0.0914  0.0217  -0.1065 142 LEU   M CG  
22396 C  CD1 . LEU   M  155 ? 1.6830 0.5555 1.4121 0.0611  0.0507  -0.0578 142 LEU   M CD1 
22397 C  CD2 . LEU   M  155 ? 1.6662 0.5353 1.4146 0.0894  0.0308  -0.1864 142 LEU   M CD2 
22398 N  N   . ALA   M  156 ? 1.6282 0.2552 1.3003 0.0390  -0.0265 -0.0199 143 ALA   M N   
22399 C  CA  . ALA   M  156 ? 1.6245 0.3728 1.2686 0.0043  -0.0743 -0.0312 143 ALA   M CA  
22400 C  C   . ALA   M  156 ? 1.5920 0.2716 1.2523 -0.0393 -0.0955 -0.0123 143 ALA   M C   
22401 O  O   . ALA   M  156 ? 1.6084 0.1318 1.2609 -0.0386 -0.0517 0.0742  143 ALA   M O   
22402 C  CB  . ALA   M  156 ? 1.6738 0.4247 1.2967 -0.0264 -0.0736 0.0294  143 ALA   M CB  
22403 N  N   . THR   M  157 ? 1.6094 0.3476 1.2187 -0.0598 -0.1167 -0.0638 144 THR   M N   
22404 C  CA  . THR   M  157 ? 1.6361 0.4764 1.2359 -0.0215 -0.1017 -0.1021 144 THR   M CA  
22405 C  C   . THR   M  157 ? 1.6212 0.5352 1.2477 0.0382  -0.1452 -0.2048 144 THR   M C   
22406 O  O   . THR   M  157 ? 1.6803 0.6566 1.2607 0.0367  -0.1140 -0.1894 144 THR   M O   
22407 C  CB  . THR   M  157 ? 1.6430 0.4122 1.2791 0.0099  -0.0581 -0.0856 144 THR   M CB  
22408 O  OG1 . THR   M  157 ? 1.6948 0.3726 1.2336 0.0102  -0.0180 -0.0596 144 THR   M OG1 
22409 C  CG2 . THR   M  157 ? 1.6404 0.4719 1.2465 0.0531  -0.0359 -0.1111 144 THR   M CG2 
22410 N  N   . GLY   M  158 ? 1.5927 0.6462 1.1710 0.0552  -0.1948 -0.2082 145 GLY   M N   
22411 C  CA  . GLY   M  158 ? 1.5354 0.6398 1.2445 0.0231  -0.2072 -0.1862 145 GLY   M CA  
22412 C  C   . GLY   M  158 ? 1.5640 0.6067 1.2782 0.0188  -0.2657 -0.1950 145 GLY   M C   
22413 O  O   . GLY   M  158 ? 1.6168 0.4634 1.3873 -0.0595 -0.2558 -0.3703 145 GLY   M O   
22414 N  N   . PHE   M  159 ? 1.5399 0.5997 1.3297 0.0105  -0.2827 -0.1543 146 PHE   M N   
22415 C  CA  . PHE   M  159 ? 1.5147 0.6474 1.3586 -0.0065 -0.2569 -0.1317 146 PHE   M CA  
22416 C  C   . PHE   M  159 ? 1.5169 0.6048 1.2960 -0.0157 -0.2434 -0.0966 146 PHE   M C   
22417 O  O   . PHE   M  159 ? 1.4886 0.7521 1.3879 -0.0857 -0.2186 -0.1131 146 PHE   M O   
22418 C  CB  . PHE   M  159 ? 1.5187 0.6676 1.4465 0.0487  -0.2795 -0.1343 146 PHE   M CB  
22419 C  CG  . PHE   M  159 ? 1.6039 0.5740 1.5108 0.0895  -0.3028 -0.1427 146 PHE   M CG  
22420 C  CD1 . PHE   M  159 ? 1.5924 0.5249 1.5587 0.0671  -0.3363 -0.0918 146 PHE   M CD1 
22421 C  CD2 . PHE   M  159 ? 1.6014 0.6079 1.5792 0.1030  -0.2783 -0.1265 146 PHE   M CD2 
22422 C  CE1 . PHE   M  159 ? 1.6386 0.5000 1.5959 0.0498  -0.3112 -0.1323 146 PHE   M CE1 
22423 C  CE2 . PHE   M  159 ? 1.6242 0.5885 1.5706 0.0792  -0.2449 -0.1319 146 PHE   M CE2 
22424 C  CZ  . PHE   M  159 ? 1.6437 0.5486 1.6300 0.0301  -0.2580 -0.0866 146 PHE   M CZ  
22425 N  N   . GLY   M  160 ? 1.4746 0.5391 1.2121 -0.0259 -0.2383 -0.0200 147 GLY   M N   
22426 C  CA  . GLY   M  160 ? 1.4941 0.5165 1.2001 -0.0329 -0.2146 -0.0386 147 GLY   M CA  
22427 C  C   . GLY   M  160 ? 1.5216 0.5055 1.2020 -0.0659 -0.2226 -0.0518 147 GLY   M C   
22428 O  O   . GLY   M  160 ? 1.5503 0.5022 1.1969 -0.1083 -0.2292 -0.0399 147 GLY   M O   
22429 N  N   . ALA   M  161 ? 1.5526 0.5187 1.2021 -0.0685 -0.2038 -0.0816 148 ALA   M N   
22430 C  CA  . ALA   M  161 ? 1.5810 0.5703 1.2501 -0.0589 -0.2462 -0.0765 148 ALA   M CA  
22431 C  C   . ALA   M  161 ? 1.6057 0.5812 1.2971 -0.0741 -0.2636 -0.0751 148 ALA   M C   
22432 O  O   . ALA   M  161 ? 1.6696 0.7834 1.3433 -0.0565 -0.3318 -0.1454 148 ALA   M O   
22433 C  CB  . ALA   M  161 ? 1.5778 0.4870 1.2421 -0.0516 -0.2514 -0.0866 148 ALA   M CB  
22434 N  N   . HIS   M  162 ? 1.6192 0.6019 1.2619 -0.0711 -0.2096 0.0040  149 HIS   M N   
22435 C  CA  . HIS   M  162 ? 1.5996 0.5776 1.2302 -0.0502 -0.1721 0.0448  149 HIS   M CA  
22436 C  C   . HIS   M  162 ? 1.5583 0.5835 1.2797 -0.0943 -0.1897 0.0573  149 HIS   M C   
22437 O  O   . HIS   M  162 ? 1.6164 0.4847 1.3108 -0.0799 -0.1857 0.0897  149 HIS   M O   
22438 C  CB  . HIS   M  162 ? 1.6365 0.5495 1.1522 -0.0284 -0.1371 0.0817  149 HIS   M CB  
22439 C  CG  . HIS   M  162 ? 1.6462 0.4681 1.1261 -0.0471 -0.1553 0.0602  149 HIS   M CG  
22440 N  ND1 . HIS   M  162 ? 1.6999 0.3002 1.0578 -0.0617 -0.1591 0.0551  149 HIS   M ND1 
22441 C  CD2 . HIS   M  162 ? 1.6955 0.4487 1.1003 -0.0234 -0.1127 0.1016  149 HIS   M CD2 
22442 C  CE1 . HIS   M  162 ? 1.7179 0.2812 1.0487 -0.0544 -0.1524 0.0451  149 HIS   M CE1 
22443 N  NE2 . HIS   M  162 ? 1.7164 0.3665 1.0139 -0.0411 -0.1481 0.0718  149 HIS   M NE2 
22444 N  N   . MET   M  163 ? 1.5240 0.6431 1.2832 -0.0932 -0.1956 0.0504  150 MET   M N   
22445 C  CA  . MET   M  163 ? 1.5357 0.6571 1.3190 -0.1236 -0.1542 0.0447  150 MET   M CA  
22446 C  C   . MET   M  163 ? 1.5303 0.7342 1.3125 -0.1511 -0.1333 0.0114  150 MET   M C   
22447 O  O   . MET   M  163 ? 1.5847 0.7492 1.4176 -0.1831 -0.0743 -0.0251 150 MET   M O   
22448 C  CB  . MET   M  163 ? 1.5884 0.6697 1.3213 -0.0797 -0.1643 0.0621  150 MET   M CB  
22449 C  CG  . MET   M  163 ? 1.6222 0.7184 1.3111 -0.0342 -0.1632 0.0830  150 MET   M CG  
22450 S  SD  . MET   M  163 ? 1.6832 0.7776 1.3481 0.0141  -0.1674 0.1113  150 MET   M SD  
22451 C  CE  . MET   M  163 ? 1.6390 0.7836 1.3674 0.0153  -0.2029 0.1009  150 MET   M CE  
22452 N  N   . ALA   M  164 ? 1.5012 0.7481 1.2524 -0.1495 -0.1175 0.0014  151 ALA   M N   
22453 C  CA  . ALA   M  164 ? 1.4922 0.8287 1.2530 -0.1515 -0.0757 0.0059  151 ALA   M CA  
22454 C  C   . ALA   M  164 ? 1.4563 0.8667 1.2626 -0.1435 -0.0496 0.0102  151 ALA   M C   
22455 O  O   . ALA   M  164 ? 1.4519 0.9065 1.2357 -0.1688 -0.0612 0.0093  151 ALA   M O   
22456 C  CB  . ALA   M  164 ? 1.5084 0.8183 1.2592 -0.1682 -0.0529 0.0167  151 ALA   M CB  
22457 N  N   . ASN   M  165 ? 1.4910 0.8602 1.2836 -0.0899 -0.0672 0.0412  152 ASN   M N   
22458 C  CA  . ASN   M  165 ? 1.4508 0.8298 1.3706 -0.0798 -0.0703 0.0293  152 ASN   M CA  
22459 C  C   . ASN   M  165 ? 1.3917 0.7735 1.4192 -0.0299 -0.0361 0.0168  152 ASN   M C   
22460 O  O   . ASN   M  165 ? 1.3911 0.7911 1.3755 -0.0634 0.0143  -0.0127 152 ASN   M O   
22461 C  CB  . ASN   M  165 ? 1.4944 0.9346 1.3397 -0.0632 -0.0922 0.0360  152 ASN   M CB  
22462 C  CG  . ASN   M  165 ? 1.4763 0.9626 1.3132 -0.0890 -0.1034 0.1147  152 ASN   M CG  
22463 O  OD1 . ASN   M  165 ? 1.4562 1.0463 1.3519 -0.0325 -0.1386 0.0907  152 ASN   M OD1 
22464 N  ND2 . ASN   M  165 ? 1.4503 1.0403 1.2664 -0.0870 -0.1161 0.0901  152 ASN   M ND2 
22465 N  N   . PRO   M  166 ? 1.4223 0.7360 1.5094 -0.0110 -0.0673 0.0687  153 PRO   M N   
22466 C  CA  . PRO   M  166 ? 1.4829 0.6188 1.5415 0.0221  -0.0578 0.0746  153 PRO   M CA  
22467 C  C   . PRO   M  166 ? 1.5146 0.5445 1.5277 0.0431  -0.0579 0.0791  153 PRO   M C   
22468 O  O   . PRO   M  166 ? 1.4941 0.3958 1.6222 0.1000  -0.0307 0.0951  153 PRO   M O   
22469 C  CB  . PRO   M  166 ? 1.4586 0.6425 1.5486 0.0211  -0.0549 0.0463  153 PRO   M CB  
22470 C  CG  . PRO   M  166 ? 1.4433 0.6587 1.5158 0.0154  -0.0728 0.0349  153 PRO   M CG  
22471 C  CD  . PRO   M  166 ? 1.4411 0.6579 1.5070 0.0151  -0.0829 0.0408  153 PRO   M CD  
22472 N  N   . LEU   M  167 ? 1.5496 0.5897 1.5184 0.0357  -0.0712 0.0830  154 LEU   M N   
22473 C  CA  . LEU   M  167 ? 1.5878 0.6568 1.4684 -0.0048 -0.1165 0.1119  154 LEU   M CA  
22474 C  C   . LEU   M  167 ? 1.5535 0.7046 1.4871 -0.0033 -0.1009 0.0638  154 LEU   M C   
22475 O  O   . LEU   M  167 ? 1.5555 0.7168 1.4335 -0.0346 -0.1068 0.0838  154 LEU   M O   
22476 C  CB  . LEU   M  167 ? 1.6298 0.6527 1.3973 -0.0249 -0.0992 0.1933  154 LEU   M CB  
22477 C  CG  . LEU   M  167 ? 1.6511 0.6155 1.3247 -0.0512 -0.1146 0.2413  154 LEU   M CG  
22478 C  CD1 . LEU   M  167 ? 1.6775 0.6573 1.3108 -0.0735 -0.1194 0.2602  154 LEU   M CD1 
22479 C  CD2 . LEU   M  167 ? 1.6790 0.6266 1.3435 -0.0798 -0.1205 0.2095  154 LEU   M CD2 
22480 N  N   . LEU   M  168 ? 1.6027 0.6694 1.5032 -0.0052 -0.1343 0.0023  155 LEU   M N   
22481 C  CA  . LEU   M  168 ? 1.6108 0.6185 1.5143 -0.0535 -0.1064 -0.0247 155 LEU   M CA  
22482 C  C   . LEU   M  168 ? 1.5077 0.6199 1.5924 -0.0341 -0.0750 -0.0512 155 LEU   M C   
22483 O  O   . LEU   M  168 ? 1.4817 0.5564 1.6540 -0.0955 -0.0594 -0.1124 155 LEU   M O   
22484 C  CB  . LEU   M  168 ? 1.6626 0.5523 1.4883 -0.0335 -0.1068 -0.0169 155 LEU   M CB  
22485 C  CG  . LEU   M  168 ? 1.6986 0.5412 1.4523 -0.0296 -0.1139 0.0089  155 LEU   M CG  
22486 C  CD1 . LEU   M  168 ? 1.6947 0.5798 1.4099 -0.0515 -0.1046 0.0127  155 LEU   M CD1 
22487 C  CD2 . LEU   M  168 ? 1.7371 0.4783 1.4703 -0.0469 -0.0885 0.0257  155 LEU   M CD2 
22488 N  N   . ARG   M  169 ? 1.5226 0.7289 1.5645 -0.0609 -0.0711 -0.0400 156 ARG   M N   
22489 C  CA  . ARG   M  169 ? 1.5136 0.7832 1.5853 -0.0817 -0.0748 -0.0177 156 ARG   M CA  
22490 C  C   . ARG   M  169 ? 1.5517 0.8394 1.6273 -0.1178 -0.0597 -0.0143 156 ARG   M C   
22491 O  O   . ARG   M  169 ? 1.5628 0.8591 1.7046 -0.0976 -0.0866 -0.0437 156 ARG   M O   
22492 C  CB  . ARG   M  169 ? 1.4920 0.7348 1.5721 -0.1223 -0.0663 0.0150  156 ARG   M CB  
22493 C  CG  . ARG   M  169 ? 1.4915 0.7153 1.5496 -0.1230 -0.0854 0.0097  156 ARG   M CG  
22494 C  CD  . ARG   M  169 ? 1.4560 0.6362 1.5331 -0.1411 -0.0980 0.0310  156 ARG   M CD  
22495 N  NE  . ARG   M  169 ? 1.3861 0.6591 1.5115 -0.1578 -0.1146 0.0118  156 ARG   M NE  
22496 C  CZ  . ARG   M  169 ? 1.3225 0.6133 1.5282 -0.1142 -0.1379 -0.0015 156 ARG   M CZ  
22497 N  NH1 . ARG   M  169 ? 1.2223 0.6125 1.4893 -0.1070 -0.1446 0.0237  156 ARG   M NH1 
22498 N  NH2 . ARG   M  169 ? 1.3267 0.6504 1.5440 -0.1234 -0.1217 0.0134  156 ARG   M NH2 
22499 N  N   . LYS   M  170 ? 1.6190 0.8883 1.6073 -0.1396 -0.0583 0.0107  157 LYS   M N   
22500 C  CA  . LYS   M  170 ? 1.6557 0.9048 1.6139 -0.1563 -0.0546 0.0298  157 LYS   M CA  
22501 C  C   . LYS   M  170 ? 1.5813 0.9102 1.5906 -0.1914 -0.0711 0.0280  157 LYS   M C   
22502 O  O   . LYS   M  170 ? 1.5693 0.9771 1.5772 -0.2113 -0.1223 0.0066  157 LYS   M O   
22503 C  CB  . LYS   M  170 ? 1.7596 0.8613 1.6532 -0.1629 -0.0137 0.0535  157 LYS   M CB  
22504 C  CG  . LYS   M  170 ? 1.8211 0.8453 1.6693 -0.1831 -0.0001 0.0449  157 LYS   M CG  
22505 C  CD  . LYS   M  170 ? 1.8546 0.9276 1.6297 -0.1750 -0.0084 0.0759  157 LYS   M CD  
22506 C  CE  . LYS   M  170 ? 1.9090 0.9607 1.6218 -0.2267 -0.0172 0.0630  157 LYS   M CE  
22507 N  NZ  . LYS   M  170 ? 1.9379 0.8959 1.6814 -0.2350 -0.0051 0.0564  157 LYS   M NZ  
22508 N  N   . VAL   M  171 ? 1.5899 0.8361 1.5767 -0.1825 -0.0401 0.0728  158 VAL   M N   
22509 C  CA  . VAL   M  171 ? 1.5656 0.7653 1.6053 -0.2079 -0.0322 0.0857  158 VAL   M CA  
22510 C  C   . VAL   M  171 ? 1.5032 0.7279 1.6669 -0.2039 -0.0684 0.0463  158 VAL   M C   
22511 O  O   . VAL   M  171 ? 1.4628 0.5425 1.6635 -0.3575 -0.0247 0.1031  158 VAL   M O   
22512 C  CB  . VAL   M  171 ? 1.6334 0.7412 1.5328 -0.1882 -0.0244 0.0946  158 VAL   M CB  
22513 C  CG1 . VAL   M  171 ? 1.6548 0.6863 1.5333 -0.2024 -0.0139 0.1087  158 VAL   M CG1 
22514 C  CG2 . VAL   M  171 ? 1.6678 0.8177 1.5233 -0.1564 -0.0450 0.1034  158 VAL   M CG2 
22515 N  N   . VAL   M  172 ? 1.4786 0.7375 1.6513 -0.1677 -0.0561 0.0272  159 VAL   M N   
22516 C  CA  . VAL   M  172 ? 1.4743 0.7723 1.6702 -0.0962 -0.1118 -0.0102 159 VAL   M CA  
22517 C  C   . VAL   M  172 ? 1.4597 0.7842 1.6503 -0.0999 -0.1424 -0.0241 159 VAL   M C   
22518 O  O   . VAL   M  172 ? 1.4571 0.5973 1.4966 -0.1443 -0.2064 -0.0649 159 VAL   M O   
22519 C  CB  . VAL   M  172 ? 1.4558 0.7742 1.7357 -0.1166 -0.1014 0.0097  159 VAL   M CB  
22520 C  CG1 . VAL   M  172 ? 1.4921 0.8326 1.7685 -0.1200 -0.0662 0.0032  159 VAL   M CG1 
22521 C  CG2 . VAL   M  172 ? 1.4453 0.7655 1.7108 -0.0815 -0.0830 0.0122  159 VAL   M CG2 
22522 N  N   . ASP   M  173 ? 1.4911 0.9084 1.6851 -0.1016 -0.1986 -0.0385 160 ASP   M N   
22523 C  CA  . ASP   M  173 ? 1.5115 0.9961 1.7006 -0.1116 -0.1811 -0.0522 160 ASP   M CA  
22524 C  C   . ASP   M  173 ? 1.5149 1.0742 1.6890 -0.1478 -0.1451 0.0029  160 ASP   M C   
22525 O  O   . ASP   M  173 ? 1.5253 1.1887 1.7018 -0.2322 -0.0989 0.0494  160 ASP   M O   
22526 C  CB  . ASP   M  173 ? 1.5070 0.9557 1.7644 -0.0718 -0.2075 -0.0742 160 ASP   M CB  
22527 C  CG  . ASP   M  173 ? 1.4846 0.9238 1.7979 -0.0747 -0.2492 -0.1122 160 ASP   M CG  
22528 O  OD1 . ASP   M  173 ? 1.4917 0.8997 1.7677 -0.0408 -0.2189 -0.1662 160 ASP   M OD1 
22529 O  OD2 . ASP   M  173 ? 1.4355 1.0005 1.8591 -0.0706 -0.2928 -0.1140 160 ASP   M OD2 
22530 N  N   . ARG   M  174 ? 1.5106 1.0683 1.7461 -0.1503 -0.1691 -0.0248 161 ARG   M N   
22531 C  CA  . ARG   M  174 ? 1.4988 1.1872 1.7188 -0.1250 -0.2342 0.0018  161 ARG   M CA  
22532 C  C   . ARG   M  174 ? 1.5622 1.2245 1.7008 -0.0848 -0.2225 0.0152  161 ARG   M C   
22533 O  O   . ARG   M  174 ? 1.6781 1.4111 1.7027 -0.1483 -0.2011 0.0096  161 ARG   M O   
22534 C  CB  . ARG   M  174 ? 1.4988 1.2547 1.7806 -0.1118 -0.2565 -0.0449 161 ARG   M CB  
22535 C  CG  . ARG   M  174 ? 1.4579 1.4007 1.8644 -0.0659 -0.2629 -0.0713 161 ARG   M CG  
22536 C  CD  . ARG   M  174 ? 1.4281 1.4167 1.9349 -0.0658 -0.2872 -0.1007 161 ARG   M CD  
22537 N  NE  . ARG   M  174 ? 1.4002 1.5723 1.9379 -0.0478 -0.3293 -0.1747 161 ARG   M NE  
22538 C  CZ  . ARG   M  174 ? 1.2687 1.6413 2.0063 -0.0154 -0.4019 -0.1120 161 ARG   M CZ  
22539 N  NH1 . ARG   M  174 ? 1.3298 1.5788 1.9652 0.0008  -0.4040 -0.1265 161 ARG   M NH1 
22540 N  NH2 . ARG   M  174 ? 1.2369 1.7658 1.9684 -0.0353 -0.4069 -0.1546 161 ARG   M NH2 
22541 N  N   . GLU   M  175 ? 1.6003 1.2508 1.7274 -0.0629 -0.1935 0.0621  162 GLU   M N   
22542 C  CA  . GLU   M  175 ? 1.6274 1.1947 1.7821 -0.0584 -0.1542 0.1051  162 GLU   M CA  
22543 C  C   . GLU   M  175 ? 1.5903 1.0189 1.8237 -0.0013 -0.1589 0.1497  162 GLU   M C   
22544 O  O   . GLU   M  175 ? 1.6724 0.9324 1.8285 0.0002  -0.1728 0.1828  162 GLU   M O   
22545 C  CB  . GLU   M  175 ? 1.6555 1.4394 1.7697 -0.0691 -0.1637 0.1993  162 GLU   M CB  
22546 C  CG  . GLU   M  175 ? 1.7133 1.5287 1.8560 -0.1187 -0.1158 0.1382  162 GLU   M CG  
22547 C  CD  . GLU   M  175 ? 1.7303 1.6543 1.8902 -0.1597 -0.0358 0.1891  162 GLU   M CD  
22548 O  OE1 . GLU   M  175 ? 1.7081 1.4657 1.9082 -0.2698 0.0800  0.4098  162 GLU   M OE1 
22549 O  OE2 . GLU   M  175 ? 1.7460 1.9826 1.9311 -0.0883 0.0684  0.1618  162 GLU   M OE2 
22550 N  N   . SER   M  176 ? 1.5856 0.9154 1.8093 0.0505  -0.1828 0.1291  163 SER   M N   
22551 C  CA  . SER   M  176 ? 1.6007 0.8516 1.8636 0.0200  -0.1622 0.1239  163 SER   M CA  
22552 C  C   . SER   M  176 ? 1.5871 0.7526 1.8682 0.0241  -0.1110 0.1158  163 SER   M C   
22553 O  O   . SER   M  176 ? 1.6162 0.7951 1.9324 0.0405  -0.0626 0.1418  163 SER   M O   
22554 C  CB  . SER   M  176 ? 1.6345 0.7943 1.8631 0.0296  -0.1901 0.1456  163 SER   M CB  
22555 O  OG  . SER   M  176 ? 1.6551 0.8731 1.8026 0.0806  -0.1980 0.1196  163 SER   M OG  
22556 N  N   . ASP   M  177 ? 1.5593 0.7410 1.9292 0.0136  -0.0591 0.0365  164 ASP   M N   
22557 C  CA  . ASP   M  177 ? 1.6065 0.8561 1.8827 0.0085  -0.0488 0.0214  164 ASP   M CA  
22558 C  C   . ASP   M  177 ? 1.5555 0.7850 1.9003 0.0120  0.0099  0.0155  164 ASP   M C   
22559 O  O   . ASP   M  177 ? 1.4986 0.7822 1.8935 -0.0366 0.0505  -0.0046 164 ASP   M O   
22560 C  CB  . ASP   M  177 ? 1.6361 0.9098 1.9453 0.0184  -0.0458 -0.0723 164 ASP   M CB  
22561 C  CG  . ASP   M  177 ? 1.7016 0.9012 1.9950 0.0415  -0.0520 -0.1062 164 ASP   M CG  
22562 O  OD1 . ASP   M  177 ? 1.7141 0.9453 2.0694 0.0069  -0.0769 -0.1077 164 ASP   M OD1 
22563 O  OD2 . ASP   M  177 ? 1.7284 0.9010 1.9392 0.0550  -0.0426 -0.0919 164 ASP   M OD2 
22564 N  N   . ILE   M  178 ? 1.5407 0.7920 1.7550 0.0430  -0.0072 0.0352  165 ILE   M N   
22565 C  CA  . ILE   M  178 ? 1.5571 0.8189 1.6586 0.0617  0.0055  0.0359  165 ILE   M CA  
22566 C  C   . ILE   M  178 ? 1.6145 0.9027 1.6737 0.0900  0.0213  0.0026  165 ILE   M C   
22567 O  O   . ILE   M  178 ? 1.6744 1.0413 1.6443 0.1600  0.0538  -0.0362 165 ILE   M O   
22568 C  CB  . ILE   M  178 ? 1.5396 0.7578 1.6467 0.0637  -0.0413 0.0217  165 ILE   M CB  
22569 C  CG1 . ILE   M  178 ? 1.5141 0.6728 1.6143 0.0736  -0.0790 0.0429  165 ILE   M CG1 
22570 C  CG2 . ILE   M  178 ? 1.5372 0.7817 1.6187 0.0514  -0.0122 0.0135  165 ILE   M CG2 
22571 C  CD1 . ILE   M  178 ? 1.4888 0.6867 1.5808 0.0831  -0.1112 0.0542  165 ILE   M CD1 
22572 N  N   . PRO   M  179 ? 1.5988 0.9203 1.7104 0.0622  0.0049  0.0125  166 PRO   M N   
22573 C  CA  . PRO   M  179 ? 1.5665 0.9562 1.7539 0.0077  0.0393  0.0347  166 PRO   M CA  
22574 C  C   . PRO   M  179 ? 1.5729 0.9061 1.7693 -0.0529 0.0640  -0.0127 166 PRO   M C   
22575 O  O   . PRO   M  179 ? 1.5302 1.0175 1.7798 -0.0862 0.1165  0.0063  166 PRO   M O   
22576 C  CB  . PRO   M  179 ? 1.5585 1.0017 1.8103 0.0023  0.0276  0.0524  166 PRO   M CB  
22577 C  CG  . PRO   M  179 ? 1.5406 0.9895 1.7836 0.0408  0.0032  0.0484  166 PRO   M CG  
22578 C  CD  . PRO   M  179 ? 1.5864 0.9204 1.7138 0.0416  -0.0020 0.0134  166 PRO   M CD  
22579 N  N   . LYS   M  180 ? 1.6126 0.8941 1.8183 -0.1215 0.0565  -0.0343 167 LYS   M N   
22580 C  CA  . LYS   M  180 ? 1.6744 0.8745 1.8671 -0.0954 0.1011  -0.0341 167 LYS   M CA  
22581 C  C   . LYS   M  180 ? 1.6773 0.7792 1.8470 -0.0795 0.1176  -0.0596 167 LYS   M C   
22582 O  O   . LYS   M  180 ? 1.8121 0.8394 1.8815 -0.0318 0.2422  -0.0268 167 LYS   M O   
22583 C  CB  . LYS   M  180 ? 1.6251 0.8884 1.8961 -0.1216 0.0645  -0.0285 167 LYS   M CB  
22584 C  CG  . LYS   M  180 ? 1.5613 0.8902 1.9731 -0.1616 0.0445  -0.0428 167 LYS   M CG  
22585 C  CD  . LYS   M  180 ? 1.5295 0.8972 2.0284 -0.2037 0.0200  -0.0408 167 LYS   M CD  
22586 C  CE  . LYS   M  180 ? 1.4981 0.9642 2.0655 -0.2155 0.0083  -0.0241 167 LYS   M CE  
22587 N  NZ  . LYS   M  180 ? 1.4873 1.0608 2.0602 -0.2221 -0.0338 -0.0564 167 LYS   M NZ  
22588 N  N   . THR   M  181 ? 1.6846 0.6722 1.7734 -0.0709 0.1010  -0.1154 168 THR   M N   
22589 C  CA  . THR   M  181 ? 1.6890 0.7581 1.7153 -0.0304 0.1324  -0.1186 168 THR   M CA  
22590 C  C   . THR   M  181 ? 1.7874 0.8002 1.6959 0.0028  0.1429  -0.1329 168 THR   M C   
22591 O  O   . THR   M  181 ? 1.8525 0.8372 1.6890 -0.0109 0.1108  -0.0582 168 THR   M O   
22592 C  CB  . THR   M  181 ? 1.6988 0.7774 1.6394 -0.0223 0.1166  -0.1301 168 THR   M CB  
22593 O  OG1 . THR   M  181 ? 1.5949 0.8655 1.6011 -0.1063 0.0985  -0.0991 168 THR   M OG1 
22594 C  CG2 . THR   M  181 ? 1.7135 0.8301 1.5992 -0.0015 0.1199  -0.1385 168 THR   M CG2 
22595 N  N   . THR   M  182 ? 1.7804 0.7599 1.6787 0.0138  0.1819  -0.1501 169 THR   M N   
22596 C  CA  . THR   M  182 ? 1.7126 0.7470 1.6729 -0.0353 0.2033  -0.1388 169 THR   M CA  
22597 C  C   . THR   M  182 ? 1.7098 0.6897 1.6376 -0.0267 0.1832  -0.1851 169 THR   M C   
22598 O  O   . THR   M  182 ? 1.7020 0.4220 1.6468 -0.1106 0.0840  -0.1928 169 THR   M O   
22599 C  CB  . THR   M  182 ? 1.7534 0.6895 1.6997 -0.0074 0.2413  -0.1260 169 THR   M CB  
22600 O  OG1 . THR   M  182 ? 1.6967 0.6869 1.6140 0.0010  0.2923  -0.1421 169 THR   M OG1 
22601 C  CG2 . THR   M  182 ? 1.7481 0.7009 1.7533 -0.0339 0.2749  -0.1224 169 THR   M CG2 
22602 N  N   . VAL   M  183 ? 1.7221 0.8429 1.6400 -0.1438 0.1203  -0.1743 170 VAL   M N   
22603 C  CA  . VAL   M  183 ? 1.7306 0.8809 1.6407 -0.1885 0.1253  -0.1947 170 VAL   M CA  
22604 C  C   . VAL   M  183 ? 1.7303 0.8241 1.6593 -0.2617 0.1129  -0.1992 170 VAL   M C   
22605 O  O   . VAL   M  183 ? 1.6656 0.6604 1.5945 -0.4112 0.1211  -0.2393 170 VAL   M O   
22606 C  CB  . VAL   M  183 ? 1.8038 0.8648 1.6546 -0.1362 0.1346  -0.2036 170 VAL   M CB  
22607 C  CG1 . VAL   M  183 ? 1.7945 0.9527 1.7070 -0.1597 0.1846  -0.1661 170 VAL   M CG1 
22608 C  CG2 . VAL   M  183 ? 1.7747 0.8522 1.6200 -0.0611 0.1480  -0.2225 170 VAL   M CG2 
22609 N  N   . GLN   M  184 ? 1.7649 0.8308 1.7006 -0.2647 0.1430  -0.1911 171 GLN   M N   
22610 C  CA  . GLN   M  184 ? 1.7996 0.8761 1.6943 -0.2393 0.0953  -0.1833 171 GLN   M CA  
22611 C  C   . GLN   M  184 ? 1.7747 0.8289 1.6523 -0.2315 0.0832  -0.1343 171 GLN   M C   
22612 O  O   . GLN   M  184 ? 1.7392 0.8317 1.5869 -0.2726 0.0102  -0.0978 171 GLN   M O   
22613 C  CB  . GLN   M  184 ? 1.8061 0.9608 1.7382 -0.2349 0.1423  -0.2572 171 GLN   M CB  
22614 C  CG  . GLN   M  184 ? 1.8710 1.0674 1.7485 -0.2564 0.1190  -0.3104 171 GLN   M CG  
22615 C  CD  . GLN   M  184 ? 1.8722 1.1018 1.7584 -0.2332 0.1509  -0.3309 171 GLN   M CD  
22616 O  OE1 . GLN   M  184 ? 1.8568 1.0481 1.7485 -0.2663 0.1523  -0.3844 171 GLN   M OE1 
22617 N  NE2 . GLN   M  184 ? 1.8926 1.2054 1.6792 -0.2357 0.1619  -0.3450 171 GLN   M NE2 
22618 N  N   . VAL   M  185 ? 1.7930 0.8550 1.6631 -0.2492 0.0645  -0.0750 172 VAL   M N   
22619 C  CA  . VAL   M  185 ? 1.7392 0.7787 1.6886 -0.2261 0.0928  -0.0440 172 VAL   M CA  
22620 C  C   . VAL   M  185 ? 1.7638 0.7846 1.6444 -0.1778 0.1040  0.0150  172 VAL   M C   
22621 O  O   . VAL   M  185 ? 1.7209 0.8929 1.6649 -0.1311 0.1386  0.0679  172 VAL   M O   
22622 C  CB  . VAL   M  185 ? 1.7472 0.6944 1.7403 -0.3068 0.0768  -0.1032 172 VAL   M CB  
22623 C  CG1 . VAL   M  185 ? 1.6592 0.6959 1.7216 -0.3525 0.0414  -0.1051 172 VAL   M CG1 
22624 C  CG2 . VAL   M  185 ? 1.7432 0.6542 1.7868 -0.3504 0.0682  -0.1267 172 VAL   M CG2 
22625 N  N   . ALA   M  186 ? 1.6913 0.7995 1.5691 -0.1374 0.1464  0.0373  173 ALA   M N   
22626 C  CA  . ALA   M  186 ? 1.6641 0.7137 1.4898 -0.1100 0.1033  0.0415  173 ALA   M CA  
22627 C  C   . ALA   M  186 ? 1.6849 0.6801 1.4192 -0.0861 0.1068  0.0797  173 ALA   M C   
22628 O  O   . ALA   M  186 ? 1.6875 0.7092 1.3417 -0.0613 0.0879  0.1119  173 ALA   M O   
22629 C  CB  . ALA   M  186 ? 1.6671 0.6995 1.5093 -0.1277 0.1036  0.0291  173 ALA   M CB  
22630 N  N   . GLU   M  187 ? 1.7077 0.6732 1.3879 -0.0877 0.1217  0.1151  174 GLU   M N   
22631 C  CA  . GLU   M  187 ? 1.7431 0.7693 1.3109 -0.1062 0.1166  0.1021  174 GLU   M CA  
22632 C  C   . GLU   M  187 ? 1.8108 0.7765 1.3251 -0.0999 0.1139  0.1092  174 GLU   M C   
22633 O  O   . GLU   M  187 ? 1.7546 0.7549 1.2182 -0.1760 0.0667  0.1601  174 GLU   M O   
22634 C  CB  . GLU   M  187 ? 1.7461 0.8394 1.2791 -0.0586 0.1602  0.1191  174 GLU   M CB  
22635 C  CG  . GLU   M  187 ? 1.7581 0.9962 1.2178 -0.0170 0.1606  0.1106  174 GLU   M CG  
22636 C  CD  . GLU   M  187 ? 1.7853 1.1603 1.1915 0.0219  0.1997  0.1070  174 GLU   M CD  
22637 O  OE1 . GLU   M  187 ? 1.7875 1.3652 1.2462 0.0721  0.1746  0.0838  174 GLU   M OE1 
22638 O  OE2 . GLU   M  187 ? 1.7452 1.2386 1.2535 0.0277  0.1864  0.1660  174 GLU   M OE2 
22639 N  N   . GLU   M  188 ? 1.8613 0.8041 1.3788 -0.1312 0.1639  0.0704  175 GLU   M N   
22640 C  CA  . GLU   M  188 ? 1.9059 0.7861 1.4291 -0.0825 0.1956  -0.0230 175 GLU   M CA  
22641 C  C   . GLU   M  188 ? 1.8928 0.6337 1.4791 -0.0418 0.1628  -0.0602 175 GLU   M C   
22642 O  O   . GLU   M  188 ? 1.8293 0.6974 1.4183 -0.0547 0.1495  -0.1137 175 GLU   M O   
22643 C  CB  . GLU   M  188 ? 1.9217 0.9072 1.5597 -0.1020 0.2483  -0.0015 175 GLU   M CB  
22644 C  CG  . GLU   M  188 ? 2.0015 0.9518 1.6350 -0.0937 0.2807  0.0521  175 GLU   M CG  
22645 C  CD  . GLU   M  188 ? 2.0195 1.1388 1.7434 -0.1126 0.3313  0.0441  175 GLU   M CD  
22646 O  OE1 . GLU   M  188 ? 2.1533 1.1437 1.7823 -0.0997 0.3496  0.0000  175 GLU   M OE1 
22647 O  OE2 . GLU   M  188 ? 2.0444 1.2003 1.8748 -0.2074 0.2919  0.0467  175 GLU   M OE2 
22648 N  N   . ALA   M  189 ? 1.8362 0.4983 1.4847 0.0235  0.1709  -0.1090 176 ALA   M N   
22649 C  CA  . ALA   M  189 ? 1.7598 0.5493 1.4653 0.0210  0.1251  -0.1232 176 ALA   M CA  
22650 C  C   . ALA   M  189 ? 1.7678 0.6034 1.4935 -0.0422 0.0555  -0.0751 176 ALA   M C   
22651 O  O   . ALA   M  189 ? 1.6431 0.8623 1.5110 0.0114  0.0760  -0.0598 176 ALA   M O   
22652 C  CB  . ALA   M  189 ? 1.7108 0.4710 1.4731 0.0406  0.1295  -0.1716 176 ALA   M CB  
22653 N  N   . ILE   M  190 ? 1.6820 0.6162 1.4654 -0.0678 0.0467  -0.0535 177 ILE   M N   
22654 C  CA  . ILE   M  190 ? 1.6795 0.6989 1.4193 -0.0894 0.0015  -0.0420 177 ILE   M CA  
22655 C  C   . ILE   M  190 ? 1.7411 0.7841 1.3653 -0.1053 0.0055  0.0303  177 ILE   M C   
22656 O  O   . ILE   M  190 ? 1.7366 0.9014 1.3869 -0.1220 0.0452  0.0559  177 ILE   M O   
22657 C  CB  . ILE   M  190 ? 1.6762 0.7246 1.4021 -0.1572 -0.0300 -0.1063 177 ILE   M CB  
22658 C  CG1 . ILE   M  190 ? 1.6790 0.6755 1.4127 -0.1781 -0.0580 -0.1266 177 ILE   M CG1 
22659 C  CG2 . ILE   M  190 ? 1.6874 0.6998 1.3697 -0.1750 -0.0267 -0.1326 177 ILE   M CG2 
22660 C  CD1 . ILE   M  190 ? 1.6551 0.6431 1.4068 -0.1872 -0.0750 -0.1250 177 ILE   M CD1 
22661 N  N   . VAL   M  191 ? 1.6982 0.8278 1.3638 -0.1037 0.0112  0.0447  178 VAL   M N   
22662 C  CA  . VAL   M  191 ? 1.6769 0.8579 1.2948 -0.1332 0.0368  0.0489  178 VAL   M CA  
22663 C  C   . VAL   M  191 ? 1.6505 0.8462 1.3288 -0.0951 -0.0297 0.0802  178 VAL   M C   
22664 O  O   . VAL   M  191 ? 1.6479 0.8042 1.3365 -0.0876 -0.0139 0.0614  178 VAL   M O   
22665 C  CB  . VAL   M  191 ? 1.6539 0.8672 1.3156 -0.1498 0.0757  0.0650  178 VAL   M CB  
22666 C  CG1 . VAL   M  191 ? 1.6517 0.8887 1.2764 -0.1508 0.0781  0.0587  178 VAL   M CG1 
22667 C  CG2 . VAL   M  191 ? 1.6462 0.8745 1.2997 -0.1693 0.1030  0.0646  178 VAL   M CG2 
22668 N  N   . ASN   M  192 ? 1.6586 0.8749 1.3449 -0.0680 -0.0783 0.0677  179 ASN   M N   
22669 C  CA  . ASN   M  192 ? 1.6283 0.8873 1.4167 -0.0302 -0.0968 0.0487  179 ASN   M CA  
22670 C  C   . ASN   M  192 ? 1.5958 0.8372 1.4095 -0.0176 -0.1118 0.0629  179 ASN   M C   
22671 O  O   . ASN   M  192 ? 1.5242 0.8854 1.3743 -0.0298 -0.0989 0.0601  179 ASN   M O   
22672 C  CB  . ASN   M  192 ? 1.6108 0.9966 1.5000 -0.0336 -0.1073 0.0452  179 ASN   M CB  
22673 C  CG  . ASN   M  192 ? 1.6237 1.0592 1.5115 -0.0581 -0.1285 -0.0157 179 ASN   M CG  
22674 O  OD1 . ASN   M  192 ? 1.6200 1.2740 1.5381 -0.0610 -0.1330 -0.1261 179 ASN   M OD1 
22675 N  ND2 . ASN   M  192 ? 1.6515 1.1001 1.5087 -0.0811 -0.1067 0.0408  179 ASN   M ND2 
22676 N  N   . ALA   M  193 ? 1.5818 0.7500 1.4272 0.0119  -0.0952 0.0297  180 ALA   M N   
22677 C  CA  . ALA   M  193 ? 1.5577 0.7102 1.4104 -0.0119 -0.1183 -0.0064 180 ALA   M CA  
22678 C  C   . ALA   M  193 ? 1.5810 0.6356 1.4219 -0.0196 -0.1572 -0.0104 180 ALA   M C   
22679 O  O   . ALA   M  193 ? 1.5833 0.4776 1.4612 -0.0277 -0.1919 -0.0342 180 ALA   M O   
22680 C  CB  . ALA   M  193 ? 1.5405 0.7466 1.3673 -0.0129 -0.1240 -0.0082 180 ALA   M CB  
22681 N  N   . MET   M  194 ? 1.6369 0.6856 1.3955 -0.0299 -0.1713 -0.0053 181 MET   M N   
22682 C  CA  . MET   M  194 ? 1.6613 0.7345 1.3780 -0.0212 -0.2010 0.0076  181 MET   M CA  
22683 C  C   . MET   M  194 ? 1.6461 0.7025 1.3675 -0.0237 -0.1602 -0.0032 181 MET   M C   
22684 O  O   . MET   M  194 ? 1.6573 0.7090 1.3146 0.0778  -0.2056 -0.0108 181 MET   M O   
22685 C  CB  . MET   M  194 ? 1.7302 0.8122 1.3905 -0.0540 -0.2138 -0.0363 181 MET   M CB  
22686 C  CG  . MET   M  194 ? 1.7444 0.7975 1.4456 -0.0848 -0.2780 -0.0491 181 MET   M CG  
22687 S  SD  . MET   M  194 ? 1.7049 0.8408 1.4036 -0.1577 -0.3382 -0.1136 181 MET   M SD  
22688 C  CE  . MET   M  194 ? 1.7229 0.9844 1.5084 -0.2195 -0.3838 -0.1001 181 MET   M CE  
22689 N  N   . ARG   M  195 ? 1.7029 0.6683 1.3713 -0.0001 -0.1339 0.0141  182 ARG   M N   
22690 C  CA  . ARG   M  195 ? 1.7251 0.6836 1.3236 0.0069  -0.1262 0.0234  182 ARG   M CA  
22691 C  C   . ARG   M  195 ? 1.7208 0.5740 1.3402 0.0466  -0.1523 0.0519  182 ARG   M C   
22692 O  O   . ARG   M  195 ? 1.7680 0.4444 1.2873 0.0636  -0.1788 0.0189  182 ARG   M O   
22693 C  CB  . ARG   M  195 ? 1.7347 0.7304 1.3532 -0.0312 -0.1101 0.0125  182 ARG   M CB  
22694 C  CG  . ARG   M  195 ? 1.7194 0.6958 1.3724 -0.0920 -0.0849 0.0034  182 ARG   M CG  
22695 C  CD  . ARG   M  195 ? 1.7324 0.7600 1.4171 -0.1272 -0.0587 0.0025  182 ARG   M CD  
22696 N  NE  . ARG   M  195 ? 1.7275 0.8486 1.4840 -0.1736 -0.0640 -0.0072 182 ARG   M NE  
22697 C  CZ  . ARG   M  195 ? 1.7052 0.9021 1.5155 -0.2074 -0.0455 -0.0456 182 ARG   M CZ  
22698 N  NH1 . ARG   M  195 ? 1.7044 0.9383 1.5437 -0.2303 -0.0489 -0.0467 182 ARG   M NH1 
22699 N  NH2 . ARG   M  195 ? 1.7510 0.9635 1.5092 -0.2240 -0.0428 -0.0620 182 ARG   M NH2 
22700 N  N   . VAL   M  196 ? 1.7294 0.4967 1.3196 0.0356  -0.1418 0.0702  183 VAL   M N   
22701 C  CA  . VAL   M  196 ? 1.6804 0.4323 1.3275 0.0468  -0.1423 0.0877  183 VAL   M CA  
22702 C  C   . VAL   M  196 ? 1.6799 0.4274 1.3178 0.0777  -0.1218 0.0879  183 VAL   M C   
22703 O  O   . VAL   M  196 ? 1.6826 0.3540 1.3328 0.0428  -0.1135 0.1035  183 VAL   M O   
22704 C  CB  . VAL   M  196 ? 1.6892 0.4226 1.3057 0.0396  -0.1447 0.0672  183 VAL   M CB  
22705 C  CG1 . VAL   M  196 ? 1.6635 0.4229 1.3105 0.0476  -0.1445 0.0631  183 VAL   M CG1 
22706 C  CG2 . VAL   M  196 ? 1.7020 0.4482 1.3148 0.0312  -0.1396 0.0836  183 VAL   M CG2 
22707 N  N   . LEU   M  197 ? 1.6873 0.4560 1.3000 0.0305  -0.1058 0.1204  184 LEU   M N   
22708 C  CA  . LEU   M  197 ? 1.6770 0.4851 1.2244 0.0447  -0.1154 0.1017  184 LEU   M CA  
22709 C  C   . LEU   M  197 ? 1.6572 0.3573 1.2200 0.0415  -0.0978 0.0860  184 LEU   M C   
22710 O  O   . LEU   M  197 ? 1.6843 0.1586 1.1904 0.0840  -0.1162 0.0686  184 LEU   M O   
22711 C  CB  . LEU   M  197 ? 1.7384 0.4930 1.1942 0.0960  -0.1482 0.1059  184 LEU   M CB  
22712 C  CG  . LEU   M  197 ? 1.8199 0.4735 1.1281 0.0947  -0.1430 0.1184  184 LEU   M CG  
22713 C  CD1 . LEU   M  197 ? 1.9082 0.4719 1.0968 0.0842  -0.1284 0.1528  184 LEU   M CD1 
22714 C  CD2 . LEU   M  197 ? 1.8046 0.5027 1.1134 0.1009  -0.1401 0.1444  184 LEU   M CD2 
22715 N  N   . TYR   M  198 ? 1.6404 0.4310 1.2173 0.0088  -0.1139 0.0886  185 TYR   M N   
22716 C  CA  . TYR   M  198 ? 1.6295 0.5339 1.2115 -0.0016 -0.1107 0.0938  185 TYR   M CA  
22717 C  C   . TYR   M  198 ? 1.6270 0.5459 1.2433 0.0183  -0.1020 0.0844  185 TYR   M C   
22718 O  O   . TYR   M  198 ? 1.6350 0.5044 1.2490 0.0393  -0.0879 0.1146  185 TYR   M O   
22719 C  CB  . TYR   M  198 ? 1.6222 0.6198 1.2028 -0.0175 -0.0907 0.1172  185 TYR   M CB  
22720 C  CG  . TYR   M  198 ? 1.6114 0.7053 1.1737 -0.0391 -0.0878 0.1158  185 TYR   M CG  
22721 C  CD1 . TYR   M  198 ? 1.5947 0.7517 1.1457 -0.0522 -0.1249 0.1113  185 TYR   M CD1 
22722 C  CD2 . TYR   M  198 ? 1.6131 0.8040 1.1189 -0.0314 -0.0689 0.1228  185 TYR   M CD2 
22723 C  CE1 . TYR   M  198 ? 1.5559 0.7725 1.1828 -0.0522 -0.1113 0.1204  185 TYR   M CE1 
22724 C  CE2 . TYR   M  198 ? 1.5853 0.8996 1.1421 -0.0248 -0.0661 0.0947  185 TYR   M CE2 
22725 C  CZ  . TYR   M  198 ? 1.5866 0.8383 1.1582 -0.0115 -0.0750 0.1307  185 TYR   M CZ  
22726 O  OH  . TYR   M  198 ? 1.5222 0.9915 1.2219 0.0338  -0.0556 0.1094  185 TYR   M OH  
22727 N  N   . TYR   M  199 ? 1.6399 0.6321 1.2568 -0.0074 -0.0985 0.0360  186 TYR   M N   
22728 C  CA  . TYR   M  199 ? 1.6875 0.6431 1.2954 0.0225  -0.0839 0.0191  186 TYR   M CA  
22729 C  C   . TYR   M  199 ? 1.6418 0.6985 1.3094 0.0018  -0.0945 0.0039  186 TYR   M C   
22730 O  O   . TYR   M  199 ? 1.6099 0.6789 1.4355 -0.0239 -0.1114 -0.0007 186 TYR   M O   
22731 C  CB  . TYR   M  199 ? 1.6935 0.5653 1.2752 0.0316  -0.0420 0.0310  186 TYR   M CB  
22732 C  CG  . TYR   M  199 ? 1.7782 0.5863 1.2437 0.0660  -0.0262 0.0344  186 TYR   M CG  
22733 C  CD1 . TYR   M  199 ? 1.8142 0.6302 1.2401 0.0988  -0.0150 0.0547  186 TYR   M CD1 
22734 C  CD2 . TYR   M  199 ? 1.7820 0.6199 1.2354 0.0514  -0.0161 0.0405  186 TYR   M CD2 
22735 C  CE1 . TYR   M  199 ? 1.8662 0.7082 1.2365 0.1080  -0.0087 0.0997  186 TYR   M CE1 
22736 C  CE2 . TYR   M  199 ? 1.8295 0.7109 1.2321 0.0396  -0.0077 0.0603  186 TYR   M CE2 
22737 C  CZ  . TYR   M  199 ? 1.8642 0.7487 1.2326 0.0661  0.0088  0.1036  186 TYR   M CZ  
22738 O  OH  . TYR   M  199 ? 1.9652 0.7493 1.2120 0.0563  0.0043  0.1976  186 TYR   M OH  
22739 N  N   . ARG   M  200 ? 1.6527 0.7052 1.3171 -0.0219 -0.1262 0.0096  187 ARG   M N   
22740 C  CA  . ARG   M  200 ? 1.6489 0.6989 1.2852 -0.0549 -0.1857 0.0228  187 ARG   M CA  
22741 C  C   . ARG   M  200 ? 1.6802 0.6293 1.2803 -0.0441 -0.1904 0.0188  187 ARG   M C   
22742 O  O   . ARG   M  200 ? 1.6720 0.6781 1.2344 -0.1038 -0.2233 -0.0150 187 ARG   M O   
22743 C  CB  . ARG   M  200 ? 1.6927 0.7238 1.2559 -0.0474 -0.2234 0.0127  187 ARG   M CB  
22744 C  CG  . ARG   M  200 ? 1.7218 0.6874 1.2816 -0.0619 -0.2416 0.0612  187 ARG   M CG  
22745 C  CD  . ARG   M  200 ? 1.7439 0.6574 1.3002 -0.0628 -0.2589 0.0615  187 ARG   M CD  
22746 N  NE  . ARG   M  200 ? 1.7500 0.6035 1.3135 -0.0681 -0.2685 0.1004  187 ARG   M NE  
22747 C  CZ  . ARG   M  200 ? 1.7851 0.5826 1.3273 -0.0676 -0.2345 0.0735  187 ARG   M CZ  
22748 N  NH1 . ARG   M  200 ? 1.8159 0.4868 1.3315 -0.0519 -0.2119 0.1050  187 ARG   M NH1 
22749 N  NH2 . ARG   M  200 ? 1.8057 0.5537 1.3559 -0.1067 -0.2102 0.0552  187 ARG   M NH2 
22750 N  N   . ASP   M  201 ? 1.6915 0.5645 1.2643 -0.0023 -0.1778 0.0968  188 ASP   M N   
22751 C  CA  . ASP   M  201 ? 1.7348 0.5293 1.2226 0.0016  -0.1807 0.1247  188 ASP   M CA  
22752 C  C   . ASP   M  201 ? 1.7083 0.4010 1.2439 -0.0213 -0.1614 0.1505  188 ASP   M C   
22753 O  O   . ASP   M  201 ? 1.7574 0.3929 1.2721 -0.0764 -0.1537 0.0701  188 ASP   M O   
22754 C  CB  . ASP   M  201 ? 1.7859 0.5419 1.2061 0.0091  -0.1854 0.0589  188 ASP   M CB  
22755 C  CG  . ASP   M  201 ? 1.8377 0.5233 1.1895 -0.0030 -0.2085 0.0533  188 ASP   M CG  
22756 O  OD1 . ASP   M  201 ? 1.8860 0.7155 1.2638 0.1152  -0.2374 -0.0755 188 ASP   M OD1 
22757 O  OD2 . ASP   M  201 ? 2.0097 0.4126 1.1002 -0.0983 -0.3597 0.2574  188 ASP   M OD2 
22758 N  N   . ALA   M  202 ? 1.7275 0.3477 1.2582 -0.0098 -0.1452 0.1650  189 ALA   M N   
22759 C  CA  . ALA   M  202 ? 1.7402 0.4927 1.3278 0.0359  -0.1705 0.1371  189 ALA   M CA  
22760 C  C   . ALA   M  202 ? 1.7308 0.4960 1.3413 0.0489  -0.2053 0.1492  189 ALA   M C   
22761 O  O   . ALA   M  202 ? 1.7714 0.4809 1.3556 0.1593  -0.2283 0.2290  189 ALA   M O   
22762 C  CB  . ALA   M  202 ? 1.7123 0.5412 1.3705 0.0312  -0.1676 0.1078  189 ALA   M CB  
22763 N  N   . ARG   M  203 ? 1.6809 0.5061 1.3575 0.0500  -0.2122 0.1378  190 ARG   M N   
22764 C  CA  . ARG   M  203 ? 1.6471 0.4995 1.4218 0.0381  -0.2163 0.1496  190 ARG   M CA  
22765 C  C   . ARG   M  203 ? 1.6125 0.5130 1.2806 -0.0372 -0.2233 0.1559  190 ARG   M C   
22766 O  O   . ARG   M  203 ? 1.6164 0.5151 1.1883 0.0017  -0.2526 0.1098  190 ARG   M O   
22767 C  CB  . ARG   M  203 ? 1.6220 0.4845 1.4524 0.1224  -0.1640 0.1516  190 ARG   M CB  
22768 C  CG  . ARG   M  203 ? 1.6600 0.5685 1.5796 0.2064  -0.1464 0.1139  190 ARG   M CG  
22769 C  CD  . ARG   M  203 ? 1.6694 0.6390 1.6428 0.2022  -0.1187 0.0609  190 ARG   M CD  
22770 N  NE  . ARG   M  203 ? 1.6755 0.6974 1.8388 0.2867  -0.1102 0.1204  190 ARG   M NE  
22771 C  CZ  . ARG   M  203 ? 1.7032 0.6438 1.9371 0.2482  -0.0379 0.1798  190 ARG   M CZ  
22772 N  NH1 . ARG   M  203 ? 1.6711 0.6141 1.9680 0.2885  -0.0394 0.2128  190 ARG   M NH1 
22773 N  NH2 . ARG   M  203 ? 1.7386 0.5821 1.9969 0.3514  -0.0258 0.1332  190 ARG   M NH2 
22774 N  N   . SER   M  204 ? 1.6661 0.5180 1.3234 -0.1067 -0.2504 0.1761  191 SER   M N   
22775 C  CA  . SER   M  204 ? 1.6872 0.5040 1.3829 -0.1342 -0.2177 0.1551  191 SER   M CA  
22776 C  C   . SER   M  204 ? 1.7651 0.3958 1.3516 -0.1752 -0.1813 0.1156  191 SER   M C   
22777 O  O   . SER   M  204 ? 1.7829 0.5023 1.3513 -0.1445 -0.2172 0.2071  191 SER   M O   
22778 C  CB  . SER   M  204 ? 1.6580 0.7119 1.4091 -0.1369 -0.2702 0.1914  191 SER   M CB  
22779 O  OG  . SER   M  204 ? 1.6628 0.7547 1.4802 -0.0061 -0.2907 0.2908  191 SER   M OG  
22780 N  N   . SER   M  205 ? 1.8367 0.3713 1.4465 -0.1787 -0.0947 0.1059  192 SER   M N   
22781 C  CA  . SER   M  205 ? 1.8799 0.3667 1.4460 -0.1766 -0.0534 0.1526  192 SER   M CA  
22782 C  C   . SER   M  205 ? 1.9660 0.2536 1.4548 -0.2240 0.0198  0.1595  192 SER   M C   
22783 O  O   . SER   M  205 ? 1.9060 0.2708 1.4592 -0.2485 0.0892  0.1924  192 SER   M O   
22784 C  CB  . SER   M  205 ? 1.8536 0.4468 1.4632 -0.1558 -0.1169 0.0908  192 SER   M CB  
22785 O  OG  . SER   M  205 ? 1.9185 0.4635 1.4680 -0.1172 -0.1066 0.0829  192 SER   M OG  
22786 N  N   . ARG   M  206 ? 1.9792 0.4436 1.3803 -0.1614 -0.0273 0.0669  193 ARG   M N   
22787 C  CA  . ARG   M  206 ? 1.9185 0.6927 1.3905 -0.1276 -0.0393 0.0169  193 ARG   M CA  
22788 C  C   . ARG   M  206 ? 1.8059 0.7738 1.4166 -0.0401 -0.0927 0.0241  193 ARG   M C   
22789 O  O   . ARG   M  206 ? 1.7696 0.7678 1.4550 -0.0142 -0.1672 0.0318  193 ARG   M O   
22790 C  CB  . ARG   M  206 ? 2.0103 0.8276 1.3475 -0.1391 -0.0652 0.0248  193 ARG   M CB  
22791 C  CG  . ARG   M  206 ? 2.0205 0.9797 1.3678 -0.1551 -0.0355 0.0227  193 ARG   M CG  
22792 C  CD  . ARG   M  206 ? 2.0628 1.1438 1.3528 -0.0933 -0.0994 0.0452  193 ARG   M CD  
22793 N  NE  . ARG   M  206 ? 2.0589 1.3404 1.3374 -0.0953 -0.0890 0.0841  193 ARG   M NE  
22794 C  CZ  . ARG   M  206 ? 2.0505 1.5694 1.3018 -0.1080 -0.0992 0.1668  193 ARG   M CZ  
22795 N  NH1 . ARG   M  206 ? 2.0358 1.7243 1.4044 -0.0658 -0.0954 0.1187  193 ARG   M NH1 
22796 N  NH2 . ARG   M  206 ? 2.0282 1.7783 1.3635 -0.1316 -0.0757 0.1275  193 ARG   M NH2 
22797 N  N   . ASN   M  207 ? 1.7474 0.8747 1.4152 -0.0684 -0.1135 0.0090  194 ASN   M N   
22798 C  CA  . ASN   M  207 ? 1.7231 0.9255 1.3301 -0.0633 -0.0975 -0.0240 194 ASN   M CA  
22799 C  C   . ASN   M  207 ? 1.6721 0.8178 1.3565 -0.0571 -0.0415 -0.0169 194 ASN   M C   
22800 O  O   . ASN   M  207 ? 1.6940 0.9295 1.3722 -0.0621 -0.0195 -0.0174 194 ASN   M O   
22801 C  CB  . ASN   M  207 ? 1.7213 1.1113 1.2814 -0.0291 -0.1282 -0.0827 194 ASN   M CB  
22802 C  CG  . ASN   M  207 ? 1.6920 1.2328 1.2461 0.0001  -0.1647 -0.1088 194 ASN   M CG  
22803 O  OD1 . ASN   M  207 ? 1.7685 1.2152 1.1285 0.0642  -0.1387 -0.2284 194 ASN   M OD1 
22804 N  ND2 . ASN   M  207 ? 1.7124 1.3686 1.2923 -0.0431 -0.1274 -0.0769 194 ASN   M ND2 
22805 N  N   . PHE   M  208 ? 1.7119 0.6987 1.3532 -0.0712 -0.0012 -0.0121 195 PHE   M N   
22806 C  CA  . PHE   M  208 ? 1.6983 0.6318 1.3676 -0.0615 0.0221  -0.0202 195 PHE   M CA  
22807 C  C   . PHE   M  208 ? 1.7650 0.6280 1.3431 -0.0441 0.0251  -0.0123 195 PHE   M C   
22808 O  O   . PHE   M  208 ? 1.8381 0.5957 1.3514 -0.0405 0.0651  0.0035  195 PHE   M O   
22809 C  CB  . PHE   M  208 ? 1.6362 0.5402 1.3372 -0.0530 0.0778  -0.0103 195 PHE   M CB  
22810 C  CG  . PHE   M  208 ? 1.6403 0.5467 1.3293 -0.0107 0.1166  0.0164  195 PHE   M CG  
22811 C  CD1 . PHE   M  208 ? 1.6111 0.5832 1.3344 -0.0472 0.1746  0.0526  195 PHE   M CD1 
22812 C  CD2 . PHE   M  208 ? 1.5996 0.5416 1.3119 -0.0384 0.1565  0.0375  195 PHE   M CD2 
22813 C  CE1 . PHE   M  208 ? 1.6215 0.5552 1.3342 -0.0534 0.1781  0.0582  195 PHE   M CE1 
22814 C  CE2 . PHE   M  208 ? 1.6198 0.5304 1.3163 -0.0626 0.1498  0.0582  195 PHE   M CE2 
22815 C  CZ  . PHE   M  208 ? 1.6027 0.5403 1.3177 -0.0794 0.1788  0.0675  195 PHE   M CZ  
22816 N  N   . SER   M  209 ? 1.7873 0.6079 1.4160 -0.0290 -0.0268 -0.0162 196 SER   M N   
22817 C  CA  . SER   M  209 ? 1.7831 0.5320 1.4427 -0.0703 -0.0350 0.0001  196 SER   M CA  
22818 C  C   . SER   M  209 ? 1.7514 0.5451 1.3961 -0.0456 -0.0085 0.0505  196 SER   M C   
22819 O  O   . SER   M  209 ? 1.7569 0.4645 1.3222 -0.0266 -0.0099 0.1562  196 SER   M O   
22820 C  CB  . SER   M  209 ? 1.8230 0.4843 1.5715 -0.0561 -0.0449 -0.0155 196 SER   M CB  
22821 O  OG  . SER   M  209 ? 1.7723 0.3277 1.7323 -0.1070 -0.0667 0.0390  196 SER   M OG  
22822 N  N   . LEU   M  210 ? 1.7169 0.5921 1.3222 -0.0988 -0.0109 0.0369  197 LEU   M N   
22823 C  CA  . LEU   M  210 ? 1.7359 0.6656 1.3200 -0.1079 -0.0304 0.0008  197 LEU   M CA  
22824 C  C   . LEU   M  210 ? 1.7698 0.6248 1.2691 -0.1665 -0.0354 -0.0472 197 LEU   M C   
22825 O  O   . LEU   M  210 ? 1.8293 0.5676 1.2844 -0.1958 -0.0067 -0.0656 197 LEU   M O   
22826 C  CB  . LEU   M  210 ? 1.7596 0.6857 1.3230 -0.1265 -0.0458 0.0064  197 LEU   M CB  
22827 C  CG  . LEU   M  210 ? 1.7693 0.7401 1.3567 -0.1185 -0.0649 -0.0380 197 LEU   M CG  
22828 C  CD1 . LEU   M  210 ? 1.7724 0.7729 1.3750 -0.1671 -0.0546 -0.0656 197 LEU   M CD1 
22829 C  CD2 . LEU   M  210 ? 1.7519 0.8241 1.3700 -0.0996 -0.0464 -0.0286 197 LEU   M CD2 
22830 N  N   . ALA   M  211 ? 1.7713 0.6110 1.2811 -0.1702 -0.0462 -0.0489 198 ALA   M N   
22831 C  CA  . ALA   M  211 ? 1.7544 0.6786 1.2843 -0.1249 -0.0352 -0.0817 198 ALA   M CA  
22832 C  C   . ALA   M  211 ? 1.7106 0.6567 1.3352 -0.1331 0.0115  -0.0801 198 ALA   M C   
22833 O  O   . ALA   M  211 ? 1.6567 0.4878 1.3888 -0.2028 -0.0096 -0.0445 198 ALA   M O   
22834 C  CB  . ALA   M  211 ? 1.7428 0.7697 1.2298 -0.1469 -0.0182 -0.0805 198 ALA   M CB  
22835 N  N   . ILE   M  212 ? 1.7318 0.7096 1.3220 -0.1217 0.0253  -0.1031 199 ILE   M N   
22836 C  CA  . ILE   M  212 ? 1.7186 0.7402 1.3397 -0.0660 0.0798  -0.1014 199 ILE   M CA  
22837 C  C   . ILE   M  212 ? 1.7438 0.7530 1.3444 -0.0464 0.0626  -0.0899 199 ILE   M C   
22838 O  O   . ILE   M  212 ? 1.7560 0.8008 1.4028 -0.0965 0.0390  -0.1198 199 ILE   M O   
22839 C  CB  . ILE   M  212 ? 1.7850 0.7161 1.3660 -0.0313 0.1193  -0.0733 199 ILE   M CB  
22840 C  CG1 . ILE   M  212 ? 1.7998 0.7354 1.3485 -0.0025 0.1298  -0.0483 199 ILE   M CG1 
22841 C  CG2 . ILE   M  212 ? 1.7757 0.7809 1.4042 -0.0559 0.1269  -0.0785 199 ILE   M CG2 
22842 C  CD1 . ILE   M  212 ? 1.8260 0.7715 1.3640 0.0094  0.1511  -0.0343 199 ILE   M CD1 
22843 N  N   . ILE   M  213 ? 1.7361 0.7296 1.3650 0.0123  0.0359  -0.1164 200 ILE   M N   
22844 C  CA  . ILE   M  213 ? 1.7192 0.7554 1.3852 0.0394  -0.0201 -0.0957 200 ILE   M CA  
22845 C  C   . ILE   M  213 ? 1.7147 0.7448 1.4154 0.0959  -0.0343 -0.0336 200 ILE   M C   
22846 O  O   . ILE   M  213 ? 1.6845 0.6760 1.3770 0.1709  -0.0424 0.0111  200 ILE   M O   
22847 C  CB  . ILE   M  213 ? 1.6802 0.6288 1.3888 0.0069  -0.0649 -0.1155 200 ILE   M CB  
22848 C  CG1 . ILE   M  213 ? 1.6795 0.5871 1.3554 -0.0245 -0.1118 -0.1545 200 ILE   M CG1 
22849 C  CG2 . ILE   M  213 ? 1.7125 0.6234 1.4574 0.0043  -0.0434 -0.1285 200 ILE   M CG2 
22850 C  CD1 . ILE   M  213 ? 1.6861 0.5979 1.3061 -0.0686 -0.1163 -0.1829 200 ILE   M CD1 
22851 N  N   . ASP   M  214 ? 1.7522 0.8177 1.4691 0.0901  0.0229  -0.0197 201 ASP   M N   
22852 C  CA  . ASP   M  214 ? 1.7633 0.8236 1.6185 0.0416  0.0254  0.0272  201 ASP   M CA  
22853 C  C   . ASP   M  214 ? 1.8176 0.7923 1.6952 0.0185  0.0071  0.0201  201 ASP   M C   
22854 O  O   . ASP   M  214 ? 1.8227 0.6636 1.6871 0.0482  -0.0389 0.1176  201 ASP   M O   
22855 C  CB  . ASP   M  214 ? 1.8313 0.9207 1.6610 -0.0113 0.0723  0.0444  201 ASP   M CB  
22856 C  CG  . ASP   M  214 ? 1.8566 0.9839 1.7336 -0.0683 0.0862  0.0458  201 ASP   M CG  
22857 O  OD1 . ASP   M  214 ? 1.8494 1.0482 1.7830 -0.0347 0.0527  0.0887  201 ASP   M OD1 
22858 O  OD2 . ASP   M  214 ? 1.8372 0.9847 1.7110 -0.0676 0.1670  -0.0157 201 ASP   M OD2 
22859 N  N   . LYS   M  215 ? 1.8120 0.6554 1.7739 0.0738  0.0074  0.0091  202 LYS   M N   
22860 C  CA  . LYS   M  215 ? 1.8177 0.6367 1.7769 0.0884  0.0418  -0.0434 202 LYS   M CA  
22861 C  C   . LYS   M  215 ? 1.8877 0.6811 1.7815 0.0987  0.0677  -0.0651 202 LYS   M C   
22862 O  O   . LYS   M  215 ? 1.9109 0.7139 1.6670 0.1570  0.0693  -0.3196 202 LYS   M O   
22863 C  CB  . LYS   M  215 ? 1.7153 0.5135 1.8457 0.0658  0.0466  -0.0593 202 LYS   M CB  
22864 C  CG  . LYS   M  215 ? 1.6881 0.4853 1.8440 0.0675  0.0471  -0.1025 202 LYS   M CG  
22865 C  CD  . LYS   M  215 ? 1.6281 0.6053 1.8707 0.0719  0.0591  -0.1083 202 LYS   M CD  
22866 C  CE  . LYS   M  215 ? 1.5648 0.8390 1.9298 0.0744  0.1262  -0.0601 202 LYS   M CE  
22867 N  NZ  . LYS   M  215 ? 1.5530 0.9963 1.9680 0.0871  0.1133  -0.0460 202 LYS   M NZ  
22868 N  N   . ASN   M  216 ? 1.9252 0.6521 1.8289 0.0719  0.0838  -0.0489 203 ASN   M N   
22869 C  CA  . ASN   M  216 ? 1.9486 0.6972 1.8512 0.0348  0.1380  -0.0046 203 ASN   M CA  
22870 C  C   . ASN   M  216 ? 2.0216 0.8201 1.8479 0.0662  0.1032  0.0520  203 ASN   M C   
22871 O  O   . ASN   M  216 ? 2.1367 0.8297 1.8374 0.0556  0.1700  0.0490  203 ASN   M O   
22872 C  CB  . ASN   M  216 ? 1.9551 0.7056 1.9310 0.0140  0.1364  0.0042  203 ASN   M CB  
22873 C  CG  . ASN   M  216 ? 1.9091 0.7123 2.0167 -0.0186 0.1360  0.0332  203 ASN   M CG  
22874 O  OD1 . ASN   M  216 ? 1.9515 0.6595 2.1136 -0.1110 0.1309  0.1068  203 ASN   M OD1 
22875 N  ND2 . ASN   M  216 ? 1.9082 0.7353 2.0149 -0.0302 0.1566  0.0109  203 ASN   M ND2 
22876 N  N   . THR   M  217 ? 2.0160 0.8385 1.8003 0.0721  0.0564  0.0258  204 THR   M N   
22877 C  CA  . THR   M  217 ? 2.0387 0.8871 1.7488 0.0386  0.0590  -0.0062 204 THR   M CA  
22878 C  C   . THR   M  217 ? 1.9767 0.8418 1.6275 0.0527  -0.0196 -0.0687 204 THR   M C   
22879 O  O   . THR   M  217 ? 2.0379 0.7823 1.6290 0.0921  -0.0536 -0.0980 204 THR   M O   
22880 C  CB  . THR   M  217 ? 2.0579 0.9254 1.7226 0.0258  0.0380  0.0402  204 THR   M CB  
22881 O  OG1 . THR   M  217 ? 2.0889 0.9407 1.7018 0.0145  -0.0064 0.0622  204 THR   M OG1 
22882 C  CG2 . THR   M  217 ? 2.0817 0.9619 1.7461 0.0157  0.0747  0.0127  204 THR   M CG2 
22883 N  N   . GLY   M  218 ? 1.8829 0.8041 1.6372 0.0562  0.0312  -0.0950 205 GLY   M N   
22884 C  CA  . GLY   M  218 ? 1.8462 0.7546 1.5892 0.0612  -0.0033 -0.1190 205 GLY   M CA  
22885 C  C   . GLY   M  218 ? 1.7698 0.8190 1.5692 0.0558  -0.0269 -0.1033 205 GLY   M C   
22886 O  O   . GLY   M  218 ? 1.7586 0.8310 1.6274 0.0949  -0.0812 -0.1525 205 GLY   M O   
22887 N  N   . LEU   M  219 ? 1.8045 0.6476 1.5151 0.0252  -0.0017 -0.1282 206 LEU   M N   
22888 C  CA  . LEU   M  219 ? 1.8141 0.6123 1.5068 0.0102  0.0396  -0.1419 206 LEU   M CA  
22889 C  C   . LEU   M  219 ? 1.8110 0.7263 1.4286 0.0356  0.0703  -0.1794 206 LEU   M C   
22890 O  O   . LEU   M  219 ? 1.8279 0.5863 1.4986 0.0353  0.0917  -0.1933 206 LEU   M O   
22891 C  CB  . LEU   M  219 ? 1.8481 0.5584 1.4969 0.0110  0.0350  -0.1255 206 LEU   M CB  
22892 C  CG  . LEU   M  219 ? 1.8588 0.5039 1.4885 0.0059  0.0247  -0.1223 206 LEU   M CG  
22893 C  CD1 . LEU   M  219 ? 1.8939 0.6242 1.4246 -0.0074 0.0205  -0.1769 206 LEU   M CD1 
22894 C  CD2 . LEU   M  219 ? 1.8490 0.5241 1.5070 0.0030  0.0149  -0.1010 206 LEU   M CD2 
22895 N  N   . THR   M  220 ? 1.7886 0.7311 1.4270 0.0323  0.1100  -0.1972 207 THR   M N   
22896 C  CA  . THR   M  220 ? 1.8257 0.7720 1.4119 0.0256  0.1026  -0.1953 207 THR   M CA  
22897 C  C   . THR   M  220 ? 1.8307 0.7230 1.3983 0.0386  0.0407  -0.2297 207 THR   M C   
22898 O  O   . THR   M  220 ? 1.8882 0.7199 1.3986 0.1210  0.0566  -0.2421 207 THR   M O   
22899 C  CB  . THR   M  220 ? 1.8263 0.8355 1.4374 0.0173  0.1546  -0.1976 207 THR   M CB  
22900 O  OG1 . THR   M  220 ? 1.8270 0.8501 1.5805 0.0073  0.2083  -0.1912 207 THR   M OG1 
22901 C  CG2 . THR   M  220 ? 1.8427 0.8640 1.4195 0.0109  0.1494  -0.1992 207 THR   M CG2 
22902 N  N   . PHE   M  221 ? 1.8712 0.7550 1.3551 0.0649  -0.0107 -0.2466 208 PHE   M N   
22903 C  CA  . PHE   M  221 ? 1.8864 0.7628 1.3233 0.0798  -0.0290 -0.3013 208 PHE   M CA  
22904 C  C   . PHE   M  221 ? 1.9169 0.7851 1.3671 0.0520  -0.0277 -0.2654 208 PHE   M C   
22905 O  O   . PHE   M  221 ? 2.0466 0.8309 1.4025 0.1320  0.0150  -0.3415 208 PHE   M O   
22906 C  CB  . PHE   M  221 ? 1.8201 0.8335 1.2546 0.0988  -0.0165 -0.2702 208 PHE   M CB  
22907 C  CG  . PHE   M  221 ? 1.8233 0.8494 1.1678 0.1421  -0.0686 -0.2862 208 PHE   M CG  
22908 C  CD1 . PHE   M  221 ? 1.8317 0.8177 1.1570 0.1390  -0.0713 -0.2854 208 PHE   M CD1 
22909 C  CD2 . PHE   M  221 ? 1.8166 0.8980 1.1543 0.1709  -0.0897 -0.3163 208 PHE   M CD2 
22910 C  CE1 . PHE   M  221 ? 1.8148 0.7770 1.1267 0.1496  -0.1079 -0.3041 208 PHE   M CE1 
22911 C  CE2 . PHE   M  221 ? 1.7751 0.8831 1.1719 0.1992  -0.1283 -0.3214 208 PHE   M CE2 
22912 C  CZ  . PHE   M  221 ? 1.7832 0.8172 1.1238 0.1708  -0.1400 -0.3225 208 PHE   M CZ  
22913 N  N   . LYS   M  222 ? 1.8530 0.7672 1.3590 -0.0152 -0.0233 -0.2517 209 LYS   M N   
22914 C  CA  . LYS   M  222 ? 1.8180 0.8147 1.3645 -0.0526 0.0190  -0.1842 209 LYS   M CA  
22915 C  C   . LYS   M  222 ? 1.7950 0.6898 1.3312 -0.0456 -0.0398 -0.1167 209 LYS   M C   
22916 O  O   . LYS   M  222 ? 1.6966 0.5376 1.3711 -0.0100 0.0219  -0.0842 209 LYS   M O   
22917 C  CB  . LYS   M  222 ? 1.8474 0.8372 1.3828 -0.0827 0.0621  -0.1614 209 LYS   M CB  
22918 C  CG  . LYS   M  222 ? 1.8471 0.9679 1.4266 -0.1112 0.1135  -0.1596 209 LYS   M CG  
22919 C  CD  . LYS   M  222 ? 1.8183 1.0022 1.4887 -0.1244 0.1380  -0.1699 209 LYS   M CD  
22920 C  CE  . LYS   M  222 ? 1.7980 1.0687 1.5618 -0.1689 0.1733  -0.1657 209 LYS   M CE  
22921 N  NZ  . LYS   M  222 ? 1.8274 1.0472 1.6168 -0.1563 0.1994  -0.1455 209 LYS   M NZ  
22922 N  N   . LYS   M  223 ? 1.8371 0.7117 1.3034 -0.0348 -0.0575 -0.0760 210 LYS   M N   
22923 C  CA  . LYS   M  223 ? 1.8089 0.8583 1.2999 -0.0602 -0.0944 -0.0877 210 LYS   M CA  
22924 C  C   . LYS   M  223 ? 1.8062 0.8834 1.2931 -0.1082 -0.1119 -0.0760 210 LYS   M C   
22925 O  O   . LYS   M  223 ? 1.8135 0.8728 1.2990 -0.1827 -0.0770 -0.1849 210 LYS   M O   
22926 C  CB  . LYS   M  223 ? 1.8176 0.8706 1.3081 -0.0793 -0.1264 -0.0405 210 LYS   M CB  
22927 C  CG  . LYS   M  223 ? 1.8236 0.9718 1.3159 -0.0781 -0.1007 0.0141  210 LYS   M CG  
22928 C  CD  . LYS   M  223 ? 1.8326 1.0197 1.3522 -0.1076 -0.1244 0.0249  210 LYS   M CD  
22929 C  CE  . LYS   M  223 ? 1.8123 1.0140 1.3889 -0.1042 -0.1210 0.0381  210 LYS   M CE  
22930 N  NZ  . LYS   M  223 ? 1.7914 1.0205 1.3814 -0.0963 -0.1361 0.0417  210 LYS   M NZ  
22931 N  N   . ASN   M  224 ? 1.7583 0.9587 1.3363 -0.0805 -0.1691 -0.0451 211 ASN   M N   
22932 C  CA  . ASN   M  224 ? 1.8219 1.0441 1.3196 -0.0950 -0.1897 0.0385  211 ASN   M CA  
22933 C  C   . ASN   M  224 ? 1.8102 1.0473 1.3394 -0.0788 -0.1791 0.1218  211 ASN   M C   
22934 O  O   . ASN   M  224 ? 1.7504 1.2039 1.2754 -0.0956 -0.1939 0.1312  211 ASN   M O   
22935 C  CB  . ASN   M  224 ? 1.9101 1.1052 1.2796 -0.0663 -0.1588 0.0260  211 ASN   M CB  
22936 C  CG  . ASN   M  224 ? 1.8705 1.2171 1.2962 -0.0819 -0.1664 0.0124  211 ASN   M CG  
22937 O  OD1 . ASN   M  224 ? 1.9568 1.3309 1.2857 0.0391  -0.1039 -0.0674 211 ASN   M OD1 
22938 N  ND2 . ASN   M  224 ? 1.8695 1.2398 1.3281 -0.0412 -0.1929 0.0027  211 ASN   M ND2 
22939 N  N   . LEU   M  225 ? 1.8138 0.9561 1.3501 -0.0310 -0.1917 0.1440  212 LEU   M N   
22940 C  CA  . LEU   M  225 ? 1.8455 0.8366 1.3594 0.0250  -0.1609 0.1616  212 LEU   M CA  
22941 C  C   . LEU   M  225 ? 1.8631 0.7894 1.3610 0.0200  -0.1821 0.1949  212 LEU   M C   
22942 O  O   . LEU   M  225 ? 1.8126 0.6187 1.3664 0.1167  -0.2039 0.2048  212 LEU   M O   
22943 C  CB  . LEU   M  225 ? 1.8133 0.7460 1.3759 0.0212  -0.1569 0.1476  212 LEU   M CB  
22944 C  CG  . LEU   M  225 ? 1.8435 0.6706 1.3716 0.0576  -0.1575 0.1921  212 LEU   M CG  
22945 C  CD1 . LEU   M  225 ? 1.8897 0.7252 1.3290 0.0793  -0.1365 0.1874  212 LEU   M CD1 
22946 C  CD2 . LEU   M  225 ? 1.7973 0.6408 1.4055 0.0973  -0.1597 0.1778  212 LEU   M CD2 
22947 N  N   . GLN   M  226 ? 1.8910 0.8638 1.3284 -0.0264 -0.1517 0.2332  213 GLN   M N   
22948 C  CA  . GLN   M  226 ? 1.8760 0.8794 1.3225 -0.0110 -0.1129 0.2910  213 GLN   M CA  
22949 C  C   . GLN   M  226 ? 1.8771 0.8451 1.2967 -0.0391 -0.0757 0.3424  213 GLN   M C   
22950 O  O   . GLN   M  226 ? 1.9062 0.8801 1.2758 -0.1192 -0.0015 0.4618  213 GLN   M O   
22951 C  CB  . GLN   M  226 ? 1.8669 0.9643 1.3031 -0.0116 -0.1256 0.2755  213 GLN   M CB  
22952 C  CG  . GLN   M  226 ? 1.8652 1.0181 1.3289 -0.0178 -0.1228 0.2471  213 GLN   M CG  
22953 C  CD  . GLN   M  226 ? 1.8189 1.1032 1.3659 0.0201  -0.1455 0.2222  213 GLN   M CD  
22954 O  OE1 . GLN   M  226 ? 1.8117 1.1492 1.4230 0.0488  -0.1411 0.1710  213 GLN   M OE1 
22955 N  NE2 . GLN   M  226 ? 1.8571 1.1423 1.3979 0.0085  -0.1187 0.2433  213 GLN   M NE2 
22956 N  N   . VAL   M  227 ? 1.8912 0.8105 1.2969 -0.0065 -0.0902 0.3594  214 VAL   M N   
22957 C  CA  . VAL   M  227 ? 1.8501 0.9249 1.3291 -0.0314 -0.0719 0.2703  214 VAL   M CA  
22958 C  C   . VAL   M  227 ? 1.8692 0.9979 1.3495 -0.0453 -0.0876 0.3112  214 VAL   M C   
22959 O  O   . VAL   M  227 ? 1.8689 0.8924 1.3152 -0.0605 -0.0595 0.3825  214 VAL   M O   
22960 C  CB  . VAL   M  227 ? 1.8520 0.9334 1.3087 -0.0343 -0.0869 0.2565  214 VAL   M CB  
22961 C  CG1 . VAL   M  227 ? 1.8310 0.9785 1.3225 -0.0426 -0.0854 0.2020  214 VAL   M CG1 
22962 C  CG2 . VAL   M  227 ? 1.8370 0.8831 1.2996 -0.0085 -0.0680 0.2303  214 VAL   M CG2 
22963 N  N   . GLU   M  228 ? 1.8920 1.0489 1.3760 -0.0686 -0.0654 0.3122  215 GLU   M N   
22964 C  CA  . GLU   M  228 ? 1.9822 1.1234 1.3566 -0.0536 -0.0575 0.3376  215 GLU   M CA  
22965 C  C   . GLU   M  228 ? 1.9927 1.1456 1.3375 -0.0501 -0.0590 0.3021  215 GLU   M C   
22966 O  O   . GLU   M  228 ? 2.0008 1.1183 1.3232 -0.0622 -0.0224 0.3665  215 GLU   M O   
22967 C  CB  . GLU   M  228 ? 2.0875 1.2016 1.4795 -0.0594 0.0147  0.2408  215 GLU   M CB  
22968 C  CG  . GLU   M  228 ? 2.1053 1.2980 1.6076 -0.0439 -0.0325 0.1722  215 GLU   M CG  
22969 C  CD  . GLU   M  228 ? 2.2546 1.2799 1.7112 -0.0316 0.0349  0.1416  215 GLU   M CD  
22970 O  OE1 . GLU   M  228 ? 2.3521 1.1856 1.6914 -0.0010 0.0649  0.2842  215 GLU   M OE1 
22971 O  OE2 . GLU   M  228 ? 2.2356 1.4558 1.9055 -0.0187 0.0208  0.1211  215 GLU   M OE2 
22972 N  N   . ASN   M  229 ? 2.0866 1.0997 1.3638 -0.0012 -0.0575 0.3033  216 ASN   M N   
22973 C  CA  . ASN   M  229 ? 2.1204 1.0309 1.4090 0.0269  -0.0512 0.2904  216 ASN   M CA  
22974 C  C   . ASN   M  229 ? 2.1559 0.9811 1.4372 0.0534  -0.0392 0.2910  216 ASN   M C   
22975 O  O   . ASN   M  229 ? 2.0870 0.9813 1.4570 0.0275  0.0051  0.2648  216 ASN   M O   
22976 C  CB  . ASN   M  229 ? 2.0981 1.0642 1.4968 0.0058  -0.0407 0.2890  216 ASN   M CB  
22977 C  CG  . ASN   M  229 ? 2.1205 1.1276 1.4756 0.0175  -0.0509 0.2986  216 ASN   M CG  
22978 O  OD1 . ASN   M  229 ? 2.1818 1.1357 1.4982 0.0214  -0.0473 0.3575  216 ASN   M OD1 
22979 N  ND2 . ASN   M  229 ? 2.1218 1.1387 1.5806 0.0199  -0.0613 0.3172  216 ASN   M ND2 
22980 N  N   . MET   M  230 ? 2.1657 0.9102 1.3914 0.0667  -0.1170 0.2919  217 MET   M N   
22981 C  CA  . MET   M  230 ? 2.1256 0.7617 1.4745 0.0387  -0.1385 0.2506  217 MET   M CA  
22982 C  C   . MET   M  230 ? 2.1610 0.7616 1.4586 0.1275  -0.1385 0.3230  217 MET   M C   
22983 O  O   . MET   M  230 ? 2.1967 0.4442 1.5117 0.1511  -0.1221 0.3452  217 MET   M O   
22984 C  CB  . MET   M  230 ? 2.1337 0.7644 1.5402 -0.0243 -0.1954 0.1879  217 MET   M CB  
22985 C  CG  . MET   M  230 ? 2.1513 0.7093 1.6417 -0.1211 -0.2335 0.0806  217 MET   M CG  
22986 S  SD  . MET   M  230 ? 2.1664 0.5947 1.7175 -0.2116 -0.2691 -0.0383 217 MET   M SD  
22987 C  CE  . MET   M  230 ? 2.1941 0.5303 1.7294 -0.1645 -0.2877 -0.0311 217 MET   M CE  
22988 N  N   . LYS   M  231 ? 2.1270 0.7583 1.5689 0.1570  -0.1255 0.2475  218 LYS   M N   
22989 C  CA  . LYS   M  231 ? 2.1102 0.7665 1.6642 0.1154  -0.1086 0.2198  218 LYS   M CA  
22990 C  C   . LYS   M  231 ? 2.0879 0.8380 1.6267 0.0535  -0.0952 0.1382  218 LYS   M C   
22991 O  O   . LYS   M  231 ? 2.1370 0.8193 1.6460 -0.0268 -0.0336 0.0769  218 LYS   M O   
22992 C  CB  . LYS   M  231 ? 2.0218 0.8287 1.7447 0.1677  -0.1277 0.2273  218 LYS   M CB  
22993 C  CG  . LYS   M  231 ? 2.0334 0.9240 1.7953 0.2380  -0.1313 0.2581  218 LYS   M CG  
22994 C  CD  . LYS   M  231 ? 2.0015 1.0195 1.8076 0.2945  -0.1616 0.2292  218 LYS   M CD  
22995 C  CE  . LYS   M  231 ? 2.0068 1.0636 1.8346 0.3368  -0.1459 0.2237  218 LYS   M CE  
22996 N  NZ  . LYS   M  231 ? 1.9583 1.0933 1.8639 0.3798  -0.1022 0.1665  218 LYS   M NZ  
22997 N  N   . TRP   M  232 ? 2.0399 0.9017 1.6194 0.0509  -0.1391 0.0854  219 TRP   M N   
22998 C  CA  . TRP   M  232 ? 1.9883 0.8682 1.5506 -0.0059 -0.1450 0.0639  219 TRP   M CA  
22999 C  C   . TRP   M  232 ? 2.0238 0.8601 1.5930 0.0114  -0.1062 0.0734  219 TRP   M C   
23000 O  O   . TRP   M  232 ? 2.0373 0.6541 1.5663 -0.0168 -0.1728 0.0985  219 TRP   M O   
23001 C  CB  . TRP   M  232 ? 1.9434 0.9492 1.4790 0.0072  -0.1335 0.0403  219 TRP   M CB  
23002 C  CG  . TRP   M  232 ? 1.8643 0.9957 1.3471 -0.0265 -0.1455 0.0307  219 TRP   M CG  
23003 C  CD1 . TRP   M  232 ? 1.9064 1.0095 1.3508 -0.0344 -0.1348 0.0153  219 TRP   M CD1 
23004 C  CD2 . TRP   M  232 ? 1.8111 0.9861 1.3140 -0.0030 -0.1687 -0.0322 219 TRP   M CD2 
23005 N  NE1 . TRP   M  232 ? 1.8802 1.0777 1.3026 -0.0578 -0.1128 -0.0126 219 TRP   M NE1 
23006 C  CE2 . TRP   M  232 ? 1.8341 0.9926 1.3443 -0.0575 -0.1518 -0.0508 219 TRP   M CE2 
23007 C  CE3 . TRP   M  232 ? 1.7620 0.9945 1.3268 -0.0010 -0.1645 -0.0224 219 TRP   M CE3 
23008 C  CZ2 . TRP   M  232 ? 1.7422 0.9980 1.3583 -0.0491 -0.1015 -0.1359 219 TRP   M CZ2 
23009 C  CZ3 . TRP   M  232 ? 1.7204 0.9839 1.3867 -0.0249 -0.1237 -0.0496 219 TRP   M CZ3 
23010 C  CH2 . TRP   M  232 ? 1.6983 0.9560 1.3922 -0.0489 -0.1049 -0.1187 219 TRP   M CH2 
23011 N  N   . ASP   M  233 ? 2.1059 0.8982 1.6460 -0.0408 -0.0590 0.1024  220 ASP   M N   
23012 C  CA  . ASP   M  233 ? 2.1418 0.9558 1.6604 -0.0957 0.0060  0.1405  220 ASP   M CA  
23013 C  C   . ASP   M  233 ? 2.0834 0.9302 1.6162 -0.1185 -0.0135 0.1711  220 ASP   M C   
23014 O  O   . ASP   M  233 ? 2.1600 0.8622 1.5943 -0.1614 0.0215  0.2989  220 ASP   M O   
23015 C  CB  . ASP   M  233 ? 2.1864 1.0998 1.7446 -0.1066 0.0716  0.0556  220 ASP   M CB  
23016 C  CG  . ASP   M  233 ? 2.2844 1.1395 1.7538 -0.1212 0.0787  0.0628  220 ASP   M CG  
23017 O  OD1 . ASP   M  233 ? 2.3664 1.3049 1.7240 -0.1657 0.0587  -0.1231 220 ASP   M OD1 
23018 O  OD2 . ASP   M  233 ? 2.3304 1.2054 1.9779 -0.1599 0.1000  -0.0812 220 ASP   M OD2 
23019 N  N   . PHE   M  234 ? 2.0017 0.8701 1.6515 -0.1694 -0.0255 0.1369  221 PHE   M N   
23020 C  CA  . PHE   M  234 ? 1.9198 0.7922 1.6791 -0.1720 -0.0308 0.1620  221 PHE   M CA  
23021 C  C   . PHE   M  234 ? 1.9329 0.6942 1.6397 -0.1590 -0.0304 0.1300  221 PHE   M C   
23022 O  O   . PHE   M  234 ? 1.8773 0.6690 1.6492 -0.0889 0.0232  0.1672  221 PHE   M O   
23023 C  CB  . PHE   M  234 ? 1.9235 0.7531 1.6570 -0.1933 -0.0292 0.1588  221 PHE   M CB  
23024 C  CG  . PHE   M  234 ? 1.8768 0.6968 1.6146 -0.1569 -0.0511 0.1385  221 PHE   M CG  
23025 C  CD1 . PHE   M  234 ? 1.9057 0.7097 1.5950 -0.1121 -0.0565 0.1608  221 PHE   M CD1 
23026 C  CD2 . PHE   M  234 ? 1.8328 0.6099 1.6089 -0.1483 -0.0545 0.1740  221 PHE   M CD2 
23027 C  CE1 . PHE   M  234 ? 1.8672 0.7673 1.5189 -0.1126 -0.0200 0.1460  221 PHE   M CE1 
23028 C  CE2 . PHE   M  234 ? 1.8021 0.6981 1.5111 -0.1238 -0.0339 0.1938  221 PHE   M CE2 
23029 C  CZ  . PHE   M  234 ? 1.8122 0.7375 1.5211 -0.1142 -0.0334 0.1303  221 PHE   M CZ  
23030 N  N   . ALA   M  235 ? 1.8766 0.7392 1.6050 -0.1435 -0.0236 0.1277  222 ALA   M N   
23031 C  CA  . ALA   M  235 ? 1.8711 0.6240 1.5624 -0.0936 -0.0492 0.1533  222 ALA   M CA  
23032 C  C   . ALA   M  235 ? 1.8798 0.5533 1.5959 -0.1103 -0.0358 0.1314  222 ALA   M C   
23033 O  O   . ALA   M  235 ? 1.8570 0.3575 1.6162 -0.0902 -0.0877 0.1712  222 ALA   M O   
23034 C  CB  . ALA   M  235 ? 1.8638 0.7039 1.5406 -0.1444 -0.0484 0.1468  222 ALA   M CB  
23035 N  N   . LYS   M  236 ? 1.8842 0.5787 1.6087 -0.0897 -0.0302 0.1615  223 LYS   M N   
23036 C  CA  . LYS   M  236 ? 1.8961 0.6598 1.6201 -0.0796 -0.0359 0.2170  223 LYS   M CA  
23037 C  C   . LYS   M  236 ? 1.8628 0.5763 1.6511 -0.0818 -0.0355 0.2859  223 LYS   M C   
23038 O  O   . LYS   M  236 ? 1.9179 0.4600 1.6347 -0.1171 -0.0473 0.3872  223 LYS   M O   
23039 C  CB  . LYS   M  236 ? 1.9290 0.7359 1.6171 -0.0626 -0.0345 0.2203  223 LYS   M CB  
23040 C  CG  . LYS   M  236 ? 1.9314 0.8208 1.6326 -0.0751 -0.0135 0.2013  223 LYS   M CG  
23041 C  CD  . LYS   M  236 ? 1.9825 0.8821 1.6460 -0.0791 -0.0195 0.2493  223 LYS   M CD  
23042 C  CE  . LYS   M  236 ? 1.9780 0.9869 1.6874 -0.1167 -0.0192 0.2292  223 LYS   M CE  
23043 N  NZ  . LYS   M  236 ? 1.9442 1.0323 1.6783 -0.1140 -0.0595 0.2106  223 LYS   M NZ  
23044 N  N   . ASP   M  237 ? 1.8585 0.6092 1.6638 -0.1231 -0.0315 0.2850  224 ASP   M N   
23045 C  CA  . ASP   M  237 ? 1.8278 0.6461 1.6752 -0.1133 -0.0473 0.2486  224 ASP   M CA  
23046 C  C   . ASP   M  237 ? 1.7929 0.6150 1.6309 -0.0980 -0.1026 0.2462  224 ASP   M C   
23047 O  O   . ASP   M  237 ? 1.7842 0.6877 1.6230 -0.1174 -0.1046 0.1875  224 ASP   M O   
23048 C  CB  . ASP   M  237 ? 1.8257 0.7352 1.7131 -0.1206 -0.0398 0.2423  224 ASP   M CB  
23049 C  CG  . ASP   M  237 ? 1.8362 0.8627 1.7622 -0.1095 0.0039  0.2273  224 ASP   M CG  
23050 O  OD1 . ASP   M  237 ? 1.8683 0.7082 1.7535 -0.1485 -0.0063 0.2194  224 ASP   M OD1 
23051 O  OD2 . ASP   M  237 ? 1.9157 1.0551 1.8055 -0.0757 -0.0030 0.3142  224 ASP   M OD2 
23052 N  N   . ILE   M  238 ? 1.7617 0.5756 1.5509 -0.0900 -0.1369 0.2014  225 ILE   M N   
23053 C  CA  . ILE   M  238 ? 1.7557 0.5887 1.5544 -0.0584 -0.1443 0.1624  225 ILE   M CA  
23054 C  C   . ILE   M  238 ? 1.7838 0.6010 1.5567 -0.0317 -0.1776 0.1925  225 ILE   M C   
23055 O  O   . ILE   M  238 ? 1.7815 0.5575 1.5501 0.0066  -0.1699 0.1685  225 ILE   M O   
23056 C  CB  . ILE   M  238 ? 1.7409 0.5733 1.5554 -0.0639 -0.1083 0.1515  225 ILE   M CB  
23057 C  CG1 . ILE   M  238 ? 1.7374 0.5876 1.5910 -0.0699 -0.1093 0.1516  225 ILE   M CG1 
23058 C  CG2 . ILE   M  238 ? 1.7134 0.5409 1.5570 -0.0591 -0.1143 0.1374  225 ILE   M CG2 
23059 C  CD1 . ILE   M  238 ? 1.7428 0.6107 1.5872 -0.0605 -0.1143 0.1680  225 ILE   M CD1 
23060 N  N   . LYS   M  239 ? 1.8278 0.6309 1.5729 -0.0344 -0.1721 0.1606  226 LYS   M N   
23061 C  CA  . LYS   M  239 ? 1.8248 0.7293 1.6435 -0.0214 -0.1413 0.1542  226 LYS   M CA  
23062 C  C   . LYS   M  239 ? 1.8713 0.6683 1.6441 -0.0251 -0.1419 0.1485  226 LYS   M C   
23063 O  O   . LYS   M  239 ? 1.8078 0.6515 1.7009 -0.0686 -0.1294 0.1944  226 LYS   M O   
23064 C  CB  . LYS   M  239 ? 1.8999 0.7384 1.7361 -0.0134 -0.1117 0.1879  226 LYS   M CB  
23065 C  CG  . LYS   M  239 ? 1.9608 0.8334 1.7568 0.0080  -0.0472 0.2188  226 LYS   M CG  
23066 C  CD  . LYS   M  239 ? 1.9994 0.8214 1.8918 -0.0091 0.0063  0.2074  226 LYS   M CD  
23067 C  CE  . LYS   M  239 ? 2.0633 0.9419 1.8945 -0.0050 0.0512  0.2503  226 LYS   M CE  
23068 N  NZ  . LYS   M  239 ? 2.1153 0.9935 1.9281 0.0086  0.0747  0.2116  226 LYS   M NZ  
23069 N  N   . GLY   M  240 ? 1.8886 0.5972 1.6411 0.0095  -0.1142 0.1510  227 GLY   M N   
23070 C  CA  . GLY   M  240 ? 1.9307 0.5653 1.6828 0.0663  -0.0915 0.1336  227 GLY   M CA  
23071 C  C   . GLY   M  240 ? 1.9271 0.4939 1.6455 0.0405  -0.0917 0.0865  227 GLY   M C   
23072 O  O   . GLY   M  240 ? 1.9422 0.3129 1.7385 -0.0562 -0.1109 0.0130  227 GLY   M O   
23073 N  N   . TYR   M  241 ? 1.9002 0.5162 1.6462 0.0619  -0.0950 0.0895  228 TYR   M N   
23074 C  CA  . TYR   M  241 ? 1.8487 0.4361 1.6522 0.0461  -0.0530 0.1191  228 TYR   M CA  
23075 C  C   . TYR   M  241 ? 1.8278 0.5352 1.6273 0.0755  -0.1052 0.1064  228 TYR   M C   
23076 O  O   . TYR   M  241 ? 1.7893 0.4148 1.6464 0.1535  -0.0628 0.1582  228 TYR   M O   
23077 C  CB  . TYR   M  241 ? 1.8763 0.3303 1.5548 0.0459  -0.0799 0.1448  228 TYR   M CB  
23078 C  CG  . TYR   M  241 ? 1.8680 0.3392 1.5623 0.0430  -0.0502 0.1822  228 TYR   M CG  
23079 C  CD1 . TYR   M  241 ? 1.9014 0.4296 1.5621 0.0692  -0.0396 0.1361  228 TYR   M CD1 
23080 C  CD2 . TYR   M  241 ? 1.8590 0.3038 1.5690 0.0363  -0.0517 0.2167  228 TYR   M CD2 
23081 C  CE1 . TYR   M  241 ? 1.8963 0.4967 1.6208 0.1094  -0.0575 0.1509  228 TYR   M CE1 
23082 C  CE2 . TYR   M  241 ? 1.8341 0.3845 1.5989 0.0591  -0.0642 0.2152  228 TYR   M CE2 
23083 C  CZ  . TYR   M  241 ? 1.8842 0.4531 1.6214 0.1012  -0.0531 0.1649  228 TYR   M CZ  
23084 O  OH  . TYR   M  241 ? 1.8591 0.5834 1.7122 0.1390  -0.0527 0.1819  228 TYR   M OH  
23085 N  N   . GLY   M  242 ? 1.8434 0.5749 1.7641 0.0159  -0.0986 0.1274  229 GLY   M N   
23086 C  CA  . GLY   M  242 ? 1.8447 0.6394 1.7534 0.0309  -0.1546 0.1165  229 GLY   M CA  
23087 C  C   . GLY   M  242 ? 1.8821 0.6539 1.7968 0.0899  -0.1975 0.1505  229 GLY   M C   
23088 O  O   . GLY   M  242 ? 1.7941 0.6044 1.7470 0.1458  -0.2893 0.2189  229 GLY   M O   
23089 N  N   . THR   M  243 ? 1.9132 0.6780 1.8480 0.1147  -0.1571 0.0914  230 THR   M N   
23090 C  CA  . THR   M  243 ? 1.9728 0.6837 1.9538 0.0520  -0.0993 0.1126  230 THR   M CA  
23091 C  C   . THR   M  243 ? 2.0034 0.7608 1.9712 0.0376  -0.1168 0.1369  230 THR   M C   
23092 O  O   . THR   M  243 ? 2.0685 0.7849 2.0910 0.1279  -0.0871 0.2056  230 THR   M O   
23093 C  CB  . THR   M  243 ? 1.9527 0.7074 1.9957 0.0678  -0.0863 0.1196  230 THR   M CB  
23094 O  OG1 . THR   M  243 ? 1.9106 0.6999 1.9668 0.1258  -0.1039 0.1163  230 THR   M OG1 
23095 C  CG2 . THR   M  243 ? 1.9547 0.6839 1.9927 0.0562  -0.0754 0.1124  230 THR   M CG2 
23096 N  N   . GLN   M  244 ? 2.0005 0.8035 1.9583 -0.0467 -0.1150 0.1781  231 GLN   M N   
23097 C  CA  . GLN   M  244 ? 1.9995 0.8437 1.9536 -0.1353 -0.1192 0.1714  231 GLN   M CA  
23098 C  C   . GLN   M  244 ? 2.0324 0.8483 1.9258 -0.2434 -0.1232 0.1687  231 GLN   M C   
23099 O  O   . GLN   M  244 ? 2.0107 0.8049 1.8449 -0.2886 -0.1509 0.1846  231 GLN   M O   
23100 C  CB  . GLN   M  244 ? 1.9718 0.8813 1.9372 -0.1501 -0.1184 0.1733  231 GLN   M CB  
23101 C  CG  . GLN   M  244 ? 1.9427 0.9494 1.9676 -0.1543 -0.1168 0.2314  231 GLN   M CG  
23102 C  CD  . GLN   M  244 ? 1.8993 0.9531 1.9654 -0.1381 -0.1006 0.2969  231 GLN   M CD  
23103 O  OE1 . GLN   M  244 ? 1.8993 0.8380 1.9847 -0.0745 -0.0840 0.3473  231 GLN   M OE1 
23104 N  NE2 . GLN   M  244 ? 1.8911 0.9896 1.9375 -0.1799 -0.1387 0.3068  231 GLN   M NE2 
23105 N  N   . LYS   M  245 ? 2.0842 0.8932 1.9515 -0.2814 -0.0968 0.2094  232 LYS   M N   
23106 C  CA  . LYS   M  245 ? 2.1287 0.9224 2.0413 -0.2940 -0.0540 0.2669  232 LYS   M CA  
23107 C  C   . LYS   M  245 ? 2.1934 1.0212 2.0494 -0.3748 -0.0477 0.2563  232 LYS   M C   
23108 O  O   . LYS   M  245 ? 2.2597 1.0591 2.1110 -0.4532 -0.0022 0.3242  232 LYS   M O   
23109 C  CB  . LYS   M  245 ? 2.0986 0.9037 2.0417 -0.2368 -0.0469 0.2835  232 LYS   M CB  
23110 C  CG  . LYS   M  245 ? 2.0681 0.7482 2.0620 -0.2275 -0.0256 0.2892  232 LYS   M CG  
23111 C  CD  . LYS   M  245 ? 2.1001 0.7295 2.1215 -0.1707 -0.0188 0.3319  232 LYS   M CD  
23112 C  CE  . LYS   M  245 ? 2.1350 0.6586 2.1229 -0.1499 -0.0153 0.3113  232 LYS   M CE  
23113 N  NZ  . LYS   M  245 ? 2.1912 0.6481 2.1958 -0.1304 -0.0083 0.2906  232 LYS   M NZ  
23114 N  N   . ILE   M  246 ? 2.2214 1.1026 2.1697 -0.4164 -0.0629 0.2416  233 ILE   M N   
23115 C  CA  . ILE   M  246 ? 2.2577 1.2153 2.1126 -0.2950 -0.1030 0.2708  233 ILE   M CA  
23116 C  C   . ILE   M  246 ? 2.2906 1.2594 2.1743 -0.3388 -0.0541 0.2257  233 ILE   M C   
23117 O  O   . ILE   M  246 ? 2.2675 1.4807 2.1792 -0.4024 -0.0668 0.2304  233 ILE   M O   
23118 C  CB  . ILE   M  246 ? 2.2313 1.1581 2.2067 -0.2538 -0.0616 0.2926  233 ILE   M CB  
23119 C  CG1 . ILE   M  246 ? 2.1806 1.1789 2.1442 -0.1746 -0.0891 0.3582  233 ILE   M CG1 
23120 C  CG2 . ILE   M  246 ? 2.2132 1.0147 2.1920 -0.2363 -0.1316 0.2803  233 ILE   M CG2 
23121 C  CD1 . ILE   M  246 ? 2.1637 1.1592 2.1979 -0.1447 -0.0602 0.3869  233 ILE   M CD1 
23122 O  OXT . ILE   M  246 ? 2.3149 1.1848 2.2494 -0.3096 -0.0277 0.2640  233 ILE   M OXT 
23123 N  N   . THR   N  1   ? 1.5846 0.6945 1.2580 -0.0768 -0.1919 -0.0518 1   THR   N N   
23124 C  CA  . THR   N  1   ? 1.6106 0.6384 1.2508 -0.0438 -0.1723 -0.0156 1   THR   N CA  
23125 C  C   . THR   N  1   ? 1.6019 0.5997 1.2014 -0.0617 -0.1993 -0.0464 1   THR   N C   
23126 O  O   . THR   N  1   ? 1.5791 0.6232 1.2669 -0.0769 -0.1785 -0.0215 1   THR   N O   
23127 C  CB  . THR   N  1   ? 1.6443 0.6012 1.2495 -0.0353 -0.1326 -0.0335 1   THR   N CB  
23128 O  OG1 . THR   N  1   ? 1.6562 0.5898 1.3668 -0.0408 -0.0717 -0.0520 1   THR   N OG1 
23129 C  CG2 . THR   N  1   ? 1.6499 0.6105 1.1689 -0.0418 -0.1614 -0.0152 1   THR   N CG2 
23130 N  N   . SER   N  2   ? 1.6288 0.5314 1.1892 -0.0461 -0.2006 -0.0348 2   SER   N N   
23131 C  CA  . SER   N  2   ? 1.6297 0.5605 1.1575 -0.0450 -0.2233 -0.0126 2   SER   N CA  
23132 C  C   . SER   N  2   ? 1.6493 0.5532 1.1020 0.0055  -0.2380 0.0137  2   SER   N C   
23133 O  O   . SER   N  2   ? 1.6415 0.5413 1.1056 0.0034  -0.2473 0.0779  2   SER   N O   
23134 C  CB  . SER   N  2   ? 1.6115 0.5907 1.1853 -0.0729 -0.2439 0.0164  2   SER   N CB  
23135 O  OG  . SER   N  2   ? 1.5843 0.6634 1.2065 -0.0501 -0.2245 -0.0246 2   SER   N OG  
23136 N  N   . ILE   N  3   ? 1.6469 0.5233 1.0300 -0.0001 -0.2537 -0.0064 3   ILE   N N   
23137 C  CA  . ILE   N  3   ? 1.6321 0.5357 0.9922 -0.0001 -0.2437 -0.0157 3   ILE   N CA  
23138 C  C   . ILE   N  3   ? 1.6339 0.3852 0.9253 -0.0405 -0.2563 0.0322  3   ILE   N C   
23139 O  O   . ILE   N  3   ? 1.6371 0.3472 0.7752 -0.0355 -0.2249 0.0203  3   ILE   N O   
23140 C  CB  . ILE   N  3   ? 1.6362 0.5345 0.9859 0.0286  -0.2655 -0.0301 3   ILE   N CB  
23141 C  CG1 . ILE   N  3   ? 1.6276 0.5558 1.0123 0.0385  -0.2732 -0.0721 3   ILE   N CG1 
23142 C  CG2 . ILE   N  3   ? 1.6268 0.5855 1.0349 0.0306  -0.2563 -0.0675 3   ILE   N CG2 
23143 C  CD1 . ILE   N  3   ? 1.6226 0.6062 0.9761 0.0616  -0.2912 -0.0583 3   ILE   N CD1 
23144 N  N   . MET   N  4   ? 1.6781 0.4527 0.8782 0.0044  -0.2051 0.0630  4   MET   N N   
23145 C  CA  . MET   N  4   ? 1.6598 0.5365 0.9420 0.0210  -0.2036 0.0643  4   MET   N CA  
23146 C  C   . MET   N  4   ? 1.6441 0.5243 0.9180 0.0493  -0.2290 0.0785  4   MET   N C   
23147 O  O   . MET   N  4   ? 1.6603 0.5292 0.8833 0.0502  -0.2853 0.0477  4   MET   N O   
23148 C  CB  . MET   N  4   ? 1.6890 0.5326 0.9895 0.0107  -0.1971 0.0681  4   MET   N CB  
23149 C  CG  . MET   N  4   ? 1.6798 0.6404 1.0198 0.0030  -0.2218 0.0134  4   MET   N CG  
23150 S  SD  . MET   N  4   ? 1.6704 0.6276 1.0724 -0.0117 -0.2044 -0.0014 4   MET   N SD  
23151 C  CE  . MET   N  4   ? 1.7037 0.6604 1.1021 -0.0132 -0.1641 -0.0307 4   MET   N CE  
23152 N  N   . ALA   N  5   ? 1.6810 0.5052 0.9217 0.0921  -0.2210 0.0871  5   ALA   N N   
23153 C  CA  . ALA   N  5   ? 1.7274 0.5447 0.8835 0.0788  -0.2261 0.0815  5   ALA   N CA  
23154 C  C   . ALA   N  5   ? 1.7530 0.4899 0.8762 0.0557  -0.2413 0.1023  5   ALA   N C   
23155 O  O   . ALA   N  5   ? 1.7591 0.4637 0.8661 0.0163  -0.2276 0.1694  5   ALA   N O   
23156 C  CB  . ALA   N  5   ? 1.7418 0.5518 0.8581 0.0769  -0.2040 0.0916  5   ALA   N CB  
23157 N  N   . VAL   N  6   ? 1.7977 0.5055 0.8828 0.0728  -0.2539 0.0998  6   VAL   N N   
23158 C  CA  . VAL   N  6   ? 1.7941 0.4747 0.9393 0.0583  -0.2190 0.0670  6   VAL   N CA  
23159 C  C   . VAL   N  6   ? 1.7891 0.4680 0.9807 0.0293  -0.2425 0.0412  6   VAL   N C   
23160 O  O   . VAL   N  6   ? 1.8922 0.3134 0.9442 0.0300  -0.2716 -0.0140 6   VAL   N O   
23161 C  CB  . VAL   N  6   ? 1.7947 0.5003 0.9908 0.0821  -0.2468 0.0722  6   VAL   N CB  
23162 C  CG1 . VAL   N  6   ? 1.8031 0.5052 0.9969 0.0960  -0.2518 0.1036  6   VAL   N CG1 
23163 C  CG2 . VAL   N  6   ? 1.7545 0.5340 0.9903 0.0645  -0.2432 0.0516  6   VAL   N CG2 
23164 N  N   . THR   N  7   ? 1.8356 0.4560 0.9490 0.0646  -0.2084 -0.0426 7   THR   N N   
23165 C  CA  . THR   N  7   ? 1.8658 0.4955 0.9591 0.0147  -0.2284 -0.1101 7   THR   N CA  
23166 C  C   . THR   N  7   ? 1.9257 0.5675 0.9838 0.0357  -0.2489 -0.0638 7   THR   N C   
23167 O  O   . THR   N  7   ? 1.9234 0.6807 0.9711 -0.0554 -0.2468 -0.1261 7   THR   N O   
23168 C  CB  . THR   N  7   ? 1.8485 0.4914 0.9133 0.0330  -0.1974 -0.1909 7   THR   N CB  
23169 O  OG1 . THR   N  7   ? 1.8592 0.4103 0.9327 0.0453  -0.1695 -0.2418 7   THR   N OG1 
23170 C  CG2 . THR   N  7   ? 1.8027 0.5163 0.9092 0.0375  -0.1850 -0.1882 7   THR   N CG2 
23171 N  N   . PHE   N  8   ? 1.9289 0.5599 0.9927 0.0073  -0.2779 -0.0124 8   PHE   N N   
23172 C  CA  . PHE   N  8   ? 1.9619 0.6912 1.0092 0.0316  -0.2587 0.0363  8   PHE   N CA  
23173 C  C   . PHE   N  8   ? 1.9760 0.7622 1.0527 0.0771  -0.2217 0.0062  8   PHE   N C   
23174 O  O   . PHE   N  8   ? 1.9004 0.9210 1.0719 0.1942  -0.2033 0.0645  8   PHE   N O   
23175 C  CB  . PHE   N  8   ? 1.9613 0.7567 0.9697 0.0357  -0.2794 0.0322  8   PHE   N CB  
23176 C  CG  . PHE   N  8   ? 1.9698 0.7351 0.9272 0.0412  -0.2977 0.0299  8   PHE   N CG  
23177 C  CD1 . PHE   N  8   ? 1.9546 0.7588 0.9363 0.0529  -0.2762 0.0229  8   PHE   N CD1 
23178 C  CD2 . PHE   N  8   ? 2.0104 0.7672 0.9210 0.0452  -0.2964 0.0068  8   PHE   N CD2 
23179 C  CE1 . PHE   N  8   ? 1.9527 0.8253 0.9023 0.0394  -0.3123 -0.0301 8   PHE   N CE1 
23180 C  CE2 . PHE   N  8   ? 2.0197 0.7897 0.9086 0.0336  -0.3210 -0.0128 8   PHE   N CE2 
23181 C  CZ  . PHE   N  8   ? 1.9955 0.8217 0.8920 0.0281  -0.3181 -0.0310 8   PHE   N CZ  
23182 N  N   . LYS   N  9   ? 2.0225 0.8303 1.0774 0.0779  -0.2409 0.0715  9   LYS   N N   
23183 C  CA  . LYS   N  9   ? 2.0404 0.8944 1.1360 0.0749  -0.2074 0.0336  9   LYS   N CA  
23184 C  C   . LYS   N  9   ? 2.0161 0.8380 1.1382 0.1241  -0.2533 0.0330  9   LYS   N C   
23185 O  O   . LYS   N  9   ? 2.0356 0.7357 1.2110 0.0722  -0.2696 0.0171  9   LYS   N O   
23186 C  CB  . LYS   N  9   ? 2.1095 1.0019 1.1447 0.0541  -0.2028 0.0687  9   LYS   N CB  
23187 C  CG  . LYS   N  9   ? 2.1491 1.1008 1.1838 0.0274  -0.1707 0.1145  9   LYS   N CG  
23188 C  CD  . LYS   N  9   ? 2.1857 1.1838 1.1858 0.0102  -0.1739 0.1040  9   LYS   N CD  
23189 C  CE  . LYS   N  9   ? 2.2059 1.2467 1.2430 0.0265  -0.2341 0.1685  9   LYS   N CE  
23190 N  NZ  . LYS   N  9   ? 2.2202 1.2827 1.2812 0.0330  -0.2896 0.2005  9   LYS   N NZ  
23191 N  N   . ASP   N  10  ? 2.0244 0.8659 1.1288 0.0658  -0.2442 0.0201  10  ASP   N N   
23192 C  CA  . ASP   N  10  ? 2.0640 0.8312 1.0724 0.0776  -0.2339 0.0296  10  ASP   N CA  
23193 C  C   . ASP   N  10  ? 2.0258 0.7402 1.0587 0.0951  -0.2400 0.0058  10  ASP   N C   
23194 O  O   . ASP   N  10  ? 2.0575 0.7283 0.9895 0.1290  -0.1975 0.0350  10  ASP   N O   
23195 C  CB  . ASP   N  10  ? 2.0516 0.9451 1.1276 0.0391  -0.2534 -0.0302 10  ASP   N CB  
23196 C  CG  . ASP   N  10  ? 2.1117 1.0393 1.1147 0.0291  -0.2885 -0.0363 10  ASP   N CG  
23197 O  OD1 . ASP   N  10  ? 2.1370 1.1876 1.1972 0.0224  -0.2428 -0.0865 10  ASP   N OD1 
23198 O  OD2 . ASP   N  10  ? 2.0772 1.1180 1.2247 0.0041  -0.2987 -0.0499 10  ASP   N OD2 
23199 N  N   . GLY   N  11  ? 2.0096 0.6034 1.0292 0.0750  -0.2390 0.0761  11  GLY   N N   
23200 C  CA  . GLY   N  11  ? 1.9783 0.5481 1.0368 0.0464  -0.2423 0.0752  11  GLY   N CA  
23201 C  C   . GLY   N  11  ? 1.9373 0.5159 1.0065 0.0185  -0.2483 0.1047  11  GLY   N C   
23202 O  O   . GLY   N  11  ? 1.9200 0.5713 0.9534 0.0064  -0.2788 0.1013  11  GLY   N O   
23203 N  N   . VAL   N  12  ? 1.9266 0.5762 0.9976 -0.0158 -0.2537 0.1131  12  VAL   N N   
23204 C  CA  . VAL   N  12  ? 1.9045 0.6406 0.9782 -0.0153 -0.2422 0.1115  12  VAL   N CA  
23205 C  C   . VAL   N  12  ? 1.8883 0.6563 1.0028 -0.0368 -0.2534 0.0976  12  VAL   N C   
23206 O  O   . VAL   N  12  ? 1.9250 0.6922 0.9987 -0.0725 -0.2602 0.0773  12  VAL   N O   
23207 C  CB  . VAL   N  12  ? 1.8894 0.6506 1.0070 -0.0146 -0.2393 0.1437  12  VAL   N CB  
23208 C  CG1 . VAL   N  12  ? 1.9083 0.6668 1.0431 -0.0414 -0.2346 0.1357  12  VAL   N CG1 
23209 C  CG2 . VAL   N  12  ? 1.8441 0.6480 0.9885 -0.0109 -0.2514 0.1503  12  VAL   N CG2 
23210 N  N   . ILE   N  13  ? 1.8498 0.6586 0.9966 0.0190  -0.2341 0.1218  13  ILE   N N   
23211 C  CA  . ILE   N  13  ? 1.8326 0.5996 0.9866 -0.0024 -0.2521 0.0865  13  ILE   N CA  
23212 C  C   . ILE   N  13  ? 1.7651 0.4583 1.0200 0.0014  -0.2639 0.0648  13  ILE   N C   
23213 O  O   . ILE   N  13  ? 1.7602 0.3512 1.0121 0.0182  -0.2250 0.0677  13  ILE   N O   
23214 C  CB  . ILE   N  13  ? 1.8720 0.5750 1.0132 -0.0230 -0.2550 0.0951  13  ILE   N CB  
23215 C  CG1 . ILE   N  13  ? 1.9073 0.6554 1.0135 -0.0255 -0.2580 0.0810  13  ILE   N CG1 
23216 C  CG2 . ILE   N  13  ? 1.8641 0.5302 1.0416 -0.0515 -0.2464 0.0832  13  ILE   N CG2 
23217 C  CD1 . ILE   N  13  ? 1.9202 0.6580 0.9869 -0.0371 -0.2761 0.0770  13  ILE   N CD1 
23218 N  N   . LEU   N  14  ? 1.7561 0.4707 0.9946 0.0223  -0.2620 0.0186  14  LEU   N N   
23219 C  CA  . LEU   N  14  ? 1.7780 0.5276 0.9995 0.0078  -0.2780 -0.0092 14  LEU   N CA  
23220 C  C   . LEU   N  14  ? 1.7330 0.6072 0.9689 0.0143  -0.3229 0.0240  14  LEU   N C   
23221 O  O   . LEU   N  14  ? 1.7782 0.6815 1.0190 -0.0253 -0.3543 -0.0444 14  LEU   N O   
23222 C  CB  . LEU   N  14  ? 1.7842 0.5310 1.0028 -0.0039 -0.2679 -0.0151 14  LEU   N CB  
23223 C  CG  . LEU   N  14  ? 1.7679 0.6035 1.0652 0.0193  -0.2579 0.0096  14  LEU   N CG  
23224 C  CD1 . LEU   N  14  ? 1.8026 0.6462 1.0488 0.0003  -0.2529 0.0175  14  LEU   N CD1 
23225 C  CD2 . LEU   N  14  ? 1.7860 0.6015 1.0650 -0.0175 -0.2506 -0.0018 14  LEU   N CD2 
23226 N  N   . GLY   N  15  ? 1.7508 0.5636 0.9315 0.0117  -0.3130 0.0784  15  GLY   N N   
23227 C  CA  . GLY   N  15  ? 1.7120 0.5973 0.8342 0.0231  -0.3252 0.1034  15  GLY   N CA  
23228 C  C   . GLY   N  15  ? 1.6397 0.6162 0.8052 0.0299  -0.3405 0.1362  15  GLY   N C   
23229 O  O   . GLY   N  15  ? 1.6701 0.6606 0.6702 0.0289  -0.3232 0.0964  15  GLY   N O   
23230 N  N   . ALA   N  16  ? 1.6227 0.6455 0.7625 0.0072  -0.3465 0.1396  16  ALA   N N   
23231 C  CA  . ALA   N  16  ? 1.6118 0.6583 0.7764 0.0016  -0.3482 0.1145  16  ALA   N CA  
23232 C  C   . ALA   N  16  ? 1.5959 0.6456 0.8271 -0.0175 -0.3451 0.1256  16  ALA   N C   
23233 O  O   . ALA   N  16  ? 1.5676 0.6531 0.8383 -0.1050 -0.3287 0.0675  16  ALA   N O   
23234 C  CB  . ALA   N  16  ? 1.6296 0.6150 0.7811 0.0157  -0.3570 0.0889  16  ALA   N CB  
23235 N  N   . ASP   N  17  ? 1.5968 0.5727 0.8872 -0.0091 -0.3450 0.1162  17  ASP   N N   
23236 C  CA  . ASP   N  17  ? 1.6183 0.6128 0.9840 0.0377  -0.3794 0.1050  17  ASP   N CA  
23237 C  C   . ASP   N  17  ? 1.5243 0.7237 1.0387 0.0168  -0.3788 0.0942  17  ASP   N C   
23238 O  O   . ASP   N  17  ? 1.4709 0.8460 1.0727 0.1467  -0.4245 0.1740  17  ASP   N O   
23239 C  CB  . ASP   N  17  ? 1.6678 0.6167 1.0195 0.0531  -0.3694 0.0872  17  ASP   N CB  
23240 C  CG  . ASP   N  17  ? 1.7172 0.5723 1.0391 0.0966  -0.3816 0.1017  17  ASP   N CG  
23241 O  OD1 . ASP   N  17  ? 1.7635 0.5449 1.0816 0.0887  -0.3812 0.1096  17  ASP   N OD1 
23242 O  OD2 . ASP   N  17  ? 1.7846 0.5945 1.0560 0.0850  -0.4328 0.0566  17  ASP   N OD2 
23243 N  N   . SER   N  18  ? 1.5580 0.5215 1.0827 0.0700  -0.4204 0.0654  18  SER   N N   
23244 C  CA  . SER   N  18  ? 1.5425 0.5045 1.0771 0.0950  -0.4238 0.0784  18  SER   N CA  
23245 C  C   . SER   N  18  ? 1.5463 0.3875 1.1221 0.1001  -0.4135 0.0608  18  SER   N C   
23246 O  O   . SER   N  18  ? 1.5659 0.3380 1.1772 0.0914  -0.4057 0.0837  18  SER   N O   
23247 C  CB  . SER   N  18  ? 1.5718 0.5013 1.0528 0.1335  -0.4515 0.1014  18  SER   N CB  
23248 O  OG  . SER   N  18  ? 1.6189 0.4098 0.9986 0.1051  -0.4951 0.1223  18  SER   N OG  
23249 N  N   . ARG   N  19  ? 1.4957 0.4225 1.1485 0.1073  -0.4196 0.0543  19  ARG   N N   
23250 C  CA  . ARG   N  19  ? 1.4876 0.4979 1.1797 0.1123  -0.4066 0.0174  19  ARG   N CA  
23251 C  C   . ARG   N  19  ? 1.4545 0.4417 1.1740 0.1159  -0.3778 0.0226  19  ARG   N C   
23252 O  O   . ARG   N  19  ? 1.4541 0.3873 1.2023 0.0750  -0.3776 -0.0206 19  ARG   N O   
23253 C  CB  . ARG   N  19  ? 1.4815 0.5102 1.2242 0.0624  -0.3998 -0.0095 19  ARG   N CB  
23254 C  CG  . ARG   N  19  ? 1.4532 0.5840 1.2401 0.0713  -0.3921 -0.0356 19  ARG   N CG  
23255 C  CD  . ARG   N  19  ? 1.4111 0.5807 1.2734 0.0916  -0.4103 -0.0283 19  ARG   N CD  
23256 N  NE  . ARG   N  19  ? 1.4071 0.5462 1.3127 0.0968  -0.4093 -0.0213 19  ARG   N NE  
23257 C  CZ  . ARG   N  19  ? 1.3441 0.5367 1.3418 0.1006  -0.4502 -0.0402 19  ARG   N CZ  
23258 N  NH1 . ARG   N  19  ? 1.3325 0.5535 1.3926 0.1002  -0.4309 -0.0529 19  ARG   N NH1 
23259 N  NH2 . ARG   N  19  ? 1.3261 0.6074 1.3703 0.0737  -0.4829 -0.0700 19  ARG   N NH2 
23260 N  N   . THR   N  20  ? 1.4933 0.4583 1.1501 0.1300  -0.3840 0.0457  20  THR   N N   
23261 C  CA  . THR   N  20  ? 1.4860 0.5312 1.1543 0.1095  -0.4057 0.0377  20  THR   N CA  
23262 C  C   . THR   N  20  ? 1.4584 0.4328 1.1781 0.1162  -0.4412 0.0404  20  THR   N C   
23263 O  O   . THR   N  20  ? 1.4736 0.3073 1.1529 0.2243  -0.4532 0.0986  20  THR   N O   
23264 C  CB  . THR   N  20  ? 1.5043 0.5488 1.1784 0.0522  -0.4265 0.0345  20  THR   N CB  
23265 O  OG1 . THR   N  20  ? 1.5222 0.5298 1.2072 0.0754  -0.3995 0.1147  20  THR   N OG1 
23266 C  CG2 . THR   N  20  ? 1.5159 0.6106 1.2070 0.0214  -0.4166 0.0009  20  THR   N CG2 
23267 N  N   . THR   N  21  ? 1.4424 0.4711 1.1878 0.0736  -0.3974 0.0111  21  THR   N N   
23268 C  CA  . THR   N  21  ? 1.4141 0.5281 1.1705 0.0330  -0.3752 -0.0127 21  THR   N CA  
23269 C  C   . THR   N  21  ? 1.4183 0.5941 1.1205 0.0124  -0.3424 -0.0656 21  THR   N C   
23270 O  O   . THR   N  21  ? 1.3745 0.6649 1.0995 -0.0173 -0.3573 -0.0680 21  THR   N O   
23271 C  CB  . THR   N  21  ? 1.3504 0.5608 1.2009 -0.0384 -0.3892 -0.0449 21  THR   N CB  
23272 O  OG1 . THR   N  21  ? 1.3494 0.4055 1.2301 -0.1039 -0.3989 -0.0806 21  THR   N OG1 
23273 C  CG2 . THR   N  21  ? 1.4014 0.6080 1.2008 -0.0490 -0.3929 -0.0303 21  THR   N CG2 
23274 N  N   . THR   N  22  ? 1.4756 0.6087 1.1097 0.0082  -0.3344 -0.1045 22  THR   N N   
23275 C  CA  . THR   N  22  ? 1.4972 0.6411 1.0887 0.0000  -0.2908 -0.0953 22  THR   N CA  
23276 C  C   . THR   N  22  ? 1.5016 0.6678 1.0860 0.0080  -0.3059 -0.1376 22  THR   N C   
23277 O  O   . THR   N  22  ? 1.5282 0.6007 1.0787 0.0172  -0.3286 -0.1458 22  THR   N O   
23278 C  CB  . THR   N  22  ? 1.5446 0.6029 1.0330 0.0088  -0.2844 -0.0801 22  THR   N CB  
23279 O  OG1 . THR   N  22  ? 1.5775 0.5511 1.0263 -0.0103 -0.2411 -0.0191 22  THR   N OG1 
23280 C  CG2 . THR   N  22  ? 1.5438 0.6455 1.0306 0.0151  -0.2779 -0.0768 22  THR   N CG2 
23281 N  N   . GLY   N  23  ? 1.4951 0.7400 1.0821 -0.0012 -0.2940 -0.1539 23  GLY   N N   
23282 C  CA  . GLY   N  23  ? 1.5254 0.7103 1.1169 0.0357  -0.2471 -0.0716 23  GLY   N CA  
23283 C  C   . GLY   N  23  ? 1.5212 0.7099 1.1270 0.0330  -0.2213 -0.0522 23  GLY   N C   
23284 O  O   . GLY   N  23  ? 1.5236 0.6689 1.1526 0.0225  -0.2181 -0.1279 23  GLY   N O   
23285 N  N   . ALA   N  24  ? 1.5473 0.7121 1.1734 0.0483  -0.2439 0.0127  24  ALA   N N   
23286 C  CA  . ALA   N  24  ? 1.6190 0.6406 1.1723 0.0199  -0.2452 0.0175  24  ALA   N CA  
23287 C  C   . ALA   N  24  ? 1.6220 0.6108 1.1305 0.0391  -0.2688 0.0313  24  ALA   N C   
23288 O  O   . ALA   N  24  ? 1.5760 0.4323 1.1644 0.0137  -0.2378 0.0286  24  ALA   N O   
23289 C  CB  . ALA   N  24  ? 1.6630 0.6250 1.1837 0.0214  -0.2377 0.0426  24  ALA   N CB  
23290 N  N   . TYR   N  25  ? 1.5821 0.5802 1.1213 0.0348  -0.2687 -0.0219 25  TYR   N N   
23291 C  CA  . TYR   N  25  ? 1.5361 0.5877 1.1475 0.0986  -0.3030 -0.0495 25  TYR   N CA  
23292 C  C   . TYR   N  25  ? 1.5212 0.5837 1.1263 0.1195  -0.3497 -0.0467 25  TYR   N C   
23293 O  O   . TYR   N  25  ? 1.5190 0.5820 1.0921 0.1257  -0.3521 -0.0974 25  TYR   N O   
23294 C  CB  . TYR   N  25  ? 1.5481 0.5502 1.1728 0.1037  -0.2844 -0.0528 25  TYR   N CB  
23295 C  CG  . TYR   N  25  ? 1.5657 0.5228 1.2200 0.1051  -0.2980 -0.0361 25  TYR   N CG  
23296 C  CD1 . TYR   N  25  ? 1.6096 0.5586 1.2318 0.1069  -0.3254 -0.0094 25  TYR   N CD1 
23297 C  CD2 . TYR   N  25  ? 1.5761 0.5040 1.2202 0.1326  -0.3111 -0.0726 25  TYR   N CD2 
23298 C  CE1 . TYR   N  25  ? 1.6422 0.4878 1.2021 0.1024  -0.3332 -0.0070 25  TYR   N CE1 
23299 C  CE2 . TYR   N  25  ? 1.5974 0.5024 1.2312 0.1219  -0.3173 -0.0853 25  TYR   N CE2 
23300 C  CZ  . TYR   N  25  ? 1.6353 0.4622 1.2182 0.1248  -0.3146 -0.0641 25  TYR   N CZ  
23301 O  OH  . TYR   N  25  ? 1.6281 0.4461 1.1885 0.1382  -0.3093 -0.0554 25  TYR   N OH  
23302 N  N   . ILE   N  26  ? 1.4914 0.5694 1.1595 0.1613  -0.3802 0.0052  26  ILE   N N   
23303 C  CA  . ILE   N  26  ? 1.4609 0.5864 1.1592 0.1575  -0.4035 -0.0015 26  ILE   N CA  
23304 C  C   . ILE   N  26  ? 1.4196 0.6413 1.1857 0.1411  -0.4271 0.0376  26  ILE   N C   
23305 O  O   . ILE   N  26  ? 1.4206 0.6912 1.2133 0.1552  -0.4472 0.1017  26  ILE   N O   
23306 C  CB  . ILE   N  26  ? 1.4619 0.5965 1.1759 0.1752  -0.4209 0.0035  26  ILE   N CB  
23307 C  CG1 . ILE   N  26  ? 1.4636 0.6016 1.1894 0.1620  -0.4088 -0.0302 26  ILE   N CG1 
23308 C  CG2 . ILE   N  26  ? 1.4519 0.6040 1.1720 0.1670  -0.4485 -0.0025 26  ILE   N CG2 
23309 C  CD1 . ILE   N  26  ? 1.4681 0.6128 1.2051 0.1670  -0.4172 -0.0135 26  ILE   N CD1 
23310 N  N   . ALA   N  27  ? 1.4672 0.5898 1.1830 0.1288  -0.4310 0.0161  27  ALA   N N   
23311 C  CA  . ALA   N  27  ? 1.4812 0.5274 1.1941 0.1422  -0.4395 -0.0361 27  ALA   N CA  
23312 C  C   . ALA   N  27  ? 1.4811 0.5051 1.2011 0.1292  -0.4452 -0.0263 27  ALA   N C   
23313 O  O   . ALA   N  27  ? 1.4753 0.5087 1.1895 0.1376  -0.4565 0.0395  27  ALA   N O   
23314 C  CB  . ALA   N  27  ? 1.4793 0.5418 1.1731 0.1385  -0.4446 -0.0392 27  ALA   N CB  
23315 N  N   . ASN   N  28  ? 1.5057 0.5292 1.2292 0.1397  -0.4204 -0.0370 28  ASN   N N   
23316 C  CA  . ASN   N  28  ? 1.5420 0.5583 1.2353 0.1491  -0.3704 -0.0788 28  ASN   N CA  
23317 C  C   . ASN   N  28  ? 1.5411 0.4791 1.2334 0.1175  -0.3614 -0.1158 28  ASN   N C   
23318 O  O   . ASN   N  28  ? 1.5695 0.2058 1.1275 0.0873  -0.3883 -0.1505 28  ASN   N O   
23319 C  CB  . ASN   N  28  ? 1.5428 0.5890 1.3071 0.1684  -0.3558 -0.1541 28  ASN   N CB  
23320 C  CG  . ASN   N  28  ? 1.5779 0.5769 1.4165 0.1639  -0.3524 -0.2227 28  ASN   N CG  
23321 O  OD1 . ASN   N  28  ? 1.5844 0.5989 1.4873 0.2189  -0.3348 -0.2562 28  ASN   N OD1 
23322 N  ND2 . ASN   N  28  ? 1.5846 0.6866 1.4736 0.2321  -0.3121 -0.2304 28  ASN   N ND2 
23323 N  N   . ARG   N  29  ? 1.6102 0.4602 1.1673 0.1221  -0.3447 -0.0917 29  ARG   N N   
23324 C  CA  . ARG   N  29  ? 1.5885 0.4894 1.1431 0.0879  -0.3858 -0.0910 29  ARG   N CA  
23325 C  C   . ARG   N  29  ? 1.5793 0.4854 1.1025 0.0849  -0.4226 -0.0669 29  ARG   N C   
23326 O  O   . ARG   N  29  ? 1.5774 0.4405 1.0883 0.1360  -0.4920 -0.0366 29  ARG   N O   
23327 C  CB  . ARG   N  29  ? 1.5150 0.5585 1.1669 0.0832  -0.4036 -0.1024 29  ARG   N CB  
23328 C  CG  . ARG   N  29  ? 1.5339 0.5906 1.2017 0.0423  -0.4050 -0.1141 29  ARG   N CG  
23329 C  CD  . ARG   N  29  ? 1.5505 0.5482 1.2390 0.0146  -0.4060 -0.0759 29  ARG   N CD  
23330 N  NE  . ARG   N  29  ? 1.5593 0.5246 1.2573 0.0158  -0.4285 -0.0461 29  ARG   N NE  
23331 C  CZ  . ARG   N  29  ? 1.5771 0.5339 1.2820 0.0019  -0.4493 0.0191  29  ARG   N CZ  
23332 N  NH1 . ARG   N  29  ? 1.5837 0.4360 1.3135 -0.0327 -0.4551 0.0291  29  ARG   N NH1 
23333 N  NH2 . ARG   N  29  ? 1.5683 0.6598 1.3619 -0.0020 -0.4502 0.0461  29  ARG   N NH2 
23334 N  N   . VAL   N  30  ? 1.5689 0.4963 1.1661 -0.0029 -0.4112 -0.1233 30  VAL   N N   
23335 C  CA  . VAL   N  30  ? 1.5895 0.4703 1.1984 -0.0262 -0.3799 -0.1335 30  VAL   N CA  
23336 C  C   . VAL   N  30  ? 1.5696 0.4639 1.2215 -0.0477 -0.3793 -0.1050 30  VAL   N C   
23337 O  O   . VAL   N  30  ? 1.5943 0.5256 1.3210 -0.0770 -0.3584 -0.1816 30  VAL   N O   
23338 C  CB  . VAL   N  30  ? 1.5864 0.4866 1.1992 0.0115  -0.3938 -0.1670 30  VAL   N CB  
23339 C  CG1 . VAL   N  30  ? 1.5971 0.4638 1.1934 0.0131  -0.3765 -0.1719 30  VAL   N CG1 
23340 C  CG2 . VAL   N  30  ? 1.5816 0.4957 1.2303 0.0302  -0.3552 -0.1819 30  VAL   N CG2 
23341 N  N   . THR   N  31  ? 1.6332 0.2821 1.1627 -0.0690 -0.3958 -0.0964 31  THR   N N   
23342 C  CA  . THR   N  31  ? 1.7266 0.2423 1.1409 -0.0580 -0.3967 -0.0710 31  THR   N CA  
23343 C  C   . THR   N  31  ? 1.7367 0.3541 1.1091 -0.0314 -0.4236 -0.0792 31  THR   N C   
23344 O  O   . THR   N  31  ? 1.7956 0.1984 1.1275 -0.0419 -0.5316 -0.1093 31  THR   N O   
23345 C  CB  . THR   N  31  ? 1.7555 0.1671 1.1190 -0.0477 -0.3944 -0.0550 31  THR   N CB  
23346 O  OG1 . THR   N  31  ? 1.8243 0.2257 1.1094 -0.0037 -0.3226 -0.0020 31  THR   N OG1 
23347 C  CG2 . THR   N  31  ? 1.6983 0.2151 1.1221 -0.0176 -0.4088 -0.0704 31  THR   N CG2 
23348 N  N   . ASP   N  32  ? 1.7333 0.3585 1.1347 -0.0161 -0.4004 -0.1452 32  ASP   N N   
23349 C  CA  . ASP   N  32  ? 1.7572 0.4424 1.1466 -0.0218 -0.3480 -0.1323 32  ASP   N CA  
23350 C  C   . ASP   N  32  ? 1.7591 0.4342 1.0918 -0.0433 -0.3550 -0.1348 32  ASP   N C   
23351 O  O   . ASP   N  32  ? 1.7170 0.5792 0.9338 -0.0750 -0.3866 -0.0919 32  ASP   N O   
23352 C  CB  . ASP   N  32  ? 1.7893 0.4528 1.2435 -0.0640 -0.3021 -0.1345 32  ASP   N CB  
23353 C  CG  . ASP   N  32  ? 1.8591 0.4789 1.2927 -0.0357 -0.2638 -0.1459 32  ASP   N CG  
23354 O  OD1 . ASP   N  32  ? 1.9098 0.3219 1.2643 0.0710  -0.2936 0.0140  32  ASP   N OD1 
23355 O  OD2 . ASP   N  32  ? 1.9287 0.5833 1.4692 -0.1031 -0.2325 -0.3453 32  ASP   N OD2 
23356 N  N   . LYS   N  33  ? 1.6890 0.5924 1.1378 -0.0625 -0.3248 -0.1590 33  LYS   N N   
23357 C  CA  . LYS   N  33  ? 1.6667 0.5756 1.1815 0.0088  -0.2934 -0.1146 33  LYS   N CA  
23358 C  C   . LYS   N  33  ? 1.7078 0.5070 1.1949 0.0252  -0.3097 -0.1223 33  LYS   N C   
23359 O  O   . LYS   N  33  ? 1.6895 0.4987 1.3210 0.0922  -0.2640 -0.0745 33  LYS   N O   
23360 C  CB  . LYS   N  33  ? 1.6743 0.5792 1.1811 -0.0166 -0.2475 -0.0829 33  LYS   N CB  
23361 C  CG  . LYS   N  33  ? 1.6668 0.5613 1.1519 0.0134  -0.2635 -0.0481 33  LYS   N CG  
23362 C  CD  . LYS   N  33  ? 1.6390 0.5465 1.1166 0.0490  -0.2769 -0.0305 33  LYS   N CD  
23363 C  CE  . LYS   N  33  ? 1.6205 0.5941 1.1298 0.0894  -0.2754 -0.0204 33  LYS   N CE  
23364 N  NZ  . LYS   N  33  ? 1.6327 0.5915 1.1223 0.0908  -0.2720 -0.0195 33  LYS   N NZ  
23365 N  N   . LEU   N  34  ? 1.6597 0.5302 1.2245 -0.0024 -0.3436 -0.1081 34  LEU   N N   
23366 C  CA  . LEU   N  34  ? 1.6327 0.5790 1.2427 0.0007  -0.3364 -0.1232 34  LEU   N CA  
23367 C  C   . LEU   N  34  ? 1.5665 0.5536 1.2778 0.0324  -0.3661 -0.1298 34  LEU   N C   
23368 O  O   . LEU   N  34  ? 1.5712 0.5100 1.3978 0.0323  -0.3970 -0.2090 34  LEU   N O   
23369 C  CB  . LEU   N  34  ? 1.6611 0.5381 1.2360 -0.0225 -0.3208 -0.1146 34  LEU   N CB  
23370 C  CG  . LEU   N  34  ? 1.6466 0.5337 1.2396 -0.0070 -0.3154 -0.1093 34  LEU   N CG  
23371 C  CD1 . LEU   N  34  ? 1.6545 0.5296 1.2291 -0.0200 -0.3257 -0.1419 34  LEU   N CD1 
23372 C  CD2 . LEU   N  34  ? 1.6323 0.5552 1.2551 0.0174  -0.2788 -0.0815 34  LEU   N CD2 
23373 N  N   . THR   N  35  ? 1.5692 0.5703 1.2260 0.0217  -0.3488 -0.0865 35  THR   N N   
23374 C  CA  . THR   N  35  ? 1.5693 0.6291 1.1352 -0.0226 -0.3318 -0.0535 35  THR   N CA  
23375 C  C   . THR   N  35  ? 1.5800 0.6068 1.1547 -0.0024 -0.3490 -0.0462 35  THR   N C   
23376 O  O   . THR   N  35  ? 1.5369 0.5559 1.1268 0.0745  -0.3725 -0.0289 35  THR   N O   
23377 C  CB  . THR   N  35  ? 1.5609 0.6580 1.1206 -0.0537 -0.2821 -0.0229 35  THR   N CB  
23378 O  OG1 . THR   N  35  ? 1.5648 0.6882 1.0701 -0.0825 -0.2593 -0.0030 35  THR   N OG1 
23379 C  CG2 . THR   N  35  ? 1.5497 0.6005 1.1053 -0.0697 -0.2878 -0.0087 35  THR   N CG2 
23380 N  N   . ARG   N  36  ? 1.6127 0.5653 1.1964 0.0232  -0.3012 -0.0600 36  ARG   N N   
23381 C  CA  . ARG   N  36  ? 1.7322 0.5558 1.2781 0.0435  -0.2107 -0.0520 36  ARG   N CA  
23382 C  C   . ARG   N  36  ? 1.6725 0.4753 1.2321 0.0364  -0.2090 -0.1225 36  ARG   N C   
23383 O  O   . ARG   N  36  ? 1.7117 0.5452 1.2118 0.0451  -0.1815 -0.1566 36  ARG   N O   
23384 C  CB  . ARG   N  36  ? 1.7686 0.5512 1.3638 0.0186  -0.1927 -0.0805 36  ARG   N CB  
23385 C  CG  . ARG   N  36  ? 1.8870 0.6288 1.4448 0.0525  -0.0948 -0.1038 36  ARG   N CG  
23386 C  CD  . ARG   N  36  ? 1.9345 0.6936 1.6012 -0.0010 -0.0722 -0.1275 36  ARG   N CD  
23387 N  NE  . ARG   N  36  ? 2.0353 0.6888 1.6544 0.0121  -0.0128 -0.1066 36  ARG   N NE  
23388 C  CZ  . ARG   N  36  ? 2.0529 0.7766 1.6695 0.0984  0.0253  -0.1452 36  ARG   N CZ  
23389 N  NH1 . ARG   N  36  ? 2.0609 0.9313 1.6727 0.0532  0.0285  -0.1817 36  ARG   N NH1 
23390 N  NH2 . ARG   N  36  ? 2.0682 0.8426 1.6680 0.1310  0.0473  -0.1052 36  ARG   N NH2 
23391 N  N   . VAL   N  37  ? 1.6712 0.4420 1.2060 0.0170  -0.1801 -0.1570 37  VAL   N N   
23392 C  CA  . VAL   N  37  ? 1.6583 0.4633 1.2288 0.0246  -0.1750 -0.1440 37  VAL   N CA  
23393 C  C   . VAL   N  37  ? 1.7599 0.4547 1.2472 0.0118  -0.1688 -0.1509 37  VAL   N C   
23394 O  O   . VAL   N  37  ? 1.8295 0.4175 1.3391 0.0482  -0.1626 -0.1836 37  VAL   N O   
23395 C  CB  . VAL   N  37  ? 1.6642 0.4211 1.1991 0.0150  -0.1613 -0.1489 37  VAL   N CB  
23396 C  CG1 . VAL   N  37  ? 1.6303 0.3783 1.1898 0.0186  -0.1821 -0.1107 37  VAL   N CG1 
23397 C  CG2 . VAL   N  37  ? 1.6962 0.4538 1.1890 -0.0016 -0.1516 -0.1451 37  VAL   N CG2 
23398 N  N   . HIS   N  38  ? 1.8088 0.4187 1.2506 0.0087  -0.1820 -0.1215 38  HIS   N N   
23399 C  CA  . HIS   N  38  ? 1.8388 0.4665 1.2792 -0.0006 -0.1872 -0.1591 38  HIS   N CA  
23400 C  C   . HIS   N  38  ? 1.8634 0.4870 1.3050 -0.0621 -0.2192 -0.1228 38  HIS   N C   
23401 O  O   . HIS   N  38  ? 1.8024 0.5009 1.3157 -0.0273 -0.2002 -0.1924 38  HIS   N O   
23402 C  CB  . HIS   N  38  ? 1.8470 0.5510 1.3230 0.0147  -0.1624 -0.1984 38  HIS   N CB  
23403 C  CG  . HIS   N  38  ? 1.8491 0.6333 1.3182 0.0066  -0.1424 -0.3212 38  HIS   N CG  
23404 N  ND1 . HIS   N  38  ? 1.8390 0.5586 1.3512 -0.0077 -0.1473 -0.3600 38  HIS   N ND1 
23405 C  CD2 . HIS   N  38  ? 1.8857 0.6595 1.3361 -0.0117 -0.2030 -0.4517 38  HIS   N CD2 
23406 C  CE1 . HIS   N  38  ? 1.8665 0.6294 1.2915 0.0062  -0.1629 -0.4006 38  HIS   N CE1 
23407 N  NE2 . HIS   N  38  ? 1.8806 0.6707 1.2978 -0.0278 -0.1689 -0.4060 38  HIS   N NE2 
23408 N  N   . ASP   N  39  ? 1.9278 0.5122 1.2468 -0.1207 -0.2620 -0.0853 39  ASP   N N   
23409 C  CA  . ASP   N  39  ? 1.9701 0.5095 1.2265 -0.1545 -0.2629 -0.0714 39  ASP   N CA  
23410 C  C   . ASP   N  39  ? 1.8816 0.4898 1.1868 -0.1277 -0.2938 -0.0777 39  ASP   N C   
23411 O  O   . ASP   N  39  ? 1.9714 0.3669 1.1321 -0.1673 -0.3214 -0.0495 39  ASP   N O   
23412 C  CB  . ASP   N  39  ? 2.0745 0.4934 1.2642 -0.1093 -0.2449 -0.0724 39  ASP   N CB  
23413 C  CG  . ASP   N  39  ? 2.1650 0.4173 1.3965 -0.1484 -0.2188 -0.1686 39  ASP   N CG  
23414 O  OD1 . ASP   N  39  ? 2.2737 0.7024 1.3632 -0.1978 -0.2358 -0.2779 39  ASP   N OD1 
23415 O  OD2 . ASP   N  39  ? 2.2528 0.4651 1.3944 -0.1302 -0.1384 -0.2255 39  ASP   N OD2 
23416 N  N   . LYS   N  40  ? 1.8910 0.5138 1.1718 -0.1794 -0.2340 -0.0556 40  LYS   N N   
23417 C  CA  . LYS   N  40  ? 1.8696 0.5107 1.1462 -0.1230 -0.2213 -0.0143 40  LYS   N CA  
23418 C  C   . LYS   N  40  ? 1.8316 0.4296 1.1229 -0.1003 -0.2001 0.0143  40  LYS   N C   
23419 O  O   . LYS   N  40  ? 1.8650 0.4479 1.1373 -0.0775 -0.1457 0.0391  40  LYS   N O   
23420 C  CB  . LYS   N  40  ? 1.8831 0.5154 1.1522 -0.1751 -0.1982 -0.0300 40  LYS   N CB  
23421 C  CG  . LYS   N  40  ? 1.8882 0.5658 1.1552 -0.1835 -0.2048 -0.0495 40  LYS   N CG  
23422 C  CD  . LYS   N  40  ? 1.9235 0.5946 1.1802 -0.2441 -0.1884 -0.0843 40  LYS   N CD  
23423 C  CE  . LYS   N  40  ? 1.9375 0.6692 1.1876 -0.2629 -0.2147 -0.1182 40  LYS   N CE  
23424 N  NZ  . LYS   N  40  ? 2.0124 0.7675 1.1903 -0.2594 -0.1698 -0.1703 40  LYS   N NZ  
23425 N  N   . ILE   N  41  ? 1.7919 0.4405 1.1169 -0.0518 -0.1974 -0.0156 41  ILE   N N   
23426 C  CA  . ILE   N  41  ? 1.7468 0.4101 1.1484 -0.0420 -0.2012 -0.0154 41  ILE   N CA  
23427 C  C   . ILE   N  41  ? 1.7024 0.4079 1.1273 -0.0441 -0.2152 0.0070  41  ILE   N C   
23428 O  O   . ILE   N  41  ? 1.7296 0.1851 1.1563 0.0113  -0.2362 0.0231  41  ILE   N O   
23429 C  CB  . ILE   N  41  ? 1.6840 0.5293 1.1183 -0.0423 -0.2592 -0.0878 41  ILE   N CB  
23430 C  CG1 . ILE   N  41  ? 1.7163 0.5983 1.1548 -0.0292 -0.2478 -0.1333 41  ILE   N CG1 
23431 C  CG2 . ILE   N  41  ? 1.6700 0.4801 1.1250 -0.0575 -0.2427 -0.0769 41  ILE   N CG2 
23432 C  CD1 . ILE   N  41  ? 1.7187 0.5716 1.1343 -0.0218 -0.2324 -0.1506 41  ILE   N CD1 
23433 N  N   . TRP   N  42  ? 1.6497 0.4081 1.0966 -0.0655 -0.2116 -0.0223 42  TRP   N N   
23434 C  CA  . TRP   N  42  ? 1.5948 0.4557 1.0847 -0.0326 -0.2181 0.0235  42  TRP   N CA  
23435 C  C   . TRP   N  42  ? 1.5901 0.4540 1.0486 -0.0110 -0.2283 0.0364  42  TRP   N C   
23436 O  O   . TRP   N  42  ? 1.5867 0.5343 1.0110 0.0407  -0.2165 0.0627  42  TRP   N O   
23437 C  CB  . TRP   N  42  ? 1.5575 0.4104 1.1067 -0.0774 -0.2349 0.0237  42  TRP   N CB  
23438 C  CG  . TRP   N  42  ? 1.5297 0.4323 1.1330 -0.0762 -0.2334 0.0174  42  TRP   N CG  
23439 C  CD1 . TRP   N  42  ? 1.5206 0.4727 1.1340 -0.1093 -0.2440 -0.0144 42  TRP   N CD1 
23440 C  CD2 . TRP   N  42  ? 1.5144 0.4172 1.1291 -0.0981 -0.2633 0.0149  42  TRP   N CD2 
23441 N  NE1 . TRP   N  42  ? 1.5214 0.5043 1.1323 -0.1071 -0.2602 -0.0210 42  TRP   N NE1 
23442 C  CE2 . TRP   N  42  ? 1.5130 0.4647 1.1388 -0.1017 -0.2755 -0.0114 42  TRP   N CE2 
23443 C  CE3 . TRP   N  42  ? 1.4875 0.4377 1.1434 -0.0835 -0.2627 0.0375  42  TRP   N CE3 
23444 C  CZ2 . TRP   N  42  ? 1.5176 0.4971 1.1629 -0.1041 -0.2849 -0.0403 42  TRP   N CZ2 
23445 C  CZ3 . TRP   N  42  ? 1.5007 0.4524 1.1769 -0.1213 -0.2876 0.0105  42  TRP   N CZ3 
23446 C  CH2 . TRP   N  42  ? 1.5329 0.4793 1.1828 -0.1084 -0.2774 -0.0344 42  TRP   N CH2 
23447 N  N   . CYS   N  43  ? 1.6178 0.4659 1.0731 0.0159  -0.2186 0.0310  43  CYS   N N   
23448 C  CA  . CYS   N  43  ? 1.6488 0.4911 1.1133 -0.0290 -0.2280 0.0410  43  CYS   N CA  
23449 C  C   . CYS   N  43  ? 1.6728 0.4469 1.1643 -0.0385 -0.2571 0.0543  43  CYS   N C   
23450 O  O   . CYS   N  43  ? 1.6804 0.4133 1.2087 -0.0346 -0.2833 0.0187  43  CYS   N O   
23451 C  CB  . CYS   N  43  ? 1.6789 0.4771 1.1195 -0.0317 -0.1842 0.0839  43  CYS   N CB  
23452 S  SG  . CYS   N  43  ? 1.7148 0.4960 1.1258 -0.0459 -0.1779 0.1589  43  CYS   N SG  
23453 N  N   . CYS   N  44  ? 1.7051 0.4556 1.1742 -0.0567 -0.2575 0.0592  44  CYS   N N   
23454 C  CA  . CYS   N  44  ? 1.7209 0.5103 1.1056 -0.0469 -0.2604 -0.0010 44  CYS   N CA  
23455 C  C   . CYS   N  44  ? 1.6213 0.4467 1.0949 -0.0797 -0.2421 -0.0095 44  CYS   N C   
23456 O  O   . CYS   N  44  ? 1.6627 0.2479 0.9412 -0.0857 -0.2856 0.0186  44  CYS   N O   
23457 C  CB  . CYS   N  44  ? 1.7837 0.4550 1.1640 -0.0396 -0.2817 0.0031  44  CYS   N CB  
23458 S  SG  . CYS   N  44  ? 1.8630 0.5779 1.1762 0.0073  -0.3299 0.0054  44  CYS   N SG  
23459 N  N   . ARG   N  45  ? 1.5888 0.4338 1.0945 -0.1020 -0.2562 -0.0532 45  ARG   N N   
23460 C  CA  . ARG   N  45  ? 1.5247 0.4674 1.1029 -0.1012 -0.2385 -0.0236 45  ARG   N CA  
23461 C  C   . ARG   N  45  ? 1.4874 0.4455 1.1860 -0.0429 -0.2778 0.0152  45  ARG   N C   
23462 O  O   . ARG   N  45  ? 1.5709 0.3578 1.2157 -0.0448 -0.3134 0.0774  45  ARG   N O   
23463 C  CB  . ARG   N  45  ? 1.4993 0.4062 1.1523 -0.1129 -0.2444 -0.0776 45  ARG   N CB  
23464 C  CG  . ARG   N  45  ? 1.4621 0.3835 1.1551 -0.1839 -0.2479 -0.0555 45  ARG   N CG  
23465 C  CD  . ARG   N  45  ? 1.4664 0.3317 1.1965 -0.2041 -0.2681 -0.0529 45  ARG   N CD  
23466 N  NE  . ARG   N  45  ? 1.4724 0.2894 1.2042 -0.2237 -0.2877 -0.0401 45  ARG   N NE  
23467 C  CZ  . ARG   N  45  ? 1.4222 0.3172 1.2072 -0.2951 -0.2954 -0.1125 45  ARG   N CZ  
23468 N  NH1 . ARG   N  45  ? 1.4784 0.3542 1.2021 -0.3485 -0.2927 -0.0990 45  ARG   N NH1 
23469 N  NH2 . ARG   N  45  ? 1.3820 0.4248 1.2688 -0.3703 -0.3090 -0.1178 45  ARG   N NH2 
23470 N  N   . SER   N  46  ? 1.4935 0.5205 1.1488 -0.0160 -0.2735 -0.0132 46  SER   N N   
23471 C  CA  . SER   N  46  ? 1.4878 0.5368 1.0626 0.0920  -0.2587 -0.0259 46  SER   N CA  
23472 C  C   . SER   N  46  ? 1.4744 0.4948 1.0621 0.0780  -0.2446 0.0108  46  SER   N C   
23473 O  O   . SER   N  46  ? 1.5091 0.4729 0.9597 0.0219  -0.2310 0.1236  46  SER   N O   
23474 C  CB  . SER   N  46  ? 1.4686 0.5732 1.0779 0.1004  -0.2548 -0.0241 46  SER   N CB  
23475 O  OG  . SER   N  46  ? 1.5263 0.6800 1.0877 0.1360  -0.3445 -0.0403 46  SER   N OG  
23476 N  N   . GLY   N  47  ? 1.4709 0.5862 0.9832 0.0483  -0.2672 -0.0155 47  GLY   N N   
23477 C  CA  . GLY   N  47  ? 1.4901 0.5702 0.9889 0.0183  -0.3063 0.0236  47  GLY   N CA  
23478 C  C   . GLY   N  47  ? 1.5054 0.5394 0.9962 -0.0357 -0.3250 -0.0194 47  GLY   N C   
23479 O  O   . GLY   N  47  ? 1.5489 0.5981 0.9363 -0.1156 -0.3672 0.0579  47  GLY   N O   
23480 N  N   . SER   N  48  ? 1.5398 0.5136 0.9793 -0.0537 -0.3195 -0.0513 48  SER   N N   
23481 C  CA  . SER   N  48  ? 1.5609 0.5929 0.9899 -0.0578 -0.2862 -0.0537 48  SER   N CA  
23482 C  C   . SER   N  48  ? 1.4757 0.6545 1.0488 -0.0635 -0.2944 -0.0741 48  SER   N C   
23483 O  O   . SER   N  48  ? 1.5153 0.6095 1.0804 -0.0400 -0.2705 0.0114  48  SER   N O   
23484 C  CB  . SER   N  48  ? 1.6202 0.6015 0.9768 -0.0552 -0.2629 -0.0379 48  SER   N CB  
23485 O  OG  . SER   N  48  ? 1.6765 0.5705 1.0323 -0.1084 -0.2745 -0.0813 48  SER   N OG  
23486 N  N   . ALA   N  49  ? 1.4539 0.7297 1.1169 -0.0797 -0.2712 -0.1042 49  ALA   N N   
23487 C  CA  . ALA   N  49  ? 1.5282 0.6391 1.0390 -0.0328 -0.2413 -0.1471 49  ALA   N CA  
23488 C  C   . ALA   N  49  ? 1.4812 0.6051 0.9890 -0.0604 -0.2526 -0.1862 49  ALA   N C   
23489 O  O   . ALA   N  49  ? 1.4617 0.6299 1.0263 -0.0574 -0.2817 -0.2132 49  ALA   N O   
23490 C  CB  . ALA   N  49  ? 1.5092 0.6814 1.0035 -0.0632 -0.2917 -0.1696 49  ALA   N CB  
23491 N  N   . ALA   N  50  ? 1.4686 0.5383 1.0020 -0.0255 -0.2073 -0.1446 50  ALA   N N   
23492 C  CA  . ALA   N  50  ? 1.4254 0.5140 1.0323 -0.0369 -0.2029 -0.1515 50  ALA   N CA  
23493 C  C   . ALA   N  50  ? 1.3556 0.5902 1.0436 -0.0550 -0.2300 -0.0702 50  ALA   N C   
23494 O  O   . ALA   N  50  ? 1.3468 0.6036 1.0560 0.0028  -0.3072 -0.0845 50  ALA   N O   
23495 C  CB  . ALA   N  50  ? 1.4459 0.5576 1.0231 -0.0531 -0.1999 -0.1227 50  ALA   N CB  
23496 N  N   . ASP   N  51  ? 1.3653 0.5308 1.0474 -0.0514 -0.2148 -0.0592 51  ASP   N N   
23497 C  CA  . ASP   N  51  ? 1.3745 0.4930 1.0610 -0.0471 -0.2044 -0.0209 51  ASP   N CA  
23498 C  C   . ASP   N  51  ? 1.3425 0.4530 1.0583 -0.0381 -0.2213 -0.0273 51  ASP   N C   
23499 O  O   . ASP   N  51  ? 1.3035 0.4601 0.9609 -0.0393 -0.2123 -0.0264 51  ASP   N O   
23500 C  CB  . ASP   N  51  ? 1.3682 0.5143 1.1431 -0.0591 -0.1975 -0.0270 51  ASP   N CB  
23501 C  CG  . ASP   N  51  ? 1.3749 0.5033 1.1455 -0.0667 -0.1543 0.0021  51  ASP   N CG  
23502 O  OD1 . ASP   N  51  ? 1.3512 0.4323 1.2384 -0.0414 -0.1141 -0.0016 51  ASP   N OD1 
23503 O  OD2 . ASP   N  51  ? 1.4081 0.5583 1.3235 -0.0906 -0.2066 -0.0535 51  ASP   N OD2 
23504 N  N   . THR   N  52  ? 1.3550 0.5078 1.0366 -0.0246 -0.2571 -0.0359 52  THR   N N   
23505 C  CA  . THR   N  52  ? 1.3715 0.4599 1.0443 -0.0263 -0.2410 -0.0211 52  THR   N CA  
23506 C  C   . THR   N  52  ? 1.4102 0.4536 1.0642 -0.0312 -0.2566 -0.0290 52  THR   N C   
23507 O  O   . THR   N  52  ? 1.3980 0.4703 0.9450 -0.0707 -0.2922 -0.0282 52  THR   N O   
23508 C  CB  . THR   N  52  ? 1.3888 0.4502 1.0992 -0.0531 -0.2202 0.0068  52  THR   N CB  
23509 O  OG1 . THR   N  52  ? 1.3625 0.4429 1.1179 -0.0656 -0.2310 0.1112  52  THR   N OG1 
23510 C  CG2 . THR   N  52  ? 1.3862 0.4696 1.0930 -0.0601 -0.2256 -0.0015 52  THR   N CG2 
23511 N  N   . GLN   N  53  ? 1.4090 0.3947 1.0587 -0.0091 -0.2591 -0.0671 53  GLN   N N   
23512 C  CA  . GLN   N  53  ? 1.4291 0.4449 1.0653 -0.0218 -0.3001 -0.1019 53  GLN   N CA  
23513 C  C   . GLN   N  53  ? 1.4654 0.4244 1.0731 -0.0267 -0.3081 -0.1215 53  GLN   N C   
23514 O  O   . GLN   N  53  ? 1.5310 0.3758 1.1861 -0.0617 -0.3124 -0.1316 53  GLN   N O   
23515 C  CB  . GLN   N  53  ? 1.4350 0.4431 1.0803 0.0000  -0.3111 -0.1356 53  GLN   N CB  
23516 C  CG  . GLN   N  53  ? 1.4467 0.4048 1.1101 -0.0148 -0.3407 -0.1552 53  GLN   N CG  
23517 C  CD  . GLN   N  53  ? 1.4352 0.4040 1.1807 -0.0350 -0.3449 -0.1411 53  GLN   N CD  
23518 O  OE1 . GLN   N  53  ? 1.3829 0.4829 1.1813 -0.0524 -0.3601 -0.1083 53  GLN   N OE1 
23519 N  NE2 . GLN   N  53  ? 1.4653 0.3999 1.2182 -0.0277 -0.3592 -0.1510 53  GLN   N NE2 
23520 N  N   . ALA   N  54  ? 1.4384 0.3926 1.0687 -0.0145 -0.3037 -0.0477 54  ALA   N N   
23521 C  CA  . ALA   N  54  ? 1.4342 0.3755 1.0053 -0.0495 -0.2842 -0.0362 54  ALA   N CA  
23522 C  C   . ALA   N  54  ? 1.4335 0.4741 0.9823 -0.0243 -0.2853 -0.0194 54  ALA   N C   
23523 O  O   . ALA   N  54  ? 1.4192 0.4948 0.9819 0.0362  -0.3012 -0.0591 54  ALA   N O   
23524 C  CB  . ALA   N  54  ? 1.4360 0.2949 1.0003 -0.0572 -0.2810 -0.0201 54  ALA   N CB  
23525 N  N   . ILE   N  55  ? 1.4262 0.4661 0.9866 -0.0110 -0.2593 -0.0381 55  ILE   N N   
23526 C  CA  . ILE   N  55  ? 1.4379 0.5249 1.0049 0.0030  -0.2441 -0.0339 55  ILE   N CA  
23527 C  C   . ILE   N  55  ? 1.4465 0.5310 1.0156 0.0069  -0.2568 -0.0408 55  ILE   N C   
23528 O  O   . ILE   N  55  ? 1.4802 0.5109 0.9915 0.0080  -0.2403 -0.0070 55  ILE   N O   
23529 C  CB  . ILE   N  55  ? 1.4133 0.5660 1.0189 -0.0114 -0.2271 -0.0600 55  ILE   N CB  
23530 C  CG1 . ILE   N  55  ? 1.4012 0.6612 0.9747 -0.0059 -0.2452 -0.0182 55  ILE   N CG1 
23531 C  CG2 . ILE   N  55  ? 1.4137 0.5768 1.0614 -0.0020 -0.2148 -0.0584 55  ILE   N CG2 
23532 C  CD1 . ILE   N  55  ? 1.3917 0.6855 0.9754 -0.0245 -0.2618 -0.0092 55  ILE   N CD1 
23533 N  N   . ALA   N  56  ? 1.4521 0.5416 1.0203 0.0243  -0.2713 -0.0566 56  ALA   N N   
23534 C  CA  . ALA   N  56  ? 1.4473 0.5235 1.0324 0.0415  -0.2879 -0.0638 56  ALA   N CA  
23535 C  C   . ALA   N  56  ? 1.4546 0.5407 1.0229 0.0276  -0.3089 -0.0407 56  ALA   N C   
23536 O  O   . ALA   N  56  ? 1.4626 0.6314 1.0502 0.0501  -0.3000 -0.0752 56  ALA   N O   
23537 C  CB  . ALA   N  56  ? 1.4575 0.4518 1.0538 0.0169  -0.2878 -0.0674 56  ALA   N CB  
23538 N  N   . ASP   N  57  ? 1.5034 0.5236 0.9849 0.0852  -0.2897 -0.0285 57  ASP   N N   
23539 C  CA  . ASP   N  57  ? 1.5819 0.5052 1.0474 0.1078  -0.2611 0.0162  57  ASP   N CA  
23540 C  C   . ASP   N  57  ? 1.5811 0.5126 1.0350 0.1064  -0.2493 0.0645  57  ASP   N C   
23541 O  O   . ASP   N  57  ? 1.6428 0.3431 1.0835 0.2277  -0.2342 0.1685  57  ASP   N O   
23542 C  CB  . ASP   N  57  ? 1.6861 0.5398 1.0576 0.0882  -0.2249 0.0001  57  ASP   N CB  
23543 C  CG  . ASP   N  57  ? 1.7258 0.4896 1.1283 0.0919  -0.2403 -0.0042 57  ASP   N CG  
23544 O  OD1 . ASP   N  57  ? 1.9019 0.3712 1.1436 0.0141  -0.2635 0.0316  57  ASP   N OD1 
23545 O  OD2 . ASP   N  57  ? 1.8036 0.4640 1.1278 0.0898  -0.1989 0.0098  57  ASP   N OD2 
23546 N  N   . ILE   N  58  ? 1.5369 0.4918 1.0295 0.0917  -0.2241 0.0617  58  ILE   N N   
23547 C  CA  . ILE   N  58  ? 1.5217 0.4828 1.0363 0.0904  -0.2068 0.0443  58  ILE   N CA  
23548 C  C   . ILE   N  58  ? 1.5314 0.5308 1.0698 0.0638  -0.1736 0.0476  58  ILE   N C   
23549 O  O   . ILE   N  58  ? 1.5976 0.5945 1.1519 0.1243  -0.1209 -0.0033 58  ILE   N O   
23550 C  CB  . ILE   N  58  ? 1.5173 0.5037 0.9706 0.1144  -0.2060 0.0951  58  ILE   N CB  
23551 C  CG1 . ILE   N  58  ? 1.5361 0.5559 0.9592 0.1044  -0.2079 0.1432  58  ILE   N CG1 
23552 C  CG2 . ILE   N  58  ? 1.5279 0.4801 0.9309 0.1139  -0.2247 0.1178  58  ILE   N CG2 
23553 C  CD1 . ILE   N  58  ? 1.5445 0.5674 0.9442 0.1086  -0.2206 0.1596  58  ILE   N CD1 
23554 N  N   . VAL   N  59  ? 1.4849 0.4967 1.0474 0.0879  -0.1762 0.0265  59  VAL   N N   
23555 C  CA  . VAL   N  59  ? 1.4866 0.4973 1.0837 0.0975  -0.1470 0.0223  59  VAL   N CA  
23556 C  C   . VAL   N  59  ? 1.4912 0.4754 1.1148 0.0872  -0.1597 0.0434  59  VAL   N C   
23557 O  O   . VAL   N  59  ? 1.4950 0.4528 1.1545 0.1133  -0.1377 0.0990  59  VAL   N O   
23558 C  CB  . VAL   N  59  ? 1.4770 0.5018 1.0879 0.0803  -0.1395 0.0097  59  VAL   N CB  
23559 C  CG1 . VAL   N  59  ? 1.4815 0.5270 1.1060 0.0904  -0.1363 -0.0471 59  VAL   N CG1 
23560 C  CG2 . VAL   N  59  ? 1.4798 0.5471 1.0642 0.0760  -0.1458 0.0204  59  VAL   N CG2 
23561 N  N   . GLN   N  60  ? 1.4944 0.4719 1.1078 0.0975  -0.1676 -0.0079 60  GLN   N N   
23562 C  CA  . GLN   N  60  ? 1.5229 0.5198 1.1156 0.0775  -0.1715 -0.0378 60  GLN   N CA  
23563 C  C   . GLN   N  60  ? 1.5611 0.5353 1.1271 0.0527  -0.1822 -0.0105 60  GLN   N C   
23564 O  O   . GLN   N  60  ? 1.5734 0.5153 1.1959 0.0804  -0.1489 -0.0324 60  GLN   N O   
23565 C  CB  . GLN   N  60  ? 1.5100 0.5583 1.1125 0.0734  -0.1737 -0.0810 60  GLN   N CB  
23566 C  CG  . GLN   N  60  ? 1.5166 0.6452 1.1360 0.0748  -0.1920 -0.0928 60  GLN   N CG  
23567 C  CD  . GLN   N  60  ? 1.5252 0.7127 1.1794 0.0923  -0.1919 -0.1072 60  GLN   N CD  
23568 O  OE1 . GLN   N  60  ? 1.5879 0.8496 1.0845 0.1021  -0.2486 -0.0971 60  GLN   N OE1 
23569 N  NE2 . GLN   N  60  ? 1.5558 0.7368 1.2201 0.0460  -0.2345 -0.1198 60  GLN   N NE2 
23570 N  N   . TYR   N  61  ? 1.5951 0.4840 1.1224 0.0083  -0.1985 -0.0175 61  TYR   N N   
23571 C  CA  . TYR   N  61  ? 1.6192 0.4367 1.1739 0.0144  -0.2065 -0.0561 61  TYR   N CA  
23572 C  C   . TYR   N  61  ? 1.6356 0.3432 1.1484 0.0102  -0.1778 0.0126  61  TYR   N C   
23573 O  O   . TYR   N  61  ? 1.7590 0.3673 1.1440 0.0534  -0.1226 -0.0077 61  TYR   N O   
23574 C  CB  . TYR   N  61  ? 1.5872 0.4000 1.1564 0.0162  -0.2765 -0.0271 61  TYR   N CB  
23575 C  CG  . TYR   N  61  ? 1.6115 0.4941 1.1836 0.0559  -0.3422 -0.0060 61  TYR   N CG  
23576 C  CD1 . TYR   N  61  ? 1.5931 0.5886 1.2515 -0.0198 -0.3465 0.0568  61  TYR   N CD1 
23577 C  CD2 . TYR   N  61  ? 1.6612 0.4900 1.1894 0.0028  -0.3794 -0.0234 61  TYR   N CD2 
23578 C  CE1 . TYR   N  61  ? 1.6261 0.6681 1.2694 -0.0022 -0.3673 0.1135  61  TYR   N CE1 
23579 C  CE2 . TYR   N  61  ? 1.6669 0.6258 1.2206 0.0244  -0.4095 0.0597  61  TYR   N CE2 
23580 C  CZ  . TYR   N  61  ? 1.6545 0.6071 1.2298 0.0461  -0.4014 0.1510  61  TYR   N CZ  
23581 O  OH  . TYR   N  61  ? 1.6531 0.6938 1.2331 0.0752  -0.3993 0.2040  61  TYR   N OH  
23582 N  N   . HIS   N  62  ? 1.6550 0.2912 1.1092 0.0055  -0.1672 -0.0109 62  HIS   N N   
23583 C  CA  . HIS   N  62  ? 1.6753 0.3489 1.1453 0.0266  -0.1440 0.0177  62  HIS   N CA  
23584 C  C   . HIS   N  62  ? 1.6772 0.3498 1.1607 -0.0504 -0.1621 -0.0289 62  HIS   N C   
23585 O  O   . HIS   N  62  ? 1.6842 0.4157 1.2436 -0.0025 -0.1378 -0.0428 62  HIS   N O   
23586 C  CB  . HIS   N  62  ? 1.6646 0.4321 1.1197 0.0155  -0.1671 0.0452  62  HIS   N CB  
23587 C  CG  . HIS   N  62  ? 1.7274 0.5213 1.1308 0.0827  -0.1361 0.1212  62  HIS   N CG  
23588 N  ND1 . HIS   N  62  ? 1.7443 0.5526 1.2048 0.1035  -0.1086 0.1639  62  HIS   N ND1 
23589 C  CD2 . HIS   N  62  ? 1.7099 0.5743 1.1333 0.1068  -0.1164 0.1261  62  HIS   N CD2 
23590 C  CE1 . HIS   N  62  ? 1.7330 0.5695 1.1952 0.1023  -0.1055 0.1400  62  HIS   N CE1 
23591 N  NE2 . HIS   N  62  ? 1.7298 0.5950 1.0958 0.0871  -0.1133 0.1343  62  HIS   N NE2 
23592 N  N   . LEU   N  63  ? 1.6721 0.4044 1.1175 -0.0455 -0.1754 -0.0383 63  LEU   N N   
23593 C  CA  . LEU   N  63  ? 1.7273 0.4531 1.1268 -0.0399 -0.1196 -0.0120 63  LEU   N CA  
23594 C  C   . LEU   N  63  ? 1.7442 0.5061 1.1345 -0.0749 -0.1287 -0.0083 63  LEU   N C   
23595 O  O   . LEU   N  63  ? 1.7676 0.5446 1.0698 -0.1225 -0.1589 -0.0113 63  LEU   N O   
23596 C  CB  . LEU   N  63  ? 1.7302 0.4159 1.1522 -0.0209 -0.1166 -0.0442 63  LEU   N CB  
23597 C  CG  . LEU   N  63  ? 1.7268 0.3834 1.1033 0.0137  -0.1315 -0.0785 63  LEU   N CG  
23598 C  CD1 . LEU   N  63  ? 1.7281 0.3548 1.1102 0.0119  -0.1270 -0.1011 63  LEU   N CD1 
23599 C  CD2 . LEU   N  63  ? 1.7177 0.3188 1.0727 0.0184  -0.1600 -0.0493 63  LEU   N CD2 
23600 N  N   . GLU   N  64  ? 1.7129 0.5649 1.1423 -0.0621 -0.1559 0.0067  64  GLU   N N   
23601 C  CA  . GLU   N  64  ? 1.7284 0.5565 1.1762 -0.0379 -0.2031 -0.0298 64  GLU   N CA  
23602 C  C   . GLU   N  64  ? 1.7637 0.5205 1.2076 -0.0558 -0.1913 -0.0353 64  GLU   N C   
23603 O  O   . GLU   N  64  ? 1.8942 0.4896 1.2183 -0.0214 -0.1059 -0.0221 64  GLU   N O   
23604 C  CB  . GLU   N  64  ? 1.7291 0.6424 1.2284 0.0254  -0.1962 0.0120  64  GLU   N CB  
23605 C  CG  . GLU   N  64  ? 1.7515 0.6088 1.3360 0.0148  -0.1572 0.0593  64  GLU   N CG  
23606 C  CD  . GLU   N  64  ? 1.7826 0.6804 1.4020 0.0465  -0.0974 0.0837  64  GLU   N CD  
23607 O  OE1 . GLU   N  64  ? 1.8959 0.5304 1.4668 0.1299  -0.1248 0.2281  64  GLU   N OE1 
23608 O  OE2 . GLU   N  64  ? 1.7666 0.7511 1.4811 0.1723  -0.1483 0.0528  64  GLU   N OE2 
23609 N  N   . LEU   N  65  ? 1.7164 0.3868 1.2002 -0.0358 -0.1793 -0.0753 65  LEU   N N   
23610 C  CA  . LEU   N  65  ? 1.6677 0.4438 1.2113 -0.0031 -0.1833 -0.0614 65  LEU   N CA  
23611 C  C   . LEU   N  65  ? 1.6332 0.4658 1.1735 -0.0182 -0.2024 0.0195  65  LEU   N C   
23612 O  O   . LEU   N  65  ? 1.6531 0.5718 1.1164 0.1027  -0.1916 -0.0205 65  LEU   N O   
23613 C  CB  . LEU   N  65  ? 1.6751 0.4743 1.2271 -0.0080 -0.1838 -0.1238 65  LEU   N CB  
23614 C  CG  . LEU   N  65  ? 1.6900 0.5036 1.2960 0.0250  -0.1639 -0.1133 65  LEU   N CG  
23615 C  CD1 . LEU   N  65  ? 1.6908 0.5372 1.3773 -0.0153 -0.1292 -0.0856 65  LEU   N CD1 
23616 C  CD2 . LEU   N  65  ? 1.6878 0.5266 1.2985 -0.0041 -0.1766 -0.1205 65  LEU   N CD2 
23617 N  N   . TYR   N  66  ? 1.6099 0.4281 1.1686 0.0093  -0.2030 0.0098  66  TYR   N N   
23618 C  CA  . TYR   N  66  ? 1.6407 0.4444 1.1761 0.0030  -0.1762 0.0130  66  TYR   N CA  
23619 C  C   . TYR   N  66  ? 1.6766 0.4859 1.2107 -0.0250 -0.1560 -0.0384 66  TYR   N C   
23620 O  O   . TYR   N  66  ? 1.6243 0.5159 1.2994 -0.0011 -0.1035 0.0223  66  TYR   N O   
23621 C  CB  . TYR   N  66  ? 1.6148 0.4730 1.1251 -0.0051 -0.1785 0.0697  66  TYR   N CB  
23622 C  CG  . TYR   N  66  ? 1.6260 0.3977 1.0969 -0.0353 -0.1792 0.1157  66  TYR   N CG  
23623 C  CD1 . TYR   N  66  ? 1.6617 0.3931 1.0964 -0.0431 -0.1920 0.1415  66  TYR   N CD1 
23624 C  CD2 . TYR   N  66  ? 1.6341 0.3835 1.0880 -0.0437 -0.1873 0.1441  66  TYR   N CD2 
23625 C  CE1 . TYR   N  66  ? 1.6757 0.4358 1.1066 -0.0658 -0.1894 0.1729  66  TYR   N CE1 
23626 C  CE2 . TYR   N  66  ? 1.6483 0.4203 1.0843 -0.0531 -0.1863 0.1737  66  TYR   N CE2 
23627 C  CZ  . TYR   N  66  ? 1.6702 0.4598 1.0824 -0.0737 -0.1789 0.1928  66  TYR   N CZ  
23628 O  OH  . TYR   N  66  ? 1.7018 0.4963 1.0651 -0.1035 -0.1597 0.2602  66  TYR   N OH  
23629 N  N   . THR   N  67  ? 1.6823 0.5160 1.2041 0.0113  -0.1632 -0.1057 67  THR   N N   
23630 C  CA  . THR   N  67  ? 1.7998 0.5774 1.1840 0.0032  -0.1291 -0.1483 67  THR   N CA  
23631 C  C   . THR   N  67  ? 1.8587 0.5540 1.1621 0.0356  -0.0974 -0.1992 67  THR   N C   
23632 O  O   . THR   N  67  ? 1.9420 0.5257 1.2213 0.0150  -0.0704 -0.2360 67  THR   N O   
23633 C  CB  . THR   N  67  ? 1.8029 0.6276 1.1456 0.0014  -0.1512 -0.1601 67  THR   N CB  
23634 O  OG1 . THR   N  67  ? 1.8464 0.6477 1.1483 -0.0635 -0.1348 -0.1311 67  THR   N OG1 
23635 C  CG2 . THR   N  67  ? 1.8280 0.7291 1.1518 -0.0132 -0.1550 -0.1799 67  THR   N CG2 
23636 N  N   . SER   N  68  ? 1.8756 0.5573 1.2154 0.0455  -0.0690 -0.1633 68  SER   N N   
23637 C  CA  . SER   N  68  ? 1.9015 0.5601 1.2745 0.0653  -0.0467 -0.1283 68  SER   N CA  
23638 C  C   . SER   N  68  ? 1.9089 0.4903 1.2292 0.0488  -0.0601 -0.1165 68  SER   N C   
23639 O  O   . SER   N  68  ? 2.0372 0.4308 1.2892 0.0964  -0.0407 -0.0966 68  SER   N O   
23640 C  CB  . SER   N  68  ? 1.9091 0.5881 1.3216 0.0827  -0.0104 -0.0877 68  SER   N CB  
23641 O  OG  . SER   N  68  ? 1.9269 0.6614 1.3920 0.1088  -0.0347 -0.1056 68  SER   N OG  
23642 N  N   . GLN   N  69  ? 1.8699 0.4830 1.2058 0.0745  -0.0696 -0.0881 69  GLN   N N   
23643 C  CA  . GLN   N  69  ? 1.8094 0.5228 1.2204 0.0482  -0.0745 -0.0875 69  GLN   N CA  
23644 C  C   . GLN   N  69  ? 1.8024 0.5495 1.2368 0.0216  -0.0853 -0.0569 69  GLN   N C   
23645 O  O   . GLN   N  69  ? 1.8452 0.4768 1.3517 -0.0046 -0.0302 -0.0298 69  GLN   N O   
23646 C  CB  . GLN   N  69  ? 1.7728 0.5402 1.2284 0.0682  -0.0672 -0.1191 69  GLN   N CB  
23647 C  CG  . GLN   N  69  ? 1.7432 0.6032 1.1996 0.0726  -0.0770 -0.1743 69  GLN   N CG  
23648 C  CD  . GLN   N  69  ? 1.7533 0.6675 1.1621 0.1051  -0.0546 -0.1760 69  GLN   N CD  
23649 O  OE1 . GLN   N  69  ? 1.7057 0.7864 1.0677 0.0960  -0.0473 -0.1951 69  GLN   N OE1 
23650 N  NE2 . GLN   N  69  ? 1.7289 0.7026 1.1331 0.1832  -0.0615 -0.1292 69  GLN   N NE2 
23651 N  N   . TYR   N  70  ? 1.7923 0.5332 1.2308 -0.0173 -0.1577 -0.1059 70  TYR   N N   
23652 C  CA  . TYR   N  70  ? 1.8222 0.6061 1.2909 -0.0257 -0.1350 -0.0673 70  TYR   N CA  
23653 C  C   . TYR   N  70  ? 1.8205 0.6243 1.2819 -0.1016 -0.2034 -0.0850 70  TYR   N C   
23654 O  O   . TYR   N  70  ? 1.8148 0.7873 1.2612 -0.1728 -0.1948 -0.1350 70  TYR   N O   
23655 C  CB  . TYR   N  70  ? 1.7627 0.6206 1.2883 -0.0019 -0.1418 -0.0305 70  TYR   N CB  
23656 C  CG  . TYR   N  70  ? 1.7698 0.6227 1.3192 0.0725  -0.1020 0.0254  70  TYR   N CG  
23657 C  CD1 . TYR   N  70  ? 1.7840 0.6218 1.3425 0.0696  -0.0581 0.0604  70  TYR   N CD1 
23658 C  CD2 . TYR   N  70  ? 1.7645 0.6415 1.2990 0.0655  -0.1090 0.0295  70  TYR   N CD2 
23659 C  CE1 . TYR   N  70  ? 1.7671 0.6120 1.3597 0.0630  -0.0227 0.1133  70  TYR   N CE1 
23660 C  CE2 . TYR   N  70  ? 1.7370 0.5885 1.3330 0.0903  -0.0747 0.0977  70  TYR   N CE2 
23661 C  CZ  . TYR   N  70  ? 1.7430 0.5869 1.3395 0.0807  -0.0389 0.1374  70  TYR   N CZ  
23662 O  OH  . TYR   N  70  ? 1.7394 0.6380 1.3502 0.0957  -0.0258 0.1674  70  TYR   N OH  
23663 N  N   . GLY   N  71  ? 1.8209 0.6367 1.3566 -0.1163 -0.2148 -0.0592 71  GLY   N N   
23664 C  CA  . GLY   N  71  ? 1.8268 0.6708 1.3772 -0.0774 -0.2231 -0.0551 71  GLY   N CA  
23665 C  C   . GLY   N  71  ? 1.8036 0.6774 1.2736 -0.0469 -0.2954 -0.0748 71  GLY   N C   
23666 O  O   . GLY   N  71  ? 1.7495 0.5784 1.2633 -0.0196 -0.3717 -0.0262 71  GLY   N O   
23667 N  N   . THR   N  72  ? 1.8271 0.7110 1.2632 -0.0519 -0.2614 -0.0655 72  THR   N N   
23668 C  CA  . THR   N  72  ? 1.7840 0.7049 1.1348 -0.0724 -0.2645 -0.0670 72  THR   N CA  
23669 C  C   . THR   N  72  ? 1.7223 0.7354 1.1615 -0.0773 -0.2140 -0.0664 72  THR   N C   
23670 O  O   . THR   N  72  ? 1.7010 0.7604 1.1556 -0.1182 -0.2064 -0.0966 72  THR   N O   
23671 C  CB  . THR   N  72  ? 1.8010 0.7604 1.1125 -0.0506 -0.2786 -0.0804 72  THR   N CB  
23672 O  OG1 . THR   N  72  ? 1.7858 0.7693 1.0862 -0.0440 -0.3284 0.0090  72  THR   N OG1 
23673 C  CG2 . THR   N  72  ? 1.7834 0.7805 1.0622 -0.0252 -0.3189 -0.0688 72  THR   N CG2 
23674 N  N   . PRO   N  73  ? 1.7291 0.7405 1.1316 -0.0753 -0.1937 -0.0448 73  PRO   N N   
23675 C  CA  . PRO   N  73  ? 1.7356 0.6570 1.1247 -0.0699 -0.1553 -0.0768 73  PRO   N CA  
23676 C  C   . PRO   N  73  ? 1.7090 0.6113 1.1479 -0.0937 -0.1716 -0.1145 73  PRO   N C   
23677 O  O   . PRO   N  73  ? 1.7379 0.5190 1.1560 -0.1078 -0.1898 -0.1252 73  PRO   N O   
23678 C  CB  . PRO   N  73  ? 1.7210 0.6420 1.0886 -0.0755 -0.1639 -0.0349 73  PRO   N CB  
23679 C  CG  . PRO   N  73  ? 1.7283 0.6696 1.0582 -0.0599 -0.1842 -0.0300 73  PRO   N CG  
23680 C  CD  . PRO   N  73  ? 1.7416 0.7106 1.0774 -0.0647 -0.1972 -0.0515 73  PRO   N CD  
23681 N  N   . SER   N  74  ? 1.6988 0.6796 1.1995 -0.0922 -0.1466 -0.1292 74  SER   N N   
23682 C  CA  . SER   N  74  ? 1.7454 0.6867 1.1864 -0.0552 -0.1524 -0.0858 74  SER   N CA  
23683 C  C   . SER   N  74  ? 1.7093 0.6112 1.2387 -0.0580 -0.2073 -0.0752 74  SER   N C   
23684 O  O   . SER   N  74  ? 1.6903 0.5055 1.2683 -0.0731 -0.1620 -0.0624 74  SER   N O   
23685 C  CB  . SER   N  74  ? 1.7555 0.7741 1.1609 -0.0576 -0.1232 -0.0510 74  SER   N CB  
23686 O  OG  . SER   N  74  ? 1.7384 0.8216 1.1581 -0.0559 -0.1261 -0.0588 74  SER   N OG  
23687 N  N   . THR   N  75  ? 1.7056 0.5403 1.3255 -0.0172 -0.2568 -0.1253 75  THR   N N   
23688 C  CA  . THR   N  75  ? 1.7193 0.5176 1.3806 -0.0333 -0.2673 -0.1285 75  THR   N CA  
23689 C  C   . THR   N  75  ? 1.6769 0.4066 1.3995 -0.0271 -0.2486 -0.1576 75  THR   N C   
23690 O  O   . THR   N  75  ? 1.6502 0.3290 1.4630 0.0010  -0.2176 -0.1953 75  THR   N O   
23691 C  CB  . THR   N  75  ? 1.7774 0.5637 1.3984 -0.0824 -0.2677 -0.0950 75  THR   N CB  
23692 O  OG1 . THR   N  75  ? 1.7888 0.5950 1.4622 -0.1005 -0.3209 -0.0759 75  THR   N OG1 
23693 C  CG2 . THR   N  75  ? 1.7683 0.6021 1.3640 -0.0812 -0.2753 -0.1244 75  THR   N CG2 
23694 N  N   . GLU   N  76  ? 1.6685 0.4107 1.3951 -0.0662 -0.2352 -0.1504 76  GLU   N N   
23695 C  CA  . GLU   N  76  ? 1.6525 0.4764 1.3073 -0.0868 -0.1985 -0.0962 76  GLU   N CA  
23696 C  C   . GLU   N  76  ? 1.6304 0.5086 1.2300 -0.0769 -0.2618 -0.0935 76  GLU   N C   
23697 O  O   . GLU   N  76  ? 1.5686 0.4777 1.1431 -0.1294 -0.2291 0.0034  76  GLU   N O   
23698 C  CB  . GLU   N  76  ? 1.6918 0.5493 1.4179 -0.0702 -0.1398 -0.1253 76  GLU   N CB  
23699 C  CG  . GLU   N  76  ? 1.6875 0.6383 1.4272 -0.0405 -0.1388 -0.1264 76  GLU   N CG  
23700 C  CD  . GLU   N  76  ? 1.7369 0.6257 1.5496 -0.0250 -0.0631 -0.1019 76  GLU   N CD  
23701 O  OE1 . GLU   N  76  ? 1.7029 0.7359 1.5942 -0.0743 -0.0205 -0.0111 76  GLU   N OE1 
23702 O  OE2 . GLU   N  76  ? 1.7880 0.5100 1.7135 -0.2264 -0.1349 -0.1065 76  GLU   N OE2 
23703 N  N   . THR   N  77  ? 1.6492 0.4825 1.1157 -0.0593 -0.2455 -0.0312 77  THR   N N   
23704 C  CA  . THR   N  77  ? 1.6496 0.5734 1.0687 -0.0217 -0.2024 -0.0289 77  THR   N CA  
23705 C  C   . THR   N  77  ? 1.6376 0.4836 1.0926 -0.0054 -0.2356 -0.0491 77  THR   N C   
23706 O  O   . THR   N  77  ? 1.6785 0.3857 1.0889 0.0102  -0.1648 -0.0616 77  THR   N O   
23707 C  CB  . THR   N  77  ? 1.6941 0.5716 1.0509 -0.0390 -0.2000 -0.0076 77  THR   N CB  
23708 O  OG1 . THR   N  77  ? 1.6863 0.6388 1.0706 -0.0271 -0.1758 0.0426  77  THR   N OG1 
23709 C  CG2 . THR   N  77  ? 1.6868 0.5550 1.0740 -0.0352 -0.1893 -0.0001 77  THR   N CG2 
23710 N  N   . ALA   N  78  ? 1.6268 0.4655 1.0325 0.0009  -0.2286 -0.0988 78  ALA   N N   
23711 C  CA  . ALA   N  78  ? 1.6185 0.5139 1.0452 0.0033  -0.2190 -0.0809 78  ALA   N CA  
23712 C  C   . ALA   N  78  ? 1.5846 0.5170 1.0484 -0.0172 -0.2168 -0.0642 78  ALA   N C   
23713 O  O   . ALA   N  78  ? 1.5629 0.6041 1.1058 -0.0008 -0.1418 -0.0212 78  ALA   N O   
23714 C  CB  . ALA   N  78  ? 1.6453 0.4750 1.0450 -0.0123 -0.2440 -0.1037 78  ALA   N CB  
23715 N  N   . ALA   N  79  ? 1.5807 0.5082 1.0336 0.0005  -0.2160 -0.0465 79  ALA   N N   
23716 C  CA  . ALA   N  79  ? 1.5859 0.4891 1.0106 0.0355  -0.1925 -0.0708 79  ALA   N CA  
23717 C  C   . ALA   N  79  ? 1.5811 0.4155 1.0096 0.0526  -0.1844 -0.0811 79  ALA   N C   
23718 O  O   . ALA   N  79  ? 1.6019 0.3632 1.0171 0.0533  -0.1773 -0.0651 79  ALA   N O   
23719 C  CB  . ALA   N  79  ? 1.5771 0.5243 1.0102 0.0138  -0.1670 -0.1089 79  ALA   N CB  
23720 N  N   . SER   N  80  ? 1.5385 0.4613 0.9749 0.0785  -0.1990 -0.0633 80  SER   N N   
23721 C  CA  . SER   N  80  ? 1.5167 0.4491 0.9534 0.0683  -0.1764 -0.0501 80  SER   N CA  
23722 C  C   . SER   N  80  ? 1.4702 0.4528 0.9739 0.0606  -0.1743 -0.0573 80  SER   N C   
23723 O  O   . SER   N  80  ? 1.4418 0.4519 0.9613 0.0845  -0.1375 -0.0844 80  SER   N O   
23724 C  CB  . SER   N  80  ? 1.5424 0.3782 0.9512 0.0536  -0.1700 -0.0107 80  SER   N CB  
23725 O  OG  . SER   N  80  ? 1.5637 0.2180 0.9872 0.0892  -0.1306 0.0419  80  SER   N OG  
23726 N  N   . VAL   N  81  ? 1.4938 0.4631 0.9413 0.0387  -0.1842 -0.0655 81  VAL   N N   
23727 C  CA  . VAL   N  81  ? 1.5409 0.5133 0.9575 0.0348  -0.1714 -0.0483 81  VAL   N CA  
23728 C  C   . VAL   N  81  ? 1.5741 0.4573 1.0025 0.0284  -0.2011 -0.0389 81  VAL   N C   
23729 O  O   . VAL   N  81  ? 1.6158 0.5348 1.0080 0.0164  -0.1811 -0.0418 81  VAL   N O   
23730 C  CB  . VAL   N  81  ? 1.5710 0.5577 0.9427 0.0301  -0.1838 -0.0824 81  VAL   N CB  
23731 C  CG1 . VAL   N  81  ? 1.5787 0.5779 0.9415 0.0151  -0.1874 -0.0703 81  VAL   N CG1 
23732 C  CG2 . VAL   N  81  ? 1.5744 0.5725 0.9525 0.0325  -0.1638 -0.0900 81  VAL   N CG2 
23733 N  N   . PHE   N  82  ? 1.5554 0.4362 1.0343 0.0293  -0.2047 -0.0407 82  PHE   N N   
23734 C  CA  . PHE   N  82  ? 1.5322 0.4264 1.0279 0.0210  -0.1912 -0.0300 82  PHE   N CA  
23735 C  C   . PHE   N  82  ? 1.5384 0.3598 1.0226 0.0295  -0.1725 -0.0555 82  PHE   N C   
23736 O  O   . PHE   N  82  ? 1.5199 0.3300 1.0256 -0.0104 -0.1430 -0.0392 82  PHE   N O   
23737 C  CB  . PHE   N  82  ? 1.5039 0.3796 1.0346 0.0300  -0.1950 -0.0496 82  PHE   N CB  
23738 C  CG  . PHE   N  82  ? 1.5087 0.3100 1.0184 0.0608  -0.2094 -0.0537 82  PHE   N CG  
23739 C  CD1 . PHE   N  82  ? 1.5213 0.2742 1.0067 0.0648  -0.2215 -0.0661 82  PHE   N CD1 
23740 C  CD2 . PHE   N  82  ? 1.5102 0.3617 1.0103 0.0658  -0.2219 -0.0483 82  PHE   N CD2 
23741 C  CE1 . PHE   N  82  ? 1.5345 0.3197 1.0201 0.0383  -0.2389 -0.0948 82  PHE   N CE1 
23742 C  CE2 . PHE   N  82  ? 1.5168 0.4022 1.0163 0.0447  -0.2276 -0.0702 82  PHE   N CE2 
23743 C  CZ  . PHE   N  82  ? 1.5465 0.3556 1.0247 0.0319  -0.2299 -0.1128 82  PHE   N CZ  
23744 N  N   . LYS   N  83  ? 1.5565 0.3792 1.0804 0.0848  -0.1358 -0.0059 83  LYS   N N   
23745 C  CA  . LYS   N  83  ? 1.5183 0.4467 1.1249 0.1273  -0.1554 0.0266  83  LYS   N CA  
23746 C  C   . LYS   N  83  ? 1.5421 0.4885 1.1633 0.1538  -0.1335 0.0720  83  LYS   N C   
23747 O  O   . LYS   N  83  ? 1.5585 0.4439 1.1408 0.1204  -0.1660 0.1225  83  LYS   N O   
23748 C  CB  . LYS   N  83  ? 1.5378 0.4615 1.1599 0.2125  -0.1364 0.0797  83  LYS   N CB  
23749 C  CG  . LYS   N  83  ? 1.5237 0.5002 1.1658 0.2677  -0.1657 0.1094  83  LYS   N CG  
23750 C  CD  . LYS   N  83  ? 1.5371 0.5644 1.2166 0.3002  -0.1597 0.1086  83  LYS   N CD  
23751 C  CE  . LYS   N  83  ? 1.5408 0.5942 1.2532 0.3473  -0.1491 0.1450  83  LYS   N CE  
23752 N  NZ  . LYS   N  83  ? 1.5119 0.6818 1.2934 0.4304  -0.1364 0.1714  83  LYS   N NZ  
23753 N  N   . GLU   N  84  ? 1.5432 0.4953 1.2307 0.1283  -0.1205 0.0524  84  GLU   N N   
23754 C  CA  . GLU   N  84  ? 1.5297 0.5895 1.2354 0.1279  -0.1322 0.0776  84  GLU   N CA  
23755 C  C   . GLU   N  84  ? 1.5402 0.5804 1.1748 0.1188  -0.1769 0.0144  84  GLU   N C   
23756 O  O   . GLU   N  84  ? 1.5114 0.6122 1.1661 0.0902  -0.1596 -0.0135 84  GLU   N O   
23757 C  CB  . GLU   N  84  ? 1.5428 0.5896 1.3693 0.1304  -0.1105 0.0627  84  GLU   N CB  
23758 C  CG  . GLU   N  84  ? 1.5385 0.6986 1.4225 0.1630  -0.1315 0.0963  84  GLU   N CG  
23759 C  CD  . GLU   N  84  ? 1.5461 0.7300 1.4472 0.1626  -0.1143 0.1671  84  GLU   N CD  
23760 O  OE1 . GLU   N  84  ? 1.6285 0.8935 1.4742 0.2010  -0.1460 0.2638  84  GLU   N OE1 
23761 O  OE2 . GLU   N  84  ? 1.5961 0.7069 1.5150 0.1416  -0.0243 0.1281  84  GLU   N OE2 
23762 N  N   . LEU   N  85  ? 1.5471 0.5806 1.1471 0.1133  -0.1945 -0.0065 85  LEU   N N   
23763 C  CA  . LEU   N  85  ? 1.5476 0.6659 1.0850 0.0605  -0.1950 0.0132  85  LEU   N CA  
23764 C  C   . LEU   N  85  ? 1.6037 0.6989 1.0593 0.0198  -0.1888 -0.0079 85  LEU   N C   
23765 O  O   . LEU   N  85  ? 1.5967 0.7263 1.0392 -0.0127 -0.1631 0.0537  85  LEU   N O   
23766 C  CB  . LEU   N  85  ? 1.5568 0.6568 1.1125 0.0090  -0.2038 0.0001  85  LEU   N CB  
23767 C  CG  . LEU   N  85  ? 1.5794 0.5926 1.1583 0.0183  -0.1815 0.0831  85  LEU   N CG  
23768 C  CD1 . LEU   N  85  ? 1.5762 0.6598 1.2465 -0.0073 -0.1995 0.0254  85  LEU   N CD1 
23769 C  CD2 . LEU   N  85  ? 1.5612 0.5845 1.1564 0.0439  -0.2107 0.1040  85  LEU   N CD2 
23770 N  N   . CYS   N  86  ? 1.6210 0.6544 1.0111 -0.0101 -0.1789 -0.0610 86  CYS   N N   
23771 C  CA  . CYS   N  86  ? 1.6095 0.6765 0.9952 -0.0398 -0.1834 -0.1073 86  CYS   N CA  
23772 C  C   . CYS   N  86  ? 1.5616 0.6611 0.9978 -0.0322 -0.1550 -0.0762 86  CYS   N C   
23773 O  O   . CYS   N  86  ? 1.6383 0.9401 0.9145 -0.1424 -0.2017 -0.1605 86  CYS   N O   
23774 C  CB  . CYS   N  86  ? 1.6163 0.6879 0.9781 -0.0263 -0.2050 -0.1249 86  CYS   N CB  
23775 S  SG  . CYS   N  86  ? 1.6336 0.6238 1.0846 -0.0234 -0.2454 -0.1631 86  CYS   N SG  
23776 N  N   . TYR   N  87  ? 1.5851 0.4910 0.9275 -0.0482 -0.1540 -0.0657 87  TYR   N N   
23777 C  CA  . TYR   N  87  ? 1.5833 0.4759 0.9114 -0.0286 -0.1584 -0.0505 87  TYR   N CA  
23778 C  C   . TYR   N  87  ? 1.6217 0.4965 0.9275 -0.0193 -0.1613 -0.0175 87  TYR   N C   
23779 O  O   . TYR   N  87  ? 1.6411 0.5125 0.8326 -0.0262 -0.1757 0.0508  87  TYR   N O   
23780 C  CB  . TYR   N  87  ? 1.5712 0.4499 0.9684 -0.0163 -0.1645 -0.0574 87  TYR   N CB  
23781 C  CG  . TYR   N  87  ? 1.5627 0.4581 0.9884 0.0185  -0.1720 -0.0717 87  TYR   N CG  
23782 C  CD1 . TYR   N  87  ? 1.5340 0.5059 1.0002 -0.0176 -0.1779 -0.0642 87  TYR   N CD1 
23783 C  CD2 . TYR   N  87  ? 1.5452 0.4551 0.9910 0.0024  -0.1785 -0.0656 87  TYR   N CD2 
23784 C  CE1 . TYR   N  87  ? 1.5264 0.5579 1.0048 0.0200  -0.1807 -0.0289 87  TYR   N CE1 
23785 C  CE2 . TYR   N  87  ? 1.5536 0.5172 0.9942 -0.0011 -0.1801 -0.0634 87  TYR   N CE2 
23786 C  CZ  . TYR   N  87  ? 1.5656 0.5048 1.0181 0.0045  -0.1555 -0.0339 87  TYR   N CZ  
23787 O  OH  . TYR   N  87  ? 1.5445 0.5716 1.0135 -0.0021 -0.1303 -0.0016 87  TYR   N OH  
23788 N  N   . GLU   N  88  ? 1.6270 0.5154 0.9353 -0.0205 -0.1621 0.0361  88  GLU   N N   
23789 C  CA  . GLU   N  88  ? 1.6132 0.6174 0.9468 -0.0013 -0.1577 0.0765  88  GLU   N CA  
23790 C  C   . GLU   N  88  ? 1.5741 0.5874 0.9622 0.0092  -0.1795 0.0688  88  GLU   N C   
23791 O  O   . GLU   N  88  ? 1.6034 0.5940 0.9485 0.0209  -0.1347 0.0553  88  GLU   N O   
23792 C  CB  . GLU   N  88  ? 1.6336 0.6083 0.9809 -0.0388 -0.1327 0.1394  88  GLU   N CB  
23793 C  CG  . GLU   N  88  ? 1.6723 0.6148 1.0270 -0.0152 -0.0945 0.1713  88  GLU   N CG  
23794 C  CD  . GLU   N  88  ? 1.6778 0.6528 1.0773 -0.0002 -0.0979 0.2027  88  GLU   N CD  
23795 O  OE1 . GLU   N  88  ? 1.7878 0.6811 1.0773 0.0137  -0.0965 0.2168  88  GLU   N OE1 
23796 O  OE2 . GLU   N  88  ? 1.7370 0.6355 1.1115 0.0277  -0.0372 0.2637  88  GLU   N OE2 
23797 N  N   . ASN   N  89  ? 1.5567 0.6251 0.9982 -0.0069 -0.2256 0.0634  89  ASN   N N   
23798 C  CA  . ASN   N  89  ? 1.5261 0.6995 1.0657 0.0118  -0.2299 0.0718  89  ASN   N CA  
23799 C  C   . ASN   N  89  ? 1.5587 0.7008 1.1782 -0.0483 -0.2223 0.0893  89  ASN   N C   
23800 O  O   . ASN   N  89  ? 1.5776 0.8252 1.3327 -0.0499 -0.1211 0.0599  89  ASN   N O   
23801 C  CB  . ASN   N  89  ? 1.5608 0.7187 1.0834 -0.0134 -0.2521 0.0458  89  ASN   N CB  
23802 C  CG  . ASN   N  89  ? 1.5620 0.7348 1.0440 0.0006  -0.2719 0.0704  89  ASN   N CG  
23803 O  OD1 . ASN   N  89  ? 1.4357 0.9028 1.0092 -0.0138 -0.2808 0.0573  89  ASN   N OD1 
23804 N  ND2 . ASN   N  89  ? 1.6214 0.8046 1.0861 0.0138  -0.2645 0.0157  89  ASN   N ND2 
23805 N  N   . LYS   N  90  ? 1.5148 0.6566 1.2088 -0.0070 -0.2190 0.0629  90  LYS   N N   
23806 C  CA  . LYS   N  90  ? 1.5436 0.6211 1.2180 -0.0387 -0.1834 -0.0275 90  LYS   N CA  
23807 C  C   . LYS   N  90  ? 1.6179 0.7457 1.0953 -0.1028 -0.2337 -0.0517 90  LYS   N C   
23808 O  O   . LYS   N  90  ? 1.5694 0.8282 1.1453 -0.0520 -0.2671 -0.0730 90  LYS   N O   
23809 C  CB  . LYS   N  90  ? 1.5496 0.4710 1.2280 -0.0268 -0.1655 -0.0359 90  LYS   N CB  
23810 C  CG  . LYS   N  90  ? 1.5695 0.4477 1.2222 0.0227  -0.1479 0.0039  90  LYS   N CG  
23811 C  CD  . LYS   N  90  ? 1.5532 0.5015 1.2670 0.0471  -0.1017 0.0029  90  LYS   N CD  
23812 C  CE  . LYS   N  90  ? 1.6118 0.5409 1.3125 0.0587  -0.0767 -0.0515 90  LYS   N CE  
23813 N  NZ  . LYS   N  90  ? 1.6271 0.6583 1.3745 0.0228  -0.0121 -0.0778 90  LYS   N NZ  
23814 N  N   . ASP   N  91  ? 1.6552 0.6752 1.1274 -0.0486 -0.2677 -0.0229 91  ASP   N N   
23815 C  CA  . ASP   N  91  ? 1.7075 0.7236 1.0887 -0.0253 -0.2278 0.0261  91  ASP   N CA  
23816 C  C   . ASP   N  91  ? 1.7086 0.6616 1.0669 -0.0719 -0.1851 -0.0299 91  ASP   N C   
23817 O  O   . ASP   N  91  ? 1.7179 0.8832 1.0349 -0.0678 -0.0830 -0.0626 91  ASP   N O   
23818 C  CB  . ASP   N  91  ? 1.8719 0.7723 1.0909 -0.0203 -0.2192 0.0939  91  ASP   N CB  
23819 C  CG  . ASP   N  91  ? 1.8968 0.8288 1.1242 0.0232  -0.2689 0.1511  91  ASP   N CG  
23820 O  OD1 . ASP   N  91  ? 2.0384 1.0244 1.0958 0.0103  -0.2093 0.1869  91  ASP   N OD1 
23821 O  OD2 . ASP   N  91  ? 2.0464 0.6855 1.2431 0.0760  -0.2452 0.2096  91  ASP   N OD2 
23822 N  N   . ASN   N  92  ? 1.6957 0.5053 1.0603 -0.0069 -0.1368 -0.0497 92  ASN   N N   
23823 C  CA  . ASN   N  92  ? 1.6760 0.5161 1.0913 0.0243  -0.1639 -0.1295 92  ASN   N CA  
23824 C  C   . ASN   N  92  ? 1.6164 0.4448 1.1529 -0.0026 -0.1931 -0.1097 92  ASN   N C   
23825 O  O   . ASN   N  92  ? 1.6343 0.3420 1.2494 0.0000  -0.1493 -0.1079 92  ASN   N O   
23826 C  CB  . ASN   N  92  ? 1.7003 0.5060 1.1210 0.0630  -0.1266 -0.1309 92  ASN   N CB  
23827 C  CG  . ASN   N  92  ? 1.7504 0.6265 1.1232 0.1070  -0.1337 -0.1808 92  ASN   N CG  
23828 O  OD1 . ASN   N  92  ? 1.7301 0.5254 1.2701 0.2140  -0.0747 -0.2209 92  ASN   N OD1 
23829 N  ND2 . ASN   N  92  ? 1.7753 0.7047 1.2289 0.1634  -0.1312 -0.1210 92  ASN   N ND2 
23830 N  N   . LEU   N  93  ? 1.5417 0.5431 1.1539 -0.0457 -0.2464 -0.0764 93  LEU   N N   
23831 C  CA  . LEU   N  93  ? 1.5430 0.5964 1.1801 -0.0616 -0.2775 -0.0559 93  LEU   N CA  
23832 C  C   . LEU   N  93  ? 1.4867 0.5766 1.2600 -0.0916 -0.3030 -0.0746 93  LEU   N C   
23833 O  O   . LEU   N  93  ? 1.5451 0.4061 1.3772 -0.0986 -0.3384 -0.0294 93  LEU   N O   
23834 C  CB  . LEU   N  93  ? 1.5272 0.6900 1.1184 -0.0328 -0.2895 -0.0446 93  LEU   N CB  
23835 C  CG  . LEU   N  93  ? 1.4845 0.7054 1.0775 -0.0294 -0.2927 0.0094  93  LEU   N CG  
23836 C  CD1 . LEU   N  93  ? 1.4672 0.7214 1.0493 -0.0170 -0.3132 0.0096  93  LEU   N CD1 
23837 C  CD2 . LEU   N  93  ? 1.4892 0.7230 1.1085 -0.0793 -0.2614 0.0022  93  LEU   N CD2 
23838 N  N   . THR   N  94  ? 1.5117 0.5829 1.2584 -0.0412 -0.2636 -0.0332 94  THR   N N   
23839 C  CA  . THR   N  94  ? 1.5487 0.6292 1.1806 -0.0525 -0.2452 -0.0228 94  THR   N CA  
23840 C  C   . THR   N  94  ? 1.5325 0.5438 1.1883 -0.0511 -0.2089 -0.0691 94  THR   N C   
23841 O  O   . THR   N  94  ? 1.5332 0.5425 1.2216 -0.0752 -0.2329 -0.1456 94  THR   N O   
23842 C  CB  . THR   N  94  ? 1.5700 0.7438 1.1359 -0.0183 -0.2303 -0.0487 94  THR   N CB  
23843 O  OG1 . THR   N  94  ? 1.5581 0.8397 1.1101 -0.0266 -0.2015 -0.0106 94  THR   N OG1 
23844 C  CG2 . THR   N  94  ? 1.5952 0.7779 1.1444 -0.0416 -0.2388 -0.0287 94  THR   N CG2 
23845 N  N   . ALA   N  95  ? 1.5149 0.4558 1.2513 -0.0440 -0.1866 -0.0479 95  ALA   N N   
23846 C  CA  . ALA   N  95  ? 1.5029 0.4539 1.2426 -0.0030 -0.1369 -0.0552 95  ALA   N CA  
23847 C  C   . ALA   N  95  ? 1.4611 0.3767 1.2688 0.0268  -0.1436 -0.0456 95  ALA   N C   
23848 O  O   . ALA   N  95  ? 1.4321 0.3544 1.3392 -0.0039 -0.1502 -0.1239 95  ALA   N O   
23849 C  CB  . ALA   N  95  ? 1.5212 0.4552 1.2578 0.0120  -0.0904 -0.0166 95  ALA   N CB  
23850 N  N   . GLY   N  96  ? 1.5225 0.3951 1.2507 -0.0100 -0.1369 -0.0156 96  GLY   N N   
23851 C  CA  . GLY   N  96  ? 1.5503 0.4605 1.1907 0.0217  -0.1533 -0.0485 96  GLY   N CA  
23852 C  C   . GLY   N  96  ? 1.6095 0.4546 1.1997 0.0308  -0.1673 -0.0665 96  GLY   N C   
23853 O  O   . GLY   N  96  ? 1.5974 0.6275 1.2653 0.0733  -0.1885 -0.1395 96  GLY   N O   
23854 N  N   . ILE   N  97  ? 1.6494 0.4188 1.1352 0.0331  -0.1753 -0.0248 97  ILE   N N   
23855 C  CA  . ILE   N  97  ? 1.6911 0.4638 1.1362 0.0217  -0.1696 -0.0490 97  ILE   N CA  
23856 C  C   . ILE   N  97  ? 1.6492 0.3926 1.1300 0.0304  -0.1867 -0.0410 97  ILE   N C   
23857 O  O   . ILE   N  97  ? 1.6401 0.3729 1.2129 0.0740  -0.1493 -0.1350 97  ILE   N O   
23858 C  CB  . ILE   N  97  ? 1.7302 0.4867 1.0752 0.0777  -0.1855 -0.0097 97  ILE   N CB  
23859 C  CG1 . ILE   N  97  ? 1.7244 0.5249 1.0312 0.0599  -0.2211 0.0140  97  ILE   N CG1 
23860 C  CG2 . ILE   N  97  ? 1.7503 0.4815 1.1427 0.0981  -0.1880 -0.0439 97  ILE   N CG2 
23861 C  CD1 . ILE   N  97  ? 1.7169 0.4787 1.1007 0.0706  -0.1990 0.0016  97  ILE   N CD1 
23862 N  N   . ILE   N  98  ? 1.6523 0.3832 1.1261 0.0098  -0.1963 -0.0064 98  ILE   N N   
23863 C  CA  . ILE   N  98  ? 1.6275 0.4899 1.0977 0.0062  -0.2390 -0.0221 98  ILE   N CA  
23864 C  C   . ILE   N  98  ? 1.5776 0.4529 1.1032 -0.0009 -0.2756 0.0473  98  ILE   N C   
23865 O  O   . ILE   N  98  ? 1.5621 0.4418 1.1615 0.0294  -0.2408 0.1233  98  ILE   N O   
23866 C  CB  . ILE   N  98  ? 1.6583 0.5574 1.0840 0.0178  -0.2667 -0.0078 98  ILE   N CB  
23867 C  CG1 . ILE   N  98  ? 1.6265 0.6348 1.0809 0.0010  -0.2778 -0.0774 98  ILE   N CG1 
23868 C  CG2 . ILE   N  98  ? 1.6911 0.5876 1.0907 0.0080  -0.2580 -0.0223 98  ILE   N CG2 
23869 C  CD1 . ILE   N  98  ? 1.6102 0.6822 1.0871 0.0087  -0.3034 -0.0705 98  ILE   N CD1 
23870 N  N   . VAL   N  99  ? 1.5661 0.4359 1.0728 -0.0193 -0.3128 0.0076  99  VAL   N N   
23871 C  CA  . VAL   N  99  ? 1.6003 0.4561 1.0357 -0.0280 -0.3294 -0.0074 99  VAL   N CA  
23872 C  C   . VAL   N  99  ? 1.6149 0.4176 1.0263 -0.0369 -0.3353 -0.0115 99  VAL   N C   
23873 O  O   . VAL   N  99  ? 1.5929 0.4348 0.9525 -0.0203 -0.3517 -0.0067 99  VAL   N O   
23874 C  CB  . VAL   N  99  ? 1.6475 0.3715 1.0379 -0.0475 -0.3392 -0.0331 99  VAL   N CB  
23875 C  CG1 . VAL   N  99  ? 1.6563 0.4037 1.0485 -0.0801 -0.3448 -0.0504 99  VAL   N CG1 
23876 C  CG2 . VAL   N  99  ? 1.6581 0.3400 1.0373 -0.0317 -0.3252 -0.0509 99  VAL   N CG2 
23877 N  N   . ALA   N  100 ? 1.6149 0.4255 1.0410 -0.0428 -0.3507 0.0120  100 ALA   N N   
23878 C  CA  . ALA   N  100 ? 1.6463 0.5090 1.0445 -0.0257 -0.3462 0.0384  100 ALA   N CA  
23879 C  C   . ALA   N  100 ? 1.6986 0.5390 1.0404 -0.0213 -0.3441 0.0007  100 ALA   N C   
23880 O  O   . ALA   N  100 ? 1.6853 0.6005 1.0892 0.0093  -0.3364 -0.0107 100 ALA   N O   
23881 C  CB  . ALA   N  100 ? 1.6295 0.5321 1.0140 -0.0256 -0.3787 0.0305  100 ALA   N CB  
23882 N  N   . GLY   N  101 ? 1.7182 0.6518 1.0643 -0.0116 -0.2715 0.0242  101 GLY   N N   
23883 C  CA  . GLY   N  101 ? 1.7909 0.7022 1.1100 -0.0275 -0.2327 -0.0408 101 GLY   N CA  
23884 C  C   . GLY   N  101 ? 1.8868 0.7716 1.1309 -0.0281 -0.1745 0.0195  101 GLY   N C   
23885 O  O   . GLY   N  101 ? 1.9321 0.7095 1.0642 -0.0224 -0.2079 0.0579  101 GLY   N O   
23886 N  N   . TYR   N  102 ? 1.9651 0.8747 1.2406 -0.0222 -0.1787 -0.0865 102 TYR   N N   
23887 C  CA  . TYR   N  102 ? 1.9906 0.9768 1.2586 0.0530  -0.1532 -0.0727 102 TYR   N CA  
23888 C  C   . TYR   N  102 ? 2.0082 0.9933 1.4030 0.0681  -0.1564 -0.0871 102 TYR   N C   
23889 O  O   . TYR   N  102 ? 2.0727 0.8880 1.3463 0.0690  -0.2299 -0.1049 102 TYR   N O   
23890 C  CB  . TYR   N  102 ? 1.9928 0.9152 1.2373 0.0656  -0.1511 -0.0921 102 TYR   N CB  
23891 C  CG  . TYR   N  102 ? 1.9884 0.8998 1.2523 0.0379  -0.1097 -0.0870 102 TYR   N CG  
23892 C  CD1 . TYR   N  102 ? 2.0037 0.8652 1.2429 0.0459  -0.0892 -0.1061 102 TYR   N CD1 
23893 C  CD2 . TYR   N  102 ? 2.0131 0.9602 1.2606 0.0176  -0.0921 -0.1415 102 TYR   N CD2 
23894 C  CE1 . TYR   N  102 ? 2.0339 0.8776 1.2335 0.0071  -0.0971 -0.1103 102 TYR   N CE1 
23895 C  CE2 . TYR   N  102 ? 2.0391 0.9242 1.2430 -0.0392 -0.0983 -0.1290 102 TYR   N CE2 
23896 C  CZ  . TYR   N  102 ? 2.0609 0.9226 1.1498 -0.0183 -0.0909 -0.1312 102 TYR   N CZ  
23897 O  OH  . TYR   N  102 ? 2.1036 0.7966 1.1211 -0.1294 -0.1264 -0.1737 102 TYR   N OH  
23898 N  N   . ASP   N  103 ? 2.0235 1.0591 1.5391 0.1671  -0.1601 -0.0593 103 ASP   N N   
23899 C  CA  . ASP   N  103 ? 2.0559 0.9943 1.5324 0.1353  -0.1901 -0.0586 103 ASP   N CA  
23900 C  C   . ASP   N  103 ? 2.0749 0.9951 1.5149 0.1180  -0.1795 -0.1970 103 ASP   N C   
23901 O  O   . ASP   N  103 ? 2.0790 0.9949 1.4983 0.0771  -0.2107 -0.2011 103 ASP   N O   
23902 C  CB  . ASP   N  103 ? 2.0293 0.9758 1.7203 0.2009  -0.1514 0.0389  103 ASP   N CB  
23903 C  CG  . ASP   N  103 ? 2.0254 1.1043 1.7782 0.2186  -0.1557 0.1252  103 ASP   N CG  
23904 O  OD1 . ASP   N  103 ? 2.0891 1.0947 2.0439 0.1264  -0.0640 0.0213  103 ASP   N OD1 
23905 O  OD2 . ASP   N  103 ? 1.9100 0.8260 1.8619 0.2180  -0.1942 0.2507  103 ASP   N OD2 
23906 N  N   . ASP   N  104 ? 2.1298 1.0154 1.4995 0.0748  -0.1463 -0.2212 104 ASP   N N   
23907 C  CA  . ASP   N  104 ? 2.2137 1.0755 1.4976 0.0287  -0.1506 -0.3134 104 ASP   N CA  
23908 C  C   . ASP   N  104 ? 2.2470 0.9754 1.4559 0.0197  -0.0759 -0.3601 104 ASP   N C   
23909 O  O   . ASP   N  104 ? 2.2554 0.9584 1.3257 0.0142  -0.0948 -0.4423 104 ASP   N O   
23910 C  CB  . ASP   N  104 ? 2.2051 1.2221 1.4618 -0.0950 -0.2152 -0.3019 104 ASP   N CB  
23911 C  CG  . ASP   N  104 ? 2.2677 1.3187 1.4509 -0.1848 -0.2463 -0.3029 104 ASP   N CG  
23912 O  OD1 . ASP   N  104 ? 2.2931 1.4130 1.4593 -0.3059 -0.2661 -0.2711 104 ASP   N OD1 
23913 O  OD2 . ASP   N  104 ? 2.2694 1.3438 1.4115 -0.1850 -0.2635 -0.3201 104 ASP   N OD2 
23914 N  N   . LYS   N  105 ? 2.2604 0.8906 1.5587 0.0407  -0.1087 -0.3809 105 LYS   N N   
23915 C  CA  . LYS   N  105 ? 2.2838 0.9955 1.6666 -0.0072 -0.0550 -0.3187 105 LYS   N CA  
23916 C  C   . LYS   N  105 ? 2.3112 0.9563 1.6420 -0.0594 -0.0258 -0.1764 105 LYS   N C   
23917 O  O   . LYS   N  105 ? 2.4782 1.2110 1.5842 -0.0613 0.0815  -0.1310 105 LYS   N O   
23918 C  CB  . LYS   N  105 ? 2.3800 1.0219 1.7353 -0.0221 -0.0832 -0.2673 105 LYS   N CB  
23919 C  CG  . LYS   N  105 ? 2.3892 1.1205 1.8605 -0.0526 -0.0499 -0.2876 105 LYS   N CG  
23920 C  CD  . LYS   N  105 ? 2.3861 1.1172 1.9920 -0.0142 -0.0467 -0.2819 105 LYS   N CD  
23921 C  CE  . LYS   N  105 ? 2.3984 1.1796 2.1208 0.0630  -0.0301 -0.3523 105 LYS   N CE  
23922 N  NZ  . LYS   N  105 ? 2.4064 1.0990 2.1108 0.1125  -0.0632 -0.3775 105 LYS   N NZ  
23923 N  N   . ASN   N  106 ? 2.2150 1.0553 1.6111 0.0062  -0.0366 -0.1068 106 ASN   N N   
23924 C  CA  . ASN   N  106 ? 2.1098 0.9750 1.6142 0.0326  -0.0469 -0.0275 106 ASN   N CA  
23925 C  C   . ASN   N  106 ? 2.0252 0.9223 1.6005 -0.0272 -0.0898 -0.0666 106 ASN   N C   
23926 O  O   . ASN   N  106 ? 1.9674 0.8393 1.6324 -0.0631 -0.0130 0.1052  106 ASN   N O   
23927 C  CB  . ASN   N  106 ? 2.0709 0.9050 1.6212 0.0323  -0.0440 0.0632  106 ASN   N CB  
23928 C  CG  . ASN   N  106 ? 2.0757 0.8278 1.6056 -0.0539 -0.0120 0.2123  106 ASN   N CG  
23929 O  OD1 . ASN   N  106 ? 2.0853 0.6501 1.6289 -0.1250 -0.0642 0.3098  106 ASN   N OD1 
23930 N  ND2 . ASN   N  106 ? 2.1242 0.9438 1.6158 -0.0718 0.0338  0.2971  106 ASN   N ND2 
23931 N  N   . LYS   N  107 ? 2.0705 1.0815 1.5856 -0.0673 -0.1113 -0.1311 107 LYS   N N   
23932 C  CA  . LYS   N  107 ? 1.9859 1.0944 1.5274 -0.1044 -0.1565 -0.2136 107 LYS   N CA  
23933 C  C   . LYS   N  107 ? 1.9155 0.9127 1.5452 -0.0945 -0.2101 -0.2139 107 LYS   N C   
23934 O  O   . LYS   N  107 ? 1.8372 0.6901 1.6088 -0.1550 -0.1686 -0.2661 107 LYS   N O   
23935 C  CB  . LYS   N  107 ? 2.0043 1.2437 1.5604 -0.2020 -0.1118 -0.2153 107 LYS   N CB  
23936 C  CG  . LYS   N  107 ? 2.0209 1.4131 1.5773 -0.2588 -0.0870 -0.2741 107 LYS   N CG  
23937 C  CD  . LYS   N  107 ? 2.0980 1.5403 1.5747 -0.2762 -0.1235 -0.3208 107 LYS   N CD  
23938 C  CE  . LYS   N  107 ? 2.1339 1.5957 1.6205 -0.2511 -0.1120 -0.3598 107 LYS   N CE  
23939 N  NZ  . LYS   N  107 ? 2.1715 1.6309 1.7033 -0.2786 -0.1542 -0.3572 107 LYS   N NZ  
23940 N  N   . GLY   N  108 ? 1.8588 0.9230 1.4540 -0.0533 -0.2304 -0.2245 108 GLY   N N   
23941 C  CA  . GLY   N  108 ? 1.8355 0.8433 1.4398 -0.0391 -0.2302 -0.1835 108 GLY   N CA  
23942 C  C   . GLY   N  108 ? 1.8308 0.7541 1.3446 0.0026  -0.1947 -0.1718 108 GLY   N C   
23943 O  O   . GLY   N  108 ? 1.8698 0.7282 1.4114 -0.0189 -0.1511 -0.1682 108 GLY   N O   
23944 N  N   . GLU   N  109 ? 1.7796 0.7222 1.3297 0.0307  -0.2055 -0.1490 109 GLU   N N   
23945 C  CA  . GLU   N  109 ? 1.7775 0.8190 1.2701 0.0495  -0.1925 -0.0890 109 GLU   N CA  
23946 C  C   . GLU   N  109 ? 1.7414 0.7638 1.2019 0.0980  -0.2337 -0.0181 109 GLU   N C   
23947 O  O   . GLU   N  109 ? 1.7415 0.6812 1.1155 0.1106  -0.2703 0.0536  109 GLU   N O   
23948 C  CB  . GLU   N  109 ? 1.8001 0.8226 1.3284 0.0384  -0.1817 -0.0603 109 GLU   N CB  
23949 C  CG  . GLU   N  109 ? 1.8297 1.0167 1.4407 -0.0191 -0.1102 -0.1148 109 GLU   N CG  
23950 C  CD  . GLU   N  109 ? 1.8541 1.0788 1.5887 0.0250  -0.1056 -0.1061 109 GLU   N CD  
23951 O  OE1 . GLU   N  109 ? 1.9470 1.3959 1.5502 -0.0908 0.0049  -0.1774 109 GLU   N OE1 
23952 O  OE2 . GLU   N  109 ? 1.8441 1.3018 1.7835 -0.0934 0.0066  -0.1864 109 GLU   N OE2 
23953 N  N   . VAL   N  110 ? 1.7195 0.6978 1.1768 0.1468  -0.2503 0.0024  110 VAL   N N   
23954 C  CA  . VAL   N  110 ? 1.6886 0.5936 1.2012 0.1210  -0.2640 0.0051  110 VAL   N CA  
23955 C  C   . VAL   N  110 ? 1.6565 0.4433 1.2000 0.1479  -0.2401 0.0245  110 VAL   N C   
23956 O  O   . VAL   N  110 ? 1.6535 0.4006 1.3796 0.2086  -0.1751 -0.0106 110 VAL   N O   
23957 C  CB  . VAL   N  110 ? 1.6929 0.6377 1.1357 0.0937  -0.3289 0.0901  110 VAL   N CB  
23958 C  CG1 . VAL   N  110 ? 1.6576 0.6313 1.1487 0.0916  -0.3390 0.0776  110 VAL   N CG1 
23959 C  CG2 . VAL   N  110 ? 1.7348 0.7164 1.1211 0.0799  -0.3482 0.1175  110 VAL   N CG2 
23960 N  N   . TYR   N  111 ? 1.6638 0.3820 1.1867 0.1534  -0.2462 0.0251  111 TYR   N N   
23961 C  CA  . TYR   N  111 ? 1.6619 0.4653 1.1909 0.1277  -0.2465 0.0069  111 TYR   N CA  
23962 C  C   . TYR   N  111 ? 1.6432 0.4010 1.1727 0.0781  -0.2238 0.0405  111 TYR   N C   
23963 O  O   . TYR   N  111 ? 1.6556 0.5663 1.2176 0.0634  -0.2010 0.1051  111 TYR   N O   
23964 C  CB  . TYR   N  111 ? 1.6634 0.4579 1.1687 0.1574  -0.2696 -0.0266 111 TYR   N CB  
23965 C  CG  . TYR   N  111 ? 1.6534 0.4620 1.1559 0.1405  -0.2875 -0.0525 111 TYR   N CG  
23966 C  CD1 . TYR   N  111 ? 1.6821 0.4276 1.1590 0.1431  -0.2819 -0.0621 111 TYR   N CD1 
23967 C  CD2 . TYR   N  111 ? 1.6404 0.4549 1.1535 0.1256  -0.2604 -0.0503 111 TYR   N CD2 
23968 C  CE1 . TYR   N  111 ? 1.6778 0.4595 1.1585 0.1322  -0.2520 -0.0575 111 TYR   N CE1 
23969 C  CE2 . TYR   N  111 ? 1.6365 0.4556 1.1384 0.0978  -0.2321 -0.0413 111 TYR   N CE2 
23970 C  CZ  . TYR   N  111 ? 1.6687 0.4772 1.1358 0.0982  -0.2376 -0.0500 111 TYR   N CZ  
23971 O  OH  . TYR   N  111 ? 1.6823 0.5760 1.1512 0.1412  -0.1825 -0.0294 111 TYR   N OH  
23972 N  N   . THR   N  112 ? 1.6292 0.3604 1.1545 0.0680  -0.1805 0.0537  112 THR   N N   
23973 C  CA  . THR   N  112 ? 1.5947 0.4704 1.1413 0.0537  -0.2164 -0.0180 112 THR   N CA  
23974 C  C   . THR   N  112 ? 1.5850 0.2882 1.0926 0.0167  -0.1792 -0.0445 112 THR   N C   
23975 O  O   . THR   N  112 ? 1.5983 0.1598 1.1021 0.0432  -0.1740 -0.0777 112 THR   N O   
23976 C  CB  . THR   N  112 ? 1.5631 0.4657 1.2163 0.0887  -0.2180 -0.0363 112 THR   N CB  
23977 O  OG1 . THR   N  112 ? 1.5178 0.6581 1.2295 0.1513  -0.2309 -0.0571 112 THR   N OG1 
23978 C  CG2 . THR   N  112 ? 1.5523 0.5573 1.2510 0.0849  -0.2352 -0.0712 112 THR   N CG2 
23979 N  N   . ILE   N  113 ? 1.6387 0.3215 1.0329 -0.0113 -0.1944 -0.0321 113 ILE   N N   
23980 C  CA  . ILE   N  113 ? 1.6868 0.4547 1.0439 0.0064  -0.1927 0.0165  113 ILE   N CA  
23981 C  C   . ILE   N  113 ? 1.7135 0.4654 0.9889 0.0065  -0.1715 0.0487  113 ILE   N C   
23982 O  O   . ILE   N  113 ? 1.7253 0.3846 0.9436 -0.0147 -0.1594 0.1177  113 ILE   N O   
23983 C  CB  . ILE   N  113 ? 1.7030 0.4540 1.0101 -0.0004 -0.1747 -0.0190 113 ILE   N CB  
23984 C  CG1 . ILE   N  113 ? 1.7192 0.4815 1.0029 0.0030  -0.1773 -0.0347 113 ILE   N CG1 
23985 C  CG2 . ILE   N  113 ? 1.6834 0.5240 1.0122 0.0183  -0.1647 -0.0034 113 ILE   N CG2 
23986 C  CD1 . ILE   N  113 ? 1.6937 0.4652 1.0138 0.0213  -0.1644 -0.0539 113 ILE   N CD1 
23987 N  N   . PRO   N  114 ? 1.7128 0.5930 0.9632 -0.0625 -0.1822 0.0750  114 PRO   N N   
23988 C  CA  . PRO   N  114 ? 1.7453 0.6286 0.9687 -0.0888 -0.1449 0.0542  114 PRO   N CA  
23989 C  C   . PRO   N  114 ? 1.7951 0.6480 0.9677 -0.0895 -0.1056 0.0350  114 PRO   N C   
23990 O  O   . PRO   N  114 ? 1.7876 0.6646 1.0008 -0.0119 -0.0858 0.1038  114 PRO   N O   
23991 C  CB  . PRO   N  114 ? 1.7684 0.6442 0.9582 -0.1035 -0.1367 0.1079  114 PRO   N CB  
23992 C  CG  . PRO   N  114 ? 1.7469 0.6040 0.9646 -0.0778 -0.1550 0.1198  114 PRO   N CG  
23993 C  CD  . PRO   N  114 ? 1.7217 0.6005 0.9631 -0.0652 -0.1718 0.1071  114 PRO   N CD  
23994 N  N   . LEU   N  115 ? 1.8023 0.6105 1.0451 -0.1491 -0.1292 -0.0053 115 LEU   N N   
23995 C  CA  . LEU   N  115 ? 1.7371 0.5960 1.0027 -0.1384 -0.2020 -0.0293 115 LEU   N CA  
23996 C  C   . LEU   N  115 ? 1.6652 0.7091 1.0231 -0.0902 -0.2757 -0.1608 115 LEU   N C   
23997 O  O   . LEU   N  115 ? 1.6178 0.9374 1.0010 -0.1230 -0.2177 -0.0963 115 LEU   N O   
23998 C  CB  . LEU   N  115 ? 1.7591 0.6269 1.0077 -0.1909 -0.2083 -0.0547 115 LEU   N CB  
23999 C  CG  . LEU   N  115 ? 1.7743 0.7386 1.0652 -0.2037 -0.1683 -0.0448 115 LEU   N CG  
24000 C  CD1 . LEU   N  115 ? 1.7762 0.7586 1.0965 -0.2687 -0.1772 -0.0753 115 LEU   N CD1 
24001 C  CD2 . LEU   N  115 ? 1.8375 0.7641 1.0567 -0.2077 -0.1752 -0.0669 115 LEU   N CD2 
24002 N  N   . GLY   N  116 ? 1.6512 0.4666 1.0046 -0.1047 -0.3218 -0.1900 116 GLY   N N   
24003 C  CA  . GLY   N  116 ? 1.6655 0.5790 1.0783 -0.0475 -0.3017 -0.1698 116 GLY   N CA  
24004 C  C   . GLY   N  116 ? 1.6653 0.5114 1.0477 -0.0100 -0.3056 -0.0231 116 GLY   N C   
24005 O  O   . GLY   N  116 ? 1.7117 0.3726 1.0683 -0.0973 -0.2222 0.0473  116 GLY   N O   
24006 N  N   . GLY   N  117 ? 1.6480 0.4996 1.1019 -0.0527 -0.2864 -0.1071 117 GLY   N N   
24007 C  CA  . GLY   N  117 ? 1.5866 0.4381 1.1442 -0.0341 -0.2527 -0.0405 117 GLY   N CA  
24008 C  C   . GLY   N  117 ? 1.5627 0.4809 1.1886 -0.0103 -0.2471 -0.0146 117 GLY   N C   
24009 O  O   . GLY   N  117 ? 1.4811 0.5304 1.2220 0.0477  -0.2538 -0.0276 117 GLY   N O   
24010 N  N   . SER   N  118 ? 1.5558 0.4151 1.1854 0.0187  -0.2283 -0.0581 118 SER   N N   
24011 C  CA  . SER   N  118 ? 1.5668 0.4072 1.2320 0.0344  -0.2013 -0.0315 118 SER   N CA  
24012 C  C   . SER   N  118 ? 1.5840 0.4240 1.2105 0.0651  -0.1810 -0.0343 118 SER   N C   
24013 O  O   . SER   N  118 ? 1.5630 0.5243 1.2930 0.0506  -0.1344 -0.0352 118 SER   N O   
24014 C  CB  . SER   N  118 ? 1.5327 0.4406 1.2752 0.0215  -0.2299 -0.0245 118 SER   N CB  
24015 O  OG  . SER   N  118 ? 1.5986 0.3017 1.3569 -0.0504 -0.2296 0.0443  118 SER   N OG  
24016 N  N   . VAL   N  119 ? 1.6234 0.4037 1.1070 0.0819  -0.2191 -0.0010 119 VAL   N N   
24017 C  CA  . VAL   N  119 ? 1.6116 0.3736 1.0830 0.1048  -0.2048 -0.0257 119 VAL   N CA  
24018 C  C   . VAL   N  119 ? 1.5475 0.4788 1.0633 0.0982  -0.2208 -0.0152 119 VAL   N C   
24019 O  O   . VAL   N  119 ? 1.5346 0.5686 1.0847 0.0673  -0.2177 -0.0305 119 VAL   N O   
24020 C  CB  . VAL   N  119 ? 1.6025 0.3901 1.0060 0.0796  -0.2010 -0.0563 119 VAL   N CB  
24021 C  CG1 . VAL   N  119 ? 1.5588 0.3738 1.0274 0.1167  -0.2031 -0.0149 119 VAL   N CG1 
24022 C  CG2 . VAL   N  119 ? 1.6267 0.4368 0.9524 0.0567  -0.1983 -0.0791 119 VAL   N CG2 
24023 N  N   . HIS   N  120 ? 1.6183 0.4270 1.0967 0.1205  -0.2221 0.0108  120 HIS   N N   
24024 C  CA  . HIS   N  120 ? 1.6502 0.3902 1.1461 0.1325  -0.2121 0.0317  120 HIS   N CA  
24025 C  C   . HIS   N  120 ? 1.6327 0.3478 1.1599 0.1262  -0.2022 0.0173  120 HIS   N C   
24026 O  O   . HIS   N  120 ? 1.6250 0.3266 1.2476 0.1101  -0.2160 0.0298  120 HIS   N O   
24027 C  CB  . HIS   N  120 ? 1.7132 0.4370 1.1568 0.1801  -0.2346 -0.0557 120 HIS   N CB  
24028 C  CG  . HIS   N  120 ? 1.7714 0.5278 1.1634 0.1977  -0.2702 -0.0573 120 HIS   N CG  
24029 N  ND1 . HIS   N  120 ? 1.7684 0.5602 1.2024 0.2040  -0.2465 -0.0755 120 HIS   N ND1 
24030 C  CD2 . HIS   N  120 ? 1.7816 0.5653 1.1748 0.1980  -0.2619 -0.0376 120 HIS   N CD2 
24031 C  CE1 . HIS   N  120 ? 1.8121 0.5877 1.2057 0.2010  -0.2748 -0.0397 120 HIS   N CE1 
24032 N  NE2 . HIS   N  120 ? 1.8137 0.5862 1.1949 0.1957  -0.2805 -0.0300 120 HIS   N NE2 
24033 N  N   . LYS   N  121 ? 1.6342 0.3722 1.1333 0.1223  -0.1841 0.0461  121 LYS   N N   
24034 C  CA  . LYS   N  121 ? 1.6171 0.5538 1.1330 0.0685  -0.1982 0.0583  121 LYS   N CA  
24035 C  C   . LYS   N  121 ? 1.5733 0.5714 1.1143 0.0584  -0.2053 0.0594  121 LYS   N C   
24036 O  O   . LYS   N  121 ? 1.5714 0.6628 1.2361 0.0576  -0.1424 0.0495  121 LYS   N O   
24037 C  CB  . LYS   N  121 ? 1.6302 0.5467 1.0894 0.0641  -0.1978 0.0755  121 LYS   N CB  
24038 C  CG  . LYS   N  121 ? 1.6676 0.6276 1.0856 0.0187  -0.2112 0.0919  121 LYS   N CG  
24039 C  CD  . LYS   N  121 ? 1.6920 0.6332 1.0756 0.0149  -0.1879 0.1000  121 LYS   N CD  
24040 C  CE  . LYS   N  121 ? 1.7456 0.6674 1.0781 -0.0221 -0.1818 0.0857  121 LYS   N CE  
24041 N  NZ  . LYS   N  121 ? 1.8106 0.7243 1.1203 -0.0237 -0.1801 0.1301  121 LYS   N NZ  
24042 N  N   . LEU   N  122 ? 1.5536 0.6102 1.0349 -0.0044 -0.2441 0.0468  122 LEU   N N   
24043 C  CA  . LEU   N  122 ? 1.5949 0.6488 0.9597 -0.0191 -0.2593 0.0490  122 LEU   N CA  
24044 C  C   . LEU   N  122 ? 1.6279 0.6867 0.9308 -0.0588 -0.2345 0.0112  122 LEU   N C   
24045 O  O   . LEU   N  122 ? 1.6478 0.7908 0.8135 -0.1204 -0.2355 0.0117  122 LEU   N O   
24046 C  CB  . LEU   N  122 ? 1.5910 0.6875 0.9643 0.0042  -0.2834 0.0317  122 LEU   N CB  
24047 C  CG  . LEU   N  122 ? 1.5935 0.6745 0.9487 0.0144  -0.2831 0.0576  122 LEU   N CG  
24048 C  CD1 . LEU   N  122 ? 1.5546 0.7019 0.8991 0.0186  -0.2931 0.0705  122 LEU   N CD1 
24049 C  CD2 . LEU   N  122 ? 1.5954 0.6825 0.9740 0.0083  -0.2906 0.0447  122 LEU   N CD2 
24050 N  N   . PRO   N  123 ? 1.6220 0.6072 0.9404 -0.0323 -0.2496 -0.0009 123 PRO   N N   
24051 C  CA  . PRO   N  123 ? 1.6910 0.5456 0.9447 -0.0003 -0.2672 0.0314  123 PRO   N CA  
24052 C  C   . PRO   N  123 ? 1.7150 0.4245 0.9293 0.0059  -0.2474 0.0683  123 PRO   N C   
24053 O  O   . PRO   N  123 ? 1.7370 0.2209 0.9500 -0.0392 -0.2369 0.1115  123 PRO   N O   
24054 C  CB  . PRO   N  123 ? 1.6353 0.5591 0.9694 -0.0127 -0.2576 0.0105  123 PRO   N CB  
24055 C  CG  . PRO   N  123 ? 1.6241 0.5717 0.9804 -0.0204 -0.2475 0.0063  123 PRO   N CG  
24056 C  CD  . PRO   N  123 ? 1.6062 0.5817 0.9740 -0.0127 -0.2418 0.0038  123 PRO   N CD  
24057 N  N   . TYR   N  124 ? 1.7944 0.4792 0.8801 0.0365  -0.2525 0.0803  124 TYR   N N   
24058 C  CA  . TYR   N  124 ? 1.7875 0.5509 0.9106 0.0335  -0.2587 0.1041  124 TYR   N CA  
24059 C  C   . TYR   N  124 ? 1.8033 0.4597 0.9063 0.0138  -0.2522 0.1203  124 TYR   N C   
24060 O  O   . TYR   N  124 ? 1.8336 0.4240 0.9132 -0.0027 -0.2650 0.1074  124 TYR   N O   
24061 C  CB  . TYR   N  124 ? 1.8102 0.5733 0.9658 0.0766  -0.3096 0.0770  124 TYR   N CB  
24062 C  CG  . TYR   N  124 ? 1.8132 0.5620 0.9936 0.1175  -0.3115 -0.0048 124 TYR   N CG  
24063 C  CD1 . TYR   N  124 ? 1.8190 0.5393 1.0281 0.1028  -0.3008 -0.0244 124 TYR   N CD1 
24064 C  CD2 . TYR   N  124 ? 1.7889 0.5741 1.0237 0.1283  -0.3119 -0.0100 124 TYR   N CD2 
24065 C  CE1 . TYR   N  124 ? 1.8016 0.5448 1.0773 0.1003  -0.2854 -0.0299 124 TYR   N CE1 
24066 C  CE2 . TYR   N  124 ? 1.7932 0.5696 1.1206 0.1222  -0.2809 -0.0139 124 TYR   N CE2 
24067 C  CZ  . TYR   N  124 ? 1.7933 0.5489 1.1294 0.1064  -0.2881 -0.0468 124 TYR   N CZ  
24068 O  OH  . TYR   N  124 ? 1.8462 0.6031 1.1045 0.0838  -0.3016 -0.1630 124 TYR   N OH  
24069 N  N   . ALA   N  125 ? 1.8017 0.3799 0.9059 0.0293  -0.2462 0.0903  125 ALA   N N   
24070 C  CA  . ALA   N  125 ? 1.8174 0.3870 0.9221 0.0324  -0.2492 0.0601  125 ALA   N CA  
24071 C  C   . ALA   N  125 ? 1.8284 0.3832 0.9421 0.0631  -0.2921 0.1051  125 ALA   N C   
24072 O  O   . ALA   N  125 ? 1.8646 0.3293 0.9708 0.0575  -0.3439 0.1267  125 ALA   N O   
24073 C  CB  . ALA   N  125 ? 1.8147 0.3850 0.8845 0.0119  -0.2354 0.0473  125 ALA   N CB  
24074 N  N   . ILE   N  126 ? 1.8766 0.4316 0.9188 0.0905  -0.2864 0.0788  126 ILE   N N   
24075 C  CA  . ILE   N  126 ? 1.8461 0.4457 0.9689 0.0838  -0.3157 0.0397  126 ILE   N CA  
24076 C  C   . ILE   N  126 ? 1.7795 0.3898 0.9708 0.0425  -0.3226 -0.0261 126 ILE   N C   
24077 O  O   . ILE   N  126 ? 1.8369 0.2898 1.0011 0.0147  -0.3997 -0.1131 126 ILE   N O   
24078 C  CB  . ILE   N  126 ? 1.8477 0.5038 0.9434 0.0890  -0.3538 0.1119  126 ILE   N CB  
24079 C  CG1 . ILE   N  126 ? 1.8510 0.5418 0.9784 0.0796  -0.3735 0.1427  126 ILE   N CG1 
24080 C  CG2 . ILE   N  126 ? 1.8591 0.5145 0.9351 0.1195  -0.3398 0.1267  126 ILE   N CG2 
24081 C  CD1 . ILE   N  126 ? 1.8484 0.5408 0.9824 0.1262  -0.3676 0.1873  126 ILE   N CD1 
24082 N  N   . ALA   N  127 ? 1.7631 0.3967 1.0320 0.0273  -0.3046 -0.0692 127 ALA   N N   
24083 C  CA  . ALA   N  127 ? 1.7333 0.4243 1.0242 -0.0189 -0.3004 -0.1352 127 ALA   N CA  
24084 C  C   . ALA   N  127 ? 1.7104 0.4703 1.0904 -0.0372 -0.3045 -0.1575 127 ALA   N C   
24085 O  O   . ALA   N  127 ? 1.7535 0.5968 1.0333 -0.0704 -0.3246 -0.1759 127 ALA   N O   
24086 C  CB  . ALA   N  127 ? 1.7505 0.4260 1.0500 0.0284  -0.2794 -0.1555 127 ALA   N CB  
24087 N  N   . GLY   N  128 ? 1.6592 0.4715 1.1132 -0.0381 -0.2456 -0.1792 128 GLY   N N   
24088 C  CA  . GLY   N  128 ? 1.6244 0.5346 1.1170 -0.0141 -0.2511 -0.1177 128 GLY   N CA  
24089 C  C   . GLY   N  128 ? 1.5771 0.5092 1.0809 0.0220  -0.2605 -0.0564 128 GLY   N C   
24090 O  O   . GLY   N  128 ? 1.6501 0.3990 1.0636 0.0291  -0.2528 0.0286  128 GLY   N O   
24091 N  N   . SER   N  129 ? 1.5317 0.4915 1.0373 0.0300  -0.2745 -0.0008 129 SER   N N   
24092 C  CA  . SER   N  129 ? 1.5457 0.5056 1.0622 -0.0047 -0.2213 -0.0294 129 SER   N CA  
24093 C  C   . SER   N  129 ? 1.5756 0.5424 1.0323 -0.0243 -0.2049 -0.0482 129 SER   N C   
24094 O  O   . SER   N  129 ? 1.5994 0.6024 1.1377 -0.0752 -0.1618 -0.0331 129 SER   N O   
24095 C  CB  . SER   N  129 ? 1.5787 0.4718 1.0335 -0.0493 -0.1862 0.0068  129 SER   N CB  
24096 O  OG  . SER   N  129 ? 1.6000 0.4527 1.0608 -0.1018 -0.1653 0.0393  129 SER   N OG  
24097 N  N   . GLY   N  130 ? 1.6020 0.5491 0.9853 0.0228  -0.1998 -0.0567 130 GLY   N N   
24098 C  CA  . GLY   N  130 ? 1.5829 0.4983 0.9789 0.0592  -0.2283 -0.0745 130 GLY   N CA  
24099 C  C   . GLY   N  130 ? 1.5955 0.5215 0.9392 0.0632  -0.2313 -0.0599 130 GLY   N C   
24100 O  O   . GLY   N  130 ? 1.5722 0.4853 0.9534 0.1019  -0.2100 -0.0784 130 GLY   N O   
24101 N  N   . SER   N  131 ? 1.5752 0.5919 0.9514 0.0975  -0.2468 -0.0251 131 SER   N N   
24102 C  CA  . SER   N  131 ? 1.6019 0.6123 0.9778 0.0842  -0.2170 -0.0092 131 SER   N CA  
24103 C  C   . SER   N  131 ? 1.6457 0.5157 0.9829 0.1341  -0.2387 0.0002  131 SER   N C   
24104 O  O   . SER   N  131 ? 1.6272 0.4263 0.8949 0.1258  -0.2618 -0.1133 131 SER   N O   
24105 C  CB  . SER   N  131 ? 1.6517 0.5960 1.0299 0.0950  -0.2001 -0.0085 131 SER   N CB  
24106 O  OG  . SER   N  131 ? 1.7219 0.6032 1.0322 0.0349  -0.1700 -0.0767 131 SER   N OG  
24107 N  N   . THR   N  132 ? 1.6746 0.4929 0.9663 0.1481  -0.2195 0.0238  132 THR   N N   
24108 C  CA  . THR   N  132 ? 1.6771 0.5561 1.0755 0.0992  -0.2023 0.0714  132 THR   N CA  
24109 C  C   . THR   N  132 ? 1.6810 0.5240 1.1444 0.0407  -0.2050 0.1000  132 THR   N C   
24110 O  O   . THR   N  132 ? 1.7655 0.4650 1.2627 0.0086  -0.1710 0.1492  132 THR   N O   
24111 C  CB  . THR   N  132 ? 1.7060 0.6640 1.0821 0.1502  -0.2127 0.0449  132 THR   N CB  
24112 O  OG1 . THR   N  132 ? 1.7175 0.7678 1.2319 0.1796  -0.2099 0.0314  132 THR   N OG1 
24113 C  CG2 . THR   N  132 ? 1.6987 0.6915 1.0547 0.1820  -0.2350 0.0199  132 THR   N CG2 
24114 N  N   . PHE   N  133 ? 1.7052 0.4286 1.0922 0.0152  -0.2499 0.1077  133 PHE   N N   
24115 C  CA  . PHE   N  133 ? 1.7234 0.3749 1.1075 0.0168  -0.2712 0.0714  133 PHE   N CA  
24116 C  C   . PHE   N  133 ? 1.7096 0.3825 1.1021 0.0286  -0.3246 0.0358  133 PHE   N C   
24117 O  O   . PHE   N  133 ? 1.6651 0.1643 1.1780 0.0757  -0.4398 -0.0676 133 PHE   N O   
24118 C  CB  . PHE   N  133 ? 1.7366 0.3494 1.0981 0.0007  -0.2287 0.0865  133 PHE   N CB  
24119 C  CG  . PHE   N  133 ? 1.7774 0.3543 1.0934 -0.0133 -0.1985 0.1301  133 PHE   N CG  
24120 C  CD1 . PHE   N  133 ? 1.7731 0.3782 1.1093 -0.0239 -0.2045 0.1246  133 PHE   N CD1 
24121 C  CD2 . PHE   N  133 ? 1.8102 0.2817 1.1113 -0.0348 -0.2240 0.1212  133 PHE   N CD2 
24122 C  CE1 . PHE   N  133 ? 1.7975 0.3884 1.1105 -0.0227 -0.2031 0.1234  133 PHE   N CE1 
24123 C  CE2 . PHE   N  133 ? 1.8142 0.3403 1.1372 -0.0226 -0.1968 0.1017  133 PHE   N CE2 
24124 C  CZ  . PHE   N  133 ? 1.8046 0.3736 1.1209 -0.0366 -0.2083 0.1051  133 PHE   N CZ  
24125 N  N   . ILE   N  134 ? 1.6897 0.3671 1.0551 0.0229  -0.3208 0.0649  134 ILE   N N   
24126 C  CA  . ILE   N  134 ? 1.7024 0.3838 1.0512 0.0223  -0.3163 0.0742  134 ILE   N CA  
24127 C  C   . ILE   N  134 ? 1.7018 0.3060 1.0652 0.0106  -0.3194 0.1074  134 ILE   N C   
24128 O  O   . ILE   N  134 ? 1.7593 0.3541 1.0366 0.0154  -0.2905 0.1495  134 ILE   N O   
24129 C  CB  . ILE   N  134 ? 1.6655 0.4651 1.0429 0.0101  -0.3370 0.0873  134 ILE   N CB  
24130 C  CG1 . ILE   N  134 ? 1.6575 0.5265 1.0254 -0.0328 -0.3044 0.1146  134 ILE   N CG1 
24131 C  CG2 . ILE   N  134 ? 1.6442 0.4898 1.0295 -0.0035 -0.3524 0.0621  134 ILE   N CG2 
24132 C  CD1 . ILE   N  134 ? 1.6536 0.6097 1.0348 -0.0613 -0.3023 0.0695  134 ILE   N CD1 
24133 N  N   . TYR   N  135 ? 1.6944 0.2479 1.0344 -0.0237 -0.2958 0.0632  135 TYR   N N   
24134 C  CA  . TYR   N  135 ? 1.7002 0.3291 1.0240 -0.0315 -0.2571 0.0518  135 TYR   N CA  
24135 C  C   . TYR   N  135 ? 1.7054 0.3540 1.0126 -0.0354 -0.2578 0.0530  135 TYR   N C   
24136 O  O   . TYR   N  135 ? 1.6989 0.3084 0.9541 -0.0011 -0.2559 0.1360  135 TYR   N O   
24137 C  CB  . TYR   N  135 ? 1.7283 0.3662 1.0101 -0.0300 -0.2478 0.0266  135 TYR   N CB  
24138 C  CG  . TYR   N  135 ? 1.7525 0.4019 1.0175 0.0012  -0.2317 0.0508  135 TYR   N CG  
24139 C  CD1 . TYR   N  135 ? 1.7500 0.4419 1.0127 0.0229  -0.2110 0.0350  135 TYR   N CD1 
24140 C  CD2 . TYR   N  135 ? 1.7575 0.4662 1.0664 0.0135  -0.2102 0.0437  135 TYR   N CD2 
24141 C  CE1 . TYR   N  135 ? 1.7519 0.4625 1.0422 0.0584  -0.2304 0.0601  135 TYR   N CE1 
24142 C  CE2 . TYR   N  135 ? 1.7539 0.4801 1.0901 0.0449  -0.2101 0.0638  135 TYR   N CE2 
24143 C  CZ  . TYR   N  135 ? 1.7587 0.4940 1.0495 0.0648  -0.2302 0.1025  135 TYR   N CZ  
24144 O  OH  . TYR   N  135 ? 1.7518 0.5425 1.0926 0.1147  -0.2949 0.1614  135 TYR   N OH  
24145 N  N   . GLY   N  136 ? 1.7258 0.3515 1.0188 -0.0660 -0.2501 0.0252  136 GLY   N N   
24146 C  CA  . GLY   N  136 ? 1.7446 0.3510 1.0524 -0.0545 -0.2406 0.0452  136 GLY   N CA  
24147 C  C   . GLY   N  136 ? 1.7256 0.3426 1.0628 -0.0487 -0.2365 0.0321  136 GLY   N C   
24148 O  O   . GLY   N  136 ? 1.7663 0.2949 1.0856 -0.0044 -0.2097 0.0540  136 GLY   N O   
24149 N  N   . TYR   N  137 ? 1.7246 0.4251 1.1175 -0.0727 -0.2181 0.0271  137 TYR   N N   
24150 C  CA  . TYR   N  137 ? 1.7804 0.5480 1.0951 -0.0684 -0.2108 -0.0046 137 TYR   N CA  
24151 C  C   . TYR   N  137 ? 1.7763 0.5885 1.0739 -0.0622 -0.2162 -0.0385 137 TYR   N C   
24152 O  O   . TYR   N  137 ? 1.8031 0.6784 1.0738 -0.1087 -0.2153 -0.0407 137 TYR   N O   
24153 C  CB  . TYR   N  137 ? 1.7847 0.5843 1.1062 -0.0710 -0.2098 -0.0230 137 TYR   N CB  
24154 C  CG  . TYR   N  137 ? 1.8257 0.6470 1.1093 -0.0613 -0.2278 -0.0230 137 TYR   N CG  
24155 C  CD1 . TYR   N  137 ? 1.8492 0.6351 1.1444 -0.0521 -0.2196 -0.0126 137 TYR   N CD1 
24156 C  CD2 . TYR   N  137 ? 1.8629 0.6754 1.1375 -0.0659 -0.2167 -0.0794 137 TYR   N CD2 
24157 C  CE1 . TYR   N  137 ? 1.8759 0.7271 1.1308 -0.0368 -0.2200 -0.0312 137 TYR   N CE1 
24158 C  CE2 . TYR   N  137 ? 1.8914 0.7536 1.0975 -0.0042 -0.2284 -0.0549 137 TYR   N CE2 
24159 C  CZ  . TYR   N  137 ? 1.8854 0.7460 1.0737 -0.0388 -0.2377 -0.0542 137 TYR   N CZ  
24160 O  OH  . TYR   N  137 ? 1.9362 0.9668 1.0762 -0.0349 -0.2399 -0.1202 137 TYR   N OH  
24161 N  N   . CYS   N  138 ? 1.7566 0.5810 1.0373 -0.0461 -0.2041 -0.0593 138 CYS   N N   
24162 C  CA  . CYS   N  138 ? 1.7310 0.5982 1.0034 -0.0262 -0.1919 -0.0748 138 CYS   N CA  
24163 C  C   . CYS   N  138 ? 1.7269 0.5717 1.0320 0.0171  -0.2048 -0.0946 138 CYS   N C   
24164 O  O   . CYS   N  138 ? 1.7566 0.6122 0.9813 0.0302  -0.1970 -0.0613 138 CYS   N O   
24165 C  CB  . CYS   N  138 ? 1.7128 0.5952 0.9852 -0.0331 -0.1789 -0.0872 138 CYS   N CB  
24166 S  SG  . CYS   N  138 ? 1.7560 0.6514 0.9386 -0.0746 -0.1231 -0.0649 138 CYS   N SG  
24167 N  N   . ASP   N  139 ? 1.7126 0.5378 1.0419 0.0640  -0.2125 -0.1265 139 ASP   N N   
24168 C  CA  . ASP   N  139 ? 1.7283 0.5620 1.0336 0.0922  -0.1981 -0.1106 139 ASP   N CA  
24169 C  C   . ASP   N  139 ? 1.7641 0.5936 0.9764 0.0724  -0.2180 -0.1470 139 ASP   N C   
24170 O  O   . ASP   N  139 ? 1.7697 0.6724 0.8137 0.0785  -0.2602 -0.1065 139 ASP   N O   
24171 C  CB  . ASP   N  139 ? 1.7034 0.5115 1.1078 0.1112  -0.2141 -0.1202 139 ASP   N CB  
24172 C  CG  . ASP   N  139 ? 1.7070 0.5359 1.1986 0.1348  -0.2052 -0.0940 139 ASP   N CG  
24173 O  OD1 . ASP   N  139 ? 1.6838 0.6241 1.2299 0.2171  -0.2211 -0.1273 139 ASP   N OD1 
24174 O  OD2 . ASP   N  139 ? 1.7379 0.4790 1.2989 0.1816  -0.1796 -0.0657 139 ASP   N OD2 
24175 N  N   . LYS   N  140 ? 1.7734 0.5898 0.9696 0.0619  -0.2112 -0.1179 140 LYS   N N   
24176 C  CA  . LYS   N  140 ? 1.8261 0.6993 1.0088 0.0249  -0.1636 -0.0602 140 LYS   N CA  
24177 C  C   . LYS   N  140 ? 1.8619 0.6954 0.9726 0.0336  -0.1700 -0.0363 140 LYS   N C   
24178 O  O   . LYS   N  140 ? 1.8951 0.7314 1.0140 0.0029  -0.1591 0.0406  140 LYS   N O   
24179 C  CB  . LYS   N  140 ? 1.8207 0.7378 1.0675 0.0668  -0.1429 -0.0291 140 LYS   N CB  
24180 C  CG  . LYS   N  140 ? 1.7914 0.8043 1.1304 0.0253  -0.1105 -0.0367 140 LYS   N CG  
24181 C  CD  . LYS   N  140 ? 1.8096 0.8427 1.1901 0.0282  -0.0717 -0.0163 140 LYS   N CD  
24182 C  CE  . LYS   N  140 ? 1.8037 0.8085 1.2801 0.0130  -0.0049 -0.0001 140 LYS   N CE  
24183 N  NZ  . LYS   N  140 ? 1.8374 0.8413 1.3372 0.0490  0.0403  0.0183  140 LYS   N NZ  
24184 N  N   . ASN   N  141 ? 1.8455 0.7880 1.0395 0.0150  -0.1704 -0.0084 141 ASN   N N   
24185 C  CA  . ASN   N  141 ? 1.8780 0.8712 1.0417 0.0232  -0.2127 0.0138  141 ASN   N CA  
24186 C  C   . ASN   N  141 ? 1.8885 0.8871 1.0491 0.0317  -0.2549 -0.0292 141 ASN   N C   
24187 O  O   . ASN   N  141 ? 1.9740 0.9685 1.1068 0.0500  -0.2436 -0.1450 141 ASN   N O   
24188 C  CB  . ASN   N  141 ? 1.8929 0.8601 1.0225 0.0398  -0.1935 0.0377  141 ASN   N CB  
24189 C  CG  . ASN   N  141 ? 1.9288 0.8392 1.0490 0.0398  -0.1613 0.0235  141 ASN   N CG  
24190 O  OD1 . ASN   N  141 ? 1.9367 0.7958 1.0009 0.0276  -0.1829 0.0629  141 ASN   N OD1 
24191 N  ND2 . ASN   N  141 ? 1.9707 0.9017 1.0511 0.0507  -0.1345 0.0504  141 ASN   N ND2 
24192 N  N   . PHE   N  142 ? 1.8451 0.8035 1.0878 0.0136  -0.2527 -0.0284 142 PHE   N N   
24193 C  CA  . PHE   N  142 ? 1.8432 0.7901 1.1075 -0.0214 -0.2511 -0.0101 142 PHE   N CA  
24194 C  C   . PHE   N  142 ? 1.8596 0.8080 1.1290 -0.0617 -0.2148 0.0311  142 PHE   N C   
24195 O  O   . PHE   N  142 ? 1.8597 0.8468 1.1599 -0.0793 -0.1636 0.0446  142 PHE   N O   
24196 C  CB  . PHE   N  142 ? 1.8167 0.8131 1.1173 -0.0448 -0.2570 0.0002  142 PHE   N CB  
24197 C  CG  . PHE   N  142 ? 1.7828 0.7883 1.1628 -0.0614 -0.2618 0.0494  142 PHE   N CG  
24198 C  CD1 . PHE   N  142 ? 1.7572 0.8156 1.1477 -0.0705 -0.2674 0.1109  142 PHE   N CD1 
24199 C  CD2 . PHE   N  142 ? 1.7793 0.8203 1.2244 -0.0665 -0.2353 0.0696  142 PHE   N CD2 
24200 C  CE1 . PHE   N  142 ? 1.7614 0.8025 1.1855 -0.0754 -0.2578 0.1396  142 PHE   N CE1 
24201 C  CE2 . PHE   N  142 ? 1.7799 0.8082 1.2366 -0.0890 -0.1899 0.0965  142 PHE   N CE2 
24202 C  CZ  . PHE   N  142 ? 1.7728 0.7963 1.2226 -0.0814 -0.2098 0.1319  142 PHE   N CZ  
24203 N  N   . ARG   N  143 ? 1.9248 0.8200 1.1209 -0.0346 -0.2090 0.0149  143 ARG   N N   
24204 C  CA  . ARG   N  143 ? 1.9561 0.8945 1.1115 0.0004  -0.2107 0.0120  143 ARG   N CA  
24205 C  C   . ARG   N  143 ? 1.9309 0.8981 1.0588 0.0682  -0.2387 0.0673  143 ARG   N C   
24206 O  O   . ARG   N  143 ? 1.8731 1.0454 0.8755 0.1057  -0.2455 0.0780  143 ARG   N O   
24207 C  CB  . ARG   N  143 ? 2.0264 0.7691 1.1427 -0.0046 -0.2177 0.0217  143 ARG   N CB  
24208 C  CG  . ARG   N  143 ? 2.0494 0.7507 1.2724 0.0131  -0.2077 -0.0293 143 ARG   N CG  
24209 C  CD  . ARG   N  143 ? 2.1281 0.7257 1.3298 0.0090  -0.2527 -0.0077 143 ARG   N CD  
24210 N  NE  . ARG   N  143 ? 2.1387 0.6901 1.4433 -0.0328 -0.2462 -0.0354 143 ARG   N NE  
24211 C  CZ  . ARG   N  143 ? 2.1942 0.5166 1.5484 -0.0834 -0.2097 0.0157  143 ARG   N CZ  
24212 N  NH1 . ARG   N  143 ? 2.2255 0.4464 1.5443 -0.0720 -0.2021 0.0634  143 ARG   N NH1 
24213 N  NH2 . ARG   N  143 ? 2.1720 0.3872 1.5956 -0.1633 -0.2085 -0.0010 143 ARG   N NH2 
24214 N  N   . GLU   N  144 ? 1.9550 0.8445 1.1072 0.0835  -0.2353 0.1107  144 GLU   N N   
24215 C  CA  . GLU   N  144 ? 2.0127 0.8342 1.1927 0.0066  -0.1882 0.1349  144 GLU   N CA  
24216 C  C   . GLU   N  144 ? 1.9857 0.8185 1.1545 -0.0016 -0.1768 0.2013  144 GLU   N C   
24217 O  O   . GLU   N  144 ? 1.9942 0.8801 1.1708 -0.0044 -0.1314 0.2274  144 GLU   N O   
24218 C  CB  . GLU   N  144 ? 2.0277 0.8039 1.2572 0.0119  -0.1942 0.1218  144 GLU   N CB  
24219 C  CG  . GLU   N  144 ? 2.0464 0.7888 1.2903 -0.0033 -0.2088 0.1574  144 GLU   N CG  
24220 C  CD  . GLU   N  144 ? 2.0376 0.8066 1.4193 -0.0353 -0.2133 0.1683  144 GLU   N CD  
24221 O  OE1 . GLU   N  144 ? 2.0374 0.9227 1.3811 -0.1031 -0.1851 0.1815  144 GLU   N OE1 
24222 O  OE2 . GLU   N  144 ? 2.0395 0.7859 1.4897 -0.0826 -0.2040 0.1600  144 GLU   N OE2 
24223 N  N   . ASN   N  145 ? 1.9668 0.8867 1.2544 -0.0525 -0.1211 0.1990  145 ASN   N N   
24224 C  CA  . ASN   N  145 ? 1.9553 0.9237 1.2045 0.0151  -0.0812 0.1779  145 ASN   N CA  
24225 C  C   . ASN   N  145 ? 2.0295 0.8366 1.1412 0.0132  -0.0981 0.1904  145 ASN   N C   
24226 O  O   . ASN   N  145 ? 2.0305 0.8414 1.1392 0.0246  -0.0923 0.2524  145 ASN   N O   
24227 C  CB  . ASN   N  145 ? 2.0149 0.9651 1.2713 -0.0187 -0.0035 0.1584  145 ASN   N CB  
24228 C  CG  . ASN   N  145 ? 1.9570 0.8699 1.3536 -0.0223 0.0809  0.1208  145 ASN   N CG  
24229 O  OD1 . ASN   N  145 ? 1.9589 1.0982 1.4295 -0.0578 0.1255  0.0411  145 ASN   N OD1 
24230 N  ND2 . ASN   N  145 ? 2.0076 0.7783 1.4497 -0.0221 0.1012  0.0417  145 ASN   N ND2 
24231 N  N   . MET   N  146 ? 2.0289 0.7111 1.2223 0.0644  -0.1590 0.1374  146 MET   N N   
24232 C  CA  . MET   N  146 ? 2.0058 0.7873 1.1620 0.0635  -0.1990 0.0328  146 MET   N CA  
24233 C  C   . MET   N  146 ? 2.0556 0.7700 1.0823 0.0657  -0.2238 0.0310  146 MET   N C   
24234 O  O   . MET   N  146 ? 2.0624 0.7537 1.0858 0.0192  -0.2228 0.0305  146 MET   N O   
24235 C  CB  . MET   N  146 ? 1.9987 0.8995 1.2088 0.1101  -0.1928 -0.0100 146 MET   N CB  
24236 C  CG  . MET   N  146 ? 1.9683 0.8883 1.1816 0.1548  -0.1869 -0.0453 146 MET   N CG  
24237 S  SD  . MET   N  146 ? 1.9684 0.9108 1.1240 0.3126  -0.2924 -0.0148 146 MET   N SD  
24238 C  CE  . MET   N  146 ? 1.9566 1.0061 1.0581 0.1860  -0.2506 0.0245  146 MET   N CE  
24239 N  N   . SER   N  147 ? 2.0383 0.7075 0.9918 -0.0115 -0.2557 -0.0325 147 SER   N N   
24240 C  CA  . SER   N  147 ? 2.0699 0.6889 0.9084 -0.0083 -0.2894 -0.0409 147 SER   N CA  
24241 C  C   . SER   N  147 ? 2.0358 0.6560 0.9036 -0.0347 -0.3118 0.0021  147 SER   N C   
24242 O  O   . SER   N  147 ? 1.9540 0.5256 0.9025 -0.0775 -0.2897 0.0539  147 SER   N O   
24243 C  CB  . SER   N  147 ? 2.0828 0.6687 0.8910 -0.0153 -0.3162 -0.0901 147 SER   N CB  
24244 O  OG  . SER   N  147 ? 2.0867 0.6704 0.8762 -0.0089 -0.3484 -0.1001 147 SER   N OG  
24245 N  N   . LYS   N  148 ? 2.0654 0.7646 0.9003 -0.0760 -0.3793 -0.0023 148 LYS   N N   
24246 C  CA  . LYS   N  148 ? 2.0696 0.8566 0.9404 -0.0690 -0.3724 -0.0103 148 LYS   N CA  
24247 C  C   . LYS   N  148 ? 2.1279 0.8339 1.0018 -0.0427 -0.4094 0.0685  148 LYS   N C   
24248 O  O   . LYS   N  148 ? 2.1153 0.7533 0.9585 0.0156  -0.3853 0.1714  148 LYS   N O   
24249 C  CB  . LYS   N  148 ? 2.0872 0.9631 0.9990 -0.1115 -0.4175 -0.0409 148 LYS   N CB  
24250 C  CG  . LYS   N  148 ? 2.0352 0.9828 1.0392 -0.1651 -0.4308 -0.0679 148 LYS   N CG  
24251 C  CD  . LYS   N  148 ? 2.0328 1.0648 1.1139 -0.1969 -0.4495 -0.0562 148 LYS   N CD  
24252 C  CE  . LYS   N  148 ? 2.0445 1.1196 1.1377 -0.2088 -0.4344 -0.0788 148 LYS   N CE  
24253 N  NZ  . LYS   N  148 ? 2.0706 1.2145 1.2201 -0.2580 -0.4490 -0.0956 148 LYS   N NZ  
24254 N  N   . GLU   N  149 ? 2.1717 0.8856 0.9654 -0.0342 -0.4412 0.0349  149 GLU   N N   
24255 C  CA  . GLU   N  149 ? 2.1688 0.9366 1.0866 -0.0019 -0.4110 0.0035  149 GLU   N CA  
24256 C  C   . GLU   N  149 ? 2.1096 0.8620 0.9893 0.0623  -0.3960 0.0272  149 GLU   N C   
24257 O  O   . GLU   N  149 ? 2.0420 0.7259 1.0171 0.0336  -0.4789 0.0107  149 GLU   N O   
24258 C  CB  . GLU   N  149 ? 2.2740 1.0871 1.1050 0.0043  -0.4335 0.0106  149 GLU   N CB  
24259 C  CG  . GLU   N  149 ? 2.2759 1.2533 1.2874 -0.0551 -0.4502 0.0016  149 GLU   N CG  
24260 C  CD  . GLU   N  149 ? 2.3595 1.2704 1.3662 -0.0080 -0.4007 0.0366  149 GLU   N CD  
24261 O  OE1 . GLU   N  149 ? 2.4059 1.4076 1.4228 0.0764  -0.3590 0.0921  149 GLU   N OE1 
24262 O  OE2 . GLU   N  149 ? 2.3453 1.3376 1.4246 -0.0307 -0.4138 0.0988  149 GLU   N OE2 
24263 N  N   . GLU   N  150 ? 2.1208 0.8696 0.9401 0.0339  -0.3811 0.0322  150 GLU   N N   
24264 C  CA  . GLU   N  150 ? 2.1240 0.8565 0.9544 0.0143  -0.3367 0.0275  150 GLU   N CA  
24265 C  C   . GLU   N  150 ? 2.0944 0.8825 0.9630 0.0360  -0.3159 0.0589  150 GLU   N C   
24266 O  O   . GLU   N  150 ? 2.0549 1.0395 0.9174 0.0802  -0.2744 -0.0137 150 GLU   N O   
24267 C  CB  . GLU   N  150 ? 2.1669 0.8475 0.9553 -0.0019 -0.2928 0.0197  150 GLU   N CB  
24268 C  CG  . GLU   N  150 ? 2.2386 0.9204 0.9721 0.0014  -0.2759 0.0460  150 GLU   N CG  
24269 C  CD  . GLU   N  150 ? 2.2886 0.9746 1.0412 0.0138  -0.2109 0.0823  150 GLU   N CD  
24270 O  OE1 . GLU   N  150 ? 2.2941 0.9878 1.1183 0.0129  -0.2142 0.1266  150 GLU   N OE1 
24271 O  OE2 . GLU   N  150 ? 2.3975 1.1848 1.0722 -0.0310 -0.0965 0.1486  150 GLU   N OE2 
24272 N  N   . THR   N  151 ? 2.0887 0.8465 0.9027 0.0159  -0.3063 0.0171  151 THR   N N   
24273 C  CA  . THR   N  151 ? 2.0275 0.7773 0.9016 0.0092  -0.3051 0.0135  151 THR   N CA  
24274 C  C   . THR   N  151 ? 1.9668 0.6554 0.9113 0.0125  -0.3544 0.0166  151 THR   N C   
24275 O  O   . THR   N  151 ? 1.9728 0.5188 0.9172 0.0612  -0.3907 0.0402  151 THR   N O   
24276 C  CB  . THR   N  151 ? 2.0103 0.7787 0.8704 0.0021  -0.3108 -0.0022 151 THR   N CB  
24277 O  OG1 . THR   N  151 ? 2.0611 0.7806 0.8381 -0.0090 -0.2796 0.0243  151 THR   N OG1 
24278 C  CG2 . THR   N  151 ? 1.9706 0.7862 0.8687 -0.0140 -0.3178 -0.0189 151 THR   N CG2 
24279 N  N   . VAL   N  152 ? 1.9526 0.6885 0.9068 0.0072  -0.3508 0.0245  152 VAL   N N   
24280 C  CA  . VAL   N  152 ? 1.9084 0.7920 0.8931 -0.0037 -0.3885 0.0269  152 VAL   N CA  
24281 C  C   . VAL   N  152 ? 1.9365 0.7936 0.8877 0.0211  -0.3447 0.0671  152 VAL   N C   
24282 O  O   . VAL   N  152 ? 1.9392 0.9429 0.9358 -0.0190 -0.2435 0.0685  152 VAL   N O   
24283 C  CB  . VAL   N  152 ? 1.9259 0.8054 0.8936 0.0167  -0.4269 0.0306  152 VAL   N CB  
24284 C  CG1 . VAL   N  152 ? 1.8928 0.7595 0.8558 0.0138  -0.4862 0.0203  152 VAL   N CG1 
24285 C  CG2 . VAL   N  152 ? 1.9168 0.8087 0.9367 0.0019  -0.4202 0.0150  152 VAL   N CG2 
24286 N  N   . ASP   N  153 ? 1.9879 0.9027 0.8760 0.0713  -0.3487 0.1259  153 ASP   N N   
24287 C  CA  . ASP   N  153 ? 2.0198 0.9072 0.9310 0.0875  -0.3442 0.0913  153 ASP   N CA  
24288 C  C   . ASP   N  153 ? 1.9839 0.7763 0.9721 0.0984  -0.3423 0.0827  153 ASP   N C   
24289 O  O   . ASP   N  153 ? 2.0023 0.8641 0.9626 0.0806  -0.3672 0.0221  153 ASP   N O   
24290 C  CB  . ASP   N  153 ? 2.0881 1.0340 0.9836 0.0848  -0.2672 0.1445  153 ASP   N CB  
24291 C  CG  . ASP   N  153 ? 2.0991 1.1546 0.9796 0.1105  -0.2757 0.2148  153 ASP   N CG  
24292 O  OD1 . ASP   N  153 ? 2.0978 1.1875 1.0459 0.1446  -0.2494 0.2324  153 ASP   N OD1 
24293 O  OD2 . ASP   N  153 ? 2.1465 1.2547 1.0616 0.1143  -0.1414 0.3147  153 ASP   N OD2 
24294 N  N   . PHE   N  154 ? 2.0026 0.6137 0.9732 0.1009  -0.3080 0.0294  154 PHE   N N   
24295 C  CA  . PHE   N  154 ? 1.9898 0.6127 0.9534 0.0997  -0.2785 0.0176  154 PHE   N CA  
24296 C  C   . PHE   N  154 ? 1.9774 0.6877 0.9705 0.0979  -0.2496 0.0191  154 PHE   N C   
24297 O  O   . PHE   N  154 ? 1.9972 0.7091 0.8808 0.0919  -0.2384 0.0500  154 PHE   N O   
24298 C  CB  . PHE   N  154 ? 1.9962 0.5925 0.9618 0.0972  -0.2938 0.0137  154 PHE   N CB  
24299 C  CG  . PHE   N  154 ? 2.0118 0.4817 0.9653 0.1121  -0.3102 0.0042  154 PHE   N CG  
24300 C  CD1 . PHE   N  154 ? 2.0098 0.4485 0.9524 0.1430  -0.3177 0.0120  154 PHE   N CD1 
24301 C  CD2 . PHE   N  154 ? 2.0162 0.4615 1.0041 0.1361  -0.3465 -0.0225 154 PHE   N CD2 
24302 C  CE1 . PHE   N  154 ? 1.9953 0.3994 1.0079 0.1148  -0.3236 -0.0027 154 PHE   N CE1 
24303 C  CE2 . PHE   N  154 ? 2.0138 0.4106 1.0222 0.1251  -0.3490 -0.0233 154 PHE   N CE2 
24304 C  CZ  . PHE   N  154 ? 1.9837 0.4056 1.0328 0.1316  -0.3456 -0.0131 154 PHE   N CZ  
24305 N  N   . ILE   N  155 ? 1.9339 0.7304 0.9195 0.0426  -0.2190 -0.0481 155 ILE   N N   
24306 C  CA  . ILE   N  155 ? 1.9102 0.7751 0.9315 0.0363  -0.2142 -0.0456 155 ILE   N CA  
24307 C  C   . ILE   N  155 ? 1.8395 0.8498 1.0359 0.0419  -0.2590 -0.0004 155 ILE   N C   
24308 O  O   . ILE   N  155 ? 1.8086 0.8295 1.0905 0.0552  -0.2071 -0.0369 155 ILE   N O   
24309 C  CB  . ILE   N  155 ? 1.9197 0.7590 0.8897 0.0517  -0.2159 -0.0802 155 ILE   N CB  
24310 C  CG1 . ILE   N  155 ? 1.9113 0.8428 0.8826 0.0634  -0.1893 -0.1203 155 ILE   N CG1 
24311 C  CG2 . ILE   N  155 ? 1.8856 0.7035 0.9097 0.0393  -0.2225 -0.0636 155 ILE   N CG2 
24312 C  CD1 . ILE   N  155 ? 1.9354 0.8796 0.8966 0.0036  -0.2099 -0.1644 155 ILE   N CD1 
24313 N  N   . LYS   N  156 ? 1.8572 0.8827 1.0341 0.0028  -0.2759 0.0045  156 LYS   N N   
24314 C  CA  . LYS   N  156 ? 1.8503 0.8873 1.0612 0.0006  -0.2910 0.0394  156 LYS   N CA  
24315 C  C   . LYS   N  156 ? 1.8363 0.8817 1.0179 -0.0067 -0.2812 0.0591  156 LYS   N C   
24316 O  O   . LYS   N  156 ? 1.8500 0.9441 0.9476 -0.0104 -0.3004 0.0676  156 LYS   N O   
24317 C  CB  . LYS   N  156 ? 1.8856 0.9364 1.0626 0.0236  -0.3088 0.0682  156 LYS   N CB  
24318 C  CG  . LYS   N  156 ? 1.8878 0.9769 1.0956 0.0446  -0.3403 0.0733  156 LYS   N CG  
24319 C  CD  . LYS   N  156 ? 1.9516 1.0391 1.0882 0.0313  -0.3600 0.0502  156 LYS   N CD  
24320 C  CE  . LYS   N  156 ? 1.9800 1.0869 1.1624 0.0146  -0.3505 -0.0048 156 LYS   N CE  
24321 N  NZ  . LYS   N  156 ? 1.9970 1.1290 1.2017 0.0372  -0.3641 0.0472  156 LYS   N NZ  
24322 N  N   . HIS   N  157 ? 1.8359 0.8009 1.0227 -0.0059 -0.3076 0.0705  157 HIS   N N   
24323 C  CA  . HIS   N  157 ? 1.8099 0.7755 1.0275 0.0069  -0.3192 0.1061  157 HIS   N CA  
24324 C  C   . HIS   N  157 ? 1.7651 0.7059 1.0609 -0.0313 -0.3278 0.0785  157 HIS   N C   
24325 O  O   . HIS   N  157 ? 1.7800 0.7781 1.0330 -0.0408 -0.2811 0.0490  157 HIS   N O   
24326 C  CB  . HIS   N  157 ? 1.8176 0.7428 1.0275 0.0286  -0.3169 0.1212  157 HIS   N CB  
24327 C  CG  . HIS   N  157 ? 1.8441 0.7852 1.0533 0.0643  -0.3284 0.1409  157 HIS   N CG  
24328 N  ND1 . HIS   N  157 ? 1.8805 0.7767 1.0170 0.0880  -0.3622 0.1630  157 HIS   N ND1 
24329 C  CD2 . HIS   N  157 ? 1.8495 0.8422 1.0185 0.1159  -0.3451 0.1799  157 HIS   N CD2 
24330 C  CE1 . HIS   N  157 ? 1.9042 0.8142 1.0367 0.0924  -0.3477 0.2120  157 HIS   N CE1 
24331 N  NE2 . HIS   N  157 ? 1.8927 0.8032 0.9989 0.1484  -0.3564 0.2284  157 HIS   N NE2 
24332 N  N   . SER   N  158 ? 1.7151 0.6542 1.0517 -0.0577 -0.3351 0.0256  158 SER   N N   
24333 C  CA  . SER   N  158 ? 1.6708 0.5955 1.0558 -0.0658 -0.3282 0.0265  158 SER   N CA  
24334 C  C   . SER   N  158 ? 1.6400 0.5572 1.0630 -0.0386 -0.3380 0.0140  158 SER   N C   
24335 O  O   . SER   N  158 ? 1.6597 0.4201 1.2032 -0.0742 -0.2898 0.0181  158 SER   N O   
24336 C  CB  . SER   N  158 ? 1.6199 0.6325 1.0031 -0.0720 -0.3041 0.0326  158 SER   N CB  
24337 O  OG  . SER   N  158 ? 1.6145 0.6334 1.0140 -0.1182 -0.3089 0.0654  158 SER   N OG  
24338 N  N   . LEU   N  159 ? 1.5843 0.6204 1.0615 -0.0519 -0.4003 0.0086  159 LEU   N N   
24339 C  CA  . LEU   N  159 ? 1.5823 0.6313 1.0549 -0.0132 -0.4081 0.0025  159 LEU   N CA  
24340 C  C   . LEU   N  159 ? 1.6304 0.6180 1.0508 0.0090  -0.4426 0.0431  159 LEU   N C   
24341 O  O   . LEU   N  159 ? 1.6097 0.5452 0.9996 0.0733  -0.4506 0.1556  159 LEU   N O   
24342 C  CB  . LEU   N  159 ? 1.6040 0.6465 1.1138 -0.0315 -0.4231 -0.0254 159 LEU   N CB  
24343 C  CG  . LEU   N  159 ? 1.5968 0.6856 1.1500 -0.0030 -0.4029 -0.0411 159 LEU   N CG  
24344 C  CD1 . LEU   N  159 ? 1.6161 0.6966 1.2143 -0.0101 -0.3777 -0.0587 159 LEU   N CD1 
24345 C  CD2 . LEU   N  159 ? 1.5620 0.6402 1.1492 -0.0242 -0.3920 -0.0542 159 LEU   N CD2 
24346 N  N   . SER   N  160 ? 1.6800 0.5972 1.0702 0.0351  -0.4452 0.0469  160 SER   N N   
24347 C  CA  . SER   N  160 ? 1.7153 0.6613 1.1203 0.0893  -0.4349 0.0761  160 SER   N CA  
24348 C  C   . SER   N  160 ? 1.6601 0.6488 1.1189 0.0883  -0.4204 0.0924  160 SER   N C   
24349 O  O   . SER   N  160 ? 1.6574 0.6257 1.1211 0.0644  -0.3979 0.1028  160 SER   N O   
24350 C  CB  . SER   N  160 ? 1.7922 0.7435 1.1253 0.1026  -0.4728 0.0820  160 SER   N CB  
24351 O  OG  . SER   N  160 ? 1.8235 0.8574 1.2058 0.1717  -0.5192 0.0698  160 SER   N OG  
24352 N  N   . GLN   N  161 ? 1.6727 0.5739 1.0915 0.0765  -0.4056 0.0924  161 GLN   N N   
24353 C  CA  . GLN   N  161 ? 1.7480 0.5062 1.0771 0.0843  -0.3468 0.0676  161 GLN   N CA  
24354 C  C   . GLN   N  161 ? 1.7861 0.5510 1.0325 0.0588  -0.3299 -0.0019 161 GLN   N C   
24355 O  O   . GLN   N  161 ? 1.8302 0.5734 1.0999 0.0915  -0.2578 -0.0047 161 GLN   N O   
24356 C  CB  . GLN   N  161 ? 1.7615 0.4695 1.0685 0.0710  -0.3453 0.1012  161 GLN   N CB  
24357 C  CG  . GLN   N  161 ? 1.7716 0.4921 1.1042 0.0900  -0.3272 0.1361  161 GLN   N CG  
24358 C  CD  . GLN   N  161 ? 1.7749 0.4315 1.1195 0.0435  -0.3217 0.1347  161 GLN   N CD  
24359 O  OE1 . GLN   N  161 ? 1.7803 0.4078 1.1824 0.0677  -0.3130 0.2121  161 GLN   N OE1 
24360 N  NE2 . GLN   N  161 ? 1.7459 0.3054 1.1368 0.0525  -0.3006 0.1622  161 GLN   N NE2 
24361 N  N   . ALA   N  162 ? 1.7754 0.5568 0.9378 0.0672  -0.3263 -0.0247 162 ALA   N N   
24362 C  CA  . ALA   N  162 ? 1.6884 0.5310 0.9406 0.0552  -0.3454 -0.0292 162 ALA   N CA  
24363 C  C   . ALA   N  162 ? 1.6253 0.5564 1.0183 0.0200  -0.3646 -0.0032 162 ALA   N C   
24364 O  O   . ALA   N  162 ? 1.6138 0.5836 1.0122 0.0480  -0.3374 0.0023  162 ALA   N O   
24365 C  CB  . ALA   N  162 ? 1.6649 0.5376 0.9165 0.0642  -0.3619 -0.0624 162 ALA   N CB  
24366 N  N   . ILE   N  163 ? 1.6259 0.5433 1.0255 0.0106  -0.3721 0.0088  163 ILE   N N   
24367 C  CA  . ILE   N  163 ? 1.5948 0.5860 1.0706 0.0037  -0.4014 0.0169  163 ILE   N CA  
24368 C  C   . ILE   N  163 ? 1.5867 0.5924 1.0859 -0.0013 -0.4069 -0.0019 163 ILE   N C   
24369 O  O   . ILE   N  163 ? 1.5881 0.5874 1.0883 -0.0145 -0.3975 0.0015  163 ILE   N O   
24370 C  CB  . ILE   N  163 ? 1.5742 0.6080 1.0978 0.0001  -0.4195 0.0445  163 ILE   N CB  
24371 C  CG1 . ILE   N  163 ? 1.5730 0.6048 1.1427 -0.0477 -0.4126 0.0098  163 ILE   N CG1 
24372 C  CG2 . ILE   N  163 ? 1.5655 0.5721 1.1211 -0.0070 -0.4162 0.0751  163 ILE   N CG2 
24373 C  CD1 . ILE   N  163 ? 1.6019 0.6863 1.1441 -0.0605 -0.4278 -0.0106 163 ILE   N CD1 
24374 N  N   . LYS   N  164 ? 1.5717 0.6438 1.0979 -0.0253 -0.3769 0.0026  164 LYS   N N   
24375 C  CA  . LYS   N  164 ? 1.5695 0.6754 1.1441 0.0324  -0.3342 0.0134  164 LYS   N CA  
24376 C  C   . LYS   N  164 ? 1.6003 0.6320 1.1697 0.0444  -0.3076 -0.0268 164 LYS   N C   
24377 O  O   . LYS   N  164 ? 1.6035 0.5586 1.2623 0.0855  -0.3483 -0.0004 164 LYS   N O   
24378 C  CB  . LYS   N  164 ? 1.5435 0.7279 1.1683 0.0401  -0.3114 0.0309  164 LYS   N CB  
24379 C  CG  . LYS   N  164 ? 1.5342 0.7240 1.2232 0.0352  -0.2754 0.0392  164 LYS   N CG  
24380 C  CD  . LYS   N  164 ? 1.5540 0.8410 1.2489 0.0118  -0.2536 0.0755  164 LYS   N CD  
24381 C  CE  . LYS   N  164 ? 1.5950 0.8789 1.3484 0.0444  -0.2194 0.0914  164 LYS   N CE  
24382 N  NZ  . LYS   N  164 ? 1.6524 0.9776 1.3719 0.0328  -0.1941 0.1232  164 LYS   N NZ  
24383 N  N   . TRP   N  165 ? 1.5805 0.6295 1.1457 0.0170  -0.2879 -0.0507 165 TRP   N N   
24384 C  CA  . TRP   N  165 ? 1.6183 0.6048 1.1073 -0.0121 -0.2502 -0.0450 165 TRP   N CA  
24385 C  C   . TRP   N  165 ? 1.6362 0.6109 1.0768 -0.0158 -0.2563 -0.0652 165 TRP   N C   
24386 O  O   . TRP   N  165 ? 1.6251 0.7332 1.0764 -0.0217 -0.1979 -0.0783 165 TRP   N O   
24387 C  CB  . TRP   N  165 ? 1.6273 0.5945 1.0836 -0.0084 -0.2337 -0.0175 165 TRP   N CB  
24388 C  CG  . TRP   N  165 ? 1.6618 0.5943 1.0754 0.0416  -0.2353 -0.0108 165 TRP   N CG  
24389 C  CD1 . TRP   N  165 ? 1.6797 0.5751 1.0186 0.0409  -0.2627 0.0287  165 TRP   N CD1 
24390 C  CD2 . TRP   N  165 ? 1.6732 0.6190 1.0680 0.0568  -0.2345 0.0687  165 TRP   N CD2 
24391 N  NE1 . TRP   N  165 ? 1.6761 0.5940 1.0369 0.0722  -0.2787 0.0547  165 TRP   N NE1 
24392 C  CE2 . TRP   N  165 ? 1.6762 0.5775 1.0570 0.0636  -0.2571 0.0717  165 TRP   N CE2 
24393 C  CE3 . TRP   N  165 ? 1.6740 0.5610 1.1202 0.0507  -0.2158 0.0851  165 TRP   N CE3 
24394 C  CZ2 . TRP   N  165 ? 1.6831 0.5862 1.1063 0.0603  -0.2521 0.0936  165 TRP   N CZ2 
24395 C  CZ3 . TRP   N  165 ? 1.6892 0.5610 1.1252 0.0617  -0.2110 0.0826  165 TRP   N CZ3 
24396 C  CH2 . TRP   N  165 ? 1.7011 0.6049 1.1171 0.0736  -0.2311 0.0940  165 TRP   N CH2 
24397 N  N   . ASP   N  166 ? 1.6562 0.6105 1.0065 0.0064  -0.2694 -0.0653 166 ASP   N N   
24398 C  CA  . ASP   N  166 ? 1.6433 0.5648 1.0150 0.0187  -0.2661 -0.0741 166 ASP   N CA  
24399 C  C   . ASP   N  166 ? 1.6183 0.4883 1.0018 0.0037  -0.3063 -0.1126 166 ASP   N C   
24400 O  O   . ASP   N  166 ? 1.6274 0.4021 1.0402 -0.0177 -0.2862 -0.1359 166 ASP   N O   
24401 C  CB  . ASP   N  166 ? 1.6920 0.5679 1.0063 0.0399  -0.2376 -0.0208 166 ASP   N CB  
24402 C  CG  . ASP   N  166 ? 1.7535 0.6008 1.0498 0.0397  -0.1876 0.0242  166 ASP   N CG  
24403 O  OD1 . ASP   N  166 ? 1.8094 0.4545 1.0649 0.0745  -0.0572 0.0567  166 ASP   N OD1 
24404 O  OD2 . ASP   N  166 ? 1.7846 0.5906 1.0092 0.0698  -0.2157 0.0698  166 ASP   N OD2 
24405 N  N   . GLY   N  167 ? 1.5662 0.5122 1.0072 -0.0004 -0.2914 -0.0996 167 GLY   N N   
24406 C  CA  . GLY   N  167 ? 1.5318 0.4810 1.0820 -0.0420 -0.3282 -0.0947 167 GLY   N CA  
24407 C  C   . GLY   N  167 ? 1.4910 0.4513 1.0898 -0.0576 -0.3639 -0.1694 167 GLY   N C   
24408 O  O   . GLY   N  167 ? 1.5004 0.3924 1.0296 -0.0525 -0.4241 -0.2408 167 GLY   N O   
24409 N  N   . SER   N  168 ? 1.4981 0.4322 1.1341 -0.0684 -0.3477 -0.1177 168 SER   N N   
24410 C  CA  . SER   N  168 ? 1.5442 0.4755 1.1533 -0.1175 -0.3090 -0.0486 168 SER   N CA  
24411 C  C   . SER   N  168 ? 1.5571 0.4472 1.1739 -0.0952 -0.3107 -0.0616 168 SER   N C   
24412 O  O   . SER   N  168 ? 1.5745 0.4684 1.2846 -0.1290 -0.2717 -0.1010 168 SER   N O   
24413 C  CB  . SER   N  168 ? 1.5423 0.5028 1.1441 -0.1255 -0.2813 0.0135  168 SER   N CB  
24414 O  OG  . SER   N  168 ? 1.5906 0.4655 1.1330 -0.1758 -0.2582 0.0431  168 SER   N OG  
24415 N  N   . SER   N  169 ? 1.5608 0.3874 1.2091 -0.0756 -0.3153 -0.0187 169 SER   N N   
24416 C  CA  . SER   N  169 ? 1.5511 0.3830 1.2012 -0.0705 -0.3280 -0.0023 169 SER   N CA  
24417 C  C   . SER   N  169 ? 1.5845 0.4208 1.2551 -0.0568 -0.3688 0.0043  169 SER   N C   
24418 O  O   . SER   N  169 ? 1.6082 0.4715 1.2883 -0.0267 -0.3569 -0.0789 169 SER   N O   
24419 C  CB  . SER   N  169 ? 1.5568 0.3518 1.2036 -0.0810 -0.3176 0.0135  169 SER   N CB  
24420 O  OG  . SER   N  169 ? 1.5096 0.3002 1.1904 -0.1033 -0.2766 0.0146  169 SER   N OG  
24421 N  N   . GLY   N  170 ? 1.5665 0.4594 1.2581 -0.0329 -0.4272 0.0235  170 GLY   N N   
24422 C  CA  . GLY   N  170 ? 1.5814 0.4573 1.3086 -0.0007 -0.4378 0.0233  170 GLY   N CA  
24423 C  C   . GLY   N  170 ? 1.5657 0.4444 1.3082 0.0288  -0.4776 0.0229  170 GLY   N C   
24424 O  O   . GLY   N  170 ? 1.5361 0.4050 1.2434 -0.0198 -0.5258 0.0024  170 GLY   N O   
24425 N  N   . GLY   N  171 ? 1.5824 0.3590 1.3494 0.1055  -0.4575 0.0238  171 GLY   N N   
24426 C  CA  . GLY   N  171 ? 1.6371 0.3168 1.2930 0.1035  -0.4220 0.0159  171 GLY   N CA  
24427 C  C   . GLY   N  171 ? 1.7019 0.3687 1.2234 0.1025  -0.4229 0.1264  171 GLY   N C   
24428 O  O   . GLY   N  171 ? 1.7556 0.2386 1.1766 0.1630  -0.4317 0.0203  171 GLY   N O   
24429 N  N   . VAL   N  172 ? 1.6968 0.4091 1.1573 0.0941  -0.4238 0.0667  172 VAL   N N   
24430 C  CA  . VAL   N  172 ? 1.6866 0.4289 1.1070 0.0722  -0.4627 0.1000  172 VAL   N CA  
24431 C  C   . VAL   N  172 ? 1.6923 0.4135 1.0936 0.0265  -0.3503 0.0819  172 VAL   N C   
24432 O  O   . VAL   N  172 ? 1.7147 0.2994 1.1148 -0.0035 -0.3514 0.1091  172 VAL   N O   
24433 C  CB  . VAL   N  172 ? 1.6494 0.4994 1.0936 0.0707  -0.5303 0.0836  172 VAL   N CB  
24434 C  CG1 . VAL   N  172 ? 1.6649 0.4799 1.1562 0.1003  -0.5201 0.0791  172 VAL   N CG1 
24435 C  CG2 . VAL   N  172 ? 1.6518 0.5322 1.0830 0.0700  -0.5425 0.0988  172 VAL   N CG2 
24436 N  N   . ILE   N  173 ? 1.7092 0.4800 1.0363 0.0155  -0.3991 0.0607  173 ILE   N N   
24437 C  CA  . ILE   N  173 ? 1.7140 0.5666 1.0117 0.0232  -0.3815 0.0300  173 ILE   N CA  
24438 C  C   . ILE   N  173 ? 1.7104 0.5942 0.9067 0.0483  -0.4108 0.0156  173 ILE   N C   
24439 O  O   . ILE   N  173 ? 1.7070 0.7005 0.9545 0.1219  -0.4882 0.0467  173 ILE   N O   
24440 C  CB  . ILE   N  173 ? 1.6893 0.5724 1.0601 -0.0155 -0.3698 0.0058  173 ILE   N CB  
24441 C  CG1 . ILE   N  173 ? 1.6978 0.5799 1.1137 -0.0145 -0.3451 -0.0194 173 ILE   N CG1 
24442 C  CG2 . ILE   N  173 ? 1.6917 0.5079 1.0703 -0.0258 -0.3796 -0.0083 173 ILE   N CG2 
24443 C  CD1 . ILE   N  173 ? 1.7234 0.5721 1.1313 -0.0148 -0.3351 -0.0153 173 ILE   N CD1 
24444 N  N   . ARG   N  174 ? 1.7058 0.6343 0.9010 0.0504  -0.3601 0.0504  174 ARG   N N   
24445 C  CA  . ARG   N  174 ? 1.7005 0.6771 0.9245 0.0304  -0.3517 -0.0209 174 ARG   N CA  
24446 C  C   . ARG   N  174 ? 1.7115 0.7388 0.9009 0.0098  -0.3256 0.0140  174 ARG   N C   
24447 O  O   . ARG   N  174 ? 1.7210 0.7056 0.8049 -0.0446 -0.2488 0.0376  174 ARG   N O   
24448 C  CB  . ARG   N  174 ? 1.6601 0.5820 0.9792 0.0511  -0.3333 -0.0312 174 ARG   N CB  
24449 C  CG  . ARG   N  174 ? 1.6233 0.5136 1.0575 0.0454  -0.3423 -0.0397 174 ARG   N CG  
24450 C  CD  . ARG   N  174 ? 1.5991 0.4054 1.1139 0.0488  -0.3443 -0.0865 174 ARG   N CD  
24451 N  NE  . ARG   N  174 ? 1.5945 0.3672 1.1372 0.0614  -0.3530 -0.1168 174 ARG   N NE  
24452 C  CZ  . ARG   N  174 ? 1.6111 0.3567 1.1678 0.0823  -0.3844 -0.1320 174 ARG   N CZ  
24453 N  NH1 . ARG   N  174 ? 1.6715 0.3209 1.1636 0.0968  -0.3882 -0.1100 174 ARG   N NH1 
24454 N  NH2 . ARG   N  174 ? 1.6087 0.3766 1.1332 0.1035  -0.4101 -0.1655 174 ARG   N NH2 
24455 N  N   . MET   N  175 ? 1.7233 0.8306 0.9172 0.0203  -0.3710 -0.0293 175 MET   N N   
24456 C  CA  . MET   N  175 ? 1.7143 0.8514 0.9596 0.0441  -0.3937 -0.0301 175 MET   N CA  
24457 C  C   . MET   N  175 ? 1.6741 0.8723 0.9478 0.0403  -0.4900 -0.0730 175 MET   N C   
24458 O  O   . MET   N  175 ? 1.7001 0.8843 0.9778 0.0651  -0.5890 -0.1045 175 MET   N O   
24459 C  CB  . MET   N  175 ? 1.7631 0.9726 0.9935 0.0510  -0.3548 0.0257  175 MET   N CB  
24460 C  CG  . MET   N  175 ? 1.7567 0.9901 1.0307 0.0289  -0.3125 0.0463  175 MET   N CG  
24461 S  SD  . MET   N  175 ? 1.7483 1.1597 1.1017 0.1110  -0.2558 0.1573  175 MET   N SD  
24462 C  CE  . MET   N  175 ? 1.7934 1.1707 1.1019 0.0868  -0.2472 0.0578  175 MET   N CE  
24463 N  N   . VAL   N  176 ? 1.7161 0.7611 0.9539 0.0348  -0.4708 -0.0672 176 VAL   N N   
24464 C  CA  . VAL   N  176 ? 1.7432 0.7559 0.9981 0.0206  -0.4384 -0.0711 176 VAL   N CA  
24465 C  C   . VAL   N  176 ? 1.7621 0.6549 0.9857 0.0083  -0.4319 -0.0548 176 VAL   N C   
24466 O  O   . VAL   N  176 ? 1.7994 0.5647 0.9312 -0.0115 -0.4644 -0.0334 176 VAL   N O   
24467 C  CB  . VAL   N  176 ? 1.7515 0.7805 0.9932 0.0138  -0.3910 -0.0649 176 VAL   N CB  
24468 C  CG1 . VAL   N  176 ? 1.7896 0.7999 1.0464 0.0117  -0.3665 -0.0972 176 VAL   N CG1 
24469 C  CG2 . VAL   N  176 ? 1.7505 0.7942 1.0029 0.0249  -0.3870 -0.0782 176 VAL   N CG2 
24470 N  N   . VAL   N  177 ? 1.7982 0.6690 0.9986 0.0165  -0.4208 -0.0806 177 VAL   N N   
24471 C  CA  . VAL   N  177 ? 1.8086 0.6913 1.0116 0.0195  -0.4065 -0.0897 177 VAL   N CA  
24472 C  C   . VAL   N  177 ? 1.7800 0.6876 1.0714 0.0090  -0.3779 -0.1090 177 VAL   N C   
24473 O  O   . VAL   N  177 ? 1.8092 0.6314 1.1363 0.0121  -0.3693 -0.0899 177 VAL   N O   
24474 C  CB  . VAL   N  177 ? 1.8304 0.7117 1.0018 0.0263  -0.4210 -0.1175 177 VAL   N CB  
24475 C  CG1 . VAL   N  177 ? 1.8534 0.7421 1.0039 0.0226  -0.4094 -0.1222 177 VAL   N CG1 
24476 C  CG2 . VAL   N  177 ? 1.8005 0.7344 1.0056 0.0389  -0.4525 -0.1171 177 VAL   N CG2 
24477 N  N   . LEU   N  178 ? 1.7840 0.7118 1.1174 0.0387  -0.3503 -0.0988 178 LEU   N N   
24478 C  CA  . LEU   N  178 ? 1.8045 0.7107 1.1599 0.0421  -0.3415 -0.0889 178 LEU   N CA  
24479 C  C   . LEU   N  178 ? 1.8211 0.7189 1.1538 0.0426  -0.3360 -0.0404 178 LEU   N C   
24480 O  O   . LEU   N  178 ? 1.8162 0.6479 1.1549 0.0746  -0.3109 -0.0046 178 LEU   N O   
24481 C  CB  . LEU   N  178 ? 1.7840 0.7231 1.1597 0.0448  -0.3332 -0.1134 178 LEU   N CB  
24482 C  CG  . LEU   N  178 ? 1.7520 0.7275 1.1827 0.0319  -0.3007 -0.1455 178 LEU   N CG  
24483 C  CD1 . LEU   N  178 ? 1.7474 0.7134 1.1902 0.0486  -0.3245 -0.1812 178 LEU   N CD1 
24484 C  CD2 . LEU   N  178 ? 1.7603 0.6932 1.1775 0.0183  -0.2938 -0.1542 178 LEU   N CD2 
24485 N  N   . THR   N  179 ? 1.8804 0.7737 1.1537 0.0343  -0.3800 -0.0423 179 THR   N N   
24486 C  CA  . THR   N  179 ? 1.9022 0.8401 1.0988 0.0416  -0.4011 0.0074  179 THR   N CA  
24487 C  C   . THR   N  179 ? 1.9329 0.8922 1.0722 0.0559  -0.4152 -0.1016 179 THR   N C   
24488 O  O   . THR   N  179 ? 1.8947 0.9605 1.0622 0.0617  -0.4216 -0.0868 179 THR   N O   
24489 C  CB  . THR   N  179 ? 1.9108 0.8130 1.1506 0.0056  -0.4187 0.0462  179 THR   N CB  
24490 O  OG1 . THR   N  179 ? 1.9294 0.7109 1.1657 -0.0211 -0.4793 0.0903  179 THR   N OG1 
24491 C  CG2 . THR   N  179 ? 1.9424 0.8089 1.1452 0.0163  -0.4094 0.0706  179 THR   N CG2 
24492 N  N   . ALA   N  180 ? 1.9554 0.9012 1.0590 0.0637  -0.4465 -0.1459 180 ALA   N N   
24493 C  CA  . ALA   N  180 ? 1.9444 0.8932 1.0461 0.0785  -0.4459 -0.1450 180 ALA   N CA  
24494 C  C   . ALA   N  180 ? 1.9810 0.9197 1.0616 0.0258  -0.4732 -0.1952 180 ALA   N C   
24495 O  O   . ALA   N  180 ? 1.9116 0.8864 0.9935 0.1055  -0.5799 -0.1119 180 ALA   N O   
24496 C  CB  . ALA   N  180 ? 1.9614 0.9151 1.0502 0.0783  -0.4288 -0.1343 180 ALA   N CB  
24497 N  N   . ALA   N  181 ? 2.0256 0.8840 1.0738 0.0328  -0.4429 -0.2156 181 ALA   N N   
24498 C  CA  . ALA   N  181 ? 2.0232 0.9238 1.0942 -0.0514 -0.4065 -0.2616 181 ALA   N CA  
24499 C  C   . ALA   N  181 ? 2.0235 0.8800 1.1244 -0.1006 -0.3776 -0.3169 181 ALA   N C   
24500 O  O   . ALA   N  181 ? 2.0169 0.9610 1.2340 -0.1442 -0.3310 -0.3289 181 ALA   N O   
24501 C  CB  . ALA   N  181 ? 2.0487 0.9667 1.0417 -0.0297 -0.4244 -0.2427 181 ALA   N CB  
24502 N  N   . GLY   N  182 ? 2.0043 0.8353 1.0758 -0.1014 -0.3372 -0.2713 182 GLY   N N   
24503 C  CA  . GLY   N  182 ? 1.9580 0.8354 1.1005 -0.1074 -0.3605 -0.2055 182 GLY   N CA  
24504 C  C   . GLY   N  182 ? 1.8976 0.8355 1.0794 -0.1279 -0.3471 -0.1905 182 GLY   N C   
24505 O  O   . GLY   N  182 ? 1.8879 0.9020 1.1099 -0.1456 -0.3542 -0.2088 182 GLY   N O   
24506 N  N   . VAL   N  183 ? 1.8773 0.8041 1.0868 -0.1076 -0.3643 -0.1828 183 VAL   N N   
24507 C  CA  . VAL   N  183 ? 1.8530 0.7146 1.1384 -0.1136 -0.4086 -0.1809 183 VAL   N CA  
24508 C  C   . VAL   N  183 ? 1.8121 0.8017 1.1531 -0.1220 -0.4340 -0.1767 183 VAL   N C   
24509 O  O   . VAL   N  183 ? 1.8220 0.7993 1.2846 -0.1216 -0.4642 -0.2407 183 VAL   N O   
24510 C  CB  . VAL   N  183 ? 1.8707 0.6510 1.1556 -0.1056 -0.4223 -0.1732 183 VAL   N CB  
24511 C  CG1 . VAL   N  183 ? 1.8594 0.6276 1.1414 -0.0696 -0.3981 -0.1407 183 VAL   N CG1 
24512 C  CG2 . VAL   N  183 ? 1.8435 0.7146 1.1808 -0.0870 -0.4156 -0.2168 183 VAL   N CG2 
24513 N  N   . GLU   N  184 ? 1.8093 0.8083 1.0901 -0.0663 -0.4183 -0.0894 184 GLU   N N   
24514 C  CA  . GLU   N  184 ? 1.8254 0.8089 1.0341 -0.0481 -0.4062 -0.0973 184 GLU   N CA  
24515 C  C   . GLU   N  184 ? 1.7694 0.7306 1.0395 -0.0359 -0.4377 -0.0710 184 GLU   N C   
24516 O  O   . GLU   N  184 ? 1.7044 0.6613 1.0567 -0.0124 -0.3890 -0.0702 184 GLU   N O   
24517 C  CB  . GLU   N  184 ? 1.8916 0.8239 1.0273 -0.0389 -0.3761 -0.1032 184 GLU   N CB  
24518 C  CG  . GLU   N  184 ? 1.9245 0.8320 1.0299 -0.0150 -0.3723 -0.1139 184 GLU   N CG  
24519 C  CD  . GLU   N  184 ? 2.0212 0.9166 0.9963 -0.0486 -0.3470 -0.1283 184 GLU   N CD  
24520 O  OE1 . GLU   N  184 ? 2.0097 0.9909 0.9249 -0.0409 -0.3874 -0.1454 184 GLU   N OE1 
24521 O  OE2 . GLU   N  184 ? 2.0656 0.8853 0.9609 -0.0262 -0.3146 -0.0985 184 GLU   N OE2 
24522 N  N   . ARG   N  185 ? 1.7806 0.7432 1.0313 -0.0055 -0.4570 -0.0526 185 ARG   N N   
24523 C  CA  . ARG   N  185 ? 1.8364 0.7221 1.0335 -0.0443 -0.4762 -0.0713 185 ARG   N CA  
24524 C  C   . ARG   N  185 ? 1.8141 0.7605 0.9583 -0.0583 -0.5230 -0.0736 185 ARG   N C   
24525 O  O   . ARG   N  185 ? 1.8202 0.9026 1.0732 -0.0628 -0.5702 -0.1039 185 ARG   N O   
24526 C  CB  . ARG   N  185 ? 1.8473 0.7250 1.0848 -0.0227 -0.4381 -0.0739 185 ARG   N CB  
24527 C  CG  . ARG   N  185 ? 1.8553 0.7528 1.1249 0.0014  -0.4505 -0.0526 185 ARG   N CG  
24528 C  CD  . ARG   N  185 ? 1.8314 0.7675 1.1608 0.0091  -0.4465 -0.0121 185 ARG   N CD  
24529 N  NE  . ARG   N  185 ? 1.8423 0.7771 1.1946 -0.0143 -0.4689 0.0240  185 ARG   N NE  
24530 C  CZ  . ARG   N  185 ? 1.8438 0.7023 1.2718 -0.0151 -0.4514 -0.0071 185 ARG   N CZ  
24531 N  NH1 . ARG   N  185 ? 1.8700 0.6508 1.3134 0.0886  -0.4704 -0.0317 185 ARG   N NH1 
24532 N  NH2 . ARG   N  185 ? 1.8301 0.8155 1.2385 0.0110  -0.4190 -0.0064 185 ARG   N NH2 
24533 N  N   . LEU   N  186 ? 1.8378 0.7117 0.9814 -0.0666 -0.4553 -0.0096 186 LEU   N N   
24534 C  CA  . LEU   N  186 ? 1.8431 0.7001 0.9690 -0.0833 -0.4170 0.0180  186 LEU   N CA  
24535 C  C   . LEU   N  186 ? 1.8232 0.6593 0.9584 -0.0813 -0.4014 0.0454  186 LEU   N C   
24536 O  O   . LEU   N  186 ? 1.8096 0.6460 0.9104 -0.0998 -0.3721 -0.0614 186 LEU   N O   
24537 C  CB  . LEU   N  186 ? 1.8837 0.6443 0.9803 -0.0460 -0.3973 0.0795  186 LEU   N CB  
24538 C  CG  . LEU   N  186 ? 1.8978 0.5868 0.9798 -0.0558 -0.4108 0.0759  186 LEU   N CG  
24539 C  CD1 . LEU   N  186 ? 1.9117 0.5980 0.9831 -0.0343 -0.3773 0.1045  186 LEU   N CD1 
24540 C  CD2 . LEU   N  186 ? 1.9221 0.5990 0.9988 -0.0662 -0.4347 0.0819  186 LEU   N CD2 
24541 N  N   . ILE   N  187 ? 1.8015 0.6792 0.9330 -0.0897 -0.4179 0.0147  187 ILE   N N   
24542 C  CA  . ILE   N  187 ? 1.8249 0.7297 0.9458 -0.1267 -0.4110 -0.0383 187 ILE   N CA  
24543 C  C   . ILE   N  187 ? 1.8580 0.7630 0.9540 -0.1060 -0.4654 -0.0299 187 ILE   N C   
24544 O  O   . ILE   N  187 ? 1.9519 0.8762 0.9866 -0.0874 -0.5262 -0.0896 187 ILE   N O   
24545 C  CB  . ILE   N  187 ? 1.8479 0.6746 0.9559 -0.1374 -0.4012 -0.0224 187 ILE   N CB  
24546 C  CG1 . ILE   N  187 ? 1.8542 0.6679 1.0090 -0.0982 -0.3410 -0.0046 187 ILE   N CG1 
24547 C  CG2 . ILE   N  187 ? 1.8629 0.6650 0.9708 -0.1797 -0.4057 -0.0517 187 ILE   N CG2 
24548 C  CD1 . ILE   N  187 ? 1.8347 0.6981 1.0730 -0.0923 -0.3271 0.0043  187 ILE   N CD1 
24549 N  N   . PHE   N  188 ? 1.8353 0.7710 1.0374 -0.1169 -0.4426 -0.0573 188 PHE   N N   
24550 C  CA  . PHE   N  188 ? 1.8170 0.7900 1.0380 -0.1065 -0.4356 -0.0219 188 PHE   N CA  
24551 C  C   . PHE   N  188 ? 1.7941 0.7194 1.1815 -0.1214 -0.3780 -0.0451 188 PHE   N C   
24552 O  O   . PHE   N  188 ? 1.7939 0.5967 1.1726 -0.1730 -0.3484 -0.1492 188 PHE   N O   
24553 C  CB  . PHE   N  188 ? 1.8337 0.7498 0.9704 -0.0870 -0.4265 0.0261  188 PHE   N CB  
24554 C  CG  . PHE   N  188 ? 1.8632 0.7984 0.9061 -0.0724 -0.4233 0.0574  188 PHE   N CG  
24555 C  CD1 . PHE   N  188 ? 1.9046 0.8091 0.9073 -0.0680 -0.4265 0.0876  188 PHE   N CD1 
24556 C  CD2 . PHE   N  188 ? 1.8626 0.8338 0.8995 -0.0570 -0.4009 0.0598  188 PHE   N CD2 
24557 C  CE1 . PHE   N  188 ? 1.9424 0.8344 0.9312 -0.0712 -0.4081 0.0685  188 PHE   N CE1 
24558 C  CE2 . PHE   N  188 ? 1.8943 0.8339 0.8497 -0.0774 -0.4390 0.0450  188 PHE   N CE2 
24559 C  CZ  . PHE   N  188 ? 1.9452 0.8322 0.8387 -0.0736 -0.4318 0.0580  188 PHE   N CZ  
24560 N  N   . TYR   N  189 ? 1.7794 0.7908 1.1553 -0.1300 -0.4037 -0.0177 189 TYR   N N   
24561 C  CA  . TYR   N  189 ? 1.7481 0.9456 1.1973 -0.0883 -0.3801 -0.0157 189 TYR   N CA  
24562 C  C   . TYR   N  189 ? 1.8144 0.9703 1.2659 -0.1134 -0.3524 -0.0329 189 TYR   N C   
24563 O  O   . TYR   N  189 ? 1.8359 1.2336 1.1994 -0.0536 -0.3389 -0.0027 189 TYR   N O   
24564 C  CB  . TYR   N  189 ? 1.7577 0.9589 1.2184 -0.0996 -0.4056 0.0072  189 TYR   N CB  
24565 C  CG  . TYR   N  189 ? 1.7200 0.9738 1.2035 -0.0981 -0.4363 -0.0161 189 TYR   N CG  
24566 C  CD1 . TYR   N  189 ? 1.7104 1.0041 1.2340 -0.0814 -0.4313 0.0136  189 TYR   N CD1 
24567 C  CD2 . TYR   N  189 ? 1.7136 1.0687 1.1452 -0.0787 -0.4693 0.0141  189 TYR   N CD2 
24568 C  CE1 . TYR   N  189 ? 1.7422 0.9913 1.2134 -0.0574 -0.4583 -0.0003 189 TYR   N CE1 
24569 C  CE2 . TYR   N  189 ? 1.7288 1.0722 1.1239 -0.0758 -0.4960 0.0031  189 TYR   N CE2 
24570 C  CZ  . TYR   N  189 ? 1.7466 0.9507 1.2022 -0.0867 -0.4905 0.0169  189 TYR   N CZ  
24571 O  OH  . TYR   N  189 ? 1.7841 0.9162 1.2281 -0.0513 -0.5059 -0.0014 189 TYR   N OH  
24572 N  N   . PRO   N  190 ? 1.8478 0.9808 1.3427 -0.1419 -0.2761 -0.0764 190 PRO   N N   
24573 C  CA  . PRO   N  190 ? 1.8424 0.9732 1.3483 -0.1490 -0.2786 -0.0679 190 PRO   N CA  
24574 C  C   . PRO   N  190 ? 1.8068 0.8995 1.4014 -0.1530 -0.3448 -0.0680 190 PRO   N C   
24575 O  O   . PRO   N  190 ? 1.7984 0.9671 1.3480 -0.1289 -0.3239 -0.0180 190 PRO   N O   
24576 C  CB  . PRO   N  190 ? 1.8333 1.0203 1.4024 -0.1803 -0.2360 -0.0743 190 PRO   N CB  
24577 C  CG  . PRO   N  190 ? 1.8256 1.0015 1.3743 -0.1625 -0.2308 -0.1076 190 PRO   N CG  
24578 C  CD  . PRO   N  190 ? 1.8363 0.9902 1.3666 -0.1358 -0.2399 -0.1008 190 PRO   N CD  
24579 N  N   . ASP   N  191 ? 1.8056 0.8946 1.4640 -0.1443 -0.3702 -0.0553 191 ASP   N N   
24580 C  CA  . ASP   N  191 ? 1.7767 1.0089 1.4711 -0.1821 -0.3787 -0.0059 191 ASP   N CA  
24581 C  C   . ASP   N  191 ? 1.8320 1.0341 1.3999 -0.1080 -0.4003 -0.0005 191 ASP   N C   
24582 O  O   . ASP   N  191 ? 1.8402 1.1617 1.3500 -0.1103 -0.4235 0.0534  191 ASP   N O   
24583 C  CB  . ASP   N  191 ? 1.7784 1.1018 1.6093 -0.2580 -0.3476 -0.0458 191 ASP   N CB  
24584 C  CG  . ASP   N  191 ? 1.6931 1.1301 1.7367 -0.3262 -0.3134 -0.0863 191 ASP   N CG  
24585 O  OD1 . ASP   N  191 ? 1.6790 1.1615 1.7345 -0.2761 -0.2862 -0.1438 191 ASP   N OD1 
24586 O  OD2 . ASP   N  191 ? 1.5961 1.3473 1.8722 -0.4364 -0.2836 -0.0785 191 ASP   N OD2 
24587 N  N   . GLU   N  192 ? 1.9275 0.9651 1.3036 -0.0985 -0.4044 0.1060  192 GLU   N N   
24588 C  CA  . GLU   N  192 ? 2.0133 1.0468 1.2829 -0.0426 -0.3756 0.1506  192 GLU   N CA  
24589 C  C   . GLU   N  192 ? 2.0292 1.0097 1.2307 -0.0339 -0.3762 0.1323  192 GLU   N C   
24590 O  O   . GLU   N  192 ? 2.0609 1.1705 1.1202 -0.1289 -0.3252 0.1282  192 GLU   N O   
24591 C  CB  . GLU   N  192 ? 2.1019 1.0623 1.3116 0.0359  -0.3835 0.1769  192 GLU   N CB  
24592 C  CG  . GLU   N  192 ? 2.1623 1.2049 1.3552 0.0643  -0.3349 0.2355  192 GLU   N CG  
24593 C  CD  . GLU   N  192 ? 2.2792 1.2808 1.3988 0.1412  -0.3334 0.1684  192 GLU   N CD  
24594 O  OE1 . GLU   N  192 ? 2.3631 1.4241 1.3579 0.1076  -0.2687 0.2460  192 GLU   N OE1 
24595 O  OE2 . GLU   N  192 ? 2.2981 1.4475 1.5035 0.0565  -0.3556 0.2226  192 GLU   N OE2 
24596 N  N   . TYR   N  193 ? 1.9843 0.9572 1.2741 0.0036  -0.3693 0.1336  193 TYR   N N   
24597 C  CA  . TYR   N  193 ? 1.9376 0.9775 1.3546 0.0297  -0.2992 0.1360  193 TYR   N CA  
24598 C  C   . TYR   N  193 ? 1.9563 0.9493 1.3758 0.0204  -0.2743 0.1680  193 TYR   N C   
24599 O  O   . TYR   N  193 ? 1.9982 0.9076 1.3076 0.0063  -0.2583 0.2517  193 TYR   N O   
24600 C  CB  . TYR   N  193 ? 1.9136 0.9243 1.3187 0.0136  -0.2427 0.1246  193 TYR   N CB  
24601 C  CG  . TYR   N  193 ? 1.8470 0.8560 1.3118 0.0238  -0.2541 0.1261  193 TYR   N CG  
24602 C  CD1 . TYR   N  193 ? 1.8140 0.8337 1.2909 0.0638  -0.2374 0.1255  193 TYR   N CD1 
24603 C  CD2 . TYR   N  193 ? 1.8097 0.8883 1.3153 -0.0102 -0.2569 0.0742  193 TYR   N CD2 
24604 C  CE1 . TYR   N  193 ? 1.7862 0.9065 1.3118 0.0549  -0.2068 0.1020  193 TYR   N CE1 
24605 C  CE2 . TYR   N  193 ? 1.7987 0.9215 1.3300 0.0135  -0.2260 0.0284  193 TYR   N CE2 
24606 C  CZ  . TYR   N  193 ? 1.7847 0.9025 1.3611 0.0193  -0.2009 0.0192  193 TYR   N CZ  
24607 O  OH  . TYR   N  193 ? 1.8117 1.0893 1.3933 0.0710  -0.1526 -0.0100 193 TYR   N OH  
24608 N  N   . GLU   N  194 ? 2.0008 0.9400 1.4187 0.0805  -0.2807 0.1611  194 GLU   N N   
24609 C  CA  . GLU   N  194 ? 2.0469 0.8793 1.5397 0.1300  -0.2528 0.1656  194 GLU   N CA  
24610 C  C   . GLU   N  194 ? 2.0717 0.9771 1.5570 0.1656  -0.2640 0.2399  194 GLU   N C   
24611 O  O   . GLU   N  194 ? 2.0559 1.0876 1.7414 0.1415  -0.2640 0.1631  194 GLU   N O   
24612 C  CB  . GLU   N  194 ? 2.0964 0.7675 1.6101 0.1752  -0.2363 0.0783  194 GLU   N CB  
24613 C  CG  . GLU   N  194 ? 2.2246 0.7914 1.5708 0.1922  -0.1908 0.0013  194 GLU   N CG  
24614 C  CD  . GLU   N  194 ? 2.2542 0.7880 1.6628 0.3051  -0.2214 -0.0818 194 GLU   N CD  
24615 O  OE1 . GLU   N  194 ? 2.4863 0.7601 1.5080 0.3312  -0.1945 -0.2029 194 GLU   N OE1 
24616 O  OE2 . GLU   N  194 ? 2.2262 0.9234 1.7227 0.2946  -0.3059 0.0271  194 GLU   N OE2 
24617 N  N   . GLN   N  195 ? 2.0586 1.0593 1.5785 0.1311  -0.3024 0.2767  195 GLN   N N   
24618 C  CA  . GLN   N  195 ? 2.1121 1.1721 1.5857 0.1556  -0.3535 0.3617  195 GLN   N CA  
24619 C  C   . GLN   N  195 ? 2.1349 1.0254 1.5898 0.2038  -0.3550 0.4077  195 GLN   N C   
24620 O  O   . GLN   N  195 ? 2.1260 1.3079 1.5947 0.2735  -0.4576 0.4945  195 GLN   N O   
24621 C  CB  . GLN   N  195 ? 2.1038 1.3420 1.6212 0.1331  -0.3579 0.4052  195 GLN   N CB  
24622 C  CG  . GLN   N  195 ? 2.2381 1.3749 1.6506 0.1123  -0.3150 0.3477  195 GLN   N CG  
24623 C  CD  . GLN   N  195 ? 2.2463 1.6117 1.6850 0.0680  -0.3556 0.2523  195 GLN   N CD  
24624 O  OE1 . GLN   N  195 ? 2.2889 1.8196 1.8921 0.1246  -0.2295 0.1884  195 GLN   N OE1 
24625 N  NE2 . GLN   N  195 ? 2.3577 1.6427 1.6778 0.0737  -0.3006 0.2023  195 GLN   N NE2 
24626 N  N   . LEU   N  196 ? 2.2245 0.8033 1.5728 0.1766  -0.3206 0.3243  196 LEU   N N   
24627 C  CA  . LEU   N  196 ? 2.2997 0.7895 1.4982 0.1677  -0.2866 0.3212  196 LEU   N CA  
24628 C  C   . LEU   N  196 ? 2.3492 0.7637 1.5060 0.1488  -0.2394 0.4160  196 LEU   N C   
24629 O  O   . LEU   N  196 ? 2.4314 0.9137 1.4875 0.1538  -0.2774 0.3910  196 LEU   N O   
24630 C  CB  . LEU   N  196 ? 2.2239 0.7795 1.4306 0.1622  -0.3166 0.2594  196 LEU   N CB  
24631 C  CG  . LEU   N  196 ? 2.2148 0.6999 1.3642 0.2323  -0.3259 0.2695  196 LEU   N CG  
24632 C  CD1 . LEU   N  196 ? 2.2030 0.6172 1.3287 0.1879  -0.3006 0.2364  196 LEU   N CD1 
24633 C  CD2 . LEU   N  196 ? 2.2196 0.6346 1.3730 0.2122  -0.3202 0.2341  196 LEU   N CD2 
24634 O  OXT . LEU   N  196 ? 2.4980 0.8527 1.4470 0.1967  -0.1692 0.3931  196 LEU   N OXT 
24635 N  N   . MET   O  1   ? 2.3810 1.3999 2.4510 0.3312  0.0011  0.0732  1   MET   O N   
24636 C  CA  . MET   O  1   ? 2.3699 1.4370 2.4904 0.2944  -0.0078 0.1267  1   MET   O CA  
24637 C  C   . MET   O  1   ? 2.3791 1.2755 2.4851 0.2017  -0.1052 0.0015  1   MET   O C   
24638 O  O   . MET   O  1   ? 2.0840 0.7660 2.5445 0.3504  -0.1497 -0.0835 1   MET   O O   
24639 C  CB  . MET   O  1   ? 2.5091 1.7244 2.3786 0.2852  0.0921  0.1299  1   MET   O CB  
24640 C  CG  . MET   O  1   ? 2.7141 1.8998 2.4398 0.1598  0.1670  0.3235  1   MET   O CG  
24641 S  SD  . MET   O  1   ? 2.8126 1.9452 2.4998 0.1616  0.3808  0.3778  1   MET   O SD  
24642 C  CE  . MET   O  1   ? 2.9355 1.8118 2.6267 0.1489  0.3846  0.2370  1   MET   O CE  
24643 N  N   . THR   O  2   ? 2.2316 1.3293 2.3758 0.1249  -0.2251 -0.0090 2   THR   O N   
24644 C  CA  . THR   O  2   ? 2.2833 1.1083 2.2086 -0.1032 -0.2954 -0.0069 2   THR   O CA  
24645 C  C   . THR   O  2   ? 2.2383 0.8803 2.1701 0.0833  -0.3337 0.0303  2   THR   O C   
24646 O  O   . THR   O  2   ? 2.4466 0.3693 2.2164 -0.1676 -0.4450 0.1753  2   THR   O O   
24647 C  CB  . THR   O  2   ? 2.3244 1.1098 2.2352 -0.0770 -0.2772 0.0271  2   THR   O CB  
24648 O  OG1 . THR   O  2   ? 2.4043 1.2100 2.2665 -0.1658 -0.2035 -0.0276 2   THR   O OG1 
24649 C  CG2 . THR   O  2   ? 2.3253 0.9118 2.1791 -0.1431 -0.2824 0.0389  2   THR   O CG2 
24650 N  N   . ASP   O  3   ? 2.2393 1.0607 1.9898 -0.1001 -0.4115 0.0395  3   ASP   O N   
24651 C  CA  . ASP   O  3   ? 2.2237 0.9331 1.8888 -0.0761 -0.4153 0.1286  3   ASP   O CA  
24652 C  C   . ASP   O  3   ? 2.1986 0.9550 1.9222 -0.0715 -0.3956 0.1107  3   ASP   O C   
24653 O  O   . ASP   O  3   ? 2.3807 1.2245 1.8830 -0.0395 -0.4037 0.1695  3   ASP   O O   
24654 C  CB  . ASP   O  3   ? 2.2015 0.8559 1.8388 -0.1308 -0.4715 0.1128  3   ASP   O CB  
24655 C  CG  . ASP   O  3   ? 2.2296 0.8349 1.8526 -0.1225 -0.5328 0.1368  3   ASP   O CG  
24656 O  OD1 . ASP   O  3   ? 2.1514 0.9490 1.8248 -0.0094 -0.5414 0.1342  3   ASP   O OD1 
24657 O  OD2 . ASP   O  3   ? 2.2476 0.5923 1.8724 -0.0880 -0.5702 0.0862  3   ASP   O OD2 
24658 N  N   . ARG   O  4   ? 2.0884 1.0299 1.8516 -0.0487 -0.3818 0.2198  4   ARG   O N   
24659 C  CA  . ARG   O  4   ? 1.9721 1.1794 1.8579 -0.0860 -0.3746 0.2145  4   ARG   O CA  
24660 C  C   . ARG   O  4   ? 1.9449 1.0735 1.7656 -0.0529 -0.3137 0.1833  4   ARG   O C   
24661 O  O   . ARG   O  4   ? 1.9431 1.1252 1.7762 -0.1132 -0.3040 0.1421  4   ARG   O O   
24662 C  CB  . ARG   O  4   ? 1.9315 1.3953 1.9619 -0.0547 -0.3734 0.2944  4   ARG   O CB  
24663 C  CG  . ARG   O  4   ? 1.8490 1.5588 2.0607 -0.0266 -0.4334 0.3415  4   ARG   O CG  
24664 C  CD  . ARG   O  4   ? 1.8395 1.5798 2.2592 -0.0182 -0.4371 0.4156  4   ARG   O CD  
24665 N  NE  . ARG   O  4   ? 1.8240 1.7186 2.2846 -0.0185 -0.4330 0.4363  4   ARG   O NE  
24666 C  CZ  . ARG   O  4   ? 1.6868 1.7772 2.4852 0.0129  -0.4610 0.5019  4   ARG   O CZ  
24667 N  NH1 . ARG   O  4   ? 1.7017 1.7754 2.5202 0.0108  -0.4787 0.5506  4   ARG   O NH1 
24668 N  NH2 . ARG   O  4   ? 1.6524 1.8271 2.4838 -0.0205 -0.4358 0.4962  4   ARG   O NH2 
24669 N  N   . TYR   O  5   ? 1.8529 0.8500 1.6816 -0.0520 -0.4099 0.0795  5   TYR   O N   
24670 C  CA  . TYR   O  5   ? 1.8703 0.7604 1.6560 -0.0196 -0.4037 0.0489  5   TYR   O CA  
24671 C  C   . TYR   O  5   ? 1.8189 0.6975 1.6512 0.0005  -0.3727 -0.0055 5   TYR   O C   
24672 O  O   . TYR   O  5   ? 1.8438 0.6693 1.6598 -0.0208 -0.3232 -0.0557 5   TYR   O O   
24673 C  CB  . TYR   O  5   ? 1.8677 0.7538 1.6155 -0.0150 -0.4347 0.0579  5   TYR   O CB  
24674 C  CG  . TYR   O  5   ? 1.9031 0.7703 1.5445 -0.0274 -0.4924 0.0402  5   TYR   O CG  
24675 C  CD1 . TYR   O  5   ? 1.9253 0.7655 1.5171 -0.0137 -0.4943 0.0570  5   TYR   O CD1 
24676 C  CD2 . TYR   O  5   ? 1.9373 0.7141 1.5692 -0.0040 -0.5017 0.1104  5   TYR   O CD2 
24677 C  CE1 . TYR   O  5   ? 1.9771 0.7356 1.4944 -0.0306 -0.5285 0.0336  5   TYR   O CE1 
24678 C  CE2 . TYR   O  5   ? 1.9918 0.7043 1.5212 -0.0361 -0.5368 0.1029  5   TYR   O CE2 
24679 C  CZ  . TYR   O  5   ? 2.0269 0.6986 1.5137 -0.0435 -0.5428 0.0915  5   TYR   O CZ  
24680 O  OH  . TYR   O  5   ? 2.0804 0.7302 1.4410 -0.0820 -0.6197 0.0967  5   TYR   O OH  
24681 N  N   . SER   O  6   ? 1.7981 0.7410 1.6429 0.0010  -0.3793 -0.0088 6   SER   O N   
24682 C  CA  . SER   O  6   ? 1.7603 0.7795 1.6327 0.0152  -0.4131 -0.0282 6   SER   O CA  
24683 C  C   . SER   O  6   ? 1.7885 0.6431 1.6295 0.0319  -0.4221 -0.0001 6   SER   O C   
24684 O  O   . SER   O  6   ? 1.7832 0.6592 1.5873 0.0497  -0.4554 -0.0573 6   SER   O O   
24685 C  CB  . SER   O  6   ? 1.7110 0.8596 1.7001 0.0256  -0.3810 -0.0110 6   SER   O CB  
24686 O  OG  . SER   O  6   ? 1.6958 1.0332 1.7767 0.0568  -0.3621 -0.0276 6   SER   O OG  
24687 N  N   . PHE   O  7   ? 1.8099 0.6456 1.5403 0.0046  -0.4599 0.0385  7   PHE   O N   
24688 C  CA  . PHE   O  7   ? 1.7715 0.4979 1.5592 0.0123  -0.4618 0.0811  7   PHE   O CA  
24689 C  C   . PHE   O  7   ? 1.7717 0.3512 1.4935 -0.0058 -0.5077 0.0027  7   PHE   O C   
24690 O  O   . PHE   O  7   ? 1.7778 0.4047 1.4830 -0.0175 -0.5037 -0.0566 7   PHE   O O   
24691 C  CB  . PHE   O  7   ? 1.7457 0.4949 1.5542 0.0134  -0.4739 0.1034  7   PHE   O CB  
24692 C  CG  . PHE   O  7   ? 1.7069 0.5580 1.5805 0.0177  -0.4801 0.1295  7   PHE   O CG  
24693 C  CD1 . PHE   O  7   ? 1.7051 0.5359 1.5422 0.0558  -0.5258 0.1796  7   PHE   O CD1 
24694 C  CD2 . PHE   O  7   ? 1.6939 0.6163 1.5617 0.0609  -0.5085 0.1655  7   PHE   O CD2 
24695 C  CE1 . PHE   O  7   ? 1.7009 0.5036 1.5797 0.0693  -0.5171 0.1991  7   PHE   O CE1 
24696 C  CE2 . PHE   O  7   ? 1.7171 0.5533 1.5943 0.0604  -0.4942 0.1906  7   PHE   O CE2 
24697 C  CZ  . PHE   O  7   ? 1.6980 0.5172 1.5917 0.0830  -0.5238 0.1958  7   PHE   O CZ  
24698 N  N   . SER   O  8   ? 1.8094 0.2478 1.5020 0.0039  -0.5090 -0.0235 8   SER   O N   
24699 C  CA  . SER   O  8   ? 1.8106 0.3324 1.4947 -0.0186 -0.5165 -0.0314 8   SER   O CA  
24700 C  C   . SER   O  8   ? 1.8297 0.4946 1.4205 -0.0293 -0.4959 0.0997  8   SER   O C   
24701 O  O   . SER   O  8   ? 1.8274 0.5635 1.4387 0.0356  -0.5114 0.1612  8   SER   O O   
24702 C  CB  . SER   O  8   ? 1.7853 0.2035 1.5360 0.0000  -0.5364 -0.0569 8   SER   O CB  
24703 O  OG  . SER   O  8   ? 1.7753 0.1986 1.5935 -0.0349 -0.5209 -0.1437 8   SER   O OG  
24704 N  N   . LEU   O  9   ? 1.8624 0.5635 1.4028 -0.0523 -0.4947 0.1321  9   LEU   O N   
24705 C  CA  . LEU   O  9   ? 1.8328 0.5139 1.4042 -0.0319 -0.4879 0.0953  9   LEU   O CA  
24706 C  C   . LEU   O  9   ? 1.8304 0.4703 1.3298 0.0009  -0.4952 0.0781  9   LEU   O C   
24707 O  O   . LEU   O  9   ? 1.8748 0.5288 1.2792 0.0152  -0.5449 0.1669  9   LEU   O O   
24708 C  CB  . LEU   O  9   ? 1.8480 0.5371 1.3998 -0.0367 -0.4877 0.1142  9   LEU   O CB  
24709 C  CG  . LEU   O  9   ? 1.8460 0.5530 1.4270 -0.0376 -0.4822 0.0955  9   LEU   O CG  
24710 C  CD1 . LEU   O  9   ? 1.8735 0.5364 1.4480 -0.0324 -0.4279 0.1097  9   LEU   O CD1 
24711 C  CD2 . LEU   O  9   ? 1.8717 0.5561 1.4228 -0.0204 -0.4535 0.0840  9   LEU   O CD2 
24712 N  N   . THR   O  10  ? 1.7683 0.4379 1.3356 -0.0298 -0.4591 0.1015  10  THR   O N   
24713 C  CA  . THR   O  10  ? 1.7625 0.4437 1.3586 -0.0626 -0.4246 0.0912  10  THR   O CA  
24714 C  C   . THR   O  10  ? 1.7246 0.4474 1.3433 -0.0694 -0.4563 0.1103  10  THR   O C   
24715 O  O   . THR   O  10  ? 1.6799 0.3815 1.2447 -0.0866 -0.4941 0.0229  10  THR   O O   
24716 C  CB  . THR   O  10  ? 1.7450 0.4630 1.3663 -0.0895 -0.3983 0.1103  10  THR   O CB  
24717 O  OG1 . THR   O  10  ? 1.7830 0.5913 1.3733 -0.1092 -0.3190 0.1520  10  THR   O OG1 
24718 C  CG2 . THR   O  10  ? 1.7557 0.5051 1.3314 -0.0907 -0.4195 0.1075  10  THR   O CG2 
24719 N  N   . THR   O  11  ? 1.7244 0.5016 1.3554 -0.0572 -0.4580 0.0660  11  THR   O N   
24720 C  CA  . THR   O  11  ? 1.7705 0.5254 1.3667 -0.0502 -0.4294 0.1077  11  THR   O CA  
24721 C  C   . THR   O  11  ? 1.8133 0.5276 1.4224 -0.0480 -0.4332 0.0742  11  THR   O C   
24722 O  O   . THR   O  11  ? 1.8708 0.5766 1.5627 -0.0419 -0.3498 0.1212  11  THR   O O   
24723 C  CB  . THR   O  11  ? 1.7688 0.5489 1.3882 -0.0523 -0.4452 0.1067  11  THR   O CB  
24724 O  OG1 . THR   O  11  ? 1.7464 0.4934 1.4389 -0.0909 -0.4725 0.0692  11  THR   O OG1 
24725 C  CG2 . THR   O  11  ? 1.7584 0.5445 1.3806 -0.0543 -0.4416 0.1197  11  THR   O CG2 
24726 N  N   . PHE   O  12  ? 1.8488 0.5308 1.4155 -0.0320 -0.4214 0.0892  12  PHE   O N   
24727 C  CA  . PHE   O  12  ? 1.8845 0.5256 1.4436 -0.0265 -0.4189 0.0615  12  PHE   O CA  
24728 C  C   . PHE   O  12  ? 1.9410 0.5060 1.4570 -0.0215 -0.3863 0.0777  12  PHE   O C   
24729 O  O   . PHE   O  12  ? 1.9424 0.4409 1.4464 0.0165  -0.3766 0.0897  12  PHE   O O   
24730 C  CB  . PHE   O  12  ? 1.8762 0.5428 1.4351 -0.0662 -0.4275 0.0458  12  PHE   O CB  
24731 C  CG  . PHE   O  12  ? 1.8697 0.4653 1.4063 -0.1143 -0.4258 0.0485  12  PHE   O CG  
24732 C  CD1 . PHE   O  12  ? 1.8685 0.4278 1.3884 -0.1156 -0.4351 0.0445  12  PHE   O CD1 
24733 C  CD2 . PHE   O  12  ? 1.8752 0.4539 1.3686 -0.0919 -0.4199 0.0806  12  PHE   O CD2 
24734 C  CE1 . PHE   O  12  ? 1.8684 0.4189 1.3431 -0.1206 -0.4412 0.0576  12  PHE   O CE1 
24735 C  CE2 . PHE   O  12  ? 1.8434 0.5052 1.3530 -0.0755 -0.4171 0.0821  12  PHE   O CE2 
24736 C  CZ  . PHE   O  12  ? 1.8518 0.4412 1.3352 -0.1315 -0.4267 0.0757  12  PHE   O CZ  
24737 N  N   . SER   O  13  ? 1.9666 0.4923 1.5396 -0.0338 -0.3266 0.0206  13  SER   O N   
24738 C  CA  . SER   O  13  ? 2.0085 0.4752 1.5697 -0.0699 -0.2931 -0.0406 13  SER   O CA  
24739 C  C   . SER   O  13  ? 1.9643 0.4365 1.5764 -0.0685 -0.3196 -0.0447 13  SER   O C   
24740 O  O   . SER   O  13  ? 1.8836 0.4412 1.5126 -0.1457 -0.3464 -0.0889 13  SER   O O   
24741 C  CB  . SER   O  13  ? 2.0378 0.4668 1.6493 -0.0273 -0.2264 -0.0164 13  SER   O CB  
24742 O  OG  . SER   O  13  ? 2.0396 0.4585 1.7041 0.0305  -0.2151 -0.0217 13  SER   O OG  
24743 N  N   . PRO   O  14  ? 2.0266 0.4236 1.5410 -0.0758 -0.3327 -0.0794 14  PRO   O N   
24744 C  CA  . PRO   O  14  ? 2.0579 0.3351 1.5726 -0.0912 -0.3276 -0.1221 14  PRO   O CA  
24745 C  C   . PRO   O  14  ? 2.0633 0.2279 1.5577 -0.0980 -0.3112 -0.1394 14  PRO   O C   
24746 O  O   . PRO   O  14  ? 2.0839 0.2049 1.5602 -0.0950 -0.2960 -0.1044 14  PRO   O O   
24747 C  CB  . PRO   O  14  ? 2.0599 0.3598 1.5848 -0.0734 -0.3444 -0.1453 14  PRO   O CB  
24748 C  CG  . PRO   O  14  ? 2.0469 0.4268 1.5914 -0.0621 -0.3395 -0.1358 14  PRO   O CG  
24749 C  CD  . PRO   O  14  ? 2.0348 0.4414 1.5829 -0.0273 -0.3094 -0.0933 14  PRO   O CD  
24750 N  N   . SER   O  15  ? 2.0883 0.2675 1.5868 -0.0874 -0.2709 -0.1447 15  SER   O N   
24751 C  CA  . SER   O  15  ? 2.0855 0.4085 1.5886 -0.0928 -0.2728 -0.1290 15  SER   O CA  
24752 C  C   . SER   O  15  ? 2.0513 0.4609 1.5528 -0.0747 -0.2923 -0.0750 15  SER   O C   
24753 O  O   . SER   O  15  ? 2.0858 0.4981 1.4847 -0.1275 -0.3127 -0.0233 15  SER   O O   
24754 C  CB  . SER   O  15  ? 2.0914 0.4234 1.5555 -0.1037 -0.2579 -0.1563 15  SER   O CB  
24755 O  OG  . SER   O  15  ? 2.1174 0.2929 1.5669 -0.0777 -0.1734 -0.2368 15  SER   O OG  
24756 N  N   . GLY   O  16  ? 2.0165 0.4659 1.5426 -0.0867 -0.2926 -0.0491 16  GLY   O N   
24757 C  CA  . GLY   O  16  ? 1.9701 0.5052 1.5256 -0.0631 -0.3048 0.0153  16  GLY   O CA  
24758 C  C   . GLY   O  16  ? 1.9316 0.5130 1.5389 -0.0530 -0.3041 0.0114  16  GLY   O C   
24759 O  O   . GLY   O  16  ? 1.8825 0.4462 1.5597 -0.1562 -0.2828 -0.0127 16  GLY   O O   
24760 N  N   . LYS   O  17  ? 1.9539 0.6510 1.5073 -0.0437 -0.3168 0.0450  17  LYS   O N   
24761 C  CA  . LYS   O  17  ? 1.9212 0.7474 1.5082 -0.0160 -0.3290 0.0311  17  LYS   O CA  
24762 C  C   . LYS   O  17  ? 1.8722 0.6443 1.4628 0.0484  -0.3371 0.0689  17  LYS   O C   
24763 O  O   . LYS   O  17  ? 1.8590 0.6036 1.3915 0.0147  -0.3639 0.0702  17  LYS   O O   
24764 C  CB  . LYS   O  17  ? 1.9630 0.8756 1.5480 -0.0626 -0.2902 0.1167  17  LYS   O CB  
24765 C  CG  . LYS   O  17  ? 2.0433 0.9626 1.6133 -0.0757 -0.2827 0.0518  17  LYS   O CG  
24766 C  CD  . LYS   O  17  ? 2.0368 1.1900 1.6713 -0.0671 -0.3008 0.0889  17  LYS   O CD  
24767 C  CE  . LYS   O  17  ? 2.0725 1.2208 1.7576 -0.1049 -0.2725 0.1057  17  LYS   O CE  
24768 N  NZ  . LYS   O  17  ? 2.0567 1.3617 1.7797 -0.0798 -0.2433 0.0885  17  LYS   O NZ  
24769 N  N   . LEU   O  18  ? 1.8700 0.5749 1.5130 0.0816  -0.3509 0.0911  18  LEU   O N   
24770 C  CA  . LEU   O  18  ? 1.8660 0.6091 1.5789 0.0707  -0.3211 0.0449  18  LEU   O CA  
24771 C  C   . LEU   O  18  ? 1.8720 0.5805 1.5909 0.1157  -0.2895 0.0438  18  LEU   O C   
24772 O  O   . LEU   O  18  ? 1.9589 0.7282 1.6391 0.0983  -0.2103 0.0206  18  LEU   O O   
24773 C  CB  . LEU   O  18  ? 1.8604 0.6279 1.5838 0.0895  -0.3205 0.0675  18  LEU   O CB  
24774 C  CG  . LEU   O  18  ? 1.8719 0.6989 1.5732 0.0585  -0.2835 0.0506  18  LEU   O CG  
24775 C  CD1 . LEU   O  18  ? 1.8736 0.7242 1.6225 0.0751  -0.2660 0.0691  18  LEU   O CD1 
24776 C  CD2 . LEU   O  18  ? 1.8646 0.7041 1.5642 0.0654  -0.2827 0.0465  18  LEU   O CD2 
24777 N  N   . GLY   O  19  ? 1.8821 0.4668 1.5634 0.0759  -0.3203 0.0297  19  GLY   O N   
24778 C  CA  . GLY   O  19  ? 1.8486 0.4092 1.5485 0.0446  -0.3387 -0.0057 19  GLY   O CA  
24779 C  C   . GLY   O  19  ? 1.8052 0.3841 1.5682 0.0704  -0.3481 -0.0068 19  GLY   O C   
24780 O  O   . GLY   O  19  ? 1.7856 0.2759 1.6286 0.0000  -0.3779 -0.0785 19  GLY   O O   
24781 N  N   . GLN   O  20  ? 1.7789 0.3460 1.5700 0.1164  -0.3710 0.0069  20  GLN   O N   
24782 C  CA  . GLN   O  20  ? 1.7991 0.3823 1.5446 0.1224  -0.3685 0.0279  20  GLN   O CA  
24783 C  C   . GLN   O  20  ? 1.7847 0.3445 1.5378 0.0876  -0.3791 0.0339  20  GLN   O C   
24784 O  O   . GLN   O  20  ? 1.7735 0.2863 1.5179 0.0860  -0.4070 0.0393  20  GLN   O O   
24785 C  CB  . GLN   O  20  ? 1.7587 0.3896 1.5601 0.1360  -0.3592 0.0674  20  GLN   O CB  
24786 C  CG  . GLN   O  20  ? 1.7622 0.4711 1.5969 0.1706  -0.3287 0.0661  20  GLN   O CG  
24787 C  CD  . GLN   O  20  ? 1.8003 0.4206 1.6203 0.1995  -0.3100 0.0748  20  GLN   O CD  
24788 O  OE1 . GLN   O  20  ? 1.8409 0.5289 1.5873 0.1817  -0.3310 0.0524  20  GLN   O OE1 
24789 N  NE2 . GLN   O  20  ? 1.8553 0.3597 1.6307 0.1723  -0.2954 0.1154  20  GLN   O NE2 
24790 N  N   . ILE   O  21  ? 1.8677 0.3945 1.4674 0.0351  -0.3783 0.0104  21  ILE   O N   
24791 C  CA  . ILE   O  21  ? 1.8597 0.4828 1.4311 0.0172  -0.3732 -0.0009 21  ILE   O CA  
24792 C  C   . ILE   O  21  ? 1.8506 0.5064 1.4183 -0.0022 -0.3722 -0.0269 21  ILE   O C   
24793 O  O   . ILE   O  21  ? 1.8190 0.4888 1.4256 0.0252  -0.3903 -0.0771 21  ILE   O O   
24794 C  CB  . ILE   O  21  ? 1.9135 0.5073 1.4122 -0.0229 -0.3637 0.0137  21  ILE   O CB  
24795 C  CG1 . ILE   O  21  ? 1.9017 0.5310 1.4107 -0.0325 -0.3470 0.0447  21  ILE   O CG1 
24796 C  CG2 . ILE   O  21  ? 1.9087 0.4738 1.4049 -0.0593 -0.3621 0.0118  21  ILE   O CG2 
24797 C  CD1 . ILE   O  21  ? 1.9183 0.5331 1.4037 -0.0538 -0.3270 0.0370  21  ILE   O CD1 
24798 N  N   . ASP   O  22  ? 1.8845 0.5382 1.4196 0.0132  -0.3801 -0.0477 22  ASP   O N   
24799 C  CA  . ASP   O  22  ? 1.8872 0.5752 1.4381 -0.0047 -0.3794 -0.0226 22  ASP   O CA  
24800 C  C   . ASP   O  22  ? 1.8273 0.5450 1.4378 0.0190  -0.3979 -0.0281 22  ASP   O C   
24801 O  O   . ASP   O  22  ? 1.8209 0.5684 1.4500 0.0555  -0.3906 0.0163  22  ASP   O O   
24802 C  CB  . ASP   O  22  ? 1.9454 0.7029 1.4316 0.0134  -0.3617 -0.0802 22  ASP   O CB  
24803 C  CG  . ASP   O  22  ? 1.9858 0.7684 1.4369 -0.0091 -0.3743 -0.0689 22  ASP   O CG  
24804 O  OD1 . ASP   O  22  ? 2.0112 0.6962 1.3848 -0.0155 -0.3612 -0.1031 22  ASP   O OD1 
24805 O  OD2 . ASP   O  22  ? 2.0588 0.9197 1.4820 -0.0719 -0.3080 -0.1682 22  ASP   O OD2 
24806 N  N   . TYR   O  23  ? 1.8417 0.4859 1.3684 0.0189  -0.4083 -0.0178 23  TYR   O N   
24807 C  CA  . TYR   O  23  ? 1.8234 0.5348 1.3867 0.0169  -0.4222 0.0124  23  TYR   O CA  
24808 C  C   . TYR   O  23  ? 1.8233 0.5071 1.3738 0.0519  -0.4446 0.0474  23  TYR   O C   
24809 O  O   . TYR   O  23  ? 1.8491 0.5266 1.4136 0.0668  -0.4584 0.1184  23  TYR   O O   
24810 C  CB  . TYR   O  23  ? 1.8071 0.5421 1.3873 0.0220  -0.3807 -0.0138 23  TYR   O CB  
24811 C  CG  . TYR   O  23  ? 1.7615 0.5414 1.4319 0.0203  -0.3745 -0.0160 23  TYR   O CG  
24812 C  CD1 . TYR   O  23  ? 1.7844 0.5245 1.4264 0.0673  -0.3794 -0.0457 23  TYR   O CD1 
24813 C  CD2 . TYR   O  23  ? 1.7586 0.5271 1.4582 0.0345  -0.3414 -0.0270 23  TYR   O CD2 
24814 C  CE1 . TYR   O  23  ? 1.7707 0.5641 1.4588 0.0697  -0.3668 -0.0676 23  TYR   O CE1 
24815 C  CE2 . TYR   O  23  ? 1.7407 0.4991 1.4942 0.0422  -0.3486 -0.0362 23  TYR   O CE2 
24816 C  CZ  . TYR   O  23  ? 1.7699 0.5648 1.4583 0.0592  -0.3520 -0.0859 23  TYR   O CZ  
24817 O  OH  . TYR   O  23  ? 1.7280 0.8024 1.4674 0.0844  -0.2821 -0.0946 23  TYR   O OH  
24818 N  N   . ALA   O  24  ? 1.8029 0.5112 1.3710 0.0419  -0.4505 0.0521  24  ALA   O N   
24819 C  CA  . ALA   O  24  ? 1.7778 0.5393 1.3405 -0.0158 -0.4563 -0.0001 24  ALA   O CA  
24820 C  C   . ALA   O  24  ? 1.7980 0.5019 1.3372 -0.0685 -0.4719 -0.0168 24  ALA   O C   
24821 O  O   . ALA   O  24  ? 1.7573 0.5082 1.2970 -0.1189 -0.5155 -0.0314 24  ALA   O O   
24822 C  CB  . ALA   O  24  ? 1.7648 0.5524 1.3345 -0.0221 -0.4621 0.0072  24  ALA   O CB  
24823 N  N   . LEU   O  25  ? 1.7641 0.4287 1.3995 -0.1110 -0.4806 -0.0431 25  LEU   O N   
24824 C  CA  . LEU   O  25  ? 1.7851 0.4032 1.4149 -0.1329 -0.4808 -0.0932 25  LEU   O CA  
24825 C  C   . LEU   O  25  ? 1.8316 0.4343 1.4561 -0.1066 -0.4636 -0.0617 25  LEU   O C   
24826 O  O   . LEU   O  25  ? 1.8728 0.4889 1.5032 -0.0701 -0.4072 -0.1244 25  LEU   O O   
24827 C  CB  . LEU   O  25  ? 1.7957 0.3347 1.4372 -0.1570 -0.5004 -0.1255 25  LEU   O CB  
24828 C  CG  . LEU   O  25  ? 1.7802 0.3724 1.3979 -0.1580 -0.5555 -0.1316 25  LEU   O CG  
24829 C  CD1 . LEU   O  25  ? 1.7802 0.3699 1.4133 -0.1450 -0.5396 -0.1455 25  LEU   O CD1 
24830 C  CD2 . LEU   O  25  ? 1.7481 0.4556 1.3841 -0.1850 -0.5755 -0.1693 25  LEU   O CD2 
24831 N  N   . THR   O  26  ? 1.7956 0.5303 1.4446 -0.0883 -0.4670 -0.0279 26  THR   O N   
24832 C  CA  . THR   O  26  ? 1.8176 0.5991 1.4405 -0.1044 -0.4579 0.0170  26  THR   O CA  
24833 C  C   . THR   O  26  ? 1.8067 0.5861 1.4434 -0.1115 -0.4259 0.0200  26  THR   O C   
24834 O  O   . THR   O  26  ? 1.8722 0.6318 1.4672 -0.1600 -0.3733 -0.0137 26  THR   O O   
24835 C  CB  . THR   O  26  ? 1.8041 0.6410 1.4489 -0.0955 -0.4631 0.0445  26  THR   O CB  
24836 O  OG1 . THR   O  26  ? 1.8257 0.7115 1.4153 -0.1096 -0.4805 0.0731  26  THR   O OG1 
24837 C  CG2 . THR   O  26  ? 1.8358 0.6515 1.5078 -0.0770 -0.4435 0.0735  26  THR   O CG2 
24838 N  N   . ALA   O  27  ? 1.7739 0.5115 1.4410 -0.0701 -0.4239 0.0622  27  ALA   O N   
24839 C  CA  . ALA   O  27  ? 1.7965 0.4343 1.4231 -0.0541 -0.4257 0.1026  27  ALA   O CA  
24840 C  C   . ALA   O  27  ? 1.7927 0.4187 1.4591 -0.0641 -0.4235 0.1217  27  ALA   O C   
24841 O  O   . ALA   O  27  ? 1.8364 0.3416 1.4888 -0.0469 -0.4058 0.1973  27  ALA   O O   
24842 C  CB  . ALA   O  27  ? 1.7700 0.4082 1.4018 -0.0286 -0.4337 0.1260  27  ALA   O CB  
24843 N  N   . VAL   O  28  ? 1.8138 0.4955 1.4358 -0.1043 -0.4547 0.1183  28  VAL   O N   
24844 C  CA  . VAL   O  28  ? 1.8107 0.5612 1.4617 -0.1128 -0.4366 0.1232  28  VAL   O CA  
24845 C  C   . VAL   O  28  ? 1.8218 0.5941 1.4857 -0.1222 -0.4000 0.1449  28  VAL   O C   
24846 O  O   . VAL   O  28  ? 1.8347 0.6787 1.4777 -0.1328 -0.3822 0.1995  28  VAL   O O   
24847 C  CB  . VAL   O  28  ? 1.8557 0.5045 1.4761 -0.1672 -0.4260 0.1400  28  VAL   O CB  
24848 C  CG1 . VAL   O  28  ? 1.8610 0.4726 1.5120 -0.1777 -0.3896 0.1419  28  VAL   O CG1 
24849 C  CG2 . VAL   O  28  ? 1.8295 0.5305 1.4664 -0.1771 -0.4450 0.1326  28  VAL   O CG2 
24850 N  N   . LYS   O  29  ? 1.8444 0.6233 1.5244 -0.0859 -0.3925 0.1182  29  LYS   O N   
24851 C  CA  . LYS   O  29  ? 1.8559 0.6802 1.6139 -0.1344 -0.3876 0.0754  29  LYS   O CA  
24852 C  C   . LYS   O  29  ? 1.8754 0.5762 1.5906 -0.1049 -0.3461 0.0190  29  LYS   O C   
24853 O  O   . LYS   O  29  ? 1.8203 0.4667 1.5834 -0.0755 -0.3625 -0.0939 29  LYS   O O   
24854 C  CB  . LYS   O  29  ? 1.9012 0.8358 1.6393 -0.1029 -0.3381 0.0238  29  LYS   O CB  
24855 C  CG  . LYS   O  29  ? 1.9417 1.0343 1.6737 -0.1343 -0.3673 0.0258  29  LYS   O CG  
24856 C  CD  . LYS   O  29  ? 1.9810 1.1795 1.7972 -0.1993 -0.3208 0.0254  29  LYS   O CD  
24857 C  CE  . LYS   O  29  ? 2.0441 1.2311 1.8644 -0.1511 -0.2872 0.0216  29  LYS   O CE  
24858 N  NZ  . LYS   O  29  ? 2.0717 1.2820 1.9344 -0.1788 -0.2483 0.0650  29  LYS   O NZ  
24859 N  N   . GLN   O  30  ? 1.8659 0.5368 1.5806 -0.1165 -0.3291 0.0479  30  GLN   O N   
24860 C  CA  . GLN   O  30  ? 1.8962 0.5231 1.6020 -0.1089 -0.2925 0.1074  30  GLN   O CA  
24861 C  C   . GLN   O  30  ? 1.8280 0.4947 1.6035 -0.1005 -0.2950 0.1426  30  GLN   O C   
24862 O  O   . GLN   O  30  ? 1.8718 0.4247 1.6384 -0.0193 -0.2770 0.1927  30  GLN   O O   
24863 C  CB  . GLN   O  30  ? 1.8980 0.5801 1.5957 -0.1109 -0.2871 0.1353  30  GLN   O CB  
24864 C  CG  . GLN   O  30  ? 1.9455 0.6476 1.6363 -0.0518 -0.2595 0.1452  30  GLN   O CG  
24865 C  CD  . GLN   O  30  ? 2.0435 0.6356 1.7467 -0.0187 -0.2303 0.1114  30  GLN   O CD  
24866 O  OE1 . GLN   O  30  ? 2.1194 0.8147 1.7000 0.0735  -0.1275 0.2583  30  GLN   O OE1 
24867 N  NE2 . GLN   O  30  ? 2.1059 0.8096 1.7552 0.0517  -0.1314 0.1738  30  GLN   O NE2 
24868 N  N   . GLY   O  31  ? 1.7554 0.4794 1.6121 -0.1092 -0.3016 0.1155  31  GLY   O N   
24869 C  CA  . GLY   O  31  ? 1.7589 0.4404 1.6076 -0.1368 -0.3089 0.1133  31  GLY   O CA  
24870 C  C   . GLY   O  31  ? 1.7930 0.3815 1.6132 -0.1694 -0.2721 0.1131  31  GLY   O C   
24871 O  O   . GLY   O  31  ? 1.8174 0.4983 1.6664 -0.2385 -0.2861 0.1026  31  GLY   O O   
24872 N  N   . VAL   O  32  ? 1.8074 0.2900 1.5957 -0.1974 -0.2849 0.1248  32  VAL   O N   
24873 C  CA  . VAL   O  32  ? 1.8277 0.3312 1.5682 -0.1834 -0.2594 0.1092  32  VAL   O CA  
24874 C  C   . VAL   O  32  ? 1.8179 0.3200 1.6024 -0.1595 -0.2699 0.0838  32  VAL   O C   
24875 O  O   . VAL   O  32  ? 1.8193 0.3548 1.5783 -0.1252 -0.2803 0.1211  32  VAL   O O   
24876 C  CB  . VAL   O  32  ? 1.8075 0.3245 1.5727 -0.1862 -0.2557 0.0973  32  VAL   O CB  
24877 C  CG1 . VAL   O  32  ? 1.8166 0.2992 1.5759 -0.1696 -0.2474 0.0985  32  VAL   O CG1 
24878 C  CG2 . VAL   O  32  ? 1.8153 0.3994 1.5575 -0.1643 -0.2817 0.0788  32  VAL   O CG2 
24879 N  N   . THR   O  33  ? 1.7942 0.3427 1.5809 -0.1394 -0.2810 0.0894  33  THR   O N   
24880 C  CA  . THR   O  33  ? 1.7941 0.4494 1.6165 -0.1381 -0.2903 0.1240  33  THR   O CA  
24881 C  C   . THR   O  33  ? 1.8107 0.4694 1.6111 -0.1450 -0.2932 0.0830  33  THR   O C   
24882 O  O   . THR   O  33  ? 1.8384 0.5047 1.5366 -0.1883 -0.3657 0.1436  33  THR   O O   
24883 C  CB  . THR   O  33  ? 1.7699 0.5288 1.6866 -0.1525 -0.2595 0.1412  33  THR   O CB  
24884 O  OG1 . THR   O  33  ? 1.7343 0.5965 1.7745 -0.0660 -0.2388 0.2106  33  THR   O OG1 
24885 C  CG2 . THR   O  33  ? 1.7700 0.5578 1.7077 -0.1483 -0.2719 0.1413  33  THR   O CG2 
24886 N  N   . SER   O  34  ? 1.8540 0.5316 1.6356 -0.1706 -0.2882 0.1218  34  SER   O N   
24887 C  CA  . SER   O  34  ? 1.8394 0.5171 1.6392 -0.1835 -0.3127 0.1382  34  SER   O CA  
24888 C  C   . SER   O  34  ? 1.7860 0.5062 1.6876 -0.1814 -0.3350 0.1209  34  SER   O C   
24889 O  O   . SER   O  34  ? 1.7657 0.5482 1.6483 -0.2205 -0.3744 0.1070  34  SER   O O   
24890 C  CB  . SER   O  34  ? 1.8549 0.4949 1.6753 -0.1780 -0.2874 0.1570  34  SER   O CB  
24891 O  OG  . SER   O  34  ? 1.8715 0.5012 1.7038 -0.1795 -0.2662 0.1396  34  SER   O OG  
24892 N  N   . LEU   O  35  ? 1.7522 0.5505 1.6893 -0.1903 -0.3555 0.0837  35  LEU   O N   
24893 C  CA  . LEU   O  35  ? 1.7696 0.6153 1.6839 -0.1978 -0.3638 0.0818  35  LEU   O CA  
24894 C  C   . LEU   O  35  ? 1.7537 0.6281 1.6435 -0.1871 -0.3924 0.1037  35  LEU   O C   
24895 O  O   . LEU   O  35  ? 1.7605 0.6074 1.6200 -0.1234 -0.3825 0.1174  35  LEU   O O   
24896 C  CB  . LEU   O  35  ? 1.7910 0.6534 1.7040 -0.2164 -0.3386 0.0962  35  LEU   O CB  
24897 C  CG  . LEU   O  35  ? 1.8208 0.6685 1.6912 -0.2321 -0.3325 0.1294  35  LEU   O CG  
24898 C  CD1 . LEU   O  35  ? 1.7791 0.7247 1.7048 -0.2353 -0.3319 0.1129  35  LEU   O CD1 
24899 C  CD2 . LEU   O  35  ? 1.8476 0.6689 1.6865 -0.2139 -0.3131 0.1600  35  LEU   O CD2 
24900 N  N   . GLY   O  36  ? 1.7742 0.6138 1.6381 -0.1819 -0.4088 0.0745  36  GLY   O N   
24901 C  CA  . GLY   O  36  ? 1.8074 0.6370 1.6310 -0.1676 -0.4324 0.1056  36  GLY   O CA  
24902 C  C   . GLY   O  36  ? 1.8217 0.6742 1.6382 -0.1506 -0.4492 0.1203  36  GLY   O C   
24903 O  O   . GLY   O  36  ? 1.8797 0.6277 1.5767 -0.1168 -0.4345 0.1789  36  GLY   O O   
24904 N  N   . ILE   O  37  ? 1.8029 0.7465 1.6679 -0.1405 -0.4635 0.1059  37  ILE   O N   
24905 C  CA  . ILE   O  37  ? 1.8330 0.7963 1.6627 -0.1825 -0.4915 0.0756  37  ILE   O CA  
24906 C  C   . ILE   O  37  ? 1.7979 0.7745 1.6563 -0.2066 -0.5020 0.0418  37  ILE   O C   
24907 O  O   . ILE   O  37  ? 1.7941 0.7514 1.6462 -0.2077 -0.4880 0.0562  37  ILE   O O   
24908 C  CB  . ILE   O  37  ? 1.8863 0.8068 1.6646 -0.2017 -0.4895 0.1045  37  ILE   O CB  
24909 C  CG1 . ILE   O  37  ? 1.9138 0.8344 1.6607 -0.1835 -0.4820 0.1177  37  ILE   O CG1 
24910 C  CG2 . ILE   O  37  ? 1.8914 0.8133 1.6935 -0.1890 -0.5027 0.1225  37  ILE   O CG2 
24911 C  CD1 . ILE   O  37  ? 1.9410 0.9789 1.6838 -0.2009 -0.4268 0.1044  37  ILE   O CD1 
24912 N  N   . LYS   O  38  ? 1.7844 0.7088 1.6463 -0.2262 -0.4880 0.0334  38  LYS   O N   
24913 C  CA  . LYS   O  38  ? 1.7449 0.6712 1.6821 -0.2285 -0.4549 0.0000  38  LYS   O CA  
24914 C  C   . LYS   O  38  ? 1.7432 0.6396 1.7521 -0.1978 -0.4692 0.0336  38  LYS   O C   
24915 O  O   . LYS   O  38  ? 1.7558 0.6339 1.7075 -0.1441 -0.4956 0.0502  38  LYS   O O   
24916 C  CB  . LYS   O  38  ? 1.7203 0.7339 1.6784 -0.2386 -0.4351 -0.0350 38  LYS   O CB  
24917 C  CG  . LYS   O  38  ? 1.7167 0.7737 1.6661 -0.2164 -0.4107 0.0010  38  LYS   O CG  
24918 C  CD  . LYS   O  38  ? 1.7150 0.8905 1.6348 -0.2192 -0.4127 -0.0169 38  LYS   O CD  
24919 C  CE  . LYS   O  38  ? 1.7018 0.9715 1.6460 -0.2383 -0.4284 -0.0115 38  LYS   O CE  
24920 N  NZ  . LYS   O  38  ? 1.7096 1.0354 1.6334 -0.2279 -0.4304 -0.0037 38  LYS   O NZ  
24921 N  N   . ALA   O  39  ? 1.7056 0.6481 1.7839 -0.2347 -0.4569 0.0120  39  ALA   O N   
24922 C  CA  . ALA   O  39  ? 1.6946 0.7850 1.8557 -0.2686 -0.4415 0.0209  39  ALA   O CA  
24923 C  C   . ALA   O  39  ? 1.6629 0.8122 1.8592 -0.2802 -0.4454 0.0412  39  ALA   O C   
24924 O  O   . ALA   O  39  ? 1.6639 0.7221 1.8168 -0.2802 -0.4833 0.0398  39  ALA   O O   
24925 C  CB  . ALA   O  39  ? 1.6852 0.7984 1.8603 -0.2785 -0.4257 0.0569  39  ALA   O CB  
24926 N  N   . THR   O  40  ? 1.6815 0.8954 1.8905 -0.2341 -0.4315 0.0852  40  THR   O N   
24927 C  CA  . THR   O  40  ? 1.7287 0.9469 1.8949 -0.2095 -0.3860 0.1315  40  THR   O CA  
24928 C  C   . THR   O  40  ? 1.7747 0.9470 1.8660 -0.1849 -0.3497 0.1217  40  THR   O C   
24929 O  O   . THR   O  40  ? 1.8849 1.0274 1.9106 -0.1399 -0.2771 0.1953  40  THR   O O   
24930 C  CB  . THR   O  40  ? 1.7188 1.0634 1.9485 -0.1794 -0.3676 0.1246  40  THR   O CB  
24931 O  OG1 . THR   O  40  ? 1.7232 1.1441 1.9796 -0.1289 -0.3344 0.1329  40  THR   O OG1 
24932 C  CG2 . THR   O  40  ? 1.7439 1.0828 1.9545 -0.1799 -0.3694 0.1111  40  THR   O CG2 
24933 N  N   . ASN   O  41  ? 1.7690 0.8329 1.8598 -0.1939 -0.3344 0.1299  41  ASN   O N   
24934 C  CA  . ASN   O  41  ? 1.7479 0.8560 1.7842 -0.2010 -0.3551 0.1396  41  ASN   O CA  
24935 C  C   . ASN   O  41  ? 1.7266 0.7309 1.7866 -0.1974 -0.3531 0.1183  41  ASN   O C   
24936 O  O   . ASN   O  41  ? 1.7246 0.7537 1.7546 -0.2038 -0.3619 0.1448  41  ASN   O O   
24937 C  CB  . ASN   O  41  ? 1.7622 0.9345 1.8068 -0.2302 -0.3172 0.1498  41  ASN   O CB  
24938 C  CG  . ASN   O  41  ? 1.7816 0.9299 1.8042 -0.2297 -0.3085 0.1418  41  ASN   O CG  
24939 O  OD1 . ASN   O  41  ? 1.7742 0.9298 1.7773 -0.2598 -0.3212 0.1030  41  ASN   O OD1 
24940 N  ND2 . ASN   O  41  ? 1.8213 1.0581 1.8305 -0.2028 -0.2844 0.1204  41  ASN   O ND2 
24941 N  N   . GLY   O  42  ? 1.7223 0.6722 1.7530 -0.2393 -0.3826 0.0305  42  GLY   O N   
24942 C  CA  . GLY   O  42  ? 1.7213 0.7062 1.7650 -0.2748 -0.3871 -0.0048 42  GLY   O CA  
24943 C  C   . GLY   O  42  ? 1.7523 0.7007 1.7485 -0.2806 -0.4142 -0.0476 42  GLY   O C   
24944 O  O   . GLY   O  42  ? 1.8696 0.8805 1.7709 -0.2978 -0.4498 -0.1248 42  GLY   O O   
24945 N  N   . VAL   O  43  ? 1.7608 0.6646 1.7218 -0.2312 -0.4030 -0.0113 43  VAL   O N   
24946 C  CA  . VAL   O  43  ? 1.7454 0.6749 1.7218 -0.2359 -0.3643 -0.0154 43  VAL   O CA  
24947 C  C   . VAL   O  43  ? 1.7874 0.6393 1.7456 -0.2227 -0.3473 0.0154  43  VAL   O C   
24948 O  O   . VAL   O  43  ? 1.8016 0.6172 1.8465 -0.2812 -0.3023 -0.0200 43  VAL   O O   
24949 C  CB  . VAL   O  43  ? 1.7212 0.6484 1.6713 -0.1852 -0.3759 0.0196  43  VAL   O CB  
24950 C  CG1 . VAL   O  43  ? 1.6848 0.6723 1.6750 -0.1821 -0.3672 0.0277  43  VAL   O CG1 
24951 C  CG2 . VAL   O  43  ? 1.7038 0.6274 1.6839 -0.1934 -0.3637 0.0361  43  VAL   O CG2 
24952 N  N   . VAL   O  44  ? 1.7965 0.6234 1.6972 -0.2521 -0.3603 -0.0161 44  VAL   O N   
24953 C  CA  . VAL   O  44  ? 1.7755 0.6100 1.6616 -0.2551 -0.3458 -0.0394 44  VAL   O CA  
24954 C  C   . VAL   O  44  ? 1.7875 0.5394 1.6064 -0.2344 -0.3942 -0.0550 44  VAL   O C   
24955 O  O   . VAL   O  44  ? 1.6832 0.5143 1.5966 -0.1768 -0.4016 -0.0378 44  VAL   O O   
24956 C  CB  . VAL   O  44  ? 1.8308 0.6686 1.6768 -0.2913 -0.3287 -0.0124 44  VAL   O CB  
24957 C  CG1 . VAL   O  44  ? 1.8539 0.7454 1.6853 -0.3159 -0.3378 -0.0304 44  VAL   O CG1 
24958 C  CG2 . VAL   O  44  ? 1.8215 0.5996 1.6616 -0.3004 -0.2992 -0.0128 44  VAL   O CG2 
24959 N  N   . ILE   O  45  ? 1.8032 0.4842 1.5765 -0.2108 -0.3931 -0.0718 45  ILE   O N   
24960 C  CA  . ILE   O  45  ? 1.8136 0.4486 1.5442 -0.2217 -0.3794 -0.0799 45  ILE   O CA  
24961 C  C   . ILE   O  45  ? 1.8885 0.4534 1.5360 -0.2310 -0.3765 -0.0823 45  ILE   O C   
24962 O  O   . ILE   O  45  ? 1.9436 0.4393 1.5346 -0.2185 -0.4049 -0.0811 45  ILE   O O   
24963 C  CB  . ILE   O  45  ? 1.7979 0.4608 1.4910 -0.2146 -0.3856 -0.0674 45  ILE   O CB  
24964 C  CG1 . ILE   O  45  ? 1.7887 0.4788 1.4874 -0.2177 -0.3903 -0.0819 45  ILE   O CG1 
24965 C  CG2 . ILE   O  45  ? 1.7724 0.3846 1.4859 -0.2003 -0.4017 -0.0699 45  ILE   O CG2 
24966 C  CD1 . ILE   O  45  ? 1.7713 0.5422 1.4756 -0.2259 -0.4085 -0.1016 45  ILE   O CD1 
24967 N  N   . ALA   O  46  ? 1.8953 0.4843 1.5853 -0.1726 -0.3490 -0.0073 46  ALA   O N   
24968 C  CA  . ALA   O  46  ? 1.9021 0.5731 1.5988 -0.1833 -0.3052 0.0337  46  ALA   O CA  
24969 C  C   . ALA   O  46  ? 1.8967 0.5616 1.6165 -0.1916 -0.3070 0.0646  46  ALA   O C   
24970 O  O   . ALA   O  46  ? 1.8961 0.6762 1.6045 -0.1851 -0.2736 0.1468  46  ALA   O O   
24971 C  CB  . ALA   O  46  ? 1.9222 0.5650 1.6444 -0.1855 -0.2688 0.0641  46  ALA   O CB  
24972 N  N   . THR   O  47  ? 1.8863 0.4729 1.6016 -0.1940 -0.3200 0.0156  47  THR   O N   
24973 C  CA  . THR   O  47  ? 1.8638 0.5102 1.6563 -0.1864 -0.3144 -0.0188 47  THR   O CA  
24974 C  C   . THR   O  47  ? 1.9517 0.5452 1.6579 -0.1426 -0.2809 -0.0201 47  THR   O C   
24975 O  O   . THR   O  47  ? 1.9357 0.4975 1.7522 -0.2002 -0.2984 -0.1213 47  THR   O O   
24976 C  CB  . THR   O  47  ? 1.8603 0.4166 1.5977 -0.2025 -0.3505 -0.0393 47  THR   O CB  
24977 O  OG1 . THR   O  47  ? 1.7552 0.4406 1.6011 -0.2402 -0.3734 -0.0724 47  THR   O OG1 
24978 C  CG2 . THR   O  47  ? 1.8273 0.4042 1.5778 -0.1948 -0.3414 -0.0255 47  THR   O CG2 
24979 N  N   . GLU   O  48  ? 2.0396 0.6049 1.7428 -0.0858 -0.2626 0.0932  48  GLU   O N   
24980 C  CA  . GLU   O  48  ? 2.1102 0.6805 1.7545 -0.0852 -0.2467 0.1300  48  GLU   O CA  
24981 C  C   . GLU   O  48  ? 2.1111 0.5625 1.7149 -0.0586 -0.2213 0.1155  48  GLU   O C   
24982 O  O   . GLU   O  48  ? 2.1233 0.3669 1.7306 -0.0753 -0.2220 0.1446  48  GLU   O O   
24983 C  CB  . GLU   O  48  ? 2.2005 0.6861 1.8259 -0.0844 -0.2437 0.1238  48  GLU   O CB  
24984 C  CG  . GLU   O  48  ? 2.2991 0.7587 1.8594 -0.0685 -0.2674 0.1701  48  GLU   O CG  
24985 C  CD  . GLU   O  48  ? 2.3948 0.7846 1.9040 0.0059  -0.2927 0.2586  48  GLU   O CD  
24986 O  OE1 . GLU   O  48  ? 2.4557 1.0011 1.9667 -0.0238 -0.3351 0.1752  48  GLU   O OE1 
24987 O  OE2 . GLU   O  48  ? 2.5723 1.0578 1.8648 0.0152  -0.3229 0.3387  48  GLU   O OE2 
24988 N  N   . LYS   O  49  ? 2.1294 0.6016 1.7307 -0.0243 -0.2109 0.0781  49  LYS   O N   
24989 C  CA  . LYS   O  49  ? 2.1229 0.7909 1.7193 -0.0379 -0.2077 0.0352  49  LYS   O CA  
24990 C  C   . LYS   O  49  ? 2.1145 0.9294 1.7284 0.0236  -0.2578 0.0473  49  LYS   O C   
24991 O  O   . LYS   O  49  ? 2.1065 1.0881 1.7467 0.0114  -0.1668 0.0214  49  LYS   O O   
24992 C  CB  . LYS   O  49  ? 2.0897 0.8919 1.6666 -0.0104 -0.2120 0.0312  49  LYS   O CB  
24993 C  CG  . LYS   O  49  ? 2.0954 0.9362 1.6541 0.0310  -0.2093 0.0613  49  LYS   O CG  
24994 C  CD  . LYS   O  49  ? 2.1140 1.0453 1.6177 0.0870  -0.1995 0.0238  49  LYS   O CD  
24995 C  CE  . LYS   O  49  ? 2.1502 1.0949 1.6229 0.1182  -0.1754 0.0186  49  LYS   O CE  
24996 N  NZ  . LYS   O  49  ? 2.1483 1.1333 1.6061 0.1534  -0.1538 -0.0004 49  LYS   O NZ  
24997 N  N   . LYS   O  50  ? 2.1570 1.1599 1.7891 0.0406  -0.2349 -0.0528 50  LYS   O N   
24998 C  CA  . LYS   O  50  ? 2.2921 1.1372 1.8313 0.0385  -0.2788 -0.0369 50  LYS   O CA  
24999 C  C   . LYS   O  50  ? 2.3887 1.0540 1.8326 -0.0278 -0.2951 -0.0279 50  LYS   O C   
25000 O  O   . LYS   O  50  ? 2.4459 0.8675 2.0223 -0.1435 -0.4465 -0.2014 50  LYS   O O   
25001 C  CB  . LYS   O  50  ? 2.3934 1.2243 1.8669 0.0235  -0.2215 -0.0779 50  LYS   O CB  
25002 C  CG  . LYS   O  50  ? 2.4494 1.0441 1.8673 0.0193  -0.1248 -0.0865 50  LYS   O CG  
25003 C  CD  . LYS   O  50  ? 2.5023 1.0174 1.8857 0.0001  -0.0590 -0.1412 50  LYS   O CD  
25004 C  CE  . LYS   O  50  ? 2.4782 1.1216 1.9247 0.0316  -0.0295 -0.1841 50  LYS   O CE  
25005 N  NZ  . LYS   O  50  ? 2.5294 1.1708 2.0343 -0.0304 -0.0070 -0.2096 50  LYS   O NZ  
25006 N  N   . SER   O  51  ? 2.3590 0.9593 1.8074 -0.0340 -0.3734 0.0087  51  SER   O N   
25007 C  CA  . SER   O  51  ? 2.3690 0.8992 1.7480 0.0100  -0.3579 0.0341  51  SER   O CA  
25008 C  C   . SER   O  51  ? 2.4512 1.0534 1.8114 0.1076  -0.4049 0.0955  51  SER   O C   
25009 O  O   . SER   O  51  ? 2.4491 1.0966 1.9498 0.0180  -0.4552 -0.0357 51  SER   O O   
25010 C  CB  . SER   O  51  ? 2.3226 0.8031 1.6889 0.0273  -0.3949 -0.0311 51  SER   O CB  
25011 O  OG  . SER   O  51  ? 2.3075 0.6782 1.6108 0.0670  -0.3287 -0.0244 51  SER   O OG  
25012 N  N   . SER   O  52  ? 2.4329 0.9473 1.8149 0.1590  -0.3936 0.2117  52  SER   O N   
25013 C  CA  . SER   O  52  ? 2.5329 0.9862 1.7975 0.2728  -0.3764 0.2634  52  SER   O CA  
25014 C  C   . SER   O  52  ? 2.4240 0.9777 1.8218 0.4437  -0.3883 0.2690  52  SER   O C   
25015 O  O   . SER   O  52  ? 2.4499 0.8740 1.6335 0.3785  -0.3866 0.3420  52  SER   O O   
25016 C  CB  . SER   O  52  ? 2.5553 0.8347 1.8637 0.3185  -0.3853 0.2603  52  SER   O CB  
25017 O  OG  . SER   O  52  ? 2.6801 0.6309 1.8820 0.3180  -0.3670 0.2408  52  SER   O OG  
25018 N  N   . SER   O  53  ? 2.4745 1.1288 1.7159 0.3729  -0.3939 0.2584  53  SER   O N   
25019 C  CA  . SER   O  53  ? 2.4668 1.0599 1.7422 0.3479  -0.4428 0.2820  53  SER   O CA  
25020 C  C   . SER   O  53  ? 2.4553 1.0829 1.6703 0.2003  -0.3917 0.2410  53  SER   O C   
25021 O  O   . SER   O  53  ? 2.5308 1.0663 1.7435 0.2151  -0.4668 0.1840  53  SER   O O   
25022 C  CB  . SER   O  53  ? 2.3779 1.0192 1.8212 0.4277  -0.4324 0.2796  53  SER   O CB  
25023 O  OG  . SER   O  53  ? 2.3431 0.9553 1.8607 0.5114  -0.4597 0.3381  53  SER   O OG  
25024 N  N   . PRO   O  54  ? 2.4546 1.0057 1.6803 0.1200  -0.4048 0.2016  54  PRO   O N   
25025 C  CA  . PRO   O  54  ? 2.4121 0.9692 1.5852 0.0535  -0.4056 0.2006  54  PRO   O CA  
25026 C  C   . PRO   O  54  ? 2.3141 1.0534 1.5312 0.0572  -0.3532 0.1631  54  PRO   O C   
25027 O  O   . PRO   O  54  ? 2.2272 1.3249 1.4985 0.1479  -0.3453 0.2526  54  PRO   O O   
25028 C  CB  . PRO   O  54  ? 2.4610 0.9874 1.5710 0.0348  -0.3809 0.1960  54  PRO   O CB  
25029 C  CG  . PRO   O  54  ? 2.5082 1.0644 1.6518 0.0852  -0.3741 0.2121  54  PRO   O CG  
25030 C  CD  . PRO   O  54  ? 2.4925 1.0192 1.6809 0.0923  -0.3740 0.2551  54  PRO   O CD  
25031 N  N   . LEU   O  55  ? 2.3482 0.8222 1.5160 -0.0526 -0.3609 0.0869  55  LEU   O N   
25032 C  CA  . LEU   O  55  ? 2.2710 0.7628 1.5206 -0.0405 -0.3757 0.1244  55  LEU   O CA  
25033 C  C   . LEU   O  55  ? 2.2704 0.6335 1.5374 -0.0469 -0.3963 0.0438  55  LEU   O C   
25034 O  O   . LEU   O  55  ? 2.3039 0.5833 1.5319 0.0637  -0.3448 0.0947  55  LEU   O O   
25035 C  CB  . LEU   O  55  ? 2.2710 0.6989 1.4637 -0.0671 -0.4079 0.0867  55  LEU   O CB  
25036 C  CG  . LEU   O  55  ? 2.2559 0.6706 1.4783 -0.0847 -0.3885 0.0817  55  LEU   O CG  
25037 C  CD1 . LEU   O  55  ? 2.2668 0.7069 1.5057 -0.0794 -0.3979 0.0655  55  LEU   O CD1 
25038 C  CD2 . LEU   O  55  ? 2.2241 0.6890 1.4990 -0.0904 -0.3802 0.0794  55  LEU   O CD2 
25039 N  N   . ALA   O  56  ? 2.1964 0.4426 1.5267 -0.0671 -0.4247 0.0865  56  ALA   O N   
25040 C  CA  . ALA   O  56  ? 2.0938 0.3239 1.5809 -0.0836 -0.4307 0.0478  56  ALA   O CA  
25041 C  C   . ALA   O  56  ? 2.0607 0.4367 1.6028 -0.0914 -0.4181 0.0418  56  ALA   O C   
25042 O  O   . ALA   O  56  ? 2.1178 0.2445 1.6510 -0.0492 -0.3985 0.0596  56  ALA   O O   
25043 C  CB  . ALA   O  56  ? 2.0537 0.2446 1.5696 -0.1059 -0.4390 0.0710  56  ALA   O CB  
25044 N  N   . MET   O  57  ? 2.0719 0.4423 1.6311 -0.0431 -0.4031 0.0470  57  MET   O N   
25045 C  CA  . MET   O  57  ? 2.0977 0.5080 1.6598 -0.0016 -0.3763 0.1036  57  MET   O CA  
25046 C  C   . MET   O  57  ? 2.0603 0.2910 1.6716 0.0031  -0.3878 0.1248  57  MET   O C   
25047 O  O   . MET   O  57  ? 2.0511 0.2367 1.6128 0.0871  -0.4268 0.1696  57  MET   O O   
25048 C  CB  . MET   O  57  ? 2.1320 0.5976 1.6585 0.0259  -0.3532 0.0263  57  MET   O CB  
25049 C  CG  . MET   O  57  ? 2.1607 0.8176 1.6591 0.0643  -0.3390 0.0439  57  MET   O CG  
25050 S  SD  . MET   O  57  ? 2.1764 0.9279 1.7220 0.0566  -0.3152 -0.0555 57  MET   O SD  
25051 C  CE  . MET   O  57  ? 2.1690 0.9817 1.6734 0.1043  -0.2798 -0.0179 57  MET   O CE  
25052 N  N   . SER   O  58  ? 2.0309 0.4691 1.6818 -0.0671 -0.4119 0.1667  58  SER   O N   
25053 C  CA  . SER   O  58  ? 2.0642 0.6461 1.6806 -0.0873 -0.3913 0.2211  58  SER   O CA  
25054 C  C   . SER   O  58  ? 2.0888 0.5638 1.6912 -0.1029 -0.3868 0.1368  58  SER   O C   
25055 O  O   . SER   O  58  ? 2.1258 0.6286 1.6871 -0.1686 -0.3939 0.1263  58  SER   O O   
25056 C  CB  . SER   O  58  ? 2.0513 0.7977 1.7150 -0.1967 -0.3854 0.2361  58  SER   O CB  
25057 O  OG  . SER   O  58  ? 2.0963 1.0752 1.8260 -0.2285 -0.3268 0.2875  58  SER   O OG  
25058 N  N   . GLU   O  59  ? 2.1061 0.6096 1.6810 -0.0576 -0.3708 0.1411  59  GLU   O N   
25059 C  CA  . GLU   O  59  ? 2.0975 0.5958 1.6699 -0.0752 -0.3604 0.1740  59  GLU   O CA  
25060 C  C   . GLU   O  59  ? 2.0836 0.3662 1.6599 0.0062  -0.3905 0.1805  59  GLU   O C   
25061 O  O   . GLU   O  59  ? 1.9835 0.5077 1.6245 0.0050  -0.4509 0.2039  59  GLU   O O   
25062 C  CB  . GLU   O  59  ? 2.1457 0.6100 1.7211 -0.0165 -0.3511 0.1583  59  GLU   O CB  
25063 C  CG  . GLU   O  59  ? 2.1862 0.7787 1.7442 -0.0569 -0.2806 0.1689  59  GLU   O CG  
25064 C  CD  . GLU   O  59  ? 2.2452 0.8311 1.7490 -0.0120 -0.3229 0.1116  59  GLU   O CD  
25065 O  OE1 . GLU   O  59  ? 2.2625 0.8868 1.7089 -0.0144 -0.2607 0.0510  59  GLU   O OE1 
25066 O  OE2 . GLU   O  59  ? 2.2766 0.8280 1.8390 -0.0186 -0.3504 0.1688  59  GLU   O OE2 
25067 N  N   . THR   O  60  ? 2.0822 0.2616 1.6648 -0.0112 -0.3820 0.1903  60  THR   O N   
25068 C  CA  . THR   O  60  ? 2.1084 0.3805 1.6774 -0.0540 -0.3539 0.2029  60  THR   O CA  
25069 C  C   . THR   O  60  ? 2.1557 0.4059 1.6619 -0.0165 -0.3486 0.2429  60  THR   O C   
25070 O  O   . THR   O  60  ? 2.1709 0.7402 1.5169 -0.0694 -0.3030 0.3121  60  THR   O O   
25071 C  CB  . THR   O  60  ? 2.0947 0.3931 1.7255 -0.0534 -0.3642 0.1978  60  THR   O CB  
25072 O  OG1 . THR   O  60  ? 2.0562 0.4048 1.7298 -0.0461 -0.3835 0.1452  60  THR   O OG1 
25073 C  CG2 . THR   O  60  ? 2.0946 0.4486 1.7646 -0.0275 -0.3202 0.1860  60  THR   O CG2 
25074 N  N   . LEU   O  61  ? 2.1692 0.4958 1.6883 0.0151  -0.3664 0.1451  61  LEU   O N   
25075 C  CA  . LEU   O  61  ? 2.1742 0.7215 1.7174 0.0664  -0.3262 0.1156  61  LEU   O CA  
25076 C  C   . LEU   O  61  ? 2.1590 0.5940 1.7227 0.0949  -0.3064 0.1017  61  LEU   O C   
25077 O  O   . LEU   O  61  ? 2.1399 0.7296 1.7966 0.0494  -0.2393 -0.0141 61  LEU   O O   
25078 C  CB  . LEU   O  61  ? 2.1667 0.8176 1.7728 0.1888  -0.3358 0.0908  61  LEU   O CB  
25079 C  CG  . LEU   O  61  ? 2.1730 1.1015 1.7772 0.1441  -0.2881 0.1594  61  LEU   O CG  
25080 C  CD1 . LEU   O  61  ? 2.2062 1.1015 1.8624 0.1385  -0.2735 0.1521  61  LEU   O CD1 
25081 C  CD2 . LEU   O  61  ? 2.1194 1.1278 1.7960 0.1525  -0.2287 0.2416  61  LEU   O CD2 
25082 N  N   . SER   O  62  ? 2.1094 0.5323 1.7186 0.0577  -0.2875 0.0659  62  SER   O N   
25083 C  CA  . SER   O  62  ? 2.0819 0.6699 1.7054 0.0617  -0.2709 0.0353  62  SER   O CA  
25084 C  C   . SER   O  62  ? 2.0084 0.5421 1.7482 -0.0016 -0.2295 0.0195  62  SER   O C   
25085 O  O   . SER   O  62  ? 1.9611 0.8499 1.8221 0.0659  -0.1096 -0.0079 62  SER   O O   
25086 C  CB  . SER   O  62  ? 2.1219 0.6690 1.7296 0.0602  -0.2792 -0.0103 62  SER   O CB  
25087 O  OG  . SER   O  62  ? 2.1796 0.5824 1.7290 0.0716  -0.3051 0.0054  62  SER   O OG  
25088 N  N   . LYS   O  63  ? 2.0433 0.3762 1.7172 0.0146  -0.1930 0.0938  63  LYS   O N   
25089 C  CA  . LYS   O  63  ? 2.0127 0.4763 1.6696 -0.0195 -0.2152 0.1143  63  LYS   O CA  
25090 C  C   . LYS   O  63  ? 2.0048 0.4141 1.5674 -0.1204 -0.2353 0.0868  63  LYS   O C   
25091 O  O   . LYS   O  63  ? 1.9666 0.4465 1.5707 -0.1671 -0.2379 0.1086  63  LYS   O O   
25092 C  CB  . LYS   O  63  ? 2.0264 0.4883 1.6646 -0.0282 -0.1955 0.1220  63  LYS   O CB  
25093 C  CG  . LYS   O  63  ? 2.0627 0.5321 1.6497 0.0205  -0.1643 0.1394  63  LYS   O CG  
25094 C  CD  . LYS   O  63  ? 2.0863 0.5201 1.6323 0.0470  -0.1907 0.1363  63  LYS   O CD  
25095 C  CE  . LYS   O  63  ? 2.1163 0.5771 1.6222 0.0507  -0.2046 0.1350  63  LYS   O CE  
25096 N  NZ  . LYS   O  63  ? 2.1659 0.5885 1.6632 0.0231  -0.2123 0.1266  63  LYS   O NZ  
25097 N  N   . VAL   O  64  ? 1.9723 0.4230 1.5492 -0.1349 -0.2727 0.0836  64  VAL   O N   
25098 C  CA  . VAL   O  64  ? 1.9907 0.5032 1.5414 -0.1500 -0.3018 0.1297  64  VAL   O CA  
25099 C  C   . VAL   O  64  ? 1.9724 0.5266 1.4751 -0.1589 -0.3387 0.1246  64  VAL   O C   
25100 O  O   . VAL   O  64  ? 2.0642 0.5903 1.4827 -0.1557 -0.3474 0.0999  64  VAL   O O   
25101 C  CB  . VAL   O  64  ? 1.9958 0.4856 1.5957 -0.1675 -0.2995 0.1635  64  VAL   O CB  
25102 C  CG1 . VAL   O  64  ? 1.9948 0.5007 1.6281 -0.1576 -0.2839 0.1931  64  VAL   O CG1 
25103 C  CG2 . VAL   O  64  ? 2.0143 0.5043 1.6521 -0.1825 -0.2762 0.1224  64  VAL   O CG2 
25104 N  N   . SER   O  65  ? 1.8903 0.4981 1.4503 -0.1743 -0.3450 0.0831  65  SER   O N   
25105 C  CA  . SER   O  65  ? 1.8371 0.4279 1.4641 -0.0894 -0.3117 0.0648  65  SER   O CA  
25106 C  C   . SER   O  65  ? 1.8319 0.3698 1.4721 -0.1079 -0.2942 0.0603  65  SER   O C   
25107 O  O   . SER   O  65  ? 1.8325 0.1397 1.4974 -0.0912 -0.2706 0.0284  65  SER   O O   
25108 C  CB  . SER   O  65  ? 1.8161 0.4422 1.4610 -0.0955 -0.3375 0.0507  65  SER   O CB  
25109 O  OG  . SER   O  65  ? 1.7708 0.5430 1.4575 -0.0514 -0.3453 0.0423  65  SER   O OG  
25110 N  N   . LEU   O  66  ? 1.7787 0.3905 1.5395 -0.0530 -0.2453 0.0686  66  LEU   O N   
25111 C  CA  . LEU   O  66  ? 1.7069 0.4524 1.5435 -0.0760 -0.2558 0.1288  66  LEU   O CA  
25112 C  C   . LEU   O  66  ? 1.6624 0.4304 1.5386 -0.0585 -0.2846 0.1406  66  LEU   O C   
25113 O  O   . LEU   O  66  ? 1.6519 0.4133 1.4783 -0.0343 -0.2815 0.1807  66  LEU   O O   
25114 C  CB  . LEU   O  66  ? 1.7022 0.4964 1.5472 -0.0884 -0.2329 0.1156  66  LEU   O CB  
25115 C  CG  . LEU   O  66  ? 1.6947 0.5048 1.5619 -0.1017 -0.2266 0.1374  66  LEU   O CG  
25116 C  CD1 . LEU   O  66  ? 1.7029 0.5329 1.5824 -0.1109 -0.2040 0.1322  66  LEU   O CD1 
25117 C  CD2 . LEU   O  66  ? 1.6954 0.4835 1.5556 -0.1105 -0.2286 0.1075  66  LEU   O CD2 
25118 N  N   . LEU   O  67  ? 1.6540 0.4615 1.5441 -0.0674 -0.3089 0.1262  67  LEU   O N   
25119 C  CA  . LEU   O  67  ? 1.6241 0.5194 1.5626 -0.1120 -0.3109 0.0759  67  LEU   O CA  
25120 C  C   . LEU   O  67  ? 1.6278 0.4887 1.6553 -0.1513 -0.3177 0.0318  67  LEU   O C   
25121 O  O   . LEU   O  67  ? 1.6555 0.6078 1.6862 -0.2086 -0.3331 -0.0326 67  LEU   O O   
25122 C  CB  . LEU   O  67  ? 1.6158 0.4655 1.5699 -0.0972 -0.3290 0.0780  67  LEU   O CB  
25123 C  CG  . LEU   O  67  ? 1.5717 0.4559 1.5283 -0.1153 -0.3503 0.0417  67  LEU   O CG  
25124 C  CD1 . LEU   O  67  ? 1.5609 0.4470 1.5253 -0.1093 -0.3581 0.0427  67  LEU   O CD1 
25125 C  CD2 . LEU   O  67  ? 1.5562 0.4878 1.5124 -0.1254 -0.3505 0.0138  67  LEU   O CD2 
25126 N  N   . THR   O  68  ? 1.6155 0.4356 1.6897 -0.1684 -0.3152 0.0306  68  THR   O N   
25127 C  CA  . THR   O  68  ? 1.6231 0.4213 1.6713 -0.1773 -0.3239 0.0582  68  THR   O CA  
25128 C  C   . THR   O  68  ? 1.6465 0.4146 1.6597 -0.1720 -0.3086 0.1025  68  THR   O C   
25129 O  O   . THR   O  68  ? 1.6717 0.4179 1.7215 -0.1782 -0.2645 0.0949  68  THR   O O   
25130 C  CB  . THR   O  68  ? 1.5711 0.3833 1.6653 -0.2013 -0.3556 0.0308  68  THR   O CB  
25131 O  OG1 . THR   O  68  ? 1.5985 0.4070 1.7186 -0.2082 -0.3645 -0.0259 68  THR   O OG1 
25132 C  CG2 . THR   O  68  ? 1.5680 0.3646 1.6654 -0.1865 -0.3585 0.0321  68  THR   O CG2 
25133 N  N   . PRO   O  69  ? 1.6734 0.4831 1.6244 -0.1007 -0.2823 0.1448  69  PRO   O N   
25134 C  CA  . PRO   O  69  ? 1.6757 0.5062 1.5846 -0.1390 -0.2949 0.1936  69  PRO   O CA  
25135 C  C   . PRO   O  69  ? 1.6610 0.4348 1.5112 -0.1037 -0.3218 0.2661  69  PRO   O C   
25136 O  O   . PRO   O  69  ? 1.6769 0.4116 1.5317 -0.0699 -0.3191 0.3699  69  PRO   O O   
25137 C  CB  . PRO   O  69  ? 1.6771 0.5398 1.6115 -0.1001 -0.2749 0.1630  69  PRO   O CB  
25138 C  CG  . PRO   O  69  ? 1.7080 0.5606 1.6287 -0.1347 -0.2462 0.1358  69  PRO   O CG  
25139 C  CD  . PRO   O  69  ? 1.6933 0.5155 1.6394 -0.1412 -0.2526 0.1449  69  PRO   O CD  
25140 N  N   . ASP   O  70  ? 1.6694 0.4676 1.4879 -0.0965 -0.3754 0.2616  70  ASP   O N   
25141 C  CA  . ASP   O  70  ? 1.6976 0.4993 1.5418 -0.1103 -0.3798 0.2084  70  ASP   O CA  
25142 C  C   . ASP   O  70  ? 1.6501 0.4131 1.4981 -0.1374 -0.4461 0.2545  70  ASP   O C   
25143 O  O   . ASP   O  70  ? 1.6855 0.3922 1.4983 -0.1155 -0.4727 0.2611  70  ASP   O O   
25144 C  CB  . ASP   O  70  ? 1.7267 0.6130 1.5438 -0.0921 -0.4306 0.2120  70  ASP   O CB  
25145 C  CG  . ASP   O  70  ? 1.7709 0.6222 1.6127 -0.0817 -0.4134 0.2089  70  ASP   O CG  
25146 O  OD1 . ASP   O  70  ? 1.7859 0.8888 1.6808 -0.1527 -0.3550 0.1796  70  ASP   O OD1 
25147 O  OD2 . ASP   O  70  ? 1.8522 0.7446 1.5855 -0.1633 -0.4294 0.2823  70  ASP   O OD2 
25148 N  N   . ILE   O  71  ? 1.6234 0.3858 1.4913 -0.1429 -0.4352 0.1849  71  ILE   O N   
25149 C  CA  . ILE   O  71  ? 1.6277 0.4480 1.5072 -0.1684 -0.3978 0.0889  71  ILE   O CA  
25150 C  C   . ILE   O  71  ? 1.6673 0.4032 1.5059 -0.1605 -0.3736 0.0922  71  ILE   O C   
25151 O  O   . ILE   O  71  ? 1.6749 0.3991 1.5226 -0.1743 -0.3795 0.0964  71  ILE   O O   
25152 C  CB  . ILE   O  71  ? 1.6049 0.3707 1.4893 -0.1656 -0.4045 0.0567  71  ILE   O CB  
25153 C  CG1 . ILE   O  71  ? 1.5731 0.3536 1.4945 -0.1693 -0.4147 0.0450  71  ILE   O CG1 
25154 C  CG2 . ILE   O  71  ? 1.6203 0.3827 1.5100 -0.1648 -0.3878 0.0286  71  ILE   O CG2 
25155 C  CD1 . ILE   O  71  ? 1.5537 0.4035 1.5070 -0.1611 -0.3934 0.0281  71  ILE   O CD1 
25156 N  N   . GLY   O  72  ? 1.6576 0.4049 1.5107 -0.1666 -0.3544 0.0854  72  GLY   O N   
25157 C  CA  . GLY   O  72  ? 1.6375 0.4451 1.5326 -0.1758 -0.3670 0.1056  72  GLY   O CA  
25158 C  C   . GLY   O  72  ? 1.6237 0.4364 1.5445 -0.1791 -0.3763 0.1128  72  GLY   O C   
25159 O  O   . GLY   O  72  ? 1.6326 0.4186 1.5621 -0.2044 -0.4150 0.1383  72  GLY   O O   
25160 N  N   . ALA   O  73  ? 1.6276 0.4745 1.5538 -0.1810 -0.3785 0.1352  73  ALA   O N   
25161 C  CA  . ALA   O  73  ? 1.6989 0.4962 1.5588 -0.2012 -0.3693 0.0456  73  ALA   O CA  
25162 C  C   . ALA   O  73  ? 1.7536 0.4256 1.5692 -0.1749 -0.3562 0.0041  73  ALA   O C   
25163 O  O   . ALA   O  73  ? 1.7645 0.3419 1.6063 -0.1433 -0.3152 -0.0781 73  ALA   O O   
25164 C  CB  . ALA   O  73  ? 1.6866 0.5489 1.5513 -0.1688 -0.3509 0.0635  73  ALA   O CB  
25165 N  N   . VAL   O  74  ? 1.8388 0.4585 1.5283 -0.1520 -0.3646 -0.0205 74  VAL   O N   
25166 C  CA  . VAL   O  74  ? 1.8770 0.4790 1.4869 -0.1871 -0.3518 0.0061  74  VAL   O CA  
25167 C  C   . VAL   O  74  ? 1.8599 0.4036 1.5494 -0.1603 -0.3855 0.0071  74  VAL   O C   
25168 O  O   . VAL   O  74  ? 1.8865 0.3885 1.5438 -0.1304 -0.3843 -0.0130 74  VAL   O O   
25169 C  CB  . VAL   O  74  ? 1.9300 0.4433 1.4160 -0.2118 -0.3421 0.0305  74  VAL   O CB  
25170 C  CG1 . VAL   O  74  ? 1.9187 0.4145 1.4236 -0.2178 -0.3588 0.0520  74  VAL   O CG1 
25171 C  CG2 . VAL   O  74  ? 1.9896 0.4824 1.3941 -0.2077 -0.3144 0.0345  74  VAL   O CG2 
25172 N  N   . TYR   O  75  ? 1.8110 0.4544 1.5480 -0.1719 -0.4125 0.0309  75  TYR   O N   
25173 C  CA  . TYR   O  75  ? 1.7773 0.5324 1.5230 -0.1784 -0.4275 0.0221  75  TYR   O CA  
25174 C  C   . TYR   O  75  ? 1.7970 0.5469 1.4873 -0.1350 -0.4362 0.0550  75  TYR   O C   
25175 O  O   . TYR   O  75  ? 1.8052 0.5747 1.4269 -0.1059 -0.4971 0.1062  75  TYR   O O   
25176 C  CB  . TYR   O  75  ? 1.8010 0.5492 1.4990 -0.2068 -0.4443 0.0165  75  TYR   O CB  
25177 C  CG  . TYR   O  75  ? 1.7844 0.5091 1.4722 -0.2018 -0.4247 -0.0017 75  TYR   O CG  
25178 C  CD1 . TYR   O  75  ? 1.7980 0.5031 1.4593 -0.2246 -0.4247 -0.0083 75  TYR   O CD1 
25179 C  CD2 . TYR   O  75  ? 1.8138 0.4772 1.4787 -0.1940 -0.4025 0.0121  75  TYR   O CD2 
25180 C  CE1 . TYR   O  75  ? 1.8142 0.4812 1.4195 -0.2092 -0.3972 -0.0354 75  TYR   O CE1 
25181 C  CE2 . TYR   O  75  ? 1.8312 0.4872 1.4343 -0.1836 -0.3773 -0.0196 75  TYR   O CE2 
25182 C  CZ  . TYR   O  75  ? 1.8332 0.4733 1.3918 -0.1981 -0.4202 -0.0322 75  TYR   O CZ  
25183 O  OH  . TYR   O  75  ? 1.7941 0.5548 1.3340 -0.1874 -0.4142 -0.0831 75  TYR   O OH  
25184 N  N   . SER   O  76  ? 1.7830 0.5319 1.4987 -0.0905 -0.4450 0.0842  76  SER   O N   
25185 C  CA  . SER   O  76  ? 1.7516 0.5538 1.5096 -0.0749 -0.4292 0.1096  76  SER   O CA  
25186 C  C   . SER   O  76  ? 1.7402 0.5082 1.4629 -0.0535 -0.4581 0.1068  76  SER   O C   
25187 O  O   . SER   O  76  ? 1.7121 0.5617 1.4578 -0.0752 -0.4560 0.1032  76  SER   O O   
25188 C  CB  . SER   O  76  ? 1.7349 0.5579 1.5578 -0.1057 -0.4285 0.1295  76  SER   O CB  
25189 O  OG  . SER   O  76  ? 1.7172 0.5599 1.6060 -0.1246 -0.4395 0.1426  76  SER   O OG  
25190 N  N   . GLY   O  77  ? 1.7232 0.4221 1.4477 -0.0475 -0.4361 0.0800  77  GLY   O N   
25191 C  CA  . GLY   O  77  ? 1.7291 0.3831 1.4250 -0.0281 -0.4331 0.1181  77  GLY   O CA  
25192 C  C   . GLY   O  77  ? 1.7374 0.3216 1.3770 -0.0002 -0.4222 0.1545  77  GLY   O C   
25193 O  O   . GLY   O  77  ? 1.7157 0.1545 1.4497 -0.0115 -0.3902 0.2289  77  GLY   O O   
25194 N  N   . MET   O  78  ? 1.7372 0.3821 1.3477 0.0038  -0.4027 0.1962  78  MET   O N   
25195 C  CA  . MET   O  78  ? 1.7519 0.4690 1.2968 0.0157  -0.4027 0.2109  78  MET   O CA  
25196 C  C   . MET   O  78  ? 1.7489 0.4723 1.2625 -0.0164 -0.3996 0.1968  78  MET   O C   
25197 O  O   . MET   O  78  ? 1.7162 0.4256 1.3003 -0.0181 -0.4342 0.1793  78  MET   O O   
25198 C  CB  . MET   O  78  ? 1.7486 0.4854 1.2549 0.0492  -0.4056 0.2391  78  MET   O CB  
25199 C  CG  . MET   O  78  ? 1.7577 0.4941 1.2341 0.0665  -0.3959 0.2494  78  MET   O CG  
25200 S  SD  . MET   O  78  ? 1.7657 0.5419 1.1794 0.0908  -0.4035 0.2632  78  MET   O SD  
25201 C  CE  . MET   O  78  ? 1.7631 0.5991 1.2094 0.0938  -0.4160 0.2347  78  MET   O CE  
25202 N  N   . GLY   O  79  ? 1.7713 0.5374 1.2698 -0.0352 -0.3786 0.1653  79  GLY   O N   
25203 C  CA  . GLY   O  79  ? 1.7090 0.4915 1.2783 -0.0834 -0.3695 0.1776  79  GLY   O CA  
25204 C  C   . GLY   O  79  ? 1.6544 0.4961 1.2614 -0.0746 -0.3864 0.1423  79  GLY   O C   
25205 O  O   . GLY   O  79  ? 1.5709 0.4516 1.2295 -0.0849 -0.4217 0.0602  79  GLY   O O   
25206 N  N   . PRO   O  80  ? 1.6468 0.5011 1.2868 -0.0985 -0.3948 0.1387  80  PRO   O N   
25207 C  CA  . PRO   O  80  ? 1.6148 0.5290 1.3369 -0.0983 -0.3839 0.1008  80  PRO   O CA  
25208 C  C   . PRO   O  80  ? 1.6185 0.5233 1.3241 -0.0881 -0.3618 0.0795  80  PRO   O C   
25209 O  O   . PRO   O  80  ? 1.5927 0.5200 1.3883 -0.0151 -0.3366 0.1097  80  PRO   O O   
25210 C  CB  . PRO   O  80  ? 1.6381 0.5273 1.3238 -0.0867 -0.3917 0.1519  80  PRO   O CB  
25211 C  CG  . PRO   O  80  ? 1.6381 0.5040 1.3510 -0.0900 -0.3988 0.1527  80  PRO   O CG  
25212 C  CD  . PRO   O  80  ? 1.6485 0.4918 1.3217 -0.1101 -0.3970 0.1555  80  PRO   O CD  
25213 N  N   . ASP   O  81  ? 1.6313 0.5914 1.3427 -0.1236 -0.3514 0.0412  81  ASP   O N   
25214 C  CA  . ASP   O  81  ? 1.6210 0.5643 1.3450 -0.1122 -0.3586 0.0420  81  ASP   O CA  
25215 C  C   . ASP   O  81  ? 1.6450 0.4415 1.3198 -0.1252 -0.3472 0.0035  81  ASP   O C   
25216 O  O   . ASP   O  81  ? 1.6436 0.3921 1.3015 -0.1589 -0.3409 -0.0506 81  ASP   O O   
25217 C  CB  . ASP   O  81  ? 1.6587 0.6443 1.3349 -0.1408 -0.3312 0.0098  81  ASP   O CB  
25218 C  CG  . ASP   O  81  ? 1.6516 0.7402 1.3712 -0.1519 -0.3006 -0.0075 81  ASP   O CG  
25219 O  OD1 . ASP   O  81  ? 1.6626 0.8921 1.4378 -0.2171 -0.3078 -0.0886 81  ASP   O OD1 
25220 O  OD2 . ASP   O  81  ? 1.7146 0.7346 1.3906 -0.1879 -0.2217 -0.0080 81  ASP   O OD2 
25221 N  N   . TYR   O  82  ? 1.6613 0.3841 1.3396 -0.1106 -0.3350 0.0379  82  TYR   O N   
25222 C  CA  . TYR   O  82  ? 1.6782 0.4298 1.3688 -0.0876 -0.3441 0.0690  82  TYR   O CA  
25223 C  C   . TYR   O  82  ? 1.6639 0.4660 1.3679 -0.0747 -0.3451 0.0406  82  TYR   O C   
25224 O  O   . TYR   O  82  ? 1.6249 0.5295 1.3477 0.0007  -0.3524 0.0252  82  TYR   O O   
25225 C  CB  . TYR   O  82  ? 1.6779 0.3741 1.3734 -0.0699 -0.3503 0.0648  82  TYR   O CB  
25226 C  CG  . TYR   O  82  ? 1.6908 0.3246 1.3432 -0.0541 -0.3857 0.0672  82  TYR   O CG  
25227 C  CD1 . TYR   O  82  ? 1.6873 0.2996 1.3652 -0.0408 -0.3915 0.0648  82  TYR   O CD1 
25228 C  CD2 . TYR   O  82  ? 1.6923 0.3088 1.3463 -0.0347 -0.3968 0.0410  82  TYR   O CD2 
25229 C  CE1 . TYR   O  82  ? 1.6898 0.3075 1.3716 -0.0481 -0.3722 0.0576  82  TYR   O CE1 
25230 C  CE2 . TYR   O  82  ? 1.6835 0.3003 1.3395 -0.0421 -0.4026 0.0478  82  TYR   O CE2 
25231 C  CZ  . TYR   O  82  ? 1.6849 0.3071 1.3468 -0.0583 -0.4008 0.0656  82  TYR   O CZ  
25232 O  OH  . TYR   O  82  ? 1.6981 0.2911 1.3477 -0.0636 -0.3728 0.0467  82  TYR   O OH  
25233 N  N   . ARG   O  83  ? 1.6661 0.5783 1.3838 -0.0647 -0.3551 0.0849  83  ARG   O N   
25234 C  CA  . ARG   O  83  ? 1.6612 0.5522 1.4127 -0.0583 -0.3340 0.0914  83  ARG   O CA  
25235 C  C   . ARG   O  83  ? 1.6851 0.5400 1.4579 -0.1016 -0.3504 0.0757  83  ARG   O C   
25236 O  O   . ARG   O  83  ? 1.6674 0.4312 1.5234 -0.2112 -0.3369 0.1670  83  ARG   O O   
25237 C  CB  . ARG   O  83  ? 1.6540 0.6603 1.4365 -0.0170 -0.3470 0.0960  83  ARG   O CB  
25238 C  CG  . ARG   O  83  ? 1.6244 0.7028 1.4032 -0.0063 -0.3615 0.0980  83  ARG   O CG  
25239 C  CD  . ARG   O  83  ? 1.6705 0.7569 1.4023 0.0109  -0.3541 0.1419  83  ARG   O CD  
25240 N  NE  . ARG   O  83  ? 1.6807 0.7769 1.3848 0.0416  -0.3643 0.1376  83  ARG   O NE  
25241 C  CZ  . ARG   O  83  ? 1.7211 0.7738 1.4256 0.0503  -0.3605 0.1247  83  ARG   O CZ  
25242 N  NH1 . ARG   O  83  ? 1.7491 0.7832 1.4473 0.0319  -0.3425 0.1196  83  ARG   O NH1 
25243 N  NH2 . ARG   O  83  ? 1.7138 0.8316 1.4480 0.0326  -0.3774 0.1361  83  ARG   O NH2 
25244 N  N   . VAL   O  84  ? 1.6926 0.4406 1.4304 -0.1179 -0.3573 0.0318  84  VAL   O N   
25245 C  CA  . VAL   O  84  ? 1.6933 0.4424 1.4329 -0.1422 -0.3663 0.0074  84  VAL   O CA  
25246 C  C   . VAL   O  84  ? 1.7333 0.5258 1.4170 -0.1531 -0.3779 -0.0023 84  VAL   O C   
25247 O  O   . VAL   O  84  ? 1.7776 0.5550 1.4152 -0.1733 -0.3633 0.0305  84  VAL   O O   
25248 C  CB  . VAL   O  84  ? 1.6964 0.4134 1.4328 -0.1258 -0.3948 -0.0102 84  VAL   O CB  
25249 C  CG1 . VAL   O  84  ? 1.7149 0.3996 1.4160 -0.1131 -0.3891 -0.0247 84  VAL   O CG1 
25250 C  CG2 . VAL   O  84  ? 1.7014 0.4489 1.4262 -0.1199 -0.3920 -0.0228 84  VAL   O CG2 
25251 N  N   . LEU   O  85  ? 1.7288 0.5585 1.3777 -0.1446 -0.4104 0.0120  85  LEU   O N   
25252 C  CA  . LEU   O  85  ? 1.7179 0.5999 1.3873 -0.1043 -0.3933 0.0469  85  LEU   O CA  
25253 C  C   . LEU   O  85  ? 1.7096 0.5716 1.3786 -0.1004 -0.4181 0.0520  85  LEU   O C   
25254 O  O   . LEU   O  85  ? 1.6792 0.6108 1.3728 -0.0516 -0.4111 0.0533  85  LEU   O O   
25255 C  CB  . LEU   O  85  ? 1.7708 0.6356 1.3629 -0.1411 -0.4143 0.0561  85  LEU   O CB  
25256 C  CG  . LEU   O  85  ? 1.7954 0.6584 1.3358 -0.1471 -0.4115 0.0699  85  LEU   O CG  
25257 C  CD1 . LEU   O  85  ? 1.8193 0.6287 1.3406 -0.1306 -0.4396 0.0915  85  LEU   O CD1 
25258 C  CD2 . LEU   O  85  ? 1.7978 0.7030 1.3437 -0.1627 -0.3991 0.0877  85  LEU   O CD2 
25259 N  N   . VAL   O  86  ? 1.6811 0.5538 1.3921 -0.0888 -0.4065 0.0269  86  VAL   O N   
25260 C  CA  . VAL   O  86  ? 1.6519 0.6453 1.4330 -0.0734 -0.3901 0.0330  86  VAL   O CA  
25261 C  C   . VAL   O  86  ? 1.6074 0.7170 1.4791 -0.1362 -0.4209 0.0418  86  VAL   O C   
25262 O  O   . VAL   O  86  ? 1.4723 0.7763 1.4911 -0.1478 -0.4861 0.0418  86  VAL   O O   
25263 C  CB  . VAL   O  86  ? 1.6711 0.5706 1.4628 -0.0798 -0.3692 0.0295  86  VAL   O CB  
25264 C  CG1 . VAL   O  86  ? 1.6525 0.6764 1.4777 -0.0594 -0.3472 0.0143  86  VAL   O CG1 
25265 C  CG2 . VAL   O  86  ? 1.6798 0.5830 1.4338 -0.0862 -0.3706 0.0165  86  VAL   O CG2 
25266 N  N   . ASP   O  87  ? 1.5929 0.7981 1.5039 -0.1499 -0.4091 0.0303  87  ASP   O N   
25267 C  CA  . ASP   O  87  ? 1.6315 0.7681 1.4735 -0.1333 -0.3866 0.0112  87  ASP   O CA  
25268 C  C   . ASP   O  87  ? 1.6666 0.7463 1.4905 -0.1156 -0.3579 0.0203  87  ASP   O C   
25269 O  O   . ASP   O  87  ? 1.6867 0.7838 1.4178 -0.0731 -0.3761 0.1457  87  ASP   O O   
25270 C  CB  . ASP   O  87  ? 1.6272 0.7803 1.4736 -0.1162 -0.3946 -0.0386 87  ASP   O CB  
25271 C  CG  . ASP   O  87  ? 1.6060 0.8314 1.4545 -0.1249 -0.3828 -0.0657 87  ASP   O CG  
25272 O  OD1 . ASP   O  87  ? 1.5501 0.8939 1.4387 -0.1730 -0.3822 -0.0382 87  ASP   O OD1 
25273 O  OD2 . ASP   O  87  ? 1.6637 0.7765 1.4471 -0.1062 -0.3815 -0.0938 87  ASP   O OD2 
25274 N  N   . LYS   O  88  ? 1.6493 0.6932 1.4785 -0.1357 -0.3594 0.0317  88  LYS   O N   
25275 C  CA  . LYS   O  88  ? 1.5926 0.6072 1.4616 -0.1358 -0.3670 -0.0027 88  LYS   O CA  
25276 C  C   . LYS   O  88  ? 1.5923 0.5598 1.4763 -0.1383 -0.3759 -0.0119 88  LYS   O C   
25277 O  O   . LYS   O  88  ? 1.5322 0.5722 1.4672 -0.0732 -0.4060 -0.0066 88  LYS   O O   
25278 C  CB  . LYS   O  88  ? 1.5846 0.5952 1.4659 -0.1748 -0.3583 -0.0276 88  LYS   O CB  
25279 C  CG  . LYS   O  88  ? 1.5606 0.6302 1.4842 -0.2012 -0.3405 -0.0658 88  LYS   O CG  
25280 C  CD  . LYS   O  88  ? 1.5766 0.6943 1.4968 -0.2116 -0.3150 -0.1348 88  LYS   O CD  
25281 C  CE  . LYS   O  88  ? 1.5564 0.7474 1.5263 -0.2293 -0.3185 -0.1531 88  LYS   O CE  
25282 N  NZ  . LYS   O  88  ? 1.5608 0.7663 1.5835 -0.2435 -0.2961 -0.1795 88  LYS   O NZ  
25283 N  N   . SER   O  89  ? 1.6369 0.4856 1.4555 -0.1400 -0.3816 0.0133  89  SER   O N   
25284 C  CA  . SER   O  89  ? 1.6738 0.5040 1.4140 -0.1439 -0.4021 0.0391  89  SER   O CA  
25285 C  C   . SER   O  89  ? 1.6867 0.5395 1.4078 -0.1425 -0.3723 0.0188  89  SER   O C   
25286 O  O   . SER   O  89  ? 1.6807 0.6389 1.4063 -0.1261 -0.3959 0.0352  89  SER   O O   
25287 C  CB  . SER   O  89  ? 1.7058 0.5036 1.3990 -0.1655 -0.4292 0.0098  89  SER   O CB  
25288 O  OG  . SER   O  89  ? 1.7122 0.6214 1.3439 -0.1968 -0.4677 -0.0922 89  SER   O OG  
25289 N  N   . ARG   O  90  ? 1.6913 0.5059 1.4081 -0.1560 -0.3489 0.0101  90  ARG   O N   
25290 C  CA  . ARG   O  90  ? 1.6921 0.4985 1.4153 -0.1665 -0.3603 -0.0026 90  ARG   O CA  
25291 C  C   . ARG   O  90  ? 1.6579 0.4377 1.3716 -0.1285 -0.3931 -0.0247 90  ARG   O C   
25292 O  O   . ARG   O  90  ? 1.6698 0.3137 1.3607 -0.2162 -0.4299 -0.0211 90  ARG   O O   
25293 C  CB  . ARG   O  90  ? 1.7326 0.5029 1.4224 -0.1446 -0.3492 0.0117  90  ARG   O CB  
25294 C  CG  . ARG   O  90  ? 1.7440 0.4644 1.4653 -0.1357 -0.3509 0.0144  90  ARG   O CG  
25295 C  CD  . ARG   O  90  ? 1.7412 0.4150 1.4795 -0.0969 -0.3526 0.0215  90  ARG   O CD  
25296 N  NE  . ARG   O  90  ? 1.7523 0.2729 1.5091 -0.0546 -0.3467 0.0295  90  ARG   O NE  
25297 C  CZ  . ARG   O  90  ? 1.7499 0.2122 1.5406 0.0468  -0.3463 0.0356  90  ARG   O CZ  
25298 N  NH1 . ARG   O  90  ? 1.7380 0.1465 1.5737 0.0562  -0.3495 0.0474  90  ARG   O NH1 
25299 N  NH2 . ARG   O  90  ? 1.7125 0.3039 1.5703 0.0642  -0.3128 0.0051  90  ARG   O NH2 
25300 N  N   . LYS   O  91  ? 1.6606 0.4655 1.3801 -0.1352 -0.3666 -0.0677 91  LYS   O N   
25301 C  CA  . LYS   O  91  ? 1.6466 0.4638 1.4197 -0.1169 -0.3504 -0.0493 91  LYS   O CA  
25302 C  C   . LYS   O  91  ? 1.7016 0.5194 1.4142 -0.1210 -0.3665 -0.0603 91  LYS   O C   
25303 O  O   . LYS   O  91  ? 1.7465 0.5425 1.4323 -0.1472 -0.3854 -0.0161 91  LYS   O O   
25304 C  CB  . LYS   O  91  ? 1.6343 0.5045 1.4611 -0.0984 -0.3242 -0.0812 91  LYS   O CB  
25305 C  CG  . LYS   O  91  ? 1.5946 0.5079 1.5392 -0.0861 -0.3112 -0.0959 91  LYS   O CG  
25306 C  CD  . LYS   O  91  ? 1.5891 0.6057 1.5936 -0.0808 -0.2811 -0.1271 91  LYS   O CD  
25307 C  CE  . LYS   O  91  ? 1.5782 0.6741 1.6631 -0.1241 -0.2540 -0.1180 91  LYS   O CE  
25308 N  NZ  . LYS   O  91  ? 1.5717 0.7893 1.6919 -0.1172 -0.2314 -0.1169 91  LYS   O NZ  
25309 N  N   . VAL   O  92  ? 1.7180 0.5029 1.3828 -0.1253 -0.3728 -0.0349 92  VAL   O N   
25310 C  CA  . VAL   O  92  ? 1.7283 0.5061 1.3895 -0.1045 -0.3553 -0.0040 92  VAL   O CA  
25311 C  C   . VAL   O  92  ? 1.7248 0.5117 1.3731 -0.1025 -0.3503 0.0049  92  VAL   O C   
25312 O  O   . VAL   O  92  ? 1.7924 0.5723 1.2572 -0.0769 -0.3922 -0.0616 92  VAL   O O   
25313 C  CB  . VAL   O  92  ? 1.7317 0.4945 1.3861 -0.1253 -0.3351 0.0011  92  VAL   O CB  
25314 C  CG1 . VAL   O  92  ? 1.7550 0.5027 1.4145 -0.1414 -0.3339 -0.0249 92  VAL   O CG1 
25315 C  CG2 . VAL   O  92  ? 1.7147 0.4808 1.3823 -0.0924 -0.3348 0.0045  92  VAL   O CG2 
25316 N  N   . ALA   O  93  ? 1.6792 0.4587 1.4004 -0.0874 -0.3706 0.0496  93  ALA   O N   
25317 C  CA  . ALA   O  93  ? 1.6863 0.4826 1.4423 -0.0733 -0.3835 0.0788  93  ALA   O CA  
25318 C  C   . ALA   O  93  ? 1.6918 0.4770 1.5429 -0.0620 -0.3788 0.0972  93  ALA   O C   
25319 O  O   . ALA   O  93  ? 1.6708 0.6637 1.6648 -0.0532 -0.4707 0.1082  93  ALA   O O   
25320 C  CB  . ALA   O  93  ? 1.6858 0.4679 1.4286 -0.0616 -0.3802 0.0650  93  ALA   O CB  
25321 N  N   . HIS   O  94  ? 1.6496 0.4620 1.5503 -0.0346 -0.3853 0.1393  94  HIS   O N   
25322 C  CA  . HIS   O  94  ? 1.6393 0.4436 1.5620 -0.0235 -0.3497 0.1495  94  HIS   O CA  
25323 C  C   . HIS   O  94  ? 1.5986 0.4088 1.6128 -0.0569 -0.3560 0.1457  94  HIS   O C   
25324 O  O   . HIS   O  94  ? 1.6159 0.5119 1.6145 -0.0660 -0.3445 0.2289  94  HIS   O O   
25325 C  CB  . HIS   O  94  ? 1.6609 0.3524 1.5455 0.0167  -0.3359 0.1482  94  HIS   O CB  
25326 C  CG  . HIS   O  94  ? 1.7046 0.3798 1.5507 0.0407  -0.3133 0.1729  94  HIS   O CG  
25327 N  ND1 . HIS   O  94  ? 1.7054 0.3922 1.5629 0.0186  -0.2801 0.1408  94  HIS   O ND1 
25328 C  CD2 . HIS   O  94  ? 1.7168 0.4543 1.5500 0.0686  -0.2650 0.1775  94  HIS   O CD2 
25329 C  CE1 . HIS   O  94  ? 1.7331 0.4170 1.5838 0.0345  -0.2631 0.1287  94  HIS   O CE1 
25330 N  NE2 . HIS   O  94  ? 1.7512 0.4069 1.5680 0.0568  -0.2595 0.1841  94  HIS   O NE2 
25331 N  N   . THR   O  95  ? 1.5818 0.3707 1.5969 -0.0703 -0.3725 0.1607  95  THR   O N   
25332 C  CA  . THR   O  95  ? 1.5751 0.4394 1.5821 -0.0676 -0.3628 0.1508  95  THR   O CA  
25333 C  C   . THR   O  95  ? 1.5864 0.4700 1.5912 -0.0739 -0.4048 0.0946  95  THR   O C   
25334 O  O   . THR   O  95  ? 1.5861 0.5812 1.6000 -0.0638 -0.4178 0.2035  95  THR   O O   
25335 C  CB  . THR   O  95  ? 1.5700 0.4869 1.5820 -0.0565 -0.3363 0.1487  95  THR   O CB  
25336 O  OG1 . THR   O  95  ? 1.5182 0.6044 1.5704 -0.1514 -0.3088 0.0344  95  THR   O OG1 
25337 C  CG2 . THR   O  95  ? 1.5979 0.5374 1.5675 -0.0628 -0.3249 0.1321  95  THR   O CG2 
25338 N  N   . SER   O  96  ? 1.6450 0.4441 1.5146 -0.0476 -0.4173 0.1058  96  SER   O N   
25339 C  CA  . SER   O  96  ? 1.6840 0.4541 1.5177 -0.0589 -0.4254 0.0655  96  SER   O CA  
25340 C  C   . SER   O  96  ? 1.7035 0.4211 1.4051 -0.0390 -0.4497 0.0253  96  SER   O C   
25341 O  O   . SER   O  96  ? 1.7172 0.3488 1.4046 0.0047  -0.4627 0.0251  96  SER   O O   
25342 C  CB  . SER   O  96  ? 1.7277 0.4343 1.5018 -0.0786 -0.4371 0.0775  96  SER   O CB  
25343 O  OG  . SER   O  96  ? 1.7960 0.5900 1.5459 -0.1372 -0.4085 0.1666  96  SER   O OG  
25344 N  N   . TYR   O  97  ? 1.6648 0.4579 1.4445 -0.0415 -0.4337 0.0353  97  TYR   O N   
25345 C  CA  . TYR   O  97  ? 1.6678 0.4547 1.4459 -0.0352 -0.4358 0.0606  97  TYR   O CA  
25346 C  C   . TYR   O  97  ? 1.6768 0.4712 1.4430 -0.0322 -0.4188 0.0582  97  TYR   O C   
25347 O  O   . TYR   O  97  ? 1.7238 0.4971 1.4272 -0.0184 -0.4473 0.0629  97  TYR   O O   
25348 C  CB  . TYR   O  97  ? 1.6725 0.4547 1.4807 -0.0374 -0.4274 0.0561  97  TYR   O CB  
25349 C  CG  . TYR   O  97  ? 1.6629 0.4794 1.5400 -0.0018 -0.4278 0.0620  97  TYR   O CG  
25350 C  CD1 . TYR   O  97  ? 1.6770 0.5148 1.5891 0.0059  -0.4042 0.0486  97  TYR   O CD1 
25351 C  CD2 . TYR   O  97  ? 1.6891 0.4863 1.5662 0.0094  -0.3931 0.0225  97  TYR   O CD2 
25352 C  CE1 . TYR   O  97  ? 1.6407 0.5620 1.6332 0.0113  -0.3938 0.0181  97  TYR   O CE1 
25353 C  CE2 . TYR   O  97  ? 1.6659 0.5193 1.6208 0.0049  -0.3995 -0.0046 97  TYR   O CE2 
25354 C  CZ  . TYR   O  97  ? 1.6248 0.5576 1.6453 0.0016  -0.4210 -0.0044 97  TYR   O CZ  
25355 O  OH  . TYR   O  97  ? 1.6125 0.6108 1.6420 -0.0038 -0.4301 -0.0671 97  TYR   O OH  
25356 N  N   . LYS   O  98  ? 1.6768 0.4436 1.4575 -0.0373 -0.3625 0.0547  98  LYS   O N   
25357 C  CA  . LYS   O  98  ? 1.6830 0.4784 1.4793 -0.0413 -0.3163 0.0517  98  LYS   O CA  
25358 C  C   . LYS   O  98  ? 1.6737 0.4518 1.4636 -0.0181 -0.3010 0.0143  98  LYS   O C   
25359 O  O   . LYS   O  98  ? 1.6669 0.3990 1.3983 -0.0474 -0.2869 -0.0571 98  LYS   O O   
25360 C  CB  . LYS   O  98  ? 1.7148 0.5195 1.4832 -0.0480 -0.2830 0.0538  98  LYS   O CB  
25361 C  CG  . LYS   O  98  ? 1.7570 0.5460 1.5227 -0.0332 -0.2542 0.0468  98  LYS   O CG  
25362 C  CD  . LYS   O  98  ? 1.8114 0.5925 1.5236 -0.0323 -0.2376 0.0355  98  LYS   O CD  
25363 C  CE  . LYS   O  98  ? 1.8448 0.5657 1.5794 -0.0255 -0.2146 0.0260  98  LYS   O CE  
25364 N  NZ  . LYS   O  98  ? 1.8794 0.5576 1.5753 -0.0306 -0.1813 0.0114  98  LYS   O NZ  
25365 N  N   . ARG   O  99  ? 1.6694 0.3934 1.4778 -0.0419 -0.2928 0.0049  99  ARG   O N   
25366 C  CA  . ARG   O  99  ? 1.6490 0.4017 1.4825 -0.0423 -0.2847 0.0077  99  ARG   O CA  
25367 C  C   . ARG   O  99  ? 1.6455 0.4138 1.4815 -0.0544 -0.2800 0.0163  99  ARG   O C   
25368 O  O   . ARG   O  99  ? 1.6572 0.3865 1.4003 -0.0233 -0.2572 0.0533  99  ARG   O O   
25369 C  CB  . ARG   O  99  ? 1.6476 0.3822 1.5365 -0.0356 -0.2829 0.0090  99  ARG   O CB  
25370 C  CG  . ARG   O  99  ? 1.6486 0.3723 1.5526 -0.0176 -0.2820 0.0413  99  ARG   O CG  
25371 C  CD  . ARG   O  99  ? 1.6554 0.3881 1.5921 0.0021  -0.2795 0.0421  99  ARG   O CD  
25372 N  NE  . ARG   O  99  ? 1.6285 0.4556 1.5932 0.0035  -0.2751 0.0492  99  ARG   O NE  
25373 C  CZ  . ARG   O  99  ? 1.5381 0.5634 1.6600 -0.0191 -0.2551 0.0075  99  ARG   O CZ  
25374 N  NH1 . ARG   O  99  ? 1.5353 0.5577 1.6915 -0.0465 -0.2462 -0.0015 99  ARG   O NH1 
25375 N  NH2 . ARG   O  99  ? 1.5507 0.6595 1.6383 -0.0130 -0.2777 0.0043  99  ARG   O NH2 
25376 N  N   . ILE   O  100 ? 1.6318 0.4386 1.4592 -0.0541 -0.3045 0.0553  100 ILE   O N   
25377 C  CA  . ILE   O  100 ? 1.6319 0.4213 1.4736 -0.0328 -0.3024 0.0742  100 ILE   O CA  
25378 C  C   . ILE   O  100 ? 1.6337 0.4177 1.4740 -0.0415 -0.3161 0.0825  100 ILE   O C   
25379 O  O   . ILE   O  100 ? 1.7150 0.4289 1.4753 0.0235  -0.3197 0.0719  100 ILE   O O   
25380 C  CB  . ILE   O  100 ? 1.6274 0.4352 1.4336 -0.0130 -0.3115 0.0906  100 ILE   O CB  
25381 C  CG1 . ILE   O  100 ? 1.6313 0.4979 1.4502 -0.0075 -0.3093 0.0712  100 ILE   O CG1 
25382 C  CG2 . ILE   O  100 ? 1.6152 0.4557 1.4413 0.0079  -0.3094 0.1012  100 ILE   O CG2 
25383 C  CD1 . ILE   O  100 ? 1.6663 0.6012 1.4323 -0.0049 -0.2989 0.0092  100 ILE   O CD1 
25384 N  N   . TYR   O  101 ? 1.6294 0.3702 1.4863 -0.0446 -0.3540 0.0718  101 TYR   O N   
25385 C  CA  . TYR   O  101 ? 1.6134 0.3799 1.5054 -0.0621 -0.3435 0.0694  101 TYR   O CA  
25386 C  C   . TYR   O  101 ? 1.6397 0.3389 1.5435 -0.0991 -0.3210 0.0208  101 TYR   O C   
25387 O  O   . TYR   O  101 ? 1.6169 0.2239 1.5436 -0.1489 -0.2970 0.0078  101 TYR   O O   
25388 C  CB  . TYR   O  101 ? 1.5837 0.4010 1.4765 -0.0501 -0.3777 0.0723  101 TYR   O CB  
25389 C  CG  . TYR   O  101 ? 1.5653 0.3760 1.4464 -0.0322 -0.3992 0.0996  101 TYR   O CG  
25390 C  CD1 . TYR   O  101 ? 1.5639 0.3850 1.4405 -0.0453 -0.3959 0.0997  101 TYR   O CD1 
25391 C  CD2 . TYR   O  101 ? 1.5555 0.3687 1.4025 -0.0394 -0.4100 0.0777  101 TYR   O CD2 
25392 C  CE1 . TYR   O  101 ? 1.5543 0.3528 1.4216 -0.0298 -0.4212 0.0925  101 TYR   O CE1 
25393 C  CE2 . TYR   O  101 ? 1.5498 0.3755 1.3851 -0.0311 -0.4221 0.0849  101 TYR   O CE2 
25394 C  CZ  . TYR   O  101 ? 1.5479 0.3599 1.4009 -0.0248 -0.4265 0.0897  101 TYR   O CZ  
25395 O  OH  . TYR   O  101 ? 1.5242 0.4039 1.4033 0.0082  -0.4257 0.1169  101 TYR   O OH  
25396 N  N   . GLY   O  102 ? 1.6299 0.3990 1.5520 -0.0752 -0.3250 0.0109  102 GLY   O N   
25397 C  CA  . GLY   O  102 ? 1.6503 0.5409 1.5815 -0.0276 -0.3034 0.0115  102 GLY   O CA  
25398 C  C   . GLY   O  102 ? 1.6414 0.5857 1.6162 -0.0438 -0.3394 0.0161  102 GLY   O C   
25399 O  O   . GLY   O  102 ? 1.6919 0.6894 1.6718 -0.0137 -0.3184 -0.0421 102 GLY   O O   
25400 N  N   . GLU   O  103 ? 1.6800 0.5826 1.5844 -0.0219 -0.3830 0.0340  103 GLU   O N   
25401 C  CA  . GLU   O  103 ? 1.6730 0.6529 1.5763 -0.0440 -0.4081 0.0665  103 GLU   O CA  
25402 C  C   . GLU   O  103 ? 1.6652 0.6169 1.5198 -0.0769 -0.4112 0.0769  103 GLU   O C   
25403 O  O   . GLU   O  103 ? 1.6667 0.6056 1.4840 -0.0570 -0.4217 0.0156  103 GLU   O O   
25404 C  CB  . GLU   O  103 ? 1.7269 0.7283 1.6022 -0.0335 -0.4511 0.0736  103 GLU   O CB  
25405 C  CG  . GLU   O  103 ? 1.7838 0.7992 1.6151 -0.0353 -0.4535 0.0361  103 GLU   O CG  
25406 C  CD  . GLU   O  103 ? 1.8289 1.0088 1.6555 -0.0225 -0.5245 0.0309  103 GLU   O CD  
25407 O  OE1 . GLU   O  103 ? 1.8710 1.0380 1.6594 0.0262  -0.5306 0.0756  103 GLU   O OE1 
25408 O  OE2 . GLU   O  103 ? 1.9569 1.0298 1.6803 -0.0228 -0.5790 -0.0029 103 GLU   O OE2 
25409 N  N   . TYR   O  104 ? 1.6680 0.5824 1.4981 -0.0429 -0.4484 0.1204  104 TYR   O N   
25410 C  CA  . TYR   O  104 ? 1.6393 0.5532 1.5186 -0.0867 -0.4207 0.1606  104 TYR   O CA  
25411 C  C   . TYR   O  104 ? 1.5574 0.5100 1.4786 -0.0703 -0.4168 0.2139  104 TYR   O C   
25412 O  O   . TYR   O  104 ? 1.5546 0.4231 1.4922 -0.0828 -0.3987 0.2938  104 TYR   O O   
25413 C  CB  . TYR   O  104 ? 1.6882 0.5892 1.5178 -0.1170 -0.4023 0.1415  104 TYR   O CB  
25414 C  CG  . TYR   O  104 ? 1.7462 0.5498 1.5433 -0.1322 -0.4246 0.1243  104 TYR   O CG  
25415 C  CD1 . TYR   O  104 ? 1.7823 0.4548 1.4866 -0.1107 -0.4302 0.1502  104 TYR   O CD1 
25416 C  CD2 . TYR   O  104 ? 1.7687 0.5982 1.5603 -0.1278 -0.4122 0.0980  104 TYR   O CD2 
25417 C  CE1 . TYR   O  104 ? 1.8136 0.4748 1.4705 -0.0905 -0.4534 0.1848  104 TYR   O CE1 
25418 C  CE2 . TYR   O  104 ? 1.8064 0.6184 1.5364 -0.1043 -0.4215 0.1256  104 TYR   O CE2 
25419 C  CZ  . TYR   O  104 ? 1.8440 0.5256 1.5073 -0.0891 -0.4240 0.1658  104 TYR   O CZ  
25420 O  OH  . TYR   O  104 ? 1.8804 0.4326 1.5260 -0.1153 -0.4466 0.1758  104 TYR   O OH  
25421 N  N   . PRO   O  105 ? 1.5193 0.5749 1.5518 -0.0697 -0.3958 0.1957  105 PRO   O N   
25422 C  CA  . PRO   O  105 ? 1.5011 0.5883 1.5600 -0.0591 -0.4102 0.1854  105 PRO   O CA  
25423 C  C   . PRO   O  105 ? 1.4371 0.6379 1.6203 -0.0347 -0.4025 0.1667  105 PRO   O C   
25424 O  O   . PRO   O  105 ? 1.3377 0.6708 1.6783 0.0011  -0.3442 0.1721  105 PRO   O O   
25425 C  CB  . PRO   O  105 ? 1.5038 0.5292 1.5631 -0.0791 -0.4075 0.1542  105 PRO   O CB  
25426 C  CG  . PRO   O  105 ? 1.5308 0.5611 1.5682 -0.0923 -0.4230 0.1451  105 PRO   O CG  
25427 C  CD  . PRO   O  105 ? 1.5158 0.5912 1.5581 -0.0688 -0.4052 0.1555  105 PRO   O CD  
25428 N  N   . PRO   O  106 ? 1.4902 0.7230 1.5975 -0.0157 -0.3959 0.1668  106 PRO   O N   
25429 C  CA  . PRO   O  106 ? 1.5221 0.7116 1.6203 -0.0251 -0.3968 0.1804  106 PRO   O CA  
25430 C  C   . PRO   O  106 ? 1.5514 0.6638 1.6352 -0.0670 -0.4101 0.1851  106 PRO   O C   
25431 O  O   . PRO   O  106 ? 1.5219 0.6173 1.6669 -0.0607 -0.4781 0.1658  106 PRO   O O   
25432 C  CB  . PRO   O  106 ? 1.5195 0.8115 1.6318 -0.0174 -0.4080 0.1844  106 PRO   O CB  
25433 C  CG  . PRO   O  106 ? 1.5205 0.8268 1.6429 -0.0284 -0.3941 0.1603  106 PRO   O CG  
25434 C  CD  . PRO   O  106 ? 1.5099 0.7602 1.6245 -0.0400 -0.3635 0.1767  106 PRO   O CD  
25435 N  N   . THR   O  107 ? 1.6031 0.6382 1.6110 -0.0510 -0.3980 0.2134  107 THR   O N   
25436 C  CA  . THR   O  107 ? 1.6498 0.5787 1.5487 -0.1241 -0.3649 0.2213  107 THR   O CA  
25437 C  C   . THR   O  107 ? 1.6643 0.4848 1.5590 -0.1213 -0.3603 0.2295  107 THR   O C   
25438 O  O   . THR   O  107 ? 1.6745 0.3413 1.4903 -0.1205 -0.3370 0.2482  107 THR   O O   
25439 C  CB  . THR   O  107 ? 1.6767 0.5733 1.5360 -0.1559 -0.3704 0.1520  107 THR   O CB  
25440 O  OG1 . THR   O  107 ? 1.6695 0.5529 1.5419 -0.1411 -0.3639 0.1703  107 THR   O OG1 
25441 C  CG2 . THR   O  107 ? 1.6864 0.5486 1.5779 -0.1618 -0.3779 0.1216  107 THR   O CG2 
25442 N  N   . LYS   O  108 ? 1.6867 0.4903 1.5632 -0.1120 -0.3590 0.2191  108 LYS   O N   
25443 C  CA  . LYS   O  108 ? 1.7148 0.5247 1.5961 -0.0715 -0.3277 0.2376  108 LYS   O CA  
25444 C  C   . LYS   O  108 ? 1.7065 0.5120 1.5717 -0.0546 -0.3052 0.1929  108 LYS   O C   
25445 O  O   . LYS   O  108 ? 1.7885 0.2083 1.5826 -0.1209 -0.3271 0.1701  108 LYS   O O   
25446 C  CB  . LYS   O  108 ? 1.7219 0.6622 1.6218 -0.0406 -0.3424 0.2982  108 LYS   O CB  
25447 C  CG  . LYS   O  108 ? 1.7806 0.6885 1.6544 -0.0344 -0.3463 0.3266  108 LYS   O CG  
25448 C  CD  . LYS   O  108 ? 1.8217 0.7622 1.6998 -0.0165 -0.3845 0.2875  108 LYS   O CD  
25449 C  CE  . LYS   O  108 ? 1.8913 0.7327 1.7351 -0.0275 -0.3716 0.2749  108 LYS   O CE  
25450 N  NZ  . LYS   O  108 ? 1.9485 0.6605 1.7273 -0.0262 -0.3737 0.3000  108 LYS   O NZ  
25451 N  N   . LEU   O  109 ? 1.7387 0.5344 1.5347 -0.0436 -0.2961 0.1474  109 LEU   O N   
25452 C  CA  . LEU   O  109 ? 1.7284 0.5833 1.5251 -0.0404 -0.2779 0.1371  109 LEU   O CA  
25453 C  C   . LEU   O  109 ? 1.7409 0.4996 1.5336 -0.0702 -0.2898 0.1301  109 LEU   O C   
25454 O  O   . LEU   O  109 ? 1.7550 0.4156 1.5313 -0.0840 -0.2676 0.1169  109 LEU   O O   
25455 C  CB  . LEU   O  109 ? 1.7573 0.6004 1.5638 0.0225  -0.2570 0.1184  109 LEU   O CB  
25456 C  CG  . LEU   O  109 ? 1.8341 0.7142 1.5458 0.0417  -0.2231 0.1194  109 LEU   O CG  
25457 C  CD1 . LEU   O  109 ? 1.8694 0.7063 1.6127 0.0045  -0.1906 0.1074  109 LEU   O CD1 
25458 C  CD2 . LEU   O  109 ? 1.8586 0.7608 1.5915 0.0779  -0.2013 0.1060  109 LEU   O CD2 
25459 N  N   . LEU   O  110 ? 1.6947 0.4618 1.5332 -0.0637 -0.2974 0.1616  110 LEU   O N   
25460 C  CA  . LEU   O  110 ? 1.6975 0.4828 1.5295 -0.0627 -0.2862 0.2028  110 LEU   O CA  
25461 C  C   . LEU   O  110 ? 1.7079 0.4857 1.5208 -0.0638 -0.2853 0.2143  110 LEU   O C   
25462 O  O   . LEU   O  110 ? 1.6929 0.6371 1.4926 -0.1086 -0.3068 0.2520  110 LEU   O O   
25463 C  CB  . LEU   O  110 ? 1.6607 0.3876 1.5036 -0.0231 -0.3183 0.2144  110 LEU   O CB  
25464 C  CG  . LEU   O  110 ? 1.6561 0.3906 1.5003 -0.0016 -0.3208 0.1981  110 LEU   O CG  
25465 C  CD1 . LEU   O  110 ? 1.6488 0.3609 1.4923 0.0104  -0.3160 0.2198  110 LEU   O CD1 
25466 C  CD2 . LEU   O  110 ? 1.6400 0.4246 1.4999 0.0139  -0.3297 0.1939  110 LEU   O CD2 
25467 N  N   . VAL   O  111 ? 1.7028 0.5848 1.5569 -0.1140 -0.2736 0.1991  111 VAL   O N   
25468 C  CA  . VAL   O  111 ? 1.6665 0.6128 1.5475 -0.1141 -0.2382 0.1592  111 VAL   O CA  
25469 C  C   . VAL   O  111 ? 1.6376 0.5518 1.5028 -0.0981 -0.2620 0.1671  111 VAL   O C   
25470 O  O   . VAL   O  111 ? 1.5947 0.5206 1.5661 -0.0820 -0.1313 0.0705  111 VAL   O O   
25471 C  CB  . VAL   O  111 ? 1.6952 0.6948 1.5767 -0.1132 -0.2999 0.1457  111 VAL   O CB  
25472 C  CG1 . VAL   O  111 ? 1.7020 0.6664 1.5834 -0.1023 -0.2992 0.1629  111 VAL   O CG1 
25473 C  CG2 . VAL   O  111 ? 1.6778 0.7585 1.6180 -0.1369 -0.2916 0.1570  111 VAL   O CG2 
25474 N  N   . SER   O  112 ? 1.5783 0.6009 1.4298 -0.1123 -0.2548 0.1471  112 SER   O N   
25475 C  CA  . SER   O  112 ? 1.5812 0.6233 1.3803 -0.0767 -0.2782 0.1731  112 SER   O CA  
25476 C  C   . SER   O  112 ? 1.5543 0.6411 1.3812 -0.0371 -0.2712 0.1944  112 SER   O C   
25477 O  O   . SER   O  112 ? 1.6100 0.4065 1.3331 -0.0375 -0.2916 0.2308  112 SER   O O   
25478 C  CB  . SER   O  112 ? 1.5624 0.6812 1.3538 -0.0691 -0.2770 0.1870  112 SER   O CB  
25479 O  OG  . SER   O  112 ? 1.5697 0.7505 1.3078 -0.0264 -0.2889 0.2126  112 SER   O OG  
25480 N  N   . GLU   O  113 ? 1.5759 0.7307 1.3799 -0.0243 -0.2916 0.1557  113 GLU   O N   
25481 C  CA  . GLU   O  113 ? 1.5748 0.7843 1.4096 0.0001  -0.3205 0.1722  113 GLU   O CA  
25482 C  C   . GLU   O  113 ? 1.5670 0.7763 1.3951 0.0196  -0.3151 0.1530  113 GLU   O C   
25483 O  O   . GLU   O  113 ? 1.5690 0.9251 1.4368 0.0572  -0.3042 0.1678  113 GLU   O O   
25484 C  CB  . GLU   O  113 ? 1.6039 0.8315 1.4361 0.0013  -0.3047 0.1427  113 GLU   O CB  
25485 C  CG  . GLU   O  113 ? 1.5794 0.8819 1.4774 0.0286  -0.3416 0.1582  113 GLU   O CG  
25486 C  CD  . GLU   O  113 ? 1.5627 0.8905 1.4570 0.0328  -0.3585 0.1556  113 GLU   O CD  
25487 O  OE1 . GLU   O  113 ? 1.4981 1.1148 1.5346 -0.0111 -0.3565 0.0641  113 GLU   O OE1 
25488 O  OE2 . GLU   O  113 ? 1.5126 0.7778 1.4553 0.0019  -0.3884 0.0934  113 GLU   O OE2 
25489 N  N   . VAL   O  114 ? 1.5812 0.6484 1.3363 0.0269  -0.3726 0.1361  114 VAL   O N   
25490 C  CA  . VAL   O  114 ? 1.6080 0.5635 1.3440 -0.0042 -0.3859 0.1027  114 VAL   O CA  
25491 C  C   . VAL   O  114 ? 1.6232 0.5152 1.2937 -0.0403 -0.4457 0.0955  114 VAL   O C   
25492 O  O   . VAL   O  114 ? 1.6035 0.5394 1.2880 -0.0596 -0.4594 0.0658  114 VAL   O O   
25493 C  CB  . VAL   O  114 ? 1.6176 0.5032 1.3734 -0.0044 -0.3847 0.1201  114 VAL   O CB  
25494 C  CG1 . VAL   O  114 ? 1.6369 0.4878 1.3799 0.0066  -0.3781 0.1092  114 VAL   O CG1 
25495 C  CG2 . VAL   O  114 ? 1.6025 0.5059 1.3881 0.0286  -0.3704 0.1655  114 VAL   O CG2 
25496 N  N   . ALA   O  115 ? 1.5964 0.5264 1.3286 -0.0561 -0.4593 0.0908  115 ALA   O N   
25497 C  CA  . ALA   O  115 ? 1.5939 0.5023 1.3469 -0.0859 -0.4600 0.0774  115 ALA   O CA  
25498 C  C   . ALA   O  115 ? 1.5917 0.5312 1.3309 -0.0864 -0.4593 0.0682  115 ALA   O C   
25499 O  O   . ALA   O  115 ? 1.5813 0.3801 1.3189 -0.1747 -0.4693 0.0731  115 ALA   O O   
25500 C  CB  . ALA   O  115 ? 1.5988 0.5187 1.3520 -0.0864 -0.4622 0.0708  115 ALA   O CB  
25501 N  N   . LYS   O  116 ? 1.6097 0.5233 1.3539 -0.0868 -0.4645 0.0269  116 LYS   O N   
25502 C  CA  . LYS   O  116 ? 1.5987 0.5615 1.3724 -0.0853 -0.4705 0.0077  116 LYS   O CA  
25503 C  C   . LYS   O  116 ? 1.6598 0.4546 1.3874 -0.0284 -0.4792 0.0331  116 LYS   O C   
25504 O  O   . LYS   O  116 ? 1.7018 0.4500 1.4012 0.0005  -0.4672 0.0170  116 LYS   O O   
25505 C  CB  . LYS   O  116 ? 1.5826 0.5809 1.3680 -0.0783 -0.4871 0.0376  116 LYS   O CB  
25506 C  CG  . LYS   O  116 ? 1.5710 0.7166 1.3922 -0.1078 -0.4844 0.0286  116 LYS   O CG  
25507 C  CD  . LYS   O  116 ? 1.5435 0.7168 1.4927 -0.1640 -0.4604 0.0058  116 LYS   O CD  
25508 C  CE  . LYS   O  116 ? 1.5570 0.9131 1.5411 -0.1758 -0.3981 -0.0178 116 LYS   O CE  
25509 N  NZ  . LYS   O  116 ? 1.5340 1.0399 1.5876 -0.1892 -0.3763 -0.0792 116 LYS   O NZ  
25510 N  N   . ILE   O  117 ? 1.7000 0.4466 1.3857 0.0174  -0.4413 0.0884  117 ILE   O N   
25511 C  CA  . ILE   O  117 ? 1.7051 0.5471 1.4264 0.0211  -0.4552 0.1191  117 ILE   O CA  
25512 C  C   . ILE   O  117 ? 1.6943 0.5519 1.4188 0.0239  -0.4395 0.1559  117 ILE   O C   
25513 O  O   . ILE   O  117 ? 1.7588 0.5058 1.4597 0.1335  -0.4111 0.3031  117 ILE   O O   
25514 C  CB  . ILE   O  117 ? 1.7152 0.5149 1.4608 -0.0070 -0.4412 0.0874  117 ILE   O CB  
25515 C  CG1 . ILE   O  117 ? 1.7068 0.5150 1.4882 0.0017  -0.4429 0.0424  117 ILE   O CG1 
25516 C  CG2 . ILE   O  117 ? 1.7305 0.5726 1.4248 -0.0546 -0.4554 0.0819  117 ILE   O CG2 
25517 C  CD1 . ILE   O  117 ? 1.7158 0.5150 1.5098 0.0001  -0.4247 0.0357  117 ILE   O CD1 
25518 N  N   . MET   O  118 ? 1.6760 0.5842 1.3723 0.0111  -0.4454 0.1751  118 MET   O N   
25519 C  CA  . MET   O  118 ? 1.6554 0.5876 1.3706 0.0211  -0.4396 0.1478  118 MET   O CA  
25520 C  C   . MET   O  118 ? 1.6874 0.6401 1.3302 -0.0210 -0.4464 0.1379  118 MET   O C   
25521 O  O   . MET   O  118 ? 1.6043 0.8030 1.3510 0.0478  -0.4391 -0.0276 118 MET   O O   
25522 C  CB  . MET   O  118 ? 1.6389 0.6355 1.4263 0.0163  -0.4638 0.1595  118 MET   O CB  
25523 C  CG  . MET   O  118 ? 1.6055 0.6464 1.4487 0.0118  -0.4501 0.1526  118 MET   O CG  
25524 S  SD  . MET   O  118 ? 1.5761 0.6467 1.4802 0.0350  -0.5102 0.1685  118 MET   O SD  
25525 C  CE  . MET   O  118 ? 1.6316 0.6576 1.4982 0.0539  -0.4915 0.1862  118 MET   O CE  
25526 N  N   . GLN   O  119 ? 1.6418 0.5325 1.3327 -0.0444 -0.4007 0.1365  119 GLN   O N   
25527 C  CA  . GLN   O  119 ? 1.6494 0.5509 1.3303 -0.0633 -0.3891 0.1511  119 GLN   O CA  
25528 C  C   . GLN   O  119 ? 1.6598 0.5482 1.3961 -0.0832 -0.3850 0.1432  119 GLN   O C   
25529 O  O   . GLN   O  119 ? 1.6573 0.5597 1.4315 -0.0417 -0.3774 0.2045  119 GLN   O O   
25530 C  CB  . GLN   O  119 ? 1.6201 0.5725 1.3024 -0.0774 -0.3876 0.1466  119 GLN   O CB  
25531 C  CG  . GLN   O  119 ? 1.6306 0.6143 1.2698 -0.0821 -0.3955 0.1784  119 GLN   O CG  
25532 C  CD  . GLN   O  119 ? 1.6334 0.6492 1.2247 -0.0923 -0.4061 0.1986  119 GLN   O CD  
25533 O  OE1 . GLN   O  119 ? 1.5883 0.6591 1.1227 -0.0842 -0.4069 0.2089  119 GLN   O OE1 
25534 N  NE2 . GLN   O  119 ? 1.6304 0.6694 1.2101 -0.1037 -0.3950 0.2055  119 GLN   O NE2 
25535 N  N   . GLU   O  120 ? 1.6977 0.6051 1.4331 -0.0849 -0.3835 0.0815  120 GLU   O N   
25536 C  CA  . GLU   O  120 ? 1.7107 0.6376 1.4550 -0.1013 -0.3886 0.0821  120 GLU   O CA  
25537 C  C   . GLU   O  120 ? 1.7961 0.5273 1.3783 -0.1439 -0.3651 0.0894  120 GLU   O C   
25538 O  O   . GLU   O  120 ? 1.8079 0.3640 1.2575 -0.1189 -0.3755 0.1347  120 GLU   O O   
25539 C  CB  . GLU   O  120 ? 1.7244 0.6511 1.5663 -0.1175 -0.3535 0.0453  120 GLU   O CB  
25540 C  CG  . GLU   O  120 ? 1.7516 0.6613 1.6395 -0.1258 -0.3433 0.0900  120 GLU   O CG  
25541 C  CD  . GLU   O  120 ? 1.8099 0.7073 1.7862 -0.1198 -0.3011 0.0128  120 GLU   O CD  
25542 O  OE1 . GLU   O  120 ? 1.8044 0.8441 1.8555 -0.0833 -0.2847 0.1055  120 GLU   O OE1 
25543 O  OE2 . GLU   O  120 ? 1.9075 0.8259 1.8004 -0.1387 -0.3364 0.0216  120 GLU   O OE2 
25544 N  N   . ALA   O  121 ? 1.8383 0.4941 1.3933 -0.1833 -0.3466 0.0604  121 ALA   O N   
25545 C  CA  . ALA   O  121 ? 1.8543 0.5313 1.4498 -0.1325 -0.3779 0.0418  121 ALA   O CA  
25546 C  C   . ALA   O  121 ? 1.9240 0.5759 1.4421 -0.1208 -0.3500 0.0201  121 ALA   O C   
25547 O  O   . ALA   O  121 ? 2.0494 0.6559 1.3540 -0.2102 -0.4382 0.1863  121 ALA   O O   
25548 C  CB  . ALA   O  121 ? 1.8376 0.5334 1.4767 -0.1400 -0.3668 0.0318  121 ALA   O CB  
25549 N  N   . THR   O  122 ? 1.8904 0.5142 1.4367 -0.1120 -0.3254 -0.0338 122 THR   O N   
25550 C  CA  . THR   O  122 ? 1.8698 0.3666 1.5597 -0.1707 -0.2861 -0.0055 122 THR   O CA  
25551 C  C   . THR   O  122 ? 1.8802 0.3839 1.5334 -0.1134 -0.2634 -0.0772 122 THR   O C   
25552 O  O   . THR   O  122 ? 1.8958 0.2519 1.6007 -0.2016 -0.2259 -0.0409 122 THR   O O   
25553 C  CB  . THR   O  122 ? 1.8726 0.2703 1.5960 -0.1388 -0.2996 -0.0395 122 THR   O CB  
25554 O  OG1 . THR   O  122 ? 1.8868 0.3344 1.5807 -0.0775 -0.2469 -0.0387 122 THR   O OG1 
25555 C  CG2 . THR   O  122 ? 1.8693 0.3472 1.5519 -0.1273 -0.2815 -0.0077 122 THR   O CG2 
25556 N  N   . GLN   O  123 ? 1.7974 0.4526 1.5206 -0.1074 -0.2660 0.0690  123 GLN   O N   
25557 C  CA  . GLN   O  123 ? 1.7520 0.4759 1.4654 -0.0488 -0.2998 0.0745  123 GLN   O CA  
25558 C  C   . GLN   O  123 ? 1.7161 0.4539 1.4792 -0.0130 -0.3265 0.1241  123 GLN   O C   
25559 O  O   . GLN   O  123 ? 1.7045 0.4971 1.4779 0.0362  -0.3421 0.1574  123 GLN   O O   
25560 C  CB  . GLN   O  123 ? 1.7251 0.4622 1.4157 -0.0577 -0.3003 0.0381  123 GLN   O CB  
25561 C  CG  . GLN   O  123 ? 1.7276 0.4802 1.3883 -0.0556 -0.3116 -0.0100 123 GLN   O CG  
25562 C  CD  . GLN   O  123 ? 1.7230 0.5276 1.3425 -0.0579 -0.3068 -0.0364 123 GLN   O CD  
25563 O  OE1 . GLN   O  123 ? 1.7082 0.6164 1.3139 -0.0473 -0.3235 -0.0748 123 GLN   O OE1 
25564 N  NE2 . GLN   O  123 ? 1.7305 0.5760 1.3490 -0.0527 -0.2894 -0.0251 123 GLN   O NE2 
25565 N  N   . SER   O  124 ? 1.6878 0.4147 1.4680 -0.0184 -0.3571 0.1412  124 SER   O N   
25566 C  CA  . SER   O  124 ? 1.6530 0.5423 1.4920 -0.0549 -0.3432 0.1506  124 SER   O CA  
25567 C  C   . SER   O  124 ? 1.6708 0.5495 1.4822 -0.0484 -0.3382 0.1544  124 SER   O C   
25568 O  O   . SER   O  124 ? 1.7056 0.5507 1.4032 -0.0418 -0.3139 0.1398  124 SER   O O   
25569 C  CB  . SER   O  124 ? 1.6118 0.6132 1.5092 -0.0258 -0.3276 0.1342  124 SER   O CB  
25570 O  OG  . SER   O  124 ? 1.5709 0.7404 1.5292 -0.0186 -0.3271 0.1109  124 SER   O OG  
25571 N  N   . GLY   O  125 ? 1.7101 0.5364 1.4970 -0.0806 -0.3472 0.1719  125 GLY   O N   
25572 C  CA  . GLY   O  125 ? 1.7823 0.3698 1.4377 -0.0689 -0.3420 0.2094  125 GLY   O CA  
25573 C  C   . GLY   O  125 ? 1.7922 0.3382 1.4464 -0.0636 -0.3648 0.2304  125 GLY   O C   
25574 O  O   . GLY   O  125 ? 1.7726 0.3224 1.3460 -0.1091 -0.3372 0.2942  125 GLY   O O   
25575 N  N   . GLY   O  126 ? 1.8318 0.3474 1.4517 -0.0057 -0.3570 0.1833  126 GLY   O N   
25576 C  CA  . GLY   O  126 ? 1.8417 0.3013 1.4652 0.0189  -0.3620 0.1877  126 GLY   O CA  
25577 C  C   . GLY   O  126 ? 1.7925 0.1971 1.4790 0.0269  -0.3849 0.1961  126 GLY   O C   
25578 O  O   . GLY   O  126 ? 1.8595 0.1719 1.4919 0.0607  -0.3153 0.1432  126 GLY   O O   
25579 N  N   . VAL   O  127 ? 1.7668 0.2511 1.4514 0.0483  -0.3952 0.2275  127 VAL   O N   
25580 C  CA  . VAL   O  127 ? 1.7584 0.4099 1.4340 0.0430  -0.4066 0.2198  127 VAL   O CA  
25581 C  C   . VAL   O  127 ? 1.7191 0.4501 1.4855 0.0286  -0.4173 0.2261  127 VAL   O C   
25582 O  O   . VAL   O  127 ? 1.6804 0.4035 1.5017 0.0391  -0.3311 0.2160  127 VAL   O O   
25583 C  CB  . VAL   O  127 ? 1.7369 0.4581 1.4451 0.0634  -0.4032 0.1603  127 VAL   O CB  
25584 C  CG1 . VAL   O  127 ? 1.7304 0.6156 1.3830 0.0205  -0.4257 0.1319  127 VAL   O CG1 
25585 C  CG2 . VAL   O  127 ? 1.7687 0.5402 1.4319 0.0351  -0.4018 0.1507  127 VAL   O CG2 
25586 N  N   . ARG   O  128 ? 1.7338 0.4961 1.3987 0.0401  -0.4271 0.2039  128 ARG   O N   
25587 C  CA  . ARG   O  128 ? 1.7614 0.4426 1.3690 0.0704  -0.4360 0.1506  128 ARG   O CA  
25588 C  C   . ARG   O  128 ? 1.7582 0.4896 1.3327 0.0741  -0.4612 0.1641  128 ARG   O C   
25589 O  O   . ARG   O  128 ? 1.7530 0.5306 1.1882 0.1087  -0.4766 0.1795  128 ARG   O O   
25590 C  CB  . ARG   O  128 ? 1.7748 0.4334 1.3619 0.0620  -0.3954 0.1378  128 ARG   O CB  
25591 C  CG  . ARG   O  128 ? 1.7717 0.4080 1.4099 0.0751  -0.3653 0.1115  128 ARG   O CG  
25592 C  CD  . ARG   O  128 ? 1.7722 0.4238 1.3974 0.0739  -0.3453 0.1051  128 ARG   O CD  
25593 N  NE  . ARG   O  128 ? 1.7639 0.4173 1.4014 0.0980  -0.3340 0.1093  128 ARG   O NE  
25594 C  CZ  . ARG   O  128 ? 1.7509 0.3799 1.4031 0.0892  -0.3327 0.1353  128 ARG   O CZ  
25595 N  NH1 . ARG   O  128 ? 1.7120 0.3136 1.4194 0.0839  -0.3185 0.1374  128 ARG   O NH1 
25596 N  NH2 . ARG   O  128 ? 1.7429 0.3560 1.4192 0.1177  -0.3072 0.1271  128 ARG   O NH2 
25597 N  N   . PRO   O  129 ? 1.7924 0.4180 1.3595 0.0812  -0.4541 0.1147  129 PRO   O N   
25598 C  CA  . PRO   O  129 ? 1.7575 0.4527 1.3524 0.0268  -0.4269 0.0799  129 PRO   O CA  
25599 C  C   . PRO   O  129 ? 1.7897 0.3878 1.3517 -0.0147 -0.4186 0.0843  129 PRO   O C   
25600 O  O   . PRO   O  129 ? 1.7804 0.2630 1.3675 -0.0311 -0.4054 0.0622  129 PRO   O O   
25601 C  CB  . PRO   O  129 ? 1.7646 0.4334 1.3539 0.0403  -0.4445 0.0925  129 PRO   O CB  
25602 C  CG  . PRO   O  129 ? 1.7773 0.4118 1.3734 0.0864  -0.4577 0.1039  129 PRO   O CG  
25603 C  CD  . PRO   O  129 ? 1.7897 0.4215 1.3596 0.0931  -0.4617 0.1147  129 PRO   O CD  
25604 N  N   . PHE   O  130 ? 1.7917 0.3613 1.4080 -0.0455 -0.3793 0.0201  130 PHE   O N   
25605 C  CA  . PHE   O  130 ? 1.8244 0.3826 1.3708 -0.1169 -0.3972 0.0660  130 PHE   O CA  
25606 C  C   . PHE   O  130 ? 1.8267 0.3303 1.3099 -0.0743 -0.4225 0.0932  130 PHE   O C   
25607 O  O   . PHE   O  130 ? 1.8576 0.2148 1.2745 -0.0439 -0.4676 0.1879  130 PHE   O O   
25608 C  CB  . PHE   O  130 ? 1.7772 0.4628 1.4166 -0.1074 -0.3718 0.0666  130 PHE   O CB  
25609 C  CG  . PHE   O  130 ? 1.8396 0.4832 1.3492 -0.1660 -0.3504 0.1145  130 PHE   O CG  
25610 C  CD1 . PHE   O  130 ? 1.8218 0.4631 1.3858 -0.2054 -0.3569 0.0734  130 PHE   O CD1 
25611 C  CD2 . PHE   O  130 ? 1.8133 0.4039 1.3813 -0.1736 -0.3826 0.1233  130 PHE   O CD2 
25612 C  CE1 . PHE   O  130 ? 1.7692 0.4568 1.3504 -0.2099 -0.3582 0.1340  130 PHE   O CE1 
25613 C  CE2 . PHE   O  130 ? 1.7595 0.4310 1.3488 -0.1978 -0.3704 0.1359  130 PHE   O CE2 
25614 C  CZ  . PHE   O  130 ? 1.7569 0.4907 1.3321 -0.1838 -0.3739 0.1527  130 PHE   O CZ  
25615 N  N   . GLY   O  131 ? 1.8396 0.4137 1.2564 -0.0947 -0.4159 0.0573  131 GLY   O N   
25616 C  CA  . GLY   O  131 ? 1.8556 0.4451 1.2626 -0.1332 -0.4077 0.0262  131 GLY   O CA  
25617 C  C   . GLY   O  131 ? 1.8558 0.4672 1.2554 -0.1306 -0.4158 -0.0033 131 GLY   O C   
25618 O  O   . GLY   O  131 ? 1.9035 0.4958 1.2009 -0.1642 -0.3953 -0.0531 131 GLY   O O   
25619 N  N   . VAL   O  132 ? 1.8564 0.3847 1.2757 -0.1596 -0.4020 0.0112  132 VAL   O N   
25620 C  CA  . VAL   O  132 ? 1.8450 0.3862 1.3041 -0.1882 -0.3933 0.0582  132 VAL   O CA  
25621 C  C   . VAL   O  132 ? 1.8113 0.3183 1.3190 -0.2019 -0.3878 0.0807  132 VAL   O C   
25622 O  O   . VAL   O  132 ? 1.7642 0.2945 1.3165 -0.2554 -0.4022 0.0502  132 VAL   O O   
25623 C  CB  . VAL   O  132 ? 1.8724 0.3972 1.2729 -0.1860 -0.3812 0.0666  132 VAL   O CB  
25624 C  CG1 . VAL   O  132 ? 1.8836 0.4265 1.2762 -0.1706 -0.3771 0.0814  132 VAL   O CG1 
25625 C  CG2 . VAL   O  132 ? 1.8711 0.4494 1.2832 -0.2099 -0.3766 0.0842  132 VAL   O CG2 
25626 N  N   . SER   O  133 ? 1.8101 0.3524 1.3931 -0.1853 -0.3398 0.1126  133 SER   O N   
25627 C  CA  . SER   O  133 ? 1.8207 0.4441 1.4274 -0.1617 -0.3368 0.1379  133 SER   O CA  
25628 C  C   . SER   O  133 ? 1.8235 0.4763 1.4784 -0.1776 -0.2928 0.1270  133 SER   O C   
25629 O  O   . SER   O  133 ? 1.8990 0.4509 1.4929 -0.2034 -0.2790 0.1386  133 SER   O O   
25630 C  CB  . SER   O  133 ? 1.8370 0.4828 1.4029 -0.1618 -0.3489 0.1110  133 SER   O CB  
25631 O  OG  . SER   O  133 ? 1.8681 0.5680 1.3356 -0.1237 -0.3790 0.1345  133 SER   O OG  
25632 N  N   . LEU   O  134 ? 1.7780 0.5078 1.5335 -0.1387 -0.3230 0.1405  134 LEU   O N   
25633 C  CA  . LEU   O  134 ? 1.7277 0.5519 1.5621 -0.1275 -0.3278 0.1371  134 LEU   O CA  
25634 C  C   . LEU   O  134 ? 1.7217 0.5549 1.5639 -0.1347 -0.3177 0.1393  134 LEU   O C   
25635 O  O   . LEU   O  134 ? 1.6841 0.5222 1.5789 -0.1557 -0.3202 0.0990  134 LEU   O O   
25636 C  CB  . LEU   O  134 ? 1.6983 0.5548 1.5566 -0.1264 -0.3478 0.1414  134 LEU   O CB  
25637 C  CG  . LEU   O  134 ? 1.6993 0.5662 1.5526 -0.1251 -0.3446 0.1449  134 LEU   O CG  
25638 C  CD1 . LEU   O  134 ? 1.6824 0.5870 1.5496 -0.1272 -0.3497 0.1769  134 LEU   O CD1 
25639 C  CD2 . LEU   O  134 ? 1.7453 0.5734 1.5469 -0.1080 -0.3207 0.1474  134 LEU   O CD2 
25640 N  N   . LEU   O  135 ? 1.7265 0.5697 1.5743 -0.1343 -0.3029 0.1781  135 LEU   O N   
25641 C  CA  . LEU   O  135 ? 1.7443 0.6237 1.5709 -0.1274 -0.3236 0.2143  135 LEU   O CA  
25642 C  C   . LEU   O  135 ? 1.7564 0.6229 1.5815 -0.1208 -0.3099 0.2242  135 LEU   O C   
25643 O  O   . LEU   O  135 ? 1.7716 0.6453 1.5537 -0.0819 -0.3402 0.2958  135 LEU   O O   
25644 C  CB  . LEU   O  135 ? 1.7814 0.6370 1.5573 -0.1331 -0.3110 0.2252  135 LEU   O CB  
25645 C  CG  . LEU   O  135 ? 1.8288 0.6670 1.5401 -0.1510 -0.3228 0.1805  135 LEU   O CG  
25646 C  CD1 . LEU   O  135 ? 1.8288 0.7278 1.5731 -0.1853 -0.3050 0.1501  135 LEU   O CD1 
25647 C  CD2 . LEU   O  135 ? 1.8348 0.6740 1.5293 -0.1685 -0.3239 0.2201  135 LEU   O CD2 
25648 N  N   . ILE   O  136 ? 1.7676 0.6277 1.6060 -0.1249 -0.2850 0.2439  136 ILE   O N   
25649 C  CA  . ILE   O  136 ? 1.7257 0.5919 1.6088 -0.1351 -0.2535 0.3162  136 ILE   O CA  
25650 C  C   . ILE   O  136 ? 1.7393 0.5428 1.5783 -0.1324 -0.2683 0.3516  136 ILE   O C   
25651 O  O   . ILE   O  136 ? 1.7397 0.4843 1.5524 -0.1360 -0.2460 0.4126  136 ILE   O O   
25652 C  CB  . ILE   O  136 ? 1.7228 0.6083 1.6412 -0.1517 -0.2310 0.2907  136 ILE   O CB  
25653 C  CG1 . ILE   O  136 ? 1.7316 0.5979 1.6602 -0.1088 -0.2024 0.2951  136 ILE   O CG1 
25654 C  CG2 . ILE   O  136 ? 1.7173 0.6472 1.6567 -0.1328 -0.2216 0.2298  136 ILE   O CG2 
25655 C  CD1 . ILE   O  136 ? 1.7427 0.6647 1.6425 -0.0581 -0.1660 0.2796  136 ILE   O CD1 
25656 N  N   . ALA   O  137 ? 1.6899 0.5253 1.6222 -0.1276 -0.2724 0.3418  137 ALA   O N   
25657 C  CA  . ALA   O  137 ? 1.6844 0.5655 1.6687 -0.1379 -0.3130 0.3304  137 ALA   O CA  
25658 C  C   . ALA   O  137 ? 1.6552 0.5735 1.6796 -0.0977 -0.3513 0.3113  137 ALA   O C   
25659 O  O   . ALA   O  137 ? 1.5880 0.5678 1.7344 -0.0976 -0.3762 0.3386  137 ALA   O O   
25660 C  CB  . ALA   O  137 ? 1.7089 0.5650 1.7127 -0.1520 -0.2930 0.3370  137 ALA   O CB  
25661 N  N   . GLY   O  138 ? 1.6750 0.6224 1.6648 -0.0860 -0.3878 0.2801  138 GLY   O N   
25662 C  CA  . GLY   O  138 ? 1.6941 0.6303 1.6866 -0.0968 -0.3988 0.2284  138 GLY   O CA  
25663 C  C   . GLY   O  138 ? 1.7019 0.6979 1.6680 -0.0992 -0.4476 0.1681  138 GLY   O C   
25664 O  O   . GLY   O  138 ? 1.7538 0.6099 1.6076 -0.0486 -0.4547 0.1691  138 GLY   O O   
25665 N  N   . HIS   O  139 ? 1.6929 0.7201 1.7062 -0.0498 -0.4534 0.1752  139 HIS   O N   
25666 C  CA  . HIS   O  139 ? 1.6845 0.8135 1.6676 -0.0883 -0.4950 0.2047  139 HIS   O CA  
25667 C  C   . HIS   O  139 ? 1.6865 0.8291 1.6365 -0.1112 -0.4821 0.1954  139 HIS   O C   
25668 O  O   . HIS   O  139 ? 1.6956 0.8574 1.6631 -0.1879 -0.4734 0.2672  139 HIS   O O   
25669 C  CB  . HIS   O  139 ? 1.6750 0.8024 1.6882 -0.0234 -0.5054 0.2387  139 HIS   O CB  
25670 C  CG  . HIS   O  139 ? 1.7479 0.7136 1.6933 -0.0008 -0.4860 0.2524  139 HIS   O CG  
25671 N  ND1 . HIS   O  139 ? 1.7477 0.7004 1.6979 0.0227  -0.4875 0.3138  139 HIS   O ND1 
25672 C  CD2 . HIS   O  139 ? 1.7549 0.6795 1.6629 0.0379  -0.4986 0.2614  139 HIS   O CD2 
25673 C  CE1 . HIS   O  139 ? 1.7424 0.7377 1.7106 0.0129  -0.4986 0.3174  139 HIS   O CE1 
25674 N  NE2 . HIS   O  139 ? 1.7614 0.6953 1.7044 0.0465  -0.4909 0.2873  139 HIS   O NE2 
25675 N  N   . ASP   O  140 ? 1.6271 0.8464 1.6034 -0.1025 -0.5115 0.1131  140 ASP   O N   
25676 C  CA  . ASP   O  140 ? 1.6710 0.8741 1.6640 -0.1229 -0.4774 0.1142  140 ASP   O CA  
25677 C  C   . ASP   O  140 ? 1.6228 0.9752 1.7048 -0.1687 -0.5208 0.0372  140 ASP   O C   
25678 O  O   . ASP   O  140 ? 1.6972 0.9695 1.7160 -0.1627 -0.4804 -0.0605 140 ASP   O O   
25679 C  CB  . ASP   O  140 ? 1.6664 0.9737 1.6312 -0.0922 -0.4899 0.0580  140 ASP   O CB  
25680 C  CG  . ASP   O  140 ? 1.6884 1.0370 1.6233 -0.1214 -0.4960 0.0376  140 ASP   O CG  
25681 O  OD1 . ASP   O  140 ? 1.7153 1.2178 1.5385 -0.1533 -0.4780 0.0048  140 ASP   O OD1 
25682 O  OD2 . ASP   O  140 ? 1.6435 1.0895 1.6590 -0.0895 -0.5397 0.0641  140 ASP   O OD2 
25683 N  N   . GLU   O  141 ? 1.6498 1.0022 1.7701 -0.1084 -0.4892 0.1975  141 GLU   O N   
25684 C  CA  . GLU   O  141 ? 1.6855 0.9205 1.8043 -0.0903 -0.4379 0.2939  141 GLU   O CA  
25685 C  C   . GLU   O  141 ? 1.7557 0.8105 1.7842 -0.0982 -0.4041 0.3217  141 GLU   O C   
25686 O  O   . GLU   O  141 ? 1.7439 0.8768 1.8013 -0.1460 -0.3497 0.3457  141 GLU   O O   
25687 C  CB  . GLU   O  141 ? 1.7063 0.9313 1.8487 -0.0851 -0.3990 0.2340  141 GLU   O CB  
25688 C  CG  . GLU   O  141 ? 1.7231 1.0485 1.9508 -0.0241 -0.3591 0.2108  141 GLU   O CG  
25689 C  CD  . GLU   O  141 ? 1.8312 1.0416 2.0437 0.0415  -0.3472 0.2531  141 GLU   O CD  
25690 O  OE1 . GLU   O  141 ? 1.7842 1.4171 2.1255 0.1459  -0.4175 0.2362  141 GLU   O OE1 
25691 O  OE2 . GLU   O  141 ? 1.8455 1.1772 2.0297 0.0884  -0.4270 0.2911  141 GLU   O OE2 
25692 N  N   . PHE   O  142 ? 1.7820 0.6837 1.8018 -0.0599 -0.3961 0.3170  142 PHE   O N   
25693 C  CA  . PHE   O  142 ? 1.8441 0.8838 1.8371 -0.0656 -0.4189 0.2145  142 PHE   O CA  
25694 C  C   . PHE   O  142 ? 1.7859 0.9204 1.7935 -0.0986 -0.4127 0.1618  142 PHE   O C   
25695 O  O   . PHE   O  142 ? 1.8373 1.0293 1.7982 -0.1078 -0.3918 0.1071  142 PHE   O O   
25696 C  CB  . PHE   O  142 ? 1.8455 0.9215 1.8872 -0.0826 -0.3907 0.1839  142 PHE   O CB  
25697 C  CG  . PHE   O  142 ? 1.8889 0.9449 1.9420 0.0000  -0.4533 0.2068  142 PHE   O CG  
25698 C  CD1 . PHE   O  142 ? 1.8781 0.8597 1.9891 0.0326  -0.4427 0.1867  142 PHE   O CD1 
25699 C  CD2 . PHE   O  142 ? 1.9006 0.9247 1.9747 0.0457  -0.4743 0.1885  142 PHE   O CD2 
25700 C  CE1 . PHE   O  142 ? 1.8696 0.8610 2.0205 0.0649  -0.4255 0.1943  142 PHE   O CE1 
25701 C  CE2 . PHE   O  142 ? 1.8737 0.9321 1.9999 0.0707  -0.4721 0.1864  142 PHE   O CE2 
25702 C  CZ  . PHE   O  142 ? 1.8714 0.9301 2.0063 0.0665  -0.4513 0.1775  142 PHE   O CZ  
25703 N  N   . ASN   O  143 ? 1.7197 0.9189 1.7343 -0.1187 -0.4082 0.1295  143 ASN   O N   
25704 C  CA  . ASN   O  143 ? 1.7366 0.9350 1.7098 -0.1416 -0.4084 0.0605  143 ASN   O CA  
25705 C  C   . ASN   O  143 ? 1.7465 0.9693 1.7829 -0.1516 -0.4158 0.1129  143 ASN   O C   
25706 O  O   . ASN   O  143 ? 1.7197 0.9973 1.8221 -0.1214 -0.4288 0.0461  143 ASN   O O   
25707 C  CB  . ASN   O  143 ? 1.7265 0.8645 1.6648 -0.1657 -0.3852 -0.0088 143 ASN   O CB  
25708 C  CG  . ASN   O  143 ? 1.7561 0.8790 1.6212 -0.1663 -0.3675 -0.0588 143 ASN   O CG  
25709 O  OD1 . ASN   O  143 ? 1.6895 0.9495 1.6259 -0.1711 -0.4230 -0.0800 143 ASN   O OD1 
25710 N  ND2 . ASN   O  143 ? 1.7769 0.9489 1.6612 -0.2094 -0.3372 -0.1036 143 ASN   O ND2 
25711 N  N   . GLY   O  144 ? 1.7987 0.9412 1.7753 -0.1425 -0.3879 0.1642  144 GLY   O N   
25712 C  CA  . GLY   O  144 ? 1.8239 0.9392 1.7896 -0.1248 -0.4210 0.2359  144 GLY   O CA  
25713 C  C   . GLY   O  144 ? 1.8636 0.8291 1.7519 -0.1633 -0.3776 0.2662  144 GLY   O C   
25714 O  O   . GLY   O  144 ? 1.8332 0.9310 1.7240 -0.1086 -0.3789 0.3419  144 GLY   O O   
25715 N  N   . PHE   O  145 ? 1.8676 0.7032 1.7214 -0.0937 -0.4218 0.2299  145 PHE   O N   
25716 C  CA  . PHE   O  145 ? 1.8356 0.5518 1.7130 -0.1632 -0.3824 0.2139  145 PHE   O CA  
25717 C  C   . PHE   O  145 ? 1.8156 0.4806 1.6493 -0.1857 -0.4146 0.2382  145 PHE   O C   
25718 O  O   . PHE   O  145 ? 1.8012 0.4318 1.6379 -0.1790 -0.4155 0.2613  145 PHE   O O   
25719 C  CB  . PHE   O  145 ? 1.8377 0.5577 1.7251 -0.1723 -0.3923 0.2208  145 PHE   O CB  
25720 C  CG  . PHE   O  145 ? 1.8613 0.5433 1.7717 -0.1627 -0.3756 0.2141  145 PHE   O CG  
25721 C  CD1 . PHE   O  145 ? 1.8807 0.4984 1.7831 -0.1864 -0.3836 0.2281  145 PHE   O CD1 
25722 C  CD2 . PHE   O  145 ? 1.8202 0.6386 1.8339 -0.2054 -0.3962 0.1946  145 PHE   O CD2 
25723 C  CE1 . PHE   O  145 ? 1.8676 0.5563 1.8212 -0.1968 -0.3646 0.2036  145 PHE   O CE1 
25724 C  CE2 . PHE   O  145 ? 1.8031 0.7025 1.8550 -0.2064 -0.3746 0.1870  145 PHE   O CE2 
25725 C  CZ  . PHE   O  145 ? 1.8454 0.6586 1.8558 -0.2114 -0.3807 0.1901  145 PHE   O CZ  
25726 N  N   . SER   O  146 ? 1.7980 0.4834 1.6689 -0.1768 -0.3817 0.2157  146 SER   O N   
25727 C  CA  . SER   O  146 ? 1.8412 0.5818 1.6670 -0.1812 -0.3528 0.1563  146 SER   O CA  
25728 C  C   . SER   O  146 ? 1.8510 0.6313 1.6700 -0.1320 -0.3559 0.1282  146 SER   O C   
25729 O  O   . SER   O  146 ? 1.8316 0.6159 1.7002 -0.1399 -0.3383 0.0925  146 SER   O O   
25730 C  CB  . SER   O  146 ? 1.8525 0.5822 1.6770 -0.1522 -0.3481 0.1935  146 SER   O CB  
25731 O  OG  . SER   O  146 ? 1.8111 0.7044 1.6858 -0.2036 -0.3508 0.1835  146 SER   O OG  
25732 N  N   . LEU   O  147 ? 1.8748 0.6372 1.6178 -0.1241 -0.3688 0.1315  147 LEU   O N   
25733 C  CA  . LEU   O  147 ? 1.8424 0.6254 1.5358 -0.1442 -0.3731 0.0993  147 LEU   O CA  
25734 C  C   . LEU   O  147 ? 1.7732 0.5711 1.5141 -0.1565 -0.4095 0.1055  147 LEU   O C   
25735 O  O   . LEU   O  147 ? 1.8219 0.4719 1.5071 -0.1604 -0.3395 0.0653  147 LEU   O O   
25736 C  CB  . LEU   O  147 ? 1.8607 0.6530 1.4956 -0.1815 -0.3973 0.0828  147 LEU   O CB  
25737 C  CG  . LEU   O  147 ? 1.8802 0.6241 1.4533 -0.1925 -0.3983 0.0630  147 LEU   O CG  
25738 C  CD1 . LEU   O  147 ? 1.8669 0.6769 1.4511 -0.1877 -0.3942 0.0679  147 LEU   O CD1 
25739 C  CD2 . LEU   O  147 ? 1.9164 0.6259 1.4514 -0.2115 -0.3957 0.0056  147 LEU   O CD2 
25740 N  N   . TYR   O  148 ? 1.7527 0.5423 1.4823 -0.1570 -0.3965 0.1146  148 TYR   O N   
25741 C  CA  . TYR   O  148 ? 1.7482 0.5863 1.4500 -0.1476 -0.4193 0.0856  148 TYR   O CA  
25742 C  C   . TYR   O  148 ? 1.7578 0.5155 1.4606 -0.1685 -0.3861 0.0916  148 TYR   O C   
25743 O  O   . TYR   O  148 ? 1.8160 0.5578 1.4509 -0.2050 -0.3283 0.1389  148 TYR   O O   
25744 C  CB  . TYR   O  148 ? 1.7001 0.6026 1.4313 -0.1271 -0.4326 0.1054  148 TYR   O CB  
25745 C  CG  . TYR   O  148 ? 1.7106 0.7027 1.4174 -0.0836 -0.4677 0.0861  148 TYR   O CG  
25746 C  CD1 . TYR   O  148 ? 1.6992 0.7251 1.4370 -0.0696 -0.4720 0.1137  148 TYR   O CD1 
25747 C  CD2 . TYR   O  148 ? 1.7165 0.6834 1.4178 -0.0552 -0.4667 0.0820  148 TYR   O CD2 
25748 C  CE1 . TYR   O  148 ? 1.7009 0.7501 1.4443 -0.0758 -0.4643 0.1413  148 TYR   O CE1 
25749 C  CE2 . TYR   O  148 ? 1.7322 0.6891 1.4157 -0.0748 -0.4558 0.1105  148 TYR   O CE2 
25750 C  CZ  . TYR   O  148 ? 1.6712 0.7730 1.4309 -0.0399 -0.4904 0.1482  148 TYR   O CZ  
25751 O  OH  . TYR   O  148 ? 1.6066 1.0890 1.4084 0.0335  -0.5816 0.1358  148 TYR   O OH  
25752 N  N   . GLN   O  149 ? 1.7680 0.4974 1.4556 -0.1805 -0.4015 0.0786  149 GLN   O N   
25753 C  CA  . GLN   O  149 ? 1.7762 0.5002 1.4956 -0.1657 -0.3854 0.0911  149 GLN   O CA  
25754 C  C   . GLN   O  149 ? 1.7513 0.3717 1.4997 -0.2003 -0.4393 0.1070  149 GLN   O C   
25755 O  O   . GLN   O  149 ? 1.7384 0.3278 1.5065 -0.2346 -0.4221 0.1301  149 GLN   O O   
25756 C  CB  . GLN   O  149 ? 1.8172 0.5250 1.5218 -0.1557 -0.3853 0.0353  149 GLN   O CB  
25757 C  CG  . GLN   O  149 ? 1.8462 0.5109 1.5365 -0.1254 -0.3772 -0.0081 149 GLN   O CG  
25758 C  CD  . GLN   O  149 ? 1.8854 0.5199 1.5316 -0.1085 -0.4001 -0.0409 149 GLN   O CD  
25759 O  OE1 . GLN   O  149 ? 1.8751 0.5481 1.5510 -0.0602 -0.4293 -0.1287 149 GLN   O OE1 
25760 N  NE2 . GLN   O  149 ? 1.8812 0.5490 1.4980 -0.0980 -0.4138 -0.0332 149 GLN   O NE2 
25761 N  N   . VAL   O  150 ? 1.7646 0.3615 1.5212 -0.2003 -0.4644 0.1269  150 VAL   O N   
25762 C  CA  . VAL   O  150 ? 1.7513 0.4101 1.5326 -0.1914 -0.4862 0.1357  150 VAL   O CA  
25763 C  C   . VAL   O  150 ? 1.7731 0.3936 1.5296 -0.1976 -0.5069 0.1303  150 VAL   O C   
25764 O  O   . VAL   O  150 ? 1.7856 0.3974 1.5447 -0.1617 -0.5068 0.1569  150 VAL   O O   
25765 C  CB  . VAL   O  150 ? 1.7449 0.4120 1.5750 -0.1947 -0.4875 0.1307  150 VAL   O CB  
25766 C  CG1 . VAL   O  150 ? 1.7431 0.4406 1.5822 -0.1693 -0.4737 0.1427  150 VAL   O CG1 
25767 C  CG2 . VAL   O  150 ? 1.7144 0.4582 1.5830 -0.1868 -0.5100 0.1274  150 VAL   O CG2 
25768 N  N   . ASP   O  151 ? 1.7629 0.3778 1.5124 -0.2072 -0.5341 0.1182  151 ASP   O N   
25769 C  CA  . ASP   O  151 ? 1.7584 0.4225 1.5440 -0.1871 -0.5466 0.1316  151 ASP   O CA  
25770 C  C   . ASP   O  151 ? 1.7585 0.3538 1.5125 -0.1849 -0.5008 0.1607  151 ASP   O C   
25771 O  O   . ASP   O  151 ? 1.7461 0.3075 1.5244 -0.1836 -0.4978 0.1147  151 ASP   O O   
25772 C  CB  . ASP   O  151 ? 1.8327 0.5051 1.5520 -0.2334 -0.5890 0.1129  151 ASP   O CB  
25773 C  CG  . ASP   O  151 ? 1.9467 0.4149 1.5680 -0.2970 -0.6404 0.0724  151 ASP   O CG  
25774 O  OD1 . ASP   O  151 ? 2.0167 0.5071 1.6189 -0.2471 -0.5755 0.2023  151 ASP   O OD1 
25775 O  OD2 . ASP   O  151 ? 2.0471 0.3434 1.6665 -0.3178 -0.6622 0.0401  151 ASP   O OD2 
25776 N  N   . PRO   O  152 ? 1.7309 0.4530 1.4746 -0.1637 -0.4935 0.1740  152 PRO   O N   
25777 C  CA  . PRO   O  152 ? 1.7166 0.3908 1.4430 -0.1425 -0.4865 0.1851  152 PRO   O CA  
25778 C  C   . PRO   O  152 ? 1.7213 0.3700 1.4551 -0.1295 -0.4673 0.1924  152 PRO   O C   
25779 O  O   . PRO   O  152 ? 1.6665 0.2611 1.4372 -0.0688 -0.3979 0.3387  152 PRO   O O   
25780 C  CB  . PRO   O  152 ? 1.7316 0.3952 1.4595 -0.1283 -0.4907 0.1855  152 PRO   O CB  
25781 C  CG  . PRO   O  152 ? 1.7494 0.3806 1.4719 -0.1140 -0.4817 0.2085  152 PRO   O CG  
25782 C  CD  . PRO   O  152 ? 1.7454 0.4281 1.4836 -0.1186 -0.4980 0.1859  152 PRO   O CD  
25783 N  N   . SER   O  153 ? 1.7337 0.4031 1.4670 -0.1683 -0.4393 0.1544  153 SER   O N   
25784 C  CA  . SER   O  153 ? 1.7391 0.4799 1.4575 -0.1584 -0.4323 0.1396  153 SER   O CA  
25785 C  C   . SER   O  153 ? 1.7432 0.4784 1.5044 -0.1378 -0.4105 0.1078  153 SER   O C   
25786 O  O   . SER   O  153 ? 1.7688 0.3879 1.5269 -0.1415 -0.4065 0.0974  153 SER   O O   
25787 C  CB  . SER   O  153 ? 1.7512 0.6056 1.4332 -0.1555 -0.4656 0.1377  153 SER   O CB  
25788 O  OG  . SER   O  153 ? 1.7509 0.6964 1.4284 -0.1247 -0.5221 0.1277  153 SER   O OG  
25789 N  N   . GLY   O  154 ? 1.7713 0.4669 1.5320 -0.1089 -0.4063 0.1062  154 GLY   O N   
25790 C  CA  . GLY   O  154 ? 1.8003 0.4535 1.5498 -0.1135 -0.3707 0.1150  154 GLY   O CA  
25791 C  C   . GLY   O  154 ? 1.7998 0.5349 1.5622 -0.1202 -0.3673 0.0957  154 GLY   O C   
25792 O  O   . GLY   O  154 ? 1.7927 0.5509 1.6106 -0.0774 -0.3893 0.0355  154 GLY   O O   
25793 N  N   . SER   O  155 ? 1.8279 0.4808 1.5479 -0.0853 -0.3531 0.1253  155 SER   O N   
25794 C  CA  . SER   O  155 ? 1.8400 0.5442 1.5150 -0.0428 -0.3579 0.1650  155 SER   O CA  
25795 C  C   . SER   O  155 ? 1.8422 0.5890 1.5477 -0.0256 -0.3489 0.1663  155 SER   O C   
25796 O  O   . SER   O  155 ? 1.8618 0.5863 1.5675 -0.0083 -0.3262 0.1817  155 SER   O O   
25797 C  CB  . SER   O  155 ? 1.8974 0.5490 1.4963 -0.0566 -0.3430 0.1686  155 SER   O CB  
25798 O  OG  . SER   O  155 ? 1.9586 0.6226 1.4493 -0.0681 -0.3030 0.2568  155 SER   O OG  
25799 N  N   . TYR   O  156 ? 1.8548 0.6787 1.5102 -0.0233 -0.3957 0.1834  156 TYR   O N   
25800 C  CA  . TYR   O  156 ? 1.8254 0.6719 1.4870 -0.0607 -0.4230 0.1628  156 TYR   O CA  
25801 C  C   . TYR   O  156 ? 1.8627 0.6668 1.4392 -0.0761 -0.4236 0.1332  156 TYR   O C   
25802 O  O   . TYR   O  156 ? 1.8924 0.8238 1.3667 -0.0463 -0.4851 -0.0028 156 TYR   O O   
25803 C  CB  . TYR   O  156 ? 1.7838 0.6587 1.4815 -0.1088 -0.4362 0.1762  156 TYR   O CB  
25804 C  CG  . TYR   O  156 ? 1.7107 0.6292 1.5174 -0.1222 -0.4611 0.1808  156 TYR   O CG  
25805 C  CD1 . TYR   O  156 ? 1.7219 0.6221 1.5051 -0.1228 -0.4570 0.2152  156 TYR   O CD1 
25806 C  CD2 . TYR   O  156 ? 1.7047 0.5673 1.5403 -0.1385 -0.4565 0.2007  156 TYR   O CD2 
25807 C  CE1 . TYR   O  156 ? 1.7137 0.6480 1.5236 -0.0778 -0.4464 0.2427  156 TYR   O CE1 
25808 C  CE2 . TYR   O  156 ? 1.6837 0.5704 1.5435 -0.0943 -0.4639 0.2081  156 TYR   O CE2 
25809 C  CZ  . TYR   O  156 ? 1.6892 0.6584 1.5439 -0.0683 -0.4295 0.2202  156 TYR   O CZ  
25810 O  OH  . TYR   O  156 ? 1.7176 0.7818 1.5051 0.0187  -0.4121 0.2888  156 TYR   O OH  
25811 N  N   . PHE   O  157 ? 1.8751 0.5487 1.4613 -0.1103 -0.4539 0.1283  157 PHE   O N   
25812 C  CA  . PHE   O  157 ? 1.8914 0.6989 1.4680 -0.1081 -0.4811 0.1179  157 PHE   O CA  
25813 C  C   . PHE   O  157 ? 1.8573 0.6123 1.4844 -0.1316 -0.4847 0.1468  157 PHE   O C   
25814 O  O   . PHE   O  157 ? 1.8565 0.5267 1.5025 -0.1281 -0.4498 0.2444  157 PHE   O O   
25815 C  CB  . PHE   O  157 ? 1.9793 0.7305 1.5403 -0.0918 -0.4786 0.0174  157 PHE   O CB  
25816 C  CG  . PHE   O  157 ? 1.9792 0.9283 1.6099 -0.0445 -0.4721 -0.0593 157 PHE   O CG  
25817 C  CD1 . PHE   O  157 ? 2.0434 0.9131 1.5900 -0.0349 -0.4751 -0.0787 157 PHE   O CD1 
25818 C  CD2 . PHE   O  157 ? 2.0534 1.0234 1.5883 -0.0646 -0.4620 -0.0641 157 PHE   O CD2 
25819 C  CE1 . PHE   O  157 ? 2.0777 0.8622 1.5822 -0.0232 -0.5037 -0.0561 157 PHE   O CE1 
25820 C  CE2 . PHE   O  157 ? 2.0736 1.0319 1.6036 -0.0494 -0.4488 -0.0758 157 PHE   O CE2 
25821 C  CZ  . PHE   O  157 ? 2.0859 0.9469 1.6335 -0.0436 -0.4645 -0.0695 157 PHE   O CZ  
25822 N  N   . PRO   O  158 ? 1.8452 0.7186 1.4543 -0.1553 -0.5172 0.1332  158 PRO   O N   
25823 C  CA  . PRO   O  158 ? 1.8456 0.8137 1.4600 -0.1688 -0.5153 0.1099  158 PRO   O CA  
25824 C  C   . PRO   O  158 ? 1.8327 0.8453 1.4237 -0.1991 -0.5421 0.0451  158 PRO   O C   
25825 O  O   . PRO   O  158 ? 1.8660 0.8499 1.4843 -0.2142 -0.5914 0.0114  158 PRO   O O   
25826 C  CB  . PRO   O  158 ? 1.8588 0.8589 1.4847 -0.1567 -0.5142 0.1394  158 PRO   O CB  
25827 C  CG  . PRO   O  158 ? 1.8664 0.8510 1.5025 -0.1461 -0.4976 0.1309  158 PRO   O CG  
25828 C  CD  . PRO   O  158 ? 1.8833 0.7666 1.4508 -0.1546 -0.4902 0.1358  158 PRO   O CD  
25829 N  N   . TRP   O  159 ? 1.7947 0.8799 1.4558 -0.1923 -0.5191 0.0481  159 TRP   O N   
25830 C  CA  . TRP   O  159 ? 1.7914 0.8483 1.5220 -0.2123 -0.4732 -0.0392 159 TRP   O CA  
25831 C  C   . TRP   O  159 ? 1.7552 0.8136 1.5065 -0.2164 -0.4964 0.0234  159 TRP   O C   
25832 O  O   . TRP   O  159 ? 1.7466 0.8543 1.5268 -0.1932 -0.4654 -0.0075 159 TRP   O O   
25833 C  CB  . TRP   O  159 ? 1.8002 0.8457 1.5201 -0.2192 -0.4579 -0.0479 159 TRP   O CB  
25834 C  CG  . TRP   O  159 ? 1.8598 0.8764 1.6121 -0.2402 -0.3863 -0.1507 159 TRP   O CG  
25835 C  CD1 . TRP   O  159 ? 1.8514 0.8592 1.6351 -0.2253 -0.3424 -0.1541 159 TRP   O CD1 
25836 C  CD2 . TRP   O  159 ? 1.8586 0.9038 1.6666 -0.2445 -0.3794 -0.1886 159 TRP   O CD2 
25837 N  NE1 . TRP   O  159 ? 1.8760 0.8189 1.6313 -0.2220 -0.3577 -0.1443 159 TRP   O NE1 
25838 C  CE2 . TRP   O  159 ? 1.8691 0.8714 1.6415 -0.2263 -0.3731 -0.1807 159 TRP   O CE2 
25839 C  CE3 . TRP   O  159 ? 1.8591 0.9474 1.7569 -0.2588 -0.3653 -0.2263 159 TRP   O CE3 
25840 C  CZ2 . TRP   O  159 ? 1.8629 0.9160 1.6276 -0.2159 -0.3653 -0.2126 159 TRP   O CZ2 
25841 C  CZ3 . TRP   O  159 ? 1.8829 0.9888 1.7575 -0.2461 -0.3505 -0.2611 159 TRP   O CZ3 
25842 C  CH2 . TRP   O  159 ? 1.8777 0.9708 1.6925 -0.2423 -0.3655 -0.2387 159 TRP   O CH2 
25843 N  N   . LYS   O  160 ? 1.7626 0.7349 1.5071 -0.1896 -0.4886 0.0030  160 LYS   O N   
25844 C  CA  . LYS   O  160 ? 1.7718 0.7509 1.5733 -0.1830 -0.4638 0.0073  160 LYS   O CA  
25845 C  C   . LYS   O  160 ? 1.7708 0.6984 1.6076 -0.1983 -0.4429 0.0391  160 LYS   O C   
25846 O  O   . LYS   O  160 ? 1.7855 0.7249 1.6570 -0.1212 -0.3915 0.0814  160 LYS   O O   
25847 C  CB  . LYS   O  160 ? 1.7858 0.7639 1.6200 -0.2072 -0.4591 -0.0125 160 LYS   O CB  
25848 C  CG  . LYS   O  160 ? 1.7626 0.8646 1.6151 -0.2065 -0.4865 -0.0196 160 LYS   O CG  
25849 C  CD  . LYS   O  160 ? 1.7562 0.9083 1.6643 -0.2615 -0.5029 -0.0283 160 LYS   O CD  
25850 C  CE  . LYS   O  160 ? 1.7438 1.0001 1.6786 -0.2613 -0.5165 -0.0027 160 LYS   O CE  
25851 N  NZ  . LYS   O  160 ? 1.7724 1.0523 1.6762 -0.2888 -0.5294 -0.0074 160 LYS   O NZ  
25852 N  N   . ALA   O  161 ? 1.7450 0.6404 1.6022 -0.2572 -0.4430 0.0335  161 ALA   O N   
25853 C  CA  . ALA   O  161 ? 1.7328 0.6300 1.6101 -0.2916 -0.4222 0.0617  161 ALA   O CA  
25854 C  C   . ALA   O  161 ? 1.7414 0.5760 1.5585 -0.2950 -0.4409 0.0962  161 ALA   O C   
25855 O  O   . ALA   O  161 ? 1.7026 0.6005 1.5348 -0.2848 -0.4603 0.1126  161 ALA   O O   
25856 C  CB  . ALA   O  161 ? 1.7565 0.6670 1.6230 -0.3044 -0.4031 0.0711  161 ALA   O CB  
25857 N  N   . THR   O  162 ? 1.7732 0.5360 1.5175 -0.3081 -0.4325 0.1104  162 THR   O N   
25858 C  CA  . THR   O  162 ? 1.8016 0.5306 1.5270 -0.3025 -0.4096 0.1028  162 THR   O CA  
25859 C  C   . THR   O  162 ? 1.8300 0.5276 1.5419 -0.3118 -0.4330 0.0901  162 THR   O C   
25860 O  O   . THR   O  162 ? 1.8565 0.5085 1.6077 -0.3188 -0.3845 0.0732  162 THR   O O   
25861 C  CB  . THR   O  162 ? 1.8003 0.5008 1.4625 -0.2815 -0.4291 0.1121  162 THR   O CB  
25862 O  OG1 . THR   O  162 ? 1.8275 0.4759 1.4294 -0.2637 -0.4295 0.1810  162 THR   O OG1 
25863 C  CG2 . THR   O  162 ? 1.7802 0.5104 1.4196 -0.2834 -0.4326 0.1222  162 THR   O CG2 
25864 N  N   . ALA   O  163 ? 1.8377 0.5474 1.6120 -0.2989 -0.4259 0.0638  163 ALA   O N   
25865 C  CA  . ALA   O  163 ? 1.8630 0.5901 1.6240 -0.3069 -0.4462 0.0617  163 ALA   O CA  
25866 C  C   . ALA   O  163 ? 1.8743 0.5584 1.5942 -0.3148 -0.4379 0.0666  163 ALA   O C   
25867 O  O   . ALA   O  163 ? 1.9188 0.5424 1.5988 -0.3363 -0.4454 0.0257  163 ALA   O O   
25868 C  CB  . ALA   O  163 ? 1.8642 0.5860 1.6535 -0.3153 -0.4421 0.0543  163 ALA   O CB  
25869 N  N   . ILE   O  164 ? 1.8945 0.5463 1.6285 -0.3050 -0.4668 0.0877  164 ILE   O N   
25870 C  CA  . ILE   O  164 ? 1.9097 0.5918 1.6275 -0.2679 -0.4680 0.0780  164 ILE   O CA  
25871 C  C   . ILE   O  164 ? 1.9464 0.6213 1.6267 -0.2474 -0.4933 0.0566  164 ILE   O C   
25872 O  O   . ILE   O  164 ? 1.9620 0.5449 1.6540 -0.2355 -0.4910 -0.0165 164 ILE   O O   
25873 C  CB  . ILE   O  164 ? 1.8831 0.6369 1.5656 -0.2765 -0.4710 0.1316  164 ILE   O CB  
25874 C  CG1 . ILE   O  164 ? 1.8589 0.6937 1.5221 -0.2683 -0.4798 0.1293  164 ILE   O CG1 
25875 C  CG2 . ILE   O  164 ? 1.9094 0.7301 1.5297 -0.2876 -0.4425 0.0971  164 ILE   O CG2 
25876 C  CD1 . ILE   O  164 ? 1.8026 0.7320 1.5099 -0.2646 -0.4931 0.1313  164 ILE   O CD1 
25877 N  N   . GLY   O  165 ? 1.9816 0.6961 1.6927 -0.2194 -0.4478 0.0091  165 GLY   O N   
25878 C  CA  . GLY   O  165 ? 2.0479 0.7483 1.6862 -0.1704 -0.4292 0.0224  165 GLY   O CA  
25879 C  C   . GLY   O  165 ? 2.1489 0.7319 1.6976 -0.1603 -0.3890 -0.0286 165 GLY   O C   
25880 O  O   . GLY   O  165 ? 2.2199 0.7825 1.7366 -0.1404 -0.3709 -0.1107 165 GLY   O O   
25881 N  N   . LYS   O  166 ? 2.1714 0.7218 1.7305 -0.1147 -0.3513 0.0122  166 LYS   O N   
25882 C  CA  . LYS   O  166 ? 2.1337 0.6954 1.8008 -0.0659 -0.3222 -0.0011 166 LYS   O CA  
25883 C  C   . LYS   O  166 ? 2.1256 0.6830 1.7405 -0.0839 -0.3040 0.0444  166 LYS   O C   
25884 O  O   . LYS   O  166 ? 2.1650 0.7293 1.7687 -0.0304 -0.2546 0.0437  166 LYS   O O   
25885 C  CB  . LYS   O  166 ? 2.1018 0.6684 1.8167 -0.0270 -0.3333 0.0512  166 LYS   O CB  
25886 C  CG  . LYS   O  166 ? 2.0703 0.7748 1.9035 0.0677  -0.3727 0.0456  166 LYS   O CG  
25887 C  CD  . LYS   O  166 ? 2.0636 0.9395 1.9177 0.0998  -0.3578 -0.0062 166 LYS   O CD  
25888 C  CE  . LYS   O  166 ? 2.1388 1.0498 1.9646 0.1462  -0.3653 0.0619  166 LYS   O CE  
25889 N  NZ  . LYS   O  166 ? 2.1473 1.2067 2.0263 0.1414  -0.3555 0.0528  166 LYS   O NZ  
25890 N  N   . GLY   O  167 ? 2.0937 0.7188 1.7239 -0.1150 -0.3222 0.1001  167 GLY   O N   
25891 C  CA  . GLY   O  167 ? 2.0412 0.7602 1.7641 -0.1082 -0.3364 0.1726  167 GLY   O CA  
25892 C  C   . GLY   O  167 ? 1.9838 0.7377 1.8321 -0.1143 -0.3488 0.1787  167 GLY   O C   
25893 O  O   . GLY   O  167 ? 1.9919 0.7256 1.8443 -0.0506 -0.3274 0.2668  167 GLY   O O   
25894 N  N   . SER   O  168 ? 1.9511 0.5921 1.8642 -0.1527 -0.3790 0.1412  168 SER   O N   
25895 C  CA  . SER   O  168 ? 1.9103 0.4447 1.8746 -0.1892 -0.3971 0.0831  168 SER   O CA  
25896 C  C   . SER   O  168 ? 1.9330 0.5136 1.8740 -0.2062 -0.4045 0.0651  168 SER   O C   
25897 O  O   . SER   O  168 ? 1.9554 0.3979 1.8326 -0.2396 -0.4281 0.1024  168 SER   O O   
25898 C  CB  . SER   O  168 ? 1.8780 0.3957 1.8736 -0.1665 -0.4104 0.0785  168 SER   O CB  
25899 O  OG  . SER   O  168 ? 1.8604 0.3380 1.8919 -0.1917 -0.4065 0.0910  168 SER   O OG  
25900 N  N   . VAL   O  169 ? 1.9395 0.5555 1.8130 -0.2857 -0.4083 -0.0671 169 VAL   O N   
25901 C  CA  . VAL   O  169 ? 1.9569 0.5064 1.8552 -0.3112 -0.3730 -0.1014 169 VAL   O CA  
25902 C  C   . VAL   O  169 ? 1.9775 0.4040 1.8652 -0.3207 -0.3514 -0.1486 169 VAL   O C   
25903 O  O   . VAL   O  169 ? 2.0403 0.3163 1.9171 -0.2966 -0.3992 -0.1788 169 VAL   O O   
25904 C  CB  . VAL   O  169 ? 1.9171 0.5568 1.8264 -0.2903 -0.3380 -0.0881 169 VAL   O CB  
25905 C  CG1 . VAL   O  169 ? 1.9265 0.6909 1.8067 -0.2982 -0.3348 -0.0965 169 VAL   O CG1 
25906 C  CG2 . VAL   O  169 ? 1.9150 0.5130 1.7616 -0.2974 -0.3540 -0.0990 169 VAL   O CG2 
25907 N  N   . ALA   O  170 ? 1.9889 0.3748 1.8518 -0.2991 -0.3397 -0.1607 170 ALA   O N   
25908 C  CA  . ALA   O  170 ? 1.9964 0.5382 1.8439 -0.2740 -0.3062 -0.1489 170 ALA   O CA  
25909 C  C   . ALA   O  170 ? 1.9388 0.5618 1.8229 -0.2876 -0.2948 -0.1725 170 ALA   O C   
25910 O  O   . ALA   O  170 ? 1.9321 0.5717 1.8722 -0.3222 -0.2765 -0.2179 170 ALA   O O   
25911 C  CB  . ALA   O  170 ? 2.0269 0.5917 1.8282 -0.2340 -0.2855 -0.1459 170 ALA   O CB  
25912 N  N   . ALA   O  171 ? 1.8553 0.6436 1.7604 -0.2974 -0.3225 -0.1766 171 ALA   O N   
25913 C  CA  . ALA   O  171 ? 1.8134 0.6923 1.7726 -0.2459 -0.3038 -0.1378 171 ALA   O CA  
25914 C  C   . ALA   O  171 ? 1.8103 0.7088 1.7912 -0.2512 -0.3187 -0.1295 171 ALA   O C   
25915 O  O   . ALA   O  171 ? 1.8164 0.7588 1.7927 -0.2374 -0.3122 -0.1169 171 ALA   O O   
25916 C  CB  . ALA   O  171 ? 1.7890 0.6867 1.7319 -0.2402 -0.2987 -0.1118 171 ALA   O CB  
25917 N  N   . LYS   O  172 ? 1.7923 0.7014 1.8315 -0.2389 -0.2994 -0.1313 172 LYS   O N   
25918 C  CA  . LYS   O  172 ? 1.8155 0.7400 1.8709 -0.2084 -0.3100 -0.1022 172 LYS   O CA  
25919 C  C   . LYS   O  172 ? 1.8530 0.7522 1.9018 -0.2407 -0.3016 -0.1243 172 LYS   O C   
25920 O  O   . LYS   O  172 ? 1.8498 0.7309 1.8761 -0.2865 -0.3485 -0.1208 172 LYS   O O   
25921 C  CB  . LYS   O  172 ? 1.8086 0.7815 1.8793 -0.1666 -0.3141 -0.1112 172 LYS   O CB  
25922 C  CG  . LYS   O  172 ? 1.7794 0.8170 1.8619 -0.1528 -0.3384 -0.1184 172 LYS   O CG  
25923 C  CD  . LYS   O  172 ? 1.7697 0.8508 1.8436 -0.1441 -0.3510 -0.1166 172 LYS   O CD  
25924 C  CE  . LYS   O  172 ? 1.8001 0.8825 1.8386 -0.1455 -0.3317 -0.1320 172 LYS   O CE  
25925 N  NZ  . LYS   O  172 ? 1.7682 0.8740 1.8614 -0.1731 -0.3211 -0.1535 172 LYS   O NZ  
25926 N  N   . THR   O  173 ? 1.9172 0.7539 1.9213 -0.2405 -0.2584 -0.1038 173 THR   O N   
25927 C  CA  . THR   O  173 ? 1.9147 0.8262 1.9632 -0.2835 -0.2435 -0.0589 173 THR   O CA  
25928 C  C   . THR   O  173 ? 1.9453 0.7210 1.9304 -0.2635 -0.2403 -0.0315 173 THR   O C   
25929 O  O   . THR   O  173 ? 1.9442 0.6888 1.9995 -0.2099 -0.2468 0.0076  173 THR   O O   
25930 C  CB  . THR   O  173 ? 1.9369 0.8362 1.9836 -0.2688 -0.1873 -0.0580 173 THR   O CB  
25931 O  OG1 . THR   O  173 ? 1.9673 0.9387 1.9805 -0.2234 -0.1691 -0.0667 173 THR   O OG1 
25932 C  CG2 . THR   O  173 ? 1.9519 0.8237 2.0207 -0.3099 -0.1544 -0.0728 173 THR   O CG2 
25933 N  N   . PHE   O  174 ? 1.9691 0.6678 1.9233 -0.3126 -0.2521 -0.0055 174 PHE   O N   
25934 C  CA  . PHE   O  174 ? 1.9631 0.7785 1.9090 -0.3613 -0.2394 0.0050  174 PHE   O CA  
25935 C  C   . PHE   O  174 ? 1.9290 0.8130 1.9230 -0.3713 -0.3097 0.0311  174 PHE   O C   
25936 O  O   . PHE   O  174 ? 1.9087 0.9392 1.9231 -0.4451 -0.3357 0.0275  174 PHE   O O   
25937 C  CB  . PHE   O  174 ? 1.9844 0.7997 1.8827 -0.3732 -0.2055 0.0076  174 PHE   O CB  
25938 C  CG  . PHE   O  174 ? 2.0359 0.8625 1.8699 -0.3881 -0.1803 -0.0093 174 PHE   O CG  
25939 C  CD1 . PHE   O  174 ? 2.0151 0.8613 1.8219 -0.4084 -0.1662 -0.0246 174 PHE   O CD1 
25940 C  CD2 . PHE   O  174 ? 2.0783 0.9061 1.8450 -0.4070 -0.1362 -0.0013 174 PHE   O CD2 
25941 C  CE1 . PHE   O  174 ? 2.0346 0.8901 1.8253 -0.4080 -0.1528 -0.0297 174 PHE   O CE1 
25942 C  CE2 . PHE   O  174 ? 2.0945 0.9063 1.8423 -0.4191 -0.1274 -0.0056 174 PHE   O CE2 
25943 C  CZ  . PHE   O  174 ? 2.0676 0.9225 1.8243 -0.4104 -0.1259 -0.0090 174 PHE   O CZ  
25944 N  N   . LEU   O  175 ? 1.9333 0.7534 1.9244 -0.3420 -0.3560 0.0609  175 LEU   O N   
25945 C  CA  . LEU   O  175 ? 1.9144 0.7905 1.9161 -0.3069 -0.4055 0.0878  175 LEU   O CA  
25946 C  C   . LEU   O  175 ? 1.9498 0.8125 1.9666 -0.3153 -0.4630 0.0272  175 LEU   O C   
25947 O  O   . LEU   O  175 ? 1.8939 0.9161 2.0511 -0.3113 -0.5343 -0.0259 175 LEU   O O   
25948 C  CB  . LEU   O  175 ? 1.8823 0.7379 1.8824 -0.2654 -0.3967 0.1433  175 LEU   O CB  
25949 C  CG  . LEU   O  175 ? 1.8447 0.6525 1.8502 -0.2648 -0.3754 0.1884  175 LEU   O CG  
25950 C  CD1 . LEU   O  175 ? 1.8149 0.6211 1.8357 -0.2321 -0.3930 0.1935  175 LEU   O CD1 
25951 C  CD2 . LEU   O  175 ? 1.8439 0.5802 1.8287 -0.2877 -0.3722 0.2078  175 LEU   O CD2 
25952 N  N   . GLU   O  176 ? 1.9509 0.8103 1.9962 -0.2853 -0.4702 0.0160  176 GLU   O N   
25953 C  CA  . GLU   O  176 ? 1.9295 0.8778 2.0018 -0.2833 -0.4668 -0.0073 176 GLU   O CA  
25954 C  C   . GLU   O  176 ? 1.9648 0.8131 1.9865 -0.3573 -0.4860 0.0056  176 GLU   O C   
25955 O  O   . GLU   O  176 ? 1.9792 0.7104 1.9992 -0.3911 -0.5072 -0.0111 176 GLU   O O   
25956 C  CB  . GLU   O  176 ? 1.9293 0.9722 2.0512 -0.2511 -0.4467 -0.0418 176 GLU   O CB  
25957 C  CG  . GLU   O  176 ? 1.8977 1.0483 2.0601 -0.1941 -0.3948 -0.0879 176 GLU   O CG  
25958 C  CD  . GLU   O  176 ? 1.9213 1.1565 2.0745 -0.2030 -0.3706 -0.1560 176 GLU   O CD  
25959 O  OE1 . GLU   O  176 ? 1.8249 1.3344 2.0736 -0.2027 -0.3694 -0.2204 176 GLU   O OE1 
25960 O  OE2 . GLU   O  176 ? 1.9075 1.2002 2.1214 -0.1393 -0.2583 -0.1718 176 GLU   O OE2 
25961 N  N   . LYS   O  177 ? 1.9647 0.8791 1.9830 -0.4018 -0.4561 0.0156  177 LYS   O N   
25962 C  CA  . LYS   O  177 ? 1.9743 0.9705 2.0140 -0.4103 -0.4205 0.0217  177 LYS   O CA  
25963 C  C   . LYS   O  177 ? 1.9427 0.9798 2.0179 -0.4426 -0.3985 0.0000  177 LYS   O C   
25964 O  O   . LYS   O  177 ? 1.9231 1.1481 2.0671 -0.5018 -0.3765 -0.0543 177 LYS   O O   
25965 C  CB  . LYS   O  177 ? 2.0372 0.9525 2.0516 -0.4397 -0.3856 0.0295  177 LYS   O CB  
25966 C  CG  . LYS   O  177 ? 2.0893 0.8907 2.0823 -0.4669 -0.3623 0.0734  177 LYS   O CG  
25967 C  CD  . LYS   O  177 ? 2.1220 0.9263 2.1034 -0.4864 -0.3196 0.1046  177 LYS   O CD  
25968 C  CE  . LYS   O  177 ? 2.1839 0.8718 2.1329 -0.5231 -0.3043 0.1276  177 LYS   O CE  
25969 N  NZ  . LYS   O  177 ? 2.2497 0.8212 2.1554 -0.5616 -0.2601 0.1296  177 LYS   O NZ  
25970 N  N   . ARG   O  178 ? 1.9444 0.8774 2.0276 -0.4335 -0.3538 0.0126  178 ARG   O N   
25971 C  CA  . ARG   O  178 ? 1.9599 1.0203 2.0721 -0.4159 -0.3177 -0.0412 178 ARG   O CA  
25972 C  C   . ARG   O  178 ? 1.9103 1.0145 2.1106 -0.4341 -0.3400 -0.0516 178 ARG   O C   
25973 O  O   . ARG   O  178 ? 1.9400 1.0137 2.1301 -0.4582 -0.3183 -0.1409 178 ARG   O O   
25974 C  CB  . ARG   O  178 ? 2.0069 1.0679 2.0470 -0.4088 -0.2954 -0.1014 178 ARG   O CB  
25975 C  CG  . ARG   O  178 ? 2.1282 1.0644 2.0974 -0.3578 -0.2587 -0.1175 178 ARG   O CG  
25976 C  CD  . ARG   O  178 ? 2.1121 1.2690 2.2149 -0.3780 -0.2079 -0.1749 178 ARG   O CD  
25977 N  NE  . ARG   O  178 ? 2.2355 1.3438 2.1761 -0.3176 -0.1705 -0.1884 178 ARG   O NE  
25978 C  CZ  . ARG   O  178 ? 2.2285 1.3818 2.1628 -0.3341 -0.2073 -0.2374 178 ARG   O CZ  
25979 N  NH1 . ARG   O  178 ? 2.2090 1.3775 2.1657 -0.3617 -0.2222 -0.3073 178 ARG   O NH1 
25980 N  NH2 . ARG   O  178 ? 2.2264 1.3609 2.1454 -0.3327 -0.2145 -0.2521 178 ARG   O NH2 
25981 N  N   . TRP   O  179 ? 1.8269 0.9010 2.1479 -0.4749 -0.3946 -0.0607 179 TRP   O N   
25982 C  CA  . TRP   O  179 ? 1.8100 0.8840 2.1570 -0.4380 -0.4344 -0.0617 179 TRP   O CA  
25983 C  C   . TRP   O  179 ? 1.7887 0.8365 2.1721 -0.4828 -0.4367 -0.0444 179 TRP   O C   
25984 O  O   . TRP   O  179 ? 1.8665 0.8143 2.1903 -0.4301 -0.4160 -0.0543 179 TRP   O O   
25985 C  CB  . TRP   O  179 ? 1.7835 0.9106 2.1199 -0.3856 -0.4530 -0.0328 179 TRP   O CB  
25986 C  CG  . TRP   O  179 ? 1.7945 0.9215 2.0961 -0.3745 -0.4750 -0.0055 179 TRP   O CG  
25987 C  CD1 . TRP   O  179 ? 1.7728 0.9273 2.0789 -0.3473 -0.4896 -0.0081 179 TRP   O CD1 
25988 C  CD2 . TRP   O  179 ? 1.8281 0.9799 2.0515 -0.3664 -0.4913 -0.0279 179 TRP   O CD2 
25989 N  NE1 . TRP   O  179 ? 1.7708 0.8971 2.0516 -0.3474 -0.5033 -0.0444 179 TRP   O NE1 
25990 C  CE2 . TRP   O  179 ? 1.8128 0.9333 2.0312 -0.3214 -0.4927 0.0265  179 TRP   O CE2 
25991 C  CE3 . TRP   O  179 ? 1.8665 1.0315 2.0147 -0.3564 -0.4745 -0.0180 179 TRP   O CE3 
25992 C  CZ2 . TRP   O  179 ? 1.8078 0.9084 2.0262 -0.3260 -0.4777 0.0193  179 TRP   O CZ2 
25993 C  CZ3 . TRP   O  179 ? 1.8712 0.9671 2.0051 -0.3573 -0.4690 -0.0507 179 TRP   O CZ3 
25994 C  CH2 . TRP   O  179 ? 1.8586 0.9269 2.0177 -0.3242 -0.4616 -0.0027 179 TRP   O CH2 
25995 N  N   . ASN   O  180 ? 1.6914 0.9388 2.2049 -0.4417 -0.4345 0.0257  180 ASN   O N   
25996 C  CA  . ASN   O  180 ? 1.6411 1.0727 2.2176 -0.4598 -0.4317 0.0628  180 ASN   O CA  
25997 C  C   . ASN   O  180 ? 1.6183 1.0530 2.1890 -0.4003 -0.4552 0.0478  180 ASN   O C   
25998 O  O   . ASN   O  180 ? 1.5427 0.8744 2.2029 -0.3702 -0.4299 0.0562  180 ASN   O O   
25999 C  CB  . ASN   O  180 ? 1.6718 1.0872 2.2505 -0.5165 -0.3999 0.1162  180 ASN   O CB  
26000 C  CG  . ASN   O  180 ? 1.6159 1.0556 2.2378 -0.5686 -0.3602 0.1701  180 ASN   O CG  
26001 O  OD1 . ASN   O  180 ? 1.5656 1.0708 2.1996 -0.5527 -0.3694 0.1440  180 ASN   O OD1 
26002 N  ND2 . ASN   O  180 ? 1.6444 1.1057 2.2590 -0.6008 -0.3195 0.1877  180 ASN   O ND2 
26003 N  N   . ASP   O  181 ? 1.6376 1.2064 2.1608 -0.3541 -0.4770 0.0427  181 ASP   O N   
26004 C  CA  . ASP   O  181 ? 1.6372 1.2168 2.1143 -0.3376 -0.4837 0.0550  181 ASP   O CA  
26005 C  C   . ASP   O  181 ? 1.6160 1.2632 2.1410 -0.2976 -0.4851 0.0713  181 ASP   O C   
26006 O  O   . ASP   O  181 ? 1.5859 1.2665 2.1046 -0.2051 -0.5516 0.1023  181 ASP   O O   
26007 C  CB  . ASP   O  181 ? 1.7394 1.4015 2.1034 -0.3187 -0.4778 0.0507  181 ASP   O CB  
26008 C  CG  . ASP   O  181 ? 1.7671 1.5580 2.1227 -0.3286 -0.4986 0.0577  181 ASP   O CG  
26009 O  OD1 . ASP   O  181 ? 1.8794 1.6391 2.1755 -0.3516 -0.4171 0.0996  181 ASP   O OD1 
26010 O  OD2 . ASP   O  181 ? 1.9446 1.7552 2.1275 -0.2575 -0.4507 0.0967  181 ASP   O OD2 
26011 N  N   . GLU   O  182 ? 1.6113 1.1927 2.1745 -0.2582 -0.4204 0.0212  182 GLU   O N   
26012 C  CA  . GLU   O  182 ? 1.6589 1.1747 2.2093 -0.2376 -0.3890 0.0193  182 GLU   O CA  
26013 C  C   . GLU   O  182 ? 1.6854 1.0450 2.1843 -0.2012 -0.3279 0.0175  182 GLU   O C   
26014 O  O   . GLU   O  182 ? 1.6584 0.9321 2.2387 -0.1686 -0.3442 0.0057  182 GLU   O O   
26015 C  CB  . GLU   O  182 ? 1.6318 1.2606 2.2519 -0.2249 -0.3674 -0.0182 182 GLU   O CB  
26016 C  CG  . GLU   O  182 ? 1.6360 1.3227 2.2658 -0.1787 -0.3622 -0.0051 182 GLU   O CG  
26017 C  CD  . GLU   O  182 ? 1.6068 1.4417 2.3039 -0.1634 -0.3892 -0.0283 182 GLU   O CD  
26018 O  OE1 . GLU   O  182 ? 1.6722 1.5383 2.3169 -0.1263 -0.3847 -0.1045 182 GLU   O OE1 
26019 O  OE2 . GLU   O  182 ? 1.6511 1.4678 2.3516 -0.1031 -0.3830 -0.0346 182 GLU   O OE2 
26020 N  N   . LEU   O  183 ? 1.7285 1.0058 2.1355 -0.1876 -0.3291 0.0634  183 LEU   O N   
26021 C  CA  . LEU   O  183 ? 1.7936 1.0114 2.1114 -0.2148 -0.2908 0.0682  183 LEU   O CA  
26022 C  C   . LEU   O  183 ? 1.7850 0.9761 2.0929 -0.2389 -0.2904 0.1123  183 LEU   O C   
26023 O  O   . LEU   O  183 ? 1.7612 0.9921 2.0970 -0.2844 -0.3248 0.0976  183 LEU   O O   
26024 C  CB  . LEU   O  183 ? 1.8134 0.9972 2.1027 -0.1974 -0.2633 0.0764  183 LEU   O CB  
26025 C  CG  . LEU   O  183 ? 1.8656 0.9824 2.1161 -0.1976 -0.2266 0.1143  183 LEU   O CG  
26026 C  CD1 . LEU   O  183 ? 1.8695 0.9082 2.0898 -0.2085 -0.2053 0.1147  183 LEU   O CD1 
26027 C  CD2 . LEU   O  183 ? 1.8744 0.9975 2.1320 -0.1808 -0.2030 0.1225  183 LEU   O CD2 
26028 N  N   . GLU   O  184 ? 1.8167 1.0276 2.0965 -0.2326 -0.2836 0.0968  184 GLU   O N   
26029 C  CA  . GLU   O  184 ? 1.8051 1.0341 2.1068 -0.2351 -0.2825 0.0847  184 GLU   O CA  
26030 C  C   . GLU   O  184 ? 1.8190 1.0433 2.0848 -0.2089 -0.2841 0.0762  184 GLU   O C   
26031 O  O   . GLU   O  184 ? 1.8077 1.0891 2.0900 -0.1399 -0.3279 0.0583  184 GLU   O O   
26032 C  CB  . GLU   O  184 ? 1.8374 1.1115 2.1645 -0.2819 -0.2275 0.0608  184 GLU   O CB  
26033 C  CG  . GLU   O  184 ? 1.8774 1.1410 2.2205 -0.2757 -0.1514 0.0338  184 GLU   O CG  
26034 C  CD  . GLU   O  184 ? 1.9298 1.2318 2.2032 -0.2869 -0.0765 0.0337  184 GLU   O CD  
26035 O  OE1 . GLU   O  184 ? 2.0166 1.1215 2.3145 -0.2791 -0.0301 0.0372  184 GLU   O OE1 
26036 O  OE2 . GLU   O  184 ? 1.9084 1.2837 2.2933 -0.3560 -0.0157 0.0667  184 GLU   O OE2 
26037 N  N   . LEU   O  185 ? 1.7368 1.0500 2.0548 -0.1590 -0.3315 0.0718  185 LEU   O N   
26038 C  CA  . LEU   O  185 ? 1.7251 1.1022 2.0594 -0.1646 -0.3342 0.0328  185 LEU   O CA  
26039 C  C   . LEU   O  185 ? 1.7596 1.0995 2.0021 -0.2028 -0.3350 -0.0192 185 LEU   O C   
26040 O  O   . LEU   O  185 ? 1.7415 1.2323 2.0097 -0.1371 -0.3613 -0.1575 185 LEU   O O   
26041 C  CB  . LEU   O  185 ? 1.6564 1.1083 2.0555 -0.1723 -0.3569 0.0638  185 LEU   O CB  
26042 C  CG  . LEU   O  185 ? 1.6407 1.1663 2.0606 -0.1382 -0.3528 0.1320  185 LEU   O CG  
26043 C  CD1 . LEU   O  185 ? 1.6378 1.1518 2.0081 -0.1334 -0.3748 0.1305  185 LEU   O CD1 
26044 C  CD2 . LEU   O  185 ? 1.6077 1.1783 2.0684 -0.1437 -0.3669 0.1167  185 LEU   O CD2 
26045 N  N   . GLU   O  186 ? 1.7936 1.1569 2.0288 -0.2289 -0.2999 -0.0438 186 GLU   O N   
26046 C  CA  . GLU   O  186 ? 1.8453 1.1885 2.0494 -0.2464 -0.2503 -0.0309 186 GLU   O CA  
26047 C  C   . GLU   O  186 ? 1.8727 1.0936 2.0564 -0.2482 -0.2434 0.1040  186 GLU   O C   
26048 O  O   . GLU   O  186 ? 1.8829 1.1227 2.0546 -0.2247 -0.2057 0.1322  186 GLU   O O   
26049 C  CB  . GLU   O  186 ? 1.8710 1.2616 2.0924 -0.2347 -0.2235 -0.0620 186 GLU   O CB  
26050 C  CG  . GLU   O  186 ? 1.8809 1.2810 2.1089 -0.2139 -0.1781 -0.0910 186 GLU   O CG  
26051 C  CD  . GLU   O  186 ? 1.9220 1.2656 2.0871 -0.2126 -0.1549 -0.0755 186 GLU   O CD  
26052 O  OE1 . GLU   O  186 ? 2.0277 1.2034 2.1433 -0.3014 -0.1200 -0.0187 186 GLU   O OE1 
26053 O  OE2 . GLU   O  186 ? 1.8843 1.4402 2.0774 -0.1921 -0.1054 -0.1759 186 GLU   O OE2 
26054 N  N   . ASP   O  187 ? 1.8734 1.0985 2.0883 -0.2723 -0.2756 0.1028  187 ASP   O N   
26055 C  CA  . ASP   O  187 ? 1.8379 1.1369 2.1375 -0.2379 -0.3119 0.0573  187 ASP   O CA  
26056 C  C   . ASP   O  187 ? 1.8053 1.0629 2.1255 -0.2308 -0.3774 0.1021  187 ASP   O C   
26057 O  O   . ASP   O  187 ? 1.8254 1.1146 2.1362 -0.1046 -0.4495 0.0824  187 ASP   O O   
26058 C  CB  . ASP   O  187 ? 1.8488 1.2445 2.1673 -0.2573 -0.3295 0.0554  187 ASP   O CB  
26059 C  CG  . ASP   O  187 ? 1.8587 1.2862 2.1974 -0.2386 -0.3134 0.0591  187 ASP   O CG  
26060 O  OD1 . ASP   O  187 ? 1.8892 1.5028 2.2083 -0.2191 -0.2308 0.0057  187 ASP   O OD1 
26061 O  OD2 . ASP   O  187 ? 1.7757 1.1722 2.2101 -0.2497 -0.3024 0.0204  187 ASP   O OD2 
26062 N  N   . ALA   O  188 ? 1.8008 0.9349 2.1201 -0.1844 -0.4155 0.1152  188 ALA   O N   
26063 C  CA  . ALA   O  188 ? 1.8046 0.8878 2.0968 -0.1876 -0.4155 0.0968  188 ALA   O CA  
26064 C  C   . ALA   O  188 ? 1.7908 0.8419 2.0756 -0.1905 -0.3914 0.0847  188 ALA   O C   
26065 O  O   . ALA   O  188 ? 1.7950 0.9343 2.1702 -0.1485 -0.3568 0.0016  188 ALA   O O   
26066 C  CB  . ALA   O  188 ? 1.7658 0.9241 2.0344 -0.1980 -0.4313 0.0900  188 ALA   O CB  
26067 N  N   . ILE   O  189 ? 1.7889 0.8248 2.0508 -0.2149 -0.3503 0.1168  189 ILE   O N   
26068 C  CA  . ILE   O  189 ? 1.7694 0.8479 2.0056 -0.1992 -0.3147 0.0953  189 ILE   O CA  
26069 C  C   . ILE   O  189 ? 1.7788 0.8708 1.9904 -0.1800 -0.3039 0.1357  189 ILE   O C   
26070 O  O   . ILE   O  189 ? 1.7676 0.9960 1.9223 -0.1566 -0.3155 0.1399  189 ILE   O O   
26071 C  CB  . ILE   O  189 ? 1.7605 0.8551 1.9918 -0.1874 -0.3121 0.1025  189 ILE   O CB  
26072 C  CG1 . ILE   O  189 ? 1.7300 0.8046 1.9615 -0.1228 -0.3427 0.0924  189 ILE   O CG1 
26073 C  CG2 . ILE   O  189 ? 1.7631 0.8486 1.9859 -0.1935 -0.2814 0.1267  189 ILE   O CG2 
26074 C  CD1 . ILE   O  189 ? 1.7266 0.7867 1.9830 -0.1219 -0.3432 0.0964  189 ILE   O CD1 
26075 N  N   . HIS   O  190 ? 1.7950 0.8284 2.0489 -0.2112 -0.2677 0.1360  190 HIS   O N   
26076 C  CA  . HIS   O  190 ? 1.8399 0.8081 2.0874 -0.2184 -0.2500 0.1216  190 HIS   O CA  
26077 C  C   . HIS   O  190 ? 1.8729 0.7213 2.1094 -0.2219 -0.2634 0.1530  190 HIS   O C   
26078 O  O   . HIS   O  190 ? 1.8705 0.7147 2.1275 -0.2115 -0.2621 0.1534  190 HIS   O O   
26079 C  CB  . HIS   O  190 ? 1.8295 0.8188 2.1414 -0.2481 -0.2211 0.1503  190 HIS   O CB  
26080 C  CG  . HIS   O  190 ? 1.8234 0.8589 2.1719 -0.2620 -0.2008 0.1870  190 HIS   O CG  
26081 N  ND1 . HIS   O  190 ? 1.8703 0.8452 2.1739 -0.2444 -0.1890 0.1893  190 HIS   O ND1 
26082 C  CD2 . HIS   O  190 ? 1.8128 0.8294 2.1869 -0.2433 -0.2139 0.1954  190 HIS   O CD2 
26083 C  CE1 . HIS   O  190 ? 1.8913 0.8308 2.2091 -0.2381 -0.1786 0.2233  190 HIS   O CE1 
26084 N  NE2 . HIS   O  190 ? 1.8555 0.8292 2.2202 -0.2424 -0.2045 0.2116  190 HIS   O NE2 
26085 N  N   . ILE   O  191 ? 1.9032 0.7006 2.1032 -0.2243 -0.2657 0.1276  191 ILE   O N   
26086 C  CA  . ILE   O  191 ? 1.9082 0.6901 2.0642 -0.2355 -0.2854 0.1252  191 ILE   O CA  
26087 C  C   . ILE   O  191 ? 1.9007 0.6800 2.0298 -0.2449 -0.2705 0.1163  191 ILE   O C   
26088 O  O   . ILE   O  191 ? 1.9027 0.6959 2.0199 -0.2344 -0.2766 0.0715  191 ILE   O O   
26089 C  CB  . ILE   O  191 ? 1.8972 0.6623 2.0669 -0.2431 -0.2991 0.1294  191 ILE   O CB  
26090 C  CG1 . ILE   O  191 ? 1.9034 0.6807 2.0943 -0.2590 -0.3138 0.1468  191 ILE   O CG1 
26091 C  CG2 . ILE   O  191 ? 1.8966 0.6688 2.0447 -0.2366 -0.3023 0.1391  191 ILE   O CG2 
26092 C  CD1 . ILE   O  191 ? 1.8878 0.6956 2.1090 -0.2521 -0.3246 0.1575  191 ILE   O CD1 
26093 N  N   . ALA   O  192 ? 1.9218 0.6335 1.9637 -0.2238 -0.2473 0.1448  192 ALA   O N   
26094 C  CA  . ALA   O  192 ? 1.9368 0.6740 1.9072 -0.1697 -0.2653 0.1243  192 ALA   O CA  
26095 C  C   . ALA   O  192 ? 1.9963 0.6442 1.9083 -0.1760 -0.2477 0.1199  192 ALA   O C   
26096 O  O   . ALA   O  192 ? 2.0149 0.6267 1.9434 -0.1685 -0.2330 0.1395  192 ALA   O O   
26097 C  CB  . ALA   O  192 ? 1.9344 0.6820 1.8326 -0.1584 -0.2877 0.0997  192 ALA   O CB  
26098 N  N   . LEU   O  193 ? 2.0192 0.6938 1.9510 -0.1682 -0.2185 0.0781  193 LEU   O N   
26099 C  CA  . LEU   O  193 ? 2.0637 0.8205 1.9469 -0.1416 -0.2213 0.1000  193 LEU   O CA  
26100 C  C   . LEU   O  193 ? 2.0523 0.8433 2.0114 -0.1738 -0.2530 0.0789  193 LEU   O C   
26101 O  O   . LEU   O  193 ? 2.0409 0.9143 2.0242 -0.1859 -0.2874 0.1092  193 LEU   O O   
26102 C  CB  . LEU   O  193 ? 2.1042 0.8498 2.0260 -0.1133 -0.1815 0.0834  193 LEU   O CB  
26103 C  CG  . LEU   O  193 ? 2.1008 0.8296 2.0345 -0.0873 -0.1642 0.0968  193 LEU   O CG  
26104 C  CD1 . LEU   O  193 ? 2.1065 0.9162 2.0876 -0.0626 -0.1427 0.1077  193 LEU   O CD1 
26105 C  CD2 . LEU   O  193 ? 2.1003 0.7766 2.0109 -0.0956 -0.1587 0.0851  193 LEU   O CD2 
26106 N  N   . LEU   O  194 ? 2.0513 0.8838 2.0324 -0.1784 -0.2683 0.0936  194 LEU   O N   
26107 C  CA  . LEU   O  194 ? 2.0465 0.8401 2.0277 -0.1667 -0.2447 0.1449  194 LEU   O CA  
26108 C  C   . LEU   O  194 ? 2.0389 0.7942 1.9447 -0.1817 -0.2595 0.1587  194 LEU   O C   
26109 O  O   . LEU   O  194 ? 1.9586 0.8118 1.9511 -0.2156 -0.1836 0.2320  194 LEU   O O   
26110 C  CB  . LEU   O  194 ? 2.0331 0.8382 2.0962 -0.1655 -0.2591 0.1377  194 LEU   O CB  
26111 C  CG  . LEU   O  194 ? 2.0582 0.8890 2.1510 -0.1293 -0.2207 0.1376  194 LEU   O CG  
26112 C  CD1 . LEU   O  194 ? 2.0548 0.9332 2.1750 -0.1346 -0.2316 0.1335  194 LEU   O CD1 
26113 C  CD2 . LEU   O  194 ? 2.1010 0.9200 2.1477 -0.0830 -0.2042 0.1805  194 LEU   O CD2 
26114 N  N   . THR   O  195 ? 2.0346 0.7983 1.8707 -0.1878 -0.2940 0.1303  195 THR   O N   
26115 C  CA  . THR   O  195 ? 2.0218 0.7957 1.8258 -0.2143 -0.3012 0.1491  195 THR   O CA  
26116 C  C   . THR   O  195 ? 2.0679 0.7925 1.7699 -0.3151 -0.3400 0.1341  195 THR   O C   
26117 O  O   . THR   O  195 ? 2.0616 0.8755 1.7380 -0.2781 -0.3174 0.1735  195 THR   O O   
26118 C  CB  . THR   O  195 ? 1.9814 0.7755 1.8240 -0.2022 -0.3151 0.1491  195 THR   O CB  
26119 O  OG1 . THR   O  195 ? 1.9920 0.8552 1.8406 -0.1612 -0.3005 0.1691  195 THR   O OG1 
26120 C  CG2 . THR   O  195 ? 1.9705 0.7656 1.8009 -0.1972 -0.3219 0.1762  195 THR   O CG2 
26121 N  N   . LEU   O  196 ? 2.1026 0.7586 1.7992 -0.3283 -0.3152 0.1238  196 LEU   O N   
26122 C  CA  . LEU   O  196 ? 2.1556 0.8693 1.7725 -0.3026 -0.3430 0.1437  196 LEU   O CA  
26123 C  C   . LEU   O  196 ? 2.1179 0.8048 1.7498 -0.2505 -0.3558 0.0973  196 LEU   O C   
26124 O  O   . LEU   O  196 ? 2.1966 0.9134 1.7353 -0.1610 -0.4143 0.0255  196 LEU   O O   
26125 C  CB  . LEU   O  196 ? 2.2267 0.9412 1.7290 -0.3293 -0.3303 0.1097  196 LEU   O CB  
26126 C  CG  . LEU   O  196 ? 2.2556 0.9262 1.7036 -0.3721 -0.3228 0.1606  196 LEU   O CG  
26127 C  CD1 . LEU   O  196 ? 2.2593 0.9491 1.7041 -0.3994 -0.3229 0.2111  196 LEU   O CD1 
26128 C  CD2 . LEU   O  196 ? 2.2598 0.8401 1.6668 -0.3918 -0.3116 0.2470  196 LEU   O CD2 
26129 N  N   . LYS   O  197 ? 2.0730 0.8391 1.7407 -0.2142 -0.3688 0.1165  197 LYS   O N   
26130 C  CA  . LYS   O  197 ? 2.0242 0.8854 1.7894 -0.2273 -0.3316 0.1639  197 LYS   O CA  
26131 C  C   . LYS   O  197 ? 2.0498 0.8120 1.8839 -0.2353 -0.2630 0.2484  197 LYS   O C   
26132 O  O   . LYS   O  197 ? 2.0384 0.9660 1.8906 -0.2025 -0.2911 0.2815  197 LYS   O O   
26133 C  CB  . LYS   O  197 ? 2.0189 0.9394 1.7639 -0.1868 -0.3274 0.1645  197 LYS   O CB  
26134 C  CG  . LYS   O  197 ? 2.0854 1.0570 1.7076 -0.1147 -0.3064 0.1964  197 LYS   O CG  
26135 C  CD  . LYS   O  197 ? 2.0951 1.1649 1.7003 -0.0795 -0.2756 0.1901  197 LYS   O CD  
26136 C  CE  . LYS   O  197 ? 2.1312 1.2085 1.6676 -0.0702 -0.2764 0.1788  197 LYS   O CE  
26137 N  NZ  . LYS   O  197 ? 2.1560 1.2819 1.7066 -0.0810 -0.2469 0.1778  197 LYS   O NZ  
26138 N  N   . GLU   O  198 ? 2.0905 0.7870 1.8841 -0.2261 -0.2230 0.2547  198 GLU   O N   
26139 C  CA  . GLU   O  198 ? 2.1817 0.8298 2.0053 -0.2311 -0.1720 0.1894  198 GLU   O CA  
26140 C  C   . GLU   O  198 ? 2.1783 0.8637 2.0404 -0.2676 -0.1682 0.1712  198 GLU   O C   
26141 O  O   . GLU   O  198 ? 2.2548 0.8212 1.9972 -0.2968 -0.1734 0.1508  198 GLU   O O   
26142 C  CB  . GLU   O  198 ? 2.2175 0.8472 2.0043 -0.2056 -0.1641 0.1610  198 GLU   O CB  
26143 C  CG  . GLU   O  198 ? 2.2257 0.9174 2.0960 -0.1666 -0.1506 0.1201  198 GLU   O CG  
26144 C  CD  . GLU   O  198 ? 2.3346 1.0176 2.1714 -0.2038 -0.0680 0.1677  198 GLU   O CD  
26145 O  OE1 . GLU   O  198 ? 2.5358 1.2850 2.2256 -0.0462 -0.0470 -0.0538 198 GLU   O OE1 
26146 O  OE2 . GLU   O  198 ? 2.4505 1.0636 2.1990 -0.0992 -0.0288 0.1353  198 GLU   O OE2 
26147 N  N   . SER   O  199 ? 2.1696 0.8227 2.1753 -0.2506 -0.1779 0.1134  199 SER   O N   
26148 C  CA  . SER   O  199 ? 2.1670 0.8635 2.2547 -0.2347 -0.1551 0.1243  199 SER   O CA  
26149 C  C   . SER   O  199 ? 2.1298 0.8390 2.3123 -0.2154 -0.2052 0.1034  199 SER   O C   
26150 O  O   . SER   O  199 ? 2.1051 0.7148 2.4233 -0.2766 -0.2127 0.0834  199 SER   O O   
26151 C  CB  . SER   O  199 ? 2.1277 0.9448 2.2668 -0.2521 -0.1157 0.1469  199 SER   O CB  
26152 O  OG  . SER   O  199 ? 2.0617 0.9514 2.2604 -0.2498 -0.0307 0.2334  199 SER   O OG  
26153 N  N   . VAL   O  200 ? 2.0982 0.8893 2.3305 -0.2146 -0.2134 0.0839  200 VAL   O N   
26154 C  CA  . VAL   O  200 ? 2.0569 1.0522 2.3477 -0.2328 -0.2406 0.0828  200 VAL   O CA  
26155 C  C   . VAL   O  200 ? 2.0543 1.0213 2.3666 -0.2196 -0.2304 0.0545  200 VAL   O C   
26156 O  O   . VAL   O  200 ? 2.0224 1.0928 2.4720 -0.2102 -0.2282 0.0549  200 VAL   O O   
26157 C  CB  . VAL   O  200 ? 1.9933 1.1327 2.3038 -0.2090 -0.2270 0.1015  200 VAL   O CB  
26158 C  CG1 . VAL   O  200 ? 2.0041 1.2424 2.2852 -0.2206 -0.2154 0.1459  200 VAL   O CG1 
26159 C  CG2 . VAL   O  200 ? 1.9604 1.1089 2.3465 -0.2178 -0.2589 0.0927  200 VAL   O CG2 
26160 N  N   . GLU   O  201 ? 2.0750 1.1274 2.3349 -0.2096 -0.2495 0.0190  201 GLU   O N   
26161 C  CA  . GLU   O  201 ? 2.1268 1.1579 2.3619 -0.2504 -0.1950 0.0426  201 GLU   O CA  
26162 C  C   . GLU   O  201 ? 2.1730 1.1048 2.3798 -0.3033 -0.1391 0.0617  201 GLU   O C   
26163 O  O   . GLU   O  201 ? 2.2265 1.2276 2.4565 -0.3228 -0.0499 0.0901  201 GLU   O O   
26164 C  CB  . GLU   O  201 ? 2.1261 1.3375 2.3992 -0.1981 -0.2493 -0.0217 201 GLU   O CB  
26165 C  CG  . GLU   O  201 ? 2.1163 1.3488 2.4921 -0.1557 -0.2744 -0.0462 201 GLU   O CG  
26166 C  CD  . GLU   O  201 ? 2.1102 1.5018 2.5540 -0.1357 -0.3198 -0.1727 201 GLU   O CD  
26167 O  OE1 . GLU   O  201 ? 1.9947 1.5909 2.7410 -0.1994 -0.3622 -0.2372 201 GLU   O OE1 
26168 O  OE2 . GLU   O  201 ? 2.0605 1.7995 2.6401 -0.0896 -0.2880 -0.1261 201 GLU   O OE2 
26169 N  N   . GLY   O  202 ? 2.1886 0.9759 2.3715 -0.2848 -0.1345 0.1095  202 GLY   O N   
26170 C  CA  . GLY   O  202 ? 2.2119 0.8614 2.3642 -0.2661 -0.1390 0.1444  202 GLY   O CA  
26171 C  C   . GLY   O  202 ? 2.2262 0.7456 2.3522 -0.2891 -0.1447 0.1727  202 GLY   O C   
26172 O  O   . GLY   O  202 ? 2.2353 0.3545 2.3997 -0.3808 -0.1418 0.2845  202 GLY   O O   
26173 N  N   . GLU   O  203 ? 2.2590 0.8365 2.2890 -0.2098 -0.1439 0.1299  203 GLU   O N   
26174 C  CA  . GLU   O  203 ? 2.2738 1.0090 2.2447 -0.1600 -0.1301 0.0821  203 GLU   O CA  
26175 C  C   . GLU   O  203 ? 2.2877 1.0523 2.2537 -0.1725 -0.1411 0.0975  203 GLU   O C   
26176 O  O   . GLU   O  203 ? 2.2978 1.0528 2.3475 -0.2621 -0.1192 0.0389  203 GLU   O O   
26177 C  CB  . GLU   O  203 ? 2.2597 1.0923 2.2123 -0.0980 -0.1299 0.0379  203 GLU   O CB  
26178 C  CG  . GLU   O  203 ? 2.3148 1.1973 2.1882 -0.0314 -0.1828 -0.0160 203 GLU   O CG  
26179 C  CD  . GLU   O  203 ? 2.2980 1.2158 2.2901 -0.0791 -0.1566 -0.1071 203 GLU   O CD  
26180 O  OE1 . GLU   O  203 ? 2.3869 1.5128 2.3160 0.0654  -0.1590 -0.1611 203 GLU   O OE1 
26181 O  OE2 . GLU   O  203 ? 2.4502 1.1229 2.3906 -0.0269 -0.1604 -0.2042 203 GLU   O OE2 
26182 N  N   . PHE   O  204 ? 2.2938 1.0449 2.1581 -0.1537 -0.1267 0.1656  204 PHE   O N   
26183 C  CA  . PHE   O  204 ? 2.3376 0.9631 2.1200 -0.1980 -0.1021 0.1844  204 PHE   O CA  
26184 C  C   . PHE   O  204 ? 2.3027 0.9924 2.0602 -0.1743 -0.1244 0.2233  204 PHE   O C   
26185 O  O   . PHE   O  204 ? 2.3224 0.9176 2.1466 -0.2161 -0.1253 0.2858  204 PHE   O O   
26186 C  CB  . PHE   O  204 ? 2.3601 0.9206 2.0267 -0.1904 -0.0548 0.1984  204 PHE   O CB  
26187 C  CG  . PHE   O  204 ? 2.3597 0.9560 1.9595 -0.2279 -0.0223 0.1746  204 PHE   O CG  
26188 C  CD1 . PHE   O  204 ? 2.3632 0.8993 1.9161 -0.2410 -0.0414 0.1683  204 PHE   O CD1 
26189 C  CD2 . PHE   O  204 ? 2.3341 1.0361 1.9127 -0.2591 -0.0165 0.1892  204 PHE   O CD2 
26190 C  CE1 . PHE   O  204 ? 2.3132 0.8341 1.9458 -0.2923 -0.0382 0.1940  204 PHE   O CE1 
26191 C  CE2 . PHE   O  204 ? 2.3225 0.9825 1.9429 -0.2850 -0.0206 0.2094  204 PHE   O CE2 
26192 C  CZ  . PHE   O  204 ? 2.3195 0.8445 1.9303 -0.2968 -0.0467 0.2526  204 PHE   O CZ  
26193 N  N   . ASN   O  205 ? 2.3262 1.0491 1.9371 -0.1735 -0.1902 0.1792  205 ASN   O N   
26194 C  CA  . ASN   O  205 ? 2.3087 1.0424 1.8615 -0.1466 -0.2052 0.2225  205 ASN   O CA  
26195 C  C   . ASN   O  205 ? 2.2640 0.9495 1.8132 -0.0653 -0.2536 0.2048  205 ASN   O C   
26196 O  O   . ASN   O  205 ? 2.2965 0.8663 1.7922 -0.0534 -0.2528 0.2615  205 ASN   O O   
26197 C  CB  . ASN   O  205 ? 2.3326 1.0800 1.8572 -0.1365 -0.2007 0.2312  205 ASN   O CB  
26198 C  CG  . ASN   O  205 ? 2.3491 1.0590 1.7627 -0.1435 -0.2063 0.2634  205 ASN   O CG  
26199 O  OD1 . ASN   O  205 ? 2.3506 0.9026 1.7619 -0.1542 -0.2867 0.1877  205 ASN   O OD1 
26200 N  ND2 . ASN   O  205 ? 2.4101 1.1572 1.7192 -0.1401 -0.1653 0.3109  205 ASN   O ND2 
26201 N  N   . GLY   O  206 ? 2.1530 1.0031 1.7624 -0.0647 -0.2659 0.1695  206 GLY   O N   
26202 C  CA  . GLY   O  206 ? 2.0665 0.9577 1.7538 -0.0552 -0.2681 0.0710  206 GLY   O CA  
26203 C  C   . GLY   O  206 ? 2.0487 1.0002 1.7065 -0.0107 -0.2767 0.0704  206 GLY   O C   
26204 O  O   . GLY   O  206 ? 1.9706 1.0375 1.7039 -0.0396 -0.2808 0.0509  206 GLY   O O   
26205 N  N   . ASP   O  207 ? 1.9972 1.0194 1.6849 -0.0421 -0.2747 0.0856  207 ASP   O N   
26206 C  CA  . ASP   O  207 ? 1.9768 1.0417 1.6921 -0.0861 -0.2357 0.0657  207 ASP   O CA  
26207 C  C   . ASP   O  207 ? 1.9213 1.0761 1.6942 -0.1250 -0.2499 0.0228  207 ASP   O C   
26208 O  O   . ASP   O  207 ? 1.9537 1.0179 1.6321 -0.1816 -0.2757 -0.0847 207 ASP   O O   
26209 C  CB  . ASP   O  207 ? 1.9780 1.0900 1.7145 -0.0931 -0.2068 0.1180  207 ASP   O CB  
26210 C  CG  . ASP   O  207 ? 1.9450 1.0753 1.7175 -0.0931 -0.1754 0.1612  207 ASP   O CG  
26211 O  OD1 . ASP   O  207 ? 1.8270 1.0825 1.7223 -0.1118 -0.1558 0.1520  207 ASP   O OD1 
26212 O  OD2 . ASP   O  207 ? 1.9679 1.1880 1.6763 -0.0341 -0.1218 0.1871  207 ASP   O OD2 
26213 N  N   . THR   O  208 ? 1.9369 1.0636 1.7199 -0.0960 -0.2431 -0.0004 208 THR   O N   
26214 C  CA  . THR   O  208 ? 1.9286 1.0278 1.7281 -0.0765 -0.2701 0.0013  208 THR   O CA  
26215 C  C   . THR   O  208 ? 1.9516 0.9227 1.7185 -0.0985 -0.2597 -0.0179 208 THR   O C   
26216 O  O   . THR   O  208 ? 1.8789 0.8111 1.7778 -0.0912 -0.2951 -0.0520 208 THR   O O   
26217 C  CB  . THR   O  208 ? 1.8954 1.0379 1.7645 -0.0816 -0.2593 -0.0046 208 THR   O CB  
26218 O  OG1 . THR   O  208 ? 1.8850 1.1026 1.7183 -0.0444 -0.2894 0.0098  208 THR   O OG1 
26219 C  CG2 . THR   O  208 ? 1.9158 1.1095 1.7561 -0.0770 -0.2477 0.0000  208 THR   O CG2 
26220 N  N   . ILE   O  209 ? 2.0024 0.9140 1.7662 -0.0847 -0.2510 0.0291  209 ILE   O N   
26221 C  CA  . ILE   O  209 ? 2.1466 0.9027 1.7707 -0.0909 -0.2239 0.0699  209 ILE   O CA  
26222 C  C   . ILE   O  209 ? 2.0536 0.8991 1.7148 -0.0856 -0.2175 0.0979  209 ILE   O C   
26223 O  O   . ILE   O  209 ? 2.0965 0.8295 1.7822 -0.0697 -0.2134 0.0780  209 ILE   O O   
26224 C  CB  . ILE   O  209 ? 2.1655 0.9940 1.8045 -0.0908 -0.2241 0.0744  209 ILE   O CB  
26225 C  CG1 . ILE   O  209 ? 2.3374 1.0001 1.8784 -0.0777 -0.2008 0.0922  209 ILE   O CG1 
26226 C  CG2 . ILE   O  209 ? 2.1830 0.9513 1.8332 -0.0692 -0.2225 0.0905  209 ILE   O CG2 
26227 C  CD1 . ILE   O  209 ? 2.3694 1.1381 1.8871 -0.0287 -0.1875 0.0879  209 ILE   O CD1 
26228 N  N   . GLU   O  210 ? 1.9946 0.7501 1.7650 -0.1086 -0.2404 0.1337  210 GLU   O N   
26229 C  CA  . GLU   O  210 ? 1.9867 0.7376 1.8157 -0.1102 -0.2213 0.1184  210 GLU   O CA  
26230 C  C   . GLU   O  210 ? 1.9011 0.6513 1.8963 -0.1081 -0.2314 0.1585  210 GLU   O C   
26231 O  O   . GLU   O  210 ? 1.8737 0.6375 1.9416 -0.1505 -0.2183 0.1339  210 GLU   O O   
26232 C  CB  . GLU   O  210 ? 1.9997 0.6844 1.8095 -0.1102 -0.2240 0.1398  210 GLU   O CB  
26233 C  CG  . GLU   O  210 ? 2.1198 0.6429 1.8335 -0.0836 -0.1831 0.1801  210 GLU   O CG  
26234 C  CD  . GLU   O  210 ? 2.1457 0.5199 1.8870 -0.1059 -0.1356 0.2155  210 GLU   O CD  
26235 O  OE1 . GLU   O  210 ? 2.2339 0.4417 1.9840 -0.1667 -0.1309 0.1153  210 GLU   O OE1 
26236 O  OE2 . GLU   O  210 ? 2.2362 0.6498 1.9454 0.0211  -0.1020 0.2376  210 GLU   O OE2 
26237 N  N   . LEU   O  211 ? 1.8842 0.6706 1.8917 -0.1028 -0.2227 0.1429  211 LEU   O N   
26238 C  CA  . LEU   O  211 ? 1.8509 0.6183 1.9030 -0.1011 -0.2264 0.1100  211 LEU   O CA  
26239 C  C   . LEU   O  211 ? 1.8364 0.6286 1.8247 -0.0663 -0.2337 0.1034  211 LEU   O C   
26240 O  O   . LEU   O  211 ? 1.8472 0.4306 1.7750 -0.0897 -0.2513 0.1724  211 LEU   O O   
26241 C  CB  . LEU   O  211 ? 1.8389 0.5825 1.9364 -0.1028 -0.2523 0.0512  211 LEU   O CB  
26242 C  CG  . LEU   O  211 ? 1.8364 0.5746 1.9554 -0.0774 -0.2682 0.0362  211 LEU   O CG  
26243 C  CD1 . LEU   O  211 ? 1.8583 0.6301 1.9901 -0.1209 -0.2693 0.0517  211 LEU   O CD1 
26244 C  CD2 . LEU   O  211 ? 1.8266 0.5411 1.9221 -0.1035 -0.2842 0.0592  211 LEU   O CD2 
26245 N  N   . ALA   O  212 ? 1.8403 0.6760 1.8181 -0.0922 -0.2670 0.1066  212 ALA   O N   
26246 C  CA  . ALA   O  212 ? 1.8393 0.6385 1.8343 -0.1838 -0.2569 0.0732  212 ALA   O CA  
26247 C  C   . ALA   O  212 ? 1.8718 0.6459 1.8357 -0.1860 -0.2626 0.0937  212 ALA   O C   
26248 O  O   . ALA   O  212 ? 1.9451 0.7328 1.8665 -0.2825 -0.2195 0.0367  212 ALA   O O   
26249 C  CB  . ALA   O  212 ? 1.7973 0.7746 1.8211 -0.1872 -0.2520 0.0714  212 ALA   O CB  
26250 N  N   . ILE   O  213 ? 1.8425 0.7172 1.7424 -0.1372 -0.2976 0.1205  213 ILE   O N   
26251 C  CA  . ILE   O  213 ? 1.7885 0.7449 1.7255 -0.1307 -0.2906 0.0770  213 ILE   O CA  
26252 C  C   . ILE   O  213 ? 1.7868 0.7159 1.6431 -0.0887 -0.3209 0.0517  213 ILE   O C   
26253 O  O   . ILE   O  213 ? 1.7960 0.6395 1.7291 -0.0622 -0.2800 0.0029  213 ILE   O O   
26254 C  CB  . ILE   O  213 ? 1.7642 0.7391 1.7177 -0.1586 -0.3185 0.0970  213 ILE   O CB  
26255 C  CG1 . ILE   O  213 ? 1.7547 0.7633 1.7241 -0.1011 -0.2851 0.1069  213 ILE   O CG1 
26256 C  CG2 . ILE   O  213 ? 1.7684 0.7498 1.7288 -0.1596 -0.3196 0.1082  213 ILE   O CG2 
26257 C  CD1 . ILE   O  213 ? 1.7592 0.8397 1.7520 -0.0804 -0.2936 0.1208  213 ILE   O CD1 
26258 N  N   . ILE   O  214 ? 1.7546 0.7012 1.6447 -0.0615 -0.3105 0.0800  214 ILE   O N   
26259 C  CA  . ILE   O  214 ? 1.7171 0.6916 1.6449 -0.0957 -0.2813 0.0859  214 ILE   O CA  
26260 C  C   . ILE   O  214 ? 1.7355 0.7779 1.6912 -0.1208 -0.3209 0.1420  214 ILE   O C   
26261 O  O   . ILE   O  214 ? 1.8586 0.8270 1.6480 -0.0910 -0.3579 0.1259  214 ILE   O O   
26262 C  CB  . ILE   O  214 ? 1.6705 0.5990 1.6441 -0.1083 -0.2893 0.1123  214 ILE   O CB  
26263 C  CG1 . ILE   O  214 ? 1.6554 0.5890 1.5876 -0.1476 -0.3133 0.0916  214 ILE   O CG1 
26264 C  CG2 . ILE   O  214 ? 1.6414 0.5872 1.6580 -0.0926 -0.2687 0.1057  214 ILE   O CG2 
26265 C  CD1 . ILE   O  214 ? 1.6694 0.5545 1.5775 -0.1391 -0.3070 0.0854  214 ILE   O CD1 
26266 N  N   . GLY   O  215 ? 1.6964 0.7901 1.7092 -0.1359 -0.3023 0.1441  215 GLY   O N   
26267 C  CA  . GLY   O  215 ? 1.6855 0.8597 1.7557 -0.1226 -0.2742 0.1442  215 GLY   O CA  
26268 C  C   . GLY   O  215 ? 1.6552 0.8533 1.7934 -0.1500 -0.2701 0.1491  215 GLY   O C   
26269 O  O   . GLY   O  215 ? 1.5839 0.8631 1.7051 -0.0986 -0.2370 0.1035  215 GLY   O O   
26270 N  N   . ASP   O  216 ? 1.6217 0.9697 1.8350 -0.1938 -0.2442 0.1831  216 ASP   O N   
26271 C  CA  . ASP   O  216 ? 1.5741 0.9506 1.8966 -0.2170 -0.3009 0.2381  216 ASP   O CA  
26272 C  C   . ASP   O  216 ? 1.5765 1.0660 1.8704 -0.2208 -0.3461 0.2297  216 ASP   O C   
26273 O  O   . ASP   O  216 ? 1.6240 0.9894 1.8289 -0.2691 -0.3511 0.2805  216 ASP   O O   
26274 C  CB  . ASP   O  216 ? 1.5570 0.9512 1.9404 -0.2425 -0.2929 0.2873  216 ASP   O CB  
26275 C  CG  . ASP   O  216 ? 1.4992 0.9598 1.9724 -0.2804 -0.2524 0.3214  216 ASP   O CG  
26276 O  OD1 . ASP   O  216 ? 1.4684 0.9634 1.9468 -0.3265 -0.3504 0.3126  216 ASP   O OD1 
26277 O  OD2 . ASP   O  216 ? 1.4907 0.9118 2.0309 -0.3439 -0.2527 0.3762  216 ASP   O OD2 
26278 N  N   . GLU   O  217 ? 1.5917 1.0604 1.8976 -0.2598 -0.3302 0.1846  217 GLU   O N   
26279 C  CA  . GLU   O  217 ? 1.6207 1.0991 1.8550 -0.2355 -0.3220 0.1286  217 GLU   O CA  
26280 C  C   . GLU   O  217 ? 1.6450 1.0384 1.8665 -0.2247 -0.2904 0.1159  217 GLU   O C   
26281 O  O   . GLU   O  217 ? 1.6652 1.0220 1.9181 -0.2856 -0.2552 0.0933  217 GLU   O O   
26282 C  CB  . GLU   O  217 ? 1.6186 1.1618 1.8392 -0.1842 -0.3514 0.1705  217 GLU   O CB  
26283 C  CG  . GLU   O  217 ? 1.5727 1.2882 1.8205 -0.2255 -0.3823 0.1558  217 GLU   O CG  
26284 C  CD  . GLU   O  217 ? 1.5250 1.3755 1.7695 -0.3086 -0.4057 0.2315  217 GLU   O CD  
26285 O  OE1 . GLU   O  217 ? 1.3896 1.4588 1.8250 -0.3671 -0.4382 0.2059  217 GLU   O OE1 
26286 O  OE2 . GLU   O  217 ? 1.5092 1.6290 1.7908 -0.3066 -0.4751 0.1768  217 GLU   O OE2 
26287 N  N   . ASN   O  218 ? 1.6783 0.9895 1.8440 -0.2020 -0.3016 0.0831  218 ASN   O N   
26288 C  CA  . ASN   O  218 ? 1.7160 0.9150 1.8454 -0.2081 -0.2994 0.0387  218 ASN   O CA  
26289 C  C   . ASN   O  218 ? 1.7272 0.8352 1.8955 -0.1301 -0.2894 0.0689  218 ASN   O C   
26290 O  O   . ASN   O  218 ? 1.7183 0.5986 1.9599 -0.1358 -0.2672 0.1091  218 ASN   O O   
26291 C  CB  . ASN   O  218 ? 1.7287 0.8339 1.8184 -0.2428 -0.2934 0.0041  218 ASN   O CB  
26292 C  CG  . ASN   O  218 ? 1.7689 0.8177 1.8121 -0.2440 -0.2597 0.0078  218 ASN   O CG  
26293 O  OD1 . ASN   O  218 ? 1.7803 0.8538 1.7960 -0.2503 -0.2162 -0.0183 218 ASN   O OD1 
26294 N  ND2 . ASN   O  218 ? 1.7912 0.7866 1.8214 -0.2501 -0.2629 -0.0073 218 ASN   O ND2 
26295 N  N   . PRO   O  219 ? 1.6910 0.8724 1.8758 -0.1266 -0.3252 0.0426  219 PRO   O N   
26296 C  CA  . PRO   O  219 ? 1.6982 0.8688 1.8632 -0.1236 -0.3171 0.0385  219 PRO   O CA  
26297 C  C   . PRO   O  219 ? 1.7100 0.7438 1.8497 -0.1201 -0.3083 0.0012  219 PRO   O C   
26298 O  O   . PRO   O  219 ? 1.7207 0.6303 1.8535 -0.0461 -0.2867 -0.0781 219 PRO   O O   
26299 C  CB  . PRO   O  219 ? 1.6770 0.9163 1.8690 -0.1340 -0.2996 0.0415  219 PRO   O CB  
26300 C  CG  . PRO   O  219 ? 1.6776 0.9671 1.8564 -0.1341 -0.3159 0.0513  219 PRO   O CG  
26301 C  CD  . PRO   O  219 ? 1.6864 0.9703 1.8572 -0.1215 -0.3175 0.0463  219 PRO   O CD  
26302 N  N   . ASP   O  220 ? 1.7099 0.7860 1.8356 -0.1300 -0.3397 0.0366  220 ASP   O N   
26303 C  CA  . ASP   O  220 ? 1.7582 0.8755 1.8364 -0.1345 -0.3402 0.0658  220 ASP   O CA  
26304 C  C   . ASP   O  220 ? 1.7380 0.8802 1.8320 -0.1824 -0.2908 0.0819  220 ASP   O C   
26305 O  O   . ASP   O  220 ? 1.8321 1.1318 1.8575 -0.2558 -0.3358 0.0940  220 ASP   O O   
26306 C  CB  . ASP   O  220 ? 1.7285 0.9357 1.8173 -0.1115 -0.3083 0.0777  220 ASP   O CB  
26307 C  CG  . ASP   O  220 ? 1.7619 0.8938 1.8569 -0.0073 -0.3027 0.1187  220 ASP   O CG  
26308 O  OD1 . ASP   O  220 ? 1.7812 1.0756 1.8611 0.0315  -0.2719 0.0562  220 ASP   O OD1 
26309 O  OD2 . ASP   O  220 ? 1.7818 0.8239 1.8830 0.0700  -0.2585 0.0779  220 ASP   O OD2 
26310 N  N   . LEU   O  221 ? 1.7049 0.7205 1.8246 -0.2095 -0.3074 0.0991  221 LEU   O N   
26311 C  CA  . LEU   O  221 ? 1.6946 0.6958 1.8138 -0.2228 -0.2870 0.1803  221 LEU   O CA  
26312 C  C   . LEU   O  221 ? 1.7298 0.6366 1.8080 -0.1840 -0.2966 0.2217  221 LEU   O C   
26313 O  O   . LEU   O  221 ? 1.7178 0.5383 1.7721 -0.2143 -0.3013 0.3336  221 LEU   O O   
26314 C  CB  . LEU   O  221 ? 1.6687 0.7138 1.8178 -0.2081 -0.2826 0.1832  221 LEU   O CB  
26315 C  CG  . LEU   O  221 ? 1.6573 0.7064 1.8444 -0.1830 -0.2786 0.2121  221 LEU   O CG  
26316 C  CD1 . LEU   O  221 ? 1.6585 0.6425 1.8769 -0.1894 -0.2798 0.2283  221 LEU   O CD1 
26317 C  CD2 . LEU   O  221 ? 1.6305 0.7413 1.8322 -0.2038 -0.2645 0.2193  221 LEU   O CD2 
26318 N  N   . LEU   O  222 ? 1.7329 0.6747 1.8353 -0.1548 -0.2847 0.2479  222 LEU   O N   
26319 C  CA  . LEU   O  222 ? 1.7395 0.5803 1.8186 -0.1242 -0.3204 0.2339  222 LEU   O CA  
26320 C  C   . LEU   O  222 ? 1.6765 0.5390 1.7971 -0.1391 -0.2954 0.2652  222 LEU   O C   
26321 O  O   . LEU   O  222 ? 1.6782 0.3877 1.7012 -0.1679 -0.3597 0.3381  222 LEU   O O   
26322 C  CB  . LEU   O  222 ? 1.7731 0.5345 1.8831 -0.0890 -0.2748 0.2515  222 LEU   O CB  
26323 C  CG  . LEU   O  222 ? 1.7976 0.5035 1.9347 -0.0951 -0.2443 0.2354  222 LEU   O CG  
26324 C  CD1 . LEU   O  222 ? 1.7826 0.4662 1.9503 -0.0580 -0.2592 0.2355  222 LEU   O CD1 
26325 C  CD2 . LEU   O  222 ? 1.8230 0.4916 1.9711 -0.0936 -0.2394 0.2628  222 LEU   O CD2 
26326 N  N   . GLY   O  223 ? 1.6735 0.5753 1.7927 -0.1234 -0.3123 0.2396  223 GLY   O N   
26327 C  CA  . GLY   O  223 ? 1.6436 0.5751 1.7446 -0.1138 -0.2839 0.2529  223 GLY   O CA  
26328 C  C   . GLY   O  223 ? 1.6272 0.5637 1.7102 -0.1550 -0.2616 0.2580  223 GLY   O C   
26329 O  O   . GLY   O  223 ? 1.5767 0.4519 1.6158 -0.1321 -0.2513 0.3472  223 GLY   O O   
26330 N  N   . TYR   O  224 ? 1.6148 0.6340 1.7335 -0.1433 -0.2787 0.2425  224 TYR   O N   
26331 C  CA  . TYR   O  224 ? 1.6399 0.6332 1.7417 -0.1388 -0.2702 0.1692  224 TYR   O CA  
26332 C  C   . TYR   O  224 ? 1.6356 0.6749 1.7382 -0.1182 -0.2723 0.1585  224 TYR   O C   
26333 O  O   . TYR   O  224 ? 1.6276 0.8183 1.6191 -0.0902 -0.3517 0.1601  224 TYR   O O   
26334 C  CB  . TYR   O  224 ? 1.7171 0.5926 1.7247 -0.1570 -0.2359 0.1686  224 TYR   O CB  
26335 C  CG  . TYR   O  224 ? 1.7577 0.5627 1.7084 -0.1938 -0.2464 0.1761  224 TYR   O CG  
26336 C  CD1 . TYR   O  224 ? 1.7475 0.6680 1.6813 -0.1398 -0.2452 0.1645  224 TYR   O CD1 
26337 C  CD2 . TYR   O  224 ? 1.7716 0.5118 1.6743 -0.2288 -0.2315 0.1699  224 TYR   O CD2 
26338 C  CE1 . TYR   O  224 ? 1.7362 0.7596 1.6511 -0.1668 -0.2333 0.2262  224 TYR   O CE1 
26339 C  CE2 . TYR   O  224 ? 1.7758 0.5922 1.6590 -0.2557 -0.2174 0.2022  224 TYR   O CE2 
26340 C  CZ  . TYR   O  224 ? 1.7115 0.7047 1.6504 -0.2062 -0.2088 0.2382  224 TYR   O CZ  
26341 O  OH  . TYR   O  224 ? 1.6461 0.9092 1.6368 -0.3116 -0.1698 0.2592  224 TYR   O OH  
26342 N  N   . THR   O  225 ? 1.5849 0.6712 1.7078 -0.1258 -0.2916 0.1591  225 THR   O N   
26343 C  CA  . THR   O  225 ? 1.5779 0.7139 1.6907 -0.0935 -0.2656 0.1680  225 THR   O CA  
26344 C  C   . THR   O  225 ? 1.5787 0.7402 1.7031 -0.1053 -0.2755 0.1981  225 THR   O C   
26345 O  O   . THR   O  225 ? 1.5717 0.7031 1.6619 -0.1140 -0.2899 0.2746  225 THR   O O   
26346 C  CB  . THR   O  225 ? 1.5679 0.7441 1.7136 -0.0727 -0.2562 0.1809  225 THR   O CB  
26347 O  OG1 . THR   O  225 ? 1.5449 0.7364 1.6876 -0.0603 -0.2336 0.2025  225 THR   O OG1 
26348 C  CG2 . THR   O  225 ? 1.5386 0.7565 1.6753 -0.1056 -0.2419 0.1555  225 THR   O CG2 
26349 N  N   . GLY   O  226 ? 1.5944 0.8149 1.7103 -0.0669 -0.2836 0.1790  226 GLY   O N   
26350 C  CA  . GLY   O  226 ? 1.6354 0.7980 1.7613 -0.0285 -0.2779 0.1605  226 GLY   O CA  
26351 C  C   . GLY   O  226 ? 1.6579 0.8958 1.7472 -0.0113 -0.2923 0.1147  226 GLY   O C   
26352 O  O   . GLY   O  226 ? 1.6630 1.0521 1.6883 0.0888  -0.3105 0.1830  226 GLY   O O   
26353 N  N   . ILE   O  227 ? 1.6673 0.8322 1.7459 -0.0631 -0.3102 0.1127  227 ILE   O N   
26354 C  CA  . ILE   O  227 ? 1.7048 0.8686 1.7459 -0.0844 -0.3110 0.1329  227 ILE   O CA  
26355 C  C   . ILE   O  227 ? 1.7068 0.9505 1.8269 -0.1024 -0.3132 0.0790  227 ILE   O C   
26356 O  O   . ILE   O  227 ? 1.7991 0.9567 1.8139 -0.0271 -0.2983 0.0321  227 ILE   O O   
26357 C  CB  . ILE   O  227 ? 1.6776 0.8549 1.7062 -0.1276 -0.3351 0.1455  227 ILE   O CB  
26358 C  CG1 . ILE   O  227 ? 1.7435 0.8195 1.6768 -0.1500 -0.3246 0.1487  227 ILE   O CG1 
26359 C  CG2 . ILE   O  227 ? 1.6808 0.8566 1.7044 -0.1210 -0.3418 0.1577  227 ILE   O CG2 
26360 C  CD1 . ILE   O  227 ? 1.7198 0.8048 1.6397 -0.1933 -0.3265 0.1405  227 ILE   O CD1 
26361 N  N   . PRO   O  228 ? 1.6626 0.9531 1.9508 -0.0736 -0.3130 0.0561  228 PRO   O N   
26362 C  CA  . PRO   O  228 ? 1.5984 1.0677 2.0073 -0.0709 -0.3298 0.0401  228 PRO   O CA  
26363 C  C   . PRO   O  228 ? 1.5868 1.2127 2.0169 -0.0549 -0.3411 -0.0359 228 PRO   O C   
26364 O  O   . PRO   O  228 ? 1.4528 1.2398 2.0422 -0.0410 -0.3908 -0.1434 228 PRO   O O   
26365 C  CB  . PRO   O  228 ? 1.6231 1.0086 2.0240 -0.0809 -0.3231 0.0479  228 PRO   O CB  
26366 C  CG  . PRO   O  228 ? 1.6498 1.0214 2.0354 -0.0701 -0.3097 0.0216  228 PRO   O CG  
26367 C  CD  . PRO   O  228 ? 1.6509 0.9444 2.0130 -0.0647 -0.3066 0.0231  228 PRO   O CD  
26368 N  N   . THR   O  229 ? 1.6378 1.2745 2.0136 -0.0956 -0.3378 0.0166  229 THR   O N   
26369 C  CA  . THR   O  229 ? 1.6316 1.2986 1.9489 -0.1096 -0.3398 0.0427  229 THR   O CA  
26370 C  C   . THR   O  229 ? 1.6593 1.2897 2.0249 -0.0689 -0.3397 0.0178  229 THR   O C   
26371 O  O   . THR   O  229 ? 1.6740 1.3758 2.0272 0.0028  -0.3283 -0.0529 229 THR   O O   
26372 C  CB  . THR   O  229 ? 1.6439 1.3502 1.8915 -0.1224 -0.3451 0.0384  229 THR   O CB  
26373 O  OG1 . THR   O  229 ? 1.6015 1.3406 1.9031 -0.1559 -0.3003 0.0694  229 THR   O OG1 
26374 C  CG2 . THR   O  229 ? 1.6414 1.3294 1.8712 -0.1369 -0.3338 0.0373  229 THR   O CG2 
26375 N  N   . ASP   O  230 ? 1.6485 1.3021 2.0339 -0.0285 -0.3737 0.1168  230 ASP   O N   
26376 C  CA  . ASP   O  230 ? 1.6818 1.3000 2.0579 -0.0464 -0.3157 0.1907  230 ASP   O CA  
26377 C  C   . ASP   O  230 ? 1.6790 1.2390 2.0483 -0.1073 -0.3540 0.1536  230 ASP   O C   
26378 O  O   . ASP   O  230 ? 1.6275 1.1353 2.0186 -0.2184 -0.3387 0.1611  230 ASP   O O   
26379 C  CB  . ASP   O  230 ? 1.6339 1.3258 2.0296 0.0028  -0.3406 0.2757  230 ASP   O CB  
26380 C  CG  . ASP   O  230 ? 1.6176 1.3420 2.0219 0.0642  -0.3242 0.3322  230 ASP   O CG  
26381 O  OD1 . ASP   O  230 ? 1.7101 1.4176 1.9957 0.0940  -0.1573 0.3982  230 ASP   O OD1 
26382 O  OD2 . ASP   O  230 ? 1.4910 1.2809 1.9453 0.1995  -0.3485 0.4615  230 ASP   O OD2 
26383 N  N   . LYS   O  231 ? 1.7349 1.2322 2.0342 -0.1150 -0.3532 0.1769  231 LYS   O N   
26384 C  CA  . LYS   O  231 ? 1.6961 1.1809 1.9825 -0.0760 -0.3780 0.1540  231 LYS   O CA  
26385 C  C   . LYS   O  231 ? 1.7377 1.0266 1.9948 -0.0779 -0.3372 0.0551  231 LYS   O C   
26386 O  O   . LYS   O  231 ? 1.6458 0.8879 1.9987 -0.1111 -0.3868 -0.0627 231 LYS   O O   
26387 C  CB  . LYS   O  231 ? 1.7307 1.3233 1.9640 -0.0954 -0.3929 0.1398  231 LYS   O CB  
26388 C  CG  . LYS   O  231 ? 1.6457 1.5206 1.9648 -0.0650 -0.4322 0.1379  231 LYS   O CG  
26389 C  CD  . LYS   O  231 ? 1.6356 1.6573 2.0043 -0.0616 -0.4584 0.1266  231 LYS   O CD  
26390 C  CE  . LYS   O  231 ? 1.5907 1.7038 2.0109 -0.0622 -0.4570 0.1216  231 LYS   O CE  
26391 N  NZ  . LYS   O  231 ? 1.5687 1.7664 2.0125 -0.0329 -0.4593 0.1240  231 LYS   O NZ  
26392 N  N   . GLY   O  232 ? 1.7948 0.8609 1.9334 0.0398  -0.3911 0.0567  232 GLY   O N   
26393 C  CA  . GLY   O  232 ? 1.8409 0.8526 1.8880 0.0028  -0.3679 0.0861  232 GLY   O CA  
26394 C  C   . GLY   O  232 ? 1.8418 0.7485 1.8889 -0.0075 -0.3672 0.1579  232 GLY   O C   
26395 O  O   . GLY   O  232 ? 1.8278 0.6490 1.9077 -0.0367 -0.3870 0.1776  232 GLY   O O   
26396 N  N   . PRO   O  233 ? 1.8417 0.6874 1.8172 -0.0527 -0.3404 0.1753  233 PRO   O N   
26397 C  CA  . PRO   O  233 ? 1.8312 0.7062 1.7698 -0.0590 -0.3607 0.1614  233 PRO   O CA  
26398 C  C   . PRO   O  233 ? 1.8224 0.7223 1.7420 -0.0365 -0.4114 0.1339  233 PRO   O C   
26399 O  O   . PRO   O  233 ? 1.8053 0.7688 1.7133 -0.0220 -0.4156 0.0746  233 PRO   O O   
26400 C  CB  . PRO   O  233 ? 1.8280 0.6796 1.7592 -0.0569 -0.3342 0.1823  233 PRO   O CB  
26401 C  CG  . PRO   O  233 ? 1.8499 0.7007 1.7661 -0.0540 -0.3127 0.1909  233 PRO   O CG  
26402 C  CD  . PRO   O  233 ? 1.8477 0.6800 1.7969 -0.0673 -0.3124 0.1814  233 PRO   O CD  
26403 N  N   . ARG   O  234 ? 1.7950 0.6683 1.7380 -0.0602 -0.4540 0.1437  234 ARG   O N   
26404 C  CA  . ARG   O  234 ? 1.8144 0.7191 1.7459 -0.0973 -0.4488 0.1156  234 ARG   O CA  
26405 C  C   . ARG   O  234 ? 1.8195 0.6858 1.7796 -0.1304 -0.4325 0.1173  234 ARG   O C   
26406 O  O   . ARG   O  234 ? 1.8615 0.7452 1.7757 -0.1748 -0.3997 0.1517  234 ARG   O O   
26407 C  CB  . ARG   O  234 ? 1.7991 0.6657 1.7479 -0.0893 -0.4766 0.0791  234 ARG   O CB  
26408 C  CG  . ARG   O  234 ? 1.7732 0.7178 1.7452 -0.0731 -0.5119 0.0651  234 ARG   O CG  
26409 C  CD  . ARG   O  234 ? 1.7508 0.7462 1.7457 -0.0714 -0.5495 0.0213  234 ARG   O CD  
26410 N  NE  . ARG   O  234 ? 1.7097 0.8263 1.7309 -0.0690 -0.5920 0.0216  234 ARG   O NE  
26411 C  CZ  . ARG   O  234 ? 1.7011 0.7377 1.7157 -0.0437 -0.6085 0.0370  234 ARG   O CZ  
26412 N  NH1 . ARG   O  234 ? 1.6579 0.7991 1.7396 -0.1011 -0.5949 0.0181  234 ARG   O NH1 
26413 N  NH2 . ARG   O  234 ? 1.7086 0.7520 1.7334 -0.0088 -0.6088 0.0177  234 ARG   O NH2 
26414 N  N   . PHE   O  235 ? 1.8150 0.6674 1.7883 -0.1859 -0.4099 0.0848  235 PHE   O N   
26415 C  CA  . PHE   O  235 ? 1.8729 0.6086 1.7252 -0.2221 -0.3668 0.1046  235 PHE   O CA  
26416 C  C   . PHE   O  235 ? 1.8889 0.5935 1.7128 -0.2468 -0.3713 0.0951  235 PHE   O C   
26417 O  O   . PHE   O  235 ? 1.9112 0.5933 1.5959 -0.3393 -0.3223 0.1448  235 PHE   O O   
26418 C  CB  . PHE   O  235 ? 1.8727 0.5713 1.7242 -0.2202 -0.3705 0.0955  235 PHE   O CB  
26419 C  CG  . PHE   O  235 ? 1.9212 0.5949 1.6912 -0.2338 -0.3911 0.1128  235 PHE   O CG  
26420 C  CD1 . PHE   O  235 ? 1.9408 0.5764 1.6904 -0.2676 -0.3687 0.0578  235 PHE   O CD1 
26421 C  CD2 . PHE   O  235 ? 1.9846 0.6098 1.7039 -0.2233 -0.3837 0.1015  235 PHE   O CD2 
26422 C  CE1 . PHE   O  235 ? 1.9638 0.5942 1.6739 -0.2639 -0.3655 0.0663  235 PHE   O CE1 
26423 C  CE2 . PHE   O  235 ? 2.0253 0.5222 1.7015 -0.2515 -0.3797 0.0865  235 PHE   O CE2 
26424 C  CZ  . PHE   O  235 ? 1.9940 0.5445 1.7051 -0.2711 -0.3876 0.0830  235 PHE   O CZ  
26425 N  N   . ARG   O  236 ? 1.9018 0.6002 1.6876 -0.2469 -0.3789 0.0990  236 ARG   O N   
26426 C  CA  . ARG   O  236 ? 1.9359 0.6070 1.6645 -0.2340 -0.3898 0.0499  236 ARG   O CA  
26427 C  C   . ARG   O  236 ? 1.9798 0.5965 1.6458 -0.2598 -0.4271 0.0457  236 ARG   O C   
26428 O  O   . ARG   O  236 ? 1.9787 0.4771 1.7309 -0.2628 -0.4480 0.0867  236 ARG   O O   
26429 C  CB  . ARG   O  236 ? 1.9503 0.5835 1.7123 -0.2390 -0.3487 0.0296  236 ARG   O CB  
26430 C  CG  . ARG   O  236 ? 1.9642 0.6225 1.7302 -0.2424 -0.2997 0.0286  236 ARG   O CG  
26431 C  CD  . ARG   O  236 ? 2.0136 0.7418 1.8237 -0.2127 -0.2214 0.0100  236 ARG   O CD  
26432 N  NE  . ARG   O  236 ? 2.1127 0.8467 1.9424 -0.2613 -0.2094 -0.1232 236 ARG   O NE  
26433 C  CZ  . ARG   O  236 ? 2.1813 1.0791 1.9894 -0.1172 -0.0517 -0.1330 236 ARG   O CZ  
26434 N  NH1 . ARG   O  236 ? 2.1999 1.1516 1.9835 -0.1006 -0.0593 -0.1560 236 ARG   O NH1 
26435 N  NH2 . ARG   O  236 ? 2.2334 1.0794 2.0841 -0.1449 -0.0204 -0.1408 236 ARG   O NH2 
26436 N  N   . LYS   O  237 ? 2.0326 0.6552 1.6163 -0.2336 -0.4183 0.0452  237 LYS   O N   
26437 C  CA  . LYS   O  237 ? 2.0332 0.6472 1.6072 -0.2161 -0.3952 0.0364  237 LYS   O CA  
26438 C  C   . LYS   O  237 ? 2.0366 0.6601 1.5934 -0.2326 -0.4136 0.0737  237 LYS   O C   
26439 O  O   . LYS   O  237 ? 2.0833 0.5974 1.5881 -0.2169 -0.3601 0.1337  237 LYS   O O   
26440 C  CB  . LYS   O  237 ? 1.9940 0.6834 1.6603 -0.1423 -0.3808 0.0625  237 LYS   O CB  
26441 C  CG  . LYS   O  237 ? 2.0121 0.7357 1.7116 -0.0967 -0.3441 0.0533  237 LYS   O CG  
26442 C  CD  . LYS   O  237 ? 1.9961 0.7936 1.7610 -0.0831 -0.3147 0.0636  237 LYS   O CD  
26443 C  CE  . LYS   O  237 ? 1.9925 0.8878 1.8018 -0.0377 -0.2756 0.0414  237 LYS   O CE  
26444 N  NZ  . LYS   O  237 ? 2.0246 0.9814 1.8065 -0.0375 -0.2673 0.0705  237 LYS   O NZ  
26445 N  N   . LEU   O  238 ? 1.9931 0.6444 1.6164 -0.2278 -0.3761 0.1177  238 LEU   O N   
26446 C  CA  . LEU   O  238 ? 2.0049 0.6141 1.7035 -0.2002 -0.3293 0.1354  238 LEU   O CA  
26447 C  C   . LEU   O  238 ? 1.9578 0.5936 1.7079 -0.2039 -0.3030 0.1491  238 LEU   O C   
26448 O  O   . LEU   O  238 ? 1.9447 0.6641 1.7782 -0.1956 -0.3044 0.1433  238 LEU   O O   
26449 C  CB  . LEU   O  238 ? 2.0354 0.5822 1.6899 -0.1819 -0.3511 0.1497  238 LEU   O CB  
26450 C  CG  . LEU   O  238 ? 2.0708 0.6026 1.7022 -0.1530 -0.3680 0.1429  238 LEU   O CG  
26451 C  CD1 . LEU   O  238 ? 2.0690 0.6138 1.7054 -0.1555 -0.3397 0.1914  238 LEU   O CD1 
26452 C  CD2 . LEU   O  238 ? 2.0416 0.6075 1.7544 -0.1501 -0.3787 0.1053  238 LEU   O CD2 
26453 N  N   . THR   O  239 ? 1.9509 0.6244 1.8082 -0.2431 -0.2132 0.1349  239 THR   O N   
26454 C  CA  . THR   O  239 ? 1.9402 0.7148 1.7975 -0.2493 -0.1930 0.1369  239 THR   O CA  
26455 C  C   . THR   O  239 ? 1.9342 0.7194 1.8127 -0.2401 -0.1700 0.1496  239 THR   O C   
26456 O  O   . THR   O  239 ? 1.9252 0.5950 1.8813 -0.2437 -0.1816 0.1891  239 THR   O O   
26457 C  CB  . THR   O  239 ? 1.9727 0.7424 1.8138 -0.2693 -0.1720 0.1126  239 THR   O CB  
26458 O  OG1 . THR   O  239 ? 1.9681 0.7640 1.8629 -0.2445 -0.1324 0.1591  239 THR   O OG1 
26459 C  CG2 . THR   O  239 ? 1.9426 0.7382 1.8027 -0.2677 -0.1676 0.0755  239 THR   O CG2 
26460 N  N   . SER   O  240 ? 1.9235 0.7593 1.7842 -0.2277 -0.1406 0.1596  240 SER   O N   
26461 C  CA  . SER   O  240 ? 1.9609 0.7690 1.7985 -0.2733 -0.1227 0.1564  240 SER   O CA  
26462 C  C   . SER   O  240 ? 1.9701 0.8992 1.8395 -0.2421 -0.0830 0.1688  240 SER   O C   
26463 O  O   . SER   O  240 ? 2.0152 1.0047 1.9065 -0.3116 -0.1309 0.1001  240 SER   O O   
26464 C  CB  . SER   O  240 ? 1.8937 0.8619 1.7879 -0.2902 -0.1087 0.1128  240 SER   O CB  
26465 O  OG  . SER   O  240 ? 1.8880 0.8934 1.7637 -0.2616 -0.1091 0.1505  240 SER   O OG  
26466 N  N   . GLN   O  241 ? 1.9983 0.7509 1.8451 -0.2866 -0.0925 0.2123  241 GLN   O N   
26467 C  CA  . GLN   O  241 ? 2.0129 0.8008 1.8560 -0.2918 -0.0667 0.2101  241 GLN   O CA  
26468 C  C   . GLN   O  241 ? 2.0838 0.8720 1.8486 -0.2527 -0.0923 0.2537  241 GLN   O C   
26469 O  O   . GLN   O  241 ? 2.0021 1.1204 1.8801 -0.2920 -0.0974 0.2716  241 GLN   O O   
26470 C  CB  . GLN   O  241 ? 1.9800 0.8126 1.8621 -0.3156 -0.0171 0.2071  241 GLN   O CB  
26471 C  CG  . GLN   O  241 ? 1.9940 0.8966 1.9001 -0.3293 0.0186  0.1786  241 GLN   O CG  
26472 C  CD  . GLN   O  241 ? 1.9977 0.9535 1.9280 -0.3393 0.0902  0.2087  241 GLN   O CD  
26473 O  OE1 . GLN   O  241 ? 1.9159 1.0775 1.9832 -0.3271 0.0538  0.1466  241 GLN   O OE1 
26474 N  NE2 . GLN   O  241 ? 1.9669 1.1100 1.9560 -0.3522 0.0906  0.1948  241 GLN   O NE2 
26475 N  N   . GLU   O  242 ? 2.0712 0.7925 1.8977 -0.2779 -0.1063 0.2543  242 GLU   O N   
26476 C  CA  . GLU   O  242 ? 2.0521 0.8647 1.9517 -0.2069 -0.1218 0.3087  242 GLU   O CA  
26477 C  C   . GLU   O  242 ? 2.0570 0.7955 1.9669 -0.1932 -0.1414 0.3678  242 GLU   O C   
26478 O  O   . GLU   O  242 ? 2.0231 0.7160 1.9516 -0.1458 -0.1677 0.4990  242 GLU   O O   
26479 C  CB  . GLU   O  242 ? 2.0257 0.7808 1.9295 -0.1368 -0.1185 0.2706  242 GLU   O CB  
26480 C  CG  . GLU   O  242 ? 1.9954 0.8567 1.9229 -0.0628 -0.0922 0.2549  242 GLU   O CG  
26481 C  CD  . GLU   O  242 ? 1.9664 0.8586 1.8754 -0.0183 -0.0658 0.2599  242 GLU   O CD  
26482 O  OE1 . GLU   O  242 ? 1.9758 0.9158 1.8019 -0.0106 -0.0863 0.3126  242 GLU   O OE1 
26483 O  OE2 . GLU   O  242 ? 1.9952 0.8308 1.8409 -0.0115 -0.0467 0.3130  242 GLU   O OE2 
26484 N  N   . ILE   O  243 ? 2.0771 0.8520 2.0053 -0.1581 -0.1405 0.3219  243 ILE   O N   
26485 C  CA  . ILE   O  243 ? 2.0642 0.9283 1.9846 -0.2153 -0.1498 0.2499  243 ILE   O CA  
26486 C  C   . ILE   O  243 ? 2.1343 0.9373 1.9468 -0.1874 -0.1466 0.3200  243 ILE   O C   
26487 O  O   . ILE   O  243 ? 2.1496 0.8167 1.9974 -0.1935 -0.1591 0.3879  243 ILE   O O   
26488 C  CB  . ILE   O  243 ? 2.0620 0.9849 1.9482 -0.2030 -0.1691 0.2195  243 ILE   O CB  
26489 C  CG1 . ILE   O  243 ? 2.0022 1.0098 1.8900 -0.1909 -0.1785 0.2137  243 ILE   O CG1 
26490 C  CG2 . ILE   O  243 ? 2.0766 0.9559 1.9637 -0.1794 -0.1737 0.2544  243 ILE   O CG2 
26491 C  CD1 . ILE   O  243 ? 1.9987 1.0370 1.8326 -0.1906 -0.1794 0.2066  243 ILE   O CD1 
26492 N  N   . ASN   O  244 ? 2.0606 0.8429 1.9388 -0.2525 -0.1488 0.3359  244 ASN   O N   
26493 C  CA  . ASN   O  244 ? 1.9937 0.9803 1.8839 -0.2841 -0.1159 0.3239  244 ASN   O CA  
26494 C  C   . ASN   O  244 ? 1.9882 1.0521 1.9637 -0.2384 -0.0755 0.3397  244 ASN   O C   
26495 O  O   . ASN   O  244 ? 1.8729 1.1048 2.0275 -0.2400 -0.0722 0.3010  244 ASN   O O   
26496 C  CB  . ASN   O  244 ? 2.0446 1.0181 1.8639 -0.3409 -0.1009 0.2901  244 ASN   O CB  
26497 C  CG  . ASN   O  244 ? 2.0339 1.0184 1.7373 -0.3897 -0.1611 0.2731  244 ASN   O CG  
26498 O  OD1 . ASN   O  244 ? 2.0215 1.0825 1.7390 -0.3546 -0.1917 0.2451  244 ASN   O OD1 
26499 N  ND2 . ASN   O  244 ? 2.0544 0.9675 1.6739 -0.4009 -0.1445 0.3140  244 ASN   O ND2 
26500 N  N   . ASP   O  245 ? 1.8833 1.0672 1.9699 -0.2381 -0.0296 0.3521  245 ASP   O N   
26501 C  CA  . ASP   O  245 ? 1.8637 1.1968 2.0258 -0.2499 -0.0009 0.3394  245 ASP   O CA  
26502 C  C   . ASP   O  245 ? 1.8229 1.2577 2.0832 -0.2489 -0.0423 0.3066  245 ASP   O C   
26503 O  O   . ASP   O  245 ? 1.7342 1.4128 2.1936 -0.1778 -0.0652 0.2231  245 ASP   O O   
26504 C  CB  . ASP   O  245 ? 1.8903 1.2102 2.0093 -0.2348 0.0406  0.3880  245 ASP   O CB  
26505 C  CG  . ASP   O  245 ? 1.9289 1.3306 1.8848 -0.1804 0.0656  0.4406  245 ASP   O CG  
26506 O  OD1 . ASP   O  245 ? 1.9299 1.3874 1.8673 -0.2000 0.0769  0.4480  245 ASP   O OD1 
26507 O  OD2 . ASP   O  245 ? 1.9616 1.2899 1.9320 -0.1081 0.0635  0.3088  245 ASP   O OD2 
26508 N  N   . ARG   O  246 ? 1.8132 1.2051 2.0038 -0.2692 -0.0970 0.3087  246 ARG   O N   
26509 C  CA  . ARG   O  246 ? 1.8693 1.1257 2.0494 -0.2571 -0.1709 0.3058  246 ARG   O CA  
26510 C  C   . ARG   O  246 ? 1.9446 1.1258 2.1055 -0.2372 -0.2051 0.3488  246 ARG   O C   
26511 O  O   . ARG   O  246 ? 2.0153 1.1457 2.1405 -0.2212 -0.2760 0.3736  246 ARG   O O   
26512 C  CB  . ARG   O  246 ? 1.8638 1.1094 2.0010 -0.2200 -0.1937 0.3069  246 ARG   O CB  
26513 C  CG  . ARG   O  246 ? 1.8740 1.1136 2.0103 -0.2032 -0.1881 0.3002  246 ARG   O CG  
26514 C  CD  . ARG   O  246 ? 1.8812 1.0471 1.9648 -0.1754 -0.2110 0.3170  246 ARG   O CD  
26515 N  NE  . ARG   O  246 ? 1.8550 1.0694 1.9135 -0.1767 -0.2064 0.3711  246 ARG   O NE  
26516 C  CZ  . ARG   O  246 ? 1.8333 1.0209 1.8939 -0.1075 -0.1970 0.4147  246 ARG   O CZ  
26517 N  NH1 . ARG   O  246 ? 1.8377 1.0486 1.8875 -0.1085 -0.1867 0.4026  246 ARG   O NH1 
26518 N  NH2 . ARG   O  246 ? 1.8054 1.0586 1.8867 -0.0751 -0.1923 0.4172  246 ARG   O NH2 
26519 N  N   . LEU   O  247 ? 1.9525 1.1060 2.1089 -0.2723 -0.2618 0.3009  247 LEU   O N   
26520 C  CA  . LEU   O  247 ? 2.0174 1.1058 2.1832 -0.2740 -0.2801 0.3072  247 LEU   O CA  
26521 C  C   . LEU   O  247 ? 2.0105 1.2034 2.2251 -0.2795 -0.2588 0.3190  247 LEU   O C   
26522 O  O   . LEU   O  247 ? 1.9829 1.2057 2.2945 -0.2070 -0.2671 0.3781  247 LEU   O O   
26523 C  CB  . LEU   O  247 ? 1.9986 0.9249 2.1658 -0.3215 -0.2630 0.3244  247 LEU   O CB  
26524 C  CG  . LEU   O  247 ? 2.0000 0.8069 2.1574 -0.3385 -0.2726 0.3307  247 LEU   O CG  
26525 C  CD1 . LEU   O  247 ? 1.9916 0.6915 2.1259 -0.3106 -0.2544 0.3394  247 LEU   O CD1 
26526 C  CD2 . LEU   O  247 ? 1.9819 0.7547 2.1438 -0.3404 -0.2624 0.3633  247 LEU   O CD2 
26527 N  N   . GLU   O  248 ? 2.0866 1.3485 2.2356 -0.2363 -0.2747 0.2060  248 GLU   O N   
26528 C  CA  . GLU   O  248 ? 2.1193 1.4304 2.2737 -0.2434 -0.2174 0.1683  248 GLU   O CA  
26529 C  C   . GLU   O  248 ? 2.1703 1.6218 2.3709 -0.2012 -0.3009 0.1718  248 GLU   O C   
26530 O  O   . GLU   O  248 ? 2.2250 1.6404 2.4536 -0.2132 -0.2948 0.2561  248 GLU   O O   
26531 C  CB  . GLU   O  248 ? 2.0990 1.4743 2.2615 -0.2432 -0.2519 0.1271  248 GLU   O CB  
26532 C  CG  . GLU   O  248 ? 2.1166 1.4601 2.2296 -0.2270 -0.2368 0.0886  248 GLU   O CG  
26533 C  CD  . GLU   O  248 ? 2.1077 1.4654 2.2085 -0.1869 -0.2426 0.0753  248 GLU   O CD  
26534 O  OE1 . GLU   O  248 ? 2.0374 1.4343 2.1417 -0.2360 -0.2464 0.1013  248 GLU   O OE1 
26535 O  OE2 . GLU   O  248 ? 2.1745 1.4306 2.1946 -0.2313 -0.2775 0.0034  248 GLU   O OE2 
26536 N  N   . ALA   O  249 ? 2.2323 1.5733 2.4430 -0.1855 -0.2770 0.1786  249 ALA   O N   
26537 C  CA  . ALA   O  249 ? 2.2809 1.5658 2.4654 -0.1867 -0.2988 0.1334  249 ALA   O CA  
26538 C  C   . ALA   O  249 ? 2.3354 1.5640 2.4594 -0.1629 -0.3217 0.0880  249 ALA   O C   
26539 O  O   . ALA   O  249 ? 2.3124 1.2851 2.5287 -0.2672 -0.3756 0.0612  249 ALA   O O   
26540 C  CB  . ALA   O  249 ? 2.2809 1.5073 2.4582 -0.2281 -0.2766 0.1355  249 ALA   O CB  
26541 N  N   . LEU   O  250 ? 2.3992 1.6059 2.4551 -0.0933 -0.2879 0.0361  250 LEU   O N   
26542 C  CA  . LEU   O  250 ? 2.4005 1.5915 2.4852 -0.0101 -0.2944 0.0689  250 LEU   O CA  
26543 C  C   . LEU   O  250 ? 2.4713 1.5040 2.5702 -0.0162 -0.2206 0.0908  250 LEU   O C   
26544 O  O   . LEU   O  250 ? 2.4108 1.5400 2.6301 -0.0152 -0.2036 0.1402  250 LEU   O O   
26545 C  CB  . LEU   O  250 ? 2.3996 1.5011 2.4071 0.0004  -0.2827 0.0212  250 LEU   O CB  
26546 C  CG  . LEU   O  250 ? 2.3667 1.4419 2.3399 0.0213  -0.3212 -0.0055 250 LEU   O CG  
26547 C  CD1 . LEU   O  250 ? 2.3405 1.4374 2.3274 0.0702  -0.3129 0.0022  250 LEU   O CD1 
26548 C  CD2 . LEU   O  250 ? 2.2840 1.4376 2.2934 -0.0193 -0.2938 -0.0395 250 LEU   O CD2 
26549 O  OXT . LEU   O  250 ? 2.5213 1.5126 2.6169 0.0057  -0.1578 0.1249  250 LEU   O OXT 
26550 N  N   . GLY   P  2   ? 2.0365 0.9086 1.7370 0.2715  -0.3392 0.0212  1   GLY   P N   
26551 C  CA  . GLY   P  2   ? 2.0443 0.8375 1.7169 0.2322  -0.3365 0.0655  1   GLY   P CA  
26552 C  C   . GLY   P  2   ? 2.0128 0.8992 1.7156 0.2620  -0.3486 0.1321  1   GLY   P C   
26553 O  O   . GLY   P  2   ? 2.0275 0.9897 1.7465 0.1709  -0.2906 0.1530  1   GLY   P O   
26554 N  N   . SER   P  3   ? 2.0177 0.7457 1.8129 0.2329  -0.3107 0.1525  2   SER   P N   
26555 C  CA  . SER   P  3   ? 2.0261 0.8278 1.8831 0.2093  -0.3166 0.1508  2   SER   P CA  
26556 C  C   . SER   P  3   ? 2.0263 0.7864 1.8923 0.3247  -0.3045 0.1592  2   SER   P C   
26557 O  O   . SER   P  3   ? 2.0287 0.8150 1.8842 0.3556  -0.3245 0.1653  2   SER   P O   
26558 C  CB  . SER   P  3   ? 2.0447 0.8551 1.9467 0.2259  -0.2604 0.0774  2   SER   P CB  
26559 O  OG  . SER   P  3   ? 2.0619 0.9636 2.0203 0.1697  -0.2059 0.0912  2   SER   P OG  
26560 N  N   . ARG   P  4   ? 1.9703 0.8706 1.8671 0.3289  -0.3613 0.1464  3   ARG   P N   
26561 C  CA  . ARG   P  4   ? 1.9811 1.0517 1.8735 0.2935  -0.3560 0.0918  3   ARG   P CA  
26562 C  C   . ARG   P  4   ? 1.9890 1.0410 1.8353 0.2844  -0.3411 0.0814  3   ARG   P C   
26563 O  O   . ARG   P  4   ? 1.9524 0.8708 1.9034 0.2225  -0.2965 -0.0112 3   ARG   P O   
26564 C  CB  . ARG   P  4   ? 1.9724 1.3344 1.9394 0.3239  -0.3840 0.1109  3   ARG   P CB  
26565 C  CG  . ARG   P  4   ? 2.0506 1.4668 1.9903 0.3303  -0.3605 0.0279  3   ARG   P CG  
26566 C  CD  . ARG   P  4   ? 2.0644 1.6907 2.1009 0.2902  -0.3311 0.0575  3   ARG   P CD  
26567 N  NE  . ARG   P  4   ? 2.1744 1.8231 2.0765 0.2566  -0.3560 0.0745  3   ARG   P NE  
26568 C  CZ  . ARG   P  4   ? 2.3153 1.7740 2.1151 0.2177  -0.2845 0.1037  3   ARG   P CZ  
26569 N  NH1 . ARG   P  4   ? 2.2944 1.6821 2.1438 0.1954  -0.2805 0.0522  3   ARG   P NH1 
26570 N  NH2 . ARG   P  4   ? 2.4095 1.8338 2.0419 0.2376  -0.2723 0.1607  3   ARG   P NH2 
26571 N  N   . ARG   P  5   ? 1.9710 0.8927 1.8349 0.2124  -0.3853 0.0392  4   ARG   P N   
26572 C  CA  . ARG   P  5   ? 1.9915 0.8992 1.8429 0.1891  -0.4149 0.0191  4   ARG   P CA  
26573 C  C   . ARG   P  5   ? 1.9911 0.8002 1.7517 0.1800  -0.3968 0.0036  4   ARG   P C   
26574 O  O   . ARG   P  5   ? 1.9912 0.7988 1.7354 0.2391  -0.3962 -0.0167 4   ARG   P O   
26575 C  CB  . ARG   P  5   ? 2.0539 1.1023 1.8359 0.1126  -0.4163 0.0072  4   ARG   P CB  
26576 C  CG  . ARG   P  5   ? 2.1007 1.0764 1.9258 0.0785  -0.4059 -0.0345 4   ARG   P CG  
26577 C  CD  . ARG   P  5   ? 2.0904 1.1544 1.9220 0.0359  -0.4294 -0.0223 4   ARG   P CD  
26578 N  NE  . ARG   P  5   ? 2.0046 1.3296 1.8334 -0.0007 -0.4647 -0.0080 4   ARG   P NE  
26579 C  CZ  . ARG   P  5   ? 1.9832 1.3484 1.8952 0.0672  -0.4174 0.0284  4   ARG   P CZ  
26580 N  NH1 . ARG   P  5   ? 1.9812 1.2239 1.9273 0.0649  -0.4653 0.0499  4   ARG   P NH1 
26581 N  NH2 . ARG   P  5   ? 2.0204 1.4463 1.9085 0.0147  -0.4120 -0.0056 4   ARG   P NH2 
26582 N  N   . TYR   P  6   ? 1.9985 0.6875 1.7123 0.1007  -0.3880 -0.0259 5   TYR   P N   
26583 C  CA  . TYR   P  6   ? 1.9986 0.6267 1.6815 0.0908  -0.3858 -0.0413 5   TYR   P CA  
26584 C  C   . TYR   P  6   ? 1.9261 0.5145 1.6690 0.0606  -0.3802 -0.0726 5   TYR   P C   
26585 O  O   . TYR   P  6   ? 1.9147 0.5000 1.6517 0.0414  -0.3829 -0.0929 5   TYR   P O   
26586 C  CB  . TYR   P  6   ? 1.9989 0.6250 1.7053 0.0799  -0.3800 -0.0679 5   TYR   P CB  
26587 C  CG  . TYR   P  6   ? 2.0398 0.6411 1.7277 0.0876  -0.4022 -0.0643 5   TYR   P CG  
26588 C  CD1 . TYR   P  6   ? 2.0507 0.6671 1.7442 0.0927  -0.4023 -0.0276 5   TYR   P CD1 
26589 C  CD2 . TYR   P  6   ? 2.0544 0.6469 1.7311 0.0896  -0.4186 -0.0618 5   TYR   P CD2 
26590 C  CE1 . TYR   P  6   ? 2.0660 0.6781 1.7393 0.0906  -0.4031 -0.0182 5   TYR   P CE1 
26591 C  CE2 . TYR   P  6   ? 2.0901 0.6369 1.7320 0.1155  -0.4159 -0.0479 5   TYR   P CE2 
26592 C  CZ  . TYR   P  6   ? 2.0846 0.6560 1.7146 0.1178  -0.4191 -0.0275 5   TYR   P CZ  
26593 O  OH  . TYR   P  6   ? 2.1161 0.7302 1.6995 0.1248  -0.3946 0.0042  5   TYR   P OH  
26594 N  N   . ASP   P  7   ? 1.9535 0.4709 1.6419 0.0525  -0.3829 -0.0733 6   ASP   P N   
26595 C  CA  . ASP   P  7   ? 1.9657 0.4705 1.6209 0.0669  -0.3444 -0.0752 6   ASP   P CA  
26596 C  C   . ASP   P  7   ? 1.9787 0.4430 1.5802 0.0565  -0.3156 -0.0462 6   ASP   P C   
26597 O  O   . ASP   P  7   ? 2.0647 0.3848 1.6439 0.0589  -0.2754 -0.0625 6   ASP   P O   
26598 C  CB  . ASP   P  7   ? 1.9474 0.3845 1.6154 0.1055  -0.3506 -0.0919 6   ASP   P CB  
26599 C  CG  . ASP   P  7   ? 1.9453 0.2244 1.6554 0.1384  -0.3186 -0.1685 6   ASP   P CG  
26600 O  OD1 . ASP   P  7   ? 1.9528 0.2092 1.6968 0.1724  -0.3328 -0.2083 6   ASP   P OD1 
26601 O  OD2 . ASP   P  7   ? 1.9845 0.2257 1.6589 0.1830  -0.2664 -0.1821 6   ASP   P OD2 
26602 N  N   . SER   P  8   ? 1.9925 0.5134 1.5071 0.0294  -0.3229 0.0231  7   SER   P N   
26603 C  CA  . SER   P  8   ? 1.9871 0.5959 1.4716 0.0423  -0.3335 0.0212  7   SER   P CA  
26604 C  C   . SER   P  8   ? 2.0156 0.6869 1.4507 0.0573  -0.2993 -0.0384 7   SER   P C   
26605 O  O   . SER   P  8   ? 2.0758 0.7558 1.4174 0.0374  -0.2622 -0.0468 7   SER   P O   
26606 C  CB  . SER   P  8   ? 1.9879 0.6134 1.4829 0.0338  -0.3618 0.0581  7   SER   P CB  
26607 O  OG  . SER   P  8   ? 1.9801 0.6446 1.4452 0.0636  -0.4217 0.1157  7   SER   P OG  
26608 N  N   . ARG   P  9   ? 2.0035 0.7030 1.4532 0.0384  -0.2960 -0.1094 8   ARG   P N   
26609 C  CA  . ARG   P  9   ? 1.9788 0.7719 1.4450 0.0510  -0.2872 -0.1125 8   ARG   P CA  
26610 C  C   . ARG   P  9   ? 1.9172 0.7746 1.5106 0.0442  -0.2898 -0.0742 8   ARG   P C   
26611 O  O   . ARG   P  9   ? 1.8980 0.8240 1.4852 0.0149  -0.3109 -0.0723 8   ARG   P O   
26612 C  CB  . ARG   P  9   ? 2.0185 0.8009 1.4990 0.1009  -0.2919 -0.1150 8   ARG   P CB  
26613 C  CG  . ARG   P  9   ? 2.0138 0.8450 1.5181 0.1634  -0.3005 -0.1147 8   ARG   P CG  
26614 C  CD  . ARG   P  9   ? 2.0483 0.9324 1.5855 0.2511  -0.2785 -0.1152 8   ARG   P CD  
26615 N  NE  . ARG   P  9   ? 2.0827 1.0367 1.6234 0.3225  -0.2562 -0.1250 8   ARG   P NE  
26616 C  CZ  . ARG   P  9   ? 2.1659 1.0549 1.6766 0.3737  -0.2298 -0.1151 8   ARG   P CZ  
26617 N  NH1 . ARG   P  9   ? 2.1913 0.9994 1.7064 0.4036  -0.1875 -0.1260 8   ARG   P NH1 
26618 N  NH2 . ARG   P  9   ? 2.2125 1.1301 1.6689 0.4358  -0.2395 -0.1322 8   ARG   P NH2 
26619 N  N   . THR   P  10  ? 1.8882 0.7185 1.4340 0.0140  -0.3132 -0.0647 9   THR   P N   
26620 C  CA  . THR   P  10  ? 1.9063 0.6924 1.4311 -0.0258 -0.3276 -0.0449 9   THR   P CA  
26621 C  C   . THR   P  10  ? 1.9238 0.7134 1.4486 -0.0188 -0.3506 -0.0001 9   THR   P C   
26622 O  O   . THR   P  10  ? 1.9822 0.8371 1.4652 -0.0465 -0.4216 0.0732  9   THR   P O   
26623 C  CB  . THR   P  10  ? 1.8926 0.6712 1.4000 -0.0551 -0.3177 -0.0417 9   THR   P CB  
26624 O  OG1 . THR   P  10  ? 1.8502 0.6572 1.3946 -0.0639 -0.2741 0.0291  9   THR   P OG1 
26625 C  CG2 . THR   P  10  ? 1.9068 0.7069 1.3857 -0.0674 -0.3168 -0.0613 9   THR   P CG2 
26626 N  N   . THR   P  11  ? 1.8598 0.7225 1.5701 -0.0043 -0.4093 -0.0690 10  THR   P N   
26627 C  CA  . THR   P  11  ? 1.8110 0.6932 1.5983 0.0274  -0.4122 -0.0568 10  THR   P CA  
26628 C  C   . THR   P  11  ? 1.8164 0.7185 1.6928 0.0551  -0.4176 -0.0885 10  THR   P C   
26629 O  O   . THR   P  11  ? 1.8411 0.7248 1.7818 0.0364  -0.3772 -0.1219 10  THR   P O   
26630 C  CB  . THR   P  11  ? 1.7591 0.6433 1.5793 0.1354  -0.4315 -0.0019 10  THR   P CB  
26631 O  OG1 . THR   P  11  ? 1.7462 0.6836 1.5690 0.1119  -0.4091 -0.0294 10  THR   P OG1 
26632 C  CG2 . THR   P  11  ? 1.7586 0.5700 1.5493 0.1615  -0.4610 0.0372  10  THR   P CG2 
26633 N  N   . ILE   P  12  ? 1.8707 0.7096 1.6776 0.0607  -0.4443 -0.0592 11  ILE   P N   
26634 C  CA  . ILE   P  12  ? 1.9450 0.7043 1.5754 0.0212  -0.4288 -0.1024 11  ILE   P CA  
26635 C  C   . ILE   P  12  ? 1.9512 0.5790 1.5614 0.0162  -0.4324 -0.0550 11  ILE   P C   
26636 O  O   . ILE   P  12  ? 1.9612 0.5088 1.4822 -0.0049 -0.4974 -0.0637 11  ILE   P O   
26637 C  CB  . ILE   P  12  ? 1.9979 0.7297 1.6424 0.0529  -0.4386 -0.0811 11  ILE   P CB  
26638 C  CG1 . ILE   P  12  ? 2.0365 0.6540 1.6211 0.0514  -0.4223 -0.1499 11  ILE   P CG1 
26639 C  CG2 . ILE   P  12  ? 2.0094 0.8735 1.6408 0.0269  -0.4677 -0.0939 11  ILE   P CG2 
26640 C  CD1 . ILE   P  12  ? 2.0332 0.7298 1.6347 0.0850  -0.4098 -0.1285 11  ILE   P CD1 
26641 N  N   . PHE   P  13  ? 2.0218 0.5354 1.5541 0.0547  -0.4171 -0.0552 12  PHE   P N   
26642 C  CA  . PHE   P  13  ? 2.0701 0.6903 1.5272 0.0689  -0.4023 -0.0858 12  PHE   P CA  
26643 C  C   . PHE   P  13  ? 2.1409 0.7134 1.5778 0.0679  -0.4202 -0.0395 12  PHE   P C   
26644 O  O   . PHE   P  13  ? 2.1800 0.8521 1.5120 0.0307  -0.4499 -0.0644 12  PHE   P O   
26645 C  CB  . PHE   P  13  ? 2.0850 0.6611 1.5510 0.0936  -0.3866 -0.0616 12  PHE   P CB  
26646 C  CG  . PHE   P  13  ? 2.0487 0.5846 1.4933 0.0832  -0.3874 -0.1334 12  PHE   P CG  
26647 C  CD1 . PHE   P  13  ? 2.0481 0.5650 1.4822 0.1043  -0.3841 -0.0988 12  PHE   P CD1 
26648 C  CD2 . PHE   P  13  ? 2.0482 0.5484 1.4080 0.1059  -0.3831 -0.1496 12  PHE   P CD2 
26649 C  CE1 . PHE   P  13  ? 2.0234 0.5363 1.4670 0.0879  -0.3884 -0.1224 12  PHE   P CE1 
26650 C  CE2 . PHE   P  13  ? 2.0230 0.5811 1.3971 0.0905  -0.3874 -0.1215 12  PHE   P CE2 
26651 C  CZ  . PHE   P  13  ? 2.0149 0.5541 1.4344 0.0806  -0.3942 -0.1380 12  PHE   P CZ  
26652 N  N   . SER   P  14  ? 2.1534 0.7259 1.6290 0.0771  -0.4257 -0.0786 13  SER   P N   
26653 C  CA  . SER   P  14  ? 2.1940 0.7574 1.6573 0.1678  -0.3908 -0.1023 13  SER   P CA  
26654 C  C   . SER   P  14  ? 2.1509 0.7324 1.6794 0.1648  -0.4053 -0.1254 13  SER   P C   
26655 O  O   . SER   P  14  ? 2.0925 0.7091 1.6430 0.0908  -0.4136 -0.1770 13  SER   P O   
26656 C  CB  . SER   P  14  ? 2.1774 0.7939 1.6657 0.1907  -0.4135 -0.0937 13  SER   P CB  
26657 O  OG  . SER   P  14  ? 2.1943 0.8607 1.6754 0.2878  -0.3903 -0.0649 13  SER   P OG  
26658 N  N   . PRO   P  15  ? 2.1472 0.7649 1.7318 0.2033  -0.4055 -0.1623 14  PRO   P N   
26659 C  CA  . PRO   P  15  ? 2.1390 0.7588 1.7633 0.2095  -0.3906 -0.1472 14  PRO   P CA  
26660 C  C   . PRO   P  15  ? 2.1576 0.6658 1.7357 0.1768  -0.3437 -0.0959 14  PRO   P C   
26661 O  O   . PRO   P  15  ? 2.1040 0.4969 1.7643 0.1638  -0.3481 -0.1054 14  PRO   P O   
26662 C  CB  . PRO   P  15  ? 2.1836 0.7995 1.7767 0.2925  -0.4004 -0.1593 14  PRO   P CB  
26663 C  CG  . PRO   P  15  ? 2.1684 0.8631 1.7644 0.2877  -0.4159 -0.1760 14  PRO   P CG  
26664 C  CD  . PRO   P  15  ? 2.1610 0.7832 1.7135 0.2619  -0.4234 -0.1537 14  PRO   P CD  
26665 N  N   . GLU   P  16  ? 2.1754 0.7140 1.7884 0.1077  -0.3526 -0.0440 15  GLU   P N   
26666 C  CA  . GLU   P  16  ? 2.1964 0.8367 1.7881 0.0169  -0.3590 -0.0322 15  GLU   P CA  
26667 C  C   . GLU   P  16  ? 2.1755 0.8385 1.6579 0.0013  -0.3990 -0.0591 15  GLU   P C   
26668 O  O   . GLU   P  16  ? 2.1799 1.0486 1.6689 -0.0088 -0.4398 -0.0808 15  GLU   P O   
26669 C  CB  . GLU   P  16  ? 2.2571 0.8694 1.8819 -0.0460 -0.3423 0.0144  15  GLU   P CB  
26670 C  CG  . GLU   P  16  ? 2.2669 0.8702 2.0338 -0.0768 -0.2884 0.0255  15  GLU   P CG  
26671 C  CD  . GLU   P  16  ? 2.2578 0.8890 2.1053 -0.1107 -0.3112 0.1251  15  GLU   P CD  
26672 O  OE1 . GLU   P  16  ? 2.2629 0.7422 2.2129 -0.1375 -0.2407 0.1504  15  GLU   P OE1 
26673 O  OE2 . GLU   P  16  ? 2.2748 1.0040 2.2293 -0.2706 -0.1968 0.0496  15  GLU   P OE2 
26674 N  N   . GLY   P  17  ? 2.1227 0.7362 1.7027 -0.0169 -0.3614 -0.0338 16  GLY   P N   
26675 C  CA  . GLY   P  17  ? 2.0173 0.7191 1.6556 -0.0294 -0.3755 -0.0653 16  GLY   P CA  
26676 C  C   . GLY   P  17  ? 2.0175 0.6509 1.6119 -0.0321 -0.3807 -0.0953 16  GLY   P C   
26677 O  O   . GLY   P  17  ? 2.0074 0.6021 1.6227 0.0003  -0.3977 -0.1563 16  GLY   P O   
26678 N  N   . ARG   P  18  ? 2.0090 0.5945 1.5904 0.0024  -0.3901 -0.0937 17  ARG   P N   
26679 C  CA  . ARG   P  18  ? 2.0135 0.6084 1.5843 0.0114  -0.3934 -0.1252 17  ARG   P CA  
26680 C  C   . ARG   P  18  ? 1.9692 0.4367 1.6198 0.0305  -0.3935 -0.1369 17  ARG   P C   
26681 O  O   . ARG   P  18  ? 1.9785 0.3381 1.6731 -0.0259 -0.4361 -0.1480 17  ARG   P O   
26682 C  CB  . ARG   P  18  ? 1.9962 0.7423 1.5902 -0.0559 -0.3785 -0.1655 17  ARG   P CB  
26683 C  CG  . ARG   P  18  ? 2.0678 0.9101 1.6156 -0.0618 -0.3454 -0.2441 17  ARG   P CG  
26684 C  CD  . ARG   P  18  ? 2.1019 0.9711 1.7112 -0.1279 -0.3110 -0.2829 17  ARG   P CD  
26685 N  NE  . ARG   P  18  ? 2.1549 1.1108 1.7234 -0.1596 -0.2671 -0.3367 17  ARG   P NE  
26686 C  CZ  . ARG   P  18  ? 2.1430 1.1848 1.7201 -0.1355 -0.2530 -0.3630 17  ARG   P CZ  
26687 N  NH1 . ARG   P  18  ? 2.1052 1.1955 1.7312 -0.1342 -0.2504 -0.3403 17  ARG   P NH1 
26688 N  NH2 . ARG   P  18  ? 2.2387 1.2263 1.7542 -0.1412 -0.2185 -0.4157 17  ARG   P NH2 
26689 N  N   . LEU   P  19  ? 1.9621 0.4762 1.5931 0.0556  -0.4093 -0.1360 18  LEU   P N   
26690 C  CA  . LEU   P  19  ? 1.9464 0.5036 1.5860 0.0779  -0.3816 -0.1282 18  LEU   P CA  
26691 C  C   . LEU   P  19  ? 1.9496 0.4236 1.6404 0.0866  -0.3657 -0.1401 18  LEU   P C   
26692 O  O   . LEU   P  19  ? 1.9407 0.4119 1.6023 0.0449  -0.3672 -0.1075 18  LEU   P O   
26693 C  CB  . LEU   P  19  ? 1.9458 0.4987 1.5317 0.0758  -0.3857 -0.1481 18  LEU   P CB  
26694 C  CG  . LEU   P  19  ? 1.9395 0.5055 1.5000 0.1000  -0.3883 -0.1290 18  LEU   P CG  
26695 C  CD1 . LEU   P  19  ? 1.9224 0.5544 1.4727 0.1285  -0.3881 -0.0918 18  LEU   P CD1 
26696 C  CD2 . LEU   P  19  ? 1.9275 0.5335 1.5280 0.0995  -0.3856 -0.1370 18  LEU   P CD2 
26697 N  N   . TYR   P  20  ? 2.0032 0.3675 1.7004 0.1312  -0.3212 -0.1304 19  TYR   P N   
26698 C  CA  . TYR   P  20  ? 2.0406 0.4744 1.7577 0.1218  -0.2466 -0.1117 19  TYR   P CA  
26699 C  C   . TYR   P  20  ? 2.0136 0.4715 1.7267 0.1337  -0.2966 -0.0908 19  TYR   P C   
26700 O  O   . TYR   P  20  ? 2.0627 0.3770 1.6598 0.1453  -0.3315 -0.1555 19  TYR   P O   
26701 C  CB  . TYR   P  20  ? 2.0540 0.5697 1.8141 0.1606  -0.2563 -0.0788 19  TYR   P CB  
26702 C  CG  . TYR   P  20  ? 2.0577 0.7060 1.9398 0.1914  -0.1958 -0.0976 19  TYR   P CG  
26703 C  CD1 . TYR   P  20  ? 2.1211 0.7141 2.0106 0.1887  -0.1602 -0.1317 19  TYR   P CD1 
26704 C  CD2 . TYR   P  20  ? 2.0930 0.7639 2.0022 0.1231  -0.1862 -0.1391 19  TYR   P CD2 
26705 C  CE1 . TYR   P  20  ? 2.1677 0.6851 2.0799 0.1778  -0.1262 -0.2043 19  TYR   P CE1 
26706 C  CE2 . TYR   P  20  ? 2.1262 0.8233 2.0455 0.1538  -0.1533 -0.1557 19  TYR   P CE2 
26707 C  CZ  . TYR   P  20  ? 2.1426 0.8062 2.0800 0.2036  -0.1467 -0.1619 19  TYR   P CZ  
26708 O  OH  . TYR   P  20  ? 2.0489 0.8992 2.0848 0.2378  -0.2614 -0.0913 19  TYR   P OH  
26709 N  N   . GLN   P  21  ? 1.9952 0.4659 1.6782 0.1166  -0.3108 -0.0621 20  GLN   P N   
26710 C  CA  . GLN   P  21  ? 1.9543 0.4829 1.6355 0.1100  -0.3422 -0.0459 20  GLN   P CA  
26711 C  C   . GLN   P  21  ? 1.9695 0.4683 1.6664 0.1265  -0.3474 -0.0293 20  GLN   P C   
26712 O  O   . GLN   P  21  ? 1.9854 0.4682 1.7041 0.1744  -0.3137 0.0263  20  GLN   P O   
26713 C  CB  . GLN   P  21  ? 1.9438 0.5104 1.6105 0.0752  -0.3560 -0.0336 20  GLN   P CB  
26714 C  CG  . GLN   P  21  ? 1.9609 0.6197 1.6099 0.0592  -0.4123 -0.0936 20  GLN   P CG  
26715 C  CD  . GLN   P  21  ? 1.9546 0.6445 1.6560 0.0109  -0.4041 -0.1364 20  GLN   P CD  
26716 O  OE1 . GLN   P  21  ? 1.9568 0.6494 1.6798 0.0115  -0.4611 -0.1028 20  GLN   P OE1 
26717 N  NE2 . GLN   P  21  ? 1.9515 0.7079 1.6829 0.0397  -0.4130 -0.1636 20  GLN   P NE2 
26718 N  N   . VAL   P  22  ? 1.8784 0.4763 1.6366 0.0799  -0.3537 -0.0839 21  VAL   P N   
26719 C  CA  . VAL   P  22  ? 1.8414 0.4669 1.6262 0.0388  -0.3704 -0.1153 21  VAL   P CA  
26720 C  C   . VAL   P  22  ? 1.8378 0.4763 1.6486 0.0586  -0.3975 -0.1524 21  VAL   P C   
26721 O  O   . VAL   P  22  ? 1.8349 0.2775 1.6308 0.0418  -0.4351 -0.2300 21  VAL   P O   
26722 C  CB  . VAL   P  22  ? 1.8220 0.5178 1.6333 0.0322  -0.3855 -0.0787 21  VAL   P CB  
26723 C  CG1 . VAL   P  22  ? 1.8118 0.5558 1.6094 0.0090  -0.3702 -0.0717 21  VAL   P CG1 
26724 C  CG2 . VAL   P  22  ? 1.7943 0.5392 1.6113 0.0002  -0.3850 -0.0475 21  VAL   P CG2 
26725 N  N   . GLU   P  23  ? 1.8869 0.4380 1.6695 0.0329  -0.3975 -0.1810 22  GLU   P N   
26726 C  CA  . GLU   P  23  ? 1.9445 0.4153 1.6881 0.0165  -0.3893 -0.1543 22  GLU   P CA  
26727 C  C   . GLU   P  23  ? 1.9261 0.3349 1.5916 0.0599  -0.4256 -0.1703 22  GLU   P C   
26728 O  O   . GLU   P  23  ? 1.9304 0.3004 1.6576 0.0506  -0.4342 -0.1396 22  GLU   P O   
26729 C  CB  . GLU   P  23  ? 1.9789 0.4778 1.7590 0.0464  -0.3479 -0.1459 22  GLU   P CB  
26730 C  CG  . GLU   P  23  ? 2.0397 0.5575 1.7986 -0.0024 -0.3197 -0.1431 22  GLU   P CG  
26731 C  CD  . GLU   P  23  ? 2.1013 0.5738 1.7980 -0.0459 -0.3515 -0.1855 22  GLU   P CD  
26732 O  OE1 . GLU   P  23  ? 2.1763 0.4957 1.9144 -0.0291 -0.2997 -0.2200 22  GLU   P OE1 
26733 O  OE2 . GLU   P  23  ? 2.2026 0.7561 1.7938 -0.1262 -0.3682 -0.2855 22  GLU   P OE2 
26734 N  N   . TYR   P  24  ? 1.8808 0.3410 1.5830 0.0597  -0.4343 -0.2337 23  TYR   P N   
26735 C  CA  . TYR   P  24  ? 1.8805 0.4742 1.4839 0.0448  -0.4668 -0.2734 23  TYR   P CA  
26736 C  C   . TYR   P  24  ? 1.9071 0.4495 1.4702 0.0588  -0.4793 -0.2524 23  TYR   P C   
26737 O  O   . TYR   P  24  ? 1.9226 0.4906 1.4861 0.0394  -0.4776 -0.2622 23  TYR   P O   
26738 C  CB  . TYR   P  24  ? 1.8456 0.5511 1.4927 0.0359  -0.4821 -0.3241 23  TYR   P CB  
26739 C  CG  . TYR   P  24  ? 1.8208 0.5765 1.4607 0.0328  -0.5147 -0.3301 23  TYR   P CG  
26740 C  CD1 . TYR   P  24  ? 1.8247 0.5822 1.4557 0.0487  -0.5172 -0.3290 23  TYR   P CD1 
26741 C  CD2 . TYR   P  24  ? 1.8013 0.6115 1.4878 0.0360  -0.5164 -0.3142 23  TYR   P CD2 
26742 C  CE1 . TYR   P  24  ? 1.8473 0.5862 1.4669 0.0632  -0.5004 -0.3485 23  TYR   P CE1 
26743 C  CE2 . TYR   P  24  ? 1.8248 0.5823 1.4918 0.0317  -0.4897 -0.3708 23  TYR   P CE2 
26744 C  CZ  . TYR   P  24  ? 1.8248 0.5713 1.4985 0.0548  -0.4994 -0.3710 23  TYR   P CZ  
26745 O  OH  . TYR   P  24  ? 1.9071 0.5739 1.5283 0.0955  -0.4199 -0.4467 23  TYR   P OH  
26746 N  N   . ALA   P  25  ? 1.8588 0.4631 1.4446 0.0364  -0.4809 -0.2232 24  ALA   P N   
26747 C  CA  . ALA   P  25  ? 1.8649 0.4714 1.4555 0.0460  -0.4694 -0.2134 24  ALA   P CA  
26748 C  C   . ALA   P  25  ? 1.8707 0.4824 1.4579 0.0321  -0.4649 -0.2272 24  ALA   P C   
26749 O  O   . ALA   P  25  ? 1.8746 0.4043 1.4737 0.0432  -0.4604 -0.2459 24  ALA   P O   
26750 C  CB  . ALA   P  25  ? 1.8150 0.4957 1.4533 0.0327  -0.4788 -0.2085 24  ALA   P CB  
26751 N  N   . LEU   P  26  ? 1.8727 0.5888 1.4777 0.0326  -0.4210 -0.2075 25  LEU   P N   
26752 C  CA  . LEU   P  26  ? 1.8665 0.6548 1.4601 0.0085  -0.3987 -0.2214 25  LEU   P CA  
26753 C  C   . LEU   P  26  ? 1.9063 0.6562 1.5127 -0.0049 -0.3904 -0.2182 25  LEU   P C   
26754 O  O   . LEU   P  26  ? 1.8952 0.6255 1.5701 -0.0280 -0.3646 -0.2155 25  LEU   P O   
26755 C  CB  . LEU   P  26  ? 1.8629 0.6820 1.4456 0.0136  -0.4103 -0.2555 25  LEU   P CB  
26756 C  CG  . LEU   P  26  ? 1.8322 0.7272 1.3862 -0.0096 -0.3988 -0.2552 25  LEU   P CG  
26757 C  CD1 . LEU   P  26  ? 1.8342 0.7482 1.3596 -0.0104 -0.4071 -0.2523 25  LEU   P CD1 
26758 C  CD2 . LEU   P  26  ? 1.8254 0.7305 1.3763 -0.0173 -0.4047 -0.2682 25  LEU   P CD2 
26759 N  N   . GLU   P  27  ? 1.8761 0.7835 1.5230 0.0356  -0.3980 -0.1706 26  GLU   P N   
26760 C  CA  . GLU   P  27  ? 1.9120 0.8553 1.5450 0.0176  -0.3846 -0.0885 26  GLU   P CA  
26761 C  C   . GLU   P  27  ? 1.9417 0.8622 1.4807 0.0243  -0.4023 -0.0879 26  GLU   P C   
26762 O  O   . GLU   P  27  ? 1.9851 0.9372 1.5197 -0.0238 -0.4466 -0.0429 26  GLU   P O   
26763 C  CB  . GLU   P  27  ? 1.9207 0.9286 1.6195 0.0715  -0.3831 -0.1058 26  GLU   P CB  
26764 C  CG  . GLU   P  27  ? 1.9941 0.9261 1.6970 0.0520  -0.3578 -0.1445 26  GLU   P CG  
26765 C  CD  . GLU   P  27  ? 2.0720 1.0202 1.6619 0.0982  -0.3570 -0.2070 26  GLU   P CD  
26766 O  OE1 . GLU   P  27  ? 2.1151 1.0789 1.7683 0.0670  -0.3013 -0.2226 26  GLU   P OE1 
26767 O  OE2 . GLU   P  27  ? 2.0812 1.0792 1.6635 0.1701  -0.3532 -0.1100 26  GLU   P OE2 
26768 N  N   . SER   P  28  ? 1.8537 0.8063 1.4771 0.0091  -0.3845 -0.0621 27  SER   P N   
26769 C  CA  . SER   P  28  ? 1.8181 0.7408 1.4685 0.0057  -0.4218 -0.1009 27  SER   P CA  
26770 C  C   . SER   P  28  ? 1.8156 0.7053 1.4708 0.0015  -0.4215 -0.1028 27  SER   P C   
26771 O  O   . SER   P  28  ? 1.7888 0.7311 1.4760 0.0272  -0.4337 -0.1239 27  SER   P O   
26772 C  CB  . SER   P  28  ? 1.7531 0.7642 1.4367 0.0146  -0.3916 -0.1163 27  SER   P CB  
26773 O  OG  . SER   P  28  ? 1.7322 0.8422 1.4332 0.0003  -0.4101 -0.1647 27  SER   P OG  
26774 N  N   . ILE   P  29  ? 1.7945 0.6466 1.5111 -0.0418 -0.4391 -0.1073 28  ILE   P N   
26775 C  CA  . ILE   P  29  ? 1.7670 0.6726 1.5283 -0.0933 -0.5009 -0.1339 28  ILE   P CA  
26776 C  C   . ILE   P  29  ? 1.7739 0.6065 1.5922 -0.1054 -0.5000 -0.1214 28  ILE   P C   
26777 O  O   . ILE   P  29  ? 1.7418 0.4507 1.6125 -0.1909 -0.5372 -0.1721 28  ILE   P O   
26778 C  CB  . ILE   P  29  ? 1.7650 0.7950 1.5011 -0.1082 -0.4799 -0.1016 28  ILE   P CB  
26779 C  CG1 . ILE   P  29  ? 1.7379 0.8046 1.4799 -0.1237 -0.4870 -0.0901 28  ILE   P CG1 
26780 C  CG2 . ILE   P  29  ? 1.7802 0.8628 1.5082 -0.0837 -0.4758 -0.0753 28  ILE   P CG2 
26781 C  CD1 . ILE   P  29  ? 1.7435 0.7364 1.4263 -0.1162 -0.5157 -0.0850 28  ILE   P CD1 
26782 N  N   . SER   P  30  ? 1.7655 0.5965 1.5714 -0.1286 -0.5542 -0.1568 29  SER   P N   
26783 C  CA  . SER   P  30  ? 1.8031 0.5798 1.5566 -0.1377 -0.5540 -0.1496 29  SER   P CA  
26784 C  C   . SER   P  30  ? 1.8658 0.5444 1.6029 -0.1314 -0.5117 -0.1072 29  SER   P C   
26785 O  O   . SER   P  30  ? 1.8144 0.5878 1.6167 -0.1999 -0.4874 -0.0253 29  SER   P O   
26786 C  CB  . SER   P  30  ? 1.8161 0.5729 1.5411 -0.1313 -0.6091 -0.1855 29  SER   P CB  
26787 O  OG  . SER   P  30  ? 1.8532 0.6224 1.5160 -0.1475 -0.6635 -0.1946 29  SER   P OG  
26788 N  N   . HIS   P  31  ? 1.8431 0.4809 1.6019 -0.1705 -0.4884 -0.0873 30  HIS   P N   
26789 C  CA  . HIS   P  31  ? 1.8831 0.5386 1.6729 -0.1803 -0.4412 -0.0748 30  HIS   P CA  
26790 C  C   . HIS   P  31  ? 1.8689 0.5403 1.6085 -0.1868 -0.4476 -0.0667 30  HIS   P C   
26791 O  O   . HIS   P  31  ? 1.9456 0.4052 1.6098 -0.1885 -0.4255 0.0029  30  HIS   P O   
26792 C  CB  . HIS   P  31  ? 1.9128 0.6002 1.7208 -0.1338 -0.4436 -0.0457 30  HIS   P CB  
26793 C  CG  . HIS   P  31  ? 1.9881 0.6466 1.8771 -0.0866 -0.3726 -0.0333 30  HIS   P CG  
26794 N  ND1 . HIS   P  31  ? 2.0528 0.6065 1.9348 -0.0917 -0.3626 -0.0161 30  HIS   P ND1 
26795 C  CD2 . HIS   P  31  ? 1.9737 0.6149 1.9277 -0.1064 -0.3574 -0.0561 30  HIS   P CD2 
26796 C  CE1 . HIS   P  31  ? 2.0772 0.6262 1.9995 -0.0669 -0.3331 0.0026  30  HIS   P CE1 
26797 N  NE2 . HIS   P  31  ? 2.0194 0.5890 2.0288 -0.0430 -0.3241 0.0181  30  HIS   P NE2 
26798 N  N   . ALA   P  32  ? 1.8361 0.5564 1.5406 -0.2247 -0.4480 -0.0845 31  ALA   P N   
26799 C  CA  . ALA   P  32  ? 1.8359 0.5691 1.5288 -0.2383 -0.4237 -0.1302 31  ALA   P CA  
26800 C  C   . ALA   P  32  ? 1.8309 0.6116 1.5474 -0.2422 -0.4248 -0.1421 31  ALA   P C   
26801 O  O   . ALA   P  32  ? 1.8456 0.7417 1.5673 -0.2778 -0.3984 -0.1795 31  ALA   P O   
26802 C  CB  . ALA   P  32  ? 1.8182 0.5585 1.4976 -0.2249 -0.4339 -0.1249 31  ALA   P CB  
26803 N  N   . GLY   P  33  ? 1.8526 0.5873 1.5299 -0.2231 -0.4168 -0.1382 32  GLY   P N   
26804 C  CA  . GLY   P  33  ? 1.8850 0.6151 1.5124 -0.2140 -0.4356 -0.1616 32  GLY   P CA  
26805 C  C   . GLY   P  33  ? 1.8924 0.6226 1.4872 -0.1965 -0.4573 -0.1725 32  GLY   P C   
26806 O  O   . GLY   P  33  ? 1.8853 0.6820 1.4888 -0.2325 -0.4968 -0.2085 32  GLY   P O   
26807 N  N   . THR   P  34  ? 1.9017 0.6841 1.4627 -0.1737 -0.4596 -0.1689 33  THR   P N   
26808 C  CA  . THR   P  34  ? 1.8872 0.6946 1.4734 -0.1541 -0.4269 -0.1690 33  THR   P CA  
26809 C  C   . THR   P  34  ? 1.8437 0.6884 1.4394 -0.1639 -0.4192 -0.1600 33  THR   P C   
26810 O  O   . THR   P  34  ? 1.8613 0.5932 1.4313 -0.1293 -0.4351 -0.1699 33  THR   P O   
26811 C  CB  . THR   P  34  ? 1.9150 0.7513 1.5040 -0.1805 -0.4368 -0.1946 33  THR   P CB  
26812 O  OG1 . THR   P  34  ? 1.9133 0.7174 1.4778 -0.2268 -0.4476 -0.2185 33  THR   P OG1 
26813 C  CG2 . THR   P  34  ? 1.9354 0.7650 1.4966 -0.1875 -0.4366 -0.2115 33  THR   P CG2 
26814 N  N   . ALA   P  35  ? 1.7764 0.6704 1.4361 -0.1361 -0.4198 -0.1642 34  ALA   P N   
26815 C  CA  . ALA   P  35  ? 1.7246 0.6929 1.4413 -0.1335 -0.4234 -0.1440 34  ALA   P CA  
26816 C  C   . ALA   P  35  ? 1.7286 0.7285 1.4717 -0.1186 -0.3793 -0.0917 34  ALA   P C   
26817 O  O   . ALA   P  35  ? 1.7044 0.7130 1.5496 -0.1331 -0.3715 -0.0553 34  ALA   P O   
26818 C  CB  . ALA   P  35  ? 1.7099 0.6920 1.3647 -0.0993 -0.4209 -0.1491 34  ALA   P CB  
26819 N  N   . ILE   P  36  ? 1.7535 0.7684 1.5021 -0.0917 -0.3805 -0.0669 35  ILE   P N   
26820 C  CA  . ILE   P  36  ? 1.7913 0.6957 1.4981 -0.0950 -0.3949 -0.0769 35  ILE   P CA  
26821 C  C   . ILE   P  36  ? 1.7533 0.6806 1.4905 -0.1187 -0.3872 -0.0849 35  ILE   P C   
26822 O  O   . ILE   P  36  ? 1.7924 0.4978 1.4824 -0.1520 -0.3992 -0.0824 35  ILE   P O   
26823 C  CB  . ILE   P  36  ? 1.8599 0.7576 1.4954 -0.1266 -0.4081 -0.1142 35  ILE   P CB  
26824 C  CG1 . ILE   P  36  ? 1.9190 0.7672 1.5229 -0.1232 -0.4014 -0.0903 35  ILE   P CG1 
26825 C  CG2 . ILE   P  36  ? 1.8702 0.7225 1.4970 -0.1064 -0.4106 -0.1225 35  ILE   P CG2 
26826 C  CD1 . ILE   P  36  ? 1.9320 0.8647 1.5806 -0.1845 -0.3996 -0.0712 35  ILE   P CD1 
26827 N  N   . GLY   P  37  ? 1.7358 0.5690 1.5114 -0.1391 -0.4039 -0.0910 36  GLY   P N   
26828 C  CA  . GLY   P  37  ? 1.7609 0.5909 1.5259 -0.1142 -0.4200 -0.0778 36  GLY   P CA  
26829 C  C   . GLY   P  37  ? 1.8094 0.6076 1.5320 -0.1139 -0.4222 -0.0883 36  GLY   P C   
26830 O  O   . GLY   P  37  ? 1.8603 0.5458 1.6214 -0.0900 -0.3976 -0.0627 36  GLY   P O   
26831 N  N   . ILE   P  38  ? 1.8016 0.7282 1.5298 -0.1320 -0.4708 -0.0800 37  ILE   P N   
26832 C  CA  . ILE   P  38  ? 1.8114 0.7572 1.5417 -0.1257 -0.5244 -0.0719 37  ILE   P CA  
26833 C  C   . ILE   P  38  ? 1.8079 0.7389 1.5602 -0.1374 -0.5426 -0.0849 37  ILE   P C   
26834 O  O   . ILE   P  38  ? 1.7431 0.6044 1.6343 -0.1723 -0.5775 -0.0621 37  ILE   P O   
26835 C  CB  . ILE   P  38  ? 1.7997 0.8585 1.4848 -0.1350 -0.5465 -0.0823 37  ILE   P CB  
26836 C  CG1 . ILE   P  38  ? 1.7934 0.8558 1.4618 -0.1289 -0.5487 -0.0947 37  ILE   P CG1 
26837 C  CG2 . ILE   P  38  ? 1.8719 0.9298 1.4783 -0.1129 -0.5269 -0.0702 37  ILE   P CG2 
26838 C  CD1 . ILE   P  38  ? 1.7834 0.9397 1.4808 -0.1469 -0.5608 -0.1115 37  ILE   P CD1 
26839 N  N   . MET   P  39  ? 1.8965 0.7689 1.5442 -0.0988 -0.5109 -0.0619 38  MET   P N   
26840 C  CA  . MET   P  39  ? 2.0012 0.8425 1.5352 -0.0224 -0.5247 0.0149  38  MET   P CA  
26841 C  C   . MET   P  39  ? 1.9363 0.7589 1.5105 -0.0067 -0.4952 0.0024  38  MET   P C   
26842 O  O   . MET   P  39  ? 1.9508 0.4877 1.4972 -0.0032 -0.5790 0.0364  38  MET   P O   
26843 C  CB  . MET   P  39  ? 2.0612 0.9044 1.5989 -0.0467 -0.4568 0.0669  38  MET   P CB  
26844 C  CG  . MET   P  39  ? 2.2046 0.9246 1.7287 -0.0514 -0.4524 0.1245  38  MET   P CG  
26845 S  SD  . MET   P  39  ? 2.4120 1.1335 1.7844 -0.0935 -0.3290 0.1834  38  MET   P SD  
26846 C  CE  . MET   P  39  ? 2.4078 0.9920 1.8416 -0.0633 -0.3601 0.2349  38  MET   P CE  
26847 N  N   . ALA   P  40  ? 1.8705 0.8953 1.5667 -0.0256 -0.5332 0.0396  39  ALA   P N   
26848 C  CA  . ALA   P  40  ? 1.8310 0.9700 1.6152 -0.0721 -0.5704 0.0061  39  ALA   P CA  
26849 C  C   . ALA   P  40  ? 1.8525 0.9910 1.6229 -0.0305 -0.5686 0.0538  39  ALA   P C   
26850 O  O   . ALA   P  40  ? 1.7974 1.0086 1.6965 -0.0182 -0.5448 0.0109  39  ALA   P O   
26851 C  CB  . ALA   P  40  ? 1.8172 0.9850 1.6419 -0.1089 -0.5973 0.0072  39  ALA   P CB  
26852 N  N   . SER   P  41  ? 1.9024 1.0074 1.6111 -0.0403 -0.5598 0.0809  40  SER   P N   
26853 C  CA  . SER   P  41  ? 1.9277 0.9769 1.6026 0.0053  -0.5469 0.0665  40  SER   P CA  
26854 C  C   . SER   P  41  ? 1.9252 0.8738 1.6477 -0.0244 -0.5245 0.0995  40  SER   P C   
26855 O  O   . SER   P  41  ? 1.9776 0.8354 1.7064 0.0039  -0.4537 0.0768  40  SER   P O   
26856 C  CB  . SER   P  41  ? 1.9430 1.0526 1.6071 0.0142  -0.5790 0.1279  40  SER   P CB  
26857 O  OG  . SER   P  41  ? 1.9396 1.0535 1.5985 0.0138  -0.5965 0.1944  40  SER   P OG  
26858 N  N   . ASP   P  42  ? 1.9018 0.8694 1.6590 0.0068  -0.5169 0.0833  41  ASP   P N   
26859 C  CA  . ASP   P  42  ? 1.8471 0.9336 1.6916 0.0210  -0.4856 0.0985  41  ASP   P CA  
26860 C  C   . ASP   P  42  ? 1.8652 0.9175 1.7047 0.0361  -0.4388 0.1256  41  ASP   P C   
26861 O  O   . ASP   P  42  ? 1.8542 0.9446 1.8387 0.0673  -0.4195 0.1127  41  ASP   P O   
26862 C  CB  . ASP   P  42  ? 1.8433 0.9807 1.6720 0.0267  -0.4825 0.0997  41  ASP   P CB  
26863 C  CG  . ASP   P  42  ? 1.8244 0.9686 1.6697 0.0469  -0.4770 0.1082  41  ASP   P CG  
26864 O  OD1 . ASP   P  42  ? 1.8241 0.9834 1.5930 0.0654  -0.4999 0.1063  41  ASP   P OD1 
26865 O  OD2 . ASP   P  42  ? 1.8422 1.0222 1.7265 0.0585  -0.4446 0.1140  41  ASP   P OD2 
26866 N  N   . GLY   P  43  ? 1.8877 0.8804 1.6946 0.0318  -0.4385 0.1398  42  GLY   P N   
26867 C  CA  . GLY   P  43  ? 1.9079 0.9151 1.6766 -0.0095 -0.4061 0.0956  42  GLY   P CA  
26868 C  C   . GLY   P  43  ? 1.9262 0.8791 1.6256 -0.0118 -0.3748 0.0546  42  GLY   P C   
26869 O  O   . GLY   P  43  ? 2.0281 0.8582 1.7079 -0.0367 -0.3160 0.0183  42  GLY   P O   
26870 N  N   . ILE   P  44  ? 1.8573 0.7908 1.6248 0.0140  -0.4041 0.0429  43  ILE   P N   
26871 C  CA  . ILE   P  44  ? 1.8363 0.7429 1.5501 -0.0002 -0.4096 -0.0034 43  ILE   P CA  
26872 C  C   . ILE   P  44  ? 1.8334 0.7852 1.5288 0.0256  -0.4096 0.0079  43  ILE   P C   
26873 O  O   . ILE   P  44  ? 1.8798 0.6520 1.5285 0.0406  -0.4462 0.0285  43  ILE   P O   
26874 C  CB  . ILE   P  44  ? 1.8248 0.7254 1.5317 0.0088  -0.3892 -0.0245 43  ILE   P CB  
26875 C  CG1 . ILE   P  44  ? 1.8472 0.7189 1.5225 0.0278  -0.3880 -0.0069 43  ILE   P CG1 
26876 C  CG2 . ILE   P  44  ? 1.7965 0.7253 1.5266 0.0130  -0.3917 -0.0518 43  ILE   P CG2 
26877 C  CD1 . ILE   P  44  ? 1.8476 0.6997 1.5311 0.0174  -0.3720 -0.0082 43  ILE   P CD1 
26878 N  N   . VAL   P  45  ? 1.8248 0.7909 1.5069 0.0381  -0.3977 0.0227  44  VAL   P N   
26879 C  CA  . VAL   P  45  ? 1.8213 0.7135 1.5019 0.0602  -0.4129 0.0191  44  VAL   P CA  
26880 C  C   . VAL   P  45  ? 1.8081 0.6642 1.5156 0.1162  -0.3684 0.0376  44  VAL   P C   
26881 O  O   . VAL   P  45  ? 1.8491 0.6049 1.5245 0.1487  -0.3420 0.0592  44  VAL   P O   
26882 C  CB  . VAL   P  45  ? 1.8464 0.7087 1.4808 0.0491  -0.4185 0.0223  44  VAL   P CB  
26883 C  CG1 . VAL   P  45  ? 1.8318 0.6827 1.4873 0.0265  -0.4223 0.0026  44  VAL   P CG1 
26884 C  CG2 . VAL   P  45  ? 1.8715 0.7791 1.4842 0.0343  -0.4455 0.0142  44  VAL   P CG2 
26885 N  N   . LEU   P  46  ? 1.8275 0.6893 1.5142 0.1096  -0.3820 0.0244  45  LEU   P N   
26886 C  CA  . LEU   P  46  ? 1.8342 0.6679 1.5073 0.0973  -0.4041 0.0021  45  LEU   P CA  
26887 C  C   . LEU   P  46  ? 1.8378 0.7266 1.5148 0.0803  -0.3998 0.0092  45  LEU   P C   
26888 O  O   . LEU   P  46  ? 1.8443 0.8349 1.4781 0.1128  -0.4090 0.0182  45  LEU   P O   
26889 C  CB  . LEU   P  46  ? 1.8287 0.6119 1.5086 0.0846  -0.3997 0.0296  45  LEU   P CB  
26890 C  CG  . LEU   P  46  ? 1.8435 0.5914 1.5057 0.0889  -0.3767 0.0186  45  LEU   P CG  
26891 C  CD1 . LEU   P  46  ? 1.8805 0.6346 1.4954 0.0907  -0.3657 0.0025  45  LEU   P CD1 
26892 C  CD2 . LEU   P  46  ? 1.8654 0.4927 1.4771 0.0559  -0.3696 0.0035  45  LEU   P CD2 
26893 N  N   . ALA   P  47  ? 1.8785 0.7112 1.5540 0.0630  -0.3949 -0.0471 46  ALA   P N   
26894 C  CA  . ALA   P  47  ? 1.9173 0.7168 1.5828 0.0401  -0.3681 -0.0632 46  ALA   P CA  
26895 C  C   . ALA   P  47  ? 1.9259 0.6830 1.5394 0.0510  -0.3510 -0.0903 46  ALA   P C   
26896 O  O   . ALA   P  47  ? 1.9362 0.6582 1.6186 0.0674  -0.3318 -0.0913 46  ALA   P O   
26897 C  CB  . ALA   P  47  ? 1.9489 0.7493 1.6094 0.0001  -0.3832 -0.0616 46  ALA   P CB  
26898 N  N   . ALA   P  48  ? 1.9380 0.6728 1.5006 0.0708  -0.3513 -0.1357 47  ALA   P N   
26899 C  CA  . ALA   P  48  ? 1.9369 0.6533 1.4168 0.0396  -0.3809 -0.1959 47  ALA   P CA  
26900 C  C   . ALA   P  48  ? 1.9850 0.7081 1.4389 0.0389  -0.3465 -0.1860 47  ALA   P C   
26901 O  O   . ALA   P  48  ? 2.0488 0.7212 1.4080 0.0838  -0.3469 -0.2705 47  ALA   P O   
26902 C  CB  . ALA   P  48  ? 1.9003 0.5919 1.3683 0.0644  -0.3785 -0.1688 47  ALA   P CB  
26903 N  N   . GLU   P  49  ? 2.0155 0.6785 1.5052 0.0290  -0.3401 -0.2051 48  GLU   P N   
26904 C  CA  . GLU   P  49  ? 2.0481 0.7124 1.5711 0.0156  -0.3342 -0.1607 48  GLU   P CA  
26905 C  C   . GLU   P  49  ? 2.0529 0.6269 1.5872 0.0344  -0.3467 -0.2025 48  GLU   P C   
26906 O  O   . GLU   P  49  ? 2.0310 0.4576 1.5317 0.0250  -0.3024 -0.2328 48  GLU   P O   
26907 C  CB  . GLU   P  49  ? 2.0988 0.7232 1.5992 0.0201  -0.3054 -0.1675 48  GLU   P CB  
26908 C  CG  . GLU   P  49  ? 2.1432 0.7672 1.6251 -0.0038 -0.3173 -0.1184 48  GLU   P CG  
26909 C  CD  . GLU   P  49  ? 2.1547 0.7136 1.6409 -0.0683 -0.3463 -0.0941 48  GLU   P CD  
26910 O  OE1 . GLU   P  49  ? 2.1879 0.5399 1.6144 -0.0227 -0.3449 -0.1042 48  GLU   P OE1 
26911 O  OE2 . GLU   P  49  ? 2.1891 0.7433 1.6923 -0.1378 -0.4057 -0.1012 48  GLU   P OE2 
26912 N  N   . ARG   P  50  ? 2.0840 0.7909 1.6673 0.0712  -0.3070 -0.2116 49  ARG   P N   
26913 C  CA  . ARG   P  50  ? 2.1629 1.0615 1.7115 0.1105  -0.4040 -0.1673 49  ARG   P CA  
26914 C  C   . ARG   P  50  ? 2.1560 1.1564 1.7401 0.1728  -0.4456 -0.1067 49  ARG   P C   
26915 O  O   . ARG   P  50  ? 2.0566 1.3202 1.6235 0.1667  -0.6072 -0.1241 49  ARG   P O   
26916 C  CB  . ARG   P  50  ? 2.2281 1.1573 1.7797 0.1353  -0.3519 -0.1752 49  ARG   P CB  
26917 C  CG  . ARG   P  50  ? 2.3368 1.1559 1.8260 0.1597  -0.3798 -0.1997 49  ARG   P CG  
26918 C  CD  . ARG   P  50  ? 2.3574 1.3074 1.8699 0.1825  -0.3671 -0.2244 49  ARG   P CD  
26919 N  NE  . ARG   P  50  ? 2.4280 1.3424 1.8884 0.2366  -0.3907 -0.2479 49  ARG   P NE  
26920 C  CZ  . ARG   P  50  ? 2.4984 1.4839 1.8561 0.2683  -0.4041 -0.3055 49  ARG   P CZ  
26921 N  NH1 . ARG   P  50  ? 2.5355 1.5021 1.8753 0.3392  -0.4063 -0.2771 49  ARG   P NH1 
26922 N  NH2 . ARG   P  50  ? 2.5211 1.4983 1.8863 0.3007  -0.3788 -0.3020 49  ARG   P NH2 
26923 N  N   . LYS   P  51  ? 2.1689 1.5359 1.7896 0.1425  -0.4672 -0.0837 50  LYS   P N   
26924 C  CA  . LYS   P  51  ? 2.2265 1.5906 1.8828 0.1327  -0.4012 0.0130  50  LYS   P CA  
26925 C  C   . LYS   P  51  ? 2.2051 1.7063 1.9877 0.0244  -0.4024 0.0099  50  LYS   P C   
26926 O  O   . LYS   P  51  ? 2.1208 1.6419 1.9752 -0.0443 -0.3824 0.0276  50  LYS   P O   
26927 C  CB  . LYS   P  51  ? 2.2556 1.7374 1.8501 0.1292  -0.4096 -0.0072 50  LYS   P CB  
26928 C  CG  . LYS   P  51  ? 2.3464 1.6481 1.7905 0.1096  -0.3651 0.0146  50  LYS   P CG  
26929 C  CD  . LYS   P  51  ? 2.3258 1.5589 1.8085 0.0957  -0.3604 0.0050  50  LYS   P CD  
26930 C  CE  . LYS   P  51  ? 2.3317 1.6033 1.7791 0.0605  -0.3636 0.0042  50  LYS   P CE  
26931 N  NZ  . LYS   P  51  ? 2.3233 1.6096 1.7963 0.0681  -0.3288 -0.0077 50  LYS   P NZ  
26932 N  N   . VAL   P  52  ? 2.2668 1.7196 2.0908 0.0054  -0.4082 0.0081  51  VAL   P N   
26933 C  CA  . VAL   P  52  ? 2.2879 1.7961 2.1542 -0.0188 -0.4051 0.0236  51  VAL   P CA  
26934 C  C   . VAL   P  52  ? 2.3467 1.9976 2.0150 -0.0505 -0.4876 -0.0721 51  VAL   P C   
26935 O  O   . VAL   P  52  ? 2.3138 2.0995 2.0180 0.0326  -0.5041 -0.1219 51  VAL   P O   
26936 C  CB  . VAL   P  52  ? 2.3403 1.7993 2.2011 -0.0735 -0.4383 0.1131  51  VAL   P CB  
26937 C  CG1 . VAL   P  52  ? 2.3681 1.8107 2.1969 -0.0809 -0.4657 0.1917  51  VAL   P CG1 
26938 C  CG2 . VAL   P  52  ? 2.3272 1.7116 2.2076 -0.0714 -0.4336 0.1445  51  VAL   P CG2 
26939 N  N   . THR   P  53  ? 2.2722 1.9756 2.1210 -0.0261 -0.3151 -0.1453 52  THR   P N   
26940 C  CA  . THR   P  53  ? 2.3207 1.8974 1.9986 -0.1445 -0.2162 -0.0843 52  THR   P CA  
26941 C  C   . THR   P  53  ? 2.3518 1.6019 2.0371 -0.1755 -0.2548 -0.1276 52  THR   P C   
26942 O  O   . THR   P  53  ? 2.2727 1.5747 1.8735 -0.2536 -0.1838 -0.0436 52  THR   P O   
26943 C  CB  . THR   P  53  ? 2.3628 2.0316 2.0051 -0.1279 -0.2671 -0.0795 52  THR   P CB  
26944 O  OG1 . THR   P  53  ? 2.2987 2.0784 1.8645 -0.1907 -0.2526 0.0216  52  THR   P OG1 
26945 C  CG2 . THR   P  53  ? 2.3539 2.1132 1.9973 -0.1302 -0.2846 -0.1039 52  THR   P CG2 
26946 N  N   . SER   P  54  ? 2.3486 1.5138 1.9844 -0.1992 -0.1918 -0.0281 53  SER   P N   
26947 C  CA  . SER   P  54  ? 2.3641 1.3355 2.0915 -0.2290 -0.1800 0.0166  53  SER   P CA  
26948 C  C   . SER   P  54  ? 2.2147 1.4049 2.1231 -0.3093 -0.1326 -0.0795 53  SER   P C   
26949 O  O   . SER   P  54  ? 2.3663 1.4572 2.3228 -0.0624 -0.0755 0.0467  53  SER   P O   
26950 C  CB  . SER   P  54  ? 2.4627 1.2474 2.0569 -0.2761 -0.1709 0.1172  53  SER   P CB  
26951 O  OG  . SER   P  54  ? 2.5843 1.1467 2.0982 -0.3418 -0.1525 0.2438  53  SER   P OG  
26952 N  N   . THR   P  55  ? 2.1075 1.2273 2.0172 -0.2419 -0.2086 -0.1803 54  THR   P N   
26953 C  CA  . THR   P  55  ? 2.0145 1.2735 1.9849 -0.3309 -0.2050 -0.1690 54  THR   P CA  
26954 C  C   . THR   P  55  ? 1.9419 1.3467 1.9516 -0.3449 -0.2365 -0.2064 54  THR   P C   
26955 O  O   . THR   P  55  ? 1.8360 1.4530 2.0769 -0.3384 -0.2510 -0.2388 54  THR   P O   
26956 C  CB  . THR   P  55  ? 2.0180 1.2538 1.9328 -0.3176 -0.1835 -0.1605 54  THR   P CB  
26957 O  OG1 . THR   P  55  ? 1.9717 1.3427 1.9523 -0.3297 -0.1527 -0.0774 54  THR   P OG1 
26958 C  CG2 . THR   P  55  ? 2.0084 1.1971 1.9003 -0.3296 -0.1520 -0.1859 54  THR   P CG2 
26959 N  N   . LEU   P  56  ? 1.9848 1.3345 1.8671 -0.3283 -0.2020 -0.2275 55  LEU   P N   
26960 C  CA  . LEU   P  56  ? 1.9847 1.4095 1.7748 -0.3172 -0.2549 -0.2332 55  LEU   P CA  
26961 C  C   . LEU   P  56  ? 1.9229 1.4148 1.7368 -0.3077 -0.2722 -0.2716 55  LEU   P C   
26962 O  O   . LEU   P  56  ? 1.9536 1.3411 1.7520 -0.2779 -0.3062 -0.2299 55  LEU   P O   
26963 C  CB  . LEU   P  56  ? 2.0066 1.3311 1.8116 -0.3519 -0.2401 -0.1823 55  LEU   P CB  
26964 C  CG  . LEU   P  56  ? 2.0171 1.3209 1.8276 -0.3969 -0.2354 -0.1299 55  LEU   P CG  
26965 C  CD1 . LEU   P  56  ? 2.0414 1.2979 1.8450 -0.4396 -0.2332 -0.1268 55  LEU   P CD1 
26966 C  CD2 . LEU   P  56  ? 2.0372 1.3037 1.8626 -0.3953 -0.2165 -0.1000 55  LEU   P CD2 
26967 N  N   . LEU   P  57  ? 1.8814 1.3661 1.7102 -0.3050 -0.3040 -0.4457 56  LEU   P N   
26968 C  CA  . LEU   P  57  ? 1.8316 1.4297 1.7829 -0.3169 -0.2412 -0.4702 56  LEU   P CA  
26969 C  C   . LEU   P  57  ? 1.7987 1.6208 1.8752 -0.2492 -0.2618 -0.4280 56  LEU   P C   
26970 O  O   . LEU   P  57  ? 1.8293 1.6474 2.0015 -0.3338 -0.2733 -0.4996 56  LEU   P O   
26971 C  CB  . LEU   P  57  ? 1.9001 1.4010 1.8396 -0.2618 -0.2409 -0.5506 56  LEU   P CB  
26972 C  CG  . LEU   P  57  ? 1.8582 1.4651 1.8722 -0.2227 -0.1763 -0.5424 56  LEU   P CG  
26973 C  CD1 . LEU   P  57  ? 1.8940 1.4644 1.8318 -0.1502 -0.1594 -0.5329 56  LEU   P CD1 
26974 C  CD2 . LEU   P  57  ? 1.8775 1.5113 1.8944 -0.2093 -0.1342 -0.5491 56  LEU   P CD2 
26975 N  N   . GLU   P  58  ? 1.8407 1.5991 1.9460 -0.2421 -0.2390 -0.4007 57  GLU   P N   
26976 C  CA  . GLU   P  58  ? 1.9025 1.7224 1.9501 -0.1601 -0.2385 -0.3301 57  GLU   P CA  
26977 C  C   . GLU   P  58  ? 2.0284 1.7740 1.9657 -0.1220 -0.2245 -0.2646 57  GLU   P C   
26978 O  O   . GLU   P  58  ? 2.0071 1.8404 1.9552 -0.0949 -0.2515 -0.1739 57  GLU   P O   
26979 C  CB  . GLU   P  58  ? 1.8478 1.7670 1.9108 -0.0791 -0.2294 -0.3622 57  GLU   P CB  
26980 C  CG  . GLU   P  58  ? 1.7269 1.8615 1.8614 -0.0432 -0.2109 -0.4212 57  GLU   P CG  
26981 C  CD  . GLU   P  58  ? 1.7274 1.9006 1.8314 -0.0236 -0.1616 -0.4496 57  GLU   P CD  
26982 O  OE1 . GLU   P  58  ? 1.5972 2.0114 1.8956 -0.0501 -0.1383 -0.4838 57  GLU   P OE1 
26983 O  OE2 . GLU   P  58  ? 1.5670 1.8135 1.8038 -0.0436 -0.2150 -0.4673 57  GLU   P OE2 
26984 N  N   . GLN   P  59  ? 2.1478 1.8831 1.9018 -0.1518 -0.2304 -0.2575 58  GLN   P N   
26985 C  CA  . GLN   P  59  ? 2.3149 2.0478 1.9133 -0.1108 -0.1920 -0.2802 58  GLN   P CA  
26986 C  C   . GLN   P  59  ? 2.4153 2.0496 1.9086 -0.0753 -0.2151 -0.2900 58  GLN   P C   
26987 O  O   . GLN   P  59  ? 2.4220 1.9556 1.8195 -0.0550 -0.2362 -0.3632 58  GLN   P O   
26988 C  CB  . GLN   P  59  ? 2.3290 2.1501 1.9947 -0.1826 -0.2006 -0.2718 58  GLN   P CB  
26989 C  CG  . GLN   P  59  ? 2.4127 2.2137 2.1171 -0.1126 -0.1380 -0.2995 58  GLN   P CG  
26990 C  CD  . GLN   P  59  ? 2.4921 2.3114 2.2020 -0.0446 -0.1411 -0.2157 58  GLN   P CD  
26991 O  OE1 . GLN   P  59  ? 2.5017 2.3602 2.3491 -0.0075 -0.0521 -0.2095 58  GLN   P OE1 
26992 N  NE2 . GLN   P  59  ? 2.4606 2.4030 2.3419 -0.0275 -0.1280 -0.1624 58  GLN   P NE2 
26993 N  N   . ASP   P  60  ? 2.4334 2.2021 1.9684 -0.0027 -0.1355 -0.2302 59  ASP   P N   
26994 C  CA  . ASP   P  60  ? 2.4584 2.2677 2.0508 -0.0028 -0.1143 -0.1468 59  ASP   P CA  
26995 C  C   . ASP   P  60  ? 2.5349 2.3037 2.0935 -0.0140 -0.1892 -0.1832 59  ASP   P C   
26996 O  O   . ASP   P  60  ? 2.6176 2.3542 2.0459 0.0048  -0.2109 -0.1413 59  ASP   P O   
26997 C  CB  . ASP   P  60  ? 2.4397 2.3124 2.0224 -0.0335 -0.0384 -0.1001 59  ASP   P CB  
26998 C  CG  . ASP   P  60  ? 2.3105 2.2588 2.0671 0.0163  0.0197  -0.0873 59  ASP   P CG  
26999 O  OD1 . ASP   P  60  ? 2.3493 2.2275 1.9490 0.0117  0.0887  0.0077  59  ASP   P OD1 
27000 O  OD2 . ASP   P  60  ? 2.3427 2.1289 1.9542 0.0415  0.0854  -0.1450 59  ASP   P OD2 
27001 N  N   . THR   P  61  ? 2.5064 2.2257 2.1228 -0.0603 -0.2325 -0.2347 60  THR   P N   
27002 C  CA  . THR   P  61  ? 2.4077 2.1424 2.1666 0.0041  -0.1819 -0.2537 60  THR   P CA  
27003 C  C   . THR   P  61  ? 2.4224 1.9822 2.2475 0.0148  -0.2055 -0.2793 60  THR   P C   
27004 O  O   . THR   P  61  ? 2.2529 1.5684 2.3223 0.1280  -0.1434 -0.3626 60  THR   P O   
27005 C  CB  . THR   P  61  ? 2.4627 2.1930 2.1080 -0.0488 -0.1587 -0.1503 60  THR   P CB  
27006 O  OG1 . THR   P  61  ? 2.4542 2.1559 1.9259 -0.1134 -0.1353 -0.2029 60  THR   P OG1 
27007 C  CG2 . THR   P  61  ? 2.4524 2.3101 2.0532 -0.0338 -0.1107 -0.1577 60  THR   P CG2 
27008 N  N   . SER   P  62  ? 2.3440 2.0281 2.1986 0.0698  -0.2053 -0.2533 61  SER   P N   
27009 C  CA  . SER   P  62  ? 2.3207 2.1086 2.1584 0.0870  -0.2362 -0.1483 61  SER   P CA  
27010 C  C   . SER   P  62  ? 2.3086 2.0405 2.1962 0.0116  -0.2736 -0.1095 61  SER   P C   
27011 O  O   . SER   P  62  ? 2.3169 2.1549 2.2252 -0.0292 -0.3680 -0.1640 61  SER   P O   
27012 C  CB  . SER   P  62  ? 2.3150 2.1181 2.0869 0.1035  -0.2447 -0.1442 61  SER   P CB  
27013 O  OG  . SER   P  62  ? 2.3299 2.2169 2.0154 0.1596  -0.3130 -0.1252 61  SER   P OG  
27014 N  N   . THR   P  63  ? 2.3009 1.9107 2.1832 0.0041  -0.2375 -0.0038 62  THR   P N   
27015 C  CA  . THR   P  63  ? 2.3681 1.7965 2.1187 0.0340  -0.2460 0.0607  62  THR   P CA  
27016 C  C   . THR   P  63  ? 2.3928 1.6177 1.9966 0.0061  -0.2211 0.0352  62  THR   P C   
27017 O  O   . THR   P  63  ? 2.4510 1.6644 2.0930 -0.0468 -0.3180 0.1149  62  THR   P O   
27018 C  CB  . THR   P  63  ? 2.4023 1.7880 2.0876 0.0836  -0.1282 0.1306  62  THR   P CB  
27019 O  OG1 . THR   P  63  ? 2.4953 1.7282 2.1277 0.1375  -0.1015 0.2182  62  THR   P OG1 
27020 C  CG2 . THR   P  63  ? 2.4132 1.8614 2.0549 0.1189  -0.1298 0.1066  62  THR   P CG2 
27021 N  N   . GLU   P  64  ? 2.3005 1.5732 1.8578 -0.0188 -0.3121 0.0703  63  GLU   P N   
27022 C  CA  . GLU   P  64  ? 2.2925 1.6093 1.7893 -0.0069 -0.2915 0.0574  63  GLU   P CA  
27023 C  C   . GLU   P  64  ? 2.1609 1.4036 1.7175 -0.0614 -0.3813 0.0860  63  GLU   P C   
27024 O  O   . GLU   P  64  ? 2.1493 1.4743 1.7327 -0.0744 -0.3583 0.1195  63  GLU   P O   
27025 C  CB  . GLU   P  64  ? 2.3918 1.6908 1.8703 -0.0640 -0.3035 0.1539  63  GLU   P CB  
27026 C  CG  . GLU   P  64  ? 2.4334 1.8612 1.9001 0.0305  -0.3319 0.2785  63  GLU   P CG  
27027 C  CD  . GLU   P  64  ? 2.4609 1.9650 1.9066 -0.0640 -0.3026 0.3411  63  GLU   P CD  
27028 O  OE1 . GLU   P  64  ? 2.5828 2.0389 1.8539 0.0402  -0.3695 0.3234  63  GLU   P OE1 
27029 O  OE2 . GLU   P  64  ? 2.5430 2.1802 1.8524 -0.1007 -0.2155 0.5191  63  GLU   P OE2 
27030 N  N   . LYS   P  65  ? 2.0934 1.1452 1.7043 -0.0418 -0.3682 0.0318  64  LYS   P N   
27031 C  CA  . LYS   P  65  ? 2.1017 0.9327 1.6916 0.0314  -0.3859 0.0593  64  LYS   P CA  
27032 C  C   . LYS   P  65  ? 1.9394 0.7602 1.6245 0.0122  -0.4756 -0.0839 64  LYS   P C   
27033 O  O   . LYS   P  65  ? 1.9002 0.3892 1.5361 0.0424  -0.5227 -0.0841 64  LYS   P O   
27034 C  CB  . LYS   P  65  ? 2.0914 1.0486 1.7653 0.0243  -0.3660 0.0088  64  LYS   P CB  
27035 C  CG  . LYS   P  65  ? 2.1409 1.0951 1.8306 0.1040  -0.2838 0.0828  64  LYS   P CG  
27036 C  CD  . LYS   P  65  ? 2.1555 1.0207 1.8429 0.1364  -0.2969 0.1283  64  LYS   P CD  
27037 C  CE  . LYS   P  65  ? 2.1186 0.9978 1.8686 0.1774  -0.2560 0.1000  64  LYS   P CE  
27038 N  NZ  . LYS   P  65  ? 2.1386 0.9170 1.8745 0.1741  -0.2623 0.0637  64  LYS   P NZ  
27039 N  N   . LEU   P  66  ? 1.9165 0.7992 1.5855 0.0105  -0.4970 -0.0613 65  LEU   P N   
27040 C  CA  . LEU   P  66  ? 1.8958 0.8365 1.4935 0.0217  -0.5197 -0.0722 65  LEU   P CA  
27041 C  C   . LEU   P  66  ? 1.8824 0.7655 1.4597 0.0872  -0.5126 -0.0260 65  LEU   P C   
27042 O  O   . LEU   P  66  ? 1.8526 0.6833 1.5073 0.1642  -0.5240 -0.0136 65  LEU   P O   
27043 C  CB  . LEU   P  66  ? 1.9045 0.8842 1.4775 0.0077  -0.5301 -0.0397 65  LEU   P CB  
27044 C  CG  . LEU   P  66  ? 1.9082 0.8777 1.4826 -0.0172 -0.5417 -0.0454 65  LEU   P CG  
27045 C  CD1 . LEU   P  66  ? 1.9101 0.8665 1.4584 -0.0244 -0.5464 -0.0525 65  LEU   P CD1 
27046 C  CD2 . LEU   P  66  ? 1.8997 0.9350 1.5193 -0.0124 -0.5323 -0.0527 65  LEU   P CD2 
27047 N  N   . TYR   P  67  ? 1.8831 0.7325 1.3663 0.1052  -0.5259 -0.0176 66  TYR   P N   
27048 C  CA  . TYR   P  67  ? 1.9115 0.7826 1.3347 0.1107  -0.5209 -0.0557 66  TYR   P CA  
27049 C  C   . TYR   P  67  ? 1.8677 0.7598 1.2763 0.0988  -0.5484 -0.0911 66  TYR   P C   
27050 O  O   . TYR   P  67  ? 1.8812 0.7101 1.2314 0.0962  -0.5832 -0.0841 66  TYR   P O   
27051 C  CB  . TYR   P  67  ? 1.9140 0.8271 1.3032 0.1086  -0.5110 -0.0900 66  TYR   P CB  
27052 C  CG  . TYR   P  67  ? 1.9460 0.9329 1.2221 0.1110  -0.4865 -0.0982 66  TYR   P CG  
27053 C  CD1 . TYR   P  67  ? 1.9423 0.9639 1.2390 0.1499  -0.4679 -0.1092 66  TYR   P CD1 
27054 C  CD2 . TYR   P  67  ? 1.9842 0.9346 1.2345 0.0997  -0.5057 -0.1554 66  TYR   P CD2 
27055 C  CE1 . TYR   P  67  ? 1.9826 1.0379 1.2253 0.1345  -0.4536 -0.0910 66  TYR   P CE1 
27056 C  CE2 . TYR   P  67  ? 1.9945 1.0235 1.2310 0.1045  -0.4848 -0.1249 66  TYR   P CE2 
27057 C  CZ  . TYR   P  67  ? 1.9974 1.0493 1.2302 0.1432  -0.4536 -0.0954 66  TYR   P CZ  
27058 O  OH  . TYR   P  67  ? 2.0401 1.1797 1.2488 0.1220  -0.4189 -0.0331 66  TYR   P OH  
27059 N  N   . LYS   P  68  ? 1.8447 0.7531 1.2937 0.0762  -0.5368 -0.0969 67  LYS   P N   
27060 C  CA  . LYS   P  68  ? 1.8197 0.7601 1.3048 0.0833  -0.5114 -0.0858 67  LYS   P CA  
27061 C  C   . LYS   P  68  ? 1.8298 0.6573 1.2814 0.0803  -0.4763 -0.0680 67  LYS   P C   
27062 O  O   . LYS   P  68  ? 1.8366 0.5596 1.2841 0.0693  -0.4251 -0.1042 67  LYS   P O   
27063 C  CB  . LYS   P  68  ? 1.8218 0.8282 1.3794 0.1043  -0.4809 -0.0817 67  LYS   P CB  
27064 C  CG  . LYS   P  68  ? 1.8176 0.8715 1.4487 0.1461  -0.4465 -0.0398 67  LYS   P CG  
27065 C  CD  . LYS   P  68  ? 1.8121 1.0304 1.5504 0.1518  -0.3848 -0.0658 67  LYS   P CD  
27066 C  CE  . LYS   P  68  ? 1.7630 1.0235 1.6236 0.1672  -0.3429 -0.0712 67  LYS   P CE  
27067 N  NZ  . LYS   P  68  ? 1.7464 1.1188 1.6837 0.1859  -0.3422 -0.0569 67  LYS   P NZ  
27068 N  N   . LEU   P  69  ? 1.8335 0.6136 1.2119 0.0850  -0.5150 -0.0612 68  LEU   P N   
27069 C  CA  . LEU   P  69  ? 1.8380 0.6613 1.2058 0.0699  -0.4936 -0.0750 68  LEU   P CA  
27070 C  C   . LEU   P  69  ? 1.8929 0.6612 1.2898 0.0598  -0.4763 -0.0753 68  LEU   P C   
27071 O  O   . LEU   P  69  ? 1.8854 0.7403 1.2415 0.0384  -0.5074 -0.0460 68  LEU   P O   
27072 C  CB  . LEU   P  69  ? 1.8638 0.6243 1.1627 0.0666  -0.4977 -0.0721 68  LEU   P CB  
27073 C  CG  . LEU   P  69  ? 1.8849 0.6024 1.1601 0.0423  -0.4560 -0.0934 68  LEU   P CG  
27074 C  CD1 . LEU   P  69  ? 1.8833 0.5810 1.1435 0.0059  -0.4511 -0.1028 68  LEU   P CD1 
27075 C  CD2 . LEU   P  69  ? 1.9035 0.5981 1.1693 0.0539  -0.4383 -0.0678 68  LEU   P CD2 
27076 N  N   . ASN   P  70  ? 1.8661 0.6570 1.2980 0.0207  -0.5137 -0.1491 69  ASN   P N   
27077 C  CA  . ASN   P  70  ? 1.8973 0.5843 1.3753 -0.0309 -0.4500 -0.1699 69  ASN   P CA  
27078 C  C   . ASN   P  70  ? 1.9110 0.6450 1.4124 0.0299  -0.4741 -0.1655 69  ASN   P C   
27079 O  O   . ASN   P  70  ? 1.9308 0.7026 1.4615 -0.0320 -0.4620 -0.1890 69  ASN   P O   
27080 C  CB  . ASN   P  70  ? 1.8994 0.5248 1.3556 -0.0317 -0.4616 -0.1909 69  ASN   P CB  
27081 C  CG  . ASN   P  70  ? 1.8707 0.4136 1.3750 -0.0922 -0.4485 -0.2275 69  ASN   P CG  
27082 O  OD1 . ASN   P  70  ? 1.8322 0.3552 1.3346 -0.0768 -0.4021 -0.1902 69  ASN   P OD1 
27083 N  ND2 . ASN   P  70  ? 1.9020 0.4387 1.4005 -0.1123 -0.4216 -0.2362 69  ASN   P ND2 
27084 N  N   . ASP   P  71  ? 1.9714 0.5987 1.4812 0.0521  -0.4170 -0.1762 70  ASP   P N   
27085 C  CA  . ASP   P  71  ? 1.9451 0.6436 1.4949 0.0672  -0.3840 -0.1626 70  ASP   P CA  
27086 C  C   . ASP   P  71  ? 1.9160 0.4276 1.4834 0.0584  -0.4170 -0.1120 70  ASP   P C   
27087 O  O   . ASP   P  71  ? 1.9321 0.3318 1.4628 0.0403  -0.4230 -0.1202 70  ASP   P O   
27088 C  CB  . ASP   P  71  ? 1.9836 0.6952 1.5380 0.1339  -0.3164 -0.1732 70  ASP   P CB  
27089 C  CG  . ASP   P  71  ? 2.0247 0.9156 1.5696 0.1175  -0.2279 -0.1941 70  ASP   P CG  
27090 O  OD1 . ASP   P  71  ? 2.0199 1.0639 1.5159 0.0898  -0.1538 -0.2256 70  ASP   P OD1 
27091 O  OD2 . ASP   P  71  ? 2.0759 0.9127 1.6165 0.1591  -0.1207 -0.2320 70  ASP   P OD2 
27092 N  N   . LYS   P  72  ? 1.9339 0.4259 1.4683 0.0592  -0.3924 -0.0785 71  LYS   P N   
27093 C  CA  . LYS   P  72  ? 1.9552 0.5477 1.4502 0.0494  -0.3990 -0.0818 71  LYS   P CA  
27094 C  C   . LYS   P  72  ? 1.9230 0.5680 1.3880 0.0552  -0.3974 -0.0856 71  LYS   P C   
27095 O  O   . LYS   P  72  ? 1.9836 0.5662 1.3727 0.0663  -0.3701 -0.0666 71  LYS   P O   
27096 C  CB  . LYS   P  72  ? 1.9926 0.5502 1.5069 0.0564  -0.3810 -0.0538 71  LYS   P CB  
27097 C  CG  . LYS   P  72  ? 2.0663 0.5879 1.6053 0.1021  -0.3794 -0.0257 71  LYS   P CG  
27098 C  CD  . LYS   P  72  ? 2.0956 0.6947 1.6374 0.0537  -0.4060 -0.0063 71  LYS   P CD  
27099 C  CE  . LYS   P  72  ? 2.1483 0.6612 1.7005 0.0315  -0.3959 0.0513  71  LYS   P CE  
27100 N  NZ  . LYS   P  72  ? 2.2195 0.5924 1.7733 0.0003  -0.4084 0.0408  71  LYS   P NZ  
27101 N  N   . ILE   P  73  ? 1.8541 0.5580 1.4083 0.0552  -0.4202 -0.0978 72  ILE   P N   
27102 C  CA  . ILE   P  73  ? 1.8107 0.4924 1.4165 0.0013  -0.4189 -0.1427 72  ILE   P CA  
27103 C  C   . ILE   P  73  ? 1.7714 0.4521 1.4995 -0.0444 -0.4230 -0.1214 72  ILE   P C   
27104 O  O   . ILE   P  73  ? 1.7713 0.3008 1.5813 -0.1063 -0.3929 -0.1387 72  ILE   P O   
27105 C  CB  . ILE   P  73  ? 1.7948 0.4631 1.3968 0.0394  -0.4004 -0.1354 72  ILE   P CB  
27106 C  CG1 . ILE   P  73  ? 1.8133 0.4989 1.3834 0.0673  -0.4190 -0.0968 72  ILE   P CG1 
27107 C  CG2 . ILE   P  73  ? 1.8198 0.4329 1.3927 0.0358  -0.3867 -0.1734 72  ILE   P CG2 
27108 C  CD1 . ILE   P  73  ? 1.7914 0.5157 1.3935 0.0605  -0.4113 -0.0387 72  ILE   P CD1 
27109 N  N   . ALA   P  74  ? 1.7567 0.4623 1.4430 -0.0488 -0.4570 -0.1385 73  ALA   P N   
27110 C  CA  . ALA   P  74  ? 1.7809 0.4604 1.4685 -0.0710 -0.4692 -0.1275 73  ALA   P CA  
27111 C  C   . ALA   P  74  ? 1.7758 0.4554 1.4470 -0.0822 -0.4597 -0.1214 73  ALA   P C   
27112 O  O   . ALA   P  74  ? 1.7588 0.4563 1.3816 -0.0963 -0.5199 -0.1418 73  ALA   P O   
27113 C  CB  . ALA   P  74  ? 1.7848 0.4167 1.4631 -0.0735 -0.4812 -0.1224 73  ALA   P CB  
27114 N  N   . VAL   P  75  ? 1.8084 0.5270 1.4575 -0.1056 -0.4423 -0.0815 74  VAL   P N   
27115 C  CA  . VAL   P  75  ? 1.8457 0.4955 1.4217 -0.1187 -0.4389 -0.0946 74  VAL   P CA  
27116 C  C   . VAL   P  75  ? 1.8652 0.4774 1.4275 -0.1123 -0.4215 -0.1078 74  VAL   P C   
27117 O  O   . VAL   P  75  ? 1.8571 0.3765 1.4033 -0.1185 -0.4407 -0.1174 74  VAL   P O   
27118 C  CB  . VAL   P  75  ? 1.8572 0.5588 1.4065 -0.1716 -0.4384 -0.0542 74  VAL   P CB  
27119 C  CG1 . VAL   P  75  ? 1.8631 0.5862 1.3627 -0.1744 -0.4370 -0.0563 74  VAL   P CG1 
27120 C  CG2 . VAL   P  75  ? 1.8801 0.5908 1.4229 -0.1789 -0.4074 -0.0555 74  VAL   P CG2 
27121 N  N   . ALA   P  76  ? 1.8805 0.4862 1.4452 -0.0716 -0.4005 -0.1052 75  ALA   P N   
27122 C  CA  . ALA   P  76  ? 1.8364 0.4260 1.4305 -0.0516 -0.4217 -0.1613 75  ALA   P CA  
27123 C  C   . ALA   P  76  ? 1.8534 0.3695 1.4085 -0.0419 -0.4088 -0.1576 75  ALA   P C   
27124 O  O   . ALA   P  76  ? 1.8640 0.2492 1.3920 -0.0335 -0.3990 -0.1736 75  ALA   P O   
27125 C  CB  . ALA   P  76  ? 1.8011 0.4257 1.4353 -0.0727 -0.4327 -0.1458 75  ALA   P CB  
27126 N  N   . VAL   P  77  ? 1.8034 0.4487 1.3735 -0.0321 -0.4431 -0.1560 76  VAL   P N   
27127 C  CA  . VAL   P  77  ? 1.7811 0.5804 1.3918 -0.0056 -0.4387 -0.1426 76  VAL   P CA  
27128 C  C   . VAL   P  77  ? 1.7411 0.5845 1.3733 0.0225  -0.4560 -0.1418 76  VAL   P C   
27129 O  O   . VAL   P  77  ? 1.6705 0.7379 1.3509 0.0563  -0.4795 -0.1281 76  VAL   P O   
27130 C  CB  . VAL   P  77  ? 1.7882 0.5469 1.3960 0.0037  -0.4177 -0.1296 76  VAL   P CB  
27131 C  CG1 . VAL   P  77  ? 1.7830 0.5605 1.4011 0.0000  -0.4165 -0.1201 76  VAL   P CG1 
27132 C  CG2 . VAL   P  77  ? 1.7979 0.5441 1.4264 0.0156  -0.4070 -0.1065 76  VAL   P CG2 
27133 N  N   . ALA   P  78  ? 1.7240 0.6954 1.3884 0.0369  -0.4423 -0.1398 77  ALA   P N   
27134 C  CA  . ALA   P  78  ? 1.7168 0.7191 1.4104 0.0668  -0.4212 -0.0989 77  ALA   P CA  
27135 C  C   . ALA   P  78  ? 1.7074 0.7063 1.3871 0.0779  -0.4003 -0.0594 77  ALA   P C   
27136 O  O   . ALA   P  78  ? 1.7201 0.7845 1.3633 0.0749  -0.3771 -0.0486 77  ALA   P O   
27137 C  CB  . ALA   P  78  ? 1.7280 0.7470 1.4205 0.0869  -0.4156 -0.1096 77  ALA   P CB  
27138 N  N   . GLY   P  79  ? 1.7125 0.6942 1.4191 0.0876  -0.3772 -0.0346 78  GLY   P N   
27139 C  CA  . GLY   P  79  ? 1.6945 0.7238 1.4102 0.0965  -0.3611 -0.0460 78  GLY   P CA  
27140 C  C   . GLY   P  79  ? 1.6517 0.7203 1.4213 0.1116  -0.3365 -0.0393 78  GLY   P C   
27141 O  O   . GLY   P  79  ? 1.6682 0.7383 1.4332 0.1972  -0.2787 -0.0994 78  GLY   P O   
27142 N  N   . LEU   P  80  ? 1.6973 0.6897 1.4099 0.0786  -0.3558 -0.0014 79  LEU   P N   
27143 C  CA  . LEU   P  80  ? 1.7352 0.7162 1.3922 0.0273  -0.3337 0.0306  79  LEU   P CA  
27144 C  C   . LEU   P  80  ? 1.7187 0.7228 1.3782 0.0138  -0.3809 0.0861  79  LEU   P C   
27145 O  O   . LEU   P  80  ? 1.7361 0.8390 1.3639 -0.0001 -0.3805 0.1489  79  LEU   P O   
27146 C  CB  . LEU   P  80  ? 1.7446 0.7272 1.4147 0.0023  -0.3412 0.0480  79  LEU   P CB  
27147 C  CG  . LEU   P  80  ? 1.8044 0.7363 1.4005 -0.0009 -0.3391 0.0942  79  LEU   P CG  
27148 C  CD1 . LEU   P  80  ? 1.8441 0.7800 1.4165 -0.0371 -0.3208 0.1209  79  LEU   P CD1 
27149 C  CD2 . LEU   P  80  ? 1.7904 0.7745 1.4240 -0.0293 -0.3307 0.0930  79  LEU   P CD2 
27150 N  N   . THR   P  81  ? 1.6939 0.6922 1.3673 -0.0082 -0.4060 0.0851  80  THR   P N   
27151 C  CA  . THR   P  81  ? 1.7084 0.7029 1.4058 0.0054  -0.4065 0.0290  80  THR   P CA  
27152 C  C   . THR   P  81  ? 1.7384 0.7154 1.3624 0.0319  -0.4218 0.0070  80  THR   P C   
27153 O  O   . THR   P  81  ? 1.7845 0.6535 1.4365 0.0016  -0.3929 -0.0541 80  THR   P O   
27154 C  CB  . THR   P  81  ? 1.7256 0.7178 1.4483 -0.0204 -0.3817 0.0239  80  THR   P CB  
27155 O  OG1 . THR   P  81  ? 1.8043 0.5944 1.5091 -0.0141 -0.3273 0.0238  80  THR   P OG1 
27156 C  CG2 . THR   P  81  ? 1.7144 0.7527 1.4810 0.0074  -0.3530 0.0000  80  THR   P CG2 
27157 N  N   . ALA   P  82  ? 1.7521 0.6924 1.3195 0.0256  -0.4206 -0.0501 81  ALA   P N   
27158 C  CA  . ALA   P  82  ? 1.7675 0.6699 1.2915 0.0550  -0.4117 -0.0707 81  ALA   P CA  
27159 C  C   . ALA   P  82  ? 1.7665 0.5745 1.2785 0.0428  -0.4460 -0.0764 81  ALA   P C   
27160 O  O   . ALA   P  82  ? 1.7869 0.5665 1.2643 0.0953  -0.4331 -0.1193 81  ALA   P O   
27161 C  CB  . ALA   P  82  ? 1.7696 0.7329 1.2517 0.0444  -0.4058 -0.0830 81  ALA   P CB  
27162 N  N   . ASP   P  83  ? 1.7861 0.5740 1.3098 0.0409  -0.4543 -0.0994 82  ASP   P N   
27163 C  CA  . ASP   P  83  ? 1.7899 0.5533 1.3432 0.0270  -0.4584 -0.0902 82  ASP   P CA  
27164 C  C   . ASP   P  83  ? 1.7790 0.5318 1.3724 0.0426  -0.4496 -0.0862 82  ASP   P C   
27165 O  O   . ASP   P  83  ? 1.7749 0.5814 1.3770 0.0304  -0.4137 -0.0717 82  ASP   P O   
27166 C  CB  . ASP   P  83  ? 1.8123 0.5866 1.3683 0.0409  -0.4716 -0.1226 82  ASP   P CB  
27167 C  CG  . ASP   P  83  ? 1.8393 0.6285 1.3905 0.0546  -0.5029 -0.1265 82  ASP   P CG  
27168 O  OD1 . ASP   P  83  ? 1.8733 0.6039 1.4190 0.0635  -0.4873 -0.1973 82  ASP   P OD1 
27169 O  OD2 . ASP   P  83  ? 1.8433 0.7193 1.4611 0.1186  -0.5111 -0.1367 82  ASP   P OD2 
27170 N  N   . ALA   P  84  ? 1.7664 0.4972 1.3884 0.0395  -0.4499 -0.0438 83  ALA   P N   
27171 C  CA  . ALA   P  84  ? 1.7933 0.5735 1.3934 0.0315  -0.4490 -0.0041 83  ALA   P CA  
27172 C  C   . ALA   P  84  ? 1.7822 0.6174 1.3780 0.0746  -0.4473 -0.0209 83  ALA   P C   
27173 O  O   . ALA   P  84  ? 1.8302 0.6580 1.4501 0.0840  -0.4418 0.0340  83  ALA   P O   
27174 C  CB  . ALA   P  84  ? 1.8208 0.5268 1.4065 0.0210  -0.4398 -0.0191 83  ALA   P CB  
27175 N  N   . GLU   P  85  ? 1.7316 0.6435 1.3620 0.0699  -0.4615 -0.0006 84  GLU   P N   
27176 C  CA  . GLU   P  85  ? 1.6786 0.6304 1.3669 0.0465  -0.4610 -0.0040 84  GLU   P CA  
27177 C  C   . GLU   P  85  ? 1.6766 0.5614 1.3677 0.0717  -0.4755 -0.0142 84  GLU   P C   
27178 O  O   . GLU   P  85  ? 1.6377 0.5545 1.3403 0.0014  -0.5281 -0.0095 84  GLU   P O   
27179 C  CB  . GLU   P  85  ? 1.7136 0.7254 1.3836 0.0656  -0.4354 0.0037  84  GLU   P CB  
27180 C  CG  . GLU   P  85  ? 1.7189 0.8182 1.4236 0.0355  -0.4182 0.0010  84  GLU   P CG  
27181 C  CD  . GLU   P  85  ? 1.7449 0.9157 1.4665 0.0309  -0.3817 0.0038  84  GLU   P CD  
27182 O  OE1 . GLU   P  85  ? 1.7643 0.9676 1.4848 -0.0003 -0.3987 -0.0268 84  GLU   P OE1 
27183 O  OE2 . GLU   P  85  ? 1.7662 0.9532 1.5235 -0.0217 -0.3857 -0.0231 84  GLU   P OE2 
27184 N  N   . ILE   P  86  ? 1.6613 0.4100 1.4075 0.0555  -0.4540 -0.0221 85  ILE   P N   
27185 C  CA  . ILE   P  86  ? 1.6576 0.4033 1.4104 0.0615  -0.4552 -0.0245 85  ILE   P CA  
27186 C  C   . ILE   P  86  ? 1.6290 0.4983 1.3825 0.0895  -0.4664 -0.0207 85  ILE   P C   
27187 O  O   . ILE   P  86  ? 1.6232 0.5340 1.4959 0.0359  -0.4313 0.0651  85  ILE   P O   
27188 C  CB  . ILE   P  86  ? 1.6684 0.3560 1.3911 0.0521  -0.4479 -0.0339 85  ILE   P CB  
27189 C  CG1 . ILE   P  86  ? 1.6937 0.3443 1.4109 0.0354  -0.4297 -0.0130 85  ILE   P CG1 
27190 C  CG2 . ILE   P  86  ? 1.6521 0.3914 1.3851 0.0640  -0.4413 -0.0390 85  ILE   P CG2 
27191 C  CD1 . ILE   P  86  ? 1.7270 0.3640 1.3985 0.0768  -0.4007 -0.0184 85  ILE   P CD1 
27192 N  N   . LEU   P  87  ? 1.5998 0.4263 1.3593 0.0814  -0.4829 0.0139  86  LEU   P N   
27193 C  CA  . LEU   P  87  ? 1.6371 0.4632 1.3562 0.0688  -0.4746 0.0048  86  LEU   P CA  
27194 C  C   . LEU   P  87  ? 1.6630 0.5090 1.3783 0.1072  -0.4659 0.0038  86  LEU   P C   
27195 O  O   . LEU   P  87  ? 1.6513 0.5238 1.3491 0.0920  -0.4469 -0.0123 86  LEU   P O   
27196 C  CB  . LEU   P  87  ? 1.6117 0.4034 1.3648 0.0742  -0.5003 0.0418  86  LEU   P CB  
27197 C  CG  . LEU   P  87  ? 1.6414 0.3767 1.3184 0.0669  -0.5340 0.0627  86  LEU   P CG  
27198 C  CD1 . LEU   P  87  ? 1.6406 0.3602 1.3524 0.0725  -0.5353 0.0611  86  LEU   P CD1 
27199 C  CD2 . LEU   P  87  ? 1.6215 0.3678 1.2777 0.0869  -0.5627 0.0758  86  LEU   P CD2 
27200 N  N   . ILE   P  88  ? 1.7075 0.5635 1.4019 0.0660  -0.4165 0.0135  87  ILE   P N   
27201 C  CA  . ILE   P  88  ? 1.7628 0.5817 1.3975 0.0838  -0.4338 0.0441  87  ILE   P CA  
27202 C  C   . ILE   P  88  ? 1.8335 0.6030 1.4384 0.0645  -0.4159 0.0122  87  ILE   P C   
27203 O  O   . ILE   P  88  ? 1.8936 0.5946 1.4763 0.0518  -0.3960 0.0290  87  ILE   P O   
27204 C  CB  . ILE   P  88  ? 1.7787 0.5886 1.3754 0.0700  -0.4361 0.0693  87  ILE   P CB  
27205 C  CG1 . ILE   P  88  ? 1.7922 0.5685 1.3965 0.0474  -0.4658 0.0876  87  ILE   P CG1 
27206 C  CG2 . ILE   P  88  ? 1.7573 0.6504 1.3506 0.0829  -0.4406 0.0770  87  ILE   P CG2 
27207 C  CD1 . ILE   P  88  ? 1.7872 0.6242 1.4234 0.0146  -0.4582 0.0696  87  ILE   P CD1 
27208 N  N   . ASN   P  89  ? 1.8435 0.5085 1.4363 0.0484  -0.4100 0.0052  88  ASN   P N   
27209 C  CA  . ASN   P  89  ? 1.8424 0.4763 1.4564 0.0145  -0.3909 0.0270  88  ASN   P CA  
27210 C  C   . ASN   P  89  ? 1.7683 0.4294 1.4754 -0.0042 -0.4457 -0.0501 88  ASN   P C   
27211 O  O   . ASN   P  89  ? 1.7358 0.4439 1.5689 -0.0031 -0.4911 -0.0113 88  ASN   P O   
27212 C  CB  . ASN   P  89  ? 1.9096 0.4765 1.4511 0.0347  -0.3484 0.0313  88  ASN   P CB  
27213 C  CG  . ASN   P  89  ? 1.9384 0.5090 1.5089 0.0725  -0.3087 0.0316  88  ASN   P CG  
27214 O  OD1 . ASN   P  89  ? 2.0543 0.3128 1.4777 0.0102  -0.2619 0.1002  88  ASN   P OD1 
27215 N  ND2 . ASN   P  89  ? 1.9602 0.5568 1.5391 0.0441  -0.2818 0.0573  88  ASN   P ND2 
27216 N  N   . THR   P  90  ? 1.7573 0.2864 1.4365 -0.0435 -0.4658 -0.0705 89  THR   P N   
27217 C  CA  . THR   P  90  ? 1.7728 0.2823 1.4073 -0.0443 -0.4592 -0.0865 89  THR   P CA  
27218 C  C   . THR   P  90  ? 1.7656 0.3659 1.3879 -0.0457 -0.4804 -0.1111 89  THR   P C   
27219 O  O   . THR   P  90  ? 1.7923 0.4280 1.3369 -0.0512 -0.4324 -0.0180 89  THR   P O   
27220 C  CB  . THR   P  90  ? 1.8042 0.2586 1.4360 -0.0374 -0.4550 -0.0643 89  THR   P CB  
27221 O  OG1 . THR   P  90  ? 1.8464 0.1776 1.4314 -0.0687 -0.4359 -0.0393 89  THR   P OG1 
27222 C  CG2 . THR   P  90  ? 1.8191 0.2983 1.4572 -0.0291 -0.4258 -0.0756 89  THR   P CG2 
27223 N  N   . ALA   P  91  ? 1.7902 0.4096 1.3597 -0.0445 -0.4932 -0.1227 90  ALA   P N   
27224 C  CA  . ALA   P  91  ? 1.8418 0.4368 1.3413 -0.0239 -0.4839 -0.1325 90  ALA   P CA  
27225 C  C   . ALA   P  91  ? 1.8463 0.4084 1.2879 -0.0371 -0.4826 -0.1451 90  ALA   P C   
27226 O  O   . ALA   P  91  ? 1.8832 0.4915 1.2646 -0.0639 -0.4762 -0.1192 90  ALA   P O   
27227 C  CB  . ALA   P  91  ? 1.8387 0.4584 1.3345 -0.0298 -0.4830 -0.1404 90  ALA   P CB  
27228 N  N   . ARG   P  92  ? 1.8356 0.4189 1.2921 -0.0106 -0.4814 -0.1682 91  ARG   P N   
27229 C  CA  . ARG   P  92  ? 1.8090 0.4857 1.3147 0.0061  -0.4733 -0.1837 91  ARG   P CA  
27230 C  C   . ARG   P  92  ? 1.8363 0.4459 1.3466 0.0252  -0.4861 -0.1514 91  ARG   P C   
27231 O  O   . ARG   P  92  ? 1.9361 0.2901 1.4273 -0.0165 -0.4412 -0.1827 91  ARG   P O   
27232 C  CB  . ARG   P  92  ? 1.7823 0.5362 1.3100 0.0140  -0.4733 -0.2056 91  ARG   P CB  
27233 C  CG  . ARG   P  92  ? 1.7495 0.5554 1.3025 0.0318  -0.4697 -0.2328 91  ARG   P CG  
27234 C  CD  . ARG   P  92  ? 1.7171 0.5817 1.3223 0.0480  -0.4451 -0.2612 91  ARG   P CD  
27235 N  NE  . ARG   P  92  ? 1.6914 0.5818 1.3198 0.0699  -0.4480 -0.2793 91  ARG   P NE  
27236 C  CZ  . ARG   P  92  ? 1.6613 0.5883 1.3607 0.0572  -0.4405 -0.3000 91  ARG   P CZ  
27237 N  NH1 . ARG   P  92  ? 1.7009 0.6348 1.3556 0.0792  -0.4095 -0.3013 91  ARG   P NH1 
27238 N  NH2 . ARG   P  92  ? 1.6481 0.6227 1.3821 0.0644  -0.4604 -0.3071 91  ARG   P NH2 
27239 N  N   . ILE   P  93  ? 1.7989 0.4473 1.3876 0.0121  -0.4867 -0.1630 92  ILE   P N   
27240 C  CA  . ILE   P  93  ? 1.7788 0.4544 1.3838 0.0245  -0.5099 -0.1726 92  ILE   P CA  
27241 C  C   . ILE   P  93  ? 1.7527 0.4935 1.4187 0.0245  -0.5194 -0.1182 92  ILE   P C   
27242 O  O   . ILE   P  93  ? 1.7575 0.5162 1.4205 0.0055  -0.5324 -0.0779 92  ILE   P O   
27243 C  CB  . ILE   P  93  ? 1.7660 0.4482 1.3355 0.0155  -0.4968 -0.2299 92  ILE   P CB  
27244 C  CG1 . ILE   P  93  ? 1.7747 0.4610 1.3219 0.0175  -0.5017 -0.2530 92  ILE   P CG1 
27245 C  CG2 . ILE   P  93  ? 1.7440 0.4916 1.3250 0.0092  -0.5088 -0.2152 92  ILE   P CG2 
27246 C  CD1 . ILE   P  93  ? 1.7584 0.4376 1.3344 0.0326  -0.4889 -0.2509 92  ILE   P CD1 
27247 N  N   . HIS   P  94  ? 1.7100 0.4451 1.4817 0.0289  -0.5322 -0.0971 93  HIS   P N   
27248 C  CA  . HIS   P  94  ? 1.7333 0.5054 1.4973 -0.0368 -0.5480 -0.0341 93  HIS   P CA  
27249 C  C   . HIS   P  94  ? 1.7289 0.3948 1.4247 -0.0816 -0.5298 -0.0716 93  HIS   P C   
27250 O  O   . HIS   P  94  ? 1.6692 0.5566 1.4061 -0.1417 -0.4921 -0.0532 93  HIS   P O   
27251 C  CB  . HIS   P  94  ? 1.7963 0.6098 1.5768 0.0080  -0.5164 -0.0993 93  HIS   P CB  
27252 C  CG  . HIS   P  94  ? 1.8149 0.8727 1.7289 0.0288  -0.5307 -0.0455 93  HIS   P CG  
27253 N  ND1 . HIS   P  94  ? 1.9211 0.9525 1.8336 -0.0568 -0.5466 -0.0588 93  HIS   P ND1 
27254 C  CD2 . HIS   P  94  ? 1.8829 0.9050 1.7712 0.0472  -0.5255 0.0284  93  HIS   P CD2 
27255 C  CE1 . HIS   P  94  ? 1.9244 0.9857 1.8296 -0.0914 -0.6158 -0.0332 93  HIS   P CE1 
27256 N  NE2 . HIS   P  94  ? 1.9082 0.8940 1.7498 0.1289  -0.6223 0.1083  93  HIS   P NE2 
27257 N  N   . ALA   P  95  ? 1.7398 0.2995 1.3978 -0.0785 -0.5266 -0.0752 94  ALA   P N   
27258 C  CA  . ALA   P  95  ? 1.7694 0.3544 1.3866 -0.0766 -0.5338 -0.0520 94  ALA   P CA  
27259 C  C   . ALA   P  95  ? 1.8092 0.3390 1.3544 -0.0817 -0.5330 -0.0202 94  ALA   P C   
27260 O  O   . ALA   P  95  ? 1.8620 0.2365 1.4645 -0.0338 -0.5205 -0.0063 94  ALA   P O   
27261 C  CB  . ALA   P  95  ? 1.7446 0.3590 1.4028 -0.0574 -0.5336 -0.0706 94  ALA   P CB  
27262 N  N   . GLN   P  96  ? 1.8150 0.4044 1.3275 -0.0717 -0.5445 0.0137  95  GLN   P N   
27263 C  CA  . GLN   P  96  ? 1.8324 0.4265 1.3059 -0.0343 -0.5539 0.0119  95  GLN   P CA  
27264 C  C   . GLN   P  96  ? 1.8263 0.5244 1.3510 -0.0691 -0.5712 0.0116  95  GLN   P C   
27265 O  O   . GLN   P  96  ? 1.8591 0.5234 1.4075 -0.1813 -0.5990 0.0704  95  GLN   P O   
27266 C  CB  . GLN   P  96  ? 1.8343 0.4579 1.2960 -0.0173 -0.5644 0.0200  95  GLN   P CB  
27267 C  CG  . GLN   P  96  ? 1.8151 0.4835 1.2439 -0.0122 -0.5867 -0.0005 95  GLN   P CG  
27268 C  CD  . GLN   P  96  ? 1.8111 0.5628 1.2095 -0.0299 -0.6058 -0.0305 95  GLN   P CD  
27269 O  OE1 . GLN   P  96  ? 1.8295 0.5344 1.2207 -0.0232 -0.6117 -0.0271 95  GLN   P OE1 
27270 N  NE2 . GLN   P  96  ? 1.8236 0.5709 1.1675 0.0010  -0.6179 -0.0366 95  GLN   P NE2 
27271 N  N   . ASN   P  97  ? 1.8250 0.4715 1.3523 -0.0683 -0.5681 -0.0052 96  ASN   P N   
27272 C  CA  . ASN   P  97  ? 1.8109 0.4798 1.3657 -0.0611 -0.5751 -0.0169 96  ASN   P CA  
27273 C  C   . ASN   P  97  ? 1.8567 0.4826 1.3289 -0.0989 -0.5719 -0.0739 96  ASN   P C   
27274 O  O   . ASN   P  97  ? 1.8513 0.6099 1.4044 -0.2366 -0.5522 0.0078  96  ASN   P O   
27275 C  CB  . ASN   P  97  ? 1.7721 0.5350 1.3496 -0.0614 -0.5752 -0.0327 96  ASN   P CB  
27276 C  CG  . ASN   P  97  ? 1.7599 0.6092 1.3430 -0.0534 -0.5609 -0.0359 96  ASN   P CG  
27277 O  OD1 . ASN   P  97  ? 1.7508 0.5831 1.2930 -0.0591 -0.6101 -0.0408 96  ASN   P OD1 
27278 N  ND2 . ASN   P  97  ? 1.7362 0.6672 1.3699 -0.0469 -0.5570 0.0035  96  ASN   P ND2 
27279 N  N   . TYR   P  98  ? 1.8650 0.4075 1.3433 -0.0546 -0.5230 -0.0856 97  TYR   P N   
27280 C  CA  . TYR   P  98  ? 1.8724 0.4122 1.3494 -0.0418 -0.5089 -0.0793 97  TYR   P CA  
27281 C  C   . TYR   P  98  ? 1.9004 0.3674 1.3448 -0.0518 -0.5606 -0.1308 97  TYR   P C   
27282 O  O   . TYR   P  98  ? 1.9645 0.3973 1.3246 -0.0275 -0.5713 -0.1055 97  TYR   P O   
27283 C  CB  . TYR   P  98  ? 1.8223 0.4307 1.3181 -0.0223 -0.4826 -0.0915 97  TYR   P CB  
27284 C  CG  . TYR   P  98  ? 1.8381 0.4891 1.3327 -0.0030 -0.4508 -0.0646 97  TYR   P CG  
27285 C  CD1 . TYR   P  98  ? 1.8453 0.4748 1.3693 0.0342  -0.4378 -0.0554 97  TYR   P CD1 
27286 C  CD2 . TYR   P  98  ? 1.8219 0.4772 1.3319 -0.0058 -0.4525 -0.0358 97  TYR   P CD2 
27287 C  CE1 . TYR   P  98  ? 1.8657 0.4487 1.3799 0.0406  -0.4225 -0.0316 97  TYR   P CE1 
27288 C  CE2 . TYR   P  98  ? 1.8493 0.4891 1.3506 0.0003  -0.4192 -0.0220 97  TYR   P CE2 
27289 C  CZ  . TYR   P  98  ? 1.8646 0.4718 1.3398 0.0177  -0.4097 -0.0216 97  TYR   P CZ  
27290 O  OH  . TYR   P  98  ? 1.8876 0.4227 1.3298 0.0231  -0.4354 0.0055  97  TYR   P OH  
27291 N  N   . LEU   P  99  ? 1.8632 0.2836 1.3095 -0.0868 -0.6067 -0.1538 98  LEU   P N   
27292 C  CA  . LEU   P  99  ? 1.8523 0.3710 1.3333 -0.0659 -0.6427 -0.1495 98  LEU   P CA  
27293 C  C   . LEU   P  99  ? 1.9137 0.3858 1.3739 -0.0532 -0.6540 -0.1841 98  LEU   P C   
27294 O  O   . LEU   P  99  ? 1.9227 0.3398 1.4615 -0.0281 -0.6682 -0.1988 98  LEU   P O   
27295 C  CB  . LEU   P  99  ? 1.8415 0.3168 1.3156 -0.0921 -0.6771 -0.1703 98  LEU   P CB  
27296 C  CG  . LEU   P  99  ? 1.8638 0.3129 1.3339 -0.0778 -0.6949 -0.1768 98  LEU   P CG  
27297 C  CD1 . LEU   P  99  ? 1.8713 0.3098 1.3515 -0.0683 -0.7012 -0.1495 98  LEU   P CD1 
27298 C  CD2 . LEU   P  99  ? 1.8485 0.3306 1.3151 -0.0594 -0.6943 -0.1814 98  LEU   P CD2 
27299 N  N   . LYS   P  100 ? 1.9432 0.4403 1.3580 -0.0282 -0.6417 -0.1739 99  LYS   P N   
27300 C  CA  . LYS   P  100 ? 1.9866 0.4176 1.3382 -0.0026 -0.5933 -0.1917 99  LYS   P CA  
27301 C  C   . LYS   P  100 ? 1.9629 0.3987 1.2806 0.0256  -0.6155 -0.1787 99  LYS   P C   
27302 O  O   . LYS   P  100 ? 1.9954 0.4029 1.2448 0.0579  -0.6492 -0.1638 99  LYS   P O   
27303 C  CB  . LYS   P  100 ? 2.0199 0.4752 1.3131 -0.0075 -0.5354 -0.1769 99  LYS   P CB  
27304 C  CG  . LYS   P  100 ? 2.0548 0.5253 1.3619 -0.0430 -0.5134 -0.2195 99  LYS   P CG  
27305 C  CD  . LYS   P  100 ? 2.0834 0.5550 1.3457 -0.0507 -0.4812 -0.2171 99  LYS   P CD  
27306 C  CE  . LYS   P  100 ? 2.0973 0.6228 1.4219 -0.0981 -0.4697 -0.2299 99  LYS   P CE  
27307 N  NZ  . LYS   P  100 ? 2.1531 0.6247 1.5410 -0.0958 -0.4368 -0.1880 99  LYS   P NZ  
27308 N  N   . THR   P  101 ? 1.9243 0.3031 1.2725 0.0008  -0.6107 -0.1286 100 THR   P N   
27309 C  CA  . THR   P  101 ? 1.9095 0.2440 1.2767 0.0392  -0.6041 -0.1102 100 THR   P CA  
27310 C  C   . THR   P  101 ? 1.9117 0.3458 1.2740 0.0306  -0.6105 -0.0914 100 THR   P C   
27311 O  O   . THR   P  101 ? 1.9329 0.3806 1.2665 0.0329  -0.5949 -0.0176 100 THR   P O   
27312 C  CB  . THR   P  101 ? 1.8971 0.1707 1.2819 0.0082  -0.5904 -0.0869 100 THR   P CB  
27313 O  OG1 . THR   P  101 ? 1.8881 0.1183 1.2678 0.0228  -0.5774 -0.1126 100 THR   P OG1 
27314 C  CG2 . THR   P  101 ? 1.8892 0.1358 1.2937 0.0068  -0.5976 -0.0780 100 THR   P CG2 
27315 N  N   . TYR   P  102 ? 1.8754 0.3095 1.2803 0.0247  -0.5868 -0.0847 101 TYR   P N   
27316 C  CA  . TYR   P  102 ? 1.8220 0.3581 1.2932 0.0195  -0.6191 -0.0856 101 TYR   P CA  
27317 C  C   . TYR   P  102 ? 1.8141 0.3354 1.3225 0.0218  -0.6171 -0.0933 101 TYR   P C   
27318 O  O   . TYR   P  102 ? 1.7797 0.3365 1.3372 0.0296  -0.6422 -0.0966 101 TYR   P O   
27319 C  CB  . TYR   P  102 ? 1.8144 0.3991 1.3049 0.0200  -0.5988 -0.1071 101 TYR   P CB  
27320 C  CG  . TYR   P  102 ? 1.8111 0.4546 1.3036 0.0254  -0.6205 -0.1025 101 TYR   P CG  
27321 C  CD1 . TYR   P  102 ? 1.7989 0.4446 1.3151 0.0012  -0.6405 -0.1371 101 TYR   P CD1 
27322 C  CD2 . TYR   P  102 ? 1.7605 0.4751 1.2713 0.0432  -0.6152 -0.1054 101 TYR   P CD2 
27323 C  CE1 . TYR   P  102 ? 1.7958 0.4422 1.2821 -0.0037 -0.6558 -0.1508 101 TYR   P CE1 
27324 C  CE2 . TYR   P  102 ? 1.7543 0.5018 1.2595 0.0375  -0.6293 -0.1316 101 TYR   P CE2 
27325 C  CZ  . TYR   P  102 ? 1.7788 0.4918 1.2483 0.0177  -0.6465 -0.1291 101 TYR   P CZ  
27326 O  OH  . TYR   P  102 ? 1.7537 0.6072 1.2349 -0.0077 -0.6540 -0.1803 101 TYR   P OH  
27327 N  N   . ASN   P  103 ? 1.7535 0.3508 1.3217 0.0399  -0.6420 -0.0692 102 ASN   P N   
27328 C  CA  . ASN   P  103 ? 1.7663 0.4296 1.3662 0.0737  -0.6457 -0.0346 102 ASN   P CA  
27329 C  C   . ASN   P  103 ? 1.7430 0.5131 1.3563 0.0621  -0.6718 -0.0179 102 ASN   P C   
27330 O  O   . ASN   P  103 ? 1.7819 0.4898 1.4198 0.1018  -0.6619 0.0198  102 ASN   P O   
27331 C  CB  . ASN   P  103 ? 1.7632 0.4387 1.3758 0.1226  -0.6693 -0.0327 102 ASN   P CB  
27332 C  CG  . ASN   P  103 ? 1.7541 0.4154 1.4094 0.1703  -0.6737 -0.0313 102 ASN   P CG  
27333 O  OD1 . ASN   P  103 ? 1.6935 0.3529 1.4441 0.2291  -0.6957 -0.0025 102 ASN   P OD1 
27334 N  ND2 . ASN   P  103 ? 1.7446 0.4873 1.4379 0.1666  -0.6779 -0.0487 102 ASN   P ND2 
27335 N  N   . GLU   P  104 ? 1.7284 0.5288 1.3810 0.0749  -0.6606 -0.0152 103 GLU   P N   
27336 C  CA  . GLU   P  104 ? 1.7208 0.6207 1.4091 0.0297  -0.6835 -0.0312 103 GLU   P CA  
27337 C  C   . GLU   P  104 ? 1.7139 0.6415 1.4022 0.0421  -0.6608 -0.0190 103 GLU   P C   
27338 O  O   . GLU   P  104 ? 1.6918 0.6779 1.3622 0.0013  -0.6489 -0.0021 103 GLU   P O   
27339 C  CB  . GLU   P  104 ? 1.7170 0.6797 1.4061 -0.0043 -0.6900 -0.0359 103 GLU   P CB  
27340 C  CG  . GLU   P  104 ? 1.7865 0.6850 1.4248 -0.0692 -0.7081 -0.0312 103 GLU   P CG  
27341 C  CD  . GLU   P  104 ? 1.7820 0.7009 1.4640 -0.1031 -0.6852 -0.0814 103 GLU   P CD  
27342 O  OE1 . GLU   P  104 ? 1.8620 0.7139 1.4261 -0.2424 -0.7493 -0.0740 103 GLU   P OE1 
27343 O  OE2 . GLU   P  104 ? 1.7673 0.7334 1.5180 -0.0379 -0.7375 -0.0472 103 GLU   P OE2 
27344 N  N   . ASP   P  105 ? 1.7262 0.6114 1.4540 0.0405  -0.6228 -0.0369 104 ASP   P N   
27345 C  CA  . ASP   P  105 ? 1.6946 0.5761 1.4048 0.0888  -0.6074 -0.0703 104 ASP   P CA  
27346 C  C   . ASP   P  105 ? 1.6830 0.5025 1.3844 0.0718  -0.6062 -0.0466 104 ASP   P C   
27347 O  O   . ASP   P  105 ? 1.6399 0.4054 1.3502 0.1667  -0.6569 -0.0231 104 ASP   P O   
27348 C  CB  . ASP   P  105 ? 1.6987 0.6047 1.4093 0.0819  -0.6018 -0.0876 104 ASP   P CB  
27349 C  CG  . ASP   P  105 ? 1.7126 0.6270 1.4333 0.1170  -0.6161 -0.1035 104 ASP   P CG  
27350 O  OD1 . ASP   P  105 ? 1.7166 0.6244 1.4433 0.0678  -0.6329 -0.1089 104 ASP   P OD1 
27351 O  OD2 . ASP   P  105 ? 1.7388 0.6756 1.4514 0.1827  -0.6464 -0.1593 104 ASP   P OD2 
27352 N  N   . ILE   P  106 ? 1.6594 0.4810 1.4048 0.0775  -0.5662 -0.0397 105 ILE   P N   
27353 C  CA  . ILE   P  106 ? 1.6769 0.4559 1.4056 0.0532  -0.5273 -0.0673 105 ILE   P CA  
27354 C  C   . ILE   P  106 ? 1.6945 0.4180 1.4482 0.0199  -0.5055 -0.0771 105 ILE   P C   
27355 O  O   . ILE   P  106 ? 1.7577 0.4003 1.4360 -0.0296 -0.5180 -0.1776 105 ILE   P O   
27356 C  CB  . ILE   P  106 ? 1.6534 0.4558 1.4139 0.0745  -0.5125 -0.0617 105 ILE   P CB  
27357 C  CG1 . ILE   P  106 ? 1.6573 0.4015 1.4130 0.0679  -0.5067 -0.0759 105 ILE   P CG1 
27358 C  CG2 . ILE   P  106 ? 1.6481 0.4713 1.4122 0.0852  -0.5036 -0.0455 105 ILE   P CG2 
27359 C  CD1 . ILE   P  106 ? 1.6337 0.3732 1.4260 0.0661  -0.5054 -0.0783 105 ILE   P CD1 
27360 N  N   . PRO   P  107 ? 1.7058 0.3650 1.4607 0.0268  -0.4936 -0.0577 106 PRO   P N   
27361 C  CA  . PRO   P  107 ? 1.6809 0.3800 1.4438 0.0334  -0.4832 -0.0562 106 PRO   P CA  
27362 C  C   . PRO   P  107 ? 1.6820 0.3880 1.4879 0.0253  -0.4803 -0.0322 106 PRO   P C   
27363 O  O   . PRO   P  107 ? 1.7123 0.2700 1.4763 -0.0065 -0.4955 -0.0153 106 PRO   P O   
27364 C  CB  . PRO   P  107 ? 1.6858 0.3645 1.4295 0.0163  -0.4865 -0.0585 106 PRO   P CB  
27365 C  CG  . PRO   P  107 ? 1.7023 0.3582 1.4393 0.0221  -0.4785 -0.0307 106 PRO   P CG  
27366 C  CD  . PRO   P  107 ? 1.7129 0.3967 1.4392 0.0297  -0.4772 -0.0189 106 PRO   P CD  
27367 N  N   . VAL   P  108 ? 1.6776 0.3582 1.5170 0.0309  -0.4808 -0.0130 107 VAL   P N   
27368 C  CA  . VAL   P  108 ? 1.7143 0.3481 1.5210 0.0381  -0.4578 -0.0230 107 VAL   P CA  
27369 C  C   . VAL   P  108 ? 1.7234 0.2664 1.4751 0.0297  -0.4311 -0.0279 107 VAL   P C   
27370 O  O   . VAL   P  108 ? 1.7549 0.1578 1.5125 0.0655  -0.4179 -0.0211 107 VAL   P O   
27371 C  CB  . VAL   P  108 ? 1.7253 0.3393 1.5695 0.0330  -0.4567 -0.0307 107 VAL   P CB  
27372 C  CG1 . VAL   P  108 ? 1.7284 0.3895 1.5715 0.0496  -0.4274 0.0184  107 VAL   P CG1 
27373 C  CG2 . VAL   P  108 ? 1.7495 0.3292 1.6045 0.0554  -0.4519 -0.0035 107 VAL   P CG2 
27374 N  N   . GLU   P  109 ? 1.7664 0.2864 1.4670 0.0103  -0.4165 -0.0285 108 GLU   P N   
27375 C  CA  . GLU   P  109 ? 1.7766 0.3092 1.4500 0.0284  -0.3966 0.0205  108 GLU   P CA  
27376 C  C   . GLU   P  109 ? 1.7635 0.3612 1.4471 0.0199  -0.3978 0.0390  108 GLU   P C   
27377 O  O   . GLU   P  109 ? 1.8166 0.1370 1.5153 0.0115  -0.3571 -0.0169 108 GLU   P O   
27378 C  CB  . GLU   P  109 ? 1.7909 0.3578 1.4718 0.0297  -0.3767 0.0650  108 GLU   P CB  
27379 C  CG  . GLU   P  109 ? 1.7749 0.4118 1.5136 0.0611  -0.3537 0.1454  108 GLU   P CG  
27380 C  CD  . GLU   P  109 ? 1.8039 0.5255 1.5620 0.0517  -0.3271 0.1840  108 GLU   P CD  
27381 O  OE1 . GLU   P  109 ? 1.8364 0.4729 1.6034 0.0582  -0.3264 0.1470  108 GLU   P OE1 
27382 O  OE2 . GLU   P  109 ? 1.7768 0.6229 1.6034 0.0972  -0.3252 0.2860  108 GLU   P OE2 
27383 N  N   . ILE   P  110 ? 1.7277 0.3800 1.4082 -0.0080 -0.4052 -0.0012 109 ILE   P N   
27384 C  CA  . ILE   P  110 ? 1.7144 0.4479 1.3541 0.0065  -0.4014 -0.0016 109 ILE   P CA  
27385 C  C   . ILE   P  110 ? 1.6795 0.4010 1.3501 0.0107  -0.4291 0.0017  109 ILE   P C   
27386 O  O   . ILE   P  110 ? 1.6834 0.3923 1.4056 0.0375  -0.4158 0.0757  109 ILE   P O   
27387 C  CB  . ILE   P  110 ? 1.7231 0.4533 1.3377 0.0221  -0.3975 0.0145  109 ILE   P CB  
27388 C  CG1 . ILE   P  110 ? 1.7442 0.5206 1.3277 0.0144  -0.3739 -0.0024 109 ILE   P CG1 
27389 C  CG2 . ILE   P  110 ? 1.7076 0.4942 1.3436 0.0144  -0.4114 0.0277  109 ILE   P CG2 
27390 C  CD1 . ILE   P  110 ? 1.7800 0.5281 1.3351 0.0162  -0.3772 0.0117  109 ILE   P CD1 
27391 N  N   . LEU   P  111 ? 1.6640 0.3762 1.2968 -0.0003 -0.4597 -0.0184 110 LEU   P N   
27392 C  CA  . LEU   P  111 ? 1.6629 0.3935 1.2968 -0.0033 -0.4665 -0.0068 110 LEU   P CA  
27393 C  C   . LEU   P  111 ? 1.6575 0.4001 1.3293 -0.0060 -0.4304 0.0320  110 LEU   P C   
27394 O  O   . LEU   P  111 ? 1.6402 0.4333 1.3480 -0.0275 -0.4066 0.0918  110 LEU   P O   
27395 C  CB  . LEU   P  111 ? 1.6626 0.3385 1.2534 -0.0094 -0.4779 -0.0265 110 LEU   P CB  
27396 C  CG  . LEU   P  111 ? 1.6777 0.3304 1.2521 0.0033  -0.4751 -0.0193 110 LEU   P CG  
27397 C  CD1 . LEU   P  111 ? 1.6752 0.3227 1.2453 -0.0010 -0.4835 -0.0261 110 LEU   P CD1 
27398 C  CD2 . LEU   P  111 ? 1.6881 0.3390 1.2729 -0.0107 -0.4664 -0.0347 110 LEU   P CD2 
27399 N  N   . VAL   P  112 ? 1.6776 0.5316 1.2840 0.0063  -0.4471 0.0203  111 VAL   P N   
27400 C  CA  . VAL   P  112 ? 1.7157 0.5435 1.3347 0.0377  -0.4273 0.0395  111 VAL   P CA  
27401 C  C   . VAL   P  112 ? 1.7205 0.5939 1.3951 0.0486  -0.4087 -0.0051 111 VAL   P C   
27402 O  O   . VAL   P  112 ? 1.7543 0.5841 1.4943 0.0865  -0.3829 0.0125  111 VAL   P O   
27403 C  CB  . VAL   P  112 ? 1.7147 0.5647 1.3262 0.0343  -0.4254 0.0506  111 VAL   P CB  
27404 C  CG1 . VAL   P  112 ? 1.7087 0.5587 1.3297 0.0252  -0.4174 0.0509  111 VAL   P CG1 
27405 C  CG2 . VAL   P  112 ? 1.7110 0.6164 1.3498 0.0219  -0.4212 0.0434  111 VAL   P CG2 
27406 N  N   . ARG   P  113 ? 1.7924 0.5774 1.3889 0.0403  -0.3908 -0.0066 112 ARG   P N   
27407 C  CA  . ARG   P  113 ? 1.7995 0.5707 1.4366 0.0337  -0.3517 -0.0304 112 ARG   P CA  
27408 C  C   . ARG   P  113 ? 1.7916 0.5558 1.4546 0.0465  -0.3914 0.0196  112 ARG   P C   
27409 O  O   . ARG   P  113 ? 1.7710 0.5076 1.4551 0.0234  -0.4325 -0.0280 112 ARG   P O   
27410 C  CB  . ARG   P  113 ? 1.8811 0.6055 1.4132 0.0102  -0.3182 -0.0468 112 ARG   P CB  
27411 C  CG  . ARG   P  113 ? 1.9293 0.6559 1.4175 0.0645  -0.2769 -0.0601 112 ARG   P CG  
27412 C  CD  . ARG   P  113 ? 1.9884 0.7188 1.3853 0.0830  -0.2536 0.0250  112 ARG   P CD  
27413 N  NE  . ARG   P  113 ? 2.0596 0.7255 1.3818 0.1526  -0.2431 0.0346  112 ARG   P NE  
27414 C  CZ  . ARG   P  113 ? 2.0928 0.8029 1.3485 0.2230  -0.2747 0.0687  112 ARG   P CZ  
27415 N  NH1 . ARG   P  113 ? 2.0813 0.8874 1.3419 0.2529  -0.2837 0.0425  112 ARG   P NH1 
27416 N  NH2 . ARG   P  113 ? 2.1493 0.8179 1.3572 0.1903  -0.2842 0.0516  112 ARG   P NH2 
27417 N  N   . ARG   P  114 ? 1.8439 0.6388 1.4684 0.0782  -0.3424 -0.0032 113 ARG   P N   
27418 C  CA  . ARG   P  114 ? 1.8974 0.7198 1.4802 0.1103  -0.3634 -0.0113 113 ARG   P CA  
27419 C  C   . ARG   P  114 ? 1.8203 0.7610 1.4951 0.0427  -0.3466 -0.0243 113 ARG   P C   
27420 O  O   . ARG   P  114 ? 1.8395 0.8786 1.6132 0.1796  -0.3590 -0.0136 113 ARG   P O   
27421 C  CB  . ARG   P  114 ? 2.0115 0.6824 1.6218 0.1435  -0.3019 0.0512  113 ARG   P CB  
27422 C  CG  . ARG   P  114 ? 2.0350 0.7249 1.6468 0.1890  -0.3071 0.0280  113 ARG   P CG  
27423 C  CD  . ARG   P  114 ? 2.1401 0.7430 1.7265 0.2368  -0.2711 0.0452  113 ARG   P CD  
27424 N  NE  . ARG   P  114 ? 2.1893 0.8093 1.7137 0.2941  -0.3178 0.1159  113 ARG   P NE  
27425 C  CZ  . ARG   P  114 ? 2.1057 0.7604 1.7496 0.3372  -0.4294 0.0247  113 ARG   P CZ  
27426 N  NH1 . ARG   P  114 ? 2.1620 0.7727 1.7394 0.2965  -0.4148 -0.0069 113 ARG   P NH1 
27427 N  NH2 . ARG   P  114 ? 2.0800 0.6708 1.7015 0.3029  -0.4808 -0.0323 113 ARG   P NH2 
27428 N  N   . LEU   P  115 ? 1.8353 0.6997 1.3234 0.0306  -0.3962 -0.0607 114 LEU   P N   
27429 C  CA  . LEU   P  115 ? 1.7899 0.6307 1.3214 0.0293  -0.4015 -0.0942 114 LEU   P CA  
27430 C  C   . LEU   P  115 ? 1.7941 0.5925 1.2658 -0.0194 -0.3584 -0.1151 114 LEU   P C   
27431 O  O   . LEU   P  115 ? 1.8511 0.6669 1.2941 -0.0342 -0.3205 -0.0464 114 LEU   P O   
27432 C  CB  . LEU   P  115 ? 1.7979 0.6282 1.3134 0.0328  -0.4400 -0.0876 114 LEU   P CB  
27433 C  CG  . LEU   P  115 ? 1.7929 0.6517 1.3300 0.0385  -0.4391 -0.0782 114 LEU   P CG  
27434 C  CD1 . LEU   P  115 ? 1.8185 0.6660 1.3407 0.0196  -0.4699 -0.1123 114 LEU   P CD1 
27435 C  CD2 . LEU   P  115 ? 1.8053 0.6234 1.3750 0.0818  -0.4186 -0.0410 114 LEU   P CD2 
27436 N  N   . SER   P  116 ? 1.7753 0.5096 1.2466 -0.0525 -0.3940 -0.1156 115 SER   P N   
27437 C  CA  . SER   P  116 ? 1.7986 0.4409 1.2402 -0.0960 -0.3945 -0.1457 115 SER   P CA  
27438 C  C   . SER   P  116 ? 1.7916 0.4479 1.2573 -0.0887 -0.3853 -0.2047 115 SER   P C   
27439 O  O   . SER   P  116 ? 1.7291 0.2894 1.2450 -0.1837 -0.3644 -0.3332 115 SER   P O   
27440 C  CB  . SER   P  116 ? 1.8221 0.4036 1.2309 -0.0625 -0.3766 -0.1236 115 SER   P CB  
27441 O  OG  . SER   P  116 ? 1.8248 0.3740 1.2238 -0.0533 -0.3758 -0.1100 115 SER   P OG  
27442 N  N   . ASP   P  117 ? 1.8078 0.4720 1.2933 -0.1171 -0.4030 -0.1998 116 ASP   P N   
27443 C  CA  . ASP   P  117 ? 1.8095 0.5377 1.2894 -0.0783 -0.4379 -0.2224 116 ASP   P CA  
27444 C  C   . ASP   P  117 ? 1.7856 0.4631 1.2787 -0.0305 -0.4364 -0.2566 116 ASP   P C   
27445 O  O   . ASP   P  117 ? 1.8365 0.3313 1.2341 0.0180  -0.4452 -0.3082 116 ASP   P O   
27446 C  CB  . ASP   P  117 ? 1.8672 0.5576 1.3347 -0.1316 -0.4260 -0.2340 116 ASP   P CB  
27447 C  CG  . ASP   P  117 ? 1.9270 0.6584 1.3404 -0.1632 -0.4248 -0.2213 116 ASP   P CG  
27448 O  OD1 . ASP   P  117 ? 1.9550 0.7720 1.3513 -0.2320 -0.3833 -0.3161 116 ASP   P OD1 
27449 O  OD2 . ASP   P  117 ? 1.9940 0.6632 1.3125 -0.1037 -0.4679 -0.2078 116 ASP   P OD2 
27450 N  N   . ILE   P  118 ? 1.7349 0.5106 1.2657 0.0030  -0.4702 -0.2251 117 ILE   P N   
27451 C  CA  . ILE   P  118 ? 1.7115 0.5763 1.2795 0.0420  -0.4494 -0.1813 117 ILE   P CA  
27452 C  C   . ILE   P  118 ? 1.7211 0.5873 1.3544 0.0123  -0.4545 -0.1362 117 ILE   P C   
27453 O  O   . ILE   P  118 ? 1.6879 0.7062 1.4384 0.0224  -0.4655 -0.0973 117 ILE   P O   
27454 C  CB  . ILE   P  118 ? 1.7294 0.6077 1.2377 0.0783  -0.4522 -0.1685 117 ILE   P CB  
27455 C  CG1 . ILE   P  118 ? 1.7268 0.6051 1.2302 0.1333  -0.4476 -0.1354 117 ILE   P CG1 
27456 C  CG2 . ILE   P  118 ? 1.7123 0.5623 1.2420 0.1020  -0.4261 -0.1736 117 ILE   P CG2 
27457 C  CD1 . ILE   P  118 ? 1.7437 0.6271 1.2226 0.1608  -0.4452 -0.1082 117 ILE   P CD1 
27458 N  N   . LYS   P  119 ? 1.6930 0.6345 1.3604 -0.0013 -0.4777 -0.1161 118 LYS   P N   
27459 C  CA  . LYS   P  119 ? 1.7111 0.6342 1.3937 0.0348  -0.4619 -0.1325 118 LYS   P CA  
27460 C  C   . LYS   P  119 ? 1.7532 0.5980 1.4351 0.0369  -0.3930 -0.1583 118 LYS   P C   
27461 O  O   . LYS   P  119 ? 1.8226 0.7825 1.4621 0.1659  -0.3875 -0.1423 118 LYS   P O   
27462 C  CB  . LYS   P  119 ? 1.7256 0.6764 1.4116 0.0021  -0.4716 -0.1194 118 LYS   P CB  
27463 C  CG  . LYS   P  119 ? 1.7273 0.7270 1.4351 -0.0378 -0.4534 -0.0844 118 LYS   P CG  
27464 C  CD  . LYS   P  119 ? 1.6904 0.7751 1.4559 -0.0609 -0.4627 -0.0474 118 LYS   P CD  
27465 C  CE  . LYS   P  119 ? 1.6836 0.7976 1.4312 -0.0656 -0.4760 -0.0405 118 LYS   P CE  
27466 N  NZ  . LYS   P  119 ? 1.7089 0.7802 1.4422 -0.0810 -0.4765 -0.0398 118 LYS   P NZ  
27467 N  N   . GLN   P  120 ? 1.7623 0.3834 1.4345 0.0465  -0.4464 -0.1281 119 GLN   P N   
27468 C  CA  . GLN   P  120 ? 1.7802 0.4001 1.4444 0.0307  -0.4146 -0.1266 119 GLN   P CA  
27469 C  C   . GLN   P  120 ? 1.7614 0.4574 1.4946 0.0017  -0.4227 -0.1152 119 GLN   P C   
27470 O  O   . GLN   P  120 ? 1.7205 0.4948 1.5914 0.0183  -0.3900 -0.1661 119 GLN   P O   
27471 C  CB  . GLN   P  120 ? 1.7886 0.3720 1.3975 0.0330  -0.4537 -0.1545 119 GLN   P CB  
27472 C  CG  . GLN   P  120 ? 1.7833 0.3761 1.3972 0.0346  -0.4671 -0.1679 119 GLN   P CG  
27473 C  CD  . GLN   P  120 ? 1.8144 0.3472 1.4074 0.0144  -0.4794 -0.1927 119 GLN   P CD  
27474 O  OE1 . GLN   P  120 ? 1.8265 0.2781 1.4022 0.0025  -0.5000 -0.2006 119 GLN   P OE1 
27475 N  NE2 . GLN   P  120 ? 1.8046 0.4183 1.3875 -0.0327 -0.4983 -0.2503 119 GLN   P NE2 
27476 N  N   . GLY   P  121 ? 1.7971 0.5292 1.4687 0.0048  -0.3861 -0.1507 120 GLY   P N   
27477 C  CA  . GLY   P  121 ? 1.7824 0.6639 1.4354 0.0360  -0.4071 -0.0529 120 GLY   P CA  
27478 C  C   . GLY   P  121 ? 1.7532 0.6375 1.4668 0.0586  -0.3754 -0.0442 120 GLY   P C   
27479 O  O   . GLY   P  121 ? 1.7557 0.6859 1.5021 0.1327  -0.3177 -0.0198 120 GLY   P O   
27480 N  N   . TYR   P  122 ? 1.7532 0.5396 1.3996 0.0574  -0.4148 -0.0285 121 TYR   P N   
27481 C  CA  . TYR   P  122 ? 1.7376 0.5503 1.4309 0.0535  -0.3997 -0.0082 121 TYR   P CA  
27482 C  C   . TYR   P  122 ? 1.7473 0.5666 1.4581 0.0555  -0.3991 -0.0288 121 TYR   P C   
27483 O  O   . TYR   P  122 ? 1.7839 0.6472 1.5016 0.0572  -0.3636 0.0272  121 TYR   P O   
27484 C  CB  . TYR   P  122 ? 1.7390 0.5412 1.4124 0.0706  -0.3839 -0.0098 121 TYR   P CB  
27485 C  CG  . TYR   P  122 ? 1.7711 0.5498 1.4300 0.0818  -0.3439 -0.0016 121 TYR   P CG  
27486 C  CD1 . TYR   P  122 ? 1.8051 0.5496 1.4232 0.1444  -0.2991 -0.0206 121 TYR   P CD1 
27487 C  CD2 . TYR   P  122 ? 1.8027 0.5729 1.4408 0.0958  -0.3146 -0.0026 121 TYR   P CD2 
27488 C  CE1 . TYR   P  122 ? 1.8525 0.5281 1.4638 0.1685  -0.2886 -0.0264 121 TYR   P CE1 
27489 C  CE2 . TYR   P  122 ? 1.8513 0.5442 1.4719 0.1405  -0.3085 0.0077  121 TYR   P CE2 
27490 C  CZ  . TYR   P  122 ? 1.8691 0.5258 1.4492 0.1687  -0.2994 -0.0368 121 TYR   P CZ  
27491 O  OH  . TYR   P  122 ? 1.8951 0.6566 1.4105 0.1238  -0.3337 -0.1127 121 TYR   P OH  
27492 N  N   . THR   P  123 ? 1.7535 0.5121 1.4144 0.0022  -0.4385 0.0508  122 THR   P N   
27493 C  CA  . THR   P  123 ? 1.7656 0.4846 1.4975 -0.0249 -0.4038 0.0540  122 THR   P CA  
27494 C  C   . THR   P  123 ? 1.7621 0.4992 1.5059 -0.0134 -0.3864 0.0704  122 THR   P C   
27495 O  O   . THR   P  123 ? 1.7540 0.5303 1.5886 -0.0421 -0.3160 -0.0258 122 THR   P O   
27496 C  CB  . THR   P  123 ? 1.8467 0.4136 1.4969 -0.0688 -0.4020 0.0693  122 THR   P CB  
27497 O  OG1 . THR   P  123 ? 1.8712 0.3493 1.5197 -0.0649 -0.3640 0.0431  122 THR   P OG1 
27498 C  CG2 . THR   P  123 ? 1.8492 0.4002 1.5420 -0.0759 -0.4160 0.0795  122 THR   P CG2 
27499 N  N   . GLN   P  124 ? 1.7225 0.4854 1.4930 -0.0033 -0.3703 0.1393  123 GLN   P N   
27500 C  CA  . GLN   P  124 ? 1.7128 0.5290 1.5319 0.0125  -0.3532 0.1002  123 GLN   P CA  
27501 C  C   . GLN   P  124 ? 1.6822 0.4920 1.5112 0.0014  -0.3464 0.1420  123 GLN   P C   
27502 O  O   . GLN   P  124 ? 1.6597 0.5386 1.5451 -0.0231 -0.3134 0.1529  123 GLN   P O   
27503 C  CB  . GLN   P  124 ? 1.7070 0.5784 1.5164 0.0121  -0.3264 0.1075  123 GLN   P CB  
27504 C  CG  . GLN   P  124 ? 1.7027 0.6159 1.5542 0.0354  -0.3147 0.0802  123 GLN   P CG  
27505 C  CD  . GLN   P  124 ? 1.7147 0.5562 1.5678 0.0716  -0.3068 0.0859  123 GLN   P CD  
27506 O  OE1 . GLN   P  124 ? 1.7690 0.6191 1.5947 0.0716  -0.2910 0.0296  123 GLN   P OE1 
27507 N  NE2 . GLN   P  124 ? 1.7458 0.5338 1.5938 0.0609  -0.3017 0.1245  123 GLN   P NE2 
27508 N  N   . HIS   P  125 ? 1.6730 0.4445 1.5025 0.0167  -0.3915 0.1312  124 HIS   P N   
27509 C  CA  . HIS   P  125 ? 1.6794 0.5035 1.5059 0.0413  -0.3837 0.0816  124 HIS   P CA  
27510 C  C   . HIS   P  125 ? 1.6405 0.4875 1.5147 0.0330  -0.3879 0.0786  124 HIS   P C   
27511 O  O   . HIS   P  125 ? 1.6265 0.4132 1.4346 0.0649  -0.3700 0.0528  124 HIS   P O   
27512 C  CB  . HIS   P  125 ? 1.6841 0.5125 1.5193 0.0307  -0.4179 0.0901  124 HIS   P CB  
27513 C  CG  . HIS   P  125 ? 1.6892 0.5017 1.5617 0.0474  -0.4369 0.0583  124 HIS   P CG  
27514 N  ND1 . HIS   P  125 ? 1.6948 0.4203 1.5465 0.0555  -0.4777 0.0346  124 HIS   P ND1 
27515 C  CD2 . HIS   P  125 ? 1.7000 0.4929 1.5823 0.0613  -0.4513 0.0715  124 HIS   P CD2 
27516 C  CE1 . HIS   P  125 ? 1.6636 0.4503 1.5752 0.0895  -0.4721 0.0191  124 HIS   P CE1 
27517 N  NE2 . HIS   P  125 ? 1.6883 0.5085 1.5949 0.0611  -0.4432 0.0260  124 HIS   P NE2 
27518 N  N   . GLY   P  126 ? 1.6587 0.5552 1.5139 0.0541  -0.3894 0.1136  125 GLY   P N   
27519 C  CA  . GLY   P  126 ? 1.6603 0.6051 1.5361 0.0789  -0.3829 0.0938  125 GLY   P CA  
27520 C  C   . GLY   P  126 ? 1.6821 0.5834 1.5735 0.0876  -0.3890 0.0901  125 GLY   P C   
27521 O  O   . GLY   P  126 ? 1.7115 0.5997 1.5949 0.1221  -0.3569 0.0770  125 GLY   P O   
27522 N  N   . GLY   P  127 ? 1.6946 0.6045 1.6090 0.0753  -0.4179 0.0545  126 GLY   P N   
27523 C  CA  . GLY   P  127 ? 1.6804 0.6072 1.5990 0.0941  -0.4036 0.0539  126 GLY   P CA  
27524 C  C   . GLY   P  127 ? 1.7101 0.5620 1.5193 0.0693  -0.3909 0.0621  126 GLY   P C   
27525 O  O   . GLY   P  127 ? 1.6455 0.4544 1.5729 0.0458  -0.3449 0.0467  126 GLY   P O   
27526 N  N   . LEU   P  128 ? 1.6876 0.5735 1.5147 0.0566  -0.4185 -0.0010 127 LEU   P N   
27527 C  CA  . LEU   P  128 ? 1.7106 0.4703 1.4751 0.0142  -0.4182 -0.0247 127 LEU   P CA  
27528 C  C   . LEU   P  128 ? 1.7543 0.3527 1.5272 -0.0196 -0.4117 0.0051  127 LEU   P C   
27529 O  O   . LEU   P  128 ? 1.7778 0.3015 1.5329 -0.0581 -0.4009 0.0180  127 LEU   P O   
27530 C  CB  . LEU   P  128 ? 1.7000 0.4710 1.4402 0.0119  -0.4439 -0.0515 127 LEU   P CB  
27531 C  CG  . LEU   P  128 ? 1.7093 0.4687 1.4169 0.0192  -0.4425 -0.0545 127 LEU   P CG  
27532 C  CD1 . LEU   P  128 ? 1.6814 0.5197 1.3888 0.0308  -0.4253 -0.1075 127 LEU   P CD1 
27533 C  CD2 . LEU   P  128 ? 1.7205 0.4312 1.4151 0.0261  -0.4492 -0.0649 127 LEU   P CD2 
27534 N  N   . ARG   P  129 ? 1.7694 0.3168 1.5022 -0.0139 -0.4163 0.0176  128 ARG   P N   
27535 C  CA  . ARG   P  129 ? 1.7992 0.3408 1.4857 0.0091  -0.4297 -0.0084 128 ARG   P CA  
27536 C  C   . ARG   P  129 ? 1.8212 0.3180 1.4765 0.0004  -0.4314 -0.0101 128 ARG   P C   
27537 O  O   . ARG   P  129 ? 1.8202 0.2931 1.4608 0.0101  -0.4161 0.0533  128 ARG   P O   
27538 C  CB  . ARG   P  129 ? 1.7860 0.3039 1.4670 0.0119  -0.4376 -0.0323 128 ARG   P CB  
27539 C  CG  . ARG   P  129 ? 1.7673 0.3191 1.4533 0.0192  -0.4540 -0.0317 128 ARG   P CG  
27540 C  CD  . ARG   P  129 ? 1.7801 0.2918 1.4423 0.0054  -0.4727 -0.0496 128 ARG   P CD  
27541 N  NE  . ARG   P  129 ? 1.7612 0.3259 1.4333 0.0007  -0.4798 -0.0460 128 ARG   P NE  
27542 C  CZ  . ARG   P  129 ? 1.7169 0.3790 1.4594 -0.0150 -0.4999 -0.1027 128 ARG   P CZ  
27543 N  NH1 . ARG   P  129 ? 1.7393 0.3836 1.4830 -0.0177 -0.4891 -0.1566 128 ARG   P NH1 
27544 N  NH2 . ARG   P  129 ? 1.6815 0.4347 1.4680 -0.0223 -0.4931 -0.1019 128 ARG   P NH2 
27545 N  N   . PRO   P  130 ? 1.8786 0.3409 1.5048 -0.0106 -0.4252 -0.0561 129 PRO   P N   
27546 C  CA  . PRO   P  130 ? 1.8845 0.3842 1.4862 -0.0007 -0.4360 -0.0804 129 PRO   P CA  
27547 C  C   . PRO   P  130 ? 1.8873 0.4117 1.5000 -0.0191 -0.4282 -0.0768 129 PRO   P C   
27548 O  O   . PRO   P  130 ? 1.9194 0.4421 1.5353 -0.0144 -0.3815 -0.0536 129 PRO   P O   
27549 C  CB  . PRO   P  130 ? 1.9095 0.3935 1.4884 0.0025  -0.4139 -0.0819 129 PRO   P CB  
27550 C  CG  . PRO   P  130 ? 1.9304 0.3853 1.5032 0.0034  -0.4113 -0.0901 129 PRO   P CG  
27551 C  CD  . PRO   P  130 ? 1.8971 0.3798 1.5204 0.0096  -0.4203 -0.0853 129 PRO   P CD  
27552 N  N   . PHE   P  131 ? 1.8611 0.4264 1.5379 0.0083  -0.4970 -0.1547 130 PHE   P N   
27553 C  CA  . PHE   P  131 ? 1.8664 0.4714 1.5052 0.0140  -0.4843 -0.1282 130 PHE   P CA  
27554 C  C   . PHE   P  131 ? 1.8663 0.5140 1.4801 -0.0426 -0.4237 -0.1379 130 PHE   P C   
27555 O  O   . PHE   P  131 ? 1.9178 0.7383 1.5202 -0.0672 -0.3870 -0.2505 130 PHE   P O   
27556 C  CB  . PHE   P  131 ? 1.9029 0.5086 1.5329 0.0183  -0.5244 -0.0883 130 PHE   P CB  
27557 C  CG  . PHE   P  131 ? 1.9358 0.5135 1.4725 0.0336  -0.5467 -0.0741 130 PHE   P CG  
27558 C  CD1 . PHE   P  131 ? 1.9467 0.4988 1.4304 0.0429  -0.5494 -0.0351 130 PHE   P CD1 
27559 C  CD2 . PHE   P  131 ? 1.9549 0.5034 1.4933 0.0430  -0.5322 -0.0524 130 PHE   P CD2 
27560 C  CE1 . PHE   P  131 ? 1.9860 0.4829 1.3975 0.0612  -0.5527 -0.0243 130 PHE   P CE1 
27561 C  CE2 . PHE   P  131 ? 1.9982 0.4970 1.4540 0.0815  -0.5390 -0.0607 130 PHE   P CE2 
27562 C  CZ  . PHE   P  131 ? 2.0001 0.4642 1.4122 0.0485  -0.5584 -0.0570 130 PHE   P CZ  
27563 N  N   . GLY   P  132 ? 1.8993 0.4807 1.3923 -0.0128 -0.4200 -0.1263 131 GLY   P N   
27564 C  CA  . GLY   P  132 ? 1.8518 0.4524 1.3729 -0.0159 -0.4021 -0.0865 131 GLY   P CA  
27565 C  C   . GLY   P  132 ? 1.8186 0.4208 1.3608 -0.0313 -0.3839 -0.0872 131 GLY   P C   
27566 O  O   . GLY   P  132 ? 1.8032 0.3401 1.3011 -0.0220 -0.4151 -0.0596 131 GLY   P O   
27567 N  N   . VAL   P  133 ? 1.8092 0.4821 1.3350 0.0180  -0.3902 -0.0810 132 VAL   P N   
27568 C  CA  . VAL   P  133 ? 1.8068 0.5729 1.3494 0.0429  -0.3863 -0.0743 132 VAL   P CA  
27569 C  C   . VAL   P  133 ? 1.7757 0.4434 1.3502 0.0496  -0.3851 -0.0934 132 VAL   P C   
27570 O  O   . VAL   P  133 ? 1.7829 0.3375 1.3418 0.1146  -0.3558 -0.0093 132 VAL   P O   
27571 C  CB  . VAL   P  133 ? 1.8563 0.6351 1.3058 0.0589  -0.3595 -0.1161 132 VAL   P CB  
27572 C  CG1 . VAL   P  133 ? 1.8653 0.7452 1.3024 0.0597  -0.3689 -0.0877 132 VAL   P CG1 
27573 C  CG2 . VAL   P  133 ? 1.8529 0.7600 1.3081 0.0418  -0.3622 -0.0743 132 VAL   P CG2 
27574 N  N   . SER   P  134 ? 1.7810 0.4668 1.3895 0.0099  -0.3837 -0.1263 133 SER   P N   
27575 C  CA  . SER   P  134 ? 1.7498 0.5601 1.3974 -0.0094 -0.4014 -0.1050 133 SER   P CA  
27576 C  C   . SER   P  134 ? 1.7063 0.5201 1.3787 -0.0526 -0.4315 -0.1528 133 SER   P C   
27577 O  O   . SER   P  134 ? 1.7007 0.5459 1.3682 -0.0500 -0.4420 -0.1170 133 SER   P O   
27578 C  CB  . SER   P  134 ? 1.7785 0.6154 1.3905 -0.0207 -0.3916 -0.1351 133 SER   P CB  
27579 O  OG  . SER   P  134 ? 1.7706 0.7555 1.4543 0.0037  -0.3640 -0.0788 133 SER   P OG  
27580 N  N   . PHE   P  135 ? 1.6799 0.4842 1.3832 -0.0853 -0.4567 -0.1847 134 PHE   P N   
27581 C  CA  . PHE   P  135 ? 1.6802 0.5165 1.4146 -0.0670 -0.4468 -0.1734 134 PHE   P CA  
27582 C  C   . PHE   P  135 ? 1.7377 0.3088 1.4342 -0.0934 -0.4598 -0.2243 134 PHE   P C   
27583 O  O   . PHE   P  135 ? 1.6934 0.2053 1.4932 -0.0669 -0.4754 -0.2590 134 PHE   P O   
27584 C  CB  . PHE   P  135 ? 1.6258 0.5594 1.3555 -0.1055 -0.4343 -0.1770 134 PHE   P CB  
27585 C  CG  . PHE   P  135 ? 1.5718 0.7071 1.3292 -0.0910 -0.4115 -0.1647 134 PHE   P CG  
27586 C  CD1 . PHE   P  135 ? 1.5711 0.8257 1.3335 -0.0984 -0.4063 -0.1512 134 PHE   P CD1 
27587 C  CD2 . PHE   P  135 ? 1.5648 0.7347 1.3069 -0.0874 -0.4084 -0.1498 134 PHE   P CD2 
27588 C  CE1 . PHE   P  135 ? 1.5440 0.8871 1.3167 -0.1065 -0.4233 -0.1270 134 PHE   P CE1 
27589 C  CE2 . PHE   P  135 ? 1.5640 0.8183 1.2765 -0.0774 -0.4111 -0.1109 134 PHE   P CE2 
27590 C  CZ  . PHE   P  135 ? 1.5449 0.8762 1.2754 -0.0950 -0.4230 -0.1212 134 PHE   P CZ  
27591 N  N   . ILE   P  136 ? 1.7495 0.3590 1.5162 -0.0945 -0.4616 -0.2007 135 ILE   P N   
27592 C  CA  . ILE   P  136 ? 1.8412 0.4986 1.5108 -0.0977 -0.4599 -0.1620 135 ILE   P CA  
27593 C  C   . ILE   P  136 ? 1.8366 0.5212 1.5092 -0.0543 -0.4411 -0.0947 135 ILE   P C   
27594 O  O   . ILE   P  136 ? 1.8753 0.6615 1.5115 -0.0471 -0.3780 -0.0139 135 ILE   P O   
27595 C  CB  . ILE   P  136 ? 1.8608 0.5220 1.5341 -0.1029 -0.4786 -0.1822 135 ILE   P CB  
27596 C  CG1 . ILE   P  136 ? 1.8761 0.5353 1.5459 -0.0706 -0.4558 -0.1711 135 ILE   P CG1 
27597 C  CG2 . ILE   P  136 ? 1.8956 0.5174 1.5439 -0.1041 -0.4889 -0.1782 135 ILE   P CG2 
27598 C  CD1 . ILE   P  136 ? 1.9022 0.4759 1.5732 -0.0781 -0.4366 -0.1629 135 ILE   P CD1 
27599 N  N   . TYR   P  137 ? 1.8348 0.6129 1.4845 -0.0794 -0.4399 -0.0787 136 TYR   P N   
27600 C  CA  . TYR   P  137 ? 1.7865 0.6113 1.4142 -0.0761 -0.4519 -0.1144 136 TYR   P CA  
27601 C  C   . TYR   P  137 ? 1.7524 0.6348 1.4287 -0.0643 -0.4473 -0.1011 136 TYR   P C   
27602 O  O   . TYR   P  137 ? 1.7185 0.6909 1.3586 -0.0977 -0.4845 -0.0332 136 TYR   P O   
27603 C  CB  . TYR   P  137 ? 1.7971 0.5263 1.3504 -0.0657 -0.4541 -0.1490 136 TYR   P CB  
27604 C  CG  . TYR   P  137 ? 1.7874 0.4390 1.3157 -0.0578 -0.4427 -0.1804 136 TYR   P CG  
27605 C  CD1 . TYR   P  137 ? 1.8005 0.4267 1.3095 -0.0562 -0.4427 -0.1666 136 TYR   P CD1 
27606 C  CD2 . TYR   P  137 ? 1.7823 0.4335 1.3039 -0.0340 -0.4444 -0.1733 136 TYR   P CD2 
27607 C  CE1 . TYR   P  137 ? 1.8300 0.3799 1.2850 -0.0586 -0.4445 -0.1831 136 TYR   P CE1 
27608 C  CE2 . TYR   P  137 ? 1.8039 0.4153 1.2895 -0.0122 -0.4411 -0.1747 136 TYR   P CE2 
27609 C  CZ  . TYR   P  137 ? 1.8347 0.3610 1.2752 -0.0310 -0.4418 -0.1744 136 TYR   P CZ  
27610 O  OH  . TYR   P  137 ? 1.8718 0.3000 1.2333 0.0111  -0.4304 -0.1401 136 TYR   P OH  
27611 N  N   . ALA   P  138 ? 1.7621 0.6265 1.4274 -0.0583 -0.4489 -0.1370 137 ALA   P N   
27612 C  CA  . ALA   P  138 ? 1.8020 0.6363 1.3834 -0.0618 -0.4564 -0.1574 137 ALA   P CA  
27613 C  C   . ALA   P  138 ? 1.8226 0.6311 1.4094 -0.0432 -0.4764 -0.1127 137 ALA   P C   
27614 O  O   . ALA   P  138 ? 1.8115 0.6464 1.4263 -0.0238 -0.4129 -0.0681 137 ALA   P O   
27615 C  CB  . ALA   P  138 ? 1.8019 0.6838 1.3869 -0.0752 -0.4562 -0.1834 137 ALA   P CB  
27616 N  N   . GLY   P  139 ? 1.8494 0.7162 1.2970 -0.0482 -0.5134 -0.1523 138 GLY   P N   
27617 C  CA  . GLY   P  139 ? 1.8677 0.7198 1.3089 -0.0467 -0.5493 -0.1491 138 GLY   P CA  
27618 C  C   . GLY   P  139 ? 1.8849 0.6789 1.2967 -0.0383 -0.6048 -0.1750 138 GLY   P C   
27619 O  O   . GLY   P  139 ? 1.8072 0.7259 1.2423 -0.0450 -0.6409 -0.1588 138 GLY   P O   
27620 N  N   . TYR   P  140 ? 1.9395 0.6870 1.3115 -0.0064 -0.6341 -0.1278 139 TYR   P N   
27621 C  CA  . TYR   P  140 ? 2.0022 0.7601 1.2690 -0.0323 -0.6290 -0.1307 139 TYR   P CA  
27622 C  C   . TYR   P  140 ? 2.0002 0.6974 1.3199 0.0011  -0.5958 -0.1135 139 TYR   P C   
27623 O  O   . TYR   P  140 ? 1.9635 0.5385 1.3471 -0.0289 -0.6354 -0.0908 139 TYR   P O   
27624 C  CB  . TYR   P  140 ? 2.0296 0.8646 1.2780 0.0055  -0.6394 -0.1157 139 TYR   P CB  
27625 C  CG  . TYR   P  140 ? 2.1226 0.8128 1.3221 0.0144  -0.6428 -0.1045 139 TYR   P CG  
27626 C  CD1 . TYR   P  140 ? 2.1487 0.8103 1.2791 -0.0212 -0.6878 -0.0936 139 TYR   P CD1 
27627 C  CD2 . TYR   P  140 ? 2.1570 0.8587 1.2934 0.0341  -0.6640 -0.0693 139 TYR   P CD2 
27628 C  CE1 . TYR   P  140 ? 2.1959 0.8348 1.3032 -0.0142 -0.6974 -0.0704 139 TYR   P CE1 
27629 C  CE2 . TYR   P  140 ? 2.2116 0.8464 1.2852 0.0158  -0.6687 -0.0738 139 TYR   P CE2 
27630 C  CZ  . TYR   P  140 ? 2.2467 0.8355 1.2481 0.0058  -0.6811 -0.0200 139 TYR   P CZ  
27631 O  OH  . TYR   P  140 ? 2.3441 0.9561 1.2300 0.0065  -0.6662 0.0225  139 TYR   P OH  
27632 N  N   . ASP   P  141 ? 2.0292 0.5461 1.3231 0.0142  -0.5589 -0.1680 140 ASP   P N   
27633 C  CA  . ASP   P  141 ? 2.0940 0.5133 1.4042 0.0488  -0.4986 -0.1643 140 ASP   P CA  
27634 C  C   . ASP   P  141 ? 2.0903 0.5976 1.3786 0.0811  -0.5230 -0.2185 140 ASP   P C   
27635 O  O   . ASP   P  141 ? 2.0658 0.3368 1.4851 0.1671  -0.4735 -0.1936 140 ASP   P O   
27636 C  CB  . ASP   P  141 ? 2.1057 0.4553 1.3614 0.0279  -0.4886 -0.1869 140 ASP   P CB  
27637 C  CG  . ASP   P  141 ? 2.2121 0.2928 1.3726 -0.0649 -0.4619 -0.2515 140 ASP   P CG  
27638 O  OD1 . ASP   P  141 ? 2.2388 0.2663 1.3651 -0.0533 -0.4666 -0.2958 140 ASP   P OD1 
27639 O  OD2 . ASP   P  141 ? 2.2227 0.2402 1.3212 -0.1179 -0.4376 -0.2437 140 ASP   P OD2 
27640 N  N   . ASP   P  142 ? 2.1014 0.6660 1.4728 0.0684  -0.5075 -0.0740 141 ASP   P N   
27641 C  CA  . ASP   P  142 ? 2.1147 0.7722 1.4022 0.0333  -0.5069 -0.1190 141 ASP   P CA  
27642 C  C   . ASP   P  142 ? 2.0636 0.7636 1.3912 0.0361  -0.5300 -0.1028 141 ASP   P C   
27643 O  O   . ASP   P  142 ? 2.1269 0.9040 1.3607 -0.0223 -0.4758 -0.1012 141 ASP   P O   
27644 C  CB  . ASP   P  142 ? 2.1514 0.7838 1.5109 0.0236  -0.5030 -0.2002 141 ASP   P CB  
27645 C  CG  . ASP   P  142 ? 2.1491 0.8207 1.5821 0.0223  -0.5118 -0.2375 141 ASP   P CG  
27646 O  OD1 . ASP   P  142 ? 2.1352 0.6716 1.5699 -0.0320 -0.5819 -0.3204 141 ASP   P OD1 
27647 O  OD2 . ASP   P  142 ? 2.1888 0.8404 1.7079 0.1403  -0.4538 -0.1907 141 ASP   P OD2 
27648 N  N   . ARG   P  143 ? 2.0412 0.7074 1.2505 0.0019  -0.5125 -0.0796 142 ARG   P N   
27649 C  CA  . ARG   P  143 ? 2.0459 0.7150 1.2748 0.0137  -0.4936 -0.0396 142 ARG   P CA  
27650 C  C   . ARG   P  143 ? 2.0675 0.7171 1.2830 -0.0120 -0.5029 -0.0215 142 ARG   P C   
27651 O  O   . ARG   P  143 ? 2.1328 0.7323 1.2810 0.0039  -0.4744 0.0990  142 ARG   P O   
27652 C  CB  . ARG   P  143 ? 2.0154 0.7152 1.2784 0.0309  -0.4600 -0.0839 142 ARG   P CB  
27653 C  CG  . ARG   P  143 ? 2.0508 0.7520 1.3007 0.0579  -0.4326 -0.0948 142 ARG   P CG  
27654 C  CD  . ARG   P  143 ? 2.0254 0.7725 1.3032 0.1062  -0.3946 -0.0908 142 ARG   P CD  
27655 N  NE  . ARG   P  143 ? 2.0208 0.7939 1.3238 0.1257  -0.3886 -0.0858 142 ARG   P NE  
27656 C  CZ  . ARG   P  143 ? 1.9929 0.7767 1.3043 0.1502  -0.3397 -0.0992 142 ARG   P CZ  
27657 N  NH1 . ARG   P  143 ? 1.9593 0.7810 1.3162 0.1430  -0.3587 -0.1015 142 ARG   P NH1 
27658 N  NH2 . ARG   P  143 ? 2.0029 0.7796 1.3437 0.1699  -0.3211 -0.1126 142 ARG   P NH2 
27659 N  N   . TYR   P  144 ? 2.0611 0.7207 1.3151 -0.0226 -0.4847 -0.0182 143 TYR   P N   
27660 C  CA  . TYR   P  144 ? 2.0015 0.7040 1.3147 -0.0240 -0.4757 -0.0109 143 TYR   P CA  
27661 C  C   . TYR   P  144 ? 1.9956 0.6580 1.2474 -0.0272 -0.5024 -0.0200 143 TYR   P C   
27662 O  O   . TYR   P  144 ? 1.9642 0.6594 1.2035 -0.0154 -0.5316 -0.0059 143 TYR   P O   
27663 C  CB  . TYR   P  144 ? 1.9840 0.6603 1.3559 -0.0226 -0.4480 -0.0123 143 TYR   P CB  
27664 C  CG  . TYR   P  144 ? 2.0143 0.7399 1.3825 -0.0416 -0.3955 -0.0279 143 TYR   P CG  
27665 C  CD1 . TYR   P  144 ? 2.0149 0.7554 1.3717 -0.0545 -0.3880 0.0096  143 TYR   P CD1 
27666 C  CD2 . TYR   P  144 ? 2.0085 0.7394 1.4047 -0.0616 -0.3807 -0.0556 143 TYR   P CD2 
27667 C  CE1 . TYR   P  144 ? 2.0355 0.6998 1.3471 -0.0844 -0.3587 0.0116  143 TYR   P CE1 
27668 C  CE2 . TYR   P  144 ? 2.0268 0.6679 1.3870 -0.0759 -0.3425 -0.0416 143 TYR   P CE2 
27669 C  CZ  . TYR   P  144 ? 1.9883 0.6245 1.3754 -0.1011 -0.3379 -0.0053 143 TYR   P CZ  
27670 O  OH  . TYR   P  144 ? 2.0030 0.4753 1.3202 -0.1354 -0.3226 0.0234  143 TYR   P OH  
27671 N  N   . GLY   P  145 ? 1.9648 0.6613 1.2534 -0.0445 -0.5166 -0.0402 144 GLY   P N   
27672 C  CA  . GLY   P  145 ? 1.9350 0.6834 1.3371 -0.0132 -0.5256 -0.0824 144 GLY   P CA  
27673 C  C   . GLY   P  145 ? 1.9424 0.5858 1.4521 0.0000  -0.4772 -0.0899 144 GLY   P C   
27674 O  O   . GLY   P  145 ? 1.9270 0.6255 1.5360 0.0906  -0.5110 -0.1532 144 GLY   P O   
27675 N  N   . TYR   P  146 ? 1.9329 0.5341 1.4488 0.0293  -0.4813 -0.0830 145 TYR   P N   
27676 C  CA  . TYR   P  146 ? 1.9063 0.4491 1.5040 0.0144  -0.4847 -0.1147 145 TYR   P CA  
27677 C  C   . TYR   P  146 ? 1.9001 0.4002 1.4809 -0.0060 -0.4655 -0.0886 145 TYR   P C   
27678 O  O   . TYR   P  146 ? 1.8991 0.3172 1.4307 -0.0172 -0.4768 -0.0071 145 TYR   P O   
27679 C  CB  . TYR   P  146 ? 1.9159 0.4668 1.5316 0.0181  -0.5026 -0.1478 145 TYR   P CB  
27680 C  CG  . TYR   P  146 ? 1.9352 0.4489 1.5687 0.0386  -0.5318 -0.1520 145 TYR   P CG  
27681 C  CD1 . TYR   P  146 ? 1.9408 0.5225 1.5973 0.0579  -0.5096 -0.1600 145 TYR   P CD1 
27682 C  CD2 . TYR   P  146 ? 1.9526 0.4314 1.5574 0.0322  -0.5361 -0.1429 145 TYR   P CD2 
27683 C  CE1 . TYR   P  146 ? 1.9331 0.6139 1.6419 0.0875  -0.5271 -0.1200 145 TYR   P CE1 
27684 C  CE2 . TYR   P  146 ? 1.9377 0.5102 1.5828 0.0465  -0.5666 -0.1265 145 TYR   P CE2 
27685 C  CZ  . TYR   P  146 ? 1.9522 0.6021 1.6236 0.0852  -0.5219 -0.1166 145 TYR   P CZ  
27686 O  OH  . TYR   P  146 ? 1.9644 0.7189 1.7524 0.1321  -0.5045 -0.1000 145 TYR   P OH  
27687 N  N   . GLN   P  147 ? 1.8843 0.4362 1.4746 -0.0061 -0.4763 -0.1070 146 GLN   P N   
27688 C  CA  . GLN   P  147 ? 1.8570 0.4746 1.4749 -0.0153 -0.4757 -0.1055 146 GLN   P CA  
27689 C  C   . GLN   P  147 ? 1.8656 0.5316 1.5020 0.0098  -0.4754 -0.0612 146 GLN   P C   
27690 O  O   . GLN   P  147 ? 1.9068 0.4496 1.5405 0.0747  -0.4634 -0.0569 146 GLN   P O   
27691 C  CB  . GLN   P  147 ? 1.8824 0.4145 1.4432 -0.0215 -0.4667 -0.0892 146 GLN   P CB  
27692 C  CG  . GLN   P  147 ? 1.9025 0.4830 1.4495 0.0011  -0.4863 -0.0351 146 GLN   P CG  
27693 C  CD  . GLN   P  147 ? 1.8880 0.4744 1.4557 -0.0154 -0.4953 0.0221  146 GLN   P CD  
27694 O  OE1 . GLN   P  147 ? 1.8933 0.4959 1.4833 0.0323  -0.4743 0.1645  146 GLN   P OE1 
27695 N  NE2 . GLN   P  147 ? 1.9283 0.4225 1.4677 -0.0476 -0.5226 -0.0049 146 GLN   P NE2 
27696 N  N   . LEU   P  148 ? 1.7943 0.5472 1.5206 -0.0213 -0.4767 -0.1251 147 LEU   P N   
27697 C  CA  . LEU   P  148 ? 1.7801 0.5184 1.4888 -0.0468 -0.4574 -0.1517 147 LEU   P CA  
27698 C  C   . LEU   P  148 ? 1.7756 0.4822 1.4732 -0.0601 -0.4266 -0.1655 147 LEU   P C   
27699 O  O   . LEU   P  148 ? 1.8323 0.4511 1.5495 -0.1056 -0.3569 -0.2132 147 LEU   P O   
27700 C  CB  . LEU   P  148 ? 1.7849 0.5321 1.4755 -0.0406 -0.4834 -0.1693 147 LEU   P CB  
27701 C  CG  . LEU   P  148 ? 1.7919 0.5752 1.4795 -0.0328 -0.4789 -0.1675 147 LEU   P CG  
27702 C  CD1 . LEU   P  148 ? 1.8185 0.5902 1.5196 -0.0708 -0.4828 -0.1598 147 LEU   P CD1 
27703 C  CD2 . LEU   P  148 ? 1.7999 0.5457 1.4707 -0.0132 -0.4948 -0.1749 147 LEU   P CD2 
27704 N  N   . TYR   P  149 ? 1.7722 0.4436 1.4467 -0.0717 -0.4096 -0.1923 148 TYR   P N   
27705 C  CA  . TYR   P  149 ? 1.7616 0.4741 1.4103 -0.0758 -0.4179 -0.2406 148 TYR   P CA  
27706 C  C   . TYR   P  149 ? 1.7277 0.4125 1.3754 -0.1226 -0.4200 -0.2992 148 TYR   P C   
27707 O  O   . TYR   P  149 ? 1.7293 0.4118 1.3618 -0.1156 -0.4080 -0.3627 148 TYR   P O   
27708 C  CB  . TYR   P  149 ? 1.7485 0.4529 1.4054 -0.0659 -0.4179 -0.2139 148 TYR   P CB  
27709 C  CG  . TYR   P  149 ? 1.7818 0.4611 1.4003 -0.0196 -0.4211 -0.1957 148 TYR   P CG  
27710 C  CD1 . TYR   P  149 ? 1.7935 0.4622 1.3921 -0.0260 -0.4176 -0.1784 148 TYR   P CD1 
27711 C  CD2 . TYR   P  149 ? 1.8197 0.3874 1.3833 -0.0514 -0.4183 -0.2008 148 TYR   P CD2 
27712 C  CE1 . TYR   P  149 ? 1.8216 0.4139 1.3915 -0.0267 -0.4329 -0.1979 148 TYR   P CE1 
27713 C  CE2 . TYR   P  149 ? 1.8402 0.3658 1.3803 -0.0158 -0.4394 -0.1987 148 TYR   P CE2 
27714 C  CZ  . TYR   P  149 ? 1.8520 0.4190 1.3782 -0.0102 -0.4409 -0.2165 148 TYR   P CZ  
27715 O  OH  . TYR   P  149 ? 1.9334 0.5327 1.3038 0.0054  -0.4485 -0.1887 148 TYR   P OH  
27716 N  N   . THR   P  150 ? 1.7234 0.3800 1.3562 -0.1332 -0.4286 -0.3428 149 THR   P N   
27717 C  CA  . THR   P  150 ? 1.7524 0.4476 1.3288 -0.1371 -0.4076 -0.3319 149 THR   P CA  
27718 C  C   . THR   P  150 ? 1.7634 0.4014 1.3386 -0.1237 -0.4160 -0.3544 149 THR   P C   
27719 O  O   . THR   P  150 ? 1.8026 0.4017 1.3867 -0.0977 -0.3686 -0.3533 149 THR   P O   
27720 C  CB  . THR   P  150 ? 1.7491 0.4709 1.2809 -0.1658 -0.3940 -0.3604 149 THR   P CB  
27721 O  OG1 . THR   P  150 ? 1.7624 0.4832 1.3063 -0.1596 -0.3761 -0.3845 149 THR   P OG1 
27722 C  CG2 . THR   P  150 ? 1.7487 0.5482 1.2960 -0.1704 -0.3955 -0.3501 149 THR   P CG2 
27723 N  N   . SER   P  151 ? 1.8194 0.4210 1.3371 -0.1107 -0.4191 -0.3623 150 SER   P N   
27724 C  CA  . SER   P  151 ? 1.8369 0.5365 1.3435 -0.0977 -0.4309 -0.3188 150 SER   P CA  
27725 C  C   . SER   P  151 ? 1.7996 0.5268 1.3517 -0.1344 -0.4307 -0.3167 150 SER   P C   
27726 O  O   . SER   P  151 ? 1.7824 0.4020 1.2953 -0.2018 -0.5032 -0.3822 150 SER   P O   
27727 C  CB  . SER   P  151 ? 1.8581 0.5743 1.3704 -0.1178 -0.4432 -0.3474 150 SER   P CB  
27728 O  OG  . SER   P  151 ? 1.8920 0.6918 1.3779 -0.0909 -0.4375 -0.3683 150 SER   P OG  
27729 N  N   . ASN   P  152 ? 1.8243 0.5752 1.3512 -0.1086 -0.4117 -0.2248 151 ASN   P N   
27730 C  CA  . ASN   P  152 ? 1.8008 0.5932 1.3766 -0.1227 -0.3964 -0.1939 151 ASN   P CA  
27731 C  C   . ASN   P  152 ? 1.7828 0.6028 1.3773 -0.0975 -0.4083 -0.1378 151 ASN   P C   
27732 O  O   . ASN   P  152 ? 1.6872 0.7039 1.3113 -0.1479 -0.4630 -0.1772 151 ASN   P O   
27733 C  CB  . ASN   P  152 ? 1.7970 0.6118 1.3342 -0.1033 -0.3657 -0.1862 151 ASN   P CB  
27734 C  CG  . ASN   P  152 ? 1.8079 0.6191 1.3040 -0.1009 -0.3610 -0.1819 151 ASN   P CG  
27735 O  OD1 . ASN   P  152 ? 1.7861 0.4836 1.2876 -0.1136 -0.3215 -0.1574 151 ASN   P OD1 
27736 N  ND2 . ASN   P  152 ? 1.8136 0.7364 1.2954 -0.1009 -0.3619 -0.1894 151 ASN   P ND2 
27737 N  N   . PRO   P  153 ? 1.7824 0.5626 1.4461 -0.0960 -0.3797 -0.1012 152 PRO   P N   
27738 C  CA  . PRO   P  153 ? 1.7809 0.5578 1.4719 -0.1113 -0.3925 -0.0436 152 PRO   P CA  
27739 C  C   . PRO   P  153 ? 1.8441 0.5977 1.5404 -0.0769 -0.2992 0.0444  152 PRO   P C   
27740 O  O   . PRO   P  153 ? 1.8232 0.5579 1.6607 -0.1325 -0.3908 0.2125  152 PRO   P O   
27741 C  CB  . PRO   P  153 ? 1.7821 0.5091 1.4749 -0.1023 -0.3606 -0.0825 152 PRO   P CB  
27742 C  CG  . PRO   P  153 ? 1.7663 0.5442 1.4482 -0.0825 -0.3661 -0.0788 152 PRO   P CG  
27743 C  CD  . PRO   P  153 ? 1.7662 0.5690 1.4362 -0.0920 -0.3744 -0.1006 152 PRO   P CD  
27744 N  N   . SER   P  154 ? 1.8543 0.5773 1.5217 -0.1035 -0.3315 0.0194  153 SER   P N   
27745 C  CA  . SER   P  154 ? 1.8831 0.6670 1.4793 -0.0845 -0.2956 0.0034  153 SER   P CA  
27746 C  C   . SER   P  154 ? 1.9448 0.6839 1.5256 -0.1110 -0.2927 0.0221  153 SER   P C   
27747 O  O   . SER   P  154 ? 1.9602 0.9451 1.6463 -0.1314 -0.1486 0.0504  153 SER   P O   
27748 C  CB  . SER   P  154 ? 1.8500 0.6751 1.4296 -0.0641 -0.2978 0.0423  153 SER   P CB  
27749 O  OG  . SER   P  154 ? 1.8370 0.7323 1.3936 -0.0619 -0.2765 0.0460  153 SER   P OG  
27750 N  N   . GLY   P  155 ? 1.9283 0.7122 1.4953 -0.1224 -0.3533 0.0180  154 GLY   P N   
27751 C  CA  . GLY   P  155 ? 1.9757 0.7127 1.5136 -0.0872 -0.3516 0.0160  154 GLY   P CA  
27752 C  C   . GLY   P  155 ? 2.0082 0.7054 1.4895 -0.1224 -0.3790 -0.1026 154 GLY   P C   
27753 O  O   . GLY   P  155 ? 2.0916 0.7754 1.3968 -0.0917 -0.3843 -0.0235 154 GLY   P O   
27754 N  N   . ASN   P  156 ? 1.9777 0.6453 1.5324 -0.1636 -0.3590 -0.0599 155 ASN   P N   
27755 C  CA  . ASN   P  156 ? 1.9586 0.6107 1.5312 -0.1481 -0.3510 -0.0140 155 ASN   P CA  
27756 C  C   . ASN   P  156 ? 1.9693 0.4764 1.5384 -0.1096 -0.3615 -0.0059 155 ASN   P C   
27757 O  O   . ASN   P  156 ? 1.9192 0.5939 1.5399 -0.0651 -0.3277 0.0017  155 ASN   P O   
27758 C  CB  . ASN   P  156 ? 2.0500 0.6402 1.5775 -0.1111 -0.3101 -0.0195 155 ASN   P CB  
27759 C  CG  . ASN   P  156 ? 2.1596 0.7832 1.5590 -0.1159 -0.2565 0.0583  155 ASN   P CG  
27760 O  OD1 . ASN   P  156 ? 2.2505 0.9258 1.6406 -0.1802 -0.2788 -0.0344 155 ASN   P OD1 
27761 N  ND2 . ASN   P  156 ? 2.1894 0.6779 1.6423 -0.2244 -0.2456 -0.0286 155 ASN   P ND2 
27762 N  N   . TYR   P  157 ? 1.8508 0.3830 1.5852 -0.0869 -0.3849 -0.0405 156 TYR   P N   
27763 C  CA  . TYR   P  157 ? 1.8561 0.3889 1.6033 -0.0956 -0.4075 -0.0422 156 TYR   P CA  
27764 C  C   . TYR   P  157 ? 1.8628 0.3306 1.6028 -0.0803 -0.4083 -0.0161 156 TYR   P C   
27765 O  O   . TYR   P  157 ? 1.8454 0.3450 1.6216 -0.0119 -0.3864 -0.0221 156 TYR   P O   
27766 C  CB  . TYR   P  157 ? 1.7952 0.4113 1.5581 -0.0931 -0.4386 -0.0619 156 TYR   P CB  
27767 C  CG  . TYR   P  157 ? 1.7531 0.3905 1.5252 -0.0852 -0.4706 -0.0717 156 TYR   P CG  
27768 C  CD1 . TYR   P  157 ? 1.7325 0.3941 1.5335 -0.0717 -0.4541 -0.0600 156 TYR   P CD1 
27769 C  CD2 . TYR   P  157 ? 1.7344 0.3684 1.5078 -0.1119 -0.4807 -0.0861 156 TYR   P CD2 
27770 C  CE1 . TYR   P  157 ? 1.7297 0.4091 1.5073 -0.0507 -0.4518 -0.0402 156 TYR   P CE1 
27771 C  CE2 . TYR   P  157 ? 1.7376 0.3663 1.4932 -0.0781 -0.4784 -0.0656 156 TYR   P CE2 
27772 C  CZ  . TYR   P  157 ? 1.7135 0.4010 1.4989 -0.0763 -0.4500 -0.0329 156 TYR   P CZ  
27773 O  OH  . TYR   P  157 ? 1.7002 0.5003 1.4941 -0.0782 -0.4179 0.0295  156 TYR   P OH  
27774 N  N   . THR   P  158 ? 1.9008 0.2634 1.6049 -0.0889 -0.4511 0.0161  157 THR   P N   
27775 C  CA  . THR   P  158 ? 1.9272 0.3764 1.6039 -0.1056 -0.4520 0.0301  157 THR   P CA  
27776 C  C   . THR   P  158 ? 1.9413 0.3862 1.5546 -0.1152 -0.5013 0.0065  157 THR   P C   
27777 O  O   . THR   P  158 ? 1.9389 0.3122 1.5431 -0.1761 -0.5096 -0.0168 157 THR   P O   
27778 C  CB  . THR   P  158 ? 1.9442 0.3926 1.6638 -0.1123 -0.3937 0.0112  157 THR   P CB  
27779 O  OG1 . THR   P  158 ? 1.9703 0.5057 1.7862 -0.1971 -0.3446 0.0342  157 THR   P OG1 
27780 C  CG2 . THR   P  158 ? 1.9304 0.4736 1.6593 -0.1371 -0.3514 0.0324  157 THR   P CG2 
27781 N  N   . GLY   P  159 ? 1.9434 0.4721 1.5371 -0.0879 -0.5090 -0.0045 158 GLY   P N   
27782 C  CA  . GLY   P  159 ? 1.9886 0.4748 1.4778 -0.0338 -0.5082 0.0353  158 GLY   P CA  
27783 C  C   . GLY   P  159 ? 1.9429 0.4883 1.4356 -0.0185 -0.5170 0.0487  158 GLY   P C   
27784 O  O   . GLY   P  159 ? 1.9877 0.5508 1.3890 -0.0304 -0.4781 0.0335  158 GLY   P O   
27785 N  N   . TRP   P  160 ? 1.9326 0.4920 1.4217 0.0324  -0.5322 0.0737  159 TRP   P N   
27786 C  CA  . TRP   P  160 ? 1.9279 0.5315 1.4591 0.0459  -0.5223 -0.0067 159 TRP   P CA  
27787 C  C   . TRP   P  160 ? 1.9204 0.5637 1.4878 0.0513  -0.5105 0.0277  159 TRP   P C   
27788 O  O   . TRP   P  160 ? 1.9032 0.6577 1.5634 0.1064  -0.4448 -0.0277 159 TRP   P O   
27789 C  CB  . TRP   P  160 ? 1.9286 0.5564 1.4101 0.0506  -0.5273 -0.0281 159 TRP   P CB  
27790 C  CG  . TRP   P  160 ? 1.9453 0.5308 1.4346 0.0954  -0.5150 -0.0558 159 TRP   P CG  
27791 C  CD1 . TRP   P  160 ? 1.9311 0.5455 1.4327 0.1172  -0.5222 -0.0467 159 TRP   P CD1 
27792 C  CD2 . TRP   P  160 ? 1.9631 0.5585 1.4188 0.0959  -0.5218 -0.0968 159 TRP   P CD2 
27793 N  NE1 . TRP   P  160 ? 1.9190 0.5626 1.4351 0.1218  -0.5267 -0.0892 159 TRP   P NE1 
27794 C  CE2 . TRP   P  160 ? 1.9524 0.5604 1.4416 0.1153  -0.5191 -0.0947 159 TRP   P CE2 
27795 C  CE3 . TRP   P  160 ? 1.9559 0.5344 1.4471 0.0938  -0.5172 -0.1087 159 TRP   P CE3 
27796 C  CZ2 . TRP   P  160 ? 1.9927 0.4988 1.4174 0.0994  -0.5263 -0.1105 159 TRP   P CZ2 
27797 C  CZ3 . TRP   P  160 ? 2.0065 0.4535 1.4246 0.0677  -0.5183 -0.1305 159 TRP   P CZ3 
27798 C  CH2 . TRP   P  160 ? 2.0209 0.4455 1.4238 0.0949  -0.5164 -0.0998 159 TRP   P CH2 
27799 N  N   . LYS   P  161 ? 1.9164 0.5105 1.4858 0.0996  -0.4756 -0.0091 160 LYS   P N   
27800 C  CA  . LYS   P  161 ? 1.9010 0.6022 1.4707 0.0677  -0.4638 -0.0630 160 LYS   P CA  
27801 C  C   . LYS   P  161 ? 1.9348 0.5478 1.4719 0.0220  -0.4815 -0.0823 160 LYS   P C   
27802 O  O   . LYS   P  161 ? 1.9146 0.5613 1.4438 0.0160  -0.5060 -0.0476 160 LYS   P O   
27803 C  CB  . LYS   P  161 ? 1.9224 0.6576 1.5082 0.0681  -0.4363 -0.1309 160 LYS   P CB  
27804 C  CG  . LYS   P  161 ? 1.9209 0.7819 1.4943 0.0685  -0.3786 -0.1636 160 LYS   P CG  
27805 C  CD  . LYS   P  161 ? 1.9328 0.8590 1.5425 0.0806  -0.3660 -0.2282 160 LYS   P CD  
27806 C  CE  . LYS   P  161 ? 1.9213 0.9744 1.5250 0.0830  -0.3204 -0.2509 160 LYS   P CE  
27807 N  NZ  . LYS   P  161 ? 1.9323 1.0325 1.5518 0.0647  -0.3332 -0.2906 160 LYS   P NZ  
27808 N  N   . ALA   P  162 ? 1.9082 0.4890 1.4453 -0.0375 -0.4857 -0.1186 161 ALA   P N   
27809 C  CA  . ALA   P  162 ? 1.8998 0.5180 1.4485 -0.0912 -0.4651 -0.1609 161 ALA   P CA  
27810 C  C   . ALA   P  162 ? 1.8780 0.4366 1.4609 -0.0962 -0.4382 -0.1833 161 ALA   P C   
27811 O  O   . ALA   P  162 ? 1.9218 0.3428 1.5512 -0.0933 -0.4173 -0.2302 161 ALA   P O   
27812 C  CB  . ALA   P  162 ? 1.9083 0.5712 1.4356 -0.1139 -0.4842 -0.1418 161 ALA   P CB  
27813 N  N   . ILE   P  163 ? 1.8312 0.4276 1.4571 -0.1120 -0.4471 -0.1808 162 ILE   P N   
27814 C  CA  . ILE   P  163 ? 1.8170 0.4244 1.4337 -0.1179 -0.4396 -0.1805 162 ILE   P CA  
27815 C  C   . ILE   P  163 ? 1.8157 0.4354 1.4332 -0.1219 -0.4508 -0.1639 162 ILE   P C   
27816 O  O   . ILE   P  163 ? 1.8077 0.4604 1.4045 -0.1016 -0.4655 -0.1235 162 ILE   P O   
27817 C  CB  . ILE   P  163 ? 1.7970 0.4467 1.4341 -0.1090 -0.4375 -0.1955 162 ILE   P CB  
27818 C  CG1 . ILE   P  163 ? 1.8148 0.4259 1.4470 -0.0993 -0.4275 -0.1882 162 ILE   P CG1 
27819 C  CG2 . ILE   P  163 ? 1.7786 0.4736 1.4171 -0.0993 -0.4417 -0.2062 162 ILE   P CG2 
27820 C  CD1 . ILE   P  163 ? 1.8452 0.4301 1.4686 -0.1128 -0.4115 -0.2057 162 ILE   P CD1 
27821 N  N   . SER   P  164 ? 1.8124 0.4326 1.4321 -0.1223 -0.4315 -0.1581 163 SER   P N   
27822 C  CA  . SER   P  164 ? 1.8251 0.3989 1.4483 -0.1237 -0.4323 -0.1379 163 SER   P CA  
27823 C  C   . SER   P  164 ? 1.8282 0.3608 1.4203 -0.1194 -0.4211 -0.0995 163 SER   P C   
27824 O  O   . SER   P  164 ? 1.8482 0.3247 1.4375 -0.1358 -0.3892 -0.0391 163 SER   P O   
27825 C  CB  . SER   P  164 ? 1.8517 0.3947 1.4674 -0.1241 -0.4214 -0.1510 163 SER   P CB  
27826 O  OG  . SER   P  164 ? 1.8982 0.3212 1.5248 -0.1330 -0.4150 -0.1626 163 SER   P OG  
27827 N  N   . VAL   P  165 ? 1.8106 0.3617 1.4045 -0.1358 -0.4626 -0.1032 164 VAL   P N   
27828 C  CA  . VAL   P  165 ? 1.8201 0.4673 1.4058 -0.1377 -0.4755 -0.1000 164 VAL   P CA  
27829 C  C   . VAL   P  165 ? 1.7897 0.4227 1.3639 -0.1716 -0.5370 -0.1261 164 VAL   P C   
27830 O  O   . VAL   P  165 ? 1.7896 0.4433 1.3899 -0.2085 -0.5467 -0.1482 164 VAL   P O   
27831 C  CB  . VAL   P  165 ? 1.8072 0.4866 1.3874 -0.1540 -0.4887 -0.0850 164 VAL   P CB  
27832 C  CG1 . VAL   P  165 ? 1.7986 0.5625 1.3823 -0.1291 -0.4767 -0.0566 164 VAL   P CG1 
27833 C  CG2 . VAL   P  165 ? 1.8197 0.5668 1.3806 -0.1292 -0.4648 -0.0681 164 VAL   P CG2 
27834 N  N   . GLY   P  166 ? 1.7768 0.4283 1.3450 -0.1829 -0.5441 -0.1353 165 GLY   P N   
27835 C  CA  . GLY   P  166 ? 1.7876 0.4937 1.3474 -0.1493 -0.5392 -0.0959 165 GLY   P CA  
27836 C  C   . GLY   P  166 ? 1.8182 0.4931 1.3652 -0.1173 -0.5297 -0.1012 165 GLY   P C   
27837 O  O   . GLY   P  166 ? 1.8425 0.4693 1.3600 -0.0738 -0.5224 -0.0622 165 GLY   P O   
27838 N  N   . ALA   P  167 ? 1.8025 0.6070 1.4050 -0.1259 -0.5180 -0.0874 166 ALA   P N   
27839 C  CA  . ALA   P  167 ? 1.8269 0.6142 1.4398 -0.1515 -0.5064 -0.0902 166 ALA   P CA  
27840 C  C   . ALA   P  167 ? 1.8519 0.6312 1.4531 -0.1597 -0.5160 -0.1167 166 ALA   P C   
27841 O  O   . ALA   P  167 ? 1.8749 0.6763 1.4458 -0.1297 -0.5340 -0.1274 166 ALA   P O   
27842 C  CB  . ALA   P  167 ? 1.8354 0.6254 1.4622 -0.1613 -0.4965 -0.0783 166 ALA   P CB  
27843 N  N   . ASN   P  168 ? 1.8748 0.6096 1.4919 -0.1759 -0.4946 -0.1184 167 ASN   P N   
27844 C  CA  . ASN   P  168 ? 1.9011 0.6153 1.5053 -0.2047 -0.4832 -0.1340 167 ASN   P CA  
27845 C  C   . ASN   P  168 ? 1.9069 0.5061 1.5451 -0.2291 -0.4461 -0.1676 167 ASN   P C   
27846 O  O   . ASN   P  168 ? 1.9355 0.3542 1.5295 -0.3212 -0.4597 -0.1398 167 ASN   P O   
27847 C  CB  . ASN   P  168 ? 1.9086 0.7505 1.5234 -0.2259 -0.4793 -0.1106 167 ASN   P CB  
27848 C  CG  . ASN   P  168 ? 1.9340 0.8223 1.5191 -0.1770 -0.4977 -0.0661 167 ASN   P CG  
27849 O  OD1 . ASN   P  168 ? 1.8731 0.9582 1.5633 -0.1215 -0.4949 -0.0476 167 ASN   P OD1 
27850 N  ND2 . ASN   P  168 ? 1.9875 0.8417 1.4656 -0.1907 -0.4742 -0.0663 167 ASN   P ND2 
27851 N  N   . THR   P  169 ? 1.8640 0.4900 1.5791 -0.1904 -0.4250 -0.2093 168 THR   P N   
27852 C  CA  . THR   P  169 ? 1.8532 0.5102 1.5440 -0.1812 -0.4050 -0.2318 168 THR   P CA  
27853 C  C   . THR   P  169 ? 1.8649 0.3999 1.6063 -0.1630 -0.4394 -0.2776 168 THR   P C   
27854 O  O   . THR   P  169 ? 1.8729 0.3258 1.5163 -0.2342 -0.4509 -0.3598 168 THR   P O   
27855 C  CB  . THR   P  169 ? 1.8188 0.5840 1.5799 -0.1866 -0.4005 -0.2139 168 THR   P CB  
27856 O  OG1 . THR   P  169 ? 1.8670 0.5252 1.6210 -0.1853 -0.3861 -0.1755 168 THR   P OG1 
27857 C  CG2 . THR   P  169 ? 1.8285 0.5760 1.5935 -0.1566 -0.3768 -0.2102 168 THR   P CG2 
27858 N  N   . SER   P  170 ? 1.8878 0.4555 1.5629 -0.0989 -0.4343 -0.2933 169 SER   P N   
27859 C  CA  . SER   P  170 ? 1.8960 0.4386 1.5828 -0.0613 -0.4270 -0.2910 169 SER   P CA  
27860 C  C   . SER   P  170 ? 1.8713 0.3799 1.6071 -0.0882 -0.4006 -0.3077 169 SER   P C   
27861 O  O   . SER   P  170 ? 1.8047 0.3788 1.6119 -0.0878 -0.4250 -0.3244 169 SER   P O   
27862 C  CB  . SER   P  170 ? 1.9845 0.4141 1.6553 -0.0511 -0.4121 -0.2792 169 SER   P CB  
27863 O  OG  . SER   P  170 ? 2.0099 0.4250 1.6849 0.0014  -0.3896 -0.2554 169 SER   P OG  
27864 N  N   . ALA   P  171 ? 1.8904 0.3553 1.5613 -0.1161 -0.4143 -0.3094 170 ALA   P N   
27865 C  CA  . ALA   P  171 ? 1.9030 0.4858 1.5908 -0.1670 -0.4136 -0.2869 170 ALA   P CA  
27866 C  C   . ALA   P  171 ? 1.8930 0.5171 1.6350 -0.1649 -0.4047 -0.2490 170 ALA   P C   
27867 O  O   . ALA   P  171 ? 1.9346 0.6742 1.6716 -0.1818 -0.4352 -0.2481 170 ALA   P O   
27868 C  CB  . ALA   P  171 ? 1.9266 0.5299 1.5711 -0.1454 -0.3978 -0.2747 170 ALA   P CB  
27869 N  N   . ALA   P  172 ? 1.8534 0.5604 1.5495 -0.1581 -0.4221 -0.2350 171 ALA   P N   
27870 C  CA  . ALA   P  172 ? 1.8378 0.5554 1.5203 -0.1769 -0.4360 -0.1859 171 ALA   P CA  
27871 C  C   . ALA   P  172 ? 1.8528 0.4748 1.5324 -0.1468 -0.4749 -0.1424 171 ALA   P C   
27872 O  O   . ALA   P  172 ? 1.8284 0.4831 1.5097 -0.1925 -0.4781 -0.1346 171 ALA   P O   
27873 C  CB  . ALA   P  172 ? 1.7986 0.5601 1.5191 -0.1706 -0.4548 -0.1856 171 ALA   P CB  
27874 N  N   . GLN   P  173 ? 1.8581 0.4536 1.5018 -0.1409 -0.4740 -0.0944 172 GLN   P N   
27875 C  CA  . GLN   P  173 ? 1.8660 0.5591 1.4728 -0.1382 -0.4821 -0.0770 172 GLN   P CA  
27876 C  C   . GLN   P  173 ? 1.9092 0.6188 1.4854 -0.1320 -0.4623 -0.1192 172 GLN   P C   
27877 O  O   . GLN   P  173 ? 1.9044 0.6324 1.4873 -0.1936 -0.4813 -0.1099 172 GLN   P O   
27878 C  CB  . GLN   P  173 ? 1.8699 0.5419 1.4664 -0.1319 -0.5169 -0.0787 172 GLN   P CB  
27879 C  CG  . GLN   P  173 ? 1.8717 0.5813 1.4670 -0.1556 -0.5213 -0.0685 172 GLN   P CG  
27880 C  CD  . GLN   P  173 ? 1.8832 0.5842 1.5098 -0.1713 -0.4915 -0.0829 172 GLN   P CD  
27881 O  OE1 . GLN   P  173 ? 1.8662 0.5264 1.5096 -0.1607 -0.4783 -0.0382 172 GLN   P OE1 
27882 N  NE2 . GLN   P  173 ? 1.8980 0.6074 1.5681 -0.1573 -0.4513 -0.0507 172 GLN   P NE2 
27883 N  N   . THR   P  174 ? 1.9308 0.6205 1.4137 -0.0887 -0.4331 -0.0927 173 THR   P N   
27884 C  CA  . THR   P  174 ? 1.9866 0.7458 1.3802 -0.0767 -0.4269 -0.1219 173 THR   P CA  
27885 C  C   . THR   P  174 ? 2.0104 0.7279 1.4142 -0.0613 -0.4504 -0.1479 173 THR   P C   
27886 O  O   . THR   P  174 ? 2.1058 0.7951 1.4199 -0.0211 -0.4717 -0.1573 173 THR   P O   
27887 C  CB  . THR   P  174 ? 1.9655 0.7556 1.3239 -0.0633 -0.4182 -0.1165 173 THR   P CB  
27888 O  OG1 . THR   P  174 ? 1.9502 0.7424 1.3038 -0.0149 -0.3734 -0.0911 173 THR   P OG1 
27889 C  CG2 . THR   P  174 ? 1.9919 0.7831 1.3374 -0.0711 -0.4118 -0.1360 173 THR   P CG2 
27890 N  N   . LEU   P  175 ? 2.0659 0.7368 1.3960 -0.0918 -0.4334 -0.1718 174 LEU   P N   
27891 C  CA  . LEU   P  175 ? 2.0520 0.7845 1.4266 -0.1322 -0.4585 -0.2324 174 LEU   P CA  
27892 C  C   . LEU   P  175 ? 2.0345 0.7996 1.4148 -0.0479 -0.4713 -0.2423 174 LEU   P C   
27893 O  O   . LEU   P  175 ? 2.0025 0.7226 1.4203 0.0043  -0.4826 -0.3775 174 LEU   P O   
27894 C  CB  . LEU   P  175 ? 2.0367 0.9221 1.4603 -0.1815 -0.4330 -0.2871 174 LEU   P CB  
27895 C  CG  . LEU   P  175 ? 2.0699 0.9495 1.5523 -0.2329 -0.4575 -0.2880 174 LEU   P CG  
27896 C  CD1 . LEU   P  175 ? 2.0576 1.0113 1.5585 -0.2295 -0.4590 -0.2980 174 LEU   P CD1 
27897 C  CD2 . LEU   P  175 ? 2.0903 1.0943 1.5690 -0.2426 -0.4772 -0.3288 174 LEU   P CD2 
27898 N  N   . LEU   P  176 ? 2.0328 0.6956 1.4699 -0.0618 -0.4515 -0.1597 175 LEU   P N   
27899 C  CA  . LEU   P  176 ? 2.0164 0.7251 1.4854 -0.0871 -0.4583 -0.0953 175 LEU   P CA  
27900 C  C   . LEU   P  176 ? 2.0319 0.7218 1.5291 -0.0819 -0.4140 -0.0375 175 LEU   P C   
27901 O  O   . LEU   P  176 ? 1.9726 0.8986 1.5564 -0.0749 -0.4351 0.0036  175 LEU   P O   
27902 C  CB  . LEU   P  176 ? 2.0492 0.6224 1.4669 -0.0812 -0.4516 -0.0761 175 LEU   P CB  
27903 C  CG  . LEU   P  176 ? 2.0516 0.5854 1.4576 -0.1238 -0.4610 -0.0823 175 LEU   P CG  
27904 C  CD1 . LEU   P  176 ? 2.0538 0.5892 1.4613 -0.1362 -0.4539 -0.0746 175 LEU   P CD1 
27905 C  CD2 . LEU   P  176 ? 2.0086 0.6118 1.4441 -0.1501 -0.4980 -0.0844 175 LEU   P CD2 
27906 N  N   . GLN   P  177 ? 2.0748 0.6442 1.5688 -0.0669 -0.4113 -0.0234 176 GLN   P N   
27907 C  CA  . GLN   P  177 ? 2.1012 0.6867 1.5644 -0.0404 -0.4198 -0.1171 176 GLN   P CA  
27908 C  C   . GLN   P  177 ? 2.1226 0.6504 1.6176 -0.0998 -0.4247 -0.1402 176 GLN   P C   
27909 O  O   . GLN   P  177 ? 2.0944 0.6770 1.5244 -0.1834 -0.4845 -0.2725 176 GLN   P O   
27910 C  CB  . GLN   P  177 ? 2.1854 0.7322 1.6522 0.0398  -0.4083 -0.1402 176 GLN   P CB  
27911 C  CG  . GLN   P  177 ? 2.2390 0.8506 1.6610 0.1374  -0.3749 -0.1773 176 GLN   P CG  
27912 C  CD  . GLN   P  177 ? 2.2967 0.9658 1.7019 0.2271  -0.3731 -0.2282 176 GLN   P CD  
27913 O  OE1 . GLN   P  177 ? 2.3905 1.1204 1.6899 0.3546  -0.3818 -0.3260 176 GLN   P OE1 
27914 N  NE2 . GLN   P  177 ? 2.3059 0.9982 1.7379 0.2429  -0.4051 -0.2008 176 GLN   P NE2 
27915 N  N   . MET   P  178 ? 2.1262 0.7123 1.6070 -0.1044 -0.4126 -0.1020 177 MET   P N   
27916 C  CA  . MET   P  178 ? 2.1450 0.8521 1.6347 -0.0848 -0.4391 -0.1622 177 MET   P CA  
27917 C  C   . MET   P  178 ? 2.1466 0.8667 1.5953 -0.1055 -0.4871 -0.1485 177 MET   P C   
27918 O  O   . MET   P  178 ? 2.1011 0.8372 1.6038 -0.1230 -0.5066 -0.1769 177 MET   P O   
27919 C  CB  . MET   P  178 ? 2.1671 0.9448 1.7421 -0.1161 -0.3367 -0.1452 177 MET   P CB  
27920 C  CG  . MET   P  178 ? 2.2042 0.9970 1.8245 -0.1141 -0.3166 -0.2127 177 MET   P CG  
27921 S  SD  . MET   P  178 ? 2.2653 1.0161 1.9883 -0.0363 -0.1930 -0.1455 177 MET   P SD  
27922 C  CE  . MET   P  178 ? 2.2524 1.0691 1.9874 -0.0212 -0.2167 -0.0933 177 MET   P CE  
27923 N  N   . ASP   P  179 ? 2.1458 0.9475 1.5263 -0.0741 -0.5471 -0.1631 178 ASP   P N   
27924 C  CA  . ASP   P  179 ? 2.1433 1.0113 1.5021 -0.0807 -0.6054 -0.1630 178 ASP   P CA  
27925 C  C   . ASP   P  179 ? 2.0913 1.0048 1.5030 -0.0735 -0.6222 -0.1779 178 ASP   P C   
27926 O  O   . ASP   P  179 ? 2.1304 0.9676 1.5613 -0.0524 -0.6157 -0.1764 178 ASP   P O   
27927 C  CB  . ASP   P  179 ? 2.1482 1.0137 1.4470 -0.0813 -0.6393 -0.1335 178 ASP   P CB  
27928 C  CG  . ASP   P  179 ? 2.1944 1.0073 1.4239 -0.0751 -0.6700 -0.0997 178 ASP   P CG  
27929 O  OD1 . ASP   P  179 ? 2.2459 1.0129 1.3826 0.0081  -0.6459 -0.0364 178 ASP   P OD1 
27930 O  OD2 . ASP   P  179 ? 2.2138 1.0112 1.3504 -0.0565 -0.6977 -0.1309 178 ASP   P OD2 
27931 N  N   . TYR   P  180 ? 2.1059 0.9854 1.4842 -0.0954 -0.6078 -0.1866 179 TYR   P N   
27932 C  CA  . TYR   P  180 ? 2.1355 0.9822 1.4975 -0.0584 -0.5717 -0.1652 179 TYR   P CA  
27933 C  C   . TYR   P  180 ? 2.2164 1.0618 1.4895 -0.0498 -0.5413 -0.1913 179 TYR   P C   
27934 O  O   . TYR   P  180 ? 2.2637 1.0762 1.4741 -0.1064 -0.5784 -0.2799 179 TYR   P O   
27935 C  CB  . TYR   P  180 ? 2.1231 0.9493 1.4332 -0.0636 -0.5409 -0.1650 179 TYR   P CB  
27936 C  CG  . TYR   P  180 ? 2.0590 0.9734 1.3602 -0.1333 -0.5678 -0.1961 179 TYR   P CG  
27937 C  CD1 . TYR   P  180 ? 2.0618 1.0247 1.3624 -0.1275 -0.5377 -0.1934 179 TYR   P CD1 
27938 C  CD2 . TYR   P  180 ? 2.0614 1.0107 1.3219 -0.1339 -0.5663 -0.2180 179 TYR   P CD2 
27939 C  CE1 . TYR   P  180 ? 2.1216 1.0174 1.4038 -0.0897 -0.4873 -0.1460 179 TYR   P CE1 
27940 C  CE2 . TYR   P  180 ? 2.1205 1.0048 1.3859 -0.1078 -0.5331 -0.1713 179 TYR   P CE2 
27941 C  CZ  . TYR   P  180 ? 2.1322 1.0284 1.4213 -0.0794 -0.4755 -0.1345 179 TYR   P CZ  
27942 O  OH  . TYR   P  180 ? 2.1984 1.0507 1.5330 -0.1296 -0.4825 -0.0517 179 TYR   P OH  
27943 N  N   . LYS   P  181 ? 2.2615 1.1199 1.5931 -0.0031 -0.5507 -0.1463 180 LYS   P N   
27944 C  CA  . LYS   P  181 ? 2.2571 1.1794 1.5781 0.0271  -0.5872 -0.1276 180 LYS   P CA  
27945 C  C   . LYS   P  181 ? 2.3054 1.1865 1.5885 0.0511  -0.5246 -0.1456 180 LYS   P C   
27946 O  O   . LYS   P  181 ? 2.4179 1.0496 1.6745 0.1088  -0.5303 -0.2400 180 LYS   P O   
27947 C  CB  . LYS   P  181 ? 2.2073 1.1948 1.6370 0.0276  -0.5958 -0.1498 180 LYS   P CB  
27948 C  CG  . LYS   P  181 ? 2.1909 1.2787 1.6933 0.0597  -0.5719 -0.1357 180 LYS   P CG  
27949 C  CD  . LYS   P  181 ? 2.1668 1.3508 1.7386 0.0527  -0.5664 -0.1767 180 LYS   P CD  
27950 C  CE  . LYS   P  181 ? 2.1473 1.4587 1.7320 0.0571  -0.5803 -0.1719 180 LYS   P CE  
27951 N  NZ  . LYS   P  181 ? 2.0819 1.5470 1.7370 0.0965  -0.6114 -0.1596 180 LYS   P NZ  
27952 N  N   . ASP   P  182 ? 2.3045 1.1783 1.6362 0.0191  -0.5221 -0.1372 181 ASP   P N   
27953 C  CA  . ASP   P  182 ? 2.2399 1.1683 1.6102 0.0244  -0.4638 -0.1101 181 ASP   P CA  
27954 C  C   . ASP   P  182 ? 2.1477 1.3059 1.5380 0.0240  -0.4859 -0.1000 181 ASP   P C   
27955 O  O   . ASP   P  182 ? 2.2299 1.3633 1.4060 0.0390  -0.3499 -0.0666 181 ASP   P O   
27956 C  CB  . ASP   P  182 ? 2.2390 1.1607 1.6400 0.0490  -0.4480 -0.0931 181 ASP   P CB  
27957 C  CG  . ASP   P  182 ? 2.2211 1.1580 1.6125 0.0383  -0.4127 -0.0916 181 ASP   P CG  
27958 O  OD1 . ASP   P  182 ? 2.2134 1.0299 1.6995 0.0142  -0.4355 -0.0433 181 ASP   P OD1 
27959 O  OD2 . ASP   P  182 ? 2.2884 1.2356 1.5085 0.0079  -0.4493 -0.1400 181 ASP   P OD2 
27960 N  N   . ASP   P  183 ? 2.1472 1.3287 1.5351 0.0237  -0.4831 -0.1866 182 ASP   P N   
27961 C  CA  . ASP   P  183 ? 2.0914 1.3886 1.5212 0.0196  -0.4829 -0.2334 182 ASP   P CA  
27962 C  C   . ASP   P  183 ? 2.0404 1.3505 1.4231 0.0667  -0.5500 -0.2136 182 ASP   P C   
27963 O  O   . ASP   P  183 ? 2.0179 1.5058 1.3350 0.0994  -0.5400 -0.2855 182 ASP   P O   
27964 C  CB  . ASP   P  183 ? 2.1080 1.3902 1.5357 -0.0159 -0.4807 -0.2690 182 ASP   P CB  
27965 C  CG  . ASP   P  183 ? 2.0970 1.4185 1.5003 -0.0483 -0.4260 -0.3130 182 ASP   P CG  
27966 O  OD1 . ASP   P  183 ? 2.0617 1.2905 1.6919 -0.0762 -0.4220 -0.2518 182 ASP   P OD1 
27967 O  OD2 . ASP   P  183 ? 2.1275 1.4960 1.5252 -0.0726 -0.4764 -0.4007 182 ASP   P OD2 
27968 N  N   . MET   P  184 ? 2.0063 1.2302 1.5139 0.0352  -0.5473 -0.1913 183 MET   P N   
27969 C  CA  . MET   P  184 ? 1.9791 1.1563 1.6270 0.0017  -0.5349 -0.1007 183 MET   P CA  
27970 C  C   . MET   P  184 ? 1.9405 1.2218 1.5951 0.1206  -0.5291 -0.0510 183 MET   P C   
27971 O  O   . MET   P  184 ? 1.8988 1.2239 1.6168 0.1579  -0.5401 -0.0864 183 MET   P O   
27972 C  CB  . MET   P  184 ? 1.9967 1.0286 1.6749 -0.0359 -0.4889 -0.0599 183 MET   P CB  
27973 C  CG  . MET   P  184 ? 2.0221 0.9950 1.7672 -0.0699 -0.4800 -0.0780 183 MET   P CG  
27974 S  SD  . MET   P  184 ? 2.0891 0.8714 1.8906 -0.0809 -0.4229 -0.0005 183 MET   P SD  
27975 C  CE  . MET   P  184 ? 2.0675 1.0486 1.8846 -0.1420 -0.4208 -0.0049 183 MET   P CE  
27976 N  N   . LYS   P  185 ? 1.9400 1.1833 1.5912 0.0313  -0.5404 0.0067  184 LYS   P N   
27977 C  CA  . LYS   P  185 ? 1.9910 1.2129 1.6215 0.0189  -0.4966 -0.0194 184 LYS   P CA  
27978 C  C   . LYS   P  185 ? 1.9186 1.1508 1.6394 0.0172  -0.5055 -0.0006 184 LYS   P C   
27979 O  O   . LYS   P  185 ? 1.8992 1.1201 1.7220 -0.0280 -0.5316 -0.0189 184 LYS   P O   
27980 C  CB  . LYS   P  185 ? 1.9791 1.2674 1.6349 0.0127  -0.4650 -0.0285 184 LYS   P CB  
27981 C  CG  . LYS   P  185 ? 2.0958 1.3208 1.6062 0.0061  -0.4463 -0.0395 184 LYS   P CG  
27982 C  CD  . LYS   P  185 ? 2.1597 1.3088 1.5907 0.0288  -0.4206 -0.0129 184 LYS   P CD  
27983 C  CE  . LYS   P  185 ? 2.2159 1.2444 1.5358 -0.0001 -0.4167 0.0131  184 LYS   P CE  
27984 N  NZ  . LYS   P  185 ? 2.2617 1.2361 1.5283 -0.0233 -0.4080 0.0125  184 LYS   P NZ  
27985 N  N   . VAL   P  186 ? 1.9056 1.2180 1.7094 0.0301  -0.4730 -0.0554 185 VAL   P N   
27986 C  CA  . VAL   P  186 ? 1.8476 1.2310 1.7133 -0.0040 -0.4781 -0.0583 185 VAL   P CA  
27987 C  C   . VAL   P  186 ? 1.7644 1.2748 1.7398 -0.0340 -0.4816 -0.1123 185 VAL   P C   
27988 O  O   . VAL   P  186 ? 1.6180 1.2769 1.6700 -0.0635 -0.4691 -0.1377 185 VAL   P O   
27989 C  CB  . VAL   P  186 ? 1.8822 1.2779 1.7132 0.0354  -0.5039 -0.0825 185 VAL   P CB  
27990 C  CG1 . VAL   P  186 ? 1.8735 1.2601 1.7144 0.0460  -0.5041 -0.0607 185 VAL   P CG1 
27991 C  CG2 . VAL   P  186 ? 1.8754 1.3274 1.7165 0.0142  -0.5227 -0.0808 185 VAL   P CG2 
27992 N  N   . ASP   P  187 ? 1.7550 1.3151 1.7734 -0.1208 -0.4805 -0.1657 186 ASP   P N   
27993 C  CA  . ASP   P  187 ? 1.8151 1.3630 1.7794 -0.1737 -0.4442 -0.2033 186 ASP   P CA  
27994 C  C   . ASP   P  187 ? 1.7863 1.2976 1.7285 -0.2551 -0.4692 -0.1762 186 ASP   P C   
27995 O  O   . ASP   P  187 ? 1.7401 1.2781 1.7433 -0.3238 -0.4739 -0.2023 186 ASP   P O   
27996 C  CB  . ASP   P  187 ? 1.7808 1.5307 1.8532 -0.1729 -0.4131 -0.1915 186 ASP   P CB  
27997 C  CG  . ASP   P  187 ? 1.8300 1.5568 1.9155 -0.1685 -0.3460 -0.2057 186 ASP   P CG  
27998 O  OD1 . ASP   P  187 ? 1.8545 1.6377 1.9147 -0.2385 -0.3405 -0.2102 186 ASP   P OD1 
27999 O  OD2 . ASP   P  187 ? 1.8686 1.8086 2.0249 -0.2255 -0.2617 -0.1631 186 ASP   P OD2 
28000 N  N   . ASP   P  188 ? 1.8041 1.2428 1.7233 -0.2313 -0.4887 -0.2506 187 ASP   P N   
28001 C  CA  . ASP   P  188 ? 1.8383 1.1995 1.7193 -0.2693 -0.4958 -0.2600 187 ASP   P CA  
28002 C  C   . ASP   P  188 ? 1.8343 1.0576 1.7374 -0.2676 -0.4890 -0.2577 187 ASP   P C   
28003 O  O   . ASP   P  188 ? 1.8349 1.0543 1.8029 -0.3260 -0.4729 -0.2585 187 ASP   P O   
28004 C  CB  . ASP   P  188 ? 1.9191 1.2434 1.7293 -0.2569 -0.4483 -0.3400 187 ASP   P CB  
28005 C  CG  . ASP   P  188 ? 1.9092 1.3434 1.7293 -0.2473 -0.4431 -0.3677 187 ASP   P CG  
28006 O  OD1 . ASP   P  188 ? 1.8964 1.4955 1.7881 -0.2640 -0.4414 -0.3764 187 ASP   P OD1 
28007 O  OD2 . ASP   P  188 ? 2.0585 1.3135 1.6841 -0.2111 -0.3766 -0.4207 187 ASP   P OD2 
28008 N  N   . ALA   P  189 ? 1.8446 0.9748 1.7091 -0.2315 -0.5028 -0.2298 188 ALA   P N   
28009 C  CA  . ALA   P  189 ? 1.8456 0.8865 1.6497 -0.2082 -0.4850 -0.2531 188 ALA   P CA  
28010 C  C   . ALA   P  189 ? 1.8227 0.8474 1.6246 -0.1742 -0.5025 -0.2619 188 ALA   P C   
28011 O  O   . ALA   P  189 ? 1.7685 0.8234 1.5543 -0.1328 -0.4690 -0.3384 188 ALA   P O   
28012 C  CB  . ALA   P  189 ? 1.8059 0.9145 1.6338 -0.2092 -0.5115 -0.2726 188 ALA   P CB  
28013 N  N   . ILE   P  190 ? 1.8241 0.8987 1.6360 -0.1613 -0.4981 -0.2526 189 ILE   P N   
28014 C  CA  . ILE   P  190 ? 1.7993 0.9623 1.6559 -0.1459 -0.4992 -0.2242 189 ILE   P CA  
28015 C  C   . ILE   P  190 ? 1.8837 0.9776 1.6403 -0.1838 -0.5018 -0.2142 189 ILE   P C   
28016 O  O   . ILE   P  190 ? 1.9631 1.0331 1.5527 -0.2061 -0.4741 -0.2267 189 ILE   P O   
28017 C  CB  . ILE   P  190 ? 1.7525 1.0394 1.7350 -0.1300 -0.5163 -0.2085 189 ILE   P CB  
28018 C  CG1 . ILE   P  190 ? 1.7055 1.0536 1.7643 -0.1192 -0.5176 -0.2290 189 ILE   P CG1 
28019 C  CG2 . ILE   P  190 ? 1.7060 1.0141 1.7437 -0.1279 -0.5302 -0.2112 189 ILE   P CG2 
28020 C  CD1 . ILE   P  190 ? 1.6980 1.1358 1.8106 -0.0920 -0.5121 -0.2396 189 ILE   P CD1 
28021 N  N   . GLU   P  191 ? 1.9206 0.9653 1.6503 -0.1982 -0.5125 -0.2148 190 GLU   P N   
28022 C  CA  . GLU   P  191 ? 1.9349 0.9455 1.6972 -0.2004 -0.4949 -0.1650 190 GLU   P CA  
28023 C  C   . GLU   P  191 ? 1.9546 0.7885 1.5872 -0.2367 -0.5121 -0.1568 190 GLU   P C   
28024 O  O   . GLU   P  191 ? 1.9518 0.7251 1.6008 -0.2481 -0.4941 -0.1988 190 GLU   P O   
28025 C  CB  . GLU   P  191 ? 1.9848 1.0274 1.7448 -0.2478 -0.5320 -0.1613 190 GLU   P CB  
28026 C  CG  . GLU   P  191 ? 2.0693 1.0478 1.8848 -0.2923 -0.4916 -0.1369 190 GLU   P CG  
28027 C  CD  . GLU   P  191 ? 2.1316 1.1790 1.9252 -0.2687 -0.5312 -0.1067 190 GLU   P CD  
28028 O  OE1 . GLU   P  191 ? 2.1931 1.1678 2.0262 -0.2542 -0.4855 -0.0626 190 GLU   P OE1 
28029 O  OE2 . GLU   P  191 ? 2.2668 1.2378 1.9298 -0.2798 -0.4976 -0.1468 190 GLU   P OE2 
28030 N  N   . LEU   P  192 ? 1.9145 0.7043 1.5407 -0.1899 -0.5389 -0.1482 191 LEU   P N   
28031 C  CA  . LEU   P  192 ? 1.8986 0.6964 1.5447 -0.2088 -0.5069 -0.1425 191 LEU   P CA  
28032 C  C   . LEU   P  192 ? 1.8990 0.7660 1.5527 -0.1926 -0.5043 -0.1400 191 LEU   P C   
28033 O  O   . LEU   P  192 ? 1.9229 0.7890 1.6040 -0.1450 -0.4595 -0.1268 191 LEU   P O   
28034 C  CB  . LEU   P  192 ? 1.8809 0.6120 1.5036 -0.1944 -0.5349 -0.1462 191 LEU   P CB  
28035 C  CG  . LEU   P  192 ? 1.8779 0.6195 1.4963 -0.2013 -0.5222 -0.1392 191 LEU   P CG  
28036 C  CD1 . LEU   P  192 ? 1.8728 0.5601 1.4850 -0.1811 -0.5183 -0.1460 191 LEU   P CD1 
28037 C  CD2 . LEU   P  192 ? 1.8913 0.6394 1.4989 -0.1888 -0.5118 -0.1232 191 LEU   P CD2 
28038 N  N   . ALA   P  193 ? 1.8722 0.7799 1.5304 -0.1914 -0.5208 -0.1373 192 ALA   P N   
28039 C  CA  . ALA   P  193 ? 1.8625 0.8534 1.5530 -0.1476 -0.5495 -0.1303 192 ALA   P CA  
28040 C  C   . ALA   P  193 ? 1.8645 0.9390 1.5637 -0.1483 -0.5490 -0.0956 192 ALA   P C   
28041 O  O   . ALA   P  193 ? 1.8300 0.9818 1.6735 -0.1313 -0.5944 -0.0999 192 ALA   P O   
28042 C  CB  . ALA   P  193 ? 1.8398 0.8460 1.5417 -0.1283 -0.5349 -0.1171 192 ALA   P CB  
28043 N  N   . LEU   P  194 ? 1.8820 1.0920 1.6052 -0.0516 -0.5801 -0.1129 193 LEU   P N   
28044 C  CA  . LEU   P  194 ? 1.9233 1.1651 1.6529 -0.0480 -0.5604 -0.0598 193 LEU   P CA  
28045 C  C   . LEU   P  194 ? 1.9083 1.1370 1.6696 -0.0815 -0.5812 -0.0130 193 LEU   P C   
28046 O  O   . LEU   P  194 ? 1.9249 1.1909 1.6733 -0.0936 -0.5417 0.0172  193 LEU   P O   
28047 C  CB  . LEU   P  194 ? 1.9366 1.3340 1.7253 0.0002  -0.5783 -0.0615 193 LEU   P CB  
28048 C  CG  . LEU   P  194 ? 2.0042 1.4180 1.7916 0.1297  -0.5154 -0.0870 193 LEU   P CG  
28049 C  CD1 . LEU   P  194 ? 1.9542 1.6194 1.8677 0.1069  -0.5252 -0.1126 193 LEU   P CD1 
28050 C  CD2 . LEU   P  194 ? 2.0062 1.5239 1.8126 0.1975  -0.5031 0.0384  193 LEU   P CD2 
28051 N  N   . LYS   P  195 ? 1.9133 1.1163 1.6616 -0.0877 -0.5768 0.0230  194 LYS   P N   
28052 C  CA  . LYS   P  195 ? 1.9168 1.0770 1.7390 -0.1021 -0.5623 0.0469  194 LYS   P CA  
28053 C  C   . LYS   P  195 ? 1.9065 1.0199 1.7213 -0.0957 -0.5069 0.0243  194 LYS   P C   
28054 O  O   . LYS   P  195 ? 1.8984 1.0014 1.8081 -0.1256 -0.4893 -0.0109 194 LYS   P O   
28055 C  CB  . LYS   P  195 ? 1.9715 1.1083 1.7497 -0.1530 -0.5922 0.0508  194 LYS   P CB  
28056 C  CG  . LYS   P  195 ? 1.9655 1.1655 1.8365 -0.2182 -0.6164 0.0320  194 LYS   P CG  
28057 C  CD  . LYS   P  195 ? 1.9602 1.1661 1.8285 -0.2571 -0.6249 -0.0029 194 LYS   P CD  
28058 C  CE  . LYS   P  195 ? 1.9656 1.1427 1.8283 -0.3170 -0.6181 0.0028  194 LYS   P CE  
28059 N  NZ  . LYS   P  195 ? 1.9843 1.1686 1.8707 -0.3409 -0.6117 0.0156  194 LYS   P NZ  
28060 N  N   . THR   P  196 ? 1.8653 0.9528 1.6515 -0.0388 -0.4571 -0.0025 195 THR   P N   
28061 C  CA  . THR   P  196 ? 1.8617 0.8878 1.6057 -0.0447 -0.4409 -0.0354 195 THR   P CA  
28062 C  C   . THR   P  196 ? 1.8556 0.9390 1.5674 -0.0250 -0.4424 -0.0903 195 THR   P C   
28063 O  O   . THR   P  196 ? 1.8488 1.0566 1.5316 0.0594  -0.4827 0.0248  195 THR   P O   
28064 C  CB  . THR   P  196 ? 1.8403 0.8021 1.5652 -0.0320 -0.4666 -0.0936 195 THR   P CB  
28065 O  OG1 . THR   P  196 ? 1.8570 0.8021 1.5992 -0.0090 -0.4699 -0.0606 195 THR   P OG1 
28066 C  CG2 . THR   P  196 ? 1.8137 0.7385 1.5531 -0.0745 -0.4678 -0.1062 195 THR   P CG2 
28067 N  N   . LEU   P  197 ? 1.8068 0.8465 1.5968 -0.0538 -0.4692 -0.0865 196 LEU   P N   
28068 C  CA  . LEU   P  197 ? 1.8090 0.8460 1.5959 -0.0634 -0.4460 -0.0825 196 LEU   P CA  
28069 C  C   . LEU   P  197 ? 1.8564 0.8801 1.6479 -0.0925 -0.4054 -0.0790 196 LEU   P C   
28070 O  O   . LEU   P  197 ? 1.8812 0.9315 1.6358 -0.1204 -0.3721 -0.0261 196 LEU   P O   
28071 C  CB  . LEU   P  197 ? 1.7805 0.8771 1.5701 -0.0520 -0.4229 -0.0717 196 LEU   P CB  
28072 C  CG  . LEU   P  197 ? 1.7974 0.8049 1.5508 -0.0214 -0.4119 -0.0578 196 LEU   P CG  
28073 C  CD1 . LEU   P  197 ? 1.8068 0.7832 1.5577 -0.0244 -0.4147 -0.0506 196 LEU   P CD1 
28074 C  CD2 . LEU   P  197 ? 1.7996 0.7728 1.5403 -0.0172 -0.4049 -0.0478 196 LEU   P CD2 
28075 N  N   . SER   P  198 ? 1.8620 0.9657 1.6977 -0.0846 -0.4206 -0.0563 197 SER   P N   
28076 C  CA  . SER   P  198 ? 1.9175 1.0578 1.7535 -0.1524 -0.4078 -0.0549 197 SER   P CA  
28077 C  C   . SER   P  198 ? 1.9736 1.0265 1.7056 -0.1679 -0.4232 -0.0407 197 SER   P C   
28078 O  O   . SER   P  198 ? 2.0516 1.0363 1.6171 -0.1825 -0.4854 -0.0377 197 SER   P O   
28079 C  CB  . SER   P  198 ? 1.9028 1.1415 1.8309 -0.1464 -0.4195 -0.0785 197 SER   P CB  
28080 O  OG  . SER   P  198 ? 1.9111 1.2724 1.9555 -0.1818 -0.3587 -0.0701 197 SER   P OG  
28081 N  N   . LYS   P  199 ? 1.9919 1.0074 1.7325 -0.1479 -0.3978 -0.0339 198 LYS   P N   
28082 C  CA  . LYS   P  199 ? 2.0175 1.0169 1.7424 -0.1135 -0.3475 0.0064  198 LYS   P CA  
28083 C  C   . LYS   P  199 ? 1.9973 1.0447 1.7510 -0.1359 -0.3411 0.0175  198 LYS   P C   
28084 O  O   . LYS   P  199 ? 2.0464 1.0686 1.7265 -0.1269 -0.3043 0.1157  198 LYS   P O   
28085 C  CB  . LYS   P  199 ? 2.0540 0.9764 1.7297 -0.1121 -0.3488 -0.0169 198 LYS   P CB  
28086 C  CG  . LYS   P  199 ? 2.0898 0.9865 1.6687 -0.1697 -0.3575 -0.0885 198 LYS   P CG  
28087 C  CD  . LYS   P  199 ? 2.1377 0.9588 1.6633 -0.2109 -0.3451 -0.1773 198 LYS   P CD  
28088 C  CE  . LYS   P  199 ? 2.2096 0.9113 1.7234 -0.2280 -0.3623 -0.1987 198 LYS   P CE  
28089 N  NZ  . LYS   P  199 ? 2.2621 0.9277 1.7296 -0.2411 -0.3492 -0.2366 198 LYS   P NZ  
28090 N  N   . THR   P  200 ? 1.9828 0.8816 1.7478 -0.0787 -0.3248 0.0750  199 THR   P N   
28091 C  CA  . THR   P  200 ? 2.0023 0.8620 1.7777 -0.0486 -0.3327 0.1268  199 THR   P CA  
28092 C  C   . THR   P  200 ? 1.9539 0.8008 1.7762 -0.1012 -0.3585 0.1410  199 THR   P C   
28093 O  O   . THR   P  200 ? 1.8793 0.8304 1.8103 -0.2247 -0.3672 0.1338  199 THR   P O   
28094 C  CB  . THR   P  200 ? 2.0215 0.7884 1.7963 0.0204  -0.2977 0.1694  199 THR   P CB  
28095 O  OG1 . THR   P  200 ? 2.0470 0.8344 1.8006 0.0205  -0.2496 0.0963  199 THR   P OG1 
28096 C  CG2 . THR   P  200 ? 2.0747 0.7804 1.7942 0.0302  -0.3019 0.1505  199 THR   P CG2 
28097 N  N   . THR   P  201 ? 1.9754 0.7229 1.6949 -0.1100 -0.3760 0.0839  200 THR   P N   
28098 C  CA  . THR   P  201 ? 2.0430 0.7828 1.6567 -0.1622 -0.4645 -0.0210 200 THR   P CA  
28099 C  C   . THR   P  201 ? 2.1016 0.8831 1.6350 -0.1327 -0.4970 0.0587  200 THR   P C   
28100 O  O   . THR   P  201 ? 2.2278 1.0554 1.7062 -0.2039 -0.5366 -0.0247 200 THR   P O   
28101 C  CB  . THR   P  201 ? 2.0506 0.7364 1.5436 -0.1648 -0.4689 0.0038  200 THR   P CB  
28102 O  OG1 . THR   P  201 ? 2.0856 0.5917 1.5251 -0.2120 -0.5060 0.0416  200 THR   P OG1 
28103 C  CG2 . THR   P  201 ? 2.0465 0.7848 1.6426 -0.1973 -0.4679 0.0202  200 THR   P CG2 
28104 N  N   . ASP   P  202 ? 2.0992 0.8673 1.6506 -0.2244 -0.5330 -0.1658 201 ASP   P N   
28105 C  CA  . ASP   P  202 ? 2.1536 0.8682 1.6905 -0.2843 -0.5235 -0.1371 201 ASP   P CA  
28106 C  C   . ASP   P  202 ? 2.1846 0.8226 1.6999 -0.2455 -0.4775 -0.1354 201 ASP   P C   
28107 O  O   . ASP   P  202 ? 2.2507 1.0477 1.6216 -0.2791 -0.4551 -0.0233 201 ASP   P O   
28108 C  CB  . ASP   P  202 ? 2.2466 0.8559 1.6851 -0.3225 -0.5893 -0.1598 201 ASP   P CB  
28109 C  CG  . ASP   P  202 ? 2.2184 0.9276 1.7453 -0.3519 -0.6143 -0.1373 201 ASP   P CG  
28110 O  OD1 . ASP   P  202 ? 2.3223 0.9978 1.7602 -0.4326 -0.6395 -0.1557 201 ASP   P OD1 
28111 O  OD2 . ASP   P  202 ? 2.2427 1.0294 1.6295 -0.2833 -0.7132 -0.0830 201 ASP   P OD2 
28112 N  N   . SER   P  203 ? 2.1821 0.8153 1.7336 -0.2222 -0.3866 -0.2063 202 SER   P N   
28113 C  CA  . SER   P  203 ? 2.2023 0.9709 1.8043 -0.1571 -0.3368 -0.1200 202 SER   P CA  
28114 C  C   . SER   P  203 ? 2.1393 0.9767 1.8463 -0.1265 -0.3416 -0.1011 202 SER   P C   
28115 O  O   . SER   P  203 ? 2.0980 0.9074 1.8546 -0.0980 -0.2642 -0.0034 202 SER   P O   
28116 C  CB  . SER   P  203 ? 2.1728 1.0735 1.8512 -0.0817 -0.3046 -0.1618 202 SER   P CB  
28117 O  OG  . SER   P  203 ? 2.1439 1.3714 1.8746 -0.1267 -0.3631 -0.1502 202 SER   P OG  
28118 N  N   . SER   P  204 ? 2.1641 1.1936 1.8508 -0.0510 -0.2688 -0.0588 203 SER   P N   
28119 C  CA  . SER   P  204 ? 2.2075 1.3125 1.8333 -0.0697 -0.2929 -0.0905 203 SER   P CA  
28120 C  C   . SER   P  204 ? 2.2897 1.2927 1.8113 -0.0718 -0.3030 -0.0959 203 SER   P C   
28121 O  O   . SER   P  204 ? 2.3722 1.2932 1.8457 -0.0495 -0.3027 -0.1439 203 SER   P O   
28122 C  CB  . SER   P  204 ? 2.1962 1.4085 1.8357 -0.0613 -0.2871 -0.0603 203 SER   P CB  
28123 O  OG  . SER   P  204 ? 2.1423 1.5299 1.7922 -0.0199 -0.2410 -0.0563 203 SER   P OG  
28124 N  N   . ALA   P  205 ? 2.3267 1.2498 1.7939 -0.0920 -0.2852 -0.0449 204 ALA   P N   
28125 C  CA  . ALA   P  205 ? 2.3368 1.2643 1.7553 -0.1206 -0.2948 -0.0350 204 ALA   P CA  
28126 C  C   . ALA   P  205 ? 2.3975 1.2160 1.6852 -0.0702 -0.2853 0.0027  204 ALA   P C   
28127 O  O   . ALA   P  205 ? 2.4814 1.1834 1.6895 -0.0442 -0.2737 -0.0225 204 ALA   P O   
28128 C  CB  . ALA   P  205 ? 2.3349 1.3687 1.7636 -0.1328 -0.2977 -0.0007 204 ALA   P CB  
28129 N  N   . LEU   P  206 ? 2.4014 1.0802 1.7655 -0.0901 -0.2969 -0.0101 205 LEU   P N   
28130 C  CA  . LEU   P  206 ? 2.3509 1.0928 1.7332 -0.0944 -0.2992 -0.0608 205 LEU   P CA  
28131 C  C   . LEU   P  206 ? 2.3360 1.0724 1.6791 -0.1192 -0.2900 -0.0571 205 LEU   P C   
28132 O  O   . LEU   P  206 ? 2.3808 1.0259 1.6094 -0.0934 -0.2994 -0.0911 205 LEU   P O   
28133 C  CB  . LEU   P  206 ? 2.3183 1.0148 1.7554 -0.1210 -0.3172 -0.0574 205 LEU   P CB  
28134 C  CG  . LEU   P  206 ? 2.2908 0.9969 1.7677 -0.0957 -0.3424 -0.0794 205 LEU   P CG  
28135 C  CD1 . LEU   P  206 ? 2.3057 0.9350 1.7632 -0.0860 -0.3416 -0.0633 205 LEU   P CD1 
28136 C  CD2 . LEU   P  206 ? 2.2803 1.0613 1.7314 -0.1013 -0.3718 -0.0955 205 LEU   P CD2 
28137 N  N   . THR   P  207 ? 2.2609 1.1094 1.6359 -0.1343 -0.2698 -0.0300 206 THR   P N   
28138 C  CA  . THR   P  207 ? 2.1898 1.1891 1.6411 -0.1529 -0.2570 -0.0114 206 THR   P CA  
28139 C  C   . THR   P  207 ? 2.1241 1.2111 1.5876 -0.0989 -0.2668 -0.1130 206 THR   P C   
28140 O  O   . THR   P  207 ? 2.1198 1.1956 1.4256 -0.0786 -0.3143 -0.2571 206 THR   P O   
28141 C  CB  . THR   P  207 ? 2.1506 1.2365 1.6835 -0.1766 -0.2599 0.0296  206 THR   P CB  
28142 O  OG1 . THR   P  207 ? 2.1460 1.1127 1.6217 -0.1905 -0.2317 0.0455  206 THR   P OG1 
28143 C  CG2 . THR   P  207 ? 2.1416 1.3084 1.7307 -0.2391 -0.2637 0.0552  206 THR   P CG2 
28144 N  N   . TYR   P  208 ? 2.0823 1.2333 1.6180 -0.1049 -0.2689 -0.0963 207 TYR   P N   
28145 C  CA  . TYR   P  208 ? 2.0114 1.2154 1.6236 -0.0996 -0.2915 -0.0449 207 TYR   P CA  
28146 C  C   . TYR   P  208 ? 1.9673 1.0724 1.6703 -0.1108 -0.2877 -0.0905 207 TYR   P C   
28147 O  O   . TYR   P  208 ? 1.9716 0.9853 1.5485 -0.0751 -0.3378 -0.2000 207 TYR   P O   
28148 C  CB  . TYR   P  208 ? 1.9945 1.2473 1.6051 -0.1084 -0.2721 -0.0067 207 TYR   P CB  
28149 C  CG  . TYR   P  208 ? 2.0018 1.2957 1.5913 -0.1082 -0.2732 -0.0233 207 TYR   P CG  
28150 C  CD1 . TYR   P  208 ? 1.9807 1.4081 1.6065 -0.1409 -0.2309 0.0174  207 TYR   P CD1 
28151 C  CD2 . TYR   P  208 ? 1.9541 1.2590 1.5656 -0.1175 -0.2571 0.0002  207 TYR   P CD2 
28152 C  CE1 . TYR   P  208 ? 1.9863 1.4680 1.6128 -0.1419 -0.2164 -0.0103 207 TYR   P CE1 
28153 C  CE2 . TYR   P  208 ? 1.9535 1.3376 1.5802 -0.1148 -0.2379 -0.0236 207 TYR   P CE2 
28154 C  CZ  . TYR   P  208 ? 1.9624 1.4157 1.6723 -0.1575 -0.2287 -0.0167 207 TYR   P CZ  
28155 O  OH  . TYR   P  208 ? 1.9866 1.5108 1.7141 -0.1604 -0.1806 -0.0633 207 TYR   P OH  
28156 N  N   . ASP   P  209 ? 1.9622 1.0952 1.7215 -0.0997 -0.2663 -0.0544 208 ASP   P N   
28157 C  CA  . ASP   P  209 ? 1.9315 1.0783 1.7457 -0.0844 -0.2694 -0.0720 208 ASP   P CA  
28158 C  C   . ASP   P  209 ? 1.9341 0.9984 1.8183 -0.0833 -0.3047 -0.0583 208 ASP   P C   
28159 O  O   . ASP   P  209 ? 1.9331 0.7341 1.8602 -0.0205 -0.2947 -0.0829 208 ASP   P O   
28160 C  CB  . ASP   P  209 ? 1.9209 1.2390 1.7714 -0.0762 -0.2182 -0.0409 208 ASP   P CB  
28161 C  CG  . ASP   P  209 ? 1.9439 1.2302 1.8397 -0.0954 -0.1777 0.0223  208 ASP   P CG  
28162 O  OD1 . ASP   P  209 ? 1.9200 1.3389 1.8476 -0.1274 -0.2123 0.0699  208 ASP   P OD1 
28163 O  OD2 . ASP   P  209 ? 1.9404 1.3189 1.7891 -0.0766 -0.1495 0.0317  208 ASP   P OD2 
28164 N  N   . ARG   P  210 ? 1.9515 1.1056 1.8082 -0.0868 -0.2902 -0.0759 209 ARG   P N   
28165 C  CA  . ARG   P  210 ? 1.9432 1.1353 1.8531 -0.0960 -0.3175 -0.0525 209 ARG   P CA  
28166 C  C   . ARG   P  210 ? 1.9591 1.0331 1.7583 -0.0947 -0.4205 -0.0579 209 ARG   P C   
28167 O  O   . ARG   P  210 ? 1.9354 0.9801 1.6596 -0.1111 -0.4746 -0.0641 209 ARG   P O   
28168 C  CB  . ARG   P  210 ? 2.0088 1.1172 1.9780 -0.1330 -0.2604 -0.0283 209 ARG   P CB  
28169 C  CG  . ARG   P  210 ? 2.0245 1.0674 2.0272 -0.1188 -0.2317 0.0093  209 ARG   P CG  
28170 C  CD  . ARG   P  210 ? 2.0775 1.0328 2.0985 -0.1555 -0.1873 0.0014  209 ARG   P CD  
28171 N  NE  . ARG   P  210 ? 2.1216 1.0365 2.1590 -0.1502 -0.1939 -0.0410 209 ARG   P NE  
28172 C  CZ  . ARG   P  210 ? 2.1752 1.1514 2.2127 -0.1390 -0.1165 -0.0001 209 ARG   P CZ  
28173 N  NH1 . ARG   P  210 ? 2.2724 1.2397 2.2057 -0.1084 -0.1355 -0.0324 209 ARG   P NH1 
28174 N  NH2 . ARG   P  210 ? 2.1895 1.2082 2.2913 -0.1418 -0.1461 -0.0337 209 ARG   P NH2 
28175 N  N   . LEU   P  211 ? 1.9200 1.0036 1.7331 -0.1119 -0.4433 -0.0971 210 LEU   P N   
28176 C  CA  . LEU   P  211 ? 1.8759 1.0783 1.6796 -0.1029 -0.4789 -0.0814 210 LEU   P CA  
28177 C  C   . LEU   P  211 ? 1.8661 1.1026 1.6662 -0.1264 -0.4734 -0.0988 210 LEU   P C   
28178 O  O   . LEU   P  211 ? 1.7577 1.3019 1.7223 -0.1555 -0.4586 -0.0739 210 LEU   P O   
28179 C  CB  . LEU   P  211 ? 1.8805 1.0474 1.6910 -0.0535 -0.5047 -0.0261 210 LEU   P CB  
28180 C  CG  . LEU   P  211 ? 1.8929 1.0102 1.7033 -0.0808 -0.5515 -0.0085 210 LEU   P CG  
28181 C  CD1 . LEU   P  211 ? 1.8959 0.9752 1.7235 -0.0830 -0.5665 -0.0002 210 LEU   P CD1 
28182 C  CD2 . LEU   P  211 ? 1.9034 1.0073 1.7196 -0.0909 -0.5344 -0.0001 210 LEU   P CD2 
28183 N  N   . GLU   P  212 ? 1.8900 1.1713 1.6385 -0.0965 -0.4228 -0.0336 211 GLU   P N   
28184 C  CA  . GLU   P  212 ? 1.9137 1.1557 1.6034 -0.0121 -0.4140 0.0065  211 GLU   P CA  
28185 C  C   . GLU   P  212 ? 1.8428 1.1003 1.5817 0.0052  -0.4677 -0.0237 211 GLU   P C   
28186 O  O   . GLU   P  212 ? 1.8591 1.0591 1.4781 0.0110  -0.5096 0.0147  211 GLU   P O   
28187 C  CB  . GLU   P  212 ? 1.9212 1.0688 1.6780 -0.0558 -0.3747 -0.0027 211 GLU   P CB  
28188 C  CG  . GLU   P  212 ? 1.9982 1.1188 1.6859 -0.0233 -0.3039 0.0152  211 GLU   P CG  
28189 C  CD  . GLU   P  212 ? 1.9913 1.1370 1.6738 0.0020  -0.3058 0.0110  211 GLU   P CD  
28190 O  OE1 . GLU   P  212 ? 1.9929 1.1488 1.7150 0.0937  -0.2599 0.0311  211 GLU   P OE1 
28191 O  OE2 . GLU   P  212 ? 2.0530 1.1857 1.7097 -0.0246 -0.2438 0.1064  211 GLU   P OE2 
28192 N  N   . PHE   P  213 ? 1.8177 1.1422 1.6029 0.0632  -0.4655 -0.0696 212 PHE   P N   
28193 C  CA  . PHE   P  213 ? 1.8795 1.2329 1.5626 0.0472  -0.4616 -0.1342 212 PHE   P CA  
28194 C  C   . PHE   P  213 ? 1.9144 1.2366 1.5573 0.0475  -0.4828 -0.1096 212 PHE   P C   
28195 O  O   . PHE   P  213 ? 1.9530 1.1918 1.5024 -0.0213 -0.5383 -0.1374 212 PHE   P O   
28196 C  CB  . PHE   P  213 ? 1.8961 1.2712 1.5579 0.0426  -0.4617 -0.2025 212 PHE   P CB  
28197 C  CG  . PHE   P  213 ? 1.8931 1.3153 1.5993 0.0396  -0.4786 -0.2857 212 PHE   P CG  
28198 C  CD1 . PHE   P  213 ? 1.8638 1.2916 1.5787 0.0337  -0.4978 -0.2608 212 PHE   P CD1 
28199 C  CD2 . PHE   P  213 ? 1.9342 1.3315 1.6454 0.0683  -0.4927 -0.2870 212 PHE   P CD2 
28200 C  CE1 . PHE   P  213 ? 1.8869 1.2659 1.6353 0.0046  -0.4775 -0.3591 212 PHE   P CE1 
28201 C  CE2 . PHE   P  213 ? 1.9698 1.3453 1.6849 0.0672  -0.4457 -0.3504 212 PHE   P CE2 
28202 C  CZ  . PHE   P  213 ? 1.9519 1.3070 1.6628 0.0310  -0.4608 -0.3418 212 PHE   P CZ  
28203 N  N   . ALA   P  214 ? 1.9217 1.1854 1.5512 0.0461  -0.4865 -0.1187 213 ALA   P N   
28204 C  CA  . ALA   P  214 ? 1.8925 1.1557 1.5748 0.0389  -0.5100 -0.1881 213 ALA   P CA  
28205 C  C   . ALA   P  214 ? 1.9244 1.0934 1.5861 0.0754  -0.4764 -0.1852 213 ALA   P C   
28206 O  O   . ALA   P  214 ? 1.9232 1.1779 1.6375 0.1051  -0.4366 -0.1966 213 ALA   P O   
28207 C  CB  . ALA   P  214 ? 1.8982 1.1730 1.5341 0.0506  -0.5213 -0.1849 213 ALA   P CB  
28208 N  N   . THR   P  215 ? 1.9354 1.0520 1.6310 0.0763  -0.4627 -0.2053 214 THR   P N   
28209 C  CA  . THR   P  215 ? 1.9082 1.0048 1.6644 0.0699  -0.4628 -0.1687 214 THR   P CA  
28210 C  C   . THR   P  215 ? 1.8838 1.0166 1.6531 0.0546  -0.4548 -0.1472 214 THR   P C   
28211 O  O   . THR   P  215 ? 1.8716 0.9452 1.6865 0.0221  -0.4274 -0.1266 214 THR   P O   
28212 C  CB  . THR   P  215 ? 1.9320 1.0660 1.7010 0.1058  -0.4979 -0.1376 214 THR   P CB  
28213 O  OG1 . THR   P  215 ? 1.9576 1.0714 1.7253 0.1655  -0.5019 -0.0935 214 THR   P OG1 
28214 C  CG2 . THR   P  215 ? 1.9124 1.0915 1.7053 0.0985  -0.5225 -0.1629 214 THR   P CG2 
28215 N  N   . ILE   P  216 ? 1.8803 0.9491 1.6113 0.0755  -0.4583 -0.1833 215 ILE   P N   
28216 C  CA  . ILE   P  216 ? 1.9068 0.9270 1.6404 0.1012  -0.4356 -0.1816 215 ILE   P CA  
28217 C  C   . ILE   P  216 ? 1.9463 0.8987 1.6533 0.1041  -0.4115 -0.1401 215 ILE   P C   
28218 O  O   . ILE   P  216 ? 1.9676 0.7231 1.7342 0.0683  -0.3409 -0.1193 215 ILE   P O   
28219 C  CB  . ILE   P  216 ? 1.9044 0.9049 1.6301 0.0984  -0.4221 -0.1900 215 ILE   P CB  
28220 C  CG1 . ILE   P  216 ? 1.8903 0.9883 1.6453 0.0859  -0.4486 -0.1995 215 ILE   P CG1 
28221 C  CG2 . ILE   P  216 ? 1.9246 0.9089 1.5837 0.1218  -0.4139 -0.1607 215 ILE   P CG2 
28222 C  CD1 . ILE   P  216 ? 1.8826 1.0204 1.6666 0.0765  -0.4385 -0.2091 215 ILE   P CD1 
28223 N  N   . ARG   P  217 ? 1.9644 1.0291 1.7546 0.1504  -0.4223 -0.0840 216 ARG   P N   
28224 C  CA  . ARG   P  217 ? 1.9900 1.2346 1.8045 0.1483  -0.4663 -0.0272 216 ARG   P CA  
28225 C  C   . ARG   P  217 ? 2.0721 1.2636 1.9200 0.1761  -0.4625 0.0754  216 ARG   P C   
28226 O  O   . ARG   P  217 ? 2.0661 1.3295 1.8187 0.1142  -0.4990 0.1639  216 ARG   P O   
28227 C  CB  . ARG   P  217 ? 1.9942 1.2823 1.7979 0.1217  -0.5007 -0.0392 216 ARG   P CB  
28228 C  CG  . ARG   P  217 ? 1.9088 1.2831 1.7656 0.1328  -0.4963 -0.0718 216 ARG   P CG  
28229 C  CD  . ARG   P  217 ? 1.8890 1.3498 1.7274 0.1458  -0.5262 -0.1121 216 ARG   P CD  
28230 N  NE  . ARG   P  217 ? 1.7857 1.3967 1.6533 0.1589  -0.5460 -0.1707 216 ARG   P NE  
28231 C  CZ  . ARG   P  217 ? 1.7584 1.4307 1.6583 0.1344  -0.5393 -0.1825 216 ARG   P CZ  
28232 N  NH1 . ARG   P  217 ? 1.7852 1.4034 1.6548 0.1307  -0.5362 -0.1953 216 ARG   P NH1 
28233 N  NH2 . ARG   P  217 ? 1.7304 1.4834 1.7030 0.0826  -0.5221 -0.1801 216 ARG   P NH2 
28234 N  N   . LYS   P  218 ? 2.1523 1.4619 1.9495 0.2520  -0.4798 0.1124  217 LYS   P N   
28235 C  CA  . LYS   P  218 ? 2.1634 1.4942 2.0551 0.3393  -0.4335 0.1198  217 LYS   P CA  
28236 C  C   . LYS   P  218 ? 2.2058 1.5833 2.1920 0.5515  -0.4863 0.0851  217 LYS   P C   
28237 O  O   . LYS   P  218 ? 2.0911 1.6213 2.1171 0.5946  -0.5160 0.0273  217 LYS   P O   
28238 C  CB  . LYS   P  218 ? 2.2075 1.3690 2.0563 0.2758  -0.4594 0.1822  217 LYS   P CB  
28239 C  CG  . LYS   P  218 ? 2.1877 1.3743 1.9993 0.2356  -0.3852 0.1721  217 LYS   P CG  
28240 C  CD  . LYS   P  218 ? 2.1455 1.3678 2.0176 0.1964  -0.3850 0.1403  217 LYS   P CD  
28241 C  CE  . LYS   P  218 ? 2.1427 1.2897 1.9439 0.1945  -0.3901 0.1766  217 LYS   P CE  
28242 N  NZ  . LYS   P  218 ? 2.1103 1.2718 1.9379 0.1811  -0.4070 0.1668  217 LYS   P NZ  
28243 N  N   . GLY   P  219 ? 2.1444 1.6097 2.3769 0.5624  -0.3623 0.0373  218 GLY   P N   
28244 C  CA  . GLY   P  219 ? 2.1553 1.6996 2.5938 0.5044  -0.2997 0.0176  218 GLY   P CA  
28245 C  C   . GLY   P  219 ? 2.3749 1.7909 2.7716 0.4667  -0.1482 -0.0740 218 GLY   P C   
28246 O  O   . GLY   P  219 ? 2.4802 1.8658 2.9303 0.2351  -0.0961 -0.0466 218 GLY   P O   
28247 N  N   . ALA   P  220 ? 2.4981 1.7203 2.9629 0.4353  -0.1007 -0.0748 219 ALA   P N   
28248 C  CA  . ALA   P  220 ? 2.5842 1.5736 2.9196 0.3073  -0.1408 -0.0571 219 ALA   P CA  
28249 C  C   . ALA   P  220 ? 2.6745 1.7784 2.8903 0.2690  -0.1662 0.0451  219 ALA   P C   
28250 O  O   . ALA   P  220 ? 2.6124 0.9203 2.9379 0.2185  -0.1774 0.2320  219 ALA   P O   
28251 C  CB  . ALA   P  220 ? 2.5601 1.5566 2.8605 0.3438  -0.1209 -0.1348 219 ALA   P CB  
28252 N  N   . ASN   P  221 ? 2.6111 1.7788 2.6946 0.3430  -0.2884 0.1596  220 ASN   P N   
28253 C  CA  . ASN   P  221 ? 2.3773 2.1674 2.4889 0.2363  -0.3649 0.2350  220 ASN   P CA  
28254 C  C   . ASN   P  221 ? 2.4670 2.0025 2.2995 0.1696  -0.4788 0.2189  220 ASN   P C   
28255 O  O   . ASN   P  221 ? 2.3726 1.9644 2.2813 0.0879  -0.5378 0.3194  220 ASN   P O   
28256 C  CB  . ASN   P  221 ? 2.1887 2.3555 2.4258 0.3002  -0.4550 0.3033  220 ASN   P CB  
28257 C  CG  . ASN   P  221 ? 1.9091 2.5776 2.3796 0.3704  -0.5179 0.2904  220 ASN   P CG  
28258 O  OD1 . ASN   P  221 ? 1.7539 2.6072 2.3162 0.2491  -0.4551 0.3342  220 ASN   P OD1 
28259 N  ND2 . ASN   P  221 ? 1.9078 2.6330 2.3431 0.3622  -0.5410 0.3177  220 ASN   P ND2 
28260 N  N   . ASP   P  222 ? 2.4341 2.0317 2.2087 0.1029  -0.4800 0.2951  221 ASP   P N   
28261 C  CA  . ASP   P  222 ? 2.3824 2.0017 2.0887 0.0948  -0.5363 0.2402  221 ASP   P CA  
28262 C  C   . ASP   P  222 ? 2.4101 1.9100 2.1403 0.0550  -0.5955 0.1248  221 ASP   P C   
28263 O  O   . ASP   P  222 ? 2.4409 1.9683 2.2826 0.0516  -0.6707 0.0280  221 ASP   P O   
28264 C  CB  . ASP   P  222 ? 2.3966 2.0400 1.9627 0.1166  -0.4717 0.3096  221 ASP   P CB  
28265 C  CG  . ASP   P  222 ? 2.3876 2.1125 1.8528 0.1001  -0.3968 0.3802  221 ASP   P CG  
28266 O  OD1 . ASP   P  222 ? 2.2696 2.1712 1.7660 0.1154  -0.4022 0.4224  221 ASP   P OD1 
28267 O  OD2 . ASP   P  222 ? 2.3800 2.2298 1.6500 0.0794  -0.3745 0.3701  221 ASP   P OD2 
28268 N  N   . GLY   P  223 ? 2.3104 1.8771 2.1873 0.0079  -0.6205 0.0961  222 GLY   P N   
28269 C  CA  . GLY   P  223 ? 2.3079 1.8035 2.3063 -0.0267 -0.4704 0.0731  222 GLY   P CA  
28270 C  C   . GLY   P  223 ? 2.2792 1.7789 2.3189 -0.0288 -0.4504 0.0775  222 GLY   P C   
28271 O  O   . GLY   P  223 ? 2.1342 1.9601 2.5438 -0.0172 -0.2731 0.0968  222 GLY   P O   
28272 N  N   . GLU   P  224 ? 2.4544 1.6589 2.3621 0.0259  -0.4151 0.1199  223 GLU   P N   
28273 C  CA  . GLU   P  224 ? 2.5204 1.4724 2.3289 0.0927  -0.3669 0.1394  223 GLU   P CA  
28274 C  C   . GLU   P  224 ? 2.4673 1.3946 2.2621 0.1547  -0.4358 0.0591  223 GLU   P C   
28275 O  O   . GLU   P  224 ? 2.5868 1.2370 2.3533 0.1690  -0.5023 -0.0132 223 GLU   P O   
28276 C  CB  . GLU   P  224 ? 2.5836 1.4390 2.3272 0.1218  -0.3368 0.1800  223 GLU   P CB  
28277 C  CG  . GLU   P  224 ? 2.5853 1.4484 2.3640 0.1474  -0.3145 0.2261  223 GLU   P CG  
28278 C  CD  . GLU   P  224 ? 2.5873 1.4013 2.3861 0.1483  -0.3069 0.2874  223 GLU   P CD  
28279 O  OE1 . GLU   P  224 ? 2.6415 1.3188 2.3960 0.1795  -0.3237 0.2978  223 GLU   P OE1 
28280 O  OE2 . GLU   P  224 ? 2.5970 1.4938 2.4481 0.0735  -0.2289 0.3800  223 GLU   P OE2 
28281 N  N   . VAL   P  225 ? 2.4448 1.0523 2.1528 0.1835  -0.3296 0.0353  224 VAL   P N   
28282 C  CA  . VAL   P  225 ? 2.3012 0.9891 1.9690 0.1475  -0.2851 -0.0743 224 VAL   P CA  
28283 C  C   . VAL   P  225 ? 2.2672 0.8964 1.9615 0.0991  -0.2748 -0.1448 224 VAL   P C   
28284 O  O   . VAL   P  225 ? 2.3228 0.8106 1.9340 0.1253  -0.2198 -0.1128 224 VAL   P O   
28285 C  CB  . VAL   P  225 ? 2.3030 0.9450 1.9777 0.1545  -0.2831 -0.0534 224 VAL   P CB  
28286 C  CG1 . VAL   P  225 ? 2.3047 1.0545 1.9479 0.1796  -0.2725 0.0040  224 VAL   P CG1 
28287 C  CG2 . VAL   P  225 ? 2.2495 0.8803 1.9635 0.1431  -0.2842 0.0072  224 VAL   P CG2 
28288 N  N   . TYR   P  226 ? 2.1054 1.1137 1.8998 -0.0186 -0.2655 -0.2502 225 TYR   P N   
28289 C  CA  . TYR   P  226 ? 2.0048 1.2058 1.9512 -0.0996 -0.2596 -0.2757 225 TYR   P CA  
28290 C  C   . TYR   P  226 ? 1.8475 1.1605 1.9009 -0.1710 -0.3426 -0.3197 225 TYR   P C   
28291 O  O   . TYR   P  226 ? 1.7916 1.2012 1.9464 -0.1574 -0.3278 -0.3572 225 TYR   P O   
28292 C  CB  . TYR   P  226 ? 1.9928 1.4077 2.0129 -0.0959 -0.2019 -0.3044 225 TYR   P CB  
28293 C  CG  . TYR   P  226 ? 2.0282 1.6219 2.1149 -0.0459 -0.1031 -0.2643 225 TYR   P CG  
28294 C  CD1 . TYR   P  226 ? 2.0199 1.7108 2.0429 -0.0389 -0.0437 -0.2193 225 TYR   P CD1 
28295 C  CD2 . TYR   P  226 ? 1.9550 1.7404 2.0940 -0.0758 -0.0514 -0.2547 225 TYR   P CD2 
28296 C  CE1 . TYR   P  226 ? 2.0267 1.8639 2.0691 -0.0212 -0.0175 -0.1846 225 TYR   P CE1 
28297 C  CE2 . TYR   P  226 ? 1.9495 1.8716 2.1251 -0.0508 -0.0276 -0.2143 225 TYR   P CE2 
28298 C  CZ  . TYR   P  226 ? 1.9484 1.9531 2.0407 -0.0418 0.0350  -0.1695 225 TYR   P CZ  
28299 O  OH  . TYR   P  226 ? 1.8693 2.1883 2.1342 -0.0405 0.0898  -0.1640 225 TYR   P OH  
28300 N  N   . GLN   P  227 ? 1.7965 1.0102 1.9405 -0.1315 -0.4040 -0.2270 226 GLN   P N   
28301 C  CA  . GLN   P  227 ? 1.7874 1.0220 1.9117 -0.0836 -0.4269 -0.2326 226 GLN   P CA  
28302 C  C   . GLN   P  227 ? 1.8113 1.0329 1.9000 -0.0488 -0.4029 -0.1927 226 GLN   P C   
28303 O  O   . GLN   P  227 ? 1.8381 1.1619 1.9420 0.0144  -0.3173 -0.1660 226 GLN   P O   
28304 C  CB  . GLN   P  227 ? 1.7793 0.8908 1.9553 -0.0666 -0.4574 -0.1792 226 GLN   P CB  
28305 C  CG  . GLN   P  227 ? 1.7631 0.8130 1.8965 -0.0709 -0.4989 -0.2011 226 GLN   P CG  
28306 C  CD  . GLN   P  227 ? 1.8190 0.7512 1.8819 -0.0837 -0.5148 -0.2219 226 GLN   P CD  
28307 O  OE1 . GLN   P  227 ? 1.8213 0.8819 1.7281 -0.0541 -0.5519 -0.2229 226 GLN   P OE1 
28308 N  NE2 . GLN   P  227 ? 1.8136 0.7098 1.8704 -0.1031 -0.5500 -0.2330 226 GLN   P NE2 
28309 N  N   . LYS   P  228 ? 1.8613 0.9883 1.8265 0.0153  -0.3813 -0.2069 227 LYS   P N   
28310 C  CA  . LYS   P  228 ? 1.8979 0.9799 1.8492 0.0102  -0.3535 -0.2080 227 LYS   P CA  
28311 C  C   . LYS   P  228 ? 1.9312 1.0850 1.7744 0.0500  -0.3911 -0.1971 227 LYS   P C   
28312 O  O   . LYS   P  228 ? 1.9749 1.2802 1.8230 0.1554  -0.3127 -0.2641 227 LYS   P O   
28313 C  CB  . LYS   P  228 ? 1.8703 0.9615 1.8601 0.0319  -0.3628 -0.1559 227 LYS   P CB  
28314 C  CG  . LYS   P  228 ? 1.8786 1.0543 1.9126 0.0206  -0.3409 -0.1471 227 LYS   P CG  
28315 C  CD  . LYS   P  228 ? 1.8592 1.1648 1.9105 -0.0298 -0.3228 -0.1492 227 LYS   P CD  
28316 C  CE  . LYS   P  228 ? 1.8374 1.2796 1.9514 -0.0635 -0.3257 -0.1692 227 LYS   P CE  
28317 N  NZ  . LYS   P  228 ? 1.8105 1.3745 1.9725 -0.0864 -0.2946 -0.1590 227 LYS   P NZ  
28318 N  N   . ILE   P  229 ? 1.9031 1.1050 1.7745 0.0675  -0.4125 -0.2201 228 ILE   P N   
28319 C  CA  . ILE   P  229 ? 1.8594 1.1221 1.7967 0.1005  -0.3945 -0.2008 228 ILE   P CA  
28320 C  C   . ILE   P  229 ? 1.9072 1.0916 1.7744 0.0639  -0.3771 -0.1916 228 ILE   P C   
28321 O  O   . ILE   P  229 ? 1.9736 1.3303 1.8372 0.1288  -0.2510 -0.1425 228 ILE   P O   
28322 C  CB  . ILE   P  229 ? 1.8303 1.0902 1.8108 0.1175  -0.4045 -0.1908 228 ILE   P CB  
28323 C  CG1 . ILE   P  229 ? 1.8391 1.0223 1.8208 0.1328  -0.4156 -0.1844 228 ILE   P CG1 
28324 C  CG2 . ILE   P  229 ? 1.8318 1.0973 1.7857 0.1028  -0.3983 -0.1882 228 ILE   P CG2 
28325 C  CD1 . ILE   P  229 ? 1.8569 0.9217 1.8185 0.1168  -0.4234 -0.2040 228 ILE   P CD1 
28326 N  N   . PHE   P  230 ? 1.8318 1.0610 1.7342 0.0314  -0.3696 -0.1454 229 PHE   P N   
28327 C  CA  . PHE   P  230 ? 1.8555 1.0606 1.7466 -0.0044 -0.4000 -0.1677 229 PHE   P CA  
28328 C  C   . PHE   P  230 ? 1.8639 1.0444 1.7151 -0.0464 -0.4078 -0.2392 229 PHE   P C   
28329 O  O   . PHE   P  230 ? 1.8468 0.9342 1.6881 -0.0807 -0.4337 -0.3097 229 PHE   P O   
28330 C  CB  . PHE   P  230 ? 1.8512 1.0468 1.7075 -0.0006 -0.3974 -0.1358 229 PHE   P CB  
28331 C  CG  . PHE   P  230 ? 1.8226 1.0306 1.7296 -0.0070 -0.4028 -0.0625 229 PHE   P CG  
28332 C  CD1 . PHE   P  230 ? 1.8141 0.9045 1.7080 0.0225  -0.4424 -0.0441 229 PHE   P CD1 
28333 C  CD2 . PHE   P  230 ? 1.8495 1.0782 1.7107 -0.0109 -0.4357 -0.0435 229 PHE   P CD2 
28334 C  CE1 . PHE   P  230 ? 1.8147 0.9005 1.7141 0.0107  -0.4513 -0.0319 229 PHE   P CE1 
28335 C  CE2 . PHE   P  230 ? 1.8359 1.0430 1.7271 -0.0211 -0.4563 -0.0212 229 PHE   P CE2 
28336 C  CZ  . PHE   P  230 ? 1.8344 0.9843 1.7362 -0.0169 -0.4646 -0.0319 229 PHE   P CZ  
28337 N  N   . LYS   P  231 ? 1.8665 1.1723 1.7805 -0.0639 -0.3755 -0.2630 230 LYS   P N   
28338 C  CA  . LYS   P  231 ? 1.9010 1.3350 1.8460 -0.0689 -0.3013 -0.2493 230 LYS   P CA  
28339 C  C   . LYS   P  231 ? 1.9398 1.3507 1.9300 -0.1043 -0.2874 -0.1767 230 LYS   P C   
28340 O  O   . LYS   P  231 ? 1.9384 1.3296 1.8777 -0.0760 -0.2525 -0.1379 230 LYS   P O   
28341 C  CB  . LYS   P  231 ? 1.8943 1.4279 1.8525 -0.0686 -0.2444 -0.2950 230 LYS   P CB  
28342 C  CG  . LYS   P  231 ? 1.8711 1.4299 1.8568 -0.0672 -0.1995 -0.2753 230 LYS   P CG  
28343 C  CD  . LYS   P  231 ? 1.8335 1.5310 1.8728 -0.0631 -0.1775 -0.2609 230 LYS   P CD  
28344 C  CE  . LYS   P  231 ? 1.7927 1.5370 1.8528 -0.0790 -0.1630 -0.2705 230 LYS   P CE  
28345 N  NZ  . LYS   P  231 ? 1.7943 1.5000 1.8658 -0.1146 -0.1350 -0.2997 230 LYS   P NZ  
28346 N  N   . PRO   P  232 ? 1.9880 1.5612 1.9054 -0.0874 -0.2903 -0.1324 231 PRO   P N   
28347 C  CA  . PRO   P  232 ? 1.9658 1.6091 1.9573 -0.1422 -0.3022 -0.1247 231 PRO   P CA  
28348 C  C   . PRO   P  232 ? 1.9069 1.7292 2.0465 -0.1183 -0.3217 -0.1144 231 PRO   P C   
28349 O  O   . PRO   P  232 ? 1.8542 1.8360 2.0178 -0.1308 -0.3884 -0.1737 231 PRO   P O   
28350 C  CB  . PRO   P  232 ? 1.9985 1.6920 1.9584 -0.1395 -0.2775 -0.1306 231 PRO   P CB  
28351 C  CG  . PRO   P  232 ? 2.0085 1.6061 1.8974 -0.1093 -0.2543 -0.1313 231 PRO   P CG  
28352 C  CD  . PRO   P  232 ? 1.9769 1.5258 1.9153 -0.0883 -0.2742 -0.1649 231 PRO   P CD  
28353 N  N   . GLN   P  233 ? 1.8782 1.7595 2.0830 -0.1170 -0.3230 -0.0944 232 GLN   P N   
28354 C  CA  . GLN   P  233 ? 1.8573 1.7768 2.1187 -0.0547 -0.3231 -0.0900 232 GLN   P CA  
28355 C  C   . GLN   P  233 ? 1.9454 1.7434 2.1611 -0.0924 -0.2706 -0.0028 232 GLN   P C   
28356 O  O   . GLN   P  233 ? 1.9287 1.9061 2.1977 -0.1690 -0.2939 0.0251  232 GLN   P O   
28357 C  CB  . GLN   P  233 ? 1.8812 1.8293 2.1270 0.0124  -0.3636 -0.0996 232 GLN   P CB  
28358 C  CG  . GLN   P  233 ? 1.8752 1.9458 2.1590 0.1019  -0.3825 -0.1259 232 GLN   P CG  
28359 C  CD  . GLN   P  233 ? 1.7995 2.0125 2.1856 0.0756  -0.4214 -0.1187 232 GLN   P CD  
28360 O  OE1 . GLN   P  233 ? 1.8106 2.1917 2.2257 0.1243  -0.5146 -0.1679 232 GLN   P OE1 
28361 N  NE2 . GLN   P  233 ? 1.7753 2.1430 2.1427 0.1091  -0.4287 -0.1258 232 GLN   P NE2 
28362 N  N   . GLU   P  234 ? 2.0116 1.5556 2.1485 -0.0534 -0.3021 0.0216  233 GLU   P N   
28363 C  CA  . GLU   P  234 ? 2.0445 1.5144 2.1652 -0.0370 -0.3190 0.0921  233 GLU   P CA  
28364 C  C   . GLU   P  234 ? 2.1118 1.5660 2.0912 -0.0368 -0.2689 0.0708  233 GLU   P C   
28365 O  O   . GLU   P  234 ? 2.2341 1.6787 2.0476 -0.0293 -0.2124 0.0993  233 GLU   P O   
28366 C  CB  . GLU   P  234 ? 2.0182 1.5075 2.2199 -0.0253 -0.3777 0.1378  233 GLU   P CB  
28367 C  CG  . GLU   P  234 ? 1.9828 1.5219 2.3114 0.0131  -0.3648 0.1979  233 GLU   P CG  
28368 C  CD  . GLU   P  234 ? 2.0372 1.4927 2.3751 0.0352  -0.3879 0.3151  233 GLU   P CD  
28369 O  OE1 . GLU   P  234 ? 2.0562 1.4517 2.4296 0.0012  -0.4337 0.3904  233 GLU   P OE1 
28370 O  OE2 . GLU   P  234 ? 2.0126 1.5526 2.4376 0.0428  -0.3954 0.3962  233 GLU   P OE2 
28371 N  N   . ILE   P  235 ? 2.0659 1.4058 2.0908 0.0002  -0.2329 -0.0130 234 ILE   P N   
28372 C  CA  . ILE   P  235 ? 2.1199 1.2819 2.0555 -0.0931 -0.2415 -0.0546 234 ILE   P CA  
28373 C  C   . ILE   P  235 ? 2.1019 1.1627 2.0517 -0.0232 -0.2390 -0.0648 234 ILE   P C   
28374 O  O   . ILE   P  235 ? 2.1000 1.2613 1.9611 -0.0783 -0.2208 -0.0445 234 ILE   P O   
28375 C  CB  . ILE   P  235 ? 2.0900 1.2255 2.0647 -0.1157 -0.2352 -0.1064 234 ILE   P CB  
28376 C  CG1 . ILE   P  235 ? 2.1129 1.2522 2.1119 -0.1433 -0.2104 -0.1040 234 ILE   P CG1 
28377 C  CG2 . ILE   P  235 ? 2.1025 1.2019 2.0693 -0.1605 -0.2252 -0.1420 234 ILE   P CG2 
28378 C  CD1 . ILE   P  235 ? 2.1270 1.2622 2.0841 -0.1514 -0.1956 -0.1042 234 ILE   P CD1 
28379 N  N   . LYS   P  236 ? 2.0915 1.1138 2.0678 0.0568  -0.2283 -0.1185 235 LYS   P N   
28380 C  CA  . LYS   P  236 ? 2.0826 1.2680 2.1114 0.0030  -0.1975 -0.0971 235 LYS   P CA  
28381 C  C   . LYS   P  236 ? 2.1299 1.3842 2.1670 0.0350  -0.2402 -0.0368 235 LYS   P C   
28382 O  O   . LYS   P  236 ? 2.1454 1.4517 2.1951 -0.0218 -0.2940 -0.0403 235 LYS   P O   
28383 C  CB  . LYS   P  236 ? 2.1375 1.3184 2.1179 0.0306  -0.1704 -0.1035 235 LYS   P CB  
28384 C  CG  . LYS   P  236 ? 2.1601 1.4413 2.0851 -0.0145 -0.1063 -0.0514 235 LYS   P CG  
28385 C  CD  . LYS   P  236 ? 2.2149 1.5444 2.0323 -0.0067 -0.0778 -0.0285 235 LYS   P CD  
28386 C  CE  . LYS   P  236 ? 2.2136 1.6721 1.9966 -0.0540 -0.0344 0.0072  235 LYS   P CE  
28387 N  NZ  . LYS   P  236 ? 2.2562 1.6963 1.9552 -0.0709 0.0011  0.0275  235 LYS   P NZ  
28388 N  N   . ASP   P  237 ? 2.1416 1.3446 2.1390 0.0056  -0.2667 -0.0850 236 ASP   P N   
28389 C  CA  . ASP   P  237 ? 2.1235 1.4078 2.1571 -0.0064 -0.2820 -0.0811 236 ASP   P CA  
28390 C  C   . ASP   P  237 ? 2.0851 1.4310 2.0786 -0.0478 -0.3516 -0.1108 236 ASP   P C   
28391 O  O   . ASP   P  237 ? 2.0892 1.5042 2.0169 -0.0162 -0.3405 -0.1319 236 ASP   P O   
28392 C  CB  . ASP   P  237 ? 2.1365 1.4143 2.1930 0.0092  -0.2708 -0.0640 236 ASP   P CB  
28393 C  CG  . ASP   P  237 ? 2.1363 1.4635 2.2455 0.0009  -0.2297 -0.0241 236 ASP   P CG  
28394 O  OD1 . ASP   P  237 ? 2.1507 1.4255 2.2278 -0.0090 -0.2363 -0.0649 236 ASP   P OD1 
28395 O  OD2 . ASP   P  237 ? 2.1989 1.4455 2.3395 0.0144  -0.1981 -0.0017 236 ASP   P OD2 
28396 N  N   . ILE   P  238 ? 2.0877 1.4387 2.1096 -0.0615 -0.4070 -0.0903 237 ILE   P N   
28397 C  CA  . ILE   P  238 ? 2.0920 1.4369 2.0501 -0.0408 -0.4685 -0.1100 237 ILE   P CA  
28398 C  C   . ILE   P  238 ? 1.9959 1.4268 2.0020 -0.0829 -0.5847 -0.1515 237 ILE   P C   
28399 O  O   . ILE   P  238 ? 1.9521 1.4046 1.9892 -0.0796 -0.6795 -0.1947 237 ILE   P O   
28400 C  CB  . ILE   P  238 ? 2.0926 1.4398 2.0668 -0.0340 -0.4565 -0.0702 237 ILE   P CB  
28401 C  CG1 . ILE   P  238 ? 2.1418 1.4964 2.0621 -0.0561 -0.4416 -0.0660 237 ILE   P CG1 
28402 C  CG2 . ILE   P  238 ? 2.1060 1.3705 2.1182 0.0194  -0.4351 -0.0727 237 ILE   P CG2 
28403 C  CD1 . ILE   P  238 ? 2.1316 1.5224 2.0322 -0.0718 -0.4162 -0.0315 237 ILE   P CD1 
28404 N  N   . LEU   P  239 ? 1.9451 1.4075 1.9729 -0.0791 -0.6280 -0.1717 238 LEU   P N   
28405 C  CA  . LEU   P  239 ? 1.9448 1.3911 1.9774 -0.1263 -0.6594 -0.1813 238 LEU   P CA  
28406 C  C   . LEU   P  239 ? 1.9396 1.4485 1.9493 -0.1243 -0.6788 -0.1797 238 LEU   P C   
28407 O  O   . LEU   P  239 ? 1.8603 1.4571 1.9477 -0.2345 -0.7808 -0.2306 238 LEU   P O   
28408 C  CB  . LEU   P  239 ? 1.9673 1.3679 1.9909 -0.1216 -0.6424 -0.1593 238 LEU   P CB  
28409 C  CG  . LEU   P  239 ? 1.9585 1.3743 2.0361 -0.1327 -0.6815 -0.1360 238 LEU   P CG  
28410 C  CD1 . LEU   P  239 ? 1.9254 1.2553 2.0421 -0.1498 -0.7283 -0.1440 238 LEU   P CD1 
28411 C  CD2 . LEU   P  239 ? 1.9433 1.4228 2.0269 -0.1290 -0.6851 -0.1506 238 LEU   P CD2 
28412 N  N   . VAL   P  240 ? 1.9715 1.5046 1.9081 -0.1016 -0.6346 -0.1940 239 VAL   P N   
28413 C  CA  . VAL   P  240 ? 1.9577 1.5805 1.8982 -0.1187 -0.5980 -0.2162 239 VAL   P CA  
28414 C  C   . VAL   P  240 ? 2.0491 1.6377 1.9193 -0.1371 -0.6517 -0.1776 239 VAL   P C   
28415 O  O   . VAL   P  240 ? 1.9489 1.8182 1.8506 -0.1670 -0.7750 -0.1433 239 VAL   P O   
28416 C  CB  . VAL   P  240 ? 1.9476 1.6061 1.8770 -0.1124 -0.6013 -0.2360 239 VAL   P CB  
28417 C  CG1 . VAL   P  240 ? 1.9280 1.6300 1.8842 -0.0914 -0.5938 -0.2535 239 VAL   P CG1 
28418 C  CG2 . VAL   P  240 ? 1.9314 1.6176 1.8540 -0.1022 -0.5558 -0.2584 239 VAL   P CG2 
28419 N  N   . LYS   P  241 ? 2.1540 1.6704 1.9338 -0.0803 -0.5965 -0.0535 240 LYS   P N   
28420 C  CA  . LYS   P  241 ? 2.2224 1.7853 1.9508 -0.0313 -0.5898 -0.0116 240 LYS   P CA  
28421 C  C   . LYS   P  241 ? 2.3159 1.7063 1.9159 -0.0784 -0.6033 -0.0356 240 LYS   P C   
28422 O  O   . LYS   P  241 ? 2.2618 1.6921 2.0015 -0.1084 -0.6820 -0.0319 240 LYS   P O   
28423 C  CB  . LYS   P  241 ? 2.2456 1.7668 2.0314 0.0166  -0.5241 0.0645  240 LYS   P CB  
28424 C  CG  . LYS   P  241 ? 2.2415 1.8704 2.0846 0.0429  -0.4978 0.1416  240 LYS   P CG  
28425 C  CD  . LYS   P  241 ? 2.2377 1.8560 2.1146 0.0518  -0.4522 0.2228  240 LYS   P CD  
28426 C  CE  . LYS   P  241 ? 2.2464 1.8377 2.1201 0.0459  -0.4447 0.2896  240 LYS   P CE  
28427 N  NZ  . LYS   P  241 ? 2.2402 1.8063 2.1591 0.0276  -0.3990 0.3422  240 LYS   P NZ  
28428 N  N   . THR   P  242 ? 2.3504 1.6904 1.8279 -0.0549 -0.5893 -0.0361 241 THR   P N   
28429 C  CA  . THR   P  242 ? 2.3994 1.7222 1.7895 -0.0753 -0.5650 -0.0511 241 THR   P CA  
28430 C  C   . THR   P  242 ? 2.4406 1.7373 1.7715 -0.0860 -0.5041 -0.0296 241 THR   P C   
28431 O  O   . THR   P  242 ? 2.5934 1.7403 1.8638 -0.0347 -0.4201 -0.0146 241 THR   P O   
28432 C  CB  . THR   P  242 ? 2.4006 1.7561 1.7192 -0.0631 -0.5884 -0.0765 241 THR   P CB  
28433 O  OG1 . THR   P  242 ? 2.3716 1.7983 1.7359 -0.0873 -0.6048 -0.0398 241 THR   P OG1 
28434 C  CG2 . THR   P  242 ? 2.3636 1.7469 1.7122 -0.0363 -0.5909 -0.0764 241 THR   P CG2 
28435 N  N   . GLY   P  243 ? 2.3969 1.7743 1.7500 -0.1423 -0.5504 -0.0194 242 GLY   P N   
28436 C  CA  . GLY   P  243 ? 2.3577 1.8435 1.7516 -0.2375 -0.5702 -0.0435 242 GLY   P CA  
28437 C  C   . GLY   P  243 ? 2.3906 1.7302 1.7836 -0.2854 -0.5386 -0.0171 242 GLY   P C   
28438 O  O   . GLY   P  243 ? 2.2989 1.7759 1.5823 -0.4372 -0.6009 -0.0144 242 GLY   P O   
28439 N  N   . ILE   P  244 ? 2.3988 1.7431 1.9192 -0.3370 -0.5344 -0.0868 243 ILE   P N   
28440 C  CA  . ILE   P  244 ? 2.2939 1.6253 2.0179 -0.3947 -0.5446 -0.1278 243 ILE   P CA  
28441 C  C   . ILE   P  244 ? 2.4345 1.6687 2.0411 -0.3818 -0.4524 -0.1502 243 ILE   P C   
28442 O  O   . ILE   P  244 ? 2.4478 1.6635 2.0588 -0.4450 -0.4656 -0.1061 243 ILE   P O   
28443 C  CB  . ILE   P  244 ? 2.3074 1.4900 1.9880 -0.3628 -0.5785 -0.1871 243 ILE   P CB  
28444 C  CG1 . ILE   P  244 ? 2.1674 1.3795 2.0272 -0.4335 -0.6089 -0.2238 243 ILE   P CG1 
28445 C  CG2 . ILE   P  244 ? 2.2347 1.4280 1.9317 -0.4299 -0.6044 -0.2413 243 ILE   P CG2 
28446 C  CD1 . ILE   P  244 ? 2.1449 1.3366 1.9898 -0.4054 -0.5930 -0.2238 243 ILE   P CD1 
28447 N  N   . THR   P  245 ? 2.5143 1.6433 2.0162 -0.4154 -0.4089 -0.2359 244 THR   P N   
28448 C  CA  . THR   P  245 ? 2.4454 1.5362 1.9444 -0.4609 -0.4473 -0.3506 244 THR   P CA  
28449 C  C   . THR   P  245 ? 2.3965 1.5707 2.0649 -0.4893 -0.4289 -0.3082 244 THR   P C   
28450 O  O   . THR   P  245 ? 2.1332 1.5681 2.2195 -0.4389 -0.4970 -0.3288 244 THR   P O   
28451 C  CB  . THR   P  245 ? 2.5052 1.3977 1.9485 -0.4865 -0.3595 -0.3880 244 THR   P CB  
28452 O  OG1 . THR   P  245 ? 2.4904 1.3441 1.7901 -0.5119 -0.4233 -0.5866 244 THR   P OG1 
28453 C  CG2 . THR   P  245 ? 2.4915 1.3446 1.8664 -0.5038 -0.3496 -0.4310 244 THR   P CG2 
28454 N  N   . GLY   Q  3   ? 2.0139 0.9278 1.7285 0.3346  -0.0578 -0.0546 1   GLY   Q N   
28455 C  CA  . GLY   Q  3   ? 1.9960 0.9409 1.7089 0.2429  -0.1114 -0.0350 1   GLY   Q CA  
28456 C  C   . GLY   Q  3   ? 1.9707 0.8797 1.6495 0.1283  -0.1469 -0.0611 1   GLY   Q C   
28457 O  O   . GLY   Q  3   ? 1.9352 0.8787 1.7230 0.1060  -0.1482 -0.0187 1   GLY   Q O   
28458 N  N   . TYR   Q  4   ? 1.9281 0.8612 1.6392 0.0879  -0.1350 -0.0254 2   TYR   Q N   
28459 C  CA  . TYR   Q  4   ? 1.8438 0.8341 1.6690 0.1110  -0.1187 0.0455  2   TYR   Q CA  
28460 C  C   . TYR   Q  4   ? 1.8701 0.7342 1.7035 0.0408  -0.0824 0.0650  2   TYR   Q C   
28461 O  O   . TYR   Q  4   ? 1.7446 0.7113 1.8382 0.0115  -0.0376 0.1226  2   TYR   Q O   
28462 C  CB  . TYR   Q  4   ? 1.8225 0.8640 1.7034 0.1143  -0.1275 0.0366  2   TYR   Q CB  
28463 C  CG  . TYR   Q  4   ? 1.8212 0.8623 1.7335 0.0996  -0.1445 0.0546  2   TYR   Q CG  
28464 C  CD1 . TYR   Q  4   ? 1.8073 0.8941 1.6986 0.0878  -0.1495 0.0547  2   TYR   Q CD1 
28465 C  CD2 . TYR   Q  4   ? 1.8338 0.8820 1.7651 0.1168  -0.1369 0.0273  2   TYR   Q CD2 
28466 C  CE1 . TYR   Q  4   ? 1.7878 0.8810 1.6921 0.1436  -0.1915 0.1075  2   TYR   Q CE1 
28467 C  CE2 . TYR   Q  4   ? 1.8004 0.8625 1.7556 0.1198  -0.1447 0.0581  2   TYR   Q CE2 
28468 C  CZ  . TYR   Q  4   ? 1.7636 0.8743 1.7297 0.1724  -0.1873 0.0763  2   TYR   Q CZ  
28469 O  OH  . TYR   Q  4   ? 1.7067 0.8494 1.7160 0.2292  -0.2563 0.1937  2   TYR   Q OH  
28470 N  N   . ASP   Q  5   ? 1.8437 0.8511 1.7160 0.0306  -0.1349 0.0472  3   ASP   Q N   
28471 C  CA  . ASP   Q  5   ? 1.8624 0.8588 1.7444 -0.0590 -0.1307 -0.0302 3   ASP   Q CA  
28472 C  C   . ASP   Q  5   ? 1.8184 0.9139 1.7220 -0.0305 -0.1637 -0.0619 3   ASP   Q C   
28473 O  O   . ASP   Q  5   ? 1.7679 0.6699 1.5861 -0.0837 -0.2444 -0.1289 3   ASP   Q O   
28474 C  CB  . ASP   Q  5   ? 1.9352 0.9548 1.7096 -0.0501 -0.1068 -0.0239 3   ASP   Q CB  
28475 C  CG  . ASP   Q  5   ? 1.9215 1.0085 1.7878 -0.0321 -0.0501 0.0202  3   ASP   Q CG  
28476 O  OD1 . ASP   Q  5   ? 2.0700 1.0989 1.7035 0.0223  -0.0400 0.0970  3   ASP   Q OD1 
28477 O  OD2 . ASP   Q  5   ? 2.0261 1.0762 1.8039 0.1275  -0.0237 0.0831  3   ASP   Q OD2 
28478 N  N   . ARG   Q  6   ? 1.8896 0.8306 1.7301 0.0273  -0.1911 -0.0793 4   ARG   Q N   
28479 C  CA  . ARG   Q  6   ? 1.9103 0.8271 1.6963 -0.0113 -0.2098 -0.1240 4   ARG   Q CA  
28480 C  C   . ARG   Q  6   ? 1.8912 0.7720 1.6899 -0.0492 -0.2153 -0.1867 4   ARG   Q C   
28481 O  O   . ARG   Q  6   ? 1.9083 0.7108 1.7161 -0.0772 -0.2405 -0.2041 4   ARG   Q O   
28482 C  CB  . ARG   Q  6   ? 1.9096 0.8515 1.7558 -0.0264 -0.1915 -0.1030 4   ARG   Q CB  
28483 C  CG  . ARG   Q  6   ? 1.9186 0.8232 1.8077 0.0222  -0.1783 -0.0925 4   ARG   Q CG  
28484 C  CD  . ARG   Q  6   ? 1.9436 0.8594 1.8533 0.0807  -0.1703 -0.0337 4   ARG   Q CD  
28485 N  NE  . ARG   Q  6   ? 2.0133 0.9876 1.8830 0.0527  -0.1150 0.0802  4   ARG   Q NE  
28486 C  CZ  . ARG   Q  6   ? 2.0974 0.9945 1.8886 0.0528  -0.0687 0.0430  4   ARG   Q CZ  
28487 N  NH1 . ARG   Q  6   ? 2.1474 1.0198 1.8984 0.0725  -0.0320 0.0120  4   ARG   Q NH1 
28488 N  NH2 . ARG   Q  6   ? 2.1188 0.9342 1.8723 0.0423  -0.0901 -0.0103 4   ARG   Q NH2 
28489 N  N   . ALA   Q  7   ? 1.8818 0.7260 1.6133 -0.0680 -0.2652 -0.1979 5   ALA   Q N   
28490 C  CA  . ALA   Q  7   ? 1.8902 0.7555 1.6390 -0.0537 -0.2449 -0.1682 5   ALA   Q CA  
28491 C  C   . ALA   Q  7   ? 1.9096 0.7389 1.6327 -0.0497 -0.2838 -0.1312 5   ALA   Q C   
28492 O  O   . ALA   Q  7   ? 1.9788 0.7256 1.7202 -0.1060 -0.2581 -0.0432 5   ALA   Q O   
28493 C  CB  . ALA   Q  7   ? 1.8982 0.7379 1.5873 -0.0640 -0.2666 -0.1863 5   ALA   Q CB  
28494 N  N   . LEU   Q  8   ? 1.8838 0.7904 1.5953 -0.0440 -0.2584 -0.1340 6   LEU   Q N   
28495 C  CA  . LEU   Q  8   ? 1.8392 0.6685 1.5283 -0.0255 -0.2346 -0.0594 6   LEU   Q CA  
28496 C  C   . LEU   Q  8   ? 1.8349 0.6253 1.4820 -0.0609 -0.2345 -0.0397 6   LEU   Q C   
28497 O  O   . LEU   Q  8   ? 1.8305 0.5782 1.4649 -0.0413 -0.1633 0.0670  6   LEU   Q O   
28498 C  CB  . LEU   Q  8   ? 1.8531 0.6716 1.5379 -0.0083 -0.2548 -0.0823 6   LEU   Q CB  
28499 C  CG  . LEU   Q  8   ? 1.8457 0.6662 1.5455 0.0071  -0.2584 -0.0770 6   LEU   Q CG  
28500 C  CD1 . LEU   Q  8   ? 1.8470 0.7426 1.5610 0.0145  -0.2700 -0.0931 6   LEU   Q CD1 
28501 C  CD2 . LEU   Q  8   ? 1.8355 0.5956 1.5823 0.0243  -0.2682 -0.0875 6   LEU   Q CD2 
28502 N  N   . SER   Q  9   ? 1.7848 0.6640 1.4186 -0.0719 -0.2247 -0.0797 7   SER   Q N   
28503 C  CA  . SER   Q  9   ? 1.7656 0.6004 1.4131 -0.0938 -0.2353 -0.0909 7   SER   Q CA  
28504 C  C   . SER   Q  9   ? 1.7622 0.6292 1.3988 -0.0934 -0.2347 -0.1324 7   SER   Q C   
28505 O  O   . SER   Q  9   ? 1.7121 0.6186 1.3609 -0.1372 -0.2294 -0.0446 7   SER   Q O   
28506 C  CB  . SER   Q  9   ? 1.7403 0.6201 1.4276 -0.1385 -0.2331 -0.0729 7   SER   Q CB  
28507 O  OG  . SER   Q  9   ? 1.7323 0.6404 1.4365 -0.1988 -0.2490 -0.0429 7   SER   Q OG  
28508 N  N   . ILE   Q  10  ? 1.7870 0.6529 1.4427 -0.0597 -0.2355 -0.1723 8   ILE   Q N   
28509 C  CA  . ILE   Q  10  ? 1.7744 0.6748 1.4465 -0.0366 -0.2125 -0.1890 8   ILE   Q CA  
28510 C  C   . ILE   Q  10  ? 1.7924 0.6750 1.5335 0.0111  -0.1756 -0.1616 8   ILE   Q C   
28511 O  O   . ILE   Q  10  ? 1.7741 0.6746 1.6085 -0.0101 -0.2006 -0.1509 8   ILE   Q O   
28512 C  CB  . ILE   Q  10  ? 1.7807 0.6382 1.4575 -0.0257 -0.2087 -0.1760 8   ILE   Q CB  
28513 C  CG1 . ILE   Q  10  ? 1.7539 0.5754 1.4542 0.0248  -0.2266 -0.2070 8   ILE   Q CG1 
28514 C  CG2 . ILE   Q  10  ? 1.7658 0.6399 1.4650 -0.0318 -0.1721 -0.1615 8   ILE   Q CG2 
28515 C  CD1 . ILE   Q  10  ? 1.7302 0.5607 1.4636 0.0701  -0.2261 -0.2153 8   ILE   Q CD1 
28516 N  N   . PHE   Q  11  ? 1.7978 0.6589 1.5225 0.0314  -0.1820 -0.1493 9   PHE   Q N   
28517 C  CA  . PHE   Q  11  ? 1.7790 0.7808 1.5312 0.0749  -0.1762 -0.1549 9   PHE   Q CA  
28518 C  C   . PHE   Q  11  ? 1.8530 0.8716 1.5094 -0.0020 -0.1649 -0.0957 9   PHE   Q C   
28519 O  O   . PHE   Q  11  ? 1.7972 1.1375 1.4916 -0.0634 -0.1897 -0.0963 9   PHE   Q O   
28520 C  CB  . PHE   Q  11  ? 1.7677 0.7425 1.4833 0.0997  -0.1803 -0.1747 9   PHE   Q CB  
28521 C  CG  . PHE   Q  11  ? 1.7206 0.7246 1.4371 0.1155  -0.1605 -0.2139 9   PHE   Q CG  
28522 C  CD1 . PHE   Q  11  ? 1.7338 0.7648 1.4372 0.1313  -0.1672 -0.2454 9   PHE   Q CD1 
28523 C  CD2 . PHE   Q  11  ? 1.7207 0.7776 1.4067 0.1085  -0.1563 -0.2535 9   PHE   Q CD2 
28524 C  CE1 . PHE   Q  11  ? 1.7401 0.7624 1.4084 0.1207  -0.1568 -0.2624 9   PHE   Q CE1 
28525 C  CE2 . PHE   Q  11  ? 1.7394 0.8389 1.4004 0.0774  -0.1302 -0.2343 9   PHE   Q CE2 
28526 C  CZ  . PHE   Q  11  ? 1.7514 0.7903 1.4000 0.0847  -0.1393 -0.2757 9   PHE   Q CZ  
28527 N  N   . SER   Q  12  ? 1.9526 0.8199 1.6584 -0.0062 -0.1622 -0.1286 10  SER   Q N   
28528 C  CA  . SER   Q  12  ? 1.9924 0.8209 1.7253 0.0690  -0.1851 -0.1085 10  SER   Q CA  
28529 C  C   . SER   Q  12  ? 2.0063 0.7383 1.7123 0.0781  -0.1779 -0.1266 10  SER   Q C   
28530 O  O   . SER   Q  12  ? 1.9896 0.5494 1.6965 0.1453  -0.2497 -0.0389 10  SER   Q O   
28531 C  CB  . SER   Q  12  ? 2.0956 0.8472 1.7755 0.0460  -0.2177 -0.1431 10  SER   Q CB  
28532 O  OG  . SER   Q  12  ? 2.0864 0.9737 1.8428 -0.0058 -0.2250 -0.1421 10  SER   Q OG  
28533 N  N   . PRO   Q  13  ? 2.0956 0.6628 1.7309 0.1186  -0.1881 -0.2134 11  PRO   Q N   
28534 C  CA  . PRO   Q  13  ? 2.1149 0.6177 1.7549 0.1285  -0.1740 -0.2667 11  PRO   Q CA  
28535 C  C   . PRO   Q  13  ? 2.0994 0.6094 1.7816 0.1199  -0.1525 -0.3017 11  PRO   Q C   
28536 O  O   . PRO   Q  13  ? 2.0980 0.3781 1.6855 0.1161  -0.1463 -0.4349 11  PRO   Q O   
28537 C  CB  . PRO   Q  13  ? 2.1543 0.6485 1.7772 0.1331  -0.1838 -0.2142 11  PRO   Q CB  
28538 C  CG  . PRO   Q  13  ? 2.1454 0.6005 1.7599 0.1237  -0.1908 -0.2089 11  PRO   Q CG  
28539 C  CD  . PRO   Q  13  ? 2.1126 0.5764 1.7491 0.1116  -0.1913 -0.2336 11  PRO   Q CD  
28540 N  N   . ASP   Q  14  ? 2.1449 0.7186 1.7826 0.1142  -0.1726 -0.2652 12  ASP   Q N   
28541 C  CA  . ASP   Q  14  ? 2.1595 0.7722 1.8101 0.1082  -0.1360 -0.2425 12  ASP   Q CA  
28542 C  C   . ASP   Q  14  ? 2.1056 0.7864 1.7926 0.0824  -0.1228 -0.2365 12  ASP   Q C   
28543 O  O   . ASP   Q  14  ? 2.0677 0.5849 1.7949 0.0649  -0.1134 -0.3202 12  ASP   Q O   
28544 C  CB  . ASP   Q  14  ? 2.2521 0.8483 1.8664 0.0572  -0.1702 -0.2629 12  ASP   Q CB  
28545 C  CG  . ASP   Q  14  ? 2.2635 0.9173 1.9589 0.0528  -0.1808 -0.2148 12  ASP   Q CG  
28546 O  OD1 . ASP   Q  14  ? 2.3613 0.9489 1.9313 -0.0079 -0.1764 -0.2589 12  ASP   Q OD1 
28547 O  OD2 . ASP   Q  14  ? 2.4378 0.9348 2.0153 -0.0348 -0.2400 -0.1956 12  ASP   Q OD2 
28548 N  N   . GLY   Q  15  ? 2.0777 0.8023 1.7598 0.1017  -0.1288 -0.2131 13  GLY   Q N   
28549 C  CA  . GLY   Q  15  ? 2.0409 0.8394 1.6914 0.1210  -0.1402 -0.1534 13  GLY   Q CA  
28550 C  C   . GLY   Q  15  ? 2.0804 0.8314 1.6725 0.1528  -0.1257 -0.1161 13  GLY   Q C   
28551 O  O   . GLY   Q  15  ? 2.0528 0.6280 1.7212 0.1695  -0.1008 -0.2410 13  GLY   Q O   
28552 N  N   . HIS   Q  16  ? 2.0512 0.9151 1.6582 0.1656  -0.1677 -0.0897 14  HIS   Q N   
28553 C  CA  . HIS   Q  16  ? 2.1197 0.9421 1.5947 0.2032  -0.1840 -0.0823 14  HIS   Q CA  
28554 C  C   . HIS   Q  16  ? 2.0659 0.7660 1.5535 0.1644  -0.2347 -0.0551 14  HIS   Q C   
28555 O  O   . HIS   Q  16  ? 2.1070 0.7459 1.5300 0.1417  -0.2882 -0.0939 14  HIS   Q O   
28556 C  CB  . HIS   Q  16  ? 2.1659 0.9807 1.5809 0.2338  -0.2152 -0.1296 14  HIS   Q CB  
28557 C  CG  . HIS   Q  16  ? 2.2578 1.0631 1.6269 0.3450  -0.2086 -0.1516 14  HIS   Q CG  
28558 N  ND1 . HIS   Q  16  ? 2.3275 1.0850 1.6483 0.3949  -0.1927 -0.1557 14  HIS   Q ND1 
28559 C  CD2 . HIS   Q  16  ? 2.2560 0.9885 1.6343 0.3896  -0.1787 -0.1739 14  HIS   Q CD2 
28560 C  CE1 . HIS   Q  16  ? 2.3224 1.2406 1.6650 0.4022  -0.1694 -0.1433 14  HIS   Q CE1 
28561 N  NE2 . HIS   Q  16  ? 2.2670 1.1402 1.6326 0.4656  -0.1438 -0.2090 14  HIS   Q NE2 
28562 N  N   . ILE   Q  17  ? 2.0120 0.7550 1.5257 0.1179  -0.2439 -0.0359 15  ILE   Q N   
28563 C  CA  . ILE   Q  17  ? 1.9425 0.8029 1.4927 0.1004  -0.2610 -0.0104 15  ILE   Q CA  
28564 C  C   . ILE   Q  17  ? 1.9995 0.6976 1.4909 0.0973  -0.3147 -0.0127 15  ILE   Q C   
28565 O  O   . ILE   Q  17  ? 1.9076 0.6077 1.5027 0.0213  -0.3204 -0.0083 15  ILE   Q O   
28566 C  CB  . ILE   Q  17  ? 1.9125 0.8169 1.4583 0.1329  -0.2262 0.0378  15  ILE   Q CB  
28567 C  CG1 . ILE   Q  17  ? 1.8925 0.9116 1.4641 0.1419  -0.1990 0.0274  15  ILE   Q CG1 
28568 C  CG2 . ILE   Q  17  ? 1.8561 0.8847 1.4512 0.1416  -0.2192 0.0797  15  ILE   Q CG2 
28569 C  CD1 . ILE   Q  17  ? 1.8960 0.9093 1.4623 0.1389  -0.1884 0.0176  15  ILE   Q CD1 
28570 N  N   . PHE   Q  18  ? 2.0224 0.5751 1.5163 0.1008  -0.3546 -0.0682 16  PHE   Q N   
28571 C  CA  . PHE   Q  18  ? 2.0824 0.4989 1.5530 0.1215  -0.4015 -0.0864 16  PHE   Q CA  
28572 C  C   . PHE   Q  18  ? 2.0979 0.4698 1.6128 0.1308  -0.3705 -0.0894 16  PHE   Q C   
28573 O  O   . PHE   Q  18  ? 2.1505 0.5039 1.6843 0.1005  -0.4232 -0.0698 16  PHE   Q O   
28574 C  CB  . PHE   Q  18  ? 2.1066 0.5333 1.5406 0.1592  -0.4051 -0.0571 16  PHE   Q CB  
28575 C  CG  . PHE   Q  18  ? 2.1726 0.5404 1.5769 0.1903  -0.4290 -0.0271 16  PHE   Q CG  
28576 C  CD1 . PHE   Q  18  ? 2.1980 0.4172 1.6078 0.2238  -0.4406 -0.0646 16  PHE   Q CD1 
28577 C  CD2 . PHE   Q  18  ? 2.1946 0.4111 1.6282 0.2234  -0.4234 -0.0341 16  PHE   Q CD2 
28578 C  CE1 . PHE   Q  18  ? 2.2711 0.2902 1.6072 0.1772  -0.4531 -0.0613 16  PHE   Q CE1 
28579 C  CE2 . PHE   Q  18  ? 2.2557 0.3159 1.6437 0.1891  -0.4543 -0.0627 16  PHE   Q CE2 
28580 C  CZ  . PHE   Q  18  ? 2.2493 0.3507 1.6176 0.1922  -0.4698 -0.0445 16  PHE   Q CZ  
28581 N  N   . GLN   Q  19  ? 2.0613 0.4740 1.5289 0.1011  -0.3874 -0.0762 17  GLN   Q N   
28582 C  CA  . GLN   Q  19  ? 2.0385 0.4316 1.5307 0.0704  -0.3695 -0.0747 17  GLN   Q CA  
28583 C  C   . GLN   Q  19  ? 2.0359 0.4255 1.5233 0.0542  -0.3900 -0.0817 17  GLN   Q C   
28584 O  O   . GLN   Q  19  ? 2.0598 0.3626 1.5503 0.0508  -0.4169 -0.0818 17  GLN   Q O   
28585 C  CB  . GLN   Q  19  ? 1.9904 0.4507 1.4921 0.0643  -0.3172 -0.0438 17  GLN   Q CB  
28586 C  CG  . GLN   Q  19  ? 1.9765 0.4352 1.5085 0.0638  -0.3236 -0.0222 17  GLN   Q CG  
28587 C  CD  . GLN   Q  19  ? 1.9814 0.3816 1.4909 0.0431  -0.3245 -0.0082 17  GLN   Q CD  
28588 O  OE1 . GLN   Q  19  ? 1.9978 0.3923 1.4225 0.0184  -0.3609 -0.0382 17  GLN   Q OE1 
28589 N  NE2 . GLN   Q  19  ? 1.9405 0.5086 1.5037 0.0777  -0.3558 0.0465  17  GLN   Q NE2 
28590 N  N   . VAL   Q  20  ? 2.0185 0.5027 1.4950 0.0539  -0.4011 -0.0818 18  VAL   Q N   
28591 C  CA  . VAL   Q  20  ? 1.9868 0.5726 1.4830 0.0671  -0.4141 -0.0665 18  VAL   Q CA  
28592 C  C   . VAL   Q  20  ? 2.0489 0.5582 1.5461 0.0809  -0.4177 -0.0996 18  VAL   Q C   
28593 O  O   . VAL   Q  20  ? 2.0766 0.5512 1.5523 0.0781  -0.4505 -0.1335 18  VAL   Q O   
28594 C  CB  . VAL   Q  20  ? 1.9614 0.5938 1.4339 0.0892  -0.4138 0.0039  18  VAL   Q CB  
28595 C  CG1 . VAL   Q  20  ? 1.9570 0.5860 1.4566 0.0695  -0.4182 0.0360  18  VAL   Q CG1 
28596 C  CG2 . VAL   Q  20  ? 1.9247 0.5390 1.4214 0.0827  -0.4054 0.0394  18  VAL   Q CG2 
28597 N  N   . GLU   Q  21  ? 2.0761 0.5509 1.5895 0.0901  -0.3963 -0.1248 19  GLU   Q N   
28598 C  CA  . GLU   Q  21  ? 2.1104 0.5863 1.6328 0.0728  -0.3919 -0.1661 19  GLU   Q CA  
28599 C  C   . GLU   Q  21  ? 2.1025 0.4701 1.5479 0.1012  -0.3702 -0.2006 19  GLU   Q C   
28600 O  O   . GLU   Q  21  ? 2.1236 0.4892 1.5396 0.1201  -0.3964 -0.1600 19  GLU   Q O   
28601 C  CB  . GLU   Q  21  ? 2.0687 0.6603 1.7508 0.0900  -0.4133 -0.1569 19  GLU   Q CB  
28602 C  CG  . GLU   Q  21  ? 2.1000 0.8028 1.8698 -0.0145 -0.3725 -0.1382 19  GLU   Q CG  
28603 C  CD  . GLU   Q  21  ? 2.1264 0.9595 1.9881 0.0069  -0.3939 -0.0650 19  GLU   Q CD  
28604 O  OE1 . GLU   Q  21  ? 2.1832 0.9905 2.0935 -0.0383 -0.3600 -0.0392 19  GLU   Q OE1 
28605 O  OE2 . GLU   Q  21  ? 2.2128 1.1154 2.1723 -0.1358 -0.3587 -0.0185 19  GLU   Q OE2 
28606 N  N   . TYR   Q  22  ? 2.1267 0.4516 1.5137 0.1181  -0.3705 -0.2097 20  TYR   Q N   
28607 C  CA  . TYR   Q  22  ? 2.1161 0.5013 1.5141 0.1391  -0.3253 -0.1933 20  TYR   Q CA  
28608 C  C   . TYR   Q  22  ? 2.1092 0.5098 1.5165 0.1160  -0.3208 -0.1607 20  TYR   Q C   
28609 O  O   . TYR   Q  22  ? 2.1429 0.5648 1.5516 0.0705  -0.3309 -0.1626 20  TYR   Q O   
28610 C  CB  . TYR   Q  22  ? 2.1543 0.4929 1.5198 0.2112  -0.3021 -0.1764 20  TYR   Q CB  
28611 C  CG  . TYR   Q  22  ? 2.2423 0.4863 1.5554 0.2318  -0.2562 -0.1358 20  TYR   Q CG  
28612 C  CD1 . TYR   Q  22  ? 2.3283 0.4787 1.5353 0.2549  -0.2388 -0.1273 20  TYR   Q CD1 
28613 C  CD2 . TYR   Q  22  ? 2.2846 0.4912 1.5918 0.2451  -0.1825 -0.0745 20  TYR   Q CD2 
28614 C  CE1 . TYR   Q  22  ? 2.3879 0.4306 1.5976 0.2765  -0.1788 -0.1187 20  TYR   Q CE1 
28615 C  CE2 . TYR   Q  22  ? 2.3387 0.4508 1.6052 0.2587  -0.1301 -0.0752 20  TYR   Q CE2 
28616 C  CZ  . TYR   Q  22  ? 2.3878 0.2943 1.6231 0.2854  -0.1754 -0.0240 20  TYR   Q CZ  
28617 O  OH  . TYR   Q  22  ? 2.4718 0.1540 1.7105 0.2403  -0.0554 -0.0552 20  TYR   Q OH  
28618 N  N   . ALA   Q  23  ? 2.0430 0.5509 1.5200 0.0706  -0.3252 -0.1601 21  ALA   Q N   
28619 C  CA  . ALA   Q  23  ? 2.0116 0.5847 1.5596 0.0881  -0.3450 -0.1521 21  ALA   Q CA  
28620 C  C   . ALA   Q  23  ? 1.9878 0.5592 1.5453 0.1042  -0.3878 -0.1099 21  ALA   Q C   
28621 O  O   . ALA   Q  23  ? 2.0298 0.5518 1.5740 0.0953  -0.4051 -0.0374 21  ALA   Q O   
28622 C  CB  . ALA   Q  23  ? 1.9917 0.6066 1.5308 0.0837  -0.3309 -0.1698 21  ALA   Q CB  
28623 N  N   . LEU   Q  24  ? 2.0046 0.5808 1.5437 0.0905  -0.3643 -0.1535 22  LEU   Q N   
28624 C  CA  . LEU   Q  24  ? 2.0126 0.6055 1.5413 0.1083  -0.3767 -0.1677 22  LEU   Q CA  
28625 C  C   . LEU   Q  24  ? 2.0480 0.6631 1.6016 0.0840  -0.4028 -0.1952 22  LEU   Q C   
28626 O  O   . LEU   Q  24  ? 2.0913 0.5235 1.6014 0.0458  -0.3924 -0.1231 22  LEU   Q O   
28627 C  CB  . LEU   Q  24  ? 2.0184 0.6326 1.5465 0.1249  -0.3783 -0.1809 22  LEU   Q CB  
28628 C  CG  . LEU   Q  24  ? 1.9978 0.6726 1.5089 0.1360  -0.3636 -0.1658 22  LEU   Q CG  
28629 C  CD1 . LEU   Q  24  ? 1.9860 0.7378 1.5511 0.1249  -0.3592 -0.1831 22  LEU   Q CD1 
28630 C  CD2 . LEU   Q  24  ? 2.0108 0.7015 1.5000 0.1548  -0.3690 -0.1780 22  LEU   Q CD2 
28631 N  N   . GLU   Q  25  ? 2.0529 0.7618 1.5820 0.0747  -0.3839 -0.1742 23  GLU   Q N   
28632 C  CA  . GLU   Q  25  ? 2.0643 0.8205 1.6304 0.0703  -0.4397 -0.2235 23  GLU   Q CA  
28633 C  C   . GLU   Q  25  ? 2.0741 0.8175 1.6032 0.0686  -0.4651 -0.2410 23  GLU   Q C   
28634 O  O   . GLU   Q  25  ? 2.1103 1.0089 1.6366 0.0212  -0.5223 -0.2200 23  GLU   Q O   
28635 C  CB  . GLU   Q  25  ? 2.0205 0.8089 1.6624 0.0752  -0.4121 -0.2166 23  GLU   Q CB  
28636 C  CG  . GLU   Q  25  ? 2.0061 0.8850 1.6970 0.0955  -0.3920 -0.2115 23  GLU   Q CG  
28637 C  CD  . GLU   Q  25  ? 1.9530 0.9716 1.7431 0.1629  -0.3434 -0.2034 23  GLU   Q CD  
28638 O  OE1 . GLU   Q  25  ? 1.9423 1.0457 1.8365 0.1169  -0.3562 -0.2082 23  GLU   Q OE1 
28639 O  OE2 . GLU   Q  25  ? 1.9602 1.0798 1.7790 0.2490  -0.3243 -0.1339 23  GLU   Q OE2 
28640 N  N   . ALA   Q  26  ? 2.0652 0.7005 1.5760 0.0242  -0.5044 -0.1944 24  ALA   Q N   
28641 C  CA  . ALA   Q  26  ? 2.0813 0.5129 1.5708 -0.0156 -0.4910 -0.1830 24  ALA   Q CA  
28642 C  C   . ALA   Q  26  ? 2.1112 0.4420 1.5736 -0.0392 -0.4952 -0.1968 24  ALA   Q C   
28643 O  O   . ALA   Q  26  ? 2.1062 0.2276 1.5876 -0.0806 -0.4973 -0.1949 24  ALA   Q O   
28644 C  CB  . ALA   Q  26  ? 2.0356 0.5146 1.5387 -0.0112 -0.4652 -0.1588 24  ALA   Q CB  
28645 N  N   . VAL   Q  27  ? 2.1108 0.5657 1.5659 -0.0508 -0.4786 -0.2033 25  VAL   Q N   
28646 C  CA  . VAL   Q  27  ? 2.1326 0.7467 1.5277 -0.0556 -0.4845 -0.2088 25  VAL   Q CA  
28647 C  C   . VAL   Q  27  ? 2.1727 0.7400 1.5464 -0.0442 -0.5036 -0.2157 25  VAL   Q C   
28648 O  O   . VAL   Q  27  ? 2.2446 0.7948 1.5093 -0.0618 -0.5220 -0.2548 25  VAL   Q O   
28649 C  CB  . VAL   Q  27  ? 2.1213 0.8606 1.5306 -0.0619 -0.4541 -0.2062 25  VAL   Q CB  
28650 C  CG1 . VAL   Q  27  ? 2.1291 0.9176 1.5114 -0.0519 -0.4603 -0.2172 25  VAL   Q CG1 
28651 C  CG2 . VAL   Q  27  ? 2.1097 0.8774 1.5160 -0.0968 -0.4377 -0.2065 25  VAL   Q CG2 
28652 N  N   . LYS   Q  28  ? 2.1450 0.8125 1.5591 0.0059  -0.5132 -0.1716 26  LYS   Q N   
28653 C  CA  . LYS   Q  28  ? 2.1480 0.9550 1.5377 0.0130  -0.5275 -0.2450 26  LYS   Q CA  
28654 C  C   . LYS   Q  28  ? 2.1796 0.9419 1.5320 -0.0142 -0.5896 -0.2680 26  LYS   Q C   
28655 O  O   . LYS   Q  28  ? 2.1922 0.9488 1.4636 0.0147  -0.5470 -0.2460 26  LYS   Q O   
28656 C  CB  . LYS   Q  28  ? 2.1101 1.0180 1.6033 0.0560  -0.5136 -0.2639 26  LYS   Q CB  
28657 C  CG  . LYS   Q  28  ? 2.1162 1.1173 1.6001 0.0617  -0.5021 -0.2739 26  LYS   Q CG  
28658 C  CD  . LYS   Q  28  ? 2.1068 1.1503 1.6067 0.0831  -0.5070 -0.2979 26  LYS   Q CD  
28659 C  CE  . LYS   Q  28  ? 2.1116 1.2298 1.6226 0.0903  -0.5093 -0.2577 26  LYS   Q CE  
28660 N  NZ  . LYS   Q  28  ? 2.0906 1.2704 1.6210 0.1089  -0.5010 -0.2269 26  LYS   Q NZ  
28661 N  N   . ARG   Q  29  ? 2.1838 0.9713 1.6106 -0.0326 -0.5539 -0.2879 27  ARG   Q N   
28662 C  CA  . ARG   Q  29  ? 2.2045 0.9353 1.7198 -0.0559 -0.5358 -0.3144 27  ARG   Q CA  
28663 C  C   . ARG   Q  29  ? 2.2113 0.8341 1.7294 -0.0265 -0.5076 -0.3790 27  ARG   Q C   
28664 O  O   . ARG   Q  29  ? 2.2117 0.8557 1.7976 -0.0107 -0.5294 -0.4172 27  ARG   Q O   
28665 C  CB  . ARG   Q  29  ? 2.2513 0.9703 1.7494 -0.0854 -0.4997 -0.3046 27  ARG   Q CB  
28666 C  CG  . ARG   Q  29  ? 2.2687 0.9974 1.8434 -0.1162 -0.4981 -0.2797 27  ARG   Q CG  
28667 C  CD  . ARG   Q  29  ? 2.2720 1.0770 1.8717 -0.1317 -0.4796 -0.2488 27  ARG   Q CD  
28668 N  NE  . ARG   Q  29  ? 2.3115 1.1532 1.9054 -0.1017 -0.5036 -0.1829 27  ARG   Q NE  
28669 C  CZ  . ARG   Q  29  ? 2.2919 1.2298 1.9757 -0.0620 -0.4914 -0.1805 27  ARG   Q CZ  
28670 N  NH1 . ARG   Q  29  ? 2.3367 1.1435 2.0087 -0.0468 -0.4443 -0.1713 27  ARG   Q NH1 
28671 N  NH2 . ARG   Q  29  ? 2.3037 1.2483 2.0641 -0.0299 -0.4642 -0.1803 27  ARG   Q NH2 
28672 N  N   . GLY   Q  30  ? 2.1797 0.7926 1.6944 0.0319  -0.4624 -0.3916 28  GLY   Q N   
28673 C  CA  . GLY   Q  30  ? 2.1919 0.7969 1.5838 0.0222  -0.4811 -0.4165 28  GLY   Q CA  
28674 C  C   . GLY   Q  30  ? 2.2081 0.6822 1.5917 0.0335  -0.5173 -0.4573 28  GLY   Q C   
28675 O  O   . GLY   Q  30  ? 2.2316 0.5538 1.3557 -0.0378 -0.6422 -0.5003 28  GLY   Q O   
28676 N  N   . THR   Q  31  ? 2.2264 0.6650 1.6465 0.0366  -0.5104 -0.4317 29  THR   Q N   
28677 C  CA  . THR   Q  31  ? 2.2645 0.6666 1.6466 0.0458  -0.4774 -0.4263 29  THR   Q CA  
28678 C  C   . THR   Q  31  ? 2.2757 0.5722 1.6593 0.0889  -0.4430 -0.4168 29  THR   Q C   
28679 O  O   . THR   Q  31  ? 2.2247 0.4363 1.7142 0.1106  -0.3788 -0.3682 29  THR   Q O   
28680 C  CB  . THR   Q  31  ? 2.2454 0.7679 1.7200 0.0307  -0.5012 -0.3688 29  THR   Q CB  
28681 O  OG1 . THR   Q  31  ? 2.2553 0.7929 1.7835 -0.0425 -0.5053 -0.3767 29  THR   Q OG1 
28682 C  CG2 . THR   Q  31  ? 2.2322 0.7589 1.7580 0.0153  -0.5094 -0.3775 29  THR   Q CG2 
28683 N  N   . CYS   Q  32  ? 2.3243 0.7129 1.6197 0.1387  -0.3859 -0.3670 30  CYS   Q N   
28684 C  CA  . CYS   Q  32  ? 2.3489 0.8543 1.6197 0.1366  -0.3708 -0.3436 30  CYS   Q CA  
28685 C  C   . CYS   Q  32  ? 2.3051 0.8430 1.5408 0.1075  -0.4000 -0.3798 30  CYS   Q C   
28686 O  O   . CYS   Q  32  ? 2.2635 0.9967 1.5798 0.0999  -0.4111 -0.4086 30  CYS   Q O   
28687 C  CB  . CYS   Q  32  ? 2.4445 0.9564 1.5985 0.1793  -0.3422 -0.3529 30  CYS   Q CB  
28688 S  SG  . CYS   Q  32  ? 2.5222 1.0663 1.6035 0.2170  -0.2721 -0.3002 30  CYS   Q SG  
28689 N  N   . ALA   Q  33  ? 2.3406 0.8527 1.4800 0.0718  -0.3726 -0.3672 31  ALA   Q N   
28690 C  CA  . ALA   Q  33  ? 2.3868 0.9138 1.4551 0.0988  -0.3373 -0.2719 31  ALA   Q CA  
28691 C  C   . ALA   Q  33  ? 2.4341 0.8807 1.4046 0.0900  -0.3171 -0.2955 31  ALA   Q C   
28692 O  O   . ALA   Q  33  ? 2.4545 0.7613 1.3275 0.1182  -0.2289 -0.3093 31  ALA   Q O   
28693 C  CB  . ALA   Q  33  ? 2.3458 0.8638 1.4420 0.1069  -0.2968 -0.2418 31  ALA   Q CB  
28694 N  N   . VAL   Q  34  ? 2.4578 0.9322 1.4144 0.0876  -0.3723 -0.2803 32  VAL   Q N   
28695 C  CA  . VAL   Q  34  ? 2.4111 0.8788 1.4719 0.0713  -0.3875 -0.2813 32  VAL   Q CA  
28696 C  C   . VAL   Q  34  ? 2.3671 0.8819 1.4573 0.0677  -0.4427 -0.2515 32  VAL   Q C   
28697 O  O   . VAL   Q  34  ? 2.4150 0.6078 1.4539 -0.0063 -0.4483 -0.1523 32  VAL   Q O   
28698 C  CB  . VAL   Q  34  ? 2.4301 0.9556 1.5109 0.0928  -0.4178 -0.3315 32  VAL   Q CB  
28699 C  CG1 . VAL   Q  34  ? 2.4574 0.9725 1.5219 0.0697  -0.4587 -0.3269 32  VAL   Q CG1 
28700 C  CG2 . VAL   Q  34  ? 2.4568 0.9804 1.5223 0.1094  -0.3928 -0.3241 32  VAL   Q CG2 
28701 N  N   . GLY   Q  35  ? 2.3856 0.8658 1.4271 0.0370  -0.4649 -0.2614 33  GLY   Q N   
28702 C  CA  . GLY   Q  35  ? 2.4040 0.8500 1.3707 0.0776  -0.4763 -0.2612 33  GLY   Q CA  
28703 C  C   . GLY   Q  35  ? 2.4535 0.9016 1.2966 0.1022  -0.5045 -0.2651 33  GLY   Q C   
28704 O  O   . GLY   Q  35  ? 2.5181 0.8834 1.2495 0.1534  -0.4542 -0.3569 33  GLY   Q O   
28705 N  N   . VAL   Q  36  ? 2.4386 0.9093 1.3175 0.1053  -0.5351 -0.2568 34  VAL   Q N   
28706 C  CA  . VAL   Q  36  ? 2.4190 0.8661 1.3544 0.1019  -0.5216 -0.2883 34  VAL   Q CA  
28707 C  C   . VAL   Q  36  ? 2.3686 0.8661 1.3200 0.1062  -0.5276 -0.2869 34  VAL   Q C   
28708 O  O   . VAL   Q  36  ? 2.3844 0.7977 1.2906 0.0765  -0.5672 -0.2765 34  VAL   Q O   
28709 C  CB  . VAL   Q  36  ? 2.4665 0.8546 1.3931 0.0893  -0.5263 -0.3113 34  VAL   Q CB  
28710 C  CG1 . VAL   Q  36  ? 2.4861 0.8337 1.3393 0.0578  -0.5491 -0.2986 34  VAL   Q CG1 
28711 C  CG2 . VAL   Q  36  ? 2.4982 0.8756 1.4584 0.0923  -0.5428 -0.2764 34  VAL   Q CG2 
28712 N  N   . LYS   Q  37  ? 2.3559 0.7723 1.2612 0.1424  -0.4951 -0.2871 35  LYS   Q N   
28713 C  CA  . LYS   Q  37  ? 2.3853 0.8190 1.2786 0.1868  -0.4211 -0.2056 35  LYS   Q CA  
28714 C  C   . LYS   Q  37  ? 2.4190 0.8464 1.3197 0.1976  -0.3679 -0.2595 35  LYS   Q C   
28715 O  O   . LYS   Q  37  ? 2.4874 0.6584 1.2937 0.2236  -0.4172 -0.0717 35  LYS   Q O   
28716 C  CB  . LYS   Q  37  ? 2.2896 0.8575 1.3452 0.1809  -0.4217 -0.1733 35  LYS   Q CB  
28717 C  CG  . LYS   Q  37  ? 2.2819 0.8839 1.3718 0.1783  -0.3888 -0.1723 35  LYS   Q CG  
28718 C  CD  . LYS   Q  37  ? 2.2279 0.8613 1.3882 0.1505  -0.3565 -0.2082 35  LYS   Q CD  
28719 C  CE  . LYS   Q  37  ? 2.2429 0.8845 1.3510 0.1390  -0.3221 -0.2427 35  LYS   Q CE  
28720 N  NZ  . LYS   Q  37  ? 2.2336 0.8943 1.3206 0.1464  -0.2844 -0.2569 35  LYS   Q NZ  
28721 N  N   . GLY   Q  38  ? 2.4590 0.9014 1.3547 0.2083  -0.3749 -0.2347 36  GLY   Q N   
28722 C  CA  . GLY   Q  38  ? 2.5002 0.9429 1.3807 0.1516  -0.3266 -0.2374 36  GLY   Q CA  
28723 C  C   . GLY   Q  38  ? 2.5518 0.8477 1.3873 0.1588  -0.3136 -0.2721 36  GLY   Q C   
28724 O  O   . GLY   Q  38  ? 2.5206 0.4681 1.3335 0.1411  -0.2161 -0.4014 36  GLY   Q O   
28725 N  N   . LYS   Q  39  ? 2.6287 0.9447 1.4265 0.1200  -0.2915 -0.2138 37  LYS   Q N   
28726 C  CA  . LYS   Q  39  ? 2.6048 1.1814 1.4388 0.0611  -0.2628 -0.1486 37  LYS   Q CA  
28727 C  C   . LYS   Q  39  ? 2.6089 1.2474 1.3056 0.0907  -0.2810 -0.1894 37  LYS   Q C   
28728 O  O   . LYS   Q  39  ? 2.6238 1.2721 1.2094 0.0863  -0.2880 -0.3096 37  LYS   Q O   
28729 C  CB  . LYS   Q  39  ? 2.6849 1.3107 1.4411 0.0375  -0.2764 -0.1292 37  LYS   Q CB  
28730 C  CG  . LYS   Q  39  ? 2.6855 1.4424 1.5233 0.0292  -0.2697 -0.1096 37  LYS   Q CG  
28731 C  CD  . LYS   Q  39  ? 2.6543 1.4643 1.5767 0.0134  -0.2749 -0.0436 37  LYS   Q CD  
28732 C  CE  . LYS   Q  39  ? 2.6650 1.4334 1.5803 -0.0312 -0.2562 -0.0188 37  LYS   Q CE  
28733 N  NZ  . LYS   Q  39  ? 2.5933 1.4529 1.5914 -0.0693 -0.2427 0.0014  37  LYS   Q NZ  
28734 N  N   . ASN   Q  40  ? 2.6373 1.3575 1.2424 0.1902  -0.2893 -0.1408 38  ASN   Q N   
28735 C  CA  . ASN   Q  40  ? 2.7217 1.3563 1.1827 0.2186  -0.3310 -0.1374 38  ASN   Q CA  
28736 C  C   . ASN   Q  40  ? 2.7237 1.2211 1.1682 0.2438  -0.3329 -0.1694 38  ASN   Q C   
28737 O  O   . ASN   Q  40  ? 2.7789 1.1892 1.1629 0.2552  -0.3145 -0.1758 38  ASN   Q O   
28738 C  CB  . ASN   Q  40  ? 2.8205 1.5019 1.2084 0.2420  -0.3066 -0.0584 38  ASN   Q CB  
28739 C  CG  . ASN   Q  40  ? 2.8524 1.6703 1.2226 0.2182  -0.3791 -0.0143 38  ASN   Q CG  
28740 O  OD1 . ASN   Q  40  ? 2.9571 1.8735 1.2841 0.2525  -0.3808 0.0988  38  ASN   Q OD1 
28741 N  ND2 . ASN   Q  40  ? 2.8815 1.6967 1.2173 0.2187  -0.3793 0.0320  38  ASN   Q ND2 
28742 N  N   . CYS   Q  41  ? 2.7340 1.0853 1.2311 0.2750  -0.3921 -0.2267 39  CYS   Q N   
28743 C  CA  . CYS   Q  41  ? 2.6895 0.9215 1.2895 0.2376  -0.4311 -0.2379 39  CYS   Q CA  
28744 C  C   . CYS   Q  41  ? 2.6638 0.8997 1.3388 0.2611  -0.4216 -0.2406 39  CYS   Q C   
28745 O  O   . CYS   Q  41  ? 2.6284 0.9434 1.3252 0.2588  -0.4564 -0.2515 39  CYS   Q O   
28746 C  CB  . CYS   Q  41  ? 2.7748 0.7536 1.3041 0.1948  -0.4699 -0.2535 39  CYS   Q CB  
28747 S  SG  . CYS   Q  41  ? 2.8725 0.6082 1.3564 0.0054  -0.5846 -0.2336 39  CYS   Q SG  
28748 N  N   . VAL   Q  42  ? 2.5628 0.9038 1.4299 0.2953  -0.3907 -0.2533 40  VAL   Q N   
28749 C  CA  . VAL   Q  42  ? 2.4842 0.8796 1.4752 0.2793  -0.4098 -0.2561 40  VAL   Q CA  
28750 C  C   . VAL   Q  42  ? 2.4935 0.7977 1.4951 0.2570  -0.4546 -0.2941 40  VAL   Q C   
28751 O  O   . VAL   Q  42  ? 2.4604 0.8172 1.6210 0.2494  -0.4743 -0.3173 40  VAL   Q O   
28752 C  CB  . VAL   Q  42  ? 2.4840 0.9011 1.4705 0.2871  -0.3907 -0.2769 40  VAL   Q CB  
28753 C  CG1 . VAL   Q  42  ? 2.5014 0.9145 1.4625 0.2912  -0.3683 -0.2688 40  VAL   Q CG1 
28754 C  CG2 . VAL   Q  42  ? 2.4752 0.9089 1.4290 0.2862  -0.3855 -0.2978 40  VAL   Q CG2 
28755 N  N   . VAL   Q  43  ? 2.4797 0.8050 1.4475 0.2282  -0.4650 -0.3203 41  VAL   Q N   
28756 C  CA  . VAL   Q  43  ? 2.4949 0.8174 1.4900 0.2187  -0.4415 -0.3028 41  VAL   Q CA  
28757 C  C   . VAL   Q  43  ? 2.5112 0.8420 1.4433 0.2107  -0.3977 -0.3331 41  VAL   Q C   
28758 O  O   . VAL   Q  43  ? 2.4870 0.8708 1.3002 0.2344  -0.3323 -0.4062 41  VAL   Q O   
28759 C  CB  . VAL   Q  43  ? 2.5216 0.7896 1.4833 0.2104  -0.4879 -0.2663 41  VAL   Q CB  
28760 C  CG1 . VAL   Q  43  ? 2.5324 0.7941 1.5288 0.1900  -0.5261 -0.2658 41  VAL   Q CG1 
28761 C  CG2 . VAL   Q  43  ? 2.5340 0.7971 1.4959 0.2147  -0.4910 -0.2516 41  VAL   Q CG2 
28762 N  N   . LEU   Q  44  ? 2.4989 0.8877 1.5219 0.1872  -0.3695 -0.3264 42  LEU   Q N   
28763 C  CA  . LEU   Q  44  ? 2.5039 0.8727 1.5905 0.1142  -0.3794 -0.3145 42  LEU   Q CA  
28764 C  C   . LEU   Q  44  ? 2.5030 0.8887 1.6570 0.1242  -0.3935 -0.3763 42  LEU   Q C   
28765 O  O   . LEU   Q  44  ? 2.5052 0.7365 1.6512 0.0781  -0.4344 -0.3596 42  LEU   Q O   
28766 C  CB  . LEU   Q  44  ? 2.4850 0.7934 1.6515 0.0748  -0.4041 -0.3422 42  LEU   Q CB  
28767 C  CG  . LEU   Q  44  ? 2.5244 0.7183 1.6765 0.0506  -0.3864 -0.3507 42  LEU   Q CG  
28768 C  CD1 . LEU   Q  44  ? 2.4747 0.7009 1.6872 0.0363  -0.3819 -0.3499 42  LEU   Q CD1 
28769 C  CD2 . LEU   Q  44  ? 2.5222 0.7148 1.6572 0.0619  -0.3633 -0.3889 42  LEU   Q CD2 
28770 N  N   . GLY   Q  45  ? 2.5569 0.9078 1.6856 0.1874  -0.3738 -0.3757 43  GLY   Q N   
28771 C  CA  . GLY   Q  45  ? 2.5484 0.8953 1.7195 0.2020  -0.3974 -0.2869 43  GLY   Q CA  
28772 C  C   . GLY   Q  45  ? 2.6031 0.9089 1.7206 0.3030  -0.4354 -0.2368 43  GLY   Q C   
28773 O  O   . GLY   Q  45  ? 2.4941 0.9294 1.7017 0.4300  -0.3420 -0.2251 43  GLY   Q O   
28774 N  N   . CYS   Q  46  ? 2.6672 0.9265 1.7851 0.2208  -0.4503 -0.1934 44  CYS   Q N   
28775 C  CA  . CYS   Q  46  ? 2.8269 0.9145 1.8149 0.1766  -0.4665 -0.1540 44  CYS   Q CA  
28776 C  C   . CYS   Q  46  ? 2.7860 0.9665 1.8735 0.1680  -0.5413 -0.0567 44  CYS   Q C   
28777 O  O   . CYS   Q  46  ? 2.8101 1.0491 1.8503 0.1552  -0.5637 -0.0237 44  CYS   Q O   
28778 C  CB  . CYS   Q  46  ? 2.9918 0.9441 1.8215 0.1793  -0.4509 -0.1876 44  CYS   Q CB  
28779 S  SG  . CYS   Q  46  ? 3.2209 0.7506 1.7980 0.1613  -0.3680 -0.2838 44  CYS   Q SG  
28780 N  N   . GLU   Q  47  ? 2.8289 0.9693 1.9855 0.1164  -0.5057 -0.0043 45  GLU   Q N   
28781 C  CA  . GLU   Q  47  ? 2.8538 1.0061 2.1041 0.0759  -0.5190 -0.0804 45  GLU   Q CA  
28782 C  C   . GLU   Q  47  ? 2.7873 1.1021 2.2045 0.1404  -0.4974 0.0048  45  GLU   Q C   
28783 O  O   . GLU   Q  47  ? 2.6603 1.2390 2.1637 0.2042  -0.4961 -0.0018 45  GLU   Q O   
28784 C  CB  . GLU   Q  47  ? 2.9269 0.8326 2.1666 -0.0217 -0.5400 -0.1670 45  GLU   Q CB  
28785 C  CG  . GLU   Q  47  ? 3.0233 0.8155 2.2152 -0.0508 -0.5696 -0.1506 45  GLU   Q CG  
28786 C  CD  . GLU   Q  47  ? 3.0407 0.5867 2.2812 -0.2052 -0.5750 -0.2071 45  GLU   Q CD  
28787 O  OE1 . GLU   Q  47  ? 3.2003 0.4545 2.3824 -0.2017 -0.6073 -0.2113 45  GLU   Q OE1 
28788 O  OE2 . GLU   Q  47  ? 3.0762 0.4641 2.2075 -0.2858 -0.6076 -0.3225 45  GLU   Q OE2 
28789 N  N   . ARG   Q  48  ? 2.7174 1.1614 2.2145 0.1824  -0.4174 0.0373  46  ARG   Q N   
28790 C  CA  . ARG   Q  48  ? 2.8047 1.2300 2.2891 0.1575  -0.3208 0.0593  46  ARG   Q CA  
28791 C  C   . ARG   Q  48  ? 2.7324 1.2584 2.2344 0.1531  -0.3098 -0.0269 46  ARG   Q C   
28792 O  O   . ARG   Q  48  ? 2.7733 0.9427 2.2057 0.2463  -0.2567 -0.0922 46  ARG   Q O   
28793 C  CB  . ARG   Q  48  ? 2.8519 1.3199 2.3786 0.2039  -0.2133 0.2047  46  ARG   Q CB  
28794 C  CG  . ARG   Q  48  ? 2.9227 1.3551 2.3910 0.0964  -0.1351 0.2616  46  ARG   Q CG  
28795 C  CD  . ARG   Q  48  ? 2.9211 1.3180 2.4645 0.0678  -0.0383 0.3373  46  ARG   Q CD  
28796 N  NE  . ARG   Q  48  ? 2.9106 1.2682 2.5184 0.0067  -0.0482 0.4007  46  ARG   Q NE  
28797 C  CZ  . ARG   Q  48  ? 2.9749 1.2852 2.5120 -0.1080 -0.0578 0.4357  46  ARG   Q CZ  
28798 N  NH1 . ARG   Q  48  ? 2.9043 1.3841 2.5316 -0.2353 -0.0853 0.3807  46  ARG   Q NH1 
28799 N  NH2 . ARG   Q  48  ? 3.0203 1.1066 2.5262 -0.1603 -0.0551 0.4626  46  ARG   Q NH2 
28800 N  N   . ARG   Q  49  ? 2.6861 1.4126 2.1623 0.0756  -0.3054 -0.0424 47  ARG   Q N   
28801 C  CA  . ARG   Q  49  ? 2.6412 1.4898 2.1915 -0.0234 -0.3256 -0.1190 47  ARG   Q CA  
28802 C  C   . ARG   Q  49  ? 2.6073 1.6134 2.2472 -0.0334 -0.2458 -0.1432 47  ARG   Q C   
28803 O  O   . ARG   Q  49  ? 2.5019 1.5494 2.3341 -0.0665 -0.2029 -0.0613 47  ARG   Q O   
28804 C  CB  . ARG   Q  49  ? 2.6355 1.5200 2.2034 -0.0415 -0.3771 -0.1278 47  ARG   Q CB  
28805 C  CG  . ARG   Q  49  ? 2.5898 1.5899 2.1442 -0.0974 -0.4364 -0.1526 47  ARG   Q CG  
28806 C  CD  . ARG   Q  49  ? 2.5567 1.5970 2.1358 -0.1519 -0.4988 -0.2069 47  ARG   Q CD  
28807 N  NE  . ARG   Q  49  ? 2.4928 1.6539 2.0609 -0.2068 -0.5857 -0.2253 47  ARG   Q NE  
28808 C  CZ  . ARG   Q  49  ? 2.4615 1.7037 2.0125 -0.1677 -0.5862 -0.2636 47  ARG   Q CZ  
28809 N  NH1 . ARG   Q  49  ? 2.4656 1.6840 2.0379 -0.1454 -0.6737 -0.2093 47  ARG   Q NH1 
28810 N  NH2 . ARG   Q  49  ? 2.4128 1.7160 2.0760 -0.1807 -0.4951 -0.2838 47  ARG   Q NH2 
28811 N  N   . SER   Q  50  ? 2.6769 1.7803 2.2720 -0.1344 -0.2282 -0.2126 48  SER   Q N   
28812 C  CA  . SER   Q  50  ? 2.7679 2.0505 2.2965 -0.1479 -0.3279 -0.2686 48  SER   Q CA  
28813 C  C   . SER   Q  50  ? 2.7028 2.1190 2.5377 -0.2220 -0.2663 -0.3279 48  SER   Q C   
28814 O  O   . SER   Q  50  ? 2.8422 2.4390 2.3813 -0.2195 -0.4018 -0.4176 48  SER   Q O   
28815 C  CB  . SER   Q  50  ? 2.8332 2.1098 2.2160 -0.2206 -0.3388 -0.1600 48  SER   Q CB  
28816 O  OG  . SER   Q  50  ? 2.8940 2.2346 2.1540 -0.2334 -0.3628 -0.0200 48  SER   Q OG  
28817 N  N   . THR   Q  51  ? 2.6296 2.1583 2.6454 -0.0411 -0.3277 -0.3539 49  THR   Q N   
28818 C  CA  . THR   Q  51  ? 2.4230 2.1108 2.8053 -0.0210 -0.3539 -0.3266 49  THR   Q CA  
28819 C  C   . THR   Q  51  ? 2.3639 2.0985 3.1016 -0.1018 -0.2929 -0.4229 49  THR   Q C   
28820 O  O   . THR   Q  51  ? 2.0833 2.3876 3.4065 -0.2477 -0.3084 -0.5324 49  THR   Q O   
28821 C  CB  . THR   Q  51  ? 2.2967 1.9860 2.7835 0.0108  -0.3237 -0.3597 49  THR   Q CB  
28822 O  OG1 . THR   Q  51  ? 2.1461 1.8555 2.5979 0.2008  -0.4181 -0.3510 49  THR   Q OG1 
28823 C  CG2 . THR   Q  51  ? 2.2486 1.9720 2.6766 0.0198  -0.3417 -0.3147 49  THR   Q CG2 
28824 N  N   . LEU   Q  52  ? 2.4151 2.0276 3.1719 0.0007  -0.2990 -0.4620 50  LEU   Q N   
28825 C  CA  . LEU   Q  52  ? 2.3809 2.0785 3.1110 0.1247  -0.3594 -0.2931 50  LEU   Q CA  
28826 C  C   . LEU   Q  52  ? 2.2931 1.9270 3.0975 0.0410  -0.3957 -0.3405 50  LEU   Q C   
28827 O  O   . LEU   Q  52  ? 2.1469 2.1388 3.2140 0.0809  -0.3721 -0.1684 50  LEU   Q O   
28828 C  CB  . LEU   Q  52  ? 2.4043 2.0849 3.0597 0.1931  -0.3329 -0.3639 50  LEU   Q CB  
28829 C  CG  . LEU   Q  52  ? 2.4631 2.0396 2.9639 0.2285  -0.3487 -0.4033 50  LEU   Q CG  
28830 C  CD1 . LEU   Q  52  ? 2.4963 1.8753 2.8203 0.3292  -0.3325 -0.4593 50  LEU   Q CD1 
28831 C  CD2 . LEU   Q  52  ? 2.4726 2.1641 2.9046 0.2768  -0.3306 -0.4125 50  LEU   Q CD2 
28832 N  N   . LYS   Q  53  ? 2.4361 1.6015 2.6992 0.0431  -0.5099 -0.3186 51  LYS   Q N   
28833 C  CA  . LYS   Q  53  ? 2.5821 1.5869 2.4703 0.0237  -0.4946 -0.2840 51  LYS   Q CA  
28834 C  C   . LYS   Q  53  ? 2.4709 1.2132 2.3387 0.0332  -0.6641 -0.2089 51  LYS   Q C   
28835 O  O   . LYS   Q  53  ? 2.6719 1.3867 2.3475 -0.0761 -0.5494 -0.2359 51  LYS   Q O   
28836 C  CB  . LYS   Q  53  ? 2.6193 1.6848 2.3455 0.0273  -0.5030 -0.2673 51  LYS   Q CB  
28837 C  CG  . LYS   Q  53  ? 2.6896 1.8095 2.3757 0.1012  -0.4544 -0.1843 51  LYS   Q CG  
28838 C  CD  . LYS   Q  53  ? 2.7096 1.8683 2.3391 0.1704  -0.3663 -0.1537 51  LYS   Q CD  
28839 C  CE  . LYS   Q  53  ? 2.7099 1.9401 2.3597 0.2150  -0.3093 -0.1385 51  LYS   Q CE  
28840 N  NZ  . LYS   Q  53  ? 2.6902 1.9584 2.3322 0.2446  -0.2613 -0.1864 51  LYS   Q NZ  
28841 N  N   . LEU   Q  54  ? 2.3622 1.0701 2.0683 -0.0953 -0.6601 -0.2416 52  LEU   Q N   
28842 C  CA  . LEU   Q  54  ? 2.2289 0.9808 1.9465 -0.1224 -0.7322 -0.1783 52  LEU   Q CA  
28843 C  C   . LEU   Q  54  ? 2.2033 0.9752 1.7815 -0.0681 -0.6798 -0.2299 52  LEU   Q C   
28844 O  O   . LEU   Q  54  ? 2.1923 0.9638 1.6648 -0.1442 -0.7188 -0.2461 52  LEU   Q O   
28845 C  CB  . LEU   Q  54  ? 2.1251 0.9183 1.9532 -0.1505 -0.7631 -0.2232 52  LEU   Q CB  
28846 C  CG  . LEU   Q  54  ? 2.1707 0.7888 1.9715 -0.2113 -0.8030 -0.2606 52  LEU   Q CG  
28847 C  CD1 . LEU   Q  54  ? 2.1985 0.7509 1.9862 -0.2308 -0.8386 -0.2621 52  LEU   Q CD1 
28848 C  CD2 . LEU   Q  54  ? 2.1362 0.7407 1.9919 -0.2524 -0.8137 -0.2911 52  LEU   Q CD2 
28849 N  N   . GLN   Q  55  ? 2.2035 1.0468 1.7533 -0.0696 -0.6860 -0.2403 53  GLN   Q N   
28850 C  CA  . GLN   Q  55  ? 2.1742 1.1169 1.7716 -0.0915 -0.6591 -0.2828 53  GLN   Q CA  
28851 C  C   . GLN   Q  55  ? 2.1750 1.1926 1.7648 -0.0342 -0.6914 -0.2853 53  GLN   Q C   
28852 O  O   . GLN   Q  55  ? 2.1279 1.2103 1.7941 -0.0409 -0.6918 -0.3610 53  GLN   Q O   
28853 C  CB  . GLN   Q  55  ? 2.1936 1.1583 1.7767 -0.0784 -0.6261 -0.2526 53  GLN   Q CB  
28854 C  CG  . GLN   Q  55  ? 2.1795 1.1715 1.8089 -0.0689 -0.5710 -0.1953 53  GLN   Q CG  
28855 C  CD  . GLN   Q  55  ? 2.0987 1.2733 1.8642 -0.0802 -0.5084 -0.1682 53  GLN   Q CD  
28856 O  OE1 . GLN   Q  55  ? 2.0886 1.2489 1.9351 -0.0362 -0.4459 -0.1574 53  GLN   Q OE1 
28857 N  NE2 . GLN   Q  55  ? 2.1445 1.3237 1.8719 -0.0583 -0.4527 -0.1764 53  GLN   Q NE2 
28858 N  N   . ASP   Q  56  ? 2.2282 1.1721 1.8424 0.0121  -0.6494 -0.3154 54  ASP   Q N   
28859 C  CA  . ASP   Q  56  ? 2.3149 1.2094 1.9109 0.0598  -0.6695 -0.2805 54  ASP   Q CA  
28860 C  C   . ASP   Q  56  ? 2.3793 1.1945 1.9297 0.0748  -0.5199 -0.2923 54  ASP   Q C   
28861 O  O   . ASP   Q  56  ? 2.4416 1.2708 1.8900 0.1550  -0.5371 -0.3100 54  ASP   Q O   
28862 C  CB  . ASP   Q  56  ? 2.1906 1.2768 1.9106 0.0709  -0.7046 -0.2566 54  ASP   Q CB  
28863 C  CG  . ASP   Q  56  ? 2.1679 1.3743 1.9761 0.0951  -0.8205 -0.2142 54  ASP   Q CG  
28864 O  OD1 . ASP   Q  56  ? 2.1847 1.4521 1.8794 0.1371  -0.8760 -0.2051 54  ASP   Q OD1 
28865 O  OD2 . ASP   Q  56  ? 2.0378 1.3225 2.0030 0.1087  -0.9192 -0.1121 54  ASP   Q OD2 
28866 N  N   . THR   Q  57  ? 2.5116 1.2253 1.9638 0.0798  -0.4508 -0.2739 55  THR   Q N   
28867 C  CA  . THR   Q  57  ? 2.5309 1.1811 1.9661 0.0854  -0.4067 -0.2800 55  THR   Q CA  
28868 C  C   . THR   Q  57  ? 2.4478 1.1916 2.0521 -0.0043 -0.3895 -0.2338 55  THR   Q C   
28869 O  O   . THR   Q  57  ? 2.4158 1.0933 2.0725 0.0344  -0.4174 -0.2198 55  THR   Q O   
28870 C  CB  . THR   Q  57  ? 2.5883 1.1819 1.9795 0.1327  -0.3730 -0.2710 55  THR   Q CB  
28871 O  OG1 . THR   Q  57  ? 2.6562 1.1664 1.9092 0.1841  -0.3779 -0.3327 55  THR   Q OG1 
28872 C  CG2 . THR   Q  57  ? 2.5372 1.1686 1.9322 0.1069  -0.3794 -0.2627 55  THR   Q CG2 
28873 N  N   . ARG   Q  58  ? 2.4543 1.2254 2.1472 0.0153  -0.3590 -0.1506 56  ARG   Q N   
28874 C  CA  . ARG   Q  58  ? 2.4203 1.2345 2.2489 0.1027  -0.3350 -0.0757 56  ARG   Q CA  
28875 C  C   . ARG   Q  58  ? 2.4847 1.3966 2.2325 0.1237  -0.3194 -0.1137 56  ARG   Q C   
28876 O  O   . ARG   Q  58  ? 2.4880 1.4834 2.3447 0.0778  -0.2967 -0.1426 56  ARG   Q O   
28877 C  CB  . ARG   Q  58  ? 2.3835 1.3495 2.2690 0.0929  -0.3715 0.0190  56  ARG   Q CB  
28878 C  CG  . ARG   Q  58  ? 2.3293 1.3208 2.2830 0.1068  -0.3886 0.0688  56  ARG   Q CG  
28879 C  CD  . ARG   Q  58  ? 2.3170 1.3750 2.3472 0.1093  -0.3811 0.0970  56  ARG   Q CD  
28880 N  NE  . ARG   Q  58  ? 2.2401 1.2972 2.3983 0.1496  -0.3594 0.1268  56  ARG   Q NE  
28881 C  CZ  . ARG   Q  58  ? 2.1857 1.3422 2.4479 0.1741  -0.3450 0.1318  56  ARG   Q CZ  
28882 N  NH1 . ARG   Q  58  ? 2.1780 1.3551 2.4732 0.2365  -0.3546 0.1016  56  ARG   Q NH1 
28883 N  NH2 . ARG   Q  58  ? 2.1275 1.2302 2.4830 0.1900  -0.3464 0.1530  56  ARG   Q NH2 
28884 N  N   . ILE   Q  59  ? 2.4615 1.3193 2.2111 0.1421  -0.3042 -0.1578 57  ILE   Q N   
28885 C  CA  . ILE   Q  59  ? 2.4393 1.3377 2.2304 0.2062  -0.2881 -0.2172 57  ILE   Q CA  
28886 C  C   . ILE   Q  59  ? 2.3780 1.4172 2.3248 0.2315  -0.3015 -0.2572 57  ILE   Q C   
28887 O  O   . ILE   Q  59  ? 2.3814 1.6415 2.2921 0.2930  -0.3128 -0.3104 57  ILE   Q O   
28888 C  CB  . ILE   Q  59  ? 2.4626 1.1758 2.1713 0.2052  -0.2884 -0.2359 57  ILE   Q CB  
28889 C  CG1 . ILE   Q  59  ? 2.5394 1.1002 2.1212 0.2429  -0.2937 -0.2671 57  ILE   Q CG1 
28890 C  CG2 . ILE   Q  59  ? 2.4961 1.1832 2.1661 0.2153  -0.2863 -0.2064 57  ILE   Q CG2 
28891 C  CD1 . ILE   Q  59  ? 2.5582 1.0455 2.1057 0.2690  -0.2891 -0.2420 57  ILE   Q CD1 
28892 N  N   . THR   Q  60  ? 2.3250 1.4140 2.4495 0.1463  -0.3381 -0.3174 58  THR   Q N   
28893 C  CA  . THR   Q  60  ? 2.3217 1.4191 2.5232 0.1904  -0.3148 -0.3506 58  THR   Q CA  
28894 C  C   . THR   Q  60  ? 2.2792 1.4997 2.5205 0.2204  -0.3092 -0.3485 58  THR   Q C   
28895 O  O   . THR   Q  60  ? 2.2646 1.5048 2.3280 0.2445  -0.4859 -0.4372 58  THR   Q O   
28896 C  CB  . THR   Q  60  ? 2.3595 1.4251 2.6426 0.2330  -0.2809 -0.3823 58  THR   Q CB  
28897 O  OG1 . THR   Q  60  ? 2.2843 1.4944 2.7920 0.2894  -0.2575 -0.3789 58  THR   Q OG1 
28898 C  CG2 . THR   Q  60  ? 2.3218 1.4462 2.6115 0.2186  -0.2714 -0.3940 58  THR   Q CG2 
28899 N  N   . PRO   Q  61  ? 2.2738 1.6194 2.4369 0.2709  -0.2435 -0.2586 59  PRO   Q N   
28900 C  CA  . PRO   Q  61  ? 2.3007 1.5820 2.3960 0.2752  -0.1241 -0.2878 59  PRO   Q CA  
28901 C  C   . PRO   Q  61  ? 2.3807 1.3405 2.3527 0.2336  -0.1206 -0.2653 59  PRO   Q C   
28902 O  O   . PRO   Q  61  ? 2.4319 1.4131 2.2448 0.3198  -0.1096 -0.5758 59  PRO   Q O   
28903 C  CB  . PRO   Q  61  ? 2.3059 1.6154 2.3979 0.2705  -0.1212 -0.2572 59  PRO   Q CB  
28904 C  CG  . PRO   Q  61  ? 2.2760 1.6207 2.3692 0.2635  -0.1468 -0.2380 59  PRO   Q CG  
28905 C  CD  . PRO   Q  61  ? 2.2322 1.6388 2.4824 0.2617  -0.1590 -0.2328 59  PRO   Q CD  
28906 N  N   . SER   Q  62  ? 2.3505 1.3668 2.1916 0.2602  -0.0898 -0.3033 60  SER   Q N   
28907 C  CA  . SER   Q  62  ? 2.3072 1.1666 2.0188 0.1580  -0.1536 -0.1964 60  SER   Q CA  
28908 C  C   . SER   Q  62  ? 2.2966 1.0103 2.0555 0.1932  -0.0929 -0.1922 60  SER   Q C   
28909 O  O   . SER   Q  62  ? 2.2973 0.8895 2.0578 0.2402  -0.1407 -0.1264 60  SER   Q O   
28910 C  CB  . SER   Q  62  ? 2.2650 1.3116 1.7629 0.1142  -0.1153 -0.2214 60  SER   Q CB  
28911 O  OG  . SER   Q  62  ? 2.2783 1.3412 1.5525 -0.0063 -0.2414 -0.2360 60  SER   Q OG  
28912 N  N   . LYS   Q  63  ? 2.2071 0.9513 2.0375 0.1567  -0.1528 -0.2044 61  LYS   Q N   
28913 C  CA  . LYS   Q  63  ? 2.1727 1.0291 2.0066 0.1299  -0.1699 -0.1678 61  LYS   Q CA  
28914 C  C   . LYS   Q  63  ? 2.2142 0.8588 1.7931 0.1488  -0.2375 -0.1795 61  LYS   Q C   
28915 O  O   . LYS   Q  63  ? 2.2112 0.9165 1.6977 0.0875  -0.2118 -0.1933 61  LYS   Q O   
28916 C  CB  . LYS   Q  63  ? 2.1879 1.0212 2.1021 0.2144  -0.1485 -0.1459 61  LYS   Q CB  
28917 C  CG  . LYS   Q  63  ? 2.1749 1.0684 2.1648 0.2180  -0.1002 -0.0686 61  LYS   Q CG  
28918 C  CD  . LYS   Q  63  ? 2.1323 1.0265 2.2002 0.2370  -0.0973 -0.0768 61  LYS   Q CD  
28919 C  CE  . LYS   Q  63  ? 2.0917 0.8997 2.1794 0.2553  -0.0450 -0.0887 61  LYS   Q CE  
28920 N  NZ  . LYS   Q  63  ? 2.1779 0.7445 2.1633 0.2673  -0.0219 -0.1469 61  LYS   Q NZ  
28921 N  N   . VAL   Q  64  ? 2.1359 0.7885 1.7369 0.1131  -0.3391 -0.2361 62  VAL   Q N   
28922 C  CA  . VAL   Q  64  ? 2.0938 0.7928 1.5924 0.1185  -0.3985 -0.2472 62  VAL   Q CA  
28923 C  C   . VAL   Q  64  ? 1.9847 0.7504 1.5696 0.1054  -0.4873 -0.2277 62  VAL   Q C   
28924 O  O   . VAL   Q  64  ? 2.0182 0.6456 1.5961 0.1077  -0.5231 -0.2338 62  VAL   Q O   
28925 C  CB  . VAL   Q  64  ? 2.1163 0.8228 1.5582 0.1120  -0.4314 -0.2912 62  VAL   Q CB  
28926 C  CG1 . VAL   Q  64  ? 2.1270 0.8636 1.5145 0.0919  -0.4091 -0.2928 62  VAL   Q CG1 
28927 C  CG2 . VAL   Q  64  ? 2.1382 0.8084 1.5154 0.1014  -0.4445 -0.2870 62  VAL   Q CG2 
28928 N  N   . SER   Q  65  ? 1.9716 0.6826 1.5409 0.1098  -0.4665 -0.2133 63  SER   Q N   
28929 C  CA  . SER   Q  65  ? 1.9363 0.6555 1.5213 0.1023  -0.4980 -0.1931 63  SER   Q CA  
28930 C  C   . SER   Q  65  ? 1.9418 0.6729 1.5005 0.1109  -0.4859 -0.1792 63  SER   Q C   
28931 O  O   . SER   Q  65  ? 1.9493 0.6721 1.4734 0.1493  -0.5060 -0.1753 63  SER   Q O   
28932 C  CB  . SER   Q  65  ? 1.8874 0.6308 1.5169 0.0477  -0.4865 -0.2037 63  SER   Q CB  
28933 O  OG  . SER   Q  65  ? 1.8718 0.7533 1.5359 -0.0401 -0.4792 -0.2248 63  SER   Q OG  
28934 N  N   . LYS   Q  66  ? 2.0111 0.6429 1.5132 0.0900  -0.4702 -0.1670 64  LYS   Q N   
28935 C  CA  . LYS   Q  66  ? 2.0543 0.5559 1.5259 0.1505  -0.4431 -0.1512 64  LYS   Q CA  
28936 C  C   . LYS   Q  66  ? 2.0569 0.4831 1.5276 0.1102  -0.4048 -0.1615 64  LYS   Q C   
28937 O  O   . LYS   Q  66  ? 2.0424 0.3483 1.5767 0.0983  -0.3793 -0.1802 64  LYS   Q O   
28938 C  CB  . LYS   Q  66  ? 2.0514 0.6085 1.5557 0.1908  -0.4540 -0.1552 64  LYS   Q CB  
28939 C  CG  . LYS   Q  66  ? 2.0552 0.6283 1.5634 0.2219  -0.4809 -0.1413 64  LYS   Q CG  
28940 C  CD  . LYS   Q  66  ? 2.0540 0.6937 1.6045 0.2405  -0.4956 -0.1179 64  LYS   Q CD  
28941 C  CE  . LYS   Q  66  ? 2.0290 0.6577 1.6068 0.2883  -0.5049 -0.0956 64  LYS   Q CE  
28942 N  NZ  . LYS   Q  66  ? 2.0506 0.6410 1.6443 0.2969  -0.4994 -0.0870 64  LYS   Q NZ  
28943 N  N   . ILE   Q  67  ? 2.0593 0.5129 1.5208 0.1060  -0.4033 -0.1263 65  ILE   Q N   
28944 C  CA  . ILE   Q  67  ? 2.0705 0.6239 1.4620 0.1266  -0.3937 -0.1166 65  ILE   Q CA  
28945 C  C   . ILE   Q  67  ? 2.0990 0.6411 1.4482 0.1540  -0.3823 -0.0581 65  ILE   Q C   
28946 O  O   . ILE   Q  67  ? 2.0052 0.7482 1.3845 0.1832  -0.3759 -0.0395 65  ILE   Q O   
28947 C  CB  . ILE   Q  67  ? 2.0721 0.5481 1.4674 0.1181  -0.3703 -0.1237 65  ILE   Q CB  
28948 C  CG1 . ILE   Q  67  ? 2.0896 0.5419 1.4716 0.0854  -0.3638 -0.1812 65  ILE   Q CG1 
28949 C  CG2 . ILE   Q  67  ? 2.0473 0.5479 1.4455 0.1152  -0.3450 -0.1217 65  ILE   Q CG2 
28950 C  CD1 . ILE   Q  67  ? 2.0844 0.5633 1.4723 0.0537  -0.3566 -0.2165 65  ILE   Q CD1 
28951 N  N   . ASP   Q  68  ? 2.1981 0.6621 1.4615 0.1701  -0.3557 -0.0408 66  ASP   Q N   
28952 C  CA  . ASP   Q  68  ? 2.2572 0.6421 1.5155 0.1578  -0.3279 -0.0532 66  ASP   Q CA  
28953 C  C   . ASP   Q  68  ? 2.3406 0.7355 1.5099 0.1746  -0.3470 -0.0402 66  ASP   Q C   
28954 O  O   . ASP   Q  68  ? 2.3676 0.7850 1.5056 0.1756  -0.3880 -0.0800 66  ASP   Q O   
28955 C  CB  . ASP   Q  68  ? 2.2521 0.5868 1.5744 0.1607  -0.2579 0.0087  66  ASP   Q CB  
28956 C  CG  . ASP   Q  68  ? 2.2750 0.5533 1.6348 0.2118  -0.1879 0.1066  66  ASP   Q CG  
28957 O  OD1 . ASP   Q  68  ? 2.2862 0.4680 1.7050 0.2082  -0.1372 0.1871  66  ASP   Q OD1 
28958 O  OD2 . ASP   Q  68  ? 2.3218 0.2662 1.5615 0.1808  -0.1035 0.1464  66  ASP   Q OD2 
28959 N  N   . SER   Q  69  ? 2.3515 0.7061 1.3661 0.1497  -0.3937 -0.1048 67  SER   Q N   
28960 C  CA  . SER   Q  69  ? 2.3596 0.6904 1.3835 0.1557  -0.4183 -0.0755 67  SER   Q CA  
28961 C  C   . SER   Q  69  ? 2.3348 0.7078 1.3915 0.1660  -0.4231 -0.0702 67  SER   Q C   
28962 O  O   . SER   Q  69  ? 2.3885 0.7439 1.3700 0.1659  -0.4119 -0.0611 67  SER   Q O   
28963 C  CB  . SER   Q  69  ? 2.3855 0.6736 1.3308 0.1434  -0.4467 -0.1073 67  SER   Q CB  
28964 O  OG  . SER   Q  69  ? 2.4158 0.7071 1.2179 0.1185  -0.4472 -0.1671 67  SER   Q OG  
28965 N  N   . HIS   Q  70  ? 2.2918 0.6682 1.4271 0.1644  -0.3859 -0.1015 68  HIS   Q N   
28966 C  CA  . HIS   Q  70  ? 2.2809 0.6419 1.4527 0.1523  -0.3851 -0.1239 68  HIS   Q CA  
28967 C  C   . HIS   Q  70  ? 2.2532 0.5975 1.4939 0.1333  -0.3588 -0.1637 68  HIS   Q C   
28968 O  O   . HIS   Q  70  ? 2.3145 0.5440 1.5459 0.1366  -0.3495 -0.2078 68  HIS   Q O   
28969 C  CB  . HIS   Q  70  ? 2.2971 0.5870 1.4363 0.1678  -0.3648 -0.1246 68  HIS   Q CB  
28970 C  CG  . HIS   Q  70  ? 2.2734 0.5505 1.4479 0.1803  -0.3645 -0.1099 68  HIS   Q CG  
28971 N  ND1 . HIS   Q  70  ? 2.2787 0.5458 1.4593 0.1912  -0.3486 -0.1013 68  HIS   Q ND1 
28972 C  CD2 . HIS   Q  70  ? 2.2672 0.5453 1.4407 0.1853  -0.3500 -0.0923 68  HIS   Q CD2 
28973 C  CE1 . HIS   Q  70  ? 2.2494 0.5066 1.4328 0.2098  -0.3264 -0.0846 68  HIS   Q CE1 
28974 N  NE2 . HIS   Q  70  ? 2.2269 0.4846 1.4302 0.2061  -0.3478 -0.0729 68  HIS   Q NE2 
28975 N  N   . VAL   Q  71  ? 2.1880 0.5838 1.5168 0.1455  -0.3769 -0.1330 69  VAL   Q N   
28976 C  CA  . VAL   Q  71  ? 2.1278 0.6034 1.5431 0.1610  -0.3865 -0.1271 69  VAL   Q CA  
28977 C  C   . VAL   Q  71  ? 2.1147 0.5849 1.5769 0.1718  -0.4121 -0.0933 69  VAL   Q C   
28978 O  O   . VAL   Q  71  ? 2.1296 0.4360 1.5790 0.1579  -0.4341 -0.1198 69  VAL   Q O   
28979 C  CB  . VAL   Q  71  ? 2.0935 0.5497 1.5421 0.1455  -0.3669 -0.1488 69  VAL   Q CB  
28980 C  CG1 . VAL   Q  71  ? 2.0895 0.5461 1.5242 0.1387  -0.3552 -0.1351 69  VAL   Q CG1 
28981 C  CG2 . VAL   Q  71  ? 2.1242 0.5330 1.5282 0.1351  -0.3692 -0.1576 69  VAL   Q CG2 
28982 N  N   . VAL   Q  72  ? 2.1180 0.5963 1.5351 0.1642  -0.4056 -0.1165 70  VAL   Q N   
28983 C  CA  . VAL   Q  72  ? 2.1008 0.6810 1.5168 0.1369  -0.3856 -0.1337 70  VAL   Q CA  
28984 C  C   . VAL   Q  72  ? 2.0888 0.6051 1.4704 0.1054  -0.3575 -0.1694 70  VAL   Q C   
28985 O  O   . VAL   Q  72  ? 2.0950 0.5815 1.4829 0.0827  -0.3218 -0.2455 70  VAL   Q O   
28986 C  CB  . VAL   Q  72  ? 2.1238 0.7450 1.5000 0.1537  -0.4055 -0.1132 70  VAL   Q CB  
28987 C  CG1 . VAL   Q  72  ? 2.1433 0.7654 1.5543 0.1797  -0.3979 -0.1086 70  VAL   Q CG1 
28988 C  CG2 . VAL   Q  72  ? 2.1351 0.7891 1.4934 0.1599  -0.3938 -0.0869 70  VAL   Q CG2 
28989 N  N   . LEU   Q  73  ? 2.0736 0.5884 1.4385 0.1028  -0.3816 -0.1713 71  LEU   Q N   
28990 C  CA  . LEU   Q  73  ? 2.0419 0.6253 1.4195 0.1072  -0.3913 -0.1590 71  LEU   Q CA  
28991 C  C   . LEU   Q  73  ? 2.0486 0.6092 1.3854 0.1116  -0.3862 -0.1546 71  LEU   Q C   
28992 O  O   . LEU   Q  73  ? 2.0291 0.6513 1.4173 0.1089  -0.4190 -0.1045 71  LEU   Q O   
28993 C  CB  . LEU   Q  73  ? 2.0211 0.5693 1.4171 0.1114  -0.4223 -0.1376 71  LEU   Q CB  
28994 C  CG  . LEU   Q  73  ? 2.0138 0.5478 1.4301 0.0775  -0.4243 -0.1220 71  LEU   Q CG  
28995 C  CD1 . LEU   Q  73  ? 2.0232 0.5285 1.4199 0.0722  -0.4216 -0.1120 71  LEU   Q CD1 
28996 C  CD2 . LEU   Q  73  ? 2.0112 0.5138 1.4385 0.0678  -0.4499 -0.1199 71  LEU   Q CD2 
28997 N  N   . SER   Q  74  ? 2.0541 0.6516 1.3207 0.1027  -0.3601 -0.1976 72  SER   Q N   
28998 C  CA  . SER   Q  74  ? 2.0802 0.6987 1.3681 0.0569  -0.3621 -0.2230 72  SER   Q CA  
28999 C  C   . SER   Q  74  ? 2.0735 0.6032 1.3253 0.0456  -0.3794 -0.3044 72  SER   Q C   
29000 O  O   . SER   Q  74  ? 2.1020 0.6729 1.2587 0.0152  -0.3755 -0.4600 72  SER   Q O   
29001 C  CB  . SER   Q  74  ? 2.1188 0.7900 1.3149 0.0464  -0.3872 -0.1781 72  SER   Q CB  
29002 O  OG  . SER   Q  74  ? 2.1268 0.8201 1.3501 0.0728  -0.3639 -0.0801 72  SER   Q OG  
29003 N  N   . PHE   Q  75  ? 2.1119 0.5487 1.3990 0.0673  -0.3852 -0.2841 73  PHE   Q N   
29004 C  CA  . PHE   Q  75  ? 2.0802 0.5951 1.4255 0.0872  -0.3701 -0.2484 73  PHE   Q CA  
29005 C  C   . PHE   Q  75  ? 2.0448 0.6043 1.4653 0.0834  -0.4127 -0.2229 73  PHE   Q C   
29006 O  O   . PHE   Q  75  ? 2.0537 0.5716 1.5646 0.0210  -0.4290 -0.2834 73  PHE   Q O   
29007 C  CB  . PHE   Q  75  ? 2.0446 0.4712 1.4404 0.0759  -0.3698 -0.2390 73  PHE   Q CB  
29008 C  CG  . PHE   Q  75  ? 2.0208 0.4455 1.5087 0.1325  -0.3972 -0.2143 73  PHE   Q CG  
29009 C  CD1 . PHE   Q  75  ? 2.0107 0.4347 1.5251 0.1072  -0.4040 -0.1696 73  PHE   Q CD1 
29010 C  CD2 . PHE   Q  75  ? 2.0048 0.4985 1.5614 0.0845  -0.3753 -0.2115 73  PHE   Q CD2 
29011 C  CE1 . PHE   Q  75  ? 1.9920 0.4563 1.5514 0.1245  -0.4425 -0.1455 73  PHE   Q CE1 
29012 C  CE2 . PHE   Q  75  ? 1.9783 0.4760 1.5906 0.1247  -0.4154 -0.2116 73  PHE   Q CE2 
29013 C  CZ  . PHE   Q  75  ? 1.9880 0.4441 1.5684 0.0980  -0.4237 -0.1802 73  PHE   Q CZ  
29014 N  N   . SER   Q  76  ? 2.0614 0.6643 1.4883 0.1271  -0.3897 -0.1914 74  SER   Q N   
29015 C  CA  . SER   Q  76  ? 2.1192 0.7075 1.5260 0.0757  -0.4045 -0.1532 74  SER   Q CA  
29016 C  C   . SER   Q  76  ? 2.0878 0.6412 1.5415 0.0818  -0.3340 -0.1314 74  SER   Q C   
29017 O  O   . SER   Q  76  ? 2.1444 0.5622 1.5557 0.0394  -0.3452 -0.1655 74  SER   Q O   
29018 C  CB  . SER   Q  76  ? 2.1540 0.8189 1.4430 0.1132  -0.4264 -0.1705 74  SER   Q CB  
29019 O  OG  . SER   Q  76  ? 2.1861 0.9881 1.4815 0.1101  -0.5160 -0.1229 74  SER   Q OG  
29020 N  N   . GLY   Q  77  ? 2.0833 0.5802 1.5939 0.1152  -0.3167 -0.0984 75  GLY   Q N   
29021 C  CA  . GLY   Q  77  ? 2.0191 0.5331 1.5867 0.1130  -0.3098 -0.1109 75  GLY   Q CA  
29022 C  C   . GLY   Q  77  ? 1.9951 0.4745 1.5775 0.1049  -0.3316 -0.1057 75  GLY   Q C   
29023 O  O   . GLY   Q  77  ? 2.0019 0.3571 1.5594 0.1327  -0.3331 -0.0539 75  GLY   Q O   
29024 N  N   . LEU   Q  78  ? 1.9582 0.5257 1.5913 0.0868  -0.3596 -0.1255 76  LEU   Q N   
29025 C  CA  . LEU   Q  78  ? 1.9124 0.6032 1.5851 0.0775  -0.3811 -0.1123 76  LEU   Q CA  
29026 C  C   . LEU   Q  78  ? 1.8766 0.6221 1.6096 0.0782  -0.4112 -0.0980 76  LEU   Q C   
29027 O  O   . LEU   Q  78  ? 1.8123 0.6247 1.5779 0.0975  -0.4244 -0.0494 76  LEU   Q O   
29028 C  CB  . LEU   Q  78  ? 1.8994 0.5969 1.5695 0.0827  -0.3634 -0.0969 76  LEU   Q CB  
29029 C  CG  . LEU   Q  78  ? 1.8987 0.6005 1.5445 0.0781  -0.3646 -0.0944 76  LEU   Q CG  
29030 C  CD1 . LEU   Q  78  ? 1.8900 0.6284 1.5347 0.0753  -0.3486 -0.0941 76  LEU   Q CD1 
29031 C  CD2 . LEU   Q  78  ? 1.8898 0.5968 1.5495 0.0828  -0.3924 -0.0877 76  LEU   Q CD2 
29032 N  N   . ASN   Q  79  ? 1.8959 0.6968 1.6406 0.0834  -0.4429 -0.1060 77  ASN   Q N   
29033 C  CA  . ASN   Q  79  ? 1.9002 0.7044 1.6721 0.0861  -0.4340 -0.0933 77  ASN   Q CA  
29034 C  C   . ASN   Q  79  ? 1.9109 0.7030 1.6164 0.0452  -0.3962 -0.0621 77  ASN   Q C   
29035 O  O   . ASN   Q  79  ? 1.9206 0.7109 1.6511 -0.0095 -0.3741 -0.1139 77  ASN   Q O   
29036 C  CB  . ASN   Q  79  ? 1.9067 0.7306 1.7639 0.0859  -0.4582 -0.1305 77  ASN   Q CB  
29037 C  CG  . ASN   Q  79  ? 1.9149 0.7654 1.7846 0.0650  -0.4975 -0.1527 77  ASN   Q CG  
29038 O  OD1 . ASN   Q  79  ? 1.9102 0.8423 1.9022 0.0643  -0.5377 -0.1362 77  ASN   Q OD1 
29039 N  ND2 . ASN   Q  79  ? 1.9096 0.8095 1.8120 0.0558  -0.4683 -0.1611 77  ASN   Q ND2 
29040 N  N   . ALA   Q  80  ? 1.9590 0.7457 1.6073 0.0606  -0.4063 -0.0327 78  ALA   Q N   
29041 C  CA  . ALA   Q  80  ? 1.9669 0.6693 1.6257 0.0432  -0.3851 -0.0210 78  ALA   Q CA  
29042 C  C   . ALA   Q  80  ? 1.9162 0.7142 1.5984 0.0743  -0.3605 -0.0062 78  ALA   Q C   
29043 O  O   . ALA   Q  80  ? 2.0294 0.7556 1.6384 0.0492  -0.3366 -0.0620 78  ALA   Q O   
29044 C  CB  . ALA   Q  80  ? 1.9667 0.7185 1.6113 0.0639  -0.3627 -0.0286 78  ALA   Q CB  
29045 N  N   . ASP   Q  81  ? 1.9165 0.6005 1.5737 0.0426  -0.3586 -0.0303 79  ASP   Q N   
29046 C  CA  . ASP   Q  81  ? 1.8992 0.6137 1.5571 0.0695  -0.3525 -0.0558 79  ASP   Q CA  
29047 C  C   . ASP   Q  81  ? 1.8784 0.6022 1.5385 0.0886  -0.3577 -0.0645 79  ASP   Q C   
29048 O  O   . ASP   Q  81  ? 1.8538 0.6286 1.5962 0.0606  -0.3647 -0.0446 79  ASP   Q O   
29049 C  CB  . ASP   Q  81  ? 1.9105 0.5999 1.5137 0.0605  -0.3483 -0.0589 79  ASP   Q CB  
29050 C  CG  . ASP   Q  81  ? 1.8953 0.5913 1.5030 0.0448  -0.3456 -0.0645 79  ASP   Q CG  
29051 O  OD1 . ASP   Q  81  ? 1.9026 0.5972 1.4614 0.0300  -0.3497 -0.0425 79  ASP   Q OD1 
29052 O  OD2 . ASP   Q  81  ? 1.9160 0.5302 1.4448 0.0283  -0.3523 -0.0369 79  ASP   Q OD2 
29053 N  N   . SER   Q  82  ? 1.8789 0.6119 1.5505 0.1002  -0.3529 -0.1161 80  SER   Q N   
29054 C  CA  . SER   Q  82  ? 1.8741 0.6229 1.5590 0.0734  -0.3307 -0.1302 80  SER   Q CA  
29055 C  C   . SER   Q  82  ? 1.8788 0.6203 1.5386 0.0723  -0.3387 -0.1198 80  SER   Q C   
29056 O  O   . SER   Q  82  ? 1.8673 0.6414 1.5024 0.0951  -0.3118 -0.0965 80  SER   Q O   
29057 C  CB  . SER   Q  82  ? 1.8991 0.6286 1.5805 0.0781  -0.3280 -0.1589 80  SER   Q CB  
29058 O  OG  . SER   Q  82  ? 1.9019 0.6742 1.6394 0.0857  -0.3275 -0.1830 80  SER   Q OG  
29059 N  N   . ARG   Q  83  ? 1.8666 0.6219 1.5396 0.0430  -0.3472 -0.1170 81  ARG   Q N   
29060 C  CA  . ARG   Q  83  ? 1.8455 0.6579 1.5390 0.0642  -0.3504 -0.1320 81  ARG   Q CA  
29061 C  C   . ARG   Q  83  ? 1.9067 0.6323 1.5131 0.0666  -0.3487 -0.1378 81  ARG   Q C   
29062 O  O   . ARG   Q  83  ? 1.9875 0.5968 1.6091 0.0125  -0.2972 -0.2183 81  ARG   Q O   
29063 C  CB  . ARG   Q  83  ? 1.8227 0.6982 1.5549 0.0491  -0.3715 -0.1041 81  ARG   Q CB  
29064 C  CG  . ARG   Q  83  ? 1.7920 0.7092 1.5604 0.0382  -0.3661 -0.0850 81  ARG   Q CG  
29065 C  CD  . ARG   Q  83  ? 1.7733 0.7580 1.5626 0.0140  -0.3602 -0.0706 81  ARG   Q CD  
29066 N  NE  . ARG   Q  83  ? 1.7200 0.7631 1.5652 0.0146  -0.3567 -0.0656 81  ARG   Q NE  
29067 C  CZ  . ARG   Q  83  ? 1.6806 0.7657 1.5559 0.0331  -0.3736 -0.0503 81  ARG   Q CZ  
29068 N  NH1 . ARG   Q  83  ? 1.6695 0.7943 1.5559 0.0325  -0.3861 -0.0660 81  ARG   Q NH1 
29069 N  NH2 . ARG   Q  83  ? 1.6741 0.7372 1.5601 0.0475  -0.3739 -0.0311 81  ARG   Q NH2 
29070 N  N   . ILE   Q  84  ? 1.9051 0.5821 1.4731 0.0694  -0.3554 -0.1838 82  ILE   Q N   
29071 C  CA  . ILE   Q  84  ? 1.8872 0.5204 1.4403 0.0744  -0.3421 -0.1611 82  ILE   Q CA  
29072 C  C   . ILE   Q  84  ? 1.8766 0.5637 1.3859 0.0639  -0.3662 -0.1602 82  ILE   Q C   
29073 O  O   . ILE   Q  84  ? 1.9076 0.5858 1.3963 -0.0005 -0.3914 -0.0961 82  ILE   Q O   
29074 C  CB  . ILE   Q  84  ? 1.8790 0.4549 1.4377 0.0972  -0.3283 -0.1869 82  ILE   Q CB  
29075 C  CG1 . ILE   Q  84  ? 1.8807 0.4200 1.4401 0.0960  -0.3252 -0.1710 82  ILE   Q CG1 
29076 C  CG2 . ILE   Q  84  ? 1.8566 0.4236 1.4365 0.1134  -0.3056 -0.1914 82  ILE   Q CG2 
29077 C  CD1 . ILE   Q  84  ? 1.8831 0.4167 1.4566 0.0936  -0.3301 -0.1555 82  ILE   Q CD1 
29078 N  N   . LEU   Q  85  ? 1.8496 0.5316 1.4028 0.0410  -0.3725 -0.1695 83  LEU   Q N   
29079 C  CA  . LEU   Q  85  ? 1.8531 0.5636 1.4417 0.0257  -0.3605 -0.1812 83  LEU   Q CA  
29080 C  C   . LEU   Q  85  ? 1.8870 0.5961 1.4563 0.0035  -0.3392 -0.1446 83  LEU   Q C   
29081 O  O   . LEU   Q  85  ? 1.8147 0.6881 1.4372 -0.0208 -0.3387 -0.1518 83  LEU   Q O   
29082 C  CB  . LEU   Q  85  ? 1.8832 0.5976 1.4720 0.0532  -0.3559 -0.1990 83  LEU   Q CB  
29083 C  CG  . LEU   Q  85  ? 1.8768 0.6299 1.4853 0.0676  -0.3590 -0.2029 83  LEU   Q CG  
29084 C  CD1 . LEU   Q  85  ? 1.9205 0.6871 1.5123 0.0924  -0.3355 -0.2229 83  LEU   Q CD1 
29085 C  CD2 . LEU   Q  85  ? 1.8822 0.5554 1.4595 0.0769  -0.3296 -0.2249 83  LEU   Q CD2 
29086 N  N   . ILE   Q  86  ? 1.8959 0.6348 1.4885 -0.0303 -0.3484 -0.0996 84  ILE   Q N   
29087 C  CA  . ILE   Q  86  ? 1.9786 0.6552 1.4966 -0.0401 -0.3134 -0.0558 84  ILE   Q CA  
29088 C  C   . ILE   Q  86  ? 1.9602 0.6816 1.4576 -0.0369 -0.2391 -0.0607 84  ILE   Q C   
29089 O  O   . ILE   Q  86  ? 2.0194 0.6008 1.5562 -0.0276 -0.2217 -0.1012 84  ILE   Q O   
29090 C  CB  . ILE   Q  86  ? 2.0155 0.7084 1.5252 -0.0606 -0.3542 -0.0288 84  ILE   Q CB  
29091 C  CG1 . ILE   Q  86  ? 2.0368 0.6916 1.5209 -0.0297 -0.3550 0.0027  84  ILE   Q CG1 
29092 C  CG2 . ILE   Q  86  ? 1.9962 0.7323 1.5295 -0.0194 -0.3723 -0.0595 84  ILE   Q CG2 
29093 C  CD1 . ILE   Q  86  ? 2.0151 0.7538 1.5589 -0.0365 -0.3727 0.0231  84  ILE   Q CD1 
29094 N  N   . GLU   Q  87  ? 1.9360 0.6225 1.4744 -0.0094 -0.2209 -0.0568 85  GLU   Q N   
29095 C  CA  . GLU   Q  87  ? 1.9124 0.6121 1.4776 0.0103  -0.1863 -0.0340 85  GLU   Q CA  
29096 C  C   . GLU   Q  87  ? 1.8892 0.6378 1.4350 0.0515  -0.2077 -0.0910 85  GLU   Q C   
29097 O  O   . GLU   Q  87  ? 1.9020 0.6524 1.4804 -0.0188 -0.2285 -0.0924 85  GLU   Q O   
29098 C  CB  . GLU   Q  87  ? 1.8953 0.6950 1.5076 0.0209  -0.1636 -0.0301 85  GLU   Q CB  
29099 C  CG  . GLU   Q  87  ? 1.8855 0.7600 1.4979 0.0451  -0.1145 -0.0346 85  GLU   Q CG  
29100 C  CD  . GLU   Q  87  ? 1.8774 0.8544 1.5686 0.0861  -0.1145 0.0030  85  GLU   Q CD  
29101 O  OE1 . GLU   Q  87  ? 1.8820 0.8974 1.5897 0.0918  -0.0835 -0.0895 85  GLU   Q OE1 
29102 O  OE2 . GLU   Q  87  ? 1.8127 1.0177 1.6618 0.0665  -0.1413 -0.0117 85  GLU   Q OE2 
29103 N  N   . LYS   Q  88  ? 1.8882 0.5177 1.4094 0.0490  -0.1918 -0.1274 86  LYS   Q N   
29104 C  CA  . LYS   Q  88  ? 1.8879 0.5458 1.4115 0.0503  -0.1942 -0.1407 86  LYS   Q CA  
29105 C  C   . LYS   Q  88  ? 1.9059 0.5999 1.4113 0.0483  -0.2137 -0.1014 86  LYS   Q C   
29106 O  O   . LYS   Q  88  ? 1.9018 0.7154 1.5238 -0.0494 -0.2070 -0.1125 86  LYS   Q O   
29107 C  CB  . LYS   Q  88  ? 1.8869 0.5512 1.3650 0.0672  -0.1765 -0.1640 86  LYS   Q CB  
29108 C  CG  . LYS   Q  88  ? 1.8956 0.5808 1.3642 0.0725  -0.1503 -0.1925 86  LYS   Q CG  
29109 C  CD  . LYS   Q  88  ? 1.8923 0.6171 1.3379 0.0938  -0.1286 -0.1956 86  LYS   Q CD  
29110 C  CE  . LYS   Q  88  ? 1.9096 0.6742 1.3422 0.0937  -0.1050 -0.2019 86  LYS   Q CE  
29111 N  NZ  . LYS   Q  88  ? 1.9381 0.7159 1.3469 0.1028  -0.0789 -0.2184 86  LYS   Q NZ  
29112 N  N   . ALA   Q  89  ? 1.8930 0.4964 1.4423 0.0045  -0.2816 -0.0923 87  ALA   Q N   
29113 C  CA  . ALA   Q  89  ? 1.8928 0.5005 1.4487 -0.0026 -0.2880 -0.0829 87  ALA   Q CA  
29114 C  C   . ALA   Q  89  ? 1.9185 0.5392 1.4812 0.0461  -0.3038 -0.0832 87  ALA   Q C   
29115 O  O   . ALA   Q  89  ? 1.9499 0.5245 1.4525 0.0864  -0.2993 -0.0125 87  ALA   Q O   
29116 C  CB  . ALA   Q  89  ? 1.8826 0.4623 1.4731 -0.0091 -0.3049 -0.0724 87  ALA   Q CB  
29117 N  N   . ARG   Q  90  ? 1.9157 0.4722 1.4942 0.0475  -0.3091 -0.0606 88  ARG   Q N   
29118 C  CA  . ARG   Q  90  ? 1.9458 0.4516 1.5032 0.0372  -0.3278 -0.0650 88  ARG   Q CA  
29119 C  C   . ARG   Q  90  ? 1.9600 0.3975 1.5088 0.1001  -0.2706 -0.0626 88  ARG   Q C   
29120 O  O   . ARG   Q  90  ? 1.9524 0.2687 1.5618 0.1064  -0.2172 -0.1694 88  ARG   Q O   
29121 C  CB  . ARG   Q  90  ? 1.9605 0.5097 1.5709 0.0056  -0.3753 0.0086  88  ARG   Q CB  
29122 C  CG  . ARG   Q  90  ? 1.9839 0.5052 1.6045 -0.0197 -0.4221 0.0202  88  ARG   Q CG  
29123 C  CD  . ARG   Q  90  ? 1.9907 0.4810 1.6776 -0.0360 -0.4674 0.0360  88  ARG   Q CD  
29124 N  NE  . ARG   Q  90  ? 1.9858 0.3809 1.7129 -0.0481 -0.4981 0.0465  88  ARG   Q NE  
29125 C  CZ  . ARG   Q  90  ? 1.9788 0.2678 1.7756 -0.0066 -0.5107 0.0467  88  ARG   Q CZ  
29126 N  NH1 . ARG   Q  90  ? 1.9550 0.2528 1.7938 -0.0099 -0.5153 0.0661  88  ARG   Q NH1 
29127 N  NH2 . ARG   Q  90  ? 1.9981 0.2354 1.7837 0.0501  -0.5027 0.0292  88  ARG   Q NH2 
29128 N  N   . VAL   Q  91  ? 1.9420 0.3100 1.4994 0.1439  -0.2570 -0.0741 89  VAL   Q N   
29129 C  CA  . VAL   Q  91  ? 1.9090 0.3068 1.4520 0.1314  -0.2718 -0.0467 89  VAL   Q CA  
29130 C  C   . VAL   Q  91  ? 1.8790 0.4195 1.4790 0.1479  -0.2867 -0.0978 89  VAL   Q C   
29131 O  O   . VAL   Q  91  ? 1.9612 0.4503 1.5509 0.0795  -0.2545 -0.1832 89  VAL   Q O   
29132 C  CB  . VAL   Q  91  ? 1.8714 0.2672 1.4335 0.1592  -0.2925 -0.0461 89  VAL   Q CB  
29133 C  CG1 . VAL   Q  91  ? 1.8503 0.2359 1.4032 0.1545  -0.2690 -0.0216 89  VAL   Q CG1 
29134 C  CG2 . VAL   Q  91  ? 1.8644 0.2960 1.4347 0.1869  -0.2866 -0.0347 89  VAL   Q CG2 
29135 N  N   . GLU   Q  92  ? 1.9227 0.2880 1.4742 0.1218  -0.3131 -0.0866 90  GLU   Q N   
29136 C  CA  . GLU   Q  92  ? 1.9258 0.3268 1.5098 0.1219  -0.3071 -0.0984 90  GLU   Q CA  
29137 C  C   . GLU   Q  92  ? 1.9535 0.3982 1.4993 0.1448  -0.3043 -0.0949 90  GLU   Q C   
29138 O  O   . GLU   Q  92  ? 1.8925 0.4568 1.4718 0.1496  -0.2803 -0.0988 90  GLU   Q O   
29139 C  CB  . GLU   Q  92  ? 1.9618 0.3130 1.5330 0.1203  -0.3123 -0.0781 90  GLU   Q CB  
29140 C  CG  . GLU   Q  92  ? 1.9765 0.3658 1.5456 0.1191  -0.2951 -0.0847 90  GLU   Q CG  
29141 C  CD  . GLU   Q  92  ? 2.0457 0.3862 1.5394 0.1273  -0.2994 -0.1045 90  GLU   Q CD  
29142 O  OE1 . GLU   Q  92  ? 2.0767 0.5171 1.5445 0.0947  -0.2715 -0.0460 90  GLU   Q OE1 
29143 O  OE2 . GLU   Q  92  ? 2.0741 0.3979 1.5223 0.1772  -0.3162 -0.1247 90  GLU   Q OE2 
29144 N  N   . ALA   Q  93  ? 1.9639 0.4282 1.5443 0.0996  -0.3233 -0.0831 91  ALA   Q N   
29145 C  CA  . ALA   Q  93  ? 2.0163 0.4849 1.5737 0.0634  -0.3431 -0.0415 91  ALA   Q CA  
29146 C  C   . ALA   Q  93  ? 2.0146 0.4629 1.6262 0.0131  -0.3303 -0.0267 91  ALA   Q C   
29147 O  O   . ALA   Q  93  ? 2.0528 0.3023 1.8496 -0.0358 -0.3832 0.0045  91  ALA   Q O   
29148 C  CB  . ALA   Q  93  ? 2.0713 0.4494 1.5853 0.0310  -0.3446 -0.0408 91  ALA   Q CB  
29149 N  N   . GLN   Q  94  ? 2.0272 0.5504 1.5620 0.0226  -0.3388 -0.0211 92  GLN   Q N   
29150 C  CA  . GLN   Q  94  ? 2.0324 0.5792 1.5311 0.0426  -0.3007 -0.0587 92  GLN   Q CA  
29151 C  C   . GLN   Q  94  ? 2.0358 0.6780 1.4434 0.0638  -0.3097 -0.0681 92  GLN   Q C   
29152 O  O   . GLN   Q  94  ? 2.0867 0.6835 1.4737 -0.0404 -0.3000 -0.1487 92  GLN   Q O   
29153 C  CB  . GLN   Q  94  ? 2.0547 0.6195 1.5242 0.0516  -0.2725 -0.0459 92  GLN   Q CB  
29154 C  CG  . GLN   Q  94  ? 2.0635 0.6727 1.5207 0.0519  -0.2867 -0.0206 92  GLN   Q CG  
29155 C  CD  . GLN   Q  94  ? 2.1531 0.7282 1.5412 0.0686  -0.3055 0.0193  92  GLN   Q CD  
29156 O  OE1 . GLN   Q  94  ? 2.2728 0.8140 1.5153 0.0365  -0.3216 0.0207  92  GLN   Q OE1 
29157 N  NE2 . GLN   Q  94  ? 2.1598 0.7251 1.4888 0.0761  -0.3245 0.0267  92  GLN   Q NE2 
29158 N  N   . SER   Q  95  ? 2.0106 0.6371 1.4164 0.0407  -0.2692 -0.0519 93  SER   Q N   
29159 C  CA  . SER   Q  95  ? 1.9879 0.6952 1.3959 0.0219  -0.2539 -0.0404 93  SER   Q CA  
29160 C  C   . SER   Q  95  ? 2.0074 0.7231 1.3838 0.0306  -0.2419 -0.0095 93  SER   Q C   
29161 O  O   . SER   Q  95  ? 1.9678 0.7538 1.4474 -0.0447 -0.2408 0.1172  93  SER   Q O   
29162 C  CB  . SER   Q  95  ? 1.9793 0.7061 1.3524 0.0131  -0.2345 -0.0553 93  SER   Q CB  
29163 O  OG  . SER   Q  95  ? 1.9775 0.8281 1.3002 0.0367  -0.2371 -0.0634 93  SER   Q OG  
29164 N  N   . HIS   Q  96  ? 1.9652 0.6485 1.4056 -0.0037 -0.2597 -0.0207 94  HIS   Q N   
29165 C  CA  . HIS   Q  96  ? 1.9365 0.6291 1.4493 0.0246  -0.2450 -0.0838 94  HIS   Q CA  
29166 C  C   . HIS   Q  96  ? 1.9582 0.6665 1.4711 0.0410  -0.2387 -0.0608 94  HIS   Q C   
29167 O  O   . HIS   Q  96  ? 1.9347 0.8937 1.5333 -0.0472 -0.1669 -0.0785 94  HIS   Q O   
29168 C  CB  . HIS   Q  96  ? 1.9273 0.5889 1.4990 0.0833  -0.2713 -0.0564 94  HIS   Q CB  
29169 C  CG  . HIS   Q  96  ? 1.8796 0.5712 1.5619 0.1112  -0.3078 -0.0577 94  HIS   Q CG  
29170 N  ND1 . HIS   Q  96  ? 1.9244 0.5629 1.5952 0.1279  -0.2908 -0.0397 94  HIS   Q ND1 
29171 C  CD2 . HIS   Q  96  ? 1.8889 0.5784 1.5515 0.1098  -0.3258 -0.0415 94  HIS   Q CD2 
29172 C  CE1 . HIS   Q  96  ? 1.9144 0.5769 1.5762 0.1526  -0.3113 -0.0371 94  HIS   Q CE1 
29173 N  NE2 . HIS   Q  96  ? 1.8597 0.6158 1.5568 0.1483  -0.3182 -0.0553 94  HIS   Q NE2 
29174 N  N   . ARG   Q  97  ? 1.9540 0.5475 1.4794 0.0637  -0.2414 -0.0672 95  ARG   Q N   
29175 C  CA  . ARG   Q  97  ? 1.9744 0.5429 1.4602 0.1019  -0.2576 -0.0858 95  ARG   Q CA  
29176 C  C   . ARG   Q  97  ? 2.0271 0.5161 1.4207 0.1052  -0.2597 -0.0571 95  ARG   Q C   
29177 O  O   . ARG   Q  97  ? 2.1202 0.3953 1.4626 0.0301  -0.2619 -0.1903 95  ARG   Q O   
29178 C  CB  . ARG   Q  97  ? 1.9642 0.5615 1.4746 0.1464  -0.2685 -0.0457 95  ARG   Q CB  
29179 C  CG  . ARG   Q  97  ? 1.9796 0.6213 1.4657 0.1805  -0.2655 -0.0735 95  ARG   Q CG  
29180 C  CD  . ARG   Q  97  ? 1.9619 0.7188 1.5014 0.2129  -0.2656 -0.0604 95  ARG   Q CD  
29181 N  NE  . ARG   Q  97  ? 2.0115 0.7851 1.4616 0.1960  -0.2647 -0.0519 95  ARG   Q NE  
29182 C  CZ  . ARG   Q  97  ? 2.0586 0.8561 1.4746 0.1856  -0.2361 -0.0890 95  ARG   Q CZ  
29183 N  NH1 . ARG   Q  97  ? 2.0097 0.8461 1.4410 0.2304  -0.2845 -0.0266 95  ARG   Q NH1 
29184 N  NH2 . ARG   Q  97  ? 2.1402 0.8628 1.5043 0.1652  -0.2237 -0.0632 95  ARG   Q NH2 
29185 N  N   . LEU   Q  98  ? 2.0274 0.4079 1.4073 0.0996  -0.2699 -0.0573 96  LEU   Q N   
29186 C  CA  . LEU   Q  98  ? 2.0090 0.3906 1.3818 0.0746  -0.2581 -0.0400 96  LEU   Q CA  
29187 C  C   . LEU   Q  98  ? 1.9903 0.5155 1.4263 0.0969  -0.2963 -0.0496 96  LEU   Q C   
29188 O  O   . LEU   Q  98  ? 2.0491 0.5443 1.5346 0.0099  -0.3117 -0.1434 96  LEU   Q O   
29189 C  CB  . LEU   Q  98  ? 2.0106 0.3559 1.3187 0.0953  -0.2700 -0.0756 96  LEU   Q CB  
29190 C  CG  . LEU   Q  98  ? 2.0087 0.3868 1.2096 0.0739  -0.2748 -0.0846 96  LEU   Q CG  
29191 C  CD1 . LEU   Q  98  ? 2.0105 0.4379 1.2375 0.0982  -0.2945 -0.1046 96  LEU   Q CD1 
29192 C  CD2 . LEU   Q  98  ? 1.9758 0.3676 1.1799 0.0872  -0.2758 -0.1186 96  LEU   Q CD2 
29193 N  N   . THR   Q  99  ? 1.9731 0.4203 1.4164 0.0638  -0.3045 -0.0935 97  THR   Q N   
29194 C  CA  . THR   Q  99  ? 1.9898 0.4411 1.3714 0.0597  -0.3082 -0.1373 97  THR   Q CA  
29195 C  C   . THR   Q  99  ? 1.9753 0.4770 1.4206 0.0592  -0.2964 -0.0980 97  THR   Q C   
29196 O  O   . THR   Q  99  ? 1.9289 0.5279 1.4579 0.0527  -0.3468 -0.1663 97  THR   Q O   
29197 C  CB  . THR   Q  99  ? 1.9738 0.4570 1.2796 0.0323  -0.3173 -0.1840 97  THR   Q CB  
29198 O  OG1 . THR   Q  99  ? 2.0363 0.4281 1.3586 -0.0178 -0.3654 -0.1596 97  THR   Q OG1 
29199 C  CG2 . THR   Q  99  ? 1.9502 0.4603 1.3137 0.0531  -0.2975 -0.1917 97  THR   Q CG2 
29200 N  N   . LEU   Q  100 ? 1.9759 0.5092 1.4347 0.0470  -0.2548 -0.1181 98  LEU   Q N   
29201 C  CA  . LEU   Q  100 ? 1.9687 0.6382 1.4352 0.0438  -0.2574 -0.0590 98  LEU   Q CA  
29202 C  C   . LEU   Q  100 ? 1.9423 0.5178 1.4170 0.0710  -0.2222 -0.0941 98  LEU   Q C   
29203 O  O   . LEU   Q  100 ? 1.9904 0.5098 1.3713 0.0419  -0.2483 -0.0430 98  LEU   Q O   
29204 C  CB  . LEU   Q  100 ? 1.9429 0.6797 1.5112 0.1004  -0.2405 -0.0548 98  LEU   Q CB  
29205 C  CG  . LEU   Q  100 ? 1.9198 0.8641 1.5017 0.0725  -0.2538 0.0257  98  LEU   Q CG  
29206 C  CD1 . LEU   Q  100 ? 1.9545 0.8991 1.4814 0.0462  -0.2663 -0.0004 98  LEU   Q CD1 
29207 C  CD2 . LEU   Q  100 ? 1.8885 0.8921 1.4814 0.1096  -0.2578 0.0254  98  LEU   Q CD2 
29208 N  N   . GLU   Q  101 ? 1.9633 0.4941 1.3889 0.1171  -0.2399 -0.0789 99  GLU   Q N   
29209 C  CA  . GLU   Q  101 ? 1.9878 0.5333 1.4295 0.1253  -0.2448 -0.0363 99  GLU   Q CA  
29210 C  C   . GLU   Q  101 ? 2.0518 0.5548 1.4280 0.1415  -0.2498 -0.0391 99  GLU   Q C   
29211 O  O   . GLU   Q  101 ? 2.0627 0.2731 1.5253 0.1910  -0.2882 -0.0055 99  GLU   Q O   
29212 C  CB  . GLU   Q  101 ? 1.9554 0.5488 1.4466 0.1095  -0.2496 -0.0350 99  GLU   Q CB  
29213 C  CG  . GLU   Q  101 ? 1.9081 0.5705 1.4601 0.1317  -0.2370 -0.0294 99  GLU   Q CG  
29214 C  CD  . GLU   Q  101 ? 1.8948 0.5614 1.4982 0.1571  -0.2342 -0.0514 99  GLU   Q CD  
29215 O  OE1 . GLU   Q  101 ? 1.8937 0.5272 1.4716 0.1113  -0.2621 -0.0884 99  GLU   Q OE1 
29216 O  OE2 . GLU   Q  101 ? 1.9016 0.5707 1.5625 0.1610  -0.2415 0.0463  99  GLU   Q OE2 
29217 N  N   . ASP   Q  102 ? 2.1152 0.5706 1.4070 0.1020  -0.2741 -0.0134 100 ASP   Q N   
29218 C  CA  . ASP   Q  102 ? 2.1862 0.6950 1.3663 0.1015  -0.2835 -0.0303 100 ASP   Q CA  
29219 C  C   . ASP   Q  102 ? 2.2054 0.6533 1.2905 0.1344  -0.3501 -0.0032 100 ASP   Q C   
29220 O  O   . ASP   Q  102 ? 2.1866 0.5379 1.2840 0.0947  -0.3729 -0.0286 100 ASP   Q O   
29221 C  CB  . ASP   Q  102 ? 2.2042 0.8226 1.3903 0.1229  -0.2519 -0.0184 100 ASP   Q CB  
29222 C  CG  . ASP   Q  102 ? 2.2597 0.9206 1.4075 0.1308  -0.1986 -0.0006 100 ASP   Q CG  
29223 O  OD1 . ASP   Q  102 ? 2.3130 1.0151 1.4049 0.1263  -0.2104 0.0764  100 ASP   Q OD1 
29224 O  OD2 . ASP   Q  102 ? 2.2724 1.0289 1.4646 0.1726  -0.1811 0.0300  100 ASP   Q OD2 
29225 N  N   . PRO   Q  103 ? 2.2227 0.6715 1.3696 0.1283  -0.3780 -0.0344 101 PRO   Q N   
29226 C  CA  . PRO   Q  103 ? 2.2131 0.6738 1.3689 0.1342  -0.3882 -0.0374 101 PRO   Q CA  
29227 C  C   . PRO   Q  103 ? 2.2368 0.6188 1.2218 0.1165  -0.4280 -0.0547 101 PRO   Q C   
29228 O  O   . PRO   Q  103 ? 2.2011 0.5661 1.2102 0.1311  -0.4634 -0.0713 101 PRO   Q O   
29229 C  CB  . PRO   Q  103 ? 2.2041 0.7068 1.4260 0.1409  -0.4293 -0.0209 101 PRO   Q CB  
29230 C  CG  . PRO   Q  103 ? 2.2147 0.7301 1.4602 0.1413  -0.4241 0.0169  101 PRO   Q CG  
29231 C  CD  . PRO   Q  103 ? 2.2281 0.7005 1.4165 0.1436  -0.4100 -0.0066 101 PRO   Q CD  
29232 N  N   . VAL   Q  104 ? 2.2521 0.6324 1.1287 0.0885  -0.4293 -0.0801 102 VAL   Q N   
29233 C  CA  . VAL   Q  104 ? 2.2069 0.6947 1.1313 0.0923  -0.4108 -0.0375 102 VAL   Q CA  
29234 C  C   . VAL   Q  104 ? 2.1710 0.7692 1.1709 0.0852  -0.3714 -0.0484 102 VAL   Q C   
29235 O  O   . VAL   Q  104 ? 2.1784 0.7558 1.2127 0.0447  -0.3960 -0.1090 102 VAL   Q O   
29236 C  CB  . VAL   Q  104 ? 2.2157 0.7138 1.1176 0.0997  -0.4121 -0.0278 102 VAL   Q CB  
29237 C  CG1 . VAL   Q  104 ? 2.2309 0.6297 1.1918 0.0901  -0.4008 -0.1139 102 VAL   Q CG1 
29238 C  CG2 . VAL   Q  104 ? 2.2350 0.7478 1.0827 0.1097  -0.4579 -0.0050 102 VAL   Q CG2 
29239 N  N   . THR   Q  105 ? 2.1376 0.8294 1.1673 0.0599  -0.3909 -0.0150 103 THR   Q N   
29240 C  CA  . THR   Q  105 ? 2.0789 0.8602 1.1566 0.0399  -0.3925 -0.0282 103 THR   Q CA  
29241 C  C   . THR   Q  105 ? 2.0759 0.8535 1.1490 0.0420  -0.3749 -0.0346 103 THR   Q C   
29242 O  O   . THR   Q  105 ? 2.0364 0.8282 1.1686 0.0033  -0.3655 -0.0135 103 THR   Q O   
29243 C  CB  . THR   Q  105 ? 2.0721 0.9022 1.0939 0.0174  -0.4084 -0.0097 103 THR   Q CB  
29244 O  OG1 . THR   Q  105 ? 2.0343 1.0166 1.0587 -0.0021 -0.4198 -0.0511 103 THR   Q OG1 
29245 C  CG2 . THR   Q  105 ? 2.0545 0.9058 1.0931 0.0136  -0.4027 -0.0048 103 THR   Q CG2 
29246 N  N   . VAL   Q  106 ? 2.0840 0.7936 1.2345 0.0296  -0.3619 -0.0595 104 VAL   Q N   
29247 C  CA  . VAL   Q  106 ? 2.0567 0.7675 1.3252 0.0468  -0.3426 -0.1132 104 VAL   Q CA  
29248 C  C   . VAL   Q  106 ? 1.9939 0.6806 1.3152 0.0800  -0.3158 -0.1936 104 VAL   Q C   
29249 O  O   . VAL   Q  106 ? 1.9584 0.6249 1.3602 0.1202  -0.2770 -0.1949 104 VAL   Q O   
29250 C  CB  . VAL   Q  106 ? 2.0739 0.8337 1.3329 0.0326  -0.3756 -0.1134 104 VAL   Q CB  
29251 C  CG1 . VAL   Q  106 ? 2.0711 0.8470 1.3808 0.0231  -0.3672 -0.1197 104 VAL   Q CG1 
29252 C  CG2 . VAL   Q  106 ? 2.0864 0.8760 1.3918 0.0141  -0.3927 -0.0609 104 VAL   Q CG2 
29253 N  N   . GLU   Q  107 ? 1.9926 0.6844 1.3380 0.0890  -0.2949 -0.2847 105 GLU   Q N   
29254 C  CA  . GLU   Q  107 ? 1.9682 0.7486 1.3186 0.0872  -0.2880 -0.2975 105 GLU   Q CA  
29255 C  C   . GLU   Q  107 ? 1.9477 0.7109 1.3008 0.1071  -0.2790 -0.2568 105 GLU   Q C   
29256 O  O   . GLU   Q  107 ? 1.9239 0.7024 1.2498 0.0769  -0.2445 -0.2898 105 GLU   Q O   
29257 C  CB  . GLU   Q  107 ? 1.9937 0.8385 1.3638 0.0549  -0.2445 -0.3479 105 GLU   Q CB  
29258 C  CG  . GLU   Q  107 ? 1.9643 0.8959 1.4222 0.0631  -0.2281 -0.3365 105 GLU   Q CG  
29259 C  CD  . GLU   Q  107 ? 1.9645 0.8934 1.4602 0.0592  -0.2067 -0.3872 105 GLU   Q CD  
29260 O  OE1 . GLU   Q  107 ? 1.8869 0.9102 1.5858 0.1145  -0.1899 -0.3350 105 GLU   Q OE1 
29261 O  OE2 . GLU   Q  107 ? 1.9989 0.9056 1.5214 0.0241  -0.1808 -0.4475 105 GLU   Q OE2 
29262 N  N   . TYR   Q  108 ? 1.9566 0.6972 1.2924 0.1312  -0.2735 -0.1895 106 TYR   Q N   
29263 C  CA  . TYR   Q  108 ? 1.9259 0.7135 1.2633 0.1039  -0.2562 -0.1556 106 TYR   Q CA  
29264 C  C   . TYR   Q  108 ? 1.9618 0.5963 1.2726 0.0860  -0.2707 -0.0976 106 TYR   Q C   
29265 O  O   . TYR   Q  108 ? 1.9483 0.5610 1.2785 0.0429  -0.2362 -0.0897 106 TYR   Q O   
29266 C  CB  . TYR   Q  108 ? 1.9147 0.7235 1.2579 0.1290  -0.2651 -0.1885 106 TYR   Q CB  
29267 C  CG  . TYR   Q  108 ? 1.8676 0.7865 1.2672 0.1519  -0.2739 -0.2139 106 TYR   Q CG  
29268 C  CD1 . TYR   Q  108 ? 1.8510 0.7743 1.2738 0.1560  -0.2954 -0.2275 106 TYR   Q CD1 
29269 C  CD2 . TYR   Q  108 ? 1.8565 0.7691 1.2603 0.1742  -0.2668 -0.2295 106 TYR   Q CD2 
29270 C  CE1 . TYR   Q  108 ? 1.8237 0.6989 1.2949 0.1618  -0.2823 -0.2269 106 TYR   Q CE1 
29271 C  CE2 . TYR   Q  108 ? 1.8260 0.7034 1.2646 0.1964  -0.2808 -0.2220 106 TYR   Q CE2 
29272 C  CZ  . TYR   Q  108 ? 1.8218 0.6670 1.2670 0.1871  -0.2812 -0.2259 106 TYR   Q CZ  
29273 O  OH  . TYR   Q  108 ? 1.7668 0.6651 1.2179 0.1920  -0.2907 -0.1721 106 TYR   Q OH  
29274 N  N   . LEU   Q  109 ? 1.9912 0.5506 1.2662 0.0699  -0.2926 -0.0556 107 LEU   Q N   
29275 C  CA  . LEU   Q  109 ? 1.9858 0.5995 1.2931 0.0736  -0.2857 -0.0723 107 LEU   Q CA  
29276 C  C   . LEU   Q  109 ? 1.9972 0.5934 1.3008 0.1044  -0.3019 -0.1063 107 LEU   Q C   
29277 O  O   . LEU   Q  109 ? 2.0220 0.6348 1.2810 0.0696  -0.2847 -0.1498 107 LEU   Q O   
29278 C  CB  . LEU   Q  109 ? 2.0137 0.5737 1.3208 0.0854  -0.2998 -0.0440 107 LEU   Q CB  
29279 C  CG  . LEU   Q  109 ? 2.0214 0.5673 1.3602 0.0922  -0.2811 -0.0476 107 LEU   Q CG  
29280 C  CD1 . LEU   Q  109 ? 2.0210 0.5885 1.4330 0.0589  -0.2938 -0.0726 107 LEU   Q CD1 
29281 C  CD2 . LEU   Q  109 ? 2.0125 0.5594 1.3442 0.0941  -0.2715 -0.0265 107 LEU   Q CD2 
29282 N  N   . THR   Q  110 ? 1.9996 0.5692 1.3511 0.1332  -0.3181 -0.1172 108 THR   Q N   
29283 C  CA  . THR   Q  110 ? 1.9688 0.5822 1.3566 0.1225  -0.3072 -0.0559 108 THR   Q CA  
29284 C  C   . THR   Q  110 ? 1.9307 0.4964 1.3533 0.1092  -0.2976 -0.0671 108 THR   Q C   
29285 O  O   . THR   Q  110 ? 1.9194 0.6103 1.3467 0.0715  -0.2407 -0.0647 108 THR   Q O   
29286 C  CB  . THR   Q  110 ? 1.9881 0.5757 1.3888 0.1559  -0.2809 -0.0389 108 THR   Q CB  
29287 O  OG1 . THR   Q  110 ? 1.9773 0.5192 1.4525 0.1482  -0.3129 -0.0423 108 THR   Q OG1 
29288 C  CG2 . THR   Q  110 ? 1.9826 0.5895 1.3782 0.1801  -0.2860 -0.0446 108 THR   Q CG2 
29289 N  N   . ARG   Q  111 ? 1.9349 0.4482 1.2876 0.1204  -0.2970 -0.0555 109 ARG   Q N   
29290 C  CA  . ARG   Q  111 ? 1.9216 0.4323 1.2355 0.1193  -0.2643 -0.0708 109 ARG   Q CA  
29291 C  C   . ARG   Q  111 ? 1.8957 0.2849 1.1912 0.1084  -0.2927 -0.0537 109 ARG   Q C   
29292 O  O   . ARG   Q  111 ? 1.8468 0.1733 1.2092 0.1036  -0.2597 -0.0742 109 ARG   Q O   
29293 C  CB  . ARG   Q  111 ? 1.9003 0.5093 1.2379 0.0972  -0.2781 -0.0793 109 ARG   Q CB  
29294 C  CG  . ARG   Q  111 ? 1.8759 0.5883 1.2365 0.1071  -0.2731 -0.0733 109 ARG   Q CG  
29295 C  CD  . ARG   Q  111 ? 1.8709 0.6871 1.2650 0.1119  -0.2580 -0.0517 109 ARG   Q CD  
29296 N  NE  . ARG   Q  111 ? 1.8897 0.7778 1.2409 0.1008  -0.2780 -0.0283 109 ARG   Q NE  
29297 C  CZ  . ARG   Q  111 ? 1.8909 0.7830 1.2161 0.1004  -0.2643 -0.0488 109 ARG   Q CZ  
29298 N  NH1 . ARG   Q  111 ? 1.9067 0.8164 1.2500 0.1074  -0.2524 -0.0118 109 ARG   Q NH1 
29299 N  NH2 . ARG   Q  111 ? 1.8749 0.8113 1.2433 0.1095  -0.2739 -0.0907 109 ARG   Q NH2 
29300 N  N   . TYR   Q  112 ? 1.8776 0.3452 1.1618 0.1253  -0.2861 -0.0767 110 TYR   Q N   
29301 C  CA  . TYR   Q  112 ? 1.8794 0.4297 1.1516 0.1155  -0.2817 -0.0766 110 TYR   Q CA  
29302 C  C   . TYR   Q  112 ? 1.8683 0.3842 1.1621 0.1481  -0.2943 -0.0719 110 TYR   Q C   
29303 O  O   . TYR   Q  112 ? 1.8866 0.4234 1.1422 0.1440  -0.2569 -0.1004 110 TYR   Q O   
29304 C  CB  . TYR   Q  112 ? 1.8737 0.4650 1.1471 0.1379  -0.2736 -0.0917 110 TYR   Q CB  
29305 C  CG  . TYR   Q  112 ? 1.9166 0.5201 1.1214 0.0914  -0.2573 -0.0960 110 TYR   Q CG  
29306 C  CD1 . TYR   Q  112 ? 1.9112 0.5208 1.0999 0.0829  -0.2230 -0.0971 110 TYR   Q CD1 
29307 C  CD2 . TYR   Q  112 ? 1.9258 0.5396 1.1190 0.0723  -0.2456 -0.0956 110 TYR   Q CD2 
29308 C  CE1 . TYR   Q  112 ? 1.9235 0.5205 1.0962 0.0769  -0.2208 -0.1150 110 TYR   Q CE1 
29309 C  CE2 . TYR   Q  112 ? 1.9267 0.5031 1.1063 0.0654  -0.2496 -0.1010 110 TYR   Q CE2 
29310 C  CZ  . TYR   Q  112 ? 1.9328 0.4846 1.1085 0.0669  -0.2291 -0.1178 110 TYR   Q CZ  
29311 O  OH  . TYR   Q  112 ? 1.9367 0.4397 1.0895 0.0281  -0.2356 -0.1361 110 TYR   Q OH  
29312 N  N   . VAL   Q  113 ? 1.8741 0.4683 1.1911 0.1801  -0.3410 -0.0819 111 VAL   Q N   
29313 C  CA  . VAL   Q  113 ? 1.8776 0.5027 1.2224 0.1684  -0.3287 -0.0773 111 VAL   Q CA  
29314 C  C   . VAL   Q  113 ? 1.8718 0.4436 1.2376 0.1449  -0.2925 -0.0833 111 VAL   Q C   
29315 O  O   . VAL   Q  113 ? 1.8710 0.3424 1.2993 0.1313  -0.3026 -0.0722 111 VAL   Q O   
29316 C  CB  . VAL   Q  113 ? 1.9376 0.5773 1.2394 0.1654  -0.3499 -0.1111 111 VAL   Q CB  
29317 C  CG1 . VAL   Q  113 ? 1.9557 0.5486 1.2296 0.1738  -0.3736 -0.0931 111 VAL   Q CG1 
29318 C  CG2 . VAL   Q  113 ? 1.9321 0.6570 1.2439 0.2003  -0.3809 -0.1253 111 VAL   Q CG2 
29319 N  N   . ALA   Q  114 ? 1.8920 0.4176 1.2263 0.1636  -0.2807 -0.0933 112 ALA   Q N   
29320 C  CA  . ALA   Q  114 ? 1.8948 0.4037 1.2325 0.1843  -0.2421 -0.1167 112 ALA   Q CA  
29321 C  C   . ALA   Q  114 ? 1.9021 0.4723 1.2362 0.1650  -0.2326 -0.1425 112 ALA   Q C   
29322 O  O   . ALA   Q  114 ? 1.9164 0.4043 1.1926 0.2031  -0.2296 -0.2075 112 ALA   Q O   
29323 C  CB  . ALA   Q  114 ? 1.9098 0.4044 1.2220 0.2016  -0.2360 -0.1047 112 ALA   Q CB  
29324 N  N   . GLY   Q  115 ? 1.8691 0.5161 1.2266 0.1232  -0.2485 -0.1616 113 GLY   Q N   
29325 C  CA  . GLY   Q  115 ? 1.8329 0.5970 1.1996 0.1438  -0.2449 -0.1375 113 GLY   Q CA  
29326 C  C   . GLY   Q  115 ? 1.7859 0.5670 1.2281 0.1475  -0.2618 -0.1151 113 GLY   Q C   
29327 O  O   . GLY   Q  115 ? 1.7882 0.4365 1.2687 0.1230  -0.2595 -0.0949 113 GLY   Q O   
29328 N  N   . VAL   Q  116 ? 1.7827 0.6109 1.2544 0.1605  -0.2511 -0.0832 114 VAL   Q N   
29329 C  CA  . VAL   Q  116 ? 1.7801 0.6468 1.2739 0.1545  -0.2490 -0.0655 114 VAL   Q CA  
29330 C  C   . VAL   Q  116 ? 1.7733 0.6379 1.2507 0.1597  -0.2472 -0.1013 114 VAL   Q C   
29331 O  O   . VAL   Q  116 ? 1.7638 0.7674 1.2198 0.1958  -0.2654 -0.1188 114 VAL   Q O   
29332 C  CB  . VAL   Q  116 ? 1.7754 0.7021 1.3089 0.1481  -0.2550 -0.0417 114 VAL   Q CB  
29333 C  CG1 . VAL   Q  116 ? 1.7889 0.6403 1.2968 0.1453  -0.2656 -0.0056 114 VAL   Q CG1 
29334 C  CG2 . VAL   Q  116 ? 1.7996 0.7088 1.3681 0.1594  -0.2438 -0.0522 114 VAL   Q CG2 
29335 N  N   . GLN   Q  117 ? 1.7969 0.6263 1.3002 0.1618  -0.2325 -0.1284 115 GLN   Q N   
29336 C  CA  . GLN   Q  117 ? 1.8220 0.6197 1.3400 0.1798  -0.2240 -0.1119 115 GLN   Q CA  
29337 C  C   . GLN   Q  117 ? 1.8208 0.5123 1.3311 0.1766  -0.2047 -0.1056 115 GLN   Q C   
29338 O  O   . GLN   Q  117 ? 1.8691 0.6627 1.3504 0.2191  -0.1600 -0.0279 115 GLN   Q O   
29339 C  CB  . GLN   Q  117 ? 1.8671 0.6072 1.3758 0.1623  -0.2159 -0.1499 115 GLN   Q CB  
29340 C  CG  . GLN   Q  117 ? 1.8821 0.6037 1.4286 0.1503  -0.2419 -0.1795 115 GLN   Q CG  
29341 C  CD  . GLN   Q  117 ? 1.9606 0.6189 1.4556 0.1373  -0.2427 -0.2083 115 GLN   Q CD  
29342 O  OE1 . GLN   Q  117 ? 1.9424 0.5781 1.4786 0.1027  -0.2320 -0.2418 115 GLN   Q OE1 
29343 N  NE2 . GLN   Q  117 ? 2.0312 0.6167 1.5327 0.1133  -0.2604 -0.1568 115 GLN   Q NE2 
29344 N  N   . GLN   Q  118 ? 1.8226 0.3648 1.2769 0.1840  -0.2134 -0.1262 116 GLN   Q N   
29345 C  CA  . GLN   Q  118 ? 1.8219 0.3325 1.2941 0.1994  -0.2116 -0.1277 116 GLN   Q CA  
29346 C  C   . GLN   Q  118 ? 1.7748 0.3565 1.2770 0.1795  -0.2288 -0.0840 116 GLN   Q C   
29347 O  O   . GLN   Q  118 ? 1.7180 0.1515 1.3604 0.2032  -0.2235 -0.1533 116 GLN   Q O   
29348 C  CB  . GLN   Q  118 ? 1.8479 0.3454 1.2431 0.2025  -0.1825 -0.1525 116 GLN   Q CB  
29349 C  CG  . GLN   Q  118 ? 1.8888 0.3342 1.2342 0.2233  -0.1896 -0.1342 116 GLN   Q CG  
29350 C  CD  . GLN   Q  118 ? 1.9331 0.3546 1.2407 0.2084  -0.1829 -0.1439 116 GLN   Q CD  
29351 O  OE1 . GLN   Q  118 ? 1.9840 0.3330 1.2120 0.1752  -0.1958 -0.1597 116 GLN   Q OE1 
29352 N  NE2 . GLN   Q  118 ? 1.9681 0.3544 1.2500 0.2112  -0.1854 -0.1419 116 GLN   Q NE2 
29353 N  N   . ARG   Q  119 ? 1.7402 0.4155 1.3278 0.2237  -0.2187 -0.0937 117 ARG   Q N   
29354 C  CA  . ARG   Q  119 ? 1.7514 0.5069 1.2869 0.1838  -0.2546 -0.0701 117 ARG   Q CA  
29355 C  C   . ARG   Q  119 ? 1.7279 0.5228 1.2788 0.1646  -0.2694 -0.0814 117 ARG   Q C   
29356 O  O   . ARG   Q  119 ? 1.6843 0.5326 1.2891 0.1563  -0.2650 -0.0538 117 ARG   Q O   
29357 C  CB  . ARG   Q  119 ? 1.8104 0.4995 1.3584 0.1918  -0.2599 -0.0170 117 ARG   Q CB  
29358 C  CG  . ARG   Q  119 ? 1.8767 0.5350 1.3450 0.2122  -0.2856 -0.0010 117 ARG   Q CG  
29359 C  CD  . ARG   Q  119 ? 1.9418 0.5531 1.4347 0.2426  -0.2769 -0.0037 117 ARG   Q CD  
29360 N  NE  . ARG   Q  119 ? 1.9802 0.5519 1.4577 0.2582  -0.3231 0.0173  117 ARG   Q NE  
29361 C  CZ  . ARG   Q  119 ? 1.9874 0.5813 1.4815 0.2395  -0.3581 0.0124  117 ARG   Q CZ  
29362 N  NH1 . ARG   Q  119 ? 1.9579 0.5551 1.4346 0.2504  -0.3860 0.0097  117 ARG   Q NH1 
29363 N  NH2 . ARG   Q  119 ? 1.9932 0.5953 1.4787 0.2007  -0.3963 0.0150  117 ARG   Q NH2 
29364 N  N   . TYR   Q  120 ? 1.7733 0.4599 1.3358 0.1297  -0.2542 -0.1215 118 TYR   Q N   
29365 C  CA  . TYR   Q  120 ? 1.7807 0.5488 1.3853 0.0660  -0.2481 -0.1501 118 TYR   Q CA  
29366 C  C   . TYR   Q  120 ? 1.7741 0.6464 1.4378 0.1494  -0.2721 -0.1430 118 TYR   Q C   
29367 O  O   . TYR   Q  120 ? 1.7925 0.7037 1.5440 0.1142  -0.2139 -0.1534 118 TYR   Q O   
29368 C  CB  . TYR   Q  120 ? 1.7722 0.5342 1.4240 0.0815  -0.2517 -0.1699 118 TYR   Q CB  
29369 C  CG  . TYR   Q  120 ? 1.7552 0.4907 1.4280 0.0439  -0.2442 -0.1959 118 TYR   Q CG  
29370 C  CD1 . TYR   Q  120 ? 1.7405 0.4934 1.4077 0.0480  -0.2391 -0.1955 118 TYR   Q CD1 
29371 C  CD2 . TYR   Q  120 ? 1.7600 0.4961 1.4326 0.0442  -0.2335 -0.2002 118 TYR   Q CD2 
29372 C  CE1 . TYR   Q  120 ? 1.7393 0.5530 1.4066 0.0752  -0.2196 -0.2026 118 TYR   Q CE1 
29373 C  CE2 . TYR   Q  120 ? 1.7542 0.4932 1.3990 0.0358  -0.2320 -0.2189 118 TYR   Q CE2 
29374 C  CZ  . TYR   Q  120 ? 1.7471 0.4890 1.4092 0.0573  -0.2171 -0.2114 118 TYR   Q CZ  
29375 O  OH  . TYR   Q  120 ? 1.7044 0.6481 1.4775 0.1146  -0.1665 -0.2061 118 TYR   Q OH  
29376 N  N   . THR   Q  121 ? 1.7609 0.6650 1.4120 0.1079  -0.2772 -0.1209 119 THR   Q N   
29377 C  CA  . THR   Q  121 ? 1.8465 0.5551 1.3974 0.0420  -0.2951 -0.1183 119 THR   Q CA  
29378 C  C   . THR   Q  121 ? 1.8779 0.5511 1.4748 0.0575  -0.3588 -0.0908 119 THR   Q C   
29379 O  O   . THR   Q  121 ? 1.9389 0.4279 1.5763 -0.0794 -0.4609 -0.1199 119 THR   Q O   
29380 C  CB  . THR   Q  121 ? 1.8748 0.4792 1.3603 -0.0040 -0.2901 -0.1193 119 THR   Q CB  
29381 O  OG1 . THR   Q  121 ? 1.8112 0.5896 1.2300 -0.0128 -0.2772 -0.1361 119 THR   Q OG1 
29382 C  CG2 . THR   Q  121 ? 1.8770 0.4290 1.3647 -0.0240 -0.2853 -0.1434 119 THR   Q CG2 
29383 N  N   . GLN   Q  122 ? 1.8828 0.5760 1.4356 0.1026  -0.3268 -0.1361 120 GLN   Q N   
29384 C  CA  . GLN   Q  122 ? 1.8680 0.5669 1.3683 0.1660  -0.2704 -0.0891 120 GLN   Q CA  
29385 C  C   . GLN   Q  122 ? 1.7669 0.5740 1.3442 0.1636  -0.2667 -0.0770 120 GLN   Q C   
29386 O  O   . GLN   Q  122 ? 1.8337 0.5555 1.2523 0.1937  -0.2440 -0.1205 120 GLN   Q O   
29387 C  CB  . GLN   Q  122 ? 1.8856 0.5553 1.4162 0.1341  -0.2439 -0.0585 120 GLN   Q CB  
29388 C  CG  . GLN   Q  122 ? 1.9211 0.5613 1.4349 0.0953  -0.2125 -0.0823 120 GLN   Q CG  
29389 C  CD  . GLN   Q  122 ? 1.9235 0.5897 1.4290 0.1093  -0.2178 -0.0878 120 GLN   Q CD  
29390 O  OE1 . GLN   Q  122 ? 1.9919 0.3249 1.3569 0.0504  -0.1732 -0.0646 120 GLN   Q OE1 
29391 N  NE2 . GLN   Q  122 ? 1.9383 0.7131 1.4082 0.0994  -0.1566 -0.1206 120 GLN   Q NE2 
29392 N  N   . SER   Q  123 ? 1.7520 0.6252 1.2970 0.1603  -0.2644 -0.0848 121 SER   Q N   
29393 C  CA  . SER   Q  123 ? 1.6381 0.6893 1.2691 0.1636  -0.2813 -0.0650 121 SER   Q CA  
29394 C  C   . SER   Q  123 ? 1.6479 0.6717 1.3077 0.1809  -0.2806 -0.0425 121 SER   Q C   
29395 O  O   . SER   Q  123 ? 1.6003 0.6691 1.3008 0.1743  -0.3508 0.0201  121 SER   Q O   
29396 C  CB  . SER   Q  123 ? 1.5940 0.7236 1.2472 0.1683  -0.2669 -0.0693 121 SER   Q CB  
29397 O  OG  . SER   Q  123 ? 1.5432 0.7231 1.2604 0.1665  -0.2624 -0.0831 121 SER   Q OG  
29398 N  N   . GLY   Q  124 ? 1.6564 0.6457 1.3269 0.1746  -0.2547 -0.0525 122 GLY   Q N   
29399 C  CA  . GLY   Q  124 ? 1.6703 0.5618 1.4065 0.1498  -0.2656 -0.0458 122 GLY   Q CA  
29400 C  C   . GLY   Q  124 ? 1.6682 0.5764 1.4314 0.1119  -0.2886 -0.0627 122 GLY   Q C   
29401 O  O   . GLY   Q  124 ? 1.6461 0.6435 1.4346 0.1554  -0.3291 -0.0365 122 GLY   Q O   
29402 N  N   . GLY   Q  125 ? 1.7019 0.5328 1.4210 0.1365  -0.2929 -0.0260 123 GLY   Q N   
29403 C  CA  . GLY   Q  125 ? 1.7092 0.5358 1.4452 0.1143  -0.2500 -0.0297 123 GLY   Q CA  
29404 C  C   . GLY   Q  125 ? 1.7789 0.5204 1.4315 0.1030  -0.2515 -0.0708 123 GLY   Q C   
29405 O  O   . GLY   Q  125 ? 1.7814 0.5535 1.4430 0.1225  -0.2241 -0.0699 123 GLY   Q O   
29406 N  N   . VAL   Q  126 ? 1.8445 0.4698 1.4300 0.0811  -0.2383 -0.1250 124 VAL   Q N   
29407 C  CA  . VAL   Q  126 ? 1.8859 0.4301 1.4634 0.0698  -0.2869 -0.1367 124 VAL   Q CA  
29408 C  C   . VAL   Q  126 ? 1.9853 0.3628 1.4696 0.0328  -0.3006 -0.1279 124 VAL   Q C   
29409 O  O   . VAL   Q  126 ? 2.0443 0.1491 1.4132 0.0314  -0.3071 -0.1134 124 VAL   Q O   
29410 C  CB  . VAL   Q  126 ? 1.8599 0.4161 1.5074 0.0810  -0.2876 -0.1352 124 VAL   Q CB  
29411 C  CG1 . VAL   Q  126 ? 1.8611 0.4536 1.5227 0.0876  -0.2629 -0.1510 124 VAL   Q CG1 
29412 C  CG2 . VAL   Q  126 ? 1.8618 0.4024 1.4992 0.1025  -0.2708 -0.1649 124 VAL   Q CG2 
29413 N  N   . ARG   Q  127 ? 2.0256 0.3719 1.4664 0.0481  -0.3095 -0.1555 125 ARG   Q N   
29414 C  CA  . ARG   Q  127 ? 1.9947 0.4275 1.4450 0.0674  -0.3007 -0.1576 125 ARG   Q CA  
29415 C  C   . ARG   Q  127 ? 1.9892 0.4956 1.4037 0.1594  -0.2504 -0.1796 125 ARG   Q C   
29416 O  O   . ARG   Q  127 ? 2.0131 0.4754 1.3780 0.1202  -0.2577 -0.1502 125 ARG   Q O   
29417 C  CB  . ARG   Q  127 ? 2.0471 0.3855 1.4698 0.0591  -0.3376 -0.1671 125 ARG   Q CB  
29418 C  CG  . ARG   Q  127 ? 2.0054 0.3594 1.4685 -0.0357 -0.3898 -0.2103 125 ARG   Q CG  
29419 C  CD  . ARG   Q  127 ? 2.0808 0.2929 1.4934 -0.0155 -0.3739 -0.2456 125 ARG   Q CD  
29420 N  NE  . ARG   Q  127 ? 2.0653 0.3314 1.4976 -0.0625 -0.4146 -0.2665 125 ARG   Q NE  
29421 C  CZ  . ARG   Q  127 ? 2.0473 0.3532 1.4952 -0.0592 -0.4419 -0.2721 125 ARG   Q CZ  
29422 N  NH1 . ARG   Q  127 ? 2.0492 0.3218 1.4831 -0.0473 -0.4302 -0.2985 125 ARG   Q NH1 
29423 N  NH2 . ARG   Q  127 ? 2.0377 0.3833 1.5580 -0.0709 -0.4589 -0.2802 125 ARG   Q NH2 
29424 N  N   . PRO   Q  128 ? 2.0175 0.4725 1.4388 0.2288  -0.2876 -0.2175 126 PRO   Q N   
29425 C  CA  . PRO   Q  128 ? 2.0342 0.4662 1.3935 0.2311  -0.2773 -0.2935 126 PRO   Q CA  
29426 C  C   . PRO   Q  128 ? 2.0614 0.4120 1.3801 0.1969  -0.2955 -0.3717 126 PRO   Q C   
29427 O  O   . PRO   Q  128 ? 2.1410 0.3528 1.4269 0.1503  -0.3197 -0.4899 126 PRO   Q O   
29428 C  CB  . PRO   Q  128 ? 2.0280 0.4512 1.3977 0.2304  -0.2907 -0.2888 126 PRO   Q CB  
29429 C  CG  . PRO   Q  128 ? 2.0524 0.4295 1.4103 0.2024  -0.2683 -0.2483 126 PRO   Q CG  
29430 C  CD  . PRO   Q  128 ? 2.0427 0.4066 1.4198 0.1957  -0.2689 -0.2337 126 PRO   Q CD  
29431 N  N   . PHE   Q  129 ? 2.1155 0.4539 1.3754 0.1851  -0.2838 -0.3532 127 PHE   Q N   
29432 C  CA  . PHE   Q  129 ? 2.1044 0.5191 1.3965 0.1356  -0.2837 -0.2557 127 PHE   Q CA  
29433 C  C   . PHE   Q  129 ? 2.1092 0.4666 1.3887 0.0986  -0.3033 -0.2099 127 PHE   Q C   
29434 O  O   . PHE   Q  129 ? 2.0562 0.4031 1.3527 0.1080  -0.3330 -0.0862 127 PHE   Q O   
29435 C  CB  . PHE   Q  129 ? 2.0866 0.5439 1.4214 0.1123  -0.2640 -0.2422 127 PHE   Q CB  
29436 C  CG  . PHE   Q  129 ? 2.0548 0.5317 1.4771 0.1109  -0.2422 -0.2316 127 PHE   Q CG  
29437 C  CD1 . PHE   Q  129 ? 2.0388 0.5682 1.5206 0.0975  -0.2509 -0.2276 127 PHE   Q CD1 
29438 C  CD2 . PHE   Q  129 ? 2.0294 0.5566 1.4983 0.0875  -0.2193 -0.2120 127 PHE   Q CD2 
29439 C  CE1 . PHE   Q  129 ? 2.0172 0.6089 1.5223 0.1128  -0.2162 -0.2494 127 PHE   Q CE1 
29440 C  CE2 . PHE   Q  129 ? 2.0099 0.5941 1.5070 0.0989  -0.1860 -0.2351 127 PHE   Q CE2 
29441 C  CZ  . PHE   Q  129 ? 1.9950 0.6433 1.5391 0.0881  -0.1955 -0.2332 127 PHE   Q CZ  
29442 N  N   . GLY   Q  130 ? 2.1215 0.5112 1.4468 0.0731  -0.3127 -0.1713 128 GLY   Q N   
29443 C  CA  . GLY   Q  130 ? 2.1073 0.5413 1.4585 0.0907  -0.3240 -0.1993 128 GLY   Q CA  
29444 C  C   . GLY   Q  130 ? 2.0681 0.5282 1.4670 0.0991  -0.3437 -0.2020 128 GLY   Q C   
29445 O  O   . GLY   Q  130 ? 2.0155 0.4935 1.5218 0.1560  -0.3593 -0.1555 128 GLY   Q O   
29446 N  N   . VAL   Q  131 ? 2.0234 0.5712 1.4800 0.0826  -0.3475 -0.2362 129 VAL   Q N   
29447 C  CA  . VAL   Q  131 ? 1.9937 0.6534 1.4840 0.0855  -0.3694 -0.2198 129 VAL   Q CA  
29448 C  C   . VAL   Q  131 ? 1.9768 0.6267 1.4852 0.0840  -0.3839 -0.2550 129 VAL   Q C   
29449 O  O   . VAL   Q  131 ? 2.0071 0.5909 1.4882 0.0518  -0.3661 -0.3209 129 VAL   Q O   
29450 C  CB  . VAL   Q  131 ? 1.9636 0.6800 1.5277 0.1003  -0.3437 -0.2099 129 VAL   Q CB  
29451 C  CG1 . VAL   Q  131 ? 1.9776 0.7036 1.5305 0.0805  -0.3366 -0.2022 129 VAL   Q CG1 
29452 C  CG2 . VAL   Q  131 ? 1.9803 0.7494 1.5498 0.0860  -0.3256 -0.1951 129 VAL   Q CG2 
29453 N  N   . SER   Q  132 ? 1.9895 0.6688 1.4783 0.1004  -0.3750 -0.2280 130 SER   Q N   
29454 C  CA  . SER   Q  132 ? 1.9968 0.7191 1.5566 0.0685  -0.3544 -0.2157 130 SER   Q CA  
29455 C  C   . SER   Q  132 ? 1.9955 0.6439 1.5489 0.0581  -0.3493 -0.2597 130 SER   Q C   
29456 O  O   . SER   Q  132 ? 2.0133 0.7396 1.5555 0.0060  -0.3426 -0.3522 130 SER   Q O   
29457 C  CB  . SER   Q  132 ? 2.0031 0.7325 1.5819 0.1143  -0.3513 -0.1842 130 SER   Q CB  
29458 O  OG  . SER   Q  132 ? 1.9959 0.8974 1.6154 0.1024  -0.3768 -0.1169 130 SER   Q OG  
29459 N  N   . THR   Q  133 ? 2.0169 0.5431 1.5537 0.1230  -0.3328 -0.2655 131 THR   Q N   
29460 C  CA  . THR   Q  133 ? 2.0146 0.5931 1.5808 0.1530  -0.3382 -0.2368 131 THR   Q CA  
29461 C  C   . THR   Q  133 ? 2.0372 0.4718 1.5331 0.1725  -0.3634 -0.2582 131 THR   Q C   
29462 O  O   . THR   Q  133 ? 2.0611 0.2839 1.5422 0.2139  -0.3413 -0.2237 131 THR   Q O   
29463 C  CB  . THR   Q  133 ? 1.9943 0.6110 1.6052 0.1319  -0.3393 -0.2524 131 THR   Q CB  
29464 O  OG1 . THR   Q  133 ? 1.9901 0.6684 1.6661 0.1134  -0.3298 -0.2199 131 THR   Q OG1 
29465 C  CG2 . THR   Q  133 ? 1.9735 0.6469 1.6112 0.1202  -0.3416 -0.2208 131 THR   Q CG2 
29466 N  N   . LEU   Q  134 ? 2.0448 0.5420 1.5036 0.1368  -0.3641 -0.2691 132 LEU   Q N   
29467 C  CA  . LEU   Q  134 ? 2.0574 0.6853 1.4892 0.1140  -0.3651 -0.2498 132 LEU   Q CA  
29468 C  C   . LEU   Q  134 ? 2.0598 0.6869 1.4488 0.0965  -0.3838 -0.2123 132 LEU   Q C   
29469 O  O   . LEU   Q  134 ? 2.0502 0.7860 1.4318 0.0798  -0.4024 -0.1983 132 LEU   Q O   
29470 C  CB  . LEU   Q  134 ? 2.0932 0.6706 1.4771 0.1318  -0.3476 -0.2625 132 LEU   Q CB  
29471 C  CG  . LEU   Q  134 ? 2.1248 0.6950 1.5129 0.1856  -0.3127 -0.2759 132 LEU   Q CG  
29472 C  CD1 . LEU   Q  134 ? 2.1738 0.7614 1.5293 0.1825  -0.3317 -0.2984 132 LEU   Q CD1 
29473 C  CD2 . LEU   Q  134 ? 2.1197 0.7308 1.4826 0.1781  -0.3089 -0.2717 132 LEU   Q CD2 
29474 N  N   . ILE   Q  135 ? 2.0239 0.7382 1.3948 0.0929  -0.3868 -0.2157 133 ILE   Q N   
29475 C  CA  . ILE   Q  135 ? 2.0216 0.7328 1.3689 0.0881  -0.3849 -0.2266 133 ILE   Q CA  
29476 C  C   . ILE   Q  135 ? 2.0582 0.7415 1.3502 0.0614  -0.4157 -0.2215 133 ILE   Q C   
29477 O  O   . ILE   Q  135 ? 2.0400 0.8378 1.4079 0.0470  -0.4489 -0.1958 133 ILE   Q O   
29478 C  CB  . ILE   Q  135 ? 2.0176 0.6864 1.3521 0.1104  -0.3569 -0.2330 133 ILE   Q CB  
29479 C  CG1 . ILE   Q  135 ? 2.0026 0.6742 1.3681 0.1155  -0.3456 -0.2372 133 ILE   Q CG1 
29480 C  CG2 . ILE   Q  135 ? 2.0241 0.6937 1.3586 0.1098  -0.3485 -0.2062 133 ILE   Q CG2 
29481 C  CD1 . ILE   Q  135 ? 1.9995 0.6533 1.3606 0.1216  -0.3296 -0.2602 133 ILE   Q CD1 
29482 N  N   . ALA   Q  136 ? 2.0769 0.7188 1.3372 0.0572  -0.4230 -0.2340 134 ALA   Q N   
29483 C  CA  . ALA   Q  136 ? 2.1594 0.7841 1.3428 0.0426  -0.4069 -0.2152 134 ALA   Q CA  
29484 C  C   . ALA   Q  136 ? 2.1705 0.7921 1.2808 0.0350  -0.4180 -0.1979 134 ALA   Q C   
29485 O  O   . ALA   Q  136 ? 2.1846 0.8225 1.1762 0.0009  -0.4109 -0.2131 134 ALA   Q O   
29486 C  CB  . ALA   Q  136 ? 2.1999 0.8057 1.3575 0.0302  -0.4121 -0.2253 134 ALA   Q CB  
29487 N  N   . GLY   Q  137 ? 2.1935 0.7903 1.3140 0.0277  -0.4225 -0.1718 135 GLY   Q N   
29488 C  CA  . GLY   Q  137 ? 2.2072 0.8116 1.3717 0.0528  -0.4237 -0.1359 135 GLY   Q CA  
29489 C  C   . GLY   Q  137 ? 2.2116 0.8325 1.4066 0.0761  -0.4054 -0.0976 135 GLY   Q C   
29490 O  O   . GLY   Q  137 ? 2.2233 0.8145 1.4589 0.0995  -0.4004 -0.0751 135 GLY   Q O   
29491 N  N   . PHE   Q  138 ? 2.2059 0.8293 1.4401 0.0788  -0.3983 -0.0633 136 PHE   Q N   
29492 C  CA  . PHE   Q  138 ? 2.2589 0.7564 1.4807 0.1217  -0.3668 -0.0146 136 PHE   Q CA  
29493 C  C   . PHE   Q  138 ? 2.2331 0.7701 1.4791 0.1443  -0.3796 -0.0137 136 PHE   Q C   
29494 O  O   . PHE   Q  138 ? 2.1814 0.9212 1.4639 0.1790  -0.3624 0.0519  136 PHE   Q O   
29495 C  CB  . PHE   Q  138 ? 2.3109 0.6972 1.4996 0.1260  -0.3611 0.0044  136 PHE   Q CB  
29496 C  CG  . PHE   Q  138 ? 2.3662 0.7211 1.5294 0.0947  -0.3343 -0.0146 136 PHE   Q CG  
29497 C  CD1 . PHE   Q  138 ? 2.3537 0.7865 1.5743 0.0886  -0.3333 -0.0128 136 PHE   Q CD1 
29498 C  CD2 . PHE   Q  138 ? 2.3787 0.7374 1.5605 0.0821  -0.3067 -0.0079 136 PHE   Q CD2 
29499 C  CE1 . PHE   Q  138 ? 2.3992 0.7928 1.6153 0.1219  -0.3268 -0.0443 136 PHE   Q CE1 
29500 C  CE2 . PHE   Q  138 ? 2.4045 0.7448 1.5867 0.1151  -0.2890 -0.0302 136 PHE   Q CE2 
29501 C  CZ  . PHE   Q  138 ? 2.4106 0.7732 1.6200 0.1094  -0.3156 -0.0477 136 PHE   Q CZ  
29502 N  N   . ASP   Q  139 ? 2.2098 0.8227 1.5014 0.1623  -0.3297 -0.0217 137 ASP   Q N   
29503 C  CA  . ASP   Q  139 ? 2.1929 0.8632 1.4565 0.1809  -0.2738 -0.0724 137 ASP   Q CA  
29504 C  C   . ASP   Q  139 ? 2.2105 0.8266 1.4415 0.1894  -0.2701 -0.1145 137 ASP   Q C   
29505 O  O   . ASP   Q  139 ? 2.1831 0.9053 1.4639 0.1750  -0.3117 -0.0565 137 ASP   Q O   
29506 C  CB  . ASP   Q  139 ? 2.1847 0.9242 1.4438 0.1849  -0.2223 -0.0908 137 ASP   Q CB  
29507 C  CG  . ASP   Q  139 ? 2.1180 0.9200 1.4573 0.2065  -0.1849 -0.1017 137 ASP   Q CG  
29508 O  OD1 . ASP   Q  139 ? 2.1734 0.9833 1.4532 0.1545  -0.1448 -0.1452 137 ASP   Q OD1 
29509 O  OD2 . ASP   Q  139 ? 2.1121 0.9544 1.4945 0.2036  -0.0988 -0.1334 137 ASP   Q OD2 
29510 N  N   . PRO   Q  140 ? 2.2081 0.7657 1.4548 0.1955  -0.2628 -0.0811 138 PRO   Q N   
29511 C  CA  . PRO   Q  140 ? 2.2026 0.6864 1.4871 0.1465  -0.2585 -0.1378 138 PRO   Q CA  
29512 C  C   . PRO   Q  140 ? 2.2044 0.7152 1.5185 0.1002  -0.2387 -0.1769 138 PRO   Q C   
29513 O  O   . PRO   Q  140 ? 2.1930 0.6367 1.5751 0.0362  -0.2494 -0.2624 138 PRO   Q O   
29514 C  CB  . PRO   Q  140 ? 2.1936 0.6564 1.4581 0.1539  -0.2539 -0.1127 138 PRO   Q CB  
29515 C  CG  . PRO   Q  140 ? 2.1887 0.6463 1.4385 0.1705  -0.2658 -0.1170 138 PRO   Q CG  
29516 C  CD  . PRO   Q  140 ? 2.1839 0.6906 1.4549 0.2199  -0.2550 -0.1132 138 PRO   Q CD  
29517 N  N   . ARG   Q  141 ? 2.2262 0.7601 1.5332 0.0969  -0.2496 -0.1560 139 ARG   Q N   
29518 C  CA  . ARG   Q  141 ? 2.2644 0.8022 1.5656 0.1009  -0.2204 -0.1337 139 ARG   Q CA  
29519 C  C   . ARG   Q  141 ? 2.3051 0.8497 1.5880 0.1193  -0.1721 -0.1476 139 ARG   Q C   
29520 O  O   . ARG   Q  141 ? 2.3467 0.6813 1.6010 0.1004  -0.1341 -0.2100 139 ARG   Q O   
29521 C  CB  . ARG   Q  141 ? 2.2674 0.8207 1.5730 0.0719  -0.2316 -0.1046 139 ARG   Q CB  
29522 C  CG  . ARG   Q  141 ? 2.2804 0.7763 1.6036 0.0697  -0.2353 -0.0769 139 ARG   Q CG  
29523 C  CD  . ARG   Q  141 ? 2.3283 0.8054 1.6083 0.0217  -0.2229 -0.0637 139 ARG   Q CD  
29524 N  NE  . ARG   Q  141 ? 2.3404 0.7566 1.6122 0.0380  -0.1973 -0.0276 139 ARG   Q NE  
29525 C  CZ  . ARG   Q  141 ? 2.3443 0.7340 1.6750 0.0480  -0.0937 -0.0166 139 ARG   Q CZ  
29526 N  NH1 . ARG   Q  141 ? 2.3350 0.7124 1.7059 0.0422  -0.1006 -0.0409 139 ARG   Q NH1 
29527 N  NH2 . ARG   Q  141 ? 2.3352 0.7062 1.7250 0.0936  -0.0737 0.0066  139 ARG   Q NH2 
29528 N  N   . ASP   Q  142 ? 2.3084 0.8464 1.6295 0.1327  -0.1687 -0.1478 140 ASP   Q N   
29529 C  CA  . ASP   Q  142 ? 2.3400 0.9382 1.6694 0.1877  -0.1518 -0.1750 140 ASP   Q CA  
29530 C  C   . ASP   Q  142 ? 2.3594 0.9894 1.6749 0.2016  -0.1989 -0.1831 140 ASP   Q C   
29531 O  O   . ASP   Q  142 ? 2.3599 1.0029 1.7270 0.3061  -0.1327 -0.1894 140 ASP   Q O   
29532 C  CB  . ASP   Q  142 ? 2.3307 0.9545 1.6845 0.2143  -0.1665 -0.2024 140 ASP   Q CB  
29533 C  CG  . ASP   Q  142 ? 2.3524 0.9551 1.7530 0.2229  -0.1801 -0.2401 140 ASP   Q CG  
29534 O  OD1 . ASP   Q  142 ? 2.3563 0.9266 1.8273 0.1832  -0.1753 -0.2049 140 ASP   Q OD1 
29535 O  OD2 . ASP   Q  142 ? 2.3174 0.8759 1.7736 0.3331  -0.2242 -0.3053 140 ASP   Q OD2 
29536 N  N   . ASP   Q  143 ? 2.4391 1.0902 1.6226 0.1839  -0.2041 -0.1879 141 ASP   Q N   
29537 C  CA  . ASP   Q  143 ? 2.4926 1.1227 1.6112 0.1668  -0.2161 -0.1958 141 ASP   Q CA  
29538 C  C   . ASP   Q  143 ? 2.5088 1.1347 1.6252 0.1946  -0.2631 -0.2411 141 ASP   Q C   
29539 O  O   . ASP   Q  143 ? 2.5723 0.9887 1.7885 0.2728  -0.2431 -0.2942 141 ASP   Q O   
29540 C  CB  . ASP   Q  143 ? 2.4623 1.2040 1.6330 0.1320  -0.1597 -0.1529 141 ASP   Q CB  
29541 C  CG  . ASP   Q  143 ? 2.5014 1.2516 1.5490 0.1325  -0.1195 -0.0775 141 ASP   Q CG  
29542 O  OD1 . ASP   Q  143 ? 2.3996 1.2621 1.5668 0.1393  -0.0629 -0.1016 141 ASP   Q OD1 
29543 O  OD2 . ASP   Q  143 ? 2.4809 1.3026 1.6130 0.0960  -0.0374 -0.0122 141 ASP   Q OD2 
29544 N  N   . GLU   Q  144 ? 2.5405 1.1134 1.5570 0.1141  -0.3034 -0.3078 142 GLU   Q N   
29545 C  CA  . GLU   Q  144 ? 2.5278 1.1071 1.5294 0.0677  -0.3720 -0.2609 142 GLU   Q CA  
29546 C  C   . GLU   Q  144 ? 2.4970 1.0729 1.5187 0.0627  -0.4034 -0.2521 142 GLU   Q C   
29547 O  O   . GLU   Q  144 ? 2.4185 0.9862 1.5034 -0.0375 -0.4178 -0.2560 142 GLU   Q O   
29548 C  CB  . GLU   Q  144 ? 2.5537 1.2300 1.5696 0.0535  -0.3985 -0.2906 142 GLU   Q CB  
29549 C  CG  . GLU   Q  144 ? 2.6308 1.2316 1.6371 0.0625  -0.3854 -0.3096 142 GLU   Q CG  
29550 C  CD  . GLU   Q  144 ? 2.6966 1.2995 1.5891 0.0248  -0.4063 -0.2747 142 GLU   Q CD  
29551 O  OE1 . GLU   Q  144 ? 2.7940 1.3974 1.5222 -0.0495 -0.4306 -0.2028 142 GLU   Q OE1 
29552 O  OE2 . GLU   Q  144 ? 2.7557 1.3806 1.6689 -0.0453 -0.3757 -0.3706 142 GLU   Q OE2 
29553 N  N   . PRO   Q  145 ? 2.4863 1.0076 1.5674 0.0581  -0.4018 -0.1542 143 PRO   Q N   
29554 C  CA  . PRO   Q  145 ? 2.4393 1.0308 1.5369 0.0824  -0.3954 -0.1713 143 PRO   Q CA  
29555 C  C   . PRO   Q  145 ? 2.3412 1.0524 1.4571 0.0893  -0.3242 -0.1984 143 PRO   Q C   
29556 O  O   . PRO   Q  145 ? 2.3275 1.2272 1.4366 0.1110  -0.4030 -0.1206 143 PRO   Q O   
29557 C  CB  . PRO   Q  145 ? 2.4777 1.0408 1.5745 0.0620  -0.4222 -0.1824 143 PRO   Q CB  
29558 C  CG  . PRO   Q  145 ? 2.5226 0.9990 1.5627 0.0620  -0.4410 -0.1777 143 PRO   Q CG  
29559 C  CD  . PRO   Q  145 ? 2.5100 0.9979 1.5497 0.0618  -0.4153 -0.1416 143 PRO   Q CD  
29560 N  N   . LYS   Q  146 ? 2.2903 0.8788 1.4115 0.0921  -0.3513 -0.2672 144 LYS   Q N   
29561 C  CA  . LYS   Q  146 ? 2.1945 0.7850 1.4039 0.0844  -0.3103 -0.2663 144 LYS   Q CA  
29562 C  C   . LYS   Q  146 ? 2.1746 0.6507 1.3773 0.1353  -0.3047 -0.3249 144 LYS   Q C   
29563 O  O   . LYS   Q  146 ? 2.1711 0.4449 1.3073 0.1194  -0.3326 -0.3858 144 LYS   Q O   
29564 C  CB  . LYS   Q  146 ? 2.1655 0.8129 1.3972 0.0645  -0.3203 -0.2681 144 LYS   Q CB  
29565 C  CG  . LYS   Q  146 ? 2.1398 0.8528 1.4361 0.0494  -0.3231 -0.2485 144 LYS   Q CG  
29566 C  CD  . LYS   Q  146 ? 2.1301 0.8798 1.4485 0.0425  -0.3019 -0.2688 144 LYS   Q CD  
29567 C  CE  . LYS   Q  146 ? 2.1280 0.8928 1.4524 0.0395  -0.2923 -0.2662 144 LYS   Q CE  
29568 N  NZ  . LYS   Q  146 ? 2.1160 0.8873 1.4818 0.0659  -0.2683 -0.2688 144 LYS   Q NZ  
29569 N  N   . LEU   Q  147 ? 2.1671 0.6761 1.4135 0.1461  -0.2433 -0.2613 145 LEU   Q N   
29570 C  CA  . LEU   Q  147 ? 2.1481 0.6533 1.4067 0.1886  -0.2515 -0.2356 145 LEU   Q CA  
29571 C  C   . LEU   Q  147 ? 2.0864 0.6190 1.3760 0.2311  -0.2107 -0.2613 145 LEU   Q C   
29572 O  O   . LEU   Q  147 ? 2.0841 0.6330 1.2894 0.2549  -0.2253 -0.2179 145 LEU   Q O   
29573 C  CB  . LEU   Q  147 ? 2.1947 0.6198 1.4441 0.1483  -0.2613 -0.2239 145 LEU   Q CB  
29574 C  CG  . LEU   Q  147 ? 2.2335 0.6377 1.4602 0.1236  -0.2779 -0.2025 145 LEU   Q CG  
29575 C  CD1 . LEU   Q  147 ? 2.2249 0.5535 1.4770 0.1048  -0.2898 -0.1872 145 LEU   Q CD1 
29576 C  CD2 . LEU   Q  147 ? 2.2548 0.6256 1.4616 0.1237  -0.2703 -0.1912 145 LEU   Q CD2 
29577 N  N   . TYR   Q  148 ? 2.0784 0.6055 1.3991 0.2322  -0.1916 -0.2900 146 TYR   Q N   
29578 C  CA  . TYR   Q  148 ? 2.0436 0.6879 1.4581 0.2296  -0.2036 -0.2438 146 TYR   Q CA  
29579 C  C   . TYR   Q  148 ? 2.0638 0.7047 1.4942 0.2467  -0.1757 -0.2223 146 TYR   Q C   
29580 O  O   . TYR   Q  148 ? 2.0606 0.8171 1.5767 0.2860  -0.1420 -0.2540 146 TYR   Q O   
29581 C  CB  . TYR   Q  148 ? 1.9793 0.7099 1.4381 0.1457  -0.1948 -0.2176 146 TYR   Q CB  
29582 C  CG  . TYR   Q  148 ? 1.9993 0.7126 1.4254 0.1395  -0.1810 -0.1729 146 TYR   Q CG  
29583 C  CD1 . TYR   Q  148 ? 1.9767 0.6771 1.4383 0.0988  -0.1647 -0.1791 146 TYR   Q CD1 
29584 C  CD2 . TYR   Q  148 ? 1.9470 0.6908 1.4132 0.1177  -0.1391 -0.1820 146 TYR   Q CD2 
29585 C  CE1 . TYR   Q  148 ? 1.9943 0.6112 1.3954 0.1097  -0.1417 -0.1982 146 TYR   Q CE1 
29586 C  CE2 . TYR   Q  148 ? 1.9532 0.6406 1.3814 0.1364  -0.1186 -0.1825 146 TYR   Q CE2 
29587 C  CZ  . TYR   Q  148 ? 1.9510 0.5969 1.3766 0.0966  -0.0981 -0.2025 146 TYR   Q CZ  
29588 O  OH  . TYR   Q  148 ? 2.0069 0.5186 1.3783 0.0984  -0.0341 -0.2071 146 TYR   Q OH  
29589 N  N   . GLN   Q  149 ? 2.0389 0.7711 1.5163 0.2743  -0.1946 -0.2105 147 GLN   Q N   
29590 C  CA  . GLN   Q  149 ? 2.0276 0.7778 1.5338 0.2441  -0.2242 -0.2084 147 GLN   Q CA  
29591 C  C   . GLN   Q  149 ? 1.9461 0.7357 1.5162 0.2268  -0.1937 -0.2379 147 GLN   Q C   
29592 O  O   . GLN   Q  149 ? 1.9687 0.6844 1.4863 0.2026  -0.2148 -0.2840 147 GLN   Q O   
29593 C  CB  . GLN   Q  149 ? 2.0956 0.8095 1.6029 0.2385  -0.2307 -0.2617 147 GLN   Q CB  
29594 C  CG  . GLN   Q  149 ? 2.1040 0.8190 1.6274 0.2524  -0.2516 -0.2227 147 GLN   Q CG  
29595 C  CD  . GLN   Q  149 ? 2.1160 0.7789 1.6601 0.2930  -0.2430 -0.2860 147 GLN   Q CD  
29596 O  OE1 . GLN   Q  149 ? 2.1792 0.7412 1.6648 0.2752  -0.2647 -0.2904 147 GLN   Q OE1 
29597 N  NE2 . GLN   Q  149 ? 2.1167 0.7619 1.6272 0.3023  -0.2508 -0.2736 147 GLN   Q NE2 
29598 N  N   . THR   Q  150 ? 1.8709 0.7328 1.4994 0.2160  -0.2347 -0.2222 148 THR   Q N   
29599 C  CA  . THR   Q  150 ? 1.8308 0.8081 1.5050 0.2091  -0.2232 -0.1692 148 THR   Q CA  
29600 C  C   . THR   Q  150 ? 1.8118 0.8049 1.4764 0.2212  -0.2381 -0.1703 148 THR   Q C   
29601 O  O   . THR   Q  150 ? 1.7904 0.8703 1.4937 0.2523  -0.2586 -0.1985 148 THR   Q O   
29602 C  CB  . THR   Q  150 ? 1.7947 0.7878 1.4885 0.1970  -0.2172 -0.1390 148 THR   Q CB  
29603 O  OG1 . THR   Q  150 ? 1.7903 0.8360 1.5065 0.1864  -0.2490 -0.0795 148 THR   Q OG1 
29604 C  CG2 . THR   Q  150 ? 1.7659 0.7971 1.4986 0.1913  -0.2340 -0.1221 148 THR   Q CG2 
29605 N  N   . GLU   Q  151 ? 1.8222 0.8374 1.4770 0.2026  -0.2330 -0.1427 149 GLU   Q N   
29606 C  CA  . GLU   Q  151 ? 1.8597 0.8368 1.4928 0.1812  -0.2707 -0.1318 149 GLU   Q CA  
29607 C  C   . GLU   Q  151 ? 1.8480 0.8315 1.4742 0.1293  -0.2809 -0.0575 149 GLU   Q C   
29608 O  O   . GLU   Q  151 ? 1.7541 0.8819 1.4355 0.1046  -0.2822 -0.0005 149 GLU   Q O   
29609 C  CB  . GLU   Q  151 ? 1.8799 0.8858 1.6103 0.2323  -0.2672 -0.1451 149 GLU   Q CB  
29610 C  CG  . GLU   Q  151 ? 1.8647 0.9440 1.6796 0.2553  -0.2540 -0.1750 149 GLU   Q CG  
29611 C  CD  . GLU   Q  151 ? 1.8776 1.0450 1.7454 0.3245  -0.2377 -0.1911 149 GLU   Q CD  
29612 O  OE1 . GLU   Q  151 ? 1.9356 0.9766 1.8836 0.3965  -0.2170 -0.1860 149 GLU   Q OE1 
29613 O  OE2 . GLU   Q  151 ? 1.8538 1.0643 1.7397 0.4018  -0.2034 -0.2109 149 GLU   Q OE2 
29614 N  N   . PRO   Q  152 ? 1.9044 0.7367 1.4472 0.0755  -0.3762 -0.0608 150 PRO   Q N   
29615 C  CA  . PRO   Q  152 ? 1.8885 0.7099 1.4241 0.0404  -0.3864 0.0270  150 PRO   Q CA  
29616 C  C   . PRO   Q  152 ? 1.8831 0.7299 1.3786 0.0493  -0.3788 0.0448  150 PRO   Q C   
29617 O  O   . PRO   Q  152 ? 1.8421 0.6436 1.3132 -0.0495 -0.4625 0.0907  150 PRO   Q O   
29618 C  CB  . PRO   Q  152 ? 1.9252 0.6862 1.4293 0.0280  -0.3929 -0.0026 150 PRO   Q CB  
29619 C  CG  . PRO   Q  152 ? 1.9393 0.6911 1.4386 0.0288  -0.4048 -0.0067 150 PRO   Q CG  
29620 C  CD  . PRO   Q  152 ? 1.9319 0.7206 1.4339 0.0577  -0.3803 -0.0343 150 PRO   Q CD  
29621 N  N   . SER   Q  153 ? 1.8982 0.7439 1.3559 0.0774  -0.3731 0.0725  151 SER   Q N   
29622 C  CA  . SER   Q  153 ? 1.8836 0.7607 1.2789 0.0889  -0.3400 0.0642  151 SER   Q CA  
29623 C  C   . SER   Q  153 ? 1.8881 0.7564 1.2472 0.1017  -0.3008 -0.0206 151 SER   Q C   
29624 O  O   . SER   Q  153 ? 1.8973 0.7791 1.1915 0.1341  -0.2675 -0.0245 151 SER   Q O   
29625 C  CB  . SER   Q  153 ? 1.8718 0.8218 1.2360 0.0831  -0.3144 0.0922  151 SER   Q CB  
29626 O  OG  . SER   Q  153 ? 1.8555 0.8516 1.2323 0.0717  -0.2770 0.0710  151 SER   Q OG  
29627 N  N   . GLY   Q  154 ? 1.9087 0.7045 1.2316 0.1112  -0.2650 -0.0406 152 GLY   Q N   
29628 C  CA  . GLY   Q  154 ? 1.9088 0.6846 1.2118 0.1439  -0.2460 -0.0439 152 GLY   Q CA  
29629 C  C   . GLY   Q  154 ? 1.9294 0.6968 1.2040 0.1619  -0.2309 -0.0626 152 GLY   Q C   
29630 O  O   . GLY   Q  154 ? 1.9198 0.7141 1.1585 0.1832  -0.1949 -0.0183 152 GLY   Q O   
29631 N  N   . ILE   Q  155 ? 1.9424 0.7533 1.2236 0.1661  -0.2296 -0.0974 153 ILE   Q N   
29632 C  CA  . ILE   Q  155 ? 1.9275 0.7909 1.2366 0.1597  -0.2293 -0.1107 153 ILE   Q CA  
29633 C  C   . ILE   Q  155 ? 1.9503 0.8202 1.2603 0.1360  -0.2638 -0.1041 153 ILE   Q C   
29634 O  O   . ILE   Q  155 ? 1.9555 0.8805 1.2611 0.1230  -0.3030 -0.1094 153 ILE   Q O   
29635 C  CB  . ILE   Q  155 ? 1.9428 0.7953 1.2456 0.1667  -0.2143 -0.1472 153 ILE   Q CB  
29636 C  CG1 . ILE   Q  155 ? 1.9448 0.8641 1.3312 0.1393  -0.2357 -0.1541 153 ILE   Q CG1 
29637 C  CG2 . ILE   Q  155 ? 1.8817 0.6891 1.2355 0.1814  -0.1897 -0.1890 153 ILE   Q CG2 
29638 C  CD1 . ILE   Q  155 ? 1.9393 0.9435 1.3802 0.1703  -0.2267 -0.1777 153 ILE   Q CD1 
29639 N  N   . TYR   Q  156 ? 1.9355 0.7847 1.2504 0.1754  -0.2795 -0.0932 154 TYR   Q N   
29640 C  CA  . TYR   Q  156 ? 1.9138 0.8103 1.2727 0.1658  -0.2995 -0.0838 154 TYR   Q CA  
29641 C  C   . TYR   Q  156 ? 1.9239 0.7625 1.2738 0.1931  -0.2903 -0.0816 154 TYR   Q C   
29642 O  O   . TYR   Q  156 ? 1.8872 0.7283 1.3115 0.2173  -0.2517 -0.0151 154 TYR   Q O   
29643 C  CB  . TYR   Q  156 ? 1.8643 0.8277 1.2706 0.1674  -0.3223 -0.0829 154 TYR   Q CB  
29644 C  CG  . TYR   Q  156 ? 1.8191 0.9335 1.3171 0.1212  -0.3166 -0.0496 154 TYR   Q CG  
29645 C  CD1 . TYR   Q  156 ? 1.7722 0.9750 1.3217 0.0796  -0.3047 -0.0298 154 TYR   Q CD1 
29646 C  CD2 . TYR   Q  156 ? 1.7813 0.9827 1.3211 0.0856  -0.3064 -0.0434 154 TYR   Q CD2 
29647 C  CE1 . TYR   Q  156 ? 1.7308 0.9908 1.3385 0.0822  -0.2715 -0.0576 154 TYR   Q CE1 
29648 C  CE2 . TYR   Q  156 ? 1.7351 1.0278 1.3302 0.0784  -0.3012 -0.0450 154 TYR   Q CE2 
29649 C  CZ  . TYR   Q  156 ? 1.6914 1.0237 1.3282 0.0694  -0.2864 -0.0533 154 TYR   Q CZ  
29650 O  OH  . TYR   Q  156 ? 1.6296 1.1274 1.3228 0.0517  -0.2886 -0.1099 154 TYR   Q OH  
29651 N  N   . SER   Q  157 ? 2.0009 0.7105 1.2433 0.1865  -0.2438 -0.1440 155 SER   Q N   
29652 C  CA  . SER   Q  157 ? 2.0827 0.7289 1.2186 0.1662  -0.2237 -0.1820 155 SER   Q CA  
29653 C  C   . SER   Q  157 ? 2.1609 0.6461 1.1809 0.1825  -0.2135 -0.2025 155 SER   Q C   
29654 O  O   . SER   Q  157 ? 2.1656 0.6055 1.1134 0.1684  -0.1934 -0.2223 155 SER   Q O   
29655 C  CB  . SER   Q  157 ? 2.0918 0.7613 1.2457 0.1954  -0.2078 -0.1503 155 SER   Q CB  
29656 O  OG  . SER   Q  157 ? 2.1131 0.8266 1.3144 0.1623  -0.1935 -0.0466 155 SER   Q OG  
29657 N  N   . SER   Q  158 ? 2.2094 0.6634 1.2319 0.1555  -0.1716 -0.2062 156 SER   Q N   
29658 C  CA  . SER   Q  158 ? 2.2679 0.7067 1.2638 0.1424  -0.2256 -0.2172 156 SER   Q CA  
29659 C  C   . SER   Q  158 ? 2.2670 0.7393 1.3009 0.1701  -0.2427 -0.2591 156 SER   Q C   
29660 O  O   . SER   Q  158 ? 2.3529 0.5510 1.1793 0.1559  -0.2504 -0.4208 156 SER   Q O   
29661 C  CB  . SER   Q  158 ? 2.3118 0.6749 1.2888 0.1521  -0.2425 -0.1859 156 SER   Q CB  
29662 O  OG  . SER   Q  158 ? 2.3867 0.5336 1.3283 0.1402  -0.2354 -0.1237 156 SER   Q OG  
29663 N  N   . TRP   Q  159 ? 2.2990 0.7949 1.2780 0.1312  -0.2474 -0.2970 157 TRP   Q N   
29664 C  CA  . TRP   Q  159 ? 2.3152 0.8701 1.2826 0.1343  -0.2505 -0.3377 157 TRP   Q CA  
29665 C  C   . TRP   Q  159 ? 2.3277 0.8871 1.2979 0.1603  -0.2476 -0.3196 157 TRP   Q C   
29666 O  O   . TRP   Q  159 ? 2.2924 0.8816 1.3165 0.1389  -0.2908 -0.3018 157 TRP   Q O   
29667 C  CB  . TRP   Q  159 ? 2.2980 0.9998 1.3104 0.1203  -0.2426 -0.2914 157 TRP   Q CB  
29668 C  CG  . TRP   Q  159 ? 2.2918 0.9942 1.2737 0.1285  -0.2379 -0.3215 157 TRP   Q CG  
29669 C  CD1 . TRP   Q  159 ? 2.2670 0.9608 1.2594 0.1093  -0.2507 -0.3054 157 TRP   Q CD1 
29670 C  CD2 . TRP   Q  159 ? 2.2943 0.9951 1.2799 0.1423  -0.2192 -0.3351 157 TRP   Q CD2 
29671 N  NE1 . TRP   Q  159 ? 2.2673 0.9604 1.2325 0.1102  -0.2531 -0.3183 157 TRP   Q NE1 
29672 C  CE2 . TRP   Q  159 ? 2.2893 1.0289 1.2622 0.1316  -0.2161 -0.3669 157 TRP   Q CE2 
29673 C  CE3 . TRP   Q  159 ? 2.3251 1.0901 1.3258 0.1205  -0.2009 -0.4125 157 TRP   Q CE3 
29674 C  CZ2 . TRP   Q  159 ? 2.2833 1.0694 1.2457 0.1507  -0.2202 -0.3571 157 TRP   Q CZ2 
29675 C  CZ3 . TRP   Q  159 ? 2.3348 1.1573 1.3016 0.1270  -0.2173 -0.3647 157 TRP   Q CZ3 
29676 C  CH2 . TRP   Q  159 ? 2.3065 1.1020 1.2856 0.1202  -0.2104 -0.3943 157 TRP   Q CH2 
29677 N  N   . SER   Q  160 ? 2.3738 0.9389 1.2935 0.1695  -0.2762 -0.3632 158 SER   Q N   
29678 C  CA  . SER   Q  160 ? 2.3760 0.9485 1.3029 0.1856  -0.3064 -0.3900 158 SER   Q CA  
29679 C  C   . SER   Q  160 ? 2.3749 0.8642 1.3267 0.2042  -0.3265 -0.4277 158 SER   Q C   
29680 O  O   . SER   Q  160 ? 2.3226 0.8030 1.3630 0.2263  -0.3486 -0.5390 158 SER   Q O   
29681 C  CB  . SER   Q  160 ? 2.4101 1.0564 1.3005 0.1922  -0.2627 -0.3751 158 SER   Q CB  
29682 O  OG  . SER   Q  160 ? 2.4195 1.1160 1.2693 0.1632  -0.2462 -0.3996 158 SER   Q OG  
29683 N  N   . ALA   Q  161 ? 2.3471 0.8823 1.3371 0.1692  -0.3388 -0.4248 159 ALA   Q N   
29684 C  CA  . ALA   Q  161 ? 2.3331 0.9308 1.3456 0.1825  -0.3340 -0.4136 159 ALA   Q CA  
29685 C  C   . ALA   Q  161 ? 2.3135 0.8920 1.3044 0.2174  -0.3059 -0.4528 159 ALA   Q C   
29686 O  O   . ALA   Q  161 ? 2.3244 1.0266 1.3066 0.2345  -0.3361 -0.3245 159 ALA   Q O   
29687 C  CB  . ALA   Q  161 ? 2.3797 1.0429 1.3482 0.1480  -0.3778 -0.4153 159 ALA   Q CB  
29688 N  N   . GLN   Q  162 ? 2.3260 0.6721 1.2658 0.2652  -0.3047 -0.5116 160 GLN   Q N   
29689 C  CA  . GLN   Q  162 ? 2.3158 0.6249 1.2991 0.2794  -0.3157 -0.5020 160 GLN   Q CA  
29690 C  C   . GLN   Q  162 ? 2.3160 0.5435 1.3157 0.2776  -0.3301 -0.4984 160 GLN   Q C   
29691 O  O   . GLN   Q  162 ? 2.3380 0.4654 1.3333 0.2702  -0.3254 -0.5427 160 GLN   Q O   
29692 C  CB  . GLN   Q  162 ? 2.2975 0.5747 1.3051 0.2834  -0.3088 -0.4960 160 GLN   Q CB  
29693 C  CG  . GLN   Q  162 ? 2.3058 0.5978 1.3220 0.2812  -0.2949 -0.4780 160 GLN   Q CG  
29694 C  CD  . GLN   Q  162 ? 2.3329 0.6290 1.3432 0.3003  -0.2799 -0.4403 160 GLN   Q CD  
29695 O  OE1 . GLN   Q  162 ? 2.4106 0.6315 1.2418 0.2529  -0.2244 -0.4936 160 GLN   Q OE1 
29696 N  NE2 . GLN   Q  162 ? 2.3686 0.6750 1.3419 0.2763  -0.2634 -0.4552 160 GLN   Q NE2 
29697 N  N   . THR   Q  163 ? 2.3224 0.5804 1.3515 0.2601  -0.3539 -0.4510 161 THR   Q N   
29698 C  CA  . THR   Q  163 ? 2.3321 0.5789 1.3701 0.2655  -0.3549 -0.3938 161 THR   Q CA  
29699 C  C   . THR   Q  163 ? 2.2539 0.5173 1.3860 0.2629  -0.3750 -0.3728 161 THR   Q C   
29700 O  O   . THR   Q  163 ? 2.2453 0.4407 1.3709 0.2354  -0.3838 -0.3863 161 THR   Q O   
29701 C  CB  . THR   Q  163 ? 2.4144 0.6330 1.3666 0.2753  -0.3643 -0.4353 161 THR   Q CB  
29702 O  OG1 . THR   Q  163 ? 2.3917 0.6341 1.3524 0.3010  -0.3454 -0.4773 161 THR   Q OG1 
29703 C  CG2 . THR   Q  163 ? 2.4307 0.6867 1.3902 0.3046  -0.3505 -0.4437 161 THR   Q CG2 
29704 N  N   . ILE   Q  164 ? 2.2454 0.5201 1.3986 0.2695  -0.3769 -0.3302 162 ILE   Q N   
29705 C  CA  . ILE   Q  164 ? 2.2572 0.6096 1.4299 0.2750  -0.3851 -0.2618 162 ILE   Q CA  
29706 C  C   . ILE   Q  164 ? 2.2770 0.6317 1.4691 0.2632  -0.3981 -0.2349 162 ILE   Q C   
29707 O  O   . ILE   Q  164 ? 2.3500 0.5466 1.4965 0.3485  -0.4001 -0.1894 162 ILE   Q O   
29708 C  CB  . ILE   Q  164 ? 2.2012 0.6215 1.4190 0.2431  -0.3841 -0.2498 162 ILE   Q CB  
29709 C  CG1 . ILE   Q  164 ? 2.2169 0.6355 1.4303 0.2340  -0.3753 -0.2064 162 ILE   Q CG1 
29710 C  CG2 . ILE   Q  164 ? 2.1767 0.6594 1.4231 0.2801  -0.3802 -0.2100 162 ILE   Q CG2 
29711 C  CD1 . ILE   Q  164 ? 2.2280 0.6576 1.4374 0.2055  -0.3329 -0.2186 162 ILE   Q CD1 
29712 N  N   . GLY   Q  165 ? 2.3040 0.6839 1.5141 0.2464  -0.4090 -0.1881 163 GLY   Q N   
29713 C  CA  . GLY   Q  165 ? 2.3064 0.6497 1.5771 0.2315  -0.4445 -0.1795 163 GLY   Q CA  
29714 C  C   . GLY   Q  165 ? 2.2676 0.6337 1.6385 0.2360  -0.4788 -0.1625 163 GLY   Q C   
29715 O  O   . GLY   Q  165 ? 2.3306 0.6125 1.7419 0.2905  -0.4522 -0.1959 163 GLY   Q O   
29716 N  N   . ARG   Q  166 ? 2.3014 0.6646 1.6571 0.1927  -0.5237 -0.1397 164 ARG   Q N   
29717 C  CA  . ARG   Q  166 ? 2.3476 0.6990 1.6611 0.1135  -0.5241 -0.1949 164 ARG   Q CA  
29718 C  C   . ARG   Q  166 ? 2.4216 0.6245 1.6231 0.0688  -0.5531 -0.1772 164 ARG   Q C   
29719 O  O   . ARG   Q  166 ? 2.4319 0.3468 1.6372 0.0318  -0.4890 -0.2287 164 ARG   Q O   
29720 C  CB  . ARG   Q  166 ? 2.3437 0.8134 1.7386 0.0772  -0.5500 -0.1962 164 ARG   Q CB  
29721 C  CG  . ARG   Q  166 ? 2.3646 0.8476 1.7668 0.0595  -0.5837 -0.1866 164 ARG   Q CG  
29722 C  CD  . ARG   Q  166 ? 2.3585 0.9644 1.8181 0.0393  -0.5922 -0.1702 164 ARG   Q CD  
29723 N  NE  . ARG   Q  166 ? 2.4269 1.0451 1.8336 0.0759  -0.6180 -0.1130 164 ARG   Q NE  
29724 C  CZ  . ARG   Q  166 ? 2.4284 1.2430 1.9007 0.1318  -0.5893 -0.0497 164 ARG   Q CZ  
29725 N  NH1 . ARG   Q  166 ? 2.4528 1.3228 1.9330 0.1513  -0.5967 -0.0010 164 ARG   Q NH1 
29726 N  NH2 . ARG   Q  166 ? 2.4421 1.3952 1.8764 0.1412  -0.5587 -0.0693 164 ARG   Q NH2 
29727 N  N   . ASN   Q  167 ? 2.4655 0.6779 1.6200 0.0801  -0.5180 -0.2544 165 ASN   Q N   
29728 C  CA  . ASN   Q  167 ? 2.5260 0.7764 1.5686 0.0332  -0.5100 -0.2043 165 ASN   Q CA  
29729 C  C   . ASN   Q  167 ? 2.5662 0.6881 1.4948 0.0718  -0.5357 -0.1882 165 ASN   Q C   
29730 O  O   . ASN   Q  167 ? 2.6074 0.6046 1.4953 0.0784  -0.5147 -0.1148 165 ASN   Q O   
29731 C  CB  . ASN   Q  167 ? 2.5678 0.8179 1.6132 0.0025  -0.5429 -0.2174 165 ASN   Q CB  
29732 C  CG  . ASN   Q  167 ? 2.5577 0.7968 1.6599 -0.0235 -0.5619 -0.2542 165 ASN   Q CG  
29733 O  OD1 . ASN   Q  167 ? 2.5317 0.7311 1.6726 -0.0577 -0.5787 -0.2885 165 ASN   Q OD1 
29734 N  ND2 . ASN   Q  167 ? 2.6056 0.8001 1.6808 -0.0088 -0.5682 -0.2474 165 ASN   Q ND2 
29735 N  N   . SER   Q  168 ? 2.5231 0.7094 1.4194 0.0904  -0.5469 -0.1620 166 SER   Q N   
29736 C  CA  . SER   Q  168 ? 2.4785 0.7746 1.3701 0.1163  -0.5039 -0.1478 166 SER   Q CA  
29737 C  C   . SER   Q  168 ? 2.5020 0.8565 1.4308 0.1657  -0.4955 -0.1635 166 SER   Q C   
29738 O  O   . SER   Q  168 ? 2.4757 0.9688 1.4404 0.2347  -0.4505 -0.1283 166 SER   Q O   
29739 C  CB  . SER   Q  168 ? 2.4683 0.7198 1.3351 0.1378  -0.4896 -0.1242 166 SER   Q CB  
29740 O  OG  . SER   Q  168 ? 2.4508 0.7011 1.2363 0.0903  -0.5026 -0.2070 166 SER   Q OG  
29741 N  N   . LYS   Q  169 ? 2.4491 0.7535 1.4642 0.1461  -0.4618 -0.2601 167 LYS   Q N   
29742 C  CA  . LYS   Q  169 ? 2.4849 0.7794 1.5382 0.1812  -0.4319 -0.2746 167 LYS   Q CA  
29743 C  C   . LYS   Q  169 ? 2.5055 0.7740 1.5345 0.2595  -0.3906 -0.2900 167 LYS   Q C   
29744 O  O   . LYS   Q  169 ? 2.4198 0.6423 1.6589 0.3196  -0.3887 -0.2369 167 LYS   Q O   
29745 C  CB  . LYS   Q  169 ? 2.4717 0.9019 1.5488 0.1991  -0.4360 -0.2070 167 LYS   Q CB  
29746 C  CG  . LYS   Q  169 ? 2.4543 1.0947 1.6072 0.1798  -0.3936 -0.1716 167 LYS   Q CG  
29747 C  CD  . LYS   Q  169 ? 2.4670 1.1985 1.6560 0.1633  -0.3631 -0.0646 167 LYS   Q CD  
29748 C  CE  . LYS   Q  169 ? 2.4835 1.2655 1.7349 0.1324  -0.3389 0.0288  167 LYS   Q CE  
29749 N  NZ  . LYS   Q  169 ? 2.4917 1.3305 1.7750 0.1336  -0.3286 0.1063  167 LYS   Q NZ  
29750 N  N   . THR   Q  170 ? 2.5130 0.8721 1.5977 0.2522  -0.3814 -0.3284 168 THR   Q N   
29751 C  CA  . THR   Q  170 ? 2.5872 0.8397 1.6243 0.2354  -0.3612 -0.4012 168 THR   Q CA  
29752 C  C   . THR   Q  170 ? 2.6517 0.9044 1.5267 0.2448  -0.3410 -0.4003 168 THR   Q C   
29753 O  O   . THR   Q  170 ? 2.7343 0.8209 1.5303 0.2921  -0.3518 -0.5096 168 THR   Q O   
29754 C  CB  . THR   Q  170 ? 2.6064 0.7770 1.6322 0.2098  -0.3796 -0.4298 168 THR   Q CB  
29755 O  OG1 . THR   Q  170 ? 2.5791 0.7104 1.7017 0.1819  -0.3578 -0.4323 168 THR   Q OG1 
29756 C  CG2 . THR   Q  170 ? 2.6078 0.8320 1.6496 0.1982  -0.3884 -0.4546 168 THR   Q CG2 
29757 N  N   . VAL   Q  171 ? 2.6523 0.8841 1.5466 0.2546  -0.3741 -0.3662 169 VAL   Q N   
29758 C  CA  . VAL   Q  171 ? 2.6579 0.9241 1.4782 0.2559  -0.4135 -0.3665 169 VAL   Q CA  
29759 C  C   . VAL   Q  171 ? 2.6430 0.9888 1.4952 0.2652  -0.4179 -0.3862 169 VAL   Q C   
29760 O  O   . VAL   Q  171 ? 2.6879 1.0979 1.5048 0.2418  -0.4075 -0.3638 169 VAL   Q O   
29761 C  CB  . VAL   Q  171 ? 2.6504 0.8455 1.4057 0.2166  -0.4358 -0.3942 169 VAL   Q CB  
29762 C  CG1 . VAL   Q  171 ? 2.6173 0.8312 1.4217 0.1982  -0.4148 -0.3825 169 VAL   Q CG1 
29763 C  CG2 . VAL   Q  171 ? 2.6357 0.8370 1.3937 0.2456  -0.4485 -0.3824 169 VAL   Q CG2 
29764 N  N   . ARG   Q  172 ? 2.6211 0.9429 1.4601 0.3098  -0.3874 -0.3881 170 ARG   Q N   
29765 C  CA  . ARG   Q  172 ? 2.5913 0.9372 1.4509 0.3486  -0.3851 -0.3627 170 ARG   Q CA  
29766 C  C   . ARG   Q  172 ? 2.5520 1.0676 1.4735 0.3815  -0.3771 -0.3763 170 ARG   Q C   
29767 O  O   . ARG   Q  172 ? 2.4901 1.0370 1.5032 0.3848  -0.3802 -0.3998 170 ARG   Q O   
29768 C  CB  . ARG   Q  172 ? 2.6020 0.9005 1.4430 0.3916  -0.3626 -0.3141 170 ARG   Q CB  
29769 C  CG  . ARG   Q  172 ? 2.5998 0.8389 1.4184 0.4140  -0.3259 -0.3141 170 ARG   Q CG  
29770 C  CD  . ARG   Q  172 ? 2.5938 0.7425 1.3705 0.4204  -0.2794 -0.3810 170 ARG   Q CD  
29771 N  NE  . ARG   Q  172 ? 2.6464 0.6147 1.3587 0.4155  -0.2999 -0.4109 170 ARG   Q NE  
29772 C  CZ  . ARG   Q  172 ? 2.6758 0.6696 1.3707 0.4072  -0.2684 -0.4125 170 ARG   Q CZ  
29773 N  NH1 . ARG   Q  172 ? 2.6988 0.6858 1.4338 0.3443  -0.2796 -0.3621 170 ARG   Q NH1 
29774 N  NH2 . ARG   Q  172 ? 2.6803 0.7231 1.3805 0.3987  -0.2093 -0.3803 170 ARG   Q NH2 
29775 N  N   . GLU   Q  173 ? 2.5534 1.0753 1.5222 0.3803  -0.3820 -0.3851 171 GLU   Q N   
29776 C  CA  . GLU   Q  173 ? 2.5935 1.1948 1.5263 0.3962  -0.3769 -0.4376 171 GLU   Q CA  
29777 C  C   . GLU   Q  173 ? 2.6865 1.0963 1.4900 0.3599  -0.3745 -0.4993 171 GLU   Q C   
29778 O  O   . GLU   Q  173 ? 2.6753 1.0411 1.5284 0.3774  -0.3445 -0.6123 171 GLU   Q O   
29779 C  CB  . GLU   Q  173 ? 2.5502 1.2542 1.5490 0.3882  -0.3886 -0.3311 171 GLU   Q CB  
29780 C  CG  . GLU   Q  173 ? 2.5354 1.3722 1.5723 0.4586  -0.3551 -0.3165 171 GLU   Q CG  
29781 C  CD  . GLU   Q  173 ? 2.5355 1.4874 1.6077 0.4919  -0.3386 -0.2717 171 GLU   Q CD  
29782 O  OE1 . GLU   Q  173 ? 2.5953 1.5536 1.5193 0.5085  -0.3294 -0.2742 171 GLU   Q OE1 
29783 O  OE2 . GLU   Q  173 ? 2.5254 1.5710 1.6257 0.5492  -0.2376 -0.2507 171 GLU   Q OE2 
29784 N  N   . PHE   Q  174 ? 2.6962 1.0549 1.5444 0.3536  -0.3912 -0.5199 172 PHE   Q N   
29785 C  CA  . PHE   Q  174 ? 2.7626 1.0965 1.5575 0.3270  -0.3978 -0.4828 172 PHE   Q CA  
29786 C  C   . PHE   Q  174 ? 2.7287 1.1248 1.5298 0.3226  -0.3566 -0.4576 172 PHE   Q C   
29787 O  O   . PHE   Q  174 ? 2.7701 0.9692 1.5043 0.3110  -0.3619 -0.4809 172 PHE   Q O   
29788 C  CB  . PHE   Q  174 ? 2.7702 1.1514 1.5736 0.3393  -0.4291 -0.5183 172 PHE   Q CB  
29789 C  CG  . PHE   Q  174 ? 2.8490 1.2141 1.5620 0.3281  -0.4565 -0.5190 172 PHE   Q CG  
29790 C  CD1 . PHE   Q  174 ? 2.8329 1.2245 1.5257 0.3520  -0.4489 -0.4846 172 PHE   Q CD1 
29791 C  CD2 . PHE   Q  174 ? 2.9068 1.3374 1.5503 0.2930  -0.5003 -0.5203 172 PHE   Q CD2 
29792 C  CE1 . PHE   Q  174 ? 2.8358 1.2711 1.5123 0.3440  -0.4662 -0.4895 172 PHE   Q CE1 
29793 C  CE2 . PHE   Q  174 ? 2.9129 1.2690 1.5808 0.3108  -0.4934 -0.5050 172 PHE   Q CE2 
29794 C  CZ  . PHE   Q  174 ? 2.8649 1.2635 1.5462 0.3356  -0.4945 -0.4998 172 PHE   Q CZ  
29795 N  N   . LEU   Q  175 ? 2.6669 1.0743 1.5192 0.2748  -0.3265 -0.4211 173 LEU   Q N   
29796 C  CA  . LEU   Q  175 ? 2.6449 1.0909 1.5419 0.2728  -0.2900 -0.3791 173 LEU   Q CA  
29797 C  C   . LEU   Q  175 ? 2.6530 0.9942 1.5222 0.2203  -0.2173 -0.3751 173 LEU   Q C   
29798 O  O   . LEU   Q  175 ? 2.6450 0.9167 1.4065 0.2718  -0.2133 -0.4320 173 LEU   Q O   
29799 C  CB  . LEU   Q  175 ? 2.6373 1.2129 1.4932 0.2815  -0.2790 -0.3755 173 LEU   Q CB  
29800 C  CG  . LEU   Q  175 ? 2.6151 1.3505 1.5486 0.2703  -0.2827 -0.3399 173 LEU   Q CG  
29801 C  CD1 . LEU   Q  175 ? 2.5787 1.3722 1.5544 0.2988  -0.2276 -0.3253 173 LEU   Q CD1 
29802 C  CD2 . LEU   Q  175 ? 2.6497 1.3960 1.5332 0.2567  -0.2975 -0.3284 173 LEU   Q CD2 
29803 N  N   . GLU   Q  176 ? 2.5997 1.0384 1.6447 0.2063  -0.2223 -0.3201 174 GLU   Q N   
29804 C  CA  . GLU   Q  176 ? 2.5873 1.1066 1.7507 0.1499  -0.1750 -0.3094 174 GLU   Q CA  
29805 C  C   . GLU   Q  176 ? 2.5635 1.0772 1.7670 0.1102  -0.1342 -0.2888 174 GLU   Q C   
29806 O  O   . GLU   Q  176 ? 2.6202 0.9639 1.8810 0.0576  -0.0993 -0.2687 174 GLU   Q O   
29807 C  CB  . GLU   Q  176 ? 2.6072 1.1735 1.8172 0.1986  -0.2089 -0.2844 174 GLU   Q CB  
29808 C  CG  . GLU   Q  176 ? 2.6293 1.1984 1.8790 0.1927  -0.2248 -0.3393 174 GLU   Q CG  
29809 C  CD  . GLU   Q  176 ? 2.6583 1.2980 1.9362 0.2206  -0.2649 -0.3121 174 GLU   Q CD  
29810 O  OE1 . GLU   Q  176 ? 2.7574 1.2729 2.0632 0.2464  -0.2445 -0.2825 174 GLU   Q OE1 
29811 O  OE2 . GLU   Q  176 ? 2.6402 1.4298 1.9944 0.1518  -0.2804 -0.4275 174 GLU   Q OE2 
29812 N  N   . LYS   Q  177 ? 2.6181 1.0965 1.7777 0.0932  -0.1576 -0.2915 175 LYS   Q N   
29813 C  CA  . LYS   Q  177 ? 2.6915 1.2294 1.7672 0.1091  -0.1178 -0.2498 175 LYS   Q CA  
29814 C  C   . LYS   Q  177 ? 2.7481 1.2382 1.7309 0.1339  -0.1034 -0.2574 175 LYS   Q C   
29815 O  O   . LYS   Q  177 ? 2.7090 1.3746 1.7773 0.2092  -0.0559 -0.1883 175 LYS   Q O   
29816 C  CB  . LYS   Q  177 ? 2.7670 1.2376 1.8862 0.0555  -0.1337 -0.2002 175 LYS   Q CB  
29817 C  CG  . LYS   Q  177 ? 2.7918 1.2550 1.9560 0.0074  -0.1670 -0.1598 175 LYS   Q CG  
29818 C  CD  . LYS   Q  177 ? 2.8321 1.2181 2.0279 -0.0800 -0.1848 -0.1383 175 LYS   Q CD  
29819 C  CE  . LYS   Q  177 ? 2.8476 1.1423 2.1350 -0.1375 -0.1784 -0.1554 175 LYS   Q CE  
29820 N  NZ  . LYS   Q  177 ? 2.8277 1.0955 2.2208 -0.1622 -0.1927 -0.1096 175 LYS   Q NZ  
29821 N  N   . ASN   Q  178 ? 2.8109 1.1533 1.7244 0.1417  -0.1390 -0.3060 176 ASN   Q N   
29822 C  CA  . ASN   Q  178 ? 2.9081 1.3061 1.6688 0.0986  -0.2026 -0.2718 176 ASN   Q CA  
29823 C  C   . ASN   Q  178 ? 2.8976 1.3321 1.5875 0.0526  -0.2184 -0.2235 176 ASN   Q C   
29824 O  O   . ASN   Q  178 ? 2.9590 1.5666 1.5740 0.0606  -0.1762 -0.0796 176 ASN   Q O   
29825 C  CB  . ASN   Q  178 ? 2.9178 1.2876 1.6964 0.0341  -0.2548 -0.3196 176 ASN   Q CB  
29826 C  CG  . ASN   Q  178 ? 2.9781 1.3766 1.6828 0.0220  -0.2987 -0.3694 176 ASN   Q CG  
29827 O  OD1 . ASN   Q  178 ? 3.0559 1.4277 1.6804 0.0199  -0.3225 -0.3998 176 ASN   Q OD1 
29828 N  ND2 . ASN   Q  178 ? 2.9617 1.4204 1.7038 -0.0009 -0.3113 -0.3278 176 ASN   Q ND2 
29829 N  N   . TYR   Q  179 ? 2.8630 1.2308 1.6118 0.0715  -0.1922 -0.2830 177 TYR   Q N   
29830 C  CA  . TYR   Q  179 ? 2.8388 1.1455 1.5656 0.1963  -0.1590 -0.2943 177 TYR   Q CA  
29831 C  C   . TYR   Q  179 ? 2.8402 0.9671 1.5264 0.2479  -0.1290 -0.3849 177 TYR   Q C   
29832 O  O   . TYR   Q  179 ? 2.8000 0.7723 1.5291 0.3383  -0.0749 -0.5403 177 TYR   Q O   
29833 C  CB  . TYR   Q  179 ? 2.8179 1.1705 1.5278 0.1827  -0.1602 -0.2332 177 TYR   Q CB  
29834 C  CG  . TYR   Q  179 ? 2.8042 1.1557 1.5299 0.1677  -0.1720 -0.1133 177 TYR   Q CG  
29835 C  CD1 . TYR   Q  179 ? 2.8144 1.1337 1.5095 0.1509  -0.1595 -0.0883 177 TYR   Q CD1 
29836 C  CD2 . TYR   Q  179 ? 2.8117 1.1070 1.4638 0.1612  -0.2051 -0.0443 177 TYR   Q CD2 
29837 C  CE1 . TYR   Q  179 ? 2.7707 1.1291 1.4354 0.1337  -0.1797 -0.0739 177 TYR   Q CE1 
29838 C  CE2 . TYR   Q  179 ? 2.7619 1.1004 1.4092 0.1578  -0.2271 -0.0209 177 TYR   Q CE2 
29839 C  CZ  . TYR   Q  179 ? 2.7438 1.2167 1.4038 0.1448  -0.2094 -0.0266 177 TYR   Q CZ  
29840 O  OH  . TYR   Q  179 ? 2.6917 1.2328 1.3375 0.0739  -0.2349 0.0315  177 TYR   Q OH  
29841 N  N   . ASP   Q  180 ? 2.8026 1.0119 1.5164 0.2465  -0.1401 -0.3763 178 ASP   Q N   
29842 C  CA  . ASP   Q  180 ? 2.7841 1.2221 1.5698 0.2221  -0.1551 -0.3426 178 ASP   Q CA  
29843 C  C   . ASP   Q  180 ? 2.7083 1.2694 1.6185 0.1547  -0.2052 -0.3266 178 ASP   Q C   
29844 O  O   . ASP   Q  180 ? 2.6421 1.3444 1.6783 0.1635  -0.2253 -0.2792 178 ASP   Q O   
29845 C  CB  . ASP   Q  180 ? 2.7989 1.3078 1.5676 0.1978  -0.1312 -0.3579 178 ASP   Q CB  
29846 C  CG  . ASP   Q  180 ? 2.8349 1.3996 1.4824 0.1938  -0.1017 -0.3471 178 ASP   Q CG  
29847 O  OD1 . ASP   Q  180 ? 2.7865 1.4696 1.4841 0.1574  -0.0980 -0.3367 178 ASP   Q OD1 
29848 O  OD2 . ASP   Q  180 ? 2.8791 1.4527 1.4319 0.2140  -0.0306 -0.3925 178 ASP   Q OD2 
29849 N  N   . ARG   Q  181 ? 2.7061 1.2820 1.6919 0.1630  -0.2321 -0.2655 179 ARG   Q N   
29850 C  CA  . ARG   Q  181 ? 2.6835 1.2493 1.7170 0.1553  -0.2433 -0.2350 179 ARG   Q CA  
29851 C  C   . ARG   Q  181 ? 2.7494 1.3133 1.6805 0.1070  -0.2347 -0.2459 179 ARG   Q C   
29852 O  O   . ARG   Q  181 ? 2.7183 1.3187 1.6128 0.1112  -0.2407 -0.2659 179 ARG   Q O   
29853 C  CB  . ARG   Q  181 ? 2.6400 1.1504 1.7606 0.1679  -0.2274 -0.2289 179 ARG   Q CB  
29854 C  CG  . ARG   Q  181 ? 2.5677 1.0787 1.7905 0.1972  -0.2418 -0.1894 179 ARG   Q CG  
29855 C  CD  . ARG   Q  181 ? 2.5054 1.0174 1.8143 0.2233  -0.2357 -0.1682 179 ARG   Q CD  
29856 N  NE  . ARG   Q  181 ? 2.4701 0.9769 1.8958 0.2547  -0.2301 -0.1039 179 ARG   Q NE  
29857 C  CZ  . ARG   Q  181 ? 2.4117 0.9596 1.9175 0.2646  -0.2230 -0.0947 179 ARG   Q CZ  
29858 N  NH1 . ARG   Q  181 ? 2.3733 0.9817 1.9353 0.2526  -0.1917 -0.1140 179 ARG   Q NH1 
29859 N  NH2 . ARG   Q  181 ? 2.3900 0.8728 1.9759 0.2667  -0.2019 -0.0620 179 ARG   Q NH2 
29860 N  N   . LYS   Q  182 ? 2.7998 1.4027 1.6661 0.1079  -0.1842 -0.2075 180 LYS   Q N   
29861 C  CA  . LYS   Q  182 ? 2.8362 1.4543 1.7342 0.0815  -0.1390 -0.1787 180 LYS   Q CA  
29862 C  C   . LYS   Q  182 ? 2.8167 1.4200 1.7712 0.0650  -0.1312 -0.1957 180 LYS   Q C   
29863 O  O   . LYS   Q  182 ? 2.8469 1.1998 1.9050 0.0390  -0.0441 -0.3841 180 LYS   Q O   
29864 C  CB  . LYS   Q  182 ? 2.7971 1.4422 1.7259 0.1568  -0.1644 -0.1127 180 LYS   Q CB  
29865 C  CG  . LYS   Q  182 ? 2.7910 1.4556 1.6862 0.1609  -0.1622 -0.0680 180 LYS   Q CG  
29866 C  CD  . LYS   Q  182 ? 2.7761 1.5297 1.6473 0.1362  -0.1525 -0.0658 180 LYS   Q CD  
29867 C  CE  . LYS   Q  182 ? 2.8065 1.5953 1.6043 0.2104  -0.1541 -0.0435 180 LYS   Q CE  
29868 N  NZ  . LYS   Q  182 ? 2.8291 1.6306 1.5584 0.1891  -0.1676 -0.0184 180 LYS   Q NZ  
29869 N  N   . GLU   Q  183 ? 2.7899 1.5896 1.7974 0.0600  -0.1290 -0.2309 181 GLU   Q N   
29870 C  CA  . GLU   Q  183 ? 2.7984 1.6455 1.7749 0.0724  -0.1330 -0.2177 181 GLU   Q CA  
29871 C  C   . GLU   Q  183 ? 2.7763 1.5880 1.6634 0.0607  -0.1810 -0.2559 181 GLU   Q C   
29872 O  O   . GLU   Q  183 ? 2.7422 1.6720 1.6801 0.0102  -0.1741 -0.2358 181 GLU   Q O   
29873 C  CB  . GLU   Q  183 ? 2.8228 1.7717 1.7360 0.0895  -0.1380 -0.1866 181 GLU   Q CB  
29874 C  CG  . GLU   Q  183 ? 2.8439 1.7972 1.8132 0.0944  -0.1354 -0.1173 181 GLU   Q CG  
29875 C  CD  . GLU   Q  183 ? 2.9137 1.9091 1.8347 0.0689  -0.0656 -0.1228 181 GLU   Q CD  
29876 O  OE1 . GLU   Q  183 ? 2.9368 1.9454 1.9482 0.0036  -0.0534 -0.1416 181 GLU   Q OE1 
29877 O  OE2 . GLU   Q  183 ? 2.9234 2.0013 1.9650 0.0530  -0.0310 -0.0949 181 GLU   Q OE2 
29878 N  N   . PRO   Q  184 ? 2.7835 1.6104 1.5886 0.0716  -0.2070 -0.2313 182 PRO   Q N   
29879 C  CA  . PRO   Q  184 ? 2.7129 1.5716 1.5448 0.0899  -0.2877 -0.2153 182 PRO   Q CA  
29880 C  C   . PRO   Q  184 ? 2.8064 1.5569 1.5151 0.1107  -0.3305 -0.1821 182 PRO   Q C   
29881 O  O   . PRO   Q  184 ? 2.7210 1.6693 1.4686 0.0398  -0.3495 -0.1835 182 PRO   Q O   
29882 C  CB  . PRO   Q  184 ? 2.7133 1.5775 1.5720 0.1026  -0.2335 -0.2434 182 PRO   Q CB  
29883 C  CG  . PRO   Q  184 ? 2.7324 1.6286 1.5493 0.0769  -0.2124 -0.2548 182 PRO   Q CG  
29884 C  CD  . PRO   Q  184 ? 2.7495 1.6580 1.5524 0.0657  -0.1781 -0.2523 182 PRO   Q CD  
29885 N  N   . PRO   Q  185 ? 2.7844 1.5152 1.5149 0.1553  -0.3471 -0.1604 183 PRO   Q N   
29886 C  CA  . PRO   Q  185 ? 2.8023 1.5210 1.5726 0.1801  -0.3580 -0.1578 183 PRO   Q CA  
29887 C  C   . PRO   Q  185 ? 2.7968 1.5072 1.6676 0.1620  -0.3491 -0.1716 183 PRO   Q C   
29888 O  O   . PRO   Q  185 ? 2.8161 1.6269 1.6166 0.1656  -0.3686 -0.2152 183 PRO   Q O   
29889 C  CB  . PRO   Q  185 ? 2.8124 1.4928 1.5168 0.1957  -0.3664 -0.1705 183 PRO   Q CB  
29890 C  CG  . PRO   Q  185 ? 2.7826 1.5277 1.4647 0.2107  -0.3673 -0.1825 183 PRO   Q CG  
29891 C  CD  . PRO   Q  185 ? 2.7817 1.5454 1.4620 0.2049  -0.3549 -0.1647 183 PRO   Q CD  
29892 N  N   . ALA   Q  186 ? 2.7362 1.3794 1.7237 0.1201  -0.3320 -0.0794 184 ALA   Q N   
29893 C  CA  . ALA   Q  186 ? 2.6630 1.3485 1.7766 0.1193  -0.3249 -0.0889 184 ALA   Q CA  
29894 C  C   . ALA   Q  186 ? 2.6307 1.3160 1.8210 0.0917  -0.3260 -0.0521 184 ALA   Q C   
29895 O  O   . ALA   Q  186 ? 2.6907 1.3233 1.9817 0.0835  -0.2898 -0.0557 184 ALA   Q O   
29896 C  CB  . ALA   Q  186 ? 2.6701 1.3072 1.7541 0.0822  -0.3448 -0.0638 184 ALA   Q CB  
29897 N  N   . THR   Q  187 ? 2.5894 1.2275 1.7626 0.1364  -0.3722 -0.0801 185 THR   Q N   
29898 C  CA  . THR   Q  187 ? 2.5152 1.3097 1.7262 0.1116  -0.4281 -0.0779 185 THR   Q CA  
29899 C  C   . THR   Q  187 ? 2.4782 1.3410 1.7476 0.1259  -0.3976 -0.1229 185 THR   Q C   
29900 O  O   . THR   Q  187 ? 2.4981 1.2884 1.7658 0.1463  -0.3891 -0.1763 185 THR   Q O   
29901 C  CB  . THR   Q  187 ? 2.4852 1.3533 1.7371 0.1141  -0.4373 -0.0614 185 THR   Q CB  
29902 O  OG1 . THR   Q  187 ? 2.4484 1.3441 1.7332 0.1904  -0.4937 -0.0605 185 THR   Q OG1 
29903 C  CG2 . THR   Q  187 ? 2.4979 1.3767 1.7207 0.1175  -0.4450 -0.0495 185 THR   Q CG2 
29904 N  N   . VAL   Q  188 ? 2.4908 1.3613 1.7481 0.1595  -0.4349 -0.1155 186 VAL   Q N   
29905 C  CA  . VAL   Q  188 ? 2.4779 1.3725 1.7505 0.1950  -0.4180 -0.1674 186 VAL   Q CA  
29906 C  C   . VAL   Q  188 ? 2.5172 1.3941 1.7921 0.2056  -0.4344 -0.2388 186 VAL   Q C   
29907 O  O   . VAL   Q  188 ? 2.4487 1.3795 1.6873 0.1921  -0.4544 -0.3069 186 VAL   Q O   
29908 C  CB  . VAL   Q  188 ? 2.4893 1.3164 1.7472 0.1693  -0.4128 -0.1892 186 VAL   Q CB  
29909 C  CG1 . VAL   Q  188 ? 2.4625 1.3073 1.7604 0.1732  -0.4072 -0.2204 186 VAL   Q CG1 
29910 C  CG2 . VAL   Q  188 ? 2.4816 1.2949 1.7069 0.1796  -0.3910 -0.1731 186 VAL   Q CG2 
29911 N  N   . GLU   Q  189 ? 2.6397 1.4288 1.7747 0.2115  -0.4201 -0.2297 187 GLU   Q N   
29912 C  CA  . GLU   Q  189 ? 2.7263 1.3851 1.8594 0.2017  -0.3892 -0.2289 187 GLU   Q CA  
29913 C  C   . GLU   Q  189 ? 2.8297 1.2294 1.9875 0.1710  -0.3501 -0.3091 187 GLU   Q C   
29914 O  O   . GLU   Q  189 ? 2.8978 1.1835 2.1081 0.1764  -0.2740 -0.3396 187 GLU   Q O   
29915 C  CB  . GLU   Q  189 ? 2.7624 1.5407 1.8441 0.1963  -0.3831 -0.2567 187 GLU   Q CB  
29916 C  CG  . GLU   Q  189 ? 2.7532 1.6883 1.8576 0.2160  -0.3764 -0.2499 187 GLU   Q CG  
29917 C  CD  . GLU   Q  189 ? 2.7782 1.7778 1.8177 0.2850  -0.3663 -0.2773 187 GLU   Q CD  
29918 O  OE1 . GLU   Q  189 ? 2.7557 1.8602 1.8369 0.3875  -0.3890 -0.2389 187 GLU   Q OE1 
29919 O  OE2 . GLU   Q  189 ? 2.8603 1.8271 1.8057 0.3271  -0.3462 -0.2655 187 GLU   Q OE2 
29920 N  N   . GLU   Q  190 ? 2.8606 1.0922 1.9955 0.0902  -0.3114 -0.3352 188 GLU   Q N   
29921 C  CA  . GLU   Q  190 ? 2.8769 1.1168 1.9829 0.0992  -0.3190 -0.3214 188 GLU   Q CA  
29922 C  C   . GLU   Q  190 ? 2.8548 1.1413 2.0277 0.1207  -0.3735 -0.2279 188 GLU   Q C   
29923 O  O   . GLU   Q  190 ? 2.7946 1.2529 2.0261 0.2418  -0.3569 -0.0116 188 GLU   Q O   
29924 C  CB  . GLU   Q  190 ? 2.9405 1.0479 1.9414 0.0439  -0.2676 -0.3862 188 GLU   Q CB  
29925 C  CG  . GLU   Q  190 ? 3.0113 1.0573 1.9562 0.0404  -0.2470 -0.4196 188 GLU   Q CG  
29926 C  CD  . GLU   Q  190 ? 3.0305 1.0562 1.9085 0.0703  -0.1948 -0.4705 188 GLU   Q CD  
29927 O  OE1 . GLU   Q  190 ? 3.0501 0.9759 2.0091 0.0815  -0.1480 -0.3774 188 GLU   Q OE1 
29928 O  OE2 . GLU   Q  190 ? 3.1233 1.0760 1.8165 0.0258  -0.2126 -0.5278 188 GLU   Q OE2 
29929 N  N   . CYS   Q  191 ? 2.8599 1.0776 1.9857 0.0790  -0.4498 -0.1615 189 CYS   Q N   
29930 C  CA  . CYS   Q  191 ? 2.8586 1.0485 1.9964 0.0578  -0.4782 -0.1369 189 CYS   Q CA  
29931 C  C   . CYS   Q  191 ? 2.8068 1.0008 1.9775 0.0483  -0.5441 -0.1549 189 CYS   Q C   
29932 O  O   . CYS   Q  191 ? 2.8845 0.9381 2.0765 0.0576  -0.5719 -0.1500 189 CYS   Q O   
29933 C  CB  . CYS   Q  191 ? 2.8852 0.9853 2.1389 0.0510  -0.4349 -0.1079 189 CYS   Q CB  
29934 S  SG  . CYS   Q  191 ? 2.9578 1.1033 2.1445 0.0100  -0.4107 -0.0558 189 CYS   Q SG  
29935 N  N   . VAL   Q  192 ? 2.8716 0.9944 1.8610 0.0712  -0.6030 -0.1263 190 VAL   Q N   
29936 C  CA  . VAL   Q  192 ? 2.8092 1.0787 1.8806 0.1226  -0.6374 -0.0849 190 VAL   Q CA  
29937 C  C   . VAL   Q  192 ? 2.9040 1.1057 1.8841 0.1120  -0.6162 -0.1152 190 VAL   Q C   
29938 O  O   . VAL   Q  192 ? 2.9342 1.3116 2.0599 0.0614  -0.5714 0.0306  190 VAL   Q O   
29939 C  CB  . VAL   Q  192 ? 2.8628 1.0024 1.8270 0.1133  -0.6777 -0.0730 190 VAL   Q CB  
29940 C  CG1 . VAL   Q  192 ? 2.8195 0.9927 1.8523 0.1442  -0.7051 -0.0785 190 VAL   Q CG1 
29941 C  CG2 . VAL   Q  192 ? 2.7939 0.9582 1.8071 0.0994  -0.6934 -0.0144 190 VAL   Q CG2 
29942 N  N   . LYS   Q  193 ? 2.9315 1.1164 1.8567 0.1310  -0.6139 -0.0909 191 LYS   Q N   
29943 C  CA  . LYS   Q  193 ? 2.9330 1.1234 1.7719 0.1868  -0.5814 -0.1229 191 LYS   Q CA  
29944 C  C   . LYS   Q  193 ? 2.8791 0.9673 1.7801 0.1586  -0.5630 -0.2019 191 LYS   Q C   
29945 O  O   . LYS   Q  193 ? 2.9687 0.9203 1.8728 0.1434  -0.5817 -0.2229 191 LYS   Q O   
29946 C  CB  . LYS   Q  193 ? 2.9852 1.1218 1.7763 0.2215  -0.5481 -0.1270 191 LYS   Q CB  
29947 C  CG  . LYS   Q  193 ? 3.0314 1.1618 1.7350 0.2319  -0.5198 -0.1588 191 LYS   Q CG  
29948 C  CD  . LYS   Q  193 ? 3.0604 1.2818 1.7400 0.2650  -0.4961 -0.1193 191 LYS   Q CD  
29949 C  CE  . LYS   Q  193 ? 3.0645 1.2928 1.7425 0.2691  -0.4897 -0.1286 191 LYS   Q CE  
29950 N  NZ  . LYS   Q  193 ? 3.0830 1.3116 1.7662 0.2947  -0.4633 -0.1336 191 LYS   Q NZ  
29951 N  N   . LEU   Q  194 ? 2.8617 0.9230 1.6775 0.1573  -0.5132 -0.2188 192 LEU   Q N   
29952 C  CA  . LEU   Q  194 ? 2.8107 0.9189 1.5575 0.1417  -0.4831 -0.2411 192 LEU   Q CA  
29953 C  C   . LEU   Q  194 ? 2.7798 0.9694 1.5442 0.1399  -0.5083 -0.2391 192 LEU   Q C   
29954 O  O   . LEU   Q  194 ? 2.7678 0.9549 1.5129 0.1477  -0.4989 -0.2737 192 LEU   Q O   
29955 C  CB  . LEU   Q  194 ? 2.7853 0.9280 1.4722 0.1692  -0.4374 -0.2455 192 LEU   Q CB  
29956 C  CG  . LEU   Q  194 ? 2.7507 0.9394 1.4430 0.1877  -0.3973 -0.2753 192 LEU   Q CG  
29957 C  CD1 . LEU   Q  194 ? 2.7720 0.9956 1.4100 0.1690  -0.3923 -0.3419 192 LEU   Q CD1 
29958 C  CD2 . LEU   Q  194 ? 2.7418 0.9523 1.4253 0.1951  -0.3616 -0.2518 192 LEU   Q CD2 
29959 N  N   . THR   Q  195 ? 2.7655 0.8937 1.5338 0.1582  -0.5239 -0.1565 193 THR   Q N   
29960 C  CA  . THR   Q  195 ? 2.7806 0.8852 1.5565 0.1731  -0.4978 -0.1472 193 THR   Q CA  
29961 C  C   . THR   Q  195 ? 2.7829 1.0196 1.6540 0.1263  -0.5160 -0.1437 193 THR   Q C   
29962 O  O   . THR   Q  195 ? 2.8991 1.0881 1.7171 0.0474  -0.4094 -0.0908 193 THR   Q O   
29963 C  CB  . THR   Q  195 ? 2.7497 0.8685 1.4824 0.1831  -0.5152 -0.1183 193 THR   Q CB  
29964 O  OG1 . THR   Q  195 ? 2.7402 0.7574 1.3682 0.2390  -0.5034 -0.1350 193 THR   Q OG1 
29965 C  CG2 . THR   Q  195 ? 2.7083 0.7623 1.4936 0.1933  -0.4972 -0.1505 193 THR   Q CG2 
29966 N  N   . VAL   Q  196 ? 2.7842 1.0390 1.6746 0.1401  -0.5318 -0.1642 194 VAL   Q N   
29967 C  CA  . VAL   Q  196 ? 2.8089 1.1477 1.7180 0.0844  -0.5404 -0.2266 194 VAL   Q CA  
29968 C  C   . VAL   Q  196 ? 2.8332 1.2098 1.7231 0.1342  -0.5036 -0.2700 194 VAL   Q C   
29969 O  O   . VAL   Q  196 ? 2.8298 1.3811 1.8065 0.0419  -0.4637 -0.2482 194 VAL   Q O   
29970 C  CB  . VAL   Q  196 ? 2.7767 1.1563 1.7515 0.0373  -0.5927 -0.2839 194 VAL   Q CB  
29971 C  CG1 . VAL   Q  196 ? 2.7878 1.1856 1.7917 0.0340  -0.6414 -0.2903 194 VAL   Q CG1 
29972 C  CG2 . VAL   Q  196 ? 2.7429 1.1834 1.7884 0.0390  -0.5555 -0.2776 194 VAL   Q CG2 
29973 N  N   . ARG   Q  197 ? 2.8933 1.3087 1.6942 0.1442  -0.4709 -0.2371 195 ARG   Q N   
29974 C  CA  . ARG   Q  197 ? 2.9024 1.3485 1.6316 0.1706  -0.4646 -0.2729 195 ARG   Q CA  
29975 C  C   . ARG   Q  197 ? 2.8826 1.3913 1.6282 0.1893  -0.4816 -0.2813 195 ARG   Q C   
29976 O  O   . ARG   Q  197 ? 2.9135 1.3814 1.5571 0.1716  -0.5069 -0.3142 195 ARG   Q O   
29977 C  CB  . ARG   Q  197 ? 2.9338 1.3471 1.5944 0.1712  -0.4600 -0.3098 195 ARG   Q CB  
29978 C  CG  . ARG   Q  197 ? 2.9308 1.3287 1.5906 0.1665  -0.4675 -0.3476 195 ARG   Q CG  
29979 C  CD  . ARG   Q  197 ? 2.9354 1.2906 1.5361 0.2032  -0.4711 -0.3709 195 ARG   Q CD  
29980 N  NE  . ARG   Q  197 ? 2.9413 1.2471 1.5114 0.1918  -0.4373 -0.3814 195 ARG   Q NE  
29981 C  CZ  . ARG   Q  197 ? 2.9493 1.1862 1.5305 0.2488  -0.4106 -0.3782 195 ARG   Q CZ  
29982 N  NH1 . ARG   Q  197 ? 2.9432 1.2062 1.5126 0.2370  -0.3945 -0.3829 195 ARG   Q NH1 
29983 N  NH2 . ARG   Q  197 ? 2.9541 1.1988 1.5698 0.2591  -0.3857 -0.3553 195 ARG   Q NH2 
29984 N  N   . SER   Q  198 ? 2.7998 1.3932 1.5691 0.2548  -0.5149 -0.2272 196 SER   Q N   
29985 C  CA  . SER   Q  198 ? 2.7382 1.3558 1.6041 0.2813  -0.4848 -0.1913 196 SER   Q CA  
29986 C  C   . SER   Q  198 ? 2.7312 1.2932 1.6903 0.2520  -0.4657 -0.1829 196 SER   Q C   
29987 O  O   . SER   Q  198 ? 2.7368 1.1956 1.9015 0.2987  -0.4292 -0.1861 196 SER   Q O   
29988 C  CB  . SER   Q  198 ? 2.6594 1.3230 1.4931 0.3291  -0.4839 -0.1541 196 SER   Q CB  
29989 O  OG  . SER   Q  198 ? 2.5818 1.2609 1.3694 0.3739  -0.5442 -0.0196 196 SER   Q OG  
29990 N  N   . LEU   Q  199 ? 2.6826 1.2662 1.7374 0.2100  -0.4953 -0.1866 197 LEU   Q N   
29991 C  CA  . LEU   Q  199 ? 2.5787 1.1845 1.8559 0.1054  -0.5363 -0.2182 197 LEU   Q CA  
29992 C  C   . LEU   Q  199 ? 2.6090 1.1899 1.8755 0.0893  -0.5481 -0.2512 197 LEU   Q C   
29993 O  O   . LEU   Q  199 ? 2.5259 1.0459 1.9414 -0.0482 -0.5487 -0.3741 197 LEU   Q O   
29994 C  CB  . LEU   Q  199 ? 2.5451 1.2586 1.9450 0.1709  -0.5733 -0.1133 197 LEU   Q CB  
29995 C  CG  . LEU   Q  199 ? 2.5208 1.2414 2.0110 0.1584  -0.5759 -0.1265 197 LEU   Q CG  
29996 C  CD1 . LEU   Q  199 ? 2.4538 1.3019 2.0527 0.1835  -0.5930 -0.1378 197 LEU   Q CD1 
29997 C  CD2 . LEU   Q  199 ? 2.5336 1.2269 2.0072 0.1327  -0.5511 -0.1431 197 LEU   Q CD2 
29998 N  N   . LEU   Q  200 ? 2.6077 1.1291 1.8795 0.0193  -0.5779 -0.2243 198 LEU   Q N   
29999 C  CA  . LEU   Q  200 ? 2.6435 1.1691 1.9429 -0.0179 -0.6005 -0.2239 198 LEU   Q CA  
30000 C  C   . LEU   Q  200 ? 2.6474 1.1146 2.0147 -0.0540 -0.5805 -0.2509 198 LEU   Q C   
30001 O  O   . LEU   Q  200 ? 2.6737 1.0237 2.1555 -0.0174 -0.5177 -0.2193 198 LEU   Q O   
30002 C  CB  . LEU   Q  200 ? 2.6943 1.2561 1.9327 -0.0083 -0.6137 -0.2395 198 LEU   Q CB  
30003 C  CG  . LEU   Q  200 ? 2.7027 1.2977 1.9429 0.0078  -0.6421 -0.2473 198 LEU   Q CG  
30004 C  CD1 . LEU   Q  200 ? 2.7311 1.3328 1.9303 0.0136  -0.6552 -0.2629 198 LEU   Q CD1 
30005 C  CD2 . LEU   Q  200 ? 2.7047 1.3359 1.9654 0.0047  -0.6481 -0.2191 198 LEU   Q CD2 
30006 N  N   . GLU   Q  201 ? 2.6479 1.0821 1.9732 -0.0541 -0.5760 -0.2372 199 GLU   Q N   
30007 C  CA  . GLU   Q  201 ? 2.6998 1.0322 1.9643 -0.0941 -0.5659 -0.2102 199 GLU   Q CA  
30008 C  C   . GLU   Q  201 ? 2.7490 1.0444 1.9918 -0.0986 -0.5554 -0.1856 199 GLU   Q C   
30009 O  O   . GLU   Q  201 ? 2.8200 1.0612 1.9704 0.0142  -0.5730 -0.2250 199 GLU   Q O   
30010 C  CB  . GLU   Q  201 ? 2.6929 1.0705 1.8888 -0.1189 -0.5249 -0.1722 199 GLU   Q CB  
30011 C  CG  . GLU   Q  201 ? 2.6820 1.1566 1.9015 -0.1513 -0.5437 -0.1281 199 GLU   Q CG  
30012 C  CD  . GLU   Q  201 ? 2.6850 1.0923 1.8706 -0.1746 -0.6009 -0.0802 199 GLU   Q CD  
30013 O  OE1 . GLU   Q  201 ? 2.6096 1.1204 1.9047 -0.1886 -0.6255 -0.0181 199 GLU   Q OE1 
30014 O  OE2 . GLU   Q  201 ? 2.7340 1.2048 1.8707 -0.2898 -0.6436 -0.0733 199 GLU   Q OE2 
30015 N  N   . VAL   Q  202 ? 2.7428 0.8906 2.1722 -0.0593 -0.5515 -0.1608 200 VAL   Q N   
30016 C  CA  . VAL   Q  202 ? 2.7499 0.8799 2.2282 -0.0602 -0.5136 -0.1315 200 VAL   Q CA  
30017 C  C   . VAL   Q  202 ? 2.7517 0.7170 2.3686 -0.0296 -0.5255 -0.0884 200 VAL   Q C   
30018 O  O   . VAL   Q  202 ? 2.7664 0.3838 2.5304 0.0036  -0.5513 -0.0943 200 VAL   Q O   
30019 C  CB  . VAL   Q  202 ? 2.7444 1.0309 2.2057 -0.0610 -0.5180 -0.1706 200 VAL   Q CB  
30020 C  CG1 . VAL   Q  202 ? 2.7073 1.0587 2.2174 -0.0472 -0.5025 -0.1940 200 VAL   Q CG1 
30021 C  CG2 . VAL   Q  202 ? 2.7439 1.0908 2.2046 -0.0585 -0.5238 -0.1800 200 VAL   Q CG2 
30022 N  N   . VAL   Q  203 ? 2.8433 0.8202 2.3576 -0.0056 -0.5384 -0.0275 201 VAL   Q N   
30023 C  CA  . VAL   Q  203 ? 2.8776 0.9205 2.3289 -0.0074 -0.4992 -0.0627 201 VAL   Q CA  
30024 C  C   . VAL   Q  203 ? 2.9461 0.9480 2.2857 -0.0557 -0.5169 -0.0660 201 VAL   Q C   
30025 O  O   . VAL   Q  203 ? 3.0052 0.8959 2.3279 -0.0942 -0.4574 -0.0804 201 VAL   Q O   
30026 C  CB  . VAL   Q  203 ? 2.8689 0.8742 2.3243 0.0059  -0.5083 -0.1167 201 VAL   Q CB  
30027 C  CG1 . VAL   Q  203 ? 2.8989 0.9453 2.3310 0.0110  -0.5256 -0.1178 201 VAL   Q CG1 
30028 C  CG2 . VAL   Q  203 ? 2.8592 0.8409 2.3089 -0.0012 -0.5225 -0.1275 201 VAL   Q CG2 
30029 N  N   . GLN   Q  204 ? 2.9387 1.0563 2.2916 -0.0614 -0.5206 -0.0950 202 GLN   Q N   
30030 C  CA  . GLN   Q  204 ? 2.9440 1.1776 2.2717 -0.0977 -0.5214 -0.1507 202 GLN   Q CA  
30031 C  C   . GLN   Q  204 ? 2.9388 1.2264 2.1827 -0.1359 -0.5388 -0.2464 202 GLN   Q C   
30032 O  O   . GLN   Q  204 ? 2.9555 1.4275 2.1084 -0.2555 -0.5988 -0.3050 202 GLN   Q O   
30033 C  CB  . GLN   Q  204 ? 2.8777 1.2157 2.2717 -0.0927 -0.5440 -0.1194 202 GLN   Q CB  
30034 C  CG  . GLN   Q  204 ? 2.8729 1.2848 2.2590 -0.0997 -0.5653 -0.1137 202 GLN   Q CG  
30035 C  CD  . GLN   Q  204 ? 2.9021 1.2841 2.2425 -0.0039 -0.5611 -0.0759 202 GLN   Q CD  
30036 O  OE1 . GLN   Q  204 ? 2.9334 1.2216 2.1477 -0.0052 -0.5317 -0.0418 202 GLN   Q OE1 
30037 N  NE2 . GLN   Q  204 ? 2.9187 1.3737 2.2717 0.0022  -0.5910 -0.0643 202 GLN   Q NE2 
30038 N  N   . THR   Q  205 ? 2.9533 1.3087 2.3557 -0.1083 -0.4916 -0.2767 203 THR   Q N   
30039 C  CA  . THR   Q  205 ? 2.9975 1.4038 2.3896 -0.0621 -0.4737 -0.2348 203 THR   Q CA  
30040 C  C   . THR   Q  205 ? 3.1373 1.3740 2.4460 -0.0332 -0.4664 -0.0903 203 THR   Q C   
30041 O  O   . THR   Q  205 ? 3.2258 1.3987 2.4617 -0.0238 -0.4781 -0.1054 203 THR   Q O   
30042 C  CB  . THR   Q  205 ? 3.0061 1.4825 2.4698 -0.1185 -0.4120 -0.2727 203 THR   Q CB  
30043 O  OG1 . THR   Q  205 ? 2.9187 1.3181 2.5630 -0.1165 -0.3676 -0.3076 203 THR   Q OG1 
30044 C  CG2 . THR   Q  205 ? 3.0130 1.5172 2.4270 -0.1062 -0.3838 -0.2867 203 THR   Q CG2 
30045 N  N   . GLY   Q  206 ? 3.2467 1.3723 2.4459 0.0559  -0.4803 -0.0653 204 GLY   Q N   
30046 C  CA  . GLY   Q  206 ? 3.2315 1.2992 2.4773 0.1758  -0.4512 -0.0787 204 GLY   Q CA  
30047 C  C   . GLY   Q  206 ? 3.3426 1.1234 2.5291 0.1933  -0.4792 -0.0413 204 GLY   Q C   
30048 O  O   . GLY   Q  206 ? 3.2681 1.0477 2.6377 0.3474  -0.3848 -0.0631 204 GLY   Q O   
30049 N  N   . ALA   Q  207 ? 3.3259 1.0745 2.4719 0.1993  -0.5027 -0.1013 205 ALA   Q N   
30050 C  CA  . ALA   Q  207 ? 3.3567 0.9043 2.4056 0.1704  -0.5479 -0.1197 205 ALA   Q CA  
30051 C  C   . ALA   Q  207 ? 3.3771 0.7041 2.4479 0.1398  -0.5724 -0.0383 205 ALA   Q C   
30052 O  O   . ALA   Q  207 ? 3.6064 0.3704 2.3839 0.1445  -0.5698 -0.1187 205 ALA   Q O   
30053 C  CB  . ALA   Q  207 ? 3.3485 1.0061 2.3653 0.1300  -0.5523 -0.1252 205 ALA   Q CB  
30054 N  N   . LYS   Q  208 ? 3.3434 0.7848 2.4088 0.1741  -0.6181 -0.0052 206 LYS   Q N   
30055 C  CA  . LYS   Q  208 ? 3.2363 1.0891 2.2885 0.1860  -0.6207 -0.0544 206 LYS   Q CA  
30056 C  C   . LYS   Q  208 ? 3.2578 1.0533 2.3168 0.1838  -0.6125 -0.0053 206 LYS   Q C   
30057 O  O   . LYS   Q  208 ? 3.3191 1.0894 2.3501 0.3395  -0.5274 0.0207  206 LYS   Q O   
30058 C  CB  . LYS   Q  208 ? 3.1739 1.3926 2.2529 0.1543  -0.6535 -0.0554 206 LYS   Q CB  
30059 C  CG  . LYS   Q  208 ? 3.0572 1.5543 2.2550 0.1543  -0.6542 -0.0566 206 LYS   Q CG  
30060 C  CD  . LYS   Q  208 ? 3.0496 1.6013 2.2618 0.1633  -0.6432 -0.0772 206 LYS   Q CD  
30061 C  CE  . LYS   Q  208 ? 2.9889 1.5621 2.3224 0.1859  -0.6159 -0.0707 206 LYS   Q CE  
30062 N  NZ  . LYS   Q  208 ? 3.0042 1.6463 2.2953 0.1867  -0.6431 -0.0542 206 LYS   Q NZ  
30063 N  N   . ASN   Q  209 ? 3.1395 1.0731 2.5089 0.0700  -0.5948 -0.0344 207 ASN   Q N   
30064 C  CA  . ASN   Q  209 ? 2.9931 1.2033 2.6220 -0.0346 -0.6083 0.0000  207 ASN   Q CA  
30065 C  C   . ASN   Q  209 ? 3.0031 1.1917 2.6482 -0.0301 -0.4948 0.0580  207 ASN   Q C   
30066 O  O   . ASN   Q  209 ? 3.0522 1.0967 2.6134 -0.0052 -0.4712 0.1467  207 ASN   Q O   
30067 C  CB  . ASN   Q  209 ? 3.0388 1.2027 2.7298 -0.1141 -0.6236 -0.0594 207 ASN   Q CB  
30068 C  CG  . ASN   Q  209 ? 3.0490 1.3401 2.8188 -0.2094 -0.6796 -0.0573 207 ASN   Q CG  
30069 O  OD1 . ASN   Q  209 ? 2.8909 1.3395 2.9214 -0.2624 -0.7348 0.0106  207 ASN   Q OD1 
30070 N  ND2 . ASN   Q  209 ? 3.0257 1.3526 2.7712 -0.3305 -0.6670 -0.1630 207 ASN   Q ND2 
30071 N  N   . ILE   Q  210 ? 2.8408 1.2988 2.6000 0.0175  -0.5434 0.0875  208 ILE   Q N   
30072 C  CA  . ILE   Q  210 ? 2.7544 1.3782 2.4431 0.0770  -0.4891 0.0985  208 ILE   Q CA  
30073 C  C   . ILE   Q  210 ? 2.6203 1.3971 2.3155 0.1211  -0.5772 0.1665  208 ILE   Q C   
30074 O  O   . ILE   Q  210 ? 2.6490 1.5279 2.2936 0.1119  -0.6168 0.1827  208 ILE   Q O   
30075 C  CB  . ILE   Q  210 ? 2.7640 1.3619 2.4112 0.0950  -0.5098 0.0893  208 ILE   Q CB  
30076 C  CG1 . ILE   Q  210 ? 2.7615 1.3144 2.4051 0.0448  -0.4605 -0.0874 208 ILE   Q CG1 
30077 C  CG2 . ILE   Q  210 ? 2.7701 1.4165 2.2907 0.1252  -0.4609 0.1863  208 ILE   Q CG2 
30078 C  CD1 . ILE   Q  210 ? 2.8020 1.3819 2.3543 -0.0018 -0.5034 -0.1211 208 ILE   Q CD1 
30079 N  N   . GLU   Q  211 ? 2.6359 1.3046 2.2682 0.0782  -0.4615 0.1410  209 GLU   Q N   
30080 C  CA  . GLU   Q  211 ? 2.5672 1.2972 2.1537 0.0588  -0.4426 0.1580  209 GLU   Q CA  
30081 C  C   . GLU   Q  211 ? 2.6325 1.1757 1.9700 0.0234  -0.4419 0.1104  209 GLU   Q C   
30082 O  O   . GLU   Q  211 ? 2.5733 1.1783 2.0220 -0.0071 -0.4005 0.0946  209 GLU   Q O   
30083 C  CB  . GLU   Q  211 ? 2.4793 1.2874 2.1600 0.0715  -0.3302 0.1885  209 GLU   Q CB  
30084 C  CG  . GLU   Q  211 ? 2.4469 1.3394 2.2301 0.0851  -0.3437 0.3090  209 GLU   Q CG  
30085 C  CD  . GLU   Q  211 ? 2.3428 1.4365 2.1607 0.0958  -0.2411 0.4342  209 GLU   Q CD  
30086 O  OE1 . GLU   Q  211 ? 2.3918 1.5830 2.0539 -0.0054 -0.2440 0.5521  209 GLU   Q OE1 
30087 O  OE2 . GLU   Q  211 ? 2.2899 1.4859 2.1541 0.1993  -0.2896 0.6156  209 GLU   Q OE2 
30088 N  N   . ILE   Q  212 ? 2.6569 1.1259 1.8561 0.0821  -0.5273 0.0306  210 ILE   Q N   
30089 C  CA  . ILE   Q  212 ? 2.6618 1.1128 1.8107 0.0864  -0.5364 0.0102  210 ILE   Q CA  
30090 C  C   . ILE   Q  212 ? 2.6035 1.1077 1.8149 0.0266  -0.5983 0.0184  210 ILE   Q C   
30091 O  O   . ILE   Q  212 ? 2.5917 1.3135 1.9004 0.0404  -0.6551 0.0611  210 ILE   Q O   
30092 C  CB  . ILE   Q  212 ? 2.7289 1.0992 1.8198 0.1223  -0.5649 -0.0151 210 ILE   Q CB  
30093 C  CG1 . ILE   Q  212 ? 2.7531 1.1068 1.8308 0.0940  -0.5697 -0.0747 210 ILE   Q CG1 
30094 C  CG2 . ILE   Q  212 ? 2.7229 1.1167 1.7831 0.1427  -0.5515 -0.0055 210 ILE   Q CG2 
30095 C  CD1 . ILE   Q  212 ? 2.7430 1.0262 1.7784 0.0916  -0.5550 -0.1449 210 ILE   Q CD1 
30096 N  N   . THR   Q  213 ? 2.6017 1.0770 1.7681 -0.0221 -0.5559 0.0458  211 THR   Q N   
30097 C  CA  . THR   Q  213 ? 2.5475 1.0711 1.6817 -0.0110 -0.5426 0.0140  211 THR   Q CA  
30098 C  C   . THR   Q  213 ? 2.5211 0.9785 1.6564 -0.0276 -0.5631 -0.0810 211 THR   Q C   
30099 O  O   . THR   Q  213 ? 2.5066 0.9968 1.5987 -0.0298 -0.5825 -0.0917 211 THR   Q O   
30100 C  CB  . THR   Q  213 ? 2.4710 0.9768 1.6408 -0.0109 -0.4457 0.0781  211 THR   Q CB  
30101 O  OG1 . THR   Q  213 ? 2.4697 1.0143 1.6394 0.0118  -0.4099 0.0680  211 THR   Q OG1 
30102 C  CG2 . THR   Q  213 ? 2.4630 0.9681 1.6443 0.0219  -0.4224 0.1242  211 THR   Q CG2 
30103 N  N   . VAL   Q  214 ? 2.5623 0.8931 1.6516 -0.0171 -0.5784 -0.1463 212 VAL   Q N   
30104 C  CA  . VAL   Q  214 ? 2.5581 1.0111 1.6387 0.0591  -0.5433 -0.1049 212 VAL   Q CA  
30105 C  C   . VAL   Q  214 ? 2.5141 0.9611 1.7827 0.1000  -0.5062 -0.0916 212 VAL   Q C   
30106 O  O   . VAL   Q  214 ? 2.5189 1.0715 1.9396 0.1549  -0.4445 -0.0491 212 VAL   Q O   
30107 C  CB  . VAL   Q  214 ? 2.6479 1.0153 1.6587 0.0577  -0.6044 -0.0766 212 VAL   Q CB  
30108 C  CG1 . VAL   Q  214 ? 2.6739 1.0199 1.5909 0.0480  -0.6224 -0.0649 212 VAL   Q CG1 
30109 C  CG2 . VAL   Q  214 ? 2.6595 1.0534 1.6771 0.0216  -0.6397 -0.0648 212 VAL   Q CG2 
30110 N  N   . VAL   Q  215 ? 2.4471 0.9341 1.8341 0.1876  -0.4613 -0.0712 213 VAL   Q N   
30111 C  CA  . VAL   Q  215 ? 2.4191 0.9128 1.7490 0.2381  -0.4593 -0.0946 213 VAL   Q CA  
30112 C  C   . VAL   Q  215 ? 2.4337 0.9965 1.7813 0.2692  -0.4011 -0.1168 213 VAL   Q C   
30113 O  O   . VAL   Q  215 ? 2.4511 0.9606 1.8394 0.3112  -0.3667 0.0028  213 VAL   Q O   
30114 C  CB  . VAL   Q  215 ? 2.4097 0.8812 1.7267 0.2506  -0.4482 -0.1020 213 VAL   Q CB  
30115 C  CG1 . VAL   Q  215 ? 2.3886 0.9273 1.6490 0.2748  -0.4567 -0.1527 213 VAL   Q CG1 
30116 C  CG2 . VAL   Q  215 ? 2.3671 0.9210 1.7075 0.2345  -0.4664 -0.0941 213 VAL   Q CG2 
30117 N  N   . LYS   Q  216 ? 2.4544 1.0301 1.7319 0.2483  -0.4199 -0.0888 214 LYS   Q N   
30118 C  CA  . LYS   Q  216 ? 2.4191 1.0952 1.6713 0.2245  -0.4340 -0.1408 214 LYS   Q CA  
30119 C  C   . LYS   Q  216 ? 2.3370 1.0771 1.6000 0.1891  -0.3996 -0.0784 214 LYS   Q C   
30120 O  O   . LYS   Q  216 ? 2.3286 1.0238 1.6392 0.2042  -0.4203 -0.1338 214 LYS   Q O   
30121 C  CB  . LYS   Q  216 ? 2.4583 1.0969 1.6721 0.2600  -0.4789 -0.2321 214 LYS   Q CB  
30122 C  CG  . LYS   Q  216 ? 2.4598 1.1501 1.6971 0.2750  -0.5391 -0.2801 214 LYS   Q CG  
30123 C  CD  . LYS   Q  216 ? 2.4588 1.0997 1.7151 0.2937  -0.5776 -0.3727 214 LYS   Q CD  
30124 C  CE  . LYS   Q  216 ? 2.4328 1.0727 1.7812 0.3216  -0.6051 -0.4069 214 LYS   Q CE  
30125 N  NZ  . LYS   Q  216 ? 2.4648 1.0983 1.8126 0.3244  -0.6343 -0.4170 214 LYS   Q NZ  
30126 N  N   . PRO   Q  217 ? 2.3646 1.0012 1.5202 0.1916  -0.4291 -0.0237 215 PRO   Q N   
30127 C  CA  . PRO   Q  217 ? 2.3373 0.9810 1.4342 0.1766  -0.4100 0.0218  215 PRO   Q CA  
30128 C  C   . PRO   Q  217 ? 2.3317 0.9878 1.4459 0.1768  -0.4415 0.0115  215 PRO   Q C   
30129 O  O   . PRO   Q  217 ? 2.3513 1.0397 1.4457 0.1827  -0.4568 0.0148  215 PRO   Q O   
30130 C  CB  . PRO   Q  217 ? 2.3409 0.9800 1.4358 0.1853  -0.4078 0.0470  215 PRO   Q CB  
30131 C  CG  . PRO   Q  217 ? 2.3463 0.9930 1.4551 0.1838  -0.3852 0.0456  215 PRO   Q CG  
30132 C  CD  . PRO   Q  217 ? 2.3533 1.0334 1.4947 0.1688  -0.4120 0.0259  215 PRO   Q CD  
30133 N  N   . ASP   Q  218 ? 2.3428 1.0354 1.4789 0.1221  -0.4400 -0.0057 216 ASP   Q N   
30134 C  CA  . ASP   Q  218 ? 2.3274 1.0739 1.5085 0.1210  -0.4121 -0.0361 216 ASP   Q CA  
30135 C  C   . ASP   Q  218 ? 2.3252 1.0645 1.5139 0.1174  -0.4116 -0.0063 216 ASP   Q C   
30136 O  O   . ASP   Q  218 ? 2.3405 1.0479 1.5262 0.1337  -0.4272 -0.0215 216 ASP   Q O   
30137 C  CB  . ASP   Q  218 ? 2.4174 1.1064 1.4622 0.1300  -0.4676 -0.0488 216 ASP   Q CB  
30138 C  CG  . ASP   Q  218 ? 2.4410 1.0954 1.4288 0.1113  -0.4590 -0.1019 216 ASP   Q CG  
30139 O  OD1 . ASP   Q  218 ? 2.5052 1.0015 1.4386 0.0790  -0.4699 -0.1686 216 ASP   Q OD1 
30140 O  OD2 . ASP   Q  218 ? 2.4916 1.1145 1.3195 0.1471  -0.5297 -0.2115 216 ASP   Q OD2 
30141 N  N   . SER   Q  219 ? 2.2778 1.0212 1.5554 0.0794  -0.3202 -0.0153 217 SER   Q N   
30142 C  CA  . SER   Q  219 ? 2.2734 0.9978 1.5751 0.0914  -0.3089 -0.0274 217 SER   Q CA  
30143 C  C   . SER   Q  219 ? 2.2455 0.9841 1.5747 0.1177  -0.3377 0.0434  217 SER   Q C   
30144 O  O   . SER   Q  219 ? 2.2551 0.9672 1.5033 0.1336  -0.3270 0.0501  217 SER   Q O   
30145 C  CB  . SER   Q  219 ? 2.2541 1.0345 1.6131 0.0822  -0.2700 -0.0611 217 SER   Q CB  
30146 O  OG  . SER   Q  219 ? 2.2380 1.1013 1.6250 0.0728  -0.2336 -0.1298 217 SER   Q OG  
30147 N  N   . ASP   Q  220 ? 2.3222 0.9508 1.5512 0.0903  -0.3723 0.0538  218 ASP   Q N   
30148 C  CA  . ASP   Q  220 ? 2.3373 1.0247 1.6094 0.0913  -0.4452 0.0966  218 ASP   Q CA  
30149 C  C   . ASP   Q  220 ? 2.3308 1.0210 1.6625 0.1103  -0.4469 0.0846  218 ASP   Q C   
30150 O  O   . ASP   Q  220 ? 2.3284 1.0825 1.7341 0.2233  -0.4234 0.1510  218 ASP   Q O   
30151 C  CB  . ASP   Q  220 ? 2.3902 0.9184 1.6229 0.0319  -0.4510 0.1890  218 ASP   Q CB  
30152 C  CG  . ASP   Q  220 ? 2.4293 0.9143 1.6524 -0.0173 -0.4866 0.2436  218 ASP   Q CG  
30153 O  OD1 . ASP   Q  220 ? 2.4382 0.8667 1.7139 -0.0398 -0.4685 0.2648  218 ASP   Q OD1 
30154 O  OD2 . ASP   Q  220 ? 2.4280 0.9733 1.6121 -0.0672 -0.4748 0.3529  218 ASP   Q OD2 
30155 N  N   . ILE   Q  221 ? 2.2925 1.0667 1.6598 0.1380  -0.4499 0.0159  219 ILE   Q N   
30156 C  CA  . ILE   Q  221 ? 2.3246 0.9973 1.6928 0.1684  -0.4757 -0.0277 219 ILE   Q CA  
30157 C  C   . ILE   Q  221 ? 2.3554 0.8941 1.8067 0.1171  -0.5036 -0.0316 219 ILE   Q C   
30158 O  O   . ILE   Q  221 ? 2.3359 0.9638 1.7956 0.1193  -0.4526 -0.0069 219 ILE   Q O   
30159 C  CB  . ILE   Q  221 ? 2.3060 1.0440 1.6738 0.1716  -0.4538 -0.0849 219 ILE   Q CB  
30160 C  CG1 . ILE   Q  221 ? 2.3037 1.1112 1.6277 0.1754  -0.4329 -0.1116 219 ILE   Q CG1 
30161 C  CG2 . ILE   Q  221 ? 2.2731 1.0572 1.6541 0.1297  -0.4588 -0.1131 219 ILE   Q CG2 
30162 C  CD1 . ILE   Q  221 ? 2.3037 1.1393 1.6224 0.1807  -0.4248 -0.1085 219 ILE   Q CD1 
30163 N  N   . VAL   Q  222 ? 2.3948 0.8444 1.9157 0.1782  -0.4928 -0.0626 220 VAL   Q N   
30164 C  CA  . VAL   Q  222 ? 2.4270 0.8928 1.8642 0.1918  -0.5470 -0.1379 220 VAL   Q CA  
30165 C  C   . VAL   Q  222 ? 2.4424 0.8969 1.9356 0.1361  -0.5465 -0.1852 220 VAL   Q C   
30166 O  O   . VAL   Q  222 ? 2.4478 0.9557 1.9359 0.1444  -0.5737 -0.2727 220 VAL   Q O   
30167 C  CB  . VAL   Q  222 ? 2.4719 0.7781 1.8366 0.2087  -0.5355 -0.1689 220 VAL   Q CB  
30168 C  CG1 . VAL   Q  222 ? 2.5059 0.8323 1.7576 0.2262  -0.5486 -0.1530 220 VAL   Q CG1 
30169 C  CG2 . VAL   Q  222 ? 2.4787 0.7786 1.8632 0.1880  -0.5426 -0.1865 220 VAL   Q CG2 
30170 N  N   . ALA   Q  223 ? 2.4153 0.8924 1.9614 0.1046  -0.5764 -0.2297 221 ALA   Q N   
30171 C  CA  . ALA   Q  223 ? 2.4120 0.8686 1.9485 0.1244  -0.5612 -0.2582 221 ALA   Q CA  
30172 C  C   . ALA   Q  223 ? 2.4470 0.9724 1.9443 0.1383  -0.6194 -0.1820 221 ALA   Q C   
30173 O  O   . ALA   Q  223 ? 2.5116 0.8818 1.9555 0.1831  -0.5882 -0.2210 221 ALA   Q O   
30174 C  CB  . ALA   Q  223 ? 2.3568 0.7655 1.9478 0.1043  -0.5699 -0.2867 221 ALA   Q CB  
30175 N  N   . LEU   Q  224 ? 2.5017 1.0289 1.9527 0.1949  -0.5554 -0.1713 222 LEU   Q N   
30176 C  CA  . LEU   Q  224 ? 2.5242 1.2141 1.9410 0.1652  -0.6042 -0.1358 222 LEU   Q CA  
30177 C  C   . LEU   Q  224 ? 2.5259 1.3409 1.9866 0.1540  -0.6076 -0.0841 222 LEU   Q C   
30178 O  O   . LEU   Q  224 ? 2.5356 1.5124 1.9404 0.1108  -0.5952 -0.1035 222 LEU   Q O   
30179 C  CB  . LEU   Q  224 ? 2.4927 1.2778 1.8659 0.1362  -0.5271 -0.1265 222 LEU   Q CB  
30180 C  CG  . LEU   Q  224 ? 2.5295 1.2874 1.7924 0.1387  -0.5424 -0.1106 222 LEU   Q CG  
30181 C  CD1 . LEU   Q  224 ? 2.4714 1.2471 1.7545 0.1411  -0.4789 -0.0683 222 LEU   Q CD1 
30182 C  CD2 . LEU   Q  224 ? 2.5438 1.3331 1.7057 0.1357  -0.5038 -0.1277 222 LEU   Q CD2 
30183 N  N   . SER   Q  225 ? 2.5724 1.4578 2.0982 0.1834  -0.6760 -0.0410 223 SER   Q N   
30184 C  CA  . SER   Q  225 ? 2.5887 1.4680 2.1350 0.1687  -0.6665 -0.0210 223 SER   Q CA  
30185 C  C   . SER   Q  225 ? 2.6973 1.4564 2.1362 0.1204  -0.6544 -0.0194 223 SER   Q C   
30186 O  O   . SER   Q  225 ? 2.7273 1.4158 2.1237 0.0438  -0.6160 -0.1006 223 SER   Q O   
30187 C  CB  . SER   Q  225 ? 2.5392 1.6049 2.1557 0.1457  -0.7172 -0.0274 223 SER   Q CB  
30188 O  OG  . SER   Q  225 ? 2.5110 1.6742 2.1528 0.1357  -0.7996 -0.0662 223 SER   Q OG  
30189 N  N   . SER   Q  226 ? 2.7286 1.3919 2.1214 0.1361  -0.6552 0.0225  224 SER   Q N   
30190 C  CA  . SER   Q  226 ? 2.8028 1.3758 2.1374 0.1977  -0.6564 0.0396  224 SER   Q CA  
30191 C  C   . SER   Q  226 ? 2.8713 1.3211 2.1248 0.2238  -0.6685 0.0633  224 SER   Q C   
30192 O  O   . SER   Q  226 ? 2.9574 1.1070 2.0108 0.2464  -0.6966 0.2151  224 SER   Q O   
30193 C  CB  . SER   Q  226 ? 2.7518 1.4550 2.2187 0.2304  -0.6608 0.0191  224 SER   Q CB  
30194 O  OG  . SER   Q  226 ? 2.7035 1.6088 2.2440 0.2493  -0.6113 -0.0793 224 SER   Q OG  
30195 N  N   . GLU   Q  227 ? 2.8377 1.4346 2.1757 0.2366  -0.7318 0.0276  225 GLU   Q N   
30196 C  CA  . GLU   Q  227 ? 2.8812 1.4957 2.2110 0.1712  -0.7028 -0.1105 225 GLU   Q CA  
30197 C  C   . GLU   Q  227 ? 2.8758 1.4518 2.1465 0.1804  -0.7038 -0.1833 225 GLU   Q C   
30198 O  O   . GLU   Q  227 ? 2.9193 1.4332 2.0735 0.1217  -0.7964 -0.2480 225 GLU   Q O   
30199 C  CB  . GLU   Q  227 ? 2.8538 1.5286 2.2357 0.1650  -0.6947 -0.0874 225 GLU   Q CB  
30200 C  CG  . GLU   Q  227 ? 2.8674 1.5489 2.3061 0.1371  -0.6918 -0.1187 225 GLU   Q CG  
30201 C  CD  . GLU   Q  227 ? 2.7469 1.5579 2.4294 0.0872  -0.6409 -0.1353 225 GLU   Q CD  
30202 O  OE1 . GLU   Q  227 ? 2.7735 1.6942 2.4041 0.1075  -0.5982 -0.1847 225 GLU   Q OE1 
30203 O  OE2 . GLU   Q  227 ? 2.8014 1.4300 2.4353 0.0279  -0.7447 -0.2096 225 GLU   Q OE2 
30204 N  N   . GLU   Q  228 ? 2.8109 1.5112 2.1973 0.1335  -0.6959 -0.1639 226 GLU   Q N   
30205 C  CA  . GLU   Q  228 ? 2.8240 1.4683 2.1447 0.1456  -0.6671 -0.1860 226 GLU   Q CA  
30206 C  C   . GLU   Q  228 ? 2.8819 1.4028 2.1624 0.1559  -0.6450 -0.2423 226 GLU   Q C   
30207 O  O   . GLU   Q  228 ? 2.9601 1.2335 2.0553 0.1592  -0.7009 -0.3004 226 GLU   Q O   
30208 C  CB  . GLU   Q  228 ? 2.7195 1.4618 2.1088 0.1491  -0.6019 -0.1911 226 GLU   Q CB  
30209 C  CG  . GLU   Q  228 ? 2.6443 1.4729 2.0812 0.1550  -0.5757 -0.2188 226 GLU   Q CG  
30210 C  CD  . GLU   Q  228 ? 2.5571 1.4420 2.0872 0.1715  -0.5191 -0.2118 226 GLU   Q CD  
30211 O  OE1 . GLU   Q  228 ? 2.5604 1.4050 2.0925 0.1359  -0.4356 -0.2707 226 GLU   Q OE1 
30212 O  OE2 . GLU   Q  228 ? 2.5354 1.3723 2.1158 0.1717  -0.5517 -0.1679 226 GLU   Q OE2 
30213 N  N   . ILE   Q  229 ? 2.9224 1.3174 2.2105 0.1348  -0.6385 -0.2202 227 ILE   Q N   
30214 C  CA  . ILE   Q  229 ? 2.9158 1.2641 2.1985 0.1237  -0.6003 -0.2514 227 ILE   Q CA  
30215 C  C   . ILE   Q  229 ? 2.9230 1.4013 2.1619 0.1038  -0.5999 -0.3398 227 ILE   Q C   
30216 O  O   . ILE   Q  229 ? 2.9508 1.4804 2.2382 0.0748  -0.5565 -0.4811 227 ILE   Q O   
30217 C  CB  . ILE   Q  229 ? 2.8877 1.2218 2.2031 0.0854  -0.6145 -0.2188 227 ILE   Q CB  
30218 C  CG1 . ILE   Q  229 ? 2.8599 1.1740 2.1499 0.0986  -0.6238 -0.1662 227 ILE   Q CG1 
30219 C  CG2 . ILE   Q  229 ? 2.8248 1.3254 2.1764 0.1139  -0.6373 -0.2077 227 ILE   Q CG2 
30220 C  CD1 . ILE   Q  229 ? 2.8163 1.1482 2.1692 0.1081  -0.6032 -0.1109 227 ILE   Q CD1 
30221 N  N   . ASN   Q  230 ? 2.9231 1.4635 2.0711 0.1168  -0.6214 -0.3221 228 ASN   Q N   
30222 C  CA  . ASN   Q  230 ? 2.8936 1.4911 2.0533 0.1028  -0.6413 -0.3142 228 ASN   Q CA  
30223 C  C   . ASN   Q  230 ? 2.9830 1.4272 1.9977 0.1277  -0.6878 -0.2271 228 ASN   Q C   
30224 O  O   . ASN   Q  230 ? 2.9961 1.5078 2.0378 0.1381  -0.7003 -0.3249 228 ASN   Q O   
30225 C  CB  . ASN   Q  230 ? 2.8811 1.5247 1.9995 0.0765  -0.6502 -0.3317 228 ASN   Q CB  
30226 C  CG  . ASN   Q  230 ? 2.7831 1.6069 2.0080 0.0201  -0.6396 -0.3802 228 ASN   Q CG  
30227 O  OD1 . ASN   Q  230 ? 2.8320 1.5864 2.0879 -0.0305 -0.5684 -0.4604 228 ASN   Q OD1 
30228 N  ND2 . ASN   Q  230 ? 2.7669 1.6865 1.9812 0.0721  -0.6564 -0.3815 228 ASN   Q ND2 
30229 N  N   . GLN   Q  231 ? 3.0143 1.4534 1.9769 0.1645  -0.7285 -0.1705 229 GLN   Q N   
30230 C  CA  . GLN   Q  231 ? 3.0860 1.3930 1.9732 0.1095  -0.7210 -0.1464 229 GLN   Q CA  
30231 C  C   . GLN   Q  231 ? 3.1071 1.2959 1.8416 0.1046  -0.7533 -0.1142 229 GLN   Q C   
30232 O  O   . GLN   Q  231 ? 3.2094 1.2729 1.7531 0.1130  -0.7293 -0.0333 229 GLN   Q O   
30233 C  CB  . GLN   Q  231 ? 3.0385 1.3892 2.0370 0.0753  -0.6742 -0.1394 229 GLN   Q CB  
30234 C  CG  . GLN   Q  231 ? 3.0127 1.3633 2.1299 0.0430  -0.6673 -0.1345 229 GLN   Q CG  
30235 C  CD  . GLN   Q  231 ? 2.9889 1.3483 2.1695 -0.0156 -0.6462 -0.1578 229 GLN   Q CD  
30236 O  OE1 . GLN   Q  231 ? 2.9872 1.3881 2.1035 -0.0264 -0.6127 -0.2156 229 GLN   Q OE1 
30237 N  NE2 . GLN   Q  231 ? 2.9592 1.3759 2.2553 -0.0315 -0.6546 -0.1664 229 GLN   Q NE2 
30238 N  N   . TYR   Q  232 ? 3.2197 1.2459 1.8314 0.0220  -0.7666 -0.1303 230 TYR   Q N   
30239 C  CA  . TYR   Q  232 ? 3.2030 1.3070 1.8515 -0.0096 -0.8043 -0.2085 230 TYR   Q CA  
30240 C  C   . TYR   Q  232 ? 3.3016 1.3086 1.8929 -0.0349 -0.8340 -0.2533 230 TYR   Q C   
30241 O  O   . TYR   Q  232 ? 3.3410 1.5636 1.7833 -0.0171 -0.8300 -0.3601 230 TYR   Q O   
30242 C  CB  . TYR   Q  232 ? 3.1995 1.1944 1.9087 -0.0442 -0.7790 -0.2275 230 TYR   Q CB  
30243 C  CG  . TYR   Q  232 ? 3.1897 1.1393 1.8538 0.0368  -0.7883 -0.2098 230 TYR   Q CG  
30244 C  CD1 . TYR   Q  232 ? 3.2082 1.1338 1.7730 0.0124  -0.7899 -0.1975 230 TYR   Q CD1 
30245 C  CD2 . TYR   Q  232 ? 3.2092 1.0142 1.8151 -0.0062 -0.8426 -0.1592 230 TYR   Q CD2 
30246 C  CE1 . TYR   Q  232 ? 3.1821 1.0425 1.7013 0.0902  -0.8251 -0.2309 230 TYR   Q CE1 
30247 C  CE2 . TYR   Q  232 ? 3.2018 0.9555 1.7736 0.0473  -0.8563 -0.1843 230 TYR   Q CE2 
30248 C  CZ  . TYR   Q  232 ? 3.1995 1.0403 1.7355 0.1075  -0.8530 -0.2190 230 TYR   Q CZ  
30249 O  OH  . TYR   Q  232 ? 3.1659 1.1320 1.7188 0.0710  -0.8265 -0.1529 230 TYR   Q OH  
30250 N  N   . VAL   Q  233 ? 3.2865 1.2717 1.9916 -0.0762 -0.8584 -0.1983 231 VAL   Q N   
30251 C  CA  . VAL   Q  233 ? 3.2653 1.2514 2.0237 -0.0731 -0.8985 -0.1962 231 VAL   Q CA  
30252 C  C   . VAL   Q  233 ? 3.2330 1.0368 2.0664 -0.1049 -0.8954 -0.1693 231 VAL   Q C   
30253 O  O   . VAL   Q  233 ? 3.2257 1.0643 2.0405 -0.0537 -0.9044 -0.1071 231 VAL   Q O   
30254 C  CB  . VAL   Q  233 ? 3.2495 1.2112 2.0887 -0.0907 -0.8927 -0.1271 231 VAL   Q CB  
30255 C  CG1 . VAL   Q  233 ? 3.2385 1.2267 2.0834 -0.1483 -0.9247 -0.1509 231 VAL   Q CG1 
30256 C  CG2 . VAL   Q  233 ? 3.2488 1.2357 2.0331 -0.0522 -0.8217 -0.1108 231 VAL   Q CG2 
30257 N  N   . THR   Q  234 ? 3.1922 0.9763 2.0561 -0.1361 -0.8901 -0.1985 232 THR   Q N   
30258 C  CA  . THR   Q  234 ? 3.1412 0.9653 2.0318 -0.0820 -0.9181 -0.1682 232 THR   Q CA  
30259 C  C   . THR   Q  234 ? 3.2440 1.1282 2.0347 -0.1055 -0.8638 -0.2406 232 THR   Q C   
30260 O  O   . THR   Q  234 ? 3.3053 1.2838 1.9881 -0.1470 -0.8544 -0.3565 232 THR   Q O   
30261 C  CB  . THR   Q  234 ? 3.1349 0.8864 1.9287 -0.1473 -0.9564 -0.1439 232 THR   Q CB  
30262 O  OG1 . THR   Q  234 ? 2.9860 0.7551 1.9138 -0.1150 -1.0280 -0.0694 232 THR   Q OG1 
30263 C  CG2 . THR   Q  234 ? 3.1309 0.8417 1.9259 -0.1163 -0.9861 -0.1180 232 THR   Q CG2 
30264 N  N   . GLN   Q  235 ? 3.2118 1.1681 2.0884 -0.1059 -0.8083 -0.2381 233 GLN   Q N   
30265 C  CA  . GLN   Q  235 ? 3.2707 1.3389 2.1061 -0.0824 -0.7687 -0.2705 233 GLN   Q CA  
30266 C  C   . GLN   Q  235 ? 3.2503 1.3415 2.1712 -0.0620 -0.7288 -0.3919 233 GLN   Q C   
30267 O  O   . GLN   Q  235 ? 3.3542 1.4164 2.0949 -0.1409 -0.7877 -0.4778 233 GLN   Q O   
30268 C  CB  . GLN   Q  235 ? 3.1867 1.3151 2.1502 -0.0225 -0.7486 -0.1506 233 GLN   Q CB  
30269 C  CG  . GLN   Q  235 ? 3.1893 1.3885 2.1542 0.0256  -0.7381 -0.1178 233 GLN   Q CG  
30270 C  CD  . GLN   Q  235 ? 3.0994 1.3994 2.1991 0.0366  -0.7037 -0.0530 233 GLN   Q CD  
30271 O  OE1 . GLN   Q  235 ? 3.0866 1.4746 2.2798 0.0623  -0.6255 -0.0404 233 GLN   Q OE1 
30272 N  NE2 . GLN   Q  235 ? 3.0837 1.4397 2.2107 0.0830  -0.7270 0.0294  233 GLN   Q NE2 
30273 N  N   . ILE   Q  236 ? 3.2385 1.5167 2.1586 -0.0975 -0.6940 -0.3975 234 ILE   Q N   
30274 C  CA  . ILE   Q  236 ? 3.1465 1.5967 2.1905 -0.0827 -0.6475 -0.4375 234 ILE   Q CA  
30275 C  C   . ILE   Q  236 ? 3.2058 1.6409 2.1412 -0.0929 -0.6261 -0.5513 234 ILE   Q C   
30276 O  O   . ILE   Q  236 ? 3.1924 1.7240 2.1136 -0.1352 -0.5797 -0.6432 234 ILE   Q O   
30277 C  CB  . ILE   Q  236 ? 3.0297 1.6580 2.1956 -0.0915 -0.6424 -0.4243 234 ILE   Q CB  
30278 C  CG1 . ILE   Q  236 ? 2.9615 1.6470 2.1801 -0.0642 -0.6290 -0.4391 234 ILE   Q CG1 
30279 C  CG2 . ILE   Q  236 ? 2.9765 1.7247 2.2382 -0.0723 -0.6228 -0.4068 234 ILE   Q CG2 
30280 C  CD1 . ILE   Q  236 ? 2.8926 1.6077 2.1933 -0.0576 -0.5991 -0.4482 234 ILE   Q CD1 
30281 N  N   . GLU   Q  237 ? 3.2352 1.6460 2.1862 -0.1512 -0.6459 -0.5711 235 GLU   Q N   
30282 C  CA  . GLU   Q  237 ? 3.2477 1.6566 2.2151 -0.1768 -0.6531 -0.5733 235 GLU   Q CA  
30283 C  C   . GLU   Q  237 ? 3.2735 1.7459 2.2159 -0.1653 -0.7045 -0.5948 235 GLU   Q C   
30284 O  O   . GLU   Q  237 ? 3.2512 1.7811 2.1944 -0.1583 -0.6378 -0.6411 235 GLU   Q O   
30285 C  CB  . GLU   Q  237 ? 3.2399 1.5175 2.2504 -0.2340 -0.6737 -0.5215 235 GLU   Q CB  
30286 C  CG  . GLU   Q  237 ? 3.1600 1.3781 2.2481 -0.2523 -0.6652 -0.4958 235 GLU   Q CG  
30287 C  CD  . GLU   Q  237 ? 3.1658 1.3231 2.1615 -0.2437 -0.6772 -0.4384 235 GLU   Q CD  
30288 O  OE1 . GLU   Q  237 ? 3.0764 1.4263 2.0922 -0.2089 -0.7251 -0.4502 235 GLU   Q OE1 
30289 O  OE2 . GLU   Q  237 ? 3.1522 1.2305 2.2717 -0.2264 -0.6790 -0.4772 235 GLU   Q OE2 
30290 N  N   . GLN   Q  238 ? 3.2754 1.8247 2.1310 -0.1455 -0.8237 -0.6370 236 GLN   Q N   
30291 C  CA  . GLN   Q  238 ? 3.3292 1.9474 2.1348 -0.1368 -0.9413 -0.6275 236 GLN   Q CA  
30292 C  C   . GLN   Q  238 ? 3.3331 1.9902 2.0976 -0.0572 -0.9643 -0.5534 236 GLN   Q C   
30293 O  O   . GLN   Q  238 ? 3.4320 2.2142 1.9573 0.0424  -1.0026 -0.5682 236 GLN   Q O   
30294 C  CB  . GLN   Q  238 ? 3.3543 1.9867 2.1237 -0.1677 -1.0163 -0.6259 236 GLN   Q CB  
30295 C  CG  . GLN   Q  238 ? 3.3557 2.1379 2.2049 -0.2614 -1.0124 -0.6241 236 GLN   Q CG  
30296 C  CD  . GLN   Q  238 ? 3.4071 2.2571 2.2439 -0.2745 -1.0790 -0.5615 236 GLN   Q CD  
30297 O  OE1 . GLN   Q  238 ? 3.4025 2.3271 2.2813 -0.3962 -1.1141 -0.6081 236 GLN   Q OE1 
30298 N  NE2 . GLN   Q  238 ? 3.4149 2.4066 2.2938 -0.3011 -1.1037 -0.5369 236 GLN   Q NE2 
30299 N  N   . GLU   Q  239 ? 3.2255 1.8652 2.1099 -0.0107 -0.9081 -0.4872 237 GLU   Q N   
30300 C  CA  . GLU   Q  239 ? 3.2195 1.8449 2.1341 -0.0110 -0.8845 -0.4267 237 GLU   Q CA  
30301 C  C   . GLU   Q  239 ? 3.1945 1.8968 2.2480 0.0532  -0.8476 -0.4016 237 GLU   Q C   
30302 O  O   . GLU   Q  239 ? 3.0793 2.1209 2.3403 0.0045  -0.7843 -0.3758 237 GLU   Q O   
30303 C  CB  . GLU   Q  239 ? 3.1078 1.8060 2.0670 0.0099  -0.8630 -0.3519 237 GLU   Q CB  
30304 C  CG  . GLU   Q  239 ? 3.0609 1.8057 2.0192 -0.0154 -0.8840 -0.3479 237 GLU   Q CG  
30305 C  CD  . GLU   Q  239 ? 2.9944 1.6909 1.9873 0.0460  -0.8721 -0.2821 237 GLU   Q CD  
30306 O  OE1 . GLU   Q  239 ? 2.9874 1.6991 2.0388 0.0284  -0.8604 -0.2904 237 GLU   Q OE1 
30307 O  OE2 . GLU   Q  239 ? 2.9818 1.5748 1.9013 -0.0106 -0.8951 -0.2113 237 GLU   Q OE2 
30308 N  N   . LYS   Q  240 ? 3.1973 1.8255 2.2865 0.1405  -0.8261 -0.3547 238 LYS   Q N   
30309 C  CA  . LYS   Q  240 ? 3.1719 1.8252 2.2845 0.1678  -0.7935 -0.3437 238 LYS   Q CA  
30310 C  C   . LYS   Q  240 ? 3.2494 1.7801 2.3208 0.2305  -0.8800 -0.3179 238 LYS   Q C   
30311 O  O   . LYS   Q  240 ? 3.2186 1.8953 2.3588 0.3069  -1.0033 -0.1825 238 LYS   Q O   
30312 C  CB  . LYS   Q  240 ? 3.0811 1.6238 2.2876 0.1685  -0.7948 -0.3039 238 LYS   Q CB  
30313 C  CG  . LYS   Q  240 ? 2.9824 1.5624 2.1876 0.1489  -0.7265 -0.3433 238 LYS   Q CG  
30314 C  CD  . LYS   Q  240 ? 2.9167 1.5279 2.1784 0.1489  -0.7366 -0.3263 238 LYS   Q CD  
30315 C  CE  . LYS   Q  240 ? 2.8901 1.5470 2.1053 0.1497  -0.6969 -0.3279 238 LYS   Q CE  
30316 N  NZ  . LYS   Q  240 ? 2.8661 1.5305 2.1111 0.1449  -0.6945 -0.3058 238 LYS   Q NZ  
30317 N  N   . GLN   Q  241 ? 3.2969 1.9445 2.2741 0.1980  -0.9101 -0.3788 239 GLN   Q N   
30318 C  CA  . GLN   Q  241 ? 3.2809 2.1058 2.1700 0.2201  -0.9175 -0.4671 239 GLN   Q CA  
30319 C  C   . GLN   Q  241 ? 3.3624 2.0241 2.0892 0.2638  -0.9527 -0.4710 239 GLN   Q C   
30320 O  O   . GLN   Q  241 ? 3.3725 1.9270 2.0785 0.2474  -1.0014 -0.5261 239 GLN   Q O   
30321 C  CB  . GLN   Q  241 ? 3.2868 2.2553 2.1033 0.2038  -0.9517 -0.4763 239 GLN   Q CB  
30322 C  CG  . GLN   Q  241 ? 3.1612 2.3654 2.1085 0.2185  -0.9638 -0.4826 239 GLN   Q CG  
30323 C  CD  . GLN   Q  241 ? 3.1630 2.4534 1.9948 0.2224  -1.0247 -0.4486 239 GLN   Q CD  
30324 O  OE1 . GLN   Q  241 ? 3.1654 2.4994 1.9173 0.2623  -0.9591 -0.4527 239 GLN   Q OE1 
30325 N  NE2 . GLN   Q  241 ? 3.0795 2.4995 2.0721 0.2422  -0.9699 -0.4243 239 GLN   Q NE2 
30326 N  N   . GLU   Q  242 ? 3.3592 2.0384 2.1797 0.2753  -0.8451 -0.4786 240 GLU   Q N   
30327 C  CA  . GLU   Q  242 ? 3.3137 1.9744 2.2621 0.2830  -0.8109 -0.4065 240 GLU   Q CA  
30328 C  C   . GLU   Q  242 ? 3.2897 1.9871 2.2703 0.2966  -0.7793 -0.4593 240 GLU   Q C   
30329 O  O   . GLU   Q  242 ? 3.2955 1.8970 2.2040 0.2881  -0.7570 -0.4779 240 GLU   Q O   
30330 C  CB  . GLU   Q  242 ? 3.2901 1.9030 2.1833 0.3282  -0.7646 -0.3211 240 GLU   Q CB  
30331 C  CG  . GLU   Q  242 ? 3.3172 1.8697 2.2239 0.3149  -0.7696 -0.2627 240 GLU   Q CG  
30332 C  CD  . GLU   Q  242 ? 3.3201 1.8946 2.2073 0.2639  -0.7964 -0.2037 240 GLU   Q CD  
30333 O  OE1 . GLU   Q  242 ? 3.3440 2.0044 2.2041 0.1806  -0.7726 -0.2262 240 GLU   Q OE1 
30334 O  OE2 . GLU   Q  242 ? 3.3235 1.9117 2.1189 0.2268  -0.8002 -0.1849 240 GLU   Q OE2 
30335 N  N   . ASP   R  9   ? 2.1076 1.6460 1.9711 -0.3254 -0.3242 0.2744  1   ASP   R N   
30336 C  CA  . ASP   R  9   ? 2.0930 1.5893 2.0586 -0.3113 -0.2736 0.1858  1   ASP   R CA  
30337 C  C   . ASP   R  9   ? 2.1028 1.5569 2.0829 -0.3100 -0.2468 0.1118  1   ASP   R C   
30338 O  O   . ASP   R  9   ? 2.1411 1.4822 2.1849 -0.3278 -0.0607 0.1774  1   ASP   R O   
30339 C  CB  . ASP   R  9   ? 2.1110 1.5545 2.0531 -0.3139 -0.3393 0.1393  1   ASP   R CB  
30340 C  CG  . ASP   R  9   ? 2.0642 1.4644 2.0431 -0.2756 -0.3587 0.1082  1   ASP   R CG  
30341 O  OD1 . ASP   R  9   ? 2.0509 1.3447 1.9895 -0.3019 -0.3940 0.0171  1   ASP   R OD1 
30342 O  OD2 . ASP   R  9   ? 2.2586 1.3521 2.0731 -0.3200 -0.3424 0.1422  1   ASP   R OD2 
30343 N  N   . ARG   R  10  ? 2.1033 1.5168 2.1995 -0.2848 -0.1943 -0.0152 2   ARG   R N   
30344 C  CA  . ARG   R  10  ? 2.0428 1.5206 2.1814 -0.1749 -0.1598 -0.1348 2   ARG   R CA  
30345 C  C   . ARG   R  10  ? 2.0228 1.4854 2.0921 -0.0849 -0.1059 -0.1427 2   ARG   R C   
30346 O  O   . ARG   R  10  ? 2.0959 1.3838 1.9821 -0.0670 -0.0020 -0.2078 2   ARG   R O   
30347 C  CB  . ARG   R  10  ? 2.0032 1.4765 2.2164 -0.1992 -0.2234 -0.1666 2   ARG   R CB  
30348 C  CG  . ARG   R  10  ? 2.0709 1.4581 2.1983 -0.2400 -0.2476 -0.2284 2   ARG   R CG  
30349 C  CD  . ARG   R  10  ? 2.0939 1.4041 2.2289 -0.2518 -0.2845 -0.2635 2   ARG   R CD  
30350 N  NE  . ARG   R  10  ? 2.1365 1.3727 2.2226 -0.2443 -0.2717 -0.3168 2   ARG   R NE  
30351 C  CZ  . ARG   R  10  ? 2.1985 1.2062 2.3279 -0.2423 -0.2746 -0.2921 2   ARG   R CZ  
30352 N  NH1 . ARG   R  10  ? 2.2049 1.1937 2.3546 -0.2004 -0.2588 -0.3106 2   ARG   R NH1 
30353 N  NH2 . ARG   R  10  ? 2.2424 1.2323 2.3284 -0.2225 -0.2589 -0.2954 2   ARG   R NH2 
30354 N  N   . GLY   R  11  ? 1.9246 1.4470 2.0943 -0.0551 -0.0898 -0.1174 3   GLY   R N   
30355 C  CA  . GLY   R  11  ? 1.9110 1.4035 2.0293 0.0158  -0.0302 -0.0845 3   GLY   R CA  
30356 C  C   . GLY   R  11  ? 1.9409 1.2545 1.9276 0.1016  -0.0508 -0.1235 3   GLY   R C   
30357 O  O   . GLY   R  11  ? 1.9894 1.2979 1.8070 0.1680  -0.0434 -0.0510 3   GLY   R O   
30358 N  N   . VAL   R  12  ? 1.9341 1.1857 1.7421 0.0592  -0.0227 -0.2256 4   VAL   R N   
30359 C  CA  . VAL   R  12  ? 1.8950 1.0624 1.6907 0.0651  -0.0412 -0.2876 4   VAL   R CA  
30360 C  C   . VAL   R  12  ? 1.8570 0.8848 1.6093 0.1170  -0.0094 -0.2922 4   VAL   R C   
30361 O  O   . VAL   R  12  ? 1.8676 0.8114 1.6003 0.1451  -0.0142 -0.2938 4   VAL   R O   
30362 C  CB  . VAL   R  12  ? 1.9500 1.1123 1.6753 0.0388  -0.0506 -0.2401 4   VAL   R CB  
30363 C  CG1 . VAL   R  12  ? 1.9349 1.1236 1.6787 0.0335  -0.0326 -0.2798 4   VAL   R CG1 
30364 C  CG2 . VAL   R  12  ? 1.9444 1.1700 1.7344 -0.0130 -0.0386 -0.2278 4   VAL   R CG2 
30365 N  N   . SER   R  13  ? 1.7477 0.9291 1.6423 0.0188  -0.1404 -0.2639 5   SER   R N   
30366 C  CA  . SER   R  13  ? 1.7725 0.9543 1.6887 -0.0370 -0.1750 -0.2142 5   SER   R CA  
30367 C  C   . SER   R  13  ? 1.7639 0.9691 1.6875 -0.0648 -0.2431 -0.2230 5   SER   R C   
30368 O  O   . SER   R  13  ? 1.6586 1.0604 1.8046 -0.1820 -0.3007 -0.1962 5   SER   R O   
30369 C  CB  . SER   R  13  ? 1.7080 0.9402 1.7309 -0.0919 -0.1889 -0.2112 5   SER   R CB  
30370 O  OG  . SER   R  13  ? 1.6955 0.8776 1.7284 -0.1149 -0.1651 -0.2372 5   SER   R OG  
30371 N  N   . THR   R  14  ? 1.8252 0.9689 1.6072 -0.0643 -0.2764 -0.2114 6   THR   R N   
30372 C  CA  . THR   R  14  ? 1.8705 0.9767 1.6083 -0.0522 -0.2806 -0.2014 6   THR   R CA  
30373 C  C   . THR   R  14  ? 1.8981 0.8159 1.5266 -0.0503 -0.2387 -0.1796 6   THR   R C   
30374 O  O   . THR   R  14  ? 1.8530 0.6411 1.5411 -0.0393 -0.1999 -0.2076 6   THR   R O   
30375 C  CB  . THR   R  14  ? 1.9145 1.0441 1.6464 -0.1013 -0.3399 -0.1727 6   THR   R CB  
30376 O  OG1 . THR   R  14  ? 1.9185 1.1408 1.6840 -0.0787 -0.3532 -0.1284 6   THR   R OG1 
30377 C  CG2 . THR   R  14  ? 1.9519 1.1131 1.6595 -0.0842 -0.3599 -0.1424 6   THR   R CG2 
30378 N  N   . PHE   R  15  ? 1.9001 0.7868 1.5780 -0.0202 -0.2514 -0.1681 7   PHE   R N   
30379 C  CA  . PHE   R  15  ? 1.9377 0.8417 1.5962 0.0320  -0.2238 -0.1340 7   PHE   R CA  
30380 C  C   . PHE   R  15  ? 1.9771 0.8410 1.5572 0.1073  -0.2191 -0.1947 7   PHE   R C   
30381 O  O   . PHE   R  15  ? 1.9330 0.9664 1.5082 0.1045  -0.2094 -0.2439 7   PHE   R O   
30382 C  CB  . PHE   R  15  ? 1.9575 0.8421 1.6136 0.0366  -0.2506 -0.0907 7   PHE   R CB  
30383 C  CG  . PHE   R  15  ? 1.9674 0.8570 1.6440 0.0310  -0.2167 -0.0239 7   PHE   R CG  
30384 C  CD1 . PHE   R  15  ? 1.9525 0.8317 1.6611 0.0757  -0.2047 -0.0255 7   PHE   R CD1 
30385 C  CD2 . PHE   R  15  ? 1.9861 0.8608 1.5994 0.0104  -0.2234 -0.0159 7   PHE   R CD2 
30386 C  CE1 . PHE   R  15  ? 1.8989 0.8270 1.6513 0.0878  -0.2183 -0.0085 7   PHE   R CE1 
30387 C  CE2 . PHE   R  15  ? 1.9458 0.8536 1.6022 0.0244  -0.2455 -0.0052 7   PHE   R CE2 
30388 C  CZ  . PHE   R  15  ? 1.9010 0.8335 1.6251 0.0420  -0.2518 -0.0291 7   PHE   R CZ  
30389 N  N   . SER   R  16  ? 1.9858 0.7401 1.5893 0.1359  -0.1928 -0.1324 8   SER   R N   
30390 C  CA  . SER   R  16  ? 2.0165 0.7255 1.6188 0.1328  -0.1473 -0.0648 8   SER   R CA  
30391 C  C   . SER   R  16  ? 2.0116 0.6946 1.6593 0.1340  -0.1744 -0.0630 8   SER   R C   
30392 O  O   . SER   R  16  ? 1.9767 0.5094 1.7050 0.1228  -0.1512 0.0145  8   SER   R O   
30393 C  CB  . SER   R  16  ? 2.0380 0.5228 1.6449 0.1366  -0.1189 -0.0581 8   SER   R CB  
30394 O  OG  . SER   R  16  ? 2.0409 0.3634 1.6136 0.1074  -0.0852 -0.0417 8   SER   R OG  
30395 N  N   . PRO   R  17  ? 2.0078 0.7056 1.6728 0.1979  -0.1666 -0.0521 9   PRO   R N   
30396 C  CA  . PRO   R  17  ? 2.0022 0.6768 1.7024 0.2208  -0.1771 -0.0561 9   PRO   R CA  
30397 C  C   . PRO   R  17  ? 1.9736 0.7768 1.7124 0.2634  -0.2136 -0.0859 9   PRO   R C   
30398 O  O   . PRO   R  17  ? 1.9981 0.7492 1.7140 0.2979  -0.2269 -0.0426 9   PRO   R O   
30399 C  CB  . PRO   R  17  ? 2.0375 0.6506 1.6969 0.2665  -0.1773 -0.0307 9   PRO   R CB  
30400 C  CG  . PRO   R  17  ? 2.0368 0.5959 1.6990 0.2471  -0.1677 -0.0396 9   PRO   R CG  
30401 C  CD  . PRO   R  17  ? 2.0268 0.6221 1.6527 0.2310  -0.1453 -0.0547 9   PRO   R CD  
30402 N  N   . GLU   R  18  ? 1.9859 0.8682 1.7362 0.2348  -0.1638 -0.1411 10  GLU   R N   
30403 C  CA  . GLU   R  18  ? 1.9859 0.9645 1.8772 0.2079  -0.1687 -0.1076 10  GLU   R CA  
30404 C  C   . GLU   R  18  ? 1.9934 0.9470 1.8949 0.2649  -0.1740 -0.1125 10  GLU   R C   
30405 O  O   . GLU   R  18  ? 1.9183 1.0119 1.9737 0.4392  -0.0902 -0.1094 10  GLU   R O   
30406 C  CB  . GLU   R  18  ? 2.0372 1.0067 1.8866 0.1636  -0.1407 -0.1072 10  GLU   R CB  
30407 C  CG  . GLU   R  18  ? 2.1706 1.0018 1.9263 0.1731  -0.1320 -0.0734 10  GLU   R CG  
30408 C  CD  . GLU   R  18  ? 2.2264 1.0430 1.9368 0.1166  -0.1466 -0.0533 10  GLU   R CD  
30409 O  OE1 . GLU   R  18  ? 2.4113 1.0814 1.9734 0.0949  -0.1558 -0.0073 10  GLU   R OE1 
30410 O  OE2 . GLU   R  18  ? 2.3565 1.0934 1.8866 0.1743  -0.1409 -0.0364 10  GLU   R OE2 
30411 N  N   . GLY   R  19  ? 1.9373 0.9890 1.8776 0.2644  -0.2073 -0.1033 11  GLY   R N   
30412 C  CA  . GLY   R  19  ? 1.9138 0.9989 1.8039 0.1655  -0.2614 -0.0533 11  GLY   R CA  
30413 C  C   . GLY   R  19  ? 1.8297 0.8102 1.8175 0.0977  -0.3012 -0.0920 11  GLY   R C   
30414 O  O   . GLY   R  19  ? 1.7865 0.8100 1.8366 0.1146  -0.2801 0.0673  11  GLY   R O   
30415 N  N   . ARG   R  20  ? 1.9314 0.8695 1.7224 0.1412  -0.3085 -0.0972 12  ARG   R N   
30416 C  CA  . ARG   R  20  ? 1.8855 0.8687 1.6614 0.1396  -0.3282 -0.1484 12  ARG   R CA  
30417 C  C   . ARG   R  20  ? 1.8764 0.8194 1.5794 0.1111  -0.3377 -0.1799 12  ARG   R C   
30418 O  O   . ARG   R  20  ? 1.8045 0.7589 1.5916 0.1120  -0.4371 -0.1734 12  ARG   R O   
30419 C  CB  . ARG   R  20  ? 1.8673 0.9923 1.6538 0.2002  -0.3356 -0.1537 12  ARG   R CB  
30420 C  CG  . ARG   R  20  ? 1.8656 1.1140 1.7281 0.2135  -0.3711 -0.1722 12  ARG   R CG  
30421 C  CD  . ARG   R  20  ? 1.8499 1.2075 1.7390 0.2661  -0.3822 -0.2020 12  ARG   R CD  
30422 N  NE  . ARG   R  20  ? 1.8310 1.3599 1.8186 0.3347  -0.4122 -0.2404 12  ARG   R NE  
30423 C  CZ  . ARG   R  20  ? 1.8787 1.3780 1.9009 0.3485  -0.4410 -0.2897 12  ARG   R CZ  
30424 N  NH1 . ARG   R  20  ? 1.8935 1.3979 1.9387 0.3216  -0.4157 -0.3090 12  ARG   R NH1 
30425 N  NH2 . ARG   R  20  ? 1.8872 1.4282 1.9426 0.3749  -0.4828 -0.2731 12  ARG   R NH2 
30426 N  N   . LEU   R  21  ? 1.9295 0.7951 1.5124 0.0777  -0.2857 -0.1914 13  LEU   R N   
30427 C  CA  . LEU   R  21  ? 1.9153 0.8611 1.4485 0.0557  -0.2699 -0.2058 13  LEU   R CA  
30428 C  C   . LEU   R  21  ? 1.9562 0.8106 1.3981 0.0693  -0.2019 -0.2139 13  LEU   R C   
30429 O  O   . LEU   R  21  ? 1.8547 0.7156 1.4430 0.1428  -0.1297 -0.3122 13  LEU   R O   
30430 C  CB  . LEU   R  21  ? 1.9589 0.8710 1.4015 0.0196  -0.2578 -0.1897 13  LEU   R CB  
30431 C  CG  . LEU   R  21  ? 1.9826 0.9242 1.3875 0.0077  -0.2351 -0.2103 13  LEU   R CG  
30432 C  CD1 . LEU   R  21  ? 1.9544 0.9300 1.3798 0.0248  -0.2346 -0.1967 13  LEU   R CD1 
30433 C  CD2 . LEU   R  21  ? 2.0296 0.9545 1.3567 -0.0164 -0.2295 -0.2294 13  LEU   R CD2 
30434 N  N   . PHE   R  22  ? 2.0184 0.8607 1.3636 0.0126  -0.2254 -0.1913 14  PHE   R N   
30435 C  CA  . PHE   R  22  ? 2.0737 0.8632 1.3197 0.0249  -0.2121 -0.2001 14  PHE   R CA  
30436 C  C   . PHE   R  22  ? 2.0014 0.8259 1.3014 0.0576  -0.2122 -0.2333 14  PHE   R C   
30437 O  O   . PHE   R  22  ? 1.9477 0.9099 1.3017 0.0424  -0.2141 -0.2503 14  PHE   R O   
30438 C  CB  . PHE   R  22  ? 2.1352 0.8827 1.2857 -0.0415 -0.2091 -0.2126 14  PHE   R CB  
30439 C  CG  . PHE   R  22  ? 2.2027 0.8462 1.3358 -0.0122 -0.2142 -0.2211 14  PHE   R CG  
30440 C  CD1 . PHE   R  22  ? 2.2265 0.8166 1.2940 0.0096  -0.1946 -0.1644 14  PHE   R CD1 
30441 C  CD2 . PHE   R  22  ? 2.2556 0.9275 1.3281 -0.0341 -0.2141 -0.1531 14  PHE   R CD2 
30442 C  CE1 . PHE   R  22  ? 2.2648 0.7455 1.3718 0.0483  -0.2117 -0.1810 14  PHE   R CE1 
30443 C  CE2 . PHE   R  22  ? 2.2939 0.8328 1.4036 0.0097  -0.2180 -0.1882 14  PHE   R CE2 
30444 C  CZ  . PHE   R  22  ? 2.3107 0.8129 1.3663 0.0114  -0.2255 -0.1725 14  PHE   R CZ  
30445 N  N   . GLN   R  23  ? 1.9741 0.7970 1.3183 0.0526  -0.2354 -0.1572 15  GLN   R N   
30446 C  CA  . GLN   R  23  ? 1.9414 0.7191 1.3519 0.0431  -0.1620 -0.1140 15  GLN   R CA  
30447 C  C   . GLN   R  23  ? 1.8618 0.6661 1.3008 0.1178  -0.1764 -0.1348 15  GLN   R C   
30448 O  O   . GLN   R  23  ? 1.9339 0.6384 1.2785 0.1595  -0.0556 -0.2189 15  GLN   R O   
30449 C  CB  . GLN   R  23  ? 1.9076 0.7350 1.4188 0.0241  -0.1348 -0.0987 15  GLN   R CB  
30450 C  CG  . GLN   R  23  ? 1.9629 0.7424 1.5237 -0.0560 -0.1300 -0.0833 15  GLN   R CG  
30451 C  CD  . GLN   R  23  ? 1.9270 0.5725 1.5948 -0.1182 -0.1348 -0.0981 15  GLN   R CD  
30452 O  OE1 . GLN   R  23  ? 1.9458 0.5651 1.6901 -0.0500 -0.0730 -0.2374 15  GLN   R OE1 
30453 N  NE2 . GLN   R  23  ? 1.8980 0.7272 1.5962 -0.0821 -0.1671 -0.0318 15  GLN   R NE2 
30454 N  N   . VAL   R  24  ? 1.8487 0.7027 1.2438 0.1551  -0.1970 -0.0932 16  VAL   R N   
30455 C  CA  . VAL   R  24  ? 1.8049 0.7956 1.2855 0.1722  -0.2127 -0.0826 16  VAL   R CA  
30456 C  C   . VAL   R  24  ? 1.8481 0.6848 1.3797 0.1729  -0.2487 -0.0641 16  VAL   R C   
30457 O  O   . VAL   R  24  ? 1.8076 0.5940 1.4193 0.1764  -0.2472 -0.0142 16  VAL   R O   
30458 C  CB  . VAL   R  24  ? 1.7705 0.9746 1.2887 0.1684  -0.2208 -0.0848 16  VAL   R CB  
30459 C  CG1 . VAL   R  24  ? 1.7956 1.0472 1.2811 0.1643  -0.1936 -0.0877 16  VAL   R CG1 
30460 C  CG2 . VAL   R  24  ? 1.7222 1.0125 1.3208 0.1963  -0.2069 -0.0830 16  VAL   R CG2 
30461 N  N   . GLU   R  25  ? 1.9140 0.7045 1.4548 0.1371  -0.2580 -0.0247 17  GLU   R N   
30462 C  CA  . GLU   R  25  ? 1.9739 0.7086 1.5777 0.1288  -0.2374 -0.0742 17  GLU   R CA  
30463 C  C   . GLU   R  25  ? 2.0033 0.6262 1.5318 0.1554  -0.2098 -0.0723 17  GLU   R C   
30464 O  O   . GLU   R  25  ? 1.9944 0.4803 1.5498 0.1512  -0.1864 -0.0315 17  GLU   R O   
30465 C  CB  . GLU   R  25  ? 2.0257 0.6882 1.6761 0.1079  -0.2301 -0.0497 17  GLU   R CB  
30466 C  CG  . GLU   R  25  ? 1.9940 0.7933 1.7826 0.0712  -0.2443 -0.0953 17  GLU   R CG  
30467 C  CD  . GLU   R  25  ? 2.0108 0.8715 1.9210 0.0999  -0.1792 -0.1026 17  GLU   R CD  
30468 O  OE1 . GLU   R  25  ? 1.8757 0.9333 1.9834 0.0622  -0.1023 -0.0945 17  GLU   R OE1 
30469 O  OE2 . GLU   R  25  ? 2.0158 0.8624 2.0237 0.0436  -0.1780 -0.1866 17  GLU   R OE2 
30470 N  N   . TYR   R  26  ? 2.0104 0.6990 1.5273 0.1589  -0.1752 -0.1113 18  TYR   R N   
30471 C  CA  . TYR   R  26  ? 2.0658 0.7002 1.4846 0.1663  -0.1424 -0.1803 18  TYR   R CA  
30472 C  C   . TYR   R  26  ? 2.0652 0.7641 1.4298 0.1792  -0.1376 -0.1822 18  TYR   R C   
30473 O  O   . TYR   R  26  ? 2.0778 0.5523 1.4587 0.2587  -0.0942 -0.2005 18  TYR   R O   
30474 C  CB  . TYR   R  26  ? 2.0895 0.6795 1.4625 0.1593  -0.1135 -0.1649 18  TYR   R CB  
30475 C  CG  . TYR   R  26  ? 2.1410 0.5814 1.5069 0.1481  -0.1230 -0.1853 18  TYR   R CG  
30476 C  CD1 . TYR   R  26  ? 2.1333 0.5748 1.4715 0.1274  -0.1383 -0.1602 18  TYR   R CD1 
30477 C  CD2 . TYR   R  26  ? 2.1388 0.5165 1.5390 0.1377  -0.1215 -0.1737 18  TYR   R CD2 
30478 C  CE1 . TYR   R  26  ? 2.1668 0.5761 1.5051 0.1329  -0.1788 -0.1304 18  TYR   R CE1 
30479 C  CE2 . TYR   R  26  ? 2.1466 0.5283 1.5412 0.1076  -0.1550 -0.1672 18  TYR   R CE2 
30480 C  CZ  . TYR   R  26  ? 2.1684 0.5406 1.5071 0.0945  -0.1781 -0.0868 18  TYR   R CZ  
30481 O  OH  . TYR   R  26  ? 2.1773 0.4472 1.6497 0.0494  -0.1888 -0.0644 18  TYR   R OH  
30482 N  N   . SER   R  27  ? 2.0507 0.8123 1.4363 0.1138  -0.1512 -0.2293 19  SER   R N   
30483 C  CA  . SER   R  27  ? 2.0185 0.9513 1.3802 0.0998  -0.1418 -0.1955 19  SER   R CA  
30484 C  C   . SER   R  27  ? 1.9974 0.9863 1.4072 0.0928  -0.1502 -0.1620 19  SER   R C   
30485 O  O   . SER   R  27  ? 2.0226 1.1564 1.4057 0.0082  -0.1789 -0.1369 19  SER   R O   
30486 C  CB  . SER   R  27  ? 1.9860 0.9887 1.4048 0.1621  -0.1161 -0.2313 19  SER   R CB  
30487 O  OG  . SER   R  27  ? 1.9484 1.0849 1.4533 0.1721  -0.0996 -0.2852 19  SER   R OG  
30488 N  N   . LEU   R  28  ? 2.0340 0.8830 1.4602 0.1232  -0.1389 -0.1294 20  LEU   R N   
30489 C  CA  . LEU   R  28  ? 2.0353 0.8040 1.4990 0.1558  -0.1469 -0.1230 20  LEU   R CA  
30490 C  C   . LEU   R  28  ? 2.0970 0.7407 1.5397 0.1590  -0.1443 -0.1180 20  LEU   R C   
30491 O  O   . LEU   R  28  ? 2.1207 0.3852 1.5377 0.1446  -0.1377 -0.1742 20  LEU   R O   
30492 C  CB  . LEU   R  28  ? 2.0047 0.8790 1.5824 0.1596  -0.1725 -0.1057 20  LEU   R CB  
30493 C  CG  . LEU   R  28  ? 1.9656 0.9017 1.6720 0.1511  -0.1596 -0.1183 20  LEU   R CG  
30494 C  CD1 . LEU   R  28  ? 1.9217 0.9274 1.6442 0.1646  -0.1717 -0.0879 20  LEU   R CD1 
30495 C  CD2 . LEU   R  28  ? 1.9569 0.9254 1.6982 0.1445  -0.1763 -0.0999 20  LEU   R CD2 
30496 N  N   . GLU   R  29  ? 2.0648 0.8662 1.5797 0.1334  -0.1261 -0.1101 21  GLU   R N   
30497 C  CA  . GLU   R  29  ? 2.1132 0.9930 1.5560 0.1823  -0.1506 -0.1650 21  GLU   R CA  
30498 C  C   . GLU   R  29  ? 2.0521 0.9345 1.5446 0.1695  -0.0990 -0.1459 21  GLU   R C   
30499 O  O   . GLU   R  29  ? 2.1085 1.1117 1.4884 0.0675  -0.1067 -0.1486 21  GLU   R O   
30500 C  CB  . GLU   R  29  ? 2.1155 1.0222 1.5850 0.2003  -0.1407 -0.1370 21  GLU   R CB  
30501 C  CG  . GLU   R  29  ? 2.1520 1.0777 1.6290 0.2643  -0.1769 -0.1514 21  GLU   R CG  
30502 C  CD  . GLU   R  29  ? 2.1619 1.1658 1.6459 0.2930  -0.2026 -0.2050 21  GLU   R CD  
30503 O  OE1 . GLU   R  29  ? 2.1812 1.2972 1.7810 0.3021  -0.2633 -0.1465 21  GLU   R OE1 
30504 O  OE2 . GLU   R  29  ? 2.1883 1.2422 1.6767 0.3026  -0.2126 -0.2901 21  GLU   R OE2 
30505 N  N   . ALA   R  30  ? 2.0206 0.8405 1.5378 0.1271  -0.1115 -0.1065 22  ALA   R N   
30506 C  CA  . ALA   R  30  ? 1.9606 0.8066 1.5377 0.1319  -0.0961 -0.1247 22  ALA   R CA  
30507 C  C   . ALA   R  30  ? 1.9411 0.7799 1.5435 0.1541  -0.0972 -0.1214 22  ALA   R C   
30508 O  O   . ALA   R  30  ? 1.9472 0.6905 1.5413 0.2166  -0.0866 -0.1562 22  ALA   R O   
30509 C  CB  . ALA   R  30  ? 1.9119 0.8604 1.5211 0.1208  -0.0841 -0.1354 22  ALA   R CB  
30510 N  N   . ILE   R  31  ? 1.9265 0.8080 1.5097 0.1461  -0.0946 -0.0858 23  ILE   R N   
30511 C  CA  . ILE   R  31  ? 1.9315 0.8075 1.4675 0.1261  -0.1209 -0.0781 23  ILE   R CA  
30512 C  C   . ILE   R  31  ? 1.9759 0.7800 1.4636 0.1152  -0.0945 -0.0680 23  ILE   R C   
30513 O  O   . ILE   R  31  ? 1.9617 0.7275 1.4400 0.1296  -0.1162 -0.0819 23  ILE   R O   
30514 C  CB  . ILE   R  31  ? 1.9038 0.8127 1.4576 0.0988  -0.1205 -0.0437 23  ILE   R CB  
30515 C  CG1 . ILE   R  31  ? 1.8656 0.8051 1.4802 0.0746  -0.1183 -0.0460 23  ILE   R CG1 
30516 C  CG2 . ILE   R  31  ? 1.9148 0.7776 1.4238 0.1100  -0.1088 -0.0632 23  ILE   R CG2 
30517 C  CD1 . ILE   R  31  ? 1.8590 0.8580 1.4940 0.0589  -0.1317 -0.0321 23  ILE   R CD1 
30518 N  N   . LYS   R  32  ? 2.0375 0.8004 1.4739 0.1043  -0.1094 -0.0362 24  LYS   R N   
30519 C  CA  . LYS   R  32  ? 2.0619 0.8409 1.4411 0.1011  -0.1152 -0.0612 24  LYS   R CA  
30520 C  C   . LYS   R  32  ? 2.1292 0.7972 1.3660 0.0915  -0.0709 -0.0652 24  LYS   R C   
30521 O  O   . LYS   R  32  ? 2.1106 0.7208 1.3257 0.0777  -0.0756 -0.0296 24  LYS   R O   
30522 C  CB  . LYS   R  32  ? 2.0954 0.8698 1.4804 0.1306  -0.1447 -0.0412 24  LYS   R CB  
30523 C  CG  . LYS   R  32  ? 2.0926 0.9048 1.5078 0.1260  -0.1596 -0.0142 24  LYS   R CG  
30524 C  CD  . LYS   R  32  ? 2.1253 0.9053 1.5259 0.1050  -0.1591 0.0012  24  LYS   R CD  
30525 C  CE  . LYS   R  32  ? 2.1039 0.9145 1.5199 0.1015  -0.1581 0.0333  24  LYS   R CE  
30526 N  NZ  . LYS   R  32  ? 2.1075 0.9247 1.5214 0.0913  -0.1788 0.0396  24  LYS   R NZ  
30527 N  N   . LEU   R  33  ? 2.1246 0.8925 1.3716 0.0324  -0.1319 -0.0612 25  LEU   R N   
30528 C  CA  . LEU   R  33  ? 2.2342 0.9342 1.3554 0.0142  -0.1501 -0.0806 25  LEU   R CA  
30529 C  C   . LEU   R  33  ? 2.2109 0.8073 1.3665 0.0147  -0.1900 -0.1455 25  LEU   R C   
30530 O  O   . LEU   R  33  ? 2.2378 0.5537 1.3767 0.0397  -0.2089 -0.1494 25  LEU   R O   
30531 C  CB  . LEU   R  33  ? 2.2499 1.1127 1.3969 0.0022  -0.1377 -0.0561 25  LEU   R CB  
30532 C  CG  . LEU   R  33  ? 2.3508 1.1150 1.4540 0.0225  -0.1478 -0.0257 25  LEU   R CG  
30533 C  CD1 . LEU   R  33  ? 2.3448 1.2186 1.5220 0.0202  -0.1541 -0.0273 25  LEU   R CD1 
30534 C  CD2 . LEU   R  33  ? 2.3160 1.0437 1.4484 0.0663  -0.1179 0.0183  25  LEU   R CD2 
30535 N  N   . GLY   R  34  ? 2.1922 0.8065 1.3921 0.0371  -0.1876 -0.1646 26  GLY   R N   
30536 C  CA  . GLY   R  34  ? 2.1480 0.7925 1.3331 0.0948  -0.1683 -0.1876 26  GLY   R CA  
30537 C  C   . GLY   R  34  ? 2.1634 0.7473 1.2917 0.1223  -0.1762 -0.1884 26  GLY   R C   
30538 O  O   . GLY   R  34  ? 2.1335 0.8250 1.1947 0.1618  -0.1146 -0.2755 26  GLY   R O   
30539 N  N   . SER   R  35  ? 2.1405 0.6886 1.3177 0.1552  -0.1722 -0.1992 27  SER   R N   
30540 C  CA  . SER   R  35  ? 2.1610 0.6765 1.3428 0.2000  -0.1525 -0.1753 27  SER   R CA  
30541 C  C   . SER   R  35  ? 2.1112 0.6927 1.3941 0.2408  -0.1482 -0.1289 27  SER   R C   
30542 O  O   . SER   R  35  ? 2.1662 0.8152 1.3009 0.2878  -0.1636 -0.1111 27  SER   R O   
30543 C  CB  . SER   R  35  ? 2.1918 0.8071 1.3429 0.1856  -0.1697 -0.1243 27  SER   R CB  
30544 O  OG  . SER   R  35  ? 2.2133 0.8056 1.3711 0.2232  -0.2090 -0.0872 27  SER   R OG  
30545 N  N   . THR   R  36  ? 2.0948 0.6751 1.4263 0.2217  -0.1503 -0.1615 28  THR   R N   
30546 C  CA  . THR   R  36  ? 2.0555 0.8224 1.4999 0.2192  -0.1094 -0.1714 28  THR   R CA  
30547 C  C   . THR   R  36  ? 2.0145 0.8569 1.4487 0.1783  -0.0766 -0.1406 28  THR   R C   
30548 O  O   . THR   R  36  ? 2.0000 1.0348 1.4475 0.1473  -0.0939 -0.0950 28  THR   R O   
30549 C  CB  . THR   R  36  ? 2.0383 0.9073 1.5990 0.2236  -0.1117 -0.2460 28  THR   R CB  
30550 O  OG1 . THR   R  36  ? 2.0478 0.9727 1.7111 0.1156  -0.1675 -0.3495 28  THR   R OG1 
30551 C  CG2 . THR   R  36  ? 2.0088 0.8850 1.6722 0.1959  -0.0797 -0.2530 28  THR   R CG2 
30552 N  N   . ALA   R  37  ? 1.9972 0.8096 1.3900 0.1888  -0.0292 -0.1352 29  ALA   R N   
30553 C  CA  . ALA   R  37  ? 1.9844 0.7740 1.3661 0.2275  0.0002  -0.1208 29  ALA   R CA  
30554 C  C   . ALA   R  37  ? 1.9586 0.7392 1.3652 0.2202  0.0312  -0.1161 29  ALA   R C   
30555 O  O   . ALA   R  37  ? 1.9137 0.7225 1.3292 0.2318  0.0352  -0.1565 29  ALA   R O   
30556 C  CB  . ALA   R  37  ? 1.9713 0.7645 1.3639 0.2445  -0.0112 -0.0993 29  ALA   R CB  
30557 N  N   . ILE   R  38  ? 1.9365 0.7449 1.4196 0.2236  0.0302  -0.0979 30  ILE   R N   
30558 C  CA  . ILE   R  38  ? 1.9412 0.7370 1.4828 0.2441  0.0143  -0.0978 30  ILE   R CA  
30559 C  C   . ILE   R  38  ? 1.9518 0.7337 1.4954 0.2503  0.0073  -0.1140 30  ILE   R C   
30560 O  O   . ILE   R  38  ? 1.9739 0.6396 1.5061 0.2152  -0.0261 -0.1525 30  ILE   R O   
30561 C  CB  . ILE   R  38  ? 1.9530 0.6953 1.5281 0.2554  0.0222  -0.0995 30  ILE   R CB  
30562 C  CG1 . ILE   R  38  ? 1.9781 0.6975 1.5333 0.2526  0.0179  -0.0792 30  ILE   R CG1 
30563 C  CG2 . ILE   R  38  ? 1.9406 0.6980 1.5606 0.2691  0.0459  -0.1165 30  ILE   R CG2 
30564 C  CD1 . ILE   R  38  ? 2.0070 0.7931 1.5164 0.2566  0.0389  -0.0855 30  ILE   R CD1 
30565 N  N   . GLY   R  39  ? 1.9368 0.7287 1.4868 0.2720  0.0143  -0.1141 31  GLY   R N   
30566 C  CA  . GLY   R  39  ? 1.9554 0.7209 1.4911 0.2696  0.0359  -0.0995 31  GLY   R CA  
30567 C  C   . GLY   R  39  ? 1.9560 0.7658 1.5489 0.2676  0.0446  -0.1012 31  GLY   R C   
30568 O  O   . GLY   R  39  ? 2.0008 0.7424 1.5041 0.2820  0.0363  -0.1413 31  GLY   R O   
30569 N  N   . ILE   R  40  ? 1.9858 0.8029 1.6276 0.2584  0.0728  -0.0719 32  ILE   R N   
30570 C  CA  . ILE   R  40  ? 1.9787 0.8140 1.6872 0.2899  0.1101  -0.0850 32  ILE   R CA  
30571 C  C   . ILE   R  40  ? 1.9643 0.7933 1.7186 0.3217  0.1025  -0.0717 32  ILE   R C   
30572 O  O   . ILE   R  40  ? 1.9607 0.7021 1.7504 0.3580  0.1404  -0.1101 32  ILE   R O   
30573 C  CB  . ILE   R  40  ? 2.0322 0.7318 1.7279 0.2918  0.1408  -0.0950 32  ILE   R CB  
30574 C  CG1 . ILE   R  40  ? 2.0550 0.7109 1.7261 0.3032  0.1569  -0.0636 32  ILE   R CG1 
30575 C  CG2 . ILE   R  40  ? 2.0249 0.6977 1.7302 0.2994  0.1606  -0.1212 32  ILE   R CG2 
30576 C  CD1 . ILE   R  40  ? 2.0934 0.7998 1.7177 0.2920  0.1907  -0.0533 32  ILE   R CD1 
30577 N  N   . ALA   R  41  ? 1.9214 0.8932 1.7406 0.3416  0.0954  -0.0479 33  ALA   R N   
30578 C  CA  . ALA   R  41  ? 1.8635 0.9060 1.7452 0.3148  0.0939  -0.0069 33  ALA   R CA  
30579 C  C   . ALA   R  41  ? 1.8437 0.9706 1.8519 0.3029  0.0798  0.0214  33  ALA   R C   
30580 O  O   . ALA   R  41  ? 1.7537 1.0434 1.9585 0.3034  0.0430  0.0370  33  ALA   R O   
30581 C  CB  . ALA   R  41  ? 1.8375 0.9159 1.7399 0.3105  0.0693  -0.0132 33  ALA   R CB  
30582 N  N   . THR   R  42  ? 1.9039 1.0294 1.8892 0.2497  0.1001  0.0426  34  THR   R N   
30583 C  CA  . THR   R  42  ? 1.9214 1.0807 1.9467 0.2227  0.1354  -0.0288 34  THR   R CA  
30584 C  C   . THR   R  42  ? 1.9431 1.1202 1.8994 0.1971  0.1670  -0.0796 34  THR   R C   
30585 O  O   . THR   R  42  ? 2.0094 1.0606 1.7602 0.1228  0.1445  -0.2004 34  THR   R O   
30586 C  CB  . THR   R  42  ? 1.9428 1.1921 1.9676 0.2152  0.1997  -0.0384 34  THR   R CB  
30587 O  OG1 . THR   R  42  ? 1.9624 1.2238 2.0372 0.2436  0.2206  -0.0103 34  THR   R OG1 
30588 C  CG2 . THR   R  42  ? 1.9427 1.1716 1.9710 0.2147  0.1797  -0.0162 34  THR   R CG2 
30589 N  N   . LYS   R  43  ? 1.9798 1.0976 1.9245 0.1475  0.1747  -0.0848 35  LYS   R N   
30590 C  CA  . LYS   R  43  ? 1.9439 1.1167 1.9016 0.1107  0.1939  -0.0604 35  LYS   R CA  
30591 C  C   . LYS   R  43  ? 1.9836 1.0647 1.8959 0.0634  0.2420  -0.0490 35  LYS   R C   
30592 O  O   . LYS   R  43  ? 1.9597 1.0744 1.8483 -0.0202 0.2799  -0.0266 35  LYS   R O   
30593 C  CB  . LYS   R  43  ? 1.9383 1.1689 1.9023 0.1192  0.1975  -0.0314 35  LYS   R CB  
30594 C  CG  . LYS   R  43  ? 1.9436 1.2099 1.9441 0.1409  0.1671  -0.0042 35  LYS   R CG  
30595 C  CD  . LYS   R  43  ? 1.9231 1.2808 2.0310 0.1353  0.1836  0.0416  35  LYS   R CD  
30596 C  CE  . LYS   R  43  ? 1.9237 1.2813 2.0636 0.1633  0.1542  0.0923  35  LYS   R CE  
30597 N  NZ  . LYS   R  43  ? 1.9346 1.2718 2.0974 0.1906  0.1318  0.0858  35  LYS   R NZ  
30598 N  N   . GLU   R  44  ? 1.9980 1.0581 1.8810 0.0819  0.2363  -0.0310 36  GLU   R N   
30599 C  CA  . GLU   R  44  ? 2.0294 1.0619 1.9361 0.1137  0.2255  -0.0109 36  GLU   R CA  
30600 C  C   . GLU   R  44  ? 2.0385 0.9835 1.9352 0.1481  0.2282  -0.0545 36  GLU   R C   
30601 O  O   . GLU   R  44  ? 2.0803 0.9700 1.9815 0.2017  0.2095  -0.0812 36  GLU   R O   
30602 C  CB  . GLU   R  44  ? 2.0183 1.1269 1.9287 0.1183  0.2378  0.0104  36  GLU   R CB  
30603 C  CG  . GLU   R  44  ? 2.0050 1.1568 1.9894 0.1259  0.2131  0.0365  36  GLU   R CG  
30604 C  CD  . GLU   R  44  ? 1.9873 1.1024 1.9917 0.1058  0.2096  0.0421  36  GLU   R CD  
30605 O  OE1 . GLU   R  44  ? 2.0456 0.8291 2.0027 0.0836  0.2169  0.0193  36  GLU   R OE1 
30606 O  OE2 . GLU   R  44  ? 1.9841 1.1488 2.0354 0.0970  0.2181  0.1050  36  GLU   R OE2 
30607 N  N   . GLY   R  45  ? 2.0338 0.8883 1.9279 0.1715  0.2177  -0.0757 37  GLY   R N   
30608 C  CA  . GLY   R  45  ? 2.0344 0.8944 1.9060 0.2046  0.2068  -0.1001 37  GLY   R CA  
30609 C  C   . GLY   R  45  ? 2.0195 0.8559 1.9207 0.2412  0.1999  -0.1180 37  GLY   R C   
30610 O  O   . GLY   R  45  ? 2.0687 0.9149 2.0557 0.3028  0.2051  -0.1139 37  GLY   R O   
30611 N  N   . VAL   R  46  ? 2.0123 0.8195 1.8648 0.2014  0.1687  -0.1373 38  VAL   R N   
30612 C  CA  . VAL   R  46  ? 2.0459 0.7432 1.7909 0.2374  0.1428  -0.1312 38  VAL   R CA  
30613 C  C   . VAL   R  46  ? 2.0923 0.7418 1.8071 0.2331  0.1068  -0.1120 38  VAL   R C   
30614 O  O   . VAL   R  46  ? 2.1464 0.7161 1.8719 0.2683  0.0162  -0.1986 38  VAL   R O   
30615 C  CB  . VAL   R  46  ? 2.0113 0.6659 1.7787 0.1820  0.1378  -0.1353 38  VAL   R CB  
30616 C  CG1 . VAL   R  46  ? 2.0009 0.6795 1.7730 0.1712  0.1424  -0.1400 38  VAL   R CG1 
30617 C  CG2 . VAL   R  46  ? 1.9639 0.6741 1.7657 0.1649  0.1685  -0.1348 38  VAL   R CG2 
30618 N  N   . VAL   R  47  ? 2.0627 0.7310 1.7597 0.3161  0.1081  -0.1012 39  VAL   R N   
30619 C  CA  . VAL   R  47  ? 2.0590 0.7043 1.7137 0.3651  0.1308  -0.1175 39  VAL   R CA  
30620 C  C   . VAL   R  47  ? 2.0542 0.6523 1.6887 0.3877  0.1028  -0.0729 39  VAL   R C   
30621 O  O   . VAL   R  47  ? 2.0528 0.4904 1.7384 0.3811  0.1467  -0.1090 39  VAL   R O   
30622 C  CB  . VAL   R  47  ? 2.1054 0.7623 1.7344 0.3854  0.1386  -0.1523 39  VAL   R CB  
30623 C  CG1 . VAL   R  47  ? 2.1292 0.7685 1.7509 0.3764  0.1251  -0.1553 39  VAL   R CG1 
30624 C  CG2 . VAL   R  47  ? 2.1137 0.7526 1.7284 0.3872  0.1545  -0.1697 39  VAL   R CG2 
30625 N  N   . LEU   R  48  ? 2.0554 0.6968 1.6143 0.3349  0.0893  -0.0160 40  LEU   R N   
30626 C  CA  . LEU   R  48  ? 2.0574 0.6838 1.5401 0.3239  0.0610  -0.0137 40  LEU   R CA  
30627 C  C   . LEU   R  48  ? 2.1099 0.6616 1.5296 0.3150  0.0702  -0.0183 40  LEU   R C   
30628 O  O   . LEU   R  48  ? 2.1650 0.5600 1.5592 0.2679  0.0644  -0.0262 40  LEU   R O   
30629 C  CB  . LEU   R  48  ? 2.0293 0.7556 1.5022 0.3240  0.0666  -0.0239 40  LEU   R CB  
30630 C  CG  . LEU   R  48  ? 1.9859 0.7879 1.4952 0.3356  0.0674  -0.0566 40  LEU   R CG  
30631 C  CD1 . LEU   R  48  ? 1.9609 0.8096 1.5326 0.3351  0.0760  -0.0752 40  LEU   R CD1 
30632 C  CD2 . LEU   R  48  ? 1.9773 0.8073 1.4602 0.3422  0.0768  -0.0474 40  LEU   R CD2 
30633 N  N   . GLY   R  49  ? 2.1203 0.6634 1.5259 0.3185  0.0676  0.0097  41  GLY   R N   
30634 C  CA  . GLY   R  49  ? 2.1311 0.7318 1.5058 0.2894  0.0528  0.0323  41  GLY   R CA  
30635 C  C   . GLY   R  49  ? 2.1040 0.7348 1.5020 0.2775  0.0122  0.0290  41  GLY   R C   
30636 O  O   . GLY   R  49  ? 2.0777 0.7939 1.5209 0.3069  0.0260  0.0561  41  GLY   R O   
30637 N  N   . VAL   R  50  ? 2.1613 0.7302 1.4132 0.2538  0.0002  0.0411  42  VAL   R N   
30638 C  CA  . VAL   R  50  ? 2.1711 0.7313 1.3965 0.2134  -0.0477 -0.0055 42  VAL   R CA  
30639 C  C   . VAL   R  50  ? 2.2088 0.6660 1.3865 0.1967  -0.0316 0.0114  42  VAL   R C   
30640 O  O   . VAL   R  50  ? 2.2516 0.4455 1.3729 0.2146  -0.0689 -0.0248 42  VAL   R O   
30641 C  CB  . VAL   R  50  ? 2.1355 0.8240 1.3581 0.2135  -0.0614 -0.0045 42  VAL   R CB  
30642 C  CG1 . VAL   R  50  ? 2.1292 0.8698 1.3714 0.1906  -0.0544 -0.0201 42  VAL   R CG1 
30643 C  CG2 . VAL   R  50  ? 2.1303 0.8710 1.3252 0.1923  -0.1028 -0.0120 42  VAL   R CG2 
30644 N  N   . GLU   R  51  ? 2.2033 0.6809 1.4926 0.1555  -0.0433 -0.0226 43  GLU   R N   
30645 C  CA  . GLU   R  51  ? 2.2041 0.7178 1.5344 0.1857  -0.0581 -0.0674 43  GLU   R CA  
30646 C  C   . GLU   R  51  ? 2.2349 0.6868 1.4772 0.2311  -0.0716 -0.0852 43  GLU   R C   
30647 O  O   . GLU   R  51  ? 2.2007 0.7291 1.5170 0.3163  -0.0615 -0.1384 43  GLU   R O   
30648 C  CB  . GLU   R  51  ? 2.2043 0.7146 1.6736 0.1729  -0.0810 -0.0557 43  GLU   R CB  
30649 C  CG  . GLU   R  51  ? 2.1907 0.7029 1.7731 0.1452  -0.1021 -0.0154 43  GLU   R CG  
30650 C  CD  . GLU   R  51  ? 2.1387 0.6548 1.8712 0.0589  -0.1399 -0.0574 43  GLU   R CD  
30651 O  OE1 . GLU   R  51  ? 2.1035 0.7639 2.0032 0.0036  -0.1765 -0.0651 43  GLU   R OE1 
30652 O  OE2 . GLU   R  51  ? 2.1435 0.6507 1.8826 0.0239  -0.1195 0.0438  43  GLU   R OE2 
30653 N  N   . LYS   R  52  ? 2.2150 0.6227 1.4682 0.2679  -0.0460 -0.0892 44  LYS   R N   
30654 C  CA  . LYS   R  52  ? 2.2181 0.5878 1.4665 0.2653  -0.0708 -0.1435 44  LYS   R CA  
30655 C  C   . LYS   R  52  ? 2.2428 0.5488 1.5157 0.2748  -0.0861 -0.1209 44  LYS   R C   
30656 O  O   . LYS   R  52  ? 2.2416 0.2227 1.4885 0.2464  -0.0972 -0.1408 44  LYS   R O   
30657 C  CB  . LYS   R  52  ? 2.2178 0.6380 1.4289 0.2465  -0.0862 -0.1685 44  LYS   R CB  
30658 C  CG  . LYS   R  52  ? 2.2066 0.6178 1.4163 0.2564  -0.1091 -0.2121 44  LYS   R CG  
30659 C  CD  . LYS   R  52  ? 2.2214 0.6523 1.4455 0.2514  -0.1295 -0.1860 44  LYS   R CD  
30660 C  CE  . LYS   R  52  ? 2.2085 0.7268 1.4777 0.2038  -0.1111 -0.1331 44  LYS   R CE  
30661 N  NZ  . LYS   R  52  ? 2.2365 0.7661 1.4969 0.2039  -0.1172 -0.1099 44  LYS   R NZ  
30662 N  N   . ARG   R  53  ? 2.3023 0.6601 1.5373 0.2842  -0.0868 -0.2044 45  ARG   R N   
30663 C  CA  . ARG   R  53  ? 2.2594 0.7566 1.5750 0.2303  -0.0929 -0.2673 45  ARG   R CA  
30664 C  C   . ARG   R  53  ? 2.2403 0.7808 1.5008 0.2464  -0.0522 -0.2930 45  ARG   R C   
30665 O  O   . ARG   R  53  ? 2.1785 0.8455 1.4981 0.2572  -0.0767 -0.4022 45  ARG   R O   
30666 C  CB  . ARG   R  53  ? 2.3120 0.7953 1.5564 0.2535  -0.0652 -0.2837 45  ARG   R CB  
30667 C  CG  . ARG   R  53  ? 2.3227 0.8208 1.5449 0.2344  -0.0435 -0.3163 45  ARG   R CG  
30668 C  CD  . ARG   R  53  ? 2.3160 0.9446 1.4964 0.2847  -0.0102 -0.3826 45  ARG   R CD  
30669 N  NE  . ARG   R  53  ? 2.3220 0.9994 1.4772 0.3253  0.0063  -0.4075 45  ARG   R NE  
30670 C  CZ  . ARG   R  53  ? 2.2904 0.9936 1.4883 0.3407  0.0156  -0.3950 45  ARG   R CZ  
30671 N  NH1 . ARG   R  53  ? 2.2505 1.1021 1.5737 0.3814  0.0330  -0.3558 45  ARG   R NH1 
30672 N  NH2 . ARG   R  53  ? 2.2885 0.8696 1.5326 0.3291  0.0180  -0.4160 45  ARG   R NH2 
30673 N  N   . ALA   R  54  ? 2.2147 0.7880 1.5414 0.2702  -0.0716 -0.2258 46  ALA   R N   
30674 C  CA  . ALA   R  54  ? 2.2264 0.7967 1.5604 0.3084  -0.0784 -0.1962 46  ALA   R CA  
30675 C  C   . ALA   R  54  ? 2.2206 0.8689 1.5904 0.2539  -0.0708 -0.1535 46  ALA   R C   
30676 O  O   . ALA   R  54  ? 2.3050 0.9087 1.6031 0.2674  -0.0128 -0.1669 46  ALA   R O   
30677 C  CB  . ALA   R  54  ? 2.1995 0.7729 1.5521 0.3417  -0.0870 -0.2108 46  ALA   R CB  
30678 N  N   . THR   R  55  ? 2.2046 0.9878 1.5927 0.2673  -0.0827 -0.1651 47  THR   R N   
30679 C  CA  . THR   R  55  ? 2.1234 1.0617 1.5855 0.2320  -0.0622 -0.2272 47  THR   R CA  
30680 C  C   . THR   R  55  ? 2.2505 1.0100 1.6361 0.1672  -0.1262 -0.2287 47  THR   R C   
30681 O  O   . THR   R  55  ? 2.1941 1.0308 1.6910 0.1092  -0.1663 -0.1453 47  THR   R O   
30682 C  CB  . THR   R  55  ? 2.0351 1.0859 1.6452 0.2819  -0.0832 -0.2349 47  THR   R CB  
30683 O  OG1 . THR   R  55  ? 1.9390 1.1067 1.5761 0.3062  -0.0279 -0.2517 47  THR   R OG1 
30684 C  CG2 . THR   R  55  ? 1.9715 1.1532 1.6339 0.2631  -0.0326 -0.2953 47  THR   R CG2 
30685 N  N   . SER   R  56  ? 2.3865 0.8828 1.6138 0.1300  -0.1396 -0.2957 48  SER   R N   
30686 C  CA  . SER   R  56  ? 2.4980 0.8435 1.5906 0.1132  -0.1020 -0.3402 48  SER   R CA  
30687 C  C   . SER   R  56  ? 2.5123 0.7610 1.5852 0.1051  -0.0817 -0.3927 48  SER   R C   
30688 O  O   . SER   R  56  ? 2.4818 0.7837 1.4158 0.1792  -0.1023 -0.5092 48  SER   R O   
30689 C  CB  . SER   R  56  ? 2.5112 0.7505 1.6685 0.1316  -0.0558 -0.3350 48  SER   R CB  
30690 O  OG  . SER   R  56  ? 2.6083 0.6537 1.6482 0.1230  -0.0323 -0.2484 48  SER   R OG  
30691 N  N   . PRO   R  57  ? 2.5719 0.9013 1.5872 0.1527  0.0179  -0.3812 49  PRO   R N   
30692 C  CA  . PRO   R  57  ? 2.5597 0.8512 1.5956 0.1720  0.0229  -0.3866 49  PRO   R CA  
30693 C  C   . PRO   R  57  ? 2.5814 0.8430 1.5929 0.1405  -0.0082 -0.3293 49  PRO   R C   
30694 O  O   . PRO   R  57  ? 2.5315 0.7337 1.6154 0.1828  -0.0501 -0.3328 49  PRO   R O   
30695 C  CB  . PRO   R  57  ? 2.6184 0.9431 1.5641 0.1658  0.0703  -0.4070 49  PRO   R CB  
30696 C  CG  . PRO   R  57  ? 2.6198 0.9894 1.5739 0.1335  0.0624  -0.4434 49  PRO   R CG  
30697 C  CD  . PRO   R  57  ? 2.5942 0.9623 1.5781 0.1276  0.0425  -0.4516 49  PRO   R CD  
30698 N  N   . LEU   R  58  ? 2.5679 0.8206 1.5639 0.2208  -0.0796 -0.3360 50  LEU   R N   
30699 C  CA  . LEU   R  58  ? 2.5960 0.8492 1.5045 0.2253  -0.1187 -0.3076 50  LEU   R CA  
30700 C  C   . LEU   R  58  ? 2.5806 0.7482 1.4496 0.2605  -0.1559 -0.2199 50  LEU   R C   
30701 O  O   . LEU   R  58  ? 2.6114 0.7144 1.4660 0.3333  -0.1750 -0.3043 50  LEU   R O   
30702 C  CB  . LEU   R  58  ? 2.5805 0.8771 1.4922 0.2402  -0.1554 -0.3759 50  LEU   R CB  
30703 C  CG  . LEU   R  58  ? 2.5937 0.9160 1.5258 0.2115  -0.1715 -0.3893 50  LEU   R CG  
30704 C  CD1 . LEU   R  58  ? 2.5745 0.9871 1.6257 0.2057  -0.1825 -0.3870 50  LEU   R CD1 
30705 C  CD2 . LEU   R  58  ? 2.6311 0.9261 1.5241 0.2322  -0.1698 -0.3806 50  LEU   R CD2 
30706 N  N   . LEU   R  59  ? 2.5356 0.7947 1.4613 0.2262  -0.1709 -0.2113 51  LEU   R N   
30707 C  CA  . LEU   R  59  ? 2.4557 0.6861 1.5108 0.2607  -0.1816 -0.1875 51  LEU   R CA  
30708 C  C   . LEU   R  59  ? 2.4237 0.6625 1.4645 0.3056  -0.1742 -0.1597 51  LEU   R C   
30709 O  O   . LEU   R  59  ? 2.4214 0.5528 1.4322 0.2731  -0.1588 -0.1676 51  LEU   R O   
30710 C  CB  . LEU   R  59  ? 2.4207 0.7803 1.4780 0.2552  -0.1999 -0.2120 51  LEU   R CB  
30711 C  CG  . LEU   R  59  ? 2.4006 0.7563 1.4945 0.2655  -0.1769 -0.2509 51  LEU   R CG  
30712 C  CD1 . LEU   R  59  ? 2.3835 0.7541 1.4838 0.2982  -0.1751 -0.2238 51  LEU   R CD1 
30713 C  CD2 . LEU   R  59  ? 2.3661 0.9038 1.4521 0.2173  -0.1430 -0.2497 51  LEU   R CD2 
30714 N  N   . GLU   R  60  ? 2.4574 0.6710 1.4439 0.2815  -0.1771 -0.0826 52  GLU   R N   
30715 C  CA  . GLU   R  60  ? 2.4639 0.7058 1.4231 0.2793  -0.1522 -0.0755 52  GLU   R CA  
30716 C  C   . GLU   R  60  ? 2.4235 0.6770 1.3697 0.2994  -0.1097 -0.0823 52  GLU   R C   
30717 O  O   . GLU   R  60  ? 2.3602 0.4964 1.3377 0.2815  -0.1601 -0.0297 52  GLU   R O   
30718 C  CB  . GLU   R  60  ? 2.5054 0.6493 1.4515 0.2546  -0.1667 -0.1191 52  GLU   R CB  
30719 C  CG  . GLU   R  60  ? 2.5391 0.6677 1.4695 0.2609  -0.1935 -0.1025 52  GLU   R CG  
30720 C  CD  . GLU   R  60  ? 2.5618 0.6939 1.4689 0.2497  -0.2048 -0.0484 52  GLU   R CD  
30721 O  OE1 . GLU   R  60  ? 2.6029 0.5985 1.4422 0.2407  -0.2056 -0.0339 52  GLU   R OE1 
30722 O  OE2 . GLU   R  60  ? 2.5292 0.7449 1.4837 0.1907  -0.2170 -0.0506 52  GLU   R OE2 
30723 N  N   . SER   R  61  ? 2.4425 0.8023 1.4616 0.3203  -0.0350 -0.0891 53  SER   R N   
30724 C  CA  . SER   R  61  ? 2.4394 0.9354 1.4832 0.2723  -0.0508 -0.1143 53  SER   R CA  
30725 C  C   . SER   R  61  ? 2.4256 0.8304 1.6131 0.3113  0.0099  -0.0857 53  SER   R C   
30726 O  O   . SER   R  61  ? 2.4386 0.9686 1.6385 0.2655  0.0023  -0.0484 53  SER   R O   
30727 C  CB  . SER   R  61  ? 2.4654 1.0181 1.5699 0.2571  0.0297  -0.1290 53  SER   R CB  
30728 O  OG  . SER   R  61  ? 2.5635 1.1706 1.7020 0.1389  0.0546  -0.0576 53  SER   R OG  
30729 N  N   . ASP   R  62  ? 2.4082 0.8354 1.5534 0.3785  -0.0399 -0.0940 54  ASP   R N   
30730 C  CA  . ASP   R  62  ? 2.3762 0.8606 1.5575 0.3896  -0.0093 -0.1492 54  ASP   R CA  
30731 C  C   . ASP   R  62  ? 2.3275 0.5563 1.5767 0.3499  -0.0787 -0.2198 54  ASP   R C   
30732 O  O   . ASP   R  62  ? 2.2928 0.3025 1.6685 0.4493  -0.0007 -0.2332 54  ASP   R O   
30733 C  CB  . ASP   R  62  ? 2.4748 0.9912 1.5721 0.3556  0.0197  -0.0989 54  ASP   R CB  
30734 C  CG  . ASP   R  62  ? 2.5443 1.1832 1.5618 0.3435  0.0049  -0.0483 54  ASP   R CG  
30735 O  OD1 . ASP   R  62  ? 2.5643 1.4613 1.7606 0.2917  0.0399  -0.0594 54  ASP   R OD1 
30736 O  OD2 . ASP   R  62  ? 2.5769 1.2616 1.6852 0.3066  0.1452  0.0553  54  ASP   R OD2 
30737 N  N   . SER   R  63  ? 2.2989 0.5730 1.4654 0.3986  -0.0354 -0.2421 55  SER   R N   
30738 C  CA  . SER   R  63  ? 2.2785 0.5400 1.4286 0.4015  -0.0774 -0.2799 55  SER   R CA  
30739 C  C   . SER   R  63  ? 2.2689 0.5770 1.3303 0.3713  0.0111  -0.3139 55  SER   R C   
30740 O  O   . SER   R  63  ? 2.2314 0.3968 1.4638 0.4764  0.0209  -0.3794 55  SER   R O   
30741 C  CB  . SER   R  63  ? 2.2897 0.5087 1.3637 0.4271  -0.1165 -0.2948 55  SER   R CB  
30742 O  OG  . SER   R  63  ? 2.2552 0.5195 1.3609 0.4182  -0.1953 -0.2192 55  SER   R OG  
30743 N  N   . ILE   R  64  ? 2.2211 0.6197 1.4236 0.3739  0.0021  -0.2467 56  ILE   R N   
30744 C  CA  . ILE   R  64  ? 2.1953 0.7214 1.4269 0.2454  -0.0114 -0.1811 56  ILE   R CA  
30745 C  C   . ILE   R  64  ? 2.1499 0.6635 1.4755 0.2417  0.0370  -0.1797 56  ILE   R C   
30746 O  O   . ILE   R  64  ? 2.1470 0.6054 1.5781 0.1597  0.0449  -0.1797 56  ILE   R O   
30747 C  CB  . ILE   R  64  ? 2.2661 0.7303 1.4161 0.2548  0.0024  -0.1725 56  ILE   R CB  
30748 C  CG1 . ILE   R  64  ? 2.3554 0.7660 1.3706 0.2070  0.0007  -0.1834 56  ILE   R CG1 
30749 C  CG2 . ILE   R  64  ? 2.2016 0.8377 1.4573 0.2447  -0.0295 -0.1375 56  ILE   R CG2 
30750 C  CD1 . ILE   R  64  ? 2.3802 0.7671 1.4080 0.1997  0.0125  -0.1998 56  ILE   R CD1 
30751 N  N   . GLU   R  65  ? 2.0362 0.6558 1.4726 0.2128  0.0125  -0.1901 57  GLU   R N   
30752 C  CA  . GLU   R  65  ? 1.9746 0.7459 1.5185 0.1475  -0.0046 -0.1458 57  GLU   R CA  
30753 C  C   . GLU   R  65  ? 1.9256 0.6773 1.5646 0.1515  0.0014  -0.0993 57  GLU   R C   
30754 O  O   . GLU   R  65  ? 1.8729 0.7279 1.5356 0.1402  -0.0046 -0.0140 57  GLU   R O   
30755 C  CB  . GLU   R  65  ? 1.9236 0.8348 1.6301 0.1788  -0.0058 -0.1789 57  GLU   R CB  
30756 C  CG  . GLU   R  65  ? 1.9166 0.9343 1.7020 0.1485  -0.0200 -0.2428 57  GLU   R CG  
30757 C  CD  . GLU   R  65  ? 1.9594 0.9154 1.7270 0.1218  -0.0336 -0.3148 57  GLU   R CD  
30758 O  OE1 . GLU   R  65  ? 1.9540 0.9841 1.7460 0.0539  -0.0482 -0.3018 57  GLU   R OE1 
30759 O  OE2 . GLU   R  65  ? 1.9664 1.0232 1.7730 0.1032  -0.0459 -0.2963 57  GLU   R OE2 
30760 N  N   . LYS   R  66  ? 1.9199 0.6837 1.5252 0.1461  -0.0123 -0.0967 58  LYS   R N   
30761 C  CA  . LYS   R  66  ? 1.9622 0.7654 1.4875 0.1157  -0.0538 -0.1197 58  LYS   R CA  
30762 C  C   . LYS   R  66  ? 1.9663 0.7446 1.4322 0.1365  -0.0690 -0.1523 58  LYS   R C   
30763 O  O   . LYS   R  66  ? 1.9270 0.6420 1.4348 0.0885  -0.0976 -0.1961 58  LYS   R O   
30764 C  CB  . LYS   R  66  ? 2.0440 0.7692 1.4514 0.1182  -0.0804 -0.1220 58  LYS   R CB  
30765 C  CG  . LYS   R  66  ? 2.0506 0.8198 1.4303 0.0963  -0.0986 -0.1398 58  LYS   R CG  
30766 C  CD  . LYS   R  66  ? 2.0934 0.8350 1.4414 0.0668  -0.0875 -0.1741 58  LYS   R CD  
30767 C  CE  . LYS   R  66  ? 2.0823 0.8755 1.4791 0.0640  -0.0822 -0.1708 58  LYS   R CE  
30768 N  NZ  . LYS   R  66  ? 2.0953 0.8634 1.5390 0.0472  -0.0713 -0.1648 58  LYS   R NZ  
30769 N  N   . ILE   R  67  ? 1.9579 0.7498 1.3670 0.1626  -0.0630 -0.1682 59  ILE   R N   
30770 C  CA  . ILE   R  67  ? 1.9053 0.7816 1.3532 0.1892  -0.0712 -0.1830 59  ILE   R CA  
30771 C  C   . ILE   R  67  ? 1.8754 0.7915 1.2873 0.2092  -0.1303 -0.1475 59  ILE   R C   
30772 O  O   . ILE   R  67  ? 1.9108 0.8191 1.3060 0.1844  -0.1587 -0.1242 59  ILE   R O   
30773 C  CB  . ILE   R  67  ? 1.9370 0.8805 1.4136 0.1673  -0.0256 -0.1970 59  ILE   R CB  
30774 C  CG1 . ILE   R  67  ? 1.9396 0.9004 1.4384 0.1952  -0.0106 -0.1833 59  ILE   R CG1 
30775 C  CG2 . ILE   R  67  ? 1.9109 0.9278 1.4483 0.1521  -0.0080 -0.1899 59  ILE   R CG2 
30776 C  CD1 . ILE   R  67  ? 1.9620 0.9585 1.4705 0.1852  0.0172  -0.1583 59  ILE   R CD1 
30777 N  N   . VAL   R  68  ? 1.8484 0.6708 1.3044 0.2650  -0.1275 -0.1353 60  VAL   R N   
30778 C  CA  . VAL   R  68  ? 1.8645 0.6774 1.2977 0.2860  -0.1435 -0.1377 60  VAL   R CA  
30779 C  C   . VAL   R  68  ? 1.8370 0.6953 1.2615 0.3165  -0.1449 -0.1624 60  VAL   R C   
30780 O  O   . VAL   R  68  ? 1.8582 0.6183 1.2540 0.3860  -0.1048 -0.1455 60  VAL   R O   
30781 C  CB  . VAL   R  68  ? 1.8459 0.6124 1.2921 0.3083  -0.1391 -0.1915 60  VAL   R CB  
30782 C  CG1 . VAL   R  68  ? 1.8531 0.6519 1.2835 0.2715  -0.1539 -0.2274 60  VAL   R CG1 
30783 C  CG2 . VAL   R  68  ? 1.8527 0.6144 1.3111 0.3263  -0.1561 -0.1854 60  VAL   R CG2 
30784 N  N   . GLU   R  69  ? 1.9007 0.6887 1.2853 0.2814  -0.1507 -0.1577 61  GLU   R N   
30785 C  CA  . GLU   R  69  ? 1.8908 0.7510 1.3474 0.2100  -0.1819 -0.1061 61  GLU   R CA  
30786 C  C   . GLU   R  69  ? 1.8551 0.7052 1.3463 0.2041  -0.1696 -0.0715 61  GLU   R C   
30787 O  O   . GLU   R  69  ? 1.8587 0.5055 1.3015 0.2255  -0.1946 0.0004  61  GLU   R O   
30788 C  CB  . GLU   R  69  ? 1.9465 0.8445 1.3438 0.2207  -0.2248 -0.0548 61  GLU   R CB  
30789 C  CG  . GLU   R  69  ? 1.9740 0.9130 1.3469 0.2015  -0.2476 -0.1082 61  GLU   R CG  
30790 C  CD  . GLU   R  69  ? 2.0463 0.9728 1.2730 0.1766  -0.2870 -0.1006 61  GLU   R CD  
30791 O  OE1 . GLU   R  69  ? 2.1462 1.0154 1.2448 0.1836  -0.2933 -0.1499 61  GLU   R OE1 
30792 O  OE2 . GLU   R  69  ? 2.0458 1.1221 1.2823 0.1528  -0.3147 -0.0744 61  GLU   R OE2 
30793 N  N   . ILE   R  70  ? 1.8631 0.7209 1.3312 0.2069  -0.1534 -0.1130 62  ILE   R N   
30794 C  CA  . ILE   R  70  ? 1.8610 0.7348 1.3090 0.2278  -0.1710 -0.0941 62  ILE   R CA  
30795 C  C   . ILE   R  70  ? 1.9132 0.7477 1.3607 0.2031  -0.2024 -0.1066 62  ILE   R C   
30796 O  O   . ILE   R  70  ? 1.8304 0.7681 1.3025 0.2117  -0.2898 -0.1012 62  ILE   R O   
30797 C  CB  . ILE   R  70  ? 1.8388 0.7141 1.3221 0.2643  -0.1401 -0.0864 62  ILE   R CB  
30798 C  CG1 . ILE   R  70  ? 1.8397 0.7127 1.3358 0.2769  -0.1368 -0.1311 62  ILE   R CG1 
30799 C  CG2 . ILE   R  70  ? 1.8135 0.7099 1.2959 0.2484  -0.1606 -0.0619 62  ILE   R CG2 
30800 C  CD1 . ILE   R  70  ? 1.8589 0.7998 1.3212 0.2643  -0.1335 -0.1095 62  ILE   R CD1 
30801 N  N   . ASP   R  71  ? 1.9458 0.7804 1.4018 0.1981  -0.1520 -0.1266 63  ASP   R N   
30802 C  CA  . ASP   R  71  ? 2.0231 0.7766 1.4182 0.2073  -0.0999 -0.1152 63  ASP   R CA  
30803 C  C   . ASP   R  71  ? 1.9703 0.6519 1.4191 0.2246  -0.1079 -0.1363 63  ASP   R C   
30804 O  O   . ASP   R  71  ? 1.8836 0.6745 1.3086 0.3452  -0.1088 -0.0878 63  ASP   R O   
30805 C  CB  . ASP   R  71  ? 2.1672 0.7755 1.4612 0.1817  -0.1021 -0.1630 63  ASP   R CB  
30806 C  CG  . ASP   R  71  ? 2.3111 0.7692 1.4851 0.1812  -0.1037 -0.1431 63  ASP   R CG  
30807 O  OD1 . ASP   R  71  ? 2.4240 0.6346 1.5231 0.1954  -0.1192 -0.1478 63  ASP   R OD1 
30808 O  OD2 . ASP   R  71  ? 2.4531 0.7672 1.5812 0.1960  -0.0433 -0.2448 63  ASP   R OD2 
30809 N  N   . ARG   R  72  ? 1.9175 0.7017 1.4506 0.1891  -0.0280 -0.1614 64  ARG   R N   
30810 C  CA  . ARG   R  72  ? 1.9465 0.6179 1.5155 0.1310  0.0236  -0.1870 64  ARG   R CA  
30811 C  C   . ARG   R  72  ? 1.9582 0.4946 1.4917 0.1084  0.0613  -0.1781 64  ARG   R C   
30812 O  O   . ARG   R  72  ? 1.9734 0.3246 1.5098 0.0629  0.0902  -0.1516 64  ARG   R O   
30813 C  CB  . ARG   R  72  ? 1.9395 0.6389 1.5809 0.1012  0.0475  -0.1819 64  ARG   R CB  
30814 C  CG  . ARG   R  72  ? 1.9786 0.7467 1.5854 0.0693  0.0661  -0.1933 64  ARG   R CG  
30815 C  CD  . ARG   R  72  ? 2.0003 0.8483 1.6733 -0.0241 0.0723  -0.2198 64  ARG   R CD  
30816 N  NE  . ARG   R  72  ? 1.9962 0.9264 1.7588 -0.0451 0.0804  -0.2438 64  ARG   R NE  
30817 C  CZ  . ARG   R  72  ? 1.9853 0.9418 1.7627 -0.1028 0.0783  -0.2455 64  ARG   R CZ  
30818 N  NH1 . ARG   R  72  ? 1.9644 0.9007 1.8278 -0.1296 0.1230  -0.2414 64  ARG   R NH1 
30819 N  NH2 . ARG   R  72  ? 2.0522 0.9704 1.7471 -0.1426 0.0607  -0.2697 64  ARG   R NH2 
30820 N  N   . HIS   R  73  ? 1.9354 0.4727 1.5035 0.1332  0.0520  -0.1690 65  HIS   R N   
30821 C  CA  . HIS   R  73  ? 1.9208 0.5807 1.5706 0.1973  0.0823  -0.2045 65  HIS   R CA  
30822 C  C   . HIS   R  73  ? 1.8744 0.5885 1.5381 0.2217  0.0617  -0.1957 65  HIS   R C   
30823 O  O   . HIS   R  73  ? 1.8688 0.6195 1.5592 0.2865  0.1396  -0.1844 65  HIS   R O   
30824 C  CB  . HIS   R  73  ? 1.9100 0.5935 1.5972 0.1702  0.0764  -0.1909 65  HIS   R CB  
30825 C  CG  . HIS   R  73  ? 1.9224 0.6247 1.6200 0.2020  0.0960  -0.1906 65  HIS   R CG  
30826 N  ND1 . HIS   R  73  ? 1.9402 0.6550 1.6002 0.2252  0.0993  -0.2228 65  HIS   R ND1 
30827 C  CD2 . HIS   R  73  ? 1.9032 0.6363 1.6105 0.2058  0.1152  -0.1943 65  HIS   R CD2 
30828 C  CE1 . HIS   R  73  ? 1.9339 0.6617 1.6012 0.2266  0.0942  -0.2061 65  HIS   R CE1 
30829 N  NE2 . HIS   R  73  ? 1.9235 0.5912 1.6196 0.2196  0.1142  -0.2062 65  HIS   R NE2 
30830 N  N   . ILE   R  74  ? 1.9193 0.6209 1.5487 0.1543  0.0197  -0.2054 66  ILE   R N   
30831 C  CA  . ILE   R  74  ? 1.9411 0.5973 1.5467 0.1620  -0.0125 -0.2034 66  ILE   R CA  
30832 C  C   . ILE   R  74  ? 1.9754 0.5635 1.6158 0.1303  -0.0574 -0.1643 66  ILE   R C   
30833 O  O   . ILE   R  74  ? 1.9338 0.6386 1.7004 0.0916  -0.1115 -0.1509 66  ILE   R O   
30834 C  CB  . ILE   R  74  ? 1.9227 0.5396 1.5307 0.1158  -0.0198 -0.2232 66  ILE   R CB  
30835 C  CG1 . ILE   R  74  ? 1.9226 0.6015 1.5094 0.1366  -0.0113 -0.2431 66  ILE   R CG1 
30836 C  CG2 . ILE   R  74  ? 1.8871 0.5514 1.4958 0.1093  -0.0074 -0.2385 66  ILE   R CG2 
30837 C  CD1 . ILE   R  74  ? 1.9084 0.6455 1.5247 0.1365  0.0059  -0.2448 66  ILE   R CD1 
30838 N  N   . GLY   R  75  ? 1.9725 0.5839 1.6599 0.1775  -0.0547 -0.1725 67  GLY   R N   
30839 C  CA  . GLY   R  75  ? 2.0060 0.6749 1.6555 0.1973  -0.0669 -0.2501 67  GLY   R CA  
30840 C  C   . GLY   R  75  ? 1.9884 0.6776 1.6655 0.1815  -0.0569 -0.2693 67  GLY   R C   
30841 O  O   . GLY   R  75  ? 1.9136 0.7689 1.6933 0.2414  -0.0584 -0.3210 67  GLY   R O   
30842 N  N   . CYS   R  76  ? 2.0532 0.6482 1.6507 0.1618  -0.0627 -0.2754 68  CYS   R N   
30843 C  CA  . CYS   R  76  ? 2.0894 0.6257 1.6251 0.2105  -0.0471 -0.2537 68  CYS   R CA  
30844 C  C   . CYS   R  76  ? 2.0913 0.6922 1.5485 0.2036  -0.0813 -0.2321 68  CYS   R C   
30845 O  O   . CYS   R  76  ? 2.1243 0.7185 1.5904 0.1501  -0.1375 -0.2132 68  CYS   R O   
30846 C  CB  . CYS   R  76  ? 2.1562 0.5357 1.6487 0.2165  -0.0260 -0.3053 68  CYS   R CB  
30847 S  SG  . CYS   R  76  ? 2.2102 0.5847 1.7427 0.1932  0.0719  -0.3194 68  CYS   R SG  
30848 N  N   . ALA   R  77  ? 2.0596 0.6961 1.4626 0.2389  -0.0640 -0.2819 69  ALA   R N   
30849 C  CA  . ALA   R  77  ? 2.0659 0.6969 1.4100 0.2769  -0.0300 -0.3130 69  ALA   R CA  
30850 C  C   . ALA   R  77  ? 2.0307 0.6431 1.4040 0.2875  -0.0296 -0.3354 69  ALA   R C   
30851 O  O   . ALA   R  77  ? 1.9789 0.5807 1.3912 0.3461  0.0096  -0.3878 69  ALA   R O   
30852 C  CB  . ALA   R  77  ? 2.0908 0.7074 1.3984 0.2774  -0.0155 -0.3325 69  ALA   R CB  
30853 N  N   . MET   R  78  ? 2.0018 0.6519 1.4319 0.2551  -0.0108 -0.2677 70  MET   R N   
30854 C  CA  . MET   R  78  ? 2.0290 0.7371 1.4542 0.2754  -0.0017 -0.1904 70  MET   R CA  
30855 C  C   . MET   R  78  ? 2.0070 0.7253 1.3969 0.2727  0.0173  -0.1606 70  MET   R C   
30856 O  O   . MET   R  78  ? 1.9850 0.8221 1.3917 0.3069  0.0234  -0.1450 70  MET   R O   
30857 C  CB  . MET   R  78  ? 2.0655 0.7335 1.5450 0.3013  -0.0179 -0.1647 70  MET   R CB  
30858 C  CG  . MET   R  78  ? 2.1437 0.7343 1.5749 0.3208  -0.0508 -0.1241 70  MET   R CG  
30859 S  SD  . MET   R  78  ? 2.2556 0.5371 1.7467 0.3078  -0.0867 -0.0347 70  MET   R SD  
30860 C  CE  . MET   R  78  ? 2.2282 0.6602 1.7949 0.2065  -0.0838 -0.0351 70  MET   R CE  
30861 N  N   . SER   R  79  ? 2.0031 0.6379 1.4255 0.2363  -0.0139 -0.1859 71  SER   R N   
30862 C  CA  . SER   R  79  ? 2.0175 0.6129 1.4454 0.2341  -0.0147 -0.1351 71  SER   R CA  
30863 C  C   . SER   R  79  ? 2.0437 0.4809 1.4345 0.1974  -0.0507 -0.1239 71  SER   R C   
30864 O  O   . SER   R  79  ? 2.0664 0.3804 1.4368 0.1863  -0.0573 -0.1330 71  SER   R O   
30865 C  CB  . SER   R  79  ? 2.0004 0.7107 1.4742 0.2511  0.0015  -0.1327 71  SER   R CB  
30866 O  OG  . SER   R  79  ? 2.0573 0.7578 1.4966 0.2003  0.0102  -0.1773 71  SER   R OG  
30867 N  N   . GLY   R  80  ? 2.0580 0.4527 1.5106 0.1656  -0.0591 -0.0745 72  GLY   R N   
30868 C  CA  . GLY   R  80  ? 2.0409 0.4781 1.5163 0.1402  -0.0772 -0.0876 72  GLY   R CA  
30869 C  C   . GLY   R  80  ? 2.0588 0.3310 1.4756 0.1318  -0.0871 -0.1050 72  GLY   R C   
30870 O  O   . GLY   R  80  ? 2.0379 0.2056 1.5287 0.1088  -0.1393 -0.0695 72  GLY   R O   
30871 N  N   . LEU   R  81  ? 2.0991 0.3741 1.4195 0.1154  -0.0973 -0.1567 73  LEU   R N   
30872 C  CA  . LEU   R  81  ? 2.0644 0.5393 1.3536 0.1012  -0.0969 -0.1758 73  LEU   R CA  
30873 C  C   . LEU   R  81  ? 2.1393 0.5669 1.3650 0.0828  -0.0940 -0.1187 73  LEU   R C   
30874 O  O   . LEU   R  81  ? 2.1902 0.5887 1.3530 0.0861  -0.0295 -0.1083 73  LEU   R O   
30875 C  CB  . LEU   R  81  ? 2.0380 0.5670 1.3664 0.0590  -0.1023 -0.1692 73  LEU   R CB  
30876 C  CG  . LEU   R  81  ? 2.0026 0.5789 1.3418 0.0372  -0.1013 -0.1765 73  LEU   R CG  
30877 C  CD1 . LEU   R  81  ? 1.9636 0.6164 1.3640 0.0091  -0.0967 -0.1755 73  LEU   R CD1 
30878 C  CD2 . LEU   R  81  ? 2.0146 0.6013 1.3046 0.0391  -0.0903 -0.1711 73  LEU   R CD2 
30879 N  N   . THR   R  82  ? 2.1495 0.6448 1.3110 0.1323  -0.1230 -0.1687 74  THR   R N   
30880 C  CA  . THR   R  82  ? 2.1041 0.6675 1.3459 0.1343  -0.1175 -0.1373 74  THR   R CA  
30881 C  C   . THR   R  82  ? 2.0068 0.8080 1.4005 0.1585  -0.1242 -0.1313 74  THR   R C   
30882 O  O   . THR   R  82  ? 2.0345 0.8095 1.4244 0.1432  -0.1382 -0.0951 74  THR   R O   
30883 C  CB  . THR   R  82  ? 2.1150 0.6139 1.3544 0.1488  -0.0967 -0.1364 74  THR   R CB  
30884 O  OG1 . THR   R  82  ? 2.1802 0.5681 1.3644 0.1483  -0.1381 -0.1143 74  THR   R OG1 
30885 C  CG2 . THR   R  82  ? 2.0735 0.6427 1.3814 0.1381  -0.0974 -0.1004 74  THR   R CG2 
30886 N  N   . ALA   R  83  ? 1.9533 0.8449 1.3993 0.2219  -0.1307 -0.1724 75  ALA   R N   
30887 C  CA  . ALA   R  83  ? 1.9158 0.8078 1.3967 0.2061  -0.1479 -0.1612 75  ALA   R CA  
30888 C  C   . ALA   R  83  ? 1.8569 0.8140 1.4008 0.2116  -0.1741 -0.1522 75  ALA   R C   
30889 O  O   . ALA   R  83  ? 1.8997 0.7554 1.4238 0.1969  -0.2397 -0.0448 75  ALA   R O   
30890 C  CB  . ALA   R  83  ? 1.9211 0.7726 1.3692 0.2134  -0.1523 -0.2294 75  ALA   R CB  
30891 N  N   . ASP   R  84  ? 1.7942 0.8402 1.4110 0.2108  -0.1695 -0.1471 76  ASP   R N   
30892 C  CA  . ASP   R  84  ? 1.7731 0.8125 1.4309 0.1460  -0.1771 -0.1443 76  ASP   R CA  
30893 C  C   . ASP   R  84  ? 1.8646 0.7452 1.3964 0.1318  -0.1798 -0.1219 76  ASP   R C   
30894 O  O   . ASP   R  84  ? 1.8316 0.5229 1.4699 -0.0584 -0.2140 -0.0979 76  ASP   R O   
30895 C  CB  . ASP   R  84  ? 1.7607 0.8132 1.4935 0.1851  -0.1426 -0.1370 76  ASP   R CB  
30896 C  CG  . ASP   R  84  ? 1.6795 0.8660 1.5144 0.1876  -0.1556 -0.1723 76  ASP   R CG  
30897 O  OD1 . ASP   R  84  ? 1.6386 0.8175 1.6009 0.2437  -0.1444 -0.1386 76  ASP   R OD1 
30898 O  OD2 . ASP   R  84  ? 1.7659 0.9392 1.4153 0.1654  -0.0863 -0.1660 76  ASP   R OD2 
30899 N  N   . ALA   R  85  ? 1.9091 0.6809 1.4001 0.1303  -0.1652 -0.0980 77  ALA   R N   
30900 C  CA  . ALA   R  85  ? 1.9326 0.7231 1.3975 0.1002  -0.1809 -0.1312 77  ALA   R CA  
30901 C  C   . ALA   R  85  ? 2.0417 0.7466 1.4364 0.1145  -0.2139 -0.0907 77  ALA   R C   
30902 O  O   . ALA   R  85  ? 1.9778 0.9455 1.4240 0.0292  -0.2872 0.0052  77  ALA   R O   
30903 C  CB  . ALA   R  85  ? 1.9384 0.6769 1.4007 0.1337  -0.1776 -0.1031 77  ALA   R CB  
30904 N  N   . ARG   R  86  ? 2.0309 0.7847 1.4968 0.0702  -0.2290 -0.1276 78  ARG   R N   
30905 C  CA  . ARG   R  86  ? 2.1453 0.7349 1.5165 0.1005  -0.1267 -0.1940 78  ARG   R CA  
30906 C  C   . ARG   R  86  ? 2.0072 0.6533 1.5114 0.1378  -0.0923 -0.1715 78  ARG   R C   
30907 O  O   . ARG   R  86  ? 2.0573 0.5522 1.5606 0.1680  -0.1257 -0.3155 78  ARG   R O   
30908 C  CB  . ARG   R  86  ? 2.1583 0.8196 1.5978 0.0520  -0.1304 -0.2019 78  ARG   R CB  
30909 C  CG  . ARG   R  86  ? 2.3485 0.8897 1.6221 0.0375  -0.0905 -0.2403 78  ARG   R CG  
30910 C  CD  . ARG   R  86  ? 2.4733 1.0472 1.6503 0.0538  -0.0076 -0.2455 78  ARG   R CD  
30911 N  NE  . ARG   R  86  ? 2.7198 1.0849 1.7525 0.0451  0.0210  -0.3225 78  ARG   R NE  
30912 C  CZ  . ARG   R  86  ? 2.7842 1.3354 1.8082 0.0891  0.0599  -0.3136 78  ARG   R CZ  
30913 N  NH1 . ARG   R  86  ? 2.8463 1.3296 1.8631 0.0718  0.0278  -0.2981 78  ARG   R NH1 
30914 N  NH2 . ARG   R  86  ? 2.8956 1.3893 1.7956 0.0688  -0.0047 -0.3712 78  ARG   R NH2 
30915 N  N   . SER   R  87  ? 1.9165 0.5930 1.4583 0.1849  -0.1288 -0.1907 79  SER   R N   
30916 C  CA  . SER   R  87  ? 1.8373 0.5717 1.4272 0.1468  -0.1390 -0.1711 79  SER   R CA  
30917 C  C   . SER   R  87  ? 1.7877 0.5494 1.4531 0.2141  -0.1044 -0.0985 79  SER   R C   
30918 O  O   . SER   R  87  ? 1.7934 0.6417 1.4280 0.1300  -0.0964 -0.1056 79  SER   R O   
30919 C  CB  . SER   R  87  ? 1.7866 0.5983 1.3992 0.1273  -0.1621 -0.2107 79  SER   R CB  
30920 O  OG  . SER   R  87  ? 1.7497 0.6632 1.4340 0.1828  -0.1647 -0.1543 79  SER   R OG  
30921 N  N   . MET   R  88  ? 1.7964 0.4882 1.4693 0.1850  -0.1163 -0.1192 80  MET   R N   
30922 C  CA  . MET   R  88  ? 1.8041 0.5937 1.5334 0.1464  -0.1353 -0.1086 80  MET   R CA  
30923 C  C   . MET   R  88  ? 1.7973 0.5173 1.5508 0.2060  -0.1549 -0.0837 80  MET   R C   
30924 O  O   . MET   R  88  ? 1.7571 0.5947 1.6265 0.1803  -0.2217 -0.0170 80  MET   R O   
30925 C  CB  . MET   R  88  ? 1.8115 0.6707 1.5736 0.2181  -0.1283 -0.0856 80  MET   R CB  
30926 C  CG  . MET   R  88  ? 1.8362 0.7834 1.5741 0.2205  -0.1253 -0.0080 80  MET   R CG  
30927 S  SD  . MET   R  88  ? 1.8538 0.8564 1.6471 0.2754  -0.0929 -0.0421 80  MET   R SD  
30928 C  CE  . MET   R  88  ? 1.8237 0.9851 1.7066 0.2318  -0.0918 -0.0310 80  MET   R CE  
30929 N  N   . ILE   R  89  ? 1.7584 0.4473 1.5474 0.2213  -0.1543 -0.0952 81  ILE   R N   
30930 C  CA  . ILE   R  89  ? 1.7397 0.5897 1.5479 0.2035  -0.1088 -0.0644 81  ILE   R CA  
30931 C  C   . ILE   R  89  ? 1.7531 0.6619 1.5910 0.2586  -0.1182 -0.1186 81  ILE   R C   
30932 O  O   . ILE   R  89  ? 1.7156 0.7221 1.6085 0.2369  -0.0917 -0.1198 81  ILE   R O   
30933 C  CB  . ILE   R  89  ? 1.7132 0.5565 1.5438 0.1849  -0.0802 -0.0699 81  ILE   R CB  
30934 C  CG1 . ILE   R  89  ? 1.7117 0.5340 1.5521 0.1831  -0.0705 -0.0219 81  ILE   R CG1 
30935 C  CG2 . ILE   R  89  ? 1.7076 0.6292 1.5117 0.1927  -0.0411 -0.0583 81  ILE   R CG2 
30936 C  CD1 . ILE   R  89  ? 1.7084 0.5591 1.5729 0.1597  -0.0588 0.0016  81  ILE   R CD1 
30937 N  N   . GLU   R  90  ? 1.7562 0.6917 1.6155 0.2963  -0.1519 -0.1501 82  GLU   R N   
30938 C  CA  . GLU   R  90  ? 1.8187 0.6379 1.6578 0.2817  -0.2099 -0.1682 82  GLU   R CA  
30939 C  C   . GLU   R  90  ? 1.7675 0.6102 1.6697 0.2913  -0.1905 -0.1946 82  GLU   R C   
30940 O  O   . GLU   R  90  ? 1.6796 0.6595 1.6888 0.2149  -0.2118 -0.1779 82  GLU   R O   
30941 C  CB  . GLU   R  90  ? 1.8115 0.6426 1.7138 0.2918  -0.2550 -0.1309 82  GLU   R CB  
30942 C  CG  . GLU   R  90  ? 1.8022 0.6433 1.8004 0.3024  -0.2536 -0.1086 82  GLU   R CG  
30943 C  CD  . GLU   R  90  ? 1.8905 0.6664 1.8900 0.2801  -0.2745 -0.0585 82  GLU   R CD  
30944 O  OE1 . GLU   R  90  ? 1.9242 0.5237 1.8394 0.2689  -0.3022 0.1653  82  GLU   R OE1 
30945 O  OE2 . GLU   R  90  ? 1.9686 0.5702 2.0338 0.2804  -0.2875 -0.0290 82  GLU   R OE2 
30946 N  N   . HIS   R  91  ? 1.7295 0.5102 1.5562 0.2409  -0.2018 -0.2958 83  HIS   R N   
30947 C  CA  . HIS   R  91  ? 1.6995 0.4864 1.5225 0.2194  -0.1640 -0.3036 83  HIS   R CA  
30948 C  C   . HIS   R  91  ? 1.6791 0.5237 1.5032 0.2463  -0.1696 -0.3090 83  HIS   R C   
30949 O  O   . HIS   R  91  ? 1.7148 0.5804 1.6059 0.1727  -0.2176 -0.3187 83  HIS   R O   
30950 C  CB  . HIS   R  91  ? 1.6821 0.5090 1.4957 0.1815  -0.1132 -0.3039 83  HIS   R CB  
30951 C  CG  . HIS   R  91  ? 1.6700 0.5514 1.4905 0.1392  -0.0782 -0.3078 83  HIS   R CG  
30952 N  ND1 . HIS   R  91  ? 1.6204 0.5924 1.5286 0.1387  -0.0610 -0.3137 83  HIS   R ND1 
30953 C  CD2 . HIS   R  91  ? 1.6487 0.5970 1.5222 0.1050  -0.0322 -0.3091 83  HIS   R CD2 
30954 C  CE1 . HIS   R  91  ? 1.6448 0.6319 1.5004 0.1000  -0.0387 -0.3486 83  HIS   R CE1 
30955 N  NE2 . HIS   R  91  ? 1.6490 0.6299 1.5270 0.0763  -0.0097 -0.3298 83  HIS   R NE2 
30956 N  N   . ALA   R  92  ? 1.7016 0.4376 1.4609 0.2151  -0.1997 -0.3231 84  ALA   R N   
30957 C  CA  . ALA   R  92  ? 1.7169 0.4224 1.4669 0.2003  -0.1832 -0.3101 84  ALA   R CA  
30958 C  C   . ALA   R  92  ? 1.7132 0.3933 1.4667 0.2377  -0.2014 -0.3274 84  ALA   R C   
30959 O  O   . ALA   R  92  ? 1.6826 0.4410 1.5126 0.2195  -0.2134 -0.2812 84  ALA   R O   
30960 C  CB  . ALA   R  92  ? 1.7445 0.4019 1.4642 0.2053  -0.1567 -0.2815 84  ALA   R CB  
30961 N  N   . ARG   R  93  ? 1.7402 0.3595 1.4511 0.2409  -0.2106 -0.3483 85  ARG   R N   
30962 C  CA  . ARG   R  93  ? 1.7876 0.3979 1.4447 0.1989  -0.1900 -0.3276 85  ARG   R CA  
30963 C  C   . ARG   R  93  ? 1.7369 0.4223 1.4494 0.1787  -0.1919 -0.3520 85  ARG   R C   
30964 O  O   . ARG   R  93  ? 1.8039 0.3235 1.4333 0.2340  -0.2204 -0.4664 85  ARG   R O   
30965 C  CB  . ARG   R  93  ? 1.8366 0.4322 1.4215 0.1634  -0.1936 -0.3083 85  ARG   R CB  
30966 C  CG  . ARG   R  93  ? 1.8658 0.4350 1.3866 0.1619  -0.1600 -0.2677 85  ARG   R CG  
30967 C  CD  . ARG   R  93  ? 1.8971 0.4524 1.4019 0.1288  -0.1870 -0.2185 85  ARG   R CD  
30968 N  NE  . ARG   R  93  ? 1.9258 0.3650 1.4124 0.0999  -0.1692 -0.2061 85  ARG   R NE  
30969 C  CZ  . ARG   R  93  ? 1.9504 0.3655 1.4603 0.0414  -0.1861 -0.1988 85  ARG   R CZ  
30970 N  NH1 . ARG   R  93  ? 1.9507 0.3124 1.4878 0.0076  -0.1922 -0.2195 85  ARG   R NH1 
30971 N  NH2 . ARG   R  93  ? 1.9321 0.4305 1.4717 0.0589  -0.1449 -0.1564 85  ARG   R NH2 
30972 N  N   . THR   R  94  ? 1.7181 0.4075 1.4047 0.2413  -0.1981 -0.3963 86  THR   R N   
30973 C  CA  . THR   R  94  ? 1.6343 0.3819 1.4394 0.2408  -0.2039 -0.3948 86  THR   R CA  
30974 C  C   . THR   R  94  ? 1.6210 0.4535 1.4369 0.2811  -0.2117 -0.3478 86  THR   R C   
30975 O  O   . THR   R  94  ? 1.5879 0.4666 1.4782 0.2929  -0.2027 -0.3791 86  THR   R O   
30976 C  CB  . THR   R  94  ? 1.6012 0.3746 1.4053 0.2422  -0.2214 -0.4327 86  THR   R CB  
30977 O  OG1 . THR   R  94  ? 1.5766 0.3603 1.4271 0.2577  -0.2277 -0.4343 86  THR   R OG1 
30978 C  CG2 . THR   R  94  ? 1.5846 0.4216 1.3921 0.2208  -0.1953 -0.4578 86  THR   R CG2 
30979 N  N   . ALA   R  95  ? 1.6278 0.4076 1.4300 0.2301  -0.2081 -0.3341 87  ALA   R N   
30980 C  CA  . ALA   R  95  ? 1.6021 0.4468 1.4407 0.2319  -0.1969 -0.3026 87  ALA   R CA  
30981 C  C   . ALA   R  95  ? 1.6482 0.4438 1.4499 0.2452  -0.1730 -0.2381 87  ALA   R C   
30982 O  O   . ALA   R  95  ? 1.5932 0.5619 1.4363 0.1906  -0.1937 -0.2158 87  ALA   R O   
30983 C  CB  . ALA   R  95  ? 1.5859 0.4618 1.4525 0.2410  -0.1933 -0.2891 87  ALA   R CB  
30984 N  N   . ALA   R  96  ? 1.7224 0.4094 1.4503 0.2509  -0.1762 -0.2547 88  ALA   R N   
30985 C  CA  . ALA   R  96  ? 1.7517 0.5338 1.4729 0.2192  -0.1596 -0.2521 88  ALA   R CA  
30986 C  C   . ALA   R  96  ? 1.7492 0.5512 1.4886 0.1966  -0.1968 -0.1935 88  ALA   R C   
30987 O  O   . ALA   R  96  ? 1.7944 0.5537 1.5467 0.1594  -0.2351 -0.1358 88  ALA   R O   
30988 C  CB  . ALA   R  96  ? 1.7985 0.5315 1.4764 0.2471  -0.1471 -0.2474 88  ALA   R CB  
30989 N  N   . VAL   R  97  ? 1.7367 0.5818 1.4415 0.1800  -0.1856 -0.1779 89  VAL   R N   
30990 C  CA  . VAL   R  97  ? 1.7243 0.5462 1.4062 0.1393  -0.1692 -0.2049 89  VAL   R CA  
30991 C  C   . VAL   R  97  ? 1.7003 0.6798 1.3890 0.1438  -0.1386 -0.2205 89  VAL   R C   
30992 O  O   . VAL   R  97  ? 1.6997 0.7855 1.4274 0.0340  -0.1200 -0.3374 89  VAL   R O   
30993 C  CB  . VAL   R  97  ? 1.7391 0.5458 1.3647 0.1384  -0.1689 -0.1862 89  VAL   R CB  
30994 C  CG1 . VAL   R  97  ? 1.7029 0.6009 1.3481 0.1903  -0.1960 -0.1626 89  VAL   R CG1 
30995 C  CG2 . VAL   R  97  ? 1.7751 0.5560 1.3405 0.1358  -0.1518 -0.1457 89  VAL   R CG2 
30996 N  N   . THR   R  98  ? 1.6595 0.4758 1.3507 0.1407  -0.1923 -0.2569 90  THR   R N   
30997 C  CA  . THR   R  98  ? 1.6366 0.4464 1.3072 0.1163  -0.2214 -0.2308 90  THR   R CA  
30998 C  C   . THR   R  98  ? 1.6193 0.4876 1.3143 0.1690  -0.2395 -0.2349 90  THR   R C   
30999 O  O   . THR   R  98  ? 1.6048 0.5450 1.3036 0.1250  -0.2821 -0.2806 90  THR   R O   
31000 C  CB  . THR   R  98  ? 1.6351 0.3836 1.2486 0.1146  -0.2489 -0.2552 90  THR   R CB  
31001 O  OG1 . THR   R  98  ? 1.6762 0.3086 1.2109 0.0611  -0.2483 -0.2838 90  THR   R OG1 
31002 C  CG2 . THR   R  98  ? 1.6037 0.4051 1.2254 0.1014  -0.2413 -0.2349 90  THR   R CG2 
31003 N  N   . HIS   R  99  ? 1.6626 0.4612 1.3405 0.1802  -0.2238 -0.2455 91  HIS   R N   
31004 C  CA  . HIS   R  99  ? 1.6578 0.4498 1.4120 0.1919  -0.2213 -0.2803 91  HIS   R CA  
31005 C  C   . HIS   R  99  ? 1.7194 0.5476 1.4294 0.1786  -0.1973 -0.2090 91  HIS   R C   
31006 O  O   . HIS   R  99  ? 1.7398 0.6176 1.5112 0.1266  -0.2177 -0.2172 91  HIS   R O   
31007 C  CB  . HIS   R  99  ? 1.7259 0.3944 1.4382 0.1807  -0.2124 -0.3070 91  HIS   R CB  
31008 C  CG  . HIS   R  99  ? 1.7215 0.3119 1.4652 0.2523  -0.2360 -0.2808 91  HIS   R CG  
31009 N  ND1 . HIS   R  99  ? 1.7588 0.3064 1.4780 0.2680  -0.2169 -0.2357 91  HIS   R ND1 
31010 C  CD2 . HIS   R  99  ? 1.7560 0.3303 1.5179 0.2581  -0.2044 -0.2507 91  HIS   R CD2 
31011 C  CE1 . HIS   R  99  ? 1.7619 0.3916 1.5353 0.2506  -0.2120 -0.2025 91  HIS   R CE1 
31012 N  NE2 . HIS   R  99  ? 1.7643 0.4033 1.5401 0.2629  -0.2124 -0.1946 91  HIS   R NE2 
31013 N  N   . ASN   R  100 ? 1.6898 0.5627 1.4255 0.1490  -0.1824 -0.1899 92  ASN   R N   
31014 C  CA  . ASN   R  100 ? 1.6881 0.5753 1.4810 0.1408  -0.1431 -0.1813 92  ASN   R CA  
31015 C  C   . ASN   R  100 ? 1.6582 0.5313 1.5119 0.1197  -0.1336 -0.1333 92  ASN   R C   
31016 O  O   . ASN   R  100 ? 1.7014 0.4740 1.5884 0.1414  -0.0998 -0.1060 92  ASN   R O   
31017 C  CB  . ASN   R  100 ? 1.7057 0.6159 1.4702 0.1312  -0.1360 -0.1528 92  ASN   R CB  
31018 C  CG  . ASN   R  100 ? 1.7520 0.6092 1.4987 0.1693  -0.1357 -0.1184 92  ASN   R CG  
31019 O  OD1 . ASN   R  100 ? 1.7337 0.6808 1.5812 0.2227  -0.1449 -0.1230 92  ASN   R OD1 
31020 N  ND2 . ASN   R  100 ? 1.7540 0.6549 1.5144 0.1696  -0.1134 -0.1081 92  ASN   R ND2 
31021 N  N   . LEU   R  101 ? 1.6538 0.4988 1.4849 0.1462  -0.1430 -0.1393 93  LEU   R N   
31022 C  CA  . LEU   R  101 ? 1.6603 0.4672 1.4785 0.1283  -0.1813 -0.1639 93  LEU   R CA  
31023 C  C   . LEU   R  101 ? 1.6857 0.5636 1.4778 0.1314  -0.1736 -0.1782 93  LEU   R C   
31024 O  O   . LEU   R  101 ? 1.7392 0.5573 1.5271 0.1173  -0.1999 -0.1270 93  LEU   R O   
31025 C  CB  . LEU   R  101 ? 1.6435 0.4386 1.4334 0.1542  -0.2113 -0.2026 93  LEU   R CB  
31026 C  CG  . LEU   R  101 ? 1.6006 0.4581 1.4517 0.1216  -0.2204 -0.2834 93  LEU   R CG  
31027 C  CD1 . LEU   R  101 ? 1.6166 0.5044 1.4604 0.1227  -0.2072 -0.2610 93  LEU   R CD1 
31028 C  CD2 . LEU   R  101 ? 1.6083 0.3950 1.4260 0.1164  -0.2188 -0.3092 93  LEU   R CD2 
31029 N  N   . TYR   R  102 ? 1.6669 0.5198 1.4411 0.1328  -0.1643 -0.2194 94  TYR   R N   
31030 C  CA  . TYR   R  102 ? 1.6174 0.5530 1.4574 0.1315  -0.1711 -0.2682 94  TYR   R CA  
31031 C  C   . TYR   R  102 ? 1.5953 0.5103 1.3976 0.1796  -0.1625 -0.2720 94  TYR   R C   
31032 O  O   . TYR   R  102 ? 1.6122 0.6229 1.3375 0.2192  -0.1735 -0.2698 94  TYR   R O   
31033 C  CB  . TYR   R  102 ? 1.6468 0.6383 1.4244 0.1178  -0.1607 -0.2400 94  TYR   R CB  
31034 C  CG  . TYR   R  102 ? 1.6787 0.8048 1.5089 0.0797  -0.1355 -0.2193 94  TYR   R CG  
31035 C  CD1 . TYR   R  102 ? 1.7138 0.8385 1.6167 0.0991  -0.1409 -0.1976 94  TYR   R CD1 
31036 C  CD2 . TYR   R  102 ? 1.7227 0.8367 1.5192 0.0643  -0.1345 -0.1849 94  TYR   R CD2 
31037 C  CE1 . TYR   R  102 ? 1.7244 0.9630 1.6675 0.0355  -0.1508 -0.1757 94  TYR   R CE1 
31038 C  CE2 . TYR   R  102 ? 1.7306 0.9022 1.5495 0.0084  -0.1447 -0.1883 94  TYR   R CE2 
31039 C  CZ  . TYR   R  102 ? 1.6502 0.9897 1.6094 0.0084  -0.1479 -0.1860 94  TYR   R CZ  
31040 O  OH  . TYR   R  102 ? 1.6865 1.1656 1.5599 -0.1625 -0.1799 -0.2003 94  TYR   R OH  
31041 N  N   . TYR   R  103 ? 1.6227 0.4433 1.3789 0.1745  -0.1775 -0.3097 95  TYR   R N   
31042 C  CA  . TYR   R  103 ? 1.6193 0.5455 1.3764 0.1541  -0.1403 -0.3138 95  TYR   R CA  
31043 C  C   . TYR   R  103 ? 1.6176 0.5569 1.3948 0.1671  -0.1403 -0.2803 95  TYR   R C   
31044 O  O   . TYR   R  103 ? 1.6097 0.5288 1.4260 0.1488  -0.0671 -0.2540 95  TYR   R O   
31045 C  CB  . TYR   R  103 ? 1.6175 0.5630 1.3441 0.1485  -0.1309 -0.2926 95  TYR   R CB  
31046 C  CG  . TYR   R  103 ? 1.6068 0.5988 1.3182 0.1198  -0.1339 -0.3242 95  TYR   R CG  
31047 C  CD1 . TYR   R  103 ? 1.5747 0.5948 1.2942 0.1276  -0.1149 -0.3136 95  TYR   R CD1 
31048 C  CD2 . TYR   R  103 ? 1.6046 0.6503 1.2716 0.0946  -0.1372 -0.2926 95  TYR   R CD2 
31049 C  CE1 . TYR   R  103 ? 1.5514 0.6258 1.2654 0.1224  -0.1545 -0.3049 95  TYR   R CE1 
31050 C  CE2 . TYR   R  103 ? 1.5820 0.6848 1.2496 0.0910  -0.1431 -0.3099 95  TYR   R CE2 
31051 C  CZ  . TYR   R  103 ? 1.5475 0.6781 1.2450 0.0981  -0.1452 -0.2997 95  TYR   R CZ  
31052 O  OH  . TYR   R  103 ? 1.5118 0.8445 1.2423 0.0684  -0.1701 -0.2699 95  TYR   R OH  
31053 N  N   . ASP   R  104 ? 1.6246 0.6628 1.4238 0.1725  -0.1736 -0.2756 96  ASP   R N   
31054 C  CA  . ASP   R  104 ? 1.6397 0.8010 1.4442 0.1618  -0.1679 -0.2387 96  ASP   R CA  
31055 C  C   . ASP   R  104 ? 1.6411 0.8236 1.4494 0.1748  -0.1651 -0.2175 96  ASP   R C   
31056 O  O   . ASP   R  104 ? 1.6799 0.8411 1.5144 0.1431  -0.1569 -0.2014 96  ASP   R O   
31057 C  CB  . ASP   R  104 ? 1.6718 0.8337 1.5013 0.1462  -0.1706 -0.3013 96  ASP   R CB  
31058 C  CG  . ASP   R  104 ? 1.7430 0.9425 1.5321 0.1399  -0.1227 -0.2848 96  ASP   R CG  
31059 O  OD1 . ASP   R  104 ? 1.8077 1.0943 1.5388 0.1001  -0.1518 -0.2887 96  ASP   R OD1 
31060 O  OD2 . ASP   R  104 ? 1.7968 0.9506 1.5812 0.1486  -0.1096 -0.4143 96  ASP   R OD2 
31061 N  N   . GLU   R  105 ? 1.6617 0.8268 1.4060 0.1599  -0.1547 -0.1824 97  GLU   R N   
31062 C  CA  . GLU   R  105 ? 1.6998 0.9094 1.4091 0.1921  -0.1047 -0.1625 97  GLU   R CA  
31063 C  C   . GLU   R  105 ? 1.7026 0.9299 1.3671 0.1829  -0.1192 -0.1639 97  GLU   R C   
31064 O  O   . GLU   R  105 ? 1.6785 0.9799 1.3260 0.1664  -0.1910 -0.1517 97  GLU   R O   
31065 C  CB  . GLU   R  105 ? 1.7239 0.9394 1.4042 0.2068  -0.1045 -0.1542 97  GLU   R CB  
31066 C  CG  . GLU   R  105 ? 1.7380 0.9054 1.3788 0.2392  -0.1072 -0.1656 97  GLU   R CG  
31067 C  CD  . GLU   R  105 ? 1.7591 0.8612 1.3846 0.3012  -0.1033 -0.1655 97  GLU   R CD  
31068 O  OE1 . GLU   R  105 ? 1.7081 0.7476 1.3965 0.2966  -0.1332 -0.2100 97  GLU   R OE1 
31069 O  OE2 . GLU   R  105 ? 1.7160 0.8406 1.3236 0.3488  -0.0726 -0.1393 97  GLU   R OE2 
31070 N  N   . ASP   R  106 ? 1.7234 0.9470 1.3899 0.2037  -0.0856 -0.1494 98  ASP   R N   
31071 C  CA  . ASP   R  106 ? 1.6912 0.9621 1.4665 0.2023  -0.0573 -0.1807 98  ASP   R CA  
31072 C  C   . ASP   R  106 ? 1.6082 0.9325 1.4917 0.1690  -0.0477 -0.1786 98  ASP   R C   
31073 O  O   . ASP   R  106 ? 1.5713 1.0100 1.5472 0.1234  -0.0412 -0.2053 98  ASP   R O   
31074 C  CB  . ASP   R  106 ? 1.7226 1.0202 1.4501 0.2152  -0.0443 -0.1653 98  ASP   R CB  
31075 C  CG  . ASP   R  106 ? 1.7760 1.0425 1.4344 0.2413  -0.0467 -0.1837 98  ASP   R CG  
31076 O  OD1 . ASP   R  106 ? 1.8251 1.0628 1.4687 0.2697  -0.1022 -0.2107 98  ASP   R OD1 
31077 O  OD2 . ASP   R  106 ? 1.7485 1.1124 1.4258 0.2421  -0.0594 -0.2033 98  ASP   R OD2 
31078 N  N   . ILE   R  107 ? 1.6129 0.9025 1.6031 0.1815  -0.0183 -0.2227 99  ILE   R N   
31079 C  CA  . ILE   R  107 ? 1.6175 0.8066 1.6396 0.2018  -0.0583 -0.2353 99  ILE   R CA  
31080 C  C   . ILE   R  107 ? 1.6159 0.6904 1.5890 0.1413  -0.0919 -0.2074 99  ILE   R C   
31081 O  O   . ILE   R  107 ? 1.5915 0.5030 1.6186 0.0355  -0.1199 -0.2279 99  ILE   R O   
31082 C  CB  . ILE   R  107 ? 1.6233 0.7012 1.6716 0.2034  -0.0529 -0.2892 99  ILE   R CB  
31083 C  CG1 . ILE   R  107 ? 1.6521 0.6816 1.6476 0.2301  -0.0632 -0.3031 99  ILE   R CG1 
31084 C  CG2 . ILE   R  107 ? 1.6370 0.8143 1.6913 0.2163  -0.0858 -0.2848 99  ILE   R CG2 
31085 C  CD1 . ILE   R  107 ? 1.7155 0.7340 1.6426 0.2159  -0.0784 -0.2756 99  ILE   R CD1 
31086 N  N   . ASN   R  108 ? 1.6231 0.7377 1.6183 0.1094  -0.0892 -0.1289 100 ASN   R N   
31087 C  CA  . ASN   R  108 ? 1.6373 0.7913 1.5708 0.1419  -0.0629 -0.1172 100 ASN   R CA  
31088 C  C   . ASN   R  108 ? 1.5996 0.7955 1.4958 0.1864  -0.0801 -0.1549 100 ASN   R C   
31089 O  O   . ASN   R  108 ? 1.5143 0.8697 1.4749 0.2760  -0.1471 -0.1432 100 ASN   R O   
31090 C  CB  . ASN   R  108 ? 1.6848 0.8441 1.5539 0.1161  -0.0528 -0.0698 100 ASN   R CB  
31091 C  CG  . ASN   R  108 ? 1.7299 0.8955 1.5142 0.0684  -0.0461 -0.0578 100 ASN   R CG  
31092 O  OD1 . ASN   R  108 ? 1.7797 0.8796 1.4583 0.0811  -0.0275 0.0235  100 ASN   R OD1 
31093 N  ND2 . ASN   R  108 ? 1.7622 1.0247 1.5776 0.0523  0.0294  -0.0462 100 ASN   R ND2 
31094 N  N   . VAL   R  109 ? 1.6571 0.8277 1.4674 0.1622  -0.0446 -0.1630 101 VAL   R N   
31095 C  CA  . VAL   R  109 ? 1.7100 0.8045 1.4693 0.1425  -0.0179 -0.1522 101 VAL   R CA  
31096 C  C   . VAL   R  109 ? 1.6942 0.7080 1.5003 0.1118  -0.0303 -0.1762 101 VAL   R C   
31097 O  O   . VAL   R  109 ? 1.7048 0.6716 1.5469 0.1060  -0.0347 -0.1374 101 VAL   R O   
31098 C  CB  . VAL   R  109 ? 1.7623 0.7926 1.4609 0.1348  -0.0022 -0.1699 101 VAL   R CB  
31099 C  CG1 . VAL   R  109 ? 1.7506 0.7633 1.4345 0.1534  0.0046  -0.1506 101 VAL   R CG1 
31100 C  CG2 . VAL   R  109 ? 1.8074 0.8290 1.4466 0.1158  0.0241  -0.1863 101 VAL   R CG2 
31101 N  N   . GLU   R  110 ? 1.6818 0.6456 1.4922 0.1381  -0.0205 -0.2068 102 GLU   R N   
31102 C  CA  . GLU   R  110 ? 1.6447 0.6449 1.4953 0.1732  -0.0279 -0.1979 102 GLU   R CA  
31103 C  C   . GLU   R  110 ? 1.6140 0.6575 1.5069 0.1701  -0.0364 -0.1802 102 GLU   R C   
31104 O  O   . GLU   R  110 ? 1.6078 0.4826 1.4595 0.2042  -0.0947 -0.2362 102 GLU   R O   
31105 C  CB  . GLU   R  110 ? 1.6053 0.7216 1.5472 0.1710  -0.0161 -0.1991 102 GLU   R CB  
31106 C  CG  . GLU   R  110 ? 1.6155 0.8065 1.5564 0.1707  -0.0199 -0.1453 102 GLU   R CG  
31107 C  CD  . GLU   R  110 ? 1.5994 0.9224 1.5576 0.1895  -0.0145 -0.1567 102 GLU   R CD  
31108 O  OE1 . GLU   R  110 ? 1.5925 1.0853 1.6615 0.1698  -0.0397 -0.1155 102 GLU   R OE1 
31109 O  OE2 . GLU   R  110 ? 1.6060 1.0420 1.5728 0.2313  0.0061  -0.1403 102 GLU   R OE2 
31110 N  N   . SER   R  111 ? 1.6008 0.6575 1.5473 0.1896  -0.0235 -0.1580 103 SER   R N   
31111 C  CA  . SER   R  111 ? 1.6239 0.6314 1.5153 0.2029  -0.0386 -0.1675 103 SER   R CA  
31112 C  C   . SER   R  111 ? 1.6576 0.5728 1.4783 0.2212  -0.0610 -0.1435 103 SER   R C   
31113 O  O   . SER   R  111 ? 1.6618 0.6228 1.4776 0.2606  -0.0496 -0.1268 103 SER   R O   
31114 C  CB  . SER   R  111 ? 1.5914 0.6526 1.5123 0.1840  -0.0668 -0.2141 103 SER   R CB  
31115 O  OG  . SER   R  111 ? 1.6102 0.7640 1.5203 0.1947  -0.0916 -0.2228 103 SER   R OG  
31116 N  N   . LEU   R  112 ? 1.7157 0.4753 1.4748 0.2127  -0.0543 -0.1359 104 LEU   R N   
31117 C  CA  . LEU   R  112 ? 1.7681 0.5262 1.4230 0.2035  -0.0562 -0.1967 104 LEU   R CA  
31118 C  C   . LEU   R  112 ? 1.7735 0.5753 1.4094 0.1598  -0.0431 -0.1624 104 LEU   R C   
31119 O  O   . LEU   R  112 ? 1.7585 0.7656 1.4011 0.1724  -0.0262 -0.2491 104 LEU   R O   
31120 C  CB  . LEU   R  112 ? 1.7900 0.3928 1.4220 0.1807  -0.0557 -0.2164 104 LEU   R CB  
31121 C  CG  . LEU   R  112 ? 1.7951 0.4031 1.4259 0.1940  -0.0627 -0.2255 104 LEU   R CG  
31122 C  CD1 . LEU   R  112 ? 1.8336 0.4086 1.3980 0.1665  -0.0802 -0.2071 104 LEU   R CD1 
31123 C  CD2 . LEU   R  112 ? 1.7777 0.3837 1.4206 0.1846  -0.0860 -0.2586 104 LEU   R CD2 
31124 N  N   . THR   R  113 ? 1.7975 0.7046 1.4270 0.2362  -0.0326 -0.0995 105 THR   R N   
31125 C  CA  . THR   R  113 ? 1.8271 0.7348 1.3675 0.2071  -0.0135 -0.0015 105 THR   R CA  
31126 C  C   . THR   R  113 ? 1.8037 0.7340 1.3691 0.1853  -0.0402 0.0616  105 THR   R C   
31127 O  O   . THR   R  113 ? 1.7787 0.7719 1.2626 0.1860  -0.0623 0.1688  105 THR   R O   
31128 C  CB  . THR   R  113 ? 1.8608 0.7118 1.4443 0.2141  0.0024  -0.0332 105 THR   R CB  
31129 O  OG1 . THR   R  113 ? 1.8934 0.9107 1.4533 0.2118  0.0438  -0.0392 105 THR   R OG1 
31130 C  CG2 . THR   R  113 ? 1.8706 0.6990 1.4264 0.2274  0.0056  -0.0406 105 THR   R CG2 
31131 N  N   . GLN   R  114 ? 1.8104 0.7101 1.3686 0.1937  -0.0101 0.0310  106 GLN   R N   
31132 C  CA  . GLN   R  114 ? 1.7782 0.7751 1.3432 0.1854  -0.0306 -0.0542 106 GLN   R CA  
31133 C  C   . GLN   R  114 ? 1.7629 0.8268 1.4010 0.1890  -0.0773 -0.0398 106 GLN   R C   
31134 O  O   . GLN   R  114 ? 1.6780 0.9562 1.4236 0.1849  -0.0617 -0.0551 106 GLN   R O   
31135 C  CB  . GLN   R  114 ? 1.7888 0.7904 1.3607 0.1814  -0.0227 -0.0909 106 GLN   R CB  
31136 C  CG  . GLN   R  114 ? 1.7992 0.8529 1.3450 0.1875  -0.0419 -0.1022 106 GLN   R CG  
31137 C  CD  . GLN   R  114 ? 1.8093 0.8957 1.2657 0.2291  -0.0746 -0.0594 106 GLN   R CD  
31138 O  OE1 . GLN   R  114 ? 1.7831 1.0438 1.2353 0.2111  -0.0505 -0.0348 106 GLN   R OE1 
31139 N  NE2 . GLN   R  114 ? 1.8064 1.0143 1.2371 0.2300  -0.0952 -0.0387 106 GLN   R NE2 
31140 N  N   . SER   R  115 ? 1.8022 0.8589 1.3978 0.1366  -0.0833 0.0105  107 SER   R N   
31141 C  CA  . SER   R  115 ? 1.8180 0.8619 1.4055 0.1498  -0.0770 -0.0088 107 SER   R CA  
31142 C  C   . SER   R  115 ? 1.8142 0.8773 1.3468 0.1344  -0.0562 0.0028  107 SER   R C   
31143 O  O   . SER   R  115 ? 1.7981 0.8767 1.3094 0.1935  -0.0632 0.0558  107 SER   R O   
31144 C  CB  . SER   R  115 ? 1.8437 0.8601 1.4406 0.1699  -0.0737 -0.0033 107 SER   R CB  
31145 O  OG  . SER   R  115 ? 1.7904 1.0335 1.4568 0.1642  -0.0728 -0.0156 107 SER   R OG  
31146 N  N   . VAL   R  116 ? 1.8822 0.8881 1.3441 0.1112  -0.0863 -0.0356 108 VAL   R N   
31147 C  CA  . VAL   R  116 ? 1.8918 0.8570 1.3845 0.1641  -0.0915 -0.1044 108 VAL   R CA  
31148 C  C   . VAL   R  116 ? 1.8858 0.7292 1.3372 0.2214  -0.1181 -0.1965 108 VAL   R C   
31149 O  O   . VAL   R  116 ? 1.8142 0.7528 1.3087 0.2973  -0.1184 -0.3127 108 VAL   R O   
31150 C  CB  . VAL   R  116 ? 1.8869 0.8991 1.4262 0.1619  -0.0332 -0.0773 108 VAL   R CB  
31151 C  CG1 . VAL   R  116 ? 1.9055 0.8730 1.4468 0.1594  -0.0327 -0.0591 108 VAL   R CG1 
31152 C  CG2 . VAL   R  116 ? 1.8790 0.9298 1.4706 0.1702  -0.0521 -0.0448 108 VAL   R CG2 
31153 N  N   . CYS   R  117 ? 1.8771 0.6347 1.3670 0.2372  -0.0979 -0.2040 109 CYS   R N   
31154 C  CA  . CYS   R  117 ? 1.8959 0.6868 1.3777 0.2125  -0.0469 -0.1556 109 CYS   R CA  
31155 C  C   . CYS   R  117 ? 1.8538 0.7248 1.3546 0.2064  -0.0575 -0.1002 109 CYS   R C   
31156 O  O   . CYS   R  117 ? 1.8666 0.6452 1.3550 0.2296  -0.0573 -0.1509 109 CYS   R O   
31157 C  CB  . CYS   R  117 ? 1.8961 0.6620 1.4187 0.2026  -0.0272 -0.1012 109 CYS   R CB  
31158 S  SG  . CYS   R  117 ? 1.9905 0.7067 1.5237 0.2470  0.0482  -0.1251 109 CYS   R SG  
31159 N  N   . ASP   R  118 ? 1.7970 0.7442 1.4161 0.2161  -0.0431 -0.1097 110 ASP   R N   
31160 C  CA  . ASP   R  118 ? 1.7488 0.9916 1.4142 0.1674  -0.0243 -0.0799 110 ASP   R CA  
31161 C  C   . ASP   R  118 ? 1.7872 1.0571 1.3836 0.1108  -0.0424 -0.0971 110 ASP   R C   
31162 O  O   . ASP   R  118 ? 1.8821 1.2313 1.2767 0.1323  -0.0876 -0.0449 110 ASP   R O   
31163 C  CB  . ASP   R  118 ? 1.6948 1.0232 1.5168 0.1654  -0.0535 -0.1241 110 ASP   R CB  
31164 C  CG  . ASP   R  118 ? 1.6530 1.0612 1.6012 0.1688  -0.0521 -0.1126 110 ASP   R CG  
31165 O  OD1 . ASP   R  118 ? 1.6525 1.1350 1.6128 0.1843  -0.0398 -0.0323 110 ASP   R OD1 
31166 O  OD2 . ASP   R  118 ? 1.5483 1.0830 1.7475 0.1722  -0.0777 -0.2019 110 ASP   R OD2 
31167 N  N   . LEU   R  119 ? 1.8173 1.1238 1.3617 0.0798  -0.0349 -0.1759 111 LEU   R N   
31168 C  CA  . LEU   R  119 ? 1.8286 1.1370 1.3198 0.0993  -0.0511 -0.2498 111 LEU   R CA  
31169 C  C   . LEU   R  119 ? 1.8346 1.1317 1.4173 0.0581  -0.0678 -0.3092 111 LEU   R C   
31170 O  O   . LEU   R  119 ? 1.8554 1.1921 1.3777 -0.0218 -0.0707 -0.4273 111 LEU   R O   
31171 C  CB  . LEU   R  119 ? 1.8128 1.0533 1.2986 0.1153  -0.0117 -0.2685 111 LEU   R CB  
31172 C  CG  . LEU   R  119 ? 1.7825 1.0581 1.3038 0.1470  0.0183  -0.2670 111 LEU   R CG  
31173 C  CD1 . LEU   R  119 ? 1.7593 0.9844 1.3074 0.1669  0.0067  -0.2825 111 LEU   R CD1 
31174 C  CD2 . LEU   R  119 ? 1.7647 1.0992 1.2876 0.1391  0.0209  -0.2421 111 LEU   R CD2 
31175 N  N   . ALA   R  120 ? 1.8064 1.4297 1.5445 0.1684  -0.0793 -0.2710 112 ALA   R N   
31176 C  CA  . ALA   R  120 ? 1.8370 1.4544 1.6484 0.2248  -0.0737 -0.1959 112 ALA   R CA  
31177 C  C   . ALA   R  120 ? 1.8012 1.7342 1.6356 0.2493  -0.0928 -0.1012 112 ALA   R C   
31178 O  O   . ALA   R  120 ? 1.7357 1.8883 1.8206 0.2266  -0.1235 -0.0345 112 ALA   R O   
31179 C  CB  . ALA   R  120 ? 1.8343 1.5688 1.6767 0.2324  -0.0450 -0.2105 112 ALA   R CB  
31180 N  N   . LEU   R  121 ? 1.7825 1.8271 1.6139 0.3050  -0.0892 -0.0785 113 LEU   R N   
31181 C  CA  . LEU   R  121 ? 1.8663 1.8530 1.5040 0.2907  -0.0955 -0.1432 113 LEU   R CA  
31182 C  C   . LEU   R  121 ? 1.9135 1.7284 1.3367 0.3027  -0.1723 -0.1720 113 LEU   R C   
31183 O  O   . LEU   R  121 ? 2.0774 1.7992 1.1346 0.3093  -0.2072 -0.2550 113 LEU   R O   
31184 C  CB  . LEU   R  121 ? 1.7998 1.8704 1.5222 0.3018  -0.0676 -0.1475 113 LEU   R CB  
31185 C  CG  . LEU   R  121 ? 1.9177 1.6418 1.6084 0.2423  -0.0367 -0.1536 113 LEU   R CG  
31186 C  CD1 . LEU   R  121 ? 1.9599 1.6333 1.5793 0.2530  -0.0099 -0.0971 113 LEU   R CD1 
31187 C  CD2 . LEU   R  121 ? 1.9158 1.4842 1.6433 0.3359  0.0018  -0.1286 113 LEU   R CD2 
31188 N  N   . ARG   R  122 ? 1.9605 1.6315 1.4533 0.1962  -0.2378 -0.1659 114 ARG   R N   
31189 C  CA  . ARG   R  122 ? 1.8528 1.5444 1.5405 0.1011  -0.2836 -0.1835 114 ARG   R CA  
31190 C  C   . ARG   R  122 ? 1.8475 1.3446 1.5317 0.1393  -0.2827 -0.1499 114 ARG   R C   
31191 O  O   . ARG   R  122 ? 1.7337 1.4549 1.6299 0.1266  -0.3365 -0.2066 114 ARG   R O   
31192 C  CB  . ARG   R  122 ? 1.8937 1.5415 1.6462 -0.0054 -0.2657 -0.1735 114 ARG   R CB  
31193 C  CG  . ARG   R  122 ? 1.9350 1.6572 1.6396 -0.1240 -0.2549 -0.1788 114 ARG   R CG  
31194 C  CD  . ARG   R  122 ? 2.0217 1.7012 1.6836 -0.0922 -0.2763 -0.1345 114 ARG   R CD  
31195 N  NE  . ARG   R  122 ? 2.1543 1.7647 1.7497 -0.1219 -0.2319 -0.0780 114 ARG   R NE  
31196 C  CZ  . ARG   R  122 ? 2.2360 1.7515 1.6799 -0.1398 -0.2869 -0.0823 114 ARG   R CZ  
31197 N  NH1 . ARG   R  122 ? 2.2378 1.7260 1.6780 -0.1349 -0.3363 -0.1527 114 ARG   R NH1 
31198 N  NH2 . ARG   R  122 ? 2.2722 1.7660 1.8621 -0.1804 -0.2239 -0.0596 114 ARG   R NH2 
31199 N  N   . PHE   R  123 ? 1.7409 1.2973 1.4328 0.1358  -0.3074 -0.2049 115 PHE   R N   
31200 C  CA  . PHE   R  123 ? 1.7878 1.1270 1.3981 0.1583  -0.3036 -0.1802 115 PHE   R CA  
31201 C  C   . PHE   R  123 ? 1.7801 1.0447 1.3950 0.1333  -0.3459 -0.1725 115 PHE   R C   
31202 O  O   . PHE   R  123 ? 1.7923 1.0135 1.3606 0.1881  -0.3372 -0.1662 115 PHE   R O   
31203 C  CB  . PHE   R  123 ? 1.8273 1.0887 1.4207 0.1679  -0.3272 -0.1795 115 PHE   R CB  
31204 C  CG  . PHE   R  123 ? 1.8600 1.0725 1.4460 0.1733  -0.3620 -0.1953 115 PHE   R CG  
31205 C  CD1 . PHE   R  123 ? 1.8615 0.9724 1.4336 0.1742  -0.3670 -0.1915 115 PHE   R CD1 
31206 C  CD2 . PHE   R  123 ? 1.8659 1.0914 1.4848 0.1804  -0.3410 -0.1851 115 PHE   R CD2 
31207 C  CE1 . PHE   R  123 ? 1.8889 0.9939 1.4585 0.2325  -0.3536 -0.2436 115 PHE   R CE1 
31208 C  CE2 . PHE   R  123 ? 1.8804 1.1441 1.4903 0.2218  -0.3648 -0.2182 115 PHE   R CE2 
31209 C  CZ  . PHE   R  123 ? 1.8894 1.0587 1.4827 0.2115  -0.3466 -0.2167 115 PHE   R CZ  
31210 N  N   . GLY   R  124 ? 1.8469 0.9592 1.4594 0.0965  -0.2989 -0.0915 116 GLY   R N   
31211 C  CA  . GLY   R  124 ? 1.8314 1.0165 1.5362 0.0705  -0.2739 -0.0435 116 GLY   R CA  
31212 C  C   . GLY   R  124 ? 1.8348 1.0166 1.6341 0.0896  -0.2584 0.0191  116 GLY   R C   
31213 O  O   . GLY   R  124 ? 1.7492 0.8758 1.7510 0.1829  -0.2081 0.1614  116 GLY   R O   
31214 N  N   . GLU   R  125 ? 1.8695 1.1112 1.7047 0.0519  -0.1770 0.0213  117 GLU   R N   
31215 C  CA  . GLU   R  125 ? 1.9076 1.2229 1.7428 0.0565  -0.1087 0.0094  117 GLU   R CA  
31216 C  C   . GLU   R  125 ? 1.9123 1.2391 1.7300 0.0740  -0.0331 0.0171  117 GLU   R C   
31217 O  O   . GLU   R  125 ? 2.0721 1.3395 1.6218 0.1283  0.0688  0.0232  117 GLU   R O   
31218 C  CB  . GLU   R  125 ? 1.9757 1.3263 1.8194 -0.0421 -0.0984 0.0783  117 GLU   R CB  
31219 C  CG  . GLU   R  125 ? 1.9893 1.3921 1.9037 -0.1458 -0.0840 0.0873  117 GLU   R CG  
31220 C  CD  . GLU   R  125 ? 2.0268 1.2948 2.0541 -0.2798 -0.0465 0.1357  117 GLU   R CD  
31221 O  OE1 . GLU   R  125 ? 2.1145 1.2949 2.1025 -0.2824 0.1363  0.2756  117 GLU   R OE1 
31222 O  OE2 . GLU   R  125 ? 2.0185 1.1896 2.2142 -0.2736 -0.0066 0.0797  117 GLU   R OE2 
31223 N  N   . LEU   R  133 ? 1.9503 1.2746 1.4886 0.1375  -0.2171 -0.1823 125 LEU   R N   
31224 C  CA  . LEU   R  133 ? 1.9403 1.2811 1.4798 0.1549  -0.2257 -0.1609 125 LEU   R CA  
31225 C  C   . LEU   R  133 ? 1.7954 1.2717 1.5105 0.1821  -0.2444 -0.1245 125 LEU   R C   
31226 O  O   . LEU   R  133 ? 1.7538 1.3588 1.5369 0.2819  -0.2605 -0.0203 125 LEU   R O   
31227 C  CB  . LEU   R  133 ? 1.9859 1.3216 1.4502 0.1703  -0.2396 -0.1721 125 LEU   R CB  
31228 C  CG  . LEU   R  133 ? 2.0080 1.3843 1.4295 0.1885  -0.2353 -0.1858 125 LEU   R CG  
31229 C  CD1 . LEU   R  133 ? 1.9648 1.4262 1.3880 0.1942  -0.2634 -0.2030 125 LEU   R CD1 
31230 C  CD2 . LEU   R  133 ? 2.0209 1.3606 1.4335 0.2007  -0.2297 -0.1731 125 LEU   R CD2 
31231 N  N   . MET   R  134 ? 1.7755 1.1570 1.4863 0.1609  -0.2842 -0.1287 126 MET   R N   
31232 C  CA  . MET   R  134 ? 1.7117 1.1074 1.4788 0.1728  -0.2828 -0.1215 126 MET   R CA  
31233 C  C   . MET   R  134 ? 1.6609 1.0942 1.4668 0.0890  -0.2807 -0.1807 126 MET   R C   
31234 O  O   . MET   R  134 ? 1.6375 1.1893 1.5090 0.1065  -0.3017 -0.1455 126 MET   R O   
31235 C  CB  . MET   R  134 ? 1.6803 0.9298 1.4544 0.2273  -0.3055 -0.1236 126 MET   R CB  
31236 C  CG  . MET   R  134 ? 1.7182 0.8323 1.4715 0.2754  -0.2862 -0.1186 126 MET   R CG  
31237 S  SD  . MET   R  134 ? 1.7507 0.6950 1.4901 0.3212  -0.3017 -0.0557 126 MET   R SD  
31238 C  CE  . MET   R  134 ? 1.7206 0.7300 1.5468 0.2786  -0.3132 -0.0398 126 MET   R CE  
31239 N  N   . SER   R  135 ? 1.6623 1.0507 1.4676 0.0849  -0.2272 -0.1979 127 SER   R N   
31240 C  CA  . SER   R  135 ? 1.6983 1.0399 1.4702 0.0977  -0.1910 -0.1934 127 SER   R CA  
31241 C  C   . SER   R  135 ? 1.6229 0.9481 1.4182 0.0309  -0.2582 -0.1417 127 SER   R C   
31242 O  O   . SER   R  135 ? 1.5988 0.9757 1.4186 0.0080  -0.3072 -0.1213 127 SER   R O   
31243 C  CB  . SER   R  135 ? 1.6982 1.1187 1.4457 0.0632  -0.1478 -0.2123 127 SER   R CB  
31244 O  OG  . SER   R  135 ? 1.8328 1.2153 1.4567 0.1380  -0.0080 -0.1701 127 SER   R OG  
31245 N  N   . ARG   R  136 ? 1.6089 0.8015 1.4047 0.0416  -0.2657 -0.1729 128 ARG   R N   
31246 C  CA  . ARG   R  136 ? 1.7235 0.6823 1.4334 0.0395  -0.2490 -0.1866 128 ARG   R CA  
31247 C  C   . ARG   R  136 ? 1.7259 0.6401 1.4729 0.0561  -0.2336 -0.2131 128 ARG   R C   
31248 O  O   . ARG   R  136 ? 1.7635 0.6409 1.5188 0.0132  -0.2959 -0.2089 128 ARG   R O   
31249 C  CB  . ARG   R  136 ? 1.7444 0.6229 1.4340 0.0594  -0.2178 -0.1877 128 ARG   R CB  
31250 C  CG  . ARG   R  136 ? 1.7956 0.6145 1.4216 0.0777  -0.1843 -0.1897 128 ARG   R CG  
31251 C  CD  . ARG   R  136 ? 1.8503 0.6073 1.4442 0.0786  -0.1351 -0.2177 128 ARG   R CD  
31252 N  NE  . ARG   R  136 ? 1.8672 0.5957 1.4028 0.0590  -0.1259 -0.2508 128 ARG   R NE  
31253 C  CZ  . ARG   R  136 ? 1.9166 0.5724 1.3697 0.0615  -0.1086 -0.2602 128 ARG   R CZ  
31254 N  NH1 . ARG   R  136 ? 1.9006 0.5165 1.4128 0.0477  -0.0787 -0.2663 128 ARG   R NH1 
31255 N  NH2 . ARG   R  136 ? 1.9339 0.5845 1.3378 0.0701  -0.0932 -0.2696 128 ARG   R NH2 
31256 N  N   . PRO   R  137 ? 1.8153 0.5387 1.4861 0.1055  -0.2003 -0.1877 129 PRO   R N   
31257 C  CA  . PRO   R  137 ? 1.8291 0.4837 1.4778 0.1305  -0.1701 -0.1594 129 PRO   R CA  
31258 C  C   . PRO   R  137 ? 1.8347 0.4888 1.4655 0.1043  -0.1406 -0.1891 129 PRO   R C   
31259 O  O   . PRO   R  137 ? 1.8212 0.3084 1.4074 0.1226  -0.1314 -0.1125 129 PRO   R O   
31260 C  CB  . PRO   R  137 ? 1.8251 0.5261 1.4885 0.1475  -0.1833 -0.1604 129 PRO   R CB  
31261 C  CG  . PRO   R  137 ? 1.8304 0.5907 1.4787 0.1197  -0.1892 -0.1610 129 PRO   R CG  
31262 C  CD  . PRO   R  137 ? 1.8380 0.5560 1.4774 0.0991  -0.2134 -0.1721 129 PRO   R CD  
31263 N  N   . PHE   R  138 ? 1.8332 0.6301 1.5350 0.0689  -0.0779 -0.2191 130 PHE   R N   
31264 C  CA  . PHE   R  138 ? 1.8453 0.6442 1.5362 0.0780  -0.0938 -0.2389 130 PHE   R CA  
31265 C  C   . PHE   R  138 ? 1.8257 0.5772 1.5401 0.0376  -0.1143 -0.2022 130 PHE   R C   
31266 O  O   . PHE   R  138 ? 1.8325 0.4975 1.6112 -0.0402 -0.1308 -0.1425 130 PHE   R O   
31267 C  CB  . PHE   R  138 ? 1.8729 0.6795 1.5903 0.0611  -0.0566 -0.2285 130 PHE   R CB  
31268 C  CG  . PHE   R  138 ? 1.8643 0.7256 1.6470 0.0904  -0.0467 -0.2730 130 PHE   R CG  
31269 C  CD1 . PHE   R  138 ? 1.8229 0.8255 1.6370 0.0905  -0.0581 -0.3191 130 PHE   R CD1 
31270 C  CD2 . PHE   R  138 ? 1.8535 0.8089 1.6594 0.0767  -0.0386 -0.3017 130 PHE   R CD2 
31271 C  CE1 . PHE   R  138 ? 1.7844 0.8430 1.6502 0.0940  -0.0318 -0.3333 130 PHE   R CE1 
31272 C  CE2 . PHE   R  138 ? 1.8428 0.8496 1.6618 0.1106  -0.0164 -0.3228 130 PHE   R CE2 
31273 C  CZ  . PHE   R  138 ? 1.8026 0.8643 1.6630 0.0764  -0.0298 -0.3374 130 PHE   R CZ  
31274 N  N   . GLY   R  139 ? 1.8023 0.4701 1.5211 0.0639  -0.1148 -0.1776 131 GLY   R N   
31275 C  CA  . GLY   R  139 ? 1.8062 0.4994 1.4454 0.0534  -0.1039 -0.1814 131 GLY   R CA  
31276 C  C   . GLY   R  139 ? 1.8168 0.5002 1.4328 0.1032  -0.0992 -0.1502 131 GLY   R C   
31277 O  O   . GLY   R  139 ? 1.7909 0.4975 1.4075 0.0734  -0.1009 -0.1262 131 GLY   R O   
31278 N  N   . VAL   R  140 ? 1.8090 0.4693 1.4019 0.1283  -0.0942 -0.1473 132 VAL   R N   
31279 C  CA  . VAL   R  140 ? 1.8277 0.5163 1.4100 0.1844  -0.0679 -0.1172 132 VAL   R CA  
31280 C  C   . VAL   R  140 ? 1.7897 0.4731 1.4143 0.2364  -0.0861 -0.0434 132 VAL   R C   
31281 O  O   . VAL   R  140 ? 1.7169 0.5023 1.3352 0.2462  -0.1112 0.0288  132 VAL   R O   
31282 C  CB  . VAL   R  140 ? 1.8673 0.5682 1.4345 0.2203  -0.0780 -0.1036 132 VAL   R CB  
31283 C  CG1 . VAL   R  140 ? 1.8622 0.6470 1.4519 0.2395  -0.0543 -0.1432 132 VAL   R CG1 
31284 C  CG2 . VAL   R  140 ? 1.8907 0.6153 1.4663 0.2240  -0.0377 -0.1270 132 VAL   R CG2 
31285 N  N   . ALA   R  141 ? 1.7784 0.4547 1.4101 0.2537  -0.1124 -0.0466 133 ALA   R N   
31286 C  CA  . ALA   R  141 ? 1.8006 0.5887 1.4442 0.2298  -0.1367 -0.0892 133 ALA   R CA  
31287 C  C   . ALA   R  141 ? 1.8133 0.6718 1.4031 0.2585  -0.1310 -0.0568 133 ALA   R C   
31288 O  O   . ALA   R  141 ? 1.8262 0.8161 1.4378 0.2647  -0.1801 -0.1113 133 ALA   R O   
31289 C  CB  . ALA   R  141 ? 1.8006 0.5586 1.4971 0.2071  -0.1142 -0.0776 133 ALA   R CB  
31290 N  N   . LEU   R  142 ? 1.8016 0.7440 1.3848 0.2635  -0.1434 -0.1029 134 LEU   R N   
31291 C  CA  . LEU   R  142 ? 1.7673 0.8122 1.3561 0.3019  -0.0889 -0.0727 134 LEU   R CA  
31292 C  C   . LEU   R  142 ? 1.7615 0.7922 1.3464 0.3418  -0.0702 -0.0908 134 LEU   R C   
31293 O  O   . LEU   R  142 ? 1.6129 0.7158 1.3661 0.4011  -0.0351 -0.1092 134 LEU   R O   
31294 C  CB  . LEU   R  142 ? 1.7883 0.8559 1.3462 0.3366  -0.0830 -0.0850 134 LEU   R CB  
31295 C  CG  . LEU   R  142 ? 1.7877 0.9184 1.3697 0.3243  -0.0601 -0.1084 134 LEU   R CG  
31296 C  CD1 . LEU   R  142 ? 1.8211 0.9386 1.3932 0.3328  -0.0482 -0.1292 134 LEU   R CD1 
31297 C  CD2 . LEU   R  142 ? 1.8164 0.9469 1.3587 0.2821  -0.0441 -0.1125 134 LEU   R CD2 
31298 N  N   . LEU   R  143 ? 1.7652 0.8017 1.3539 0.3412  -0.0722 -0.0697 135 LEU   R N   
31299 C  CA  . LEU   R  143 ? 1.7923 0.7914 1.4299 0.2790  -0.1070 -0.0494 135 LEU   R CA  
31300 C  C   . LEU   R  143 ? 1.7978 0.7925 1.4205 0.1905  -0.0977 -0.0542 135 LEU   R C   
31301 O  O   . LEU   R  143 ? 1.7813 0.8669 1.4755 0.1404  -0.1361 -0.0083 135 LEU   R O   
31302 C  CB  . LEU   R  143 ? 1.8396 0.9195 1.4582 0.2905  -0.0837 -0.0799 135 LEU   R CB  
31303 C  CG  . LEU   R  143 ? 1.9102 0.9244 1.5024 0.2536  -0.0979 -0.0775 135 LEU   R CG  
31304 C  CD1 . LEU   R  143 ? 1.9574 0.9490 1.5310 0.2424  -0.0753 -0.1091 135 LEU   R CD1 
31305 C  CD2 . LEU   R  143 ? 1.8961 0.9901 1.5201 0.2438  -0.1075 -0.0675 135 LEU   R CD2 
31306 N  N   . ILE   R  144 ? 1.8152 0.6669 1.4071 0.1710  -0.0678 -0.0204 136 ILE   R N   
31307 C  CA  . ILE   R  144 ? 1.8139 0.6565 1.4333 0.1794  -0.0311 -0.0713 136 ILE   R CA  
31308 C  C   . ILE   R  144 ? 1.8211 0.5242 1.5128 0.1685  -0.0296 -0.0841 136 ILE   R C   
31309 O  O   . ILE   R  144 ? 1.8139 0.4119 1.4748 0.1526  -0.0006 -0.0658 136 ILE   R O   
31310 C  CB  . ILE   R  144 ? 1.8146 0.6157 1.4459 0.1671  -0.0116 -0.0686 136 ILE   R CB  
31311 C  CG1 . ILE   R  144 ? 1.8209 0.5831 1.4073 0.1529  -0.0146 -0.0819 136 ILE   R CG1 
31312 C  CG2 . ILE   R  144 ? 1.8227 0.6356 1.4800 0.1336  0.0025  -0.0553 136 ILE   R CG2 
31313 C  CD1 . ILE   R  144 ? 1.8189 0.5714 1.4140 0.1517  -0.0052 -0.0767 136 ILE   R CD1 
31314 N  N   . ALA   R  145 ? 1.8348 0.5193 1.5542 0.1663  -0.0209 -0.0616 137 ALA   R N   
31315 C  CA  . ALA   R  145 ? 1.8095 0.6268 1.6709 0.1824  -0.0104 -0.0905 137 ALA   R CA  
31316 C  C   . ALA   R  145 ? 1.8566 0.6216 1.7330 0.1747  -0.0036 -0.1221 137 ALA   R C   
31317 O  O   . ALA   R  145 ? 1.7948 0.6580 1.8181 0.1562  -0.0140 -0.1531 137 ALA   R O   
31318 C  CB  . ALA   R  145 ? 1.8387 0.5889 1.7007 0.1900  -0.0137 -0.1148 137 ALA   R CB  
31319 N  N   . GLY   R  146 ? 1.8438 0.6238 1.7418 0.2090  -0.0171 -0.1493 138 GLY   R N   
31320 C  CA  . GLY   R  146 ? 1.8719 0.6352 1.7725 0.1849  0.0077  -0.1573 138 GLY   R CA  
31321 C  C   . GLY   R  146 ? 1.7969 0.6732 1.8016 0.2705  0.0333  -0.1329 138 GLY   R C   
31322 O  O   . GLY   R  146 ? 1.8152 0.6015 1.7915 0.2637  0.0650  -0.1385 138 GLY   R O   
31323 N  N   . HIS   R  147 ? 1.7803 0.7051 1.8022 0.1503  0.0295  -0.1006 139 HIS   R N   
31324 C  CA  . HIS   R  147 ? 1.7287 0.6527 1.7819 0.2093  0.0370  -0.1067 139 HIS   R CA  
31325 C  C   . HIS   R  147 ? 1.7821 0.5371 1.8460 0.1776  0.0043  -0.0838 139 HIS   R C   
31326 O  O   . HIS   R  147 ? 1.7907 0.4383 1.8323 0.1434  -0.0248 -0.1187 139 HIS   R O   
31327 C  CB  . HIS   R  147 ? 1.6763 0.6341 1.7912 0.2482  0.0414  -0.0925 139 HIS   R CB  
31328 C  CG  . HIS   R  147 ? 1.6440 0.5542 1.7758 0.2815  0.0734  -0.0900 139 HIS   R CG  
31329 N  ND1 . HIS   R  147 ? 1.5903 0.5598 1.7735 0.2992  0.0876  -0.1114 139 HIS   R ND1 
31330 C  CD2 . HIS   R  147 ? 1.6198 0.5620 1.7866 0.2545  0.0901  -0.0824 139 HIS   R CD2 
31331 C  CE1 . HIS   R  147 ? 1.5690 0.6201 1.8069 0.3178  0.1098  -0.1008 139 HIS   R CE1 
31332 N  NE2 . HIS   R  147 ? 1.6279 0.5244 1.8105 0.2677  0.1123  -0.0833 139 HIS   R NE2 
31333 N  N   . ASP   R  148 ? 1.7661 0.5769 1.8947 0.1917  -0.0244 -0.0365 140 ASP   R N   
31334 C  CA  . ASP   R  148 ? 1.7903 0.6352 1.8862 0.1700  -0.0272 -0.0636 140 ASP   R CA  
31335 C  C   . ASP   R  148 ? 1.7838 0.7223 1.9135 0.1636  -0.0170 -0.0601 140 ASP   R C   
31336 O  O   . ASP   R  148 ? 1.8475 0.5206 1.9747 0.1209  -0.0153 0.0117  140 ASP   R O   
31337 C  CB  . ASP   R  148 ? 1.7864 0.6048 1.8870 0.1843  -0.0301 -0.0460 140 ASP   R CB  
31338 C  CG  . ASP   R  148 ? 1.7803 0.4941 1.9740 0.1650  0.0001  -0.0421 140 ASP   R CG  
31339 O  OD1 . ASP   R  148 ? 1.7743 0.3287 2.0381 0.2286  -0.0043 -0.0212 140 ASP   R OD1 
31340 O  OD2 . ASP   R  148 ? 1.7721 0.6526 1.9822 0.1002  -0.0175 0.0086  140 ASP   R OD2 
31341 N  N   . ALA   R  149 ? 1.7794 0.7870 1.8614 0.1395  -0.0170 -0.1247 141 ALA   R N   
31342 C  CA  . ALA   R  149 ? 1.7548 0.9029 1.8637 0.1438  0.0076  -0.1343 141 ALA   R CA  
31343 C  C   . ALA   R  149 ? 1.7349 0.9414 1.8759 0.1791  0.0044  -0.1543 141 ALA   R C   
31344 O  O   . ALA   R  149 ? 1.7339 1.0043 1.9891 0.2649  -0.0179 -0.2031 141 ALA   R O   
31345 C  CB  . ALA   R  149 ? 1.7370 0.9043 1.8094 0.1231  0.0233  -0.1173 141 ALA   R CB  
31346 N  N   . ASP   R  150 ? 1.7100 0.9684 1.8510 0.1796  -0.0023 -0.1569 142 ASP   R N   
31347 C  CA  . ASP   R  150 ? 1.7063 1.0019 1.8521 0.1516  0.0070  -0.1208 142 ASP   R CA  
31348 C  C   . ASP   R  150 ? 1.7280 0.9508 1.8541 0.0743  0.0551  -0.1323 142 ASP   R C   
31349 O  O   . ASP   R  150 ? 1.7156 0.8793 1.8730 0.0511  0.0749  -0.1776 142 ASP   R O   
31350 C  CB  . ASP   R  150 ? 1.6984 1.1375 1.8268 0.1657  -0.0200 -0.0760 142 ASP   R CB  
31351 C  CG  . ASP   R  150 ? 1.7577 1.1708 1.8532 0.1949  -0.0458 -0.0900 142 ASP   R CG  
31352 O  OD1 . ASP   R  150 ? 1.7244 1.3773 1.7887 0.1217  -0.0727 -0.0633 142 ASP   R OD1 
31353 O  OD2 . ASP   R  150 ? 1.6975 1.3476 1.8941 0.1567  -0.0933 -0.0653 142 ASP   R OD2 
31354 N  N   . ASP   R  151 ? 1.6681 0.9271 1.8665 0.0774  0.0504  -0.0777 143 ASP   R N   
31355 C  CA  . ASP   R  151 ? 1.6396 0.8946 1.8693 0.0393  0.0640  -0.0215 143 ASP   R CA  
31356 C  C   . ASP   R  151 ? 1.6779 0.8339 1.8792 0.0972  0.0300  -0.0316 143 ASP   R C   
31357 O  O   . ASP   R  151 ? 1.6224 0.8111 1.8960 0.1009  0.0092  0.0276  143 ASP   R O   
31358 C  CB  . ASP   R  151 ? 1.6487 0.8484 1.9405 0.0158  0.0660  -0.0217 143 ASP   R CB  
31359 C  CG  . ASP   R  151 ? 1.6228 0.8929 1.9583 -0.0676 0.0779  -0.0628 143 ASP   R CG  
31360 O  OD1 . ASP   R  151 ? 1.6520 0.8612 1.9683 -0.0794 0.0929  -0.0313 143 ASP   R OD1 
31361 O  OD2 . ASP   R  151 ? 1.6323 0.9628 2.0524 -0.1397 0.1456  -0.0116 143 ASP   R OD2 
31362 N  N   . GLY   R  152 ? 1.7512 0.8792 1.8063 0.1226  0.0412  -0.0510 144 GLY   R N   
31363 C  CA  . GLY   R  152 ? 1.8114 0.8214 1.8172 0.1321  0.0917  -0.0584 144 GLY   R CA  
31364 C  C   . GLY   R  152 ? 1.8995 0.6400 1.7842 0.1551  0.1071  -0.0724 144 GLY   R C   
31365 O  O   . GLY   R  152 ? 1.9122 0.5342 1.7948 0.1057  0.1260  -0.0068 144 GLY   R O   
31366 N  N   . TYR   R  153 ? 1.8562 0.5308 1.8411 0.1840  0.1030  -0.0617 145 TYR   R N   
31367 C  CA  . TYR   R  153 ? 1.8414 0.5395 1.7759 0.2468  0.0945  -0.1180 145 TYR   R CA  
31368 C  C   . TYR   R  153 ? 1.7629 0.5365 1.7212 0.2886  0.0442  -0.1143 145 TYR   R C   
31369 O  O   . TYR   R  153 ? 1.7609 0.4353 1.7205 0.2845  0.0880  -0.0765 145 TYR   R O   
31370 C  CB  . TYR   R  153 ? 1.8571 0.5441 1.8095 0.2919  0.1209  -0.1147 145 TYR   R CB  
31371 C  CG  . TYR   R  153 ? 1.8913 0.4739 1.8608 0.3106  0.1403  -0.1192 145 TYR   R CG  
31372 C  CD1 . TYR   R  153 ? 1.9173 0.4614 1.8619 0.3315  0.1443  -0.1064 145 TYR   R CD1 
31373 C  CD2 . TYR   R  153 ? 1.8813 0.5009 1.8980 0.3310  0.1548  -0.1324 145 TYR   R CD2 
31374 C  CE1 . TYR   R  153 ? 1.9464 0.5603 1.8350 0.3602  0.1522  -0.0716 145 TYR   R CE1 
31375 C  CE2 . TYR   R  153 ? 1.9209 0.5806 1.8681 0.3578  0.1730  -0.1096 145 TYR   R CE2 
31376 C  CZ  . TYR   R  153 ? 1.9604 0.5706 1.8317 0.3673  0.1825  -0.0613 145 TYR   R CZ  
31377 O  OH  . TYR   R  153 ? 2.0064 0.5692 1.8581 0.3534  0.2429  -0.0537 145 TYR   R OH  
31378 N  N   . GLN   R  154 ? 1.7841 0.6181 1.7125 0.2317  0.0362  -0.1686 146 GLN   R N   
31379 C  CA  . GLN   R  154 ? 1.8002 0.6299 1.6812 0.2288  0.0324  -0.1851 146 GLN   R CA  
31380 C  C   . GLN   R  154 ? 1.8686 0.7005 1.7278 0.2072  -0.0361 -0.1928 146 GLN   R C   
31381 O  O   . GLN   R  154 ? 1.9275 0.7153 1.7429 0.2022  -0.0785 -0.1843 146 GLN   R O   
31382 C  CB  . GLN   R  154 ? 1.7518 0.6900 1.6757 0.1869  0.0174  -0.2279 146 GLN   R CB  
31383 C  CG  . GLN   R  154 ? 1.7196 0.7532 1.6564 0.1774  0.0457  -0.2455 146 GLN   R CG  
31384 C  CD  . GLN   R  154 ? 1.7125 0.7241 1.6175 0.1428  0.0410  -0.2358 146 GLN   R CD  
31385 O  OE1 . GLN   R  154 ? 1.6327 0.6126 1.5746 0.2074  0.0981  -0.3789 146 GLN   R OE1 
31386 N  NE2 . GLN   R  154 ? 1.7144 0.8714 1.5654 0.1272  0.0185  -0.2821 146 GLN   R NE2 
31387 N  N   . LEU   R  155 ? 1.9504 0.7150 1.7900 0.1535  -0.0393 -0.1808 147 LEU   R N   
31388 C  CA  . LEU   R  155 ? 1.9319 0.7927 1.7717 0.1421  -0.0545 -0.1734 147 LEU   R CA  
31389 C  C   . LEU   R  155 ? 1.8648 0.7853 1.7393 0.1871  -0.0816 -0.1617 147 LEU   R C   
31390 O  O   . LEU   R  155 ? 1.9652 0.6773 1.7146 0.2328  -0.0508 -0.1036 147 LEU   R O   
31391 C  CB  . LEU   R  155 ? 1.9498 0.7603 1.8466 0.1377  -0.0699 -0.2013 147 LEU   R CB  
31392 C  CG  . LEU   R  155 ? 2.0052 0.6858 1.8855 0.1351  -0.0680 -0.1732 147 LEU   R CG  
31393 C  CD1 . LEU   R  155 ? 2.0149 0.6810 1.8869 0.1086  -0.0830 -0.1763 147 LEU   R CD1 
31394 C  CD2 . LEU   R  155 ? 1.9851 0.6628 1.9202 0.1550  -0.0766 -0.1344 147 LEU   R CD2 
31395 N  N   . PHE   R  156 ? 1.8678 0.7281 1.6857 0.1795  -0.0508 -0.1737 148 PHE   R N   
31396 C  CA  . PHE   R  156 ? 1.8490 0.6186 1.6929 0.1681  -0.1032 -0.1312 148 PHE   R CA  
31397 C  C   . PHE   R  156 ? 1.8848 0.4421 1.6613 0.2190  -0.0942 -0.1179 148 PHE   R C   
31398 O  O   . PHE   R  156 ? 1.8566 0.2159 1.7131 0.2507  -0.1074 -0.1692 148 PHE   R O   
31399 C  CB  . PHE   R  156 ? 1.8236 0.6822 1.6958 0.1710  -0.0954 -0.1484 148 PHE   R CB  
31400 C  CG  . PHE   R  156 ? 1.7993 0.6686 1.7514 0.1579  -0.1318 -0.0860 148 PHE   R CG  
31401 C  CD1 . PHE   R  156 ? 1.7653 0.7020 1.7666 0.1606  -0.1491 -0.0788 148 PHE   R CD1 
31402 C  CD2 . PHE   R  156 ? 1.8071 0.6037 1.7919 0.1922  -0.1282 -0.1281 148 PHE   R CD2 
31403 C  CE1 . PHE   R  156 ? 1.7641 0.6031 1.7507 0.2040  -0.1399 -0.0901 148 PHE   R CE1 
31404 C  CE2 . PHE   R  156 ? 1.8016 0.5755 1.7643 0.2104  -0.1260 -0.1257 148 PHE   R CE2 
31405 C  CZ  . PHE   R  156 ? 1.7732 0.5484 1.7716 0.2283  -0.1307 -0.1349 148 PHE   R CZ  
31406 N  N   . HIS   R  157 ? 1.8672 0.5428 1.5916 0.2273  -0.1383 -0.0579 149 HIS   R N   
31407 C  CA  . HIS   R  157 ? 1.8572 0.5912 1.5352 0.2111  -0.1377 -0.0105 149 HIS   R CA  
31408 C  C   . HIS   R  157 ? 1.8336 0.5918 1.4981 0.2083  -0.1664 -0.0225 149 HIS   R C   
31409 O  O   . HIS   R  157 ? 1.8726 0.5997 1.4740 0.1130  -0.1513 -0.0157 149 HIS   R O   
31410 C  CB  . HIS   R  157 ? 1.8611 0.5895 1.5823 0.2125  -0.1521 0.0350  149 HIS   R CB  
31411 C  CG  . HIS   R  157 ? 1.8738 0.5319 1.5805 0.2309  -0.2071 0.0815  149 HIS   R CG  
31412 N  ND1 . HIS   R  157 ? 1.9140 0.5370 1.6174 0.1753  -0.2165 0.1061  149 HIS   R ND1 
31413 C  CD2 . HIS   R  157 ? 1.8880 0.4939 1.5749 0.2080  -0.2225 0.1042  149 HIS   R CD2 
31414 C  CE1 . HIS   R  157 ? 1.8896 0.5646 1.5755 0.1866  -0.2521 0.1418  149 HIS   R CE1 
31415 N  NE2 . HIS   R  157 ? 1.9063 0.4822 1.5937 0.2208  -0.2335 0.1249  149 HIS   R NE2 
31416 N  N   . ALA   R  158 ? 1.8492 0.5575 1.4154 0.2366  -0.1766 -0.0775 150 ALA   R N   
31417 C  CA  . ALA   R  158 ? 1.8472 0.6360 1.3729 0.2099  -0.2053 -0.1533 150 ALA   R CA  
31418 C  C   . ALA   R  158 ? 1.8237 0.6910 1.3891 0.1931  -0.2121 -0.1969 150 ALA   R C   
31419 O  O   . ALA   R  158 ? 1.9066 0.7118 1.3945 0.1228  -0.2371 -0.1601 150 ALA   R O   
31420 C  CB  . ALA   R  158 ? 1.8683 0.6289 1.3581 0.2010  -0.2118 -0.1601 150 ALA   R CB  
31421 N  N   . GLU   R  159 ? 1.7615 0.8003 1.3352 0.1964  -0.2112 -0.2198 151 GLU   R N   
31422 C  CA  . GLU   R  159 ? 1.7757 0.8858 1.4410 0.1347  -0.2215 -0.2522 151 GLU   R CA  
31423 C  C   . GLU   R  159 ? 1.7657 0.9556 1.4723 0.0846  -0.1971 -0.2802 151 GLU   R C   
31424 O  O   . GLU   R  159 ? 1.7810 1.0776 1.5375 0.0693  -0.1534 -0.3776 151 GLU   R O   
31425 C  CB  . GLU   R  159 ? 1.7954 0.9144 1.5184 0.1494  -0.2394 -0.2319 151 GLU   R CB  
31426 C  CG  . GLU   R  159 ? 1.7980 0.9433 1.5902 0.1680  -0.2296 -0.2508 151 GLU   R CG  
31427 C  CD  . GLU   R  159 ? 1.7942 1.0849 1.6664 0.2040  -0.2503 -0.1747 151 GLU   R CD  
31428 O  OE1 . GLU   R  159 ? 1.8632 1.1472 1.6043 0.1778  -0.2520 -0.2177 151 GLU   R OE1 
31429 O  OE2 . GLU   R  159 ? 1.7668 1.1492 1.6524 0.2438  -0.2488 -0.1470 151 GLU   R OE2 
31430 N  N   . PRO   R  160 ? 1.8685 0.9163 1.4951 0.0123  -0.1985 -0.2718 152 PRO   R N   
31431 C  CA  . PRO   R  160 ? 1.8795 0.8760 1.5155 -0.0313 -0.1822 -0.2363 152 PRO   R CA  
31432 C  C   . PRO   R  160 ? 1.9213 0.7900 1.5669 -0.0525 -0.2003 -0.1331 152 PRO   R C   
31433 O  O   . PRO   R  160 ? 1.9129 0.7791 1.6652 -0.1042 -0.1524 -0.1155 152 PRO   R O   
31434 C  CB  . PRO   R  160 ? 1.8813 0.9359 1.4887 -0.0368 -0.2086 -0.2416 152 PRO   R CB  
31435 C  CG  . PRO   R  160 ? 1.8751 0.9494 1.5112 0.0106  -0.1892 -0.2575 152 PRO   R CG  
31436 C  CD  . PRO   R  160 ? 1.8671 0.9047 1.4954 0.0241  -0.1756 -0.2729 152 PRO   R CD  
31437 N  N   . SER   R  161 ? 1.9407 0.7038 1.6663 -0.0098 -0.1472 -0.0605 153 SER   R N   
31438 C  CA  . SER   R  161 ? 1.9351 0.7180 1.6821 0.0027  -0.1477 -0.0042 153 SER   R CA  
31439 C  C   . SER   R  161 ? 1.9681 0.7921 1.6506 -0.0088 -0.1701 -0.0586 153 SER   R C   
31440 O  O   . SER   R  161 ? 2.0334 0.5442 1.6422 -0.0941 -0.1571 0.0581  153 SER   R O   
31441 C  CB  . SER   R  161 ? 1.9040 0.8083 1.7278 0.0097  -0.1489 0.0637  153 SER   R CB  
31442 O  OG  . SER   R  161 ? 1.9165 0.8014 1.8128 0.0081  -0.1572 0.1495  153 SER   R OG  
31443 N  N   . GLY   R  162 ? 1.9266 0.7990 1.5800 0.0106  -0.1685 -0.0868 154 GLY   R N   
31444 C  CA  . GLY   R  162 ? 1.8391 0.8243 1.5818 0.0835  -0.1815 -0.1771 154 GLY   R CA  
31445 C  C   . GLY   R  162 ? 1.8255 0.8916 1.6217 0.1962  -0.1646 -0.1808 154 GLY   R C   
31446 O  O   . GLY   R  162 ? 1.7689 1.0164 1.6770 0.1695  -0.2488 -0.2047 154 GLY   R O   
31447 N  N   . THR   R  163 ? 1.8246 0.8389 1.6227 0.1656  -0.1972 -0.2050 155 THR   R N   
31448 C  CA  . THR   R  163 ? 1.8367 0.7194 1.6487 0.2384  -0.1648 -0.1874 155 THR   R CA  
31449 C  C   . THR   R  163 ? 1.8384 0.6742 1.6378 0.2047  -0.1617 -0.2223 155 THR   R C   
31450 O  O   . THR   R  163 ? 1.8189 0.7482 1.6372 0.2504  -0.1536 -0.2703 155 THR   R O   
31451 C  CB  . THR   R  163 ? 1.8546 0.7792 1.7229 0.2542  -0.1949 -0.0796 155 THR   R CB  
31452 O  OG1 . THR   R  163 ? 1.8374 0.5828 1.6830 0.3426  -0.1943 -0.1256 155 THR   R OG1 
31453 C  CG2 . THR   R  163 ? 1.8598 0.8762 1.7773 0.2375  -0.2135 -0.0111 155 THR   R CG2 
31454 N  N   . PHE   R  164 ? 1.9005 0.5847 1.6060 0.1773  -0.1508 -0.2381 156 PHE   R N   
31455 C  CA  . PHE   R  164 ? 1.9255 0.6024 1.5959 0.1292  -0.1634 -0.2317 156 PHE   R CA  
31456 C  C   . PHE   R  164 ? 1.9156 0.5889 1.5754 0.0926  -0.1714 -0.2745 156 PHE   R C   
31457 O  O   . PHE   R  164 ? 1.8715 0.7045 1.6509 0.0242  -0.2321 -0.2608 156 PHE   R O   
31458 C  CB  . PHE   R  164 ? 1.9340 0.6244 1.5384 0.1209  -0.1747 -0.2034 156 PHE   R CB  
31459 C  CG  . PHE   R  164 ? 1.9050 0.5923 1.5399 0.1228  -0.1523 -0.2015 156 PHE   R CG  
31460 C  CD1 . PHE   R  164 ? 1.8649 0.5074 1.5342 0.1190  -0.1703 -0.2062 156 PHE   R CD1 
31461 C  CD2 . PHE   R  164 ? 1.9196 0.5477 1.5618 0.1219  -0.1425 -0.2372 156 PHE   R CD2 
31462 C  CE1 . PHE   R  164 ? 1.8525 0.5325 1.5388 0.1385  -0.1652 -0.2290 156 PHE   R CE1 
31463 C  CE2 . PHE   R  164 ? 1.9042 0.6108 1.5514 0.0982  -0.1498 -0.2471 156 PHE   R CE2 
31464 C  CZ  . PHE   R  164 ? 1.8464 0.6519 1.5566 0.1128  -0.1553 -0.2204 156 PHE   R CZ  
31465 N  N   . TYR   R  165 ? 2.0216 0.6578 1.5734 0.0869  -0.1279 -0.2944 157 TYR   R N   
31466 C  CA  . TYR   R  165 ? 2.0373 0.7807 1.5786 0.1077  -0.0935 -0.2917 157 TYR   R CA  
31467 C  C   . TYR   R  165 ? 1.9377 0.6861 1.6044 0.1292  -0.0465 -0.3434 157 TYR   R C   
31468 O  O   . TYR   R  165 ? 1.9261 0.7364 1.6056 0.1396  -0.0445 -0.3774 157 TYR   R O   
31469 C  CB  . TYR   R  165 ? 2.2121 0.7827 1.6052 0.1350  -0.1017 -0.2590 157 TYR   R CB  
31470 C  CG  . TYR   R  165 ? 2.4194 0.9228 1.5590 0.0621  -0.1364 -0.2382 157 TYR   R CG  
31471 C  CD1 . TYR   R  165 ? 2.4785 1.0536 1.5663 0.0386  -0.1735 -0.2137 157 TYR   R CD1 
31472 C  CD2 . TYR   R  165 ? 2.4740 0.8913 1.4868 -0.0118 -0.1962 -0.2813 157 TYR   R CD2 
31473 C  CE1 . TYR   R  165 ? 2.5535 1.1071 1.5862 -0.0080 -0.1680 -0.1862 157 TYR   R CE1 
31474 C  CE2 . TYR   R  165 ? 2.5826 0.9705 1.4763 -0.0826 -0.1573 -0.2603 157 TYR   R CE2 
31475 C  CZ  . TYR   R  165 ? 2.5993 1.0667 1.5713 -0.0560 -0.1752 -0.2262 157 TYR   R CZ  
31476 O  OH  . TYR   R  165 ? 2.6638 0.8601 1.6375 -0.1680 -0.0677 -0.2317 157 TYR   R OH  
31477 N  N   . ARG   R  166 ? 1.8635 0.6863 1.6024 0.1965  -0.0213 -0.3192 158 ARG   R N   
31478 C  CA  . ARG   R  166 ? 1.8675 0.7384 1.6578 0.2018  -0.0424 -0.2114 158 ARG   R CA  
31479 C  C   . ARG   R  166 ? 1.8862 0.6827 1.6442 0.2301  -0.0915 -0.1609 158 ARG   R C   
31480 O  O   . ARG   R  166 ? 1.9307 0.5677 1.7141 0.2490  -0.1202 -0.2247 158 ARG   R O   
31481 C  CB  . ARG   R  166 ? 1.7959 0.7012 1.6661 0.2238  0.0031  -0.1864 158 ARG   R CB  
31482 C  CG  . ARG   R  166 ? 1.7689 0.7449 1.7322 0.2160  0.0255  -0.1477 158 ARG   R CG  
31483 C  CD  . ARG   R  166 ? 1.7045 0.8294 1.7377 0.1930  0.0330  -0.1027 158 ARG   R CD  
31484 N  NE  . ARG   R  166 ? 1.7178 0.8455 1.7690 0.1693  0.0357  -0.0619 158 ARG   R NE  
31485 C  CZ  . ARG   R  166 ? 1.7055 0.7979 1.7142 0.1920  0.0254  -0.0672 158 ARG   R CZ  
31486 N  NH1 . ARG   R  166 ? 1.6269 0.6323 1.7428 0.2164  0.0198  -0.0622 158 ARG   R NH1 
31487 N  NH2 . ARG   R  166 ? 1.7062 0.8436 1.7764 0.1398  0.0525  -0.0465 158 ARG   R NH2 
31488 N  N   . TYR   R  167 ? 1.8839 0.7772 1.6487 0.1922  -0.1020 -0.1233 159 TYR   R N   
31489 C  CA  . TYR   R  167 ? 1.8316 0.7136 1.6943 0.2581  -0.1072 -0.0489 159 TYR   R CA  
31490 C  C   . TYR   R  167 ? 1.7675 0.7792 1.7539 0.2335  -0.0743 -0.0874 159 TYR   R C   
31491 O  O   . TYR   R  167 ? 1.8108 0.8098 1.7884 0.1350  -0.0754 0.0055  159 TYR   R O   
31492 C  CB  . TYR   R  167 ? 1.8107 0.7352 1.6990 0.2804  -0.1503 -0.0042 159 TYR   R CB  
31493 C  CG  . TYR   R  167 ? 1.7424 0.7625 1.6943 0.3310  -0.1824 0.0554  159 TYR   R CG  
31494 C  CD1 . TYR   R  167 ? 1.7074 0.7393 1.6666 0.3447  -0.2145 0.0685  159 TYR   R CD1 
31495 C  CD2 . TYR   R  167 ? 1.7307 0.7780 1.7239 0.3417  -0.1817 0.0734  159 TYR   R CD2 
31496 C  CE1 . TYR   R  167 ? 1.6752 0.7406 1.6576 0.3578  -0.2333 0.0788  159 TYR   R CE1 
31497 C  CE2 . TYR   R  167 ? 1.7329 0.7494 1.7361 0.3270  -0.1999 0.0584  159 TYR   R CE2 
31498 C  CZ  . TYR   R  167 ? 1.7135 0.7131 1.7078 0.3390  -0.2229 0.0599  159 TYR   R CZ  
31499 O  OH  . TYR   R  167 ? 1.7094 0.6140 1.7210 0.3564  -0.2067 0.0003  159 TYR   R OH  
31500 N  N   . ASN   R  168 ? 1.8485 0.6134 1.7655 0.2978  -0.1173 -0.0491 160 ASN   R N   
31501 C  CA  . ASN   R  168 ? 1.8997 0.6753 1.7872 0.3566  -0.0641 -0.0833 160 ASN   R CA  
31502 C  C   . ASN   R  168 ? 1.9169 0.6840 1.7975 0.3511  -0.0395 -0.1352 160 ASN   R C   
31503 O  O   . ASN   R  168 ? 1.9682 0.6922 1.8507 0.3936  0.0146  -0.0959 160 ASN   R O   
31504 C  CB  . ASN   R  168 ? 1.9294 0.7094 1.8086 0.3800  -0.1086 -0.0161 160 ASN   R CB  
31505 C  CG  . ASN   R  168 ? 1.9299 0.7283 1.8009 0.4087  -0.1325 0.0045  160 ASN   R CG  
31506 O  OD1 . ASN   R  168 ? 1.9768 0.8616 1.8444 0.3871  -0.1843 0.0825  160 ASN   R OD1 
31507 N  ND2 . ASN   R  168 ? 1.9010 0.7213 1.8044 0.4856  -0.1031 -0.0277 160 ASN   R ND2 
31508 N  N   . ALA   R  169 ? 1.9184 0.6892 1.7659 0.3444  -0.0112 -0.1620 161 ALA   R N   
31509 C  CA  . ALA   R  169 ? 1.9602 0.7214 1.7045 0.3461  0.0353  -0.2302 161 ALA   R CA  
31510 C  C   . ALA   R  169 ? 1.9153 0.7129 1.6329 0.3456  0.0060  -0.2689 161 ALA   R C   
31511 O  O   . ALA   R  169 ? 1.9325 0.8394 1.6106 0.3888  -0.0028 -0.2688 161 ALA   R O   
31512 C  CB  . ALA   R  169 ? 2.0114 0.7595 1.7029 0.3404  0.0554  -0.2506 161 ALA   R CB  
31513 N  N   . LYS   R  170 ? 1.9009 0.6256 1.5825 0.2864  0.0367  -0.3009 162 LYS   R N   
31514 C  CA  . LYS   R  170 ? 1.9279 0.6352 1.5873 0.2547  0.0274  -0.2837 162 LYS   R CA  
31515 C  C   . LYS   R  170 ? 1.9452 0.7073 1.5588 0.2517  0.0279  -0.2375 162 LYS   R C   
31516 O  O   . LYS   R  170 ? 1.9407 0.6262 1.5977 0.2349  0.1044  -0.2251 162 LYS   R O   
31517 C  CB  . LYS   R  170 ? 1.8805 0.6062 1.5379 0.2300  -0.0247 -0.2799 162 LYS   R CB  
31518 C  CG  . LYS   R  170 ? 1.8782 0.6271 1.5169 0.2086  -0.0683 -0.2459 162 LYS   R CG  
31519 C  CD  . LYS   R  170 ? 1.8875 0.7178 1.5235 0.2395  -0.1082 -0.1706 162 LYS   R CD  
31520 C  CE  . LYS   R  170 ? 1.8643 0.8529 1.5298 0.2386  -0.1257 -0.1342 162 LYS   R CE  
31521 N  NZ  . LYS   R  170 ? 1.8876 0.8996 1.5628 0.2277  -0.1597 -0.0654 162 LYS   R NZ  
31522 N  N   . ALA   R  171 ? 2.0201 0.7327 1.5806 0.2105  0.0485  -0.2379 163 ALA   R N   
31523 C  CA  . ALA   R  171 ? 2.0471 0.7044 1.5173 0.2167  0.0494  -0.2323 163 ALA   R CA  
31524 C  C   . ALA   R  171 ? 1.9960 0.5966 1.4977 0.2441  0.0117  -0.2067 163 ALA   R C   
31525 O  O   . ALA   R  171 ? 2.0790 0.4880 1.4477 0.1674  0.0485  -0.2447 163 ALA   R O   
31526 C  CB  . ALA   R  171 ? 2.0904 0.7528 1.5089 0.2491  0.0724  -0.2410 163 ALA   R CB  
31527 N  N   . ILE   R  172 ? 2.0259 0.5564 1.4742 0.2928  0.0005  -0.1495 164 ILE   R N   
31528 C  CA  . ILE   R  172 ? 1.9842 0.6364 1.4748 0.3059  -0.0457 -0.0787 164 ILE   R CA  
31529 C  C   . ILE   R  172 ? 1.9931 0.6059 1.4994 0.3447  -0.0729 -0.0806 164 ILE   R C   
31530 O  O   . ILE   R  172 ? 2.0029 0.5693 1.5077 0.3562  -0.0471 -0.0803 164 ILE   R O   
31531 C  CB  . ILE   R  172 ? 1.9485 0.6740 1.4399 0.3067  -0.0426 -0.0759 164 ILE   R CB  
31532 C  CG1 . ILE   R  172 ? 1.9584 0.6909 1.4272 0.2795  -0.0288 -0.0675 164 ILE   R CG1 
31533 C  CG2 . ILE   R  172 ? 1.9285 0.7120 1.4573 0.3005  -0.0632 -0.0320 164 ILE   R CG2 
31534 C  CD1 . ILE   R  172 ? 1.9457 0.6828 1.4105 0.2669  -0.0359 -0.0798 164 ILE   R CD1 
31535 N  N   . GLY   R  173 ? 2.0065 0.6338 1.5164 0.3413  -0.0829 -0.0410 165 GLY   R N   
31536 C  CA  . GLY   R  173 ? 2.0460 0.7118 1.4964 0.3407  -0.1180 -0.0468 165 GLY   R CA  
31537 C  C   . GLY   R  173 ? 2.0970 0.7256 1.5254 0.3485  -0.1405 -0.0834 165 GLY   R C   
31538 O  O   . GLY   R  173 ? 2.1073 0.7410 1.6243 0.4249  -0.1600 -0.1180 165 GLY   R O   
31539 N  N   . SER   R  174 ? 2.1496 0.8344 1.5066 0.3053  -0.1189 -0.1137 166 SER   R N   
31540 C  CA  . SER   R  174 ? 2.1823 0.8630 1.5031 0.2862  -0.0616 -0.1626 166 SER   R CA  
31541 C  C   . SER   R  174 ? 2.1923 0.9843 1.5217 0.2438  0.0622  -0.1644 166 SER   R C   
31542 O  O   . SER   R  174 ? 2.3800 1.0794 1.5701 0.3513  0.0547  -0.1156 166 SER   R O   
31543 C  CB  . SER   R  174 ? 2.1931 0.9171 1.4481 0.2706  -0.0418 -0.1407 166 SER   R CB  
31544 O  OG  . SER   R  174 ? 2.2027 0.7693 1.4551 0.2364  -0.0149 -0.1982 166 SER   R OG  
31545 N  N   . GLY   R  175 ? 2.2100 0.9096 1.5613 0.2125  0.0902  -0.2063 167 GLY   R N   
31546 C  CA  . GLY   R  175 ? 2.2176 0.9349 1.6114 0.1531  0.1683  -0.2122 167 GLY   R CA  
31547 C  C   . GLY   R  175 ? 2.1987 0.9511 1.6158 0.1303  0.1983  -0.2336 167 GLY   R C   
31548 O  O   . GLY   R  175 ? 2.2035 0.9097 1.5693 0.1108  0.1930  -0.3396 167 GLY   R O   
31549 N  N   . SER   R  176 ? 2.2095 1.0274 1.6202 0.1620  0.3140  -0.1483 168 SER   R N   
31550 C  CA  . SER   R  176 ? 2.1486 0.8881 1.7264 0.1815  0.3231  -0.1137 168 SER   R CA  
31551 C  C   . SER   R  176 ? 2.1886 0.9024 1.8453 0.2007  0.3458  0.0291  168 SER   R C   
31552 O  O   . SER   R  176 ? 2.1958 0.7835 1.9184 0.2023  0.3235  0.0664  168 SER   R O   
31553 C  CB  . SER   R  176 ? 2.1874 0.8530 1.7802 0.1555  0.3310  -0.1861 168 SER   R CB  
31554 O  OG  . SER   R  176 ? 2.2507 0.9353 1.7370 0.1575  0.4301  -0.2069 168 SER   R OG  
31555 N  N   . GLU   R  177 ? 2.1853 0.8604 1.8770 0.3840  0.2487  0.0987  169 GLU   R N   
31556 C  CA  . GLU   R  177 ? 2.2594 0.6563 1.8693 0.3607  0.2445  0.0963  169 GLU   R CA  
31557 C  C   . GLU   R  177 ? 2.2701 0.3472 1.8907 0.4219  0.1970  0.0663  169 GLU   R C   
31558 O  O   . GLU   R  177 ? 2.2688 0.2618 1.8841 0.4572  0.2340  -0.0074 169 GLU   R O   
31559 C  CB  . GLU   R  177 ? 2.2657 0.7908 1.8719 0.3034  0.2222  0.1684  169 GLU   R CB  
31560 C  CG  . GLU   R  177 ? 2.3159 0.8788 1.8540 0.2436  0.2164  0.1405  169 GLU   R CG  
31561 C  CD  . GLU   R  177 ? 2.3825 1.0000 1.8867 0.2724  0.1864  0.2959  169 GLU   R CD  
31562 O  OE1 . GLU   R  177 ? 2.4251 1.2998 1.8406 0.1883  0.2286  0.2626  169 GLU   R OE1 
31563 O  OE2 . GLU   R  177 ? 2.3839 0.9246 1.8890 0.2279  0.2099  0.4797  169 GLU   R OE2 
31564 N  N   . GLY   R  178 ? 2.2518 0.4125 1.9241 0.3980  0.1377  0.0809  170 GLY   R N   
31565 C  CA  . GLY   R  178 ? 2.2365 0.6645 1.9510 0.4480  0.1231  0.0409  170 GLY   R CA  
31566 C  C   . GLY   R  178 ? 2.1913 0.6916 2.0311 0.4144  0.1203  0.0006  170 GLY   R C   
31567 O  O   . GLY   R  178 ? 2.1882 0.9171 2.1845 0.4555  0.1137  -0.0734 170 GLY   R O   
31568 N  N   . ALA   R  179 ? 2.2419 0.7476 1.9824 0.4671  0.0625  0.0035  171 ALA   R N   
31569 C  CA  . ALA   R  179 ? 2.2584 0.8208 1.8949 0.4124  0.0793  0.0046  171 ALA   R CA  
31570 C  C   . ALA   R  179 ? 2.2738 0.8275 1.8649 0.4827  0.0584  -0.0260 171 ALA   R C   
31571 O  O   . ALA   R  179 ? 2.2349 0.9077 1.8251 0.4780  0.0749  -0.1146 171 ALA   R O   
31572 C  CB  . ALA   R  179 ? 2.2503 0.8476 1.8835 0.4333  0.0869  -0.0413 171 ALA   R CB  
31573 N  N   . GLN   R  180 ? 2.2547 0.7143 1.8235 0.5009  -0.0297 -0.0214 172 GLN   R N   
31574 C  CA  . GLN   R  180 ? 2.2506 0.7160 1.8107 0.5199  -0.0467 -0.0059 172 GLN   R CA  
31575 C  C   . GLN   R  180 ? 2.2035 0.7416 1.8760 0.4852  -0.0403 -0.0129 172 GLN   R C   
31576 O  O   . GLN   R  180 ? 2.2121 0.5088 1.8781 0.5256  -0.0006 0.0025  172 GLN   R O   
31577 C  CB  . GLN   R  180 ? 2.2852 0.7663 1.7328 0.5044  -0.1102 0.0366  172 GLN   R CB  
31578 C  CG  . GLN   R  180 ? 2.3047 0.9640 1.7052 0.4746  -0.1354 0.0404  172 GLN   R CG  
31579 C  CD  . GLN   R  180 ? 2.3465 0.9768 1.7014 0.4703  -0.1406 -0.0037 172 GLN   R CD  
31580 O  OE1 . GLN   R  180 ? 2.2853 1.1003 1.7055 0.5126  -0.1581 -0.0404 172 GLN   R OE1 
31581 N  NE2 . GLN   R  180 ? 2.3609 1.1924 1.6801 0.4524  -0.1467 -0.0504 172 GLN   R NE2 
31582 N  N   . ALA   R  181 ? 2.2331 0.7732 1.9357 0.4319  -0.0244 -0.0974 173 ALA   R N   
31583 C  CA  . ALA   R  181 ? 2.2190 0.7590 1.9884 0.4118  0.0001  -0.1212 173 ALA   R CA  
31584 C  C   . ALA   R  181 ? 2.1882 0.8269 2.0220 0.3944  0.0324  -0.1657 173 ALA   R C   
31585 O  O   . ALA   R  181 ? 2.1759 0.8112 2.0577 0.3737  0.0613  -0.2103 173 ALA   R O   
31586 C  CB  . ALA   R  181 ? 2.2632 0.7588 2.0142 0.3828  -0.0144 -0.0602 173 ALA   R CB  
31587 N  N   . GLU   R  182 ? 2.1597 0.8557 2.0090 0.4091  0.0573  -0.1590 174 GLU   R N   
31588 C  CA  . GLU   R  182 ? 2.1370 0.9145 2.0363 0.4352  0.0886  -0.1508 174 GLU   R CA  
31589 C  C   . GLU   R  182 ? 2.0885 0.9206 2.0137 0.4412  0.0796  -0.1536 174 GLU   R C   
31590 O  O   . GLU   R  182 ? 2.0967 0.8937 1.9816 0.5123  0.1262  -0.1382 174 GLU   R O   
31591 C  CB  . GLU   R  182 ? 2.1490 0.9939 2.0300 0.4655  0.1004  -0.1133 174 GLU   R CB  
31592 C  CG  . GLU   R  182 ? 2.1740 1.1413 2.0628 0.4186  0.1421  -0.1247 174 GLU   R CG  
31593 C  CD  . GLU   R  182 ? 2.1897 1.1344 2.0933 0.3674  0.1451  -0.1550 174 GLU   R CD  
31594 O  OE1 . GLU   R  182 ? 2.1512 1.3560 2.1989 0.2921  0.1509  -0.1279 174 GLU   R OE1 
31595 O  OE2 . GLU   R  182 ? 2.2608 1.2172 2.0271 0.2768  0.1117  -0.1621 174 GLU   R OE2 
31596 N  N   . LEU   R  183 ? 2.0902 0.8728 2.0236 0.4049  0.0643  -0.1757 175 LEU   R N   
31597 C  CA  . LEU   R  183 ? 2.1203 0.8902 2.0418 0.3676  0.0814  -0.1796 175 LEU   R CA  
31598 C  C   . LEU   R  183 ? 2.0680 0.8993 2.0511 0.3348  0.0957  -0.2243 175 LEU   R C   
31599 O  O   . LEU   R  183 ? 2.0338 0.8560 1.9811 0.3658  0.1073  -0.2423 175 LEU   R O   
31600 C  CB  . LEU   R  183 ? 2.1427 0.8800 2.0348 0.3207  0.1201  -0.2239 175 LEU   R CB  
31601 C  CG  . LEU   R  183 ? 2.1609 0.9172 2.0290 0.2629  0.0825  -0.2342 175 LEU   R CG  
31602 C  CD1 . LEU   R  183 ? 2.1244 0.9045 1.9975 0.2069  0.0800  -0.2409 175 LEU   R CD1 
31603 C  CD2 . LEU   R  183 ? 2.2228 0.8835 2.0889 0.2454  0.1049  -0.2505 175 LEU   R CD2 
31604 N  N   . LEU   R  184 ? 2.1003 0.9902 2.0038 0.3591  0.0729  -0.1918 176 LEU   R N   
31605 C  CA  . LEU   R  184 ? 2.0438 1.1132 2.0306 0.3453  0.0765  -0.2423 176 LEU   R CA  
31606 C  C   . LEU   R  184 ? 1.9130 1.1269 2.1717 0.2760  0.0215  -0.2295 176 LEU   R C   
31607 O  O   . LEU   R  184 ? 1.8895 0.9351 2.2617 0.2748  0.0944  -0.2841 176 LEU   R O   
31608 C  CB  . LEU   R  184 ? 2.1344 1.1511 1.9847 0.3504  0.1057  -0.2371 176 LEU   R CB  
31609 C  CG  . LEU   R  184 ? 2.1602 1.1747 1.9783 0.3676  0.1242  -0.2638 176 LEU   R CG  
31610 C  CD1 . LEU   R  184 ? 2.0959 1.1440 1.9622 0.4135  0.1731  -0.2731 176 LEU   R CD1 
31611 C  CD2 . LEU   R  184 ? 2.1914 1.1450 1.9534 0.3606  0.1158  -0.2929 176 LEU   R CD2 
31612 N  N   . ASN   R  185 ? 1.9902 1.2492 2.1508 0.3131  0.0251  -0.2328 177 ASN   R N   
31613 C  CA  . ASN   R  185 ? 1.9597 1.3253 2.2716 0.3384  0.0495  -0.1485 177 ASN   R CA  
31614 C  C   . ASN   R  185 ? 2.0418 1.2671 2.2663 0.3567  0.0807  -0.1911 177 ASN   R C   
31615 O  O   . ASN   R  185 ? 2.0446 1.4131 2.2823 0.3393  0.0613  -0.1712 177 ASN   R O   
31616 C  CB  . ASN   R  185 ? 1.9855 1.2024 2.3023 0.3496  0.0055  -0.0648 177 ASN   R CB  
31617 C  CG  . ASN   R  185 ? 1.9522 1.2307 2.4116 0.4073  -0.0607 0.0126  177 ASN   R CG  
31618 O  OD1 . ASN   R  185 ? 1.8728 1.1293 2.5427 0.3936  -0.1011 0.0810  177 ASN   R OD1 
31619 N  ND2 . ASN   R  185 ? 1.9869 1.2284 2.4059 0.3918  -0.0932 0.0560  177 ASN   R ND2 
31620 N  N   . GLU   R  186 ? 2.0803 1.1641 2.2821 0.4367  0.1104  -0.3045 178 GLU   R N   
31621 C  CA  . GLU   R  186 ? 2.1817 1.2017 2.2464 0.4583  0.1628  -0.3300 178 GLU   R CA  
31622 C  C   . GLU   R  186 ? 2.2185 1.2007 2.1924 0.4523  0.1840  -0.3126 178 GLU   R C   
31623 O  O   . GLU   R  186 ? 2.2511 1.3129 2.2332 0.4847  0.2472  -0.2482 178 GLU   R O   
31624 C  CB  . GLU   R  186 ? 2.2022 1.2414 2.2526 0.4762  0.1398  -0.4283 178 GLU   R CB  
31625 C  CG  . GLU   R  186 ? 2.2326 1.2821 2.2752 0.5311  0.1667  -0.5090 178 GLU   R CG  
31626 C  CD  . GLU   R  186 ? 2.2479 1.3224 2.3334 0.5613  0.1864  -0.5951 178 GLU   R CD  
31627 O  OE1 . GLU   R  186 ? 2.3624 1.2916 2.2790 0.5946  0.2513  -0.6916 178 GLU   R OE1 
31628 O  OE2 . GLU   R  186 ? 2.2225 1.3853 2.3143 0.6256  0.3071  -0.6079 178 GLU   R OE2 
31629 N  N   . TRP   R  187 ? 2.2176 1.1067 2.1299 0.4427  0.1577  -0.2537 179 TRP   R N   
31630 C  CA  . TRP   R  187 ? 2.1449 1.0262 2.0746 0.4745  0.1847  -0.1783 179 TRP   R CA  
31631 C  C   . TRP   R  187 ? 2.1107 0.9406 2.1032 0.4814  0.2122  -0.1840 179 TRP   R C   
31632 O  O   . TRP   R  187 ? 2.0889 1.0535 2.1878 0.4989  0.1743  -0.1143 179 TRP   R O   
31633 C  CB  . TRP   R  187 ? 2.1776 0.9522 2.0198 0.4485  0.1715  -0.1850 179 TRP   R CB  
31634 C  CG  . TRP   R  187 ? 2.2298 0.9699 2.0316 0.3923  0.1448  -0.1954 179 TRP   R CG  
31635 C  CD1 . TRP   R  187 ? 2.2322 0.9329 2.0408 0.4104  0.1539  -0.2500 179 TRP   R CD1 
31636 C  CD2 . TRP   R  187 ? 2.2607 0.9355 2.0049 0.4292  0.1299  -0.1899 179 TRP   R CD2 
31637 N  NE1 . TRP   R  187 ? 2.2546 0.9076 2.0174 0.4495  0.1570  -0.2504 179 TRP   R NE1 
31638 C  CE2 . TRP   R  187 ? 2.2688 0.9337 1.9723 0.4309  0.1451  -0.2865 179 TRP   R CE2 
31639 C  CE3 . TRP   R  187 ? 2.2503 0.9898 1.9673 0.3858  0.1117  -0.1935 179 TRP   R CE3 
31640 C  CZ2 . TRP   R  187 ? 2.2541 0.9060 1.9401 0.4388  0.1298  -0.2543 179 TRP   R CZ2 
31641 C  CZ3 . TRP   R  187 ? 2.2259 0.9082 1.9461 0.4581  0.1411  -0.2232 179 TRP   R CZ3 
31642 C  CH2 . TRP   R  187 ? 2.2203 0.9010 1.9328 0.4391  0.1335  -0.2805 179 TRP   R CH2 
31643 N  N   . HIS   R  188 ? 1.9690 1.0543 2.0639 0.4188  0.2266  -0.2070 180 HIS   R N   
31644 C  CA  . HIS   R  188 ? 1.9348 1.2011 2.0901 0.4102  0.2332  -0.2081 180 HIS   R CA  
31645 C  C   . HIS   R  188 ? 1.8660 1.1760 2.1086 0.3428  0.2384  -0.1638 180 HIS   R C   
31646 O  O   . HIS   R  188 ? 1.7915 0.9661 2.1330 0.3098  0.3177  -0.1512 180 HIS   R O   
31647 C  CB  . HIS   R  188 ? 1.9401 1.3517 2.0828 0.4366  0.2281  -0.2288 180 HIS   R CB  
31648 C  CG  . HIS   R  188 ? 1.9756 1.5222 2.0518 0.4497  0.2643  -0.2493 180 HIS   R CG  
31649 N  ND1 . HIS   R  188 ? 1.9353 1.5795 2.0324 0.4384  0.2992  -0.2543 180 HIS   R ND1 
31650 C  CD2 . HIS   R  188 ? 2.0146 1.5526 2.0303 0.4431  0.2917  -0.2711 180 HIS   R CD2 
31651 C  CE1 . HIS   R  188 ? 1.9819 1.6700 2.0121 0.4397  0.3506  -0.2790 180 HIS   R CE1 
31652 N  NE2 . HIS   R  188 ? 2.0200 1.6699 1.9932 0.4325  0.3433  -0.2779 180 HIS   R NE2 
31653 N  N   . SER   R  189 ? 1.8922 1.0959 2.1551 0.2927  0.2581  -0.1657 181 SER   R N   
31654 C  CA  . SER   R  189 ? 1.8668 1.0917 2.1469 0.2696  0.2986  -0.1560 181 SER   R CA  
31655 C  C   . SER   R  189 ? 1.8850 1.1868 2.1080 0.1864  0.3182  -0.1703 181 SER   R C   
31656 O  O   . SER   R  189 ? 1.8407 1.1647 2.0795 0.1060  0.3481  -0.1063 181 SER   R O   
31657 C  CB  . SER   R  189 ? 1.8065 1.1051 2.2113 0.2956  0.2797  -0.1590 181 SER   R CB  
31658 O  OG  . SER   R  189 ? 1.8234 1.0545 2.3472 0.3256  0.3045  -0.1611 181 SER   R OG  
31659 N  N   . SER   R  190 ? 1.9257 1.1691 2.0992 0.1212  0.3567  -0.1563 182 SER   R N   
31660 C  CA  . SER   R  190 ? 1.9239 1.1240 2.1407 0.0865  0.3833  -0.1716 182 SER   R CA  
31661 C  C   . SER   R  190 ? 2.0334 1.0498 2.0685 0.0821  0.4035  -0.1562 182 SER   R C   
31662 O  O   . SER   R  190 ? 2.0010 0.9676 2.1157 0.0571  0.4464  -0.1655 182 SER   R O   
31663 C  CB  . SER   R  190 ? 1.8815 1.2149 2.1407 0.0390  0.3719  -0.1495 182 SER   R CB  
31664 O  OG  . SER   R  190 ? 1.7910 1.2589 2.1732 0.0291  0.3684  -0.1374 182 SER   R OG  
31665 N  N   . LEU   R  191 ? 2.0337 1.0267 2.0816 0.0860  0.3731  -0.1954 183 LEU   R N   
31666 C  CA  . LEU   R  191 ? 2.1330 0.9849 2.0324 0.1334  0.3618  -0.1879 183 LEU   R CA  
31667 C  C   . LEU   R  191 ? 2.1639 0.9289 2.0530 0.1277  0.3756  -0.2363 183 LEU   R C   
31668 O  O   . LEU   R  191 ? 2.1311 0.8692 2.0525 0.1699  0.3851  -0.1800 183 LEU   R O   
31669 C  CB  . LEU   R  191 ? 2.1230 1.0391 2.0107 0.1498  0.3797  -0.1684 183 LEU   R CB  
31670 C  CG  . LEU   R  191 ? 2.1463 1.0447 2.0316 0.1761  0.3933  -0.1338 183 LEU   R CG  
31671 C  CD1 . LEU   R  191 ? 2.1408 1.0317 2.0184 0.1775  0.3739  -0.1125 183 LEU   R CD1 
31672 C  CD2 . LEU   R  191 ? 2.1733 1.0793 2.0303 0.1855  0.4070  -0.1437 183 LEU   R CD2 
31673 N  N   . THR   R  192 ? 2.2269 1.0232 2.0440 0.1103  0.4107  -0.2934 184 THR   R N   
31674 C  CA  . THR   R  192 ? 2.2289 1.1562 2.0554 0.1642  0.4195  -0.2368 184 THR   R CA  
31675 C  C   . THR   R  192 ? 2.2269 1.1122 2.0493 0.1205  0.4267  -0.2480 184 THR   R C   
31676 O  O   . THR   R  192 ? 2.1372 1.0363 2.0695 0.1688  0.4448  -0.3694 184 THR   R O   
31677 C  CB  . THR   R  192 ? 2.2587 1.3668 2.1201 0.1519  0.4954  -0.2635 184 THR   R CB  
31678 O  OG1 . THR   R  192 ? 2.3172 1.2404 2.1574 0.1489  0.5501  -0.2298 184 THR   R OG1 
31679 C  CG2 . THR   R  192 ? 2.2481 1.4761 2.1409 0.1536  0.5278  -0.2643 184 THR   R CG2 
31680 N  N   . LEU   R  193 ? 2.2249 1.2645 2.0453 0.2122  0.3767  -0.1786 185 LEU   R N   
31681 C  CA  . LEU   R  193 ? 2.2415 1.2073 2.0048 0.1959  0.3107  -0.1447 185 LEU   R CA  
31682 C  C   . LEU   R  193 ? 2.2297 1.0024 2.0276 0.1602  0.2671  -0.0548 185 LEU   R C   
31683 O  O   . LEU   R  193 ? 2.3132 0.8249 1.9985 0.1757  0.2103  0.0490  185 LEU   R O   
31684 C  CB  . LEU   R  193 ? 2.3308 1.2278 2.0434 0.2400  0.3469  -0.1578 185 LEU   R CB  
31685 C  CG  . LEU   R  193 ? 2.3354 1.3381 2.0305 0.2469  0.3591  -0.1758 185 LEU   R CG  
31686 C  CD1 . LEU   R  193 ? 2.3434 1.3843 2.0058 0.2471  0.3335  -0.1613 185 LEU   R CD1 
31687 C  CD2 . LEU   R  193 ? 2.3372 1.3428 2.0317 0.2358  0.3695  -0.1575 185 LEU   R CD2 
31688 N  N   . LYS   R  194 ? 2.2236 1.0637 1.9757 0.1418  0.2272  -0.1078 186 LYS   R N   
31689 C  CA  . LYS   R  194 ? 2.2733 1.1853 1.9628 0.1288  0.2194  -0.1398 186 LYS   R CA  
31690 C  C   . LYS   R  194 ? 2.2913 1.1849 1.9694 0.2018  0.1625  -0.1817 186 LYS   R C   
31691 O  O   . LYS   R  194 ? 2.3430 1.2632 2.0469 0.1810  0.1437  -0.2544 186 LYS   R O   
31692 C  CB  . LYS   R  194 ? 2.2992 1.3295 1.9368 0.0743  0.2264  -0.1815 186 LYS   R CB  
31693 C  CG  . LYS   R  194 ? 2.2950 1.4188 1.8263 0.0504  0.2231  -0.1457 186 LYS   R CG  
31694 C  CD  . LYS   R  194 ? 2.3210 1.5283 1.8058 0.0197  0.2309  -0.1701 186 LYS   R CD  
31695 C  CE  . LYS   R  194 ? 2.3304 1.5436 1.7769 0.0010  0.2473  -0.1553 186 LYS   R CE  
31696 N  NZ  . LYS   R  194 ? 2.3238 1.5677 1.7807 0.0000  0.2427  -0.1546 186 LYS   R NZ  
31697 N  N   . GLU   R  195 ? 2.2932 1.1392 1.9907 0.2425  0.1606  -0.1985 187 GLU   R N   
31698 C  CA  . GLU   R  195 ? 2.2461 1.1394 1.9773 0.2496  0.1456  -0.1944 187 GLU   R CA  
31699 C  C   . GLU   R  195 ? 2.2659 1.0089 1.9152 0.2518  0.1207  -0.1735 187 GLU   R C   
31700 O  O   . GLU   R  195 ? 2.2163 1.0442 1.8546 0.2106  0.1147  -0.1433 187 GLU   R O   
31701 C  CB  . GLU   R  195 ? 2.1944 1.1364 2.0276 0.2865  0.1782  -0.1573 187 GLU   R CB  
31702 C  CG  . GLU   R  195 ? 2.1732 1.1924 2.0656 0.2978  0.1858  -0.1146 187 GLU   R CG  
31703 C  CD  . GLU   R  195 ? 2.1117 1.2148 2.1096 0.3303  0.2197  -0.0546 187 GLU   R CD  
31704 O  OE1 . GLU   R  195 ? 2.0571 1.1622 2.1976 0.2969  0.2212  -0.0172 187 GLU   R OE1 
31705 O  OE2 . GLU   R  195 ? 2.0167 1.3360 2.0975 0.3509  0.2608  -0.0274 187 GLU   R OE2 
31706 N  N   . ALA   R  196 ? 2.3053 0.8905 1.9559 0.2671  0.0831  -0.1571 188 ALA   R N   
31707 C  CA  . ALA   R  196 ? 2.3126 0.8332 1.9570 0.2421  0.0635  -0.1554 188 ALA   R CA  
31708 C  C   . ALA   R  196 ? 2.4193 0.8508 1.9308 0.2271  0.0119  -0.2224 188 ALA   R C   
31709 O  O   . ALA   R  196 ? 2.4334 0.8346 1.9251 0.2505  0.0030  -0.2020 188 ALA   R O   
31710 C  CB  . ALA   R  196 ? 2.3217 0.8757 1.9330 0.2748  0.0535  -0.1609 188 ALA   R CB  
31711 N  N   . GLU   R  197 ? 2.4881 0.8705 1.8578 0.1167  0.0218  -0.2258 189 GLU   R N   
31712 C  CA  . GLU   R  197 ? 2.5184 0.9743 1.8545 0.1220  0.0041  -0.1947 189 GLU   R CA  
31713 C  C   . GLU   R  197 ? 2.4972 0.9105 1.9089 0.2264  0.0467  -0.1509 189 GLU   R C   
31714 O  O   . GLU   R  197 ? 2.4747 0.7220 1.9798 0.3006  0.0009  -0.0397 189 GLU   R O   
31715 C  CB  . GLU   R  197 ? 2.5888 1.0402 1.8668 0.0464  -0.0051 -0.1652 189 GLU   R CB  
31716 C  CG  . GLU   R  197 ? 2.6195 1.0461 1.8636 0.0633  0.0026  -0.1464 189 GLU   R CG  
31717 C  CD  . GLU   R  197 ? 2.6813 1.2627 1.8773 -0.0033 0.0135  -0.0529 189 GLU   R CD  
31718 O  OE1 . GLU   R  197 ? 2.6372 1.2681 1.9351 0.0540  0.0512  -0.0212 189 GLU   R OE1 
31719 O  OE2 . GLU   R  197 ? 2.7503 1.3619 1.7818 -0.0497 -0.0451 -0.0487 189 GLU   R OE2 
31720 N  N   . LEU   R  198 ? 2.5034 0.9017 1.9344 0.2155  0.0701  -0.1910 190 LEU   R N   
31721 C  CA  . LEU   R  198 ? 2.4076 0.9660 1.8628 0.1767  0.1012  -0.2409 190 LEU   R CA  
31722 C  C   . LEU   R  198 ? 2.3988 0.9617 1.8419 0.1725  0.0709  -0.2429 190 LEU   R C   
31723 O  O   . LEU   R  198 ? 2.4362 0.9222 1.8690 0.1129  0.0383  -0.1121 190 LEU   R O   
31724 C  CB  . LEU   R  198 ? 2.3964 0.9748 1.8644 0.1803  0.1058  -0.2800 190 LEU   R CB  
31725 C  CG  . LEU   R  198 ? 2.3204 0.9312 1.8679 0.1745  0.1454  -0.2743 190 LEU   R CG  
31726 C  CD1 . LEU   R  198 ? 2.3492 0.8817 1.7983 0.1367  0.1248  -0.2693 190 LEU   R CD1 
31727 C  CD2 . LEU   R  198 ? 2.3258 0.9277 1.8667 0.1910  0.1824  -0.2753 190 LEU   R CD2 
31728 N  N   . LEU   R  199 ? 2.3386 0.9134 1.8323 0.2160  0.0854  -0.2301 191 LEU   R N   
31729 C  CA  . LEU   R  199 ? 2.2588 0.8727 1.8567 0.2381  0.1135  -0.2432 191 LEU   R CA  
31730 C  C   . LEU   R  199 ? 2.2581 0.7311 1.8017 0.2213  0.1198  -0.2488 191 LEU   R C   
31731 O  O   . LEU   R  199 ? 2.2365 0.7019 1.8215 0.2053  0.1391  -0.3518 191 LEU   R O   
31732 C  CB  . LEU   R  199 ? 2.2808 0.9843 1.8957 0.2794  0.0805  -0.2865 191 LEU   R CB  
31733 C  CG  . LEU   R  199 ? 2.2944 1.0629 1.9335 0.3291  0.0510  -0.2896 191 LEU   R CG  
31734 C  CD1 . LEU   R  199 ? 2.3183 1.1278 1.9719 0.3130  0.0975  -0.2986 191 LEU   R CD1 
31735 C  CD2 . LEU   R  199 ? 2.2840 1.1267 1.9232 0.3641  0.0594  -0.3222 191 LEU   R CD2 
31736 N  N   . VAL   R  200 ? 2.1333 0.7371 1.7229 0.1868  0.1831  -0.1704 192 VAL   R N   
31737 C  CA  . VAL   R  200 ? 2.1345 0.6961 1.6975 0.1946  0.1997  -0.1541 192 VAL   R CA  
31738 C  C   . VAL   R  200 ? 2.1553 0.7043 1.6855 0.1956  0.2259  -0.1784 192 VAL   R C   
31739 O  O   . VAL   R  200 ? 2.1557 0.6599 1.6905 0.2266  0.2593  -0.1911 192 VAL   R O   
31740 C  CB  . VAL   R  200 ? 2.0944 0.6641 1.6896 0.1556  0.2069  -0.1378 192 VAL   R CB  
31741 C  CG1 . VAL   R  200 ? 2.0954 0.6415 1.6740 0.1369  0.1960  -0.1421 192 VAL   R CG1 
31742 C  CG2 . VAL   R  200 ? 2.0414 0.6502 1.6956 0.1571  0.1941  -0.1115 192 VAL   R CG2 
31743 N  N   . LEU   R  201 ? 2.2376 0.8049 1.6958 0.2139  0.2640  -0.1715 193 LEU   R N   
31744 C  CA  . LEU   R  201 ? 2.3165 0.8990 1.7115 0.2191  0.2247  -0.1820 193 LEU   R CA  
31745 C  C   . LEU   R  201 ? 2.3579 0.9082 1.8212 0.2290  0.1673  -0.1496 193 LEU   R C   
31746 O  O   . LEU   R  201 ? 2.4500 1.0767 1.8762 0.1321  0.1074  -0.2099 193 LEU   R O   
31747 C  CB  . LEU   R  201 ? 2.3470 0.8759 1.6991 0.2713  0.2568  -0.1935 193 LEU   R CB  
31748 C  CG  . LEU   R  201 ? 2.3823 0.7901 1.6155 0.2763  0.2920  -0.2230 193 LEU   R CG  
31749 C  CD1 . LEU   R  201 ? 2.3834 0.6941 1.5887 0.2688  0.2673  -0.2325 193 LEU   R CD1 
31750 C  CD2 . LEU   R  201 ? 2.3894 0.7337 1.6045 0.2989  0.3101  -0.2519 193 LEU   R CD2 
31751 N  N   . LYS   R  202 ? 2.3698 1.0466 1.8863 0.2420  0.1086  -0.1066 194 LYS   R N   
31752 C  CA  . LYS   R  202 ? 2.3412 1.0741 1.8899 0.2727  0.1047  -0.1269 194 LYS   R CA  
31753 C  C   . LYS   R  202 ? 2.3252 1.0287 1.8419 0.2770  0.0721  -0.1394 194 LYS   R C   
31754 O  O   . LYS   R  202 ? 2.3196 1.0880 1.9001 0.1965  0.0678  -0.1166 194 LYS   R O   
31755 C  CB  . LYS   R  202 ? 2.3406 1.2351 1.9586 0.2936  0.1041  -0.1373 194 LYS   R CB  
31756 C  CG  . LYS   R  202 ? 2.3255 1.2905 2.0162 0.3265  0.0755  -0.0842 194 LYS   R CG  
31757 C  CD  . LYS   R  202 ? 2.3293 1.3922 2.0443 0.3239  0.0466  -0.0329 194 LYS   R CD  
31758 C  CE  . LYS   R  202 ? 2.3267 1.4042 2.0444 0.3245  -0.0041 0.0021  194 LYS   R CE  
31759 N  NZ  . LYS   R  202 ? 2.3056 1.4160 2.0545 0.3399  -0.0607 0.0322  194 LYS   R NZ  
31760 N  N   . ILE   R  203 ? 2.2536 0.9006 1.8028 0.2625  0.0856  -0.0730 195 ILE   R N   
31761 C  CA  . ILE   R  203 ? 2.2132 0.8518 1.7624 0.2829  0.0660  -0.0949 195 ILE   R CA  
31762 C  C   . ILE   R  203 ? 2.2126 0.7961 1.7082 0.3254  0.0476  -0.1019 195 ILE   R C   
31763 O  O   . ILE   R  203 ? 2.2187 0.8636 1.6884 0.2894  -0.0055 -0.0485 195 ILE   R O   
31764 C  CB  . ILE   R  203 ? 2.1594 0.8362 1.7452 0.2957  0.0828  -0.0840 195 ILE   R CB  
31765 C  CG1 . ILE   R  203 ? 2.1569 0.9400 1.7771 0.2759  0.0894  -0.0976 195 ILE   R CG1 
31766 C  CG2 . ILE   R  203 ? 2.1396 0.7664 1.7392 0.3129  0.0604  -0.0827 195 ILE   R CG2 
31767 C  CD1 . ILE   R  203 ? 2.1418 0.9818 1.7838 0.2914  0.1138  -0.1408 195 ILE   R CD1 
31768 N  N   . LEU   R  204 ? 2.2250 0.7623 1.6750 0.3278  0.0956  -0.1118 196 LEU   R N   
31769 C  CA  . LEU   R  204 ? 2.2288 0.8405 1.6966 0.3321  0.0970  -0.1011 196 LEU   R CA  
31770 C  C   . LEU   R  204 ? 2.2941 0.8014 1.6920 0.4137  0.1034  -0.0962 196 LEU   R C   
31771 O  O   . LEU   R  204 ? 2.2206 0.8841 1.8229 0.4386  0.0813  -0.0522 196 LEU   R O   
31772 C  CB  . LEU   R  204 ? 2.2537 0.8455 1.6566 0.3111  0.0683  -0.0937 196 LEU   R CB  
31773 C  CG  . LEU   R  204 ? 2.2649 0.8766 1.6383 0.3038  0.0556  -0.0988 196 LEU   R CG  
31774 C  CD1 . LEU   R  204 ? 2.2813 0.9229 1.5807 0.3099  0.0235  -0.0670 196 LEU   R CD1 
31775 C  CD2 . LEU   R  204 ? 2.2454 0.8815 1.6348 0.2981  0.0488  -0.1249 196 LEU   R CD2 
31776 N  N   . LYS   R  205 ? 2.3327 0.7737 1.7321 0.4096  0.1511  -0.0393 197 LYS   R N   
31777 C  CA  . LYS   R  205 ? 2.4008 0.8043 1.7550 0.3796  0.1748  -0.0769 197 LYS   R CA  
31778 C  C   . LYS   R  205 ? 2.4160 0.7059 1.7448 0.2720  0.1657  -0.1975 197 LYS   R C   
31779 O  O   . LYS   R  205 ? 2.4337 0.8231 1.7099 0.2300  0.1019  -0.1843 197 LYS   R O   
31780 C  CB  . LYS   R  205 ? 2.4674 0.8321 1.7793 0.4252  0.2143  -0.0191 197 LYS   R CB  
31781 C  CG  . LYS   R  205 ? 2.5262 0.8297 1.7933 0.4438  0.2114  -0.0235 197 LYS   R CG  
31782 C  CD  . LYS   R  205 ? 2.5684 0.8765 1.7843 0.5375  0.2661  -0.0348 197 LYS   R CD  
31783 C  CE  . LYS   R  205 ? 2.6519 0.8470 1.8060 0.5982  0.2759  -0.0429 197 LYS   R CE  
31784 N  NZ  . LYS   R  205 ? 2.6060 0.8307 1.8239 0.6619  0.2786  -0.0419 197 LYS   R NZ  
31785 N  N   . GLN   R  206 ? 2.3858 0.7157 1.7480 0.2350  0.1638  -0.2536 198 GLN   R N   
31786 C  CA  . GLN   R  206 ? 2.3751 0.7157 1.7845 0.1908  0.1798  -0.2309 198 GLN   R CA  
31787 C  C   . GLN   R  206 ? 2.4017 0.8006 1.7485 0.1405  0.1807  -0.2449 198 GLN   R C   
31788 O  O   . GLN   R  206 ? 2.3620 0.8162 1.7920 0.1223  0.2359  -0.2440 198 GLN   R O   
31789 C  CB  . GLN   R  206 ? 2.3998 0.7779 1.8403 0.2077  0.1407  -0.2381 198 GLN   R CB  
31790 C  CG  . GLN   R  206 ? 2.3854 0.8861 1.8952 0.2110  0.1289  -0.2024 198 GLN   R CG  
31791 C  CD  . GLN   R  206 ? 2.4481 0.9059 1.9361 0.2293  0.0661  -0.1660 198 GLN   R CD  
31792 O  OE1 . GLN   R  206 ? 2.4575 0.9075 1.9583 0.1999  0.0336  -0.1699 198 GLN   R OE1 
31793 N  NE2 . GLN   R  206 ? 2.4246 0.9089 1.9512 0.2315  0.0318  -0.1372 198 GLN   R NE2 
31794 N  N   . VAL   R  207 ? 2.4214 0.6295 1.7132 0.0438  0.1379  -0.2445 199 VAL   R N   
31795 C  CA  . VAL   R  207 ? 2.3931 0.6391 1.6911 0.0439  0.1144  -0.2581 199 VAL   R CA  
31796 C  C   . VAL   R  207 ? 2.4251 0.6078 1.6942 0.0747  0.0844  -0.2107 199 VAL   R C   
31797 O  O   . VAL   R  207 ? 2.3286 0.8019 1.6280 0.1445  0.1321  -0.2876 199 VAL   R O   
31798 C  CB  . VAL   R  207 ? 2.3732 0.5604 1.6994 0.0579  0.1783  -0.2653 199 VAL   R CB  
31799 C  CG1 . VAL   R  207 ? 2.3698 0.6104 1.7123 0.0193  0.1741  -0.2784 199 VAL   R CG1 
31800 C  CG2 . VAL   R  207 ? 2.3050 0.5764 1.6244 0.1169  0.2029  -0.2790 199 VAL   R CG2 
31801 N  N   . MET   R  208 ? 2.4823 0.5044 1.8164 0.0876  0.0418  -0.1625 200 MET   R N   
31802 C  CA  . MET   R  208 ? 2.5309 0.6909 1.8689 0.1587  0.0183  -0.1161 200 MET   R CA  
31803 C  C   . MET   R  208 ? 2.5899 0.7503 1.9023 0.0866  -0.0833 -0.0775 200 MET   R C   
31804 O  O   . MET   R  208 ? 2.5993 0.9944 1.9777 0.1596  -0.0256 -0.0673 200 MET   R O   
31805 C  CB  . MET   R  208 ? 2.5992 0.7429 1.8178 0.1202  0.0206  -0.1242 200 MET   R CB  
31806 C  CG  . MET   R  208 ? 2.6039 0.8264 1.7931 0.1138  0.0394  -0.2112 200 MET   R CG  
31807 S  SD  . MET   R  208 ? 2.6724 0.8794 1.7878 0.1315  0.0571  -0.1894 200 MET   R SD  
31808 C  CE  . MET   R  208 ? 2.7137 0.8406 1.8023 0.1279  0.0109  -0.1846 200 MET   R CE  
31809 N  N   . GLU   R  209 ? 2.5552 0.9865 1.9272 0.1936  -0.0945 -0.0053 201 GLU   R N   
31810 C  CA  . GLU   R  209 ? 2.4824 1.2137 1.9198 0.1310  -0.1392 -0.0543 201 GLU   R CA  
31811 C  C   . GLU   R  209 ? 2.5600 1.2019 1.9359 0.1993  -0.1541 0.0103  201 GLU   R C   
31812 O  O   . GLU   R  209 ? 2.5845 1.3488 1.9842 0.2140  -0.1115 -0.0377 201 GLU   R O   
31813 C  CB  . GLU   R  209 ? 2.4761 1.3926 1.9343 0.1751  -0.1112 -0.0604 201 GLU   R CB  
31814 C  CG  . GLU   R  209 ? 2.4051 1.4586 1.9007 0.1593  -0.0702 -0.0808 201 GLU   R CG  
31815 C  CD  . GLU   R  209 ? 2.4534 1.4592 1.9381 0.1102  -0.0344 -0.2397 201 GLU   R CD  
31816 O  OE1 . GLU   R  209 ? 2.4756 1.3069 1.9710 0.1149  0.0333  -0.2831 201 GLU   R OE1 
31817 O  OE2 . GLU   R  209 ? 2.4582 1.5674 1.9504 0.1508  -0.0525 -0.2807 201 GLU   R OE2 
31818 N  N   . GLU   R  210 ? 2.5468 1.1497 1.9079 0.2121  -0.1322 -0.0391 202 GLU   R N   
31819 C  CA  . GLU   R  210 ? 2.4986 1.1285 1.8852 0.2623  -0.1638 -0.0720 202 GLU   R CA  
31820 C  C   . GLU   R  210 ? 2.5196 0.9952 1.7417 0.2487  -0.1985 -0.1102 202 GLU   R C   
31821 O  O   . GLU   R  210 ? 2.5165 0.7346 1.8687 0.2569  -0.1307 -0.2287 202 GLU   R O   
31822 C  CB  . GLU   R  210 ? 2.4896 1.1799 1.9288 0.2685  -0.1556 -0.0132 202 GLU   R CB  
31823 C  CG  . GLU   R  210 ? 2.4673 1.2320 1.9566 0.2070  -0.1165 -0.0148 202 GLU   R CG  
31824 C  CD  . GLU   R  210 ? 2.4376 1.3104 2.0358 0.1755  -0.1279 0.1095  202 GLU   R CD  
31825 O  OE1 . GLU   R  210 ? 2.2951 1.2049 2.0724 0.2314  -0.0538 0.1795  202 GLU   R OE1 
31826 O  OE2 . GLU   R  210 ? 2.4971 1.5315 2.0316 0.0625  -0.1277 0.1202  202 GLU   R OE2 
31827 N  N   . LYS   R  211 ? 2.5075 1.0104 1.7291 0.2442  -0.1991 0.0229  203 LYS   R N   
31828 C  CA  . LYS   R  211 ? 2.5148 1.0368 1.7311 0.2515  -0.1832 0.0549  203 LYS   R CA  
31829 C  C   . LYS   R  211 ? 2.5674 1.0622 1.7023 0.2824  -0.1717 -0.0506 203 LYS   R C   
31830 O  O   . LYS   R  211 ? 2.4857 1.1636 1.6837 0.3097  -0.2179 -0.2210 203 LYS   R O   
31831 C  CB  . LYS   R  211 ? 2.4823 1.0887 1.7054 0.2369  -0.1298 0.1407  203 LYS   R CB  
31832 C  CG  . LYS   R  211 ? 2.4870 1.1762 1.7631 0.2294  -0.1026 0.1559  203 LYS   R CG  
31833 C  CD  . LYS   R  211 ? 2.4499 1.3302 1.7621 0.1872  -0.0595 0.1116  203 LYS   R CD  
31834 C  CE  . LYS   R  211 ? 2.4198 1.4879 1.8131 0.1667  -0.0187 0.0679  203 LYS   R CE  
31835 N  NZ  . LYS   R  211 ? 2.4233 1.5962 1.8059 0.1290  0.0140  0.0309  203 LYS   R NZ  
31836 N  N   . LEU   R  212 ? 2.5697 1.1983 1.6996 0.2762  -0.1806 -0.0556 204 LEU   R N   
31837 C  CA  . LEU   R  212 ? 2.6167 1.2032 1.7116 0.2700  -0.1401 -0.0489 204 LEU   R CA  
31838 C  C   . LEU   R  212 ? 2.6921 1.1872 1.6989 0.2617  -0.0668 -0.0759 204 LEU   R C   
31839 O  O   . LEU   R  212 ? 2.7844 1.1522 1.7421 0.2825  -0.0077 -0.0738 204 LEU   R O   
31840 C  CB  . LEU   R  212 ? 2.5784 1.2624 1.7200 0.2921  -0.1331 0.0115  204 LEU   R CB  
31841 C  CG  . LEU   R  212 ? 2.5297 1.1916 1.7468 0.2887  -0.1042 0.1219  204 LEU   R CG  
31842 C  CD1 . LEU   R  212 ? 2.4863 1.1740 1.7743 0.3073  -0.1238 0.1044  204 LEU   R CD1 
31843 C  CD2 . LEU   R  212 ? 2.5359 1.1775 1.7220 0.2962  -0.1063 0.1392  204 LEU   R CD2 
31844 N  N   . ASP   R  213 ? 2.6782 1.1716 1.7338 0.2474  -0.0729 -0.1476 205 ASP   R N   
31845 C  CA  . ASP   R  213 ? 2.6467 1.1302 1.6821 0.2219  -0.0667 -0.2014 205 ASP   R CA  
31846 C  C   . ASP   R  213 ? 2.6400 1.0647 1.7423 0.2409  -0.0729 -0.1425 205 ASP   R C   
31847 O  O   . ASP   R  213 ? 2.6788 1.0160 1.7388 0.2590  -0.0943 -0.1274 205 ASP   R O   
31848 C  CB  . ASP   R  213 ? 2.6354 1.1932 1.6860 0.1723  -0.0549 -0.2185 205 ASP   R CB  
31849 C  CG  . ASP   R  213 ? 2.6085 1.1863 1.6555 0.1072  -0.1256 -0.2488 205 ASP   R CG  
31850 O  OD1 . ASP   R  213 ? 2.5098 1.1448 1.7023 0.0725  -0.1248 -0.2693 205 ASP   R OD1 
31851 O  OD2 . ASP   R  213 ? 2.6061 1.3404 1.6241 0.0460  -0.1456 -0.2047 205 ASP   R OD2 
31852 N  N   . GLU   R  214 ? 2.6105 1.0015 1.6756 0.2572  -0.0412 -0.2067 206 GLU   R N   
31853 C  CA  . GLU   R  214 ? 2.5449 1.0147 1.6142 0.2815  -0.0408 -0.2174 206 GLU   R CA  
31854 C  C   . GLU   R  214 ? 2.5515 0.9475 1.5498 0.3066  -0.0682 -0.3181 206 GLU   R C   
31855 O  O   . GLU   R  214 ? 2.6166 1.0035 1.5253 0.3638  0.0049  -0.3238 206 GLU   R O   
31856 C  CB  . GLU   R  214 ? 2.5151 0.9102 1.6090 0.3039  -0.0802 -0.2334 206 GLU   R CB  
31857 C  CG  . GLU   R  214 ? 2.5336 0.8900 1.5697 0.3035  -0.0674 -0.2170 206 GLU   R CG  
31858 C  CD  . GLU   R  214 ? 2.5374 1.0115 1.4915 0.2676  -0.0738 -0.2202 206 GLU   R CD  
31859 O  OE1 . GLU   R  214 ? 2.4991 0.9807 1.5285 0.2697  -0.0983 -0.1931 206 GLU   R OE1 
31860 O  OE2 . GLU   R  214 ? 2.4802 1.0956 1.4740 0.2890  -0.1063 -0.2202 206 GLU   R OE2 
31861 N  N   . ASN   R  215 ? 2.5414 0.9695 1.4866 0.3240  -0.1182 -0.3626 207 ASN   R N   
31862 C  CA  . ASN   R  215 ? 2.5061 0.9016 1.4023 0.3006  -0.1984 -0.3921 207 ASN   R CA  
31863 C  C   . ASN   R  215 ? 2.4218 0.8862 1.3950 0.3120  -0.1851 -0.4189 207 ASN   R C   
31864 O  O   . ASN   R  215 ? 2.3224 0.9359 1.3853 0.3305  -0.2460 -0.3264 207 ASN   R O   
31865 C  CB  . ASN   R  215 ? 2.5830 0.8983 1.4057 0.2747  -0.2331 -0.3696 207 ASN   R CB  
31866 C  CG  . ASN   R  215 ? 2.6666 0.9231 1.3917 0.2395  -0.2869 -0.3693 207 ASN   R CG  
31867 O  OD1 . ASN   R  215 ? 2.6948 0.9274 1.3638 0.2259  -0.3090 -0.4024 207 ASN   R OD1 
31868 N  ND2 . ASN   R  215 ? 2.7052 0.9612 1.4330 0.1976  -0.3317 -0.3269 207 ASN   R ND2 
31869 N  N   . ASN   R  216 ? 2.4337 0.8190 1.4333 0.3203  -0.1661 -0.4775 208 ASN   R N   
31870 C  CA  . ASN   R  216 ? 2.4376 0.8849 1.4800 0.3257  -0.1467 -0.4386 208 ASN   R CA  
31871 C  C   . ASN   R  216 ? 2.4332 0.8500 1.4821 0.3628  -0.1474 -0.4267 208 ASN   R C   
31872 O  O   . ASN   R  216 ? 2.4862 0.8248 1.5330 0.3581  -0.0698 -0.4148 208 ASN   R O   
31873 C  CB  . ASN   R  216 ? 2.4574 0.9105 1.5557 0.2684  -0.1890 -0.4503 208 ASN   R CB  
31874 C  CG  . ASN   R  216 ? 2.4638 0.9961 1.6224 0.2609  -0.1368 -0.4259 208 ASN   R CG  
31875 O  OD1 . ASN   R  216 ? 2.4993 1.0834 1.6535 0.1950  -0.1050 -0.4161 208 ASN   R OD1 
31876 N  ND2 . ASN   R  216 ? 2.5563 1.0080 1.6384 0.2358  -0.1283 -0.4351 208 ASN   R ND2 
31877 N  N   . ALA   R  217 ? 2.4431 0.8827 1.5003 0.3766  -0.0952 -0.3414 209 ALA   R N   
31878 C  CA  . ALA   R  217 ? 2.4199 0.8066 1.5159 0.3485  -0.0892 -0.3078 209 ALA   R CA  
31879 C  C   . ALA   R  217 ? 2.4619 0.8074 1.4240 0.3320  -0.1028 -0.2580 209 ALA   R C   
31880 O  O   . ALA   R  217 ? 2.5387 0.6294 1.4021 0.2886  -0.1566 -0.3164 209 ALA   R O   
31881 C  CB  . ALA   R  217 ? 2.3989 0.9549 1.5622 0.3731  -0.0752 -0.2965 209 ALA   R CB  
31882 N  N   . GLN   R  218 ? 2.4077 0.7419 1.4303 0.3007  -0.1080 -0.2272 210 GLN   R N   
31883 C  CA  . GLN   R  218 ? 2.3586 0.7190 1.4277 0.3506  -0.0673 -0.1864 210 GLN   R CA  
31884 C  C   . GLN   R  218 ? 2.3578 0.5204 1.4519 0.3165  -0.0359 -0.2451 210 GLN   R C   
31885 O  O   . GLN   R  218 ? 2.3979 0.5480 1.3829 0.3332  -0.0520 -0.3105 210 GLN   R O   
31886 C  CB  . GLN   R  218 ? 2.2710 0.7499 1.3783 0.3406  -0.1192 -0.1562 210 GLN   R CB  
31887 C  CG  . GLN   R  218 ? 2.1874 0.7650 1.3519 0.3607  -0.1224 -0.1114 210 GLN   R CG  
31888 C  CD  . GLN   R  218 ? 2.1453 0.8319 1.2871 0.3777  -0.1659 -0.0440 210 GLN   R CD  
31889 O  OE1 . GLN   R  218 ? 2.1029 0.7537 1.3359 0.3944  -0.1416 -0.0243 210 GLN   R OE1 
31890 N  NE2 . GLN   R  218 ? 2.0730 0.9203 1.2890 0.4030  -0.1678 -0.0203 210 GLN   R NE2 
31891 N  N   . LEU   R  219 ? 2.4315 0.4909 1.4872 0.3272  0.0526  -0.2523 211 LEU   R N   
31892 C  CA  . LEU   R  219 ? 2.3518 0.7122 1.5309 0.2980  0.0818  -0.1861 211 LEU   R CA  
31893 C  C   . LEU   R  219 ? 2.3888 0.7248 1.5758 0.3115  0.0879  -0.1902 211 LEU   R C   
31894 O  O   . LEU   R  219 ? 2.4512 0.6463 1.6142 0.3222  0.0886  -0.1717 211 LEU   R O   
31895 C  CB  . LEU   R  219 ? 2.4113 0.6737 1.5623 0.3443  0.1373  -0.2083 211 LEU   R CB  
31896 C  CG  . LEU   R  219 ? 2.4028 0.7146 1.5884 0.3772  0.1717  -0.1939 211 LEU   R CG  
31897 C  CD1 . LEU   R  219 ? 2.4317 0.7842 1.6643 0.3711  0.2075  -0.1558 211 LEU   R CD1 
31898 C  CD2 . LEU   R  219 ? 2.3786 0.8228 1.5353 0.3491  0.1890  -0.2331 211 LEU   R CD2 
31899 N  N   . SER   R  220 ? 2.3707 0.8821 1.6099 0.2270  0.0696  -0.1579 212 SER   R N   
31900 C  CA  . SER   R  220 ? 2.3709 0.8361 1.6970 0.2073  0.0746  -0.1077 212 SER   R CA  
31901 C  C   . SER   R  220 ? 2.3820 0.9020 1.7571 0.1764  0.0551  -0.0908 212 SER   R C   
31902 O  O   . SER   R  220 ? 2.3925 0.9270 1.7475 0.1668  0.0282  -0.0440 212 SER   R O   
31903 C  CB  . SER   R  220 ? 2.3224 0.9101 1.7021 0.2035  0.0621  -0.0508 212 SER   R CB  
31904 O  OG  . SER   R  220 ? 2.2854 0.9271 1.7048 0.2317  0.0888  -0.0390 212 SER   R OG  
31905 N  N   . CYS   R  221 ? 2.4473 0.9294 1.7958 0.1566  0.0589  -0.1429 213 CYS   R N   
31906 C  CA  . CYS   R  221 ? 2.4090 0.9112 1.7758 0.1408  0.1045  -0.1479 213 CYS   R CA  
31907 C  C   . CYS   R  221 ? 2.4747 0.9223 1.7318 0.1135  0.0350  -0.1603 213 CYS   R C   
31908 O  O   . CYS   R  221 ? 2.4606 1.0123 1.7933 0.1032  -0.0200 -0.1241 213 CYS   R O   
31909 C  CB  . CYS   R  221 ? 2.4618 0.8152 1.7997 0.1217  0.1717  -0.1536 213 CYS   R CB  
31910 S  SG  . CYS   R  221 ? 2.4569 0.6724 1.8418 0.1209  0.3218  -0.2513 213 CYS   R SG  
31911 N  N   . ILE   R  222 ? 2.4718 1.0085 1.7036 0.1239  0.0399  -0.1317 214 ILE   R N   
31912 C  CA  . ILE   R  222 ? 2.3543 1.0227 1.6370 0.1243  0.0731  -0.1327 214 ILE   R CA  
31913 C  C   . ILE   R  222 ? 2.3247 1.0418 1.6487 0.1546  0.0776  -0.1614 214 ILE   R C   
31914 O  O   . ILE   R  222 ? 2.2520 0.9126 1.6890 0.0853  0.1246  -0.1540 214 ILE   R O   
31915 C  CB  . ILE   R  222 ? 2.3946 1.0385 1.6303 0.1414  0.0830  -0.1317 214 ILE   R CB  
31916 C  CG1 . ILE   R  222 ? 2.3555 1.0550 1.6312 0.1261  0.1020  -0.1301 214 ILE   R CG1 
31917 C  CG2 . ILE   R  222 ? 2.4040 1.0826 1.5873 0.1144  0.1303  -0.1104 214 ILE   R CG2 
31918 C  CD1 . ILE   R  222 ? 2.3566 1.0700 1.6738 0.1444  0.0903  -0.1244 214 ILE   R CD1 
31919 N  N   . THR   R  223 ? 2.2010 1.0414 1.5927 0.2147  0.0734  -0.1505 215 THR   R N   
31920 C  CA  . THR   R  223 ? 2.1358 1.1183 1.5883 0.2691  0.1011  -0.1241 215 THR   R CA  
31921 C  C   . THR   R  223 ? 2.1066 1.0998 1.6503 0.2858  0.0653  -0.1057 215 THR   R C   
31922 O  O   . THR   R  223 ? 2.1033 1.1105 1.5239 0.2667  0.0043  -0.0845 215 THR   R O   
31923 C  CB  . THR   R  223 ? 2.1135 1.1156 1.6011 0.3276  0.1267  -0.1557 215 THR   R CB  
31924 O  OG1 . THR   R  223 ? 2.1613 1.0852 1.5606 0.3806  0.1705  -0.1834 215 THR   R OG1 
31925 C  CG2 . THR   R  223 ? 2.1109 1.1332 1.5788 0.3093  0.1382  -0.1619 215 THR   R CG2 
31926 N  N   . LYS   R  224 ? 2.0672 1.1773 1.7713 0.2567  0.0588  -0.0888 216 LYS   R N   
31927 C  CA  . LYS   R  224 ? 2.0502 1.1639 1.7895 0.2646  0.0549  -0.0780 216 LYS   R CA  
31928 C  C   . LYS   R  224 ? 2.1762 1.2168 1.7972 0.2205  0.0724  -0.0204 216 LYS   R C   
31929 O  O   . LYS   R  224 ? 2.1433 1.2276 1.8738 0.2074  0.1338  0.0464  216 LYS   R O   
31930 C  CB  . LYS   R  224 ? 2.0430 1.2089 1.7758 0.2789  0.0427  -0.0589 216 LYS   R CB  
31931 C  CG  . LYS   R  224 ? 1.9639 1.2302 1.7316 0.2437  -0.0121 -0.0384 216 LYS   R CG  
31932 C  CD  . LYS   R  224 ? 1.9378 1.3320 1.7343 0.2365  -0.0025 -0.0276 216 LYS   R CD  
31933 C  CE  . LYS   R  224 ? 1.9171 1.3750 1.7091 0.2080  -0.0351 -0.0616 216 LYS   R CE  
31934 N  NZ  . LYS   R  224 ? 1.8913 1.4842 1.7211 0.1840  -0.0239 -0.0783 216 LYS   R NZ  
31935 N  N   . GLN   R  225 ? 2.2200 1.2998 1.7774 0.2550  0.0557  -0.0753 217 GLN   R N   
31936 C  CA  . GLN   R  225 ? 2.2909 1.3927 1.7149 0.3019  0.0605  -0.0679 217 GLN   R CA  
31937 C  C   . GLN   R  225 ? 2.3213 1.2431 1.7004 0.2515  0.0275  -0.1150 217 GLN   R C   
31938 O  O   . GLN   R  225 ? 2.5512 1.2458 1.7370 0.3043  0.0602  -0.1177 217 GLN   R O   
31939 C  CB  . GLN   R  225 ? 2.2033 1.6172 1.7557 0.3543  0.0330  -0.0848 217 GLN   R CB  
31940 C  CG  . GLN   R  225 ? 2.1963 1.6550 1.8320 0.3974  -0.0276 -0.0009 217 GLN   R CG  
31941 C  CD  . GLN   R  225 ? 2.2663 1.7960 1.8171 0.4547  -0.0774 -0.0287 217 GLN   R CD  
31942 O  OE1 . GLN   R  225 ? 2.3180 1.8216 1.8507 0.5098  -0.1428 -0.0385 217 GLN   R OE1 
31943 N  NE2 . GLN   R  225 ? 2.2607 1.9121 1.9361 0.4437  -0.1068 -0.0242 217 GLN   R NE2 
31944 N  N   . ASP   R  226 ? 2.3696 1.1697 1.6874 0.2499  0.0907  -0.0994 218 ASP   R N   
31945 C  CA  . ASP   R  226 ? 2.4061 1.0828 1.6248 0.2349  0.0787  -0.1098 218 ASP   R CA  
31946 C  C   . ASP   R  226 ? 2.3364 1.0133 1.6261 0.2571  0.0234  -0.0869 218 ASP   R C   
31947 O  O   . ASP   R  226 ? 2.4059 0.9064 1.5762 0.3062  -0.0392 -0.0155 218 ASP   R O   
31948 C  CB  . ASP   R  226 ? 2.4734 1.1227 1.6308 0.2379  0.1039  -0.1248 218 ASP   R CB  
31949 C  CG  . ASP   R  226 ? 2.5252 1.1101 1.6849 0.1892  0.1265  -0.1307 218 ASP   R CG  
31950 O  OD1 . ASP   R  226 ? 2.5520 1.0777 1.6583 0.1461  0.1158  -0.2350 218 ASP   R OD1 
31951 O  OD2 . ASP   R  226 ? 2.5571 1.2035 1.8516 0.2552  0.1309  -0.1549 218 ASP   R OD2 
31952 N  N   . GLY   R  227 ? 2.3072 0.9776 1.6151 0.2423  0.0545  -0.0978 219 GLY   R N   
31953 C  CA  . GLY   R  227 ? 2.2524 0.9173 1.6067 0.2336  0.0153  -0.1007 219 GLY   R CA  
31954 C  C   . GLY   R  227 ? 2.1789 0.9207 1.5422 0.2096  0.0161  -0.0505 219 GLY   R C   
31955 O  O   . GLY   R  227 ? 2.2316 0.8956 1.5651 0.2335  0.0057  -0.0508 219 GLY   R O   
31956 N  N   . PHE   R  228 ? 2.1596 0.8632 1.4787 0.2314  0.0141  -0.0660 220 PHE   R N   
31957 C  CA  . PHE   R  228 ? 2.1631 0.8651 1.5198 0.2235  0.0362  -0.0843 220 PHE   R CA  
31958 C  C   . PHE   R  228 ? 2.1971 0.8351 1.5350 0.2039  0.0189  -0.0329 220 PHE   R C   
31959 O  O   . PHE   R  228 ? 2.1330 0.9882 1.5471 0.2600  0.0169  -0.0020 220 PHE   R O   
31960 C  CB  . PHE   R  228 ? 2.1448 0.8703 1.5352 0.1932  0.0465  -0.1700 220 PHE   R CB  
31961 C  CG  . PHE   R  228 ? 2.1803 0.9385 1.5965 0.1501  0.0537  -0.2323 220 PHE   R CG  
31962 C  CD1 . PHE   R  228 ? 2.1794 0.9646 1.6625 0.1545  0.0612  -0.1799 220 PHE   R CD1 
31963 C  CD2 . PHE   R  228 ? 2.1869 0.8931 1.5976 0.1843  0.0526  -0.2457 220 PHE   R CD2 
31964 C  CE1 . PHE   R  228 ? 2.1798 0.9862 1.7139 0.1321  0.0608  -0.1509 220 PHE   R CE1 
31965 C  CE2 . PHE   R  228 ? 2.1585 1.0121 1.6594 0.1074  0.0261  -0.2046 220 PHE   R CE2 
31966 C  CZ  . PHE   R  228 ? 2.1877 1.0400 1.7187 0.1228  0.0420  -0.1552 220 PHE   R CZ  
31967 N  N   . LYS   R  229 ? 2.2079 0.7799 1.5771 0.2182  -0.0046 -0.0177 221 LYS   R N   
31968 C  CA  . LYS   R  229 ? 2.2521 0.8282 1.5856 0.2207  -0.0259 -0.0162 221 LYS   R CA  
31969 C  C   . LYS   R  229 ? 2.2322 0.8231 1.5791 0.2628  -0.0642 -0.0386 221 LYS   R C   
31970 O  O   . LYS   R  229 ? 2.2578 0.7301 1.5712 0.2439  -0.0843 -0.1228 221 LYS   R O   
31971 C  CB  . LYS   R  229 ? 2.2873 0.9238 1.6152 0.2126  0.0135  -0.0220 221 LYS   R CB  
31972 C  CG  . LYS   R  229 ? 2.3330 0.9486 1.6453 0.1736  0.0467  -0.0159 221 LYS   R CG  
31973 C  CD  . LYS   R  229 ? 2.3492 1.0436 1.6139 0.1693  0.0352  -0.0164 221 LYS   R CD  
31974 C  CE  . LYS   R  229 ? 2.3768 1.0305 1.6028 0.1714  0.0670  -0.0367 221 LYS   R CE  
31975 N  NZ  . LYS   R  229 ? 2.3693 0.9994 1.6520 0.1647  0.0521  -0.0492 221 LYS   R NZ  
31976 N  N   . ILE   R  230 ? 2.2453 0.8695 1.5884 0.2454  -0.0714 -0.0227 222 ILE   R N   
31977 C  CA  . ILE   R  230 ? 2.3177 0.7737 1.6219 0.2744  0.0189  0.0029  222 ILE   R CA  
31978 C  C   . ILE   R  230 ? 2.3736 0.8522 1.6655 0.2646  0.1004  -0.0035 222 ILE   R C   
31979 O  O   . ILE   R  230 ? 2.4464 0.8890 1.6522 0.3610  0.2010  0.0035  222 ILE   R O   
31980 C  CB  . ILE   R  230 ? 2.3205 0.7616 1.5868 0.2564  -0.0007 0.0032  222 ILE   R CB  
31981 C  CG1 . ILE   R  230 ? 2.2656 0.7583 1.5798 0.2344  -0.0098 -0.0197 222 ILE   R CG1 
31982 C  CG2 . ILE   R  230 ? 2.3305 0.8435 1.5620 0.2624  -0.0278 -0.0553 222 ILE   R CG2 
31983 C  CD1 . ILE   R  230 ? 2.2565 0.7782 1.5281 0.2067  -0.0283 -0.0341 222 ILE   R CD1 
31984 N  N   . TYR   R  231 ? 2.3480 0.8146 1.6814 0.2272  0.1325  0.0276  223 TYR   R N   
31985 C  CA  . TYR   R  231 ? 2.3843 0.7911 1.6854 0.1821  0.1492  0.0306  223 TYR   R CA  
31986 C  C   . TYR   R  231 ? 2.4203 0.8058 1.6350 0.1352  0.1610  0.0229  223 TYR   R C   
31987 O  O   . TYR   R  231 ? 2.4373 0.7437 1.6015 0.1451  0.1883  -0.0106 223 TYR   R O   
31988 C  CB  . TYR   R  231 ? 2.3979 0.7350 1.7377 0.1590  0.1562  0.0081  223 TYR   R CB  
31989 C  CG  . TYR   R  231 ? 2.3904 0.7151 1.8331 0.1453  0.1356  0.0225  223 TYR   R CG  
31990 C  CD1 . TYR   R  231 ? 2.3798 0.7218 1.8928 0.1024  0.1268  0.0328  223 TYR   R CD1 
31991 C  CD2 . TYR   R  231 ? 2.4425 0.6440 1.8851 0.1309  0.1325  -0.0141 223 TYR   R CD2 
31992 C  CE1 . TYR   R  231 ? 2.3617 0.7216 1.9802 0.0952  0.1181  0.0698  223 TYR   R CE1 
31993 C  CE2 . TYR   R  231 ? 2.4230 0.6574 1.9691 0.1122  0.1269  0.0074  223 TYR   R CE2 
31994 C  CZ  . TYR   R  231 ? 2.4232 0.6287 2.0148 0.0755  0.1225  0.0444  223 TYR   R CZ  
31995 O  OH  . TYR   R  231 ? 2.3825 0.5438 2.0894 0.1070  0.1200  0.1102  223 TYR   R OH  
31996 N  N   . ASP   R  232 ? 2.4761 0.9340 1.6055 0.1087  0.1142  0.0260  224 ASP   R N   
31997 C  CA  . ASP   R  232 ? 2.5096 1.0633 1.6495 0.1046  0.0580  0.0566  224 ASP   R CA  
31998 C  C   . ASP   R  232 ? 2.4966 1.0482 1.6096 0.0991  0.0232  0.0998  224 ASP   R C   
31999 O  O   . ASP   R  232 ? 2.4840 1.0896 1.6723 0.1065  0.0664  0.1785  224 ASP   R O   
32000 C  CB  . ASP   R  232 ? 2.5343 1.1770 1.6457 0.0931  0.0522  0.0926  224 ASP   R CB  
32001 C  CG  . ASP   R  232 ? 2.5340 1.1990 1.6996 0.0559  0.0524  0.1076  224 ASP   R CG  
32002 O  OD1 . ASP   R  232 ? 2.5035 1.3386 1.6326 0.0472  0.0118  0.1743  224 ASP   R OD1 
32003 O  OD2 . ASP   R  232 ? 2.4754 1.3526 1.7735 0.0114  0.0666  0.1557  224 ASP   R OD2 
32004 N  N   . ASN   R  233 ? 2.5363 1.0366 1.5368 0.1245  -0.0076 0.1068  225 ASN   R N   
32005 C  CA  . ASN   R  233 ? 2.5184 1.1029 1.4791 0.1480  -0.0471 0.0240  225 ASN   R CA  
32006 C  C   . ASN   R  233 ? 2.5999 1.1432 1.5256 0.0801  0.0118  0.0056  225 ASN   R C   
32007 O  O   . ASN   R  233 ? 2.6519 1.2769 1.6804 0.1942  0.0288  0.0266  225 ASN   R O   
32008 C  CB  . ASN   R  233 ? 2.5079 1.1684 1.4031 0.2052  -0.0899 0.0435  225 ASN   R CB  
32009 C  CG  . ASN   R  233 ? 2.4377 1.2150 1.3639 0.1836  -0.1516 0.0641  225 ASN   R CG  
32010 O  OD1 . ASN   R  233 ? 2.4779 1.3093 1.4299 0.1389  -0.2266 0.1140  225 ASN   R OD1 
32011 N  ND2 . ASN   R  233 ? 2.3960 1.2398 1.3689 0.1672  -0.1552 0.0635  225 ASN   R ND2 
32012 N  N   . GLU   R  234 ? 2.6205 0.9913 1.6014 0.0972  -0.0068 -0.0831 226 GLU   R N   
32013 C  CA  . GLU   R  234 ? 2.6481 1.0852 1.6801 0.0595  0.0464  -0.1355 226 GLU   R CA  
32014 C  C   . GLU   R  234 ? 2.6302 1.0555 1.6206 0.0551  0.0840  -0.0989 226 GLU   R C   
32015 O  O   . GLU   R  234 ? 2.5956 1.0532 1.5471 -0.0018 0.1380  -0.0527 226 GLU   R O   
32016 C  CB  . GLU   R  234 ? 2.6633 1.1111 1.7356 0.0387  0.0362  -0.1077 226 GLU   R CB  
32017 C  CG  . GLU   R  234 ? 2.7187 1.1933 1.7615 0.0146  -0.0051 -0.1264 226 GLU   R CG  
32018 C  CD  . GLU   R  234 ? 2.6718 1.2921 1.8504 -0.0062 -0.0528 -0.1128 226 GLU   R CD  
32019 O  OE1 . GLU   R  234 ? 2.7115 1.3767 1.9410 -0.0405 -0.0920 -0.1566 226 GLU   R OE1 
32020 O  OE2 . GLU   R  234 ? 2.6802 1.2906 1.8826 -0.0130 -0.0871 -0.1320 226 GLU   R OE2 
32021 N  N   . LYS   R  235 ? 2.6488 1.0779 1.5993 0.1012  0.1052  -0.1033 227 LYS   R N   
32022 C  CA  . LYS   R  235 ? 2.6320 1.1152 1.6125 0.0717  0.1245  -0.1619 227 LYS   R CA  
32023 C  C   . LYS   R  235 ? 2.6877 1.1410 1.6175 0.1133  0.1302  -0.1559 227 LYS   R C   
32024 O  O   . LYS   R  235 ? 2.6825 1.0529 1.5846 0.0793  0.1899  -0.1399 227 LYS   R O   
32025 C  CB  . LYS   R  235 ? 2.5971 1.0933 1.6695 0.0272  0.1174  -0.1844 227 LYS   R CB  
32026 C  CG  . LYS   R  235 ? 2.5697 1.1828 1.7476 0.0050  0.1428  -0.2023 227 LYS   R CG  
32027 C  CD  . LYS   R  235 ? 2.5298 1.2896 1.7357 -0.0333 0.1109  -0.2312 227 LYS   R CD  
32028 C  CE  . LYS   R  235 ? 2.5142 1.3326 1.7542 -0.0489 0.1258  -0.2344 227 LYS   R CE  
32029 N  NZ  . LYS   R  235 ? 2.4732 1.3168 1.7351 -0.0611 0.1257  -0.2154 227 LYS   R NZ  
32030 N  N   . THR   R  236 ? 2.6536 1.1644 1.6093 0.1141  0.1254  -0.2012 228 THR   R N   
32031 C  CA  . THR   R  236 ? 2.5986 1.1681 1.6918 0.1379  0.1319  -0.1867 228 THR   R CA  
32032 C  C   . THR   R  236 ? 2.6137 1.2275 1.6614 0.1924  0.0971  -0.1841 228 THR   R C   
32033 O  O   . THR   R  236 ? 2.6010 1.2565 1.8419 0.1929  0.0983  -0.1314 228 THR   R O   
32034 C  CB  . THR   R  236 ? 2.5570 1.1392 1.6966 0.1418  0.1316  -0.2474 228 THR   R CB  
32035 O  OG1 . THR   R  236 ? 2.4447 1.0985 1.7499 0.1096  0.1921  -0.2486 228 THR   R OG1 
32036 C  CG2 . THR   R  236 ? 2.5328 1.1338 1.6876 0.1598  0.1498  -0.2603 228 THR   R CG2 
32037 N  N   . ALA   R  237 ? 2.6233 1.2632 1.6670 0.2483  0.1000  -0.1233 229 ALA   R N   
32038 C  CA  . ALA   R  237 ? 2.6386 1.2630 1.5872 0.2591  0.0765  -0.0869 229 ALA   R CA  
32039 C  C   . ALA   R  237 ? 2.6233 1.3680 1.6368 0.2599  0.0581  -0.0615 229 ALA   R C   
32040 O  O   . ALA   R  237 ? 2.5852 1.3394 1.5811 0.2810  -0.0135 0.0037  229 ALA   R O   
32041 C  CB  . ALA   R  237 ? 2.6724 1.2227 1.5241 0.2944  0.0979  -0.1260 229 ALA   R CB  
32042 N  N   . GLU   R  238 ? 2.5318 1.4663 1.7637 0.2222  0.0805  -0.0293 230 GLU   R N   
32043 C  CA  . GLU   R  238 ? 2.5463 1.5277 1.9024 0.2281  0.1448  -0.0268 230 GLU   R CA  
32044 C  C   . GLU   R  238 ? 2.4460 1.4532 1.8564 0.2707  0.2116  -0.1045 230 GLU   R C   
32045 O  O   . GLU   R  238 ? 2.4836 1.3939 1.9416 0.2094  0.3120  -0.1796 230 GLU   R O   
32046 C  CB  . GLU   R  238 ? 2.4406 1.5803 1.9672 0.2094  0.1172  0.0896  230 GLU   R CB  
32047 C  CG  . GLU   R  238 ? 2.4592 1.7624 2.0236 0.2197  0.0649  0.1309  230 GLU   R CG  
32048 C  CD  . GLU   R  238 ? 2.4568 1.8413 2.1033 0.1666  0.0525  0.1897  230 GLU   R CD  
32049 O  OE1 . GLU   R  238 ? 2.4607 1.9748 2.2764 0.2144  0.0039  0.2213  230 GLU   R OE1 
32050 O  OE2 . GLU   R  238 ? 2.3885 2.0269 2.0839 0.3194  0.0044  0.2059  230 GLU   R OE2 
32051 N  N   . LEU   R  239 ? 2.5571 1.4541 1.8786 0.2178  0.2555  -0.1436 231 LEU   R N   
32052 C  CA  . LEU   R  239 ? 2.5792 1.3034 1.8606 0.2285  0.2920  -0.1619 231 LEU   R CA  
32053 C  C   . LEU   R  239 ? 2.5602 1.2925 1.7848 0.2608  0.2895  -0.1833 231 LEU   R C   
32054 O  O   . LEU   R  239 ? 2.5895 1.3602 1.7491 0.3308  0.3418  -0.2055 231 LEU   R O   
32055 C  CB  . LEU   R  239 ? 2.5973 1.1627 1.8990 0.1483  0.2853  -0.2122 231 LEU   R CB  
32056 C  CG  . LEU   R  239 ? 2.6035 1.1609 1.8501 0.1409  0.3442  -0.2649 231 LEU   R CG  
32057 C  CD1 . LEU   R  239 ? 2.5591 1.1302 1.8604 0.1268  0.3372  -0.2618 231 LEU   R CD1 
32058 C  CD2 . LEU   R  239 ? 2.5927 1.0122 1.8298 0.1092  0.3767  -0.2718 231 LEU   R CD2 
32059 N  N   . ILE   R  240 ? 2.5585 1.2090 1.6977 0.2830  0.2659  -0.1284 232 ILE   R N   
32060 C  CA  . ILE   R  240 ? 2.5251 1.1728 1.6662 0.3159  0.2597  -0.0579 232 ILE   R CA  
32061 C  C   . ILE   R  240 ? 2.5579 1.2171 1.7257 0.3032  0.3019  -0.0989 232 ILE   R C   
32062 O  O   . ILE   R  240 ? 2.4708 1.2883 1.7002 0.3448  0.3230  -0.0805 232 ILE   R O   
32063 C  CB  . ILE   R  240 ? 2.5538 1.0649 1.6232 0.3005  0.1802  -0.0026 232 ILE   R CB  
32064 C  CG1 . ILE   R  240 ? 2.4936 1.0458 1.5871 0.2961  0.1490  0.0569  232 ILE   R CG1 
32065 C  CG2 . ILE   R  240 ? 2.5571 1.0935 1.5969 0.3098  0.1627  -0.0408 232 ILE   R CG2 
32066 C  CD1 . ILE   R  240 ? 2.4990 1.0215 1.5566 0.2862  0.1223  0.0845  232 ILE   R CD1 
32067 N  N   . LYS   R  241 ? 2.5844 1.2540 1.6938 0.3328  0.3386  -0.1168 233 LYS   R N   
32068 C  CA  . LYS   R  241 ? 2.6295 1.3078 1.7191 0.3524  0.3465  -0.1662 233 LYS   R CA  
32069 C  C   . LYS   R  241 ? 2.6268 1.2616 1.8102 0.3938  0.3496  -0.1834 233 LYS   R C   
32070 O  O   . LYS   R  241 ? 2.6280 1.3975 1.8913 0.5174  0.3630  -0.1339 233 LYS   R O   
32071 C  CB  . LYS   R  241 ? 2.6248 1.4352 1.6569 0.3043  0.3467  -0.1438 233 LYS   R CB  
32072 C  CG  . LYS   R  241 ? 2.6243 1.5330 1.6532 0.2672  0.4057  -0.0891 233 LYS   R CG  
32073 C  CD  . LYS   R  241 ? 2.6450 1.5754 1.5960 0.2263  0.4477  -0.0402 233 LYS   R CD  
32074 C  CE  . LYS   R  241 ? 2.6490 1.5983 1.5450 0.1965  0.4606  -0.0051 233 LYS   R CE  
32075 N  NZ  . LYS   R  241 ? 2.6768 1.6269 1.5417 0.1749  0.4775  -0.0108 233 LYS   R NZ  
32076 N  N   . GLU   R  242 ? 2.5954 1.2289 1.9227 0.3716  0.3365  -0.1814 234 GLU   R N   
32077 C  CA  . GLU   R  242 ? 2.5764 1.2409 2.0141 0.3507  0.3492  -0.1814 234 GLU   R CA  
32078 C  C   . GLU   R  242 ? 2.5530 1.1947 2.0253 0.3758  0.3819  -0.2061 234 GLU   R C   
32079 O  O   . GLU   R  242 ? 2.5086 1.2222 2.0370 0.3158  0.3867  -0.2481 234 GLU   R O   
32080 C  CB  . GLU   R  242 ? 2.5416 1.2988 2.0748 0.2457  0.2629  -0.1950 234 GLU   R CB  
32081 C  CG  . GLU   R  242 ? 2.5511 1.3743 2.1567 0.2243  0.2334  -0.1993 234 GLU   R CG  
32082 C  CD  . GLU   R  242 ? 2.5024 1.4162 2.2056 0.1316  0.1610  -0.2055 234 GLU   R CD  
32083 O  OE1 . GLU   R  242 ? 2.4601 1.4355 2.2195 0.1120  0.0829  -0.2285 234 GLU   R OE1 
32084 O  OE2 . GLU   R  242 ? 2.4889 1.4436 2.3054 0.0755  0.1220  -0.1871 234 GLU   R OE2 
32085 N  N   . LEU   R  243 ? 2.5631 1.2707 2.0231 0.4214  0.4031  -0.1599 235 LEU   R N   
32086 C  CA  . LEU   R  243 ? 2.5558 1.4077 1.9977 0.4096  0.4205  -0.0917 235 LEU   R CA  
32087 C  C   . LEU   R  243 ? 2.6676 1.4403 1.8901 0.3248  0.3860  -0.1086 235 LEU   R C   
32088 O  O   . LEU   R  243 ? 2.6683 1.4129 1.8547 0.3419  0.4408  -0.1417 235 LEU   R O   
32089 C  CB  . LEU   R  243 ? 2.5071 1.4108 2.0436 0.4774  0.4141  -0.1067 235 LEU   R CB  
32090 C  CG  . LEU   R  243 ? 2.4173 1.4434 2.0524 0.4880  0.4662  -0.0880 235 LEU   R CG  
32091 C  CD1 . LEU   R  243 ? 2.3621 1.4562 2.0695 0.4676  0.4873  -0.0452 235 LEU   R CD1 
32092 C  CD2 . LEU   R  243 ? 2.4163 1.4877 2.0859 0.4755  0.4553  -0.0831 235 LEU   R CD2 
32093 N  N   . LYS   R  244 ? 2.7648 1.3799 1.8567 0.2531  0.3567  -0.0622 236 LYS   R N   
32094 C  CA  . LYS   R  244 ? 2.7138 1.3940 1.8569 0.1971  0.2853  -0.0726 236 LYS   R CA  
32095 C  C   . LYS   R  244 ? 2.7592 1.3427 1.8640 0.2137  0.3261  -0.1027 236 LYS   R C   
32096 O  O   . LYS   R  244 ? 2.6617 1.4104 1.8460 0.2458  0.3405  -0.2284 236 LYS   R O   
32097 C  CB  . LYS   R  244 ? 2.7704 1.4550 1.8700 0.1675  0.2346  -0.0262 236 LYS   R CB  
32098 C  CG  . LYS   R  244 ? 2.6999 1.5145 1.8729 0.1320  0.1790  -0.0367 236 LYS   R CG  
32099 C  CD  . LYS   R  244 ? 2.6868 1.5782 1.8568 0.1473  0.1688  -0.0030 236 LYS   R CD  
32100 C  CE  . LYS   R  244 ? 2.6941 1.5933 1.8340 0.1254  0.1303  0.0139  236 LYS   R CE  
32101 N  NZ  . LYS   R  244 ? 2.6980 1.5757 1.8749 0.1211  0.1369  0.0034  236 LYS   R NZ  
32102 N  N   . GLU   R  245 ? 2.7937 1.3602 1.8421 0.2307  0.3531  -0.0799 237 GLU   R N   
32103 C  CA  . GLU   R  245 ? 2.8551 1.4304 1.8396 0.2104  0.3968  -0.0372 237 GLU   R CA  
32104 C  C   . GLU   R  245 ? 2.8887 1.4755 1.9153 0.2406  0.3600  -0.0343 237 GLU   R C   
32105 O  O   . GLU   R  245 ? 2.9467 1.4276 1.9763 0.2864  0.3943  0.0521  237 GLU   R O   
32106 C  CB  . GLU   R  245 ? 2.8510 1.5156 1.7618 0.1573  0.4180  0.0186  237 GLU   R CB  
32107 C  CG  . GLU   R  245 ? 2.9122 1.4867 1.6979 0.0680  0.4292  0.0795  237 GLU   R CG  
32108 C  CD  . GLU   R  245 ? 2.9343 1.5214 1.6491 -0.0531 0.4256  0.1442  237 GLU   R CD  
32109 O  OE1 . GLU   R  245 ? 2.9495 1.4934 1.6863 -0.1035 0.4223  0.2527  237 GLU   R OE1 
32110 O  OE2 . GLU   R  245 ? 3.0010 1.4781 1.5069 -0.1454 0.4288  0.2011  237 GLU   R OE2 
32111 N  N   . LYS   R  246 ? 2.8705 1.5263 1.9506 0.2480  0.3060  -0.0928 238 LYS   R N   
32112 C  CA  . LYS   R  246 ? 2.8695 1.6092 1.9865 0.2030  0.2753  -0.1288 238 LYS   R CA  
32113 C  C   . LYS   R  246 ? 2.8264 1.6365 1.9425 0.1995  0.2288  -0.1087 238 LYS   R C   
32114 O  O   . LYS   R  246 ? 2.8068 1.9143 1.9387 0.1898  0.1556  -0.0835 238 LYS   R O   
32115 C  CB  . LYS   R  246 ? 2.8443 1.6658 1.9845 0.1579  0.2308  -0.1551 238 LYS   R CB  
32116 C  CG  . LYS   R  246 ? 2.8799 1.6923 2.0215 0.1087  0.2360  -0.1831 238 LYS   R CG  
32117 C  CD  . LYS   R  246 ? 2.8822 1.6776 2.0196 0.1059  0.2230  -0.1848 238 LYS   R CD  
32118 C  CE  . LYS   R  246 ? 2.9104 1.6884 1.9898 0.0852  0.2243  -0.1855 238 LYS   R CE  
32119 N  NZ  . LYS   R  246 ? 2.8962 1.6339 1.9660 0.0714  0.1764  -0.1489 238 LYS   R NZ  
32120 N  N   . GLU   R  247 ? 2.8377 1.6948 1.9447 0.1593  0.2247  -0.1310 239 GLU   R N   
32121 C  CA  . GLU   R  247 ? 2.7995 1.6566 1.9956 0.0297  0.2609  -0.1873 239 GLU   R CA  
32122 C  C   . GLU   R  247 ? 2.9103 1.6846 2.0086 -0.0345 0.2154  -0.2883 239 GLU   R C   
32123 O  O   . GLU   R  247 ? 3.0197 1.4128 1.8219 -0.1215 0.2135  -0.4347 239 GLU   R O   
32124 C  CB  . GLU   R  247 ? 2.8198 1.5774 2.1069 -0.0201 0.2548  -0.1075 239 GLU   R CB  
32125 C  CG  . GLU   R  247 ? 2.7939 1.4484 2.1518 -0.0654 0.2864  -0.0908 239 GLU   R CG  
32126 C  CD  . GLU   R  247 ? 2.8704 1.3425 2.2423 -0.1133 0.2803  -0.0688 239 GLU   R CD  
32127 O  OE1 . GLU   R  247 ? 2.8305 1.0948 2.2704 -0.1532 0.3004  -0.0481 239 GLU   R OE1 
32128 O  OE2 . GLU   R  247 ? 2.8982 1.2901 2.2635 -0.1740 0.2640  -0.0142 239 GLU   R OE2 
32129 N  N   . ALA   R  248 ? 2.8963 1.8067 1.9497 -0.0391 0.2184  -0.4201 240 ALA   R N   
32130 C  CA  . ALA   R  248 ? 2.8607 1.9946 2.0223 0.0127  0.2933  -0.4707 240 ALA   R CA  
32131 C  C   . ALA   R  248 ? 2.8561 2.1231 2.1272 0.0864  0.3516  -0.4900 240 ALA   R C   
32132 O  O   . ALA   R  248 ? 2.9106 2.1569 2.1658 0.1188  0.3677  -0.4922 240 ALA   R O   
32133 C  CB  . ALA   R  248 ? 2.8582 2.0867 1.9855 -0.0164 0.2962  -0.4873 240 ALA   R CB  
32134 N  N   . ALA   R  249 ? 2.8016 2.0795 2.2188 0.1582  0.3887  -0.5350 241 ALA   R N   
32135 C  CA  . ALA   R  249 ? 2.7701 2.1129 2.3447 0.2260  0.4045  -0.4428 241 ALA   R CA  
32136 C  C   . ALA   R  249 ? 2.7429 2.1017 2.4967 0.2577  0.4253  -0.3544 241 ALA   R C   
32137 O  O   . ALA   R  249 ? 2.6839 2.1468 2.6807 0.3039  0.4436  -0.3176 241 ALA   R O   
32138 C  CB  . ALA   R  249 ? 2.7730 2.1105 2.3252 0.2073  0.4480  -0.4173 241 ALA   R CB  
32139 N  N   . GLU   R  250 ? 2.6257 2.1144 2.4733 0.3379  0.3333  -0.2683 242 GLU   R N   
32140 C  CA  . GLU   R  250 ? 2.6069 2.0004 2.4616 0.2483  0.3721  -0.1700 242 GLU   R CA  
32141 C  C   . GLU   R  250 ? 2.4905 1.9633 2.2955 0.2984  0.3541  -0.1738 242 GLU   R C   
32142 O  O   . GLU   R  250 ? 2.4882 1.8832 2.3474 0.2623  0.3185  -0.1335 242 GLU   R O   
32143 C  CB  . GLU   R  250 ? 2.5564 2.0168 2.4633 0.3353  0.3367  -0.1672 242 GLU   R CB  
32144 C  CG  . GLU   R  250 ? 2.5668 1.9706 2.5714 0.3700  0.3457  -0.1544 242 GLU   R CG  
32145 C  CD  . GLU   R  250 ? 2.4920 1.9096 2.6350 0.4096  0.3785  -0.2475 242 GLU   R CD  
32146 O  OE1 . GLU   R  250 ? 2.4406 1.7189 2.6789 0.4564  0.3652  -0.1947 242 GLU   R OE1 
32147 O  OE2 . GLU   R  250 ? 2.4038 1.8486 2.6568 0.5007  0.4450  -0.2661 242 GLU   R OE2 
32148 N  N   . ASN   S  4   ? 1.8595 0.7587 1.7881 0.0766  -0.0775 0.0190  3   ASN   S N   
32149 C  CA  . ASN   S  4   ? 1.9331 0.8716 1.8091 0.0688  -0.0922 -0.0592 3   ASN   S CA  
32150 C  C   . ASN   S  4   ? 2.0029 0.7423 1.7128 0.0550  -0.1547 -0.0216 3   ASN   S C   
32151 O  O   . ASN   S  4   ? 2.0151 0.6370 1.6671 -0.0195 -0.1147 -0.0759 3   ASN   S O   
32152 C  CB  . ASN   S  4   ? 1.9973 0.9222 1.8918 0.0812  -0.0438 -0.0040 3   ASN   S CB  
32153 C  CG  . ASN   S  4   ? 2.0205 1.0688 1.9777 0.0301  -0.0550 -0.0190 3   ASN   S CG  
32154 O  OD1 . ASN   S  4   ? 2.0336 1.3001 1.9915 0.0902  0.0526  0.0439  3   ASN   S OD1 
32155 N  ND2 . ASN   S  4   ? 2.0923 1.1757 1.9927 0.0516  0.0040  0.0584  3   ASN   S ND2 
32156 N  N   . ASN   S  5   ? 1.9837 0.7894 1.6884 0.0727  -0.1804 -0.0242 4   ASN   S N   
32157 C  CA  . ASN   S  5   ? 1.9986 0.7912 1.6506 0.0765  -0.2504 0.0024  4   ASN   S CA  
32158 C  C   . ASN   S  5   ? 1.9542 0.7995 1.6283 0.0980  -0.2759 -0.0050 4   ASN   S C   
32159 O  O   . ASN   S  5   ? 1.8978 0.9018 1.6004 0.1017  -0.3187 -0.1262 4   ASN   S O   
32160 C  CB  . ASN   S  5   ? 1.9847 0.8244 1.6528 0.0611  -0.2679 0.0025  4   ASN   S CB  
32161 C  CG  . ASN   S  5   ? 2.0053 0.9075 1.6312 0.0626  -0.2972 -0.0150 4   ASN   S CG  
32162 O  OD1 . ASN   S  5   ? 2.0655 0.9191 1.7708 0.0179  -0.3078 -0.0066 4   ASN   S OD1 
32163 N  ND2 . ASN   S  5   ? 1.9846 0.8083 1.6462 0.0737  -0.2727 -0.0023 4   ASN   S ND2 
32164 N  N   . TYR   S  6   ? 1.9657 0.8322 1.6123 0.0788  -0.2739 0.0051  5   TYR   S N   
32165 C  CA  . TYR   S  6   ? 1.9393 0.8555 1.5894 0.0302  -0.2729 0.0208  5   TYR   S CA  
32166 C  C   . TYR   S  6   ? 1.9661 0.8991 1.6418 0.0284  -0.2447 0.0770  5   TYR   S C   
32167 O  O   . TYR   S  6   ? 1.9847 0.7782 1.6747 -0.0228 -0.1870 0.1562  5   TYR   S O   
32168 C  CB  . TYR   S  6   ? 1.9394 0.8929 1.6243 0.0439  -0.2682 0.0878  5   TYR   S CB  
32169 C  CG  . TYR   S  6   ? 1.9616 0.7745 1.5849 0.0868  -0.2907 0.0763  5   TYR   S CG  
32170 C  CD1 . TYR   S  6   ? 1.9239 0.7729 1.5501 0.0874  -0.3115 0.0625  5   TYR   S CD1 
32171 C  CD2 . TYR   S  6   ? 1.9173 0.8103 1.5611 0.0344  -0.2884 0.1420  5   TYR   S CD2 
32172 C  CE1 . TYR   S  6   ? 1.9024 0.7951 1.5371 0.0786  -0.3313 0.0721  5   TYR   S CE1 
32173 C  CE2 . TYR   S  6   ? 1.9045 0.7538 1.5500 0.0276  -0.3234 0.0984  5   TYR   S CE2 
32174 C  CZ  . TYR   S  6   ? 1.9013 0.7781 1.5299 0.0653  -0.3278 0.0782  5   TYR   S CZ  
32175 O  OH  . TYR   S  6   ? 1.9053 0.8384 1.5321 0.0775  -0.3011 0.1329  5   TYR   S OH  
32176 N  N   . ASP   S  7   ? 1.9377 0.7292 1.6136 -0.0191 -0.3321 -0.0570 6   ASP   S N   
32177 C  CA  . ASP   S  7   ? 1.8860 0.6799 1.6494 -0.0186 -0.3634 -0.0920 6   ASP   S CA  
32178 C  C   . ASP   S  7   ? 1.8481 0.6232 1.6228 -0.0483 -0.3854 -0.1348 6   ASP   S C   
32179 O  O   . ASP   S  7   ? 1.7803 0.5160 1.5799 -0.0341 -0.4312 -0.1584 6   ASP   S O   
32180 C  CB  . ASP   S  7   ? 1.9127 0.6885 1.7284 0.0118  -0.3475 -0.0650 6   ASP   S CB  
32181 C  CG  . ASP   S  7   ? 1.9696 0.7388 1.7114 0.0221  -0.3475 -0.0694 6   ASP   S CG  
32182 O  OD1 . ASP   S  7   ? 1.9585 0.8550 1.8271 0.0288  -0.3391 -0.0107 6   ASP   S OD1 
32183 O  OD2 . ASP   S  7   ? 1.9721 0.6933 1.7237 0.0617  -0.3446 -0.0008 6   ASP   S OD2 
32184 N  N   . GLY   S  8   ? 1.8514 0.6566 1.6447 -0.0595 -0.4112 -0.1403 7   GLY   S N   
32185 C  CA  . GLY   S  8   ? 1.8504 0.7783 1.6351 -0.0911 -0.4068 -0.0842 7   GLY   S CA  
32186 C  C   . GLY   S  8   ? 1.8589 0.7810 1.6626 -0.1149 -0.3775 -0.0315 7   GLY   S C   
32187 O  O   . GLY   S  8   ? 1.8869 0.8635 1.6426 -0.1038 -0.3809 -0.0199 7   GLY   S O   
32188 N  N   . ASP   S  9   ? 1.8533 0.8258 1.6707 -0.1018 -0.3463 -0.0490 8   ASP   S N   
32189 C  CA  . ASP   S  9   ? 1.7527 0.8434 1.7376 -0.1216 -0.3440 -0.0730 8   ASP   S CA  
32190 C  C   . ASP   S  9   ? 1.7235 0.8341 1.7465 -0.1239 -0.3443 -0.0798 8   ASP   S C   
32191 O  O   . ASP   S  9   ? 1.7298 0.6971 1.7665 -0.2535 -0.3294 -0.1503 8   ASP   S O   
32192 C  CB  . ASP   S  9   ? 1.7115 0.9988 1.7716 -0.1119 -0.3364 -0.0738 8   ASP   S CB  
32193 C  CG  . ASP   S  9   ? 1.6550 1.0356 1.7916 -0.1126 -0.3959 -0.0399 8   ASP   S CG  
32194 O  OD1 . ASP   S  9   ? 1.6949 0.9907 1.8544 -0.0011 -0.3769 0.0406  8   ASP   S OD1 
32195 O  OD2 . ASP   S  9   ? 1.6958 1.1748 1.7716 -0.1683 -0.4057 -0.0641 8   ASP   S OD2 
32196 N  N   . THR   S  10  ? 1.6876 0.7877 1.7263 -0.0515 -0.3484 -0.0701 9   THR   S N   
32197 C  CA  . THR   S  10  ? 1.6797 0.7576 1.7023 0.0257  -0.3490 -0.0694 9   THR   S CA  
32198 C  C   . THR   S  10  ? 1.6594 0.6438 1.6901 0.0689  -0.3625 -0.0530 9   THR   S C   
32199 O  O   . THR   S  10  ? 1.6621 0.7072 1.6857 0.0623  -0.3501 -0.0259 9   THR   S O   
32200 C  CB  . THR   S  10  ? 1.6299 0.7680 1.7768 0.0332  -0.3501 -0.0749 9   THR   S CB  
32201 O  OG1 . THR   S  10  ? 1.6050 0.8289 1.7619 0.0654  -0.3462 -0.1230 9   THR   S OG1 
32202 C  CG2 . THR   S  10  ? 1.6320 0.8441 1.7716 0.0222  -0.3481 -0.0655 9   THR   S CG2 
32203 N  N   . VAL   S  11  ? 1.6785 0.5625 1.6373 0.1101  -0.3810 -0.0554 10  VAL   S N   
32204 C  CA  . VAL   S  11  ? 1.7154 0.5746 1.6363 0.1302  -0.3758 -0.0650 10  VAL   S CA  
32205 C  C   . VAL   S  11  ? 1.7586 0.5536 1.6388 0.1533  -0.4401 -0.0490 10  VAL   S C   
32206 O  O   . VAL   S  11  ? 1.7147 0.3948 1.6517 0.2300  -0.4512 0.0183  10  VAL   S O   
32207 C  CB  . VAL   S  11  ? 1.7008 0.6315 1.6250 0.1303  -0.3772 -0.0789 10  VAL   S CB  
32208 C  CG1 . VAL   S  11  ? 1.7276 0.6293 1.6025 0.1298  -0.3609 -0.1186 10  VAL   S CG1 
32209 C  CG2 . VAL   S  11  ? 1.6986 0.6553 1.6386 0.1303  -0.3582 -0.0779 10  VAL   S CG2 
32210 N  N   . THR   S  12  ? 1.8042 0.5418 1.5976 0.1120  -0.4492 -0.0779 11  THR   S N   
32211 C  CA  . THR   S  12  ? 1.8340 0.5571 1.6188 0.0816  -0.4801 -0.0628 11  THR   S CA  
32212 C  C   . THR   S  12  ? 1.8473 0.4812 1.6463 0.0633  -0.5254 -0.1088 11  THR   S C   
32213 O  O   . THR   S  12  ? 1.7952 0.4836 1.6943 0.0161  -0.5745 -0.1223 11  THR   S O   
32214 C  CB  . THR   S  12  ? 1.8978 0.6055 1.5799 0.0831  -0.4454 -0.0720 11  THR   S CB  
32215 O  OG1 . THR   S  12  ? 1.8873 0.6503 1.5602 0.0926  -0.3868 0.0000  11  THR   S OG1 
32216 C  CG2 . THR   S  12  ? 1.9268 0.6026 1.6103 0.0797  -0.4365 -0.0700 11  THR   S CG2 
32217 N  N   . PHE   S  13  ? 1.8142 0.3932 1.6479 0.1000  -0.5343 -0.1010 12  PHE   S N   
32218 C  CA  . PHE   S  13  ? 1.8265 0.4418 1.6593 0.1145  -0.5172 -0.0542 12  PHE   S CA  
32219 C  C   . PHE   S  13  ? 1.8732 0.4323 1.6703 0.1344  -0.5186 -0.0371 12  PHE   S C   
32220 O  O   . PHE   S  13  ? 1.8720 0.4525 1.6708 0.1546  -0.5415 -0.0363 12  PHE   S O   
32221 C  CB  . PHE   S  13  ? 1.7871 0.4117 1.6506 0.1361  -0.5379 -0.0451 12  PHE   S CB  
32222 C  CG  . PHE   S  13  ? 1.7347 0.4706 1.6491 0.1350  -0.5524 -0.0575 12  PHE   S CG  
32223 C  CD1 . PHE   S  13  ? 1.7317 0.5345 1.7063 0.1398  -0.5332 -0.0787 12  PHE   S CD1 
32224 C  CD2 . PHE   S  13  ? 1.6913 0.4668 1.5905 0.1346  -0.5642 -0.0364 12  PHE   S CD2 
32225 C  CE1 . PHE   S  13  ? 1.7282 0.5057 1.6862 0.1597  -0.5077 -0.0894 12  PHE   S CE1 
32226 C  CE2 . PHE   S  13  ? 1.6943 0.4051 1.5911 0.1518  -0.5283 -0.0321 12  PHE   S CE2 
32227 C  CZ  . PHE   S  13  ? 1.6929 0.4353 1.6386 0.1324  -0.5298 -0.0461 12  PHE   S CZ  
32228 N  N   . SER   S  14  ? 1.8535 0.5009 1.6788 0.1451  -0.4871 -0.0512 13  SER   S N   
32229 C  CA  . SER   S  14  ? 1.9122 0.4967 1.6440 0.1016  -0.4683 -0.0176 13  SER   S CA  
32230 C  C   . SER   S  14  ? 1.9379 0.3864 1.6768 0.0666  -0.4826 0.0099  13  SER   S C   
32231 O  O   . SER   S  14  ? 1.9781 0.3982 1.6653 0.0676  -0.4610 0.0178  13  SER   S O   
32232 C  CB  . SER   S  14  ? 1.9428 0.4753 1.6973 0.1305  -0.4535 -0.0172 13  SER   S CB  
32233 O  OG  . SER   S  14  ? 1.9125 0.4257 1.7267 0.1705  -0.4587 0.0137  13  SER   S OG  
32234 N  N   . PRO   S  15  ? 1.9607 0.3720 1.5754 0.0769  -0.4853 -0.0082 14  PRO   S N   
32235 C  CA  . PRO   S  15  ? 1.9591 0.3231 1.5966 0.0513  -0.5153 0.0184  14  PRO   S CA  
32236 C  C   . PRO   S  15  ? 1.9455 0.3201 1.5889 0.0502  -0.5127 0.0733  14  PRO   S C   
32237 O  O   . PRO   S  15  ? 1.9128 0.2898 1.5533 0.0323  -0.6059 0.1641  14  PRO   S O   
32238 C  CB  . PRO   S  15  ? 2.0070 0.3168 1.6039 0.0723  -0.4985 0.0018  14  PRO   S CB  
32239 C  CG  . PRO   S  15  ? 1.9911 0.3282 1.5996 0.0708  -0.4896 0.0078  14  PRO   S CG  
32240 C  CD  . PRO   S  15  ? 1.9741 0.3030 1.6098 0.0867  -0.4754 -0.0096 14  PRO   S CD  
32241 N  N   . THR   S  16  ? 1.9423 0.3645 1.6281 0.0778  -0.4927 0.0677  15  THR   S N   
32242 C  CA  . THR   S  16  ? 1.9291 0.4333 1.6591 0.0679  -0.4814 0.0363  15  THR   S CA  
32243 C  C   . THR   S  16  ? 1.9162 0.4389 1.6570 0.0811  -0.4909 -0.0041 15  THR   S C   
32244 O  O   . THR   S  16  ? 1.9247 0.4335 1.6820 0.0806  -0.4939 -0.0544 15  THR   S O   
32245 C  CB  . THR   S  16  ? 1.9810 0.3902 1.7099 0.0531  -0.4276 0.0000  15  THR   S CB  
32246 O  OG1 . THR   S  16  ? 2.0144 0.3925 1.7265 0.0301  -0.3853 -0.0195 15  THR   S OG1 
32247 C  CG2 . THR   S  16  ? 1.9955 0.4018 1.7065 0.0418  -0.4395 -0.0569 15  THR   S CG2 
32248 N  N   . GLY   S  17  ? 1.9205 0.5460 1.6177 0.0986  -0.5240 0.0282  16  GLY   S N   
32249 C  CA  . GLY   S  17  ? 1.9386 0.5539 1.6165 0.0831  -0.5179 0.0346  16  GLY   S CA  
32250 C  C   . GLY   S  17  ? 1.9612 0.5991 1.6063 0.1156  -0.4930 0.0587  16  GLY   S C   
32251 O  O   . GLY   S  17  ? 2.0420 0.4488 1.5538 0.1491  -0.4978 0.1512  16  GLY   S O   
32252 N  N   . ARG   S  18  ? 1.9572 0.6216 1.6606 0.1261  -0.4559 0.0041  17  ARG   S N   
32253 C  CA  . ARG   S  18  ? 1.9346 0.5634 1.7861 0.1291  -0.3828 -0.0513 17  ARG   S CA  
32254 C  C   . ARG   S  18  ? 1.9817 0.4662 1.8121 0.1177  -0.3500 -0.0409 17  ARG   S C   
32255 O  O   . ARG   S  18  ? 1.9949 0.3028 1.9415 0.0576  -0.3143 -0.0006 17  ARG   S O   
32256 C  CB  . ARG   S  18  ? 1.8957 0.5966 1.8059 0.1622  -0.3953 -0.0433 17  ARG   S CB  
32257 C  CG  . ARG   S  18  ? 1.9068 0.5301 1.8246 0.1410  -0.3996 -0.0524 17  ARG   S CG  
32258 C  CD  . ARG   S  18  ? 1.8936 0.5269 1.8652 0.1612  -0.3955 -0.0496 17  ARG   S CD  
32259 N  NE  . ARG   S  18  ? 1.8508 0.4689 1.8978 0.1856  -0.3993 -0.0710 17  ARG   S NE  
32260 C  CZ  . ARG   S  18  ? 1.8363 0.5491 1.9097 0.1702  -0.3921 -0.1271 17  ARG   S CZ  
32261 N  NH1 . ARG   S  18  ? 1.8647 0.5750 1.9571 0.1427  -0.3985 -0.1322 17  ARG   S NH1 
32262 N  NH2 . ARG   S  18  ? 1.8395 0.4945 1.9070 0.1565  -0.3935 -0.1312 17  ARG   S NH2 
32263 N  N   . LEU   S  19  ? 1.9286 0.4850 1.8307 0.0913  -0.3071 -0.1125 18  LEU   S N   
32264 C  CA  . LEU   S  19  ? 1.8871 0.5290 1.8295 0.1226  -0.3065 -0.1170 18  LEU   S CA  
32265 C  C   . LEU   S  19  ? 1.9480 0.4640 1.8261 0.1602  -0.3171 -0.1460 18  LEU   S C   
32266 O  O   . LEU   S  19  ? 1.9448 0.3590 1.8700 0.1859  -0.3091 -0.1436 18  LEU   S O   
32267 C  CB  . LEU   S  19  ? 1.7949 0.5429 1.8878 0.0861  -0.3143 -0.1302 18  LEU   S CB  
32268 C  CG  . LEU   S  19  ? 1.7090 0.6181 1.8916 0.0836  -0.3140 -0.1003 18  LEU   S CG  
32269 C  CD1 . LEU   S  19  ? 1.6606 0.6342 1.9010 0.0688  -0.3056 -0.1139 18  LEU   S CD1 
32270 C  CD2 . LEU   S  19  ? 1.7106 0.6288 1.8889 0.0805  -0.3420 -0.0738 18  LEU   S CD2 
32271 N  N   . PHE   S  20  ? 1.9796 0.4685 1.7749 0.1992  -0.3391 -0.1436 19  PHE   S N   
32272 C  CA  . PHE   S  20  ? 1.9602 0.4937 1.7197 0.1791  -0.3547 -0.1262 19  PHE   S CA  
32273 C  C   . PHE   S  20  ? 1.9213 0.3674 1.6511 0.1790  -0.3680 -0.2172 19  PHE   S C   
32274 O  O   . PHE   S  20  ? 1.9330 0.3658 1.6348 0.1625  -0.3611 -0.2382 19  PHE   S O   
32275 C  CB  . PHE   S  20  ? 1.9473 0.5205 1.7686 0.1416  -0.3789 -0.0878 19  PHE   S CB  
32276 C  CG  . PHE   S  20  ? 1.9622 0.5502 1.8393 0.1542  -0.3434 -0.0445 19  PHE   S CG  
32277 C  CD1 . PHE   S  20  ? 1.9839 0.5536 1.8723 0.1799  -0.3413 -0.0139 19  PHE   S CD1 
32278 C  CD2 . PHE   S  20  ? 1.9848 0.5981 1.8430 0.1773  -0.3291 0.0148  19  PHE   S CD2 
32279 C  CE1 . PHE   S  20  ? 1.9657 0.5629 1.9341 0.2326  -0.3424 0.0090  19  PHE   S CE1 
32280 C  CE2 . PHE   S  20  ? 1.9837 0.5730 1.9059 0.2104  -0.3252 0.0141  19  PHE   S CE2 
32281 C  CZ  . PHE   S  20  ? 2.0016 0.5378 1.9205 0.2248  -0.3546 0.0634  19  PHE   S CZ  
32282 N  N   . GLN   S  21  ? 1.8846 0.3330 1.5843 0.1483  -0.3667 -0.2300 20  GLN   S N   
32283 C  CA  . GLN   S  21  ? 1.8474 0.4166 1.5649 0.1524  -0.3527 -0.1970 20  GLN   S CA  
32284 C  C   . GLN   S  21  ? 1.8122 0.4329 1.5840 0.1368  -0.3288 -0.1395 20  GLN   S C   
32285 O  O   . GLN   S  21  ? 1.8394 0.3509 1.5724 0.1819  -0.3107 -0.1213 20  GLN   S O   
32286 C  CB  . GLN   S  21  ? 1.8219 0.4343 1.5398 0.1413  -0.3550 -0.2026 20  GLN   S CB  
32287 C  CG  . GLN   S  21  ? 1.8521 0.3982 1.5098 0.1362  -0.3260 -0.2496 20  GLN   S CG  
32288 C  CD  . GLN   S  21  ? 1.8613 0.4150 1.5075 0.1265  -0.3232 -0.2660 20  GLN   S CD  
32289 O  OE1 . GLN   S  21  ? 1.8329 0.3262 1.4601 0.1379  -0.3120 -0.3474 20  GLN   S OE1 
32290 N  NE2 . GLN   S  21  ? 1.8837 0.4453 1.4989 0.1495  -0.3188 -0.2992 20  GLN   S NE2 
32291 N  N   . VAL   S  22  ? 1.7710 0.4940 1.5777 0.0953  -0.3589 -0.1119 21  VAL   S N   
32292 C  CA  . VAL   S  22  ? 1.7171 0.5442 1.5469 0.1129  -0.3523 -0.1012 21  VAL   S CA  
32293 C  C   . VAL   S  22  ? 1.6480 0.6148 1.5890 0.0987  -0.3684 -0.1209 21  VAL   S C   
32294 O  O   . VAL   S  22  ? 1.6115 0.5683 1.6153 0.1420  -0.3651 -0.1308 21  VAL   S O   
32295 C  CB  . VAL   S  22  ? 1.7551 0.5809 1.5228 0.1024  -0.3458 -0.0572 21  VAL   S CB  
32296 C  CG1 . VAL   S  22  ? 1.7235 0.6052 1.5566 0.1015  -0.3282 -0.0438 21  VAL   S CG1 
32297 C  CG2 . VAL   S  22  ? 1.7199 0.6157 1.4806 0.1028  -0.3776 -0.0205 21  VAL   S CG2 
32298 N  N   . GLU   S  23  ? 1.6371 0.6214 1.6361 0.0859  -0.3981 -0.1156 22  GLU   S N   
32299 C  CA  . GLU   S  23  ? 1.6164 0.7187 1.7202 0.1094  -0.4052 -0.1573 22  GLU   S CA  
32300 C  C   . GLU   S  23  ? 1.6029 0.6432 1.7428 0.1126  -0.3780 -0.1754 22  GLU   S C   
32301 O  O   . GLU   S  23  ? 1.5747 0.6377 1.7669 0.0875  -0.4290 -0.2076 22  GLU   S O   
32302 C  CB  . GLU   S  23  ? 1.6522 0.7788 1.7492 0.0501  -0.4022 -0.1350 22  GLU   S CB  
32303 C  CG  . GLU   S  23  ? 1.6543 0.9115 1.7491 0.0388  -0.4288 -0.1426 22  GLU   S CG  
32304 C  CD  . GLU   S  23  ? 1.6922 0.9356 1.7661 0.0219  -0.4180 -0.1296 22  GLU   S CD  
32305 O  OE1 . GLU   S  23  ? 1.7303 1.0260 1.8434 0.1329  -0.3390 -0.1858 22  GLU   S OE1 
32306 O  OE2 . GLU   S  23  ? 1.6976 1.1106 1.7284 -0.0507 -0.4724 -0.1394 22  GLU   S OE2 
32307 N  N   . TYR   S  24  ? 1.6316 0.6224 1.7302 0.1456  -0.3780 -0.1767 23  TYR   S N   
32308 C  CA  . TYR   S  24  ? 1.6936 0.6833 1.7575 0.1842  -0.3193 -0.1965 23  TYR   S CA  
32309 C  C   . TYR   S  24  ? 1.7135 0.7007 1.7757 0.1425  -0.2968 -0.2601 23  TYR   S C   
32310 O  O   . TYR   S  24  ? 1.7486 0.8186 1.8314 0.1411  -0.2566 -0.3028 23  TYR   S O   
32311 C  CB  . TYR   S  24  ? 1.6812 0.6797 1.7580 0.1993  -0.3142 -0.1653 23  TYR   S CB  
32312 C  CG  . TYR   S  24  ? 1.7068 0.6197 1.7754 0.2470  -0.3130 -0.1705 23  TYR   S CG  
32313 C  CD1 . TYR   S  24  ? 1.7109 0.5930 1.8118 0.2678  -0.3146 -0.1918 23  TYR   S CD1 
32314 C  CD2 . TYR   S  24  ? 1.7165 0.6156 1.7613 0.2445  -0.3116 -0.1893 23  TYR   S CD2 
32315 C  CE1 . TYR   S  24  ? 1.7501 0.5625 1.8146 0.2874  -0.3208 -0.1517 23  TYR   S CE1 
32316 C  CE2 . TYR   S  24  ? 1.7433 0.5742 1.7492 0.2746  -0.3201 -0.1760 23  TYR   S CE2 
32317 C  CZ  . TYR   S  24  ? 1.7555 0.5799 1.7898 0.2781  -0.3173 -0.1498 23  TYR   S CZ  
32318 O  OH  . TYR   S  24  ? 1.7678 0.5842 1.8147 0.2787  -0.3180 -0.1282 23  TYR   S OH  
32319 N  N   . ALA   S  25  ? 1.7524 0.7169 1.7801 0.1319  -0.3068 -0.2936 24  ALA   S N   
32320 C  CA  . ALA   S  25  ? 1.7997 0.6940 1.8163 0.1388  -0.2735 -0.2954 24  ALA   S CA  
32321 C  C   . ALA   S  25  ? 1.7734 0.6786 1.8483 0.1390  -0.2293 -0.2953 24  ALA   S C   
32322 O  O   . ALA   S  25  ? 1.7924 0.6727 1.8621 0.1121  -0.1879 -0.3781 24  ALA   S O   
32323 C  CB  . ALA   S  25  ? 1.7750 0.7269 1.8096 0.1478  -0.2668 -0.2909 24  ALA   S CB  
32324 N  N   . LEU   S  26  ? 1.8930 0.6821 1.9002 0.1686  -0.2381 -0.2401 25  LEU   S N   
32325 C  CA  . LEU   S  26  ? 1.9127 0.6573 1.9433 0.2247  -0.2284 -0.2299 25  LEU   S CA  
32326 C  C   . LEU   S  26  ? 1.9432 0.6232 1.9631 0.2110  -0.1875 -0.2167 25  LEU   S C   
32327 O  O   . LEU   S  26  ? 1.9459 0.4842 1.9737 0.1902  -0.1011 -0.2263 25  LEU   S O   
32328 C  CB  . LEU   S  26  ? 1.9868 0.6877 1.9641 0.2366  -0.2591 -0.1953 25  LEU   S CB  
32329 C  CG  . LEU   S  26  ? 2.0064 0.7309 1.9480 0.2469  -0.2901 -0.1797 25  LEU   S CG  
32330 C  CD1 . LEU   S  26  ? 1.9997 0.7192 1.9545 0.2320  -0.2815 -0.1796 25  LEU   S CD1 
32331 C  CD2 . LEU   S  26  ? 2.0332 0.7855 1.9119 0.2420  -0.3057 -0.1702 25  LEU   S CD2 
32332 N  N   . GLU   S  27  ? 1.9709 0.7335 1.9128 0.2080  -0.2291 -0.2271 26  GLU   S N   
32333 C  CA  . GLU   S  27  ? 2.0054 0.8150 1.9639 0.2268  -0.2222 -0.2792 26  GLU   S CA  
32334 C  C   . GLU   S  27  ? 1.9483 0.7372 1.9758 0.2224  -0.2455 -0.2960 26  GLU   S C   
32335 O  O   . GLU   S  27  ? 2.0251 0.6212 2.0121 0.2463  -0.2124 -0.3698 26  GLU   S O   
32336 C  CB  . GLU   S  27  ? 2.0311 0.9276 1.9664 0.1519  -0.2291 -0.2549 26  GLU   S CB  
32337 C  CG  . GLU   S  27  ? 2.0982 1.0074 2.0056 0.1779  -0.1519 -0.2781 26  GLU   S CG  
32338 C  CD  . GLU   S  27  ? 2.1651 1.0554 2.0367 0.1796  -0.1473 -0.2140 26  GLU   S CD  
32339 O  OE1 . GLU   S  27  ? 2.2910 0.9855 2.0542 0.1895  -0.0420 -0.2477 26  GLU   S OE1 
32340 O  OE2 . GLU   S  27  ? 2.2581 1.1572 2.0474 0.1220  -0.1371 -0.1529 26  GLU   S OE2 
32341 N  N   . ALA   S  28  ? 1.9124 0.7342 1.9853 0.2044  -0.3228 -0.3348 27  ALA   S N   
32342 C  CA  . ALA   S  28  ? 1.9215 0.7360 1.9405 0.1754  -0.2968 -0.4005 27  ALA   S CA  
32343 C  C   . ALA   S  28  ? 1.8865 0.7098 2.0037 0.2248  -0.2743 -0.4422 27  ALA   S C   
32344 O  O   . ALA   S  28  ? 1.9576 0.7796 1.9466 0.3022  -0.2315 -0.5024 27  ALA   S O   
32345 C  CB  . ALA   S  28  ? 1.8809 0.6548 1.8773 0.1007  -0.3502 -0.4200 27  ALA   S CB  
32346 N  N   . ILE   S  29  ? 1.9369 0.6822 2.0023 0.2841  -0.2815 -0.4216 28  ILE   S N   
32347 C  CA  . ILE   S  29  ? 1.9325 0.7023 2.0544 0.2521  -0.2714 -0.3990 28  ILE   S CA  
32348 C  C   . ILE   S  29  ? 1.9342 0.8227 2.1529 0.2962  -0.2379 -0.4406 28  ILE   S C   
32349 O  O   . ILE   S  29  ? 1.9268 0.6277 2.1487 0.2913  -0.2506 -0.4961 28  ILE   S O   
32350 C  CB  . ILE   S  29  ? 1.9167 0.7264 2.0190 0.2079  -0.2842 -0.3628 28  ILE   S CB  
32351 C  CG1 . ILE   S  29  ? 1.8844 0.7562 1.9719 0.1905  -0.2663 -0.3468 28  ILE   S CG1 
32352 C  CG2 . ILE   S  29  ? 1.8838 0.7430 2.0192 0.2288  -0.2714 -0.3554 28  ILE   S CG2 
32353 C  CD1 . ILE   S  29  ? 1.8896 0.8046 1.9673 0.1833  -0.2520 -0.2982 28  ILE   S CD1 
32354 N  N   . LYS   S  30  ? 2.0468 0.9181 2.2044 0.1989  -0.1928 -0.3717 29  LYS   S N   
32355 C  CA  . LYS   S  30  ? 2.0557 0.9878 2.2029 0.2334  -0.1506 -0.4099 29  LYS   S CA  
32356 C  C   . LYS   S  30  ? 2.1526 0.9638 2.2054 0.1600  -0.1420 -0.4907 29  LYS   S C   
32357 O  O   . LYS   S  30  ? 2.1651 1.0608 2.2286 0.1424  -0.0734 -0.5220 29  LYS   S O   
32358 C  CB  . LYS   S  30  ? 2.0696 1.1357 2.1997 0.1553  -0.1464 -0.3393 29  LYS   S CB  
32359 C  CG  . LYS   S  30  ? 2.0892 1.2845 2.2348 0.1492  -0.1532 -0.2628 29  LYS   S CG  
32360 C  CD  . LYS   S  30  ? 2.0797 1.3465 2.1401 0.1065  -0.1566 -0.2400 29  LYS   S CD  
32361 C  CE  . LYS   S  30  ? 2.0789 1.3864 2.0892 0.0609  -0.1968 -0.1759 29  LYS   S CE  
32362 N  NZ  . LYS   S  30  ? 2.0892 1.4380 2.0687 0.0215  -0.2137 -0.1322 29  LYS   S NZ  
32363 N  N   . GLN   S  31  ? 2.0703 0.8966 2.1533 0.1433  -0.1141 -0.5703 30  GLN   S N   
32364 C  CA  . GLN   S  31  ? 2.0869 1.0011 2.1573 0.1195  -0.0885 -0.5375 30  GLN   S CA  
32365 C  C   . GLN   S  31  ? 2.0443 0.9031 2.0657 0.1853  -0.0995 -0.5641 30  GLN   S C   
32366 O  O   . GLN   S  31  ? 2.1945 0.6127 1.9929 0.0853  -0.1103 -0.7242 30  GLN   S O   
32367 C  CB  . GLN   S  31  ? 2.1113 1.2087 2.2180 0.1211  -0.1188 -0.4843 30  GLN   S CB  
32368 C  CG  . GLN   S  31  ? 2.1757 1.3328 2.3065 0.0655  -0.1161 -0.4100 30  GLN   S CG  
32369 C  CD  . GLN   S  31  ? 2.2644 1.3779 2.4349 0.1469  -0.1553 -0.4193 30  GLN   S CD  
32370 O  OE1 . GLN   S  31  ? 2.3259 1.3560 2.4191 0.1897  -0.1201 -0.4711 30  GLN   S OE1 
32371 N  NE2 . GLN   S  31  ? 2.3065 1.4718 2.5009 0.0767  -0.1816 -0.3897 30  GLN   S NE2 
32372 N  N   . GLY   S  32  ? 1.9574 0.8519 2.0372 0.2576  -0.1221 -0.4985 31  GLY   S N   
32373 C  CA  . GLY   S  32  ? 1.9030 0.8783 2.0627 0.2650  -0.1340 -0.4598 31  GLY   S CA  
32374 C  C   . GLY   S  32  ? 1.8995 0.9212 2.1088 0.2817  -0.1229 -0.4762 31  GLY   S C   
32375 O  O   . GLY   S  32  ? 1.9619 1.1125 2.0625 0.1948  -0.1734 -0.3682 31  GLY   S O   
32376 N  N   . SER   S  33  ? 1.8232 0.8097 2.1040 0.3491  -0.1221 -0.5062 32  SER   S N   
32377 C  CA  . SER   S  33  ? 1.8193 0.8668 2.1266 0.3602  -0.1168 -0.5369 32  SER   S CA  
32378 C  C   . SER   S  33  ? 1.7830 0.8310 2.1426 0.4149  -0.1349 -0.5558 32  SER   S C   
32379 O  O   . SER   S  33  ? 1.7852 0.8887 2.1489 0.4610  -0.1237 -0.5396 32  SER   S O   
32380 C  CB  . SER   S  33  ? 1.7884 0.9070 2.1443 0.3374  -0.0953 -0.5411 32  SER   S CB  
32381 O  OG  . SER   S  33  ? 1.7862 0.9877 2.2204 0.2814  -0.0829 -0.5333 32  SER   S OG  
32382 N  N   . VAL   S  34  ? 1.7707 0.9324 2.1460 0.4273  -0.1637 -0.5890 33  VAL   S N   
32383 C  CA  . VAL   S  34  ? 1.7366 1.0234 2.1731 0.4358  -0.2010 -0.5975 33  VAL   S CA  
32384 C  C   . VAL   S  34  ? 1.6195 1.0340 2.1509 0.4482  -0.2224 -0.5993 33  VAL   S C   
32385 O  O   . VAL   S  34  ? 1.5074 1.1149 2.1443 0.4580  -0.2062 -0.6292 33  VAL   S O   
32386 C  CB  . VAL   S  34  ? 1.7575 1.0784 2.2039 0.4526  -0.2332 -0.6045 33  VAL   S CB  
32387 C  CG1 . VAL   S  34  ? 1.7942 1.0998 2.2201 0.4295  -0.2028 -0.6165 33  VAL   S CG1 
32388 C  CG2 . VAL   S  34  ? 1.8001 1.1354 2.2132 0.4290  -0.2545 -0.6065 33  VAL   S CG2 
32389 N  N   . THR   S  35  ? 1.6200 1.0602 2.1320 0.4736  -0.2503 -0.5969 34  THR   S N   
32390 C  CA  . THR   S  35  ? 1.6537 1.0827 2.1334 0.4373  -0.2532 -0.5922 34  THR   S CA  
32391 C  C   . THR   S  35  ? 1.6628 1.0770 2.1529 0.4689  -0.2715 -0.5245 34  THR   S C   
32392 O  O   . THR   S  35  ? 1.6727 1.0535 2.1499 0.4906  -0.2937 -0.4878 34  THR   S O   
32393 C  CB  . THR   S  35  ? 1.6461 1.0788 2.0823 0.4293  -0.2649 -0.6274 34  THR   S CB  
32394 O  OG1 . THR   S  35  ? 1.6500 1.0712 2.0729 0.4415  -0.2381 -0.6605 34  THR   S OG1 
32395 C  CG2 . THR   S  35  ? 1.6516 1.0883 2.0458 0.4071  -0.2777 -0.6341 34  THR   S CG2 
32396 N  N   . VAL   S  36  ? 1.6779 1.1034 2.1842 0.4372  -0.2667 -0.5002 35  VAL   S N   
32397 C  CA  . VAL   S  36  ? 1.7330 1.1232 2.1846 0.4084  -0.2730 -0.4710 35  VAL   S CA  
32398 C  C   . VAL   S  36  ? 1.7730 1.0772 2.1342 0.3576  -0.2705 -0.4089 35  VAL   S C   
32399 O  O   . VAL   S  36  ? 1.8213 1.0547 2.2030 0.2973  -0.2952 -0.3904 35  VAL   S O   
32400 C  CB  . VAL   S  36  ? 1.7361 1.1618 2.2413 0.4160  -0.2498 -0.4789 35  VAL   S CB  
32401 C  CG1 . VAL   S  36  ? 1.7770 1.1652 2.2390 0.4077  -0.2573 -0.4813 35  VAL   S CG1 
32402 C  CG2 . VAL   S  36  ? 1.7514 1.1524 2.2870 0.4153  -0.2387 -0.4711 35  VAL   S CG2 
32403 N  N   . GLY   S  37  ? 1.7979 1.1111 2.1285 0.3240  -0.2702 -0.3918 36  GLY   S N   
32404 C  CA  . GLY   S  37  ? 1.7452 1.0658 2.0473 0.2819  -0.2881 -0.3318 36  GLY   S CA  
32405 C  C   . GLY   S  37  ? 1.7179 1.0017 2.0628 0.2694  -0.3026 -0.3445 36  GLY   S C   
32406 O  O   . GLY   S  37  ? 1.6461 0.9485 2.0099 0.3715  -0.3157 -0.3735 36  GLY   S O   
32407 N  N   . LEU   S  38  ? 1.7190 1.0011 2.0585 0.2580  -0.3458 -0.2736 37  LEU   S N   
32408 C  CA  . LEU   S  38  ? 1.7284 0.9826 2.0987 0.3035  -0.3789 -0.2278 37  LEU   S CA  
32409 C  C   . LEU   S  38  ? 1.7727 0.9688 2.0592 0.3013  -0.4226 -0.1871 37  LEU   S C   
32410 O  O   . LEU   S  38  ? 1.8037 0.9126 2.0707 0.3414  -0.4219 -0.2082 37  LEU   S O   
32411 C  CB  . LEU   S  38  ? 1.7466 0.9511 2.1357 0.3132  -0.3919 -0.2334 37  LEU   S CB  
32412 C  CG  . LEU   S  38  ? 1.7479 0.9846 2.1411 0.3130  -0.3748 -0.2468 37  LEU   S CG  
32413 C  CD1 . LEU   S  38  ? 1.7500 0.9956 2.1903 0.3175  -0.3715 -0.2546 37  LEU   S CD1 
32414 C  CD2 . LEU   S  38  ? 1.7371 0.9791 2.1189 0.3220  -0.3462 -0.2802 37  LEU   S CD2 
32415 N  N   . ARG   S  39  ? 1.7939 0.9291 2.0870 0.2852  -0.4794 -0.1714 38  ARG   S N   
32416 C  CA  . ARG   S  39  ? 1.7858 0.8574 2.1397 0.2988  -0.4773 -0.1085 38  ARG   S CA  
32417 C  C   . ARG   S  39  ? 1.8205 0.9236 2.2141 0.2801  -0.5356 -0.1349 38  ARG   S C   
32418 O  O   . ARG   S  39  ? 1.8605 0.9617 2.2724 0.2419  -0.5781 -0.0851 38  ARG   S O   
32419 C  CB  . ARG   S  39  ? 1.7936 0.7560 2.0506 0.2753  -0.4575 -0.0691 38  ARG   S CB  
32420 C  CG  . ARG   S  39  ? 1.8138 0.7067 2.0599 0.2614  -0.4691 -0.0373 38  ARG   S CG  
32421 C  CD  . ARG   S  39  ? 1.8141 0.7276 1.9602 0.2442  -0.4260 0.0022  38  ARG   S CD  
32422 N  NE  . ARG   S  39  ? 1.8692 0.6986 1.9849 0.2188  -0.4261 0.0573  38  ARG   S NE  
32423 C  CZ  . ARG   S  39  ? 1.8921 0.7108 1.9584 0.2250  -0.4185 0.0825  38  ARG   S CZ  
32424 N  NH1 . ARG   S  39  ? 1.8854 0.7623 1.9488 0.2192  -0.3950 0.0823  38  ARG   S NH1 
32425 N  NH2 . ARG   S  39  ? 1.8853 0.6630 1.9453 0.2288  -0.4436 0.0922  38  ARG   S NH2 
32426 N  N   . SER   S  40  ? 1.8275 0.9245 2.2139 0.2923  -0.5480 -0.1630 39  SER   S N   
32427 C  CA  . SER   S  40  ? 1.8407 1.0495 2.2285 0.2998  -0.5776 -0.1455 39  SER   S CA  
32428 C  C   . SER   S  40  ? 1.7494 1.1045 2.1775 0.2975  -0.5894 -0.1241 39  SER   S C   
32429 O  O   . SER   S  40  ? 1.7374 1.2104 2.2367 0.3739  -0.5464 -0.0181 39  SER   S O   
32430 C  CB  . SER   S  40  ? 1.8028 1.1082 2.2071 0.3046  -0.5970 -0.2109 39  SER   S CB  
32431 O  OG  . SER   S  40  ? 1.8531 1.1102 2.1780 0.2466  -0.6278 -0.2196 39  SER   S OG  
32432 N  N   . ASN   S  41  ? 1.7987 1.1194 2.1389 0.2914  -0.5576 -0.1621 40  ASN   S N   
32433 C  CA  . ASN   S  41  ? 1.7726 1.0777 2.1256 0.2620  -0.5301 -0.1462 40  ASN   S CA  
32434 C  C   . ASN   S  41  ? 1.7255 0.9733 2.1217 0.2880  -0.5250 -0.2291 40  ASN   S C   
32435 O  O   . ASN   S  41  ? 1.6594 1.0277 2.0580 0.2653  -0.5260 -0.2744 40  ASN   S O   
32436 C  CB  . ASN   S  41  ? 1.8107 1.1759 2.0992 0.2513  -0.5038 -0.1769 40  ASN   S CB  
32437 C  CG  . ASN   S  41  ? 1.7984 1.2739 2.1073 0.2027  -0.4442 -0.1663 40  ASN   S CG  
32438 O  OD1 . ASN   S  41  ? 1.7666 1.3419 2.1572 0.1761  -0.4502 -0.2023 40  ASN   S OD1 
32439 N  ND2 . ASN   S  41  ? 1.8697 1.2910 2.1346 0.2330  -0.4805 -0.1677 40  ASN   S ND2 
32440 N  N   . THR   S  42  ? 1.7141 0.8435 2.1546 0.2851  -0.5138 -0.1663 41  THR   S N   
32441 C  CA  . THR   S  42  ? 1.6594 0.8882 2.1756 0.2653  -0.5074 -0.1265 41  THR   S CA  
32442 C  C   . THR   S  42  ? 1.6560 0.8286 2.1681 0.2514  -0.5042 -0.1082 41  THR   S C   
32443 O  O   . THR   S  42  ? 1.6217 0.8836 2.1937 0.2202  -0.5268 -0.0289 41  THR   S O   
32444 C  CB  . THR   S  42  ? 1.6544 0.8799 2.2323 0.2814  -0.4723 -0.0845 41  THR   S CB  
32445 O  OG1 . THR   S  42  ? 1.5965 0.8003 2.3094 0.2695  -0.4795 -0.0451 41  THR   S OG1 
32446 C  CG2 . THR   S  42  ? 1.6343 0.9266 2.2399 0.2854  -0.4799 -0.0774 41  THR   S CG2 
32447 N  N   . HIS   S  43  ? 1.6709 0.8575 2.1102 0.2716  -0.4991 -0.1202 42  HIS   S N   
32448 C  CA  . HIS   S  43  ? 1.6779 0.9065 2.0628 0.2812  -0.4450 -0.1130 42  HIS   S CA  
32449 C  C   . HIS   S  43  ? 1.6447 0.9186 2.0593 0.2877  -0.4236 -0.1137 42  HIS   S C   
32450 O  O   . HIS   S  43  ? 1.6583 1.0194 2.0407 0.2691  -0.4542 -0.0666 42  HIS   S O   
32451 C  CB  . HIS   S  43  ? 1.7123 0.9017 2.0394 0.2262  -0.4289 -0.1266 42  HIS   S CB  
32452 C  CG  . HIS   S  43  ? 1.7653 0.8996 2.0151 0.1981  -0.4481 -0.1481 42  HIS   S CG  
32453 N  ND1 . HIS   S  43  ? 1.7961 0.9349 2.0125 0.1899  -0.4607 -0.1524 42  HIS   S ND1 
32454 C  CD2 . HIS   S  43  ? 1.8142 0.9279 1.9920 0.1854  -0.4332 -0.1478 42  HIS   S CD2 
32455 C  CE1 . HIS   S  43  ? 1.7983 0.9632 2.0065 0.1862  -0.4408 -0.1401 42  HIS   S CE1 
32456 N  NE2 . HIS   S  43  ? 1.8050 1.0188 1.9865 0.1732  -0.4497 -0.1616 42  HIS   S NE2 
32457 N  N   . ALA   S  44  ? 1.5895 0.8596 2.0302 0.2919  -0.3794 -0.1291 43  ALA   S N   
32458 C  CA  . ALA   S  44  ? 1.6098 0.8201 2.0483 0.2968  -0.3003 -0.1713 43  ALA   S CA  
32459 C  C   . ALA   S  44  ? 1.5930 0.7874 2.0859 0.2873  -0.2573 -0.2579 43  ALA   S C   
32460 O  O   . ALA   S  44  ? 1.5689 0.6979 2.0564 0.3173  -0.2077 -0.3274 43  ALA   S O   
32461 C  CB  . ALA   S  44  ? 1.6051 0.8244 2.0264 0.2691  -0.2819 -0.1285 43  ALA   S CB  
32462 N  N   . VAL   S  45  ? 1.6094 0.8067 2.1258 0.2457  -0.2493 -0.3080 44  VAL   S N   
32463 C  CA  . VAL   S  45  ? 1.6385 0.8059 2.1567 0.2532  -0.2256 -0.3402 44  VAL   S CA  
32464 C  C   . VAL   S  45  ? 1.7178 0.7198 2.1139 0.2724  -0.2103 -0.3689 44  VAL   S C   
32465 O  O   . VAL   S  45  ? 1.8029 0.7230 2.0901 0.2903  -0.1961 -0.3719 44  VAL   S O   
32466 C  CB  . VAL   S  45  ? 1.6259 0.8442 2.2472 0.2443  -0.2273 -0.3732 44  VAL   S CB  
32467 C  CG1 . VAL   S  45  ? 1.6050 0.8837 2.2669 0.2420  -0.2248 -0.4012 44  VAL   S CG1 
32468 C  CG2 . VAL   S  45  ? 1.6514 0.8555 2.2931 0.2245  -0.2221 -0.3746 44  VAL   S CG2 
32469 N  N   . LEU   S  46  ? 1.7398 0.6390 2.0929 0.2788  -0.1935 -0.3683 45  LEU   S N   
32470 C  CA  . LEU   S  46  ? 1.7320 0.6760 2.0957 0.2695  -0.2450 -0.3444 45  LEU   S CA  
32471 C  C   . LEU   S  46  ? 1.7431 0.8663 2.1320 0.2535  -0.1993 -0.3493 45  LEU   S C   
32472 O  O   . LEU   S  46  ? 1.8304 0.7949 2.1663 0.2273  -0.2519 -0.3028 45  LEU   S O   
32473 C  CB  . LEU   S  46  ? 1.7341 0.5806 2.0528 0.2765  -0.2167 -0.3494 45  LEU   S CB  
32474 C  CG  . LEU   S  46  ? 1.7323 0.6063 2.0090 0.2626  -0.2223 -0.3150 45  LEU   S CG  
32475 C  CD1 . LEU   S  46  ? 1.7381 0.6863 2.0028 0.2524  -0.2374 -0.2828 45  LEU   S CD1 
32476 C  CD2 . LEU   S  46  ? 1.7425 0.5787 1.9970 0.2882  -0.2429 -0.2988 45  LEU   S CD2 
32477 N  N   . VAL   S  47  ? 1.7570 0.8904 2.1926 0.2803  -0.1894 -0.4153 46  VAL   S N   
32478 C  CA  . VAL   S  47  ? 1.8152 0.9335 2.2397 0.2576  -0.1507 -0.4628 46  VAL   S CA  
32479 C  C   . VAL   S  47  ? 1.7824 0.9509 2.2436 0.2503  -0.1241 -0.4696 46  VAL   S C   
32480 O  O   . VAL   S  47  ? 1.7081 0.9732 2.2110 0.2663  -0.1097 -0.4956 46  VAL   S O   
32481 C  CB  . VAL   S  47  ? 1.8708 0.9355 2.3066 0.2688  -0.1676 -0.4258 46  VAL   S CB  
32482 C  CG1 . VAL   S  47  ? 1.9145 0.9100 2.3497 0.2669  -0.1264 -0.4267 46  VAL   S CG1 
32483 C  CG2 . VAL   S  47  ? 1.8682 1.0130 2.3075 0.2476  -0.1750 -0.4244 46  VAL   S CG2 
32484 N  N   . ALA   S  48  ? 1.8365 1.0366 2.2480 0.2340  -0.1361 -0.4632 47  ALA   S N   
32485 C  CA  . ALA   S  48  ? 1.8583 1.0918 2.2720 0.2413  -0.1904 -0.4372 47  ALA   S CA  
32486 C  C   . ALA   S  48  ? 1.9869 1.2019 2.3290 0.2549  -0.1178 -0.4651 47  ALA   S C   
32487 O  O   . ALA   S  48  ? 1.9854 1.0823 2.4824 0.2267  -0.1125 -0.4686 47  ALA   S O   
32488 C  CB  . ALA   S  48  ? 1.8743 1.0225 2.2050 0.2370  -0.1705 -0.4419 47  ALA   S CB  
32489 N  N   . LEU   S  49  ? 2.1325 1.2139 2.3573 0.2289  -0.1617 -0.4635 48  LEU   S N   
32490 C  CA  . LEU   S  49  ? 2.1918 1.3879 2.2992 0.1974  -0.1846 -0.4766 48  LEU   S CA  
32491 C  C   . LEU   S  49  ? 2.2102 1.3586 2.2498 0.1629  -0.1902 -0.4871 48  LEU   S C   
32492 O  O   . LEU   S  49  ? 2.1965 1.3073 2.1950 0.2174  -0.1441 -0.5881 48  LEU   S O   
32493 C  CB  . LEU   S  49  ? 2.2610 1.4421 2.3586 0.2320  -0.1889 -0.3616 48  LEU   S CB  
32494 C  CG  . LEU   S  49  ? 2.2884 1.5576 2.3212 0.2761  -0.1280 -0.3370 48  LEU   S CG  
32495 C  CD1 . LEU   S  49  ? 2.3067 1.6748 2.3668 0.2817  -0.0861 -0.3135 48  LEU   S CD1 
32496 C  CD2 . LEU   S  49  ? 2.3086 1.5358 2.3295 0.3107  -0.1411 -0.3177 48  LEU   S CD2 
32497 N  N   . LYS   S  50  ? 2.1993 1.3879 2.2685 0.1717  -0.2369 -0.4295 49  LYS   S N   
32498 C  CA  . LYS   S  50  ? 2.1908 1.3287 2.3166 0.2102  -0.2080 -0.3314 49  LYS   S CA  
32499 C  C   . LYS   S  50  ? 2.1582 1.2720 2.3123 0.2531  -0.2938 -0.2821 49  LYS   S C   
32500 O  O   . LYS   S  50  ? 2.3155 1.0872 2.3732 0.2818  -0.2392 -0.2769 49  LYS   S O   
32501 C  CB  . LYS   S  50  ? 2.1453 1.2546 2.3346 0.2065  -0.1607 -0.4099 49  LYS   S CB  
32502 C  CG  . LYS   S  50  ? 2.1135 1.3888 2.2919 0.2049  -0.0968 -0.4835 49  LYS   S CG  
32503 C  CD  . LYS   S  50  ? 2.1794 1.5368 2.3103 0.1389  -0.0365 -0.4164 49  LYS   S CD  
32504 C  CE  . LYS   S  50  ? 2.2041 1.6087 2.3537 0.1178  0.0083  -0.4081 49  LYS   S CE  
32505 N  NZ  . LYS   S  50  ? 2.2241 1.6125 2.3390 0.0878  0.0478  -0.4173 49  LYS   S NZ  
32506 N  N   . ARG   S  51  ? 2.1991 1.2511 2.2534 0.2161  -0.3277 -0.2481 50  ARG   S N   
32507 C  CA  . ARG   S  51  ? 2.1801 1.2473 2.2160 0.2246  -0.2939 -0.2568 50  ARG   S CA  
32508 C  C   . ARG   S  51  ? 2.2806 1.2641 2.1453 0.2676  -0.2593 -0.3206 50  ARG   S C   
32509 O  O   . ARG   S  51  ? 2.2944 1.3211 2.1009 0.3029  -0.2630 -0.3102 50  ARG   S O   
32510 C  CB  . ARG   S  51  ? 2.1447 1.2939 2.1921 0.1750  -0.3830 -0.2102 50  ARG   S CB  
32511 C  CG  . ARG   S  51  ? 2.0634 1.3442 2.2241 0.0670  -0.4188 -0.1753 50  ARG   S CG  
32512 C  CD  . ARG   S  51  ? 2.0672 1.2841 2.3036 -0.0004 -0.4821 -0.1621 50  ARG   S CD  
32513 N  NE  . ARG   S  51  ? 2.0659 1.1822 2.4121 -0.0190 -0.5287 -0.1381 50  ARG   S NE  
32514 C  CZ  . ARG   S  51  ? 2.0988 1.1804 2.4871 -0.0729 -0.4937 -0.1607 50  ARG   S CZ  
32515 N  NH1 . ARG   S  51  ? 2.1035 1.1477 2.4491 -0.0633 -0.5570 -0.1185 50  ARG   S NH1 
32516 N  NH2 . ARG   S  51  ? 2.0819 1.1067 2.5197 -0.0373 -0.5077 -0.2033 50  ARG   S NH2 
32517 N  N   . ASN   S  52  ? 2.3379 1.4047 2.2372 0.3298  -0.1800 -0.3637 51  ASN   S N   
32518 C  CA  . ASN   S  52  ? 2.3430 1.5002 2.1923 0.3482  -0.1057 -0.3901 51  ASN   S CA  
32519 C  C   . ASN   S  52  ? 2.3645 1.6971 2.1868 0.2655  -0.1236 -0.4137 51  ASN   S C   
32520 O  O   . ASN   S  52  ? 2.3695 1.7815 2.2925 0.1577  -0.0449 -0.3632 51  ASN   S O   
32521 C  CB  . ASN   S  52  ? 2.3268 1.4640 2.2592 0.4751  -0.0733 -0.4255 51  ASN   S CB  
32522 C  CG  . ASN   S  52  ? 2.2550 1.6127 2.2570 0.5846  -0.0199 -0.4409 51  ASN   S CG  
32523 O  OD1 . ASN   S  52  ? 2.1969 1.4875 2.2298 0.8124  -0.0642 -0.4500 51  ASN   S OD1 
32524 N  ND2 . ASN   S  52  ? 2.1847 1.5385 2.3362 0.7173  -0.0152 -0.4746 51  ASN   S ND2 
32525 N  N   . ALA   S  53  ? 2.3845 1.6307 2.1451 0.2236  -0.1208 -0.4316 52  ALA   S N   
32526 C  CA  . ALA   S  53  ? 2.3722 1.5253 2.0596 0.3043  -0.1418 -0.4159 52  ALA   S CA  
32527 C  C   . ALA   S  53  ? 2.4610 1.2493 2.1732 0.2880  -0.2061 -0.4707 52  ALA   S C   
32528 O  O   . ALA   S  53  ? 2.4444 1.1991 2.0779 0.3891  -0.1808 -0.6019 52  ALA   S O   
32529 C  CB  . ALA   S  53  ? 2.3409 1.5588 2.0427 0.2462  -0.1643 -0.3853 52  ALA   S CB  
32530 N  N   . ASP   S  54  ? 2.4276 1.2354 2.2245 0.3451  -0.1699 -0.4795 53  ASP   S N   
32531 C  CA  . ASP   S  54  ? 2.4003 1.2683 2.3425 0.3498  -0.1268 -0.4421 53  ASP   S CA  
32532 C  C   . ASP   S  54  ? 2.3791 1.2625 2.4101 0.3589  -0.1555 -0.4173 53  ASP   S C   
32533 O  O   . ASP   S  54  ? 2.2838 1.2531 2.3303 0.4453  -0.0723 -0.3933 53  ASP   S O   
32534 C  CB  . ASP   S  54  ? 2.4635 1.3625 2.3289 0.2973  -0.1587 -0.3923 53  ASP   S CB  
32535 C  CG  . ASP   S  54  ? 2.4983 1.2639 2.3272 0.2597  -0.1427 -0.4071 53  ASP   S CG  
32536 O  OD1 . ASP   S  54  ? 2.4945 1.2103 2.2663 0.3290  -0.1101 -0.4557 53  ASP   S OD1 
32537 O  OD2 . ASP   S  54  ? 2.5215 1.3165 2.3050 0.2539  -0.1956 -0.2894 53  ASP   S OD2 
32538 N  N   . GLU   S  55  ? 2.3244 1.3421 2.5071 0.3176  -0.1239 -0.3820 54  GLU   S N   
32539 C  CA  . GLU   S  55  ? 2.3521 1.4054 2.6238 0.2703  -0.1737 -0.3244 54  GLU   S CA  
32540 C  C   . GLU   S  55  ? 2.2961 1.3736 2.5759 0.3031  -0.1207 -0.3668 54  GLU   S C   
32541 O  O   . GLU   S  55  ? 2.3246 1.2272 2.6476 0.3383  -0.0862 -0.4354 54  GLU   S O   
32542 C  CB  . GLU   S  55  ? 2.3130 1.4055 2.7081 0.2740  -0.1921 -0.2960 54  GLU   S CB  
32543 C  CG  . GLU   S  55  ? 2.3385 1.4136 2.8192 0.2788  -0.2409 -0.2335 54  GLU   S CG  
32544 C  CD  . GLU   S  55  ? 2.3241 1.3500 2.8214 0.3011  -0.3596 -0.1841 54  GLU   S CD  
32545 O  OE1 . GLU   S  55  ? 2.3133 1.4274 2.7909 0.3013  -0.4336 -0.1398 54  GLU   S OE1 
32546 O  OE2 . GLU   S  55  ? 2.3955 1.2460 2.9263 0.3415  -0.4789 -0.1786 54  GLU   S OE2 
32547 N  N   . LEU   S  56  ? 2.3129 1.4659 2.4772 0.3106  -0.1155 -0.3977 55  LEU   S N   
32548 C  CA  . LEU   S  56  ? 2.3427 1.5077 2.3471 0.2656  -0.1010 -0.3835 55  LEU   S CA  
32549 C  C   . LEU   S  56  ? 2.3263 1.5316 2.2872 0.2018  -0.1394 -0.4420 55  LEU   S C   
32550 O  O   . LEU   S  56  ? 2.3002 1.5332 2.1755 0.0589  -0.1262 -0.4641 55  LEU   S O   
32551 C  CB  . LEU   S  56  ? 2.3809 1.5790 2.2833 0.2446  -0.0770 -0.3684 55  LEU   S CB  
32552 C  CG  . LEU   S  56  ? 2.3872 1.6366 2.3022 0.2352  -0.0522 -0.3794 55  LEU   S CG  
32553 C  CD1 . LEU   S  56  ? 2.4118 1.6687 2.3447 0.2753  -0.0307 -0.3596 55  LEU   S CD1 
32554 C  CD2 . LEU   S  56  ? 2.4137 1.6207 2.3047 0.1944  -0.0353 -0.3755 55  LEU   S CD2 
32555 N  N   . SER   S  57  ? 2.2804 1.3689 2.2766 0.2586  -0.1660 -0.4394 56  SER   S N   
32556 C  CA  . SER   S  57  ? 2.2262 1.2955 2.2488 0.2758  -0.1995 -0.3897 56  SER   S CA  
32557 C  C   . SER   S  57  ? 2.1918 1.2856 2.2072 0.3728  -0.1909 -0.4284 56  SER   S C   
32558 O  O   . SER   S  57  ? 2.2228 1.4007 2.2117 0.4265  -0.1636 -0.2970 56  SER   S O   
32559 C  CB  . SER   S  57  ? 2.2158 1.1091 2.1810 0.3170  -0.2643 -0.3553 56  SER   S CB  
32560 O  OG  . SER   S  57  ? 2.1613 0.9450 2.2149 0.3214  -0.2819 -0.3862 56  SER   S OG  
32561 N  N   . SER   S  58  ? 2.2579 1.2637 2.1827 0.3363  -0.2239 -0.4783 57  SER   S N   
32562 C  CA  . SER   S  58  ? 2.2554 1.2228 2.1674 0.3398  -0.2503 -0.4361 57  SER   S CA  
32563 C  C   . SER   S  58  ? 2.2597 1.1323 2.2348 0.3709  -0.2530 -0.4059 57  SER   S C   
32564 O  O   . SER   S  58  ? 2.2634 1.0286 2.0892 0.4416  -0.3000 -0.3077 57  SER   S O   
32565 C  CB  . SER   S  58  ? 2.2350 1.2189 2.1560 0.3215  -0.2845 -0.4809 57  SER   S CB  
32566 O  OG  . SER   S  58  ? 2.2264 1.2055 2.1189 0.3438  -0.2745 -0.5286 57  SER   S OG  
32567 N  N   . TYR   S  59  ? 2.1648 1.1423 2.2721 0.3295  -0.2131 -0.4446 58  TYR   S N   
32568 C  CA  . TYR   S  59  ? 2.0386 1.1918 2.3118 0.3292  -0.1518 -0.4144 58  TYR   S CA  
32569 C  C   . TYR   S  59  ? 1.9959 1.3006 2.3134 0.2576  -0.0739 -0.4014 58  TYR   S C   
32570 O  O   . TYR   S  59  ? 1.9936 1.3068 2.2561 0.1635  -0.0587 -0.3194 58  TYR   S O   
32571 C  CB  . TYR   S  59  ? 1.9896 1.1947 2.3567 0.4032  -0.1043 -0.4441 58  TYR   S CB  
32572 C  CG  . TYR   S  59  ? 1.9341 1.2949 2.3761 0.4610  -0.0865 -0.4319 58  TYR   S CG  
32573 C  CD1 . TYR   S  59  ? 1.9107 1.3451 2.4105 0.4986  -0.0442 -0.4798 58  TYR   S CD1 
32574 C  CD2 . TYR   S  59  ? 1.8712 1.2969 2.3736 0.5479  -0.0799 -0.4310 58  TYR   S CD2 
32575 C  CE1 . TYR   S  59  ? 1.8723 1.3660 2.4108 0.5508  -0.0314 -0.4092 58  TYR   S CE1 
32576 C  CE2 . TYR   S  59  ? 1.8277 1.2790 2.4153 0.5667  -0.0801 -0.3837 58  TYR   S CE2 
32577 C  CZ  . TYR   S  59  ? 1.7772 1.2707 2.4422 0.6459  -0.0268 -0.4825 58  TYR   S CZ  
32578 O  OH  . TYR   S  59  ? 1.7899 1.1568 2.4699 0.6067  -0.0383 -0.4550 58  TYR   S OH  
32579 N  N   . GLN   S  60  ? 2.0003 1.3086 2.3429 0.2214  -0.0955 -0.4371 59  GLN   S N   
32580 C  CA  . GLN   S  60  ? 1.9154 1.3497 2.2759 0.1911  -0.1384 -0.4123 59  GLN   S CA  
32581 C  C   . GLN   S  60  ? 1.8549 1.4058 2.2466 0.2430  -0.1502 -0.4112 59  GLN   S C   
32582 O  O   . GLN   S  60  ? 1.9186 1.5705 2.1034 0.1792  -0.2693 -0.4690 59  GLN   S O   
32583 C  CB  . GLN   S  60  ? 1.9875 1.2867 2.3369 0.1866  -0.1437 -0.4076 59  GLN   S CB  
32584 C  CG  . GLN   S  60  ? 2.0026 1.1802 2.3263 0.1983  -0.1465 -0.3711 59  GLN   S CG  
32585 C  CD  . GLN   S  60  ? 2.0289 1.0850 2.3413 0.2204  -0.1464 -0.3592 59  GLN   S CD  
32586 O  OE1 . GLN   S  60  ? 2.0682 0.9499 2.3730 0.2271  -0.1246 -0.3364 59  GLN   S OE1 
32587 N  NE2 . GLN   S  60  ? 2.0363 1.0628 2.3203 0.2183  -0.1417 -0.3580 59  GLN   S NE2 
32588 N  N   . LYS   S  61  ? 1.7099 1.3951 2.1730 0.3141  -0.1321 -0.3054 60  LYS   S N   
32589 C  CA  . LYS   S  61  ? 1.6313 1.3124 2.1609 0.3676  -0.1210 -0.2745 60  LYS   S CA  
32590 C  C   . LYS   S  61  ? 1.6175 1.2259 2.1834 0.3896  -0.1156 -0.2579 60  LYS   S C   
32591 O  O   . LYS   S  61  ? 1.6161 1.2427 2.1340 0.4106  -0.1386 -0.2450 60  LYS   S O   
32592 C  CB  . LYS   S  61  ? 1.5723 1.3383 2.1236 0.4040  -0.0769 -0.2368 60  LYS   S CB  
32593 C  CG  . LYS   S  61  ? 1.5390 1.4120 2.0968 0.3871  -0.0562 -0.2224 60  LYS   S CG  
32594 C  CD  . LYS   S  61  ? 1.5087 1.4549 2.0955 0.3646  -0.0520 -0.1650 60  LYS   S CD  
32595 C  CE  . LYS   S  61  ? 1.4191 1.4779 2.0657 0.3640  -0.0636 -0.1470 60  LYS   S CE  
32596 N  NZ  . LYS   S  61  ? 1.4200 1.4655 2.0309 0.3898  -0.0657 -0.1290 60  LYS   S NZ  
32597 N  N   . LYS   S  62  ? 1.7073 1.1341 2.1848 0.3744  -0.1343 -0.2484 61  LYS   S N   
32598 C  CA  . LYS   S  62  ? 1.8073 1.1099 2.1937 0.2869  -0.1299 -0.2697 61  LYS   S CA  
32599 C  C   . LYS   S  62  ? 1.6893 0.9350 2.2145 0.2526  -0.2014 -0.2179 61  LYS   S C   
32600 O  O   . LYS   S  62  ? 1.6529 0.8226 2.1694 0.2410  -0.2453 -0.2430 61  LYS   S O   
32601 C  CB  . LYS   S  62  ? 1.9434 1.1284 2.3181 0.2852  -0.1560 -0.1656 61  LYS   S CB  
32602 C  CG  . LYS   S  62  ? 2.1149 1.0731 2.3626 0.1502  -0.1519 -0.1715 61  LYS   S CG  
32603 C  CD  . LYS   S  62  ? 2.1926 1.0298 2.3698 0.1324  -0.1734 -0.1293 61  LYS   S CD  
32604 C  CE  . LYS   S  62  ? 2.2063 0.9151 2.4250 0.1283  -0.1625 -0.1339 61  LYS   S CE  
32605 N  NZ  . LYS   S  62  ? 2.2236 0.8393 2.3889 0.1447  -0.1734 -0.1187 61  LYS   S NZ  
32606 N  N   . ILE   S  63  ? 1.6513 0.9434 2.1361 0.2461  -0.2102 -0.2653 62  ILE   S N   
32607 C  CA  . ILE   S  63  ? 1.5995 0.9437 2.1005 0.2445  -0.2292 -0.2469 62  ILE   S CA  
32608 C  C   . ILE   S  63  ? 1.5834 0.8899 1.9723 0.2016  -0.2460 -0.2833 62  ILE   S C   
32609 O  O   . ILE   S  63  ? 1.5482 0.8085 1.9579 0.1509  -0.2439 -0.3121 62  ILE   S O   
32610 C  CB  . ILE   S  63  ? 1.5826 0.9894 2.1346 0.2383  -0.1965 -0.2473 62  ILE   S CB  
32611 C  CG1 . ILE   S  63  ? 1.5906 0.9897 2.1761 0.2458  -0.1917 -0.2280 62  ILE   S CG1 
32612 C  CG2 . ILE   S  63  ? 1.5540 1.0310 2.1179 0.2019  -0.1871 -0.2592 62  ILE   S CG2 
32613 C  CD1 . ILE   S  63  ? 1.5914 0.9834 2.1971 0.2579  -0.1981 -0.2048 62  ILE   S CD1 
32614 N  N   . ILE   S  64  ? 1.5689 0.7549 1.9714 0.2373  -0.2978 -0.2641 63  ILE   S N   
32615 C  CA  . ILE   S  64  ? 1.5854 0.7005 1.9310 0.1910  -0.3027 -0.2314 63  ILE   S CA  
32616 C  C   . ILE   S  64  ? 1.6211 0.6734 1.9282 0.2279  -0.2686 -0.2376 63  ILE   S C   
32617 O  O   . ILE   S  64  ? 1.6569 0.4672 1.9316 0.2492  -0.2284 -0.2735 63  ILE   S O   
32618 C  CB  . ILE   S  64  ? 1.5787 0.6260 1.8706 0.2329  -0.3531 -0.2072 63  ILE   S CB  
32619 C  CG1 . ILE   S  64  ? 1.6063 0.6138 1.8574 0.2770  -0.3358 -0.2128 63  ILE   S CG1 
32620 C  CG2 . ILE   S  64  ? 1.5568 0.5702 1.8245 0.1849  -0.3623 -0.2345 63  ILE   S CG2 
32621 C  CD1 . ILE   S  64  ? 1.6124 0.5507 1.8378 0.2830  -0.3308 -0.2026 63  ILE   S CD1 
32622 N  N   . LYS   S  65  ? 1.6252 0.7219 1.9377 0.2040  -0.2253 -0.1750 64  LYS   S N   
32623 C  CA  . LYS   S  65  ? 1.6465 0.7530 1.9241 0.1473  -0.2372 -0.1709 64  LYS   S CA  
32624 C  C   . LYS   S  65  ? 1.6445 0.7476 1.9363 0.1300  -0.2254 -0.1243 64  LYS   S C   
32625 O  O   . LYS   S  65  ? 1.7443 0.7596 1.9422 0.0898  -0.2768 -0.1062 64  LYS   S O   
32626 C  CB  . LYS   S  65  ? 1.6294 0.7732 1.9176 0.1492  -0.2038 -0.1824 64  LYS   S CB  
32627 C  CG  . LYS   S  65  ? 1.6255 0.8295 1.8717 0.1192  -0.1865 -0.1897 64  LYS   S CG  
32628 C  CD  . LYS   S  65  ? 1.6227 0.8824 1.8418 0.0910  -0.1714 -0.2195 64  LYS   S CD  
32629 C  CE  . LYS   S  65  ? 1.6191 0.8691 1.8102 0.0947  -0.1593 -0.2079 64  LYS   S CE  
32630 N  NZ  . LYS   S  65  ? 1.6409 0.8345 1.7965 0.1087  -0.1406 -0.2180 64  LYS   S NZ  
32631 N  N   . CYS   S  66  ? 1.6838 0.7498 1.9119 0.1046  -0.2258 -0.0460 65  CYS   S N   
32632 C  CA  . CYS   S  66  ? 1.6673 0.8313 1.9173 0.1109  -0.2029 0.0389  65  CYS   S CA  
32633 C  C   . CYS   S  66  ? 1.6973 0.8578 1.8585 0.0919  -0.2017 0.0298  65  CYS   S C   
32634 O  O   . CYS   S  66  ? 1.5729 1.0546 1.8113 0.0752  -0.2053 0.0893  65  CYS   S O   
32635 C  CB  . CYS   S  66  ? 1.6783 0.8263 1.9780 0.1387  -0.2001 0.0898  65  CYS   S CB  
32636 S  SG  . CYS   S  66  ? 1.6848 0.8574 2.0993 0.0648  -0.2355 0.1605  65  CYS   S SG  
32637 N  N   . ASP   S  67  ? 1.7116 0.8225 1.8120 0.1395  -0.2168 0.0224  66  ASP   S N   
32638 C  CA  . ASP   S  67  ? 1.6973 0.7985 1.8490 0.1478  -0.1873 0.0310  66  ASP   S CA  
32639 C  C   . ASP   S  67  ? 1.6725 0.6664 1.8513 0.1621  -0.2159 0.0193  66  ASP   S C   
32640 O  O   . ASP   S  67  ? 1.5358 0.6378 1.7660 0.1132  -0.2486 0.0513  66  ASP   S O   
32641 C  CB  . ASP   S  67  ? 1.8172 0.8667 1.8564 0.1557  -0.1450 0.0486  66  ASP   S CB  
32642 C  CG  . ASP   S  67  ? 1.8587 0.9179 1.8981 0.2196  -0.0977 -0.0213 66  ASP   S CG  
32643 O  OD1 . ASP   S  67  ? 1.9019 0.9856 1.9945 0.2274  -0.0697 0.0496  66  ASP   S OD1 
32644 O  OD2 . ASP   S  67  ? 1.8974 0.9925 1.8301 0.2016  -0.0968 -0.0135 66  ASP   S OD2 
32645 N  N   . GLU   S  68  ? 1.6154 0.7185 1.9182 0.1650  -0.2017 -0.0498 67  GLU   S N   
32646 C  CA  . GLU   S  68  ? 1.6314 0.7130 1.9555 0.1424  -0.2176 -0.1212 67  GLU   S CA  
32647 C  C   . GLU   S  68  ? 1.6254 0.6581 1.9157 0.1068  -0.2344 -0.1625 67  GLU   S C   
32648 O  O   . GLU   S  68  ? 1.5876 0.6580 1.9360 0.0040  -0.2349 -0.2146 67  GLU   S O   
32649 C  CB  . GLU   S  68  ? 1.6644 0.7301 1.9933 0.0974  -0.2189 -0.1291 67  GLU   S CB  
32650 C  CG  . GLU   S  68  ? 1.7149 0.7426 1.9613 0.0713  -0.1972 -0.1243 67  GLU   S CG  
32651 C  CD  . GLU   S  68  ? 1.6717 0.7520 2.0129 0.0998  -0.1620 -0.1599 67  GLU   S CD  
32652 O  OE1 . GLU   S  68  ? 1.6870 0.6181 1.9816 0.1610  -0.1200 -0.1869 67  GLU   S OE1 
32653 O  OE2 . GLU   S  68  ? 1.8303 0.8822 1.9684 0.1211  -0.1823 -0.1516 67  GLU   S OE2 
32654 N  N   . HIS   S  69  ? 1.5950 0.6316 1.8880 0.1291  -0.2348 -0.1988 68  HIS   S N   
32655 C  CA  . HIS   S  69  ? 1.5718 0.6930 1.8867 0.1811  -0.2710 -0.2236 68  HIS   S CA  
32656 C  C   . HIS   S  69  ? 1.5642 0.7058 1.8982 0.1701  -0.2965 -0.1687 68  HIS   S C   
32657 O  O   . HIS   S  69  ? 1.5406 0.7201 1.9153 0.1273  -0.2707 -0.1281 68  HIS   S O   
32658 C  CB  . HIS   S  69  ? 1.5352 0.6360 1.9192 0.1940  -0.2819 -0.2442 68  HIS   S CB  
32659 C  CG  . HIS   S  69  ? 1.5341 0.5248 1.8885 0.2000  -0.2781 -0.2927 68  HIS   S CG  
32660 N  ND1 . HIS   S  69  ? 1.5266 0.4137 1.8870 0.1774  -0.3022 -0.3362 68  HIS   S ND1 
32661 C  CD2 . HIS   S  69  ? 1.5314 0.4700 1.8973 0.2013  -0.2652 -0.3020 68  HIS   S CD2 
32662 C  CE1 . HIS   S  69  ? 1.5249 0.3697 1.8744 0.1672  -0.2980 -0.3353 68  HIS   S CE1 
32663 N  NE2 . HIS   S  69  ? 1.5200 0.3909 1.8942 0.1956  -0.2830 -0.3186 68  HIS   S NE2 
32664 N  N   . MET   S  70  ? 1.5856 0.6536 1.8966 0.1630  -0.2866 -0.1879 69  MET   S N   
32665 C  CA  . MET   S  70  ? 1.6246 0.5938 1.9038 0.2019  -0.2664 -0.2149 69  MET   S CA  
32666 C  C   . MET   S  70  ? 1.6493 0.6191 1.9177 0.1816  -0.2627 -0.2287 69  MET   S C   
32667 O  O   . MET   S  70  ? 1.7016 0.3423 1.9994 0.1835  -0.2535 -0.2984 69  MET   S O   
32668 C  CB  . MET   S  70  ? 1.6472 0.6062 1.8532 0.2212  -0.2523 -0.2284 69  MET   S CB  
32669 C  CG  . MET   S  70  ? 1.6777 0.6318 1.8346 0.2185  -0.2434 -0.2183 69  MET   S CG  
32670 S  SD  . MET   S  70  ? 1.6949 0.7232 1.8698 0.3106  -0.2533 -0.2515 69  MET   S SD  
32671 C  CE  . MET   S  70  ? 1.6825 0.7148 1.8584 0.2364  -0.2853 -0.2320 69  MET   S CE  
32672 N  N   . GLY   S  71  ? 1.6218 0.6225 2.0028 0.1731  -0.2820 -0.2208 70  GLY   S N   
32673 C  CA  . GLY   S  71  ? 1.6019 0.6832 1.9916 0.1850  -0.2679 -0.2337 70  GLY   S CA  
32674 C  C   . GLY   S  71  ? 1.6043 0.6736 2.0040 0.2135  -0.2722 -0.2416 70  GLY   S C   
32675 O  O   . GLY   S  71  ? 1.5780 0.6462 2.0055 0.2275  -0.3272 -0.2834 70  GLY   S O   
32676 N  N   . LEU   S  72  ? 1.6002 0.7196 1.9734 0.1802  -0.2575 -0.2317 71  LEU   S N   
32677 C  CA  . LEU   S  72  ? 1.5918 0.7361 2.0020 0.1441  -0.2788 -0.2007 71  LEU   S CA  
32678 C  C   . LEU   S  72  ? 1.5375 0.7118 2.0120 0.1206  -0.2642 -0.1973 71  LEU   S C   
32679 O  O   . LEU   S  72  ? 1.4962 0.6752 2.0092 0.1180  -0.2665 -0.2043 71  LEU   S O   
32680 C  CB  . LEU   S  72  ? 1.6003 0.7682 1.9687 0.1250  -0.3003 -0.1787 71  LEU   S CB  
32681 C  CG  . LEU   S  72  ? 1.6563 0.7178 1.9245 0.1774  -0.2982 -0.1557 71  LEU   S CG  
32682 C  CD1 . LEU   S  72  ? 1.6417 0.7000 1.8943 0.1665  -0.3159 -0.1698 71  LEU   S CD1 
32683 C  CD2 . LEU   S  72  ? 1.6867 0.7766 1.9241 0.1576  -0.2830 -0.1294 71  LEU   S CD2 
32684 N  N   . SER   S  73  ? 1.5722 0.7129 2.1034 0.1351  -0.2897 -0.2001 72  SER   S N   
32685 C  CA  . SER   S  73  ? 1.6275 0.6830 2.1324 0.1119  -0.2867 -0.1998 72  SER   S CA  
32686 C  C   . SER   S  73  ? 1.6613 0.5964 2.1156 0.1166  -0.3121 -0.1626 72  SER   S C   
32687 O  O   . SER   S  73  ? 1.5889 0.3677 2.0989 0.0861  -0.3533 -0.1335 72  SER   S O   
32688 C  CB  . SER   S  73  ? 1.6325 0.7545 2.1997 0.1331  -0.2799 -0.1842 72  SER   S CB  
32689 O  OG  . SER   S  73  ? 1.6689 0.7122 2.2640 0.0946  -0.2883 -0.1740 72  SER   S OG  
32690 N  N   . LEU   S  74  ? 1.7285 0.6311 2.0925 0.1035  -0.3093 -0.1484 73  LEU   S N   
32691 C  CA  . LEU   S  74  ? 1.7309 0.6381 2.0845 0.1056  -0.3185 -0.1298 73  LEU   S CA  
32692 C  C   . LEU   S  74  ? 1.7732 0.6323 2.1220 0.1379  -0.3110 -0.1095 73  LEU   S C   
32693 O  O   . LEU   S  74  ? 1.8152 0.6264 2.1990 0.2075  -0.2781 -0.1686 73  LEU   S O   
32694 C  CB  . LEU   S  74  ? 1.7288 0.6939 2.0460 0.0874  -0.3125 -0.1187 73  LEU   S CB  
32695 C  CG  . LEU   S  74  ? 1.7616 0.7350 2.0396 0.0464  -0.3097 -0.1421 73  LEU   S CG  
32696 C  CD1 . LEU   S  74  ? 1.8214 0.7735 2.0161 0.0302  -0.3059 -0.1628 73  LEU   S CD1 
32697 C  CD2 . LEU   S  74  ? 1.7447 0.7312 2.0264 0.0666  -0.2840 -0.1495 73  LEU   S CD2 
32698 N  N   . ALA   S  75  ? 1.8064 0.4810 2.0573 0.2033  -0.3445 -0.0774 74  ALA   S N   
32699 C  CA  . ALA   S  75  ? 1.8185 0.4559 2.0594 0.1628  -0.3201 -0.0489 74  ALA   S CA  
32700 C  C   . ALA   S  75  ? 1.8185 0.3718 1.9674 0.1840  -0.3313 -0.0289 74  ALA   S C   
32701 O  O   . ALA   S  75  ? 1.8378 0.3300 1.9825 0.2166  -0.3143 -0.0699 74  ALA   S O   
32702 C  CB  . ALA   S  75  ? 1.8270 0.5545 2.0671 0.1750  -0.3617 -0.0484 74  ALA   S CB  
32703 N  N   . GLY   S  76  ? 1.8485 0.4231 1.9297 0.1786  -0.3186 0.0081  75  GLY   S N   
32704 C  CA  . GLY   S  76  ? 1.8674 0.5726 1.8824 0.1385  -0.3065 -0.0494 75  GLY   S CA  
32705 C  C   . GLY   S  76  ? 1.8459 0.5713 1.8296 0.1550  -0.2878 -0.0886 75  GLY   S C   
32706 O  O   . GLY   S  76  ? 1.9220 0.5710 1.8439 0.0863  -0.2286 -0.1912 75  GLY   S O   
32707 N  N   . LEU   S  77  ? 1.8280 0.6675 1.8121 0.1365  -0.2415 -0.1398 76  LEU   S N   
32708 C  CA  . LEU   S  77  ? 1.7617 0.8361 1.7422 0.1305  -0.2609 -0.1474 76  LEU   S CA  
32709 C  C   . LEU   S  77  ? 1.7435 0.8338 1.7116 0.1341  -0.2420 -0.1266 76  LEU   S C   
32710 O  O   . LEU   S  77  ? 1.7222 0.8111 1.7563 0.1771  -0.2459 -0.1403 76  LEU   S O   
32711 C  CB  . LEU   S  77  ? 1.7533 0.9375 1.7251 0.0889  -0.2857 -0.1483 76  LEU   S CB  
32712 C  CG  . LEU   S  77  ? 1.7622 1.0455 1.7269 0.0517  -0.3088 -0.1696 76  LEU   S CG  
32713 C  CD1 . LEU   S  77  ? 1.7590 1.0907 1.6968 0.0286  -0.3251 -0.1603 76  LEU   S CD1 
32714 C  CD2 . LEU   S  77  ? 1.7370 1.1269 1.7293 0.0325  -0.2765 -0.1880 76  LEU   S CD2 
32715 N  N   . ALA   S  78  ? 1.7631 0.8924 1.6801 0.1634  -0.2425 -0.1124 77  ALA   S N   
32716 C  CA  . ALA   S  78  ? 1.7394 0.9039 1.6689 0.1689  -0.2155 -0.0764 77  ALA   S CA  
32717 C  C   . ALA   S  78  ? 1.7339 0.8686 1.6442 0.1454  -0.2112 -0.0223 77  ALA   S C   
32718 O  O   . ALA   S  78  ? 1.7382 0.7822 1.6642 0.1181  -0.2189 0.0554  77  ALA   S O   
32719 C  CB  . ALA   S  78  ? 1.7595 0.9739 1.6698 0.1722  -0.2037 -0.1012 77  ALA   S CB  
32720 N  N   . PRO   S  79  ? 1.7061 0.8878 1.6117 0.1782  -0.1864 0.0053  78  PRO   S N   
32721 C  CA  . PRO   S  79  ? 1.6969 0.8489 1.5993 0.1591  -0.1787 0.0050  78  PRO   S CA  
32722 C  C   . PRO   S  79  ? 1.6796 0.7775 1.6392 0.1872  -0.1525 -0.0001 78  PRO   S C   
32723 O  O   . PRO   S  79  ? 1.6541 0.8232 1.7170 0.2354  -0.1029 -0.0205 78  PRO   S O   
32724 C  CB  . PRO   S  79  ? 1.6801 0.9170 1.5572 0.1785  -0.1906 0.0375  78  PRO   S CB  
32725 C  CG  . PRO   S  79  ? 1.7266 0.9421 1.5882 0.1874  -0.1715 0.0198  78  PRO   S CG  
32726 C  CD  . PRO   S  79  ? 1.7389 0.9327 1.5917 0.1941  -0.1883 -0.0113 78  PRO   S CD  
32727 N  N   . ASP   S  80  ? 1.6965 0.7388 1.6796 0.2007  -0.1686 -0.0037 79  ASP   S N   
32728 C  CA  . ASP   S  80  ? 1.6238 0.6994 1.6676 0.2173  -0.2111 -0.0395 79  ASP   S CA  
32729 C  C   . ASP   S  80  ? 1.6117 0.5273 1.6343 0.2802  -0.2142 -0.0251 79  ASP   S C   
32730 O  O   . ASP   S  80  ? 1.6056 0.3906 1.5997 0.3292  -0.2795 0.0360  79  ASP   S O   
32731 C  CB  . ASP   S  80  ? 1.5918 0.7446 1.7136 0.1656  -0.1956 -0.0157 79  ASP   S CB  
32732 C  CG  . ASP   S  80  ? 1.5729 0.7720 1.7301 0.1462  -0.1753 -0.0147 79  ASP   S CG  
32733 O  OD1 . ASP   S  80  ? 1.4517 0.9056 1.7198 0.1358  -0.1947 -0.0387 79  ASP   S OD1 
32734 O  OD2 . ASP   S  80  ? 1.5224 0.7589 1.7465 0.1470  -0.1847 -0.0238 79  ASP   S OD2 
32735 N  N   . ALA   S  81  ? 1.6040 0.5558 1.6463 0.2610  -0.2176 -0.0580 80  ALA   S N   
32736 C  CA  . ALA   S  81  ? 1.6206 0.6293 1.6546 0.2479  -0.2158 -0.0987 80  ALA   S CA  
32737 C  C   . ALA   S  81  ? 1.5980 0.6208 1.6127 0.2648  -0.2247 -0.1278 80  ALA   S C   
32738 O  O   . ALA   S  81  ? 1.5868 0.6685 1.5836 0.2769  -0.2401 -0.1344 80  ALA   S O   
32739 C  CB  . ALA   S  81  ? 1.6220 0.6691 1.6980 0.2434  -0.1999 -0.0937 80  ALA   S CB  
32740 N  N   . ARG   S  82  ? 1.6249 0.6742 1.5830 0.2372  -0.2264 -0.1804 81  ARG   S N   
32741 C  CA  . ARG   S  82  ? 1.6550 0.6464 1.5826 0.1829  -0.2023 -0.1980 81  ARG   S CA  
32742 C  C   . ARG   S  82  ? 1.6075 0.6790 1.6064 0.1894  -0.2066 -0.1625 81  ARG   S C   
32743 O  O   . ARG   S  82  ? 1.6070 0.7037 1.6278 0.2332  -0.2175 -0.2146 81  ARG   S O   
32744 C  CB  . ARG   S  82  ? 1.7098 0.7184 1.5756 0.1311  -0.1775 -0.2203 81  ARG   S CB  
32745 C  CG  . ARG   S  82  ? 1.7174 0.7538 1.5535 0.1424  -0.1737 -0.1979 81  ARG   S CG  
32746 C  CD  . ARG   S  82  ? 1.7533 0.8318 1.5560 0.1199  -0.1662 -0.2126 81  ARG   S CD  
32747 N  NE  . ARG   S  82  ? 1.7715 0.8400 1.5388 0.1106  -0.1751 -0.1962 81  ARG   S NE  
32748 C  CZ  . ARG   S  82  ? 1.8140 0.8449 1.5171 0.1098  -0.1569 -0.2198 81  ARG   S CZ  
32749 N  NH1 . ARG   S  82  ? 1.8360 0.8639 1.5059 0.1117  -0.1573 -0.2570 81  ARG   S NH1 
32750 N  NH2 . ARG   S  82  ? 1.7806 0.8948 1.5100 0.1388  -0.1552 -0.2300 81  ARG   S NH2 
32751 N  N   . VAL   S  83  ? 1.6138 0.4893 1.5867 0.2123  -0.2358 -0.1983 82  VAL   S N   
32752 C  CA  . VAL   S  83  ? 1.5898 0.4556 1.5597 0.2128  -0.2570 -0.1824 82  VAL   S CA  
32753 C  C   . VAL   S  83  ? 1.5809 0.5165 1.5548 0.2128  -0.2501 -0.1894 82  VAL   S C   
32754 O  O   . VAL   S  83  ? 1.5985 0.5751 1.5355 0.2283  -0.2368 -0.2451 82  VAL   S O   
32755 C  CB  . VAL   S  83  ? 1.5935 0.3989 1.5391 0.2356  -0.2715 -0.1810 82  VAL   S CB  
32756 C  CG1 . VAL   S  83  ? 1.5862 0.3647 1.5260 0.2484  -0.2779 -0.1555 82  VAL   S CG1 
32757 C  CG2 . VAL   S  83  ? 1.6134 0.4195 1.5392 0.2285  -0.2749 -0.1862 82  VAL   S CG2 
32758 N  N   . LEU   S  84  ? 1.5962 0.5212 1.5278 0.1985  -0.2624 -0.1877 83  LEU   S N   
32759 C  CA  . LEU   S  84  ? 1.6145 0.6089 1.5252 0.1872  -0.2510 -0.2066 83  LEU   S CA  
32760 C  C   . LEU   S  84  ? 1.6091 0.5454 1.5180 0.2166  -0.2559 -0.1904 83  LEU   S C   
32761 O  O   . LEU   S  84  ? 1.5440 0.4559 1.5308 0.2133  -0.2739 -0.1745 83  LEU   S O   
32762 C  CB  . LEU   S  84  ? 1.6536 0.6151 1.5431 0.1977  -0.2544 -0.2154 83  LEU   S CB  
32763 C  CG  . LEU   S  84  ? 1.6826 0.6601 1.5552 0.1675  -0.2392 -0.2392 83  LEU   S CG  
32764 C  CD1 . LEU   S  84  ? 1.7209 0.6664 1.5646 0.1911  -0.2294 -0.2395 83  LEU   S CD1 
32765 C  CD2 . LEU   S  84  ? 1.6862 0.7107 1.5502 0.1596  -0.2387 -0.2475 83  LEU   S CD2 
32766 N  N   . SER   S  85  ? 1.6470 0.6237 1.5225 0.2200  -0.2365 -0.1907 84  SER   S N   
32767 C  CA  . SER   S  85  ? 1.6532 0.6819 1.5227 0.1980  -0.2179 -0.2162 84  SER   S CA  
32768 C  C   . SER   S  85  ? 1.6615 0.6672 1.5315 0.1916  -0.2213 -0.2416 84  SER   S C   
32769 O  O   . SER   S  85  ? 1.6682 0.6432 1.5596 0.1843  -0.1927 -0.2504 84  SER   S O   
32770 C  CB  . SER   S  85  ? 1.7049 0.7715 1.5126 0.1931  -0.1898 -0.2253 84  SER   S CB  
32771 O  OG  . SER   S  85  ? 1.7122 0.8924 1.4865 0.1692  -0.1559 -0.2369 84  SER   S OG  
32772 N  N   . ASN   S  86  ? 1.6704 0.6716 1.5512 0.2001  -0.2322 -0.2355 85  ASN   S N   
32773 C  CA  . ASN   S  86  ? 1.6991 0.6645 1.5268 0.2009  -0.2300 -0.2421 85  ASN   S CA  
32774 C  C   . ASN   S  86  ? 1.7107 0.6293 1.5154 0.1835  -0.2334 -0.2526 85  ASN   S C   
32775 O  O   . ASN   S  86  ? 1.7433 0.6163 1.5232 0.2338  -0.2173 -0.2173 85  ASN   S O   
32776 C  CB  . ASN   S  86  ? 1.7243 0.6798 1.5337 0.1977  -0.2466 -0.2304 85  ASN   S CB  
32777 C  CG  . ASN   S  86  ? 1.7156 0.6794 1.5328 0.2317  -0.2498 -0.2677 85  ASN   S CG  
32778 O  OD1 . ASN   S  86  ? 1.6816 0.6378 1.5672 0.1962  -0.2596 -0.2986 85  ASN   S OD1 
32779 N  ND2 . ASN   S  86  ? 1.7613 0.6772 1.5055 0.2323  -0.2386 -0.2785 85  ASN   S ND2 
32780 N  N   . TYR   S  87  ? 1.6783 0.6374 1.4902 0.1763  -0.2016 -0.2945 86  TYR   S N   
32781 C  CA  . TYR   S  87  ? 1.6526 0.6252 1.5251 0.2068  -0.1863 -0.2982 86  TYR   S CA  
32782 C  C   . TYR   S  87  ? 1.6290 0.6121 1.5271 0.2371  -0.1833 -0.3076 86  TYR   S C   
32783 O  O   . TYR   S  87  ? 1.6362 0.6634 1.4598 0.2325  -0.1860 -0.3304 86  TYR   S O   
32784 C  CB  . TYR   S  87  ? 1.6538 0.6479 1.5192 0.2078  -0.1462 -0.3023 86  TYR   S CB  
32785 C  CG  . TYR   S  87  ? 1.6389 0.6238 1.5580 0.2589  -0.1179 -0.2997 86  TYR   S CG  
32786 C  CD1 . TYR   S  87  ? 1.6553 0.5817 1.5314 0.2637  -0.1088 -0.2883 86  TYR   S CD1 
32787 C  CD2 . TYR   S  87  ? 1.6710 0.6664 1.5483 0.2572  -0.1044 -0.2891 86  TYR   S CD2 
32788 C  CE1 . TYR   S  87  ? 1.6140 0.5527 1.5644 0.2734  -0.0912 -0.2985 86  TYR   S CE1 
32789 C  CE2 . TYR   S  87  ? 1.6209 0.6142 1.5730 0.2771  -0.1081 -0.3247 86  TYR   S CE2 
32790 C  CZ  . TYR   S  87  ? 1.6047 0.5711 1.5070 0.2529  -0.0730 -0.3370 86  TYR   S CZ  
32791 O  OH  . TYR   S  87  ? 1.5218 0.6543 1.5662 0.2249  -0.0517 -0.4226 86  TYR   S OH  
32792 N  N   . LEU   S  88  ? 1.6492 0.6472 1.5570 0.2595  -0.2130 -0.2868 87  LEU   S N   
32793 C  CA  . LEU   S  88  ? 1.6654 0.6306 1.5151 0.2980  -0.2276 -0.2818 87  LEU   S CA  
32794 C  C   . LEU   S  88  ? 1.6203 0.6616 1.4770 0.3033  -0.2183 -0.2384 87  LEU   S C   
32795 O  O   . LEU   S  88  ? 1.6014 0.7275 1.4385 0.2835  -0.2646 -0.2168 87  LEU   S O   
32796 C  CB  . LEU   S  88  ? 1.6801 0.6572 1.5772 0.3153  -0.2551 -0.2638 87  LEU   S CB  
32797 C  CG  . LEU   S  88  ? 1.7246 0.7063 1.5654 0.3096  -0.2677 -0.2660 87  LEU   S CG  
32798 C  CD1 . LEU   S  88  ? 1.7020 0.8328 1.6217 0.3408  -0.2619 -0.2595 87  LEU   S CD1 
32799 C  CD2 . LEU   S  88  ? 1.7038 0.6162 1.5956 0.3164  -0.2635 -0.2555 87  LEU   S CD2 
32800 N  N   . ARG   S  89  ? 1.5928 0.6041 1.4892 0.2797  -0.2194 -0.2107 88  ARG   S N   
32801 C  CA  . ARG   S  89  ? 1.5776 0.6372 1.4854 0.2738  -0.2341 -0.1643 88  ARG   S CA  
32802 C  C   . ARG   S  89  ? 1.5665 0.6131 1.4639 0.2729  -0.2497 -0.1342 88  ARG   S C   
32803 O  O   . ARG   S  89  ? 1.6344 0.5274 1.4895 0.3220  -0.2651 -0.1099 88  ARG   S O   
32804 C  CB  . ARG   S  89  ? 1.5678 0.6439 1.4870 0.2637  -0.2315 -0.1130 88  ARG   S CB  
32805 C  CG  . ARG   S  89  ? 1.5665 0.6268 1.5249 0.2581  -0.2154 -0.0935 88  ARG   S CG  
32806 C  CD  . ARG   S  89  ? 1.5796 0.6101 1.5231 0.2572  -0.1906 -0.0739 88  ARG   S CD  
32807 N  NE  . ARG   S  89  ? 1.5779 0.5731 1.5598 0.2569  -0.1894 -0.0674 88  ARG   S NE  
32808 C  CZ  . ARG   S  89  ? 1.6154 0.5632 1.5649 0.2227  -0.1836 -0.0783 88  ARG   S CZ  
32809 N  NH1 . ARG   S  89  ? 1.6368 0.5139 1.5521 0.1786  -0.1950 -0.0910 88  ARG   S NH1 
32810 N  NH2 . ARG   S  89  ? 1.6206 0.5717 1.5918 0.2367  -0.1833 -0.0745 88  ARG   S NH2 
32811 N  N   . GLN   S  90  ? 1.5726 0.5814 1.4550 0.2401  -0.2709 -0.1319 89  GLN   S N   
32812 C  CA  . GLN   S  90  ? 1.5381 0.5758 1.5209 0.2314  -0.2809 -0.1256 89  GLN   S CA  
32813 C  C   . GLN   S  90  ? 1.5221 0.6173 1.5142 0.2576  -0.3083 -0.0789 89  GLN   S C   
32814 O  O   . GLN   S  90  ? 1.5328 0.6210 1.5089 0.2846  -0.3175 -0.0702 89  GLN   S O   
32815 C  CB  . GLN   S  90  ? 1.5577 0.5992 1.5083 0.1948  -0.2714 -0.1553 89  GLN   S CB  
32816 C  CG  . GLN   S  90  ? 1.5654 0.6919 1.5009 0.1710  -0.2586 -0.1657 89  GLN   S CG  
32817 C  CD  . GLN   S  90  ? 1.5645 0.7899 1.5518 0.1323  -0.2547 -0.1484 89  GLN   S CD  
32818 O  OE1 . GLN   S  90  ? 1.5891 0.8874 1.5862 0.1214  -0.2299 -0.1142 89  GLN   S OE1 
32819 N  NE2 . GLN   S  90  ? 1.6146 0.8818 1.5503 0.1132  -0.2520 -0.1453 89  GLN   S NE2 
32820 N  N   . GLN   S  91  ? 1.4979 0.5870 1.5493 0.2538  -0.3247 -0.0925 90  GLN   S N   
32821 C  CA  . GLN   S  91  ? 1.4741 0.5997 1.5512 0.2401  -0.3386 -0.1109 90  GLN   S CA  
32822 C  C   . GLN   S  91  ? 1.4964 0.6411 1.6049 0.1910  -0.3254 -0.1259 90  GLN   S C   
32823 O  O   . GLN   S  91  ? 1.4787 0.6623 1.5995 0.1406  -0.3433 -0.1452 90  GLN   S O   
32824 C  CB  . GLN   S  91  ? 1.4691 0.6118 1.5357 0.3123  -0.3696 -0.0820 90  GLN   S CB  
32825 C  CG  . GLN   S  91  ? 1.4344 0.6277 1.5227 0.3558  -0.4018 -0.0480 90  GLN   S CG  
32826 C  CD  . GLN   S  91  ? 1.4421 0.6100 1.4963 0.3701  -0.4313 -0.0451 90  GLN   S CD  
32827 O  OE1 . GLN   S  91  ? 1.4377 0.5238 1.4537 0.4131  -0.4830 0.0191  90  GLN   S OE1 
32828 N  NE2 . GLN   S  91  ? 1.4192 0.6866 1.5418 0.3822  -0.4377 -0.0515 90  GLN   S NE2 
32829 N  N   . CYS   S  92  ? 1.4633 0.6078 1.6403 0.1354  -0.3320 -0.1690 91  CYS   S N   
32830 C  CA  . CYS   S  92  ? 1.4745 0.6641 1.6993 0.1019  -0.3156 -0.1785 91  CYS   S CA  
32831 C  C   . CYS   S  92  ? 1.4917 0.6320 1.6831 0.0485  -0.3162 -0.2292 91  CYS   S C   
32832 O  O   . CYS   S  92  ? 1.5333 0.5609 1.7736 0.0311  -0.2604 -0.2702 91  CYS   S O   
32833 C  CB  . CYS   S  92  ? 1.4739 0.7172 1.7583 0.0751  -0.2937 -0.2229 91  CYS   S CB  
32834 S  SG  . CYS   S  92  ? 1.4540 0.7214 1.8645 0.0739  -0.2686 -0.2102 91  CYS   S SG  
32835 N  N   . ASN   S  93  ? 1.5074 0.6492 1.6901 0.0425  -0.2999 -0.1565 92  ASN   S N   
32836 C  CA  . ASN   S  93  ? 1.5069 0.6312 1.6836 0.0059  -0.2700 -0.1595 92  ASN   S CA  
32837 C  C   . ASN   S  93  ? 1.4910 0.6409 1.6613 0.0225  -0.2776 -0.1384 92  ASN   S C   
32838 O  O   . ASN   S  93  ? 1.3940 0.7146 1.6581 -0.0254 -0.2701 -0.1986 92  ASN   S O   
32839 C  CB  . ASN   S  93  ? 1.5433 0.6368 1.6770 -0.0326 -0.2597 -0.1187 92  ASN   S CB  
32840 C  CG  . ASN   S  93  ? 1.5903 0.6886 1.6920 -0.0371 -0.2564 -0.0686 92  ASN   S CG  
32841 O  OD1 . ASN   S  93  ? 1.5473 0.6771 1.7052 -0.0751 -0.2413 -0.0180 92  ASN   S OD1 
32842 N  ND2 . ASN   S  93  ? 1.5963 0.8246 1.7085 -0.0691 -0.2798 -0.0607 92  ASN   S ND2 
32843 N  N   . TYR   S  94  ? 1.5030 0.5390 1.6133 0.0634  -0.2551 -0.1174 93  TYR   S N   
32844 C  CA  . TYR   S  94  ? 1.5475 0.5153 1.5890 0.0951  -0.2363 -0.0672 93  TYR   S CA  
32845 C  C   . TYR   S  94  ? 1.4985 0.6073 1.5743 0.1135  -0.2573 -0.0166 93  TYR   S C   
32846 O  O   . TYR   S  94  ? 1.4896 0.6978 1.5808 0.1844  -0.2668 -0.0865 93  TYR   S O   
32847 C  CB  . TYR   S  94  ? 1.5937 0.4840 1.5513 0.0986  -0.2207 -0.0422 93  TYR   S CB  
32848 C  CG  . TYR   S  94  ? 1.6607 0.4381 1.5685 0.1407  -0.2047 -0.0402 93  TYR   S CG  
32849 C  CD1 . TYR   S  94  ? 1.6911 0.4348 1.5536 0.1504  -0.1996 -0.0268 93  TYR   S CD1 
32850 C  CD2 . TYR   S  94  ? 1.7040 0.4608 1.5677 0.1723  -0.2007 -0.0614 93  TYR   S CD2 
32851 C  CE1 . TYR   S  94  ? 1.7421 0.4688 1.5766 0.1552  -0.1631 -0.0339 93  TYR   S CE1 
32852 C  CE2 . TYR   S  94  ? 1.7261 0.4752 1.5883 0.1871  -0.1797 -0.0424 93  TYR   S CE2 
32853 C  CZ  . TYR   S  94  ? 1.7554 0.4539 1.5902 0.1864  -0.1680 0.0002  93  TYR   S CZ  
32854 O  OH  . TYR   S  94  ? 1.8289 0.4057 1.6661 0.2128  -0.1058 0.0171  93  TYR   S OH  
32855 N  N   . SER   S  95  ? 1.4670 0.6067 1.5960 0.1265  -0.2361 -0.0250 94  SER   S N   
32856 C  CA  . SER   S  95  ? 1.4855 0.6497 1.6080 0.1111  -0.2314 -0.0702 94  SER   S CA  
32857 C  C   . SER   S  95  ? 1.4799 0.6143 1.6231 0.1353  -0.2421 -0.0915 94  SER   S C   
32858 O  O   . SER   S  95  ? 1.4963 0.6547 1.6241 0.1650  -0.2519 -0.1018 94  SER   S O   
32859 C  CB  . SER   S  95  ? 1.4778 0.6851 1.6391 0.1211  -0.2382 -0.0572 94  SER   S CB  
32860 O  OG  . SER   S  95  ? 1.4584 0.7222 1.6605 0.0821  -0.2416 -0.0987 94  SER   S OG  
32861 N  N   . SER   S  96  ? 1.4983 0.6224 1.5803 0.1387  -0.2540 -0.1754 95  SER   S N   
32862 C  CA  . SER   S  96  ? 1.5043 0.6574 1.5735 0.0916  -0.2618 -0.2235 95  SER   S CA  
32863 C  C   . SER   S  96  ? 1.5691 0.5926 1.6018 0.0510  -0.2647 -0.2104 95  SER   S C   
32864 O  O   . SER   S  96  ? 1.5705 0.6300 1.6794 -0.0374 -0.2845 -0.1986 95  SER   S O   
32865 C  CB  . SER   S  96  ? 1.4564 0.6875 1.5823 0.0669  -0.2630 -0.2252 95  SER   S CB  
32866 O  OG  . SER   S  96  ? 1.4285 0.7722 1.6017 0.0850  -0.2665 -0.1819 95  SER   S OG  
32867 N  N   . LEU   S  97  ? 1.6355 0.5724 1.5651 0.0725  -0.2886 -0.2239 96  LEU   S N   
32868 C  CA  . LEU   S  97  ? 1.6703 0.6023 1.5788 0.1155  -0.2462 -0.2294 96  LEU   S CA  
32869 C  C   . LEU   S  97  ? 1.6286 0.6529 1.5467 0.1292  -0.2178 -0.1349 96  LEU   S C   
32870 O  O   . LEU   S  97  ? 1.6940 0.7301 1.6047 0.1094  -0.1939 -0.2818 96  LEU   S O   
32871 C  CB  . LEU   S  97  ? 1.7390 0.6729 1.5712 0.0537  -0.2364 -0.2908 96  LEU   S CB  
32872 C  CG  . LEU   S  97  ? 1.7819 0.7315 1.5903 0.0287  -0.2038 -0.3001 96  LEU   S CG  
32873 C  CD1 . LEU   S  97  ? 1.7831 0.7496 1.6092 0.0294  -0.2121 -0.2985 96  LEU   S CD1 
32874 C  CD2 . LEU   S  97  ? 1.7831 0.7761 1.5758 -0.0279 -0.2125 -0.3537 96  LEU   S CD2 
32875 N  N   . VAL   S  98  ? 1.5903 0.4476 1.4730 0.2089  -0.2664 -0.1561 97  VAL   S N   
32876 C  CA  . VAL   S  98  ? 1.6034 0.4126 1.4455 0.1735  -0.2491 -0.1289 97  VAL   S CA  
32877 C  C   . VAL   S  98  ? 1.5662 0.4356 1.4505 0.1839  -0.2420 -0.1402 97  VAL   S C   
32878 O  O   . VAL   S  98  ? 1.5651 0.5039 1.4385 0.2231  -0.2319 -0.1590 97  VAL   S O   
32879 C  CB  . VAL   S  98  ? 1.6275 0.4036 1.4506 0.1730  -0.2229 -0.1403 97  VAL   S CB  
32880 C  CG1 . VAL   S  98  ? 1.6465 0.4201 1.4437 0.1574  -0.2104 -0.1397 97  VAL   S CG1 
32881 C  CG2 . VAL   S  98  ? 1.6614 0.3996 1.4427 0.1889  -0.2245 -0.1311 97  VAL   S CG2 
32882 N  N   . PHE   S  99  ? 1.5064 0.4542 1.4047 0.1604  -0.2577 -0.1837 98  PHE   S N   
32883 C  CA  . PHE   S  99  ? 1.5081 0.4793 1.3872 0.1140  -0.2490 -0.1961 98  PHE   S CA  
32884 C  C   . PHE   S  99  ? 1.5021 0.5116 1.3988 0.1092  -0.2794 -0.1862 98  PHE   S C   
32885 O  O   . PHE   S  99  ? 1.4741 0.4943 1.3765 0.1640  -0.2635 -0.1263 98  PHE   S O   
32886 C  CB  . PHE   S  99  ? 1.4895 0.4806 1.3157 0.1018  -0.2720 -0.2115 98  PHE   S CB  
32887 C  CG  . PHE   S  99  ? 1.5060 0.4791 1.3029 0.0811  -0.2604 -0.2191 98  PHE   S CG  
32888 C  CD1 . PHE   S  99  ? 1.5267 0.4569 1.2962 0.0618  -0.2657 -0.2301 98  PHE   S CD1 
32889 C  CD2 . PHE   S  99  ? 1.5199 0.5001 1.3291 0.0600  -0.2511 -0.2336 98  PHE   S CD2 
32890 C  CE1 . PHE   S  99  ? 1.5382 0.4512 1.3092 0.0445  -0.2592 -0.2207 98  PHE   S CE1 
32891 C  CE2 . PHE   S  99  ? 1.5370 0.5236 1.3353 0.0514  -0.2271 -0.2289 98  PHE   S CE2 
32892 C  CZ  . PHE   S  99  ? 1.5325 0.4842 1.3058 0.0389  -0.2558 -0.2304 98  PHE   S CZ  
32893 N  N   . ASN   S  100 ? 1.5038 0.5815 1.4313 0.0469  -0.2607 -0.1852 99  ASN   S N   
32894 C  CA  . ASN   S  100 ? 1.4959 0.7103 1.5240 0.0253  -0.3051 -0.1884 99  ASN   S CA  
32895 C  C   . ASN   S  100 ? 1.5158 0.7276 1.5524 0.0229  -0.3270 -0.1742 99  ASN   S C   
32896 O  O   . ASN   S  100 ? 1.5301 0.8567 1.6416 -0.0137 -0.3760 -0.1328 99  ASN   S O   
32897 C  CB  . ASN   S  100 ? 1.5114 0.7507 1.5584 -0.0011 -0.3081 -0.2350 99  ASN   S CB  
32898 C  CG  . ASN   S  100 ? 1.5432 0.7516 1.6142 -0.0706 -0.3189 -0.2564 99  ASN   S CG  
32899 O  OD1 . ASN   S  100 ? 1.7201 0.6979 1.5706 -0.0203 -0.2772 -0.3204 99  ASN   S OD1 
32900 N  ND2 . ASN   S  100 ? 1.5351 0.8587 1.6371 -0.0648 -0.2949 -0.2708 99  ASN   S ND2 
32901 N  N   . ARG   S  101 ? 1.5182 0.7379 1.5692 0.0158  -0.3091 -0.1993 100 ARG   S N   
32902 C  CA  . ARG   S  101 ? 1.5128 0.7460 1.5860 0.0550  -0.2799 -0.1972 100 ARG   S CA  
32903 C  C   . ARG   S  101 ? 1.4915 0.7455 1.5782 0.1061  -0.2893 -0.1774 100 ARG   S C   
32904 O  O   . ARG   S  101 ? 1.5019 0.7730 1.5723 0.1367  -0.2907 -0.1992 100 ARG   S O   
32905 C  CB  . ARG   S  101 ? 1.5553 0.6946 1.5970 0.0790  -0.2360 -0.2219 100 ARG   S CB  
32906 C  CG  . ARG   S  101 ? 1.5645 0.6595 1.6280 0.1128  -0.2173 -0.2390 100 ARG   S CG  
32907 C  CD  . ARG   S  101 ? 1.5900 0.6319 1.6791 0.1068  -0.1662 -0.3037 100 ARG   S CD  
32908 N  NE  . ARG   S  101 ? 1.5967 0.5756 1.6821 0.1093  -0.1513 -0.3316 100 ARG   S NE  
32909 C  CZ  . ARG   S  101 ? 1.5985 0.5158 1.7077 0.1129  -0.1327 -0.3367 100 ARG   S CZ  
32910 N  NH1 . ARG   S  101 ? 1.5989 0.5576 1.7595 0.1053  -0.0840 -0.3451 100 ARG   S NH1 
32911 N  NH2 . ARG   S  101 ? 1.5581 0.4173 1.7463 0.1255  -0.1365 -0.3527 100 ARG   S NH2 
32912 N  N   . LYS   S  102 ? 1.4494 0.8369 1.5489 0.0751  -0.3500 -0.1372 101 LYS   S N   
32913 C  CA  . LYS   S  102 ? 1.4377 0.8404 1.5446 0.0875  -0.3524 -0.1304 101 LYS   S CA  
32914 C  C   . LYS   S  102 ? 1.4876 0.7792 1.4764 0.1166  -0.3977 -0.1199 101 LYS   S C   
32915 O  O   . LYS   S  102 ? 1.5108 0.7196 1.4925 0.2065  -0.4275 -0.0963 101 LYS   S O   
32916 C  CB  . LYS   S  102 ? 1.4286 0.9239 1.6209 0.0807  -0.3573 -0.1302 101 LYS   S CB  
32917 C  CG  . LYS   S  102 ? 1.3992 1.0233 1.7058 0.0499  -0.3141 -0.1122 101 LYS   S CG  
32918 C  CD  . LYS   S  102 ? 1.3827 1.1321 1.7949 0.0454  -0.2861 -0.0788 101 LYS   S CD  
32919 C  CE  . LYS   S  102 ? 1.3813 1.2094 1.8658 0.0357  -0.2474 -0.0504 101 LYS   S CE  
32920 N  NZ  . LYS   S  102 ? 1.3806 1.2722 1.9236 0.0301  -0.2482 -0.0362 101 LYS   S NZ  
32921 N  N   . LEU   S  103 ? 1.5029 0.7503 1.5028 0.0677  -0.3692 -0.1167 102 LEU   S N   
32922 C  CA  . LEU   S  103 ? 1.5261 0.7371 1.5031 0.0665  -0.3916 -0.1042 102 LEU   S CA  
32923 C  C   . LEU   S  103 ? 1.5937 0.6883 1.5222 0.0715  -0.4022 -0.1162 102 LEU   S C   
32924 O  O   . LEU   S  103 ? 1.6775 0.6215 1.5359 0.0446  -0.3486 -0.1731 102 LEU   S O   
32925 C  CB  . LEU   S  103 ? 1.4842 0.7316 1.5112 0.0316  -0.3683 -0.1056 102 LEU   S CB  
32926 C  CG  . LEU   S  103 ? 1.4787 0.6957 1.5012 0.0413  -0.3837 -0.1083 102 LEU   S CG  
32927 C  CD1 . LEU   S  103 ? 1.4558 0.6647 1.4756 -0.0014 -0.3884 -0.1153 102 LEU   S CD1 
32928 C  CD2 . LEU   S  103 ? 1.4800 0.7155 1.4895 0.0366  -0.3537 -0.1193 102 LEU   S CD2 
32929 N  N   . ALA   S  104 ? 1.6398 0.6692 1.5130 0.0743  -0.4478 -0.0988 103 ALA   S N   
32930 C  CA  . ALA   S  104 ? 1.6684 0.6776 1.5235 0.1104  -0.4362 -0.0970 103 ALA   S CA  
32931 C  C   . ALA   S  104 ? 1.6668 0.5987 1.5537 0.1849  -0.4383 -0.0508 103 ALA   S C   
32932 O  O   . ALA   S  104 ? 1.5997 0.5144 1.5512 0.2783  -0.4369 0.0084  103 ALA   S O   
32933 C  CB  . ALA   S  104 ? 1.6772 0.6977 1.5096 0.1021  -0.4557 -0.0574 103 ALA   S CB  
32934 N  N   . VAL   S  105 ? 1.7088 0.5992 1.5888 0.1793  -0.3858 -0.0950 104 VAL   S N   
32935 C  CA  . VAL   S  105 ? 1.7262 0.5867 1.6293 0.1725  -0.3692 -0.1043 104 VAL   S CA  
32936 C  C   . VAL   S  105 ? 1.7767 0.5031 1.6664 0.1390  -0.3706 -0.1603 104 VAL   S C   
32937 O  O   . VAL   S  105 ? 1.7485 0.4120 1.7124 0.1277  -0.3258 -0.1416 104 VAL   S O   
32938 C  CB  . VAL   S  105 ? 1.7481 0.5250 1.6419 0.2066  -0.3981 -0.0842 104 VAL   S CB  
32939 C  CG1 . VAL   S  105 ? 1.7374 0.5083 1.6647 0.2205  -0.4097 -0.0711 104 VAL   S CG1 
32940 C  CG2 . VAL   S  105 ? 1.7299 0.4925 1.6584 0.2095  -0.3966 -0.1082 104 VAL   S CG2 
32941 N  N   . GLU   S  106 ? 1.8313 0.5407 1.6769 0.0959  -0.3613 -0.1890 105 GLU   S N   
32942 C  CA  . GLU   S  106 ? 1.8333 0.5600 1.7362 0.0700  -0.3723 -0.1714 105 GLU   S CA  
32943 C  C   . GLU   S  106 ? 1.8344 0.6599 1.7204 0.1030  -0.3641 -0.1490 105 GLU   S C   
32944 O  O   . GLU   S  106 ? 1.8474 0.5610 1.7771 0.1589  -0.3457 -0.1373 105 GLU   S O   
32945 C  CB  . GLU   S  106 ? 1.9617 0.6742 1.7498 0.0211  -0.3678 -0.2141 105 GLU   S CB  
32946 C  CG  . GLU   S  106 ? 2.0558 0.7143 1.8176 -0.0566 -0.3366 -0.2248 105 GLU   S CG  
32947 C  CD  . GLU   S  106 ? 2.1751 0.8832 1.8484 -0.1230 -0.3886 -0.2814 105 GLU   S CD  
32948 O  OE1 . GLU   S  106 ? 2.2528 1.0194 1.9252 -0.1618 -0.3284 -0.2411 105 GLU   S OE1 
32949 O  OE2 . GLU   S  106 ? 2.2159 0.9594 1.9897 -0.2246 -0.4129 -0.3271 105 GLU   S OE2 
32950 N  N   . ARG   S  107 ? 1.7260 0.6866 1.7105 0.1175  -0.3844 -0.1016 106 ARG   S N   
32951 C  CA  . ARG   S  107 ? 1.7242 0.7326 1.6716 0.1336  -0.3586 -0.0608 106 ARG   S CA  
32952 C  C   . ARG   S  107 ? 1.6416 0.6155 1.6515 0.1415  -0.3490 -0.0113 106 ARG   S C   
32953 O  O   . ARG   S  107 ? 1.6366 0.5959 1.6277 0.1124  -0.3497 0.0775  106 ARG   S O   
32954 C  CB  . ARG   S  107 ? 1.6916 0.7623 1.6417 0.1690  -0.3426 -0.1323 106 ARG   S CB  
32955 C  CG  . ARG   S  107 ? 1.6844 0.9449 1.6104 0.1588  -0.3609 -0.1437 106 ARG   S CG  
32956 C  CD  . ARG   S  107 ? 1.6614 0.9864 1.6080 0.1795  -0.3549 -0.1739 106 ARG   S CD  
32957 N  NE  . ARG   S  107 ? 1.6776 1.0997 1.5508 0.1289  -0.3761 -0.1876 106 ARG   S NE  
32958 C  CZ  . ARG   S  107 ? 1.6544 1.1171 1.5802 0.1349  -0.3733 -0.1590 106 ARG   S CZ  
32959 N  NH1 . ARG   S  107 ? 1.6588 1.1547 1.5877 0.1508  -0.3847 -0.1180 106 ARG   S NH1 
32960 N  NH2 . ARG   S  107 ? 1.6508 1.0777 1.5647 0.1310  -0.3472 -0.1745 106 ARG   S NH2 
32961 N  N   . ALA   S  108 ? 1.6582 0.5785 1.6466 0.1973  -0.3297 -0.0360 107 ALA   S N   
32962 C  CA  . ALA   S  108 ? 1.6067 0.5552 1.6757 0.2148  -0.3211 -0.0902 107 ALA   S CA  
32963 C  C   . ALA   S  108 ? 1.6178 0.5285 1.6647 0.2566  -0.3128 -0.1213 107 ALA   S C   
32964 O  O   . ALA   S  108 ? 1.5772 0.4946 1.6932 0.2936  -0.3180 -0.0946 107 ALA   S O   
32965 C  CB  . ALA   S  108 ? 1.5983 0.5496 1.6707 0.2327  -0.3178 -0.1075 107 ALA   S CB  
32966 N  N   . GLY   S  109 ? 1.5844 0.6000 1.6151 0.2525  -0.3483 -0.1452 108 GLY   S N   
32967 C  CA  . GLY   S  109 ? 1.5903 0.6130 1.6612 0.2377  -0.3511 -0.1250 108 GLY   S CA  
32968 C  C   . GLY   S  109 ? 1.5903 0.6221 1.6581 0.2558  -0.3457 -0.1125 108 GLY   S C   
32969 O  O   . GLY   S  109 ? 1.5624 0.5551 1.7033 0.2879  -0.3467 -0.1096 108 GLY   S O   
32970 N  N   . HIS   S  110 ? 1.6057 0.6218 1.6445 0.2301  -0.3716 -0.1316 109 HIS   S N   
32971 C  CA  . HIS   S  110 ? 1.6311 0.6538 1.6420 0.2037  -0.3561 -0.1124 109 HIS   S CA  
32972 C  C   . HIS   S  110 ? 1.6535 0.6118 1.6352 0.1828  -0.3747 -0.1399 109 HIS   S C   
32973 O  O   . HIS   S  110 ? 1.6563 0.5125 1.6277 0.1964  -0.3596 -0.1427 109 HIS   S O   
32974 C  CB  . HIS   S  110 ? 1.6285 0.7108 1.6147 0.1673  -0.3623 -0.1175 109 HIS   S CB  
32975 C  CG  . HIS   S  110 ? 1.5993 0.7706 1.6358 0.1379  -0.3741 -0.1073 109 HIS   S CG  
32976 N  ND1 . HIS   S  110 ? 1.5999 0.7783 1.6263 0.1407  -0.3986 -0.1002 109 HIS   S ND1 
32977 C  CD2 . HIS   S  110 ? 1.5747 0.8721 1.6254 0.1117  -0.3793 -0.0903 109 HIS   S CD2 
32978 C  CE1 . HIS   S  110 ? 1.6085 0.7987 1.6200 0.1206  -0.3983 -0.0802 109 HIS   S CE1 
32979 N  NE2 . HIS   S  110 ? 1.5671 0.8357 1.6368 0.1024  -0.3881 -0.0983 109 HIS   S NE2 
32980 N  N   . LEU   S  111 ? 1.7253 0.6443 1.6393 0.1658  -0.3790 -0.1219 110 LEU   S N   
32981 C  CA  . LEU   S  111 ? 1.7259 0.6748 1.6469 0.1102  -0.4041 -0.1130 110 LEU   S CA  
32982 C  C   . LEU   S  111 ? 1.6767 0.7605 1.6185 0.0806  -0.4325 -0.1297 110 LEU   S C   
32983 O  O   . LEU   S  111 ? 1.6644 0.9812 1.6948 -0.0128 -0.4184 -0.1158 110 LEU   S O   
32984 C  CB  . LEU   S  111 ? 1.7617 0.5772 1.7013 0.1433  -0.4054 -0.1656 110 LEU   S CB  
32985 C  CG  . LEU   S  111 ? 1.7077 0.4921 1.7297 0.1481  -0.4222 -0.1285 110 LEU   S CG  
32986 C  CD1 . LEU   S  111 ? 1.6954 0.5007 1.7477 0.1276  -0.4302 -0.1638 110 LEU   S CD1 
32987 C  CD2 . LEU   S  111 ? 1.6997 0.4322 1.6887 0.1376  -0.4045 -0.1702 110 LEU   S CD2 
32988 N  N   . LEU   S  112 ? 1.6627 0.7749 1.5623 0.1016  -0.4609 -0.0967 111 LEU   S N   
32989 C  CA  . LEU   S  112 ? 1.6431 0.7826 1.5327 0.0980  -0.4417 -0.0871 111 LEU   S CA  
32990 C  C   . LEU   S  112 ? 1.6909 0.7430 1.5369 0.0794  -0.4791 -0.0956 111 LEU   S C   
32991 O  O   . LEU   S  112 ? 1.7336 0.6592 1.5432 0.0076  -0.4687 -0.0528 111 LEU   S O   
32992 C  CB  . LEU   S  112 ? 1.6498 0.8545 1.5351 0.1445  -0.4593 -0.0915 111 LEU   S CB  
32993 C  CG  . LEU   S  112 ? 1.6441 0.8872 1.5320 0.1366  -0.4430 -0.1037 111 LEU   S CG  
32994 C  CD1 . LEU   S  112 ? 1.6614 0.8710 1.5596 0.1560  -0.4428 -0.1152 111 LEU   S CD1 
32995 C  CD2 . LEU   S  112 ? 1.6531 0.9435 1.5189 0.1296  -0.4391 -0.1270 111 LEU   S CD2 
32996 N  N   . CYS   S  113 ? 1.6806 0.6970 1.5441 0.0845  -0.4543 -0.0837 112 CYS   S N   
32997 C  CA  . CYS   S  113 ? 1.6773 0.6667 1.5991 0.0756  -0.4396 -0.1139 112 CYS   S CA  
32998 C  C   . CYS   S  113 ? 1.6888 0.6279 1.5595 0.1046  -0.4483 -0.1368 112 CYS   S C   
32999 O  O   . CYS   S  113 ? 1.7002 0.6575 1.6209 0.1126  -0.4706 -0.1786 112 CYS   S O   
33000 C  CB  . CYS   S  113 ? 1.6748 0.6839 1.5998 0.0809  -0.4247 -0.0681 112 CYS   S CB  
33001 S  SG  . CYS   S  113 ? 1.7625 0.6266 1.6413 0.0568  -0.4391 -0.0298 112 CYS   S SG  
33002 N  N   . ASP   S  114 ? 1.6795 0.5676 1.5276 0.0749  -0.4481 -0.0781 113 ASP   S N   
33003 C  CA  . ASP   S  114 ? 1.7017 0.4980 1.5435 0.0924  -0.4165 -0.0501 113 ASP   S CA  
33004 C  C   . ASP   S  114 ? 1.7489 0.4161 1.5302 0.0917  -0.4047 -0.0473 113 ASP   S C   
33005 O  O   . ASP   S  114 ? 1.7540 0.2832 1.5313 0.1089  -0.4348 0.0115  113 ASP   S O   
33006 C  CB  . ASP   S  114 ? 1.7261 0.5265 1.5603 0.0710  -0.3678 -0.0691 113 ASP   S CB  
33007 C  CG  . ASP   S  114 ? 1.7480 0.5703 1.5665 0.0503  -0.3776 -0.1153 113 ASP   S CG  
33008 O  OD1 . ASP   S  114 ? 1.7832 0.6090 1.6522 0.1940  -0.3392 -0.0796 113 ASP   S OD1 
33009 O  OD2 . ASP   S  114 ? 1.7669 0.4508 1.7125 -0.0617 -0.3347 -0.0359 113 ASP   S OD2 
33010 N  N   . LYS   S  115 ? 1.7045 0.5121 1.5779 0.0950  -0.3694 -0.0907 114 LYS   S N   
33011 C  CA  . LYS   S  115 ? 1.6698 0.6469 1.5848 0.1130  -0.3787 -0.0991 114 LYS   S CA  
33012 C  C   . LYS   S  115 ? 1.6607 0.6371 1.5787 0.1501  -0.4018 -0.0983 114 LYS   S C   
33013 O  O   . LYS   S  115 ? 1.6930 0.5351 1.5474 0.1802  -0.4125 -0.1503 114 LYS   S O   
33014 C  CB  . LYS   S  115 ? 1.6603 0.7489 1.5902 0.1036  -0.3501 -0.1001 114 LYS   S CB  
33015 C  CG  . LYS   S  115 ? 1.6401 0.8240 1.5834 0.0886  -0.3437 -0.0755 114 LYS   S CG  
33016 C  CD  . LYS   S  115 ? 1.6529 0.9283 1.6130 0.0762  -0.3208 -0.1012 114 LYS   S CD  
33017 C  CE  . LYS   S  115 ? 1.6540 0.9698 1.6205 0.0620  -0.3370 -0.0847 114 LYS   S CE  
33018 N  NZ  . LYS   S  115 ? 1.6637 0.9877 1.6291 0.0494  -0.3380 -0.1091 114 LYS   S NZ  
33019 N  N   . ALA   S  116 ? 1.6594 0.6970 1.6244 0.1771  -0.3865 -0.0801 115 ALA   S N   
33020 C  CA  . ALA   S  116 ? 1.6751 0.7068 1.6481 0.1492  -0.3666 -0.0828 115 ALA   S CA  
33021 C  C   . ALA   S  116 ? 1.6720 0.7317 1.6725 0.1600  -0.3426 -0.0623 115 ALA   S C   
33022 O  O   . ALA   S  116 ? 1.5914 0.6815 1.7043 0.0560  -0.3452 0.0829  115 ALA   S O   
33023 C  CB  . ALA   S  116 ? 1.6914 0.7633 1.6762 0.1713  -0.3841 -0.0767 115 ALA   S CB  
33024 N  N   . GLN   S  117 ? 1.6449 0.6918 1.7095 0.1895  -0.3286 -0.1352 116 GLN   S N   
33025 C  CA  . GLN   S  117 ? 1.7124 0.6730 1.6838 0.1993  -0.2916 -0.1543 116 GLN   S CA  
33026 C  C   . GLN   S  117 ? 1.7507 0.6708 1.7276 0.1943  -0.3289 -0.2093 116 GLN   S C   
33027 O  O   . GLN   S  117 ? 1.8792 0.6109 1.7978 0.1883  -0.3077 -0.2561 116 GLN   S O   
33028 C  CB  . GLN   S  117 ? 1.6631 0.7165 1.6470 0.2186  -0.3009 -0.1099 116 GLN   S CB  
33029 C  CG  . GLN   S  117 ? 1.7189 0.7243 1.6151 0.2161  -0.3091 -0.0886 116 GLN   S CG  
33030 C  CD  . GLN   S  117 ? 1.6988 0.7999 1.5723 0.1534  -0.2884 -0.0633 116 GLN   S CD  
33031 O  OE1 . GLN   S  117 ? 1.7749 0.6877 1.4987 0.1670  -0.2859 -0.1036 116 GLN   S OE1 
33032 N  NE2 . GLN   S  117 ? 1.7248 0.8438 1.5592 0.1964  -0.2719 -0.0077 116 GLN   S NE2 
33033 N  N   . LYS   S  118 ? 1.8829 0.6924 1.7583 0.2019  -0.3197 -0.1702 117 LYS   S N   
33034 C  CA  . LYS   S  118 ? 1.8931 0.6689 1.7588 0.1955  -0.3246 -0.1602 117 LYS   S CA  
33035 C  C   . LYS   S  118 ? 1.9421 0.5880 1.7356 0.1950  -0.3371 -0.1163 117 LYS   S C   
33036 O  O   . LYS   S  118 ? 1.9128 0.5001 1.7682 0.2618  -0.3706 -0.0868 117 LYS   S O   
33037 C  CB  . LYS   S  118 ? 1.8934 0.6587 1.8650 0.1243  -0.2604 -0.1428 117 LYS   S CB  
33038 C  CG  . LYS   S  118 ? 1.9310 0.7068 1.8891 0.1149  -0.2144 -0.1632 117 LYS   S CG  
33039 C  CD  . LYS   S  118 ? 1.9587 0.7291 1.9072 0.1060  -0.1766 -0.1414 117 LYS   S CD  
33040 C  CE  . LYS   S  118 ? 1.9965 0.7924 1.8960 0.1193  -0.1804 -0.1592 117 LYS   S CE  
33041 N  NZ  . LYS   S  118 ? 2.0057 0.8171 1.9444 0.1127  -0.1495 -0.1112 117 LYS   S NZ  
33042 N  N   . ASN   S  119 ? 2.0410 0.4615 1.6214 0.1615  -0.3173 -0.1338 118 ASN   S N   
33043 C  CA  . ASN   S  119 ? 2.1110 0.4798 1.5942 0.1220  -0.2829 -0.1257 118 ASN   S CA  
33044 C  C   . ASN   S  119 ? 2.2323 0.4856 1.5881 0.0874  -0.3081 -0.1273 118 ASN   S C   
33045 O  O   . ASN   S  119 ? 2.3124 0.2931 1.5837 0.0531  -0.2617 -0.0557 118 ASN   S O   
33046 C  CB  . ASN   S  119 ? 2.1173 0.4919 1.5556 0.1135  -0.2820 -0.1559 118 ASN   S CB  
33047 C  CG  . ASN   S  119 ? 2.1065 0.5347 1.5359 0.1303  -0.2849 -0.1313 118 ASN   S CG  
33048 O  OD1 . ASN   S  119 ? 2.1584 0.4317 1.5433 0.2012  -0.2574 -0.0732 118 ASN   S OD1 
33049 N  ND2 . ASN   S  119 ? 2.0949 0.5759 1.4632 0.1030  -0.2747 -0.1542 118 ASN   S ND2 
33050 N  N   . THR   S  120 ? 2.2172 0.4823 1.5937 0.0646  -0.3450 -0.1296 119 THR   S N   
33051 C  CA  . THR   S  120 ? 2.1319 0.4599 1.6654 -0.0040 -0.3296 -0.1685 119 THR   S CA  
33052 C  C   . THR   S  120 ? 2.0500 0.4941 1.7066 -0.0024 -0.3757 -0.1512 119 THR   S C   
33053 O  O   . THR   S  120 ? 2.0222 0.5574 1.7260 -0.0162 -0.3649 -0.0764 119 THR   S O   
33054 C  CB  . THR   S  120 ? 2.1585 0.3983 1.6387 -0.0034 -0.3392 -0.2114 119 THR   S CB  
33055 O  OG1 . THR   S  120 ? 2.1935 0.2985 1.5713 -0.0494 -0.3883 -0.1328 119 THR   S OG1 
33056 C  CG2 . THR   S  120 ? 2.1387 0.3989 1.6803 0.0122  -0.3282 -0.2790 119 THR   S CG2 
33057 N  N   . GLN   S  121 ? 1.9991 0.3891 1.7175 -0.0693 -0.3899 -0.1204 120 GLN   S N   
33058 C  CA  . GLN   S  121 ? 2.0393 0.3758 1.7054 -0.0534 -0.3796 -0.0712 120 GLN   S CA  
33059 C  C   . GLN   S  121 ? 2.1173 0.3123 1.7314 -0.0327 -0.4220 -0.0594 120 GLN   S C   
33060 O  O   . GLN   S  121 ? 2.1847 0.1448 1.6949 0.0051  -0.3778 0.0159  120 GLN   S O   
33061 C  CB  . GLN   S  121 ? 2.0212 0.4221 1.6692 -0.0455 -0.3734 -0.0601 120 GLN   S CB  
33062 C  CG  . GLN   S  121 ? 2.0501 0.3916 1.6417 -0.0452 -0.3876 -0.0171 120 GLN   S CG  
33063 C  CD  . GLN   S  121 ? 2.0283 0.4537 1.5732 -0.0309 -0.3752 0.0436  120 GLN   S CD  
33064 O  OE1 . GLN   S  121 ? 2.0796 0.4261 1.5671 -0.0516 -0.4012 0.1046  120 GLN   S OE1 
33065 N  NE2 . GLN   S  121 ? 1.9503 0.5670 1.5959 -0.0369 -0.4178 -0.0191 120 GLN   S NE2 
33066 N  N   . SER   S  122 ? 2.1229 0.3749 1.7337 -0.0472 -0.4073 -0.0553 121 SER   S N   
33067 C  CA  . SER   S  122 ? 2.1119 0.4638 1.7017 -0.0724 -0.4182 -0.0640 121 SER   S CA  
33068 C  C   . SER   S  122 ? 2.1114 0.5512 1.6739 0.0199  -0.4010 -0.0903 121 SER   S C   
33069 O  O   . SER   S  122 ? 2.1282 0.4341 1.6045 0.0832  -0.4500 -0.0987 121 SER   S O   
33070 C  CB  . SER   S  122 ? 2.0844 0.4945 1.6936 -0.1482 -0.3874 -0.0408 121 SER   S CB  
33071 O  OG  . SER   S  122 ? 2.0805 0.4103 1.7490 -0.1982 -0.3728 -0.0546 121 SER   S OG  
33072 N  N   . TYR   S  123 ? 2.1662 0.7564 1.7259 -0.0150 -0.4527 -0.1084 122 TYR   S N   
33073 C  CA  . TYR   S  123 ? 2.2394 0.9117 1.6955 -0.0653 -0.4540 -0.1165 122 TYR   S CA  
33074 C  C   . TYR   S  123 ? 2.1668 0.8445 1.7528 -0.0589 -0.4258 -0.1014 122 TYR   S C   
33075 O  O   . TYR   S  123 ? 2.2449 0.8486 1.7007 -0.0614 -0.3672 -0.1132 122 TYR   S O   
33076 C  CB  . TYR   S  123 ? 2.2651 1.2268 1.8068 -0.1133 -0.5346 -0.1529 122 TYR   S CB  
33077 C  CG  . TYR   S  123 ? 2.4275 1.5360 1.8246 -0.1201 -0.5778 -0.2077 122 TYR   S CG  
33078 C  CD1 . TYR   S  123 ? 2.4435 1.5723 1.7893 -0.1283 -0.6121 -0.2911 122 TYR   S CD1 
33079 C  CD2 . TYR   S  123 ? 2.4746 1.6672 1.8567 -0.1145 -0.6391 -0.1840 122 TYR   S CD2 
33080 C  CE1 . TYR   S  123 ? 2.4040 1.4897 1.8715 -0.1684 -0.5966 -0.3763 122 TYR   S CE1 
33081 C  CE2 . TYR   S  123 ? 2.4461 1.6539 1.9296 -0.1486 -0.6601 -0.2498 122 TYR   S CE2 
33082 C  CZ  . TYR   S  123 ? 2.3865 1.6810 1.8627 -0.2000 -0.6689 -0.3496 122 TYR   S CZ  
33083 O  OH  . TYR   S  123 ? 2.2611 1.7968 1.8303 -0.1201 -0.6883 -0.3219 122 TYR   S OH  
33084 N  N   . GLY   S  124 ? 2.0434 0.8089 1.7820 -0.0188 -0.3613 -0.0347 123 GLY   S N   
33085 C  CA  . GLY   S  124 ? 1.9420 0.8353 1.8198 -0.0337 -0.3127 -0.0345 123 GLY   S CA  
33086 C  C   . GLY   S  124 ? 1.9105 0.7727 1.7985 0.0024  -0.3485 -0.0672 123 GLY   S C   
33087 O  O   . GLY   S  124 ? 1.9233 0.9135 1.8944 -0.0001 -0.2324 -0.0104 123 GLY   S O   
33088 N  N   . GLY   S  125 ? 1.7505 0.6133 1.8447 0.0080  -0.3440 -0.0697 124 GLY   S N   
33089 C  CA  . GLY   S  125 ? 1.7465 0.6032 1.8438 0.0092  -0.3477 -0.0711 124 GLY   S CA  
33090 C  C   . GLY   S  125 ? 1.7509 0.5096 1.8856 -0.0529 -0.3481 -0.0383 124 GLY   S C   
33091 O  O   . GLY   S  125 ? 1.7340 0.6100 1.9354 -0.1448 -0.3552 -0.0159 124 GLY   S O   
33092 N  N   . ARG   S  126 ? 1.7395 0.4455 1.8673 0.0034  -0.3366 -0.0214 125 ARG   S N   
33093 C  CA  . ARG   S  126 ? 1.7855 0.4303 1.8135 0.0218  -0.3209 -0.0182 125 ARG   S CA  
33094 C  C   . ARG   S  126 ? 1.7513 0.4553 1.7959 0.0370  -0.3116 0.0143  125 ARG   S C   
33095 O  O   . ARG   S  126 ? 1.7206 0.4822 1.8379 -0.0227 -0.2902 0.0508  125 ARG   S O   
33096 C  CB  . ARG   S  126 ? 1.7961 0.4235 1.8036 0.0335  -0.3368 -0.0274 125 ARG   S CB  
33097 C  CG  . ARG   S  126 ? 1.7897 0.3216 1.8090 0.0555  -0.3736 -0.0416 125 ARG   S CG  
33098 C  CD  . ARG   S  126 ? 1.7789 0.3659 1.8078 0.0780  -0.4006 -0.0560 125 ARG   S CD  
33099 N  NE  . ARG   S  126 ? 1.7344 0.3722 1.7863 0.0810  -0.4151 -0.0660 125 ARG   S NE  
33100 C  CZ  . ARG   S  126 ? 1.6796 0.4520 1.8087 0.1187  -0.4311 -0.0558 125 ARG   S CZ  
33101 N  NH1 . ARG   S  126 ? 1.6864 0.4618 1.8315 0.1596  -0.4390 -0.0548 125 ARG   S NH1 
33102 N  NH2 . ARG   S  126 ? 1.6444 0.4845 1.8190 0.1152  -0.4445 -0.0314 125 ARG   S NH2 
33103 N  N   . PRO   S  127 ? 1.7533 0.5268 1.7574 0.0549  -0.2940 0.0430  126 PRO   S N   
33104 C  CA  . PRO   S  127 ? 1.7228 0.4959 1.7449 0.0696  -0.2761 0.0540  126 PRO   S CA  
33105 C  C   . PRO   S  127 ? 1.7496 0.4488 1.6781 0.1081  -0.2651 0.0333  126 PRO   S C   
33106 O  O   . PRO   S  127 ? 1.7496 0.3343 1.7020 0.0183  -0.2384 0.0074  126 PRO   S O   
33107 C  CB  . PRO   S  127 ? 1.7140 0.5127 1.7822 0.1149  -0.2932 0.0358  126 PRO   S CB  
33108 C  CG  . PRO   S  127 ? 1.7341 0.5416 1.7922 0.0953  -0.2924 0.0229  126 PRO   S CG  
33109 C  CD  . PRO   S  127 ? 1.7734 0.5197 1.7721 0.0794  -0.2815 0.0504  126 PRO   S CD  
33110 N  N   . TYR   S  128 ? 1.7247 0.4418 1.6966 0.1510  -0.2942 0.0187  127 TYR   S N   
33111 C  CA  . TYR   S  128 ? 1.7240 0.5145 1.6635 0.1880  -0.2665 -0.0375 127 TYR   S CA  
33112 C  C   . TYR   S  128 ? 1.8067 0.5130 1.6449 0.2212  -0.2850 -0.0307 127 TYR   S C   
33113 O  O   . TYR   S  128 ? 1.8685 0.4689 1.6474 0.2108  -0.2836 -0.0437 127 TYR   S O   
33114 C  CB  . TYR   S  128 ? 1.6969 0.5719 1.6554 0.1873  -0.2724 -0.0714 127 TYR   S CB  
33115 C  CG  . TYR   S  128 ? 1.6558 0.5699 1.5838 0.1708  -0.2488 -0.0747 127 TYR   S CG  
33116 C  CD1 . TYR   S  128 ? 1.6144 0.5117 1.5832 0.1525  -0.2497 -0.0986 127 TYR   S CD1 
33117 C  CD2 . TYR   S  128 ? 1.6615 0.5727 1.5863 0.1892  -0.2541 -0.0958 127 TYR   S CD2 
33118 C  CE1 . TYR   S  128 ? 1.5952 0.4739 1.5418 0.1181  -0.2465 -0.0626 127 TYR   S CE1 
33119 C  CE2 . TYR   S  128 ? 1.6407 0.5246 1.5410 0.1515  -0.2546 -0.0341 127 TYR   S CE2 
33120 C  CZ  . TYR   S  128 ? 1.5867 0.4812 1.5470 0.1374  -0.2486 -0.0502 127 TYR   S CZ  
33121 O  OH  . TYR   S  128 ? 1.5567 0.4691 1.5508 0.1202  -0.2329 -0.0092 127 TYR   S OH  
33122 N  N   . GLY   S  129 ? 1.8401 0.5366 1.6775 0.2412  -0.2710 -0.0912 128 GLY   S N   
33123 C  CA  . GLY   S  129 ? 1.8407 0.5494 1.7261 0.2506  -0.2807 -0.1017 128 GLY   S CA  
33124 C  C   . GLY   S  129 ? 1.8267 0.5374 1.7467 0.2670  -0.3087 -0.1211 128 GLY   S C   
33125 O  O   . GLY   S  129 ? 1.7794 0.5825 1.8199 0.3275  -0.2975 -0.1144 128 GLY   S O   
33126 N  N   . VAL   S  130 ? 1.7718 0.5416 1.7349 0.2539  -0.3180 -0.0945 129 VAL   S N   
33127 C  CA  . VAL   S  130 ? 1.7616 0.5800 1.7915 0.2681  -0.2901 -0.0931 129 VAL   S CA  
33128 C  C   . VAL   S  130 ? 1.7345 0.5254 1.8009 0.2912  -0.2988 -0.0928 129 VAL   S C   
33129 O  O   . VAL   S  130 ? 1.7470 0.5136 1.7871 0.2645  -0.2905 -0.1011 129 VAL   S O   
33130 C  CB  . VAL   S  130 ? 1.7783 0.6188 1.7729 0.2459  -0.2576 -0.0800 129 VAL   S CB  
33131 C  CG1 . VAL   S  130 ? 1.7665 0.6022 1.7556 0.2382  -0.2642 -0.0689 129 VAL   S CG1 
33132 C  CG2 . VAL   S  130 ? 1.7762 0.6713 1.8131 0.2657  -0.2391 -0.1033 129 VAL   S CG2 
33133 N  N   . GLY   S  131 ? 1.7309 0.5171 1.8525 0.2850  -0.3162 -0.1332 130 GLY   S N   
33134 C  CA  . GLY   S  131 ? 1.6929 0.5524 1.8792 0.2618  -0.3246 -0.1556 130 GLY   S CA  
33135 C  C   . GLY   S  131 ? 1.6793 0.5919 1.8840 0.2472  -0.2981 -0.1582 130 GLY   S C   
33136 O  O   . GLY   S  131 ? 1.6799 0.5935 1.8933 0.2018  -0.2884 -0.1522 130 GLY   S O   
33137 N  N   . LEU   S  132 ? 1.6711 0.6615 1.8940 0.2389  -0.3047 -0.1890 131 LEU   S N   
33138 C  CA  . LEU   S  132 ? 1.6409 0.7322 1.8916 0.2027  -0.3089 -0.2165 131 LEU   S CA  
33139 C  C   . LEU   S  132 ? 1.6195 0.8351 1.9283 0.1804  -0.3209 -0.2466 131 LEU   S C   
33140 O  O   . LEU   S  132 ? 1.6250 0.8969 1.9392 0.1688  -0.3021 -0.2458 131 LEU   S O   
33141 C  CB  . LEU   S  132 ? 1.6518 0.6724 1.8417 0.1665  -0.3269 -0.2129 131 LEU   S CB  
33142 C  CG  . LEU   S  132 ? 1.6509 0.6775 1.8257 0.1580  -0.3201 -0.2147 131 LEU   S CG  
33143 C  CD1 . LEU   S  132 ? 1.6390 0.6560 1.7926 0.1451  -0.3188 -0.2087 131 LEU   S CD1 
33144 C  CD2 . LEU   S  132 ? 1.6525 0.7138 1.8303 0.1333  -0.3130 -0.2305 131 LEU   S CD2 
33145 N  N   . LEU   S  133 ? 1.6400 0.8580 1.9223 0.1623  -0.2873 -0.2536 132 LEU   S N   
33146 C  CA  . LEU   S  133 ? 1.6425 0.8293 1.9111 0.1805  -0.2930 -0.2321 132 LEU   S CA  
33147 C  C   . LEU   S  133 ? 1.6323 0.8099 1.8934 0.2353  -0.2665 -0.2028 132 LEU   S C   
33148 O  O   . LEU   S  133 ? 1.6420 0.7169 1.9090 0.2884  -0.2451 -0.1958 132 LEU   S O   
33149 C  CB  . LEU   S  133 ? 1.6506 0.8480 1.8961 0.1931  -0.3005 -0.2384 132 LEU   S CB  
33150 C  CG  . LEU   S  133 ? 1.6806 0.8473 1.8762 0.2085  -0.3120 -0.2343 132 LEU   S CG  
33151 C  CD1 . LEU   S  133 ? 1.6677 0.9415 1.8921 0.2036  -0.3015 -0.2430 132 LEU   S CD1 
33152 C  CD2 . LEU   S  133 ? 1.6877 0.8694 1.8591 0.1978  -0.3334 -0.2310 132 LEU   S CD2 
33153 N  N   . ILE   S  134 ? 1.6110 0.7897 1.8749 0.2366  -0.2702 -0.1799 133 ILE   S N   
33154 C  CA  . ILE   S  134 ? 1.6168 0.7912 1.8568 0.1999  -0.2746 -0.1704 133 ILE   S CA  
33155 C  C   . ILE   S  134 ? 1.6206 0.7342 1.8524 0.2230  -0.2831 -0.1776 133 ILE   S C   
33156 O  O   . ILE   S  134 ? 1.5852 0.7335 1.8086 0.2321  -0.3001 -0.2276 133 ILE   S O   
33157 C  CB  . ILE   S  134 ? 1.6335 0.7663 1.8642 0.1828  -0.2484 -0.1664 133 ILE   S CB  
33158 C  CG1 . ILE   S  134 ? 1.6887 0.7751 1.8638 0.1164  -0.2583 -0.1640 133 ILE   S CG1 
33159 C  CG2 . ILE   S  134 ? 1.6073 0.7724 1.8642 0.1685  -0.2344 -0.1652 133 ILE   S CG2 
33160 C  CD1 . ILE   S  134 ? 1.7175 0.8775 1.8863 0.0808  -0.2515 -0.0854 133 ILE   S CD1 
33161 N  N   . ILE   S  135 ? 1.6381 0.6896 1.8516 0.2306  -0.2971 -0.1701 134 ILE   S N   
33162 C  CA  . ILE   S  135 ? 1.6478 0.7867 1.8657 0.2295  -0.3333 -0.1505 134 ILE   S CA  
33163 C  C   . ILE   S  135 ? 1.6984 0.7891 1.8739 0.1867  -0.3338 -0.1711 134 ILE   S C   
33164 O  O   . ILE   S  135 ? 1.6780 0.9908 1.8510 0.1527  -0.3645 -0.1461 134 ILE   S O   
33165 C  CB  . ILE   S  135 ? 1.6549 0.6964 1.9216 0.2662  -0.3346 -0.1537 134 ILE   S CB  
33166 C  CG1 . ILE   S  135 ? 1.6329 0.6178 1.9297 0.2627  -0.3112 -0.1704 134 ILE   S CG1 
33167 C  CG2 . ILE   S  135 ? 1.6836 0.7089 1.9590 0.2948  -0.3378 -0.1132 134 ILE   S CG2 
33168 C  CD1 . ILE   S  135 ? 1.6273 0.6005 1.9714 0.2696  -0.3100 -0.1829 134 ILE   S CD1 
33169 N  N   . GLY   S  136 ? 1.7131 0.9163 1.8460 0.1793  -0.3689 -0.1494 135 GLY   S N   
33170 C  CA  . GLY   S  136 ? 1.6866 0.9147 1.8020 0.2008  -0.3658 -0.1508 135 GLY   S CA  
33171 C  C   . GLY   S  136 ? 1.7057 0.8988 1.7880 0.2165  -0.3790 -0.1358 135 GLY   S C   
33172 O  O   . GLY   S  136 ? 1.7396 0.9963 1.7296 0.1765  -0.4530 -0.1218 135 GLY   S O   
33173 N  N   . TYR   S  137 ? 1.6737 0.8986 1.7922 0.2233  -0.3347 -0.1228 136 TYR   S N   
33174 C  CA  . TYR   S  137 ? 1.6461 0.9535 1.7658 0.2242  -0.3337 -0.1014 136 TYR   S CA  
33175 C  C   . TYR   S  137 ? 1.6216 0.9293 1.7715 0.1869  -0.2906 -0.0995 136 TYR   S C   
33176 O  O   . TYR   S  137 ? 1.6608 0.8244 1.7889 0.2254  -0.2398 -0.1542 136 TYR   S O   
33177 C  CB  . TYR   S  137 ? 1.6386 1.0208 1.7739 0.2346  -0.3294 -0.0880 136 TYR   S CB  
33178 C  CG  . TYR   S  137 ? 1.6561 1.0480 1.7866 0.2319  -0.3433 -0.0956 136 TYR   S CG  
33179 C  CD1 . TYR   S  137 ? 1.6877 1.0240 1.8078 0.2165  -0.3531 -0.0769 136 TYR   S CD1 
33180 C  CD2 . TYR   S  137 ? 1.6307 1.0996 1.8344 0.2731  -0.3382 -0.1165 136 TYR   S CD2 
33181 C  CE1 . TYR   S  137 ? 1.6863 1.0232 1.8241 0.2226  -0.3650 -0.0687 136 TYR   S CE1 
33182 C  CE2 . TYR   S  137 ? 1.6289 1.1474 1.8718 0.2693  -0.3570 -0.1268 136 TYR   S CE2 
33183 C  CZ  . TYR   S  137 ? 1.6086 1.1083 1.8565 0.2394  -0.3916 -0.0847 136 TYR   S CZ  
33184 O  OH  . TYR   S  137 ? 1.4953 1.1432 1.9427 0.2166  -0.4160 -0.0624 136 TYR   S OH  
33185 N  N   . ASP   S  138 ? 1.5563 0.8651 1.7542 0.1802  -0.3245 -0.0656 137 ASP   S N   
33186 C  CA  . ASP   S  138 ? 1.5310 0.8774 1.6985 0.1490  -0.3356 -0.0904 137 ASP   S CA  
33187 C  C   . ASP   S  138 ? 1.4606 0.9065 1.7395 0.1118  -0.3884 -0.0552 137 ASP   S C   
33188 O  O   . ASP   S  138 ? 1.4574 0.7573 1.6685 0.1052  -0.4014 -0.0136 137 ASP   S O   
33189 C  CB  . ASP   S  138 ? 1.5186 0.9136 1.7036 0.1637  -0.3351 -0.0967 137 ASP   S CB  
33190 C  CG  . ASP   S  138 ? 1.4999 0.9583 1.6747 0.1979  -0.3631 -0.0701 137 ASP   S CG  
33191 O  OD1 . ASP   S  138 ? 1.5212 0.9846 1.7133 0.2939  -0.3638 -0.0729 137 ASP   S OD1 
33192 O  OD2 . ASP   S  138 ? 1.4750 1.0645 1.6428 0.1759  -0.3564 -0.0751 137 ASP   S OD2 
33193 N  N   . LYS   S  139 ? 1.5210 0.9260 1.7358 0.0868  -0.3931 -0.1164 138 LYS   S N   
33194 C  CA  . LYS   S  139 ? 1.5312 0.9485 1.7913 0.0677  -0.4240 -0.1509 138 LYS   S CA  
33195 C  C   . LYS   S  139 ? 1.5306 0.9676 1.8261 0.0828  -0.4596 -0.1478 138 LYS   S C   
33196 O  O   . LYS   S  139 ? 1.5390 0.9834 1.9180 0.0523  -0.4871 -0.2081 138 LYS   S O   
33197 C  CB  . LYS   S  139 ? 1.5160 0.9793 1.8039 0.0540  -0.4067 -0.1504 138 LYS   S CB  
33198 C  CG  . LYS   S  139 ? 1.5169 0.9670 1.8203 0.0152  -0.3707 -0.1555 138 LYS   S CG  
33199 C  CD  . LYS   S  139 ? 1.5423 0.9453 1.8793 -0.0091 -0.3299 -0.1765 138 LYS   S CD  
33200 C  CE  . LYS   S  139 ? 1.5946 0.9670 1.9442 -0.0493 -0.2614 -0.1974 138 LYS   S CE  
33201 N  NZ  . LYS   S  139 ? 1.6499 1.0712 1.9643 -0.0648 -0.2173 -0.2456 138 LYS   S NZ  
33202 N  N   . SER   S  140 ? 1.5311 0.9386 1.8285 0.1226  -0.4753 -0.1075 139 SER   S N   
33203 C  CA  . SER   S  140 ? 1.5431 0.9720 1.8280 0.1166  -0.4650 -0.0695 139 SER   S CA  
33204 C  C   . SER   S  140 ? 1.5945 0.9238 1.8585 0.1628  -0.4622 -0.0203 139 SER   S C   
33205 O  O   . SER   S  140 ? 1.6497 0.9479 1.8867 0.1724  -0.4741 0.0320  139 SER   S O   
33206 C  CB  . SER   S  140 ? 1.5224 0.9627 1.7746 0.1419  -0.4855 -0.0282 139 SER   S CB  
33207 O  OG  . SER   S  140 ? 1.4687 1.0272 1.7687 0.1424  -0.4834 -0.0293 139 SER   S OG  
33208 N  N   . GLY   S  141 ? 1.6088 1.0072 1.8927 0.1535  -0.4019 -0.0534 140 GLY   S N   
33209 C  CA  . GLY   S  141 ? 1.6241 0.9799 1.9400 0.1828  -0.4074 -0.0507 140 GLY   S CA  
33210 C  C   . GLY   S  141 ? 1.6548 0.9056 1.9661 0.2204  -0.3715 -0.0831 140 GLY   S C   
33211 O  O   . GLY   S  141 ? 1.6047 1.0340 1.9984 0.2152  -0.3661 -0.1353 140 GLY   S O   
33212 N  N   . ALA   S  142 ? 1.6932 0.8931 1.9670 0.2293  -0.3878 -0.0850 141 ALA   S N   
33213 C  CA  . ALA   S  142 ? 1.6494 0.8780 1.9857 0.1961  -0.3776 -0.0831 141 ALA   S CA  
33214 C  C   . ALA   S  142 ? 1.6551 0.7639 1.9508 0.2229  -0.4058 -0.1020 141 ALA   S C   
33215 O  O   . ALA   S  142 ? 1.5967 0.5973 1.9684 0.1675  -0.4107 -0.1065 141 ALA   S O   
33216 C  CB  . ALA   S  142 ? 1.6821 0.9294 2.0367 0.2627  -0.3849 -0.0721 141 ALA   S CB  
33217 N  N   . HIS   S  143 ? 1.5756 0.6053 1.9978 0.2070  -0.3718 -0.1311 142 HIS   S N   
33218 C  CA  . HIS   S  143 ? 1.5357 0.6462 2.0081 0.2079  -0.3879 -0.1262 142 HIS   S CA  
33219 C  C   . HIS   S  143 ? 1.5112 0.7531 2.0055 0.1928  -0.3506 -0.1559 142 HIS   S C   
33220 O  O   . HIS   S  143 ? 1.4755 0.7617 2.0612 0.1839  -0.3566 -0.0912 142 HIS   S O   
33221 C  CB  . HIS   S  143 ? 1.5281 0.5962 1.9739 0.1986  -0.4291 -0.1222 142 HIS   S CB  
33222 C  CG  . HIS   S  143 ? 1.5816 0.7024 1.9272 0.1715  -0.4818 -0.1239 142 HIS   S CG  
33223 N  ND1 . HIS   S  143 ? 1.5853 0.6565 1.9274 0.1650  -0.5619 -0.0720 142 HIS   S ND1 
33224 C  CD2 . HIS   S  143 ? 1.6312 0.7204 1.9486 0.1426  -0.4868 -0.1571 142 HIS   S CD2 
33225 C  CE1 . HIS   S  143 ? 1.6077 0.7093 1.8915 0.1747  -0.5776 -0.0852 142 HIS   S CE1 
33226 N  NE2 . HIS   S  143 ? 1.6421 0.6790 1.9233 0.1518  -0.5333 -0.1299 142 HIS   S NE2 
33227 N  N   . LEU   S  144 ? 1.5233 0.7421 2.0141 0.2020  -0.3089 -0.1834 143 LEU   S N   
33228 C  CA  . LEU   S  144 ? 1.5503 0.7010 1.9935 0.2260  -0.2778 -0.1844 143 LEU   S CA  
33229 C  C   . LEU   S  144 ? 1.5327 0.6769 1.9471 0.2505  -0.2693 -0.1924 143 LEU   S C   
33230 O  O   . LEU   S  144 ? 1.4761 0.6750 1.9851 0.2835  -0.2551 -0.1503 143 LEU   S O   
33231 C  CB  . LEU   S  144 ? 1.6215 0.6962 2.0302 0.2592  -0.3090 -0.1911 143 LEU   S CB  
33232 C  CG  . LEU   S  144 ? 1.6714 0.6810 2.0614 0.2682  -0.3311 -0.1951 143 LEU   S CG  
33233 C  CD1 . LEU   S  144 ? 1.6715 0.6608 2.0557 0.2519  -0.3347 -0.2072 143 LEU   S CD1 
33234 C  CD2 . LEU   S  144 ? 1.6932 0.6843 2.1112 0.2833  -0.3456 -0.2330 143 LEU   S CD2 
33235 N  N   . LEU   S  145 ? 1.5396 0.6797 1.8938 0.2277  -0.2500 -0.2009 144 LEU   S N   
33236 C  CA  . LEU   S  145 ? 1.5524 0.7001 1.8948 0.2133  -0.2542 -0.1811 144 LEU   S CA  
33237 C  C   . LEU   S  145 ? 1.6028 0.7215 1.9257 0.2166  -0.2384 -0.2061 144 LEU   S C   
33238 O  O   . LEU   S  145 ? 1.6077 0.7513 1.9737 0.2252  -0.1931 -0.1944 144 LEU   S O   
33239 C  CB  . LEU   S  145 ? 1.5359 0.6635 1.8384 0.1908  -0.2523 -0.1933 144 LEU   S CB  
33240 C  CG  . LEU   S  145 ? 1.5136 0.6577 1.8278 0.1973  -0.2426 -0.1612 144 LEU   S CG  
33241 C  CD1 . LEU   S  145 ? 1.4816 0.6753 1.8533 0.2107  -0.2512 -0.1317 144 LEU   S CD1 
33242 C  CD2 . LEU   S  145 ? 1.4978 0.6697 1.8130 0.1919  -0.2532 -0.1533 144 LEU   S CD2 
33243 N  N   . GLU   S  146 ? 1.6342 0.6958 1.9658 0.2112  -0.2633 -0.2083 145 GLU   S N   
33244 C  CA  . GLU   S  146 ? 1.6161 0.7365 1.9975 0.1844  -0.2828 -0.2210 145 GLU   S CA  
33245 C  C   . GLU   S  146 ? 1.6140 0.6643 1.9309 0.1985  -0.3038 -0.2048 145 GLU   S C   
33246 O  O   . GLU   S  146 ? 1.5554 0.6695 1.9283 0.2053  -0.3130 -0.2306 145 GLU   S O   
33247 C  CB  . GLU   S  146 ? 1.6998 0.7458 2.0718 0.1713  -0.2912 -0.1883 145 GLU   S CB  
33248 C  CG  . GLU   S  146 ? 1.7964 0.8563 2.0706 0.1323  -0.2791 -0.2331 145 GLU   S CG  
33249 C  CD  . GLU   S  146 ? 1.8685 0.8436 2.1457 0.0913  -0.2873 -0.2197 145 GLU   S CD  
33250 O  OE1 . GLU   S  146 ? 1.9602 0.9646 2.1601 0.2012  -0.3238 -0.2037 145 GLU   S OE1 
33251 O  OE2 . GLU   S  146 ? 2.0023 0.7090 2.2627 0.0136  -0.1652 -0.2127 145 GLU   S OE2 
33252 N  N   . PHE   S  147 ? 1.6141 0.6690 1.9109 0.2101  -0.2906 -0.2106 146 PHE   S N   
33253 C  CA  . PHE   S  147 ? 1.6270 0.6776 1.8649 0.2435  -0.3102 -0.1938 146 PHE   S CA  
33254 C  C   . PHE   S  147 ? 1.6562 0.6913 1.8933 0.2927  -0.3349 -0.2346 146 PHE   S C   
33255 O  O   . PHE   S  147 ? 1.6048 0.6678 1.9732 0.4191  -0.2946 -0.1902 146 PHE   S O   
33256 C  CB  . PHE   S  147 ? 1.6105 0.6051 1.8243 0.2344  -0.2867 -0.2452 146 PHE   S CB  
33257 C  CG  . PHE   S  147 ? 1.6178 0.5900 1.7634 0.2413  -0.2805 -0.2246 146 PHE   S CG  
33258 C  CD1 . PHE   S  147 ? 1.6339 0.6208 1.7133 0.2065  -0.2630 -0.2215 146 PHE   S CD1 
33259 C  CD2 . PHE   S  147 ? 1.6367 0.5883 1.7419 0.2553  -0.2610 -0.2095 146 PHE   S CD2 
33260 C  CE1 . PHE   S  147 ? 1.6438 0.6460 1.6663 0.2030  -0.2651 -0.1851 146 PHE   S CE1 
33261 C  CE2 . PHE   S  147 ? 1.6558 0.5748 1.6980 0.2362  -0.2702 -0.1998 146 PHE   S CE2 
33262 C  CZ  . PHE   S  147 ? 1.6519 0.5991 1.6696 0.2151  -0.2624 -0.1863 146 PHE   S CZ  
33263 N  N   . GLN   S  148 ? 1.6658 0.7752 1.9065 0.2503  -0.3773 -0.2039 147 GLN   S N   
33264 C  CA  . GLN   S  148 ? 1.7535 0.8223 1.9306 0.2418  -0.4201 -0.2490 147 GLN   S CA  
33265 C  C   . GLN   S  148 ? 1.7688 0.7264 1.8207 0.2261  -0.4460 -0.2535 147 GLN   S C   
33266 O  O   . GLN   S  148 ? 1.7658 0.8004 1.7708 0.2493  -0.4060 -0.1943 147 GLN   S O   
33267 C  CB  . GLN   S  148 ? 1.7690 0.8116 1.9878 0.2665  -0.4606 -0.2458 147 GLN   S CB  
33268 C  CG  . GLN   S  148 ? 1.7880 0.9323 2.1345 0.2985  -0.4333 -0.3660 147 GLN   S CG  
33269 C  CD  . GLN   S  148 ? 1.8783 1.0368 2.1973 0.3007  -0.3883 -0.3127 147 GLN   S CD  
33270 O  OE1 . GLN   S  148 ? 1.8142 1.4064 2.3805 0.3724  -0.3647 -0.4629 147 GLN   S OE1 
33271 N  NE2 . GLN   S  148 ? 1.8707 1.1495 2.2761 0.2655  -0.3766 -0.3472 147 GLN   S NE2 
33272 N  N   . PRO   S  149 ? 1.8196 0.5848 1.8208 0.2246  -0.4253 -0.2924 148 PRO   S N   
33273 C  CA  . PRO   S  149 ? 1.7867 0.6036 1.7603 0.1764  -0.4252 -0.3172 148 PRO   S CA  
33274 C  C   . PRO   S  149 ? 1.8198 0.5170 1.7039 0.1383  -0.4434 -0.3343 148 PRO   S C   
33275 O  O   . PRO   S  149 ? 1.7385 0.4898 1.6478 0.0202  -0.4164 -0.4252 148 PRO   S O   
33276 C  CB  . PRO   S  149 ? 1.8189 0.5768 1.7742 0.1908  -0.4227 -0.3344 148 PRO   S CB  
33277 C  CG  . PRO   S  149 ? 1.8381 0.5947 1.8172 0.2151  -0.4235 -0.2931 148 PRO   S CG  
33278 C  CD  . PRO   S  149 ? 1.8385 0.5853 1.8292 0.2214  -0.4228 -0.3049 148 PRO   S CD  
33279 N  N   . SER   S  150 ? 1.7975 0.5468 1.6981 0.1518  -0.4751 -0.3399 149 SER   S N   
33280 C  CA  . SER   S  150 ? 1.7988 0.6532 1.6806 0.1392  -0.5060 -0.3032 149 SER   S CA  
33281 C  C   . SER   S  150 ? 1.7983 0.7031 1.6891 0.1432  -0.4788 -0.3256 149 SER   S C   
33282 O  O   . SER   S  150 ? 1.7748 0.8839 1.7159 0.0828  -0.4922 -0.3699 149 SER   S O   
33283 C  CB  . SER   S  150 ? 1.8557 0.6775 1.6620 0.1358  -0.5443 -0.2913 149 SER   S CB  
33284 O  OG  . SER   S  150 ? 1.9111 0.6781 1.6099 0.1617  -0.6043 -0.2473 149 SER   S OG  
33285 N  N   . GLY   S  151 ? 1.7869 0.7025 1.7335 0.1483  -0.4445 -0.2331 150 GLY   S N   
33286 C  CA  . GLY   S  151 ? 1.7795 0.6331 1.7875 0.1753  -0.4070 -0.1949 150 GLY   S CA  
33287 C  C   . GLY   S  151 ? 1.7514 0.6666 1.8418 0.1922  -0.4156 -0.1614 150 GLY   S C   
33288 O  O   . GLY   S  151 ? 1.6716 0.6397 1.7956 0.1536  -0.4486 -0.0990 150 GLY   S O   
33289 N  N   . ASN   S  152 ? 1.7820 0.6810 1.9373 0.2297  -0.3830 -0.1937 151 ASN   S N   
33290 C  CA  . ASN   S  152 ? 1.7592 0.5958 1.9364 0.2277  -0.3625 -0.1923 151 ASN   S CA  
33291 C  C   . ASN   S  152 ? 1.7427 0.6783 1.9601 0.2154  -0.3167 -0.2193 151 ASN   S C   
33292 O  O   . ASN   S  152 ? 1.7014 0.7106 2.0351 0.1623  -0.2535 -0.2359 151 ASN   S O   
33293 C  CB  . ASN   S  152 ? 1.8486 0.5779 1.9769 0.2602  -0.3905 -0.2447 151 ASN   S CB  
33294 C  CG  . ASN   S  152 ? 1.8925 0.3954 1.9865 0.2765  -0.4049 -0.2386 151 ASN   S CG  
33295 O  OD1 . ASN   S  152 ? 1.8906 0.2872 1.9601 0.3058  -0.4480 -0.2047 151 ASN   S OD1 
33296 N  ND2 . ASN   S  152 ? 1.9754 0.4251 2.0418 0.2548  -0.4026 -0.2825 151 ASN   S ND2 
33297 N  N   . VAL   S  153 ? 1.6464 0.6555 1.8991 0.2114  -0.2946 -0.1815 152 VAL   S N   
33298 C  CA  . VAL   S  153 ? 1.6013 0.6898 1.9016 0.2403  -0.3068 -0.1365 152 VAL   S CA  
33299 C  C   . VAL   S  153 ? 1.5825 0.6696 1.9214 0.2549  -0.3017 -0.1202 152 VAL   S C   
33300 O  O   . VAL   S  153 ? 1.5280 0.6055 1.9586 0.3331  -0.2637 -0.1069 152 VAL   S O   
33301 C  CB  . VAL   S  153 ? 1.5993 0.7084 1.8419 0.2228  -0.3273 -0.0302 152 VAL   S CB  
33302 C  CG1 . VAL   S  153 ? 1.5643 0.7643 1.8176 0.2378  -0.3380 0.0160  152 VAL   S CG1 
33303 C  CG2 . VAL   S  153 ? 1.6206 0.7309 1.8274 0.1841  -0.3274 -0.0144 152 VAL   S CG2 
33304 N  N   . THR   S  154 ? 1.5599 0.7186 2.0500 0.2107  -0.3269 -0.1168 153 THR   S N   
33305 C  CA  . THR   S  154 ? 1.6143 0.7575 2.0898 0.1899  -0.3722 -0.0938 153 THR   S CA  
33306 C  C   . THR   S  154 ? 1.6516 0.8055 2.1030 0.1449  -0.4034 -0.1182 153 THR   S C   
33307 O  O   . THR   S  154 ? 1.7499 0.8861 2.1400 0.1862  -0.3418 -0.1353 153 THR   S O   
33308 C  CB  . THR   S  154 ? 1.5667 0.7558 2.1134 0.1944  -0.3880 -0.0795 153 THR   S CB  
33309 O  OG1 . THR   S  154 ? 1.6042 0.8002 2.1380 0.1619  -0.3578 -0.0458 153 THR   S OG1 
33310 C  CG2 . THR   S  154 ? 1.5593 0.7949 2.1323 0.1956  -0.3979 -0.0729 153 THR   S CG2 
33311 N  N   . GLU   S  155 ? 1.7316 0.8052 2.0686 0.1393  -0.4169 -0.0978 154 GLU   S N   
33312 C  CA  . GLU   S  155 ? 1.7352 0.8135 2.0356 0.1317  -0.4400 -0.0558 154 GLU   S CA  
33313 C  C   . GLU   S  155 ? 1.7641 0.6713 2.0193 0.0987  -0.4412 -0.0875 154 GLU   S C   
33314 O  O   . GLU   S  155 ? 1.8112 0.3103 2.0795 0.1416  -0.4776 -0.1676 154 GLU   S O   
33315 C  CB  . GLU   S  155 ? 1.7437 0.8368 1.9549 0.0772  -0.4493 -0.0245 154 GLU   S CB  
33316 C  CG  . GLU   S  155 ? 1.7713 0.8814 1.9660 0.0380  -0.4544 0.0666  154 GLU   S CG  
33317 C  CD  . GLU   S  155 ? 1.7957 0.8705 1.9370 -0.0398 -0.4505 0.0872  154 GLU   S CD  
33318 O  OE1 . GLU   S  155 ? 1.7545 1.0367 1.9369 -0.1033 -0.5013 0.1014  154 GLU   S OE1 
33319 O  OE2 . GLU   S  155 ? 1.7799 0.8775 1.9254 -0.1326 -0.4196 0.2077  154 GLU   S OE2 
33320 N  N   . LEU   S  156 ? 1.7303 0.7374 2.0676 0.0943  -0.4442 -0.1189 155 LEU   S N   
33321 C  CA  . LEU   S  156 ? 1.7548 0.8147 2.0867 0.1395  -0.4553 -0.0935 155 LEU   S CA  
33322 C  C   . LEU   S  156 ? 1.6868 0.9920 2.1310 0.1681  -0.4655 -0.1148 155 LEU   S C   
33323 O  O   . LEU   S  156 ? 1.8029 1.1236 2.0951 0.2269  -0.4549 -0.0032 155 LEU   S O   
33324 C  CB  . LEU   S  156 ? 1.7618 0.8496 2.0563 0.1274  -0.4272 -0.0919 155 LEU   S CB  
33325 C  CG  . LEU   S  156 ? 1.7863 0.8809 2.0469 0.1056  -0.4065 -0.0693 155 LEU   S CG  
33326 C  CD1 . LEU   S  156 ? 1.8054 0.8809 2.0242 0.0847  -0.3896 -0.0487 155 LEU   S CD1 
33327 C  CD2 . LEU   S  156 ? 1.7913 0.8636 2.1026 0.1299  -0.4175 -0.0919 155 LEU   S CD2 
33328 N  N   . TYR   S  157 ? 1.7934 0.9743 2.1549 0.2314  -0.4849 -0.0810 156 TYR   S N   
33329 C  CA  . TYR   S  157 ? 1.7468 1.0213 2.1584 0.2837  -0.5061 -0.0866 156 TYR   S CA  
33330 C  C   . TYR   S  157 ? 1.7362 0.9306 2.1847 0.2967  -0.4940 -0.1290 156 TYR   S C   
33331 O  O   . TYR   S  157 ? 1.6716 1.0901 2.1876 0.2308  -0.4797 -0.1285 156 TYR   S O   
33332 C  CB  . TYR   S  157 ? 1.7286 1.0368 2.2089 0.2858  -0.5281 -0.0860 156 TYR   S CB  
33333 C  CG  . TYR   S  157 ? 1.7255 1.0705 2.1997 0.2591  -0.5837 -0.0921 156 TYR   S CG  
33334 C  CD1 . TYR   S  157 ? 1.7127 1.1150 2.1821 0.1864  -0.5990 -0.0997 156 TYR   S CD1 
33335 C  CD2 . TYR   S  157 ? 1.7335 1.0572 2.2139 0.2587  -0.6138 -0.0808 156 TYR   S CD2 
33336 C  CE1 . TYR   S  157 ? 1.7461 1.1473 2.1772 0.1429  -0.6393 -0.1075 156 TYR   S CE1 
33337 C  CE2 . TYR   S  157 ? 1.7631 1.1011 2.2096 0.2191  -0.6453 -0.0910 156 TYR   S CE2 
33338 C  CZ  . TYR   S  157 ? 1.7827 1.1529 2.1550 0.1512  -0.6557 -0.1061 156 TYR   S CZ  
33339 O  OH  . TYR   S  157 ? 1.8561 1.3189 2.1370 0.0904  -0.6916 -0.1153 156 TYR   S OH  
33340 N  N   . GLY   S  158 ? 1.7545 0.8354 2.1913 0.3916  -0.4820 -0.1111 157 GLY   S N   
33341 C  CA  . GLY   S  158 ? 1.7287 0.8356 2.2084 0.4112  -0.4614 -0.1232 157 GLY   S CA  
33342 C  C   . GLY   S  158 ? 1.7311 0.8703 2.1806 0.3971  -0.4571 -0.1309 157 GLY   S C   
33343 O  O   . GLY   S  158 ? 1.7224 1.0550 2.2000 0.3464  -0.4426 -0.1155 157 GLY   S O   
33344 N  N   . THR   S  159 ? 1.7092 0.7952 2.1657 0.3879  -0.4058 -0.1484 158 THR   S N   
33345 C  CA  . THR   S  159 ? 1.7262 0.7916 2.1151 0.3809  -0.3636 -0.1825 158 THR   S CA  
33346 C  C   . THR   S  159 ? 1.7424 0.7258 2.1167 0.3505  -0.3566 -0.2083 158 THR   S C   
33347 O  O   . THR   S  159 ? 1.7339 0.5597 2.1136 0.3902  -0.3772 -0.2243 158 THR   S O   
33348 C  CB  . THR   S  159 ? 1.7179 0.7263 2.0792 0.3635  -0.3536 -0.1533 158 THR   S CB  
33349 O  OG1 . THR   S  159 ? 1.6870 0.7917 2.0450 0.3447  -0.3148 -0.2017 158 THR   S OG1 
33350 C  CG2 . THR   S  159 ? 1.6829 0.7417 2.0481 0.3636  -0.3403 -0.1466 158 THR   S CG2 
33351 N  N   . ALA   S  160 ? 1.7931 0.7914 2.0933 0.3311  -0.3732 -0.2385 159 ALA   S N   
33352 C  CA  . ALA   S  160 ? 1.7945 0.7819 2.1012 0.3290  -0.3622 -0.2638 159 ALA   S CA  
33353 C  C   . ALA   S  160 ? 1.8322 0.6964 2.0586 0.3021  -0.3654 -0.2563 159 ALA   S C   
33354 O  O   . ALA   S  160 ? 1.8471 0.6822 2.0524 0.2810  -0.4024 -0.2450 159 ALA   S O   
33355 C  CB  . ALA   S  160 ? 1.8255 0.7901 2.1544 0.3429  -0.3512 -0.2950 159 ALA   S CB  
33356 N  N   . ILE   S  161 ? 1.8380 0.6956 2.0301 0.3014  -0.3729 -0.3127 160 ILE   S N   
33357 C  CA  . ILE   S  161 ? 1.8573 0.6708 1.9917 0.3027  -0.3688 -0.3328 160 ILE   S CA  
33358 C  C   . ILE   S  161 ? 1.9016 0.6775 2.0039 0.2987  -0.3403 -0.3449 160 ILE   S C   
33359 O  O   . ILE   S  161 ? 1.9139 0.6474 1.9813 0.3086  -0.3394 -0.3415 160 ILE   S O   
33360 C  CB  . ILE   S  161 ? 1.8340 0.6875 1.9116 0.2979  -0.3937 -0.3455 160 ILE   S CB  
33361 C  CG1 . ILE   S  161 ? 1.8115 0.7137 1.8516 0.2628  -0.3757 -0.3595 160 ILE   S CG1 
33362 C  CG2 . ILE   S  161 ? 1.8306 0.6023 1.8933 0.2816  -0.4155 -0.3319 160 ILE   S CG2 
33363 C  CD1 . ILE   S  161 ? 1.8018 0.7288 1.7996 0.2609  -0.3623 -0.3594 160 ILE   S CD1 
33364 N  N   . GLY   S  162 ? 1.9327 0.7065 2.0476 0.2653  -0.3357 -0.3530 161 GLY   S N   
33365 C  CA  . GLY   S  162 ? 1.9537 0.7847 2.0652 0.2635  -0.2932 -0.3759 161 GLY   S CA  
33366 C  C   . GLY   S  162 ? 1.9663 0.7936 2.1413 0.2791  -0.2814 -0.3791 161 GLY   S C   
33367 O  O   . GLY   S  162 ? 1.9979 0.7625 2.2290 0.3221  -0.2841 -0.3203 161 GLY   S O   
33368 N  N   . ALA   S  163 ? 1.9244 0.7523 2.1817 0.2802  -0.2862 -0.4252 162 ALA   S N   
33369 C  CA  . ALA   S  163 ? 1.9358 0.8014 2.1841 0.3038  -0.2558 -0.5100 162 ALA   S CA  
33370 C  C   . ALA   S  163 ? 1.9109 0.7283 2.2532 0.2592  -0.2508 -0.5177 162 ALA   S C   
33371 O  O   . ALA   S  163 ? 1.9532 0.5579 2.2713 0.2568  -0.2445 -0.6355 162 ALA   S O   
33372 C  CB  . ALA   S  163 ? 1.9387 0.9249 2.1821 0.3269  -0.2388 -0.5192 162 ALA   S CB  
33373 N  N   . ARG   S  164 ? 1.9558 0.7487 2.3272 0.2891  -0.2640 -0.4799 163 ARG   S N   
33374 C  CA  . ARG   S  164 ? 1.9566 0.8025 2.3882 0.2688  -0.2859 -0.4367 163 ARG   S CA  
33375 C  C   . ARG   S  164 ? 1.8683 0.6902 2.3967 0.2851  -0.2793 -0.3809 163 ARG   S C   
33376 O  O   . ARG   S  164 ? 1.8624 0.6152 2.4170 0.2640  -0.2557 -0.3761 163 ARG   S O   
33377 C  CB  . ARG   S  164 ? 1.9941 1.1657 2.4246 0.2266  -0.2131 -0.3816 163 ARG   S CB  
33378 C  CG  . ARG   S  164 ? 2.1110 1.3035 2.4012 0.0943  -0.2338 -0.4659 163 ARG   S CG  
33379 C  CD  . ARG   S  164 ? 2.1708 1.6038 2.4041 0.0246  -0.1978 -0.3923 163 ARG   S CD  
33380 N  NE  . ARG   S  164 ? 2.1914 1.7730 2.3573 -0.0833 -0.1905 -0.3219 163 ARG   S NE  
33381 C  CZ  . ARG   S  164 ? 2.2730 1.8880 2.3676 -0.0940 -0.2033 -0.2605 163 ARG   S CZ  
33382 N  NH1 . ARG   S  164 ? 2.2789 1.9759 2.4217 -0.1007 -0.1957 -0.2328 163 ARG   S NH1 
33383 N  NH2 . ARG   S  164 ? 2.2157 1.8932 2.3500 -0.1415 -0.1799 -0.2470 163 ARG   S NH2 
33384 N  N   . SER   S  165 ? 1.8293 0.6026 2.3595 0.2548  -0.3235 -0.3753 164 SER   S N   
33385 C  CA  . SER   S  165 ? 1.7943 0.5060 2.3961 0.2827  -0.3333 -0.3482 164 SER   S CA  
33386 C  C   . SER   S  165 ? 1.8390 0.6331 2.4193 0.3343  -0.3599 -0.3330 164 SER   S C   
33387 O  O   . SER   S  165 ? 1.8549 0.3813 2.4587 0.3811  -0.3635 -0.2823 164 SER   S O   
33388 C  CB  . SER   S  165 ? 1.7385 0.4262 2.3360 0.2250  -0.3628 -0.3610 164 SER   S CB  
33389 O  OG  . SER   S  165 ? 1.7113 0.3513 2.3406 0.2725  -0.3992 -0.3682 164 SER   S OG  
33390 N  N   . GLN   S  166 ? 1.8984 0.6601 2.4710 0.3177  -0.3219 -0.2963 165 GLN   S N   
33391 C  CA  . GLN   S  166 ? 1.9131 0.8932 2.4406 0.3868  -0.3353 -0.2913 165 GLN   S CA  
33392 C  C   . GLN   S  166 ? 1.9024 0.8598 2.4887 0.4315  -0.3228 -0.3128 165 GLN   S C   
33393 O  O   . GLN   S  166 ? 1.8360 0.9422 2.5333 0.4686  -0.3664 -0.3039 165 GLN   S O   
33394 C  CB  . GLN   S  166 ? 1.9777 0.9807 2.4611 0.2856  -0.3007 -0.3262 165 GLN   S CB  
33395 C  CG  . GLN   S  166 ? 2.0025 1.1569 2.4248 0.2815  -0.3138 -0.3110 165 GLN   S CG  
33396 C  CD  . GLN   S  166 ? 1.9918 1.2540 2.3781 0.2492  -0.3265 -0.3308 165 GLN   S CD  
33397 O  OE1 . GLN   S  166 ? 1.9411 1.4199 2.2800 0.2582  -0.3593 -0.3474 165 GLN   S OE1 
33398 N  NE2 . GLN   S  166 ? 2.0134 1.2614 2.3076 0.2437  -0.2881 -0.3659 165 GLN   S NE2 
33399 N  N   . GLY   S  167 ? 1.8519 0.8134 2.5341 0.4830  -0.3021 -0.3358 166 GLY   S N   
33400 C  CA  . GLY   S  167 ? 1.8564 0.8858 2.5850 0.5002  -0.2531 -0.3203 166 GLY   S CA  
33401 C  C   . GLY   S  167 ? 1.8510 0.8800 2.5890 0.4829  -0.2308 -0.3018 166 GLY   S C   
33402 O  O   . GLY   S  167 ? 1.8418 0.8295 2.6145 0.4801  -0.2377 -0.2749 166 GLY   S O   
33403 N  N   . ALA   S  168 ? 1.8440 0.9558 2.5488 0.5003  -0.2083 -0.2437 167 ALA   S N   
33404 C  CA  . ALA   S  168 ? 1.8170 1.0134 2.5513 0.4676  -0.2133 -0.2787 167 ALA   S CA  
33405 C  C   . ALA   S  168 ? 1.8393 1.1359 2.5397 0.4606  -0.2188 -0.2472 167 ALA   S C   
33406 O  O   . ALA   S  168 ? 1.8296 1.2033 2.5730 0.4420  -0.2379 -0.2334 167 ALA   S O   
33407 C  CB  . ALA   S  168 ? 1.7689 0.9805 2.5076 0.4699  -0.1769 -0.2974 167 ALA   S CB  
33408 N  N   . LYS   S  169 ? 1.8351 1.1889 2.5539 0.4139  -0.2924 -0.2106 168 LYS   S N   
33409 C  CA  . LYS   S  169 ? 1.7930 1.2247 2.5207 0.3892  -0.3245 -0.1687 168 LYS   S CA  
33410 C  C   . LYS   S  169 ? 1.8301 1.1546 2.5906 0.3972  -0.3663 -0.1843 168 LYS   S C   
33411 O  O   . LYS   S  169 ? 1.8186 1.1310 2.6085 0.4620  -0.3317 -0.2164 168 LYS   S O   
33412 C  CB  . LYS   S  169 ? 1.7914 1.2727 2.4680 0.3794  -0.3665 -0.1048 168 LYS   S CB  
33413 C  CG  . LYS   S  169 ? 1.6718 1.3639 2.3950 0.3640  -0.3997 -0.0289 168 LYS   S CG  
33414 C  CD  . LYS   S  169 ? 1.6739 1.3758 2.3536 0.3632  -0.4307 0.0489  168 LYS   S CD  
33415 C  CE  . LYS   S  169 ? 1.6194 1.3939 2.2750 0.3278  -0.4546 0.0949  168 LYS   S CE  
33416 N  NZ  . LYS   S  169 ? 1.6307 1.4380 2.2386 0.2383  -0.4579 0.1142  168 LYS   S NZ  
33417 N  N   . THR   S  170 ? 1.8333 1.1271 2.6486 0.3433  -0.3940 -0.2342 169 THR   S N   
33418 C  CA  . THR   S  170 ? 1.8020 1.2071 2.6442 0.3142  -0.4428 -0.2407 169 THR   S CA  
33419 C  C   . THR   S  170 ? 1.7944 1.2214 2.6965 0.3231  -0.4522 -0.2568 169 THR   S C   
33420 O  O   . THR   S  170 ? 1.8330 1.1890 2.7251 0.2720  -0.4920 -0.2818 169 THR   S O   
33421 C  CB  . THR   S  170 ? 1.7911 1.2177 2.6025 0.2946  -0.4555 -0.2587 169 THR   S CB  
33422 O  OG1 . THR   S  170 ? 1.8332 1.2082 2.5602 0.2480  -0.4175 -0.2702 169 THR   S OG1 
33423 C  CG2 . THR   S  170 ? 1.7910 1.1827 2.6296 0.3014  -0.4619 -0.2672 169 THR   S CG2 
33424 N  N   . TYR   S  171 ? 1.8130 1.2243 2.7281 0.3928  -0.3942 -0.2523 170 TYR   S N   
33425 C  CA  . TYR   S  171 ? 1.7981 1.2110 2.7522 0.4169  -0.3730 -0.2277 170 TYR   S CA  
33426 C  C   . TYR   S  171 ? 1.8072 1.1631 2.7080 0.4427  -0.3806 -0.1788 170 TYR   S C   
33427 O  O   . TYR   S  171 ? 1.8345 1.2197 2.7131 0.4163  -0.3955 -0.1323 170 TYR   S O   
33428 C  CB  . TYR   S  171 ? 1.7719 1.2250 2.7717 0.4460  -0.3440 -0.2184 170 TYR   S CB  
33429 C  CG  . TYR   S  171 ? 1.6953 1.2958 2.8236 0.4614  -0.3464 -0.1930 170 TYR   S CG  
33430 C  CD1 . TYR   S  171 ? 1.6903 1.3093 2.8265 0.4946  -0.3461 -0.1520 170 TYR   S CD1 
33431 C  CD2 . TYR   S  171 ? 1.6931 1.3310 2.8828 0.4807  -0.3761 -0.1831 170 TYR   S CD2 
33432 C  CE1 . TYR   S  171 ? 1.5997 1.4331 2.8838 0.4957  -0.3566 -0.1404 170 TYR   S CE1 
33433 C  CE2 . TYR   S  171 ? 1.6138 1.4466 2.9347 0.4818  -0.3814 -0.1531 170 TYR   S CE2 
33434 C  CZ  . TYR   S  171 ? 1.5829 1.4582 2.9479 0.4801  -0.3723 -0.1547 170 TYR   S CZ  
33435 O  OH  . TYR   S  171 ? 1.5728 1.6032 3.0463 0.4227  -0.3769 -0.1778 170 TYR   S OH  
33436 N  N   . LEU   S  172 ? 1.8088 1.1117 2.6120 0.4265  -0.3898 -0.1925 171 LEU   S N   
33437 C  CA  . LEU   S  172 ? 1.8063 1.1187 2.5650 0.4539  -0.3966 -0.1810 171 LEU   S CA  
33438 C  C   . LEU   S  172 ? 1.8270 1.0686 2.5807 0.4913  -0.4107 -0.1444 171 LEU   S C   
33439 O  O   . LEU   S  172 ? 1.8741 1.1785 2.6029 0.4145  -0.4483 -0.1368 171 LEU   S O   
33440 C  CB  . LEU   S  172 ? 1.7689 1.1555 2.4951 0.4370  -0.4061 -0.2191 171 LEU   S CB  
33441 C  CG  . LEU   S  172 ? 1.7505 1.2018 2.4514 0.4505  -0.3907 -0.2569 171 LEU   S CG  
33442 C  CD1 . LEU   S  172 ? 1.7547 1.1670 2.3885 0.4324  -0.4013 -0.2757 171 LEU   S CD1 
33443 C  CD2 . LEU   S  172 ? 1.7284 1.2013 2.4800 0.4622  -0.3752 -0.2610 171 LEU   S CD2 
33444 N  N   . GLU   S  173 ? 1.8241 0.9658 2.5486 0.5692  -0.4295 -0.1425 172 GLU   S N   
33445 C  CA  . GLU   S  173 ? 1.8435 0.9322 2.5666 0.5647  -0.4589 -0.0977 172 GLU   S CA  
33446 C  C   . GLU   S  173 ? 1.9239 0.9895 2.4891 0.5867  -0.5035 -0.0554 172 GLU   S C   
33447 O  O   . GLU   S  173 ? 1.9200 0.7761 2.4598 0.6210  -0.5538 0.0236  172 GLU   S O   
33448 C  CB  . GLU   S  173 ? 1.8465 0.9884 2.5894 0.5276  -0.4579 -0.1116 172 GLU   S CB  
33449 C  CG  . GLU   S  173 ? 1.8393 0.9854 2.5855 0.4719  -0.4733 -0.1227 172 GLU   S CG  
33450 C  CD  . GLU   S  173 ? 1.9065 0.9382 2.5613 0.4408  -0.4893 -0.1871 172 GLU   S CD  
33451 O  OE1 . GLU   S  173 ? 1.8595 0.9008 2.5781 0.4432  -0.4972 -0.1654 172 GLU   S OE1 
33452 O  OE2 . GLU   S  173 ? 1.9711 0.8592 2.6733 0.3498  -0.4914 -0.2529 172 GLU   S OE2 
33453 N  N   . ARG   S  174 ? 1.9569 1.1939 2.5616 0.6299  -0.4490 -0.0579 173 ARG   S N   
33454 C  CA  . ARG   S  174 ? 1.9540 1.3152 2.6206 0.6242  -0.4680 -0.0544 173 ARG   S CA  
33455 C  C   . ARG   S  174 ? 1.9171 1.3750 2.6159 0.5838  -0.4800 -0.0923 173 ARG   S C   
33456 O  O   . ARG   S  174 ? 1.9201 1.3524 2.6203 0.5568  -0.5046 0.0787  173 ARG   S O   
33457 C  CB  . ARG   S  174 ? 2.0038 1.4608 2.7106 0.7407  -0.4011 -0.0523 173 ARG   S CB  
33458 C  CG  . ARG   S  174 ? 2.0323 1.4766 2.7768 0.7457  -0.3841 -0.0100 173 ARG   S CG  
33459 C  CD  . ARG   S  174 ? 2.0709 1.5855 2.8358 0.8293  -0.3566 -0.0228 173 ARG   S CD  
33460 N  NE  . ARG   S  174 ? 2.0598 1.6652 2.8954 0.8826  -0.3612 0.0105  173 ARG   S NE  
33461 C  CZ  . ARG   S  174 ? 1.9740 1.6265 2.9062 0.9208  -0.3499 -0.0015 173 ARG   S CZ  
33462 N  NH1 . ARG   S  174 ? 2.0934 1.4891 2.8288 0.8912  -0.2895 0.0078  173 ARG   S NH1 
33463 N  NH2 . ARG   S  174 ? 1.9572 1.7092 2.9322 0.9392  -0.3365 0.0162  173 ARG   S NH2 
33464 N  N   . THR   S  175 ? 1.8823 1.3287 2.5803 0.5438  -0.4482 -0.1339 174 THR   S N   
33465 C  CA  . THR   S  175 ? 1.8362 1.3946 2.6152 0.5212  -0.3986 -0.1985 174 THR   S CA  
33466 C  C   . THR   S  175 ? 1.7748 1.3781 2.6513 0.5229  -0.4151 -0.2054 174 THR   S C   
33467 O  O   . THR   S  175 ? 1.7649 1.3025 2.6435 0.5766  -0.4366 -0.2657 174 THR   S O   
33468 C  CB  . THR   S  175 ? 1.8236 1.4172 2.5775 0.5089  -0.3468 -0.2519 174 THR   S CB  
33469 O  OG1 . THR   S  175 ? 1.7948 1.4424 2.5486 0.5274  -0.3308 -0.2657 174 THR   S OG1 
33470 C  CG2 . THR   S  175 ? 1.8483 1.4689 2.5806 0.4948  -0.2960 -0.2239 174 THR   S CG2 
33471 N  N   . LEU   S  176 ? 1.7600 1.3424 2.6307 0.5393  -0.4196 -0.2411 175 LEU   S N   
33472 C  CA  . LEU   S  176 ? 1.7620 1.2570 2.5968 0.4698  -0.4232 -0.2457 175 LEU   S CA  
33473 C  C   . LEU   S  176 ? 1.7204 1.3206 2.6002 0.4614  -0.4505 -0.2126 175 LEU   S C   
33474 O  O   . LEU   S  176 ? 1.7851 1.3289 2.6506 0.3583  -0.4173 -0.2042 175 LEU   S O   
33475 C  CB  . LEU   S  176 ? 1.7446 1.1904 2.5821 0.4830  -0.4154 -0.2910 175 LEU   S CB  
33476 C  CG  . LEU   S  176 ? 1.7341 1.1906 2.5548 0.4331  -0.4034 -0.3164 175 LEU   S CG  
33477 C  CD1 . LEU   S  176 ? 1.7080 1.2617 2.4939 0.4240  -0.4010 -0.3013 175 LEU   S CD1 
33478 C  CD2 . LEU   S  176 ? 1.7636 1.0911 2.5228 0.4400  -0.4089 -0.3239 175 LEU   S CD2 
33479 N  N   . ASP   S  177 ? 1.7284 1.2911 2.6095 0.4230  -0.4498 -0.1584 176 ASP   S N   
33480 C  CA  . ASP   S  177 ? 1.7163 1.2991 2.5622 0.4370  -0.4804 -0.0971 176 ASP   S CA  
33481 C  C   . ASP   S  177 ? 1.7074 1.2981 2.6042 0.4387  -0.5211 -0.0443 176 ASP   S C   
33482 O  O   . ASP   S  177 ? 1.7174 1.3365 2.5095 0.4641  -0.5867 -0.0497 176 ASP   S O   
33483 C  CB  . ASP   S  177 ? 1.6953 1.3059 2.5485 0.4166  -0.4458 -0.0726 176 ASP   S CB  
33484 C  CG  . ASP   S  177 ? 1.7312 1.2366 2.5339 0.4032  -0.4483 -0.0788 176 ASP   S CG  
33485 O  OD1 . ASP   S  177 ? 1.7318 1.2546 2.4635 0.3769  -0.4247 -0.0624 176 ASP   S OD1 
33486 O  OD2 . ASP   S  177 ? 1.6593 1.2277 2.5434 0.4507  -0.3885 -0.1091 176 ASP   S OD2 
33487 N  N   . THR   S  178 ? 1.7218 1.3267 2.6191 0.4702  -0.5204 -0.0436 177 THR   S N   
33488 C  CA  . THR   S  178 ? 1.6899 1.3792 2.6670 0.4534  -0.5248 -0.0365 177 THR   S CA  
33489 C  C   . THR   S  178 ? 1.7365 1.3556 2.6279 0.3827  -0.5136 0.0055  177 THR   S C   
33490 O  O   . THR   S  178 ? 1.9134 1.4159 2.6872 0.2468  -0.4588 0.0480  177 THR   S O   
33491 C  CB  . THR   S  178 ? 1.6054 1.3883 2.6800 0.4985  -0.5414 -0.0238 177 THR   S CB  
33492 O  OG1 . THR   S  178 ? 1.6267 1.3791 2.7482 0.4953  -0.5768 -0.0217 177 THR   S OG1 
33493 C  CG2 . THR   S  178 ? 1.5471 1.4245 2.6804 0.5172  -0.5388 -0.0455 177 THR   S CG2 
33494 N  N   . PHE   S  179 ? 1.6996 1.2898 2.5977 0.3750  -0.4837 -0.0049 178 PHE   S N   
33495 C  CA  . PHE   S  179 ? 1.6049 1.2656 2.5561 0.3669  -0.4956 -0.0445 178 PHE   S CA  
33496 C  C   . PHE   S  179 ? 1.5335 1.3434 2.4921 0.3673  -0.5174 -0.0677 178 PHE   S C   
33497 O  O   . PHE   S  179 ? 1.4926 1.3534 2.4972 0.3126  -0.4398 -0.0636 178 PHE   S O   
33498 C  CB  . PHE   S  179 ? 1.7144 1.1636 2.5512 0.3693  -0.4861 -0.0814 178 PHE   S CB  
33499 C  CG  . PHE   S  179 ? 1.7823 1.1007 2.5635 0.2921  -0.4857 -0.0861 178 PHE   S CG  
33500 C  CD1 . PHE   S  179 ? 1.8155 1.1121 2.5687 0.2993  -0.4836 -0.1170 178 PHE   S CD1 
33501 C  CD2 . PHE   S  179 ? 1.8530 1.0686 2.5801 0.3239  -0.5104 -0.1284 178 PHE   S CD2 
33502 C  CE1 . PHE   S  179 ? 1.8495 1.0342 2.5394 0.2464  -0.4865 -0.1257 178 PHE   S CE1 
33503 C  CE2 . PHE   S  179 ? 1.8638 1.0387 2.5470 0.2910  -0.5294 -0.1330 178 PHE   S CE2 
33504 C  CZ  . PHE   S  179 ? 1.8180 1.0276 2.5085 0.2537  -0.5110 -0.1294 178 PHE   S CZ  
33505 N  N   . ILE   S  180 ? 1.5387 1.2853 2.4246 0.4091  -0.5847 -0.0568 179 ILE   S N   
33506 C  CA  . ILE   S  180 ? 1.5427 1.3361 2.3414 0.3777  -0.5814 -0.0877 179 ILE   S CA  
33507 C  C   . ILE   S  180 ? 1.5044 1.4210 2.3723 0.3472  -0.6160 -0.0839 179 ILE   S C   
33508 O  O   . ILE   S  180 ? 1.3748 1.4077 2.3499 0.3217  -0.6527 -0.0646 179 ILE   S O   
33509 C  CB  . ILE   S  180 ? 1.5808 1.2823 2.2938 0.4250  -0.5903 -0.0796 179 ILE   S CB  
33510 C  CG1 . ILE   S  180 ? 1.5723 1.4206 2.2353 0.4068  -0.5253 -0.1019 179 ILE   S CG1 
33511 C  CG2 . ILE   S  180 ? 1.5932 1.1739 2.3079 0.4300  -0.5896 -0.0879 179 ILE   S CG2 
33512 C  CD1 . ILE   S  180 ? 1.5650 1.4679 2.2059 0.3969  -0.5133 -0.0917 179 ILE   S CD1 
33513 N  N   . LYS   S  181 ? 1.5033 1.4391 2.4533 0.3416  -0.6220 -0.0785 180 LYS   S N   
33514 C  CA  . LYS   S  181 ? 1.5402 1.4781 2.4955 0.2825  -0.5970 -0.0631 180 LYS   S CA  
33515 C  C   . LYS   S  181 ? 1.5008 1.4819 2.5259 0.3028  -0.5522 -0.1130 180 LYS   S C   
33516 O  O   . LYS   S  181 ? 1.4533 1.5471 2.6306 0.3011  -0.5192 -0.0719 180 LYS   S O   
33517 C  CB  . LYS   S  181 ? 1.5682 1.5005 2.5181 0.2551  -0.6290 -0.0413 180 LYS   S CB  
33518 C  CG  . LYS   S  181 ? 1.5832 1.4893 2.4650 0.2267  -0.6796 -0.0145 180 LYS   S CG  
33519 C  CD  . LYS   S  181 ? 1.5932 1.4873 2.4898 0.2022  -0.7025 0.0026  180 LYS   S CD  
33520 C  CE  . LYS   S  181 ? 1.6047 1.5031 2.5254 0.1983  -0.6977 -0.0223 180 LYS   S CE  
33521 N  NZ  . LYS   S  181 ? 1.6398 1.5372 2.5432 0.1839  -0.7142 -0.0021 180 LYS   S NZ  
33522 N  N   . ILE   S  182 ? 1.5140 1.4153 2.4874 0.3206  -0.4939 -0.2109 181 ILE   S N   
33523 C  CA  . ILE   S  182 ? 1.4771 1.4223 2.4545 0.3306  -0.4534 -0.2766 181 ILE   S CA  
33524 C  C   . ILE   S  182 ? 1.5088 1.3931 2.4018 0.3016  -0.4589 -0.2838 181 ILE   S C   
33525 O  O   . ILE   S  182 ? 1.5039 1.3516 2.3209 0.3104  -0.4450 -0.3731 181 ILE   S O   
33526 C  CB  . ILE   S  182 ? 1.4437 1.4049 2.4850 0.3555  -0.4228 -0.3106 181 ILE   S CB  
33527 C  CG1 . ILE   S  182 ? 1.4709 1.4330 2.5406 0.3882  -0.4226 -0.2926 181 ILE   S CG1 
33528 C  CG2 . ILE   S  182 ? 1.3975 1.4051 2.4754 0.3772  -0.4084 -0.3316 181 ILE   S CG2 
33529 C  CD1 . ILE   S  182 ? 1.5003 1.5086 2.5429 0.4003  -0.3953 -0.3260 181 ILE   S CD1 
33530 N  N   . ASP   S  183 ? 1.4962 1.3190 2.4498 0.2879  -0.4626 -0.2655 182 ASP   S N   
33531 C  CA  . ASP   S  183 ? 1.4742 1.2937 2.4166 0.2613  -0.4461 -0.2247 182 ASP   S CA  
33532 C  C   . ASP   S  183 ? 1.4381 1.2519 2.5020 0.2948  -0.4430 -0.1843 182 ASP   S C   
33533 O  O   . ASP   S  183 ? 1.4923 1.0473 2.4885 0.4097  -0.4811 -0.1185 182 ASP   S O   
33534 C  CB  . ASP   S  183 ? 1.4550 1.3641 2.4181 0.2406  -0.4664 -0.2606 182 ASP   S CB  
33535 C  CG  . ASP   S  183 ? 1.3817 1.3830 2.3520 0.2091  -0.4873 -0.3437 182 ASP   S CG  
33536 O  OD1 . ASP   S  183 ? 1.2801 1.3929 2.3759 0.2314  -0.4451 -0.3250 182 ASP   S OD1 
33537 O  OD2 . ASP   S  183 ? 1.4560 1.4306 2.3017 0.1996  -0.4213 -0.4007 182 ASP   S OD2 
33538 N  N   . GLY   S  184 ? 1.5618 1.2152 2.4916 0.1637  -0.3851 -0.0827 183 GLY   S N   
33539 C  CA  . GLY   S  184 ? 1.5889 1.2929 2.5435 0.0928  -0.3409 -0.1138 183 GLY   S CA  
33540 C  C   . GLY   S  184 ? 1.6145 1.1991 2.6109 0.0619  -0.3149 -0.1526 183 GLY   S C   
33541 O  O   . GLY   S  184 ? 1.5898 1.3582 2.6701 0.0765  -0.2584 -0.1679 183 GLY   S O   
33542 N  N   . ASN   S  185 ? 1.6416 1.1011 2.6575 0.0796  -0.2927 -0.1218 184 ASN   S N   
33543 C  CA  . ASN   S  185 ? 1.6141 1.1311 2.6468 0.0170  -0.3152 -0.1619 184 ASN   S CA  
33544 C  C   . ASN   S  185 ? 1.7082 1.1679 2.6241 0.0342  -0.3715 -0.1811 184 ASN   S C   
33545 O  O   . ASN   S  185 ? 1.7144 1.2074 2.6039 -0.0242 -0.4494 -0.1825 184 ASN   S O   
33546 C  CB  . ASN   S  185 ? 1.5727 1.1636 2.7001 0.0129  -0.2913 -0.1349 184 ASN   S CB  
33547 C  CG  . ASN   S  185 ? 1.5587 1.1401 2.7402 -0.0165 -0.2647 -0.1333 184 ASN   S CG  
33548 O  OD1 . ASN   S  185 ? 1.5372 1.1576 2.8071 -0.0134 -0.2447 -0.1018 184 ASN   S OD1 
33549 N  ND2 . ASN   S  185 ? 1.5616 1.0976 2.7176 -0.0677 -0.2345 -0.1576 184 ASN   S ND2 
33550 N  N   . PRO   S  186 ? 1.7848 1.1264 2.6160 0.0354  -0.3474 -0.1799 185 PRO   S N   
33551 C  CA  . PRO   S  186 ? 1.7676 1.1917 2.6232 0.0587  -0.3570 -0.1540 185 PRO   S CA  
33552 C  C   . PRO   S  186 ? 1.7670 1.3388 2.7143 0.2176  -0.2596 -0.1615 185 PRO   S C   
33553 O  O   . PRO   S  186 ? 1.7349 1.3447 2.7310 0.2313  -0.2813 -0.1683 185 PRO   S O   
33554 C  CB  . PRO   S  186 ? 1.7776 1.1164 2.5935 0.0414  -0.3319 -0.2023 185 PRO   S CB  
33555 C  CG  . PRO   S  186 ? 1.7660 1.1398 2.5392 0.0435  -0.3359 -0.2000 185 PRO   S CG  
33556 C  CD  . PRO   S  186 ? 1.7444 1.1379 2.5652 0.0124  -0.3498 -0.2004 185 PRO   S CD  
33557 N  N   . ASP   S  187 ? 1.7564 1.4276 2.8182 0.2656  -0.2316 -0.1148 186 ASP   S N   
33558 C  CA  . ASP   S  187 ? 1.7490 1.5057 2.8363 0.2696  -0.1978 -0.1452 186 ASP   S CA  
33559 C  C   . ASP   S  187 ? 1.8498 1.5120 2.8084 0.2908  -0.2445 -0.1573 186 ASP   S C   
33560 O  O   . ASP   S  187 ? 1.9360 1.6323 2.8558 0.2585  -0.2830 -0.2494 186 ASP   S O   
33561 C  CB  . ASP   S  187 ? 1.7565 1.5175 2.8895 0.2701  -0.1614 -0.1617 186 ASP   S CB  
33562 C  CG  . ASP   S  187 ? 1.6628 1.5020 2.8526 0.2673  -0.1110 -0.1858 186 ASP   S CG  
33563 O  OD1 . ASP   S  187 ? 1.5970 1.4318 2.8596 0.2034  -0.1599 -0.1736 186 ASP   S OD1 
33564 O  OD2 . ASP   S  187 ? 1.7051 1.6105 2.9236 0.2659  -0.0444 -0.2676 186 ASP   S OD2 
33565 N  N   . GLU   S  188 ? 1.8452 1.5226 2.8086 0.3112  -0.2447 -0.0814 187 GLU   S N   
33566 C  CA  . GLU   S  188 ? 1.7354 1.5194 2.7467 0.3158  -0.2544 -0.0955 187 GLU   S CA  
33567 C  C   . GLU   S  188 ? 1.7166 1.3223 2.6317 0.3476  -0.3056 -0.1194 187 GLU   S C   
33568 O  O   . GLU   S  188 ? 1.7142 1.3296 2.6294 0.3102  -0.3582 -0.1230 187 GLU   S O   
33569 C  CB  . GLU   S  188 ? 1.6229 1.5869 2.7373 0.3161  -0.2309 -0.0356 187 GLU   S CB  
33570 C  CG  . GLU   S  188 ? 1.6223 1.6700 2.7552 0.3073  -0.1861 -0.0225 187 GLU   S CG  
33571 C  CD  . GLU   S  188 ? 1.5141 1.7058 2.7839 0.3286  -0.1067 0.0025  187 GLU   S CD  
33572 O  OE1 . GLU   S  188 ? 1.5930 1.8207 2.8333 0.3081  -0.0451 0.0102  187 GLU   S OE1 
33573 O  OE2 . GLU   S  188 ? 1.3713 1.6626 2.7908 0.4185  -0.1211 0.0247  187 GLU   S OE2 
33574 N  N   . LEU   S  189 ? 1.6934 1.2775 2.5050 0.3060  -0.3228 -0.1663 188 LEU   S N   
33575 C  CA  . LEU   S  189 ? 1.7000 1.1837 2.4046 0.3061  -0.3336 -0.2018 188 LEU   S CA  
33576 C  C   . LEU   S  189 ? 1.7283 1.2135 2.4314 0.3127  -0.3420 -0.2379 188 LEU   S C   
33577 O  O   . LEU   S  189 ? 1.7265 1.1828 2.3687 0.3403  -0.3209 -0.1935 188 LEU   S O   
33578 C  CB  . LEU   S  189 ? 1.6796 1.1630 2.2779 0.2686  -0.3252 -0.2017 188 LEU   S CB  
33579 C  CG  . LEU   S  189 ? 1.6619 1.0845 2.2469 0.2536  -0.3512 -0.1929 188 LEU   S CG  
33580 C  CD1 . LEU   S  189 ? 1.6461 1.1166 2.1697 0.2634  -0.3436 -0.1668 188 LEU   S CD1 
33581 C  CD2 . LEU   S  189 ? 1.6589 1.0592 2.2121 0.2737  -0.3458 -0.1989 188 LEU   S CD2 
33582 N  N   . ILE   S  190 ? 1.7251 1.2821 2.4449 0.3006  -0.3040 -0.2478 189 ILE   S N   
33583 C  CA  . ILE   S  190 ? 1.7235 1.3661 2.4745 0.2837  -0.3098 -0.2861 189 ILE   S CA  
33584 C  C   . ILE   S  190 ? 1.7536 1.4023 2.5778 0.3206  -0.3178 -0.2904 189 ILE   S C   
33585 O  O   . ILE   S  190 ? 1.7775 1.4911 2.6437 0.2771  -0.3439 -0.3171 189 ILE   S O   
33586 C  CB  . ILE   S  190 ? 1.6834 1.3725 2.4367 0.2768  -0.2708 -0.3176 189 ILE   S CB  
33587 C  CG1 . ILE   S  190 ? 1.6689 1.3294 2.3939 0.2361  -0.2671 -0.3037 189 ILE   S CG1 
33588 C  CG2 . ILE   S  190 ? 1.6763 1.4085 2.4187 0.2969  -0.2368 -0.3273 189 ILE   S CG2 
33589 C  CD1 . ILE   S  190 ? 1.6557 1.3810 2.3713 0.2199  -0.2495 -0.2948 189 ILE   S CD1 
33590 N  N   . LYS   S  191 ? 1.7611 1.3956 2.5928 0.3016  -0.3574 -0.2884 190 LYS   S N   
33591 C  CA  . LYS   S  191 ? 1.7586 1.3764 2.5672 0.2906  -0.3926 -0.3335 190 LYS   S CA  
33592 C  C   . LYS   S  191 ? 1.7735 1.2886 2.6171 0.3046  -0.4448 -0.3432 190 LYS   S C   
33593 O  O   . LYS   S  191 ? 1.8167 1.3278 2.5935 0.3014  -0.4790 -0.3707 190 LYS   S O   
33594 C  CB  . LYS   S  191 ? 1.7403 1.3431 2.5372 0.2777  -0.3603 -0.3259 190 LYS   S CB  
33595 C  CG  . LYS   S  191 ? 1.7296 1.3359 2.5328 0.2570  -0.3511 -0.3659 190 LYS   S CG  
33596 C  CD  . LYS   S  191 ? 1.7350 1.3363 2.5575 0.2234  -0.3519 -0.3661 190 LYS   S CD  
33597 C  CE  . LYS   S  191 ? 1.7593 1.3406 2.5623 0.1895  -0.3385 -0.3901 190 LYS   S CE  
33598 N  NZ  . LYS   S  191 ? 1.7662 1.3339 2.6011 0.1629  -0.3420 -0.4007 190 LYS   S NZ  
33599 N  N   . ALA   S  192 ? 1.7268 1.2813 2.6351 0.3141  -0.4604 -0.3726 191 ALA   S N   
33600 C  CA  . ALA   S  192 ? 1.6994 1.2450 2.7000 0.2884  -0.4546 -0.3985 191 ALA   S CA  
33601 C  C   . ALA   S  192 ? 1.6904 1.2277 2.7090 0.2863  -0.4362 -0.4172 191 ALA   S C   
33602 O  O   . ALA   S  192 ? 1.7745 1.2998 2.7934 0.1715  -0.3998 -0.3913 191 ALA   S O   
33603 C  CB  . ALA   S  192 ? 1.6703 1.2583 2.6763 0.2937  -0.4824 -0.3797 191 ALA   S CB  
33604 N  N   . GLY   S  193 ? 1.6810 1.1395 2.7074 0.2922  -0.3817 -0.4513 192 GLY   S N   
33605 C  CA  . GLY   S  193 ? 1.6406 1.1269 2.6944 0.3513  -0.3543 -0.4695 192 GLY   S CA  
33606 C  C   . GLY   S  193 ? 1.6496 1.1924 2.7266 0.3918  -0.3012 -0.5006 192 GLY   S C   
33607 O  O   . GLY   S  193 ? 1.5318 1.3466 2.7782 0.4310  -0.3780 -0.5090 192 GLY   S O   
33608 N  N   . VAL   S  194 ? 1.7312 1.2234 2.7336 0.3913  -0.2292 -0.5054 193 VAL   S N   
33609 C  CA  . VAL   S  194 ? 1.7753 1.2727 2.7262 0.4035  -0.1657 -0.4811 193 VAL   S CA  
33610 C  C   . VAL   S  194 ? 1.7943 1.2713 2.7341 0.4584  -0.1457 -0.5436 193 VAL   S C   
33611 O  O   . VAL   S  194 ? 1.8007 1.1500 2.7748 0.5581  -0.0866 -0.5674 193 VAL   S O   
33612 C  CB  . VAL   S  194 ? 1.8236 1.2606 2.7017 0.4037  -0.1451 -0.4750 193 VAL   S CB  
33613 C  CG1 . VAL   S  194 ? 1.8481 1.3033 2.7313 0.4067  -0.1095 -0.4976 193 VAL   S CG1 
33614 C  CG2 . VAL   S  194 ? 1.8028 1.2470 2.6564 0.3808  -0.1383 -0.4638 193 VAL   S CG2 
33615 N  N   . GLU   S  195 ? 1.7747 1.3361 2.7606 0.4843  -0.1411 -0.4912 194 GLU   S N   
33616 C  CA  . GLU   S  195 ? 1.8104 1.3913 2.7631 0.4726  -0.1541 -0.4092 194 GLU   S CA  
33617 C  C   . GLU   S  195 ? 1.7894 1.3623 2.7410 0.4902  -0.1655 -0.4196 194 GLU   S C   
33618 O  O   . GLU   S  195 ? 1.8419 1.3629 2.8080 0.4756  -0.1648 -0.4312 194 GLU   S O   
33619 C  CB  . GLU   S  195 ? 1.8450 1.5759 2.7702 0.4144  -0.1739 -0.3514 194 GLU   S CB  
33620 C  CG  . GLU   S  195 ? 1.9349 1.6242 2.8282 0.4159  -0.1705 -0.2706 194 GLU   S CG  
33621 C  CD  . GLU   S  195 ? 1.9491 1.8083 2.8722 0.3843  -0.1820 -0.2279 194 GLU   S CD  
33622 O  OE1 . GLU   S  195 ? 2.0614 1.8891 2.9166 0.3570  -0.1682 -0.1538 194 GLU   S OE1 
33623 O  OE2 . GLU   S  195 ? 2.0452 1.9798 2.9334 0.3745  -0.0870 -0.1730 194 GLU   S OE2 
33624 N  N   . ALA   S  196 ? 1.7628 1.3180 2.6879 0.4837  -0.2051 -0.4083 195 ALA   S N   
33625 C  CA  . ALA   S  196 ? 1.7604 1.3202 2.6706 0.4459  -0.2590 -0.3977 195 ALA   S CA  
33626 C  C   . ALA   S  196 ? 1.7658 1.2179 2.6837 0.4452  -0.2414 -0.4150 195 ALA   S C   
33627 O  O   . ALA   S  196 ? 1.8310 1.1697 2.6978 0.4935  -0.2220 -0.4266 195 ALA   S O   
33628 C  CB  . ALA   S  196 ? 1.7081 1.3391 2.5809 0.4178  -0.2765 -0.3928 195 ALA   S CB  
33629 N  N   . ILE   S  197 ? 1.7451 1.2022 2.6988 0.4385  -0.2259 -0.4071 196 ILE   S N   
33630 C  CA  . ILE   S  197 ? 1.7506 1.1580 2.7015 0.4222  -0.2315 -0.3818 196 ILE   S CA  
33631 C  C   . ILE   S  197 ? 1.7488 1.2085 2.7598 0.4340  -0.1791 -0.3890 196 ILE   S C   
33632 O  O   . ILE   S  197 ? 1.7790 1.2876 2.7958 0.3848  -0.1875 -0.3988 196 ILE   S O   
33633 C  CB  . ILE   S  197 ? 1.7357 1.1180 2.6912 0.3842  -0.2343 -0.3919 196 ILE   S CB  
33634 C  CG1 . ILE   S  197 ? 1.8121 1.1429 2.6741 0.3200  -0.2698 -0.3804 196 ILE   S CG1 
33635 C  CG2 . ILE   S  197 ? 1.7163 1.0871 2.7142 0.4410  -0.2038 -0.4017 196 ILE   S CG2 
33636 C  CD1 . ILE   S  197 ? 1.7986 1.1624 2.6115 0.2849  -0.3035 -0.3592 196 ILE   S CD1 
33637 N  N   . SER   S  198 ? 1.7488 1.1560 2.7547 0.4532  -0.1693 -0.3559 197 SER   S N   
33638 C  CA  . SER   S  198 ? 1.7487 1.1787 2.7716 0.4730  -0.1639 -0.3579 197 SER   S CA  
33639 C  C   . SER   S  198 ? 1.8382 1.1771 2.7946 0.4484  -0.1869 -0.3700 197 SER   S C   
33640 O  O   . SER   S  198 ? 1.9125 1.2228 2.7823 0.3850  -0.1413 -0.4151 197 SER   S O   
33641 C  CB  . SER   S  198 ? 1.7333 1.1375 2.7884 0.4921  -0.1243 -0.3547 197 SER   S CB  
33642 O  OG  . SER   S  198 ? 1.6567 1.1549 2.7495 0.5259  -0.1071 -0.3418 197 SER   S OG  
33643 N  N   . GLN   S  199 ? 1.8463 1.2011 2.7507 0.4496  -0.2392 -0.3524 198 GLN   S N   
33644 C  CA  . GLN   S  199 ? 1.8689 1.1678 2.7548 0.4601  -0.3070 -0.3548 198 GLN   S CA  
33645 C  C   . GLN   S  199 ? 1.8843 1.1023 2.7095 0.4907  -0.3425 -0.3382 198 GLN   S C   
33646 O  O   . GLN   S  199 ? 1.8772 1.1821 2.6864 0.3706  -0.3799 -0.3535 198 GLN   S O   
33647 C  CB  . GLN   S  199 ? 1.8434 1.1675 2.7413 0.4477  -0.3429 -0.3315 198 GLN   S CB  
33648 C  CG  . GLN   S  199 ? 1.8118 1.2262 2.7310 0.4629  -0.3470 -0.3204 198 GLN   S CG  
33649 C  CD  . GLN   S  199 ? 1.8244 1.2152 2.7818 0.4776  -0.3530 -0.3561 198 GLN   S CD  
33650 O  OE1 . GLN   S  199 ? 1.8048 1.2038 2.7689 0.4464  -0.3176 -0.3705 198 GLN   S OE1 
33651 N  NE2 . GLN   S  199 ? 1.7672 1.2852 2.8010 0.4938  -0.3382 -0.3534 198 GLN   S NE2 
33652 N  N   . SER   S  200 ? 1.9111 1.0814 2.6969 0.5383  -0.3382 -0.3710 199 SER   S N   
33653 C  CA  . SER   S  200 ? 1.9454 1.0352 2.6202 0.5620  -0.3631 -0.3511 199 SER   S CA  
33654 C  C   . SER   S  200 ? 1.9739 0.9818 2.6232 0.5805  -0.3210 -0.3524 199 SER   S C   
33655 O  O   . SER   S  200 ? 2.0209 0.7852 2.5222 0.6116  -0.3285 -0.3748 199 SER   S O   
33656 C  CB  . SER   S  200 ? 1.9350 1.0451 2.5785 0.5809  -0.3909 -0.3104 199 SER   S CB  
33657 O  OG  . SER   S  200 ? 1.9217 1.0779 2.5665 0.6021  -0.4118 -0.2840 199 SER   S OG  
33658 N  N   . LEU   S  201 ? 1.9870 1.0564 2.6518 0.5473  -0.2986 -0.3193 200 LEU   S N   
33659 C  CA  . LEU   S  201 ? 2.0224 1.2201 2.6539 0.4670  -0.2727 -0.2972 200 LEU   S CA  
33660 C  C   . LEU   S  201 ? 2.0740 1.2566 2.6622 0.4379  -0.2763 -0.3607 200 LEU   S C   
33661 O  O   . LEU   S  201 ? 2.0677 1.3920 2.7201 0.4150  -0.2908 -0.2664 200 LEU   S O   
33662 C  CB  . LEU   S  201 ? 2.0412 1.2063 2.6987 0.4620  -0.2484 -0.2886 200 LEU   S CB  
33663 C  CG  . LEU   S  201 ? 2.0177 1.2145 2.6669 0.4183  -0.2201 -0.3039 200 LEU   S CG  
33664 C  CD1 . LEU   S  201 ? 2.0114 1.2547 2.6942 0.4204  -0.2119 -0.3012 200 LEU   S CD1 
33665 C  CD2 . LEU   S  201 ? 1.9620 1.1910 2.6283 0.4048  -0.1963 -0.3304 200 LEU   S CD2 
33666 N  N   . ARG   S  202 ? 2.1561 1.3376 2.6478 0.3987  -0.2293 -0.4216 201 ARG   S N   
33667 C  CA  . ARG   S  202 ? 2.2804 1.3627 2.6972 0.4108  -0.1857 -0.4694 201 ARG   S CA  
33668 C  C   . ARG   S  202 ? 2.2890 1.3004 2.7168 0.4245  -0.1058 -0.5595 201 ARG   S C   
33669 O  O   . ARG   S  202 ? 2.2200 1.1781 2.7263 0.5040  -0.0518 -0.6739 201 ARG   S O   
33670 C  CB  . ARG   S  202 ? 2.3918 1.3493 2.6014 0.3312  -0.2183 -0.4551 201 ARG   S CB  
33671 C  CG  . ARG   S  202 ? 2.4932 1.4887 2.5797 0.2604  -0.2866 -0.4479 201 ARG   S CG  
33672 C  CD  . ARG   S  202 ? 2.6085 1.4919 2.5268 0.2216  -0.3030 -0.4330 201 ARG   S CD  
33673 N  NE  . ARG   S  202 ? 2.7077 1.5973 2.4121 0.1333  -0.3252 -0.4582 201 ARG   S NE  
33674 C  CZ  . ARG   S  202 ? 2.7688 1.6914 2.3360 0.1003  -0.3457 -0.3957 201 ARG   S CZ  
33675 N  NH1 . ARG   S  202 ? 2.7500 1.7714 2.2811 0.0727  -0.3548 -0.3493 201 ARG   S NH1 
33676 N  NH2 . ARG   S  202 ? 2.8097 1.6427 2.2848 0.1013  -0.3403 -0.4128 201 ARG   S NH2 
33677 N  N   . ASP   S  203 ? 2.2860 1.4062 2.8558 0.3928  -0.0509 -0.5736 202 ASP   S N   
33678 C  CA  . ASP   S  203 ? 2.3979 1.5658 2.8731 0.2742  0.0012  -0.5003 202 ASP   S CA  
33679 C  C   . ASP   S  203 ? 2.3291 1.5122 2.7746 0.2357  0.0047  -0.5984 202 ASP   S C   
33680 O  O   . ASP   S  203 ? 2.4134 1.5771 2.7639 0.0567  0.0126  -0.5786 202 ASP   S O   
33681 C  CB  . ASP   S  203 ? 2.3898 1.6653 2.9369 0.2135  -0.0062 -0.4703 202 ASP   S CB  
33682 C  CG  . ASP   S  203 ? 2.4442 1.6634 3.0573 0.2390  0.0518  -0.4576 202 ASP   S CG  
33683 O  OD1 . ASP   S  203 ? 2.4424 1.7938 3.1459 0.1437  0.0316  -0.2948 202 ASP   S OD1 
33684 O  OD2 . ASP   S  203 ? 2.4378 1.7285 3.0922 0.3150  0.1776  -0.4541 202 ASP   S OD2 
33685 N  N   . GLU   S  204 ? 2.2494 1.4712 2.7410 0.2456  -0.0323 -0.5482 203 GLU   S N   
33686 C  CA  . GLU   S  204 ? 2.2288 1.4969 2.7237 0.2462  -0.0395 -0.5093 203 GLU   S CA  
33687 C  C   . GLU   S  204 ? 2.3170 1.4292 2.7563 0.2573  -0.0543 -0.5457 203 GLU   S C   
33688 O  O   . GLU   S  204 ? 2.3081 1.1650 2.7949 0.2723  -0.0629 -0.5208 203 GLU   S O   
33689 C  CB  . GLU   S  204 ? 2.1821 1.5649 2.6453 0.2117  -0.0835 -0.4680 203 GLU   S CB  
33690 C  CG  . GLU   S  204 ? 2.1067 1.6172 2.5726 0.2240  -0.0885 -0.4396 203 GLU   S CG  
33691 C  CD  . GLU   S  204 ? 2.0802 1.6278 2.4643 0.2080  -0.0952 -0.3967 203 GLU   S CD  
33692 O  OE1 . GLU   S  204 ? 2.0479 1.6333 2.3706 0.1724  -0.0332 -0.4250 203 GLU   S OE1 
33693 O  OE2 . GLU   S  204 ? 1.9824 1.6340 2.4662 0.2660  -0.1332 -0.3764 203 GLU   S OE2 
33694 N  N   . SER   S  205 ? 2.4137 1.4419 2.7442 0.2363  0.0098  -0.5609 204 SER   S N   
33695 C  CA  . SER   S  205 ? 2.4602 1.4712 2.7092 0.2502  -0.0197 -0.5531 204 SER   S CA  
33696 C  C   . SER   S  205 ? 2.4880 1.4672 2.6179 0.2300  -0.0466 -0.5370 204 SER   S C   
33697 O  O   . SER   S  205 ? 2.5873 1.5573 2.6136 0.2307  -0.0172 -0.4224 204 SER   S O   
33698 C  CB  . SER   S  205 ? 2.4762 1.5354 2.7183 0.2607  0.0329  -0.5710 204 SER   S CB  
33699 O  OG  . SER   S  205 ? 2.5048 1.5273 2.7293 0.2348  0.0845  -0.6410 204 SER   S OG  
33700 N  N   . LEU   S  206 ? 2.4039 1.3745 2.6009 0.3021  -0.0957 -0.4959 205 LEU   S N   
33701 C  CA  . LEU   S  206 ? 2.2572 1.3609 2.4773 0.2855  -0.1265 -0.5480 205 LEU   S CA  
33702 C  C   . LEU   S  206 ? 2.2684 1.2926 2.4282 0.2626  -0.1295 -0.6072 205 LEU   S C   
33703 O  O   . LEU   S  206 ? 2.2663 1.2568 2.3219 0.2605  -0.1191 -0.6564 205 LEU   S O   
33704 C  CB  . LEU   S  206 ? 2.1700 1.2621 2.5110 0.3753  -0.1715 -0.5505 205 LEU   S CB  
33705 C  CG  . LEU   S  206 ? 2.1058 1.2043 2.5600 0.4200  -0.1788 -0.5135 205 LEU   S CG  
33706 C  CD1 . LEU   S  206 ? 2.0700 1.1958 2.5689 0.4465  -0.1982 -0.5058 205 LEU   S CD1 
33707 C  CD2 . LEU   S  206 ? 2.1091 1.1041 2.5271 0.4268  -0.2081 -0.5145 205 LEU   S CD2 
33708 N  N   . THR   S  207 ? 2.2328 1.2780 2.3944 0.2321  -0.1077 -0.6112 206 THR   S N   
33709 C  CA  . THR   S  207 ? 2.2070 1.3679 2.3676 0.2104  -0.0767 -0.6422 206 THR   S CA  
33710 C  C   . THR   S  207 ? 2.2124 1.3564 2.3204 0.1706  -0.0324 -0.6439 206 THR   S C   
33711 O  O   . THR   S  207 ? 2.1876 1.3653 2.3337 0.1543  -0.0358 -0.6860 206 THR   S O   
33712 C  CB  . THR   S  207 ? 2.1749 1.4224 2.3592 0.2124  -0.0729 -0.6454 206 THR   S CB  
33713 O  OG1 . THR   S  207 ? 2.1460 1.4604 2.2622 0.1821  -0.0951 -0.6896 206 THR   S OG1 
33714 C  CG2 . THR   S  207 ? 2.1992 1.4247 2.3661 0.2090  -0.0974 -0.6284 206 THR   S CG2 
33715 N  N   . VAL   S  208 ? 2.2799 1.4255 2.3591 0.1368  -0.0155 -0.6047 207 VAL   S N   
33716 C  CA  . VAL   S  208 ? 2.2375 1.4194 2.3102 0.1588  0.0097  -0.5570 207 VAL   S CA  
33717 C  C   . VAL   S  208 ? 2.2301 1.3149 2.2442 0.1690  0.0415  -0.5781 207 VAL   S C   
33718 O  O   . VAL   S  208 ? 2.2363 1.2438 2.2219 0.1754  0.0004  -0.5180 207 VAL   S O   
33719 C  CB  . VAL   S  208 ? 2.3149 1.4872 2.3223 0.1260  0.0296  -0.5182 207 VAL   S CB  
33720 C  CG1 . VAL   S  208 ? 2.3518 1.4866 2.2846 0.0697  0.0543  -0.5370 207 VAL   S CG1 
33721 C  CG2 . VAL   S  208 ? 2.2658 1.4508 2.3006 0.1547  0.0447  -0.4950 207 VAL   S CG2 
33722 N  N   . ASP   S  209 ? 2.1344 1.3566 2.2676 0.1607  0.0433  -0.5444 208 ASP   S N   
33723 C  CA  . ASP   S  209 ? 2.1075 1.3319 2.2698 0.1361  0.0735  -0.5113 208 ASP   S CA  
33724 C  C   . ASP   S  209 ? 2.1001 1.3051 2.3243 0.1204  0.0242  -0.4821 208 ASP   S C   
33725 O  O   . ASP   S  209 ? 2.1031 1.1831 2.3372 0.1507  0.0057  -0.4151 208 ASP   S O   
33726 C  CB  . ASP   S  209 ? 2.0902 1.3208 2.2445 0.1412  0.1615  -0.5288 208 ASP   S CB  
33727 C  CG  . ASP   S  209 ? 2.1614 1.2671 2.2751 0.1051  0.2018  -0.5473 208 ASP   S CG  
33728 O  OD1 . ASP   S  209 ? 2.1851 1.2342 2.2649 0.0438  0.2361  -0.5952 208 ASP   S OD1 
33729 O  OD2 . ASP   S  209 ? 2.2085 1.3173 2.3009 0.1370  0.2660  -0.5654 208 ASP   S OD2 
33730 N  N   . ASN   S  210 ? 2.1920 1.3820 2.3373 0.0905  -0.0147 -0.4605 209 ASN   S N   
33731 C  CA  . ASN   S  210 ? 2.2528 1.5330 2.4423 -0.0265 0.0406  -0.4664 209 ASN   S CA  
33732 C  C   . ASN   S  210 ? 2.1973 1.4970 2.4611 -0.0549 -0.0584 -0.5375 209 ASN   S C   
33733 O  O   . ASN   S  210 ? 2.1502 1.5309 2.4647 -0.0963 -0.1209 -0.5403 209 ASN   S O   
33734 C  CB  . ASN   S  210 ? 2.3317 1.6255 2.5767 0.0519  0.1101  -0.4536 209 ASN   S CB  
33735 C  CG  . ASN   S  210 ? 2.3988 1.6901 2.6591 0.0811  0.1341  -0.3357 209 ASN   S CG  
33736 O  OD1 . ASN   S  210 ? 2.4167 1.8523 2.7592 -0.0458 0.1872  -0.2967 209 ASN   S OD1 
33737 N  ND2 . ASN   S  210 ? 2.3485 1.7992 2.7429 0.1641  0.1737  -0.3112 209 ASN   S ND2 
33738 N  N   . LEU   S  211 ? 2.1634 1.4888 2.4533 -0.0286 -0.0510 -0.5527 210 LEU   S N   
33739 C  CA  . LEU   S  211 ? 2.0675 1.3806 2.4592 0.0450  -0.0391 -0.5673 210 LEU   S CA  
33740 C  C   . LEU   S  211 ? 1.9196 1.4163 2.3569 0.0786  -0.0519 -0.5588 210 LEU   S C   
33741 O  O   . LEU   S  211 ? 1.7556 1.3655 2.3111 0.0408  -0.0198 -0.6389 210 LEU   S O   
33742 C  CB  . LEU   S  211 ? 2.0761 1.4608 2.4668 -0.0427 -0.0562 -0.5916 210 LEU   S CB  
33743 C  CG  . LEU   S  211 ? 2.1012 1.4336 2.4778 -0.0713 -0.0601 -0.6189 210 LEU   S CG  
33744 C  CD1 . LEU   S  211 ? 2.1220 1.3840 2.4450 -0.0780 -0.0838 -0.6421 210 LEU   S CD1 
33745 C  CD2 . LEU   S  211 ? 2.1008 1.4884 2.5094 -0.0861 -0.0620 -0.6105 210 LEU   S CD2 
33746 N  N   . SER   S  212 ? 1.8671 1.3504 2.3474 0.2072  -0.0996 -0.5483 211 SER   S N   
33747 C  CA  . SER   S  212 ? 1.8347 1.3372 2.3167 0.2383  -0.1356 -0.5012 211 SER   S CA  
33748 C  C   . SER   S  212 ? 1.8008 1.3076 2.2960 0.3393  -0.1078 -0.4694 211 SER   S C   
33749 O  O   . SER   S  212 ? 1.8191 1.1962 2.2683 0.4213  -0.1007 -0.4987 211 SER   S O   
33750 C  CB  . SER   S  212 ? 1.8437 1.2625 2.2828 0.2593  -0.1503 -0.5162 211 SER   S CB  
33751 O  OG  . SER   S  212 ? 1.8912 1.2467 2.2622 0.2356  -0.1506 -0.4863 211 SER   S OG  
33752 N  N   . ILE   S  213 ? 1.7527 1.2998 2.2811 0.3484  -0.0992 -0.4360 212 ILE   S N   
33753 C  CA  . ILE   S  213 ? 1.7061 1.3415 2.2627 0.3514  -0.1324 -0.3673 212 ILE   S CA  
33754 C  C   . ILE   S  213 ? 1.7409 1.3136 2.2453 0.3381  -0.1342 -0.3307 212 ILE   S C   
33755 O  O   . ILE   S  213 ? 1.7491 1.4140 2.2689 0.2961  -0.1193 -0.2769 212 ILE   S O   
33756 C  CB  . ILE   S  213 ? 1.6980 1.3742 2.2900 0.3674  -0.1352 -0.3383 212 ILE   S CB  
33757 C  CG1 . ILE   S  213 ? 1.7171 1.3768 2.3262 0.3761  -0.1442 -0.3209 212 ILE   S CG1 
33758 C  CG2 . ILE   S  213 ? 1.6127 1.3220 2.2869 0.3926  -0.1552 -0.3132 212 ILE   S CG2 
33759 C  CD1 . ILE   S  213 ? 1.7203 1.4661 2.3776 0.3379  -0.1444 -0.3080 212 ILE   S CD1 
33760 N  N   . ALA   S  214 ? 1.7442 1.2825 2.1999 0.3143  -0.1674 -0.3050 213 ALA   S N   
33761 C  CA  . ALA   S  214 ? 1.6520 1.2266 2.1384 0.2639  -0.2135 -0.2797 213 ALA   S CA  
33762 C  C   . ALA   S  214 ? 1.6533 1.0923 2.1680 0.2214  -0.2408 -0.2912 213 ALA   S C   
33763 O  O   . ALA   S  214 ? 1.7178 1.1482 2.1553 0.1598  -0.2855 -0.2464 213 ALA   S O   
33764 C  CB  . ALA   S  214 ? 1.6487 1.1991 2.1018 0.3014  -0.2045 -0.2685 213 ALA   S CB  
33765 N  N   . ILE   S  215 ? 1.6050 1.0461 2.1337 0.2755  -0.2454 -0.2474 214 ILE   S N   
33766 C  CA  . ILE   S  215 ? 1.5601 0.9665 2.1451 0.2712  -0.2733 -0.2171 214 ILE   S CA  
33767 C  C   . ILE   S  215 ? 1.5878 0.9233 2.1089 0.2204  -0.2824 -0.2345 214 ILE   S C   
33768 O  O   . ILE   S  215 ? 1.5966 0.8104 2.0303 0.1191  -0.2170 -0.2952 214 ILE   S O   
33769 C  CB  . ILE   S  215 ? 1.5575 0.9240 2.1605 0.2426  -0.2914 -0.2035 214 ILE   S CB  
33770 C  CG1 . ILE   S  215 ? 1.5684 0.9066 2.1799 0.2122  -0.3009 -0.2028 214 ILE   S CG1 
33771 C  CG2 . ILE   S  215 ? 1.4885 0.9000 2.1350 0.2143  -0.2998 -0.2408 214 ILE   S CG2 
33772 C  CD1 . ILE   S  215 ? 1.5683 0.9197 2.2689 0.2120  -0.2817 -0.1842 214 ILE   S CD1 
33773 N  N   . VAL   S  216 ? 1.6064 0.8990 2.0801 0.2334  -0.3438 -0.1884 215 VAL   S N   
33774 C  CA  . VAL   S  216 ? 1.6640 0.8748 2.1297 0.2230  -0.3707 -0.1945 215 VAL   S CA  
33775 C  C   . VAL   S  216 ? 1.6610 0.8841 2.1733 0.2392  -0.4104 -0.1307 215 VAL   S C   
33776 O  O   . VAL   S  216 ? 1.7498 0.8227 2.2842 0.2399  -0.3911 -0.1635 215 VAL   S O   
33777 C  CB  . VAL   S  216 ? 1.6718 0.9227 2.1419 0.2060  -0.3714 -0.2000 215 VAL   S CB  
33778 C  CG1 . VAL   S  216 ? 1.6872 0.9228 2.1369 0.2175  -0.4011 -0.1747 215 VAL   S CG1 
33779 C  CG2 . VAL   S  216 ? 1.6919 0.9595 2.1198 0.2122  -0.3593 -0.2520 215 VAL   S CG2 
33780 N  N   . GLY   S  217 ? 1.6417 0.9215 2.1565 0.2472  -0.4338 -0.1564 216 GLY   S N   
33781 C  CA  . GLY   S  217 ? 1.6092 0.9553 2.1935 0.2506  -0.4632 -0.1640 216 GLY   S CA  
33782 C  C   . GLY   S  217 ? 1.5769 0.9500 2.2286 0.2558  -0.4488 -0.1708 216 GLY   S C   
33783 O  O   . GLY   S  217 ? 1.6114 0.8874 2.2184 0.1995  -0.5077 -0.1972 216 GLY   S O   
33784 N  N   . LYS   S  218 ? 1.5329 0.9563 2.2327 0.2323  -0.4205 -0.1997 217 LYS   S N   
33785 C  CA  . LYS   S  218 ? 1.5721 1.0928 2.2080 0.1820  -0.3819 -0.2898 217 LYS   S CA  
33786 C  C   . LYS   S  218 ? 1.5988 1.2113 2.1729 0.1244  -0.3062 -0.2864 217 LYS   S C   
33787 O  O   . LYS   S  218 ? 1.6132 1.2732 2.2638 0.1606  -0.2863 -0.3256 217 LYS   S O   
33788 C  CB  . LYS   S  218 ? 1.5859 1.1050 2.1935 0.1327  -0.3775 -0.2203 217 LYS   S CB  
33789 C  CG  . LYS   S  218 ? 1.6119 1.1352 2.1506 0.0514  -0.3595 -0.2065 217 LYS   S CG  
33790 C  CD  . LYS   S  218 ? 1.6176 1.1414 2.1345 -0.0328 -0.3578 -0.2132 217 LYS   S CD  
33791 C  CE  . LYS   S  218 ? 1.6329 1.1752 2.0935 -0.0764 -0.3378 -0.2087 217 LYS   S CE  
33792 N  NZ  . LYS   S  218 ? 1.6420 1.2654 2.0977 -0.0730 -0.3421 -0.1964 217 LYS   S NZ  
33793 N  N   . ASP   S  219 ? 1.6795 1.3465 2.1997 0.1498  -0.2664 -0.4426 218 ASP   S N   
33794 C  CA  . ASP   S  219 ? 1.7466 1.3673 2.1203 0.1291  -0.2342 -0.4878 218 ASP   S CA  
33795 C  C   . ASP   S  219 ? 1.7350 1.3207 2.1387 0.1785  -0.1375 -0.5133 218 ASP   S C   
33796 O  O   . ASP   S  219 ? 1.8647 1.1772 2.0750 0.1194  -0.0654 -0.6323 218 ASP   S O   
33797 C  CB  . ASP   S  219 ? 1.7899 1.5102 2.1383 0.0997  -0.2946 -0.5238 218 ASP   S CB  
33798 C  CG  . ASP   S  219 ? 1.8405 1.5900 2.1418 0.0936  -0.3876 -0.5568 218 ASP   S CG  
33799 O  OD1 . ASP   S  219 ? 1.8510 1.5580 2.1208 0.0996  -0.4443 -0.5974 218 ASP   S OD1 
33800 O  OD2 . ASP   S  219 ? 1.8658 1.6826 2.1814 0.0885  -0.4242 -0.6664 218 ASP   S OD2 
33801 N  N   . THR   S  220 ? 1.6453 1.2992 2.1577 0.2448  -0.1251 -0.4749 219 THR   S N   
33802 C  CA  . THR   S  220 ? 1.6517 1.3169 2.1214 0.2539  -0.1506 -0.4175 219 THR   S CA  
33803 C  C   . THR   S  220 ? 1.6520 1.2181 2.0401 0.2897  -0.1610 -0.3169 219 THR   S C   
33804 O  O   . THR   S  220 ? 1.6981 1.2320 1.9825 0.3008  -0.0951 -0.3554 219 THR   S O   
33805 C  CB  . THR   S  220 ? 1.7262 1.3233 2.2673 0.2776  -0.1492 -0.3757 219 THR   S CB  
33806 O  OG1 . THR   S  220 ? 1.7966 1.3175 2.3183 0.3286  -0.2139 -0.2930 219 THR   S OG1 
33807 C  CG2 . THR   S  220 ? 1.7519 1.3614 2.2837 0.2603  -0.1327 -0.4110 219 THR   S CG2 
33808 N  N   . PRO   S  221 ? 1.6257 1.1707 2.0748 0.2546  -0.1899 -0.3038 220 PRO   S N   
33809 C  CA  . PRO   S  221 ? 1.6355 1.0872 2.0767 0.2643  -0.2140 -0.2550 220 PRO   S CA  
33810 C  C   . PRO   S  221 ? 1.5777 1.0467 2.0930 0.2408  -0.2198 -0.2161 220 PRO   S C   
33811 O  O   . PRO   S  221 ? 1.6625 0.9003 2.0497 0.2659  -0.2259 -0.2498 220 PRO   S O   
33812 C  CB  . PRO   S  221 ? 1.6337 1.0812 2.0724 0.2474  -0.1975 -0.2553 220 PRO   S CB  
33813 C  CG  . PRO   S  221 ? 1.6360 1.0754 2.0260 0.2537  -0.2026 -0.3011 220 PRO   S CG  
33814 C  CD  . PRO   S  221 ? 1.6213 1.0964 2.0479 0.2743  -0.1996 -0.3327 220 PRO   S CD  
33815 N  N   . PHE   S  222 ? 1.6080 1.0051 2.0570 0.2035  -0.2803 -0.1908 221 PHE   S N   
33816 C  CA  . PHE   S  222 ? 1.6177 1.0504 2.0045 0.1962  -0.2930 -0.2130 221 PHE   S CA  
33817 C  C   . PHE   S  222 ? 1.5569 1.0553 2.0296 0.1636  -0.2460 -0.2253 221 PHE   S C   
33818 O  O   . PHE   S  222 ? 1.6125 1.0301 1.9478 0.1474  -0.1937 -0.2027 221 PHE   S O   
33819 C  CB  . PHE   S  222 ? 1.6085 1.0566 1.9874 0.2174  -0.3282 -0.2139 221 PHE   S CB  
33820 C  CG  . PHE   S  222 ? 1.6246 1.0560 1.9972 0.2336  -0.3551 -0.2105 221 PHE   S CG  
33821 C  CD1 . PHE   S  222 ? 1.6160 1.1135 2.0087 0.2349  -0.3679 -0.2222 221 PHE   S CD1 
33822 C  CD2 . PHE   S  222 ? 1.5919 1.0622 1.9749 0.2737  -0.3851 -0.2023 221 PHE   S CD2 
33823 C  CE1 . PHE   S  222 ? 1.5855 1.0737 2.0276 0.2626  -0.3826 -0.2008 221 PHE   S CE1 
33824 C  CE2 . PHE   S  222 ? 1.5758 1.0472 2.0011 0.2744  -0.3781 -0.1975 221 PHE   S CE2 
33825 C  CZ  . PHE   S  222 ? 1.5700 1.0277 2.0159 0.2668  -0.3903 -0.2318 221 PHE   S CZ  
33826 N  N   . THR   S  223 ? 1.4840 1.1516 2.1385 0.1567  -0.2395 -0.2336 222 THR   S N   
33827 C  CA  . THR   S  223 ? 1.5388 1.2930 2.1541 0.1459  -0.2237 -0.2226 222 THR   S CA  
33828 C  C   . THR   S  223 ? 1.6150 1.3147 2.1342 0.1998  -0.2229 -0.2337 222 THR   S C   
33829 O  O   . THR   S  223 ? 1.6285 1.3618 2.2050 0.2928  -0.2198 -0.2092 222 THR   S O   
33830 C  CB  . THR   S  223 ? 1.5343 1.4350 2.2531 0.1078  -0.2294 -0.2256 222 THR   S CB  
33831 O  OG1 . THR   S  223 ? 1.5844 1.5852 2.3154 0.0499  -0.2829 -0.1486 222 THR   S OG1 
33832 C  CG2 . THR   S  223 ? 1.4749 1.4428 2.2451 0.1412  -0.2366 -0.2308 222 THR   S CG2 
33833 N  N   . ILE   S  224 ? 1.6707 1.1956 2.1401 0.2192  -0.2065 -0.2950 223 ILE   S N   
33834 C  CA  . ILE   S  224 ? 1.7077 1.1862 2.1407 0.2218  -0.2286 -0.3009 223 ILE   S CA  
33835 C  C   . ILE   S  224 ? 1.7653 1.2246 2.1352 0.1521  -0.1942 -0.3655 223 ILE   S C   
33836 O  O   . ILE   S  224 ? 1.7968 1.1002 2.0409 0.1188  -0.1913 -0.4932 223 ILE   S O   
33837 C  CB  . ILE   S  224 ? 1.7006 1.1378 2.1136 0.2828  -0.2462 -0.2383 223 ILE   S CB  
33838 C  CG1 . ILE   S  224 ? 1.7248 1.0298 2.0438 0.3314  -0.2694 -0.2230 223 ILE   S CG1 
33839 C  CG2 . ILE   S  224 ? 1.7302 1.1487 2.1548 0.2958  -0.2290 -0.2481 223 ILE   S CG2 
33840 C  CD1 . ILE   S  224 ? 1.7351 1.0365 2.0331 0.3569  -0.2662 -0.1943 223 ILE   S CD1 
33841 N  N   . TYR   S  225 ? 1.7623 1.3268 2.2382 0.2216  -0.1875 -0.4164 224 TYR   S N   
33842 C  CA  . TYR   S  225 ? 1.8413 1.4960 2.3272 0.1716  -0.1031 -0.5029 224 TYR   S CA  
33843 C  C   . TYR   S  225 ? 1.8079 1.5631 2.3667 0.1385  -0.1275 -0.5397 224 TYR   S C   
33844 O  O   . TYR   S  225 ? 1.8725 1.5405 2.3657 0.1553  -0.1147 -0.5517 224 TYR   S O   
33845 C  CB  . TYR   S  225 ? 1.8799 1.5608 2.3644 0.1956  -0.1277 -0.5469 224 TYR   S CB  
33846 C  CG  . TYR   S  225 ? 2.0076 1.4726 2.4371 0.2151  -0.0360 -0.5826 224 TYR   S CG  
33847 C  CD1 . TYR   S  225 ? 2.0244 1.4095 2.4194 0.2522  -0.0066 -0.6313 224 TYR   S CD1 
33848 C  CD2 . TYR   S  225 ? 2.0903 1.4372 2.4200 0.2332  -0.0241 -0.6575 224 TYR   S CD2 
33849 C  CE1 . TYR   S  225 ? 2.0599 1.4193 2.4433 0.2327  -0.0275 -0.6288 224 TYR   S CE1 
33850 C  CE2 . TYR   S  225 ? 2.1284 1.4314 2.4682 0.1935  -0.0486 -0.6496 224 TYR   S CE2 
33851 C  CZ  . TYR   S  225 ? 2.1290 1.4966 2.4651 0.2152  -0.0360 -0.5722 224 TYR   S CZ  
33852 O  OH  . TYR   S  225 ? 2.1623 1.5127 2.5014 0.3102  -0.0474 -0.6360 224 TYR   S OH  
33853 N  N   . ASP   S  226 ? 1.7402 1.6478 2.3891 0.0722  -0.1157 -0.4954 225 ASP   S N   
33854 C  CA  . ASP   S  226 ? 1.7310 1.7044 2.3654 0.0347  -0.0986 -0.4976 225 ASP   S CA  
33855 C  C   . ASP   S  226 ? 1.7561 1.5822 2.3544 0.0095  -0.0826 -0.5020 225 ASP   S C   
33856 O  O   . ASP   S  226 ? 1.8652 1.6351 2.3145 -0.0940 -0.0664 -0.4424 225 ASP   S O   
33857 C  CB  . ASP   S  226 ? 1.7155 1.8097 2.4120 -0.0073 -0.1099 -0.4579 225 ASP   S CB  
33858 C  CG  . ASP   S  226 ? 1.6622 1.8665 2.4717 -0.0637 -0.1500 -0.4289 225 ASP   S CG  
33859 O  OD1 . ASP   S  226 ? 1.5797 1.9413 2.5108 -0.1482 -0.1452 -0.3727 225 ASP   S OD1 
33860 O  OD2 . ASP   S  226 ? 1.6137 1.7876 2.4916 -0.1270 -0.1579 -0.4318 225 ASP   S OD2 
33861 N  N   . GLY   S  227 ? 1.7506 1.5416 2.3807 0.1520  -0.0172 -0.4848 226 GLY   S N   
33862 C  CA  . GLY   S  227 ? 1.7032 1.5330 2.4165 0.1942  -0.0195 -0.4651 226 GLY   S CA  
33863 C  C   . GLY   S  227 ? 1.6791 1.5166 2.4327 0.2337  -0.0070 -0.4616 226 GLY   S C   
33864 O  O   . GLY   S  227 ? 1.6872 1.5961 2.4339 0.1523  -0.0414 -0.4218 226 GLY   S O   
33865 N  N   . GLU   S  228 ? 1.5575 1.4803 2.4064 0.3121  -0.0082 -0.4692 227 GLU   S N   
33866 C  CA  . GLU   S  228 ? 1.5620 1.5832 2.4352 0.3676  -0.0318 -0.4855 227 GLU   S CA  
33867 C  C   . GLU   S  228 ? 1.4645 1.5389 2.4209 0.4167  -0.0133 -0.4848 227 GLU   S C   
33868 O  O   . GLU   S  228 ? 1.4834 1.7009 2.4336 0.3399  -0.0852 -0.5046 227 GLU   S O   
33869 C  CB  . GLU   S  228 ? 1.5761 1.5872 2.4627 0.3959  -0.0020 -0.4766 227 GLU   S CB  
33870 C  CG  . GLU   S  228 ? 1.6018 1.6681 2.5395 0.4309  0.0185  -0.5228 227 GLU   S CG  
33871 C  CD  . GLU   S  228 ? 1.5874 1.7186 2.5943 0.4481  0.0574  -0.5876 227 GLU   S CD  
33872 O  OE1 . GLU   S  228 ? 1.5462 1.6105 2.5994 0.4560  0.0936  -0.6452 227 GLU   S OE1 
33873 O  OE2 . GLU   S  228 ? 1.6125 1.7052 2.6912 0.4720  0.0683  -0.5993 227 GLU   S OE2 
33874 N  N   . ALA   S  229 ? 1.4056 1.4516 2.3978 0.4501  -0.0781 -0.4460 228 ALA   S N   
33875 C  CA  . ALA   S  229 ? 1.4001 1.4887 2.4146 0.4081  -0.0880 -0.4623 228 ALA   S CA  
33876 C  C   . ALA   S  229 ? 1.4623 1.4777 2.4816 0.4220  -0.0437 -0.4483 228 ALA   S C   
33877 O  O   . ALA   S  229 ? 1.5304 1.4499 2.4771 0.4276  -0.0231 -0.4765 228 ALA   S O   
33878 C  CB  . ALA   S  229 ? 1.3716 1.4693 2.3545 0.3851  -0.1104 -0.4565 228 ALA   S CB  
33879 N  N   . VAL   S  230 ? 1.5241 1.5345 2.5083 0.3486  -0.0060 -0.4843 229 VAL   S N   
33880 C  CA  . VAL   S  230 ? 1.5830 1.5591 2.5418 0.3460  0.0142  -0.4573 229 VAL   S CA  
33881 C  C   . VAL   S  230 ? 1.5950 1.5448 2.6694 0.3551  0.0458  -0.4263 229 VAL   S C   
33882 O  O   . VAL   S  230 ? 1.5797 1.5868 2.6483 0.3918  0.0922  -0.4077 229 VAL   S O   
33883 C  CB  . VAL   S  230 ? 1.6130 1.6084 2.5106 0.3145  0.0007  -0.4765 229 VAL   S CB  
33884 C  CG1 . VAL   S  230 ? 1.6203 1.5826 2.4750 0.3242  -0.0244 -0.4533 229 VAL   S CG1 
33885 C  CG2 . VAL   S  230 ? 1.6999 1.6518 2.5057 0.3399  0.0216  -0.4976 229 VAL   S CG2 
33886 N  N   . ALA   S  231 ? 1.6275 1.5737 2.7591 0.3014  0.0691  -0.3367 230 ALA   S N   
33887 C  CA  . ALA   S  231 ? 1.5781 1.6443 2.8046 0.2932  0.0733  -0.3124 230 ALA   S CA  
33888 C  C   . ALA   S  231 ? 1.5654 1.6782 2.8566 0.2748  0.0459  -0.2906 230 ALA   S C   
33889 O  O   . ALA   S  231 ? 1.4498 1.8011 2.9528 0.3375  0.0822  -0.2595 230 ALA   S O   
33890 C  CB  . ALA   S  231 ? 1.5929 1.6314 2.8131 0.2661  0.0869  -0.3239 230 ALA   S CB  
33891 N  N   . LYS   S  232 ? 1.5922 1.6287 2.7792 0.2536  0.0266  -0.2406 231 LYS   S N   
33892 C  CA  . LYS   S  232 ? 1.6825 1.5827 2.7275 0.2690  0.0318  -0.2578 231 LYS   S CA  
33893 C  C   . LYS   S  232 ? 1.6861 1.5691 2.7290 0.2983  -0.0247 -0.2479 231 LYS   S C   
33894 O  O   . LYS   S  232 ? 1.7597 1.6683 2.6894 0.2672  -0.0844 -0.2290 231 LYS   S O   
33895 C  CB  . LYS   S  232 ? 1.7151 1.5868 2.6785 0.2531  0.0713  -0.2422 231 LYS   S CB  
33896 C  CG  . LYS   S  232 ? 1.7228 1.6088 2.6876 0.2592  0.0579  -0.2238 231 LYS   S CG  
33897 C  CD  . LYS   S  232 ? 1.7165 1.5647 2.6421 0.2471  0.0405  -0.1974 231 LYS   S CD  
33898 C  CE  . LYS   S  232 ? 1.6533 1.5669 2.5845 0.2665  0.0453  -0.1927 231 LYS   S CE  
33899 N  NZ  . LYS   S  232 ? 1.6451 1.4946 2.5469 0.2893  0.0750  -0.1770 231 LYS   S NZ  
33900 N  N   . TYR   S  233 ? 1.6273 1.5301 2.7147 0.3682  -0.0583 -0.2229 232 TYR   S N   
33901 C  CA  . TYR   S  233 ? 1.6056 1.4371 2.7481 0.4295  -0.1039 -0.2060 232 TYR   S CA  
33902 C  C   . TYR   S  233 ? 1.6306 1.3219 2.7650 0.4486  -0.0891 -0.0952 232 TYR   S C   
33903 O  O   . TYR   S  233 ? 1.6155 1.0250 2.7898 0.5201  -0.1312 -0.1737 232 TYR   S O   
33904 C  CB  . TYR   S  233 ? 1.5912 1.4817 2.7408 0.4503  -0.1377 -0.2200 232 TYR   S CB  
33905 C  CG  . TYR   S  233 ? 1.5730 1.4721 2.7643 0.4354  -0.2140 -0.2109 232 TYR   S CG  
33906 C  CD1 . TYR   S  233 ? 1.5707 1.5131 2.7994 0.4243  -0.2560 -0.2081 232 TYR   S CD1 
33907 C  CD2 . TYR   S  233 ? 1.5261 1.4741 2.7548 0.4310  -0.2386 -0.2223 232 TYR   S CD2 
33908 C  CE1 . TYR   S  233 ? 1.5280 1.4681 2.7781 0.4581  -0.2737 -0.1652 232 TYR   S CE1 
33909 C  CE2 . TYR   S  233 ? 1.4544 1.4423 2.7444 0.4790  -0.2574 -0.2022 232 TYR   S CE2 
33910 C  CZ  . TYR   S  233 ? 1.4534 1.4210 2.7484 0.4917  -0.2515 -0.2360 232 TYR   S CZ  
33911 O  OH  . TYR   S  233 ? 1.4040 1.4119 2.7184 0.5797  -0.2462 -0.2228 232 TYR   S OH  
33912 N  N   . ILE   S  234 ? 1.6858 1.2861 2.7661 0.4659  -0.0821 -0.0836 233 ILE   S N   
33913 C  CA  . ILE   S  234 ? 1.7352 1.2740 2.7644 0.4444  -0.0961 -0.0513 233 ILE   S CA  
33914 C  C   . ILE   S  234 ? 1.7314 1.4131 2.8467 0.4569  -0.0964 0.0220  233 ILE   S C   
33915 O  O   . ILE   S  234 ? 1.7410 1.5211 2.8767 0.4457  -0.0891 0.0935  233 ILE   S O   
33916 C  CB  . ILE   S  234 ? 1.6986 1.2400 2.7493 0.4525  -0.0743 -0.0786 233 ILE   S CB  
33917 C  CG1 . ILE   S  234 ? 1.7150 1.1387 2.6791 0.4540  -0.0867 -0.0929 233 ILE   S CG1 
33918 C  CG2 . ILE   S  234 ? 1.7498 1.2336 2.7598 0.4420  -0.0568 -0.0807 233 ILE   S CG2 
33919 C  CD1 . ILE   S  234 ? 1.6716 1.1101 2.6708 0.4820  -0.0789 -0.1122 233 ILE   S CD1 
33920 O  OXT . ILE   S  234 ? 1.8137 1.3890 2.8879 0.4051  -0.0830 0.0328  233 ILE   S OXT 
33921 N  N   . THR   T  6   ? 2.5113 0.7101 2.0929 0.2061  -0.4993 0.0610  2   THR   T N   
33922 C  CA  . THR   T  6   ? 2.4671 0.7546 2.0428 0.1751  -0.4809 0.1098  2   THR   T CA  
33923 C  C   . THR   T  6   ? 2.3750 0.7713 2.0534 0.1011  -0.4750 0.0873  2   THR   T C   
33924 O  O   . THR   T  6   ? 2.3853 0.6084 2.0204 0.0379  -0.4435 0.1240  2   THR   T O   
33925 C  CB  . THR   T  6   ? 2.5320 0.8495 2.1297 0.2531  -0.4700 0.1760  2   THR   T CB  
33926 O  OG1 . THR   T  6   ? 2.5769 0.8781 2.1363 0.2039  -0.5073 0.0717  2   THR   T OG1 
33927 C  CG2 . THR   T  6   ? 2.5534 0.8316 2.1162 0.2790  -0.4846 0.1991  2   THR   T CG2 
33928 N  N   . GLY   T  7   ? 2.3771 0.6271 1.9900 0.0477  -0.3999 0.1766  3   GLY   T N   
33929 C  CA  . GLY   T  7   ? 2.2593 0.7006 1.8769 0.0366  -0.3918 0.1896  3   GLY   T CA  
33930 C  C   . GLY   T  7   ? 2.1628 0.6629 1.7653 0.0602  -0.3742 0.2682  3   GLY   T C   
33931 O  O   . GLY   T  7   ? 2.1288 0.5861 1.7704 0.1455  -0.4105 0.2438  3   GLY   T O   
33932 N  N   . TYR   T  8   ? 2.1061 0.6484 1.7478 0.0977  -0.3815 0.2605  4   TYR   T N   
33933 C  CA  . TYR   T  8   ? 2.0516 0.5348 1.6853 0.0731  -0.4086 0.3142  4   TYR   T CA  
33934 C  C   . TYR   T  8   ? 2.0547 0.4236 1.6114 0.0837  -0.4041 0.3444  4   TYR   T C   
33935 O  O   . TYR   T  8   ? 2.0075 0.4460 1.5779 0.1977  -0.4165 0.3912  4   TYR   T O   
33936 C  CB  . TYR   T  8   ? 2.0839 0.6618 1.6700 0.1097  -0.3691 0.3118  4   TYR   T CB  
33937 C  CG  . TYR   T  8   ? 2.0862 0.6928 1.6947 0.1416  -0.3974 0.2718  4   TYR   T CG  
33938 C  CD1 . TYR   T  8   ? 2.1088 0.7281 1.6381 0.1683  -0.4008 0.3005  4   TYR   T CD1 
33939 C  CD2 . TYR   T  8   ? 2.1521 0.7090 1.7317 0.1079  -0.3899 0.2062  4   TYR   T CD2 
33940 C  CE1 . TYR   T  8   ? 2.1218 0.6231 1.5818 0.1812  -0.3992 0.2542  4   TYR   T CE1 
33941 C  CE2 . TYR   T  8   ? 2.1398 0.6763 1.6946 0.1344  -0.4049 0.2088  4   TYR   T CE2 
33942 C  CZ  . TYR   T  8   ? 2.1503 0.6326 1.5992 0.1262  -0.4061 0.2229  4   TYR   T CZ  
33943 O  OH  . TYR   T  8   ? 2.1429 0.5383 1.5487 0.1569  -0.4019 0.2349  4   TYR   T OH  
33944 N  N   . ASP   T  9   ? 2.0238 0.2455 1.5421 0.0094  -0.4313 0.2628  5   ASP   T N   
33945 C  CA  . ASP   T  9   ? 2.0221 0.3338 1.5672 -0.0102 -0.4228 0.2245  5   ASP   T CA  
33946 C  C   . ASP   T  9   ? 2.0343 0.4217 1.5369 0.0051  -0.3927 0.2240  5   ASP   T C   
33947 O  O   . ASP   T  9   ? 2.0064 0.4973 1.5486 0.0212  -0.4276 0.3171  5   ASP   T O   
33948 C  CB  . ASP   T  9   ? 2.0139 0.2724 1.6395 -0.0327 -0.4279 0.2027  5   ASP   T CB  
33949 C  CG  . ASP   T  9   ? 2.0158 0.3254 1.6795 -0.0253 -0.4160 0.1722  5   ASP   T CG  
33950 O  OD1 . ASP   T  9   ? 2.0352 0.5211 1.6577 0.0053  -0.4297 0.2228  5   ASP   T OD1 
33951 O  OD2 . ASP   T  9   ? 2.0280 0.3047 1.7497 -0.0101 -0.4212 0.1554  5   ASP   T OD2 
33952 N  N   . LEU   T  10  ? 2.0017 0.4538 1.4842 -0.0671 -0.3438 0.1394  6   LEU   T N   
33953 C  CA  . LEU   T  10  ? 1.9927 0.5112 1.5156 -0.1071 -0.2959 0.1003  6   LEU   T CA  
33954 C  C   . LEU   T  10  ? 1.9209 0.4934 1.4586 -0.1664 -0.2765 0.1311  6   LEU   T C   
33955 O  O   . LEU   T  10  ? 1.9389 0.3177 1.4348 -0.1525 -0.3121 0.1030  6   LEU   T O   
33956 C  CB  . LEU   T  10  ? 2.0270 0.5671 1.5133 -0.1515 -0.2725 0.0899  6   LEU   T CB  
33957 C  CG  . LEU   T  10  ? 2.0872 0.5554 1.5532 -0.1589 -0.2481 0.1203  6   LEU   T CG  
33958 C  CD1 . LEU   T  10  ? 2.1116 0.6158 1.5399 -0.1812 -0.2357 0.1125  6   LEU   T CD1 
33959 C  CD2 . LEU   T  10  ? 2.0862 0.4944 1.5675 -0.1609 -0.2431 0.1258  6   LEU   T CD2 
33960 N  N   . SER   T  11  ? 1.9039 0.4996 1.4988 -0.1455 -0.3025 0.1154  7   SER   T N   
33961 C  CA  . SER   T  11  ? 1.8839 0.4929 1.4643 -0.1660 -0.3163 0.1385  7   SER   T CA  
33962 C  C   . SER   T  11  ? 1.9089 0.5716 1.4538 -0.1416 -0.3865 0.1072  7   SER   T C   
33963 O  O   . SER   T  11  ? 1.9242 0.5839 1.5237 -0.1930 -0.3076 0.0276  7   SER   T O   
33964 C  CB  . SER   T  11  ? 1.8581 0.5452 1.4773 -0.2390 -0.3129 0.1139  7   SER   T CB  
33965 O  OG  . SER   T  11  ? 1.8214 0.5591 1.5456 -0.2472 -0.2562 0.1589  7   SER   T OG  
33966 N  N   . ASN   T  12  ? 1.8784 0.5291 1.3135 -0.1108 -0.4088 0.1691  8   ASN   T N   
33967 C  CA  . ASN   T  12  ? 1.8847 0.4517 1.3049 -0.0847 -0.4144 0.1978  8   ASN   T CA  
33968 C  C   . ASN   T  12  ? 1.8853 0.4352 1.2764 -0.0761 -0.4434 0.2062  8   ASN   T C   
33969 O  O   . ASN   T  12  ? 1.8628 0.3782 1.2204 -0.1085 -0.4048 0.1827  8   ASN   T O   
33970 C  CB  . ASN   T  12  ? 1.9021 0.4599 1.2596 -0.1063 -0.4051 0.2489  8   ASN   T CB  
33971 C  CG  . ASN   T  12  ? 1.9154 0.5102 1.2383 -0.1306 -0.4511 0.2510  8   ASN   T CG  
33972 O  OD1 . ASN   T  12  ? 1.9618 0.5894 1.2811 -0.1655 -0.4270 0.2775  8   ASN   T OD1 
33973 N  ND2 . ASN   T  12  ? 1.8894 0.5183 1.1824 -0.1380 -0.4494 0.2666  8   ASN   T ND2 
33974 N  N   . SER   T  13  ? 1.8887 0.4998 1.2940 -0.0612 -0.4325 0.1908  9   SER   T N   
33975 C  CA  . SER   T  13  ? 1.8836 0.4776 1.3046 -0.0746 -0.4404 0.1974  9   SER   T CA  
33976 C  C   . SER   T  13  ? 1.9713 0.3341 1.3197 -0.0580 -0.4064 0.1504  9   SER   T C   
33977 O  O   . SER   T  13  ? 1.9486 0.1965 1.3514 -0.1084 -0.4109 0.2058  9   SER   T O   
33978 C  CB  . SER   T  13  ? 1.8887 0.5029 1.3177 -0.0549 -0.4384 0.2180  9   SER   T CB  
33979 O  OG  . SER   T  13  ? 1.9149 0.6395 1.3162 -0.0186 -0.4548 0.2530  9   SER   T OG  
33980 N  N   . VAL   T  14  ? 1.9258 0.3291 1.3197 -0.1111 -0.4087 0.1094  10  VAL   T N   
33981 C  CA  . VAL   T  14  ? 1.9490 0.3145 1.2767 -0.0830 -0.4259 0.0168  10  VAL   T CA  
33982 C  C   . VAL   T  14  ? 2.0004 0.2311 1.2506 -0.1084 -0.4212 -0.0373 10  VAL   T C   
33983 O  O   . VAL   T  14  ? 2.0653 0.1562 1.1824 -0.1331 -0.4741 -0.0644 10  VAL   T O   
33984 C  CB  . VAL   T  14  ? 1.9418 0.3281 1.2806 -0.0902 -0.4177 0.0137  10  VAL   T CB  
33985 C  CG1 . VAL   T  14  ? 1.9293 0.4113 1.3395 -0.1422 -0.4094 0.0117  10  VAL   T CG1 
33986 C  CG2 . VAL   T  14  ? 1.9154 0.2756 1.3106 -0.1120 -0.4032 0.0232  10  VAL   T CG2 
33987 N  N   . PHE   T  15  ? 1.9763 0.1926 1.2003 -0.0856 -0.4444 -0.0593 11  PHE   T N   
33988 C  CA  . PHE   T  15  ? 1.9635 0.3664 1.1781 -0.0687 -0.4563 0.0086  11  PHE   T CA  
33989 C  C   . PHE   T  15  ? 1.9540 0.3766 1.1751 -0.0159 -0.4454 0.0148  11  PHE   T C   
33990 O  O   . PHE   T  15  ? 1.9470 0.4690 1.1444 -0.0164 -0.4371 0.0440  11  PHE   T O   
33991 C  CB  . PHE   T  15  ? 1.9770 0.3313 1.1693 -0.0562 -0.4615 -0.0224 11  PHE   T CB  
33992 C  CG  . PHE   T  15  ? 2.0108 0.4132 1.1395 -0.0343 -0.4529 -0.0639 11  PHE   T CG  
33993 C  CD1 . PHE   T  15  ? 2.0086 0.4346 1.1453 -0.0125 -0.4621 -0.0583 11  PHE   T CD1 
33994 C  CD2 . PHE   T  15  ? 1.9940 0.4405 1.1296 -0.0066 -0.4398 -0.0932 11  PHE   T CD2 
33995 C  CE1 . PHE   T  15  ? 1.9783 0.4295 1.1346 -0.0263 -0.4789 -0.0560 11  PHE   T CE1 
33996 C  CE2 . PHE   T  15  ? 1.9795 0.3963 1.1392 -0.0558 -0.4544 -0.0751 11  PHE   T CE2 
33997 C  CZ  . PHE   T  15  ? 1.9798 0.3596 1.1367 -0.0501 -0.4535 -0.0854 11  PHE   T CZ  
33998 N  N   . SER   T  16  ? 1.9239 0.4375 1.2459 0.0251  -0.4372 0.0355  12  SER   T N   
33999 C  CA  . SER   T  16  ? 1.9039 0.4514 1.3019 -0.0090 -0.4221 -0.0113 12  SER   T CA  
34000 C  C   . SER   T  16  ? 1.9095 0.3919 1.2844 -0.0261 -0.4361 -0.0110 12  SER   T C   
34001 O  O   . SER   T  16  ? 1.9103 0.2897 1.3178 -0.0769 -0.4639 -0.0471 12  SER   T O   
34002 C  CB  . SER   T  16  ? 1.8924 0.5149 1.4144 0.0101  -0.4265 0.0167  12  SER   T CB  
34003 O  OG  . SER   T  16  ? 1.8820 0.5484 1.4186 0.0160  -0.4028 0.0732  12  SER   T OG  
34004 N  N   . PRO   T  17  ? 1.9220 0.3368 1.2908 0.0012  -0.4016 0.0517  13  PRO   T N   
34005 C  CA  . PRO   T  17  ? 1.9550 0.3129 1.3139 -0.0072 -0.3945 0.0926  13  PRO   T CA  
34006 C  C   . PRO   T  17  ? 1.9902 0.3476 1.3150 -0.0151 -0.3863 0.1288  13  PRO   T C   
34007 O  O   . PRO   T  17  ? 2.0149 0.3714 1.3414 -0.0399 -0.3551 0.1614  13  PRO   T O   
34008 C  CB  . PRO   T  17  ? 1.9577 0.3286 1.3252 -0.0106 -0.3822 0.0714  13  PRO   T CB  
34009 C  CG  . PRO   T  17  ? 1.9356 0.3113 1.3240 -0.0187 -0.3834 0.0665  13  PRO   T CG  
34010 C  CD  . PRO   T  17  ? 1.9271 0.2720 1.3201 0.0005  -0.3836 0.0703  13  PRO   T CD  
34011 N  N   . ASP   T  18  ? 2.0254 0.4301 1.3418 0.0132  -0.4219 0.1585  14  ASP   T N   
34012 C  CA  . ASP   T  18  ? 2.1384 0.5626 1.3402 0.0303  -0.4356 0.1826  14  ASP   T CA  
34013 C  C   . ASP   T  18  ? 2.1499 0.6306 1.2575 0.0586  -0.4549 0.1313  14  ASP   T C   
34014 O  O   . ASP   T  18  ? 2.2692 0.7189 1.2607 0.1237  -0.4249 0.1223  14  ASP   T O   
34015 C  CB  . ASP   T  18  ? 2.1540 0.6495 1.4042 -0.0019 -0.4590 0.2277  14  ASP   T CB  
34016 C  CG  . ASP   T  18  ? 2.2072 0.7670 1.4302 -0.0115 -0.3887 0.1880  14  ASP   T CG  
34017 O  OD1 . ASP   T  18  ? 2.2590 0.8201 1.5247 0.0137  -0.5181 0.2253  14  ASP   T OD1 
34018 O  OD2 . ASP   T  18  ? 2.2653 0.8272 1.5202 -0.1056 -0.3508 0.3072  14  ASP   T OD2 
34019 N  N   . GLY   T  19  ? 2.1102 0.6919 1.2179 0.0163  -0.5058 0.1510  15  GLY   T N   
34020 C  CA  . GLY   T  19  ? 2.0174 0.7158 1.2153 -0.0409 -0.5811 0.0940  15  GLY   T CA  
34021 C  C   . GLY   T  19  ? 2.0097 0.8001 1.2675 -0.0372 -0.6242 0.0437  15  GLY   T C   
34022 O  O   . GLY   T  19  ? 1.9821 0.8540 1.2916 -0.0269 -0.7228 0.0082  15  GLY   T O   
34023 N  N   . ARG   T  20  ? 1.9762 0.7254 1.3352 -0.0586 -0.6332 0.0086  16  ARG   T N   
34024 C  CA  . ARG   T  20  ? 1.9585 0.6370 1.3913 -0.0399 -0.6044 0.0271  16  ARG   T CA  
34025 C  C   . ARG   T  20  ? 1.9405 0.5311 1.4448 -0.0420 -0.5935 0.0488  16  ARG   T C   
34026 O  O   . ARG   T  20  ? 1.9829 0.4055 1.4782 -0.0677 -0.5887 0.0030  16  ARG   T O   
34027 C  CB  . ARG   T  20  ? 1.9316 0.6297 1.5173 -0.0476 -0.6061 0.0250  16  ARG   T CB  
34028 C  CG  . ARG   T  20  ? 1.9641 0.6781 1.5769 -0.0742 -0.5680 0.0825  16  ARG   T CG  
34029 C  CD  . ARG   T  20  ? 2.0122 0.7011 1.7069 -0.0213 -0.5260 0.0515  16  ARG   T CD  
34030 N  NE  . ARG   T  20  ? 2.0254 0.6907 1.8044 -0.0059 -0.5016 0.0526  16  ARG   T NE  
34031 C  CZ  . ARG   T  20  ? 2.0831 0.7192 1.8987 0.0247  -0.4716 0.0465  16  ARG   T CZ  
34032 N  NH1 . ARG   T  20  ? 2.0614 0.8386 1.9953 -0.0431 -0.4538 0.0479  16  ARG   T NH1 
34033 N  NH2 . ARG   T  20  ? 2.0845 0.7950 1.9326 -0.0046 -0.4477 0.0737  16  ARG   T NH2 
34034 N  N   . ASN   T  21  ? 1.9211 0.4564 1.3994 -0.0163 -0.5761 0.1372  17  ASN   T N   
34035 C  CA  . ASN   T  21  ? 1.8888 0.5335 1.4423 0.0282  -0.5173 0.1550  17  ASN   T CA  
34036 C  C   . ASN   T  21  ? 1.9517 0.3590 1.4739 0.0843  -0.4930 0.1400  17  ASN   T C   
34037 O  O   . ASN   T  21  ? 1.8698 0.3538 1.4934 0.1552  -0.5053 0.1554  17  ASN   T O   
34038 C  CB  . ASN   T  21  ? 1.9304 0.5338 1.4055 -0.0123 -0.4855 0.1889  17  ASN   T CB  
34039 C  CG  . ASN   T  21  ? 1.9386 0.5901 1.4481 -0.0130 -0.4815 0.2422  17  ASN   T CG  
34040 O  OD1 . ASN   T  21  ? 1.9515 0.7075 1.4323 -0.0363 -0.4000 0.2816  17  ASN   T OD1 
34041 N  ND2 . ASN   T  21  ? 1.9067 0.5756 1.4010 0.0153  -0.4893 0.2895  17  ASN   T ND2 
34042 N  N   . PHE   T  22  ? 1.9822 0.3761 1.5404 0.0863  -0.4410 0.1081  18  PHE   T N   
34043 C  CA  . PHE   T  22  ? 1.9552 0.5415 1.5867 0.1041  -0.3872 0.0864  18  PHE   T CA  
34044 C  C   . PHE   T  22  ? 1.9783 0.4119 1.5666 0.1271  -0.3753 0.0569  18  PHE   T C   
34045 O  O   . PHE   T  22  ? 1.9065 0.3713 1.6771 0.1508  -0.3191 0.0379  18  PHE   T O   
34046 C  CB  . PHE   T  22  ? 2.0024 0.6370 1.5878 0.1067  -0.3560 0.0346  18  PHE   T CB  
34047 C  CG  . PHE   T  22  ? 2.0095 0.6156 1.6711 0.1777  -0.3531 0.0926  18  PHE   T CG  
34048 C  CD1 . PHE   T  22  ? 1.9996 0.7245 1.7071 0.2298  -0.3791 0.1185  18  PHE   T CD1 
34049 C  CD2 . PHE   T  22  ? 2.0102 0.6832 1.7418 0.1651  -0.3490 0.1251  18  PHE   T CD2 
34050 C  CE1 . PHE   T  22  ? 1.9984 0.8000 1.7697 0.1737  -0.3707 0.1537  18  PHE   T CE1 
34051 C  CE2 . PHE   T  22  ? 2.0003 0.6892 1.7848 0.1732  -0.3615 0.1552  18  PHE   T CE2 
34052 C  CZ  . PHE   T  22  ? 1.9868 0.7636 1.7845 0.2003  -0.3844 0.1694  18  PHE   T CZ  
34053 N  N   . GLN   T  23  ? 1.9776 0.4190 1.4995 0.1724  -0.3981 0.0244  19  GLN   T N   
34054 C  CA  . GLN   T  23  ? 1.9337 0.5212 1.4651 0.1678  -0.4083 0.0248  19  GLN   T CA  
34055 C  C   . GLN   T  23  ? 1.9332 0.5411 1.4379 0.1934  -0.4366 0.0570  19  GLN   T C   
34056 O  O   . GLN   T  23  ? 1.9308 0.5908 1.4567 0.2031  -0.4386 0.0904  19  GLN   T O   
34057 C  CB  . GLN   T  23  ? 1.9416 0.5758 1.4226 0.1827  -0.4307 0.0079  19  GLN   T CB  
34058 C  CG  . GLN   T  23  ? 1.9710 0.5821 1.4522 0.1885  -0.4286 -0.0372 19  GLN   T CG  
34059 C  CD  . GLN   T  23  ? 1.9633 0.6001 1.4643 0.1473  -0.4422 -0.0663 19  GLN   T CD  
34060 O  OE1 . GLN   T  23  ? 2.0045 0.6452 1.5019 0.1827  -0.4341 -0.0871 19  GLN   T OE1 
34061 N  NE2 . GLN   T  23  ? 1.9285 0.6938 1.4484 0.0846  -0.4697 -0.0774 19  GLN   T NE2 
34062 N  N   . VAL   T  24  ? 1.9093 0.5229 1.3927 0.1732  -0.4663 0.0565  20  VAL   T N   
34063 C  CA  . VAL   T  24  ? 1.8987 0.5105 1.4142 0.1488  -0.4637 0.0328  20  VAL   T CA  
34064 C  C   . VAL   T  24  ? 1.9036 0.5376 1.4318 0.1615  -0.4668 0.0429  20  VAL   T C   
34065 O  O   . VAL   T  24  ? 1.9018 0.3598 1.3942 0.1585  -0.4535 0.0662  20  VAL   T O   
34066 C  CB  . VAL   T  24  ? 1.8755 0.5439 1.3268 0.1029  -0.5008 -0.0152 20  VAL   T CB  
34067 C  CG1 . VAL   T  24  ? 1.8924 0.5977 1.3255 0.0871  -0.5065 -0.0141 20  VAL   T CG1 
34068 C  CG2 . VAL   T  24  ? 1.8521 0.5485 1.3134 0.1080  -0.4977 -0.0328 20  VAL   T CG2 
34069 N  N   . GLU   T  25  ? 1.9266 0.5387 1.4825 0.1616  -0.4590 0.0413  21  GLU   T N   
34070 C  CA  . GLU   T  25  ? 1.9355 0.4863 1.5493 0.2164  -0.4452 -0.0311 21  GLU   T CA  
34071 C  C   . GLU   T  25  ? 1.9710 0.3308 1.4999 0.1770  -0.4202 -0.0850 21  GLU   T C   
34072 O  O   . GLU   T  25  ? 1.9188 0.3697 1.6128 0.1815  -0.4689 -0.1964 21  GLU   T O   
34073 C  CB  . GLU   T  25  ? 1.8987 0.5897 1.6100 0.1732  -0.4265 -0.0579 21  GLU   T CB  
34074 C  CG  . GLU   T  25  ? 1.9330 0.7828 1.6133 0.2266  -0.4080 -0.0447 21  GLU   T CG  
34075 C  CD  . GLU   T  25  ? 1.9235 0.9102 1.6725 0.1816  -0.3546 -0.0119 21  GLU   T CD  
34076 O  OE1 . GLU   T  25  ? 1.9869 1.0034 1.7515 0.2940  -0.2956 -0.0190 21  GLU   T OE1 
34077 O  OE2 . GLU   T  25  ? 2.0137 1.2220 1.6783 0.3061  -0.2456 0.0022  21  GLU   T OE2 
34078 N  N   . TYR   T  26  ? 1.9481 0.2420 1.4921 0.1582  -0.4724 -0.0445 22  TYR   T N   
34079 C  CA  . TYR   T  26  ? 1.9530 0.3641 1.4617 0.1139  -0.4625 -0.0004 22  TYR   T CA  
34080 C  C   . TYR   T  26  ? 1.9201 0.3771 1.4816 0.1288  -0.4696 -0.0099 22  TYR   T C   
34081 O  O   . TYR   T  26  ? 1.9212 0.3949 1.5252 0.1390  -0.4433 -0.0309 22  TYR   T O   
34082 C  CB  . TYR   T  26  ? 1.9797 0.3992 1.4535 0.0651  -0.4511 0.0128  22  TYR   T CB  
34083 C  CG  . TYR   T  26  ? 2.0243 0.4398 1.3987 0.0256  -0.4571 0.0119  22  TYR   T CG  
34084 C  CD1 . TYR   T  26  ? 2.0579 0.3786 1.4167 0.0259  -0.4843 0.0041  22  TYR   T CD1 
34085 C  CD2 . TYR   T  26  ? 2.0355 0.4750 1.4048 -0.0160 -0.4653 -0.0042 22  TYR   T CD2 
34086 C  CE1 . TYR   T  26  ? 2.0914 0.3381 1.4014 0.0137  -0.4828 0.0589  22  TYR   T CE1 
34087 C  CE2 . TYR   T  26  ? 2.0628 0.4448 1.3872 -0.0188 -0.4709 0.0339  22  TYR   T CE2 
34088 C  CZ  . TYR   T  26  ? 2.0833 0.3742 1.4139 -0.0012 -0.5022 0.0350  22  TYR   T CZ  
34089 O  OH  . TYR   T  26  ? 2.1135 0.4040 1.3697 -0.0024 -0.4955 -0.0065 22  TYR   T OH  
34090 N  N   . ALA   T  27  ? 1.8733 0.3991 1.4758 0.1528  -0.4776 0.0021  23  ALA   T N   
34091 C  CA  . ALA   T  27  ? 1.8591 0.4420 1.4928 0.1270  -0.4740 0.0003  23  ALA   T CA  
34092 C  C   . ALA   T  27  ? 1.8610 0.4524 1.4915 0.1100  -0.4753 -0.0006 23  ALA   T C   
34093 O  O   . ALA   T  27  ? 1.8614 0.5248 1.5181 0.1088  -0.4796 -0.0377 23  ALA   T O   
34094 C  CB  . ALA   T  27  ? 1.8512 0.4705 1.4774 0.1455  -0.4625 -0.0053 23  ALA   T CB  
34095 N  N   . VAL   T  28  ? 1.8724 0.4428 1.5033 0.0810  -0.4778 -0.0055 24  VAL   T N   
34096 C  CA  . VAL   T  28  ? 1.8638 0.4351 1.5221 0.0935  -0.4819 0.0205  24  VAL   T CA  
34097 C  C   . VAL   T  28  ? 1.8685 0.3840 1.5688 0.0838  -0.5211 0.0356  24  VAL   T C   
34098 O  O   . VAL   T  28  ? 1.8441 0.2394 1.6200 0.0437  -0.5208 -0.0390 24  VAL   T O   
34099 C  CB  . VAL   T  28  ? 1.8690 0.4871 1.5131 0.1217  -0.4519 0.0267  24  VAL   T CB  
34100 C  CG1 . VAL   T  28  ? 1.9050 0.4837 1.5304 0.1426  -0.4459 0.0394  24  VAL   T CG1 
34101 C  CG2 . VAL   T  28  ? 1.8438 0.5295 1.4865 0.1153  -0.4181 0.0350  24  VAL   T CG2 
34102 N  N   . LYS   T  29  ? 1.9044 0.4437 1.5517 0.0942  -0.5369 0.0254  25  LYS   T N   
34103 C  CA  . LYS   T  29  ? 1.8698 0.5707 1.6199 0.1228  -0.5489 0.0351  25  LYS   T CA  
34104 C  C   . LYS   T  29  ? 1.8947 0.4919 1.5904 0.1149  -0.5721 0.0371  25  LYS   T C   
34105 O  O   . LYS   T  29  ? 1.8800 0.5181 1.6166 0.0943  -0.5911 0.0227  25  LYS   T O   
34106 C  CB  . LYS   T  29  ? 1.8791 0.6273 1.6272 0.0993  -0.5595 0.0184  25  LYS   T CB  
34107 C  CG  . LYS   T  29  ? 1.8859 0.6196 1.6525 0.0947  -0.5807 0.0407  25  LYS   T CG  
34108 C  CD  . LYS   T  29  ? 1.8999 0.7013 1.6847 0.0997  -0.5867 0.0989  25  LYS   T CD  
34109 C  CE  . LYS   T  29  ? 1.8593 0.8365 1.7147 0.0510  -0.5637 0.1334  25  LYS   T CE  
34110 N  NZ  . LYS   T  29  ? 1.8772 0.8959 1.7702 0.0977  -0.5697 0.1676  25  LYS   T NZ  
34111 N  N   . ALA   T  30  ? 1.8983 0.4704 1.5672 0.1236  -0.5651 0.0129  26  ALA   T N   
34112 C  CA  . ALA   T  30  ? 1.8638 0.5186 1.5936 0.1283  -0.5596 -0.0126 26  ALA   T CA  
34113 C  C   . ALA   T  30  ? 1.8717 0.5310 1.5884 0.1506  -0.5841 0.0032  26  ALA   T C   
34114 O  O   . ALA   T  30  ? 1.8548 0.5281 1.6062 0.1736  -0.5410 -0.0011 26  ALA   T O   
34115 C  CB  . ALA   T  30  ? 1.8668 0.4833 1.5611 0.1096  -0.5458 -0.0324 26  ALA   T CB  
34116 N  N   . VAL   T  31  ? 1.8887 0.5410 1.5845 0.1573  -0.5747 0.0440  27  VAL   T N   
34117 C  CA  . VAL   T  31  ? 1.9226 0.5502 1.6164 0.1200  -0.5845 0.0237  27  VAL   T CA  
34118 C  C   . VAL   T  31  ? 1.9412 0.5704 1.7107 0.1205  -0.6083 0.0484  27  VAL   T C   
34119 O  O   . VAL   T  31  ? 1.9075 0.7334 1.8458 0.1094  -0.6106 0.0299  27  VAL   T O   
34120 C  CB  . VAL   T  31  ? 1.9173 0.4870 1.5859 0.1411  -0.5970 0.0662  27  VAL   T CB  
34121 C  CG1 . VAL   T  31  ? 1.9176 0.4995 1.5688 0.1560  -0.5999 0.0864  27  VAL   T CG1 
34122 C  CG2 . VAL   T  31  ? 1.8825 0.4857 1.5464 0.1532  -0.5903 0.0232  27  VAL   T CG2 
34123 N  N   . GLU   T  32  ? 2.0151 0.5423 1.7561 0.1274  -0.5918 0.0351  28  GLU   T N   
34124 C  CA  . GLU   T  32  ? 2.0403 0.5582 1.7613 0.1212  -0.5832 0.0701  28  GLU   T CA  
34125 C  C   . GLU   T  32  ? 2.0343 0.4469 1.7912 0.0695  -0.5717 0.0477  28  GLU   T C   
34126 O  O   . GLU   T  32  ? 2.0656 0.4583 1.8047 -0.0184 -0.6337 0.0073  28  GLU   T O   
34127 C  CB  . GLU   T  32  ? 2.0202 0.6716 1.7874 0.0469  -0.5421 0.1263  28  GLU   T CB  
34128 C  CG  . GLU   T  32  ? 2.0769 0.7766 1.7617 0.0762  -0.4952 0.1480  28  GLU   T CG  
34129 C  CD  . GLU   T  32  ? 2.0728 0.8258 1.7906 0.0468  -0.4363 0.1228  28  GLU   T CD  
34130 O  OE1 . GLU   T  32  ? 2.1950 0.6697 1.9120 -0.0626 -0.4437 0.0998  28  GLU   T OE1 
34131 O  OE2 . GLU   T  32  ? 2.1036 0.9541 1.7821 0.1131  -0.4056 0.1690  28  GLU   T OE2 
34132 N  N   . ASN   T  33  ? 1.9776 0.4287 1.7962 0.1146  -0.5632 0.0687  29  ASN   T N   
34133 C  CA  . ASN   T  33  ? 1.9907 0.5523 1.8355 0.1303  -0.5382 0.0731  29  ASN   T CA  
34134 C  C   . ASN   T  33  ? 1.9319 0.5826 1.7868 0.1664  -0.5608 0.0522  29  ASN   T C   
34135 O  O   . ASN   T  33  ? 1.9200 0.6275 1.8481 0.1500  -0.5382 -0.0328 29  ASN   T O   
34136 C  CB  . ASN   T  33  ? 2.0505 0.5815 1.8372 0.1344  -0.5068 0.0993  29  ASN   T CB  
34137 C  CG  . ASN   T  33  ? 2.0903 0.6621 1.9025 0.1349  -0.4627 0.0776  29  ASN   T CG  
34138 O  OD1 . ASN   T  33  ? 2.1411 0.6055 1.8891 0.1804  -0.4730 0.1193  29  ASN   T OD1 
34139 N  ND2 . ASN   T  33  ? 2.1453 0.6383 1.9659 0.0945  -0.4563 0.0792  29  ASN   T ND2 
34140 N  N   . GLY   T  34  ? 1.8564 0.6205 1.7431 0.2281  -0.5739 0.0968  30  GLY   T N   
34141 C  CA  . GLY   T  34  ? 1.7756 0.7119 1.7414 0.1980  -0.6035 0.1366  30  GLY   T CA  
34142 C  C   . GLY   T  34  ? 1.7387 0.7769 1.7931 0.2228  -0.6399 0.1455  30  GLY   T C   
34143 O  O   . GLY   T  34  ? 1.7124 0.8153 1.7841 0.1712  -0.6653 0.1511  30  GLY   T O   
34144 N  N   . THR   T  35  ? 1.6912 0.7689 1.7820 0.2570  -0.6683 0.1605  31  THR   T N   
34145 C  CA  . THR   T  35  ? 1.7019 0.7930 1.7980 0.2793  -0.6815 0.1775  31  THR   T CA  
34146 C  C   . THR   T  35  ? 1.7127 0.7347 1.7846 0.2715  -0.6718 0.2032  31  THR   T C   
34147 O  O   . THR   T  35  ? 1.7758 0.6179 1.7131 0.2920  -0.6719 0.2732  31  THR   T O   
34148 C  CB  . THR   T  35  ? 1.6623 0.8001 1.8089 0.2995  -0.7182 0.1623  31  THR   T CB  
34149 O  OG1 . THR   T  35  ? 1.6014 0.8192 1.7442 0.3217  -0.7746 0.1644  31  THR   T OG1 
34150 C  CG2 . THR   T  35  ? 1.6539 0.8362 1.8281 0.2961  -0.7098 0.1575  31  THR   T CG2 
34151 N  N   . THR   T  36  ? 1.7667 0.8004 1.7565 0.2068  -0.6611 0.1972  32  THR   T N   
34152 C  CA  . THR   T  36  ? 1.7933 0.8122 1.7690 0.1718  -0.6371 0.2057  32  THR   T CA  
34153 C  C   . THR   T  36  ? 1.7652 0.8105 1.7748 0.1571  -0.6274 0.1994  32  THR   T C   
34154 O  O   . THR   T  36  ? 1.7683 0.7757 1.7988 0.1634  -0.6160 0.1852  32  THR   T O   
34155 C  CB  . THR   T  36  ? 1.8390 0.9101 1.7880 0.1700  -0.6448 0.2569  32  THR   T CB  
34156 O  OG1 . THR   T  36  ? 1.8508 0.9246 1.8042 0.1805  -0.6565 0.2484  32  THR   T OG1 
34157 C  CG2 . THR   T  36  ? 1.8655 0.9148 1.7608 0.1709  -0.6485 0.2693  32  THR   T CG2 
34158 N  N   . SER   T  37  ? 1.7718 0.6925 1.7656 0.1391  -0.6430 0.1749  33  SER   T N   
34159 C  CA  . SER   T  37  ? 1.8059 0.7166 1.7889 0.0832  -0.6499 0.1275  33  SER   T CA  
34160 C  C   . SER   T  37  ? 1.8170 0.6712 1.7771 0.1016  -0.6551 0.1470  33  SER   T C   
34161 O  O   . SER   T  37  ? 1.8346 0.5935 1.7953 0.1278  -0.7073 0.1771  33  SER   T O   
34162 C  CB  . SER   T  37  ? 1.8111 0.7154 1.7452 0.0395  -0.6620 0.1111  33  SER   T CB  
34163 O  OG  . SER   T  37  ? 1.8640 0.7302 1.7697 -0.0434 -0.6466 0.0291  33  SER   T OG  
34164 N  N   . ILE   T  38  ? 1.8239 0.7387 1.7639 0.1221  -0.6333 0.1196  34  ILE   T N   
34165 C  CA  . ILE   T  38  ? 1.8493 0.7663 1.7407 0.1266  -0.6415 0.1356  34  ILE   T CA  
34166 C  C   . ILE   T  38  ? 1.8437 0.7999 1.6926 0.1147  -0.6091 0.0957  34  ILE   T C   
34167 O  O   . ILE   T  38  ? 1.8114 0.7323 1.7288 0.1380  -0.5857 0.0487  34  ILE   T O   
34168 C  CB  . ILE   T  38  ? 1.8726 0.7704 1.7799 0.1214  -0.6628 0.1562  34  ILE   T CB  
34169 C  CG1 . ILE   T  38  ? 1.8705 0.8208 1.8523 0.1079  -0.6435 0.1493  34  ILE   T CG1 
34170 C  CG2 . ILE   T  38  ? 1.9148 0.7790 1.8232 0.1081  -0.6617 0.1400  34  ILE   T CG2 
34171 C  CD1 . ILE   T  38  ? 1.8986 0.8644 1.8751 0.1057  -0.6559 0.1717  34  ILE   T CD1 
34172 N  N   . GLY   T  39  ? 1.9041 0.8578 1.6294 0.1140  -0.6078 0.0857  35  GLY   T N   
34173 C  CA  . GLY   T  39  ? 1.9257 0.8604 1.5884 0.0813  -0.6039 0.0809  35  GLY   T CA  
34174 C  C   . GLY   T  39  ? 1.9443 0.8716 1.5943 0.0498  -0.6153 0.1007  35  GLY   T C   
34175 O  O   . GLY   T  39  ? 2.0011 0.8300 1.6267 0.0525  -0.6138 0.1376  35  GLY   T O   
34176 N  N   . ILE   T  40  ? 1.9067 0.8992 1.5729 0.0228  -0.6065 0.1224  36  ILE   T N   
34177 C  CA  . ILE   T  40  ? 1.8734 0.8815 1.5595 -0.0297 -0.6372 0.1329  36  ILE   T CA  
34178 C  C   . ILE   T  40  ? 1.8849 0.8763 1.4988 -0.0419 -0.6056 0.1596  36  ILE   T C   
34179 O  O   . ILE   T  40  ? 1.9240 0.8249 1.4954 -0.0202 -0.5949 0.1993  36  ILE   T O   
34180 C  CB  . ILE   T  40  ? 1.8232 0.8598 1.6079 -0.0774 -0.6488 0.0891  36  ILE   T CB  
34181 C  CG1 . ILE   T  40  ? 1.8063 0.8555 1.6406 -0.1120 -0.6423 0.0626  36  ILE   T CG1 
34182 C  CG2 . ILE   T  40  ? 1.8196 0.8486 1.6140 -0.1078 -0.6471 0.0864  36  ILE   T CG2 
34183 C  CD1 . ILE   T  40  ? 1.8133 0.8866 1.6639 -0.1248 -0.6654 0.0735  36  ILE   T CD1 
34184 N  N   . LYS   T  41  ? 1.9173 0.9087 1.4653 -0.0236 -0.5750 0.2038  37  LYS   T N   
34185 C  CA  . LYS   T  41  ? 1.9439 0.8500 1.4745 -0.0121 -0.5754 0.2434  37  LYS   T CA  
34186 C  C   . LYS   T  41  ? 1.9795 0.9547 1.5015 -0.0153 -0.6108 0.2301  37  LYS   T C   
34187 O  O   . LYS   T  41  ? 1.9917 0.9956 1.5954 0.0603  -0.6984 0.2301  37  LYS   T O   
34188 C  CB  . LYS   T  41  ? 1.9402 0.8032 1.4403 -0.0009 -0.5434 0.2674  37  LYS   T CB  
34189 C  CG  . LYS   T  41  ? 1.9014 0.8219 1.4597 -0.0217 -0.4841 0.2714  37  LYS   T CG  
34190 C  CD  . LYS   T  41  ? 1.9210 0.8303 1.4834 -0.0298 -0.4225 0.2976  37  LYS   T CD  
34191 C  CE  . LYS   T  41  ? 1.9080 0.8655 1.5342 -0.0403 -0.3539 0.2903  37  LYS   T CE  
34192 N  NZ  . LYS   T  41  ? 1.9235 0.8877 1.5660 -0.0641 -0.3175 0.3140  37  LYS   T NZ  
34193 N  N   . CYS   T  42  ? 1.9615 0.8910 1.4785 -0.0287 -0.6306 0.3131  38  CYS   T N   
34194 C  CA  . CYS   T  42  ? 1.9541 0.9663 1.4938 -0.0106 -0.6522 0.3139  38  CYS   T CA  
34195 C  C   . CYS   T  42  ? 1.9409 0.9843 1.4639 -0.0205 -0.6414 0.3171  38  CYS   T C   
34196 O  O   . CYS   T  42  ? 1.8984 0.9345 1.4221 -0.0331 -0.5944 0.2893  38  CYS   T O   
34197 C  CB  . CYS   T  42  ? 1.9253 1.1328 1.5284 0.0299  -0.6594 0.2822  38  CYS   T CB  
34198 S  SG  . CYS   T  42  ? 1.9539 1.1878 1.5701 -0.0132 -0.5903 0.2885  38  CYS   T SG  
34199 N  N   . ASN   T  43  ? 1.9527 1.0721 1.4641 0.0362  -0.6735 0.3289  39  ASN   T N   
34200 C  CA  . ASN   T  43  ? 1.9696 1.1800 1.4792 0.0557  -0.6650 0.2791  39  ASN   T CA  
34201 C  C   . ASN   T  43  ? 1.9481 1.1702 1.5193 0.1192  -0.6637 0.2180  39  ASN   T C   
34202 O  O   . ASN   T  43  ? 1.9652 1.2511 1.5950 0.1016  -0.5737 0.0966  39  ASN   T O   
34203 C  CB  . ASN   T  43  ? 1.9868 1.2481 1.4545 0.0659  -0.6648 0.2665  39  ASN   T CB  
34204 C  CG  . ASN   T  43  ? 2.0190 1.3225 1.4457 0.0449  -0.6748 0.2977  39  ASN   T CG  
34205 O  OD1 . ASN   T  43  ? 1.9789 1.4269 1.4242 0.0308  -0.6444 0.2702  39  ASN   T OD1 
34206 N  ND2 . ASN   T  43  ? 2.0202 1.4093 1.5318 0.0168  -0.6940 0.2859  39  ASN   T ND2 
34207 N  N   . ASP   T  44  ? 2.0190 1.0833 1.5380 0.1137  -0.6890 0.2385  40  ASP   T N   
34208 C  CA  . ASP   T  44  ? 2.0935 1.0719 1.5066 0.1229  -0.7163 0.2198  40  ASP   T CA  
34209 C  C   . ASP   T  44  ? 2.1595 0.9987 1.4826 0.1147  -0.7365 0.1605  40  ASP   T C   
34210 O  O   . ASP   T  44  ? 2.1937 0.9939 1.4320 0.0814  -0.7258 0.1154  40  ASP   T O   
34211 C  CB  . ASP   T  44  ? 2.1261 1.1121 1.5144 0.1460  -0.8052 0.2260  40  ASP   T CB  
34212 C  CG  . ASP   T  44  ? 2.1350 1.1805 1.5622 0.2683  -0.8540 0.2894  40  ASP   T CG  
34213 O  OD1 . ASP   T  44  ? 2.1779 1.1091 1.6179 0.2433  -0.9302 0.2652  40  ASP   T OD1 
34214 O  OD2 . ASP   T  44  ? 2.1852 1.2392 1.5453 0.2372  -0.9438 0.3366  40  ASP   T OD2 
34215 N  N   . GLY   T  45  ? 2.1833 0.8934 1.4792 0.0836  -0.7173 0.2431  41  GLY   T N   
34216 C  CA  . GLY   T  45  ? 2.1369 0.7674 1.5112 0.0665  -0.6710 0.2085  41  GLY   T CA  
34217 C  C   . GLY   T  45  ? 2.0877 0.6517 1.5298 0.0662  -0.6725 0.3153  41  GLY   T C   
34218 O  O   . GLY   T  45  ? 2.0978 0.4747 1.5800 0.1212  -0.7451 0.3041  41  GLY   T O   
34219 N  N   . VAL   T  46  ? 2.0319 0.5304 1.5454 0.0557  -0.6814 0.2380  42  VAL   T N   
34220 C  CA  . VAL   T  46  ? 1.9989 0.5751 1.5900 0.0558  -0.6367 0.1953  42  VAL   T CA  
34221 C  C   . VAL   T  46  ? 1.9379 0.5905 1.5535 0.0143  -0.7061 0.1822  42  VAL   T C   
34222 O  O   . VAL   T  46  ? 1.8974 0.4593 1.5720 0.1142  -0.7017 0.1487  42  VAL   T O   
34223 C  CB  . VAL   T  46  ? 2.0437 0.6523 1.6010 0.0359  -0.6411 0.1620  42  VAL   T CB  
34224 C  CG1 . VAL   T  46  ? 2.0792 0.6894 1.6450 0.0177  -0.5859 0.1649  42  VAL   T CG1 
34225 C  CG2 . VAL   T  46  ? 2.0866 0.6435 1.6079 -0.0122 -0.5746 0.1381  42  VAL   T CG2 
34226 N  N   . VAL   T  47  ? 1.8833 0.6440 1.5371 0.0571  -0.7051 0.1527  43  VAL   T N   
34227 C  CA  . VAL   T  47  ? 1.8383 0.6503 1.5237 0.0540  -0.7477 0.1815  43  VAL   T CA  
34228 C  C   . VAL   T  47  ? 1.8702 0.6185 1.5741 0.0655  -0.6839 0.1501  43  VAL   T C   
34229 O  O   . VAL   T  47  ? 1.9212 0.6329 1.6302 0.0389  -0.6477 0.1536  43  VAL   T O   
34230 C  CB  . VAL   T  47  ? 1.8041 0.6430 1.5358 0.0413  -0.7650 0.1729  43  VAL   T CB  
34231 C  CG1 . VAL   T  47  ? 1.7952 0.6223 1.5199 0.0559  -0.7865 0.1749  43  VAL   T CG1 
34232 C  CG2 . VAL   T  47  ? 1.8008 0.6649 1.5191 0.0331  -0.7792 0.1821  43  VAL   T CG2 
34233 N  N   . PHE   T  48  ? 1.8487 0.6460 1.6073 0.0906  -0.6615 0.1587  44  PHE   T N   
34234 C  CA  . PHE   T  48  ? 1.8305 0.6432 1.6057 0.1258  -0.6865 0.1630  44  PHE   T CA  
34235 C  C   . PHE   T  48  ? 1.8431 0.6276 1.6308 0.1509  -0.6900 0.2203  44  PHE   T C   
34236 O  O   . PHE   T  48  ? 1.8727 0.5440 1.6295 0.1397  -0.6914 0.2850  44  PHE   T O   
34237 C  CB  . PHE   T  48  ? 1.8061 0.6522 1.5911 0.1365  -0.7009 0.1407  44  PHE   T CB  
34238 C  CG  . PHE   T  48  ? 1.8063 0.6769 1.5707 0.1531  -0.7273 0.1470  44  PHE   T CG  
34239 C  CD1 . PHE   T  48  ? 1.8122 0.6464 1.5732 0.1581  -0.7458 0.1590  44  PHE   T CD1 
34240 C  CD2 . PHE   T  48  ? 1.7953 0.6856 1.5524 0.1381  -0.7339 0.1416  44  PHE   T CD2 
34241 C  CE1 . PHE   T  48  ? 1.8037 0.6691 1.5274 0.1590  -0.7538 0.1638  44  PHE   T CE1 
34242 C  CE2 . PHE   T  48  ? 1.7975 0.7229 1.5152 0.1418  -0.7281 0.1243  44  PHE   T CE2 
34243 C  CZ  . PHE   T  48  ? 1.8019 0.6990 1.4870 0.1504  -0.7563 0.1246  44  PHE   T CZ  
34244 N  N   . ALA   T  49  ? 1.8407 0.6298 1.6360 0.2003  -0.6912 0.2253  45  ALA   T N   
34245 C  CA  . ALA   T  49  ? 1.8521 0.6540 1.6700 0.2164  -0.6787 0.2234  45  ALA   T CA  
34246 C  C   . ALA   T  49  ? 1.8244 0.6512 1.6991 0.2141  -0.6460 0.1968  45  ALA   T C   
34247 O  O   . ALA   T  49  ? 1.8150 0.6165 1.6830 0.2351  -0.6547 0.1733  45  ALA   T O   
34248 C  CB  . ALA   T  49  ? 1.8656 0.6696 1.6919 0.2148  -0.7026 0.2327  45  ALA   T CB  
34249 N  N   . VAL   T  50  ? 1.8622 0.7238 1.7631 0.2137  -0.5976 0.1918  46  VAL   T N   
34250 C  CA  . VAL   T  50  ? 1.8691 0.7441 1.8034 0.2281  -0.5876 0.1594  46  VAL   T CA  
34251 C  C   . VAL   T  50  ? 1.9086 0.7317 1.9040 0.2754  -0.5974 0.1842  46  VAL   T C   
34252 O  O   . VAL   T  50  ? 1.8929 0.7159 1.8926 0.3058  -0.6236 0.2054  46  VAL   T O   
34253 C  CB  . VAL   T  50  ? 1.8404 0.7431 1.7877 0.2185  -0.5747 0.1522  46  VAL   T CB  
34254 C  CG1 . VAL   T  50  ? 1.8537 0.6902 1.7829 0.2225  -0.5665 0.0907  46  VAL   T CG1 
34255 C  CG2 . VAL   T  50  ? 1.8420 0.7808 1.7862 0.2140  -0.5594 0.1443  46  VAL   T CG2 
34256 N  N   . GLU   T  51  ? 1.9173 0.7198 1.9965 0.3360  -0.5775 0.1594  47  GLU   T N   
34257 C  CA  . GLU   T  51  ? 1.9050 0.8606 2.0909 0.3723  -0.5624 0.1327  47  GLU   T CA  
34258 C  C   . GLU   T  51  ? 1.8337 0.7369 2.0877 0.3419  -0.5600 0.0998  47  GLU   T C   
34259 O  O   . GLU   T  51  ? 1.8496 0.6768 2.0606 0.3918  -0.5573 0.1382  47  GLU   T O   
34260 C  CB  . GLU   T  51  ? 1.9341 0.8562 2.2207 0.3969  -0.5553 0.1325  47  GLU   T CB  
34261 C  CG  . GLU   T  51  ? 1.9522 1.0040 2.3233 0.4814  -0.5304 0.1169  47  GLU   T CG  
34262 C  CD  . GLU   T  51  ? 1.9892 1.0339 2.4300 0.4534  -0.5216 0.1188  47  GLU   T CD  
34263 O  OE1 . GLU   T  51  ? 2.0945 1.1037 2.5242 0.5201  -0.4794 0.0512  47  GLU   T OE1 
34264 O  OE2 . GLU   T  51  ? 1.9366 1.1208 2.4510 0.5908  -0.5156 0.1840  47  GLU   T OE2 
34265 N  N   . LYS   T  52  ? 1.8602 0.7159 2.0507 0.2927  -0.5579 0.0719  48  LYS   T N   
34266 C  CA  . LYS   T  52  ? 1.8878 0.8208 2.0059 0.2575  -0.5738 0.0357  48  LYS   T CA  
34267 C  C   . LYS   T  52  ? 1.9496 0.7360 2.0444 0.2196  -0.5496 0.0057  48  LYS   T C   
34268 O  O   . LYS   T  52  ? 1.9573 0.6339 2.1181 0.1443  -0.5530 0.0026  48  LYS   T O   
34269 C  CB  . LYS   T  52  ? 1.8513 0.8823 1.9631 0.2222  -0.5757 0.0140  48  LYS   T CB  
34270 C  CG  . LYS   T  52  ? 1.8183 0.9474 1.9111 0.2463  -0.5874 0.0183  48  LYS   T CG  
34271 C  CD  . LYS   T  52  ? 1.8274 1.0590 1.8813 0.1587  -0.5921 0.0131  48  LYS   T CD  
34272 C  CE  . LYS   T  52  ? 1.8249 1.1689 1.8327 0.1457  -0.5921 -0.0100 48  LYS   T CE  
34273 N  NZ  . LYS   T  52  ? 1.8399 1.2166 1.7822 0.1229  -0.5856 -0.0427 48  LYS   T NZ  
34274 N  N   . LEU   T  53  ? 1.9856 0.8593 1.9988 0.2236  -0.5694 -0.0428 49  LEU   T N   
34275 C  CA  . LEU   T  53  ? 2.0024 0.8853 2.0264 0.2544  -0.5672 -0.0429 49  LEU   T CA  
34276 C  C   . LEU   T  53  ? 1.9601 0.8697 1.9958 0.2729  -0.5858 -0.0502 49  LEU   T C   
34277 O  O   . LEU   T  53  ? 1.9173 0.7017 1.9636 0.1480  -0.5814 -0.0955 49  LEU   T O   
34278 C  CB  . LEU   T  53  ? 2.0785 0.7901 2.0169 0.3006  -0.5434 -0.0682 49  LEU   T CB  
34279 C  CG  . LEU   T  53  ? 2.1029 0.7806 2.0126 0.3111  -0.5235 -0.0729 49  LEU   T CG  
34280 C  CD1 . LEU   T  53  ? 2.1069 0.7890 1.9942 0.3426  -0.5187 -0.0921 49  LEU   T CD1 
34281 C  CD2 . LEU   T  53  ? 2.1601 0.9144 2.0178 0.3235  -0.5498 -0.0449 49  LEU   T CD2 
34282 N  N   . ILE   T  54  ? 1.9369 0.9382 2.1082 0.3205  -0.5495 -0.0760 50  ILE   T N   
34283 C  CA  . ILE   T  54  ? 1.9479 0.9676 2.1664 0.3382  -0.5122 -0.0693 50  ILE   T CA  
34284 C  C   . ILE   T  54  ? 1.9114 1.0941 2.1724 0.3520  -0.5032 -0.1179 50  ILE   T C   
34285 O  O   . ILE   T  54  ? 1.9081 1.1863 2.3135 0.4305  -0.5095 -0.1421 50  ILE   T O   
34286 C  CB  . ILE   T  54  ? 1.9659 0.9728 2.1987 0.3404  -0.5310 -0.0752 50  ILE   T CB  
34287 C  CG1 . ILE   T  54  ? 1.9991 1.0400 2.1395 0.3368  -0.5370 -0.0597 50  ILE   T CG1 
34288 C  CG2 . ILE   T  54  ? 1.9738 0.9223 2.2104 0.3622  -0.5064 -0.0899 50  ILE   T CG2 
34289 C  CD1 . ILE   T  54  ? 2.0329 1.1365 2.1491 0.3492  -0.5585 -0.0419 50  ILE   T CD1 
34290 N  N   . THR   T  55  ? 1.8234 1.0483 2.2042 0.3642  -0.4908 -0.0591 51  THR   T N   
34291 C  CA  . THR   T  55  ? 1.8069 1.0835 2.2061 0.3451  -0.4667 -0.0660 51  THR   T CA  
34292 C  C   . THR   T  55  ? 1.8246 1.1352 2.2678 0.3028  -0.4052 -0.0647 51  THR   T C   
34293 O  O   . THR   T  55  ? 1.9495 1.1704 2.3474 0.3268  -0.3752 -0.1163 51  THR   T O   
34294 C  CB  . THR   T  55  ? 1.6968 1.0619 2.1963 0.3326  -0.4448 -0.0792 51  THR   T CB  
34295 O  OG1 . THR   T  55  ? 1.6598 1.0947 2.1729 0.3164  -0.4785 -0.0760 51  THR   T OG1 
34296 C  CG2 . THR   T  55  ? 1.6731 1.0755 2.1901 0.3306  -0.4375 -0.0839 51  THR   T CG2 
34297 N  N   . SER   T  56  ? 1.9197 1.0816 2.2491 0.2899  -0.3704 -0.0215 52  SER   T N   
34298 C  CA  . SER   T  56  ? 1.9449 1.0636 2.2898 0.2068  -0.3321 -0.0083 52  SER   T CA  
34299 C  C   . SER   T  56  ? 1.9417 0.9674 2.3069 0.2448  -0.3191 -0.0156 52  SER   T C   
34300 O  O   . SER   T  56  ? 1.9028 0.9058 2.3274 0.2776  -0.3503 0.0333  52  SER   T O   
34301 C  CB  . SER   T  56  ? 1.9712 1.0747 2.3018 0.1591  -0.2899 0.0051  52  SER   T CB  
34302 O  OG  . SER   T  56  ? 2.0249 1.1283 2.3106 0.0764  -0.2508 0.0226  52  SER   T OG  
34303 N  N   . LYS   T  57  ? 1.9392 1.0067 2.3635 0.2284  -0.3541 0.0122  53  LYS   T N   
34304 C  CA  . LYS   T  57  ? 1.9255 0.9726 2.3461 0.2576  -0.3725 0.0336  53  LYS   T CA  
34305 C  C   . LYS   T  57  ? 1.9118 0.9018 2.2727 0.2896  -0.3774 -0.0600 53  LYS   T C   
34306 O  O   . LYS   T  57  ? 1.8431 0.6858 2.2592 0.3959  -0.3823 0.0329  53  LYS   T O   
34307 C  CB  . LYS   T  57  ? 1.8940 1.1584 2.4367 0.2456  -0.3548 0.0081  53  LYS   T CB  
34308 C  CG  . LYS   T  57  ? 1.8568 1.2921 2.4369 0.2352  -0.3751 0.0470  53  LYS   T CG  
34309 C  CD  . LYS   T  57  ? 1.8238 1.4165 2.4380 0.2034  -0.3602 0.0162  53  LYS   T CD  
34310 C  CE  . LYS   T  57  ? 1.7958 1.5113 2.4168 0.1807  -0.4026 0.0217  53  LYS   T CE  
34311 N  NZ  . LYS   T  57  ? 1.7903 1.5715 2.4153 0.1642  -0.4087 0.0115  53  LYS   T NZ  
34312 N  N   . LEU   T  58  ? 1.9550 0.7917 2.2497 0.3030  -0.3597 -0.0647 54  LEU   T N   
34313 C  CA  . LEU   T  58  ? 1.9703 0.8075 2.1847 0.2502  -0.3738 -0.0750 54  LEU   T CA  
34314 C  C   . LEU   T  58  ? 1.9057 0.9140 2.0586 0.2606  -0.4038 -0.0599 54  LEU   T C   
34315 O  O   . LEU   T  58  ? 1.8958 0.9358 1.9310 0.2553  -0.4444 -0.0541 54  LEU   T O   
34316 C  CB  . LEU   T  58  ? 1.9921 0.6813 2.2079 0.2498  -0.3541 -0.1080 54  LEU   T CB  
34317 C  CG  . LEU   T  58  ? 2.0306 0.6413 2.3053 0.2472  -0.3306 -0.1319 54  LEU   T CG  
34318 C  CD1 . LEU   T  58  ? 2.0652 0.6698 2.3234 0.2175  -0.3229 -0.1526 54  LEU   T CD1 
34319 C  CD2 . LEU   T  58  ? 2.0421 0.5873 2.3134 0.2551  -0.3286 -0.1434 54  LEU   T CD2 
34320 N  N   . LEU   T  59  ? 1.8845 0.9636 2.0576 0.2355  -0.4416 -0.0251 55  LEU   T N   
34321 C  CA  . LEU   T  59  ? 1.8749 0.9394 2.0429 0.2541  -0.4498 0.0250  55  LEU   T CA  
34322 C  C   . LEU   T  59  ? 1.8808 0.9529 2.0889 0.2825  -0.4501 -0.0151 55  LEU   T C   
34323 O  O   . LEU   T  59  ? 1.9462 0.9873 2.1307 0.3462  -0.4648 -0.0080 55  LEU   T O   
34324 C  CB  . LEU   T  59  ? 1.9033 0.9254 2.0091 0.2358  -0.4702 0.0402  55  LEU   T CB  
34325 C  CG  . LEU   T  59  ? 1.9158 0.9503 1.9554 0.2345  -0.4736 0.0558  55  LEU   T CG  
34326 C  CD1 . LEU   T  59  ? 1.9210 1.0816 1.9509 0.2077  -0.4445 0.0567  55  LEU   T CD1 
34327 C  CD2 . LEU   T  59  ? 1.9141 0.8536 1.9054 0.2095  -0.4291 0.0605  55  LEU   T CD2 
34328 N  N   . VAL   T  60  ? 1.8470 0.9662 2.0788 0.2905  -0.4312 0.0310  56  VAL   T N   
34329 C  CA  . VAL   T  60  ? 1.8345 0.9464 2.0635 0.2892  -0.4206 0.0495  56  VAL   T CA  
34330 C  C   . VAL   T  60  ? 1.8191 0.8657 2.0532 0.2654  -0.4375 0.0922  56  VAL   T C   
34331 O  O   . VAL   T  60  ? 1.8314 0.6511 1.9926 0.3136  -0.4568 0.1725  56  VAL   T O   
34332 C  CB  . VAL   T  60  ? 1.8144 0.9624 2.0148 0.3300  -0.4122 0.0513  56  VAL   T CB  
34333 C  CG1 . VAL   T  60  ? 1.8176 1.0233 2.0000 0.3288  -0.4142 0.0253  56  VAL   T CG1 
34334 C  CG2 . VAL   T  60  ? 1.8143 1.0152 2.0229 0.3526  -0.4005 0.0357  56  VAL   T CG2 
34335 N  N   . PRO   T  61  ? 1.8768 0.9283 2.0540 0.1980  -0.4798 0.0755  57  PRO   T N   
34336 C  CA  . PRO   T  61  ? 1.9004 0.9634 2.0478 0.1852  -0.4834 0.0818  57  PRO   T CA  
34337 C  C   . PRO   T  61  ? 1.9402 0.9630 2.0439 0.1938  -0.4705 0.0903  57  PRO   T C   
34338 O  O   . PRO   T  61  ? 1.9518 1.0153 2.0708 0.1784  -0.4509 0.1428  57  PRO   T O   
34339 C  CB  . PRO   T  61  ? 1.8953 0.9955 2.0759 0.1627  -0.5101 0.0679  57  PRO   T CB  
34340 C  CG  . PRO   T  61  ? 1.9035 1.0185 2.0992 0.1644  -0.5041 0.0533  57  PRO   T CG  
34341 C  CD  . PRO   T  61  ? 1.8656 0.9765 2.0934 0.1694  -0.4950 0.0417  57  PRO   T CD  
34342 N  N   . GLN   T  62  ? 1.9646 1.0567 2.0397 0.1740  -0.4554 0.1311  58  GLN   T N   
34343 C  CA  . GLN   T  62  ? 1.9624 1.1578 2.0109 0.2037  -0.4152 0.1131  58  GLN   T CA  
34344 C  C   . GLN   T  62  ? 2.0120 1.2344 1.9556 0.2253  -0.4271 0.0863  58  GLN   T C   
34345 O  O   . GLN   T  62  ? 2.0177 1.4098 1.9983 0.2905  -0.2915 0.0258  58  GLN   T O   
34346 C  CB  . GLN   T  62  ? 1.9397 1.2354 1.9322 0.2029  -0.4316 0.1437  58  GLN   T CB  
34347 C  CG  . GLN   T  62  ? 1.9417 1.2768 1.9321 0.1854  -0.4468 0.1682  58  GLN   T CG  
34348 C  CD  . GLN   T  62  ? 1.9862 1.3145 1.9893 0.1964  -0.4637 0.2206  58  GLN   T CD  
34349 O  OE1 . GLN   T  62  ? 1.9719 1.4212 2.0105 0.1821  -0.4221 0.2558  58  GLN   T OE1 
34350 N  NE2 . GLN   T  62  ? 1.9614 1.4191 2.0150 0.1757  -0.4362 0.2103  58  GLN   T NE2 
34351 N  N   . LYS   T  63  ? 2.0559 1.1561 1.9877 0.1927  -0.5154 0.0025  59  LYS   T N   
34352 C  CA  . LYS   T  63  ? 2.0546 1.1007 1.9966 0.1884  -0.5429 -0.0214 59  LYS   T CA  
34353 C  C   . LYS   T  63  ? 2.0227 0.8480 1.9961 0.2306  -0.5226 -0.0025 59  LYS   T C   
34354 O  O   . LYS   T  63  ? 2.0725 0.9122 2.0053 0.3179  -0.5630 0.0032  59  LYS   T O   
34355 C  CB  . LYS   T  63  ? 2.0567 1.1856 2.0699 0.1181  -0.5423 -0.0308 59  LYS   T CB  
34356 C  CG  . LYS   T  63  ? 2.1096 1.2269 2.1544 0.0084  -0.5118 0.0151  59  LYS   T CG  
34357 C  CD  . LYS   T  63  ? 2.1137 1.2397 2.2240 -0.0119 -0.4903 -0.0129 59  LYS   T CD  
34358 C  CE  . LYS   T  63  ? 2.1605 1.4479 2.2175 -0.0797 -0.4535 0.0452  59  LYS   T CE  
34359 N  NZ  . LYS   T  63  ? 2.1548 1.6108 2.3088 -0.1273 -0.4557 -0.0077 59  LYS   T NZ  
34360 N  N   . ASN   T  64  ? 1.9658 0.7325 1.9668 0.3037  -0.5353 -0.0163 60  ASN   T N   
34361 C  CA  . ASN   T  64  ? 1.9356 0.5734 1.8676 0.3253  -0.4996 0.0081  60  ASN   T CA  
34362 C  C   . ASN   T  64  ? 1.9303 0.5836 1.8132 0.3632  -0.5201 0.0481  60  ASN   T C   
34363 O  O   . ASN   T  64  ? 1.9606 0.4313 1.8426 0.4371  -0.5171 -0.0501 60  ASN   T O   
34364 C  CB  . ASN   T  64  ? 1.9127 0.5236 1.8818 0.2371  -0.5270 0.0218  60  ASN   T CB  
34365 C  CG  . ASN   T  64  ? 1.9132 0.3748 1.8622 0.2102  -0.5331 -0.0212 60  ASN   T CG  
34366 O  OD1 . ASN   T  64  ? 1.8708 0.3573 1.8444 0.1551  -0.5264 -0.0206 60  ASN   T OD1 
34367 N  ND2 . ASN   T  64  ? 1.9375 0.3278 1.8896 0.2075  -0.5089 -0.0793 60  ASN   T ND2 
34368 N  N   . VAL   T  65  ? 1.9215 0.6591 1.7052 0.4525  -0.5269 0.0514  61  VAL   T N   
34369 C  CA  . VAL   T  65  ? 1.9215 0.7710 1.6643 0.4369  -0.5433 0.0665  61  VAL   T CA  
34370 C  C   . VAL   T  65  ? 1.9201 0.7808 1.6670 0.4240  -0.5329 0.0684  61  VAL   T C   
34371 O  O   . VAL   T  65  ? 1.9300 0.8076 1.6183 0.4166  -0.4940 0.0231  61  VAL   T O   
34372 C  CB  . VAL   T  65  ? 1.9273 0.8187 1.6243 0.4196  -0.5233 -0.0019 61  VAL   T CB  
34373 C  CG1 . VAL   T  65  ? 1.9391 0.9062 1.6069 0.3714  -0.5185 0.0056  61  VAL   T CG1 
34374 C  CG2 . VAL   T  65  ? 1.8977 0.8605 1.6598 0.4549  -0.5253 0.0098  61  VAL   T CG2 
34375 N  N   . LYS   T  66  ? 1.9451 0.7982 1.6217 0.4052  -0.5828 0.0937  62  LYS   T N   
34376 C  CA  . LYS   T  66  ? 1.9907 0.8315 1.6076 0.3727  -0.5743 0.0310  62  LYS   T CA  
34377 C  C   . LYS   T  66  ? 2.0132 0.7798 1.5906 0.3466  -0.5646 0.0063  62  LYS   T C   
34378 O  O   . LYS   T  66  ? 1.9692 0.7598 1.6376 0.3869  -0.5318 -0.0867 62  LYS   T O   
34379 C  CB  . LYS   T  66  ? 2.0716 0.8368 1.6625 0.3907  -0.6008 0.0376  62  LYS   T CB  
34380 C  CG  . LYS   T  66  ? 2.0988 1.0197 1.6876 0.3591  -0.5595 -0.0254 62  LYS   T CG  
34381 C  CD  . LYS   T  66  ? 2.2197 1.0351 1.7771 0.2512  -0.5637 -0.0442 62  LYS   T CD  
34382 C  CE  . LYS   T  66  ? 2.2524 1.2392 1.7803 0.2142  -0.5945 -0.0793 62  LYS   T CE  
34383 N  NZ  . LYS   T  66  ? 2.2978 1.2343 1.8333 0.1712  -0.6083 -0.0731 62  LYS   T NZ  
34384 N  N   . ILE   T  67  ? 1.9450 0.7458 1.5959 0.3008  -0.5808 0.0137  63  ILE   T N   
34385 C  CA  . ILE   T  67  ? 1.8936 0.8003 1.5285 0.2327  -0.5848 -0.0121 63  ILE   T CA  
34386 C  C   . ILE   T  67  ? 1.8268 0.7698 1.4970 0.2082  -0.5615 -0.0486 63  ILE   T C   
34387 O  O   . ILE   T  67  ? 1.8022 0.8721 1.4660 0.1656  -0.5630 -0.1631 63  ILE   T O   
34388 C  CB  . ILE   T  67  ? 1.8974 0.8163 1.5439 0.2231  -0.6165 0.0176  63  ILE   T CB  
34389 C  CG1 . ILE   T  67  ? 1.9410 0.8183 1.5986 0.2611  -0.6261 0.0224  63  ILE   T CG1 
34390 C  CG2 . ILE   T  67  ? 1.8604 0.8455 1.5149 0.2144  -0.6305 0.0144  63  ILE   T CG2 
34391 C  CD1 . ILE   T  67  ? 1.9707 0.8683 1.6033 0.2701  -0.6376 0.0384  63  ILE   T CD1 
34392 N  N   . GLN   T  68  ? 1.8253 0.6284 1.4570 0.1877  -0.5324 -0.0099 64  GLN   T N   
34393 C  CA  . GLN   T  68  ? 1.8530 0.6578 1.4330 0.1496  -0.5221 0.0529  64  GLN   T CA  
34394 C  C   . GLN   T  68  ? 1.8706 0.6191 1.3895 0.1579  -0.5274 0.1049  64  GLN   T C   
34395 O  O   . GLN   T  68  ? 1.9025 0.8454 1.4773 0.1202  -0.5110 0.2005  64  GLN   T O   
34396 C  CB  . GLN   T  68  ? 1.8449 0.4974 1.4203 0.1448  -0.4998 0.0331  64  GLN   T CB  
34397 C  CG  . GLN   T  68  ? 1.8350 0.4829 1.4630 0.1361  -0.4802 0.0251  64  GLN   T CG  
34398 C  CD  . GLN   T  68  ? 1.8441 0.5056 1.4701 0.1259  -0.4873 0.0505  64  GLN   T CD  
34399 O  OE1 . GLN   T  68  ? 1.8158 0.5781 1.4906 0.0828  -0.5108 0.0631  64  GLN   T OE1 
34400 N  NE2 . GLN   T  68  ? 1.8500 0.4560 1.4705 0.0563  -0.4562 0.0110  64  GLN   T NE2 
34401 N  N   . VAL   T  69  ? 1.8773 0.6209 1.3103 0.1147  -0.5315 0.0973  65  VAL   T N   
34402 C  CA  . VAL   T  69  ? 1.9152 0.5801 1.2982 0.0755  -0.5126 0.0885  65  VAL   T CA  
34403 C  C   . VAL   T  69  ? 1.8707 0.5451 1.2504 0.0507  -0.4989 0.0551  65  VAL   T C   
34404 O  O   . VAL   T  69  ? 1.8273 0.5479 1.2426 0.0561  -0.5129 0.0553  65  VAL   T O   
34405 C  CB  . VAL   T  69  ? 1.9647 0.6078 1.3058 0.0203  -0.4873 0.1099  65  VAL   T CB  
34406 C  CG1 . VAL   T  69  ? 1.9898 0.6201 1.3167 0.0156  -0.4359 0.0847  65  VAL   T CG1 
34407 C  CG2 . VAL   T  69  ? 1.9889 0.6253 1.2863 0.0262  -0.4583 0.1424  65  VAL   T CG2 
34408 N  N   . VAL   T  70  ? 1.8402 0.5028 1.2634 0.0810  -0.5291 0.0462  66  VAL   T N   
34409 C  CA  . VAL   T  70  ? 1.8217 0.5100 1.2949 0.0917  -0.5050 0.0501  66  VAL   T CA  
34410 C  C   . VAL   T  70  ? 1.8200 0.5354 1.2650 0.0611  -0.4970 0.0452  66  VAL   T C   
34411 O  O   . VAL   T  70  ? 1.8011 0.6771 1.2887 0.0682  -0.5409 0.1312  66  VAL   T O   
34412 C  CB  . VAL   T  70  ? 1.8325 0.4255 1.3497 0.1083  -0.4830 0.0476  66  VAL   T CB  
34413 C  CG1 . VAL   T  70  ? 1.8025 0.4897 1.3748 0.1260  -0.4681 0.0057  66  VAL   T CG1 
34414 C  CG2 . VAL   T  70  ? 1.8270 0.3730 1.3696 0.1069  -0.4787 0.0689  66  VAL   T CG2 
34415 N  N   . ASP   T  71  ? 1.8322 0.4991 1.2639 0.0408  -0.4725 0.0204  67  ASP   T N   
34416 C  CA  . ASP   T  71  ? 1.8251 0.4967 1.2472 0.0748  -0.4920 0.0244  67  ASP   T CA  
34417 C  C   . ASP   T  71  ? 1.8315 0.4797 1.2049 0.0990  -0.4974 0.0191  67  ASP   T C   
34418 O  O   . ASP   T  71  ? 1.7993 0.4062 1.1425 0.1453  -0.5522 0.0112  67  ASP   T O   
34419 C  CB  . ASP   T  71  ? 1.8647 0.4181 1.2652 0.0554  -0.4610 -0.0074 67  ASP   T CB  
34420 C  CG  . ASP   T  71  ? 1.9211 0.3674 1.2811 -0.0440 -0.4833 -0.0401 67  ASP   T CG  
34421 O  OD1 . ASP   T  71  ? 2.0269 0.2307 1.3392 -0.0680 -0.4273 -0.0847 67  ASP   T OD1 
34422 O  OD2 . ASP   T  71  ? 1.9929 0.1807 1.3675 0.0420  -0.4191 0.0082  67  ASP   T OD2 
34423 N  N   . ARG   T  72  ? 1.7882 0.5380 1.1905 0.0838  -0.5260 0.0426  68  ARG   T N   
34424 C  CA  . ARG   T  72  ? 1.7858 0.6193 1.2083 0.0459  -0.5280 0.0357  68  ARG   T CA  
34425 C  C   . ARG   T  72  ? 1.7855 0.6073 1.2009 0.0320  -0.5574 0.0317  68  ARG   T C   
34426 O  O   . ARG   T  72  ? 1.7832 0.5533 1.2001 0.0876  -0.5506 0.0823  68  ARG   T O   
34427 C  CB  . ARG   T  72  ? 1.7782 0.6287 1.1939 0.0660  -0.5420 0.0144  68  ARG   T CB  
34428 C  CG  . ARG   T  72  ? 1.7734 0.6997 1.2310 0.0490  -0.5273 -0.0042 68  ARG   T CG  
34429 C  CD  . ARG   T  72  ? 1.7691 0.6892 1.2402 0.0413  -0.5471 -0.0223 68  ARG   T CD  
34430 N  NE  . ARG   T  72  ? 1.7640 0.7968 1.2407 0.0015  -0.5765 -0.0791 68  ARG   T NE  
34431 C  CZ  . ARG   T  72  ? 1.7467 0.7867 1.2658 -0.0180 -0.5991 -0.0995 68  ARG   T CZ  
34432 N  NH1 . ARG   T  72  ? 1.7737 0.8467 1.2658 0.0025  -0.5440 -0.0873 68  ARG   T NH1 
34433 N  NH2 . ARG   T  72  ? 1.7401 0.8226 1.2994 -0.0409 -0.6253 -0.1212 68  ARG   T NH2 
34434 N  N   . HIS   T  73  ? 1.8521 0.5555 1.2531 0.0005  -0.5189 0.0476  69  HIS   T N   
34435 C  CA  . HIS   T  73  ? 1.8933 0.5342 1.2889 -0.0301 -0.5220 0.0687  69  HIS   T CA  
34436 C  C   . HIS   T  73  ? 1.9110 0.5126 1.3236 0.0056  -0.4973 0.0702  69  HIS   T C   
34437 O  O   . HIS   T  73  ? 1.9861 0.4747 1.3820 0.0262  -0.4387 0.0845  69  HIS   T O   
34438 C  CB  . HIS   T  73  ? 1.8856 0.4958 1.3066 -0.0740 -0.4993 0.0722  69  HIS   T CB  
34439 C  CG  . HIS   T  73  ? 1.8680 0.4471 1.3827 -0.1436 -0.4955 0.0501  69  HIS   T CG  
34440 N  ND1 . HIS   T  73  ? 1.9022 0.4471 1.3932 -0.1669 -0.4687 0.0634  69  HIS   T ND1 
34441 C  CD2 . HIS   T  73  ? 1.9168 0.4403 1.4116 -0.1814 -0.4625 0.0536  69  HIS   T CD2 
34442 C  CE1 . HIS   T  73  ? 1.9210 0.3713 1.4054 -0.2093 -0.4741 0.0528  69  HIS   T CE1 
34443 N  NE2 . HIS   T  73  ? 1.9141 0.4079 1.4081 -0.2179 -0.4605 0.0419  69  HIS   T NE2 
34444 N  N   . ILE   T  74  ? 1.8786 0.5359 1.3183 0.0251  -0.4893 0.0738  70  ILE   T N   
34445 C  CA  . ILE   T  74  ? 1.8276 0.5448 1.3179 0.0155  -0.5016 0.0728  70  ILE   T CA  
34446 C  C   . ILE   T  74  ? 1.8496 0.5623 1.3313 0.0130  -0.4817 0.0493  70  ILE   T C   
34447 O  O   . ILE   T  74  ? 1.9012 0.5317 1.2968 0.0103  -0.4826 0.0435  70  ILE   T O   
34448 C  CB  . ILE   T  74  ? 1.8069 0.4814 1.3319 -0.0043 -0.4989 0.0455  70  ILE   T CB  
34449 C  CG1 . ILE   T  74  ? 1.7929 0.4360 1.3393 -0.0316 -0.4912 0.0571  70  ILE   T CG1 
34450 C  CG2 . ILE   T  74  ? 1.8187 0.4769 1.3286 0.0270  -0.5129 0.0225  70  ILE   T CG2 
34451 C  CD1 . ILE   T  74  ? 1.7843 0.3911 1.3407 -0.0496 -0.4819 0.0718  70  ILE   T CD1 
34452 N  N   . GLY   T  75  ? 1.8386 0.5797 1.3737 0.0548  -0.4711 0.0586  71  GLY   T N   
34453 C  CA  . GLY   T  75  ? 1.8192 0.6909 1.4007 0.1078  -0.4409 0.1061  71  GLY   T CA  
34454 C  C   . GLY   T  75  ? 1.7829 0.6524 1.3929 0.1034  -0.4349 0.1629  71  GLY   T C   
34455 O  O   . GLY   T  75  ? 1.7805 0.6072 1.3697 0.1586  -0.4487 0.2610  71  GLY   T O   
34456 N  N   . CYS   T  76  ? 1.8013 0.6702 1.4210 0.1352  -0.4259 0.1464  72  CYS   T N   
34457 C  CA  . CYS   T  76  ? 1.8274 0.6532 1.5176 0.1195  -0.4217 0.1312  72  CYS   T CA  
34458 C  C   . CYS   T  76  ? 1.8631 0.6088 1.4843 0.1228  -0.4412 0.1450  72  CYS   T C   
34459 O  O   . CYS   T  76  ? 1.8815 0.7372 1.4756 0.1022  -0.4283 0.1706  72  CYS   T O   
34460 C  CB  . CYS   T  76  ? 1.7836 0.7051 1.5385 0.1580  -0.4211 0.1027  72  CYS   T CB  
34461 S  SG  . CYS   T  76  ? 1.8232 0.7520 1.6893 0.1832  -0.3583 0.0641  72  CYS   T SG  
34462 N  N   . VAL   T  77  ? 1.8895 0.5834 1.5004 0.1326  -0.4634 0.0697  73  VAL   T N   
34463 C  CA  . VAL   T  77  ? 1.8970 0.5634 1.5435 0.1762  -0.5032 0.1122  73  VAL   T CA  
34464 C  C   . VAL   T  77  ? 1.9349 0.4570 1.5311 0.2177  -0.4684 0.1068  73  VAL   T C   
34465 O  O   . VAL   T  77  ? 1.9575 0.3128 1.5712 0.2341  -0.4446 0.2213  73  VAL   T O   
34466 C  CB  . VAL   T  77  ? 1.8456 0.5877 1.5838 0.1777  -0.5352 0.0831  73  VAL   T CB  
34467 C  CG1 . VAL   T  77  ? 1.8194 0.6252 1.5723 0.1772  -0.5384 0.0790  73  VAL   T CG1 
34468 C  CG2 . VAL   T  77  ? 1.8364 0.6570 1.6292 0.1615  -0.5101 0.0490  73  VAL   T CG2 
34469 N  N   . TYR   T  78  ? 1.9719 0.4794 1.5334 0.2079  -0.4716 0.0764  74  TYR   T N   
34470 C  CA  . TYR   T  78  ? 1.9784 0.5656 1.4850 0.1594  -0.4526 0.0651  74  TYR   T CA  
34471 C  C   . TYR   T  78  ? 1.9818 0.5920 1.5396 0.1641  -0.4316 0.0619  74  TYR   T C   
34472 O  O   . TYR   T  78  ? 1.9813 0.7207 1.5046 0.1147  -0.4746 0.0758  74  TYR   T O   
34473 C  CB  . TYR   T  78  ? 1.9090 0.4925 1.4447 0.1911  -0.4240 0.0078  74  TYR   T CB  
34474 C  CG  . TYR   T  78  ? 1.8712 0.5181 1.4142 0.1879  -0.3979 -0.0290 74  TYR   T CG  
34475 C  CD1 . TYR   T  78  ? 1.8621 0.5265 1.4633 0.1872  -0.3823 -0.0383 74  TYR   T CD1 
34476 C  CD2 . TYR   T  78  ? 1.8503 0.5288 1.3669 0.1893  -0.3841 -0.0474 74  TYR   T CD2 
34477 C  CE1 . TYR   T  78  ? 1.8178 0.5312 1.4546 0.1979  -0.3627 -0.0626 74  TYR   T CE1 
34478 C  CE2 . TYR   T  78  ? 1.8314 0.5287 1.3496 0.1954  -0.3729 -0.0614 74  TYR   T CE2 
34479 C  CZ  . TYR   T  78  ? 1.8103 0.5213 1.3775 0.1911  -0.3578 -0.0356 74  TYR   T CZ  
34480 O  OH  . TYR   T  78  ? 1.8161 0.4663 1.3369 0.2156  -0.3398 -0.0624 74  TYR   T OH  
34481 N  N   . SER   T  79  ? 2.0597 0.5660 1.5807 0.1542  -0.4225 0.0818  75  SER   T N   
34482 C  CA  . SER   T  79  ? 2.0770 0.6039 1.6404 0.1461  -0.4249 0.0149  75  SER   T CA  
34483 C  C   . SER   T  79  ? 2.0649 0.4845 1.6232 0.0811  -0.4010 0.0542  75  SER   T C   
34484 O  O   . SER   T  79  ? 2.0533 0.2972 1.6032 0.0523  -0.4070 0.0468  75  SER   T O   
34485 C  CB  . SER   T  79  ? 2.1326 0.6615 1.6851 0.1311  -0.4133 0.0512  75  SER   T CB  
34486 O  OG  . SER   T  79  ? 2.1742 0.8716 1.7060 0.1656  -0.4022 -0.0589 75  SER   T OG  
34487 N  N   . GLY   T  80  ? 2.0771 0.4998 1.6729 0.0672  -0.3485 0.0649  76  GLY   T N   
34488 C  CA  . GLY   T  80  ? 2.0537 0.5105 1.6758 0.0831  -0.3449 0.0598  76  GLY   T CA  
34489 C  C   . GLY   T  80  ? 2.0302 0.4981 1.6616 0.1101  -0.3540 0.0626  76  GLY   T C   
34490 O  O   . GLY   T  80  ? 2.0324 0.5339 1.7444 0.1004  -0.3170 0.0065  76  GLY   T O   
34491 N  N   . LEU   T  81  ? 1.9753 0.4678 1.6575 0.1141  -0.3393 0.0567  77  LEU   T N   
34492 C  CA  . LEU   T  81  ? 1.9232 0.4940 1.6252 0.1351  -0.3654 0.0660  77  LEU   T CA  
34493 C  C   . LEU   T  81  ? 1.9012 0.4775 1.5948 0.0968  -0.3433 0.1123  77  LEU   T C   
34494 O  O   . LEU   T  81  ? 1.8223 0.3809 1.5029 0.0296  -0.3889 0.1366  77  LEU   T O   
34495 C  CB  . LEU   T  81  ? 1.9109 0.5285 1.5943 0.1599  -0.3490 0.0710  77  LEU   T CB  
34496 C  CG  . LEU   T  81  ? 1.9089 0.5297 1.6096 0.1711  -0.3552 0.0695  77  LEU   T CG  
34497 C  CD1 . LEU   T  81  ? 1.9072 0.5937 1.6030 0.1835  -0.3414 0.0839  77  LEU   T CD1 
34498 C  CD2 . LEU   T  81  ? 1.9088 0.5958 1.6421 0.1966  -0.3445 0.0736  77  LEU   T CD2 
34499 N  N   . ILE   T  82  ? 1.8899 0.5053 1.6114 0.1145  -0.3357 0.1210  78  ILE   T N   
34500 C  CA  . ILE   T  82  ? 1.8740 0.5455 1.5975 0.1253  -0.3467 0.0891  78  ILE   T CA  
34501 C  C   . ILE   T  82  ? 1.9020 0.5345 1.5188 0.1163  -0.3230 0.0793  78  ILE   T C   
34502 O  O   . ILE   T  82  ? 1.9158 0.3634 1.5660 0.1220  -0.3369 0.1775  78  ILE   T O   
34503 C  CB  . ILE   T  82  ? 1.8635 0.5920 1.6254 0.1827  -0.3484 0.1016  78  ILE   T CB  
34504 C  CG1 . ILE   T  82  ? 1.8721 0.6016 1.6922 0.2103  -0.3516 0.1223  78  ILE   T CG1 
34505 C  CG2 . ILE   T  82  ? 1.8316 0.6563 1.5927 0.1395  -0.3480 0.0644  78  ILE   T CG2 
34506 C  CD1 . ILE   T  82  ? 1.8663 0.5984 1.6930 0.2364  -0.3535 0.1326  78  ILE   T CD1 
34507 N  N   . PRO   T  83  ? 1.8962 0.5613 1.5112 0.0747  -0.3455 0.0720  79  PRO   T N   
34508 C  CA  . PRO   T  83  ? 1.8785 0.5417 1.4873 0.0691  -0.3533 0.0454  79  PRO   T CA  
34509 C  C   . PRO   T  83  ? 1.8719 0.5572 1.4630 0.0639  -0.3758 0.0377  79  PRO   T C   
34510 O  O   . PRO   T  83  ? 1.8634 0.5820 1.5279 0.0747  -0.3894 -0.0489 79  PRO   T O   
34511 C  CB  . PRO   T  83  ? 1.8841 0.5735 1.4989 0.0514  -0.3254 0.0326  79  PRO   T CB  
34512 C  CG  . PRO   T  83  ? 1.8922 0.5906 1.5299 0.0612  -0.3232 0.0365  79  PRO   T CG  
34513 C  CD  . PRO   T  83  ? 1.9035 0.6038 1.5339 0.0749  -0.3319 0.0459  79  PRO   T CD  
34514 N  N   . ASP   T  84  ? 1.8926 0.5487 1.4348 0.0697  -0.4052 0.0766  80  ASP   T N   
34515 C  CA  . ASP   T  84  ? 1.8859 0.5519 1.3547 0.1093  -0.4452 0.0918  80  ASP   T CA  
34516 C  C   . ASP   T  84  ? 1.8842 0.4818 1.3447 0.0994  -0.4722 0.1061  80  ASP   T C   
34517 O  O   . ASP   T  84  ? 1.8803 0.4376 1.2115 0.1030  -0.5230 0.1925  80  ASP   T O   
34518 C  CB  . ASP   T  84  ? 1.8933 0.5747 1.3610 0.0922  -0.4769 0.1195  80  ASP   T CB  
34519 C  CG  . ASP   T  84  ? 1.8892 0.6235 1.3409 0.1045  -0.4994 0.1518  80  ASP   T CG  
34520 O  OD1 . ASP   T  84  ? 1.9074 0.7603 1.2973 0.0836  -0.5152 0.1441  80  ASP   T OD1 
34521 O  OD2 . ASP   T  84  ? 1.9027 0.5361 1.3505 0.1268  -0.5595 0.1487  80  ASP   T OD2 
34522 N  N   . GLY   T  85  ? 1.8711 0.4879 1.3758 0.0995  -0.4955 0.0412  81  GLY   T N   
34523 C  CA  . GLY   T  85  ? 1.8921 0.4929 1.3935 0.0914  -0.4857 0.0274  81  GLY   T CA  
34524 C  C   . GLY   T  85  ? 1.8818 0.4793 1.3752 0.1121  -0.4579 -0.0026 81  GLY   T C   
34525 O  O   . GLY   T  85  ? 1.9408 0.3385 1.3453 0.0852  -0.5075 -0.0267 81  GLY   T O   
34526 N  N   . ARG   T  86  ? 1.8924 0.4387 1.4165 0.0808  -0.4625 0.0225  82  ARG   T N   
34527 C  CA  . ARG   T  86  ? 1.8886 0.4006 1.4571 0.1042  -0.4670 -0.0306 82  ARG   T CA  
34528 C  C   . ARG   T  86  ? 1.8539 0.4451 1.4846 0.0757  -0.4691 0.0038  82  ARG   T C   
34529 O  O   . ARG   T  86  ? 1.8386 0.4615 1.4666 0.1716  -0.4518 0.0557  82  ARG   T O   
34530 C  CB  . ARG   T  86  ? 1.9094 0.3255 1.4865 0.0679  -0.4455 -0.0465 82  ARG   T CB  
34531 C  CG  . ARG   T  86  ? 1.9221 0.3815 1.5141 0.0621  -0.4550 -0.0334 82  ARG   T CG  
34532 C  CD  . ARG   T  86  ? 1.9731 0.4475 1.5390 0.0256  -0.4158 -0.0603 82  ARG   T CD  
34533 N  NE  . ARG   T  86  ? 1.9851 0.4719 1.5345 -0.0086 -0.4024 -0.0310 82  ARG   T NE  
34534 C  CZ  . ARG   T  86  ? 1.9937 0.5021 1.5402 -0.0673 -0.4021 -0.0406 82  ARG   T CZ  
34535 N  NH1 . ARG   T  86  ? 2.0252 0.6257 1.5302 -0.0946 -0.3876 -0.0927 82  ARG   T NH1 
34536 N  NH2 . ARG   T  86  ? 1.9439 0.4468 1.5569 -0.0423 -0.4047 -0.0826 82  ARG   T NH2 
34537 N  N   . HIS   T  87  ? 1.8168 0.4281 1.5114 0.1097  -0.4600 -0.0288 83  HIS   T N   
34538 C  CA  . HIS   T  87  ? 1.8163 0.4536 1.4723 0.1066  -0.4381 0.0109  83  HIS   T CA  
34539 C  C   . HIS   T  87  ? 1.8128 0.4828 1.4753 0.1072  -0.4407 0.0004  83  HIS   T C   
34540 O  O   . HIS   T  87  ? 1.8288 0.4292 1.5166 0.0611  -0.4451 0.0517  83  HIS   T O   
34541 C  CB  . HIS   T  87  ? 1.8047 0.4627 1.4197 0.1231  -0.4368 0.0274  83  HIS   T CB  
34542 C  CG  . HIS   T  87  ? 1.8239 0.4583 1.3494 0.1090  -0.4297 0.0856  83  HIS   T CG  
34543 N  ND1 . HIS   T  87  ? 1.8327 0.4699 1.3579 0.1029  -0.4090 0.0995  83  HIS   T ND1 
34544 C  CD2 . HIS   T  87  ? 1.8257 0.4778 1.3370 0.1078  -0.4336 0.1198  83  HIS   T CD2 
34545 C  CE1 . HIS   T  87  ? 1.8220 0.5299 1.3532 0.0880  -0.3977 0.1163  83  HIS   T CE1 
34546 N  NE2 . HIS   T  87  ? 1.8412 0.4992 1.3244 0.0989  -0.4201 0.1469  83  HIS   T NE2 
34547 N  N   . LEU   T  88  ? 1.8037 0.5692 1.4075 0.0927  -0.4427 -0.0022 84  LEU   T N   
34548 C  CA  . LEU   T  88  ? 1.7832 0.6087 1.3744 0.0730  -0.4613 0.0377  84  LEU   T CA  
34549 C  C   . LEU   T  88  ? 1.7424 0.6678 1.3722 0.0840  -0.4752 0.0059  84  LEU   T C   
34550 O  O   . LEU   T  88  ? 1.7711 0.6294 1.3327 0.0749  -0.4846 -0.0245 84  LEU   T O   
34551 C  CB  . LEU   T  88  ? 1.7928 0.6351 1.3904 0.0621  -0.4692 0.0726  84  LEU   T CB  
34552 C  CG  . LEU   T  88  ? 1.8200 0.7142 1.3855 0.0511  -0.4633 0.1341  84  LEU   T CG  
34553 C  CD1 . LEU   T  88  ? 1.8355 0.6915 1.3530 0.0342  -0.4700 0.1825  84  LEU   T CD1 
34554 C  CD2 . LEU   T  88  ? 1.9020 0.7380 1.4377 0.0658  -0.4196 0.1520  84  LEU   T CD2 
34555 N  N   . VAL   T  89  ? 1.7438 0.6174 1.3693 0.0711  -0.4775 -0.0233 85  VAL   T N   
34556 C  CA  . VAL   T  89  ? 1.7602 0.6043 1.3846 0.0897  -0.4379 -0.0626 85  VAL   T CA  
34557 C  C   . VAL   T  89  ? 1.7647 0.6211 1.3475 0.0747  -0.4252 -0.0613 85  VAL   T C   
34558 O  O   . VAL   T  89  ? 1.7568 0.7387 1.3828 0.0737  -0.3792 -0.1344 85  VAL   T O   
34559 C  CB  . VAL   T  89  ? 1.7624 0.5933 1.4074 0.0796  -0.4470 -0.1024 85  VAL   T CB  
34560 C  CG1 . VAL   T  89  ? 1.7612 0.5943 1.4103 0.0629  -0.4433 -0.0876 85  VAL   T CG1 
34561 C  CG2 . VAL   T  89  ? 1.7865 0.5970 1.4206 0.0718  -0.4595 -0.0987 85  VAL   T CG2 
34562 N  N   . ASN   T  90  ? 1.7534 0.5224 1.3551 0.0687  -0.4012 -0.0694 86  ASN   T N   
34563 C  CA  . ASN   T  90  ? 1.7101 0.4543 1.3803 0.0225  -0.3752 -0.0831 86  ASN   T CA  
34564 C  C   . ASN   T  90  ? 1.7293 0.4784 1.3594 0.0480  -0.3521 -0.0277 86  ASN   T C   
34565 O  O   . ASN   T  90  ? 1.7641 0.4991 1.3892 0.0815  -0.2868 -0.0447 86  ASN   T O   
34566 C  CB  . ASN   T  90  ? 1.6390 0.3563 1.3770 0.0041  -0.3831 -0.0706 86  ASN   T CB  
34567 C  CG  . ASN   T  90  ? 1.6267 0.3268 1.4194 -0.0223 -0.3947 -0.0932 86  ASN   T CG  
34568 O  OD1 . ASN   T  90  ? 1.6438 0.2732 1.4515 -0.0375 -0.3836 -0.0873 86  ASN   T OD1 
34569 N  ND2 . ASN   T  90  ? 1.5568 0.4286 1.4486 -0.0295 -0.4224 -0.1018 86  ASN   T ND2 
34570 N  N   . ARG   T  91  ? 1.7098 0.4827 1.3520 0.0610  -0.3567 -0.0453 87  ARG   T N   
34571 C  CA  . ARG   T  91  ? 1.7250 0.4561 1.3372 0.0926  -0.3549 -0.0094 87  ARG   T CA  
34572 C  C   . ARG   T  91  ? 1.6924 0.3778 1.3269 0.0724  -0.3846 -0.0064 87  ARG   T C   
34573 O  O   . ARG   T  91  ? 1.6957 0.2584 1.2725 0.0068  -0.4073 0.0602  87  ARG   T O   
34574 C  CB  . ARG   T  91  ? 1.7438 0.4436 1.3674 0.0971  -0.3534 -0.0008 87  ARG   T CB  
34575 C  CG  . ARG   T  91  ? 1.7571 0.4386 1.3611 0.1611  -0.3742 0.0527  87  ARG   T CG  
34576 C  CD  . ARG   T  91  ? 1.7701 0.4397 1.3858 0.1826  -0.3699 0.0642  87  ARG   T CD  
34577 N  NE  . ARG   T  91  ? 1.7816 0.4555 1.4023 0.1933  -0.3475 0.0938  87  ARG   T NE  
34578 C  CZ  . ARG   T  91  ? 1.8289 0.4513 1.3661 0.1779  -0.3347 0.1361  87  ARG   T CZ  
34579 N  NH1 . ARG   T  91  ? 1.8317 0.4304 1.3470 0.1869  -0.3401 0.1169  87  ARG   T NH1 
34580 N  NH2 . ARG   T  91  ? 1.8314 0.4820 1.3977 0.1604  -0.3171 0.1777  87  ARG   T NH2 
34581 N  N   . GLY   T  92  ? 1.7097 0.5055 1.2741 0.0569  -0.4157 -0.0098 88  GLY   T N   
34582 C  CA  . GLY   T  92  ? 1.7432 0.4760 1.2999 0.0429  -0.3841 -0.0461 88  GLY   T CA  
34583 C  C   . GLY   T  92  ? 1.7573 0.4582 1.2694 0.0627  -0.3692 -0.0501 88  GLY   T C   
34584 O  O   . GLY   T  92  ? 1.8170 0.4207 1.1961 0.0304  -0.3898 -0.0653 88  GLY   T O   
34585 N  N   . ARG   T  93  ? 1.7333 0.4037 1.3104 0.0411  -0.3926 -0.0597 89  ARG   T N   
34586 C  CA  . ARG   T  93  ? 1.6973 0.4383 1.3229 0.0178  -0.4159 -0.0938 89  ARG   T CA  
34587 C  C   . ARG   T  93  ? 1.6468 0.4239 1.2866 -0.0131 -0.4210 -0.1030 89  ARG   T C   
34588 O  O   . ARG   T  93  ? 1.5753 0.4245 1.2367 0.0703  -0.4402 -0.0651 89  ARG   T O   
34589 C  CB  . ARG   T  93  ? 1.6967 0.4488 1.3762 0.0496  -0.4059 -0.1085 89  ARG   T CB  
34590 C  CG  . ARG   T  93  ? 1.7314 0.4868 1.4155 0.0873  -0.4196 -0.1077 89  ARG   T CG  
34591 C  CD  . ARG   T  93  ? 1.7427 0.5200 1.4703 0.0882  -0.4052 -0.1394 89  ARG   T CD  
34592 N  NE  . ARG   T  93  ? 1.7380 0.5415 1.5004 0.0967  -0.4310 -0.1441 89  ARG   T NE  
34593 C  CZ  . ARG   T  93  ? 1.7199 0.5654 1.5224 0.0841  -0.4558 -0.1727 89  ARG   T CZ  
34594 N  NH1 . ARG   T  93  ? 1.7272 0.5895 1.5256 0.0619  -0.4428 -0.2267 89  ARG   T NH1 
34595 N  NH2 . ARG   T  93  ? 1.7077 0.5691 1.5586 0.0925  -0.4647 -0.1759 89  ARG   T NH2 
34596 N  N   . GLU   T  94  ? 1.6444 0.4387 1.2782 -0.0370 -0.4163 -0.0818 90  GLU   T N   
34597 C  CA  . GLU   T  94  ? 1.6616 0.4187 1.2730 -0.0394 -0.3812 -0.0551 90  GLU   T CA  
34598 C  C   . GLU   T  94  ? 1.6913 0.4417 1.2331 -0.0559 -0.3827 -0.1127 90  GLU   T C   
34599 O  O   . GLU   T  94  ? 1.6534 0.4352 1.1740 -0.0978 -0.3723 -0.2285 90  GLU   T O   
34600 C  CB  . GLU   T  94  ? 1.6522 0.4683 1.2357 -0.0506 -0.3297 -0.0461 90  GLU   T CB  
34601 C  CG  . GLU   T  94  ? 1.6714 0.5549 1.2536 -0.0367 -0.3026 -0.0471 90  GLU   T CG  
34602 C  CD  . GLU   T  94  ? 1.6722 0.7241 1.1969 -0.0301 -0.2902 -0.0467 90  GLU   T CD  
34603 O  OE1 . GLU   T  94  ? 1.6243 0.8789 1.2040 -0.0386 -0.2251 0.0086  90  GLU   T OE1 
34604 O  OE2 . GLU   T  94  ? 1.7103 0.9476 1.2849 0.0484  -0.2313 0.0269  90  GLU   T OE2 
34605 N  N   . GLU   T  95  ? 1.7420 0.4652 1.2185 -0.0214 -0.3999 -0.0618 91  GLU   T N   
34606 C  CA  . GLU   T  95  ? 1.7445 0.4773 1.2252 0.0137  -0.4010 -0.0328 91  GLU   T CA  
34607 C  C   . GLU   T  95  ? 1.7501 0.3679 1.2181 0.0615  -0.4192 0.0102  91  GLU   T C   
34608 O  O   . GLU   T  95  ? 1.7449 0.3255 1.2440 0.0922  -0.4518 0.0888  91  GLU   T O   
34609 C  CB  . GLU   T  95  ? 1.7825 0.4800 1.2551 -0.0161 -0.4093 -0.0457 91  GLU   T CB  
34610 C  CG  . GLU   T  95  ? 1.8362 0.5149 1.3059 -0.0400 -0.4123 -0.0820 91  GLU   T CG  
34611 C  CD  . GLU   T  95  ? 1.8359 0.5683 1.3459 -0.0223 -0.4090 -0.1270 91  GLU   T CD  
34612 O  OE1 . GLU   T  95  ? 1.9681 0.4547 1.3982 -0.1221 -0.3505 -0.1947 91  GLU   T OE1 
34613 O  OE2 . GLU   T  95  ? 1.8575 0.8987 1.2023 -0.0468 -0.5367 -0.1769 91  GLU   T OE2 
34614 N  N   . ALA   T  96  ? 1.7567 0.3876 1.2674 0.0850  -0.4203 0.0656  92  ALA   T N   
34615 C  CA  . ALA   T  96  ? 1.7753 0.3445 1.2504 0.0910  -0.3930 0.0816  92  ALA   T CA  
34616 C  C   . ALA   T  96  ? 1.7761 0.3286 1.2186 0.1593  -0.3705 0.0848  92  ALA   T C   
34617 O  O   . ALA   T  96  ? 1.8045 0.1685 1.2662 0.1091  -0.3642 0.1484  92  ALA   T O   
34618 C  CB  . ALA   T  96  ? 1.7664 0.4093 1.2851 0.1016  -0.3931 0.0790  92  ALA   T CB  
34619 N  N   . ALA   T  97  ? 1.7650 0.3655 1.2227 0.1410  -0.3796 0.0914  93  ALA   T N   
34620 C  CA  . ALA   T  97  ? 1.7604 0.3688 1.2311 0.0926  -0.3757 0.0626  93  ALA   T CA  
34621 C  C   . ALA   T  97  ? 1.7610 0.3845 1.2372 0.0929  -0.4010 0.0526  93  ALA   T C   
34622 O  O   . ALA   T  97  ? 1.8295 0.3261 1.2905 0.1728  -0.3875 0.1205  93  ALA   T O   
34623 C  CB  . ALA   T  97  ? 1.7471 0.4493 1.2516 0.0822  -0.3648 0.0481  93  ALA   T CB  
34624 N  N   . SER   T  98  ? 1.7332 0.4129 1.2685 0.0956  -0.4129 0.0553  94  SER   T N   
34625 C  CA  . SER   T  98  ? 1.7250 0.3972 1.2559 0.0842  -0.4425 0.0309  94  SER   T CA  
34626 C  C   . SER   T  98  ? 1.6955 0.3872 1.2720 0.0771  -0.4351 0.0338  94  SER   T C   
34627 O  O   . SER   T  98  ? 1.6277 0.3864 1.3133 0.0514  -0.4333 0.0610  94  SER   T O   
34628 C  CB  . SER   T  98  ? 1.7142 0.4265 1.2563 0.1133  -0.4898 0.0478  94  SER   T CB  
34629 O  OG  . SER   T  98  ? 1.7205 0.3899 1.1917 0.1327  -0.5534 0.0853  94  SER   T OG  
34630 N  N   . PHE   T  99  ? 1.7454 0.4533 1.2259 0.0309  -0.4160 0.0511  95  PHE   T N   
34631 C  CA  . PHE   T  99  ? 1.7544 0.5254 1.2298 0.0270  -0.4137 0.0463  95  PHE   T CA  
34632 C  C   . PHE   T  99  ? 1.7347 0.5365 1.2485 0.0383  -0.4006 0.0253  95  PHE   T C   
34633 O  O   . PHE   T  99  ? 1.7422 0.5322 1.3067 0.0460  -0.3730 0.0441  95  PHE   T O   
34634 C  CB  . PHE   T  99  ? 1.7652 0.5652 1.1949 0.0043  -0.4486 0.0743  95  PHE   T CB  
34635 C  CG  . PHE   T  99  ? 1.7857 0.5599 1.1949 -0.0080 -0.4454 0.1165  95  PHE   T CG  
34636 C  CD1 . PHE   T  99  ? 1.7991 0.5939 1.1905 -0.0216 -0.4318 0.1183  95  PHE   T CD1 
34637 C  CD2 . PHE   T  99  ? 1.7882 0.5855 1.1510 -0.0147 -0.4466 0.1622  95  PHE   T CD2 
34638 C  CE1 . PHE   T  99  ? 1.8152 0.6010 1.2328 -0.0504 -0.4061 0.1676  95  PHE   T CE1 
34639 C  CE2 . PHE   T  99  ? 1.8199 0.6067 1.1615 -0.0217 -0.4323 0.1730  95  PHE   T CE2 
34640 C  CZ  . PHE   T  99  ? 1.8326 0.5957 1.1890 -0.0625 -0.4273 0.1673  95  PHE   T CZ  
34641 N  N   . LYS   T  100 ? 1.7260 0.5833 1.2231 0.0652  -0.4083 -0.0031 96  LYS   T N   
34642 C  CA  . LYS   T  100 ? 1.7277 0.6426 1.2002 0.0869  -0.4231 -0.0550 96  LYS   T CA  
34643 C  C   . LYS   T  100 ? 1.7655 0.6712 1.1304 0.0896  -0.4517 -0.0591 96  LYS   T C   
34644 O  O   . LYS   T  100 ? 1.7886 0.6110 1.2018 0.1735  -0.4347 -0.0255 96  LYS   T O   
34645 C  CB  . LYS   T  100 ? 1.7327 0.6737 1.2177 0.1161  -0.4048 -0.0408 96  LYS   T CB  
34646 C  CG  . LYS   T  100 ? 1.7060 0.7314 1.2307 0.0938  -0.3959 -0.0500 96  LYS   T CG  
34647 C  CD  . LYS   T  100 ? 1.7475 0.7784 1.2143 0.0730  -0.3965 -0.0205 96  LYS   T CD  
34648 C  CE  . LYS   T  100 ? 1.7276 0.8091 1.1914 0.0813  -0.4401 0.0005  96  LYS   T CE  
34649 N  NZ  . LYS   T  100 ? 1.7195 0.8399 1.1973 0.0543  -0.4733 0.0146  96  LYS   T NZ  
34650 N  N   . LYS   T  101 ? 1.7608 0.6717 1.1248 0.0856  -0.4601 -0.1122 97  LYS   T N   
34651 C  CA  . LYS   T  101 ? 1.7610 0.6121 1.1665 0.0854  -0.4571 -0.1424 97  LYS   T CA  
34652 C  C   . LYS   T  101 ? 1.7268 0.6706 1.1115 0.0411  -0.4556 -0.1374 97  LYS   T C   
34653 O  O   . LYS   T  101 ? 1.7607 0.7456 1.0695 0.0913  -0.4423 -0.2350 97  LYS   T O   
34654 C  CB  . LYS   T  101 ? 1.7693 0.7016 1.1688 0.1081  -0.4154 -0.1373 97  LYS   T CB  
34655 C  CG  . LYS   T  101 ? 1.7836 0.7297 1.2251 0.1242  -0.3898 -0.0997 97  LYS   T CG  
34656 C  CD  . LYS   T  101 ? 1.7876 0.9017 1.2056 0.1593  -0.3937 -0.0650 97  LYS   T CD  
34657 C  CE  . LYS   T  101 ? 1.8164 0.9422 1.2554 0.1539  -0.3999 -0.0382 97  LYS   T CE  
34658 N  NZ  . LYS   T  101 ? 1.7932 1.0356 1.3181 0.1453  -0.3726 -0.1371 97  LYS   T NZ  
34659 N  N   . LEU   T  102 ? 1.7679 0.5199 1.1017 0.0741  -0.4465 -0.1059 98  LEU   T N   
34660 C  CA  . LEU   T  102 ? 1.7599 0.4706 1.1528 0.0597  -0.4409 -0.0617 98  LEU   T CA  
34661 C  C   . LEU   T  102 ? 1.7334 0.4285 1.1379 0.0166  -0.4791 -0.0552 98  LEU   T C   
34662 O  O   . LEU   T  102 ? 1.6669 0.4342 1.1049 0.0057  -0.5133 -0.0548 98  LEU   T O   
34663 C  CB  . LEU   T  102 ? 1.7798 0.4101 1.1787 0.0629  -0.4300 -0.0360 98  LEU   T CB  
34664 C  CG  . LEU   T  102 ? 1.7962 0.4199 1.1870 0.0856  -0.4243 -0.0242 98  LEU   T CG  
34665 C  CD1 . LEU   T  102 ? 1.7948 0.4703 1.1904 0.1242  -0.4335 0.0041  98  LEU   T CD1 
34666 C  CD2 . LEU   T  102 ? 1.8352 0.4272 1.1586 0.0854  -0.4548 -0.0236 98  LEU   T CD2 
34667 N  N   . TYR   T  103 ? 1.7397 0.4002 1.1984 0.0179  -0.4759 -0.0420 99  TYR   T N   
34668 C  CA  . TYR   T  103 ? 1.7460 0.4443 1.2242 0.0071  -0.4434 -0.0241 99  TYR   T CA  
34669 C  C   . TYR   T  103 ? 1.7296 0.4315 1.2567 0.0204  -0.4572 -0.0056 99  TYR   T C   
34670 O  O   . TYR   T  103 ? 1.7142 0.3564 1.2500 0.0435  -0.4560 0.0103  99  TYR   T O   
34671 C  CB  . TYR   T  103 ? 1.7464 0.4571 1.2280 -0.0224 -0.4619 -0.0251 99  TYR   T CB  
34672 C  CG  . TYR   T  103 ? 1.7416 0.4835 1.2327 -0.0320 -0.4654 -0.0165 99  TYR   T CG  
34673 C  CD1 . TYR   T  103 ? 1.7391 0.4652 1.2397 -0.0338 -0.4589 -0.0310 99  TYR   T CD1 
34674 C  CD2 . TYR   T  103 ? 1.7338 0.4672 1.2304 -0.0622 -0.4812 -0.0102 99  TYR   T CD2 
34675 C  CE1 . TYR   T  103 ? 1.7341 0.4302 1.2879 -0.0768 -0.4342 -0.0330 99  TYR   T CE1 
34676 C  CE2 . TYR   T  103 ? 1.7436 0.3795 1.2785 -0.0999 -0.4590 -0.0188 99  TYR   T CE2 
34677 C  CZ  . TYR   T  103 ? 1.6934 0.3941 1.2993 -0.1439 -0.4591 -0.0265 99  TYR   T CZ  
34678 O  OH  . TYR   T  103 ? 1.7052 0.2900 1.3912 -0.2520 -0.4146 -0.0212 99  TYR   T OH  
34679 N  N   . LYS   T  104 ? 1.7364 0.4886 1.3306 0.0476  -0.4218 0.0173  100 LYS   T N   
34680 C  CA  . LYS   T  104 ? 1.7446 0.6384 1.3650 0.0139  -0.4361 0.0129  100 LYS   T CA  
34681 C  C   . LYS   T  104 ? 1.7626 0.6080 1.3479 0.0110  -0.4180 0.0069  100 LYS   T C   
34682 O  O   . LYS   T  104 ? 1.7605 0.5629 1.4080 -0.0550 -0.4010 -0.0399 100 LYS   T O   
34683 C  CB  . LYS   T  104 ? 1.7693 0.7167 1.3462 0.0392  -0.4056 0.0041  100 LYS   T CB  
34684 C  CG  . LYS   T  104 ? 1.7403 0.8189 1.3594 0.0198  -0.4279 0.0465  100 LYS   T CG  
34685 C  CD  . LYS   T  104 ? 1.7341 0.9333 1.4105 0.0206  -0.3989 0.0932  100 LYS   T CD  
34686 C  CE  . LYS   T  104 ? 1.7060 1.0752 1.3569 0.0201  -0.4618 0.0655  100 LYS   T CE  
34687 N  NZ  . LYS   T  104 ? 1.7607 1.1094 1.3371 0.0524  -0.4757 0.0958  100 LYS   T NZ  
34688 N  N   . THR   T  105 ? 1.7851 0.7326 1.2877 0.0218  -0.4105 0.0291  101 THR   T N   
34689 C  CA  . THR   T  105 ? 1.7839 0.8690 1.2364 0.0432  -0.4505 0.0500  101 THR   T CA  
34690 C  C   . THR   T  105 ? 1.7789 0.8263 1.3512 0.0383  -0.4752 0.0169  101 THR   T C   
34691 O  O   . THR   T  105 ? 1.7553 0.6721 1.4346 0.0836  -0.4795 -0.0693 101 THR   T O   
34692 C  CB  . THR   T  105 ? 1.8297 0.9449 1.1550 0.0490  -0.4777 0.1051  101 THR   T CB  
34693 O  OG1 . THR   T  105 ? 1.9457 0.9829 1.0932 0.0320  -0.3954 0.2039  101 THR   T OG1 
34694 C  CG2 . THR   T  105 ? 1.8296 0.9274 1.1364 0.0290  -0.4588 0.1059  101 THR   T CG2 
34695 N  N   . PRO   T  106 ? 1.7341 0.7831 1.4162 -0.0134 -0.4849 -0.0083 102 PRO   T N   
34696 C  CA  . PRO   T  106 ? 1.7213 0.7392 1.4098 -0.0159 -0.5062 0.0258  102 PRO   T CA  
34697 C  C   . PRO   T  106 ? 1.7565 0.7099 1.3377 -0.0168 -0.5156 -0.0166 102 PRO   T C   
34698 O  O   . PRO   T  106 ? 1.8053 0.8286 1.3907 -0.1255 -0.4856 0.0548  102 PRO   T O   
34699 C  CB  . PRO   T  106 ? 1.6886 0.7365 1.4654 -0.0143 -0.4953 0.0407  102 PRO   T CB  
34700 C  CG  . PRO   T  106 ? 1.6917 0.7902 1.4549 -0.0204 -0.4985 0.0001  102 PRO   T CG  
34701 C  CD  . PRO   T  106 ? 1.6964 0.8543 1.4322 -0.0192 -0.4766 -0.0148 102 PRO   T CD  
34702 N  N   . ILE   T  107 ? 1.7155 0.6565 1.3244 0.0490  -0.5053 -0.0040 103 ILE   T N   
34703 C  CA  . ILE   T  107 ? 1.7309 0.5803 1.2516 0.0840  -0.4834 -0.0135 103 ILE   T CA  
34704 C  C   . ILE   T  107 ? 1.7109 0.5703 1.2138 0.1394  -0.4974 -0.0439 103 ILE   T C   
34705 O  O   . ILE   T  107 ? 1.7048 0.6227 1.1693 0.1358  -0.5244 -0.0474 103 ILE   T O   
34706 C  CB  . ILE   T  107 ? 1.7144 0.5435 1.2704 0.0672  -0.4797 -0.0181 103 ILE   T CB  
34707 C  CG1 . ILE   T  107 ? 1.7432 0.5048 1.2948 0.0599  -0.4859 -0.0356 103 ILE   T CG1 
34708 C  CG2 . ILE   T  107 ? 1.7228 0.5748 1.2915 0.0918  -0.4892 0.0007  103 ILE   T CG2 
34709 C  CD1 . ILE   T  107 ? 1.7119 0.4765 1.3088 0.0266  -0.4879 -0.0402 103 ILE   T CD1 
34710 N  N   . PRO   T  108 ? 1.7554 0.5187 1.1645 0.1373  -0.4836 -0.0540 104 PRO   T N   
34711 C  CA  . PRO   T  108 ? 1.7472 0.5307 1.1850 0.1249  -0.4768 -0.0313 104 PRO   T CA  
34712 C  C   . PRO   T  108 ? 1.8055 0.4830 1.2297 0.1176  -0.4679 0.0101  104 PRO   T C   
34713 O  O   . PRO   T  108 ? 1.7872 0.4516 1.2406 0.1524  -0.5141 0.0586  104 PRO   T O   
34714 C  CB  . PRO   T  108 ? 1.7563 0.5294 1.1124 0.1110  -0.4705 -0.0556 104 PRO   T CB  
34715 C  CG  . PRO   T  108 ? 1.7370 0.5314 1.1191 0.1129  -0.4706 -0.0731 104 PRO   T CG  
34716 C  CD  . PRO   T  108 ? 1.7249 0.5612 1.1244 0.1242  -0.4691 -0.0768 104 PRO   T CD  
34717 N  N   . ILE   T  109 ? 1.8211 0.4803 1.2806 0.1107  -0.4478 0.0460  105 ILE   T N   
34718 C  CA  . ILE   T  109 ? 1.8123 0.4443 1.3084 0.0942  -0.4506 0.0668  105 ILE   T CA  
34719 C  C   . ILE   T  109 ? 1.8149 0.3228 1.2742 0.1245  -0.4195 0.0490  105 ILE   T C   
34720 O  O   . ILE   T  109 ? 1.8829 0.1854 1.3427 0.1357  -0.4000 0.0599  105 ILE   T O   
34721 C  CB  . ILE   T  109 ? 1.8316 0.3924 1.3801 0.1087  -0.4528 0.0865  105 ILE   T CB  
34722 C  CG1 . ILE   T  109 ? 1.8383 0.4818 1.3961 0.0917  -0.4567 0.0530  105 ILE   T CG1 
34723 C  CG2 . ILE   T  109 ? 1.8588 0.3904 1.4085 0.0956  -0.4504 0.0598  105 ILE   T CG2 
34724 C  CD1 . ILE   T  109 ? 1.8225 0.5210 1.3968 0.1031  -0.4463 0.0548  105 ILE   T CD1 
34725 N  N   . PRO   T  110 ? 1.7805 0.3822 1.2588 0.1052  -0.4451 0.0381  106 PRO   T N   
34726 C  CA  . PRO   T  110 ? 1.7500 0.3803 1.2343 0.1133  -0.4280 0.0471  106 PRO   T CA  
34727 C  C   . PRO   T  110 ? 1.6923 0.4134 1.2059 0.1071  -0.4259 0.0230  106 PRO   T C   
34728 O  O   . PRO   T  110 ? 1.6272 0.3805 1.1849 0.1376  -0.4325 0.0436  106 PRO   T O   
34729 C  CB  . PRO   T  110 ? 1.7516 0.3718 1.2294 0.0911  -0.4283 0.0465  106 PRO   T CB  
34730 C  CG  . PRO   T  110 ? 1.7720 0.4153 1.2253 0.0960  -0.4416 0.0602  106 PRO   T CG  
34731 C  CD  . PRO   T  110 ? 1.7727 0.4619 1.2377 0.0928  -0.4276 0.0571  106 PRO   T CD  
34732 N  N   . ALA   T  111 ? 1.6826 0.4240 1.1856 0.1169  -0.4331 0.0736  107 ALA   T N   
34733 C  CA  . ALA   T  111 ? 1.6958 0.4398 1.1782 0.1144  -0.4457 0.0640  107 ALA   T CA  
34734 C  C   . ALA   T  111 ? 1.6908 0.3297 1.1703 0.1023  -0.4731 0.0375  107 ALA   T C   
34735 O  O   . ALA   T  111 ? 1.7085 0.2184 1.2228 0.0429  -0.4854 0.0020  107 ALA   T O   
34736 C  CB  . ALA   T  111 ? 1.6954 0.4520 1.1760 0.1225  -0.4149 0.0376  107 ALA   T CB  
34737 N  N   . PHE   T  112 ? 1.7001 0.3768 1.1548 0.1296  -0.5042 0.0560  108 PHE   T N   
34738 C  CA  . PHE   T  112 ? 1.7060 0.4685 1.1286 0.1375  -0.5154 0.0372  108 PHE   T CA  
34739 C  C   . PHE   T  112 ? 1.7590 0.4862 1.1495 0.1094  -0.4969 0.0152  108 PHE   T C   
34740 O  O   . PHE   T  112 ? 1.7860 0.5224 1.1183 0.1440  -0.4679 0.0911  108 PHE   T O   
34741 C  CB  . PHE   T  112 ? 1.7059 0.5238 1.1040 0.1675  -0.5291 0.0189  108 PHE   T CB  
34742 C  CG  . PHE   T  112 ? 1.7093 0.5519 1.0695 0.1636  -0.5442 -0.0100 108 PHE   T CG  
34743 C  CD1 . PHE   T  112 ? 1.6946 0.5110 1.0744 0.1752  -0.5453 -0.0086 108 PHE   T CD1 
34744 C  CD2 . PHE   T  112 ? 1.7037 0.5344 1.1031 0.1701  -0.5469 -0.0605 108 PHE   T CD2 
34745 C  CE1 . PHE   T  112 ? 1.6849 0.5308 1.0887 0.1779  -0.5450 -0.0072 108 PHE   T CE1 
34746 C  CE2 . PHE   T  112 ? 1.7040 0.5313 1.1208 0.1673  -0.5399 -0.0572 108 PHE   T CE2 
34747 C  CZ  . PHE   T  112 ? 1.6937 0.5357 1.1370 0.1939  -0.5482 -0.0279 108 PHE   T CZ  
34748 N  N   . ALA   T  113 ? 1.7989 0.5633 1.1426 0.0584  -0.4949 0.0269  109 ALA   T N   
34749 C  CA  . ALA   T  113 ? 1.7912 0.5834 1.1661 0.0094  -0.5077 -0.0024 109 ALA   T CA  
34750 C  C   . ALA   T  113 ? 1.7972 0.5654 1.1978 0.0010  -0.5239 -0.0135 109 ALA   T C   
34751 O  O   . ALA   T  113 ? 1.7926 0.5904 1.2099 -0.0250 -0.5405 -0.0422 109 ALA   T O   
34752 C  CB  . ALA   T  113 ? 1.8149 0.6126 1.1560 -0.0119 -0.5114 -0.0032 109 ALA   T CB  
34753 N  N   . ASP   T  114 ? 1.8097 0.5221 1.1682 0.0133  -0.5694 0.0040  110 ASP   T N   
34754 C  CA  . ASP   T  114 ? 1.8109 0.5439 1.1461 0.0454  -0.5742 0.0410  110 ASP   T CA  
34755 C  C   . ASP   T  114 ? 1.8060 0.5075 1.1139 0.0160  -0.5457 -0.0167 110 ASP   T C   
34756 O  O   . ASP   T  114 ? 1.7799 0.5881 0.9813 0.0339  -0.5427 0.0642  110 ASP   T O   
34757 C  CB  . ASP   T  114 ? 1.8316 0.5510 1.1902 0.1003  -0.5941 0.0632  110 ASP   T CB  
34758 C  CG  . ASP   T  114 ? 1.8359 0.6196 1.2196 0.1220  -0.6440 0.0961  110 ASP   T CG  
34759 O  OD1 . ASP   T  114 ? 1.8710 0.6034 1.1324 0.0879  -0.6568 0.2404  110 ASP   T OD1 
34760 O  OD2 . ASP   T  114 ? 1.8510 0.7586 1.2819 0.1780  -0.7263 0.0550  110 ASP   T OD2 
34761 N  N   . ARG   T  115 ? 1.8420 0.5297 1.1555 -0.0105 -0.5037 -0.0342 111 ARG   T N   
34762 C  CA  . ARG   T  115 ? 1.8798 0.5986 1.1502 -0.0282 -0.4963 -0.0391 111 ARG   T CA  
34763 C  C   . ARG   T  115 ? 1.8670 0.5407 1.1201 -0.0568 -0.5428 -0.0454 111 ARG   T C   
34764 O  O   . ARG   T  115 ? 1.8956 0.7616 1.1230 -0.1852 -0.5162 -0.1063 111 ARG   T O   
34765 C  CB  . ARG   T  115 ? 1.8663 0.6064 1.2270 -0.0289 -0.4717 -0.0258 111 ARG   T CB  
34766 C  CG  . ARG   T  115 ? 1.8852 0.6146 1.2418 0.0060  -0.4780 -0.0123 111 ARG   T CG  
34767 C  CD  . ARG   T  115 ? 1.8868 0.6915 1.2550 0.0068  -0.4772 0.0363  111 ARG   T CD  
34768 N  NE  . ARG   T  115 ? 1.8749 0.7772 1.3042 0.0620  -0.4326 0.0574  111 ARG   T NE  
34769 C  CZ  . ARG   T  115 ? 1.9142 0.8126 1.3509 0.0138  -0.3992 0.1018  111 ARG   T CZ  
34770 N  NH1 . ARG   T  115 ? 1.9511 0.8812 1.3990 -0.0045 -0.3743 0.1417  111 ARG   T NH1 
34771 N  NH2 . ARG   T  115 ? 1.9323 0.6822 1.3303 -0.0930 -0.4474 0.0256  111 ARG   T NH2 
34772 N  N   . LEU   T  116 ? 1.9029 0.5129 1.1733 -0.0335 -0.5354 -0.0090 112 LEU   T N   
34773 C  CA  . LEU   T  116 ? 1.9396 0.4819 1.1907 0.0176  -0.5301 0.0522  112 LEU   T CA  
34774 C  C   . LEU   T  116 ? 1.9653 0.3774 1.1995 0.0651  -0.5204 0.0686  112 LEU   T C   
34775 O  O   . LEU   T  116 ? 1.9795 0.5070 1.1485 0.1066  -0.4414 0.0952  112 LEU   T O   
34776 C  CB  . LEU   T  116 ? 1.9614 0.4612 1.2164 0.0345  -0.5316 0.0770  112 LEU   T CB  
34777 C  CG  . LEU   T  116 ? 1.9603 0.5398 1.2136 0.0035  -0.5072 0.0917  112 LEU   T CG  
34778 C  CD1 . LEU   T  116 ? 1.9905 0.5153 1.2276 0.0270  -0.5095 0.0786  112 LEU   T CD1 
34779 C  CD2 . LEU   T  116 ? 1.9706 0.5999 1.2248 0.0064  -0.4699 0.0865  112 LEU   T CD2 
34780 N  N   . GLY   T  117 ? 1.9918 0.3007 1.1916 0.1164  -0.5279 0.1283  113 GLY   T N   
34781 C  CA  . GLY   T  117 ? 2.0181 0.2868 1.2191 0.1125  -0.5373 0.1753  113 GLY   T CA  
34782 C  C   . GLY   T  117 ? 1.9947 0.2341 1.2336 0.1196  -0.5342 0.1523  113 GLY   T C   
34783 O  O   . GLY   T  117 ? 2.1712 0.1315 1.2530 0.0486  -0.5503 0.2335  113 GLY   T O   
34784 N  N   . GLN   T  118 ? 1.8471 0.2332 1.2368 0.0886  -0.5087 0.1305  114 GLN   T N   
34785 C  CA  . GLN   T  118 ? 1.7825 0.1579 1.1904 0.0270  -0.4699 0.1536  114 GLN   T CA  
34786 C  C   . GLN   T  118 ? 1.7340 0.1008 1.2099 0.0482  -0.4600 0.1723  114 GLN   T C   
34787 O  O   . GLN   T  118 ? 1.6842 0.1063 1.2124 0.0344  -0.4401 0.1950  114 GLN   T O   
34788 C  CB  . GLN   T  118 ? 1.7676 0.1179 1.1962 -0.0150 -0.4733 0.1777  114 GLN   T CB  
34789 C  CG  . GLN   T  118 ? 1.7568 0.1700 1.2166 -0.0389 -0.4593 0.1986  114 GLN   T CG  
34790 C  CD  . GLN   T  118 ? 1.7537 0.1953 1.2264 -0.0363 -0.4877 0.1452  114 GLN   T CD  
34791 O  OE1 . GLN   T  118 ? 1.7537 0.2795 1.2030 -0.0213 -0.4776 0.1358  114 GLN   T OE1 
34792 N  NE2 . GLN   T  118 ? 1.7573 0.2476 1.2538 -0.0370 -0.4592 0.1116  114 GLN   T NE2 
34793 N  N   . TYR   T  119 ? 1.7234 0.1149 1.1988 0.0486  -0.4795 0.1060  115 TYR   T N   
34794 C  CA  . TYR   T  119 ? 1.7343 0.3172 1.1983 0.0594  -0.4799 0.0681  115 TYR   T CA  
34795 C  C   . TYR   T  119 ? 1.7645 0.3304 1.2356 0.0827  -0.4546 0.0695  115 TYR   T C   
34796 O  O   . TYR   T  119 ? 1.7855 0.4941 1.1906 0.1030  -0.4286 0.1144  115 TYR   T O   
34797 C  CB  . TYR   T  119 ? 1.7101 0.3687 1.1733 0.0734  -0.4745 0.0205  115 TYR   T CB  
34798 C  CG  . TYR   T  119 ? 1.6862 0.3856 1.1243 0.0911  -0.5038 0.0137  115 TYR   T CG  
34799 C  CD1 . TYR   T  119 ? 1.6708 0.3843 1.1049 0.0880  -0.5051 0.0048  115 TYR   T CD1 
34800 C  CD2 . TYR   T  119 ? 1.6799 0.3989 1.1300 0.0898  -0.5115 -0.0072 115 TYR   T CD2 
34801 C  CE1 . TYR   T  119 ? 1.6658 0.3971 1.1088 0.0910  -0.5047 -0.0008 115 TYR   T CE1 
34802 C  CE2 . TYR   T  119 ? 1.6684 0.4008 1.1286 0.0916  -0.5164 -0.0140 115 TYR   T CE2 
34803 C  CZ  . TYR   T  119 ? 1.6664 0.4031 1.1342 0.0941  -0.5172 -0.0124 115 TYR   T CZ  
34804 O  OH  . TYR   T  119 ? 1.6580 0.4221 1.1623 0.0946  -0.4907 -0.0370 115 TYR   T OH  
34805 N  N   . VAL   T  120 ? 1.7705 0.3636 1.2613 0.0760  -0.4668 0.0932  116 VAL   T N   
34806 C  CA  . VAL   T  120 ? 1.7774 0.3517 1.2801 0.0695  -0.4724 0.0998  116 VAL   T CA  
34807 C  C   . VAL   T  120 ? 1.7940 0.3300 1.2899 0.0605  -0.4525 0.0714  116 VAL   T C   
34808 O  O   . VAL   T  120 ? 1.8341 0.5196 1.2064 -0.0527 -0.4337 0.0403  116 VAL   T O   
34809 C  CB  . VAL   T  120 ? 1.7816 0.3548 1.3143 0.0818  -0.4941 0.1098  116 VAL   T CB  
34810 C  CG1 . VAL   T  120 ? 1.7891 0.3564 1.3525 0.0743  -0.5175 0.1020  116 VAL   T CG1 
34811 C  CG2 . VAL   T  120 ? 1.7894 0.2868 1.3028 0.0867  -0.5010 0.1301  116 VAL   T CG2 
34812 N  N   . GLN   T  121 ? 1.7829 0.2884 1.2904 0.1031  -0.4717 0.0881  117 GLN   T N   
34813 C  CA  . GLN   T  121 ? 1.7508 0.2973 1.2745 0.1442  -0.5082 0.1239  117 GLN   T CA  
34814 C  C   . GLN   T  121 ? 1.7425 0.2470 1.2479 0.1608  -0.4756 0.1116  117 GLN   T C   
34815 O  O   . GLN   T  121 ? 1.7012 0.1939 1.2056 0.1631  -0.4763 0.1736  117 GLN   T O   
34816 C  CB  . GLN   T  121 ? 1.7408 0.3381 1.2898 0.1747  -0.5131 0.1548  117 GLN   T CB  
34817 C  CG  . GLN   T  121 ? 1.7728 0.3328 1.3553 0.1591  -0.4901 0.1097  117 GLN   T CG  
34818 C  CD  . GLN   T  121 ? 1.7808 0.3291 1.3727 0.1643  -0.5083 0.0588  117 GLN   T CD  
34819 O  OE1 . GLN   T  121 ? 1.8706 0.1705 1.3984 0.2217  -0.4758 -0.0410 117 GLN   T OE1 
34820 N  NE2 . GLN   T  121 ? 1.8195 0.3488 1.4302 0.1245  -0.4649 0.0936  117 GLN   T NE2 
34821 N  N   . ALA   T  122 ? 1.7636 0.2830 1.2062 0.1112  -0.4577 0.1142  118 ALA   T N   
34822 C  CA  . ALA   T  122 ? 1.7763 0.2536 1.1957 0.1085  -0.4486 0.1088  118 ALA   T CA  
34823 C  C   . ALA   T  122 ? 1.7918 0.2593 1.2310 0.1273  -0.4416 0.0881  118 ALA   T C   
34824 O  O   . ALA   T  122 ? 1.8284 0.1739 1.2030 0.1358  -0.4208 0.0744  118 ALA   T O   
34825 C  CB  . ALA   T  122 ? 1.7712 0.2655 1.1854 0.0777  -0.4674 0.1126  118 ALA   T CB  
34826 N  N   . HIS   T  123 ? 1.7694 0.3338 1.2473 0.1279  -0.4506 0.0700  119 HIS   T N   
34827 C  CA  . HIS   T  123 ? 1.7812 0.3899 1.2469 0.1099  -0.4414 0.0418  119 HIS   T CA  
34828 C  C   . HIS   T  123 ? 1.7697 0.4056 1.2646 0.0777  -0.4426 -0.0088 119 HIS   T C   
34829 O  O   . HIS   T  123 ? 1.8349 0.3435 1.2635 0.0147  -0.4286 -0.0539 119 HIS   T O   
34830 C  CB  . HIS   T  123 ? 1.7932 0.4480 1.2436 0.0872  -0.4435 0.0502  119 HIS   T CB  
34831 C  CG  . HIS   T  123 ? 1.8305 0.4277 1.1428 0.1132  -0.4312 0.0504  119 HIS   T CG  
34832 N  ND1 . HIS   T  123 ? 1.8626 0.4447 1.1287 0.1247  -0.4379 0.0379  119 HIS   T ND1 
34833 C  CD2 . HIS   T  123 ? 1.8577 0.4801 1.0987 0.1113  -0.4413 0.0584  119 HIS   T CD2 
34834 C  CE1 . HIS   T  123 ? 1.8526 0.4907 1.0683 0.1241  -0.4094 0.0284  119 HIS   T CE1 
34835 N  NE2 . HIS   T  123 ? 1.8619 0.4834 1.0675 0.1181  -0.4197 0.0086  119 HIS   T NE2 
34836 N  N   . THR   T  124 ? 1.7433 0.3563 1.2639 0.0900  -0.4519 -0.0267 120 THR   T N   
34837 C  CA  . THR   T  124 ? 1.7497 0.3766 1.3061 0.0716  -0.4340 -0.0447 120 THR   T CA  
34838 C  C   . THR   T  124 ? 1.7691 0.4064 1.2569 0.0649  -0.4353 -0.0084 120 THR   T C   
34839 O  O   . THR   T  124 ? 1.7849 0.3722 1.2219 0.0734  -0.4468 0.0862  120 THR   T O   
34840 C  CB  . THR   T  124 ? 1.7239 0.3925 1.2917 0.0852  -0.4288 -0.0758 120 THR   T CB  
34841 O  OG1 . THR   T  124 ? 1.7334 0.3282 1.3608 0.0655  -0.4497 -0.1535 120 THR   T OG1 
34842 C  CG2 . THR   T  124 ? 1.7474 0.3992 1.3136 0.0934  -0.4545 -0.0836 120 THR   T CG2 
34843 N  N   . LEU   T  125 ? 1.8307 0.3545 1.2890 0.0423  -0.4042 -0.0372 121 LEU   T N   
34844 C  CA  . LEU   T  125 ? 1.8238 0.4292 1.3135 0.0133  -0.4028 -0.0146 121 LEU   T CA  
34845 C  C   . LEU   T  125 ? 1.7918 0.3988 1.3064 -0.0180 -0.4165 0.0235  121 LEU   T C   
34846 O  O   . LEU   T  125 ? 1.8515 0.5244 1.2710 -0.0842 -0.4735 0.0764  121 LEU   T O   
34847 C  CB  . LEU   T  125 ? 1.8760 0.4453 1.3466 0.0426  -0.3594 -0.0048 121 LEU   T CB  
34848 C  CG  . LEU   T  125 ? 1.9302 0.5024 1.3559 0.0336  -0.3594 -0.0288 121 LEU   T CG  
34849 C  CD1 . LEU   T  125 ? 1.9473 0.4816 1.3511 -0.0390 -0.3523 -0.0496 121 LEU   T CD1 
34850 C  CD2 . LEU   T  125 ? 1.9324 0.5285 1.3818 0.0249  -0.3695 -0.0102 121 LEU   T CD2 
34851 N  N   . TYR   T  126 ? 1.7944 0.3581 1.3305 0.0049  -0.4030 0.0596  122 TYR   T N   
34852 C  CA  . TYR   T  126 ? 1.7834 0.4235 1.3295 0.0009  -0.3967 0.0616  122 TYR   T CA  
34853 C  C   . TYR   T  126 ? 1.8087 0.4286 1.3757 -0.0071 -0.3562 0.0571  122 TYR   T C   
34854 O  O   . TYR   T  126 ? 1.8332 0.5221 1.3948 -0.0272 -0.3819 0.0518  122 TYR   T O   
34855 C  CB  . TYR   T  126 ? 1.7745 0.4039 1.3064 -0.0012 -0.3942 0.0224  122 TYR   T CB  
34856 C  CG  . TYR   T  126 ? 1.7719 0.4203 1.3305 -0.0100 -0.4045 -0.0119 122 TYR   T CG  
34857 C  CD1 . TYR   T  126 ? 1.7785 0.3873 1.3248 -0.0001 -0.4028 -0.0339 122 TYR   T CD1 
34858 C  CD2 . TYR   T  126 ? 1.7344 0.3168 1.3962 -0.0217 -0.3917 -0.0280 122 TYR   T CD2 
34859 C  CE1 . TYR   T  126 ? 1.7656 0.3102 1.3744 -0.0294 -0.3930 -0.0064 122 TYR   T CE1 
34860 C  CE2 . TYR   T  126 ? 1.7490 0.2280 1.4215 -0.0545 -0.3937 -0.0060 122 TYR   T CE2 
34861 C  CZ  . TYR   T  126 ? 1.7473 0.2410 1.4206 -0.0598 -0.3925 -0.0009 122 TYR   T CZ  
34862 O  OH  . TYR   T  126 ? 1.7665 0.3595 1.4822 0.0069  -0.3077 -0.0050 122 TYR   T OH  
34863 N  N   . ASN   T  127 ? 1.7507 0.4440 1.4057 -0.0300 -0.3965 0.0507  123 ASN   T N   
34864 C  CA  . ASN   T  127 ? 1.7409 0.5372 1.4837 0.0042  -0.3640 0.0333  123 ASN   T CA  
34865 C  C   . ASN   T  127 ? 1.7266 0.5163 1.5167 -0.0017 -0.3584 0.0190  123 ASN   T C   
34866 O  O   . ASN   T  127 ? 1.6859 0.5629 1.5416 -0.0322 -0.3256 0.0161  123 ASN   T O   
34867 C  CB  . ASN   T  127 ? 1.7464 0.5969 1.5346 -0.0020 -0.3832 0.0030  123 ASN   T CB  
34868 C  CG  . ASN   T  127 ? 1.7526 0.6074 1.5527 -0.0166 -0.4132 -0.0069 123 ASN   T CG  
34869 O  OD1 . ASN   T  127 ? 1.8048 0.6103 1.6768 -0.0338 -0.3993 -0.1041 123 ASN   T OD1 
34870 N  ND2 . ASN   T  127 ? 1.7904 0.6294 1.6003 -0.0286 -0.4027 0.0484  123 ASN   T ND2 
34871 N  N   . SER   T  128 ? 1.6909 0.5184 1.5326 0.0185  -0.3052 0.0341  124 SER   T N   
34872 C  CA  . SER   T  128 ? 1.7044 0.5574 1.5576 0.0509  -0.2380 0.0390  124 SER   T CA  
34873 C  C   . SER   T  128 ? 1.7008 0.4486 1.5550 0.0371  -0.2184 0.0536  124 SER   T C   
34874 O  O   . SER   T  128 ? 1.7560 0.2749 1.6381 0.0230  -0.2004 0.0242  124 SER   T O   
34875 C  CB  . SER   T  128 ? 1.6772 0.5678 1.5864 0.0601  -0.2132 0.0512  124 SER   T CB  
34876 O  OG  . SER   T  128 ? 1.6274 0.6580 1.6566 0.1084  -0.1611 0.0722  124 SER   T OG  
34877 N  N   . VAL   T  129 ? 1.7640 0.4904 1.5179 0.0693  -0.2632 -0.0159 125 VAL   T N   
34878 C  CA  . VAL   T  129 ? 1.7883 0.4601 1.5342 0.0603  -0.2770 -0.0474 125 VAL   T CA  
34879 C  C   . VAL   T  129 ? 1.7632 0.4605 1.4807 0.0767  -0.3086 -0.0831 125 VAL   T C   
34880 O  O   . VAL   T  129 ? 1.7879 0.3173 1.4198 0.1274  -0.2907 -0.1459 125 VAL   T O   
34881 C  CB  . VAL   T  129 ? 1.8287 0.4275 1.6025 0.0541  -0.2579 -0.0532 125 VAL   T CB  
34882 C  CG1 . VAL   T  129 ? 1.8497 0.5128 1.5764 0.0323  -0.2388 0.0157  125 VAL   T CG1 
34883 C  CG2 . VAL   T  129 ? 1.8254 0.3768 1.6277 0.0714  -0.2568 -0.0264 125 VAL   T CG2 
34884 N  N   . ARG   T  130 ? 1.7938 0.4780 1.4525 0.0590  -0.3508 -0.0511 126 ARG   T N   
34885 C  CA  . ARG   T  130 ? 1.8016 0.4567 1.4325 0.0228  -0.3766 -0.0435 126 ARG   T CA  
34886 C  C   . ARG   T  130 ? 1.7732 0.4356 1.3906 0.0442  -0.3879 0.0383  126 ARG   T C   
34887 O  O   . ARG   T  130 ? 1.7824 0.5217 1.3525 0.0191  -0.3634 -0.0682 126 ARG   T O   
34888 C  CB  . ARG   T  130 ? 1.7952 0.4174 1.4440 0.0355  -0.3968 -0.0324 126 ARG   T CB  
34889 C  CG  . ARG   T  130 ? 1.8360 0.4469 1.4654 0.0356  -0.4149 -0.0102 126 ARG   T CG  
34890 C  CD  . ARG   T  130 ? 1.8380 0.4582 1.4896 -0.0108 -0.3959 -0.0148 126 ARG   T CD  
34891 N  NE  . ARG   T  130 ? 1.8434 0.4526 1.4620 -0.0094 -0.4001 0.0338  126 ARG   T NE  
34892 C  CZ  . ARG   T  130 ? 1.8279 0.4790 1.4654 -0.0169 -0.4208 0.0569  126 ARG   T CZ  
34893 N  NH1 . ARG   T  130 ? 1.8421 0.4987 1.4767 -0.0203 -0.4489 0.0742  126 ARG   T NH1 
34894 N  NH2 . ARG   T  130 ? 1.7939 0.5031 1.4292 -0.0370 -0.4343 0.0087  126 ARG   T NH2 
34895 N  N   . PRO   T  131 ? 1.7776 0.4016 1.3909 0.0715  -0.4176 0.0476  127 PRO   T N   
34896 C  CA  . PRO   T  131 ? 1.7840 0.3926 1.3875 0.0746  -0.4326 0.0706  127 PRO   T CA  
34897 C  C   . PRO   T  131 ? 1.7914 0.3133 1.3943 0.0626  -0.4336 0.0651  127 PRO   T C   
34898 O  O   . PRO   T  131 ? 1.7906 0.2577 1.4140 0.0820  -0.4316 0.0501  127 PRO   T O   
34899 C  CB  . PRO   T  131 ? 1.8054 0.3953 1.3897 0.0689  -0.4269 0.0659  127 PRO   T CB  
34900 C  CG  . PRO   T  131 ? 1.8004 0.3961 1.4004 0.0649  -0.4256 0.0545  127 PRO   T CG  
34901 C  CD  . PRO   T  131 ? 1.7917 0.3976 1.4124 0.0666  -0.4177 0.0597  127 PRO   T CD  
34902 N  N   . PHE   T  132 ? 1.8233 0.2831 1.4209 0.0420  -0.4795 0.0624  128 PHE   T N   
34903 C  CA  . PHE   T  132 ? 1.8215 0.3582 1.4925 0.0610  -0.4924 0.0257  128 PHE   T CA  
34904 C  C   . PHE   T  132 ? 1.8119 0.3922 1.5445 0.1232  -0.4946 -0.0174 128 PHE   T C   
34905 O  O   . PHE   T  132 ? 1.7661 0.3563 1.5976 0.1201  -0.4814 -0.0481 128 PHE   T O   
34906 C  CB  . PHE   T  132 ? 1.8433 0.4031 1.4958 0.0788  -0.5068 0.0075  128 PHE   T CB  
34907 C  CG  . PHE   T  132 ? 1.8398 0.4178 1.5470 0.1014  -0.5168 0.0178  128 PHE   T CG  
34908 C  CD1 . PHE   T  132 ? 1.8177 0.4890 1.5785 0.0827  -0.5318 -0.0292 128 PHE   T CD1 
34909 C  CD2 . PHE   T  132 ? 1.8327 0.4052 1.6183 0.0842  -0.5093 -0.0496 128 PHE   T CD2 
34910 C  CE1 . PHE   T  132 ? 1.8042 0.4127 1.5771 0.0237  -0.5377 -0.0964 128 PHE   T CE1 
34911 C  CE2 . PHE   T  132 ? 1.8299 0.3535 1.6198 0.0405  -0.4897 -0.0929 128 PHE   T CE2 
34912 C  CZ  . PHE   T  132 ? 1.8274 0.3732 1.5670 0.0241  -0.5278 -0.0921 128 PHE   T CZ  
34913 N  N   . GLY   T  133 ? 1.8106 0.4177 1.5634 0.1105  -0.4853 -0.0292 129 GLY   T N   
34914 C  CA  . GLY   T  133 ? 1.8206 0.4102 1.5966 0.1075  -0.5066 -0.0356 129 GLY   T CA  
34915 C  C   . GLY   T  133 ? 1.8064 0.3777 1.6149 0.0918  -0.5207 -0.0222 129 GLY   T C   
34916 O  O   . GLY   T  133 ? 1.7861 0.2505 1.6280 0.0388  -0.5423 -0.0418 129 GLY   T O   
34917 N  N   . VAL   T  134 ? 1.7985 0.3822 1.5694 0.0994  -0.5465 -0.0094 130 VAL   T N   
34918 C  CA  . VAL   T  134 ? 1.8215 0.4772 1.5643 0.1219  -0.5504 -0.0133 130 VAL   T CA  
34919 C  C   . VAL   T  134 ? 1.8314 0.4294 1.5796 0.1444  -0.5354 -0.0206 130 VAL   T C   
34920 O  O   . VAL   T  134 ? 1.8534 0.4730 1.5066 0.1753  -0.5617 0.0082  130 VAL   T O   
34921 C  CB  . VAL   T  134 ? 1.7915 0.5072 1.5758 0.1043  -0.5699 -0.0008 130 VAL   T CB  
34922 C  CG1 . VAL   T  134 ? 1.8054 0.5849 1.6164 0.1051  -0.5515 -0.0368 130 VAL   T CG1 
34923 C  CG2 . VAL   T  134 ? 1.7724 0.5639 1.5413 0.1071  -0.5895 0.0090  130 VAL   T CG2 
34924 N  N   . SER   T  135 ? 1.9164 0.4536 1.5527 0.1366  -0.5391 -0.0415 131 SER   T N   
34925 C  CA  . SER   T  135 ? 1.9336 0.6063 1.5607 0.1523  -0.5348 -0.0553 131 SER   T CA  
34926 C  C   . SER   T  135 ? 1.8772 0.6085 1.5493 0.1597  -0.5629 -0.0035 131 SER   T C   
34927 O  O   . SER   T  135 ? 1.8736 0.8256 1.6303 0.1624  -0.5479 0.0422  131 SER   T O   
34928 C  CB  . SER   T  135 ? 1.9759 0.6087 1.5613 0.1300  -0.5588 -0.0695 131 SER   T CB  
34929 O  OG  . SER   T  135 ? 1.9876 0.7344 1.6269 0.0931  -0.5494 -0.1572 131 SER   T OG  
34930 N  N   . THR   T  136 ? 1.9066 0.6013 1.5145 0.1940  -0.5444 0.0501  132 THR   T N   
34931 C  CA  . THR   T  136 ? 1.9206 0.5334 1.5070 0.2208  -0.5062 0.0640  132 THR   T CA  
34932 C  C   . THR   T  136 ? 1.8446 0.4459 1.4850 0.2637  -0.5563 0.1228  132 THR   T C   
34933 O  O   . THR   T  136 ? 1.8451 0.3545 1.5392 0.3054  -0.5487 0.1471  132 THR   T O   
34934 C  CB  . THR   T  136 ? 1.9681 0.5330 1.4712 0.2202  -0.4296 0.0753  132 THR   T CB  
34935 O  OG1 . THR   T  136 ? 2.0366 0.4958 1.4916 0.2233  -0.3690 0.0498  132 THR   T OG1 
34936 C  CG2 . THR   T  136 ? 1.9519 0.6139 1.4812 0.1874  -0.4243 0.0470  132 THR   T CG2 
34937 N  N   . ILE   T  137 ? 1.8759 0.4797 1.4542 0.2427  -0.5709 0.1336  133 ILE   T N   
34938 C  CA  . ILE   T  137 ? 1.8753 0.5689 1.4374 0.1965  -0.5815 0.1369  133 ILE   T CA  
34939 C  C   . ILE   T  137 ? 1.8090 0.5706 1.3385 0.1978  -0.6030 0.1561  133 ILE   T C   
34940 O  O   . ILE   T  137 ? 1.7959 0.5949 1.3232 0.1889  -0.6130 0.1332  133 ILE   T O   
34941 C  CB  . ILE   T  137 ? 1.9105 0.6750 1.4304 0.2070  -0.6164 0.1541  133 ILE   T CB  
34942 C  CG1 . ILE   T  137 ? 1.9461 0.6977 1.4966 0.1765  -0.6074 0.1348  133 ILE   T CG1 
34943 C  CG2 . ILE   T  137 ? 1.9511 0.7019 1.4391 0.1637  -0.6123 0.1350  133 ILE   T CG2 
34944 C  CD1 . ILE   T  137 ? 1.9583 0.7255 1.5568 0.2041  -0.6133 0.1155  133 ILE   T CD1 
34945 N  N   . PHE   T  138 ? 1.8086 0.5486 1.2793 0.1584  -0.5984 0.1509  134 PHE   T N   
34946 C  CA  . PHE   T  138 ? 1.8160 0.5541 1.2956 0.1221  -0.5949 0.1444  134 PHE   T CA  
34947 C  C   . PHE   T  138 ? 1.8316 0.5250 1.2739 0.0858  -0.5694 0.1858  134 PHE   T C   
34948 O  O   . PHE   T  138 ? 1.8872 0.5801 1.2742 0.0349  -0.5567 0.1850  134 PHE   T O   
34949 C  CB  . PHE   T  138 ? 1.8242 0.4630 1.3172 0.1385  -0.5837 0.1369  134 PHE   T CB  
34950 C  CG  . PHE   T  138 ? 1.8221 0.3974 1.3466 0.1421  -0.5868 0.1185  134 PHE   T CG  
34951 C  CD1 . PHE   T  138 ? 1.8038 0.4121 1.3564 0.1413  -0.5976 0.1105  134 PHE   T CD1 
34952 C  CD2 . PHE   T  138 ? 1.8074 0.4277 1.3246 0.1474  -0.5883 0.1188  134 PHE   T CD2 
34953 C  CE1 . PHE   T  138 ? 1.8033 0.3779 1.3306 0.1438  -0.5865 0.1351  134 PHE   T CE1 
34954 C  CE2 . PHE   T  138 ? 1.8175 0.3760 1.2722 0.1162  -0.6060 0.1271  134 PHE   T CE2 
34955 C  CZ  . PHE   T  138 ? 1.8178 0.3166 1.2904 0.1249  -0.5916 0.1567  134 PHE   T CZ  
34956 N  N   . GLY   T  139 ? 1.8362 0.4941 1.3272 0.0945  -0.5324 0.2019  135 GLY   T N   
34957 C  CA  . GLY   T  139 ? 1.8350 0.4848 1.3467 0.0878  -0.4997 0.2139  135 GLY   T CA  
34958 C  C   . GLY   T  139 ? 1.8605 0.4455 1.3298 0.0907  -0.4835 0.2283  135 GLY   T C   
34959 O  O   . GLY   T  139 ? 1.8575 0.2889 1.3750 0.0643  -0.4835 0.1979  135 GLY   T O   
34960 N  N   . GLY   T  140 ? 1.8882 0.4616 1.2676 0.0679  -0.4992 0.2600  136 GLY   T N   
34961 C  CA  . GLY   T  140 ? 1.9120 0.5271 1.2619 0.0192  -0.5036 0.2570  136 GLY   T CA  
34962 C  C   . GLY   T  140 ? 1.9658 0.6093 1.2632 0.0470  -0.4783 0.2801  136 GLY   T C   
34963 O  O   . GLY   T  140 ? 1.9999 0.6735 1.3098 0.0294  -0.4781 0.3346  136 GLY   T O   
34964 N  N   . VAL   T  141 ? 1.9672 0.6277 1.3250 0.0240  -0.4962 0.2507  137 VAL   T N   
34965 C  CA  . VAL   T  141 ? 1.9374 0.6240 1.3591 -0.0004 -0.5283 0.1966  137 VAL   T CA  
34966 C  C   . VAL   T  141 ? 1.9275 0.5575 1.3747 -0.0267 -0.5182 0.1760  137 VAL   T C   
34967 O  O   . VAL   T  141 ? 1.9082 0.4527 1.4508 0.0030  -0.5013 0.1589  137 VAL   T O   
34968 C  CB  . VAL   T  141 ? 1.9346 0.7830 1.4568 -0.0286 -0.5582 0.1687  137 VAL   T CB  
34969 C  CG1 . VAL   T  141 ? 1.9601 0.8229 1.5105 -0.0339 -0.5126 0.1428  137 VAL   T CG1 
34970 C  CG2 . VAL   T  141 ? 1.9166 0.7682 1.4905 -0.0405 -0.5819 0.1568  137 VAL   T CG2 
34971 N  N   . ASP   T  142 ? 1.9235 0.4158 1.3393 0.0223  -0.5289 0.1899  138 ASP   T N   
34972 C  CA  . ASP   T  142 ? 1.9877 0.4195 1.3994 0.0697  -0.4729 0.1604  138 ASP   T CA  
34973 C  C   . ASP   T  142 ? 1.9766 0.5285 1.2624 0.0171  -0.5654 0.2212  138 ASP   T C   
34974 O  O   . ASP   T  142 ? 1.9469 0.3549 1.3546 -0.0055 -0.5531 0.2564  138 ASP   T O   
34975 C  CB  . ASP   T  142 ? 2.0513 0.4511 1.4031 0.1272  -0.4856 0.1024  138 ASP   T CB  
34976 C  CG  . ASP   T  142 ? 2.0852 0.4485 1.4498 0.1698  -0.4314 0.1318  138 ASP   T CG  
34977 O  OD1 . ASP   T  142 ? 2.2201 0.5091 1.4679 0.3209  -0.4064 0.2054  138 ASP   T OD1 
34978 O  OD2 . ASP   T  142 ? 2.1315 0.5730 1.4047 0.2598  -0.4680 0.0445  138 ASP   T OD2 
34979 N  N   . LYS   T  143 ? 1.9301 0.7411 1.3573 0.0715  -0.4880 0.0856  139 LYS   T N   
34980 C  CA  . LYS   T  143 ? 1.9267 0.8698 1.2925 0.0460  -0.4886 0.0923  139 LYS   T CA  
34981 C  C   . LYS   T  143 ? 1.9219 0.8286 1.2084 0.0548  -0.5380 0.0811  139 LYS   T C   
34982 O  O   . LYS   T  143 ? 1.8948 0.9591 1.1300 0.0549  -0.5472 0.1988  139 LYS   T O   
34983 C  CB  . LYS   T  143 ? 1.8850 0.9688 1.3849 0.1088  -0.4938 0.0458  139 LYS   T CB  
34984 C  CG  . LYS   T  143 ? 1.8506 1.1300 1.4072 0.1078  -0.5000 0.0262  139 LYS   T CG  
34985 C  CD  . LYS   T  143 ? 1.8518 1.2666 1.4314 0.0876  -0.5063 0.0013  139 LYS   T CD  
34986 C  CE  . LYS   T  143 ? 1.8073 1.4380 1.3650 0.0614  -0.5553 -0.0242 139 LYS   T CE  
34987 N  NZ  . LYS   T  143 ? 1.7926 1.5691 1.3709 0.0731  -0.5656 -0.0557 139 LYS   T NZ  
34988 N  N   . ASN   T  144 ? 1.9143 0.7531 1.1869 0.0505  -0.5106 0.1671  140 ASN   T N   
34989 C  CA  . ASN   T  144 ? 1.9489 0.7502 1.2429 0.0055  -0.4738 0.1422  140 ASN   T CA  
34990 C  C   . ASN   T  144 ? 1.9500 0.6875 1.2859 -0.0458 -0.4638 0.2066  140 ASN   T C   
34991 O  O   . ASN   T  144 ? 1.9911 0.6320 1.3222 0.0035  -0.5136 0.2256  140 ASN   T O   
34992 C  CB  . ASN   T  144 ? 1.9485 0.7095 1.2651 -0.0103 -0.4373 0.1221  140 ASN   T CB  
34993 C  CG  . ASN   T  144 ? 1.9564 0.6802 1.2731 0.0025  -0.3623 0.0485  140 ASN   T CG  
34994 O  OD1 . ASN   T  144 ? 1.9882 0.7527 1.2522 -0.0416 -0.3440 0.0655  140 ASN   T OD1 
34995 N  ND2 . ASN   T  144 ? 1.9836 0.6755 1.2999 -0.0107 -0.3525 0.0100  140 ASN   T ND2 
34996 N  N   . GLY   T  145 ? 1.9297 0.7710 1.3314 0.0009  -0.4465 0.1769  141 GLY   T N   
34997 C  CA  . GLY   T  145 ? 1.9865 0.7204 1.2826 0.0114  -0.4526 0.1976  141 GLY   T CA  
34998 C  C   . GLY   T  145 ? 1.9999 0.7523 1.2755 0.0327  -0.4620 0.1880  141 GLY   T C   
34999 O  O   . GLY   T  145 ? 2.0398 0.7499 1.2385 0.0887  -0.4674 0.1349  141 GLY   T O   
35000 N  N   . ALA   T  146 ? 1.9685 0.7804 1.2412 0.0785  -0.4617 0.1329  142 ALA   T N   
35001 C  CA  . ALA   T  146 ? 1.9635 0.7669 1.2806 0.1163  -0.4698 0.1330  142 ALA   T CA  
35002 C  C   . ALA   T  146 ? 1.9844 0.7105 1.2588 0.1449  -0.4514 0.1015  142 ALA   T C   
35003 O  O   . ALA   T  146 ? 2.0038 0.6019 1.2676 0.2188  -0.3985 0.0944  142 ALA   T O   
35004 C  CB  . ALA   T  146 ? 1.9607 0.7933 1.3188 0.1139  -0.4877 0.1412  142 ALA   T CB  
35005 N  N   . HIS   T  147 ? 2.0003 0.7173 1.2524 0.1333  -0.4874 0.0825  143 HIS   T N   
35006 C  CA  . HIS   T  147 ? 2.0047 0.7561 1.2074 0.1231  -0.5148 0.1039  143 HIS   T CA  
35007 C  C   . HIS   T  147 ? 1.9755 0.7493 1.2219 0.0992  -0.5310 0.0800  143 HIS   T C   
35008 O  O   . HIS   T  147 ? 1.9769 0.7868 1.1180 0.1050  -0.5862 0.1328  143 HIS   T O   
35009 C  CB  . HIS   T  147 ? 2.0250 0.7458 1.1163 0.1565  -0.4715 0.0987  143 HIS   T CB  
35010 C  CG  . HIS   T  147 ? 2.0484 0.8248 1.0860 0.1530  -0.4275 0.0916  143 HIS   T CG  
35011 N  ND1 . HIS   T  147 ? 2.0509 0.8449 1.1087 0.1353  -0.4016 0.0636  143 HIS   T ND1 
35012 C  CD2 . HIS   T  147 ? 2.0843 0.8455 1.0403 0.1494  -0.3883 0.1150  143 HIS   T CD2 
35013 C  CE1 . HIS   T  147 ? 2.0819 0.8739 1.1029 0.1329  -0.3578 0.0868  143 HIS   T CE1 
35014 N  NE2 . HIS   T  147 ? 2.0703 0.8900 1.0297 0.1400  -0.3445 0.0911  143 HIS   T NE2 
35015 N  N   . LEU   T  148 ? 1.9669 0.7564 1.3148 0.0570  -0.5616 0.0959  144 LEU   T N   
35016 C  CA  . LEU   T  148 ? 1.9698 0.6531 1.3747 0.0529  -0.5362 0.1299  144 LEU   T CA  
35017 C  C   . LEU   T  148 ? 1.9656 0.5207 1.4661 -0.0222 -0.4903 0.1575  144 LEU   T C   
35018 O  O   . LEU   T  148 ? 2.0537 0.3248 1.5473 -0.0667 -0.4633 0.2256  144 LEU   T O   
35019 C  CB  . LEU   T  148 ? 1.9607 0.6865 1.3804 0.0542  -0.5574 0.1322  144 LEU   T CB  
35020 C  CG  . LEU   T  148 ? 1.9650 0.7506 1.3985 0.0535  -0.5342 0.0966  144 LEU   T CG  
35021 C  CD1 . LEU   T  148 ? 1.9650 0.7409 1.3791 0.0786  -0.5219 0.0995  144 LEU   T CD1 
35022 C  CD2 . LEU   T  148 ? 1.9699 0.7799 1.4092 0.0697  -0.5602 0.0979  144 LEU   T CD2 
35023 N  N   . TYR   T  149 ? 1.9823 0.4935 1.4778 -0.0218 -0.4989 0.1124  145 TYR   T N   
35024 C  CA  . TYR   T  149 ? 1.9514 0.4204 1.5205 0.0128  -0.5341 0.1352  145 TYR   T CA  
35025 C  C   . TYR   T  149 ? 1.9991 0.4117 1.5622 0.0218  -0.5204 0.1236  145 TYR   T C   
35026 O  O   . TYR   T  149 ? 2.0101 0.3535 1.6174 0.0117  -0.5003 0.0920  145 TYR   T O   
35027 C  CB  . TYR   T  149 ? 1.9115 0.4295 1.4987 0.0237  -0.5501 0.1066  145 TYR   T CB  
35028 C  CG  . TYR   T  149 ? 1.9300 0.3641 1.4990 0.0383  -0.5580 0.1216  145 TYR   T CG  
35029 C  CD1 . TYR   T  149 ? 1.9344 0.3316 1.4827 0.0453  -0.5453 0.1633  145 TYR   T CD1 
35030 C  CD2 . TYR   T  149 ? 1.9216 0.2914 1.5474 0.0588  -0.5601 0.1619  145 TYR   T CD2 
35031 C  CE1 . TYR   T  149 ? 1.9190 0.2653 1.4739 0.0643  -0.5607 0.2191  145 TYR   T CE1 
35032 C  CE2 . TYR   T  149 ? 1.9177 0.2931 1.5576 0.0753  -0.5582 0.1907  145 TYR   T CE2 
35033 C  CZ  . TYR   T  149 ? 1.8968 0.2321 1.5085 0.1158  -0.5512 0.2160  145 TYR   T CZ  
35034 O  OH  . TYR   T  149 ? 1.8707 0.2869 1.5240 0.1909  -0.5607 0.2814  145 TYR   T OH  
35035 N  N   . MET   T  150 ? 2.0096 0.3582 1.5636 0.0271  -0.5292 0.1674  146 MET   T N   
35036 C  CA  . MET   T  150 ? 2.0488 0.3710 1.5824 0.0417  -0.5065 0.1735  146 MET   T CA  
35037 C  C   . MET   T  150 ? 2.0157 0.2668 1.5841 0.0267  -0.4912 0.2409  146 MET   T C   
35038 O  O   . MET   T  150 ? 2.0416 0.1950 1.6060 -0.0056 -0.4852 0.2736  146 MET   T O   
35039 C  CB  . MET   T  150 ? 2.1081 0.4000 1.6241 0.0842  -0.5188 0.1920  146 MET   T CB  
35040 C  CG  . MET   T  150 ? 2.1775 0.4293 1.6837 0.0718  -0.5186 0.1198  146 MET   T CG  
35041 S  SD  . MET   T  150 ? 2.2720 0.3287 1.7897 0.0404  -0.5726 0.0594  146 MET   T SD  
35042 C  CE  . MET   T  150 ? 2.2502 0.4736 1.7426 0.0585  -0.5002 0.0445  146 MET   T CE  
35043 N  N   . LEU   T  151 ? 2.0357 0.3285 1.5716 0.0482  -0.4878 0.2175  147 LEU   T N   
35044 C  CA  . LEU   T  151 ? 2.0295 0.4675 1.5594 0.0554  -0.4856 0.1701  147 LEU   T CA  
35045 C  C   . LEU   T  151 ? 2.0340 0.5007 1.5769 0.0566  -0.4612 0.1541  147 LEU   T C   
35046 O  O   . LEU   T  151 ? 2.0381 0.6133 1.6867 0.0649  -0.4431 0.1275  147 LEU   T O   
35047 C  CB  . LEU   T  151 ? 2.0226 0.5073 1.5360 0.0231  -0.5261 0.2041  147 LEU   T CB  
35048 C  CG  . LEU   T  151 ? 2.0503 0.5313 1.5290 -0.0106 -0.5288 0.2201  147 LEU   T CG  
35049 C  CD1 . LEU   T  151 ? 2.0492 0.5724 1.4997 0.0121  -0.5435 0.2214  147 LEU   T CD1 
35050 C  CD2 . LEU   T  151 ? 2.0064 0.5703 1.5256 -0.0841 -0.4960 0.1984  147 LEU   T CD2 
35051 N  N   . GLU   T  152 ? 1.9978 0.5681 1.5113 0.0630  -0.4312 0.1189  148 GLU   T N   
35052 C  CA  . GLU   T  152 ? 1.9722 0.6026 1.5555 0.0984  -0.4248 0.0810  148 GLU   T CA  
35053 C  C   . GLU   T  152 ? 1.9061 0.5046 1.5046 0.0646  -0.4061 -0.0147 148 GLU   T C   
35054 O  O   . GLU   T  152 ? 1.8529 0.5935 1.5050 0.0611  -0.4469 0.0120  148 GLU   T O   
35055 C  CB  . GLU   T  152 ? 2.0351 0.6351 1.6117 0.1192  -0.2997 0.0911  148 GLU   T CB  
35056 C  CG  . GLU   T  152 ? 2.0826 0.7508 1.6364 0.1758  -0.2727 0.1324  148 GLU   T CG  
35057 C  CD  . GLU   T  152 ? 2.2058 0.9254 1.6925 0.1450  -0.1173 0.1487  148 GLU   T CD  
35058 O  OE1 . GLU   T  152 ? 2.2072 1.0953 1.7549 0.2577  -0.1299 0.2210  148 GLU   T OE1 
35059 O  OE2 . GLU   T  152 ? 2.2156 1.0695 1.8154 0.3593  -0.1636 -0.0479 148 GLU   T OE2 
35060 N  N   . PRO   T  153 ? 1.8450 0.3777 1.5030 0.0760  -0.4836 -0.0227 149 PRO   T N   
35061 C  CA  . PRO   T  153 ? 1.8200 0.3738 1.4726 0.0559  -0.4718 -0.0920 149 PRO   T CA  
35062 C  C   . PRO   T  153 ? 1.8044 0.3783 1.4516 0.0231  -0.4469 -0.1574 149 PRO   T C   
35063 O  O   . PRO   T  153 ? 1.7486 0.4768 1.3484 0.0495  -0.4676 -0.2579 149 PRO   T O   
35064 C  CB  . PRO   T  153 ? 1.8171 0.3767 1.4980 0.0765  -0.4910 -0.0918 149 PRO   T CB  
35065 C  CG  . PRO   T  153 ? 1.8268 0.4551 1.5196 0.0859  -0.5057 -0.0733 149 PRO   T CG  
35066 C  CD  . PRO   T  153 ? 1.8319 0.4514 1.5105 0.1055  -0.4992 -0.0441 149 PRO   T CD  
35067 N  N   . SER   T  154 ? 1.8315 0.3312 1.4010 0.0083  -0.4890 -0.1377 150 SER   T N   
35068 C  CA  . SER   T  154 ? 1.8317 0.4595 1.3908 -0.0333 -0.4951 -0.1173 150 SER   T CA  
35069 C  C   . SER   T  154 ? 1.8685 0.4667 1.3872 -0.0198 -0.4465 -0.0842 150 SER   T C   
35070 O  O   . SER   T  154 ? 1.8274 0.5335 1.4696 -0.0539 -0.4081 -0.0273 150 SER   T O   
35071 C  CB  . SER   T  154 ? 1.8240 0.5068 1.3129 -0.0339 -0.4908 -0.1416 150 SER   T CB  
35072 O  OG  . SER   T  154 ? 1.8105 0.6100 1.3425 -0.0803 -0.4891 -0.2310 150 SER   T OG  
35073 N  N   . GLY   T  155 ? 1.8841 0.5255 1.3175 -0.0240 -0.4795 -0.0506 151 GLY   T N   
35074 C  CA  . GLY   T  155 ? 1.9031 0.4540 1.3114 -0.0343 -0.4703 0.0252  151 GLY   T CA  
35075 C  C   . GLY   T  155 ? 1.9348 0.4654 1.3324 -0.0402 -0.4575 0.1152  151 GLY   T C   
35076 O  O   . GLY   T  155 ? 1.9402 0.2503 1.2659 -0.0940 -0.4905 0.2730  151 GLY   T O   
35077 N  N   . SER   T  156 ? 1.9432 0.4657 1.3659 0.0153  -0.4414 0.1199  152 SER   T N   
35078 C  CA  . SER   T  156 ? 1.9627 0.5056 1.3608 0.0510  -0.4442 0.1149  152 SER   T CA  
35079 C  C   . SER   T  156 ? 1.9348 0.4397 1.3635 0.0948  -0.4607 0.1527  152 SER   T C   
35080 O  O   . SER   T  156 ? 1.9525 0.3465 1.2609 0.1662  -0.4657 0.2019  152 SER   T O   
35081 C  CB  . SER   T  156 ? 2.0070 0.5003 1.4848 0.0185  -0.4219 0.0632  152 SER   T CB  
35082 O  OG  . SER   T  156 ? 2.0698 0.5932 1.4850 0.0400  -0.3948 0.0379  152 SER   T OG  
35083 N  N   . TYR   T  157 ? 1.9368 0.4400 1.3838 0.0999  -0.4545 0.1452  153 TYR   T N   
35084 C  CA  . TYR   T  157 ? 1.9070 0.4676 1.3823 0.1061  -0.4519 0.1538  153 TYR   T CA  
35085 C  C   . TYR   T  157 ? 1.9035 0.4165 1.3463 0.0997  -0.4868 0.1689  153 TYR   T C   
35086 O  O   . TYR   T  157 ? 1.9050 0.4722 1.2999 0.0687  -0.4390 0.1309  153 TYR   T O   
35087 C  CB  . TYR   T  157 ? 1.8433 0.4962 1.3716 0.0924  -0.4066 0.1489  153 TYR   T CB  
35088 C  CG  . TYR   T  157 ? 1.8171 0.5121 1.3023 0.0954  -0.3936 0.1635  153 TYR   T CG  
35089 C  CD1 . TYR   T  157 ? 1.7765 0.5019 1.3094 0.1074  -0.3725 0.1629  153 TYR   T CD1 
35090 C  CD2 . TYR   T  157 ? 1.7832 0.5012 1.2965 0.1156  -0.3504 0.1947  153 TYR   T CD2 
35091 C  CE1 . TYR   T  157 ? 1.7530 0.5338 1.2494 0.1072  -0.3506 0.1549  153 TYR   T CE1 
35092 C  CE2 . TYR   T  157 ? 1.7551 0.5331 1.2673 0.1064  -0.3251 0.1441  153 TYR   T CE2 
35093 C  CZ  . TYR   T  157 ? 1.7362 0.5337 1.2492 0.1117  -0.3453 0.1514  153 TYR   T CZ  
35094 O  OH  . TYR   T  157 ? 1.6979 0.6147 1.2441 0.1331  -0.3322 0.1296  153 TYR   T OH  
35095 N  N   . TRP   T  158 ? 1.9199 0.3449 1.4047 0.0982  -0.5281 0.2053  154 TRP   T N   
35096 C  CA  . TRP   T  158 ? 1.9172 0.3751 1.3939 0.0632  -0.5577 0.2060  154 TRP   T CA  
35097 C  C   . TRP   T  158 ? 1.9751 0.2957 1.3567 0.0475  -0.5580 0.2272  154 TRP   T C   
35098 O  O   . TRP   T  158 ? 1.9711 0.2798 1.4058 0.0292  -0.5715 0.2496  154 TRP   T O   
35099 C  CB  . TRP   T  158 ? 1.9139 0.3821 1.4551 0.0169  -0.5801 0.2092  154 TRP   T CB  
35100 C  CG  . TRP   T  158 ? 1.8926 0.3279 1.4886 0.0724  -0.5852 0.1607  154 TRP   T CG  
35101 C  CD1 . TRP   T  158 ? 1.8751 0.2488 1.5519 0.0427  -0.6300 0.1773  154 TRP   T CD1 
35102 C  CD2 . TRP   T  158 ? 1.8864 0.3332 1.4530 0.0412  -0.6414 0.1651  154 TRP   T CD2 
35103 N  NE1 . TRP   T  158 ? 1.8886 0.1869 1.5307 0.0660  -0.6370 0.1502  154 TRP   T NE1 
35104 C  CE2 . TRP   T  158 ? 1.8971 0.2323 1.4912 0.0845  -0.6232 0.1800  154 TRP   T CE2 
35105 C  CE3 . TRP   T  158 ? 1.8810 0.3772 1.4366 0.0531  -0.6214 0.1673  154 TRP   T CE3 
35106 C  CZ2 . TRP   T  158 ? 1.9059 0.2629 1.4904 0.0613  -0.6170 0.1891  154 TRP   T CZ2 
35107 C  CZ3 . TRP   T  158 ? 1.8780 0.4099 1.4385 0.0421  -0.6032 0.1425  154 TRP   T CZ3 
35108 C  CH2 . TRP   T  158 ? 1.9030 0.3487 1.4619 0.0675  -0.5873 0.1530  154 TRP   T CH2 
35109 N  N   . GLY   T  159 ? 1.9756 0.2989 1.3433 0.0438  -0.5486 0.2343  155 GLY   T N   
35110 C  CA  . GLY   T  159 ? 1.9820 0.4280 1.3748 0.0190  -0.5403 0.1833  155 GLY   T CA  
35111 C  C   . GLY   T  159 ? 1.9933 0.4061 1.4275 0.0323  -0.5332 0.1622  155 GLY   T C   
35112 O  O   . GLY   T  159 ? 2.0109 0.3451 1.4459 0.0720  -0.5264 0.1614  155 GLY   T O   
35113 N  N   . TYR   T  160 ? 1.9919 0.5458 1.4612 -0.0196 -0.5101 0.0975  156 TYR   T N   
35114 C  CA  . TYR   T  160 ? 2.0023 0.5626 1.4325 -0.0455 -0.5443 0.1099  156 TYR   T CA  
35115 C  C   . TYR   T  160 ? 2.0442 0.6717 1.3762 -0.0448 -0.5606 0.1667  156 TYR   T C   
35116 O  O   . TYR   T  160 ? 2.0047 0.7448 1.3629 -0.1464 -0.5415 0.1706  156 TYR   T O   
35117 C  CB  . TYR   T  160 ? 2.0025 0.6280 1.4763 -0.0879 -0.5207 0.0550  156 TYR   T CB  
35118 C  CG  . TYR   T  160 ? 2.0212 0.6180 1.5063 -0.1094 -0.4932 0.0284  156 TYR   T CG  
35119 C  CD1 . TYR   T  160 ? 2.0005 0.6588 1.4532 -0.1216 -0.4998 -0.0260 156 TYR   T CD1 
35120 C  CD2 . TYR   T  160 ? 2.0065 0.6015 1.4864 -0.1195 -0.5234 -0.0115 156 TYR   T CD2 
35121 C  CE1 . TYR   T  160 ? 2.0097 0.5382 1.4816 -0.1253 -0.4642 -0.0234 156 TYR   T CE1 
35122 C  CE2 . TYR   T  160 ? 2.0315 0.4850 1.5307 -0.1206 -0.4792 -0.0302 156 TYR   T CE2 
35123 C  CZ  . TYR   T  160 ? 2.0129 0.5099 1.4478 -0.1645 -0.4911 -0.1131 156 TYR   T CZ  
35124 O  OH  . TYR   T  160 ? 2.0961 0.3794 1.5108 -0.1334 -0.3928 -0.1927 156 TYR   T OH  
35125 N  N   . LYS   T  161 ? 2.0792 0.6083 1.4229 -0.0571 -0.5731 0.1666  157 LYS   T N   
35126 C  CA  . LYS   T  161 ? 2.0519 0.6104 1.4319 -0.0560 -0.5734 0.2262  157 LYS   T CA  
35127 C  C   . LYS   T  161 ? 2.0199 0.5420 1.4665 -0.0219 -0.6104 0.2567  157 LYS   T C   
35128 O  O   . LYS   T  161 ? 2.0137 0.5238 1.4721 -0.0068 -0.6097 0.2451  157 LYS   T O   
35129 C  CB  . LYS   T  161 ? 2.0941 0.6671 1.4259 -0.0690 -0.5729 0.2481  157 LYS   T CB  
35130 C  CG  . LYS   T  161 ? 2.1309 0.7564 1.3828 -0.1093 -0.5366 0.2627  157 LYS   T CG  
35131 C  CD  . LYS   T  161 ? 2.1814 0.8159 1.3705 -0.1472 -0.5430 0.2856  157 LYS   T CD  
35132 C  CE  . LYS   T  161 ? 2.2109 0.8814 1.3067 -0.1853 -0.5189 0.2961  157 LYS   T CE  
35133 N  NZ  . LYS   T  161 ? 2.2566 0.9536 1.2640 -0.2185 -0.5151 0.3273  157 LYS   T NZ  
35134 N  N   . GLY   T  162 ? 2.0027 0.5293 1.4399 -0.0045 -0.6156 0.2816  158 GLY   T N   
35135 C  CA  . GLY   T  162 ? 1.9984 0.5800 1.4460 0.0056  -0.6070 0.3259  158 GLY   T CA  
35136 C  C   . GLY   T  162 ? 2.0140 0.5683 1.4376 0.0166  -0.5849 0.3208  158 GLY   T C   
35137 O  O   . GLY   T  162 ? 2.0578 0.5367 1.4596 -0.0321 -0.5368 0.3433  158 GLY   T O   
35138 N  N   . ALA   T  163 ? 1.9878 0.5708 1.4495 0.0646  -0.5784 0.2930  159 ALA   T N   
35139 C  CA  . ALA   T  163 ? 1.9631 0.5308 1.4698 0.1199  -0.5982 0.2614  159 ALA   T CA  
35140 C  C   . ALA   T  163 ? 1.9631 0.5117 1.5062 0.1429  -0.6121 0.2430  159 ALA   T C   
35141 O  O   . ALA   T  163 ? 1.9630 0.4418 1.5554 0.1359  -0.5789 0.2483  159 ALA   T O   
35142 C  CB  . ALA   T  163 ? 1.9477 0.5286 1.4324 0.1180  -0.5977 0.2457  159 ALA   T CB  
35143 N  N   . ALA   T  164 ? 1.9533 0.5215 1.5071 0.1789  -0.6136 0.2311  160 ALA   T N   
35144 C  CA  . ALA   T  164 ? 1.9476 0.5435 1.5585 0.1958  -0.5975 0.2478  160 ALA   T CA  
35145 C  C   . ALA   T  164 ? 1.9500 0.5290 1.5701 0.1865  -0.5628 0.2071  160 ALA   T C   
35146 O  O   . ALA   T  164 ? 1.9398 0.5175 1.6185 0.2025  -0.5506 0.2117  160 ALA   T O   
35147 C  CB  . ALA   T  164 ? 1.9541 0.5810 1.5718 0.2081  -0.6320 0.2586  160 ALA   T CB  
35148 N  N   . THR   T  165 ? 1.9592 0.5107 1.5903 0.1661  -0.5459 0.1964  161 THR   T N   
35149 C  CA  . THR   T  165 ? 1.9584 0.5278 1.5802 0.1539  -0.5328 0.1939  161 THR   T CA  
35150 C  C   . THR   T  165 ? 1.9531 0.4781 1.5849 0.1684  -0.5383 0.2026  161 THR   T C   
35151 O  O   . THR   T  165 ? 1.9432 0.3820 1.5927 0.1762  -0.5138 0.2427  161 THR   T O   
35152 C  CB  . THR   T  165 ? 1.9477 0.5343 1.5128 0.1260  -0.5392 0.1824  161 THR   T CB  
35153 O  OG1 . THR   T  165 ? 2.0510 0.6014 1.5031 0.1113  -0.5027 0.1395  161 THR   T OG1 
35154 C  CG2 . THR   T  165 ? 1.9216 0.5759 1.5213 0.0940  -0.5248 0.1602  161 THR   T CG2 
35155 N  N   . GLY   T  166 ? 1.9380 0.5260 1.5916 0.1786  -0.5274 0.1741  162 GLY   T N   
35156 C  CA  . GLY   T  166 ? 1.9459 0.6284 1.6387 0.1661  -0.5060 0.1194  162 GLY   T CA  
35157 C  C   . GLY   T  166 ? 1.9644 0.6305 1.7282 0.1955  -0.4964 0.0874  162 GLY   T C   
35158 O  O   . GLY   T  166 ? 2.0161 0.5845 1.7630 0.1833  -0.4766 0.0880  162 GLY   T O   
35159 N  N   . LYS   T  167 ? 1.9722 0.6976 1.7792 0.2298  -0.5077 0.0732  163 LYS   T N   
35160 C  CA  . LYS   T  167 ? 1.9745 0.7250 1.8531 0.2933  -0.4933 0.0890  163 LYS   T CA  
35161 C  C   . LYS   T  167 ? 2.0293 0.7043 1.8440 0.3110  -0.5050 0.0576  163 LYS   T C   
35162 O  O   . LYS   T  167 ? 1.9993 0.7035 1.9478 0.3016  -0.5021 0.0307  163 LYS   T O   
35163 C  CB  . LYS   T  167 ? 1.9808 0.8801 1.8871 0.3102  -0.4660 0.1464  163 LYS   T CB  
35164 C  CG  . LYS   T  167 ? 2.0142 0.9120 1.9266 0.2976  -0.4288 0.1201  163 LYS   T CG  
35165 C  CD  . LYS   T  167 ? 2.0171 1.0104 1.9349 0.2863  -0.3968 0.1440  163 LYS   T CD  
35166 C  CE  . LYS   T  167 ? 2.0339 1.1041 1.9576 0.2848  -0.3556 0.1659  163 LYS   T CE  
35167 N  NZ  . LYS   T  167 ? 2.0499 1.1527 1.9620 0.2899  -0.3322 0.1622  163 LYS   T NZ  
35168 N  N   . GLY   T  168 ? 2.1033 0.6271 1.9104 0.2978  -0.5017 0.0490  164 GLY   T N   
35169 C  CA  . GLY   T  168 ? 2.1384 0.6209 1.9208 0.2931  -0.5309 0.0483  164 GLY   T CA  
35170 C  C   . GLY   T  168 ? 2.1812 0.5121 1.8656 0.2474  -0.5228 0.0327  164 GLY   T C   
35171 O  O   . GLY   T  168 ? 2.1625 0.3360 1.9077 0.2299  -0.5403 -0.0177 164 GLY   T O   
35172 N  N   . ARG   T  169 ? 2.1783 0.4820 1.8494 0.2164  -0.5059 0.0925  165 ARG   T N   
35173 C  CA  . ARG   T  169 ? 2.1942 0.4685 1.7670 0.2181  -0.4892 0.1640  165 ARG   T CA  
35174 C  C   . ARG   T  169 ? 2.2231 0.6118 1.7754 0.1777  -0.4799 0.2005  165 ARG   T C   
35175 O  O   . ARG   T  169 ? 2.2466 0.3768 1.7894 0.0875  -0.4851 0.2244  165 ARG   T O   
35176 C  CB  . ARG   T  169 ? 2.2437 0.4587 1.6930 0.2446  -0.4672 0.2378  165 ARG   T CB  
35177 C  CG  . ARG   T  169 ? 2.2548 0.4610 1.6590 0.2402  -0.4659 0.2974  165 ARG   T CG  
35178 C  CD  . ARG   T  169 ? 2.2853 0.4858 1.6124 0.2872  -0.4272 0.3584  165 ARG   T CD  
35179 N  NE  . ARG   T  169 ? 2.3063 0.5076 1.5978 0.3204  -0.4195 0.3981  165 ARG   T NE  
35180 C  CZ  . ARG   T  169 ? 2.3159 0.5570 1.5600 0.2998  -0.4039 0.3669  165 ARG   T CZ  
35181 N  NH1 . ARG   T  169 ? 2.3342 0.5834 1.6043 0.2705  -0.3910 0.3610  165 ARG   T NH1 
35182 N  NH2 . ARG   T  169 ? 2.3517 0.6790 1.5448 0.3177  -0.3940 0.3805  165 ARG   T NH2 
35183 N  N   . GLN   T  170 ? 2.2190 0.6137 1.8450 0.2337  -0.4788 0.2052  166 GLN   T N   
35184 C  CA  . GLN   T  170 ? 2.1744 0.6877 1.8655 0.2486  -0.4848 0.2506  166 GLN   T CA  
35185 C  C   . GLN   T  170 ? 2.1636 0.6671 1.9205 0.3365  -0.5240 0.3085  166 GLN   T C   
35186 O  O   . GLN   T  170 ? 2.1485 0.5567 1.9055 0.3847  -0.5308 0.4003  166 GLN   T O   
35187 C  CB  . GLN   T  170 ? 2.1970 0.7800 1.9672 0.1521  -0.3861 0.1400  166 GLN   T CB  
35188 C  CG  . GLN   T  170 ? 2.1361 0.9713 2.0018 0.0854  -0.3422 0.1317  166 GLN   T CG  
35189 C  CD  . GLN   T  170 ? 2.2384 1.0918 2.1083 0.0036  -0.2509 0.0034  166 GLN   T CD  
35190 O  OE1 . GLN   T  170 ? 2.2249 1.3400 2.2344 -0.0548 -0.1482 -0.0238 166 GLN   T OE1 
35191 N  NE2 . GLN   T  170 ? 2.2271 1.2892 2.1399 -0.0188 -0.1813 0.0186  166 GLN   T NE2 
35192 N  N   . SER   T  171 ? 2.1186 0.7459 1.9005 0.3817  -0.6322 0.3116  167 SER   T N   
35193 C  CA  . SER   T  171 ? 2.1151 0.8593 1.9250 0.3798  -0.6566 0.3270  167 SER   T CA  
35194 C  C   . SER   T  171 ? 2.0879 0.8190 1.8279 0.3778  -0.7260 0.3813  167 SER   T C   
35195 O  O   . SER   T  171 ? 2.0960 0.8131 1.8282 0.4266  -0.7701 0.4122  167 SER   T O   
35196 C  CB  . SER   T  171 ? 2.0747 0.9697 1.9521 0.3894  -0.6837 0.2897  167 SER   T CB  
35197 O  OG  . SER   T  171 ? 2.0021 1.1301 2.0410 0.3761  -0.6572 0.2302  167 SER   T OG  
35198 N  N   . ALA   T  172 ? 2.0681 0.8023 1.7749 0.2930  -0.6902 0.3692  168 ALA   T N   
35199 C  CA  . ALA   T  172 ? 2.0300 0.8153 1.7058 0.2476  -0.6865 0.3588  168 ALA   T CA  
35200 C  C   . ALA   T  172 ? 2.0546 0.7913 1.6578 0.2052  -0.6728 0.3555  168 ALA   T C   
35201 O  O   . ALA   T  172 ? 2.0175 0.8241 1.6440 0.1646  -0.6534 0.3579  168 ALA   T O   
35202 C  CB  . ALA   T  172 ? 1.9914 0.8314 1.6888 0.2758  -0.6921 0.3556  168 ALA   T CB  
35203 N  N   . LYS   T  173 ? 2.0768 0.7851 1.6799 0.1821  -0.6526 0.3182  169 LYS   T N   
35204 C  CA  . LYS   T  173 ? 2.1105 0.8432 1.7305 0.1826  -0.6161 0.2565  169 LYS   T CA  
35205 C  C   . LYS   T  173 ? 2.1640 0.9113 1.7349 0.1500  -0.6218 0.2665  169 LYS   T C   
35206 O  O   . LYS   T  173 ? 2.2223 0.9013 1.8544 0.2021  -0.5740 0.2231  169 LYS   T O   
35207 C  CB  . LYS   T  173 ? 2.1352 0.8025 1.7227 0.1728  -0.6169 0.2676  169 LYS   T CB  
35208 C  CG  . LYS   T  173 ? 2.1186 0.7861 1.7058 0.1626  -0.6101 0.2587  169 LYS   T CG  
35209 C  CD  . LYS   T  173 ? 2.1336 0.8206 1.7070 0.1349  -0.6110 0.2607  169 LYS   T CD  
35210 C  CE  . LYS   T  173 ? 2.1670 0.8434 1.6885 0.1077  -0.5797 0.2953  169 LYS   T CE  
35211 N  NZ  . LYS   T  173 ? 2.1826 0.8462 1.7102 0.1303  -0.5558 0.3067  169 LYS   T NZ  
35212 N  N   . ALA   T  174 ? 2.1339 0.9264 1.8916 0.1542  -0.6227 0.2235  170 ALA   T N   
35213 C  CA  . ALA   T  174 ? 2.1311 1.0566 1.8928 0.1056  -0.6598 0.2443  170 ALA   T CA  
35214 C  C   . ALA   T  174 ? 2.1080 1.1295 1.9391 0.0748  -0.6831 0.2394  170 ALA   T C   
35215 O  O   . ALA   T  174 ? 2.0479 1.3093 1.9091 0.0045  -0.7413 0.2755  170 ALA   T O   
35216 C  CB  . ALA   T  174 ? 2.1408 1.0752 1.9884 0.1083  -0.6392 0.2059  170 ALA   T CB  
35217 N  N   . GLU   T  175 ? 2.1239 1.0343 1.9984 0.0818  -0.6946 0.2415  171 GLU   T N   
35218 C  CA  . GLU   T  175 ? 2.1873 0.9258 2.0463 0.0942  -0.7064 0.2316  171 GLU   T CA  
35219 C  C   . GLU   T  175 ? 2.1928 0.8664 1.9785 0.0593  -0.6952 0.2568  171 GLU   T C   
35220 O  O   . GLU   T  175 ? 2.1850 0.6635 1.9355 0.1323  -0.6703 0.3248  171 GLU   T O   
35221 C  CB  . GLU   T  175 ? 2.2045 0.9537 2.1212 0.0652  -0.6843 0.2211  171 GLU   T CB  
35222 C  CG  . GLU   T  175 ? 2.2299 1.1031 2.2139 0.0511  -0.7266 0.1762  171 GLU   T CG  
35223 C  CD  . GLU   T  175 ? 2.3375 1.0908 2.3253 0.0776  -0.7345 0.1663  171 GLU   T CD  
35224 O  OE1 . GLU   T  175 ? 2.3920 1.0853 2.4343 0.1260  -0.7445 0.1120  171 GLU   T OE1 
35225 O  OE2 . GLU   T  175 ? 2.4776 1.3225 2.3394 0.0266  -0.7644 0.0031  171 GLU   T OE2 
35226 N  N   . LEU   T  176 ? 2.1478 0.9347 1.8964 0.0407  -0.7077 0.1836  172 LEU   T N   
35227 C  CA  . LEU   T  176 ? 2.1676 0.9810 1.8162 0.0483  -0.6700 0.1577  172 LEU   T CA  
35228 C  C   . LEU   T  176 ? 2.2231 0.9998 1.7873 0.0064  -0.6884 0.2016  172 LEU   T C   
35229 O  O   . LEU   T  176 ? 2.2592 1.0827 1.7085 0.0598  -0.6634 0.2324  172 LEU   T O   
35230 C  CB  . LEU   T  176 ? 2.1844 0.9583 1.7612 0.0328  -0.6402 0.1409  172 LEU   T CB  
35231 C  CG  . LEU   T  176 ? 2.1749 0.9520 1.7332 -0.0031 -0.5971 0.0792  172 LEU   T CG  
35232 C  CD1 . LEU   T  176 ? 2.1718 0.9004 1.7406 0.0042  -0.6081 0.0864  172 LEU   T CD1 
35233 C  CD2 . LEU   T  176 ? 2.1990 1.0140 1.7180 0.0027  -0.5628 0.0337  172 LEU   T CD2 
35234 N  N   . GLU   T  177 ? 2.2939 0.9420 1.7332 0.0237  -0.6705 0.2204  173 GLU   T N   
35235 C  CA  . GLU   T  177 ? 2.3544 0.9252 1.7766 0.0073  -0.6387 0.2545  173 GLU   T CA  
35236 C  C   . GLU   T  177 ? 2.3331 0.8349 1.8178 -0.0009 -0.6774 0.2310  173 GLU   T C   
35237 O  O   . GLU   T  177 ? 2.4417 0.8397 1.8421 -0.0768 -0.5998 0.2303  173 GLU   T O   
35238 C  CB  . GLU   T  177 ? 2.3685 0.9504 1.8134 -0.0359 -0.6107 0.2689  173 GLU   T CB  
35239 C  CG  . GLU   T  177 ? 2.3611 1.0878 1.8079 0.0074  -0.5819 0.3063  173 GLU   T CG  
35240 C  CD  . GLU   T  177 ? 2.3831 1.2143 1.8524 -0.0285 -0.5815 0.1832  173 GLU   T CD  
35241 O  OE1 . GLU   T  177 ? 2.3961 1.3492 1.8567 0.0362  -0.5381 0.1266  173 GLU   T OE1 
35242 O  OE2 . GLU   T  177 ? 2.3872 1.3918 1.9286 -0.0546 -0.5288 0.2506  173 GLU   T OE2 
35243 N  N   . LYS   T  178 ? 2.3475 0.8301 1.9422 0.0414  -0.6741 0.2051  174 LYS   T N   
35244 C  CA  . LYS   T  178 ? 2.2932 0.9840 2.0147 0.0928  -0.7075 0.2578  174 LYS   T CA  
35245 C  C   . LYS   T  178 ? 2.2803 0.9842 1.9531 0.1495  -0.7344 0.2709  174 LYS   T C   
35246 O  O   . LYS   T  178 ? 2.2645 1.0235 1.9190 0.1797  -0.7826 0.3644  174 LYS   T O   
35247 C  CB  . LYS   T  178 ? 2.2477 1.0860 2.0973 0.0668  -0.6997 0.2048  174 LYS   T CB  
35248 C  CG  . LYS   T  178 ? 2.2635 1.0910 2.1809 0.0925  -0.6931 0.2342  174 LYS   T CG  
35249 C  CD  . LYS   T  178 ? 2.2430 1.2114 2.2634 0.1460  -0.6686 0.2424  174 LYS   T CD  
35250 C  CE  . LYS   T  178 ? 2.2636 1.2201 2.3551 0.1409  -0.6676 0.2417  174 LYS   T CE  
35251 N  NZ  . LYS   T  178 ? 2.2527 1.3052 2.4372 0.1657  -0.6291 0.2270  174 LYS   T NZ  
35252 N  N   . LEU   T  179 ? 2.2654 1.0139 1.9294 0.2126  -0.7048 0.3027  175 LEU   T N   
35253 C  CA  . LEU   T  179 ? 2.2533 1.0009 1.8797 0.2653  -0.6863 0.3096  175 LEU   T CA  
35254 C  C   . LEU   T  179 ? 2.3186 0.9139 1.8544 0.2908  -0.6360 0.3594  175 LEU   T C   
35255 O  O   . LEU   T  179 ? 2.3994 0.9824 1.7701 0.3367  -0.6804 0.4252  175 LEU   T O   
35256 C  CB  . LEU   T  179 ? 2.1198 1.0530 1.8344 0.3130  -0.6667 0.2908  175 LEU   T CB  
35257 C  CG  . LEU   T  179 ? 2.1078 1.1461 1.8437 0.3301  -0.6871 0.2824  175 LEU   T CG  
35258 C  CD1 . LEU   T  179 ? 2.0545 1.1241 1.8281 0.3742  -0.6837 0.2800  175 LEU   T CD1 
35259 C  CD2 . LEU   T  179 ? 2.1135 1.2440 1.8693 0.3049  -0.6978 0.2632  175 LEU   T CD2 
35260 N  N   . VAL   T  180 ? 2.3277 0.7938 1.8161 0.2633  -0.6044 0.3376  176 VAL   T N   
35261 C  CA  . VAL   T  180 ? 2.3484 0.8664 1.8076 0.2380  -0.5247 0.3329  176 VAL   T CA  
35262 C  C   . VAL   T  180 ? 2.4025 0.8720 1.8291 0.2187  -0.5157 0.3526  176 VAL   T C   
35263 O  O   . VAL   T  180 ? 2.3302 0.8074 1.8022 0.2784  -0.5141 0.4513  176 VAL   T O   
35264 C  CB  . VAL   T  180 ? 2.3410 0.8894 1.7784 0.2205  -0.4893 0.3041  176 VAL   T CB  
35265 C  CG1 . VAL   T  180 ? 2.3428 0.9530 1.7591 0.1941  -0.4694 0.2824  176 VAL   T CG1 
35266 C  CG2 . VAL   T  180 ? 2.3293 0.8900 1.7911 0.2219  -0.4566 0.3045  176 VAL   T CG2 
35267 N  N   . ASP   T  181 ? 2.5310 0.8510 1.9031 0.1846  -0.4930 0.3445  177 ASP   T N   
35268 C  CA  . ASP   T  181 ? 2.6431 1.0147 1.8533 0.1652  -0.5121 0.3638  177 ASP   T CA  
35269 C  C   . ASP   T  181 ? 2.6783 1.0773 1.7713 0.1887  -0.5540 0.4854  177 ASP   T C   
35270 O  O   . ASP   T  181 ? 2.6659 1.0937 1.7517 0.2005  -0.5551 0.5524  177 ASP   T O   
35271 C  CB  . ASP   T  181 ? 2.7914 1.0430 2.0391 0.1884  -0.4556 0.2783  177 ASP   T CB  
35272 C  CG  . ASP   T  181 ? 2.8946 0.9401 2.1608 0.1476  -0.4107 0.1051  177 ASP   T CG  
35273 O  OD1 . ASP   T  181 ? 3.0104 0.7714 2.3071 0.2429  -0.3038 -0.0085 177 ASP   T OD1 
35274 O  OD2 . ASP   T  181 ? 3.0630 1.0980 2.2572 0.1034  -0.3526 -0.0531 177 ASP   T OD2 
35275 N  N   . HIS   T  182 ? 2.6655 1.1523 1.6886 0.2029  -0.6147 0.5635  178 HIS   T N   
35276 C  CA  . HIS   T  182 ? 2.7327 1.3304 1.6889 0.2021  -0.6601 0.5530  178 HIS   T CA  
35277 C  C   . HIS   T  182 ? 2.6949 1.3572 1.5113 0.1750  -0.7100 0.5350  178 HIS   T C   
35278 O  O   . HIS   T  182 ? 2.7714 1.4732 1.5128 0.2247  -0.7985 0.6145  178 HIS   T O   
35279 C  CB  . HIS   T  182 ? 2.7220 1.4896 1.7651 0.2126  -0.6652 0.5365  178 HIS   T CB  
35280 C  CG  . HIS   T  182 ? 2.8179 1.4983 1.9603 0.1884  -0.6520 0.5387  178 HIS   T CG  
35281 N  ND1 . HIS   T  182 ? 2.8513 1.6376 2.0389 0.1978  -0.5891 0.5297  178 HIS   T ND1 
35282 C  CD2 . HIS   T  182 ? 2.8514 1.5638 1.9698 0.1606  -0.6465 0.5827  178 HIS   T CD2 
35283 C  CE1 . HIS   T  182 ? 2.8713 1.6336 2.0981 0.1183  -0.6042 0.5449  178 HIS   T CE1 
35284 N  NE2 . HIS   T  182 ? 2.9117 1.4396 2.0342 0.0741  -0.6510 0.6094  178 HIS   T NE2 
35285 N  N   . HIS   T  183 ? 2.6165 1.3186 1.5822 0.2385  -0.6619 0.4905  179 HIS   T N   
35286 C  CA  . HIS   T  183 ? 2.5524 1.3418 1.6450 0.2346  -0.6054 0.4081  179 HIS   T CA  
35287 C  C   . HIS   T  183 ? 2.5414 1.3605 1.7180 0.2396  -0.5824 0.3645  179 HIS   T C   
35288 O  O   . HIS   T  183 ? 2.5275 1.4209 1.6692 0.2274  -0.5160 0.3801  179 HIS   T O   
35289 C  CB  . HIS   T  183 ? 2.5452 1.2350 1.6765 0.2416  -0.5736 0.3488  179 HIS   T CB  
35290 C  CG  . HIS   T  183 ? 2.5546 1.1792 1.7073 0.2520  -0.5242 0.3205  179 HIS   T CG  
35291 N  ND1 . HIS   T  183 ? 2.5793 1.0935 1.6471 0.2548  -0.5001 0.3294  179 HIS   T ND1 
35292 C  CD2 . HIS   T  183 ? 2.5446 1.2304 1.7688 0.2647  -0.4992 0.2955  179 HIS   T CD2 
35293 C  CE1 . HIS   T  183 ? 2.5699 1.1713 1.6665 0.2828  -0.5210 0.3612  179 HIS   T CE1 
35294 N  NE2 . HIS   T  183 ? 2.5497 1.2363 1.7234 0.3075  -0.4903 0.2957  179 HIS   T NE2 
35295 N  N   . PRO   T  184 ? 2.4887 1.3265 1.7094 0.2407  -0.6252 0.3892  180 PRO   T N   
35296 C  CA  . PRO   T  184 ? 2.4595 1.2899 1.7359 0.2003  -0.6128 0.3369  180 PRO   T CA  
35297 C  C   . PRO   T  184 ? 2.3889 1.2785 1.7376 0.1694  -0.6300 0.3353  180 PRO   T C   
35298 O  O   . PRO   T  184 ? 2.4126 0.8842 1.7356 0.1347  -0.5420 0.3470  180 PRO   T O   
35299 C  CB  . PRO   T  184 ? 2.4619 1.2940 1.6946 0.2232  -0.6514 0.3665  180 PRO   T CB  
35300 C  CG  . PRO   T  184 ? 2.4995 1.3219 1.7013 0.2242  -0.6726 0.3833  180 PRO   T CG  
35301 C  CD  . PRO   T  184 ? 2.4874 1.3480 1.7179 0.2369  -0.6791 0.3940  180 PRO   T CD  
35302 N  N   . GLU   T  185 ? 2.4192 1.3533 1.7663 0.1381  -0.6434 0.3066  181 GLU   T N   
35303 C  CA  . GLU   T  185 ? 2.3851 1.3867 1.7676 0.1535  -0.6808 0.2579  181 GLU   T CA  
35304 C  C   . GLU   T  185 ? 2.3725 1.5254 1.7637 0.1246  -0.5940 0.2208  181 GLU   T C   
35305 O  O   . GLU   T  185 ? 2.4389 1.5708 1.8937 0.1785  -0.5687 0.2195  181 GLU   T O   
35306 C  CB  . GLU   T  185 ? 2.3806 1.5163 1.7939 0.1165  -0.7126 0.2737  181 GLU   T CB  
35307 C  CG  . GLU   T  185 ? 2.3643 1.5796 1.8312 0.1139  -0.7755 0.2867  181 GLU   T CG  
35308 C  CD  . GLU   T  185 ? 2.3438 1.6502 1.8781 0.1288  -0.7902 0.2551  181 GLU   T CD  
35309 O  OE1 . GLU   T  185 ? 2.3907 1.6005 1.9981 0.0534  -0.8088 0.2772  181 GLU   T OE1 
35310 O  OE2 . GLU   T  185 ? 2.3360 1.6624 1.7581 0.1547  -0.8490 0.2763  181 GLU   T OE2 
35311 N  N   . GLY   T  186 ? 2.3007 1.3943 1.6925 0.1403  -0.6808 0.2503  182 GLY   T N   
35312 C  CA  . GLY   T  186 ? 2.1853 1.3543 1.6316 0.1284  -0.7063 0.1962  182 GLY   T CA  
35313 C  C   . GLY   T  186 ? 2.1708 1.3029 1.5785 0.1047  -0.7406 0.2258  182 GLY   T C   
35314 O  O   . GLY   T  186 ? 2.1679 1.2139 1.6697 0.1045  -0.7736 0.3022  182 GLY   T O   
35315 N  N   . LEU   T  187 ? 2.1170 1.3486 1.5527 0.1081  -0.7681 0.1871  183 LEU   T N   
35316 C  CA  . LEU   T  187 ? 2.1043 1.3984 1.5886 0.1131  -0.7806 0.1838  183 LEU   T CA  
35317 C  C   . LEU   T  187 ? 2.0518 1.4255 1.5549 0.0370  -0.7433 0.0898  183 LEU   T C   
35318 O  O   . LEU   T  187 ? 2.0495 1.3062 1.6076 0.0232  -0.7220 0.0602  183 LEU   T O   
35319 C  CB  . LEU   T  187 ? 2.0953 1.3770 1.6203 0.2047  -0.7330 0.1918  183 LEU   T CB  
35320 C  CG  . LEU   T  187 ? 2.0980 1.4554 1.6552 0.2521  -0.7514 0.2475  183 LEU   T CG  
35321 C  CD1 . LEU   T  187 ? 2.1157 1.5356 1.6639 0.2734  -0.7676 0.2704  183 LEU   T CD1 
35322 C  CD2 . LEU   T  187 ? 2.0855 1.4743 1.6405 0.2757  -0.7055 0.2564  183 LEU   T CD2 
35323 N  N   . SER   T  188 ? 2.0262 1.4277 1.5671 0.0027  -0.6891 0.1022  184 SER   T N   
35324 C  CA  . SER   T  188 ? 1.9854 1.4265 1.5518 -0.0023 -0.6580 0.0892  184 SER   T CA  
35325 C  C   . SER   T  188 ? 2.0246 1.3660 1.5925 -0.0209 -0.6029 0.1047  184 SER   T C   
35326 O  O   . SER   T  188 ? 2.0221 1.3995 1.5640 0.0363  -0.5944 0.1247  184 SER   T O   
35327 C  CB  . SER   T  188 ? 1.9106 1.4195 1.6073 -0.0306 -0.6461 0.0938  184 SER   T CB  
35328 O  OG  . SER   T  188 ? 1.8037 1.5025 1.6418 -0.0808 -0.7140 0.0464  184 SER   T OG  
35329 N  N   . ALA   T  189 ? 2.0827 1.3336 1.6320 -0.0826 -0.5676 0.0677  185 ALA   T N   
35330 C  CA  . ALA   T  189 ? 2.0946 1.3251 1.6288 -0.0666 -0.5592 0.0355  185 ALA   T CA  
35331 C  C   . ALA   T  189 ? 2.0853 1.3073 1.6827 -0.0711 -0.5901 0.0308  185 ALA   T C   
35332 O  O   . ALA   T  189 ? 2.0584 1.2806 1.6837 -0.0960 -0.6457 0.0202  185 ALA   T O   
35333 C  CB  . ALA   T  189 ? 2.1097 1.3219 1.6506 -0.0452 -0.5466 0.0250  185 ALA   T CB  
35334 N  N   . ARG   T  190 ? 2.1084 1.3091 1.6851 -0.0844 -0.6073 0.0645  186 ARG   T N   
35335 C  CA  . ARG   T  190 ? 2.1215 1.2436 1.6966 -0.0750 -0.6318 0.1068  186 ARG   T CA  
35336 C  C   . ARG   T  190 ? 2.1310 1.2464 1.6926 -0.0546 -0.6699 0.1505  186 ARG   T C   
35337 O  O   . ARG   T  190 ? 2.1159 1.1160 1.7209 -0.0514 -0.6712 0.2044  186 ARG   T O   
35338 C  CB  . ARG   T  190 ? 2.1382 1.3668 1.7000 -0.0974 -0.6536 0.1024  186 ARG   T CB  
35339 C  CG  . ARG   T  190 ? 2.1757 1.3725 1.7736 -0.1311 -0.6012 0.0666  186 ARG   T CG  
35340 C  CD  . ARG   T  190 ? 2.1880 1.4382 1.8199 -0.1672 -0.6057 0.0472  186 ARG   T CD  
35341 N  NE  . ARG   T  190 ? 2.1741 1.5083 1.8747 -0.1920 -0.5407 0.0519  186 ARG   T NE  
35342 C  CZ  . ARG   T  190 ? 2.1641 1.4826 1.9036 -0.1765 -0.5374 0.0488  186 ARG   T CZ  
35343 N  NH1 . ARG   T  190 ? 2.1315 1.4483 1.9167 -0.1848 -0.5371 0.1069  186 ARG   T NH1 
35344 N  NH2 . ARG   T  190 ? 2.1337 1.5265 1.8912 -0.2190 -0.5200 0.0156  186 ARG   T NH2 
35345 N  N   . GLU   T  191 ? 2.1182 1.1962 1.6793 -0.0452 -0.7029 0.1641  187 GLU   T N   
35346 C  CA  . GLU   T  191 ? 2.1268 1.1770 1.7675 0.0238  -0.7559 0.1670  187 GLU   T CA  
35347 C  C   . GLU   T  191 ? 2.0814 1.0676 1.7684 0.0176  -0.7417 0.1892  187 GLU   T C   
35348 O  O   . GLU   T  191 ? 2.0827 1.0214 1.7940 -0.0142 -0.7281 0.2098  187 GLU   T O   
35349 C  CB  . GLU   T  191 ? 2.1283 1.1795 1.8144 0.0161  -0.7435 0.1737  187 GLU   T CB  
35350 C  CG  . GLU   T  191 ? 2.1716 1.3582 1.8561 -0.0081 -0.8138 0.1553  187 GLU   T CG  
35351 C  CD  . GLU   T  191 ? 2.2054 1.4081 2.0303 0.0478  -0.8197 0.1281  187 GLU   T CD  
35352 O  OE1 . GLU   T  191 ? 2.2083 1.4814 2.0476 0.0188  -0.8738 0.0844  187 GLU   T OE1 
35353 O  OE2 . GLU   T  191 ? 2.2312 1.5178 2.1629 0.1069  -0.8728 0.1481  187 GLU   T OE2 
35354 N  N   . ALA   T  192 ? 2.0442 1.0206 1.7175 0.0073  -0.7263 0.1404  188 ALA   T N   
35355 C  CA  . ALA   T  192 ? 2.0138 0.9455 1.7229 0.0027  -0.7129 0.1382  188 ALA   T CA  
35356 C  C   . ALA   T  192 ? 1.9795 0.9105 1.7151 0.0558  -0.7343 0.1277  188 ALA   T C   
35357 O  O   . ALA   T  192 ? 1.9822 0.7664 1.7912 0.0433  -0.7419 0.1709  188 ALA   T O   
35358 C  CB  . ALA   T  192 ? 1.9685 0.9566 1.6884 -0.0175 -0.6773 0.1145  188 ALA   T CB  
35359 N  N   . VAL   T  193 ? 1.9137 0.9860 1.6836 0.0489  -0.7507 0.1342  189 VAL   T N   
35360 C  CA  . VAL   T  193 ? 1.8999 1.0246 1.6831 0.0584  -0.7557 0.1078  189 VAL   T CA  
35361 C  C   . VAL   T  193 ? 1.9260 1.0883 1.6672 0.1059  -0.7717 0.1366  189 VAL   T C   
35362 O  O   . VAL   T  193 ? 1.9168 1.0627 1.7107 0.0916  -0.7621 0.1037  189 VAL   T O   
35363 C  CB  . VAL   T  193 ? 1.8909 1.0455 1.6756 0.0494  -0.7717 0.0529  189 VAL   T CB  
35364 C  CG1 . VAL   T  193 ? 1.8780 0.9984 1.6939 0.0508  -0.7767 0.0271  189 VAL   T CG1 
35365 C  CG2 . VAL   T  193 ? 1.8349 1.0535 1.6559 0.0441  -0.7652 0.0325  189 VAL   T CG2 
35366 N  N   . LYS   T  194 ? 1.9647 1.1910 1.6637 0.1205  -0.7776 0.1512  190 LYS   T N   
35367 C  CA  . LYS   T  194 ? 1.9908 1.2024 1.6412 0.1322  -0.7982 0.1686  190 LYS   T CA  
35368 C  C   . LYS   T  194 ? 1.9523 1.1487 1.5994 0.1770  -0.8057 0.1955  190 LYS   T C   
35369 O  O   . LYS   T  194 ? 1.8880 1.1484 1.5858 0.1963  -0.8359 0.2187  190 LYS   T O   
35370 C  CB  . LYS   T  194 ? 2.0456 1.2845 1.6568 0.1313  -0.8296 0.1900  190 LYS   T CB  
35371 C  CG  . LYS   T  194 ? 2.0492 1.3702 1.6554 0.0892  -0.8510 0.1753  190 LYS   T CG  
35372 C  CD  . LYS   T  194 ? 2.0858 1.4436 1.6567 0.0654  -0.8400 0.1675  190 LYS   T CD  
35373 C  CE  . LYS   T  194 ? 2.0947 1.4654 1.6819 0.0881  -0.8378 0.1743  190 LYS   T CE  
35374 N  NZ  . LYS   T  194 ? 2.1192 1.4889 1.6550 0.0727  -0.8487 0.2111  190 LYS   T NZ  
35375 N  N   . GLN   T  195 ? 1.9809 1.0846 1.5787 0.1480  -0.7797 0.2014  191 GLN   T N   
35376 C  CA  . GLN   T  195 ? 2.0731 1.0043 1.6561 0.1537  -0.7468 0.2043  191 GLN   T CA  
35377 C  C   . GLN   T  195 ? 2.0734 0.9694 1.6644 0.1512  -0.7122 0.1573  191 GLN   T C   
35378 O  O   . GLN   T  195 ? 2.0766 0.9461 1.6913 0.1533  -0.7240 0.1808  191 GLN   T O   
35379 C  CB  . GLN   T  195 ? 2.0921 0.9655 1.6345 0.1215  -0.7307 0.2053  191 GLN   T CB  
35380 C  CG  . GLN   T  195 ? 2.1338 0.9934 1.6409 0.0887  -0.7221 0.2205  191 GLN   T CG  
35381 C  CD  . GLN   T  195 ? 2.1254 0.9670 1.7774 0.0949  -0.7198 0.1939  191 GLN   T CD  
35382 O  OE1 . GLN   T  195 ? 2.0616 0.9772 1.8659 0.0766  -0.7264 0.2471  191 GLN   T OE1 
35383 N  NE2 . GLN   T  195 ? 2.1549 0.9807 1.8079 0.1121  -0.7028 0.1444  191 GLN   T NE2 
35384 N  N   . ALA   T  196 ? 2.0944 0.9895 1.6842 0.1686  -0.6725 0.1783  192 ALA   T N   
35385 C  CA  . ALA   T  196 ? 2.0817 0.9935 1.6838 0.1831  -0.6427 0.1527  192 ALA   T CA  
35386 C  C   . ALA   T  196 ? 2.0584 0.9234 1.7833 0.2066  -0.6655 0.1804  192 ALA   T C   
35387 O  O   . ALA   T  196 ? 2.0671 0.8744 1.8125 0.2426  -0.6515 0.1821  192 ALA   T O   
35388 C  CB  . ALA   T  196 ? 2.0704 1.0101 1.6862 0.1862  -0.6106 0.1667  192 ALA   T CB  
35389 N  N   . ALA   T  197 ? 2.0646 0.9601 1.8066 0.2097  -0.6937 0.1882  193 ALA   T N   
35390 C  CA  . ALA   T  197 ? 2.0604 1.0094 1.8625 0.2033  -0.6838 0.1844  193 ALA   T CA  
35391 C  C   . ALA   T  197 ? 2.1165 1.0333 1.8885 0.1896  -0.6957 0.2522  193 ALA   T C   
35392 O  O   . ALA   T  197 ? 2.1357 1.0042 1.9341 0.2689  -0.6900 0.2793  193 ALA   T O   
35393 C  CB  . ALA   T  197 ? 2.0711 1.0860 1.8797 0.1866  -0.7010 0.1817  193 ALA   T CB  
35394 N  N   . LYS   T  198 ? 2.1300 1.0086 1.8951 0.1686  -0.7095 0.2745  194 LYS   T N   
35395 C  CA  . LYS   T  198 ? 2.1449 0.9978 1.9157 0.1256  -0.7113 0.2548  194 LYS   T CA  
35396 C  C   . LYS   T  198 ? 2.1225 0.8798 1.9223 0.1551  -0.6986 0.2534  194 LYS   T C   
35397 O  O   . LYS   T  198 ? 2.1740 0.9038 1.9083 0.1322  -0.7208 0.1940  194 LYS   T O   
35398 C  CB  . LYS   T  198 ? 2.2127 1.1535 1.9340 0.0978  -0.6765 0.2613  194 LYS   T CB  
35399 C  CG  . LYS   T  198 ? 2.2592 1.1508 2.0003 0.0599  -0.6758 0.2533  194 LYS   T CG  
35400 C  CD  . LYS   T  198 ? 2.2772 1.1948 2.0100 0.0291  -0.6774 0.2773  194 LYS   T CD  
35401 C  CE  . LYS   T  198 ? 2.2708 1.1279 1.9996 -0.0438 -0.6647 0.2381  194 LYS   T CE  
35402 N  NZ  . LYS   T  198 ? 2.3170 1.0982 2.0066 -0.0486 -0.6526 0.2259  194 LYS   T NZ  
35403 N  N   . ILE   T  199 ? 2.0971 0.6977 1.8735 0.1091  -0.6837 0.2140  195 ILE   T N   
35404 C  CA  . ILE   T  199 ? 2.0941 0.6396 1.8826 0.1000  -0.6535 0.1970  195 ILE   T CA  
35405 C  C   . ILE   T  199 ? 2.0695 0.6783 1.8975 0.1378  -0.6441 0.1762  195 ILE   T C   
35406 O  O   . ILE   T  199 ? 2.0554 0.7736 1.9430 0.1330  -0.6693 0.0903  195 ILE   T O   
35407 C  CB  . ILE   T  199 ? 2.0635 0.5576 1.8051 0.0484  -0.6516 0.2096  195 ILE   T CB  
35408 C  CG1 . ILE   T  199 ? 2.0766 0.5531 1.8138 0.0136  -0.6442 0.2325  195 ILE   T CG1 
35409 C  CG2 . ILE   T  199 ? 2.0598 0.5435 1.7743 0.0635  -0.6470 0.2173  195 ILE   T CG2 
35410 C  CD1 . ILE   T  199 ? 2.0565 0.5559 1.7728 0.0052  -0.6335 0.2455  195 ILE   T CD1 
35411 N  N   . ILE   T  200 ? 2.0570 0.6753 1.9010 0.1352  -0.6299 0.1564  196 ILE   T N   
35412 C  CA  . ILE   T  200 ? 2.0475 0.7818 1.9272 0.1696  -0.6062 0.1188  196 ILE   T CA  
35413 C  C   . ILE   T  200 ? 2.0535 0.7608 2.0061 0.1719  -0.6181 0.1709  196 ILE   T C   
35414 O  O   . ILE   T  200 ? 2.0472 0.7745 1.9603 0.1501  -0.6417 0.1989  196 ILE   T O   
35415 C  CB  . ILE   T  200 ? 2.0321 0.8102 1.9244 0.1336  -0.5776 0.0942  196 ILE   T CB  
35416 C  CG1 . ILE   T  200 ? 2.0269 0.8261 1.8719 0.1528  -0.5509 0.0491  196 ILE   T CG1 
35417 C  CG2 . ILE   T  200 ? 2.0308 0.8703 1.9571 0.1434  -0.5586 0.0696  196 ILE   T CG2 
35418 C  CD1 . ILE   T  200 ? 2.0198 0.8244 1.8494 0.1634  -0.5361 0.0505  196 ILE   T CD1 
35419 N  N   . TYR   T  201 ? 2.0359 0.8435 2.0556 0.1876  -0.6319 0.1535  197 TYR   T N   
35420 C  CA  . TYR   T  201 ? 2.0386 0.9091 2.1326 0.2224  -0.6201 0.1171  197 TYR   T CA  
35421 C  C   . TYR   T  201 ? 2.0828 0.8519 2.1744 0.2806  -0.6374 0.1306  197 TYR   T C   
35422 O  O   . TYR   T  201 ? 2.0913 0.8590 2.1893 0.2903  -0.6451 0.1216  197 TYR   T O   
35423 C  CB  . TYR   T  201 ? 2.0220 0.9420 2.1279 0.2177  -0.6096 0.0968  197 TYR   T CB  
35424 C  CG  . TYR   T  201 ? 1.9793 0.9633 2.1059 0.2214  -0.6086 0.0421  197 TYR   T CG  
35425 C  CD1 . TYR   T  201 ? 1.9613 0.9612 2.0473 0.1991  -0.5810 0.0313  197 TYR   T CD1 
35426 C  CD2 . TYR   T  201 ? 1.9601 0.9903 2.1569 0.2245  -0.6183 0.0444  197 TYR   T CD2 
35427 C  CE1 . TYR   T  201 ? 1.9472 0.9846 2.0463 0.1993  -0.5612 0.0044  197 TYR   T CE1 
35428 C  CE2 . TYR   T  201 ? 1.9494 0.9946 2.1414 0.2338  -0.6020 0.0331  197 TYR   T CE2 
35429 C  CZ  . TYR   T  201 ? 1.9537 0.9943 2.0830 0.2151  -0.5647 0.0078  197 TYR   T CZ  
35430 O  OH  . TYR   T  201 ? 1.9500 1.0669 2.0762 0.1906  -0.5336 -0.0480 197 TYR   T OH  
35431 N  N   . LEU   T  202 ? 2.1097 0.8134 2.1600 0.2881  -0.6339 0.1602  198 LEU   T N   
35432 C  CA  . LEU   T  202 ? 2.1730 0.8056 2.2438 0.2679  -0.6242 0.1314  198 LEU   T CA  
35433 C  C   . LEU   T  202 ? 2.1760 0.7272 2.2597 0.2705  -0.6127 0.1027  198 LEU   T C   
35434 O  O   . LEU   T  202 ? 2.2551 0.7648 2.3789 0.2087  -0.5936 0.0301  198 LEU   T O   
35435 C  CB  . LEU   T  202 ? 2.1884 0.9077 2.2551 0.2470  -0.6110 0.1223  198 LEU   T CB  
35436 C  CG  . LEU   T  202 ? 2.2477 1.0384 2.2810 0.2499  -0.6193 0.1612  198 LEU   T CG  
35437 C  CD1 . LEU   T  202 ? 2.2551 1.1138 2.3493 0.2332  -0.6220 0.1681  198 LEU   T CD1 
35438 C  CD2 . LEU   T  202 ? 2.2359 1.0719 2.2952 0.2250  -0.6055 0.1672  198 LEU   T CD2 
35439 N  N   . ALA   T  203 ? 2.1702 0.6456 2.2540 0.2984  -0.6049 0.0245  199 ALA   T N   
35440 C  CA  . ALA   T  203 ? 2.1700 0.6155 2.2588 0.3037  -0.5974 -0.0399 199 ALA   T CA  
35441 C  C   . ALA   T  203 ? 2.1678 0.5795 2.3003 0.3258  -0.5878 -0.0939 199 ALA   T C   
35442 O  O   . ALA   T  203 ? 2.1673 0.4868 2.3554 0.3171  -0.5639 -0.1754 199 ALA   T O   
35443 C  CB  . ALA   T  203 ? 2.1257 0.6860 2.2218 0.3262  -0.6005 -0.0414 199 ALA   T CB  
35444 N  N   . HIS   T  204 ? 2.1740 0.6991 2.3188 0.3128  -0.6009 -0.0669 200 HIS   T N   
35445 C  CA  . HIS   T  204 ? 2.2210 0.9064 2.3088 0.2640  -0.5722 -0.0303 200 HIS   T CA  
35446 C  C   . HIS   T  204 ? 2.3155 0.9196 2.3271 0.2630  -0.6111 -0.0741 200 HIS   T C   
35447 O  O   . HIS   T  204 ? 2.3977 1.1160 2.3038 0.2311  -0.6067 -0.1121 200 HIS   T O   
35448 C  CB  . HIS   T  204 ? 2.1955 0.9060 2.3337 0.2623  -0.5449 0.0305  200 HIS   T CB  
35449 C  CG  . HIS   T  204 ? 2.1826 0.9108 2.3646 0.2656  -0.5279 0.0668  200 HIS   T CG  
35450 N  ND1 . HIS   T  204 ? 2.1542 0.8386 2.3693 0.2881  -0.4970 0.0833  200 HIS   T ND1 
35451 C  CD2 . HIS   T  204 ? 2.1708 0.9379 2.4260 0.2652  -0.4972 0.0622  200 HIS   T CD2 
35452 C  CE1 . HIS   T  204 ? 2.1634 0.8361 2.3899 0.2867  -0.4825 0.0640  200 HIS   T CE1 
35453 N  NE2 . HIS   T  204 ? 2.1100 0.9072 2.4321 0.3089  -0.4868 0.0286  200 HIS   T NE2 
35454 N  N   . GLU   T  205 ? 2.3555 1.0759 2.3001 0.2506  -0.6440 -0.0099 201 GLU   T N   
35455 C  CA  . GLU   T  205 ? 2.3466 1.0864 2.3421 0.2831  -0.6966 -0.0082 201 GLU   T CA  
35456 C  C   . GLU   T  205 ? 2.3430 0.9975 2.2965 0.2437  -0.6577 0.0299  201 GLU   T C   
35457 O  O   . GLU   T  205 ? 2.3197 0.8974 2.2504 0.2013  -0.6999 0.0829  201 GLU   T O   
35458 C  CB  . GLU   T  205 ? 2.3437 1.1953 2.3321 0.2967  -0.6952 -0.0097 201 GLU   T CB  
35459 C  CG  . GLU   T  205 ? 2.3494 1.3101 2.4041 0.3260  -0.7466 -0.0593 201 GLU   T CG  
35460 C  CD  . GLU   T  205 ? 2.3295 1.3409 2.4845 0.3079  -0.8069 -0.1315 201 GLU   T CD  
35461 O  OE1 . GLU   T  205 ? 2.3005 1.4325 2.4878 0.2594  -0.8171 -0.1152 201 GLU   T OE1 
35462 O  OE2 . GLU   T  205 ? 2.4291 1.3938 2.6471 0.3853  -0.8274 -0.1890 201 GLU   T OE2 
35463 N  N   . ASP   T  206 ? 2.3011 1.0368 2.2925 0.2068  -0.6453 0.0509  202 ASP   T N   
35464 C  CA  . ASP   T  206 ? 2.3234 1.0250 2.2737 0.1695  -0.6154 0.0421  202 ASP   T CA  
35465 C  C   . ASP   T  206 ? 2.3653 1.0335 2.2074 0.1819  -0.6584 0.0298  202 ASP   T C   
35466 O  O   . ASP   T  206 ? 2.3399 0.8687 2.1518 0.2355  -0.6405 0.1125  202 ASP   T O   
35467 C  CB  . ASP   T  206 ? 2.3052 1.0318 2.3025 0.1448  -0.6042 0.0644  202 ASP   T CB  
35468 C  CG  . ASP   T  206 ? 2.2889 1.0023 2.3565 0.1295  -0.6098 0.1204  202 ASP   T CG  
35469 O  OD1 . ASP   T  206 ? 2.3957 0.8702 2.3869 0.1101  -0.5961 0.1136  202 ASP   T OD1 
35470 O  OD2 . ASP   T  206 ? 2.1801 1.1328 2.4068 0.0406  -0.5942 0.1452  202 ASP   T OD2 
35471 N  N   . ASN   T  207 ? 2.4012 1.0960 2.1956 0.1383  -0.6385 0.0432  203 ASN   T N   
35472 C  CA  . ASN   T  207 ? 2.4254 1.1539 2.1232 0.1659  -0.6383 0.0177  203 ASN   T CA  
35473 C  C   . ASN   T  207 ? 2.4139 1.1711 2.1725 0.2188  -0.6051 0.0157  203 ASN   T C   
35474 O  O   . ASN   T  207 ? 2.3081 1.3216 2.0605 0.1444  -0.5644 -0.0146 203 ASN   T O   
35475 C  CB  . ASN   T  207 ? 2.4671 1.1293 2.0427 0.1477  -0.6902 0.0054  203 ASN   T CB  
35476 C  CG  . ASN   T  207 ? 2.4655 1.0604 2.0438 0.1313  -0.7010 -0.0106 203 ASN   T CG  
35477 O  OD1 . ASN   T  207 ? 2.4518 0.9191 1.9931 0.0707  -0.7381 -0.0366 203 ASN   T OD1 
35478 N  ND2 . ASN   T  207 ? 2.4634 1.0542 2.1052 0.1880  -0.6780 -0.0102 203 ASN   T ND2 
35479 N  N   . LYS   T  208 ? 2.4262 1.0248 2.3341 0.2288  -0.5177 -0.0405 204 LYS   T N   
35480 C  CA  . LYS   T  208 ? 2.4091 0.9815 2.4177 0.2450  -0.5037 -0.0488 204 LYS   T CA  
35481 C  C   . LYS   T  208 ? 2.4700 0.8751 2.4695 0.2241  -0.4626 -0.1072 204 LYS   T C   
35482 O  O   . LYS   T  208 ? 2.4923 0.9384 2.5123 0.2193  -0.4996 -0.1419 204 LYS   T O   
35483 C  CB  . LYS   T  208 ? 2.4431 1.0329 2.4319 0.2302  -0.4840 -0.0207 204 LYS   T CB  
35484 C  CG  . LYS   T  208 ? 2.4575 1.0044 2.4661 0.2387  -0.4649 0.0257  204 LYS   T CG  
35485 C  CD  . LYS   T  208 ? 2.4839 1.0029 2.4940 0.2407  -0.4490 0.0373  204 LYS   T CD  
35486 C  CE  . LYS   T  208 ? 2.4889 1.1036 2.5064 0.2329  -0.4503 0.0061  204 LYS   T CE  
35487 N  NZ  . LYS   T  208 ? 2.5213 1.1394 2.5309 0.2073  -0.4219 0.0175  204 LYS   T NZ  
35488 N  N   . GLU   T  209 ? 2.4642 0.7640 2.4761 0.2031  -0.4711 -0.1052 205 GLU   T N   
35489 C  CA  . GLU   T  209 ? 2.4515 0.9476 2.4746 0.1488  -0.4605 -0.0759 205 GLU   T CA  
35490 C  C   . GLU   T  209 ? 2.4598 0.8477 2.5113 0.2203  -0.4395 -0.0288 205 GLU   T C   
35491 O  O   . GLU   T  209 ? 2.4408 0.6899 2.5914 0.1921  -0.4099 -0.0455 205 GLU   T O   
35492 C  CB  . GLU   T  209 ? 2.4372 1.2097 2.4490 0.1526  -0.4585 -0.0687 205 GLU   T CB  
35493 C  CG  . GLU   T  209 ? 2.4176 1.3387 2.3857 0.0412  -0.4980 -0.0930 205 GLU   T CG  
35494 C  CD  . GLU   T  209 ? 2.4102 1.4631 2.2947 0.0587  -0.5273 -0.0515 205 GLU   T CD  
35495 O  OE1 . GLU   T  209 ? 2.4910 1.5618 2.1098 0.0265  -0.5159 -0.1074 205 GLU   T OE1 
35496 O  OE2 . GLU   T  209 ? 2.3726 1.3674 2.2673 0.2273  -0.5815 0.1194  205 GLU   T OE2 
35497 N  N   . LYS   T  210 ? 2.3802 0.9822 2.4452 0.2441  -0.4787 0.0494  206 LYS   T N   
35498 C  CA  . LYS   T  210 ? 2.3553 0.9899 2.3891 0.2433  -0.4859 0.0944  206 LYS   T CA  
35499 C  C   . LYS   T  210 ? 2.3231 0.9793 2.3968 0.2406  -0.4787 0.0863  206 LYS   T C   
35500 O  O   . LYS   T  210 ? 2.3276 0.8396 2.3563 0.3065  -0.4735 0.0645  206 LYS   T O   
35501 C  CB  . LYS   T  210 ? 2.3469 0.9464 2.3409 0.2448  -0.4568 0.0826  206 LYS   T CB  
35502 C  CG  . LYS   T  210 ? 2.3388 0.9166 2.3350 0.2565  -0.4815 0.0922  206 LYS   T CG  
35503 C  CD  . LYS   T  210 ? 2.3552 0.9651 2.3347 0.2456  -0.4645 0.0562  206 LYS   T CD  
35504 C  CE  . LYS   T  210 ? 2.3737 1.0060 2.4029 0.2680  -0.4737 0.0358  206 LYS   T CE  
35505 N  NZ  . LYS   T  210 ? 2.4015 1.0449 2.4299 0.2749  -0.4819 0.0052  206 LYS   T NZ  
35506 N  N   . ASP   T  211 ? 2.2983 0.9955 2.4386 0.2056  -0.4367 0.0919  207 ASP   T N   
35507 C  CA  . ASP   T  211 ? 2.2172 1.0660 2.3849 0.1547  -0.4490 0.1142  207 ASP   T CA  
35508 C  C   . ASP   T  211 ? 2.1420 1.1223 2.3098 0.1718  -0.4717 0.1488  207 ASP   T C   
35509 O  O   . ASP   T  211 ? 2.0862 1.0999 2.3216 0.1686  -0.4527 0.1973  207 ASP   T O   
35510 C  CB  . ASP   T  211 ? 2.2067 1.2303 2.4023 0.1021  -0.4386 0.1282  207 ASP   T CB  
35511 C  CG  . ASP   T  211 ? 2.1860 1.4100 2.4276 0.0835  -0.4055 0.1155  207 ASP   T CG  
35512 O  OD1 . ASP   T  211 ? 2.2247 1.4584 2.4123 0.0230  -0.3390 0.0995  207 ASP   T OD1 
35513 O  OD2 . ASP   T  211 ? 2.1580 1.6737 2.3126 0.1067  -0.4470 0.1710  207 ASP   T OD2 
35514 N  N   . PHE   T  212 ? 2.0986 1.0716 2.3152 0.2080  -0.5220 0.1584  208 PHE   T N   
35515 C  CA  . PHE   T  212 ? 2.0791 1.0271 2.2105 0.1780  -0.5343 0.1505  208 PHE   T CA  
35516 C  C   . PHE   T  212 ? 2.0698 1.0297 2.1654 0.2483  -0.5740 0.1259  208 PHE   T C   
35517 O  O   . PHE   T  212 ? 2.0765 1.1935 2.2597 0.2922  -0.6053 0.1448  208 PHE   T O   
35518 C  CB  . PHE   T  212 ? 2.0914 0.9525 2.1862 0.1466  -0.5455 0.1727  208 PHE   T CB  
35519 C  CG  . PHE   T  212 ? 2.1000 0.9301 2.1839 0.1032  -0.5500 0.1886  208 PHE   T CG  
35520 C  CD1 . PHE   T  212 ? 2.1350 0.9588 2.2173 0.1187  -0.5590 0.2097  208 PHE   T CD1 
35521 C  CD2 . PHE   T  212 ? 2.0998 0.8747 2.1439 0.0607  -0.5446 0.2083  208 PHE   T CD2 
35522 C  CE1 . PHE   T  212 ? 2.1627 0.9721 2.2181 0.1069  -0.5768 0.2301  208 PHE   T CE1 
35523 C  CE2 . PHE   T  212 ? 2.1148 0.9067 2.1455 0.0676  -0.5540 0.2335  208 PHE   T CE2 
35524 C  CZ  . PHE   T  212 ? 2.1413 0.9511 2.1770 0.0889  -0.5804 0.2485  208 PHE   T CZ  
35525 N  N   . GLU   T  213 ? 2.1014 1.0242 2.0383 0.2523  -0.5747 0.1308  209 GLU   T N   
35526 C  CA  . GLU   T  213 ? 2.0820 0.9417 1.9957 0.3050  -0.5526 0.1903  209 GLU   T CA  
35527 C  C   . GLU   T  213 ? 2.0686 0.7204 1.8739 0.3134  -0.6034 0.2158  209 GLU   T C   
35528 O  O   . GLU   T  213 ? 2.0596 0.5554 1.7500 0.3687  -0.5750 0.2723  209 GLU   T O   
35529 C  CB  . GLU   T  213 ? 2.1025 0.9927 1.9987 0.2623  -0.5107 0.1793  209 GLU   T CB  
35530 C  CG  . GLU   T  213 ? 2.1148 1.0695 2.0293 0.2446  -0.4969 0.1091  209 GLU   T CG  
35531 C  CD  . GLU   T  213 ? 2.1100 1.1337 2.0284 0.2739  -0.4585 0.1258  209 GLU   T CD  
35532 O  OE1 . GLU   T  213 ? 2.1807 1.2921 2.0481 0.2431  -0.4078 0.0679  209 GLU   T OE1 
35533 O  OE2 . GLU   T  213 ? 1.9977 1.2052 1.9641 0.3904  -0.5055 0.1624  209 GLU   T OE2 
35534 N  N   . LEU   T  214 ? 2.0385 0.7166 1.8929 0.3243  -0.5638 0.1697  210 LEU   T N   
35535 C  CA  . LEU   T  214 ? 2.0088 0.8592 1.8738 0.2738  -0.5575 0.1578  210 LEU   T CA  
35536 C  C   . LEU   T  214 ? 1.9323 0.8655 1.8138 0.2608  -0.5833 0.1755  210 LEU   T C   
35537 O  O   . LEU   T  214 ? 1.9963 0.8732 1.8942 0.2190  -0.5414 0.1287  210 LEU   T O   
35538 C  CB  . LEU   T  214 ? 2.0371 0.9291 1.8640 0.2786  -0.5558 0.1374  210 LEU   T CB  
35539 C  CG  . LEU   T  214 ? 2.0688 0.9754 1.8705 0.2702  -0.5501 0.0959  210 LEU   T CG  
35540 C  CD1 . LEU   T  214 ? 2.0819 0.9531 1.8678 0.2637  -0.5532 0.0720  210 LEU   T CD1 
35541 C  CD2 . LEU   T  214 ? 2.0867 0.9951 1.9025 0.2865  -0.5846 0.1122  210 LEU   T CD2 
35542 N  N   . GLU   T  215 ? 1.9171 0.9089 1.7170 0.2378  -0.6285 0.1969  211 GLU   T N   
35543 C  CA  . GLU   T  215 ? 1.8903 0.9264 1.6539 0.2477  -0.6514 0.2126  211 GLU   T CA  
35544 C  C   . GLU   T  215 ? 1.8595 0.9324 1.5550 0.2147  -0.7027 0.2324  211 GLU   T C   
35545 O  O   . GLU   T  215 ? 1.8809 0.8239 1.4460 0.2346  -0.7550 0.2609  211 GLU   T O   
35546 C  CB  . GLU   T  215 ? 1.8681 0.9817 1.6484 0.2495  -0.6078 0.2485  211 GLU   T CB  
35547 C  CG  . GLU   T  215 ? 1.8557 1.0003 1.6774 0.2492  -0.5718 0.3035  211 GLU   T CG  
35548 C  CD  . GLU   T  215 ? 1.8488 0.9946 1.7028 0.2662  -0.5494 0.3650  211 GLU   T CD  
35549 O  OE1 . GLU   T  215 ? 1.8389 0.9406 1.7307 0.2614  -0.5204 0.3816  211 GLU   T OE1 
35550 O  OE2 . GLU   T  215 ? 1.7990 0.9768 1.7552 0.3681  -0.5697 0.4274  211 GLU   T OE2 
35551 N  N   . ILE   T  216 ? 1.8840 0.9846 1.5384 0.2536  -0.6918 0.2086  212 ILE   T N   
35552 C  CA  . ILE   T  216 ? 1.8847 1.0182 1.5796 0.2382  -0.6677 0.1792  212 ILE   T CA  
35553 C  C   . ILE   T  216 ? 1.8848 1.0167 1.5673 0.2354  -0.6546 0.1126  212 ILE   T C   
35554 O  O   . ILE   T  216 ? 1.8290 1.1157 1.6857 0.2275  -0.6032 0.0683  212 ILE   T O   
35555 C  CB  . ILE   T  216 ? 1.9344 0.9441 1.5768 0.2296  -0.6524 0.1868  212 ILE   T CB  
35556 C  CG1 . ILE   T  216 ? 1.9567 0.9435 1.6363 0.2338  -0.6655 0.2188  212 ILE   T CG1 
35557 C  CG2 . ILE   T  216 ? 1.9471 0.9369 1.5614 0.2097  -0.6475 0.1913  212 ILE   T CG2 
35558 C  CD1 . ILE   T  216 ? 1.9510 0.9554 1.6599 0.2449  -0.6932 0.2018  212 ILE   T CD1 
35559 N  N   . SER   T  217 ? 1.8717 1.1561 1.5546 0.1933  -0.6346 0.0565  213 SER   T N   
35560 C  CA  . SER   T  217 ? 1.9059 1.1650 1.5087 0.2003  -0.6358 0.0554  213 SER   T CA  
35561 C  C   . SER   T  217 ? 1.9476 1.1783 1.4699 0.1794  -0.6394 0.0375  213 SER   T C   
35562 O  O   . SER   T  217 ? 1.9418 1.2177 1.3907 0.1330  -0.6829 0.0336  213 SER   T O   
35563 C  CB  . SER   T  217 ? 1.9118 1.2219 1.4875 0.2030  -0.6395 0.0435  213 SER   T CB  
35564 O  OG  . SER   T  217 ? 1.9082 1.1972 1.4446 0.2183  -0.6610 0.0805  213 SER   T OG  
35565 N  N   . TRP   T  218 ? 1.9536 1.1492 1.4473 0.1315  -0.6060 0.0398  214 TRP   T N   
35566 C  CA  . TRP   T  218 ? 1.9467 1.0350 1.4389 0.1057  -0.6087 0.0524  214 TRP   T CA  
35567 C  C   . TRP   T  218 ? 1.9237 0.9626 1.3983 0.0245  -0.6051 0.0236  214 TRP   T C   
35568 O  O   . TRP   T  218 ? 1.9036 0.8234 1.3239 0.0374  -0.6766 -0.0674 214 TRP   T O   
35569 C  CB  . TRP   T  218 ? 1.9539 1.0292 1.4519 0.1061  -0.6108 0.0789  214 TRP   T CB  
35570 C  CG  . TRP   T  218 ? 1.9636 1.0202 1.4447 0.1035  -0.5946 0.0489  214 TRP   T CG  
35571 C  CD1 . TRP   T  218 ? 1.9406 1.0466 1.4521 0.1167  -0.5670 0.0335  214 TRP   T CD1 
35572 C  CD2 . TRP   T  218 ? 1.9788 1.0557 1.4418 0.0917  -0.5913 0.0405  214 TRP   T CD2 
35573 N  NE1 . TRP   T  218 ? 1.9332 1.0962 1.4286 0.1250  -0.5667 0.0203  214 TRP   T NE1 
35574 C  CE2 . TRP   T  218 ? 1.9497 1.0986 1.4356 0.0954  -0.5826 0.0342  214 TRP   T CE2 
35575 C  CE3 . TRP   T  218 ? 1.9846 1.0487 1.4632 0.0776  -0.5912 0.0595  214 TRP   T CE3 
35576 C  CZ2 . TRP   T  218 ? 1.9238 1.1156 1.4809 0.0769  -0.6005 0.0394  214 TRP   T CZ2 
35577 C  CZ3 . TRP   T  218 ? 1.9646 1.0906 1.4873 0.0819  -0.6149 0.0823  214 TRP   T CZ3 
35578 C  CH2 . TRP   T  218 ? 1.9485 1.1190 1.5007 0.0794  -0.6085 0.0715  214 TRP   T CH2 
35579 N  N   . CYS   T  219 ? 1.9339 0.9516 1.3888 0.0266  -0.5932 0.0505  215 CYS   T N   
35580 C  CA  . CYS   T  219 ? 1.9654 0.9464 1.4198 0.0259  -0.5702 0.0577  215 CYS   T CA  
35581 C  C   . CYS   T  219 ? 1.9489 0.9112 1.4641 0.0292  -0.5321 0.1387  215 CYS   T C   
35582 O  O   . CYS   T  219 ? 1.9750 0.9068 1.5749 -0.0435 -0.5257 0.0424  215 CYS   T O   
35583 C  CB  . CYS   T  219 ? 1.9994 1.0595 1.3925 -0.0074 -0.5992 0.0710  215 CYS   T CB  
35584 S  SG  . CYS   T  219 ? 2.1035 1.3275 1.3975 0.0206  -0.5567 0.2082  215 CYS   T SG  
35585 N  N   . SER   T  220 ? 1.9003 0.9160 1.4602 0.0753  -0.5596 0.1445  216 SER   T N   
35586 C  CA  . SER   T  220 ? 1.8900 0.8885 1.4579 0.1033  -0.5578 0.1985  216 SER   T CA  
35587 C  C   . SER   T  220 ? 1.8676 0.8860 1.4611 0.1008  -0.5543 0.1978  216 SER   T C   
35588 O  O   . SER   T  220 ? 1.7757 0.7285 1.5291 0.1910  -0.5894 0.1567  216 SER   T O   
35589 C  CB  . SER   T  220 ? 1.9288 0.8548 1.4329 0.1209  -0.5430 0.2265  216 SER   T CB  
35590 O  OG  . SER   T  220 ? 1.9252 0.7823 1.4220 0.1600  -0.5427 0.2706  216 SER   T OG  
35591 N  N   . LEU   T  221 ? 1.8885 0.9862 1.4799 0.0372  -0.5095 0.2414  217 LEU   T N   
35592 C  CA  . LEU   T  221 ? 1.9126 1.0558 1.5569 0.0108  -0.4696 0.1606  217 LEU   T CA  
35593 C  C   . LEU   T  221 ? 1.9158 1.1992 1.5907 -0.0475 -0.4883 0.1761  217 LEU   T C   
35594 O  O   . LEU   T  221 ? 2.0240 1.2369 1.7321 -0.1707 -0.4731 0.0937  217 LEU   T O   
35595 C  CB  . LEU   T  221 ? 1.9100 1.2252 1.6388 0.0006  -0.4600 0.2318  217 LEU   T CB  
35596 C  CG  . LEU   T  221 ? 1.8236 1.3505 1.6620 0.0582  -0.4373 0.1999  217 LEU   T CG  
35597 C  CD1 . LEU   T  221 ? 1.7519 1.4029 1.6737 0.0864  -0.4660 0.2027  217 LEU   T CD1 
35598 C  CD2 . LEU   T  221 ? 1.8115 1.3990 1.6503 0.0586  -0.4435 0.2055  217 LEU   T CD2 
35599 N  N   . SER   T  222 ? 1.8371 1.0581 1.5124 -0.1480 -0.5344 0.1014  218 SER   T N   
35600 C  CA  . SER   T  222 ? 1.8732 1.0788 1.4701 -0.1791 -0.5288 0.0906  218 SER   T CA  
35601 C  C   . SER   T  222 ? 1.8796 1.0640 1.4689 -0.1880 -0.5239 0.0158  218 SER   T C   
35602 O  O   . SER   T  222 ? 1.8416 1.2137 1.5887 -0.2747 -0.4753 0.0380  218 SER   T O   
35603 C  CB  . SER   T  222 ? 1.8701 1.0673 1.4523 -0.2044 -0.5629 0.0799  218 SER   T CB  
35604 O  OG  . SER   T  222 ? 1.8439 1.0573 1.4093 -0.2506 -0.6227 0.0592  218 SER   T OG  
35605 N  N   . GLU   T  223 ? 1.8837 1.0587 1.4695 -0.1903 -0.5165 0.0114  219 GLU   T N   
35606 C  CA  . GLU   T  223 ? 1.8832 1.0526 1.5337 -0.1742 -0.5215 -0.0369 219 GLU   T CA  
35607 C  C   . GLU   T  223 ? 1.8841 0.9490 1.5633 -0.2094 -0.4812 -0.0806 219 GLU   T C   
35608 O  O   . GLU   T  223 ? 1.8581 0.9410 1.6441 -0.2188 -0.5550 -0.2271 219 GLU   T O   
35609 C  CB  . GLU   T  223 ? 1.9092 1.0588 1.5748 -0.1218 -0.4980 -0.0029 219 GLU   T CB  
35610 C  CG  . GLU   T  223 ? 1.9624 1.1538 1.5724 -0.1361 -0.4826 0.0142  219 GLU   T CG  
35611 C  CD  . GLU   T  223 ? 1.9641 1.1930 1.6332 -0.1429 -0.4895 -0.0148 219 GLU   T CD  
35612 O  OE1 . GLU   T  223 ? 2.0368 1.1957 1.6547 -0.1050 -0.4115 0.0300  219 GLU   T OE1 
35613 O  OE2 . GLU   T  223 ? 1.9977 1.1794 1.7047 -0.1625 -0.4480 -0.0215 219 GLU   T OE2 
35614 N  N   . THR   T  224 ? 1.9339 0.9336 1.5391 -0.1745 -0.4723 -0.0320 220 THR   T N   
35615 C  CA  . THR   T  224 ? 1.9930 0.9028 1.5510 -0.1683 -0.4242 -0.0263 220 THR   T CA  
35616 C  C   . THR   T  224 ? 1.9916 0.9245 1.5284 -0.1647 -0.3997 0.0186  220 THR   T C   
35617 O  O   . THR   T  224 ? 2.0742 0.9813 1.4943 -0.1474 -0.3780 -0.0062 220 THR   T O   
35618 C  CB  . THR   T  224 ? 2.0030 0.8432 1.5534 -0.1761 -0.4030 -0.0095 220 THR   T CB  
35619 O  OG1 . THR   T  224 ? 1.9952 0.7255 1.5054 -0.1601 -0.4057 -0.0443 220 THR   T OG1 
35620 C  CG2 . THR   T  224 ? 2.0331 0.8701 1.5696 -0.1526 -0.4289 -0.0217 220 THR   T CG2 
35621 N  N   . ASN   T  225 ? 1.9363 0.9469 1.4843 -0.1881 -0.4087 0.0806  221 ASN   T N   
35622 C  CA  . ASN   T  225 ? 1.8642 0.9769 1.4071 -0.1858 -0.4788 0.0974  221 ASN   T CA  
35623 C  C   . ASN   T  225 ? 1.8573 0.9199 1.2946 -0.1543 -0.4571 0.1456  221 ASN   T C   
35624 O  O   . ASN   T  225 ? 1.7989 0.9069 1.2081 -0.1764 -0.5412 0.0663  221 ASN   T O   
35625 C  CB  . ASN   T  225 ? 1.8581 1.0309 1.5086 -0.2386 -0.5003 0.0804  221 ASN   T CB  
35626 C  CG  . ASN   T  225 ? 1.8766 1.0526 1.5553 -0.3588 -0.5648 0.0001  221 ASN   T CG  
35627 O  OD1 . ASN   T  225 ? 1.8421 1.2552 1.6661 -0.4036 -0.6246 0.0261  221 ASN   T OD1 
35628 N  ND2 . ASN   T  225 ? 1.8607 1.0704 1.6274 -0.3908 -0.5893 0.0056  221 ASN   T ND2 
35629 N  N   . GLY   T  226 ? 1.7900 0.8951 1.1808 -0.1259 -0.4999 0.2177  222 GLY   T N   
35630 C  CA  . GLY   T  226 ? 1.7772 0.9241 1.1384 -0.0699 -0.5063 0.2442  222 GLY   T CA  
35631 C  C   . GLY   T  226 ? 1.7572 0.9512 1.1373 -0.0507 -0.5159 0.2250  222 GLY   T C   
35632 O  O   . GLY   T  226 ? 1.7757 1.0749 1.1157 -0.0762 -0.5132 0.2076  222 GLY   T O   
35633 N  N   . LEU   T  227 ? 1.7482 0.9555 1.1517 -0.0296 -0.5135 0.2113  223 LEU   T N   
35634 C  CA  . LEU   T  227 ? 1.7645 0.8848 1.1534 0.0093  -0.5076 0.1697  223 LEU   T CA  
35635 C  C   . LEU   T  227 ? 1.8087 0.8209 1.1582 0.0050  -0.5288 0.2234  223 LEU   T C   
35636 O  O   . LEU   T  227 ? 1.8092 0.7136 1.1765 0.0262  -0.5038 0.2118  223 LEU   T O   
35637 C  CB  . LEU   T  227 ? 1.7445 0.9151 1.1641 -0.0036 -0.5021 0.1440  223 LEU   T CB  
35638 C  CG  . LEU   T  227 ? 1.7309 0.9125 1.1604 -0.0126 -0.5036 0.1355  223 LEU   T CG  
35639 C  CD1 . LEU   T  227 ? 1.7294 0.9557 1.1800 -0.0281 -0.4707 0.1260  223 LEU   T CD1 
35640 C  CD2 . LEU   T  227 ? 1.7212 0.9186 1.1573 -0.0185 -0.5105 0.1096  223 LEU   T CD2 
35641 N  N   . HIS   T  228 ? 1.8618 0.7221 1.2015 -0.0034 -0.5228 0.1793  224 HIS   T N   
35642 C  CA  . HIS   T  228 ? 1.8871 0.6901 1.2924 0.0124  -0.5538 0.1943  224 HIS   T CA  
35643 C  C   . HIS   T  228 ? 1.8704 0.7492 1.3804 0.0376  -0.5866 0.1916  224 HIS   T C   
35644 O  O   . HIS   T  228 ? 1.8727 0.8091 1.4408 0.0243  -0.5545 0.2376  224 HIS   T O   
35645 C  CB  . HIS   T  228 ? 1.9313 0.6211 1.2680 0.0171  -0.5084 0.1602  224 HIS   T CB  
35646 C  CG  . HIS   T  228 ? 1.9453 0.6294 1.2303 0.0215  -0.4965 0.1517  224 HIS   T CG  
35647 N  ND1 . HIS   T  228 ? 1.9705 0.5730 1.2084 0.0373  -0.4930 0.1082  224 HIS   T ND1 
35648 C  CD2 . HIS   T  228 ? 1.9652 0.5822 1.2062 0.0501  -0.5141 0.0955  224 HIS   T CD2 
35649 C  CE1 . HIS   T  228 ? 1.9857 0.5638 1.2055 0.0306  -0.5162 0.1108  224 HIS   T CE1 
35650 N  NE2 . HIS   T  228 ? 1.9721 0.5119 1.2142 0.0516  -0.5295 0.1147  224 HIS   T NE2 
35651 N  N   . LYS   T  229 ? 1.8342 0.8225 1.4758 0.0767  -0.6233 0.1539  225 LYS   T N   
35652 C  CA  . LYS   T  229 ? 1.8334 0.8719 1.5780 0.0673  -0.6098 0.1145  225 LYS   T CA  
35653 C  C   . LYS   T  229 ? 1.7974 0.8662 1.5626 0.0562  -0.6675 0.0970  225 LYS   T C   
35654 O  O   . LYS   T  229 ? 1.7939 0.7635 1.5377 0.0771  -0.7322 0.0729  225 LYS   T O   
35655 C  CB  . LYS   T  229 ? 1.8102 0.9134 1.6288 0.0119  -0.5872 0.0745  225 LYS   T CB  
35656 C  CG  . LYS   T  229 ? 1.8274 0.9096 1.7039 -0.0089 -0.5132 0.0794  225 LYS   T CG  
35657 C  CD  . LYS   T  229 ? 1.8162 0.9920 1.7668 -0.0539 -0.5017 0.0545  225 LYS   T CD  
35658 C  CE  . LYS   T  229 ? 1.8324 0.9760 1.8091 -0.0567 -0.4427 0.0808  225 LYS   T CE  
35659 N  NZ  . LYS   T  229 ? 1.8105 0.9151 1.8272 -0.0568 -0.4349 0.0627  225 LYS   T NZ  
35660 N  N   . PHE   T  230 ? 1.8046 0.8927 1.5680 0.0752  -0.6740 0.0408  226 PHE   T N   
35661 C  CA  . PHE   T  230 ? 1.8772 0.8411 1.6264 0.0576  -0.6643 0.0374  226 PHE   T CA  
35662 C  C   . PHE   T  230 ? 1.8512 0.8567 1.7142 0.1066  -0.6799 0.0927  226 PHE   T C   
35663 O  O   . PHE   T  230 ? 1.8381 0.8718 1.8615 0.0659  -0.6434 0.0976  226 PHE   T O   
35664 C  CB  . PHE   T  230 ? 1.9104 0.8540 1.5742 0.0721  -0.6890 -0.0045 226 PHE   T CB  
35665 C  CG  . PHE   T  230 ? 1.9694 0.8105 1.5274 0.0918  -0.6782 -0.0130 226 PHE   T CG  
35666 C  CD1 . PHE   T  230 ? 1.9826 0.8063 1.4659 0.1041  -0.6805 -0.0276 226 PHE   T CD1 
35667 C  CD2 . PHE   T  230 ? 2.0190 0.8775 1.5063 0.0632  -0.6764 -0.0736 226 PHE   T CD2 
35668 C  CE1 . PHE   T  230 ? 1.9977 0.7401 1.4621 0.1148  -0.6802 -0.0375 226 PHE   T CE1 
35669 C  CE2 . PHE   T  230 ? 2.0316 0.8403 1.4969 0.1140  -0.6858 -0.0137 226 PHE   T CE2 
35670 C  CZ  . PHE   T  230 ? 2.0360 0.7403 1.5275 0.1164  -0.6432 -0.0585 226 PHE   T CZ  
35671 N  N   . VAL   T  231 ? 1.8388 0.7914 1.7969 0.0901  -0.6811 0.0339  227 VAL   T N   
35672 C  CA  . VAL   T  231 ? 1.8566 0.7460 1.8488 0.1194  -0.6784 0.1043  227 VAL   T CA  
35673 C  C   . VAL   T  231 ? 1.8519 0.7323 1.9172 0.1625  -0.6822 0.1134  227 VAL   T C   
35674 O  O   . VAL   T  231 ? 1.7839 0.7397 1.9269 0.1521  -0.7146 0.1003  227 VAL   T O   
35675 C  CB  . VAL   T  231 ? 1.8651 0.7677 1.8267 0.1276  -0.6999 0.1320  227 VAL   T CB  
35676 C  CG1 . VAL   T  231 ? 1.8829 0.8638 1.8425 0.1083  -0.7285 0.1427  227 VAL   T CG1 
35677 C  CG2 . VAL   T  231 ? 1.8610 0.7298 1.7944 0.1318  -0.7065 0.1505  227 VAL   T CG2 
35678 N  N   . LYS   T  232 ? 1.8316 0.7531 1.9827 0.1559  -0.6734 0.1416  228 LYS   T N   
35679 C  CA  . LYS   T  232 ? 1.8599 0.7944 2.0685 0.1876  -0.6257 0.1313  228 LYS   T CA  
35680 C  C   . LYS   T  232 ? 1.8534 0.7221 2.0892 0.2285  -0.6373 0.1386  228 LYS   T C   
35681 O  O   . LYS   T  232 ? 1.8322 0.5479 2.0960 0.2840  -0.6679 0.1365  228 LYS   T O   
35682 C  CB  . LYS   T  232 ? 1.8899 0.9063 2.0840 0.0842  -0.5289 0.1603  228 LYS   T CB  
35683 C  CG  . LYS   T  232 ? 1.8774 1.0410 2.0767 0.0444  -0.5201 0.1304  228 LYS   T CG  
35684 C  CD  . LYS   T  232 ? 1.8901 1.0208 2.0930 0.0024  -0.4616 0.1316  228 LYS   T CD  
35685 C  CE  . LYS   T  232 ? 1.9050 1.0825 2.0858 -0.0304 -0.4335 0.1190  228 LYS   T CE  
35686 N  NZ  . LYS   T  232 ? 1.9022 1.1083 2.0892 -0.0453 -0.4012 0.1245  228 LYS   T NZ  
35687 N  N   . GLY   T  233 ? 1.8438 0.8303 2.1106 0.2169  -0.6350 0.1176  229 GLY   T N   
35688 C  CA  . GLY   T  233 ? 1.8771 1.0184 2.1671 0.1736  -0.6669 0.0884  229 GLY   T CA  
35689 C  C   . GLY   T  233 ? 1.9280 1.1783 2.1655 0.1500  -0.6964 0.1258  229 GLY   T C   
35690 O  O   . GLY   T  233 ? 1.9002 1.1884 2.2640 0.1396  -0.6774 0.0988  229 GLY   T O   
35691 N  N   . ASP   T  234 ? 1.9696 1.2500 2.2027 0.1246  -0.7408 0.0913  230 ASP   T N   
35692 C  CA  . ASP   T  234 ? 1.9875 1.2696 2.2231 0.1114  -0.7773 0.1063  230 ASP   T CA  
35693 C  C   . ASP   T  234 ? 1.9820 1.2795 2.1951 0.1153  -0.7913 0.1483  230 ASP   T C   
35694 O  O   . ASP   T  234 ? 1.9504 1.3490 2.2217 0.0927  -0.8567 0.2334  230 ASP   T O   
35695 C  CB  . ASP   T  234 ? 2.0523 1.2626 2.2499 0.1128  -0.7921 0.0901  230 ASP   T CB  
35696 C  CG  . ASP   T  234 ? 2.0776 1.2345 2.2533 0.0832  -0.8390 0.0679  230 ASP   T CG  
35697 O  OD1 . ASP   T  234 ? 2.1670 1.1231 2.3116 0.0660  -0.8070 0.0209  230 ASP   T OD1 
35698 O  OD2 . ASP   T  234 ? 2.1337 1.2738 2.1315 0.1622  -0.8768 0.1034  230 ASP   T OD2 
35699 N  N   . LEU   T  235 ? 1.9244 1.2412 2.1063 0.0794  -0.7255 0.0759  231 LEU   T N   
35700 C  CA  . LEU   T  235 ? 1.9638 1.1867 2.0452 0.0786  -0.6958 0.0882  231 LEU   T CA  
35701 C  C   . LEU   T  235 ? 1.9593 1.0917 1.9964 0.0898  -0.6779 0.1706  231 LEU   T C   
35702 O  O   . LEU   T  235 ? 1.9629 1.0179 2.0127 0.1775  -0.7382 0.2525  231 LEU   T O   
35703 C  CB  . LEU   T  235 ? 1.9344 1.1383 2.0106 0.0529  -0.6420 0.0217  231 LEU   T CB  
35704 C  CG  . LEU   T  235 ? 1.9916 1.1116 1.9846 -0.0241 -0.6279 -0.0005 231 LEU   T CG  
35705 C  CD1 . LEU   T  235 ? 1.9763 1.1337 1.9872 -0.0423 -0.6517 0.0325  231 LEU   T CD1 
35706 C  CD2 . LEU   T  235 ? 1.9748 1.0652 1.9769 -0.0486 -0.5951 -0.0018 231 LEU   T CD2 
35707 N  N   . LEU   T  236 ? 2.0139 1.1414 1.9862 0.1273  -0.6724 0.1476  232 LEU   T N   
35708 C  CA  . LEU   T  236 ? 2.0292 1.1051 1.8930 0.1572  -0.6634 0.1970  232 LEU   T CA  
35709 C  C   . LEU   T  236 ? 2.0476 1.1360 1.8746 0.1660  -0.6711 0.2360  232 LEU   T C   
35710 O  O   . LEU   T  236 ? 2.0270 1.1889 1.8822 0.1154  -0.6830 0.2655  232 LEU   T O   
35711 C  CB  . LEU   T  236 ? 2.0442 1.0795 1.8774 0.1739  -0.6603 0.1811  232 LEU   T CB  
35712 C  CG  . LEU   T  236 ? 2.0445 1.0648 1.8389 0.2037  -0.6450 0.2023  232 LEU   T CG  
35713 C  CD1 . LEU   T  236 ? 2.0393 1.0686 1.8030 0.2144  -0.6672 0.2185  232 LEU   T CD1 
35714 C  CD2 . LEU   T  236 ? 2.0553 1.0090 1.8504 0.2130  -0.6169 0.1894  232 LEU   T CD2 
35715 N  N   . GLN   T  237 ? 2.0266 1.1907 1.8289 0.1982  -0.6519 0.2556  233 GLN   T N   
35716 C  CA  . GLN   T  237 ? 2.0721 1.2449 1.8301 0.2383  -0.6615 0.2682  233 GLN   T CA  
35717 C  C   . GLN   T  237 ? 2.0900 1.2334 1.8320 0.2409  -0.7013 0.2885  233 GLN   T C   
35718 O  O   . GLN   T  237 ? 2.0633 1.2622 1.8234 0.2767  -0.7731 0.3191  233 GLN   T O   
35719 C  CB  . GLN   T  237 ? 2.0434 1.2830 1.7867 0.2706  -0.6544 0.2660  233 GLN   T CB  
35720 C  CG  . GLN   T  237 ? 2.0876 1.3022 1.7872 0.3064  -0.6685 0.2719  233 GLN   T CG  
35721 C  CD  . GLN   T  237 ? 2.0873 1.3019 1.7749 0.3520  -0.6504 0.2744  233 GLN   T CD  
35722 O  OE1 . GLN   T  237 ? 2.1005 1.2495 1.7110 0.3835  -0.6126 0.1799  233 GLN   T OE1 
35723 N  NE2 . GLN   T  237 ? 2.0993 1.3102 1.8095 0.3762  -0.6653 0.2804  233 GLN   T NE2 
35724 N  N   . GLU   T  238 ? 2.1524 1.2506 1.7959 0.2190  -0.6895 0.2855  234 GLU   T N   
35725 C  CA  . GLU   T  238 ? 2.2149 1.2285 1.8073 0.2444  -0.6963 0.3277  234 GLU   T CA  
35726 C  C   . GLU   T  238 ? 2.2359 1.1798 1.7869 0.2473  -0.7105 0.3659  234 GLU   T C   
35727 O  O   . GLU   T  238 ? 2.3088 1.1642 1.7931 0.1430  -0.6610 0.3584  234 GLU   T O   
35728 C  CB  . GLU   T  238 ? 2.2690 1.2592 1.8044 0.2430  -0.6355 0.3216  234 GLU   T CB  
35729 C  CG  . GLU   T  238 ? 2.3325 1.2985 1.8331 0.2589  -0.5819 0.3287  234 GLU   T CG  
35730 C  CD  . GLU   T  238 ? 2.3884 1.3575 1.8653 0.2550  -0.5063 0.3010  234 GLU   T CD  
35731 O  OE1 . GLU   T  238 ? 2.4183 1.3083 1.9421 0.2688  -0.4504 0.2876  234 GLU   T OE1 
35732 O  OE2 . GLU   T  238 ? 2.4443 1.4162 1.9247 0.1636  -0.3928 0.2287  234 GLU   T OE2 
35733 N  N   . ALA   T  239 ? 2.1375 1.2129 1.8804 0.2324  -0.7259 0.3071  235 ALA   T N   
35734 C  CA  . ALA   T  239 ? 2.1391 1.1805 1.9908 0.2095  -0.6819 0.3366  235 ALA   T CA  
35735 C  C   . ALA   T  239 ? 2.0927 1.1450 2.0682 0.2300  -0.7038 0.3613  235 ALA   T C   
35736 O  O   . ALA   T  239 ? 2.0798 1.2516 2.0656 0.1943  -0.7217 0.4696  235 ALA   T O   
35737 C  CB  . ALA   T  239 ? 2.0899 1.2452 1.9621 0.2201  -0.6741 0.2954  235 ALA   T CB  
35738 N  N   . ILE   T  240 ? 2.0505 1.0279 2.1307 0.2098  -0.6927 0.3115  236 ILE   T N   
35739 C  CA  . ILE   T  240 ? 2.0273 1.0530 2.1266 0.1908  -0.6902 0.2759  236 ILE   T CA  
35740 C  C   . ILE   T  240 ? 2.0767 1.0915 2.1830 0.2031  -0.7490 0.2926  236 ILE   T C   
35741 O  O   . ILE   T  240 ? 2.1045 1.0572 2.2127 0.2461  -0.7912 0.3970  236 ILE   T O   
35742 C  CB  . ILE   T  240 ? 2.0000 1.0141 2.1273 0.1980  -0.6446 0.1685  236 ILE   T CB  
35743 C  CG1 . ILE   T  240 ? 1.9541 0.9745 2.0477 0.1906  -0.5934 0.1284  236 ILE   T CG1 
35744 C  CG2 . ILE   T  240 ? 1.9908 1.0560 2.1571 0.1994  -0.6160 0.1413  236 ILE   T CG2 
35745 C  CD1 . ILE   T  240 ? 1.9240 1.0147 2.0484 0.1929  -0.5528 0.0776  236 ILE   T CD1 
35746 N  N   . ASP   T  241 ? 2.0863 1.1680 2.1610 0.2245  -0.7933 0.3227  237 ASP   T N   
35747 C  CA  . ASP   T  241 ? 2.1067 1.2238 2.1631 0.2200  -0.8293 0.3192  237 ASP   T CA  
35748 C  C   . ASP   T  241 ? 2.1600 1.2372 2.0999 0.2539  -0.8421 0.3856  237 ASP   T C   
35749 O  O   . ASP   T  241 ? 2.2429 1.2741 2.0785 0.2239  -0.9133 0.5067  237 ASP   T O   
35750 C  CB  . ASP   T  241 ? 2.1077 1.3078 2.1762 0.2257  -0.8516 0.2764  237 ASP   T CB  
35751 C  CG  . ASP   T  241 ? 2.0767 1.3352 2.1876 0.2205  -0.8400 0.2136  237 ASP   T CG  
35752 O  OD1 . ASP   T  241 ? 2.0930 1.3786 2.2539 0.2286  -0.8119 0.1689  237 ASP   T OD1 
35753 O  OD2 . ASP   T  241 ? 2.0829 1.3726 2.1573 0.2153  -0.8523 0.1687  237 ASP   T OD2 
35754 N  N   . PHE   T  242 ? 2.1953 1.2167 2.0275 0.2587  -0.8214 0.3806  238 PHE   T N   
35755 C  CA  . PHE   T  242 ? 2.2207 1.2754 2.0136 0.2618  -0.8034 0.4017  238 PHE   T CA  
35756 C  C   . PHE   T  242 ? 2.2054 1.2975 2.0696 0.2269  -0.7905 0.4136  238 PHE   T C   
35757 O  O   . PHE   T  242 ? 2.2534 1.4680 2.0606 0.1691  -0.7808 0.5264  238 PHE   T O   
35758 C  CB  . PHE   T  242 ? 2.1934 1.2893 1.9294 0.2073  -0.7799 0.2982  238 PHE   T CB  
35759 C  CG  . PHE   T  242 ? 2.2071 1.2746 1.8762 0.1886  -0.7891 0.2714  238 PHE   T CG  
35760 C  CD1 . PHE   T  242 ? 2.2037 1.3110 1.8777 0.2008  -0.8109 0.3107  238 PHE   T CD1 
35761 C  CD2 . PHE   T  242 ? 2.2248 1.2255 1.8847 0.1777  -0.7549 0.1996  238 PHE   T CD2 
35762 C  CE1 . PHE   T  242 ? 2.2111 1.2967 1.8298 0.2029  -0.8158 0.2989  238 PHE   T CE1 
35763 C  CE2 . PHE   T  242 ? 2.2558 1.1940 1.8265 0.1783  -0.7533 0.1940  238 PHE   T CE2 
35764 C  CZ  . PHE   T  242 ? 2.2403 1.2185 1.8263 0.1838  -0.7925 0.2490  238 PHE   T CZ  
35765 N  N   . ALA   T  243 ? 2.2236 1.4270 2.0585 0.2479  -0.7139 0.4619  239 ALA   T N   
35766 C  CA  . ALA   T  243 ? 2.2193 1.4668 2.1259 0.2045  -0.6798 0.4418  239 ALA   T CA  
35767 C  C   . ALA   T  243 ? 2.2187 1.5076 2.1776 0.2308  -0.6123 0.5208  239 ALA   T C   
35768 O  O   . ALA   T  243 ? 2.2883 1.5018 2.1950 0.2347  -0.5648 0.5960  239 ALA   T O   
35769 C  CB  . ALA   T  243 ? 2.1964 1.4457 2.1370 0.2076  -0.6787 0.4462  239 ALA   T CB  
35770 N  N   . GLN   T  244 ? 2.2005 1.6145 2.1764 0.2979  -0.5459 0.5049  240 GLN   T N   
35771 C  CA  . GLN   T  244 ? 2.1719 1.6622 2.1941 0.3076  -0.5093 0.5292  240 GLN   T CA  
35772 C  C   . GLN   T  244 ? 2.1203 1.6579 2.2291 0.2069  -0.5137 0.5630  240 GLN   T C   
35773 O  O   . GLN   T  244 ? 2.1036 1.6374 2.2957 0.1250  -0.5238 0.5634  240 GLN   T O   
35774 C  CB  . GLN   T  244 ? 2.1101 1.7189 2.1684 0.3772  -0.4654 0.5240  240 GLN   T CB  
35775 C  CG  . GLN   T  244 ? 2.1080 1.7954 2.1698 0.4073  -0.3857 0.4970  240 GLN   T CG  
35776 C  CD  . GLN   T  244 ? 2.1208 1.8404 2.1562 0.4700  -0.3416 0.4954  240 GLN   T CD  
35777 O  OE1 . GLN   T  244 ? 2.1497 2.0282 2.1123 0.4474  -0.2397 0.4028  240 GLN   T OE1 
35778 N  NE2 . GLN   T  244 ? 2.1240 1.8734 2.2082 0.5220  -0.3559 0.5225  240 GLN   T NE2 
35779 N  N   . LYS   T  245 ? 2.0726 1.5731 2.2044 0.1384  -0.4985 0.6025  241 LYS   T N   
35780 C  CA  . LYS   T  245 ? 2.0942 1.6395 2.1864 0.0862  -0.5013 0.6161  241 LYS   T CA  
35781 C  C   . LYS   T  245 ? 2.1644 1.6932 2.1513 0.0315  -0.5045 0.6330  241 LYS   T C   
35782 O  O   . LYS   T  245 ? 2.1491 1.7603 2.0713 -0.0446 -0.5389 0.6801  241 LYS   T O   
35783 C  CB  . LYS   T  245 ? 2.0248 1.6178 2.1271 0.0216  -0.4688 0.6502  241 LYS   T CB  
35784 C  CG  . LYS   T  245 ? 2.0345 1.7265 2.1053 -0.0401 -0.4828 0.6364  241 LYS   T CG  
35785 C  CD  . LYS   T  245 ? 2.0401 1.7800 2.1337 -0.0975 -0.4546 0.6018  241 LYS   T CD  
35786 C  CE  . LYS   T  245 ? 2.0603 1.9013 2.1664 -0.1120 -0.5014 0.6143  241 LYS   T CE  
35787 N  NZ  . LYS   T  245 ? 2.0974 1.9818 2.1160 -0.1257 -0.5227 0.6038  241 LYS   T NZ  
35788 N  N   . GLU   T  246 ? 2.2413 1.6497 2.1524 0.1219  -0.5391 0.6132  242 GLU   T N   
35789 C  CA  . GLU   T  246 ? 2.3460 1.6334 2.1651 0.0548  -0.5356 0.6208  242 GLU   T CA  
35790 C  C   . GLU   T  246 ? 2.4312 1.5912 2.2931 0.0642  -0.5740 0.5953  242 GLU   T C   
35791 O  O   . GLU   T  246 ? 2.4217 1.6184 2.1933 0.0437  -0.5288 0.5531  242 GLU   T O   
35792 C  CB  . GLU   T  246 ? 2.3148 1.7130 2.1501 0.0422  -0.5221 0.6241  242 GLU   T CB  
35793 C  CG  . GLU   T  246 ? 2.3692 1.7955 2.0338 -0.0516 -0.5397 0.6223  242 GLU   T CG  
35794 C  CD  . GLU   T  246 ? 2.3908 1.8048 2.0641 -0.1164 -0.5628 0.6899  242 GLU   T CD  
35795 O  OE1 . GLU   T  246 ? 2.4342 1.7942 2.0476 -0.1102 -0.5853 0.7391  242 GLU   T OE1 
35796 O  OE2 . GLU   T  246 ? 2.4578 1.7474 1.8884 -0.1567 -0.5682 0.7591  242 GLU   T OE2 
35797 N  N   . ILE   T  247 ? 2.5410 1.6403 2.2807 0.0668  -0.5572 0.4650  243 ILE   T N   
35798 C  CA  . ILE   T  247 ? 2.6086 1.6327 2.4777 0.0472  -0.6352 0.3868  243 ILE   T CA  
35799 C  C   . ILE   T  247 ? 2.6556 1.6829 2.5634 0.0950  -0.6370 0.4189  243 ILE   T C   
35800 O  O   . ILE   T  247 ? 2.6664 1.7381 2.6733 0.0602  -0.6627 0.3399  243 ILE   T O   
35801 C  CB  . ILE   T  247 ? 2.6021 1.6201 2.4458 0.0237  -0.6312 0.3126  243 ILE   T CB  
35802 C  CG1 . ILE   T  247 ? 2.6262 1.6592 2.4687 -0.0101 -0.5921 0.2700  243 ILE   T CG1 
35803 C  CG2 . ILE   T  247 ? 2.5582 1.5942 2.3956 0.0046  -0.6501 0.2868  243 ILE   T CG2 
35804 C  CD1 . ILE   T  247 ? 2.5723 1.6211 2.4796 -0.0155 -0.5824 0.2423  243 ILE   T CD1 
35805 N  N   . ASN   T  248 ? 2.5992 1.6636 2.5907 0.1552  -0.6386 0.4214  244 ASN   T N   
35806 C  CA  . ASN   T  248 ? 2.4711 1.7426 2.5648 0.1104  -0.6402 0.4320  244 ASN   T CA  
35807 C  C   . ASN   T  248 ? 2.5262 1.7649 2.5147 0.2435  -0.8030 0.5540  244 ASN   T C   
35808 O  O   . ASN   T  248 ? 2.5433 1.6892 2.3751 0.3742  -0.8456 0.6260  244 ASN   T O   
35809 C  CB  . ASN   T  248 ? 2.4971 1.7017 2.5768 0.0562  -0.5918 0.3373  244 ASN   T CB  
35810 C  CG  . ASN   T  248 ? 2.3180 1.6077 2.6156 -0.0580 -0.4227 0.2475  244 ASN   T CG  
35811 O  OD1 . ASN   T  248 ? 2.3202 1.6925 2.6026 -0.0952 -0.2765 0.1728  244 ASN   T OD1 
35812 N  ND2 . ASN   T  248 ? 2.2540 1.5949 2.5635 -0.0554 -0.3981 0.1464  244 ASN   T ND2 
35813 N  N   . GLY   U  11  ? 2.4399 1.0165 1.6492 0.0594  -0.3090 -0.2768 2   GLY   U N   
35814 C  CA  . GLY   U  11  ? 2.3809 1.0088 1.5852 -0.0085 -0.3205 -0.2464 2   GLY   U CA  
35815 C  C   . GLY   U  11  ? 2.3416 1.0112 1.5426 -0.1009 -0.3766 -0.1761 2   GLY   U C   
35816 O  O   . GLY   U  11  ? 2.2508 1.0967 1.5454 -0.1811 -0.4774 -0.0691 2   GLY   U O   
35817 N  N   . TYR   U  12  ? 2.3624 0.9556 1.5781 -0.1359 -0.3920 -0.2071 3   TYR   U N   
35818 C  CA  . TYR   U  12  ? 2.3367 0.9464 1.6085 -0.1099 -0.4054 -0.2283 3   TYR   U CA  
35819 C  C   . TYR   U  12  ? 2.3881 0.7655 1.5850 -0.0739 -0.4238 -0.1673 3   TYR   U C   
35820 O  O   . TYR   U  12  ? 2.3470 0.7267 1.6293 -0.0937 -0.3790 -0.1504 3   TYR   U O   
35821 C  CB  . TYR   U  12  ? 2.2746 0.9025 1.6582 -0.2024 -0.4059 -0.2940 3   TYR   U CB  
35822 C  CG  . TYR   U  12  ? 2.2448 1.0170 1.8519 -0.2298 -0.4241 -0.3451 3   TYR   U CG  
35823 C  CD1 . TYR   U  12  ? 2.2391 1.0713 1.8376 -0.2468 -0.4199 -0.3486 3   TYR   U CD1 
35824 C  CD2 . TYR   U  12  ? 2.2516 1.1146 1.8691 -0.2515 -0.4199 -0.3146 3   TYR   U CD2 
35825 C  CE1 . TYR   U  12  ? 2.2322 1.1610 1.9586 -0.2318 -0.4177 -0.3416 3   TYR   U CE1 
35826 C  CE2 . TYR   U  12  ? 2.2568 1.1856 1.9664 -0.2408 -0.3948 -0.3156 3   TYR   U CE2 
35827 C  CZ  . TYR   U  12  ? 2.2271 1.2141 1.9818 -0.2347 -0.3954 -0.3469 3   TYR   U CZ  
35828 O  OH  . TYR   U  12  ? 2.2274 1.3091 2.0825 -0.2195 -0.3939 -0.3715 3   TYR   U OH  
35829 N  N   . ASP   U  13  ? 2.4318 0.6538 1.5648 -0.0640 -0.5123 -0.1377 4   ASP   U N   
35830 C  CA  . ASP   U  13  ? 2.4308 0.6270 1.6017 -0.0250 -0.5334 -0.0545 4   ASP   U CA  
35831 C  C   . ASP   U  13  ? 2.4335 0.5488 1.6198 -0.0537 -0.6442 0.0326  4   ASP   U C   
35832 O  O   . ASP   U  13  ? 2.3847 0.2921 1.5902 -0.0286 -0.6987 0.1927  4   ASP   U O   
35833 C  CB  . ASP   U  13  ? 2.4426 0.7078 1.6992 -0.0673 -0.5309 -0.0555 4   ASP   U CB  
35834 C  CG  . ASP   U  13  ? 2.5370 0.7256 1.8146 -0.1119 -0.4703 -0.0272 4   ASP   U CG  
35835 O  OD1 . ASP   U  13  ? 2.5335 0.9570 1.9286 -0.0504 -0.4381 0.0112  4   ASP   U OD1 
35836 O  OD2 . ASP   U  13  ? 2.5210 1.0504 1.8885 -0.1369 -0.4023 -0.0343 4   ASP   U OD2 
35837 N  N   . ARG   U  14  ? 2.4238 0.6063 1.4590 -0.0233 -0.6138 0.0024  5   ARG   U N   
35838 C  CA  . ARG   U  14  ? 2.3384 0.6253 1.4488 -0.0274 -0.6091 -0.0052 5   ARG   U CA  
35839 C  C   . ARG   U  14  ? 2.3366 0.5625 1.3661 -0.0025 -0.6062 0.0121  5   ARG   U C   
35840 O  O   . ARG   U  14  ? 2.3507 0.4309 1.3760 -0.0865 -0.6388 -0.0085 5   ARG   U O   
35841 C  CB  . ARG   U  14  ? 2.3617 0.6259 1.4439 0.0071  -0.5675 -0.0382 5   ARG   U CB  
35842 C  CG  . ARG   U  14  ? 2.3409 0.7521 1.4769 -0.0363 -0.5859 -0.0485 5   ARG   U CG  
35843 C  CD  . ARG   U  14  ? 2.3552 0.8578 1.5047 -0.0334 -0.5516 0.0295  5   ARG   U CD  
35844 N  NE  . ARG   U  14  ? 2.3663 0.9090 1.5490 -0.0535 -0.5556 0.0142  5   ARG   U NE  
35845 C  CZ  . ARG   U  14  ? 2.3764 0.9239 1.5761 -0.0603 -0.5373 0.0095  5   ARG   U CZ  
35846 N  NH1 . ARG   U  14  ? 2.3869 0.9765 1.5863 -0.0170 -0.5240 0.0356  5   ARG   U NH1 
35847 N  NH2 . ARG   U  14  ? 2.4257 1.0164 1.5829 -0.0913 -0.5464 -0.0495 5   ARG   U NH2 
35848 N  N   . HIS   U  15  ? 2.2490 0.5041 1.3538 0.0024  -0.6180 -0.0384 6   HIS   U N   
35849 C  CA  . HIS   U  15  ? 2.1760 0.5717 1.3718 0.0252  -0.6001 -0.0622 6   HIS   U CA  
35850 C  C   . HIS   U  15  ? 2.1067 0.5976 1.3278 0.0459  -0.5740 -0.0951 6   HIS   U C   
35851 O  O   . HIS   U  15  ? 2.0700 0.4903 1.3587 0.0781  -0.5249 -0.1255 6   HIS   U O   
35852 C  CB  . HIS   U  15  ? 2.1726 0.5872 1.4377 0.0527  -0.5862 -0.0909 6   HIS   U CB  
35853 C  CG  . HIS   U  15  ? 2.1855 0.5839 1.5539 0.0534  -0.5966 -0.0944 6   HIS   U CG  
35854 N  ND1 . HIS   U  15  ? 2.1683 0.6391 1.6262 0.0135  -0.6289 -0.1116 6   HIS   U ND1 
35855 C  CD2 . HIS   U  15  ? 2.2300 0.6233 1.6607 0.0055  -0.5864 -0.0527 6   HIS   U CD2 
35856 C  CE1 . HIS   U  15  ? 2.2132 0.6490 1.7229 0.0347  -0.6007 -0.0483 6   HIS   U CE1 
35857 N  NE2 . HIS   U  15  ? 2.2275 0.6708 1.7363 0.0192  -0.5901 -0.0449 6   HIS   U NE2 
35858 N  N   . ILE   U  16  ? 2.0727 0.5640 1.3205 0.0510  -0.5545 -0.1078 7   ILE   U N   
35859 C  CA  . ILE   U  16  ? 1.9907 0.5667 1.2727 0.0435  -0.5513 -0.0552 7   ILE   U CA  
35860 C  C   . ILE   U  16  ? 1.9808 0.5492 1.2514 0.0190  -0.5662 -0.0353 7   ILE   U C   
35861 O  O   . ILE   U  16  ? 1.9474 0.5430 1.2596 0.0684  -0.6651 -0.1986 7   ILE   U O   
35862 C  CB  . ILE   U  16  ? 2.0143 0.6375 1.2294 0.0437  -0.5550 -0.0684 7   ILE   U CB  
35863 C  CG1 . ILE   U  16  ? 2.0573 0.6044 1.2631 0.0451  -0.5534 -0.0963 7   ILE   U CG1 
35864 C  CG2 . ILE   U  16  ? 2.0050 0.7158 1.2622 0.0559  -0.5367 -0.0485 7   ILE   U CG2 
35865 C  CD1 . ILE   U  16  ? 2.0586 0.6534 1.2415 0.0529  -0.5548 -0.1004 7   ILE   U CD1 
35866 N  N   . THR   U  17  ? 1.9000 0.5761 1.2197 0.0602  -0.4976 0.0916  8   THR   U N   
35867 C  CA  . THR   U  17  ? 1.9004 0.6111 1.2407 0.0502  -0.4695 0.1667  8   THR   U CA  
35868 C  C   . THR   U  17  ? 1.8782 0.6364 1.2644 0.0065  -0.4820 0.1394  8   THR   U C   
35869 O  O   . THR   U  17  ? 1.8336 0.7285 1.3004 0.0637  -0.4865 0.1395  8   THR   U O   
35870 C  CB  . THR   U  17  ? 1.8654 0.6441 1.1703 0.0967  -0.4280 0.2023  8   THR   U CB  
35871 O  OG1 . THR   U  17  ? 1.8626 0.6693 1.1422 0.1355  -0.3967 0.2487  8   THR   U OG1 
35872 C  CG2 . THR   U  17  ? 1.8589 0.6601 1.1621 0.0783  -0.4099 0.2091  8   THR   U CG2 
35873 N  N   . ILE   U  18  ? 1.9308 0.5531 1.3679 0.0301  -0.4373 0.1558  9   ILE   U N   
35874 C  CA  . ILE   U  18  ? 1.9257 0.5964 1.4151 0.0284  -0.4538 0.1508  9   ILE   U CA  
35875 C  C   . ILE   U  18  ? 1.9471 0.6148 1.5187 -0.0169 -0.4654 0.0980  9   ILE   U C   
35876 O  O   . ILE   U  18  ? 1.9454 0.6510 1.5511 0.0143  -0.4793 0.0951  9   ILE   U O   
35877 C  CB  . ILE   U  18  ? 1.9213 0.5438 1.4471 0.0465  -0.4187 0.1678  9   ILE   U CB  
35878 C  CG1 . ILE   U  18  ? 1.9525 0.4806 1.3810 0.0277  -0.4054 0.1510  9   ILE   U CG1 
35879 C  CG2 . ILE   U  18  ? 1.9078 0.5741 1.4627 0.0311  -0.3883 0.1686  9   ILE   U CG2 
35880 C  CD1 . ILE   U  18  ? 1.9715 0.4346 1.3632 0.0262  -0.4330 0.1445  9   ILE   U CD1 
35881 N  N   . PHE   U  19  ? 2.0006 0.5922 1.4789 -0.0179 -0.4972 0.0648  10  PHE   U N   
35882 C  CA  . PHE   U  19  ? 1.9959 0.5963 1.4445 -0.0249 -0.5163 0.0365  10  PHE   U CA  
35883 C  C   . PHE   U  19  ? 2.0314 0.6234 1.4488 0.0306  -0.5123 0.0568  10  PHE   U C   
35884 O  O   . PHE   U  19  ? 2.0318 0.8555 1.4316 0.0331  -0.5247 0.0547  10  PHE   U O   
35885 C  CB  . PHE   U  19  ? 2.0224 0.5905 1.3828 -0.0472 -0.5366 0.0254  10  PHE   U CB  
35886 C  CG  . PHE   U  19  ? 2.0226 0.5362 1.3096 -0.0650 -0.5526 0.0492  10  PHE   U CG  
35887 C  CD1 . PHE   U  19  ? 2.0322 0.5502 1.3294 -0.0700 -0.5261 0.0478  10  PHE   U CD1 
35888 C  CD2 . PHE   U  19  ? 2.0172 0.5871 1.2425 -0.0641 -0.5592 0.0682  10  PHE   U CD2 
35889 C  CE1 . PHE   U  19  ? 2.0045 0.5717 1.3380 -0.0530 -0.5116 0.0778  10  PHE   U CE1 
35890 C  CE2 . PHE   U  19  ? 1.9923 0.6609 1.2457 -0.0477 -0.5438 0.0613  10  PHE   U CE2 
35891 C  CZ  . PHE   U  19  ? 1.9895 0.6469 1.2701 -0.0554 -0.5288 0.1054  10  PHE   U CZ  
35892 N  N   . SER   U  20  ? 2.0721 0.4733 1.5213 0.0755  -0.5233 0.0060  11  SER   U N   
35893 C  CA  . SER   U  20  ? 2.1279 0.4812 1.4949 0.1132  -0.5569 -0.0108 11  SER   U CA  
35894 C  C   . SER   U  20  ? 2.1766 0.3827 1.4815 0.1233  -0.5718 -0.0463 11  SER   U C   
35895 O  O   . SER   U  20  ? 2.2133 0.3239 1.4435 0.1371  -0.5939 -0.0866 11  SER   U O   
35896 C  CB  . SER   U  20  ? 2.1200 0.4296 1.5172 0.1442  -0.5599 -0.0235 11  SER   U CB  
35897 O  OG  . SER   U  20  ? 2.0952 0.3470 1.5478 0.1276  -0.5744 -0.0343 11  SER   U OG  
35898 N  N   . PRO   U  21  ? 2.2262 0.3226 1.5064 0.1029  -0.5654 -0.0161 12  PRO   U N   
35899 C  CA  . PRO   U  21  ? 2.2825 0.2297 1.5199 0.0727  -0.5706 -0.0427 12  PRO   U CA  
35900 C  C   . PRO   U  21  ? 2.3002 0.2476 1.5175 0.0284  -0.5699 -0.0490 12  PRO   U C   
35901 O  O   . PRO   U  21  ? 2.2762 0.2433 1.5813 -0.0520 -0.5727 -0.0881 12  PRO   U O   
35902 C  CB  . PRO   U  21  ? 2.3202 0.2142 1.5366 0.0751  -0.5665 -0.0290 12  PRO   U CB  
35903 C  CG  . PRO   U  21  ? 2.3214 0.1885 1.5083 0.0882  -0.5447 -0.0323 12  PRO   U CG  
35904 C  CD  . PRO   U  21  ? 2.2656 0.2184 1.4827 0.0964  -0.5499 -0.0237 12  PRO   U CD  
35905 N  N   . GLU   U  22  ? 2.3068 0.2884 1.5166 0.0691  -0.5922 -0.0414 13  GLU   U N   
35906 C  CA  . GLU   U  22  ? 2.3265 0.4013 1.5182 0.0690  -0.5805 -0.0657 13  GLU   U CA  
35907 C  C   . GLU   U  22  ? 2.3076 0.3663 1.4486 0.0742  -0.5672 -0.0055 13  GLU   U C   
35908 O  O   . GLU   U  22  ? 2.3406 0.3026 1.4291 0.0644  -0.5611 -0.0120 13  GLU   U O   
35909 C  CB  . GLU   U  22  ? 2.3897 0.3902 1.5552 0.0790  -0.5848 -0.0699 13  GLU   U CB  
35910 C  CG  . GLU   U  22  ? 2.3934 0.4856 1.6206 0.0984  -0.5928 -0.1210 13  GLU   U CG  
35911 C  CD  . GLU   U  22  ? 2.4855 0.4608 1.6654 0.1421  -0.5796 -0.1487 13  GLU   U CD  
35912 O  OE1 . GLU   U  22  ? 2.5734 0.5358 1.6767 0.1098  -0.6546 -0.1467 13  GLU   U OE1 
35913 O  OE2 . GLU   U  22  ? 2.5080 0.3818 1.6439 0.1572  -0.6196 -0.1910 13  GLU   U OE2 
35914 N  N   . GLY   U  23  ? 2.3000 0.3810 1.4019 0.0961  -0.5556 0.0190  14  GLY   U N   
35915 C  CA  . GLY   U  23  ? 2.2825 0.4151 1.3661 0.1403  -0.5360 0.0222  14  GLY   U CA  
35916 C  C   . GLY   U  23  ? 2.2709 0.4424 1.3475 0.1323  -0.5126 0.0228  14  GLY   U C   
35917 O  O   . GLY   U  23  ? 2.2854 0.4033 1.3768 0.1115  -0.5205 -0.0031 14  GLY   U O   
35918 N  N   . ARG   U  24  ? 2.2634 0.4578 1.3349 0.1235  -0.5079 0.0172  15  ARG   U N   
35919 C  CA  . ARG   U  24  ? 2.2563 0.3693 1.3406 0.0429  -0.4919 -0.0037 15  ARG   U CA  
35920 C  C   . ARG   U  24  ? 2.3158 0.2295 1.2738 0.0273  -0.4854 -0.0162 15  ARG   U C   
35921 O  O   . ARG   U  24  ? 2.3878 0.1037 1.2122 -0.0493 -0.5113 -0.0584 15  ARG   U O   
35922 C  CB  . ARG   U  24  ? 2.2609 0.4144 1.3657 0.0670  -0.4821 0.0377  15  ARG   U CB  
35923 C  CG  . ARG   U  24  ? 2.2495 0.4481 1.4263 0.0362  -0.4848 0.0054  15  ARG   U CG  
35924 C  CD  . ARG   U  24  ? 2.2717 0.4160 1.4617 0.0159  -0.4809 -0.0448 15  ARG   U CD  
35925 N  NE  . ARG   U  24  ? 2.2390 0.3309 1.4729 0.0182  -0.4670 -0.0332 15  ARG   U NE  
35926 C  CZ  . ARG   U  24  ? 2.2261 0.3817 1.4598 0.0131  -0.4652 0.0316  15  ARG   U CZ  
35927 N  NH1 . ARG   U  24  ? 2.2611 0.4694 1.5154 -0.0630 -0.4604 0.0004  15  ARG   U NH1 
35928 N  NH2 . ARG   U  24  ? 2.2209 0.4062 1.4182 -0.0259 -0.4479 0.0025  15  ARG   U NH2 
35929 N  N   . LEU   U  25  ? 2.2604 0.2645 1.3094 0.0115  -0.5241 -0.0186 16  LEU   U N   
35930 C  CA  . LEU   U  25  ? 2.1768 0.3334 1.3213 0.0655  -0.5283 0.0296  16  LEU   U CA  
35931 C  C   . LEU   U  25  ? 2.1582 0.2685 1.3813 0.1265  -0.5220 0.0114  16  LEU   U C   
35932 O  O   . LEU   U  25  ? 2.1378 0.2603 1.3203 0.1719  -0.5881 0.1041  16  LEU   U O   
35933 C  CB  . LEU   U  25  ? 2.1430 0.3501 1.3294 0.0564  -0.4800 0.0093  16  LEU   U CB  
35934 C  CG  . LEU   U  25  ? 2.1113 0.4011 1.3183 0.0664  -0.4616 0.0156  16  LEU   U CG  
35935 C  CD1 . LEU   U  25  ? 2.0719 0.4063 1.3367 0.0671  -0.4300 0.0146  16  LEU   U CD1 
35936 C  CD2 . LEU   U  25  ? 2.1313 0.4321 1.3043 0.0738  -0.4621 0.0002  16  LEU   U CD2 
35937 N  N   . TYR   U  26  ? 2.1549 0.2330 1.4289 0.1204  -0.5261 0.0021  17  TYR   U N   
35938 C  CA  . TYR   U  26  ? 2.1261 0.2687 1.4250 0.1103  -0.5167 0.0166  17  TYR   U CA  
35939 C  C   . TYR   U  26  ? 2.0246 0.2202 1.4558 0.0997  -0.4377 0.0118  17  TYR   U C   
35940 O  O   . TYR   U  26  ? 1.9777 0.2334 1.4556 0.0996  -0.4377 -0.0042 17  TYR   U O   
35941 C  CB  . TYR   U  26  ? 2.1800 0.3329 1.3913 0.1252  -0.5304 -0.0155 17  TYR   U CB  
35942 C  CG  . TYR   U  26  ? 2.2876 0.2942 1.3865 0.1196  -0.5805 0.0045  17  TYR   U CG  
35943 C  CD1 . TYR   U  26  ? 2.3438 0.2129 1.4093 0.1206  -0.5899 -0.0140 17  TYR   U CD1 
35944 C  CD2 . TYR   U  26  ? 2.3637 0.2892 1.3953 0.1272  -0.5990 -0.0239 17  TYR   U CD2 
35945 C  CE1 . TYR   U  26  ? 2.4055 0.2376 1.4291 0.0804  -0.5914 -0.0075 17  TYR   U CE1 
35946 C  CE2 . TYR   U  26  ? 2.4234 0.2162 1.4190 0.1419  -0.6030 -0.0004 17  TYR   U CE2 
35947 C  CZ  . TYR   U  26  ? 2.4381 0.2775 1.4279 0.1032  -0.6014 0.0214  17  TYR   U CZ  
35948 O  OH  . TYR   U  26  ? 2.4633 0.3958 1.4859 0.0281  -0.6226 0.0008  17  TYR   U OH  
35949 N  N   . GLN   U  27  ? 1.9684 0.2449 1.4274 0.1233  -0.3983 0.0244  18  GLN   U N   
35950 C  CA  . GLN   U  27  ? 1.9522 0.1756 1.3829 0.1229  -0.3649 0.0584  18  GLN   U CA  
35951 C  C   . GLN   U  27  ? 1.9037 0.1527 1.3944 0.0787  -0.3633 0.0488  18  GLN   U C   
35952 O  O   . GLN   U  27  ? 1.9388 0.1124 1.4265 0.0504  -0.3774 0.0185  18  GLN   U O   
35953 C  CB  . GLN   U  27  ? 1.9454 0.2033 1.3605 0.1520  -0.3573 0.0789  18  GLN   U CB  
35954 C  CG  . GLN   U  27  ? 1.9725 0.2250 1.3487 0.1727  -0.3523 0.0887  18  GLN   U CG  
35955 C  CD  . GLN   U  27  ? 1.9810 0.2659 1.3192 0.1701  -0.3510 0.1086  18  GLN   U CD  
35956 O  OE1 . GLN   U  27  ? 1.9651 0.2896 1.2773 0.1914  -0.3709 0.1087  18  GLN   U OE1 
35957 N  NE2 . GLN   U  27  ? 1.9778 0.3038 1.3144 0.2316  -0.3435 0.1411  18  GLN   U NE2 
35958 N  N   . VAL   U  28  ? 1.8777 0.1901 1.3309 0.0243  -0.3872 0.0658  19  VAL   U N   
35959 C  CA  . VAL   U  28  ? 1.8189 0.2737 1.3340 -0.0049 -0.3876 0.0507  19  VAL   U CA  
35960 C  C   . VAL   U  28  ? 1.8348 0.3311 1.3688 -0.0512 -0.3504 0.0796  19  VAL   U C   
35961 O  O   . VAL   U  28  ? 1.7962 0.1744 1.3949 -0.1164 -0.3323 0.0469  19  VAL   U O   
35962 C  CB  . VAL   U  28  ? 1.8024 0.3174 1.2882 -0.0147 -0.3848 0.0419  19  VAL   U CB  
35963 C  CG1 . VAL   U  28  ? 1.7535 0.3353 1.2558 -0.0291 -0.4105 0.0540  19  VAL   U CG1 
35964 C  CG2 . VAL   U  28  ? 1.7984 0.3592 1.2797 0.0019  -0.3578 0.0565  19  VAL   U CG2 
35965 N  N   . GLU   U  29  ? 1.8792 0.3798 1.3769 -0.0400 -0.3648 0.0170  20  GLU   U N   
35966 C  CA  . GLU   U  29  ? 1.8941 0.4572 1.3562 -0.0014 -0.3762 0.0771  20  GLU   U CA  
35967 C  C   . GLU   U  29  ? 1.9173 0.4477 1.3009 0.0005  -0.3723 0.1043  20  GLU   U C   
35968 O  O   . GLU   U  29  ? 1.9182 0.4846 1.2848 0.0005  -0.3839 0.0910  20  GLU   U O   
35969 C  CB  . GLU   U  29  ? 1.9141 0.5297 1.3846 -0.0121 -0.3807 0.0248  20  GLU   U CB  
35970 C  CG  . GLU   U  29  ? 1.9015 0.6505 1.4414 -0.0144 -0.3842 -0.0004 20  GLU   U CG  
35971 C  CD  . GLU   U  29  ? 1.9379 0.7050 1.4818 0.0066  -0.4078 -0.0633 20  GLU   U CD  
35972 O  OE1 . GLU   U  29  ? 1.9482 1.0547 1.5186 -0.0104 -0.4276 -0.1160 20  GLU   U OE1 
35973 O  OE2 . GLU   U  29  ? 1.9556 0.7359 1.5368 0.0356  -0.4115 -0.0204 20  GLU   U OE2 
35974 N  N   . TYR   U  30  ? 1.9173 0.4575 1.2512 0.0304  -0.3841 0.1467  21  TYR   U N   
35975 C  CA  . TYR   U  30  ? 1.9493 0.4740 1.2281 0.0515  -0.4001 0.1762  21  TYR   U CA  
35976 C  C   . TYR   U  30  ? 1.9025 0.4747 1.2293 0.0604  -0.3966 0.1726  21  TYR   U C   
35977 O  O   . TYR   U  30  ? 1.8758 0.4715 1.2574 0.0952  -0.4116 0.1408  21  TYR   U O   
35978 C  CB  . TYR   U  30  ? 1.9809 0.4921 1.2238 0.0727  -0.3860 0.2169  21  TYR   U CB  
35979 C  CG  . TYR   U  30  ? 2.0750 0.4863 1.2697 0.1027  -0.3868 0.1993  21  TYR   U CG  
35980 C  CD1 . TYR   U  30  ? 2.0816 0.5435 1.3160 0.0764  -0.3830 0.2082  21  TYR   U CD1 
35981 C  CD2 . TYR   U  30  ? 2.0987 0.5145 1.2965 0.1274  -0.3579 0.2205  21  TYR   U CD2 
35982 C  CE1 . TYR   U  30  ? 2.1131 0.5421 1.3330 0.0928  -0.3896 0.1930  21  TYR   U CE1 
35983 C  CE2 . TYR   U  30  ? 2.1147 0.5505 1.3018 0.1371  -0.3682 0.2009  21  TYR   U CE2 
35984 C  CZ  . TYR   U  30  ? 2.1408 0.4967 1.3176 0.1324  -0.3920 0.1624  21  TYR   U CZ  
35985 O  OH  . TYR   U  30  ? 2.1503 0.4472 1.3828 0.1829  -0.3720 0.1415  21  TYR   U OH  
35986 N  N   . ALA   U  31  ? 1.9017 0.4503 1.1704 0.0147  -0.4078 0.1705  22  ALA   U N   
35987 C  CA  . ALA   U  31  ? 1.9110 0.4899 1.1877 -0.0248 -0.4143 0.1489  22  ALA   U CA  
35988 C  C   . ALA   U  31  ? 1.9389 0.4641 1.2560 -0.0554 -0.3693 0.1566  22  ALA   U C   
35989 O  O   . ALA   U  31  ? 1.9631 0.4624 1.3107 -0.0591 -0.4173 0.1477  22  ALA   U O   
35990 C  CB  . ALA   U  31  ? 1.8758 0.5324 1.1358 -0.0157 -0.4333 0.1553  22  ALA   U CB  
35991 N  N   . PHE   U  32  ? 1.9874 0.4180 1.2823 -0.0833 -0.3788 0.1075  23  PHE   U N   
35992 C  CA  . PHE   U  32  ? 2.0083 0.3619 1.2985 -0.0802 -0.3627 0.1096  23  PHE   U CA  
35993 C  C   . PHE   U  32  ? 1.9983 0.3374 1.2845 -0.0791 -0.3561 0.0929  23  PHE   U C   
35994 O  O   . PHE   U  32  ? 1.9740 0.3226 1.2812 -0.0768 -0.3705 0.1042  23  PHE   U O   
35995 C  CB  . PHE   U  32  ? 2.0173 0.3288 1.3057 -0.0591 -0.3767 0.1019  23  PHE   U CB  
35996 C  CG  . PHE   U  32  ? 2.0791 0.2547 1.3003 -0.0456 -0.3586 0.0920  23  PHE   U CG  
35997 C  CD1 . PHE   U  32  ? 2.0844 0.1789 1.3115 -0.0274 -0.3482 0.1125  23  PHE   U CD1 
35998 C  CD2 . PHE   U  32  ? 2.0971 0.2151 1.2959 -0.0286 -0.3485 0.0814  23  PHE   U CD2 
35999 C  CE1 . PHE   U  32  ? 2.0625 0.2272 1.3389 -0.0211 -0.3410 0.0859  23  PHE   U CE1 
36000 C  CE2 . PHE   U  32  ? 2.0831 0.2120 1.3006 -0.0390 -0.3330 0.0774  23  PHE   U CE2 
36001 C  CZ  . PHE   U  32  ? 2.0794 0.2635 1.3057 -0.0400 -0.3292 0.0713  23  PHE   U CZ  
36002 N  N   . LYS   U  33  ? 2.0271 0.3721 1.2883 -0.0469 -0.3596 0.0849  24  LYS   U N   
36003 C  CA  . LYS   U  33  ? 2.0806 0.4492 1.2614 -0.0148 -0.3805 0.0985  24  LYS   U CA  
36004 C  C   . LYS   U  33  ? 2.0562 0.3152 1.2995 0.0034  -0.3567 0.1179  24  LYS   U C   
36005 O  O   . LYS   U  33  ? 2.1210 0.4258 1.3107 0.0033  -0.3531 0.1414  24  LYS   U O   
36006 C  CB  . LYS   U  33  ? 2.1603 0.5363 1.2798 -0.0542 -0.3860 0.0108  24  LYS   U CB  
36007 C  CG  . LYS   U  33  ? 2.2479 0.5968 1.3551 -0.1380 -0.3810 -0.0742 24  LYS   U CG  
36008 C  CD  . LYS   U  33  ? 2.3187 0.6879 1.4477 -0.1656 -0.3423 -0.1615 24  LYS   U CD  
36009 C  CE  . LYS   U  33  ? 2.3099 0.6981 1.4512 -0.2329 -0.3517 -0.1927 24  LYS   U CE  
36010 N  NZ  . LYS   U  33  ? 2.3131 0.6999 1.4346 -0.3197 -0.3816 -0.2466 24  LYS   U NZ  
36011 N  N   . ALA   U  34  ? 2.0533 0.2402 1.2369 0.0818  -0.3881 0.1312  25  ALA   U N   
36012 C  CA  . ALA   U  34  ? 2.0109 0.2774 1.2393 0.0980  -0.3931 0.1376  25  ALA   U CA  
36013 C  C   . ALA   U  34  ? 1.9621 0.2630 1.2535 0.1050  -0.4042 0.1276  25  ALA   U C   
36014 O  O   . ALA   U  34  ? 2.0087 0.2036 1.2678 0.0679  -0.4257 0.1420  25  ALA   U O   
36015 C  CB  . ALA   U  34  ? 2.0007 0.3142 1.2346 0.0714  -0.3726 0.1303  25  ALA   U CB  
36016 N  N   . THR   U  35  ? 1.9599 0.2767 1.2802 0.1251  -0.3982 0.0725  26  THR   U N   
36017 C  CA  . THR   U  35  ? 1.9022 0.2731 1.3298 0.1449  -0.4050 0.0352  26  THR   U CA  
36018 C  C   . THR   U  35  ? 1.8935 0.3033 1.3408 0.1139  -0.4037 0.0607  26  THR   U C   
36019 O  O   . THR   U  35  ? 1.8567 0.0957 1.4814 0.1327  -0.3773 0.0185  26  THR   U O   
36020 C  CB  . THR   U  35  ? 1.8985 0.3119 1.3184 0.1345  -0.3715 -0.0522 26  THR   U CB  
36021 O  OG1 . THR   U  35  ? 1.8802 0.3640 1.2645 0.1687  -0.3695 -0.0564 26  THR   U OG1 
36022 C  CG2 . THR   U  35  ? 1.9001 0.2367 1.3000 0.1476  -0.3802 -0.0415 26  THR   U CG2 
36023 N  N   . ASN   U  36  ? 1.8906 0.3004 1.3633 0.0843  -0.4061 0.1067  27  ASN   U N   
36024 C  CA  . ASN   U  36  ? 1.8676 0.3529 1.4004 0.1249  -0.4403 0.1462  27  ASN   U CA  
36025 C  C   . ASN   U  36  ? 1.8510 0.3968 1.4211 0.0619  -0.4449 0.1964  27  ASN   U C   
36026 O  O   . ASN   U  36  ? 1.9357 0.6168 1.3287 -0.0018 -0.4896 0.1949  27  ASN   U O   
36027 C  CB  . ASN   U  36  ? 1.8379 0.3535 1.3647 0.1416  -0.4748 0.1454  27  ASN   U CB  
36028 C  CG  . ASN   U  36  ? 1.8389 0.3572 1.3621 0.1559  -0.4844 0.1301  27  ASN   U CG  
36029 O  OD1 . ASN   U  36  ? 1.7937 0.4859 1.3559 0.1340  -0.4557 0.0779  27  ASN   U OD1 
36030 N  ND2 . ASN   U  36  ? 1.8498 0.4142 1.3552 0.1539  -0.4943 0.1157  27  ASN   U ND2 
36031 N  N   . GLN   U  37  ? 1.8746 0.4689 1.4192 0.0525  -0.4560 0.2577  28  GLN   U N   
36032 C  CA  . GLN   U  37  ? 1.8693 0.6112 1.4989 0.0449  -0.4183 0.2781  28  GLN   U CA  
36033 C  C   . GLN   U  37  ? 1.8734 0.6278 1.4575 -0.0003 -0.3531 0.2683  28  GLN   U C   
36034 O  O   . GLN   U  37  ? 1.7660 0.6837 1.4163 -0.0528 -0.3120 0.3070  28  GLN   U O   
36035 C  CB  . GLN   U  37  ? 1.8903 0.7210 1.5453 0.0536  -0.4082 0.3397  28  GLN   U CB  
36036 C  CG  . GLN   U  37  ? 1.9268 0.8480 1.6739 0.1206  -0.3721 0.3921  28  GLN   U CG  
36037 C  CD  . GLN   U  37  ? 1.9301 0.8749 1.8339 0.0357  -0.3093 0.4036  28  GLN   U CD  
36038 O  OE1 . GLN   U  37  ? 1.8737 0.8814 1.8783 0.0303  -0.1820 0.4482  28  GLN   U OE1 
36039 N  NE2 . GLN   U  37  ? 2.0084 1.1343 1.9537 0.1676  -0.3159 0.4628  28  GLN   U NE2 
36040 N  N   . THR   U  38  ? 1.9282 0.6471 1.4223 0.0008  -0.3690 0.2460  29  THR   U N   
36041 C  CA  . THR   U  38  ? 1.9270 0.6986 1.4005 0.0119  -0.3908 0.2779  29  THR   U CA  
36042 C  C   . THR   U  38  ? 1.9232 0.6249 1.3568 0.0347  -0.4471 0.2656  29  THR   U C   
36043 O  O   . THR   U  38  ? 1.9149 0.5718 1.3535 0.0657  -0.4503 0.2817  29  THR   U O   
36044 C  CB  . THR   U  38  ? 1.9495 0.7269 1.3676 0.0124  -0.3830 0.2368  29  THR   U CB  
36045 O  OG1 . THR   U  38  ? 1.9550 0.8341 1.3432 0.0533  -0.3208 0.2711  29  THR   U OG1 
36046 C  CG2 . THR   U  38  ? 1.9270 0.7251 1.3494 0.0199  -0.4065 0.2444  29  THR   U CG2 
36047 N  N   . ASN   U  39  ? 1.9572 0.6642 1.3659 0.0128  -0.4461 0.2143  30  ASN   U N   
36048 C  CA  . ASN   U  39  ? 1.9712 0.6612 1.3477 0.0129  -0.4428 0.2042  30  ASN   U CA  
36049 C  C   . ASN   U  39  ? 1.9647 0.7083 1.3477 -0.0087 -0.4312 0.1915  30  ASN   U C   
36050 O  O   . ASN   U  39  ? 1.9969 0.7595 1.3438 -0.1144 -0.3750 0.2460  30  ASN   U O   
36051 C  CB  . ASN   U  39  ? 2.0201 0.5792 1.3531 0.0104  -0.4256 0.1892  30  ASN   U CB  
36052 C  CG  . ASN   U  39  ? 2.0493 0.4979 1.3810 0.0401  -0.4238 0.1654  30  ASN   U CG  
36053 O  OD1 . ASN   U  39  ? 2.0476 0.5997 1.3667 0.0744  -0.4363 0.1173  30  ASN   U OD1 
36054 N  ND2 . ASN   U  39  ? 2.0842 0.4519 1.3823 0.0594  -0.4518 0.1360  30  ASN   U ND2 
36055 N  N   . ILE   U  40  ? 1.9505 0.7184 1.3614 0.0049  -0.4731 0.1545  31  ILE   U N   
36056 C  CA  . ILE   U  40  ? 1.9665 0.7813 1.3838 0.0238  -0.4746 0.1211  31  ILE   U CA  
36057 C  C   . ILE   U  40  ? 1.9415 0.7071 1.4644 -0.0219 -0.4202 0.0822  31  ILE   U C   
36058 O  O   . ILE   U  40  ? 1.9367 0.7412 1.5278 -0.0055 -0.5133 0.0154  31  ILE   U O   
36059 C  CB  . ILE   U  40  ? 1.9549 0.8423 1.4374 -0.0172 -0.4611 0.0703  31  ILE   U CB  
36060 C  CG1 . ILE   U  40  ? 1.9588 0.9080 1.4499 0.0461  -0.4598 0.1166  31  ILE   U CG1 
36061 C  CG2 . ILE   U  40  ? 1.9666 0.9082 1.4604 -0.0345 -0.4467 0.0059  31  ILE   U CG2 
36062 C  CD1 . ILE   U  40  ? 1.9790 0.9284 1.4619 0.0451  -0.4330 0.1444  31  ILE   U CD1 
36063 N  N   . ASN   U  41  ? 1.9942 0.6444 1.3830 -0.0077 -0.4556 0.1635  32  ASN   U N   
36064 C  CA  . ASN   U  41  ? 2.0035 0.6612 1.4319 0.0176  -0.4319 0.1708  32  ASN   U CA  
36065 C  C   . ASN   U  41  ? 2.0573 0.6378 1.4790 -0.0420 -0.3899 0.1549  32  ASN   U C   
36066 O  O   . ASN   U  41  ? 2.0091 0.4940 1.4817 -0.0096 -0.3999 0.1853  32  ASN   U O   
36067 C  CB  . ASN   U  41  ? 2.0176 0.6894 1.4481 0.0352  -0.4519 0.2260  32  ASN   U CB  
36068 C  CG  . ASN   U  41  ? 2.0212 0.7124 1.4881 0.0644  -0.4588 0.2075  32  ASN   U CG  
36069 O  OD1 . ASN   U  41  ? 2.0083 0.6885 1.4685 0.0558  -0.4769 0.3404  32  ASN   U OD1 
36070 N  ND2 . ASN   U  41  ? 1.9882 0.8611 1.5160 0.1081  -0.4959 0.2017  32  ASN   U ND2 
36071 N  N   . SER   U  42  ? 2.0723 0.6007 1.5085 -0.0251 -0.3678 0.1428  33  SER   U N   
36072 C  CA  . SER   U  42  ? 2.1010 0.6055 1.5029 -0.0710 -0.2878 0.1075  33  SER   U CA  
36073 C  C   . SER   U  42  ? 2.0889 0.5509 1.4907 -0.0410 -0.2684 0.0735  33  SER   U C   
36074 O  O   . SER   U  42  ? 2.0174 0.5468 1.5334 -0.0861 -0.2671 0.1352  33  SER   U O   
36075 C  CB  . SER   U  42  ? 2.2243 0.5762 1.5397 -0.1328 -0.2142 0.0705  33  SER   U CB  
36076 O  OG  . SER   U  42  ? 2.2695 0.5047 1.4686 -0.2330 -0.1763 0.0642  33  SER   U OG  
36077 N  N   . LEU   U  43  ? 2.0251 0.5720 1.4961 -0.0158 -0.2757 0.0844  34  LEU   U N   
36078 C  CA  . LEU   U  43  ? 2.0039 0.5441 1.4715 -0.0342 -0.3189 0.1155  34  LEU   U CA  
36079 C  C   . LEU   U  43  ? 1.9464 0.5425 1.4209 -0.0198 -0.3749 0.1453  34  LEU   U C   
36080 O  O   . LEU   U  43  ? 2.0615 0.5194 1.4771 -0.0871 -0.3517 0.1125  34  LEU   U O   
36081 C  CB  . LEU   U  43  ? 2.0050 0.4884 1.5100 -0.0026 -0.3276 0.1307  34  LEU   U CB  
36082 C  CG  . LEU   U  43  ? 2.0143 0.5037 1.5277 -0.0149 -0.3149 0.1280  34  LEU   U CG  
36083 C  CD1 . LEU   U  43  ? 2.0198 0.5113 1.5275 -0.0307 -0.3083 0.1282  34  LEU   U CD1 
36084 C  CD2 . LEU   U  43  ? 2.0133 0.5405 1.5229 -0.0147 -0.2936 0.1084  34  LEU   U CD2 
36085 N  N   . ALA   U  44  ? 1.9711 0.4816 1.3679 0.0002  -0.3728 0.1966  35  ALA   U N   
36086 C  CA  . ALA   U  44  ? 1.9049 0.4974 1.3411 0.0073  -0.3662 0.2088  35  ALA   U CA  
36087 C  C   . ALA   U  44  ? 1.9156 0.4426 1.3395 0.0220  -0.3458 0.2174  35  ALA   U C   
36088 O  O   . ALA   U  44  ? 1.9288 0.3509 1.3702 0.0052  -0.2988 0.2404  35  ALA   U O   
36089 C  CB  . ALA   U  44  ? 1.8725 0.5187 1.3394 -0.0045 -0.3788 0.2155  35  ALA   U CB  
36090 N  N   . VAL   U  45  ? 1.8967 0.4662 1.3392 0.0508  -0.3358 0.2259  36  VAL   U N   
36091 C  CA  . VAL   U  45  ? 1.8963 0.4541 1.3582 0.0473  -0.3251 0.2536  36  VAL   U CA  
36092 C  C   . VAL   U  45  ? 1.8748 0.4598 1.3502 0.0391  -0.3241 0.2366  36  VAL   U C   
36093 O  O   . VAL   U  45  ? 1.9169 0.2988 1.3719 0.0795  -0.3371 0.2162  36  VAL   U O   
36094 C  CB  . VAL   U  45  ? 1.8775 0.4407 1.3902 0.0602  -0.3241 0.2744  36  VAL   U CB  
36095 C  CG1 . VAL   U  45  ? 1.8933 0.4595 1.4269 0.0526  -0.3375 0.2428  36  VAL   U CG1 
36096 C  CG2 . VAL   U  45  ? 1.8789 0.4024 1.3765 0.0815  -0.3191 0.2651  36  VAL   U CG2 
36097 N  N   . ARG   U  46  ? 1.8863 0.5459 1.3403 0.0601  -0.3036 0.2554  37  ARG   U N   
36098 C  CA  . ARG   U  46  ? 1.8869 0.5493 1.3718 0.0511  -0.2934 0.2355  37  ARG   U CA  
36099 C  C   . ARG   U  46  ? 1.9145 0.6624 1.4163 0.0451  -0.2514 0.2447  37  ARG   U C   
36100 O  O   . ARG   U  46  ? 1.8836 0.6380 1.4744 0.0651  -0.2457 0.2152  37  ARG   U O   
36101 C  CB  . ARG   U  46  ? 1.8865 0.5238 1.4038 0.0479  -0.2983 0.2656  37  ARG   U CB  
36102 C  CG  . ARG   U  46  ? 1.8783 0.4778 1.3994 0.0575  -0.3118 0.3086  37  ARG   U CG  
36103 C  CD  . ARG   U  46  ? 1.9132 0.4723 1.4279 0.0587  -0.3248 0.3501  37  ARG   U CD  
36104 N  NE  . ARG   U  46  ? 1.9274 0.4741 1.4353 0.0498  -0.3404 0.3706  37  ARG   U NE  
36105 C  CZ  . ARG   U  46  ? 1.9447 0.5111 1.4680 0.0588  -0.3607 0.3562  37  ARG   U CZ  
36106 N  NH1 . ARG   U  46  ? 1.9604 0.5163 1.5131 0.0241  -0.3434 0.3762  37  ARG   U NH1 
36107 N  NH2 . ARG   U  46  ? 1.9908 0.4722 1.4574 0.0455  -0.3451 0.3709  37  ARG   U NH2 
36108 N  N   . GLY   U  47  ? 1.9572 0.6927 1.4601 -0.0024 -0.2702 0.2303  38  GLY   U N   
36109 C  CA  . GLY   U  47  ? 1.9810 0.6722 1.4615 0.0211  -0.2739 0.2266  38  GLY   U CA  
36110 C  C   . GLY   U  47  ? 2.0305 0.5965 1.4832 0.0241  -0.2777 0.2132  38  GLY   U C   
36111 O  O   . GLY   U  47  ? 2.0060 0.5473 1.5118 0.0716  -0.3034 0.2320  38  GLY   U O   
36112 N  N   . LYS   U  48  ? 2.0728 0.7022 1.4765 0.0253  -0.2698 0.1801  39  LYS   U N   
36113 C  CA  . LYS   U  48  ? 2.0679 0.7813 1.5165 0.0674  -0.2446 0.1210  39  LYS   U CA  
36114 C  C   . LYS   U  48  ? 2.1642 0.6659 1.4535 0.1158  -0.2904 0.1184  39  LYS   U C   
36115 O  O   . LYS   U  48  ? 2.2893 0.5023 1.4681 0.1417  -0.2937 0.0869  39  LYS   U O   
36116 C  CB  . LYS   U  48  ? 2.1174 0.9949 1.5606 0.0482  -0.2024 0.0677  39  LYS   U CB  
36117 C  CG  . LYS   U  48  ? 2.0879 1.1072 1.6984 0.0269  -0.1806 0.0731  39  LYS   U CG  
36118 C  CD  . LYS   U  48  ? 2.0968 1.2076 1.7348 0.0615  -0.1293 0.0829  39  LYS   U CD  
36119 C  CE  . LYS   U  48  ? 2.0650 1.2810 1.8448 0.0637  -0.0954 0.0020  39  LYS   U CE  
36120 N  NZ  . LYS   U  48  ? 2.0425 1.3808 1.9243 0.0702  -0.0830 -0.0157 39  LYS   U NZ  
36121 N  N   . ASP   U  49  ? 2.1489 0.7010 1.4715 0.0966  -0.2666 0.0851  40  ASP   U N   
36122 C  CA  . ASP   U  49  ? 2.0934 0.7902 1.4706 0.0428  -0.2355 0.0960  40  ASP   U CA  
36123 C  C   . ASP   U  49  ? 2.0876 0.6866 1.4174 0.0729  -0.2600 0.0891  40  ASP   U C   
36124 O  O   . ASP   U  49  ? 2.0260 0.8630 1.3537 0.0488  -0.2124 0.1768  40  ASP   U O   
36125 C  CB  . ASP   U  49  ? 2.1220 1.0188 1.4723 -0.0108 -0.2332 0.0574  40  ASP   U CB  
36126 C  CG  . ASP   U  49  ? 2.1125 1.2837 1.4972 -0.0142 -0.1664 -0.0296 40  ASP   U CG  
36127 O  OD1 . ASP   U  49  ? 2.1116 1.5406 1.5213 -0.0278 -0.1630 -0.0528 40  ASP   U OD1 
36128 O  OD2 . ASP   U  49  ? 2.1079 1.5787 1.5381 -0.0730 -0.1716 -0.1461 40  ASP   U OD2 
36129 N  N   . CYS   U  50  ? 2.1039 0.6634 1.3782 0.0242  -0.2351 0.0635  41  CYS   U N   
36130 C  CA  . CYS   U  50  ? 2.0847 0.6985 1.3339 -0.0115 -0.2605 0.0820  41  CYS   U CA  
36131 C  C   . CYS   U  50  ? 2.1234 0.6383 1.3700 -0.0043 -0.2368 0.1008  41  CYS   U C   
36132 O  O   . CYS   U  50  ? 2.1524 0.5441 1.3905 0.0053  -0.2351 0.1119  41  CYS   U O   
36133 C  CB  . CYS   U  50  ? 2.1139 0.7946 1.3304 -0.0163 -0.2886 0.0678  41  CYS   U CB  
36134 S  SG  . CYS   U  50  ? 2.1193 0.8876 1.2515 -0.0003 -0.3501 0.1388  41  CYS   U SG  
36135 N  N   . THR   U  51  ? 2.1123 0.4383 1.3796 0.0077  -0.2456 0.0682  42  THR   U N   
36136 C  CA  . THR   U  51  ? 2.1156 0.3458 1.4502 -0.0071 -0.2731 0.0805  42  THR   U CA  
36137 C  C   . THR   U  51  ? 2.0662 0.3654 1.4714 -0.0464 -0.2670 0.0519  42  THR   U C   
36138 O  O   . THR   U  51  ? 2.1685 0.1402 1.4685 -0.0094 -0.2805 0.0470  42  THR   U O   
36139 C  CB  . THR   U  51  ? 2.1400 0.2960 1.4366 -0.0168 -0.2859 0.0470  42  THR   U CB  
36140 O  OG1 . THR   U  51  ? 2.1371 0.2772 1.4308 -0.0145 -0.2737 -0.0190 42  THR   U OG1 
36141 C  CG2 . THR   U  51  ? 2.1315 0.3530 1.4046 0.0335  -0.2911 0.0328  42  THR   U CG2 
36142 N  N   . VAL   U  52  ? 2.0805 0.4381 1.4692 0.0674  -0.2819 0.1298  43  VAL   U N   
36143 C  CA  . VAL   U  52  ? 2.0547 0.5011 1.4633 0.0624  -0.2925 0.1021  43  VAL   U CA  
36144 C  C   . VAL   U  52  ? 2.0121 0.4160 1.4755 0.0333  -0.3015 0.1140  43  VAL   U C   
36145 O  O   . VAL   U  52  ? 2.0425 0.3502 1.5298 0.0315  -0.2842 0.1085  43  VAL   U O   
36146 C  CB  . VAL   U  52  ? 2.0638 0.5565 1.4676 0.1111  -0.2968 0.1242  43  VAL   U CB  
36147 C  CG1 . VAL   U  52  ? 2.0636 0.5747 1.4907 0.1223  -0.3035 0.1211  43  VAL   U CG1 
36148 C  CG2 . VAL   U  52  ? 2.0923 0.5974 1.4887 0.1161  -0.2989 0.0910  43  VAL   U CG2 
36149 N  N   . VAL   U  53  ? 1.9909 0.3662 1.4312 -0.0188 -0.3431 0.0785  44  VAL   U N   
36150 C  CA  . VAL   U  53  ? 1.9723 0.3956 1.3893 -0.0331 -0.3681 0.0604  44  VAL   U CA  
36151 C  C   . VAL   U  53  ? 1.9686 0.4606 1.3643 -0.0808 -0.4200 0.0460  44  VAL   U C   
36152 O  O   . VAL   U  53  ? 1.9836 0.3653 1.3153 -0.0715 -0.4302 0.1096  44  VAL   U O   
36153 C  CB  . VAL   U  53  ? 1.9830 0.4074 1.3843 -0.0518 -0.3699 0.0556  44  VAL   U CB  
36154 C  CG1 . VAL   U  53  ? 1.9864 0.4023 1.3550 -0.0486 -0.3736 0.0430  44  VAL   U CG1 
36155 C  CG2 . VAL   U  53  ? 1.9927 0.4875 1.3513 -0.0277 -0.3405 0.0558  44  VAL   U CG2 
36156 N  N   . ILE   U  54  ? 1.9693 0.4660 1.4323 -0.0700 -0.4228 0.0529  45  ILE   U N   
36157 C  CA  . ILE   U  54  ? 1.9555 0.4838 1.4264 -0.0618 -0.4015 0.0492  45  ILE   U CA  
36158 C  C   . ILE   U  54  ? 1.9123 0.4239 1.4966 -0.0357 -0.4201 0.0348  45  ILE   U C   
36159 O  O   . ILE   U  54  ? 1.8412 0.3018 1.5086 -0.0117 -0.3600 -0.0209 45  ILE   U O   
36160 C  CB  . ILE   U  54  ? 2.0177 0.4897 1.4378 -0.0957 -0.4066 0.0679  45  ILE   U CB  
36161 C  CG1 . ILE   U  54  ? 2.0479 0.4279 1.4558 -0.0971 -0.4029 0.1295  45  ILE   U CG1 
36162 C  CG2 . ILE   U  54  ? 2.0476 0.5316 1.4178 -0.0969 -0.3824 0.0655  45  ILE   U CG2 
36163 C  CD1 . ILE   U  54  ? 2.0834 0.4452 1.4625 -0.0771 -0.4073 0.1435  45  ILE   U CD1 
36164 N  N   . SER   U  55  ? 1.9403 0.3801 1.5308 0.0454  -0.4076 0.0430  46  SER   U N   
36165 C  CA  . SER   U  55  ? 1.9904 0.3736 1.5372 0.0460  -0.3778 0.0620  46  SER   U CA  
36166 C  C   . SER   U  55  ? 2.0464 0.3912 1.4579 -0.0080 -0.4139 0.0923  46  SER   U C   
36167 O  O   . SER   U  55  ? 2.1061 0.4200 1.4486 -0.0622 -0.3910 0.0830  46  SER   U O   
36168 C  CB  . SER   U  55  ? 1.9888 0.3461 1.6025 0.1112  -0.3789 0.1282  46  SER   U CB  
36169 O  OG  . SER   U  55  ? 1.9637 0.4030 1.7304 0.1467  -0.3414 0.1355  46  SER   U OG  
36170 N  N   . GLN   U  56  ? 2.0723 0.3673 1.4599 0.0203  -0.4083 0.1527  47  GLN   U N   
36171 C  CA  . GLN   U  56  ? 2.0857 0.4296 1.4514 0.0038  -0.4426 0.1703  47  GLN   U CA  
36172 C  C   . GLN   U  56  ? 2.1207 0.4045 1.4002 -0.0187 -0.4456 0.1913  47  GLN   U C   
36173 O  O   . GLN   U  56  ? 2.1625 0.3537 1.4098 -0.0028 -0.4651 0.1963  47  GLN   U O   
36174 C  CB  . GLN   U  56  ? 2.1087 0.4494 1.4819 -0.0134 -0.4542 0.1370  47  GLN   U CB  
36175 C  CG  . GLN   U  56  ? 2.1094 0.4351 1.5073 -0.0270 -0.4686 0.1163  47  GLN   U CG  
36176 C  CD  . GLN   U  56  ? 2.1079 0.4123 1.5261 -0.0069 -0.4914 0.1461  47  GLN   U CD  
36177 O  OE1 . GLN   U  56  ? 2.1399 0.3330 1.5586 0.0185  -0.4480 0.0225  47  GLN   U OE1 
36178 N  NE2 . GLN   U  56  ? 2.1512 0.3532 1.5769 0.0060  -0.4793 0.1625  47  GLN   U NE2 
36179 N  N   . LYS   U  57  ? 2.0960 0.4945 1.4321 -0.0377 -0.4527 0.1511  48  LYS   U N   
36180 C  CA  . LYS   U  57  ? 2.0644 0.5888 1.4662 -0.0135 -0.4171 0.1331  48  LYS   U CA  
36181 C  C   . LYS   U  57  ? 2.0366 0.6493 1.4454 0.0259  -0.3833 0.0868  48  LYS   U C   
36182 O  O   . LYS   U  57  ? 2.0661 0.7030 1.4705 0.0469  -0.4014 0.1148  48  LYS   U O   
36183 C  CB  . LYS   U  57  ? 2.0818 0.6054 1.4939 -0.0405 -0.4041 0.1179  48  LYS   U CB  
36184 C  CG  . LYS   U  57  ? 2.0765 0.6782 1.5352 -0.0526 -0.3967 0.0980  48  LYS   U CG  
36185 C  CD  . LYS   U  57  ? 2.0730 0.7596 1.5543 -0.0864 -0.3917 0.0366  48  LYS   U CD  
36186 C  CE  . LYS   U  57  ? 2.0564 0.8313 1.5755 -0.0942 -0.3933 -0.0148 48  LYS   U CE  
36187 N  NZ  . LYS   U  57  ? 2.0899 0.8718 1.5676 -0.1035 -0.3973 -0.0559 48  LYS   U NZ  
36188 N  N   . LYS   U  58  ? 2.0065 0.7310 1.4093 0.0247  -0.3910 0.0887  49  LYS   U N   
36189 C  CA  . LYS   U  58  ? 1.9850 0.7802 1.3881 0.0466  -0.3661 0.0654  49  LYS   U CA  
36190 C  C   . LYS   U  58  ? 1.9407 0.7844 1.3719 0.0983  -0.3597 0.0688  49  LYS   U C   
36191 O  O   . LYS   U  58  ? 1.9525 0.8090 1.3244 0.1525  -0.3428 0.0138  49  LYS   U O   
36192 C  CB  . LYS   U  58  ? 1.9796 0.8281 1.3696 0.0499  -0.3681 0.0451  49  LYS   U CB  
36193 C  CG  . LYS   U  58  ? 1.9783 0.8852 1.3615 0.0277  -0.3610 -0.0064 49  LYS   U CG  
36194 C  CD  . LYS   U  58  ? 1.9646 0.9049 1.3392 0.0072  -0.3601 -0.0072 49  LYS   U CD  
36195 C  CE  . LYS   U  58  ? 1.9707 0.8958 1.2982 -0.0243 -0.3848 -0.0473 49  LYS   U CE  
36196 N  NZ  . LYS   U  58  ? 1.9790 0.9725 1.2918 -0.0368 -0.4135 -0.0716 49  LYS   U NZ  
36197 N  N   . VAL   U  59  ? 1.8836 0.7904 1.4453 0.0756  -0.3768 0.0636  50  VAL   U N   
36198 C  CA  . VAL   U  59  ? 1.9108 0.8541 1.5118 0.0211  -0.3929 0.1102  50  VAL   U CA  
36199 C  C   . VAL   U  59  ? 1.9286 0.9093 1.5615 0.0384  -0.4636 0.1202  50  VAL   U C   
36200 O  O   . VAL   U  59  ? 1.9479 0.9882 1.5230 0.0138  -0.4691 0.0893  50  VAL   U O   
36201 C  CB  . VAL   U  59  ? 1.9003 0.8117 1.4682 0.0256  -0.3840 0.1568  50  VAL   U CB  
36202 C  CG1 . VAL   U  59  ? 1.8762 0.8618 1.4827 0.0472  -0.3805 0.1708  50  VAL   U CG1 
36203 C  CG2 . VAL   U  59  ? 1.8804 0.7911 1.4558 0.0041  -0.3791 0.2100  50  VAL   U CG2 
36204 N  N   . PRO   U  60  ? 1.9710 0.9694 1.6052 0.0363  -0.4490 0.0850  51  PRO   U N   
36205 C  CA  . PRO   U  60  ? 2.0606 0.9273 1.6872 0.0265  -0.4481 0.1515  51  PRO   U CA  
36206 C  C   . PRO   U  60  ? 2.0948 0.8727 1.6812 0.0078  -0.4882 0.1927  51  PRO   U C   
36207 O  O   . PRO   U  60  ? 2.3054 0.6006 1.6740 -0.1019 -0.4892 0.1998  51  PRO   U O   
36208 C  CB  . PRO   U  60  ? 2.0089 0.9355 1.6850 0.0621  -0.4296 0.1479  51  PRO   U CB  
36209 C  CG  . PRO   U  60  ? 1.9797 1.0002 1.6374 0.0733  -0.4357 0.1657  51  PRO   U CG  
36210 C  CD  . PRO   U  60  ? 1.9733 1.0227 1.6141 0.0452  -0.4444 0.1327  51  PRO   U CD  
36211 N  N   . ASP   U  61  ? 2.1990 0.9346 1.7640 -0.0244 -0.3889 0.1961  52  ASP   U N   
36212 C  CA  . ASP   U  61  ? 2.1912 0.9761 1.7878 -0.0004 -0.3725 0.2358  52  ASP   U CA  
36213 C  C   . ASP   U  61  ? 2.2067 0.8640 1.7077 0.0727  -0.3463 0.3233  52  ASP   U C   
36214 O  O   . ASP   U  61  ? 2.2737 0.7001 1.6707 0.0617  -0.3352 0.4623  52  ASP   U O   
36215 C  CB  . ASP   U  61  ? 2.2743 0.9181 1.7982 -0.0052 -0.3454 0.2110  52  ASP   U CB  
36216 C  CG  . ASP   U  61  ? 2.2829 0.9607 1.8238 -0.0403 -0.3362 0.1917  52  ASP   U CG  
36217 O  OD1 . ASP   U  61  ? 2.2688 1.1737 1.9334 -0.1074 -0.4384 0.1600  52  ASP   U OD1 
36218 O  OD2 . ASP   U  61  ? 2.3279 0.7248 1.7932 -0.0591 -0.3597 0.1803  52  ASP   U OD2 
36219 N  N   . LYS   U  62  ? 2.2343 0.9414 1.6640 0.0346  -0.3579 0.3616  53  LYS   U N   
36220 C  CA  . LYS   U  62  ? 2.2026 0.8628 1.6746 0.0160  -0.3654 0.3739  53  LYS   U CA  
36221 C  C   . LYS   U  62  ? 2.2310 0.7235 1.6203 0.1046  -0.3892 0.3295  53  LYS   U C   
36222 O  O   . LYS   U  62  ? 2.2379 0.4619 1.6879 0.0867  -0.3255 0.3849  53  LYS   U O   
36223 C  CB  . LYS   U  62  ? 2.1994 1.0200 1.6844 0.0407  -0.3949 0.4133  53  LYS   U CB  
36224 C  CG  . LYS   U  62  ? 2.1877 1.0836 1.7147 0.0148  -0.3632 0.4404  53  LYS   U CG  
36225 C  CD  . LYS   U  62  ? 2.1955 1.2180 1.7535 0.0140  -0.3633 0.5292  53  LYS   U CD  
36226 C  CE  . LYS   U  62  ? 2.1848 1.2633 1.7769 0.0302  -0.3643 0.5271  53  LYS   U CE  
36227 N  NZ  . LYS   U  62  ? 2.1958 1.4720 1.7928 0.0023  -0.4031 0.5702  53  LYS   U NZ  
36228 N  N   . LEU   U  63  ? 2.1558 0.6523 1.6359 0.1202  -0.4154 0.3823  54  LEU   U N   
36229 C  CA  . LEU   U  63  ? 2.1081 0.6858 1.6643 0.0831  -0.4597 0.3512  54  LEU   U CA  
36230 C  C   . LEU   U  63  ? 2.0125 0.7045 1.6711 0.0827  -0.4978 0.2677  54  LEU   U C   
36231 O  O   . LEU   U  63  ? 1.9130 0.7002 1.6724 0.1064  -0.5443 0.2590  54  LEU   U O   
36232 C  CB  . LEU   U  63  ? 2.0774 0.6688 1.6760 0.1336  -0.4611 0.4260  54  LEU   U CB  
36233 C  CG  . LEU   U  63  ? 2.0697 0.7344 1.6818 0.1312  -0.4998 0.4684  54  LEU   U CG  
36234 C  CD1 . LEU   U  63  ? 2.0732 0.7724 1.6796 0.1260  -0.4818 0.5323  54  LEU   U CD1 
36235 C  CD2 . LEU   U  63  ? 2.0579 0.7416 1.7157 0.1117  -0.5158 0.4435  54  LEU   U CD2 
36236 N  N   . LEU   U  64  ? 2.0181 0.7444 1.6811 0.0718  -0.4916 0.2365  55  LEU   U N   
36237 C  CA  . LEU   U  64  ? 2.0911 0.6870 1.6007 0.0581  -0.4763 0.2768  55  LEU   U CA  
36238 C  C   . LEU   U  64  ? 2.0951 0.7688 1.4980 0.0590  -0.4831 0.3089  55  LEU   U C   
36239 O  O   . LEU   U  64  ? 2.0779 0.8014 1.4361 0.0141  -0.5386 0.2567  55  LEU   U O   
36240 C  CB  . LEU   U  64  ? 2.1078 0.7342 1.5754 0.0434  -0.4897 0.2808  55  LEU   U CB  
36241 C  CG  . LEU   U  64  ? 2.1679 0.8699 1.5312 0.0587  -0.4696 0.3133  55  LEU   U CG  
36242 C  CD1 . LEU   U  64  ? 2.1581 0.9759 1.5593 0.0313  -0.4485 0.3317  55  LEU   U CD1 
36243 C  CD2 . LEU   U  64  ? 2.1284 0.7338 1.5903 -0.0004 -0.4487 0.2767  55  LEU   U CD2 
36244 N  N   . ASP   U  65  ? 2.0900 0.7544 1.5103 0.0794  -0.4331 0.2655  56  ASP   U N   
36245 C  CA  . ASP   U  65  ? 2.0744 0.7534 1.4532 0.0526  -0.4516 0.2564  56  ASP   U CA  
36246 C  C   . ASP   U  65  ? 2.0655 0.6451 1.4137 0.0363  -0.4113 0.3002  56  ASP   U C   
36247 O  O   . ASP   U  65  ? 2.0096 0.4025 1.4787 0.0802  -0.3586 0.3754  56  ASP   U O   
36248 C  CB  . ASP   U  65  ? 2.0790 0.7380 1.4435 0.0666  -0.4428 0.2223  56  ASP   U CB  
36249 C  CG  . ASP   U  65  ? 2.0876 0.8386 1.4525 0.1326  -0.4604 0.1905  56  ASP   U CG  
36250 O  OD1 . ASP   U  65  ? 2.0924 0.8363 1.4085 0.1692  -0.4849 0.2217  56  ASP   U OD1 
36251 O  OD2 . ASP   U  65  ? 2.0762 0.7785 1.4373 0.1993  -0.4819 0.1278  56  ASP   U OD2 
36252 N  N   . PRO   U  66  ? 2.0666 0.7310 1.3614 0.0119  -0.4524 0.3151  57  PRO   U N   
36253 C  CA  . PRO   U  66  ? 2.0598 0.6829 1.3850 0.0284  -0.4328 0.3446  57  PRO   U CA  
36254 C  C   . PRO   U  66  ? 2.0689 0.5923 1.4497 -0.0165 -0.4166 0.3557  57  PRO   U C   
36255 O  O   . PRO   U  66  ? 2.0219 0.4852 1.4973 0.0134  -0.3978 0.3848  57  PRO   U O   
36256 C  CB  . PRO   U  66  ? 2.1023 0.7561 1.3453 0.0234  -0.4590 0.3436  57  PRO   U CB  
36257 C  CG  . PRO   U  66  ? 2.1077 0.8002 1.3446 0.0009  -0.4576 0.3472  57  PRO   U CG  
36258 C  CD  . PRO   U  66  ? 2.0817 0.7755 1.3698 0.0023  -0.4649 0.3357  57  PRO   U CD  
36259 N  N   . THR   U  67  ? 2.0482 0.5707 1.4491 -0.0206 -0.4376 0.3970  58  THR   U N   
36260 C  CA  . THR   U  67  ? 2.0008 0.6034 1.3729 -0.0149 -0.4642 0.4022  58  THR   U CA  
36261 C  C   . THR   U  67  ? 1.9155 0.4487 1.4151 0.0637  -0.5220 0.4319  58  THR   U C   
36262 O  O   . THR   U  67  ? 1.9969 0.4115 1.3461 0.0343  -0.5550 0.4611  58  THR   U O   
36263 C  CB  . THR   U  67  ? 1.9916 0.6695 1.3783 -0.0474 -0.4469 0.3708  58  THR   U CB  
36264 O  OG1 . THR   U  67  ? 1.9729 0.7246 1.4698 -0.0891 -0.4928 0.3386  58  THR   U OG1 
36265 C  CG2 . THR   U  67  ? 1.9696 0.7555 1.3572 -0.0673 -0.4526 0.3348  58  THR   U CG2 
36266 N  N   . THR   U  68  ? 1.9462 0.4609 1.3177 0.0486  -0.5380 0.4445  59  THR   U N   
36267 C  CA  . THR   U  68  ? 1.9097 0.4350 1.3155 0.0444  -0.5338 0.4389  59  THR   U CA  
36268 C  C   . THR   U  68  ? 1.9222 0.4910 1.3208 0.0539  -0.5173 0.3740  59  THR   U C   
36269 O  O   . THR   U  68  ? 1.9202 0.4251 1.2895 0.0042  -0.4873 0.3308  59  THR   U O   
36270 C  CB  . THR   U  68  ? 1.9007 0.4489 1.3449 0.0679  -0.5405 0.4735  59  THR   U CB  
36271 O  OG1 . THR   U  68  ? 1.8730 0.4417 1.3850 0.0554  -0.5422 0.4520  59  THR   U OG1 
36272 C  CG2 . THR   U  68  ? 1.9136 0.5320 1.3277 0.0574  -0.5555 0.4546  59  THR   U CG2 
36273 N  N   . VAL   U  69  ? 1.9377 0.5401 1.2759 0.0084  -0.4733 0.3698  60  VAL   U N   
36274 C  CA  . VAL   U  69  ? 1.9330 0.5987 1.2867 0.0131  -0.4635 0.3232  60  VAL   U CA  
36275 C  C   . VAL   U  69  ? 1.9438 0.6335 1.2782 -0.0024 -0.4067 0.2741  60  VAL   U C   
36276 O  O   . VAL   U  69  ? 1.9707 0.6863 1.2477 -0.0176 -0.4045 0.1979  60  VAL   U O   
36277 C  CB  . VAL   U  69  ? 1.9525 0.6330 1.2911 0.0441  -0.4688 0.3544  60  VAL   U CB  
36278 C  CG1 . VAL   U  69  ? 1.9173 0.6551 1.3088 0.0667  -0.4902 0.3410  60  VAL   U CG1 
36279 C  CG2 . VAL   U  69  ? 1.9476 0.6323 1.2696 0.0378  -0.4778 0.3873  60  VAL   U CG2 
36280 N  N   . SER   U  70  ? 1.9167 0.6196 1.2899 0.0090  -0.4101 0.2524  61  SER   U N   
36281 C  CA  . SER   U  70  ? 1.9096 0.6274 1.3458 -0.0077 -0.3483 0.1966  61  SER   U CA  
36282 C  C   . SER   U  70  ? 1.8623 0.6046 1.3954 -0.0163 -0.3726 0.1666  61  SER   U C   
36283 O  O   . SER   U  70  ? 1.9541 0.5802 1.4093 0.0104  -0.3390 0.1759  61  SER   U O   
36284 C  CB  . SER   U  70  ? 1.9280 0.6709 1.3157 -0.0173 -0.3335 0.1447  61  SER   U CB  
36285 O  OG  . SER   U  70  ? 1.9236 0.7477 1.2887 -0.0240 -0.3008 0.1595  61  SER   U OG  
36286 N  N   . TYR   U  71  ? 1.8375 0.6005 1.3691 0.0052  -0.3758 0.1777  62  TYR   U N   
36287 C  CA  . TYR   U  71  ? 1.7879 0.4798 1.3772 0.0611  -0.3782 0.1983  62  TYR   U CA  
36288 C  C   . TYR   U  71  ? 1.8219 0.3631 1.3543 0.0488  -0.3766 0.1879  62  TYR   U C   
36289 O  O   . TYR   U  71  ? 1.8127 0.3948 1.3698 0.0641  -0.3720 0.1861  62  TYR   U O   
36290 C  CB  . TYR   U  71  ? 1.7868 0.4685 1.3651 0.0844  -0.3826 0.2001  62  TYR   U CB  
36291 C  CG  . TYR   U  71  ? 1.7939 0.3593 1.3349 0.1160  -0.4332 0.2592  62  TYR   U CG  
36292 C  CD1 . TYR   U  71  ? 1.8335 0.3442 1.3057 0.1138  -0.4331 0.2763  62  TYR   U CD1 
36293 C  CD2 . TYR   U  71  ? 1.7948 0.3203 1.3446 0.1282  -0.4088 0.2584  62  TYR   U CD2 
36294 C  CE1 . TYR   U  71  ? 1.8206 0.3919 1.2965 0.1266  -0.4580 0.2654  62  TYR   U CE1 
36295 C  CE2 . TYR   U  71  ? 1.8091 0.2754 1.3287 0.1421  -0.4274 0.2728  62  TYR   U CE2 
36296 C  CZ  . TYR   U  71  ? 1.8198 0.3343 1.3053 0.1329  -0.4488 0.2655  62  TYR   U CZ  
36297 O  OH  . TYR   U  71  ? 1.7798 0.3230 1.3307 0.1507  -0.5065 0.2766  62  TYR   U OH  
36298 N  N   . ILE   U  72  ? 1.7945 0.3592 1.3409 0.0216  -0.3893 0.1895  63  ILE   U N   
36299 C  CA  . ILE   U  72  ? 1.7914 0.3568 1.3049 -0.0022 -0.3506 0.1557  63  ILE   U CA  
36300 C  C   . ILE   U  72  ? 1.7808 0.3257 1.2902 0.0243  -0.3834 0.1615  63  ILE   U C   
36301 O  O   . ILE   U  72  ? 1.7776 0.1274 1.2972 0.0141  -0.3666 0.1744  63  ILE   U O   
36302 C  CB  . ILE   U  72  ? 1.8541 0.4109 1.3006 0.0109  -0.3388 0.1721  63  ILE   U CB  
36303 C  CG1 . ILE   U  72  ? 1.8888 0.3600 1.2591 0.0639  -0.3306 0.2016  63  ILE   U CG1 
36304 C  CG2 . ILE   U  72  ? 1.8669 0.4009 1.3079 0.0094  -0.3362 0.1669  63  ILE   U CG2 
36305 C  CD1 . ILE   U  72  ? 1.9136 0.3880 1.2679 0.0791  -0.3157 0.2037  63  ILE   U CD1 
36306 N  N   . PHE   U  73  ? 1.7663 0.3609 1.2743 -0.0006 -0.4175 0.1637  64  PHE   U N   
36307 C  CA  . PHE   U  73  ? 1.7684 0.3977 1.2541 -0.0327 -0.4298 0.1818  64  PHE   U CA  
36308 C  C   . PHE   U  73  ? 1.8381 0.3050 1.3295 -0.0269 -0.4388 0.2045  64  PHE   U C   
36309 O  O   . PHE   U  73  ? 1.8431 0.1148 1.3592 -0.0209 -0.4502 0.2248  64  PHE   U O   
36310 C  CB  . PHE   U  73  ? 1.7084 0.4459 1.2425 -0.0372 -0.4387 0.1663  64  PHE   U CB  
36311 C  CG  . PHE   U  73  ? 1.6720 0.4727 1.1774 -0.0393 -0.4568 0.1624  64  PHE   U CG  
36312 C  CD1 . PHE   U  73  ? 1.6617 0.5113 1.1510 -0.0338 -0.4666 0.1642  64  PHE   U CD1 
36313 C  CD2 . PHE   U  73  ? 1.6747 0.4545 1.1884 -0.0108 -0.4653 0.1717  64  PHE   U CD2 
36314 C  CE1 . PHE   U  73  ? 1.6591 0.4811 1.1691 -0.0497 -0.4590 0.1692  64  PHE   U CE1 
36315 C  CE2 . PHE   U  73  ? 1.6678 0.4912 1.2109 -0.0087 -0.4547 0.1640  64  PHE   U CE2 
36316 C  CZ  . PHE   U  73  ? 1.6815 0.4739 1.2007 -0.0350 -0.4615 0.1649  64  PHE   U CZ  
36317 N  N   . CYS   U  74  ? 1.9426 0.3657 1.3557 -0.0898 -0.4411 0.1706  65  CYS   U N   
36318 C  CA  . CYS   U  74  ? 1.9154 0.4293 1.4115 -0.0818 -0.4121 0.1249  65  CYS   U CA  
36319 C  C   . CYS   U  74  ? 1.9260 0.3488 1.4327 -0.1139 -0.4527 0.1135  65  CYS   U C   
36320 O  O   . CYS   U  74  ? 1.9311 0.4039 1.6377 -0.1591 -0.4516 0.0338  65  CYS   U O   
36321 C  CB  . CYS   U  74  ? 1.9205 0.5187 1.4304 -0.1378 -0.4326 0.1146  65  CYS   U CB  
36322 S  SG  . CYS   U  74  ? 1.9631 0.7237 1.4254 -0.1161 -0.4777 0.1480  65  CYS   U SG  
36323 N  N   . ILE   U  75  ? 1.9144 0.3827 1.3894 -0.1165 -0.4361 0.1184  66  ILE   U N   
36324 C  CA  . ILE   U  75  ? 1.8923 0.4604 1.3803 -0.1137 -0.4174 0.1325  66  ILE   U CA  
36325 C  C   . ILE   U  75  ? 1.8253 0.4440 1.3008 -0.1405 -0.3971 0.1705  66  ILE   U C   
36326 O  O   . ILE   U  75  ? 1.8583 0.3886 1.3657 -0.1379 -0.3727 0.1595  66  ILE   U O   
36327 C  CB  . ILE   U  75  ? 1.8787 0.5091 1.3923 -0.1080 -0.4158 0.1234  66  ILE   U CB  
36328 C  CG1 . ILE   U  75  ? 1.8801 0.5038 1.3951 -0.1057 -0.4025 0.1359  66  ILE   U CG1 
36329 C  CG2 . ILE   U  75  ? 1.8954 0.5643 1.3778 -0.0993 -0.3983 0.1208  66  ILE   U CG2 
36330 C  CD1 . ILE   U  75  ? 1.8843 0.4904 1.3969 -0.1041 -0.3954 0.1306  66  ILE   U CD1 
36331 N  N   . SER   U  76  ? 1.7943 0.4422 1.2805 -0.1429 -0.4115 0.1804  67  SER   U N   
36332 C  CA  . SER   U  76  ? 1.7830 0.4386 1.3497 -0.1715 -0.3987 0.1627  67  SER   U CA  
36333 C  C   . SER   U  76  ? 1.7963 0.4606 1.3540 -0.1496 -0.4033 0.1616  67  SER   U C   
36334 O  O   . SER   U  76  ? 1.7854 0.4507 1.4689 -0.1330 -0.4291 0.1742  67  SER   U O   
36335 C  CB  . SER   U  76  ? 1.7493 0.5214 1.3299 -0.1935 -0.3951 0.1567  67  SER   U CB  
36336 O  OG  . SER   U  76  ? 1.7686 0.5170 1.3569 -0.2117 -0.3850 0.1606  67  SER   U OG  
36337 N  N   . ARG   U  77  ? 1.8034 0.5073 1.3434 -0.1306 -0.3752 0.1349  68  ARG   U N   
36338 C  CA  . ARG   U  77  ? 1.8421 0.5128 1.3450 -0.1167 -0.3672 0.1249  68  ARG   U CA  
36339 C  C   . ARG   U  77  ? 1.8395 0.4226 1.2748 -0.0884 -0.3642 0.0968  68  ARG   U C   
36340 O  O   . ARG   U  77  ? 1.8363 0.4282 1.2735 -0.1651 -0.3520 0.0928  68  ARG   U O   
36341 C  CB  . ARG   U  77  ? 1.9338 0.5255 1.4858 -0.0971 -0.3366 0.1071  68  ARG   U CB  
36342 C  CG  . ARG   U  77  ? 2.0657 0.6323 1.5152 -0.0707 -0.2739 0.0847  68  ARG   U CG  
36343 C  CD  . ARG   U  77  ? 2.2025 0.6494 1.6827 -0.0577 -0.2224 0.0444  68  ARG   U CD  
36344 N  NE  . ARG   U  77  ? 2.2026 0.8323 1.7720 -0.1092 -0.2187 0.0242  68  ARG   U NE  
36345 C  CZ  . ARG   U  77  ? 2.3542 0.8319 1.9032 -0.1452 -0.2048 -0.0037 68  ARG   U CZ  
36346 N  NH1 . ARG   U  77  ? 2.3864 0.8782 1.9955 -0.1164 -0.1660 -0.0699 68  ARG   U NH1 
36347 N  NH2 . ARG   U  77  ? 2.3339 0.9664 1.9425 -0.1606 -0.2163 -0.0249 68  ARG   U NH2 
36348 N  N   . THR   U  78  ? 1.8348 0.3707 1.2419 -0.0683 -0.3406 0.0656  69  THR   U N   
36349 C  CA  . THR   U  78  ? 1.8204 0.4280 1.2435 -0.0607 -0.3099 0.0520  69  THR   U CA  
36350 C  C   . THR   U  78  ? 1.8127 0.4185 1.2410 -0.0515 -0.3410 0.0671  69  THR   U C   
36351 O  O   . THR   U  78  ? 1.8351 0.3629 1.2022 -0.0435 -0.3490 0.0576  69  THR   U O   
36352 C  CB  . THR   U  78  ? 1.7878 0.4068 1.2552 -0.0489 -0.2794 0.0055  69  THR   U CB  
36353 O  OG1 . THR   U  78  ? 1.7962 0.3633 1.2525 -0.0504 -0.2613 -0.0182 69  THR   U OG1 
36354 C  CG2 . THR   U  78  ? 1.8082 0.4414 1.2702 -0.0470 -0.2631 -0.0244 69  THR   U CG2 
36355 N  N   . ILE   U  79  ? 1.8101 0.4923 1.2388 -0.0116 -0.3524 0.0848  70  ILE   U N   
36356 C  CA  . ILE   U  79  ? 1.8320 0.4930 1.2539 -0.0091 -0.3632 0.0833  70  ILE   U CA  
36357 C  C   . ILE   U  79  ? 1.8446 0.4673 1.2283 -0.0197 -0.3787 0.0844  70  ILE   U C   
36358 O  O   . ILE   U  79  ? 1.8718 0.3860 1.1223 -0.0304 -0.3997 0.0415  70  ILE   U O   
36359 C  CB  . ILE   U  79  ? 1.8436 0.5646 1.2618 0.0179  -0.3669 0.1130  70  ILE   U CB  
36360 C  CG1 . ILE   U  79  ? 1.8486 0.6489 1.3232 0.0434  -0.3585 0.1260  70  ILE   U CG1 
36361 C  CG2 . ILE   U  79  ? 1.8325 0.5549 1.2773 0.0096  -0.3703 0.1147  70  ILE   U CG2 
36362 C  CD1 . ILE   U  79  ? 1.8715 0.7144 1.3278 0.0364  -0.3461 0.1423  70  ILE   U CD1 
36363 N  N   . GLY   U  80  ? 1.8356 0.4747 1.2600 -0.0166 -0.3693 0.1034  71  GLY   U N   
36364 C  CA  . GLY   U  80  ? 1.8211 0.4689 1.3067 -0.0259 -0.3626 0.1232  71  GLY   U CA  
36365 C  C   . GLY   U  80  ? 1.7706 0.4557 1.3241 -0.0190 -0.3763 0.1268  71  GLY   U C   
36366 O  O   . GLY   U  80  ? 1.7918 0.4887 1.3008 -0.0005 -0.4165 0.1715  71  GLY   U O   
36367 N  N   . MET   U  81  ? 1.7685 0.4528 1.3688 -0.0352 -0.3521 0.1052  72  MET   U N   
36368 C  CA  . MET   U  81  ? 1.7811 0.4245 1.4038 -0.0666 -0.3504 0.0991  72  MET   U CA  
36369 C  C   . MET   U  81  ? 1.7604 0.4880 1.4018 -0.0529 -0.3660 0.1073  72  MET   U C   
36370 O  O   . MET   U  81  ? 1.8119 0.3260 1.3748 -0.1009 -0.3871 0.0666  72  MET   U O   
36371 C  CB  . MET   U  81  ? 1.8011 0.3575 1.4315 -0.0573 -0.3599 0.1321  72  MET   U CB  
36372 C  CG  . MET   U  81  ? 1.8403 0.3742 1.4857 -0.0578 -0.3603 0.1012  72  MET   U CG  
36373 S  SD  . MET   U  81  ? 1.8441 0.3854 1.5659 -0.0956 -0.3147 0.0700  72  MET   U SD  
36374 C  CE  . MET   U  81  ? 1.8452 0.3957 1.5516 -0.1195 -0.3279 0.0906  72  MET   U CE  
36375 N  N   . VAL   U  82  ? 1.7219 0.5071 1.3963 -0.0552 -0.3652 0.1703  73  VAL   U N   
36376 C  CA  . VAL   U  82  ? 1.7050 0.5180 1.3694 -0.0445 -0.3683 0.1315  73  VAL   U CA  
36377 C  C   . VAL   U  82  ? 1.7042 0.5167 1.3708 -0.0730 -0.4087 0.1092  73  VAL   U C   
36378 O  O   . VAL   U  82  ? 1.6862 0.4490 1.4100 -0.0407 -0.4172 0.0900  73  VAL   U O   
36379 C  CB  . VAL   U  82  ? 1.7127 0.5627 1.4184 -0.0400 -0.3487 0.1713  73  VAL   U CB  
36380 C  CG1 . VAL   U  82  ? 1.7126 0.5992 1.4255 -0.0432 -0.3412 0.1502  73  VAL   U CG1 
36381 C  CG2 . VAL   U  82  ? 1.7318 0.6018 1.4135 -0.0233 -0.3519 0.2036  73  VAL   U CG2 
36382 N  N   . VAL   U  83  ? 1.7211 0.5541 1.2771 -0.0786 -0.3877 0.0525  74  VAL   U N   
36383 C  CA  . VAL   U  83  ? 1.7677 0.5911 1.2479 -0.0821 -0.3891 0.0570  74  VAL   U CA  
36384 C  C   . VAL   U  83  ? 1.8534 0.5924 1.1836 -0.0936 -0.3831 0.0674  74  VAL   U C   
36385 O  O   . VAL   U  83  ? 1.8720 0.7451 1.1987 -0.1115 -0.4079 0.0819  74  VAL   U O   
36386 C  CB  . VAL   U  83  ? 1.7393 0.5958 1.2232 -0.0664 -0.3943 0.0338  74  VAL   U CB  
36387 C  CG1 . VAL   U  83  ? 1.7354 0.6221 1.2175 -0.0538 -0.3843 0.0463  74  VAL   U CG1 
36388 C  CG2 . VAL   U  83  ? 1.7264 0.5951 1.1948 -0.0418 -0.3965 0.0350  74  VAL   U CG2 
36389 N  N   . ASN   U  84  ? 1.8857 0.4848 1.1709 -0.0644 -0.3825 0.0974  75  ASN   U N   
36390 C  CA  . ASN   U  84  ? 1.9085 0.4712 1.2010 -0.0589 -0.3795 0.1002  75  ASN   U CA  
36391 C  C   . ASN   U  84  ? 1.8205 0.3235 1.2620 -0.0011 -0.3807 0.0893  75  ASN   U C   
36392 O  O   . ASN   U  84  ? 1.8448 0.2697 1.2903 0.0219  -0.4025 0.0430  75  ASN   U O   
36393 C  CB  . ASN   U  84  ? 1.9504 0.4637 1.2115 -0.0817 -0.3499 0.0944  75  ASN   U CB  
36394 C  CG  . ASN   U  84  ? 2.0187 0.5565 1.2450 -0.1102 -0.2988 0.0797  75  ASN   U CG  
36395 O  OD1 . ASN   U  84  ? 2.1022 0.5348 1.2991 -0.1721 -0.2700 0.0252  75  ASN   U OD1 
36396 N  ND2 . ASN   U  84  ? 2.0693 0.6194 1.2711 -0.1092 -0.2841 0.1511  75  ASN   U ND2 
36397 N  N   . GLY   U  85  ? 1.8222 0.3358 1.2738 0.0092  -0.4154 0.1112  76  GLY   U N   
36398 C  CA  . GLY   U  85  ? 1.7865 0.4186 1.2693 0.0126  -0.4330 0.1164  76  GLY   U CA  
36399 C  C   . GLY   U  85  ? 1.7853 0.4478 1.2788 0.0141  -0.4504 0.1236  76  GLY   U C   
36400 O  O   . GLY   U  85  ? 1.7371 0.3844 1.2885 0.0488  -0.4663 0.1350  76  GLY   U O   
36401 N  N   . PRO   U  86  ? 1.7915 0.4979 1.2473 -0.0020 -0.4598 0.1094  77  PRO   U N   
36402 C  CA  . PRO   U  86  ? 1.7777 0.5584 1.2354 0.0151  -0.4513 0.1161  77  PRO   U CA  
36403 C  C   . PRO   U  86  ? 1.7927 0.5498 1.2442 0.0761  -0.4594 0.1161  77  PRO   U C   
36404 O  O   . PRO   U  86  ? 1.7736 0.5683 1.2395 0.1168  -0.4613 0.0575  77  PRO   U O   
36405 C  CB  . PRO   U  86  ? 1.7861 0.5489 1.2358 0.0066  -0.4502 0.0955  77  PRO   U CB  
36406 C  CG  . PRO   U  86  ? 1.7939 0.5692 1.2364 -0.0111 -0.4380 0.0916  77  PRO   U CG  
36407 C  CD  . PRO   U  86  ? 1.7979 0.5280 1.2506 -0.0014 -0.4447 0.0922  77  PRO   U CD  
36408 N  N   . ILE   U  87  ? 1.8124 0.6081 1.2419 0.0682  -0.4584 0.0931  78  ILE   U N   
36409 C  CA  . ILE   U  87  ? 1.8238 0.5901 1.2251 0.0591  -0.4224 0.1188  78  ILE   U CA  
36410 C  C   . ILE   U  87  ? 1.8004 0.6107 1.1902 0.0832  -0.4198 0.1173  78  ILE   U C   
36411 O  O   . ILE   U  87  ? 1.8208 0.6075 1.2164 0.1001  -0.4548 0.1630  78  ILE   U O   
36412 C  CB  . ILE   U  87  ? 1.8530 0.6096 1.1973 0.0552  -0.4133 0.1017  78  ILE   U CB  
36413 C  CG1 . ILE   U  87  ? 1.8635 0.5902 1.1853 0.0422  -0.3756 0.1216  78  ILE   U CG1 
36414 C  CG2 . ILE   U  87  ? 1.8561 0.6460 1.2174 0.0801  -0.4194 0.0956  78  ILE   U CG2 
36415 C  CD1 . ILE   U  87  ? 1.8632 0.5441 1.1835 0.0296  -0.3668 0.1327  78  ILE   U CD1 
36416 N  N   . PRO   U  88  ? 1.8134 0.6270 1.1446 0.0661  -0.4169 0.1451  79  PRO   U N   
36417 C  CA  . PRO   U  88  ? 1.7942 0.6333 1.1283 0.0696  -0.3941 0.1375  79  PRO   U CA  
36418 C  C   . PRO   U  88  ? 1.7459 0.6851 1.0885 0.0232  -0.3923 0.1123  79  PRO   U C   
36419 O  O   . PRO   U  88  ? 1.7015 0.7439 1.0136 0.1674  -0.4305 0.1419  79  PRO   U O   
36420 C  CB  . PRO   U  88  ? 1.8016 0.6328 1.1217 0.0739  -0.3895 0.1459  79  PRO   U CB  
36421 C  CG  . PRO   U  88  ? 1.8287 0.6436 1.1284 0.0801  -0.3989 0.1497  79  PRO   U CG  
36422 C  CD  . PRO   U  88  ? 1.8193 0.6297 1.1385 0.0704  -0.4048 0.1458  79  PRO   U CD  
36423 N  N   . ASP   U  89  ? 1.7724 0.6309 1.1136 0.0013  -0.3447 0.1164  80  ASP   U N   
36424 C  CA  . ASP   U  89  ? 1.7427 0.5896 1.1487 -0.0115 -0.3199 0.1172  80  ASP   U CA  
36425 C  C   . ASP   U  89  ? 1.7429 0.4249 1.1503 -0.0398 -0.3522 0.1020  80  ASP   U C   
36426 O  O   . ASP   U  89  ? 1.7328 0.3901 1.1458 -0.0464 -0.3213 0.0898  80  ASP   U O   
36427 C  CB  . ASP   U  89  ? 1.7656 0.6665 1.1863 -0.0681 -0.2846 0.0819  80  ASP   U CB  
36428 C  CG  . ASP   U  89  ? 1.7944 0.7748 1.2313 -0.0883 -0.2255 0.0556  80  ASP   U CG  
36429 O  OD1 . ASP   U  89  ? 1.8588 0.8864 1.2724 -0.1371 -0.1560 0.0605  80  ASP   U OD1 
36430 O  OD2 . ASP   U  89  ? 1.8178 0.8444 1.2931 -0.1215 -0.1993 -0.0121 80  ASP   U OD2 
36431 N  N   . ALA   U  90  ? 1.7745 0.4186 1.1577 -0.0521 -0.3859 0.1022  81  ALA   U N   
36432 C  CA  . ALA   U  90  ? 1.7786 0.4588 1.2047 -0.0302 -0.3835 0.0752  81  ALA   U CA  
36433 C  C   . ALA   U  90  ? 1.7876 0.4752 1.2254 -0.0450 -0.4292 0.0533  81  ALA   U C   
36434 O  O   . ALA   U  90  ? 1.7639 0.5675 1.2266 -0.0336 -0.4498 -0.0032 81  ALA   U O   
36435 C  CB  . ALA   U  90  ? 1.8053 0.4873 1.2011 -0.0460 -0.3686 0.0864  81  ALA   U CB  
36436 N  N   . ARG   U  91  ? 1.7763 0.4814 1.2545 -0.0227 -0.4464 0.0408  82  ARG   U N   
36437 C  CA  . ARG   U  91  ? 1.8226 0.4704 1.2615 -0.0139 -0.4563 0.0416  82  ARG   U CA  
36438 C  C   . ARG   U  91  ? 1.8934 0.5125 1.1977 -0.0695 -0.4123 0.0376  82  ARG   U C   
36439 O  O   . ARG   U  91  ? 1.8707 0.5374 1.0780 -0.0383 -0.3809 0.0387  82  ARG   U O   
36440 C  CB  . ARG   U  91  ? 1.8257 0.4672 1.3289 0.0263  -0.4786 0.0336  82  ARG   U CB  
36441 C  CG  . ARG   U  91  ? 1.7600 0.4185 1.3448 0.0316  -0.4897 0.0516  82  ARG   U CG  
36442 C  CD  . ARG   U  91  ? 1.7574 0.4249 1.3288 0.0294  -0.5047 0.0904  82  ARG   U CD  
36443 N  NE  . ARG   U  91  ? 1.7181 0.4436 1.3225 0.0195  -0.4957 0.0878  82  ARG   U NE  
36444 C  CZ  . ARG   U  91  ? 1.6919 0.5410 1.3182 0.0256  -0.5100 0.0701  82  ARG   U CZ  
36445 N  NH1 . ARG   U  91  ? 1.6817 0.5652 1.3651 0.0288  -0.4880 0.0859  82  ARG   U NH1 
36446 N  NH2 . ARG   U  91  ? 1.6815 0.5695 1.3103 0.0373  -0.5423 0.0504  82  ARG   U NH2 
36447 N  N   . ASN   U  92  ? 1.9465 0.3920 1.2079 -0.0985 -0.3577 0.0658  83  ASN   U N   
36448 C  CA  . ASN   U  92  ? 1.8735 0.3455 1.2625 -0.0981 -0.3033 0.1294  83  ASN   U CA  
36449 C  C   . ASN   U  92  ? 1.8763 0.2767 1.2536 -0.0701 -0.3106 0.1429  83  ASN   U C   
36450 O  O   . ASN   U  92  ? 1.8048 0.3051 1.2565 -0.0220 -0.2894 0.1617  83  ASN   U O   
36451 C  CB  . ASN   U  92  ? 1.9111 0.3230 1.2839 -0.1142 -0.2612 0.1376  83  ASN   U CB  
36452 C  CG  . ASN   U  92  ? 1.9019 0.2798 1.3164 -0.1510 -0.2649 0.1754  83  ASN   U CG  
36453 O  OD1 . ASN   U  92  ? 1.9384 0.3165 1.3119 -0.1165 -0.2469 0.2058  83  ASN   U OD1 
36454 N  ND2 . ASN   U  92  ? 1.8782 0.1937 1.3636 -0.2107 -0.2446 0.1652  83  ASN   U ND2 
36455 N  N   . ALA   U  93  ? 1.7844 0.3252 1.2977 -0.0599 -0.3260 0.1253  84  ALA   U N   
36456 C  CA  . ALA   U  93  ? 1.8013 0.3681 1.3114 -0.0073 -0.3652 0.1304  84  ALA   U CA  
36457 C  C   . ALA   U  93  ? 1.7559 0.3498 1.2705 -0.0108 -0.4132 0.1476  84  ALA   U C   
36458 O  O   . ALA   U  93  ? 1.7889 0.3694 1.2308 0.0021  -0.4365 0.1799  84  ALA   U O   
36459 C  CB  . ALA   U  93  ? 1.8051 0.4068 1.3634 -0.0174 -0.3477 0.1600  84  ALA   U CB  
36460 N  N   . ALA   U  94  ? 1.7382 0.4406 1.2648 -0.0059 -0.4102 0.1221  85  ALA   U N   
36461 C  CA  . ALA   U  94  ? 1.7042 0.4939 1.2443 0.0035  -0.4017 0.1186  85  ALA   U CA  
36462 C  C   . ALA   U  94  ? 1.6558 0.4831 1.1918 0.0164  -0.4063 0.1036  85  ALA   U C   
36463 O  O   . ALA   U  94  ? 1.6574 0.4704 1.2194 0.0395  -0.4308 0.1325  85  ALA   U O   
36464 C  CB  . ALA   U  94  ? 1.6962 0.5338 1.2610 0.0122  -0.4051 0.1268  85  ALA   U CB  
36465 N  N   . LEU   U  95  ? 1.6654 0.4994 1.1350 -0.0220 -0.4158 0.0865  86  LEU   U N   
36466 C  CA  . LEU   U  95  ? 1.6738 0.4938 1.1596 -0.0263 -0.3801 0.0583  86  LEU   U CA  
36467 C  C   . LEU   U  95  ? 1.6647 0.4511 1.1727 -0.0100 -0.3561 0.0611  86  LEU   U C   
36468 O  O   . LEU   U  95  ? 1.6994 0.4519 1.2425 -0.0050 -0.3105 0.0877  86  LEU   U O   
36469 C  CB  . LEU   U  95  ? 1.6760 0.5701 1.1299 -0.0364 -0.3903 0.0334  86  LEU   U CB  
36470 C  CG  . LEU   U  95  ? 1.6967 0.5715 1.1561 -0.0363 -0.3834 0.0453  86  LEU   U CG  
36471 C  CD1 . LEU   U  95  ? 1.6983 0.5871 1.1775 -0.0320 -0.3775 0.0312  86  LEU   U CD1 
36472 C  CD2 . LEU   U  95  ? 1.7119 0.5796 1.1251 -0.0563 -0.3705 0.0349  86  LEU   U CD2 
36473 N  N   . ARG   U  96  ? 1.6581 0.3691 1.1908 0.0127  -0.3402 0.0597  87  ARG   U N   
36474 C  CA  . ARG   U  96  ? 1.6874 0.3427 1.1881 0.0175  -0.3375 0.0807  87  ARG   U CA  
36475 C  C   . ARG   U  96  ? 1.7201 0.3796 1.1661 0.0133  -0.3127 0.0783  87  ARG   U C   
36476 O  O   . ARG   U  96  ? 1.7297 0.4494 1.2038 0.0945  -0.2959 0.0775  87  ARG   U O   
36477 C  CB  . ARG   U  96  ? 1.6793 0.3198 1.2209 0.0187  -0.3402 0.0765  87  ARG   U CB  
36478 C  CG  . ARG   U  96  ? 1.6762 0.3874 1.2241 0.0220  -0.3655 0.0391  87  ARG   U CG  
36479 C  CD  . ARG   U  96  ? 1.6927 0.4512 1.2566 -0.0084 -0.3369 0.0629  87  ARG   U CD  
36480 N  NE  . ARG   U  96  ? 1.7026 0.5631 1.2869 0.0320  -0.3773 0.0109  87  ARG   U NE  
36481 C  CZ  . ARG   U  96  ? 1.7310 0.5901 1.3260 0.0508  -0.3785 -0.0495 87  ARG   U CZ  
36482 N  NH1 . ARG   U  96  ? 1.7163 0.6317 1.3918 0.0429  -0.3540 -0.0790 87  ARG   U NH1 
36483 N  NH2 . ARG   U  96  ? 1.7674 0.5996 1.3609 0.0813  -0.4026 -0.0399 87  ARG   U NH2 
36484 N  N   . ALA   U  97  ? 1.7875 0.3887 1.1317 0.0004  -0.3415 0.0840  88  ALA   U N   
36485 C  CA  . ALA   U  97  ? 1.7944 0.4427 1.1232 0.0247  -0.3504 0.0860  88  ALA   U CA  
36486 C  C   . ALA   U  97  ? 1.7836 0.3628 1.1117 0.0812  -0.3539 0.1487  88  ALA   U C   
36487 O  O   . ALA   U  97  ? 1.7519 0.5004 1.0453 0.1235  -0.4168 0.2302  88  ALA   U O   
36488 C  CB  . ALA   U  97  ? 1.8265 0.5003 1.0990 -0.0177 -0.3296 0.0864  88  ALA   U CB  
36489 N  N   . LYS   U  98  ? 1.7813 0.3375 1.1731 0.0526  -0.3451 0.0980  89  LYS   U N   
36490 C  CA  . LYS   U  98  ? 1.7983 0.3498 1.2101 0.0648  -0.3253 0.0623  89  LYS   U CA  
36491 C  C   . LYS   U  98  ? 1.7961 0.3052 1.2418 0.1120  -0.2810 0.0470  89  LYS   U C   
36492 O  O   . LYS   U  98  ? 1.8595 0.2331 1.4054 0.1321  -0.2713 0.1215  89  LYS   U O   
36493 C  CB  . LYS   U  98  ? 1.7999 0.3655 1.2092 0.0423  -0.3390 0.0080  89  LYS   U CB  
36494 C  CG  . LYS   U  98  ? 1.7789 0.3033 1.2115 0.0214  -0.3556 -0.0148 89  LYS   U CG  
36495 C  CD  . LYS   U  98  ? 1.7829 0.2760 1.2069 0.0153  -0.3657 -0.0286 89  LYS   U CD  
36496 C  CE  . LYS   U  98  ? 1.7927 0.2579 1.1869 0.0007  -0.3605 -0.0468 89  LYS   U CE  
36497 N  NZ  . LYS   U  98  ? 1.8025 0.3055 1.1840 0.0032  -0.3717 -0.0583 89  LYS   U NZ  
36498 N  N   . ALA   U  99  ? 1.8088 0.2984 1.2142 0.0986  -0.2876 0.0885  90  ALA   U N   
36499 C  CA  . ALA   U  99  ? 1.7910 0.2897 1.2236 0.1151  -0.2863 0.0937  90  ALA   U CA  
36500 C  C   . ALA   U  99  ? 1.7644 0.3398 1.2330 0.0582  -0.2935 0.0755  90  ALA   U C   
36501 O  O   . ALA   U  99  ? 1.8455 0.3909 1.3240 0.1718  -0.2622 0.0475  90  ALA   U O   
36502 C  CB  . ALA   U  99  ? 1.7801 0.2979 1.2188 0.1189  -0.2827 0.1239  90  ALA   U CB  
36503 N  N   . GLU   U  100 ? 1.7305 0.3080 1.2200 0.0623  -0.3125 0.1413  91  GLU   U N   
36504 C  CA  . GLU   U  100 ? 1.7389 0.3896 1.2190 0.0641  -0.3252 0.1470  91  GLU   U CA  
36505 C  C   . GLU   U  100 ? 1.7831 0.2551 1.1814 0.0142  -0.3632 0.1005  91  GLU   U C   
36506 O  O   . GLU   U  100 ? 1.7127 0.3706 1.2012 0.0424  -0.3908 0.0845  91  GLU   U O   
36507 C  CB  . GLU   U  100 ? 1.6744 0.4809 1.1977 0.0098  -0.3458 0.1318  91  GLU   U CB  
36508 C  CG  . GLU   U  100 ? 1.6290 0.6183 1.2091 0.0271  -0.3245 0.1301  91  GLU   U CG  
36509 C  CD  . GLU   U  100 ? 1.6155 0.7242 1.2186 0.0410  -0.3062 0.1667  91  GLU   U CD  
36510 O  OE1 . GLU   U  100 ? 1.5703 0.8414 1.2648 0.0685  -0.3277 0.1446  91  GLU   U OE1 
36511 O  OE2 . GLU   U  100 ? 1.5776 0.8687 1.3129 0.1147  -0.2707 0.1418  91  GLU   U OE2 
36512 N  N   . ALA   U  101 ? 1.8116 0.1298 1.1827 0.0121  -0.4219 0.0792  92  ALA   U N   
36513 C  CA  . ALA   U  101 ? 1.7943 0.2724 1.1833 0.0241  -0.4180 0.0883  92  ALA   U CA  
36514 C  C   . ALA   U  101 ? 1.7903 0.2950 1.2115 -0.0195 -0.4470 0.1042  92  ALA   U C   
36515 O  O   . ALA   U  101 ? 1.7542 0.2581 1.2241 -0.0410 -0.4853 0.0790  92  ALA   U O   
36516 C  CB  . ALA   U  101 ? 1.8127 0.2243 1.1845 -0.0030 -0.4201 0.0736  92  ALA   U CB  
36517 N  N   . ALA   U  102 ? 1.7988 0.4214 1.2177 -0.0267 -0.4371 0.1567  93  ALA   U N   
36518 C  CA  . ALA   U  102 ? 1.8715 0.4063 1.2333 -0.0079 -0.4398 0.1300  93  ALA   U CA  
36519 C  C   . ALA   U  102 ? 1.8876 0.4455 1.2651 0.0264  -0.4496 0.1456  93  ALA   U C   
36520 O  O   . ALA   U  102 ? 1.9527 0.4742 1.1936 0.0474  -0.4150 0.1341  93  ALA   U O   
36521 C  CB  . ALA   U  102 ? 1.8749 0.4479 1.2292 -0.0277 -0.4434 0.1434  93  ALA   U CB  
36522 N  N   . GLU   U  103 ? 1.8561 0.4207 1.2906 0.0315  -0.4490 0.1210  94  GLU   U N   
36523 C  CA  . GLU   U  103 ? 1.7885 0.4523 1.2598 -0.0277 -0.4338 0.1263  94  GLU   U CA  
36524 C  C   . GLU   U  103 ? 1.7764 0.3443 1.2758 -0.0541 -0.4343 0.1617  94  GLU   U C   
36525 O  O   . GLU   U  103 ? 1.7179 0.3267 1.3003 -0.0738 -0.4416 0.1543  94  GLU   U O   
36526 C  CB  . GLU   U  103 ? 1.7614 0.5586 1.2917 -0.0223 -0.3983 0.0871  94  GLU   U CB  
36527 C  CG  . GLU   U  103 ? 1.7687 0.6512 1.3093 -0.0277 -0.3886 0.1233  94  GLU   U CG  
36528 C  CD  . GLU   U  103 ? 1.7339 0.8134 1.3396 -0.0244 -0.4208 0.0532  94  GLU   U CD  
36529 O  OE1 . GLU   U  103 ? 1.7172 1.0435 1.5265 -0.0075 -0.3662 0.0161  94  GLU   U OE1 
36530 O  OE2 . GLU   U  103 ? 1.7839 0.9175 1.3190 -0.0313 -0.4550 0.0630  94  GLU   U OE2 
36531 N  N   . PHE   U  104 ? 1.7809 0.3429 1.2666 -0.0438 -0.4098 0.1792  95  PHE   U N   
36532 C  CA  . PHE   U  104 ? 1.7817 0.1603 1.2308 -0.0741 -0.3842 0.2422  95  PHE   U CA  
36533 C  C   . PHE   U  104 ? 1.7798 0.2246 1.2132 -0.0420 -0.4092 0.2128  95  PHE   U C   
36534 O  O   . PHE   U  104 ? 1.8247 0.0961 1.1784 -0.1051 -0.4144 0.2371  95  PHE   U O   
36535 C  CB  . PHE   U  104 ? 1.8258 0.1458 1.2392 -0.0229 -0.4192 0.2363  95  PHE   U CB  
36536 C  CG  . PHE   U  104 ? 1.8264 0.1476 1.2255 -0.0633 -0.4027 0.3244  95  PHE   U CG  
36537 C  CD1 . PHE   U  104 ? 1.8506 0.1670 1.2211 -0.0741 -0.3972 0.3397  95  PHE   U CD1 
36538 C  CD2 . PHE   U  104 ? 1.8464 0.1987 1.1866 -0.0473 -0.4218 0.3682  95  PHE   U CD2 
36539 C  CE1 . PHE   U  104 ? 1.8529 0.2010 1.2185 -0.0560 -0.3851 0.3703  95  PHE   U CE1 
36540 C  CE2 . PHE   U  104 ? 1.8493 0.2305 1.1976 -0.0247 -0.4061 0.3944  95  PHE   U CE2 
36541 C  CZ  . PHE   U  104 ? 1.8494 0.2268 1.2043 -0.0343 -0.4087 0.3890  95  PHE   U CZ  
36542 N  N   . ARG   U  105 ? 1.8046 0.3083 1.1922 -0.0514 -0.3938 0.1695  96  ARG   U N   
36543 C  CA  . ARG   U  105 ? 1.8449 0.3766 1.1941 -0.0051 -0.3848 0.1499  96  ARG   U CA  
36544 C  C   . ARG   U  105 ? 1.8286 0.3699 1.1747 -0.0046 -0.3893 0.1279  96  ARG   U C   
36545 O  O   . ARG   U  105 ? 1.8888 0.3169 1.1548 -0.0341 -0.4073 0.0128  96  ARG   U O   
36546 C  CB  . ARG   U  105 ? 1.8782 0.4044 1.1865 0.0082  -0.3715 0.1870  96  ARG   U CB  
36547 C  CG  . ARG   U  105 ? 1.9231 0.4004 1.2045 0.0398  -0.3499 0.1839  96  ARG   U CG  
36548 C  CD  . ARG   U  105 ? 1.9380 0.4190 1.2288 0.0580  -0.3322 0.1923  96  ARG   U CD  
36549 N  NE  . ARG   U  105 ? 1.9824 0.4584 1.2373 0.0375  -0.3190 0.1643  96  ARG   U NE  
36550 C  CZ  . ARG   U  105 ? 2.0086 0.5078 1.1629 0.0007  -0.2990 0.2237  96  ARG   U CZ  
36551 N  NH1 . ARG   U  105 ? 2.0026 0.4798 1.1935 -0.0075 -0.2782 0.2867  96  ARG   U NH1 
36552 N  NH2 . ARG   U  105 ? 2.0462 0.5451 1.1576 -0.0076 -0.2950 0.2034  96  ARG   U NH2 
36553 N  N   . TYR   U  106 ? 1.7892 0.4093 1.1521 0.0065  -0.4166 0.0935  97  TYR   U N   
36554 C  CA  . TYR   U  106 ? 1.7881 0.3663 1.1480 0.0313  -0.4083 0.0653  97  TYR   U CA  
36555 C  C   . TYR   U  106 ? 1.8052 0.3563 1.2022 0.0711  -0.4084 0.1040  97  TYR   U C   
36556 O  O   . TYR   U  106 ? 1.8025 0.3869 1.1963 0.1241  -0.4296 0.0697  97  TYR   U O   
36557 C  CB  . TYR   U  106 ? 1.7860 0.3925 1.1027 0.0635  -0.4189 0.0692  97  TYR   U CB  
36558 C  CG  . TYR   U  106 ? 1.7580 0.4414 1.0541 0.1016  -0.3973 0.0995  97  TYR   U CG  
36559 C  CD1 . TYR   U  106 ? 1.7622 0.4228 1.0853 0.1000  -0.3896 0.1144  97  TYR   U CD1 
36560 C  CD2 . TYR   U  106 ? 1.7168 0.4248 1.0442 0.1332  -0.4160 0.1187  97  TYR   U CD2 
36561 C  CE1 . TYR   U  106 ? 1.7515 0.4137 1.0616 0.1269  -0.4010 0.1236  97  TYR   U CE1 
36562 C  CE2 . TYR   U  106 ? 1.7113 0.4349 1.0060 0.1392  -0.4157 0.1154  97  TYR   U CE2 
36563 C  CZ  . TYR   U  106 ? 1.7247 0.4115 1.0571 0.1325  -0.4108 0.1193  97  TYR   U CZ  
36564 O  OH  . TYR   U  106 ? 1.7263 0.3742 1.0765 0.1596  -0.4141 0.1122  97  TYR   U OH  
36565 N  N   . LYS   U  107 ? 1.8329 0.3824 1.2099 0.0650  -0.3909 0.0889  98  LYS   U N   
36566 C  CA  . LYS   U  107 ? 1.8516 0.3648 1.2113 0.1151  -0.3681 0.1549  98  LYS   U CA  
36567 C  C   . LYS   U  107 ? 1.8587 0.3499 1.2469 0.1175  -0.3664 0.1127  98  LYS   U C   
36568 O  O   . LYS   U  107 ? 1.8489 0.3186 1.2564 0.1514  -0.3931 0.0318  98  LYS   U O   
36569 C  CB  . LYS   U  107 ? 1.8755 0.4040 1.1755 0.1086  -0.3501 0.1508  98  LYS   U CB  
36570 C  CG  . LYS   U  107 ? 1.8990 0.4946 1.2392 0.1285  -0.3117 0.1613  98  LYS   U CG  
36571 C  CD  . LYS   U  107 ? 1.9470 0.5347 1.3262 0.1391  -0.2861 0.0894  98  LYS   U CD  
36572 C  CE  . LYS   U  107 ? 1.9645 0.6212 1.3900 0.1415  -0.2389 0.0778  98  LYS   U CE  
36573 N  NZ  . LYS   U  107 ? 1.9618 0.6615 1.4509 0.1494  -0.2493 0.0284  98  LYS   U NZ  
36574 N  N   . TYR   U  108 ? 1.8548 0.3608 1.2763 0.1353  -0.3567 0.1305  99  TYR   U N   
36575 C  CA  . TYR   U  108 ? 1.8592 0.3996 1.2790 0.1391  -0.3504 0.1195  99  TYR   U CA  
36576 C  C   . TYR   U  108 ? 1.8653 0.3511 1.3122 0.1035  -0.3218 0.0966  99  TYR   U C   
36577 O  O   . TYR   U  108 ? 1.8747 0.4138 1.3597 0.1163  -0.2938 0.0936  99  TYR   U O   
36578 C  CB  . TYR   U  108 ? 1.8531 0.4098 1.2614 0.1386  -0.3700 0.1069  99  TYR   U CB  
36579 C  CG  . TYR   U  108 ? 1.8598 0.4947 1.1823 0.1539  -0.4191 0.1661  99  TYR   U CG  
36580 C  CD1 . TYR   U  108 ? 1.8659 0.4505 1.1705 0.1654  -0.3797 0.1893  99  TYR   U CD1 
36581 C  CD2 . TYR   U  108 ? 1.8687 0.5298 1.1873 0.1527  -0.3831 0.1020  99  TYR   U CD2 
36582 C  CE1 . TYR   U  108 ? 1.8558 0.4594 1.1157 0.1785  -0.4241 0.2321  99  TYR   U CE1 
36583 C  CE2 . TYR   U  108 ? 1.8620 0.5362 1.1140 0.1521  -0.4369 0.1581  99  TYR   U CE2 
36584 C  CZ  . TYR   U  108 ? 1.8514 0.5139 1.0766 0.1874  -0.3961 0.1445  99  TYR   U CZ  
36585 O  OH  . TYR   U  108 ? 1.8457 0.6450 1.0114 0.2338  -0.4546 0.1706  99  TYR   U OH  
36586 N  N   . GLY   U  109 ? 1.8978 0.2402 1.3054 0.0688  -0.3202 0.0953  100 GLY   U N   
36587 C  CA  . GLY   U  109 ? 1.9213 0.2634 1.2476 0.0325  -0.3431 0.1190  100 GLY   U CA  
36588 C  C   . GLY   U  109 ? 1.9424 0.3033 1.2396 0.0392  -0.3711 0.1574  100 GLY   U C   
36589 O  O   . GLY   U  109 ? 2.0116 0.1879 1.2200 0.0712  -0.3818 0.2065  100 GLY   U O   
36590 N  N   . TYR   U  110 ? 1.9142 0.3051 1.2346 0.0281  -0.3639 0.1694  101 TYR   U N   
36591 C  CA  . TYR   U  110 ? 1.8960 0.3875 1.2478 0.0193  -0.3231 0.1845  101 TYR   U CA  
36592 C  C   . TYR   U  110 ? 1.8869 0.4059 1.2913 0.0320  -0.3136 0.1812  101 TYR   U C   
36593 O  O   . TYR   U  110 ? 1.9017 0.4765 1.2569 0.1148  -0.3257 0.2512  101 TYR   U O   
36594 C  CB  . TYR   U  110 ? 1.8910 0.3911 1.2231 0.0180  -0.3150 0.2333  101 TYR   U CB  
36595 C  CG  . TYR   U  110 ? 1.8570 0.3141 1.2427 0.0074  -0.3223 0.2673  101 TYR   U CG  
36596 C  CD1 . TYR   U  110 ? 1.8618 0.3555 1.2405 0.0015  -0.3420 0.2532  101 TYR   U CD1 
36597 C  CD2 . TYR   U  110 ? 1.8584 0.3302 1.1911 0.0207  -0.3455 0.3243  101 TYR   U CD2 
36598 C  CE1 . TYR   U  110 ? 1.8486 0.3001 1.2763 -0.0202 -0.3366 0.2673  101 TYR   U CE1 
36599 C  CE2 . TYR   U  110 ? 1.8600 0.2752 1.2273 0.0019  -0.3494 0.3395  101 TYR   U CE2 
36600 C  CZ  . TYR   U  110 ? 1.8618 0.3103 1.2028 -0.0083 -0.3595 0.3043  101 TYR   U CZ  
36601 O  OH  . TYR   U  110 ? 1.8968 0.1600 1.2963 -0.0611 -0.3217 0.3215  101 TYR   U OH  
36602 N  N   . ASP   U  111 ? 1.8582 0.5038 1.2154 -0.0408 -0.2742 0.1548  102 ASP   U N   
36603 C  CA  . ASP   U  111 ? 1.8293 0.5048 1.2261 -0.0471 -0.2740 0.1078  102 ASP   U CA  
36604 C  C   . ASP   U  111 ? 1.8511 0.4719 1.2392 -0.0089 -0.2753 0.0923  102 ASP   U C   
36605 O  O   . ASP   U  111 ? 1.8403 0.4452 1.1770 0.0292  -0.2799 -0.0013 102 ASP   U O   
36606 C  CB  . ASP   U  111 ? 1.8275 0.5761 1.2075 -0.0874 -0.2620 0.0822  102 ASP   U CB  
36607 C  CG  . ASP   U  111 ? 1.8545 0.6158 1.2500 -0.1227 -0.2498 0.0485  102 ASP   U CG  
36608 O  OD1 . ASP   U  111 ? 1.8722 0.6591 1.2051 -0.1506 -0.2521 0.0459  102 ASP   U OD1 
36609 O  OD2 . ASP   U  111 ? 1.8799 0.6757 1.2533 -0.1415 -0.2460 -0.0093 102 ASP   U OD2 
36610 N  N   . MET   U  112 ? 1.8369 0.3901 1.2654 -0.0084 -0.3001 0.1017  103 MET   U N   
36611 C  CA  . MET   U  112 ? 1.8200 0.2938 1.2903 -0.0153 -0.3173 0.1627  103 MET   U CA  
36612 C  C   . MET   U  112 ? 1.8094 0.2323 1.3284 -0.0143 -0.3322 0.1480  103 MET   U C   
36613 O  O   . MET   U  112 ? 1.7865 0.1497 1.3287 0.0457  -0.3284 0.0882  103 MET   U O   
36614 C  CB  . MET   U  112 ? 1.8383 0.1705 1.2862 -0.0140 -0.3183 0.1834  103 MET   U CB  
36615 C  CG  . MET   U  112 ? 1.8843 0.1337 1.2852 -0.0050 -0.3213 0.2113  103 MET   U CG  
36616 S  SD  . MET   U  112 ? 1.8720 0.2560 1.3339 -0.0207 -0.3052 0.2595  103 MET   U SD  
36617 C  CE  . MET   U  112 ? 1.9024 0.3610 1.3358 -0.0186 -0.3064 0.2388  103 MET   U CE  
36618 N  N   . PRO   U  113 ? 1.8309 0.3231 1.3518 -0.0461 -0.3626 0.1483  104 PRO   U N   
36619 C  CA  . PRO   U  113 ? 1.8078 0.4359 1.3396 -0.1121 -0.3561 0.1536  104 PRO   U CA  
36620 C  C   . PRO   U  113 ? 1.7628 0.4732 1.3537 -0.0846 -0.3873 0.1728  104 PRO   U C   
36621 O  O   . PRO   U  113 ? 1.7247 0.5901 1.3233 -0.1324 -0.4148 0.1879  104 PRO   U O   
36622 C  CB  . PRO   U  113 ? 1.8166 0.3947 1.3540 -0.1107 -0.3663 0.1652  104 PRO   U CB  
36623 C  CG  . PRO   U  113 ? 1.8313 0.3879 1.3652 -0.1017 -0.3650 0.1667  104 PRO   U CG  
36624 C  CD  . PRO   U  113 ? 1.8385 0.3331 1.3542 -0.0979 -0.3679 0.1996  104 PRO   U CD  
36625 N  N   . CYS   U  114 ? 1.8118 0.5450 1.3668 -0.1088 -0.3864 0.2070  105 CYS   U N   
36626 C  CA  . CYS   U  114 ? 1.8307 0.5832 1.4320 -0.0728 -0.3735 0.1597  105 CYS   U CA  
36627 C  C   . CYS   U  114 ? 1.7856 0.5821 1.5037 -0.0630 -0.4045 0.1289  105 CYS   U C   
36628 O  O   . CYS   U  114 ? 1.7212 0.5772 1.5631 -0.0294 -0.3837 0.2349  105 CYS   U O   
36629 C  CB  . CYS   U  114 ? 1.9070 0.7177 1.3834 -0.1116 -0.3608 0.1607  105 CYS   U CB  
36630 S  SG  . CYS   U  114 ? 1.9887 0.7101 1.3738 -0.1599 -0.3190 0.2108  105 CYS   U SG  
36631 N  N   . ASP   U  115 ? 1.7741 0.5582 1.5842 -0.0563 -0.3903 0.1049  106 ASP   U N   
36632 C  CA  . ASP   U  115 ? 1.7590 0.4890 1.5169 -0.0357 -0.3537 0.1383  106 ASP   U CA  
36633 C  C   . ASP   U  115 ? 1.7582 0.4088 1.4936 -0.0523 -0.3534 0.1165  106 ASP   U C   
36634 O  O   . ASP   U  115 ? 1.7900 0.5629 1.4531 -0.0646 -0.2682 0.0989  106 ASP   U O   
36635 C  CB  . ASP   U  115 ? 1.7482 0.3594 1.6287 0.0239  -0.3695 0.1154  106 ASP   U CB  
36636 C  CG  . ASP   U  115 ? 1.7546 0.3122 1.6633 -0.0095 -0.3705 0.1331  106 ASP   U CG  
36637 O  OD1 . ASP   U  115 ? 1.7287 0.1000 1.7810 0.0696  -0.3440 0.1082  106 ASP   U OD1 
36638 O  OD2 . ASP   U  115 ? 1.7425 0.1263 1.6884 -0.0116 -0.3441 0.1880  106 ASP   U OD2 
36639 N  N   . VAL   U  116 ? 1.7138 0.3916 1.3216 -0.0205 -0.3513 0.1093  107 VAL   U N   
36640 C  CA  . VAL   U  116 ? 1.6992 0.3599 1.2883 -0.0163 -0.3685 0.0872  107 VAL   U CA  
36641 C  C   . VAL   U  116 ? 1.7340 0.2558 1.2651 0.0043  -0.3203 0.0670  107 VAL   U C   
36642 O  O   . VAL   U  116 ? 1.6821 0.2541 1.2394 0.0276  -0.3405 0.1030  107 VAL   U O   
36643 C  CB  . VAL   U  116 ? 1.6945 0.3646 1.2279 0.0137  -0.3662 0.1373  107 VAL   U CB  
36644 C  CG1 . VAL   U  116 ? 1.6937 0.3547 1.2292 0.0476  -0.3859 0.1701  107 VAL   U CG1 
36645 C  CG2 . VAL   U  116 ? 1.6868 0.3378 1.2136 0.0056  -0.3772 0.1412  107 VAL   U CG2 
36646 N  N   . LEU   U  117 ? 1.7796 0.2262 1.2484 0.0037  -0.3210 0.0557  108 LEU   U N   
36647 C  CA  . LEU   U  117 ? 1.7618 0.3692 1.2324 -0.0228 -0.3121 0.0670  108 LEU   U CA  
36648 C  C   . LEU   U  117 ? 1.8123 0.3860 1.2426 -0.0431 -0.2983 0.0514  108 LEU   U C   
36649 O  O   . LEU   U  117 ? 1.8218 0.5635 1.2702 -0.0481 -0.2676 0.0592  108 LEU   U O   
36650 C  CB  . LEU   U  117 ? 1.7926 0.3053 1.2331 -0.0549 -0.3101 0.0412  108 LEU   U CB  
36651 C  CG  . LEU   U  117 ? 1.7902 0.3448 1.2138 -0.0665 -0.3188 0.0322  108 LEU   U CG  
36652 C  CD1 . LEU   U  117 ? 1.8241 0.3210 1.2042 -0.0701 -0.3006 0.0066  108 LEU   U CD1 
36653 C  CD2 . LEU   U  117 ? 1.8043 0.3597 1.2192 -0.0709 -0.3300 0.0317  108 LEU   U CD2 
36654 N  N   . ALA   U  118 ? 1.8288 0.4091 1.2167 -0.0372 -0.2933 0.0882  109 ALA   U N   
36655 C  CA  . ALA   U  118 ? 1.8391 0.3994 1.2058 -0.0184 -0.2756 0.1004  109 ALA   U CA  
36656 C  C   . ALA   U  118 ? 1.8060 0.3448 1.1989 0.0067  -0.2708 0.0997  109 ALA   U C   
36657 O  O   . ALA   U  118 ? 1.8186 0.3447 1.1018 -0.0282 -0.2586 0.1177  109 ALA   U O   
36658 C  CB  . ALA   U  118 ? 1.8545 0.4845 1.2441 -0.0310 -0.2436 0.0989  109 ALA   U CB  
36659 N  N   . LYS   U  119 ? 1.7916 0.3590 1.1728 0.0136  -0.2775 0.0660  110 LYS   U N   
36660 C  CA  . LYS   U  119 ? 1.7544 0.3737 1.1767 0.0387  -0.2788 0.0929  110 LYS   U CA  
36661 C  C   . LYS   U  119 ? 1.7520 0.3166 1.1809 0.0268  -0.3007 0.1215  110 LYS   U C   
36662 O  O   . LYS   U  119 ? 1.7542 0.3395 1.1299 0.0074  -0.2605 0.1833  110 LYS   U O   
36663 C  CB  . LYS   U  119 ? 1.7641 0.4016 1.2053 0.0539  -0.2807 0.1225  110 LYS   U CB  
36664 C  CG  . LYS   U  119 ? 1.7618 0.4740 1.2137 0.0830  -0.2878 0.1382  110 LYS   U CG  
36665 C  CD  . LYS   U  119 ? 1.7609 0.5033 1.2749 0.1007  -0.2869 0.1385  110 LYS   U CD  
36666 C  CE  . LYS   U  119 ? 1.7662 0.5553 1.2871 0.1208  -0.3107 0.1527  110 LYS   U CE  
36667 N  NZ  . LYS   U  119 ? 1.7532 0.6386 1.3228 0.1401  -0.3281 0.1628  110 LYS   U NZ  
36668 N  N   . ARG   U  120 ? 1.7643 0.3015 1.1436 0.0543  -0.3196 0.1088  111 ARG   U N   
36669 C  CA  . ARG   U  120 ? 1.7639 0.3658 1.1316 0.0567  -0.3251 0.1212  111 ARG   U CA  
36670 C  C   . ARG   U  120 ? 1.7691 0.3671 1.1328 0.0622  -0.3570 0.1257  111 ARG   U C   
36671 O  O   . ARG   U  120 ? 1.7434 0.4361 1.0024 0.0593  -0.4657 0.2120  111 ARG   U O   
36672 C  CB  . ARG   U  120 ? 1.7728 0.3839 1.1491 0.0431  -0.3178 0.1082  111 ARG   U CB  
36673 C  CG  . ARG   U  120 ? 1.7812 0.3848 1.1282 0.0495  -0.3069 0.1061  111 ARG   U CG  
36674 C  CD  . ARG   U  120 ? 1.8040 0.3760 1.1306 0.0720  -0.2837 0.1188  111 ARG   U CD  
36675 N  NE  . ARG   U  120 ? 1.8129 0.3649 1.1223 0.0652  -0.2782 0.1005  111 ARG   U NE  
36676 C  CZ  . ARG   U  120 ? 1.8259 0.4126 1.1520 0.0813  -0.2385 0.1087  111 ARG   U CZ  
36677 N  NH1 . ARG   U  120 ? 1.8639 0.4074 1.1374 0.1452  -0.2795 0.1281  111 ARG   U NH1 
36678 N  NH2 . ARG   U  120 ? 1.8247 0.4360 1.1625 0.0610  -0.2375 0.0693  111 ARG   U NH2 
36679 N  N   . MET   U  121 ? 1.7921 0.3595 1.1710 0.0611  -0.3721 0.1451  112 MET   U N   
36680 C  CA  . MET   U  121 ? 1.7897 0.3171 1.2015 0.0414  -0.3893 0.1338  112 MET   U CA  
36681 C  C   . MET   U  121 ? 1.7807 0.3013 1.2214 0.0343  -0.3549 0.1255  112 MET   U C   
36682 O  O   . MET   U  121 ? 1.8601 0.2424 1.1563 0.0122  -0.3294 0.1051  112 MET   U O   
36683 C  CB  . MET   U  121 ? 1.7607 0.3378 1.2201 0.0579  -0.4258 0.1399  112 MET   U CB  
36684 C  CG  . MET   U  121 ? 1.7649 0.3252 1.2458 0.0687  -0.4353 0.1293  112 MET   U CG  
36685 S  SD  . MET   U  121 ? 1.7272 0.4502 1.2859 0.0883  -0.4295 0.0819  112 MET   U SD  
36686 C  CE  . MET   U  121 ? 1.7495 0.3501 1.3548 0.0292  -0.4063 0.1199  112 MET   U CE  
36687 N  N   . ALA   U  122 ? 1.7917 0.2788 1.2419 0.0023  -0.3491 0.0958  113 ALA   U N   
36688 C  CA  . ALA   U  122 ? 1.7855 0.3391 1.2640 -0.0401 -0.3450 0.0793  113 ALA   U CA  
36689 C  C   . ALA   U  122 ? 1.7639 0.3531 1.2680 -0.0568 -0.3445 0.0839  113 ALA   U C   
36690 O  O   . ALA   U  122 ? 1.7236 0.3475 1.2451 -0.0604 -0.3413 0.1001  113 ALA   U O   
36691 C  CB  . ALA   U  122 ? 1.8030 0.3560 1.2555 -0.0431 -0.3236 0.0870  113 ALA   U CB  
36692 N  N   . ASN   U  123 ? 1.7346 0.3068 1.2971 -0.0742 -0.3270 0.0276  114 ASN   U N   
36693 C  CA  . ASN   U  123 ? 1.7112 0.3539 1.2802 -0.1016 -0.3500 0.0092  114 ASN   U CA  
36694 C  C   . ASN   U  123 ? 1.7042 0.2302 1.2740 -0.0493 -0.3680 0.0159  114 ASN   U C   
36695 O  O   . ASN   U  123 ? 1.6772 0.2035 1.2681 -0.1205 -0.3945 0.0062  114 ASN   U O   
36696 C  CB  . ASN   U  123 ? 1.6581 0.4276 1.3297 -0.0414 -0.3527 0.0120  114 ASN   U CB  
36697 C  CG  . ASN   U  123 ? 1.6433 0.6186 1.3447 -0.1239 -0.3678 -0.0442 114 ASN   U CG  
36698 O  OD1 . ASN   U  123 ? 1.5941 0.8463 1.4086 0.0550  -0.3209 -0.0621 114 ASN   U OD1 
36699 N  ND2 . ASN   U  123 ? 1.6497 0.5566 1.3396 -0.0885 -0.3599 -0.0369 114 ASN   U ND2 
36700 N  N   . LEU   U  124 ? 1.6925 0.2926 1.2886 0.0151  -0.4101 0.0390  115 LEU   U N   
36701 C  CA  . LEU   U  124 ? 1.7056 0.4892 1.2988 0.0134  -0.3967 0.0384  115 LEU   U CA  
36702 C  C   . LEU   U  124 ? 1.7623 0.4835 1.2735 -0.0285 -0.3860 0.0176  115 LEU   U C   
36703 O  O   . LEU   U  124 ? 1.8467 0.5511 1.1774 -0.0485 -0.4018 0.0524  115 LEU   U O   
36704 C  CB  . LEU   U  124 ? 1.7144 0.5305 1.3246 0.0372  -0.4182 0.0146  115 LEU   U CB  
36705 C  CG  . LEU   U  124 ? 1.6757 0.5463 1.3351 0.0543  -0.4294 0.0854  115 LEU   U CG  
36706 C  CD1 . LEU   U  124 ? 1.6498 0.6134 1.3566 0.0651  -0.4429 0.0850  115 LEU   U CD1 
36707 C  CD2 . LEU   U  124 ? 1.6695 0.5786 1.3398 0.0771  -0.4159 0.0718  115 LEU   U CD2 
36708 N  N   . SER   U  125 ? 1.7203 0.5229 1.2958 -0.0941 -0.3647 0.0018  116 SER   U N   
36709 C  CA  . SER   U  125 ? 1.6902 0.5326 1.3058 -0.0966 -0.3533 -0.0410 116 SER   U CA  
36710 C  C   . SER   U  125 ? 1.6810 0.5362 1.3152 -0.0796 -0.3510 -0.0555 116 SER   U C   
36711 O  O   . SER   U  125 ? 1.6819 0.6192 1.3463 -0.1248 -0.3130 -0.1379 116 SER   U O   
36712 C  CB  . SER   U  125 ? 1.6583 0.6136 1.2613 -0.1299 -0.3858 -0.0461 116 SER   U CB  
36713 O  OG  . SER   U  125 ? 1.6050 0.6765 1.2556 -0.1354 -0.3891 0.0015  116 SER   U OG  
36714 N  N   . GLN   U  126 ? 1.7097 0.4027 1.2832 -0.0677 -0.3489 -0.0212 117 GLN   U N   
36715 C  CA  . GLN   U  126 ? 1.7386 0.3221 1.2737 -0.0717 -0.3329 -0.0412 117 GLN   U CA  
36716 C  C   . GLN   U  126 ? 1.7337 0.2991 1.2664 -0.0439 -0.3405 -0.0249 117 GLN   U C   
36717 O  O   . GLN   U  126 ? 1.7446 0.2569 1.2719 -0.0925 -0.3523 -0.0121 117 GLN   U O   
36718 C  CB  . GLN   U  126 ? 1.7432 0.2934 1.2912 -0.0769 -0.2919 -0.0527 117 GLN   U CB  
36719 C  CG  . GLN   U  126 ? 1.7906 0.2895 1.2816 -0.0915 -0.2745 -0.0851 117 GLN   U CG  
36720 C  CD  . GLN   U  126 ? 1.8338 0.3084 1.2804 -0.0733 -0.2327 -0.1095 117 GLN   U CD  
36721 O  OE1 . GLN   U  126 ? 1.8971 0.1967 1.2767 -0.0726 -0.1426 -0.0787 117 GLN   U OE1 
36722 N  NE2 . GLN   U  126 ? 1.8066 0.3470 1.2707 -0.1171 -0.2462 -0.1292 117 GLN   U NE2 
36723 N  N   . ILE   U  127 ? 1.7190 0.3115 1.2844 -0.0478 -0.3495 -0.0073 118 ILE   U N   
36724 C  CA  . ILE   U  127 ? 1.7649 0.3946 1.2545 -0.0242 -0.3526 0.0134  118 ILE   U CA  
36725 C  C   . ILE   U  127 ? 1.8031 0.3412 1.2456 -0.0214 -0.3711 0.0436  118 ILE   U C   
36726 O  O   . ILE   U  127 ? 1.8034 0.4086 1.2212 -0.0173 -0.3969 0.0629  118 ILE   U O   
36727 C  CB  . ILE   U  127 ? 1.7541 0.3716 1.2633 -0.0054 -0.3514 0.0527  118 ILE   U CB  
36728 C  CG1 . ILE   U  127 ? 1.7448 0.4478 1.2979 0.0196  -0.3560 0.0911  118 ILE   U CG1 
36729 C  CG2 . ILE   U  127 ? 1.7776 0.3375 1.2168 0.0272  -0.3514 0.0777  118 ILE   U CG2 
36730 C  CD1 . ILE   U  127 ? 1.7360 0.4931 1.2968 -0.0050 -0.3465 0.0510  118 ILE   U CD1 
36731 N  N   . TYR   U  128 ? 1.8769 0.3197 1.2585 -0.0585 -0.3727 0.0999  119 TYR   U N   
36732 C  CA  . TYR   U  128 ? 1.8955 0.3345 1.2959 -0.0612 -0.3389 0.0925  119 TYR   U CA  
36733 C  C   . TYR   U  128 ? 1.8957 0.2965 1.2658 -0.0619 -0.3792 0.1538  119 TYR   U C   
36734 O  O   . TYR   U  128 ? 1.9244 0.1258 1.1786 -0.0935 -0.4124 0.2068  119 TYR   U O   
36735 C  CB  . TYR   U  128 ? 1.9311 0.4438 1.2724 -0.1096 -0.3242 0.0589  119 TYR   U CB  
36736 C  CG  . TYR   U  128 ? 1.9461 0.3860 1.3529 -0.1685 -0.2374 0.0732  119 TYR   U CG  
36737 C  CD1 . TYR   U  128 ? 1.9152 0.3691 1.3598 -0.1900 -0.2153 0.0339  119 TYR   U CD1 
36738 C  CD2 . TYR   U  128 ? 1.9381 0.3807 1.3558 -0.2009 -0.2158 0.0082  119 TYR   U CD2 
36739 C  CE1 . TYR   U  128 ? 1.8742 0.4058 1.3970 -0.2290 -0.1989 0.0059  119 TYR   U CE1 
36740 C  CE2 . TYR   U  128 ? 1.8931 0.3526 1.4007 -0.2387 -0.1943 0.0235  119 TYR   U CE2 
36741 C  CZ  . TYR   U  128 ? 1.8555 0.3761 1.4063 -0.2759 -0.1806 0.0153  119 TYR   U CZ  
36742 O  OH  . TYR   U  128 ? 1.7805 0.4097 1.5800 -0.3576 -0.1594 -0.0491 119 TYR   U OH  
36743 N  N   . THR   U  129 ? 1.8681 0.2450 1.2931 -0.0271 -0.4104 0.1325  120 THR   U N   
36744 C  CA  . THR   U  129 ? 1.8976 0.2373 1.3203 0.0179  -0.4231 0.0774  120 THR   U CA  
36745 C  C   . THR   U  129 ? 1.8968 0.3396 1.3245 0.0180  -0.4431 0.0477  120 THR   U C   
36746 O  O   . THR   U  129 ? 1.8866 0.3386 1.3214 0.0077  -0.4664 0.0610  120 THR   U O   
36747 C  CB  . THR   U  129 ? 1.8762 0.2079 1.3446 0.0477  -0.4197 0.0639  120 THR   U CB  
36748 O  OG1 . THR   U  129 ? 1.9310 0.1837 1.3173 0.0577  -0.4346 0.0896  120 THR   U OG1 
36749 C  CG2 . THR   U  129 ? 1.8715 0.2531 1.3444 0.0292  -0.4066 0.0494  120 THR   U CG2 
36750 N  N   . GLN   U  130 ? 1.9027 0.3266 1.4041 -0.0041 -0.4257 0.0403  121 GLN   U N   
36751 C  CA  . GLN   U  130 ? 1.9282 0.4286 1.3980 -0.0282 -0.4559 -0.0145 121 GLN   U CA  
36752 C  C   . GLN   U  130 ? 1.9396 0.5260 1.4021 -0.0364 -0.4198 -0.0622 121 GLN   U C   
36753 O  O   . GLN   U  130 ? 1.9483 0.6817 1.3936 -0.1519 -0.4268 -0.1026 121 GLN   U O   
36754 C  CB  . GLN   U  130 ? 1.9433 0.3683 1.4460 -0.0487 -0.4778 0.0116  121 GLN   U CB  
36755 C  CG  . GLN   U  130 ? 1.9775 0.3042 1.4526 -0.0707 -0.4919 0.0252  121 GLN   U CG  
36756 C  CD  . GLN   U  130 ? 1.9601 0.3475 1.4872 -0.0944 -0.5128 0.0698  121 GLN   U CD  
36757 O  OE1 . GLN   U  130 ? 1.9555 0.2145 1.4800 -0.1570 -0.4943 0.0649  121 GLN   U OE1 
36758 N  NE2 . GLN   U  130 ? 1.9449 0.4180 1.4820 -0.0526 -0.4948 0.0854  121 GLN   U NE2 
36759 N  N   . ARG   U  131 ? 1.9066 0.5448 1.5296 -0.0305 -0.4529 -0.0654 122 ARG   U N   
36760 C  CA  . ARG   U  131 ? 1.9155 0.7139 1.5897 0.0104  -0.4100 -0.0015 122 ARG   U CA  
36761 C  C   . ARG   U  131 ? 1.9532 0.6408 1.6033 0.0162  -0.3719 -0.1019 122 ARG   U C   
36762 O  O   . ARG   U  131 ? 1.9853 0.6916 1.5800 0.0119  -0.3297 -0.1300 122 ARG   U O   
36763 C  CB  . ARG   U  131 ? 1.9343 0.7703 1.7174 0.0014  -0.4565 -0.0483 122 ARG   U CB  
36764 C  CG  . ARG   U  131 ? 1.9657 0.8200 1.7531 0.0628  -0.4732 0.0240  122 ARG   U CG  
36765 C  CD  . ARG   U  131 ? 2.0037 0.8467 1.8533 0.0791  -0.5253 0.0452  122 ARG   U CD  
36766 N  NE  . ARG   U  131 ? 2.1016 0.9677 1.9054 0.1182  -0.5403 -0.0208 122 ARG   U NE  
36767 C  CZ  . ARG   U  131 ? 2.0369 1.2817 2.0001 0.2318  -0.5832 0.1229  122 ARG   U CZ  
36768 N  NH1 . ARG   U  131 ? 2.0881 1.3988 2.0163 0.1993  -0.6193 0.1157  122 ARG   U NH1 
36769 N  NH2 . ARG   U  131 ? 2.0654 1.3002 2.0276 0.2211  -0.5556 0.1004  122 ARG   U NH2 
36770 N  N   . ALA   U  132 ? 1.9900 0.6089 1.5089 0.0345  -0.3916 -0.0188 123 ALA   U N   
36771 C  CA  . ALA   U  132 ? 2.0506 0.5744 1.5435 0.0403  -0.3851 0.0318  123 ALA   U CA  
36772 C  C   . ALA   U  132 ? 2.0264 0.5819 1.6027 0.0909  -0.4136 0.1180  123 ALA   U C   
36773 O  O   . ALA   U  132 ? 2.0860 0.5268 1.6998 0.0852  -0.4328 0.1334  123 ALA   U O   
36774 C  CB  . ALA   U  132 ? 2.0812 0.5271 1.5161 0.0497  -0.4091 0.0631  123 ALA   U CB  
36775 N  N   . TYR   U  133 ? 2.0791 0.6068 1.6765 0.0505  -0.3468 0.0726  124 TYR   U N   
36776 C  CA  . TYR   U  133 ? 2.0865 0.5787 1.6163 0.0340  -0.3246 0.0646  124 TYR   U CA  
36777 C  C   . TYR   U  133 ? 2.0865 0.5224 1.6003 0.0289  -0.2823 0.1215  124 TYR   U C   
36778 O  O   . TYR   U  133 ? 2.1031 0.4446 1.5349 -0.0101 -0.2663 0.2589  124 TYR   U O   
36779 C  CB  . TYR   U  133 ? 2.0742 0.5763 1.6812 0.0383  -0.3029 0.0710  124 TYR   U CB  
36780 C  CG  . TYR   U  133 ? 2.1183 0.5545 1.7415 0.0222  -0.2947 0.0664  124 TYR   U CG  
36781 C  CD1 . TYR   U  133 ? 2.0933 0.5269 1.7773 -0.0255 -0.2926 0.0401  124 TYR   U CD1 
36782 C  CD2 . TYR   U  133 ? 2.1296 0.4626 1.7828 0.0303  -0.2939 0.0709  124 TYR   U CD2 
36783 C  CE1 . TYR   U  133 ? 2.1173 0.4734 1.8305 -0.0393 -0.2768 0.0609  124 TYR   U CE1 
36784 C  CE2 . TYR   U  133 ? 2.1739 0.4556 1.7951 -0.0249 -0.2885 0.0448  124 TYR   U CE2 
36785 C  CZ  . TYR   U  133 ? 2.1403 0.5570 1.8082 -0.0542 -0.2795 0.0437  124 TYR   U CZ  
36786 O  OH  . TYR   U  133 ? 2.1525 0.6617 1.7529 -0.0068 -0.1821 0.0264  124 TYR   U OH  
36787 N  N   . MET   U  134 ? 2.0799 0.5089 1.5545 0.0672  -0.2984 0.1251  125 MET   U N   
36788 C  CA  . MET   U  134 ? 2.0549 0.5483 1.5741 0.1088  -0.2431 0.1134  125 MET   U CA  
36789 C  C   . MET   U  134 ? 1.9423 0.5529 1.4204 0.1469  -0.2776 0.1234  125 MET   U C   
36790 O  O   . MET   U  134 ? 1.9074 0.4297 1.3384 0.1971  -0.2454 0.1170  125 MET   U O   
36791 C  CB  . MET   U  134 ? 2.0900 0.6339 1.6925 0.1379  -0.2403 0.0211  125 MET   U CB  
36792 C  CG  . MET   U  134 ? 2.1355 0.6606 1.7391 0.0917  -0.2451 -0.0097 125 MET   U CG  
36793 S  SD  . MET   U  134 ? 2.1782 0.5586 1.9114 0.1674  -0.2513 -0.1368 125 MET   U SD  
36794 C  CE  . MET   U  134 ? 2.1488 0.8444 1.8300 0.1395  -0.3455 -0.0545 125 MET   U CE  
36795 N  N   . ARG   U  135 ? 1.9191 0.5144 1.3567 0.1153  -0.2577 0.1161  126 ARG   U N   
36796 C  CA  . ARG   U  135 ? 1.9173 0.4811 1.2692 0.0791  -0.3307 0.0709  126 ARG   U CA  
36797 C  C   . ARG   U  135 ? 1.8776 0.5264 1.1960 0.0166  -0.3374 0.1269  126 ARG   U C   
36798 O  O   . ARG   U  135 ? 1.9417 0.6369 1.1406 0.1021  -0.3578 0.0187  126 ARG   U O   
36799 C  CB  . ARG   U  135 ? 1.9286 0.4746 1.2685 0.0760  -0.3358 0.0738  126 ARG   U CB  
36800 C  CG  . ARG   U  135 ? 1.9011 0.4009 1.2823 0.0775  -0.3385 0.0859  126 ARG   U CG  
36801 C  CD  . ARG   U  135 ? 1.8875 0.3824 1.2789 0.0725  -0.3501 0.0672  126 ARG   U CD  
36802 N  NE  . ARG   U  135 ? 1.8628 0.3366 1.2960 0.0801  -0.3446 0.0600  126 ARG   U NE  
36803 C  CZ  . ARG   U  135 ? 1.8413 0.3126 1.3057 0.0592  -0.3453 0.0184  126 ARG   U CZ  
36804 N  NH1 . ARG   U  135 ? 1.8422 0.2385 1.3009 0.0370  -0.3612 0.0000  126 ARG   U NH1 
36805 N  NH2 . ARG   U  135 ? 1.8449 0.3438 1.3192 0.0522  -0.3370 -0.0090 126 ARG   U NH2 
36806 N  N   . PRO   U  136 ? 1.9340 0.5250 1.1139 -0.0331 -0.3807 0.1396  127 PRO   U N   
36807 C  CA  . PRO   U  136 ? 1.9439 0.4559 1.1432 -0.0817 -0.3477 0.1309  127 PRO   U CA  
36808 C  C   . PRO   U  136 ? 1.9129 0.4014 1.1827 -0.0767 -0.3510 0.1345  127 PRO   U C   
36809 O  O   . PRO   U  136 ? 1.9642 0.3829 1.2304 -0.0382 -0.3164 0.1113  127 PRO   U O   
36810 C  CB  . PRO   U  136 ? 1.9182 0.5466 1.1219 -0.1187 -0.3691 0.1365  127 PRO   U CB  
36811 C  CG  . PRO   U  136 ? 1.9581 0.5813 1.0987 -0.0878 -0.3757 0.1627  127 PRO   U CG  
36812 C  CD  . PRO   U  136 ? 1.9441 0.5546 1.0950 -0.0757 -0.3835 0.1530  127 PRO   U CD  
36813 N  N   . LEU   U  137 ? 1.9299 0.3847 1.2062 -0.0887 -0.3165 0.1417  128 LEU   U N   
36814 C  CA  . LEU   U  137 ? 1.9270 0.3971 1.2243 -0.0622 -0.3306 0.1483  128 LEU   U CA  
36815 C  C   . LEU   U  137 ? 1.9315 0.3566 1.2510 -0.0244 -0.3499 0.1570  128 LEU   U C   
36816 O  O   . LEU   U  137 ? 1.9315 0.4501 1.2837 -0.0390 -0.3876 0.1583  128 LEU   U O   
36817 C  CB  . LEU   U  137 ? 1.8946 0.3572 1.2104 -0.0683 -0.3120 0.1847  128 LEU   U CB  
36818 C  CG  . LEU   U  137 ? 1.8600 0.3114 1.2080 -0.0264 -0.3220 0.1700  128 LEU   U CG  
36819 C  CD1 . LEU   U  137 ? 1.8152 0.2675 1.2263 -0.0423 -0.3138 0.1896  128 LEU   U CD1 
36820 C  CD2 . LEU   U  137 ? 1.8612 0.2753 1.1914 -0.0405 -0.3194 0.1901  128 LEU   U CD2 
36821 N  N   . GLY   U  138 ? 1.9628 0.3614 1.2696 0.0072  -0.3535 0.1418  129 GLY   U N   
36822 C  CA  . GLY   U  138 ? 1.9800 0.4071 1.2081 0.0085  -0.3709 0.1717  129 GLY   U CA  
36823 C  C   . GLY   U  138 ? 1.9546 0.3660 1.1893 0.0204  -0.3933 0.1823  129 GLY   U C   
36824 O  O   . GLY   U  138 ? 2.0255 0.4574 1.1598 0.0303  -0.3980 0.1907  129 GLY   U O   
36825 N  N   . VAL   U  139 ? 1.8967 0.3430 1.1719 -0.0109 -0.4338 0.1994  130 VAL   U N   
36826 C  CA  . VAL   U  139 ? 1.8348 0.4267 1.1624 -0.0397 -0.4297 0.2116  130 VAL   U CA  
36827 C  C   . VAL   U  139 ? 1.8237 0.3758 1.1580 -0.1105 -0.4270 0.1947  130 VAL   U C   
36828 O  O   . VAL   U  139 ? 1.7699 0.3059 1.1559 -0.2047 -0.4626 0.1066  130 VAL   U O   
36829 C  CB  . VAL   U  139 ? 1.7912 0.4780 1.1827 -0.0551 -0.4552 0.1788  130 VAL   U CB  
36830 C  CG1 . VAL   U  139 ? 1.7969 0.5593 1.1833 -0.0421 -0.4670 0.1844  130 VAL   U CG1 
36831 C  CG2 . VAL   U  139 ? 1.7849 0.5022 1.1886 -0.0320 -0.4362 0.1902  130 VAL   U CG2 
36832 N  N   . ILE   U  140 ? 1.8112 0.3907 1.1536 -0.1065 -0.4289 0.1876  131 ILE   U N   
36833 C  CA  . ILE   U  140 ? 1.8173 0.4192 1.2259 -0.0765 -0.4476 0.1353  131 ILE   U CA  
36834 C  C   . ILE   U  140 ? 1.8191 0.3129 1.2793 -0.0976 -0.4033 0.1671  131 ILE   U C   
36835 O  O   . ILE   U  140 ? 1.7971 0.1240 1.3644 -0.0881 -0.4636 0.1505  131 ILE   U O   
36836 C  CB  . ILE   U  140 ? 1.7968 0.4688 1.2747 -0.1377 -0.4634 0.0876  131 ILE   U CB  
36837 C  CG1 . ILE   U  140 ? 1.8628 0.6079 1.2716 -0.0929 -0.4725 0.0379  131 ILE   U CG1 
36838 C  CG2 . ILE   U  140 ? 1.7867 0.4944 1.2348 -0.1351 -0.4963 0.0254  131 ILE   U CG2 
36839 C  CD1 . ILE   U  140 ? 1.8787 0.6164 1.3312 -0.0678 -0.4616 0.0918  131 ILE   U CD1 
36840 N  N   . LEU   U  141 ? 1.7955 0.3312 1.2867 -0.0723 -0.3545 0.1517  132 LEU   U N   
36841 C  CA  . LEU   U  141 ? 1.8118 0.3823 1.2749 -0.0878 -0.2941 0.1203  132 LEU   U CA  
36842 C  C   . LEU   U  141 ? 1.8410 0.4718 1.2668 -0.1330 -0.2648 0.1324  132 LEU   U C   
36843 O  O   . LEU   U  141 ? 1.8457 0.4339 1.1937 -0.1607 -0.2426 0.1889  132 LEU   U O   
36844 C  CB  . LEU   U  141 ? 1.7794 0.3000 1.3108 -0.0515 -0.2625 0.0758  132 LEU   U CB  
36845 C  CG  . LEU   U  141 ? 1.7905 0.2606 1.3040 -0.0186 -0.2583 0.0588  132 LEU   U CG  
36846 C  CD1 . LEU   U  141 ? 1.7861 0.2755 1.2598 -0.0090 -0.2406 0.0539  132 LEU   U CD1 
36847 C  CD2 . LEU   U  141 ? 1.7862 0.2820 1.3328 -0.0142 -0.2596 0.0537  132 LEU   U CD2 
36848 N  N   . THR   U  142 ? 1.8835 0.6072 1.2732 -0.1510 -0.2748 0.1050  133 THR   U N   
36849 C  CA  . THR   U  142 ? 1.8652 0.6528 1.3310 -0.1355 -0.2810 0.0717  133 THR   U CA  
36850 C  C   . THR   U  142 ? 1.8466 0.6304 1.3093 -0.0573 -0.3070 0.0935  133 THR   U C   
36851 O  O   . THR   U  142 ? 1.8906 0.8510 1.3049 -0.0941 -0.3105 0.0363  133 THR   U O   
36852 C  CB  . THR   U  142 ? 1.8679 0.7593 1.2935 -0.1531 -0.2890 0.0975  133 THR   U CB  
36853 O  OG1 . THR   U  142 ? 1.9146 0.7856 1.3054 -0.1679 -0.3396 0.0319  133 THR   U OG1 
36854 C  CG2 . THR   U  142 ? 1.8713 0.7973 1.2779 -0.1677 -0.2821 0.0961  133 THR   U CG2 
36855 N  N   . PHE   U  143 ? 1.8892 0.5442 1.2752 -0.0552 -0.2974 0.0928  134 PHE   U N   
36856 C  CA  . PHE   U  143 ? 1.8574 0.5209 1.2368 0.0035  -0.2976 0.1291  134 PHE   U CA  
36857 C  C   . PHE   U  143 ? 1.8185 0.4339 1.2541 0.0136  -0.3038 0.1494  134 PHE   U C   
36858 O  O   . PHE   U  143 ? 1.8244 0.3586 1.2295 0.0179  -0.2878 0.1578  134 PHE   U O   
36859 C  CB  . PHE   U  143 ? 1.8672 0.4298 1.2291 0.0253  -0.2908 0.0871  134 PHE   U CB  
36860 C  CG  . PHE   U  143 ? 1.8940 0.3850 1.1895 0.0037  -0.3006 0.1085  134 PHE   U CG  
36861 C  CD1 . PHE   U  143 ? 1.9041 0.3796 1.1565 0.0048  -0.3333 0.1055  134 PHE   U CD1 
36862 C  CD2 . PHE   U  143 ? 1.9353 0.4021 1.1829 -0.0153 -0.3050 0.1117  134 PHE   U CD2 
36863 C  CE1 . PHE   U  143 ? 1.9132 0.3852 1.1349 0.0017  -0.3453 0.1128  134 PHE   U CE1 
36864 C  CE2 . PHE   U  143 ? 1.9427 0.3939 1.1894 -0.0182 -0.3017 0.1253  134 PHE   U CE2 
36865 C  CZ  . PHE   U  143 ? 1.9395 0.3835 1.1578 -0.0010 -0.3324 0.0967  134 PHE   U CZ  
36866 N  N   . VAL   U  144 ? 1.7926 0.4795 1.2219 0.0246  -0.3169 0.1673  135 VAL   U N   
36867 C  CA  . VAL   U  144 ? 1.7656 0.5544 1.2216 0.0118  -0.3187 0.1917  135 VAL   U CA  
36868 C  C   . VAL   U  144 ? 1.7672 0.5762 1.2082 0.0149  -0.3173 0.1645  135 VAL   U C   
36869 O  O   . VAL   U  144 ? 1.7521 0.5772 1.1779 0.0156  -0.3448 0.1309  135 VAL   U O   
36870 C  CB  . VAL   U  144 ? 1.7676 0.5350 1.2287 0.0038  -0.3223 0.1929  135 VAL   U CB  
36871 C  CG1 . VAL   U  144 ? 1.7577 0.5513 1.2434 -0.0315 -0.3201 0.1924  135 VAL   U CG1 
36872 C  CG2 . VAL   U  144 ? 1.7772 0.5245 1.2319 -0.0021 -0.3238 0.1815  135 VAL   U CG2 
36873 N  N   . SER   U  145 ? 1.7519 0.6456 1.2233 0.0121  -0.2991 0.2103  136 SER   U N   
36874 C  CA  . SER   U  145 ? 1.7487 0.6683 1.2349 0.0395  -0.2948 0.2012  136 SER   U CA  
36875 C  C   . SER   U  145 ? 1.7424 0.7006 1.2517 0.0186  -0.2941 0.2781  136 SER   U C   
36876 O  O   . SER   U  145 ? 1.7869 0.5523 1.2197 0.1025  -0.3255 0.2810  136 SER   U O   
36877 C  CB  . SER   U  145 ? 1.7420 0.7022 1.2448 0.0329  -0.2857 0.2191  136 SER   U CB  
36878 O  OG  . SER   U  145 ? 1.7364 0.7591 1.2640 0.0170  -0.2839 0.1933  136 SER   U OG  
36879 N  N   . VAL   U  146 ? 1.7834 0.7283 1.2868 0.0198  -0.3019 0.2598  137 VAL   U N   
36880 C  CA  . VAL   U  146 ? 1.7737 0.7735 1.3186 -0.0301 -0.2613 0.2989  137 VAL   U CA  
36881 C  C   . VAL   U  146 ? 1.7644 0.7416 1.3805 -0.0779 -0.2685 0.3150  137 VAL   U C   
36882 O  O   . VAL   U  146 ? 1.7979 0.7339 1.3965 -0.1592 -0.2275 0.3693  137 VAL   U O   
36883 C  CB  . VAL   U  146 ? 1.7971 0.7565 1.2887 -0.0334 -0.2530 0.3549  137 VAL   U CB  
36884 C  CG1 . VAL   U  146 ? 1.8084 0.6960 1.2420 -0.0347 -0.2333 0.4190  137 VAL   U CG1 
36885 C  CG2 . VAL   U  146 ? 1.7860 0.7739 1.2736 0.0006  -0.2585 0.3314  137 VAL   U CG2 
36886 N  N   . ASP   U  147 ? 1.6859 0.7992 1.4419 -0.1404 -0.2797 0.2601  138 ASP   U N   
36887 C  CA  . ASP   U  147 ? 1.6660 0.8082 1.4359 -0.1404 -0.2741 0.2532  138 ASP   U CA  
36888 C  C   . ASP   U  147 ? 1.7246 0.7977 1.5343 -0.1016 -0.2879 0.2106  138 ASP   U C   
36889 O  O   . ASP   U  147 ? 1.7351 0.8121 1.5392 -0.0858 -0.2631 0.1921  138 ASP   U O   
36890 C  CB  . ASP   U  147 ? 1.6815 0.9289 1.4138 -0.1932 -0.2560 0.2536  138 ASP   U CB  
36891 C  CG  . ASP   U  147 ? 1.6716 1.0362 1.3372 -0.2628 -0.2370 0.2574  138 ASP   U CG  
36892 O  OD1 . ASP   U  147 ? 1.6759 1.0784 1.3751 -0.3275 -0.2530 0.2098  138 ASP   U OD1 
36893 O  OD2 . ASP   U  147 ? 1.6656 1.2810 1.3122 -0.2820 -0.2813 0.1682  138 ASP   U OD2 
36894 N  N   . GLU   U  148 ? 1.7166 0.7472 1.5715 0.0116  -0.2577 0.1585  139 GLU   U N   
36895 C  CA  . GLU   U  148 ? 1.7601 0.7466 1.6363 0.0584  -0.2314 0.1884  139 GLU   U CA  
36896 C  C   . GLU   U  148 ? 1.7160 0.6333 1.6245 0.1029  -0.1776 0.1478  139 GLU   U C   
36897 O  O   . GLU   U  148 ? 1.7183 0.6484 1.7425 0.1740  -0.1467 0.2105  139 GLU   U O   
36898 C  CB  . GLU   U  148 ? 1.7924 0.7399 1.6445 0.0811  -0.2228 0.2250  139 GLU   U CB  
36899 C  CG  . GLU   U  148 ? 1.8149 0.7895 1.6428 0.1401  -0.2402 0.2313  139 GLU   U CG  
36900 C  CD  . GLU   U  148 ? 1.8837 0.7255 1.6787 0.2102  -0.2651 0.1887  139 GLU   U CD  
36901 O  OE1 . GLU   U  148 ? 1.9125 0.7192 1.6198 0.2782  -0.2842 0.2356  139 GLU   U OE1 
36902 O  OE2 . GLU   U  148 ? 1.9540 0.6746 1.8058 0.2632  -0.2970 0.1550  139 GLU   U OE2 
36903 N  N   . GLU   U  149 ? 1.6914 0.6734 1.6100 0.0759  -0.1748 0.1428  140 GLU   U N   
36904 C  CA  . GLU   U  149 ? 1.6817 0.7434 1.6052 0.0471  -0.1536 0.1285  140 GLU   U CA  
36905 C  C   . GLU   U  149 ? 1.6574 0.7741 1.5412 -0.0007 -0.1607 0.1212  140 GLU   U C   
36906 O  O   . GLU   U  149 ? 1.6004 0.7890 1.5845 -0.0132 -0.2078 0.0959  140 GLU   U O   
36907 C  CB  . GLU   U  149 ? 1.6715 0.8798 1.6006 0.0353  -0.1342 0.1036  140 GLU   U CB  
36908 C  CG  . GLU   U  149 ? 1.6853 0.8727 1.6867 -0.0328 -0.0725 0.0408  140 GLU   U CG  
36909 C  CD  . GLU   U  149 ? 1.6166 1.0538 1.6723 -0.0611 -0.0696 -0.0010 140 GLU   U CD  
36910 O  OE1 . GLU   U  149 ? 1.5986 1.0693 1.8171 -0.1111 -0.0370 -0.0357 140 GLU   U OE1 
36911 O  OE2 . GLU   U  149 ? 1.5369 1.2013 1.7516 -0.0795 0.0063  -0.0808 140 GLU   U OE2 
36912 N  N   . LEU   U  150 ? 1.7003 0.6989 1.4568 -0.0506 -0.1573 0.1013  141 LEU   U N   
36913 C  CA  . LEU   U  150 ? 1.7363 0.6864 1.4292 -0.0367 -0.1527 0.1575  141 LEU   U CA  
36914 C  C   . LEU   U  150 ? 1.7364 0.6501 1.4008 -0.0333 -0.1580 0.1218  141 LEU   U C   
36915 O  O   . LEU   U  150 ? 1.7696 0.6456 1.3586 -0.0349 -0.1366 0.1057  141 LEU   U O   
36916 C  CB  . LEU   U  150 ? 1.7703 0.6490 1.3800 -0.0414 -0.1455 0.2033  141 LEU   U CB  
36917 C  CG  . LEU   U  150 ? 1.7595 0.6601 1.3787 -0.0485 -0.1461 0.2164  141 LEU   U CG  
36918 C  CD1 . LEU   U  150 ? 1.7880 0.5994 1.3379 -0.0714 -0.1516 0.2303  141 LEU   U CD1 
36919 C  CD2 . LEU   U  150 ? 1.7560 0.6871 1.3661 -0.0398 -0.1563 0.2319  141 LEU   U CD2 
36920 N  N   . GLY   U  151 ? 1.7455 0.6255 1.4132 -0.0323 -0.1622 0.1224  142 GLY   U N   
36921 C  CA  . GLY   U  151 ? 1.7909 0.6366 1.4112 -0.0183 -0.1532 0.1225  142 GLY   U CA  
36922 C  C   . GLY   U  151 ? 1.8284 0.5755 1.3957 -0.0226 -0.1929 0.1350  142 GLY   U C   
36923 O  O   . GLY   U  151 ? 1.8506 0.6022 1.4284 -0.0250 -0.1691 0.0843  142 GLY   U O   
36924 N  N   . PRO   U  152 ? 1.7950 0.5074 1.3755 -0.0170 -0.1758 0.1006  143 PRO   U N   
36925 C  CA  . PRO   U  152 ? 1.8070 0.4548 1.3759 -0.0294 -0.2015 0.1171  143 PRO   U CA  
36926 C  C   . PRO   U  152 ? 1.7855 0.4156 1.3963 -0.0079 -0.2440 0.1121  143 PRO   U C   
36927 O  O   . PRO   U  152 ? 1.7833 0.3614 1.4445 -0.0089 -0.2476 0.1302  143 PRO   U O   
36928 C  CB  . PRO   U  152 ? 1.7946 0.4507 1.4063 -0.0361 -0.1781 0.1202  143 PRO   U CB  
36929 C  CG  . PRO   U  152 ? 1.8075 0.4566 1.4486 -0.0288 -0.1491 0.1202  143 PRO   U CG  
36930 C  CD  . PRO   U  152 ? 1.8019 0.5092 1.4068 -0.0410 -0.1572 0.1288  143 PRO   U CD  
36931 N  N   . SER   U  153 ? 1.7793 0.4408 1.4118 0.0379  -0.2540 0.1137  144 SER   U N   
36932 C  CA  . SER   U  153 ? 1.7854 0.4665 1.4170 0.0544  -0.2539 0.1063  144 SER   U CA  
36933 C  C   . SER   U  153 ? 1.7933 0.4229 1.3626 0.0518  -0.2735 0.1500  144 SER   U C   
36934 O  O   . SER   U  153 ? 1.7928 0.4207 1.3313 0.0505  -0.2818 0.1967  144 SER   U O   
36935 C  CB  . SER   U  153 ? 1.7715 0.4414 1.4304 0.0904  -0.2470 0.0927  144 SER   U CB  
36936 O  OG  . SER   U  153 ? 1.7827 0.4729 1.5029 0.1106  -0.2624 0.0560  144 SER   U OG  
36937 N  N   . ILE   U  154 ? 1.8116 0.4412 1.3397 0.0607  -0.2670 0.1327  145 ILE   U N   
36938 C  CA  . ILE   U  154 ? 1.8183 0.3745 1.2971 0.0404  -0.2818 0.1370  145 ILE   U CA  
36939 C  C   . ILE   U  154 ? 1.7992 0.4095 1.3115 0.0113  -0.3041 0.1194  145 ILE   U C   
36940 O  O   . ILE   U  154 ? 1.8301 0.4077 1.3680 -0.0164 -0.3322 0.1104  145 ILE   U O   
36941 C  CB  . ILE   U  154 ? 1.8356 0.3550 1.2926 0.0521  -0.2695 0.1256  145 ILE   U CB  
36942 C  CG1 . ILE   U  154 ? 1.8653 0.3475 1.3017 0.0571  -0.2331 0.1202  145 ILE   U CG1 
36943 C  CG2 . ILE   U  154 ? 1.8457 0.3217 1.2363 0.0502  -0.2773 0.1430  145 ILE   U CG2 
36944 C  CD1 . ILE   U  154 ? 1.8865 0.3944 1.3529 0.0402  -0.1895 0.1408  145 ILE   U CD1 
36945 N  N   . TYR   U  155 ? 1.7993 0.4143 1.2981 0.0026  -0.3162 0.1357  146 TYR   U N   
36946 C  CA  . TYR   U  155 ? 1.8196 0.4487 1.2993 -0.0258 -0.3405 0.1214  146 TYR   U CA  
36947 C  C   . TYR   U  155 ? 1.8258 0.3997 1.2993 -0.0465 -0.3234 0.1593  146 TYR   U C   
36948 O  O   . TYR   U  155 ? 1.8752 0.4133 1.2964 -0.1305 -0.3225 0.1764  146 TYR   U O   
36949 C  CB  . TYR   U  155 ? 1.7759 0.4457 1.2552 -0.0023 -0.3594 0.0928  146 TYR   U CB  
36950 C  CG  . TYR   U  155 ? 1.7784 0.5308 1.2863 0.0143  -0.3524 0.0338  146 TYR   U CG  
36951 C  CD1 . TYR   U  155 ? 1.7785 0.4985 1.3074 0.0175  -0.3698 -0.0053 146 TYR   U CD1 
36952 C  CD2 . TYR   U  155 ? 1.7683 0.5293 1.3051 0.0334  -0.3575 0.0235  146 TYR   U CD2 
36953 C  CE1 . TYR   U  155 ? 1.7841 0.4986 1.3464 0.0322  -0.3752 -0.0114 146 TYR   U CE1 
36954 C  CE2 . TYR   U  155 ? 1.7649 0.4965 1.3504 0.0348  -0.3630 0.0009  146 TYR   U CE2 
36955 C  CZ  . TYR   U  155 ? 1.7566 0.4885 1.3638 0.0400  -0.3759 -0.0165 146 TYR   U CZ  
36956 O  OH  . TYR   U  155 ? 1.7480 0.5205 1.4387 0.0307  -0.3875 -0.0626 146 TYR   U OH  
36957 N  N   . LYS   U  156 ? 1.8795 0.3378 1.3048 -0.0578 -0.3204 0.1946  147 LYS   U N   
36958 C  CA  . LYS   U  156 ? 1.8927 0.3623 1.3172 -0.0428 -0.3126 0.1805  147 LYS   U CA  
36959 C  C   . LYS   U  156 ? 1.8799 0.2105 1.3100 -0.0582 -0.3293 0.1890  147 LYS   U C   
36960 O  O   . LYS   U  156 ? 1.8596 0.0608 1.3420 -0.0977 -0.3190 0.1326  147 LYS   U O   
36961 C  CB  . LYS   U  156 ? 1.9355 0.3681 1.3554 -0.0655 -0.2922 0.1773  147 LYS   U CB  
36962 C  CG  . LYS   U  156 ? 1.9442 0.4335 1.3578 -0.0409 -0.2860 0.1520  147 LYS   U CG  
36963 C  CD  . LYS   U  156 ? 1.9754 0.4536 1.3677 -0.0670 -0.2820 0.1666  147 LYS   U CD  
36964 C  CE  . LYS   U  156 ? 1.9900 0.5131 1.3870 -0.1099 -0.2750 0.1436  147 LYS   U CE  
36965 N  NZ  . LYS   U  156 ? 2.0116 0.6148 1.4080 -0.0904 -0.2749 0.2039  147 LYS   U NZ  
36966 N  N   . THR   U  157 ? 1.8772 0.2359 1.3194 -0.0553 -0.3411 0.2012  148 THR   U N   
36967 C  CA  . THR   U  157 ? 1.9450 0.3774 1.3074 -0.0579 -0.3538 0.1720  148 THR   U CA  
36968 C  C   . THR   U  157 ? 1.9157 0.3328 1.3364 -0.1079 -0.3528 0.1562  148 THR   U C   
36969 O  O   . THR   U  157 ? 1.8955 0.3845 1.3065 -0.1934 -0.4047 0.0939  148 THR   U O   
36970 C  CB  . THR   U  157 ? 1.9555 0.4381 1.3234 -0.0919 -0.3258 0.1706  148 THR   U CB  
36971 O  OG1 . THR   U  157 ? 1.9953 0.5552 1.3263 -0.0072 -0.3583 0.1394  148 THR   U OG1 
36972 C  CG2 . THR   U  157 ? 1.9513 0.5054 1.3507 -0.0491 -0.3036 0.1408  148 THR   U CG2 
36973 N  N   . ASP   U  158 ? 1.9081 0.3769 1.3120 -0.0974 -0.3418 0.1819  149 ASP   U N   
36974 C  CA  . ASP   U  158 ? 1.9049 0.4529 1.3698 -0.0478 -0.3137 0.1937  149 ASP   U CA  
36975 C  C   . ASP   U  158 ? 1.8942 0.4525 1.3831 -0.0222 -0.3090 0.2365  149 ASP   U C   
36976 O  O   . ASP   U  158 ? 1.9026 0.4771 1.4308 0.0199  -0.2828 0.2587  149 ASP   U O   
36977 C  CB  . ASP   U  158 ? 1.9433 0.4714 1.4306 -0.0732 -0.3368 0.1803  149 ASP   U CB  
36978 C  CG  . ASP   U  158 ? 1.9689 0.5067 1.4470 -0.0959 -0.3616 0.1505  149 ASP   U CG  
36979 O  OD1 . ASP   U  158 ? 2.0031 0.4591 1.4372 -0.0846 -0.3603 0.1280  149 ASP   U OD1 
36980 O  OD2 . ASP   U  158 ? 1.9752 0.5706 1.5205 -0.1209 -0.3492 0.1529  149 ASP   U OD2 
36981 N  N   . PRO   U  159 ? 1.9079 0.4157 1.3386 -0.0225 -0.3325 0.2329  150 PRO   U N   
36982 C  CA  . PRO   U  159 ? 1.8948 0.3762 1.3239 -0.0172 -0.3415 0.1834  150 PRO   U CA  
36983 C  C   . PRO   U  159 ? 1.8436 0.3125 1.3786 -0.0041 -0.3625 0.1454  150 PRO   U C   
36984 O  O   . PRO   U  159 ? 1.8707 0.3428 1.3286 0.0855  -0.3932 0.1755  150 PRO   U O   
36985 C  CB  . PRO   U  159 ? 1.9364 0.3268 1.2934 -0.0296 -0.3517 0.1840  150 PRO   U CB  
36986 C  CG  . PRO   U  159 ? 1.9455 0.3770 1.3002 -0.0211 -0.3413 0.2075  150 PRO   U CG  
36987 C  CD  . PRO   U  159 ? 1.9417 0.3981 1.3291 -0.0250 -0.3342 0.2219  150 PRO   U CD  
36988 N  N   . ALA   U  160 ? 1.8323 0.2988 1.4079 -0.0006 -0.3768 0.1135  151 ALA   U N   
36989 C  CA  . ALA   U  160 ? 1.8513 0.3760 1.3979 0.0194  -0.3862 0.1113  151 ALA   U CA  
36990 C  C   . ALA   U  160 ? 1.7932 0.3996 1.4114 0.0257  -0.3839 0.1390  151 ALA   U C   
36991 O  O   . ALA   U  160 ? 1.7406 0.4183 1.4136 0.0256  -0.3809 0.1147  151 ALA   U O   
36992 C  CB  . ALA   U  160 ? 1.8348 0.4652 1.4041 -0.0079 -0.3933 0.0956  151 ALA   U CB  
36993 N  N   . GLY   U  161 ? 1.7974 0.4294 1.4056 0.0526  -0.3768 0.1334  152 GLY   U N   
36994 C  CA  . GLY   U  161 ? 1.8094 0.4378 1.4641 0.0648  -0.3760 0.1630  152 GLY   U CA  
36995 C  C   . GLY   U  161 ? 1.8089 0.4409 1.4956 0.0552  -0.3753 0.1889  152 GLY   U C   
36996 O  O   . GLY   U  161 ? 1.7834 0.5120 1.5854 0.0957  -0.4301 0.1558  152 GLY   U O   
36997 N  N   . TYR   U  162 ? 1.8335 0.4880 1.4911 0.0186  -0.3598 0.2036  153 TYR   U N   
36998 C  CA  . TYR   U  162 ? 1.8333 0.4854 1.5154 0.0129  -0.3528 0.1854  153 TYR   U CA  
36999 C  C   . TYR   U  162 ? 1.8197 0.3464 1.5328 0.0297  -0.3263 0.2031  153 TYR   U C   
37000 O  O   . TYR   U  162 ? 1.8403 0.2999 1.5140 -0.0490 -0.3245 0.1947  153 TYR   U O   
37001 C  CB  . TYR   U  162 ? 1.8568 0.4883 1.5603 -0.0009 -0.3490 0.1714  153 TYR   U CB  
37002 C  CG  . TYR   U  162 ? 1.8819 0.5812 1.6054 -0.0045 -0.3172 0.1832  153 TYR   U CG  
37003 C  CD1 . TYR   U  162 ? 1.8909 0.6443 1.6029 0.0023  -0.3242 0.1704  153 TYR   U CD1 
37004 C  CD2 . TYR   U  162 ? 1.9013 0.7118 1.6527 0.0011  -0.3396 0.1861  153 TYR   U CD2 
37005 C  CE1 . TYR   U  162 ? 1.9068 0.8217 1.6623 0.0179  -0.2785 0.1515  153 TYR   U CE1 
37006 C  CE2 . TYR   U  162 ? 1.9364 0.8309 1.6818 0.0058  -0.2955 0.1678  153 TYR   U CE2 
37007 C  CZ  . TYR   U  162 ? 1.9269 0.8914 1.6738 0.0137  -0.2936 0.1375  153 TYR   U CZ  
37008 O  OH  . TYR   U  162 ? 1.9519 0.9624 1.8007 -0.0309 -0.2260 0.0593  153 TYR   U OH  
37009 N  N   . TYR   U  163 ? 1.8479 0.1795 1.4950 0.0325  -0.3565 0.1783  154 TYR   U N   
37010 C  CA  . TYR   U  163 ? 1.8691 0.2723 1.4888 0.0228  -0.3649 0.1523  154 TYR   U CA  
37011 C  C   . TYR   U  163 ? 1.8804 0.2923 1.4802 -0.0268 -0.3507 0.1374  154 TYR   U C   
37012 O  O   . TYR   U  163 ? 1.8596 0.4676 1.5206 -0.0761 -0.3665 0.0554  154 TYR   U O   
37013 C  CB  . TYR   U  163 ? 1.8691 0.2940 1.4790 0.0051  -0.3635 0.1362  154 TYR   U CB  
37014 C  CG  . TYR   U  163 ? 1.8903 0.3738 1.4409 0.0603  -0.3861 0.1422  154 TYR   U CG  
37015 C  CD1 . TYR   U  163 ? 1.8748 0.3291 1.4661 0.0819  -0.4116 0.1504  154 TYR   U CD1 
37016 C  CD2 . TYR   U  163 ? 1.8799 0.3565 1.4882 0.1270  -0.3680 0.1487  154 TYR   U CD2 
37017 C  CE1 . TYR   U  163 ? 1.8517 0.3134 1.4701 0.0663  -0.4026 0.1097  154 TYR   U CE1 
37018 C  CE2 . TYR   U  163 ? 1.8917 0.3110 1.4789 0.1032  -0.3693 0.1822  154 TYR   U CE2 
37019 C  CZ  . TYR   U  163 ? 1.8418 0.1944 1.4957 0.1164  -0.3830 0.1576  154 TYR   U CZ  
37020 O  OH  . TYR   U  163 ? 1.9591 0.0980 1.6146 0.0565  -0.3684 0.2058  154 TYR   U OH  
37021 N  N   . VAL   U  164 ? 1.8971 0.3164 1.4771 -0.0346 -0.3534 0.1476  155 VAL   U N   
37022 C  CA  . VAL   U  164 ? 1.9211 0.3719 1.4838 -0.0491 -0.3341 0.1387  155 VAL   U CA  
37023 C  C   . VAL   U  164 ? 1.9300 0.4533 1.4928 -0.0237 -0.3359 0.1050  155 VAL   U C   
37024 O  O   . VAL   U  164 ? 1.9251 0.4835 1.4499 -0.0005 -0.3248 0.0955  155 VAL   U O   
37025 C  CB  . VAL   U  164 ? 1.9818 0.3718 1.5346 -0.0719 -0.3311 0.1480  155 VAL   U CB  
37026 C  CG1 . VAL   U  164 ? 1.9648 0.4170 1.5252 -0.0567 -0.3328 0.1521  155 VAL   U CG1 
37027 C  CG2 . VAL   U  164 ? 1.9808 0.3118 1.5452 -0.0706 -0.3432 0.1851  155 VAL   U CG2 
37028 N  N   . GLY   U  165 ? 1.9606 0.5025 1.5024 -0.0262 -0.3030 0.0830  156 GLY   U N   
37029 C  CA  . GLY   U  165 ? 1.9660 0.4492 1.4796 -0.0584 -0.2765 0.1594  156 GLY   U CA  
37030 C  C   . GLY   U  165 ? 1.9421 0.4029 1.5088 -0.0999 -0.2790 0.1165  156 GLY   U C   
37031 O  O   . GLY   U  165 ? 1.9564 0.2468 1.4663 -0.1187 -0.2317 0.2111  156 GLY   U O   
37032 N  N   . TYR   U  166 ? 1.9420 0.4821 1.4971 -0.0834 -0.2391 0.1561  157 TYR   U N   
37033 C  CA  . TYR   U  166 ? 1.9185 0.5014 1.5032 -0.0689 -0.2531 0.1731  157 TYR   U CA  
37034 C  C   . TYR   U  166 ? 1.9126 0.6238 1.5171 -0.0559 -0.2064 0.2220  157 TYR   U C   
37035 O  O   . TYR   U  166 ? 1.9178 0.6472 1.5507 -0.0416 -0.2102 0.1991  157 TYR   U O   
37036 C  CB  . TYR   U  166 ? 1.9286 0.4821 1.4735 -0.0582 -0.2468 0.1644  157 TYR   U CB  
37037 C  CG  . TYR   U  166 ? 1.9369 0.4518 1.4777 -0.0493 -0.2445 0.1715  157 TYR   U CG  
37038 C  CD1 . TYR   U  166 ? 1.9158 0.4249 1.4708 -0.0538 -0.2388 0.1382  157 TYR   U CD1 
37039 C  CD2 . TYR   U  166 ? 1.9752 0.4251 1.4986 -0.0026 -0.2251 0.1787  157 TYR   U CD2 
37040 C  CE1 . TYR   U  166 ? 1.9223 0.3952 1.4867 -0.0396 -0.2262 0.1482  157 TYR   U CE1 
37041 C  CE2 . TYR   U  166 ? 1.9746 0.4154 1.4978 0.0157  -0.2275 0.1887  157 TYR   U CE2 
37042 C  CZ  . TYR   U  166 ? 1.9638 0.3595 1.4771 0.0238  -0.2262 0.1598  157 TYR   U CZ  
37043 O  OH  . TYR   U  166 ? 1.9689 0.2773 1.4624 0.0590  -0.2463 0.1868  157 TYR   U OH  
37044 N  N   . LYS   U  167 ? 1.9365 0.5380 1.6127 -0.1017 -0.2634 0.1959  158 LYS   U N   
37045 C  CA  . LYS   U  167 ? 1.9332 0.5662 1.6263 -0.1225 -0.2569 0.2304  158 LYS   U CA  
37046 C  C   . LYS   U  167 ? 1.9320 0.4583 1.6112 -0.1074 -0.2457 0.2406  158 LYS   U C   
37047 O  O   . LYS   U  167 ? 1.8899 0.2922 1.6737 -0.1757 -0.2513 0.2551  158 LYS   U O   
37048 C  CB  . LYS   U  167 ? 1.9755 0.6470 1.7302 -0.1909 -0.2605 0.1825  158 LYS   U CB  
37049 C  CG  . LYS   U  167 ? 1.9637 0.7074 1.7911 -0.2373 -0.2814 0.1797  158 LYS   U CG  
37050 C  CD  . LYS   U  167 ? 1.9959 0.7613 1.8822 -0.2922 -0.2615 0.2136  158 LYS   U CD  
37051 C  CE  . LYS   U  167 ? 2.0047 0.7547 1.9162 -0.3474 -0.2818 0.2202  158 LYS   U CE  
37052 N  NZ  . LYS   U  167 ? 2.1279 0.7330 1.9560 -0.3773 -0.2612 0.2420  158 LYS   U NZ  
37053 N  N   . ALA   U  168 ? 1.9172 0.4808 1.5310 -0.0792 -0.2918 0.2464  159 ALA   U N   
37054 C  CA  . ALA   U  168 ? 1.9179 0.4831 1.4642 -0.0505 -0.2779 0.2171  159 ALA   U CA  
37055 C  C   . ALA   U  168 ? 1.8733 0.4667 1.3965 -0.0694 -0.3239 0.2235  159 ALA   U C   
37056 O  O   . ALA   U  168 ? 1.8596 0.4377 1.3430 -0.0422 -0.3124 0.2675  159 ALA   U O   
37057 C  CB  . ALA   U  168 ? 1.9349 0.5035 1.4615 -0.0148 -0.2815 0.2264  159 ALA   U CB  
37058 N  N   . THR   U  169 ? 1.8650 0.4965 1.3783 -0.1014 -0.3397 0.1962  160 THR   U N   
37059 C  CA  . THR   U  169 ? 1.9238 0.4911 1.3387 -0.1179 -0.3736 0.1640  160 THR   U CA  
37060 C  C   . THR   U  169 ? 1.9639 0.4866 1.3770 -0.0896 -0.3878 0.1956  160 THR   U C   
37061 O  O   . THR   U  169 ? 1.9987 0.5173 1.3868 -0.0644 -0.4347 0.2153  160 THR   U O   
37062 C  CB  . THR   U  169 ? 1.9528 0.4306 1.3096 -0.1361 -0.3704 0.1186  160 THR   U CB  
37063 O  OG1 . THR   U  169 ? 1.9860 0.5440 1.3135 -0.1641 -0.3588 0.0558  160 THR   U OG1 
37064 C  CG2 . THR   U  169 ? 1.9722 0.4018 1.3078 -0.1359 -0.3613 0.1386  160 THR   U CG2 
37065 N  N   . ALA   U  170 ? 1.9227 0.4509 1.3422 -0.1026 -0.4180 0.2150  161 ALA   U N   
37066 C  CA  . ALA   U  170 ? 1.9005 0.4363 1.3475 -0.1312 -0.4063 0.2446  161 ALA   U CA  
37067 C  C   . ALA   U  170 ? 1.9102 0.3917 1.3442 -0.1384 -0.3943 0.2803  161 ALA   U C   
37068 O  O   . ALA   U  170 ? 1.8906 0.2179 1.3104 -0.1572 -0.3735 0.3662  161 ALA   U O   
37069 C  CB  . ALA   U  170 ? 1.8942 0.4297 1.3519 -0.1387 -0.4246 0.2416  161 ALA   U CB  
37070 N  N   . THR   U  171 ? 1.9195 0.4376 1.3631 -0.0948 -0.4154 0.3070  162 THR   U N   
37071 C  CA  . THR   U  171 ? 1.9619 0.5310 1.3762 -0.0273 -0.4177 0.2992  162 THR   U CA  
37072 C  C   . THR   U  171 ? 2.0122 0.4128 1.3649 -0.0266 -0.4301 0.2755  162 THR   U C   
37073 O  O   . THR   U  171 ? 2.0465 0.3485 1.3698 -0.0583 -0.4178 0.2411  162 THR   U O   
37074 C  CB  . THR   U  171 ? 1.9513 0.6265 1.4096 -0.0274 -0.4151 0.3877  162 THR   U CB  
37075 O  OG1 . THR   U  171 ? 1.9566 0.6953 1.5035 0.0046  -0.4591 0.4699  162 THR   U OG1 
37076 C  CG2 . THR   U  171 ? 1.9530 0.7559 1.4395 -0.0033 -0.3952 0.3542  162 THR   U CG2 
37077 N  N   . GLY   U  172 ? 2.0264 0.4473 1.3804 0.0141  -0.4630 0.2435  163 GLY   U N   
37078 C  CA  . GLY   U  172 ? 2.0292 0.5096 1.3289 0.0466  -0.4829 0.1870  163 GLY   U CA  
37079 C  C   . GLY   U  172 ? 2.0284 0.5037 1.3147 0.0675  -0.5135 0.1913  163 GLY   U C   
37080 O  O   . GLY   U  172 ? 2.0618 0.4072 1.3139 0.0373  -0.5184 0.2044  163 GLY   U O   
37081 N  N   . PRO   U  173 ? 2.0418 0.5110 1.2811 0.0790  -0.5145 0.1884  164 PRO   U N   
37082 C  CA  . PRO   U  173 ? 2.0572 0.5006 1.2575 0.0817  -0.5208 0.2194  164 PRO   U CA  
37083 C  C   . PRO   U  173 ? 2.0760 0.5052 1.2474 0.1267  -0.4874 0.2638  164 PRO   U C   
37084 O  O   . PRO   U  173 ? 2.0779 0.4622 1.1974 0.1116  -0.4940 0.3485  164 PRO   U O   
37085 C  CB  . PRO   U  173 ? 2.0787 0.4959 1.2447 0.0819  -0.5326 0.2544  164 PRO   U CB  
37086 C  CG  . PRO   U  173 ? 2.0512 0.5168 1.2433 0.0803  -0.5128 0.2347  164 PRO   U CG  
37087 C  CD  . PRO   U  173 ? 2.0386 0.5276 1.2656 0.0735  -0.5084 0.2004  164 PRO   U CD  
37088 N  N   . LYS   U  174 ? 2.0756 0.4998 1.3011 0.1376  -0.4852 0.1622  165 LYS   U N   
37089 C  CA  . LYS   U  174 ? 2.0818 0.5693 1.4233 0.1115  -0.4327 0.1141  165 LYS   U CA  
37090 C  C   . LYS   U  174 ? 2.0697 0.5733 1.4308 0.0924  -0.4067 0.0403  165 LYS   U C   
37091 O  O   . LYS   U  174 ? 2.0511 0.5476 1.4265 0.0676  -0.4017 0.0542  165 LYS   U O   
37092 C  CB  . LYS   U  174 ? 2.1081 0.7061 1.4374 0.1302  -0.4682 0.1072  165 LYS   U CB  
37093 C  CG  . LYS   U  174 ? 2.0901 0.8382 1.5322 0.2179  -0.5166 0.1116  165 LYS   U CG  
37094 C  CD  . LYS   U  174 ? 2.1227 0.9692 1.5429 0.2102  -0.5301 0.1445  165 LYS   U CD  
37095 C  CE  . LYS   U  174 ? 2.1413 1.1190 1.6075 0.2028  -0.5545 0.0944  165 LYS   U CE  
37096 N  NZ  . LYS   U  174 ? 2.1178 1.2765 1.6594 0.2074  -0.5486 0.1129  165 LYS   U NZ  
37097 N  N   . GLN   U  175 ? 2.0653 0.5791 1.4229 0.0902  -0.3917 0.0310  166 GLN   U N   
37098 C  CA  . GLN   U  175 ? 2.0337 0.5658 1.5249 0.0694  -0.3312 0.0079  166 GLN   U CA  
37099 C  C   . GLN   U  175 ? 2.0355 0.6672 1.6057 0.0528  -0.3123 0.0895  166 GLN   U C   
37100 O  O   . GLN   U  175 ? 1.9314 0.6139 1.7033 0.0079  -0.3019 0.1043  166 GLN   U O   
37101 C  CB  . GLN   U  175 ? 2.0675 0.5552 1.4766 0.0550  -0.3113 -0.0428 166 GLN   U CB  
37102 C  CG  . GLN   U  175 ? 2.0448 0.6024 1.5320 0.0601  -0.3011 -0.0707 166 GLN   U CG  
37103 C  CD  . GLN   U  175 ? 2.0950 0.6271 1.5777 0.0571  -0.2971 -0.1149 166 GLN   U CD  
37104 O  OE1 . GLN   U  175 ? 2.0674 0.7193 1.6538 0.0270  -0.1914 -0.0741 166 GLN   U OE1 
37105 N  NE2 . GLN   U  175 ? 2.0919 0.6771 1.6392 0.0929  -0.2710 -0.1053 166 GLN   U NE2 
37106 N  N   . GLN   U  176 ? 2.0497 0.6489 1.5868 0.0593  -0.2822 0.1085  167 GLN   U N   
37107 C  CA  . GLN   U  176 ? 2.0744 0.7357 1.6309 0.0210  -0.3030 0.1676  167 GLN   U CA  
37108 C  C   . GLN   U  176 ? 2.1359 0.6982 1.6259 0.0204  -0.3081 0.1497  167 GLN   U C   
37109 O  O   . GLN   U  176 ? 2.1303 0.5181 1.7097 0.0477  -0.3411 0.1628  167 GLN   U O   
37110 C  CB  . GLN   U  176 ? 2.1538 0.8563 1.5350 0.0492  -0.2565 0.1404  167 GLN   U CB  
37111 C  CG  . GLN   U  176 ? 2.1668 1.0471 1.5616 -0.0142 -0.2233 0.1776  167 GLN   U CG  
37112 C  CD  . GLN   U  176 ? 2.1770 1.0829 1.5519 -0.0123 -0.1632 0.2440  167 GLN   U CD  
37113 O  OE1 . GLN   U  176 ? 2.3029 1.2060 1.5328 -0.0703 -0.0423 0.2277  167 GLN   U OE1 
37114 N  NE2 . GLN   U  176 ? 2.1676 1.1738 1.6324 -0.0511 -0.1364 0.2236  167 GLN   U NE2 
37115 N  N   . GLU   U  177 ? 2.1188 0.8140 1.6831 0.0372  -0.3537 0.1207  168 GLU   U N   
37116 C  CA  . GLU   U  177 ? 2.1183 0.8438 1.6876 0.0596  -0.3562 0.1255  168 GLU   U CA  
37117 C  C   . GLU   U  177 ? 2.0642 0.7322 1.6522 -0.0344 -0.3664 0.1620  168 GLU   U C   
37118 O  O   . GLU   U  177 ? 2.0810 0.8495 1.6258 -0.0761 -0.3572 0.1024  168 GLU   U O   
37119 C  CB  . GLU   U  177 ? 2.1442 0.9092 1.7728 0.1489  -0.3326 0.1229  168 GLU   U CB  
37120 C  CG  . GLU   U  177 ? 2.1847 0.9268 1.7721 0.1949  -0.2986 0.1251  168 GLU   U CG  
37121 C  CD  . GLU   U  177 ? 2.2313 0.9032 1.6540 0.2193  -0.3387 0.1229  168 GLU   U CD  
37122 O  OE1 . GLU   U  177 ? 2.2883 0.9644 1.7768 0.3099  -0.2589 0.0562  168 GLU   U OE1 
37123 O  OE2 . GLU   U  177 ? 2.0313 1.0134 1.4190 0.2108  -0.4110 -0.0208 168 GLU   U OE2 
37124 N  N   . ILE   U  178 ? 2.0893 0.6090 1.5796 0.0383  -0.3851 0.1487  169 ILE   U N   
37125 C  CA  . ILE   U  178 ? 2.0393 0.5165 1.5790 0.0302  -0.3691 0.2289  169 ILE   U CA  
37126 C  C   . ILE   U  178 ? 2.0441 0.4306 1.5572 0.0088  -0.3850 0.2168  169 ILE   U C   
37127 O  O   . ILE   U  178 ? 2.0325 0.4189 1.5586 0.0329  -0.4075 0.2188  169 ILE   U O   
37128 C  CB  . ILE   U  178 ? 2.0576 0.4108 1.5482 0.0776  -0.3388 0.2719  169 ILE   U CB  
37129 C  CG1 . ILE   U  178 ? 2.0598 0.4163 1.5416 0.0892  -0.3240 0.2794  169 ILE   U CG1 
37130 C  CG2 . ILE   U  178 ? 2.0489 0.4251 1.5495 0.0711  -0.3183 0.2660  169 ILE   U CG2 
37131 C  CD1 . ILE   U  178 ? 2.0500 0.3228 1.5010 0.1231  -0.3434 0.2969  169 ILE   U CD1 
37132 N  N   . THR   U  179 ? 2.0569 0.4029 1.5486 -0.0509 -0.3448 0.2125  170 THR   U N   
37133 C  CA  . THR   U  179 ? 2.0206 0.4239 1.6258 -0.0775 -0.3372 0.2363  170 THR   U CA  
37134 C  C   . THR   U  179 ? 1.9970 0.5580 1.6393 -0.0549 -0.2970 0.2445  170 THR   U C   
37135 O  O   . THR   U  179 ? 1.9932 0.4398 1.6104 -0.0736 -0.3259 0.2640  170 THR   U O   
37136 C  CB  . THR   U  179 ? 2.0223 0.3793 1.6309 -0.1114 -0.3451 0.2393  170 THR   U CB  
37137 O  OG1 . THR   U  179 ? 2.0673 0.1755 1.6774 -0.1585 -0.3696 0.2071  170 THR   U OG1 
37138 C  CG2 . THR   U  179 ? 2.0013 0.3875 1.6420 -0.1169 -0.3388 0.2468  170 THR   U CG2 
37139 N  N   . THR   U  180 ? 2.0647 0.5639 1.6859 -0.0281 -0.3052 0.2881  171 THR   U N   
37140 C  CA  . THR   U  180 ? 2.0606 0.6440 1.6859 -0.0145 -0.2867 0.3177  171 THR   U CA  
37141 C  C   . THR   U  180 ? 2.1239 0.6685 1.6756 0.0078  -0.3072 0.3273  171 THR   U C   
37142 O  O   . THR   U  180 ? 2.1593 0.7352 1.6353 0.0464  -0.2750 0.3985  171 THR   U O   
37143 C  CB  . THR   U  180 ? 2.0526 0.6565 1.6825 0.0091  -0.3014 0.2927  171 THR   U CB  
37144 O  OG1 . THR   U  180 ? 2.0657 0.7222 1.6976 0.0544  -0.2915 0.2878  171 THR   U OG1 
37145 C  CG2 . THR   U  180 ? 2.0569 0.6607 1.6871 -0.0181 -0.3006 0.2859  171 THR   U CG2 
37146 N  N   . ASN   U  181 ? 2.1160 0.5684 1.7047 -0.0104 -0.3108 0.2787  172 ASN   U N   
37147 C  CA  . ASN   U  181 ? 2.1182 0.5015 1.7510 -0.0499 -0.3000 0.1978  172 ASN   U CA  
37148 C  C   . ASN   U  181 ? 2.0978 0.4669 1.7615 -0.0844 -0.2892 0.1984  172 ASN   U C   
37149 O  O   . ASN   U  181 ? 2.1100 0.3589 1.8380 -0.0788 -0.2508 0.1033  172 ASN   U O   
37150 C  CB  . ASN   U  181 ? 2.1271 0.5010 1.7934 -0.0808 -0.3079 0.1736  172 ASN   U CB  
37151 C  CG  . ASN   U  181 ? 2.1807 0.5481 1.7928 -0.0986 -0.2933 0.1793  172 ASN   U CG  
37152 O  OD1 . ASN   U  181 ? 2.1589 0.6179 1.8487 -0.0494 -0.3091 0.0850  172 ASN   U OD1 
37153 N  ND2 . ASN   U  181 ? 2.2274 0.5704 1.8147 -0.1124 -0.2521 0.2159  172 ASN   U ND2 
37154 N  N   . LEU   U  182 ? 2.0476 0.4818 1.7313 -0.0866 -0.2735 0.1902  173 LEU   U N   
37155 C  CA  . LEU   U  182 ? 2.0213 0.4885 1.7271 -0.0878 -0.2553 0.1914  173 LEU   U CA  
37156 C  C   . LEU   U  182 ? 2.0127 0.4899 1.7837 -0.1263 -0.2399 0.1633  173 LEU   U C   
37157 O  O   . LEU   U  182 ? 1.9788 0.4287 1.8491 -0.1724 -0.2095 0.1708  173 LEU   U O   
37158 C  CB  . LEU   U  182 ? 1.9954 0.4890 1.6656 -0.0368 -0.2697 0.2178  173 LEU   U CB  
37159 C  CG  . LEU   U  182 ? 1.9714 0.4982 1.6198 0.0025  -0.2719 0.2404  173 LEU   U CG  
37160 C  CD1 . LEU   U  182 ? 1.9243 0.4481 1.5838 0.0301  -0.2870 0.2181  173 LEU   U CD1 
37161 C  CD2 . LEU   U  182 ? 1.9830 0.4891 1.6084 -0.0037 -0.2727 0.2527  173 LEU   U CD2 
37162 N  N   . GLU   U  183 ? 2.0762 0.5056 1.8019 -0.1367 -0.2265 0.1397  174 GLU   U N   
37163 C  CA  . GLU   U  183 ? 2.0836 0.5198 1.8296 -0.1263 -0.2358 0.1318  174 GLU   U CA  
37164 C  C   . GLU   U  183 ? 2.0657 0.4983 1.8668 -0.0923 -0.1940 0.1011  174 GLU   U C   
37165 O  O   . GLU   U  183 ? 2.1538 0.3541 1.9429 -0.0095 -0.1648 0.0417  174 GLU   U O   
37166 C  CB  . GLU   U  183 ? 2.1355 0.5334 1.7835 -0.1662 -0.2466 0.1515  174 GLU   U CB  
37167 C  CG  . GLU   U  183 ? 2.1570 0.5388 1.7659 -0.1836 -0.2905 0.1767  174 GLU   U CG  
37168 C  CD  . GLU   U  183 ? 2.2194 0.6526 1.7063 -0.1971 -0.3261 0.1486  174 GLU   U CD  
37169 O  OE1 . GLU   U  183 ? 2.1861 0.8589 1.7021 -0.3485 -0.2925 0.1714  174 GLU   U OE1 
37170 O  OE2 . GLU   U  183 ? 2.2293 0.6978 1.6521 -0.2146 -0.3682 0.1676  174 GLU   U OE2 
37171 N  N   . ASN   U  184 ? 2.0468 0.5611 1.8352 -0.1156 -0.2213 0.1347  175 ASN   U N   
37172 C  CA  . ASN   U  184 ? 2.0192 0.6770 1.8669 -0.1459 -0.2209 0.1569  175 ASN   U CA  
37173 C  C   . ASN   U  184 ? 2.0281 0.6648 1.8773 -0.1510 -0.2279 0.1564  175 ASN   U C   
37174 O  O   . ASN   U  184 ? 1.9843 0.7727 1.9841 -0.1262 -0.2525 0.1567  175 ASN   U O   
37175 C  CB  . ASN   U  184 ? 2.0386 0.6459 1.8835 -0.1194 -0.2352 0.0714  175 ASN   U CB  
37176 C  CG  . ASN   U  184 ? 2.0454 0.5976 1.9168 -0.1494 -0.2748 0.0601  175 ASN   U CG  
37177 O  OD1 . ASN   U  184 ? 2.0746 0.4819 1.9123 -0.1535 -0.2839 0.0458  175 ASN   U OD1 
37178 N  ND2 . ASN   U  184 ? 2.0471 0.6118 1.9217 -0.1414 -0.2800 0.0392  175 ASN   U ND2 
37179 N  N   . HIS   U  185 ? 1.9708 0.7711 1.8705 -0.1917 -0.2269 0.1988  176 HIS   U N   
37180 C  CA  . HIS   U  185 ? 1.9702 0.9062 1.8385 -0.1683 -0.1922 0.1755  176 HIS   U CA  
37181 C  C   . HIS   U  185 ? 1.9842 0.8959 1.8674 -0.1534 -0.1540 0.2019  176 HIS   U C   
37182 O  O   . HIS   U  185 ? 2.0110 0.9333 1.8639 -0.1017 -0.1423 0.2404  176 HIS   U O   
37183 C  CB  . HIS   U  185 ? 1.9676 0.9705 1.8149 -0.1753 -0.2117 0.1640  176 HIS   U CB  
37184 C  CG  . HIS   U  185 ? 1.9463 1.0590 1.7292 -0.2088 -0.2103 0.1402  176 HIS   U CG  
37185 N  ND1 . HIS   U  185 ? 1.9384 1.1206 1.7184 -0.1888 -0.2451 0.1762  176 HIS   U ND1 
37186 C  CD2 . HIS   U  185 ? 1.9439 1.1337 1.7178 -0.2290 -0.2109 0.1580  176 HIS   U CD2 
37187 C  CE1 . HIS   U  185 ? 1.9288 1.2686 1.6457 -0.2081 -0.2118 0.1789  176 HIS   U CE1 
37188 N  NE2 . HIS   U  185 ? 1.9538 1.1932 1.6124 -0.1941 -0.1870 0.1397  176 HIS   U NE2 
37189 N  N   . PHE   U  186 ? 2.0138 0.8043 1.8736 -0.1884 -0.1301 0.1777  177 PHE   U N   
37190 C  CA  . PHE   U  186 ? 2.0438 0.7449 1.9315 -0.1751 -0.1052 0.1567  177 PHE   U CA  
37191 C  C   . PHE   U  186 ? 1.9894 0.9460 1.9277 -0.1456 -0.1289 0.1783  177 PHE   U C   
37192 O  O   . PHE   U  186 ? 2.0841 0.8981 1.9561 -0.0974 -0.1187 0.1630  177 PHE   U O   
37193 C  CB  . PHE   U  186 ? 2.0268 0.6635 1.9492 -0.2223 -0.1023 0.1194  177 PHE   U CB  
37194 C  CG  . PHE   U  186 ? 2.0705 0.6486 1.9684 -0.2275 -0.0749 0.0432  177 PHE   U CG  
37195 C  CD1 . PHE   U  186 ? 2.0600 0.4741 2.0703 -0.3524 -0.0868 0.0627  177 PHE   U CD1 
37196 C  CD2 . PHE   U  186 ? 2.0281 0.5546 2.0089 -0.3068 -0.0942 0.0200  177 PHE   U CD2 
37197 C  CE1 . PHE   U  186 ? 2.1252 0.2942 2.0734 -0.3314 -0.0252 0.0438  177 PHE   U CE1 
37198 C  CE2 . PHE   U  186 ? 2.1180 0.3245 2.0106 -0.2805 -0.0404 0.0073  177 PHE   U CE2 
37199 C  CZ  . PHE   U  186 ? 2.1083 0.2803 2.0432 -0.3345 -0.0467 0.0218  177 PHE   U CZ  
37200 N  N   . LYS   U  187 ? 2.0410 0.9416 1.9028 -0.0951 -0.1135 0.2126  178 LYS   U N   
37201 C  CA  . LYS   U  187 ? 2.0249 1.0061 1.9322 -0.1058 -0.1178 0.2435  178 LYS   U CA  
37202 C  C   . LYS   U  187 ? 1.9807 0.9501 1.9720 -0.0972 -0.0920 0.2122  178 LYS   U C   
37203 O  O   . LYS   U  187 ? 1.9578 0.9356 2.0052 -0.1412 -0.1449 0.2703  178 LYS   U O   
37204 C  CB  . LYS   U  187 ? 2.0762 1.0873 1.9332 -0.0454 -0.1279 0.1500  178 LYS   U CB  
37205 C  CG  . LYS   U  187 ? 2.0839 1.3146 1.9243 0.0075  -0.1581 0.1504  178 LYS   U CG  
37206 C  CD  . LYS   U  187 ? 2.1212 1.3393 1.9711 0.0294  -0.1595 0.1315  178 LYS   U CD  
37207 C  CE  . LYS   U  187 ? 2.1343 1.4791 1.9430 0.0661  -0.1929 0.1529  178 LYS   U CE  
37208 N  NZ  . LYS   U  187 ? 2.1539 1.5551 1.9193 0.0764  -0.1752 0.1568  178 LYS   U NZ  
37209 N  N   . LYS   U  188 ? 1.9879 0.9739 1.9342 -0.0738 -0.0777 0.1338  179 LYS   U N   
37210 C  CA  . LYS   U  188 ? 1.9785 1.0478 1.9210 -0.0281 -0.0844 0.1260  179 LYS   U CA  
37211 C  C   . LYS   U  188 ? 2.0114 1.0688 1.8802 -0.0031 -0.0281 0.1446  179 LYS   U C   
37212 O  O   . LYS   U  188 ? 2.0170 1.1476 1.9393 -0.0409 0.0018  0.1622  179 LYS   U O   
37213 C  CB  . LYS   U  188 ? 2.0039 0.9691 1.8713 0.0074  -0.0748 0.0980  179 LYS   U CB  
37214 C  CG  . LYS   U  188 ? 2.0357 0.9438 1.8915 0.0332  -0.0718 0.1166  179 LYS   U CG  
37215 C  CD  . LYS   U  188 ? 2.0846 0.9882 1.8874 0.0598  -0.0877 0.1140  179 LYS   U CD  
37216 C  CE  . LYS   U  188 ? 2.1419 1.0298 1.9305 0.0495  -0.0803 0.1484  179 LYS   U CE  
37217 N  NZ  . LYS   U  188 ? 2.1927 1.0531 1.9402 0.0751  -0.1155 0.1348  179 LYS   U NZ  
37218 N  N   . SER   U  189 ? 2.0214 1.0400 1.8218 0.0266  -0.0206 0.1887  180 SER   U N   
37219 C  CA  . SER   U  189 ? 2.0394 1.0375 1.7771 0.0668  -0.0003 0.2183  180 SER   U CA  
37220 C  C   . SER   U  189 ? 2.0744 1.0157 1.7778 0.0612  -0.0086 0.2474  180 SER   U C   
37221 O  O   . SER   U  189 ? 2.0800 0.9467 1.7403 0.0740  -0.0277 0.3026  180 SER   U O   
37222 C  CB  . SER   U  189 ? 2.0147 1.0017 1.6998 0.0993  0.0239  0.2257  180 SER   U CB  
37223 O  OG  . SER   U  189 ? 1.9576 0.9550 1.7075 0.1256  0.0414  0.2285  180 SER   U OG  
37224 N  N   . LYS   U  190 ? 2.1339 1.0590 1.7904 0.0121  -0.0403 0.2461  181 LYS   U N   
37225 C  CA  . LYS   U  190 ? 2.1243 1.1365 1.8391 -0.0391 -0.0870 0.2338  181 LYS   U CA  
37226 C  C   . LYS   U  190 ? 2.1159 1.1836 1.8073 -0.1528 -0.0798 0.2417  181 LYS   U C   
37227 O  O   . LYS   U  190 ? 2.0828 1.2688 1.7139 -0.2058 -0.0804 0.3290  181 LYS   U O   
37228 C  CB  . LYS   U  190 ? 2.1449 1.1485 1.8928 -0.0370 -0.0590 0.2373  181 LYS   U CB  
37229 C  CG  . LYS   U  190 ? 2.1672 1.1217 1.9530 -0.0709 -0.0801 0.2189  181 LYS   U CG  
37230 C  CD  . LYS   U  190 ? 2.2015 1.1232 1.9939 -0.0712 -0.1053 0.2704  181 LYS   U CD  
37231 C  CE  . LYS   U  190 ? 2.2164 1.1217 2.0116 -0.0409 -0.1294 0.2742  181 LYS   U CE  
37232 N  NZ  . LYS   U  190 ? 2.2644 1.1490 2.0687 -0.0601 -0.1465 0.3044  181 LYS   U NZ  
37233 N  N   . ILE   U  191 ? 2.1778 1.1362 1.8065 -0.2042 -0.1129 0.1963  182 ILE   U N   
37234 C  CA  . ILE   U  191 ? 2.1716 1.1038 1.7758 -0.1991 -0.1447 0.1479  182 ILE   U CA  
37235 C  C   . ILE   U  191 ? 2.1359 1.0146 1.7483 -0.2116 -0.1771 0.1404  182 ILE   U C   
37236 O  O   . ILE   U  191 ? 2.1267 1.0120 1.7013 -0.2268 -0.1767 0.0878  182 ILE   U O   
37237 C  CB  . ILE   U  191 ? 2.1652 1.0343 1.8054 -0.2268 -0.1287 0.1430  182 ILE   U CB  
37238 C  CG1 . ILE   U  191 ? 2.1199 1.0673 1.8182 -0.2530 -0.1435 0.1265  182 ILE   U CG1 
37239 C  CG2 . ILE   U  191 ? 2.1734 1.0320 1.7919 -0.2107 -0.1192 0.1851  182 ILE   U CG2 
37240 C  CD1 . ILE   U  191 ? 2.1047 1.0954 1.8273 -0.2489 -0.1265 0.1029  182 ILE   U CD1 
37241 N  N   . ASP   U  192 ? 2.1294 1.0104 1.7617 -0.1786 -0.2275 0.1674  183 ASP   U N   
37242 C  CA  . ASP   U  192 ? 2.1332 1.0671 1.7485 -0.1034 -0.2340 0.2105  183 ASP   U CA  
37243 C  C   . ASP   U  192 ? 2.1399 1.0664 1.7375 -0.0742 -0.2443 0.2106  183 ASP   U C   
37244 O  O   . ASP   U  192 ? 2.2290 1.1368 1.6675 -0.0773 -0.2046 0.1196  183 ASP   U O   
37245 C  CB  . ASP   U  192 ? 2.1254 1.0899 1.8428 -0.0455 -0.2728 0.2225  183 ASP   U CB  
37246 C  CG  . ASP   U  192 ? 2.1344 1.0552 1.9118 -0.0171 -0.3406 0.2763  183 ASP   U CG  
37247 O  OD1 . ASP   U  192 ? 2.2310 1.0837 2.0670 -0.0778 -0.3229 0.2709  183 ASP   U OD1 
37248 O  OD2 . ASP   U  192 ? 2.1915 0.8933 2.0622 -0.0029 -0.2647 0.2804  183 ASP   U OD2 
37249 N  N   . HIS   U  193 ? 2.0917 0.9497 1.7285 -0.0272 -0.2487 0.3065  184 HIS   U N   
37250 C  CA  . HIS   U  193 ? 2.0416 0.8411 1.7385 -0.0049 -0.2301 0.3358  184 HIS   U CA  
37251 C  C   . HIS   U  193 ? 2.0814 0.8203 1.7331 -0.0119 -0.2079 0.3360  184 HIS   U C   
37252 O  O   . HIS   U  193 ? 2.0750 1.1234 1.7699 -0.0694 -0.0985 0.3184  184 HIS   U O   
37253 C  CB  . HIS   U  193 ? 1.9267 0.8503 1.7992 0.0435  -0.2402 0.2727  184 HIS   U CB  
37254 C  CG  . HIS   U  193 ? 1.8500 0.7689 1.9649 0.0895  -0.2467 0.3157  184 HIS   U CG  
37255 N  ND1 . HIS   U  193 ? 1.8006 0.7956 1.9638 0.1560  -0.2351 0.3330  184 HIS   U ND1 
37256 C  CD2 . HIS   U  193 ? 1.8169 0.6809 2.0291 0.0941  -0.2105 0.3217  184 HIS   U CD2 
37257 C  CE1 . HIS   U  193 ? 1.7937 0.7348 2.0281 0.1384  -0.2109 0.3584  184 HIS   U CE1 
37258 N  NE2 . HIS   U  193 ? 1.7475 0.6944 2.0586 0.1322  -0.2084 0.3516  184 HIS   U NE2 
37259 N  N   . ILE   U  194 ? 2.0699 0.6556 1.6296 -0.0359 -0.1642 0.3898  185 ILE   U N   
37260 C  CA  . ILE   U  194 ? 2.0644 0.7789 1.6022 -0.0310 -0.1373 0.3828  185 ILE   U CA  
37261 C  C   . ILE   U  194 ? 2.1247 0.7035 1.5517 -0.0491 -0.1220 0.4254  185 ILE   U C   
37262 O  O   . ILE   U  194 ? 2.1522 0.7538 1.4499 -0.1169 -0.0909 0.4419  185 ILE   U O   
37263 C  CB  . ILE   U  194 ? 2.0693 0.8478 1.5480 -0.0305 -0.1559 0.3771  185 ILE   U CB  
37264 C  CG1 . ILE   U  194 ? 2.0418 0.8706 1.5401 -0.0260 -0.1798 0.3674  185 ILE   U CG1 
37265 C  CG2 . ILE   U  194 ? 2.0819 0.9532 1.5200 -0.0019 -0.1470 0.3634  185 ILE   U CG2 
37266 C  CD1 . ILE   U  194 ? 2.0656 0.8452 1.5667 0.0052  -0.1966 0.3645  185 ILE   U CD1 
37267 N  N   . ASN   U  195 ? 2.0940 0.8254 1.5714 -0.0082 -0.0950 0.3734  186 ASN   U N   
37268 C  CA  . ASN   U  195 ? 2.1217 0.8653 1.6034 0.0417  -0.1156 0.3530  186 ASN   U CA  
37269 C  C   . ASN   U  195 ? 2.1522 0.8265 1.5905 0.0286  -0.1027 0.3394  186 ASN   U C   
37270 O  O   . ASN   U  195 ? 2.1732 0.8673 1.5399 0.0999  -0.1071 0.3275  186 ASN   U O   
37271 C  CB  . ASN   U  195 ? 2.0611 0.9397 1.5916 0.0969  -0.1242 0.3505  186 ASN   U CB  
37272 C  CG  . ASN   U  195 ? 2.0422 0.9902 1.5373 0.1256  -0.1398 0.3621  186 ASN   U CG  
37273 O  OD1 . ASN   U  195 ? 2.0692 1.0014 1.4963 0.1584  -0.1607 0.3719  186 ASN   U OD1 
37274 N  ND2 . ASN   U  195 ? 1.9903 0.9429 1.5826 0.1458  -0.1601 0.3224  186 ASN   U ND2 
37275 N  N   . GLU   U  196 ? 2.1957 0.8286 1.6771 -0.0030 -0.0980 0.3058  187 GLU   U N   
37276 C  CA  . GLU   U  196 ? 2.2411 1.0341 1.7051 0.0254  -0.1320 0.2731  187 GLU   U CA  
37277 C  C   . GLU   U  196 ? 2.2814 1.0431 1.7955 0.0447  -0.0992 0.2312  187 GLU   U C   
37278 O  O   . GLU   U  196 ? 2.2959 1.1150 1.8101 0.0357  -0.0491 0.2538  187 GLU   U O   
37279 C  CB  . GLU   U  196 ? 2.2563 0.9246 1.7447 -0.0088 -0.1172 0.2377  187 GLU   U CB  
37280 C  CG  . GLU   U  196 ? 2.2912 0.9975 1.7350 -0.0271 -0.1193 0.2078  187 GLU   U CG  
37281 C  CD  . GLU   U  196 ? 2.2882 1.1278 1.7107 -0.0400 -0.0428 0.1890  187 GLU   U CD  
37282 O  OE1 . GLU   U  196 ? 2.2469 1.2137 1.7513 -0.0242 -0.0554 0.0722  187 GLU   U OE1 
37283 O  OE2 . GLU   U  196 ? 2.3047 1.1778 1.7288 -0.0821 -0.0124 0.1526  187 GLU   U OE2 
37284 N  N   . GLU   U  197 ? 2.3013 1.2188 1.8005 0.0811  -0.0818 0.1756  188 GLU   U N   
37285 C  CA  . GLU   U  197 ? 2.2417 1.2320 1.7472 0.0565  -0.0588 0.1775  188 GLU   U CA  
37286 C  C   . GLU   U  197 ? 2.2219 1.1506 1.5829 0.0496  -0.1423 0.2348  188 GLU   U C   
37287 O  O   . GLU   U  197 ? 2.2050 1.2921 1.5094 0.0702  -0.1390 0.2648  188 GLU   U O   
37288 C  CB  . GLU   U  197 ? 2.2895 1.4398 1.7962 0.1295  0.0042  0.1360  188 GLU   U CB  
37289 C  CG  . GLU   U  197 ? 2.3293 1.5922 1.8720 0.1287  0.1065  0.1032  188 GLU   U CG  
37290 C  CD  . GLU   U  197 ? 2.3183 1.7236 1.9726 0.2035  0.1490  0.0919  188 GLU   U CD  
37291 O  OE1 . GLU   U  197 ? 2.4080 2.0629 2.1052 0.1330  0.2640  -0.0419 188 GLU   U OE1 
37292 O  OE2 . GLU   U  197 ? 2.3649 1.9283 1.9451 0.0812  0.3066  0.0465  188 GLU   U OE2 
37293 N  N   . SER   U  198 ? 2.2168 0.9284 1.5454 -0.0122 -0.1382 0.2196  189 SER   U N   
37294 C  CA  . SER   U  198 ? 2.2167 0.8008 1.4604 -0.0015 -0.1543 0.2350  189 SER   U CA  
37295 C  C   . SER   U  198 ? 2.2047 0.5573 1.4374 -0.0424 -0.2323 0.2437  189 SER   U C   
37296 O  O   . SER   U  198 ? 2.1500 0.5155 1.4345 -0.0377 -0.2139 0.3238  189 SER   U O   
37297 C  CB  . SER   U  198 ? 2.2460 0.7247 1.4406 -0.0008 -0.1367 0.2435  189 SER   U CB  
37298 O  OG  . SER   U  198 ? 2.2243 0.6962 1.3851 -0.0338 -0.1326 0.1853  189 SER   U OG  
37299 N  N   . TRP   U  199 ? 2.1836 0.6500 1.3889 -0.0315 -0.2494 0.2538  190 TRP   U N   
37300 C  CA  . TRP   U  199 ? 2.1709 0.5846 1.4159 -0.0466 -0.2808 0.2164  190 TRP   U CA  
37301 C  C   . TRP   U  199 ? 2.1817 0.5899 1.4718 -0.0761 -0.2921 0.2632  190 TRP   U C   
37302 O  O   . TRP   U  199 ? 2.2037 0.7048 1.4488 -0.0758 -0.2422 0.2083  190 TRP   U O   
37303 C  CB  . TRP   U  199 ? 2.1212 0.5696 1.4171 -0.0541 -0.3084 0.1987  190 TRP   U CB  
37304 C  CG  . TRP   U  199 ? 2.1326 0.4962 1.4206 -0.0519 -0.3070 0.2146  190 TRP   U CG  
37305 C  CD1 . TRP   U  199 ? 2.1582 0.4835 1.4314 -0.0971 -0.3069 0.2091  190 TRP   U CD1 
37306 C  CD2 . TRP   U  199 ? 2.1077 0.5907 1.4402 -0.0925 -0.3317 0.1634  190 TRP   U CD2 
37307 N  NE1 . TRP   U  199 ? 2.1525 0.4741 1.4315 -0.0631 -0.3210 0.2097  190 TRP   U NE1 
37308 C  CE2 . TRP   U  199 ? 2.1486 0.4644 1.4597 -0.0647 -0.3054 0.1997  190 TRP   U CE2 
37309 C  CE3 . TRP   U  199 ? 2.0835 0.6615 1.4914 -0.0748 -0.2898 0.1011  190 TRP   U CE3 
37310 C  CZ2 . TRP   U  199 ? 2.1267 0.5567 1.4801 -0.1248 -0.2947 0.1288  190 TRP   U CZ2 
37311 C  CZ3 . TRP   U  199 ? 2.0713 0.6808 1.5145 -0.0939 -0.2864 0.0983  190 TRP   U CZ3 
37312 C  CH2 . TRP   U  199 ? 2.0557 0.6701 1.5162 -0.0773 -0.2774 0.0866  190 TRP   U CH2 
37313 N  N   . GLU   U  200 ? 2.2030 0.5147 1.4941 -0.1024 -0.2941 0.2056  191 GLU   U N   
37314 C  CA  . GLU   U  200 ? 2.1944 0.5512 1.5045 -0.0923 -0.3043 0.2083  191 GLU   U CA  
37315 C  C   . GLU   U  200 ? 2.1419 0.4836 1.5151 -0.0090 -0.3004 0.2272  191 GLU   U C   
37316 O  O   . GLU   U  200 ? 2.1733 0.2781 1.5866 -0.0994 -0.3546 0.2544  191 GLU   U O   
37317 C  CB  . GLU   U  200 ? 2.2688 0.6233 1.5053 -0.1022 -0.2705 0.1862  191 GLU   U CB  
37318 C  CG  . GLU   U  200 ? 2.2986 0.7225 1.5080 -0.1637 -0.2752 0.1508  191 GLU   U CG  
37319 C  CD  . GLU   U  200 ? 2.3116 0.7109 1.4979 -0.1884 -0.2621 0.0952  191 GLU   U CD  
37320 O  OE1 . GLU   U  200 ? 2.3786 0.8168 1.4828 -0.2773 -0.2502 0.0749  191 GLU   U OE1 
37321 O  OE2 . GLU   U  200 ? 2.2725 0.8961 1.5203 -0.2009 -0.2492 0.0900  191 GLU   U OE2 
37322 N  N   . LYS   U  201 ? 2.1517 0.4900 1.5040 -0.0155 -0.2673 0.2330  192 LYS   U N   
37323 C  CA  . LYS   U  201 ? 2.1452 0.4901 1.4886 -0.0160 -0.2487 0.1895  192 LYS   U CA  
37324 C  C   . LYS   U  201 ? 2.0854 0.5487 1.4672 -0.0305 -0.2804 0.2167  192 LYS   U C   
37325 O  O   . LYS   U  201 ? 2.0844 0.5956 1.4922 -0.0912 -0.2748 0.0760  192 LYS   U O   
37326 C  CB  . LYS   U  201 ? 2.1843 0.5493 1.5164 0.0017  -0.2108 0.1904  192 LYS   U CB  
37327 C  CG  . LYS   U  201 ? 2.2323 0.6586 1.5149 0.0158  -0.1954 0.1747  192 LYS   U CG  
37328 C  CD  . LYS   U  201 ? 2.2419 0.7808 1.4986 0.0196  -0.1519 0.1696  192 LYS   U CD  
37329 C  CE  . LYS   U  201 ? 2.2395 0.8614 1.4506 0.0350  -0.1733 0.1918  192 LYS   U CE  
37330 N  NZ  . LYS   U  201 ? 2.2640 0.9097 1.4581 0.0364  -0.1767 0.1501  192 LYS   U NZ  
37331 N  N   . VAL   U  202 ? 2.0386 0.4516 1.3996 -0.0242 -0.3227 0.1349  193 VAL   U N   
37332 C  CA  . VAL   U  202 ? 2.0083 0.4339 1.4115 -0.0223 -0.3394 0.1176  193 VAL   U CA  
37333 C  C   . VAL   U  202 ? 1.9773 0.4505 1.3733 -0.0353 -0.3660 0.1272  193 VAL   U C   
37334 O  O   . VAL   U  202 ? 1.9859 0.3889 1.4220 -0.0404 -0.3782 0.1498  193 VAL   U O   
37335 C  CB  . VAL   U  202 ? 1.9895 0.4131 1.4085 -0.0148 -0.3462 0.0948  193 VAL   U CB  
37336 C  CG1 . VAL   U  202 ? 1.9603 0.3910 1.4193 -0.0210 -0.3572 0.0867  193 VAL   U CG1 
37337 C  CG2 . VAL   U  202 ? 1.9964 0.4418 1.4163 0.0004  -0.3385 0.1128  193 VAL   U CG2 
37338 N  N   . VAL   U  203 ? 1.9788 0.4876 1.2966 -0.0275 -0.3633 0.1025  194 VAL   U N   
37339 C  CA  . VAL   U  203 ? 1.9705 0.5447 1.2716 -0.0332 -0.3576 0.0807  194 VAL   U CA  
37340 C  C   . VAL   U  203 ? 1.9798 0.5745 1.2442 -0.0493 -0.3398 0.1022  194 VAL   U C   
37341 O  O   . VAL   U  203 ? 1.9277 0.6166 1.2503 -0.0631 -0.3404 0.0737  194 VAL   U O   
37342 C  CB  . VAL   U  203 ? 1.9931 0.5172 1.2699 -0.0274 -0.3689 0.0761  194 VAL   U CB  
37343 C  CG1 . VAL   U  203 ? 1.9933 0.5108 1.2631 -0.0304 -0.3769 0.0543  194 VAL   U CG1 
37344 C  CG2 . VAL   U  203 ? 1.9867 0.5289 1.2698 -0.0071 -0.3698 0.0890  194 VAL   U CG2 
37345 N  N   . GLU   U  204 ? 2.0164 0.6272 1.2679 -0.0279 -0.3050 0.1149  195 GLU   U N   
37346 C  CA  . GLU   U  204 ? 2.0426 0.6571 1.3128 0.0108  -0.2942 0.1604  195 GLU   U CA  
37347 C  C   . GLU   U  204 ? 2.0533 0.5829 1.3350 0.0168  -0.2876 0.1893  195 GLU   U C   
37348 O  O   . GLU   U  204 ? 2.0650 0.5595 1.3584 -0.0077 -0.2985 0.1804  195 GLU   U O   
37349 C  CB  . GLU   U  204 ? 2.0696 0.7261 1.3127 0.0371  -0.2634 0.2228  195 GLU   U CB  
37350 C  CG  . GLU   U  204 ? 2.0547 0.8124 1.2820 0.0405  -0.2780 0.2475  195 GLU   U CG  
37351 C  CD  . GLU   U  204 ? 2.0814 0.9539 1.2743 0.0591  -0.2471 0.2624  195 GLU   U CD  
37352 O  OE1 . GLU   U  204 ? 2.0783 0.9205 1.2205 0.0289  -0.2065 0.3145  195 GLU   U OE1 
37353 O  OE2 . GLU   U  204 ? 2.0506 1.1297 1.2897 0.0601  -0.2307 0.2422  195 GLU   U OE2 
37354 N  N   . PHE   U  205 ? 2.0362 0.5917 1.3762 0.0127  -0.2770 0.1981  196 PHE   U N   
37355 C  CA  . PHE   U  205 ? 2.0470 0.5363 1.4239 -0.0029 -0.2653 0.2018  196 PHE   U CA  
37356 C  C   . PHE   U  205 ? 2.0602 0.5668 1.4027 -0.0110 -0.2851 0.1809  196 PHE   U C   
37357 O  O   . PHE   U  205 ? 2.0751 0.5738 1.3970 -0.0622 -0.3003 0.1862  196 PHE   U O   
37358 C  CB  . PHE   U  205 ? 2.0217 0.5364 1.4446 -0.0253 -0.2697 0.2028  196 PHE   U CB  
37359 C  CG  . PHE   U  205 ? 2.0282 0.4848 1.4898 -0.0284 -0.2685 0.1909  196 PHE   U CG  
37360 C  CD1 . PHE   U  205 ? 2.0137 0.4651 1.4989 -0.0420 -0.2576 0.2065  196 PHE   U CD1 
37361 C  CD2 . PHE   U  205 ? 2.0261 0.5316 1.5133 -0.0295 -0.2488 0.1930  196 PHE   U CD2 
37362 C  CE1 . PHE   U  205 ? 2.0027 0.5016 1.5538 -0.0583 -0.2866 0.2172  196 PHE   U CE1 
37363 C  CE2 . PHE   U  205 ? 1.9995 0.5636 1.5686 -0.0470 -0.2715 0.2049  196 PHE   U CE2 
37364 C  CZ  . PHE   U  205 ? 1.9881 0.5634 1.5781 -0.0522 -0.2697 0.2202  196 PHE   U CZ  
37365 N  N   . ALA   U  206 ? 2.0560 0.5859 1.3618 0.0017  -0.2782 0.1742  197 ALA   U N   
37366 C  CA  . ALA   U  206 ? 2.0527 0.6281 1.3521 0.0240  -0.3006 0.1496  197 ALA   U CA  
37367 C  C   . ALA   U  206 ? 2.0449 0.6692 1.4015 0.0378  -0.2928 0.1668  197 ALA   U C   
37368 O  O   . ALA   U  206 ? 2.0483 0.7496 1.3684 -0.0072 -0.2954 0.1322  197 ALA   U O   
37369 C  CB  . ALA   U  206 ? 2.0305 0.6491 1.2953 0.0237  -0.3193 0.1577  197 ALA   U CB  
37370 N  N   . ILE   U  207 ? 2.0577 0.6652 1.4073 0.0496  -0.2923 0.1292  198 ILE   U N   
37371 C  CA  . ILE   U  207 ? 2.0485 0.7187 1.4285 0.0551  -0.3178 0.1242  198 ILE   U CA  
37372 C  C   . ILE   U  207 ? 2.0802 0.6799 1.4805 0.0890  -0.2954 0.1206  198 ILE   U C   
37373 O  O   . ILE   U  207 ? 2.1038 0.6169 1.5317 0.1326  -0.3826 0.1897  198 ILE   U O   
37374 C  CB  . ILE   U  207 ? 2.0488 0.7188 1.4309 0.0603  -0.3125 0.0997  198 ILE   U CB  
37375 C  CG1 . ILE   U  207 ? 2.0509 0.6854 1.4096 0.0510  -0.3405 0.0525  198 ILE   U CG1 
37376 C  CG2 . ILE   U  207 ? 2.0297 0.7660 1.4440 0.0579  -0.3306 0.1213  198 ILE   U CG2 
37377 C  CD1 . ILE   U  207 ? 2.0818 0.7645 1.3944 0.0392  -0.3622 0.0500  198 ILE   U CD1 
37378 N  N   . THR   U  208 ? 2.1195 0.7400 1.4953 0.0224  -0.2579 0.1416  199 THR   U N   
37379 C  CA  . THR   U  208 ? 2.1863 0.6922 1.4974 0.0275  -0.2750 0.1484  199 THR   U CA  
37380 C  C   . THR   U  208 ? 2.1638 0.6909 1.5478 0.0010  -0.3019 0.1381  199 THR   U C   
37381 O  O   . THR   U  208 ? 2.1361 0.6939 1.6030 0.0028  -0.3166 0.0927  199 THR   U O   
37382 C  CB  . THR   U  208 ? 2.2248 0.7353 1.4695 0.0057  -0.2280 0.2014  199 THR   U CB  
37383 O  OG1 . THR   U  208 ? 2.3023 0.8123 1.3898 -0.0034 -0.2291 0.2559  199 THR   U OG1 
37384 C  CG2 . THR   U  208 ? 2.2249 0.7516 1.4682 0.0078  -0.2033 0.2114  199 THR   U CG2 
37385 N  N   . HIS   U  209 ? 2.1498 0.6330 1.5428 -0.0177 -0.3454 0.0769  200 HIS   U N   
37386 C  CA  . HIS   U  209 ? 2.1453 0.6504 1.5671 -0.0045 -0.3819 0.0748  200 HIS   U CA  
37387 C  C   . HIS   U  209 ? 2.1596 0.6761 1.5707 0.0054  -0.3829 0.0483  200 HIS   U C   
37388 O  O   . HIS   U  209 ? 2.1251 0.7207 1.5764 0.0385  -0.3610 0.0045  200 HIS   U O   
37389 C  CB  . HIS   U  209 ? 2.1395 0.6267 1.5864 -0.0200 -0.4053 0.0637  200 HIS   U CB  
37390 C  CG  . HIS   U  209 ? 2.1121 0.6391 1.5782 -0.0282 -0.4385 0.0816  200 HIS   U CG  
37391 N  ND1 . HIS   U  209 ? 2.1082 0.6792 1.6164 -0.0371 -0.4656 0.1087  200 HIS   U ND1 
37392 C  CD2 . HIS   U  209 ? 2.1324 0.6667 1.5428 -0.0413 -0.4480 0.1094  200 HIS   U CD2 
37393 C  CE1 . HIS   U  209 ? 2.1223 0.6708 1.5698 -0.0662 -0.4719 0.1281  200 HIS   U CE1 
37394 N  NE2 . HIS   U  209 ? 2.1335 0.6721 1.5359 -0.0485 -0.4507 0.1322  200 HIS   U NE2 
37395 N  N   . MET   U  210 ? 2.1743 0.6472 1.5428 0.0047  -0.4077 0.0207  201 MET   U N   
37396 C  CA  . MET   U  210 ? 2.2315 0.6445 1.5169 0.0285  -0.3985 0.0111  201 MET   U CA  
37397 C  C   . MET   U  210 ? 2.2491 0.6493 1.5246 -0.0219 -0.3949 0.0688  201 MET   U C   
37398 O  O   . MET   U  210 ? 2.2513 0.6597 1.5167 0.0108  -0.3545 0.0999  201 MET   U O   
37399 C  CB  . MET   U  210 ? 2.2903 0.5867 1.5133 0.0351  -0.4124 0.0196  201 MET   U CB  
37400 C  CG  . MET   U  210 ? 2.3447 0.6578 1.5690 0.1269  -0.4462 -0.0470 201 MET   U CG  
37401 S  SD  . MET   U  210 ? 2.4503 0.6479 1.6229 0.1714  -0.4767 -0.0141 201 MET   U SD  
37402 C  CE  . MET   U  210 ? 2.4358 0.7045 1.6630 0.1951  -0.4990 -0.0418 201 MET   U CE  
37403 N  N   . ILE   U  211 ? 2.2321 0.6396 1.5214 -0.0430 -0.3757 0.1217  202 ILE   U N   
37404 C  CA  . ILE   U  211 ? 2.2280 0.6721 1.5822 -0.0110 -0.3453 0.1654  202 ILE   U CA  
37405 C  C   . ILE   U  211 ? 2.1975 0.6345 1.5663 0.0051  -0.3490 0.2627  202 ILE   U C   
37406 O  O   . ILE   U  211 ? 2.1666 0.6278 1.5196 -0.0017 -0.3187 0.3118  202 ILE   U O   
37407 C  CB  . ILE   U  211 ? 2.2497 0.6679 1.5865 -0.0368 -0.3315 0.1627  202 ILE   U CB  
37408 C  CG1 . ILE   U  211 ? 2.2097 0.8558 1.6196 -0.0682 -0.3482 0.1384  202 ILE   U CG1 
37409 C  CG2 . ILE   U  211 ? 2.2584 0.6333 1.6370 -0.0616 -0.3052 0.1645  202 ILE   U CG2 
37410 C  CD1 . ILE   U  211 ? 2.2559 0.9892 1.5969 -0.0710 -0.3340 0.1267  202 ILE   U CD1 
37411 N  N   . ASP   U  212 ? 2.2128 0.7033 1.6164 0.0834  -0.3320 0.3213  203 ASP   U N   
37412 C  CA  . ASP   U  212 ? 2.2097 0.7076 1.6640 0.0973  -0.3645 0.3114  203 ASP   U CA  
37413 C  C   . ASP   U  212 ? 2.1971 0.7284 1.6477 0.0740  -0.4511 0.2905  203 ASP   U C   
37414 O  O   . ASP   U  212 ? 2.2288 0.7403 1.5806 0.0481  -0.5139 0.2096  203 ASP   U O   
37415 C  CB  . ASP   U  212 ? 2.2206 0.7857 1.8382 0.1354  -0.3353 0.3801  203 ASP   U CB  
37416 C  CG  . ASP   U  212 ? 2.1904 0.7862 1.8914 0.2255  -0.2669 0.3915  203 ASP   U CG  
37417 O  OD1 . ASP   U  212 ? 2.2919 0.7859 2.0064 0.3401  -0.3213 0.5495  203 ASP   U OD1 
37418 O  OD2 . ASP   U  212 ? 2.1785 0.7901 2.1709 0.1941  -0.1607 0.4061  203 ASP   U OD2 
37419 N  N   . ALA   U  213 ? 2.1518 0.6795 1.5674 0.0208  -0.4730 0.2193  204 ALA   U N   
37420 C  CA  . ALA   U  213 ? 2.1197 0.6449 1.5734 0.0277  -0.4659 0.2120  204 ALA   U CA  
37421 C  C   . ALA   U  213 ? 2.1052 0.6559 1.5602 0.0312  -0.4828 0.2124  204 ALA   U C   
37422 O  O   . ALA   U  213 ? 2.1518 0.5603 1.5490 0.0844  -0.4959 0.2911  204 ALA   U O   
37423 C  CB  . ALA   U  213 ? 2.1032 0.6009 1.5494 -0.0051 -0.4684 0.1885  204 ALA   U CB  
37424 N  N   . LEU   U  214 ? 2.0993 0.6149 1.5220 0.0441  -0.4455 0.1425  205 LEU   U N   
37425 C  CA  . LEU   U  214 ? 2.1068 0.6552 1.5405 0.0319  -0.4182 0.0958  205 LEU   U CA  
37426 C  C   . LEU   U  214 ? 2.0749 0.5854 1.5991 0.0619  -0.3922 0.0677  205 LEU   U C   
37427 O  O   . LEU   U  214 ? 2.0779 0.5501 1.7318 0.0773  -0.4136 0.0650  205 LEU   U O   
37428 C  CB  . LEU   U  214 ? 2.1000 0.6719 1.4921 0.0297  -0.4074 0.0877  205 LEU   U CB  
37429 C  CG  . LEU   U  214 ? 2.0971 0.6835 1.4824 0.0355  -0.4002 0.0818  205 LEU   U CG  
37430 C  CD1 . LEU   U  214 ? 2.0895 0.6765 1.4637 0.0386  -0.3929 0.0722  205 LEU   U CD1 
37431 C  CD2 . LEU   U  214 ? 2.1134 0.7231 1.5024 0.0361  -0.4230 0.0604  205 LEU   U CD2 
37432 N  N   . GLY   U  215 ? 2.0928 0.6112 1.6168 0.0233  -0.3681 0.0757  206 GLY   U N   
37433 C  CA  . GLY   U  215 ? 2.1148 0.5734 1.6580 0.0391  -0.3478 0.0856  206 GLY   U CA  
37434 C  C   . GLY   U  215 ? 2.1107 0.6362 1.6679 0.0542  -0.3476 0.0852  206 GLY   U C   
37435 O  O   . GLY   U  215 ? 2.1407 0.4905 1.6833 0.0279  -0.3174 0.0087  206 GLY   U O   
37436 N  N   . THR   U  216 ? 2.0804 0.7359 1.6731 -0.0332 -0.3512 0.0988  207 THR   U N   
37437 C  CA  . THR   U  216 ? 2.0650 0.9466 1.6414 -0.0088 -0.3655 0.1310  207 THR   U CA  
37438 C  C   . THR   U  216 ? 2.0794 0.9666 1.7108 -0.0207 -0.3688 0.0924  207 THR   U C   
37439 O  O   . THR   U  216 ? 2.0459 0.9460 1.7950 -0.0530 -0.3977 0.0649  207 THR   U O   
37440 C  CB  . THR   U  216 ? 2.0568 1.0001 1.5428 0.0079  -0.3826 0.0993  207 THR   U CB  
37441 O  OG1 . THR   U  216 ? 2.0465 1.0333 1.4948 -0.0138 -0.3127 0.1505  207 THR   U OG1 
37442 C  CG2 . THR   U  216 ? 2.0454 0.9969 1.4685 0.0129  -0.3960 0.1149  207 THR   U CG2 
37443 N  N   . GLU   U  217 ? 2.0451 0.9970 1.7586 -0.0012 -0.3725 0.1644  208 GLU   U N   
37444 C  CA  . GLU   U  217 ? 2.0692 0.9335 1.7808 -0.0044 -0.2775 0.1759  208 GLU   U CA  
37445 C  C   . GLU   U  217 ? 2.0636 0.7899 1.7583 0.0816  -0.3315 0.2632  208 GLU   U C   
37446 O  O   . GLU   U  217 ? 2.0200 0.5378 1.8368 0.1452  -0.3415 0.3705  208 GLU   U O   
37447 C  CB  . GLU   U  217 ? 2.1133 1.0981 1.7334 -0.0235 -0.2409 0.1671  208 GLU   U CB  
37448 C  CG  . GLU   U  217 ? 2.1070 1.1386 1.8412 -0.0807 -0.1355 0.1227  208 GLU   U CG  
37449 C  CD  . GLU   U  217 ? 2.1863 1.0324 1.8802 -0.1651 -0.1002 0.0968  208 GLU   U CD  
37450 O  OE1 . GLU   U  217 ? 2.1672 1.0376 1.8763 -0.2188 -0.1008 0.0917  208 GLU   U OE1 
37451 O  OE2 . GLU   U  217 ? 2.0987 0.8295 1.8583 -0.2912 -0.0545 0.0527  208 GLU   U OE2 
37452 N  N   . PHE   U  218 ? 2.0215 0.8065 1.6859 0.0073  -0.3195 0.2204  209 PHE   U N   
37453 C  CA  . PHE   U  218 ? 2.0456 0.7909 1.6303 -0.0109 -0.3167 0.1781  209 PHE   U CA  
37454 C  C   . PHE   U  218 ? 2.0307 0.8423 1.5528 0.0438  -0.2963 0.1933  209 PHE   U C   
37455 O  O   . PHE   U  218 ? 2.0611 0.9350 1.4977 0.1090  -0.3047 0.2611  209 PHE   U O   
37456 C  CB  . PHE   U  218 ? 2.0546 0.6903 1.6061 -0.1018 -0.3100 0.2001  209 PHE   U CB  
37457 C  CG  . PHE   U  218 ? 2.0636 0.7306 1.6252 -0.1702 -0.3352 0.2328  209 PHE   U CG  
37458 C  CD1 . PHE   U  218 ? 2.0473 0.7934 1.6253 -0.1685 -0.3385 0.2424  209 PHE   U CD1 
37459 C  CD2 . PHE   U  218 ? 2.0528 0.8065 1.6382 -0.1680 -0.2854 0.2545  209 PHE   U CD2 
37460 C  CE1 . PHE   U  218 ? 2.1055 0.8462 1.6104 -0.1710 -0.3310 0.2237  209 PHE   U CE1 
37461 C  CE2 . PHE   U  218 ? 2.0842 0.9039 1.6489 -0.1656 -0.3012 0.2370  209 PHE   U CE2 
37462 C  CZ  . PHE   U  218 ? 2.1050 0.8911 1.6341 -0.1749 -0.3133 0.2149  209 PHE   U CZ  
37463 N  N   . SER   U  219 ? 2.0291 0.8739 1.5544 0.0375  -0.3107 0.1682  210 SER   U N   
37464 C  CA  . SER   U  219 ? 2.0403 0.9953 1.5017 0.0408  -0.3284 0.1284  210 SER   U CA  
37465 C  C   . SER   U  219 ? 2.0245 0.9757 1.4513 0.0284  -0.3545 0.0775  210 SER   U C   
37466 O  O   . SER   U  219 ? 1.9853 1.1133 1.4849 0.0119  -0.3973 0.0187  210 SER   U O   
37467 C  CB  . SER   U  219 ? 2.0599 1.0236 1.4930 0.0645  -0.3830 0.1547  210 SER   U CB  
37468 O  OG  . SER   U  219 ? 2.0220 1.0451 1.5383 0.0705  -0.3585 0.1351  210 SER   U OG  
37469 N  N   . LYS   U  220 ? 2.0303 0.9302 1.4064 0.0232  -0.3380 0.1177  211 LYS   U N   
37470 C  CA  . LYS   U  220 ? 1.9950 0.9448 1.3400 0.0318  -0.3387 0.1712  211 LYS   U CA  
37471 C  C   . LYS   U  220 ? 1.9741 0.9025 1.3268 0.0549  -0.3605 0.1972  211 LYS   U C   
37472 O  O   . LYS   U  220 ? 1.9737 0.9703 1.3254 0.1032  -0.3634 0.2080  211 LYS   U O   
37473 C  CB  . LYS   U  220 ? 2.0357 0.8765 1.3358 0.0271  -0.3092 0.1839  211 LYS   U CB  
37474 C  CG  . LYS   U  220 ? 2.0238 0.8862 1.3225 -0.0015 -0.2981 0.1557  211 LYS   U CG  
37475 C  CD  . LYS   U  220 ? 2.0349 0.9034 1.3106 -0.0335 -0.2701 0.1456  211 LYS   U CD  
37476 C  CE  . LYS   U  220 ? 2.0249 0.9122 1.2791 -0.0661 -0.2682 0.1033  211 LYS   U CE  
37477 N  NZ  . LYS   U  220 ? 2.0638 0.9298 1.2659 -0.0931 -0.2536 0.1046  211 LYS   U NZ  
37478 N  N   . ASN   U  221 ? 1.9738 0.8332 1.3009 0.0700  -0.3976 0.2719  212 ASN   U N   
37479 C  CA  . ASN   U  221 ? 1.9424 0.8402 1.3167 0.0672  -0.4030 0.2762  212 ASN   U CA  
37480 C  C   . ASN   U  221 ? 1.9442 0.7939 1.3496 0.0391  -0.3996 0.2790  212 ASN   U C   
37481 O  O   . ASN   U  221 ? 1.8855 0.7920 1.3636 0.0468  -0.3954 0.2205  212 ASN   U O   
37482 C  CB  . ASN   U  221 ? 1.9482 0.8714 1.3092 0.0737  -0.4139 0.2861  212 ASN   U CB  
37483 C  CG  . ASN   U  221 ? 1.9451 0.9158 1.3393 0.0679  -0.4082 0.2430  212 ASN   U CG  
37484 O  OD1 . ASN   U  221 ? 1.9169 0.9264 1.3294 0.0171  -0.3965 0.2222  212 ASN   U OD1 
37485 N  ND2 . ASN   U  221 ? 1.9538 1.0069 1.3025 0.0974  -0.4171 0.2373  212 ASN   U ND2 
37486 N  N   . ASP   U  222 ? 1.9849 0.8112 1.3853 0.0146  -0.3755 0.3062  213 ASP   U N   
37487 C  CA  . ASP   U  222 ? 1.9954 0.8439 1.3947 0.0134  -0.3634 0.2835  213 ASP   U CA  
37488 C  C   . ASP   U  222 ? 2.0043 0.8025 1.3318 -0.0235 -0.3671 0.2953  213 ASP   U C   
37489 O  O   . ASP   U  222 ? 1.9860 0.8300 1.3252 -0.0395 -0.3679 0.2957  213 ASP   U O   
37490 C  CB  . ASP   U  222 ? 2.0074 0.8582 1.4605 -0.0046 -0.3275 0.2755  213 ASP   U CB  
37491 C  CG  . ASP   U  222 ? 2.0134 0.9159 1.4590 0.0014  -0.3370 0.2942  213 ASP   U CG  
37492 O  OD1 . ASP   U  222 ? 2.0020 1.0302 1.5521 0.0493  -0.3216 0.2713  213 ASP   U OD1 
37493 O  OD2 . ASP   U  222 ? 2.0441 0.9476 1.5036 -0.0608 -0.3150 0.2969  213 ASP   U OD2 
37494 N  N   . LEU   U  223 ? 1.9980 0.8013 1.3552 0.0016  -0.3651 0.3160  214 LEU   U N   
37495 C  CA  . LEU   U  223 ? 2.0117 0.7885 1.3716 0.0106  -0.3702 0.3126  214 LEU   U CA  
37496 C  C   . LEU   U  223 ? 2.0083 0.7466 1.3578 0.0455  -0.3658 0.2701  214 LEU   U C   
37497 O  O   . LEU   U  223 ? 1.9724 0.7043 1.3512 0.0873  -0.3795 0.3224  214 LEU   U O   
37498 C  CB  . LEU   U  223 ? 2.0626 0.8738 1.3621 -0.0104 -0.3496 0.3347  214 LEU   U CB  
37499 C  CG  . LEU   U  223 ? 2.1139 0.9436 1.4214 -0.0620 -0.3496 0.3711  214 LEU   U CG  
37500 C  CD1 . LEU   U  223 ? 2.1627 1.0312 1.4222 -0.0394 -0.3310 0.3629  214 LEU   U CD1 
37501 C  CD2 . LEU   U  223 ? 2.1435 0.9901 1.4230 -0.0630 -0.3396 0.3377  214 LEU   U CD2 
37502 N  N   . GLU   U  224 ? 2.0309 0.6427 1.3238 0.0452  -0.3634 0.2270  215 GLU   U N   
37503 C  CA  . GLU   U  224 ? 2.0205 0.6105 1.3239 0.0847  -0.3685 0.2026  215 GLU   U CA  
37504 C  C   . GLU   U  224 ? 1.9984 0.5208 1.2638 0.0406  -0.3992 0.2335  215 GLU   U C   
37505 O  O   . GLU   U  224 ? 1.9545 0.4691 1.2902 0.0941  -0.4285 0.2425  215 GLU   U O   
37506 C  CB  . GLU   U  224 ? 2.0678 0.5630 1.3763 0.1215  -0.3076 0.1758  215 GLU   U CB  
37507 C  CG  . GLU   U  224 ? 2.1237 0.5815 1.4664 0.0888  -0.2494 0.1622  215 GLU   U CG  
37508 C  CD  . GLU   U  224 ? 2.1731 0.6476 1.5147 0.1194  -0.2079 0.0770  215 GLU   U CD  
37509 O  OE1 . GLU   U  224 ? 2.1867 0.4684 1.5885 0.2598  -0.2285 0.1982  215 GLU   U OE1 
37510 O  OE2 . GLU   U  224 ? 2.2463 0.7316 1.5401 -0.0105 -0.1852 -0.0078 215 GLU   U OE2 
37511 N  N   . VAL   U  225 ? 1.9979 0.5603 1.2357 0.0341  -0.3929 0.2064  216 VAL   U N   
37512 C  CA  . VAL   U  225 ? 1.9777 0.5897 1.2462 -0.0005 -0.3893 0.1325  216 VAL   U CA  
37513 C  C   . VAL   U  225 ? 2.0043 0.5313 1.2515 -0.0563 -0.4071 0.0482  216 VAL   U C   
37514 O  O   . VAL   U  225 ? 2.1055 0.5712 1.2630 -0.0781 -0.3990 -0.0530 216 VAL   U O   
37515 C  CB  . VAL   U  225 ? 2.0007 0.5711 1.2313 -0.0058 -0.4047 0.1445  216 VAL   U CB  
37516 C  CG1 . VAL   U  225 ? 1.9962 0.5570 1.2178 -0.0234 -0.3912 0.1193  216 VAL   U CG1 
37517 C  CG2 . VAL   U  225 ? 1.9982 0.5937 1.2586 0.0128  -0.4076 0.1694  216 VAL   U CG2 
37518 N  N   . GLY   U  226 ? 1.9998 0.5553 1.2835 -0.0044 -0.4009 0.0679  217 GLY   U N   
37519 C  CA  . GLY   U  226 ? 1.9646 0.5518 1.3093 0.0235  -0.3952 0.0403  217 GLY   U CA  
37520 C  C   . GLY   U  226 ? 1.9846 0.5933 1.3205 0.0315  -0.3633 0.0636  217 GLY   U C   
37521 O  O   . GLY   U  226 ? 2.0011 0.5856 1.2678 0.0297  -0.3534 0.0774  217 GLY   U O   
37522 N  N   . VAL   U  227 ? 1.9705 0.6051 1.3420 0.0661  -0.3190 0.0786  218 VAL   U N   
37523 C  CA  . VAL   U  227 ? 1.9731 0.5863 1.3864 0.0780  -0.3042 0.1050  218 VAL   U CA  
37524 C  C   . VAL   U  227 ? 1.9410 0.5167 1.4259 0.0434  -0.2908 0.0631  218 VAL   U C   
37525 O  O   . VAL   U  227 ? 1.9151 0.5152 1.4601 0.0494  -0.2664 0.0346  218 VAL   U O   
37526 C  CB  . VAL   U  227 ? 1.9895 0.5905 1.3863 0.0874  -0.2921 0.1361  218 VAL   U CB  
37527 C  CG1 . VAL   U  227 ? 1.9877 0.5714 1.4034 0.0913  -0.2902 0.1552  218 VAL   U CG1 
37528 C  CG2 . VAL   U  227 ? 2.0150 0.6142 1.4306 0.0913  -0.2866 0.1702  218 VAL   U CG2 
37529 N  N   . ALA   U  228 ? 1.9801 0.4711 1.3924 0.0341  -0.3109 0.0610  219 ALA   U N   
37530 C  CA  . ALA   U  228 ? 2.0012 0.4416 1.3300 0.0028  -0.3241 0.0535  219 ALA   U CA  
37531 C  C   . ALA   U  228 ? 2.0039 0.4855 1.3110 -0.0070 -0.3196 0.0692  219 ALA   U C   
37532 O  O   . ALA   U  228 ? 2.0321 0.3345 1.2516 0.0007  -0.3938 0.0169  219 ALA   U O   
37533 C  CB  . ALA   U  228 ? 1.9566 0.3597 1.3266 0.0036  -0.3069 0.0552  219 ALA   U CB  
37534 N  N   . THR   U  229 ? 2.0860 0.5000 1.3226 -0.0241 -0.3067 0.0539  220 THR   U N   
37535 C  CA  . THR   U  229 ? 2.1113 0.4755 1.3784 -0.0306 -0.2721 0.0505  220 THR   U CA  
37536 C  C   . THR   U  229 ? 2.1400 0.4482 1.4166 -0.0038 -0.2749 0.0282  220 THR   U C   
37537 O  O   . THR   U  229 ? 2.1609 0.4999 1.3761 -0.0125 -0.2980 0.0093  220 THR   U O   
37538 C  CB  . THR   U  229 ? 2.1745 0.4872 1.3853 -0.0430 -0.2511 0.0126  220 THR   U CB  
37539 O  OG1 . THR   U  229 ? 2.1750 0.5404 1.3954 -0.0500 -0.2484 0.0637  220 THR   U OG1 
37540 C  CG2 . THR   U  229 ? 2.1792 0.5243 1.4009 -0.0291 -0.2554 0.0363  220 THR   U CG2 
37541 N  N   . LYS   U  230 ? 2.1728 0.5660 1.4928 0.0360  -0.2152 0.0218  221 LYS   U N   
37542 C  CA  . LYS   U  230 ? 2.1915 0.6134 1.5763 0.0868  -0.1916 0.0729  221 LYS   U CA  
37543 C  C   . LYS   U  230 ? 2.2534 0.5144 1.6391 0.0893  -0.2082 0.1014  221 LYS   U C   
37544 O  O   . LYS   U  230 ? 2.3474 0.4595 1.5310 0.1144  -0.1982 0.2617  221 LYS   U O   
37545 C  CB  . LYS   U  230 ? 2.1510 0.6410 1.6754 0.0742  -0.1688 0.0901  221 LYS   U CB  
37546 C  CG  . LYS   U  230 ? 2.1040 0.6200 1.7618 0.0778  -0.1572 0.0972  221 LYS   U CG  
37547 C  CD  . LYS   U  230 ? 2.1021 0.7873 1.8360 0.0902  -0.1017 0.0123  221 LYS   U CD  
37548 C  CE  . LYS   U  230 ? 2.0754 0.8606 1.8760 0.1145  -0.1151 0.0398  221 LYS   U CE  
37549 N  NZ  . LYS   U  230 ? 2.0973 0.8893 1.9194 0.1230  -0.0927 0.0284  221 LYS   U NZ  
37550 N  N   . ASP   U  231 ? 2.3012 0.6126 1.6697 0.1259  -0.1399 0.0698  222 ASP   U N   
37551 C  CA  . ASP   U  231 ? 2.2136 0.7821 1.8831 0.0717  -0.2068 -0.0406 222 ASP   U CA  
37552 C  C   . ASP   U  231 ? 2.2151 0.7290 1.8646 0.0451  -0.2839 -0.0510 222 ASP   U C   
37553 O  O   . ASP   U  231 ? 2.1625 0.7897 1.9493 0.0300  -0.3415 -0.1825 222 ASP   U O   
37554 C  CB  . ASP   U  231 ? 2.4043 0.8943 1.9652 0.0551  -0.1664 -0.1476 222 ASP   U CB  
37555 C  CG  . ASP   U  231 ? 2.4378 1.0137 2.0024 0.1104  -0.1410 -0.1199 222 ASP   U CG  
37556 O  OD1 . ASP   U  231 ? 2.6545 1.1276 2.0357 0.0211  -0.1363 -0.0107 222 ASP   U OD1 
37557 O  OD2 . ASP   U  231 ? 2.6378 1.1281 2.0924 0.0795  -0.0561 -0.3168 222 ASP   U OD2 
37558 N  N   . LYS   U  232 ? 2.0711 0.7486 1.7714 0.0442  -0.3166 0.0015  223 LYS   U N   
37559 C  CA  . LYS   U  232 ? 2.0423 0.7285 1.6671 0.0108  -0.3224 -0.0097 223 LYS   U CA  
37560 C  C   . LYS   U  232 ? 1.9430 0.7212 1.5752 0.0329  -0.2782 0.0447  223 LYS   U C   
37561 O  O   . LYS   U  232 ? 1.9848 0.6695 1.5767 0.0404  -0.3113 0.1167  223 LYS   U O   
37562 C  CB  . LYS   U  232 ? 2.0828 0.7972 1.7108 0.0043  -0.3469 -0.0671 223 LYS   U CB  
37563 C  CG  . LYS   U  232 ? 2.1158 0.8259 1.7654 0.0107  -0.3140 -0.0222 223 LYS   U CG  
37564 C  CD  . LYS   U  232 ? 2.1421 0.9618 1.7682 0.0500  -0.3764 0.0062  223 LYS   U CD  
37565 C  CE  . LYS   U  232 ? 2.1916 0.9382 1.7942 0.1015  -0.3872 0.0899  223 LYS   U CE  
37566 N  NZ  . LYS   U  232 ? 2.1762 1.0402 1.7706 0.1056  -0.4360 0.1148  223 LYS   U NZ  
37567 N  N   . PHE   U  233 ? 1.9424 0.5629 1.4822 0.0204  -0.3358 0.0312  224 PHE   U N   
37568 C  CA  . PHE   U  233 ? 1.9143 0.5440 1.3978 -0.0125 -0.3205 -0.0037 224 PHE   U CA  
37569 C  C   . PHE   U  233 ? 1.9105 0.4880 1.4152 -0.0259 -0.3203 -0.0812 224 PHE   U C   
37570 O  O   . PHE   U  233 ? 1.9598 0.2996 1.4214 -0.0434 -0.3140 -0.2083 224 PHE   U O   
37571 C  CB  . PHE   U  233 ? 1.8694 0.5545 1.3645 -0.0184 -0.3368 0.0385  224 PHE   U CB  
37572 C  CG  . PHE   U  233 ? 1.8811 0.5405 1.3397 -0.0160 -0.3717 0.0882  224 PHE   U CG  
37573 C  CD1 . PHE   U  233 ? 1.8604 0.5342 1.3103 0.0020  -0.3901 0.1064  224 PHE   U CD1 
37574 C  CD2 . PHE   U  233 ? 1.8768 0.4754 1.3302 0.0011  -0.3839 0.1126  224 PHE   U CD2 
37575 C  CE1 . PHE   U  233 ? 1.8634 0.5717 1.3049 0.0316  -0.3912 0.0832  224 PHE   U CE1 
37576 C  CE2 . PHE   U  233 ? 1.8795 0.5121 1.3295 0.0358  -0.3891 0.0940  224 PHE   U CE2 
37577 C  CZ  . PHE   U  233 ? 1.8697 0.5762 1.3347 -0.0026 -0.3722 0.0770  224 PHE   U CZ  
37578 N  N   . PHE   U  234 ? 1.8883 0.4803 1.4530 -0.0089 -0.3328 -0.0778 225 PHE   U N   
37579 C  CA  . PHE   U  234 ? 1.8721 0.4638 1.4636 -0.0325 -0.3406 -0.0924 225 PHE   U CA  
37580 C  C   . PHE   U  234 ? 1.8495 0.4563 1.4750 -0.0745 -0.3298 -0.0709 225 PHE   U C   
37581 O  O   . PHE   U  234 ? 1.8683 0.3945 1.4474 -0.0678 -0.3394 -0.0987 225 PHE   U O   
37582 C  CB  . PHE   U  234 ? 1.8371 0.3843 1.4666 -0.0287 -0.3846 -0.0815 225 PHE   U CB  
37583 C  CG  . PHE   U  234 ? 1.8495 0.3370 1.4502 -0.0105 -0.3884 -0.0454 225 PHE   U CG  
37584 C  CD1 . PHE   U  234 ? 1.8551 0.3261 1.4749 -0.0074 -0.3587 -0.0380 225 PHE   U CD1 
37585 C  CD2 . PHE   U  234 ? 1.8408 0.4100 1.4210 0.0150  -0.4218 -0.0298 225 PHE   U CD2 
37586 C  CE1 . PHE   U  234 ? 1.8616 0.3409 1.4737 -0.0063 -0.3534 -0.0359 225 PHE   U CE1 
37587 C  CE2 . PHE   U  234 ? 1.8367 0.4411 1.4207 0.0305  -0.4127 -0.0524 225 PHE   U CE2 
37588 C  CZ  . PHE   U  234 ? 1.8428 0.4030 1.4178 0.0283  -0.3897 -0.0435 225 PHE   U CZ  
37589 N  N   . THR   U  235 ? 1.8241 0.5396 1.4723 -0.1142 -0.3263 -0.0864 226 THR   U N   
37590 C  CA  . THR   U  235 ? 1.8406 0.4821 1.4009 -0.1792 -0.2945 -0.1041 226 THR   U CA  
37591 C  C   . THR   U  235 ? 1.9075 0.5626 1.3790 -0.2006 -0.2843 -0.1071 226 THR   U C   
37592 O  O   . THR   U  235 ? 1.9195 0.6085 1.3061 -0.2839 -0.2518 -0.0883 226 THR   U O   
37593 C  CB  . THR   U  235 ? 1.7918 0.4407 1.4574 -0.2120 -0.3044 -0.1508 226 THR   U CB  
37594 O  OG1 . THR   U  235 ? 1.7669 0.5512 1.5499 -0.2164 -0.2961 -0.2515 226 THR   U OG1 
37595 C  CG2 . THR   U  235 ? 1.7547 0.4379 1.4435 -0.1926 -0.2903 -0.1783 226 THR   U CG2 
37596 N  N   . LEU   U  236 ? 1.9455 0.6192 1.2598 -0.1450 -0.2922 -0.0768 227 LEU   U N   
37597 C  CA  . LEU   U  236 ? 1.9337 0.6642 1.2633 -0.0997 -0.3100 -0.0559 227 LEU   U CA  
37598 C  C   . LEU   U  236 ? 1.9528 0.6507 1.2018 -0.0695 -0.3297 -0.0167 227 LEU   U C   
37599 O  O   . LEU   U  236 ? 1.9231 0.7046 1.1058 -0.0178 -0.3620 0.0366  227 LEU   U O   
37600 C  CB  . LEU   U  236 ? 1.9992 0.6631 1.2302 -0.0904 -0.2984 -0.0083 227 LEU   U CB  
37601 C  CG  . LEU   U  236 ? 2.0000 0.6968 1.2477 -0.1053 -0.2512 -0.0177 227 LEU   U CG  
37602 C  CD1 . LEU   U  236 ? 2.0259 0.7085 1.2330 -0.0873 -0.2433 0.0209  227 LEU   U CD1 
37603 C  CD2 . LEU   U  236 ? 2.0537 0.7461 1.2609 -0.1038 -0.2332 -0.0710 227 LEU   U CD2 
37604 N  N   . SER   U  237 ? 1.9122 0.6880 1.2427 -0.0689 -0.3687 0.0077  228 SER   U N   
37605 C  CA  . SER   U  237 ? 1.9126 0.7541 1.3330 -0.0407 -0.3705 0.0218  228 SER   U CA  
37606 C  C   . SER   U  237 ? 1.9314 0.7636 1.3819 -0.0224 -0.3659 0.0346  228 SER   U C   
37607 O  O   . SER   U  237 ? 1.8984 0.8936 1.4699 -0.0039 -0.3281 -0.0184 228 SER   U O   
37608 C  CB  . SER   U  237 ? 1.8862 0.8223 1.3015 -0.0132 -0.4162 0.0336  228 SER   U CB  
37609 O  OG  . SER   U  237 ? 1.8601 0.8341 1.3093 -0.0023 -0.4189 0.0737  228 SER   U OG  
37610 N  N   . ALA   U  238 ? 1.9548 0.7468 1.3843 -0.0177 -0.3576 0.0862  229 ALA   U N   
37611 C  CA  . ALA   U  238 ? 2.0002 0.7576 1.3850 -0.0326 -0.3247 0.1257  229 ALA   U CA  
37612 C  C   . ALA   U  238 ? 2.0540 0.7118 1.3940 -0.0124 -0.3094 0.1391  229 ALA   U C   
37613 O  O   . ALA   U  238 ? 2.0588 0.7214 1.5192 -0.0534 -0.3164 0.0626  229 ALA   U O   
37614 C  CB  . ALA   U  238 ? 2.0099 0.6857 1.3322 -0.0325 -0.3184 0.1885  229 ALA   U CB  
37615 N  N   . GLU   U  239 ? 2.0963 0.6863 1.4362 0.0053  -0.3209 0.1369  230 GLU   U N   
37616 C  CA  . GLU   U  239 ? 2.1512 0.7041 1.4830 0.0560  -0.2785 0.0819  230 GLU   U CA  
37617 C  C   . GLU   U  239 ? 2.1520 0.5548 1.3887 0.0386  -0.2930 0.0268  230 GLU   U C   
37618 O  O   . GLU   U  239 ? 2.1515 0.5024 1.4039 0.0475  -0.2461 -0.0455 230 GLU   U O   
37619 C  CB  . GLU   U  239 ? 2.1729 0.7334 1.6136 0.0487  -0.2910 0.0394  230 GLU   U CB  
37620 C  CG  . GLU   U  239 ? 2.1985 0.9068 1.7376 0.0938  -0.3155 0.0927  230 GLU   U CG  
37621 C  CD  . GLU   U  239 ? 2.2157 1.0158 1.8730 0.1321  -0.2615 0.0885  230 GLU   U CD  
37622 O  OE1 . GLU   U  239 ? 2.3225 1.1533 1.9809 0.0577  -0.2408 0.1914  230 GLU   U OE1 
37623 O  OE2 . GLU   U  239 ? 2.2518 1.1073 1.9632 0.1716  -0.3066 0.2324  230 GLU   U OE2 
37624 N  N   . ASN   U  240 ? 2.1787 0.5855 1.3262 0.0081  -0.3002 0.0074  231 ASN   U N   
37625 C  CA  . ASN   U  240 ? 2.1704 0.6707 1.3440 -0.0120 -0.2847 -0.0101 231 ASN   U CA  
37626 C  C   . ASN   U  240 ? 2.1730 0.6135 1.3118 -0.0004 -0.2835 0.0865  231 ASN   U C   
37627 O  O   . ASN   U  240 ? 2.1942 0.4777 1.2000 0.0161  -0.2848 0.1041  231 ASN   U O   
37628 C  CB  . ASN   U  240 ? 2.1832 0.7432 1.3347 0.0237  -0.2819 -0.0120 231 ASN   U CB  
37629 C  CG  . ASN   U  240 ? 2.1790 0.8148 1.3488 0.0118  -0.2846 -0.1509 231 ASN   U CG  
37630 O  OD1 . ASN   U  240 ? 2.1242 0.9692 1.3385 -0.0438 -0.2178 -0.2309 231 ASN   U OD1 
37631 N  ND2 . ASN   U  240 ? 2.2140 0.9490 1.3424 0.0784  -0.2737 -0.1511 231 ASN   U ND2 
37632 N  N   . ILE   U  241 ? 2.1352 0.6158 1.3447 0.0105  -0.2756 0.1016  232 ILE   U N   
37633 C  CA  . ILE   U  241 ? 2.1166 0.6314 1.4129 -0.0160 -0.2605 0.1093  232 ILE   U CA  
37634 C  C   . ILE   U  241 ? 2.1241 0.6618 1.4691 0.0076  -0.2558 0.1597  232 ILE   U C   
37635 O  O   . ILE   U  241 ? 2.1228 0.5615 1.4983 0.0684  -0.2424 0.2243  232 ILE   U O   
37636 C  CB  . ILE   U  241 ? 2.1110 0.6256 1.4212 -0.0262 -0.2703 0.0784  232 ILE   U CB  
37637 C  CG1 . ILE   U  241 ? 2.0969 0.5603 1.3881 -0.0733 -0.2426 0.0515  232 ILE   U CG1 
37638 C  CG2 . ILE   U  241 ? 2.1104 0.6216 1.4435 -0.0234 -0.2579 0.0835  232 ILE   U CG2 
37639 C  CD1 . ILE   U  241 ? 2.0780 0.5165 1.3631 -0.0979 -0.2602 0.0376  232 ILE   U CD1 
37640 N  N   . GLU   U  242 ? 2.1470 0.6781 1.4801 -0.0206 -0.2714 0.1489  233 GLU   U N   
37641 C  CA  . GLU   U  242 ? 2.2266 0.7180 1.4584 -0.0291 -0.2818 0.1461  233 GLU   U CA  
37642 C  C   . GLU   U  242 ? 2.2091 0.7152 1.4300 -0.0427 -0.3174 0.0846  233 GLU   U C   
37643 O  O   . GLU   U  242 ? 2.2153 0.7757 1.4221 -0.1011 -0.3415 0.0920  233 GLU   U O   
37644 C  CB  . GLU   U  242 ? 2.2414 0.7471 1.4913 -0.0386 -0.2835 0.1389  233 GLU   U CB  
37645 C  CG  . GLU   U  242 ? 2.3404 0.8119 1.5046 -0.0288 -0.2464 0.1712  233 GLU   U CG  
37646 C  CD  . GLU   U  242 ? 2.4077 0.8083 1.5886 -0.0316 -0.2026 0.2338  233 GLU   U CD  
37647 O  OE1 . GLU   U  242 ? 2.4734 0.8965 1.5755 0.0410  -0.1725 0.2789  233 GLU   U OE1 
37648 O  OE2 . GLU   U  242 ? 2.4697 0.7763 1.6013 -0.0660 -0.1205 0.2742  233 GLU   U OE2 
37649 N  N   . GLU   U  243 ? 2.2088 0.7456 1.4610 -0.0210 -0.3026 0.0313  234 GLU   U N   
37650 C  CA  . GLU   U  243 ? 2.2607 0.8290 1.5024 -0.0224 -0.2522 0.0109  234 GLU   U CA  
37651 C  C   . GLU   U  243 ? 2.2882 0.7400 1.4701 -0.0554 -0.2040 0.0197  234 GLU   U C   
37652 O  O   . GLU   U  243 ? 2.3911 0.5446 1.3843 -0.0753 -0.1993 -0.0284 234 GLU   U O   
37653 C  CB  . GLU   U  243 ? 2.2514 0.8246 1.5482 -0.0039 -0.2197 -0.0719 234 GLU   U CB  
37654 C  CG  . GLU   U  243 ? 2.2750 0.9053 1.5959 0.0313  -0.1869 -0.0855 234 GLU   U CG  
37655 C  CD  . GLU   U  243 ? 2.2772 0.9276 1.6293 0.1420  -0.1554 -0.1329 234 GLU   U CD  
37656 O  OE1 . GLU   U  243 ? 2.3006 1.0647 1.6364 0.1417  -0.1100 -0.1794 234 GLU   U OE1 
37657 O  OE2 . GLU   U  243 ? 2.2406 0.9599 1.6748 0.1950  -0.1072 -0.1288 234 GLU   U OE2 
37658 N  N   . ARG   U  244 ? 2.3270 0.7665 1.4842 -0.0336 -0.2339 0.0257  235 ARG   U N   
37659 C  CA  . ARG   U  244 ? 2.2551 0.8141 1.5444 -0.0175 -0.2452 0.1267  235 ARG   U CA  
37660 C  C   . ARG   U  244 ? 2.2222 0.8375 1.5270 0.0174  -0.2210 0.2146  235 ARG   U C   
37661 O  O   . ARG   U  244 ? 2.2366 1.0240 1.5814 -0.0370 -0.1910 0.1932  235 ARG   U O   
37662 C  CB  . ARG   U  244 ? 2.2184 0.7769 1.5479 0.0365  -0.2779 0.1281  235 ARG   U CB  
37663 C  CG  . ARG   U  244 ? 2.2435 0.6589 1.5612 0.0865  -0.2770 0.1255  235 ARG   U CG  
37664 C  CD  . ARG   U  244 ? 2.2912 0.6467 1.5636 0.0817  -0.2846 0.1401  235 ARG   U CD  
37665 N  NE  . ARG   U  244 ? 2.3417 0.5750 1.5572 0.1160  -0.3016 0.1041  235 ARG   U NE  
37666 C  CZ  . ARG   U  244 ? 2.3457 0.5564 1.5254 0.1824  -0.3023 0.1038  235 ARG   U CZ  
37667 N  NH1 . ARG   U  244 ? 2.3282 0.4416 1.5304 0.2448  -0.3623 0.1279  235 ARG   U NH1 
37668 N  NH2 . ARG   U  244 ? 2.3877 0.6269 1.4972 0.1736  -0.2961 0.0951  235 ARG   U NH2 
37669 N  N   . LEU   U  245 ? 2.2482 0.7130 1.4376 0.0262  -0.2455 0.2767  236 LEU   U N   
37670 C  CA  . LEU   U  245 ? 2.2550 0.7053 1.3877 -0.0063 -0.2391 0.3026  236 LEU   U CA  
37671 C  C   . LEU   U  245 ? 2.2856 0.6940 1.3804 0.0001  -0.2142 0.2775  236 LEU   U C   
37672 O  O   . LEU   U  245 ? 2.2796 0.7282 1.2685 -0.0239 -0.1888 0.2520  236 LEU   U O   
37673 C  CB  . LEU   U  245 ? 2.2452 0.6219 1.4103 0.0101  -0.2637 0.3821  236 LEU   U CB  
37674 C  CG  . LEU   U  245 ? 2.2224 0.5906 1.3729 0.0042  -0.2755 0.4334  236 LEU   U CG  
37675 C  CD1 . LEU   U  245 ? 2.2018 0.5699 1.3929 -0.0153 -0.2816 0.4296  236 LEU   U CD1 
37676 C  CD2 . LEU   U  245 ? 2.2017 0.6130 1.3731 0.0401  -0.2907 0.4493  236 LEU   U CD2 
37677 N  N   . VAL   U  246 ? 2.2850 0.8065 1.3092 0.0008  -0.2143 0.2817  237 VAL   U N   
37678 C  CA  . VAL   U  246 ? 2.2860 0.8557 1.3171 0.0124  -0.2092 0.3097  237 VAL   U CA  
37679 C  C   . VAL   U  246 ? 2.2870 0.8669 1.3471 -0.0070 -0.1986 0.3540  237 VAL   U C   
37680 O  O   . VAL   U  246 ? 2.3221 0.8357 1.3951 -0.0093 -0.2118 0.3707  237 VAL   U O   
37681 C  CB  . VAL   U  246 ? 2.2939 0.9321 1.2805 0.0257  -0.2052 0.2565  237 VAL   U CB  
37682 C  CG1 . VAL   U  246 ? 2.3150 0.9844 1.2929 0.0227  -0.1881 0.2529  237 VAL   U CG1 
37683 C  CG2 . VAL   U  246 ? 2.2920 0.9190 1.2492 0.0224  -0.2217 0.2256  237 VAL   U CG2 
37684 N  N   . ALA   U  247 ? 2.2647 0.9676 1.3851 0.0193  -0.2457 0.3649  238 ALA   U N   
37685 C  CA  . ALA   U  247 ? 2.2615 1.0227 1.4480 -0.0179 -0.2353 0.3326  238 ALA   U CA  
37686 C  C   . ALA   U  247 ? 2.2791 0.9731 1.5011 0.0126  -0.2571 0.3285  238 ALA   U C   
37687 O  O   . ALA   U  247 ? 2.2618 0.9208 1.4789 0.0172  -0.2915 0.3414  238 ALA   U O   
37688 C  CB  . ALA   U  247 ? 2.2782 1.0384 1.4591 0.0060  -0.2361 0.3301  238 ALA   U CB  
37689 N  N   . ILE   U  248 ? 2.2286 0.9138 1.5450 0.0102  -0.2463 0.3095  239 ILE   U N   
37690 C  CA  . ILE   U  248 ? 2.2097 0.8853 1.6151 0.0147  -0.2285 0.3229  239 ILE   U CA  
37691 C  C   . ILE   U  248 ? 2.2903 0.8413 1.7301 -0.0109 -0.2212 0.3541  239 ILE   U C   
37692 O  O   . ILE   U  248 ? 2.4118 0.7170 1.8258 -0.1090 -0.2741 0.2635  239 ILE   U O   
37693 C  CB  . ILE   U  248 ? 2.1237 0.8342 1.6470 0.0007  -0.2240 0.2675  239 ILE   U CB  
37694 C  CG1 . ILE   U  248 ? 2.1175 0.8579 1.6045 -0.0172 -0.2136 0.2743  239 ILE   U CG1 
37695 C  CG2 . ILE   U  248 ? 2.0862 0.7952 1.6616 0.0118  -0.2042 0.2955  239 ILE   U CG2 
37696 C  CD1 . ILE   U  248 ? 2.0945 0.8276 1.5660 -0.0195 -0.2518 0.2727  239 ILE   U CD1 
37697 N  N   . ALA   U  249 ? 2.2942 0.9272 1.8189 0.0596  -0.2002 0.3756  240 ALA   U N   
37698 C  CA  . ALA   U  249 ? 2.3699 0.9692 1.8978 0.1252  -0.1579 0.4217  240 ALA   U CA  
37699 C  C   . ALA   U  249 ? 2.4388 0.9688 1.9422 0.1204  -0.1011 0.4710  240 ALA   U C   
37700 O  O   . ALA   U  249 ? 2.4665 1.0771 2.0456 0.0705  -0.0782 0.5791  240 ALA   U O   
37701 C  CB  . ALA   U  249 ? 2.3631 0.9890 1.9083 0.1685  -0.1431 0.4318  240 ALA   U CB  
37702 N  N   . GLU   U  250 ? 2.5214 1.1023 1.9723 0.1192  -0.0522 0.3311  241 GLU   U N   
37703 C  CA  . GLU   U  250 ? 2.5571 1.2095 1.9980 0.1521  -0.0253 0.2978  241 GLU   U CA  
37704 C  C   . GLU   U  250 ? 2.5576 1.1942 1.9581 0.2445  -0.0572 0.2387  241 GLU   U C   
37705 O  O   . GLU   U  250 ? 2.4947 1.4499 1.9224 0.3206  -0.0427 0.2519  241 GLU   U O   
37706 C  CB  . GLU   U  250 ? 2.6316 1.2964 2.0100 0.0862  0.0129  0.2419  241 GLU   U CB  
37707 C  CG  . GLU   U  250 ? 2.6503 1.3301 2.0240 0.0684  -0.0049 0.2521  241 GLU   U CG  
37708 C  CD  . GLU   U  250 ? 2.6812 1.3099 2.0435 0.0725  0.0014  0.2503  241 GLU   U CD  
37709 O  OE1 . GLU   U  250 ? 2.6949 1.1554 2.0145 0.1085  -0.0700 0.2070  241 GLU   U OE1 
37710 O  OE2 . GLU   U  250 ? 2.7476 1.2725 2.0498 0.0766  0.0582  0.2934  241 GLU   U OE2 
37711 N  N   . GLN   U  251 ? 2.5727 1.0307 1.9993 0.3377  -0.0719 0.2274  242 GLN   U N   
37712 C  CA  . GLN   U  251 ? 2.5791 1.0776 2.0440 0.3257  -0.0738 0.1641  242 GLN   U CA  
37713 C  C   . GLN   U  251 ? 2.5747 0.9279 1.9788 0.3494  -0.1385 0.3279  242 GLN   U C   
37714 O  O   . GLN   U  251 ? 2.5274 0.9250 1.9306 0.3671  -0.1405 0.3270  242 GLN   U O   
37715 C  CB  . GLN   U  251 ? 2.6097 1.1186 2.0803 0.3041  -0.0966 0.1928  242 GLN   U CB  
37716 C  CG  . GLN   U  251 ? 2.6677 1.3149 2.1792 0.1677  -0.1393 0.1390  242 GLN   U CG  
37717 C  CD  . GLN   U  251 ? 2.7642 1.6077 2.2886 0.0696  -0.0436 0.1402  242 GLN   U CD  
37718 O  OE1 . GLN   U  251 ? 2.8847 2.0142 2.3204 -0.0319 -0.0941 0.2098  242 GLN   U OE1 
37719 N  NE2 . GLN   U  251 ? 2.8077 1.6542 2.2786 0.0210  -0.1246 0.1186  242 GLN   U NE2 
37720 N  N   . THR   V  1   ? 1.8161 0.8188 1.4613 0.0854  -0.3109 0.1658  2   THR   V N   
37721 C  CA  . THR   V  1   ? 1.7272 0.7858 1.4571 0.0364  -0.3179 0.1682  2   THR   V CA  
37722 C  C   . THR   V  1   ? 1.7043 0.8290 1.4599 0.0448  -0.2914 0.2215  2   THR   V C   
37723 O  O   . THR   V  1   ? 1.7009 0.9451 1.5243 -0.0053 -0.2363 0.1922  2   THR   V O   
37724 C  CB  . THR   V  1   ? 1.7041 0.7460 1.4169 0.0016  -0.3264 0.1574  2   THR   V CB  
37725 O  OG1 . THR   V  1   ? 1.7354 0.7851 1.3899 0.0405  -0.3257 0.1966  2   THR   V OG1 
37726 C  CG2 . THR   V  1   ? 1.6431 0.7346 1.4129 -0.0135 -0.3273 0.1531  2   THR   V CG2 
37727 N  N   . ILE   V  2   ? 1.6581 0.7342 1.4069 -0.0067 -0.2433 0.2470  3   ILE   V N   
37728 C  CA  . ILE   V  2   ? 1.6664 0.6978 1.3770 -0.0033 -0.2220 0.2063  3   ILE   V CA  
37729 C  C   . ILE   V  2   ? 1.5550 0.5669 1.3817 0.0204  -0.2275 0.2262  3   ILE   V C   
37730 O  O   . ILE   V  2   ? 1.4715 0.6163 1.3749 0.0653  -0.2349 0.2478  3   ILE   V O   
37731 C  CB  . ILE   V  2   ? 1.7785 0.6147 1.3546 -0.0363 -0.1873 0.1790  3   ILE   V CB  
37732 C  CG1 . ILE   V  2   ? 1.8321 0.6281 1.3635 -0.0466 -0.1972 0.2012  3   ILE   V CG1 
37733 C  CG2 . ILE   V  2   ? 1.8357 0.6594 1.3073 -0.0439 -0.2227 0.2064  3   ILE   V CG2 
37734 C  CD1 . ILE   V  2   ? 1.8447 0.7044 1.4149 -0.0302 -0.1549 0.2020  3   ILE   V CD1 
37735 N  N   . VAL   V  3   ? 1.4871 0.5576 1.3921 0.0400  -0.2321 0.2071  4   VAL   V N   
37736 C  CA  . VAL   V  3   ? 1.4587 0.5996 1.3871 0.0488  -0.2460 0.2008  4   VAL   V CA  
37737 C  C   . VAL   V  3   ? 1.4240 0.6014 1.3458 0.0584  -0.2534 0.2022  4   VAL   V C   
37738 O  O   . VAL   V  3   ? 1.3479 0.5391 1.3165 0.1019  -0.2790 0.2586  4   VAL   V O   
37739 C  CB  . VAL   V  3   ? 1.4738 0.5906 1.4031 0.0387  -0.2348 0.1904  4   VAL   V CB  
37740 C  CG1 . VAL   V  3   ? 1.5098 0.5978 1.4575 0.0302  -0.2226 0.1990  4   VAL   V CG1 
37741 C  CG2 . VAL   V  3   ? 1.4701 0.5982 1.3895 0.0373  -0.2298 0.1927  4   VAL   V CG2 
37742 N  N   . GLY   V  4   ? 1.4329 0.6123 1.3351 0.0654  -0.2404 0.1985  5   GLY   V N   
37743 C  CA  . GLY   V  4   ? 1.4501 0.6323 1.3392 0.0210  -0.2154 0.1956  5   GLY   V CA  
37744 C  C   . GLY   V  4   ? 1.4692 0.6316 1.3341 -0.0011 -0.2402 0.1722  5   GLY   V C   
37745 O  O   . GLY   V  4   ? 1.5294 0.5483 1.2171 0.0469  -0.2592 0.1774  5   GLY   V O   
37746 N  N   . VAL   V  5   ? 1.4915 0.7256 1.3279 -0.0231 -0.2141 0.1623  6   VAL   V N   
37747 C  CA  . VAL   V  5   ? 1.5390 0.7407 1.3134 -0.0208 -0.2360 0.1505  6   VAL   V CA  
37748 C  C   . VAL   V  5   ? 1.5740 0.7015 1.3094 0.0101  -0.2440 0.1265  6   VAL   V C   
37749 O  O   . VAL   V  5   ? 1.6230 0.5728 1.3277 0.0287  -0.2449 0.1540  6   VAL   V O   
37750 C  CB  . VAL   V  5   ? 1.5436 0.7786 1.3440 -0.0085 -0.2203 0.1796  6   VAL   V CB  
37751 C  CG1 . VAL   V  5   ? 1.5503 0.8826 1.3463 -0.0062 -0.2196 0.1512  6   VAL   V CG1 
37752 C  CG2 . VAL   V  5   ? 1.5488 0.8032 1.3646 -0.0274 -0.2249 0.2132  6   VAL   V CG2 
37753 N  N   . LYS   V  6   ? 1.6005 0.7129 1.3022 0.0241  -0.2286 0.1438  7   LYS   V N   
37754 C  CA  . LYS   V  6   ? 1.6664 0.7405 1.3309 0.0073  -0.1966 0.1633  7   LYS   V CA  
37755 C  C   . LYS   V  6   ? 1.6770 0.8125 1.3849 -0.0425 -0.1603 0.1826  7   LYS   V C   
37756 O  O   . LYS   V  6   ? 1.7722 0.8051 1.3774 -0.0792 -0.1565 0.1953  7   LYS   V O   
37757 C  CB  . LYS   V  6   ? 1.7119 0.7440 1.2899 0.0400  -0.2058 0.1885  7   LYS   V CB  
37758 C  CG  . LYS   V  6   ? 1.7520 0.7349 1.2715 0.0609  -0.2114 0.1909  7   LYS   V CG  
37759 C  CD  . LYS   V  6   ? 1.7865 0.7420 1.3021 0.0988  -0.2118 0.1828  7   LYS   V CD  
37760 C  CE  . LYS   V  6   ? 1.8004 0.7065 1.3090 0.1442  -0.2124 0.1954  7   LYS   V CE  
37761 N  NZ  . LYS   V  6   ? 1.8281 0.6834 1.3165 0.1056  -0.2049 0.2211  7   LYS   V NZ  
37762 N  N   . PHE   V  7   ? 1.7198 0.7431 1.4781 -0.0291 -0.1567 0.1764  8   PHE   V N   
37763 C  CA  . PHE   V  7   ? 1.7105 0.7068 1.5417 -0.0224 -0.1315 0.2292  8   PHE   V CA  
37764 C  C   . PHE   V  7   ? 1.6978 0.7175 1.5800 0.0391  -0.1171 0.2417  8   PHE   V C   
37765 O  O   . PHE   V  7   ? 1.6991 0.6470 1.5523 0.0478  -0.1798 0.3047  8   PHE   V O   
37766 C  CB  . PHE   V  7   ? 1.6974 0.6952 1.5746 -0.0342 -0.1221 0.2428  8   PHE   V CB  
37767 C  CG  . PHE   V  7   ? 1.7155 0.6490 1.6170 -0.0462 -0.1253 0.2568  8   PHE   V CG  
37768 C  CD1 . PHE   V  7   ? 1.7242 0.6725 1.6901 -0.0812 -0.1080 0.2418  8   PHE   V CD1 
37769 C  CD2 . PHE   V  7   ? 1.7093 0.5871 1.6123 -0.0400 -0.1485 0.2947  8   PHE   V CD2 
37770 C  CE1 . PHE   V  7   ? 1.7191 0.7356 1.6968 -0.1097 -0.1233 0.2330  8   PHE   V CE1 
37771 C  CE2 . PHE   V  7   ? 1.7241 0.5878 1.6226 -0.0519 -0.1527 0.2959  8   PHE   V CE2 
37772 C  CZ  . PHE   V  7   ? 1.7038 0.6747 1.6956 -0.1201 -0.1269 0.2804  8   PHE   V CZ  
37773 N  N   . ASN   V  8   ? 1.7338 0.8007 1.6325 0.0867  -0.0691 0.2840  9   ASN   V N   
37774 C  CA  . ASN   V  8   ? 1.7791 0.8825 1.7092 0.0721  -0.0699 0.3616  9   ASN   V CA  
37775 C  C   . ASN   V  8   ? 1.8628 0.9080 1.7373 -0.0329 -0.0708 0.3170  9   ASN   V C   
37776 O  O   . ASN   V  8   ? 1.8680 0.9346 1.7668 -0.0643 -0.0947 0.4206  9   ASN   V O   
37777 C  CB  . ASN   V  8   ? 1.7812 0.9208 1.8347 0.0389  -0.0331 0.4202  9   ASN   V CB  
37778 C  CG  . ASN   V  8   ? 1.7669 0.9702 1.9461 0.1012  -0.0348 0.5049  9   ASN   V CG  
37779 O  OD1 . ASN   V  8   ? 1.8067 0.9935 2.0550 0.0844  -0.1092 0.5160  9   ASN   V OD1 
37780 N  ND2 . ASN   V  8   ? 1.7680 0.9491 2.0080 0.0280  -0.0215 0.5556  9   ASN   V ND2 
37781 N  N   . ASN   V  9   ? 1.8660 0.9938 1.7764 -0.0659 -0.0832 0.3156  10  ASN   V N   
37782 C  CA  . ASN   V  9   ? 1.8926 1.0277 1.8256 -0.0871 -0.0486 0.2609  10  ASN   V CA  
37783 C  C   . ASN   V  9   ? 1.8555 0.8584 1.8432 -0.0765 -0.0399 0.2116  10  ASN   V C   
37784 O  O   . ASN   V  9   ? 1.8321 0.8490 1.9312 -0.0995 0.0459  0.1923  10  ASN   V O   
37785 C  CB  . ASN   V  9   ? 1.8707 1.2282 1.8968 -0.0727 -0.0368 0.2522  10  ASN   V CB  
37786 C  CG  . ASN   V  9   ? 1.9520 1.2418 1.9809 -0.0361 -0.0606 0.2714  10  ASN   V CG  
37787 O  OD1 . ASN   V  9   ? 2.1009 1.3950 1.9324 0.0159  -0.0870 0.3511  10  ASN   V OD1 
37788 N  ND2 . ASN   V  9   ? 1.9092 1.3936 2.0994 -0.0385 -0.0696 0.2332  10  ASN   V ND2 
37789 N  N   . GLY   V  10  ? 1.8074 0.8027 1.7245 -0.0534 -0.0673 0.1551  11  GLY   V N   
37790 C  CA  . GLY   V  10  ? 1.7713 0.7151 1.7085 -0.0537 -0.0910 0.0938  11  GLY   V CA  
37791 C  C   . GLY   V  10  ? 1.7269 0.7341 1.6401 -0.0868 -0.0884 0.0543  11  GLY   V C   
37792 O  O   . GLY   V  10  ? 1.7630 0.8098 1.6677 -0.1287 -0.1130 0.0235  11  GLY   V O   
37793 N  N   . VAL   V  11  ? 1.6498 0.5500 1.6178 -0.0887 -0.1083 0.0064  12  VAL   V N   
37794 C  CA  . VAL   V  11  ? 1.5955 0.4559 1.5860 -0.0369 -0.1570 -0.0153 12  VAL   V CA  
37795 C  C   . VAL   V  11  ? 1.6073 0.4519 1.5980 -0.0428 -0.1794 -0.0303 12  VAL   V C   
37796 O  O   . VAL   V  11  ? 1.6183 0.2583 1.6385 0.0531  -0.1729 0.0127  12  VAL   V O   
37797 C  CB  . VAL   V  11  ? 1.5718 0.4243 1.5642 -0.0562 -0.1722 -0.0192 12  VAL   V CB  
37798 C  CG1 . VAL   V  11  ? 1.5785 0.4778 1.5630 -0.0541 -0.1760 -0.0457 12  VAL   V CG1 
37799 C  CG2 . VAL   V  11  ? 1.4990 0.4865 1.5238 -0.0699 -0.1608 -0.0116 12  VAL   V CG2 
37800 N  N   . VAL   V  12  ? 1.6298 0.4763 1.5660 -0.0010 -0.2018 -0.0039 13  VAL   V N   
37801 C  CA  . VAL   V  12  ? 1.6320 0.4739 1.5136 -0.0056 -0.1857 -0.0180 13  VAL   V CA  
37802 C  C   . VAL   V  12  ? 1.6268 0.2891 1.4446 -0.0026 -0.2415 -0.0717 13  VAL   V C   
37803 O  O   . VAL   V  12  ? 1.6796 0.2306 1.4420 -0.0479 -0.1827 0.0066  13  VAL   V O   
37804 C  CB  . VAL   V  12  ? 1.6575 0.5154 1.5504 0.0410  -0.2116 -0.0427 13  VAL   V CB  
37805 C  CG1 . VAL   V  12  ? 1.6394 0.5132 1.5393 0.0424  -0.2029 -0.0365 13  VAL   V CG1 
37806 C  CG2 . VAL   V  12  ? 1.6764 0.5126 1.5519 0.0508  -0.2215 -0.0594 13  VAL   V CG2 
37807 N  N   . ILE   V  13  ? 1.6351 0.3308 1.4382 0.0130  -0.1910 0.0154  14  ILE   V N   
37808 C  CA  . ILE   V  13  ? 1.6484 0.3303 1.4741 -0.0006 -0.2085 0.0407  14  ILE   V CA  
37809 C  C   . ILE   V  13  ? 1.6525 0.3562 1.4480 0.0178  -0.2096 0.0156  14  ILE   V C   
37810 O  O   . ILE   V  13  ? 1.6788 0.2588 1.4264 -0.0103 -0.1882 0.0926  14  ILE   V O   
37811 C  CB  . ILE   V  13  ? 1.6282 0.4034 1.4906 0.0294  -0.1905 0.0988  14  ILE   V CB  
37812 C  CG1 . ILE   V  13  ? 1.6346 0.4855 1.4649 0.0365  -0.2067 0.0933  14  ILE   V CG1 
37813 C  CG2 . ILE   V  13  ? 1.6421 0.4046 1.5008 0.0184  -0.2004 0.1209  14  ILE   V CG2 
37814 C  CD1 . ILE   V  13  ? 1.6210 0.5170 1.4727 0.0469  -0.2024 0.1095  14  ILE   V CD1 
37815 N  N   . ALA   V  14  ? 1.6523 0.3915 1.4295 -0.0005 -0.1854 0.0388  15  ALA   V N   
37816 C  CA  . ALA   V  14  ? 1.5767 0.5525 1.4154 0.0381  -0.2005 0.0071  15  ALA   V CA  
37817 C  C   . ALA   V  14  ? 1.5572 0.5512 1.3716 0.0524  -0.1866 -0.0285 15  ALA   V C   
37818 O  O   . ALA   V  14  ? 1.5414 0.5696 1.3488 0.0778  -0.1681 -0.0852 15  ALA   V O   
37819 C  CB  . ALA   V  14  ? 1.5191 0.5996 1.4215 0.0428  -0.1906 0.0366  15  ALA   V CB  
37820 N  N   . ALA   V  15  ? 1.5251 0.5574 1.3538 0.0533  -0.1569 -0.0292 16  ALA   V N   
37821 C  CA  . ALA   V  15  ? 1.4922 0.5739 1.4194 0.0241  -0.1271 -0.0355 16  ALA   V CA  
37822 C  C   . ALA   V  15  ? 1.4558 0.5883 1.4306 0.0018  -0.1206 -0.0110 16  ALA   V C   
37823 O  O   . ALA   V  15  ? 1.4486 0.6462 1.4670 0.0056  -0.1072 0.0055  16  ALA   V O   
37824 C  CB  . ALA   V  15  ? 1.4902 0.5570 1.4566 0.0367  -0.1128 -0.0178 16  ALA   V CB  
37825 N  N   . ASP   V  16  ? 1.4125 0.5883 1.4404 0.0000  -0.1499 -0.0012 17  ASP   V N   
37826 C  CA  . ASP   V  16  ? 1.4194 0.6770 1.4847 0.0119  -0.1746 0.0215  17  ASP   V CA  
37827 C  C   . ASP   V  16  ? 1.4679 0.6793 1.5133 -0.0048 -0.1946 -0.0053 17  ASP   V C   
37828 O  O   . ASP   V  16  ? 1.4710 0.7994 1.5630 0.1010  -0.1819 -0.0652 17  ASP   V O   
37829 C  CB  . ASP   V  16  ? 1.3983 0.6982 1.4954 -0.0030 -0.1873 0.0946  17  ASP   V CB  
37830 C  CG  . ASP   V  16  ? 1.3782 0.8059 1.5191 0.0078  -0.1948 0.1145  17  ASP   V CG  
37831 O  OD1 . ASP   V  16  ? 1.4077 0.7354 1.4986 0.0131  -0.2347 0.2234  17  ASP   V OD1 
37832 O  OD2 . ASP   V  16  ? 1.3750 0.8200 1.6033 -0.0048 -0.2567 0.1366  17  ASP   V OD2 
37833 N  N   . THR   V  17  ? 1.4761 0.5790 1.5205 -0.0194 -0.1935 -0.0141 18  THR   V N   
37834 C  CA  . THR   V  17  ? 1.5292 0.5704 1.5495 -0.0395 -0.1908 -0.0447 18  THR   V CA  
37835 C  C   . THR   V  17  ? 1.5294 0.6633 1.4681 -0.0350 -0.2112 -0.0613 18  THR   V C   
37836 O  O   . THR   V  17  ? 1.5798 0.6814 1.4783 -0.0632 -0.1940 -0.0957 18  THR   V O   
37837 C  CB  . THR   V  17  ? 1.5260 0.5814 1.6343 -0.0521 -0.1532 -0.0718 18  THR   V CB  
37838 O  OG1 . THR   V  17  ? 1.5471 0.4872 1.6626 -0.0888 -0.1607 -0.1070 18  THR   V OG1 
37839 C  CG2 . THR   V  17  ? 1.5507 0.6035 1.6823 -0.0791 -0.1297 -0.0947 18  THR   V CG2 
37840 N  N   . ARG   V  18  ? 1.4868 0.6910 1.4289 -0.0314 -0.2535 -0.0164 19  ARG   V N   
37841 C  CA  . ARG   V  18  ? 1.4906 0.7558 1.4029 0.0510  -0.3126 0.0734  19  ARG   V CA  
37842 C  C   . ARG   V  18  ? 1.5044 0.6091 1.3448 0.0991  -0.3402 0.0798  19  ARG   V C   
37843 O  O   . ARG   V  18  ? 1.4537 0.6407 1.4211 0.1642  -0.3544 0.1040  19  ARG   V O   
37844 C  CB  . ARG   V  18  ? 1.5100 0.7570 1.4024 0.0621  -0.3303 0.1006  19  ARG   V CB  
37845 C  CG  . ARG   V  18  ? 1.4987 0.8438 1.3799 0.0657  -0.3589 0.1477  19  ARG   V CG  
37846 C  CD  . ARG   V  18  ? 1.4797 0.8265 1.3570 0.0830  -0.3655 0.1642  19  ARG   V CD  
37847 N  NE  . ARG   V  18  ? 1.4348 0.9805 1.2938 0.0889  -0.4174 0.2206  19  ARG   V NE  
37848 C  CZ  . ARG   V  18  ? 1.3813 1.0090 1.3387 0.1978  -0.4011 0.2666  19  ARG   V CZ  
37849 N  NH1 . ARG   V  18  ? 1.4085 1.1750 1.3913 0.1021  -0.4051 0.2395  19  ARG   V NH1 
37850 N  NH2 . ARG   V  18  ? 1.4136 1.0501 1.1891 0.1736  -0.5167 0.3527  19  ARG   V NH2 
37851 N  N   . SER   V  19  ? 1.5118 0.5479 1.3337 0.1226  -0.3478 0.1030  20  SER   V N   
37852 C  CA  . SER   V  19  ? 1.5107 0.5209 1.3463 0.1355  -0.3504 0.1299  20  SER   V CA  
37853 C  C   . SER   V  19  ? 1.4778 0.4369 1.3989 0.1266  -0.3548 0.1000  20  SER   V C   
37854 O  O   . SER   V  19  ? 1.5030 0.4137 1.4443 0.1741  -0.3545 0.1539  20  SER   V O   
37855 C  CB  . SER   V  19  ? 1.5545 0.4834 1.3347 0.1499  -0.3426 0.1741  20  SER   V CB  
37856 O  OG  . SER   V  19  ? 1.6279 0.4779 1.3496 0.1421  -0.2919 0.1817  20  SER   V OG  
37857 N  N   . THR   V  20  ? 1.4815 0.3857 1.4242 0.1324  -0.3558 0.0693  21  THR   V N   
37858 C  CA  . THR   V  20  ? 1.4816 0.4010 1.4372 0.0986  -0.3246 0.0614  21  THR   V CA  
37859 C  C   . THR   V  20  ? 1.4730 0.4121 1.4230 0.1283  -0.3429 0.0413  21  THR   V C   
37860 O  O   . THR   V  20  ? 1.4507 0.3001 1.3628 0.0705  -0.3304 0.0405  21  THR   V O   
37861 C  CB  . THR   V  20  ? 1.4662 0.3877 1.5050 0.0863  -0.3191 0.0478  21  THR   V CB  
37862 O  OG1 . THR   V  20  ? 1.4550 0.2542 1.5512 0.0924  -0.3227 0.0717  21  THR   V OG1 
37863 C  CG2 . THR   V  20  ? 1.4503 0.3884 1.5412 0.0798  -0.3172 0.0350  21  THR   V CG2 
37864 N  N   . GLN   V  21  ? 1.5604 0.5950 1.3745 0.0752  -0.2651 0.0203  22  GLN   V N   
37865 C  CA  . GLN   V  21  ? 1.5716 0.7464 1.3902 0.0649  -0.2492 -0.0227 22  GLN   V CA  
37866 C  C   . GLN   V  21  ? 1.4325 0.7476 1.3740 0.0815  -0.2663 -0.0145 22  GLN   V C   
37867 O  O   . GLN   V  21  ? 1.3792 0.5908 1.3959 0.1144  -0.2041 -0.0548 22  GLN   V O   
37868 C  CB  . GLN   V  21  ? 1.7780 0.8684 1.3767 0.0385  -0.2132 -0.0488 22  GLN   V CB  
37869 C  CG  . GLN   V  21  ? 1.8248 0.9796 1.3599 0.0422  -0.1909 -0.0577 22  GLN   V CG  
37870 C  CD  . GLN   V  21  ? 1.9700 1.1498 1.3468 -0.0507 -0.2543 -0.0831 22  GLN   V CD  
37871 O  OE1 . GLN   V  21  ? 2.1002 1.2196 1.2627 -0.1688 -0.3332 -0.1336 22  GLN   V OE1 
37872 N  NE2 . GLN   V  21  ? 1.9859 1.2717 1.3166 -0.0720 -0.2563 -0.0786 22  GLN   V NE2 
37873 N  N   . GLY   V  22  ? 1.4273 0.7772 1.3754 0.0678  -0.2657 0.0039  23  GLY   V N   
37874 C  CA  . GLY   V  22  ? 1.4595 0.7722 1.3192 0.0599  -0.2958 0.0455  23  GLY   V CA  
37875 C  C   . GLY   V  22  ? 1.4280 0.8210 1.2491 0.0275  -0.2992 0.0720  23  GLY   V C   
37876 O  O   . GLY   V  22  ? 1.4643 0.8453 1.2321 -0.0075 -0.3424 0.0964  23  GLY   V O   
37877 N  N   . PRO   V  23  ? 1.4655 0.7990 1.2718 -0.0216 -0.3355 0.0971  24  PRO   V N   
37878 C  CA  . PRO   V  23  ? 1.4798 0.7066 1.3108 -0.0537 -0.2961 0.1125  24  PRO   V CA  
37879 C  C   . PRO   V  23  ? 1.4276 0.7444 1.3697 -0.0526 -0.2641 0.1730  24  PRO   V C   
37880 O  O   . PRO   V  23  ? 1.4306 0.6635 1.3787 -0.0425 -0.2535 0.2531  24  PRO   V O   
37881 C  CB  . PRO   V  23  ? 1.4683 0.6844 1.3138 -0.0864 -0.3102 0.0608  24  PRO   V CB  
37882 C  CG  . PRO   V  23  ? 1.4849 0.6721 1.3112 -0.0950 -0.3150 0.0459  24  PRO   V CG  
37883 C  CD  . PRO   V  23  ? 1.4738 0.7302 1.2823 -0.0513 -0.3190 0.0640  24  PRO   V CD  
37884 N  N   . ILE   V  24  ? 1.4326 0.7379 1.3922 -0.0785 -0.2618 0.1678  25  ILE   V N   
37885 C  CA  . ILE   V  24  ? 1.4129 0.8180 1.4049 -0.0224 -0.3022 0.1509  25  ILE   V CA  
37886 C  C   . ILE   V  24  ? 1.4051 0.8380 1.4058 -0.0381 -0.2976 0.1500  25  ILE   V C   
37887 O  O   . ILE   V  24  ? 1.4346 0.8749 1.4754 -0.0130 -0.3013 0.1881  25  ILE   V O   
37888 C  CB  . ILE   V  24  ? 1.4475 0.8530 1.4153 -0.0085 -0.2764 0.1579  25  ILE   V CB  
37889 C  CG1 . ILE   V  24  ? 1.4577 0.8553 1.4546 -0.0054 -0.2587 0.1710  25  ILE   V CG1 
37890 C  CG2 . ILE   V  24  ? 1.4777 0.9015 1.4343 -0.0326 -0.2717 0.1254  25  ILE   V CG2 
37891 C  CD1 . ILE   V  24  ? 1.4592 0.9144 1.4781 -0.0016 -0.2496 0.1841  25  ILE   V CD1 
37892 N  N   . VAL   V  25  ? 1.4033 0.7985 1.4128 -0.0485 -0.3050 0.1060  26  VAL   V N   
37893 C  CA  . VAL   V  25  ? 1.4423 0.7879 1.4642 -0.0503 -0.3007 0.1142  26  VAL   V CA  
37894 C  C   . VAL   V  25  ? 1.4518 0.7782 1.5078 -0.0068 -0.3214 0.0997  26  VAL   V C   
37895 O  O   . VAL   V  25  ? 1.4545 0.8449 1.5659 -0.0018 -0.3410 0.1322  26  VAL   V O   
37896 C  CB  . VAL   V  25  ? 1.4695 0.7532 1.4572 -0.0544 -0.2846 0.0855  26  VAL   V CB  
37897 C  CG1 . VAL   V  25  ? 1.5003 0.8057 1.4595 -0.0953 -0.2611 0.0914  26  VAL   V CG1 
37898 C  CG2 . VAL   V  25  ? 1.4550 0.7246 1.5123 -0.0380 -0.2700 0.0696  26  VAL   V CG2 
37899 N  N   . ALA   V  26  ? 1.4584 0.7946 1.5714 0.0074  -0.3301 0.0922  27  ALA   V N   
37900 C  CA  . ALA   V  26  ? 1.4159 0.7363 1.5943 0.0141  -0.3354 0.1132  27  ALA   V CA  
37901 C  C   . ALA   V  26  ? 1.4734 0.6966 1.6248 -0.0149 -0.3190 0.0910  27  ALA   V C   
37902 O  O   . ALA   V  26  ? 1.5181 0.5632 1.6922 -0.0483 -0.3211 0.0220  27  ALA   V O   
37903 C  CB  . ALA   V  26  ? 1.4660 0.6612 1.5770 0.0399  -0.3457 0.1243  27  ALA   V CB  
37904 N  N   . ASP   V  27  ? 1.4151 0.6676 1.6347 -0.0568 -0.2912 0.0973  28  ASP   V N   
37905 C  CA  . ASP   V  27  ? 1.4315 0.6796 1.6337 -0.0567 -0.2414 0.0887  28  ASP   V CA  
37906 C  C   . ASP   V  27  ? 1.3872 0.5445 1.6353 -0.0775 -0.2578 0.1014  28  ASP   V C   
37907 O  O   . ASP   V  27  ? 1.3237 0.4107 1.6518 -0.0841 -0.2473 0.1138  28  ASP   V O   
37908 C  CB  . ASP   V  27  ? 1.4582 0.7204 1.6779 0.0131  -0.1849 0.0954  28  ASP   V CB  
37909 C  CG  . ASP   V  27  ? 1.4527 0.8247 1.7681 -0.0340 -0.1085 0.0900  28  ASP   V CG  
37910 O  OD1 . ASP   V  27  ? 1.5070 0.8470 1.8247 0.0223  -0.0155 0.1563  28  ASP   V OD1 
37911 O  OD2 . ASP   V  27  ? 1.5018 0.9660 1.8571 0.0624  -0.0244 0.1405  28  ASP   V OD2 
37912 N  N   . LYS   V  28  ? 1.3974 0.5398 1.6197 -0.0657 -0.2699 0.0809  29  LYS   V N   
37913 C  CA  . LYS   V  28  ? 1.4278 0.5931 1.5869 -0.0775 -0.2657 0.0785  29  LYS   V CA  
37914 C  C   . LYS   V  28  ? 1.4577 0.5924 1.5770 -0.0903 -0.2424 0.0659  29  LYS   V C   
37915 O  O   . LYS   V  28  ? 1.4606 0.5552 1.6001 -0.1066 -0.1723 0.0734  29  LYS   V O   
37916 C  CB  . LYS   V  28  ? 1.4306 0.6616 1.6131 -0.0604 -0.2744 0.0860  29  LYS   V CB  
37917 C  CG  . LYS   V  28  ? 1.4082 0.6723 1.5978 -0.0229 -0.2815 0.1037  29  LYS   V CG  
37918 C  CD  . LYS   V  28  ? 1.4095 0.6983 1.6310 -0.0110 -0.2731 0.1173  29  LYS   V CD  
37919 C  CE  . LYS   V  28  ? 1.4365 0.7373 1.6523 0.0207  -0.2913 0.0929  29  LYS   V CE  
37920 N  NZ  . LYS   V  28  ? 1.4565 0.7890 1.6800 0.0432  -0.3104 0.1068  29  LYS   V NZ  
37921 N  N   . ASN   V  29  ? 1.4594 0.6071 1.5560 -0.1041 -0.2434 0.0454  30  ASN   V N   
37922 C  CA  . ASN   V  29  ? 1.4744 0.6437 1.5567 -0.1320 -0.2429 0.0615  30  ASN   V CA  
37923 C  C   . ASN   V  29  ? 1.5075 0.6273 1.5880 -0.1212 -0.2586 0.1123  30  ASN   V C   
37924 O  O   . ASN   V  29  ? 1.6099 0.6127 1.6530 -0.1546 -0.2543 0.0953  30  ASN   V O   
37925 C  CB  . ASN   V  29  ? 1.4381 0.6047 1.5403 -0.0702 -0.1819 0.0524  30  ASN   V CB  
37926 C  CG  . ASN   V  29  ? 1.4183 0.5940 1.5339 -0.0688 -0.1690 0.0371  30  ASN   V CG  
37927 O  OD1 . ASN   V  29  ? 1.4168 0.5182 1.6007 -0.0492 -0.1573 0.0434  30  ASN   V OD1 
37928 N  ND2 . ASN   V  29  ? 1.4174 0.6142 1.5164 -0.0751 -0.2057 0.0325  30  ASN   V ND2 
37929 N  N   . CYS   V  30  ? 1.5487 0.6556 1.5861 -0.2035 -0.2999 0.1528  31  CYS   V N   
37930 C  CA  . CYS   V  30  ? 1.5388 0.6497 1.6880 -0.2192 -0.2944 0.1328  31  CYS   V CA  
37931 C  C   . CYS   V  30  ? 1.5418 0.6335 1.7102 -0.2484 -0.3278 0.1254  31  CYS   V C   
37932 O  O   . CYS   V  30  ? 1.4601 0.7821 1.8138 -0.2323 -0.2877 0.0083  31  CYS   V O   
37933 C  CB  . CYS   V  30  ? 1.6065 0.6914 1.7041 -0.1971 -0.2407 0.2756  31  CYS   V CB  
37934 S  SG  . CYS   V  30  ? 1.6028 0.6799 1.6845 -0.2863 -0.2521 0.4367  31  CYS   V SG  
37935 N  N   . ALA   V  31  ? 1.5647 0.6045 1.7417 -0.2807 -0.3852 0.0293  32  ALA   V N   
37936 C  CA  . ALA   V  31  ? 1.5787 0.5576 1.7625 -0.2508 -0.3992 0.0187  32  ALA   V CA  
37937 C  C   . ALA   V  31  ? 1.5860 0.5074 1.7257 -0.2153 -0.3984 0.0432  32  ALA   V C   
37938 O  O   . ALA   V  31  ? 1.6189 0.3731 1.7336 -0.2329 -0.3902 0.0227  32  ALA   V O   
37939 C  CB  . ALA   V  31  ? 1.5646 0.5592 1.8000 -0.2500 -0.4123 -0.0510 32  ALA   V CB  
37940 N  N   . LYS   V  32  ? 1.7026 0.4861 1.6624 -0.2215 -0.3829 0.0947  33  LYS   V N   
37941 C  CA  . LYS   V  32  ? 1.7030 0.4948 1.6209 -0.1654 -0.3657 0.1218  33  LYS   V CA  
37942 C  C   . LYS   V  32  ? 1.7298 0.3666 1.6541 -0.1051 -0.3676 0.0638  33  LYS   V C   
37943 O  O   . LYS   V  32  ? 1.7515 0.2118 1.7337 -0.0205 -0.3983 0.1044  33  LYS   V O   
37944 C  CB  . LYS   V  32  ? 1.7251 0.4969 1.5759 -0.1421 -0.3339 0.1120  33  LYS   V CB  
37945 C  CG  . LYS   V  32  ? 1.6971 0.5673 1.5544 -0.0807 -0.3423 0.1164  33  LYS   V CG  
37946 C  CD  . LYS   V  32  ? 1.6602 0.5482 1.4804 -0.0854 -0.3296 0.1589  33  LYS   V CD  
37947 C  CE  . LYS   V  32  ? 1.6438 0.5328 1.4882 -0.0741 -0.2789 0.1768  33  LYS   V CE  
37948 N  NZ  . LYS   V  32  ? 1.6534 0.5361 1.4352 -0.0399 -0.2802 0.1791  33  LYS   V NZ  
37949 N  N   . LEU   V  33  ? 1.7510 0.4418 1.6245 -0.1239 -0.2985 0.0576  34  LEU   V N   
37950 C  CA  . LEU   V  33  ? 1.7169 0.4935 1.5495 -0.1406 -0.2595 0.0590  34  LEU   V CA  
37951 C  C   . LEU   V  33  ? 1.7419 0.4903 1.5355 -0.0738 -0.2951 0.0742  34  LEU   V C   
37952 O  O   . LEU   V  33  ? 1.8291 0.4272 1.5152 -0.0427 -0.2998 -0.0128 34  LEU   V O   
37953 C  CB  . LEU   V  33  ? 1.7535 0.5011 1.5271 -0.1598 -0.2239 0.0354  34  LEU   V CB  
37954 C  CG  . LEU   V  33  ? 1.7025 0.4252 1.5385 -0.1544 -0.2105 0.0364  34  LEU   V CG  
37955 C  CD1 . LEU   V  33  ? 1.6814 0.3935 1.4921 -0.1234 -0.1916 0.0446  34  LEU   V CD1 
37956 C  CD2 . LEU   V  33  ? 1.7029 0.4476 1.5398 -0.1449 -0.2199 0.0089  34  LEU   V CD2 
37957 N  N   . HIS   V  34  ? 1.7280 0.6559 1.5153 -0.0558 -0.3445 0.0951  35  HIS   V N   
37958 C  CA  . HIS   V  34  ? 1.7596 0.7502 1.4945 -0.0050 -0.3207 0.0598  35  HIS   V CA  
37959 C  C   . HIS   V  34  ? 1.7062 0.7089 1.5019 -0.0363 -0.3458 0.0455  35  HIS   V C   
37960 O  O   . HIS   V  34  ? 1.6984 0.6462 1.4799 -0.0083 -0.3450 0.0944  35  HIS   V O   
37961 C  CB  . HIS   V  34  ? 1.7860 0.9030 1.5029 0.0255  -0.2891 0.0715  35  HIS   V CB  
37962 C  CG  . HIS   V  34  ? 1.8625 0.9581 1.4411 0.0917  -0.2735 0.1290  35  HIS   V CG  
37963 N  ND1 . HIS   V  34  ? 1.8721 1.0810 1.4226 0.1541  -0.2926 0.0506  35  HIS   V ND1 
37964 C  CD2 . HIS   V  34  ? 1.9232 1.0173 1.4133 0.1377  -0.2963 0.0337  35  HIS   V CD2 
37965 C  CE1 . HIS   V  34  ? 1.9307 1.0748 1.4142 0.2129  -0.2911 0.0738  35  HIS   V CE1 
37966 N  NE2 . HIS   V  34  ? 1.9369 1.1587 1.3928 0.2143  -0.3117 0.0840  35  HIS   V NE2 
37967 N  N   . ARG   V  35  ? 1.6780 0.6586 1.4783 -0.0169 -0.3393 0.0890  36  ARG   V N   
37968 C  CA  . ARG   V  35  ? 1.6520 0.6334 1.4224 0.0001  -0.3576 0.0579  36  ARG   V CA  
37969 C  C   . ARG   V  35  ? 1.6758 0.5183 1.3622 0.0007  -0.3897 0.0683  36  ARG   V C   
37970 O  O   . ARG   V  35  ? 1.7458 0.4959 1.3295 0.0604  -0.3827 0.1351  36  ARG   V O   
37971 C  CB  . ARG   V  35  ? 1.5970 0.7139 1.4265 0.0081  -0.3380 0.0412  36  ARG   V CB  
37972 C  CG  . ARG   V  35  ? 1.5469 0.7290 1.4403 -0.0427 -0.3209 0.0378  36  ARG   V CG  
37973 C  CD  . ARG   V  35  ? 1.5327 0.8397 1.4842 -0.0674 -0.3336 -0.0001 36  ARG   V CD  
37974 N  NE  . ARG   V  35  ? 1.5150 0.8771 1.4873 -0.1382 -0.3503 -0.0330 36  ARG   V NE  
37975 C  CZ  . ARG   V  35  ? 1.5526 0.9591 1.4988 -0.1511 -0.3673 -0.0135 36  ARG   V CZ  
37976 N  NH1 . ARG   V  35  ? 1.5920 0.9886 1.5524 -0.1306 -0.2936 -0.0161 36  ARG   V NH1 
37977 N  NH2 . ARG   V  35  ? 1.6218 1.0126 1.5192 -0.1372 -0.2960 0.0217  36  ARG   V NH2 
37978 N  N   . ILE   V  36  ? 1.6614 0.5450 1.3894 -0.0602 -0.4094 0.0789  37  ILE   V N   
37979 C  CA  . ILE   V  36  ? 1.6275 0.6677 1.3787 -0.0513 -0.4383 0.0820  37  ILE   V CA  
37980 C  C   . ILE   V  36  ? 1.6480 0.6770 1.2762 -0.0789 -0.4534 0.0577  37  ILE   V C   
37981 O  O   . ILE   V  36  ? 1.6865 0.6175 1.2330 -0.0574 -0.5091 0.0817  37  ILE   V O   
37982 C  CB  . ILE   V  36  ? 1.6496 0.6801 1.4361 -0.0852 -0.4667 0.0995  37  ILE   V CB  
37983 C  CG1 . ILE   V  36  ? 1.6823 0.6551 1.4464 -0.0375 -0.4796 0.1448  37  ILE   V CG1 
37984 C  CG2 . ILE   V  36  ? 1.6722 0.6579 1.4991 -0.0820 -0.4429 0.1272  37  ILE   V CG2 
37985 C  CD1 . ILE   V  36  ? 1.6751 0.7251 1.4543 -0.0330 -0.4910 0.1440  37  ILE   V CD1 
37986 N  N   . SER   V  37  ? 1.6675 0.7137 1.2897 -0.1105 -0.4405 0.0709  38  SER   V N   
37987 C  CA  . SER   V  37  ? 1.6929 0.7237 1.3521 -0.1223 -0.4033 0.0685  38  SER   V CA  
37988 C  C   . SER   V  37  ? 1.6933 0.6869 1.4225 -0.1520 -0.3747 0.0878  38  SER   V C   
37989 O  O   . SER   V  37  ? 1.6805 0.6949 1.4700 -0.1196 -0.3930 0.0992  38  SER   V O   
37990 C  CB  . SER   V  37  ? 1.6881 0.6983 1.3590 -0.1156 -0.3932 0.0685  38  SER   V CB  
37991 O  OG  . SER   V  37  ? 1.7041 0.6845 1.3284 -0.1385 -0.4125 0.1147  38  SER   V OG  
37992 N  N   . PRO   V  38  ? 1.7488 0.6394 1.4668 -0.1484 -0.3375 0.0757  39  PRO   V N   
37993 C  CA  . PRO   V  38  ? 1.7526 0.6557 1.4676 -0.1569 -0.3286 0.0771  39  PRO   V CA  
37994 C  C   . PRO   V  38  ? 1.7166 0.6388 1.4674 -0.1331 -0.3171 0.0811  39  PRO   V C   
37995 O  O   . PRO   V  38  ? 1.7471 0.5344 1.4568 -0.1733 -0.2915 0.0835  39  PRO   V O   
37996 C  CB  . PRO   V  38  ? 1.8100 0.6230 1.4850 -0.1236 -0.3349 0.0878  39  PRO   V CB  
37997 C  CG  . PRO   V  38  ? 1.8035 0.6216 1.4891 -0.1301 -0.3291 0.0812  39  PRO   V CG  
37998 C  CD  . PRO   V  38  ? 1.8079 0.6258 1.4516 -0.1525 -0.3266 0.0699  39  PRO   V CD  
37999 N  N   . LYS   V  39  ? 1.6839 0.7318 1.4375 -0.1281 -0.3065 0.0312  40  LYS   V N   
38000 C  CA  . LYS   V  39  ? 1.6635 0.8381 1.4258 -0.0815 -0.3134 0.0156  40  LYS   V CA  
38001 C  C   . LYS   V  39  ? 1.6382 0.7974 1.3871 -0.0446 -0.3172 0.0115  40  LYS   V C   
38002 O  O   . LYS   V  39  ? 1.6826 0.8121 1.3982 -0.0031 -0.2997 -0.0223 40  LYS   V O   
38003 C  CB  . LYS   V  39  ? 1.6806 0.9424 1.4106 -0.0916 -0.2877 0.0467  40  LYS   V CB  
38004 C  CG  . LYS   V  39  ? 1.6513 1.0869 1.4755 -0.0998 -0.2687 0.0299  40  LYS   V CG  
38005 C  CD  . LYS   V  39  ? 1.6540 1.2151 1.5332 -0.0850 -0.2182 0.0256  40  LYS   V CD  
38006 C  CE  . LYS   V  39  ? 1.6631 1.2746 1.6512 -0.1065 -0.2121 0.0233  40  LYS   V CE  
38007 N  NZ  . LYS   V  39  ? 1.6849 1.2913 1.7100 -0.0996 -0.1766 0.0198  40  LYS   V NZ  
38008 N  N   . ILE   V  40  ? 1.6270 0.7600 1.3469 -0.0157 -0.3482 0.0279  41  ILE   V N   
38009 C  CA  . ILE   V  40  ? 1.6281 0.7772 1.3817 -0.0244 -0.3801 0.0115  41  ILE   V CA  
38010 C  C   . ILE   V  40  ? 1.6028 0.7611 1.4072 -0.0030 -0.3918 0.0028  41  ILE   V C   
38011 O  O   . ILE   V  40  ? 1.5599 0.7547 1.4581 0.0688  -0.4242 -0.0710 41  ILE   V O   
38012 C  CB  . ILE   V  40  ? 1.5948 0.7900 1.3496 -0.0527 -0.4290 0.0533  41  ILE   V CB  
38013 C  CG1 . ILE   V  40  ? 1.6268 0.8134 1.3929 -0.0689 -0.4354 0.0885  41  ILE   V CG1 
38014 C  CG2 . ILE   V  40  ? 1.5833 0.7891 1.3037 -0.0512 -0.4501 0.0765  41  ILE   V CG2 
38015 C  CD1 . ILE   V  40  ? 1.6275 0.7864 1.4351 -0.0667 -0.4217 0.0916  41  ILE   V CD1 
38016 N  N   . TRP   V  41  ? 1.6024 0.7385 1.4695 -0.0391 -0.3504 0.0256  42  TRP   V N   
38017 C  CA  . TRP   V  41  ? 1.6122 0.7911 1.4484 -0.0733 -0.3266 0.0566  42  TRP   V CA  
38018 C  C   . TRP   V  41  ? 1.6023 0.7721 1.4026 -0.0629 -0.2943 0.0532  42  TRP   V C   
38019 O  O   . TRP   V  41  ? 1.6149 0.7260 1.4444 0.0005  -0.3390 0.0176  42  TRP   V O   
38020 C  CB  . TRP   V  41  ? 1.5998 0.7981 1.4689 -0.0921 -0.3267 0.0774  42  TRP   V CB  
38021 C  CG  . TRP   V  41  ? 1.6185 0.7905 1.4843 -0.1055 -0.3366 0.0902  42  TRP   V CG  
38022 C  CD1 . TRP   V  41  ? 1.6084 0.7770 1.5060 -0.1094 -0.3301 0.0778  42  TRP   V CD1 
38023 C  CD2 . TRP   V  41  ? 1.6100 0.7901 1.5045 -0.1178 -0.3436 0.1123  42  TRP   V CD2 
38024 N  NE1 . TRP   V  41  ? 1.6075 0.7684 1.5252 -0.1066 -0.3410 0.0920  42  TRP   V NE1 
38025 C  CE2 . TRP   V  41  ? 1.6260 0.7780 1.5433 -0.1204 -0.3267 0.1226  42  TRP   V CE2 
38026 C  CE3 . TRP   V  41  ? 1.6296 0.8043 1.5095 -0.0989 -0.3398 0.1162  42  TRP   V CE3 
38027 C  CZ2 . TRP   V  41  ? 1.6164 0.7615 1.5577 -0.1336 -0.3338 0.1460  42  TRP   V CZ2 
38028 C  CZ3 . TRP   V  41  ? 1.6238 0.8568 1.5531 -0.1290 -0.3503 0.0982  42  TRP   V CZ3 
38029 C  CH2 . TRP   V  41  ? 1.6206 0.8269 1.5295 -0.1148 -0.3441 0.1567  42  TRP   V CH2 
38030 N  N   . CYS   V  42  ? 1.5959 0.7436 1.3606 -0.1011 -0.2828 0.0064  43  CYS   V N   
38031 C  CA  . CYS   V  42  ? 1.6311 0.7286 1.3280 -0.1183 -0.2532 0.0047  43  CYS   V CA  
38032 C  C   . CYS   V  42  ? 1.5939 0.6869 1.2944 -0.1420 -0.2576 -0.0261 43  CYS   V C   
38033 O  O   . CYS   V  42  ? 1.6168 0.5243 1.3657 -0.2435 -0.2765 -0.0607 43  CYS   V O   
38034 C  CB  . CYS   V  42  ? 1.6397 0.7794 1.4040 -0.1105 -0.2302 0.0078  43  CYS   V CB  
38035 S  SG  . CYS   V  42  ? 1.7027 1.0105 1.5035 -0.1101 -0.1071 0.0963  43  CYS   V SG  
38036 N  N   . ALA   V  43  ? 1.6065 0.6562 1.2891 -0.0980 -0.2550 -0.0062 44  ALA   V N   
38037 C  CA  . ALA   V  43  ? 1.5840 0.6562 1.3070 -0.0861 -0.2578 -0.0077 44  ALA   V CA  
38038 C  C   . ALA   V  43  ? 1.5766 0.6235 1.2649 -0.0729 -0.2657 0.0126  44  ALA   V C   
38039 O  O   . ALA   V  43  ? 1.5575 0.6845 1.2965 -0.1100 -0.2679 0.0353  44  ALA   V O   
38040 C  CB  . ALA   V  43  ? 1.6115 0.5495 1.3690 -0.0591 -0.2696 0.0007  44  ALA   V CB  
38041 N  N   . GLY   V  44  ? 1.5336 0.5858 1.2799 -0.0481 -0.2707 0.0298  45  GLY   V N   
38042 C  CA  . GLY   V  44  ? 1.4946 0.6208 1.2931 -0.0107 -0.2841 0.0356  45  GLY   V CA  
38043 C  C   . GLY   V  44  ? 1.4309 0.6497 1.2806 0.0274  -0.3037 0.0512  45  GLY   V C   
38044 O  O   . GLY   V  44  ? 1.4605 0.7439 1.2215 0.0763  -0.2990 0.0364  45  GLY   V O   
38045 N  N   . ALA   V  45  ? 1.4102 0.5754 1.2882 0.0555  -0.2960 0.0869  46  ALA   V N   
38046 C  CA  . ALA   V  45  ? 1.4151 0.5189 1.2756 0.1223  -0.3306 0.0579  46  ALA   V CA  
38047 C  C   . ALA   V  45  ? 1.4576 0.5414 1.2546 0.0914  -0.3195 0.0505  46  ALA   V C   
38048 O  O   . ALA   V  45  ? 1.4591 0.6943 1.2754 0.1652  -0.3514 0.0867  46  ALA   V O   
38049 C  CB  . ALA   V  45  ? 1.3862 0.4495 1.2649 0.1254  -0.3195 0.0933  46  ALA   V CB  
38050 N  N   . GLY   V  46  ? 1.4752 0.4949 1.2527 0.0772  -0.3229 0.0101  47  GLY   V N   
38051 C  CA  . GLY   V  46  ? 1.4768 0.5488 1.2999 0.0656  -0.3076 0.0115  47  GLY   V CA  
38052 C  C   . GLY   V  46  ? 1.4991 0.5897 1.2974 0.0605  -0.3212 0.0335  47  GLY   V C   
38053 O  O   . GLY   V  46  ? 1.5115 0.5984 1.3426 0.1396  -0.3324 0.0698  47  GLY   V O   
38054 N  N   . THR   V  47  ? 1.4932 0.6291 1.3085 0.0264  -0.2843 0.0772  48  THR   V N   
38055 C  CA  . THR   V  47  ? 1.5528 0.6151 1.2998 0.0140  -0.2982 0.1057  48  THR   V CA  
38056 C  C   . THR   V  47  ? 1.5788 0.5205 1.3648 0.0524  -0.3256 0.0810  48  THR   V C   
38057 O  O   . THR   V  47  ? 1.6311 0.5495 1.3115 0.0884  -0.3486 0.0669  48  THR   V O   
38058 C  CB  . THR   V  47  ? 1.5709 0.6230 1.3210 0.0158  -0.2776 0.1221  48  THR   V CB  
38059 O  OG1 . THR   V  47  ? 1.5961 0.7412 1.2227 -0.0329 -0.3503 0.0826  48  THR   V OG1 
38060 C  CG2 . THR   V  47  ? 1.6156 0.5925 1.3306 0.0040  -0.2627 0.1009  48  THR   V CG2 
38061 N  N   . ALA   V  48  ? 1.5752 0.4414 1.4488 0.0835  -0.3432 0.0796  49  ALA   V N   
38062 C  CA  . ALA   V  48  ? 1.5268 0.5206 1.4429 0.0876  -0.3489 0.0975  49  ALA   V CA  
38063 C  C   . ALA   V  48  ? 1.5291 0.5489 1.4247 0.0916  -0.3149 0.0831  49  ALA   V C   
38064 O  O   . ALA   V  48  ? 1.5611 0.4669 1.4752 0.1514  -0.3190 0.0871  49  ALA   V O   
38065 C  CB  . ALA   V  48  ? 1.5548 0.3994 1.4421 0.1174  -0.3301 0.0993  49  ALA   V CB  
38066 N  N   . ALA   V  49  ? 1.5196 0.7065 1.4121 0.0988  -0.3301 0.0100  50  ALA   V N   
38067 C  CA  . ALA   V  49  ? 1.5776 0.6177 1.3977 0.0380  -0.3525 0.0409  50  ALA   V CA  
38068 C  C   . ALA   V  49  ? 1.5937 0.6295 1.4006 0.0412  -0.3684 0.0435  50  ALA   V C   
38069 O  O   . ALA   V  49  ? 1.6171 0.6287 1.5148 0.0974  -0.4381 0.0647  50  ALA   V O   
38070 C  CB  . ALA   V  49  ? 1.6198 0.7731 1.4109 0.0177  -0.3205 0.0099  50  ALA   V CB  
38071 N  N   . ASP   V  50  ? 1.5937 0.4486 1.3464 0.0744  -0.3435 0.0772  51  ASP   V N   
38072 C  CA  . ASP   V  50  ? 1.5875 0.4220 1.3167 0.0846  -0.3381 0.0433  51  ASP   V CA  
38073 C  C   . ASP   V  50  ? 1.6033 0.5044 1.2770 0.1126  -0.3331 0.0390  51  ASP   V C   
38074 O  O   . ASP   V  50  ? 1.5876 0.5673 1.2386 0.1689  -0.2965 0.0837  51  ASP   V O   
38075 C  CB  . ASP   V  50  ? 1.5829 0.4547 1.2945 0.0806  -0.3470 0.0357  51  ASP   V CB  
38076 C  CG  . ASP   V  50  ? 1.5932 0.4846 1.2726 0.0469  -0.3605 0.0133  51  ASP   V CG  
38077 O  OD1 . ASP   V  50  ? 1.6907 0.4511 1.2534 0.0855  -0.3561 0.0500  51  ASP   V OD1 
38078 O  OD2 . ASP   V  50  ? 1.5868 0.6055 1.3134 -0.0637 -0.4069 -0.0672 51  ASP   V OD2 
38079 N  N   . THR   V  51  ? 1.6048 0.5128 1.2916 0.1360  -0.3399 0.0637  52  THR   V N   
38080 C  CA  . THR   V  51  ? 1.6227 0.5502 1.3054 0.0952  -0.3769 0.1174  52  THR   V CA  
38081 C  C   . THR   V  51  ? 1.5962 0.6205 1.3969 0.0516  -0.3907 0.1011  52  THR   V C   
38082 O  O   . THR   V  51  ? 1.5744 0.7135 1.4006 0.0107  -0.4332 0.1520  52  THR   V O   
38083 C  CB  . THR   V  51  ? 1.6436 0.5739 1.3023 0.1273  -0.3673 0.1455  52  THR   V CB  
38084 O  OG1 . THR   V  51  ? 1.6566 0.6677 1.3280 0.1025  -0.4219 0.0881  52  THR   V OG1 
38085 C  CG2 . THR   V  51  ? 1.6450 0.5473 1.3077 0.1369  -0.3367 0.1370  52  THR   V CG2 
38086 N  N   . GLU   V  52  ? 1.5581 0.6217 1.4233 0.0036  -0.3965 0.1704  53  GLU   V N   
38087 C  CA  . GLU   V  52  ? 1.5330 0.6843 1.4914 -0.0162 -0.4009 0.1306  53  GLU   V CA  
38088 C  C   . GLU   V  52  ? 1.5004 0.6667 1.4110 -0.0638 -0.3949 0.0364  53  GLU   V C   
38089 O  O   . GLU   V  52  ? 1.5218 0.5995 1.4458 -0.0125 -0.4549 0.0132  53  GLU   V O   
38090 C  CB  . GLU   V  52  ? 1.5931 0.8162 1.5448 -0.0287 -0.4231 0.2310  53  GLU   V CB  
38091 C  CG  . GLU   V  52  ? 1.7409 0.8229 1.6683 -0.0473 -0.4501 0.1790  53  GLU   V CG  
38092 C  CD  . GLU   V  52  ? 1.8086 0.8898 1.7929 -0.0997 -0.3774 0.1880  53  GLU   V CD  
38093 O  OE1 . GLU   V  52  ? 1.8820 1.2683 1.8980 0.1670  -0.2834 0.1024  53  GLU   V OE1 
38094 O  OE2 . GLU   V  52  ? 1.7951 0.9626 1.7985 -0.1921 -0.3384 0.1590  53  GLU   V OE2 
38095 N  N   . ALA   V  53  ? 1.4863 0.5356 1.3281 -0.0338 -0.4042 -0.0015 54  ALA   V N   
38096 C  CA  . ALA   V  53  ? 1.4467 0.5672 1.3107 -0.0071 -0.4121 0.0357  54  ALA   V CA  
38097 C  C   . ALA   V  53  ? 1.4432 0.5733 1.3547 0.0433  -0.3786 0.0717  54  ALA   V C   
38098 O  O   . ALA   V  53  ? 1.4682 0.5728 1.4184 0.0802  -0.3356 0.1190  54  ALA   V O   
38099 C  CB  . ALA   V  53  ? 1.4092 0.4848 1.2613 -0.0077 -0.4452 -0.0006 54  ALA   V CB  
38100 N  N   . VAL   V  54  ? 1.4237 0.5050 1.3405 0.0702  -0.3731 0.0950  55  VAL   V N   
38101 C  CA  . VAL   V  54  ? 1.4447 0.5040 1.3773 0.1089  -0.3753 0.1236  55  VAL   V CA  
38102 C  C   . VAL   V  54  ? 1.4473 0.5701 1.4083 0.0627  -0.3795 0.1169  55  VAL   V C   
38103 O  O   . VAL   V  54  ? 1.4704 0.5855 1.4130 0.0460  -0.4084 0.1344  55  VAL   V O   
38104 C  CB  . VAL   V  54  ? 1.4298 0.4663 1.3394 0.1453  -0.3808 0.1421  55  VAL   V CB  
38105 C  CG1 . VAL   V  54  ? 1.4214 0.5034 1.3311 0.1498  -0.3758 0.1343  55  VAL   V CG1 
38106 C  CG2 . VAL   V  54  ? 1.4474 0.4969 1.3473 0.1567  -0.3863 0.1459  55  VAL   V CG2 
38107 N  N   . THR   V  55  ? 1.4699 0.5432 1.4712 0.0601  -0.3277 0.1091  56  THR   V N   
38108 C  CA  . THR   V  55  ? 1.5476 0.6406 1.5169 0.0110  -0.2890 0.1224  56  THR   V CA  
38109 C  C   . THR   V  55  ? 1.5959 0.6245 1.5125 0.0562  -0.3257 0.1263  56  THR   V C   
38110 O  O   . THR   V  55  ? 1.6272 0.5737 1.5818 0.0384  -0.3467 0.1234  56  THR   V O   
38111 C  CB  . THR   V  55  ? 1.5562 0.6398 1.5759 0.0034  -0.2478 0.1105  56  THR   V CB  
38112 O  OG1 . THR   V  55  ? 1.5372 0.5868 1.5762 -0.1019 -0.2607 0.1592  56  THR   V OG1 
38113 C  CG2 . THR   V  55  ? 1.5529 0.7855 1.6228 -0.0244 -0.2172 0.0979  56  THR   V CG2 
38114 N  N   . GLN   V  56  ? 1.6521 0.6747 1.5159 0.0238  -0.3480 0.0925  57  GLN   V N   
38115 C  CA  . GLN   V  56  ? 1.6802 0.6815 1.4982 0.0150  -0.3789 0.0988  57  GLN   V CA  
38116 C  C   . GLN   V  56  ? 1.6303 0.6149 1.4128 -0.0432 -0.3749 0.1045  57  GLN   V C   
38117 O  O   . GLN   V  56  ? 1.7381 0.6006 1.4754 0.0187  -0.3730 0.1825  57  GLN   V O   
38118 C  CB  . GLN   V  56  ? 1.7285 0.7920 1.5245 0.0625  -0.4304 0.1066  57  GLN   V CB  
38119 C  CG  . GLN   V  56  ? 1.7590 0.8637 1.6237 0.1100  -0.4345 0.1068  57  GLN   V CG  
38120 C  CD  . GLN   V  56  ? 1.8558 1.0339 1.6650 0.1844  -0.4920 0.1347  57  GLN   V CD  
38121 O  OE1 . GLN   V  56  ? 1.8995 1.1100 1.7599 0.2591  -0.4902 0.1003  57  GLN   V OE1 
38122 N  NE2 . GLN   V  56  ? 1.8581 1.1649 1.7363 0.3200  -0.4880 0.1666  57  GLN   V NE2 
38123 N  N   . LEU   V  57  ? 1.6412 0.5275 1.2963 -0.0691 -0.3829 0.0619  58  LEU   V N   
38124 C  CA  . LEU   V  57  ? 1.6280 0.4685 1.2809 -0.0938 -0.3743 0.0554  58  LEU   V CA  
38125 C  C   . LEU   V  57  ? 1.6208 0.5194 1.2685 -0.1039 -0.3594 0.0545  58  LEU   V C   
38126 O  O   . LEU   V  57  ? 1.6286 0.5417 1.3704 -0.0530 -0.3217 0.1156  58  LEU   V O   
38127 C  CB  . LEU   V  57  ? 1.6159 0.4409 1.2183 -0.0825 -0.3856 0.0469  58  LEU   V CB  
38128 C  CG  . LEU   V  57  ? 1.6372 0.4155 1.2228 -0.0720 -0.3845 0.0551  58  LEU   V CG  
38129 C  CD1 . LEU   V  57  ? 1.6523 0.4608 1.2019 -0.0662 -0.3783 0.0458  58  LEU   V CD1 
38130 C  CD2 . LEU   V  57  ? 1.6162 0.4311 1.2200 -0.0559 -0.3822 0.0772  58  LEU   V CD2 
38131 N  N   . ILE   V  58  ? 1.5998 0.4792 1.2392 -0.1024 -0.3511 0.0878  59  ILE   V N   
38132 C  CA  . ILE   V  58  ? 1.6299 0.4813 1.2422 -0.0816 -0.3379 0.0989  59  ILE   V CA  
38133 C  C   . ILE   V  58  ? 1.5795 0.5215 1.2612 -0.0594 -0.3501 0.0664  59  ILE   V C   
38134 O  O   . ILE   V  58  ? 1.7218 0.5471 1.3131 -0.0676 -0.2967 0.1045  59  ILE   V O   
38135 C  CB  . ILE   V  58  ? 1.5871 0.5128 1.1909 -0.0855 -0.3250 0.1066  59  ILE   V CB  
38136 C  CG1 . ILE   V  58  ? 1.5716 0.5854 1.1618 -0.0683 -0.3474 0.0983  59  ILE   V CG1 
38137 C  CG2 . ILE   V  58  ? 1.6074 0.4956 1.1945 -0.0973 -0.3040 0.0851  59  ILE   V CG2 
38138 C  CD1 . ILE   V  58  ? 1.5439 0.6504 1.1450 -0.0483 -0.3632 0.0986  59  ILE   V CD1 
38139 N  N   . GLY   V  59  ? 1.5871 0.4723 1.2717 -0.0280 -0.3330 0.0656  60  GLY   V N   
38140 C  CA  . GLY   V  59  ? 1.5664 0.5164 1.3193 -0.0137 -0.2990 0.0905  60  GLY   V CA  
38141 C  C   . GLY   V  59  ? 1.5817 0.5050 1.3504 -0.0093 -0.2741 0.1006  60  GLY   V C   
38142 O  O   . GLY   V  59  ? 1.5526 0.4601 1.3294 0.0184  -0.2930 0.0882  60  GLY   V O   
38143 N  N   . SER   V  60  ? 1.6278 0.4940 1.3816 0.0095  -0.2448 0.0344  61  SER   V N   
38144 C  CA  . SER   V  60  ? 1.6671 0.4140 1.4573 -0.0227 -0.2711 0.0524  61  SER   V CA  
38145 C  C   . SER   V  60  ? 1.6429 0.4552 1.4517 -0.0091 -0.3058 0.0060  61  SER   V C   
38146 O  O   . SER   V  60  ? 1.6595 0.5087 1.5422 -0.0547 -0.3061 0.0615  61  SER   V O   
38147 C  CB  . SER   V  60  ? 1.6913 0.3891 1.4233 0.0086  -0.2723 -0.0063 61  SER   V CB  
38148 O  OG  . SER   V  60  ? 1.7224 0.3849 1.4073 -0.0015 -0.2669 -0.0063 61  SER   V OG  
38149 N  N   . ASN   V  61  ? 1.6645 0.3450 1.4156 -0.0200 -0.2950 -0.0027 62  ASN   V N   
38150 C  CA  . ASN   V  61  ? 1.6432 0.3740 1.4201 -0.0265 -0.2921 0.0013  62  ASN   V CA  
38151 C  C   . ASN   V  61  ? 1.6742 0.3431 1.4176 -0.0339 -0.2867 0.0019  62  ASN   V C   
38152 O  O   . ASN   V  61  ? 1.6535 0.3217 1.3140 -0.1008 -0.3062 0.0015  62  ASN   V O   
38153 C  CB  . ASN   V  61  ? 1.6198 0.4344 1.4455 -0.0269 -0.2944 0.0241  62  ASN   V CB  
38154 C  CG  . ASN   V  61  ? 1.6054 0.5173 1.4345 0.0037  -0.3100 0.0283  62  ASN   V CG  
38155 O  OD1 . ASN   V  61  ? 1.5994 0.5166 1.4374 -0.0605 -0.3174 0.0248  62  ASN   V OD1 
38156 N  ND2 . ASN   V  61  ? 1.5348 0.5961 1.4460 0.0013  -0.3153 0.1201  62  ASN   V ND2 
38157 N  N   . ILE   V  62  ? 1.6964 0.3643 1.4135 -0.0039 -0.2488 0.0626  63  ILE   V N   
38158 C  CA  . ILE   V  62  ? 1.7176 0.3539 1.4119 0.0118  -0.2680 0.1211  63  ILE   V CA  
38159 C  C   . ILE   V  62  ? 1.7333 0.3624 1.4305 -0.0043 -0.2638 0.1213  63  ILE   V C   
38160 O  O   . ILE   V  62  ? 1.7493 0.4324 1.3852 -0.0069 -0.2538 0.1291  63  ILE   V O   
38161 C  CB  . ILE   V  62  ? 1.7311 0.3576 1.4049 0.0379  -0.2690 0.1425  63  ILE   V CB  
38162 C  CG1 . ILE   V  62  ? 1.7092 0.3452 1.3606 0.0676  -0.2869 0.1603  63  ILE   V CG1 
38163 C  CG2 . ILE   V  62  ? 1.7440 0.3266 1.4227 0.0135  -0.2715 0.1667  63  ILE   V CG2 
38164 C  CD1 . ILE   V  62  ? 1.7098 0.3466 1.3619 0.0622  -0.2904 0.1618  63  ILE   V CD1 
38165 N  N   . GLU   V  63  ? 1.7167 0.3786 1.4542 -0.0259 -0.2784 0.1540  64  GLU   V N   
38166 C  CA  . GLU   V  63  ? 1.7183 0.4273 1.5289 -0.0521 -0.3069 0.1636  64  GLU   V CA  
38167 C  C   . GLU   V  63  ? 1.7296 0.3858 1.5331 -0.0911 -0.3281 0.1229  64  GLU   V C   
38168 O  O   . GLU   V  63  ? 1.8443 0.2873 1.5956 -0.0750 -0.3654 0.1105  64  GLU   V O   
38169 C  CB  . GLU   V  63  ? 1.7406 0.4851 1.5625 -0.0400 -0.3180 0.2106  64  GLU   V CB  
38170 C  CG  . GLU   V  63  ? 1.7829 0.5246 1.6840 -0.0671 -0.3055 0.1600  64  GLU   V CG  
38171 C  CD  . GLU   V  63  ? 1.8084 0.6293 1.7204 -0.0526 -0.3186 0.1918  64  GLU   V CD  
38172 O  OE1 . GLU   V  63  ? 1.8238 0.8535 1.6792 -0.0121 -0.3729 0.0884  64  GLU   V OE1 
38173 O  OE2 . GLU   V  63  ? 1.8207 0.6322 1.8257 -0.0545 -0.2858 0.2207  64  GLU   V OE2 
38174 N  N   . LEU   V  64  ? 1.7216 0.3587 1.4933 -0.1074 -0.3396 0.1076  65  LEU   V N   
38175 C  CA  . LEU   V  64  ? 1.7176 0.3799 1.4900 -0.0915 -0.3250 0.1213  65  LEU   V CA  
38176 C  C   . LEU   V  64  ? 1.7116 0.4501 1.4744 -0.1041 -0.3273 0.1049  65  LEU   V C   
38177 O  O   . LEU   V  64  ? 1.7700 0.5227 1.4943 -0.0480 -0.2905 0.2774  65  LEU   V O   
38178 C  CB  . LEU   V  64  ? 1.7221 0.3647 1.4274 -0.0662 -0.3457 0.1472  65  LEU   V CB  
38179 C  CG  . LEU   V  64  ? 1.7241 0.4111 1.4401 -0.0392 -0.3497 0.1761  65  LEU   V CG  
38180 C  CD1 . LEU   V  64  ? 1.7115 0.4537 1.4176 -0.0302 -0.3590 0.1663  65  LEU   V CD1 
38181 C  CD2 . LEU   V  64  ? 1.7238 0.4002 1.4494 -0.0486 -0.3579 0.2031  65  LEU   V CD2 
38182 N  N   . HIS   V  65  ? 1.6982 0.4249 1.4518 -0.0654 -0.3410 0.1120  66  HIS   V N   
38183 C  CA  . HIS   V  65  ? 1.7125 0.3936 1.4636 -0.0596 -0.3563 0.1279  66  HIS   V CA  
38184 C  C   . HIS   V  65  ? 1.7396 0.3129 1.4497 -0.1052 -0.3791 0.0997  66  HIS   V C   
38185 O  O   . HIS   V  65  ? 1.8253 0.2348 1.4709 -0.0890 -0.4159 0.0353  66  HIS   V O   
38186 C  CB  . HIS   V  65  ? 1.6484 0.3859 1.4685 -0.0234 -0.4000 0.1361  66  HIS   V CB  
38187 C  CG  . HIS   V  65  ? 1.5905 0.4562 1.5436 0.0663  -0.4182 0.1888  66  HIS   V CG  
38188 N  ND1 . HIS   V  65  ? 1.5919 0.4622 1.5467 0.0980  -0.4229 0.1911  66  HIS   V ND1 
38189 C  CD2 . HIS   V  65  ? 1.6156 0.4744 1.5654 0.1188  -0.4318 0.2141  66  HIS   V CD2 
38190 C  CE1 . HIS   V  65  ? 1.5795 0.4708 1.5701 0.1333  -0.4156 0.2057  66  HIS   V CE1 
38191 N  NE2 . HIS   V  65  ? 1.5681 0.4779 1.5724 0.1528  -0.4343 0.2034  66  HIS   V NE2 
38192 N  N   . SER   V  66  ? 1.7091 0.3237 1.4263 -0.1322 -0.3447 0.1014  67  SER   V N   
38193 C  CA  . SER   V  66  ? 1.7262 0.4303 1.4401 -0.1261 -0.3059 0.1167  67  SER   V CA  
38194 C  C   . SER   V  66  ? 1.7325 0.4335 1.4256 -0.1226 -0.3292 0.1172  67  SER   V C   
38195 O  O   . SER   V  66  ? 1.7436 0.4081 1.4281 -0.1533 -0.2888 0.0946  67  SER   V O   
38196 C  CB  . SER   V  66  ? 1.6912 0.4524 1.4711 -0.1317 -0.2526 0.1146  67  SER   V CB  
38197 O  OG  . SER   V  66  ? 1.6943 0.5793 1.5589 -0.1146 -0.2001 0.1100  67  SER   V OG  
38198 N  N   . LEU   V  67  ? 1.7311 0.4316 1.4317 -0.1333 -0.3968 0.1205  68  LEU   V N   
38199 C  CA  . LEU   V  67  ? 1.7304 0.4272 1.4760 -0.1495 -0.4433 0.1260  68  LEU   V CA  
38200 C  C   . LEU   V  67  ? 1.7355 0.3960 1.4951 -0.1654 -0.4783 0.1106  68  LEU   V C   
38201 O  O   . LEU   V  67  ? 1.7674 0.3358 1.4985 -0.0518 -0.5412 0.1281  68  LEU   V O   
38202 C  CB  . LEU   V  67  ? 1.7532 0.4406 1.4725 -0.1507 -0.4487 0.0948  68  LEU   V CB  
38203 C  CG  . LEU   V  67  ? 1.7415 0.5261 1.4904 -0.1322 -0.4364 0.0841  68  LEU   V CG  
38204 C  CD1 . LEU   V  67  ? 1.7274 0.5610 1.4761 -0.1438 -0.4142 0.1004  68  LEU   V CD1 
38205 C  CD2 . LEU   V  67  ? 1.7377 0.5886 1.4673 -0.1341 -0.4516 0.0691  68  LEU   V CD2 
38206 N  N   . TYR   V  68  ? 1.7331 0.3868 1.5103 -0.1644 -0.4777 0.1151  69  TYR   V N   
38207 C  CA  . TYR   V  68  ? 1.7865 0.3015 1.4993 -0.1515 -0.4762 0.1250  69  TYR   V CA  
38208 C  C   . TYR   V  68  ? 1.7587 0.3470 1.5050 -0.1676 -0.4505 0.1456  69  TYR   V C   
38209 O  O   . TYR   V  68  ? 1.7847 0.4108 1.4872 -0.0426 -0.5070 0.1063  69  TYR   V O   
38210 C  CB  . TYR   V  68  ? 1.7662 0.2780 1.4763 -0.1264 -0.5019 0.1076  69  TYR   V CB  
38211 C  CG  . TYR   V  68  ? 1.8630 0.1767 1.4448 -0.1212 -0.5618 0.1138  69  TYR   V CG  
38212 C  CD1 . TYR   V  68  ? 1.8698 0.1703 1.4552 -0.1071 -0.5696 0.1209  69  TYR   V CD1 
38213 C  CD2 . TYR   V  68  ? 1.8794 0.1794 1.4458 -0.1130 -0.5872 0.1118  69  TYR   V CD2 
38214 C  CE1 . TYR   V  68  ? 1.8584 0.1714 1.4632 -0.1317 -0.6163 0.1372  69  TYR   V CE1 
38215 C  CE2 . TYR   V  68  ? 1.8648 0.1813 1.4434 -0.1318 -0.6208 0.1301  69  TYR   V CE2 
38216 C  CZ  . TYR   V  68  ? 1.8767 0.1795 1.4413 -0.1585 -0.6259 0.1416  69  TYR   V CZ  
38217 O  OH  . TYR   V  68  ? 1.8403 0.1904 1.4934 -0.1944 -0.7044 0.1803  69  TYR   V OH  
38218 N  N   . THR   V  69  ? 1.6945 0.4337 1.4660 -0.1559 -0.3967 0.1493  70  THR   V N   
38219 C  CA  . THR   V  69  ? 1.6767 0.5063 1.4647 -0.1168 -0.3611 0.1580  70  THR   V CA  
38220 C  C   . THR   V  69  ? 1.7010 0.5331 1.4789 -0.0966 -0.3192 0.1756  70  THR   V C   
38221 O  O   . THR   V  69  ? 1.7406 0.5589 1.4921 -0.0249 -0.2746 0.2088  70  THR   V O   
38222 C  CB  . THR   V  69  ? 1.6295 0.5506 1.4257 -0.0706 -0.3664 0.1083  70  THR   V CB  
38223 O  OG1 . THR   V  69  ? 1.5629 0.6010 1.4105 -0.0753 -0.3440 0.1019  70  THR   V OG1 
38224 C  CG2 . THR   V  69  ? 1.6146 0.5869 1.4101 -0.0503 -0.3701 0.0943  70  THR   V CG2 
38225 N  N   . SER   V  70  ? 1.7088 0.5479 1.4908 -0.1297 -0.3216 0.1666  71  SER   V N   
38226 C  CA  . SER   V  70  ? 1.7412 0.5264 1.5177 -0.1898 -0.3282 0.1865  71  SER   V CA  
38227 C  C   . SER   V  70  ? 1.7427 0.5459 1.4986 -0.1926 -0.3351 0.1933  71  SER   V C   
38228 O  O   . SER   V  70  ? 1.7156 0.3931 1.5371 -0.2601 -0.3734 0.1816  71  SER   V O   
38229 C  CB  . SER   V  70  ? 1.7593 0.5224 1.5141 -0.2320 -0.2984 0.1771  71  SER   V CB  
38230 O  OG  . SER   V  70  ? 1.8129 0.5553 1.4987 -0.2587 -0.2829 0.1686  71  SER   V OG  
38231 N  N   . ARG   V  71  ? 1.7754 0.5444 1.5465 -0.1847 -0.3565 0.2076  72  ARG   V N   
38232 C  CA  . ARG   V  71  ? 1.8037 0.5974 1.5518 -0.1948 -0.3564 0.1786  72  ARG   V CA  
38233 C  C   . ARG   V  71  ? 1.8243 0.6246 1.5645 -0.1162 -0.3346 0.1392  72  ARG   V C   
38234 O  O   . ARG   V  71  ? 1.8617 0.7179 1.5604 -0.0447 -0.3303 0.1613  72  ARG   V O   
38235 C  CB  . ARG   V  71  ? 1.8370 0.5639 1.5463 -0.2007 -0.3859 0.1902  72  ARG   V CB  
38236 C  CG  . ARG   V  71  ? 1.8672 0.5298 1.5838 -0.2197 -0.3819 0.2069  72  ARG   V CG  
38237 C  CD  . ARG   V  71  ? 1.8675 0.5286 1.5830 -0.1763 -0.3977 0.2316  72  ARG   V CD  
38238 N  NE  . ARG   V  71  ? 1.9026 0.4931 1.6449 -0.1221 -0.3899 0.2534  72  ARG   V NE  
38239 C  CZ  . ARG   V  71  ? 1.9013 0.5206 1.6245 -0.0551 -0.4338 0.2744  72  ARG   V CZ  
38240 N  NH1 . ARG   V  71  ? 1.8656 0.5167 1.6189 -0.0489 -0.5018 0.2628  72  ARG   V NH1 
38241 N  NH2 . ARG   V  71  ? 1.9545 0.6314 1.6146 -0.0620 -0.3904 0.3118  72  ARG   V NH2 
38242 N  N   . GLU   V  72  ? 1.8744 0.7139 1.5616 -0.1445 -0.2695 0.1133  73  GLU   V N   
38243 C  CA  . GLU   V  72  ? 1.8546 0.6773 1.5279 -0.2059 -0.2433 0.1392  73  GLU   V CA  
38244 C  C   . GLU   V  72  ? 1.9210 0.5057 1.5009 -0.1923 -0.2368 0.1054  73  GLU   V C   
38245 O  O   . GLU   V  72  ? 1.8450 0.2771 1.4978 -0.3758 -0.2119 0.1362  73  GLU   V O   
38246 C  CB  . GLU   V  72  ? 1.9530 0.8371 1.5408 -0.0780 -0.2069 0.1877  73  GLU   V CB  
38247 C  CG  . GLU   V  72  ? 1.9731 0.9421 1.5920 -0.1048 -0.1976 0.2021  73  GLU   V CG  
38248 C  CD  . GLU   V  72  ? 2.0740 1.0504 1.6061 0.0126  -0.1750 0.2094  73  GLU   V CD  
38249 O  OE1 . GLU   V  72  ? 2.1924 1.0935 1.6307 0.0513  -0.1497 0.1825  73  GLU   V OE1 
38250 O  OE2 . GLU   V  72  ? 2.1629 1.2016 1.5486 -0.0139 -0.1609 0.1664  73  GLU   V OE2 
38251 N  N   . PRO   V  73  ? 1.8424 0.4657 1.4641 -0.1893 -0.2301 0.0614  74  PRO   V N   
38252 C  CA  . PRO   V  73  ? 1.8154 0.5258 1.4744 -0.1902 -0.2331 0.0634  74  PRO   V CA  
38253 C  C   . PRO   V  73  ? 1.8430 0.5036 1.4108 -0.2164 -0.2705 0.1110  74  PRO   V C   
38254 O  O   . PRO   V  73  ? 1.8541 0.5320 1.4047 -0.2708 -0.2200 0.1655  74  PRO   V O   
38255 C  CB  . PRO   V  73  ? 1.8016 0.5800 1.4205 -0.1909 -0.2314 0.0143  74  PRO   V CB  
38256 C  CG  . PRO   V  73  ? 1.8005 0.5981 1.4386 -0.2160 -0.2255 -0.0039 74  PRO   V CG  
38257 C  CD  . PRO   V  73  ? 1.8106 0.5579 1.4729 -0.1848 -0.2370 -0.0045 74  PRO   V CD  
38258 N  N   . ARG   V  74  ? 1.8240 0.5000 1.3845 -0.1755 -0.3006 0.1324  75  ARG   V N   
38259 C  CA  . ARG   V  74  ? 1.8386 0.5871 1.3854 -0.1276 -0.2974 0.0847  75  ARG   V CA  
38260 C  C   . ARG   V  74  ? 1.8400 0.5533 1.3947 -0.0847 -0.2852 0.0635  75  ARG   V C   
38261 O  O   . ARG   V  74  ? 1.8781 0.5336 1.4027 -0.0619 -0.2641 0.0529  75  ARG   V O   
38262 C  CB  . ARG   V  74  ? 1.8542 0.5361 1.3838 -0.1201 -0.2962 0.0788  75  ARG   V CB  
38263 C  CG  . ARG   V  74  ? 1.8537 0.4885 1.4227 -0.1064 -0.3017 0.0449  75  ARG   V CG  
38264 C  CD  . ARG   V  74  ? 1.8589 0.5212 1.4099 -0.0995 -0.2995 0.0470  75  ARG   V CD  
38265 N  NE  . ARG   V  74  ? 1.8677 0.5670 1.4051 -0.0805 -0.3032 0.1045  75  ARG   V NE  
38266 C  CZ  . ARG   V  74  ? 1.8653 0.4873 1.4728 -0.0509 -0.3031 0.1256  75  ARG   V CZ  
38267 N  NH1 . ARG   V  74  ? 1.8623 0.5193 1.4992 -0.0526 -0.3202 0.1351  75  ARG   V NH1 
38268 N  NH2 . ARG   V  74  ? 1.8872 0.4616 1.5304 -0.0445 -0.2807 0.1059  75  ARG   V NH2 
38269 N  N   . VAL   V  75  ? 1.8168 0.5799 1.3955 -0.0880 -0.2520 0.0526  76  VAL   V N   
38270 C  CA  . VAL   V  75  ? 1.7531 0.5830 1.3627 -0.1208 -0.2346 0.0348  76  VAL   V CA  
38271 C  C   . VAL   V  75  ? 1.7378 0.4941 1.3435 -0.0824 -0.2254 0.0307  76  VAL   V C   
38272 O  O   . VAL   V  75  ? 1.7084 0.5150 1.3533 -0.0892 -0.1884 0.0115  76  VAL   V O   
38273 C  CB  . VAL   V  75  ? 1.7229 0.6891 1.3186 -0.1378 -0.2071 0.0180  76  VAL   V CB  
38274 C  CG1 . VAL   V  75  ? 1.7029 0.7143 1.2954 -0.1473 -0.2071 0.0450  76  VAL   V CG1 
38275 C  CG2 . VAL   V  75  ? 1.7244 0.7277 1.3076 -0.1474 -0.2103 0.0234  76  VAL   V CG2 
38276 N  N   . VAL   V  76  ? 1.7820 0.4171 1.3218 -0.0560 -0.1963 0.0541  77  VAL   V N   
38277 C  CA  . VAL   V  76  ? 1.7916 0.4821 1.2739 -0.0374 -0.2094 0.0924  77  VAL   V CA  
38278 C  C   . VAL   V  76  ? 1.8098 0.5383 1.2838 -0.0244 -0.1899 0.1038  77  VAL   V C   
38279 O  O   . VAL   V  76  ? 1.8034 0.5481 1.3857 -0.0060 -0.1546 0.0714  77  VAL   V O   
38280 C  CB  . VAL   V  76  ? 1.8854 0.5093 1.2445 -0.0349 -0.1942 0.0980  77  VAL   V CB  
38281 C  CG1 . VAL   V  76  ? 1.9232 0.4966 1.2255 0.0031  -0.1594 0.1544  77  VAL   V CG1 
38282 C  CG2 . VAL   V  76  ? 1.8675 0.5115 1.2395 -0.0826 -0.1973 0.0305  77  VAL   V CG2 
38283 N  N   . SER   V  77  ? 1.7309 0.6008 1.2640 -0.0886 -0.2180 0.1429  78  SER   V N   
38284 C  CA  . SER   V  77  ? 1.6888 0.6889 1.2485 -0.0871 -0.2410 0.1222  78  SER   V CA  
38285 C  C   . SER   V  77  ? 1.6667 0.7210 1.2629 -0.0596 -0.2824 0.1294  78  SER   V C   
38286 O  O   . SER   V  77  ? 1.6445 0.9061 1.2913 -0.0358 -0.2725 0.0932  78  SER   V O   
38287 C  CB  . SER   V  77  ? 1.6625 0.7121 1.2233 -0.0950 -0.2597 0.1247  78  SER   V CB  
38288 O  OG  . SER   V  77  ? 1.6700 0.7753 1.1910 -0.0579 -0.2653 0.1236  78  SER   V OG  
38289 N  N   . ALA   V  78  ? 1.6703 0.6630 1.2878 -0.0655 -0.2744 0.1587  79  ALA   V N   
38290 C  CA  . ALA   V  78  ? 1.7064 0.6117 1.3179 -0.0670 -0.2553 0.1616  79  ALA   V CA  
38291 C  C   . ALA   V  78  ? 1.7014 0.6127 1.3003 -0.0693 -0.2528 0.1751  79  ALA   V C   
38292 O  O   . ALA   V  78  ? 1.6757 0.6743 1.2850 -0.1247 -0.2066 0.0988  79  ALA   V O   
38293 C  CB  . ALA   V  78  ? 1.7120 0.5371 1.3069 -0.0621 -0.2409 0.1856  79  ALA   V CB  
38294 N  N   . LEU   V  79  ? 1.6834 0.6188 1.2712 -0.0851 -0.2735 0.2338  80  LEU   V N   
38295 C  CA  . LEU   V  79  ? 1.6270 0.6389 1.2990 -0.1123 -0.2551 0.2731  80  LEU   V CA  
38296 C  C   . LEU   V  79  ? 1.6182 0.5677 1.3263 -0.0719 -0.2809 0.2675  80  LEU   V C   
38297 O  O   . LEU   V  79  ? 1.5666 0.6602 1.4089 -0.1065 -0.2544 0.2882  80  LEU   V O   
38298 C  CB  . LEU   V  79  ? 1.6545 0.6468 1.2938 -0.0966 -0.2397 0.2986  80  LEU   V CB  
38299 C  CG  . LEU   V  79  ? 1.6522 0.6297 1.2939 -0.0900 -0.2235 0.3073  80  LEU   V CG  
38300 C  CD1 . LEU   V  79  ? 1.6716 0.6053 1.3225 -0.0941 -0.1744 0.3229  80  LEU   V CD1 
38301 C  CD2 . LEU   V  79  ? 1.6390 0.6746 1.2982 -0.0870 -0.2363 0.3073  80  LEU   V CD2 
38302 N  N   . GLN   V  80  ? 1.5960 0.4596 1.3315 -0.1337 -0.2550 0.1858  81  GLN   V N   
38303 C  CA  . GLN   V  80  ? 1.5921 0.4131 1.3417 -0.1445 -0.2858 0.1456  81  GLN   V CA  
38304 C  C   . GLN   V  80  ? 1.6229 0.4160 1.3328 -0.1466 -0.3093 0.1313  81  GLN   V C   
38305 O  O   . GLN   V  80  ? 1.6188 0.3433 1.3047 -0.1644 -0.3500 0.1018  81  GLN   V O   
38306 C  CB  . GLN   V  80  ? 1.5956 0.4036 1.3736 -0.1518 -0.3211 0.1389  81  GLN   V CB  
38307 C  CG  . GLN   V  80  ? 1.5963 0.3990 1.3511 -0.1667 -0.3676 0.1024  81  GLN   V CG  
38308 C  CD  . GLN   V  80  ? 1.6206 0.3158 1.3840 -0.1480 -0.3531 0.0648  81  GLN   V CD  
38309 O  OE1 . GLN   V  80  ? 1.5706 0.4306 1.2553 -0.0808 -0.3933 0.0422  81  GLN   V OE1 
38310 N  NE2 . GLN   V  80  ? 1.6366 0.2677 1.4029 -0.1752 -0.3894 0.0519  81  GLN   V NE2 
38311 N  N   . MET   V  81  ? 1.6324 0.4700 1.2876 -0.1464 -0.3190 0.1419  82  MET   V N   
38312 C  CA  . MET   V  81  ? 1.6752 0.5185 1.2848 -0.0873 -0.3077 0.1466  82  MET   V CA  
38313 C  C   . MET   V  81  ? 1.6459 0.4969 1.2569 -0.0846 -0.2960 0.1219  82  MET   V C   
38314 O  O   . MET   V  81  ? 1.6169 0.5748 1.2255 -0.0672 -0.3068 0.0780  82  MET   V O   
38315 C  CB  . MET   V  81  ? 1.7149 0.5554 1.2836 -0.1160 -0.3134 0.1523  82  MET   V CB  
38316 C  CG  . MET   V  81  ? 1.8013 0.5860 1.2883 -0.0735 -0.3102 0.1885  82  MET   V CG  
38317 S  SD  . MET   V  81  ? 1.8000 0.6102 1.3090 -0.0634 -0.3552 0.1886  82  MET   V SD  
38318 C  CE  . MET   V  81  ? 1.7773 0.5708 1.3099 -0.0602 -0.3892 0.1553  82  MET   V CE  
38319 N  N   . LEU   V  82  ? 1.6665 0.5132 1.2641 -0.0857 -0.2652 0.1049  83  LEU   V N   
38320 C  CA  . LEU   V  82  ? 1.6258 0.4682 1.2378 -0.0774 -0.2542 0.0550  83  LEU   V CA  
38321 C  C   . LEU   V  82  ? 1.6685 0.3019 1.1933 -0.0752 -0.2414 0.1035  83  LEU   V C   
38322 O  O   . LEU   V  82  ? 1.6501 0.2777 1.1801 -0.1185 -0.2696 0.0895  83  LEU   V O   
38323 C  CB  . LEU   V  82  ? 1.6408 0.4693 1.2211 -0.0585 -0.2539 0.0451  83  LEU   V CB  
38324 C  CG  . LEU   V  82  ? 1.6316 0.5250 1.2536 -0.0565 -0.2467 0.0173  83  LEU   V CG  
38325 C  CD1 . LEU   V  82  ? 1.6488 0.5313 1.2421 -0.0743 -0.2375 0.0065  83  LEU   V CD1 
38326 C  CD2 . LEU   V  82  ? 1.6391 0.5589 1.2434 -0.0566 -0.2189 0.0091  83  LEU   V CD2 
38327 N  N   . LYS   V  83  ? 1.6715 0.3234 1.1849 -0.0388 -0.2307 0.0931  84  LYS   V N   
38328 C  CA  . LYS   V  83  ? 1.6272 0.3986 1.2036 -0.0213 -0.2470 0.0826  84  LYS   V CA  
38329 C  C   . LYS   V  83  ? 1.6569 0.4103 1.1967 0.0465  -0.2572 0.0720  84  LYS   V C   
38330 O  O   . LYS   V  83  ? 1.5822 0.3877 1.2239 0.0734  -0.2758 0.0345  84  LYS   V O   
38331 C  CB  . LYS   V  83  ? 1.6628 0.4611 1.2077 0.0091  -0.2403 0.0922  84  LYS   V CB  
38332 C  CG  . LYS   V  83  ? 1.6443 0.4918 1.2290 0.0378  -0.2802 0.0672  84  LYS   V CG  
38333 C  CD  . LYS   V  83  ? 1.6369 0.5843 1.2571 0.0116  -0.2829 0.0286  84  LYS   V CD  
38334 C  CE  . LYS   V  83  ? 1.6188 0.6261 1.2505 -0.0101 -0.2860 0.0112  84  LYS   V CE  
38335 N  NZ  . LYS   V  83  ? 1.6223 0.6409 1.2803 -0.0488 -0.2651 -0.0337 84  LYS   V NZ  
38336 N  N   . GLN   V  84  ? 1.6728 0.4121 1.1812 0.0323  -0.2606 0.0525  85  GLN   V N   
38337 C  CA  . GLN   V  84  ? 1.6749 0.4342 1.1661 0.0346  -0.2637 0.0504  85  GLN   V CA  
38338 C  C   . GLN   V  84  ? 1.6732 0.4195 1.1637 0.0134  -0.2522 0.0243  85  GLN   V C   
38339 O  O   . GLN   V  84  ? 1.6955 0.2958 1.2390 -0.0264 -0.2201 -0.0187 85  GLN   V O   
38340 C  CB  . GLN   V  84  ? 1.6631 0.4406 1.1202 0.0527  -0.2832 0.0492  85  GLN   V CB  
38341 C  CG  . GLN   V  84  ? 1.6697 0.4423 1.1253 0.0562  -0.2825 0.0649  85  GLN   V CG  
38342 C  CD  . GLN   V  84  ? 1.6881 0.4332 1.1199 0.0292  -0.2974 0.0680  85  GLN   V CD  
38343 O  OE1 . GLN   V  84  ? 1.6595 0.4340 1.0156 0.1041  -0.3542 0.1142  85  GLN   V OE1 
38344 N  NE2 . GLN   V  84  ? 1.7029 0.3562 1.1245 0.0216  -0.2825 0.1003  85  GLN   V NE2 
38345 N  N   . HIS   V  85  ? 1.6735 0.4193 1.1887 0.0218  -0.2659 0.0278  86  HIS   V N   
38346 C  CA  . HIS   V  85  ? 1.6488 0.5164 1.1914 0.0705  -0.2946 0.0194  86  HIS   V CA  
38347 C  C   . HIS   V  85  ? 1.6438 0.5450 1.1906 0.0283  -0.2929 0.0313  86  HIS   V C   
38348 O  O   . HIS   V  85  ? 1.6334 0.7519 1.1858 0.0591  -0.2665 0.0206  86  HIS   V O   
38349 C  CB  . HIS   V  85  ? 1.6193 0.4774 1.2230 0.1089  -0.2855 0.0298  86  HIS   V CB  
38350 C  CG  . HIS   V  85  ? 1.6114 0.5802 1.2166 0.1439  -0.2816 0.0089  86  HIS   V CG  
38351 N  ND1 . HIS   V  85  ? 1.6026 0.6314 1.1586 0.1726  -0.2995 0.0253  86  HIS   V ND1 
38352 C  CD2 . HIS   V  85  ? 1.5651 0.6868 1.1756 0.1771  -0.2884 0.0030  86  HIS   V CD2 
38353 C  CE1 . HIS   V  85  ? 1.6026 0.6981 1.1331 0.1737  -0.2913 -0.0004 86  HIS   V CE1 
38354 N  NE2 . HIS   V  85  ? 1.5930 0.7182 1.1979 0.1742  -0.2444 -0.0323 86  HIS   V NE2 
38355 N  N   . LEU   V  86  ? 1.6270 0.5035 1.1224 -0.0260 -0.2997 0.0408  87  LEU   V N   
38356 C  CA  . LEU   V  86  ? 1.5754 0.5006 1.0621 -0.0550 -0.3050 0.0561  87  LEU   V CA  
38357 C  C   . LEU   V  86  ? 1.5942 0.4766 1.1153 -0.0827 -0.2974 0.0226  87  LEU   V C   
38358 O  O   . LEU   V  86  ? 1.5292 0.6006 1.0818 -0.1689 -0.2217 -0.0371 87  LEU   V O   
38359 C  CB  . LEU   V  86  ? 1.5875 0.4084 1.0316 -0.0567 -0.2923 0.1087  87  LEU   V CB  
38360 C  CG  . LEU   V  86  ? 1.5808 0.4316 1.0639 -0.0616 -0.2662 0.1209  87  LEU   V CG  
38361 C  CD1 . LEU   V  86  ? 1.6043 0.4081 1.0261 -0.0917 -0.2495 0.1457  87  LEU   V CD1 
38362 C  CD2 . LEU   V  86  ? 1.6102 0.5124 1.0499 -0.0152 -0.2652 0.1110  87  LEU   V CD2 
38363 N  N   . PHE   V  87  ? 1.5856 0.4094 1.1560 -0.0885 -0.2972 0.0424  88  PHE   V N   
38364 C  CA  . PHE   V  87  ? 1.5796 0.4267 1.2012 -0.0562 -0.3291 0.0645  88  PHE   V CA  
38365 C  C   . PHE   V  87  ? 1.6310 0.3985 1.1700 -0.0378 -0.3301 0.0787  88  PHE   V C   
38366 O  O   . PHE   V  87  ? 1.6211 0.4970 1.0595 -0.0778 -0.3373 0.0445  88  PHE   V O   
38367 C  CB  . PHE   V  87  ? 1.5432 0.3525 1.2671 -0.0106 -0.3441 0.0655  88  PHE   V CB  
38368 C  CG  . PHE   V  87  ? 1.5206 0.3127 1.3504 0.0268  -0.3626 0.0820  88  PHE   V CG  
38369 C  CD1 . PHE   V  87  ? 1.5124 0.3982 1.3402 -0.0261 -0.3978 0.0455  88  PHE   V CD1 
38370 C  CD2 . PHE   V  87  ? 1.5220 0.2418 1.3686 0.0206  -0.4047 0.0381  88  PHE   V CD2 
38371 C  CE1 . PHE   V  87  ? 1.4770 0.4133 1.3418 0.0236  -0.3984 0.0786  88  PHE   V CE1 
38372 C  CE2 . PHE   V  87  ? 1.5029 0.2499 1.3799 0.0381  -0.4027 0.0702  88  PHE   V CE2 
38373 C  CZ  . PHE   V  87  ? 1.5124 0.2817 1.3375 0.0267  -0.4264 0.0703  88  PHE   V CZ  
38374 N  N   . LYS   V  88  ? 1.6715 0.4019 1.2189 -0.0653 -0.3675 0.0791  89  LYS   V N   
38375 C  CA  . LYS   V  88  ? 1.6894 0.5077 1.2202 -0.0718 -0.3533 0.0795  89  LYS   V CA  
38376 C  C   . LYS   V  88  ? 1.6798 0.4144 1.2484 -0.1009 -0.3394 0.0595  89  LYS   V C   
38377 O  O   . LYS   V  88  ? 1.7029 0.2814 1.2138 -0.1740 -0.3290 -0.0135 89  LYS   V O   
38378 C  CB  . LYS   V  88  ? 1.7457 0.5992 1.3032 -0.1265 -0.3933 0.0042  89  LYS   V CB  
38379 C  CG  . LYS   V  88  ? 1.7714 0.8095 1.3369 -0.1239 -0.3555 -0.0230 89  LYS   V CG  
38380 C  CD  . LYS   V  88  ? 1.8934 0.8791 1.4817 -0.2321 -0.3706 -0.0371 89  LYS   V CD  
38381 C  CE  . LYS   V  88  ? 1.8884 0.9811 1.5885 -0.2551 -0.3808 -0.0400 89  LYS   V CE  
38382 N  NZ  . LYS   V  88  ? 1.9533 0.9460 1.6667 -0.2380 -0.3694 -0.0756 89  LYS   V NZ  
38383 N  N   . TYR   V  89  ? 1.6967 0.5066 1.2894 -0.0525 -0.3570 0.0522  90  TYR   V N   
38384 C  CA  . TYR   V  89  ? 1.7003 0.5859 1.3150 0.0333  -0.3751 0.0809  90  TYR   V CA  
38385 C  C   . TYR   V  89  ? 1.7215 0.5153 1.3223 0.0694  -0.3498 0.1583  90  TYR   V C   
38386 O  O   . TYR   V  89  ? 1.7039 0.4014 1.3065 0.0294  -0.3490 0.0982  90  TYR   V O   
38387 C  CB  . TYR   V  89  ? 1.6923 0.6501 1.3607 0.0333  -0.3686 0.0629  90  TYR   V CB  
38388 C  CG  . TYR   V  89  ? 1.7159 0.6475 1.3729 0.0633  -0.3472 0.0501  90  TYR   V CG  
38389 C  CD1 . TYR   V  89  ? 1.7092 0.6683 1.3669 0.0738  -0.3471 0.0465  90  TYR   V CD1 
38390 C  CD2 . TYR   V  89  ? 1.7633 0.6577 1.3770 0.0397  -0.3323 0.0513  90  TYR   V CD2 
38391 C  CE1 . TYR   V  89  ? 1.7550 0.6731 1.3719 0.0541  -0.3100 0.0436  90  TYR   V CE1 
38392 C  CE2 . TYR   V  89  ? 1.7941 0.6711 1.3925 0.0116  -0.3328 0.0362  90  TYR   V CE2 
38393 C  CZ  . TYR   V  89  ? 1.8156 0.6336 1.3823 0.0175  -0.2962 -0.0294 90  TYR   V CZ  
38394 O  OH  . TYR   V  89  ? 1.8492 0.6117 1.4990 -0.0609 -0.2219 -0.0705 90  TYR   V OH  
38395 N  N   . GLN   V  90  ? 1.6992 0.4991 1.3056 0.1354  -0.3370 0.1917  91  GLN   V N   
38396 C  CA  . GLN   V  90  ? 1.6519 0.5078 1.3608 0.1006  -0.3386 0.2417  91  GLN   V CA  
38397 C  C   . GLN   V  90  ? 1.6376 0.6074 1.3805 0.1426  -0.3129 0.2993  91  GLN   V C   
38398 O  O   . GLN   V  90  ? 1.7171 0.5548 1.5751 0.1677  -0.2956 0.3020  91  GLN   V O   
38399 C  CB  . GLN   V  90  ? 1.6197 0.5902 1.3669 0.2008  -0.3470 0.2820  91  GLN   V CB  
38400 C  CG  . GLN   V  90  ? 1.6808 0.5417 1.4568 0.2398  -0.3185 0.2859  91  GLN   V CG  
38401 C  CD  . GLN   V  90  ? 1.7051 0.6845 1.4308 0.3404  -0.3575 0.4204  91  GLN   V CD  
38402 O  OE1 . GLN   V  90  ? 1.7477 0.7233 1.5904 0.4496  -0.3673 0.3205  91  GLN   V OE1 
38403 N  NE2 . GLN   V  90  ? 1.6872 0.7245 1.4245 0.3519  -0.3782 0.4415  91  GLN   V NE2 
38404 N  N   . GLY   V  91  ? 1.6340 0.5941 1.3155 0.1685  -0.2895 0.3431  92  GLY   V N   
38405 C  CA  . GLY   V  91  ? 1.6012 0.5537 1.3066 0.1382  -0.2636 0.3280  92  GLY   V CA  
38406 C  C   . GLY   V  91  ? 1.6127 0.5033 1.2816 0.1517  -0.2391 0.3087  92  GLY   V C   
38407 O  O   . GLY   V  91  ? 1.6119 0.5964 1.2628 0.1772  -0.2076 0.3735  92  GLY   V O   
38408 N  N   . HIS   V  92  ? 1.5685 0.4582 1.2698 0.1552  -0.2724 0.3050  93  HIS   V N   
38409 C  CA  . HIS   V  92  ? 1.4818 0.5032 1.2550 0.1452  -0.2773 0.2480  93  HIS   V CA  
38410 C  C   . HIS   V  92  ? 1.5215 0.4791 1.2579 0.0937  -0.2849 0.2002  93  HIS   V C   
38411 O  O   . HIS   V  92  ? 1.4734 0.7899 1.2975 0.1194  -0.3875 0.1385  93  HIS   V O   
38412 C  CB  . HIS   V  92  ? 1.5034 0.5058 1.2312 0.1409  -0.2648 0.2484  93  HIS   V CB  
38413 C  CG  . HIS   V  92  ? 1.5067 0.5274 1.2475 0.1274  -0.2126 0.2395  93  HIS   V CG  
38414 N  ND1 . HIS   V  92  ? 1.5147 0.5781 1.2573 0.0794  -0.1722 0.2757  93  HIS   V ND1 
38415 C  CD2 . HIS   V  92  ? 1.5166 0.4456 1.2201 0.1284  -0.2079 0.2699  93  HIS   V CD2 
38416 C  CE1 . HIS   V  92  ? 1.5058 0.6535 1.2734 0.1042  -0.2161 0.2692  93  HIS   V CE1 
38417 N  NE2 . HIS   V  92  ? 1.5239 0.5265 1.2709 0.0718  -0.1929 0.2479  93  HIS   V NE2 
38418 N  N   . ILE   V  93  ? 1.4209 0.4796 1.2282 0.0031  -0.2816 0.1246  94  ILE   V N   
38419 C  CA  . ILE   V  93  ? 1.4358 0.5657 1.1988 -0.0405 -0.2486 0.0870  94  ILE   V CA  
38420 C  C   . ILE   V  93  ? 1.4164 0.4920 1.1670 -0.1039 -0.2442 0.1007  94  ILE   V C   
38421 O  O   . ILE   V  93  ? 1.4261 0.4911 1.1160 -0.2429 -0.1636 0.0671  94  ILE   V O   
38422 C  CB  . ILE   V  93  ? 1.4192 0.5769 1.2094 -0.0826 -0.2322 0.0932  94  ILE   V CB  
38423 C  CG1 . ILE   V  93  ? 1.4271 0.6776 1.2175 -0.0973 -0.2218 0.0604  94  ILE   V CG1 
38424 C  CG2 . ILE   V  93  ? 1.4187 0.5906 1.1700 -0.0850 -0.2327 0.0646  94  ILE   V CG2 
38425 C  CD1 . ILE   V  93  ? 1.4432 0.6905 1.2241 -0.1021 -0.2216 0.0850  94  ILE   V CD1 
38426 N  N   . GLY   V  94  ? 1.4141 0.4913 1.1519 -0.1124 -0.2552 0.1034  95  GLY   V N   
38427 C  CA  . GLY   V  94  ? 1.4052 0.5199 1.2043 -0.1027 -0.2489 0.0840  95  GLY   V CA  
38428 C  C   . GLY   V  94  ? 1.4349 0.4407 1.2506 -0.1298 -0.2576 0.1463  95  GLY   V C   
38429 O  O   . GLY   V  94  ? 1.3304 0.5390 1.3089 -0.1840 -0.2481 0.1304  95  GLY   V O   
38430 N  N   . ALA   V  95  ? 1.4343 0.4103 1.3114 -0.0141 -0.2905 0.1461  96  ALA   V N   
38431 C  CA  . ALA   V  95  ? 1.4292 0.4324 1.3020 0.0292  -0.2806 0.1579  96  ALA   V CA  
38432 C  C   . ALA   V  95  ? 1.4371 0.3195 1.3175 0.0810  -0.2896 0.1379  96  ALA   V C   
38433 O  O   . ALA   V  95  ? 1.4241 0.3322 1.2965 0.0545  -0.3062 0.0507  96  ALA   V O   
38434 C  CB  . ALA   V  95  ? 1.4184 0.4459 1.3482 -0.0012 -0.2927 0.1126  96  ALA   V CB  
38435 N  N   . TYR   V  96  ? 1.4616 0.3310 1.2790 0.0908  -0.2823 0.1382  97  TYR   V N   
38436 C  CA  . TYR   V  96  ? 1.4833 0.4203 1.2697 0.0283  -0.2837 0.1369  97  TYR   V CA  
38437 C  C   . TYR   V  96  ? 1.5138 0.4307 1.2283 -0.0049 -0.2886 0.1251  97  TYR   V C   
38438 O  O   . TYR   V  96  ? 1.5497 0.4575 1.2075 -0.0425 -0.3275 0.2023  97  TYR   V O   
38439 C  CB  . TYR   V  96  ? 1.4859 0.4301 1.3414 -0.0086 -0.2539 0.0963  97  TYR   V CB  
38440 C  CG  . TYR   V  96  ? 1.4804 0.4763 1.4244 -0.0271 -0.2309 0.0586  97  TYR   V CG  
38441 C  CD1 . TYR   V  96  ? 1.5011 0.5340 1.4273 -0.0484 -0.1999 0.0327  97  TYR   V CD1 
38442 C  CD2 . TYR   V  96  ? 1.4756 0.4833 1.3973 -0.0198 -0.2202 0.0532  97  TYR   V CD2 
38443 C  CE1 . TYR   V  96  ? 1.4753 0.5907 1.5175 -0.0769 -0.2184 -0.0142 97  TYR   V CE1 
38444 C  CE2 . TYR   V  96  ? 1.4902 0.4922 1.4858 -0.0677 -0.2306 0.0230  97  TYR   V CE2 
38445 C  CZ  . TYR   V  96  ? 1.4926 0.5442 1.5026 -0.1165 -0.2196 0.0072  97  TYR   V CZ  
38446 O  OH  . TYR   V  96  ? 1.4553 0.5560 1.6767 -0.2103 -0.3036 -0.0778 97  TYR   V OH  
38447 N  N   . LEU   V  97  ? 1.5139 0.4374 1.1857 -0.0403 -0.2681 0.1166  98  LEU   V N   
38448 C  CA  . LEU   V  97  ? 1.5301 0.5098 1.2062 -0.0598 -0.2361 0.1554  98  LEU   V CA  
38449 C  C   . LEU   V  97  ? 1.5139 0.5007 1.1989 -0.0722 -0.2547 0.1461  98  LEU   V C   
38450 O  O   . LEU   V  97  ? 1.5183 0.4064 1.1672 -0.0925 -0.2441 0.1563  98  LEU   V O   
38451 C  CB  . LEU   V  97  ? 1.5609 0.5024 1.2240 -0.0580 -0.2257 0.1744  98  LEU   V CB  
38452 C  CG  . LEU   V  97  ? 1.5576 0.5173 1.2195 -0.0507 -0.2282 0.2021  98  LEU   V CG  
38453 C  CD1 . LEU   V  97  ? 1.5581 0.5344 1.2493 -0.0322 -0.2295 0.1929  98  LEU   V CD1 
38454 C  CD2 . LEU   V  97  ? 1.5558 0.5726 1.2344 -0.0696 -0.2359 0.2242  98  LEU   V CD2 
38455 N  N   . ILE   V  98  ? 1.5206 0.5753 1.1907 -0.0679 -0.2419 0.1700  99  ILE   V N   
38456 C  CA  . ILE   V  98  ? 1.5116 0.5870 1.1938 -0.0515 -0.2338 0.1796  99  ILE   V CA  
38457 C  C   . ILE   V  98  ? 1.5261 0.5897 1.2460 -0.0602 -0.2460 0.2005  99  ILE   V C   
38458 O  O   . ILE   V  98  ? 1.5536 0.6390 1.2426 -0.0512 -0.2877 0.2640  99  ILE   V O   
38459 C  CB  . ILE   V  98  ? 1.5177 0.6269 1.1586 -0.0392 -0.2139 0.1797  99  ILE   V CB  
38460 C  CG1 . ILE   V  98  ? 1.4955 0.6052 1.1338 -0.0233 -0.2110 0.2089  99  ILE   V CG1 
38461 C  CG2 . ILE   V  98  ? 1.5273 0.6523 1.1741 -0.0386 -0.1831 0.1595  99  ILE   V CG2 
38462 C  CD1 . ILE   V  98  ? 1.5047 0.6241 1.1352 -0.0117 -0.2042 0.2196  99  ILE   V CD1 
38463 N  N   . VAL   V  99  ? 1.5141 0.5448 1.3084 -0.0583 -0.2398 0.1844  100 VAL   V N   
38464 C  CA  . VAL   V  99  ? 1.5206 0.5355 1.2995 -0.0555 -0.2275 0.1884  100 VAL   V CA  
38465 C  C   . VAL   V  99  ? 1.5177 0.3995 1.2744 -0.0661 -0.2591 0.1908  100 VAL   V C   
38466 O  O   . VAL   V  99  ? 1.5220 0.4166 1.2569 -0.0591 -0.2807 0.2416  100 VAL   V O   
38467 C  CB  . VAL   V  99  ? 1.5351 0.4410 1.3183 -0.0744 -0.2086 0.1970  100 VAL   V CB  
38468 C  CG1 . VAL   V  99  ? 1.5531 0.4350 1.3399 -0.0604 -0.2119 0.1985  100 VAL   V CG1 
38469 C  CG2 . VAL   V  99  ? 1.5088 0.5043 1.3434 -0.0800 -0.1774 0.1571  100 VAL   V CG2 
38470 N  N   . ALA   V  100 ? 1.5176 0.3941 1.3008 -0.0595 -0.2603 0.1380  101 ALA   V N   
38471 C  CA  . ALA   V  100 ? 1.5372 0.4796 1.3043 -0.0543 -0.2346 0.1132  101 ALA   V CA  
38472 C  C   . ALA   V  100 ? 1.5438 0.5369 1.3226 -0.1031 -0.2268 0.0930  101 ALA   V C   
38473 O  O   . ALA   V  100 ? 1.5569 0.6139 1.3134 -0.1581 -0.2092 0.0923  101 ALA   V O   
38474 C  CB  . ALA   V  100 ? 1.5767 0.4401 1.3291 -0.0472 -0.2510 0.1147  101 ALA   V CB  
38475 N  N   . GLY   V  101 ? 1.5305 0.5448 1.3096 -0.0879 -0.2223 0.0850  102 GLY   V N   
38476 C  CA  . GLY   V  101 ? 1.5437 0.5650 1.3459 -0.1059 -0.2344 0.0712  102 GLY   V CA  
38477 C  C   . GLY   V  101 ? 1.5522 0.6336 1.3247 -0.1223 -0.2395 0.0733  102 GLY   V C   
38478 O  O   . GLY   V  101 ? 1.5213 0.5929 1.3158 -0.0834 -0.2207 0.0499  102 GLY   V O   
38479 N  N   . VAL   V  102 ? 1.6038 0.6668 1.3772 -0.1643 -0.2287 0.1173  103 VAL   V N   
38480 C  CA  . VAL   V  102 ? 1.6520 0.6796 1.4167 -0.1964 -0.2129 0.1481  103 VAL   V CA  
38481 C  C   . VAL   V  102 ? 1.6729 0.6919 1.5223 -0.1637 -0.1867 0.1729  103 VAL   V C   
38482 O  O   . VAL   V  102 ? 1.7089 0.7483 1.4738 -0.2308 -0.1596 0.2669  103 VAL   V O   
38483 C  CB  . VAL   V  102 ? 1.6703 0.6281 1.4074 -0.2039 -0.1965 0.1584  103 VAL   V CB  
38484 C  CG1 . VAL   V  102 ? 1.6680 0.6410 1.3673 -0.1992 -0.2063 0.1530  103 VAL   V CG1 
38485 C  CG2 . VAL   V  102 ? 1.6564 0.6262 1.4284 -0.2159 -0.2000 0.1739  103 VAL   V CG2 
38486 N  N   . ASP   V  103 ? 1.6965 0.7764 1.5589 -0.0941 -0.2187 0.1484  104 ASP   V N   
38487 C  CA  . ASP   V  103 ? 1.7539 0.8031 1.6666 -0.0707 -0.1626 0.1162  104 ASP   V CA  
38488 C  C   . ASP   V  103 ? 1.8538 0.7360 1.7283 -0.0901 -0.1463 0.1505  104 ASP   V C   
38489 O  O   . ASP   V  103 ? 1.9577 0.3831 1.7500 -0.1915 -0.1131 0.1837  104 ASP   V O   
38490 C  CB  . ASP   V  103 ? 1.7431 0.8190 1.6664 -0.0214 -0.1394 0.0463  104 ASP   V CB  
38491 C  CG  . ASP   V  103 ? 1.6753 0.7861 1.6689 0.0157  -0.0881 0.0042  104 ASP   V CG  
38492 O  OD1 . ASP   V  103 ? 1.6411 0.8429 1.6483 0.0859  -0.0768 -0.0553 104 ASP   V OD1 
38493 O  OD2 . ASP   V  103 ? 1.6689 0.6987 1.5764 0.1164  -0.0502 -0.0012 104 ASP   V OD2 
38494 N  N   . PRO   V  104 ? 1.8356 0.7545 1.8021 -0.0678 -0.2053 0.1549  105 PRO   V N   
38495 C  CA  . PRO   V  104 ? 1.7826 0.9080 1.7545 -0.0619 -0.2411 0.1582  105 PRO   V CA  
38496 C  C   . PRO   V  104 ? 1.7225 0.9630 1.6753 0.0010  -0.2623 0.2120  105 PRO   V C   
38497 O  O   . PRO   V  104 ? 1.6919 1.1264 1.6884 0.0056  -0.2579 0.2588  105 PRO   V O   
38498 C  CB  . PRO   V  104 ? 1.8181 0.8345 1.8230 -0.1211 -0.2590 0.1130  105 PRO   V CB  
38499 C  CG  . PRO   V  104 ? 1.8631 0.8284 1.8320 -0.1228 -0.2525 0.1051  105 PRO   V CG  
38500 C  CD  . PRO   V  104 ? 1.8486 0.8119 1.8201 -0.1209 -0.2273 0.0977  105 PRO   V CD  
38501 N  N   . THR   V  105 ? 1.7094 0.8397 1.6163 0.0705  -0.2917 0.2279  106 THR   V N   
38502 C  CA  . THR   V  105 ? 1.7582 0.8962 1.5459 0.0853  -0.3007 0.2438  106 THR   V CA  
38503 C  C   . THR   V  105 ? 1.7278 0.9442 1.4815 0.1079  -0.2888 0.2851  106 THR   V C   
38504 O  O   . THR   V  105 ? 1.7120 1.0341 1.4604 0.0855  -0.2665 0.2904  106 THR   V O   
38505 C  CB  . THR   V  105 ? 1.7918 0.8856 1.5040 0.0808  -0.2868 0.2521  106 THR   V CB  
38506 O  OG1 . THR   V  105 ? 1.8618 0.8931 1.5457 0.0759  -0.2269 0.2338  106 THR   V OG1 
38507 C  CG2 . THR   V  105 ? 1.7707 0.8597 1.4926 0.0898  -0.2715 0.2501  106 THR   V CG2 
38508 N  N   . GLY   V  106 ? 1.7178 0.9698 1.5377 0.0800  -0.3107 0.3131  107 GLY   V N   
38509 C  CA  . GLY   V  106 ? 1.7555 0.9152 1.5639 -0.0084 -0.2670 0.2212  107 GLY   V CA  
38510 C  C   . GLY   V  106 ? 1.7366 0.7998 1.6424 -0.0354 -0.3026 0.2082  107 GLY   V C   
38511 O  O   . GLY   V  106 ? 1.7496 0.6920 1.6457 -0.0190 -0.2719 0.2511  107 GLY   V O   
38512 N  N   . SER   V  107 ? 1.6738 0.8445 1.5726 -0.0594 -0.3134 0.1247  108 SER   V N   
38513 C  CA  . SER   V  107 ? 1.6594 0.8606 1.4995 -0.1326 -0.2972 0.1183  108 SER   V CA  
38514 C  C   . SER   V  107 ? 1.6707 0.7922 1.4054 -0.1203 -0.2899 0.1311  108 SER   V C   
38515 O  O   . SER   V  107 ? 1.7041 0.7876 1.4003 -0.1752 -0.2584 0.0606  108 SER   V O   
38516 C  CB  . SER   V  107 ? 1.6622 0.9204 1.5042 -0.1521 -0.2665 0.0676  108 SER   V CB  
38517 O  OG  . SER   V  107 ? 1.6593 0.9113 1.5230 -0.2081 -0.2757 0.0734  108 SER   V OG  
38518 N  N   . HIS   V  108 ? 1.6584 0.7159 1.4154 -0.0969 -0.3294 0.1585  109 HIS   V N   
38519 C  CA  . HIS   V  108 ? 1.6479 0.7525 1.3935 -0.0957 -0.3481 0.1664  109 HIS   V CA  
38520 C  C   . HIS   V  108 ? 1.6526 0.7163 1.4109 -0.1241 -0.3249 0.1581  109 HIS   V C   
38521 O  O   . HIS   V  108 ? 1.7014 0.7519 1.4471 -0.1626 -0.3609 0.1807  109 HIS   V O   
38522 C  CB  . HIS   V  108 ? 1.6814 0.7273 1.3598 -0.0754 -0.3594 0.1986  109 HIS   V CB  
38523 C  CG  . HIS   V  108 ? 1.7239 0.7732 1.3147 -0.0854 -0.3988 0.2290  109 HIS   V CG  
38524 N  ND1 . HIS   V  108 ? 1.7119 0.6744 1.3190 -0.0289 -0.3980 0.2941  109 HIS   V ND1 
38525 C  CD2 . HIS   V  108 ? 1.7595 0.7335 1.3249 -0.0469 -0.4260 0.2808  109 HIS   V CD2 
38526 C  CE1 . HIS   V  108 ? 1.7143 0.6938 1.3438 0.0034  -0.4260 0.3092  109 HIS   V CE1 
38527 N  NE2 . HIS   V  108 ? 1.7413 0.8227 1.3366 -0.0102 -0.4546 0.2774  109 HIS   V NE2 
38528 N  N   . LEU   V  109 ? 1.5870 0.7439 1.3332 -0.1206 -0.3179 0.1559  110 LEU   V N   
38529 C  CA  . LEU   V  109 ? 1.5331 0.7489 1.2986 -0.1214 -0.2833 0.1458  110 LEU   V CA  
38530 C  C   . LEU   V  109 ? 1.5207 0.7370 1.2344 -0.1009 -0.2667 0.1142  110 LEU   V C   
38531 O  O   . LEU   V  109 ? 1.4790 0.7944 1.2061 -0.1122 -0.2347 0.1206  110 LEU   V O   
38532 C  CB  . LEU   V  109 ? 1.5434 0.7161 1.3169 -0.1385 -0.2810 0.1456  110 LEU   V CB  
38533 C  CG  . LEU   V  109 ? 1.5549 0.6775 1.3205 -0.1910 -0.2496 0.1273  110 LEU   V CG  
38534 C  CD1 . LEU   V  109 ? 1.5603 0.6322 1.3101 -0.2048 -0.2470 0.1742  110 LEU   V CD1 
38535 C  CD2 . LEU   V  109 ? 1.5845 0.6486 1.2975 -0.1954 -0.2585 0.1274  110 LEU   V CD2 
38536 N  N   . PHE   V  110 ? 1.5140 0.6636 1.2620 -0.0987 -0.2253 0.0793  111 PHE   V N   
38537 C  CA  . PHE   V  110 ? 1.4885 0.6138 1.2836 -0.0961 -0.2598 0.0425  111 PHE   V CA  
38538 C  C   . PHE   V  110 ? 1.5251 0.5913 1.2868 -0.0768 -0.2264 0.0325  111 PHE   V C   
38539 O  O   . PHE   V  110 ? 1.5455 0.5496 1.2668 -0.0831 -0.2331 0.0323  111 PHE   V O   
38540 C  CB  . PHE   V  110 ? 1.4735 0.5959 1.2804 -0.1117 -0.2676 0.0443  111 PHE   V CB  
38541 C  CG  . PHE   V  110 ? 1.4860 0.6154 1.2577 -0.1183 -0.2899 0.0444  111 PHE   V CG  
38542 C  CD1 . PHE   V  110 ? 1.4935 0.5635 1.2642 -0.1315 -0.2928 0.0334  111 PHE   V CD1 
38543 C  CD2 . PHE   V  110 ? 1.4970 0.6050 1.2811 -0.1228 -0.2806 0.0696  111 PHE   V CD2 
38544 C  CE1 . PHE   V  110 ? 1.5070 0.5844 1.2858 -0.1119 -0.2806 0.0552  111 PHE   V CE1 
38545 C  CE2 . PHE   V  110 ? 1.4893 0.6164 1.2763 -0.1302 -0.2821 0.0719  111 PHE   V CE2 
38546 C  CZ  . PHE   V  110 ? 1.4848 0.6263 1.2953 -0.1391 -0.2863 0.0426  111 PHE   V CZ  
38547 N  N   . SER   V  111 ? 1.4792 0.5926 1.2843 -0.0531 -0.2516 0.0093  112 SER   V N   
38548 C  CA  . SER   V  111 ? 1.5118 0.6154 1.2988 -0.0560 -0.2537 0.0196  112 SER   V CA  
38549 C  C   . SER   V  111 ? 1.5395 0.5385 1.3118 -0.0309 -0.2492 -0.0143 112 SER   V C   
38550 O  O   . SER   V  111 ? 1.5904 0.4910 1.2705 -0.0419 -0.2769 -0.0195 112 SER   V O   
38551 C  CB  . SER   V  111 ? 1.4788 0.6383 1.2884 -0.0608 -0.2793 -0.0079 112 SER   V CB  
38552 O  OG  . SER   V  111 ? 1.4888 0.7451 1.2495 -0.0536 -0.3137 -0.0279 112 SER   V OG  
38553 N  N   . ILE   V  112 ? 1.6415 0.4914 1.3185 -0.0228 -0.2018 -0.0257 113 ILE   V N   
38554 C  CA  . ILE   V  112 ? 1.6780 0.5462 1.3476 -0.0111 -0.1702 -0.0164 113 ILE   V CA  
38555 C  C   . ILE   V  112 ? 1.6769 0.4310 1.3331 0.0303  -0.1902 -0.0786 113 ILE   V C   
38556 O  O   . ILE   V  112 ? 1.6675 0.4419 1.3652 0.1011  -0.1725 -0.1099 113 ILE   V O   
38557 C  CB  . ILE   V  112 ? 1.7455 0.5989 1.3549 -0.0548 -0.1564 -0.0507 113 ILE   V CB  
38558 C  CG1 . ILE   V  112 ? 1.7649 0.6789 1.3826 -0.0964 -0.1705 -0.0095 113 ILE   V CG1 
38559 C  CG2 . ILE   V  112 ? 1.7369 0.6665 1.3508 -0.0537 -0.1479 -0.0026 113 ILE   V CG2 
38560 C  CD1 . ILE   V  112 ? 1.7802 0.6878 1.3951 -0.0764 -0.1916 -0.0227 113 ILE   V CD1 
38561 N  N   . HIS   V  113 ? 1.6755 0.3964 1.3295 0.0406  -0.2208 -0.0869 114 HIS   V N   
38562 C  CA  . HIS   V  113 ? 1.7011 0.4134 1.3450 0.0296  -0.2389 -0.0628 114 HIS   V CA  
38563 C  C   . HIS   V  113 ? 1.6387 0.2539 1.3328 -0.0018 -0.2757 -0.0616 114 HIS   V C   
38564 O  O   . HIS   V  113 ? 1.5934 0.2865 1.2298 0.0298  -0.3310 -0.1254 114 HIS   V O   
38565 C  CB  . HIS   V  113 ? 1.7397 0.4523 1.3959 0.0233  -0.2928 -0.0642 114 HIS   V CB  
38566 C  CG  . HIS   V  113 ? 1.7998 0.4565 1.4645 0.1002  -0.3170 -0.0532 114 HIS   V CG  
38567 N  ND1 . HIS   V  113 ? 1.8136 0.4151 1.4796 0.0880  -0.3243 -0.0263 114 HIS   V ND1 
38568 C  CD2 . HIS   V  113 ? 1.8012 0.4632 1.5126 0.1593  -0.3657 -0.0236 114 HIS   V CD2 
38569 C  CE1 . HIS   V  113 ? 1.7910 0.4366 1.4845 0.1504  -0.3782 -0.0112 114 HIS   V CE1 
38570 N  NE2 . HIS   V  113 ? 1.8012 0.4265 1.4706 0.1646  -0.3849 -0.0238 114 HIS   V NE2 
38571 N  N   . ALA   V  114 ? 1.6189 0.2966 1.3444 -0.0751 -0.2370 -0.0454 115 ALA   V N   
38572 C  CA  . ALA   V  114 ? 1.5712 0.2404 1.3590 -0.0674 -0.2290 -0.0231 115 ALA   V CA  
38573 C  C   . ALA   V  114 ? 1.5560 0.2225 1.3854 -0.1056 -0.2838 0.0160  115 ALA   V C   
38574 O  O   . ALA   V  114 ? 1.4969 0.1708 1.4859 -0.0797 -0.1984 0.0886  115 ALA   V O   
38575 C  CB  . ALA   V  114 ? 1.5895 0.3279 1.3417 -0.0566 -0.2329 0.0177  115 ALA   V CB  
38576 N  N   . HIS   V  115 ? 1.5698 0.2447 1.3133 -0.0300 -0.2680 -0.0374 116 HIS   V N   
38577 C  CA  . HIS   V  115 ? 1.5740 0.2817 1.2622 -0.0355 -0.2825 -0.0714 116 HIS   V CA  
38578 C  C   . HIS   V  115 ? 1.5615 0.2813 1.2175 -0.0766 -0.2630 -0.0774 116 HIS   V C   
38579 O  O   . HIS   V  115 ? 1.5860 0.2133 1.1899 -0.0787 -0.2756 -0.0863 116 HIS   V O   
38580 C  CB  . HIS   V  115 ? 1.5880 0.2679 1.2652 -0.0248 -0.2961 -0.0676 116 HIS   V CB  
38581 C  CG  . HIS   V  115 ? 1.6144 0.2157 1.2288 -0.0084 -0.3683 -0.0635 116 HIS   V CG  
38582 N  ND1 . HIS   V  115 ? 1.6155 0.2180 1.1965 0.0165  -0.3985 -0.0792 116 HIS   V ND1 
38583 C  CD2 . HIS   V  115 ? 1.6351 0.2318 1.2347 0.0119  -0.4269 -0.0579 116 HIS   V CD2 
38584 C  CE1 . HIS   V  115 ? 1.6182 0.2217 1.1996 0.0233  -0.4269 -0.0897 116 HIS   V CE1 
38585 N  NE2 . HIS   V  115 ? 1.6087 0.2047 1.2536 0.0431  -0.4306 -0.0734 116 HIS   V NE2 
38586 N  N   . GLY   V  116 ? 1.5607 0.3575 1.2196 -0.0843 -0.2479 -0.1001 117 GLY   V N   
38587 C  CA  . GLY   V  116 ? 1.5486 0.3558 1.2209 -0.0193 -0.2549 -0.0903 117 GLY   V CA  
38588 C  C   . GLY   V  116 ? 1.5498 0.4255 1.2229 0.0047  -0.2472 -0.0224 117 GLY   V C   
38589 O  O   . GLY   V  116 ? 1.5273 0.4030 1.2085 -0.0165 -0.2565 -0.0562 117 GLY   V O   
38590 N  N   . SER   V  117 ? 1.5624 0.4208 1.2617 0.0069  -0.2034 -0.0222 118 SER   V N   
38591 C  CA  . SER   V  117 ? 1.5492 0.4138 1.2679 0.0120  -0.1674 -0.0046 118 SER   V CA  
38592 C  C   . SER   V  117 ? 1.5788 0.3951 1.3189 -0.0071 -0.1294 0.0127  118 SER   V C   
38593 O  O   . SER   V  117 ? 1.5752 0.3972 1.2429 -0.0187 -0.0773 0.0701  118 SER   V O   
38594 C  CB  . SER   V  117 ? 1.5260 0.4611 1.2670 -0.0071 -0.1724 -0.0553 118 SER   V CB  
38595 O  OG  . SER   V  117 ? 1.5472 0.4290 1.3294 0.0204  -0.1672 -0.0713 118 SER   V OG  
38596 N  N   . THR   V  118 ? 1.6012 0.4020 1.3315 -0.0154 -0.1719 0.0308  119 THR   V N   
38597 C  CA  . THR   V  118 ? 1.5881 0.5483 1.4268 -0.0577 -0.1947 0.0208  119 THR   V CA  
38598 C  C   . THR   V  118 ? 1.5400 0.3969 1.4257 -0.0788 -0.2346 0.0346  119 THR   V C   
38599 O  O   . THR   V  118 ? 1.5522 0.1698 1.4302 -0.1148 -0.2404 0.0632  119 THR   V O   
38600 C  CB  . THR   V  118 ? 1.6265 0.5638 1.4438 -0.1035 -0.2340 0.0060  119 THR   V CB  
38601 O  OG1 . THR   V  118 ? 1.5996 0.6452 1.4988 -0.1172 -0.2667 0.0250  119 THR   V OG1 
38602 C  CG2 . THR   V  118 ? 1.6731 0.6966 1.4597 -0.1142 -0.2160 -0.0382 119 THR   V CG2 
38603 N  N   . ASP   V  119 ? 1.5637 0.4502 1.4744 -0.0577 -0.1900 0.0448  120 ASP   V N   
38604 C  CA  . ASP   V  119 ? 1.5944 0.5627 1.4618 -0.0369 -0.1831 0.0458  120 ASP   V CA  
38605 C  C   . ASP   V  119 ? 1.6499 0.4503 1.3989 0.0160  -0.1813 0.0820  120 ASP   V C   
38606 O  O   . ASP   V  119 ? 1.7374 0.3937 1.4790 -0.0028 -0.1770 0.0687  120 ASP   V O   
38607 C  CB  . ASP   V  119 ? 1.6220 0.7001 1.5740 0.0985  -0.1817 0.0629  120 ASP   V CB  
38608 C  CG  . ASP   V  119 ? 1.5508 0.9479 1.6941 0.0546  -0.1021 0.0971  120 ASP   V CG  
38609 O  OD1 . ASP   V  119 ? 1.6189 1.1350 1.7339 0.2778  -0.1895 0.1552  120 ASP   V OD1 
38610 O  OD2 . ASP   V  119 ? 1.7368 1.0830 1.8879 0.2711  -0.0898 0.0717  120 ASP   V OD2 
38611 N  N   . VAL   V  120 ? 1.5994 0.3880 1.3719 -0.0061 -0.2346 0.0897  121 VAL   V N   
38612 C  CA  . VAL   V  120 ? 1.6351 0.4565 1.3695 -0.0108 -0.1993 0.1048  121 VAL   V CA  
38613 C  C   . VAL   V  120 ? 1.5877 0.4296 1.3692 0.0252  -0.1957 0.1885  121 VAL   V C   
38614 O  O   . VAL   V  120 ? 1.5590 0.5027 1.4088 0.0097  -0.1884 0.1575  121 VAL   V O   
38615 C  CB  . VAL   V  120 ? 1.6457 0.5655 1.3602 0.0418  -0.1939 0.1233  121 VAL   V CB  
38616 C  CG1 . VAL   V  120 ? 1.6463 0.6461 1.3945 0.0513  -0.1346 0.1169  121 VAL   V CG1 
38617 C  CG2 . VAL   V  120 ? 1.6180 0.6189 1.3617 0.0565  -0.2039 0.1335  121 VAL   V CG2 
38618 N  N   . GLY   V  121 ? 1.5950 0.3379 1.3551 -0.0664 -0.2467 0.2382  122 GLY   V N   
38619 C  CA  . GLY   V  121 ? 1.5980 0.4411 1.3769 -0.0648 -0.2307 0.1962  122 GLY   V CA  
38620 C  C   . GLY   V  121 ? 1.6325 0.4495 1.4210 -0.1192 -0.2358 0.2429  122 GLY   V C   
38621 O  O   . GLY   V  121 ? 1.6871 0.4747 1.4218 -0.1059 -0.2686 0.2361  122 GLY   V O   
38622 N  N   . TYR   V  122 ? 1.6587 0.4608 1.4378 -0.1100 -0.2315 0.2179  123 TYR   V N   
38623 C  CA  . TYR   V  122 ? 1.6489 0.5205 1.4658 -0.0542 -0.2348 0.2149  123 TYR   V CA  
38624 C  C   . TYR   V  122 ? 1.6583 0.4563 1.4433 -0.0217 -0.2296 0.1620  123 TYR   V C   
38625 O  O   . TYR   V  122 ? 1.6200 0.3372 1.4712 0.0270  -0.2112 0.2035  123 TYR   V O   
38626 C  CB  . TYR   V  122 ? 1.7102 0.6284 1.4932 -0.0275 -0.2035 0.2158  123 TYR   V CB  
38627 C  CG  . TYR   V  122 ? 1.7139 0.7642 1.5604 -0.0067 -0.2524 0.2721  123 TYR   V CG  
38628 C  CD1 . TYR   V  122 ? 1.7609 0.8023 1.6205 -0.0254 -0.2469 0.3271  123 TYR   V CD1 
38629 C  CD2 . TYR   V  122 ? 1.6882 0.7673 1.5853 0.0149  -0.2576 0.2866  123 TYR   V CD2 
38630 C  CE1 . TYR   V  122 ? 1.7467 0.8969 1.6562 0.0186  -0.2951 0.3406  123 TYR   V CE1 
38631 C  CE2 . TYR   V  122 ? 1.6718 0.8603 1.6186 0.0467  -0.2880 0.3152  123 TYR   V CE2 
38632 C  CZ  . TYR   V  122 ? 1.7046 0.9243 1.6801 0.0182  -0.2734 0.3664  123 TYR   V CZ  
38633 O  OH  . TYR   V  122 ? 1.7622 1.0414 1.7104 0.0850  -0.2688 0.4109  123 TYR   V OH  
38634 N  N   . TYR   V  123 ? 1.5858 0.5194 1.4159 -0.0686 -0.2343 0.1476  124 TYR   V N   
38635 C  CA  . TYR   V  123 ? 1.5441 0.5325 1.4120 -0.0853 -0.2095 0.1674  124 TYR   V CA  
38636 C  C   . TYR   V  123 ? 1.5157 0.4703 1.4018 -0.0936 -0.2280 0.1546  124 TYR   V C   
38637 O  O   . TYR   V  123 ? 1.4633 0.4430 1.4252 -0.1201 -0.2015 0.2255  124 TYR   V O   
38638 C  CB  . TYR   V  123 ? 1.5430 0.5392 1.4139 -0.0838 -0.2125 0.1582  124 TYR   V CB  
38639 C  CG  . TYR   V  123 ? 1.5101 0.5832 1.4101 -0.0900 -0.2067 0.1490  124 TYR   V CG  
38640 C  CD1 . TYR   V  123 ? 1.5259 0.5954 1.4245 -0.0976 -0.1985 0.1734  124 TYR   V CD1 
38641 C  CD2 . TYR   V  123 ? 1.4734 0.6447 1.3959 -0.1400 -0.1886 0.1620  124 TYR   V CD2 
38642 C  CE1 . TYR   V  123 ? 1.5058 0.6328 1.4443 -0.1413 -0.1833 0.1813  124 TYR   V CE1 
38643 C  CE2 . TYR   V  123 ? 1.4744 0.6859 1.4241 -0.1532 -0.1999 0.1507  124 TYR   V CE2 
38644 C  CZ  . TYR   V  123 ? 1.5090 0.6280 1.4301 -0.1498 -0.1842 0.1666  124 TYR   V CZ  
38645 O  OH  . TYR   V  123 ? 1.5707 0.5313 1.3670 -0.1421 -0.1338 0.1632  124 TYR   V OH  
38646 N  N   . LEU   V  124 ? 1.5466 0.4460 1.3987 -0.0686 -0.1958 0.1051  125 LEU   V N   
38647 C  CA  . LEU   V  124 ? 1.5763 0.4692 1.3916 -0.0606 -0.1608 0.0459  125 LEU   V CA  
38648 C  C   . LEU   V  124 ? 1.5883 0.4364 1.3730 -0.0566 -0.1632 0.0033  125 LEU   V C   
38649 O  O   . LEU   V  124 ? 1.6070 0.4382 1.4307 -0.1160 -0.1192 -0.0371 125 LEU   V O   
38650 C  CB  . LEU   V  124 ? 1.5997 0.4674 1.3850 -0.0282 -0.1844 0.0754  125 LEU   V CB  
38651 C  CG  . LEU   V  124 ? 1.6341 0.4763 1.3969 -0.0364 -0.1916 0.0958  125 LEU   V CG  
38652 C  CD1 . LEU   V  124 ? 1.6687 0.5217 1.3988 -0.0006 -0.1855 0.0730  125 LEU   V CD1 
38653 C  CD2 . LEU   V  124 ? 1.6448 0.4385 1.3799 -0.0353 -0.1802 0.0700  125 LEU   V CD2 
38654 N  N   . SER   V  125 ? 1.5932 0.4299 1.3873 -0.0831 -0.1308 -0.0423 126 SER   V N   
38655 C  CA  . SER   V  125 ? 1.5728 0.4551 1.3821 -0.0968 -0.1334 -0.0501 126 SER   V CA  
38656 C  C   . SER   V  125 ? 1.5317 0.4205 1.3831 -0.1282 -0.1560 -0.0941 126 SER   V C   
38657 O  O   . SER   V  125 ? 1.5411 0.4087 1.3957 -0.1473 -0.1500 -0.1395 126 SER   V O   
38658 C  CB  . SER   V  125 ? 1.5599 0.4557 1.4307 -0.0982 -0.1305 -0.0388 126 SER   V CB  
38659 O  OG  . SER   V  125 ? 1.5636 0.4592 1.4554 -0.1089 -0.1213 -0.0339 126 SER   V OG  
38660 N  N   . LEU   V  126 ? 1.5945 0.4833 1.3584 -0.0704 -0.1131 -0.0524 127 LEU   V N   
38661 C  CA  . LEU   V  126 ? 1.5948 0.5023 1.3983 -0.0400 -0.0951 -0.0287 127 LEU   V CA  
38662 C  C   . LEU   V  126 ? 1.5924 0.4307 1.3844 -0.0382 -0.0857 -0.0615 127 LEU   V C   
38663 O  O   . LEU   V  126 ? 1.5916 0.3880 1.4149 -0.0450 -0.0611 -0.1447 127 LEU   V O   
38664 C  CB  . LEU   V  126 ? 1.6450 0.4919 1.4125 0.0212  -0.1088 0.0324  127 LEU   V CB  
38665 C  CG  . LEU   V  126 ? 1.6768 0.5275 1.4266 0.0136  -0.1515 0.0697  127 LEU   V CG  
38666 C  CD1 . LEU   V  126 ? 1.6725 0.4616 1.4416 -0.0159 -0.1363 0.0390  127 LEU   V CD1 
38667 C  CD2 . LEU   V  126 ? 1.7486 0.5478 1.4503 0.0539  -0.1624 0.0249  127 LEU   V CD2 
38668 N  N   . GLY   V  127 ? 1.5987 0.3959 1.3619 -0.0335 -0.0964 -0.0645 128 GLY   V N   
38669 C  CA  . GLY   V  127 ? 1.5603 0.4840 1.3772 -0.0315 -0.1014 -0.0359 128 GLY   V CA  
38670 C  C   . GLY   V  127 ? 1.4746 0.4686 1.3641 -0.0137 -0.1205 0.0316  128 GLY   V C   
38671 O  O   . GLY   V  127 ? 1.3953 0.5124 1.3451 -0.0270 -0.1209 0.0488  128 GLY   V O   
38672 N  N   . SER   V  128 ? 1.4124 0.5274 1.4297 -0.0131 -0.1105 0.0983  129 SER   V N   
38673 C  CA  . SER   V  128 ? 1.3608 0.5270 1.4437 -0.0608 -0.1376 0.0465  129 SER   V CA  
38674 C  C   . SER   V  128 ? 1.3071 0.5492 1.4547 -0.0855 -0.1498 0.0414  129 SER   V C   
38675 O  O   . SER   V  128 ? 1.3088 0.5398 1.5425 -0.0382 -0.2558 0.0453  129 SER   V O   
38676 C  CB  . SER   V  128 ? 1.3075 0.5055 1.4615 -0.0277 -0.1288 0.0674  129 SER   V CB  
38677 O  OG  . SER   V  128 ? 1.2466 0.4998 1.4392 0.0203  -0.1217 0.1545  129 SER   V OG  
38678 N  N   . GLY   V  129 ? 1.3312 0.5322 1.4365 -0.1093 -0.1496 0.0029  130 GLY   V N   
38679 C  CA  . GLY   V  129 ? 1.3509 0.5305 1.4245 -0.1289 -0.1336 0.0086  130 GLY   V CA  
38680 C  C   . GLY   V  129 ? 1.3763 0.4812 1.4261 -0.1378 -0.1294 0.0024  130 GLY   V C   
38681 O  O   . GLY   V  129 ? 1.4477 0.4535 1.4171 -0.1696 -0.0893 0.0015  130 GLY   V O   
38682 N  N   . SER   V  130 ? 1.3742 0.4366 1.4325 -0.1491 -0.1254 0.0166  131 SER   V N   
38683 C  CA  . SER   V  130 ? 1.4114 0.5184 1.3984 -0.1647 -0.1113 0.0110  131 SER   V CA  
38684 C  C   . SER   V  130 ? 1.4004 0.4886 1.3710 -0.1416 -0.1103 0.0358  131 SER   V C   
38685 O  O   . SER   V  130 ? 1.4074 0.4750 1.3687 -0.1769 -0.0897 -0.0024 131 SER   V O   
38686 C  CB  . SER   V  130 ? 1.3834 0.6145 1.4519 -0.1720 -0.0897 0.0072  131 SER   V CB  
38687 O  OG  . SER   V  130 ? 1.3849 0.6439 1.4892 -0.1859 -0.0701 -0.0117 131 SER   V OG  
38688 N  N   . LEU   V  131 ? 1.4226 0.4705 1.3306 -0.1176 -0.1297 0.0376  132 LEU   V N   
38689 C  CA  . LEU   V  131 ? 1.4699 0.4572 1.3544 -0.1103 -0.1494 0.0325  132 LEU   V CA  
38690 C  C   . LEU   V  131 ? 1.4810 0.3730 1.3163 -0.0950 -0.1745 0.0359  132 LEU   V C   
38691 O  O   . LEU   V  131 ? 1.5703 0.2829 1.2760 -0.0242 -0.1892 0.1562  132 LEU   V O   
38692 C  CB  . LEU   V  131 ? 1.4242 0.5583 1.4266 -0.1764 -0.1247 -0.0009 132 LEU   V CB  
38693 C  CG  . LEU   V  131 ? 1.4306 0.6617 1.4684 -0.1554 -0.1240 -0.0346 132 LEU   V CG  
38694 C  CD1 . LEU   V  131 ? 1.4337 0.5714 1.4552 -0.2020 -0.1459 -0.0371 132 LEU   V CD1 
38695 C  CD2 . LEU   V  131 ? 1.4492 0.7038 1.5573 -0.1907 -0.0942 -0.0173 132 LEU   V CD2 
38696 N  N   . ALA   V  132 ? 1.4663 0.3899 1.3719 -0.1228 -0.2129 -0.0397 133 ALA   V N   
38697 C  CA  . ALA   V  132 ? 1.4667 0.4416 1.3472 -0.1205 -0.2172 -0.0136 133 ALA   V CA  
38698 C  C   . ALA   V  132 ? 1.5080 0.4659 1.3048 -0.0903 -0.2019 0.0222  133 ALA   V C   
38699 O  O   . ALA   V  132 ? 1.5597 0.3218 1.2102 -0.1404 -0.2336 0.0243  133 ALA   V O   
38700 C  CB  . ALA   V  132 ? 1.4919 0.4853 1.3631 -0.0989 -0.2363 -0.0100 133 ALA   V CB  
38701 N  N   . ALA   V  133 ? 1.5107 0.4600 1.3177 -0.0442 -0.1675 0.0715  134 ALA   V N   
38702 C  CA  . ALA   V  133 ? 1.4895 0.5217 1.3073 -0.0483 -0.1438 0.1119  134 ALA   V CA  
38703 C  C   . ALA   V  133 ? 1.4845 0.5161 1.2742 -0.0281 -0.0936 0.1631  134 ALA   V C   
38704 O  O   . ALA   V  133 ? 1.5072 0.5029 1.2406 -0.0144 -0.1128 0.2391  134 ALA   V O   
38705 C  CB  . ALA   V  133 ? 1.4827 0.4966 1.3407 -0.0603 -0.1610 0.1061  134 ALA   V CB  
38706 N  N   . MET   V  134 ? 1.4940 0.5023 1.2925 -0.0275 -0.1115 0.1555  135 MET   V N   
38707 C  CA  . MET   V  134 ? 1.5585 0.5182 1.2745 -0.0448 -0.1168 0.1565  135 MET   V CA  
38708 C  C   . MET   V  134 ? 1.5411 0.5247 1.2830 -0.0778 -0.0956 0.1495  135 MET   V C   
38709 O  O   . MET   V  134 ? 1.5387 0.4888 1.3033 -0.1283 -0.1081 0.1749  135 MET   V O   
38710 C  CB  . MET   V  134 ? 1.5645 0.5016 1.3049 -0.0460 -0.1213 0.1342  135 MET   V CB  
38711 C  CG  . MET   V  134 ? 1.5949 0.5505 1.3216 -0.0435 -0.1492 0.0807  135 MET   V CG  
38712 S  SD  . MET   V  134 ? 1.6751 0.5449 1.4010 -0.0255 -0.1200 0.0983  135 MET   V SD  
38713 C  CE  . MET   V  134 ? 1.6930 0.5255 1.4060 -0.0524 -0.1283 0.0949  135 MET   V CE  
38714 N  N   . ALA   V  135 ? 1.5434 0.5477 1.3420 -0.0621 -0.0929 0.1719  136 ALA   V N   
38715 C  CA  . ALA   V  135 ? 1.5433 0.6210 1.3433 -0.0575 -0.0907 0.1337  136 ALA   V CA  
38716 C  C   . ALA   V  135 ? 1.5363 0.5917 1.3553 -0.0842 -0.1119 0.1115  136 ALA   V C   
38717 O  O   . ALA   V  135 ? 1.5464 0.5858 1.3488 -0.0713 -0.1066 0.1345  136 ALA   V O   
38718 C  CB  . ALA   V  135 ? 1.5335 0.6340 1.3603 -0.0685 -0.0764 0.1588  136 ALA   V CB  
38719 N  N   . VAL   V  136 ? 1.5722 0.5318 1.4106 -0.0912 -0.1373 0.1106  137 VAL   V N   
38720 C  CA  . VAL   V  136 ? 1.5559 0.5720 1.4082 -0.0987 -0.1505 0.0820  137 VAL   V CA  
38721 C  C   . VAL   V  136 ? 1.6018 0.6199 1.3259 -0.1014 -0.1254 0.0814  137 VAL   V C   
38722 O  O   . VAL   V  136 ? 1.5955 0.6381 1.3262 -0.1627 -0.1116 -0.0144 137 VAL   V O   
38723 C  CB  . VAL   V  136 ? 1.5334 0.5773 1.4550 -0.0905 -0.1804 0.0958  137 VAL   V CB  
38724 C  CG1 . VAL   V  136 ? 1.5285 0.6278 1.4540 -0.0885 -0.1647 0.1174  137 VAL   V CG1 
38725 C  CG2 . VAL   V  136 ? 1.5480 0.5575 1.4907 -0.0891 -0.2127 0.0730  137 VAL   V CG2 
38726 N  N   . LEU   V  137 ? 1.6410 0.6424 1.3710 -0.0632 -0.1444 0.0805  138 LEU   V N   
38727 C  CA  . LEU   V  137 ? 1.6741 0.6790 1.3352 -0.0933 -0.1347 0.1203  138 LEU   V CA  
38728 C  C   . LEU   V  137 ? 1.6667 0.6864 1.2732 -0.1126 -0.0715 0.1385  138 LEU   V C   
38729 O  O   . LEU   V  137 ? 1.5678 0.7261 1.3048 -0.1503 -0.0204 0.1087  138 LEU   V O   
38730 C  CB  . LEU   V  137 ? 1.7165 0.6279 1.3315 -0.0464 -0.1765 0.1344  138 LEU   V CB  
38731 C  CG  . LEU   V  137 ? 1.7134 0.5871 1.3283 -0.0137 -0.1730 0.1314  138 LEU   V CG  
38732 C  CD1 . LEU   V  137 ? 1.6945 0.5831 1.3052 0.0146  -0.1937 0.1564  138 LEU   V CD1 
38733 C  CD2 . LEU   V  137 ? 1.7559 0.5290 1.3484 -0.0206 -0.1869 0.1410  138 LEU   V CD2 
38734 N  N   . GLU   V  138 ? 1.6743 0.7234 1.3144 -0.1300 -0.1022 0.1036  139 GLU   V N   
38735 C  CA  . GLU   V  138 ? 1.6916 0.7314 1.2973 -0.0855 -0.1187 0.1110  139 GLU   V CA  
38736 C  C   . GLU   V  138 ? 1.6601 0.7435 1.2700 -0.0666 -0.1601 0.1067  139 GLU   V C   
38737 O  O   . GLU   V  138 ? 1.7157 0.7832 1.2761 -0.0056 -0.1654 0.0187  139 GLU   V O   
38738 C  CB  . GLU   V  138 ? 1.7182 0.7192 1.3683 -0.1047 -0.1359 0.1081  139 GLU   V CB  
38739 C  CG  . GLU   V  138 ? 1.7468 0.7408 1.4267 -0.0830 -0.1267 0.1095  139 GLU   V CG  
38740 C  CD  . GLU   V  138 ? 1.7987 0.7083 1.4260 -0.1088 -0.1161 0.1466  139 GLU   V CD  
38741 O  OE1 . GLU   V  138 ? 1.7946 0.7647 1.5358 -0.1130 -0.1296 0.0701  139 GLU   V OE1 
38742 O  OE2 . GLU   V  138 ? 1.8896 0.6542 1.5309 -0.1511 -0.0198 0.1346  139 GLU   V OE2 
38743 N  N   . SER   V  139 ? 1.6441 0.7996 1.2896 -0.0979 -0.1859 0.1428  140 SER   V N   
38744 C  CA  . SER   V  139 ? 1.5914 0.8043 1.2771 -0.0910 -0.2011 0.1991  140 SER   V CA  
38745 C  C   . SER   V  139 ? 1.6271 0.7814 1.2516 -0.0868 -0.1972 0.2117  140 SER   V C   
38746 O  O   . SER   V  139 ? 1.6021 0.7599 1.2062 -0.0936 -0.2003 0.2916  140 SER   V O   
38747 C  CB  . SER   V  139 ? 1.5828 0.8040 1.3344 -0.1032 -0.1961 0.2359  140 SER   V CB  
38748 O  OG  . SER   V  139 ? 1.5634 0.7967 1.3245 -0.0779 -0.2186 0.2819  140 SER   V OG  
38749 N  N   . HIS   V  140 ? 1.6942 0.7370 1.3697 -0.0884 -0.1759 0.1990  141 HIS   V N   
38750 C  CA  . HIS   V  140 ? 1.6526 0.8802 1.4326 -0.0870 -0.1225 0.1662  141 HIS   V CA  
38751 C  C   . HIS   V  140 ? 1.6103 0.8865 1.3973 -0.0819 -0.1001 0.1615  141 HIS   V C   
38752 O  O   . HIS   V  140 ? 1.5641 0.7977 1.3296 -0.0605 -0.1245 0.1202  141 HIS   V O   
38753 C  CB  . HIS   V  140 ? 1.6551 0.8865 1.5112 -0.0587 -0.1589 0.1658  141 HIS   V CB  
38754 C  CG  . HIS   V  140 ? 1.6890 0.8559 1.6303 -0.0777 -0.1598 0.1316  141 HIS   V CG  
38755 N  ND1 . HIS   V  140 ? 1.6825 0.9069 1.6302 -0.1346 -0.1311 0.1069  141 HIS   V ND1 
38756 C  CD2 . HIS   V  140 ? 1.7799 0.8968 1.6415 -0.1107 -0.1875 0.1433  141 HIS   V CD2 
38757 C  CE1 . HIS   V  140 ? 1.7308 0.9549 1.6844 -0.0895 -0.1482 0.1231  141 HIS   V CE1 
38758 N  NE2 . HIS   V  140 ? 1.7957 0.9434 1.6923 -0.0784 -0.1526 0.1195  141 HIS   V NE2 
38759 N  N   . TRP   V  141 ? 1.6507 0.9333 1.4504 -0.0055 -0.1395 0.1296  142 TRP   V N   
38760 C  CA  . TRP   V  141 ? 1.6637 0.9058 1.4886 -0.0463 -0.1223 0.1279  142 TRP   V CA  
38761 C  C   . TRP   V  141 ? 1.6553 0.9958 1.4703 -0.0739 -0.0878 0.0717  142 TRP   V C   
38762 O  O   . TRP   V  141 ? 1.6290 1.0119 1.4867 -0.1052 -0.0605 0.0651  142 TRP   V O   
38763 C  CB  . TRP   V  141 ? 1.6380 0.9193 1.5614 -0.0223 -0.1499 0.1362  142 TRP   V CB  
38764 C  CG  . TRP   V  141 ? 1.6160 0.9201 1.6097 -0.0388 -0.1868 0.1548  142 TRP   V CG  
38765 C  CD1 . TRP   V  141 ? 1.5895 0.8464 1.6766 -0.0550 -0.1721 0.1841  142 TRP   V CD1 
38766 C  CD2 . TRP   V  141 ? 1.6356 0.8882 1.6404 -0.0124 -0.1860 0.1796  142 TRP   V CD2 
38767 N  NE1 . TRP   V  141 ? 1.5540 0.8513 1.6662 -0.0676 -0.1949 0.1772  142 TRP   V NE1 
38768 C  CE2 . TRP   V  141 ? 1.5890 0.8723 1.6198 -0.0337 -0.1959 0.2010  142 TRP   V CE2 
38769 C  CE3 . TRP   V  141 ? 1.6830 0.9665 1.6083 0.0089  -0.2036 0.1901  142 TRP   V CE3 
38770 C  CZ2 . TRP   V  141 ? 1.6303 0.8387 1.6277 -0.0079 -0.1719 0.2148  142 TRP   V CZ2 
38771 C  CZ3 . TRP   V  141 ? 1.6955 0.8714 1.6490 0.0184  -0.1675 0.2086  142 TRP   V CZ3 
38772 C  CH2 . TRP   V  141 ? 1.6525 0.8610 1.6027 0.0368  -0.1959 0.2305  142 TRP   V CH2 
38773 N  N   . LYS   V  142 ? 1.6699 1.0188 1.4431 -0.0961 -0.1078 0.0759  143 LYS   V N   
38774 C  CA  . LYS   V  142 ? 1.6949 1.0249 1.4562 -0.0766 -0.1338 0.0934  143 LYS   V CA  
38775 C  C   . LYS   V  142 ? 1.7777 1.0108 1.4707 -0.1144 -0.1563 0.1523  143 LYS   V C   
38776 O  O   . LYS   V  142 ? 1.8617 1.0043 1.3870 -0.1166 -0.2024 0.2370  143 LYS   V O   
38777 C  CB  . LYS   V  142 ? 1.6975 1.0755 1.4584 -0.1018 -0.1144 0.0830  143 LYS   V CB  
38778 C  CG  . LYS   V  142 ? 1.7110 1.0682 1.4901 -0.1539 -0.0775 0.0399  143 LYS   V CG  
38779 C  CD  . LYS   V  142 ? 1.7162 1.1230 1.5214 -0.1944 -0.0585 0.0123  143 LYS   V CD  
38780 C  CE  . LYS   V  142 ? 1.6929 1.1227 1.5720 -0.2304 -0.0517 -0.0080 143 LYS   V CE  
38781 N  NZ  . LYS   V  142 ? 1.7050 1.0764 1.6219 -0.2051 -0.0319 0.0197  143 LYS   V NZ  
38782 N  N   . GLN   V  143 ? 1.8230 1.0910 1.4974 -0.0661 -0.1685 0.1669  144 GLN   V N   
38783 C  CA  . GLN   V  143 ? 1.8908 1.1395 1.5835 0.0536  -0.1606 0.2080  144 GLN   V CA  
38784 C  C   . GLN   V  143 ? 1.9035 1.0494 1.5434 0.0467  -0.2020 0.1850  144 GLN   V C   
38785 O  O   . GLN   V  143 ? 1.9079 1.3020 1.5201 0.0917  -0.1736 0.1465  144 GLN   V O   
38786 C  CB  . GLN   V  143 ? 1.9229 1.2560 1.5983 0.0522  -0.1718 0.2296  144 GLN   V CB  
38787 C  CG  . GLN   V  143 ? 2.0049 1.2838 1.6417 0.0680  -0.1986 0.2761  144 GLN   V CG  
38788 C  CD  . GLN   V  143 ? 1.9824 1.3214 1.6232 0.0486  -0.2239 0.2633  144 GLN   V CD  
38789 O  OE1 . GLN   V  143 ? 2.0674 1.2628 1.5186 -0.0571 -0.3666 0.2689  144 GLN   V OE1 
38790 N  NE2 . GLN   V  143 ? 2.1369 1.3460 1.5750 0.0633  -0.1858 0.2657  144 GLN   V NE2 
38791 N  N   . ASP   V  144 ? 1.9058 0.9953 1.5354 0.0942  -0.1870 0.2117  145 ASP   V N   
38792 C  CA  . ASP   V  144 ? 1.9420 0.8923 1.6195 0.1003  -0.1513 0.1542  145 ASP   V CA  
38793 C  C   . ASP   V  144 ? 1.8596 0.7387 1.6248 0.1019  -0.0671 0.1497  145 ASP   V C   
38794 O  O   . ASP   V  144 ? 1.9124 0.6617 1.6764 0.1019  -0.0110 0.1278  145 ASP   V O   
38795 C  CB  . ASP   V  144 ? 2.0362 0.9590 1.6216 0.0944  -0.1367 0.1129  145 ASP   V CB  
38796 C  CG  . ASP   V  144 ? 2.1359 0.9848 1.6420 0.1020  -0.1854 0.1184  145 ASP   V CG  
38797 O  OD1 . ASP   V  144 ? 2.2317 0.9670 1.7298 0.0613  -0.1454 0.0993  145 ASP   V OD1 
38798 O  OD2 . ASP   V  144 ? 2.3481 1.0019 1.6645 0.0892  -0.1515 0.0296  145 ASP   V OD2 
38799 N  N   . LEU   V  145 ? 1.8185 0.6632 1.6303 0.0792  -0.0651 0.1667  146 LEU   V N   
38800 C  CA  . LEU   V  145 ? 1.7946 0.7008 1.6091 0.0118  -0.0686 0.1736  146 LEU   V CA  
38801 C  C   . LEU   V  145 ? 1.8354 0.6586 1.5835 0.0104  -0.0523 0.1898  146 LEU   V C   
38802 O  O   . LEU   V  145 ? 1.8538 0.5715 1.5385 -0.0704 -0.0672 0.1980  146 LEU   V O   
38803 C  CB  . LEU   V  145 ? 1.7778 0.7970 1.6254 0.0032  -0.0662 0.2003  146 LEU   V CB  
38804 C  CG  . LEU   V  145 ? 1.7537 0.8109 1.6440 -0.0066 -0.0673 0.2482  146 LEU   V CG  
38805 C  CD1 . LEU   V  145 ? 1.7480 0.9184 1.6296 0.0164  -0.0722 0.2357  146 LEU   V CD1 
38806 C  CD2 . LEU   V  145 ? 1.7588 0.8195 1.6757 0.0081  -0.0418 0.2609  146 LEU   V CD2 
38807 N  N   . THR   V  146 ? 1.8175 0.6192 1.6014 -0.0410 -0.0449 0.1646  147 THR   V N   
38808 C  CA  . THR   V  146 ? 1.8233 0.6902 1.6651 -0.0835 -0.0462 0.1472  147 THR   V CA  
38809 C  C   . THR   V  146 ? 1.8209 0.8194 1.6725 -0.1557 -0.0489 0.1625  147 THR   V C   
38810 O  O   . THR   V  146 ? 1.8273 0.7913 1.6803 -0.1901 -0.0428 0.1058  147 THR   V O   
38811 C  CB  . THR   V  146 ? 1.8333 0.6634 1.6307 -0.0935 -0.0316 0.1267  147 THR   V CB  
38812 O  OG1 . THR   V  146 ? 1.8298 0.6020 1.6767 -0.1231 -0.0256 0.1016  147 THR   V OG1 
38813 C  CG2 . THR   V  146 ? 1.8313 0.6885 1.6265 -0.0718 -0.0364 0.1481  147 THR   V CG2 
38814 N  N   . LYS   V  147 ? 1.7987 0.9683 1.8096 -0.2528 -0.0813 0.1180  148 LYS   V N   
38815 C  CA  . LYS   V  147 ? 1.7940 1.0258 1.8138 -0.2673 -0.0267 0.1292  148 LYS   V CA  
38816 C  C   . LYS   V  147 ? 1.8007 1.0413 1.8843 -0.3060 -0.0367 0.2002  148 LYS   V C   
38817 O  O   . LYS   V  147 ? 1.7898 1.1291 1.8500 -0.2329 -0.0498 0.2597  148 LYS   V O   
38818 C  CB  . LYS   V  147 ? 1.8008 1.0215 1.8558 -0.2393 -0.0026 0.0576  148 LYS   V CB  
38819 C  CG  . LYS   V  147 ? 1.7602 1.0601 1.8576 -0.2412 0.0148  0.0182  148 LYS   V CG  
38820 C  CD  . LYS   V  147 ? 1.6908 1.1658 1.8558 -0.2419 0.0076  -0.0356 148 LYS   V CD  
38821 C  CE  . LYS   V  147 ? 1.6248 1.2270 1.8612 -0.2565 0.0201  -0.0767 148 LYS   V CE  
38822 N  NZ  . LYS   V  147 ? 1.6057 1.2900 1.9042 -0.2662 0.0373  -0.1271 148 LYS   V NZ  
38823 N  N   . GLU   V  148 ? 1.7780 0.9791 1.9284 -0.3236 -0.0433 0.2348  149 GLU   V N   
38824 C  CA  . GLU   V  148 ? 1.7948 0.9219 1.9091 -0.3305 -0.0470 0.1900  149 GLU   V CA  
38825 C  C   . GLU   V  148 ? 1.7956 0.8955 1.7396 -0.2456 -0.1012 0.1019  149 GLU   V C   
38826 O  O   . GLU   V  148 ? 1.7645 0.6435 1.7157 -0.3195 -0.1861 -0.0622 149 GLU   V O   
38827 C  CB  . GLU   V  148 ? 1.8073 1.0545 2.0245 -0.3438 -0.0116 0.2332  149 GLU   V CB  
38828 C  CG  . GLU   V  148 ? 1.7962 1.2420 2.1095 -0.4184 -0.0662 0.2089  149 GLU   V CG  
38829 C  CD  . GLU   V  148 ? 1.8918 1.3514 2.1717 -0.3895 -0.1120 0.3317  149 GLU   V CD  
38830 O  OE1 . GLU   V  148 ? 1.9731 1.5140 2.2163 -0.4832 -0.2185 0.2934  149 GLU   V OE1 
38831 O  OE2 . GLU   V  148 ? 1.9430 1.6031 2.1478 -0.4125 -0.0550 0.4996  149 GLU   V OE2 
38832 N  N   . GLU   V  149 ? 1.8142 0.7910 1.6658 -0.1744 -0.0680 0.1195  150 GLU   V N   
38833 C  CA  . GLU   V  149 ? 1.7890 0.7434 1.6214 -0.1539 -0.0399 0.1729  150 GLU   V CA  
38834 C  C   . GLU   V  149 ? 1.7464 0.6992 1.5972 -0.1027 -0.0657 0.2140  150 GLU   V C   
38835 O  O   . GLU   V  149 ? 1.7342 0.8424 1.4427 -0.1423 -0.0171 0.3097  150 GLU   V O   
38836 C  CB  . GLU   V  149 ? 1.7982 0.7218 1.6019 -0.1335 -0.0165 0.1551  150 GLU   V CB  
38837 C  CG  . GLU   V  149 ? 1.8164 0.7478 1.5623 -0.1481 -0.0219 0.1227  150 GLU   V CG  
38838 C  CD  . GLU   V  149 ? 1.7813 0.7323 1.5427 -0.1301 -0.0072 0.0674  150 GLU   V CD  
38839 O  OE1 . GLU   V  149 ? 1.7288 0.7878 1.4994 -0.0869 -0.0414 -0.0250 150 GLU   V OE1 
38840 O  OE2 . GLU   V  149 ? 1.8163 0.7655 1.4999 -0.1741 0.0067  0.0518  150 GLU   V OE2 
38841 N  N   . ALA   V  150 ? 1.6683 0.6752 1.6118 -0.1229 -0.0881 0.2532  151 ALA   V N   
38842 C  CA  . ALA   V  150 ? 1.6379 0.6547 1.6028 -0.1477 -0.1146 0.2608  151 ALA   V CA  
38843 C  C   . ALA   V  150 ? 1.6015 0.6033 1.6327 -0.1166 -0.1844 0.2479  151 ALA   V C   
38844 O  O   . ALA   V  150 ? 1.6211 0.6220 1.6911 -0.1280 -0.2029 0.2939  151 ALA   V O   
38845 C  CB  . ALA   V  150 ? 1.6824 0.6546 1.6437 -0.1386 -0.1042 0.2407  151 ALA   V CB  
38846 N  N   . ILE   V  151 ? 1.5599 0.6552 1.6347 -0.1199 -0.1458 0.2266  152 ILE   V N   
38847 C  CA  . ILE   V  151 ? 1.5208 0.7422 1.6267 -0.0965 -0.1592 0.1767  152 ILE   V CA  
38848 C  C   . ILE   V  151 ? 1.5267 0.7612 1.5342 -0.0180 -0.1634 0.1115  152 ILE   V C   
38849 O  O   . ILE   V  151 ? 1.5127 0.7441 1.4239 0.0907  -0.1752 0.0671  152 ILE   V O   
38850 C  CB  . ILE   V  151 ? 1.5061 0.8213 1.6755 -0.1083 -0.1760 0.1747  152 ILE   V CB  
38851 C  CG1 . ILE   V  151 ? 1.5116 0.8303 1.6836 -0.0914 -0.2057 0.1264  152 ILE   V CG1 
38852 C  CG2 . ILE   V  151 ? 1.4674 0.8015 1.6885 -0.1262 -0.1800 0.1829  152 ILE   V CG2 
38853 C  CD1 . ILE   V  151 ? 1.5125 0.8446 1.6987 -0.0981 -0.2236 0.1120  152 ILE   V CD1 
38854 N  N   . LYS   V  152 ? 1.5532 0.7752 1.5229 -0.0045 -0.1500 0.1268  153 LYS   V N   
38855 C  CA  . LYS   V  152 ? 1.5297 0.7689 1.4914 -0.0150 -0.1445 0.1547  153 LYS   V CA  
38856 C  C   . LYS   V  152 ? 1.5816 0.6244 1.4345 -0.0223 -0.1212 0.1517  153 LYS   V C   
38857 O  O   . LYS   V  152 ? 1.4398 0.5770 1.4082 -0.1197 -0.1493 0.1099  153 LYS   V O   
38858 C  CB  . LYS   V  152 ? 1.5786 0.8449 1.5076 0.0130  -0.1201 0.1558  153 LYS   V CB  
38859 C  CG  . LYS   V  152 ? 1.5611 0.9130 1.5353 0.0354  -0.0897 0.1512  153 LYS   V CG  
38860 C  CD  . LYS   V  152 ? 1.6105 0.9179 1.5794 0.0261  -0.0490 0.1914  153 LYS   V CD  
38861 C  CE  . LYS   V  152 ? 1.6222 0.9574 1.6522 0.0663  -0.0200 0.2106  153 LYS   V CE  
38862 N  NZ  . LYS   V  152 ? 1.6343 0.9785 1.7117 0.0621  -0.0226 0.1585  153 LYS   V NZ  
38863 N  N   . LEU   V  153 ? 1.5308 0.5616 1.4390 -0.0377 -0.1016 0.1140  154 LEU   V N   
38864 C  CA  . LEU   V  153 ? 1.5328 0.5759 1.4348 -0.0463 -0.0854 0.1261  154 LEU   V CA  
38865 C  C   . LEU   V  153 ? 1.5473 0.6064 1.4581 -0.0207 -0.0675 0.1336  154 LEU   V C   
38866 O  O   . LEU   V  153 ? 1.5833 0.6389 1.5058 -0.0712 -0.0643 0.1224  154 LEU   V O   
38867 C  CB  . LEU   V  153 ? 1.5323 0.5956 1.3957 -0.0409 -0.0816 0.0993  154 LEU   V CB  
38868 C  CG  . LEU   V  153 ? 1.5329 0.6279 1.3911 -0.0469 -0.0780 0.1131  154 LEU   V CG  
38869 C  CD1 . LEU   V  153 ? 1.5555 0.6260 1.3881 -0.0676 -0.0816 0.1147  154 LEU   V CD1 
38870 C  CD2 . LEU   V  153 ? 1.5403 0.6481 1.3964 -0.0445 -0.0734 0.1257  154 LEU   V CD2 
38871 N  N   . ALA   V  154 ? 1.5585 0.5869 1.5244 -0.0388 -0.0678 0.1405  155 ALA   V N   
38872 C  CA  . ALA   V  154 ? 1.5693 0.7137 1.5262 -0.0447 -0.0754 0.1108  155 ALA   V CA  
38873 C  C   . ALA   V  154 ? 1.5766 0.7297 1.5680 0.0067  -0.0971 0.0979  155 ALA   V C   
38874 O  O   . ALA   V  154 ? 1.5483 0.8246 1.6008 0.0182  -0.0442 0.0895  155 ALA   V O   
38875 C  CB  . ALA   V  154 ? 1.5659 0.7393 1.5324 -0.0962 -0.1043 0.0616  155 ALA   V CB  
38876 N  N   . SER   V  155 ? 1.5642 0.7750 1.5806 -0.0292 -0.0456 0.0530  156 SER   V N   
38877 C  CA  . SER   V  155 ? 1.5425 0.8741 1.5220 -0.0343 -0.0393 0.0241  156 SER   V CA  
38878 C  C   . SER   V  155 ? 1.6260 0.8511 1.5133 0.0338  -0.0470 0.1031  156 SER   V C   
38879 O  O   . SER   V  155 ? 1.6920 0.7518 1.4921 0.1195  -0.1374 0.0709  156 SER   V O   
38880 C  CB  . SER   V  155 ? 1.5112 0.9648 1.4959 -0.0493 0.0525  -0.0213 156 SER   V CB  
38881 O  OG  . SER   V  155 ? 1.4085 1.1015 1.5571 -0.1087 0.0798  -0.0513 156 SER   V OG  
38882 N  N   . ASP   V  156 ? 1.6061 0.8747 1.5158 0.0736  -0.0199 0.1072  157 ASP   V N   
38883 C  CA  . ASP   V  156 ? 1.4738 0.8492 1.5210 0.0548  -0.0277 0.1682  157 ASP   V CA  
38884 C  C   . ASP   V  156 ? 1.4394 0.8028 1.4546 0.0252  -0.1154 0.1640  157 ASP   V C   
38885 O  O   . ASP   V  156 ? 1.2618 0.7990 1.3899 -0.0282 -0.1487 0.1427  157 ASP   V O   
38886 C  CB  . ASP   V  156 ? 1.5334 0.8487 1.5285 0.0826  0.0000  0.1766  157 ASP   V CB  
38887 C  CG  . ASP   V  156 ? 1.5724 0.8781 1.5514 0.0963  0.0721  0.2068  157 ASP   V CG  
38888 O  OD1 . ASP   V  156 ? 1.5229 0.8895 1.5869 0.0916  0.0584  0.3194  157 ASP   V OD1 
38889 O  OD2 . ASP   V  156 ? 1.6367 0.9010 1.5644 0.0857  0.0729  0.1663  157 ASP   V OD2 
38890 N  N   . ALA   V  157 ? 1.3991 0.8220 1.4292 -0.0014 -0.1311 0.1656  158 ALA   V N   
38891 C  CA  . ALA   V  157 ? 1.3980 0.8327 1.4186 0.0235  -0.1191 0.1569  158 ALA   V CA  
38892 C  C   . ALA   V  157 ? 1.4016 0.8029 1.4091 0.0359  -0.1688 0.1602  158 ALA   V C   
38893 O  O   . ALA   V  157 ? 1.3827 0.7523 1.4129 0.0714  -0.2066 0.1904  158 ALA   V O   
38894 C  CB  . ALA   V  157 ? 1.3860 0.8576 1.3887 0.0385  -0.1038 0.1520  158 ALA   V CB  
38895 N  N   . ILE   V  158 ? 1.4303 0.8195 1.4332 0.0282  -0.1977 0.1569  159 ILE   V N   
38896 C  CA  . ILE   V  158 ? 1.4736 0.8082 1.4363 0.0088  -0.2229 0.1200  159 ILE   V CA  
38897 C  C   . ILE   V  158 ? 1.4849 0.7728 1.4775 0.0007  -0.2299 0.0923  159 ILE   V C   
38898 O  O   . ILE   V  158 ? 1.4426 0.7106 1.4691 -0.0717 -0.2664 0.0498  159 ILE   V O   
38899 C  CB  . ILE   V  158 ? 1.4666 0.7815 1.4719 -0.0173 -0.2155 0.1619  159 ILE   V CB  
38900 C  CG1 . ILE   V  158 ? 1.5038 0.7557 1.4454 -0.0297 -0.2194 0.1644  159 ILE   V CG1 
38901 C  CG2 . ILE   V  158 ? 1.4412 0.7971 1.4787 -0.0263 -0.2381 0.1507  159 ILE   V CG2 
38902 C  CD1 . ILE   V  158 ? 1.5094 0.7387 1.4218 -0.0170 -0.2197 0.1712  159 ILE   V CD1 
38903 N  N   . GLN   V  159 ? 1.5072 0.7755 1.5093 0.0052  -0.2116 0.0627  160 GLN   V N   
38904 C  CA  . GLN   V  159 ? 1.5352 0.7634 1.5376 0.0180  -0.1830 0.0689  160 GLN   V CA  
38905 C  C   . GLN   V  159 ? 1.5160 0.7421 1.5796 0.0450  -0.2058 0.0976  160 GLN   V C   
38906 O  O   . GLN   V  159 ? 1.5597 0.8016 1.6569 0.0565  -0.1985 0.1613  160 GLN   V O   
38907 C  CB  . GLN   V  159 ? 1.5383 0.7530 1.5500 -0.0023 -0.1676 0.0736  160 GLN   V CB  
38908 C  CG  . GLN   V  159 ? 1.5301 0.8352 1.5597 -0.0021 -0.1728 0.0410  160 GLN   V CG  
38909 C  CD  . GLN   V  159 ? 1.5535 0.8521 1.5939 0.0470  -0.1744 0.0425  160 GLN   V CD  
38910 O  OE1 . GLN   V  159 ? 1.6470 0.7169 1.6267 -0.0348 -0.1726 0.0116  160 GLN   V OE1 
38911 N  NE2 . GLN   V  159 ? 1.5419 0.9986 1.6043 -0.0384 -0.1340 0.0209  160 GLN   V NE2 
38912 N  N   . ALA   V  160 ? 1.4883 0.7163 1.5552 0.0236  -0.1796 0.0948  161 ALA   V N   
38913 C  CA  . ALA   V  160 ? 1.5346 0.6613 1.5280 0.0216  -0.1394 0.1050  161 ALA   V CA  
38914 C  C   . ALA   V  160 ? 1.5479 0.5890 1.5197 0.0090  -0.1528 0.1193  161 ALA   V C   
38915 O  O   . ALA   V  160 ? 1.5789 0.6196 1.6155 -0.0128 -0.1674 0.1692  161 ALA   V O   
38916 C  CB  . ALA   V  160 ? 1.5157 0.6868 1.5011 0.0291  -0.1111 0.0898  161 ALA   V CB  
38917 N  N   . GLY   V  161 ? 1.6094 0.5554 1.4875 -0.0168 -0.1489 0.1120  162 GLY   V N   
38918 C  CA  . GLY   V  161 ? 1.5969 0.4976 1.4699 -0.0119 -0.1649 0.1028  162 GLY   V CA  
38919 C  C   . GLY   V  161 ? 1.5683 0.4508 1.4966 -0.0174 -0.1753 0.1105  162 GLY   V C   
38920 O  O   . GLY   V  161 ? 1.5860 0.4551 1.4609 -0.0400 -0.1812 0.0893  162 GLY   V O   
38921 N  N   . ILE   V  162 ? 1.5389 0.5101 1.4926 -0.0073 -0.1951 0.1313  163 ILE   V N   
38922 C  CA  . ILE   V  162 ? 1.5478 0.5473 1.4982 -0.0268 -0.1961 0.1650  163 ILE   V CA  
38923 C  C   . ILE   V  162 ? 1.5366 0.5437 1.4620 -0.0191 -0.2136 0.1291  163 ILE   V C   
38924 O  O   . ILE   V  162 ? 1.5390 0.2782 1.4874 0.0397  -0.2532 0.1077  163 ILE   V O   
38925 C  CB  . ILE   V  162 ? 1.5441 0.6684 1.5415 -0.0595 -0.1858 0.1803  163 ILE   V CB  
38926 C  CG1 . ILE   V  162 ? 1.6088 0.6827 1.5846 -0.0558 -0.1792 0.1490  163 ILE   V CG1 
38927 C  CG2 . ILE   V  162 ? 1.5209 0.6585 1.5352 -0.0731 -0.1767 0.1959  163 ILE   V CG2 
38928 C  CD1 . ILE   V  162 ? 1.6374 0.7308 1.5942 -0.0881 -0.1817 0.1541  163 ILE   V CD1 
38929 N  N   . TRP   V  163 ? 1.5044 0.5433 1.3927 -0.0400 -0.2296 0.1721  164 TRP   V N   
38930 C  CA  . TRP   V  163 ? 1.4714 0.5597 1.3882 -0.0174 -0.2373 0.1879  164 TRP   V CA  
38931 C  C   . TRP   V  163 ? 1.4639 0.5939 1.4171 -0.0272 -0.2433 0.1766  164 TRP   V C   
38932 O  O   . TRP   V  163 ? 1.4344 0.5323 1.4862 -0.0472 -0.2457 0.1571  164 TRP   V O   
38933 C  CB  . TRP   V  163 ? 1.4659 0.5983 1.3664 -0.0133 -0.2469 0.2057  164 TRP   V CB  
38934 C  CG  . TRP   V  163 ? 1.4646 0.6169 1.3771 -0.0245 -0.2655 0.1929  164 TRP   V CG  
38935 C  CD1 . TRP   V  163 ? 1.4719 0.6557 1.3874 -0.0232 -0.2519 0.2059  164 TRP   V CD1 
38936 C  CD2 . TRP   V  163 ? 1.4880 0.7148 1.3802 -0.0483 -0.2683 0.1688  164 TRP   V CD2 
38937 N  NE1 . TRP   V  163 ? 1.4387 0.7763 1.3779 -0.0292 -0.2579 0.2153  164 TRP   V NE1 
38938 C  CE2 . TRP   V  163 ? 1.4912 0.7734 1.3620 -0.0388 -0.2523 0.2041  164 TRP   V CE2 
38939 C  CE3 . TRP   V  163 ? 1.5233 0.7372 1.3548 -0.0892 -0.2339 0.1539  164 TRP   V CE3 
38940 C  CZ2 . TRP   V  163 ? 1.5179 0.8337 1.3774 -0.0620 -0.2498 0.1625  164 TRP   V CZ2 
38941 C  CZ3 . TRP   V  163 ? 1.5316 0.8462 1.3784 -0.0896 -0.2474 0.1320  164 TRP   V CZ3 
38942 C  CH2 . TRP   V  163 ? 1.5388 0.8769 1.3674 -0.0800 -0.2397 0.1566  164 TRP   V CH2 
38943 N  N   . ASN   V  164 ? 1.4591 0.5594 1.3846 -0.0700 -0.2380 0.2067  165 ASN   V N   
38944 C  CA  . ASN   V  164 ? 1.4745 0.5538 1.3947 -0.0987 -0.1935 0.2130  165 ASN   V CA  
38945 C  C   . ASN   V  164 ? 1.4613 0.5801 1.3941 -0.1520 -0.1775 0.2272  165 ASN   V C   
38946 O  O   . ASN   V  164 ? 1.3717 0.6676 1.4247 -0.1993 -0.1419 0.1552  165 ASN   V O   
38947 C  CB  . ASN   V  164 ? 1.4801 0.5131 1.4099 -0.1214 -0.2223 0.1889  165 ASN   V CB  
38948 C  CG  . ASN   V  164 ? 1.4794 0.4738 1.4445 -0.1148 -0.2239 0.1435  165 ASN   V CG  
38949 O  OD1 . ASN   V  164 ? 1.4424 0.5404 1.4228 -0.1486 -0.2067 0.1381  165 ASN   V OD1 
38950 N  ND2 . ASN   V  164 ? 1.4740 0.4498 1.4129 -0.1265 -0.2166 0.1021  165 ASN   V ND2 
38951 N  N   . ASP   V  165 ? 1.4837 0.5409 1.3702 -0.1621 -0.1868 0.2824  166 ASP   V N   
38952 C  CA  . ASP   V  165 ? 1.4727 0.5464 1.3641 -0.1672 -0.1993 0.2937  166 ASP   V CA  
38953 C  C   . ASP   V  165 ? 1.5129 0.4673 1.3919 -0.1545 -0.2347 0.2550  166 ASP   V C   
38954 O  O   . ASP   V  165 ? 1.5658 0.2639 1.3736 -0.1356 -0.1815 0.2697  166 ASP   V O   
38955 C  CB  . ASP   V  165 ? 1.4559 0.5997 1.3098 -0.1550 -0.2629 0.3064  166 ASP   V CB  
38956 C  CG  . ASP   V  165 ? 1.4901 0.6742 1.2562 -0.1589 -0.2700 0.2935  166 ASP   V CG  
38957 O  OD1 . ASP   V  165 ? 1.5613 0.6695 1.1958 -0.1365 -0.3223 0.3814  166 ASP   V OD1 
38958 O  OD2 . ASP   V  165 ? 1.5147 0.6027 1.2587 -0.2688 -0.2797 0.3590  166 ASP   V OD2 
38959 N  N   . LEU   V  166 ? 1.5187 0.5197 1.3888 -0.1598 -0.2199 0.2434  167 LEU   V N   
38960 C  CA  . LEU   V  166 ? 1.5200 0.5181 1.4282 -0.1233 -0.2982 0.1907  167 LEU   V CA  
38961 C  C   . LEU   V  166 ? 1.5323 0.4630 1.4819 -0.1568 -0.3516 0.1923  167 LEU   V C   
38962 O  O   . LEU   V  166 ? 1.5192 0.3319 1.6056 -0.2431 -0.3853 0.1154  167 LEU   V O   
38963 C  CB  . LEU   V  166 ? 1.5018 0.5140 1.4343 -0.1060 -0.2992 0.2010  167 LEU   V CB  
38964 C  CG  . LEU   V  166 ? 1.4954 0.5124 1.4464 -0.0928 -0.3133 0.1986  167 LEU   V CG  
38965 C  CD1 . LEU   V  166 ? 1.4932 0.5003 1.4461 -0.0772 -0.3223 0.2061  167 LEU   V CD1 
38966 C  CD2 . LEU   V  166 ? 1.4922 0.4989 1.4161 -0.0987 -0.3110 0.1825  167 LEU   V CD2 
38967 N  N   . GLY   V  167 ? 1.5740 0.4656 1.4577 -0.1332 -0.3447 0.2081  168 GLY   V N   
38968 C  CA  . GLY   V  167 ? 1.5695 0.4377 1.4080 -0.1415 -0.3335 0.2492  168 GLY   V CA  
38969 C  C   . GLY   V  167 ? 1.5955 0.3386 1.3912 -0.0997 -0.3011 0.2765  168 GLY   V C   
38970 O  O   . GLY   V  167 ? 1.6698 0.2933 1.4388 -0.1982 -0.2782 0.2887  168 GLY   V O   
38971 N  N   . SER   V  168 ? 1.5848 0.3357 1.3891 -0.0096 -0.3140 0.2925  169 SER   V N   
38972 C  CA  . SER   V  168 ? 1.5267 0.3739 1.3761 0.0189  -0.2971 0.2947  169 SER   V CA  
38973 C  C   . SER   V  168 ? 1.5109 0.5107 1.3491 0.0235  -0.3096 0.3446  169 SER   V C   
38974 O  O   . SER   V  168 ? 1.4916 0.5582 1.2741 0.0225  -0.3172 0.2650  169 SER   V O   
38975 C  CB  . SER   V  168 ? 1.6053 0.4638 1.3532 -0.0042 -0.2787 0.2469  169 SER   V CB  
38976 O  OG  . SER   V  168 ? 1.6215 0.5555 1.3871 -0.0428 -0.3018 0.1957  169 SER   V OG  
38977 N  N   . GLY   V  169 ? 1.5009 0.3586 1.3672 0.0873  -0.2852 0.3351  170 GLY   V N   
38978 C  CA  . GLY   V  169 ? 1.4925 0.4223 1.4357 0.0893  -0.2726 0.3027  170 GLY   V CA  
38979 C  C   . GLY   V  169 ? 1.4786 0.4890 1.4692 0.0686  -0.2552 0.2606  170 GLY   V C   
38980 O  O   . GLY   V  169 ? 1.4595 0.5271 1.5204 0.1410  -0.2207 0.2458  170 GLY   V O   
38981 N  N   . SER   V  170 ? 1.4584 0.5548 1.4809 0.0404  -0.2556 0.2210  171 SER   V N   
38982 C  CA  . SER   V  170 ? 1.5119 0.5339 1.4865 0.0219  -0.2349 0.1684  171 SER   V CA  
38983 C  C   . SER   V  170 ? 1.5489 0.5396 1.5033 -0.0186 -0.2440 0.1689  171 SER   V C   
38984 O  O   . SER   V  170 ? 1.6190 0.5120 1.6055 0.0252  -0.2061 0.1588  171 SER   V O   
38985 C  CB  . SER   V  170 ? 1.4913 0.5288 1.5072 -0.0022 -0.2407 0.1441  171 SER   V CB  
38986 O  OG  . SER   V  170 ? 1.5043 0.5865 1.4788 0.0165  -0.1956 0.1188  171 SER   V OG  
38987 N  N   . ASN   V  171 ? 1.5554 0.5272 1.4911 -0.0406 -0.2749 0.1164  172 ASN   V N   
38988 C  CA  . ASN   V  171 ? 1.5732 0.5130 1.4908 -0.0866 -0.3023 0.1116  172 ASN   V CA  
38989 C  C   . ASN   V  171 ? 1.5617 0.4655 1.4753 -0.1355 -0.2966 0.1288  172 ASN   V C   
38990 O  O   . ASN   V  171 ? 1.5545 0.4985 1.4544 -0.1135 -0.3201 0.1095  172 ASN   V O   
38991 C  CB  . ASN   V  171 ? 1.5893 0.4891 1.4606 -0.1000 -0.3270 0.1609  172 ASN   V CB  
38992 C  CG  . ASN   V  171 ? 1.6081 0.5609 1.4797 -0.1196 -0.3610 0.1733  172 ASN   V CG  
38993 O  OD1 . ASN   V  171 ? 1.6489 0.4487 1.4651 -0.1072 -0.4307 0.2039  172 ASN   V OD1 
38994 N  ND2 . ASN   V  171 ? 1.5541 0.6150 1.4487 -0.1199 -0.3522 0.1364  172 ASN   V ND2 
38995 N  N   . VAL   V  172 ? 1.5322 0.4919 1.5129 -0.1685 -0.2820 0.1255  173 VAL   V N   
38996 C  CA  . VAL   V  172 ? 1.5205 0.6344 1.4913 -0.1403 -0.2889 0.1197  173 VAL   V CA  
38997 C  C   . VAL   V  172 ? 1.5608 0.6406 1.5603 -0.1525 -0.2680 0.1233  173 VAL   V C   
38998 O  O   . VAL   V  172 ? 1.5744 0.6948 1.5845 -0.1811 -0.2649 0.2087  173 VAL   V O   
38999 C  CB  . VAL   V  172 ? 1.4673 0.6121 1.5039 -0.1600 -0.2817 0.0968  173 VAL   V CB  
39000 C  CG1 . VAL   V  172 ? 1.4575 0.6494 1.4730 -0.1585 -0.2778 0.0861  173 VAL   V CG1 
39001 C  CG2 . VAL   V  172 ? 1.4416 0.6070 1.4876 -0.1610 -0.2681 0.1142  173 VAL   V CG2 
39002 N  N   . ASP   V  173 ? 1.6012 0.6612 1.5506 -0.1263 -0.2393 0.1126  174 ASP   V N   
39003 C  CA  . ASP   V  173 ? 1.6175 0.6526 1.5188 -0.1460 -0.1893 0.0923  174 ASP   V CA  
39004 C  C   . ASP   V  173 ? 1.6132 0.5648 1.5154 -0.1308 -0.1703 0.0873  174 ASP   V C   
39005 O  O   . ASP   V  173 ? 1.5554 0.5544 1.4561 -0.1267 -0.1389 0.1261  174 ASP   V O   
39006 C  CB  . ASP   V  173 ? 1.6666 0.6773 1.4883 -0.1258 -0.1996 0.0872  174 ASP   V CB  
39007 C  CG  . ASP   V  173 ? 1.7355 0.7302 1.4803 -0.0872 -0.1973 0.0852  174 ASP   V CG  
39008 O  OD1 . ASP   V  173 ? 1.7316 0.6066 1.4900 -0.0978 -0.1648 0.0979  174 ASP   V OD1 
39009 O  OD2 . ASP   V  173 ? 1.8644 0.9061 1.3878 -0.0413 -0.2054 0.0624  174 ASP   V OD2 
39010 N  N   . VAL   V  174 ? 1.6894 0.5636 1.5514 -0.1060 -0.1386 0.1190  175 VAL   V N   
39011 C  CA  . VAL   V  174 ? 1.7583 0.5646 1.5918 -0.0807 -0.1443 0.1568  175 VAL   V CA  
39012 C  C   . VAL   V  174 ? 1.7753 0.5616 1.6174 -0.0876 -0.1402 0.1537  175 VAL   V C   
39013 O  O   . VAL   V  174 ? 1.8771 0.3709 1.6594 -0.1001 -0.1553 0.1611  175 VAL   V O   
39014 C  CB  . VAL   V  174 ? 1.7981 0.6266 1.6239 -0.0729 -0.1113 0.1788  175 VAL   V CB  
39015 C  CG1 . VAL   V  174 ? 1.8287 0.6638 1.6530 -0.0374 -0.1159 0.2136  175 VAL   V CG1 
39016 C  CG2 . VAL   V  174 ? 1.7814 0.6244 1.6287 -0.1145 -0.1494 0.1622  175 VAL   V CG2 
39017 N  N   . CYS   V  175 ? 1.7233 0.5655 1.6398 -0.0783 -0.1310 0.1304  176 CYS   V N   
39018 C  CA  . CYS   V  175 ? 1.7269 0.5783 1.6602 -0.0537 -0.1109 0.1646  176 CYS   V CA  
39019 C  C   . CYS   V  175 ? 1.6778 0.6098 1.6491 -0.0682 -0.1375 0.1249  176 CYS   V C   
39020 O  O   . CYS   V  175 ? 1.6591 0.4683 1.6896 -0.0646 -0.1036 0.0788  176 CYS   V O   
39021 C  CB  . CYS   V  175 ? 1.7386 0.4431 1.6738 -0.0506 -0.0969 0.2300  176 CYS   V CB  
39022 S  SG  . CYS   V  175 ? 1.7537 0.4403 1.6778 -0.0656 -0.0723 0.3685  176 CYS   V SG  
39023 N  N   . VAL   V  176 ? 1.6994 0.7215 1.6946 -0.0738 -0.0813 0.1542  177 VAL   V N   
39024 C  CA  . VAL   V  176 ? 1.7268 0.7826 1.6627 -0.0806 -0.0831 0.1005  177 VAL   V CA  
39025 C  C   . VAL   V  176 ? 1.7216 0.7936 1.6637 -0.0613 -0.1079 0.0673  177 VAL   V C   
39026 O  O   . VAL   V  176 ? 1.6621 0.8439 1.7623 -0.0408 -0.0630 -0.0290 177 VAL   V O   
39027 C  CB  . VAL   V  176 ? 1.7449 0.8022 1.6864 -0.1040 -0.0559 0.0983  177 VAL   V CB  
39028 C  CG1 . VAL   V  176 ? 1.7611 0.8106 1.6918 -0.1211 -0.0615 0.1082  177 VAL   V CG1 
39029 C  CG2 . VAL   V  176 ? 1.7598 0.7870 1.6729 -0.1099 -0.0457 0.0892  177 VAL   V CG2 
39030 N  N   . MET   V  177 ? 1.7875 0.7309 1.5539 -0.0865 -0.1494 0.0332  178 MET   V N   
39031 C  CA  . MET   V  177 ? 1.8175 0.7065 1.4938 -0.1059 -0.1694 0.0197  178 MET   V CA  
39032 C  C   . MET   V  177 ? 1.8359 0.6952 1.5074 -0.1183 -0.1567 0.0558  178 MET   V C   
39033 O  O   . MET   V  177 ? 1.8180 0.6340 1.5317 -0.1336 -0.1551 0.0867  178 MET   V O   
39034 C  CB  . MET   V  177 ? 1.8016 0.6616 1.4485 -0.1278 -0.1952 -0.0098 178 MET   V CB  
39035 C  CG  . MET   V  177 ? 1.8254 0.7151 1.4465 -0.1154 -0.2080 -0.0096 178 MET   V CG  
39036 S  SD  . MET   V  177 ? 1.8152 0.7397 1.4132 -0.1085 -0.2213 -0.0315 178 MET   V SD  
39037 C  CE  . MET   V  177 ? 1.8262 0.7425 1.4108 -0.0980 -0.2031 -0.0163 178 MET   V CE  
39038 N  N   . GLU   V  178 ? 1.8579 0.7491 1.5045 -0.1287 -0.1332 0.1008  179 GLU   V N   
39039 C  CA  . GLU   V  178 ? 1.8548 0.7852 1.5017 -0.0869 -0.1569 0.1319  179 GLU   V CA  
39040 C  C   . GLU   V  178 ? 1.8572 0.8192 1.4774 -0.0557 -0.1888 0.1928  179 GLU   V C   
39041 O  O   . GLU   V  178 ? 1.9149 0.7256 1.4795 0.1181  -0.2441 0.2235  179 GLU   V O   
39042 C  CB  . GLU   V  178 ? 1.8711 0.9074 1.4683 -0.0808 -0.1264 0.0975  179 GLU   V CB  
39043 C  CG  . GLU   V  178 ? 1.9202 1.0093 1.4528 -0.0500 -0.1336 0.1039  179 GLU   V CG  
39044 C  CD  . GLU   V  178 ? 1.9332 1.0504 1.4180 -0.0469 -0.1038 0.1187  179 GLU   V CD  
39045 O  OE1 . GLU   V  178 ? 1.9923 1.1083 1.3742 -0.0318 -0.0910 0.2167  179 GLU   V OE1 
39046 O  OE2 . GLU   V  178 ? 1.9435 1.0322 1.3809 -0.0788 -0.1173 0.0359  179 GLU   V OE2 
39047 N  N   . ILE   V  179 ? 1.8147 0.7451 1.4801 -0.0698 -0.1619 0.2280  180 ILE   V N   
39048 C  CA  . ILE   V  179 ? 1.7815 0.7663 1.4624 -0.0934 -0.1410 0.3005  180 ILE   V CA  
39049 C  C   . ILE   V  179 ? 1.7611 0.7602 1.5106 -0.0756 -0.0736 0.3515  180 ILE   V C   
39050 O  O   . ILE   V  179 ? 1.7179 0.7684 1.5168 -0.2196 -0.0074 0.3816  180 ILE   V O   
39051 C  CB  . ILE   V  179 ? 1.8177 0.6999 1.4538 -0.0625 -0.1503 0.3773  180 ILE   V CB  
39052 C  CG1 . ILE   V  179 ? 1.8070 0.6705 1.4081 -0.0425 -0.1698 0.4036  180 ILE   V CG1 
39053 C  CG2 . ILE   V  179 ? 1.8338 0.6935 1.4835 -0.0787 -0.1414 0.3877  180 ILE   V CG2 
39054 C  CD1 . ILE   V  179 ? 1.8135 0.6674 1.3786 -0.0152 -0.1961 0.4652  180 ILE   V CD1 
39055 N  N   . GLY   V  180 ? 1.7522 0.7341 1.5576 -0.0224 -0.0693 0.3690  181 GLY   V N   
39056 C  CA  . GLY   V  180 ? 1.7190 0.8289 1.5937 -0.0464 -0.0651 0.3184  181 GLY   V CA  
39057 C  C   . GLY   V  180 ? 1.7370 0.8815 1.6076 -0.0245 -0.0890 0.2535  181 GLY   V C   
39058 O  O   . GLY   V  180 ? 1.8249 0.8236 1.6124 -0.0497 -0.0891 0.2603  181 GLY   V O   
39059 N  N   . LYS   V  181 ? 1.6883 0.9340 1.5552 -0.0071 -0.0882 0.2624  182 LYS   V N   
39060 C  CA  . LYS   V  181 ? 1.6559 0.9572 1.6330 0.0691  -0.0934 0.2258  182 LYS   V CA  
39061 C  C   . LYS   V  181 ? 1.5842 0.9587 1.6141 0.0461  -0.1072 0.1704  182 LYS   V C   
39062 O  O   . LYS   V  181 ? 1.5544 0.9483 1.7483 0.0821  -0.1345 0.0728  182 LYS   V O   
39063 C  CB  . LYS   V  181 ? 1.7034 0.9390 1.6490 0.1028  -0.0888 0.2773  182 LYS   V CB  
39064 C  CG  . LYS   V  181 ? 1.7380 1.0136 1.6475 0.1942  -0.0645 0.2467  182 LYS   V CG  
39065 C  CD  . LYS   V  181 ? 1.7778 1.0487 1.7052 0.2255  -0.0220 0.1896  182 LYS   V CD  
39066 C  CE  . LYS   V  181 ? 1.7892 1.1146 1.7277 0.2926  0.0224  0.1464  182 LYS   V CE  
39067 N  NZ  . LYS   V  181 ? 1.8070 1.1884 1.7999 0.3366  0.0500  0.1181  182 LYS   V NZ  
39068 N  N   . ASP   V  182 ? 1.5902 1.0135 1.5679 0.0349  -0.0753 0.1558  183 ASP   V N   
39069 C  CA  . ASP   V  182 ? 1.5923 1.0665 1.5306 0.0089  -0.1165 0.1481  183 ASP   V CA  
39070 C  C   . ASP   V  182 ? 1.5883 1.0808 1.4156 -0.0283 -0.0907 0.1532  183 ASP   V C   
39071 O  O   . ASP   V  182 ? 1.6409 1.1362 1.2714 -0.0446 -0.0513 0.1459  183 ASP   V O   
39072 C  CB  . ASP   V  182 ? 1.6022 1.1891 1.5102 0.0097  -0.1328 0.1719  183 ASP   V CB  
39073 C  CG  . ASP   V  182 ? 1.6370 1.2297 1.5296 -0.0547 -0.1574 0.1497  183 ASP   V CG  
39074 O  OD1 . ASP   V  182 ? 1.6398 1.3256 1.6163 -0.0037 -0.1371 0.1723  183 ASP   V OD1 
39075 O  OD2 . ASP   V  182 ? 1.6231 1.4462 1.4368 0.0004  -0.2316 0.2423  183 ASP   V OD2 
39076 N  N   . ALA   V  183 ? 1.5570 0.9830 1.4398 -0.0506 -0.1232 0.1259  184 ALA   V N   
39077 C  CA  . ALA   V  183 ? 1.5144 0.9634 1.5064 -0.0998 -0.1343 0.0639  184 ALA   V CA  
39078 C  C   . ALA   V  183 ? 1.5486 0.9760 1.5417 -0.0880 -0.1526 0.0743  184 ALA   V C   
39079 O  O   . ALA   V  183 ? 1.6616 0.9282 1.5573 -0.0494 -0.1675 0.0660  184 ALA   V O   
39080 C  CB  . ALA   V  183 ? 1.4852 0.9053 1.4993 -0.1021 -0.1616 0.0485  184 ALA   V CB  
39081 N  N   . GLU   V  184 ? 1.5371 1.0141 1.5688 -0.0952 -0.1185 0.0195  185 GLU   V N   
39082 C  CA  . GLU   V  184 ? 1.5309 0.9686 1.6093 -0.1104 -0.1086 0.0494  185 GLU   V CA  
39083 C  C   . GLU   V  184 ? 1.5108 0.8392 1.6082 -0.0940 -0.1396 -0.0260 185 GLU   V C   
39084 O  O   . GLU   V  184 ? 1.3867 0.7592 1.5721 -0.1273 -0.1132 0.0487  185 GLU   V O   
39085 C  CB  . GLU   V  184 ? 1.5101 1.1323 1.6858 -0.1065 -0.0984 0.0625  185 GLU   V CB  
39086 C  CG  . GLU   V  184 ? 1.4782 1.2020 1.6584 -0.1035 -0.1198 0.0709  185 GLU   V CG  
39087 C  CD  . GLU   V  184 ? 1.3712 1.3362 1.7524 -0.0935 -0.1899 0.1514  185 GLU   V CD  
39088 O  OE1 . GLU   V  184 ? 1.3739 1.5283 1.7654 -0.0711 -0.0922 0.1604  185 GLU   V OE1 
39089 O  OE2 . GLU   V  184 ? 1.3555 1.3114 1.8262 -0.1214 -0.2162 0.1878  185 GLU   V OE2 
39090 N  N   . TYR   V  185 ? 1.5296 0.7963 1.6093 -0.1026 -0.1279 0.0220  186 TYR   V N   
39091 C  CA  . TYR   V  185 ? 1.4910 0.7190 1.6778 -0.1367 -0.1425 -0.0120 186 TYR   V CA  
39092 C  C   . TYR   V  185 ? 1.4188 0.7292 1.7448 -0.1919 -0.1802 0.0014  186 TYR   V C   
39093 O  O   . TYR   V  185 ? 1.4377 0.6774 1.8134 -0.1616 -0.2003 -0.0757 186 TYR   V O   
39094 C  CB  . TYR   V  185 ? 1.5497 0.7546 1.6677 -0.1173 -0.1265 0.0012  186 TYR   V CB  
39095 C  CG  . TYR   V  185 ? 1.5968 0.7349 1.6151 -0.0529 -0.1458 0.0096  186 TYR   V CG  
39096 C  CD1 . TYR   V  185 ? 1.5606 0.7551 1.5707 -0.0478 -0.1647 0.0265  186 TYR   V CD1 
39097 C  CD2 . TYR   V  185 ? 1.6419 0.7411 1.6144 -0.0384 -0.1631 0.0321  186 TYR   V CD2 
39098 C  CE1 . TYR   V  185 ? 1.5752 0.8431 1.5689 -0.0365 -0.1538 0.0625  186 TYR   V CE1 
39099 C  CE2 . TYR   V  185 ? 1.6700 0.7699 1.6260 -0.0231 -0.1416 0.0415  186 TYR   V CE2 
39100 C  CZ  . TYR   V  185 ? 1.6034 0.8369 1.5645 -0.0517 -0.1355 0.0630  186 TYR   V CZ  
39101 O  OH  . TYR   V  185 ? 1.5793 0.9719 1.5813 0.0043  -0.0668 0.1390  186 TYR   V OH  
39102 N  N   . LEU   V  186 ? 1.3815 0.7104 1.7454 -0.1357 -0.1922 0.0372  187 LEU   V N   
39103 C  CA  . LEU   V  186 ? 1.3621 0.7664 1.7375 -0.1332 -0.1995 0.1082  187 LEU   V CA  
39104 C  C   . LEU   V  186 ? 1.3477 0.6504 1.7196 -0.1234 -0.2433 0.0732  187 LEU   V C   
39105 O  O   . LEU   V  186 ? 1.2889 0.5652 1.7436 -0.0976 -0.2245 0.1675  187 LEU   V O   
39106 C  CB  . LEU   V  186 ? 1.3556 0.7827 1.7444 -0.1256 -0.1972 0.1054  187 LEU   V CB  
39107 C  CG  . LEU   V  186 ? 1.3926 0.8203 1.7766 -0.1560 -0.2051 0.1342  187 LEU   V CG  
39108 C  CD1 . LEU   V  186 ? 1.4045 0.7832 1.7771 -0.1704 -0.2064 0.1359  187 LEU   V CD1 
39109 C  CD2 . LEU   V  186 ? 1.3952 0.8758 1.8265 -0.1700 -0.2139 0.1556  187 LEU   V CD2 
39110 N  N   . ARG   V  187 ? 1.4069 0.7177 1.6976 -0.1050 -0.2478 0.0891  188 ARG   V N   
39111 C  CA  . ARG   V  187 ? 1.4642 0.6437 1.7126 -0.1098 -0.2278 0.0693  188 ARG   V CA  
39112 C  C   . ARG   V  187 ? 1.5013 0.6276 1.6874 -0.1018 -0.2313 0.0779  188 ARG   V C   
39113 O  O   . ARG   V  187 ? 1.5388 0.3893 1.7530 -0.1670 -0.2252 0.0809  188 ARG   V O   
39114 C  CB  . ARG   V  187 ? 1.4914 0.7686 1.6814 -0.0865 -0.2080 0.0555  188 ARG   V CB  
39115 C  CG  . ARG   V  187 ? 1.4940 0.7361 1.6956 -0.0761 -0.2008 0.0626  188 ARG   V CG  
39116 C  CD  . ARG   V  187 ? 1.4751 0.7265 1.6881 -0.0596 -0.2002 0.0514  188 ARG   V CD  
39117 N  NE  . ARG   V  187 ? 1.4802 0.7747 1.6788 -0.0005 -0.2114 0.0301  188 ARG   V NE  
39118 C  CZ  . ARG   V  187 ? 1.4342 0.7645 1.6670 0.0205  -0.2180 0.0044  188 ARG   V CZ  
39119 N  NH1 . ARG   V  187 ? 1.4316 0.7236 1.6850 0.0232  -0.2228 0.0043  188 ARG   V NH1 
39120 N  NH2 . ARG   V  187 ? 1.4192 0.7657 1.6686 0.0558  -0.1870 0.0112  188 ARG   V NH2 
39121 N  N   . ASN   V  188 ? 1.5737 0.5744 1.6200 -0.0388 -0.2252 0.1236  189 ASN   V N   
39122 C  CA  . ASN   V  188 ? 1.6135 0.5976 1.5621 -0.0061 -0.1836 0.1226  189 ASN   V CA  
39123 C  C   . ASN   V  188 ? 1.5853 0.5784 1.5922 0.0027  -0.1625 0.1515  189 ASN   V C   
39124 O  O   . ASN   V  188 ? 1.5636 0.4984 1.6084 0.0117  -0.0919 0.1779  189 ASN   V O   
39125 C  CB  . ASN   V  188 ? 1.6588 0.5727 1.5582 0.0314  -0.1980 0.0959  189 ASN   V CB  
39126 C  CG  . ASN   V  188 ? 1.6526 0.5354 1.4918 0.0563  -0.2280 0.0613  189 ASN   V CG  
39127 O  OD1 . ASN   V  188 ? 1.6374 0.4478 1.4317 0.0109  -0.1977 0.0078  189 ASN   V OD1 
39128 N  ND2 . ASN   V  188 ? 1.6967 0.5404 1.4932 0.0880  -0.2427 0.0423  189 ASN   V ND2 
39129 N  N   . TYR   V  189 ? 1.6173 0.6462 1.5411 -0.0195 -0.1208 0.1586  190 TYR   V N   
39130 C  CA  . TYR   V  189 ? 1.6584 0.7360 1.5717 -0.0644 -0.0828 0.1140  190 TYR   V CA  
39131 C  C   . TYR   V  189 ? 1.7013 0.7522 1.5912 -0.0272 -0.1006 0.1463  190 TYR   V C   
39132 O  O   . TYR   V  189 ? 1.7178 0.8074 1.6103 -0.0745 -0.0782 0.1850  190 TYR   V O   
39133 C  CB  . TYR   V  189 ? 1.6484 0.8158 1.4959 -0.1146 -0.0664 0.0450  190 TYR   V CB  
39134 C  CG  . TYR   V  189 ? 1.6468 0.8167 1.5030 -0.1565 -0.0473 0.0329  190 TYR   V CG  
39135 C  CD1 . TYR   V  189 ? 1.6447 0.8383 1.4044 -0.1381 -0.0224 0.0358  190 TYR   V CD1 
39136 C  CD2 . TYR   V  189 ? 1.6653 0.8851 1.4071 -0.1520 0.0041  -0.0035 190 TYR   V CD2 
39137 C  CE1 . TYR   V  189 ? 1.6348 0.8353 1.4075 -0.1577 -0.0126 0.0367  190 TYR   V CE1 
39138 C  CE2 . TYR   V  189 ? 1.6631 0.8701 1.4038 -0.1728 0.0180  0.0211  190 TYR   V CE2 
39139 C  CZ  . TYR   V  189 ? 1.6730 0.8487 1.3789 -0.1653 0.0097  0.0300  190 TYR   V CZ  
39140 O  OH  . TYR   V  189 ? 1.7007 0.8936 1.4125 -0.1633 0.0628  0.0467  190 TYR   V OH  
39141 N  N   . LEU   V  190 ? 1.7210 0.7470 1.6276 -0.0231 -0.0961 0.1510  191 LEU   V N   
39142 C  CA  . LEU   V  190 ? 1.7659 0.7559 1.7272 0.0065  -0.1008 0.1278  191 LEU   V CA  
39143 C  C   . LEU   V  190 ? 1.7646 0.5792 1.7728 0.0291  -0.1634 0.1619  191 LEU   V C   
39144 O  O   . LEU   V  190 ? 1.7708 0.4591 1.9124 0.0987  -0.1531 0.1759  191 LEU   V O   
39145 C  CB  . LEU   V  190 ? 1.7725 0.7718 1.7325 0.0407  -0.0965 0.1027  191 LEU   V CB  
39146 C  CG  . LEU   V  190 ? 1.7919 0.9068 1.7793 0.0706  -0.0209 0.0970  191 LEU   V CG  
39147 C  CD1 . LEU   V  190 ? 1.7880 0.9414 1.7906 0.0777  -0.0092 0.0675  191 LEU   V CD1 
39148 C  CD2 . LEU   V  190 ? 1.7688 0.9424 1.8255 0.0578  -0.0368 0.1198  191 LEU   V CD2 
39149 N  N   . THR   V  191 ? 1.6739 0.6408 1.8333 -0.0086 -0.1990 0.1146  192 THR   V N   
39150 C  CA  . THR   V  191 ? 1.6174 0.7026 1.7920 -0.0488 -0.2432 0.0985  192 THR   V CA  
39151 C  C   . THR   V  191 ? 1.6106 0.7434 1.8553 0.0342  -0.2440 0.1611  192 THR   V C   
39152 O  O   . THR   V  191 ? 1.6219 0.9323 1.9003 0.0379  -0.2931 0.1282  192 THR   V O   
39153 C  CB  . THR   V  191 ? 1.6010 0.6249 1.7730 -0.1007 -0.1761 0.0971  192 THR   V CB  
39154 O  OG1 . THR   V  191 ? 1.6169 0.5857 1.8013 -0.1981 -0.1593 0.0455  192 THR   V OG1 
39155 C  CG2 . THR   V  191 ? 1.6042 0.5596 1.7487 -0.1683 -0.2031 0.0871  192 THR   V CG2 
39156 N  N   . PRO   V  192 ? 1.5292 0.7619 1.8321 0.0292  -0.2532 0.2322  193 PRO   V N   
39157 C  CA  . PRO   V  192 ? 1.5293 0.7826 1.7969 0.0498  -0.1823 0.2408  193 PRO   V CA  
39158 C  C   . PRO   V  192 ? 1.5291 0.8262 1.6920 0.1103  -0.1785 0.2247  193 PRO   V C   
39159 O  O   . PRO   V  192 ? 1.4986 0.7870 1.7367 0.2512  -0.1797 0.3177  193 PRO   V O   
39160 C  CB  . PRO   V  192 ? 1.5381 0.7924 1.7821 0.0831  -0.1848 0.2673  193 PRO   V CB  
39161 C  CG  . PRO   V  192 ? 1.5603 0.7514 1.8264 0.0829  -0.1847 0.2823  193 PRO   V CG  
39162 C  CD  . PRO   V  192 ? 1.5329 0.7859 1.8486 0.0531  -0.2247 0.2735  193 PRO   V CD  
39163 N  N   . ASN   V  193 ? 1.5198 0.8428 1.6535 0.0691  -0.2132 0.2199  194 ASN   V N   
39164 C  CA  . ASN   V  193 ? 1.4905 0.8182 1.5711 0.0879  -0.2116 0.1636  194 ASN   V CA  
39165 C  C   . ASN   V  193 ? 1.4671 0.8012 1.5834 0.0872  -0.1799 0.1017  194 ASN   V C   
39166 O  O   . ASN   V  193 ? 1.5635 0.8273 1.5833 0.0367  -0.1467 0.0925  194 ASN   V O   
39167 C  CB  . ASN   V  193 ? 1.4798 0.8084 1.5029 0.0514  -0.2401 0.2072  194 ASN   V CB  
39168 C  CG  . ASN   V  193 ? 1.4419 0.8023 1.5234 0.0018  -0.2358 0.2406  194 ASN   V CG  
39169 O  OD1 . ASN   V  193 ? 1.3536 0.8087 1.4276 -0.0209 -0.2833 0.3464  194 ASN   V OD1 
39170 N  ND2 . ASN   V  193 ? 1.4539 0.7758 1.5539 -0.0001 -0.2370 0.2527  194 ASN   V ND2 
39171 N  N   . VAL   V  194 ? 1.4564 0.7667 1.6338 0.1109  -0.1693 0.0601  195 VAL   V N   
39172 C  CA  . VAL   V  194 ? 1.4701 0.8110 1.6311 0.1335  -0.1757 0.0507  195 VAL   V CA  
39173 C  C   . VAL   V  194 ? 1.4908 0.8232 1.6096 0.1045  -0.2199 0.0414  195 VAL   V C   
39174 O  O   . VAL   V  194 ? 1.5290 0.8921 1.5845 0.0495  -0.2003 -0.0254 195 VAL   V O   
39175 C  CB  . VAL   V  194 ? 1.4689 0.7753 1.6412 0.1693  -0.1667 0.1124  195 VAL   V CB  
39176 C  CG1 . VAL   V  194 ? 1.4346 0.7100 1.6100 0.2406  -0.1712 0.1789  195 VAL   V CG1 
39177 C  CG2 . VAL   V  194 ? 1.5352 0.8022 1.6599 0.1571  -0.1367 0.1354  195 VAL   V CG2 
39178 N  N   . ARG   V  195 ? 1.5363 0.9411 1.6343 0.0531  -0.2207 -0.0994 196 ARG   V N   
39179 C  CA  . ARG   V  195 ? 1.5939 0.8137 1.7603 -0.0184 -0.2319 -0.1241 196 ARG   V CA  
39180 C  C   . ARG   V  195 ? 1.6098 0.7709 1.8152 -0.0108 -0.2906 -0.1250 196 ARG   V C   
39181 O  O   . ARG   V  195 ? 1.5359 0.8970 1.9355 -0.0322 -0.3144 -0.0925 196 ARG   V O   
39182 C  CB  . ARG   V  195 ? 1.5856 0.8826 1.7793 -0.0504 -0.1893 -0.1204 196 ARG   V CB  
39183 C  CG  . ARG   V  195 ? 1.5827 0.7698 1.8187 -0.0482 -0.2286 -0.1283 196 ARG   V CG  
39184 C  CD  . ARG   V  195 ? 1.6157 0.7923 1.8749 -0.0450 -0.2332 -0.0817 196 ARG   V CD  
39185 N  NE  . ARG   V  195 ? 1.6442 0.8988 1.9476 -0.0306 -0.1955 -0.1156 196 ARG   V NE  
39186 C  CZ  . ARG   V  195 ? 1.6607 1.0259 2.0092 -0.0309 -0.2188 -0.0503 196 ARG   V CZ  
39187 N  NH1 . ARG   V  195 ? 1.6601 1.0409 2.0347 -0.0070 -0.2637 -0.0486 196 ARG   V NH1 
39188 N  NH2 . ARG   V  195 ? 1.6095 1.1364 2.0675 -0.0370 -0.1975 -0.0868 196 ARG   V NH2 
39189 N  N   . GLU   V  196 ? 1.6661 0.7619 1.8335 -0.0349 -0.3400 -0.1246 197 GLU   V N   
39190 C  CA  . GLU   V  196 ? 1.6413 0.8446 1.7990 -0.0472 -0.3428 -0.1362 197 GLU   V CA  
39191 C  C   . GLU   V  196 ? 1.6140 0.8242 1.7928 -0.0709 -0.3403 -0.1127 197 GLU   V C   
39192 O  O   . GLU   V  196 ? 1.5913 0.7826 1.6628 -0.1218 -0.4211 -0.1626 197 GLU   V O   
39193 C  CB  . GLU   V  196 ? 1.7103 0.8464 1.8075 0.0414  -0.3486 -0.1418 197 GLU   V CB  
39194 C  CG  . GLU   V  196 ? 1.7479 0.8508 1.7762 0.0878  -0.3777 -0.1070 197 GLU   V CG  
39195 C  CD  . GLU   V  196 ? 1.7601 0.8643 1.7379 0.0969  -0.4251 -0.1313 197 GLU   V CD  
39196 O  OE1 . GLU   V  196 ? 1.8229 0.8275 1.7808 0.1805  -0.4258 -0.1497 197 GLU   V OE1 
39197 O  OE2 . GLU   V  196 ? 1.6906 0.6855 1.7982 0.0870  -0.4839 -0.1808 197 GLU   V OE2 
39198 N  N   . GLU   V  197 ? 1.6028 0.8492 1.7696 -0.0449 -0.2924 -0.0353 198 GLU   V N   
39199 C  CA  . GLU   V  197 ? 1.5824 0.9551 1.7689 -0.0392 -0.2874 -0.0121 198 GLU   V CA  
39200 C  C   . GLU   V  197 ? 1.5300 1.0198 1.7461 -0.0636 -0.2884 -0.0138 198 GLU   V C   
39201 O  O   . GLU   V  197 ? 1.5433 1.0231 1.7687 -0.1207 -0.2429 -0.0182 198 GLU   V O   
39202 C  CB  . GLU   V  197 ? 1.5940 1.0633 1.7900 -0.0321 -0.2438 0.0191  198 GLU   V CB  
39203 C  CG  . GLU   V  197 ? 1.6840 1.1202 1.8803 -0.0907 -0.1865 0.0346  198 GLU   V CG  
39204 C  CD  . GLU   V  197 ? 1.7033 1.2793 1.9767 0.0048  -0.1666 0.1032  198 GLU   V CD  
39205 O  OE1 . GLU   V  197 ? 1.8093 1.2500 1.9978 0.0381  -0.0689 0.1608  198 GLU   V OE1 
39206 O  OE2 . GLU   V  197 ? 1.8155 1.4396 2.0753 0.0606  -0.0570 0.1783  198 GLU   V OE2 
39207 N  N   . LYS   V  198 ? 1.4568 1.0999 1.7461 -0.0442 -0.3232 -0.0353 199 LYS   V N   
39208 C  CA  . LYS   V  198 ? 1.4345 1.0550 1.7871 -0.0290 -0.3507 -0.0137 199 LYS   V CA  
39209 C  C   . LYS   V  198 ? 1.4195 0.9345 1.7407 -0.0814 -0.3609 -0.0209 199 LYS   V C   
39210 O  O   . LYS   V  198 ? 1.3944 0.9062 1.7868 -0.0330 -0.3500 0.0417  199 LYS   V O   
39211 C  CB  . LYS   V  198 ? 1.5080 1.1662 1.7628 0.0136  -0.3302 0.0069  199 LYS   V CB  
39212 C  CG  . LYS   V  198 ? 1.5621 1.1666 1.8133 0.0923  -0.3089 0.0337  199 LYS   V CG  
39213 C  CD  . LYS   V  198 ? 1.6266 1.1530 1.7960 0.1329  -0.3043 0.0557  199 LYS   V CD  
39214 C  CE  . LYS   V  198 ? 1.7137 1.1496 1.8103 0.1502  -0.2948 0.0459  199 LYS   V CE  
39215 N  NZ  . LYS   V  198 ? 1.7092 1.1816 1.8689 0.1614  -0.3062 0.0292  199 LYS   V NZ  
39216 N  N   . GLN   V  199 ? 1.4142 0.9397 1.7333 -0.0716 -0.3390 -0.0170 200 GLN   V N   
39217 C  CA  . GLN   V  199 ? 1.4411 0.9479 1.7754 -0.0463 -0.2858 0.0021  200 GLN   V CA  
39218 C  C   . GLN   V  199 ? 1.4032 0.9942 1.7732 -0.0489 -0.2673 -0.0120 200 GLN   V C   
39219 O  O   . GLN   V  199 ? 1.3599 0.9791 1.7894 -0.1185 -0.3116 0.0122  200 GLN   V O   
39220 C  CB  . GLN   V  199 ? 1.5265 0.9025 1.8185 -0.0111 -0.2401 0.0479  200 GLN   V CB  
39221 C  CG  . GLN   V  199 ? 1.5882 0.7927 1.8333 -0.0073 -0.2260 0.0349  200 GLN   V CG  
39222 C  CD  . GLN   V  199 ? 1.6483 0.7119 1.8916 0.0123  -0.1806 0.0449  200 GLN   V CD  
39223 O  OE1 . GLN   V  199 ? 1.7143 0.3690 1.9833 -0.0231 -0.1816 0.0781  200 GLN   V OE1 
39224 N  NE2 . GLN   V  199 ? 1.6721 0.7734 1.9301 0.0660  -0.1873 0.0266  200 GLN   V NE2 
39225 N  N   . LYS   V  200 ? 1.4258 1.0818 1.7314 -0.0123 -0.2339 0.0111  201 LYS   V N   
39226 C  CA  . LYS   V  200 ? 1.4186 1.1334 1.7061 0.0556  -0.2312 0.0616  201 LYS   V CA  
39227 C  C   . LYS   V  200 ? 1.4461 1.1133 1.6591 0.0126  -0.2633 0.0563  201 LYS   V C   
39228 O  O   . LYS   V  200 ? 1.3998 1.1216 1.6960 -0.0148 -0.2465 0.0538  201 LYS   V O   
39229 C  CB  . LYS   V  200 ? 1.4200 1.1288 1.6497 0.1174  -0.2086 0.0740  201 LYS   V CB  
39230 C  CG  . LYS   V  200 ? 1.4572 1.1750 1.6420 0.1856  -0.1958 0.0561  201 LYS   V CG  
39231 C  CD  . LYS   V  200 ? 1.5140 1.1573 1.6755 0.1932  -0.1580 0.0516  201 LYS   V CD  
39232 C  CE  . LYS   V  200 ? 1.5885 1.2058 1.6619 0.2021  -0.1366 0.0701  201 LYS   V CE  
39233 N  NZ  . LYS   V  200 ? 1.6372 1.2506 1.6572 0.2321  -0.1255 0.0627  201 LYS   V NZ  
39234 N  N   . SER   V  201 ? 1.4282 1.1430 1.6671 0.0151  -0.3156 0.1196  202 SER   V N   
39235 C  CA  . SER   V  201 ? 1.4363 1.1256 1.6950 0.0492  -0.3408 0.1352  202 SER   V CA  
39236 C  C   . SER   V  201 ? 1.4162 1.0585 1.6936 0.0718  -0.3925 0.2097  202 SER   V C   
39237 O  O   . SER   V  201 ? 1.4491 1.0194 1.7134 -0.0076 -0.4389 0.2363  202 SER   V O   
39238 C  CB  . SER   V  201 ? 1.4435 1.1518 1.7192 0.0424  -0.3286 0.1007  202 SER   V CB  
39239 O  OG  . SER   V  201 ? 1.4736 1.1942 1.7392 0.0752  -0.3291 0.0698  202 SER   V OG  
39240 N  N   . TYR   V  202 ? 1.4415 1.0420 1.6767 0.0852  -0.3692 0.2257  203 TYR   V N   
39241 C  CA  . TYR   V  202 ? 1.5296 1.0115 1.6399 0.0611  -0.3800 0.2595  203 TYR   V CA  
39242 C  C   . TYR   V  202 ? 1.4792 1.0693 1.6086 0.0491  -0.4023 0.2491  203 TYR   V C   
39243 O  O   . TYR   V  202 ? 1.5545 1.0640 1.5391 -0.0132 -0.3729 0.2731  203 TYR   V O   
39244 C  CB  . TYR   V  202 ? 1.5532 0.9789 1.6117 0.0330  -0.3833 0.2704  203 TYR   V CB  
39245 C  CG  . TYR   V  202 ? 1.6370 1.0239 1.6309 0.0536  -0.3921 0.2319  203 TYR   V CG  
39246 C  CD1 . TYR   V  202 ? 1.7040 1.0344 1.6315 0.0540  -0.3826 0.2357  203 TYR   V CD1 
39247 C  CD2 . TYR   V  202 ? 1.6811 0.9940 1.6286 0.0293  -0.3748 0.1966  203 TYR   V CD2 
39248 C  CE1 . TYR   V  202 ? 1.7451 1.1024 1.6385 0.0067  -0.3809 0.1897  203 TYR   V CE1 
39249 C  CE2 . TYR   V  202 ? 1.7282 1.0197 1.6707 0.0234  -0.3527 0.1647  203 TYR   V CE2 
39250 C  CZ  . TYR   V  202 ? 1.7523 1.0129 1.6325 -0.0005 -0.3715 0.1460  203 TYR   V CZ  
39251 O  OH  . TYR   V  202 ? 1.7924 0.9762 1.7892 -0.0708 -0.3143 0.1102  203 TYR   V OH  
39252 N  N   . LYS   V  203 ? 1.4160 1.1176 1.6864 0.0794  -0.4049 0.2454  204 LYS   V N   
39253 C  CA  . LYS   V  203 ? 1.4223 1.1508 1.7322 0.0687  -0.3898 0.2086  204 LYS   V CA  
39254 C  C   . LYS   V  203 ? 1.4202 1.1920 1.7024 0.0521  -0.3766 0.2057  204 LYS   V C   
39255 O  O   . LYS   V  203 ? 1.4863 1.2030 1.7087 0.0800  -0.3274 0.2136  204 LYS   V O   
39256 C  CB  . LYS   V  203 ? 1.4313 1.2412 1.8439 0.0489  -0.3484 0.1820  204 LYS   V CB  
39257 C  CG  . LYS   V  203 ? 1.4709 1.2933 1.8819 0.0256  -0.3233 0.1358  204 LYS   V CG  
39258 C  CD  . LYS   V  203 ? 1.4793 1.3074 1.9204 -0.0048 -0.3080 0.1216  204 LYS   V CD  
39259 C  CE  . LYS   V  203 ? 1.4791 1.3330 1.9179 -0.0005 -0.3121 0.1072  204 LYS   V CE  
39260 N  NZ  . LYS   V  203 ? 1.4940 1.3554 1.9386 -0.0116 -0.2981 0.0920  204 LYS   V NZ  
39261 N  N   . PHE   V  204 ? 1.3649 1.2139 1.6536 0.0517  -0.4344 0.1842  205 PHE   V N   
39262 C  CA  . PHE   V  204 ? 1.3670 1.3166 1.6217 0.0365  -0.4263 0.1725  205 PHE   V CA  
39263 C  C   . PHE   V  204 ? 1.3933 1.3610 1.6967 -0.0194 -0.4119 0.1045  205 PHE   V C   
39264 O  O   . PHE   V  204 ? 1.3751 1.3519 1.7380 -0.0075 -0.4325 0.1465  205 PHE   V O   
39265 C  CB  . PHE   V  204 ? 1.3391 1.3546 1.5975 0.0603  -0.4633 0.1712  205 PHE   V CB  
39266 C  CG  . PHE   V  204 ? 1.3325 1.3696 1.5978 0.0654  -0.4714 0.1779  205 PHE   V CG  
39267 C  CD1 . PHE   V  204 ? 1.3137 1.3863 1.5682 0.0521  -0.4909 0.2063  205 PHE   V CD1 
39268 C  CD2 . PHE   V  204 ? 1.3045 1.3355 1.6271 0.0792  -0.4680 0.1632  205 PHE   V CD2 
39269 C  CE1 . PHE   V  204 ? 1.3171 1.3679 1.5931 0.0343  -0.4726 0.1991  205 PHE   V CE1 
39270 C  CE2 . PHE   V  204 ? 1.2838 1.3223 1.6656 0.0694  -0.4434 0.1456  205 PHE   V CE2 
39271 C  CZ  . PHE   V  204 ? 1.2945 1.3383 1.6325 0.0722  -0.4641 0.1822  205 PHE   V CZ  
39272 N  N   . PRO   V  205 ? 1.3736 1.4078 1.6747 0.0050  -0.4144 0.0799  206 PRO   V N   
39273 C  CA  . PRO   V  205 ? 1.3921 1.4200 1.6738 -0.0024 -0.4036 0.0449  206 PRO   V CA  
39274 C  C   . PRO   V  205 ? 1.4363 1.4130 1.6714 -0.0453 -0.4010 -0.0015 206 PRO   V C   
39275 O  O   . PRO   V  205 ? 1.4242 1.5562 1.7068 -0.0564 -0.3881 -0.0355 206 PRO   V O   
39276 C  CB  . PRO   V  205 ? 1.3669 1.4636 1.6496 0.0255  -0.4287 0.0635  206 PRO   V CB  
39277 C  CG  . PRO   V  205 ? 1.3569 1.4527 1.6526 0.0178  -0.4026 0.0700  206 PRO   V CG  
39278 C  CD  . PRO   V  205 ? 1.3383 1.4099 1.6878 0.0122  -0.3997 0.0754  206 PRO   V CD  
39279 N  N   . ARG   V  206 ? 1.5090 1.3514 1.6216 0.0085  -0.3617 -0.0372 207 ARG   V N   
39280 C  CA  . ARG   V  206 ? 1.5282 1.3297 1.5213 0.0064  -0.4034 -0.0298 207 ARG   V CA  
39281 C  C   . ARG   V  206 ? 1.4658 1.2480 1.4863 0.0627  -0.4302 -0.0518 207 ARG   V C   
39282 O  O   . ARG   V  206 ? 1.4671 1.1500 1.3973 0.0020  -0.4501 -0.0858 207 ARG   V O   
39283 C  CB  . ARG   V  206 ? 1.5904 1.3319 1.5311 -0.0052 -0.4344 -0.1088 207 ARG   V CB  
39284 C  CG  . ARG   V  206 ? 1.6599 1.3359 1.5435 -0.0252 -0.4314 -0.1029 207 ARG   V CG  
39285 C  CD  . ARG   V  206 ? 1.7020 1.3769 1.5592 -0.0635 -0.4663 -0.1315 207 ARG   V CD  
39286 N  NE  . ARG   V  206 ? 1.7510 1.3684 1.5924 -0.0928 -0.4627 -0.1092 207 ARG   V NE  
39287 C  CZ  . ARG   V  206 ? 1.8052 1.2975 1.5902 -0.0342 -0.4806 -0.1536 207 ARG   V CZ  
39288 N  NH1 . ARG   V  206 ? 1.8227 1.2022 1.6505 0.0125  -0.4938 -0.1577 207 ARG   V NH1 
39289 N  NH2 . ARG   V  206 ? 1.8342 1.2707 1.6115 -0.0221 -0.4649 -0.1297 207 ARG   V NH2 
39290 N  N   . GLY   V  207 ? 1.4829 1.2254 1.4269 0.1184  -0.4151 -0.0025 208 GLY   V N   
39291 C  CA  . GLY   V  207 ? 1.4893 1.2810 1.4326 0.2038  -0.3861 0.0268  208 GLY   V CA  
39292 C  C   . GLY   V  207 ? 1.4626 1.2821 1.4552 0.2066  -0.3607 0.0837  208 GLY   V C   
39293 O  O   . GLY   V  207 ? 1.5086 1.3702 1.4671 0.2733  -0.2676 0.0627  208 GLY   V O   
39294 N  N   . THR   V  208 ? 1.4719 1.3766 1.4226 0.2281  -0.3780 0.1185  209 THR   V N   
39295 C  CA  . THR   V  208 ? 1.4662 1.3995 1.5235 0.1990  -0.3404 0.1197  209 THR   V CA  
39296 C  C   . THR   V  208 ? 1.4839 1.4299 1.4792 0.2479  -0.3316 0.1356  209 THR   V C   
39297 O  O   . THR   V  208 ? 1.4380 1.4391 1.4485 0.3455  -0.3324 0.2176  209 THR   V O   
39298 C  CB  . THR   V  208 ? 1.5384 1.4405 1.5534 0.1832  -0.2581 0.0726  209 THR   V CB  
39299 O  OG1 . THR   V  208 ? 1.5019 1.3723 1.6751 0.0823  -0.2555 0.0213  209 THR   V OG1 
39300 C  CG2 . THR   V  208 ? 1.5420 1.4539 1.6437 0.1648  -0.2344 0.0798  209 THR   V CG2 
39301 N  N   . THR   V  209 ? 1.5216 1.3663 1.5019 0.2064  -0.3015 0.0950  210 THR   V N   
39302 C  CA  . THR   V  209 ? 1.5369 1.2892 1.4555 0.2298  -0.3171 0.0874  210 THR   V CA  
39303 C  C   . THR   V  209 ? 1.5638 1.2018 1.4566 0.1970  -0.3680 0.0725  210 THR   V C   
39304 O  O   . THR   V  209 ? 1.5351 1.1499 1.4575 0.2319  -0.3795 0.0774  210 THR   V O   
39305 C  CB  . THR   V  209 ? 1.5097 1.2472 1.4628 0.2364  -0.3324 0.0483  210 THR   V CB  
39306 O  OG1 . THR   V  209 ? 1.4820 1.2697 1.4747 0.2593  -0.2898 0.0604  210 THR   V OG1 
39307 C  CG2 . THR   V  209 ? 1.5125 1.2312 1.4603 0.2609  -0.3355 0.0507  210 THR   V CG2 
39308 N  N   . ALA   V  210 ? 1.6048 1.2690 1.3484 0.2455  -0.3741 0.1409  211 ALA   V N   
39309 C  CA  . ALA   V  210 ? 1.5571 1.2690 1.3009 0.2646  -0.4647 0.1546  211 ALA   V CA  
39310 C  C   . ALA   V  210 ? 1.5660 1.2466 1.3076 0.2518  -0.4645 0.1675  211 ALA   V C   
39311 O  O   . ALA   V  210 ? 1.4956 1.1839 1.3841 0.1472  -0.4764 0.0664  211 ALA   V O   
39312 C  CB  . ALA   V  210 ? 1.5373 1.3226 1.2572 0.2688  -0.4497 0.1846  211 ALA   V CB  
39313 N  N   . VAL   V  211 ? 1.5383 1.2784 1.2662 0.2766  -0.5262 0.2004  212 VAL   V N   
39314 C  CA  . VAL   V  211 ? 1.5103 1.2830 1.3249 0.2794  -0.5191 0.2066  212 VAL   V CA  
39315 C  C   . VAL   V  211 ? 1.4582 1.3067 1.3014 0.2988  -0.5673 0.1894  212 VAL   V C   
39316 O  O   . VAL   V  211 ? 1.4253 1.3612 1.2889 0.2331  -0.6329 0.0912  212 VAL   V O   
39317 C  CB  . VAL   V  211 ? 1.4992 1.2480 1.3826 0.2849  -0.5145 0.1714  212 VAL   V CB  
39318 C  CG1 . VAL   V  211 ? 1.4891 1.2766 1.3540 0.2852  -0.5175 0.1268  212 VAL   V CG1 
39319 C  CG2 . VAL   V  211 ? 1.5031 1.2209 1.4300 0.2531  -0.4396 0.1686  212 VAL   V CG2 
39320 N  N   . LEU   V  212 ? 1.4672 1.3090 1.3546 0.3035  -0.5408 0.2007  213 LEU   V N   
39321 C  CA  . LEU   V  212 ? 1.4796 1.4236 1.3613 0.2941  -0.5314 0.2122  213 LEU   V CA  
39322 C  C   . LEU   V  212 ? 1.4401 1.5323 1.3657 0.2272  -0.5858 0.1224  213 LEU   V C   
39323 O  O   . LEU   V  212 ? 1.3492 1.5874 1.3751 0.2129  -0.6051 0.1571  213 LEU   V O   
39324 C  CB  . LEU   V  212 ? 1.4795 1.4347 1.4070 0.2868  -0.4888 0.2553  213 LEU   V CB  
39325 C  CG  . LEU   V  212 ? 1.5101 1.4136 1.4655 0.2854  -0.4310 0.2876  213 LEU   V CG  
39326 C  CD1 . LEU   V  212 ? 1.5033 1.4365 1.5384 0.2968  -0.3543 0.3239  213 LEU   V CD1 
39327 C  CD2 . LEU   V  212 ? 1.4705 1.5226 1.4209 0.3092  -0.4496 0.2958  213 LEU   V CD2 
39328 N  N   . LYS   V  213 ? 1.5016 1.4644 1.4499 0.1889  -0.5288 0.1238  214 LYS   V N   
39329 C  CA  . LYS   V  213 ? 1.5227 1.5277 1.5282 0.1909  -0.5024 -0.0252 214 LYS   V CA  
39330 C  C   . LYS   V  213 ? 1.5513 1.4439 1.6373 0.1193  -0.4641 -0.0702 214 LYS   V C   
39331 O  O   . LYS   V  213 ? 1.5901 1.4293 1.6825 0.1006  -0.3728 -0.1327 214 LYS   V O   
39332 C  CB  . LYS   V  213 ? 1.5693 1.4947 1.5353 0.2187  -0.4382 -0.0419 214 LYS   V CB  
39333 C  CG  . LYS   V  213 ? 1.6140 1.5427 1.5384 0.2730  -0.4050 -0.0235 214 LYS   V CG  
39334 C  CD  . LYS   V  213 ? 1.6555 1.5653 1.6098 0.3142  -0.3472 0.0112  214 LYS   V CD  
39335 C  CE  . LYS   V  213 ? 1.7109 1.6159 1.6374 0.3136  -0.3304 0.0758  214 LYS   V CE  
39336 N  NZ  . LYS   V  213 ? 1.7283 1.6313 1.6849 0.3247  -0.3029 0.0915  214 LYS   V NZ  
39337 N  N   . GLU   V  214 ? 1.6140 1.4967 1.5614 0.1289  -0.5161 -0.1397 215 GLU   V N   
39338 C  CA  . GLU   V  214 ? 1.6463 1.5334 1.5838 0.0824  -0.5218 -0.1301 215 GLU   V CA  
39339 C  C   . GLU   V  214 ? 1.7264 1.5203 1.4875 0.0584  -0.5737 -0.1425 215 GLU   V C   
39340 O  O   . GLU   V  214 ? 1.7547 1.5549 1.4661 0.0348  -0.6177 -0.1728 215 GLU   V O   
39341 C  CB  . GLU   V  214 ? 1.6392 1.5754 1.6504 0.0506  -0.4860 -0.1548 215 GLU   V CB  
39342 C  CG  . GLU   V  214 ? 1.6037 1.6106 1.7103 0.0238  -0.4083 -0.1574 215 GLU   V CG  
39343 C  CD  . GLU   V  214 ? 1.6320 1.6594 1.8090 -0.0415 -0.3621 -0.1466 215 GLU   V CD  
39344 O  OE1 . GLU   V  214 ? 1.6575 1.6306 1.8331 -0.0311 -0.3113 -0.2317 215 GLU   V OE1 
39345 O  OE2 . GLU   V  214 ? 1.5891 1.7111 1.9301 -0.0253 -0.3193 -0.0890 215 GLU   V OE2 
39346 N  N   . SER   V  215 ? 1.7729 1.4818 1.5392 0.0257  -0.6012 -0.1369 216 SER   V N   
39347 C  CA  . SER   V  215 ? 1.7297 1.4962 1.5573 0.0371  -0.6270 -0.1722 216 SER   V CA  
39348 C  C   . SER   V  215 ? 1.7974 1.4138 1.6598 0.0327  -0.6526 -0.1396 216 SER   V C   
39349 O  O   . SER   V  215 ? 1.8659 1.4018 1.6827 0.0569  -0.6943 -0.1492 216 SER   V O   
39350 C  CB  . SER   V  215 ? 1.7290 1.5002 1.5117 0.0537  -0.6158 -0.1405 216 SER   V CB  
39351 O  OG  . SER   V  215 ? 1.5891 1.5111 1.5195 0.0524  -0.5860 -0.0909 216 SER   V OG  
39352 N  N   . ILE   V  216 ? 1.8120 1.3853 1.7003 0.0430  -0.6379 -0.1082 217 ILE   V N   
39353 C  CA  . ILE   V  216 ? 1.7805 1.3216 1.7461 0.0357  -0.6136 -0.1251 217 ILE   V CA  
39354 C  C   . ILE   V  216 ? 1.7809 1.2315 1.7377 0.0590  -0.5468 -0.1394 217 ILE   V C   
39355 O  O   . ILE   V  216 ? 1.7592 1.1077 1.7583 0.1112  -0.5714 -0.1855 217 ILE   V O   
39356 C  CB  . ILE   V  216 ? 1.7470 1.3299 1.7699 0.0422  -0.6293 -0.1109 217 ILE   V CB  
39357 C  CG1 . ILE   V  216 ? 1.7110 1.3303 1.8041 0.0167  -0.6262 -0.1221 217 ILE   V CG1 
39358 C  CG2 . ILE   V  216 ? 1.7408 1.3191 1.7890 0.0405  -0.6414 -0.1059 217 ILE   V CG2 
39359 C  CD1 . ILE   V  216 ? 1.6893 1.2884 1.8055 0.0059  -0.6198 -0.1072 217 ILE   V CD1 
39360 N  N   . VAL   V  217 ? 1.8594 1.2230 1.7431 0.0120  -0.5371 -0.0997 218 VAL   V N   
39361 C  CA  . VAL   V  217 ? 1.8661 1.3249 1.8023 0.0437  -0.5115 -0.0960 218 VAL   V CA  
39362 C  C   . VAL   V  217 ? 1.9567 1.3358 1.8940 -0.0226 -0.4744 -0.1498 218 VAL   V C   
39363 O  O   . VAL   V  217 ? 1.9550 1.4884 1.9652 -0.0885 -0.4591 -0.1961 218 VAL   V O   
39364 C  CB  . VAL   V  217 ? 1.9108 1.1996 1.7978 -0.0041 -0.4780 -0.0672 218 VAL   V CB  
39365 C  CG1 . VAL   V  217 ? 1.8890 1.1784 1.7982 -0.0280 -0.4694 -0.0784 218 VAL   V CG1 
39366 C  CG2 . VAL   V  217 ? 1.9220 1.2113 1.7806 0.0214  -0.4591 -0.0296 218 VAL   V CG2 
39367 N  N   . ASN   V  218 ? 1.9952 1.4987 1.9582 0.0112  -0.4094 -0.2113 219 ASN   V N   
39368 C  CA  . ASN   V  218 ? 2.0299 1.4944 2.0397 0.0203  -0.3547 -0.2322 219 ASN   V CA  
39369 C  C   . ASN   V  218 ? 1.9812 1.4679 2.0588 0.0043  -0.3190 -0.1509 219 ASN   V C   
39370 O  O   . ASN   V  218 ? 1.9754 1.3312 2.0459 -0.0021 -0.2882 -0.1027 219 ASN   V O   
39371 C  CB  . ASN   V  218 ? 2.0690 1.6304 2.1091 0.0595  -0.3414 -0.3169 219 ASN   V CB  
39372 C  CG  . ASN   V  218 ? 2.1225 1.6196 2.2208 0.0922  -0.3255 -0.4061 219 ASN   V CG  
39373 O  OD1 . ASN   V  218 ? 2.1110 1.8917 2.3600 0.0815  -0.3416 -0.5109 219 ASN   V OD1 
39374 N  ND2 . ASN   V  218 ? 2.0571 1.7898 2.2598 0.1235  -0.3208 -0.3842 219 ASN   V ND2 
39375 N  N   . ILE   V  219 ? 2.0133 1.5089 1.9554 0.0674  -0.3831 -0.0932 220 ILE   V N   
39376 C  CA  . ILE   V  219 ? 1.9823 1.5944 1.9354 0.0582  -0.4078 -0.1245 220 ILE   V CA  
39377 C  C   . ILE   V  219 ? 1.9690 1.6117 1.9742 0.1467  -0.3510 -0.1342 220 ILE   V C   
39378 O  O   . ILE   V  219 ? 1.8946 1.6355 1.9045 0.1062  -0.3631 -0.1956 220 ILE   V O   
39379 C  CB  . ILE   V  219 ? 2.0220 1.4395 1.8880 0.0433  -0.4329 -0.0849 220 ILE   V CB  
39380 C  CG1 . ILE   V  219 ? 2.0400 1.4112 1.8774 0.0313  -0.4649 -0.0662 220 ILE   V CG1 
39381 C  CG2 . ILE   V  219 ? 1.9746 1.4065 1.9021 0.0661  -0.4339 -0.0090 220 ILE   V CG2 
39382 C  CD1 . ILE   V  219 ? 2.0545 1.3372 1.8927 0.0100  -0.4428 -0.0708 220 ILE   V CD1 
39383 N  N   . CYS   V  220 ? 1.9250 1.9938 2.0085 0.1163  -0.3525 -0.2168 221 CYS   V N   
39384 C  CA  . CYS   V  220 ? 1.8733 2.0234 2.1106 0.0958  -0.2900 -0.2089 221 CYS   V CA  
39385 C  C   . CYS   V  220 ? 1.8724 2.2627 2.1508 0.1306  -0.2457 -0.1730 221 CYS   V C   
39386 O  O   . CYS   V  220 ? 1.7950 2.4595 2.2310 0.1222  -0.1559 -0.1762 221 CYS   V O   
39387 C  CB  . CYS   V  220 ? 1.8486 2.1287 2.1532 0.0819  -0.2801 -0.2383 221 CYS   V CB  
39388 S  SG  . CYS   V  220 ? 1.7858 2.2348 2.1906 0.1079  -0.3308 -0.2413 221 CYS   V SG  
39389 N  N   . ASP   V  221 ? 1.8323 2.2531 2.1531 0.0980  -0.2665 -0.0907 222 ASP   V N   
39390 C  CA  . ASP   V  221 ? 1.7770 2.3463 1.9860 0.1186  -0.3489 -0.0818 222 ASP   V CA  
39391 C  C   . ASP   V  221 ? 1.8318 2.3253 1.9885 0.0854  -0.3305 -0.2048 222 ASP   V C   
39392 O  O   . ASP   V  221 ? 1.7839 2.5221 1.3268 0.1109  -0.3881 -0.3474 222 ASP   V O   
39393 C  CB  . ASP   V  221 ? 1.6686 2.4141 2.1053 0.1248  -0.3618 0.0055  222 ASP   V CB  
39394 C  CG  . ASP   V  221 ? 1.5417 2.4261 2.1346 0.0813  -0.3746 0.0505  222 ASP   V CG  
39395 O  OD1 . ASP   V  221 ? 1.5490 2.4172 2.1575 0.0753  -0.4261 0.1179  222 ASP   V OD1 
39396 O  OD2 . ASP   V  221 ? 1.3876 2.5824 2.2861 0.0345  -0.2842 0.0686  222 ASP   V OD2 
39397 N  N   . SER   W  2   ? 1.9247 1.4258 1.9159 0.0527  -0.1084 0.1786  1   SER   W N   
39398 C  CA  . SER   W  2   ? 1.8671 1.3886 1.8959 0.0334  -0.1127 0.1144  1   SER   W CA  
39399 C  C   . SER   W  2   ? 1.9106 1.2989 1.7401 0.0649  -0.2081 0.0935  1   SER   W C   
39400 O  O   . SER   W  2   ? 1.9653 1.2588 1.7124 0.1470  -0.1844 0.0731  1   SER   W O   
39401 C  CB  . SER   W  2   ? 1.8427 1.4300 1.9613 0.0132  -0.0610 0.1119  1   SER   W CB  
39402 O  OG  . SER   W  2   ? 1.7661 1.5287 2.0169 -0.0116 -0.0317 0.0997  1   SER   W OG  
39403 N  N   . ASP   W  3   ? 1.9094 1.2059 1.6276 0.0179  -0.2715 0.0344  2   ASP   W N   
39404 C  CA  . ASP   W  3   ? 1.9792 1.0618 1.4514 0.0347  -0.3490 0.0385  2   ASP   W CA  
39405 C  C   . ASP   W  3   ? 1.9679 0.8773 1.4913 0.0691  -0.3074 0.0914  2   ASP   W C   
39406 O  O   . ASP   W  3   ? 1.8869 0.9036 1.5413 0.0209  -0.3227 -0.0065 2   ASP   W O   
39407 C  CB  . ASP   W  3   ? 2.0157 1.1269 1.3202 0.0347  -0.3170 0.0509  2   ASP   W CB  
39408 C  CG  . ASP   W  3   ? 2.1401 1.0733 1.2242 0.0250  -0.3595 0.1328  2   ASP   W CG  
39409 O  OD1 . ASP   W  3   ? 2.0887 1.0537 1.2940 0.1054  -0.4000 0.0896  2   ASP   W OD1 
39410 O  OD2 . ASP   W  3   ? 2.1175 1.1368 1.2186 -0.0505 -0.3471 0.1616  2   ASP   W OD2 
39411 N  N   . PRO   W  4   ? 1.8435 0.8620 1.4024 0.0449  -0.3975 0.0635  3   PRO   W N   
39412 C  CA  . PRO   W  4   ? 1.8124 0.7895 1.4357 0.0441  -0.3725 0.0725  3   PRO   W CA  
39413 C  C   . PRO   W  4   ? 1.7856 0.6552 1.4902 0.0941  -0.2917 0.0825  3   PRO   W C   
39414 O  O   . PRO   W  4   ? 1.9092 0.4770 1.4934 0.1123  -0.2719 0.0964  3   PRO   W O   
39415 C  CB  . PRO   W  4   ? 1.7677 0.7940 1.3890 0.0046  -0.4181 0.0593  3   PRO   W CB  
39416 C  CG  . PRO   W  4   ? 1.7963 0.8856 1.4062 0.0058  -0.4269 0.0260  3   PRO   W CG  
39417 C  CD  . PRO   W  4   ? 1.8391 0.9080 1.4170 0.0692  -0.4067 0.0527  3   PRO   W CD  
39418 N  N   . SER   W  5   ? 1.7626 0.6845 1.4698 0.1209  -0.3147 0.0697  4   SER   W N   
39419 C  CA  . SER   W  5   ? 1.7454 0.7568 1.4565 0.1516  -0.2674 0.0738  4   SER   W CA  
39420 C  C   . SER   W  5   ? 1.7789 0.7930 1.5056 0.1277  -0.2570 0.1461  4   SER   W C   
39421 O  O   . SER   W  5   ? 1.7539 0.7818 1.5458 0.1549  -0.1948 0.2641  4   SER   W O   
39422 C  CB  . SER   W  5   ? 1.7038 0.8096 1.4500 0.1593  -0.2787 0.0380  4   SER   W CB  
39423 O  OG  . SER   W  5   ? 1.7106 0.8543 1.5046 0.1407  -0.3004 -0.0008 4   SER   W OG  
39424 N  N   . SER   W  6   ? 1.7578 0.7473 1.5192 0.1004  -0.3585 0.1261  5   SER   W N   
39425 C  CA  . SER   W  6   ? 1.7625 0.7284 1.5020 0.0368  -0.3923 0.1402  5   SER   W CA  
39426 C  C   . SER   W  6   ? 1.7835 0.7183 1.4125 0.0422  -0.4224 0.1111  5   SER   W C   
39427 O  O   . SER   W  6   ? 1.8370 0.7981 1.3244 0.1226  -0.4722 0.2420  5   SER   W O   
39428 C  CB  . SER   W  6   ? 1.7691 0.7825 1.5214 0.1058  -0.4234 0.1167  5   SER   W CB  
39429 O  OG  . SER   W  6   ? 1.7838 0.9488 1.5424 0.1557  -0.5045 0.1312  5   SER   W OG  
39430 N  N   . ILE   W  7   ? 1.7483 0.5719 1.3803 -0.0543 -0.4248 0.1384  6   ILE   W N   
39431 C  CA  . ILE   W  7   ? 1.7776 0.6096 1.4308 -0.0603 -0.3778 0.1266  6   ILE   W CA  
39432 C  C   . ILE   W  7   ? 1.7731 0.6072 1.4432 -0.0520 -0.3707 0.1029  6   ILE   W C   
39433 O  O   . ILE   W  7   ? 1.8768 0.4430 1.5277 -0.1499 -0.3075 0.0606  6   ILE   W O   
39434 C  CB  . ILE   W  7   ? 1.7474 0.6718 1.4298 -0.0593 -0.4092 0.1373  6   ILE   W CB  
39435 C  CG1 . ILE   W  7   ? 1.7712 0.6908 1.4960 -0.0763 -0.4281 0.0752  6   ILE   W CG1 
39436 C  CG2 . ILE   W  7   ? 1.7770 0.7381 1.4317 -0.0731 -0.4015 0.1477  6   ILE   W CG2 
39437 C  CD1 . ILE   W  7   ? 1.7988 0.6603 1.5885 -0.0613 -0.3758 0.0308  6   ILE   W CD1 
39438 N  N   . ASN   W  8   ? 1.7286 0.6124 1.4067 -0.0305 -0.3498 0.1001  7   ASN   W N   
39439 C  CA  . ASN   W  8   ? 1.6824 0.5865 1.3922 0.0159  -0.3335 0.0877  7   ASN   W CA  
39440 C  C   . ASN   W  8   ? 1.6909 0.5852 1.3660 0.0479  -0.3566 0.0821  7   ASN   W C   
39441 O  O   . ASN   W  8   ? 1.6552 0.6045 1.3389 0.1026  -0.3465 0.0008  7   ASN   W O   
39442 C  CB  . ASN   W  8   ? 1.6637 0.5871 1.3856 -0.0556 -0.3273 0.1077  7   ASN   W CB  
39443 C  CG  . ASN   W  8   ? 1.6698 0.5819 1.3841 -0.0570 -0.3005 0.0998  7   ASN   W CG  
39444 O  OD1 . ASN   W  8   ? 1.6589 0.6428 1.3191 -0.1234 -0.3560 0.1164  7   ASN   W OD1 
39445 N  ND2 . ASN   W  8   ? 1.7352 0.5367 1.3652 -0.0245 -0.2915 0.1528  7   ASN   W ND2 
39446 N  N   . GLY   W  9   ? 1.6618 0.5596 1.3661 0.0572  -0.3560 0.1158  8   GLY   W N   
39447 C  CA  . GLY   W  9   ? 1.6455 0.5199 1.3668 0.0385  -0.3821 0.1363  8   GLY   W CA  
39448 C  C   . GLY   W  9   ? 1.6872 0.4029 1.3329 0.0751  -0.3862 0.1191  8   GLY   W C   
39449 O  O   . GLY   W  9   ? 1.7717 0.4083 1.3261 0.1318  -0.4018 0.1396  8   GLY   W O   
39450 N  N   . GLY   W  10  ? 1.6350 0.4683 1.2938 0.0051  -0.4164 0.1120  9   GLY   W N   
39451 C  CA  . GLY   W  10  ? 1.6242 0.5214 1.2270 -0.0012 -0.4271 0.0728  9   GLY   W CA  
39452 C  C   . GLY   W  10  ? 1.6021 0.5317 1.2208 -0.0373 -0.4347 0.0387  9   GLY   W C   
39453 O  O   . GLY   W  10  ? 1.6112 0.5134 1.2055 -0.0654 -0.3964 -0.0018 9   GLY   W O   
39454 N  N   . ILE   W  11  ? 1.5933 0.5879 1.1785 -0.0208 -0.4635 0.0307  10  ILE   W N   
39455 C  CA  . ILE   W  11  ? 1.5383 0.6500 1.1789 -0.0081 -0.4808 0.0235  10  ILE   W CA  
39456 C  C   . ILE   W  11  ? 1.4996 0.6804 1.1937 0.0005  -0.4750 -0.0239 10  ILE   W C   
39457 O  O   . ILE   W  11  ? 1.4210 0.6794 1.1645 0.0576  -0.4893 0.0227  10  ILE   W O   
39458 C  CB  . ILE   W  11  ? 1.5213 0.6379 1.2059 -0.0071 -0.5127 0.0607  10  ILE   W CB  
39459 C  CG1 . ILE   W  11  ? 1.5283 0.6949 1.2398 -0.0163 -0.5340 0.0909  10  ILE   W CG1 
39460 C  CG2 . ILE   W  11  ? 1.5509 0.6202 1.1973 -0.0105 -0.5061 0.0672  10  ILE   W CG2 
39461 C  CD1 . ILE   W  11  ? 1.5283 0.7397 1.2975 -0.0078 -0.5189 0.0764  10  ILE   W CD1 
39462 N  N   . VAL   W  12  ? 1.5111 0.6858 1.1893 -0.0293 -0.4333 -0.0852 11  VAL   W N   
39463 C  CA  . VAL   W  12  ? 1.5362 0.7002 1.2137 -0.0482 -0.4309 -0.1340 11  VAL   W CA  
39464 C  C   . VAL   W  12  ? 1.5542 0.7119 1.2197 -0.0497 -0.4311 -0.1723 11  VAL   W C   
39465 O  O   . VAL   W  12  ? 1.5877 0.5961 1.2617 -0.0810 -0.3831 -0.2123 11  VAL   W O   
39466 C  CB  . VAL   W  12  ? 1.5531 0.6948 1.2138 -0.0433 -0.4038 -0.1395 11  VAL   W CB  
39467 C  CG1 . VAL   W  12  ? 1.5613 0.6761 1.2124 -0.0374 -0.4073 -0.1429 11  VAL   W CG1 
39468 C  CG2 . VAL   W  12  ? 1.5488 0.6988 1.2125 -0.0442 -0.4059 -0.1346 11  VAL   W CG2 
39469 N  N   . VAL   W  13  ? 1.5695 0.7814 1.1862 -0.0375 -0.4903 -0.2162 12  VAL   W N   
39470 C  CA  . VAL   W  13  ? 1.6087 0.7626 1.1618 -0.0144 -0.4872 -0.2208 12  VAL   W CA  
39471 C  C   . VAL   W  13  ? 1.6487 0.7533 1.1853 -0.0319 -0.4583 -0.1956 12  VAL   W C   
39472 O  O   . VAL   W  13  ? 1.7094 0.7962 1.2185 -0.0371 -0.4242 -0.2760 12  VAL   W O   
39473 C  CB  . VAL   W  13  ? 1.6526 0.7594 1.1497 -0.0033 -0.5220 -0.2297 12  VAL   W CB  
39474 C  CG1 . VAL   W  13  ? 1.6821 0.7579 1.1725 0.0239  -0.5384 -0.2041 12  VAL   W CG1 
39475 C  CG2 . VAL   W  13  ? 1.6621 0.7746 1.1502 0.0022  -0.5174 -0.2327 12  VAL   W CG2 
39476 N  N   . ALA   W  14  ? 1.6595 0.6604 1.2379 -0.0260 -0.4569 -0.1568 13  ALA   W N   
39477 C  CA  . ALA   W  14  ? 1.6867 0.6061 1.2999 -0.0115 -0.4371 -0.1393 13  ALA   W CA  
39478 C  C   . ALA   W  14  ? 1.6605 0.5923 1.3683 0.0044  -0.4256 -0.1104 13  ALA   W C   
39479 O  O   . ALA   W  14  ? 1.6325 0.6605 1.3156 0.0172  -0.3886 -0.1036 13  ALA   W O   
39480 C  CB  . ALA   W  14  ? 1.6983 0.5624 1.3279 -0.0458 -0.4311 -0.1421 13  ALA   W CB  
39481 N  N   . MET   W  15  ? 1.6843 0.5867 1.3981 0.0073  -0.4649 -0.1288 14  MET   W N   
39482 C  CA  . MET   W  15  ? 1.7171 0.7104 1.4465 0.0104  -0.4375 -0.1470 14  MET   W CA  
39483 C  C   . MET   W  15  ? 1.7304 0.6836 1.4827 0.0265  -0.3899 -0.1297 14  MET   W C   
39484 O  O   . MET   W  15  ? 1.7174 0.6509 1.5291 0.0203  -0.3834 -0.1452 14  MET   W O   
39485 C  CB  . MET   W  15  ? 1.7659 0.7871 1.4875 0.0292  -0.5064 -0.1285 14  MET   W CB  
39486 C  CG  . MET   W  15  ? 1.8315 0.8509 1.4846 0.0125  -0.5519 -0.1920 14  MET   W CG  
39487 S  SD  . MET   W  15  ? 1.9184 0.8839 1.5298 0.0615  -0.6341 -0.2506 14  MET   W SD  
39488 C  CE  . MET   W  15  ? 1.9237 0.8767 1.5414 0.0445  -0.6229 -0.2432 14  MET   W CE  
39489 N  N   . THR   W  16  ? 1.7572 0.7088 1.5148 0.0321  -0.3574 -0.1087 15  THR   W N   
39490 C  CA  . THR   W  16  ? 1.7413 0.7320 1.5615 0.0323  -0.3398 -0.1045 15  THR   W CA  
39491 C  C   . THR   W  16  ? 1.7388 0.8023 1.6292 0.0524  -0.3296 -0.0696 15  THR   W C   
39492 O  O   . THR   W  16  ? 1.7240 0.7703 1.6150 0.0383  -0.3264 -0.0311 15  THR   W O   
39493 C  CB  . THR   W  16  ? 1.7590 0.7103 1.5677 0.0684  -0.3180 -0.0994 15  THR   W CB  
39494 O  OG1 . THR   W  16  ? 1.8275 0.7492 1.5811 0.0469  -0.2740 -0.1229 15  THR   W OG1 
39495 C  CG2 . THR   W  16  ? 1.7680 0.6811 1.5349 0.0807  -0.3141 -0.0796 15  THR   W CG2 
39496 N  N   . GLY   W  17  ? 1.6832 0.9180 1.6747 0.0504  -0.3551 -0.0657 16  GLY   W N   
39497 C  CA  . GLY   W  17  ? 1.6870 1.0571 1.7416 0.0660  -0.3294 -0.0007 16  GLY   W CA  
39498 C  C   . GLY   W  17  ? 1.6997 1.1395 1.7971 0.0453  -0.2966 0.0553  16  GLY   W C   
39499 O  O   . GLY   W  17  ? 1.6845 1.1826 1.7989 0.0772  -0.1909 0.1185  16  GLY   W O   
39500 N  N   . LYS   W  18  ? 1.7119 1.1952 1.8299 -0.0219 -0.3228 0.0691  17  LYS   W N   
39501 C  CA  . LYS   W  18  ? 1.7072 1.1813 1.8744 -0.0329 -0.3366 0.0463  17  LYS   W CA  
39502 C  C   . LYS   W  18  ? 1.7048 1.0657 1.9787 -0.0583 -0.3608 0.0672  17  LYS   W C   
39503 O  O   . LYS   W  18  ? 1.7220 1.0228 1.9780 -0.0726 -0.3375 0.1105  17  LYS   W O   
39504 C  CB  . LYS   W  18  ? 1.6980 1.3248 1.9227 -0.0220 -0.3268 0.0600  17  LYS   W CB  
39505 C  CG  . LYS   W  18  ? 1.6853 1.4302 1.9674 -0.0369 -0.2965 0.0833  17  LYS   W CG  
39506 C  CD  . LYS   W  18  ? 1.6905 1.5299 2.0105 0.0120  -0.2952 0.1110  17  LYS   W CD  
39507 C  CE  . LYS   W  18  ? 1.6932 1.5886 2.0703 0.0000  -0.2630 0.1320  17  LYS   W CE  
39508 N  NZ  . LYS   W  18  ? 1.7272 1.6111 2.0486 -0.0018 -0.2360 0.1416  17  LYS   W NZ  
39509 N  N   . ASP   W  19  ? 1.7069 0.9816 1.9817 -0.0821 -0.3775 0.0149  18  ASP   W N   
39510 C  CA  . ASP   W  19  ? 1.6909 0.9672 2.0113 -0.0186 -0.4089 0.0426  18  ASP   W CA  
39511 C  C   . ASP   W  19  ? 1.6205 0.8196 1.9753 0.0245  -0.4482 0.0187  18  ASP   W C   
39512 O  O   . ASP   W  19  ? 1.5994 0.8353 1.9992 0.0976  -0.4715 -0.0062 18  ASP   W O   
39513 C  CB  . ASP   W  19  ? 1.7320 1.0250 2.0435 -0.0725 -0.4069 0.0375  18  ASP   W CB  
39514 C  CG  . ASP   W  19  ? 1.7320 1.0387 2.0828 -0.1268 -0.4039 0.0536  18  ASP   W CG  
39515 O  OD1 . ASP   W  19  ? 1.7893 1.1007 2.0520 -0.1366 -0.4064 0.0481  18  ASP   W OD1 
39516 O  OD2 . ASP   W  19  ? 1.7042 0.9922 2.0946 -0.1982 -0.3794 0.0554  18  ASP   W OD2 
39517 N  N   . CYS   W  20  ? 1.6260 0.7765 1.9143 0.0499  -0.4673 -0.0039 19  CYS   W N   
39518 C  CA  . CYS   W  20  ? 1.6729 0.8204 1.8568 0.0752  -0.4482 -0.0616 19  CYS   W CA  
39519 C  C   . CYS   W  20  ? 1.6741 0.8008 1.7665 0.0935  -0.4384 -0.0611 19  CYS   W C   
39520 O  O   . CYS   W  20  ? 1.7459 0.9084 1.7553 0.0524  -0.4248 -0.0710 19  CYS   W O   
39521 C  CB  . CYS   W  20  ? 1.6817 0.8565 1.8754 0.1037  -0.4782 -0.0857 19  CYS   W CB  
39522 S  SG  . CYS   W  20  ? 1.7237 0.8514 1.9443 0.0797  -0.4759 -0.1268 19  CYS   W SG  
39523 N  N   . VAL   W  21  ? 1.7215 0.7323 1.6509 0.1501  -0.4300 -0.0850 20  VAL   W N   
39524 C  CA  . VAL   W  21  ? 1.7379 0.7743 1.5584 0.1311  -0.4082 -0.1118 20  VAL   W CA  
39525 C  C   . VAL   W  21  ? 1.7418 0.7948 1.5369 0.0988  -0.4145 -0.1322 20  VAL   W C   
39526 O  O   . VAL   W  21  ? 1.8342 0.9275 1.5246 0.1624  -0.3879 -0.1705 20  VAL   W O   
39527 C  CB  . VAL   W  21  ? 1.7353 0.7704 1.5535 0.1271  -0.4148 -0.1295 20  VAL   W CB  
39528 C  CG1 . VAL   W  21  ? 1.7370 0.8189 1.5558 0.1286  -0.4032 -0.1464 20  VAL   W CG1 
39529 C  CG2 . VAL   W  21  ? 1.7774 0.7818 1.6064 0.0987  -0.4068 -0.1575 20  VAL   W CG2 
39530 N  N   . ALA   W  22  ? 1.6942 0.8261 1.4641 0.0723  -0.4493 -0.1205 21  ALA   W N   
39531 C  CA  . ALA   W  22  ? 1.6686 0.7046 1.4701 0.0677  -0.5005 -0.1246 21  ALA   W CA  
39532 C  C   . ALA   W  22  ? 1.6545 0.6285 1.4132 0.0835  -0.4789 -0.0883 21  ALA   W C   
39533 O  O   . ALA   W  22  ? 1.6717 0.5737 1.3465 0.1002  -0.4802 0.0333  21  ALA   W O   
39534 C  CB  . ALA   W  22  ? 1.6751 0.7086 1.4811 0.0706  -0.5187 -0.1210 21  ALA   W CB  
39535 N  N   . ILE   W  23  ? 1.6346 0.5700 1.3858 0.0765  -0.5020 -0.1150 22  ILE   W N   
39536 C  CA  . ILE   W  23  ? 1.6356 0.5540 1.3106 0.0669  -0.5144 -0.1011 22  ILE   W CA  
39537 C  C   . ILE   W  23  ? 1.6588 0.6028 1.2391 0.0844  -0.5230 -0.1267 22  ILE   W C   
39538 O  O   . ILE   W  23  ? 1.6931 0.5376 1.2012 0.1018  -0.4990 -0.0906 22  ILE   W O   
39539 C  CB  . ILE   W  23  ? 1.6091 0.5755 1.3295 0.0579  -0.5496 -0.0828 22  ILE   W CB  
39540 C  CG1 . ILE   W  23  ? 1.6218 0.5876 1.3708 0.0252  -0.5186 -0.0973 22  ILE   W CG1 
39541 C  CG2 . ILE   W  23  ? 1.6049 0.6264 1.2927 0.0751  -0.5756 -0.0816 22  ILE   W CG2 
39542 C  CD1 . ILE   W  23  ? 1.6113 0.6035 1.3808 0.0322  -0.5057 -0.0957 22  ILE   W CD1 
39543 N  N   . ALA   W  24  ? 1.6333 0.6165 1.2183 0.0736  -0.5286 -0.0919 23  ALA   W N   
39544 C  CA  . ALA   W  24  ? 1.6464 0.6307 1.2026 0.1160  -0.5499 -0.0687 23  ALA   W CA  
39545 C  C   . ALA   W  24  ? 1.6209 0.5980 1.2225 0.1434  -0.4819 -0.0395 23  ALA   W C   
39546 O  O   . ALA   W  24  ? 1.6466 0.6760 1.2128 0.1576  -0.4672 -0.0382 23  ALA   W O   
39547 C  CB  . ALA   W  24  ? 1.6538 0.6268 1.2029 0.1165  -0.5683 -0.0402 23  ALA   W CB  
39548 N  N   . CYS   W  25  ? 1.6243 0.5872 1.1783 0.1693  -0.4985 -0.0531 24  CYS   W N   
39549 C  CA  . CYS   W  25  ? 1.6552 0.6323 1.2027 0.1253  -0.4887 -0.0579 24  CYS   W CA  
39550 C  C   . CYS   W  25  ? 1.6280 0.6466 1.1779 0.1287  -0.5362 -0.0584 24  CYS   W C   
39551 O  O   . CYS   W  25  ? 1.6120 0.6776 1.2132 0.1387  -0.5550 -0.0784 24  CYS   W O   
39552 C  CB  . CYS   W  25  ? 1.6451 0.6671 1.2065 0.1340  -0.4823 -0.0582 24  CYS   W CB  
39553 S  SG  . CYS   W  25  ? 1.7063 0.7406 1.2370 0.0557  -0.5081 -0.1204 24  CYS   W SG  
39554 N  N   . ASP   W  26  ? 1.6248 0.6651 1.2287 0.1171  -0.5307 -0.0144 25  ASP   W N   
39555 C  CA  . ASP   W  26  ? 1.6251 0.6372 1.2569 0.1464  -0.5743 0.0248  25  ASP   W CA  
39556 C  C   . ASP   W  26  ? 1.6126 0.6743 1.2215 0.1463  -0.5945 0.0095  25  ASP   W C   
39557 O  O   . ASP   W  26  ? 1.5536 0.6501 1.1780 0.1101  -0.6003 -0.0207 25  ASP   W O   
39558 C  CB  . ASP   W  26  ? 1.6415 0.5709 1.3152 0.1523  -0.5682 0.0667  25  ASP   W CB  
39559 C  CG  . ASP   W  26  ? 1.6413 0.5518 1.3658 0.1630  -0.5629 0.0839  25  ASP   W CG  
39560 O  OD1 . ASP   W  26  ? 1.6385 0.5986 1.3727 0.1724  -0.5696 0.1214  25  ASP   W OD1 
39561 O  OD2 . ASP   W  26  ? 1.6812 0.4776 1.4486 0.2018  -0.5556 0.1511  25  ASP   W OD2 
39562 N  N   . LEU   W  27  ? 1.6297 0.6857 1.2230 0.1554  -0.5940 0.0187  26  LEU   W N   
39563 C  CA  . LEU   W  27  ? 1.6270 0.6945 1.2829 0.1777  -0.5823 0.0138  26  LEU   W CA  
39564 C  C   . LEU   W  27  ? 1.6336 0.6020 1.3042 0.1869  -0.5678 0.0089  26  LEU   W C   
39565 O  O   . LEU   W  27  ? 1.6203 0.5577 1.3837 0.2742  -0.5669 0.0520  26  LEU   W O   
39566 C  CB  . LEU   W  27  ? 1.6543 0.7570 1.3243 0.1477  -0.6315 0.0026  26  LEU   W CB  
39567 C  CG  . LEU   W  27  ? 1.6827 0.7247 1.2781 0.1373  -0.6822 -0.0457 26  LEU   W CG  
39568 C  CD1 . LEU   W  27  ? 1.7159 0.7728 1.2845 0.1281  -0.7005 -0.0660 26  LEU   W CD1 
39569 C  CD2 . LEU   W  27  ? 1.6580 0.7092 1.2519 0.1205  -0.6816 -0.0754 26  LEU   W CD2 
39570 N  N   . ARG   W  28  ? 1.6173 0.6102 1.2963 0.1429  -0.5199 0.0097  27  ARG   W N   
39571 C  CA  . ARG   W  28  ? 1.6225 0.6751 1.3071 0.1250  -0.4712 -0.0058 27  ARG   W CA  
39572 C  C   . ARG   W  28  ? 1.6043 0.6388 1.3070 0.1218  -0.4467 -0.0197 27  ARG   W C   
39573 O  O   . ARG   W  28  ? 1.6045 0.6475 1.3004 0.0814  -0.4034 -0.0443 27  ARG   W O   
39574 C  CB  . ARG   W  28  ? 1.6387 0.7084 1.3365 0.0504  -0.4250 -0.0456 27  ARG   W CB  
39575 C  CG  . ARG   W  28  ? 1.7067 0.7264 1.4061 0.0104  -0.3646 -0.0765 27  ARG   W CG  
39576 C  CD  . ARG   W  28  ? 1.7628 0.7436 1.4798 -0.0276 -0.3145 -0.1138 27  ARG   W CD  
39577 N  NE  . ARG   W  28  ? 1.8289 0.7179 1.5203 -0.0750 -0.2698 -0.1803 27  ARG   W NE  
39578 C  CZ  . ARG   W  28  ? 1.7884 0.6881 1.5028 -0.0830 -0.2242 -0.1819 27  ARG   W CZ  
39579 N  NH1 . ARG   W  28  ? 1.8114 0.5359 1.5136 -0.0998 -0.1722 -0.2085 27  ARG   W NH1 
39580 N  NH2 . ARG   W  28  ? 1.7442 0.8700 1.5966 -0.0910 -0.1461 -0.1816 27  ARG   W NH2 
39581 N  N   . LEU   W  29  ? 1.6109 0.5847 1.3108 0.1461  -0.4371 -0.0079 28  LEU   W N   
39582 C  CA  . LEU   W  29  ? 1.5789 0.6223 1.3469 0.0990  -0.4303 -0.0059 28  LEU   W CA  
39583 C  C   . LEU   W  29  ? 1.5903 0.5567 1.3280 0.1428  -0.4383 0.0230  28  LEU   W C   
39584 O  O   . LEU   W  29  ? 1.5597 0.4184 1.3141 0.1665  -0.4967 0.0177  28  LEU   W O   
39585 C  CB  . LEU   W  29  ? 1.5866 0.6217 1.3934 0.0908  -0.4311 -0.0166 28  LEU   W CB  
39586 C  CG  . LEU   W  29  ? 1.5714 0.6707 1.4280 0.0631  -0.4384 0.0138  28  LEU   W CG  
39587 C  CD1 . LEU   W  29  ? 1.5805 0.6868 1.4123 0.0431  -0.4402 0.0445  28  LEU   W CD1 
39588 C  CD2 . LEU   W  29  ? 1.5764 0.6834 1.4623 0.0656  -0.4199 0.0046  28  LEU   W CD2 
39589 N  N   . GLY   W  30  ? 1.5841 0.5761 1.3067 0.1394  -0.4495 0.0493  29  GLY   W N   
39590 C  CA  . GLY   W  30  ? 1.5773 0.6462 1.2848 0.1262  -0.4540 0.1185  29  GLY   W CA  
39591 C  C   . GLY   W  30  ? 1.6050 0.6688 1.2265 0.1345  -0.4727 0.1484  29  GLY   W C   
39592 O  O   . GLY   W  30  ? 1.5360 0.6660 1.1918 0.1922  -0.5118 0.1114  29  GLY   W O   
39593 N  N   . SER   W  31  ? 1.6155 0.7387 1.2188 0.1107  -0.4650 0.1808  30  SER   W N   
39594 C  CA  . SER   W  31  ? 1.5703 0.7898 1.2634 0.1027  -0.4243 0.1610  30  SER   W CA  
39595 C  C   . SER   W  31  ? 1.6446 0.8015 1.2205 0.0962  -0.3853 0.1617  30  SER   W C   
39596 O  O   . SER   W  31  ? 1.6664 0.7849 1.1599 0.1945  -0.5011 0.2375  30  SER   W O   
39597 C  CB  . SER   W  31  ? 1.5970 0.7851 1.3363 0.0969  -0.3734 0.1606  30  SER   W CB  
39598 O  OG  . SER   W  31  ? 1.5460 0.7867 1.4376 0.0990  -0.3534 0.1576  30  SER   W OG  
39599 N  N   . GLN   W  32  ? 1.6942 0.8581 1.2752 0.0984  -0.3250 0.0524  31  GLN   W N   
39600 C  CA  . GLN   W  32  ? 1.6795 0.8763 1.2787 0.1004  -0.3344 0.0248  31  GLN   W CA  
39601 C  C   . GLN   W  32  ? 1.6630 0.8184 1.1998 0.0806  -0.3370 -0.0265 31  GLN   W C   
39602 O  O   . GLN   W  32  ? 1.6658 0.7940 0.9386 0.1027  -0.4364 -0.0591 31  GLN   W O   
39603 C  CB  . GLN   W  32  ? 1.6844 0.9959 1.3261 0.0947  -0.3460 -0.0442 31  GLN   W CB  
39604 C  CG  . GLN   W  32  ? 1.7620 1.1099 1.2728 0.1271  -0.3534 -0.0802 31  GLN   W CG  
39605 C  CD  . GLN   W  32  ? 1.7645 1.2919 1.3483 0.1346  -0.3475 -0.1151 31  GLN   W CD  
39606 O  OE1 . GLN   W  32  ? 1.9212 1.4711 1.3175 0.1912  -0.3381 -0.1695 31  GLN   W OE1 
39607 N  NE2 . GLN   W  32  ? 1.8370 1.3806 1.3951 0.1743  -0.3045 -0.1406 31  GLN   W NE2 
39608 N  N   . SER   W  33  ? 1.7243 0.8314 1.2292 0.0676  -0.3026 -0.0305 32  SER   W N   
39609 C  CA  . SER   W  33  ? 1.7433 0.7454 1.3047 0.0488  -0.3125 -0.0444 32  SER   W CA  
39610 C  C   . SER   W  33  ? 1.7489 0.7445 1.3006 0.0639  -0.3731 0.0026  32  SER   W C   
39611 O  O   . SER   W  33  ? 1.7839 0.7158 1.2655 0.1196  -0.3821 0.0025  32  SER   W O   
39612 C  CB  . SER   W  33  ? 1.7811 0.7318 1.4004 0.0269  -0.2593 -0.1118 32  SER   W CB  
39613 O  OG  . SER   W  33  ? 1.8227 0.6131 1.4652 -0.0424 -0.2040 -0.1917 32  SER   W OG  
39614 N  N   . LEU   W  34  ? 1.7070 0.6715 1.3158 0.0604  -0.3942 0.0495  33  LEU   W N   
39615 C  CA  . LEU   W  34  ? 1.7108 0.6538 1.2746 0.0475  -0.4438 0.1248  33  LEU   W CA  
39616 C  C   . LEU   W  34  ? 1.7176 0.6522 1.2629 0.0407  -0.4705 0.1101  33  LEU   W C   
39617 O  O   . LEU   W  34  ? 1.6977 0.5825 1.3377 0.0508  -0.4693 0.0781  33  LEU   W O   
39618 C  CB  . LEU   W  34  ? 1.7049 0.6369 1.2372 0.0439  -0.4514 0.1412  33  LEU   W CB  
39619 C  CG  . LEU   W  34  ? 1.6922 0.6164 1.2141 0.0411  -0.4622 0.1629  33  LEU   W CG  
39620 C  CD1 . LEU   W  34  ? 1.7219 0.6488 1.2019 0.0241  -0.4559 0.1775  33  LEU   W CD1 
39621 C  CD2 . LEU   W  34  ? 1.7060 0.5996 1.2032 0.0464  -0.4512 0.1633  33  LEU   W CD2 
39622 N  N   . GLY   W  35  ? 1.7545 0.6573 1.2588 0.0535  -0.4901 0.1386  34  GLY   W N   
39623 C  CA  . GLY   W  35  ? 1.7492 0.6253 1.3009 0.0692  -0.4948 0.1665  34  GLY   W CA  
39624 C  C   . GLY   W  35  ? 1.7715 0.5900 1.3575 0.1066  -0.4877 0.1741  34  GLY   W C   
39625 O  O   . GLY   W  35  ? 1.8401 0.5547 1.4139 0.1569  -0.4939 0.2654  34  GLY   W O   
39626 N  N   . VAL   W  36  ? 1.7100 0.5696 1.3789 0.1103  -0.5031 0.1101  35  VAL   W N   
39627 C  CA  . VAL   W  36  ? 1.7291 0.5101 1.4237 0.1220  -0.4989 0.1280  35  VAL   W CA  
39628 C  C   . VAL   W  36  ? 1.7817 0.4159 1.4511 0.1377  -0.4960 0.1117  35  VAL   W C   
39629 O  O   . VAL   W  36  ? 1.7910 0.4257 1.4558 0.1214  -0.5159 0.0867  35  VAL   W O   
39630 C  CB  . VAL   W  36  ? 1.6951 0.4600 1.3994 0.1093  -0.4836 0.1013  35  VAL   W CB  
39631 C  CG1 . VAL   W  36  ? 1.6583 0.4260 1.4115 0.1287  -0.4979 0.1207  35  VAL   W CG1 
39632 C  CG2 . VAL   W  36  ? 1.6893 0.5067 1.4447 0.0811  -0.4737 0.1101  35  VAL   W CG2 
39633 N  N   . SER   W  37  ? 1.8110 0.3929 1.4496 0.1592  -0.4758 0.1003  36  SER   W N   
39634 C  CA  . SER   W  37  ? 1.8329 0.4437 1.3997 0.1728  -0.5067 0.0224  36  SER   W CA  
39635 C  C   . SER   W  37  ? 1.8547 0.3955 1.4019 0.1668  -0.5086 0.0039  36  SER   W C   
39636 O  O   . SER   W  37  ? 1.8227 0.3833 1.4488 0.1821  -0.4753 -0.0200 36  SER   W O   
39637 C  CB  . SER   W  37  ? 1.8170 0.4599 1.3797 0.2304  -0.4915 0.0020  36  SER   W CB  
39638 O  OG  . SER   W  37  ? 1.7929 0.4486 1.3778 0.2752  -0.4826 -0.0397 36  SER   W OG  
39639 N  N   . ASN   W  38  ? 1.9412 0.4078 1.3631 0.1581  -0.5370 0.0121  37  ASN   W N   
39640 C  CA  . ASN   W  38  ? 1.9457 0.6052 1.3904 0.0742  -0.5111 -0.0519 37  ASN   W CA  
39641 C  C   . ASN   W  38  ? 1.8838 0.7164 1.2676 0.0409  -0.5925 -0.1380 37  ASN   W C   
39642 O  O   . ASN   W  38  ? 1.8903 0.7011 1.2409 -0.0291 -0.6426 -0.2939 37  ASN   W O   
39643 C  CB  . ASN   W  38  ? 2.1276 0.7430 1.4576 0.0933  -0.5260 0.0632  37  ASN   W CB  
39644 C  CG  . ASN   W  38  ? 2.2583 0.9471 1.4429 0.1083  -0.4937 0.0361  37  ASN   W CG  
39645 O  OD1 . ASN   W  38  ? 2.4048 1.1172 1.5518 0.0391  -0.5240 0.3518  37  ASN   W OD1 
39646 N  ND2 . ASN   W  38  ? 2.2620 0.9051 1.4306 0.0941  -0.5688 0.0385  37  ASN   W ND2 
39647 N  N   . LYS   W  39  ? 1.8437 0.7294 1.1959 0.0302  -0.6121 -0.1483 38  LYS   W N   
39648 C  CA  . LYS   W  39  ? 1.8419 0.7599 1.2274 -0.0093 -0.5904 -0.1391 38  LYS   W CA  
39649 C  C   . LYS   W  39  ? 1.7838 0.7603 1.2347 -0.0083 -0.5798 -0.1341 38  LYS   W C   
39650 O  O   . LYS   W  39  ? 1.8067 0.7825 1.1984 -0.0291 -0.5933 -0.1972 38  LYS   W O   
39651 C  CB  . LYS   W  39  ? 1.9103 0.8148 1.2643 0.0137  -0.5490 -0.1584 38  LYS   W CB  
39652 C  CG  . LYS   W  39  ? 1.9600 0.8719 1.2628 0.0259  -0.5796 -0.1796 38  LYS   W CG  
39653 C  CD  . LYS   W  39  ? 1.9510 0.9339 1.2697 0.0381  -0.5860 -0.1922 38  LYS   W CD  
39654 C  CE  . LYS   W  39  ? 1.9198 0.9900 1.3357 0.0673  -0.6440 -0.1876 38  LYS   W CE  
39655 N  NZ  . LYS   W  39  ? 1.9210 0.9588 1.3829 0.0528  -0.6738 -0.2073 38  LYS   W NZ  
39656 N  N   . PHE   W  40  ? 1.7426 0.7058 1.2168 0.0002  -0.5665 -0.1040 39  PHE   W N   
39657 C  CA  . PHE   W  40  ? 1.6992 0.6706 1.2563 0.0161  -0.5207 -0.0622 39  PHE   W CA  
39658 C  C   . PHE   W  40  ? 1.6578 0.6521 1.2502 0.0167  -0.5462 -0.0592 39  PHE   W C   
39659 O  O   . PHE   W  40  ? 1.6284 0.5350 1.2417 -0.0108 -0.5662 -0.0157 39  PHE   W O   
39660 C  CB  . PHE   W  40  ? 1.6833 0.6421 1.2235 0.0143  -0.5097 -0.0210 39  PHE   W CB  
39661 C  CG  . PHE   W  40  ? 1.6952 0.6980 1.1930 0.0123  -0.4826 0.0151  39  PHE   W CG  
39662 C  CD1 . PHE   W  40  ? 1.7029 0.7650 1.1863 0.0489  -0.4610 0.0496  39  PHE   W CD1 
39663 C  CD2 . PHE   W  40  ? 1.6806 0.7109 1.1884 0.0216  -0.4737 0.0663  39  PHE   W CD2 
39664 C  CE1 . PHE   W  40  ? 1.7437 0.7209 1.1493 0.0384  -0.4171 0.0854  39  PHE   W CE1 
39665 C  CE2 . PHE   W  40  ? 1.7152 0.6789 1.1489 0.0142  -0.4283 0.0994  39  PHE   W CE2 
39666 C  CZ  . PHE   W  40  ? 1.7276 0.6571 1.1363 0.0322  -0.4352 0.1249  39  PHE   W CZ  
39667 N  N   . GLU   W  41  ? 1.6418 0.6988 1.2654 -0.0095 -0.5436 -0.0863 40  GLU   W N   
39668 C  CA  . GLU   W  41  ? 1.6513 0.6907 1.2507 -0.0236 -0.5357 -0.1127 40  GLU   W CA  
39669 C  C   . GLU   W  41  ? 1.6393 0.6395 1.2384 -0.0218 -0.5071 -0.1077 40  GLU   W C   
39670 O  O   . GLU   W  41  ? 1.6890 0.5350 1.1490 -0.0150 -0.4992 -0.1124 40  GLU   W O   
39671 C  CB  . GLU   W  41  ? 1.6776 0.7247 1.2926 -0.0441 -0.5238 -0.1539 40  GLU   W CB  
39672 C  CG  . GLU   W  41  ? 1.7248 0.7181 1.2811 -0.0761 -0.5553 -0.1948 40  GLU   W CG  
39673 C  CD  . GLU   W  41  ? 1.8171 0.6601 1.2683 -0.0806 -0.5745 -0.2519 40  GLU   W CD  
39674 O  OE1 . GLU   W  41  ? 1.8751 0.7363 1.2045 -0.1231 -0.5958 -0.3310 40  GLU   W OE1 
39675 O  OE2 . GLU   W  41  ? 1.8831 0.4801 1.4407 -0.0388 -0.5856 -0.3097 40  GLU   W OE2 
39676 N  N   . LYS   W  42  ? 1.6144 0.6624 1.2428 -0.0291 -0.5120 -0.1075 41  LYS   W N   
39677 C  CA  . LYS   W  42  ? 1.5936 0.6763 1.2629 -0.0249 -0.4948 -0.0543 41  LYS   W CA  
39678 C  C   . LYS   W  42  ? 1.5874 0.6390 1.3000 -0.0390 -0.5047 -0.0737 41  LYS   W C   
39679 O  O   . LYS   W  42  ? 1.5804 0.5932 1.2918 -0.0931 -0.4626 -0.0594 41  LYS   W O   
39680 C  CB  . LYS   W  42  ? 1.5913 0.6867 1.2936 0.0111  -0.4648 -0.0759 41  LYS   W CB  
39681 C  CG  . LYS   W  42  ? 1.5888 0.6998 1.3028 0.0172  -0.4433 -0.0726 41  LYS   W CG  
39682 C  CD  . LYS   W  42  ? 1.6050 0.7123 1.3164 0.0442  -0.4140 -0.0801 41  LYS   W CD  
39683 C  CE  . LYS   W  42  ? 1.6197 0.7550 1.2904 0.0623  -0.3996 -0.0522 41  LYS   W CE  
39684 N  NZ  . LYS   W  42  ? 1.6368 0.7948 1.2709 0.0720  -0.3979 -0.0731 41  LYS   W NZ  
39685 N  N   . ILE   W  43  ? 1.5749 0.6724 1.2741 -0.0204 -0.5281 -0.0268 42  ILE   W N   
39686 C  CA  . ILE   W  43  ? 1.5822 0.6815 1.2981 -0.0071 -0.4977 -0.0153 42  ILE   W CA  
39687 C  C   . ILE   W  43  ? 1.6063 0.7069 1.2923 -0.0026 -0.4672 -0.0330 42  ILE   W C   
39688 O  O   . ILE   W  43  ? 1.6363 0.7107 1.2828 -0.0117 -0.4459 -0.1146 42  ILE   W O   
39689 C  CB  . ILE   W  43  ? 1.5995 0.6763 1.3173 0.0189  -0.5164 0.0166  42  ILE   W CB  
39690 C  CG1 . ILE   W  43  ? 1.5699 0.6743 1.2676 0.0180  -0.5643 0.0205  42  ILE   W CG1 
39691 C  CG2 . ILE   W  43  ? 1.5886 0.7296 1.3561 -0.0036 -0.5088 0.0300  42  ILE   W CG2 
39692 C  CD1 . ILE   W  43  ? 1.5550 0.7055 1.2682 0.0116  -0.5815 -0.0078 42  ILE   W CD1 
39693 N  N   . PHE   W  44  ? 1.6000 0.6383 1.3184 0.0081  -0.4420 -0.0710 43  PHE   W N   
39694 C  CA  . PHE   W  44  ? 1.6177 0.6230 1.3194 0.0020  -0.4416 -0.0546 43  PHE   W CA  
39695 C  C   . PHE   W  44  ? 1.6594 0.6159 1.3517 -0.0108 -0.4703 -0.0001 43  PHE   W C   
39696 O  O   . PHE   W  44  ? 1.7236 0.4536 1.3532 -0.0166 -0.4644 0.0182  43  PHE   W O   
39697 C  CB  . PHE   W  44  ? 1.5899 0.5784 1.2976 -0.0187 -0.4106 -0.1004 43  PHE   W CB  
39698 C  CG  . PHE   W  44  ? 1.5453 0.5547 1.2936 -0.0029 -0.4180 -0.1424 43  PHE   W CG  
39699 C  CD1 . PHE   W  44  ? 1.5445 0.5399 1.2904 -0.0199 -0.4205 -0.1782 43  PHE   W CD1 
39700 C  CD2 . PHE   W  44  ? 1.5040 0.5103 1.3122 -0.0064 -0.4033 -0.1285 43  PHE   W CD2 
39701 C  CE1 . PHE   W  44  ? 1.5514 0.5328 1.3014 -0.0131 -0.4080 -0.1649 43  PHE   W CE1 
39702 C  CE2 . PHE   W  44  ? 1.5072 0.5295 1.3282 -0.0143 -0.3893 -0.1318 43  PHE   W CE2 
39703 C  CZ  . PHE   W  44  ? 1.5471 0.5333 1.3022 -0.0131 -0.4044 -0.1629 43  PHE   W CZ  
39704 N  N   . HIS   W  45  ? 1.6862 0.6511 1.3522 -0.0163 -0.5138 -0.0237 44  HIS   W N   
39705 C  CA  . HIS   W  45  ? 1.7371 0.6119 1.3698 -0.0022 -0.4880 -0.0292 44  HIS   W CA  
39706 C  C   . HIS   W  45  ? 1.7493 0.6099 1.3198 0.0002  -0.4822 -0.0691 44  HIS   W C   
39707 O  O   . HIS   W  45  ? 1.8074 0.3288 1.2930 0.0419  -0.5143 -0.1150 44  HIS   W O   
39708 C  CB  . HIS   W  45  ? 1.7600 0.7532 1.3811 -0.0443 -0.5121 0.0054  44  HIS   W CB  
39709 C  CG  . HIS   W  45  ? 1.8357 0.7828 1.3591 -0.0727 -0.5047 0.0453  44  HIS   W CG  
39710 N  ND1 . HIS   W  45  ? 1.8700 0.7992 1.3817 -0.0965 -0.4912 0.0332  44  HIS   W ND1 
39711 C  CD2 . HIS   W  45  ? 1.8604 0.8392 1.3501 -0.0766 -0.5015 0.0633  44  HIS   W CD2 
39712 C  CE1 . HIS   W  45  ? 1.8811 0.8236 1.3846 -0.0716 -0.4976 0.0810  44  HIS   W CE1 
39713 N  NE2 . HIS   W  45  ? 1.8644 0.8086 1.3754 -0.0756 -0.5086 0.0597  44  HIS   W NE2 
39714 N  N   . TYR   W  46  ? 1.7440 0.5290 1.3541 0.0556  -0.4894 -0.0650 45  TYR   W N   
39715 C  CA  . TYR   W  46  ? 1.6789 0.5238 1.3481 0.0387  -0.4681 -0.0688 45  TYR   W CA  
39716 C  C   . TYR   W  46  ? 1.6879 0.4595 1.3439 0.0328  -0.4850 -0.0677 45  TYR   W C   
39717 O  O   . TYR   W  46  ? 1.6415 0.4667 1.3844 0.0560  -0.4279 -0.1586 45  TYR   W O   
39718 C  CB  . TYR   W  46  ? 1.6566 0.5302 1.3358 0.0280  -0.4574 -0.1059 45  TYR   W CB  
39719 C  CG  . TYR   W  46  ? 1.6259 0.5269 1.3118 0.0395  -0.4678 -0.1301 45  TYR   W CG  
39720 C  CD1 . TYR   W  46  ? 1.6294 0.5097 1.2979 0.0273  -0.4689 -0.1647 45  TYR   W CD1 
39721 C  CD2 . TYR   W  46  ? 1.5911 0.5128 1.2991 0.0505  -0.4641 -0.1140 45  TYR   W CD2 
39722 C  CE1 . TYR   W  46  ? 1.5888 0.5208 1.2714 0.0450  -0.4550 -0.1405 45  TYR   W CE1 
39723 C  CE2 . TYR   W  46  ? 1.5742 0.5263 1.2453 0.0488  -0.4701 -0.1430 45  TYR   W CE2 
39724 C  CZ  . TYR   W  46  ? 1.5638 0.5354 1.2407 0.0389  -0.4771 -0.1395 45  TYR   W CZ  
39725 O  OH  . TYR   W  46  ? 1.5651 0.4895 1.1544 0.0557  -0.4861 -0.1794 45  TYR   W OH  
39726 N  N   . GLY   W  47  ? 1.6900 0.4259 1.3407 0.0273  -0.5296 -0.0095 46  GLY   W N   
39727 C  CA  . GLY   W  47  ? 1.6752 0.5014 1.3908 0.0526  -0.5370 0.0386  46  GLY   W CA  
39728 C  C   . GLY   W  47  ? 1.6899 0.4963 1.3839 0.0714  -0.5492 0.1021  46  GLY   W C   
39729 O  O   . GLY   W  47  ? 1.7417 0.5433 1.3903 0.0306  -0.4996 0.1239  46  GLY   W O   
39730 N  N   . HIS   W  48  ? 1.6843 0.5468 1.3896 0.0507  -0.5552 0.1330  47  HIS   W N   
39731 C  CA  . HIS   W  48  ? 1.6720 0.5634 1.4286 0.0611  -0.5508 0.1696  47  HIS   W CA  
39732 C  C   . HIS   W  48  ? 1.6513 0.5389 1.4048 0.0600  -0.5544 0.2087  47  HIS   W C   
39733 O  O   . HIS   W  48  ? 1.6007 0.5936 1.4404 0.0946  -0.5464 0.2594  47  HIS   W O   
39734 C  CB  . HIS   W  48  ? 1.6731 0.6121 1.4829 0.0402  -0.5472 0.1532  47  HIS   W CB  
39735 C  CG  . HIS   W  48  ? 1.6783 0.6774 1.4609 0.0111  -0.5318 0.1575  47  HIS   W CG  
39736 N  ND1 . HIS   W  48  ? 1.6845 0.7005 1.4991 0.0443  -0.5426 0.1806  47  HIS   W ND1 
39737 C  CD2 . HIS   W  48  ? 1.6508 0.6657 1.4734 -0.0029 -0.5241 0.1404  47  HIS   W CD2 
39738 C  CE1 . HIS   W  48  ? 1.6773 0.7211 1.4856 0.0535  -0.5408 0.1589  47  HIS   W CE1 
39739 N  NE2 . HIS   W  48  ? 1.6418 0.6891 1.4970 0.0128  -0.5364 0.1557  47  HIS   W NE2 
39740 N  N   . VAL   W  49  ? 1.6458 0.5131 1.4219 0.0511  -0.5451 0.2338  48  VAL   W N   
39741 C  CA  . VAL   W  49  ? 1.6659 0.5117 1.4448 0.0128  -0.4702 0.1852  48  VAL   W CA  
39742 C  C   . VAL   W  49  ? 1.6394 0.5851 1.4097 0.0000  -0.4327 0.1676  48  VAL   W C   
39743 O  O   . VAL   W  49  ? 1.6641 0.5760 1.3971 0.0320  -0.4193 0.2059  48  VAL   W O   
39744 C  CB  . VAL   W  49  ? 1.6700 0.4884 1.4132 -0.0013 -0.4728 0.1649  48  VAL   W CB  
39745 C  CG1 . VAL   W  49  ? 1.6648 0.4261 1.3960 -0.0197 -0.4355 0.1812  48  VAL   W CG1 
39746 C  CG2 . VAL   W  49  ? 1.6720 0.6053 1.4428 -0.0258 -0.4243 0.1966  48  VAL   W CG2 
39747 N  N   . PHE   W  50  ? 1.6282 0.6272 1.4270 0.0219  -0.4044 0.0711  49  PHE   W N   
39748 C  CA  . PHE   W  50  ? 1.5698 0.5973 1.4034 -0.0017 -0.4106 0.0034  49  PHE   W CA  
39749 C  C   . PHE   W  50  ? 1.5821 0.5619 1.3815 0.0032  -0.3937 -0.0213 49  PHE   W C   
39750 O  O   . PHE   W  50  ? 1.4712 0.5717 1.3881 -0.0211 -0.3898 -0.0141 49  PHE   W O   
39751 C  CB  . PHE   W  50  ? 1.5782 0.6058 1.4153 -0.0056 -0.4202 0.0222  49  PHE   W CB  
39752 C  CG  . PHE   W  50  ? 1.6092 0.6849 1.4315 -0.0299 -0.4264 -0.0017 49  PHE   W CG  
39753 C  CD1 . PHE   W  50  ? 1.6053 0.7554 1.4930 -0.0606 -0.4195 -0.0046 49  PHE   W CD1 
39754 C  CD2 . PHE   W  50  ? 1.6229 0.7048 1.4340 -0.0534 -0.4142 -0.0060 49  PHE   W CD2 
39755 C  CE1 . PHE   W  50  ? 1.6176 0.8067 1.5042 -0.0855 -0.4289 -0.0085 49  PHE   W CE1 
39756 C  CE2 . PHE   W  50  ? 1.6452 0.7747 1.4484 -0.0509 -0.4458 0.0034  49  PHE   W CE2 
39757 C  CZ  . PHE   W  50  ? 1.6444 0.8053 1.4758 -0.0697 -0.4624 -0.0123 49  PHE   W CZ  
39758 N  N   . LEU   W  51  ? 1.6050 0.5419 1.3362 -0.0166 -0.4032 -0.0346 50  LEU   W N   
39759 C  CA  . LEU   W  51  ? 1.6481 0.5985 1.3432 -0.0174 -0.4432 -0.0421 50  LEU   W CA  
39760 C  C   . LEU   W  51  ? 1.6766 0.6640 1.3136 -0.0378 -0.4319 -0.0190 50  LEU   W C   
39761 O  O   . LEU   W  51  ? 1.6951 0.6946 1.3057 -0.0078 -0.4613 -0.0853 50  LEU   W O   
39762 C  CB  . LEU   W  51  ? 1.6582 0.5985 1.3334 -0.0207 -0.4603 -0.0280 50  LEU   W CB  
39763 C  CG  . LEU   W  51  ? 1.6971 0.5997 1.2825 -0.0371 -0.4606 -0.0450 50  LEU   W CG  
39764 C  CD1 . LEU   W  51  ? 1.7272 0.6122 1.2767 -0.0581 -0.4870 -0.0744 50  LEU   W CD1 
39765 C  CD2 . LEU   W  51  ? 1.6772 0.6226 1.2919 -0.0353 -0.4745 -0.0470 50  LEU   W CD2 
39766 N  N   . GLY   W  52  ? 1.6874 0.6903 1.3283 -0.0636 -0.4335 -0.0485 51  GLY   W N   
39767 C  CA  . GLY   W  52  ? 1.6498 0.6597 1.3013 -0.0430 -0.4698 -0.0553 51  GLY   W CA  
39768 C  C   . GLY   W  52  ? 1.6189 0.6177 1.2736 -0.0376 -0.4498 -0.0244 51  GLY   W C   
39769 O  O   . GLY   W  52  ? 1.6408 0.6144 1.2808 -0.0051 -0.4804 0.0055  51  GLY   W O   
39770 N  N   . ILE   W  53  ? 1.5296 0.6284 1.2759 -0.0290 -0.4985 -0.0306 52  ILE   W N   
39771 C  CA  . ILE   W  53  ? 1.5176 0.6488 1.2677 0.0009  -0.5156 -0.0178 52  ILE   W CA  
39772 C  C   . ILE   W  53  ? 1.5102 0.6698 1.2094 0.0061  -0.5557 0.0119  52  ILE   W C   
39773 O  O   . ILE   W  53  ? 1.5143 0.7821 1.1947 -0.0111 -0.5625 -0.0105 52  ILE   W O   
39774 C  CB  . ILE   W  53  ? 1.4946 0.6631 1.3112 -0.0065 -0.5086 -0.0257 52  ILE   W CB  
39775 C  CG1 . ILE   W  53  ? 1.4832 0.7032 1.3542 -0.0501 -0.5022 -0.0497 52  ILE   W CG1 
39776 C  CG2 . ILE   W  53  ? 1.4774 0.6032 1.3413 -0.0335 -0.4967 -0.0221 52  ILE   W CG2 
39777 C  CD1 . ILE   W  53  ? 1.4989 0.7619 1.3738 -0.0388 -0.4913 -0.0961 52  ILE   W CD1 
39778 N  N   . THR   W  54  ? 1.5211 0.5636 1.2046 0.0410  -0.5476 0.0583  53  THR   W N   
39779 C  CA  . THR   W  54  ? 1.5701 0.4902 1.2164 0.1038  -0.5128 0.0627  53  THR   W CA  
39780 C  C   . THR   W  54  ? 1.5547 0.3919 1.2106 0.0713  -0.4783 0.0419  53  THR   W C   
39781 O  O   . THR   W  54  ? 1.6010 0.4417 1.1553 0.0842  -0.4964 0.0433  53  THR   W O   
39782 C  CB  . THR   W  54  ? 1.5489 0.4683 1.2026 0.1177  -0.5207 0.1053  53  THR   W CB  
39783 O  OG1 . THR   W  54  ? 1.5603 0.3971 1.2352 0.1487  -0.5114 0.1919  53  THR   W OG1 
39784 C  CG2 . THR   W  54  ? 1.5600 0.5117 1.2323 0.1162  -0.5418 0.0911  53  THR   W CG2 
39785 N  N   . GLY   W  55  ? 1.5986 0.3447 1.2339 0.0901  -0.4411 0.0315  54  GLY   W N   
39786 C  CA  . GLY   W  55  ? 1.5963 0.3417 1.2271 0.1133  -0.4451 0.0325  54  GLY   W CA  
39787 C  C   . GLY   W  55  ? 1.5989 0.3161 1.2597 0.1353  -0.4332 0.0220  54  GLY   W C   
39788 O  O   . GLY   W  55  ? 1.6638 0.3561 1.2625 0.1978  -0.4134 0.0427  54  GLY   W O   
39789 N  N   . LEU   W  56  ? 1.6201 0.2253 1.1927 0.1222  -0.4705 0.0445  55  LEU   W N   
39790 C  CA  . LEU   W  56  ? 1.6157 0.2628 1.2340 0.1260  -0.4558 0.0679  55  LEU   W CA  
39791 C  C   . LEU   W  56  ? 1.6611 0.2941 1.1950 0.1254  -0.4800 0.0822  55  LEU   W C   
39792 O  O   . LEU   W  56  ? 1.6595 0.3504 1.1618 0.1218  -0.5041 0.1584  55  LEU   W O   
39793 C  CB  . LEU   W  56  ? 1.5829 0.2246 1.2573 0.1273  -0.4344 0.0351  55  LEU   W CB  
39794 C  CG  . LEU   W  56  ? 1.5730 0.2365 1.3200 0.1329  -0.4205 0.0355  55  LEU   W CG  
39795 C  CD1 . LEU   W  56  ? 1.5837 0.2629 1.3269 0.1007  -0.4068 0.0835  55  LEU   W CD1 
39796 C  CD2 . LEU   W  56  ? 1.5460 0.2309 1.3279 0.1323  -0.4164 0.0195  55  LEU   W CD2 
39797 N  N   . ALA   W  57  ? 1.7414 0.3806 1.1910 0.0815  -0.4333 0.0929  56  ALA   W N   
39798 C  CA  . ALA   W  57  ? 1.7250 0.4786 1.2022 0.0286  -0.4297 0.0789  56  ALA   W CA  
39799 C  C   . ALA   W  57  ? 1.6611 0.5523 1.1953 0.0604  -0.4106 0.0385  56  ALA   W C   
39800 O  O   . ALA   W  57  ? 1.6821 0.6841 1.1982 -0.0162 -0.4294 0.0238  56  ALA   W O   
39801 C  CB  . ALA   W  57  ? 1.7328 0.4741 1.2239 0.0417  -0.4477 0.0950  56  ALA   W CB  
39802 N  N   . THR   W  58  ? 1.6333 0.5862 1.2027 0.0384  -0.3716 0.0010  57  THR   W N   
39803 C  CA  . THR   W  58  ? 1.5685 0.5749 1.2054 0.0062  -0.3443 -0.0489 57  THR   W CA  
39804 C  C   . THR   W  58  ? 1.5827 0.6036 1.1803 0.0406  -0.2949 -0.0567 57  THR   W C   
39805 O  O   . THR   W  58  ? 1.6684 0.6142 1.2262 0.0211  -0.2265 -0.0726 57  THR   W O   
39806 C  CB  . THR   W  58  ? 1.5678 0.5287 1.1890 -0.0130 -0.3541 -0.0667 57  THR   W CB  
39807 O  OG1 . THR   W  58  ? 1.5329 0.5275 1.1960 -0.0261 -0.3953 -0.0878 57  THR   W OG1 
39808 C  CG2 . THR   W  58  ? 1.5306 0.5305 1.1840 -0.0147 -0.3693 -0.0532 57  THR   W CG2 
39809 N  N   . ASP   W  59  ? 1.5429 0.5627 1.1746 0.0396  -0.2988 -0.0433 58  ASP   W N   
39810 C  CA  . ASP   W  59  ? 1.4907 0.5497 1.2147 0.0106  -0.2968 -0.0410 58  ASP   W CA  
39811 C  C   . ASP   W  59  ? 1.5029 0.5447 1.1600 0.0015  -0.3221 -0.0712 58  ASP   W C   
39812 O  O   . ASP   W  59  ? 1.4507 0.5722 1.1242 -0.0336 -0.3321 -0.0817 58  ASP   W O   
39813 C  CB  . ASP   W  59  ? 1.4623 0.5023 1.2180 0.0110  -0.2411 -0.0318 58  ASP   W CB  
39814 C  CG  . ASP   W  59  ? 1.4404 0.4822 1.2745 -0.0322 -0.1999 -0.0595 58  ASP   W CG  
39815 O  OD1 . ASP   W  59  ? 1.4151 0.7149 1.4137 -0.0366 -0.0879 -0.0337 58  ASP   W OD1 
39816 O  OD2 . ASP   W  59  ? 1.4110 0.2880 1.2989 -0.0115 -0.0935 -0.0813 58  ASP   W OD2 
39817 N  N   . VAL   W  60  ? 1.4971 0.5993 1.1645 -0.0103 -0.3584 -0.0576 59  VAL   W N   
39818 C  CA  . VAL   W  60  ? 1.5257 0.6261 1.1704 -0.0388 -0.3812 -0.0514 59  VAL   W CA  
39819 C  C   . VAL   W  60  ? 1.5367 0.6373 1.2169 -0.0363 -0.3621 -0.0769 59  VAL   W C   
39820 O  O   . VAL   W  60  ? 1.5439 0.6351 1.2200 -0.0490 -0.3651 -0.1114 59  VAL   W O   
39821 C  CB  . VAL   W  60  ? 1.5539 0.6966 1.1406 -0.0424 -0.4154 0.0018  59  VAL   W CB  
39822 C  CG1 . VAL   W  60  ? 1.5572 0.7055 1.1647 -0.0531 -0.4341 0.0397  59  VAL   W CG1 
39823 C  CG2 . VAL   W  60  ? 1.5603 0.6941 1.1125 -0.0170 -0.4161 0.0192  59  VAL   W CG2 
39824 N  N   . THR   W  61  ? 1.5282 0.6319 1.2412 -0.0471 -0.3482 -0.0999 60  THR   W N   
39825 C  CA  . THR   W  61  ? 1.5253 0.6429 1.2409 -0.0581 -0.3703 -0.1116 60  THR   W CA  
39826 C  C   . THR   W  61  ? 1.5004 0.6819 1.2773 -0.0122 -0.4255 -0.1159 60  THR   W C   
39827 O  O   . THR   W  61  ? 1.5109 0.7067 1.3884 -0.0339 -0.4314 -0.1002 60  THR   W O   
39828 C  CB  . THR   W  61  ? 1.5401 0.6621 1.2170 -0.0567 -0.3633 -0.1282 60  THR   W CB  
39829 O  OG1 . THR   W  61  ? 1.5494 0.6737 1.1804 -0.0316 -0.3824 -0.1394 60  THR   W OG1 
39830 C  CG2 . THR   W  61  ? 1.5529 0.7009 1.1991 -0.0491 -0.3334 -0.1340 60  THR   W CG2 
39831 N  N   . THR   W  62  ? 1.4963 0.5371 1.2702 -0.0015 -0.4290 -0.1174 61  THR   W N   
39832 C  CA  . THR   W  62  ? 1.5062 0.5220 1.2446 -0.0056 -0.4292 -0.1239 61  THR   W CA  
39833 C  C   . THR   W  62  ? 1.5381 0.5631 1.2167 0.0374  -0.3979 -0.0853 61  THR   W C   
39834 O  O   . THR   W  62  ? 1.5907 0.5750 1.3040 -0.0257 -0.3527 -0.0617 61  THR   W O   
39835 C  CB  . THR   W  62  ? 1.4940 0.5005 1.2268 0.0281  -0.4412 -0.1042 61  THR   W CB  
39836 O  OG1 . THR   W  62  ? 1.4413 0.5353 1.2169 0.0878  -0.4451 -0.1072 61  THR   W OG1 
39837 C  CG2 . THR   W  62  ? 1.4662 0.4831 1.2157 -0.0086 -0.4543 -0.1082 61  THR   W CG2 
39838 N  N   . LEU   W  63  ? 1.6012 0.4253 1.2055 0.0350  -0.4220 -0.0813 62  LEU   W N   
39839 C  CA  . LEU   W  63  ? 1.6257 0.4151 1.2326 0.0335  -0.4121 -0.0721 62  LEU   W CA  
39840 C  C   . LEU   W  63  ? 1.6357 0.5003 1.2052 0.0510  -0.4366 -0.0912 62  LEU   W C   
39841 O  O   . LEU   W  63  ? 1.6332 0.6070 1.2410 -0.0232 -0.3692 -0.0785 62  LEU   W O   
39842 C  CB  . LEU   W  63  ? 1.6567 0.3680 1.2974 0.0573  -0.3956 -0.0540 62  LEU   W CB  
39843 C  CG  . LEU   W  63  ? 1.6838 0.3379 1.3280 0.0504  -0.3932 -0.1046 62  LEU   W CG  
39844 C  CD1 . LEU   W  63  ? 1.7092 0.2608 1.3743 0.0709  -0.3879 -0.0870 62  LEU   W CD1 
39845 C  CD2 . LEU   W  63  ? 1.6919 0.3612 1.3864 0.0694  -0.3902 -0.0849 62  LEU   W CD2 
39846 N  N   . ASN   W  64  ? 1.6270 0.5012 1.2073 0.0229  -0.4703 -0.1032 63  ASN   W N   
39847 C  CA  . ASN   W  64  ? 1.6561 0.5141 1.2891 -0.0123 -0.4755 -0.1494 63  ASN   W CA  
39848 C  C   . ASN   W  64  ? 1.6719 0.4941 1.2711 -0.0664 -0.4931 -0.1882 63  ASN   W C   
39849 O  O   . ASN   W  64  ? 1.6581 0.5337 1.2646 -0.1092 -0.4898 -0.2829 63  ASN   W O   
39850 C  CB  . ASN   W  64  ? 1.6448 0.5855 1.2382 -0.0327 -0.5273 -0.1808 63  ASN   W CB  
39851 C  CG  . ASN   W  64  ? 1.6824 0.5964 1.2467 -0.0248 -0.5303 -0.2201 63  ASN   W CG  
39852 O  OD1 . ASN   W  64  ? 1.6979 0.5605 1.2236 -0.0295 -0.5559 -0.1993 63  ASN   W OD1 
39853 N  ND2 . ASN   W  64  ? 1.6963 0.6234 1.2395 0.0011  -0.5261 -0.2543 63  ASN   W ND2 
39854 N  N   . GLU   W  65  ? 1.6855 0.4704 1.2706 -0.0901 -0.4756 -0.1789 64  GLU   W N   
39855 C  CA  . GLU   W  65  ? 1.6878 0.5198 1.3111 -0.0467 -0.4400 -0.1611 64  GLU   W CA  
39856 C  C   . GLU   W  65  ? 1.7056 0.5410 1.3690 -0.0131 -0.4463 -0.1213 64  GLU   W C   
39857 O  O   . GLU   W  65  ? 1.7399 0.4253 1.4887 0.0656  -0.3971 0.0766  64  GLU   W O   
39858 C  CB  . GLU   W  65  ? 1.7311 0.5243 1.3248 -0.1133 -0.4125 -0.1827 64  GLU   W CB  
39859 C  CG  . GLU   W  65  ? 1.7725 0.5031 1.3457 -0.1309 -0.3944 -0.1793 64  GLU   W CG  
39860 C  CD  . GLU   W  65  ? 1.8176 0.5162 1.3836 -0.1502 -0.3388 -0.2346 64  GLU   W CD  
39861 O  OE1 . GLU   W  65  ? 1.9391 0.5353 1.3673 -0.1543 -0.2950 -0.2502 64  GLU   W OE1 
39862 O  OE2 . GLU   W  65  ? 1.8508 0.4275 1.3130 -0.2008 -0.3706 -0.3276 64  GLU   W OE2 
39863 N  N   . MET   W  66  ? 1.6877 0.5585 1.3260 0.0470  -0.4389 -0.0938 65  MET   W N   
39864 C  CA  . MET   W  66  ? 1.6707 0.5403 1.3481 0.0736  -0.4352 -0.0810 65  MET   W CA  
39865 C  C   . MET   W  66  ? 1.6491 0.5345 1.3349 0.0634  -0.4684 -0.0855 65  MET   W C   
39866 O  O   . MET   W  66  ? 1.6652 0.5303 1.4097 0.0606  -0.4601 -0.0914 65  MET   W O   
39867 C  CB  . MET   W  66  ? 1.6926 0.5645 1.3340 0.1158  -0.4199 -0.1158 65  MET   W CB  
39868 C  CG  . MET   W  66  ? 1.7131 0.6485 1.3528 0.1512  -0.3955 -0.0820 65  MET   W CG  
39869 S  SD  . MET   W  66  ? 1.7743 0.7473 1.3215 0.1756  -0.3524 -0.1077 65  MET   W SD  
39870 C  CE  . MET   W  66  ? 1.7623 0.7847 1.3557 0.1072  -0.3254 -0.0817 65  MET   W CE  
39871 N  N   . PHE   W  67  ? 1.6427 0.4276 1.2886 0.0264  -0.4903 -0.0547 66  PHE   W N   
39872 C  CA  . PHE   W  67  ? 1.6597 0.4490 1.3207 0.0282  -0.4750 -0.0219 66  PHE   W CA  
39873 C  C   . PHE   W  67  ? 1.6998 0.5281 1.3534 0.0305  -0.4930 -0.0565 66  PHE   W C   
39874 O  O   . PHE   W  67  ? 1.7002 0.5864 1.5075 0.0081  -0.4336 -0.0718 66  PHE   W O   
39875 C  CB  . PHE   W  67  ? 1.6662 0.4184 1.2855 0.0112  -0.4927 -0.0309 66  PHE   W CB  
39876 C  CG  . PHE   W  67  ? 1.6787 0.4674 1.2469 0.0584  -0.4836 -0.0251 66  PHE   W CG  
39877 C  CD1 . PHE   W  67  ? 1.6644 0.4582 1.2392 0.0748  -0.4981 -0.0451 66  PHE   W CD1 
39878 C  CD2 . PHE   W  67  ? 1.6939 0.4740 1.2454 0.0480  -0.4799 -0.0674 66  PHE   W CD2 
39879 C  CE1 . PHE   W  67  ? 1.6245 0.4584 1.2305 0.0927  -0.4807 -0.0620 66  PHE   W CE1 
39880 C  CE2 . PHE   W  67  ? 1.6608 0.5143 1.1969 0.0575  -0.4967 -0.0280 66  PHE   W CE2 
39881 C  CZ  . PHE   W  67  ? 1.6166 0.4630 1.1994 0.0718  -0.4982 -0.0438 66  PHE   W CZ  
39882 N  N   . ARG   W  68  ? 1.6950 0.4980 1.3504 0.0048  -0.4881 -0.0647 67  ARG   W N   
39883 C  CA  . ARG   W  68  ? 1.6888 0.5345 1.4032 -0.0272 -0.5051 -0.0971 67  ARG   W CA  
39884 C  C   . ARG   W  68  ? 1.6213 0.5775 1.3789 -0.0148 -0.5566 -0.0947 67  ARG   W C   
39885 O  O   . ARG   W  68  ? 1.6010 0.6315 1.4412 -0.0387 -0.5175 -0.0203 67  ARG   W O   
39886 C  CB  . ARG   W  68  ? 1.7458 0.4715 1.4352 -0.0295 -0.4436 -0.1122 67  ARG   W CB  
39887 C  CG  . ARG   W  68  ? 1.8040 0.5213 1.4509 -0.0069 -0.4047 -0.1688 67  ARG   W CG  
39888 C  CD  . ARG   W  68  ? 1.8428 0.5337 1.4628 -0.0100 -0.3721 -0.1688 67  ARG   W CD  
39889 N  NE  . ARG   W  68  ? 1.8494 0.5064 1.5389 -0.0303 -0.3645 -0.2213 67  ARG   W NE  
39890 C  CZ  . ARG   W  68  ? 1.8255 0.6240 1.5702 -0.0528 -0.3494 -0.2197 67  ARG   W CZ  
39891 N  NH1 . ARG   W  68  ? 1.8878 0.6882 1.6454 0.0106  -0.3792 -0.1614 67  ARG   W NH1 
39892 N  NH2 . ARG   W  68  ? 1.8210 0.6377 1.6175 -0.0833 -0.3678 -0.2826 67  ARG   W NH2 
39893 N  N   . TYR   W  69  ? 1.6250 0.5611 1.3819 -0.0690 -0.5933 -0.1197 68  TYR   W N   
39894 C  CA  . TYR   W  69  ? 1.6810 0.4867 1.3494 -0.0951 -0.5642 -0.1070 68  TYR   W CA  
39895 C  C   . TYR   W  69  ? 1.6988 0.5021 1.2844 -0.0741 -0.5928 -0.0916 68  TYR   W C   
39896 O  O   . TYR   W  69  ? 1.7712 0.4914 1.2460 -0.0926 -0.5542 0.0141  68  TYR   W O   
39897 C  CB  . TYR   W  69  ? 1.6548 0.5186 1.4225 -0.0495 -0.5541 -0.1459 68  TYR   W CB  
39898 C  CG  . TYR   W  69  ? 1.7230 0.4226 1.4242 -0.0412 -0.5424 -0.1945 68  TYR   W CG  
39899 C  CD1 . TYR   W  69  ? 1.7115 0.3806 1.4078 -0.0402 -0.5477 -0.2153 68  TYR   W CD1 
39900 C  CD2 . TYR   W  69  ? 1.7477 0.3932 1.4286 -0.0093 -0.5460 -0.2428 68  TYR   W CD2 
39901 C  CE1 . TYR   W  69  ? 1.7017 0.4425 1.4149 -0.0149 -0.5769 -0.2564 68  TYR   W CE1 
39902 C  CE2 . TYR   W  69  ? 1.7337 0.4154 1.4154 -0.0083 -0.5859 -0.2750 68  TYR   W CE2 
39903 C  CZ  . TYR   W  69  ? 1.7232 0.4833 1.3957 -0.0289 -0.5772 -0.2865 68  TYR   W CZ  
39904 O  OH  . TYR   W  69  ? 1.6955 0.4908 1.4821 0.0069  -0.5875 -0.4195 68  TYR   W OH  
39905 N  N   . LYS   W  70  ? 1.6748 0.4485 1.1797 -0.0757 -0.5658 0.0106  69  LYS   W N   
39906 C  CA  . LYS   W  70  ? 1.7218 0.4740 1.1780 -0.0637 -0.5392 0.0073  69  LYS   W CA  
39907 C  C   . LYS   W  70  ? 1.7038 0.5860 1.1347 -0.0440 -0.5881 -0.0321 69  LYS   W C   
39908 O  O   . LYS   W  70  ? 1.8026 0.6056 1.0989 -0.1143 -0.5468 -0.0691 69  LYS   W O   
39909 C  CB  . LYS   W  70  ? 1.7127 0.4142 1.1665 -0.0533 -0.5047 0.0329  69  LYS   W CB  
39910 C  CG  . LYS   W  70  ? 1.7120 0.4115 1.1517 -0.0422 -0.4983 0.0019  69  LYS   W CG  
39911 C  CD  . LYS   W  70  ? 1.7378 0.3886 1.1799 -0.0158 -0.4765 -0.0246 69  LYS   W CD  
39912 C  CE  . LYS   W  70  ? 1.7396 0.4433 1.2160 0.0195  -0.4631 -0.0625 69  LYS   W CE  
39913 N  NZ  . LYS   W  70  ? 1.7895 0.4544 1.2149 0.0699  -0.4436 -0.0727 69  LYS   W NZ  
39914 N  N   . THR   W  71  ? 1.7384 0.5541 1.1353 -0.0394 -0.5774 -0.0062 70  THR   W N   
39915 C  CA  . THR   W  71  ? 1.7430 0.5924 1.1959 -0.0431 -0.5396 -0.0277 70  THR   W CA  
39916 C  C   . THR   W  71  ? 1.7830 0.6151 1.1836 -0.0606 -0.5175 -0.0371 70  THR   W C   
39917 O  O   . THR   W  71  ? 1.8458 0.6934 1.1603 -0.1383 -0.5532 -0.0349 70  THR   W O   
39918 C  CB  . THR   W  71  ? 1.7195 0.6086 1.2094 -0.0130 -0.5359 -0.0802 70  THR   W CB  
39919 O  OG1 . THR   W  71  ? 1.6859 0.6037 1.1854 0.0203  -0.5696 -0.0622 70  THR   W OG1 
39920 C  CG2 . THR   W  71  ? 1.7006 0.5906 1.2241 -0.0312 -0.5153 -0.0838 70  THR   W CG2 
39921 N  N   . ASN   W  72  ? 1.7705 0.6056 1.1742 -0.0394 -0.5238 -0.0613 71  ASN   W N   
39922 C  CA  . ASN   W  72  ? 1.7470 0.6399 1.1540 -0.0172 -0.5055 -0.0716 71  ASN   W CA  
39923 C  C   . ASN   W  72  ? 1.7297 0.6323 1.1929 -0.0195 -0.5111 -0.0687 71  ASN   W C   
39924 O  O   . ASN   W  72  ? 1.7677 0.6214 1.3331 -0.0451 -0.4762 -0.0452 71  ASN   W O   
39925 C  CB  . ASN   W  72  ? 1.7622 0.6394 1.1095 0.0031  -0.5108 -0.0920 71  ASN   W CB  
39926 C  CG  . ASN   W  72  ? 1.7610 0.6263 1.0975 0.0305  -0.4750 -0.0962 71  ASN   W CG  
39927 O  OD1 . ASN   W  72  ? 1.7693 0.5115 1.0448 0.0208  -0.5064 -0.0755 71  ASN   W OD1 
39928 N  ND2 . ASN   W  72  ? 1.8015 0.6923 1.1102 0.0510  -0.4528 -0.0813 71  ASN   W ND2 
39929 N  N   . LEU   W  73  ? 1.7020 0.5913 1.1479 -0.0425 -0.4827 -0.0635 72  LEU   W N   
39930 C  CA  . LEU   W  73  ? 1.6755 0.6301 1.0975 -0.0666 -0.4787 -0.0376 72  LEU   W CA  
39931 C  C   . LEU   W  73  ? 1.6610 0.6203 1.1236 -0.0496 -0.4699 -0.0274 72  LEU   W C   
39932 O  O   . LEU   W  73  ? 1.6658 0.6357 1.1562 -0.0881 -0.4266 -0.0315 72  LEU   W O   
39933 C  CB  . LEU   W  73  ? 1.6698 0.6375 1.0373 -0.0866 -0.4586 -0.0131 72  LEU   W CB  
39934 C  CG  . LEU   W  73  ? 1.6773 0.6599 1.0142 -0.1035 -0.4594 0.0050  72  LEU   W CG  
39935 C  CD1 . LEU   W  73  ? 1.6718 0.6918 0.9739 -0.0997 -0.4446 0.0230  72  LEU   W CD1 
39936 C  CD2 . LEU   W  73  ? 1.6746 0.6522 1.0393 -0.1141 -0.4665 -0.0021 72  LEU   W CD2 
39937 N  N   . TYR   W  74  ? 1.6362 0.5551 1.1635 -0.0281 -0.4994 0.0288  73  TYR   W N   
39938 C  CA  . TYR   W  74  ? 1.6117 0.5216 1.2282 -0.0131 -0.4892 0.0382  73  TYR   W CA  
39939 C  C   . TYR   W  74  ? 1.6497 0.5600 1.3160 -0.0306 -0.5155 0.0002  73  TYR   W C   
39940 O  O   . TYR   W  74  ? 1.6267 0.6570 1.3204 -0.0973 -0.5288 0.0329  73  TYR   W O   
39941 C  CB  . TYR   W  74  ? 1.5649 0.5049 1.2323 -0.0038 -0.4944 0.0731  73  TYR   W CB  
39942 C  CG  . TYR   W  74  ? 1.5786 0.5040 1.3003 0.0090  -0.4557 0.0785  73  TYR   W CG  
39943 C  CD1 . TYR   W  74  ? 1.5791 0.5117 1.3363 -0.0146 -0.4469 0.0773  73  TYR   W CD1 
39944 C  CD2 . TYR   W  74  ? 1.5613 0.4703 1.2998 -0.0069 -0.4336 0.0390  73  TYR   W CD2 
39945 C  CE1 . TYR   W  74  ? 1.5837 0.5011 1.3803 -0.0409 -0.4223 0.0700  73  TYR   W CE1 
39946 C  CE2 . TYR   W  74  ? 1.5712 0.4666 1.3550 -0.0248 -0.4011 0.0285  73  TYR   W CE2 
39947 C  CZ  . TYR   W  74  ? 1.5622 0.4808 1.3660 -0.0447 -0.3836 0.0436  73  TYR   W CZ  
39948 O  OH  . TYR   W  74  ? 1.5629 0.4794 1.4297 -0.0768 -0.3474 0.0246  73  TYR   W OH  
39949 N  N   . LYS   W  75  ? 1.7175 0.5284 1.3073 0.0028  -0.5126 -0.0253 74  LYS   W N   
39950 C  CA  . LYS   W  75  ? 1.7391 0.5572 1.3960 0.0048  -0.5233 -0.0852 74  LYS   W CA  
39951 C  C   . LYS   W  75  ? 1.7767 0.5417 1.4466 -0.0168 -0.5230 -0.0863 74  LYS   W C   
39952 O  O   . LYS   W  75  ? 1.8740 0.4070 1.5394 -0.0190 -0.5169 -0.1089 74  LYS   W O   
39953 C  CB  . LYS   W  75  ? 1.7576 0.5690 1.3924 0.0571  -0.5279 -0.1009 74  LYS   W CB  
39954 C  CG  . LYS   W  75  ? 1.7566 0.6624 1.4395 0.0843  -0.5404 -0.1269 74  LYS   W CG  
39955 C  CD  . LYS   W  75  ? 1.8050 0.7240 1.4220 0.1358  -0.5341 -0.1321 74  LYS   W CD  
39956 C  CE  . LYS   W  75  ? 1.7974 0.8571 1.5278 0.1357  -0.5311 -0.1551 74  LYS   W CE  
39957 N  NZ  . LYS   W  75  ? 1.8408 0.9352 1.5402 0.1526  -0.5293 -0.1228 74  LYS   W NZ  
39958 N  N   . LEU   W  76  ? 1.8053 0.5117 1.4471 0.0313  -0.5198 -0.1065 75  LEU   W N   
39959 C  CA  . LEU   W  76  ? 1.8460 0.5271 1.4804 0.0317  -0.5366 -0.1496 75  LEU   W CA  
39960 C  C   . LEU   W  76  ? 1.8588 0.5772 1.5024 0.0085  -0.5305 -0.1227 75  LEU   W C   
39961 O  O   . LEU   W  76  ? 1.9097 0.5827 1.5556 -0.0076 -0.5232 -0.1152 75  LEU   W O   
39962 C  CB  . LEU   W  76  ? 1.8591 0.4908 1.3920 0.0641  -0.5370 -0.1546 75  LEU   W CB  
39963 C  CG  . LEU   W  76  ? 1.8677 0.4745 1.3833 0.0982  -0.5614 -0.1625 75  LEU   W CG  
39964 C  CD1 . LEU   W  76  ? 1.8482 0.4307 1.3020 0.1119  -0.5799 -0.1959 75  LEU   W CD1 
39965 C  CD2 . LEU   W  76  ? 1.8930 0.4932 1.4206 0.0890  -0.5812 -0.1796 75  LEU   W CD2 
39966 N  N   . LYS   W  77  ? 1.8249 0.5232 1.5557 -0.0264 -0.5182 -0.1803 76  LYS   W N   
39967 C  CA  . LYS   W  77  ? 1.7907 0.5257 1.5514 -0.0581 -0.5201 -0.1826 76  LYS   W CA  
39968 C  C   . LYS   W  77  ? 1.7687 0.5434 1.5924 -0.0150 -0.5200 -0.1931 76  LYS   W C   
39969 O  O   . LYS   W  77  ? 1.7033 0.6458 1.5920 0.0023  -0.5142 -0.0982 76  LYS   W O   
39970 C  CB  . LYS   W  77  ? 1.8064 0.5518 1.5636 -0.0819 -0.5030 -0.2229 76  LYS   W CB  
39971 C  CG  . LYS   W  77  ? 1.7971 0.6471 1.5448 -0.1361 -0.5212 -0.2852 76  LYS   W CG  
39972 C  CD  . LYS   W  77  ? 1.8058 0.7443 1.5044 -0.1374 -0.4955 -0.3687 76  LYS   W CD  
39973 C  CE  . LYS   W  77  ? 1.8382 0.7715 1.4154 -0.1601 -0.5023 -0.4351 76  LYS   W CE  
39974 N  NZ  . LYS   W  77  ? 1.8163 0.9172 1.3827 -0.1762 -0.4807 -0.4965 76  LYS   W NZ  
39975 N  N   . GLU   W  78  ? 1.7875 0.4726 1.5667 -0.0613 -0.4883 -0.1611 77  GLU   W N   
39976 C  CA  . GLU   W  78  ? 1.8029 0.5948 1.5906 -0.0989 -0.4566 -0.0838 77  GLU   W CA  
39977 C  C   . GLU   W  78  ? 1.7854 0.5251 1.6588 -0.1237 -0.4543 -0.0717 77  GLU   W C   
39978 O  O   . GLU   W  78  ? 1.8065 0.4914 1.7401 -0.0848 -0.4101 0.0044  77  GLU   W O   
39979 C  CB  . GLU   W  78  ? 1.8197 0.6421 1.5440 -0.0164 -0.4101 -0.0853 77  GLU   W CB  
39980 C  CG  . GLU   W  78  ? 1.8200 0.7366 1.4600 -0.0080 -0.3914 -0.0600 77  GLU   W CG  
39981 C  CD  . GLU   W  78  ? 1.8294 0.7950 1.4631 0.0273  -0.3784 -0.0447 77  GLU   W CD  
39982 O  OE1 . GLU   W  78  ? 1.8196 0.8830 1.5185 0.0562  -0.3244 -0.0115 77  GLU   W OE1 
39983 O  OE2 . GLU   W  78  ? 1.8374 0.7625 1.3780 0.0934  -0.3775 -0.0304 77  GLU   W OE2 
39984 N  N   . GLU   W  79  ? 1.7983 0.6518 1.6482 -0.1343 -0.5018 -0.0903 78  GLU   W N   
39985 C  CA  . GLU   W  79  ? 1.7931 0.8034 1.6984 -0.1378 -0.5278 -0.1221 78  GLU   W CA  
39986 C  C   . GLU   W  79  ? 1.7007 0.7978 1.6821 -0.1820 -0.5827 -0.1226 78  GLU   W C   
39987 O  O   . GLU   W  79  ? 1.6930 0.8218 1.6794 -0.1582 -0.6455 -0.1906 78  GLU   W O   
39988 C  CB  . GLU   W  79  ? 1.8523 0.8227 1.7470 -0.1879 -0.5448 -0.1502 78  GLU   W CB  
39989 C  CG  . GLU   W  79  ? 1.9244 0.9800 1.7343 -0.1515 -0.5140 -0.2232 78  GLU   W CG  
39990 C  CD  . GLU   W  79  ? 2.0330 1.0117 1.8220 -0.1704 -0.4624 -0.2083 78  GLU   W CD  
39991 O  OE1 . GLU   W  79  ? 2.1234 1.2117 1.8057 -0.1438 -0.4354 -0.2013 78  GLU   W OE1 
39992 O  OE2 . GLU   W  79  ? 2.1205 1.2217 1.8144 -0.0889 -0.3965 -0.2619 78  GLU   W OE2 
39993 N  N   . ARG   W  80  ? 1.7174 0.7698 1.6453 -0.1541 -0.5864 -0.0700 79  ARG   W N   
39994 C  CA  . ARG   W  80  ? 1.7017 0.8183 1.6338 -0.1445 -0.5840 -0.0385 79  ARG   W CA  
39995 C  C   . ARG   W  80  ? 1.6716 0.7690 1.5953 -0.0872 -0.6066 -0.0510 79  ARG   W C   
39996 O  O   . ARG   W  80  ? 1.6735 0.8279 1.5531 -0.0797 -0.6156 -0.0397 79  ARG   W O   
39997 C  CB  . ARG   W  80  ? 1.7410 0.8093 1.6327 -0.2022 -0.5756 -0.0051 79  ARG   W CB  
39998 C  CG  . ARG   W  80  ? 1.7940 0.7769 1.5635 -0.2213 -0.5331 0.0114  79  ARG   W CG  
39999 C  CD  . ARG   W  80  ? 1.8588 0.7709 1.5946 -0.2550 -0.5039 0.0297  79  ARG   W CD  
40000 N  NE  . ARG   W  80  ? 1.9497 0.7760 1.5424 -0.2553 -0.4849 0.0464  79  ARG   W NE  
40001 C  CZ  . ARG   W  80  ? 2.0003 0.7209 1.5259 -0.2555 -0.4828 0.0989  79  ARG   W CZ  
40002 N  NH1 . ARG   W  80  ? 2.0120 0.7133 1.5339 -0.2306 -0.4863 0.0675  79  ARG   W NH1 
40003 N  NH2 . ARG   W  80  ? 2.0445 0.6807 1.5062 -0.2928 -0.4803 0.1196  79  ARG   W NH2 
40004 N  N   . ALA   W  81  ? 1.6671 0.7466 1.6093 -0.0752 -0.5819 -0.0656 80  ALA   W N   
40005 C  CA  . ALA   W  81  ? 1.6163 0.7490 1.5386 -0.0815 -0.5655 -0.0951 80  ALA   W CA  
40006 C  C   . ALA   W  81  ? 1.5419 0.6002 1.5409 -0.1054 -0.5630 -0.0786 80  ALA   W C   
40007 O  O   . ALA   W  81  ? 1.5535 0.5588 1.4992 -0.0876 -0.5583 -0.1201 80  ALA   W O   
40008 C  CB  . ALA   W  81  ? 1.6097 0.8159 1.6010 -0.0636 -0.5801 -0.0901 80  ALA   W CB  
40009 N  N   . ILE   W  82  ? 1.5410 0.5913 1.5048 -0.0994 -0.5653 -0.0874 81  ILE   W N   
40010 C  CA  . ILE   W  82  ? 1.5325 0.5905 1.5196 -0.1048 -0.5382 -0.1041 81  ILE   W CA  
40011 C  C   . ILE   W  82  ? 1.5311 0.6081 1.5668 -0.0943 -0.5285 -0.1070 81  ILE   W C   
40012 O  O   . ILE   W  82  ? 1.4477 0.4600 1.5954 -0.0904 -0.5261 -0.1453 81  ILE   W O   
40013 C  CB  . ILE   W  82  ? 1.5678 0.5382 1.4907 -0.1357 -0.5461 -0.1022 81  ILE   W CB  
40014 C  CG1 . ILE   W  82  ? 1.5729 0.5458 1.5005 -0.1610 -0.5278 -0.1214 81  ILE   W CG1 
40015 C  CG2 . ILE   W  82  ? 1.5604 0.5351 1.4427 -0.1608 -0.5583 -0.1211 81  ILE   W CG2 
40016 C  CD1 . ILE   W  82  ? 1.5582 0.5403 1.5354 -0.1286 -0.4864 -0.0935 81  ILE   W CD1 
40017 N  N   . GLU   W  83  ? 1.5468 0.6459 1.5846 -0.0631 -0.5104 -0.1106 82  GLU   W N   
40018 C  CA  . GLU   W  83  ? 1.5578 0.6886 1.6566 -0.0310 -0.5104 -0.0949 82  GLU   W CA  
40019 C  C   . GLU   W  83  ? 1.5022 0.6871 1.6166 -0.0534 -0.5137 -0.0304 82  GLU   W C   
40020 O  O   . GLU   W  83  ? 1.4882 0.5903 1.6228 -0.0470 -0.5044 0.0262  82  GLU   W O   
40021 C  CB  . GLU   W  83  ? 1.5629 0.7280 1.6832 -0.0545 -0.4865 -0.1283 82  GLU   W CB  
40022 C  CG  . GLU   W  83  ? 1.5874 0.7489 1.7700 -0.0591 -0.4954 -0.1836 82  GLU   W CG  
40023 C  CD  . GLU   W  83  ? 1.6010 0.8074 1.8170 -0.0119 -0.5116 -0.1656 82  GLU   W CD  
40024 O  OE1 . GLU   W  83  ? 1.5449 0.7727 1.7757 -0.0181 -0.5222 -0.2435 82  GLU   W OE1 
40025 O  OE2 . GLU   W  83  ? 1.6645 0.9454 1.8660 -0.0712 -0.5474 -0.2453 82  GLU   W OE2 
40026 N  N   . PRO   W  84  ? 1.5247 0.6890 1.6154 -0.0403 -0.4786 -0.0600 83  PRO   W N   
40027 C  CA  . PRO   W  84  ? 1.5196 0.6792 1.5733 -0.0265 -0.4524 -0.0658 83  PRO   W CA  
40028 C  C   . PRO   W  84  ? 1.5189 0.6524 1.5362 -0.0346 -0.4162 -0.0190 83  PRO   W C   
40029 O  O   . PRO   W  84  ? 1.5583 0.6521 1.5019 -0.0605 -0.4580 -0.0713 83  PRO   W O   
40030 C  CB  . PRO   W  84  ? 1.5002 0.7376 1.6102 -0.0178 -0.4457 -0.0766 83  PRO   W CB  
40031 C  CG  . PRO   W  84  ? 1.5090 0.7252 1.6635 -0.0202 -0.4577 -0.0990 83  PRO   W CG  
40032 C  CD  . PRO   W  84  ? 1.5098 0.7288 1.6800 -0.0126 -0.4601 -0.0783 83  PRO   W CD  
40033 N  N   . GLU   W  85  ? 1.5439 0.6779 1.5891 -0.0053 -0.3879 0.0354  84  GLU   W N   
40034 C  CA  . GLU   W  85  ? 1.5465 0.6732 1.5744 0.0162  -0.3743 0.0883  84  GLU   W CA  
40035 C  C   . GLU   W  85  ? 1.5678 0.6371 1.5166 0.0273  -0.3569 0.0780  84  GLU   W C   
40036 O  O   . GLU   W  85  ? 1.5587 0.5652 1.5085 0.0015  -0.3542 0.1712  84  GLU   W O   
40037 C  CB  . GLU   W  85  ? 1.5730 0.6998 1.5909 0.0410  -0.3634 0.1391  84  GLU   W CB  
40038 C  CG  . GLU   W  85  ? 1.6099 0.7110 1.6629 0.0676  -0.3279 0.1691  84  GLU   W CG  
40039 C  CD  . GLU   W  85  ? 1.5747 0.7180 1.7648 0.0751  -0.3522 0.2045  84  GLU   W CD  
40040 O  OE1 . GLU   W  85  ? 1.6246 0.6185 1.8106 0.1103  -0.3417 0.1923  84  GLU   W OE1 
40041 O  OE2 . GLU   W  85  ? 1.6076 0.7072 1.8111 0.1546  -0.3221 0.2687  84  GLU   W OE2 
40042 N  N   . THR   W  86  ? 1.5333 0.6841 1.5117 -0.0052 -0.3583 0.0250  85  THR   W N   
40043 C  CA  . THR   W  86  ? 1.5521 0.6742 1.5015 0.0005  -0.3466 -0.0330 85  THR   W CA  
40044 C  C   . THR   W  86  ? 1.5570 0.5914 1.4520 -0.0221 -0.3714 -0.1020 85  THR   W C   
40045 O  O   . THR   W  86  ? 1.5705 0.6228 1.4339 -0.0093 -0.3836 -0.1620 85  THR   W O   
40046 C  CB  . THR   W  86  ? 1.5453 0.6542 1.5193 -0.0195 -0.3419 -0.0004 85  THR   W CB  
40047 O  OG1 . THR   W  86  ? 1.5198 0.7152 1.5427 0.0153  -0.3267 0.0351  85  THR   W OG1 
40048 C  CG2 . THR   W  86  ? 1.5701 0.6437 1.5207 -0.0046 -0.3447 0.0142  85  THR   W CG2 
40049 N  N   . PHE   W  87  ? 1.5888 0.4813 1.4621 -0.0282 -0.3908 -0.1287 86  PHE   W N   
40050 C  CA  . PHE   W  87  ? 1.5977 0.4478 1.4683 -0.0431 -0.4049 -0.1326 86  PHE   W CA  
40051 C  C   . PHE   W  87  ? 1.6021 0.4498 1.5057 -0.0757 -0.4008 -0.1213 86  PHE   W C   
40052 O  O   . PHE   W  87  ? 1.5905 0.5354 1.6102 -0.0449 -0.3989 -0.0449 86  PHE   W O   
40053 C  CB  . PHE   W  87  ? 1.5876 0.4248 1.4481 -0.0408 -0.4058 -0.1575 86  PHE   W CB  
40054 C  CG  . PHE   W  87  ? 1.5765 0.4383 1.3810 -0.0224 -0.4043 -0.1878 86  PHE   W CG  
40055 C  CD1 . PHE   W  87  ? 1.6056 0.3827 1.3823 -0.0126 -0.4148 -0.1983 86  PHE   W CD1 
40056 C  CD2 . PHE   W  87  ? 1.5715 0.4512 1.3670 -0.0126 -0.4307 -0.1540 86  PHE   W CD2 
40057 C  CE1 . PHE   W  87  ? 1.5756 0.3969 1.3569 0.0065  -0.4078 -0.2331 86  PHE   W CE1 
40058 C  CE2 . PHE   W  87  ? 1.5567 0.4924 1.3470 0.0034  -0.4227 -0.1583 86  PHE   W CE2 
40059 C  CZ  . PHE   W  87  ? 1.5860 0.4110 1.3538 -0.0165 -0.4260 -0.1852 86  PHE   W CZ  
40060 N  N   . THR   W  88  ? 1.5842 0.4710 1.5089 -0.0716 -0.3698 -0.0797 87  THR   W N   
40061 C  CA  . THR   W  88  ? 1.5831 0.4339 1.4588 -0.0718 -0.3737 -0.0384 87  THR   W CA  
40062 C  C   . THR   W  88  ? 1.6067 0.4349 1.4331 -0.0825 -0.3837 -0.0356 87  THR   W C   
40063 O  O   . THR   W  88  ? 1.6117 0.3636 1.3909 -0.0553 -0.4174 -0.0302 87  THR   W O   
40064 C  CB  . THR   W  88  ? 1.6044 0.3497 1.4439 -0.1244 -0.3449 -0.0609 87  THR   W CB  
40065 O  OG1 . THR   W  88  ? 1.6103 0.2511 1.4730 -0.1386 -0.3466 -0.0840 87  THR   W OG1 
40066 C  CG2 . THR   W  88  ? 1.6045 0.3276 1.3971 -0.1035 -0.3439 -0.0341 87  THR   W CG2 
40067 N  N   . GLN   W  89  ? 1.6082 0.4575 1.4595 -0.0546 -0.3856 0.0012  88  GLN   W N   
40068 C  CA  . GLN   W  89  ? 1.5990 0.4396 1.4558 -0.0406 -0.3680 0.0000  88  GLN   W CA  
40069 C  C   . GLN   W  89  ? 1.5656 0.3773 1.4269 -0.0521 -0.4009 0.0046  88  GLN   W C   
40070 O  O   . GLN   W  89  ? 1.5719 0.2976 1.4782 -0.0529 -0.4144 -0.0037 88  GLN   W O   
40071 C  CB  . GLN   W  89  ? 1.6135 0.4931 1.4626 -0.0413 -0.3116 0.0218  88  GLN   W CB  
40072 C  CG  . GLN   W  89  ? 1.6320 0.5291 1.5043 -0.0235 -0.2802 0.0189  88  GLN   W CG  
40073 C  CD  . GLN   W  89  ? 1.6315 0.4533 1.4958 0.0247  -0.2421 0.0065  88  GLN   W CD  
40074 O  OE1 . GLN   W  89  ? 1.6604 0.3692 1.5539 0.0392  -0.1734 0.1503  88  GLN   W OE1 
40075 N  NE2 . GLN   W  89  ? 1.6287 0.5413 1.5048 0.0324  -0.2561 -0.0231 88  GLN   W NE2 
40076 N  N   . LEU   W  90  ? 1.5698 0.4093 1.3986 -0.0441 -0.4030 0.0285  89  LEU   W N   
40077 C  CA  . LEU   W  90  ? 1.5622 0.4610 1.3775 -0.0414 -0.4162 0.0315  89  LEU   W CA  
40078 C  C   . LEU   W  90  ? 1.5117 0.4503 1.3505 -0.0280 -0.4415 0.0206  89  LEU   W C   
40079 O  O   . LEU   W  90  ? 1.5122 0.3451 1.3080 0.0324  -0.4724 0.0118  89  LEU   W O   
40080 C  CB  . LEU   W  90  ? 1.5969 0.5269 1.3691 -0.0605 -0.4342 0.0360  89  LEU   W CB  
40081 C  CG  . LEU   W  90  ? 1.6032 0.5524 1.3288 -0.0531 -0.4489 0.0412  89  LEU   W CG  
40082 C  CD1 . LEU   W  90  ? 1.6125 0.5217 1.3308 -0.0410 -0.4302 0.0222  89  LEU   W CD1 
40083 C  CD2 . LEU   W  90  ? 1.6250 0.5459 1.3377 -0.0597 -0.4623 0.0498  89  LEU   W CD2 
40084 N  N   . VAL   W  91  ? 1.4836 0.4725 1.3537 -0.0231 -0.4313 0.0245  90  VAL   W N   
40085 C  CA  . VAL   W  91  ? 1.4628 0.4701 1.3212 -0.0293 -0.4164 -0.0139 90  VAL   W CA  
40086 C  C   . VAL   W  91  ? 1.4906 0.4485 1.2587 -0.0223 -0.3741 -0.0136 90  VAL   W C   
40087 O  O   . VAL   W  91  ? 1.4839 0.4356 1.2426 -0.0240 -0.3845 -0.0774 90  VAL   W O   
40088 C  CB  . VAL   W  91  ? 1.4344 0.4821 1.3351 -0.0224 -0.4106 -0.0271 90  VAL   W CB  
40089 C  CG1 . VAL   W  91  ? 1.4076 0.4750 1.3026 -0.0048 -0.4135 -0.0168 90  VAL   W CG1 
40090 C  CG2 . VAL   W  91  ? 1.4224 0.5008 1.3499 -0.0321 -0.4268 -0.0165 90  VAL   W CG2 
40091 N  N   . SER   W  92  ? 1.4929 0.4218 1.2702 -0.0177 -0.3627 0.0524  91  SER   W N   
40092 C  CA  . SER   W  92  ? 1.4617 0.4371 1.2654 -0.0269 -0.3614 0.0696  91  SER   W CA  
40093 C  C   . SER   W  92  ? 1.4282 0.5342 1.2614 -0.0378 -0.3826 0.0492  91  SER   W C   
40094 O  O   . SER   W  92  ? 1.4266 0.5584 1.2536 -0.0530 -0.3696 0.0828  91  SER   W O   
40095 C  CB  . SER   W  92  ? 1.4616 0.4018 1.2852 -0.0071 -0.3479 0.0777  91  SER   W CB  
40096 O  OG  . SER   W  92  ? 1.4074 0.2715 1.3208 -0.0042 -0.3456 0.0841  91  SER   W OG  
40097 N  N   . SER   W  93  ? 1.4564 0.5411 1.2974 -0.0827 -0.3747 -0.0046 92  SER   W N   
40098 C  CA  . SER   W  93  ? 1.4801 0.5713 1.2788 -0.0691 -0.3948 0.0132  92  SER   W CA  
40099 C  C   . SER   W  93  ? 1.4899 0.5354 1.2503 -0.0833 -0.3883 -0.0668 92  SER   W C   
40100 O  O   . SER   W  93  ? 1.5261 0.4745 1.2389 -0.0518 -0.4229 -0.1571 92  SER   W O   
40101 C  CB  . SER   W  93  ? 1.4890 0.5618 1.2808 -0.1060 -0.3880 0.1121  92  SER   W CB  
40102 O  OG  . SER   W  93  ? 1.5186 0.6258 1.2930 -0.1226 -0.3763 0.1691  92  SER   W OG  
40103 N  N   . SER   W  94  ? 1.5387 0.5310 1.2531 -0.0673 -0.4038 -0.0686 93  SER   W N   
40104 C  CA  . SER   W  94  ? 1.5693 0.5118 1.2020 -0.0615 -0.4261 -0.0537 93  SER   W CA  
40105 C  C   . SER   W  94  ? 1.5820 0.5667 1.1872 -0.0977 -0.4684 -0.1017 93  SER   W C   
40106 O  O   . SER   W  94  ? 1.5631 0.5488 1.1304 -0.1608 -0.5238 -0.1469 93  SER   W O   
40107 C  CB  . SER   W  94  ? 1.5646 0.4954 1.2062 -0.0379 -0.4344 -0.0176 93  SER   W CB  
40108 O  OG  . SER   W  94  ? 1.5717 0.5148 1.2290 -0.0567 -0.4233 -0.0277 93  SER   W OG  
40109 N  N   . LEU   W  95  ? 1.5776 0.6277 1.2146 -0.0584 -0.4540 -0.0953 94  LEU   W N   
40110 C  CA  . LEU   W  95  ? 1.5687 0.6312 1.2297 -0.0556 -0.4490 -0.1041 94  LEU   W CA  
40111 C  C   . LEU   W  95  ? 1.5883 0.5225 1.1788 -0.1105 -0.4205 -0.1270 94  LEU   W C   
40112 O  O   . LEU   W  95  ? 1.5638 0.6788 1.3040 -0.1381 -0.4176 -0.2584 94  LEU   W O   
40113 C  CB  . LEU   W  95  ? 1.5716 0.7336 1.2716 -0.0089 -0.4236 -0.1041 94  LEU   W CB  
40114 C  CG  . LEU   W  95  ? 1.5438 0.7653 1.2971 0.0188  -0.4202 -0.0839 94  LEU   W CG  
40115 C  CD1 . LEU   W  95  ? 1.5481 0.7346 1.3309 0.0176  -0.4324 -0.0930 94  LEU   W CD1 
40116 C  CD2 . LEU   W  95  ? 1.5684 0.7756 1.2783 0.0377  -0.4186 -0.0603 94  LEU   W CD2 
40117 N  N   . TYR   W  96  ? 1.5781 0.3965 1.1488 -0.1275 -0.4780 -0.1329 95  TYR   W N   
40118 C  CA  . TYR   W  96  ? 1.5833 0.3836 1.1135 -0.1122 -0.4618 -0.0600 95  TYR   W CA  
40119 C  C   . TYR   W  96  ? 1.6142 0.3667 1.1439 -0.0952 -0.4743 -0.0563 95  TYR   W C   
40120 O  O   . TYR   W  96  ? 1.5956 0.2788 1.2094 -0.1108 -0.4619 -0.0902 95  TYR   W O   
40121 C  CB  . TYR   W  96  ? 1.5867 0.3485 1.1065 -0.1059 -0.4903 0.0025  95  TYR   W CB  
40122 C  CG  . TYR   W  96  ? 1.6000 0.3625 1.0532 -0.0804 -0.4845 0.0789  95  TYR   W CG  
40123 C  CD1 . TYR   W  96  ? 1.6118 0.4067 1.0042 -0.0543 -0.4756 0.0617  95  TYR   W CD1 
40124 C  CD2 . TYR   W  96  ? 1.6151 0.3018 1.0322 -0.0811 -0.4745 0.0644  95  TYR   W CD2 
40125 C  CE1 . TYR   W  96  ? 1.5999 0.4587 0.9838 -0.0350 -0.4874 0.0860  95  TYR   W CE1 
40126 C  CE2 . TYR   W  96  ? 1.5875 0.3559 1.0320 -0.0517 -0.5151 0.0969  95  TYR   W CE2 
40127 C  CZ  . TYR   W  96  ? 1.5979 0.4298 1.0075 -0.0146 -0.4925 0.0537  95  TYR   W CZ  
40128 O  OH  . TYR   W  96  ? 1.5960 0.5537 0.9652 0.0666  -0.5148 0.1063  95  TYR   W OH  
40129 N  N   . GLU   W  97  ? 1.6507 0.4415 1.1179 -0.0868 -0.5075 -0.0775 96  GLU   W N   
40130 C  CA  . GLU   W  97  ? 1.6825 0.5431 1.2136 -0.0287 -0.5225 -0.0774 96  GLU   W CA  
40131 C  C   . GLU   W  97  ? 1.6433 0.5767 1.2188 -0.0479 -0.5683 -0.1116 96  GLU   W C   
40132 O  O   . GLU   W  97  ? 1.6371 0.5569 1.2553 -0.0813 -0.6160 -0.1220 96  GLU   W O   
40133 C  CB  . GLU   W  97  ? 1.7835 0.6006 1.2573 -0.0265 -0.5202 -0.1278 96  GLU   W CB  
40134 C  CG  . GLU   W  97  ? 1.8357 0.6965 1.3258 0.0350  -0.5018 -0.1223 96  GLU   W CG  
40135 C  CD  . GLU   W  97  ? 1.9518 0.6823 1.3658 0.0173  -0.5086 -0.1203 96  GLU   W CD  
40136 O  OE1 . GLU   W  97  ? 2.1112 0.6542 1.4562 -0.0007 -0.4783 -0.0496 96  GLU   W OE1 
40137 O  OE2 . GLU   W  97  ? 1.8969 0.7804 1.4894 0.0809  -0.5280 -0.0727 96  GLU   W OE2 
40138 N  N   . ARG   W  98  ? 1.6914 0.6320 1.2267 0.0453  -0.5539 -0.0968 97  ARG   W N   
40139 C  CA  . ARG   W  98  ? 1.7302 0.6151 1.2906 0.0763  -0.4636 -0.1112 97  ARG   W CA  
40140 C  C   . ARG   W  98  ? 1.7154 0.6888 1.1312 0.0801  -0.4905 -0.0979 97  ARG   W C   
40141 O  O   . ARG   W  98  ? 1.7121 0.5887 1.1686 0.1241  -0.4852 -0.2319 97  ARG   W O   
40142 C  CB  . ARG   W  98  ? 1.8402 0.7512 1.2808 0.1542  -0.4359 -0.1331 97  ARG   W CB  
40143 C  CG  . ARG   W  98  ? 1.9370 0.8221 1.3996 0.2377  -0.3725 -0.1825 97  ARG   W CG  
40144 C  CD  . ARG   W  98  ? 1.9859 0.9352 1.4622 0.2998  -0.2738 -0.1852 97  ARG   W CD  
40145 N  NE  . ARG   W  98  ? 2.1359 1.0894 1.4906 0.3533  -0.1511 -0.2520 97  ARG   W NE  
40146 C  CZ  . ARG   W  98  ? 2.3141 1.0051 1.5866 0.3110  -0.0902 -0.2291 97  ARG   W CZ  
40147 N  NH1 . ARG   W  98  ? 2.3852 1.0998 1.5869 0.2662  -0.0564 -0.1749 97  ARG   W NH1 
40148 N  NH2 . ARG   W  98  ? 2.4288 0.9845 1.5388 0.1790  -0.0884 -0.2859 97  ARG   W NH2 
40149 N  N   . ARG   W  99  ? 1.7276 0.5953 1.1458 0.0124  -0.4670 -0.0660 98  ARG   W N   
40150 C  CA  . ARG   W  99  ? 1.6801 0.5489 1.1714 -0.0005 -0.4686 -0.0546 98  ARG   W CA  
40151 C  C   . ARG   W  99  ? 1.6748 0.4762 1.1504 0.0292  -0.5075 -0.0559 98  ARG   W C   
40152 O  O   . ARG   W  99  ? 1.5303 0.4485 1.1508 -0.0058 -0.5869 -0.0413 98  ARG   W O   
40153 C  CB  . ARG   W  99  ? 1.7306 0.6413 1.1272 0.0071  -0.4547 -0.0835 98  ARG   W CB  
40154 C  CG  . ARG   W  99  ? 1.7664 0.6470 1.1385 0.0144  -0.4150 -0.0953 98  ARG   W CG  
40155 C  CD  . ARG   W  99  ? 1.7613 0.6722 1.1295 0.0143  -0.3906 -0.0888 98  ARG   W CD  
40156 N  NE  . ARG   W  99  ? 1.8340 0.7122 1.1437 -0.0190 -0.3253 -0.1113 98  ARG   W NE  
40157 C  CZ  . ARG   W  99  ? 1.8242 0.7076 1.0598 -0.0150 -0.3342 -0.1758 98  ARG   W CZ  
40158 N  NH1 . ARG   W  99  ? 1.8302 0.7247 1.0250 -0.0044 -0.3843 -0.1638 98  ARG   W NH1 
40159 N  NH2 . ARG   W  99  ? 1.8084 0.7761 1.0899 -0.0190 -0.3153 -0.1607 98  ARG   W NH2 
40160 N  N   . PHE   W  100 ? 1.6426 0.5331 1.1358 -0.0491 -0.4879 -0.0709 99  PHE   W N   
40161 C  CA  . PHE   W  100 ? 1.6964 0.5376 1.1588 -0.0780 -0.4852 -0.1007 99  PHE   W CA  
40162 C  C   . PHE   W  100 ? 1.6775 0.6188 1.1649 -0.0961 -0.4777 -0.1372 99  PHE   W C   
40163 O  O   . PHE   W  100 ? 1.6766 0.8103 1.2263 -0.1230 -0.5208 -0.1395 99  PHE   W O   
40164 C  CB  . PHE   W  100 ? 1.7611 0.4965 1.1595 -0.0547 -0.4739 -0.0462 99  PHE   W CB  
40165 C  CG  . PHE   W  100 ? 1.8321 0.4526 1.1638 -0.0425 -0.4691 0.0277  99  PHE   W CG  
40166 C  CD1 . PHE   W  100 ? 1.8939 0.4919 1.1405 -0.0349 -0.4619 0.0069  99  PHE   W CD1 
40167 C  CD2 . PHE   W  100 ? 1.8225 0.4515 1.1308 -0.0273 -0.4782 0.0250  99  PHE   W CD2 
40168 C  CE1 . PHE   W  100 ? 1.9152 0.4398 1.1200 -0.0315 -0.4836 0.0377  99  PHE   W CE1 
40169 C  CE2 . PHE   W  100 ? 1.8477 0.4431 1.1194 -0.0432 -0.4857 0.0343  99  PHE   W CE2 
40170 C  CZ  . PHE   W  100 ? 1.8891 0.4519 1.0918 -0.0243 -0.4805 0.0454  99  PHE   W CZ  
40171 N  N   . GLY   W  101 ? 1.6203 0.6026 1.1664 -0.0901 -0.4545 -0.1473 100 GLY   W N   
40172 C  CA  . GLY   W  101 ? 1.5809 0.5919 1.1624 -0.0705 -0.4648 -0.1388 100 GLY   W CA  
40173 C  C   . GLY   W  101 ? 1.5518 0.5761 1.1301 -0.0426 -0.4402 -0.1141 100 GLY   W C   
40174 O  O   . GLY   W  101 ? 1.4976 0.7318 1.0259 -0.0550 -0.4208 -0.1048 100 GLY   W O   
40175 N  N   . PRO   W  102 ? 1.6167 0.4650 1.1362 -0.0369 -0.4369 -0.0988 101 PRO   W N   
40176 C  CA  . PRO   W  102 ? 1.6212 0.4686 1.1562 -0.0236 -0.4333 -0.0808 101 PRO   W CA  
40177 C  C   . PRO   W  102 ? 1.6810 0.4433 1.1547 -0.0055 -0.4252 -0.0898 101 PRO   W C   
40178 O  O   . PRO   W  102 ? 1.7740 0.3328 1.1773 0.0064  -0.4199 -0.0822 101 PRO   W O   
40179 C  CB  . PRO   W  102 ? 1.6043 0.4256 1.1555 -0.0484 -0.4276 -0.0659 101 PRO   W CB  
40180 C  CG  . PRO   W  102 ? 1.6197 0.4128 1.1559 -0.0453 -0.4422 -0.0716 101 PRO   W CG  
40181 C  CD  . PRO   W  102 ? 1.6075 0.4229 1.1565 -0.0538 -0.4540 -0.0760 101 PRO   W CD  
40182 N  N   . TYR   W  103 ? 1.6521 0.4723 1.2449 0.0231  -0.4447 -0.1040 102 TYR   W N   
40183 C  CA  . TYR   W  103 ? 1.6746 0.4610 1.2836 0.0364  -0.4179 -0.0181 102 TYR   W CA  
40184 C  C   . TYR   W  103 ? 1.6483 0.3962 1.3026 -0.0337 -0.3661 0.0076  102 TYR   W C   
40185 O  O   . TYR   W  103 ? 1.6898 0.2073 1.2191 -0.1188 -0.3818 0.1111  102 TYR   W O   
40186 C  CB  . TYR   W  103 ? 1.6662 0.4929 1.2703 0.0660  -0.4502 -0.0487 102 TYR   W CB  
40187 C  CG  . TYR   W  103 ? 1.7150 0.4997 1.2913 0.0768  -0.4337 -0.0566 102 TYR   W CG  
40188 C  CD1 . TYR   W  103 ? 1.7333 0.5065 1.3344 0.1047  -0.4064 -0.0810 102 TYR   W CD1 
40189 C  CD2 . TYR   W  103 ? 1.7365 0.4571 1.2788 0.1190  -0.4193 -0.0801 102 TYR   W CD2 
40190 C  CE1 . TYR   W  103 ? 1.7445 0.5070 1.3560 0.1132  -0.3830 -0.0635 102 TYR   W CE1 
40191 C  CE2 . TYR   W  103 ? 1.7884 0.4638 1.3038 0.1657  -0.4385 -0.0494 102 TYR   W CE2 
40192 C  CZ  . TYR   W  103 ? 1.7681 0.5185 1.3625 0.1682  -0.4122 -0.0221 102 TYR   W CZ  
40193 O  OH  . TYR   W  103 ? 1.7816 0.6533 1.4737 0.2903  -0.3895 -0.0573 102 TYR   W OH  
40194 N  N   . PHE   W  104 ? 1.6531 0.4099 1.3473 -0.0362 -0.3659 0.0289  103 PHE   W N   
40195 C  CA  . PHE   W  104 ? 1.5821 0.4249 1.2893 -0.0284 -0.3808 0.0183  103 PHE   W CA  
40196 C  C   . PHE   W  104 ? 1.5929 0.4146 1.2995 0.0478  -0.3866 -0.0253 103 PHE   W C   
40197 O  O   . PHE   W  104 ? 1.6304 0.4236 1.2786 0.0024  -0.3539 -0.0429 103 PHE   W O   
40198 C  CB  . PHE   W  104 ? 1.5684 0.4336 1.3100 -0.0453 -0.4117 0.0320  103 PHE   W CB  
40199 C  CG  . PHE   W  104 ? 1.5428 0.4522 1.3178 -0.1004 -0.3967 0.0426  103 PHE   W CG  
40200 C  CD1 . PHE   W  104 ? 1.4956 0.4899 1.3091 -0.1272 -0.3988 0.0442  103 PHE   W CD1 
40201 C  CD2 . PHE   W  104 ? 1.5158 0.4718 1.3402 -0.1251 -0.4036 0.0209  103 PHE   W CD2 
40202 C  CE1 . PHE   W  104 ? 1.5115 0.4968 1.2998 -0.1515 -0.4146 0.0192  103 PHE   W CE1 
40203 C  CE2 . PHE   W  104 ? 1.5161 0.5076 1.3463 -0.1359 -0.4054 0.0037  103 PHE   W CE2 
40204 C  CZ  . PHE   W  104 ? 1.5112 0.5185 1.3300 -0.1479 -0.4127 0.0143  103 PHE   W CZ  
40205 N  N   . VAL   W  105 ? 1.5857 0.3389 1.2102 0.0903  -0.4093 -0.0086 104 VAL   W N   
40206 C  CA  . VAL   W  105 ? 1.6153 0.3720 1.1966 0.1032  -0.4403 0.0073  104 VAL   W CA  
40207 C  C   . VAL   W  105 ? 1.6023 0.3768 1.1671 0.1040  -0.4684 0.0099  104 VAL   W C   
40208 O  O   . VAL   W  105 ? 1.6383 0.3968 1.1776 0.0762  -0.5188 0.0439  104 VAL   W O   
40209 C  CB  . VAL   W  105 ? 1.6458 0.3701 1.1763 0.1500  -0.4151 0.0030  104 VAL   W CB  
40210 C  CG1 . VAL   W  105 ? 1.6459 0.3432 1.1543 0.1566  -0.4199 0.0555  104 VAL   W CG1 
40211 C  CG2 . VAL   W  105 ? 1.6595 0.3838 1.1419 0.1537  -0.4028 -0.0141 104 VAL   W CG2 
40212 N  N   . GLY   W  106 ? 1.5857 0.4517 1.2649 0.0912  -0.4887 -0.0276 105 GLY   W N   
40213 C  CA  . GLY   W  106 ? 1.5650 0.5060 1.3058 0.0932  -0.4932 -0.0435 105 GLY   W CA  
40214 C  C   . GLY   W  106 ? 1.5579 0.5579 1.3841 0.0624  -0.4753 -0.0547 105 GLY   W C   
40215 O  O   . GLY   W  106 ? 1.4747 0.6675 1.5580 0.1225  -0.4637 -0.0923 105 GLY   W O   
40216 N  N   . PRO   W  107 ? 1.5105 0.5654 1.3096 0.0658  -0.5115 -0.0410 106 PRO   W N   
40217 C  CA  . PRO   W  107 ? 1.5059 0.5580 1.3007 0.0731  -0.4865 -0.0655 106 PRO   W CA  
40218 C  C   . PRO   W  107 ? 1.5317 0.5415 1.2642 0.1183  -0.4622 -0.0514 106 PRO   W C   
40219 O  O   . PRO   W  107 ? 1.5432 0.5641 1.2135 0.1677  -0.4336 0.0195  106 PRO   W O   
40220 C  CB  . PRO   W  107 ? 1.4955 0.5704 1.2890 0.0775  -0.5141 -0.0749 106 PRO   W CB  
40221 C  CG  . PRO   W  107 ? 1.5155 0.5580 1.2580 0.0598  -0.5026 -0.0889 106 PRO   W CG  
40222 C  CD  . PRO   W  107 ? 1.5044 0.5583 1.2806 0.0524  -0.5149 -0.0614 106 PRO   W CD  
40223 N  N   . VAL   W  108 ? 1.4778 0.5913 1.3254 0.1182  -0.4591 -0.0325 107 VAL   W N   
40224 C  CA  . VAL   W  108 ? 1.4965 0.6615 1.3636 0.0966  -0.4188 -0.0272 107 VAL   W CA  
40225 C  C   . VAL   W  108 ? 1.4784 0.6465 1.3418 0.0721  -0.4268 0.0390  107 VAL   W C   
40226 O  O   . VAL   W  108 ? 1.5330 0.8131 1.3632 0.0271  -0.4114 -0.0552 107 VAL   W O   
40227 C  CB  . VAL   W  108 ? 1.5011 0.6455 1.3925 0.1016  -0.4141 -0.0466 107 VAL   W CB  
40228 C  CG1 . VAL   W  108 ? 1.5009 0.6383 1.4155 0.0926  -0.4071 -0.0614 107 VAL   W CG1 
40229 C  CG2 . VAL   W  108 ? 1.4733 0.6904 1.3869 0.0809  -0.4388 -0.0602 107 VAL   W CG2 
40230 N  N   . VAL   W  109 ? 1.4738 0.5815 1.3778 0.1158  -0.4682 0.0858  108 VAL   W N   
40231 C  CA  . VAL   W  109 ? 1.4818 0.5605 1.3863 0.1153  -0.4576 0.0999  108 VAL   W CA  
40232 C  C   . VAL   W  109 ? 1.4892 0.4939 1.3882 0.1221  -0.4412 0.1503  108 VAL   W C   
40233 O  O   . VAL   W  109 ? 1.4931 0.4487 1.3842 0.1571  -0.3934 0.2207  108 VAL   W O   
40234 C  CB  . VAL   W  109 ? 1.4745 0.5635 1.3797 0.0921  -0.4759 0.0982  108 VAL   W CB  
40235 C  CG1 . VAL   W  109 ? 1.4469 0.5807 1.4026 0.0944  -0.4896 0.0848  108 VAL   W CG1 
40236 C  CG2 . VAL   W  109 ? 1.4606 0.5800 1.3695 0.0723  -0.4793 0.0934  108 VAL   W CG2 
40237 N  N   . ALA   W  110 ? 1.4913 0.5077 1.4074 0.1122  -0.4450 0.1387  109 ALA   W N   
40238 C  CA  . ALA   W  110 ? 1.4866 0.5903 1.4703 0.1155  -0.4259 0.1406  109 ALA   W CA  
40239 C  C   . ALA   W  110 ? 1.4912 0.6451 1.4912 0.0799  -0.4351 0.1229  109 ALA   W C   
40240 O  O   . ALA   W  110 ? 1.4985 0.7059 1.4848 0.0861  -0.4353 0.1135  109 ALA   W O   
40241 C  CB  . ALA   W  110 ? 1.5312 0.5826 1.4846 0.1143  -0.4262 0.1412  109 ALA   W CB  
40242 N  N   . GLY   W  111 ? 1.5116 0.7389 1.5133 0.0354  -0.4366 0.1318  110 GLY   W N   
40243 C  CA  . GLY   W  111 ? 1.5670 0.7782 1.5428 -0.0166 -0.4608 0.1488  110 GLY   W CA  
40244 C  C   . GLY   W  111 ? 1.6242 0.8214 1.5564 -0.0523 -0.4471 0.1876  110 GLY   W C   
40245 O  O   . GLY   W  111 ? 1.6893 0.8044 1.5039 -0.1176 -0.4656 0.2057  110 GLY   W O   
40246 N  N   . ILE   W  112 ? 1.6165 0.8440 1.6169 -0.0859 -0.4510 0.2086  111 ILE   W N   
40247 C  CA  . ILE   W  112 ? 1.5960 0.9074 1.6766 -0.0877 -0.4372 0.2117  111 ILE   W CA  
40248 C  C   . ILE   W  112 ? 1.5975 0.8987 1.7029 -0.0830 -0.4545 0.1771  111 ILE   W C   
40249 O  O   . ILE   W  112 ? 1.5619 0.9063 1.6827 -0.0905 -0.4900 0.1716  111 ILE   W O   
40250 C  CB  . ILE   W  112 ? 1.5549 0.9190 1.7363 -0.0947 -0.4247 0.2332  111 ILE   W CB  
40251 C  CG1 . ILE   W  112 ? 1.5410 0.9278 1.7690 -0.0854 -0.3940 0.2445  111 ILE   W CG1 
40252 C  CG2 . ILE   W  112 ? 1.5647 0.8994 1.7971 -0.0947 -0.4188 0.2545  111 ILE   W CG2 
40253 C  CD1 . ILE   W  112 ? 1.5495 1.0057 1.7710 -0.1095 -0.4090 0.2093  111 ILE   W CD1 
40254 N  N   . ASN   W  113 ? 1.6484 0.9617 1.6860 -0.0934 -0.4415 0.1492  112 ASN   W N   
40255 C  CA  . ASN   W  113 ? 1.6742 0.9377 1.7173 -0.1076 -0.4553 0.1195  112 ASN   W CA  
40256 C  C   . ASN   W  113 ? 1.7104 0.9045 1.7926 -0.1104 -0.4345 0.0372  112 ASN   W C   
40257 O  O   . ASN   W  113 ? 1.7293 0.8356 1.8133 -0.0947 -0.4164 0.0528  112 ASN   W O   
40258 C  CB  . ASN   W  113 ? 1.6833 0.9682 1.7193 -0.0775 -0.4854 0.1986  112 ASN   W CB  
40259 C  CG  . ASN   W  113 ? 1.6738 1.0462 1.6426 -0.0819 -0.5509 0.2708  112 ASN   W CG  
40260 O  OD1 . ASN   W  113 ? 1.6521 1.0768 1.6585 -0.0916 -0.6184 0.2962  112 ASN   W OD1 
40261 N  ND2 . ASN   W  113 ? 1.6895 1.1514 1.6139 -0.1059 -0.5536 0.2789  112 ASN   W ND2 
40262 N  N   . SER   W  114 ? 1.6854 0.9117 1.8452 -0.1592 -0.4622 -0.0297 113 SER   W N   
40263 C  CA  . SER   W  114 ? 1.6881 0.8812 1.9305 -0.1472 -0.4511 -0.0881 113 SER   W CA  
40264 C  C   . SER   W  114 ? 1.6793 0.9158 1.9953 -0.1806 -0.4390 -0.0900 113 SER   W C   
40265 O  O   . SER   W  114 ? 1.6585 1.0304 2.1040 -0.2422 -0.4015 -0.0999 113 SER   W O   
40266 C  CB  . SER   W  114 ? 1.6829 0.7711 1.9618 -0.1450 -0.4950 -0.1169 113 SER   W CB  
40267 O  OG  . SER   W  114 ? 1.6614 0.6792 1.9623 -0.1317 -0.4793 -0.1959 113 SER   W OG  
40268 N  N   . LYS   W  115 ? 1.6802 0.9031 2.0047 -0.1428 -0.4144 -0.0572 114 LYS   W N   
40269 C  CA  . LYS   W  115 ? 1.6737 0.8939 2.1225 -0.1429 -0.3805 -0.0354 114 LYS   W CA  
40270 C  C   . LYS   W  115 ? 1.6352 0.8648 2.1745 -0.1090 -0.3948 0.0130  114 LYS   W C   
40271 O  O   . LYS   W  115 ? 1.6582 0.8388 2.2147 -0.1437 -0.4585 -0.0261 114 LYS   W O   
40272 C  CB  . LYS   W  115 ? 1.6980 0.9016 2.1477 -0.1258 -0.3607 0.0005  114 LYS   W CB  
40273 C  CG  . LYS   W  115 ? 1.7364 0.9437 2.2506 -0.1717 -0.3163 0.0304  114 LYS   W CG  
40274 C  CD  . LYS   W  115 ? 1.7670 0.9830 2.2803 -0.1762 -0.2826 0.0134  114 LYS   W CD  
40275 C  CE  . LYS   W  115 ? 1.7804 1.0373 2.3432 -0.1958 -0.2553 0.0864  114 LYS   W CE  
40276 N  NZ  . LYS   W  115 ? 1.7801 1.0047 2.3639 -0.1621 -0.1869 0.1484  114 LYS   W NZ  
40277 N  N   . SER   W  116 ? 1.6396 0.7770 2.1169 -0.0112 -0.3267 0.0341  115 SER   W N   
40278 C  CA  . SER   W  116 ? 1.6404 0.7454 2.0974 0.0025  -0.2957 0.0950  115 SER   W CA  
40279 C  C   . SER   W  116 ? 1.6064 0.6809 2.1452 0.0225  -0.2516 0.0769  115 SER   W C   
40280 O  O   . SER   W  116 ? 1.6307 0.5402 2.1592 0.0308  -0.2375 0.0717  115 SER   W O   
40281 C  CB  . SER   W  116 ? 1.6231 0.6713 2.0055 0.0090  -0.2441 0.1266  115 SER   W CB  
40282 O  OG  . SER   W  116 ? 1.6620 0.5334 1.9093 0.0741  -0.2792 0.1249  115 SER   W OG  
40283 N  N   . GLY   W  117 ? 1.6002 0.6524 2.1351 0.0418  -0.2830 0.1034  116 GLY   W N   
40284 C  CA  . GLY   W  117 ? 1.6001 0.8149 2.0895 0.0715  -0.3189 0.1426  116 GLY   W CA  
40285 C  C   . GLY   W  117 ? 1.6156 0.8383 2.0211 0.0965  -0.3149 0.1263  116 GLY   W C   
40286 O  O   . GLY   W  117 ? 1.7014 0.6845 2.0898 0.0699  -0.2439 0.1216  116 GLY   W O   
40287 N  N   . LYS   W  118 ? 1.6226 1.0120 1.9790 0.0702  -0.2900 0.1030  117 LYS   W N   
40288 C  CA  . LYS   W  118 ? 1.6339 1.0008 1.9354 0.0765  -0.2714 0.1131  117 LYS   W CA  
40289 C  C   . LYS   W  118 ? 1.6098 0.9717 1.8715 0.0669  -0.3418 0.1231  117 LYS   W C   
40290 O  O   . LYS   W  118 ? 1.6359 0.8330 1.8879 0.0935  -0.3517 0.1850  117 LYS   W O   
40291 C  CB  . LYS   W  118 ? 1.6990 1.1586 1.8769 0.1007  -0.2387 0.0380  117 LYS   W CB  
40292 C  CG  . LYS   W  118 ? 1.7689 1.3339 1.9208 0.1303  -0.1549 -0.0012 117 LYS   W CG  
40293 C  CD  . LYS   W  118 ? 1.8866 1.4396 1.9113 0.1807  -0.1619 0.0039  117 LYS   W CD  
40294 C  CE  . LYS   W  118 ? 1.9669 1.5486 1.9472 0.1929  -0.1093 0.0363  117 LYS   W CE  
40295 N  NZ  . LYS   W  118 ? 2.0259 1.6311 1.9753 0.2575  -0.0917 0.0246  117 LYS   W NZ  
40296 N  N   . PRO   W  119 ? 1.5807 0.9620 1.8177 0.0079  -0.3831 0.1274  118 PRO   W N   
40297 C  CA  . PRO   W  119 ? 1.5518 0.9433 1.7319 -0.0090 -0.4235 0.0932  118 PRO   W CA  
40298 C  C   . PRO   W  119 ? 1.5621 0.8934 1.5704 -0.0340 -0.3593 0.0866  118 PRO   W C   
40299 O  O   . PRO   W  119 ? 1.5643 0.9285 1.5508 -0.0848 -0.3903 0.0457  118 PRO   W O   
40300 C  CB  . PRO   W  119 ? 1.5867 0.9102 1.7959 -0.0206 -0.3913 0.0961  118 PRO   W CB  
40301 C  CG  . PRO   W  119 ? 1.5935 0.9482 1.8681 -0.0298 -0.3835 0.0820  118 PRO   W CG  
40302 C  CD  . PRO   W  119 ? 1.5725 1.0191 1.8414 -0.0019 -0.3657 0.1103  118 PRO   W CD  
40303 N  N   . PHE   W  120 ? 1.5358 0.8447 1.5653 -0.0423 -0.3948 0.0765  119 PHE   W N   
40304 C  CA  . PHE   W  120 ? 1.5464 0.8270 1.5320 -0.0205 -0.3947 0.0501  119 PHE   W CA  
40305 C  C   . PHE   W  120 ? 1.5134 0.7083 1.5572 0.0158  -0.4348 0.0495  119 PHE   W C   
40306 O  O   . PHE   W  120 ? 1.5149 0.7224 1.5570 0.0695  -0.4627 0.0434  119 PHE   W O   
40307 C  CB  . PHE   W  120 ? 1.5405 0.8373 1.5256 -0.0091 -0.4113 0.0206  119 PHE   W CB  
40308 C  CG  . PHE   W  120 ? 1.5666 0.9074 1.4946 -0.0218 -0.4122 -0.0164 119 PHE   W CG  
40309 C  CD1 . PHE   W  120 ? 1.5672 0.8860 1.4424 -0.0350 -0.4245 -0.0409 119 PHE   W CD1 
40310 C  CD2 . PHE   W  120 ? 1.5881 0.9826 1.5081 -0.0265 -0.3778 0.0048  119 PHE   W CD2 
40311 C  CE1 . PHE   W  120 ? 1.5377 0.8905 1.4615 -0.0632 -0.4116 -0.0607 119 PHE   W CE1 
40312 C  CE2 . PHE   W  120 ? 1.5872 0.9936 1.5206 -0.0569 -0.3800 -0.0025 119 PHE   W CE2 
40313 C  CZ  . PHE   W  120 ? 1.5801 0.9499 1.4710 -0.0719 -0.3971 -0.0421 119 PHE   W CZ  
40314 N  N   . ILE   W  121 ? 1.4662 0.6577 1.5701 0.0180  -0.3946 0.0687  120 ILE   W N   
40315 C  CA  . ILE   W  121 ? 1.4811 0.6623 1.5829 -0.0037 -0.3770 0.0411  120 ILE   W CA  
40316 C  C   . ILE   W  121 ? 1.4878 0.5419 1.5393 0.0182  -0.3574 0.0292  120 ILE   W C   
40317 O  O   . ILE   W  121 ? 1.5035 0.5283 1.5433 -0.0017 -0.3359 0.0048  120 ILE   W O   
40318 C  CB  . ILE   W  121 ? 1.4501 0.6459 1.6065 -0.0581 -0.3498 0.0801  120 ILE   W CB  
40319 C  CG1 . ILE   W  121 ? 1.4565 0.6528 1.6625 -0.0600 -0.3193 0.0664  120 ILE   W CG1 
40320 C  CG2 . ILE   W  121 ? 1.4575 0.6790 1.5836 -0.1012 -0.3335 0.1081  120 ILE   W CG2 
40321 C  CD1 . ILE   W  121 ? 1.4670 0.6632 1.6930 -0.0158 -0.3321 0.0544  120 ILE   W CD1 
40322 N  N   . ALA   W  122 ? 1.4670 0.4576 1.5264 0.0642  -0.3726 0.0132  121 ALA   W N   
40323 C  CA  . ALA   W  122 ? 1.4978 0.4470 1.5095 0.0919  -0.3826 0.0319  121 ALA   W CA  
40324 C  C   . ALA   W  122 ? 1.5160 0.4827 1.4756 0.0903  -0.3740 0.0481  121 ALA   W C   
40325 O  O   . ALA   W  122 ? 1.5174 0.5043 1.4575 0.1331  -0.4142 0.0465  121 ALA   W O   
40326 C  CB  . ALA   W  122 ? 1.5475 0.3974 1.5442 0.0620  -0.3598 0.0147  121 ALA   W CB  
40327 N  N   . GLY   W  123 ? 1.5410 0.4382 1.4807 0.0659  -0.3525 0.0559  122 GLY   W N   
40328 C  CA  . GLY   W  123 ? 1.5469 0.4192 1.4841 0.0801  -0.3312 0.0637  122 GLY   W CA  
40329 C  C   . GLY   W  123 ? 1.5618 0.2877 1.4484 0.1002  -0.3014 0.1047  122 GLY   W C   
40330 O  O   . GLY   W  123 ? 1.5341 0.2421 1.4445 0.1620  -0.3292 0.0956  122 GLY   W O   
40331 N  N   . PHE   W  124 ? 1.5345 0.2831 1.5230 0.0894  -0.3207 0.0899  123 PHE   W N   
40332 C  CA  . PHE   W  124 ? 1.5473 0.3832 1.5318 0.0344  -0.3490 0.1229  123 PHE   W CA  
40333 C  C   . PHE   W  124 ? 1.5911 0.3624 1.6124 0.0299  -0.3161 0.1036  123 PHE   W C   
40334 O  O   . PHE   W  124 ? 1.6397 0.5331 1.6450 0.0062  -0.3124 0.1712  123 PHE   W O   
40335 C  CB  . PHE   W  124 ? 1.5485 0.4960 1.5472 0.0200  -0.3201 0.0345  123 PHE   W CB  
40336 C  CG  . PHE   W  124 ? 1.5500 0.5991 1.5517 -0.0425 -0.3432 0.0369  123 PHE   W CG  
40337 C  CD1 . PHE   W  124 ? 1.5720 0.6415 1.5459 -0.0404 -0.3513 0.0237  123 PHE   W CD1 
40338 C  CD2 . PHE   W  124 ? 1.5589 0.6324 1.5372 -0.0456 -0.3362 0.0564  123 PHE   W CD2 
40339 C  CE1 . PHE   W  124 ? 1.5966 0.7031 1.5441 -0.0843 -0.3541 0.0317  123 PHE   W CE1 
40340 C  CE2 . PHE   W  124 ? 1.5598 0.7100 1.5543 -0.0895 -0.3417 0.0571  123 PHE   W CE2 
40341 C  CZ  . PHE   W  124 ? 1.6054 0.7549 1.5434 -0.0909 -0.3427 0.0675  123 PHE   W CZ  
40342 N  N   . ASP   W  125 ? 1.6367 0.3379 1.5040 0.0076  -0.2936 0.1984  124 ASP   W N   
40343 C  CA  . ASP   W  125 ? 1.6372 0.4955 1.4689 -0.0512 -0.3022 0.1347  124 ASP   W CA  
40344 C  C   . ASP   W  125 ? 1.6424 0.4100 1.4459 -0.0260 -0.3509 0.1597  124 ASP   W C   
40345 O  O   . ASP   W  125 ? 1.5705 0.4044 1.3451 -0.0308 -0.3540 0.1806  124 ASP   W O   
40346 C  CB  . ASP   W  125 ? 1.7397 0.5011 1.4684 -0.0616 -0.2250 0.0627  124 ASP   W CB  
40347 C  CG  . ASP   W  125 ? 1.7901 0.3805 1.5148 -0.1005 -0.1450 0.0584  124 ASP   W CG  
40348 O  OD1 . ASP   W  125 ? 1.8183 0.3750 1.6123 -0.1857 -0.1203 0.0459  124 ASP   W OD1 
40349 O  OD2 . ASP   W  125 ? 1.8569 0.3845 1.5286 -0.1402 -0.0037 -0.0339 124 ASP   W OD2 
40350 N  N   . LEU   W  126 ? 1.5572 0.6409 1.4498 -0.0221 -0.3622 0.1610  125 LEU   W N   
40351 C  CA  . LEU   W  126 ? 1.5091 0.6347 1.4460 -0.0358 -0.4155 0.1070  125 LEU   W CA  
40352 C  C   . LEU   W  126 ? 1.5520 0.6947 1.3919 -0.0573 -0.4585 0.1241  125 LEU   W C   
40353 O  O   . LEU   W  126 ? 1.5515 0.9020 1.3827 -0.1433 -0.4285 -0.0415 125 LEU   W O   
40354 C  CB  . LEU   W  126 ? 1.4383 0.6524 1.3933 -0.0283 -0.4798 0.1199  125 LEU   W CB  
40355 C  CG  . LEU   W  126 ? 1.4502 0.5815 1.3604 -0.0210 -0.4748 0.1001  125 LEU   W CG  
40356 C  CD1 . LEU   W  126 ? 1.3915 0.6641 1.3204 -0.0090 -0.4954 0.0778  125 LEU   W CD1 
40357 C  CD2 . LEU   W  126 ? 1.4301 0.5643 1.3497 -0.0422 -0.4824 0.0985  125 LEU   W CD2 
40358 N  N   . ILE   W  127 ? 1.5249 0.6386 1.4044 -0.0466 -0.4194 0.0924  126 ILE   W N   
40359 C  CA  . ILE   W  127 ? 1.5302 0.5509 1.5113 -0.0033 -0.4031 0.0914  126 ILE   W CA  
40360 C  C   . ILE   W  127 ? 1.5258 0.4434 1.3861 0.0273  -0.4259 0.0119  126 ILE   W C   
40361 O  O   . ILE   W  127 ? 1.5521 0.4296 1.2945 0.0510  -0.4596 -0.0646 126 ILE   W O   
40362 C  CB  . ILE   W  127 ? 1.5243 0.5062 1.5593 -0.0305 -0.4007 0.1113  126 ILE   W CB  
40363 C  CG1 . ILE   W  127 ? 1.5382 0.6100 1.6759 -0.0026 -0.4127 0.1068  126 ILE   W CG1 
40364 C  CG2 . ILE   W  127 ? 1.5288 0.4263 1.5437 -0.0573 -0.3885 0.1742  126 ILE   W CG2 
40365 C  CD1 . ILE   W  127 ? 1.5720 0.7030 1.6932 -0.0184 -0.3856 0.0744  126 ILE   W CD1 
40366 N  N   . GLY   W  128 ? 1.5110 0.4102 1.3849 0.0122  -0.3986 -0.0174 127 GLY   W N   
40367 C  CA  . GLY   W  128 ? 1.5637 0.4228 1.4004 -0.0117 -0.3381 0.0347  127 GLY   W CA  
40368 C  C   . GLY   W  128 ? 1.6255 0.4259 1.3856 -0.0070 -0.3004 0.0651  127 GLY   W C   
40369 O  O   . GLY   W  128 ? 1.6177 0.5515 1.3793 -0.0633 -0.2778 0.0822  127 GLY   W O   
40370 N  N   . CYS   W  129 ? 1.6179 0.4229 1.3718 -0.0501 -0.3105 0.0663  128 CYS   W N   
40371 C  CA  . CYS   W  129 ? 1.6498 0.4923 1.3898 -0.0180 -0.2911 0.0598  128 CYS   W CA  
40372 C  C   . CYS   W  129 ? 1.6483 0.5248 1.4346 -0.0049 -0.2942 -0.0073 128 CYS   W C   
40373 O  O   . CYS   W  129 ? 1.6627 0.4543 1.4979 0.0819  -0.2515 -0.0574 128 CYS   W O   
40374 C  CB  . CYS   W  129 ? 1.6563 0.5197 1.4054 -0.0068 -0.3233 0.0400  128 CYS   W CB  
40375 S  SG  . CYS   W  129 ? 1.6249 0.6218 1.5058 0.0293  -0.2870 0.1205  128 CYS   W SG  
40376 N  N   . ILE   W  130 ? 1.6658 0.5621 1.4293 -0.0292 -0.3075 0.0054  129 ILE   W N   
40377 C  CA  . ILE   W  130 ? 1.6816 0.5825 1.4576 -0.0047 -0.3309 -0.0101 129 ILE   W CA  
40378 C  C   . ILE   W  130 ? 1.7691 0.5258 1.4275 -0.0192 -0.3181 -0.0299 129 ILE   W C   
40379 O  O   . ILE   W  130 ? 1.7265 0.3844 1.4299 0.0188  -0.2786 -0.0727 129 ILE   W O   
40380 C  CB  . ILE   W  130 ? 1.6681 0.5981 1.4661 -0.0217 -0.3368 -0.0074 129 ILE   W CB  
40381 C  CG1 . ILE   W  130 ? 1.5938 0.5819 1.4386 -0.0097 -0.3762 0.0396  129 ILE   W CG1 
40382 C  CG2 . ILE   W  130 ? 1.6598 0.5958 1.5071 -0.0674 -0.3213 -0.0353 129 ILE   W CG2 
40383 C  CD1 . ILE   W  130 ? 1.5757 0.6117 1.4306 -0.0077 -0.3672 0.0702  129 ILE   W CD1 
40384 N  N   . ASP   W  131 ? 1.8356 0.5257 1.5505 0.0105  -0.3449 0.0096  130 ASP   W N   
40385 C  CA  . ASP   W  131 ? 1.9121 0.6752 1.6384 0.1063  -0.2944 0.0209  130 ASP   W CA  
40386 C  C   . ASP   W  131 ? 1.8543 0.6251 1.7165 0.0433  -0.2371 0.1114  130 ASP   W C   
40387 O  O   . ASP   W  131 ? 1.7997 0.4587 1.7307 0.0413  -0.2689 0.0988  130 ASP   W O   
40388 C  CB  . ASP   W  131 ? 2.0852 0.7288 1.6631 0.0808  -0.2756 0.0800  130 ASP   W CB  
40389 C  CG  . ASP   W  131 ? 2.1769 0.8936 1.7161 0.1962  -0.2937 0.0419  130 ASP   W CG  
40390 O  OD1 . ASP   W  131 ? 2.2755 1.1215 1.6839 0.1924  -0.2451 0.0425  130 ASP   W OD1 
40391 O  OD2 . ASP   W  131 ? 2.3695 1.0316 1.6847 0.1393  -0.3340 0.0952  130 ASP   W OD2 
40392 N  N   . GLU   W  132 ? 1.8399 0.7929 1.7315 0.0812  -0.2118 0.1887  131 GLU   W N   
40393 C  CA  . GLU   W  132 ? 1.8252 0.8908 1.7595 0.0557  -0.2017 0.2165  131 GLU   W CA  
40394 C  C   . GLU   W  132 ? 1.7910 0.9018 1.7284 0.0451  -0.1931 0.2375  131 GLU   W C   
40395 O  O   . GLU   W  132 ? 1.8007 0.9933 1.5748 0.0743  -0.2102 0.3146  131 GLU   W O   
40396 C  CB  . GLU   W  132 ? 1.8443 0.8883 1.8660 0.0474  -0.1379 0.2232  131 GLU   W CB  
40397 C  CG  . GLU   W  132 ? 1.8454 1.0065 1.9118 0.0895  -0.1552 0.1356  131 GLU   W CG  
40398 C  CD  . GLU   W  132 ? 1.8482 1.0962 1.9548 0.1372  -0.0672 0.2032  131 GLU   W CD  
40399 O  OE1 . GLU   W  132 ? 2.0173 1.0495 1.8463 0.1607  -0.1484 0.2905  131 GLU   W OE1 
40400 O  OE2 . GLU   W  132 ? 1.8659 1.3196 2.0946 0.1073  -0.0114 0.2060  131 GLU   W OE2 
40401 N  N   . ALA   W  133 ? 1.7306 0.8649 1.7717 -0.0840 -0.2061 0.2000  132 ALA   W N   
40402 C  CA  . ALA   W  133 ? 1.6927 0.8873 1.7790 -0.0931 -0.2118 0.2286  132 ALA   W CA  
40403 C  C   . ALA   W  133 ? 1.7417 0.7951 1.7396 -0.1379 -0.2183 0.2241  132 ALA   W C   
40404 O  O   . ALA   W  133 ? 1.7048 0.8608 1.7406 -0.1537 -0.2632 0.1936  132 ALA   W O   
40405 C  CB  . ALA   W  133 ? 1.7076 0.9820 1.7801 -0.0769 -0.1746 0.2859  132 ALA   W CB  
40406 N  N   . LYS   W  134 ? 1.7619 0.8368 1.7260 -0.1191 -0.2089 0.2407  133 LYS   W N   
40407 C  CA  . LYS   W  134 ? 1.7827 0.9947 1.7724 -0.1028 -0.2432 0.2230  133 LYS   W CA  
40408 C  C   . LYS   W  134 ? 1.7910 0.9089 1.8041 -0.0708 -0.2676 0.2099  133 LYS   W C   
40409 O  O   . LYS   W  134 ? 1.8554 0.8503 1.7942 0.0215  -0.3022 0.1825  133 LYS   W O   
40410 C  CB  . LYS   W  134 ? 1.8597 1.2240 1.8300 -0.1571 -0.1597 0.1839  133 LYS   W CB  
40411 C  CG  . LYS   W  134 ? 1.9498 1.3701 1.8257 -0.2468 -0.0643 0.2182  133 LYS   W CG  
40412 C  CD  . LYS   W  134 ? 2.0085 1.4820 1.9180 -0.3442 0.0423  0.1813  133 LYS   W CD  
40413 C  CE  . LYS   W  134 ? 2.0876 1.5168 1.9150 -0.4066 0.1287  0.1879  133 LYS   W CE  
40414 N  NZ  . LYS   W  134 ? 2.1329 1.5908 1.9637 -0.4244 0.2087  0.1712  133 LYS   W NZ  
40415 N  N   . ASP   W  135 ? 1.7690 0.8656 1.7091 -0.0241 -0.3132 0.2109  134 ASP   W N   
40416 C  CA  . ASP   W  135 ? 1.7835 0.7128 1.7313 0.0190  -0.2860 0.1417  134 ASP   W CA  
40417 C  C   . ASP   W  135 ? 1.6884 0.6470 1.7283 0.0287  -0.3226 0.1323  134 ASP   W C   
40418 O  O   . ASP   W  135 ? 1.7591 0.7247 1.7385 0.0316  -0.3015 0.1049  134 ASP   W O   
40419 C  CB  . ASP   W  135 ? 1.8412 0.7068 1.7544 0.0805  -0.2742 0.1617  134 ASP   W CB  
40420 C  CG  . ASP   W  135 ? 1.8091 0.6527 1.7641 0.1358  -0.2876 0.2082  134 ASP   W CG  
40421 O  OD1 . ASP   W  135 ? 1.9284 0.3977 1.7447 0.1978  -0.3016 0.2523  134 ASP   W OD1 
40422 O  OD2 . ASP   W  135 ? 1.9385 0.8619 1.7531 0.0934  -0.2041 0.1497  134 ASP   W OD2 
40423 N  N   . PHE   W  136 ? 1.6668 0.5563 1.5606 0.0823  -0.3637 0.0984  135 PHE   W N   
40424 C  CA  . PHE   W  136 ? 1.5858 0.5919 1.5304 0.0618  -0.4148 0.0842  135 PHE   W CA  
40425 C  C   . PHE   W  136 ? 1.5798 0.5758 1.4740 0.0697  -0.3970 0.0916  135 PHE   W C   
40426 O  O   . PHE   W  136 ? 1.5792 0.4402 1.4425 0.1002  -0.3635 0.1386  135 PHE   W O   
40427 C  CB  . PHE   W  136 ? 1.5948 0.6127 1.5345 0.0667  -0.4340 0.1052  135 PHE   W CB  
40428 C  CG  . PHE   W  136 ? 1.6124 0.6148 1.5180 0.0569  -0.4534 0.1168  135 PHE   W CG  
40429 C  CD1 . PHE   W  136 ? 1.5894 0.6228 1.5121 0.0664  -0.4568 0.1416  135 PHE   W CD1 
40430 C  CD2 . PHE   W  136 ? 1.6302 0.6300 1.5322 0.0658  -0.4353 0.1409  135 PHE   W CD2 
40431 C  CE1 . PHE   W  136 ? 1.6237 0.6364 1.5128 0.0906  -0.4452 0.1393  135 PHE   W CE1 
40432 C  CE2 . PHE   W  136 ? 1.6404 0.6234 1.5158 0.0861  -0.4355 0.1519  135 PHE   W CE2 
40433 C  CZ  . PHE   W  136 ? 1.6315 0.6530 1.5215 0.0893  -0.4327 0.1454  135 PHE   W CZ  
40434 N  N   . ILE   W  137 ? 1.5628 0.6708 1.4330 0.0530  -0.4178 0.0753  136 ILE   W N   
40435 C  CA  . ILE   W  137 ? 1.5676 0.7655 1.3686 0.0100  -0.4305 0.0596  136 ILE   W CA  
40436 C  C   . ILE   W  137 ? 1.5167 0.6492 1.3317 0.0416  -0.4753 0.0288  136 ILE   W C   
40437 O  O   . ILE   W  137 ? 1.5453 0.6311 1.3099 0.0370  -0.4593 0.0782  136 ILE   W O   
40438 C  CB  . ILE   W  137 ? 1.5683 0.7919 1.3889 0.0053  -0.4167 -0.0020 136 ILE   W CB  
40439 C  CG1 . ILE   W  137 ? 1.5991 0.9203 1.3892 -0.0523 -0.3768 0.0001  136 ILE   W CG1 
40440 C  CG2 . ILE   W  137 ? 1.5685 0.8293 1.3574 -0.0292 -0.4114 -0.0175 136 ILE   W CG2 
40441 C  CD1 . ILE   W  137 ? 1.6025 1.0147 1.3756 -0.0506 -0.3617 0.0004  136 ILE   W CD1 
40442 N  N   . VAL   W  138 ? 1.4910 0.5862 1.2915 0.0930  -0.4943 0.0180  137 VAL   W N   
40443 C  CA  . VAL   W  138 ? 1.4552 0.5967 1.2430 0.1071  -0.5266 0.0199  137 VAL   W CA  
40444 C  C   . VAL   W  138 ? 1.4499 0.5520 1.2373 0.0937  -0.5069 0.0097  137 VAL   W C   
40445 O  O   . VAL   W  138 ? 1.4341 0.4072 1.3134 0.1242  -0.5163 0.0220  137 VAL   W O   
40446 C  CB  . VAL   W  138 ? 1.4603 0.6015 1.2620 0.1386  -0.5414 0.0337  137 VAL   W CB  
40447 C  CG1 . VAL   W  138 ? 1.4627 0.6279 1.2743 0.1388  -0.5513 0.0201  137 VAL   W CG1 
40448 C  CG2 . VAL   W  138 ? 1.4352 0.6127 1.2725 0.1391  -0.5489 0.0414  137 VAL   W CG2 
40449 N  N   . SER   W  139 ? 1.4760 0.5871 1.1859 0.0848  -0.5389 0.0239  138 SER   W N   
40450 C  CA  . SER   W  139 ? 1.4885 0.6257 1.1973 0.0816  -0.5040 0.0426  138 SER   W CA  
40451 C  C   . SER   W  139 ? 1.5126 0.6359 1.1661 0.0628  -0.5275 0.0380  138 SER   W C   
40452 O  O   . SER   W  139 ? 1.5246 0.6904 1.2132 0.1016  -0.5382 0.0627  138 SER   W O   
40453 C  CB  . SER   W  139 ? 1.5095 0.6196 1.2386 0.0945  -0.4891 0.0691  138 SER   W CB  
40454 O  OG  . SER   W  139 ? 1.5022 0.6780 1.3318 0.1095  -0.4521 0.0746  138 SER   W OG  
40455 N  N   . GLY   W  140 ? 1.5428 0.6087 1.1823 0.0105  -0.5094 0.0145  139 GLY   W N   
40456 C  CA  . GLY   W  140 ? 1.5597 0.6315 1.2140 0.0006  -0.4990 0.0330  139 GLY   W CA  
40457 C  C   . GLY   W  140 ? 1.6010 0.6263 1.2783 -0.0154 -0.4550 0.0390  139 GLY   W C   
40458 O  O   . GLY   W  140 ? 1.6821 0.6267 1.3240 0.0225  -0.3648 0.0094  139 GLY   W O   
40459 N  N   . THR   W  141 ? 1.5739 0.5666 1.3535 -0.0675 -0.4479 0.0285  140 THR   W N   
40460 C  CA  . THR   W  141 ? 1.6021 0.5298 1.3930 -0.0385 -0.4390 0.0344  140 THR   W CA  
40461 C  C   . THR   W  141 ? 1.5587 0.5973 1.4516 -0.0276 -0.4408 0.0459  140 THR   W C   
40462 O  O   . THR   W  141 ? 1.6044 0.6208 1.5279 0.0049  -0.4224 -0.0160 140 THR   W O   
40463 C  CB  . THR   W  141 ? 1.6181 0.4711 1.3898 -0.0416 -0.4477 0.0510  140 THR   W CB  
40464 O  OG1 . THR   W  141 ? 1.6083 0.3743 1.3952 -0.0556 -0.4565 0.0765  140 THR   W OG1 
40465 C  CG2 . THR   W  141 ? 1.6337 0.4384 1.3970 -0.0330 -0.4271 0.0570  140 THR   W CG2 
40466 N  N   . ALA   W  142 ? 1.6001 0.4942 1.4232 -0.0826 -0.4492 0.0039  141 ALA   W N   
40467 C  CA  . ALA   W  142 ? 1.6212 0.5273 1.4404 -0.0696 -0.4418 -0.0145 141 ALA   W CA  
40468 C  C   . ALA   W  142 ? 1.6787 0.4008 1.4266 -0.0856 -0.4550 -0.0313 141 ALA   W C   
40469 O  O   . ALA   W  142 ? 1.6850 0.2899 1.4194 -0.0706 -0.4777 -0.0198 141 ALA   W O   
40470 C  CB  . ALA   W  142 ? 1.6420 0.6071 1.4256 -0.0662 -0.4323 -0.0112 141 ALA   W CB  
40471 N  N   . SER   W  143 ? 1.6981 0.4164 1.4173 -0.0862 -0.4822 -0.0573 142 SER   W N   
40472 C  CA  . SER   W  143 ? 1.7295 0.4827 1.4494 -0.1182 -0.4384 -0.0771 142 SER   W CA  
40473 C  C   . SER   W  143 ? 1.7241 0.4986 1.4933 -0.0640 -0.4342 -0.0531 142 SER   W C   
40474 O  O   . SER   W  143 ? 1.7360 0.3271 1.5015 -0.1138 -0.4420 -0.1104 142 SER   W O   
40475 C  CB  . SER   W  143 ? 1.7559 0.4548 1.4841 -0.1344 -0.4528 -0.0773 142 SER   W CB  
40476 O  OG  . SER   W  143 ? 1.8762 0.4979 1.5941 -0.2525 -0.4330 -0.1268 142 SER   W OG  
40477 N  N   . ASP   W  144 ? 1.7400 0.4885 1.4972 -0.0536 -0.4500 -0.0491 143 ASP   W N   
40478 C  CA  . ASP   W  144 ? 1.7504 0.5515 1.5007 -0.0173 -0.4289 -0.0486 143 ASP   W CA  
40479 C  C   . ASP   W  144 ? 1.7376 0.4786 1.4671 -0.0336 -0.4146 -0.0296 143 ASP   W C   
40480 O  O   . ASP   W  144 ? 1.7340 0.4673 1.5143 -0.0426 -0.3974 0.0089  143 ASP   W O   
40481 C  CB  . ASP   W  144 ? 1.7708 0.6531 1.5888 -0.0842 -0.4212 -0.0464 143 ASP   W CB  
40482 C  CG  . ASP   W  144 ? 1.8040 0.7230 1.6145 0.0090  -0.4098 0.0107  143 ASP   W CG  
40483 O  OD1 . ASP   W  144 ? 1.7957 0.6231 1.6515 -0.0217 -0.3581 -0.1126 143 ASP   W OD1 
40484 O  OD2 . ASP   W  144 ? 1.8415 0.8971 1.6430 -0.0355 -0.3744 -0.1307 143 ASP   W OD2 
40485 N  N   . GLN   W  145 ? 1.6472 0.4058 1.4568 0.0082  -0.4562 -0.0243 144 GLN   W N   
40486 C  CA  . GLN   W  145 ? 1.6521 0.4238 1.4489 0.0308  -0.4515 -0.0011 144 GLN   W CA  
40487 C  C   . GLN   W  145 ? 1.5694 0.5058 1.4555 0.0346  -0.4773 0.0230  144 GLN   W C   
40488 O  O   . GLN   W  145 ? 1.6027 0.4890 1.4530 0.1255  -0.5011 0.0906  144 GLN   W O   
40489 C  CB  . GLN   W  145 ? 1.6042 0.3972 1.4454 0.0148  -0.4643 -0.0014 144 GLN   W CB  
40490 C  CG  . GLN   W  145 ? 1.5973 0.4356 1.4578 -0.0055 -0.4432 0.0034  144 GLN   W CG  
40491 C  CD  . GLN   W  145 ? 1.5815 0.3682 1.4341 -0.0373 -0.4430 0.0120  144 GLN   W CD  
40492 O  OE1 . GLN   W  145 ? 1.5337 0.2444 1.4147 -0.0617 -0.4378 -0.0585 144 GLN   W OE1 
40493 N  NE2 . GLN   W  145 ? 1.5653 0.4643 1.4631 -0.0808 -0.4287 -0.0029 144 GLN   W NE2 
40494 N  N   . LEU   W  146 ? 1.5915 0.5439 1.4531 0.0857  -0.4814 0.0058  145 LEU   W N   
40495 C  CA  . LEU   W  146 ? 1.5814 0.5260 1.4583 0.1035  -0.5053 0.0257  145 LEU   W CA  
40496 C  C   . LEU   W  146 ? 1.5720 0.4765 1.4475 0.1271  -0.5174 0.0172  145 LEU   W C   
40497 O  O   . LEU   W  146 ? 1.5609 0.4986 1.4913 0.1447  -0.5294 0.0422  145 LEU   W O   
40498 C  CB  . LEU   W  146 ? 1.5609 0.5764 1.4367 0.1390  -0.5156 0.0312  145 LEU   W CB  
40499 C  CG  . LEU   W  146 ? 1.5441 0.5714 1.4308 0.1354  -0.5589 -0.0046 145 LEU   W CG  
40500 C  CD1 . LEU   W  146 ? 1.5348 0.5423 1.4397 0.1140  -0.5616 -0.0264 145 LEU   W CD1 
40501 C  CD2 . LEU   W  146 ? 1.5654 0.5979 1.4423 0.1179  -0.5696 -0.0352 145 LEU   W CD2 
40502 N  N   . PHE   W  147 ? 1.5847 0.4541 1.4646 0.1225  -0.5272 -0.0231 146 PHE   W N   
40503 C  CA  . PHE   W  147 ? 1.5889 0.5903 1.4653 0.1028  -0.5326 -0.0470 146 PHE   W CA  
40504 C  C   . PHE   W  147 ? 1.5278 0.6830 1.5203 0.1123  -0.5384 -0.0261 146 PHE   W C   
40505 O  O   . PHE   W  147 ? 1.4978 0.8138 1.5698 0.1059  -0.5355 -0.0443 146 PHE   W O   
40506 C  CB  . PHE   W  147 ? 1.6163 0.5744 1.4514 0.1114  -0.5397 -0.0555 146 PHE   W CB  
40507 C  CG  . PHE   W  147 ? 1.6336 0.5888 1.4074 0.1065  -0.5477 -0.0406 146 PHE   W CG  
40508 C  CD1 . PHE   W  147 ? 1.6311 0.5829 1.3924 0.0919  -0.5596 -0.0593 146 PHE   W CD1 
40509 C  CD2 . PHE   W  147 ? 1.6339 0.6032 1.3965 0.1012  -0.5484 -0.0292 146 PHE   W CD2 
40510 C  CE1 . PHE   W  147 ? 1.6412 0.5572 1.3990 0.0692  -0.5515 -0.0585 146 PHE   W CE1 
40511 C  CE2 . PHE   W  147 ? 1.6376 0.5839 1.3892 0.0903  -0.5480 -0.0421 146 PHE   W CE2 
40512 C  CZ  . PHE   W  147 ? 1.6433 0.5948 1.4073 0.0677  -0.5431 -0.0635 146 PHE   W CZ  
40513 N  N   . GLY   W  148 ? 1.5137 0.6939 1.5406 0.1174  -0.5493 -0.0033 147 GLY   W N   
40514 C  CA  . GLY   W  148 ? 1.5177 0.7074 1.5794 0.1243  -0.5268 0.0035  147 GLY   W CA  
40515 C  C   . GLY   W  148 ? 1.5112 0.7692 1.5693 0.0848  -0.5129 0.0103  147 GLY   W C   
40516 O  O   . GLY   W  148 ? 1.4312 0.8735 1.5100 0.0066  -0.5613 0.0257  147 GLY   W O   
40517 N  N   . MET   W  149 ? 1.5266 0.7959 1.5723 0.1328  -0.4536 0.0469  148 MET   W N   
40518 C  CA  . MET   W  149 ? 1.5005 0.8328 1.5839 0.1541  -0.4482 0.0646  148 MET   W CA  
40519 C  C   . MET   W  149 ? 1.5144 0.8250 1.6694 0.1620  -0.4370 0.0856  148 MET   W C   
40520 O  O   . MET   W  149 ? 1.5275 0.7914 1.7583 0.2199  -0.3977 0.0984  148 MET   W O   
40521 C  CB  . MET   W  149 ? 1.5199 0.8736 1.5681 0.1424  -0.4362 0.0658  148 MET   W CB  
40522 C  CG  . MET   W  149 ? 1.5464 0.9277 1.5150 0.1389  -0.4062 0.0711  148 MET   W CG  
40523 S  SD  . MET   W  149 ? 1.5503 1.0680 1.4870 0.2132  -0.4009 0.1193  148 MET   W SD  
40524 C  CE  . MET   W  149 ? 1.6194 0.9800 1.4859 0.1667  -0.3984 0.0827  148 MET   W CE  
40525 N  N   . CYS   W  150 ? 1.5301 0.8454 1.6388 0.1491  -0.4656 0.1115  149 CYS   W N   
40526 C  CA  . CYS   W  150 ? 1.5314 0.8900 1.5784 0.1406  -0.4728 0.1506  149 CYS   W CA  
40527 C  C   . CYS   W  150 ? 1.6192 0.9164 1.5270 0.1090  -0.4785 0.1271  149 CYS   W C   
40528 O  O   . CYS   W  150 ? 1.6057 0.9886 1.5270 0.1383  -0.4418 0.1531  149 CYS   W O   
40529 C  CB  . CYS   W  150 ? 1.5238 0.9116 1.5878 0.1433  -0.4998 0.1719  149 CYS   W CB  
40530 S  SG  . CYS   W  150 ? 1.4920 0.8018 1.5782 0.2460  -0.5652 0.1972  149 CYS   W SG  
40531 N  N   . GLU   W  151 ? 1.6516 0.9111 1.4962 0.0773  -0.4288 0.1077  150 GLU   W N   
40532 C  CA  . GLU   W  151 ? 1.6898 0.9907 1.4948 0.0573  -0.4203 0.0983  150 GLU   W CA  
40533 C  C   . GLU   W  151 ? 1.7017 1.0435 1.4581 0.0737  -0.4315 0.1925  150 GLU   W C   
40534 O  O   . GLU   W  151 ? 1.6943 1.1691 1.5054 0.0391  -0.4088 0.1569  150 GLU   W O   
40535 C  CB  . GLU   W  151 ? 1.7331 1.0106 1.5258 0.0297  -0.4182 0.0601  150 GLU   W CB  
40536 C  CG  . GLU   W  151 ? 1.7630 0.9903 1.5429 -0.0093 -0.4010 0.0463  150 GLU   W CG  
40537 C  CD  . GLU   W  151 ? 1.7285 0.9698 1.6068 -0.0516 -0.3972 0.0330  150 GLU   W CD  
40538 O  OE1 . GLU   W  151 ? 1.6513 0.8632 1.5021 -0.1403 -0.4380 -0.0138 150 GLU   W OE1 
40539 O  OE2 . GLU   W  151 ? 1.7661 0.9659 1.6763 -0.0670 -0.3691 0.1010  150 GLU   W OE2 
40540 N  N   . SER   W  152 ? 1.6963 1.0994 1.4798 0.1357  -0.4723 0.2234  151 SER   W N   
40541 C  CA  . SER   W  152 ? 1.7332 1.1230 1.5008 0.1708  -0.4683 0.2539  151 SER   W CA  
40542 C  C   . SER   W  152 ? 1.6938 1.0744 1.6079 0.1559  -0.4793 0.2590  151 SER   W C   
40543 O  O   . SER   W  152 ? 1.7128 1.0284 1.5356 0.1915  -0.4515 0.2846  151 SER   W O   
40544 C  CB  . SER   W  152 ? 1.7524 1.1177 1.5072 0.2226  -0.4529 0.2857  151 SER   W CB  
40545 O  OG  . SER   W  152 ? 1.7668 1.1402 1.5483 0.2102  -0.4051 0.3754  151 SER   W OG  
40546 N  N   . LEU   W  153 ? 1.6708 1.0328 1.6689 0.1229  -0.4884 0.2002  152 LEU   W N   
40547 C  CA  . LEU   W  153 ? 1.6678 1.0318 1.6550 0.0922  -0.4594 0.1831  152 LEU   W CA  
40548 C  C   . LEU   W  153 ? 1.6717 0.9922 1.7350 0.1018  -0.5072 0.1818  152 LEU   W C   
40549 O  O   . LEU   W  153 ? 1.6917 0.9390 1.8077 0.0273  -0.4955 0.1590  152 LEU   W O   
40550 C  CB  . LEU   W  153 ? 1.6735 1.0376 1.5925 0.0782  -0.4903 0.1580  152 LEU   W CB  
40551 C  CG  . LEU   W  153 ? 1.6979 1.1061 1.5131 0.0883  -0.4442 0.1800  152 LEU   W CG  
40552 C  CD1 . LEU   W  153 ? 1.7105 1.0841 1.5201 0.0799  -0.4608 0.1463  152 LEU   W CD1 
40553 C  CD2 . LEU   W  153 ? 1.7198 1.1778 1.5167 0.1330  -0.4474 0.1940  152 LEU   W CD2 
40554 N  N   . TYR   W  154 ? 1.5851 0.9420 1.7620 0.0897  -0.4820 0.1674  153 TYR   W N   
40555 C  CA  . TYR   W  154 ? 1.6143 0.9403 1.7394 0.0773  -0.4628 0.1440  153 TYR   W CA  
40556 C  C   . TYR   W  154 ? 1.5655 0.9232 1.7265 0.1313  -0.4989 0.1797  153 TYR   W C   
40557 O  O   . TYR   W  154 ? 1.5532 0.9581 1.6453 0.1906  -0.5338 0.2166  153 TYR   W O   
40558 C  CB  . TYR   W  154 ? 1.6198 0.9073 1.7236 0.0653  -0.4507 0.1318  153 TYR   W CB  
40559 C  CG  . TYR   W  154 ? 1.7379 0.8985 1.7795 0.0338  -0.4116 0.0715  153 TYR   W CG  
40560 C  CD1 . TYR   W  154 ? 1.7763 0.8688 1.8030 0.0280  -0.4122 0.0716  153 TYR   W CD1 
40561 C  CD2 . TYR   W  154 ? 1.7941 0.8548 1.8071 0.0392  -0.3628 0.0590  153 TYR   W CD2 
40562 C  CE1 . TYR   W  154 ? 1.8244 0.8784 1.8423 0.0043  -0.3722 0.0694  153 TYR   W CE1 
40563 C  CE2 . TYR   W  154 ? 1.8144 0.8791 1.8535 0.0011  -0.3332 0.0759  153 TYR   W CE2 
40564 C  CZ  . TYR   W  154 ? 1.8300 0.8694 1.8879 -0.0355 -0.3244 0.0610  153 TYR   W CZ  
40565 O  OH  . TYR   W  154 ? 1.8502 0.9048 1.9937 -0.0709 -0.2534 0.1146  153 TYR   W OH  
40566 N  N   . GLU   W  155 ? 1.5767 0.9349 1.7555 0.1120  -0.4756 0.1669  154 GLU   W N   
40567 C  CA  . GLU   W  155 ? 1.6090 1.0212 1.8108 0.0860  -0.4358 0.1610  154 GLU   W CA  
40568 C  C   . GLU   W  155 ? 1.5712 1.0259 1.8184 0.0650  -0.4072 0.1721  154 GLU   W C   
40569 O  O   . GLU   W  155 ? 1.5088 1.1115 1.8372 0.0837  -0.3805 0.1590  154 GLU   W O   
40570 C  CB  . GLU   W  155 ? 1.6265 1.0338 1.8820 0.1063  -0.4377 0.1637  154 GLU   W CB  
40571 C  CG  . GLU   W  155 ? 1.6588 1.1177 1.8850 0.0685  -0.4382 0.1725  154 GLU   W CG  
40572 C  CD  . GLU   W  155 ? 1.6271 1.2136 1.9786 0.0628  -0.4206 0.1841  154 GLU   W CD  
40573 O  OE1 . GLU   W  155 ? 1.6402 1.3394 2.0942 0.0235  -0.3855 0.1848  154 GLU   W OE1 
40574 O  OE2 . GLU   W  155 ? 1.7052 1.2276 1.9875 0.0880  -0.4366 0.2001  154 GLU   W OE2 
40575 N  N   . PRO   W  156 ? 1.5294 0.8739 1.8374 0.0825  -0.4125 0.1471  155 PRO   W N   
40576 C  CA  . PRO   W  156 ? 1.4879 0.8652 1.8478 0.1106  -0.3902 0.1813  155 PRO   W CA  
40577 C  C   . PRO   W  156 ? 1.5023 0.9036 1.8909 0.1361  -0.4255 0.1687  155 PRO   W C   
40578 O  O   . PRO   W  156 ? 1.5245 0.9066 1.9274 0.1409  -0.4481 0.1808  155 PRO   W O   
40579 C  CB  . PRO   W  156 ? 1.4646 0.8367 1.8457 0.0814  -0.3704 0.1596  155 PRO   W CB  
40580 C  CG  . PRO   W  156 ? 1.4773 0.8367 1.8180 0.0705  -0.3612 0.1649  155 PRO   W CG  
40581 C  CD  . PRO   W  156 ? 1.5256 0.8859 1.8017 0.0597  -0.3953 0.1816  155 PRO   W CD  
40582 N  N   . ASN   W  157 ? 1.5528 0.9540 1.9009 0.1295  -0.3987 0.1023  156 ASN   W N   
40583 C  CA  . ASN   W  157 ? 1.5513 1.0254 1.9309 0.1013  -0.3994 0.0916  156 ASN   W CA  
40584 C  C   . ASN   W  157 ? 1.5662 0.9715 1.9333 0.0865  -0.4224 0.0749  156 ASN   W C   
40585 O  O   . ASN   W  157 ? 1.5806 0.9621 1.9490 0.1041  -0.4500 0.0415  156 ASN   W O   
40586 C  CB  . ASN   W  157 ? 1.5814 1.1275 2.0197 0.0922  -0.3381 0.0711  156 ASN   W CB  
40587 C  CG  . ASN   W  157 ? 1.6218 1.1569 2.0060 0.0831  -0.2869 0.0873  156 ASN   W CG  
40588 O  OD1 . ASN   W  157 ? 1.6508 1.2599 2.0515 0.0523  -0.2216 0.0314  156 ASN   W OD1 
40589 N  ND2 . ASN   W  157 ? 1.6534 1.1850 2.0448 0.0806  -0.2429 0.0220  156 ASN   W ND2 
40590 N  N   . LEU   W  158 ? 1.5910 0.9408 1.8840 0.0626  -0.4458 0.0801  157 LEU   W N   
40591 C  CA  . LEU   W  158 ? 1.6206 1.0380 1.8399 0.0124  -0.4636 0.0442  157 LEU   W CA  
40592 C  C   . LEU   W  158 ? 1.6316 1.0053 1.8684 0.0247  -0.4395 0.0455  157 LEU   W C   
40593 O  O   . LEU   W  158 ? 1.5413 1.0575 1.8123 0.0266  -0.4783 0.1086  157 LEU   W O   
40594 C  CB  . LEU   W  158 ? 1.6304 1.0346 1.8398 0.0007  -0.4676 0.0252  157 LEU   W CB  
40595 C  CG  . LEU   W  158 ? 1.6363 1.0195 1.8473 -0.0198 -0.4640 0.0373  157 LEU   W CG  
40596 C  CD1 . LEU   W  158 ? 1.6359 0.9668 1.7978 -0.0171 -0.4855 0.0302  157 LEU   W CD1 
40597 C  CD2 . LEU   W  158 ? 1.6409 1.0440 1.8765 -0.0116 -0.4719 0.0421  157 LEU   W CD2 
40598 N  N   . GLU   W  159 ? 1.6877 1.2031 1.7933 -0.0562 -0.4468 -0.0391 158 GLU   W N   
40599 C  CA  . GLU   W  159 ? 1.7035 1.2506 1.8315 -0.0877 -0.4077 -0.0942 158 GLU   W CA  
40600 C  C   . GLU   W  159 ? 1.6871 1.2855 1.7385 -0.0592 -0.4498 -0.1169 158 GLU   W C   
40601 O  O   . GLU   W  159 ? 1.6849 1.2783 1.6885 -0.0379 -0.4104 -0.1211 158 GLU   W O   
40602 C  CB  . GLU   W  159 ? 1.6732 1.3029 1.7991 -0.1188 -0.3919 -0.1578 158 GLU   W CB  
40603 C  CG  . GLU   W  159 ? 1.7359 1.3456 1.8356 -0.1162 -0.3136 -0.2007 158 GLU   W CG  
40604 C  CD  . GLU   W  159 ? 1.7183 1.3350 1.8423 -0.1361 -0.2327 -0.2373 158 GLU   W CD  
40605 O  OE1 . GLU   W  159 ? 1.7140 1.3445 1.8753 -0.1395 -0.2411 -0.2617 158 GLU   W OE1 
40606 O  OE2 . GLU   W  159 ? 1.7335 1.2783 1.8709 -0.1335 -0.1625 -0.2865 158 GLU   W OE2 
40607 N  N   . PRO   W  160 ? 1.6200 1.2920 1.7310 -0.0831 -0.5156 -0.1434 159 PRO   W N   
40608 C  CA  . PRO   W  160 ? 1.5459 1.3198 1.7154 -0.0898 -0.5695 -0.1533 159 PRO   W CA  
40609 C  C   . PRO   W  160 ? 1.5041 1.3121 1.7305 -0.0797 -0.5744 -0.1609 159 PRO   W C   
40610 O  O   . PRO   W  160 ? 1.4169 1.4409 1.6634 -0.0363 -0.6405 -0.1823 159 PRO   W O   
40611 C  CB  . PRO   W  160 ? 1.5756 1.3217 1.7138 -0.0911 -0.5769 -0.1522 159 PRO   W CB  
40612 C  CG  . PRO   W  160 ? 1.5976 1.3415 1.7464 -0.0980 -0.5633 -0.1391 159 PRO   W CG  
40613 C  CD  . PRO   W  160 ? 1.6139 1.3313 1.7740 -0.1121 -0.5287 -0.1332 159 PRO   W CD  
40614 N  N   . GLU   W  161 ? 1.5454 1.3067 1.8341 -0.0206 -0.5993 -0.1880 160 GLU   W N   
40615 C  CA  . GLU   W  161 ? 1.5613 1.2887 1.8559 0.0103  -0.6052 -0.1833 160 GLU   W CA  
40616 C  C   . GLU   W  161 ? 1.5719 1.2070 1.8444 0.0581  -0.5618 -0.1285 160 GLU   W C   
40617 O  O   . GLU   W  161 ? 1.5031 1.2068 1.8057 0.1117  -0.5710 -0.0914 160 GLU   W O   
40618 C  CB  . GLU   W  161 ? 1.5836 1.3425 1.9014 0.0001  -0.6416 -0.1722 160 GLU   W CB  
40619 C  CG  . GLU   W  161 ? 1.5869 1.4050 1.9139 -0.0015 -0.6517 -0.2071 160 GLU   W CG  
40620 C  CD  . GLU   W  161 ? 1.5570 1.4296 2.0076 -0.0241 -0.6420 -0.1943 160 GLU   W CD  
40621 O  OE1 . GLU   W  161 ? 1.4852 1.4694 2.0169 -0.0136 -0.6077 -0.1410 160 GLU   W OE1 
40622 O  OE2 . GLU   W  161 ? 1.6024 1.4013 2.0444 -0.0669 -0.6429 -0.1772 160 GLU   W OE2 
40623 N  N   . ASP   W  162 ? 1.6038 1.1189 1.8526 0.0725  -0.5650 -0.2009 161 ASP   W N   
40624 C  CA  . ASP   W  162 ? 1.5793 1.0839 1.8766 0.0783  -0.5527 -0.1967 161 ASP   W CA  
40625 C  C   . ASP   W  162 ? 1.5482 1.0338 1.8652 0.0945  -0.5017 -0.1998 161 ASP   W C   
40626 O  O   . ASP   W  162 ? 1.5977 1.0012 1.9191 0.1194  -0.4133 -0.1388 161 ASP   W O   
40627 C  CB  . ASP   W  162 ? 1.5334 1.0556 1.8662 0.0920  -0.5804 -0.2370 161 ASP   W CB  
40628 C  CG  . ASP   W  162 ? 1.5539 1.1059 1.8659 0.1220  -0.6100 -0.2549 161 ASP   W CG  
40629 O  OD1 . ASP   W  162 ? 1.5905 1.0934 1.8354 0.1259  -0.6606 -0.2894 161 ASP   W OD1 
40630 O  OD2 . ASP   W  162 ? 1.4619 1.1575 1.8771 0.1399  -0.6062 -0.2805 161 ASP   W OD2 
40631 N  N   . LEU   W  163 ? 1.5358 1.0252 1.8422 0.0691  -0.4676 -0.1826 162 LEU   W N   
40632 C  CA  . LEU   W  163 ? 1.5401 1.0144 1.7615 0.0529  -0.4583 -0.1677 162 LEU   W CA  
40633 C  C   . LEU   W  163 ? 1.5234 0.9282 1.7219 0.0232  -0.4935 -0.1840 162 LEU   W C   
40634 O  O   . LEU   W  163 ? 1.5472 0.8982 1.6822 0.0072  -0.4709 -0.2307 162 LEU   W O   
40635 C  CB  . LEU   W  163 ? 1.5587 1.0321 1.7499 0.0475  -0.4631 -0.1468 162 LEU   W CB  
40636 C  CG  . LEU   W  163 ? 1.5398 1.0802 1.7007 0.0068  -0.4641 -0.1628 162 LEU   W CG  
40637 C  CD1 . LEU   W  163 ? 1.5309 1.0760 1.7078 -0.0114 -0.4605 -0.1690 162 LEU   W CD1 
40638 C  CD2 . LEU   W  163 ? 1.5057 1.0829 1.7241 0.0175  -0.4564 -0.1491 162 LEU   W CD2 
40639 N  N   . PHE   W  164 ? 1.5566 0.9291 1.6931 0.0382  -0.4830 -0.1378 163 PHE   W N   
40640 C  CA  . PHE   W  164 ? 1.5630 0.9194 1.6418 0.0475  -0.5205 -0.0986 163 PHE   W CA  
40641 C  C   . PHE   W  164 ? 1.5785 0.9169 1.6073 0.0591  -0.5180 -0.0794 163 PHE   W C   
40642 O  O   . PHE   W  164 ? 1.5629 0.8843 1.5961 0.0909  -0.5123 -0.0572 163 PHE   W O   
40643 C  CB  . PHE   W  164 ? 1.5672 0.9768 1.6358 0.0463  -0.5411 -0.0789 163 PHE   W CB  
40644 C  CG  . PHE   W  164 ? 1.5645 1.0187 1.6276 0.0605  -0.5410 -0.0704 163 PHE   W CG  
40645 C  CD1 . PHE   W  164 ? 1.5554 1.0109 1.5850 0.0691  -0.5617 -0.0523 163 PHE   W CD1 
40646 C  CD2 . PHE   W  164 ? 1.5845 1.0455 1.6522 0.0871  -0.5555 -0.0748 163 PHE   W CD2 
40647 C  CE1 . PHE   W  164 ? 1.5562 1.0575 1.5642 0.0657  -0.5551 -0.0697 163 PHE   W CE1 
40648 C  CE2 . PHE   W  164 ? 1.5959 1.0728 1.6167 0.0952  -0.5586 -0.0893 163 PHE   W CE2 
40649 C  CZ  . PHE   W  164 ? 1.5932 1.0706 1.5676 0.0913  -0.5629 -0.0828 163 PHE   W CZ  
40650 N  N   . GLU   W  165 ? 1.6002 0.9407 1.6166 0.0808  -0.5180 -0.0724 164 GLU   W N   
40651 C  CA  . GLU   W  165 ? 1.6375 0.9414 1.6074 0.0588  -0.5227 -0.0783 164 GLU   W CA  
40652 C  C   . GLU   W  165 ? 1.6608 0.8429 1.5728 0.0072  -0.4638 -0.0765 164 GLU   W C   
40653 O  O   . GLU   W  165 ? 1.7260 0.7897 1.6005 0.0023  -0.4507 -0.0998 164 GLU   W O   
40654 C  CB  . GLU   W  165 ? 1.6521 0.9893 1.6352 0.0917  -0.5448 -0.0519 164 GLU   W CB  
40655 C  CG  . GLU   W  165 ? 1.6469 1.0010 1.6558 0.1270  -0.5782 -0.0399 164 GLU   W CG  
40656 C  CD  . GLU   W  165 ? 1.6550 0.9031 1.6545 0.1346  -0.6128 -0.0195 164 GLU   W CD  
40657 O  OE1 . GLU   W  165 ? 1.6150 0.9167 1.6722 0.1665  -0.6403 -0.0262 164 GLU   W OE1 
40658 O  OE2 . GLU   W  165 ? 1.7630 0.7292 1.6224 0.1742  -0.6233 -0.0318 164 GLU   W OE2 
40659 N  N   . THR   W  166 ? 1.6280 0.7834 1.5596 -0.0036 -0.4775 -0.0904 165 THR   W N   
40660 C  CA  . THR   W  166 ? 1.5869 0.7230 1.5134 -0.0174 -0.4497 -0.0477 165 THR   W CA  
40661 C  C   . THR   W  166 ? 1.6037 0.7072 1.4777 0.0409  -0.4431 -0.0538 165 THR   W C   
40662 O  O   . THR   W  166 ? 1.5776 0.7009 1.4597 0.0645  -0.4231 -0.0688 165 THR   W O   
40663 C  CB  . THR   W  166 ? 1.5708 0.7271 1.5486 -0.0535 -0.4344 -0.0445 165 THR   W CB  
40664 O  OG1 . THR   W  166 ? 1.5649 0.7712 1.4832 -0.0696 -0.4549 -0.0202 165 THR   W OG1 
40665 C  CG2 . THR   W  166 ? 1.5611 0.7160 1.5489 -0.0955 -0.4104 -0.0383 165 THR   W CG2 
40666 N  N   . ILE   W  167 ? 1.5967 0.7009 1.4995 0.0219  -0.4362 -0.0576 166 ILE   W N   
40667 C  CA  . ILE   W  167 ? 1.5860 0.7384 1.4985 -0.0025 -0.4299 -0.0573 166 ILE   W CA  
40668 C  C   . ILE   W  167 ? 1.5888 0.7030 1.4704 0.0051  -0.4686 -0.0469 166 ILE   W C   
40669 O  O   . ILE   W  167 ? 1.6080 0.6482 1.4349 0.0046  -0.5257 -0.0283 166 ILE   W O   
40670 C  CB  . ILE   W  167 ? 1.5698 0.7429 1.4933 0.0064  -0.4292 -0.0753 166 ILE   W CB  
40671 C  CG1 . ILE   W  167 ? 1.5518 0.7125 1.4980 -0.0076 -0.4138 -0.0658 166 ILE   W CG1 
40672 C  CG2 . ILE   W  167 ? 1.6198 0.7479 1.5084 0.0003  -0.4309 -0.1007 166 ILE   W CG2 
40673 C  CD1 . ILE   W  167 ? 1.5300 0.7046 1.5198 -0.0080 -0.4090 -0.0876 166 ILE   W CD1 
40674 N  N   . SER   W  168 ? 1.6113 0.7256 1.4901 0.0393  -0.4853 -0.0519 167 SER   W N   
40675 C  CA  . SER   W  168 ? 1.6257 0.7818 1.4750 0.0604  -0.4595 -0.0594 167 SER   W CA  
40676 C  C   . SER   W  168 ? 1.6889 0.7895 1.5522 0.0531  -0.4381 -0.0809 167 SER   W C   
40677 O  O   . SER   W  168 ? 1.6967 0.7953 1.5944 0.0688  -0.3866 -0.0794 167 SER   W O   
40678 C  CB  . SER   W  168 ? 1.6278 0.8128 1.4540 0.1028  -0.4582 -0.0510 167 SER   W CB  
40679 O  OG  . SER   W  168 ? 1.5968 0.8135 1.3799 0.1712  -0.4591 -0.0651 167 SER   W OG  
40680 N  N   . GLN   W  169 ? 1.6690 0.8139 1.5842 0.0480  -0.4427 -0.0938 168 GLN   W N   
40681 C  CA  . GLN   W  169 ? 1.6862 0.8137 1.5563 -0.0081 -0.4821 -0.0851 168 GLN   W CA  
40682 C  C   . GLN   W  169 ? 1.6659 0.7772 1.4917 0.0440  -0.4553 -0.0573 168 GLN   W C   
40683 O  O   . GLN   W  169 ? 1.6194 0.8800 1.4487 -0.0294 -0.4828 -0.0698 168 GLN   W O   
40684 C  CB  . GLN   W  169 ? 1.6648 0.8067 1.5577 -0.0370 -0.5105 -0.0904 168 GLN   W CB  
40685 C  CG  . GLN   W  169 ? 1.7121 0.7761 1.5646 -0.0763 -0.5469 -0.0828 168 GLN   W CG  
40686 C  CD  . GLN   W  169 ? 1.7288 0.8102 1.5311 -0.0465 -0.5836 -0.0422 168 GLN   W CD  
40687 O  OE1 . GLN   W  169 ? 1.7233 0.8297 1.5433 -0.0618 -0.6125 -0.0369 168 GLN   W OE1 
40688 N  NE2 . GLN   W  169 ? 1.7024 0.6699 1.5552 -0.1005 -0.6005 -0.0872 168 GLN   W NE2 
40689 N  N   . ALA   W  170 ? 1.5993 0.7236 1.4755 0.0242  -0.4449 -0.0842 169 ALA   W N   
40690 C  CA  . ALA   W  170 ? 1.5870 0.6797 1.4682 0.0474  -0.4308 -0.0615 169 ALA   W CA  
40691 C  C   . ALA   W  170 ? 1.6096 0.6489 1.4698 0.0735  -0.4058 -0.0370 169 ALA   W C   
40692 O  O   . ALA   W  170 ? 1.5866 0.6562 1.5039 0.0584  -0.3897 -0.0170 169 ALA   W O   
40693 C  CB  . ALA   W  170 ? 1.5516 0.7091 1.4456 0.0361  -0.4138 -0.0567 169 ALA   W CB  
40694 N  N   . LEU   W  171 ? 1.6800 0.6759 1.4412 0.1104  -0.4114 -0.0214 170 LEU   W N   
40695 C  CA  . LEU   W  171 ? 1.6936 0.6683 1.3989 0.1210  -0.4161 0.0355  170 LEU   W CA  
40696 C  C   . LEU   W  171 ? 1.7220 0.5616 1.4272 0.1614  -0.4733 -0.0001 170 LEU   W C   
40697 O  O   . LEU   W  171 ? 1.7686 0.3956 1.4081 0.1701  -0.4766 -0.0512 170 LEU   W O   
40698 C  CB  . LEU   W  171 ? 1.7017 0.7015 1.3194 0.1268  -0.4331 0.0400  170 LEU   W CB  
40699 C  CG  . LEU   W  171 ? 1.6934 0.6799 1.2683 0.1359  -0.4559 0.0501  170 LEU   W CG  
40700 C  CD1 . LEU   W  171 ? 1.6781 0.6751 1.2591 0.1180  -0.4650 0.0407  170 LEU   W CD1 
40701 C  CD2 . LEU   W  171 ? 1.7211 0.7704 1.2454 0.1238  -0.4536 0.0395  170 LEU   W CD2 
40702 N  N   . LEU   W  172 ? 1.7295 0.5684 1.4950 0.2043  -0.4913 0.0216  171 LEU   W N   
40703 C  CA  . LEU   W  172 ? 1.7349 0.6470 1.4892 0.1835  -0.4995 0.0531  171 LEU   W CA  
40704 C  C   . LEU   W  172 ? 1.7424 0.6432 1.5305 0.1471  -0.4543 0.0516  171 LEU   W C   
40705 O  O   . LEU   W  172 ? 1.7947 0.5625 1.5911 0.1637  -0.4096 0.1001  171 LEU   W O   
40706 C  CB  . LEU   W  172 ? 1.7638 0.6868 1.4804 0.2029  -0.5233 0.0381  171 LEU   W CB  
40707 C  CG  . LEU   W  172 ? 1.7075 0.5982 1.4778 0.2192  -0.5833 0.0479  171 LEU   W CG  
40708 C  CD1 . LEU   W  172 ? 1.7238 0.5888 1.4614 0.2061  -0.5567 -0.0089 171 LEU   W CD1 
40709 C  CD2 . LEU   W  172 ? 1.7195 0.5754 1.4717 0.2195  -0.6190 0.0553  171 LEU   W CD2 
40710 N  N   . ASN   W  173 ? 1.7119 0.6792 1.5458 0.1309  -0.4405 0.0595  172 ASN   W N   
40711 C  CA  . ASN   W  173 ? 1.6450 0.6942 1.5015 0.1163  -0.4497 0.0622  172 ASN   W CA  
40712 C  C   . ASN   W  173 ? 1.6744 0.6767 1.4705 0.0957  -0.4683 0.0658  172 ASN   W C   
40713 O  O   . ASN   W  173 ? 1.6156 0.7571 1.4996 0.0441  -0.5418 0.1090  172 ASN   W O   
40714 C  CB  . ASN   W  173 ? 1.6161 0.7539 1.5116 0.1387  -0.4584 0.0815  172 ASN   W CB  
40715 C  CG  . ASN   W  173 ? 1.5764 0.7773 1.5303 0.1871  -0.4284 0.0943  172 ASN   W CG  
40716 O  OD1 . ASN   W  173 ? 1.5225 0.8212 1.5195 0.2906  -0.4280 0.1207  172 ASN   W OD1 
40717 N  ND2 . ASN   W  173 ? 1.5897 0.7640 1.5375 0.1888  -0.4398 0.0944  172 ASN   W ND2 
40718 N  N   . ALA   W  174 ? 1.6374 0.6370 1.4287 0.0469  -0.4827 0.0377  173 ALA   W N   
40719 C  CA  . ALA   W  174 ? 1.6144 0.7103 1.4521 -0.0085 -0.4773 0.0067  173 ALA   W CA  
40720 C  C   . ALA   W  174 ? 1.7175 0.7356 1.4380 -0.0215 -0.4209 0.0376  173 ALA   W C   
40721 O  O   . ALA   W  174 ? 1.7911 0.7127 1.4923 -0.0592 -0.3985 0.0076  173 ALA   W O   
40722 C  CB  . ALA   W  174 ? 1.6143 0.7369 1.4524 -0.0284 -0.4671 0.0250  173 ALA   W CB  
40723 N  N   . ALA   W  175 ? 1.6746 0.7994 1.4010 -0.0385 -0.4479 0.0549  174 ALA   W N   
40724 C  CA  . ALA   W  175 ? 1.6711 0.7911 1.4111 0.0119  -0.4502 0.0734  174 ALA   W CA  
40725 C  C   . ALA   W  175 ? 1.6955 0.7562 1.4359 0.0801  -0.4799 0.0866  174 ALA   W C   
40726 O  O   . ALA   W  175 ? 1.6898 0.4812 1.4330 0.1292  -0.4712 0.0866  174 ALA   W O   
40727 C  CB  . ALA   W  175 ? 1.6519 0.8059 1.3921 0.0036  -0.4618 0.0854  174 ALA   W CB  
40728 N  N   . ASP   W  176 ? 1.6797 0.8246 1.4421 0.0952  -0.5063 0.1150  175 ASP   W N   
40729 C  CA  . ASP   W  176 ? 1.7102 0.8836 1.4653 0.0321  -0.4559 0.1529  175 ASP   W CA  
40730 C  C   . ASP   W  176 ? 1.7333 0.8307 1.4895 0.0336  -0.4240 0.1402  175 ASP   W C   
40731 O  O   . ASP   W  176 ? 1.8128 0.7956 1.5964 0.0346  -0.3472 0.1098  175 ASP   W O   
40732 C  CB  . ASP   W  176 ? 1.7099 1.0295 1.5136 0.0429  -0.4770 0.1616  175 ASP   W CB  
40733 C  CG  . ASP   W  176 ? 1.7266 1.0907 1.4944 0.0324  -0.4934 0.1766  175 ASP   W CG  
40734 O  OD1 . ASP   W  176 ? 1.6804 1.0018 1.4439 -0.0449 -0.5008 0.1551  175 ASP   W OD1 
40735 O  OD2 . ASP   W  176 ? 1.7474 1.2366 1.5745 0.0070  -0.5294 0.2819  175 ASP   W OD2 
40736 N  N   . ARG   W  177 ? 1.7296 0.8179 1.5121 0.0849  -0.4221 0.1788  176 ARG   W N   
40737 C  CA  . ARG   W  177 ? 1.7392 0.8368 1.4999 0.1231  -0.4453 0.1773  176 ARG   W CA  
40738 C  C   . ARG   W  177 ? 1.7443 0.7399 1.5750 0.1419  -0.3640 0.2234  176 ARG   W C   
40739 O  O   . ARG   W  177 ? 1.7418 0.7182 1.6100 0.1564  -0.3977 0.2738  176 ARG   W O   
40740 C  CB  . ARG   W  177 ? 1.7339 0.8815 1.4785 0.1746  -0.4701 0.1596  176 ARG   W CB  
40741 C  CG  . ARG   W  177 ? 1.7411 0.9552 1.4605 0.2195  -0.5054 0.1545  176 ARG   W CG  
40742 C  CD  . ARG   W  177 ? 1.7544 0.9564 1.4825 0.2183  -0.5188 0.1340  176 ARG   W CD  
40743 N  NE  . ARG   W  177 ? 1.7588 0.9852 1.5373 0.2470  -0.5190 0.0851  176 ARG   W NE  
40744 C  CZ  . ARG   W  177 ? 1.8157 1.0037 1.5796 0.2023  -0.5353 0.0293  176 ARG   W CZ  
40745 N  NH1 . ARG   W  177 ? 1.8029 1.0397 1.5804 0.2199  -0.5499 0.0200  176 ARG   W NH1 
40746 N  NH2 . ARG   W  177 ? 1.8325 1.0827 1.6186 0.2425  -0.5483 0.0285  176 ARG   W NH2 
40747 N  N   . ASP   W  178 ? 1.7592 0.6511 1.5680 0.0679  -0.3721 0.2313  177 ASP   W N   
40748 C  CA  . ASP   W  178 ? 1.7577 0.5946 1.5818 0.0578  -0.3252 0.1886  177 ASP   W CA  
40749 C  C   . ASP   W  178 ? 1.7638 0.4795 1.5671 0.0069  -0.3305 0.2066  177 ASP   W C   
40750 O  O   . ASP   W  178 ? 1.7892 0.2694 1.5654 -0.0123 -0.2550 0.1569  177 ASP   W O   
40751 C  CB  . ASP   W  178 ? 1.7920 0.5353 1.6927 0.0284  -0.3345 0.1117  177 ASP   W CB  
40752 C  CG  . ASP   W  178 ? 1.7862 0.6223 1.7865 0.0503  -0.3309 0.0758  177 ASP   W CG  
40753 O  OD1 . ASP   W  178 ? 1.7644 0.5896 1.9414 0.0514  -0.2930 0.1231  177 ASP   W OD1 
40754 O  OD2 . ASP   W  178 ? 1.7253 0.6250 1.7258 0.0516  -0.4136 -0.0388 177 ASP   W OD2 
40755 N  N   . ALA   W  179 ? 1.7584 0.5376 1.5252 -0.0071 -0.3056 0.2173  178 ALA   W N   
40756 C  CA  . ALA   W  179 ? 1.7513 0.5748 1.5122 -0.0130 -0.3017 0.1500  178 ALA   W CA  
40757 C  C   . ALA   W  179 ? 1.7073 0.5867 1.3986 -0.0685 -0.3206 0.1069  178 ALA   W C   
40758 O  O   . ALA   W  179 ? 1.7439 0.4634 1.4093 -0.0740 -0.3015 0.0397  178 ALA   W O   
40759 C  CB  . ALA   W  179 ? 1.7373 0.6347 1.5531 -0.0243 -0.3048 0.1745  178 ALA   W CB  
40760 N  N   . LEU   W  180 ? 1.6711 0.6404 1.3795 -0.0815 -0.3541 0.1200  179 LEU   W N   
40761 C  CA  . LEU   W  180 ? 1.6437 0.7250 1.4243 -0.0024 -0.3440 0.1384  179 LEU   W CA  
40762 C  C   . LEU   W  180 ? 1.6001 0.8088 1.4570 -0.0150 -0.3324 0.1261  179 LEU   W C   
40763 O  O   . LEU   W  180 ? 1.6135 0.8423 1.4629 -0.0028 -0.3350 0.0940  179 LEU   W O   
40764 C  CB  . LEU   W  180 ? 1.6271 0.7780 1.4637 -0.0455 -0.3822 0.1596  179 LEU   W CB  
40765 C  CG  . LEU   W  180 ? 1.6237 0.7840 1.5552 -0.0697 -0.3739 0.2236  179 LEU   W CG  
40766 C  CD1 . LEU   W  180 ? 1.6432 0.8702 1.6175 -0.0398 -0.3843 0.2519  179 LEU   W CD1 
40767 C  CD2 . LEU   W  180 ? 1.6522 0.7459 1.5374 -0.0654 -0.3980 0.2709  179 LEU   W CD2 
40768 N  N   . SER   W  181 ? 1.5933 0.8935 1.4581 -0.0157 -0.3422 0.1102  180 SER   W N   
40769 C  CA  . SER   W  181 ? 1.6586 0.8437 1.3730 -0.0039 -0.4057 0.0521  180 SER   W CA  
40770 C  C   . SER   W  181 ? 1.6733 0.8615 1.3380 0.0000  -0.4094 0.0299  180 SER   W C   
40771 O  O   . SER   W  181 ? 1.6508 0.9415 1.1965 -0.0919 -0.4537 0.1119  180 SER   W O   
40772 C  CB  . SER   W  181 ? 1.6716 0.8746 1.4305 -0.0525 -0.3698 0.0235  180 SER   W CB  
40773 O  OG  . SER   W  181 ? 1.6858 0.8598 1.4933 -0.0383 -0.3683 0.0648  180 SER   W OG  
40774 N  N   . GLY   W  182 ? 1.7048 0.7067 1.3444 0.0667  -0.4165 0.0579  181 GLY   W N   
40775 C  CA  . GLY   W  182 ? 1.6956 0.7194 1.3715 0.1072  -0.4191 0.0382  181 GLY   W CA  
40776 C  C   . GLY   W  182 ? 1.6845 0.7397 1.4197 0.1085  -0.3951 -0.0026 181 GLY   W C   
40777 O  O   . GLY   W  182 ? 1.6755 0.7866 1.3621 0.1787  -0.3998 -0.0169 181 GLY   W O   
40778 N  N   . TRP   W  183 ? 1.6491 0.7064 1.4234 0.1065  -0.3648 -0.0135 182 TRP   W N   
40779 C  CA  . TRP   W  183 ? 1.6642 0.7441 1.4315 0.1451  -0.3510 -0.0117 182 TRP   W CA  
40780 C  C   . TRP   W  183 ? 1.6275 0.8239 1.4485 0.1434  -0.3720 -0.0440 182 TRP   W C   
40781 O  O   . TRP   W  183 ? 1.5614 0.9725 1.4867 0.2306  -0.2924 -0.0248 182 TRP   W O   
40782 C  CB  . TRP   W  183 ? 1.6525 0.6918 1.4008 0.0975  -0.3269 -0.0422 182 TRP   W CB  
40783 C  CG  . TRP   W  183 ? 1.7139 0.7236 1.3517 0.0841  -0.3270 -0.0257 182 TRP   W CG  
40784 C  CD1 . TRP   W  183 ? 1.7118 0.7612 1.3255 0.1076  -0.3622 0.0448  182 TRP   W CD1 
40785 C  CD2 . TRP   W  183 ? 1.7517 0.6980 1.2932 0.0654  -0.3080 -0.0419 182 TRP   W CD2 
40786 N  NE1 . TRP   W  183 ? 1.7291 0.8470 1.2744 0.1103  -0.3487 0.0433  182 TRP   W NE1 
40787 C  CE2 . TRP   W  183 ? 1.7601 0.7617 1.2613 0.0692  -0.3149 0.0174  182 TRP   W CE2 
40788 C  CE3 . TRP   W  183 ? 1.7310 0.7103 1.2735 0.0577  -0.2989 -0.0459 182 TRP   W CE3 
40789 C  CZ2 . TRP   W  183 ? 1.7649 0.7859 1.2645 0.0834  -0.3011 -0.0105 182 TRP   W CZ2 
40790 C  CZ3 . TRP   W  183 ? 1.7557 0.7247 1.2637 0.0319  -0.2910 -0.0155 182 TRP   W CZ3 
40791 C  CH2 . TRP   W  183 ? 1.7755 0.7226 1.2692 0.0401  -0.2866 -0.0093 182 TRP   W CH2 
40792 N  N   . GLY   W  184 ? 1.6349 0.8984 1.4736 0.1218  -0.3739 -0.0228 183 GLY   W N   
40793 C  CA  . GLY   W  184 ? 1.7229 0.8879 1.4878 0.1080  -0.4197 -0.0635 183 GLY   W CA  
40794 C  C   . GLY   W  184 ? 1.7183 0.7971 1.5172 0.0401  -0.4145 -0.0918 183 GLY   W C   
40795 O  O   . GLY   W  184 ? 1.7587 0.8329 1.5265 0.0483  -0.4316 -0.0657 183 GLY   W O   
40796 N  N   . ALA   W  185 ? 1.7311 0.7868 1.4577 0.0370  -0.4738 -0.1292 184 ALA   W N   
40797 C  CA  . ALA   W  185 ? 1.7111 0.7310 1.4317 0.0294  -0.5101 -0.1420 184 ALA   W CA  
40798 C  C   . ALA   W  185 ? 1.7440 0.6838 1.4078 0.0562  -0.5147 -0.1285 184 ALA   W C   
40799 O  O   . ALA   W  185 ? 1.7254 0.6495 1.4533 0.0866  -0.5476 -0.2384 184 ALA   W O   
40800 C  CB  . ALA   W  185 ? 1.7080 0.7087 1.4327 0.0269  -0.5141 -0.1390 184 ALA   W CB  
40801 N  N   . VAL   W  186 ? 1.7258 0.6873 1.3433 0.0512  -0.5224 -0.1467 185 VAL   W N   
40802 C  CA  . VAL   W  186 ? 1.7243 0.6852 1.3107 0.0360  -0.5208 -0.0906 185 VAL   W CA  
40803 C  C   . VAL   W  186 ? 1.6642 0.5500 1.3663 -0.0021 -0.5056 -0.0795 185 VAL   W C   
40804 O  O   . VAL   W  186 ? 1.6701 0.3859 1.3457 -0.0142 -0.4764 -0.0203 185 VAL   W O   
40805 C  CB  . VAL   W  186 ? 1.7324 0.6755 1.3384 0.0550  -0.5330 -0.0386 185 VAL   W CB  
40806 C  CG1 . VAL   W  186 ? 1.7241 0.6800 1.3473 0.0519  -0.5439 -0.0135 185 VAL   W CG1 
40807 C  CG2 . VAL   W  186 ? 1.7591 0.7624 1.3613 0.0688  -0.5129 -0.0227 185 VAL   W CG2 
40808 N  N   . VAL   W  187 ? 1.6572 0.5912 1.3282 0.0114  -0.5683 -0.0869 186 VAL   W N   
40809 C  CA  . VAL   W  187 ? 1.5982 0.7130 1.3681 0.0163  -0.5579 -0.0986 186 VAL   W CA  
40810 C  C   . VAL   W  187 ? 1.6213 0.7492 1.3926 0.0052  -0.5761 -0.1672 186 VAL   W C   
40811 O  O   . VAL   W  187 ? 1.6717 0.7505 1.4064 0.0742  -0.5907 -0.2191 186 VAL   W O   
40812 C  CB  . VAL   W  187 ? 1.6044 0.7149 1.4129 0.0245  -0.5712 -0.0986 186 VAL   W CB  
40813 C  CG1 . VAL   W  187 ? 1.5989 0.7287 1.4422 0.0247  -0.5477 -0.1088 186 VAL   W CG1 
40814 C  CG2 . VAL   W  187 ? 1.5962 0.7351 1.4203 -0.0038 -0.5759 -0.0893 186 VAL   W CG2 
40815 N  N   . TYR   W  188 ? 1.5939 0.7552 1.4091 -0.0301 -0.5363 -0.1461 187 TYR   W N   
40816 C  CA  . TYR   W  188 ? 1.5974 0.8010 1.4354 -0.0862 -0.5146 -0.1481 187 TYR   W CA  
40817 C  C   . TYR   W  188 ? 1.5759 0.8186 1.5397 -0.0776 -0.4933 -0.1748 187 TYR   W C   
40818 O  O   . TYR   W  188 ? 1.5281 0.7128 1.5522 -0.0844 -0.4668 -0.1915 187 TYR   W O   
40819 C  CB  . TYR   W  188 ? 1.5592 0.8771 1.3542 -0.0887 -0.4853 -0.1171 187 TYR   W CB  
40820 C  CG  . TYR   W  188 ? 1.6142 0.8889 1.2554 -0.1138 -0.4799 -0.1097 187 TYR   W CG  
40821 C  CD1 . TYR   W  188 ? 1.6200 0.8976 1.1744 -0.1177 -0.4389 -0.0928 187 TYR   W CD1 
40822 C  CD2 . TYR   W  188 ? 1.6033 0.8939 1.2074 -0.1099 -0.4781 -0.0998 187 TYR   W CD2 
40823 C  CE1 . TYR   W  188 ? 1.6272 0.9085 1.1354 -0.1012 -0.4433 -0.0669 187 TYR   W CE1 
40824 C  CE2 . TYR   W  188 ? 1.6298 0.9064 1.1500 -0.1017 -0.4830 -0.0908 187 TYR   W CE2 
40825 C  CZ  . TYR   W  188 ? 1.5928 0.9338 1.1168 -0.0781 -0.4341 -0.0757 187 TYR   W CZ  
40826 O  OH  . TYR   W  188 ? 1.6096 1.0949 1.1232 -0.0212 -0.4221 -0.0350 187 TYR   W OH  
40827 N  N   . ILE   W  189 ? 1.6348 0.8996 1.6250 -0.0688 -0.5785 -0.2123 188 ILE   W N   
40828 C  CA  . ILE   W  189 ? 1.6374 0.8051 1.6931 -0.0804 -0.5885 -0.1982 188 ILE   W CA  
40829 C  C   . ILE   W  189 ? 1.6741 0.7934 1.6801 -0.0705 -0.5898 -0.2169 188 ILE   W C   
40830 O  O   . ILE   W  189 ? 1.7193 0.5310 1.7354 0.0022  -0.5374 -0.1857 188 ILE   W O   
40831 C  CB  . ILE   W  189 ? 1.7060 0.9065 1.7820 -0.0430 -0.6552 -0.1854 188 ILE   W CB  
40832 C  CG1 . ILE   W  189 ? 1.6933 0.9077 1.7307 -0.0646 -0.6733 -0.1758 188 ILE   W CG1 
40833 C  CG2 . ILE   W  189 ? 1.7211 0.9847 1.8486 -0.0554 -0.6314 -0.1775 188 ILE   W CG2 
40834 C  CD1 . ILE   W  189 ? 1.6641 0.9041 1.7266 -0.0775 -0.6459 -0.1760 188 ILE   W CD1 
40835 N  N   . ILE   W  190 ? 1.6671 0.6069 1.7201 -0.1208 -0.5720 -0.2165 189 ILE   W N   
40836 C  CA  . ILE   W  190 ? 1.6961 0.6173 1.7315 -0.0906 -0.5605 -0.1945 189 ILE   W CA  
40837 C  C   . ILE   W  190 ? 1.7579 0.6644 1.7701 -0.0967 -0.5271 -0.1353 189 ILE   W C   
40838 O  O   . ILE   W  190 ? 1.8209 0.5193 1.7202 -0.0634 -0.5764 -0.0765 189 ILE   W O   
40839 C  CB  . ILE   W  190 ? 1.6555 0.5232 1.6773 -0.0972 -0.5200 -0.2092 189 ILE   W CB  
40840 C  CG1 . ILE   W  190 ? 1.6692 0.4314 1.6500 -0.0733 -0.5082 -0.2173 189 ILE   W CG1 
40841 C  CG2 . ILE   W  190 ? 1.6524 0.5310 1.7179 -0.0839 -0.4924 -0.1929 189 ILE   W CG2 
40842 C  CD1 . ILE   W  190 ? 1.6514 0.4089 1.6279 -0.0473 -0.4873 -0.1881 189 ILE   W CD1 
40843 N  N   . LYS   W  191 ? 1.8059 0.7729 1.8410 -0.1545 -0.5609 -0.1639 190 LYS   W N   
40844 C  CA  . LYS   W  191 ? 1.7824 0.8863 1.9074 -0.1945 -0.5417 -0.2205 190 LYS   W CA  
40845 C  C   . LYS   W  191 ? 1.8553 0.8732 1.9910 -0.1869 -0.5254 -0.2860 190 LYS   W C   
40846 O  O   . LYS   W  191 ? 1.7638 0.8415 1.8988 -0.2987 -0.5860 -0.3638 190 LYS   W O   
40847 C  CB  . LYS   W  191 ? 1.7586 0.9312 1.9451 -0.1498 -0.5378 -0.2280 190 LYS   W CB  
40848 C  CG  . LYS   W  191 ? 1.6973 0.9645 1.9303 -0.0956 -0.5434 -0.2289 190 LYS   W CG  
40849 C  CD  . LYS   W  191 ? 1.7198 1.0430 1.9548 -0.0609 -0.5639 -0.2417 190 LYS   W CD  
40850 C  CE  . LYS   W  191 ? 1.7303 1.1020 1.9972 -0.0679 -0.5503 -0.2331 190 LYS   W CE  
40851 N  NZ  . LYS   W  191 ? 1.7962 1.1776 2.0075 -0.0527 -0.5853 -0.2463 190 LYS   W NZ  
40852 N  N   . LYS   W  192 ? 1.9421 1.0185 2.1330 -0.2051 -0.4117 -0.2383 191 LYS   W N   
40853 C  CA  . LYS   W  192 ? 2.0379 1.0477 2.2214 -0.1317 -0.3878 -0.2266 191 LYS   W CA  
40854 C  C   . LYS   W  192 ? 2.0618 0.9764 2.2412 -0.1579 -0.4681 -0.2878 191 LYS   W C   
40855 O  O   . LYS   W  192 ? 2.0694 0.8058 2.3814 -0.1804 -0.4696 -0.4212 191 LYS   W O   
40856 C  CB  . LYS   W  192 ? 2.0776 1.1273 2.2849 -0.1180 -0.3191 -0.1748 191 LYS   W CB  
40857 C  CG  . LYS   W  192 ? 2.0946 1.2277 2.2540 -0.0828 -0.2641 -0.1134 191 LYS   W CG  
40858 C  CD  . LYS   W  192 ? 2.0668 1.2909 2.3066 -0.0955 -0.2911 -0.1152 191 LYS   W CD  
40859 C  CE  . LYS   W  192 ? 2.0188 1.4350 2.3196 0.0085  -0.2870 -0.0496 191 LYS   W CE  
40860 N  NZ  . LYS   W  192 ? 2.0056 1.4615 2.2604 0.0421  -0.2783 -0.0146 191 LYS   W NZ  
40861 N  N   . ASP   W  193 ? 2.1013 0.9641 2.2197 -0.2022 -0.4943 -0.3385 192 ASP   W N   
40862 C  CA  . ASP   W  193 ? 2.0850 1.1308 2.1207 -0.1590 -0.5312 -0.3125 192 ASP   W CA  
40863 C  C   . ASP   W  193 ? 1.9889 1.0471 2.0623 -0.1583 -0.5610 -0.3864 192 ASP   W C   
40864 O  O   . ASP   W  193 ? 1.9678 1.1296 1.9930 -0.0946 -0.5705 -0.3622 192 ASP   W O   
40865 C  CB  . ASP   W  193 ? 2.1286 1.2020 2.2327 -0.2345 -0.5469 -0.2545 192 ASP   W CB  
40866 C  CG  . ASP   W  193 ? 2.1193 1.4155 2.3680 -0.1730 -0.5418 -0.1962 192 ASP   W CG  
40867 O  OD1 . ASP   W  193 ? 2.1080 1.4495 2.4027 -0.1660 -0.5934 -0.1090 192 ASP   W OD1 
40868 O  OD2 . ASP   W  193 ? 2.2726 1.5463 2.4880 -0.2309 -0.5184 -0.0902 192 ASP   W OD2 
40869 N  N   . GLU   W  194 ? 1.8841 1.0371 2.0373 -0.1277 -0.5748 -0.3603 193 GLU   W N   
40870 C  CA  . GLU   W  194 ? 1.8478 1.0493 2.0361 -0.0556 -0.5947 -0.3260 193 GLU   W CA  
40871 C  C   . GLU   W  194 ? 1.7849 0.9107 2.0332 -0.0181 -0.5249 -0.2076 193 GLU   W C   
40872 O  O   . GLU   W  194 ? 1.8505 0.7798 2.0681 0.0171  -0.4625 -0.1708 193 GLU   W O   
40873 C  CB  . GLU   W  194 ? 1.8705 1.1987 2.0732 -0.0789 -0.6547 -0.3572 193 GLU   W CB  
40874 C  CG  . GLU   W  194 ? 1.8786 1.2591 2.1555 -0.0449 -0.6204 -0.3808 193 GLU   W CG  
40875 C  CD  . GLU   W  194 ? 1.9569 1.4602 2.1861 -0.0362 -0.6626 -0.3548 193 GLU   W CD  
40876 O  OE1 . GLU   W  194 ? 2.0502 1.5493 2.2345 -0.0379 -0.5928 -0.4712 193 GLU   W OE1 
40877 O  OE2 . GLU   W  194 ? 2.0208 1.6130 2.4068 -0.0070 -0.5348 -0.3808 193 GLU   W OE2 
40878 N  N   . VAL   W  195 ? 1.7428 0.8324 1.9942 0.0131  -0.5576 -0.1911 194 VAL   W N   
40879 C  CA  . VAL   W  195 ? 1.7043 0.8652 1.8873 0.0049  -0.5793 -0.1955 194 VAL   W CA  
40880 C  C   . VAL   W  195 ? 1.6789 0.9595 1.8305 -0.0339 -0.6184 -0.1981 194 VAL   W C   
40881 O  O   . VAL   W  195 ? 1.7317 0.9310 1.8370 -0.0051 -0.6078 -0.1948 194 VAL   W O   
40882 C  CB  . VAL   W  195 ? 1.7043 0.7705 1.8701 -0.0021 -0.5706 -0.2184 194 VAL   W CB  
40883 C  CG1 . VAL   W  195 ? 1.7061 0.8005 1.8807 -0.0316 -0.5343 -0.1693 194 VAL   W CG1 
40884 C  CG2 . VAL   W  195 ? 1.6730 0.7323 1.8419 -0.0529 -0.5628 -0.2471 194 VAL   W CG2 
40885 N  N   . VAL   W  196 ? 1.6233 0.9613 1.7726 -0.0154 -0.6341 -0.1550 195 VAL   W N   
40886 C  CA  . VAL   W  196 ? 1.6009 1.0336 1.7379 0.0241  -0.6483 -0.1335 195 VAL   W CA  
40887 C  C   . VAL   W  196 ? 1.5913 1.0194 1.6701 0.0223  -0.6125 -0.0883 195 VAL   W C   
40888 O  O   . VAL   W  196 ? 1.5642 1.0769 1.6222 0.0308  -0.5668 -0.0575 195 VAL   W O   
40889 C  CB  . VAL   W  196 ? 1.5865 1.0857 1.7853 0.0234  -0.6705 -0.1245 195 VAL   W CB  
40890 C  CG1 . VAL   W  196 ? 1.5962 1.1457 1.7602 0.0159  -0.6532 -0.1227 195 VAL   W CG1 
40891 C  CG2 . VAL   W  196 ? 1.5934 1.0699 1.8502 0.0276  -0.6894 -0.1136 195 VAL   W CG2 
40892 N  N   . LYS   W  197 ? 1.6267 0.9927 1.6083 0.0110  -0.6306 -0.1175 196 LYS   W N   
40893 C  CA  . LYS   W  197 ? 1.6592 0.9520 1.6140 0.0004  -0.6166 -0.1325 196 LYS   W CA  
40894 C  C   . LYS   W  197 ? 1.6653 0.9711 1.5661 -0.0322 -0.6613 -0.1364 196 LYS   W C   
40895 O  O   . LYS   W  197 ? 1.6535 0.8961 1.6154 -0.1085 -0.7433 -0.1935 196 LYS   W O   
40896 C  CB  . LYS   W  197 ? 1.6765 0.9361 1.6628 -0.0113 -0.5827 -0.1580 196 LYS   W CB  
40897 C  CG  . LYS   W  197 ? 1.6743 0.9355 1.6918 -0.0007 -0.5101 -0.1500 196 LYS   W CG  
40898 C  CD  . LYS   W  197 ? 1.7378 0.9515 1.7291 0.0123  -0.4549 -0.1557 196 LYS   W CD  
40899 C  CE  . LYS   W  197 ? 1.7459 0.9514 1.7256 0.0265  -0.3930 -0.1179 196 LYS   W CE  
40900 N  NZ  . LYS   W  197 ? 1.7870 0.9478 1.7388 0.0581  -0.3781 -0.0928 196 LYS   W NZ  
40901 N  N   . ARG   W  198 ? 1.6499 0.9378 1.5515 0.0046  -0.6389 -0.0974 197 ARG   W N   
40902 C  CA  . ARG   W  198 ? 1.6766 0.9745 1.5455 0.0452  -0.6582 -0.0779 197 ARG   W CA  
40903 C  C   . ARG   W  198 ? 1.6686 0.9070 1.5462 0.0789  -0.6199 -0.0804 197 ARG   W C   
40904 O  O   . ARG   W  198 ? 1.6646 0.8555 1.5181 0.0976  -0.5916 -0.0474 197 ARG   W O   
40905 C  CB  . ARG   W  198 ? 1.6522 1.0082 1.5416 0.0394  -0.6518 -0.0205 197 ARG   W CB  
40906 C  CG  . ARG   W  198 ? 1.7161 1.1122 1.5655 -0.0373 -0.6621 0.0116  197 ARG   W CG  
40907 C  CD  . ARG   W  198 ? 1.7043 1.1851 1.5717 -0.0319 -0.6709 0.0495  197 ARG   W CD  
40908 N  NE  . ARG   W  198 ? 1.6978 1.3138 1.5293 -0.0713 -0.7303 0.0802  197 ARG   W NE  
40909 C  CZ  . ARG   W  198 ? 1.6872 1.3456 1.5712 -0.0983 -0.7411 0.1282  197 ARG   W CZ  
40910 N  NH1 . ARG   W  198 ? 1.7325 1.3872 1.5123 -0.0883 -0.6989 0.1741  197 ARG   W NH1 
40911 N  NH2 . ARG   W  198 ? 1.6821 1.3504 1.5010 -0.0925 -0.8122 0.1466  197 ARG   W NH2 
40912 N  N   . TYR   W  199 ? 1.7021 1.0059 1.4539 0.1456  -0.6745 -0.0877 198 TYR   W N   
40913 C  CA  . TYR   W  199 ? 1.7185 1.0363 1.4566 0.1278  -0.6842 -0.0894 198 TYR   W CA  
40914 C  C   . TYR   W  199 ? 1.7466 0.9893 1.3925 0.0961  -0.7280 -0.0867 198 TYR   W C   
40915 O  O   . TYR   W  199 ? 1.6929 1.0338 1.4633 0.0802  -0.7273 -0.0846 198 TYR   W O   
40916 C  CB  . TYR   W  199 ? 1.7256 1.1210 1.4691 0.1839  -0.6856 -0.1024 198 TYR   W CB  
40917 C  CG  . TYR   W  199 ? 1.6868 1.1045 1.5405 0.1580  -0.6874 -0.1359 198 TYR   W CG  
40918 C  CD1 . TYR   W  199 ? 1.6874 1.0926 1.5626 0.1770  -0.6912 -0.1599 198 TYR   W CD1 
40919 C  CD2 . TYR   W  199 ? 1.6747 1.1170 1.5550 0.1885  -0.6592 -0.1397 198 TYR   W CD2 
40920 C  CE1 . TYR   W  199 ? 1.6586 1.1135 1.5641 0.1818  -0.6803 -0.1593 198 TYR   W CE1 
40921 C  CE2 . TYR   W  199 ? 1.6902 1.0620 1.5550 0.1617  -0.6407 -0.1614 198 TYR   W CE2 
40922 C  CZ  . TYR   W  199 ? 1.6530 1.0448 1.5702 0.1892  -0.6490 -0.1538 198 TYR   W CZ  
40923 O  OH  . TYR   W  199 ? 1.6682 1.0456 1.6191 0.1922  -0.5994 -0.1473 198 TYR   W OH  
40924 N  N   . LEU   W  200 ? 1.8282 0.8967 1.3978 0.0817  -0.6957 -0.0656 199 LEU   W N   
40925 C  CA  . LEU   W  200 ? 1.8562 0.8578 1.4445 0.0526  -0.6923 -0.0759 199 LEU   W CA  
40926 C  C   . LEU   W  200 ? 1.9479 0.8188 1.3836 0.0515  -0.7272 -0.0875 199 LEU   W C   
40927 O  O   . LEU   W  200 ? 1.9296 0.8118 1.3067 0.0463  -0.8150 -0.1274 199 LEU   W O   
40928 C  CB  . LEU   W  200 ? 1.8270 0.7575 1.4630 0.0252  -0.6252 -0.1012 199 LEU   W CB  
40929 C  CG  . LEU   W  200 ? 1.8194 0.7395 1.5427 -0.0061 -0.5904 -0.1093 199 LEU   W CG  
40930 C  CD1 . LEU   W  200 ? 1.7568 0.6651 1.5517 -0.0489 -0.6207 -0.1047 199 LEU   W CD1 
40931 C  CD2 . LEU   W  200 ? 1.8155 0.7884 1.6198 0.0092  -0.6057 -0.1159 199 LEU   W CD2 
40932 N  N   . LYS   W  201 ? 1.9125 0.8817 1.3856 0.0670  -0.7162 -0.0632 200 LYS   W N   
40933 C  CA  . LYS   W  201 ? 1.9219 0.9385 1.4081 0.0764  -0.6952 0.0030  200 LYS   W CA  
40934 C  C   . LYS   W  201 ? 1.8532 0.8661 1.4260 0.0434  -0.6827 0.0401  200 LYS   W C   
40935 O  O   . LYS   W  201 ? 1.8084 0.7947 1.3833 -0.0087 -0.7152 0.0239  200 LYS   W O   
40936 C  CB  . LYS   W  201 ? 1.9477 0.9592 1.4765 0.1076  -0.7111 0.0248  200 LYS   W CB  
40937 C  CG  . LYS   W  201 ? 1.9889 1.0183 1.5543 0.0923  -0.6954 0.0831  200 LYS   W CG  
40938 C  CD  . LYS   W  201 ? 2.0393 1.0991 1.5944 0.1025  -0.7188 0.1476  200 LYS   W CD  
40939 C  CE  . LYS   W  201 ? 2.1002 1.1314 1.6345 0.1068  -0.6760 0.2388  200 LYS   W CE  
40940 N  NZ  . LYS   W  201 ? 2.1209 1.2247 1.6762 0.1297  -0.6810 0.2627  200 LYS   W NZ  
40941 N  N   . MET   W  202 ? 1.8272 0.8875 1.4736 0.0743  -0.6386 0.0667  201 MET   W N   
40942 C  CA  . MET   W  202 ? 1.8057 0.8341 1.5291 0.1053  -0.5901 0.0369  201 MET   W CA  
40943 C  C   . MET   W  202 ? 1.7907 0.8652 1.4817 0.1509  -0.5621 0.0764  201 MET   W C   
40944 O  O   . MET   W  202 ? 1.7555 0.8468 1.3786 0.2113  -0.6241 0.1492  201 MET   W O   
40945 C  CB  . MET   W  202 ? 1.7773 0.7688 1.5897 0.1415  -0.5769 0.0524  201 MET   W CB  
40946 C  CG  . MET   W  202 ? 1.7806 0.6987 1.6259 0.1375  -0.5636 0.0749  201 MET   W CG  
40947 S  SD  . MET   W  202 ? 1.7398 0.5688 1.6772 0.1382  -0.5613 0.0888  201 MET   W SD  
40948 C  CE  . MET   W  202 ? 1.7637 0.6059 1.6770 0.1793  -0.5485 0.0549  201 MET   W CE  
40949 N  N   . ARG   W  203 ? 1.7513 0.8643 1.5637 0.0748  -0.5302 0.0827  202 ARG   W N   
40950 C  CA  . ARG   W  203 ? 1.7760 0.9168 1.5600 0.0564  -0.4945 0.0917  202 ARG   W CA  
40951 C  C   . ARG   W  203 ? 1.7688 0.8357 1.5019 0.0214  -0.4361 0.0488  202 ARG   W C   
40952 O  O   . ARG   W  203 ? 1.8448 0.7063 1.6123 0.0292  -0.4283 0.0509  202 ARG   W O   
40953 C  CB  . ARG   W  203 ? 1.7560 0.9503 1.5533 0.0757  -0.4656 0.0766  202 ARG   W CB  
40954 C  CG  . ARG   W  203 ? 1.7160 1.0281 1.5383 0.0634  -0.4365 0.0682  202 ARG   W CG  
40955 C  CD  . ARG   W  203 ? 1.7044 1.0488 1.5176 0.0455  -0.4373 0.0599  202 ARG   W CD  
40956 N  NE  . ARG   W  203 ? 1.6870 1.0897 1.4851 0.0437  -0.4787 0.1022  202 ARG   W NE  
40957 C  CZ  . ARG   W  203 ? 1.6826 1.1929 1.3981 0.0526  -0.5259 0.1469  202 ARG   W CZ  
40958 N  NH1 . ARG   W  203 ? 1.6797 1.2443 1.3598 0.0421  -0.5507 0.1300  202 ARG   W NH1 
40959 N  NH2 . ARG   W  203 ? 1.7109 1.2551 1.3906 0.0407  -0.5147 0.1883  202 ARG   W NH2 
40960 N  N   . GLN   W  204 ? 1.8351 0.8427 1.3773 0.0291  -0.4808 0.0491  203 GLN   W N   
40961 C  CA  . GLN   W  204 ? 1.8480 0.8904 1.2991 0.0289  -0.4434 0.0466  203 GLN   W CA  
40962 C  C   . GLN   W  204 ? 1.7830 0.9699 1.4469 0.0190  -0.3671 0.0431  203 GLN   W C   
40963 O  O   . GLN   W  204 ? 1.8191 1.0064 1.4238 0.0892  -0.3519 0.0376  203 GLN   W O   
40964 C  CB  . GLN   W  204 ? 1.8872 1.0008 1.2339 0.0191  -0.5126 0.1240  203 GLN   W CB  
40965 C  CG  . GLN   W  204 ? 1.9056 1.1448 1.1583 -0.0269 -0.5342 0.0657  203 GLN   W CG  
40966 C  CD  . GLN   W  204 ? 1.9295 1.1161 1.1198 -0.0576 -0.5123 0.0127  203 GLN   W CD  
40967 O  OE1 . GLN   W  204 ? 1.9527 1.1551 1.0104 -0.1213 -0.4369 -0.1881 203 GLN   W OE1 
40968 N  NE2 . GLN   W  204 ? 1.9352 1.2323 1.1816 -0.0954 -0.4758 -0.0150 203 GLN   W NE2 
40969 N  N   . ASP   W  205 ? 1.7389 1.0384 1.5416 0.0078  -0.3402 -0.0439 204 ASP   W N   
40970 C  CA  . ASP   W  205 ? 1.7184 0.9482 1.6611 0.0282  -0.3165 -0.0311 204 ASP   W CA  
40971 C  C   . ASP   W  205 ? 1.6565 1.0031 1.6542 0.0283  -0.3092 -0.0318 204 ASP   W C   
40972 O  O   . ASP   W  205 ? 1.6449 0.9400 1.6493 0.0163  -0.3121 0.0196  204 ASP   W O   
40973 C  CB  . ASP   W  205 ? 1.7255 0.9301 1.7802 0.0111  -0.3221 -0.0201 204 ASP   W CB  
40974 C  CG  . ASP   W  205 ? 1.7022 0.8494 1.8609 0.0293  -0.3182 -0.0083 204 ASP   W CG  
40975 O  OD1 . ASP   W  205 ? 1.6825 0.6528 1.9759 0.0264  -0.3406 -0.1345 204 ASP   W OD1 
40976 O  OD2 . ASP   W  205 ? 1.7026 0.8665 1.9032 0.1241  -0.3243 0.1073  204 ASP   W OD2 
40977 O  OXT . ASP   W  205 ? 1.6083 1.0011 1.6002 0.0977  -0.2757 -0.0370 204 ASP   W OXT 
40978 N  N   . MET   X  1   ? 2.0207 0.6488 2.0344 -0.2525 -0.4357 -0.0996 1   MET   X N   
40979 C  CA  . MET   X  1   ? 2.0200 0.5181 2.0177 -0.2522 -0.4037 -0.1153 1   MET   X CA  
40980 C  C   . MET   X  1   ? 1.8853 0.5232 2.0242 -0.2616 -0.3953 -0.1943 1   MET   X C   
40981 O  O   . MET   X  1   ? 2.0071 0.3465 2.1578 -0.2110 -0.4112 -0.2023 1   MET   X O   
40982 C  CB  . MET   X  1   ? 2.0891 0.7418 2.0280 -0.3289 -0.3399 -0.0989 1   MET   X CB  
40983 C  CG  . MET   X  1   ? 2.1722 0.9007 2.1583 -0.2041 -0.2659 0.0780  1   MET   X CG  
40984 S  SD  . MET   X  1   ? 2.3691 1.0673 2.1275 -0.3675 -0.2564 0.1211  1   MET   X SD  
40985 C  CE  . MET   X  1   ? 2.4610 0.7323 1.9983 -0.3404 -0.2548 0.2106  1   MET   X CE  
40986 N  N   . ASP   X  2   ? 1.8426 0.4429 1.9551 -0.1331 -0.4544 -0.2060 2   ASP   X N   
40987 C  CA  . ASP   X  2   ? 1.8271 0.5195 1.8771 -0.0800 -0.4631 -0.1894 2   ASP   X CA  
40988 C  C   . ASP   X  2   ? 1.8964 0.5193 1.6699 -0.0525 -0.4602 -0.1454 2   ASP   X C   
40989 O  O   . ASP   X  2   ? 2.0138 0.5823 1.7298 -0.0685 -0.3532 -0.1805 2   ASP   X O   
40990 C  CB  . ASP   X  2   ? 1.7335 0.4297 1.9257 -0.0130 -0.5287 -0.2406 2   ASP   X CB  
40991 C  CG  . ASP   X  2   ? 1.6240 0.3677 2.0339 0.0147  -0.6508 -0.2613 2   ASP   X CG  
40992 O  OD1 . ASP   X  2   ? 1.6554 0.2207 2.0343 0.1037  -0.7367 -0.2500 2   ASP   X OD1 
40993 O  OD2 . ASP   X  2   ? 1.7435 0.2629 2.1154 0.0836  -0.6619 -0.3751 2   ASP   X OD2 
40994 N  N   . ILE   X  3   ? 1.9521 0.4973 1.6524 -0.0340 -0.3927 -0.1021 3   ILE   X N   
40995 C  CA  . ILE   X  3   ? 1.9985 0.4713 1.4973 0.0047  -0.3756 -0.0524 3   ILE   X CA  
40996 C  C   . ILE   X  3   ? 1.9929 0.4395 1.3491 0.0270  -0.3802 0.0077  3   ILE   X C   
40997 O  O   . ILE   X  3   ? 1.9703 0.3277 1.2741 0.0136  -0.3860 0.0999  3   ILE   X O   
40998 C  CB  . ILE   X  3   ? 1.9930 0.4956 1.5009 -0.0068 -0.3648 -0.0434 3   ILE   X CB  
40999 C  CG1 . ILE   X  3   ? 2.0296 0.5366 1.5616 -0.0668 -0.3790 -0.0791 3   ILE   X CG1 
41000 C  CG2 . ILE   X  3   ? 2.0049 0.3853 1.4411 0.0027  -0.3525 -0.0898 3   ILE   X CG2 
41001 C  CD1 . ILE   X  3   ? 2.0622 0.6574 1.5343 -0.0792 -0.3993 -0.0262 3   ILE   X CD1 
41002 N  N   . ILE   X  4   ? 1.9805 0.4578 1.2779 0.0595  -0.3786 0.0453  4   ILE   X N   
41003 C  CA  . ILE   X  4   ? 2.0034 0.5314 1.2433 0.0661  -0.3813 -0.0004 4   ILE   X CA  
41004 C  C   . ILE   X  4   ? 2.0213 0.4390 1.2366 0.1339  -0.3619 0.0592  4   ILE   X C   
41005 O  O   . ILE   X  4   ? 1.9981 0.3379 1.1421 0.1778  -0.4367 0.0857  4   ILE   X O   
41006 C  CB  . ILE   X  4   ? 2.0384 0.5934 1.1961 0.0517  -0.3266 0.0504  4   ILE   X CB  
41007 C  CG1 . ILE   X  4   ? 2.0171 0.6544 1.2019 0.0144  -0.3110 0.0018  4   ILE   X CG1 
41008 C  CG2 . ILE   X  4   ? 2.0287 0.6753 1.2366 0.0326  -0.3312 0.0221  4   ILE   X CG2 
41009 C  CD1 . ILE   X  4   ? 1.9958 0.6468 1.2037 0.0126  -0.2938 -0.0125 4   ILE   X CD1 
41010 N  N   . LEU   X  5   ? 2.0391 0.4442 1.2483 0.1086  -0.3623 0.0546  5   LEU   X N   
41011 C  CA  . LEU   X  5   ? 2.0226 0.4672 1.2426 0.0892  -0.3534 0.0174  5   LEU   X CA  
41012 C  C   . LEU   X  5   ? 1.9566 0.5176 1.1893 0.0501  -0.3799 0.0248  5   LEU   X C   
41013 O  O   . LEU   X  5   ? 1.9573 0.5003 1.1345 -0.0627 -0.3170 -0.1030 5   LEU   X O   
41014 C  CB  . LEU   X  5   ? 2.1086 0.5783 1.2294 0.1348  -0.3316 0.0688  5   LEU   X CB  
41015 C  CG  . LEU   X  5   ? 2.1805 0.5376 1.2926 0.1652  -0.2664 0.0581  5   LEU   X CG  
41016 C  CD1 . LEU   X  5   ? 2.2291 0.5125 1.3584 0.1892  -0.2511 0.0919  5   LEU   X CD1 
41017 C  CD2 . LEU   X  5   ? 2.2156 0.5621 1.3231 0.1955  -0.2390 0.0602  5   LEU   X CD2 
41018 N  N   . GLY   X  6   ? 1.9430 0.4487 1.1635 0.0962  -0.4035 0.0215  6   GLY   X N   
41019 C  CA  . GLY   X  6   ? 1.9344 0.4582 1.1642 0.1047  -0.4167 0.0165  6   GLY   X CA  
41020 C  C   . GLY   X  6   ? 1.9668 0.4461 1.1507 0.1276  -0.4293 0.0426  6   GLY   X C   
41021 O  O   . GLY   X  6   ? 1.9609 0.3594 1.1898 0.1606  -0.4341 0.0911  6   GLY   X O   
41022 N  N   . ILE   X  7   ? 1.9658 0.5438 1.1442 0.1208  -0.4546 0.0523  7   ILE   X N   
41023 C  CA  . ILE   X  7   ? 1.9823 0.6044 1.1471 0.0871  -0.4988 -0.0080 7   ILE   X CA  
41024 C  C   . ILE   X  7   ? 1.9333 0.6296 1.1537 0.0860  -0.5045 -0.0261 7   ILE   X C   
41025 O  O   . ILE   X  7   ? 1.9482 0.5767 1.1843 0.1064  -0.5086 -0.0380 7   ILE   X O   
41026 C  CB  . ILE   X  7   ? 2.0455 0.6645 1.1364 0.0760  -0.5297 0.0175  7   ILE   X CB  
41027 C  CG1 . ILE   X  7   ? 2.0871 0.6882 1.1706 0.0689  -0.5126 -0.0066 7   ILE   X CG1 
41028 C  CG2 . ILE   X  7   ? 2.0803 0.6430 1.1292 0.0573  -0.5634 0.0072  7   ILE   X CG2 
41029 C  CD1 . ILE   X  7   ? 2.1125 0.7669 1.1639 0.0844  -0.5160 0.0399  7   ILE   X CD1 
41030 N  N   . ARG   X  8   ? 1.9192 0.6429 1.1520 0.0799  -0.5108 -0.0516 8   ARG   X N   
41031 C  CA  . ARG   X  8   ? 1.9283 0.6552 1.1622 0.0755  -0.4887 -0.0876 8   ARG   X CA  
41032 C  C   . ARG   X  8   ? 1.9407 0.6639 1.2127 0.0815  -0.5195 -0.0919 8   ARG   X C   
41033 O  O   . ARG   X  8   ? 1.9324 0.7126 1.2962 0.1148  -0.5213 -0.0862 8   ARG   X O   
41034 C  CB  . ARG   X  8   ? 1.9141 0.6060 1.1377 0.0545  -0.4891 -0.1337 8   ARG   X CB  
41035 C  CG  . ARG   X  8   ? 1.9230 0.6329 1.1880 0.0442  -0.4897 -0.1551 8   ARG   X CG  
41036 C  CD  . ARG   X  8   ? 1.8946 0.6391 1.2254 0.0300  -0.4339 -0.1940 8   ARG   X CD  
41037 N  NE  . ARG   X  8   ? 1.8850 0.5712 1.2968 -0.0037 -0.4635 -0.2782 8   ARG   X NE  
41038 C  CZ  . ARG   X  8   ? 1.8663 0.6098 1.2867 -0.0165 -0.4921 -0.2792 8   ARG   X CZ  
41039 N  NH1 . ARG   X  8   ? 1.9004 0.6619 1.2695 0.0192  -0.4963 -0.2278 8   ARG   X NH1 
41040 N  NH2 . ARG   X  8   ? 1.8112 0.6089 1.3621 -0.0356 -0.4577 -0.3059 8   ARG   X NH2 
41041 N  N   . VAL   X  9   ? 1.9268 0.6742 1.1772 0.1070  -0.5184 -0.0514 9   VAL   X N   
41042 C  CA  . VAL   X  9   ? 1.9467 0.7196 1.1861 0.0821  -0.5430 -0.0374 9   VAL   X CA  
41043 C  C   . VAL   X  9   ? 1.9473 0.7414 1.2012 0.0546  -0.5405 -0.0334 9   VAL   X C   
41044 O  O   . VAL   X  9   ? 1.8719 0.7817 1.1327 0.0255  -0.5644 -0.0344 9   VAL   X O   
41045 C  CB  . VAL   X  9   ? 1.9749 0.8077 1.1733 0.0961  -0.5222 -0.0355 9   VAL   X CB  
41046 C  CG1 . VAL   X  9   ? 1.9831 0.8454 1.1779 0.0579  -0.5189 -0.0621 9   VAL   X CG1 
41047 C  CG2 . VAL   X  9   ? 1.9886 0.7985 1.1617 0.1214  -0.5304 -0.0096 9   VAL   X CG2 
41048 N  N   . GLN   X  10  ? 2.0099 0.7679 1.2067 -0.0078 -0.5630 -0.0382 10  GLN   X N   
41049 C  CA  . GLN   X  10  ? 2.0419 0.8294 1.2507 -0.0381 -0.5667 -0.0792 10  GLN   X CA  
41050 C  C   . GLN   X  10  ? 2.0409 0.7782 1.2226 -0.0838 -0.5735 -0.1401 10  GLN   X C   
41051 O  O   . GLN   X  10  ? 2.0318 0.6654 1.1628 -0.1263 -0.6302 -0.2601 10  GLN   X O   
41052 C  CB  . GLN   X  10  ? 2.0908 0.9059 1.2506 -0.0608 -0.5671 -0.0669 10  GLN   X CB  
41053 C  CG  . GLN   X  10  ? 2.0949 0.9307 1.3215 -0.0878 -0.5480 -0.0920 10  GLN   X CG  
41054 C  CD  . GLN   X  10  ? 2.0911 0.9710 1.3865 -0.0942 -0.5413 -0.0906 10  GLN   X CD  
41055 O  OE1 . GLN   X  10  ? 2.0717 0.9790 1.4019 -0.1000 -0.5236 -0.0823 10  GLN   X OE1 
41056 N  NE2 . GLN   X  10  ? 2.1038 1.0449 1.4211 -0.0928 -0.5683 -0.0970 10  GLN   X NE2 
41057 N  N   . ASP   X  11  ? 2.0652 0.8168 1.2541 -0.0659 -0.5439 -0.1259 11  ASP   X N   
41058 C  CA  . ASP   X  11  ? 2.0999 0.8336 1.3329 -0.0300 -0.4984 -0.0940 11  ASP   X CA  
41059 C  C   . ASP   X  11  ? 2.0946 0.8035 1.3398 -0.0126 -0.4785 -0.0775 11  ASP   X C   
41060 O  O   . ASP   X  11  ? 2.1157 0.8871 1.3475 0.0291  -0.4335 -0.1144 11  ASP   X O   
41061 C  CB  . ASP   X  11  ? 2.1911 0.9478 1.3402 -0.0110 -0.4474 -0.0469 11  ASP   X CB  
41062 C  CG  . ASP   X  11  ? 2.1865 1.0660 1.4786 0.0004  -0.4538 -0.0180 11  ASP   X CG  
41063 O  OD1 . ASP   X  11  ? 2.2159 1.1185 1.5653 -0.0108 -0.3758 -0.0240 11  ASP   X OD1 
41064 O  OD2 . ASP   X  11  ? 2.2894 1.1696 1.5423 0.0103  -0.3916 0.0703  11  ASP   X OD2 
41065 N  N   . SER   X  12  ? 2.0889 0.7123 1.3443 0.0262  -0.4715 -0.0453 12  SER   X N   
41066 C  CA  . SER   X  12  ? 2.0682 0.6823 1.3076 0.0313  -0.4387 -0.0150 12  SER   X CA  
41067 C  C   . SER   X  12  ? 2.0405 0.6179 1.3123 0.0376  -0.4484 0.0010  12  SER   X C   
41068 O  O   . SER   X  12  ? 2.0872 0.5871 1.3732 0.0214  -0.3913 -0.0145 12  SER   X O   
41069 C  CB  . SER   X  12  ? 2.0910 0.7164 1.3217 0.0261  -0.4256 0.0107  12  SER   X CB  
41070 O  OG  . SER   X  12  ? 2.1158 0.7351 1.3109 -0.0187 -0.3973 0.0765  12  SER   X OG  
41071 N  N   . VAL   X  13  ? 2.0180 0.6026 1.2409 -0.0034 -0.4464 -0.0594 13  VAL   X N   
41072 C  CA  . VAL   X  13  ? 2.0166 0.6067 1.2579 -0.0222 -0.4475 -0.0729 13  VAL   X CA  
41073 C  C   . VAL   X  13  ? 2.0298 0.6288 1.1787 -0.0044 -0.4430 -0.0313 13  VAL   X C   
41074 O  O   . VAL   X  13  ? 2.1061 0.4771 1.1295 -0.0293 -0.5011 -0.0988 13  VAL   X O   
41075 C  CB  . VAL   X  13  ? 1.9909 0.6386 1.2540 -0.0509 -0.4151 -0.0660 13  VAL   X CB  
41076 C  CG1 . VAL   X  13  ? 2.0072 0.6831 1.2589 -0.0572 -0.3884 -0.0802 13  VAL   X CG1 
41077 C  CG2 . VAL   X  13  ? 1.9453 0.7005 1.2784 -0.0557 -0.4319 -0.1007 13  VAL   X CG2 
41078 N  N   . ILE   X  14  ? 2.0602 0.6115 1.1945 -0.0020 -0.4412 0.0228  14  ILE   X N   
41079 C  CA  . ILE   X  14  ? 2.0906 0.5960 1.2503 -0.0264 -0.4140 -0.0125 14  ILE   X CA  
41080 C  C   . ILE   X  14  ? 2.0585 0.4848 1.2494 0.0007  -0.3731 -0.0441 14  ILE   X C   
41081 O  O   . ILE   X  14  ? 2.0589 0.5123 1.2864 0.0220  -0.3277 -0.0071 14  ILE   X O   
41082 C  CB  . ILE   X  14  ? 2.1483 0.6336 1.3047 -0.0338 -0.4267 0.0274  14  ILE   X CB  
41083 C  CG1 . ILE   X  14  ? 2.1774 0.6859 1.3714 -0.0536 -0.4572 0.0111  14  ILE   X CG1 
41084 C  CG2 . ILE   X  14  ? 2.1548 0.7338 1.3226 -0.0581 -0.4059 0.0016  14  ILE   X CG2 
41085 C  CD1 . ILE   X  14  ? 2.2166 0.7458 1.3986 -0.0145 -0.4637 0.0374  14  ILE   X CD1 
41086 N  N   . LEU   X  15  ? 2.0593 0.4989 1.2485 0.0281  -0.3465 -0.0709 15  LEU   X N   
41087 C  CA  . LEU   X  15  ? 2.0415 0.4460 1.1986 0.0684  -0.3346 -0.0429 15  LEU   X CA  
41088 C  C   . LEU   X  15  ? 2.0553 0.4650 1.2062 0.0531  -0.3258 -0.0473 15  LEU   X C   
41089 O  O   . LEU   X  15  ? 2.0994 0.3525 1.2754 0.0368  -0.2996 -0.1262 15  LEU   X O   
41090 C  CB  . LEU   X  15  ? 2.0012 0.4153 1.1490 0.0405  -0.3190 -0.0546 15  LEU   X CB  
41091 C  CG  . LEU   X  15  ? 1.9852 0.3143 1.1451 0.0566  -0.3431 -0.1001 15  LEU   X CG  
41092 C  CD1 . LEU   X  15  ? 1.9538 0.3119 1.1494 0.0479  -0.3395 -0.1046 15  LEU   X CD1 
41093 C  CD2 . LEU   X  15  ? 1.9783 0.2731 1.1529 0.0695  -0.3542 -0.0899 15  LEU   X CD2 
41094 N  N   . ALA   X  16  ? 2.0980 0.4287 1.1846 0.0750  -0.3851 0.0000  16  ALA   X N   
41095 C  CA  . ALA   X  16  ? 2.0927 0.4973 1.1535 0.0668  -0.3914 0.0696  16  ALA   X CA  
41096 C  C   . ALA   X  16  ? 2.0717 0.3647 1.1214 0.1142  -0.3731 0.0915  16  ALA   X C   
41097 O  O   . ALA   X  16  ? 2.0677 0.3156 1.1014 0.1100  -0.3883 0.0547  16  ALA   X O   
41098 C  CB  . ALA   X  16  ? 2.1150 0.5503 1.1938 0.1105  -0.4131 0.0872  16  ALA   X CB  
41099 N  N   . SER   X  17  ? 2.0754 0.3579 1.1252 0.1183  -0.3654 0.1389  17  SER   X N   
41100 C  CA  . SER   X  17  ? 2.1093 0.4546 1.0967 0.0978  -0.3553 0.1907  17  SER   X CA  
41101 C  C   . SER   X  17  ? 2.0660 0.4684 1.1229 0.1239  -0.3291 0.1575  17  SER   X C   
41102 O  O   . SER   X  17  ? 2.0906 0.6361 1.1876 0.1075  -0.2581 0.1711  17  SER   X O   
41103 C  CB  . SER   X  17  ? 2.2114 0.4917 1.0347 0.0825  -0.3870 0.2833  17  SER   X CB  
41104 O  OG  . SER   X  17  ? 2.3062 0.4477 1.0486 0.0718  -0.4607 0.2983  17  SER   X OG  
41105 N  N   . SER   X  18  ? 1.9924 0.4312 1.1193 0.1351  -0.3356 0.1719  18  SER   X N   
41106 C  CA  . SER   X  18  ? 1.9956 0.4657 1.1302 0.1141  -0.3179 0.1868  18  SER   X CA  
41107 C  C   . SER   X  18  ? 1.9928 0.4713 1.0798 0.1100  -0.2997 0.1318  18  SER   X C   
41108 O  O   . SER   X  18  ? 1.9452 0.5863 0.9254 0.1436  -0.3230 0.1870  18  SER   X O   
41109 C  CB  . SER   X  18  ? 2.0025 0.4692 1.1284 0.0760  -0.3244 0.1958  18  SER   X CB  
41110 O  OG  . SER   X  18  ? 1.9799 0.4543 1.1756 0.0946  -0.3444 0.2352  18  SER   X OG  
41111 N  N   . LYS   X  19  ? 1.9977 0.4566 1.1355 0.0970  -0.2804 0.1099  19  LYS   X N   
41112 C  CA  . LYS   X  19  ? 1.9843 0.4924 1.1865 0.0906  -0.2844 0.0988  19  LYS   X CA  
41113 C  C   . LYS   X  19  ? 2.0049 0.4088 1.2352 0.0960  -0.2963 0.0673  19  LYS   X C   
41114 O  O   . LYS   X  19  ? 2.0177 0.3902 1.2740 0.0905  -0.2751 0.0263  19  LYS   X O   
41115 C  CB  . LYS   X  19  ? 2.0044 0.5995 1.2006 0.0600  -0.2606 0.1118  19  LYS   X CB  
41116 C  CG  . LYS   X  19  ? 1.9821 0.7036 1.1859 0.0420  -0.2541 0.1171  19  LYS   X CG  
41117 C  CD  . LYS   X  19  ? 1.9814 0.8061 1.2051 0.0330  -0.2262 0.1160  19  LYS   X CD  
41118 C  CE  . LYS   X  19  ? 1.9810 0.8542 1.1665 0.0447  -0.2142 0.1460  19  LYS   X CE  
41119 N  NZ  . LYS   X  19  ? 1.9931 0.9504 1.1772 0.0490  -0.2020 0.1475  19  LYS   X NZ  
41120 N  N   . ALA   X  20  ? 1.9954 0.4109 1.2812 0.1139  -0.2886 0.0532  20  ALA   X N   
41121 C  CA  . ALA   X  20  ? 1.9863 0.4792 1.3364 0.0780  -0.2678 0.0220  20  ALA   X CA  
41122 C  C   . ALA   X  20  ? 1.9711 0.4535 1.3120 0.0601  -0.2580 0.0017  20  ALA   X C   
41123 O  O   . ALA   X  20  ? 1.9678 0.4522 1.2618 0.0672  -0.2478 -0.0248 20  ALA   X O   
41124 C  CB  . ALA   X  20  ? 1.9957 0.4926 1.3548 0.0771  -0.2574 -0.0025 20  ALA   X CB  
41125 N  N   . VAL   X  21  ? 1.9735 0.4779 1.3747 0.0336  -0.2853 -0.0276 21  VAL   X N   
41126 C  CA  . VAL   X  21  ? 1.9705 0.5156 1.3624 0.0000  -0.3188 -0.0693 21  VAL   X CA  
41127 C  C   . VAL   X  21  ? 1.9815 0.4698 1.4177 -0.0139 -0.2961 -0.0572 21  VAL   X C   
41128 O  O   . VAL   X  21  ? 1.9951 0.3641 1.4028 -0.0542 -0.2838 -0.0271 21  VAL   X O   
41129 C  CB  . VAL   X  21  ? 1.9717 0.5600 1.4110 0.0339  -0.3192 -0.1101 21  VAL   X CB  
41130 C  CG1 . VAL   X  21  ? 1.9655 0.6114 1.3764 0.0234  -0.3240 -0.1511 21  VAL   X CG1 
41131 C  CG2 . VAL   X  21  ? 1.9804 0.5731 1.4196 0.0286  -0.3256 -0.1242 21  VAL   X CG2 
41132 N  N   . THR   X  22  ? 1.9794 0.5490 1.4047 -0.0389 -0.2780 -0.0778 22  THR   X N   
41133 C  CA  . THR   X  22  ? 2.0059 0.6434 1.4452 -0.1160 -0.2681 -0.1067 22  THR   X CA  
41134 C  C   . THR   X  22  ? 1.9234 0.6479 1.4253 -0.1475 -0.2419 -0.1205 22  THR   X C   
41135 O  O   . THR   X  22  ? 1.9648 0.5941 1.4232 -0.0841 -0.2182 -0.0605 22  THR   X O   
41136 C  CB  . THR   X  22  ? 2.0548 0.6208 1.4604 -0.1212 -0.2749 -0.1632 22  THR   X CB  
41137 O  OG1 . THR   X  22  ? 2.1250 0.6607 1.4588 -0.1200 -0.3011 -0.1986 22  THR   X OG1 
41138 C  CG2 . THR   X  22  ? 2.0832 0.6814 1.4854 -0.1417 -0.2945 -0.1979 22  THR   X CG2 
41139 N  N   . ARG   X  23  ? 1.9221 0.7642 1.4570 -0.1582 -0.2409 -0.1660 23  ARG   X N   
41140 C  CA  . ARG   X  23  ? 1.8999 0.9012 1.4568 -0.1721 -0.2494 -0.1753 23  ARG   X CA  
41141 C  C   . ARG   X  23  ? 1.8568 0.9878 1.4026 -0.2016 -0.2803 -0.2032 23  ARG   X C   
41142 O  O   . ARG   X  23  ? 1.7954 1.0742 1.4187 -0.2081 -0.3122 -0.2309 23  ARG   X O   
41143 C  CB  . ARG   X  23  ? 1.8373 1.0195 1.5610 -0.1285 -0.2467 -0.2254 23  ARG   X CB  
41144 C  CG  . ARG   X  23  ? 1.8490 1.0918 1.5889 -0.1690 -0.2385 -0.2208 23  ARG   X CG  
41145 C  CD  . ARG   X  23  ? 1.9011 1.1046 1.6472 -0.1290 -0.2592 -0.3143 23  ARG   X CD  
41146 N  NE  . ARG   X  23  ? 1.9074 1.1277 1.7119 -0.1185 -0.2699 -0.3603 23  ARG   X NE  
41147 C  CZ  . ARG   X  23  ? 1.9175 1.0126 1.8275 -0.1104 -0.2251 -0.3132 23  ARG   X CZ  
41148 N  NH1 . ARG   X  23  ? 1.9188 1.0864 1.9394 -0.0848 -0.2092 -0.3274 23  ARG   X NH1 
41149 N  NH2 . ARG   X  23  ? 1.9253 1.0427 1.8467 -0.0228 -0.1909 -0.2408 23  ARG   X NH2 
41150 N  N   . GLY   X  24  ? 1.8636 1.0580 1.3331 -0.1985 -0.2941 -0.1917 24  GLY   X N   
41151 C  CA  . GLY   X  24  ? 1.8567 1.0329 1.3458 -0.1851 -0.2815 -0.1807 24  GLY   X CA  
41152 C  C   . GLY   X  24  ? 1.8761 0.9882 1.3911 -0.2156 -0.2527 -0.1693 24  GLY   X C   
41153 O  O   . GLY   X  24  ? 1.8671 1.0347 1.3987 -0.1884 -0.2367 -0.1886 24  GLY   X O   
41154 N  N   . ILE   X  25  ? 1.8916 0.9566 1.4530 -0.2385 -0.2831 -0.1698 25  ILE   X N   
41155 C  CA  . ILE   X  25  ? 1.9178 0.9466 1.4837 -0.2578 -0.2535 -0.1571 25  ILE   X CA  
41156 C  C   . ILE   X  25  ? 1.9229 0.8730 1.5017 -0.2577 -0.2243 -0.1441 25  ILE   X C   
41157 O  O   . ILE   X  25  ? 1.9266 1.0361 1.4563 -0.2956 -0.1613 -0.1387 25  ILE   X O   
41158 C  CB  . ILE   X  25  ? 1.9288 0.9722 1.5416 -0.2596 -0.2860 -0.1839 25  ILE   X CB  
41159 C  CG1 . ILE   X  25  ? 1.9268 0.9858 1.5714 -0.2716 -0.3128 -0.1869 25  ILE   X CG1 
41160 C  CG2 . ILE   X  25  ? 1.9566 0.9655 1.5239 -0.2497 -0.2989 -0.1845 25  ILE   X CG2 
41161 C  CD1 . ILE   X  25  ? 1.9336 1.0035 1.6352 -0.2900 -0.3285 -0.2009 25  ILE   X CD1 
41162 N  N   . SER   X  26  ? 1.8916 0.8312 1.4460 -0.2455 -0.2025 -0.0635 26  SER   X N   
41163 C  CA  . SER   X  26  ? 1.9104 0.7294 1.4671 -0.2238 -0.1824 -0.0400 26  SER   X CA  
41164 C  C   . SER   X  26  ? 1.8855 0.7150 1.4290 -0.2014 -0.1820 -0.0197 26  SER   X C   
41165 O  O   . SER   X  26  ? 1.8685 0.7293 1.4285 -0.1800 -0.1577 -0.0135 26  SER   X O   
41166 C  CB  . SER   X  26  ? 1.8934 0.6763 1.4876 -0.2491 -0.1810 -0.0673 26  SER   X CB  
41167 O  OG  . SER   X  26  ? 1.9954 0.5763 1.5177 -0.2765 -0.1631 -0.0916 26  SER   X OG  
41168 N  N   . VAL   X  27  ? 1.9174 0.6914 1.4320 -0.1785 -0.1813 -0.0062 27  VAL   X N   
41169 C  CA  . VAL   X  27  ? 1.9000 0.6643 1.4139 -0.1482 -0.2123 0.0172  27  VAL   X CA  
41170 C  C   . VAL   X  27  ? 1.9363 0.6996 1.4427 -0.1048 -0.2287 0.0086  27  VAL   X C   
41171 O  O   . VAL   X  27  ? 1.9607 0.6339 1.4669 -0.1194 -0.2095 0.0021  27  VAL   X O   
41172 C  CB  . VAL   X  27  ? 1.9044 0.6532 1.4343 -0.1506 -0.2041 0.0446  27  VAL   X CB  
41173 C  CG1 . VAL   X  27  ? 1.8906 0.6200 1.4133 -0.1391 -0.1979 0.0661  27  VAL   X CG1 
41174 C  CG2 . VAL   X  27  ? 1.9095 0.6324 1.4216 -0.1623 -0.2274 0.0275  27  VAL   X CG2 
41175 N  N   . LEU   X  28  ? 1.9608 0.7318 1.4204 -0.0046 -0.2717 0.0240  28  LEU   X N   
41176 C  CA  . LEU   X  28  ? 1.9987 0.7754 1.4321 0.0367  -0.2857 0.0033  28  LEU   X CA  
41177 C  C   . LEU   X  28  ? 2.0033 0.6765 1.4054 0.0922  -0.2597 0.0280  28  LEU   X C   
41178 O  O   . LEU   X  28  ? 2.0500 0.6696 1.3563 0.1630  -0.2687 0.0756  28  LEU   X O   
41179 C  CB  . LEU   X  28  ? 1.9985 0.8069 1.3898 0.0406  -0.3039 -0.0101 28  LEU   X CB  
41180 C  CG  . LEU   X  28  ? 2.0156 0.9059 1.4290 0.0093  -0.3369 -0.0417 28  LEU   X CG  
41181 C  CD1 . LEU   X  28  ? 1.9648 0.8624 1.4258 -0.0069 -0.3703 -0.0658 28  LEU   X CD1 
41182 C  CD2 . LEU   X  28  ? 2.0438 0.9118 1.4421 -0.0284 -0.3257 -0.0272 28  LEU   X CD2 
41183 N  N   . LYS   X  29  ? 1.9861 0.6102 1.4475 0.0697  -0.2352 0.0443  29  LYS   X N   
41184 C  CA  . LYS   X  29  ? 1.9700 0.6497 1.4693 0.0322  -0.2138 0.0234  29  LYS   X CA  
41185 C  C   . LYS   X  29  ? 1.9655 0.5778 1.4413 0.0011  -0.2052 0.0577  29  LYS   X C   
41186 O  O   . LYS   X  29  ? 1.9215 0.5979 1.4619 -0.0369 -0.1772 0.1032  29  LYS   X O   
41187 C  CB  . LYS   X  29  ? 1.9871 0.6580 1.4959 0.0134  -0.2114 0.0220  29  LYS   X CB  
41188 C  CG  . LYS   X  29  ? 2.0096 0.7264 1.5329 0.0291  -0.1797 -0.0225 29  LYS   X CG  
41189 C  CD  . LYS   X  29  ? 1.9748 0.7101 1.5628 0.0479  -0.1559 -0.0511 29  LYS   X CD  
41190 C  CE  . LYS   X  29  ? 1.9890 0.7519 1.5640 0.0700  -0.1149 -0.0756 29  LYS   X CE  
41191 N  NZ  . LYS   X  29  ? 1.9771 0.7568 1.5891 0.1221  -0.1080 -0.0631 29  LYS   X NZ  
41192 N  N   . ASP   X  30  ? 1.9725 0.6100 1.4279 -0.0194 -0.1686 0.0443  30  ASP   X N   
41193 C  CA  . ASP   X  30  ? 1.9651 0.7018 1.3574 -0.0261 -0.1720 0.0405  30  ASP   X CA  
41194 C  C   . ASP   X  30  ? 2.0081 0.6372 1.3215 -0.0152 -0.1553 0.0479  30  ASP   X C   
41195 O  O   . ASP   X  30  ? 2.0199 0.5489 1.2647 -0.0784 -0.1623 0.0168  30  ASP   X O   
41196 C  CB  . ASP   X  30  ? 1.9433 0.8246 1.3882 -0.0085 -0.1148 0.1347  30  ASP   X CB  
41197 C  CG  . ASP   X  30  ? 1.9182 0.9241 1.4601 0.0049  -0.0814 0.1524  30  ASP   X CG  
41198 O  OD1 . ASP   X  30  ? 1.8117 0.9588 1.4247 0.0391  -0.0313 0.1624  30  ASP   X OD1 
41199 O  OD2 . ASP   X  30  ? 1.8515 1.0526 1.5333 -0.0568 -0.0047 0.1953  30  ASP   X OD2 
41200 N  N   . SER   X  31  ? 2.0344 0.6130 1.2808 0.0021  -0.1493 -0.0520 31  SER   X N   
41201 C  CA  . SER   X  31  ? 2.0784 0.6058 1.2643 0.0482  -0.1111 -0.0955 31  SER   X CA  
41202 C  C   . SER   X  31  ? 2.1059 0.5056 1.2444 0.0758  -0.1311 -0.1504 31  SER   X C   
41203 O  O   . SER   X  31  ? 2.1746 0.4530 1.2484 0.0793  -0.1303 -0.1004 31  SER   X O   
41204 C  CB  . SER   X  31  ? 2.0793 0.6231 1.3011 0.0334  -0.0821 -0.0909 31  SER   X CB  
41205 O  OG  . SER   X  31  ? 2.0469 0.5575 1.2867 0.0298  -0.0568 -0.1158 31  SER   X OG  
41206 N  N   . ASP   X  32  ? 2.0797 0.4881 1.2672 0.0964  -0.1422 -0.2294 32  ASP   X N   
41207 C  CA  . ASP   X  32  ? 2.0518 0.4033 1.3057 0.0799  -0.1559 -0.2777 32  ASP   X CA  
41208 C  C   . ASP   X  32  ? 2.0459 0.4815 1.2711 0.1065  -0.2026 -0.3011 32  ASP   X C   
41209 O  O   . ASP   X  32  ? 2.2173 0.3667 1.2255 0.0246  -0.2584 -0.2696 32  ASP   X O   
41210 C  CB  . ASP   X  32  ? 2.0207 0.4538 1.3169 0.1070  -0.1387 -0.3077 32  ASP   X CB  
41211 C  CG  . ASP   X  32  ? 2.0140 0.4391 1.3669 0.0699  -0.1327 -0.3148 32  ASP   X CG  
41212 O  OD1 . ASP   X  32  ? 1.9777 0.4324 1.3446 0.0412  -0.1144 -0.3418 32  ASP   X OD1 
41213 O  OD2 . ASP   X  32  ? 1.9969 0.4573 1.4775 0.0906  -0.0911 -0.3430 32  ASP   X OD2 
41214 N  N   . ASP   X  33  ? 2.0884 0.5046 1.3186 -0.0068 -0.2346 -0.2864 33  ASP   X N   
41215 C  CA  . ASP   X  33  ? 2.0867 0.6670 1.3285 -0.0363 -0.2817 -0.2539 33  ASP   X CA  
41216 C  C   . ASP   X  33  ? 2.0125 0.6456 1.3126 -0.0101 -0.2882 -0.2681 33  ASP   X C   
41217 O  O   . ASP   X  33  ? 2.0449 0.5596 1.3158 -0.0351 -0.2756 -0.3221 33  ASP   X O   
41218 C  CB  . ASP   X  33  ? 2.1673 0.6642 1.3743 -0.0498 -0.3062 -0.2789 33  ASP   X CB  
41219 C  CG  . ASP   X  33  ? 2.2529 0.7403 1.3875 -0.0859 -0.3711 -0.2991 33  ASP   X CG  
41220 O  OD1 . ASP   X  33  ? 2.1964 0.9167 1.4485 -0.0726 -0.3812 -0.1965 33  ASP   X OD1 
41221 O  OD2 . ASP   X  33  ? 2.3492 0.8962 1.3436 -0.0894 -0.3685 -0.4059 33  ASP   X OD2 
41222 N  N   . LYS   X  34  ? 1.9264 0.7840 1.3328 -0.0019 -0.2816 -0.2292 34  LYS   X N   
41223 C  CA  . LYS   X  34  ? 1.8409 0.6993 1.3450 -0.0247 -0.3361 -0.1600 34  LYS   X CA  
41224 C  C   . LYS   X  34  ? 1.8251 0.5957 1.3060 0.0195  -0.3901 -0.1223 34  LYS   X C   
41225 O  O   . LYS   X  34  ? 1.7561 0.3691 1.2214 -0.0514 -0.4580 -0.1227 34  LYS   X O   
41226 C  CB  . LYS   X  34  ? 1.8719 0.7131 1.3857 0.0021  -0.2987 -0.1550 34  LYS   X CB  
41227 C  CG  . LYS   X  34  ? 1.8797 0.6824 1.4090 -0.0126 -0.2621 -0.1401 34  LYS   X CG  
41228 C  CD  . LYS   X  34  ? 1.9092 0.7125 1.4046 0.0494  -0.2295 -0.0946 34  LYS   X CD  
41229 C  CE  . LYS   X  34  ? 1.9099 0.7727 1.4307 0.0276  -0.2135 -0.1043 34  LYS   X CE  
41230 N  NZ  . LYS   X  34  ? 1.9270 0.8350 1.4843 0.0606  -0.1745 -0.1213 34  LYS   X NZ  
41231 N  N   . THR   X  35  ? 1.7545 0.6129 1.2856 0.0073  -0.3715 -0.1253 35  THR   X N   
41232 C  CA  . THR   X  35  ? 1.7267 0.6933 1.2947 -0.0243 -0.3659 -0.1025 35  THR   X CA  
41233 C  C   . THR   X  35  ? 1.7353 0.6798 1.3247 -0.0363 -0.3064 -0.0969 35  THR   X C   
41234 O  O   . THR   X  35  ? 1.7588 0.6030 1.4091 -0.0528 -0.2417 -0.0631 35  THR   X O   
41235 C  CB  . THR   X  35  ? 1.7503 0.8128 1.3016 -0.0131 -0.3747 -0.0802 35  THR   X CB  
41236 O  OG1 . THR   X  35  ? 1.7120 0.9628 1.3021 0.0080  -0.4234 -0.0679 35  THR   X OG1 
41237 C  CG2 . THR   X  35  ? 1.7372 0.8569 1.2848 -0.0200 -0.3706 -0.0721 35  THR   X CG2 
41238 N  N   . ARG   X  36  ? 1.7684 0.6052 1.3101 -0.0137 -0.3079 -0.1278 36  ARG   X N   
41239 C  CA  . ARG   X  36  ? 1.7518 0.5731 1.2528 -0.0994 -0.3262 -0.1720 36  ARG   X CA  
41240 C  C   . ARG   X  36  ? 1.7583 0.5131 1.1626 -0.0791 -0.3333 -0.1337 36  ARG   X C   
41241 O  O   . ARG   X  36  ? 1.7433 0.2917 1.1120 -0.1022 -0.3798 -0.1759 36  ARG   X O   
41242 C  CB  . ARG   X  36  ? 1.7106 0.5687 1.2372 -0.1091 -0.3422 -0.2064 36  ARG   X CB  
41243 C  CG  . ARG   X  36  ? 1.6832 0.6611 1.2439 -0.0867 -0.3316 -0.2387 36  ARG   X CG  
41244 C  CD  . ARG   X  36  ? 1.6747 0.7302 1.2767 -0.0568 -0.3263 -0.2724 36  ARG   X CD  
41245 N  NE  . ARG   X  36  ? 1.6222 0.7826 1.2596 -0.0582 -0.3439 -0.3083 36  ARG   X NE  
41246 C  CZ  . ARG   X  36  ? 1.6182 0.7538 1.2981 -0.0532 -0.3493 -0.3364 36  ARG   X CZ  
41247 N  NH1 . ARG   X  36  ? 1.6361 0.7759 1.3199 -0.0287 -0.3503 -0.3258 36  ARG   X NH1 
41248 N  NH2 . ARG   X  36  ? 1.6379 0.7587 1.3393 -0.0687 -0.3267 -0.3104 36  ARG   X NH2 
41249 N  N   . GLN   X  37  ? 1.8006 0.5860 1.0772 -0.0270 -0.2946 -0.1023 37  GLN   X N   
41250 C  CA  . GLN   X  37  ? 1.8035 0.5704 1.0665 -0.0050 -0.2835 -0.1388 37  GLN   X CA  
41251 C  C   . GLN   X  37  ? 1.7671 0.5356 1.0855 0.0105  -0.2865 -0.1517 37  GLN   X C   
41252 O  O   . GLN   X  37  ? 1.7589 0.5959 1.2028 0.0370  -0.2398 -0.1433 37  GLN   X O   
41253 C  CB  . GLN   X  37  ? 1.8452 0.6306 1.0816 0.0177  -0.2252 -0.1138 37  GLN   X CB  
41254 C  CG  . GLN   X  37  ? 1.8603 0.6780 1.0173 0.0130  -0.2062 -0.1328 37  GLN   X CG  
41255 C  CD  . GLN   X  37  ? 1.9216 0.7308 0.9985 0.0254  -0.1707 -0.0943 37  GLN   X CD  
41256 O  OE1 . GLN   X  37  ? 1.9732 0.7476 1.0224 0.0122  -0.1404 -0.1194 37  GLN   X OE1 
41257 N  NE2 . GLN   X  37  ? 1.9324 0.7802 0.9789 0.0381  -0.1455 -0.0772 37  GLN   X NE2 
41258 N  N   . LEU   X  38  ? 1.7539 0.5330 1.0609 0.0039  -0.3107 -0.1274 38  LEU   X N   
41259 C  CA  . LEU   X  38  ? 1.7560 0.5807 1.0781 0.0087  -0.3133 -0.0885 38  LEU   X CA  
41260 C  C   . LEU   X  38  ? 1.7691 0.6395 1.0908 -0.0248 -0.3466 -0.1150 38  LEU   X C   
41261 O  O   . LEU   X  38  ? 1.7793 0.5981 1.1476 -0.0129 -0.3386 -0.1893 38  LEU   X O   
41262 C  CB  . LEU   X  38  ? 1.7374 0.6183 1.0712 0.0237  -0.3107 -0.0348 38  LEU   X CB  
41263 C  CG  . LEU   X  38  ? 1.7251 0.6370 1.0764 -0.0198 -0.3100 -0.0249 38  LEU   X CG  
41264 C  CD1 . LEU   X  38  ? 1.7006 0.7138 1.0998 -0.0134 -0.3061 0.0180  38  LEU   X CD1 
41265 C  CD2 . LEU   X  38  ? 1.7094 0.6820 1.0954 -0.0487 -0.2951 -0.0180 38  LEU   X CD2 
41266 N  N   . SER   X  39  ? 1.7971 0.5930 1.1088 -0.0156 -0.3659 -0.1093 39  SER   X N   
41267 C  CA  . SER   X  39  ? 1.8583 0.5903 1.1581 0.0049  -0.3599 -0.1451 39  SER   X CA  
41268 C  C   . SER   X  39  ? 1.8882 0.6628 1.1463 -0.0057 -0.3422 -0.1340 39  SER   X C   
41269 O  O   . SER   X  39  ? 1.8491 0.6457 1.0864 -0.0371 -0.3705 -0.2039 39  SER   X O   
41270 C  CB  . SER   X  39  ? 1.8523 0.5171 1.1772 0.0015  -0.3764 -0.1912 39  SER   X CB  
41271 O  OG  . SER   X  39  ? 1.8963 0.4458 1.1840 0.0177  -0.3916 -0.2463 39  SER   X OG  
41272 N  N   . PRO   X  40  ? 1.9223 0.6411 1.1301 0.0226  -0.3184 -0.1206 40  PRO   X N   
41273 C  CA  . PRO   X  40  ? 1.9634 0.6528 1.1600 0.0533  -0.3136 -0.0800 40  PRO   X CA  
41274 C  C   . PRO   X  40  ? 2.0446 0.6246 1.1586 0.0625  -0.3474 0.0063  40  PRO   X C   
41275 O  O   . PRO   X  40  ? 2.0513 0.5343 1.1791 0.1842  -0.3742 0.0130  40  PRO   X O   
41276 C  CB  . PRO   X  40  ? 1.9822 0.6933 1.1554 0.0360  -0.3129 -0.1024 40  PRO   X CB  
41277 C  CG  . PRO   X  40  ? 1.9490 0.7362 1.1692 0.0656  -0.3094 -0.1014 40  PRO   X CG  
41278 C  CD  . PRO   X  40  ? 1.9222 0.6454 1.1817 0.0634  -0.2966 -0.1208 40  PRO   X CD  
41279 N  N   . HIS   X  41  ? 2.0331 0.6066 1.1851 0.0510  -0.3577 0.0207  41  HIS   X N   
41280 C  CA  . HIS   X  41  ? 2.0684 0.6012 1.1914 0.0605  -0.4009 0.0421  41  HIS   X CA  
41281 C  C   . HIS   X  41  ? 2.0279 0.6140 1.2049 0.0341  -0.4243 0.0215  41  HIS   X C   
41282 O  O   . HIS   X  41  ? 2.0135 0.7172 1.2878 0.0591  -0.4648 0.0153  41  HIS   X O   
41283 C  CB  . HIS   X  41  ? 2.1198 0.6037 1.2330 0.0283  -0.4264 0.0605  41  HIS   X CB  
41284 C  CG  . HIS   X  41  ? 2.2324 0.6987 1.2108 0.0447  -0.4189 0.0655  41  HIS   X CG  
41285 N  ND1 . HIS   X  41  ? 2.2503 0.7265 1.3033 0.1161  -0.4099 0.0207  41  HIS   X ND1 
41286 C  CD2 . HIS   X  41  ? 2.2970 0.7216 1.2427 0.0579  -0.4442 0.1110  41  HIS   X CD2 
41287 C  CE1 . HIS   X  41  ? 2.3054 0.7506 1.2764 0.1144  -0.4195 0.0758  41  HIS   X CE1 
41288 N  NE2 . HIS   X  41  ? 2.3277 0.7683 1.2535 0.0932  -0.4411 0.0843  41  HIS   X NE2 
41289 N  N   . THR   X  42  ? 1.9967 0.5372 1.1902 0.0084  -0.3975 -0.0141 42  THR   X N   
41290 C  CA  . THR   X  42  ? 1.9258 0.5080 1.1938 -0.0090 -0.4010 -0.0203 42  THR   X CA  
41291 C  C   . THR   X  42  ? 1.8967 0.4989 1.1254 0.0119  -0.3780 -0.0444 42  THR   X C   
41292 O  O   . THR   X  42  ? 1.8920 0.4881 1.0957 0.0085  -0.3618 -0.0257 42  THR   X O   
41293 C  CB  . THR   X  42  ? 1.9426 0.4546 1.1512 -0.0286 -0.3934 -0.0769 42  THR   X CB  
41294 O  OG1 . THR   X  42  ? 1.9427 0.4639 1.2133 -0.0244 -0.3906 -0.0445 42  THR   X OG1 
41295 C  CG2 . THR   X  42  ? 1.9200 0.4879 1.1671 -0.0354 -0.3897 -0.1037 42  THR   X CG2 
41296 N  N   . LEU   X  43  ? 1.8533 0.5029 1.1258 -0.0140 -0.3786 -0.0743 43  LEU   X N   
41297 C  CA  . LEU   X  43  ? 1.8462 0.4921 1.1427 -0.0097 -0.3524 -0.0875 43  LEU   X CA  
41298 C  C   . LEU   X  43  ? 1.8257 0.4296 1.1339 -0.0256 -0.3703 -0.0738 43  LEU   X C   
41299 O  O   . LEU   X  43  ? 1.8052 0.3491 1.1337 -0.0478 -0.3964 -0.0773 43  LEU   X O   
41300 C  CB  . LEU   X  43  ? 1.8549 0.4550 1.1815 -0.0002 -0.3374 -0.0803 43  LEU   X CB  
41301 C  CG  . LEU   X  43  ? 1.8589 0.4370 1.2310 0.0098  -0.2933 -0.0797 43  LEU   X CG  
41302 C  CD1 . LEU   X  43  ? 1.8835 0.4134 1.2614 0.0123  -0.2578 -0.0973 43  LEU   X CD1 
41303 C  CD2 . LEU   X  43  ? 1.8699 0.5494 1.2194 0.0344  -0.3148 -0.0412 43  LEU   X CD2 
41304 N  N   . MET   X  44  ? 1.8344 0.3961 1.0923 -0.0262 -0.3656 -0.0738 44  MET   X N   
41305 C  CA  . MET   X  44  ? 1.8075 0.4326 1.0823 -0.0076 -0.3708 -0.0765 44  MET   X CA  
41306 C  C   . MET   X  44  ? 1.8000 0.4340 1.0302 -0.0004 -0.3532 -0.0831 44  MET   X C   
41307 O  O   . MET   X  44  ? 1.8197 0.5524 1.0122 0.0310  -0.3178 -0.0635 44  MET   X O   
41308 C  CB  . MET   X  44  ? 1.7876 0.4121 1.1420 -0.0155 -0.3751 -0.0495 44  MET   X CB  
41309 C  CG  . MET   X  44  ? 1.7831 0.3815 1.1667 -0.0089 -0.3785 -0.0543 44  MET   X CG  
41310 S  SD  . MET   X  44  ? 1.7877 0.3334 1.2484 0.0039  -0.3990 -0.0240 44  MET   X SD  
41311 C  CE  . MET   X  44  ? 1.7809 0.3578 1.3027 -0.0159 -0.3837 -0.0620 44  MET   X CE  
41312 N  N   . SER   X  45  ? 1.8448 0.4224 1.0455 -0.0133 -0.3609 -0.1050 45  SER   X N   
41313 C  CA  . SER   X  45  ? 1.9075 0.3898 1.0920 -0.0047 -0.3387 -0.1621 45  SER   X CA  
41314 C  C   . SER   X  45  ? 1.8512 0.1973 1.1001 -0.0207 -0.3944 -0.1618 45  SER   X C   
41315 O  O   . SER   X  45  ? 1.8571 0.2001 1.0471 0.0027  -0.3923 -0.1845 45  SER   X O   
41316 C  CB  . SER   X  45  ? 1.9469 0.3655 1.1474 0.0067  -0.3277 -0.1785 45  SER   X CB  
41317 O  OG  . SER   X  45  ? 1.9795 0.4729 1.2284 -0.0048 -0.2902 -0.3195 45  SER   X OG  
41318 N  N   . PHE   X  46  ? 1.8488 0.1947 1.1038 -0.0384 -0.3850 -0.1496 46  PHE   X N   
41319 C  CA  . PHE   X  46  ? 1.8329 0.2781 1.0835 -0.0081 -0.3774 -0.0894 46  PHE   X CA  
41320 C  C   . PHE   X  46  ? 1.8483 0.3124 1.1142 -0.0243 -0.3751 -0.1360 46  PHE   X C   
41321 O  O   . PHE   X  46  ? 1.9117 0.3652 1.1661 -0.0074 -0.3087 -0.1367 46  PHE   X O   
41322 C  CB  . PHE   X  46  ? 1.8151 0.2275 1.0304 -0.0610 -0.3789 -0.0807 46  PHE   X CB  
41323 C  CG  . PHE   X  46  ? 1.7913 0.2183 1.0646 -0.0671 -0.3683 -0.0409 46  PHE   X CG  
41324 C  CD1 . PHE   X  46  ? 1.7960 0.2182 1.0683 -0.0733 -0.3629 -0.0259 46  PHE   X CD1 
41325 C  CD2 . PHE   X  46  ? 1.8046 0.2830 1.0664 -0.0845 -0.3779 -0.0680 46  PHE   X CD2 
41326 C  CE1 . PHE   X  46  ? 1.7870 0.2381 1.1014 -0.0921 -0.3483 -0.0119 46  PHE   X CE1 
41327 C  CE2 . PHE   X  46  ? 1.7848 0.3302 1.1072 -0.1008 -0.3586 -0.0293 46  PHE   X CE2 
41328 C  CZ  . PHE   X  46  ? 1.8053 0.2653 1.1041 -0.1105 -0.3565 -0.0223 46  PHE   X CZ  
41329 N  N   . ALA   X  47  ? 1.8102 0.3821 1.1028 0.0121  -0.3560 -0.1243 47  ALA   X N   
41330 C  CA  . ALA   X  47  ? 1.7754 0.3967 1.1392 -0.0131 -0.3383 -0.1122 47  ALA   X CA  
41331 C  C   . ALA   X  47  ? 1.7399 0.3704 1.1387 -0.0142 -0.3411 -0.1156 47  ALA   X C   
41332 O  O   . ALA   X  47  ? 1.7259 0.4046 1.1063 -0.0146 -0.3514 -0.1218 47  ALA   X O   
41333 C  CB  . ALA   X  47  ? 1.7701 0.4512 1.1637 0.0189  -0.3355 -0.0931 47  ALA   X CB  
41334 N  N   . GLY   X  48  ? 1.7280 0.3328 1.1459 -0.0196 -0.3294 -0.1064 48  GLY   X N   
41335 C  CA  . GLY   X  48  ? 1.6844 0.3622 1.1500 -0.0283 -0.3490 -0.0946 48  GLY   X CA  
41336 C  C   . GLY   X  48  ? 1.6771 0.3761 1.2022 -0.0420 -0.3427 -0.1122 48  GLY   X C   
41337 O  O   . GLY   X  48  ? 1.6660 0.3534 1.1774 -0.0441 -0.3833 -0.0752 48  GLY   X O   
41338 N  N   . GLU   X  49  ? 1.6780 0.4400 1.1910 -0.0356 -0.3264 -0.1140 49  GLU   X N   
41339 C  CA  . GLU   X  49  ? 1.6533 0.5304 1.2800 -0.0295 -0.3271 -0.1273 49  GLU   X CA  
41340 C  C   . GLU   X  49  ? 1.6308 0.4692 1.1868 -0.0369 -0.3491 -0.0693 49  GLU   X C   
41341 O  O   . GLU   X  49  ? 1.5780 0.4397 1.1420 -0.0597 -0.3913 0.0002  49  GLU   X O   
41342 C  CB  . GLU   X  49  ? 1.7117 0.6078 1.3064 -0.0123 -0.2791 -0.1225 49  GLU   X CB  
41343 C  CG  . GLU   X  49  ? 1.6792 0.7543 1.4907 -0.0024 -0.2874 -0.1928 49  GLU   X CG  
41344 C  CD  . GLU   X  49  ? 1.8011 0.8559 1.6378 -0.0841 -0.2498 -0.2940 49  GLU   X CD  
41345 O  OE1 . GLU   X  49  ? 1.8477 1.0237 1.7591 -0.0073 -0.1697 -0.3840 49  GLU   X OE1 
41346 O  OE2 . GLU   X  49  ? 1.8009 1.0455 1.7682 -0.0125 -0.2493 -0.3408 49  GLU   X OE2 
41347 N  N   . ALA   X  50  ? 1.6349 0.4872 1.1942 -0.0434 -0.3499 -0.0827 50  ALA   X N   
41348 C  CA  . ALA   X  50  ? 1.6564 0.5952 1.2352 -0.0316 -0.3306 -0.1233 50  ALA   X CA  
41349 C  C   . ALA   X  50  ? 1.6321 0.6260 1.2384 -0.0014 -0.3243 -0.1178 50  ALA   X C   
41350 O  O   . ALA   X  50  ? 1.6316 0.8314 1.2331 -0.0414 -0.2864 -0.1415 50  ALA   X O   
41351 C  CB  . ALA   X  50  ? 1.6600 0.5974 1.2779 -0.0323 -0.3293 -0.1350 50  ALA   X CB  
41352 N  N   . GLY   X  51  ? 1.6328 0.6351 1.2373 -0.0224 -0.3222 -0.1341 51  GLY   X N   
41353 C  CA  . GLY   X  51  ? 1.6447 0.6471 1.2388 0.0201  -0.3329 -0.1443 51  GLY   X CA  
41354 C  C   . GLY   X  51  ? 1.6118 0.6526 1.2382 0.0572  -0.3276 -0.1089 51  GLY   X C   
41355 O  O   . GLY   X  51  ? 1.6300 0.5924 1.3302 0.0524  -0.3530 -0.0921 51  GLY   X O   
41356 N  N   . ASP   X  52  ? 1.6495 0.6451 1.1974 0.0893  -0.3436 -0.1095 52  ASP   X N   
41357 C  CA  . ASP   X  52  ? 1.6792 0.6076 1.1925 0.0761  -0.3531 -0.0668 52  ASP   X CA  
41358 C  C   . ASP   X  52  ? 1.6613 0.5161 1.2148 0.0519  -0.3358 -0.1051 52  ASP   X C   
41359 O  O   . ASP   X  52  ? 1.6623 0.4410 1.2812 0.1159  -0.2947 -0.0696 52  ASP   X O   
41360 C  CB  . ASP   X  52  ? 1.6824 0.6650 1.1491 0.0767  -0.3537 -0.0569 52  ASP   X CB  
41361 C  CG  . ASP   X  52  ? 1.6876 0.7021 1.1728 0.0906  -0.3855 -0.0141 52  ASP   X CG  
41362 O  OD1 . ASP   X  52  ? 1.7134 0.6859 1.1819 0.0985  -0.4107 -0.0109 52  ASP   X OD1 
41363 O  OD2 . ASP   X  52  ? 1.7236 0.8055 1.0506 0.0253  -0.3567 -0.0053 52  ASP   X OD2 
41364 N  N   . THR   X  53  ? 1.7128 0.5915 1.1613 0.0494  -0.3476 -0.0938 53  THR   X N   
41365 C  CA  . THR   X  53  ? 1.7180 0.5337 1.1515 0.0336  -0.3501 -0.1106 53  THR   X CA  
41366 C  C   . THR   X  53  ? 1.6565 0.4979 1.1032 -0.0121 -0.3806 -0.0974 53  THR   X C   
41367 O  O   . THR   X  53  ? 1.6583 0.4755 1.0919 -0.0009 -0.4172 -0.0636 53  THR   X O   
41368 C  CB  . THR   X  53  ? 1.7678 0.5103 1.2021 0.0772  -0.3687 -0.1061 53  THR   X CB  
41369 O  OG1 . THR   X  53  ? 1.7720 0.4069 1.3182 0.1098  -0.3201 -0.1421 53  THR   X OG1 
41370 C  CG2 . THR   X  53  ? 1.7666 0.5532 1.1803 0.0901  -0.3672 -0.1196 53  THR   X CG2 
41371 N  N   . VAL   X  54  ? 1.6711 0.5006 1.0816 -0.0029 -0.3630 -0.1149 54  VAL   X N   
41372 C  CA  . VAL   X  54  ? 1.6521 0.5761 1.0595 0.0023  -0.3276 -0.1235 54  VAL   X CA  
41373 C  C   . VAL   X  54  ? 1.6480 0.6075 1.0639 0.0329  -0.3350 -0.0964 54  VAL   X C   
41374 O  O   . VAL   X  54  ? 1.6377 0.6018 1.0430 0.0680  -0.3454 -0.0976 54  VAL   X O   
41375 C  CB  . VAL   X  54  ? 1.6673 0.6109 1.0729 -0.0170 -0.3116 -0.1219 54  VAL   X CB  
41376 C  CG1 . VAL   X  54  ? 1.6499 0.6512 1.0766 -0.0273 -0.2847 -0.1360 54  VAL   X CG1 
41377 C  CG2 . VAL   X  54  ? 1.6816 0.6040 1.0756 -0.0147 -0.2960 -0.1257 54  VAL   X CG2 
41378 N  N   . GLN   X  55  ? 1.6371 0.5849 1.0713 0.0519  -0.3379 -0.0898 55  GLN   X N   
41379 C  CA  . GLN   X  55  ? 1.6374 0.5280 1.1366 0.0494  -0.3222 -0.1031 55  GLN   X CA  
41380 C  C   . GLN   X  55  ? 1.6624 0.4897 1.1408 0.0335  -0.3398 -0.0808 55  GLN   X C   
41381 O  O   . GLN   X  55  ? 1.6764 0.5063 1.2095 -0.0415 -0.3729 -0.0937 55  GLN   X O   
41382 C  CB  . GLN   X  55  ? 1.6365 0.5447 1.1119 0.0793  -0.3130 -0.0704 55  GLN   X CB  
41383 C  CG  . GLN   X  55  ? 1.6385 0.5872 1.1454 0.0775  -0.2882 -0.0503 55  GLN   X CG  
41384 C  CD  . GLN   X  55  ? 1.6280 0.5795 1.1699 0.0709  -0.2748 -0.0291 55  GLN   X CD  
41385 O  OE1 . GLN   X  55  ? 1.6236 0.5904 1.1800 0.1497  -0.2734 0.0327  55  GLN   X OE1 
41386 N  NE2 . GLN   X  55  ? 1.6427 0.5674 1.1967 0.0661  -0.2680 -0.0715 55  GLN   X NE2 
41387 N  N   . PHE   X  56  ? 1.6821 0.3978 1.1355 0.0077  -0.3442 -0.0912 56  PHE   X N   
41388 C  CA  . PHE   X  56  ? 1.7196 0.3263 1.1600 -0.0360 -0.3392 -0.0533 56  PHE   X CA  
41389 C  C   . PHE   X  56  ? 1.7492 0.3279 1.1651 -0.0398 -0.3337 -0.0477 56  PHE   X C   
41390 O  O   . PHE   X  56  ? 1.7585 0.3535 1.2469 -0.0805 -0.2866 0.0475  56  PHE   X O   
41391 C  CB  . PHE   X  56  ? 1.6850 0.3586 1.1015 -0.0345 -0.3529 -0.0473 56  PHE   X CB  
41392 C  CG  . PHE   X  56  ? 1.6920 0.3249 1.0961 -0.0423 -0.3563 -0.0174 56  PHE   X CG  
41393 C  CD1 . PHE   X  56  ? 1.7151 0.3094 1.0799 -0.0026 -0.3662 -0.0098 56  PHE   X CD1 
41394 C  CD2 . PHE   X  56  ? 1.7305 0.3800 1.1193 -0.0354 -0.3584 0.0373  56  PHE   X CD2 
41395 C  CE1 . PHE   X  56  ? 1.7124 0.3595 1.1077 0.0132  -0.3446 0.0066  56  PHE   X CE1 
41396 C  CE2 . PHE   X  56  ? 1.7369 0.3967 1.1420 -0.0300 -0.3442 0.0659  56  PHE   X CE2 
41397 C  CZ  . PHE   X  56  ? 1.7429 0.3868 1.1109 -0.0007 -0.3413 0.0533  56  PHE   X CZ  
41398 N  N   . ALA   X  57  ? 1.7854 0.3753 1.1645 -0.0522 -0.3131 -0.0427 57  ALA   X N   
41399 C  CA  . ALA   X  57  ? 1.7752 0.4269 1.1953 -0.0522 -0.3307 -0.0938 57  ALA   X CA  
41400 C  C   . ALA   X  57  ? 1.7454 0.4168 1.2039 -0.0647 -0.3400 -0.0943 57  ALA   X C   
41401 O  O   . ALA   X  57  ? 1.7173 0.4361 1.2397 -0.0518 -0.3422 -0.1168 57  ALA   X O   
41402 C  CB  . ALA   X  57  ? 1.7970 0.4544 1.2031 -0.0477 -0.3129 -0.0778 57  ALA   X CB  
41403 N  N   . GLU   X  58  ? 1.7380 0.4494 1.1777 -0.0645 -0.3464 -0.1011 58  GLU   X N   
41404 C  CA  . GLU   X  58  ? 1.7061 0.5371 1.1783 -0.0296 -0.3236 -0.1293 58  GLU   X CA  
41405 C  C   . GLU   X  58  ? 1.7010 0.5124 1.1843 -0.0108 -0.3241 -0.1384 58  GLU   X C   
41406 O  O   . GLU   X  58  ? 1.6675 0.4699 1.2660 0.0012  -0.3076 -0.1262 58  GLU   X O   
41407 C  CB  . GLU   X  58  ? 1.7128 0.6272 1.1912 -0.0675 -0.3110 -0.1202 58  GLU   X CB  
41408 C  CG  . GLU   X  58  ? 1.7770 0.7140 1.1905 -0.0612 -0.2684 -0.0983 58  GLU   X CG  
41409 C  CD  . GLU   X  58  ? 1.7809 0.8251 1.2558 -0.0432 -0.2223 -0.0683 58  GLU   X CD  
41410 O  OE1 . GLU   X  58  ? 1.7993 0.9113 1.3181 0.0391  -0.1881 -0.0401 58  GLU   X OE1 
41411 O  OE2 . GLU   X  58  ? 1.8583 0.8351 1.2754 -0.0390 -0.2310 -0.0223 58  GLU   X OE2 
41412 N  N   . TYR   X  59  ? 1.7038 0.5138 1.1903 -0.0006 -0.2976 -0.1237 59  TYR   X N   
41413 C  CA  . TYR   X  59  ? 1.6989 0.4629 1.2555 -0.0079 -0.3232 -0.1078 59  TYR   X CA  
41414 C  C   . TYR   X  59  ? 1.7127 0.5158 1.2227 -0.0196 -0.3483 -0.1037 59  TYR   X C   
41415 O  O   . TYR   X  59  ? 1.7203 0.5213 1.3061 -0.0325 -0.3680 -0.0194 59  TYR   X O   
41416 C  CB  . TYR   X  59  ? 1.7211 0.4671 1.2230 0.0093  -0.2810 -0.0464 59  TYR   X CB  
41417 C  CG  . TYR   X  59  ? 1.7327 0.5144 1.2656 -0.0116 -0.2687 -0.0257 59  TYR   X CG  
41418 C  CD1 . TYR   X  59  ? 1.6927 0.5269 1.2777 0.0183  -0.2657 -0.0579 59  TYR   X CD1 
41419 C  CD2 . TYR   X  59  ? 1.7221 0.4846 1.3129 0.0088  -0.2690 0.0368  59  TYR   X CD2 
41420 C  CE1 . TYR   X  59  ? 1.6952 0.5708 1.3182 -0.0204 -0.2771 -0.0405 59  TYR   X CE1 
41421 C  CE2 . TYR   X  59  ? 1.7087 0.5561 1.3381 -0.0367 -0.2520 0.0167  59  TYR   X CE2 
41422 C  CZ  . TYR   X  59  ? 1.6903 0.5535 1.3303 -0.0439 -0.2451 0.0110  59  TYR   X CZ  
41423 O  OH  . TYR   X  59  ? 1.7495 0.5057 1.3502 -0.0123 -0.2721 0.0849  59  TYR   X OH  
41424 N  N   . ILE   X  60  ? 1.7093 0.4368 1.1573 -0.0518 -0.3598 -0.1536 60  ILE   X N   
41425 C  CA  . ILE   X  60  ? 1.7211 0.4735 1.1160 -0.0561 -0.3575 -0.1494 60  ILE   X CA  
41426 C  C   . ILE   X  60  ? 1.7213 0.5318 1.0921 -0.0546 -0.3689 -0.1499 60  ILE   X C   
41427 O  O   . ILE   X  60  ? 1.7333 0.5817 1.0013 -0.0547 -0.4379 -0.2155 60  ILE   X O   
41428 C  CB  . ILE   X  60  ? 1.7179 0.4772 1.0823 -0.0629 -0.3625 -0.1072 60  ILE   X CB  
41429 C  CG1 . ILE   X  60  ? 1.7427 0.5613 1.0659 -0.0707 -0.3533 -0.1076 60  ILE   X CG1 
41430 C  CG2 . ILE   X  60  ? 1.7148 0.4282 1.0727 -0.0724 -0.3638 -0.0867 60  ILE   X CG2 
41431 C  CD1 . ILE   X  60  ? 1.7605 0.5707 1.0956 -0.0958 -0.3301 -0.1187 60  ILE   X CD1 
41432 N  N   . GLN   X  61  ? 1.7044 0.5282 1.0240 -0.0503 -0.3737 -0.1968 61  GLN   X N   
41433 C  CA  . GLN   X  61  ? 1.6840 0.5696 1.0407 -0.0551 -0.3907 -0.2359 61  GLN   X CA  
41434 C  C   . GLN   X  61  ? 1.6852 0.6033 1.0434 -0.0048 -0.3760 -0.1882 61  GLN   X C   
41435 O  O   . GLN   X  61  ? 1.6804 0.5913 1.0429 0.0130  -0.3734 -0.1913 61  GLN   X O   
41436 C  CB  . GLN   X  61  ? 1.6656 0.5874 1.0406 -0.0792 -0.3898 -0.2892 61  GLN   X CB  
41437 C  CG  . GLN   X  61  ? 1.6601 0.6160 1.0520 -0.0907 -0.4259 -0.3389 61  GLN   X CG  
41438 C  CD  . GLN   X  61  ? 1.6514 0.6277 1.0387 -0.0789 -0.4196 -0.3501 61  GLN   X CD  
41439 O  OE1 . GLN   X  61  ? 1.5961 0.7881 1.1564 -0.0384 -0.4179 -0.3651 61  GLN   X OE1 
41440 N  NE2 . GLN   X  61  ? 1.6350 0.5702 1.0167 -0.0986 -0.4720 -0.4217 61  GLN   X NE2 
41441 N  N   . ALA   X  62  ? 1.6758 0.5789 1.0672 0.0169  -0.3659 -0.1656 62  ALA   X N   
41442 C  CA  . ALA   X  62  ? 1.7114 0.5637 1.1056 0.0061  -0.3562 -0.1496 62  ALA   X CA  
41443 C  C   . ALA   X  62  ? 1.7070 0.5225 1.1522 0.0320  -0.3448 -0.1497 62  ALA   X C   
41444 O  O   . ALA   X  62  ? 1.7576 0.5469 1.1457 0.0522  -0.3730 -0.1730 62  ALA   X O   
41445 C  CB  . ALA   X  62  ? 1.7012 0.5364 1.1171 0.0277  -0.3586 -0.0940 62  ALA   X CB  
41446 N  N   . ASN   X  63  ? 1.7098 0.4989 1.1993 0.0526  -0.3383 -0.1670 63  ASN   X N   
41447 C  CA  . ASN   X  63  ? 1.7074 0.4939 1.2192 0.0626  -0.3370 -0.1506 63  ASN   X CA  
41448 C  C   . ASN   X  63  ? 1.7029 0.4861 1.1903 0.0774  -0.3214 -0.1664 63  ASN   X C   
41449 O  O   . ASN   X  63  ? 1.7425 0.4905 1.1569 0.0598  -0.2963 -0.1818 63  ASN   X O   
41450 C  CB  . ASN   X  63  ? 1.7081 0.4614 1.2252 0.0482  -0.3473 -0.1570 63  ASN   X CB  
41451 C  CG  . ASN   X  63  ? 1.7097 0.4377 1.2731 0.0502  -0.3747 -0.1252 63  ASN   X CG  
41452 O  OD1 . ASN   X  63  ? 1.7008 0.3936 1.3331 0.0512  -0.3982 -0.1020 63  ASN   X OD1 
41453 N  ND2 . ASN   X  63  ? 1.7251 0.4376 1.3139 0.0310  -0.3726 -0.1261 63  ASN   X ND2 
41454 N  N   . ILE   X  64  ? 1.6669 0.5778 1.1923 0.1021  -0.3404 -0.1319 64  ILE   X N   
41455 C  CA  . ILE   X  64  ? 1.6652 0.6259 1.2200 0.0817  -0.3572 -0.0988 64  ILE   X CA  
41456 C  C   . ILE   X  64  ? 1.6705 0.6379 1.2380 0.0923  -0.3826 -0.1236 64  ILE   X C   
41457 O  O   . ILE   X  64  ? 1.6243 0.7372 1.2647 0.0742  -0.3989 -0.1467 64  ILE   X O   
41458 C  CB  . ILE   X  64  ? 1.6855 0.6662 1.2104 0.0256  -0.3397 -0.0019 64  ILE   X CB  
41459 C  CG1 . ILE   X  64  ? 1.6764 0.6444 1.2020 0.0181  -0.3217 0.0293  64  ILE   X CG1 
41460 C  CG2 . ILE   X  64  ? 1.7012 0.6886 1.2120 0.0081  -0.3427 0.0034  64  ILE   X CG2 
41461 C  CD1 . ILE   X  64  ? 1.6832 0.7068 1.2245 0.0300  -0.3043 0.0572  64  ILE   X CD1 
41462 N  N   . GLN   X  65  ? 1.6799 0.6020 1.2321 0.0759  -0.3796 -0.1251 65  GLN   X N   
41463 C  CA  . GLN   X  65  ? 1.7428 0.5855 1.2410 0.0705  -0.3730 -0.1362 65  GLN   X CA  
41464 C  C   . GLN   X  65  ? 1.7899 0.5442 1.2854 0.0377  -0.3605 -0.1705 65  GLN   X C   
41465 O  O   . GLN   X  65  ? 1.8224 0.3896 1.4430 0.0159  -0.3673 -0.1547 65  GLN   X O   
41466 C  CB  . GLN   X  65  ? 1.7415 0.5712 1.2160 0.0718  -0.3898 -0.1333 65  GLN   X CB  
41467 C  CG  . GLN   X  65  ? 1.7639 0.5698 1.1718 0.1081  -0.4330 -0.1501 65  GLN   X CG  
41468 C  CD  . GLN   X  65  ? 1.7570 0.5629 1.1300 0.1217  -0.4436 -0.1501 65  GLN   X CD  
41469 O  OE1 . GLN   X  65  ? 1.7625 0.6085 1.1511 0.1574  -0.4608 -0.2194 65  GLN   X OE1 
41470 N  NE2 . GLN   X  65  ? 1.7735 0.5574 1.1053 0.0936  -0.4301 -0.1615 65  GLN   X NE2 
41471 N  N   . LEU   X  66  ? 1.8116 0.5326 1.2949 0.0439  -0.3375 -0.1107 66  LEU   X N   
41472 C  CA  . LEU   X  66  ? 1.8138 0.5122 1.3185 0.0303  -0.3194 -0.1216 66  LEU   X CA  
41473 C  C   . LEU   X  66  ? 1.8220 0.4676 1.3223 0.0224  -0.2919 -0.1098 66  LEU   X C   
41474 O  O   . LEU   X  66  ? 1.8893 0.4404 1.4513 0.0072  -0.2880 -0.0682 66  LEU   X O   
41475 C  CB  . LEU   X  66  ? 1.8195 0.5082 1.3030 0.0449  -0.3116 -0.0869 66  LEU   X CB  
41476 C  CG  . LEU   X  66  ? 1.8265 0.5162 1.3048 0.0364  -0.3116 -0.0773 66  LEU   X CG  
41477 C  CD1 . LEU   X  66  ? 1.8147 0.5895 1.3162 0.0601  -0.3045 -0.0769 66  LEU   X CD1 
41478 C  CD2 . LEU   X  66  ? 1.8159 0.4815 1.3043 0.0446  -0.3157 -0.0657 66  LEU   X CD2 
41479 N  N   . TYR   X  67  ? 1.8053 0.4726 1.2499 0.0102  -0.2736 -0.0984 67  TYR   X N   
41480 C  CA  . TYR   X  67  ? 1.7975 0.4967 1.2329 0.0168  -0.2722 -0.0544 67  TYR   X CA  
41481 C  C   . TYR   X  67  ? 1.8336 0.5585 1.2352 0.0405  -0.2621 -0.0719 67  TYR   X C   
41482 O  O   . TYR   X  67  ? 1.8628 0.5647 1.2830 -0.0097 -0.2200 0.0084  67  TYR   X O   
41483 C  CB  . TYR   X  67  ? 1.7646 0.5144 1.2002 0.0246  -0.2849 -0.0115 67  TYR   X CB  
41484 C  CG  . TYR   X  67  ? 1.7896 0.5001 1.2256 -0.0051 -0.2848 0.0175  67  TYR   X CG  
41485 C  CD1 . TYR   X  67  ? 1.7797 0.5079 1.2336 -0.0129 -0.2929 0.0437  67  TYR   X CD1 
41486 C  CD2 . TYR   X  67  ? 1.7627 0.5272 1.2355 -0.0221 -0.2825 0.0215  67  TYR   X CD2 
41487 C  CE1 . TYR   X  67  ? 1.7679 0.5341 1.2725 -0.0029 -0.2972 0.0546  67  TYR   X CE1 
41488 C  CE2 . TYR   X  67  ? 1.7598 0.5832 1.2645 -0.0312 -0.2758 0.0223  67  TYR   X CE2 
41489 C  CZ  . TYR   X  67  ? 1.7562 0.5999 1.2784 -0.0149 -0.2882 0.0329  67  TYR   X CZ  
41490 O  OH  . TYR   X  67  ? 1.7497 0.6544 1.3396 -0.0118 -0.2761 0.0217  67  TYR   X OH  
41491 N  N   . SER   X  68  ? 1.8423 0.6071 1.1714 0.0405  -0.2557 -0.0960 68  SER   X N   
41492 C  CA  . SER   X  68  ? 1.8724 0.6929 1.1871 0.0154  -0.2817 -0.1464 68  SER   X CA  
41493 C  C   . SER   X  68  ? 1.8769 0.7162 1.2102 -0.0109 -0.2763 -0.2342 68  SER   X C   
41494 O  O   . SER   X  68  ? 1.9260 0.7170 1.2592 -0.0242 -0.2645 -0.2749 68  SER   X O   
41495 C  CB  . SER   X  68  ? 1.9111 0.7571 1.0915 0.0019  -0.2954 -0.1289 68  SER   X CB  
41496 O  OG  . SER   X  68  ? 1.8941 0.8310 1.0277 0.0440  -0.3053 -0.1122 68  SER   X OG  
41497 N  N   . ILE   X  69  ? 1.8571 0.6870 1.2414 -0.0093 -0.2559 -0.2551 69  ILE   X N   
41498 C  CA  . ILE   X  69  ? 1.9014 0.6445 1.3059 -0.0165 -0.2601 -0.2534 69  ILE   X CA  
41499 C  C   . ILE   X  69  ? 1.8913 0.6255 1.3441 -0.0197 -0.2436 -0.2813 69  ILE   X C   
41500 O  O   . ILE   X  69  ? 1.9895 0.6474 1.4709 -0.0482 -0.2402 -0.3342 69  ILE   X O   
41501 C  CB  . ILE   X  69  ? 1.8864 0.6545 1.3632 -0.0016 -0.2277 -0.2267 69  ILE   X CB  
41502 C  CG1 . ILE   X  69  ? 1.8886 0.7286 1.3468 0.0074  -0.2118 -0.2264 69  ILE   X CG1 
41503 C  CG2 . ILE   X  69  ? 1.9182 0.6607 1.4297 0.0096  -0.2088 -0.2203 69  ILE   X CG2 
41504 C  CD1 . ILE   X  69  ? 1.8830 0.7058 1.3914 -0.0032 -0.2287 -0.2696 69  ILE   X CD1 
41505 N  N   . ARG   X  70  ? 1.8672 0.5901 1.3470 -0.0361 -0.2461 -0.2954 70  ARG   X N   
41506 C  CA  . ARG   X  70  ? 1.8674 0.5694 1.4454 -0.0530 -0.2498 -0.2739 70  ARG   X CA  
41507 C  C   . ARG   X  70  ? 1.8685 0.5268 1.4065 -0.0298 -0.2543 -0.2886 70  ARG   X C   
41508 O  O   . ARG   X  70  ? 1.8957 0.5597 1.4813 -0.0962 -0.2512 -0.3467 70  ARG   X O   
41509 C  CB  . ARG   X  70  ? 1.8602 0.6078 1.4154 -0.0639 -0.2178 -0.1817 70  ARG   X CB  
41510 C  CG  . ARG   X  70  ? 1.8716 0.6830 1.4771 -0.0634 -0.2102 -0.1150 70  ARG   X CG  
41511 C  CD  . ARG   X  70  ? 1.8439 0.6872 1.4622 -0.0269 -0.2078 -0.0714 70  ARG   X CD  
41512 N  NE  . ARG   X  70  ? 1.8415 0.6165 1.4671 0.0005  -0.2222 -0.0493 70  ARG   X NE  
41513 C  CZ  . ARG   X  70  ? 1.8343 0.6024 1.4568 0.0348  -0.1990 -0.0383 70  ARG   X CZ  
41514 N  NH1 . ARG   X  70  ? 1.8009 0.7475 1.4707 0.0837  -0.1812 0.0016  70  ARG   X NH1 
41515 N  NH2 . ARG   X  70  ? 1.8158 0.6463 1.4775 0.0624  -0.2192 0.0234  70  ARG   X NH2 
41516 N  N   . GLU   X  71  ? 1.8805 0.4806 1.3841 -0.0504 -0.2843 -0.2889 71  GLU   X N   
41517 C  CA  . GLU   X  71  ? 1.8900 0.4581 1.4627 -0.0588 -0.3094 -0.2379 71  GLU   X CA  
41518 C  C   . GLU   X  71  ? 1.9191 0.4335 1.4675 -0.0419 -0.2757 -0.1941 71  GLU   X C   
41519 O  O   . GLU   X  71  ? 1.9315 0.3193 1.5182 -0.0603 -0.2867 -0.1629 71  GLU   X O   
41520 C  CB  . GLU   X  71  ? 1.8448 0.5265 1.4439 -0.0334 -0.3408 -0.2227 71  GLU   X CB  
41521 C  CG  . GLU   X  71  ? 1.8374 0.5808 1.4483 -0.0374 -0.3733 -0.1797 71  GLU   X CG  
41522 C  CD  . GLU   X  71  ? 1.8495 0.5342 1.5119 -0.0371 -0.4082 -0.1917 71  GLU   X CD  
41523 O  OE1 . GLU   X  71  ? 1.8943 0.6997 1.5251 0.0598  -0.4210 -0.0967 71  GLU   X OE1 
41524 O  OE2 . GLU   X  71  ? 1.9179 0.5174 1.5360 0.0157  -0.4329 -0.2665 71  GLU   X OE2 
41525 N  N   . ASP   X  72  ? 1.9310 0.4971 1.4802 -0.0222 -0.2475 -0.1809 72  ASP   X N   
41526 C  CA  . ASP   X  72  ? 1.9341 0.5587 1.4713 -0.0092 -0.2406 -0.1915 72  ASP   X CA  
41527 C  C   . ASP   X  72  ? 1.9433 0.6036 1.3955 0.0063  -0.2692 -0.2180 72  ASP   X C   
41528 O  O   . ASP   X  72  ? 1.9488 0.5786 1.4099 -0.0082 -0.2488 -0.2537 72  ASP   X O   
41529 C  CB  . ASP   X  72  ? 1.9438 0.5422 1.5436 -0.0203 -0.2206 -0.1943 72  ASP   X CB  
41530 C  CG  . ASP   X  72  ? 1.9508 0.5778 1.5741 -0.0490 -0.1815 -0.1286 72  ASP   X CG  
41531 O  OD1 . ASP   X  72  ? 2.0128 0.4540 1.6009 -0.0165 -0.1712 -0.1169 72  ASP   X OD1 
41532 O  OD2 . ASP   X  72  ? 1.9407 0.7468 1.6228 -0.0873 -0.2199 -0.1516 72  ASP   X OD2 
41533 N  N   . TYR   X  73  ? 1.9232 0.6009 1.3708 0.0334  -0.3176 -0.2106 73  TYR   X N   
41534 C  CA  . TYR   X  73  ? 1.9654 0.6325 1.3603 0.0736  -0.4009 -0.2242 73  TYR   X CA  
41535 C  C   . TYR   X  73  ? 1.9795 0.6338 1.3390 0.1086  -0.3773 -0.2449 73  TYR   X C   
41536 O  O   . TYR   X  73  ? 2.0109 0.7599 1.3100 0.1534  -0.3608 -0.3153 73  TYR   X O   
41537 C  CB  . TYR   X  73  ? 1.9233 0.6233 1.3778 0.1237  -0.4225 -0.1899 73  TYR   X CB  
41538 C  CG  . TYR   X  73  ? 1.9790 0.5577 1.4209 0.1985  -0.4437 -0.2029 73  TYR   X CG  
41539 C  CD1 . TYR   X  73  ? 2.0080 0.6244 1.4547 0.2104  -0.4733 -0.2259 73  TYR   X CD1 
41540 C  CD2 . TYR   X  73  ? 1.9765 0.4491 1.4276 0.2172  -0.4868 -0.1939 73  TYR   X CD2 
41541 C  CE1 . TYR   X  73  ? 2.0138 0.6061 1.4787 0.2220  -0.4894 -0.2593 73  TYR   X CE1 
41542 C  CE2 . TYR   X  73  ? 1.9629 0.5154 1.4706 0.2289  -0.4735 -0.2412 73  TYR   X CE2 
41543 C  CZ  . TYR   X  73  ? 1.9691 0.5688 1.5093 0.2227  -0.5065 -0.2631 73  TYR   X CZ  
41544 O  OH  . TYR   X  73  ? 1.9299 0.6656 1.5536 0.1991  -0.5062 -0.3499 73  TYR   X OH  
41545 N  N   . GLU   X  74  ? 1.9972 0.6390 1.2607 0.0871  -0.4138 -0.2584 74  GLU   X N   
41546 C  CA  . GLU   X  74  ? 2.0116 0.6460 1.1475 0.0152  -0.4137 -0.2455 74  GLU   X CA  
41547 C  C   . GLU   X  74  ? 2.0135 0.5507 1.1131 -0.0052 -0.4280 -0.2585 74  GLU   X C   
41548 O  O   . GLU   X  74  ? 2.0222 0.4408 1.0578 0.0419  -0.4419 -0.3304 74  GLU   X O   
41549 C  CB  . GLU   X  74  ? 2.0471 0.6672 1.1238 -0.0251 -0.4111 -0.2532 74  GLU   X CB  
41550 C  CG  . GLU   X  74  ? 2.0557 0.6493 1.1256 -0.0152 -0.4014 -0.1994 74  GLU   X CG  
41551 C  CD  . GLU   X  74  ? 2.1022 0.6443 1.1478 0.0012  -0.4002 -0.1803 74  GLU   X CD  
41552 O  OE1 . GLU   X  74  ? 2.1063 0.6177 1.1966 0.0108  -0.3903 -0.1118 74  GLU   X OE1 
41553 O  OE2 . GLU   X  74  ? 2.1312 0.4292 1.1682 -0.0115 -0.3757 -0.1945 74  GLU   X OE2 
41554 N  N   . LEU   X  75  ? 1.9693 0.5801 1.0652 -0.0270 -0.3969 -0.2139 75  LEU   X N   
41555 C  CA  . LEU   X  75  ? 1.9103 0.6835 1.0353 -0.0287 -0.4211 -0.2192 75  LEU   X CA  
41556 C  C   . LEU   X  75  ? 1.8415 0.7325 0.9465 -0.0034 -0.4429 -0.2573 75  LEU   X C   
41557 O  O   . LEU   X  75  ? 1.8534 0.6531 0.8723 0.0513  -0.4241 -0.2926 75  LEU   X O   
41558 C  CB  . LEU   X  75  ? 1.8858 0.7525 1.0758 -0.0561 -0.4411 -0.2147 75  LEU   X CB  
41559 C  CG  . LEU   X  75  ? 1.9023 0.7736 1.1452 -0.0783 -0.4302 -0.1591 75  LEU   X CG  
41560 C  CD1 . LEU   X  75  ? 1.9163 0.8157 1.1784 -0.1170 -0.4500 -0.2208 75  LEU   X CD1 
41561 C  CD2 . LEU   X  75  ? 1.8806 0.8539 1.1873 -0.0563 -0.4214 -0.1185 75  LEU   X CD2 
41562 N  N   . SER   X  76  ? 1.8124 0.7311 0.9554 -0.0182 -0.4895 -0.2686 76  SER   X N   
41563 C  CA  . SER   X  76  ? 1.8113 0.7220 1.0108 -0.0411 -0.5067 -0.2319 76  SER   X CA  
41564 C  C   . SER   X  76  ? 1.8018 0.6656 1.0294 -0.0491 -0.4979 -0.1664 76  SER   X C   
41565 O  O   . SER   X  76  ? 1.7119 0.6652 1.0577 -0.0010 -0.4833 -0.0389 76  SER   X O   
41566 C  CB  . SER   X  76  ? 1.7840 0.7552 1.0038 -0.0554 -0.5599 -0.2565 76  SER   X CB  
41567 O  OG  . SER   X  76  ? 1.7572 0.7589 0.9755 -0.1056 -0.6442 -0.2581 76  SER   X OG  
41568 N  N   . PRO   X  77  ? 1.8559 0.6485 1.0755 -0.0423 -0.4873 -0.1648 77  PRO   X N   
41569 C  CA  . PRO   X  77  ? 1.8215 0.5933 1.1068 -0.0042 -0.4697 -0.1491 77  PRO   X CA  
41570 C  C   . PRO   X  77  ? 1.7655 0.5102 1.1425 -0.0417 -0.4546 -0.1971 77  PRO   X C   
41571 O  O   . PRO   X  77  ? 1.7131 0.6041 1.2230 -0.0799 -0.4574 -0.2278 77  PRO   X O   
41572 C  CB  . PRO   X  77  ? 1.8369 0.6073 1.1063 0.0079  -0.4898 -0.1533 77  PRO   X CB  
41573 C  CG  . PRO   X  77  ? 1.8544 0.6263 1.1013 0.0100  -0.5244 -0.1530 77  PRO   X CG  
41574 C  CD  . PRO   X  77  ? 1.8640 0.6353 1.1021 -0.0182 -0.5267 -0.1614 77  PRO   X CD  
41575 N  N   . GLN   X  78  ? 1.7793 0.4475 1.2369 -0.0365 -0.4233 -0.1656 78  GLN   X N   
41576 C  CA  . GLN   X  78  ? 1.7615 0.4536 1.2242 -0.0610 -0.4389 -0.1426 78  GLN   X CA  
41577 C  C   . GLN   X  78  ? 1.7286 0.4389 1.1729 -0.0966 -0.4446 -0.1655 78  GLN   X C   
41578 O  O   . GLN   X  78  ? 1.6696 0.3216 1.1461 -0.0914 -0.4248 -0.1215 78  GLN   X O   
41579 C  CB  . GLN   X  78  ? 1.7753 0.4805 1.2817 -0.0836 -0.4386 -0.1263 78  GLN   X CB  
41580 C  CG  . GLN   X  78  ? 1.8031 0.4949 1.2459 -0.0912 -0.4400 -0.1213 78  GLN   X CG  
41581 C  CD  . GLN   X  78  ? 1.8110 0.5432 1.2331 -0.1001 -0.4222 -0.1103 78  GLN   X CD  
41582 O  OE1 . GLN   X  78  ? 1.8281 0.5609 1.2059 -0.0782 -0.4215 -0.0985 78  GLN   X OE1 
41583 N  NE2 . GLN   X  78  ? 1.7946 0.5467 1.2306 -0.1218 -0.4258 -0.1209 78  GLN   X NE2 
41584 N  N   . ALA   X  79  ? 1.7338 0.4674 1.2040 -0.0627 -0.4455 -0.1817 79  ALA   X N   
41585 C  CA  . ALA   X  79  ? 1.6729 0.5627 1.1776 -0.0728 -0.4641 -0.1745 79  ALA   X CA  
41586 C  C   . ALA   X  79  ? 1.6872 0.4991 1.1344 -0.1011 -0.4300 -0.1940 79  ALA   X C   
41587 O  O   . ALA   X  79  ? 1.6388 0.4669 1.1472 -0.1441 -0.4444 -0.1789 79  ALA   X O   
41588 C  CB  . ALA   X  79  ? 1.7085 0.5942 1.2071 -0.0465 -0.4499 -0.2030 79  ALA   X CB  
41589 N  N   . VAL   X  80  ? 1.6648 0.4733 1.1316 -0.1002 -0.4307 -0.2034 80  VAL   X N   
41590 C  CA  . VAL   X  80  ? 1.6315 0.5332 1.1587 -0.0830 -0.4169 -0.1336 80  VAL   X CA  
41591 C  C   . VAL   X  80  ? 1.6368 0.5293 1.1372 -0.0528 -0.3967 -0.1075 80  VAL   X C   
41592 O  O   . VAL   X  80  ? 1.5793 0.5262 1.1464 -0.0245 -0.3927 -0.0451 80  VAL   X O   
41593 C  CB  . VAL   X  80  ? 1.6603 0.5222 1.1418 -0.0822 -0.4181 -0.1589 80  VAL   X CB  
41594 C  CG1 . VAL   X  80  ? 1.6481 0.5142 1.1721 -0.0780 -0.4114 -0.1303 80  VAL   X CG1 
41595 C  CG2 . VAL   X  80  ? 1.6830 0.5660 1.1633 -0.0741 -0.3990 -0.1832 80  VAL   X CG2 
41596 N  N   . SER   X  81  ? 1.6493 0.5606 1.1673 -0.0381 -0.3884 -0.0908 81  SER   X N   
41597 C  CA  . SER   X  81  ? 1.6827 0.5835 1.1779 -0.1139 -0.4042 -0.1423 81  SER   X CA  
41598 C  C   . SER   X  81  ? 1.7073 0.5398 1.2070 -0.1207 -0.3911 -0.1075 81  SER   X C   
41599 O  O   . SER   X  81  ? 1.7360 0.5812 1.2400 -0.2063 -0.4183 -0.0678 81  SER   X O   
41600 C  CB  . SER   X  81  ? 1.6941 0.6456 1.2016 -0.0918 -0.4150 -0.1440 81  SER   X CB  
41601 O  OG  . SER   X  81  ? 1.7246 0.7031 1.2759 -0.1003 -0.3509 -0.1351 81  SER   X OG  
41602 N  N   . SER   X  82  ? 1.6790 0.5154 1.1996 -0.0979 -0.3990 -0.1238 82  SER   X N   
41603 C  CA  . SER   X  82  ? 1.6435 0.5298 1.1813 -0.0512 -0.4126 -0.1276 82  SER   X CA  
41604 C  C   . SER   X  82  ? 1.6315 0.4892 1.1456 -0.0499 -0.4074 -0.1645 82  SER   X C   
41605 O  O   . SER   X  82  ? 1.5920 0.4968 1.1571 -0.0399 -0.3976 -0.2215 82  SER   X O   
41606 C  CB  . SER   X  82  ? 1.6368 0.5260 1.2050 -0.0454 -0.3991 -0.1144 82  SER   X CB  
41607 O  OG  . SER   X  82  ? 1.6327 0.5922 1.2445 -0.0300 -0.4037 -0.1090 82  SER   X OG  
41608 N  N   . PHE   X  83  ? 1.6077 0.4689 1.1702 -0.0392 -0.4145 -0.1414 83  PHE   X N   
41609 C  CA  . PHE   X  83  ? 1.6275 0.4448 1.1728 -0.0403 -0.4162 -0.0916 83  PHE   X CA  
41610 C  C   . PHE   X  83  ? 1.6185 0.4171 1.1280 -0.0264 -0.4068 -0.0664 83  PHE   X C   
41611 O  O   . PHE   X  83  ? 1.6050 0.4460 1.1411 0.0412  -0.4231 -0.0100 83  PHE   X O   
41612 C  CB  . PHE   X  83  ? 1.5960 0.3288 1.2024 -0.0736 -0.4398 -0.0969 83  PHE   X CB  
41613 C  CG  . PHE   X  83  ? 1.5865 0.2527 1.2185 -0.1078 -0.4511 -0.0834 83  PHE   X CG  
41614 C  CD1 . PHE   X  83  ? 1.5977 0.2853 1.2311 -0.1153 -0.4441 -0.0557 83  PHE   X CD1 
41615 C  CD2 . PHE   X  83  ? 1.6021 0.2130 1.2445 -0.1173 -0.4570 -0.0607 83  PHE   X CD2 
41616 C  CE1 . PHE   X  83  ? 1.6034 0.2835 1.2392 -0.1183 -0.4426 -0.0142 83  PHE   X CE1 
41617 C  CE2 . PHE   X  83  ? 1.5963 0.2461 1.2667 -0.1141 -0.4438 -0.0512 83  PHE   X CE2 
41618 C  CZ  . PHE   X  83  ? 1.5917 0.2807 1.2630 -0.1212 -0.4407 -0.0346 83  PHE   X CZ  
41619 N  N   . VAL   X  84  ? 1.6786 0.4453 1.1350 0.0148  -0.3447 -0.0492 84  VAL   X N   
41620 C  CA  . VAL   X  84  ? 1.6674 0.4710 1.1087 0.0005  -0.3433 -0.0157 84  VAL   X CA  
41621 C  C   . VAL   X  84  ? 1.6681 0.4979 1.0890 0.0025  -0.3560 -0.0178 84  VAL   X C   
41622 O  O   . VAL   X  84  ? 1.6459 0.4869 1.1121 -0.0063 -0.3523 -0.0231 84  VAL   X O   
41623 C  CB  . VAL   X  84  ? 1.6885 0.4905 1.1206 0.0309  -0.3252 0.0024  84  VAL   X CB  
41624 C  CG1 . VAL   X  84  ? 1.6837 0.4800 1.1013 0.0449  -0.3224 -0.0171 84  VAL   X CG1 
41625 C  CG2 . VAL   X  84  ? 1.7130 0.4633 1.1291 0.0418  -0.3137 0.0141  84  VAL   X CG2 
41626 N  N   . ARG   X  85  ? 1.6671 0.4850 1.0903 0.0054  -0.3704 0.0107  85  ARG   X N   
41627 C  CA  . ARG   X  85  ? 1.6696 0.4613 1.1164 0.0091  -0.3737 0.0007  85  ARG   X CA  
41628 C  C   . ARG   X  85  ? 1.7205 0.5602 1.0451 -0.0328 -0.3698 -0.0336 85  ARG   X C   
41629 O  O   . ARG   X  85  ? 1.7884 0.3661 1.1323 -0.0581 -0.3089 -0.0570 85  ARG   X O   
41630 C  CB  . ARG   X  85  ? 1.6737 0.4619 1.1428 0.0274  -0.3998 0.0295  85  ARG   X CB  
41631 C  CG  . ARG   X  85  ? 1.6912 0.4767 1.1326 0.0224  -0.4232 0.0087  85  ARG   X CG  
41632 C  CD  . ARG   X  85  ? 1.6943 0.4334 1.1246 0.0285  -0.4375 0.0488  85  ARG   X CD  
41633 N  NE  . ARG   X  85  ? 1.6911 0.3980 1.1146 0.0946  -0.4983 0.0441  85  ARG   X NE  
41634 C  CZ  . ARG   X  85  ? 1.6981 0.3395 1.1142 0.1270  -0.5043 0.0450  85  ARG   X CZ  
41635 N  NH1 . ARG   X  85  ? 1.7136 0.3730 1.0980 0.0989  -0.5033 0.0143  85  ARG   X NH1 
41636 N  NH2 . ARG   X  85  ? 1.7204 0.3655 1.1202 0.1571  -0.4837 0.0607  85  ARG   X NH2 
41637 N  N   . GLN   X  86  ? 1.7392 0.5749 1.1077 -0.0536 -0.3365 -0.0420 86  GLN   X N   
41638 C  CA  . GLN   X  86  ? 1.7020 0.6610 1.0683 -0.0033 -0.3533 -0.0580 86  GLN   X CA  
41639 C  C   . GLN   X  86  ? 1.6934 0.6756 1.0420 0.0040  -0.3493 -0.0682 86  GLN   X C   
41640 O  O   . GLN   X  86  ? 1.6795 0.7439 1.0551 0.0329  -0.3840 -0.0683 86  GLN   X O   
41641 C  CB  . GLN   X  86  ? 1.7647 0.6506 1.0715 0.0030  -0.3263 -0.0555 86  GLN   X CB  
41642 C  CG  . GLN   X  86  ? 1.8165 0.7788 1.0193 0.0105  -0.3338 -0.0610 86  GLN   X CG  
41643 C  CD  . GLN   X  86  ? 1.8685 0.7927 1.0672 -0.0075 -0.3325 -0.0393 86  GLN   X CD  
41644 O  OE1 . GLN   X  86  ? 1.8300 0.9279 1.1547 0.1185  -0.2659 0.0434  86  GLN   X OE1 
41645 N  NE2 . GLN   X  86  ? 1.8933 0.8510 1.0207 -0.0222 -0.3227 -0.0641 86  GLN   X NE2 
41646 N  N   . GLU   X  87  ? 1.6722 0.6566 1.0578 -0.0170 -0.3485 -0.0929 87  GLU   X N   
41647 C  CA  . GLU   X  87  ? 1.6722 0.6775 1.0810 -0.0432 -0.3319 -0.0774 87  GLU   X CA  
41648 C  C   . GLU   X  87  ? 1.6680 0.6480 1.0915 -0.0416 -0.3169 -0.0527 87  GLU   X C   
41649 O  O   . GLU   X  87  ? 1.6579 0.7292 1.0470 -0.1303 -0.2810 -0.0886 87  GLU   X O   
41650 C  CB  . GLU   X  87  ? 1.6886 0.7348 1.0735 -0.0479 -0.3340 -0.0835 87  GLU   X CB  
41651 C  CG  . GLU   X  87  ? 1.6882 0.7324 1.1355 -0.0315 -0.3234 -0.0676 87  GLU   X CG  
41652 C  CD  . GLU   X  87  ? 1.6667 0.7692 1.1745 -0.0226 -0.3107 -0.0343 87  GLU   X CD  
41653 O  OE1 . GLU   X  87  ? 1.6780 0.8104 1.2416 -0.0432 -0.3082 -0.1300 87  GLU   X OE1 
41654 O  OE2 . GLU   X  87  ? 1.7223 0.8034 1.2215 -0.0152 -0.2554 0.0226  87  GLU   X OE2 
41655 N  N   . LEU   X  88  ? 1.6702 0.5789 1.1131 -0.0455 -0.2923 -0.0807 88  LEU   X N   
41656 C  CA  . LEU   X  88  ? 1.6752 0.5510 1.1100 -0.0181 -0.3047 -0.0585 88  LEU   X CA  
41657 C  C   . LEU   X  88  ? 1.7159 0.4478 1.1206 -0.0100 -0.2873 -0.0373 88  LEU   X C   
41658 O  O   . LEU   X  88  ? 1.7033 0.5319 1.1085 0.0048  -0.2976 -0.0372 88  LEU   X O   
41659 C  CB  . LEU   X  88  ? 1.6628 0.5831 1.0577 -0.0449 -0.2930 -0.0503 88  LEU   X CB  
41660 C  CG  . LEU   X  88  ? 1.6425 0.5486 1.0554 -0.0537 -0.3052 -0.0382 88  LEU   X CG  
41661 C  CD1 . LEU   X  88  ? 1.6540 0.5304 1.0470 -0.0740 -0.2879 -0.0123 88  LEU   X CD1 
41662 C  CD2 . LEU   X  88  ? 1.6400 0.5464 1.0416 -0.0553 -0.3008 -0.0441 88  LEU   X CD2 
41663 N  N   . ALA   X  89  ? 1.7538 0.3158 1.1501 -0.0155 -0.3203 -0.0013 89  ALA   X N   
41664 C  CA  . ALA   X  89  ? 1.7956 0.2997 1.1545 -0.0084 -0.3102 0.0021  89  ALA   X CA  
41665 C  C   . ALA   X  89  ? 1.8390 0.3083 1.2040 0.0078  -0.3426 0.0095  89  ALA   X C   
41666 O  O   . ALA   X  89  ? 1.8061 0.1680 1.2410 0.0209  -0.3686 -0.0013 89  ALA   X O   
41667 C  CB  . ALA   X  89  ? 1.8001 0.2780 1.1477 -0.0177 -0.3048 0.0283  89  ALA   X CB  
41668 N  N   . LYS   X  90  ? 1.8498 0.4545 1.2489 0.0797  -0.3215 -0.0508 90  LYS   X N   
41669 C  CA  . LYS   X  90  ? 1.8653 0.5831 1.2000 0.0338  -0.3665 -0.0454 90  LYS   X CA  
41670 C  C   . LYS   X  90  ? 1.8445 0.6648 1.0880 0.0197  -0.3983 -0.0646 90  LYS   X C   
41671 O  O   . LYS   X  90  ? 1.6872 0.6507 1.0798 -0.0099 -0.4249 0.0095  90  LYS   X O   
41672 C  CB  . LYS   X  90  ? 1.9539 0.6548 1.2349 0.1244  -0.3633 -0.0535 90  LYS   X CB  
41673 C  CG  . LYS   X  90  ? 2.0265 0.6715 1.2663 0.0931  -0.3559 -0.0932 90  LYS   X CG  
41674 C  CD  . LYS   X  90  ? 2.0800 0.7907 1.3414 0.1633  -0.3084 -0.1081 90  LYS   X CD  
41675 C  CE  . LYS   X  90  ? 2.1119 0.9030 1.4165 0.1389  -0.2949 -0.1899 90  LYS   X CE  
41676 N  NZ  . LYS   X  90  ? 2.1432 1.0501 1.4768 0.2095  -0.2652 -0.2125 90  LYS   X NZ  
41677 N  N   . SER   X  91  ? 1.8367 0.7125 1.1520 -0.0429 -0.3532 -0.0886 91  SER   X N   
41678 C  CA  . SER   X  91  ? 1.8510 0.7158 1.2213 -0.0396 -0.3747 -0.0881 91  SER   X CA  
41679 C  C   . SER   X  91  ? 1.8524 0.6645 1.2600 0.0602  -0.3425 -0.0423 91  SER   X C   
41680 O  O   . SER   X  91  ? 1.9068 0.6100 1.1952 0.1157  -0.4175 0.1204  91  SER   X O   
41681 C  CB  . SER   X  91  ? 1.9111 0.7530 1.2073 -0.0787 -0.3669 -0.1217 91  SER   X CB  
41682 O  OG  . SER   X  91  ? 1.9509 0.9233 1.2410 -0.1809 -0.3614 -0.1642 91  SER   X OG  
41683 N  N   . ILE   X  92  ? 1.8369 0.6563 1.3099 0.0531  -0.3404 -0.0770 92  ILE   X N   
41684 C  CA  . ILE   X  92  ? 1.7900 0.6048 1.3225 0.0819  -0.3469 -0.0366 92  ILE   X CA  
41685 C  C   . ILE   X  92  ? 1.8310 0.5133 1.2941 0.0761  -0.2712 -0.0364 92  ILE   X C   
41686 O  O   . ILE   X  92  ? 1.8368 0.5221 1.2531 0.0590  -0.2312 -0.0377 92  ILE   X O   
41687 C  CB  . ILE   X  92  ? 1.7902 0.5798 1.3550 0.0706  -0.3812 -0.0385 92  ILE   X CB  
41688 C  CG1 . ILE   X  92  ? 1.7881 0.5780 1.4279 0.0621  -0.3681 -0.0214 92  ILE   X CG1 
41689 C  CG2 . ILE   X  92  ? 1.7602 0.4447 1.2731 0.1030  -0.4181 -0.0532 92  ILE   X CG2 
41690 C  CD1 . ILE   X  92  ? 1.7969 0.6390 1.4709 0.0367  -0.3779 0.0220  92  ILE   X CD1 
41691 N  N   . ARG   X  93  ? 1.8047 0.5266 1.2607 0.1188  -0.2713 -0.0136 93  ARG   X N   
41692 C  CA  . ARG   X  93  ? 1.8302 0.4638 1.2806 0.1093  -0.2642 0.0268  93  ARG   X CA  
41693 C  C   . ARG   X  93  ? 1.8740 0.4454 1.2426 0.1206  -0.2945 0.0494  93  ARG   X C   
41694 O  O   . ARG   X  93  ? 1.8549 0.3571 1.2814 0.1360  -0.2797 0.0989  93  ARG   X O   
41695 C  CB  . ARG   X  93  ? 1.8664 0.3744 1.3015 0.1148  -0.2571 0.0603  93  ARG   X CB  
41696 C  CG  . ARG   X  93  ? 1.8517 0.3965 1.3713 0.1074  -0.2312 0.0667  93  ARG   X CG  
41697 C  CD  . ARG   X  93  ? 1.9070 0.3869 1.4301 0.0743  -0.2088 0.0824  93  ARG   X CD  
41698 N  NE  . ARG   X  93  ? 1.8450 0.4603 1.5280 0.0535  -0.2044 0.0628  93  ARG   X NE  
41699 C  CZ  . ARG   X  93  ? 1.8392 0.4608 1.5457 0.0224  -0.1912 0.0421  93  ARG   X CZ  
41700 N  NH1 . ARG   X  93  ? 1.8707 0.3785 1.5473 -0.0410 -0.1645 0.0180  93  ARG   X NH1 
41701 N  NH2 . ARG   X  93  ? 1.8366 0.4223 1.4975 0.0248  -0.1856 0.0188  93  ARG   X NH2 
41702 N  N   . SER   X  94  ? 1.8963 0.5384 1.2986 0.0995  -0.2680 -0.0352 94  SER   X N   
41703 C  CA  . SER   X  94  ? 1.9014 0.6320 1.3561 0.1117  -0.3284 -0.0346 94  SER   X CA  
41704 C  C   . SER   X  94  ? 1.9243 0.6653 1.3463 0.1019  -0.3416 -0.0385 94  SER   X C   
41705 O  O   . SER   X  94  ? 1.9312 0.6486 1.2555 0.0586  -0.3936 -0.0725 94  SER   X O   
41706 C  CB  . SER   X  94  ? 1.9199 0.7148 1.4258 0.1324  -0.2692 -0.0540 94  SER   X CB  
41707 O  OG  . SER   X  94  ? 1.9578 0.8130 1.5621 0.0882  -0.2933 -0.0835 94  SER   X OG  
41708 N  N   . ARG   X  95  ? 1.9085 0.7286 1.4349 0.1330  -0.3014 -0.0762 95  ARG   X N   
41709 C  CA  . ARG   X  95  ? 1.9452 0.7699 1.4909 0.0999  -0.2739 -0.1299 95  ARG   X CA  
41710 C  C   . ARG   X  95  ? 1.9155 0.6859 1.3927 0.1427  -0.2961 -0.1888 95  ARG   X C   
41711 O  O   . ARG   X  95  ? 1.9125 0.6456 1.4000 0.1788  -0.2510 -0.1713 95  ARG   X O   
41712 C  CB  . ARG   X  95  ? 1.9421 0.8905 1.6227 0.1451  -0.2446 -0.1038 95  ARG   X CB  
41713 C  CG  . ARG   X  95  ? 1.9812 0.9985 1.6896 0.1003  -0.2436 -0.1434 95  ARG   X CG  
41714 C  CD  . ARG   X  95  ? 1.9916 1.0659 1.7888 0.1335  -0.2144 -0.1366 95  ARG   X CD  
41715 N  NE  . ARG   X  95  ? 2.0188 1.0821 1.8720 0.1228  -0.1427 -0.1659 95  ARG   X NE  
41716 C  CZ  . ARG   X  95  ? 2.0095 1.0621 1.9257 0.0858  -0.0718 -0.2434 95  ARG   X CZ  
41717 N  NH1 . ARG   X  95  ? 2.0472 1.0593 1.9925 0.0213  -0.0513 -0.2086 95  ARG   X NH1 
41718 N  NH2 . ARG   X  95  ? 1.9421 1.1440 1.9313 0.0732  -0.0455 -0.2421 95  ARG   X NH2 
41719 N  N   . ARG   X  96  ? 1.8982 0.6942 1.3929 0.1101  -0.3224 -0.2395 96  ARG   X N   
41720 C  CA  . ARG   X  96  ? 1.8869 0.6879 1.3083 0.0466  -0.3278 -0.3075 96  ARG   X CA  
41721 C  C   . ARG   X  96  ? 1.8731 0.5947 1.2992 0.0529  -0.3281 -0.3041 96  ARG   X C   
41722 O  O   . ARG   X  96  ? 1.9003 0.7733 1.1747 0.0598  -0.3234 -0.3176 96  ARG   X O   
41723 C  CB  . ARG   X  96  ? 1.9005 0.8236 1.3574 0.0480  -0.2975 -0.3723 96  ARG   X CB  
41724 C  CG  . ARG   X  96  ? 1.8980 0.8908 1.3628 0.0288  -0.2606 -0.3457 96  ARG   X CG  
41725 C  CD  . ARG   X  96  ? 1.8859 1.0238 1.4197 0.0322  -0.2753 -0.3508 96  ARG   X CD  
41726 N  NE  . ARG   X  96  ? 1.8707 1.0591 1.4282 0.0021  -0.2944 -0.3907 96  ARG   X NE  
41727 C  CZ  . ARG   X  96  ? 1.8919 1.1152 1.4341 -0.0402 -0.2772 -0.3245 96  ARG   X CZ  
41728 N  NH1 . ARG   X  96  ? 1.9232 1.0313 1.4967 -0.0446 -0.2287 -0.3335 96  ARG   X NH1 
41729 N  NH2 . ARG   X  96  ? 1.8781 1.1270 1.4827 -0.0540 -0.2299 -0.3310 96  ARG   X NH2 
41730 N  N   . PRO   X  97  ? 1.8909 0.4190 1.2659 0.0089  -0.3765 -0.2821 97  PRO   X N   
41731 C  CA  . PRO   X  97  ? 1.8586 0.4090 1.2868 0.0169  -0.3713 -0.3046 97  PRO   X CA  
41732 C  C   . PRO   X  97  ? 1.8803 0.4167 1.3248 0.0520  -0.3547 -0.2610 97  PRO   X C   
41733 O  O   . PRO   X  97  ? 1.8696 0.5149 1.3526 -0.0065 -0.3294 -0.3239 97  PRO   X O   
41734 C  CB  . PRO   X  97  ? 1.8574 0.3662 1.2918 -0.0067 -0.3584 -0.3006 97  PRO   X CB  
41735 C  CG  . PRO   X  97  ? 1.8791 0.4204 1.2833 0.0009  -0.3803 -0.2770 97  PRO   X CG  
41736 C  CD  . PRO   X  97  ? 1.8817 0.4368 1.2669 0.0255  -0.3773 -0.2787 97  PRO   X CD  
41737 N  N   . TYR   X  98  ? 1.8572 0.5135 1.2454 0.0746  -0.4177 -0.1987 98  TYR   X N   
41738 C  CA  . TYR   X  98  ? 1.8293 0.6000 1.2963 0.1321  -0.4348 -0.0967 98  TYR   X CA  
41739 C  C   . TYR   X  98  ? 1.8121 0.6281 1.3292 0.1514  -0.4705 -0.1184 98  TYR   X C   
41740 O  O   . TYR   X  98  ? 1.7970 0.7212 1.3997 0.2307  -0.5098 -0.1875 98  TYR   X O   
41741 C  CB  . TYR   X  98  ? 1.7904 0.6939 1.2304 0.1353  -0.4551 -0.0830 98  TYR   X CB  
41742 C  CG  . TYR   X  98  ? 1.7396 0.7457 1.2513 0.1796  -0.4407 0.0058  98  TYR   X CG  
41743 C  CD1 . TYR   X  98  ? 1.7307 0.7923 1.2810 0.2156  -0.4379 0.0342  98  TYR   X CD1 
41744 C  CD2 . TYR   X  98  ? 1.7068 0.7615 1.2520 0.1880  -0.4266 0.0451  98  TYR   X CD2 
41745 C  CE1 . TYR   X  98  ? 1.7324 0.8112 1.3486 0.2386  -0.4165 0.0745  98  TYR   X CE1 
41746 C  CE2 . TYR   X  98  ? 1.6829 0.8076 1.3195 0.2170  -0.4070 0.0800  98  TYR   X CE2 
41747 C  CZ  . TYR   X  98  ? 1.6969 0.8491 1.3812 0.2279  -0.3834 0.1004  98  TYR   X CZ  
41748 O  OH  . TYR   X  98  ? 1.7419 0.8547 1.4395 0.2580  -0.3492 0.1417  98  TYR   X OH  
41749 N  N   . GLN   X  99  ? 1.7603 0.6291 1.3234 0.1769  -0.4776 -0.0811 99  GLN   X N   
41750 C  CA  . GLN   X  99  ? 1.7540 0.5347 1.2478 0.0942  -0.4568 -0.1114 99  GLN   X CA  
41751 C  C   . GLN   X  99  ? 1.6864 0.3907 1.2380 0.1185  -0.4533 -0.1005 99  GLN   X C   
41752 O  O   . GLN   X  99  ? 1.6735 0.2832 1.1735 0.1418  -0.4515 -0.1682 99  GLN   X O   
41753 C  CB  . GLN   X  99  ? 1.7542 0.6065 1.3124 0.0583  -0.4971 -0.1132 99  GLN   X CB  
41754 C  CG  . GLN   X  99  ? 1.7895 0.7424 1.3093 0.0755  -0.5215 -0.0513 99  GLN   X CG  
41755 C  CD  . GLN   X  99  ? 1.7989 0.9020 1.3371 0.0474  -0.6079 -0.0992 99  GLN   X CD  
41756 O  OE1 . GLN   X  99  ? 1.8735 0.8551 1.4624 0.0534  -0.5831 -0.1719 99  GLN   X OE1 
41757 N  NE2 . GLN   X  99  ? 1.8533 0.9479 1.3515 0.0778  -0.6224 -0.0635 99  GLN   X NE2 
41758 N  N   . VAL   X  100 ? 1.6672 0.3938 1.1374 0.1265  -0.4508 -0.0689 100 VAL   X N   
41759 C  CA  . VAL   X  100 ? 1.6594 0.4218 1.1381 0.0808  -0.4577 -0.0897 100 VAL   X CA  
41760 C  C   . VAL   X  100 ? 1.6576 0.4254 1.0970 0.0810  -0.4426 -0.1075 100 VAL   X C   
41761 O  O   . VAL   X  100 ? 1.7118 0.3322 1.1271 0.0855  -0.4172 -0.1210 100 VAL   X O   
41762 C  CB  . VAL   X  100 ? 1.6383 0.4248 1.0927 0.0756  -0.4727 -0.0877 100 VAL   X CB  
41763 C  CG1 . VAL   X  100 ? 1.6531 0.4770 1.0868 0.0709  -0.4769 -0.0610 100 VAL   X CG1 
41764 C  CG2 . VAL   X  100 ? 1.6161 0.4527 1.1659 0.0438  -0.4637 -0.1027 100 VAL   X CG2 
41765 N  N   . ASN   X  101 ? 1.6838 0.4848 1.0661 0.0831  -0.4454 -0.1003 101 ASN   X N   
41766 C  CA  . ASN   X  101 ? 1.6811 0.5567 1.0638 0.0736  -0.4463 -0.1235 101 ASN   X CA  
41767 C  C   . ASN   X  101 ? 1.6750 0.4712 1.0681 0.0920  -0.4694 -0.1201 101 ASN   X C   
41768 O  O   . ASN   X  101 ? 1.6630 0.4428 1.0055 0.1238  -0.4778 -0.1448 101 ASN   X O   
41769 C  CB  . ASN   X  101 ? 1.6940 0.5498 1.0989 0.0474  -0.4233 -0.1740 101 ASN   X CB  
41770 C  CG  . ASN   X  101 ? 1.6640 0.5923 1.1125 -0.0037 -0.4424 -0.2082 101 ASN   X CG  
41771 O  OD1 . ASN   X  101 ? 1.6426 0.5607 1.0469 0.0264  -0.4620 -0.2279 101 ASN   X OD1 
41772 N  ND2 . ASN   X  101 ? 1.6678 0.6480 1.1831 -0.0483 -0.4703 -0.2281 101 ASN   X ND2 
41773 N  N   . VAL   X  102 ? 1.6786 0.4419 1.0350 0.0961  -0.4823 -0.0817 102 VAL   X N   
41774 C  CA  . VAL   X  102 ? 1.7334 0.4681 0.9976 0.0911  -0.4750 -0.0513 102 VAL   X CA  
41775 C  C   . VAL   X  102 ? 1.7658 0.4724 0.9594 0.0795  -0.4913 -0.0352 102 VAL   X C   
41776 O  O   . VAL   X  102 ? 1.8156 0.4852 0.9086 0.0744  -0.4674 -0.0317 102 VAL   X O   
41777 C  CB  . VAL   X  102 ? 1.7120 0.4741 0.9765 0.0889  -0.4962 -0.0307 102 VAL   X CB  
41778 C  CG1 . VAL   X  102 ? 1.6989 0.5033 0.9842 0.0575  -0.5007 -0.0342 102 VAL   X CG1 
41779 C  CG2 . VAL   X  102 ? 1.6963 0.4837 0.9659 0.1058  -0.5018 -0.0173 102 VAL   X CG2 
41780 N  N   . LEU   X  103 ? 1.8132 0.4908 0.9608 0.0583  -0.4689 -0.0289 103 LEU   X N   
41781 C  CA  . LEU   X  103 ? 1.8236 0.6037 0.9561 0.0407  -0.4745 0.0050  103 LEU   X CA  
41782 C  C   . LEU   X  103 ? 1.7917 0.6131 0.9016 0.0138  -0.4528 0.0207  103 LEU   X C   
41783 O  O   . LEU   X  103 ? 1.7791 0.7493 0.8744 0.0471  -0.4669 0.0992  103 LEU   X O   
41784 C  CB  . LEU   X  103 ? 1.8571 0.6160 0.9516 0.0603  -0.4828 0.0059  103 LEU   X CB  
41785 C  CG  . LEU   X  103 ? 1.8840 0.6290 0.9977 0.1023  -0.4757 -0.0005 103 LEU   X CG  
41786 C  CD1 . LEU   X  103 ? 1.9258 0.6818 1.0056 0.1058  -0.4688 0.0280  103 LEU   X CD1 
41787 C  CD2 . LEU   X  103 ? 1.8715 0.6387 1.0127 0.1001  -0.4833 0.0092  103 LEU   X CD2 
41788 N  N   . ILE   X  104 ? 1.8005 0.6483 0.9255 -0.0222 -0.4335 0.0620  104 ILE   X N   
41789 C  CA  . ILE   X  104 ? 1.7847 0.6186 1.0095 -0.0854 -0.4058 0.0527  104 ILE   X CA  
41790 C  C   . ILE   X  104 ? 1.8213 0.5803 0.9868 -0.1272 -0.4085 0.0393  104 ILE   X C   
41791 O  O   . ILE   X  104 ? 1.8331 0.5629 0.9863 -0.1513 -0.3803 0.0410  104 ILE   X O   
41792 C  CB  . ILE   X  104 ? 1.7510 0.6238 1.0487 -0.0962 -0.4041 0.0609  104 ILE   X CB  
41793 C  CG1 . ILE   X  104 ? 1.7247 0.6286 1.0687 -0.0923 -0.3926 0.0863  104 ILE   X CG1 
41794 C  CG2 . ILE   X  104 ? 1.7751 0.6515 1.0731 -0.0938 -0.3915 0.0302  104 ILE   X CG2 
41795 C  CD1 . ILE   X  104 ? 1.7156 0.6473 1.0667 -0.0650 -0.3919 0.1040  104 ILE   X CD1 
41796 N  N   . GLY   X  105 ? 1.8488 0.6017 1.0348 -0.1542 -0.3512 0.0045  105 GLY   X N   
41797 C  CA  . GLY   X  105 ? 1.8651 0.6719 1.0635 -0.1466 -0.3715 -0.0122 105 GLY   X CA  
41798 C  C   . GLY   X  105 ? 1.8382 0.6875 1.1089 -0.1537 -0.3594 -0.0392 105 GLY   X C   
41799 O  O   . GLY   X  105 ? 1.8903 0.7133 1.1401 -0.1057 -0.3123 -0.0313 105 GLY   X O   
41800 N  N   . GLY   X  106 ? 1.8279 0.7192 1.1331 -0.1471 -0.3767 -0.0497 106 GLY   X N   
41801 C  CA  . GLY   X  106 ? 1.7928 0.7712 1.1021 -0.1382 -0.4215 -0.1103 106 GLY   X CA  
41802 C  C   . GLY   X  106 ? 1.8226 0.7889 1.1107 -0.1386 -0.4471 -0.1399 106 GLY   X C   
41803 O  O   . GLY   X  106 ? 1.7741 0.7220 0.9578 -0.1927 -0.5308 -0.2012 106 GLY   X O   
41804 N  N   . TYR   X  107 ? 1.8299 0.8143 1.1551 -0.1038 -0.4536 -0.1667 107 TYR   X N   
41805 C  CA  . TYR   X  107 ? 1.8530 0.8470 1.1669 -0.0847 -0.4811 -0.1549 107 TYR   X CA  
41806 C  C   . TYR   X  107 ? 1.8774 0.8142 1.2251 -0.0410 -0.4742 -0.1518 107 TYR   X C   
41807 O  O   . TYR   X  107 ? 1.9045 0.6814 1.2556 -0.0858 -0.4908 -0.1149 107 TYR   X O   
41808 C  CB  . TYR   X  107 ? 1.8970 0.8738 1.1599 -0.0803 -0.4695 -0.1652 107 TYR   X CB  
41809 C  CG  . TYR   X  107 ? 1.9157 0.9257 1.1652 -0.0587 -0.4845 -0.1450 107 TYR   X CG  
41810 C  CD1 . TYR   X  107 ? 1.9299 0.9615 1.2009 -0.0626 -0.5001 -0.1904 107 TYR   X CD1 
41811 C  CD2 . TYR   X  107 ? 1.9146 0.9188 1.1753 -0.0777 -0.5031 -0.1239 107 TYR   X CD2 
41812 C  CE1 . TYR   X  107 ? 1.9572 0.9795 1.2131 -0.0469 -0.5289 -0.1863 107 TYR   X CE1 
41813 C  CE2 . TYR   X  107 ? 1.9390 0.9808 1.2185 -0.0420 -0.5407 -0.1198 107 TYR   X CE2 
41814 C  CZ  . TYR   X  107 ? 1.9706 1.0152 1.2102 -0.0373 -0.5549 -0.1664 107 TYR   X CZ  
41815 O  OH  . TYR   X  107 ? 2.0052 1.1463 1.2553 -0.0281 -0.5885 -0.2012 107 TYR   X OH  
41816 N  N   . ASP   X  108 ? 1.8896 0.8419 1.2368 -0.0557 -0.4654 -0.1339 108 ASP   X N   
41817 C  CA  . ASP   X  108 ? 1.8746 0.8496 1.2945 -0.0631 -0.4670 -0.1459 108 ASP   X CA  
41818 C  C   . ASP   X  108 ? 1.8990 0.8957 1.3177 0.0004  -0.5264 -0.1562 108 ASP   X C   
41819 O  O   . ASP   X  108 ? 1.8997 0.9799 1.4259 0.0380  -0.5469 -0.1407 108 ASP   X O   
41820 C  CB  . ASP   X  108 ? 1.8702 0.9193 1.3021 -0.0980 -0.4595 -0.1516 108 ASP   X CB  
41821 C  CG  . ASP   X  108 ? 1.8686 0.9830 1.2830 -0.1443 -0.4145 -0.1470 108 ASP   X CG  
41822 O  OD1 . ASP   X  108 ? 1.8637 1.0143 1.2847 -0.2420 -0.3945 -0.2015 108 ASP   X OD1 
41823 O  OD2 . ASP   X  108 ? 1.8859 1.1683 1.3096 -0.1331 -0.3710 -0.0120 108 ASP   X OD2 
41824 N  N   . LYS   X  109 ? 1.9361 0.8835 1.3539 0.0239  -0.5249 -0.1312 109 LYS   X N   
41825 C  CA  . LYS   X  109 ? 1.9443 0.8027 1.3429 0.0164  -0.5297 -0.1073 109 LYS   X CA  
41826 C  C   . LYS   X  109 ? 1.9396 0.7790 1.3958 0.0161  -0.5596 -0.1296 109 LYS   X C   
41827 O  O   . LYS   X  109 ? 1.9255 0.7414 1.4135 0.0026  -0.5618 -0.1292 109 LYS   X O   
41828 C  CB  . LYS   X  109 ? 1.9827 0.7846 1.2818 0.0092  -0.4842 -0.1189 109 LYS   X CB  
41829 C  CG  . LYS   X  109 ? 2.0135 0.7640 1.2266 0.0146  -0.4512 -0.0652 109 LYS   X CG  
41830 C  CD  . LYS   X  109 ? 2.0679 0.7447 1.2594 0.0241  -0.4538 -0.0219 109 LYS   X CD  
41831 C  CE  . LYS   X  109 ? 2.1344 0.7533 1.2739 0.0132  -0.4144 -0.0244 109 LYS   X CE  
41832 N  NZ  . LYS   X  109 ? 2.2006 0.7896 1.2820 0.0106  -0.3890 -0.0091 109 LYS   X NZ  
41833 N  N   . LYS   X  110 ? 1.9010 0.8213 1.4283 -0.0061 -0.5637 -0.0928 110 LYS   X N   
41834 C  CA  . LYS   X  110 ? 1.9040 0.9295 1.5478 -0.0459 -0.5766 -0.1182 110 LYS   X CA  
41835 C  C   . LYS   X  110 ? 1.8958 0.9614 1.5234 -0.0474 -0.6060 -0.1082 110 LYS   X C   
41836 O  O   . LYS   X  110 ? 1.9097 0.9862 1.5885 -0.0781 -0.6039 -0.1243 110 LYS   X O   
41837 C  CB  . LYS   X  110 ? 1.9171 0.9112 1.6148 -0.0264 -0.5237 -0.0670 110 LYS   X CB  
41838 C  CG  . LYS   X  110 ? 1.9541 0.8248 1.7154 -0.0248 -0.4754 -0.0281 110 LYS   X CG  
41839 C  CD  . LYS   X  110 ? 1.9651 0.7765 1.8181 -0.0034 -0.4586 -0.0201 110 LYS   X CD  
41840 C  CE  . LYS   X  110 ? 2.0019 0.8098 1.8855 -0.0189 -0.4542 -0.0631 110 LYS   X CE  
41841 N  NZ  . LYS   X  110 ? 2.0157 0.7466 1.9600 -0.0456 -0.4036 -0.1032 110 LYS   X NZ  
41842 N  N   . LYS   X  111 ? 1.8553 0.9851 1.4773 -0.0931 -0.6143 -0.1165 111 LYS   X N   
41843 C  CA  . LYS   X  111 ? 1.7951 1.0815 1.4920 -0.0820 -0.6120 -0.1485 111 LYS   X CA  
41844 C  C   . LYS   X  111 ? 1.7722 1.0618 1.4802 -0.0571 -0.6932 -0.1505 111 LYS   X C   
41845 O  O   . LYS   X  111 ? 1.7333 1.0692 1.4700 -0.0651 -0.6867 -0.1691 111 LYS   X O   
41846 C  CB  . LYS   X  111 ? 1.7908 1.1550 1.4534 -0.0818 -0.5666 -0.1466 111 LYS   X CB  
41847 C  CG  . LYS   X  111 ? 1.7985 1.2440 1.4535 -0.0755 -0.5333 -0.1471 111 LYS   X CG  
41848 C  CD  . LYS   X  111 ? 1.8426 1.3249 1.4548 -0.0700 -0.5014 -0.1795 111 LYS   X CD  
41849 C  CE  . LYS   X  111 ? 1.8811 1.3820 1.4736 -0.1005 -0.4521 -0.2282 111 LYS   X CE  
41850 N  NZ  . LYS   X  111 ? 1.9439 1.3747 1.5065 -0.1228 -0.4426 -0.2479 111 LYS   X NZ  
41851 N  N   . ASN   X  112 ? 1.8322 1.0888 1.4456 -0.0802 -0.6598 -0.1541 112 ASN   X N   
41852 C  CA  . ASN   X  112 ? 1.8929 1.0642 1.4098 -0.0565 -0.7076 -0.1538 112 ASN   X CA  
41853 C  C   . ASN   X  112 ? 1.8933 1.0304 1.4432 0.0046  -0.6801 -0.0681 112 ASN   X C   
41854 O  O   . ASN   X  112 ? 1.9179 1.0384 1.4341 0.0126  -0.6765 -0.0583 112 ASN   X O   
41855 C  CB  . ASN   X  112 ? 1.9275 1.1014 1.4429 -0.1015 -0.7301 -0.1742 112 ASN   X CB  
41856 C  CG  . ASN   X  112 ? 1.9577 1.1472 1.4159 -0.1351 -0.7388 -0.2441 112 ASN   X CG  
41857 O  OD1 . ASN   X  112 ? 1.9342 1.1084 1.3270 -0.2152 -0.7758 -0.3033 112 ASN   X OD1 
41858 N  ND2 . ASN   X  112 ? 1.9933 1.1822 1.4892 -0.1661 -0.7263 -0.2441 112 ASN   X ND2 
41859 N  N   . LYS   X  113 ? 1.8749 0.9826 1.4701 0.0117  -0.6583 -0.1079 113 LYS   X N   
41860 C  CA  . LYS   X  113 ? 1.8213 0.9752 1.5304 0.0249  -0.6511 -0.1127 113 LYS   X CA  
41861 C  C   . LYS   X  113 ? 1.8499 0.8470 1.4943 0.0126  -0.6337 -0.1540 113 LYS   X C   
41862 O  O   . LYS   X  113 ? 1.7892 0.8399 1.5254 -0.0130 -0.6957 -0.2112 113 LYS   X O   
41863 C  CB  . LYS   X  113 ? 1.8394 1.0040 1.5993 0.0739  -0.6010 -0.1431 113 LYS   X CB  
41864 C  CG  . LYS   X  113 ? 1.8498 1.1427 1.6409 0.1010  -0.6106 -0.1479 113 LYS   X CG  
41865 C  CD  . LYS   X  113 ? 1.8759 1.2341 1.6609 0.0944  -0.5876 -0.1619 113 LYS   X CD  
41866 C  CE  . LYS   X  113 ? 1.8458 1.3600 1.6844 0.0923  -0.6204 -0.1530 113 LYS   X CE  
41867 N  NZ  . LYS   X  113 ? 1.8928 1.4122 1.7292 0.0577  -0.6387 -0.1801 113 LYS   X NZ  
41868 N  N   . PRO   X  114 ? 1.8534 0.8731 1.4315 -0.0009 -0.6021 -0.0977 114 PRO   X N   
41869 C  CA  . PRO   X  114 ? 1.8427 0.8187 1.3827 -0.0411 -0.5319 -0.0808 114 PRO   X CA  
41870 C  C   . PRO   X  114 ? 1.8434 0.7452 1.3803 -0.0778 -0.4930 -0.0469 114 PRO   X C   
41871 O  O   . PRO   X  114 ? 1.8598 0.6846 1.3884 -0.1266 -0.4262 -0.0787 114 PRO   X O   
41872 C  CB  . PRO   X  114 ? 1.8408 0.8338 1.3828 -0.0318 -0.5632 -0.0643 114 PRO   X CB  
41873 C  CG  . PRO   X  114 ? 1.8646 0.8724 1.4275 -0.0109 -0.5979 -0.0624 114 PRO   X CG  
41874 C  CD  . PRO   X  114 ? 1.8559 0.8975 1.4303 -0.0134 -0.6252 -0.0943 114 PRO   X CD  
41875 N  N   . GLU   X  115 ? 1.8108 0.7066 1.3044 -0.0715 -0.4431 0.0098  115 GLU   X N   
41876 C  CA  . GLU   X  115 ? 1.7815 0.7718 1.3081 -0.0540 -0.4317 0.0100  115 GLU   X CA  
41877 C  C   . GLU   X  115 ? 1.7895 0.6119 1.2214 -0.0517 -0.3758 0.0420  115 GLU   X C   
41878 O  O   . GLU   X  115 ? 1.7979 0.5285 1.1869 -0.0939 -0.3112 0.0806  115 GLU   X O   
41879 C  CB  . GLU   X  115 ? 1.7842 0.8131 1.3714 -0.0699 -0.3959 0.0404  115 GLU   X CB  
41880 C  CG  . GLU   X  115 ? 1.7573 0.9675 1.4552 -0.0590 -0.3955 0.0000  115 GLU   X CG  
41881 C  CD  . GLU   X  115 ? 1.7840 0.9813 1.4780 -0.0841 -0.3109 -0.0147 115 GLU   X CD  
41882 O  OE1 . GLU   X  115 ? 1.7410 1.0594 1.5747 -0.0094 -0.2505 -0.0177 115 GLU   X OE1 
41883 O  OE2 . GLU   X  115 ? 1.7313 1.2470 1.3335 -0.0510 -0.3540 -0.0993 115 GLU   X OE2 
41884 N  N   . LEU   X  116 ? 1.7664 0.6220 1.1952 -0.0512 -0.4078 0.0326  116 LEU   X N   
41885 C  CA  . LEU   X  116 ? 1.7508 0.6165 1.1420 -0.0083 -0.4204 0.0146  116 LEU   X CA  
41886 C  C   . LEU   X  116 ? 1.7158 0.5568 1.1244 0.0170  -0.4741 -0.0005 116 LEU   X C   
41887 O  O   . LEU   X  116 ? 1.7117 0.6647 1.2169 0.0221  -0.4699 -0.0376 116 LEU   X O   
41888 C  CB  . LEU   X  116 ? 1.7476 0.6369 1.1048 0.0024  -0.4361 0.0296  116 LEU   X CB  
41889 C  CG  . LEU   X  116 ? 1.7206 0.6842 1.0796 -0.0012 -0.4613 0.0381  116 LEU   X CG  
41890 C  CD1 . LEU   X  116 ? 1.7176 0.6700 1.0341 -0.0036 -0.4701 0.0286  116 LEU   X CD1 
41891 C  CD2 . LEU   X  116 ? 1.7445 0.6919 1.1252 -0.0034 -0.4655 0.0525  116 LEU   X CD2 
41892 N  N   . TYR   X  117 ? 1.7443 0.4683 1.0859 0.0154  -0.4652 0.0173  117 TYR   X N   
41893 C  CA  . TYR   X  117 ? 1.7459 0.4838 1.0844 0.0066  -0.4712 0.0094  117 TYR   X CA  
41894 C  C   . TYR   X  117 ? 1.7353 0.3821 1.0079 0.0443  -0.4661 0.0498  117 TYR   X C   
41895 O  O   . TYR   X  117 ? 1.7185 0.3629 0.9489 0.0601  -0.4941 0.1133  117 TYR   X O   
41896 C  CB  . TYR   X  117 ? 1.7618 0.4566 1.1201 -0.0053 -0.4811 -0.0249 117 TYR   X CB  
41897 C  CG  . TYR   X  117 ? 1.7725 0.5168 1.1541 -0.0115 -0.4998 -0.0801 117 TYR   X CG  
41898 C  CD1 . TYR   X  117 ? 1.7507 0.5239 1.1788 -0.0142 -0.5096 -0.0840 117 TYR   X CD1 
41899 C  CD2 . TYR   X  117 ? 1.7621 0.4996 1.1554 -0.0181 -0.5360 -0.0905 117 TYR   X CD2 
41900 C  CE1 . TYR   X  117 ? 1.7434 0.4907 1.1792 0.0084  -0.5140 -0.0909 117 TYR   X CE1 
41901 C  CE2 . TYR   X  117 ? 1.7824 0.4513 1.1767 -0.0081 -0.5323 -0.0970 117 TYR   X CE2 
41902 C  CZ  . TYR   X  117 ? 1.7585 0.4065 1.2145 -0.0244 -0.5400 -0.1051 117 TYR   X CZ  
41903 O  OH  . TYR   X  117 ? 1.7399 0.3976 1.3276 -0.0475 -0.5042 -0.0815 117 TYR   X OH  
41904 N  N   . GLN   X  118 ? 1.7378 0.3867 1.0085 0.0144  -0.4789 0.0207  118 GLN   X N   
41905 C  CA  . GLN   X  118 ? 1.7614 0.4365 1.0421 -0.0204 -0.4456 -0.0352 118 GLN   X CA  
41906 C  C   . GLN   X  118 ? 1.7188 0.2949 1.0419 0.0028  -0.4476 -0.0722 118 GLN   X C   
41907 O  O   . GLN   X  118 ? 1.7203 0.2048 1.0141 0.0099  -0.4375 -0.1365 118 GLN   X O   
41908 C  CB  . GLN   X  118 ? 1.7903 0.4477 1.0557 -0.0097 -0.4327 -0.0412 118 GLN   X CB  
41909 C  CG  . GLN   X  118 ? 1.8054 0.5870 1.0825 -0.0789 -0.4062 -0.0845 118 GLN   X CG  
41910 C  CD  . GLN   X  118 ? 1.8535 0.6014 1.1115 -0.0702 -0.3942 -0.1418 118 GLN   X CD  
41911 O  OE1 . GLN   X  118 ? 1.9275 0.8155 1.1116 -0.2596 -0.4256 -0.2018 118 GLN   X OE1 
41912 N  NE2 . GLN   X  118 ? 1.8745 0.7562 1.1312 -0.0889 -0.4193 -0.1169 118 GLN   X NE2 
41913 N  N   . ILE   X  119 ? 1.7214 0.2821 1.0786 0.0014  -0.4571 -0.0720 119 ILE   X N   
41914 C  CA  . ILE   X  119 ? 1.7447 0.3687 1.0886 0.0194  -0.4408 -0.0352 119 ILE   X CA  
41915 C  C   . ILE   X  119 ? 1.7638 0.3632 1.0819 0.0239  -0.4358 -0.0539 119 ILE   X C   
41916 O  O   . ILE   X  119 ? 1.8097 0.3570 1.0809 0.0530  -0.4037 -0.0345 119 ILE   X O   
41917 C  CB  . ILE   X  119 ? 1.7261 0.3745 1.0665 0.0313  -0.4863 0.0040  119 ILE   X CB  
41918 C  CG1 . ILE   X  119 ? 1.7231 0.3925 1.0808 0.0356  -0.5106 0.0154  119 ILE   X CG1 
41919 C  CG2 . ILE   X  119 ? 1.7334 0.4228 1.0528 0.0171  -0.4666 0.0005  119 ILE   X CG2 
41920 C  CD1 . ILE   X  119 ? 1.7117 0.3817 1.0922 0.0299  -0.5183 0.0235  119 ILE   X CD1 
41921 N  N   . ASP   X  120 ? 1.7674 0.4624 1.0861 0.0195  -0.3643 -0.0482 120 ASP   X N   
41922 C  CA  . ASP   X  120 ? 1.7693 0.4882 1.1357 -0.0305 -0.3480 -0.0328 120 ASP   X CA  
41923 C  C   . ASP   X  120 ? 1.7347 0.4477 1.1241 -0.0166 -0.3209 -0.0554 120 ASP   X C   
41924 O  O   . ASP   X  120 ? 1.7513 0.4665 1.1457 -0.0447 -0.2371 -0.0627 120 ASP   X O   
41925 C  CB  . ASP   X  120 ? 1.8013 0.5129 1.1591 -0.0380 -0.3169 -0.0488 120 ASP   X CB  
41926 C  CG  . ASP   X  120 ? 1.7823 0.5833 1.1685 -0.0766 -0.3554 0.0231  120 ASP   X CG  
41927 O  OD1 . ASP   X  120 ? 1.7562 0.5808 1.1437 -0.0144 -0.3941 0.0510  120 ASP   X OD1 
41928 O  OD2 . ASP   X  120 ? 1.7153 0.7199 1.0895 -0.0104 -0.4002 0.0052  120 ASP   X OD2 
41929 N  N   . TYR   X  121 ? 1.7370 0.4246 1.1080 -0.0012 -0.3205 -0.0732 121 TYR   X N   
41930 C  CA  . TYR   X  121 ? 1.7471 0.3995 1.1255 0.0155  -0.3102 -0.0649 121 TYR   X CA  
41931 C  C   . TYR   X  121 ? 1.6724 0.3226 1.1324 -0.0047 -0.3264 -0.0914 121 TYR   X C   
41932 O  O   . TYR   X  121 ? 1.6297 0.1969 1.1178 -0.0409 -0.2554 -0.1360 121 TYR   X O   
41933 C  CB  . TYR   X  121 ? 1.7538 0.4557 1.1356 0.0030  -0.3405 -0.0327 121 TYR   X CB  
41934 C  CG  . TYR   X  121 ? 1.8297 0.5286 1.0922 0.0247  -0.3262 -0.0380 121 TYR   X CG  
41935 C  CD1 . TYR   X  121 ? 1.8604 0.5337 1.1428 0.0302  -0.3293 -0.0194 121 TYR   X CD1 
41936 C  CD2 . TYR   X  121 ? 1.8782 0.5932 1.0943 0.0324  -0.3291 -0.0013 121 TYR   X CD2 
41937 C  CE1 . TYR   X  121 ? 1.9120 0.5571 1.1192 0.0503  -0.3128 -0.0120 121 TYR   X CE1 
41938 C  CE2 . TYR   X  121 ? 1.9239 0.6139 1.1081 0.0627  -0.3133 -0.0021 121 TYR   X CE2 
41939 C  CZ  . TYR   X  121 ? 1.9450 0.6216 1.1220 0.0616  -0.3098 0.0334  121 TYR   X CZ  
41940 O  OH  . TYR   X  121 ? 1.9765 0.6583 1.1430 0.0580  -0.2916 0.0088  121 TYR   X OH  
41941 N  N   . LEU   X  122 ? 1.6535 0.3234 1.1360 -0.0032 -0.3565 -0.0769 122 LEU   X N   
41942 C  CA  . LEU   X  122 ? 1.6656 0.3716 1.0979 0.0316  -0.3856 -0.0343 122 LEU   X CA  
41943 C  C   . LEU   X  122 ? 1.6740 0.3476 1.1390 0.0401  -0.4197 0.0002  122 LEU   X C   
41944 O  O   . LEU   X  122 ? 1.6648 0.2647 1.1189 0.1236  -0.4857 0.0325  122 LEU   X O   
41945 C  CB  . LEU   X  122 ? 1.6748 0.3699 1.0889 0.0324  -0.3818 -0.0405 122 LEU   X CB  
41946 C  CG  . LEU   X  122 ? 1.6699 0.3841 1.0541 0.0588  -0.3973 -0.0719 122 LEU   X CG  
41947 C  CD1 . LEU   X  122 ? 1.6894 0.4351 1.0872 0.0821  -0.3754 -0.0903 122 LEU   X CD1 
41948 C  CD2 . LEU   X  122 ? 1.6795 0.4015 1.0336 0.0546  -0.3897 -0.0875 122 LEU   X CD2 
41949 N  N   . GLY   X  123 ? 1.7051 0.4157 1.1575 0.0228  -0.4443 -0.0215 123 GLY   X N   
41950 C  CA  . GLY   X  123 ? 1.7045 0.3873 1.2353 0.0063  -0.4431 0.0042  123 GLY   X CA  
41951 C  C   . GLY   X  123 ? 1.6805 0.3934 1.3119 -0.0308 -0.4427 0.0185  123 GLY   X C   
41952 O  O   . GLY   X  123 ? 1.7422 0.3837 1.3633 -0.0410 -0.4405 0.1004  123 GLY   X O   
41953 N  N   . THR   X  124 ? 1.6757 0.4024 1.3496 0.0362  -0.4782 0.0062  124 THR   X N   
41954 C  CA  . THR   X  124 ? 1.6957 0.3874 1.2947 0.0420  -0.4812 0.0249  124 THR   X CA  
41955 C  C   . THR   X  124 ? 1.7626 0.3969 1.2743 0.0355  -0.4821 0.0468  124 THR   X C   
41956 O  O   . THR   X  124 ? 1.8108 0.5407 1.2463 -0.0183 -0.4811 0.0670  124 THR   X O   
41957 C  CB  . THR   X  124 ? 1.6907 0.4011 1.3540 0.0426  -0.4631 -0.0115 124 THR   X CB  
41958 O  OG1 . THR   X  124 ? 1.6544 0.3058 1.3545 0.0862  -0.4745 0.0352  124 THR   X OG1 
41959 C  CG2 . THR   X  124 ? 1.7072 0.3750 1.3780 0.0643  -0.4443 -0.0502 124 THR   X CG2 
41960 N  N   . LYS   X  125 ? 1.7969 0.3466 1.1518 0.0643  -0.4716 0.0219  125 LYS   X N   
41961 C  CA  . LYS   X  125 ? 1.7780 0.3816 1.1468 0.0667  -0.4677 0.0249  125 LYS   X CA  
41962 C  C   . LYS   X  125 ? 1.7940 0.2896 1.0999 0.0619  -0.4812 0.0050  125 LYS   X C   
41963 O  O   . LYS   X  125 ? 1.7642 0.1394 1.0922 0.0767  -0.4922 -0.0378 125 LYS   X O   
41964 C  CB  . LYS   X  125 ? 1.7894 0.3758 1.1565 0.0714  -0.4315 0.0551  125 LYS   X CB  
41965 C  CG  . LYS   X  125 ? 1.7911 0.4554 1.1648 0.0458  -0.4281 0.0375  125 LYS   X CG  
41966 C  CD  . LYS   X  125 ? 1.7956 0.4672 1.2159 0.0062  -0.4095 0.0170  125 LYS   X CD  
41967 C  CE  . LYS   X  125 ? 1.7966 0.5255 1.2970 -0.0305 -0.3504 0.0413  125 LYS   X CE  
41968 N  NZ  . LYS   X  125 ? 1.8371 0.5160 1.3349 -0.0187 -0.2817 0.0505  125 LYS   X NZ  
41969 N  N   . VAL   X  126 ? 1.7851 0.3101 1.1091 0.0916  -0.5246 0.0220  126 VAL   X N   
41970 C  CA  . VAL   X  126 ? 1.8274 0.4066 1.1226 0.1317  -0.5249 0.1054  126 VAL   X CA  
41971 C  C   . VAL   X  126 ? 1.8171 0.3570 1.1048 0.1300  -0.5642 0.1439  126 VAL   X C   
41972 O  O   . VAL   X  126 ? 1.8237 0.3124 1.1155 0.1301  -0.5701 0.2061  126 VAL   X O   
41973 C  CB  . VAL   X  126 ? 1.8402 0.4416 1.1064 0.2059  -0.5419 0.0929  126 VAL   X CB  
41974 C  CG1 . VAL   X  126 ? 1.8567 0.5958 1.1629 0.2331  -0.5577 0.1092  126 VAL   X CG1 
41975 C  CG2 . VAL   X  126 ? 1.8029 0.4643 1.1045 0.1781  -0.5554 0.0924  126 VAL   X CG2 
41976 N  N   . GLU   X  127 ? 1.8055 0.4628 1.1452 0.1128  -0.5774 0.1473  127 GLU   X N   
41977 C  CA  . GLU   X  127 ? 1.8017 0.6616 1.1469 0.0972  -0.5527 0.1089  127 GLU   X CA  
41978 C  C   . GLU   X  127 ? 1.7827 0.6257 1.1441 0.1144  -0.5243 0.0475  127 GLU   X C   
41979 O  O   . GLU   X  127 ? 1.7694 0.6020 1.1819 0.0766  -0.5133 0.0210  127 GLU   X O   
41980 C  CB  . GLU   X  127 ? 1.7833 0.7355 1.1956 0.0727  -0.5888 0.1199  127 GLU   X CB  
41981 C  CG  . GLU   X  127 ? 1.8016 0.8835 1.2121 0.0605  -0.5922 0.0763  127 GLU   X CG  
41982 C  CD  . GLU   X  127 ? 1.7940 1.0247 1.2702 0.0572  -0.6593 0.1177  127 GLU   X CD  
41983 O  OE1 . GLU   X  127 ? 1.7840 1.1841 1.4043 0.0706  -0.6667 0.1107  127 GLU   X OE1 
41984 O  OE2 . GLU   X  127 ? 1.7769 1.1412 1.2203 0.0232  -0.6958 0.1039  127 GLU   X OE2 
41985 N  N   . LEU   X  128 ? 1.7984 0.7122 1.1251 0.1131  -0.4803 0.0104  128 LEU   X N   
41986 C  CA  . LEU   X  128 ? 1.8333 0.7429 1.1056 0.1232  -0.4877 0.0360  128 LEU   X CA  
41987 C  C   . LEU   X  128 ? 1.8526 0.7413 1.0968 0.1103  -0.5341 0.0262  128 LEU   X C   
41988 O  O   . LEU   X  128 ? 1.8463 0.8831 1.0022 0.1468  -0.5184 0.0624  128 LEU   X O   
41989 C  CB  . LEU   X  128 ? 1.8220 0.8359 1.1717 0.0870  -0.5002 0.0393  128 LEU   X CB  
41990 C  CG  . LEU   X  128 ? 1.8523 0.9309 1.1766 0.0783  -0.4828 0.0517  128 LEU   X CG  
41991 C  CD1 . LEU   X  128 ? 1.8399 1.0190 1.2571 0.0463  -0.4761 0.0447  128 LEU   X CD1 
41992 C  CD2 . LEU   X  128 ? 1.8523 0.9697 1.2386 0.1072  -0.4981 0.0887  128 LEU   X CD2 
41993 N  N   . PRO   X  129 ? 1.8744 0.5704 1.1168 0.0922  -0.5241 -0.0299 129 PRO   X N   
41994 C  CA  . PRO   X  129 ? 1.9016 0.5166 1.1535 0.0984  -0.5356 0.0361  129 PRO   X CA  
41995 C  C   . PRO   X  129 ? 1.8981 0.4499 1.1853 0.1185  -0.5349 0.0594  129 PRO   X C   
41996 O  O   . PRO   X  129 ? 1.8810 0.3171 1.1525 0.1391  -0.5701 0.0646  129 PRO   X O   
41997 C  CB  . PRO   X  129 ? 1.8903 0.5821 1.1643 0.1112  -0.5464 0.0156  129 PRO   X CB  
41998 C  CG  . PRO   X  129 ? 1.8781 0.5988 1.1401 0.0894  -0.5600 0.0139  129 PRO   X CG  
41999 C  CD  . PRO   X  129 ? 1.8611 0.5575 1.1022 0.0812  -0.5266 -0.0138 129 PRO   X CD  
42000 N  N   . TYR   X  130 ? 1.8895 0.4840 1.2073 0.0846  -0.5257 0.0528  130 TYR   X N   
42001 C  CA  . TYR   X  130 ? 1.8918 0.5427 1.2453 0.0713  -0.4825 0.0785  130 TYR   X CA  
42002 C  C   . TYR   X  130 ? 1.8748 0.4814 1.2355 0.0391  -0.4629 0.0482  130 TYR   X C   
42003 O  O   . TYR   X  130 ? 1.8618 0.4736 1.1572 -0.0080 -0.5109 0.0121  130 TYR   X O   
42004 C  CB  . TYR   X  130 ? 1.9180 0.5375 1.3315 0.0808  -0.4435 0.0974  130 TYR   X CB  
42005 C  CG  . TYR   X  130 ? 1.9177 0.5274 1.3742 0.0998  -0.4668 0.1199  130 TYR   X CG  
42006 C  CD1 . TYR   X  130 ? 1.9067 0.5583 1.3939 0.1017  -0.4398 0.0994  130 TYR   X CD1 
42007 C  CD2 . TYR   X  130 ? 1.9289 0.5353 1.3707 0.1436  -0.4991 0.1753  130 TYR   X CD2 
42008 C  CE1 . TYR   X  130 ? 1.8994 0.5649 1.4237 0.1125  -0.4582 0.1309  130 TYR   X CE1 
42009 C  CE2 . TYR   X  130 ? 1.9216 0.6001 1.3724 0.1529  -0.5070 0.1654  130 TYR   X CE2 
42010 C  CZ  . TYR   X  130 ? 1.9120 0.5812 1.4095 0.1535  -0.4791 0.1527  130 TYR   X CZ  
42011 O  OH  . TYR   X  130 ? 1.9449 0.5051 1.4699 0.1662  -0.4701 0.1704  130 TYR   X OH  
42012 N  N   . GLY   X  131 ? 1.8656 0.4293 1.2439 0.0072  -0.4369 0.0256  131 GLY   X N   
42013 C  CA  . GLY   X  131 ? 1.8950 0.4012 1.2149 0.0154  -0.4088 0.0242  131 GLY   X CA  
42014 C  C   . GLY   X  131 ? 1.9349 0.3356 1.2555 0.0057  -0.3767 0.0181  131 GLY   X C   
42015 O  O   . GLY   X  131 ? 2.0094 0.3502 1.2839 0.0178  -0.3368 0.0023  131 GLY   X O   
42016 N  N   . ALA   X  132 ? 1.9306 0.3194 1.2087 0.0067  -0.3333 0.0352  132 ALA   X N   
42017 C  CA  . ALA   X  132 ? 1.9094 0.4448 1.2186 -0.0248 -0.3058 0.0449  132 ALA   X CA  
42018 C  C   . ALA   X  132 ? 1.8150 0.4453 1.2323 -0.0156 -0.3100 0.0398  132 ALA   X C   
42019 O  O   . ALA   X  132 ? 1.8619 0.5117 1.2611 -0.0108 -0.2731 0.0461  132 ALA   X O   
42020 C  CB  . ALA   X  132 ? 1.9726 0.4332 1.2820 -0.0672 -0.2685 0.0549  132 ALA   X CB  
42021 N  N   . HIS   X  133 ? 1.8024 0.4862 1.2414 -0.0216 -0.2968 0.0070  133 HIS   X N   
42022 C  CA  . HIS   X  133 ? 1.7598 0.5808 1.2488 -0.0428 -0.3079 -0.0403 133 HIS   X CA  
42023 C  C   . HIS   X  133 ? 1.7377 0.5850 1.3063 -0.0471 -0.3012 -0.0178 133 HIS   X C   
42024 O  O   . HIS   X  133 ? 1.6910 0.5900 1.3043 -0.0564 -0.3118 -0.0304 133 HIS   X O   
42025 C  CB  . HIS   X  133 ? 1.7502 0.6171 1.2069 -0.0268 -0.3239 -0.0781 133 HIS   X CB  
42026 C  CG  . HIS   X  133 ? 1.7802 0.6910 1.1251 -0.0746 -0.3068 -0.0853 133 HIS   X CG  
42027 N  ND1 . HIS   X  133 ? 1.7974 0.7549 1.1168 -0.0469 -0.3062 -0.0736 133 HIS   X ND1 
42028 C  CD2 . HIS   X  133 ? 1.8153 0.6911 1.0833 -0.0661 -0.3265 -0.0814 133 HIS   X CD2 
42029 C  CE1 . HIS   X  133 ? 1.8493 0.6837 1.0476 -0.0042 -0.3439 -0.0976 133 HIS   X CE1 
42030 N  NE2 . HIS   X  133 ? 1.8360 0.6028 1.0438 -0.0541 -0.3564 -0.0841 133 HIS   X NE2 
42031 N  N   . GLY   X  134 ? 1.7401 0.6062 1.3202 -0.0750 -0.2963 -0.0284 134 GLY   X N   
42032 C  CA  . GLY   X  134 ? 1.7906 0.6415 1.3426 -0.1094 -0.2946 -0.0506 134 GLY   X CA  
42033 C  C   . GLY   X  134 ? 1.8578 0.6666 1.3365 -0.0828 -0.2852 -0.0314 134 GLY   X C   
42034 O  O   . GLY   X  134 ? 1.8607 0.5320 1.2716 -0.1739 -0.3068 -0.0604 134 GLY   X O   
42035 N  N   . TYR   X  135 ? 1.9629 0.6789 1.3306 -0.1011 -0.2623 0.0304  135 TYR   X N   
42036 C  CA  . TYR   X  135 ? 1.9913 0.6878 1.3494 -0.1020 -0.3065 0.0441  135 TYR   X CA  
42037 C  C   . TYR   X  135 ? 2.0391 0.7772 1.3249 -0.1043 -0.2953 -0.0180 135 TYR   X C   
42038 O  O   . TYR   X  135 ? 2.0902 0.7143 1.3841 -0.1316 -0.2829 -0.0156 135 TYR   X O   
42039 C  CB  . TYR   X  135 ? 2.0336 0.6938 1.3279 -0.1334 -0.3392 0.0750  135 TYR   X CB  
42040 C  CG  . TYR   X  135 ? 2.0572 0.6968 1.3395 -0.1894 -0.3627 0.0964  135 TYR   X CG  
42041 C  CD1 . TYR   X  135 ? 2.0499 0.7192 1.3405 -0.2128 -0.3446 0.1381  135 TYR   X CD1 
42042 C  CD2 . TYR   X  135 ? 2.0611 0.7297 1.3451 -0.1738 -0.3584 0.1146  135 TYR   X CD2 
42043 C  CE1 . TYR   X  135 ? 2.0788 0.8001 1.3439 -0.2393 -0.3475 0.1419  135 TYR   X CE1 
42044 C  CE2 . TYR   X  135 ? 2.0754 0.7639 1.3601 -0.1772 -0.3800 0.1209  135 TYR   X CE2 
42045 C  CZ  . TYR   X  135 ? 2.0838 0.8102 1.3708 -0.2286 -0.3588 0.1088  135 TYR   X CZ  
42046 O  OH  . TYR   X  135 ? 2.1145 0.8013 1.4006 -0.3132 -0.3619 0.0032  135 TYR   X OH  
42047 N  N   . SER   X  136 ? 1.9518 0.8036 1.3043 -0.0654 -0.3219 -0.0192 136 SER   X N   
42048 C  CA  . SER   X  136 ? 1.9183 0.7899 1.2915 -0.0851 -0.3072 -0.0124 136 SER   X CA  
42049 C  C   . SER   X  136 ? 1.9124 0.6468 1.2302 -0.1123 -0.3414 0.0041  136 SER   X C   
42050 O  O   . SER   X  136 ? 1.8704 0.7940 1.2248 -0.1330 -0.3772 0.0458  136 SER   X O   
42051 C  CB  . SER   X  136 ? 1.9037 0.8770 1.2425 -0.1009 -0.2850 -0.0636 136 SER   X CB  
42052 O  OG  . SER   X  136 ? 1.8882 1.0522 1.2333 -0.1124 -0.2491 -0.1017 136 SER   X OG  
42053 N  N   . GLY   X  137 ? 1.8804 0.5392 1.2480 -0.1308 -0.3554 -0.0503 137 GLY   X N   
42054 C  CA  . GLY   X  137 ? 1.8770 0.5076 1.2115 -0.1071 -0.3926 -0.0246 137 GLY   X CA  
42055 C  C   . GLY   X  137 ? 1.9152 0.4692 1.1720 -0.1244 -0.4141 0.0479  137 GLY   X C   
42056 O  O   . GLY   X  137 ? 1.9262 0.3351 1.1358 -0.1757 -0.4174 0.0950  137 GLY   X O   
42057 N  N   . PHE   X  138 ? 1.9581 0.3919 1.1493 -0.0758 -0.3938 0.0400  138 PHE   X N   
42058 C  CA  . PHE   X  138 ? 2.0376 0.3849 1.2029 -0.0562 -0.3942 0.0453  138 PHE   X CA  
42059 C  C   . PHE   X  138 ? 2.1193 0.3577 1.1918 -0.0798 -0.4286 0.0204  138 PHE   X C   
42060 O  O   . PHE   X  138 ? 2.1668 0.3248 1.2220 -0.0769 -0.4047 0.0624  138 PHE   X O   
42061 C  CB  . PHE   X  138 ? 2.0377 0.3805 1.1827 -0.0533 -0.3945 0.0688  138 PHE   X CB  
42062 C  CG  . PHE   X  138 ? 2.0696 0.3947 1.1829 -0.0148 -0.3805 0.0754  138 PHE   X CG  
42063 C  CD1 . PHE   X  138 ? 2.0669 0.4491 1.1110 0.0091  -0.3646 0.0878  138 PHE   X CD1 
42064 C  CD2 . PHE   X  138 ? 2.0922 0.4044 1.1593 0.0105  -0.3833 0.0990  138 PHE   X CD2 
42065 C  CE1 . PHE   X  138 ? 2.0862 0.4364 1.1198 0.0143  -0.3593 0.1015  138 PHE   X CE1 
42066 C  CE2 . PHE   X  138 ? 2.1049 0.4250 1.1657 0.0104  -0.3701 0.1091  138 PHE   X CE2 
42067 C  CZ  . PHE   X  138 ? 2.0999 0.4240 1.1276 0.0144  -0.3513 0.1062  138 PHE   X CZ  
42068 N  N   . TYR   X  139 ? 2.1509 0.3385 1.2158 -0.0690 -0.4382 -0.0538 139 TYR   X N   
42069 C  CA  . TYR   X  139 ? 2.2382 0.4138 1.2776 -0.0683 -0.4515 0.0189  139 TYR   X CA  
42070 C  C   . TYR   X  139 ? 2.2123 0.5703 1.2781 -0.0182 -0.5246 0.0011  139 TYR   X C   
42071 O  O   . TYR   X  139 ? 2.2737 0.7722 1.3021 0.0244  -0.5366 0.0728  139 TYR   X O   
42072 C  CB  . TYR   X  139 ? 2.2859 0.4867 1.2871 -0.0919 -0.4149 0.0437  139 TYR   X CB  
42073 C  CG  . TYR   X  139 ? 2.3550 0.6656 1.2913 -0.2038 -0.4529 0.0179  139 TYR   X CG  
42074 C  CD1 . TYR   X  139 ? 2.4453 0.6768 1.3484 -0.2044 -0.4320 0.0512  139 TYR   X CD1 
42075 C  CD2 . TYR   X  139 ? 2.3848 0.6833 1.2566 -0.1474 -0.4388 0.1044  139 TYR   X CD2 
42076 C  CE1 . TYR   X  139 ? 2.5030 0.6890 1.3531 -0.2318 -0.4159 0.0359  139 TYR   X CE1 
42077 C  CE2 . TYR   X  139 ? 2.4247 0.7589 1.2301 -0.2137 -0.4426 0.0948  139 TYR   X CE2 
42078 C  CZ  . TYR   X  139 ? 2.5129 0.7566 1.3205 -0.2090 -0.4040 0.0750  139 TYR   X CZ  
42079 O  OH  . TYR   X  139 ? 2.4751 0.9703 1.2218 -0.3090 -0.4809 0.0891  139 TYR   X OH  
42080 N  N   . THR   X  140 ? 2.1542 0.5788 1.2580 0.0034  -0.5633 -0.0606 140 THR   X N   
42081 C  CA  . THR   X  140 ? 2.1255 0.6007 1.2242 0.0095  -0.5593 -0.0590 140 THR   X CA  
42082 C  C   . THR   X  140 ? 2.0830 0.4619 1.1477 0.0101  -0.6621 -0.1314 140 THR   X C   
42083 O  O   . THR   X  140 ? 2.1301 0.2449 1.1063 0.0340  -0.6274 -0.0176 140 THR   X O   
42084 C  CB  . THR   X  140 ? 2.0561 0.7956 1.2265 0.0911  -0.5106 -0.0981 140 THR   X CB  
42085 O  OG1 . THR   X  140 ? 2.1146 0.9442 1.2711 0.2020  -0.4712 -0.0322 140 THR   X OG1 
42086 C  CG2 . THR   X  140 ? 2.0885 0.8171 1.1557 0.0511  -0.4960 -0.0831 140 THR   X CG2 
42087 N  N   . PHE   X  141 ? 2.0303 0.5897 1.1486 -0.0497 -0.6132 -0.2130 141 PHE   X N   
42088 C  CA  . PHE   X  141 ? 2.0021 0.7028 1.2314 -0.0799 -0.6530 -0.2582 141 PHE   X CA  
42089 C  C   . PHE   X  141 ? 2.0509 0.5622 1.2272 -0.0869 -0.6173 -0.2750 141 PHE   X C   
42090 O  O   . PHE   X  141 ? 1.9935 0.6473 1.1883 -0.0288 -0.6506 -0.1983 141 PHE   X O   
42091 C  CB  . PHE   X  141 ? 1.9683 0.7083 1.2479 -0.0711 -0.6416 -0.2412 141 PHE   X CB  
42092 C  CG  . PHE   X  141 ? 1.9360 0.6749 1.3958 -0.1026 -0.6495 -0.2343 141 PHE   X CG  
42093 C  CD1 . PHE   X  141 ? 1.9192 0.7487 1.4074 -0.1009 -0.7204 -0.2710 141 PHE   X CD1 
42094 C  CD2 . PHE   X  141 ? 1.8772 0.6580 1.4790 -0.0788 -0.6435 -0.2287 141 PHE   X CD2 
42095 C  CE1 . PHE   X  141 ? 1.8952 0.8168 1.4649 0.0061  -0.7198 -0.2918 141 PHE   X CE1 
42096 C  CE2 . PHE   X  141 ? 1.8674 0.6962 1.5293 -0.0365 -0.6365 -0.2247 141 PHE   X CE2 
42097 C  CZ  . PHE   X  141 ? 1.8255 0.8395 1.4988 -0.0377 -0.7042 -0.3079 141 PHE   X CZ  
42098 N  N   . SER   X  142 ? 2.1336 0.5649 1.2892 -0.1730 -0.5677 -0.2681 142 SER   X N   
42099 C  CA  . SER   X  142 ? 2.1419 0.6209 1.3384 -0.1833 -0.5708 -0.2198 142 SER   X CA  
42100 C  C   . SER   X  142 ? 2.0782 0.6432 1.3327 -0.2373 -0.5704 -0.2355 142 SER   X C   
42101 O  O   . SER   X  142 ? 2.1703 0.5439 1.4041 -0.2537 -0.6060 -0.1431 142 SER   X O   
42102 C  CB  . SER   X  142 ? 2.1746 0.5311 1.4717 -0.1968 -0.5030 -0.1740 142 SER   X CB  
42103 O  OG  . SER   X  142 ? 2.2817 0.3432 1.5626 -0.2017 -0.4998 -0.1328 142 SER   X OG  
42104 N  N   . LEU   X  143 ? 2.1150 0.7648 1.3158 -0.2219 -0.5212 -0.1928 143 LEU   X N   
42105 C  CA  . LEU   X  143 ? 2.0943 0.8482 1.3328 -0.1269 -0.4949 -0.0626 143 LEU   X CA  
42106 C  C   . LEU   X  143 ? 1.9652 0.8432 1.2539 -0.0817 -0.5545 0.0030  143 LEU   X C   
42107 O  O   . LEU   X  143 ? 1.9643 0.8327 1.3207 0.0756  -0.5048 0.2135  143 LEU   X O   
42108 C  CB  . LEU   X  143 ? 2.1143 0.8879 1.2721 -0.1890 -0.4594 -0.0877 143 LEU   X CB  
42109 C  CG  . LEU   X  143 ? 2.1543 0.9391 1.2489 -0.1887 -0.5076 -0.0493 143 LEU   X CG  
42110 C  CD1 . LEU   X  143 ? 2.1717 0.9488 1.2317 -0.2108 -0.4580 -0.0373 143 LEU   X CD1 
42111 C  CD2 . LEU   X  143 ? 2.1650 0.9680 1.1707 -0.1835 -0.5234 -0.0337 143 LEU   X CD2 
42112 N  N   . LEU   X  144 ? 2.0112 0.8502 1.3347 -0.0321 -0.4458 0.0183  144 LEU   X N   
42113 C  CA  . LEU   X  144 ? 2.0110 0.8433 1.2641 0.0069  -0.4488 -0.0083 144 LEU   X CA  
42114 C  C   . LEU   X  144 ? 1.9646 0.8070 1.3169 0.0047  -0.5414 0.0501  144 LEU   X C   
42115 O  O   . LEU   X  144 ? 2.0114 0.8311 1.1551 0.0968  -0.5093 0.0073  144 LEU   X O   
42116 C  CB  . LEU   X  144 ? 2.0348 0.8021 1.2095 0.0134  -0.4201 -0.0451 144 LEU   X CB  
42117 C  CG  . LEU   X  144 ? 2.0563 0.8486 1.1947 0.0191  -0.4078 -0.0439 144 LEU   X CG  
42118 C  CD1 . LEU   X  144 ? 2.1029 0.8627 1.2224 0.0001  -0.3962 -0.0353 144 LEU   X CD1 
42119 C  CD2 . LEU   X  144 ? 2.0321 0.8270 1.1631 0.0156  -0.3823 -0.0520 144 LEU   X CD2 
42120 N  N   . ASP   X  145 ? 1.9312 0.7830 1.3409 0.0554  -0.4661 0.1416  145 ASP   X N   
42121 C  CA  . ASP   X  145 ? 1.8993 0.8036 1.4631 0.0731  -0.5090 0.2675  145 ASP   X CA  
42122 C  C   . ASP   X  145 ? 1.9785 0.7566 1.5093 0.0932  -0.5226 0.2989  145 ASP   X C   
42123 O  O   . ASP   X  145 ? 1.9721 0.6740 1.4986 0.1298  -0.5747 0.3773  145 ASP   X O   
42124 C  CB  . ASP   X  145 ? 1.8780 0.8873 1.4928 0.0755  -0.4826 0.2449  145 ASP   X CB  
42125 C  CG  . ASP   X  145 ? 1.8298 1.0227 1.4792 0.0821  -0.5404 0.2600  145 ASP   X CG  
42126 O  OD1 . ASP   X  145 ? 1.7884 1.0405 1.5730 0.0271  -0.5304 0.1924  145 ASP   X OD1 
42127 O  OD2 . ASP   X  145 ? 1.8341 1.0737 1.5063 0.0879  -0.5634 0.2183  145 ASP   X OD2 
42128 N  N   . HIS   X  146 ? 2.0517 0.7698 1.5604 0.1354  -0.5040 0.3779  146 HIS   X N   
42129 C  CA  . HIS   X  146 ? 2.1030 0.7676 1.5590 0.1382  -0.5225 0.3660  146 HIS   X CA  
42130 C  C   . HIS   X  146 ? 2.0560 0.7538 1.5581 0.1241  -0.6010 0.3306  146 HIS   X C   
42131 O  O   . HIS   X  146 ? 2.1604 0.6307 1.3947 0.1129  -0.6416 0.2612  146 HIS   X O   
42132 C  CB  . HIS   X  146 ? 2.1329 0.7422 1.6879 0.1567  -0.4897 0.4714  146 HIS   X CB  
42133 C  CG  . HIS   X  146 ? 2.1398 0.6549 1.8034 0.1365  -0.4380 0.5315  146 HIS   X CG  
42134 N  ND1 . HIS   X  146 ? 2.1657 0.5454 1.8627 0.1910  -0.4799 0.5998  146 HIS   X ND1 
42135 C  CD2 . HIS   X  146 ? 2.2289 0.6174 1.8272 0.1941  -0.4568 0.6070  146 HIS   X CD2 
42136 C  CE1 . HIS   X  146 ? 2.1839 0.6711 1.8140 0.1814  -0.4905 0.6381  146 HIS   X CE1 
42137 N  NE2 . HIS   X  146 ? 2.1825 0.7509 1.8345 0.1880  -0.4753 0.6225  146 HIS   X NE2 
42138 N  N   . HIS   X  147 ? 2.1044 0.7110 1.4498 0.1272  -0.5866 0.2492  147 HIS   X N   
42139 C  CA  . HIS   X  147 ? 2.0819 0.8596 1.4165 0.1327  -0.6247 0.2573  147 HIS   X CA  
42140 C  C   . HIS   X  147 ? 1.9908 0.9000 1.3300 0.0997  -0.7047 0.2163  147 HIS   X C   
42141 O  O   . HIS   X  147 ? 1.9193 1.0298 1.2866 0.1317  -0.7563 0.2970  147 HIS   X O   
42142 C  CB  . HIS   X  147 ? 2.1343 0.8747 1.4301 0.1279  -0.5363 0.2458  147 HIS   X CB  
42143 C  CG  . HIS   X  147 ? 2.2135 0.8953 1.4962 0.1404  -0.4720 0.3466  147 HIS   X CG  
42144 N  ND1 . HIS   X  147 ? 2.2188 0.9083 1.5306 0.0955  -0.4266 0.3379  147 HIS   X ND1 
42145 C  CD2 . HIS   X  147 ? 2.2434 0.9350 1.5110 0.1353  -0.4799 0.3847  147 HIS   X CD2 
42146 C  CE1 . HIS   X  147 ? 2.2528 0.9410 1.5432 0.1482  -0.4267 0.4094  147 HIS   X CE1 
42147 N  NE2 . HIS   X  147 ? 2.2770 0.8354 1.5654 0.1955  -0.4380 0.4482  147 HIS   X NE2 
42148 N  N   . TYR   X  148 ? 2.0026 0.8865 1.3617 0.0759  -0.7051 0.2237  148 TYR   X N   
42149 C  CA  . TYR   X  148 ? 1.9882 0.8963 1.3775 0.0528  -0.7334 0.1470  148 TYR   X CA  
42150 C  C   . TYR   X  148 ? 1.9881 0.8989 1.5032 0.0608  -0.7648 0.1489  148 TYR   X C   
42151 O  O   . TYR   X  148 ? 1.9234 0.8066 1.5257 0.0482  -0.8376 0.0931  148 TYR   X O   
42152 C  CB  . TYR   X  148 ? 2.0014 0.8328 1.3579 0.0335  -0.6890 0.1480  148 TYR   X CB  
42153 C  CG  . TYR   X  148 ? 2.0096 0.8474 1.2897 -0.0121 -0.6816 0.1010  148 TYR   X CG  
42154 C  CD1 . TYR   X  148 ? 2.0359 0.8059 1.2684 -0.0310 -0.6522 0.1101  148 TYR   X CD1 
42155 C  CD2 . TYR   X  148 ? 1.9829 0.8525 1.2425 0.0065  -0.7046 0.1097  148 TYR   X CD2 
42156 C  CE1 . TYR   X  148 ? 2.0310 0.7810 1.2240 0.0445  -0.6629 0.1792  148 TYR   X CE1 
42157 C  CE2 . TYR   X  148 ? 1.9748 0.8305 1.1688 0.0590  -0.7105 0.1837  148 TYR   X CE2 
42158 C  CZ  . TYR   X  148 ? 2.0158 0.7269 1.1782 0.0614  -0.7031 0.2189  148 TYR   X CZ  
42159 O  OH  . TYR   X  148 ? 1.9649 0.7418 1.1392 -0.0046 -0.7047 0.2219  148 TYR   X OH  
42160 N  N   . ARG   X  149 ? 2.0550 0.9243 1.5546 0.0788  -0.7314 0.1187  149 ARG   X N   
42161 C  CA  . ARG   X  149 ? 2.0605 0.9844 1.6884 0.0455  -0.7260 0.1407  149 ARG   X CA  
42162 C  C   . ARG   X  149 ? 2.1083 0.9569 1.5504 -0.0140 -0.7162 0.1020  149 ARG   X C   
42163 O  O   . ARG   X  149 ? 2.1179 0.9446 1.3964 -0.0688 -0.7001 0.0465  149 ARG   X O   
42164 C  CB  . ARG   X  149 ? 2.0842 1.0575 1.7470 0.0887  -0.7639 0.1604  149 ARG   X CB  
42165 C  CG  . ARG   X  149 ? 2.1155 1.0757 1.8874 0.1178  -0.7569 0.2121  149 ARG   X CG  
42166 C  CD  . ARG   X  149 ? 2.0736 1.0907 1.9896 0.1597  -0.7715 0.2124  149 ARG   X CD  
42167 N  NE  . ARG   X  149 ? 2.0443 1.1365 2.0378 0.2334  -0.7941 0.2484  149 ARG   X NE  
42168 C  CZ  . ARG   X  149 ? 2.0927 0.9634 2.1307 0.2793  -0.7338 0.2783  149 ARG   X CZ  
42169 N  NH1 . ARG   X  149 ? 2.0714 1.0899 2.1320 0.2334  -0.7288 0.2440  149 ARG   X NH1 
42170 N  NH2 . ARG   X  149 ? 2.0636 1.0282 2.0361 0.3055  -0.8228 0.3673  149 ARG   X NH2 
42171 N  N   . PRO   X  150 ? 2.1550 0.8914 1.5256 -0.0221 -0.7051 0.0595  150 PRO   X N   
42172 C  CA  . PRO   X  150 ? 2.1428 0.8816 1.4635 -0.0138 -0.6776 0.0435  150 PRO   X CA  
42173 C  C   . PRO   X  150 ? 2.1420 0.8524 1.4357 0.0184  -0.7002 0.0750  150 PRO   X C   
42174 O  O   . PRO   X  150 ? 2.1204 0.8793 1.4345 0.0295  -0.6827 0.1554  150 PRO   X O   
42175 C  CB  . PRO   X  150 ? 2.1474 0.8575 1.4574 -0.0088 -0.6708 0.0371  150 PRO   X CB  
42176 C  CG  . PRO   X  150 ? 2.1309 0.9185 1.4980 -0.0126 -0.7052 0.0462  150 PRO   X CG  
42177 C  CD  . PRO   X  150 ? 2.1493 0.9195 1.5372 -0.0085 -0.7114 0.0846  150 PRO   X CD  
42178 N  N   . ASP   X  151 ? 2.1605 0.8889 1.3989 -0.0014 -0.7249 0.0334  151 ASP   X N   
42179 C  CA  . ASP   X  151 ? 2.1519 0.8656 1.4269 -0.0168 -0.7668 0.0062  151 ASP   X CA  
42180 C  C   . ASP   X  151 ? 2.1915 0.7951 1.3200 0.0014  -0.7815 0.0030  151 ASP   X C   
42181 O  O   . ASP   X  151 ? 2.2274 0.7209 1.3038 0.0095  -0.8482 0.0526  151 ASP   X O   
42182 C  CB  . ASP   X  151 ? 2.1839 0.9230 1.4166 -0.0152 -0.8023 -0.0212 151 ASP   X CB  
42183 C  CG  . ASP   X  151 ? 2.1962 0.9612 1.4660 0.0297  -0.8234 0.0040  151 ASP   X CG  
42184 O  OD1 . ASP   X  151 ? 2.1980 1.0732 1.4914 0.0182  -0.8452 -0.0553 151 ASP   X OD1 
42185 O  OD2 . ASP   X  151 ? 2.1581 0.9676 1.5035 -0.0173 -0.8685 -0.1119 151 ASP   X OD2 
42186 N  N   . MET   X  152 ? 2.1305 0.7916 1.4218 -0.0120 -0.7497 0.0342  152 MET   X N   
42187 C  CA  . MET   X  152 ? 2.1370 0.8153 1.4097 -0.0031 -0.7255 0.0170  152 MET   X CA  
42188 C  C   . MET   X  152 ? 2.1160 0.7801 1.3793 -0.0357 -0.7408 -0.0064 152 MET   X C   
42189 O  O   . MET   X  152 ? 2.0582 0.7096 1.3733 -0.0533 -0.7291 -0.0787 152 MET   X O   
42190 C  CB  . MET   X  152 ? 2.1545 0.9501 1.3860 -0.0558 -0.7426 0.0206  152 MET   X CB  
42191 C  CG  . MET   X  152 ? 2.1796 0.9943 1.3713 -0.0530 -0.7511 -0.0340 152 MET   X CG  
42192 S  SD  . MET   X  152 ? 2.1402 1.2340 1.3262 -0.1526 -0.7754 0.0142  152 MET   X SD  
42193 C  CE  . MET   X  152 ? 2.1577 1.2725 1.2895 -0.1329 -0.7517 0.0138  152 MET   X CE  
42194 N  N   . THR   X  153 ? 2.1282 0.7359 1.3469 -0.0029 -0.7485 -0.0229 153 THR   X N   
42195 C  CA  . THR   X  153 ? 2.1544 0.7869 1.3763 0.0051  -0.7294 -0.0566 153 THR   X CA  
42196 C  C   . THR   X  153 ? 2.1444 0.7785 1.3514 -0.0020 -0.7090 -0.0679 153 THR   X C   
42197 O  O   . THR   X  153 ? 2.1086 0.6818 1.3815 0.0031  -0.7376 -0.0094 153 THR   X O   
42198 C  CB  . THR   X  153 ? 2.1873 0.8919 1.3753 0.0169  -0.7323 -0.0728 153 THR   X CB  
42199 O  OG1 . THR   X  153 ? 2.2347 0.8856 1.4518 0.0053  -0.7002 -0.1204 153 THR   X OG1 
42200 C  CG2 . THR   X  153 ? 2.1886 0.9599 1.4219 0.0218  -0.7502 -0.0822 153 THR   X CG2 
42201 N  N   . THR   X  154 ? 2.1346 0.8682 1.3836 0.0069  -0.6743 -0.1410 154 THR   X N   
42202 C  CA  . THR   X  154 ? 2.1015 0.9486 1.4334 -0.0069 -0.6312 -0.1564 154 THR   X CA  
42203 C  C   . THR   X  154 ? 2.1402 0.9788 1.4423 0.0514  -0.5636 -0.0533 154 THR   X C   
42204 O  O   . THR   X  154 ? 2.0797 1.0907 1.5157 0.0583  -0.5729 -0.0875 154 THR   X O   
42205 C  CB  . THR   X  154 ? 2.1021 1.0382 1.4652 0.0243  -0.6160 -0.1999 154 THR   X CB  
42206 O  OG1 . THR   X  154 ? 2.0446 1.1834 1.4962 -0.0333 -0.6262 -0.1302 154 THR   X OG1 
42207 C  CG2 . THR   X  154 ? 2.0876 0.9448 1.4582 -0.0178 -0.5857 -0.2023 154 THR   X CG2 
42208 N  N   . GLU   X  155 ? 2.1517 0.9984 1.4333 0.0502  -0.5824 -0.0533 155 GLU   X N   
42209 C  CA  . GLU   X  155 ? 2.2028 1.0110 1.4352 0.0864  -0.5272 -0.0191 155 GLU   X CA  
42210 C  C   . GLU   X  155 ? 2.2067 0.8860 1.3720 0.0473  -0.5771 0.0348  155 GLU   X C   
42211 O  O   . GLU   X  155 ? 2.2235 0.6827 1.3500 0.1396  -0.5259 0.0325  155 GLU   X O   
42212 C  CB  . GLU   X  155 ? 2.2573 1.1781 1.4583 0.0793  -0.5391 0.0184  155 GLU   X CB  
42213 C  CG  . GLU   X  155 ? 2.3222 1.2676 1.5401 0.1096  -0.4846 -0.0082 155 GLU   X CG  
42214 C  CD  . GLU   X  155 ? 2.3085 1.3358 1.6629 0.0992  -0.4335 0.0116  155 GLU   X CD  
42215 O  OE1 . GLU   X  155 ? 2.3709 1.3398 1.8438 0.1510  -0.4222 0.0416  155 GLU   X OE1 
42216 O  OE2 . GLU   X  155 ? 2.3621 1.3844 1.7327 0.1659  -0.3849 0.0209  155 GLU   X OE2 
42217 N  N   . GLU   X  156 ? 2.1967 0.8065 1.3185 0.0614  -0.6081 0.0139  156 GLU   X N   
42218 C  CA  . GLU   X  156 ? 2.1992 0.7696 1.3307 0.0569  -0.6243 0.0158  156 GLU   X CA  
42219 C  C   . GLU   X  156 ? 2.1933 0.7804 1.3032 0.0721  -0.5934 -0.0314 156 GLU   X C   
42220 O  O   . GLU   X  156 ? 2.1972 0.8833 1.1858 0.0432  -0.6005 -0.0925 156 GLU   X O   
42221 C  CB  . GLU   X  156 ? 2.1953 0.7800 1.3739 0.0520  -0.6518 0.0375  156 GLU   X CB  
42222 C  CG  . GLU   X  156 ? 2.2582 0.8704 1.4094 0.0564  -0.6766 0.0911  156 GLU   X CG  
42223 C  CD  . GLU   X  156 ? 2.2498 0.9452 1.4828 0.0716  -0.7075 0.1407  156 GLU   X CD  
42224 O  OE1 . GLU   X  156 ? 2.2484 0.9944 1.5577 0.0932  -0.7498 0.1758  156 GLU   X OE1 
42225 O  OE2 . GLU   X  156 ? 2.2500 0.9376 1.5828 0.0898  -0.7071 0.1119  156 GLU   X OE2 
42226 N  N   . GLY   X  157 ? 2.1696 0.7502 1.2399 0.0625  -0.6146 -0.0809 157 GLY   X N   
42227 C  CA  . GLY   X  157 ? 2.1158 0.7343 1.2194 0.0475  -0.5973 -0.1158 157 GLY   X CA  
42228 C  C   . GLY   X  157 ? 2.1158 0.7482 1.2247 0.0421  -0.5675 -0.1181 157 GLY   X C   
42229 O  O   . GLY   X  157 ? 2.0965 0.7667 1.2523 0.0832  -0.5392 -0.1682 157 GLY   X O   
42230 N  N   . LEU   X  158 ? 2.1459 0.7980 1.1828 0.0080  -0.5769 -0.1194 158 LEU   X N   
42231 C  CA  . LEU   X  158 ? 2.1579 0.8100 1.1820 -0.0010 -0.5383 -0.1074 158 LEU   X CA  
42232 C  C   . LEU   X  158 ? 2.2084 0.8136 1.1935 0.0200  -0.5317 -0.0665 158 LEU   X C   
42233 O  O   . LEU   X  158 ? 2.1954 0.7474 1.2764 0.0099  -0.5407 -0.0225 158 LEU   X O   
42234 C  CB  . LEU   X  158 ? 2.1612 0.8590 1.1834 -0.0268 -0.5308 -0.1274 158 LEU   X CB  
42235 C  CG  . LEU   X  158 ? 2.1249 0.8436 1.1991 -0.0456 -0.5267 -0.1812 158 LEU   X CG  
42236 C  CD1 . LEU   X  158 ? 2.1569 0.9333 1.1893 -0.0467 -0.5210 -0.1859 158 LEU   X CD1 
42237 C  CD2 . LEU   X  158 ? 2.0950 0.8412 1.1783 -0.0707 -0.5058 -0.1950 158 LEU   X CD2 
42238 N  N   . ASP   X  159 ? 2.2538 0.8558 1.1699 0.0337  -0.5412 -0.0531 159 ASP   X N   
42239 C  CA  . ASP   X  159 ? 2.3046 0.8647 1.1832 0.0485  -0.5133 -0.0196 159 ASP   X CA  
42240 C  C   . ASP   X  159 ? 2.2694 0.8400 1.1924 0.0617  -0.4682 0.0186  159 ASP   X C   
42241 O  O   . ASP   X  159 ? 2.2747 0.7890 1.1847 0.1207  -0.4488 0.0070  159 ASP   X O   
42242 C  CB  . ASP   X  159 ? 2.3454 0.8646 1.1939 0.0574  -0.5413 -0.0330 159 ASP   X CB  
42243 C  CG  . ASP   X  159 ? 2.3906 0.9039 1.2032 0.0522  -0.5340 -0.0607 159 ASP   X CG  
42244 O  OD1 . ASP   X  159 ? 2.4060 0.9500 1.2056 0.0606  -0.4925 -0.0975 159 ASP   X OD1 
42245 O  OD2 . ASP   X  159 ? 2.4223 0.9373 1.2199 0.0384  -0.5524 -0.0825 159 ASP   X OD2 
42246 N  N   . LEU   X  160 ? 2.2681 0.8542 1.1628 0.0558  -0.4718 0.0224  160 LEU   X N   
42247 C  CA  . LEU   X  160 ? 2.2252 0.8023 1.1289 0.0404  -0.5013 0.0457  160 LEU   X CA  
42248 C  C   . LEU   X  160 ? 2.1976 0.8127 1.0988 0.0301  -0.4742 0.0292  160 LEU   X C   
42249 O  O   . LEU   X  160 ? 2.1959 0.8275 1.0787 0.0148  -0.4458 0.0345  160 LEU   X O   
42250 C  CB  . LEU   X  160 ? 2.2260 0.7968 1.0635 0.0443  -0.4987 0.0396  160 LEU   X CB  
42251 C  CG  . LEU   X  160 ? 2.2318 0.7490 1.0393 0.0661  -0.5241 0.0246  160 LEU   X CG  
42252 C  CD1 . LEU   X  160 ? 2.2697 0.7583 1.0360 0.0696  -0.5256 0.0767  160 LEU   X CD1 
42253 C  CD2 . LEU   X  160 ? 2.2153 0.7833 1.0386 0.0422  -0.5195 0.0028  160 LEU   X CD2 
42254 N  N   . LEU   X  161 ? 2.1741 0.8444 1.1072 0.0434  -0.4934 0.0477  161 LEU   X N   
42255 C  CA  . LEU   X  161 ? 2.1745 0.8963 1.1185 0.0649  -0.4936 0.0678  161 LEU   X CA  
42256 C  C   . LEU   X  161 ? 2.1582 0.9057 1.1304 0.0764  -0.4799 0.0934  161 LEU   X C   
42257 O  O   . LEU   X  161 ? 2.1077 0.8862 1.1192 0.1315  -0.4935 0.1180  161 LEU   X O   
42258 C  CB  . LEU   X  161 ? 2.2027 0.9447 1.1553 0.1091  -0.4806 0.0582  161 LEU   X CB  
42259 C  CG  . LEU   X  161 ? 2.1861 1.0286 1.1968 0.1407  -0.4683 0.0827  161 LEU   X CG  
42260 C  CD1 . LEU   X  161 ? 2.1616 1.0546 1.2242 0.1768  -0.4423 0.1015  161 LEU   X CD1 
42261 C  CD2 . LEU   X  161 ? 2.1977 1.0886 1.1866 0.1546  -0.4482 0.0513  161 LEU   X CD2 
42262 N  N   . LYS   X  162 ? 2.1611 0.9374 1.1543 0.0135  -0.4491 0.1158  162 LYS   X N   
42263 C  CA  . LYS   X  162 ? 2.1832 0.9687 1.2346 0.0027  -0.4366 0.1718  162 LYS   X CA  
42264 C  C   . LYS   X  162 ? 2.1346 0.9302 1.2772 -0.0176 -0.4416 0.1874  162 LYS   X C   
42265 O  O   . LYS   X  162 ? 2.1468 0.8852 1.3560 -0.0377 -0.4097 0.2044  162 LYS   X O   
42266 C  CB  . LYS   X  162 ? 2.2629 1.0155 1.2665 -0.0131 -0.4173 0.2915  162 LYS   X CB  
42267 C  CG  . LYS   X  162 ? 2.2655 1.0683 1.3103 -0.0003 -0.3388 0.3510  162 LYS   X CG  
42268 C  CD  . LYS   X  162 ? 2.3346 1.1448 1.3566 -0.0109 -0.3176 0.4399  162 LYS   X CD  
42269 C  CE  . LYS   X  162 ? 2.3774 1.1319 1.4475 0.0037  -0.2969 0.5005  162 LYS   X CE  
42270 N  NZ  . LYS   X  162 ? 2.4184 1.1359 1.5022 0.0080  -0.3175 0.5846  162 LYS   X NZ  
42271 N  N   . LEU   X  163 ? 2.1304 0.9128 1.2699 -0.0095 -0.4644 0.1817  163 LEU   X N   
42272 C  CA  . LEU   X  163 ? 2.1386 0.8873 1.3436 -0.0385 -0.4601 0.1489  163 LEU   X CA  
42273 C  C   . LEU   X  163 ? 2.1264 0.8115 1.3492 -0.0359 -0.4444 0.0657  163 LEU   X C   
42274 O  O   . LEU   X  163 ? 2.2239 0.8334 1.5360 -0.1255 -0.3901 0.0269  163 LEU   X O   
42275 C  CB  . LEU   X  163 ? 2.1419 0.9404 1.3035 -0.0366 -0.4900 0.1722  163 LEU   X CB  
42276 C  CG  . LEU   X  163 ? 2.1868 0.9367 1.3612 -0.0328 -0.4826 0.1869  163 LEU   X CG  
42277 C  CD1 . LEU   X  163 ? 2.2029 0.9385 1.3972 -0.0655 -0.4722 0.1998  163 LEU   X CD1 
42278 C  CD2 . LEU   X  163 ? 2.1809 0.9883 1.3727 -0.0156 -0.4671 0.2101  163 LEU   X CD2 
42279 N  N   . CYS   X  164 ? 2.0587 0.7700 1.3387 0.0026  -0.4495 0.0182  164 CYS   X N   
42280 C  CA  . CYS   X  164 ? 1.9395 0.7440 1.3293 0.0119  -0.4598 -0.0497 164 CYS   X CA  
42281 C  C   . CYS   X  164 ? 1.9650 0.5730 1.2497 -0.0266 -0.4730 -0.0819 164 CYS   X C   
42282 O  O   . CYS   X  164 ? 1.9378 0.4043 1.3360 0.0235  -0.4250 -0.0993 164 CYS   X O   
42283 C  CB  . CYS   X  164 ? 1.9257 0.7797 1.3084 -0.0030 -0.4403 -0.0418 164 CYS   X CB  
42284 S  SG  . CYS   X  164 ? 1.8863 0.9295 1.3519 0.0675  -0.4537 -0.0999 164 CYS   X SG  
42285 N  N   . VAL   X  165 ? 1.9383 0.6409 1.2411 -0.0442 -0.4613 -0.0651 165 VAL   X N   
42286 C  CA  . VAL   X  165 ? 1.9373 0.6722 1.2614 -0.0429 -0.4348 -0.0674 165 VAL   X CA  
42287 C  C   . VAL   X  165 ? 1.9779 0.6741 1.2581 0.0021  -0.4212 -0.0024 165 VAL   X C   
42288 O  O   . VAL   X  165 ? 1.9388 0.7371 1.3048 -0.0272 -0.4160 0.0146  165 VAL   X O   
42289 C  CB  . VAL   X  165 ? 1.9351 0.6946 1.2820 -0.0485 -0.4364 -0.0952 165 VAL   X CB  
42290 C  CG1 . VAL   X  165 ? 1.9372 0.6958 1.3147 -0.0472 -0.4125 -0.0962 165 VAL   X CG1 
42291 C  CG2 . VAL   X  165 ? 1.9131 0.6862 1.2886 -0.0571 -0.4464 -0.1299 165 VAL   X CG2 
42292 N  N   . GLN   X  166 ? 2.0062 0.6902 1.2355 0.0199  -0.4058 0.0089  166 GLN   X N   
42293 C  CA  . GLN   X  166 ? 2.0214 0.7004 1.2278 0.0344  -0.3856 0.0450  166 GLN   X CA  
42294 C  C   . GLN   X  166 ? 2.0258 0.5168 1.2782 -0.0121 -0.3930 0.0534  166 GLN   X C   
42295 O  O   . GLN   X  166 ? 2.0671 0.3643 1.3045 0.0126  -0.3399 0.0986  166 GLN   X O   
42296 C  CB  . GLN   X  166 ? 2.0456 0.7588 1.2238 0.0840  -0.3729 0.0664  166 GLN   X CB  
42297 C  CG  . GLN   X  166 ? 2.0655 0.8310 1.2046 0.1033  -0.3882 0.0626  166 GLN   X CG  
42298 C  CD  . GLN   X  166 ? 2.1234 0.8864 1.1590 0.1421  -0.3919 0.0681  166 GLN   X CD  
42299 O  OE1 . GLN   X  166 ? 2.1621 0.8741 1.1116 0.1793  -0.4160 0.0587  166 GLN   X OE1 
42300 N  NE2 . GLN   X  166 ? 2.1545 0.9695 1.1156 0.1524  -0.3847 0.0882  166 GLN   X NE2 
42301 N  N   . GLU   X  167 ? 2.0317 0.5577 1.2763 -0.0256 -0.3960 0.0443  167 GLU   X N   
42302 C  CA  . GLU   X  167 ? 2.0400 0.5333 1.2964 -0.0434 -0.4053 0.0200  167 GLU   X CA  
42303 C  C   . GLU   X  167 ? 2.0273 0.5615 1.2842 -0.0943 -0.4078 -0.0079 167 GLU   X C   
42304 O  O   . GLU   X  167 ? 2.0149 0.6723 1.2370 -0.1421 -0.4517 -0.0388 167 GLU   X O   
42305 C  CB  . GLU   X  167 ? 2.0304 0.5310 1.3144 -0.0231 -0.3956 0.0227  167 GLU   X CB  
42306 C  CG  . GLU   X  167 ? 2.0285 0.5409 1.3214 -0.0182 -0.3819 0.0276  167 GLU   X CG  
42307 C  CD  . GLU   X  167 ? 2.0905 0.5474 1.3387 -0.0336 -0.3644 0.1254  167 GLU   X CD  
42308 O  OE1 . GLU   X  167 ? 2.1067 0.4326 1.4230 -0.0397 -0.3372 0.0963  167 GLU   X OE1 
42309 O  OE2 . GLU   X  167 ? 2.1532 0.5837 1.3788 -0.0205 -0.3766 0.1844  167 GLU   X OE2 
42310 N  N   . LEU   X  168 ? 1.9830 0.5795 1.2444 -0.0987 -0.4302 0.0110  168 LEU   X N   
42311 C  CA  . LEU   X  168 ? 1.9532 0.6057 1.2354 -0.1216 -0.4198 0.0047  168 LEU   X CA  
42312 C  C   . LEU   X  168 ? 1.9798 0.5715 1.2725 -0.1140 -0.3738 0.0156  168 LEU   X C   
42313 O  O   . LEU   X  168 ? 1.9845 0.5399 1.3125 -0.1042 -0.3824 -0.0024 168 LEU   X O   
42314 C  CB  . LEU   X  168 ? 1.9453 0.6138 1.1839 -0.1161 -0.4188 0.0418  168 LEU   X CB  
42315 C  CG  . LEU   X  168 ? 1.9501 0.6213 1.1420 -0.1007 -0.4273 0.0878  168 LEU   X CG  
42316 C  CD1 . LEU   X  168 ? 1.9404 0.6327 1.1263 -0.0872 -0.4307 0.0823  168 LEU   X CD1 
42317 C  CD2 . LEU   X  168 ? 1.9444 0.6191 1.1430 -0.1223 -0.4220 0.0846  168 LEU   X CD2 
42318 N  N   . GLU   X  169 ? 1.9718 0.6164 1.2680 -0.1266 -0.3812 0.0427  169 GLU   X N   
42319 C  CA  . GLU   X  169 ? 1.9898 0.7002 1.3054 -0.1369 -0.3606 0.0951  169 GLU   X CA  
42320 C  C   . GLU   X  169 ? 1.9870 0.6885 1.2981 -0.1461 -0.3400 0.1472  169 GLU   X C   
42321 O  O   . GLU   X  169 ? 2.0140 0.6319 1.3057 -0.1475 -0.3230 0.2146  169 GLU   X O   
42322 C  CB  . GLU   X  169 ? 2.0338 0.8208 1.2881 -0.1402 -0.3631 0.1192  169 GLU   X CB  
42323 C  CG  . GLU   X  169 ? 2.0178 0.8824 1.3417 -0.1010 -0.3556 0.1326  169 GLU   X CG  
42324 C  CD  . GLU   X  169 ? 2.0699 1.0150 1.3322 -0.0785 -0.3300 0.1639  169 GLU   X CD  
42325 O  OE1 . GLU   X  169 ? 2.0584 1.0091 1.4226 -0.0589 -0.3441 0.2645  169 GLU   X OE1 
42326 O  OE2 . GLU   X  169 ? 2.1523 1.1383 1.4151 -0.0404 -0.3697 0.2284  169 GLU   X OE2 
42327 N  N   . LYS   X  170 ? 1.9852 0.6858 1.2881 -0.1553 -0.3361 0.1390  170 LYS   X N   
42328 C  CA  . LYS   X  170 ? 2.0321 0.6674 1.3357 -0.2115 -0.3243 0.0882  170 LYS   X CA  
42329 C  C   . LYS   X  170 ? 2.0220 0.6404 1.3479 -0.2242 -0.3400 0.0641  170 LYS   X C   
42330 O  O   . LYS   X  170 ? 2.0132 0.6935 1.3569 -0.2760 -0.3093 0.0655  170 LYS   X O   
42331 C  CB  . LYS   X  170 ? 2.0383 0.6940 1.3752 -0.1834 -0.3228 0.0804  170 LYS   X CB  
42332 C  CG  . LYS   X  170 ? 2.0795 0.7060 1.4226 -0.1689 -0.2930 0.0689  170 LYS   X CG  
42333 C  CD  . LYS   X  170 ? 2.0915 0.7499 1.4542 -0.1355 -0.2982 0.0718  170 LYS   X CD  
42334 C  CE  . LYS   X  170 ? 2.1115 0.7605 1.5314 -0.1319 -0.2635 0.0401  170 LYS   X CE  
42335 N  NZ  . LYS   X  170 ? 2.1430 0.7796 1.5747 -0.1435 -0.2128 0.0674  170 LYS   X NZ  
42336 N  N   . ARG   X  171 ? 2.0023 0.5788 1.3304 -0.2707 -0.3804 0.0165  171 ARG   X N   
42337 C  CA  . ARG   X  171 ? 1.9917 0.6303 1.3370 -0.2688 -0.4036 -0.0125 171 ARG   X CA  
42338 C  C   . ARG   X  171 ? 1.9599 0.6423 1.3530 -0.2794 -0.4284 -0.0266 171 ARG   X C   
42339 O  O   . ARG   X  171 ? 1.9023 0.7559 1.3186 -0.3035 -0.4421 -0.0071 171 ARG   X O   
42340 C  CB  . ARG   X  171 ? 1.9763 0.6477 1.3151 -0.2461 -0.4370 -0.0084 171 ARG   X CB  
42341 C  CG  . ARG   X  171 ? 1.9966 0.7493 1.3174 -0.2412 -0.4596 0.0328  171 ARG   X CG  
42342 C  CD  . ARG   X  171 ? 2.0129 0.7572 1.3556 -0.2502 -0.4632 0.0309  171 ARG   X CD  
42343 N  NE  . ARG   X  171 ? 2.0279 0.8287 1.4228 -0.2203 -0.4750 0.0573  171 ARG   X NE  
42344 C  CZ  . ARG   X  171 ? 2.0670 0.8402 1.4768 -0.2430 -0.4518 0.0397  171 ARG   X CZ  
42345 N  NH1 . ARG   X  171 ? 2.0587 0.9086 1.4479 -0.2459 -0.4535 0.0389  171 ARG   X NH1 
42346 N  NH2 . ARG   X  171 ? 2.0762 0.9014 1.5383 -0.2239 -0.4627 0.0597  171 ARG   X NH2 
42347 N  N   . MET   X  172 ? 1.9828 0.6446 1.3246 -0.2666 -0.4419 -0.0267 172 MET   X N   
42348 C  CA  . MET   X  172 ? 2.0259 0.7112 1.3215 -0.2612 -0.4247 0.0220  172 MET   X CA  
42349 C  C   . MET   X  172 ? 2.0437 0.5455 1.3701 -0.2522 -0.3679 0.0248  172 MET   X C   
42350 O  O   . MET   X  172 ? 2.1018 0.3997 1.4146 -0.2295 -0.3135 -0.0007 172 MET   X O   
42351 C  CB  . MET   X  172 ? 2.0381 0.7436 1.2989 -0.3022 -0.4214 -0.0131 172 MET   X CB  
42352 C  CG  . MET   X  172 ? 2.0561 0.8631 1.3052 -0.3458 -0.4104 0.0440  172 MET   X CG  
42353 S  SD  . MET   X  172 ? 2.0812 1.0447 1.2943 -0.3668 -0.4420 0.0648  172 MET   X SD  
42354 C  CE  . MET   X  172 ? 2.0688 1.1203 1.3218 -0.3209 -0.3889 0.0471  172 MET   X CE  
42355 N  N   . PRO   X  173 ? 2.0518 0.5693 1.3765 -0.2362 -0.3754 0.0235  173 PRO   X N   
42356 C  CA  . PRO   X  173 ? 2.0446 0.5617 1.4051 -0.2550 -0.3404 0.0384  173 PRO   X CA  
42357 C  C   . PRO   X  173 ? 1.9839 0.6387 1.4194 -0.2954 -0.3139 0.0645  173 PRO   X C   
42358 O  O   . PRO   X  173 ? 2.0010 0.4656 1.4226 -0.2563 -0.3591 0.0823  173 PRO   X O   
42359 C  CB  . PRO   X  173 ? 2.0535 0.5888 1.4048 -0.2641 -0.3598 -0.0250 173 PRO   X CB  
42360 C  CG  . PRO   X  173 ? 2.0412 0.6284 1.4120 -0.2405 -0.3594 -0.0476 173 PRO   X CG  
42361 C  CD  . PRO   X  173 ? 2.0398 0.6560 1.3514 -0.2331 -0.3549 -0.0230 173 PRO   X CD  
42362 N  N   . MET   X  174 ? 1.9789 0.6593 1.4885 -0.2473 -0.2671 0.0085  174 MET   X N   
42363 C  CA  . MET   X  174 ? 1.9745 0.7735 1.5977 -0.2347 -0.2195 -0.0242 174 MET   X CA  
42364 C  C   . MET   X  174 ? 1.9290 0.7299 1.5621 -0.1747 -0.2243 0.0353  174 MET   X C   
42365 O  O   . MET   X  174 ? 1.9493 0.6843 1.5448 -0.1674 -0.2450 0.0436  174 MET   X O   
42366 C  CB  . MET   X  174 ? 2.0000 0.7752 1.6779 -0.2269 -0.1821 -0.0050 174 MET   X CB  
42367 C  CG  . MET   X  174 ? 2.0782 0.8961 1.7889 -0.3136 -0.1718 -0.0688 174 MET   X CG  
42368 S  SD  . MET   X  174 ? 2.1016 0.9431 1.9657 -0.2930 -0.1344 -0.1463 174 MET   X SD  
42369 C  CE  . MET   X  174 ? 2.0252 1.0865 1.9019 -0.4053 -0.1888 -0.1900 174 MET   X CE  
42370 N  N   . ASP   X  175 ? 1.9359 0.7172 1.5109 -0.1276 -0.2379 0.0153  175 ASP   X N   
42371 C  CA  . ASP   X  175 ? 1.9157 0.7335 1.4989 -0.0959 -0.2613 0.0107  175 ASP   X CA  
42372 C  C   . ASP   X  175 ? 1.9017 0.7392 1.4387 -0.0509 -0.2942 0.0118  175 ASP   X C   
42373 O  O   . ASP   X  175 ? 1.8825 0.8516 1.5512 -0.0041 -0.3065 -0.0220 175 ASP   X O   
42374 C  CB  . ASP   X  175 ? 1.9213 0.8073 1.4801 -0.1105 -0.2348 -0.0360 175 ASP   X CB  
42375 C  CG  . ASP   X  175 ? 1.9271 0.8645 1.4818 -0.1164 -0.2235 -0.0524 175 ASP   X CG  
42376 O  OD1 . ASP   X  175 ? 1.9057 0.8588 1.4518 -0.1174 -0.2198 -0.0333 175 ASP   X OD1 
42377 O  OD2 . ASP   X  175 ? 1.9361 0.9048 1.5064 -0.1438 -0.1860 -0.0725 175 ASP   X OD2 
42378 N  N   . PHE   X  176 ? 1.9111 0.6402 1.3480 -0.0151 -0.3173 0.0608  176 PHE   X N   
42379 C  CA  . PHE   X  176 ? 1.8969 0.6336 1.2692 -0.0033 -0.3242 0.0804  176 PHE   X CA  
42380 C  C   . PHE   X  176 ? 1.8956 0.5844 1.2397 -0.0033 -0.3083 0.1284  176 PHE   X C   
42381 O  O   . PHE   X  176 ? 1.8523 0.5992 1.2026 0.0045  -0.3186 0.0736  176 PHE   X O   
42382 C  CB  . PHE   X  176 ? 1.8872 0.5764 1.2379 0.0154  -0.3390 0.0799  176 PHE   X CB  
42383 C  CG  . PHE   X  176 ? 1.9290 0.5243 1.2293 0.0269  -0.3508 0.0778  176 PHE   X CG  
42384 C  CD1 . PHE   X  176 ? 1.9631 0.5335 1.2389 0.0292  -0.3617 0.0711  176 PHE   X CD1 
42385 C  CD2 . PHE   X  176 ? 1.9644 0.5121 1.2386 0.0271  -0.3611 0.0760  176 PHE   X CD2 
42386 C  CE1 . PHE   X  176 ? 1.9937 0.5061 1.2513 0.0524  -0.3570 0.1072  176 PHE   X CE1 
42387 C  CE2 . PHE   X  176 ? 1.9980 0.5182 1.2513 0.0472  -0.3712 0.0948  176 PHE   X CE2 
42388 C  CZ  . PHE   X  176 ? 2.0096 0.5010 1.2468 0.0530  -0.3676 0.1045  176 PHE   X CZ  
42389 N  N   . LYS   X  177 ? 1.9297 0.5969 1.2489 0.0048  -0.2927 0.1445  177 LYS   X N   
42390 C  CA  . LYS   X  177 ? 1.9498 0.5722 1.2414 0.0040  -0.2769 0.1721  177 LYS   X CA  
42391 C  C   . LYS   X  177 ? 1.9339 0.5646 1.2157 0.0260  -0.3006 0.2035  177 LYS   X C   
42392 O  O   . LYS   X  177 ? 1.9228 0.5831 1.2083 0.0287  -0.2875 0.2132  177 LYS   X O   
42393 C  CB  . LYS   X  177 ? 1.9231 0.5840 1.2270 -0.0109 -0.2702 0.1617  177 LYS   X CB  
42394 C  CG  . LYS   X  177 ? 1.9345 0.5909 1.2353 -0.0345 -0.2625 0.1610  177 LYS   X CG  
42395 C  CD  . LYS   X  177 ? 1.9632 0.6226 1.2707 -0.0418 -0.2470 0.1919  177 LYS   X CD  
42396 C  CE  . LYS   X  177 ? 1.9548 0.6393 1.2785 -0.0598 -0.2398 0.1996  177 LYS   X CE  
42397 N  NZ  . LYS   X  177 ? 1.9883 0.6476 1.3187 -0.0753 -0.2211 0.2077  177 LYS   X NZ  
42398 N  N   . GLY   X  178 ? 1.9514 0.5496 1.2007 0.0609  -0.3024 0.2047  178 GLY   X N   
42399 C  CA  . GLY   X  178 ? 1.9767 0.6052 1.1842 0.0802  -0.3150 0.1749  178 GLY   X CA  
42400 C  C   . GLY   X  178 ? 1.9709 0.5937 1.1648 0.0729  -0.3067 0.1430  178 GLY   X C   
42401 O  O   . GLY   X  178 ? 1.9466 0.7018 1.1100 0.1002  -0.2913 0.0699  178 GLY   X O   
42402 N  N   . VAL   X  179 ? 2.0079 0.6139 1.1806 0.0721  -0.3340 0.1351  179 VAL   X N   
42403 C  CA  . VAL   X  179 ? 1.9967 0.6128 1.2089 0.0529  -0.3302 0.0985  179 VAL   X CA  
42404 C  C   . VAL   X  179 ? 2.0196 0.6091 1.1780 0.0433  -0.3503 0.1005  179 VAL   X C   
42405 O  O   . VAL   X  179 ? 2.0697 0.6046 1.1736 0.0139  -0.3366 0.0967  179 VAL   X O   
42406 C  CB  . VAL   X  179 ? 1.9955 0.6145 1.1972 0.0808  -0.3453 0.1071  179 VAL   X CB  
42407 C  CG1 . VAL   X  179 ? 1.9906 0.5615 1.2367 0.0713  -0.3415 0.0936  179 VAL   X CG1 
42408 C  CG2 . VAL   X  179 ? 2.0211 0.5815 1.2266 0.0923  -0.3520 0.1431  179 VAL   X CG2 
42409 N  N   . ILE   X  180 ? 1.9732 0.5534 1.1764 0.0294  -0.3854 0.0308  180 ILE   X N   
42410 C  CA  . ILE   X  180 ? 1.9669 0.5087 1.1907 -0.0019 -0.3820 0.0571  180 ILE   X CA  
42411 C  C   . ILE   X  180 ? 1.9681 0.4241 1.1799 0.0054  -0.4269 0.0806  180 ILE   X C   
42412 O  O   . ILE   X  180 ? 1.9297 0.4880 1.1426 0.0165  -0.4359 0.0025  180 ILE   X O   
42413 C  CB  . ILE   X  180 ? 1.9232 0.4769 1.2429 0.0164  -0.3592 -0.0282 180 ILE   X CB  
42414 C  CG1 . ILE   X  180 ? 1.9351 0.4934 1.2397 0.0280  -0.3272 -0.0389 180 ILE   X CG1 
42415 C  CG2 . ILE   X  180 ? 1.9198 0.5127 1.2895 -0.0072 -0.3592 -0.0664 180 ILE   X CG2 
42416 C  CD1 . ILE   X  180 ? 1.9049 0.4978 1.2660 0.0418  -0.3181 -0.0658 180 ILE   X CD1 
42417 N  N   . VAL   X  181 ? 1.9895 0.4207 1.1876 -0.0170 -0.4379 0.0989  181 VAL   X N   
42418 C  CA  . VAL   X  181 ? 1.9959 0.5309 1.2509 -0.0323 -0.4378 0.0758  181 VAL   X CA  
42419 C  C   . VAL   X  181 ? 2.0157 0.5437 1.1755 0.0022  -0.4431 0.0743  181 VAL   X C   
42420 O  O   . VAL   X  181 ? 2.0641 0.5435 1.1441 0.0104  -0.4273 0.0984  181 VAL   X O   
42421 C  CB  . VAL   X  181 ? 2.0108 0.5791 1.3103 -0.0164 -0.4683 0.0868  181 VAL   X CB  
42422 C  CG1 . VAL   X  181 ? 2.0152 0.6292 1.3664 -0.0230 -0.4793 0.0633  181 VAL   X CG1 
42423 C  CG2 . VAL   X  181 ? 2.0191 0.5985 1.3401 -0.0282 -0.4422 0.0590  181 VAL   X CG2 
42424 N  N   . LYS   X  182 ? 1.9919 0.6011 1.1774 -0.0447 -0.4490 0.0398  182 LYS   X N   
42425 C  CA  . LYS   X  182 ? 1.9865 0.6077 1.1878 -0.0586 -0.4357 0.0274  182 LYS   X CA  
42426 C  C   . LYS   X  182 ? 1.9885 0.6337 1.1611 -0.0639 -0.4248 0.0297  182 LYS   X C   
42427 O  O   . LYS   X  182 ? 1.9910 0.5931 1.1268 -0.0851 -0.4210 0.0380  182 LYS   X O   
42428 C  CB  . LYS   X  182 ? 1.9234 0.5245 1.2294 -0.0607 -0.4241 0.0096  182 LYS   X CB  
42429 C  CG  . LYS   X  182 ? 1.9227 0.5051 1.2635 -0.0686 -0.4049 -0.0061 182 LYS   X CG  
42430 C  CD  . LYS   X  182 ? 1.8686 0.5797 1.2920 -0.0290 -0.3965 -0.0100 182 LYS   X CD  
42431 C  CE  . LYS   X  182 ? 1.8675 0.6383 1.3412 -0.0431 -0.3720 -0.0142 182 LYS   X CE  
42432 N  NZ  . LYS   X  182 ? 1.8066 0.7514 1.3837 0.0089  -0.3818 0.0111  182 LYS   X NZ  
42433 N  N   . ILE   X  183 ? 2.0194 0.7224 1.1544 -0.0878 -0.4631 0.0207  183 ILE   X N   
42434 C  CA  . ILE   X  183 ? 2.0162 0.8376 1.1445 -0.0792 -0.4836 -0.0123 183 ILE   X CA  
42435 C  C   . ILE   X  183 ? 1.9628 0.8304 1.1297 -0.0949 -0.4882 -0.0598 183 ILE   X C   
42436 O  O   . ILE   X  183 ? 1.9624 0.8885 1.1742 -0.0845 -0.5248 -0.1359 183 ILE   X O   
42437 C  CB  . ILE   X  183 ? 2.0983 0.8891 1.1455 -0.0836 -0.4767 0.0129  183 ILE   X CB  
42438 C  CG1 . ILE   X  183 ? 2.1374 0.9121 1.1768 -0.1162 -0.4391 0.0197  183 ILE   X CG1 
42439 C  CG2 . ILE   X  183 ? 2.1034 0.8787 1.1658 -0.0831 -0.4896 0.0188  183 ILE   X CG2 
42440 C  CD1 . ILE   X  183 ? 2.2005 0.9850 1.1901 -0.1296 -0.4058 0.0448  183 ILE   X CD1 
42441 N  N   . VAL   X  184 ? 1.9368 0.8883 1.1235 -0.0915 -0.4886 -0.0901 184 VAL   X N   
42442 C  CA  . VAL   X  184 ? 1.9565 0.8785 1.1652 -0.0835 -0.4747 -0.0943 184 VAL   X CA  
42443 C  C   . VAL   X  184 ? 1.9904 0.9473 1.1369 -0.0969 -0.4920 -0.0938 184 VAL   X C   
42444 O  O   . VAL   X  184 ? 2.0345 0.9205 1.1533 -0.1021 -0.4941 -0.1505 184 VAL   X O   
42445 C  CB  . VAL   X  184 ? 1.9235 0.8680 1.1785 -0.0755 -0.4923 -0.0859 184 VAL   X CB  
42446 C  CG1 . VAL   X  184 ? 1.9178 0.8561 1.2474 -0.0815 -0.5092 -0.1139 184 VAL   X CG1 
42447 C  CG2 . VAL   X  184 ? 1.9069 0.7882 1.2197 -0.0919 -0.4609 -0.0901 184 VAL   X CG2 
42448 N  N   . ASP   X  185 ? 2.0683 0.9475 1.1606 -0.0482 -0.4214 -0.1093 185 ASP   X N   
42449 C  CA  . ASP   X  185 ? 2.1013 0.9101 1.1334 -0.0450 -0.4356 -0.0957 185 ASP   X CA  
42450 C  C   . ASP   X  185 ? 2.0971 0.9083 1.1909 -0.0416 -0.4623 -0.1099 185 ASP   X C   
42451 O  O   . ASP   X  185 ? 2.1155 0.8292 1.3617 0.0138  -0.4221 -0.0789 185 ASP   X O   
42452 C  CB  . ASP   X  185 ? 2.1327 1.0037 1.0725 -0.0375 -0.3976 -0.1028 185 ASP   X CB  
42453 C  CG  . ASP   X  185 ? 2.1999 0.9869 1.0011 -0.0341 -0.3808 -0.1040 185 ASP   X CG  
42454 O  OD1 . ASP   X  185 ? 2.1780 0.9752 0.8573 -0.0397 -0.3181 -0.1267 185 ASP   X OD1 
42455 O  OD2 . ASP   X  185 ? 2.2017 1.0851 0.9949 -0.0471 -0.3372 -0.0703 185 ASP   X OD2 
42456 N  N   . LYS   X  186 ? 2.1435 0.8992 1.1619 -0.0599 -0.4689 -0.1153 186 LYS   X N   
42457 C  CA  . LYS   X  186 ? 2.1166 0.9089 1.1599 -0.0757 -0.4795 -0.1305 186 LYS   X CA  
42458 C  C   . LYS   X  186 ? 2.1028 0.8755 1.1510 -0.0954 -0.4773 -0.1288 186 LYS   X C   
42459 O  O   . LYS   X  186 ? 2.1247 0.8541 1.1934 -0.1209 -0.4629 -0.1841 186 LYS   X O   
42460 C  CB  . LYS   X  186 ? 2.1470 0.9708 1.1974 -0.1100 -0.4992 -0.1458 186 LYS   X CB  
42461 C  CG  . LYS   X  186 ? 2.2140 1.0243 1.1777 -0.1437 -0.4756 -0.1591 186 LYS   X CG  
42462 C  CD  . LYS   X  186 ? 2.2502 1.0575 1.1770 -0.1823 -0.4902 -0.2018 186 LYS   X CD  
42463 C  CE  . LYS   X  186 ? 2.2838 1.0672 1.1857 -0.2062 -0.5012 -0.1966 186 LYS   X CE  
42464 N  NZ  . LYS   X  186 ? 2.3161 1.1099 1.2056 -0.2230 -0.4813 -0.2309 186 LYS   X NZ  
42465 N  N   . ASP   X  187 ? 2.1023 0.8040 1.1483 -0.0515 -0.4831 -0.0971 187 ASP   X N   
42466 C  CA  . ASP   X  187 ? 2.1291 0.7815 1.1599 -0.0671 -0.4296 -0.0667 187 ASP   X CA  
42467 C  C   . ASP   X  187 ? 2.0515 0.7717 1.1885 -0.0652 -0.3826 -0.0740 187 ASP   X C   
42468 O  O   . ASP   X  187 ? 2.0943 0.7970 1.1956 -0.0710 -0.3225 -0.0845 187 ASP   X O   
42469 C  CB  . ASP   X  187 ? 2.1615 0.7700 1.1749 -0.0699 -0.4476 -0.0470 187 ASP   X CB  
42470 C  CG  . ASP   X  187 ? 2.2061 0.8397 1.2090 -0.0453 -0.4933 -0.0210 187 ASP   X CG  
42471 O  OD1 . ASP   X  187 ? 2.2501 0.8008 1.2496 -0.0319 -0.4954 0.0379  187 ASP   X OD1 
42472 O  OD2 . ASP   X  187 ? 2.2345 0.8073 1.2721 -0.0663 -0.5238 -0.0257 187 ASP   X OD2 
42473 N  N   . GLY   X  188 ? 2.0267 0.7718 1.2007 -0.0518 -0.3496 -0.0647 188 GLY   X N   
42474 C  CA  . GLY   X  188 ? 1.9747 0.7275 1.2143 -0.0495 -0.3322 -0.0546 188 GLY   X CA  
42475 C  C   . GLY   X  188 ? 1.9643 0.6901 1.2284 -0.0271 -0.3232 0.0002  188 GLY   X C   
42476 O  O   . GLY   X  188 ? 1.9561 0.6396 1.2851 -0.0623 -0.3286 0.0438  188 GLY   X O   
42477 N  N   . ILE   X  189 ? 1.9484 0.6942 1.2194 0.0046  -0.2947 -0.0196 189 ILE   X N   
42478 C  CA  . ILE   X  189 ? 1.9780 0.6544 1.2022 0.0391  -0.2637 -0.0398 189 ILE   X CA  
42479 C  C   . ILE   X  189 ? 1.9699 0.7014 1.1763 0.0161  -0.2697 -0.0708 189 ILE   X C   
42480 O  O   . ILE   X  189 ? 2.0093 0.6339 1.2115 0.0172  -0.2143 0.0009  189 ILE   X O   
42481 C  CB  . ILE   X  189 ? 1.9674 0.6393 1.1944 0.0544  -0.2422 -0.0621 189 ILE   X CB  
42482 C  CG1 . ILE   X  189 ? 1.9828 0.6726 1.1951 0.0664  -0.2251 -0.0771 189 ILE   X CG1 
42483 C  CG2 . ILE   X  189 ? 1.9418 0.6187 1.2283 0.0443  -0.2202 -0.0091 189 ILE   X CG2 
42484 C  CD1 . ILE   X  189 ? 1.9745 0.7051 1.1617 0.0687  -0.2179 -0.0826 189 ILE   X CD1 
42485 N  N   . ARG   X  190 ? 1.9741 0.7122 1.1499 -0.0018 -0.3159 -0.0676 190 ARG   X N   
42486 C  CA  . ARG   X  190 ? 1.9994 0.8317 1.1078 -0.0042 -0.3199 -0.0448 190 ARG   X CA  
42487 C  C   . ARG   X  190 ? 2.0149 0.7836 1.1206 0.0225  -0.3273 0.0179  190 ARG   X C   
42488 O  O   . ARG   X  190 ? 2.0006 0.6532 1.0734 0.0064  -0.3345 0.0751  190 ARG   X O   
42489 C  CB  . ARG   X  190 ? 2.0462 0.9290 1.1142 -0.0081 -0.3384 -0.0640 190 ARG   X CB  
42490 C  CG  . ARG   X  190 ? 2.0318 1.0237 1.1520 0.0056  -0.3886 -0.0783 190 ARG   X CG  
42491 C  CD  . ARG   X  190 ? 2.1252 1.2066 1.1664 -0.0032 -0.4120 -0.1103 190 ARG   X CD  
42492 N  NE  . ARG   X  190 ? 2.2093 1.2444 1.1898 0.0410  -0.4602 -0.1099 190 ARG   X NE  
42493 C  CZ  . ARG   X  190 ? 2.1985 1.3248 1.2203 0.0889  -0.4773 -0.1192 190 ARG   X CZ  
42494 N  NH1 . ARG   X  190 ? 2.2245 1.3964 1.2689 0.0640  -0.4380 -0.0848 190 ARG   X NH1 
42495 N  NH2 . ARG   X  190 ? 2.2804 1.2585 1.1757 0.0892  -0.4999 -0.1369 190 ARG   X NH2 
42496 N  N   . GLN   X  191 ? 2.0271 0.8417 1.1640 0.0012  -0.3306 0.0164  191 GLN   X N   
42497 C  CA  . GLN   X  191 ? 2.0807 0.9063 1.2601 0.0062  -0.3379 -0.1052 191 GLN   X CA  
42498 C  C   . GLN   X  191 ? 2.1892 0.9924 1.2118 -0.0070 -0.3615 -0.1089 191 GLN   X C   
42499 O  O   . GLN   X  191 ? 2.2469 1.0771 1.2823 0.0538  -0.3132 -0.1603 191 GLN   X O   
42500 C  CB  . GLN   X  191 ? 2.0486 0.9231 1.3387 0.0005  -0.3063 -0.1101 191 GLN   X CB  
42501 C  CG  . GLN   X  191 ? 2.0310 0.9269 1.4067 -0.0046 -0.2833 -0.1325 191 GLN   X CG  
42502 C  CD  . GLN   X  191 ? 2.0098 0.8954 1.4718 -0.0350 -0.2554 -0.1556 191 GLN   X CD  
42503 O  OE1 . GLN   X  191 ? 2.0704 0.8930 1.5488 -0.0713 -0.2093 -0.2280 191 GLN   X OE1 
42504 N  NE2 . GLN   X  191 ? 2.0145 0.9195 1.5145 -0.0238 -0.2686 -0.1298 191 GLN   X NE2 
42505 N  N   . VAL   X  192 ? 2.2210 0.9756 1.2499 -0.0416 -0.4016 -0.1726 192 VAL   X N   
42506 C  CA  . VAL   X  192 ? 2.2607 0.9904 1.2389 -0.0611 -0.4182 -0.1709 192 VAL   X CA  
42507 C  C   . VAL   X  192 ? 2.3297 1.1364 1.3948 -0.1704 -0.3433 -0.1827 192 VAL   X C   
42508 O  O   . VAL   X  192 ? 2.4152 1.1424 1.4028 -0.2238 -0.2747 -0.2312 192 VAL   X O   
42509 C  CB  . VAL   X  192 ? 2.2005 0.8985 1.1656 -0.0907 -0.5059 -0.1508 192 VAL   X CB  
42510 C  CG1 . VAL   X  192 ? 2.2187 0.9368 1.1580 -0.0852 -0.4964 -0.1330 192 VAL   X CG1 
42511 C  CG2 . VAL   X  192 ? 2.1792 0.8304 1.1087 -0.0535 -0.5434 -0.1721 192 VAL   X CG2 
42512 N  N   . ASP   X  193 ? 2.5935 1.3902 1.3906 -0.1282 -0.2580 -0.2300 193 ASP   X N   
42513 C  CA  . ASP   X  193 ? 2.5977 1.5757 1.5553 -0.1227 -0.2202 -0.2473 193 ASP   X CA  
42514 C  C   . ASP   X  193 ? 2.7311 1.6026 1.6389 -0.0296 -0.2428 -0.1301 193 ASP   X C   
42515 O  O   . ASP   X  193 ? 2.7192 1.6911 1.8231 -0.1381 -0.2130 -0.0395 193 ASP   X O   
42516 C  CB  . ASP   X  193 ? 2.7400 1.6558 1.5644 -0.1293 -0.1864 -0.3218 193 ASP   X CB  
42517 C  CG  . ASP   X  193 ? 2.8101 1.6520 1.5410 -0.1118 -0.1658 -0.3706 193 ASP   X CG  
42518 O  OD1 . ASP   X  193 ? 2.8821 1.6653 1.6012 -0.0798 -0.2140 -0.3309 193 ASP   X OD1 
42519 O  OD2 . ASP   X  193 ? 2.8538 1.6619 1.6870 -0.0746 -0.0664 -0.3710 193 ASP   X OD2 
42520 N  N   . ASP   X  194 ? 2.8165 1.7909 1.6135 0.0544  -0.2732 -0.1082 194 ASP   X N   
42521 C  CA  . ASP   X  194 ? 2.7890 1.7926 1.6369 0.1267  -0.2089 -0.1279 194 ASP   X CA  
42522 C  C   . ASP   X  194 ? 2.7758 1.6225 1.5104 0.0998  -0.2813 -0.1513 194 ASP   X C   
42523 O  O   . ASP   X  194 ? 2.7327 1.6573 1.6158 0.1985  -0.2468 -0.1908 194 ASP   X O   
42524 C  CB  . ASP   X  194 ? 2.9476 2.0086 1.6437 0.1317  -0.2075 -0.1045 194 ASP   X CB  
42525 C  CG  . ASP   X  194 ? 3.0051 2.1421 1.6134 0.1539  -0.2528 -0.1846 194 ASP   X CG  
42526 O  OD1 . ASP   X  194 ? 2.9635 2.2713 1.7955 0.1515  -0.2279 -0.1923 194 ASP   X OD1 
42527 O  OD2 . ASP   X  194 ? 3.0875 2.3030 1.5614 0.2154  -0.2277 -0.0988 194 ASP   X OD2 
42528 N  N   . PHE   X  195 ? 2.6021 1.3749 1.4891 0.1158  -0.1910 -0.1397 195 PHE   X N   
42529 C  CA  . PHE   X  195 ? 2.4993 1.3290 1.4416 0.0684  -0.2122 -0.1055 195 PHE   X CA  
42530 C  C   . PHE   X  195 ? 2.4357 1.2978 1.5059 0.0871  -0.1630 -0.1222 195 PHE   X C   
42531 O  O   . PHE   X  195 ? 2.3467 1.1513 1.4248 0.0222  -0.1469 -0.2641 195 PHE   X O   
42532 C  CB  . PHE   X  195 ? 2.4619 1.2936 1.4683 0.0845  -0.2454 -0.0693 195 PHE   X CB  
42533 C  CG  . PHE   X  195 ? 2.4126 1.2423 1.4321 0.0607  -0.2936 -0.0136 195 PHE   X CG  
42534 C  CD1 . PHE   X  195 ? 2.4056 1.1775 1.4610 0.0859  -0.2600 0.0083  195 PHE   X CD1 
42535 C  CD2 . PHE   X  195 ? 2.4180 1.2391 1.3649 0.0743  -0.3261 0.0191  195 PHE   X CD2 
42536 C  CE1 . PHE   X  195 ? 2.3741 1.1206 1.4212 0.0824  -0.3119 0.0085  195 PHE   X CE1 
42537 C  CE2 . PHE   X  195 ? 2.3831 1.1886 1.3568 0.0660  -0.3673 0.0205  195 PHE   X CE2 
42538 C  CZ  . PHE   X  195 ? 2.3627 1.1358 1.4017 0.1056  -0.3457 0.0272  195 PHE   X CZ  
42539 N  N   . THR   Y  1   ? 1.6476 0.6756 1.3875 -0.0734 -0.0671 -0.0441 2   THR   Y N   
42540 C  CA  . THR   Y  1   ? 1.6420 0.6777 1.3906 -0.0882 -0.0774 -0.0077 2   THR   Y CA  
42541 C  C   . THR   Y  1   ? 1.6297 0.7429 1.3561 -0.0454 -0.0776 -0.0310 2   THR   Y C   
42542 O  O   . THR   Y  1   ? 1.5952 0.7050 1.2687 -0.1281 -0.0548 -0.0757 2   THR   Y O   
42543 C  CB  . THR   Y  1   ? 1.6605 0.7161 1.3869 -0.1249 -0.0961 0.0136  2   THR   Y CB  
42544 O  OG1 . THR   Y  1   ? 1.6887 0.7163 1.3390 -0.2105 -0.0948 0.0185  2   THR   Y OG1 
42545 C  CG2 . THR   Y  1   ? 1.6712 0.6836 1.3680 -0.1614 -0.0821 0.0475  2   THR   Y CG2 
42546 N  N   . THR   Y  2   ? 1.5810 0.7493 1.3417 -0.0050 -0.0906 -0.0224 3   THR   Y N   
42547 C  CA  . THR   Y  2   ? 1.5994 0.8296 1.3587 0.0333  -0.0576 -0.0680 3   THR   Y CA  
42548 C  C   . THR   Y  2   ? 1.6232 0.7446 1.3143 -0.0082 -0.0330 -0.0263 3   THR   Y C   
42549 O  O   . THR   Y  2   ? 1.6175 0.6800 1.3193 -0.0536 0.0338  -0.0079 3   THR   Y O   
42550 C  CB  . THR   Y  2   ? 1.5513 0.8528 1.3508 0.0714  -0.0695 -0.0473 3   THR   Y CB  
42551 O  OG1 . THR   Y  2   ? 1.5204 0.9979 1.3773 0.1505  -0.0945 -0.1161 3   THR   Y OG1 
42552 C  CG2 . THR   Y  2   ? 1.5694 0.8780 1.3645 0.1115  -0.0871 -0.0506 3   THR   Y CG2 
42553 N  N   . LEU   Y  3   ? 1.6699 0.7763 1.3436 -0.0184 -0.0052 -0.0519 4   LEU   Y N   
42554 C  CA  . LEU   Y  3   ? 1.7030 0.8772 1.3899 -0.0434 -0.0352 -0.1082 4   LEU   Y CA  
42555 C  C   . LEU   Y  3   ? 1.7122 0.8286 1.4137 -0.0671 -0.0180 -0.0922 4   LEU   Y C   
42556 O  O   . LEU   Y  3   ? 1.6937 0.8155 1.3833 -0.0767 0.0128  -0.1060 4   LEU   Y O   
42557 C  CB  . LEU   Y  3   ? 1.7479 0.8832 1.4027 -0.0170 -0.0811 -0.1197 4   LEU   Y CB  
42558 C  CG  . LEU   Y  3   ? 1.7221 0.9914 1.4342 -0.0255 -0.0601 -0.1859 4   LEU   Y CG  
42559 C  CD1 . LEU   Y  3   ? 1.6679 1.0455 1.4936 -0.0223 -0.0708 -0.1768 4   LEU   Y CD1 
42560 C  CD2 . LEU   Y  3   ? 1.7022 1.0547 1.4162 -0.0090 -0.0556 -0.1926 4   LEU   Y CD2 
42561 N  N   . ALA   Y  4   ? 1.7445 0.7615 1.4633 -0.1103 -0.0233 -0.0867 5   ALA   Y N   
42562 C  CA  . ALA   Y  4   ? 1.8046 0.7729 1.4707 -0.0776 -0.0081 -0.0815 5   ALA   Y CA  
42563 C  C   . ALA   Y  4   ? 1.8830 0.7583 1.4122 -0.1067 -0.0127 -0.0787 5   ALA   Y C   
42564 O  O   . ALA   Y  4   ? 1.8548 0.6299 1.3324 -0.1278 -0.0925 -0.0733 5   ALA   Y O   
42565 C  CB  . ALA   Y  4   ? 1.7966 0.7891 1.5293 -0.0474 -0.0095 -0.0433 5   ALA   Y CB  
42566 N  N   . PHE   Y  5   ? 1.9141 0.8193 1.4426 -0.1101 0.0377  -0.0828 6   PHE   Y N   
42567 C  CA  . PHE   Y  5   ? 1.9220 0.8971 1.4607 -0.1071 0.0260  -0.0945 6   PHE   Y CA  
42568 C  C   . PHE   Y  5   ? 1.9911 0.8788 1.4838 -0.1077 0.0370  -0.0997 6   PHE   Y C   
42569 O  O   . PHE   Y  5   ? 1.9997 0.8248 1.5164 -0.1028 0.0493  -0.1213 6   PHE   Y O   
42570 C  CB  . PHE   Y  5   ? 1.9131 0.8869 1.5163 -0.1165 0.0503  -0.1096 6   PHE   Y CB  
42571 C  CG  . PHE   Y  5   ? 1.9107 0.9580 1.5854 -0.1058 0.0924  -0.1448 6   PHE   Y CG  
42572 C  CD1 . PHE   Y  5   ? 1.9234 1.0498 1.6092 -0.1374 0.1356  -0.1550 6   PHE   Y CD1 
42573 C  CD2 . PHE   Y  5   ? 1.8144 0.9507 1.5701 -0.0795 0.1160  -0.1383 6   PHE   Y CD2 
42574 C  CE1 . PHE   Y  5   ? 1.9264 1.0691 1.6381 -0.1495 0.1447  -0.1598 6   PHE   Y CE1 
42575 C  CE2 . PHE   Y  5   ? 1.8139 0.9930 1.6160 -0.0877 0.1224  -0.1256 6   PHE   Y CE2 
42576 C  CZ  . PHE   Y  5   ? 1.8697 1.0371 1.6364 -0.1242 0.1537  -0.1500 6   PHE   Y CZ  
42577 N  N   . ARG   Y  6   ? 2.0820 0.9451 1.4812 -0.0990 0.0014  -0.1311 7   ARG   Y N   
42578 C  CA  . ARG   Y  6   ? 2.1417 1.0135 1.4907 -0.0824 0.0134  -0.1645 7   ARG   Y CA  
42579 C  C   . ARG   Y  6   ? 2.2365 1.1180 1.4145 -0.1045 0.0531  -0.2041 7   ARG   Y C   
42580 O  O   . ARG   Y  6   ? 2.3016 1.0810 1.2277 -0.1546 0.0279  -0.1283 7   ARG   Y O   
42581 C  CB  . ARG   Y  6   ? 2.1305 0.9719 1.5327 -0.0577 -0.0332 -0.1869 7   ARG   Y CB  
42582 C  CG  . ARG   Y  6   ? 2.0920 0.9581 1.5449 -0.0385 -0.0341 -0.2258 7   ARG   Y CG  
42583 C  CD  . ARG   Y  6   ? 2.0623 0.9558 1.5311 -0.0164 -0.0844 -0.2163 7   ARG   Y CD  
42584 N  NE  . ARG   Y  6   ? 2.0594 0.9195 1.5737 -0.0323 -0.1238 -0.2065 7   ARG   Y NE  
42585 C  CZ  . ARG   Y  6   ? 2.0879 1.0134 1.5397 -0.0563 -0.1672 -0.2057 7   ARG   Y CZ  
42586 N  NH1 . ARG   Y  6   ? 2.1104 1.0124 1.5313 -0.0520 -0.1361 -0.2263 7   ARG   Y NH1 
42587 N  NH2 . ARG   Y  6   ? 2.1291 1.0059 1.6002 -0.0421 -0.1959 -0.1696 7   ARG   Y NH2 
42588 N  N   . PHE   Y  7   ? 2.2755 1.1307 1.4605 -0.0494 0.0591  -0.2270 8   PHE   Y N   
42589 C  CA  . PHE   Y  7   ? 2.3024 1.1347 1.4670 -0.0567 0.1139  -0.2673 8   PHE   Y CA  
42590 C  C   . PHE   Y  7   ? 2.3444 1.1465 1.5035 -0.0365 0.1683  -0.2627 8   PHE   Y C   
42591 O  O   . PHE   Y  7   ? 2.3365 1.0963 1.4250 -0.0088 0.1962  -0.3322 8   PHE   Y O   
42592 C  CB  . PHE   Y  7   ? 2.3005 1.1160 1.5866 -0.0408 0.1054  -0.3283 8   PHE   Y CB  
42593 C  CG  . PHE   Y  7   ? 2.3201 1.0577 1.6463 0.0069  0.1041  -0.3855 8   PHE   Y CG  
42594 C  CD1 . PHE   Y  7   ? 2.2605 0.9297 1.6602 0.0264  0.1393  -0.3843 8   PHE   Y CD1 
42595 C  CD2 . PHE   Y  7   ? 2.3558 1.1155 1.6847 -0.0052 0.1424  -0.4453 8   PHE   Y CD2 
42596 C  CE1 . PHE   Y  7   ? 2.2741 0.9066 1.6971 0.0544  0.1312  -0.4090 8   PHE   Y CE1 
42597 C  CE2 . PHE   Y  7   ? 2.3624 1.0927 1.7137 0.0143  0.1465  -0.4586 8   PHE   Y CE2 
42598 C  CZ  . PHE   Y  7   ? 2.3034 0.9877 1.7459 0.0417  0.1687  -0.4438 8   PHE   Y CZ  
42599 N  N   . GLN   Y  8   ? 2.3858 1.2433 1.4863 -0.0868 0.1816  -0.2953 9   GLN   Y N   
42600 C  CA  . GLN   Y  8   ? 2.4185 1.2319 1.4061 -0.1507 0.1628  -0.2901 9   GLN   Y CA  
42601 C  C   . GLN   Y  8   ? 2.3926 1.1784 1.4606 -0.1150 0.2123  -0.3403 9   GLN   Y C   
42602 O  O   . GLN   Y  8   ? 2.3191 1.1652 1.3993 -0.0991 0.2113  -0.2740 9   GLN   Y O   
42603 C  CB  . GLN   Y  8   ? 2.4975 1.3551 1.4219 -0.2160 0.1474  -0.2391 9   GLN   Y CB  
42604 C  CG  . GLN   Y  8   ? 2.5145 1.4249 1.4613 -0.2419 0.2060  -0.2210 9   GLN   Y CG  
42605 C  CD  . GLN   Y  8   ? 2.4790 1.5203 1.4801 -0.2486 0.2193  -0.2040 9   GLN   Y CD  
42606 O  OE1 . GLN   Y  8   ? 2.4497 1.3884 1.4418 -0.2499 0.2959  -0.2100 9   GLN   Y OE1 
42607 N  NE2 . GLN   Y  8   ? 2.4925 1.5538 1.5154 -0.2994 0.1781  -0.1392 9   GLN   Y NE2 
42608 N  N   . GLY   Y  9   ? 2.3275 1.1234 1.5359 -0.0703 0.2337  -0.3581 10  GLY   Y N   
42609 C  CA  . GLY   Y  9   ? 2.2878 1.0094 1.5725 -0.0520 0.3019  -0.3946 10  GLY   Y CA  
42610 C  C   . GLY   Y  9   ? 2.1890 0.8781 1.5821 -0.0447 0.3218  -0.4413 10  GLY   Y C   
42611 O  O   . GLY   Y  9   ? 2.1946 0.7901 1.5952 -0.0954 0.3568  -0.4254 10  GLY   Y O   
42612 N  N   . GLY   Y  10  ? 2.1629 0.8489 1.5216 -0.0709 0.3027  -0.3832 11  GLY   Y N   
42613 C  CA  . GLY   Y  10  ? 2.1044 0.8463 1.5621 -0.0340 0.2723  -0.3344 11  GLY   Y CA  
42614 C  C   . GLY   Y  10  ? 2.0327 0.8760 1.5453 -0.0121 0.2905  -0.2826 11  GLY   Y C   
42615 O  O   . GLY   Y  10  ? 2.0247 0.9545 1.6081 -0.0152 0.2600  -0.2237 11  GLY   Y O   
42616 N  N   . ILE   Y  11  ? 1.9346 0.8735 1.6187 0.0326  0.2609  -0.2163 12  ILE   Y N   
42617 C  CA  . ILE   Y  11  ? 1.8565 0.8646 1.6007 0.0371  0.2253  -0.2076 12  ILE   Y CA  
42618 C  C   . ILE   Y  11  ? 1.7939 0.9210 1.6299 0.0450  0.2507  -0.2122 12  ILE   Y C   
42619 O  O   . ILE   Y  11  ? 1.8043 0.6893 1.6555 0.0031  0.3105  -0.2706 12  ILE   Y O   
42620 C  CB  . ILE   Y  11  ? 1.8285 0.8676 1.5958 0.0810  0.2046  -0.1721 12  ILE   Y CB  
42621 C  CG1 . ILE   Y  11  ? 1.8412 0.8758 1.6424 0.0552  0.1876  -0.1292 12  ILE   Y CG1 
42622 C  CG2 . ILE   Y  11  ? 1.7554 0.8817 1.5201 0.0799  0.1794  -0.1280 12  ILE   Y CG2 
42623 C  CD1 . ILE   Y  11  ? 1.8313 0.8877 1.6582 0.0991  0.1956  -0.0948 12  ILE   Y CD1 
42624 N  N   . ILE   Y  12  ? 1.7777 0.9430 1.5943 0.0423  0.2343  -0.2383 13  ILE   Y N   
42625 C  CA  . ILE   Y  12  ? 1.7263 0.9969 1.5286 0.0612  0.2447  -0.2279 13  ILE   Y CA  
42626 C  C   . ILE   Y  12  ? 1.6609 0.9301 1.4876 0.0827  0.1931  -0.2133 13  ILE   Y C   
42627 O  O   . ILE   Y  12  ? 1.6677 0.8535 1.3865 0.0877  0.1900  -0.2101 13  ILE   Y O   
42628 C  CB  . ILE   Y  12  ? 1.7541 1.0047 1.5897 0.0708  0.2423  -0.1996 13  ILE   Y CB  
42629 C  CG1 . ILE   Y  12  ? 1.8109 1.0968 1.6275 0.0636  0.2878  -0.1956 13  ILE   Y CG1 
42630 C  CG2 . ILE   Y  12  ? 1.7106 1.0027 1.5871 0.1038  0.2470  -0.2100 13  ILE   Y CG2 
42631 C  CD1 . ILE   Y  12  ? 1.8066 1.1282 1.6689 0.0812  0.2965  -0.2100 13  ILE   Y CD1 
42632 N  N   . VAL   Y  13  ? 1.6555 0.9271 1.4154 0.0709  0.2215  -0.2285 14  VAL   Y N   
42633 C  CA  . VAL   Y  13  ? 1.6231 0.9206 1.3996 0.1010  0.1830  -0.2204 14  VAL   Y CA  
42634 C  C   . VAL   Y  13  ? 1.6330 0.8834 1.3778 0.1110  0.1620  -0.1817 14  VAL   Y C   
42635 O  O   . VAL   Y  13  ? 1.6445 0.9282 1.3569 0.1352  0.2045  -0.1937 14  VAL   Y O   
42636 C  CB  . VAL   Y  13  ? 1.5817 0.9249 1.3641 0.1244  0.1795  -0.2360 14  VAL   Y CB  
42637 C  CG1 . VAL   Y  13  ? 1.5249 0.9586 1.3531 0.1406  0.1558  -0.2352 14  VAL   Y CG1 
42638 C  CG2 . VAL   Y  13  ? 1.5943 0.9432 1.3974 0.1208  0.1811  -0.2632 14  VAL   Y CG2 
42639 N  N   . ALA   Y  14  ? 1.6819 0.8264 1.3264 0.1139  0.1115  -0.1392 15  ALA   Y N   
42640 C  CA  . ALA   Y  14  ? 1.6978 0.7830 1.3056 0.0845  0.0997  -0.0681 15  ALA   Y CA  
42641 C  C   . ALA   Y  14  ? 1.6955 0.6624 1.2465 0.1072  0.0381  -0.0331 15  ALA   Y C   
42642 O  O   . ALA   Y  14  ? 1.6954 0.6228 1.2061 0.1179  0.0196  -0.0249 15  ALA   Y O   
42643 C  CB  . ALA   Y  14  ? 1.7237 0.7856 1.3155 0.0196  0.1226  -0.0649 15  ALA   Y CB  
42644 N  N   . VAL   Y  15  ? 1.7121 0.6118 1.2474 0.1130  0.0298  -0.0228 16  VAL   Y N   
42645 C  CA  . VAL   Y  15  ? 1.7110 0.6336 1.2440 0.1332  0.0302  -0.0060 16  VAL   Y CA  
42646 C  C   . VAL   Y  15  ? 1.7033 0.5808 1.2561 0.1352  0.0212  0.0620  16  VAL   Y C   
42647 O  O   . VAL   Y  15  ? 1.7274 0.6191 1.2695 0.1251  0.0417  0.1403  16  VAL   Y O   
42648 C  CB  . VAL   Y  15  ? 1.7241 0.6012 1.2022 0.1199  0.0425  -0.0457 16  VAL   Y CB  
42649 C  CG1 . VAL   Y  15  ? 1.7150 0.6090 1.2096 0.1245  0.0562  -0.0666 16  VAL   Y CG1 
42650 C  CG2 . VAL   Y  15  ? 1.7362 0.6152 1.2218 0.1378  0.0378  -0.0658 16  VAL   Y CG2 
42651 N  N   . ASP   Y  16  ? 1.6700 0.5271 1.2670 0.1750  0.0103  0.0806  17  ASP   Y N   
42652 C  CA  . ASP   Y  16  ? 1.6388 0.6253 1.3461 0.1372  0.0093  0.0694  17  ASP   Y CA  
42653 C  C   . ASP   Y  16  ? 1.5982 0.7165 1.3551 0.1752  -0.0173 0.0607  17  ASP   Y C   
42654 O  O   . ASP   Y  16  ? 1.6379 0.7660 1.3943 0.0832  -0.0605 0.0192  17  ASP   Y O   
42655 C  CB  . ASP   Y  16  ? 1.6406 0.6109 1.3610 0.1223  0.0102  0.0700  17  ASP   Y CB  
42656 C  CG  . ASP   Y  16  ? 1.6425 0.5773 1.3470 0.1199  -0.0040 0.0583  17  ASP   Y CG  
42657 O  OD1 . ASP   Y  16  ? 1.6189 0.6723 1.4385 0.0872  -0.0146 0.1170  17  ASP   Y OD1 
42658 O  OD2 . ASP   Y  16  ? 1.6082 0.4262 1.4185 0.1363  0.0058  0.0551  17  ASP   Y OD2 
42659 N  N   . SER   Y  17  ? 1.5608 0.6979 1.3661 0.1745  0.0042  0.0467  18  SER   Y N   
42660 C  CA  . SER   Y  17  ? 1.5363 0.7357 1.3758 0.1830  0.0046  0.0559  18  SER   Y CA  
42661 C  C   . SER   Y  17  ? 1.5312 0.6996 1.3767 0.2030  0.0065  0.0693  18  SER   Y C   
42662 O  O   . SER   Y  17  ? 1.5310 0.6823 1.4171 0.2950  0.0064  0.0703  18  SER   Y O   
42663 C  CB  . SER   Y  17  ? 1.5250 0.7968 1.3566 0.1503  0.0155  0.0667  18  SER   Y CB  
42664 O  OG  . SER   Y  17  ? 1.5424 0.7152 1.3555 0.1978  0.0309  0.0538  18  SER   Y OG  
42665 N  N   . ARG   Y  18  ? 1.4910 0.7417 1.4099 0.1884  0.0218  0.1233  19  ARG   Y N   
42666 C  CA  . ARG   Y  18  ? 1.5233 0.7878 1.3919 0.1717  0.0265  0.1303  19  ARG   Y CA  
42667 C  C   . ARG   Y  18  ? 1.5320 0.7109 1.3925 0.2013  0.0196  0.1770  19  ARG   Y C   
42668 O  O   . ARG   Y  18  ? 1.4957 0.6066 1.2844 0.2473  0.0759  0.2384  19  ARG   Y O   
42669 C  CB  . ARG   Y  18  ? 1.5601 0.7876 1.4248 0.1874  0.0159  0.0987  19  ARG   Y CB  
42670 C  CG  . ARG   Y  18  ? 1.6181 0.8956 1.4050 0.1555  -0.0009 0.0850  19  ARG   Y CG  
42671 C  CD  . ARG   Y  18  ? 1.6680 0.8908 1.3945 0.1443  0.0008  0.1054  19  ARG   Y CD  
42672 N  NE  . ARG   Y  18  ? 1.6790 0.8952 1.4314 0.1348  -0.0245 0.0857  19  ARG   Y NE  
42673 C  CZ  . ARG   Y  18  ? 1.7183 0.9213 1.4572 0.1009  -0.0208 0.1220  19  ARG   Y CZ  
42674 N  NH1 . ARG   Y  18  ? 1.7081 0.9833 1.4652 0.0892  -0.0412 0.1110  19  ARG   Y NH1 
42675 N  NH2 . ARG   Y  18  ? 1.6632 0.9819 1.4405 0.1361  -0.0029 0.1957  19  ARG   Y NH2 
42676 N  N   . ALA   Y  19  ? 1.5529 0.8507 1.4069 0.1879  -0.0351 0.1415  20  ALA   Y N   
42677 C  CA  . ALA   Y  19  ? 1.5409 0.9414 1.3988 0.1872  -0.0129 0.0669  20  ALA   Y CA  
42678 C  C   . ALA   Y  19  ? 1.5165 0.9171 1.4176 0.1712  -0.0518 0.0600  20  ALA   Y C   
42679 O  O   . ALA   Y  19  ? 1.5550 0.7074 1.3760 0.1672  -0.0253 0.0792  20  ALA   Y O   
42680 C  CB  . ALA   Y  19  ? 1.5807 0.9781 1.4336 0.1937  -0.0702 0.0905  20  ALA   Y CB  
42681 N  N   . THR   Y  20  ? 1.5206 1.0451 1.4318 0.1962  -0.0506 0.0739  21  THR   Y N   
42682 C  CA  . THR   Y  20  ? 1.5552 1.1258 1.4269 0.1818  -0.0593 0.0461  21  THR   Y CA  
42683 C  C   . THR   Y  20  ? 1.5845 1.3284 1.4167 0.1398  -0.0337 0.0164  21  THR   Y C   
42684 O  O   . THR   Y  20  ? 1.6206 1.3467 1.3617 0.1414  -0.0531 -0.0997 21  THR   Y O   
42685 C  CB  . THR   Y  20  ? 1.5589 1.1038 1.4562 0.1498  0.0005  0.1188  21  THR   Y CB  
42686 O  OG1 . THR   Y  20  ? 1.5182 1.0366 1.4750 0.1718  0.0190  0.2143  21  THR   Y OG1 
42687 C  CG2 . THR   Y  20  ? 1.4909 1.0917 1.4845 0.1373  -0.0077 0.1180  21  THR   Y CG2 
42688 N  N   . ALA   Y  21  ? 1.6795 1.4899 1.5273 0.1225  -0.1528 -0.0596 22  ALA   Y N   
42689 C  CA  . ALA   Y  21  ? 1.6881 1.4409 1.5701 0.1720  -0.1467 -0.0116 22  ALA   Y CA  
42690 C  C   . ALA   Y  21  ? 1.7406 1.3526 1.6541 0.1266  -0.1876 -0.0018 22  ALA   Y C   
42691 O  O   . ALA   Y  21  ? 1.5752 1.1764 1.6241 0.2276  -0.1551 0.0431  22  ALA   Y O   
42692 C  CB  . ALA   Y  21  ? 1.7147 1.5307 1.6447 0.1537  -0.2212 0.0204  22  ALA   Y CB  
42693 N  N   . GLY   Y  22  ? 1.7712 1.2457 1.6654 0.1669  -0.1612 0.0474  23  GLY   Y N   
42694 C  CA  . GLY   Y  22  ? 1.8722 1.1899 1.6198 0.0991  -0.1010 0.0644  23  GLY   Y CA  
42695 C  C   . GLY   Y  22  ? 1.8927 1.2123 1.6953 0.0698  -0.0941 0.1042  23  GLY   Y C   
42696 O  O   . GLY   Y  22  ? 1.9322 1.2511 1.6574 0.0139  -0.1056 0.2105  23  GLY   Y O   
42697 N  N   . ASN   Y  23  ? 1.8955 1.1674 1.6368 0.0842  -0.0142 0.0911  24  ASN   Y N   
42698 C  CA  . ASN   Y  23  ? 1.8392 1.1788 1.6818 0.1110  0.0238  0.0913  24  ASN   Y CA  
42699 C  C   . ASN   Y  23  ? 1.8299 1.0333 1.5675 0.0932  0.0164  0.1003  24  ASN   Y C   
42700 O  O   . ASN   Y  23  ? 1.7326 0.9979 1.5170 0.0921  -0.0200 0.0371  24  ASN   Y O   
42701 C  CB  . ASN   Y  23  ? 1.9037 1.1873 1.7876 0.0900  0.0655  0.0638  24  ASN   Y CB  
42702 C  CG  . ASN   Y  23  ? 1.8708 1.3094 1.8969 0.0563  0.0856  0.0679  24  ASN   Y CG  
42703 O  OD1 . ASN   Y  23  ? 1.7986 1.2794 1.9383 0.0122  0.0835  0.0066  24  ASN   Y OD1 
42704 N  ND2 . ASN   Y  23  ? 1.9139 1.4212 1.8615 0.0105  0.0982  0.0368  24  ASN   Y ND2 
42705 N  N   . TRP   Y  24  ? 1.7940 1.0198 1.5513 0.1435  -0.0025 0.0387  25  TRP   Y N   
42706 C  CA  . TRP   Y  24  ? 1.7909 0.8970 1.5264 0.1213  -0.0079 0.0347  25  TRP   Y CA  
42707 C  C   . TRP   Y  24  ? 1.7774 0.9056 1.5131 0.1776  0.0780  0.0876  25  TRP   Y C   
42708 O  O   . TRP   Y  24  ? 1.8006 0.9045 1.5116 0.1751  0.0841  0.1043  25  TRP   Y O   
42709 C  CB  . TRP   Y  24  ? 1.7840 0.8498 1.5149 0.1104  -0.0505 -0.0016 25  TRP   Y CB  
42710 C  CG  . TRP   Y  24  ? 1.6852 0.9220 1.5384 0.0932  -0.0834 -0.0067 25  TRP   Y CG  
42711 C  CD1 . TRP   Y  24  ? 1.6651 0.8973 1.5730 0.1589  -0.0845 0.0431  25  TRP   Y CD1 
42712 C  CD2 . TRP   Y  24  ? 1.6811 0.8642 1.5401 0.0774  -0.1065 -0.0033 25  TRP   Y CD2 
42713 N  NE1 . TRP   Y  24  ? 1.6426 0.8658 1.5956 0.1227  -0.1275 0.0683  25  TRP   Y NE1 
42714 C  CE2 . TRP   Y  24  ? 1.6584 0.8918 1.5688 0.1016  -0.1361 0.0335  25  TRP   Y CE2 
42715 C  CE3 . TRP   Y  24  ? 1.6805 0.8495 1.5384 0.0746  -0.0906 0.0306  25  TRP   Y CE3 
42716 C  CZ2 . TRP   Y  24  ? 1.6541 0.8796 1.5856 0.0601  -0.1370 0.0375  25  TRP   Y CZ2 
42717 C  CZ3 . TRP   Y  24  ? 1.6825 0.9078 1.5733 0.0440  -0.1020 0.0451  25  TRP   Y CZ3 
42718 C  CH2 . TRP   Y  24  ? 1.7064 0.8901 1.5958 0.0316  -0.1124 0.0408  25  TRP   Y CH2 
42719 N  N   . VAL   Y  25  ? 1.7429 0.8355 1.5593 0.1195  0.0586  0.0684  26  VAL   Y N   
42720 C  CA  . VAL   Y  25  ? 1.6550 0.9085 1.5776 0.1344  0.0664  0.0464  26  VAL   Y CA  
42721 C  C   . VAL   Y  25  ? 1.5833 0.8988 1.5350 0.0725  0.0554  0.0634  26  VAL   Y C   
42722 O  O   . VAL   Y  25  ? 1.5681 0.9530 1.5275 0.0341  0.0723  0.0785  26  VAL   Y O   
42723 C  CB  . VAL   Y  25  ? 1.5967 0.8715 1.6561 0.1238  0.0709  0.0359  26  VAL   Y CB  
42724 C  CG1 . VAL   Y  25  ? 1.5565 0.9983 1.6869 0.1558  0.0885  0.0154  26  VAL   Y CG1 
42725 C  CG2 . VAL   Y  25  ? 1.6212 0.8273 1.6710 0.1325  0.0932  0.0178  26  VAL   Y CG2 
42726 N  N   . ALA   Y  26  ? 1.6552 0.8504 1.5353 0.0884  0.0283  0.0253  27  ALA   Y N   
42727 C  CA  . ALA   Y  26  ? 1.6915 0.8081 1.5213 0.0303  -0.0303 0.0175  27  ALA   Y CA  
42728 C  C   . ALA   Y  26  ? 1.6320 0.7851 1.5537 -0.0298 -0.0407 -0.0100 27  ALA   Y C   
42729 O  O   . ALA   Y  26  ? 1.5832 0.6136 1.6092 -0.2111 -0.0798 -0.0496 27  ALA   Y O   
42730 C  CB  . ALA   Y  26  ? 1.6615 0.8477 1.4750 0.0381  -0.0194 0.0352  27  ALA   Y CB  
42731 N  N   . SER   Y  27  ? 1.6745 0.8176 1.5207 0.0232  0.0236  -0.0201 28  SER   Y N   
42732 C  CA  . SER   Y  27  ? 1.6459 0.9307 1.5485 0.0632  0.0610  0.0413  28  SER   Y CA  
42733 C  C   . SER   Y  27  ? 1.6055 0.8525 1.5944 0.0492  0.0572  0.0673  28  SER   Y C   
42734 O  O   . SER   Y  27  ? 1.6624 0.4971 1.5217 0.0585  0.1488  0.0886  28  SER   Y O   
42735 C  CB  . SER   Y  27  ? 1.6552 0.9157 1.5755 0.1383  0.0587  0.0441  28  SER   Y CB  
42736 O  OG  . SER   Y  27  ? 1.6383 0.9173 1.6465 0.2206  0.0586  0.0409  28  SER   Y OG  
42737 N  N   . GLN   Y  28  ? 1.5732 0.9981 1.6386 -0.0234 0.0408  0.0672  29  GLN   Y N   
42738 C  CA  . GLN   Y  28  ? 1.5956 0.9860 1.6062 0.0185  -0.0354 0.0267  29  GLN   Y CA  
42739 C  C   . GLN   Y  28  ? 1.6187 1.0793 1.5578 0.0101  -0.0304 -0.0207 29  GLN   Y C   
42740 O  O   . GLN   Y  28  ? 1.5811 0.9577 1.5546 0.0459  -0.0247 -0.0308 29  GLN   Y O   
42741 C  CB  . GLN   Y  28  ? 1.5878 1.0271 1.6394 -0.0061 -0.0693 0.0297  29  GLN   Y CB  
42742 C  CG  . GLN   Y  28  ? 1.5998 1.1152 1.5960 -0.0453 -0.0839 -0.0479 29  GLN   Y CG  
42743 C  CD  . GLN   Y  28  ? 1.6044 1.0955 1.5844 -0.0617 -0.0765 -0.0532 29  GLN   Y CD  
42744 O  OE1 . GLN   Y  28  ? 1.5801 1.2588 1.6826 -0.0695 -0.0855 -0.0908 29  GLN   Y OE1 
42745 N  NE2 . GLN   Y  28  ? 1.6041 1.1106 1.5448 -0.0839 -0.0614 -0.0645 29  GLN   Y NE2 
42746 N  N   . THR   Y  29  ? 1.6490 1.0889 1.5807 0.0627  -0.0573 -0.0239 30  THR   Y N   
42747 C  CA  . THR   Y  29  ? 1.6350 1.1310 1.6349 0.1217  -0.0476 -0.0093 30  THR   Y CA  
42748 C  C   . THR   Y  29  ? 1.6495 1.1553 1.6384 0.0995  -0.0679 -0.0133 30  THR   Y C   
42749 O  O   . THR   Y  29  ? 1.8102 1.1686 1.7393 0.0767  -0.0884 -0.1292 30  THR   Y O   
42750 C  CB  . THR   Y  29  ? 1.5947 1.2797 1.6888 0.0668  -0.0665 -0.0322 30  THR   Y CB  
42751 O  OG1 . THR   Y  29  ? 1.7002 1.5252 1.5718 0.0412  -0.0367 -0.0846 30  THR   Y OG1 
42752 C  CG2 . THR   Y  29  ? 1.5507 1.2543 1.6269 0.0846  -0.0726 -0.0135 30  THR   Y CG2 
42753 N  N   . VAL   Y  30  ? 1.6527 0.9966 1.5133 0.0786  -0.0398 0.0091  31  VAL   Y N   
42754 C  CA  . VAL   Y  30  ? 1.6250 1.0305 1.4481 0.0722  -0.0060 0.0113  31  VAL   Y CA  
42755 C  C   . VAL   Y  30  ? 1.6326 0.9977 1.4394 0.1154  0.0034  0.0168  31  VAL   Y C   
42756 O  O   . VAL   Y  30  ? 1.6246 0.8308 1.4503 0.2342  -0.0053 -0.0624 31  VAL   Y O   
42757 C  CB  . VAL   Y  30  ? 1.6496 1.0536 1.3869 0.0472  0.0128  -0.0110 31  VAL   Y CB  
42758 C  CG1 . VAL   Y  30  ? 1.6473 1.1381 1.3967 0.0120  0.0234  0.0146  31  VAL   Y CG1 
42759 C  CG2 . VAL   Y  30  ? 1.6253 0.9797 1.4221 0.0358  0.0253  -0.0391 31  VAL   Y CG2 
42760 N  N   . LYS   Y  31  ? 1.6781 0.9909 1.4608 0.0809  -0.0181 0.0676  32  LYS   Y N   
42761 C  CA  . LYS   Y  31  ? 1.7172 0.9071 1.5008 0.0728  -0.0004 0.0598  32  LYS   Y CA  
42762 C  C   . LYS   Y  31  ? 1.7154 0.8426 1.5508 0.0974  -0.0015 0.0792  32  LYS   Y C   
42763 O  O   . LYS   Y  31  ? 1.8322 0.8643 1.5414 0.1686  -0.0021 0.1397  32  LYS   Y O   
42764 C  CB  . LYS   Y  31  ? 1.6938 1.0037 1.5466 0.1582  0.0447  0.0566  32  LYS   Y CB  
42765 C  CG  . LYS   Y  31  ? 1.7095 1.1616 1.6299 0.1319  0.0790  0.0472  32  LYS   Y CG  
42766 C  CD  . LYS   Y  31  ? 1.7619 1.2482 1.7254 0.1540  0.1333  -0.0249 32  LYS   Y CD  
42767 C  CE  . LYS   Y  31  ? 1.7923 1.2170 1.7585 0.1124  0.1609  -0.0776 32  LYS   Y CE  
42768 N  NZ  . LYS   Y  31  ? 1.8070 1.2078 1.8618 0.1455  0.1953  -0.0469 32  LYS   Y NZ  
42769 N  N   . LYS   Y  32  ? 1.6035 0.7942 1.5839 0.1189  0.0229  0.0445  33  LYS   Y N   
42770 C  CA  . LYS   Y  32  ? 1.5988 0.7858 1.5286 0.1393  -0.0054 -0.0072 33  LYS   Y CA  
42771 C  C   . LYS   Y  32  ? 1.5983 0.7640 1.5239 0.1496  -0.0112 -0.0085 33  LYS   Y C   
42772 O  O   . LYS   Y  32  ? 1.5835 0.6215 1.4107 0.1881  0.0262  -0.0247 33  LYS   Y O   
42773 C  CB  . LYS   Y  32  ? 1.5696 0.7959 1.5236 0.1396  -0.0280 -0.0089 33  LYS   Y CB  
42774 C  CG  . LYS   Y  32  ? 1.5454 0.8801 1.5321 0.0981  -0.0573 -0.0332 33  LYS   Y CG  
42775 C  CD  . LYS   Y  32  ? 1.5321 0.8601 1.5065 0.0773  -0.0488 -0.0485 33  LYS   Y CD  
42776 C  CE  . LYS   Y  32  ? 1.5570 0.8710 1.5080 0.0397  -0.0474 -0.0421 33  LYS   Y CE  
42777 N  NZ  . LYS   Y  32  ? 1.5749 0.8829 1.4846 0.0363  -0.0622 0.0032  33  LYS   Y NZ  
42778 N  N   . VAL   Y  33  ? 1.6295 0.7749 1.5323 0.1491  -0.0404 -0.0668 34  VAL   Y N   
42779 C  CA  . VAL   Y  33  ? 1.7023 0.7063 1.6104 0.1500  -0.0878 -0.0550 34  VAL   Y CA  
42780 C  C   . VAL   Y  33  ? 1.7047 0.6753 1.6864 0.1372  -0.1132 -0.0649 34  VAL   Y C   
42781 O  O   . VAL   Y  33  ? 1.7596 0.4376 1.7122 0.1725  -0.1869 -0.0658 34  VAL   Y O   
42782 C  CB  . VAL   Y  33  ? 1.7873 0.7359 1.5656 0.1441  -0.1130 -0.0739 34  VAL   Y CB  
42783 C  CG1 . VAL   Y  33  ? 1.8250 0.7848 1.5642 0.1201  -0.1246 -0.0937 34  VAL   Y CG1 
42784 C  CG2 . VAL   Y  33  ? 1.8106 0.7617 1.5118 0.1583  -0.1256 -0.0711 34  VAL   Y CG2 
42785 N  N   . ILE   Y  34  ? 1.6266 0.7439 1.7293 0.1258  -0.1040 -0.0260 35  ILE   Y N   
42786 C  CA  . ILE   Y  34  ? 1.6199 0.6815 1.8222 0.0914  -0.0689 -0.0596 35  ILE   Y CA  
42787 C  C   . ILE   Y  34  ? 1.6641 0.5714 1.8478 0.0999  -0.0107 -0.0427 35  ILE   Y C   
42788 O  O   . ILE   Y  34  ? 1.6873 0.4671 1.7042 0.1330  0.0325  -0.1256 35  ILE   Y O   
42789 C  CB  . ILE   Y  34  ? 1.5703 0.7261 1.8441 0.1212  -0.0654 -0.0562 35  ILE   Y CB  
42790 C  CG1 . ILE   Y  34  ? 1.6200 0.8115 1.9161 0.1501  -0.0859 0.0489  35  ILE   Y CG1 
42791 C  CG2 . ILE   Y  34  ? 1.5540 0.7478 1.7974 0.1530  -0.0239 -0.0620 35  ILE   Y CG2 
42792 C  CD1 . ILE   Y  34  ? 1.6469 0.9351 1.9400 0.1174  -0.0867 -0.0057 35  ILE   Y CD1 
42793 N  N   . GLU   Y  35  ? 1.6713 0.6114 1.9406 0.1245  0.0040  0.0060  36  GLU   Y N   
42794 C  CA  . GLU   Y  35  ? 1.7133 0.7166 1.9937 0.1393  0.0208  -0.0332 36  GLU   Y CA  
42795 C  C   . GLU   Y  35  ? 1.7066 0.7292 1.9557 0.0686  -0.0262 -0.0976 36  GLU   Y C   
42796 O  O   . GLU   Y  35  ? 1.9004 0.4598 1.9469 0.0097  -0.0713 -0.1550 36  GLU   Y O   
42797 C  CB  . GLU   Y  35  ? 1.6904 0.8125 2.2169 0.1308  0.0156  0.0889  36  GLU   Y CB  
42798 C  CG  . GLU   Y  35  ? 1.7077 0.7595 2.3174 0.1864  -0.0210 0.1528  36  GLU   Y CG  
42799 C  CD  . GLU   Y  35  ? 1.6873 0.8401 2.4728 0.1974  -0.0003 0.2122  36  GLU   Y CD  
42800 O  OE1 . GLU   Y  35  ? 1.7168 0.9161 2.5756 0.2588  -0.0079 0.1835  36  GLU   Y OE1 
42801 O  OE2 . GLU   Y  35  ? 1.7242 0.7799 2.6041 0.2608  -0.0466 0.2604  36  GLU   Y OE2 
42802 N  N   . ILE   Y  36  ? 1.7083 0.7191 1.8907 0.0435  -0.0265 -0.1382 37  ILE   Y N   
42803 C  CA  . ILE   Y  36  ? 1.6338 0.8023 1.8905 0.0111  -0.0642 -0.0879 37  ILE   Y CA  
42804 C  C   . ILE   Y  36  ? 1.6218 0.7512 1.9411 0.0617  -0.1016 -0.0339 37  ILE   Y C   
42805 O  O   . ILE   Y  36  ? 1.5729 0.7193 2.0224 0.0501  -0.1575 -0.0431 37  ILE   Y O   
42806 C  CB  . ILE   Y  36  ? 1.6334 0.8749 1.8143 0.0328  -0.0334 -0.1231 37  ILE   Y CB  
42807 C  CG1 . ILE   Y  36  ? 1.6087 0.8361 1.7314 0.0111  -0.0777 -0.1272 37  ILE   Y CG1 
42808 C  CG2 . ILE   Y  36  ? 1.6918 0.9082 1.8646 -0.0176 -0.0347 -0.0339 37  ILE   Y CG2 
42809 C  CD1 . ILE   Y  36  ? 1.6027 0.8149 1.6543 0.0284  -0.0539 -0.1563 37  ILE   Y CD1 
42810 N  N   . ASN   Y  37  ? 1.6809 0.7830 1.9393 0.0865  -0.0362 -0.1351 38  ASN   Y N   
42811 C  CA  . ASN   Y  37  ? 1.7719 0.7815 2.0811 0.1413  -0.0053 -0.1716 38  ASN   Y CA  
42812 C  C   . ASN   Y  37  ? 1.7754 0.8522 2.0865 0.1000  0.1199  -0.2714 38  ASN   Y C   
42813 O  O   . ASN   Y  37  ? 1.8051 0.8606 2.0608 0.0729  0.1895  -0.2125 38  ASN   Y O   
42814 C  CB  . ASN   Y  37  ? 1.7940 0.7989 2.1325 0.1217  -0.0260 -0.1486 38  ASN   Y CB  
42815 C  CG  . ASN   Y  37  ? 1.7773 0.8608 2.2175 0.1032  -0.0689 -0.1543 38  ASN   Y CG  
42816 O  OD1 . ASN   Y  37  ? 1.8126 0.9843 2.2315 0.0951  -0.0235 -0.1291 38  ASN   Y OD1 
42817 N  ND2 . ASN   Y  37  ? 1.8240 0.7854 2.2455 0.0694  -0.0836 -0.0986 38  ASN   Y ND2 
42818 N  N   . PRO   Y  38  ? 1.7997 0.9163 2.2108 0.1733  0.1554  -0.2944 39  PRO   Y N   
42819 C  CA  . PRO   Y  38  ? 1.8506 0.9153 2.2153 0.1571  0.1882  -0.3274 39  PRO   Y CA  
42820 C  C   . PRO   Y  38  ? 1.8602 0.8571 2.1123 0.1801  0.1673  -0.4832 39  PRO   Y C   
42821 O  O   . PRO   Y  38  ? 1.8658 0.6873 2.0849 0.1819  0.2344  -0.6509 39  PRO   Y O   
42822 C  CB  . PRO   Y  38  ? 1.8763 0.9677 2.2882 0.2153  0.2370  -0.3023 39  PRO   Y CB  
42823 C  CG  . PRO   Y  38  ? 1.8653 1.0629 2.3528 0.1991  0.1884  -0.2361 39  PRO   Y CG  
42824 C  CD  . PRO   Y  38  ? 1.8187 0.9585 2.2987 0.2326  0.1411  -0.2311 39  PRO   Y CD  
42825 N  N   . PHE   Y  39  ? 1.8575 0.9686 2.0002 0.1617  0.1517  -0.4830 40  PHE   Y N   
42826 C  CA  . PHE   Y  39  ? 1.8278 1.0419 1.9261 0.1790  0.1721  -0.5338 40  PHE   Y CA  
42827 C  C   . PHE   Y  39  ? 1.7081 0.9357 1.7697 0.1872  0.0894  -0.4119 40  PHE   Y C   
42828 O  O   . PHE   Y  39  ? 1.6412 0.9967 1.8353 0.1806  0.0861  -0.3935 40  PHE   Y O   
42829 C  CB  . PHE   Y  39  ? 1.8920 1.2219 1.9311 0.1325  0.1661  -0.6365 40  PHE   Y CB  
42830 C  CG  . PHE   Y  39  ? 1.9983 1.2436 2.0812 0.2184  0.2070  -0.7988 40  PHE   Y CG  
42831 C  CD1 . PHE   Y  39  ? 2.0755 1.3459 1.9798 0.2097  0.2435  -0.8622 40  PHE   Y CD1 
42832 C  CD2 . PHE   Y  39  ? 2.0253 1.2001 2.1211 0.2203  0.2334  -0.9185 40  PHE   Y CD2 
42833 C  CE1 . PHE   Y  39  ? 2.1191 1.2946 2.0215 0.1930  0.2543  -0.9499 40  PHE   Y CE1 
42834 C  CE2 . PHE   Y  39  ? 2.0121 1.3552 2.1619 0.2630  0.2857  -0.8897 40  PHE   Y CE2 
42835 C  CZ  . PHE   Y  39  ? 2.0670 1.4148 2.1066 0.2317  0.2990  -0.8983 40  PHE   Y CZ  
42836 N  N   . LEU   Y  40  ? 1.6972 0.9091 1.7560 0.1906  0.0505  -0.2930 41  LEU   Y N   
42837 C  CA  . LEU   Y  40  ? 1.6854 0.8920 1.6565 0.2178  0.0193  -0.2110 41  LEU   Y CA  
42838 C  C   . LEU   Y  40  ? 1.7077 0.8532 1.6386 0.2242  -0.0053 -0.1750 41  LEU   Y C   
42839 O  O   . LEU   Y  40  ? 1.8109 0.5576 1.6710 0.2964  -0.0380 -0.1846 41  LEU   Y O   
42840 C  CB  . LEU   Y  40  ? 1.6843 0.9061 1.6262 0.2238  -0.0098 -0.1874 41  LEU   Y CB  
42841 C  CG  . LEU   Y  40  ? 1.7005 0.8927 1.5567 0.2064  -0.0047 -0.2088 41  LEU   Y CG  
42842 C  CD1 . LEU   Y  40  ? 1.6853 0.8669 1.5046 0.2280  -0.0383 -0.1996 41  LEU   Y CD1 
42843 C  CD2 . LEU   Y  40  ? 1.7393 0.9053 1.5222 0.1900  0.0086  -0.1819 41  LEU   Y CD2 
42844 N  N   . LEU   Y  41  ? 1.6844 0.8798 1.5507 0.2396  0.0336  -0.1455 42  LEU   Y N   
42845 C  CA  . LEU   Y  41  ? 1.6453 0.9073 1.4672 0.1952  0.0395  -0.1120 42  LEU   Y CA  
42846 C  C   . LEU   Y  41  ? 1.6688 0.8513 1.3868 0.1810  0.0373  -0.0815 42  LEU   Y C   
42847 O  O   . LEU   Y  41  ? 1.6861 0.8439 1.3368 0.2126  0.0301  -0.0140 42  LEU   Y O   
42848 C  CB  . LEU   Y  41  ? 1.6185 0.8892 1.4899 0.1846  0.0487  -0.1261 42  LEU   Y CB  
42849 C  CG  . LEU   Y  41  ? 1.6205 0.9856 1.5610 0.1755  0.0548  -0.1278 42  LEU   Y CG  
42850 C  CD1 . LEU   Y  41  ? 1.6013 0.9732 1.5708 0.2210  0.0903  -0.1236 42  LEU   Y CD1 
42851 C  CD2 . LEU   Y  41  ? 1.6302 1.0168 1.5761 0.1714  0.0463  -0.1032 42  LEU   Y CD2 
42852 N  N   . GLY   Y  42  ? 1.6375 0.8165 1.3933 0.1407  0.0322  -0.0736 43  GLY   Y N   
42853 C  CA  . GLY   Y  42  ? 1.5880 0.9152 1.3827 0.1782  0.0389  0.0078  43  GLY   Y CA  
42854 C  C   . GLY   Y  42  ? 1.5619 0.8936 1.3979 0.1869  0.0521  0.0515  43  GLY   Y C   
42855 O  O   . GLY   Y  42  ? 1.5156 0.9911 1.4730 0.1790  0.0941  0.0363  43  GLY   Y O   
42856 N  N   . THR   Y  43  ? 1.5457 0.9741 1.3675 0.2013  -0.0020 0.1196  44  THR   Y N   
42857 C  CA  . THR   Y  43  ? 1.5839 0.9815 1.3852 0.0835  -0.0455 0.1351  44  THR   Y CA  
42858 C  C   . THR   Y  43  ? 1.6039 0.8823 1.3459 0.0914  -0.1034 0.1503  44  THR   Y C   
42859 O  O   . THR   Y  43  ? 1.6344 1.0318 1.3157 0.0683  -0.0672 0.2256  44  THR   Y O   
42860 C  CB  . THR   Y  43  ? 1.6289 0.9625 1.3749 0.0471  -0.0516 0.1669  44  THR   Y CB  
42861 O  OG1 . THR   Y  43  ? 1.6263 1.1107 1.4748 0.0372  -0.1124 0.1699  44  THR   Y OG1 
42862 C  CG2 . THR   Y  43  ? 1.5858 0.9663 1.4233 -0.0126 -0.0125 0.1499  44  THR   Y CG2 
42863 N  N   . MET   Y  44  ? 1.5441 0.7027 1.4473 0.1136  -0.1056 0.1743  45  MET   Y N   
42864 C  CA  . MET   Y  44  ? 1.5094 0.7413 1.4491 0.1289  -0.1177 0.1631  45  MET   Y CA  
42865 C  C   . MET   Y  44  ? 1.4817 0.7661 1.4724 0.1633  -0.0478 0.2005  45  MET   Y C   
42866 O  O   . MET   Y  44  ? 1.5064 0.8789 1.6165 0.0895  -0.0175 0.2144  45  MET   Y O   
42867 C  CB  . MET   Y  44  ? 1.5056 0.7201 1.4771 0.1343  -0.1434 0.0929  45  MET   Y CB  
42868 C  CG  . MET   Y  44  ? 1.4802 0.7353 1.4889 0.1655  -0.2069 0.1027  45  MET   Y CG  
42869 S  SD  . MET   Y  44  ? 1.4739 0.7167 1.5084 0.1685  -0.2372 0.0503  45  MET   Y SD  
42870 C  CE  . MET   Y  44  ? 1.4819 0.8314 1.6178 0.2290  -0.2055 -0.0258 45  MET   Y CE  
42871 N  N   . ALA   Y  45  ? 1.5185 0.7845 1.4047 0.2102  -0.0382 0.1962  46  ALA   Y N   
42872 C  CA  . ALA   Y  45  ? 1.5888 0.7475 1.4235 0.1667  -0.0674 0.1434  46  ALA   Y CA  
42873 C  C   . ALA   Y  45  ? 1.6064 0.6719 1.3661 0.2246  -0.0939 0.0907  46  ALA   Y C   
42874 O  O   . ALA   Y  45  ? 1.5840 0.7266 1.4365 0.1979  -0.0730 0.1488  46  ALA   Y O   
42875 C  CB  . ALA   Y  45  ? 1.5754 0.7208 1.4675 0.1606  -0.0864 0.1312  46  ALA   Y CB  
42876 N  N   . GLY   Y  46  ? 1.5863 0.6063 1.4356 0.2078  -0.1213 0.0897  47  GLY   Y N   
42877 C  CA  . GLY   Y  46  ? 1.5718 0.5936 1.4463 0.1694  -0.1105 0.0344  47  GLY   Y CA  
42878 C  C   . GLY   Y  46  ? 1.5754 0.6476 1.4245 0.1425  -0.1442 -0.0036 47  GLY   Y C   
42879 O  O   . GLY   Y  46  ? 1.5901 0.6266 1.4895 0.1354  -0.1199 -0.0104 47  GLY   Y O   
42880 N  N   . GLY   Y  47  ? 1.5364 0.7382 1.3638 0.1049  -0.1183 -0.0505 48  GLY   Y N   
42881 C  CA  . GLY   Y  47  ? 1.5353 0.7564 1.3268 0.1108  -0.1271 -0.0937 48  GLY   Y CA  
42882 C  C   . GLY   Y  47  ? 1.5117 0.7502 1.3444 0.0882  -0.1293 -0.1118 48  GLY   Y C   
42883 O  O   . GLY   Y  47  ? 1.5648 0.7710 1.3630 0.0509  -0.1558 -0.1103 48  GLY   Y O   
42884 N  N   . ALA   Y  48  ? 1.5053 0.7573 1.3164 0.0598  -0.0952 -0.1127 49  ALA   Y N   
42885 C  CA  . ALA   Y  48  ? 1.4941 0.7815 1.2602 0.0480  -0.0680 -0.0737 49  ALA   Y CA  
42886 C  C   . ALA   Y  48  ? 1.5003 0.7888 1.1969 0.0791  -0.0755 -0.0684 49  ALA   Y C   
42887 O  O   . ALA   Y  48  ? 1.4562 0.7957 1.1943 0.1046  -0.0405 -0.0593 49  ALA   Y O   
42888 C  CB  . ALA   Y  48  ? 1.4820 0.7938 1.2787 0.0365  -0.0501 -0.0649 49  ALA   Y CB  
42889 N  N   . ALA   Y  49  ? 1.5516 0.7907 1.2177 0.0651  -0.1065 0.0160  50  ALA   Y N   
42890 C  CA  . ALA   Y  49  ? 1.5510 0.7465 1.2382 0.0675  -0.0974 -0.0233 50  ALA   Y CA  
42891 C  C   . ALA   Y  49  ? 1.5315 0.6019 1.1999 0.1253  -0.1026 0.0108  50  ALA   Y C   
42892 O  O   . ALA   Y  49  ? 1.5419 0.6028 1.2340 0.1626  -0.1116 0.0348  50  ALA   Y O   
42893 C  CB  . ALA   Y  49  ? 1.6012 0.7940 1.2418 0.0301  -0.0741 0.0071  50  ALA   Y CB  
42894 N  N   . ASP   Y  50  ? 1.5311 0.6039 1.1743 0.1279  -0.1032 0.0163  51  ASP   Y N   
42895 C  CA  . ASP   Y  50  ? 1.5279 0.5801 1.2079 0.1404  -0.1107 0.0143  51  ASP   Y CA  
42896 C  C   . ASP   Y  50  ? 1.4785 0.6334 1.2408 0.1801  -0.0903 0.0088  51  ASP   Y C   
42897 O  O   . ASP   Y  50  ? 1.4172 0.6308 1.3223 0.1495  -0.1223 0.0179  51  ASP   Y O   
42898 C  CB  . ASP   Y  50  ? 1.5389 0.5939 1.1684 0.1443  -0.0989 -0.0096 51  ASP   Y CB  
42899 C  CG  . ASP   Y  50  ? 1.6150 0.6071 1.1571 0.1234  -0.1051 -0.0164 51  ASP   Y CG  
42900 O  OD1 . ASP   Y  50  ? 1.6351 0.4946 1.2387 0.1461  -0.1100 0.0103  51  ASP   Y OD1 
42901 O  OD2 . ASP   Y  50  ? 1.6611 0.6422 1.1457 0.1509  -0.1006 -0.1057 51  ASP   Y OD2 
42902 N  N   . CYS   Y  51  ? 1.4853 0.6405 1.2378 0.2006  -0.0414 -0.0022 52  CYS   Y N   
42903 C  CA  . CYS   Y  51  ? 1.5148 0.6646 1.2416 0.2084  -0.0499 -0.0382 52  CYS   Y CA  
42904 C  C   . CYS   Y  51  ? 1.4950 0.6921 1.2083 0.2086  -0.0729 -0.0370 52  CYS   Y C   
42905 O  O   . CYS   Y  51  ? 1.5062 0.6937 1.1468 0.2025  -0.0913 -0.0158 52  CYS   Y O   
42906 C  CB  . CYS   Y  51  ? 1.5453 0.6652 1.2549 0.2018  -0.0451 -0.0355 52  CYS   Y CB  
42907 S  SG  . CYS   Y  51  ? 1.5313 0.6703 1.3303 0.1844  -0.0851 0.0027  52  CYS   Y SG  
42908 N  N   . GLN   Y  52  ? 1.4896 0.7028 1.2397 0.1981  -0.0731 -0.0500 53  GLN   Y N   
42909 C  CA  . GLN   Y  52  ? 1.4726 0.7058 1.2766 0.1853  -0.0742 -0.0687 53  GLN   Y CA  
42910 C  C   . GLN   Y  52  ? 1.4643 0.6661 1.2504 0.1991  -0.0656 -0.1268 53  GLN   Y C   
42911 O  O   . GLN   Y  52  ? 1.4659 0.6063 1.3041 0.2156  -0.1010 -0.1157 53  GLN   Y O   
42912 C  CB  . GLN   Y  52  ? 1.4492 0.7461 1.3201 0.1832  -0.0995 -0.0573 53  GLN   Y CB  
42913 C  CG  . GLN   Y  52  ? 1.4536 0.7699 1.3873 0.1957  -0.1300 -0.0490 53  GLN   Y CG  
42914 C  CD  . GLN   Y  52  ? 1.4702 0.7833 1.4822 0.1802  -0.1555 -0.0547 53  GLN   Y CD  
42915 O  OE1 . GLN   Y  52  ? 1.5559 0.7285 1.5698 0.1899  -0.1918 -0.0061 53  GLN   Y OE1 
42916 N  NE2 . GLN   Y  52  ? 1.4563 0.7980 1.4785 0.1856  -0.1745 -0.0299 53  GLN   Y NE2 
42917 N  N   . PHE   Y  53  ? 1.4686 0.5783 1.2261 0.1509  -0.0904 -0.1044 54  PHE   Y N   
42918 C  CA  . PHE   Y  53  ? 1.4569 0.5369 1.2581 0.1647  -0.1196 -0.1220 54  PHE   Y CA  
42919 C  C   . PHE   Y  53  ? 1.4435 0.5551 1.2605 0.1561  -0.1461 -0.0884 54  PHE   Y C   
42920 O  O   . PHE   Y  53  ? 1.4131 0.6079 1.3687 0.1655  -0.1750 -0.1766 54  PHE   Y O   
42921 C  CB  . PHE   Y  53  ? 1.4611 0.5071 1.2514 0.1055  -0.1180 -0.1064 54  PHE   Y CB  
42922 C  CG  . PHE   Y  53  ? 1.4347 0.5629 1.2280 0.0418  -0.1182 -0.0905 54  PHE   Y CG  
42923 C  CD1 . PHE   Y  53  ? 1.4431 0.5782 1.2269 0.0199  -0.1219 -0.0639 54  PHE   Y CD1 
42924 C  CD2 . PHE   Y  53  ? 1.4522 0.5228 1.1894 0.0311  -0.0979 -0.0947 54  PHE   Y CD2 
42925 C  CE1 . PHE   Y  53  ? 1.4286 0.5312 1.2274 0.0323  -0.1481 -0.1006 54  PHE   Y CE1 
42926 C  CE2 . PHE   Y  53  ? 1.4555 0.4757 1.1864 0.0366  -0.1224 -0.1332 54  PHE   Y CE2 
42927 C  CZ  . PHE   Y  53  ? 1.4503 0.4727 1.2147 0.0388  -0.1359 -0.1331 54  PHE   Y CZ  
42928 N  N   . TRP   Y  54  ? 1.4463 0.4742 1.2326 0.1557  -0.1226 -0.0875 55  TRP   Y N   
42929 C  CA  . TRP   Y  54  ? 1.4537 0.4621 1.2389 0.1341  -0.1236 -0.0614 55  TRP   Y CA  
42930 C  C   . TRP   Y  54  ? 1.4784 0.4551 1.2510 0.1226  -0.1219 -0.1104 55  TRP   Y C   
42931 O  O   . TRP   Y  54  ? 1.4833 0.5053 1.1970 0.0835  -0.1272 -0.1097 55  TRP   Y O   
42932 C  CB  . TRP   Y  54  ? 1.4448 0.4690 1.1932 0.1250  -0.1242 -0.0358 55  TRP   Y CB  
42933 C  CG  . TRP   Y  54  ? 1.4921 0.4944 1.1802 0.0989  -0.1386 -0.0009 55  TRP   Y CG  
42934 C  CD1 . TRP   Y  54  ? 1.5210 0.5032 1.1715 0.0795  -0.1123 0.0046  55  TRP   Y CD1 
42935 C  CD2 . TRP   Y  54  ? 1.4967 0.5112 1.1751 0.0917  -0.1339 0.0052  55  TRP   Y CD2 
42936 N  NE1 . TRP   Y  54  ? 1.5284 0.5247 1.1935 0.0688  -0.0924 0.0084  55  TRP   Y NE1 
42937 C  CE2 . TRP   Y  54  ? 1.5237 0.5259 1.1837 0.0739  -0.1146 0.0062  55  TRP   Y CE2 
42938 C  CE3 . TRP   Y  54  ? 1.4736 0.5050 1.1600 0.1119  -0.1368 0.0157  55  TRP   Y CE3 
42939 C  CZ2 . TRP   Y  54  ? 1.5428 0.5102 1.1804 0.0810  -0.1348 0.0172  55  TRP   Y CZ2 
42940 C  CZ3 . TRP   Y  54  ? 1.4944 0.4993 1.1856 0.1074  -0.1572 0.0376  55  TRP   Y CZ3 
42941 C  CH2 . TRP   Y  54  ? 1.5236 0.4917 1.1825 0.0999  -0.1530 0.0438  55  TRP   Y CH2 
42942 N  N   . GLU   Y  55  ? 1.5001 0.5233 1.3253 0.1181  -0.0761 -0.0793 56  GLU   Y N   
42943 C  CA  . GLU   Y  55  ? 1.5921 0.5884 1.3292 0.1320  -0.0904 -0.1184 56  GLU   Y CA  
42944 C  C   . GLU   Y  55  ? 1.6082 0.5189 1.3570 0.1052  -0.1160 -0.1259 56  GLU   Y C   
42945 O  O   . GLU   Y  55  ? 1.6373 0.4229 1.4045 0.0587  -0.1156 -0.1221 56  GLU   Y O   
42946 C  CB  . GLU   Y  55  ? 1.6484 0.5807 1.3952 0.1896  -0.0809 -0.0739 56  GLU   Y CB  
42947 C  CG  . GLU   Y  55  ? 1.6430 0.6398 1.4048 0.2120  -0.0785 -0.0854 56  GLU   Y CG  
42948 C  CD  . GLU   Y  55  ? 1.6532 0.6226 1.4476 0.2603  -0.0681 -0.0664 56  GLU   Y CD  
42949 O  OE1 . GLU   Y  55  ? 1.7233 0.7879 1.4887 0.2306  -0.0018 -0.0700 56  GLU   Y OE1 
42950 O  OE2 . GLU   Y  55  ? 1.6581 0.5783 1.5690 0.2450  -0.0770 -0.0800 56  GLU   Y OE2 
42951 N  N   . THR   Y  56  ? 1.6076 0.5820 1.3633 0.1097  -0.1206 -0.0947 57  THR   Y N   
42952 C  CA  . THR   Y  56  ? 1.5727 0.6448 1.3318 0.1263  -0.1300 -0.1186 57  THR   Y CA  
42953 C  C   . THR   Y  56  ? 1.5559 0.6750 1.3268 0.1331  -0.1084 -0.0663 57  THR   Y C   
42954 O  O   . THR   Y  56  ? 1.5244 0.6529 1.3385 0.1444  -0.1171 -0.0297 57  THR   Y O   
42955 C  CB  . THR   Y  56  ? 1.5939 0.7053 1.3180 0.1192  -0.1392 -0.1360 57  THR   Y CB  
42956 O  OG1 . THR   Y  56  ? 1.5695 0.7607 1.2705 0.0616  -0.1861 -0.2039 57  THR   Y OG1 
42957 C  CG2 . THR   Y  56  ? 1.5830 0.7413 1.3167 0.0950  -0.1358 -0.0948 57  THR   Y CG2 
42958 N  N   . TRP   Y  57  ? 1.5542 0.6675 1.2603 0.1525  -0.1282 -0.0753 58  TRP   Y N   
42959 C  CA  . TRP   Y  57  ? 1.5456 0.6140 1.2288 0.1761  -0.1510 -0.1006 58  TRP   Y CA  
42960 C  C   . TRP   Y  57  ? 1.5728 0.5960 1.2121 0.1935  -0.1075 -0.1597 58  TRP   Y C   
42961 O  O   . TRP   Y  57  ? 1.6388 0.6221 1.2617 0.1517  -0.0828 -0.2099 58  TRP   Y O   
42962 C  CB  . TRP   Y  57  ? 1.4695 0.5428 1.1925 0.1390  -0.1961 -0.0770 58  TRP   Y CB  
42963 C  CG  . TRP   Y  57  ? 1.4931 0.4636 1.1772 0.1515  -0.2413 -0.0912 58  TRP   Y CG  
42964 C  CD1 . TRP   Y  57  ? 1.4758 0.4188 1.2004 0.1180  -0.2570 -0.1181 58  TRP   Y CD1 
42965 C  CD2 . TRP   Y  57  ? 1.4862 0.3933 1.1806 0.1080  -0.2380 -0.1004 58  TRP   Y CD2 
42966 N  NE1 . TRP   Y  57  ? 1.4900 0.3712 1.1683 0.1218  -0.2646 -0.1201 58  TRP   Y NE1 
42967 C  CE2 . TRP   Y  57  ? 1.4833 0.3551 1.1493 0.1208  -0.2538 -0.1269 58  TRP   Y CE2 
42968 C  CE3 . TRP   Y  57  ? 1.4970 0.4473 1.1679 0.0888  -0.2609 -0.0834 58  TRP   Y CE3 
42969 C  CZ2 . TRP   Y  57  ? 1.4946 0.3209 1.1119 0.0933  -0.2478 -0.1288 58  TRP   Y CZ2 
42970 C  CZ3 . TRP   Y  57  ? 1.5196 0.3935 1.1276 0.0547  -0.2571 -0.1130 58  TRP   Y CZ3 
42971 C  CH2 . TRP   Y  57  ? 1.5083 0.3470 1.0952 0.0879  -0.2601 -0.1254 58  TRP   Y CH2 
42972 N  N   . LEU   Y  58  ? 1.5693 0.6242 1.1771 0.2342  -0.0902 -0.1758 59  LEU   Y N   
42973 C  CA  . LEU   Y  58  ? 1.6085 0.6077 1.1946 0.1908  -0.0969 -0.2218 59  LEU   Y CA  
42974 C  C   . LEU   Y  58  ? 1.6209 0.6166 1.2401 0.1924  -0.0583 -0.1935 59  LEU   Y C   
42975 O  O   . LEU   Y  58  ? 1.5916 0.6010 1.2661 0.1218  -0.0831 -0.1375 59  LEU   Y O   
42976 C  CB  . LEU   Y  58  ? 1.6291 0.6150 1.1352 0.1891  -0.0980 -0.2291 59  LEU   Y CB  
42977 C  CG  . LEU   Y  58  ? 1.6644 0.5812 1.1174 0.1557  -0.0802 -0.2648 59  LEU   Y CG  
42978 C  CD1 . LEU   Y  58  ? 1.6708 0.5845 1.0763 0.1506  -0.0981 -0.2643 59  LEU   Y CD1 
42979 C  CD2 . LEU   Y  58  ? 1.6985 0.6031 1.0572 0.1327  -0.0826 -0.2377 59  LEU   Y CD2 
42980 N  N   . GLY   Y  59  ? 1.6339 0.6835 1.2850 0.1726  -0.0238 -0.1595 60  GLY   Y N   
42981 C  CA  . GLY   Y  59  ? 1.6582 0.7219 1.3168 0.1910  0.0087  -0.1379 60  GLY   Y CA  
42982 C  C   . GLY   Y  59  ? 1.6764 0.7281 1.3244 0.1852  -0.0028 -0.1148 60  GLY   Y C   
42983 O  O   . GLY   Y  59  ? 1.6592 0.6605 1.3569 0.1389  0.0067  -0.1204 60  GLY   Y O   
42984 N  N   . SER   Y  60  ? 1.6978 0.7080 1.3326 0.2176  -0.0557 -0.0767 61  SER   Y N   
42985 C  CA  . SER   Y  60  ? 1.7260 0.6785 1.3684 0.2263  -0.0976 -0.1124 61  SER   Y CA  
42986 C  C   . SER   Y  60  ? 1.7327 0.5844 1.3648 0.2533  -0.1252 -0.0624 61  SER   Y C   
42987 O  O   . SER   Y  60  ? 1.8391 0.5807 1.3891 0.2778  -0.1191 -0.0483 61  SER   Y O   
42988 C  CB  . SER   Y  60  ? 1.6962 0.6724 1.3691 0.1789  -0.1337 -0.1034 61  SER   Y CB  
42989 O  OG  . SER   Y  60  ? 1.6587 0.8899 1.3703 0.1678  -0.1575 -0.1068 61  SER   Y OG  
42990 N  N   . GLN   Y  61  ? 1.7203 0.6025 1.3599 0.2503  -0.1127 -0.0933 62  GLN   Y N   
42991 C  CA  . GLN   Y  61  ? 1.7602 0.6344 1.3960 0.1989  -0.1104 -0.0896 62  GLN   Y CA  
42992 C  C   . GLN   Y  61  ? 1.7375 0.5571 1.4268 0.2100  -0.0992 -0.1866 62  GLN   Y C   
42993 O  O   . GLN   Y  61  ? 1.6853 0.5259 1.3604 0.2265  -0.0761 -0.1612 62  GLN   Y O   
42994 C  CB  . GLN   Y  61  ? 1.7434 0.7112 1.4014 0.2041  -0.1309 -0.0669 62  GLN   Y CB  
42995 C  CG  . GLN   Y  61  ? 1.7983 0.7767 1.3623 0.1668  -0.1969 -0.0258 62  GLN   Y CG  
42996 C  CD  . GLN   Y  61  ? 1.8407 0.7264 1.4080 0.1688  -0.2837 -0.0441 62  GLN   Y CD  
42997 O  OE1 . GLN   Y  61  ? 1.9237 0.6835 1.4717 0.1414  -0.2858 -0.0674 62  GLN   Y OE1 
42998 N  NE2 . GLN   Y  61  ? 1.8737 0.7848 1.4844 0.2544  -0.3234 -0.0299 62  GLN   Y NE2 
42999 N  N   . CYS   Y  62  ? 1.7728 0.6606 1.4293 0.2007  -0.0590 -0.1506 63  CYS   Y N   
43000 C  CA  . CYS   Y  62  ? 1.8153 0.6687 1.4242 0.2068  -0.0853 -0.2152 63  CYS   Y CA  
43001 C  C   . CYS   Y  62  ? 1.7998 0.6063 1.4353 0.1738  -0.0891 -0.2105 63  CYS   Y C   
43002 O  O   . CYS   Y  62  ? 1.7563 0.4380 1.4816 0.1966  -0.1286 -0.1848 63  CYS   Y O   
43003 C  CB  . CYS   Y  62  ? 1.9126 0.7178 1.4781 0.1301  -0.0816 -0.2109 63  CYS   Y CB  
43004 S  SG  . CYS   Y  62  ? 1.9533 0.7264 1.6477 0.1361  -0.1312 -0.2030 63  CYS   Y SG  
43005 N  N   . ARG   Y  63  ? 1.7316 0.6701 1.4819 0.1766  -0.0633 -0.1919 64  ARG   Y N   
43006 C  CA  . ARG   Y  63  ? 1.6765 0.7373 1.5312 0.1720  -0.0219 -0.2113 64  ARG   Y CA  
43007 C  C   . ARG   Y  63  ? 1.7117 0.7341 1.5065 0.1575  -0.0135 -0.2465 64  ARG   Y C   
43008 O  O   . ARG   Y  63  ? 1.7765 0.6447 1.5469 0.1723  -0.0251 -0.2112 64  ARG   Y O   
43009 C  CB  . ARG   Y  63  ? 1.6184 0.8028 1.5788 0.1672  -0.0211 -0.1626 64  ARG   Y CB  
43010 C  CG  . ARG   Y  63  ? 1.5955 0.8301 1.6458 0.1771  -0.0412 -0.1585 64  ARG   Y CG  
43011 C  CD  . ARG   Y  63  ? 1.5998 0.8532 1.6740 0.1817  -0.0207 -0.1952 64  ARG   Y CD  
43012 N  NE  . ARG   Y  63  ? 1.6045 0.8617 1.7519 0.1864  -0.0173 -0.2280 64  ARG   Y NE  
43013 C  CZ  . ARG   Y  63  ? 1.6118 0.8883 1.7743 0.1654  -0.0276 -0.2544 64  ARG   Y CZ  
43014 N  NH1 . ARG   Y  63  ? 1.6369 0.9096 1.7376 0.1453  -0.0163 -0.2751 64  ARG   Y NH1 
43015 N  NH2 . ARG   Y  63  ? 1.6447 0.8709 1.8716 0.1729  -0.0318 -0.2521 64  ARG   Y NH2 
43016 N  N   . LEU   Y  64  ? 1.6569 0.6967 1.5148 0.1093  -0.0348 -0.2396 65  LEU   Y N   
43017 C  CA  . LEU   Y  64  ? 1.6288 0.6360 1.5543 0.1521  -0.0315 -0.2578 65  LEU   Y CA  
43018 C  C   . LEU   Y  64  ? 1.6397 0.6117 1.5492 0.1395  -0.0296 -0.2411 65  LEU   Y C   
43019 O  O   . LEU   Y  64  ? 1.6952 0.6086 1.6449 0.1370  -0.0342 -0.2400 65  LEU   Y O   
43020 C  CB  . LEU   Y  64  ? 1.5613 0.6212 1.5467 0.1291  -0.0508 -0.2311 65  LEU   Y CB  
43021 C  CG  . LEU   Y  64  ? 1.5430 0.5937 1.5968 0.1624  -0.0628 -0.1912 65  LEU   Y CG  
43022 C  CD1 . LEU   Y  64  ? 1.5162 0.6181 1.5693 0.1467  -0.0675 -0.1515 65  LEU   Y CD1 
43023 C  CD2 . LEU   Y  64  ? 1.5640 0.5825 1.6390 0.1620  -0.0650 -0.2345 65  LEU   Y CD2 
43024 N  N   . HIS   Y  65  ? 1.6466 0.6494 1.5245 0.1175  -0.0422 -0.2109 66  HIS   Y N   
43025 C  CA  . HIS   Y  65  ? 1.7088 0.6245 1.5328 0.0722  -0.0670 -0.2134 66  HIS   Y CA  
43026 C  C   . HIS   Y  65  ? 1.7536 0.6095 1.5250 0.0604  -0.0777 -0.2347 66  HIS   Y C   
43027 O  O   . HIS   Y  65  ? 1.7841 0.6435 1.5029 -0.0007 -0.1067 -0.1934 66  HIS   Y O   
43028 C  CB  . HIS   Y  65  ? 1.6912 0.6532 1.4954 0.0725  -0.0837 -0.2009 66  HIS   Y CB  
43029 C  CG  . HIS   Y  65  ? 1.6719 0.5987 1.5536 0.0370  -0.1134 -0.2558 66  HIS   Y CG  
43030 N  ND1 . HIS   Y  65  ? 1.6634 0.4770 1.5109 0.0378  -0.1004 -0.2490 66  HIS   Y ND1 
43031 C  CD2 . HIS   Y  65  ? 1.7300 0.5943 1.5627 0.0328  -0.1047 -0.3061 66  HIS   Y CD2 
43032 C  CE1 . HIS   Y  65  ? 1.6845 0.4322 1.5366 0.0421  -0.1396 -0.2815 66  HIS   Y CE1 
43033 N  NE2 . HIS   Y  65  ? 1.7336 0.4980 1.5594 0.0292  -0.1057 -0.3165 66  HIS   Y NE2 
43034 N  N   . GLU   Y  66  ? 1.7557 0.7182 1.5833 0.0597  -0.0529 -0.2168 67  GLU   Y N   
43035 C  CA  . GLU   Y  66  ? 1.8395 0.8289 1.6229 0.0912  -0.0183 -0.2321 67  GLU   Y CA  
43036 C  C   . GLU   Y  66  ? 1.8170 0.8693 1.6472 0.1029  -0.0308 -0.1730 67  GLU   Y C   
43037 O  O   . GLU   Y  66  ? 1.8295 0.8266 1.6985 0.1313  -0.0590 -0.1942 67  GLU   Y O   
43038 C  CB  . GLU   Y  66  ? 1.9148 0.9198 1.7317 0.0333  0.0374  -0.2211 67  GLU   Y CB  
43039 C  CG  . GLU   Y  66  ? 1.8983 1.0321 1.8184 0.0442  0.0205  -0.2073 67  GLU   Y CG  
43040 C  CD  . GLU   Y  66  ? 1.9790 1.1108 1.8827 0.0399  0.1348  -0.1400 67  GLU   Y CD  
43041 O  OE1 . GLU   Y  66  ? 2.0250 1.0603 1.7991 0.0281  0.1861  -0.1979 67  GLU   Y OE1 
43042 O  OE2 . GLU   Y  66  ? 1.9877 1.2329 2.0107 0.0304  0.2448  -0.0639 67  GLU   Y OE2 
43043 N  N   . LEU   Y  67  ? 1.7721 0.8457 1.6739 0.1412  -0.0146 -0.1158 68  LEU   Y N   
43044 C  CA  . LEU   Y  67  ? 1.8004 0.8421 1.7199 0.1508  -0.0100 -0.1134 68  LEU   Y CA  
43045 C  C   . LEU   Y  67  ? 1.8357 0.7254 1.6457 0.1851  -0.0319 -0.1343 68  LEU   Y C   
43046 O  O   . LEU   Y  67  ? 1.8132 0.7114 1.6048 0.1819  -0.0288 -0.1158 68  LEU   Y O   
43047 C  CB  . LEU   Y  67  ? 1.7644 0.8719 1.7417 0.1760  -0.0415 -0.0612 68  LEU   Y CB  
43048 C  CG  . LEU   Y  67  ? 1.7299 0.9164 1.8249 0.2160  -0.0280 -0.0306 68  LEU   Y CG  
43049 C  CD1 . LEU   Y  67  ? 1.7249 0.9517 1.8236 0.2162  -0.0567 0.0034  68  LEU   Y CD1 
43050 C  CD2 . LEU   Y  67  ? 1.7360 0.9186 1.8985 0.2269  -0.0146 -0.0397 68  LEU   Y CD2 
43051 N  N   . ARG   Y  68  ? 1.8436 0.6809 1.5935 0.2095  -0.0671 -0.1398 69  ARG   Y N   
43052 C  CA  . ARG   Y  68  ? 1.9017 0.6201 1.5999 0.1931  -0.0869 -0.1649 69  ARG   Y CA  
43053 C  C   . ARG   Y  68  ? 1.9855 0.5670 1.5852 0.1846  -0.0715 -0.2142 69  ARG   Y C   
43054 O  O   . ARG   Y  68  ? 2.0636 0.6436 1.5857 0.1045  -0.0668 -0.2510 69  ARG   Y O   
43055 C  CB  . ARG   Y  68  ? 1.8626 0.6665 1.5756 0.2127  -0.0985 -0.1159 69  ARG   Y CB  
43056 C  CG  . ARG   Y  68  ? 1.8516 0.7455 1.5972 0.2355  -0.1069 -0.0775 69  ARG   Y CG  
43057 C  CD  . ARG   Y  68  ? 1.8468 0.7611 1.5786 0.2536  -0.1172 -0.0446 69  ARG   Y CD  
43058 N  NE  . ARG   Y  68  ? 1.8490 0.7521 1.5364 0.2717  -0.1151 -0.0269 69  ARG   Y NE  
43059 C  CZ  . ARG   Y  68  ? 1.8848 0.7595 1.5241 0.2943  -0.1351 -0.0040 69  ARG   Y CZ  
43060 N  NH1 . ARG   Y  68  ? 1.9131 0.7769 1.5563 0.3388  -0.1606 -0.0018 69  ARG   Y NH1 
43061 N  NH2 . ARG   Y  68  ? 1.8955 0.7460 1.5544 0.2821  -0.1342 0.0418  69  ARG   Y NH2 
43062 N  N   . GLU   Y  69  ? 1.9820 0.5240 1.5535 0.1929  -0.0801 -0.2556 70  GLU   Y N   
43063 C  CA  . GLU   Y  69  ? 2.0081 0.5237 1.5293 0.1398  -0.0750 -0.2835 70  GLU   Y CA  
43064 C  C   . GLU   Y  69  ? 2.0315 0.4797 1.5380 0.2088  -0.0609 -0.3221 70  GLU   Y C   
43065 O  O   . GLU   Y  69  ? 2.0288 0.4215 1.5332 0.1940  -0.0531 -0.3431 70  GLU   Y O   
43066 C  CB  . GLU   Y  69  ? 1.9709 0.5350 1.4810 0.1140  -0.1327 -0.2238 70  GLU   Y CB  
43067 C  CG  . GLU   Y  69  ? 1.9241 0.5434 1.4594 0.0204  -0.1599 -0.1822 70  GLU   Y CG  
43068 C  CD  . GLU   Y  69  ? 1.9979 0.5163 1.4493 -0.0119 -0.2130 -0.2301 70  GLU   Y CD  
43069 O  OE1 . GLU   Y  69  ? 2.0829 0.4005 1.5188 -0.0294 -0.1826 -0.2661 70  GLU   Y OE1 
43070 O  OE2 . GLU   Y  69  ? 1.9772 0.4660 1.4927 -0.1145 -0.2129 -0.1740 70  GLU   Y OE2 
43071 N  N   . LYS   Y  70  ? 2.0196 0.5680 1.5898 0.2663  -0.0251 -0.3437 71  LYS   Y N   
43072 C  CA  . LYS   Y  70  ? 2.0757 0.7564 1.6167 0.2663  0.0108  -0.3656 71  LYS   Y CA  
43073 C  C   . LYS   Y  70  ? 2.1027 0.7820 1.5814 0.2827  0.0285  -0.3698 71  LYS   Y C   
43074 O  O   . LYS   Y  70  ? 2.1415 0.7952 1.5791 0.3018  0.0410  -0.3664 71  LYS   Y O   
43075 C  CB  . LYS   Y  70  ? 2.1396 0.8116 1.6246 0.2335  0.0082  -0.4291 71  LYS   Y CB  
43076 C  CG  . LYS   Y  70  ? 2.1222 0.8262 1.6826 0.2674  -0.0155 -0.4273 71  LYS   Y CG  
43077 C  CD  . LYS   Y  70  ? 2.1984 0.8638 1.7434 0.2483  -0.0187 -0.4770 71  LYS   Y CD  
43078 C  CE  . LYS   Y  70  ? 2.2191 0.9667 1.8223 0.2404  -0.0650 -0.4050 71  LYS   Y CE  
43079 N  NZ  . LYS   Y  70  ? 2.2980 0.9949 1.8776 0.2091  -0.0522 -0.4437 71  LYS   Y NZ  
43080 N  N   . GLU   Y  71  ? 2.1040 0.7900 1.5672 0.2629  0.0327  -0.3853 72  GLU   Y N   
43081 C  CA  . GLU   Y  71  ? 2.1663 0.8567 1.5904 0.2356  0.0391  -0.3205 72  GLU   Y CA  
43082 C  C   . GLU   Y  71  ? 2.1477 0.7959 1.6091 0.2278  0.0172  -0.2736 72  GLU   Y C   
43083 O  O   . GLU   Y  71  ? 2.1115 0.7239 1.6444 0.2371  0.0347  -0.1797 72  GLU   Y O   
43084 C  CB  . GLU   Y  71  ? 2.1970 0.8923 1.6312 0.2141  0.0126  -0.3481 72  GLU   Y CB  
43085 C  CG  . GLU   Y  71  ? 2.2733 0.8915 1.6814 0.2282  0.0140  -0.3288 72  GLU   Y CG  
43086 C  CD  . GLU   Y  71  ? 2.3116 0.9723 1.7547 0.1930  -0.0188 -0.3387 72  GLU   Y CD  
43087 O  OE1 . GLU   Y  71  ? 2.4067 1.0577 1.8272 0.1824  -0.0287 -0.4255 72  GLU   Y OE1 
43088 O  OE2 . GLU   Y  71  ? 2.3379 1.0198 1.7751 0.2205  0.0128  -0.3529 72  GLU   Y OE2 
43089 N  N   . ARG   Y  72  ? 2.1395 0.8857 1.6207 0.2104  0.0552  -0.2225 73  ARG   Y N   
43090 C  CA  . ARG   Y  72  ? 2.0242 0.8412 1.6199 0.2453  0.0712  -0.1882 73  ARG   Y CA  
43091 C  C   . ARG   Y  72  ? 1.9777 0.6857 1.4820 0.2026  0.0125  -0.1781 73  ARG   Y C   
43092 O  O   . ARG   Y  72  ? 1.9490 0.5808 1.4969 0.2640  0.0075  -0.1683 73  ARG   Y O   
43093 C  CB  . ARG   Y  72  ? 2.1855 0.9132 1.6458 0.2151  0.1527  -0.1559 73  ARG   Y CB  
43094 C  CG  . ARG   Y  72  ? 2.2127 1.0589 1.7490 0.2577  0.1217  -0.1512 73  ARG   Y CG  
43095 C  CD  . ARG   Y  72  ? 2.3316 1.2791 1.7748 0.2258  0.2066  -0.1386 73  ARG   Y CD  
43096 N  NE  . ARG   Y  72  ? 2.4655 1.3948 1.7439 0.3051  0.1524  -0.1365 73  ARG   Y NE  
43097 C  CZ  . ARG   Y  72  ? 2.5659 1.5128 1.7686 0.2661  0.0805  -0.1297 73  ARG   Y CZ  
43098 N  NH1 . ARG   Y  72  ? 2.7311 1.6488 1.7785 0.2153  0.0545  -0.2519 73  ARG   Y NH1 
43099 N  NH2 . ARG   Y  72  ? 2.5131 1.5341 1.6344 0.2219  0.0578  -0.1103 73  ARG   Y NH2 
43100 N  N   . ILE   Y  73  ? 1.8158 0.6415 1.4624 0.1867  0.0052  -0.1545 74  ILE   Y N   
43101 C  CA  . ILE   Y  73  ? 1.7694 0.7265 1.4113 0.1530  -0.0135 -0.1665 74  ILE   Y CA  
43102 C  C   . ILE   Y  73  ? 1.7826 0.7392 1.3113 0.0994  -0.0079 -0.1821 74  ILE   Y C   
43103 O  O   . ILE   Y  73  ? 1.7327 0.8350 1.2753 0.0916  0.0346  -0.2348 74  ILE   Y O   
43104 C  CB  . ILE   Y  73  ? 1.7288 0.7534 1.3835 0.1913  -0.0047 -0.0978 74  ILE   Y CB  
43105 C  CG1 . ILE   Y  73  ? 1.7074 0.7920 1.3771 0.1539  0.0002  -0.0598 74  ILE   Y CG1 
43106 C  CG2 . ILE   Y  73  ? 1.6640 0.8148 1.4103 0.1842  0.0001  -0.0853 74  ILE   Y CG2 
43107 C  CD1 . ILE   Y  73  ? 1.6715 0.8197 1.3944 0.1564  0.0210  -0.0214 74  ILE   Y CD1 
43108 N  N   . SER   Y  74  ? 1.8124 0.7476 1.2982 0.0885  -0.0527 -0.2034 75  SER   Y N   
43109 C  CA  . SER   Y  74  ? 1.8489 0.7592 1.2936 0.0782  -0.0319 -0.1688 75  SER   Y CA  
43110 C  C   . SER   Y  74  ? 1.8551 0.7578 1.2544 0.1088  -0.0446 -0.1467 75  SER   Y C   
43111 O  O   . SER   Y  74  ? 1.8529 0.7833 1.2765 0.1467  -0.0290 -0.0657 75  SER   Y O   
43112 C  CB  . SER   Y  74  ? 1.8443 0.6881 1.2932 0.0744  -0.0288 -0.1684 75  SER   Y CB  
43113 O  OG  . SER   Y  74  ? 1.7220 0.6485 1.3095 0.0776  -0.0734 -0.1732 75  SER   Y OG  
43114 N  N   . VAL   Y  75  ? 1.8755 0.7542 1.2375 0.1022  -0.0445 -0.1579 76  VAL   Y N   
43115 C  CA  . VAL   Y  75  ? 1.7946 0.7776 1.2009 0.1319  -0.0256 -0.1752 76  VAL   Y CA  
43116 C  C   . VAL   Y  75  ? 1.7606 0.6839 1.1005 0.1283  -0.0615 -0.1611 76  VAL   Y C   
43117 O  O   . VAL   Y  75  ? 1.6383 0.6411 1.0949 0.1314  -0.0653 -0.1467 76  VAL   Y O   
43118 C  CB  . VAL   Y  75  ? 1.8760 0.7927 1.2344 0.1076  -0.0045 -0.1707 76  VAL   Y CB  
43119 C  CG1 . VAL   Y  75  ? 1.8827 0.8236 1.2436 0.1070  -0.0131 -0.1963 76  VAL   Y CG1 
43120 C  CG2 . VAL   Y  75  ? 1.8937 0.8281 1.2841 0.1160  0.0230  -0.2103 76  VAL   Y CG2 
43121 N  N   . ALA   Y  76  ? 1.7496 0.7365 1.0906 0.1329  -0.0596 -0.1551 77  ALA   Y N   
43122 C  CA  . ALA   Y  76  ? 1.7437 0.8097 1.0933 0.1297  -0.0797 -0.1349 77  ALA   Y CA  
43123 C  C   . ALA   Y  76  ? 1.7455 0.8086 1.1077 0.1752  -0.1052 -0.1174 77  ALA   Y C   
43124 O  O   . ALA   Y  76  ? 1.7576 0.9297 1.1026 0.1937  -0.0847 -0.1109 77  ALA   Y O   
43125 C  CB  . ALA   Y  76  ? 1.7814 0.8547 1.1039 0.1025  -0.0936 -0.1385 77  ALA   Y CB  
43126 N  N   . ALA   Y  77  ? 1.7511 0.7916 1.1349 0.1587  -0.0810 -0.1261 78  ALA   Y N   
43127 C  CA  . ALA   Y  77  ? 1.7169 0.7759 1.1721 0.1250  -0.0628 -0.1165 78  ALA   Y CA  
43128 C  C   . ALA   Y  77  ? 1.6502 0.6676 1.2051 0.1369  -0.0504 -0.1202 78  ALA   Y C   
43129 O  O   . ALA   Y  77  ? 1.6203 0.6834 1.1866 0.1384  -0.0769 -0.1383 78  ALA   Y O   
43130 C  CB  . ALA   Y  77  ? 1.7375 0.8105 1.1823 0.1264  -0.0540 -0.1613 78  ALA   Y CB  
43131 N  N   . ALA   Y  78  ? 1.6487 0.5852 1.1939 0.1362  -0.0615 -0.1404 79  ALA   Y N   
43132 C  CA  . ALA   Y  78  ? 1.6298 0.6038 1.1965 0.1223  -0.0633 -0.1156 79  ALA   Y CA  
43133 C  C   . ALA   Y  78  ? 1.5878 0.6160 1.2072 0.1462  -0.0505 -0.0808 79  ALA   Y C   
43134 O  O   . ALA   Y  78  ? 1.6151 0.6469 1.2181 0.1681  0.0055  0.0108  79  ALA   Y O   
43135 C  CB  . ALA   Y  78  ? 1.6369 0.5903 1.1842 0.1425  -0.0397 -0.1484 79  ALA   Y CB  
43136 N  N   . SER   Y  79  ? 1.5580 0.6350 1.1856 0.1123  -0.0613 -0.0630 80  SER   Y N   
43137 C  CA  . SER   Y  79  ? 1.5439 0.5957 1.1756 0.0700  -0.0630 -0.0688 80  SER   Y CA  
43138 C  C   . SER   Y  79  ? 1.5142 0.5594 1.1623 0.0567  -0.0949 -0.0739 80  SER   Y C   
43139 O  O   . SER   Y  79  ? 1.4977 0.3938 1.1864 0.0324  -0.1109 -0.0490 80  SER   Y O   
43140 C  CB  . SER   Y  79  ? 1.5516 0.6089 1.1635 0.0645  -0.0679 -0.0736 80  SER   Y CB  
43141 O  OG  . SER   Y  79  ? 1.5595 0.5773 1.2085 0.0203  -0.0658 -0.0574 80  SER   Y OG  
43142 N  N   . LYS   Y  80  ? 1.5215 0.5840 1.2056 0.0531  -0.1332 -0.0844 81  LYS   Y N   
43143 C  CA  . LYS   Y  80  ? 1.5160 0.5259 1.2439 0.0730  -0.1422 -0.0379 81  LYS   Y CA  
43144 C  C   . LYS   Y  80  ? 1.5080 0.4609 1.2691 0.0952  -0.1450 -0.0449 81  LYS   Y C   
43145 O  O   . LYS   Y  80  ? 1.4767 0.3979 1.3392 0.1095  -0.1258 -0.0154 81  LYS   Y O   
43146 C  CB  . LYS   Y  80  ? 1.5406 0.4604 1.3024 0.0573  -0.1732 -0.0040 81  LYS   Y CB  
43147 C  CG  . LYS   Y  80  ? 1.5276 0.4417 1.3526 0.0612  -0.1984 0.0329  81  LYS   Y CG  
43148 C  CD  . LYS   Y  80  ? 1.5534 0.4638 1.4097 0.0632  -0.2430 0.0407  81  LYS   Y CD  
43149 C  CE  . LYS   Y  80  ? 1.5415 0.4816 1.4576 0.0673  -0.2715 0.0683  81  LYS   Y CE  
43150 N  NZ  . LYS   Y  80  ? 1.5804 0.4828 1.4930 0.0598  -0.3060 0.0664  81  LYS   Y NZ  
43151 N  N   . ILE   Y  81  ? 1.5074 0.5216 1.2785 0.1162  -0.1257 -0.0889 82  ILE   Y N   
43152 C  CA  . ILE   Y  81  ? 1.5376 0.6320 1.2755 0.1212  -0.1305 -0.0769 82  ILE   Y CA  
43153 C  C   . ILE   Y  81  ? 1.5443 0.6118 1.2486 0.1313  -0.1142 -0.0558 82  ILE   Y C   
43154 O  O   . ILE   Y  81  ? 1.5517 0.7700 1.2275 0.1143  -0.1197 -0.0673 82  ILE   Y O   
43155 C  CB  . ILE   Y  81  ? 1.5587 0.6568 1.3163 0.1274  -0.0987 -0.1154 82  ILE   Y CB  
43156 C  CG1 . ILE   Y  81  ? 1.5890 0.6609 1.2854 0.1102  -0.0995 -0.1101 82  ILE   Y CG1 
43157 C  CG2 . ILE   Y  81  ? 1.5654 0.6679 1.3429 0.1398  -0.1170 -0.0997 82  ILE   Y CG2 
43158 C  CD1 . ILE   Y  81  ? 1.6166 0.6955 1.2961 0.1187  -0.0776 -0.1371 82  ILE   Y CD1 
43159 N  N   . LEU   Y  82  ? 1.5996 0.5615 1.2454 0.1540  -0.1234 -0.0454 83  LEU   Y N   
43160 C  CA  . LEU   Y  82  ? 1.5477 0.5684 1.2068 0.1511  -0.1114 -0.0407 83  LEU   Y CA  
43161 C  C   . LEU   Y  82  ? 1.5310 0.4374 1.1366 0.1023  -0.1037 -0.0657 83  LEU   Y C   
43162 O  O   . LEU   Y  82  ? 1.4096 0.4234 1.1259 0.1033  -0.0901 -0.0306 83  LEU   Y O   
43163 C  CB  . LEU   Y  82  ? 1.5601 0.6395 1.1977 0.1525  -0.0923 -0.0094 83  LEU   Y CB  
43164 C  CG  . LEU   Y  82  ? 1.5776 0.6536 1.1769 0.1721  -0.0867 -0.0163 83  LEU   Y CG  
43165 C  CD1 . LEU   Y  82  ? 1.5806 0.7602 1.1725 0.1924  -0.0769 -0.0035 83  LEU   Y CD1 
43166 C  CD2 . LEU   Y  82  ? 1.5757 0.6698 1.2064 0.1847  -0.0497 -0.0157 83  LEU   Y CD2 
43167 N  N   . SER   Y  83  ? 1.5135 0.3552 1.1782 0.0722  -0.1252 -0.0817 84  SER   Y N   
43168 C  CA  . SER   Y  83  ? 1.4907 0.3810 1.1933 0.0459  -0.1331 -0.0797 84  SER   Y CA  
43169 C  C   . SER   Y  83  ? 1.5181 0.4122 1.1661 0.0148  -0.1486 -0.0797 84  SER   Y C   
43170 O  O   . SER   Y  83  ? 1.5732 0.2936 1.2113 -0.0254 -0.1497 -0.0926 84  SER   Y O   
43171 C  CB  . SER   Y  83  ? 1.4925 0.4000 1.2254 0.0268  -0.1604 -0.0609 84  SER   Y CB  
43172 O  OG  . SER   Y  83  ? 1.5392 0.3051 1.2528 0.0641  -0.1612 -0.0294 84  SER   Y OG  
43173 N  N   . ASN   Y  84  ? 1.5362 0.4132 1.1936 0.0759  -0.1873 -0.0928 85  ASN   Y N   
43174 C  CA  . ASN   Y  84  ? 1.5244 0.4139 1.2555 0.1099  -0.1943 -0.0351 85  ASN   Y CA  
43175 C  C   . ASN   Y  84  ? 1.5021 0.4288 1.2716 0.1348  -0.1921 -0.0345 85  ASN   Y C   
43176 O  O   . ASN   Y  84  ? 1.4591 0.3498 1.3886 0.1576  -0.1352 -0.0155 85  ASN   Y O   
43177 C  CB  . ASN   Y  84  ? 1.5573 0.3847 1.2774 0.0996  -0.2156 -0.0026 85  ASN   Y CB  
43178 C  CG  . ASN   Y  84  ? 1.5678 0.4524 1.3232 0.0860  -0.2420 0.0029  85  ASN   Y CG  
43179 O  OD1 . ASN   Y  84  ? 1.5907 0.4493 1.2471 0.1401  -0.2150 0.0138  85  ASN   Y OD1 
43180 N  ND2 . ASN   Y  84  ? 1.5291 0.4653 1.4382 0.0998  -0.2628 -0.0434 85  ASN   Y ND2 
43181 N  N   . LEU   Y  85  ? 1.5011 0.5311 1.3299 0.1472  -0.1853 -0.0810 86  LEU   Y N   
43182 C  CA  . LEU   Y  85  ? 1.4746 0.6276 1.3229 0.1096  -0.1833 -0.0907 86  LEU   Y CA  
43183 C  C   . LEU   Y  85  ? 1.4749 0.6671 1.2203 0.1035  -0.1914 -0.0899 86  LEU   Y C   
43184 O  O   . LEU   Y  85  ? 1.4588 0.7364 1.2166 0.0726  -0.2078 -0.0414 86  LEU   Y O   
43185 C  CB  . LEU   Y  85  ? 1.4705 0.6430 1.3262 0.0937  -0.1705 -0.1200 86  LEU   Y CB  
43186 C  CG  . LEU   Y  85  ? 1.4741 0.6700 1.3090 0.0908  -0.1495 -0.0545 86  LEU   Y CG  
43187 C  CD1 . LEU   Y  85  ? 1.5076 0.6874 1.3421 0.0847  -0.1134 -0.0799 86  LEU   Y CD1 
43188 C  CD2 . LEU   Y  85  ? 1.4692 0.6165 1.3258 0.1011  -0.1836 -0.0388 86  LEU   Y CD2 
43189 N  N   . VAL   Y  86  ? 1.4842 0.6843 1.2280 0.0994  -0.2002 -0.0712 87  VAL   Y N   
43190 C  CA  . VAL   Y  86  ? 1.4593 0.6935 1.2036 0.1292  -0.1753 -0.0507 87  VAL   Y CA  
43191 C  C   . VAL   Y  86  ? 1.4541 0.6882 1.1925 0.1391  -0.1884 -0.0476 87  VAL   Y C   
43192 O  O   . VAL   Y  86  ? 1.4635 0.7937 1.1648 0.2312  -0.1670 -0.0172 87  VAL   Y O   
43193 C  CB  . VAL   Y  86  ? 1.4457 0.7108 1.1990 0.1391  -0.1908 -0.0162 87  VAL   Y CB  
43194 C  CG1 . VAL   Y  86  ? 1.4431 0.6956 1.2283 0.1343  -0.1843 0.0009  87  VAL   Y CG1 
43195 C  CG2 . VAL   Y  86  ? 1.4655 0.6813 1.1843 0.1142  -0.1850 -0.0212 87  VAL   Y CG2 
43196 N  N   . TYR   Y  87  ? 1.4505 0.5559 1.1840 0.1102  -0.1493 -0.0323 88  TYR   Y N   
43197 C  CA  . TYR   Y  87  ? 1.4539 0.4859 1.1913 0.0746  -0.1247 -0.0386 88  TYR   Y CA  
43198 C  C   . TYR   Y  87  ? 1.4873 0.4884 1.1684 0.0651  -0.1117 -0.0653 88  TYR   Y C   
43199 O  O   . TYR   Y  87  ? 1.5424 0.3123 1.1032 0.1267  -0.1475 -0.0957 88  TYR   Y O   
43200 C  CB  . TYR   Y  87  ? 1.4357 0.4212 1.2023 0.0585  -0.1175 -0.0314 88  TYR   Y CB  
43201 C  CG  . TYR   Y  87  ? 1.4299 0.4364 1.2029 0.0570  -0.1269 -0.0332 88  TYR   Y CG  
43202 C  CD1 . TYR   Y  87  ? 1.4225 0.4564 1.2151 0.0676  -0.0990 0.0000  88  TYR   Y CD1 
43203 C  CD2 . TYR   Y  87  ? 1.4245 0.4266 1.2147 0.0628  -0.1319 -0.0391 88  TYR   Y CD2 
43204 C  CE1 . TYR   Y  87  ? 1.4211 0.5265 1.2410 0.0404  -0.0872 -0.0192 88  TYR   Y CE1 
43205 C  CE2 . TYR   Y  87  ? 1.4341 0.4796 1.2292 0.0660  -0.1120 -0.0370 88  TYR   Y CE2 
43206 C  CZ  . TYR   Y  87  ? 1.4575 0.4723 1.2395 0.0555  -0.1047 -0.0257 88  TYR   Y CZ  
43207 O  OH  . TYR   Y  87  ? 1.4598 0.5793 1.2464 0.0468  -0.0925 -0.0219 88  TYR   Y OH  
43208 N  N   . GLN   Y  88  ? 1.4926 0.5521 1.2192 0.0844  -0.1493 -0.0379 89  GLN   Y N   
43209 C  CA  . GLN   Y  88  ? 1.5162 0.6703 1.2336 0.0242  -0.1229 -0.0105 89  GLN   Y CA  
43210 C  C   . GLN   Y  88  ? 1.4698 0.6079 1.2479 0.0246  -0.0863 -0.0111 89  GLN   Y C   
43211 O  O   . GLN   Y  88  ? 1.4643 0.6469 1.2640 0.0208  -0.0939 0.0690  89  GLN   Y O   
43212 C  CB  . GLN   Y  88  ? 1.5290 0.6940 1.3045 0.0365  -0.1478 0.0005  89  GLN   Y CB  
43213 C  CG  . GLN   Y  88  ? 1.5876 0.7909 1.3771 -0.0392 -0.1409 -0.0533 89  GLN   Y CG  
43214 C  CD  . GLN   Y  88  ? 1.6257 0.8327 1.4797 -0.0663 -0.1550 0.0013  89  GLN   Y CD  
43215 O  OE1 . GLN   Y  88  ? 1.5008 1.0952 1.6393 -0.1663 -0.1103 -0.0819 89  GLN   Y OE1 
43216 N  NE2 . GLN   Y  88  ? 1.6681 1.0680 1.5733 -0.1677 -0.1164 -0.0270 89  GLN   Y NE2 
43217 N  N   . TYR   Y  89  ? 1.4660 0.5905 1.2619 0.0271  -0.0983 -0.0554 90  TYR   Y N   
43218 C  CA  . TYR   Y  89  ? 1.4912 0.6370 1.2398 0.0067  -0.1029 -0.0580 90  TYR   Y CA  
43219 C  C   . TYR   Y  89  ? 1.4752 0.6296 1.2491 -0.0066 -0.0706 -0.0923 90  TYR   Y C   
43220 O  O   . TYR   Y  89  ? 1.4947 0.6833 1.1595 -0.0114 -0.0452 -0.0833 90  TYR   Y O   
43221 C  CB  . TYR   Y  89  ? 1.4843 0.5942 1.1932 0.0293  -0.1410 -0.0849 90  TYR   Y CB  
43222 C  CG  . TYR   Y  89  ? 1.5551 0.5769 1.1495 0.0337  -0.1730 -0.1031 90  TYR   Y CG  
43223 C  CD1 . TYR   Y  89  ? 1.5865 0.5883 1.1537 0.0304  -0.1886 -0.1174 90  TYR   Y CD1 
43224 C  CD2 . TYR   Y  89  ? 1.5685 0.5271 1.1861 0.0584  -0.2053 -0.0936 90  TYR   Y CD2 
43225 C  CE1 . TYR   Y  89  ? 1.5992 0.5706 1.1493 0.0376  -0.2029 -0.1407 90  TYR   Y CE1 
43226 C  CE2 . TYR   Y  89  ? 1.5943 0.4816 1.1813 0.0545  -0.2250 -0.1208 90  TYR   Y CE2 
43227 C  CZ  . TYR   Y  89  ? 1.5915 0.4815 1.1885 0.0846  -0.2386 -0.1020 90  TYR   Y CZ  
43228 O  OH  . TYR   Y  89  ? 1.6453 0.5392 1.2129 0.1190  -0.2599 -0.0744 90  TYR   Y OH  
43229 N  N   . LYS   Y  90  ? 1.4593 0.6276 1.3006 -0.0155 -0.0852 -0.0704 91  LYS   Y N   
43230 C  CA  . LYS   Y  90  ? 1.5080 0.6141 1.3287 -0.0008 -0.0783 -0.1039 91  LYS   Y CA  
43231 C  C   . LYS   Y  90  ? 1.5062 0.7111 1.3369 -0.0015 -0.0135 -0.0433 91  LYS   Y C   
43232 O  O   . LYS   Y  90  ? 1.5407 0.6896 1.3928 -0.0463 -0.0335 -0.0368 91  LYS   Y O   
43233 C  CB  . LYS   Y  90  ? 1.5397 0.6219 1.3553 -0.0030 -0.1061 -0.1162 91  LYS   Y CB  
43234 C  CG  . LYS   Y  90  ? 1.5772 0.6464 1.3857 0.0446  -0.1271 -0.1389 91  LYS   Y CG  
43235 C  CD  . LYS   Y  90  ? 1.6055 0.7002 1.4028 0.0356  -0.1450 -0.1365 91  LYS   Y CD  
43236 C  CE  . LYS   Y  90  ? 1.6089 0.7358 1.4090 0.0565  -0.1243 -0.1010 91  LYS   Y CE  
43237 N  NZ  . LYS   Y  90  ? 1.6342 0.7610 1.3567 0.0727  -0.1191 -0.0523 91  LYS   Y NZ  
43238 N  N   . GLY   Y  91  ? 1.5447 0.7574 1.2946 0.0693  -0.0323 -0.1491 92  GLY   Y N   
43239 C  CA  . GLY   Y  91  ? 1.5534 0.7799 1.2919 0.0996  -0.0384 -0.1558 92  GLY   Y CA  
43240 C  C   . GLY   Y  91  ? 1.5321 0.7601 1.2905 0.1095  -0.0278 -0.1485 92  GLY   Y C   
43241 O  O   . GLY   Y  91  ? 1.5204 0.7418 1.2558 0.0486  -0.0439 -0.1261 92  GLY   Y O   
43242 N  N   . ALA   Y  92  ? 1.5358 0.7050 1.2404 0.0866  -0.0465 -0.1611 93  ALA   Y N   
43243 C  CA  . ALA   Y  92  ? 1.5543 0.6324 1.1991 0.0644  -0.0416 -0.1650 93  ALA   Y CA  
43244 C  C   . ALA   Y  92  ? 1.6013 0.6062 1.1975 0.0626  -0.0586 -0.2066 93  ALA   Y C   
43245 O  O   . ALA   Y  92  ? 1.6596 0.5205 1.1872 0.0627  -0.0537 -0.2555 93  ALA   Y O   
43246 C  CB  . ALA   Y  92  ? 1.5293 0.6120 1.1958 0.0602  -0.0616 -0.1228 93  ALA   Y CB  
43247 N  N   . GLY   Y  93  ? 1.5799 0.5476 1.2304 0.0506  -0.0623 -0.2044 94  GLY   Y N   
43248 C  CA  . GLY   Y  93  ? 1.5176 0.6239 1.2074 0.0201  -0.0463 -0.1855 94  GLY   Y CA  
43249 C  C   . GLY   Y  93  ? 1.4902 0.6471 1.1691 0.0286  -0.0696 -0.1660 94  GLY   Y C   
43250 O  O   . GLY   Y  93  ? 1.3837 0.8332 1.1568 -0.0192 -0.0188 -0.1392 94  GLY   Y O   
43251 N  N   . LEU   Y  94  ? 1.4948 0.5834 1.1488 0.0496  -0.1174 -0.1177 95  LEU   Y N   
43252 C  CA  . LEU   Y  94  ? 1.4652 0.6471 1.1859 0.0535  -0.1290 -0.0623 95  LEU   Y CA  
43253 C  C   . LEU   Y  94  ? 1.4785 0.5758 1.2134 0.0094  -0.1684 -0.0981 95  LEU   Y C   
43254 O  O   . LEU   Y  94  ? 1.4707 0.5442 1.3088 0.0016  -0.1748 -0.0851 95  LEU   Y O   
43255 C  CB  . LEU   Y  94  ? 1.4883 0.6670 1.1950 0.0579  -0.1440 -0.0694 95  LEU   Y CB  
43256 C  CG  . LEU   Y  94  ? 1.4865 0.7120 1.2076 0.0531  -0.1464 -0.0276 95  LEU   Y CG  
43257 C  CD1 . LEU   Y  94  ? 1.4564 0.7181 1.2319 0.0412  -0.1506 -0.0397 95  LEU   Y CD1 
43258 C  CD2 . LEU   Y  94  ? 1.4839 0.7849 1.2210 0.0617  -0.1407 -0.0291 95  LEU   Y CD2 
43259 N  N   . SER   Y  95  ? 1.4737 0.5876 1.1889 0.0094  -0.1842 -0.0851 96  SER   Y N   
43260 C  CA  . SER   Y  95  ? 1.4832 0.6033 1.2196 0.0362  -0.1772 -0.0575 96  SER   Y CA  
43261 C  C   . SER   Y  95  ? 1.4661 0.5422 1.2964 0.0695  -0.1493 -0.0245 96  SER   Y C   
43262 O  O   . SER   Y  95  ? 1.4695 0.4973 1.2784 0.0821  -0.1588 -0.0148 96  SER   Y O   
43263 C  CB  . SER   Y  95  ? 1.5244 0.6199 1.1825 0.0146  -0.1760 -0.0546 96  SER   Y CB  
43264 O  OG  . SER   Y  95  ? 1.5653 0.5787 1.1841 0.0392  -0.1792 -0.0587 96  SER   Y OG  
43265 N  N   . MET   Y  96  ? 1.4557 0.4772 1.3313 0.0943  -0.1789 -0.0226 97  MET   Y N   
43266 C  CA  . MET   Y  96  ? 1.4405 0.4997 1.3789 0.1165  -0.1685 -0.0187 97  MET   Y CA  
43267 C  C   . MET   Y  96  ? 1.3627 0.3923 1.3947 0.1203  -0.1755 -0.0584 97  MET   Y C   
43268 O  O   . MET   Y  96  ? 1.3748 0.3116 1.3972 0.1077  -0.2043 -0.1247 97  MET   Y O   
43269 C  CB  . MET   Y  96  ? 1.4800 0.5005 1.4096 0.1457  -0.1938 0.0184  97  MET   Y CB  
43270 C  CG  . MET   Y  96  ? 1.5201 0.5606 1.4397 0.1468  -0.2475 0.0744  97  MET   Y CG  
43271 S  SD  . MET   Y  96  ? 1.6158 0.5355 1.4714 0.1671  -0.3360 0.1037  97  MET   Y SD  
43272 C  CE  . MET   Y  96  ? 1.6242 0.5942 1.4355 0.2022  -0.3149 0.0870  97  MET   Y CE  
43273 N  N   . GLY   Y  97  ? 1.3807 0.3910 1.4128 0.1463  -0.1433 -0.0512 98  GLY   Y N   
43274 C  CA  . GLY   Y  97  ? 1.4088 0.4232 1.4216 0.1216  -0.1559 -0.0597 98  GLY   Y CA  
43275 C  C   . GLY   Y  97  ? 1.4322 0.4417 1.4750 0.1501  -0.1440 -0.0431 98  GLY   Y C   
43276 O  O   . GLY   Y  97  ? 1.4625 0.3831 1.5544 0.1489  -0.2156 -0.1061 98  GLY   Y O   
43277 N  N   . THR   Y  98  ? 1.4376 0.5525 1.4520 0.1251  -0.1774 -0.0857 99  THR   Y N   
43278 C  CA  . THR   Y  98  ? 1.4366 0.7367 1.4826 0.1654  -0.1317 -0.0561 99  THR   Y CA  
43279 C  C   . THR   Y  98  ? 1.4983 0.8369 1.4681 0.1541  -0.1060 -0.0738 99  THR   Y C   
43280 O  O   . THR   Y  98  ? 1.4733 0.8924 1.4704 0.1350  -0.0436 -0.0991 99  THR   Y O   
43281 C  CB  . THR   Y  98  ? 1.4168 0.7406 1.5277 0.1682  -0.1405 -0.0513 99  THR   Y CB  
43282 O  OG1 . THR   Y  98  ? 1.4341 0.5800 1.4979 0.1987  -0.2115 -0.0394 99  THR   Y OG1 
43283 C  CG2 . THR   Y  98  ? 1.4387 0.8426 1.5521 0.1880  -0.1539 -0.0673 99  THR   Y CG2 
43284 N  N   . MET   Y  99  ? 1.5415 0.9532 1.5204 0.1402  -0.0643 -0.0805 100 MET   Y N   
43285 C  CA  . MET   Y  99  ? 1.6977 0.9816 1.5570 0.0847  -0.1382 -0.1049 100 MET   Y CA  
43286 C  C   . MET   Y  99  ? 1.7675 0.9305 1.5388 0.0079  -0.1120 -0.2085 100 MET   Y C   
43287 O  O   . MET   Y  99  ? 1.7775 0.9844 1.5165 -0.0916 -0.1295 -0.3049 100 MET   Y O   
43288 C  CB  . MET   Y  99  ? 1.7818 1.0258 1.6027 0.1519  -0.1575 -0.0039 100 MET   Y CB  
43289 C  CG  . MET   Y  99  ? 1.8375 1.0406 1.6363 0.2041  -0.1735 -0.0290 100 MET   Y CG  
43290 S  SD  . MET   Y  99  ? 2.0289 1.0552 1.7094 0.2382  -0.2145 -0.0076 100 MET   Y SD  
43291 C  CE  . MET   Y  99  ? 1.9899 1.1073 1.7710 0.2039  -0.1677 -0.0462 100 MET   Y CE  
43292 N  N   . ILE   Y  100 ? 1.7763 0.8858 1.5168 0.0041  -0.0906 -0.1753 101 ILE   Y N   
43293 C  CA  . ILE   Y  100 ? 1.8426 0.8568 1.4709 0.0072  -0.0649 -0.1459 101 ILE   Y CA  
43294 C  C   . ILE   Y  100 ? 1.8437 0.7085 1.4702 -0.0289 -0.0394 -0.1171 101 ILE   Y C   
43295 O  O   . ILE   Y  100 ? 1.8841 0.6787 1.4027 -0.0596 -0.0462 -0.1515 101 ILE   Y O   
43296 C  CB  . ILE   Y  100 ? 1.8252 0.9042 1.4634 -0.0019 -0.0359 -0.1494 101 ILE   Y CB  
43297 C  CG1 . ILE   Y  100 ? 1.7661 0.9391 1.4321 0.0235  -0.0834 -0.1644 101 ILE   Y CG1 
43298 C  CG2 . ILE   Y  100 ? 1.8552 0.9657 1.5414 0.0457  -0.0238 -0.1780 101 ILE   Y CG2 
43299 C  CD1 . ILE   Y  100 ? 1.7594 0.9299 1.3811 0.0336  -0.0756 -0.1504 101 ILE   Y CD1 
43300 N  N   . CYS   Y  101 ? 1.8526 0.6718 1.4684 -0.0225 -0.0215 -0.0876 102 CYS   Y N   
43301 C  CA  . CYS   Y  101 ? 1.9387 0.7986 1.4819 -0.0393 -0.0141 -0.0666 102 CYS   Y CA  
43302 C  C   . CYS   Y  101 ? 1.9470 0.8011 1.5069 -0.0173 -0.0338 -0.0479 102 CYS   Y C   
43303 O  O   . CYS   Y  101 ? 1.9252 0.7898 1.5366 -0.0780 -0.0499 0.0018  102 CYS   Y O   
43304 C  CB  . CYS   Y  101 ? 1.9700 0.8412 1.5420 -0.0777 -0.0262 -0.0460 102 CYS   Y CB  
43305 S  SG  . CYS   Y  101 ? 2.0448 0.9073 1.4305 -0.1087 0.0134  -0.0307 102 CYS   Y SG  
43306 N  N   . GLY   Y  102 ? 2.0321 0.8643 1.5087 -0.0174 -0.0050 -0.0849 103 GLY   Y N   
43307 C  CA  . GLY   Y  102 ? 2.0876 0.8798 1.5657 0.0013  0.0094  -0.1057 103 GLY   Y CA  
43308 C  C   . GLY   Y  102 ? 2.1486 0.8836 1.5827 -0.0200 0.0042  -0.1466 103 GLY   Y C   
43309 O  O   . GLY   Y  102 ? 2.1323 0.8121 1.6249 -0.0848 -0.0549 -0.1585 103 GLY   Y O   
43310 N  N   . TYR   Y  103 ? 2.2534 1.0238 1.5193 -0.0224 0.0430  -0.2379 104 TYR   Y N   
43311 C  CA  . TYR   Y  103 ? 2.3042 1.2678 1.4256 0.0414  0.0970  -0.2225 104 TYR   Y CA  
43312 C  C   . TYR   Y  103 ? 2.2615 1.2587 1.4121 0.0645  0.0546  -0.2293 104 TYR   Y C   
43313 O  O   . TYR   Y  103 ? 2.2700 1.2974 1.5423 0.1756  0.1034  -0.2348 104 TYR   Y O   
43314 C  CB  . TYR   Y  103 ? 2.4027 1.5012 1.4380 0.0346  0.1818  -0.2596 104 TYR   Y CB  
43315 C  CG  . TYR   Y  103 ? 2.5073 1.8280 1.3817 0.0063  0.2909  -0.3147 104 TYR   Y CG  
43316 C  CD1 . TYR   Y  103 ? 2.5881 1.8617 1.4995 0.0946  0.3166  -0.2059 104 TYR   Y CD1 
43317 C  CD2 . TYR   Y  103 ? 2.4912 1.8819 1.4030 0.0412  0.3396  -0.2704 104 TYR   Y CD2 
43318 C  CE1 . TYR   Y  103 ? 2.6549 2.1284 1.4932 0.0413  0.3184  -0.2428 104 TYR   Y CE1 
43319 C  CE2 . TYR   Y  103 ? 2.6159 2.2023 1.3503 -0.0386 0.2885  -0.2543 104 TYR   Y CE2 
43320 C  CZ  . TYR   Y  103 ? 2.6841 2.2383 1.3827 -0.0188 0.2901  -0.2813 104 TYR   Y CZ  
43321 O  OH  . TYR   Y  103 ? 2.7147 2.3991 1.3525 -0.0403 0.3931  -0.3428 104 TYR   Y OH  
43322 N  N   . THR   Y  104 ? 2.2920 1.0776 1.2929 0.0858  0.0396  -0.1888 105 THR   Y N   
43323 C  CA  . THR   Y  104 ? 2.2540 1.0679 1.3325 0.0734  0.0553  -0.1613 105 THR   Y CA  
43324 C  C   . THR   Y  104 ? 2.3050 1.1392 1.3282 0.0360  0.0535  -0.1267 105 THR   Y C   
43325 O  O   . THR   Y  104 ? 2.3583 1.2110 1.4353 -0.0115 0.1096  0.0145  105 THR   Y O   
43326 C  CB  . THR   Y  104 ? 2.2210 0.9980 1.2604 0.1029  0.0265  -0.1809 105 THR   Y CB  
43327 O  OG1 . THR   Y  104 ? 2.2415 0.8707 1.1089 0.0878  0.0216  -0.1799 105 THR   Y OG1 
43328 C  CG2 . THR   Y  104 ? 2.1680 0.9275 1.2667 0.0875  0.0207  -0.2325 105 THR   Y CG2 
43329 N  N   . ARG   Y  105 ? 2.2841 1.2114 1.2794 0.0302  0.0407  -0.2150 106 ARG   Y N   
43330 C  CA  . ARG   Y  105 ? 2.3458 1.2639 1.2754 0.0037  0.0789  -0.2717 106 ARG   Y CA  
43331 C  C   . ARG   Y  105 ? 2.3589 1.0638 1.1680 -0.0228 0.0182  -0.3498 106 ARG   Y C   
43332 O  O   . ARG   Y  105 ? 2.4028 1.0369 1.0960 -0.1122 0.0145  -0.3737 106 ARG   Y O   
43333 C  CB  . ARG   Y  105 ? 2.3251 1.3490 1.3456 0.1018  0.1247  -0.2802 106 ARG   Y CB  
43334 C  CG  . ARG   Y  105 ? 2.3464 1.5787 1.3910 0.0925  0.1627  -0.2443 106 ARG   Y CG  
43335 C  CD  . ARG   Y  105 ? 2.3958 1.6601 1.3732 0.0747  0.1880  -0.2310 106 ARG   Y CD  
43336 N  NE  . ARG   Y  105 ? 2.4480 1.7820 1.3876 0.0862  0.2531  -0.2573 106 ARG   Y NE  
43337 C  CZ  . ARG   Y  105 ? 2.4811 1.7957 1.4834 0.0607  0.2388  -0.2330 106 ARG   Y CZ  
43338 N  NH1 . ARG   Y  105 ? 2.4616 1.7626 1.4646 0.0783  0.2273  -0.2372 106 ARG   Y NH1 
43339 N  NH2 . ARG   Y  105 ? 2.5468 1.8295 1.5139 0.0497  0.2681  -0.2584 106 ARG   Y NH2 
43340 N  N   . LYS   Y  106 ? 2.2956 1.0131 1.1925 -0.0119 0.0221  -0.4083 107 LYS   Y N   
43341 C  CA  . LYS   Y  106 ? 2.3039 1.0572 1.2248 0.0108  -0.0266 -0.4109 107 LYS   Y CA  
43342 C  C   . LYS   Y  106 ? 2.2215 1.0500 1.1648 0.0274  -0.0815 -0.3052 107 LYS   Y C   
43343 O  O   . LYS   Y  106 ? 2.2895 1.0435 1.0792 0.0167  -0.1277 -0.3089 107 LYS   Y O   
43344 C  CB  . LYS   Y  106 ? 2.2693 1.0346 1.3200 -0.0043 0.0091  -0.4373 107 LYS   Y CB  
43345 C  CG  . LYS   Y  106 ? 2.1969 1.0291 1.3360 0.0314  0.0409  -0.4680 107 LYS   Y CG  
43346 C  CD  . LYS   Y  106 ? 2.1772 1.0600 1.4094 -0.0035 0.0316  -0.4459 107 LYS   Y CD  
43347 C  CE  . LYS   Y  106 ? 2.1112 1.1480 1.4342 -0.0172 0.0345  -0.4143 107 LYS   Y CE  
43348 N  NZ  . LYS   Y  106 ? 2.1014 1.1465 1.4055 -0.0279 0.0209  -0.4377 107 LYS   Y NZ  
43349 N  N   . GLU   Y  107 ? 2.1213 1.0189 1.2242 0.0185  -0.0979 -0.2572 108 GLU   Y N   
43350 C  CA  . GLU   Y  107 ? 2.0691 1.0255 1.1959 0.0430  -0.1248 -0.2394 108 GLU   Y CA  
43351 C  C   . GLU   Y  107 ? 2.0950 1.0249 1.2102 0.0435  -0.1416 -0.2193 108 GLU   Y C   
43352 O  O   . GLU   Y  107 ? 2.0376 0.9998 1.1360 0.0164  -0.1592 -0.2619 108 GLU   Y O   
43353 C  CB  . GLU   Y  107 ? 2.0150 1.0023 1.1990 0.0718  -0.1059 -0.2642 108 GLU   Y CB  
43354 C  CG  . GLU   Y  107 ? 2.0078 1.0078 1.2248 0.0784  -0.1059 -0.2523 108 GLU   Y CG  
43355 C  CD  . GLU   Y  107 ? 1.9836 1.0712 1.2280 0.0830  -0.1157 -0.2143 108 GLU   Y CD  
43356 O  OE1 . GLU   Y  107 ? 1.8697 1.1502 1.3328 0.0799  -0.1036 -0.1646 108 GLU   Y OE1 
43357 O  OE2 . GLU   Y  107 ? 1.9786 1.1021 1.3271 0.0994  -0.0991 -0.2168 108 GLU   Y OE2 
43358 N  N   . GLY   Y  108 ? 2.1162 1.0335 1.2852 0.0532  -0.1101 -0.1954 109 GLY   Y N   
43359 C  CA  . GLY   Y  108 ? 2.2111 1.0038 1.2965 0.0519  -0.0746 -0.1714 109 GLY   Y CA  
43360 C  C   . GLY   Y  108 ? 2.1962 0.9383 1.3163 0.0577  -0.0612 -0.1640 109 GLY   Y C   
43361 O  O   . GLY   Y  108 ? 2.1952 0.8494 1.3492 0.1235  -0.0125 -0.1506 109 GLY   Y O   
43362 N  N   . PRO   Y  109 ? 2.1822 1.0068 1.3026 0.0142  -0.0315 -0.1232 110 PRO   Y N   
43363 C  CA  . PRO   Y  109 ? 2.0576 0.9501 1.2955 0.0371  -0.0178 -0.1095 110 PRO   Y CA  
43364 C  C   . PRO   Y  109 ? 2.0281 0.8426 1.2445 0.0388  -0.0686 -0.1256 110 PRO   Y C   
43365 O  O   . PRO   Y  109 ? 2.0919 0.7501 1.2794 0.0552  -0.0885 -0.0885 110 PRO   Y O   
43366 C  CB  . PRO   Y  109 ? 2.0570 0.9312 1.2975 0.0324  -0.0252 -0.1238 110 PRO   Y CB  
43367 C  CG  . PRO   Y  109 ? 2.1435 1.0335 1.2888 -0.0020 -0.0217 -0.0819 110 PRO   Y CG  
43368 C  CD  . PRO   Y  109 ? 2.2132 1.0515 1.3113 -0.0213 -0.0199 -0.1196 110 PRO   Y CD  
43369 N  N   . THR   Y  110 ? 1.9410 0.8589 1.2382 0.0282  -0.0302 -0.1623 111 THR   Y N   
43370 C  CA  . THR   Y  110 ? 1.9197 0.8755 1.2672 0.0441  -0.0224 -0.1281 111 THR   Y CA  
43371 C  C   . THR   Y  110 ? 1.8104 0.8307 1.2387 0.0590  -0.0090 -0.0890 111 THR   Y C   
43372 O  O   . THR   Y  110 ? 1.7679 0.8321 1.1796 0.0762  0.0448  -0.0990 111 THR   Y O   
43373 C  CB  . THR   Y  110 ? 1.9345 0.9011 1.2725 0.0193  -0.0050 -0.1387 111 THR   Y CB  
43374 O  OG1 . THR   Y  110 ? 2.0543 1.0447 1.2578 -0.0142 0.0041  -0.1624 111 THR   Y OG1 
43375 C  CG2 . THR   Y  110 ? 1.9056 0.8744 1.2658 0.0337  -0.0342 -0.1300 111 THR   Y CG2 
43376 N  N   . ILE   Y  111 ? 1.7972 0.7821 1.2288 0.0372  -0.0169 -0.0640 112 ILE   Y N   
43377 C  CA  . ILE   Y  111 ? 1.7706 0.7526 1.2246 0.0361  -0.0535 -0.0509 112 ILE   Y CA  
43378 C  C   . ILE   Y  111 ? 1.7615 0.6275 1.2457 0.0275  -0.0671 -0.0714 112 ILE   Y C   
43379 O  O   . ILE   Y  111 ? 1.8073 0.6278 1.2505 0.0169  -0.1004 -0.0566 112 ILE   Y O   
43380 C  CB  . ILE   Y  111 ? 1.7686 0.7686 1.2244 0.0196  -0.0407 -0.0364 112 ILE   Y CB  
43381 C  CG1 . ILE   Y  111 ? 1.7995 0.8813 1.2750 0.0190  -0.0097 -0.0473 112 ILE   Y CG1 
43382 C  CG2 . ILE   Y  111 ? 1.7063 0.7689 1.2198 0.0359  -0.0270 -0.0375 112 ILE   Y CG2 
43383 C  CD1 . ILE   Y  111 ? 1.8465 0.8915 1.3355 -0.0079 0.0049  -0.0375 112 ILE   Y CD1 
43384 N  N   . TYR   Y  112 ? 1.7540 0.5765 1.2416 0.0402  -0.0870 -0.1006 113 TYR   Y N   
43385 C  CA  . TYR   Y  112 ? 1.7465 0.6210 1.3190 0.0488  -0.0668 -0.0619 113 TYR   Y CA  
43386 C  C   . TYR   Y  112 ? 1.7533 0.5973 1.3002 0.0887  -0.0450 -0.0428 113 TYR   Y C   
43387 O  O   . TYR   Y  112 ? 1.7257 0.7190 1.3949 0.1045  -0.0353 0.0241  113 TYR   Y O   
43388 C  CB  . TYR   Y  112 ? 1.7766 0.6160 1.3339 0.0226  -0.0813 -0.0796 113 TYR   Y CB  
43389 C  CG  . TYR   Y  112 ? 1.7906 0.6043 1.4398 -0.0246 -0.1147 -0.0528 113 TYR   Y CG  
43390 C  CD1 . TYR   Y  112 ? 1.7806 0.5463 1.4641 -0.0311 -0.1224 -0.0215 113 TYR   Y CD1 
43391 C  CD2 . TYR   Y  112 ? 1.8302 0.5364 1.5104 -0.0484 -0.1094 -0.0771 113 TYR   Y CD2 
43392 C  CE1 . TYR   Y  112 ? 1.7734 0.4811 1.5111 -0.0572 -0.1163 -0.0017 113 TYR   Y CE1 
43393 C  CE2 . TYR   Y  112 ? 1.8682 0.4987 1.5199 -0.0629 -0.1124 -0.0738 113 TYR   Y CE2 
43394 C  CZ  . TYR   Y  112 ? 1.8525 0.4376 1.5040 -0.1093 -0.1504 -0.0538 113 TYR   Y CZ  
43395 O  OH  . TYR   Y  112 ? 1.8824 0.4182 1.5426 -0.1523 -0.1274 -0.0319 113 TYR   Y OH  
43396 N  N   . TYR   Y  113 ? 1.7817 0.5929 1.2824 0.1043  -0.0263 -0.0195 114 TYR   Y N   
43397 C  CA  . TYR   Y  113 ? 1.7785 0.5710 1.2852 0.1098  -0.0361 -0.0223 114 TYR   Y CA  
43398 C  C   . TYR   Y  113 ? 1.7857 0.4593 1.2585 0.1603  -0.0617 -0.0354 114 TYR   Y C   
43399 O  O   . TYR   Y  113 ? 1.7662 0.3681 1.2374 0.2224  -0.1013 -0.0518 114 TYR   Y O   
43400 C  CB  . TYR   Y  113 ? 1.7876 0.5162 1.2704 0.0498  -0.0284 0.0126  114 TYR   Y CB  
43401 C  CG  . TYR   Y  113 ? 1.7548 0.4418 1.2763 -0.0203 -0.0482 0.0115  114 TYR   Y CG  
43402 C  CD1 . TYR   Y  113 ? 1.7427 0.4948 1.2596 -0.0363 -0.0472 0.0023  114 TYR   Y CD1 
43403 C  CD2 . TYR   Y  113 ? 1.7673 0.4218 1.2748 -0.0178 -0.0404 0.0249  114 TYR   Y CD2 
43404 C  CE1 . TYR   Y  113 ? 1.7363 0.5529 1.2565 -0.0577 -0.0394 -0.0156 114 TYR   Y CE1 
43405 C  CE2 . TYR   Y  113 ? 1.7510 0.4433 1.2419 -0.0660 -0.0532 0.0289  114 TYR   Y CE2 
43406 C  CZ  . TYR   Y  113 ? 1.7500 0.5415 1.2462 -0.1064 -0.0473 0.0136  114 TYR   Y CZ  
43407 O  OH  . TYR   Y  113 ? 1.8533 0.6816 1.1546 -0.1571 -0.0166 0.0410  114 TYR   Y OH  
43408 N  N   . VAL   Y  114 ? 1.7873 0.4526 1.2842 0.1495  -0.0919 -0.0700 115 VAL   Y N   
43409 C  CA  . VAL   Y  114 ? 1.7830 0.4854 1.2542 0.0996  -0.1013 -0.1008 115 VAL   Y CA  
43410 C  C   . VAL   Y  114 ? 1.6970 0.4108 1.3216 0.0769  -0.0924 -0.1283 115 VAL   Y C   
43411 O  O   . VAL   Y  114 ? 1.7243 0.3879 1.3461 0.0256  -0.0945 -0.2142 115 VAL   Y O   
43412 C  CB  . VAL   Y  114 ? 1.8227 0.4994 1.2388 0.1160  -0.1059 -0.0804 115 VAL   Y CB  
43413 C  CG1 . VAL   Y  114 ? 1.8205 0.5046 1.2435 0.0946  -0.1239 -0.0724 115 VAL   Y CG1 
43414 C  CG2 . VAL   Y  114 ? 1.8719 0.5196 1.2294 0.0919  -0.0876 -0.0824 115 VAL   Y CG2 
43415 N  N   . ASP   Y  115 ? 1.6680 0.4284 1.3439 0.0701  -0.1000 -0.1417 116 ASP   Y N   
43416 C  CA  . ASP   Y  115 ? 1.6696 0.5720 1.3297 0.0322  -0.0937 -0.1684 116 ASP   Y CA  
43417 C  C   . ASP   Y  115 ? 1.6873 0.4836 1.3460 0.0724  -0.1136 -0.1240 116 ASP   Y C   
43418 O  O   . ASP   Y  115 ? 1.6345 0.4028 1.4018 0.1138  -0.1311 -0.0104 116 ASP   Y O   
43419 C  CB  . ASP   Y  115 ? 1.7152 0.5537 1.4291 0.0310  -0.1155 -0.2403 116 ASP   Y CB  
43420 C  CG  . ASP   Y  115 ? 1.7094 0.7101 1.5106 -0.0566 -0.1201 -0.3349 116 ASP   Y CG  
43421 O  OD1 . ASP   Y  115 ? 1.7123 0.7812 1.5929 -0.1264 -0.1457 -0.3389 116 ASP   Y OD1 
43422 O  OD2 . ASP   Y  115 ? 1.7476 0.6039 1.4592 -0.1280 -0.1285 -0.4119 116 ASP   Y OD2 
43423 N  N   . SER   Y  116 ? 1.6720 0.4844 1.2901 0.0237  -0.0532 -0.0817 117 SER   Y N   
43424 C  CA  . SER   Y  116 ? 1.6487 0.4741 1.2329 0.0047  -0.0715 -0.1219 117 SER   Y CA  
43425 C  C   . SER   Y  116 ? 1.6619 0.5188 1.3014 0.0168  -0.0351 -0.1281 117 SER   Y C   
43426 O  O   . SER   Y  116 ? 1.7064 0.4663 1.2816 0.0330  -0.0304 -0.1585 117 SER   Y O   
43427 C  CB  . SER   Y  116 ? 1.6515 0.4886 1.1557 0.0061  -0.0622 -0.0712 117 SER   Y CB  
43428 O  OG  . SER   Y  116 ? 1.7082 0.4807 1.0591 -0.0296 -0.0734 -0.1051 117 SER   Y OG  
43429 N  N   . ASP   Y  117 ? 1.6573 0.6009 1.3565 0.0270  -0.0328 -0.0784 118 ASP   Y N   
43430 C  CA  . ASP   Y  117 ? 1.6633 0.7365 1.3911 0.0079  -0.0415 -0.0898 118 ASP   Y CA  
43431 C  C   . ASP   Y  117 ? 1.6602 0.7074 1.3228 0.0566  -0.0542 -0.0621 118 ASP   Y C   
43432 O  O   . ASP   Y  117 ? 1.6576 0.6930 1.3156 0.0566  -0.0308 -0.0203 118 ASP   Y O   
43433 C  CB  . ASP   Y  117 ? 1.6797 0.7823 1.5064 0.0434  -0.0010 -0.1052 118 ASP   Y CB  
43434 C  CG  . ASP   Y  117 ? 1.7117 0.8354 1.5925 -0.0184 0.0371  -0.1250 118 ASP   Y CG  
43435 O  OD1 . ASP   Y  117 ? 1.7278 1.0483 1.6009 -0.0073 0.0348  -0.2163 118 ASP   Y OD1 
43436 O  OD2 . ASP   Y  117 ? 1.7848 1.0609 1.4712 0.0615  0.0836  -0.3001 118 ASP   Y OD2 
43437 N  N   . GLY   Y  118 ? 1.6551 0.6044 1.2483 0.0259  -0.1040 -0.0772 119 GLY   Y N   
43438 C  CA  . GLY   Y  118 ? 1.6968 0.5538 1.2903 0.0041  -0.0972 -0.0566 119 GLY   Y CA  
43439 C  C   . GLY   Y  118 ? 1.7413 0.5382 1.2774 0.0071  -0.0990 -0.0863 119 GLY   Y C   
43440 O  O   . GLY   Y  118 ? 1.8310 0.5937 1.2868 -0.0006 -0.1125 -0.1256 119 GLY   Y O   
43441 N  N   . THR   Y  119 ? 1.6643 0.5626 1.2058 0.0329  -0.1036 -0.0529 120 THR   Y N   
43442 C  CA  . THR   Y  119 ? 1.5953 0.6358 1.1925 0.0508  -0.1007 -0.0538 120 THR   Y CA  
43443 C  C   . THR   Y  119 ? 1.5639 0.5399 1.1869 0.0488  -0.1191 -0.0231 120 THR   Y C   
43444 O  O   . THR   Y  119 ? 1.5455 0.5092 1.1531 0.0666  -0.0934 -0.0427 120 THR   Y O   
43445 C  CB  . THR   Y  119 ? 1.6122 0.6496 1.2121 0.0404  -0.1111 -0.0175 120 THR   Y CB  
43446 O  OG1 . THR   Y  119 ? 1.6065 0.7278 1.2313 0.0942  -0.0767 0.0476  120 THR   Y OG1 
43447 C  CG2 . THR   Y  119 ? 1.6071 0.6896 1.2080 0.0436  -0.1283 -0.0323 120 THR   Y CG2 
43448 N  N   . ARG   Y  120 ? 1.5539 0.4902 1.2164 0.0453  -0.1178 -0.0339 121 ARG   Y N   
43449 C  CA  . ARG   Y  120 ? 1.5658 0.5652 1.1822 0.0518  -0.1343 -0.0567 121 ARG   Y CA  
43450 C  C   . ARG   Y  120 ? 1.5531 0.5353 1.1741 0.0330  -0.1775 -0.0988 121 ARG   Y C   
43451 O  O   . ARG   Y  120 ? 1.5636 0.5221 1.1232 -0.0026 -0.1882 -0.0576 121 ARG   Y O   
43452 C  CB  . ARG   Y  120 ? 1.5856 0.5680 1.2238 0.0822  -0.1313 -0.0263 121 ARG   Y CB  
43453 C  CG  . ARG   Y  120 ? 1.6130 0.6139 1.2476 0.1059  -0.1210 -0.0259 121 ARG   Y CG  
43454 C  CD  . ARG   Y  120 ? 1.6379 0.6238 1.2491 0.1046  -0.1342 -0.0038 121 ARG   Y CD  
43455 N  NE  . ARG   Y  120 ? 1.6358 0.5631 1.2474 0.1293  -0.1414 0.0264  121 ARG   Y NE  
43456 C  CZ  . ARG   Y  120 ? 1.6343 0.5905 1.2165 0.1519  -0.1628 0.0635  121 ARG   Y CZ  
43457 N  NH1 . ARG   Y  120 ? 1.6246 0.5731 1.2160 0.1674  -0.1627 0.0725  121 ARG   Y NH1 
43458 N  NH2 . ARG   Y  120 ? 1.6320 0.6574 1.2331 0.1263  -0.2135 0.1129  121 ARG   Y NH2 
43459 N  N   . LEU   Y  121 ? 1.5657 0.5674 1.1589 0.0505  -0.1547 -0.1132 122 LEU   Y N   
43460 C  CA  . LEU   Y  121 ? 1.5980 0.6476 1.1721 0.0818  -0.1881 -0.1010 122 LEU   Y CA  
43461 C  C   . LEU   Y  121 ? 1.6150 0.6552 1.1715 0.0821  -0.1760 -0.0995 122 LEU   Y C   
43462 O  O   . LEU   Y  121 ? 1.6224 0.6393 1.1583 0.0381  -0.1621 -0.1469 122 LEU   Y O   
43463 C  CB  . LEU   Y  121 ? 1.5841 0.6452 1.1757 0.0915  -0.1936 -0.0801 122 LEU   Y CB  
43464 C  CG  . LEU   Y  121 ? 1.5512 0.6512 1.2109 0.1230  -0.2057 -0.0672 122 LEU   Y CG  
43465 C  CD1 . LEU   Y  121 ? 1.5425 0.6441 1.2489 0.1122  -0.2000 -0.0392 122 LEU   Y CD1 
43466 C  CD2 . LEU   Y  121 ? 1.5686 0.6554 1.1991 0.1152  -0.2268 -0.0731 122 LEU   Y CD2 
43467 N  N   . LYS   Y  122 ? 1.6997 0.6648 1.1481 0.1037  -0.1830 -0.0800 123 LYS   Y N   
43468 C  CA  . LYS   Y  122 ? 1.7218 0.7098 1.2048 0.1052  -0.1457 -0.0810 123 LYS   Y CA  
43469 C  C   . LYS   Y  122 ? 1.7043 0.6614 1.2608 0.0812  -0.1531 -0.1226 123 LYS   Y C   
43470 O  O   . LYS   Y  122 ? 1.7442 0.5650 1.2974 0.0836  -0.1719 -0.1689 123 LYS   Y O   
43471 C  CB  . LYS   Y  122 ? 1.7766 0.6921 1.2174 0.0833  -0.1502 -0.0698 123 LYS   Y CB  
43472 C  CG  . LYS   Y  122 ? 1.8165 0.7448 1.2211 0.0637  -0.1271 -0.0944 123 LYS   Y CG  
43473 C  CD  . LYS   Y  122 ? 1.8682 0.8056 1.2178 0.0401  -0.1382 -0.1442 123 LYS   Y CD  
43474 C  CE  . LYS   Y  122 ? 1.9068 0.9088 1.2274 0.0372  -0.1661 -0.1299 123 LYS   Y CE  
43475 N  NZ  . LYS   Y  122 ? 1.9642 0.9459 1.2535 0.0306  -0.1567 -0.1744 123 LYS   Y NZ  
43476 N  N   . GLY   Y  123 ? 1.6899 0.6294 1.2909 0.0752  -0.1515 -0.1583 124 GLY   Y N   
43477 C  CA  . GLY   Y  123 ? 1.7184 0.6688 1.2906 0.0801  -0.1401 -0.1243 124 GLY   Y CA  
43478 C  C   . GLY   Y  123 ? 1.7369 0.7776 1.2972 0.0975  -0.1168 -0.1348 124 GLY   Y C   
43479 O  O   . GLY   Y  123 ? 1.7269 0.8008 1.3217 0.0955  -0.1318 -0.1003 124 GLY   Y O   
43480 N  N   . ASP   Y  124 ? 1.7964 0.8439 1.2807 0.0454  -0.1047 -0.1077 125 ASP   Y N   
43481 C  CA  . ASP   Y  124 ? 1.8499 0.8966 1.2721 0.0070  -0.0911 -0.0853 125 ASP   Y CA  
43482 C  C   . ASP   Y  124 ? 1.8221 0.8690 1.2461 0.0054  -0.0552 -0.0693 125 ASP   Y C   
43483 O  O   . ASP   Y  124 ? 1.8458 0.8447 1.2116 0.0589  0.0133  -0.0409 125 ASP   Y O   
43484 C  CB  . ASP   Y  124 ? 1.9315 0.9682 1.3407 -0.0090 -0.1677 -0.0302 125 ASP   Y CB  
43485 C  CG  . ASP   Y  124 ? 1.9429 1.1420 1.3937 -0.0785 -0.2753 0.0066  125 ASP   Y CG  
43486 O  OD1 . ASP   Y  124 ? 1.9405 1.1554 1.4689 -0.1289 -0.2941 0.0492  125 ASP   Y OD1 
43487 O  OD2 . ASP   Y  124 ? 2.0303 1.1017 1.5523 -0.0817 -0.3174 0.1386  125 ASP   Y OD2 
43488 N  N   . ILE   Y  125 ? 1.7955 0.8840 1.2197 -0.0048 -0.0385 -0.0606 126 ILE   Y N   
43489 C  CA  . ILE   Y  125 ? 1.7736 0.8371 1.2496 -0.0138 0.0075  -0.0738 126 ILE   Y CA  
43490 C  C   . ILE   Y  125 ? 1.7384 0.7674 1.2731 -0.0220 0.0235  -0.1017 126 ILE   Y C   
43491 O  O   . ILE   Y  125 ? 1.7433 0.8422 1.2952 -0.0210 0.0315  -0.1008 126 ILE   Y O   
43492 C  CB  . ILE   Y  125 ? 1.7667 0.8075 1.2404 -0.0604 -0.0251 -0.1011 126 ILE   Y CB  
43493 C  CG1 . ILE   Y  125 ? 1.8111 0.8672 1.2529 -0.1115 -0.0141 -0.1106 126 ILE   Y CG1 
43494 C  CG2 . ILE   Y  125 ? 1.7150 0.8146 1.2207 -0.0459 -0.0218 -0.0821 126 ILE   Y CG2 
43495 C  CD1 . ILE   Y  125 ? 1.8344 0.8639 1.3007 -0.1367 -0.0392 -0.0942 126 ILE   Y CD1 
43496 N  N   . PHE   Y  126 ? 1.6636 0.6806 1.3352 0.0090  0.0174  -0.0601 127 PHE   Y N   
43497 C  CA  . PHE   Y  126 ? 1.6580 0.6869 1.3266 0.0789  0.0039  -0.0038 127 PHE   Y CA  
43498 C  C   . PHE   Y  126 ? 1.5900 0.5590 1.3525 0.0986  0.0395  0.0566  127 PHE   Y C   
43499 O  O   . PHE   Y  126 ? 1.6267 0.4298 1.3297 0.1704  0.0466  0.1175  127 PHE   Y O   
43500 C  CB  . PHE   Y  126 ? 1.6525 0.7027 1.3472 0.1377  -0.0580 0.0470  127 PHE   Y CB  
43501 C  CG  . PHE   Y  126 ? 1.6514 0.8635 1.3793 0.1185  -0.1055 0.0368  127 PHE   Y CG  
43502 C  CD1 . PHE   Y  126 ? 1.6653 0.8907 1.4220 0.1238  -0.0830 0.0238  127 PHE   Y CD1 
43503 C  CD2 . PHE   Y  126 ? 1.6633 0.9011 1.3809 0.1666  -0.0931 0.0270  127 PHE   Y CD2 
43504 C  CE1 . PHE   Y  126 ? 1.6709 0.9811 1.4818 0.0938  -0.0876 0.0313  127 PHE   Y CE1 
43505 C  CE2 . PHE   Y  126 ? 1.6862 0.9806 1.4368 0.1214  -0.1095 0.0696  127 PHE   Y CE2 
43506 C  CZ  . PHE   Y  126 ? 1.7136 1.0127 1.4741 0.1284  -0.0865 0.0269  127 PHE   Y CZ  
43507 N  N   . CYS   Y  127 ? 1.7069 0.5688 1.3509 0.0513  0.0501  0.0336  128 CYS   Y N   
43508 C  CA  . CYS   Y  127 ? 1.7190 0.5278 1.3181 0.0544  0.0810  0.0178  128 CYS   Y CA  
43509 C  C   . CYS   Y  127 ? 1.7256 0.3888 1.2856 0.0717  0.0583  -0.0038 128 CYS   Y C   
43510 O  O   . CYS   Y  127 ? 1.7842 0.3199 1.2181 0.1223  0.1051  -0.0332 128 CYS   Y O   
43511 C  CB  . CYS   Y  127 ? 1.7511 0.4983 1.4616 0.0394  0.0911  -0.0289 128 CYS   Y CB  
43512 S  SG  . CYS   Y  127 ? 1.8574 0.5296 1.5195 0.0044  0.1512  0.0052  128 CYS   Y SG  
43513 N  N   . VAL   Y  128 ? 1.7217 0.4234 1.1825 0.0169  0.0756  -0.0244 129 VAL   Y N   
43514 C  CA  . VAL   Y  128 ? 1.7330 0.5396 1.1637 0.0149  0.0927  -0.0639 129 VAL   Y CA  
43515 C  C   . VAL   Y  128 ? 1.7481 0.4678 1.1377 0.0035  0.1057  -0.0279 129 VAL   Y C   
43516 O  O   . VAL   Y  128 ? 1.7925 0.3821 1.0792 0.0053  0.1532  0.0424  129 VAL   Y O   
43517 C  CB  . VAL   Y  128 ? 1.7372 0.5495 1.1369 -0.0090 0.1033  -0.0532 129 VAL   Y CB  
43518 C  CG1 . VAL   Y  128 ? 1.7247 0.5517 1.0962 0.0112  0.0948  -0.1011 129 VAL   Y CG1 
43519 C  CG2 . VAL   Y  128 ? 1.7595 0.6276 1.1499 -0.0407 0.0618  -0.0407 129 VAL   Y CG2 
43520 N  N   . GLY   Y  129 ? 1.7392 0.5418 1.1598 0.0254  0.1165  -0.0421 130 GLY   Y N   
43521 C  CA  . GLY   Y  129 ? 1.7263 0.6172 1.2048 0.0478  0.1062  -0.0966 130 GLY   Y CA  
43522 C  C   . GLY   Y  129 ? 1.6945 0.6239 1.2228 0.0646  0.0941  -0.0785 130 GLY   Y C   
43523 O  O   . GLY   Y  129 ? 1.6841 0.6432 1.0849 0.0042  0.1051  -0.0810 130 GLY   Y O   
43524 N  N   . SER   Y  130 ? 1.6853 0.6531 1.3492 0.0503  0.1179  -0.1819 131 SER   Y N   
43525 C  CA  . SER   Y  130 ? 1.6595 0.7053 1.4340 0.1333  0.1426  -0.2087 131 SER   Y CA  
43526 C  C   . SER   Y  130 ? 1.6231 0.6180 1.4177 0.1962  0.1350  -0.2377 131 SER   Y C   
43527 O  O   . SER   Y  130 ? 1.6490 0.6102 1.4734 0.2141  0.1864  -0.3324 131 SER   Y O   
43528 C  CB  . SER   Y  130 ? 1.6026 0.7350 1.4761 0.1201  0.1619  -0.2731 131 SER   Y CB  
43529 O  OG  . SER   Y  130 ? 1.5543 0.8269 1.5773 0.0175  0.1366  -0.2835 131 SER   Y OG  
43530 N  N   . GLY   Y  131 ? 1.5881 0.6673 1.3512 0.1429  0.1199  -0.2081 132 GLY   Y N   
43531 C  CA  . GLY   Y  131 ? 1.5736 0.5608 1.3851 0.1109  0.0854  -0.2111 132 GLY   Y CA  
43532 C  C   . GLY   Y  131 ? 1.6042 0.5386 1.3266 0.1444  0.1046  -0.1732 132 GLY   Y C   
43533 O  O   . GLY   Y  131 ? 1.5475 0.3723 1.3782 0.1240  0.1038  -0.1661 132 GLY   Y O   
43534 N  N   . GLN   Y  132 ? 1.5897 0.6497 1.3515 0.1116  0.0658  -0.2166 133 GLN   Y N   
43535 C  CA  . GLN   Y  132 ? 1.5955 0.7408 1.2968 0.1113  0.0354  -0.1591 133 GLN   Y CA  
43536 C  C   . GLN   Y  132 ? 1.5904 0.6982 1.2576 0.1271  0.0277  -0.1989 133 GLN   Y C   
43537 O  O   . GLN   Y  132 ? 1.5831 0.6528 1.2314 0.1069  0.0252  -0.1038 133 GLN   Y O   
43538 C  CB  . GLN   Y  132 ? 1.5508 0.8888 1.3399 0.0708  0.0546  -0.1678 133 GLN   Y CB  
43539 C  CG  . GLN   Y  132 ? 1.5268 0.8955 1.4171 0.0852  0.0396  -0.1858 133 GLN   Y CG  
43540 C  CD  . GLN   Y  132 ? 1.4066 1.1315 1.5127 0.0034  0.0264  -0.2452 133 GLN   Y CD  
43541 O  OE1 . GLN   Y  132 ? 1.4302 1.2959 1.5620 0.0626  -0.0169 -0.2034 133 GLN   Y OE1 
43542 N  NE2 . GLN   Y  132 ? 1.5035 1.1516 1.4627 0.1122  -0.0465 -0.1662 133 GLN   Y NE2 
43543 N  N   . THR   Y  133 ? 1.5550 0.6721 1.2220 0.1242  -0.0030 -0.1724 134 THR   Y N   
43544 C  CA  . THR   Y  133 ? 1.5573 0.6513 1.1824 0.0580  -0.0384 -0.1628 134 THR   Y CA  
43545 C  C   . THR   Y  133 ? 1.5887 0.6002 1.1454 0.0403  -0.0735 -0.1546 134 THR   Y C   
43546 O  O   . THR   Y  133 ? 1.5893 0.4568 1.1536 0.0391  -0.0917 -0.1780 134 THR   Y O   
43547 C  CB  . THR   Y  133 ? 1.5378 0.5814 1.2206 0.0641  -0.0644 -0.1560 134 THR   Y CB  
43548 O  OG1 . THR   Y  133 ? 1.5309 0.5004 1.2502 0.0452  -0.0032 -0.2374 134 THR   Y OG1 
43549 C  CG2 . THR   Y  133 ? 1.5124 0.6025 1.2395 0.0865  -0.0630 -0.1476 134 THR   Y CG2 
43550 N  N   . PHE   Y  134 ? 1.5917 0.6352 1.1899 0.0115  -0.0719 -0.1638 135 PHE   Y N   
43551 C  CA  . PHE   Y  134 ? 1.6482 0.6350 1.2303 0.0209  -0.0349 -0.1032 135 PHE   Y CA  
43552 C  C   . PHE   Y  134 ? 1.6293 0.6112 1.2110 -0.0011 -0.0293 -0.0872 135 PHE   Y C   
43553 O  O   . PHE   Y  134 ? 1.6240 0.4481 1.2338 0.0114  -0.0459 -0.0905 135 PHE   Y O   
43554 C  CB  . PHE   Y  134 ? 1.6618 0.7183 1.2636 0.0128  -0.0534 -0.1030 135 PHE   Y CB  
43555 C  CG  . PHE   Y  134 ? 1.6901 0.7226 1.3574 0.0262  -0.0584 -0.1674 135 PHE   Y CG  
43556 C  CD1 . PHE   Y  134 ? 1.6561 0.7299 1.3650 0.0159  -0.0734 -0.1284 135 PHE   Y CD1 
43557 C  CD2 . PHE   Y  134 ? 1.7259 0.7994 1.3357 0.0536  -0.0489 -0.1931 135 PHE   Y CD2 
43558 C  CE1 . PHE   Y  134 ? 1.6772 0.7746 1.4234 0.0356  -0.0700 -0.1772 135 PHE   Y CE1 
43559 C  CE2 . PHE   Y  134 ? 1.7108 0.7574 1.4321 0.0636  -0.0445 -0.2407 135 PHE   Y CE2 
43560 C  CZ  . PHE   Y  134 ? 1.7091 0.7656 1.4324 0.0485  -0.0527 -0.1838 135 PHE   Y CZ  
43561 N  N   . ALA   Y  135 ? 1.6335 0.6210 1.3153 0.0418  -0.0414 -0.0881 136 ALA   Y N   
43562 C  CA  . ALA   Y  135 ? 1.6413 0.6790 1.3205 0.0531  -0.0184 -0.0979 136 ALA   Y CA  
43563 C  C   . ALA   Y  135 ? 1.6853 0.6271 1.2509 0.0702  0.0002  -0.0673 136 ALA   Y C   
43564 O  O   . ALA   Y  135 ? 1.6733 0.4981 1.2298 0.0537  0.0014  -0.1021 136 ALA   Y O   
43565 C  CB  . ALA   Y  135 ? 1.6413 0.6641 1.3554 0.0535  -0.0183 -0.1098 136 ALA   Y CB  
43566 N  N   . TYR   Y  136 ? 1.6632 0.6448 1.3862 0.0819  -0.0664 -0.0456 137 TYR   Y N   
43567 C  CA  . TYR   Y  136 ? 1.7445 0.7398 1.4107 0.0286  -0.1229 -0.0612 137 TYR   Y CA  
43568 C  C   . TYR   Y  136 ? 1.8298 0.9177 1.3811 -0.0332 -0.0926 0.0330  137 TYR   Y C   
43569 O  O   . TYR   Y  136 ? 1.7936 0.8122 1.4308 -0.0482 -0.0879 -0.2459 137 TYR   Y O   
43570 C  CB  . TYR   Y  136 ? 1.7055 0.7526 1.4766 0.0323  -0.1534 -0.0270 137 TYR   Y CB  
43571 C  CG  . TYR   Y  136 ? 1.6831 0.7700 1.5484 0.0400  -0.1519 -0.0021 137 TYR   Y CG  
43572 C  CD1 . TYR   Y  136 ? 1.6813 0.8416 1.5093 0.0770  -0.1396 -0.0161 137 TYR   Y CD1 
43573 C  CD2 . TYR   Y  136 ? 1.6733 0.8485 1.5889 0.0693  -0.1068 -0.0232 137 TYR   Y CD2 
43574 C  CE1 . TYR   Y  136 ? 1.6559 0.8035 1.5867 0.1022  -0.1390 -0.0518 137 TYR   Y CE1 
43575 C  CE2 . TYR   Y  136 ? 1.6762 0.8285 1.6511 0.0714  -0.0933 -0.0709 137 TYR   Y CE2 
43576 C  CZ  . TYR   Y  136 ? 1.6584 0.7823 1.6408 0.1134  -0.0953 -0.0500 137 TYR   Y CZ  
43577 O  OH  . TYR   Y  136 ? 1.6143 0.5722 1.7751 0.3004  -0.0969 -0.1595 137 TYR   Y OH  
43578 N  N   . GLY   Y  137 ? 1.9162 0.9023 1.5630 -0.1318 -0.0769 0.0299  138 GLY   Y N   
43579 C  CA  . GLY   Y  137 ? 1.9315 1.0211 1.6307 -0.1816 -0.0821 0.1569  138 GLY   Y CA  
43580 C  C   . GLY   Y  137 ? 1.9314 1.1095 1.5877 -0.1907 -0.1060 0.2083  138 GLY   Y C   
43581 O  O   . GLY   Y  137 ? 2.0299 1.2420 1.5139 -0.2492 -0.1139 0.1832  138 GLY   Y O   
43582 N  N   . VAL   Y  138 ? 1.9135 1.1410 1.6663 -0.1801 -0.0889 0.1688  139 VAL   Y N   
43583 C  CA  . VAL   Y  138 ? 1.9978 1.0750 1.5936 -0.1957 -0.0827 0.1353  139 VAL   Y CA  
43584 C  C   . VAL   Y  138 ? 1.9505 1.0117 1.5129 -0.1503 -0.1284 0.1958  139 VAL   Y C   
43585 O  O   . VAL   Y  138 ? 1.8970 0.8771 1.5330 -0.1878 -0.1731 0.3052  139 VAL   Y O   
43586 C  CB  . VAL   Y  138 ? 1.9589 1.2013 1.6940 -0.1891 -0.0437 0.1426  139 VAL   Y CB  
43587 C  CG1 . VAL   Y  138 ? 2.0253 1.1145 1.6334 -0.2194 -0.0272 0.0960  139 VAL   Y CG1 
43588 C  CG2 . VAL   Y  138 ? 2.0471 1.2692 1.7989 -0.2305 -0.0415 0.0858  139 VAL   Y CG2 
43589 N  N   . LEU   Y  139 ? 1.9391 0.8878 1.5657 -0.1202 -0.1168 0.0844  140 LEU   Y N   
43590 C  CA  . LEU   Y  139 ? 1.9751 0.9414 1.5407 -0.0825 -0.0630 0.0317  140 LEU   Y CA  
43591 C  C   . LEU   Y  139 ? 2.0083 0.8338 1.4160 -0.0799 -0.0317 0.0108  140 LEU   Y C   
43592 O  O   . LEU   Y  139 ? 2.0210 0.7121 1.4225 -0.0871 -0.0329 -0.0389 140 LEU   Y O   
43593 C  CB  . LEU   Y  139 ? 2.0227 0.8930 1.5499 -0.0528 -0.0364 0.0070  140 LEU   Y CB  
43594 C  CG  . LEU   Y  139 ? 2.1023 0.9371 1.5206 -0.0203 -0.0055 -0.0512 140 LEU   Y CG  
43595 C  CD1 . LEU   Y  139 ? 2.1399 0.9939 1.5264 -0.0425 0.0201  -0.0618 140 LEU   Y CD1 
43596 C  CD2 . LEU   Y  139 ? 2.0920 0.8767 1.5001 0.0162  0.0287  -0.0870 140 LEU   Y CD2 
43597 N  N   . ASP   Y  140 ? 1.9531 0.8606 1.5037 -0.0851 -0.0728 0.0594  141 ASP   Y N   
43598 C  CA  . ASP   Y  140 ? 1.9813 0.9295 1.5230 -0.1351 -0.1143 0.0512  141 ASP   Y CA  
43599 C  C   . ASP   Y  140 ? 1.9714 1.0317 1.4582 -0.1065 -0.1341 0.0658  141 ASP   Y C   
43600 O  O   . ASP   Y  140 ? 1.8801 0.7076 1.5353 -0.1503 -0.1394 -0.0348 141 ASP   Y O   
43601 C  CB  . ASP   Y  140 ? 1.9685 0.9862 1.5382 -0.1293 -0.1147 0.0769  141 ASP   Y CB  
43602 C  CG  . ASP   Y  140 ? 1.9635 1.0422 1.5678 -0.1755 -0.1086 0.0687  141 ASP   Y CG  
43603 O  OD1 . ASP   Y  140 ? 1.9383 1.1469 1.4026 -0.1925 -0.1402 -0.0004 141 ASP   Y OD1 
43604 O  OD2 . ASP   Y  140 ? 2.0284 1.1505 1.6818 -0.1444 0.0052  0.0094  141 ASP   Y OD2 
43605 N  N   . SER   Y  141 ? 1.9342 1.0829 1.6550 -0.1681 -0.1335 0.1228  142 SER   Y N   
43606 C  CA  . SER   Y  141 ? 1.9647 1.3164 1.6186 -0.1178 -0.1236 0.2630  142 SER   Y CA  
43607 C  C   . SER   Y  141 ? 1.9854 1.4184 1.4800 -0.1656 -0.1306 0.3133  142 SER   Y C   
43608 O  O   . SER   Y  141 ? 1.9620 1.6010 1.3956 -0.1259 -0.1153 0.3851  142 SER   Y O   
43609 C  CB  . SER   Y  141 ? 2.0301 1.3254 1.7579 -0.0952 -0.1299 0.2195  142 SER   Y CB  
43610 O  OG  . SER   Y  141 ? 2.0259 1.4103 1.8272 -0.0301 -0.1440 0.1659  142 SER   Y OG  
43611 N  N   . ASN   Y  142 ? 1.9678 1.3900 1.4286 -0.1884 -0.0887 0.2276  143 ASN   Y N   
43612 C  CA  . ASN   Y  142 ? 1.9852 1.5232 1.3638 -0.2378 -0.0724 0.2394  143 ASN   Y CA  
43613 C  C   . ASN   Y  142 ? 2.0128 1.6377 1.2860 -0.1983 -0.1132 0.1230  143 ASN   Y C   
43614 O  O   . ASN   Y  142 ? 1.8888 1.8093 1.2852 -0.2346 -0.0829 0.2047  143 ASN   Y O   
43615 C  CB  . ASN   Y  142 ? 1.9366 1.5881 1.3991 -0.2212 -0.0370 0.2783  143 ASN   Y CB  
43616 C  CG  . ASN   Y  142 ? 1.9294 1.6298 1.4524 -0.3018 -0.0262 0.3800  143 ASN   Y CG  
43617 O  OD1 . ASN   Y  142 ? 1.8666 1.7526 1.4521 -0.3278 -0.0603 0.3806  143 ASN   Y OD1 
43618 N  ND2 . ASN   Y  142 ? 1.9737 1.7707 1.4249 -0.3349 -0.0034 0.3896  143 ASN   Y ND2 
43619 N  N   . TYR   Y  143 ? 2.0175 1.6640 1.3305 -0.2271 -0.1554 0.1197  144 TYR   Y N   
43620 C  CA  . TYR   Y  143 ? 2.1057 1.6679 1.3539 -0.1476 -0.1747 0.0356  144 TYR   Y CA  
43621 C  C   . TYR   Y  143 ? 2.2054 1.6539 1.3584 -0.1878 -0.1860 -0.0138 144 TYR   Y C   
43622 O  O   . TYR   Y  143 ? 2.2030 1.8165 1.4360 -0.1379 -0.2343 -0.0778 144 TYR   Y O   
43623 C  CB  . TYR   Y  143 ? 2.0605 1.5375 1.3592 -0.1310 -0.1794 -0.0317 144 TYR   Y CB  
43624 C  CG  . TYR   Y  143 ? 2.0564 1.5628 1.2981 -0.0377 -0.1997 -0.1643 144 TYR   Y CG  
43625 C  CD1 . TYR   Y  143 ? 2.0347 1.5402 1.2394 -0.0130 -0.1613 -0.2349 144 TYR   Y CD1 
43626 C  CD2 . TYR   Y  143 ? 2.0720 1.5821 1.3229 -0.0282 -0.2186 -0.1894 144 TYR   Y CD2 
43627 C  CE1 . TYR   Y  143 ? 2.0156 1.5114 1.2332 0.0535  -0.1473 -0.2284 144 TYR   Y CE1 
43628 C  CE2 . TYR   Y  143 ? 2.0619 1.5603 1.3454 0.0206  -0.2063 -0.1873 144 TYR   Y CE2 
43629 C  CZ  . TYR   Y  143 ? 2.0413 1.5281 1.2870 0.0307  -0.1694 -0.2412 144 TYR   Y CZ  
43630 O  OH  . TYR   Y  143 ? 1.9828 1.5162 1.2514 0.1363  -0.1520 -0.3080 144 TYR   Y OH  
43631 N  N   . LYS   Y  144 ? 2.2472 1.6244 1.5043 -0.1720 -0.1290 -0.0176 145 LYS   Y N   
43632 C  CA  . LYS   Y  144 ? 2.3249 1.6998 1.5646 -0.2644 -0.2006 0.0062  145 LYS   Y CA  
43633 C  C   . LYS   Y  144 ? 2.3661 1.7073 1.5488 -0.2406 -0.1938 0.0148  145 LYS   Y C   
43634 O  O   . LYS   Y  144 ? 2.3667 1.6029 1.5395 -0.2183 -0.1665 0.0236  145 LYS   Y O   
43635 C  CB  . LYS   Y  144 ? 2.3745 1.7095 1.6566 -0.3196 -0.1486 0.0370  145 LYS   Y CB  
43636 C  CG  . LYS   Y  144 ? 2.3775 1.7125 1.6657 -0.3305 -0.0997 0.1126  145 LYS   Y CG  
43637 C  CD  . LYS   Y  144 ? 2.4470 1.6882 1.6992 -0.3187 -0.0663 0.1412  145 LYS   Y CD  
43638 C  CE  . LYS   Y  144 ? 2.4755 1.6876 1.7641 -0.3177 -0.0738 0.1620  145 LYS   Y CE  
43639 N  NZ  . LYS   Y  144 ? 2.5016 1.7454 1.7936 -0.3275 -0.0363 0.1489  145 LYS   Y NZ  
43640 N  N   . TRP   Y  145 ? 2.4007 1.7393 1.5524 -0.2982 -0.1989 0.0532  146 TRP   Y N   
43641 C  CA  . TRP   Y  145 ? 2.4044 1.7305 1.5323 -0.3737 -0.1727 0.0443  146 TRP   Y CA  
43642 C  C   . TRP   Y  145 ? 2.4378 1.8172 1.5671 -0.3991 -0.1236 0.0375  146 TRP   Y C   
43643 O  O   . TRP   Y  145 ? 2.4197 1.6982 1.4844 -0.4661 -0.1352 0.0120  146 TRP   Y O   
43644 C  CB  . TRP   Y  145 ? 2.4310 1.8754 1.4828 -0.3866 -0.1998 0.0149  146 TRP   Y CB  
43645 C  CG  . TRP   Y  145 ? 2.4262 1.9306 1.3572 -0.3386 -0.1829 -0.0638 146 TRP   Y CG  
43646 C  CD1 . TRP   Y  145 ? 2.4794 2.0208 1.3718 -0.3231 -0.1559 -0.0890 146 TRP   Y CD1 
43647 C  CD2 . TRP   Y  145 ? 2.3297 1.9131 1.3582 -0.3094 -0.2123 -0.0629 146 TRP   Y CD2 
43648 N  NE1 . TRP   Y  145 ? 2.4061 1.9908 1.2777 -0.3360 -0.1167 -0.1388 146 TRP   Y NE1 
43649 C  CE2 . TRP   Y  145 ? 2.3227 1.9583 1.2535 -0.3278 -0.1804 -0.1121 146 TRP   Y CE2 
43650 C  CE3 . TRP   Y  145 ? 2.2373 1.9546 1.3962 -0.3051 -0.1998 -0.0402 146 TRP   Y CE3 
43651 C  CZ2 . TRP   Y  145 ? 2.2576 1.8430 1.3187 -0.2824 -0.1935 -0.1973 146 TRP   Y CZ2 
43652 C  CZ3 . TRP   Y  145 ? 2.1903 1.8906 1.4542 -0.2904 -0.1887 -0.0886 146 TRP   Y CZ3 
43653 C  CH2 . TRP   Y  145 ? 2.1970 1.9054 1.3684 -0.3073 -0.1572 -0.1134 146 TRP   Y CH2 
43654 N  N   . ASP   Y  146 ? 2.4663 2.0717 1.4916 -0.4844 0.0270  0.0039  147 ASP   Y N   
43655 C  CA  . ASP   Y  146 ? 2.5713 2.2348 1.5077 -0.4926 0.0666  -0.1792 147 ASP   Y CA  
43656 C  C   . ASP   Y  146 ? 2.4958 2.2857 1.4333 -0.4358 0.1223  -0.1789 147 ASP   Y C   
43657 O  O   . ASP   Y  146 ? 2.5955 2.3226 1.4247 -0.3398 0.1846  -0.4098 147 ASP   Y O   
43658 C  CB  . ASP   Y  146 ? 2.6212 2.3626 1.4547 -0.5357 0.0670  -0.2026 147 ASP   Y CB  
43659 C  CG  . ASP   Y  146 ? 2.6324 2.4468 1.5693 -0.5747 0.0643  -0.2105 147 ASP   Y CG  
43660 O  OD1 . ASP   Y  146 ? 2.6474 2.3797 1.7075 -0.5145 0.2311  -0.1106 147 ASP   Y OD1 
43661 O  OD2 . ASP   Y  146 ? 2.7596 2.4628 1.6509 -0.5163 0.0470  -0.2217 147 ASP   Y OD2 
43662 N  N   . LEU   Y  147 ? 2.5271 2.2016 1.3994 -0.3890 0.0521  -0.0946 148 LEU   Y N   
43663 C  CA  . LEU   Y  147 ? 2.5123 2.0202 1.3205 -0.2841 0.0436  -0.0961 148 LEU   Y CA  
43664 C  C   . LEU   Y  147 ? 2.6300 1.8626 1.1964 -0.2935 0.0799  -0.0838 148 LEU   Y C   
43665 O  O   . LEU   Y  147 ? 2.5793 1.7736 1.0125 -0.1889 0.1580  -0.1284 148 LEU   Y O   
43666 C  CB  . LEU   Y  147 ? 2.5052 1.9907 1.3139 -0.2732 0.0020  -0.1020 148 LEU   Y CB  
43667 C  CG  . LEU   Y  147 ? 2.5372 2.0126 1.3986 -0.3136 -0.0707 -0.1589 148 LEU   Y CG  
43668 C  CD1 . LEU   Y  147 ? 2.5446 2.0960 1.4411 -0.3308 -0.1102 -0.1282 148 LEU   Y CD1 
43669 C  CD2 . LEU   Y  147 ? 2.4987 1.9747 1.3790 -0.3177 -0.1125 -0.1337 148 LEU   Y CD2 
43670 N  N   . SER   Y  148 ? 2.5841 1.8989 1.1745 -0.1764 0.1310  -0.1216 149 SER   Y N   
43671 C  CA  . SER   Y  148 ? 2.6683 1.8580 1.2269 -0.1448 0.1881  -0.2134 149 SER   Y CA  
43672 C  C   . SER   Y  148 ? 2.5887 1.6971 1.3742 -0.0745 0.1508  -0.0954 149 SER   Y C   
43673 O  O   . SER   Y  148 ? 2.5853 1.8276 1.4544 -0.0290 0.2681  -0.0859 149 SER   Y O   
43674 C  CB  . SER   Y  148 ? 2.6670 1.9850 1.1954 -0.1319 0.2279  -0.2243 149 SER   Y CB  
43675 O  OG  . SER   Y  148 ? 2.6011 2.1003 1.1147 -0.1763 0.1808  -0.2147 149 SER   Y OG  
43676 N  N   . VAL   Y  149 ? 2.5780 1.6103 1.4292 -0.1082 0.2326  -0.2369 150 VAL   Y N   
43677 C  CA  . VAL   Y  149 ? 2.4615 1.5595 1.5238 -0.0585 0.2250  -0.1939 150 VAL   Y CA  
43678 C  C   . VAL   Y  149 ? 2.4150 1.5506 1.5331 -0.0816 0.2339  -0.1529 150 VAL   Y C   
43679 O  O   . VAL   Y  149 ? 2.4381 1.5747 1.4705 -0.0593 0.0791  -0.0706 150 VAL   Y O   
43680 C  CB  . VAL   Y  149 ? 2.4567 1.5806 1.5792 -0.0464 0.2528  -0.1893 150 VAL   Y CB  
43681 C  CG1 . VAL   Y  149 ? 2.4164 1.5598 1.5834 -0.0058 0.2841  -0.1641 150 VAL   Y CG1 
43682 C  CG2 . VAL   Y  149 ? 2.4757 1.5454 1.5797 -0.0388 0.2429  -0.1700 150 VAL   Y CG2 
43683 N  N   . GLU   Y  150 ? 2.3528 1.5813 1.6825 -0.1653 0.2718  -0.2254 151 GLU   Y N   
43684 C  CA  . GLU   Y  150 ? 2.2810 1.7054 1.6982 -0.2299 0.3004  -0.2375 151 GLU   Y CA  
43685 C  C   . GLU   Y  150 ? 2.2130 1.5983 1.5358 -0.3416 0.2444  -0.2625 151 GLU   Y C   
43686 O  O   . GLU   Y  150 ? 2.0921 1.5246 1.4728 -0.3553 0.2763  -0.1817 151 GLU   Y O   
43687 C  CB  . GLU   Y  150 ? 2.2796 1.8561 1.7671 -0.2296 0.3738  -0.2700 151 GLU   Y CB  
43688 C  CG  . GLU   Y  150 ? 2.2217 1.9871 1.8301 -0.2102 0.3519  -0.2937 151 GLU   Y CG  
43689 C  CD  . GLU   Y  150 ? 2.2881 2.1383 1.8914 -0.2287 0.4227  -0.2718 151 GLU   Y CD  
43690 O  OE1 . GLU   Y  150 ? 2.2738 2.3043 1.9651 -0.1517 0.3668  -0.2770 151 GLU   Y OE1 
43691 O  OE2 . GLU   Y  150 ? 2.3618 2.2894 1.8943 -0.2359 0.3652  -0.3137 151 GLU   Y OE2 
43692 N  N   . ASP   Y  151 ? 2.2250 1.5874 1.5871 -0.3744 0.2099  -0.2557 152 ASP   Y N   
43693 C  CA  . ASP   Y  151 ? 2.2136 1.6275 1.5767 -0.3597 0.2300  -0.2217 152 ASP   Y CA  
43694 C  C   . ASP   Y  151 ? 2.1934 1.5240 1.5615 -0.3522 0.1708  -0.1360 152 ASP   Y C   
43695 O  O   . ASP   Y  151 ? 2.2788 1.6467 1.4868 -0.3260 0.1003  -0.1386 152 ASP   Y O   
43696 C  CB  . ASP   Y  151 ? 2.2564 1.7560 1.5872 -0.4498 0.1694  -0.2185 152 ASP   Y CB  
43697 C  CG  . ASP   Y  151 ? 2.2630 1.8885 1.5829 -0.5561 0.1613  -0.2373 152 ASP   Y CG  
43698 O  OD1 . ASP   Y  151 ? 2.1983 2.0595 1.8532 -0.6407 0.2549  -0.1469 152 ASP   Y OD1 
43699 O  OD2 . ASP   Y  151 ? 2.3081 1.8233 1.4989 -0.6688 0.2265  -0.3101 152 ASP   Y OD2 
43700 N  N   . ALA   Y  152 ? 2.1606 1.4442 1.4236 -0.2662 0.1986  -0.2227 153 ALA   Y N   
43701 C  CA  . ALA   Y  152 ? 2.0858 1.3552 1.4632 -0.2630 0.1565  -0.1884 153 ALA   Y CA  
43702 C  C   . ALA   Y  152 ? 1.9284 1.3305 1.5413 -0.2133 0.1434  -0.1417 153 ALA   Y C   
43703 O  O   . ALA   Y  152 ? 1.9331 1.4299 1.5055 -0.2857 0.1861  -0.0774 153 ALA   Y O   
43704 C  CB  . ALA   Y  152 ? 2.1219 1.3468 1.4017 -0.2443 0.1709  -0.2046 153 ALA   Y CB  
43705 N  N   . LEU   Y  153 ? 1.9471 1.2783 1.5626 -0.1754 0.1680  -0.1588 154 LEU   Y N   
43706 C  CA  . LEU   Y  153 ? 1.8747 1.2701 1.5674 -0.1203 0.1908  -0.1356 154 LEU   Y CA  
43707 C  C   . LEU   Y  153 ? 1.8342 1.2733 1.4329 -0.1258 0.1532  -0.1010 154 LEU   Y C   
43708 O  O   . LEU   Y  153 ? 1.8030 1.3467 1.4098 -0.1048 0.1142  -0.0574 154 LEU   Y O   
43709 C  CB  . LEU   Y  153 ? 1.9074 1.2911 1.6585 -0.1015 0.2217  -0.1634 154 LEU   Y CB  
43710 C  CG  . LEU   Y  153 ? 1.9078 1.2932 1.7073 -0.0877 0.2438  -0.1598 154 LEU   Y CG  
43711 C  CD1 . LEU   Y  153 ? 1.9598 1.3743 1.7969 -0.0470 0.2871  -0.1696 154 LEU   Y CD1 
43712 C  CD2 . LEU   Y  153 ? 1.8079 1.2596 1.6781 -0.0559 0.2432  -0.1990 154 LEU   Y CD2 
43713 N  N   . TYR   Y  154 ? 1.8464 1.2034 1.4717 -0.1628 0.1399  -0.1285 155 TYR   Y N   
43714 C  CA  . TYR   Y  154 ? 1.8597 1.1951 1.4515 -0.1493 0.1419  -0.1231 155 TYR   Y CA  
43715 C  C   . TYR   Y  154 ? 1.8624 1.0924 1.4059 -0.1346 0.1271  -0.0851 155 TYR   Y C   
43716 O  O   . TYR   Y  154 ? 1.8073 1.1839 1.3565 -0.0877 0.1503  -0.0520 155 TYR   Y O   
43717 C  CB  . TYR   Y  154 ? 1.9207 1.2224 1.4760 -0.1982 0.1524  -0.1199 155 TYR   Y CB  
43718 C  CG  . TYR   Y  154 ? 1.9607 1.1991 1.5225 -0.2616 0.1511  -0.0499 155 TYR   Y CG  
43719 C  CD1 . TYR   Y  154 ? 1.9317 1.1710 1.5714 -0.2691 0.1666  -0.0386 155 TYR   Y CD1 
43720 C  CD2 . TYR   Y  154 ? 1.9782 1.1590 1.5357 -0.3154 0.0973  0.0087  155 TYR   Y CD2 
43721 C  CE1 . TYR   Y  154 ? 1.9864 1.1963 1.6062 -0.3123 0.1316  -0.0476 155 TYR   Y CE1 
43722 C  CE2 . TYR   Y  154 ? 2.0557 1.1804 1.5985 -0.3359 0.0754  -0.0164 155 TYR   Y CE2 
43723 C  CZ  . TYR   Y  154 ? 2.0402 1.2146 1.6191 -0.3172 0.0742  -0.0165 155 TYR   Y CZ  
43724 O  OH  . TYR   Y  154 ? 2.0840 1.2682 1.6890 -0.4901 0.0220  0.0021  155 TYR   Y OH  
43725 N  N   . LEU   Y  155 ? 1.9004 0.9575 1.3364 -0.1481 0.1258  -0.0993 156 LEU   Y N   
43726 C  CA  . LEU   Y  155 ? 1.8961 0.9475 1.3384 -0.1290 0.1042  -0.0631 156 LEU   Y CA  
43727 C  C   . LEU   Y  155 ? 1.8895 0.8542 1.3793 -0.0857 0.0682  0.0053  156 LEU   Y C   
43728 O  O   . LEU   Y  155 ? 1.8381 0.7640 1.3218 -0.0348 0.0622  0.1081  156 LEU   Y O   
43729 C  CB  . LEU   Y  155 ? 1.9686 1.0040 1.3345 -0.1842 0.0936  -0.1138 156 LEU   Y CB  
43730 C  CG  . LEU   Y  155 ? 1.9301 1.1378 1.3785 -0.2137 0.0649  -0.1211 156 LEU   Y CG  
43731 C  CD1 . LEU   Y  155 ? 1.9798 1.1446 1.4588 -0.2506 0.0453  -0.1207 156 LEU   Y CD1 
43732 C  CD2 . LEU   Y  155 ? 1.9913 1.1739 1.3578 -0.2498 0.0642  -0.1517 156 LEU   Y CD2 
43733 N  N   . GLY   Y  156 ? 1.9253 0.8468 1.3577 -0.0325 0.0816  -0.0581 157 GLY   Y N   
43734 C  CA  . GLY   Y  156 ? 1.9248 0.8333 1.3590 0.0097  0.0774  -0.0576 157 GLY   Y CA  
43735 C  C   . GLY   Y  156 ? 1.8923 0.7746 1.3754 0.0051  0.1055  -0.0693 157 GLY   Y C   
43736 O  O   . GLY   Y  156 ? 1.9824 0.7667 1.3515 0.0694  0.0728  -0.0887 157 GLY   Y O   
43737 N  N   . LYS   Y  157 ? 1.9034 0.7499 1.4022 -0.0518 0.1238  -0.0727 158 LYS   Y N   
43738 C  CA  . LYS   Y  157 ? 1.8540 0.8538 1.3936 -0.0840 0.1427  -0.0562 158 LYS   Y CA  
43739 C  C   . LYS   Y  157 ? 1.8662 0.8568 1.3857 -0.0871 0.1197  -0.0602 158 LYS   Y C   
43740 O  O   . LYS   Y  157 ? 1.8714 0.8284 1.3314 -0.0968 0.1239  0.0200  158 LYS   Y O   
43741 C  CB  . LYS   Y  157 ? 1.8782 0.8294 1.4199 -0.0968 0.1817  -0.0835 158 LYS   Y CB  
43742 C  CG  . LYS   Y  157 ? 1.8252 0.8176 1.4567 -0.1288 0.2216  -0.0939 158 LYS   Y CG  
43743 C  CD  . LYS   Y  157 ? 1.8348 0.8864 1.5017 -0.1671 0.2493  -0.1293 158 LYS   Y CD  
43744 C  CE  . LYS   Y  157 ? 1.8295 0.9396 1.5447 -0.1819 0.3035  -0.1511 158 LYS   Y CE  
43745 N  NZ  . LYS   Y  157 ? 1.8224 1.0730 1.6141 -0.2202 0.3272  -0.1685 158 LYS   Y NZ  
43746 N  N   . ARG   Y  158 ? 1.8789 0.9842 1.3874 -0.0974 0.0769  -0.0365 159 ARG   Y N   
43747 C  CA  . ARG   Y  158 ? 1.8625 0.9840 1.4420 -0.1044 0.0764  -0.0487 159 ARG   Y CA  
43748 C  C   . ARG   Y  158 ? 1.8283 1.0377 1.4718 -0.1027 0.0776  0.0190  159 ARG   Y C   
43749 O  O   . ARG   Y  158 ? 1.7944 1.0666 1.4799 -0.1001 0.1331  0.0128  159 ARG   Y O   
43750 C  CB  . ARG   Y  158 ? 1.9205 1.0618 1.4392 -0.1626 0.0442  -0.0382 159 ARG   Y CB  
43751 C  CG  . ARG   Y  158 ? 1.9894 1.0646 1.5131 -0.1739 0.0219  0.0109  159 ARG   Y CG  
43752 C  CD  . ARG   Y  158 ? 2.0308 1.0987 1.5925 -0.2175 0.0030  0.0258  159 ARG   Y CD  
43753 N  NE  . ARG   Y  158 ? 2.1638 1.0672 1.6672 -0.2635 -0.0435 0.1300  159 ARG   Y NE  
43754 C  CZ  . ARG   Y  158 ? 2.1662 1.0499 1.7019 -0.2083 -0.0564 0.1830  159 ARG   Y CZ  
43755 N  NH1 . ARG   Y  158 ? 2.0529 1.1688 1.7239 -0.3196 -0.0252 0.0859  159 ARG   Y NH1 
43756 N  NH2 . ARG   Y  158 ? 2.2522 1.0840 1.7346 -0.1077 -0.1247 0.3482  159 ARG   Y NH2 
43757 N  N   . SER   Y  159 ? 1.8433 0.9170 1.3935 -0.0556 0.0976  0.0028  160 SER   Y N   
43758 C  CA  . SER   Y  159 ? 1.8490 0.8664 1.3619 -0.0381 0.0899  0.0424  160 SER   Y CA  
43759 C  C   . SER   Y  159 ? 1.8293 0.8108 1.3605 -0.0305 0.1053  0.0508  160 SER   Y C   
43760 O  O   . SER   Y  159 ? 1.8136 0.7606 1.3168 -0.0492 0.1595  0.1538  160 SER   Y O   
43761 C  CB  . SER   Y  159 ? 1.8627 0.8526 1.3280 -0.0295 0.0639  0.0646  160 SER   Y CB  
43762 O  OG  . SER   Y  159 ? 1.9138 0.9042 1.3277 -0.0300 0.0785  0.0886  160 SER   Y OG  
43763 N  N   . ILE   Y  160 ? 1.7742 0.8530 1.3687 0.0049  0.1053  -0.0587 161 ILE   Y N   
43764 C  CA  . ILE   Y  160 ? 1.7461 0.9037 1.3557 -0.0151 0.1002  -0.1303 161 ILE   Y CA  
43765 C  C   . ILE   Y  160 ? 1.7087 0.8860 1.3758 -0.0226 0.1353  -0.1073 161 ILE   Y C   
43766 O  O   . ILE   Y  160 ? 1.7599 0.9716 1.3701 -0.0222 0.1414  -0.1217 161 ILE   Y O   
43767 C  CB  . ILE   Y  160 ? 1.7555 0.9003 1.3647 -0.0177 0.1071  -0.1353 161 ILE   Y CB  
43768 C  CG1 . ILE   Y  160 ? 1.7449 0.9696 1.3895 -0.0634 0.0779  -0.1359 161 ILE   Y CG1 
43769 C  CG2 . ILE   Y  160 ? 1.7419 0.8556 1.3544 -0.0369 0.1160  -0.1360 161 ILE   Y CG2 
43770 C  CD1 . ILE   Y  160 ? 1.6823 1.0228 1.3776 -0.0661 0.0479  -0.1569 161 ILE   Y CD1 
43771 N  N   . LEU   Y  161 ? 1.6809 0.7973 1.4040 -0.0436 0.1117  -0.1166 162 LEU   Y N   
43772 C  CA  . LEU   Y  161 ? 1.6918 0.7950 1.4330 -0.0348 0.0933  -0.1430 162 LEU   Y CA  
43773 C  C   . LEU   Y  161 ? 1.6640 0.7241 1.4594 -0.0586 0.0287  -0.1010 162 LEU   Y C   
43774 O  O   . LEU   Y  161 ? 1.5869 0.6494 1.5948 -0.0920 0.0020  -0.1385 162 LEU   Y O   
43775 C  CB  . LEU   Y  161 ? 1.7487 0.7758 1.4158 -0.0852 0.0901  -0.1476 162 LEU   Y CB  
43776 C  CG  . LEU   Y  161 ? 1.8127 0.7219 1.4199 -0.0710 0.0900  -0.1479 162 LEU   Y CG  
43777 C  CD1 . LEU   Y  161 ? 1.7924 0.7222 1.4399 -0.0849 0.0804  -0.1913 162 LEU   Y CD1 
43778 C  CD2 . LEU   Y  161 ? 1.8282 0.7227 1.4229 -0.0947 0.0924  -0.1442 162 LEU   Y CD2 
43779 N  N   . ALA   Y  162 ? 1.7452 0.6325 1.3989 -0.0292 0.0118  -0.0511 163 ALA   Y N   
43780 C  CA  . ALA   Y  162 ? 1.8008 0.6059 1.3811 -0.0073 -0.0095 0.0029  163 ALA   Y CA  
43781 C  C   . ALA   Y  162 ? 1.8280 0.5661 1.3528 0.0361  -0.0228 -0.0511 163 ALA   Y C   
43782 O  O   . ALA   Y  162 ? 1.8786 0.6646 1.3165 0.0875  0.0016  -0.1100 163 ALA   Y O   
43783 C  CB  . ALA   Y  162 ? 1.8279 0.5941 1.3905 -0.0271 -0.0282 0.0239  163 ALA   Y CB  
43784 N  N   . ALA   Y  163 ? 1.8016 0.5939 1.3490 0.0438  -0.0168 -0.0105 164 ALA   Y N   
43785 C  CA  . ALA   Y  163 ? 1.7508 0.5332 1.3427 0.0668  -0.0394 -0.0053 164 ALA   Y CA  
43786 C  C   . ALA   Y  163 ? 1.7507 0.4238 1.3473 0.0504  -0.0403 -0.0170 164 ALA   Y C   
43787 O  O   . ALA   Y  163 ? 1.7345 0.3799 1.3751 0.0392  -0.0882 0.0107  164 ALA   Y O   
43788 C  CB  . ALA   Y  163 ? 1.7489 0.5273 1.3448 0.0751  -0.0645 -0.0346 164 ALA   Y CB  
43789 N  N   . ALA   Y  164 ? 1.7027 0.5387 1.3688 0.0252  -0.0281 -0.0369 165 ALA   Y N   
43790 C  CA  . ALA   Y  164 ? 1.6739 0.6412 1.4214 -0.0256 -0.0254 -0.0942 165 ALA   Y CA  
43791 C  C   . ALA   Y  164 ? 1.6483 0.6243 1.4988 -0.0528 -0.0204 -0.0577 165 ALA   Y C   
43792 O  O   . ALA   Y  164 ? 1.6318 0.4812 1.5212 -0.0844 -0.0844 -0.0135 165 ALA   Y O   
43793 C  CB  . ALA   Y  164 ? 1.6677 0.7268 1.4473 -0.0339 0.0030  -0.0867 165 ALA   Y CB  
43794 N  N   . HIS   Y  165 ? 1.6271 0.7605 1.4009 -0.0641 -0.0004 -0.0548 166 HIS   Y N   
43795 C  CA  . HIS   Y  165 ? 1.6561 0.7986 1.4779 -0.1199 -0.0038 -0.1298 166 HIS   Y CA  
43796 C  C   . HIS   Y  165 ? 1.6396 0.8008 1.5165 -0.1335 -0.0022 -0.1515 166 HIS   Y C   
43797 O  O   . HIS   Y  165 ? 1.6038 0.5861 1.6616 -0.2147 0.0137  -0.1471 166 HIS   Y O   
43798 C  CB  . HIS   Y  165 ? 1.7266 0.9235 1.4431 -0.0771 -0.0258 -0.1237 166 HIS   Y CB  
43799 C  CG  . HIS   Y  165 ? 1.8197 0.9151 1.4772 -0.0105 -0.0486 -0.1940 166 HIS   Y CG  
43800 N  ND1 . HIS   Y  165 ? 1.8608 0.9799 1.5149 -0.0061 -0.0557 -0.2631 166 HIS   Y ND1 
43801 C  CD2 . HIS   Y  165 ? 1.8304 0.9628 1.4508 0.0295  -0.0748 -0.2156 166 HIS   Y CD2 
43802 C  CE1 . HIS   Y  165 ? 1.8406 1.0036 1.5300 -0.0163 -0.0707 -0.1772 166 HIS   Y CE1 
43803 N  NE2 . HIS   Y  165 ? 1.8465 0.9387 1.4921 -0.0075 -0.0519 -0.1561 166 HIS   Y NE2 
43804 N  N   . ARG   Y  166 ? 1.6327 0.8682 1.5000 -0.0654 -0.0220 -0.1775 167 ARG   Y N   
43805 C  CA  . ARG   Y  166 ? 1.7395 0.7993 1.5119 -0.0110 0.0098  -0.1808 167 ARG   Y CA  
43806 C  C   . ARG   Y  166 ? 1.7136 0.8839 1.4935 0.0485  0.0603  -0.1978 167 ARG   Y C   
43807 O  O   . ARG   Y  166 ? 1.7279 0.7619 1.5926 0.0737  0.1079  -0.1929 167 ARG   Y O   
43808 C  CB  . ARG   Y  166 ? 1.7557 0.7843 1.5218 0.0065  0.0058  -0.1730 167 ARG   Y CB  
43809 C  CG  . ARG   Y  166 ? 1.8101 0.7563 1.5862 -0.0516 0.0260  -0.1749 167 ARG   Y CG  
43810 C  CD  . ARG   Y  166 ? 1.8265 0.7778 1.5957 -0.0565 0.0478  -0.1952 167 ARG   Y CD  
43811 N  NE  . ARG   Y  166 ? 1.8428 0.7834 1.6222 -0.0614 0.0547  -0.1766 167 ARG   Y NE  
43812 C  CZ  . ARG   Y  166 ? 1.8093 0.7543 1.6825 -0.0776 0.0607  -0.1318 167 ARG   Y CZ  
43813 N  NH1 . ARG   Y  166 ? 1.7839 0.6498 1.7247 -0.0445 0.0756  -0.1383 167 ARG   Y NH1 
43814 N  NH2 . ARG   Y  166 ? 1.7876 0.7314 1.6773 -0.0855 0.0549  -0.1464 167 ARG   Y NH2 
43815 N  N   . ASP   Y  167 ? 1.7169 0.8720 1.4302 0.0998  0.0629  -0.1850 168 ASP   Y N   
43816 C  CA  . ASP   Y  167 ? 1.7398 0.8369 1.3934 0.1603  0.0340  -0.1800 168 ASP   Y CA  
43817 C  C   . ASP   Y  167 ? 1.7368 0.8136 1.3373 0.1907  0.0616  -0.1839 168 ASP   Y C   
43818 O  O   . ASP   Y  167 ? 1.7532 0.7423 1.3728 0.1819  0.0972  -0.1915 168 ASP   Y O   
43819 C  CB  . ASP   Y  167 ? 1.7305 0.8914 1.3997 0.1360  0.0047  -0.2244 168 ASP   Y CB  
43820 C  CG  . ASP   Y  167 ? 1.7440 0.9638 1.4016 0.1166  0.0510  -0.2457 168 ASP   Y CG  
43821 O  OD1 . ASP   Y  167 ? 1.6866 1.0615 1.5008 0.0821  0.0882  -0.3528 168 ASP   Y OD1 
43822 O  OD2 . ASP   Y  167 ? 1.7931 0.9534 1.4679 0.1274  0.0613  -0.2404 168 ASP   Y OD2 
43823 N  N   . ALA   Y  168 ? 1.7699 0.8626 1.3094 0.2066  0.0113  -0.1873 169 ALA   Y N   
43824 C  CA  . ALA   Y  168 ? 1.7732 0.8831 1.3073 0.2413  0.0063  -0.2061 169 ALA   Y CA  
43825 C  C   . ALA   Y  168 ? 1.6739 0.9199 1.2437 0.3225  -0.0380 -0.2342 169 ALA   Y C   
43826 O  O   . ALA   Y  168 ? 1.6578 0.9038 1.2491 0.3930  -0.0030 -0.2533 169 ALA   Y O   
43827 C  CB  . ALA   Y  168 ? 1.8240 0.9169 1.3342 0.2295  0.0170  -0.2404 169 ALA   Y CB  
43828 N  N   . TYR   Y  169 ? 1.6925 0.8260 1.2010 0.3526  -0.0608 -0.1699 170 TYR   Y N   
43829 C  CA  . TYR   Y  169 ? 1.7132 0.8370 1.2178 0.3177  -0.0556 -0.1423 170 TYR   Y CA  
43830 C  C   . TYR   Y  169 ? 1.7103 0.8394 1.1556 0.2945  -0.0582 -0.1157 170 TYR   Y C   
43831 O  O   . TYR   Y  169 ? 1.7808 0.8537 1.1987 0.4129  -0.0938 -0.1927 170 TYR   Y O   
43832 C  CB  . TYR   Y  169 ? 1.6935 0.8988 1.2203 0.3700  -0.0144 -0.1746 170 TYR   Y CB  
43833 C  CG  . TYR   Y  169 ? 1.6797 0.8649 1.3097 0.3775  -0.0064 -0.2005 170 TYR   Y CG  
43834 C  CD1 . TYR   Y  169 ? 1.7008 0.8930 1.3328 0.3537  -0.0048 -0.2417 170 TYR   Y CD1 
43835 C  CD2 . TYR   Y  169 ? 1.6710 0.8804 1.3290 0.3688  -0.0203 -0.2139 170 TYR   Y CD2 
43836 C  CE1 . TYR   Y  169 ? 1.7394 0.9671 1.3263 0.3551  0.0249  -0.2560 170 TYR   Y CE1 
43837 C  CE2 . TYR   Y  169 ? 1.7184 0.9529 1.3574 0.3619  0.0119  -0.2547 170 TYR   Y CE2 
43838 C  CZ  . TYR   Y  169 ? 1.7283 1.0457 1.3568 0.3471  0.0067  -0.2374 170 TYR   Y CZ  
43839 O  OH  . TYR   Y  169 ? 1.8133 1.1040 1.3827 0.3203  0.0594  -0.2724 170 TYR   Y OH  
43840 N  N   . SER   Y  170 ? 1.6533 0.6752 1.2649 0.2463  -0.1018 -0.0231 171 SER   Y N   
43841 C  CA  . SER   Y  170 ? 1.6536 0.6940 1.2244 0.2502  -0.0904 0.0314  171 SER   Y CA  
43842 C  C   . SER   Y  170 ? 1.6768 0.7383 1.2570 0.2170  -0.1335 0.0570  171 SER   Y C   
43843 O  O   . SER   Y  170 ? 1.7519 0.7191 1.2445 0.2594  -0.1814 0.0781  171 SER   Y O   
43844 C  CB  . SER   Y  170 ? 1.6683 0.6771 1.2337 0.2589  -0.0798 0.0974  171 SER   Y CB  
43845 O  OG  . SER   Y  170 ? 1.6606 0.6805 1.2516 0.2855  -0.0738 0.1322  171 SER   Y OG  
43846 N  N   . GLY   Y  171 ? 1.6563 0.8275 1.2421 0.2102  -0.1133 0.0338  172 GLY   Y N   
43847 C  CA  . GLY   Y  171 ? 1.6532 0.8528 1.2382 0.1972  -0.1238 0.0535  172 GLY   Y CA  
43848 C  C   . GLY   Y  171 ? 1.6035 0.8952 1.2367 0.2008  -0.1306 0.0813  172 GLY   Y C   
43849 O  O   . GLY   Y  171 ? 1.5752 0.8330 1.2389 0.2885  -0.1782 0.1266  172 GLY   Y O   
43850 N  N   . GLY   Y  172 ? 1.6197 0.8623 1.2446 0.1206  -0.0933 0.0979  173 GLY   Y N   
43851 C  CA  . GLY   Y  172 ? 1.5938 0.8818 1.2817 0.1099  -0.0403 0.0888  173 GLY   Y CA  
43852 C  C   . GLY   Y  172 ? 1.6195 0.9117 1.2969 0.0592  0.0084  0.1282  173 GLY   Y C   
43853 O  O   . GLY   Y  172 ? 1.6671 0.8167 1.2666 0.0774  -0.0107 0.1412  173 GLY   Y O   
43854 N  N   . SER   Y  173 ? 1.6437 0.9397 1.3473 0.0467  0.0244  0.0910  174 SER   Y N   
43855 C  CA  . SER   Y  173 ? 1.6872 0.9669 1.3889 0.0367  0.0549  0.0605  174 SER   Y CA  
43856 C  C   . SER   Y  173 ? 1.6460 0.9603 1.4307 0.0791  0.0329  0.0761  174 SER   Y C   
43857 O  O   . SER   Y  173 ? 1.6057 0.9054 1.4337 0.1938  0.0478  0.0702  174 SER   Y O   
43858 C  CB  . SER   Y  173 ? 1.6806 1.0046 1.4913 0.0364  0.0393  0.0727  174 SER   Y CB  
43859 O  OG  . SER   Y  173 ? 1.7591 1.0503 1.4919 0.0547  0.0078  0.1311  174 SER   Y OG  
43860 N  N   . VAL   Y  174 ? 1.6976 1.0272 1.4163 0.0529  -0.0180 0.0587  175 VAL   Y N   
43861 C  CA  . VAL   Y  174 ? 1.7593 1.0659 1.4384 0.0460  -0.0345 0.0051  175 VAL   Y CA  
43862 C  C   . VAL   Y  174 ? 1.7842 1.0865 1.4150 0.0422  -0.0360 -0.0438 175 VAL   Y C   
43863 O  O   . VAL   Y  174 ? 1.8033 1.2108 1.4320 0.0361  -0.0023 -0.1096 175 VAL   Y O   
43864 C  CB  . VAL   Y  174 ? 1.7944 1.0443 1.4678 0.0301  -0.0548 0.0161  175 VAL   Y CB  
43865 C  CG1 . VAL   Y  174 ? 1.7836 1.0574 1.5058 0.0180  -0.0470 0.0118  175 VAL   Y CG1 
43866 C  CG2 . VAL   Y  174 ? 1.8026 1.0468 1.5079 0.0167  -0.0692 -0.0021 175 VAL   Y CG2 
43867 N  N   . ASN   Y  175 ? 1.8010 1.0290 1.4018 0.0667  -0.0327 -0.0423 176 ASN   Y N   
43868 C  CA  . ASN   Y  175 ? 1.8210 1.0014 1.4569 0.0490  -0.0193 -0.0304 176 ASN   Y CA  
43869 C  C   . ASN   Y  175 ? 1.7956 0.9280 1.4223 0.0583  0.0085  -0.0011 176 ASN   Y C   
43870 O  O   . ASN   Y  175 ? 1.7973 0.8676 1.4315 0.0807  0.0497  0.0615  176 ASN   Y O   
43871 C  CB  . ASN   Y  175 ? 1.8159 1.0683 1.3673 0.0480  -0.0635 -0.0459 176 ASN   Y CB  
43872 C  CG  . ASN   Y  175 ? 1.8283 1.1345 1.3622 0.0219  -0.0705 -0.0797 176 ASN   Y CG  
43873 O  OD1 . ASN   Y  175 ? 1.8395 1.0537 1.3293 -0.0135 -0.0766 -0.0300 176 ASN   Y OD1 
43874 N  ND2 . ASN   Y  175 ? 1.7692 1.2557 1.3988 0.0000  -0.0977 -0.1068 176 ASN   Y ND2 
43875 N  N   . LEU   Y  176 ? 1.8384 0.9793 1.4585 0.0548  0.0383  -0.0467 177 LEU   Y N   
43876 C  CA  . LEU   Y  176 ? 1.8729 0.9750 1.4979 0.0609  0.0234  -0.1225 177 LEU   Y CA  
43877 C  C   . LEU   Y  176 ? 1.8961 0.9760 1.4935 0.0805  0.0179  -0.1325 177 LEU   Y C   
43878 O  O   . LEU   Y  176 ? 1.9062 0.8668 1.4800 0.0922  0.0505  -0.1689 177 LEU   Y O   
43879 C  CB  . LEU   Y  176 ? 1.8709 0.9515 1.5533 0.0687  0.0482  -0.1128 177 LEU   Y CB  
43880 C  CG  . LEU   Y  176 ? 1.8756 0.9256 1.5971 0.0676  0.0678  -0.1323 177 LEU   Y CG  
43881 C  CD1 . LEU   Y  176 ? 1.8760 0.9628 1.6626 0.0514  0.1030  -0.1379 177 LEU   Y CD1 
43882 C  CD2 . LEU   Y  176 ? 1.8830 0.8668 1.6039 0.0827  0.0608  -0.1465 177 LEU   Y CD2 
43883 N  N   . TYR   Y  177 ? 1.9273 0.9391 1.5402 0.0685  0.0187  -0.1857 178 TYR   Y N   
43884 C  CA  . TYR   Y  177 ? 1.9227 0.9796 1.6120 0.0784  0.0225  -0.2638 178 TYR   Y CA  
43885 C  C   . TYR   Y  177 ? 1.9712 0.9944 1.5748 0.0593  0.0492  -0.3086 178 TYR   Y C   
43886 O  O   . TYR   Y  177 ? 1.9695 1.0105 1.5789 0.0562  0.0228  -0.2979 178 TYR   Y O   
43887 C  CB  . TYR   Y  177 ? 1.8711 0.8700 1.5705 0.1040  -0.0128 -0.3133 178 TYR   Y CB  
43888 C  CG  . TYR   Y  177 ? 1.8324 0.8219 1.6221 0.1696  -0.0475 -0.3723 178 TYR   Y CG  
43889 C  CD1 . TYR   Y  177 ? 1.7945 0.8868 1.5912 0.2134  -0.0360 -0.3680 178 TYR   Y CD1 
43890 C  CD2 . TYR   Y  177 ? 1.8831 0.7870 1.6838 0.1601  -0.0849 -0.4223 178 TYR   Y CD2 
43891 C  CE1 . TYR   Y  177 ? 1.7511 0.8482 1.5917 0.2527  -0.0282 -0.3931 178 TYR   Y CE1 
43892 C  CE2 . TYR   Y  177 ? 1.8459 0.8054 1.6809 0.1811  -0.0816 -0.4466 178 TYR   Y CE2 
43893 C  CZ  . TYR   Y  177 ? 1.7522 0.8504 1.6022 0.2561  -0.0503 -0.4038 178 TYR   Y CZ  
43894 O  OH  . TYR   Y  177 ? 1.7168 0.8573 1.5140 0.2745  -0.0062 -0.4793 178 TYR   Y OH  
43895 N  N   . HIS   Y  178 ? 1.9898 1.0267 1.6938 0.0929  0.1109  -0.3468 179 HIS   Y N   
43896 C  CA  . HIS   Y  178 ? 1.9911 0.9809 1.7712 0.0368  0.0904  -0.4457 179 HIS   Y CA  
43897 C  C   . HIS   Y  178 ? 1.9038 0.9516 1.9031 0.1038  0.0813  -0.4617 179 HIS   Y C   
43898 O  O   . HIS   Y  178 ? 1.8389 0.9420 2.0054 0.0577  0.0041  -0.4829 179 HIS   Y O   
43899 C  CB  . HIS   Y  178 ? 2.0899 1.0243 1.7617 -0.0273 0.1259  -0.4996 179 HIS   Y CB  
43900 C  CG  . HIS   Y  178 ? 2.1990 0.9950 1.6889 -0.0909 0.2152  -0.6089 179 HIS   Y CG  
43901 N  ND1 . HIS   Y  178 ? 2.2428 0.9561 1.7592 -0.0796 0.2329  -0.6752 179 HIS   Y ND1 
43902 C  CD2 . HIS   Y  178 ? 2.2301 1.0389 1.6347 -0.1484 0.1653  -0.6321 179 HIS   Y CD2 
43903 C  CE1 . HIS   Y  178 ? 2.3298 1.0377 1.7054 -0.1041 0.2530  -0.7302 179 HIS   Y CE1 
43904 N  NE2 . HIS   Y  178 ? 2.2898 1.0378 1.6658 -0.1373 0.2126  -0.7134 179 HIS   Y NE2 
43905 N  N   . VAL   Y  179 ? 1.8721 1.0570 1.9830 0.0995  0.1510  -0.4365 180 VAL   Y N   
43906 C  CA  . VAL   Y  179 ? 1.9237 1.0332 2.0607 0.1105  0.2091  -0.4022 180 VAL   Y CA  
43907 C  C   . VAL   Y  179 ? 2.1186 1.2743 2.0894 0.0438  0.2336  -0.4909 180 VAL   Y C   
43908 O  O   . VAL   Y  179 ? 2.0836 1.2121 2.1496 0.0861  0.2693  -0.5715 180 VAL   Y O   
43909 C  CB  . VAL   Y  179 ? 1.8913 1.0043 1.9840 0.1548  0.1684  -0.3507 180 VAL   Y CB  
43910 C  CG1 . VAL   Y  179 ? 1.8696 1.0140 2.0622 0.1608  0.1740  -0.2768 180 VAL   Y CG1 
43911 C  CG2 . VAL   Y  179 ? 1.8365 0.9147 1.9638 0.1799  0.1538  -0.3240 180 VAL   Y CG2 
43912 N  N   . THR   Y  180 ? 2.2693 1.3569 2.2092 0.1092  0.2732  -0.5433 181 THR   Y N   
43913 C  CA  . THR   Y  180 ? 2.4587 1.3735 2.2666 0.0096  0.2401  -0.5971 181 THR   Y CA  
43914 C  C   . THR   Y  180 ? 2.5631 1.3394 2.2922 0.0221  0.1679  -0.6348 181 THR   Y C   
43915 O  O   . THR   Y  180 ? 2.5225 0.9490 2.2188 -0.0290 0.1235  -0.7781 181 THR   Y O   
43916 C  CB  . THR   Y  180 ? 2.5148 1.5337 2.3538 0.0232  0.3162  -0.5946 181 THR   Y CB  
43917 O  OG1 . THR   Y  180 ? 2.4768 1.3849 2.3788 0.0287  0.3981  -0.6346 181 THR   Y OG1 
43918 C  CG2 . THR   Y  180 ? 2.4986 1.5889 2.3579 -0.0319 0.3200  -0.5315 181 THR   Y CG2 
43919 N  N   . GLU   Y  181 ? 2.5944 1.4327 2.2835 -0.0437 0.1136  -0.6102 182 GLU   Y N   
43920 C  CA  . GLU   Y  181 ? 2.5001 1.4172 2.3229 -0.0435 0.1310  -0.5298 182 GLU   Y CA  
43921 C  C   . GLU   Y  181 ? 2.5336 1.4020 2.3787 0.0243  0.1645  -0.5588 182 GLU   Y C   
43922 O  O   . GLU   Y  181 ? 2.4419 1.5374 2.5008 -0.0550 0.2054  -0.4226 182 GLU   Y O   
43923 C  CB  . GLU   Y  181 ? 2.5397 1.5552 2.2732 -0.0522 0.1604  -0.4369 182 GLU   Y CB  
43924 C  CG  . GLU   Y  181 ? 2.5654 1.6364 2.2408 -0.0790 0.1614  -0.3869 182 GLU   Y CG  
43925 C  CD  . GLU   Y  181 ? 2.5884 1.7473 2.2109 -0.1223 0.1924  -0.3263 182 GLU   Y CD  
43926 O  OE1 . GLU   Y  181 ? 2.5102 1.8647 2.2534 -0.1482 0.1672  -0.3265 182 GLU   Y OE1 
43927 O  OE2 . GLU   Y  181 ? 2.6389 1.7805 2.1492 -0.1291 0.1110  -0.2452 182 GLU   Y OE2 
43928 N  N   . ASP   Y  182 ? 2.5192 1.4421 2.2818 0.0541  0.1815  -0.6050 183 ASP   Y N   
43929 C  CA  . ASP   Y  182 ? 2.5288 1.4913 2.1465 0.0905  0.2553  -0.5774 183 ASP   Y CA  
43930 C  C   . ASP   Y  182 ? 2.4390 1.2662 2.1299 0.1755  0.2542  -0.5731 183 ASP   Y C   
43931 O  O   . ASP   Y  182 ? 2.4897 1.0632 2.1110 0.1986  0.3375  -0.5921 183 ASP   Y O   
43932 C  CB  . ASP   Y  182 ? 2.5884 1.6103 2.1179 0.0900  0.3243  -0.5589 183 ASP   Y CB  
43933 C  CG  . ASP   Y  182 ? 2.6520 1.6444 2.0946 0.0594  0.4553  -0.5303 183 ASP   Y CG  
43934 O  OD1 . ASP   Y  182 ? 2.6686 1.6636 1.9808 0.1384  0.5520  -0.6301 183 ASP   Y OD1 
43935 O  OD2 . ASP   Y  182 ? 2.7190 1.7097 1.9319 0.0466  0.4891  -0.5410 183 ASP   Y OD2 
43936 N  N   . GLY   Y  183 ? 2.4139 1.2743 2.0152 0.1193  0.2809  -0.5654 184 GLY   Y N   
43937 C  CA  . GLY   Y  183 ? 2.3070 1.2380 2.0020 0.0883  0.2513  -0.4903 184 GLY   Y CA  
43938 C  C   . GLY   Y  183 ? 2.2362 1.2265 2.0420 0.1202  0.2407  -0.4890 184 GLY   Y C   
43939 O  O   . GLY   Y  183 ? 2.3128 1.2733 1.9967 0.1412  0.1909  -0.5041 184 GLY   Y O   
43940 N  N   . TRP   Y  184 ? 2.0857 1.1555 2.0109 0.1255  0.2098  -0.3806 185 TRP   Y N   
43941 C  CA  . TRP   Y  184 ? 2.0043 1.1541 2.0194 0.0895  0.1464  -0.3320 185 TRP   Y CA  
43942 C  C   . TRP   Y  184 ? 1.9745 1.1114 2.0349 0.1681  0.1710  -0.3465 185 TRP   Y C   
43943 O  O   . TRP   Y  184 ? 1.9421 1.2694 2.0291 0.2785  0.2463  -0.3790 185 TRP   Y O   
43944 C  CB  . TRP   Y  184 ? 1.9493 0.9428 1.9660 0.0725  0.0567  -0.3037 185 TRP   Y CB  
43945 C  CG  . TRP   Y  184 ? 1.8798 0.8181 2.1364 0.0504  -0.0091 -0.2792 185 TRP   Y CG  
43946 C  CD1 . TRP   Y  184 ? 1.8626 0.9043 2.1834 0.0325  -0.0262 -0.2057 185 TRP   Y CD1 
43947 C  CD2 . TRP   Y  184 ? 1.9285 0.7094 2.1604 0.0001  -0.0687 -0.3074 185 TRP   Y CD2 
43948 N  NE1 . TRP   Y  184 ? 1.8570 1.0165 2.1710 -0.0383 -0.0672 -0.1770 185 TRP   Y NE1 
43949 C  CE2 . TRP   Y  184 ? 1.9170 0.8712 2.1412 -0.0571 -0.1076 -0.2286 185 TRP   Y CE2 
43950 C  CE3 . TRP   Y  184 ? 1.9581 0.6101 2.1456 0.0202  -0.0663 -0.3450 185 TRP   Y CE3 
43951 C  CZ2 . TRP   Y  184 ? 1.9423 0.8778 2.1280 -0.0657 -0.1277 -0.2348 185 TRP   Y CZ2 
43952 C  CZ3 . TRP   Y  184 ? 1.9567 0.6911 2.1731 0.0010  -0.0767 -0.3210 185 TRP   Y CZ3 
43953 C  CH2 . TRP   Y  184 ? 1.9397 0.8031 2.1558 -0.0354 -0.1052 -0.2663 185 TRP   Y CH2 
43954 N  N   . ILE   Y  185 ? 1.9630 1.1725 2.0187 0.0334  0.1812  -0.3819 186 ILE   Y N   
43955 C  CA  . ILE   Y  185 ? 1.9316 1.2907 2.0598 0.0600  0.2201  -0.3531 186 ILE   Y CA  
43956 C  C   . ILE   Y  185 ? 1.8788 1.3250 1.9530 0.0057  0.1582  -0.3140 186 ILE   Y C   
43957 O  O   . ILE   Y  185 ? 1.8913 1.3245 1.9714 0.0175  0.2064  -0.3195 186 ILE   Y O   
43958 C  CB  . ILE   Y  185 ? 1.9083 1.3436 2.0556 0.0535  0.3150  -0.4578 186 ILE   Y CB  
43959 C  CG1 . ILE   Y  185 ? 1.9388 1.3402 2.0484 0.0739  0.3400  -0.4623 186 ILE   Y CG1 
43960 C  CG2 . ILE   Y  185 ? 1.8903 1.3830 2.0663 0.0768  0.3742  -0.5006 186 ILE   Y CG2 
43961 C  CD1 . ILE   Y  185 ? 1.9828 1.4322 2.0113 0.0358  0.3512  -0.4614 186 ILE   Y CD1 
43962 N  N   . TYR   Y  186 ? 1.8297 1.2589 1.9536 0.0546  0.1767  -0.2022 187 TYR   Y N   
43963 C  CA  . TYR   Y  186 ? 1.7625 1.2013 1.8683 0.1490  0.1469  -0.1574 187 TYR   Y CA  
43964 C  C   . TYR   Y  186 ? 1.7395 1.3010 1.9407 0.1131  0.1943  -0.1549 187 TYR   Y C   
43965 O  O   . TYR   Y  186 ? 1.6759 1.5248 2.1213 0.1212  0.2275  -0.2009 187 TYR   Y O   
43966 C  CB  . TYR   Y  186 ? 1.7490 1.0362 1.8770 0.1626  0.1857  -0.1172 187 TYR   Y CB  
43967 C  CG  . TYR   Y  186 ? 1.7237 0.8607 1.9030 0.1769  0.1631  -0.0428 187 TYR   Y CG  
43968 C  CD1 . TYR   Y  186 ? 1.6987 0.7485 1.8267 0.1395  0.1274  -0.0369 187 TYR   Y CD1 
43969 C  CD2 . TYR   Y  186 ? 1.7283 0.7572 1.9563 0.1553  0.1696  -0.0479 187 TYR   Y CD2 
43970 C  CE1 . TYR   Y  186 ? 1.6781 0.7096 1.8219 0.1643  0.1408  -0.0332 187 TYR   Y CE1 
43971 C  CE2 . TYR   Y  186 ? 1.6939 0.7560 1.9407 0.1577  0.1552  -0.0375 187 TYR   Y CE2 
43972 C  CZ  . TYR   Y  186 ? 1.6838 0.7671 1.8569 0.1558  0.1346  -0.0382 187 TYR   Y CZ  
43973 O  OH  . TYR   Y  186 ? 1.6609 0.8764 1.8197 0.1822  0.1371  -0.0756 187 TYR   Y OH  
43974 N  N   . HIS   Y  187 ? 1.7269 1.2713 1.9175 0.0929  0.1395  -0.0858 188 HIS   Y N   
43975 C  CA  . HIS   Y  187 ? 1.7200 1.3434 1.9030 0.0667  0.1480  -0.0482 188 HIS   Y CA  
43976 C  C   . HIS   Y  187 ? 1.6989 1.3508 1.8397 0.0832  0.1147  -0.0067 188 HIS   Y C   
43977 O  O   . HIS   Y  187 ? 1.7253 1.3523 1.8384 0.1012  0.1157  -0.0330 188 HIS   Y O   
43978 C  CB  . HIS   Y  187 ? 1.7373 1.4080 1.8644 0.0428  0.1540  -0.0217 188 HIS   Y CB  
43979 C  CG  . HIS   Y  187 ? 1.7712 1.4360 1.8736 0.0543  0.2265  -0.0436 188 HIS   Y CG  
43980 N  ND1 . HIS   Y  187 ? 1.7237 1.5444 1.9675 0.0513  0.2905  -0.0867 188 HIS   Y ND1 
43981 C  CD2 . HIS   Y  187 ? 1.7889 1.3633 1.8720 0.0848  0.2289  -0.0169 188 HIS   Y CD2 
43982 C  CE1 . HIS   Y  187 ? 1.7713 1.5005 1.9771 0.0736  0.3286  -0.0962 188 HIS   Y CE1 
43983 N  NE2 . HIS   Y  187 ? 1.7949 1.4070 1.9280 0.1122  0.3050  -0.0487 188 HIS   Y NE2 
43984 N  N   . GLY   Y  188 ? 1.7046 1.2480 1.8464 0.0894  0.1311  0.0030  189 GLY   Y N   
43985 C  CA  . GLY   Y  188 ? 1.6914 1.1756 1.8112 0.1290  0.1360  0.0062  189 GLY   Y CA  
43986 C  C   . GLY   Y  188 ? 1.6485 1.0736 1.7695 0.1299  0.0708  0.0107  189 GLY   Y C   
43987 O  O   . GLY   Y  188 ? 1.6395 0.9849 1.7071 0.0870  0.0401  0.0397  189 GLY   Y O   
43988 N  N   . ASN   Y  189 ? 1.6740 1.0823 1.7626 0.1662  0.0825  -0.0417 190 ASN   Y N   
43989 C  CA  . ASN   Y  189 ? 1.6469 1.0934 1.7617 0.1887  0.0854  -0.0419 190 ASN   Y CA  
43990 C  C   . ASN   Y  189 ? 1.6303 1.0622 1.8101 0.1808  0.0796  -0.1069 190 ASN   Y C   
43991 O  O   . ASN   Y  189 ? 1.6274 1.1015 1.9750 0.0802  0.0558  -0.1298 190 ASN   Y O   
43992 C  CB  . ASN   Y  189 ? 1.6225 1.0580 1.7035 0.2287  0.1295  -0.0994 190 ASN   Y CB  
43993 C  CG  . ASN   Y  189 ? 1.5671 0.9692 1.7057 0.2342  0.0874  -0.0849 190 ASN   Y CG  
43994 O  OD1 . ASN   Y  189 ? 1.5388 0.8698 1.6518 0.2676  0.1426  -0.0746 190 ASN   Y OD1 
43995 N  ND2 . ASN   Y  189 ? 1.5561 0.9189 1.6805 0.3260  0.0917  -0.1047 190 ASN   Y ND2 
43996 N  N   . HIS   Y  190 ? 1.6810 0.9958 1.7437 0.1631  0.0776  -0.1495 191 HIS   Y N   
43997 C  CA  . HIS   Y  190 ? 1.7518 1.0559 1.7253 0.1108  0.0806  -0.0886 191 HIS   Y CA  
43998 C  C   . HIS   Y  190 ? 1.8010 1.0851 1.6414 0.0842  0.0272  -0.0690 191 HIS   Y C   
43999 O  O   . HIS   Y  190 ? 1.7977 1.0985 1.6322 0.1051  -0.0129 0.0246  191 HIS   Y O   
44000 C  CB  . HIS   Y  190 ? 1.7831 1.0085 1.6513 0.1179  0.1204  -0.1258 191 HIS   Y CB  
44001 C  CG  . HIS   Y  190 ? 1.7896 1.0535 1.6456 0.1501  0.1843  -0.1297 191 HIS   Y CG  
44002 N  ND1 . HIS   Y  190 ? 1.7916 1.0566 1.6964 0.1350  0.2140  -0.1266 191 HIS   Y ND1 
44003 C  CD2 . HIS   Y  190 ? 1.8032 1.0446 1.6249 0.1628  0.1856  -0.1347 191 HIS   Y CD2 
44004 C  CE1 . HIS   Y  190 ? 1.8365 1.1244 1.6992 0.1364  0.2226  -0.1637 191 HIS   Y CE1 
44005 N  NE2 . HIS   Y  190 ? 1.8338 1.1340 1.6507 0.1564  0.2291  -0.1408 191 HIS   Y NE2 
44006 N  N   . ASP   Y  191 ? 1.8101 1.0986 1.6597 0.0704  0.0096  -0.0430 192 ASP   Y N   
44007 C  CA  . ASP   Y  191 ? 1.8050 1.0245 1.6866 0.0656  0.0003  -0.0339 192 ASP   Y CA  
44008 C  C   . ASP   Y  191 ? 1.7848 0.9639 1.5948 0.0424  0.0466  -0.0825 192 ASP   Y C   
44009 O  O   . ASP   Y  191 ? 1.7938 0.9613 1.6593 -0.0036 0.0800  -0.0639 192 ASP   Y O   
44010 C  CB  . ASP   Y  191 ? 1.8210 0.9998 1.7463 0.0551  -0.0216 -0.0489 192 ASP   Y CB  
44011 C  CG  . ASP   Y  191 ? 1.8110 0.8818 1.7923 0.0928  -0.0671 -0.0699 192 ASP   Y CG  
44012 O  OD1 . ASP   Y  191 ? 1.7963 1.0044 1.8527 0.0572  -0.1411 -0.0849 192 ASP   Y OD1 
44013 O  OD2 . ASP   Y  191 ? 1.8759 0.7972 1.7954 0.0854  -0.1139 -0.0341 192 ASP   Y OD2 
44014 N  N   . VAL   Y  192 ? 1.7847 0.9657 1.5446 0.0175  0.0297  -0.1267 193 VAL   Y N   
44015 C  CA  . VAL   Y  192 ? 1.7705 0.9918 1.5051 0.0331  0.0325  -0.1215 193 VAL   Y CA  
44016 C  C   . VAL   Y  192 ? 1.7464 0.9669 1.5282 0.0424  0.0696  -0.0835 193 VAL   Y C   
44017 O  O   . VAL   Y  192 ? 1.6539 0.9729 1.4936 0.1389  0.0732  -0.0965 193 VAL   Y O   
44018 C  CB  . VAL   Y  192 ? 1.7643 0.9455 1.4758 0.0370  0.0081  -0.1383 193 VAL   Y CB  
44019 C  CG1 . VAL   Y  192 ? 1.8220 0.9471 1.4446 0.0287  -0.0205 -0.0945 193 VAL   Y CG1 
44020 C  CG2 . VAL   Y  192 ? 1.7523 0.9680 1.4706 0.0341  0.0063  -0.1625 193 VAL   Y CG2 
44021 N  N   . GLY   Y  193 ? 1.7395 1.0557 1.5810 -0.0103 0.0365  -0.1287 194 GLY   Y N   
44022 C  CA  . GLY   Y  193 ? 1.7828 1.0719 1.6174 -0.0405 0.0560  -0.1604 194 GLY   Y CA  
44023 C  C   . GLY   Y  193 ? 1.8265 1.1183 1.6192 -0.0606 0.0696  -0.1590 194 GLY   Y C   
44024 O  O   . GLY   Y  193 ? 1.8257 1.1379 1.5816 -0.0951 0.0728  -0.1124 194 GLY   Y O   
44025 N  N   . GLU   Y  194 ? 1.8762 1.1412 1.6492 -0.0319 0.0798  -0.1723 195 GLU   Y N   
44026 C  CA  . GLU   Y  194 ? 1.9234 1.1396 1.6533 -0.0149 0.0918  -0.1508 195 GLU   Y CA  
44027 C  C   . GLU   Y  194 ? 1.8763 1.0371 1.5881 0.0106  0.1502  -0.1311 195 GLU   Y C   
44028 O  O   . GLU   Y  194 ? 1.8420 1.0500 1.5159 0.0504  0.2135  -0.1639 195 GLU   Y O   
44029 C  CB  . GLU   Y  194 ? 1.9810 1.2138 1.7392 0.0412  0.0946  -0.1713 195 GLU   Y CB  
44030 C  CG  . GLU   Y  194 ? 2.0068 1.3276 1.8639 0.0684  0.0337  -0.1934 195 GLU   Y CG  
44031 C  CD  . GLU   Y  194 ? 2.0908 1.3848 1.8909 0.1475  -0.0240 -0.1632 195 GLU   Y CD  
44032 O  OE1 . GLU   Y  194 ? 2.1726 1.4781 1.9197 0.2308  -0.0805 -0.2466 195 GLU   Y OE1 
44033 O  OE2 . GLU   Y  194 ? 2.1624 1.4230 1.9987 0.2277  -0.0483 -0.2093 195 GLU   Y OE2 
44034 N  N   . LEU   Y  195 ? 1.8549 1.0321 1.5960 0.0270  0.1269  -0.1180 196 LEU   Y N   
44035 C  CA  . LEU   Y  195 ? 1.8666 1.0163 1.5782 0.0283  0.1331  -0.1020 196 LEU   Y CA  
44036 C  C   . LEU   Y  195 ? 1.8745 1.0008 1.5587 0.0244  0.1287  -0.1138 196 LEU   Y C   
44037 O  O   . LEU   Y  195 ? 1.8606 0.9990 1.5471 0.0385  0.1913  -0.1018 196 LEU   Y O   
44038 C  CB  . LEU   Y  195 ? 1.8846 1.0316 1.5637 0.0012  0.1148  -0.1152 196 LEU   Y CB  
44039 C  CG  . LEU   Y  195 ? 1.9044 1.0237 1.5168 -0.0128 0.1272  -0.1077 196 LEU   Y CG  
44040 C  CD1 . LEU   Y  195 ? 1.9438 1.0378 1.5011 -0.0605 0.1424  -0.0763 196 LEU   Y CD1 
44041 C  CD2 . LEU   Y  195 ? 1.8641 1.0511 1.4874 0.0016  0.1476  -0.1118 196 LEU   Y CD2 
44042 N  N   . PHE   Y  196 ? 1.8235 0.9401 1.6161 0.0558  0.0843  -0.1505 197 PHE   Y N   
44043 C  CA  . PHE   Y  196 ? 1.8038 0.9024 1.6252 0.0178  0.0513  -0.1234 197 PHE   Y CA  
44044 C  C   . PHE   Y  196 ? 1.8479 0.7772 1.5744 0.0621  0.0227  -0.1297 197 PHE   Y C   
44045 O  O   . PHE   Y  196 ? 1.8217 0.6537 1.5442 -0.0138 0.0051  -0.1756 197 PHE   Y O   
44046 C  CB  . PHE   Y  196 ? 1.7771 0.8950 1.6648 0.0508  0.0428  -0.1549 197 PHE   Y CB  
44047 C  CG  . PHE   Y  196 ? 1.7849 0.8875 1.7249 0.0450  -0.0078 -0.1289 197 PHE   Y CG  
44048 C  CD1 . PHE   Y  196 ? 1.7947 0.8995 1.7156 0.0470  -0.0750 -0.1338 197 PHE   Y CD1 
44049 C  CD2 . PHE   Y  196 ? 1.7539 0.9033 1.7583 0.0369  0.0035  -0.1294 197 PHE   Y CD2 
44050 C  CE1 . PHE   Y  196 ? 1.8253 0.8550 1.7360 0.0201  -0.0970 -0.1365 197 PHE   Y CE1 
44051 C  CE2 . PHE   Y  196 ? 1.8277 0.8349 1.7748 0.0116  -0.0340 -0.1455 197 PHE   Y CE2 
44052 C  CZ  . PHE   Y  196 ? 1.8364 0.8255 1.7752 0.0396  -0.0879 -0.1558 197 PHE   Y CZ  
44053 N  N   . TRP   Y  197 ? 1.8171 0.8416 1.6505 0.0817  0.0486  -0.1068 198 TRP   Y N   
44054 C  CA  . TRP   Y  197 ? 1.8241 0.9938 1.6935 0.0642  0.1060  -0.0514 198 TRP   Y CA  
44055 C  C   . TRP   Y  197 ? 1.8128 1.0872 1.7237 0.0444  0.1510  -0.0842 198 TRP   Y C   
44056 O  O   . TRP   Y  197 ? 1.8061 1.1391 1.7555 0.0254  0.1883  -0.0444 198 TRP   Y O   
44057 C  CB  . TRP   Y  197 ? 1.8431 1.0793 1.7417 0.0889  0.0656  -0.0320 198 TRP   Y CB  
44058 C  CG  . TRP   Y  197 ? 1.9141 1.1132 1.7385 0.1082  -0.0025 -0.0668 198 TRP   Y CG  
44059 C  CD1 . TRP   Y  197 ? 1.9443 1.1340 1.7699 0.1651  -0.0484 -0.0677 198 TRP   Y CD1 
44060 C  CD2 . TRP   Y  197 ? 1.9985 1.0820 1.7967 0.1040  -0.0274 -0.0679 198 TRP   Y CD2 
44061 N  NE1 . TRP   Y  197 ? 2.0112 1.1399 1.8263 0.1902  -0.0431 -0.0982 198 TRP   Y NE1 
44062 C  CE2 . TRP   Y  197 ? 2.0424 1.1475 1.8050 0.1396  -0.0491 -0.0287 198 TRP   Y CE2 
44063 C  CE3 . TRP   Y  197 ? 2.0199 1.1054 1.7788 0.0574  -0.0369 -0.0259 198 TRP   Y CE3 
44064 C  CZ2 . TRP   Y  197 ? 2.0678 1.0998 1.9068 0.1429  -0.0222 -0.0099 198 TRP   Y CZ2 
44065 C  CZ3 . TRP   Y  197 ? 2.0166 1.1288 1.8601 0.0922  -0.0315 -0.0357 198 TRP   Y CZ3 
44066 C  CH2 . TRP   Y  197 ? 2.0654 1.1283 1.8736 0.0993  -0.0436 0.0145  198 TRP   Y CH2 
44067 N  N   . LYS   Y  198 ? 1.8000 1.1239 1.6906 0.0540  0.1961  -0.1457 199 LYS   Y N   
44068 C  CA  . LYS   Y  198 ? 1.7997 1.2630 1.6761 0.0291  0.2404  -0.1403 199 LYS   Y CA  
44069 C  C   . LYS   Y  198 ? 1.8160 1.1641 1.4974 -0.0067 0.2911  -0.1189 199 LYS   Y C   
44070 O  O   . LYS   Y  198 ? 1.8070 1.0997 1.5058 -0.0690 0.3239  -0.1313 199 LYS   Y O   
44071 C  CB  . LYS   Y  198 ? 1.8117 1.3017 1.6969 0.1165  0.2604  -0.2032 199 LYS   Y CB  
44072 C  CG  . LYS   Y  198 ? 1.8528 1.5069 1.6877 0.1245  0.3204  -0.2266 199 LYS   Y CG  
44073 C  CD  . LYS   Y  198 ? 1.8548 1.5594 1.7087 0.2144  0.3537  -0.2521 199 LYS   Y CD  
44074 C  CE  . LYS   Y  198 ? 1.8707 1.6072 1.7104 0.2184  0.3801  -0.2877 199 LYS   Y CE  
44075 N  NZ  . LYS   Y  198 ? 1.9288 1.7015 1.7515 0.2015  0.4285  -0.2876 199 LYS   Y NZ  
44076 N  N   . VAL   Y  199 ? 1.7534 1.1657 1.5132 0.0139  0.2402  -0.1700 200 VAL   Y N   
44077 C  CA  . VAL   Y  199 ? 1.7899 1.1848 1.4451 -0.0096 0.2214  -0.1762 200 VAL   Y CA  
44078 C  C   . VAL   Y  199 ? 1.8043 1.2072 1.4624 -0.0797 0.2170  -0.0206 200 VAL   Y C   
44079 O  O   . VAL   Y  199 ? 1.8210 1.2529 1.4021 -0.1540 0.2563  -0.0435 200 VAL   Y O   
44080 C  CB  . VAL   Y  199 ? 1.7382 1.1540 1.4126 0.0147  0.2026  -0.2320 200 VAL   Y CB  
44081 C  CG1 . VAL   Y  199 ? 1.7688 1.1501 1.3912 0.0195  0.1719  -0.2353 200 VAL   Y CG1 
44082 C  CG2 . VAL   Y  199 ? 1.7234 1.1658 1.3993 0.0401  0.2161  -0.2676 200 VAL   Y CG2 
44083 N  N   . LYS   Y  200 ? 1.8186 1.1507 1.5255 -0.1200 0.1915  -0.0235 201 LYS   Y N   
44084 C  CA  . LYS   Y  200 ? 1.8223 1.1451 1.6113 -0.1447 0.1845  0.0965  201 LYS   Y CA  
44085 C  C   . LYS   Y  200 ? 1.8311 1.1020 1.6165 -0.1664 0.1701  0.1042  201 LYS   Y C   
44086 O  O   . LYS   Y  200 ? 1.7994 1.0604 1.6192 -0.2141 0.1717  0.1138  201 LYS   Y O   
44087 C  CB  . LYS   Y  200 ? 1.8478 1.1356 1.6355 -0.1474 0.1458  0.1061  201 LYS   Y CB  
44088 C  CG  . LYS   Y  200 ? 1.8967 1.1298 1.7218 -0.1660 0.1601  0.2143  201 LYS   Y CG  
44089 C  CD  . LYS   Y  200 ? 1.9057 1.0893 1.7279 -0.1999 0.1561  0.2430  201 LYS   Y CD  
44090 C  CE  . LYS   Y  200 ? 1.9182 1.1011 1.7446 -0.2510 0.1699  0.4010  201 LYS   Y CE  
44091 N  NZ  . LYS   Y  200 ? 1.9794 0.9736 1.7170 -0.2885 0.1943  0.5033  201 LYS   Y NZ  
44092 N  N   . GLU   Y  201 ? 1.8320 1.1624 1.6753 -0.1669 0.1803  0.0949  202 GLU   Y N   
44093 C  CA  . GLU   Y  201 ? 1.9022 1.2361 1.7137 -0.1898 0.2109  0.1239  202 GLU   Y CA  
44094 C  C   . GLU   Y  201 ? 1.9697 1.2532 1.6905 -0.2071 0.2431  0.1346  202 GLU   Y C   
44095 O  O   . GLU   Y  201 ? 2.0513 1.2619 1.6828 -0.2862 0.2833  0.1606  202 GLU   Y O   
44096 C  CB  . GLU   Y  201 ? 1.8902 1.3171 1.8012 -0.1755 0.2083  0.0726  202 GLU   Y CB  
44097 C  CG  . GLU   Y  201 ? 1.8865 1.4109 1.8402 -0.1770 0.2369  0.0571  202 GLU   Y CG  
44098 C  CD  . GLU   Y  201 ? 1.8650 1.5008 1.9575 -0.1493 0.2494  0.0068  202 GLU   Y CD  
44099 O  OE1 . GLU   Y  201 ? 1.8434 1.5370 2.0721 -0.1411 0.2118  -0.0507 202 GLU   Y OE1 
44100 O  OE2 . GLU   Y  201 ? 1.9546 1.5289 1.9493 -0.1765 0.2669  -0.1011 202 GLU   Y OE2 
44101 N  N   . GLU   Y  202 ? 1.9711 1.2682 1.6722 -0.1603 0.2764  0.0856  203 GLU   Y N   
44102 C  CA  . GLU   Y  202 ? 1.9939 1.3395 1.6460 -0.1698 0.3346  0.0839  203 GLU   Y CA  
44103 C  C   . GLU   Y  202 ? 2.0125 1.3444 1.5479 -0.1854 0.3349  0.1160  203 GLU   Y C   
44104 O  O   . GLU   Y  202 ? 2.0162 1.3906 1.5393 -0.2046 0.3872  0.1290  203 GLU   Y O   
44105 C  CB  . GLU   Y  202 ? 1.9990 1.3284 1.7052 -0.1768 0.3369  0.0065  203 GLU   Y CB  
44106 C  CG  . GLU   Y  202 ? 1.9984 1.3333 1.7977 -0.1693 0.3306  -0.0465 203 GLU   Y CG  
44107 C  CD  . GLU   Y  202 ? 1.9506 1.3279 1.8547 -0.1655 0.3183  -0.1061 203 GLU   Y CD  
44108 O  OE1 . GLU   Y  202 ? 1.9631 1.3204 1.8567 -0.1662 0.3383  -0.1413 203 GLU   Y OE1 
44109 O  OE2 . GLU   Y  202 ? 1.9732 1.1912 1.9491 -0.1392 0.2881  -0.1467 203 GLU   Y OE2 
44110 N  N   . GLU   Y  203 ? 1.9992 1.3402 1.5870 -0.1869 0.3361  0.1114  204 GLU   Y N   
44111 C  CA  . GLU   Y  203 ? 2.0536 1.3235 1.5532 -0.1995 0.2673  0.1178  204 GLU   Y CA  
44112 C  C   . GLU   Y  203 ? 2.0723 1.3281 1.4717 -0.2061 0.2432  0.2425  204 GLU   Y C   
44113 O  O   . GLU   Y  203 ? 2.1338 1.3056 1.3079 -0.2869 0.3156  0.3275  204 GLU   Y O   
44114 C  CB  . GLU   Y  203 ? 2.0290 1.2868 1.5788 -0.2100 0.2670  0.0826  204 GLU   Y CB  
44115 C  CG  . GLU   Y  203 ? 2.0817 1.3427 1.5719 -0.1955 0.2124  0.0390  204 GLU   Y CG  
44116 C  CD  . GLU   Y  203 ? 2.0479 1.2884 1.5569 -0.2011 0.1900  -0.0086 204 GLU   Y CD  
44117 O  OE1 . GLU   Y  203 ? 2.0426 1.2360 1.6042 -0.2203 0.1492  0.0412  204 GLU   Y OE1 
44118 O  OE2 . GLU   Y  203 ? 2.0581 1.4085 1.5687 -0.1539 0.2061  -0.0202 204 GLU   Y OE2 
44119 N  N   . GLY   Y  204 ? 2.0852 1.2657 1.5620 -0.1859 0.2412  0.2103  205 GLY   Y N   
44120 C  CA  . GLY   Y  204 ? 2.0806 1.2708 1.5764 -0.1678 0.2189  0.2207  205 GLY   Y CA  
44121 C  C   . GLY   Y  204 ? 2.0610 1.2199 1.5954 -0.1380 0.2011  0.2094  205 GLY   Y C   
44122 O  O   . GLY   Y  204 ? 2.0404 1.2795 1.6663 -0.0856 0.1879  0.1858  205 GLY   Y O   
44123 N  N   . SER   Y  205 ? 2.0036 1.1554 1.5342 -0.0912 0.2223  0.1600  206 SER   Y N   
44124 C  CA  . SER   Y  205 ? 2.0061 1.0890 1.5358 -0.0814 0.2267  0.1922  206 SER   Y CA  
44125 C  C   . SER   Y  205 ? 2.0312 1.1065 1.5931 -0.0734 0.1583  0.1773  206 SER   Y C   
44126 O  O   . SER   Y  205 ? 1.9979 1.1284 1.5257 -0.1018 0.2602  0.2568  206 SER   Y O   
44127 C  CB  . SER   Y  205 ? 1.9858 1.0799 1.4483 -0.0672 0.2417  0.1344  206 SER   Y CB  
44128 O  OG  . SER   Y  205 ? 1.9483 1.0453 1.4205 -0.0674 0.2924  0.0693  206 SER   Y OG  
44129 N  N   . PHE   Y  206 ? 2.0527 1.1317 1.7284 -0.0230 0.2191  0.1482  207 PHE   Y N   
44130 C  CA  . PHE   Y  206 ? 2.1403 1.0493 1.7981 0.0153  0.1013  0.1196  207 PHE   Y CA  
44131 C  C   . PHE   Y  206 ? 2.1732 1.0262 1.9848 0.0242  0.1283  0.2021  207 PHE   Y C   
44132 O  O   . PHE   Y  206 ? 2.0397 1.0124 2.1805 0.0849  0.1703  0.2574  207 PHE   Y O   
44133 C  CB  . PHE   Y  206 ? 2.1782 0.9518 1.8436 0.0268  0.1111  0.0869  207 PHE   Y CB  
44134 C  CG  . PHE   Y  206 ? 2.2024 0.8616 1.8342 0.1174  0.0603  0.1075  207 PHE   Y CG  
44135 C  CD1 . PHE   Y  206 ? 2.1575 0.8043 1.8736 0.1506  0.0376  0.1257  207 PHE   Y CD1 
44136 C  CD2 . PHE   Y  206 ? 2.2291 0.8540 1.7861 0.0843  0.0653  0.0900  207 PHE   Y CD2 
44137 C  CE1 . PHE   Y  206 ? 2.1834 0.7457 1.8194 0.2022  0.0344  0.1125  207 PHE   Y CE1 
44138 C  CE2 . PHE   Y  206 ? 2.2661 0.8162 1.7536 0.0834  0.0366  0.0196  207 PHE   Y CE2 
44139 C  CZ  . PHE   Y  206 ? 2.2508 0.7446 1.7737 0.1049  0.0327  0.0104  207 PHE   Y CZ  
44140 N  N   . ASN   Y  207 ? 2.2822 0.9494 1.9710 -0.0418 0.1162  0.2770  208 ASN   Y N   
44141 C  CA  . ASN   Y  207 ? 2.2824 0.9777 2.0740 -0.1058 0.0779  0.2882  208 ASN   Y CA  
44142 C  C   . ASN   Y  207 ? 2.3803 0.6721 2.0967 -0.2055 0.0042  0.2476  208 ASN   Y C   
44143 O  O   . ASN   Y  207 ? 2.3267 0.6129 2.0467 -0.1959 0.0027  0.4031  208 ASN   Y O   
44144 C  CB  . ASN   Y  207 ? 2.2281 1.0560 2.1220 -0.0418 0.0264  0.2532  208 ASN   Y CB  
44145 C  CG  . ASN   Y  207 ? 2.1476 1.1657 2.1892 -0.0502 0.0463  0.1874  208 ASN   Y CG  
44146 O  OD1 . ASN   Y  207 ? 2.1643 1.2457 2.2309 0.0387  -0.0059 0.0738  208 ASN   Y OD1 
44147 N  ND2 . ASN   Y  207 ? 2.1405 1.2084 2.2332 -0.0598 0.0513  0.1919  208 ASN   Y ND2 
44148 N  N   . ASN   Y  208 ? 2.3859 0.8860 2.2358 -0.2537 0.0770  0.2101  209 ASN   Y N   
44149 C  CA  . ASN   Y  208 ? 2.3861 0.8876 2.3775 -0.2260 0.0801  0.0085  209 ASN   Y CA  
44150 C  C   . ASN   Y  208 ? 2.4198 0.7504 2.5155 -0.1996 0.0170  -0.0994 209 ASN   Y C   
44151 O  O   . ASN   Y  208 ? 2.4346 0.4570 2.8413 -0.1555 0.1388  -0.0229 209 ASN   Y O   
44152 C  CB  . ASN   Y  208 ? 2.2919 1.1430 2.3757 -0.2831 0.1026  -0.0177 209 ASN   Y CB  
44153 C  CG  . ASN   Y  208 ? 2.2500 1.1511 2.3326 -0.3046 0.1727  0.0507  209 ASN   Y CG  
44154 O  OD1 . ASN   Y  208 ? 2.2908 1.2017 2.4217 -0.2995 0.2377  0.0321  209 ASN   Y OD1 
44155 N  ND2 . ASN   Y  208 ? 2.2431 1.3068 2.2850 -0.3260 0.2181  0.0287  209 ASN   Y ND2 
44156 N  N   . VAL   Y  209 ? 2.3085 0.9484 2.5243 -0.1637 -0.0648 -0.1514 210 VAL   Y N   
44157 C  CA  . VAL   Y  209 ? 2.1356 0.7713 2.5984 -0.1373 0.0065  -0.1970 210 VAL   Y CA  
44158 C  C   . VAL   Y  209 ? 2.2033 0.8041 2.5455 -0.2081 -0.0624 -0.1202 210 VAL   Y C   
44159 O  O   . VAL   Y  209 ? 2.1768 0.5679 2.5989 -0.3549 -0.0305 0.0735  210 VAL   Y O   
44160 C  CB  . VAL   Y  209 ? 2.0884 0.8908 2.4810 0.0159  0.0203  -0.4478 210 VAL   Y CB  
44161 C  CG1 . VAL   Y  209 ? 2.0374 0.8635 2.5135 0.0689  0.0668  -0.4881 210 VAL   Y CG1 
44162 C  CG2 . VAL   Y  209 ? 2.0412 0.7363 2.4048 0.0842  0.0247  -0.5444 210 VAL   Y CG2 
44163 N  N   . ILE   Y  210 ? 2.1680 0.8589 2.6644 -0.2343 -0.1028 -0.1750 211 ILE   Y N   
44164 C  CA  . ILE   Y  210 ? 2.0388 1.0015 2.6022 -0.1913 -0.0723 -0.2141 211 ILE   Y CA  
44165 C  C   . ILE   Y  210 ? 2.0155 0.9278 2.5791 -0.2234 -0.0429 -0.1826 211 ILE   Y C   
44166 O  O   . ILE   Y  210 ? 1.8107 0.6372 2.7568 -0.1899 0.0513  -0.3360 211 ILE   Y O   
44167 C  CB  . ILE   Y  210 ? 2.1151 1.1616 2.5991 -0.1690 -0.1033 -0.2457 211 ILE   Y CB  
44168 C  CG1 . ILE   Y  210 ? 2.1881 1.1047 2.4416 -0.1289 -0.1653 -0.2287 211 ILE   Y CG1 
44169 C  CG2 . ILE   Y  210 ? 2.1010 1.2292 2.6475 -0.1785 -0.0810 -0.2542 211 ILE   Y CG2 
44170 C  CD1 . ILE   Y  210 ? 2.2208 1.1202 2.4070 -0.1142 -0.1501 -0.2151 211 ILE   Y CD1 
44171 N  N   . GLY   Y  211 ? 1.9809 0.9815 2.5611 -0.1865 -0.0288 -0.1846 212 GLY   Y N   
44172 C  CA  . GLY   Y  211 ? 2.0953 0.9797 2.5205 -0.1931 0.0128  -0.2120 212 GLY   Y CA  
44173 C  C   . GLY   Y  211 ? 2.1023 0.9284 2.5499 -0.1818 0.0138  -0.2434 212 GLY   Y C   
44174 O  O   . GLY   Y  211 ? 2.3131 1.1115 2.5676 -0.2340 -0.0021 -0.3416 212 GLY   Y O   
44175 O  OXT . GLY   Y  211 ? 2.2681 0.6983 2.5018 -0.2293 0.0219  -0.1996 212 GLY   Y OXT 
44176 N  N   . GLN   Z  1   ? 1.7450 1.1428 1.4569 0.0210  0.0417  -0.0373 1   GLN   Z N   
44177 C  CA  . GLN   Z  1   ? 1.6875 1.1204 1.4147 0.0418  0.0169  -0.0033 1   GLN   Z CA  
44178 C  C   . GLN   Z  1   ? 1.6824 0.8902 1.3655 0.0438  -0.0024 0.0212  1   GLN   Z C   
44179 O  O   . GLN   Z  1   ? 1.6014 1.0359 1.4263 0.0100  0.0477  -0.0152 1   GLN   Z O   
44180 C  CB  . GLN   Z  1   ? 1.8393 1.2026 1.4106 0.0279  0.0128  0.0403  1   GLN   Z CB  
44181 C  CG  . GLN   Z  1   ? 1.9249 1.2501 1.4225 0.0192  -0.0639 0.0317  1   GLN   Z CG  
44182 C  CD  . GLN   Z  1   ? 1.9893 1.2789 1.3672 0.0560  -0.0699 0.0657  1   GLN   Z CD  
44183 O  OE1 . GLN   Z  1   ? 1.9922 1.3714 1.3933 -0.0094 -0.1521 0.2064  1   GLN   Z OE1 
44184 N  NE2 . GLN   Z  1   ? 2.0439 1.2984 1.4355 0.0546  -0.1111 0.1021  1   GLN   Z NE2 
44185 N  N   . PHE   Z  2   ? 1.5661 0.9089 1.3054 0.1085  -0.0844 0.0033  2   PHE   Z N   
44186 C  CA  . PHE   Z  2   ? 1.5580 0.7861 1.2151 0.0761  -0.1266 0.0405  2   PHE   Z CA  
44187 C  C   . PHE   Z  2   ? 1.4736 0.6762 1.1897 0.0443  -0.1715 0.0523  2   PHE   Z C   
44188 O  O   . PHE   Z  2   ? 1.5023 0.6867 1.0322 0.0862  -0.1080 0.1097  2   PHE   Z O   
44189 C  CB  . PHE   Z  2   ? 1.5192 0.7728 1.2526 0.0634  -0.1586 0.0214  2   PHE   Z CB  
44190 C  CG  . PHE   Z  2   ? 1.5279 0.6306 1.2119 0.0419  -0.1506 -0.0242 2   PHE   Z CG  
44191 C  CD1 . PHE   Z  2   ? 1.5139 0.6533 1.2446 0.0382  -0.1410 -0.0561 2   PHE   Z CD1 
44192 C  CD2 . PHE   Z  2   ? 1.5074 0.6071 1.1862 0.0301  -0.1410 -0.0015 2   PHE   Z CD2 
44193 C  CE1 . PHE   Z  2   ? 1.5245 0.5722 1.2505 0.0198  -0.1232 -0.0770 2   PHE   Z CE1 
44194 C  CE2 . PHE   Z  2   ? 1.4941 0.6280 1.1875 0.0184  -0.1371 -0.0164 2   PHE   Z CE2 
44195 C  CZ  . PHE   Z  2   ? 1.5068 0.5780 1.2009 0.0177  -0.1270 -0.0583 2   PHE   Z CZ  
44196 N  N   . ASN   Z  3   ? 1.4465 0.6122 1.1773 0.0756  -0.2075 0.0298  3   ASN   Z N   
44197 C  CA  . ASN   Z  3   ? 1.3569 0.6817 1.1292 0.1020  -0.2493 -0.0441 3   ASN   Z CA  
44198 C  C   . ASN   Z  3   ? 1.3192 0.6546 1.1848 0.0724  -0.2789 -0.0243 3   ASN   Z C   
44199 O  O   . ASN   Z  3   ? 1.3137 0.5930 1.1878 0.0352  -0.2703 -0.0841 3   ASN   Z O   
44200 C  CB  . ASN   Z  3   ? 1.3605 0.7132 1.1127 0.0679  -0.2600 -0.0452 3   ASN   Z CB  
44201 C  CG  . ASN   Z  3   ? 1.3779 0.7523 1.0791 0.1090  -0.2466 -0.0885 3   ASN   Z CG  
44202 O  OD1 . ASN   Z  3   ? 1.4032 0.8484 1.1906 0.0424  -0.3119 -0.0419 3   ASN   Z OD1 
44203 N  ND2 . ASN   Z  3   ? 1.3386 0.7252 1.1585 0.0817  -0.2133 -0.1305 3   ASN   Z ND2 
44204 N  N   . PRO   Z  4   ? 1.3059 0.6407 1.2315 0.0925  -0.2829 -0.0276 4   PRO   Z N   
44205 C  CA  . PRO   Z  4   ? 1.2697 0.6881 1.2489 0.1022  -0.2777 -0.0067 4   PRO   Z CA  
44206 C  C   . PRO   Z  4   ? 1.2534 0.6271 1.2090 0.1340  -0.2786 0.0013  4   PRO   Z C   
44207 O  O   . PRO   Z  4   ? 1.1785 0.6128 1.1950 0.0984  -0.2710 -0.0266 4   PRO   Z O   
44208 C  CB  . PRO   Z  4   ? 1.2824 0.6829 1.2540 0.1299  -0.2796 -0.0217 4   PRO   Z CB  
44209 C  CG  . PRO   Z  4   ? 1.3006 0.7032 1.2465 0.1221  -0.2830 -0.0076 4   PRO   Z CG  
44210 C  CD  . PRO   Z  4   ? 1.3082 0.6498 1.2448 0.1160  -0.2996 0.0177  4   PRO   Z CD  
44211 N  N   . TYR   Z  5   ? 1.3148 0.6514 1.1746 0.1417  -0.2640 0.0228  5   TYR   Z N   
44212 C  CA  . TYR   Z  5   ? 1.3146 0.6361 1.1650 0.1737  -0.2493 0.0290  5   TYR   Z CA  
44213 C  C   . TYR   Z  5   ? 1.3212 0.6925 1.1372 0.1826  -0.2362 0.0030  5   TYR   Z C   
44214 O  O   . TYR   Z  5   ? 1.3775 0.7808 1.1388 0.1516  -0.1702 -0.0281 5   TYR   Z O   
44215 C  CB  . TYR   Z  5   ? 1.3551 0.5916 1.1889 0.1986  -0.2613 0.0352  5   TYR   Z CB  
44216 C  CG  . TYR   Z  5   ? 1.3625 0.5249 1.2025 0.2225  -0.3029 0.0636  5   TYR   Z CG  
44217 C  CD1 . TYR   Z  5   ? 1.3874 0.4898 1.2057 0.2236  -0.3074 0.0912  5   TYR   Z CD1 
44218 C  CD2 . TYR   Z  5   ? 1.3686 0.5081 1.1781 0.2371  -0.3091 0.0644  5   TYR   Z CD2 
44219 C  CE1 . TYR   Z  5   ? 1.3810 0.5007 1.1356 0.2169  -0.3408 0.1327  5   TYR   Z CE1 
44220 C  CE2 . TYR   Z  5   ? 1.3708 0.5007 1.1637 0.2062  -0.3259 0.0949  5   TYR   Z CE2 
44221 C  CZ  . TYR   Z  5   ? 1.3706 0.5075 1.1420 0.2308  -0.3282 0.1637  5   TYR   Z CZ  
44222 O  OH  . TYR   Z  5   ? 1.3936 0.5151 1.1031 0.2129  -0.3326 0.2007  5   TYR   Z OH  
44223 N  N   . GLY   Z  6   ? 1.3097 0.6740 1.1492 0.2498  -0.2287 -0.0195 6   GLY   Z N   
44224 C  CA  . GLY   Z  6   ? 1.3298 0.6823 1.1358 0.2648  -0.2356 -0.0510 6   GLY   Z CA  
44225 C  C   . GLY   Z  6   ? 1.3250 0.6802 1.1260 0.2765  -0.2300 -0.0699 6   GLY   Z C   
44226 O  O   . GLY   Z  6   ? 1.2897 0.6639 1.0602 0.2900  -0.2264 -0.0154 6   GLY   Z O   
44227 N  N   . ASP   Z  7   ? 1.3215 0.7694 1.2200 0.1989  -0.2381 -0.0472 7   ASP   Z N   
44228 C  CA  . ASP   Z  7   ? 1.3430 0.8424 1.2727 0.1802  -0.2136 -0.0476 7   ASP   Z CA  
44229 C  C   . ASP   Z  7   ? 1.3838 0.7885 1.3340 0.1583  -0.2634 -0.1067 7   ASP   Z C   
44230 O  O   . ASP   Z  7   ? 1.2781 0.8950 1.2989 0.1728  -0.3389 -0.1305 7   ASP   Z O   
44231 C  CB  . ASP   Z  7   ? 1.4220 0.9247 1.3101 0.1624  -0.1871 0.0522  7   ASP   Z CB  
44232 C  CG  . ASP   Z  7   ? 1.4243 1.1198 1.3804 0.1684  -0.1255 0.0246  7   ASP   Z CG  
44233 O  OD1 . ASP   Z  7   ? 1.4899 0.8720 1.3831 0.1832  -0.2137 0.2256  7   ASP   Z OD1 
44234 O  OD2 . ASP   Z  7   ? 1.5238 1.0928 1.4076 0.0540  -0.0434 0.0040  7   ASP   Z OD2 
44235 N  N   . ASN   Z  8   ? 1.4539 0.6530 1.3622 0.1128  -0.2603 -0.1925 8   ASN   Z N   
44236 C  CA  . ASN   Z  8   ? 1.5079 0.5386 1.3294 0.0195  -0.2962 -0.1780 8   ASN   Z CA  
44237 C  C   . ASN   Z  8   ? 1.5550 0.4566 1.3430 0.0256  -0.2462 -0.2127 8   ASN   Z C   
44238 O  O   . ASN   Z  8   ? 1.5388 0.3417 1.4355 0.1133  -0.2087 -0.2042 8   ASN   Z O   
44239 C  CB  . ASN   Z  8   ? 1.5045 0.5184 1.3269 -0.0525 -0.3106 -0.1297 8   ASN   Z CB  
44240 C  CG  . ASN   Z  8   ? 1.5807 0.4927 1.3469 -0.0767 -0.3119 -0.0783 8   ASN   Z CG  
44241 O  OD1 . ASN   Z  8   ? 1.5084 0.6305 1.3407 -0.1322 -0.3520 -0.0304 8   ASN   Z OD1 
44242 N  ND2 . ASN   Z  8   ? 1.5873 0.3374 1.3948 -0.1525 -0.3218 -0.1488 8   ASN   Z ND2 
44243 N  N   . GLY   Z  9   ? 1.5698 0.4162 1.3212 0.0183  -0.2041 -0.2244 9   GLY   Z N   
44244 C  CA  . GLY   Z  9   ? 1.5651 0.4708 1.3419 0.0388  -0.1541 -0.1824 9   GLY   Z CA  
44245 C  C   . GLY   Z  9   ? 1.6112 0.4452 1.3583 0.0481  -0.1316 -0.2197 9   GLY   Z C   
44246 O  O   . GLY   Z  9   ? 1.5915 0.4194 1.4053 0.0036  -0.1119 -0.2037 9   GLY   Z O   
44247 N  N   . GLY   Z  10  ? 1.4985 0.6478 1.4288 0.1006  -0.1018 -0.1765 10  GLY   Z N   
44248 C  CA  . GLY   Z  10  ? 1.4965 0.7166 1.4237 0.1641  -0.1404 -0.1683 10  GLY   Z CA  
44249 C  C   . GLY   Z  10  ? 1.4784 0.7419 1.4148 0.1848  -0.1790 -0.1933 10  GLY   Z C   
44250 O  O   . GLY   Z  10  ? 1.5123 0.7423 1.2829 0.2526  -0.1672 -0.2652 10  GLY   Z O   
44251 N  N   . THR   Z  11  ? 1.4684 0.7301 1.4213 0.1602  -0.1810 -0.1522 11  THR   Z N   
44252 C  CA  . THR   Z  11  ? 1.5323 0.6801 1.4222 0.1071  -0.2055 -0.1050 11  THR   Z CA  
44253 C  C   . THR   Z  11  ? 1.5627 0.5886 1.4676 0.0811  -0.2007 -0.1056 11  THR   Z C   
44254 O  O   . THR   Z  11  ? 1.6337 0.6109 1.4620 0.0293  -0.2275 -0.0657 11  THR   Z O   
44255 C  CB  . THR   Z  11  ? 1.6180 0.6738 1.4677 0.1027  -0.2336 -0.0942 11  THR   Z CB  
44256 O  OG1 . THR   Z  11  ? 1.6168 0.5530 1.4950 0.1716  -0.2513 0.0305  11  THR   Z OG1 
44257 C  CG2 . THR   Z  11  ? 1.6786 0.6090 1.5059 0.0380  -0.2510 -0.1376 11  THR   Z CG2 
44258 N  N   . ILE   Z  12  ? 1.5121 0.5209 1.4833 0.0903  -0.2035 -0.1168 12  ILE   Z N   
44259 C  CA  . ILE   Z  12  ? 1.5151 0.6173 1.5236 0.1310  -0.1884 -0.1399 12  ILE   Z CA  
44260 C  C   . ILE   Z  12  ? 1.5274 0.6332 1.5271 0.1444  -0.1603 -0.1583 12  ILE   Z C   
44261 O  O   . ILE   Z  12  ? 1.5467 0.6782 1.5377 0.1442  -0.2162 -0.1735 12  ILE   Z O   
44262 C  CB  . ILE   Z  12  ? 1.4846 0.6109 1.5308 0.1503  -0.1918 -0.1773 12  ILE   Z CB  
44263 C  CG1 . ILE   Z  12  ? 1.4984 0.6615 1.5053 0.1615  -0.1947 -0.2047 12  ILE   Z CG1 
44264 C  CG2 . ILE   Z  12  ? 1.4652 0.5835 1.5341 0.1905  -0.2143 -0.1671 12  ILE   Z CG2 
44265 C  CD1 . ILE   Z  12  ? 1.5167 0.6766 1.4976 0.1580  -0.1893 -0.2273 12  ILE   Z CD1 
44266 N  N   . LEU   Z  13  ? 1.5473 0.6867 1.5196 0.1845  -0.1511 -0.1287 13  LEU   Z N   
44267 C  CA  . LEU   Z  13  ? 1.6193 0.7320 1.5281 0.1620  -0.1258 -0.1228 13  LEU   Z CA  
44268 C  C   . LEU   Z  13  ? 1.6908 0.7587 1.4830 0.1865  -0.0956 -0.1124 13  LEU   Z C   
44269 O  O   . LEU   Z  13  ? 1.8121 0.8360 1.4514 0.2090  -0.1145 -0.0769 13  LEU   Z O   
44270 C  CB  . LEU   Z  13  ? 1.6350 0.7109 1.5886 0.1466  -0.0929 -0.1024 13  LEU   Z CB  
44271 C  CG  . LEU   Z  13  ? 1.6933 0.7717 1.6180 0.1301  -0.0434 -0.0610 13  LEU   Z CG  
44272 C  CD1 . LEU   Z  13  ? 1.6979 0.6842 1.6178 0.1351  -0.0498 -0.0376 13  LEU   Z CD1 
44273 C  CD2 . LEU   Z  13  ? 1.7190 0.8110 1.7107 0.0975  -0.0479 -0.0724 13  LEU   Z CD2 
44274 N  N   . GLY   Z  14  ? 1.6584 0.7095 1.4790 0.1669  -0.0935 -0.0981 14  GLY   Z N   
44275 C  CA  . GLY   Z  14  ? 1.6467 0.6143 1.4868 0.0990  -0.1036 -0.1055 14  GLY   Z CA  
44276 C  C   . GLY   Z  14  ? 1.6130 0.5907 1.4966 0.1065  -0.0824 -0.1358 14  GLY   Z C   
44277 O  O   . GLY   Z  14  ? 1.6140 0.6365 1.4251 0.0620  -0.1443 -0.2426 14  GLY   Z O   
44278 N  N   . ILE   Z  15  ? 1.6173 0.5869 1.5740 0.1180  -0.0138 -0.1084 15  ILE   Z N   
44279 C  CA  . ILE   Z  15  ? 1.6565 0.6499 1.6437 0.1045  0.0325  -0.0676 15  ILE   Z CA  
44280 C  C   . ILE   Z  15  ? 1.6780 0.6398 1.6925 0.0964  0.0838  -0.0452 15  ILE   Z C   
44281 O  O   . ILE   Z  15  ? 1.6966 0.6919 1.7306 -0.0043 0.0666  0.0201  15  ILE   Z O   
44282 C  CB  . ILE   Z  15  ? 1.6460 0.6678 1.7078 0.0926  0.0543  -0.0743 15  ILE   Z CB  
44283 C  CG1 . ILE   Z  15  ? 1.6247 0.6924 1.7294 0.1176  0.0640  -0.0583 15  ILE   Z CG1 
44284 C  CG2 . ILE   Z  15  ? 1.6776 0.6652 1.7108 0.1103  0.0811  -0.0917 15  ILE   Z CG2 
44285 C  CD1 . ILE   Z  15  ? 1.6200 0.6773 1.7535 0.1272  0.0754  -0.0705 15  ILE   Z CD1 
44286 N  N   . ALA   Z  16  ? 1.7149 0.5679 1.6729 0.1278  0.0873  0.0422  16  ALA   Z N   
44287 C  CA  . ALA   Z  16  ? 1.7904 0.5574 1.6609 0.1072  0.0817  0.0084  16  ALA   Z CA  
44288 C  C   . ALA   Z  16  ? 1.8306 0.5712 1.7178 0.1321  0.1279  0.0440  16  ALA   Z C   
44289 O  O   . ALA   Z  16  ? 1.8883 0.5858 1.7240 0.2400  0.0751  0.0376  16  ALA   Z O   
44290 C  CB  . ALA   Z  16  ? 1.7878 0.5869 1.6033 0.1170  0.0748  0.0383  16  ALA   Z CB  
44291 N  N   . GLY   Z  17  ? 1.8074 0.6930 1.8278 0.1603  0.1454  0.0248  17  GLY   Z N   
44292 C  CA  . GLY   Z  17  ? 1.8130 0.8595 1.8843 0.1463  0.1680  0.0041  17  GLY   Z CA  
44293 C  C   . GLY   Z  17  ? 1.7779 1.0319 1.8557 0.0860  0.1556  -0.0722 17  GLY   Z C   
44294 O  O   . GLY   Z  17  ? 1.8239 1.0962 1.7854 0.0578  0.1439  -0.1485 17  GLY   Z O   
44295 N  N   . GLU   Z  18  ? 1.7852 1.1791 1.8922 0.0782  0.1717  -0.0907 18  GLU   Z N   
44296 C  CA  . GLU   Z  18  ? 1.8105 1.1751 1.8730 0.0453  0.1497  -0.0994 18  GLU   Z CA  
44297 C  C   . GLU   Z  18  ? 1.7837 1.1473 1.8435 0.0203  0.1155  -0.1295 18  GLU   Z C   
44298 O  O   . GLU   Z  18  ? 1.7387 1.1429 1.8610 0.0180  0.0900  -0.1092 18  GLU   Z O   
44299 C  CB  . GLU   Z  18  ? 1.8475 1.3177 1.8984 0.0325  0.1921  -0.0925 18  GLU   Z CB  
44300 C  CG  . GLU   Z  18  ? 1.8913 1.4266 1.8691 0.0057  0.2150  -0.0929 18  GLU   Z CG  
44301 C  CD  . GLU   Z  18  ? 1.9051 1.5605 1.9327 -0.0510 0.2186  -0.0640 18  GLU   Z CD  
44302 O  OE1 . GLU   Z  18  ? 1.8238 1.6519 1.9891 -0.1118 0.1947  -0.0531 18  GLU   Z OE1 
44303 O  OE2 . GLU   Z  18  ? 1.9564 1.6673 1.8808 -0.0741 0.2317  -0.0868 18  GLU   Z OE2 
44304 N  N   . ASP   Z  19  ? 1.8042 1.0654 1.8509 0.0032  0.1119  -0.0877 19  ASP   Z N   
44305 C  CA  . ASP   Z  19  ? 1.7863 1.1108 1.8017 -0.0015 0.0957  -0.0548 19  ASP   Z CA  
44306 C  C   . ASP   Z  19  ? 1.7560 1.0591 1.8047 0.0212  0.1048  -0.1067 19  ASP   Z C   
44307 O  O   . ASP   Z  19  ? 1.7366 1.0566 1.7407 0.0146  0.1162  -0.1373 19  ASP   Z O   
44308 C  CB  . ASP   Z  19  ? 1.7483 1.2205 1.8459 -0.0299 0.0983  0.0028  19  ASP   Z CB  
44309 C  CG  . ASP   Z  19  ? 1.6581 1.2303 1.8740 -0.0349 0.0902  0.0724  19  ASP   Z CG  
44310 O  OD1 . ASP   Z  19  ? 1.6368 1.2087 1.8777 -0.0518 0.0964  0.1474  19  ASP   Z OD1 
44311 O  OD2 . ASP   Z  19  ? 1.6278 1.4048 1.9273 0.0006  0.1140  0.1310  19  ASP   Z OD2 
44312 N  N   . PHE   Z  20  ? 1.7499 0.9368 1.8198 0.0291  0.0668  0.0022  20  PHE   Z N   
44313 C  CA  . PHE   Z  20  ? 1.7240 0.8564 1.8066 0.0407  0.0408  0.0365  20  PHE   Z CA  
44314 C  C   . PHE   Z  20  ? 1.7003 0.7621 1.7492 -0.0074 0.0172  0.1319  20  PHE   Z C   
44315 O  O   . PHE   Z  20  ? 1.7227 0.7572 1.8421 -0.0552 -0.0202 0.2058  20  PHE   Z O   
44316 C  CB  . PHE   Z  20  ? 1.7561 0.8675 1.8289 0.0669  0.0231  -0.0085 20  PHE   Z CB  
44317 C  CG  . PHE   Z  20  ? 1.8139 0.8558 1.8288 0.1277  0.0470  -0.0249 20  PHE   Z CG  
44318 C  CD1 . PHE   Z  20  ? 1.8567 0.8767 1.8542 0.1376  0.0877  -0.0256 20  PHE   Z CD1 
44319 C  CD2 . PHE   Z  20  ? 1.8697 0.8431 1.8386 0.1229  0.0499  -0.0517 20  PHE   Z CD2 
44320 C  CE1 . PHE   Z  20  ? 1.9096 0.8628 1.8921 0.1176  0.1284  -0.0714 20  PHE   Z CE1 
44321 C  CE2 . PHE   Z  20  ? 1.9038 0.8333 1.8647 0.1196  0.1064  -0.0925 20  PHE   Z CE2 
44322 C  CZ  . PHE   Z  20  ? 1.9226 0.8781 1.8933 0.1193  0.1320  -0.0785 20  PHE   Z CZ  
44323 N  N   . ALA   Z  21  ? 1.6820 0.7223 1.7055 -0.0229 -0.0147 0.1392  21  ALA   Z N   
44324 C  CA  . ALA   Z  21  ? 1.6923 0.6523 1.6404 -0.0168 -0.0446 0.1418  21  ALA   Z CA  
44325 C  C   . ALA   Z  21  ? 1.6888 0.6300 1.6714 0.0045  -0.0512 0.0794  21  ALA   Z C   
44326 O  O   . ALA   Z  21  ? 1.7862 0.6083 1.7260 0.0155  -0.0672 0.0812  21  ALA   Z O   
44327 C  CB  . ALA   Z  21  ? 1.6930 0.6448 1.5794 -0.0040 -0.0527 0.1368  21  ALA   Z CB  
44328 N  N   . VAL   Z  22  ? 1.6257 0.5905 1.6712 0.0235  -0.1015 0.1592  22  VAL   Z N   
44329 C  CA  . VAL   Z  22  ? 1.6061 0.6266 1.6891 0.0636  -0.1019 0.1396  22  VAL   Z CA  
44330 C  C   . VAL   Z  22  ? 1.6033 0.5056 1.6310 0.0672  -0.1388 0.0937  22  VAL   Z C   
44331 O  O   . VAL   Z  22  ? 1.6207 0.4336 1.5823 0.0487  -0.1161 0.0818  22  VAL   Z O   
44332 C  CB  . VAL   Z  22  ? 1.6058 0.6432 1.7473 0.0504  -0.0981 0.1525  22  VAL   Z CB  
44333 C  CG1 . VAL   Z  22  ? 1.6226 0.7525 1.8294 0.0776  -0.0746 0.2038  22  VAL   Z CG1 
44334 C  CG2 . VAL   Z  22  ? 1.6051 0.6751 1.7143 0.0802  -0.0817 0.1547  22  VAL   Z CG2 
44335 N  N   . LEU   Z  23  ? 1.6190 0.5261 1.5831 0.0813  -0.1412 0.0255  23  LEU   Z N   
44336 C  CA  . LEU   Z  23  ? 1.6137 0.5302 1.5708 0.1168  -0.1865 -0.0403 23  LEU   Z CA  
44337 C  C   . LEU   Z  23  ? 1.6310 0.5206 1.6113 0.0790  -0.1941 -0.0751 23  LEU   Z C   
44338 O  O   . LEU   Z  23  ? 1.7620 0.5151 1.6453 0.0906  -0.1927 -0.0550 23  LEU   Z O   
44339 C  CB  . LEU   Z  23  ? 1.5673 0.5768 1.5369 0.0985  -0.2186 -0.0847 23  LEU   Z CB  
44340 C  CG  . LEU   Z  23  ? 1.5793 0.5975 1.5088 0.1469  -0.2260 -0.1235 23  LEU   Z CG  
44341 C  CD1 . LEU   Z  23  ? 1.5559 0.6092 1.4890 0.1316  -0.2431 -0.1432 23  LEU   Z CD1 
44342 C  CD2 . LEU   Z  23  ? 1.5811 0.6027 1.4986 0.1201  -0.2209 -0.1541 23  LEU   Z CD2 
44343 N  N   . ALA   Z  24  ? 1.5717 0.5039 1.6072 0.0064  -0.2080 -0.0985 24  ALA   Z N   
44344 C  CA  . ALA   Z  24  ? 1.5243 0.4752 1.6545 -0.0443 -0.1934 -0.1327 24  ALA   Z CA  
44345 C  C   . ALA   Z  24  ? 1.4936 0.3902 1.5237 -0.1057 -0.2123 -0.1648 24  ALA   Z C   
44346 O  O   . ALA   Z  24  ? 1.4352 0.3315 1.5327 -0.1250 -0.1855 -0.1801 24  ALA   Z O   
44347 C  CB  . ALA   Z  24  ? 1.5414 0.5078 1.7005 -0.0809 -0.1824 -0.1717 24  ALA   Z CB  
44348 N  N   . GLY   Z  25  ? 1.4720 0.4427 1.5178 -0.0859 -0.1899 -0.1444 25  GLY   Z N   
44349 C  CA  . GLY   Z  25  ? 1.4638 0.5404 1.5342 -0.0309 -0.1915 -0.0878 25  GLY   Z CA  
44350 C  C   . GLY   Z  25  ? 1.5190 0.6022 1.5138 0.0149  -0.1787 -0.0815 25  GLY   Z C   
44351 O  O   . GLY   Z  25  ? 1.5858 0.7760 1.5787 0.0782  -0.1631 0.0179  25  GLY   Z O   
44352 N  N   . ASP   Z  26  ? 1.5485 0.5458 1.5831 0.0213  -0.2031 -0.0409 26  ASP   Z N   
44353 C  CA  . ASP   Z  26  ? 1.5926 0.6478 1.6183 -0.0266 -0.2292 -0.0842 26  ASP   Z CA  
44354 C  C   . ASP   Z  26  ? 1.5432 0.5902 1.5955 -0.0121 -0.2688 -0.0946 26  ASP   Z C   
44355 O  O   . ASP   Z  26  ? 1.4184 0.7112 1.6380 -0.0136 -0.2938 -0.0510 26  ASP   Z O   
44356 C  CB  . ASP   Z  26  ? 1.6785 0.6681 1.7142 -0.0246 -0.2132 -0.1937 26  ASP   Z CB  
44357 C  CG  . ASP   Z  26  ? 1.6906 0.7847 1.7296 -0.1033 -0.2485 -0.2600 26  ASP   Z CG  
44358 O  OD1 . ASP   Z  26  ? 1.7800 0.9158 1.7006 -0.1582 -0.2609 -0.2971 26  ASP   Z OD1 
44359 O  OD2 . ASP   Z  26  ? 1.8374 0.5838 1.7553 -0.1812 -0.3156 -0.3214 26  ASP   Z OD2 
44360 N  N   . THR   Z  27  ? 1.5673 0.5835 1.5736 -0.0348 -0.2492 -0.0852 27  THR   Z N   
44361 C  CA  . THR   Z  27  ? 1.5409 0.5946 1.5287 -0.0178 -0.2723 -0.0876 27  THR   Z CA  
44362 C  C   . THR   Z  27  ? 1.5445 0.6078 1.5127 -0.0193 -0.2848 -0.1077 27  THR   Z C   
44363 O  O   . THR   Z  27  ? 1.5308 0.6369 1.5236 -0.0338 -0.2900 -0.0967 27  THR   Z O   
44364 C  CB  . THR   Z  27  ? 1.5365 0.5520 1.5360 -0.0392 -0.2830 -0.0881 27  THR   Z CB  
44365 O  OG1 . THR   Z  27  ? 1.5107 0.5063 1.6148 -0.0789 -0.2750 -0.0293 27  THR   Z OG1 
44366 C  CG2 . THR   Z  27  ? 1.5320 0.6224 1.5372 -0.0223 -0.2654 -0.0674 27  THR   Z CG2 
44367 N  N   . ARG   Z  28  ? 1.5587 0.6426 1.4873 0.0155  -0.3130 -0.1032 28  ARG   Z N   
44368 C  CA  . ARG   Z  28  ? 1.5836 0.7273 1.4529 0.0134  -0.3271 -0.1555 28  ARG   Z CA  
44369 C  C   . ARG   Z  28  ? 1.6110 0.6241 1.3952 -0.0162 -0.2981 -0.1723 28  ARG   Z C   
44370 O  O   . ARG   Z  28  ? 1.6138 0.6773 1.4415 -0.1434 -0.3404 -0.2238 28  ARG   Z O   
44371 C  CB  . ARG   Z  28  ? 1.6809 0.7358 1.5072 0.0341  -0.3102 -0.1432 28  ARG   Z CB  
44372 C  CG  . ARG   Z  28  ? 1.6985 0.8905 1.4929 0.0674  -0.3064 -0.1640 28  ARG   Z CG  
44373 C  CD  . ARG   Z  28  ? 1.7015 0.8748 1.4911 0.0802  -0.3299 -0.2156 28  ARG   Z CD  
44374 N  NE  . ARG   Z  28  ? 1.7386 0.8989 1.4572 0.1100  -0.3361 -0.2522 28  ARG   Z NE  
44375 C  CZ  . ARG   Z  28  ? 1.7406 0.9394 1.5008 0.0555  -0.3573 -0.2635 28  ARG   Z CZ  
44376 N  NH1 . ARG   Z  28  ? 1.7403 1.0713 1.4892 0.0605  -0.3930 -0.2352 28  ARG   Z NH1 
44377 N  NH2 . ARG   Z  28  ? 1.7287 1.1422 1.5434 0.0847  -0.3812 -0.1947 28  ARG   Z NH2 
44378 N  N   . ASN   Z  29  ? 1.5420 0.5604 1.3448 0.0094  -0.3277 -0.2088 29  ASN   Z N   
44379 C  CA  . ASN   Z  29  ? 1.5244 0.5761 1.2935 0.0311  -0.3290 -0.1999 29  ASN   Z CA  
44380 C  C   . ASN   Z  29  ? 1.5111 0.5790 1.3118 0.0283  -0.3514 -0.2185 29  ASN   Z C   
44381 O  O   . ASN   Z  29  ? 1.5708 0.6075 1.3302 -0.0003 -0.3771 -0.2367 29  ASN   Z O   
44382 C  CB  . ASN   Z  29  ? 1.5267 0.5816 1.2563 0.0923  -0.3272 -0.1866 29  ASN   Z CB  
44383 C  CG  . ASN   Z  29  ? 1.5337 0.5034 1.2308 0.1056  -0.3050 -0.1795 29  ASN   Z CG  
44384 O  OD1 . ASN   Z  29  ? 1.6279 0.4654 1.1844 0.1804  -0.3106 -0.2090 29  ASN   Z OD1 
44385 N  ND2 . ASN   Z  29  ? 1.5822 0.4421 1.2504 0.0942  -0.2969 -0.1482 29  ASN   Z ND2 
44386 N  N   . ILE   Z  30  ? 1.5299 0.6134 1.3299 0.0172  -0.3712 -0.1661 30  ILE   Z N   
44387 C  CA  . ILE   Z  30  ? 1.5617 0.6525 1.3401 0.0641  -0.3559 -0.1406 30  ILE   Z CA  
44388 C  C   . ILE   Z  30  ? 1.5327 0.6829 1.3253 0.1105  -0.2771 -0.0739 30  ILE   Z C   
44389 O  O   . ILE   Z  30  ? 1.5964 0.5857 1.3295 0.1224  -0.2444 -0.0400 30  ILE   Z O   
44390 C  CB  . ILE   Z  30  ? 1.5756 0.6437 1.3952 0.0445  -0.3518 -0.1465 30  ILE   Z CB  
44391 C  CG1 . ILE   Z  30  ? 1.6224 0.6566 1.3745 0.0213  -0.3343 -0.1644 30  ILE   Z CG1 
44392 C  CG2 . ILE   Z  30  ? 1.5553 0.6592 1.4465 0.0690  -0.3236 -0.1197 30  ILE   Z CG2 
44393 C  CD1 . ILE   Z  30  ? 1.6475 0.6692 1.3635 0.0466  -0.3292 -0.1382 30  ILE   Z CD1 
44394 N  N   . THR   Z  31  ? 1.5622 0.7974 1.2461 0.0974  -0.2715 -0.0997 31  THR   Z N   
44395 C  CA  . THR   Z  31  ? 1.5655 0.9055 1.2888 0.1184  -0.2496 -0.1101 31  THR   Z CA  
44396 C  C   . THR   Z  31  ? 1.5823 0.8841 1.3598 0.1228  -0.2646 -0.0854 31  THR   Z C   
44397 O  O   . THR   Z  31  ? 1.5559 0.8792 1.4202 0.0831  -0.2935 -0.1145 31  THR   Z O   
44398 C  CB  . THR   Z  31  ? 1.5585 1.0374 1.2088 0.0960  -0.2301 -0.1013 31  THR   Z CB  
44399 O  OG1 . THR   Z  31  ? 1.6551 1.2288 1.1875 0.0860  -0.2206 -0.1560 31  THR   Z OG1 
44400 C  CG2 . THR   Z  31  ? 1.5273 1.0624 1.2778 0.1263  -0.1908 -0.1259 31  THR   Z CG2 
44401 N  N   . ASP   Z  32  ? 1.6063 0.7436 1.4397 0.1236  -0.2338 -0.0491 32  ASP   Z N   
44402 C  CA  . ASP   Z  32  ? 1.6136 0.7312 1.4562 0.1157  -0.2368 -0.0362 32  ASP   Z CA  
44403 C  C   . ASP   Z  32  ? 1.6654 0.6835 1.4491 0.1048  -0.2807 -0.0636 32  ASP   Z C   
44404 O  O   . ASP   Z  32  ? 1.5996 0.5109 1.4480 0.0942  -0.3178 -0.1014 32  ASP   Z O   
44405 C  CB  . ASP   Z  32  ? 1.6443 0.7416 1.4927 0.1857  -0.2074 -0.0025 32  ASP   Z CB  
44406 C  CG  . ASP   Z  32  ? 1.6152 0.7163 1.5537 0.2068  -0.1793 0.0440  32  ASP   Z CG  
44407 O  OD1 . ASP   Z  32  ? 1.6656 0.8267 1.5322 0.2767  -0.1382 0.0206  32  ASP   Z OD1 
44408 O  OD2 . ASP   Z  32  ? 1.6826 0.6704 1.5871 0.2821  -0.1867 0.1488  32  ASP   Z OD2 
44409 N  N   . TYR   Z  33  ? 1.6930 0.7472 1.4433 0.1080  -0.3078 -0.0714 33  TYR   Z N   
44410 C  CA  . TYR   Z  33  ? 1.6934 0.7980 1.4388 0.1048  -0.3336 -0.1004 33  TYR   Z CA  
44411 C  C   . TYR   Z  33  ? 1.6862 0.7674 1.3905 0.1185  -0.3122 -0.1315 33  TYR   Z C   
44412 O  O   . TYR   Z  33  ? 1.6613 0.7877 1.4335 0.0876  -0.3107 -0.1038 33  TYR   Z O   
44413 C  CB  . TYR   Z  33  ? 1.7449 0.7659 1.5043 0.0804  -0.3675 -0.1213 33  TYR   Z CB  
44414 C  CG  . TYR   Z  33  ? 1.7601 0.7324 1.5996 0.0575  -0.4070 -0.0865 33  TYR   Z CG  
44415 C  CD1 . TYR   Z  33  ? 1.7265 0.7578 1.6642 0.0177  -0.4240 -0.1009 33  TYR   Z CD1 
44416 C  CD2 . TYR   Z  33  ? 1.7588 0.7812 1.6689 0.0737  -0.4091 -0.0569 33  TYR   Z CD2 
44417 C  CE1 . TYR   Z  33  ? 1.7625 0.8274 1.6682 -0.0105 -0.4306 -0.0594 33  TYR   Z CE1 
44418 C  CE2 . TYR   Z  33  ? 1.7539 0.8686 1.6606 0.0427  -0.4260 -0.0295 33  TYR   Z CE2 
44419 C  CZ  . TYR   Z  33  ? 1.7651 0.9059 1.6983 -0.0177 -0.4315 -0.0528 33  TYR   Z CZ  
44420 O  OH  . TYR   Z  33  ? 1.7998 0.9866 1.6702 -0.0745 -0.4734 -0.0335 33  TYR   Z OH  
44421 N  N   . SER   Z  34  ? 1.6560 0.7484 1.3240 0.1311  -0.2980 -0.2013 34  SER   Z N   
44422 C  CA  . SER   Z  34  ? 1.6473 0.6851 1.3234 0.1194  -0.2961 -0.2162 34  SER   Z CA  
44423 C  C   . SER   Z  34  ? 1.6130 0.5887 1.3607 0.1372  -0.3295 -0.1562 34  SER   Z C   
44424 O  O   . SER   Z  34  ? 1.6344 0.5437 1.3075 0.1694  -0.3520 -0.0673 34  SER   Z O   
44425 C  CB  . SER   Z  34  ? 1.6596 0.6918 1.3602 0.0944  -0.2944 -0.2049 34  SER   Z CB  
44426 O  OG  . SER   Z  34  ? 1.6493 0.8165 1.3787 0.0696  -0.2514 -0.2364 34  SER   Z OG  
44427 N  N   . ILE   Z  35  ? 1.6147 0.5732 1.3355 0.1173  -0.3413 -0.1835 35  ILE   Z N   
44428 C  CA  . ILE   Z  35  ? 1.5642 0.5930 1.3213 0.1028  -0.3388 -0.1710 35  ILE   Z CA  
44429 C  C   . ILE   Z  35  ? 1.6228 0.6227 1.2427 0.1681  -0.3419 -0.1413 35  ILE   Z C   
44430 O  O   . ILE   Z  35  ? 1.6380 0.4428 1.2279 0.1473  -0.3972 -0.0676 35  ILE   Z O   
44431 C  CB  . ILE   Z  35  ? 1.5484 0.6873 1.3530 0.1072  -0.3778 -0.2287 35  ILE   Z CB  
44432 C  CG1 . ILE   Z  35  ? 1.5398 0.7067 1.4112 0.0930  -0.3616 -0.2110 35  ILE   Z CG1 
44433 C  CG2 . ILE   Z  35  ? 1.4762 0.6703 1.3296 0.0911  -0.4165 -0.2038 35  ILE   Z CG2 
44434 C  CD1 . ILE   Z  35  ? 1.5124 0.8383 1.4439 0.0869  -0.3731 -0.2214 35  ILE   Z CD1 
44435 N  N   . ASN   Z  36  ? 1.6336 0.5359 1.3084 0.2003  -0.2984 -0.1098 36  ASN   Z N   
44436 C  CA  . ASN   Z  36  ? 1.6349 0.5234 1.3451 0.2011  -0.2734 -0.1224 36  ASN   Z CA  
44437 C  C   . ASN   Z  36  ? 1.5862 0.4330 1.3576 0.1534  -0.2367 -0.1621 36  ASN   Z C   
44438 O  O   . ASN   Z  36  ? 1.6190 0.3565 1.4564 0.1425  -0.2958 -0.1328 36  ASN   Z O   
44439 C  CB  . ASN   Z  36  ? 1.6133 0.5676 1.3472 0.2280  -0.2968 -0.1260 36  ASN   Z CB  
44440 C  CG  . ASN   Z  36  ? 1.6625 0.5572 1.3261 0.3080  -0.2560 -0.1112 36  ASN   Z CG  
44441 O  OD1 . ASN   Z  36  ? 1.6378 0.4345 1.4106 0.3674  -0.2632 -0.0834 36  ASN   Z OD1 
44442 N  ND2 . ASN   Z  36  ? 1.7021 0.6505 1.2989 0.3332  -0.2703 -0.0560 36  ASN   Z ND2 
44443 N  N   . SER   Z  37  ? 1.5396 0.4260 1.3978 0.1457  -0.2182 -0.1888 37  SER   Z N   
44444 C  CA  . SER   Z  37  ? 1.5121 0.5220 1.3670 0.1404  -0.1770 -0.1555 37  SER   Z CA  
44445 C  C   . SER   Z  37  ? 1.4923 0.4903 1.3790 0.1230  -0.1671 -0.2018 37  SER   Z C   
44446 O  O   . SER   Z  37  ? 1.5075 0.4179 1.3891 0.1104  -0.1148 -0.1553 37  SER   Z O   
44447 C  CB  . SER   Z  37  ? 1.4994 0.5072 1.3662 0.1681  -0.1872 -0.1303 37  SER   Z CB  
44448 O  OG  . SER   Z  37  ? 1.5058 0.5778 1.3730 0.1847  -0.2038 -0.0759 37  SER   Z OG  
44449 N  N   . ARG   Z  38  ? 1.4821 0.5555 1.3026 0.1256  -0.1616 -0.2020 38  ARG   Z N   
44450 C  CA  . ARG   Z  38  ? 1.4631 0.6416 1.3158 0.1078  -0.1862 -0.1606 38  ARG   Z CA  
44451 C  C   . ARG   Z  38  ? 1.4367 0.6528 1.3372 0.1124  -0.1961 -0.1664 38  ARG   Z C   
44452 O  O   . ARG   Z  38  ? 1.4544 0.4719 1.4108 0.0740  -0.1715 -0.1658 38  ARG   Z O   
44453 C  CB  . ARG   Z  38  ? 1.4621 0.7171 1.2741 0.1099  -0.1792 -0.1670 38  ARG   Z CB  
44454 C  CG  . ARG   Z  38  ? 1.4913 0.7382 1.2517 0.1168  -0.1737 -0.1713 38  ARG   Z CG  
44455 C  CD  . ARG   Z  38  ? 1.5044 0.7952 1.2665 0.1038  -0.1907 -0.1887 38  ARG   Z CD  
44456 N  NE  . ARG   Z  38  ? 1.5510 0.8743 1.2514 0.1014  -0.1773 -0.2308 38  ARG   Z NE  
44457 C  CZ  . ARG   Z  38  ? 1.5429 0.8585 1.2396 0.0928  -0.1374 -0.2323 38  ARG   Z CZ  
44458 N  NH1 . ARG   Z  38  ? 1.5229 0.8120 1.2512 0.0799  -0.1162 -0.2207 38  ARG   Z NH1 
44459 N  NH2 . ARG   Z  38  ? 1.5496 0.8662 1.2943 0.1146  -0.1141 -0.2359 38  ARG   Z NH2 
44460 N  N   . TYR   Z  39  ? 1.4255 0.6936 1.3413 0.0928  -0.2512 -0.1075 39  TYR   Z N   
44461 C  CA  . TYR   Z  39  ? 1.3842 0.7599 1.3648 0.0987  -0.2362 -0.1372 39  TYR   Z CA  
44462 C  C   . TYR   Z  39  ? 1.3951 0.7478 1.3943 0.0921  -0.2213 -0.0814 39  TYR   Z C   
44463 O  O   . TYR   Z  39  ? 1.3230 0.7872 1.4159 0.1818  -0.2365 -0.0490 39  TYR   Z O   
44464 C  CB  . TYR   Z  39  ? 1.3932 0.8163 1.3837 0.1130  -0.2482 -0.1337 39  TYR   Z CB  
44465 C  CG  . TYR   Z  39  ? 1.4338 0.7973 1.4260 0.1175  -0.2224 -0.1250 39  TYR   Z CG  
44466 C  CD1 . TYR   Z  39  ? 1.4660 0.8343 1.4383 0.1424  -0.2015 -0.1181 39  TYR   Z CD1 
44467 C  CD2 . TYR   Z  39  ? 1.4572 0.8023 1.4249 0.1124  -0.1793 -0.1141 39  TYR   Z CD2 
44468 C  CE1 . TYR   Z  39  ? 1.4823 0.8172 1.4996 0.1661  -0.1702 -0.1005 39  TYR   Z CE1 
44469 C  CE2 . TYR   Z  39  ? 1.4706 0.8212 1.4939 0.1664  -0.1522 -0.0980 39  TYR   Z CE2 
44470 C  CZ  . TYR   Z  39  ? 1.4839 0.8281 1.5115 0.1769  -0.1434 -0.0816 39  TYR   Z CZ  
44471 O  OH  . TYR   Z  39  ? 1.5237 0.9630 1.5561 0.2822  -0.0815 -0.0651 39  TYR   Z OH  
44472 N  N   . GLU   Z  40  ? 1.4027 0.7315 1.4363 0.0333  -0.2486 -0.1470 40  GLU   Z N   
44473 C  CA  . GLU   Z  40  ? 1.4369 0.7037 1.4481 0.0588  -0.2554 -0.2010 40  GLU   Z CA  
44474 C  C   . GLU   Z  40  ? 1.4243 0.6456 1.4656 0.0503  -0.2555 -0.2406 40  GLU   Z C   
44475 O  O   . GLU   Z  40  ? 1.4058 0.5985 1.4943 0.0485  -0.2897 -0.2732 40  GLU   Z O   
44476 C  CB  . GLU   Z  40  ? 1.4142 0.6484 1.4268 0.0294  -0.2946 -0.2220 40  GLU   Z CB  
44477 C  CG  . GLU   Z  40  ? 1.4106 0.6337 1.4441 0.0442  -0.3086 -0.2248 40  GLU   Z CG  
44478 C  CD  . GLU   Z  40  ? 1.4361 0.5897 1.5048 0.0510  -0.3202 -0.2326 40  GLU   Z CD  
44479 O  OE1 . GLU   Z  40  ? 1.4434 0.4070 1.5430 0.0533  -0.3299 -0.3183 40  GLU   Z OE1 
44480 O  OE2 . GLU   Z  40  ? 1.4051 0.5608 1.5611 0.0408  -0.3465 -0.1933 40  GLU   Z OE2 
44481 N  N   . PRO   Z  41  ? 1.4295 0.6577 1.5404 0.0710  -0.2427 -0.2181 41  PRO   Z N   
44482 C  CA  . PRO   Z  41  ? 1.4399 0.5956 1.5594 0.0569  -0.2205 -0.2392 41  PRO   Z CA  
44483 C  C   . PRO   Z  41  ? 1.5146 0.4808 1.5423 0.0317  -0.2242 -0.2866 41  PRO   Z C   
44484 O  O   . PRO   Z  41  ? 1.5440 0.4311 1.5316 -0.0240 -0.2055 -0.4132 41  PRO   Z O   
44485 C  CB  . PRO   Z  41  ? 1.4058 0.6296 1.5748 0.0610  -0.2181 -0.2533 41  PRO   Z CB  
44486 C  CG  . PRO   Z  41  ? 1.4134 0.6977 1.5794 0.0590  -0.2236 -0.2228 41  PRO   Z CG  
44487 C  CD  . PRO   Z  41  ? 1.4083 0.7050 1.5480 0.0810  -0.2402 -0.1990 41  PRO   Z CD  
44488 N  N   . LYS   Z  42  ? 1.5354 0.5035 1.5694 0.0383  -0.2057 -0.2457 42  LYS   Z N   
44489 C  CA  . LYS   Z  42  ? 1.4890 0.5400 1.5808 0.0624  -0.1932 -0.2408 42  LYS   Z CA  
44490 C  C   . LYS   Z  42  ? 1.4403 0.4920 1.6032 0.0907  -0.1745 -0.2390 42  LYS   Z C   
44491 O  O   . LYS   Z  42  ? 1.4684 0.3942 1.5231 0.1471  -0.1376 -0.2805 42  LYS   Z O   
44492 C  CB  . LYS   Z  42  ? 1.4799 0.6229 1.6555 0.1021  -0.1941 -0.2436 42  LYS   Z CB  
44493 C  CG  . LYS   Z  42  ? 1.5285 0.6610 1.7034 0.0435  -0.1844 -0.2410 42  LYS   Z CG  
44494 C  CD  . LYS   Z  42  ? 1.5455 0.6502 1.7510 0.0418  -0.2016 -0.2473 42  LYS   Z CD  
44495 C  CE  . LYS   Z  42  ? 1.5816 0.7530 1.7868 -0.0336 -0.1850 -0.2028 42  LYS   Z CE  
44496 N  NZ  . LYS   Z  42  ? 1.6099 0.7767 1.7873 -0.0643 -0.1830 -0.2244 42  LYS   Z NZ  
44497 N  N   . VAL   Z  43  ? 1.4237 0.5421 1.5933 0.0619  -0.1518 -0.2184 43  VAL   Z N   
44498 C  CA  . VAL   Z  43  ? 1.3894 0.7377 1.5563 0.0463  -0.1532 -0.2170 43  VAL   Z CA  
44499 C  C   . VAL   Z  43  ? 1.4230 0.7521 1.5299 0.0376  -0.1951 -0.2037 43  VAL   Z C   
44500 O  O   . VAL   Z  43  ? 1.4111 0.9540 1.5795 -0.0588 -0.2319 -0.2337 43  VAL   Z O   
44501 C  CB  . VAL   Z  43  ? 1.3673 0.8135 1.6148 0.0447  -0.1308 -0.2100 43  VAL   Z CB  
44502 C  CG1 . VAL   Z  43  ? 1.3963 0.8909 1.6072 0.0141  -0.1220 -0.2274 43  VAL   Z CG1 
44503 C  CG2 . VAL   Z  43  ? 1.3372 0.8635 1.6262 0.1177  -0.1351 -0.1924 43  VAL   Z CG2 
44504 N  N   . PHE   Z  44  ? 1.4694 0.7449 1.4644 0.0924  -0.2019 -0.2046 44  PHE   Z N   
44505 C  CA  . PHE   Z  44  ? 1.4932 0.7680 1.4481 0.0921  -0.2107 -0.1634 44  PHE   Z CA  
44506 C  C   . PHE   Z  44  ? 1.4945 0.7289 1.4900 0.0864  -0.2147 -0.1863 44  PHE   Z C   
44507 O  O   . PHE   Z  44  ? 1.4977 0.6236 1.4581 0.0346  -0.2028 -0.2633 44  PHE   Z O   
44508 C  CB  . PHE   Z  44  ? 1.4948 0.7207 1.3383 0.1202  -0.2126 -0.1303 44  PHE   Z CB  
44509 C  CG  . PHE   Z  44  ? 1.5164 0.6824 1.2901 0.1632  -0.2282 -0.0824 44  PHE   Z CG  
44510 C  CD1 . PHE   Z  44  ? 1.5602 0.6467 1.2856 0.1946  -0.2124 -0.0431 44  PHE   Z CD1 
44511 C  CD2 . PHE   Z  44  ? 1.4926 0.7276 1.2732 0.1618  -0.2409 -0.0874 44  PHE   Z CD2 
44512 C  CE1 . PHE   Z  44  ? 1.5713 0.6604 1.2149 0.1854  -0.2349 -0.0150 44  PHE   Z CE1 
44513 C  CE2 . PHE   Z  44  ? 1.5048 0.7257 1.2357 0.1602  -0.2593 -0.0775 44  PHE   Z CE2 
44514 C  CZ  . PHE   Z  44  ? 1.5309 0.6827 1.2396 0.1695  -0.2531 -0.0378 44  PHE   Z CZ  
44515 N  N   . ASP   Z  45  ? 1.4993 0.7662 1.5342 0.0942  -0.2238 -0.1449 45  ASP   Z N   
44516 C  CA  . ASP   Z  45  ? 1.4821 0.7924 1.5416 0.1361  -0.1962 -0.1052 45  ASP   Z CA  
44517 C  C   . ASP   Z  45  ? 1.5491 0.7486 1.5365 0.1251  -0.1924 -0.0501 45  ASP   Z C   
44518 O  O   . ASP   Z  45  ? 1.5550 0.7587 1.5505 0.0289  -0.1981 -0.0483 45  ASP   Z O   
44519 C  CB  . ASP   Z  45  ? 1.4750 0.8922 1.5949 0.1418  -0.1954 -0.0605 45  ASP   Z CB  
44520 C  CG  . ASP   Z  45  ? 1.4394 0.9447 1.6438 0.2156  -0.1751 -0.0185 45  ASP   Z CG  
44521 O  OD1 . ASP   Z  45  ? 1.4144 1.0240 1.6583 0.2081  -0.2098 0.0060  45  ASP   Z OD1 
44522 O  OD2 . ASP   Z  45  ? 1.4386 1.0288 1.6668 0.2441  -0.1526 0.0328  45  ASP   Z OD2 
44523 N  N   . CYS   Z  46  ? 1.5674 0.6562 1.5698 0.1402  -0.2086 -0.0763 46  CYS   Z N   
44524 C  CA  . CYS   Z  46  ? 1.5710 0.6785 1.6246 0.1372  -0.1783 -0.0959 46  CYS   Z CA  
44525 C  C   . CYS   Z  46  ? 1.6251 0.6344 1.6538 0.1627  -0.2015 -0.0570 46  CYS   Z C   
44526 O  O   . CYS   Z  46  ? 1.6902 0.3715 1.6644 0.2452  -0.2049 -0.0266 46  CYS   Z O   
44527 C  CB  . CYS   Z  46  ? 1.5636 0.7833 1.6516 0.1277  -0.1919 -0.0846 46  CYS   Z CB  
44528 S  SG  . CYS   Z  46  ? 1.5561 0.8134 1.6522 0.0313  -0.1497 -0.1929 46  CYS   Z SG  
44529 N  N   . GLY   Z  47  ? 1.6572 0.5630 1.6446 0.2857  -0.1473 -0.0577 47  GLY   Z N   
44530 C  CA  . GLY   Z  47  ? 1.7106 0.5375 1.6814 0.3031  -0.1388 -0.0434 47  GLY   Z CA  
44531 C  C   . GLY   Z  47  ? 1.7554 0.5507 1.6827 0.3193  -0.1276 -0.0512 47  GLY   Z C   
44532 O  O   . GLY   Z  47  ? 1.7286 0.5559 1.6226 0.3690  -0.1364 -0.1415 47  GLY   Z O   
44533 N  N   . ASP   Z  48  ? 1.7325 0.6828 1.6612 0.3003  -0.0838 -0.0868 48  ASP   Z N   
44534 C  CA  . ASP   Z  48  ? 1.7638 0.6728 1.6681 0.2683  -0.0577 -0.0526 48  ASP   Z CA  
44535 C  C   . ASP   Z  48  ? 1.6869 0.6323 1.7083 0.3175  -0.0393 -0.0667 48  ASP   Z C   
44536 O  O   . ASP   Z  48  ? 1.6696 0.5698 1.7032 0.3212  -0.0474 -0.1041 48  ASP   Z O   
44537 C  CB  . ASP   Z  48  ? 1.8136 0.7337 1.6593 0.2335  -0.0704 -0.0452 48  ASP   Z CB  
44538 C  CG  . ASP   Z  48  ? 1.8584 0.7523 1.6504 0.2237  -0.0879 0.0270  48  ASP   Z CG  
44539 O  OD1 . ASP   Z  48  ? 1.8962 0.5089 1.7728 0.2901  -0.0423 0.0629  48  ASP   Z OD1 
44540 O  OD2 . ASP   Z  48  ? 1.8834 0.8051 1.6774 0.1238  -0.0520 0.0126  48  ASP   Z OD2 
44541 N  N   . ASN   Z  49  ? 1.5948 0.6041 1.7366 0.3426  -0.0306 -0.0479 49  ASN   Z N   
44542 C  CA  . ASN   Z  49  ? 1.6066 0.6154 1.7929 0.3214  -0.0082 -0.0607 49  ASN   Z CA  
44543 C  C   . ASN   Z  49  ? 1.6137 0.5330 1.7308 0.2859  0.0077  -0.0436 49  ASN   Z C   
44544 O  O   . ASN   Z  49  ? 1.7196 0.4516 1.8379 0.2031  0.0447  -0.0277 49  ASN   Z O   
44545 C  CB  . ASN   Z  49  ? 1.5651 0.6335 1.8692 0.3643  0.0045  -0.0645 49  ASN   Z CB  
44546 C  CG  . ASN   Z  49  ? 1.5762 0.6385 1.9453 0.3177  -0.0179 -0.0844 49  ASN   Z CG  
44547 O  OD1 . ASN   Z  49  ? 1.6345 0.5631 1.9561 0.2561  -0.0428 -0.1161 49  ASN   Z OD1 
44548 N  ND2 . ASN   Z  49  ? 1.6167 0.6546 1.9651 0.2915  -0.0094 -0.0570 49  ASN   Z ND2 
44549 N  N   . ILE   Z  50  ? 1.5918 0.6137 1.6539 0.2596  -0.0266 -0.0769 50  ILE   Z N   
44550 C  CA  . ILE   Z  50  ? 1.5600 0.6913 1.5869 0.2705  -0.0423 -0.1081 50  ILE   Z CA  
44551 C  C   . ILE   Z  50  ? 1.5491 0.6780 1.5711 0.2098  -0.0683 -0.1046 50  ILE   Z C   
44552 O  O   . ILE   Z  50  ? 1.5548 0.6475 1.5559 0.1932  -0.0943 -0.1221 50  ILE   Z O   
44553 C  CB  . ILE   Z  50  ? 1.5744 0.7495 1.5607 0.2772  -0.0706 -0.1189 50  ILE   Z CB  
44554 C  CG1 . ILE   Z  50  ? 1.5911 0.7648 1.5549 0.3008  -0.0416 -0.1133 50  ILE   Z CG1 
44555 C  CG2 . ILE   Z  50  ? 1.5788 0.8115 1.5575 0.3076  -0.0871 -0.1286 50  ILE   Z CG2 
44556 C  CD1 . ILE   Z  50  ? 1.5746 0.7751 1.5237 0.3001  -0.0548 -0.1048 50  ILE   Z CD1 
44557 N  N   . VAL   Z  51  ? 1.5211 0.6734 1.5294 0.2228  -0.0706 -0.0759 51  VAL   Z N   
44558 C  CA  . VAL   Z  51  ? 1.4570 0.5482 1.5385 0.2273  -0.1050 -0.0473 51  VAL   Z CA  
44559 C  C   . VAL   Z  51  ? 1.4457 0.5049 1.5081 0.2341  -0.0686 -0.0605 51  VAL   Z C   
44560 O  O   . VAL   Z  51  ? 1.4242 0.4721 1.4872 0.2668  -0.0213 -0.0999 51  VAL   Z O   
44561 C  CB  . VAL   Z  51  ? 1.4795 0.5969 1.5449 0.2049  -0.1221 -0.0571 51  VAL   Z CB  
44562 C  CG1 . VAL   Z  51  ? 1.4910 0.5642 1.5922 0.2188  -0.1246 -0.0611 51  VAL   Z CG1 
44563 C  CG2 . VAL   Z  51  ? 1.5065 0.6660 1.5193 0.2198  -0.1199 -0.0496 51  VAL   Z CG2 
44564 N  N   . MET   Z  52  ? 1.4006 0.5213 1.4649 0.2455  -0.1012 -0.0245 52  MET   Z N   
44565 C  CA  . MET   Z  52  ? 1.3886 0.5521 1.4616 0.2356  -0.0931 -0.0530 52  MET   Z CA  
44566 C  C   . MET   Z  52  ? 1.3801 0.5998 1.4038 0.1908  -0.1373 -0.0775 52  MET   Z C   
44567 O  O   . MET   Z  52  ? 1.3512 0.5430 1.4229 0.1857  -0.1664 -0.1036 52  MET   Z O   
44568 C  CB  . MET   Z  52  ? 1.3937 0.4964 1.5287 0.2667  -0.0803 -0.0551 52  MET   Z CB  
44569 C  CG  . MET   Z  52  ? 1.3999 0.5418 1.5930 0.2888  -0.0485 -0.0578 52  MET   Z CG  
44570 S  SD  . MET   Z  52  ? 1.4054 0.5269 1.7432 0.3045  0.0011  -0.0467 52  MET   Z SD  
44571 C  CE  . MET   Z  52  ? 1.3844 0.5397 1.7433 0.2739  0.0061  -0.0500 52  MET   Z CE  
44572 N  N   . SER   Z  53  ? 1.3971 0.5336 1.3721 0.1660  -0.1449 -0.1226 53  SER   Z N   
44573 C  CA  . SER   Z  53  ? 1.4303 0.5370 1.3452 0.1269  -0.1420 -0.1412 53  SER   Z CA  
44574 C  C   . SER   Z  53  ? 1.4183 0.5140 1.3489 0.1356  -0.1100 -0.1437 53  SER   Z C   
44575 O  O   . SER   Z  53  ? 1.4513 0.4379 1.3611 0.1510  -0.0903 -0.1357 53  SER   Z O   
44576 C  CB  . SER   Z  53  ? 1.4210 0.5635 1.3569 0.1128  -0.1351 -0.1584 53  SER   Z CB  
44577 O  OG  . SER   Z  53  ? 1.4264 0.6400 1.3506 0.0939  -0.1267 -0.1847 53  SER   Z OG  
44578 N  N   . ALA   Z  54  ? 1.4775 0.5671 1.2627 0.1249  -0.1204 -0.1155 54  ALA   Z N   
44579 C  CA  . ALA   Z  54  ? 1.5071 0.6955 1.2559 0.1255  -0.1776 -0.0663 54  ALA   Z CA  
44580 C  C   . ALA   Z  54  ? 1.5551 0.7335 1.1652 0.1061  -0.2098 -0.0619 54  ALA   Z C   
44581 O  O   . ALA   Z  54  ? 1.6398 0.7692 1.1609 0.0924  -0.2640 0.0041  54  ALA   Z O   
44582 C  CB  . ALA   Z  54  ? 1.5565 0.6668 1.2432 0.1144  -0.1938 -0.1201 54  ALA   Z CB  
44583 N  N   . ASN   Z  55  ? 1.5237 0.7645 1.1817 0.0982  -0.2290 -0.0229 55  ASN   Z N   
44584 C  CA  . ASN   Z  55  ? 1.4975 0.8200 1.1607 0.1401  -0.2521 -0.0436 55  ASN   Z CA  
44585 C  C   . ASN   Z  55  ? 1.4892 0.8219 1.1326 0.1407  -0.2590 -0.0368 55  ASN   Z C   
44586 O  O   . ASN   Z  55  ? 1.5021 0.9357 1.1382 0.1606  -0.2673 -0.0461 55  ASN   Z O   
44587 C  CB  . ASN   Z  55  ? 1.5325 0.9339 1.2218 0.1190  -0.2092 0.0336  55  ASN   Z CB  
44588 C  CG  . ASN   Z  55  ? 1.5974 0.9399 1.2257 0.1501  -0.2097 0.0357  55  ASN   Z CG  
44589 O  OD1 . ASN   Z  55  ? 1.5807 0.9915 1.2947 0.1991  -0.1606 0.1253  55  ASN   Z OD1 
44590 N  ND2 . ASN   Z  55  ? 1.6658 1.0749 1.2262 0.1425  -0.2109 0.0582  55  ASN   Z ND2 
44591 N  N   . GLY   Z  56  ? 1.4421 0.7549 1.1252 0.1746  -0.2752 -0.0155 56  GLY   Z N   
44592 C  CA  . GLY   Z  56  ? 1.4360 0.7825 1.1073 0.1628  -0.2486 -0.0464 56  GLY   Z CA  
44593 C  C   . GLY   Z  56  ? 1.4309 0.7169 1.1037 0.1385  -0.2586 -0.0565 56  GLY   Z C   
44594 O  O   . GLY   Z  56  ? 1.5000 0.8999 1.0957 0.1169  -0.2691 -0.0941 56  GLY   Z O   
44595 N  N   . PHE   Z  57  ? 1.4468 0.6447 1.0907 0.1592  -0.2488 -0.1061 57  PHE   Z N   
44596 C  CA  . PHE   Z  57  ? 1.4295 0.6298 1.0930 0.1492  -0.2403 -0.1276 57  PHE   Z CA  
44597 C  C   . PHE   Z  57  ? 1.4460 0.6321 1.1081 0.1295  -0.2627 -0.0860 57  PHE   Z C   
44598 O  O   . PHE   Z  57  ? 1.4873 0.6218 1.0740 0.1824  -0.2906 -0.0709 57  PHE   Z O   
44599 C  CB  . PHE   Z  57  ? 1.4180 0.6295 1.0455 0.1635  -0.2086 -0.1535 57  PHE   Z CB  
44600 C  CG  . PHE   Z  57  ? 1.3992 0.5970 1.0241 0.1597  -0.2050 -0.1851 57  PHE   Z CG  
44601 C  CD1 . PHE   Z  57  ? 1.4175 0.6533 1.0041 0.1675  -0.2113 -0.1613 57  PHE   Z CD1 
44602 C  CD2 . PHE   Z  57  ? 1.3598 0.6020 0.9801 0.1684  -0.2063 -0.1905 57  PHE   Z CD2 
44603 C  CE1 . PHE   Z  57  ? 1.3870 0.6554 1.0443 0.1360  -0.2295 -0.1415 57  PHE   Z CE1 
44604 C  CE2 . PHE   Z  57  ? 1.3367 0.5935 1.0026 0.1562  -0.2101 -0.1910 57  PHE   Z CE2 
44605 C  CZ  . PHE   Z  57  ? 1.3673 0.6359 1.0021 0.1660  -0.2258 -0.1881 57  PHE   Z CZ  
44606 N  N   . ALA   Z  58  ? 1.4650 0.6418 1.1157 0.0692  -0.2639 -0.1172 58  ALA   Z N   
44607 C  CA  . ALA   Z  58  ? 1.4418 0.6766 1.1782 0.0776  -0.2501 -0.1180 58  ALA   Z CA  
44608 C  C   . ALA   Z  58  ? 1.4514 0.6683 1.2127 0.1114  -0.2298 -0.0373 58  ALA   Z C   
44609 O  O   . ALA   Z  58  ? 1.4665 0.7099 1.2447 0.2100  -0.2218 0.1007  58  ALA   Z O   
44610 C  CB  . ALA   Z  58  ? 1.4562 0.7166 1.2000 0.0575  -0.2424 -0.1654 58  ALA   Z CB  
44611 N  N   . ALA   Z  59  ? 1.4519 0.6546 1.2507 0.0649  -0.2268 -0.0183 59  ALA   Z N   
44612 C  CA  . ALA   Z  59  ? 1.4207 0.6405 1.2716 0.0552  -0.2505 -0.0801 59  ALA   Z CA  
44613 C  C   . ALA   Z  59  ? 1.3991 0.5676 1.2961 -0.0144 -0.2616 -0.0758 59  ALA   Z C   
44614 O  O   . ALA   Z  59  ? 1.4374 0.5838 1.3132 0.0020  -0.2929 -0.2091 59  ALA   Z O   
44615 C  CB  . ALA   Z  59  ? 1.4130 0.6374 1.2734 0.0345  -0.2471 -0.0704 59  ALA   Z CB  
44616 N  N   . ASP   Z  60  ? 1.3882 0.4454 1.2900 -0.0610 -0.2197 -0.0793 60  ASP   Z N   
44617 C  CA  . ASP   Z  60  ? 1.4244 0.4060 1.2838 -0.0326 -0.1846 -0.0793 60  ASP   Z CA  
44618 C  C   . ASP   Z  60  ? 1.4020 0.4160 1.3255 -0.0387 -0.2038 -0.0502 60  ASP   Z C   
44619 O  O   . ASP   Z  60  ? 1.4319 0.4529 1.3950 -0.0120 -0.1798 -0.0794 60  ASP   Z O   
44620 C  CB  . ASP   Z  60  ? 1.4479 0.4317 1.2713 -0.0102 -0.1628 -0.0713 60  ASP   Z CB  
44621 C  CG  . ASP   Z  60  ? 1.4610 0.4092 1.2810 -0.0053 -0.1421 -0.0503 60  ASP   Z CG  
44622 O  OD1 . ASP   Z  60  ? 1.4995 0.3723 1.2839 -0.0126 -0.1286 -0.0719 60  ASP   Z OD1 
44623 O  OD2 . ASP   Z  60  ? 1.4700 0.5132 1.3229 0.0432  -0.1634 -0.0482 60  ASP   Z OD2 
44624 N  N   . GLY   Z  61  ? 1.3989 0.4538 1.3201 -0.0184 -0.2484 -0.1079 61  GLY   Z N   
44625 C  CA  . GLY   Z  61  ? 1.4089 0.5335 1.3685 -0.0046 -0.2359 -0.1167 61  GLY   Z CA  
44626 C  C   . GLY   Z  61  ? 1.4661 0.5536 1.3979 0.0007  -0.2586 -0.0938 61  GLY   Z C   
44627 O  O   . GLY   Z  61  ? 1.4640 0.6589 1.3780 0.0022  -0.2544 -0.1136 61  GLY   Z O   
44628 N  N   . ASP   Z  62  ? 1.4721 0.6511 1.3819 0.0295  -0.2222 -0.1407 62  ASP   Z N   
44629 C  CA  . ASP   Z  62  ? 1.4319 0.6762 1.4256 0.0339  -0.2278 -0.1264 62  ASP   Z CA  
44630 C  C   . ASP   Z  62  ? 1.3225 0.6178 1.4658 0.0658  -0.1767 -0.1003 62  ASP   Z C   
44631 O  O   . ASP   Z  62  ? 1.3558 0.5740 1.5537 0.0485  -0.1597 -0.1169 62  ASP   Z O   
44632 C  CB  . ASP   Z  62  ? 1.4654 0.7663 1.4213 0.0168  -0.2527 -0.1435 62  ASP   Z CB  
44633 C  CG  . ASP   Z  62  ? 1.5272 0.8494 1.4474 -0.0106 -0.3098 -0.1611 62  ASP   Z CG  
44634 O  OD1 . ASP   Z  62  ? 1.5353 0.8037 1.4906 -0.1023 -0.3194 -0.2324 62  ASP   Z OD1 
44635 O  OD2 . ASP   Z  62  ? 1.5505 1.0295 1.3947 -0.0405 -0.3120 -0.0948 62  ASP   Z OD2 
44636 N  N   . ALA   Z  63  ? 1.3177 0.5953 1.4098 0.0495  -0.1824 -0.0796 63  ALA   Z N   
44637 C  CA  . ALA   Z  63  ? 1.3571 0.5703 1.3747 0.0715  -0.1677 -0.1191 63  ALA   Z CA  
44638 C  C   . ALA   Z  63  ? 1.3670 0.6251 1.3869 0.0710  -0.1434 -0.1250 63  ALA   Z C   
44639 O  O   . ALA   Z  63  ? 1.3504 0.6774 1.4320 0.1805  -0.1005 -0.1817 63  ALA   Z O   
44640 C  CB  . ALA   Z  63  ? 1.3694 0.5129 1.3658 0.0806  -0.1804 -0.0903 63  ALA   Z CB  
44641 N  N   . LEU   Z  64  ? 1.4022 0.5232 1.4088 0.0568  -0.1517 -0.1671 64  LEU   Z N   
44642 C  CA  . LEU   Z  64  ? 1.4613 0.5644 1.3900 0.0325  -0.1791 -0.1784 64  LEU   Z CA  
44643 C  C   . LEU   Z  64  ? 1.4417 0.5782 1.4091 0.0075  -0.2230 -0.1411 64  LEU   Z C   
44644 O  O   . LEU   Z  64  ? 1.4966 0.5593 1.3980 -0.0451 -0.2427 -0.1404 64  LEU   Z O   
44645 C  CB  . LEU   Z  64  ? 1.4777 0.5727 1.3640 0.0449  -0.2065 -0.1869 64  LEU   Z CB  
44646 C  CG  . LEU   Z  64  ? 1.4935 0.6001 1.3605 0.0464  -0.2381 -0.1846 64  LEU   Z CG  
44647 C  CD1 . LEU   Z  64  ? 1.4868 0.6639 1.3934 0.0546  -0.2650 -0.1957 64  LEU   Z CD1 
44648 C  CD2 . LEU   Z  64  ? 1.4665 0.5853 1.3827 0.0199  -0.2584 -0.1927 64  LEU   Z CD2 
44649 N  N   . VAL   Z  65  ? 1.4619 0.6131 1.4078 0.0072  -0.2512 -0.1331 65  VAL   Z N   
44650 C  CA  . VAL   Z  65  ? 1.4797 0.6284 1.4327 0.0264  -0.2280 -0.1125 65  VAL   Z CA  
44651 C  C   . VAL   Z  65  ? 1.4420 0.5777 1.3836 0.0176  -0.2215 -0.1850 65  VAL   Z C   
44652 O  O   . VAL   Z  65  ? 1.4370 0.5755 1.4020 0.0272  -0.2175 -0.1797 65  VAL   Z O   
44653 C  CB  . VAL   Z  65  ? 1.4870 0.6389 1.4648 0.0171  -0.2376 -0.1111 65  VAL   Z CB  
44654 C  CG1 . VAL   Z  65  ? 1.4824 0.7036 1.5483 0.0577  -0.2028 -0.0863 65  VAL   Z CG1 
44655 C  CG2 . VAL   Z  65  ? 1.5217 0.6504 1.4702 -0.0039 -0.2173 -0.1071 65  VAL   Z CG2 
44656 N  N   . LYS   Z  66  ? 1.4749 0.5154 1.3318 -0.0091 -0.2523 -0.1538 66  LYS   Z N   
44657 C  CA  . LYS   Z  66  ? 1.4845 0.5200 1.3521 0.0413  -0.2531 -0.1257 66  LYS   Z CA  
44658 C  C   . LYS   Z  66  ? 1.5030 0.4617 1.3504 0.0421  -0.2735 -0.0869 66  LYS   Z C   
44659 O  O   . LYS   Z  66  ? 1.5250 0.4059 1.3574 -0.0004 -0.3218 -0.1047 66  LYS   Z O   
44660 C  CB  . LYS   Z  66  ? 1.5080 0.5287 1.3475 0.0350  -0.2433 -0.1212 66  LYS   Z CB  
44661 C  CG  . LYS   Z  66  ? 1.5186 0.5733 1.3499 0.0920  -0.2262 -0.0989 66  LYS   Z CG  
44662 C  CD  . LYS   Z  66  ? 1.5350 0.6470 1.3485 0.1001  -0.2549 -0.1453 66  LYS   Z CD  
44663 C  CE  . LYS   Z  66  ? 1.5518 0.6862 1.3342 0.1494  -0.2690 -0.1414 66  LYS   Z CE  
44664 N  NZ  . LYS   Z  66  ? 1.5392 0.7616 1.3394 0.1480  -0.2814 -0.1643 66  LYS   Z NZ  
44665 N  N   . ARG   Z  67  ? 1.5248 0.4726 1.3391 0.0416  -0.2676 -0.0544 67  ARG   Z N   
44666 C  CA  . ARG   Z  67  ? 1.4661 0.4421 1.3306 0.0487  -0.2460 -0.0476 67  ARG   Z CA  
44667 C  C   . ARG   Z  67  ? 1.5082 0.4785 1.3147 0.0598  -0.2369 -0.0939 67  ARG   Z C   
44668 O  O   . ARG   Z  67  ? 1.4251 0.4935 1.2615 0.0563  -0.1791 -0.0967 67  ARG   Z O   
44669 C  CB  . ARG   Z  67  ? 1.4650 0.4461 1.3339 0.0328  -0.2704 -0.0267 67  ARG   Z CB  
44670 C  CG  . ARG   Z  67  ? 1.4590 0.4902 1.3578 0.0437  -0.2645 -0.0028 67  ARG   Z CG  
44671 C  CD  . ARG   Z  67  ? 1.4857 0.6211 1.4000 0.0151  -0.2620 -0.0567 67  ARG   Z CD  
44672 N  NE  . ARG   Z  67  ? 1.5271 0.7334 1.3661 -0.0157 -0.2858 -0.0170 67  ARG   Z NE  
44673 C  CZ  . ARG   Z  67  ? 1.6197 0.7615 1.3739 -0.0426 -0.2903 -0.1231 67  ARG   Z CZ  
44674 N  NH1 . ARG   Z  67  ? 1.6625 0.7600 1.3926 -0.0095 -0.2873 -0.1824 67  ARG   Z NH1 
44675 N  NH2 . ARG   Z  67  ? 1.6576 0.8153 1.3364 -0.0633 -0.2902 -0.0850 67  ARG   Z NH2 
44676 N  N   . PHE   Z  68  ? 1.4815 0.4920 1.2827 0.0723  -0.2019 -0.1168 68  PHE   Z N   
44677 C  CA  . PHE   Z  68  ? 1.5114 0.5266 1.2721 0.0914  -0.2069 -0.1578 68  PHE   Z CA  
44678 C  C   . PHE   Z  68  ? 1.5482 0.5466 1.3648 0.1007  -0.2314 -0.1226 68  PHE   Z C   
44679 O  O   . PHE   Z  68  ? 1.5684 0.6737 1.3606 0.1364  -0.1995 -0.1440 68  PHE   Z O   
44680 C  CB  . PHE   Z  68  ? 1.4701 0.5450 1.2196 0.0935  -0.2210 -0.1438 68  PHE   Z CB  
44681 C  CG  . PHE   Z  68  ? 1.4813 0.5432 1.2066 0.0858  -0.2190 -0.1696 68  PHE   Z CG  
44682 C  CD1 . PHE   Z  68  ? 1.4913 0.5223 1.2075 0.0840  -0.1948 -0.1788 68  PHE   Z CD1 
44683 C  CD2 . PHE   Z  68  ? 1.4767 0.5718 1.1881 0.0714  -0.1950 -0.1794 68  PHE   Z CD2 
44684 C  CE1 . PHE   Z  68  ? 1.5055 0.5454 1.2252 0.0651  -0.1717 -0.1670 68  PHE   Z CE1 
44685 C  CE2 . PHE   Z  68  ? 1.5005 0.5653 1.1936 0.0704  -0.1748 -0.1689 68  PHE   Z CE2 
44686 C  CZ  . PHE   Z  68  ? 1.5062 0.5731 1.1931 0.0622  -0.1656 -0.1706 68  PHE   Z CZ  
44687 N  N   . LYS   Z  69  ? 1.5860 0.5104 1.3609 0.1085  -0.2247 -0.1419 69  LYS   Z N   
44688 C  CA  . LYS   Z  69  ? 1.5909 0.6266 1.3968 0.1316  -0.2293 -0.0998 69  LYS   Z CA  
44689 C  C   . LYS   Z  69  ? 1.5597 0.6389 1.4490 0.1268  -0.1866 -0.0557 69  LYS   Z C   
44690 O  O   . LYS   Z  69  ? 1.5830 0.6110 1.4672 0.1466  -0.2074 -0.0507 69  LYS   Z O   
44691 C  CB  . LYS   Z  69  ? 1.6048 0.6412 1.4123 0.1199  -0.2448 -0.1134 69  LYS   Z CB  
44692 C  CG  . LYS   Z  69  ? 1.5939 0.7478 1.4206 0.0689  -0.2479 -0.0825 69  LYS   Z CG  
44693 C  CD  . LYS   Z  69  ? 1.6116 0.8423 1.4112 0.0788  -0.2576 -0.0555 69  LYS   Z CD  
44694 C  CE  . LYS   Z  69  ? 1.5651 0.8972 1.3902 0.0937  -0.2905 -0.0819 69  LYS   Z CE  
44695 N  NZ  . LYS   Z  69  ? 1.5608 0.9490 1.3796 0.1229  -0.2863 -0.0766 69  LYS   Z NZ  
44696 N  N   . ASN   Z  70  ? 1.5939 0.6953 1.4736 0.1022  -0.1362 -0.0252 70  ASN   Z N   
44697 C  CA  . ASN   Z  70  ? 1.6443 0.6007 1.5025 0.1799  -0.1147 -0.0598 70  ASN   Z CA  
44698 C  C   . ASN   Z  70  ? 1.6745 0.5485 1.4731 0.2131  -0.1123 -0.0205 70  ASN   Z C   
44699 O  O   . ASN   Z  70  ? 1.7396 0.5593 1.4869 0.2535  -0.0738 -0.0149 70  ASN   Z O   
44700 C  CB  . ASN   Z  70  ? 1.6327 0.5719 1.5499 0.1512  -0.1087 -0.0554 70  ASN   Z CB  
44701 C  CG  . ASN   Z  70  ? 1.5962 0.5593 1.6255 0.1730  -0.0931 -0.0525 70  ASN   Z CG  
44702 O  OD1 . ASN   Z  70  ? 1.6028 0.5873 1.6789 0.1461  -0.1282 -0.0522 70  ASN   Z OD1 
44703 N  ND2 . ASN   Z  70  ? 1.6170 0.7118 1.6701 0.2328  -0.0954 -0.0096 70  ASN   Z ND2 
44704 N  N   . SER   Z  71  ? 1.6750 0.6207 1.3709 0.1985  -0.1400 -0.0491 71  SER   Z N   
44705 C  CA  . SER   Z  71  ? 1.6870 0.6706 1.3771 0.1984  -0.1404 -0.0687 71  SER   Z CA  
44706 C  C   . SER   Z  71  ? 1.6651 0.5764 1.3924 0.2358  -0.2001 -0.0256 71  SER   Z C   
44707 O  O   . SER   Z  71  ? 1.6944 0.4112 1.4298 0.2470  -0.2402 0.0651  71  SER   Z O   
44708 C  CB  . SER   Z  71  ? 1.7472 0.6810 1.3325 0.1809  -0.1230 -0.0587 71  SER   Z CB  
44709 O  OG  . SER   Z  71  ? 1.8009 0.8491 1.3211 0.1461  -0.1047 -0.0702 71  SER   Z OG  
44710 N  N   . VAL   Z  72  ? 1.6568 0.6336 1.4115 0.2364  -0.2189 -0.0543 72  VAL   Z N   
44711 C  CA  . VAL   Z  72  ? 1.6452 0.7391 1.4525 0.2222  -0.2237 -0.0805 72  VAL   Z CA  
44712 C  C   . VAL   Z  72  ? 1.6321 0.7394 1.4387 0.2004  -0.2232 -0.0745 72  VAL   Z C   
44713 O  O   . VAL   Z  72  ? 1.6290 0.7591 1.4024 0.1878  -0.2057 -0.0661 72  VAL   Z O   
44714 C  CB  . VAL   Z  72  ? 1.6561 0.7776 1.4792 0.2273  -0.2505 -0.1113 72  VAL   Z CB  
44715 C  CG1 . VAL   Z  72  ? 1.6606 0.8178 1.4953 0.2438  -0.2570 -0.1018 72  VAL   Z CG1 
44716 C  CG2 . VAL   Z  72  ? 1.6705 0.7841 1.4588 0.2386  -0.2409 -0.1157 72  VAL   Z CG2 
44717 N  N   . LYS   Z  73  ? 1.6056 0.7674 1.4462 0.1921  -0.2107 -0.0899 73  LYS   Z N   
44718 C  CA  . LYS   Z  73  ? 1.6128 0.7095 1.5576 0.2472  -0.1876 -0.1274 73  LYS   Z CA  
44719 C  C   . LYS   Z  73  ? 1.6221 0.7091 1.5886 0.2402  -0.2026 -0.1244 73  LYS   Z C   
44720 O  O   . LYS   Z  73  ? 1.5642 0.7307 1.6352 0.2277  -0.2138 -0.1635 73  LYS   Z O   
44721 C  CB  . LYS   Z  73  ? 1.6202 0.7201 1.5697 0.2872  -0.1748 -0.1357 73  LYS   Z CB  
44722 C  CG  . LYS   Z  73  ? 1.6507 0.7057 1.6117 0.3107  -0.1680 -0.1302 73  LYS   Z CG  
44723 C  CD  . LYS   Z  73  ? 1.6492 0.7118 1.6503 0.2795  -0.1329 -0.1332 73  LYS   Z CD  
44724 C  CE  . LYS   Z  73  ? 1.6937 0.7675 1.6974 0.2305  -0.1449 -0.0668 73  LYS   Z CE  
44725 N  NZ  . LYS   Z  73  ? 1.6838 0.8422 1.7400 0.2042  -0.1233 -0.0944 73  LYS   Z NZ  
44726 N  N   . TRP   Z  74  ? 1.6155 0.6394 1.5812 0.2063  -0.1932 -0.1327 74  TRP   Z N   
44727 C  CA  . TRP   Z  74  ? 1.6903 0.5646 1.5730 0.1938  -0.1469 -0.1403 74  TRP   Z CA  
44728 C  C   . TRP   Z  74  ? 1.6865 0.5492 1.5600 0.1660  -0.1727 -0.1997 74  TRP   Z C   
44729 O  O   . TRP   Z  74  ? 1.6856 0.6395 1.4911 0.0776  -0.2009 -0.2600 74  TRP   Z O   
44730 C  CB  . TRP   Z  74  ? 1.6916 0.5492 1.5710 0.1991  -0.1590 -0.1084 74  TRP   Z CB  
44731 C  CG  . TRP   Z  74  ? 1.7339 0.5483 1.5872 0.2066  -0.1372 -0.0976 74  TRP   Z CG  
44732 C  CD1 . TRP   Z  74  ? 1.7289 0.5743 1.5556 0.2020  -0.1244 -0.0826 74  TRP   Z CD1 
44733 C  CD2 . TRP   Z  74  ? 1.7755 0.5753 1.5771 0.1657  -0.1312 -0.0843 74  TRP   Z CD2 
44734 N  NE1 . TRP   Z  74  ? 1.7505 0.5445 1.5678 0.2254  -0.1306 -0.0641 74  TRP   Z NE1 
44735 C  CE2 . TRP   Z  74  ? 1.7687 0.5416 1.5746 0.1644  -0.1279 -0.0508 74  TRP   Z CE2 
44736 C  CE3 . TRP   Z  74  ? 1.8035 0.5501 1.5993 0.1691  -0.1185 -0.0654 74  TRP   Z CE3 
44737 C  CZ2 . TRP   Z  74  ? 1.7706 0.5653 1.5931 0.1405  -0.1262 -0.0399 74  TRP   Z CZ2 
44738 C  CZ3 . TRP   Z  74  ? 1.8252 0.5881 1.6242 0.1839  -0.1041 -0.0226 74  TRP   Z CZ3 
44739 C  CH2 . TRP   Z  74  ? 1.8093 0.5796 1.6262 0.1726  -0.1140 -0.0540 74  TRP   Z CH2 
44740 N  N   . TYR   Z  75  ? 1.6531 0.6216 1.4997 0.1505  -0.1376 -0.1960 75  TYR   Z N   
44741 C  CA  . TYR   Z  75  ? 1.6671 0.6972 1.5163 0.1700  -0.1238 -0.2623 75  TYR   Z CA  
44742 C  C   . TYR   Z  75  ? 1.7090 0.6100 1.5660 0.1574  -0.1266 -0.2143 75  TYR   Z C   
44743 O  O   . TYR   Z  75  ? 1.7595 0.6862 1.5696 0.1628  -0.1435 -0.2452 75  TYR   Z O   
44744 C  CB  . TYR   Z  75  ? 1.6269 0.7662 1.4779 0.1183  -0.0859 -0.2595 75  TYR   Z CB  
44745 C  CG  . TYR   Z  75  ? 1.6422 0.8624 1.4729 0.1399  -0.0765 -0.3417 75  TYR   Z CG  
44746 C  CD1 . TYR   Z  75  ? 1.6431 0.8090 1.4422 0.1352  -0.0683 -0.3944 75  TYR   Z CD1 
44747 C  CD2 . TYR   Z  75  ? 1.6606 0.8302 1.4673 0.1695  -0.0379 -0.3837 75  TYR   Z CD2 
44748 C  CE1 . TYR   Z  75  ? 1.6593 0.7676 1.4325 0.1562  -0.0757 -0.4345 75  TYR   Z CE1 
44749 C  CE2 . TYR   Z  75  ? 1.6714 0.8003 1.4620 0.2022  -0.0391 -0.4228 75  TYR   Z CE2 
44750 C  CZ  . TYR   Z  75  ? 1.6785 0.7748 1.4378 0.1946  -0.0361 -0.4479 75  TYR   Z CZ  
44751 O  OH  . TYR   Z  75  ? 1.6876 0.8050 1.4128 0.2418  -0.0577 -0.4910 75  TYR   Z OH  
44752 N  N   . HIS   Z  76  ? 1.6925 0.5888 1.5844 0.1342  -0.1298 -0.1579 76  HIS   Z N   
44753 C  CA  . HIS   Z  76  ? 1.6604 0.6396 1.6198 0.1270  -0.1141 -0.0965 76  HIS   Z CA  
44754 C  C   . HIS   Z  76  ? 1.7167 0.6117 1.6976 0.1669  -0.1193 -0.0323 76  HIS   Z C   
44755 O  O   . HIS   Z  76  ? 1.7135 0.5130 1.6846 0.1918  -0.1053 0.0588  76  HIS   Z O   
44756 C  CB  . HIS   Z  76  ? 1.6031 0.6713 1.6070 0.0873  -0.0812 -0.0863 76  HIS   Z CB  
44757 C  CG  . HIS   Z  76  ? 1.5460 0.7206 1.5258 0.0656  -0.0458 -0.0807 76  HIS   Z CG  
44758 N  ND1 . HIS   Z  76  ? 1.5189 0.7427 1.5561 0.0490  -0.0007 -0.0961 76  HIS   Z ND1 
44759 C  CD2 . HIS   Z  76  ? 1.4469 0.7315 1.5222 0.0191  -0.0536 -0.0634 76  HIS   Z CD2 
44760 C  CE1 . HIS   Z  76  ? 1.4402 0.7843 1.4994 0.0342  -0.0093 -0.1059 76  HIS   Z CE1 
44761 N  NE2 . HIS   Z  76  ? 1.3976 0.7592 1.4846 0.0068  -0.0495 -0.0905 76  HIS   Z NE2 
44762 N  N   . PHE   Z  77  ? 1.7115 0.5722 1.7452 0.1649  -0.1155 0.0138  77  PHE   Z N   
44763 C  CA  . PHE   Z  77  ? 1.7459 0.5187 1.8143 0.1835  -0.1530 -0.0083 77  PHE   Z CA  
44764 C  C   . PHE   Z  77  ? 1.7550 0.6420 1.8217 0.1321  -0.1714 -0.0020 77  PHE   Z C   
44765 O  O   . PHE   Z  77  ? 1.7811 0.6777 1.9252 0.1286  -0.2046 -0.1060 77  PHE   Z O   
44766 C  CB  . PHE   Z  77  ? 1.7320 0.4742 1.7809 0.2071  -0.1795 0.0110  77  PHE   Z CB  
44767 C  CG  . PHE   Z  77  ? 1.7687 0.4908 1.7840 0.2570  -0.2034 0.0368  77  PHE   Z CG  
44768 C  CD1 . PHE   Z  77  ? 1.7943 0.5687 1.8114 0.3144  -0.1936 0.0195  77  PHE   Z CD1 
44769 C  CD2 . PHE   Z  77  ? 1.7558 0.4656 1.7990 0.3018  -0.2172 0.0617  77  PHE   Z CD2 
44770 C  CE1 . PHE   Z  77  ? 1.8189 0.6635 1.8315 0.3321  -0.2263 0.0452  77  PHE   Z CE1 
44771 C  CE2 . PHE   Z  77  ? 1.7815 0.4844 1.8165 0.3403  -0.2371 0.0499  77  PHE   Z CE2 
44772 C  CZ  . PHE   Z  77  ? 1.7907 0.5976 1.8490 0.3601  -0.2530 0.0693  77  PHE   Z CZ  
44773 N  N   . ASP   Z  78  ? 1.7816 0.4918 1.7814 0.0955  -0.1240 -0.0270 78  ASP   Z N   
44774 C  CA  . ASP   Z  78  ? 1.8753 0.5333 1.7881 0.0501  -0.1259 -0.0605 78  ASP   Z CA  
44775 C  C   . ASP   Z  78  ? 1.9055 0.5590 1.8533 0.0368  -0.0726 -0.0637 78  ASP   Z C   
44776 O  O   . ASP   Z  78  ? 1.9325 0.6866 1.8428 0.0038  -0.0882 -0.0629 78  ASP   Z O   
44777 C  CB  . ASP   Z  78  ? 1.8743 0.5774 1.7375 0.0622  -0.1180 -0.0707 78  ASP   Z CB  
44778 C  CG  . ASP   Z  78  ? 1.8696 0.6810 1.7324 0.0177  -0.1313 -0.0196 78  ASP   Z CG  
44779 O  OD1 . ASP   Z  78  ? 1.8604 0.6498 1.7436 0.0484  -0.1208 -0.0402 78  ASP   Z OD1 
44780 O  OD2 . ASP   Z  78  ? 1.8228 0.7757 1.7184 0.1181  -0.1133 0.0145  78  ASP   Z OD2 
44781 N  N   . HIS   Z  79  ? 1.9061 0.5418 1.8873 0.0330  -0.1083 -0.1444 79  HIS   Z N   
44782 C  CA  . HIS   Z  79  ? 1.9330 0.5684 1.8686 0.0892  -0.1104 -0.1795 79  HIS   Z CA  
44783 C  C   . HIS   Z  79  ? 1.9190 0.5593 1.8659 0.1055  -0.0754 -0.1746 79  HIS   Z C   
44784 O  O   . HIS   Z  79  ? 1.8401 0.7077 1.8319 0.0647  -0.0532 -0.2423 79  HIS   Z O   
44785 C  CB  . HIS   Z  79  ? 1.9484 0.5544 1.8804 0.1457  -0.1426 -0.2099 79  HIS   Z CB  
44786 C  CG  . HIS   Z  79  ? 1.9936 0.5006 1.9433 0.1748  -0.2295 -0.1402 79  HIS   Z CG  
44787 N  ND1 . HIS   Z  79  ? 1.9901 0.6203 1.9067 0.1796  -0.2130 -0.1098 79  HIS   Z ND1 
44788 C  CD2 . HIS   Z  79  ? 2.0500 0.4208 1.9741 0.1717  -0.2509 -0.1920 79  HIS   Z CD2 
44789 C  CE1 . HIS   Z  79  ? 2.0322 0.6168 1.8931 0.1457  -0.2769 -0.1088 79  HIS   Z CE1 
44790 N  NE2 . HIS   Z  79  ? 1.9971 0.5203 1.9724 0.1450  -0.3120 -0.1466 79  HIS   Z NE2 
44791 N  N   . ASN   Z  80  ? 1.9494 0.5662 1.9112 0.1268  -0.0258 -0.1441 80  ASN   Z N   
44792 C  CA  . ASN   Z  80  ? 1.9499 0.6701 1.9638 0.1415  0.0151  -0.0837 80  ASN   Z CA  
44793 C  C   . ASN   Z  80  ? 1.9480 0.6222 1.9064 0.1590  0.0227  -0.0750 80  ASN   Z C   
44794 O  O   . ASN   Z  80  ? 1.9955 0.4938 1.9025 0.1602  0.0549  -0.0401 80  ASN   Z O   
44795 C  CB  . ASN   Z  80  ? 2.0700 0.8560 1.9529 0.1961  0.0941  -0.0719 80  ASN   Z CB  
44796 C  CG  . ASN   Z  80  ? 2.1320 0.9291 2.0621 0.2575  0.1253  -0.0216 80  ASN   Z CG  
44797 O  OD1 . ASN   Z  80  ? 2.2793 1.1061 2.0516 0.2503  0.2015  -0.0378 80  ASN   Z OD1 
44798 N  ND2 . ASN   Z  80  ? 2.1353 0.9462 2.1161 0.2675  0.1546  0.0199  80  ASN   Z ND2 
44799 N  N   . ASP   Z  81  ? 1.8603 0.7040 1.8399 0.1354  -0.0197 -0.0847 81  ASP   Z N   
44800 C  CA  . ASP   Z  81  ? 1.7907 0.8083 1.8304 0.1304  -0.0387 -0.1011 81  ASP   Z CA  
44801 C  C   . ASP   Z  81  ? 1.7360 0.8103 1.7790 0.1213  -0.0650 -0.1264 81  ASP   Z C   
44802 O  O   . ASP   Z  81  ? 1.7089 0.7618 1.9429 0.1444  -0.0403 -0.1311 81  ASP   Z O   
44803 C  CB  . ASP   Z  81  ? 1.7808 0.8034 1.8391 0.1323  -0.0244 -0.0832 81  ASP   Z CB  
44804 C  CG  . ASP   Z  81  ? 1.7696 0.9053 1.8228 0.1024  -0.0163 -0.1224 81  ASP   Z CG  
44805 O  OD1 . ASP   Z  81  ? 1.7437 0.7605 1.7604 0.1053  -0.0851 -0.0649 81  ASP   Z OD1 
44806 O  OD2 . ASP   Z  81  ? 1.7465 1.0273 1.8172 0.1610  -0.0583 -0.1289 81  ASP   Z OD2 
44807 N  N   . LYS   Z  82  ? 1.7136 0.7932 1.7503 0.0975  -0.0544 -0.1444 82  LYS   Z N   
44808 C  CA  . LYS   Z  82  ? 1.6979 0.8084 1.7015 0.0880  -0.0747 -0.1517 82  LYS   Z CA  
44809 C  C   . LYS   Z  82  ? 1.6664 0.7849 1.6415 0.0620  -0.0997 -0.1029 82  LYS   Z C   
44810 O  O   . LYS   Z  82  ? 1.5679 0.7979 1.6112 0.0417  -0.1394 -0.0412 82  LYS   Z O   
44811 C  CB  . LYS   Z  82  ? 1.7494 0.8318 1.6583 0.0850  -0.0657 -0.1894 82  LYS   Z CB  
44812 C  CG  . LYS   Z  82  ? 1.7523 0.8477 1.6098 0.0867  -0.0530 -0.2118 82  LYS   Z CG  
44813 C  CD  . LYS   Z  82  ? 1.7674 0.9155 1.5985 0.0987  -0.0509 -0.2518 82  LYS   Z CD  
44814 C  CE  . LYS   Z  82  ? 1.7400 1.0079 1.4748 0.0912  -0.0439 -0.2637 82  LYS   Z CE  
44815 N  NZ  . LYS   Z  82  ? 1.7454 1.0781 1.4623 0.0903  -0.0236 -0.3091 82  LYS   Z NZ  
44816 N  N   . LYS   Z  83  ? 1.6707 0.8612 1.6592 0.0709  -0.0436 -0.0715 83  LYS   Z N   
44817 C  CA  . LYS   Z  83  ? 1.5950 0.8280 1.6748 0.0828  -0.0346 -0.0355 83  LYS   Z CA  
44818 C  C   . LYS   Z  83  ? 1.5931 0.7134 1.6201 0.0848  -0.0079 -0.0739 83  LYS   Z C   
44819 O  O   . LYS   Z  83  ? 1.5655 0.5574 1.6203 0.1089  -0.0222 -0.0571 83  LYS   Z O   
44820 C  CB  . LYS   Z  83  ? 1.6236 0.8931 1.7322 0.0513  0.0003  -0.0308 83  LYS   Z CB  
44821 C  CG  . LYS   Z  83  ? 1.5604 0.9304 1.7532 0.0104  0.0051  -0.0366 83  LYS   Z CG  
44822 C  CD  . LYS   Z  83  ? 1.5499 1.0282 1.8059 -0.0022 0.0294  -0.0086 83  LYS   Z CD  
44823 C  CE  . LYS   Z  83  ? 1.5065 1.0324 1.8645 -0.0792 0.0159  0.0183  83  LYS   Z CE  
44824 N  NZ  . LYS   Z  83  ? 1.5258 1.1723 1.9246 -0.0872 0.0505  0.0835  83  LYS   Z NZ  
44825 N  N   . LEU   Z  84  ? 1.5105 0.7271 1.5890 0.1306  -0.0383 -0.0264 84  LEU   Z N   
44826 C  CA  . LEU   Z  84  ? 1.5194 0.7958 1.5259 0.1751  -0.0263 -0.0300 84  LEU   Z CA  
44827 C  C   . LEU   Z  84  ? 1.4987 0.7713 1.5406 0.2310  -0.0245 0.0040  84  LEU   Z C   
44828 O  O   . LEU   Z  84  ? 1.4519 0.6079 1.5219 0.2758  0.0024  0.0537  84  LEU   Z O   
44829 C  CB  . LEU   Z  84  ? 1.5028 0.8194 1.5125 0.2060  -0.0469 -0.0355 84  LEU   Z CB  
44830 C  CG  . LEU   Z  84  ? 1.4988 0.9112 1.4662 0.2250  -0.0670 -0.0467 84  LEU   Z CG  
44831 C  CD1 . LEU   Z  84  ? 1.5477 0.8919 1.4313 0.2391  -0.0580 -0.0749 84  LEU   Z CD1 
44832 C  CD2 . LEU   Z  84  ? 1.4849 0.9804 1.4743 0.1987  -0.0496 -0.0336 84  LEU   Z CD2 
44833 N  N   . SER   Z  85  ? 1.5449 0.8556 1.5464 0.2449  -0.0303 0.0092  85  SER   Z N   
44834 C  CA  . SER   Z  85  ? 1.5972 0.9157 1.5757 0.2109  -0.0199 0.0389  85  SER   Z CA  
44835 C  C   . SER   Z  85  ? 1.6087 0.9032 1.6027 0.2008  -0.0513 0.0128  85  SER   Z C   
44836 O  O   . SER   Z  85  ? 1.5934 0.9081 1.6189 0.1757  -0.0822 0.0009  85  SER   Z O   
44837 C  CB  . SER   Z  85  ? 1.6141 1.0271 1.5705 0.2181  -0.0192 0.0411  85  SER   Z CB  
44838 O  OG  . SER   Z  85  ? 1.6083 1.1458 1.4993 0.1990  -0.0151 0.0648  85  SER   Z OG  
44839 N  N   . ILE   Z  86  ? 1.6755 0.8751 1.6005 0.2035  -0.0925 0.0207  86  ILE   Z N   
44840 C  CA  . ILE   Z  86  ? 1.6271 0.8136 1.5728 0.1557  -0.1059 0.0521  86  ILE   Z CA  
44841 C  C   . ILE   Z  86  ? 1.6146 0.7882 1.5401 0.1292  -0.1004 0.0057  86  ILE   Z C   
44842 O  O   . ILE   Z  86  ? 1.6178 0.6733 1.5085 0.0659  -0.0786 0.0105  86  ILE   Z O   
44843 C  CB  . ILE   Z  86  ? 1.6226 0.8248 1.5913 0.1589  -0.0970 0.1095  86  ILE   Z CB  
44844 C  CG1 . ILE   Z  86  ? 1.6052 0.8226 1.5791 0.1642  -0.0923 0.1240  86  ILE   Z CG1 
44845 C  CG2 . ILE   Z  86  ? 1.6448 0.8174 1.6099 0.1502  -0.0760 0.1337  86  ILE   Z CG2 
44846 C  CD1 . ILE   Z  86  ? 1.5857 0.8171 1.5789 0.1712  -0.0833 0.1423  86  ILE   Z CD1 
44847 N  N   . ASN   Z  87  ? 1.6094 0.8538 1.5438 0.1447  -0.0868 -0.0178 87  ASN   Z N   
44848 C  CA  . ASN   Z  87  ? 1.6196 0.8685 1.4650 0.1429  -0.0690 -0.0398 87  ASN   Z CA  
44849 C  C   . ASN   Z  87  ? 1.6315 0.8069 1.4964 0.1304  -0.1393 -0.0217 87  ASN   Z C   
44850 O  O   . ASN   Z  87  ? 1.6451 0.7816 1.5206 0.1186  -0.2154 0.0256  87  ASN   Z O   
44851 C  CB  . ASN   Z  87  ? 1.6221 0.9488 1.4723 0.1531  -0.0489 -0.0712 87  ASN   Z CB  
44852 C  CG  . ASN   Z  87  ? 1.6245 0.9556 1.4174 0.1100  -0.0404 -0.1127 87  ASN   Z CG  
44853 O  OD1 . ASN   Z  87  ? 1.6027 0.9603 1.3987 0.0919  -0.0306 -0.0988 87  ASN   Z OD1 
44854 N  ND2 . ASN   Z  87  ? 1.6436 1.0236 1.3983 0.0804  -0.0455 -0.1049 87  ASN   Z ND2 
44855 N  N   . SER   Z  88  ? 1.6380 0.7301 1.4877 0.0634  -0.1202 -0.0734 88  SER   Z N   
44856 C  CA  . SER   Z  88  ? 1.6453 0.6923 1.4307 0.0664  -0.1356 -0.0885 88  SER   Z CA  
44857 C  C   . SER   Z  88  ? 1.5977 0.5858 1.4455 0.0413  -0.1407 -0.1100 88  SER   Z C   
44858 O  O   . SER   Z  88  ? 1.5960 0.5202 1.4439 0.0522  -0.1307 -0.1424 88  SER   Z O   
44859 C  CB  . SER   Z  88  ? 1.6434 0.6957 1.4044 0.0657  -0.1338 -0.0667 88  SER   Z CB  
44860 O  OG  . SER   Z  88  ? 1.6919 0.7102 1.3588 0.0242  -0.1630 -0.0511 88  SER   Z OG  
44861 N  N   . ALA   Z  89  ? 1.6108 0.6027 1.4130 0.0691  -0.1344 -0.1394 89  ALA   Z N   
44862 C  CA  . ALA   Z  89  ? 1.6082 0.7014 1.3959 0.1045  -0.1467 -0.1357 89  ALA   Z CA  
44863 C  C   . ALA   Z  89  ? 1.5829 0.7494 1.3592 0.1266  -0.1389 -0.1571 89  ALA   Z C   
44864 O  O   . ALA   Z  89  ? 1.5366 0.6338 1.3239 0.0788  -0.1796 -0.1971 89  ALA   Z O   
44865 C  CB  . ALA   Z  89  ? 1.5948 0.7789 1.4198 0.1255  -0.1661 -0.1169 89  ALA   Z CB  
44866 N  N   . ALA   Z  90  ? 1.6300 0.7994 1.3433 0.1692  -0.1128 -0.1299 90  ALA   Z N   
44867 C  CA  . ALA   Z  90  ? 1.6571 0.8208 1.3380 0.1780  -0.1061 -0.1026 90  ALA   Z CA  
44868 C  C   . ALA   Z  90  ? 1.6999 0.7670 1.3152 0.1496  -0.1200 -0.1308 90  ALA   Z C   
44869 O  O   . ALA   Z  90  ? 1.7068 0.8578 1.3413 0.1776  -0.0885 -0.0826 90  ALA   Z O   
44870 C  CB  . ALA   Z  90  ? 1.6756 0.9505 1.3287 0.1706  -0.0477 -0.1164 90  ALA   Z CB  
44871 N  N   . ARG   Z  91  ? 1.7149 0.7164 1.3440 0.1341  -0.1476 -0.1231 91  ARG   Z N   
44872 C  CA  . ARG   Z  91  ? 1.7383 0.6784 1.3285 0.1469  -0.1812 -0.1332 91  ARG   Z CA  
44873 C  C   . ARG   Z  91  ? 1.6162 0.6038 1.3553 0.1453  -0.2219 -0.1328 91  ARG   Z C   
44874 O  O   . ARG   Z  91  ? 1.6115 0.5291 1.2992 0.2047  -0.3323 -0.0951 91  ARG   Z O   
44875 C  CB  . ARG   Z  91  ? 1.8253 0.6799 1.3584 0.1490  -0.1561 -0.1465 91  ARG   Z CB  
44876 C  CG  . ARG   Z  91  ? 1.8778 0.6645 1.3615 0.1202  -0.1574 -0.1811 91  ARG   Z CG  
44877 C  CD  . ARG   Z  91  ? 1.9211 0.6857 1.3370 0.1464  -0.1575 -0.1954 91  ARG   Z CD  
44878 N  NE  . ARG   Z  91  ? 2.0229 0.7459 1.2833 0.1402  -0.1430 -0.2426 91  ARG   Z NE  
44879 C  CZ  . ARG   Z  91  ? 2.0939 0.6487 1.3353 0.1147  -0.0994 -0.2946 91  ARG   Z CZ  
44880 N  NH1 . ARG   Z  91  ? 2.1027 0.7075 1.3529 0.0628  -0.1007 -0.2999 91  ARG   Z NH1 
44881 N  NH2 . ARG   Z  91  ? 2.1566 0.6600 1.3055 0.1142  -0.0591 -0.3435 91  ARG   Z NH2 
44882 N  N   . ASN   Z  92  ? 1.6392 0.5890 1.3813 0.1393  -0.2302 -0.1239 92  ASN   Z N   
44883 C  CA  . ASN   Z  92  ? 1.6097 0.5837 1.4157 0.1134  -0.2106 -0.1401 92  ASN   Z CA  
44884 C  C   . ASN   Z  92  ? 1.6080 0.5104 1.4675 0.1082  -0.1835 -0.1139 92  ASN   Z C   
44885 O  O   . ASN   Z  92  ? 1.6149 0.4167 1.5306 0.0934  -0.1646 -0.1329 92  ASN   Z O   
44886 C  CB  . ASN   Z  92  ? 1.5829 0.6293 1.4785 0.1052  -0.2401 -0.1276 92  ASN   Z CB  
44887 C  CG  . ASN   Z  92  ? 1.4939 0.6000 1.5467 0.0619  -0.2534 -0.0983 92  ASN   Z CG  
44888 O  OD1 . ASN   Z  92  ? 1.5023 0.6192 1.5784 0.0832  -0.2812 -0.0855 92  ASN   Z OD1 
44889 N  ND2 . ASN   Z  92  ? 1.4761 0.6477 1.5638 0.0719  -0.2852 -0.1182 92  ASN   Z ND2 
44890 N  N   . ILE   Z  93  ? 1.5934 0.4706 1.4531 0.1133  -0.1460 -0.0778 93  ILE   Z N   
44891 C  CA  . ILE   Z  93  ? 1.5329 0.4296 1.4187 0.1186  -0.1628 -0.0437 93  ILE   Z CA  
44892 C  C   . ILE   Z  93  ? 1.5210 0.2960 1.3566 0.0987  -0.1456 -0.0823 93  ILE   Z C   
44893 O  O   . ILE   Z  93  ? 1.4867 0.2766 1.3096 0.0453  -0.1513 -0.0570 93  ILE   Z O   
44894 C  CB  . ILE   Z  93  ? 1.4973 0.4754 1.4191 0.1231  -0.1523 -0.0448 93  ILE   Z CB  
44895 C  CG1 . ILE   Z  93  ? 1.5087 0.5539 1.4091 0.1262  -0.1564 -0.0279 93  ILE   Z CG1 
44896 C  CG2 . ILE   Z  93  ? 1.4761 0.5008 1.4083 0.1311  -0.1461 -0.0485 93  ILE   Z CG2 
44897 C  CD1 . ILE   Z  93  ? 1.5320 0.5468 1.4190 0.1134  -0.1481 -0.0595 93  ILE   Z CD1 
44898 N  N   . GLN   Z  94  ? 1.5333 0.3057 1.3475 0.1027  -0.1528 -0.1059 94  GLN   Z N   
44899 C  CA  . GLN   Z  94  ? 1.5552 0.4236 1.2780 0.1060  -0.1827 -0.1383 94  GLN   Z CA  
44900 C  C   . GLN   Z  94  ? 1.5810 0.4642 1.3019 0.0669  -0.2067 -0.1214 94  GLN   Z C   
44901 O  O   . GLN   Z  94  ? 1.5878 0.2798 1.3969 0.0574  -0.2305 -0.0382 94  GLN   Z O   
44902 C  CB  . GLN   Z  94  ? 1.5892 0.4750 1.2694 0.0986  -0.1887 -0.2054 94  GLN   Z CB  
44903 C  CG  . GLN   Z  94  ? 1.6134 0.5311 1.2043 0.0945  -0.2068 -0.2199 94  GLN   Z CG  
44904 C  CD  . GLN   Z  94  ? 1.6483 0.6014 1.2067 0.0941  -0.2231 -0.1947 94  GLN   Z CD  
44905 O  OE1 . GLN   Z  94  ? 1.6473 0.5942 1.2052 0.1365  -0.2904 -0.1920 94  GLN   Z OE1 
44906 N  NE2 . GLN   Z  94  ? 1.6591 0.6198 1.1864 0.1065  -0.1951 -0.1715 94  GLN   Z NE2 
44907 N  N   . HIS   Z  95  ? 1.5924 0.4738 1.2404 0.1004  -0.2309 -0.1637 95  HIS   Z N   
44908 C  CA  . HIS   Z  95  ? 1.5688 0.5241 1.2589 0.0948  -0.2556 -0.1479 95  HIS   Z CA  
44909 C  C   . HIS   Z  95  ? 1.5521 0.5921 1.2640 0.0980  -0.2588 -0.1089 95  HIS   Z C   
44910 O  O   . HIS   Z  95  ? 1.5320 0.6617 1.3376 0.0775  -0.3019 -0.0609 95  HIS   Z O   
44911 C  CB  . HIS   Z  95  ? 1.6090 0.5121 1.2848 0.1335  -0.2656 -0.1198 95  HIS   Z CB  
44912 C  CG  . HIS   Z  95  ? 1.6378 0.5455 1.3197 0.1417  -0.3129 -0.1660 95  HIS   Z CG  
44913 N  ND1 . HIS   Z  95  ? 1.6622 0.5709 1.3468 0.1486  -0.2831 -0.1995 95  HIS   Z ND1 
44914 C  CD2 . HIS   Z  95  ? 1.6551 0.5718 1.3328 0.1453  -0.3372 -0.1970 95  HIS   Z CD2 
44915 C  CE1 . HIS   Z  95  ? 1.6609 0.6197 1.3715 0.1417  -0.2959 -0.2656 95  HIS   Z CE1 
44916 N  NE2 . HIS   Z  95  ? 1.6361 0.6221 1.3108 0.1364  -0.3868 -0.2715 95  HIS   Z NE2 
44917 N  N   . LEU   Z  96  ? 1.5069 0.6508 1.3041 0.1240  -0.2499 -0.1327 96  LEU   Z N   
44918 C  CA  . LEU   Z  96  ? 1.4921 0.6540 1.3111 0.1296  -0.2610 -0.1694 96  LEU   Z CA  
44919 C  C   . LEU   Z  96  ? 1.4956 0.6500 1.2734 0.1262  -0.2647 -0.1684 96  LEU   Z C   
44920 O  O   . LEU   Z  96  ? 1.4802 0.6577 1.2973 0.1104  -0.2661 -0.2370 96  LEU   Z O   
44921 C  CB  . LEU   Z  96  ? 1.4479 0.5609 1.3461 0.1948  -0.2417 -0.1662 96  LEU   Z CB  
44922 C  CG  . LEU   Z  96  ? 1.4648 0.5088 1.3722 0.1672  -0.2304 -0.1671 96  LEU   Z CG  
44923 C  CD1 . LEU   Z  96  ? 1.4443 0.4821 1.3916 0.1578  -0.2059 -0.1868 96  LEU   Z CD1 
44924 C  CD2 . LEU   Z  96  ? 1.4446 0.4405 1.4065 0.1763  -0.2627 -0.1775 96  LEU   Z CD2 
44925 N  N   . LEU   Z  97  ? 1.4650 0.6986 1.1924 0.1606  -0.2472 -0.1319 97  LEU   Z N   
44926 C  CA  . LEU   Z  97  ? 1.4209 0.6967 1.1791 0.1611  -0.2498 -0.0856 97  LEU   Z CA  
44927 C  C   . LEU   Z  97  ? 1.3843 0.6929 1.1927 0.1181  -0.2131 -0.0711 97  LEU   Z C   
44928 O  O   . LEU   Z  97  ? 1.3053 0.8208 1.1457 0.0999  -0.2299 0.0265  97  LEU   Z O   
44929 C  CB  . LEU   Z  97  ? 1.4383 0.7045 1.1855 0.1414  -0.2276 -0.1222 97  LEU   Z CB  
44930 C  CG  . LEU   Z  97  ? 1.4281 0.7932 1.2360 0.1501  -0.2401 -0.1279 97  LEU   Z CG  
44931 C  CD1 . LEU   Z  97  ? 1.4149 0.8788 1.2011 0.1694  -0.1904 -0.1629 97  LEU   Z CD1 
44932 C  CD2 . LEU   Z  97  ? 1.4896 0.9387 1.1895 0.1389  -0.2279 -0.1211 97  LEU   Z CD2 
44933 N  N   . TYR   Z  98  ? 1.3338 0.6386 1.2264 0.0855  -0.1720 -0.1244 98  TYR   Z N   
44934 C  CA  . TYR   Z  98  ? 1.3290 0.6260 1.2513 0.0518  -0.1782 -0.1480 98  TYR   Z CA  
44935 C  C   . TYR   Z  98  ? 1.3725 0.5320 1.2691 0.0612  -0.1953 -0.1493 98  TYR   Z C   
44936 O  O   . TYR   Z  98  ? 1.3699 0.5066 1.2979 0.0252  -0.2237 -0.1488 98  TYR   Z O   
44937 C  CB  . TYR   Z  98  ? 1.3134 0.6307 1.2615 0.0322  -0.1693 -0.1723 98  TYR   Z CB  
44938 C  CG  . TYR   Z  98  ? 1.3017 0.6404 1.2504 -0.0138 -0.1833 -0.1567 98  TYR   Z CG  
44939 C  CD1 . TYR   Z  98  ? 1.3265 0.6807 1.2294 -0.0115 -0.1839 -0.1041 98  TYR   Z CD1 
44940 C  CD2 . TYR   Z  98  ? 1.3105 0.6426 1.2572 -0.0154 -0.2043 -0.1632 98  TYR   Z CD2 
44941 C  CE1 . TYR   Z  98  ? 1.2946 0.7322 1.2237 -0.0544 -0.2089 -0.1201 98  TYR   Z CE1 
44942 C  CE2 . TYR   Z  98  ? 1.2984 0.6692 1.2455 -0.0581 -0.2180 -0.1378 98  TYR   Z CE2 
44943 C  CZ  . TYR   Z  98  ? 1.3168 0.6935 1.2229 -0.0569 -0.2231 -0.1076 98  TYR   Z CZ  
44944 O  OH  . TYR   Z  98  ? 1.2808 0.7530 1.2390 -0.1081 -0.2562 -0.1248 98  TYR   Z OH  
44945 N  N   . GLY   Z  99  ? 1.4101 0.5185 1.2793 0.0729  -0.1949 -0.1591 99  GLY   Z N   
44946 C  CA  . GLY   Z  99  ? 1.4255 0.6132 1.2779 0.0388  -0.1848 -0.1459 99  GLY   Z CA  
44947 C  C   . GLY   Z  99  ? 1.4652 0.5994 1.2370 0.0467  -0.1916 -0.1321 99  GLY   Z C   
44948 O  O   . GLY   Z  99  ? 1.4363 0.7747 1.2100 0.0181  -0.2303 -0.1290 99  GLY   Z O   
44949 N  N   . LYS   Z  100 ? 1.5043 0.5297 1.2006 0.0758  -0.1811 -0.0822 100 LYS   Z N   
44950 C  CA  . LYS   Z  100 ? 1.5086 0.5464 1.1933 0.1018  -0.1834 -0.0628 100 LYS   Z CA  
44951 C  C   . LYS   Z  100 ? 1.5284 0.6094 1.1762 0.1121  -0.1976 -0.0210 100 LYS   Z C   
44952 O  O   . LYS   Z  100 ? 1.6287 0.5299 1.1930 0.1799  -0.1961 0.0328  100 LYS   Z O   
44953 C  CB  . LYS   Z  100 ? 1.4870 0.5359 1.2043 0.1170  -0.1982 -0.0336 100 LYS   Z CB  
44954 C  CG  . LYS   Z  100 ? 1.4586 0.5397 1.2101 0.1625  -0.2234 -0.0213 100 LYS   Z CG  
44955 C  CD  . LYS   Z  100 ? 1.4585 0.5791 1.2094 0.1844  -0.2275 -0.0165 100 LYS   Z CD  
44956 C  CE  . LYS   Z  100 ? 1.4803 0.6137 1.1451 0.1835  -0.2218 -0.0178 100 LYS   Z CE  
44957 N  NZ  . LYS   Z  100 ? 1.4733 0.7125 1.1223 0.1670  -0.2375 -0.0143 100 LYS   Z NZ  
44958 N  N   . ARG   Z  101 ? 1.4767 0.5648 1.1784 0.1006  -0.1895 -0.0679 101 ARG   Z N   
44959 C  CA  . ARG   Z  101 ? 1.4592 0.5354 1.1975 0.0878  -0.1763 -0.0672 101 ARG   Z CA  
44960 C  C   . ARG   Z  101 ? 1.4441 0.5653 1.1985 0.1063  -0.1624 -0.0249 101 ARG   Z C   
44961 O  O   . ARG   Z  101 ? 1.4484 0.5597 1.2342 0.2035  -0.1269 0.0102  101 ARG   Z O   
44962 C  CB  . ARG   Z  101 ? 1.4675 0.5510 1.2096 0.0572  -0.1881 -0.0600 101 ARG   Z CB  
44963 C  CG  . ARG   Z  101 ? 1.4606 0.6115 1.2090 0.0503  -0.1996 -0.0299 101 ARG   Z CG  
44964 C  CD  . ARG   Z  101 ? 1.4511 0.6545 1.1766 0.0319  -0.1685 -0.0267 101 ARG   Z CD  
44965 N  NE  . ARG   Z  101 ? 1.4470 0.6596 1.1658 0.0035  -0.1619 -0.0038 101 ARG   Z NE  
44966 C  CZ  . ARG   Z  101 ? 1.4099 0.7050 1.1319 -0.0121 -0.1336 0.0128  101 ARG   Z CZ  
44967 N  NH1 . ARG   Z  101 ? 1.3812 0.7496 1.1081 -0.0309 -0.1597 0.0088  101 ARG   Z NH1 
44968 N  NH2 . ARG   Z  101 ? 1.4475 0.7473 1.1747 0.0051  -0.1169 0.0612  101 ARG   Z NH2 
44969 N  N   . PHE   Z  102 ? 1.4208 0.5133 1.2162 0.1256  -0.1575 -0.0468 102 PHE   Z N   
44970 C  CA  . PHE   Z  102 ? 1.4338 0.5185 1.2629 0.1615  -0.1626 -0.0354 102 PHE   Z CA  
44971 C  C   . PHE   Z  102 ? 1.4590 0.5091 1.2740 0.1336  -0.1662 -0.0229 102 PHE   Z C   
44972 O  O   . PHE   Z  102 ? 1.4719 0.5998 1.3598 0.1106  -0.1076 -0.0095 102 PHE   Z O   
44973 C  CB  . PHE   Z  102 ? 1.4135 0.5685 1.2129 0.1941  -0.1864 -0.0575 102 PHE   Z CB  
44974 C  CG  . PHE   Z  102 ? 1.4660 0.6491 1.2102 0.2246  -0.1531 -0.0830 102 PHE   Z CG  
44975 C  CD1 . PHE   Z  102 ? 1.5149 0.6443 1.1801 0.1871  -0.1235 -0.0772 102 PHE   Z CD1 
44976 C  CD2 . PHE   Z  102 ? 1.4614 0.6586 1.2192 0.2569  -0.1551 -0.0849 102 PHE   Z CD2 
44977 C  CE1 . PHE   Z  102 ? 1.5405 0.7181 1.1781 0.1824  -0.1182 -0.0869 102 PHE   Z CE1 
44978 C  CE2 . PHE   Z  102 ? 1.4777 0.6801 1.2181 0.2513  -0.1592 -0.1091 102 PHE   Z CE2 
44979 C  CZ  . PHE   Z  102 ? 1.5208 0.7125 1.1766 0.2100  -0.1541 -0.0798 102 PHE   Z CZ  
44980 N  N   . PHE   Z  103 ? 1.4622 0.4797 1.3323 0.1241  -0.1828 -0.0090 103 PHE   Z N   
44981 C  CA  . PHE   Z  103 ? 1.4821 0.5493 1.3393 0.1263  -0.2170 0.0058  103 PHE   Z CA  
44982 C  C   . PHE   Z  103 ? 1.4712 0.5232 1.3658 0.1592  -0.2157 0.0325  103 PHE   Z C   
44983 O  O   . PHE   Z  103 ? 1.4306 0.5370 1.4224 0.2395  -0.1764 0.0065  103 PHE   Z O   
44984 C  CB  . PHE   Z  103 ? 1.5343 0.5517 1.3332 0.0761  -0.2219 -0.0145 103 PHE   Z CB  
44985 C  CG  . PHE   Z  103 ? 1.6091 0.6567 1.3364 0.0690  -0.2160 -0.0459 103 PHE   Z CG  
44986 C  CD1 . PHE   Z  103 ? 1.6995 0.6628 1.3202 0.0532  -0.1890 -0.0466 103 PHE   Z CD1 
44987 C  CD2 . PHE   Z  103 ? 1.6073 0.6715 1.3173 0.0606  -0.2315 -0.0505 103 PHE   Z CD2 
44988 C  CE1 . PHE   Z  103 ? 1.7420 0.7304 1.3140 0.0464  -0.1512 -0.0463 103 PHE   Z CE1 
44989 C  CE2 . PHE   Z  103 ? 1.6378 0.7099 1.3094 0.1045  -0.1915 -0.0441 103 PHE   Z CE2 
44990 C  CZ  . PHE   Z  103 ? 1.7143 0.7101 1.3198 0.0989  -0.1605 -0.0452 103 PHE   Z CZ  
44991 N  N   . PRO   Z  104 ? 1.4850 0.5039 1.3996 0.1119  -0.2515 0.0197  104 PRO   Z N   
44992 C  CA  . PRO   Z  104 ? 1.4835 0.5350 1.4126 0.1049  -0.2736 0.0180  104 PRO   Z CA  
44993 C  C   . PRO   Z  104 ? 1.4970 0.4886 1.4299 0.1405  -0.2939 0.0954  104 PRO   Z C   
44994 O  O   . PRO   Z  104 ? 1.5095 0.5653 1.4082 0.1513  -0.2430 0.1454  104 PRO   Z O   
44995 C  CB  . PRO   Z  104 ? 1.5094 0.5370 1.3964 0.1352  -0.2551 0.0123  104 PRO   Z CB  
44996 C  CG  . PRO   Z  104 ? 1.4963 0.5496 1.3941 0.1340  -0.2433 -0.0169 104 PRO   Z CG  
44997 C  CD  . PRO   Z  104 ? 1.4833 0.4842 1.4198 0.1195  -0.2473 -0.0092 104 PRO   Z CD  
44998 N  N   . TYR   Z  105 ? 1.5076 0.4492 1.4934 0.1672  -0.3331 0.1066  105 TYR   Z N   
44999 C  CA  . TYR   Z  105 ? 1.5852 0.5954 1.4344 0.1269  -0.3376 0.0390  105 TYR   Z CA  
45000 C  C   . TYR   Z  105 ? 1.5292 0.6088 1.3188 0.1308  -0.3348 0.0656  105 TYR   Z C   
45001 O  O   . TYR   Z  105 ? 1.4897 0.6072 1.3415 0.0957  -0.2910 0.0491  105 TYR   Z O   
45002 C  CB  . TYR   Z  105 ? 1.5975 0.6548 1.4299 0.1100  -0.3138 -0.0364 105 TYR   Z CB  
45003 C  CG  . TYR   Z  105 ? 1.7107 0.6230 1.3508 0.0613  -0.3409 -0.1288 105 TYR   Z CG  
45004 C  CD1 . TYR   Z  105 ? 1.7622 0.6472 1.3541 0.0285  -0.3745 -0.1188 105 TYR   Z CD1 
45005 C  CD2 . TYR   Z  105 ? 1.7316 0.6428 1.3646 0.0614  -0.3175 -0.1525 105 TYR   Z CD2 
45006 C  CE1 . TYR   Z  105 ? 1.7949 0.6062 1.3719 0.0024  -0.3615 -0.2194 105 TYR   Z CE1 
45007 C  CE2 . TYR   Z  105 ? 1.7861 0.6380 1.3701 0.0090  -0.3352 -0.1856 105 TYR   Z CE2 
45008 C  CZ  . TYR   Z  105 ? 1.7956 0.6594 1.3465 -0.0160 -0.3561 -0.2303 105 TYR   Z CZ  
45009 O  OH  . TYR   Z  105 ? 1.6722 0.6000 1.4418 -0.0297 -0.4124 -0.3405 105 TYR   Z OH  
45010 N  N   . TYR   Z  106 ? 1.5514 0.6676 1.2454 0.1462  -0.3865 0.0780  106 TYR   Z N   
45011 C  CA  . TYR   Z  106 ? 1.5273 0.6691 1.2209 0.1503  -0.4023 0.0817  106 TYR   Z CA  
45012 C  C   . TYR   Z  106 ? 1.5242 0.5872 1.1977 0.1140  -0.3731 0.0897  106 TYR   Z C   
45013 O  O   . TYR   Z  106 ? 1.4928 0.5284 1.2245 0.1129  -0.3877 0.1162  106 TYR   Z O   
45014 C  CB  . TYR   Z  106 ? 1.5669 0.7687 1.2460 0.2037  -0.3927 0.0570  106 TYR   Z CB  
45015 C  CG  . TYR   Z  106 ? 1.6583 0.8550 1.3258 0.3207  -0.3528 0.0770  106 TYR   Z CG  
45016 C  CD1 . TYR   Z  106 ? 1.6613 0.8928 1.4949 0.2853  -0.3224 0.0272  106 TYR   Z CD1 
45017 C  CD2 . TYR   Z  106 ? 1.7197 0.8567 1.3462 0.3392  -0.3535 0.0702  106 TYR   Z CD2 
45018 C  CE1 . TYR   Z  106 ? 1.7461 0.9227 1.6130 0.3910  -0.2485 0.0995  106 TYR   Z CE1 
45019 C  CE2 . TYR   Z  106 ? 1.7561 0.9298 1.5352 0.4426  -0.2933 0.0939  106 TYR   Z CE2 
45020 C  CZ  . TYR   Z  106 ? 1.6980 0.9249 1.6335 0.4592  -0.2878 0.1231  106 TYR   Z CZ  
45021 O  OH  . TYR   Z  106 ? 1.6440 1.3008 1.7458 0.5804  -0.2756 0.1540  106 TYR   Z OH  
45022 N  N   . VAL   Z  107 ? 1.5120 0.5000 1.1265 0.0686  -0.4173 0.0565  107 VAL   Z N   
45023 C  CA  . VAL   Z  107 ? 1.5194 0.5476 1.1589 0.0386  -0.3722 0.0313  107 VAL   Z CA  
45024 C  C   . VAL   Z  107 ? 1.5592 0.5446 1.1617 0.0669  -0.3672 0.0412  107 VAL   Z C   
45025 O  O   . VAL   Z  107 ? 1.4104 0.5555 1.2229 -0.0012 -0.3983 0.1406  107 VAL   Z O   
45026 C  CB  . VAL   Z  107 ? 1.5545 0.5457 1.2466 0.0575  -0.3547 0.0343  107 VAL   Z CB  
45027 C  CG1 . VAL   Z  107 ? 1.5952 0.5957 1.2724 0.0366  -0.3007 0.0101  107 VAL   Z CG1 
45028 C  CG2 . VAL   Z  107 ? 1.5686 0.6056 1.2294 0.0315  -0.3670 0.0157  107 VAL   Z CG2 
45029 N  N   . HIS   Z  108 ? 1.5894 0.6483 1.2141 0.0306  -0.3411 -0.0099 108 HIS   Z N   
45030 C  CA  . HIS   Z  108 ? 1.7315 0.8068 1.2145 0.0479  -0.2981 -0.0053 108 HIS   Z CA  
45031 C  C   . HIS   Z  108 ? 1.7566 0.7891 1.2116 0.0624  -0.2402 -0.0624 108 HIS   Z C   
45032 O  O   . HIS   Z  108 ? 1.7415 0.8947 1.2663 0.0696  -0.2732 0.0196  108 HIS   Z O   
45033 C  CB  . HIS   Z  108 ? 1.8611 0.8893 1.2768 -0.0771 -0.3000 0.0688  108 HIS   Z CB  
45034 C  CG  . HIS   Z  108 ? 2.0888 1.1218 1.2619 -0.1298 -0.2837 0.1714  108 HIS   Z CG  
45035 N  ND1 . HIS   Z  108 ? 2.2332 1.2012 1.3122 -0.2333 -0.2328 0.2132  108 HIS   Z ND1 
45036 C  CD2 . HIS   Z  108 ? 2.2423 1.0168 1.2649 -0.2993 -0.2210 0.0661  108 HIS   Z CD2 
45037 C  CE1 . HIS   Z  108 ? 2.3426 1.3684 1.2145 -0.2585 -0.1404 0.2307  108 HIS   Z CE1 
45038 N  NE2 . HIS   Z  108 ? 2.4259 1.2533 1.2838 -0.2866 -0.0851 0.2379  108 HIS   Z NE2 
45039 N  N   . THR   Z  109 ? 1.7145 0.7103 1.1898 0.1109  -0.2022 -0.0213 109 THR   Z N   
45040 C  CA  . THR   Z  109 ? 1.7156 0.5568 1.1525 0.0433  -0.1972 -0.0947 109 THR   Z CA  
45041 C  C   . THR   Z  109 ? 1.6180 0.4686 1.2109 0.0906  -0.2122 -0.0909 109 THR   Z C   
45042 O  O   . THR   Z  109 ? 1.7029 0.3572 1.2102 0.0939  -0.2027 -0.0920 109 THR   Z O   
45043 C  CB  . THR   Z  109 ? 1.7122 0.6099 1.1460 -0.0006 -0.2133 -0.0987 109 THR   Z CB  
45044 O  OG1 . THR   Z  109 ? 1.7155 0.4509 1.0338 -0.0411 -0.2318 -0.2176 109 THR   Z OG1 
45045 C  CG2 . THR   Z  109 ? 1.7201 0.6992 1.1804 0.0412  -0.2266 -0.0760 109 THR   Z CG2 
45046 N  N   . ILE   Z  110 ? 1.5778 0.5042 1.2158 0.1162  -0.1802 -0.0883 110 ILE   Z N   
45047 C  CA  . ILE   Z  110 ? 1.5363 0.5939 1.2704 0.1406  -0.1801 -0.0949 110 ILE   Z CA  
45048 C  C   . ILE   Z  110 ? 1.5082 0.6099 1.3011 0.1558  -0.1470 -0.1015 110 ILE   Z C   
45049 O  O   . ILE   Z  110 ? 1.4962 0.5702 1.2858 0.1902  -0.0690 -0.0967 110 ILE   Z O   
45050 C  CB  . ILE   Z  110 ? 1.4926 0.6264 1.3083 0.1216  -0.1632 -0.0742 110 ILE   Z CB  
45051 C  CG1 . ILE   Z  110 ? 1.4806 0.6894 1.3463 0.1527  -0.1767 -0.0544 110 ILE   Z CG1 
45052 C  CG2 . ILE   Z  110 ? 1.5051 0.6357 1.3140 0.1334  -0.1486 -0.0633 110 ILE   Z CG2 
45053 C  CD1 . ILE   Z  110 ? 1.5036 0.7048 1.4036 0.1361  -0.1700 -0.0604 110 ILE   Z CD1 
45054 N  N   . ILE   Z  111 ? 1.5056 0.6923 1.2903 0.1356  -0.1336 -0.1209 111 ILE   Z N   
45055 C  CA  . ILE   Z  111 ? 1.4832 0.6984 1.3027 0.1309  -0.1158 -0.1097 111 ILE   Z CA  
45056 C  C   . ILE   Z  111 ? 1.4436 0.6922 1.3740 0.1355  -0.1145 -0.0995 111 ILE   Z C   
45057 O  O   . ILE   Z  111 ? 1.4394 0.7689 1.3492 0.0333  -0.1096 -0.0861 111 ILE   Z O   
45058 C  CB  . ILE   Z  111 ? 1.5082 0.6614 1.2997 0.1718  -0.1070 -0.1203 111 ILE   Z CB  
45059 C  CG1 . ILE   Z  111 ? 1.5617 0.7071 1.3043 0.1854  -0.1077 -0.1426 111 ILE   Z CG1 
45060 C  CG2 . ILE   Z  111 ? 1.5019 0.6295 1.2665 0.1708  -0.1278 -0.1046 111 ILE   Z CG2 
45061 C  CD1 . ILE   Z  111 ? 1.5750 0.6928 1.3397 0.1904  -0.1094 -0.1321 111 ILE   Z CD1 
45062 N  N   . ALA   Z  112 ? 1.4618 0.6216 1.3932 0.1743  -0.0787 -0.0402 112 ALA   Z N   
45063 C  CA  . ALA   Z  112 ? 1.4972 0.6301 1.4288 0.2102  -0.0359 -0.0097 112 ALA   Z CA  
45064 C  C   . ALA   Z  112 ? 1.5192 0.5949 1.4413 0.1862  -0.0282 -0.0129 112 ALA   Z C   
45065 O  O   . ALA   Z  112 ? 1.5100 0.4922 1.4848 0.1774  -0.0209 -0.0440 112 ALA   Z O   
45066 C  CB  . ALA   Z  112 ? 1.5135 0.6148 1.4461 0.2229  -0.0390 -0.0157 112 ALA   Z CB  
45067 N  N   . GLY   Z  113 ? 1.5191 0.5590 1.4585 0.2229  -0.0238 0.0020  113 GLY   Z N   
45068 C  CA  . GLY   Z  113 ? 1.5577 0.5613 1.5241 0.2514  -0.0470 0.0424  113 GLY   Z CA  
45069 C  C   . GLY   Z  113 ? 1.5931 0.6264 1.5265 0.2718  -0.0407 0.0528  113 GLY   Z C   
45070 O  O   . GLY   Z  113 ? 1.5895 0.6326 1.5386 0.2977  -0.0497 0.0712  113 GLY   Z O   
45071 N  N   . LEU   Z  114 ? 1.6469 0.6462 1.5215 0.2632  -0.0422 0.0205  114 LEU   Z N   
45072 C  CA  . LEU   Z  114 ? 1.6946 0.6702 1.5526 0.2931  -0.0055 0.0138  114 LEU   Z CA  
45073 C  C   . LEU   Z  114 ? 1.7236 0.7282 1.5643 0.3093  -0.0426 0.0089  114 LEU   Z C   
45074 O  O   . LEU   Z  114 ? 1.7280 0.7416 1.6045 0.3491  -0.0022 0.0542  114 LEU   Z O   
45075 C  CB  . LEU   Z  114 ? 1.6827 0.6489 1.6013 0.2932  0.0341  -0.0259 114 LEU   Z CB  
45076 C  CG  . LEU   Z  114 ? 1.6627 0.6300 1.6415 0.2853  0.0462  -0.0483 114 LEU   Z CG  
45077 C  CD1 . LEU   Z  114 ? 1.6628 0.6055 1.6670 0.2784  0.0551  -0.0437 114 LEU   Z CD1 
45078 C  CD2 . LEU   Z  114 ? 1.6761 0.6575 1.6563 0.2844  0.0570  -0.0102 114 LEU   Z CD2 
45079 N  N   . ASP   Z  115 ? 1.7612 0.7932 1.5503 0.3006  -0.0454 -0.0058 115 ASP   Z N   
45080 C  CA  . ASP   Z  115 ? 1.7991 0.8573 1.5758 0.2914  -0.0664 -0.0496 115 ASP   Z CA  
45081 C  C   . ASP   Z  115 ? 1.7948 0.8346 1.6013 0.2594  -0.0491 -0.0654 115 ASP   Z C   
45082 O  O   . ASP   Z  115 ? 1.7151 0.8390 1.6383 0.2347  0.0080  -0.0645 115 ASP   Z O   
45083 C  CB  . ASP   Z  115 ? 1.8328 0.9075 1.5161 0.3195  -0.1323 -0.1028 115 ASP   Z CB  
45084 C  CG  . ASP   Z  115 ? 1.8338 0.9581 1.5503 0.3331  -0.1217 -0.1114 115 ASP   Z CG  
45085 O  OD1 . ASP   Z  115 ? 1.8691 1.0255 1.5916 0.3874  -0.1531 -0.1492 115 ASP   Z OD1 
45086 O  OD2 . ASP   Z  115 ? 1.9365 0.9090 1.5890 0.3666  -0.1480 -0.1142 115 ASP   Z OD2 
45087 N  N   . GLU   Z  116 ? 1.8329 0.9586 1.6099 0.1852  -0.0865 -0.0709 116 GLU   Z N   
45088 C  CA  . GLU   Z  116 ? 1.8944 1.0180 1.6453 0.2339  -0.0764 -0.0913 116 GLU   Z CA  
45089 C  C   . GLU   Z  116 ? 1.9173 0.9275 1.6398 0.2064  -0.0702 -0.0729 116 GLU   Z C   
45090 O  O   . GLU   Z  116 ? 1.9256 1.0316 1.6536 0.2807  -0.0678 -0.0646 116 GLU   Z O   
45091 C  CB  . GLU   Z  116 ? 1.9554 1.1831 1.6906 0.2186  -0.1605 -0.1262 116 GLU   Z CB  
45092 C  CG  . GLU   Z  116 ? 1.9910 1.2141 1.7128 0.2343  -0.1580 -0.0936 116 GLU   Z CG  
45093 C  CD  . GLU   Z  116 ? 2.0508 1.2484 1.8140 0.2313  -0.2167 -0.1522 116 GLU   Z CD  
45094 O  OE1 . GLU   Z  116 ? 2.0770 1.1730 1.9113 0.2903  -0.2860 -0.2589 116 GLU   Z OE1 
45095 O  OE2 . GLU   Z  116 ? 2.1577 1.4754 1.8582 0.3295  -0.2544 -0.0927 116 GLU   Z OE2 
45096 N  N   . ASP   Z  117 ? 1.9619 0.9081 1.6771 0.2074  -0.0497 -0.0826 117 ASP   Z N   
45097 C  CA  . ASP   Z  117 ? 2.0200 0.7800 1.7637 0.2088  -0.0009 -0.0003 117 ASP   Z CA  
45098 C  C   . ASP   Z  117 ? 1.9444 0.7656 1.8323 0.1909  0.0148  0.0174  117 ASP   Z C   
45099 O  O   . ASP   Z  117 ? 1.9395 0.7153 1.9117 0.2543  0.0404  0.0970  117 ASP   Z O   
45100 C  CB  . ASP   Z  117 ? 2.0772 0.7114 1.8058 0.1888  0.0325  0.0154  117 ASP   Z CB  
45101 C  CG  . ASP   Z  117 ? 2.1415 0.6917 1.7622 0.2100  0.0193  0.0488  117 ASP   Z CG  
45102 O  OD1 . ASP   Z  117 ? 2.2217 0.6987 1.8359 0.1197  0.0725  -0.0165 117 ASP   Z OD1 
45103 O  OD2 . ASP   Z  117 ? 2.2076 0.5087 1.8604 0.2485  0.0828  0.0557  117 ASP   Z OD2 
45104 N  N   . GLY   Z  118 ? 1.9348 0.8099 1.8571 0.1704  0.0512  0.0076  118 GLY   Z N   
45105 C  CA  . GLY   Z  118 ? 1.8948 0.8398 1.9004 0.1413  0.0631  -0.0129 118 GLY   Z CA  
45106 C  C   . GLY   Z  118 ? 1.8811 0.8460 1.9050 0.0953  0.0821  -0.0466 118 GLY   Z C   
45107 O  O   . GLY   Z  118 ? 1.8449 0.6820 1.9808 0.0496  0.0677  -0.0107 118 GLY   Z O   
45108 N  N   . LYS   Z  119 ? 1.8822 0.9410 1.8363 0.1063  0.0929  -0.0545 119 LYS   Z N   
45109 C  CA  . LYS   Z  119 ? 1.9066 0.9401 1.7595 0.0804  0.1211  -0.0443 119 LYS   Z CA  
45110 C  C   . LYS   Z  119 ? 1.9216 0.9033 1.7312 0.1099  0.0874  -0.0885 119 LYS   Z C   
45111 O  O   . LYS   Z  119 ? 1.8908 0.9052 1.7249 0.0849  0.0645  -0.2365 119 LYS   Z O   
45112 C  CB  . LYS   Z  119 ? 1.9515 1.0799 1.7324 0.0473  0.1232  -0.0254 119 LYS   Z CB  
45113 C  CG  . LYS   Z  119 ? 2.0260 1.2136 1.7011 0.0348  0.1437  -0.0222 119 LYS   Z CG  
45114 C  CD  . LYS   Z  119 ? 2.0978 1.3437 1.6384 0.0051  0.1460  -0.0121 119 LYS   Z CD  
45115 C  CE  . LYS   Z  119 ? 2.1575 1.3956 1.6275 -0.0189 0.1725  0.0331  119 LYS   Z CE  
45116 N  NZ  . LYS   Z  119 ? 2.2128 1.4077 1.6258 -0.0251 0.1656  0.0357  119 LYS   Z NZ  
45117 N  N   . GLY   Z  120 ? 1.9094 0.8592 1.6468 0.1846  0.1152  -0.0581 120 GLY   Z N   
45118 C  CA  . GLY   Z  120 ? 1.8433 0.7848 1.5687 0.1932  0.0324  -0.0549 120 GLY   Z CA  
45119 C  C   . GLY   Z  120 ? 1.8538 0.7050 1.4353 0.2112  0.0186  -0.0837 120 GLY   Z C   
45120 O  O   . GLY   Z  120 ? 1.8122 0.7662 1.3814 0.2149  -0.0233 -0.1475 120 GLY   Z O   
45121 N  N   . ALA   Z  121 ? 1.7527 0.5887 1.4123 0.2410  -0.0388 -0.0936 121 ALA   Z N   
45122 C  CA  . ALA   Z  121 ? 1.7547 0.5434 1.3926 0.2762  -0.0600 -0.0769 121 ALA   Z CA  
45123 C  C   . ALA   Z  121 ? 1.7005 0.5246 1.3883 0.2930  -0.0863 -0.0618 121 ALA   Z C   
45124 O  O   . ALA   Z  121 ? 1.6847 0.3728 1.4333 0.3523  -0.0855 -0.0345 121 ALA   Z O   
45125 C  CB  . ALA   Z  121 ? 1.7504 0.5803 1.3721 0.2397  -0.0617 -0.0899 121 ALA   Z CB  
45126 N  N   . VAL   Z  122 ? 1.6525 0.6825 1.4244 0.3294  -0.1219 -0.0666 122 VAL   Z N   
45127 C  CA  . VAL   Z  122 ? 1.6880 0.7309 1.4141 0.3038  -0.0972 -0.0838 122 VAL   Z CA  
45128 C  C   . VAL   Z  122 ? 1.6628 0.7162 1.3975 0.2697  -0.0537 -0.0515 122 VAL   Z C   
45129 O  O   . VAL   Z  122 ? 1.7752 0.7672 1.4315 0.3766  -0.0840 -0.0207 122 VAL   Z O   
45130 C  CB  . VAL   Z  122 ? 1.6901 0.7318 1.4594 0.3248  -0.1135 -0.1130 122 VAL   Z CB  
45131 C  CG1 . VAL   Z  122 ? 1.6811 0.7635 1.4692 0.3080  -0.1027 -0.1322 122 VAL   Z CG1 
45132 C  CG2 . VAL   Z  122 ? 1.6771 0.7486 1.5140 0.3540  -0.1253 -0.0993 122 VAL   Z CG2 
45133 N  N   . TYR   Z  123 ? 1.6703 0.6363 1.3951 0.2392  -0.0691 -0.0538 123 TYR   Z N   
45134 C  CA  . TYR   Z  123 ? 1.6539 0.6167 1.3586 0.2306  -0.0512 -0.0230 123 TYR   Z CA  
45135 C  C   . TYR   Z  123 ? 1.6195 0.5333 1.3451 0.1702  -0.0616 -0.0266 123 TYR   Z C   
45136 O  O   . TYR   Z  123 ? 1.5945 0.4661 1.3626 0.1785  -0.0564 0.0196  123 TYR   Z O   
45137 C  CB  . TYR   Z  123 ? 1.6549 0.6052 1.3479 0.2544  -0.0548 0.0113  123 TYR   Z CB  
45138 C  CG  . TYR   Z  123 ? 1.6878 0.6077 1.3444 0.3141  -0.0456 0.0418  123 TYR   Z CG  
45139 C  CD1 . TYR   Z  123 ? 1.7204 0.5617 1.3921 0.3464  -0.0386 0.0668  123 TYR   Z CD1 
45140 C  CD2 . TYR   Z  123 ? 1.7145 0.5763 1.3112 0.3331  -0.0526 0.0793  123 TYR   Z CD2 
45141 C  CE1 . TYR   Z  123 ? 1.7267 0.5690 1.3727 0.3585  -0.0398 0.0825  123 TYR   Z CE1 
45142 C  CE2 . TYR   Z  123 ? 1.7498 0.5269 1.2797 0.3494  -0.0605 0.1169  123 TYR   Z CE2 
45143 C  CZ  . TYR   Z  123 ? 1.7546 0.5662 1.3221 0.3572  -0.0319 0.1168  123 TYR   Z CZ  
45144 O  OH  . TYR   Z  123 ? 1.7719 0.6855 1.2641 0.3392  -0.0043 0.1362  123 TYR   Z OH  
45145 N  N   . SER   Z  124 ? 1.6156 0.5725 1.2991 0.1367  -0.1099 -0.0119 124 SER   Z N   
45146 C  CA  . SER   Z  124 ? 1.6105 0.6840 1.2630 0.1095  -0.0977 -0.0488 124 SER   Z CA  
45147 C  C   . SER   Z  124 ? 1.6181 0.6117 1.2503 0.0964  -0.0959 -0.0654 124 SER   Z C   
45148 O  O   . SER   Z  124 ? 1.6316 0.5057 1.2546 0.1239  -0.1228 -0.0142 124 SER   Z O   
45149 C  CB  . SER   Z  124 ? 1.6418 0.7078 1.2755 0.0559  -0.1017 -0.0456 124 SER   Z CB  
45150 O  OG  . SER   Z  124 ? 1.7141 0.8321 1.2726 0.0474  -0.1358 -0.0422 124 SER   Z OG  
45151 N  N   . PHE   Z  125 ? 1.5533 0.5995 1.2575 0.0859  -0.1081 -0.1153 125 PHE   Z N   
45152 C  CA  . PHE   Z  125 ? 1.5295 0.6462 1.2718 0.1165  -0.1184 -0.1625 125 PHE   Z CA  
45153 C  C   . PHE   Z  125 ? 1.4952 0.6897 1.3089 0.1439  -0.1233 -0.1623 125 PHE   Z C   
45154 O  O   . PHE   Z  125 ? 1.4646 0.8508 1.3569 0.1948  -0.1471 -0.2370 125 PHE   Z O   
45155 C  CB  . PHE   Z  125 ? 1.4920 0.6719 1.2937 0.0694  -0.1130 -0.1596 125 PHE   Z CB  
45156 C  CG  . PHE   Z  125 ? 1.4651 0.7002 1.3124 0.0769  -0.1229 -0.1829 125 PHE   Z CG  
45157 C  CD1 . PHE   Z  125 ? 1.4591 0.7066 1.3549 0.0925  -0.1215 -0.1893 125 PHE   Z CD1 
45158 C  CD2 . PHE   Z  125 ? 1.4598 0.6548 1.3307 0.0740  -0.1250 -0.1563 125 PHE   Z CD2 
45159 C  CE1 . PHE   Z  125 ? 1.4578 0.7118 1.3866 0.0830  -0.1104 -0.2058 125 PHE   Z CE1 
45160 C  CE2 . PHE   Z  125 ? 1.4545 0.6601 1.3568 0.0631  -0.1159 -0.1818 125 PHE   Z CE2 
45161 C  CZ  . PHE   Z  125 ? 1.4453 0.7089 1.3887 0.0695  -0.1010 -0.2007 125 PHE   Z CZ  
45162 N  N   . ASP   Z  126 ? 1.5006 0.7099 1.2344 0.1222  -0.1337 -0.2282 126 ASP   Z N   
45163 C  CA  . ASP   Z  126 ? 1.5412 0.6774 1.2685 0.1195  -0.1148 -0.2519 126 ASP   Z CA  
45164 C  C   . ASP   Z  126 ? 1.5159 0.6012 1.2132 0.1608  -0.1552 -0.2630 126 ASP   Z C   
45165 O  O   . ASP   Z  126 ? 1.4492 0.5595 1.1745 0.1335  -0.1206 -0.3502 126 ASP   Z O   
45166 C  CB  . ASP   Z  126 ? 1.5653 0.6181 1.3259 0.1504  -0.1031 -0.2428 126 ASP   Z CB  
45167 C  CG  . ASP   Z  126 ? 1.5999 0.6739 1.4015 0.0979  -0.0817 -0.2659 126 ASP   Z CG  
45168 O  OD1 . ASP   Z  126 ? 1.6682 0.6815 1.5456 0.0785  -0.0478 -0.2194 126 ASP   Z OD1 
45169 O  OD2 . ASP   Z  126 ? 1.6543 0.4157 1.3600 0.1291  -0.0235 -0.2524 126 ASP   Z OD2 
45170 N  N   . PRO   Z  127 ? 1.5103 0.6606 1.1922 0.1971  -0.1642 -0.2229 127 PRO   Z N   
45171 C  CA  . PRO   Z  127 ? 1.5149 0.6098 1.1938 0.2100  -0.2048 -0.1923 127 PRO   Z CA  
45172 C  C   . PRO   Z  127 ? 1.5185 0.5892 1.1586 0.2319  -0.2369 -0.1781 127 PRO   Z C   
45173 O  O   . PRO   Z  127 ? 1.4826 0.4564 1.1369 0.3157  -0.2536 -0.2446 127 PRO   Z O   
45174 C  CB  . PRO   Z  127 ? 1.5105 0.6410 1.1873 0.2395  -0.2177 -0.1881 127 PRO   Z CB  
45175 C  CG  . PRO   Z  127 ? 1.5279 0.6995 1.1971 0.1976  -0.1899 -0.1847 127 PRO   Z CG  
45176 C  CD  . PRO   Z  127 ? 1.5370 0.6798 1.2156 0.2301  -0.1738 -0.1998 127 PRO   Z CD  
45177 N  N   . VAL   Z  128 ? 1.5087 0.5526 1.1428 0.2495  -0.2161 -0.0734 128 VAL   Z N   
45178 C  CA  . VAL   Z  128 ? 1.4660 0.5445 1.1936 0.2366  -0.2345 -0.0074 128 VAL   Z CA  
45179 C  C   . VAL   Z  128 ? 1.4892 0.5720 1.1643 0.2257  -0.2276 0.0000  128 VAL   Z C   
45180 O  O   . VAL   Z  128 ? 1.4648 0.6569 1.1121 0.2301  -0.2996 0.0098  128 VAL   Z O   
45181 C  CB  . VAL   Z  128 ? 1.4621 0.5909 1.2092 0.2659  -0.2120 0.0094  128 VAL   Z CB  
45182 C  CG1 . VAL   Z  128 ? 1.4381 0.5341 1.2004 0.2635  -0.2209 0.0734  128 VAL   Z CG1 
45183 C  CG2 . VAL   Z  128 ? 1.4677 0.6066 1.2339 0.2510  -0.2020 0.0174  128 VAL   Z CG2 
45184 N  N   . GLY   Z  129 ? 1.5087 0.5692 1.1800 0.2315  -0.1583 0.0332  129 GLY   Z N   
45185 C  CA  . GLY   Z  129 ? 1.5855 0.5474 1.1179 0.2074  -0.1459 -0.0072 129 GLY   Z CA  
45186 C  C   . GLY   Z  129 ? 1.6483 0.5315 1.1116 0.2040  -0.1462 -0.0088 129 GLY   Z C   
45187 O  O   . GLY   Z  129 ? 1.7005 0.5357 1.0836 0.2051  -0.1335 0.0034  129 GLY   Z O   
45188 N  N   . SER   Z  130 ? 1.6472 0.5091 1.0980 0.1974  -0.1166 -0.0336 130 SER   Z N   
45189 C  CA  . SER   Z  130 ? 1.6674 0.5166 1.1410 0.1802  -0.0919 -0.0157 130 SER   Z CA  
45190 C  C   . SER   Z  130 ? 1.6726 0.3524 1.1835 0.1797  -0.0943 -0.0094 130 SER   Z C   
45191 O  O   . SER   Z  130 ? 1.6756 0.3160 1.2029 0.1296  -0.0791 0.0030  130 SER   Z O   
45192 C  CB  . SER   Z  130 ? 1.6075 0.5962 1.1534 0.2253  -0.0843 0.0234  130 SER   Z CB  
45193 O  OG  . SER   Z  130 ? 1.6256 0.6846 1.2096 0.2140  -0.0251 0.0734  130 SER   Z OG  
45194 N  N   . TYR   Z  131 ? 1.7104 0.3382 1.1833 0.1985  -0.1041 -0.0208 131 TYR   Z N   
45195 C  CA  . TYR   Z  131 ? 1.7113 0.4735 1.2279 0.1506  -0.1001 -0.0253 131 TYR   Z CA  
45196 C  C   . TYR   Z  131 ? 1.7516 0.4106 1.2830 0.1438  -0.0627 0.0301  131 TYR   Z C   
45197 O  O   . TYR   Z  131 ? 1.7581 0.4971 1.3249 0.1016  -0.0911 0.0536  131 TYR   Z O   
45198 C  CB  . TYR   Z  131 ? 1.7235 0.5231 1.2373 0.1781  -0.1332 -0.0097 131 TYR   Z CB  
45199 C  CG  . TYR   Z  131 ? 1.7712 0.5518 1.2664 0.1562  -0.1195 -0.0439 131 TYR   Z CG  
45200 C  CD1 . TYR   Z  131 ? 1.7488 0.5937 1.2534 0.1506  -0.1421 -0.0138 131 TYR   Z CD1 
45201 C  CD2 . TYR   Z  131 ? 1.8120 0.6228 1.2933 0.1464  -0.0754 -0.0377 131 TYR   Z CD2 
45202 C  CE1 . TYR   Z  131 ? 1.8044 0.6606 1.2494 0.1472  -0.1407 -0.0507 131 TYR   Z CE1 
45203 C  CE2 . TYR   Z  131 ? 1.8609 0.6479 1.2854 0.1254  -0.0799 -0.0496 131 TYR   Z CE2 
45204 C  CZ  . TYR   Z  131 ? 1.8463 0.6824 1.2567 0.1278  -0.1067 -0.0727 131 TYR   Z CZ  
45205 O  OH  . TYR   Z  131 ? 1.9093 0.6573 1.2430 0.0628  -0.1214 -0.0691 131 TYR   Z OH  
45206 N  N   . GLU   Z  132 ? 1.7412 0.4697 1.3019 0.1436  -0.0351 0.0336  132 GLU   Z N   
45207 C  CA  . GLU   Z  132 ? 1.7447 0.6749 1.3766 0.1661  0.0589  0.0215  132 GLU   Z CA  
45208 C  C   . GLU   Z  132 ? 1.7315 0.7626 1.4062 0.1962  0.0614  0.0142  132 GLU   Z C   
45209 O  O   . GLU   Z  132 ? 1.6260 0.7888 1.3682 0.2378  0.1301  0.0205  132 GLU   Z O   
45210 C  CB  . GLU   Z  132 ? 1.8362 0.6936 1.4070 0.1934  0.1293  0.0744  132 GLU   Z CB  
45211 C  CG  . GLU   Z  132 ? 1.9516 0.8237 1.4023 0.2260  0.1608  0.1486  132 GLU   Z CG  
45212 C  CD  . GLU   Z  132 ? 2.0465 0.8301 1.4375 0.2321  0.1639  0.3087  132 GLU   Z CD  
45213 O  OE1 . GLU   Z  132 ? 2.0855 0.7996 1.4637 0.2162  0.1739  0.3110  132 GLU   Z OE1 
45214 O  OE2 . GLU   Z  132 ? 2.1795 0.8816 1.4170 0.1761  0.2198  0.2895  132 GLU   Z OE2 
45215 N  N   . ARG   Z  133 ? 1.7010 0.8263 1.5024 0.2207  0.0639  -0.0175 133 ARG   Z N   
45216 C  CA  . ARG   Z  133 ? 1.7235 0.8851 1.5507 0.2126  0.0185  -0.0473 133 ARG   Z CA  
45217 C  C   . ARG   Z  133 ? 1.7574 0.9256 1.6507 0.1696  0.0037  -0.0180 133 ARG   Z C   
45218 O  O   . ARG   Z  133 ? 1.8373 0.8470 1.6826 0.1378  -0.0435 -0.0169 133 ARG   Z O   
45219 C  CB  . ARG   Z  133 ? 1.7230 0.8315 1.5057 0.1721  0.0071  -0.0517 133 ARG   Z CB  
45220 C  CG  . ARG   Z  133 ? 1.7055 0.8366 1.4841 0.1712  0.0273  -0.0474 133 ARG   Z CG  
45221 C  CD  . ARG   Z  133 ? 1.6906 0.8389 1.4762 0.1711  0.0227  -0.0458 133 ARG   Z CD  
45222 N  NE  . ARG   Z  133 ? 1.6705 0.8110 1.5000 0.1916  0.0505  -0.0256 133 ARG   Z NE  
45223 C  CZ  . ARG   Z  133 ? 1.6999 0.8150 1.4795 0.1859  0.0672  -0.0363 133 ARG   Z CZ  
45224 N  NH1 . ARG   Z  133 ? 1.7129 0.8947 1.4122 0.1860  0.0509  -0.0253 133 ARG   Z NH1 
45225 N  NH2 . ARG   Z  133 ? 1.6964 0.8295 1.5428 0.1596  0.0739  -0.0223 133 ARG   Z NH2 
45226 N  N   . GLU   Z  134 ? 1.7472 1.0588 1.7099 0.1755  -0.0115 -0.0690 134 GLU   Z N   
45227 C  CA  . GLU   Z  134 ? 1.7284 1.0501 1.7426 0.1993  0.0289  -0.1089 134 GLU   Z CA  
45228 C  C   . GLU   Z  134 ? 1.7294 1.1503 1.6958 0.1494  0.0219  -0.1746 134 GLU   Z C   
45229 O  O   . GLU   Z  134 ? 1.7739 1.3079 1.5362 0.0833  -0.0326 -0.1318 134 GLU   Z O   
45230 C  CB  . GLU   Z  134 ? 1.7743 1.1042 1.7816 0.2117  0.0553  -0.1519 134 GLU   Z CB  
45231 C  CG  . GLU   Z  134 ? 1.7822 1.1352 1.8235 0.2050  0.0417  -0.1242 134 GLU   Z CG  
45232 C  CD  . GLU   Z  134 ? 1.7304 1.0856 1.7998 0.1916  0.0700  -0.0266 134 GLU   Z CD  
45233 O  OE1 . GLU   Z  134 ? 1.8102 1.1749 1.9160 0.3528  0.0750  0.0587  134 GLU   Z OE1 
45234 O  OE2 . GLU   Z  134 ? 1.5852 1.0585 1.8345 0.0845  0.0215  -0.0398 134 GLU   Z OE2 
45235 N  N   . GLN   Z  135 ? 1.6812 1.0510 1.6990 0.1693  0.0020  -0.2573 135 GLN   Z N   
45236 C  CA  . GLN   Z  135 ? 1.6705 1.0696 1.7931 0.1035  0.0336  -0.3138 135 GLN   Z CA  
45237 C  C   . GLN   Z  135 ? 1.5981 0.9459 1.7946 0.0867  0.0897  -0.2744 135 GLN   Z C   
45238 O  O   . GLN   Z  135 ? 1.4645 1.1370 1.8584 0.0355  0.1392  -0.2884 135 GLN   Z O   
45239 C  CB  . GLN   Z  135 ? 1.7277 1.1417 1.8967 0.0619  0.0239  -0.2673 135 GLN   Z CB  
45240 C  CG  . GLN   Z  135 ? 1.8892 1.2995 1.9406 0.0300  0.0398  -0.3716 135 GLN   Z CG  
45241 C  CD  . GLN   Z  135 ? 1.9099 1.4403 2.0893 0.0501  -0.0454 -0.3854 135 GLN   Z CD  
45242 O  OE1 . GLN   Z  135 ? 2.1234 1.5700 2.0731 0.0984  0.0317  -0.5058 135 GLN   Z OE1 
45243 N  NE2 . GLN   Z  135 ? 1.9774 1.4826 2.1908 -0.0076 -0.0751 -0.4399 135 GLN   Z NE2 
45244 N  N   . CYS   Z  136 ? 1.6235 0.7608 1.7414 0.0813  0.0684  -0.2473 136 CYS   Z N   
45245 C  CA  . CYS   Z  136 ? 1.6388 0.7415 1.7246 0.0019  0.0517  -0.2510 136 CYS   Z CA  
45246 C  C   . CYS   Z  136 ? 1.6176 0.5623 1.5618 0.0177  0.0136  -0.2413 136 CYS   Z C   
45247 O  O   . CYS   Z  136 ? 1.5489 0.4820 1.5627 0.0170  0.0425  -0.2608 136 CYS   Z O   
45248 C  CB  . CYS   Z  136 ? 1.7548 0.6941 1.7764 -0.0165 0.0871  -0.3061 136 CYS   Z CB  
45249 S  SG  . CYS   Z  136 ? 1.8359 0.6881 1.8820 -0.0169 0.1331  -0.4403 136 CYS   Z SG  
45250 N  N   . ARG   Z  137 ? 1.5589 0.4988 1.5572 0.0465  0.0111  -0.2292 137 ARG   Z N   
45251 C  CA  . ARG   Z  137 ? 1.5472 0.5011 1.5602 0.0885  -0.0178 -0.2117 137 ARG   Z CA  
45252 C  C   . ARG   Z  137 ? 1.5655 0.5012 1.5594 0.0529  -0.0201 -0.1882 137 ARG   Z C   
45253 O  O   . ARG   Z  137 ? 1.5544 0.6106 1.5693 0.0857  -0.0164 -0.1647 137 ARG   Z O   
45254 C  CB  . ARG   Z  137 ? 1.5131 0.5679 1.5277 0.0713  -0.0422 -0.2385 137 ARG   Z CB  
45255 C  CG  . ARG   Z  137 ? 1.5058 0.5896 1.5035 0.1273  -0.0668 -0.2417 137 ARG   Z CG  
45256 C  CD  . ARG   Z  137 ? 1.4758 0.6048 1.5050 0.1366  -0.0602 -0.2458 137 ARG   Z CD  
45257 N  NE  . ARG   Z  137 ? 1.5038 0.7472 1.5141 0.1340  -0.0689 -0.2732 137 ARG   Z NE  
45258 C  CZ  . ARG   Z  137 ? 1.4854 0.8532 1.5280 0.1424  -0.1114 -0.2595 137 ARG   Z CZ  
45259 N  NH1 . ARG   Z  137 ? 1.4049 0.8460 1.5775 0.0891  -0.1110 -0.2686 137 ARG   Z NH1 
45260 N  NH2 . ARG   Z  137 ? 1.5388 1.0476 1.5305 0.1620  -0.1122 -0.2922 137 ARG   Z NH2 
45261 N  N   . ALA   Z  138 ? 1.5180 0.5362 1.5397 0.0638  -0.0067 -0.1745 138 ALA   Z N   
45262 C  CA  . ALA   Z  138 ? 1.4458 0.5935 1.5116 0.0115  -0.0123 -0.1437 138 ALA   Z CA  
45263 C  C   . ALA   Z  138 ? 1.4332 0.5627 1.4462 -0.0068 -0.0551 -0.1342 138 ALA   Z C   
45264 O  O   . ALA   Z  138 ? 1.3673 0.6220 1.4726 -0.0487 -0.0487 -0.1231 138 ALA   Z O   
45265 C  CB  . ALA   Z  138 ? 1.4591 0.5863 1.5498 0.0593  0.0053  -0.1862 138 ALA   Z CB  
45266 N  N   . GLY   Z  139 ? 1.4372 0.5731 1.4244 -0.0286 -0.0592 -0.1678 139 GLY   Z N   
45267 C  CA  . GLY   Z  139 ? 1.4458 0.6115 1.4157 -0.0197 -0.0390 -0.1949 139 GLY   Z CA  
45268 C  C   . GLY   Z  139 ? 1.4430 0.6351 1.4394 0.0155  -0.0185 -0.2134 139 GLY   Z C   
45269 O  O   . GLY   Z  139 ? 1.3997 0.6932 1.5054 -0.0392 -0.0020 -0.2283 139 GLY   Z O   
45270 N  N   . GLY   Z  140 ? 1.4489 0.6542 1.4459 0.0857  -0.0487 -0.1993 140 GLY   Z N   
45271 C  CA  . GLY   Z  140 ? 1.4642 0.7357 1.3924 0.0677  -0.0982 -0.1723 140 GLY   Z CA  
45272 C  C   . GLY   Z  140 ? 1.4931 0.7111 1.3278 -0.0059 -0.1503 -0.1547 140 GLY   Z C   
45273 O  O   . GLY   Z  140 ? 1.4412 0.6777 1.3218 -0.1017 -0.1409 -0.1551 140 GLY   Z O   
45274 N  N   . ALA   Z  141 ? 1.5267 0.7101 1.3445 -0.0275 -0.1676 -0.1749 141 ALA   Z N   
45275 C  CA  . ALA   Z  141 ? 1.5185 0.7125 1.3849 0.0119  -0.1651 -0.1329 141 ALA   Z CA  
45276 C  C   . ALA   Z  141 ? 1.4612 0.7335 1.3654 0.0355  -0.1681 -0.1247 141 ALA   Z C   
45277 O  O   . ALA   Z  141 ? 1.5286 0.7789 1.3644 0.0371  -0.2552 -0.0948 141 ALA   Z O   
45278 C  CB  . ALA   Z  141 ? 1.5515 0.6824 1.3858 -0.0084 -0.1489 -0.1339 141 ALA   Z CB  
45279 N  N   . ALA   Z  142 ? 1.4622 0.7469 1.3727 -0.0069 -0.1061 -0.1611 142 ALA   Z N   
45280 C  CA  . ALA   Z  142 ? 1.4491 0.6532 1.3953 0.0009  -0.1366 -0.1911 142 ALA   Z CA  
45281 C  C   . ALA   Z  142 ? 1.4608 0.6612 1.3748 -0.0005 -0.1167 -0.1217 142 ALA   Z C   
45282 O  O   . ALA   Z  142 ? 1.5088 0.4604 1.4676 -0.0605 -0.1990 -0.0876 142 ALA   Z O   
45283 C  CB  . ALA   Z  142 ? 1.4238 0.6086 1.4164 -0.0316 -0.1179 -0.2159 142 ALA   Z CB  
45284 N  N   . ALA   Z  143 ? 1.4860 0.7403 1.3495 0.0467  -0.1591 -0.1917 143 ALA   Z N   
45285 C  CA  . ALA   Z  143 ? 1.4938 0.7528 1.3568 0.1113  -0.1155 -0.1741 143 ALA   Z CA  
45286 C  C   . ALA   Z  143 ? 1.4692 0.7030 1.3331 0.1458  -0.0642 -0.2037 143 ALA   Z C   
45287 O  O   . ALA   Z  143 ? 1.3966 0.4513 1.3439 0.2470  -0.0635 -0.2511 143 ALA   Z O   
45288 C  CB  . ALA   Z  143 ? 1.4826 0.8693 1.3244 0.0797  -0.1388 -0.1992 143 ALA   Z CB  
45289 N  N   . SER   Z  144 ? 1.4808 0.6935 1.3638 0.1625  -0.0928 -0.1448 144 SER   Z N   
45290 C  CA  . SER   Z  144 ? 1.5153 0.7199 1.3394 0.1068  -0.0552 -0.1160 144 SER   Z CA  
45291 C  C   . SER   Z  144 ? 1.5301 0.6771 1.3703 0.1178  -0.0725 -0.1034 144 SER   Z C   
45292 O  O   . SER   Z  144 ? 1.5909 0.6270 1.3827 0.1427  -0.0067 -0.1365 144 SER   Z O   
45293 C  CB  . SER   Z  144 ? 1.4901 0.7668 1.3000 0.0707  -0.0363 -0.1711 144 SER   Z CB  
45294 O  OG  . SER   Z  144 ? 1.4786 0.7649 1.3383 -0.0187 -0.0299 -0.2230 144 SER   Z OG  
45295 N  N   . LEU   Z  145 ? 1.5581 0.6144 1.3703 0.1379  -0.0804 -0.0352 145 LEU   Z N   
45296 C  CA  . LEU   Z  145 ? 1.5916 0.5813 1.4146 0.1121  -0.0637 0.0069  145 LEU   Z CA  
45297 C  C   . LEU   Z  145 ? 1.6019 0.6133 1.3983 0.0830  -0.0162 0.0350  145 LEU   Z C   
45298 O  O   . LEU   Z  145 ? 1.6679 0.4228 1.4288 0.0607  -0.0213 -0.0364 145 LEU   Z O   
45299 C  CB  . LEU   Z  145 ? 1.5724 0.6106 1.4249 0.1184  -0.0871 0.0125  145 LEU   Z CB  
45300 C  CG  . LEU   Z  145 ? 1.5475 0.6054 1.4581 0.1342  -0.1239 0.0030  145 LEU   Z CG  
45301 C  CD1 . LEU   Z  145 ? 1.5383 0.6792 1.4820 0.1420  -0.1228 0.0305  145 LEU   Z CD1 
45302 C  CD2 . LEU   Z  145 ? 1.5214 0.5377 1.5174 0.1235  -0.1358 -0.0440 145 LEU   Z CD2 
45303 N  N   . ILE   Z  146 ? 1.6274 0.6338 1.4471 0.1498  -0.0434 0.0096  146 ILE   Z N   
45304 C  CA  . ILE   Z  146 ? 1.5610 0.7661 1.4670 0.1004  -0.0349 -0.0246 146 ILE   Z CA  
45305 C  C   . ILE   Z  146 ? 1.5018 0.7608 1.4681 0.0417  -0.0044 -0.0323 146 ILE   Z C   
45306 O  O   . ILE   Z  146 ? 1.4902 0.6724 1.4747 -0.0407 -0.0180 -0.0589 146 ILE   Z O   
45307 C  CB  . ILE   Z  146 ? 1.6006 0.7704 1.4964 0.1181  -0.0433 -0.0136 146 ILE   Z CB  
45308 C  CG1 . ILE   Z  146 ? 1.6487 0.8567 1.5007 0.1004  -0.0567 -0.0051 146 ILE   Z CG1 
45309 C  CG2 . ILE   Z  146 ? 1.6205 0.7308 1.4718 0.1300  -0.0320 0.0006  146 ILE   Z CG2 
45310 C  CD1 . ILE   Z  146 ? 1.6572 0.8754 1.5176 0.1018  -0.0448 0.0062  146 ILE   Z CD1 
45311 N  N   . MET   Z  147 ? 1.5645 0.7915 1.4919 0.0491  -0.0792 -0.0304 147 MET   Z N   
45312 C  CA  . MET   Z  147 ? 1.5765 0.8300 1.4834 0.0542  -0.0710 -0.0227 147 MET   Z CA  
45313 C  C   . MET   Z  147 ? 1.5690 0.8002 1.5566 0.0725  -0.0556 0.0039  147 MET   Z C   
45314 O  O   . MET   Z  147 ? 1.5066 0.6411 1.6019 0.0770  -0.0361 0.0766  147 MET   Z O   
45315 C  CB  . MET   Z  147 ? 1.6006 0.8218 1.5032 0.0422  -0.1108 -0.0305 147 MET   Z CB  
45316 C  CG  . MET   Z  147 ? 1.5848 0.7131 1.5660 0.0751  -0.1519 -0.0315 147 MET   Z CG  
45317 S  SD  . MET   Z  147 ? 1.6922 0.5238 1.6514 -0.0127 -0.1991 -0.0010 147 MET   Z SD  
45318 C  CE  . MET   Z  147 ? 1.7170 0.6542 1.6322 0.0352  -0.1643 0.0268  147 MET   Z CE  
45319 N  N   . PRO   Z  148 ? 1.5898 0.8079 1.5652 0.0633  -0.0753 -0.0185 148 PRO   Z N   
45320 C  CA  . PRO   Z  148 ? 1.6021 0.8659 1.5676 0.0288  -0.0691 -0.0095 148 PRO   Z CA  
45321 C  C   . PRO   Z  148 ? 1.6112 0.8253 1.6719 0.0361  -0.1190 -0.0243 148 PRO   Z C   
45322 O  O   . PRO   Z  148 ? 1.7139 0.8276 1.6942 0.0191  -0.1124 0.0373  148 PRO   Z O   
45323 C  CB  . PRO   Z  148 ? 1.5883 0.8073 1.5309 -0.0127 -0.0908 -0.0058 148 PRO   Z CB  
45324 C  CG  . PRO   Z  148 ? 1.5889 0.8765 1.5120 -0.0193 -0.1022 -0.0506 148 PRO   Z CG  
45325 C  CD  . PRO   Z  148 ? 1.6151 0.8762 1.5152 0.0083  -0.0784 -0.0602 148 PRO   Z CD  
45326 N  N   . PHE   Z  149 ? 1.6641 0.7164 1.6742 0.0677  -0.1345 -0.0525 149 PHE   Z N   
45327 C  CA  . PHE   Z  149 ? 1.6597 0.6230 1.7756 0.0422  -0.1147 -0.0141 149 PHE   Z CA  
45328 C  C   . PHE   Z  149 ? 1.6641 0.7039 1.6605 0.0389  -0.0590 -0.0138 149 PHE   Z C   
45329 O  O   . PHE   Z  149 ? 1.6793 0.6476 1.5787 -0.0461 -0.0790 0.0077  149 PHE   Z O   
45330 C  CB  . PHE   Z  149 ? 1.6159 0.5259 1.8026 0.0628  -0.1475 0.0093  149 PHE   Z CB  
45331 C  CG  . PHE   Z  149 ? 1.5996 0.5524 1.9237 0.0568  -0.1337 0.0329  149 PHE   Z CG  
45332 C  CD1 . PHE   Z  149 ? 1.5802 0.5338 1.9840 0.0978  -0.1175 0.0734  149 PHE   Z CD1 
45333 C  CD2 . PHE   Z  149 ? 1.5899 0.5778 1.9304 0.0223  -0.1484 0.0735  149 PHE   Z CD2 
45334 C  CE1 . PHE   Z  149 ? 1.5803 0.6494 2.0434 0.0843  -0.1190 0.0582  149 PHE   Z CE1 
45335 C  CE2 . PHE   Z  149 ? 1.5848 0.6084 1.9797 0.0091  -0.1393 0.0783  149 PHE   Z CE2 
45336 C  CZ  . PHE   Z  149 ? 1.5796 0.6303 2.0303 0.0148  -0.1073 0.0918  149 PHE   Z CZ  
45337 N  N   . LEU   Z  150 ? 1.7807 0.6869 1.6611 0.0221  -0.0550 -0.0590 150 LEU   Z N   
45338 C  CA  . LEU   Z  150 ? 1.7808 0.7341 1.6681 0.0423  0.0107  -0.0736 150 LEU   Z CA  
45339 C  C   . LEU   Z  150 ? 1.6982 0.7944 1.6705 0.0423  0.0659  -0.0394 150 LEU   Z C   
45340 O  O   . LEU   Z  150 ? 1.6319 0.8267 1.7678 -0.0012 0.1122  0.0569  150 LEU   Z O   
45341 C  CB  . LEU   Z  150 ? 1.8681 0.6242 1.6300 0.0878  0.0120  -0.0825 150 LEU   Z CB  
45342 C  CG  . LEU   Z  150 ? 1.9282 0.5602 1.6382 0.0818  0.0060  -0.0945 150 LEU   Z CG  
45343 C  CD1 . LEU   Z  150 ? 1.9479 0.4398 1.6872 0.0634  0.0293  -0.1004 150 LEU   Z CD1 
45344 C  CD2 . LEU   Z  150 ? 1.9282 0.6873 1.6393 0.0784  0.0343  -0.1029 150 LEU   Z CD2 
45345 N  N   . ASP   Z  151 ? 1.6932 0.8838 1.6615 0.0461  0.0531  -0.0421 151 ASP   Z N   
45346 C  CA  . ASP   Z  151 ? 1.6870 1.0117 1.6696 0.0871  0.0556  -0.0218 151 ASP   Z CA  
45347 C  C   . ASP   Z  151 ? 1.6563 1.0576 1.7470 0.0833  0.0191  0.0249  151 ASP   Z C   
45348 O  O   . ASP   Z  151 ? 1.7415 1.2685 1.7225 0.0726  0.0333  0.0511  151 ASP   Z O   
45349 C  CB  . ASP   Z  151 ? 1.7140 0.9787 1.6840 0.1164  0.0567  -0.0780 151 ASP   Z CB  
45350 C  CG  . ASP   Z  151 ? 1.6882 0.9756 1.6664 0.1200  0.0311  -0.1429 151 ASP   Z CG  
45351 O  OD1 . ASP   Z  151 ? 1.7453 1.0651 1.6873 -0.0290 -0.0982 -0.2677 151 ASP   Z OD1 
45352 O  OD2 . ASP   Z  151 ? 1.7534 0.8883 1.6394 0.1405  0.0104  -0.1910 151 ASP   Z OD2 
45353 N  N   . ASN   Z  152 ? 1.5876 0.9915 1.7592 0.1319  -0.0144 0.0582  152 ASN   Z N   
45354 C  CA  . ASN   Z  152 ? 1.6113 0.9880 1.8431 0.1341  -0.0448 0.1268  152 ASN   Z CA  
45355 C  C   . ASN   Z  152 ? 1.6351 1.0260 1.9442 0.1679  -0.0313 0.1258  152 ASN   Z C   
45356 O  O   . ASN   Z  152 ? 1.6619 1.0155 2.0047 0.1215  -0.0189 0.1778  152 ASN   Z O   
45357 C  CB  . ASN   Z  152 ? 1.5430 1.0184 1.8289 0.1167  -0.0801 0.1075  152 ASN   Z CB  
45358 C  CG  . ASN   Z  152 ? 1.5163 1.1147 1.8905 0.0658  -0.0727 0.1163  152 ASN   Z CG  
45359 O  OD1 . ASN   Z  152 ? 1.4381 1.0562 1.9625 0.0009  -0.0702 0.1717  152 ASN   Z OD1 
45360 N  ND2 . ASN   Z  152 ? 1.5327 1.1476 1.9022 0.0258  -0.0023 0.1318  152 ASN   Z ND2 
45361 N  N   . GLN   Z  153 ? 1.6662 1.0692 1.9908 0.2208  -0.0660 0.1464  153 GLN   Z N   
45362 C  CA  . GLN   Z  153 ? 1.6546 1.1335 2.0165 0.2381  -0.0420 0.1517  153 GLN   Z CA  
45363 C  C   . GLN   Z  153 ? 1.6341 1.2022 2.0883 0.3174  0.0073  0.0991  153 GLN   Z C   
45364 O  O   . GLN   Z  153 ? 1.6463 1.2754 2.0983 0.3507  0.0547  0.1125  153 GLN   Z O   
45365 C  CB  . GLN   Z  153 ? 1.6019 1.0798 2.0093 0.2375  -0.0259 0.1433  153 GLN   Z CB  
45366 C  CG  . GLN   Z  153 ? 1.5008 1.0527 1.9646 0.2593  0.0235  0.1987  153 GLN   Z CG  
45367 C  CD  . GLN   Z  153 ? 1.4564 1.0625 2.0101 0.3062  0.0612  0.2290  153 GLN   Z CD  
45368 O  OE1 . GLN   Z  153 ? 1.3679 1.2236 2.0241 0.1962  0.1331  0.2739  153 GLN   Z OE1 
45369 N  NE2 . GLN   Z  153 ? 1.4414 0.9928 2.0316 0.2787  0.1205  0.2060  153 GLN   Z NE2 
45370 N  N   . VAL   Z  154 ? 1.7238 1.1831 2.1035 0.2889  0.0048  0.0211  154 VAL   Z N   
45371 C  CA  . VAL   Z  154 ? 1.7908 1.2471 2.0635 0.3520  0.0513  -0.0410 154 VAL   Z CA  
45372 C  C   . VAL   Z  154 ? 1.8052 1.2902 2.0351 0.3355  0.1326  0.0104  154 VAL   Z C   
45373 O  O   . VAL   Z  154 ? 1.7280 1.4193 2.0807 0.2515  0.2433  0.1430  154 VAL   Z O   
45374 C  CB  . VAL   Z  154 ? 1.8129 1.3626 2.0433 0.3710  0.0802  -0.0058 154 VAL   Z CB  
45375 C  CG1 . VAL   Z  154 ? 1.8726 1.4089 2.0581 0.4581  0.0887  -0.0219 154 VAL   Z CG1 
45376 C  CG2 . VAL   Z  154 ? 1.7610 1.2931 2.0562 0.3769  0.0236  -0.0166 154 VAL   Z CG2 
45377 N  N   . ASN   Z  155 ? 1.8590 1.2851 2.0150 0.3625  0.0935  -0.0168 155 ASN   Z N   
45378 C  CA  . ASN   Z  155 ? 1.8073 1.4164 2.0471 0.2841  0.0629  -0.0370 155 ASN   Z CA  
45379 C  C   . ASN   Z  155 ? 1.8203 1.3951 2.0434 0.2826  0.1252  -0.0727 155 ASN   Z C   
45380 O  O   . ASN   Z  155 ? 1.9071 1.3949 2.0454 0.2744  0.1340  -0.0143 155 ASN   Z O   
45381 C  CB  . ASN   Z  155 ? 1.8311 1.5118 2.1043 0.2263  -0.0070 -0.1153 155 ASN   Z CB  
45382 C  CG  . ASN   Z  155 ? 1.6342 1.6029 2.1541 0.0593  -0.0658 -0.1411 155 ASN   Z CG  
45383 O  OD1 . ASN   Z  155 ? 1.5049 1.7501 2.2060 0.0824  -0.2154 -0.2614 155 ASN   Z OD1 
45384 N  ND2 . ASN   Z  155 ? 1.5758 1.6759 2.1920 0.1020  -0.0899 -0.2082 155 ASN   Z ND2 
45385 N  N   . PHE   Z  156 ? 1.7325 1.4752 1.9267 0.3087  0.1421  -0.1127 156 PHE   Z N   
45386 C  CA  . PHE   Z  156 ? 1.7120 1.5004 1.8677 0.2882  0.0788  -0.1035 156 PHE   Z CA  
45387 C  C   . PHE   Z  156 ? 1.7833 1.4554 1.7081 0.2469  0.0873  -0.0635 156 PHE   Z C   
45388 O  O   . PHE   Z  156 ? 1.7851 1.3121 1.7653 0.1737  0.0471  -0.0148 156 PHE   Z O   
45389 C  CB  . PHE   Z  156 ? 1.7389 1.6503 1.9649 0.2711  0.1411  -0.1089 156 PHE   Z CB  
45390 C  CG  . PHE   Z  156 ? 1.7789 1.8031 2.0487 0.2445  0.0433  -0.0686 156 PHE   Z CG  
45391 C  CD1 . PHE   Z  156 ? 1.7827 1.7225 2.1079 0.2221  0.0674  -0.1697 156 PHE   Z CD1 
45392 C  CD2 . PHE   Z  156 ? 1.8892 1.8252 2.1557 0.2742  0.0891  -0.0588 156 PHE   Z CD2 
45393 C  CE1 . PHE   Z  156 ? 1.7901 1.8089 2.1173 0.1584  -0.0175 -0.1451 156 PHE   Z CE1 
45394 C  CE2 . PHE   Z  156 ? 1.8782 1.8733 2.1812 0.2188  0.0228  -0.0604 156 PHE   Z CE2 
45395 C  CZ  . PHE   Z  156 ? 1.8284 1.8064 2.2234 0.1916  0.0192  -0.1075 156 PHE   Z CZ  
45396 N  N   . LYS   Z  157 ? 1.7516 1.4371 1.6520 0.2891  0.0321  -0.0509 157 LYS   Z N   
45397 C  CA  . LYS   Z  157 ? 1.7402 1.4447 1.6506 0.2895  0.0519  -0.0209 157 LYS   Z CA  
45398 C  C   . LYS   Z  157 ? 1.7268 1.4408 1.5862 0.3078  0.0386  -0.0556 157 LYS   Z C   
45399 O  O   . LYS   Z  157 ? 1.6935 1.5221 1.5664 0.3008  0.0024  0.0014  157 LYS   Z O   
45400 C  CB  . LYS   Z  157 ? 1.6782 1.4487 1.7277 0.2632  -0.0123 0.0419  157 LYS   Z CB  
45401 C  CG  . LYS   Z  157 ? 1.6158 1.4588 1.8287 0.2377  -0.0099 0.0967  157 LYS   Z CG  
45402 C  CD  . LYS   Z  157 ? 1.6092 1.4743 1.8185 0.2360  -0.0050 0.1273  157 LYS   Z CD  
45403 C  CE  . LYS   Z  157 ? 1.6900 1.4923 1.9078 0.2227  -0.0166 0.0855  157 LYS   Z CE  
45404 N  NZ  . LYS   Z  157 ? 1.7223 1.5404 1.9529 0.1851  -0.0133 0.1179  157 LYS   Z NZ  
45405 N  N   . ASN   Z  158 ? 1.7186 1.3954 1.5726 0.3305  0.1026  -0.0646 158 ASN   Z N   
45406 C  CA  . ASN   Z  158 ? 1.6989 1.3832 1.5909 0.3048  0.1342  -0.0950 158 ASN   Z CA  
45407 C  C   . ASN   Z  158 ? 1.6934 1.2950 1.6342 0.3270  0.1538  -0.1063 158 ASN   Z C   
45408 O  O   . ASN   Z  158 ? 1.7015 1.3003 1.6320 0.2985  0.1750  -0.1090 158 ASN   Z O   
45409 C  CB  . ASN   Z  158 ? 1.7154 1.3430 1.5528 0.2596  0.1023  -0.1233 158 ASN   Z CB  
45410 C  CG  . ASN   Z  158 ? 1.7108 1.3716 1.4866 0.2982  0.1162  -0.1405 158 ASN   Z CG  
45411 O  OD1 . ASN   Z  158 ? 1.6511 1.5365 1.3968 0.3249  0.1554  -0.2064 158 ASN   Z OD1 
45412 N  ND2 . ASN   Z  158 ? 1.7806 1.2807 1.5047 0.3139  0.1616  -0.0911 158 ASN   Z ND2 
45413 N  N   . GLN   Z  159 ? 1.7047 1.4073 1.6586 0.3860  0.1344  -0.1049 159 GLN   Z N   
45414 C  CA  . GLN   Z  159 ? 1.7244 1.4617 1.7707 0.3505  0.1214  -0.0719 159 GLN   Z CA  
45415 C  C   . GLN   Z  159 ? 1.7724 1.5351 1.7888 0.3403  0.1667  -0.0183 159 GLN   Z C   
45416 O  O   . GLN   Z  159 ? 1.8770 1.6576 1.8704 0.2982  0.1169  -0.1468 159 GLN   Z O   
45417 C  CB  . GLN   Z  159 ? 1.7610 1.5815 1.7582 0.3465  0.1000  -0.0296 159 GLN   Z CB  
45418 C  CG  . GLN   Z  159 ? 1.7256 1.5247 1.7609 0.3588  0.0852  -0.0362 159 GLN   Z CG  
45419 C  CD  . GLN   Z  159 ? 1.7292 1.5327 1.7786 0.3049  0.0537  -0.0035 159 GLN   Z CD  
45420 O  OE1 . GLN   Z  159 ? 1.7690 1.7010 1.6754 0.3617  -0.0454 0.0694  159 GLN   Z OE1 
45421 N  NE2 . GLN   Z  159 ? 1.7497 1.3995 1.7833 0.2845  0.0014  0.0371  159 GLN   Z NE2 
45422 N  N   . TYR   Z  160 ? 1.7907 1.3682 1.8358 0.4122  0.1975  -0.0884 160 TYR   Z N   
45423 C  CA  . TYR   Z  160 ? 1.8674 1.4116 1.8867 0.4235  0.2752  -0.0290 160 TYR   Z CA  
45424 C  C   . TYR   Z  160 ? 1.8795 1.4552 1.9532 0.3997  0.2792  0.0221  160 TYR   Z C   
45425 O  O   . TYR   Z  160 ? 1.8125 1.1517 1.8655 0.5367  0.4654  -0.0257 160 TYR   Z O   
45426 C  CB  . TYR   Z  160 ? 1.8827 1.3570 1.8975 0.4205  0.3064  -0.0370 160 TYR   Z CB  
45427 C  CG  . TYR   Z  160 ? 1.9066 1.3888 1.9149 0.3939  0.2989  -0.0467 160 TYR   Z CG  
45428 C  CD1 . TYR   Z  160 ? 1.9262 1.2934 1.9039 0.3693  0.2790  -0.1229 160 TYR   Z CD1 
45429 C  CD2 . TYR   Z  160 ? 1.9614 1.5035 1.8597 0.3543  0.2872  -0.0267 160 TYR   Z CD2 
45430 C  CE1 . TYR   Z  160 ? 1.9222 1.3145 1.8921 0.3571  0.2812  -0.1127 160 TYR   Z CE1 
45431 C  CE2 . TYR   Z  160 ? 1.9573 1.5358 1.8677 0.3382  0.2948  -0.0144 160 TYR   Z CE2 
45432 C  CZ  . TYR   Z  160 ? 1.9213 1.4267 1.8385 0.3102  0.2394  -0.0802 160 TYR   Z CZ  
45433 O  OH  . TYR   Z  160 ? 1.9231 1.4846 1.8566 0.2865  0.2437  -0.0580 160 TYR   Z OH  
45434 N  N   . GLU   Z  161 ? 2.0061 1.6767 1.9830 0.4392  0.3700  0.0525  161 GLU   Z N   
45435 C  CA  . GLU   Z  161 ? 2.0094 1.7863 2.1507 0.4229  0.3143  0.1124  161 GLU   Z CA  
45436 C  C   . GLU   Z  161 ? 1.9546 1.8083 2.1337 0.4184  0.3147  0.1613  161 GLU   Z C   
45437 O  O   . GLU   Z  161 ? 2.0323 1.9723 2.2472 0.5546  0.3375  0.2632  161 GLU   Z O   
45438 C  CB  . GLU   Z  161 ? 2.1837 1.7970 2.1906 0.4999  0.2883  0.0778  161 GLU   Z CB  
45439 C  CG  . GLU   Z  161 ? 2.1977 1.9439 2.2807 0.5246  0.2074  0.0760  161 GLU   Z CG  
45440 C  CD  . GLU   Z  161 ? 2.3116 2.0535 2.2122 0.5603  0.0571  0.1235  161 GLU   Z CD  
45441 O  OE1 . GLU   Z  161 ? 2.4459 2.1347 2.2128 0.5236  -0.0347 0.0326  161 GLU   Z OE1 
45442 O  OE2 . GLU   Z  161 ? 2.3734 2.2867 2.2127 0.4792  -0.0055 0.1180  161 GLU   Z OE2 
45443 N  N   . PRO   Z  162 ? 1.8187 1.6913 2.1584 0.4135  0.4020  0.1359  162 PRO   Z N   
45444 C  CA  . PRO   Z  162 ? 1.6809 1.6383 2.1507 0.4547  0.4401  0.1115  162 PRO   Z CA  
45445 C  C   . PRO   Z  162 ? 1.6720 1.5825 2.2405 0.4242  0.4688  0.1905  162 PRO   Z C   
45446 O  O   . PRO   Z  162 ? 1.5737 1.6220 2.2962 0.3934  0.4832  0.2238  162 PRO   Z O   
45447 C  CB  . PRO   Z  162 ? 1.6471 1.5800 2.1796 0.4235  0.4567  0.0650  162 PRO   Z CB  
45448 C  CG  . PRO   Z  162 ? 1.6806 1.6327 2.1327 0.4075  0.4368  0.0641  162 PRO   Z CG  
45449 C  CD  . PRO   Z  162 ? 1.7482 1.7068 2.0983 0.3774  0.3851  0.0690  162 PRO   Z CD  
45450 N  N   . GLY   Z  163 ? 1.6931 1.5637 2.2503 0.4304  0.5224  0.1964  163 GLY   Z N   
45451 C  CA  . GLY   Z  163 ? 1.7900 1.6037 2.3003 0.4477  0.5520  0.2625  163 GLY   Z CA  
45452 C  C   . GLY   Z  163 ? 1.9053 1.7006 2.1678 0.4825  0.5619  0.3213  163 GLY   Z C   
45453 O  O   . GLY   Z  163 ? 1.9543 1.5727 2.2204 0.5014  0.5611  0.3565  163 GLY   Z O   
45454 N  N   . THR   Z  164 ? 1.9671 1.7861 2.1560 0.4288  0.5407  0.3310  164 THR   Z N   
45455 C  CA  . THR   Z  164 ? 2.1034 2.0658 2.0583 0.4980  0.4893  0.3052  164 THR   Z CA  
45456 C  C   . THR   Z  164 ? 2.1890 1.9160 2.0931 0.5439  0.4774  0.3184  164 THR   Z C   
45457 O  O   . THR   Z  164 ? 2.2341 2.0378 2.0865 0.5818  0.4769  0.2519  164 THR   Z O   
45458 C  CB  . THR   Z  164 ? 2.1672 2.1232 2.0493 0.5040  0.4728  0.3340  164 THR   Z CB  
45459 O  OG1 . THR   Z  164 ? 2.1611 2.3717 2.0516 0.4618  0.4698  0.3025  164 THR   Z OG1 
45460 C  CG2 . THR   Z  164 ? 2.1365 2.2158 2.0636 0.5176  0.5067  0.3112  164 THR   Z CG2 
45461 N  N   . ASN   Z  165 ? 2.1686 1.7862 2.1359 0.5185  0.3955  0.3665  165 ASN   Z N   
45462 C  CA  . ASN   Z  165 ? 2.1787 1.7423 2.2080 0.4957  0.3516  0.3672  165 ASN   Z CA  
45463 C  C   . ASN   Z  165 ? 2.1699 1.7474 2.0909 0.5140  0.3696  0.3269  165 ASN   Z C   
45464 O  O   . ASN   Z  165 ? 2.1685 1.8094 2.0401 0.5979  0.4205  0.3282  165 ASN   Z O   
45465 C  CB  . ASN   Z  165 ? 2.2606 1.7837 2.2273 0.4652  0.3272  0.4053  165 ASN   Z CB  
45466 C  CG  . ASN   Z  165 ? 2.3095 1.7831 2.3064 0.4500  0.2563  0.4293  165 ASN   Z CG  
45467 O  OD1 . ASN   Z  165 ? 2.4747 1.9019 2.3165 0.4239  0.2129  0.3869  165 ASN   Z OD1 
45468 N  ND2 . ASN   Z  165 ? 2.2891 1.7801 2.3413 0.3818  0.2323  0.3993  165 ASN   Z ND2 
45469 N  N   . GLY   Z  166 ? 2.1156 1.6771 2.0687 0.4969  0.3308  0.2787  166 GLY   Z N   
45470 C  CA  . GLY   Z  166 ? 2.1593 1.6204 2.1213 0.4435  0.3037  0.2237  166 GLY   Z CA  
45471 C  C   . GLY   Z  166 ? 2.2327 1.6407 2.1096 0.4207  0.3060  0.2255  166 GLY   Z C   
45472 O  O   . GLY   Z  166 ? 2.2465 1.7499 2.1953 0.3922  0.2739  0.1835  166 GLY   Z O   
45473 N  N   . LYS   Z  167 ? 2.2003 1.6552 2.1079 0.4194  0.3248  0.2868  167 LYS   Z N   
45474 C  CA  . LYS   Z  167 ? 2.2368 1.6221 2.0708 0.4445  0.3105  0.3231  167 LYS   Z CA  
45475 C  C   . LYS   Z  167 ? 2.3027 1.6104 2.1037 0.4867  0.2603  0.2511  167 LYS   Z C   
45476 O  O   . LYS   Z  167 ? 2.4392 1.4497 2.1017 0.5898  0.2069  0.2546  167 LYS   Z O   
45477 C  CB  . LYS   Z  167 ? 2.1784 1.6739 2.1161 0.4156  0.3142  0.3635  167 LYS   Z CB  
45478 C  CG  . LYS   Z  167 ? 2.1953 1.5906 2.0585 0.4399  0.3453  0.4292  167 LYS   Z CG  
45479 C  CD  . LYS   Z  167 ? 2.2028 1.5762 2.0033 0.3998  0.3020  0.4791  167 LYS   Z CD  
45480 C  CE  . LYS   Z  167 ? 2.1777 1.4971 1.9656 0.3792  0.2629  0.4592  167 LYS   Z CE  
45481 N  NZ  . LYS   Z  167 ? 2.2061 1.5277 1.9307 0.3712  0.2601  0.4775  167 LYS   Z NZ  
45482 N  N   . VAL   Z  168 ? 2.2450 1.5412 2.1611 0.5537  0.2840  0.2147  168 VAL   Z N   
45483 C  CA  . VAL   Z  168 ? 2.1735 1.5899 2.0807 0.6062  0.3079  0.1868  168 VAL   Z CA  
45484 C  C   . VAL   Z  168 ? 2.1109 1.4439 2.0360 0.6070  0.2802  0.0829  168 VAL   Z C   
45485 O  O   . VAL   Z  168 ? 2.0257 1.3172 2.0114 0.7422  0.3036  0.0657  168 VAL   Z O   
45486 C  CB  . VAL   Z  168 ? 2.1868 1.7884 2.1259 0.5464  0.3546  0.2219  168 VAL   Z CB  
45487 C  CG1 . VAL   Z  168 ? 2.1710 1.8513 2.1419 0.5544  0.3071  0.2407  168 VAL   Z CG1 
45488 C  CG2 . VAL   Z  168 ? 2.2203 1.8331 2.1418 0.5395  0.4014  0.2896  168 VAL   Z CG2 
45489 N  N   . LYS   Z  169 ? 2.1584 1.5524 1.9627 0.5639  0.3391  0.1414  169 LYS   Z N   
45490 C  CA  . LYS   Z  169 ? 2.1434 1.6425 1.9325 0.5345  0.3461  0.0905  169 LYS   Z CA  
45491 C  C   . LYS   Z  169 ? 2.1527 1.6425 1.8680 0.5235  0.3411  0.0826  169 LYS   Z C   
45492 O  O   . LYS   Z  169 ? 1.9999 1.7373 1.9904 0.4759  0.4039  0.1923  169 LYS   Z O   
45493 C  CB  . LYS   Z  169 ? 2.0938 1.7897 1.9092 0.4914  0.3479  0.1192  169 LYS   Z CB  
45494 C  CG  . LYS   Z  169 ? 2.0745 1.7977 1.8990 0.4260  0.3368  0.1614  169 LYS   Z CG  
45495 C  CD  . LYS   Z  169 ? 2.1112 1.8036 1.8755 0.3951  0.2751  0.1800  169 LYS   Z CD  
45496 C  CE  . LYS   Z  169 ? 2.1500 1.6888 1.8439 0.3321  0.2281  0.1995  169 LYS   Z CE  
45497 N  NZ  . LYS   Z  169 ? 2.2362 1.6378 1.8432 0.3202  0.1717  0.1906  169 LYS   Z NZ  
45498 N  N   . LYS   Z  170 ? 2.1442 1.5027 1.8847 0.6084  0.2921  0.0204  170 LYS   Z N   
45499 C  CA  . LYS   Z  170 ? 2.1291 1.6126 1.9214 0.6111  0.2503  0.0130  170 LYS   Z CA  
45500 C  C   . LYS   Z  170 ? 2.1715 1.6249 1.8489 0.6092  0.2952  0.0317  170 LYS   Z C   
45501 O  O   . LYS   Z  170 ? 2.2203 1.7781 1.8835 0.5203  0.2147  0.0733  170 LYS   Z O   
45502 C  CB  . LYS   Z  170 ? 2.1291 1.4365 1.9851 0.6631  0.1353  -0.0934 170 LYS   Z CB  
45503 C  CG  . LYS   Z  170 ? 2.1139 1.4667 2.0347 0.6277  0.0838  -0.1366 170 LYS   Z CG  
45504 C  CD  . LYS   Z  170 ? 2.0797 1.3736 2.0806 0.6810  0.0528  -0.1742 170 LYS   Z CD  
45505 C  CE  . LYS   Z  170 ? 2.0960 1.3734 2.0687 0.6469  0.0372  -0.1897 170 LYS   Z CE  
45506 N  NZ  . LYS   Z  170 ? 2.1191 1.3868 2.0333 0.6397  0.0000  -0.2064 170 LYS   Z NZ  
45507 N  N   . PRO   Z  171 ? 2.0512 1.7130 1.8290 0.5433  0.3908  0.0926  171 PRO   Z N   
45508 C  CA  . PRO   Z  171 ? 2.0747 1.7210 1.8612 0.5706  0.3755  0.0788  171 PRO   Z CA  
45509 C  C   . PRO   Z  171 ? 2.1446 1.7139 1.8590 0.5391  0.2690  0.0973  171 PRO   Z C   
45510 O  O   . PRO   Z  171 ? 2.1365 1.7116 1.8678 0.6354  0.2599  0.0214  171 PRO   Z O   
45511 C  CB  . PRO   Z  171 ? 2.0357 1.7721 1.8550 0.5394  0.3868  0.1450  171 PRO   Z CB  
45512 C  CG  . PRO   Z  171 ? 1.9536 1.7347 1.8725 0.5745  0.4015  0.1501  171 PRO   Z CG  
45513 C  CD  . PRO   Z  171 ? 2.0230 1.6984 1.8520 0.5619  0.4083  0.1084  171 PRO   Z CD  
45514 N  N   . LEU   Z  172 ? 2.2278 1.7371 2.0340 0.4783  0.2352  0.2249  172 LEU   Z N   
45515 C  CA  . LEU   Z  172 ? 2.2042 1.7710 2.0739 0.4956  0.1877  0.2785  172 LEU   Z CA  
45516 C  C   . LEU   Z  172 ? 2.1874 1.7133 2.1203 0.4522  0.1255  0.2720  172 LEU   Z C   
45517 O  O   . LEU   Z  172 ? 2.0996 1.7234 2.1819 0.4899  0.1715  0.3538  172 LEU   Z O   
45518 C  CB  . LEU   Z  172 ? 2.1415 1.8738 2.1043 0.5091  0.1953  0.2805  172 LEU   Z CB  
45519 C  CG  . LEU   Z  172 ? 2.1149 1.9073 2.0389 0.5201  0.2498  0.2927  172 LEU   Z CG  
45520 C  CD1 . LEU   Z  172 ? 2.0504 1.9866 1.9648 0.5156  0.2222  0.3181  172 LEU   Z CD1 
45521 C  CD2 . LEU   Z  172 ? 2.0451 1.8040 2.0836 0.5481  0.2380  0.2889  172 LEU   Z CD2 
45522 N  N   . LYS   Z  173 ? 2.1699 1.5876 2.1333 0.3815  0.0217  0.1841  173 LYS   Z N   
45523 C  CA  . LYS   Z  173 ? 2.1238 1.5701 2.1240 0.3011  -0.0763 0.1790  173 LYS   Z CA  
45524 C  C   . LYS   Z  173 ? 2.1542 1.6324 2.0213 0.2984  -0.1198 0.0767  173 LYS   Z C   
45525 O  O   . LYS   Z  173 ? 2.0775 1.3419 2.0886 0.3679  -0.3220 0.0364  173 LYS   Z O   
45526 C  CB  . LYS   Z  173 ? 2.2045 1.4402 2.0772 0.2354  -0.0430 0.2078  173 LYS   Z CB  
45527 C  CG  . LYS   Z  173 ? 2.2020 1.3362 2.0884 0.2073  -0.0254 0.2572  173 LYS   Z CG  
45528 C  CD  . LYS   Z  173 ? 2.2022 1.3484 2.1082 0.1927  -0.0038 0.2903  173 LYS   Z CD  
45529 C  CE  . LYS   Z  173 ? 2.2204 1.3235 2.0923 0.1881  -0.0265 0.3165  173 LYS   Z CE  
45530 N  NZ  . LYS   Z  173 ? 2.2580 1.3306 2.1054 0.2088  -0.0515 0.3177  173 LYS   Z NZ  
45531 N  N   . TYR   Z  174 ? 2.2171 1.6367 2.2104 0.2839  -0.1605 0.0701  174 TYR   Z N   
45532 C  CA  . TYR   Z  174 ? 2.1570 1.5864 2.0983 0.1800  -0.2095 -0.0560 174 TYR   Z CA  
45533 C  C   . TYR   Z  174 ? 2.0088 1.4176 1.9651 0.2182  -0.0732 -0.0390 174 TYR   Z C   
45534 O  O   . TYR   Z  174 ? 1.8885 1.1569 1.8811 0.2312  -0.2517 -0.1392 174 TYR   Z O   
45535 C  CB  . TYR   Z  174 ? 2.2218 1.6130 2.2922 0.2034  -0.1891 -0.1230 174 TYR   Z CB  
45536 C  CG  . TYR   Z  174 ? 2.3459 1.7517 2.3757 0.1918  -0.2128 -0.2903 174 TYR   Z CG  
45537 C  CD1 . TYR   Z  174 ? 2.3514 1.8709 2.4274 0.1512  -0.2227 -0.3220 174 TYR   Z CD1 
45538 C  CD2 . TYR   Z  174 ? 2.3366 1.8718 2.4423 0.2421  -0.1409 -0.3433 174 TYR   Z CD2 
45539 C  CE1 . TYR   Z  174 ? 2.3452 1.9687 2.4073 0.1807  -0.2545 -0.3859 174 TYR   Z CE1 
45540 C  CE2 . TYR   Z  174 ? 2.3698 1.9691 2.3901 0.2747  -0.1860 -0.4066 174 TYR   Z CE2 
45541 C  CZ  . TYR   Z  174 ? 2.3108 2.0046 2.4068 0.2261  -0.2797 -0.4007 174 TYR   Z CZ  
45542 O  OH  . TYR   Z  174 ? 2.1901 2.0370 2.3107 0.3352  -0.3937 -0.3359 174 TYR   Z OH  
45543 N  N   . LEU   Z  175 ? 1.9398 1.2555 1.9301 0.2012  -0.1172 -0.1175 175 LEU   Z N   
45544 C  CA  . LEU   Z  175 ? 1.7473 1.1953 1.9536 0.1575  -0.0645 -0.0930 175 LEU   Z CA  
45545 C  C   . LEU   Z  175 ? 1.6245 1.1648 1.9331 0.1763  -0.0314 -0.1411 175 LEU   Z C   
45546 O  O   . LEU   Z  175 ? 1.6609 1.1277 1.9123 0.2300  0.0100  -0.1095 175 LEU   Z O   
45547 C  CB  . LEU   Z  175 ? 1.7198 1.2545 1.9628 0.1326  -0.0651 -0.1264 175 LEU   Z CB  
45548 C  CG  . LEU   Z  175 ? 1.7310 1.2685 1.9703 0.1117  -0.0302 -0.0920 175 LEU   Z CG  
45549 C  CD1 . LEU   Z  175 ? 1.7379 1.3785 1.9422 0.1172  -0.0268 -0.0710 175 LEU   Z CD1 
45550 C  CD2 . LEU   Z  175 ? 1.7271 1.2484 1.9899 0.0612  -0.0488 -0.1187 175 LEU   Z CD2 
45551 N  N   . SER   Z  176 ? 1.5769 1.0184 1.9088 0.1509  0.0279  -0.0976 176 SER   Z N   
45552 C  CA  . SER   Z  176 ? 1.5554 1.0408 1.8886 0.1191  0.0114  -0.0854 176 SER   Z CA  
45553 C  C   . SER   Z  176 ? 1.5112 0.9643 1.8385 0.1108  -0.0457 -0.0470 176 SER   Z C   
45554 O  O   . SER   Z  176 ? 1.5217 0.8615 1.8282 0.0624  -0.0468 -0.0218 176 SER   Z O   
45555 C  CB  . SER   Z  176 ? 1.5336 1.0761 1.9173 0.1459  0.0176  -0.0748 176 SER   Z CB  
45556 O  OG  . SER   Z  176 ? 1.5670 1.1274 1.9354 0.1517  0.0198  -0.1348 176 SER   Z OG  
45557 N  N   . VAL   Z  177 ? 1.4901 1.0362 1.8440 0.1269  -0.0936 -0.0085 177 VAL   Z N   
45558 C  CA  . VAL   Z  177 ? 1.4941 0.9887 1.8351 0.1546  -0.1153 0.0497  177 VAL   Z CA  
45559 C  C   . VAL   Z  177 ? 1.5368 0.9774 1.8842 0.1741  -0.1016 0.0262  177 VAL   Z C   
45560 O  O   . VAL   Z  177 ? 1.5925 0.9424 1.8265 0.2331  -0.1149 0.0502  177 VAL   Z O   
45561 C  CB  . VAL   Z  177 ? 1.4833 0.9845 1.8332 0.1614  -0.1213 0.0503  177 VAL   Z CB  
45562 C  CG1 . VAL   Z  177 ? 1.4747 0.9827 1.8820 0.1566  -0.1044 0.0785  177 VAL   Z CG1 
45563 C  CG2 . VAL   Z  177 ? 1.4164 0.9573 1.7980 0.1795  -0.1677 0.0558  177 VAL   Z CG2 
45564 N  N   . GLU   Z  178 ? 1.5604 0.9795 1.9799 0.1490  -0.0777 0.0191  178 GLU   Z N   
45565 C  CA  . GLU   Z  178 ? 1.6022 1.0219 2.0245 0.1146  -0.0851 -0.0091 178 GLU   Z CA  
45566 C  C   . GLU   Z  178 ? 1.6143 0.9061 2.0306 0.0806  -0.0437 -0.0790 178 GLU   Z C   
45567 O  O   . GLU   Z  178 ? 1.6029 0.7198 2.0422 0.0423  -0.0652 -0.0746 178 GLU   Z O   
45568 C  CB  . GLU   Z  178 ? 1.6088 1.1991 2.0912 0.1233  -0.0571 -0.0029 178 GLU   Z CB  
45569 C  CG  . GLU   Z  178 ? 1.6501 1.2743 2.1128 0.1637  -0.0610 0.0134  178 GLU   Z CG  
45570 C  CD  . GLU   Z  178 ? 1.7019 1.3882 2.0807 0.1608  -0.0042 -0.0508 178 GLU   Z CD  
45571 O  OE1 . GLU   Z  178 ? 1.7608 1.3734 2.0700 0.1480  0.0203  -0.0304 178 GLU   Z OE1 
45572 O  OE2 . GLU   Z  178 ? 1.6951 1.5866 2.0583 0.1770  0.0363  -0.0644 178 GLU   Z OE2 
45573 N  N   . GLU   Z  179 ? 1.6667 0.8963 2.0411 0.0632  -0.0535 -0.0741 179 GLU   Z N   
45574 C  CA  . GLU   Z  179 ? 1.6783 0.8563 2.1076 0.0570  -0.0490 -0.0876 179 GLU   Z CA  
45575 C  C   . GLU   Z  179 ? 1.7057 0.8325 2.0032 0.0259  0.0010  -0.1306 179 GLU   Z C   
45576 O  O   . GLU   Z  179 ? 1.6506 0.9067 1.9594 -0.0222 0.0606  -0.2391 179 GLU   Z O   
45577 C  CB  . GLU   Z  179 ? 1.7832 0.9374 2.1197 0.0476  -0.0772 -0.0366 179 GLU   Z CB  
45578 C  CG  . GLU   Z  179 ? 1.8056 1.1579 2.2055 -0.0264 -0.0852 0.0823  179 GLU   Z CG  
45579 C  CD  . GLU   Z  179 ? 1.8544 1.2147 2.2346 -0.0424 -0.1528 0.0111  179 GLU   Z CD  
45580 O  OE1 . GLU   Z  179 ? 1.8679 1.3886 2.3212 -0.1560 -0.1692 0.0344  179 GLU   Z OE1 
45581 O  OE2 . GLU   Z  179 ? 1.9646 1.3892 2.2611 0.0525  -0.2161 0.0995  179 GLU   Z OE2 
45582 N  N   . VAL   Z  180 ? 1.6327 0.8084 1.9660 0.0561  0.0710  -0.0718 180 VAL   Z N   
45583 C  CA  . VAL   Z  180 ? 1.5982 0.8264 1.9124 0.0999  0.0494  -0.0990 180 VAL   Z CA  
45584 C  C   . VAL   Z  180 ? 1.5624 0.7774 1.9249 0.1484  0.0505  -0.1217 180 VAL   Z C   
45585 O  O   . VAL   Z  180 ? 1.5829 0.7204 1.8912 0.1808  0.0025  -0.0932 180 VAL   Z O   
45586 C  CB  . VAL   Z  180 ? 1.5323 0.8908 1.8962 0.0441  0.0356  -0.1439 180 VAL   Z CB  
45587 C  CG1 . VAL   Z  180 ? 1.5038 0.9124 1.8567 0.0765  0.0284  -0.1613 180 VAL   Z CG1 
45588 C  CG2 . VAL   Z  180 ? 1.5507 0.9329 1.8889 0.0375  0.0563  -0.1191 180 VAL   Z CG2 
45589 N  N   . ILE   Z  181 ? 1.5848 0.8289 1.9502 0.1508  0.0269  -0.1158 181 ILE   Z N   
45590 C  CA  . ILE   Z  181 ? 1.5595 0.8245 1.9334 0.1008  -0.0151 -0.0892 181 ILE   Z CA  
45591 C  C   . ILE   Z  181 ? 1.4700 0.8133 1.9404 0.0370  -0.0378 -0.0534 181 ILE   Z C   
45592 O  O   . ILE   Z  181 ? 1.3093 0.8171 1.8596 -0.0344 -0.0884 0.0003  181 ILE   Z O   
45593 C  CB  . ILE   Z  181 ? 1.6456 0.8191 1.9389 0.1259  -0.0222 -0.0748 181 ILE   Z CB  
45594 C  CG1 . ILE   Z  181 ? 1.7081 0.8143 1.9720 0.1220  0.0091  -0.0441 181 ILE   Z CG1 
45595 C  CG2 . ILE   Z  181 ? 1.6503 0.8061 1.9571 0.0886  -0.0491 -0.1007 181 ILE   Z CG2 
45596 C  CD1 . ILE   Z  181 ? 1.7514 0.8217 2.0019 0.1334  0.0051  -0.0272 181 ILE   Z CD1 
45597 N  N   . LYS   Z  182 ? 1.5026 0.8020 2.0186 0.0413  -0.0005 -0.0370 182 LYS   Z N   
45598 C  CA  . LYS   Z  182 ? 1.4644 0.8101 2.0588 0.0616  0.0320  -0.0876 182 LYS   Z CA  
45599 C  C   . LYS   Z  182 ? 1.4893 0.6864 1.9965 0.1010  0.0727  -0.0880 182 LYS   Z C   
45600 O  O   . LYS   Z  182 ? 1.2607 0.5324 2.0159 0.1341  0.0076  -0.0110 182 LYS   Z O   
45601 C  CB  . LYS   Z  182 ? 1.5026 0.8482 2.1567 -0.0025 0.0982  -0.1553 182 LYS   Z CB  
45602 C  CG  . LYS   Z  182 ? 1.4823 0.8903 2.2407 -0.0313 0.1053  -0.1715 182 LYS   Z CG  
45603 C  CD  . LYS   Z  182 ? 1.5354 0.9296 2.3531 -0.0804 0.1517  -0.1658 182 LYS   Z CD  
45604 C  CE  . LYS   Z  182 ? 1.5246 0.9832 2.4337 -0.0972 0.1613  -0.1324 182 LYS   Z CE  
45605 N  NZ  . LYS   Z  182 ? 1.5542 1.0075 2.5116 -0.0816 0.2127  -0.1039 182 LYS   Z NZ  
45606 N  N   . LEU   Z  183 ? 1.5335 0.6904 1.9276 0.1530  0.0793  -0.0316 183 LEU   Z N   
45607 C  CA  . LEU   Z  183 ? 1.5794 0.6791 1.8732 0.2004  0.1045  -0.0113 183 LEU   Z CA  
45608 C  C   . LEU   Z  183 ? 1.5601 0.6285 1.8074 0.1919  0.0655  -0.0252 183 LEU   Z C   
45609 O  O   . LEU   Z  183 ? 1.5254 0.6477 1.7960 0.2066  0.0528  0.0225  183 LEU   Z O   
45610 C  CB  . LEU   Z  183 ? 1.7339 0.7285 1.8689 0.1884  0.1278  -0.0280 183 LEU   Z CB  
45611 C  CG  . LEU   Z  183 ? 1.8158 0.8282 1.9087 0.1851  0.1895  -0.0312 183 LEU   Z CG  
45612 C  CD1 . LEU   Z  183 ? 1.8749 0.7647 1.9248 0.1786  0.2274  -0.0523 183 LEU   Z CD1 
45613 C  CD2 . LEU   Z  183 ? 1.8469 0.8317 1.9254 0.2183  0.1928  -0.0432 183 LEU   Z CD2 
45614 N  N   . VAL   Z  184 ? 1.4993 0.6482 1.7491 0.1433  0.0550  -0.0070 184 VAL   Z N   
45615 C  CA  . VAL   Z  184 ? 1.4403 0.6619 1.6997 0.1147  -0.0036 -0.0141 184 VAL   Z CA  
45616 C  C   . VAL   Z  184 ? 1.4814 0.6260 1.7284 0.0878  -0.0254 -0.0218 184 VAL   Z C   
45617 O  O   . VAL   Z  184 ? 1.4247 0.5461 1.7303 0.0734  -0.0767 -0.0075 184 VAL   Z O   
45618 C  CB  . VAL   Z  184 ? 1.3851 0.6733 1.6721 0.1052  -0.0079 0.0166  184 VAL   Z CB  
45619 C  CG1 . VAL   Z  184 ? 1.3509 0.6864 1.6653 0.0825  -0.0331 0.0195  184 VAL   Z CG1 
45620 C  CG2 . VAL   Z  184 ? 1.3695 0.6622 1.6511 0.1197  0.0044  0.0234  184 VAL   Z CG2 
45621 N  N   . ARG   Z  185 ? 1.5206 0.6630 1.7291 0.0597  -0.0519 -0.0353 185 ARG   Z N   
45622 C  CA  . ARG   Z  185 ? 1.5191 0.6951 1.7283 0.0518  -0.0727 -0.0359 185 ARG   Z CA  
45623 C  C   . ARG   Z  185 ? 1.5612 0.6934 1.6740 0.0647  -0.0689 -0.0429 185 ARG   Z C   
45624 O  O   . ARG   Z  185 ? 1.5426 0.6001 1.5829 0.0973  -0.1162 0.0302  185 ARG   Z O   
45625 C  CB  . ARG   Z  185 ? 1.4884 0.7446 1.8237 0.0075  -0.0482 -0.0514 185 ARG   Z CB  
45626 C  CG  . ARG   Z  185 ? 1.4582 0.7028 1.8684 -0.0247 -0.0278 -0.0680 185 ARG   Z CG  
45627 C  CD  . ARG   Z  185 ? 1.4366 0.7469 1.9374 -0.0486 -0.0230 -0.0572 185 ARG   Z CD  
45628 N  NE  . ARG   Z  185 ? 1.4519 0.8199 1.9392 -0.0576 -0.0199 -0.0755 185 ARG   Z NE  
45629 C  CZ  . ARG   Z  185 ? 1.4278 0.9117 2.0645 -0.0857 -0.0347 -0.0469 185 ARG   Z CZ  
45630 N  NH1 . ARG   Z  185 ? 1.4648 0.9293 2.0946 -0.0711 0.0248  -0.0368 185 ARG   Z NH1 
45631 N  NH2 . ARG   Z  185 ? 1.4854 0.9454 2.1120 -0.1171 -0.0258 -0.0832 185 ARG   Z NH2 
45632 N  N   . ASP   Z  186 ? 1.6099 0.6470 1.7197 0.0596  -0.0254 -0.0389 186 ASP   Z N   
45633 C  CA  . ASP   Z  186 ? 1.6429 0.6375 1.8119 0.0972  0.0062  -0.1088 186 ASP   Z CA  
45634 C  C   . ASP   Z  186 ? 1.6423 0.7048 1.7974 0.0747  0.0207  -0.0716 186 ASP   Z C   
45635 O  O   . ASP   Z  186 ? 1.6292 0.8546 1.8499 0.1340  0.0663  -0.1276 186 ASP   Z O   
45636 C  CB  . ASP   Z  186 ? 1.6441 0.5791 1.8486 0.1031  0.0514  -0.1488 186 ASP   Z CB  
45637 C  CG  . ASP   Z  186 ? 1.6658 0.4552 1.8547 0.1054  0.0368  -0.2027 186 ASP   Z CG  
45638 O  OD1 . ASP   Z  186 ? 1.6624 0.3706 1.9217 0.0808  -0.0082 -0.2668 186 ASP   Z OD1 
45639 O  OD2 . ASP   Z  186 ? 1.6911 0.3512 1.9092 0.1326  0.0753  -0.1789 186 ASP   Z OD2 
45640 N  N   . SER   Z  187 ? 1.6312 0.6377 1.7442 0.0780  0.0305  -0.0117 187 SER   Z N   
45641 C  CA  . SER   Z  187 ? 1.6312 0.6002 1.6644 0.0999  0.0035  0.0485  187 SER   Z CA  
45642 C  C   . SER   Z  187 ? 1.6010 0.4982 1.6452 0.1216  -0.0211 0.0326  187 SER   Z C   
45643 O  O   . SER   Z  187 ? 1.6332 0.3876 1.5382 0.1300  -0.0864 0.0849  187 SER   Z O   
45644 C  CB  . SER   Z  187 ? 1.6296 0.6569 1.6285 0.0369  -0.0094 0.0532  187 SER   Z CB  
45645 O  OG  . SER   Z  187 ? 1.6879 0.7898 1.6534 -0.0024 -0.0078 0.1461  187 SER   Z OG  
45646 N  N   . PHE   Z  188 ? 1.6519 0.5640 1.6398 0.1149  -0.0595 0.0336  188 PHE   Z N   
45647 C  CA  . PHE   Z  188 ? 1.6533 0.5795 1.6278 0.1238  -0.0776 0.0308  188 PHE   Z CA  
45648 C  C   . PHE   Z  188 ? 1.6165 0.5223 1.6976 0.1376  -0.1239 0.0463  188 PHE   Z C   
45649 O  O   . PHE   Z  188 ? 1.6377 0.4814 1.7009 0.2710  -0.1433 0.1231  188 PHE   Z O   
45650 C  CB  . PHE   Z  188 ? 1.6546 0.5160 1.6489 0.0985  -0.0833 -0.0170 188 PHE   Z CB  
45651 C  CG  . PHE   Z  188 ? 1.6626 0.4680 1.6069 0.0973  -0.0332 0.0066  188 PHE   Z CG  
45652 C  CD1 . PHE   Z  188 ? 1.6977 0.5723 1.5507 0.0623  -0.0134 0.0064  188 PHE   Z CD1 
45653 C  CD2 . PHE   Z  188 ? 1.6325 0.4681 1.6074 0.1164  -0.0377 -0.0132 188 PHE   Z CD2 
45654 C  CE1 . PHE   Z  188 ? 1.6456 0.6964 1.4851 0.0374  -0.0256 -0.0394 188 PHE   Z CE1 
45655 C  CE2 . PHE   Z  188 ? 1.5594 0.6519 1.5581 0.0679  -0.0574 -0.0682 188 PHE   Z CE2 
45656 C  CZ  . PHE   Z  188 ? 1.5779 0.7613 1.5119 0.0591  -0.0460 -0.0735 188 PHE   Z CZ  
45657 N  N   . THR   Z  189 ? 1.6420 0.4756 1.7224 0.1090  -0.1623 0.0015  189 THR   Z N   
45658 C  CA  . THR   Z  189 ? 1.6239 0.5462 1.7679 0.0930  -0.1762 -0.0599 189 THR   Z CA  
45659 C  C   . THR   Z  189 ? 1.6028 0.5437 1.8067 0.1201  -0.1965 -0.1293 189 THR   Z C   
45660 O  O   . THR   Z  189 ? 1.6810 0.6530 1.8337 0.1183  -0.1934 -0.1983 189 THR   Z O   
45661 C  CB  . THR   Z  189 ? 1.6434 0.5518 1.7807 0.0513  -0.1777 -0.0591 189 THR   Z CB  
45662 O  OG1 . THR   Z  189 ? 1.6857 0.5752 1.7927 -0.0057 -0.1537 -0.0449 189 THR   Z OG1 
45663 C  CG2 . THR   Z  189 ? 1.6349 0.5220 1.7871 0.0356  -0.1895 -0.0705 189 THR   Z CG2 
45664 N  N   . SER   Z  190 ? 1.5683 0.5447 1.7902 0.1276  -0.1620 -0.1774 190 SER   Z N   
45665 C  CA  . SER   Z  190 ? 1.5526 0.5539 1.8239 0.1350  -0.1385 -0.1624 190 SER   Z CA  
45666 C  C   . SER   Z  190 ? 1.5300 0.5446 1.7156 0.1512  -0.1536 -0.2214 190 SER   Z C   
45667 O  O   . SER   Z  190 ? 1.4152 0.6505 1.6789 0.1673  -0.1498 -0.2434 190 SER   Z O   
45668 C  CB  . SER   Z  190 ? 1.5382 0.5311 1.8427 0.1472  -0.0866 -0.1043 190 SER   Z CB  
45669 O  OG  . SER   Z  190 ? 1.5257 0.4841 1.9323 0.1699  -0.0703 -0.0604 190 SER   Z OG  
45670 N  N   . ALA   Z  191 ? 1.4652 0.5991 1.6864 0.0937  -0.1502 -0.2193 191 ALA   Z N   
45671 C  CA  . ALA   Z  191 ? 1.4393 0.6495 1.5857 0.1256  -0.1536 -0.2565 191 ALA   Z CA  
45672 C  C   . ALA   Z  191 ? 1.4701 0.5414 1.5947 0.1398  -0.1771 -0.3272 191 ALA   Z C   
45673 O  O   . ALA   Z  191 ? 1.5593 0.3388 1.5143 0.1828  -0.2174 -0.3565 191 ALA   Z O   
45674 C  CB  . ALA   Z  191 ? 1.4264 0.6564 1.6253 0.1075  -0.1656 -0.2583 191 ALA   Z CB  
45675 N  N   . THR   Z  192 ? 1.4679 0.6010 1.5607 0.1148  -0.1748 -0.3336 192 THR   Z N   
45676 C  CA  . THR   Z  192 ? 1.4627 0.7067 1.5452 0.1097  -0.2354 -0.2824 192 THR   Z CA  
45677 C  C   . THR   Z  192 ? 1.4986 0.6832 1.5755 0.0578  -0.2138 -0.2617 192 THR   Z C   
45678 O  O   . THR   Z  192 ? 1.5340 0.6249 1.5253 0.0509  -0.2298 -0.2604 192 THR   Z O   
45679 C  CB  . THR   Z  192 ? 1.4868 0.6971 1.5550 0.1349  -0.2507 -0.2915 192 THR   Z CB  
45680 O  OG1 . THR   Z  192 ? 1.4961 0.7151 1.4811 0.1980  -0.2851 -0.2982 192 THR   Z OG1 
45681 C  CG2 . THR   Z  192 ? 1.4833 0.7235 1.5544 0.1411  -0.2782 -0.2923 192 THR   Z CG2 
45682 N  N   . GLU   Z  193 ? 1.5028 0.8353 1.6249 0.0105  -0.1842 -0.2055 193 GLU   Z N   
45683 C  CA  . GLU   Z  193 ? 1.5362 0.8411 1.6360 0.0263  -0.1843 -0.2012 193 GLU   Z CA  
45684 C  C   . GLU   Z  193 ? 1.5060 0.8094 1.5467 -0.0051 -0.1475 -0.1745 193 GLU   Z C   
45685 O  O   . GLU   Z  193 ? 1.4773 0.8334 1.5295 0.0114  -0.0717 -0.1223 193 GLU   Z O   
45686 C  CB  . GLU   Z  193 ? 1.6437 0.9412 1.6761 0.0088  -0.1592 -0.1371 193 GLU   Z CB  
45687 C  CG  . GLU   Z  193 ? 1.6680 1.0604 1.7889 0.0397  -0.1854 -0.1054 193 GLU   Z CG  
45688 C  CD  . GLU   Z  193 ? 1.8140 1.1483 1.8186 0.0221  -0.2095 -0.1358 193 GLU   Z CD  
45689 O  OE1 . GLU   Z  193 ? 1.9209 1.3168 1.8652 0.0443  -0.2270 -0.0502 193 GLU   Z OE1 
45690 O  OE2 . GLU   Z  193 ? 1.8582 1.1427 1.8531 0.0783  -0.2026 -0.0562 193 GLU   Z OE2 
45691 N  N   . ARG   Z  194 ? 1.4950 0.7569 1.5259 0.0077  -0.1427 -0.1574 194 ARG   Z N   
45692 C  CA  . ARG   Z  194 ? 1.5108 0.7332 1.5238 0.0068  -0.1540 -0.1532 194 ARG   Z CA  
45693 C  C   . ARG   Z  194 ? 1.4386 0.7339 1.4814 0.0591  -0.1585 -0.1005 194 ARG   Z C   
45694 O  O   . ARG   Z  194 ? 1.3953 0.8653 1.4859 0.0540  -0.1667 -0.1703 194 ARG   Z O   
45695 C  CB  . ARG   Z  194 ? 1.5792 0.7179 1.5370 -0.0038 -0.1507 -0.1392 194 ARG   Z CB  
45696 C  CG  . ARG   Z  194 ? 1.6029 0.7604 1.6004 -0.0355 -0.1626 -0.1186 194 ARG   Z CG  
45697 C  CD  . ARG   Z  194 ? 1.6358 0.7811 1.6083 -0.0277 -0.1626 -0.1326 194 ARG   Z CD  
45698 N  NE  . ARG   Z  194 ? 1.6602 0.7837 1.6479 -0.0457 -0.1732 -0.1389 194 ARG   Z NE  
45699 C  CZ  . ARG   Z  194 ? 1.6864 0.7993 1.6497 -0.0491 -0.2114 -0.1717 194 ARG   Z CZ  
45700 N  NH1 . ARG   Z  194 ? 1.6663 0.8574 1.6068 -0.0723 -0.2210 -0.1363 194 ARG   Z NH1 
45701 N  NH2 . ARG   Z  194 ? 1.6697 0.9060 1.6861 -0.0977 -0.2145 -0.1729 194 ARG   Z NH2 
45702 N  N   . HIS   Z  195 ? 1.4012 0.7555 1.5095 0.0474  -0.1415 -0.0470 195 HIS   Z N   
45703 C  CA  . HIS   Z  195 ? 1.4297 0.6293 1.4977 0.0823  -0.1531 -0.0125 195 HIS   Z CA  
45704 C  C   . HIS   Z  195 ? 1.4099 0.6489 1.5267 0.0872  -0.1591 0.0367  195 HIS   Z C   
45705 O  O   . HIS   Z  195 ? 1.3894 0.6648 1.5163 0.1153  -0.0923 0.0573  195 HIS   Z O   
45706 C  CB  . HIS   Z  195 ? 1.4663 0.5538 1.5315 0.0819  -0.1210 0.0079  195 HIS   Z CB  
45707 C  CG  . HIS   Z  195 ? 1.5143 0.4323 1.5352 0.0604  -0.1027 -0.0022 195 HIS   Z CG  
45708 N  ND1 . HIS   Z  195 ? 1.5635 0.3707 1.5026 0.0596  -0.0859 0.0351  195 HIS   Z ND1 
45709 C  CD2 . HIS   Z  195 ? 1.5621 0.4031 1.5194 0.0561  -0.0924 -0.0196 195 HIS   Z CD2 
45710 C  CE1 . HIS   Z  195 ? 1.5650 0.3268 1.5308 0.0613  -0.0935 0.0261  195 HIS   Z CE1 
45711 N  NE2 . HIS   Z  195 ? 1.5618 0.3944 1.5066 0.0454  -0.0900 0.0029  195 HIS   Z NE2 
45712 N  N   . ILE   Z  196 ? 1.3718 0.6381 1.5469 0.1074  -0.1831 0.0829  196 ILE   Z N   
45713 C  CA  . ILE   Z  196 ? 1.4245 0.6829 1.5566 0.1388  -0.2294 0.1040  196 ILE   Z CA  
45714 C  C   . ILE   Z  196 ? 1.4307 0.6914 1.5761 0.1919  -0.2721 0.1160  196 ILE   Z C   
45715 O  O   . ILE   Z  196 ? 1.5138 0.7100 1.6804 0.2907  -0.2791 0.2553  196 ILE   Z O   
45716 C  CB  . ILE   Z  196 ? 1.4515 0.6174 1.5424 0.1484  -0.2336 0.1192  196 ILE   Z CB  
45717 C  CG1 . ILE   Z  196 ? 1.4469 0.6418 1.5127 0.1574  -0.2340 0.1461  196 ILE   Z CG1 
45718 C  CG2 . ILE   Z  196 ? 1.4751 0.6104 1.5821 0.1420  -0.2242 0.0966  196 ILE   Z CG2 
45719 C  CD1 . ILE   Z  196 ? 1.4817 0.6150 1.4851 0.1855  -0.2321 0.1527  196 ILE   Z CD1 
45720 N  N   . GLN   Z  197 ? 1.4142 0.7108 1.5459 0.2150  -0.2591 0.0894  197 GLN   Z N   
45721 C  CA  . GLN   Z  197 ? 1.4161 0.6952 1.4767 0.2289  -0.2667 0.0448  197 GLN   Z CA  
45722 C  C   . GLN   Z  197 ? 1.3875 0.8179 1.4458 0.1979  -0.2205 0.0030  197 GLN   Z C   
45723 O  O   . GLN   Z  197 ? 1.4036 0.8596 1.4432 0.1961  -0.2689 0.0673  197 GLN   Z O   
45724 C  CB  . GLN   Z  197 ? 1.4043 0.6783 1.4841 0.2500  -0.2790 0.0634  197 GLN   Z CB  
45725 C  CG  . GLN   Z  197 ? 1.4115 0.6956 1.5063 0.2553  -0.2830 0.0490  197 GLN   Z CG  
45726 C  CD  . GLN   Z  197 ? 1.4242 0.7190 1.4942 0.2713  -0.2992 0.0588  197 GLN   Z CD  
45727 O  OE1 . GLN   Z  197 ? 1.4247 0.5962 1.4981 0.3143  -0.2614 0.1075  197 GLN   Z OE1 
45728 N  NE2 . GLN   Z  197 ? 1.4284 0.8007 1.5200 0.2986  -0.2988 0.0526  197 GLN   Z NE2 
45729 N  N   . VAL   Z  198 ? 1.4411 0.6357 1.4065 0.1989  -0.2178 -0.0458 198 VAL   Z N   
45730 C  CA  . VAL   Z  198 ? 1.4290 0.6427 1.4114 0.1757  -0.2084 -0.0566 198 VAL   Z CA  
45731 C  C   . VAL   Z  198 ? 1.4821 0.6578 1.4407 0.1080  -0.1989 -0.1141 198 VAL   Z C   
45732 O  O   . VAL   Z  198 ? 1.4728 0.6232 1.4094 0.1814  -0.2094 -0.0495 198 VAL   Z O   
45733 C  CB  . VAL   Z  198 ? 1.4186 0.6066 1.4349 0.2038  -0.1689 -0.0458 198 VAL   Z CB  
45734 C  CG1 . VAL   Z  198 ? 1.3800 0.6235 1.4380 0.1678  -0.1795 -0.0420 198 VAL   Z CG1 
45735 C  CG2 . VAL   Z  198 ? 1.3881 0.6209 1.4075 0.2672  -0.1714 -0.0285 198 VAL   Z CG2 
45736 N  N   . GLY   Z  199 ? 1.4701 0.6759 1.4674 0.1022  -0.2067 -0.1171 199 GLY   Z N   
45737 C  CA  . GLY   Z  199 ? 1.5003 0.7587 1.5182 0.0341  -0.2090 -0.1543 199 GLY   Z CA  
45738 C  C   . GLY   Z  199 ? 1.5346 0.7876 1.5059 0.0222  -0.2055 -0.1286 199 GLY   Z C   
45739 O  O   . GLY   Z  199 ? 1.4958 0.8296 1.5113 0.0181  -0.2143 -0.1737 199 GLY   Z O   
45740 N  N   . ASP   Z  200 ? 1.6020 0.7767 1.4930 -0.0535 -0.1916 -0.1401 200 ASP   Z N   
45741 C  CA  . ASP   Z  200 ? 1.6160 0.7183 1.4856 -0.0922 -0.1691 -0.1354 200 ASP   Z CA  
45742 C  C   . ASP   Z  200 ? 1.5948 0.6354 1.4906 -0.1047 -0.1532 -0.0489 200 ASP   Z C   
45743 O  O   . ASP   Z  200 ? 1.5859 0.5026 1.4807 -0.1704 -0.1206 -0.0320 200 ASP   Z O   
45744 C  CB  . ASP   Z  200 ? 1.6328 0.7603 1.4804 -0.1282 -0.1732 -0.1535 200 ASP   Z CB  
45745 C  CG  . ASP   Z  200 ? 1.6537 0.8391 1.4683 -0.1727 -0.1751 -0.2482 200 ASP   Z CG  
45746 O  OD1 . ASP   Z  200 ? 1.7438 0.9471 1.5289 -0.2550 -0.1476 -0.3168 200 ASP   Z OD1 
45747 O  OD2 . ASP   Z  200 ? 1.6749 0.9428 1.4737 -0.1865 -0.2500 -0.2674 200 ASP   Z OD2 
45748 N  N   . GLY   Z  201 ? 1.5992 0.6149 1.4633 -0.0755 -0.1371 -0.0305 201 GLY   Z N   
45749 C  CA  . GLY   Z  201 ? 1.5848 0.6690 1.5429 -0.0706 -0.1162 -0.0387 201 GLY   Z CA  
45750 C  C   . GLY   Z  201 ? 1.5622 0.6982 1.5605 -0.0548 -0.1194 -0.0636 201 GLY   Z C   
45751 O  O   . GLY   Z  201 ? 1.5697 0.6818 1.5795 -0.0327 -0.1412 -0.0618 201 GLY   Z O   
45752 N  N   . LEU   Z  202 ? 1.5511 0.7159 1.6016 -0.0591 -0.1295 -0.1250 202 LEU   Z N   
45753 C  CA  . LEU   Z  202 ? 1.5151 0.7756 1.6180 -0.0503 -0.1516 -0.1658 202 LEU   Z CA  
45754 C  C   . LEU   Z  202 ? 1.4928 0.8083 1.6411 -0.0271 -0.1707 -0.1349 202 LEU   Z C   
45755 O  O   . LEU   Z  202 ? 1.5118 0.9332 1.6714 -0.0258 -0.2005 -0.1563 202 LEU   Z O   
45756 C  CB  . LEU   Z  202 ? 1.4873 0.7319 1.6113 -0.0629 -0.1411 -0.2237 202 LEU   Z CB  
45757 C  CG  . LEU   Z  202 ? 1.4603 0.7358 1.6497 -0.0280 -0.1388 -0.2733 202 LEU   Z CG  
45758 C  CD1 . LEU   Z  202 ? 1.4662 0.7390 1.6150 0.0105  -0.1493 -0.2841 202 LEU   Z CD1 
45759 C  CD2 . LEU   Z  202 ? 1.4365 0.7329 1.6762 -0.0312 -0.1186 -0.2945 202 LEU   Z CD2 
45760 N  N   . GLU   Z  203 ? 1.4069 0.8535 1.6610 -0.0612 -0.1948 -0.0747 203 GLU   Z N   
45761 C  CA  . GLU   Z  203 ? 1.3747 0.8592 1.6199 -0.0645 -0.1926 -0.0804 203 GLU   Z CA  
45762 C  C   . GLU   Z  203 ? 1.3258 0.7585 1.6061 -0.0695 -0.1566 -0.0749 203 GLU   Z C   
45763 O  O   . GLU   Z  203 ? 1.3354 0.6780 1.4118 -0.0499 -0.1192 -0.1093 203 GLU   Z O   
45764 C  CB  . GLU   Z  203 ? 1.3715 0.9315 1.6755 -0.0726 -0.2180 -0.0089 203 GLU   Z CB  
45765 C  CG  . GLU   Z  203 ? 1.3941 0.9902 1.7307 -0.0257 -0.2376 0.0286  203 GLU   Z CG  
45766 C  CD  . GLU   Z  203 ? 1.4177 1.1246 1.7358 -0.0532 -0.2683 0.0822  203 GLU   Z CD  
45767 O  OE1 . GLU   Z  203 ? 1.5492 1.1669 1.7392 -0.0547 -0.3145 0.1898  203 GLU   Z OE1 
45768 O  OE2 . GLU   Z  203 ? 1.4049 1.2264 1.7307 -0.0699 -0.3010 0.0618  203 GLU   Z OE2 
45769 N  N   . ILE   Z  204 ? 1.3576 0.7147 1.6160 -0.0482 -0.1411 -0.0825 204 ILE   Z N   
45770 C  CA  . ILE   Z  204 ? 1.4352 0.7806 1.6191 0.0150  -0.1700 -0.0863 204 ILE   Z CA  
45771 C  C   . ILE   Z  204 ? 1.4059 0.8095 1.6504 0.0648  -0.1578 -0.0374 204 ILE   Z C   
45772 O  O   . ILE   Z  204 ? 1.4306 0.9873 1.6602 0.0662  -0.1655 0.0282  204 ILE   Z O   
45773 C  CB  . ILE   Z  204 ? 1.4866 0.7213 1.6748 0.0183  -0.1570 -0.0855 204 ILE   Z CB  
45774 C  CG1 . ILE   Z  204 ? 1.5146 0.7229 1.7050 0.0465  -0.1863 -0.0817 204 ILE   Z CG1 
45775 C  CG2 . ILE   Z  204 ? 1.5055 0.7324 1.6720 0.0478  -0.1333 -0.0802 204 ILE   Z CG2 
45776 C  CD1 . ILE   Z  204 ? 1.5237 0.7056 1.7471 0.0460  -0.1774 -0.0690 204 ILE   Z CD1 
45777 N  N   . LEU   Z  205 ? 1.3367 0.7993 1.6461 0.1139  -0.1472 -0.0556 205 LEU   Z N   
45778 C  CA  . LEU   Z  205 ? 1.3385 0.8012 1.6550 0.1326  -0.1274 -0.0533 205 LEU   Z CA  
45779 C  C   . LEU   Z  205 ? 1.3969 0.8160 1.6593 0.1280  -0.1187 -0.0417 205 LEU   Z C   
45780 O  O   . LEU   Z  205 ? 1.3677 0.8399 1.6734 0.1669  -0.1105 -0.0555 205 LEU   Z O   
45781 C  CB  . LEU   Z  205 ? 1.3061 0.7460 1.6194 0.1729  -0.1049 -0.0871 205 LEU   Z CB  
45782 C  CG  . LEU   Z  205 ? 1.3012 0.7732 1.6144 0.1638  -0.0928 -0.1039 205 LEU   Z CG  
45783 C  CD1 . LEU   Z  205 ? 1.2814 0.7931 1.6038 0.1658  -0.0971 -0.1042 205 LEU   Z CD1 
45784 C  CD2 . LEU   Z  205 ? 1.3141 0.7781 1.6054 0.1586  -0.0982 -0.1306 205 LEU   Z CD2 
45785 N  N   . ILE   Z  206 ? 1.3886 0.8607 1.7354 0.1109  -0.1006 -0.0099 206 ILE   Z N   
45786 C  CA  . ILE   Z  206 ? 1.5077 0.9145 1.7436 0.1269  -0.0630 -0.0028 206 ILE   Z CA  
45787 C  C   . ILE   Z  206 ? 1.4551 0.9116 1.7340 0.1332  -0.0677 0.0015  206 ILE   Z C   
45788 O  O   . ILE   Z  206 ? 1.4485 0.9695 1.7242 0.1239  -0.0558 0.0350  206 ILE   Z O   
45789 C  CB  . ILE   Z  206 ? 1.5459 1.0289 1.8179 0.0777  -0.0555 0.0079  206 ILE   Z CB  
45790 C  CG1 . ILE   Z  206 ? 1.6591 1.0700 1.8523 0.0590  -0.0693 -0.0258 206 ILE   Z CG1 
45791 C  CG2 . ILE   Z  206 ? 1.6245 1.0537 1.8263 0.1044  -0.0199 -0.0059 206 ILE   Z CG2 
45792 C  CD1 . ILE   Z  206 ? 1.6994 1.1480 1.8615 0.0440  -0.0821 0.0046  206 ILE   Z CD1 
45793 N  N   . VAL   Z  207 ? 1.4741 0.8216 1.7322 0.1635  -0.0576 -0.0104 207 VAL   Z N   
45794 C  CA  . VAL   Z  207 ? 1.4990 0.7985 1.7585 0.1617  -0.0208 -0.0026 207 VAL   Z CA  
45795 C  C   . VAL   Z  207 ? 1.5466 0.7754 1.7651 0.1670  0.0056  0.0024  207 VAL   Z C   
45796 O  O   . VAL   Z  207 ? 1.5753 0.6957 1.7073 0.2316  0.0602  -0.0569 207 VAL   Z O   
45797 C  CB  . VAL   Z  207 ? 1.5188 0.7162 1.7283 0.1525  -0.0314 -0.0202 207 VAL   Z CB  
45798 C  CG1 . VAL   Z  207 ? 1.5443 0.7714 1.7020 0.1257  -0.0410 -0.0626 207 VAL   Z CG1 
45799 C  CG2 . VAL   Z  207 ? 1.5089 0.6160 1.6991 0.1602  -0.0517 -0.0320 207 VAL   Z CG2 
45800 N  N   . THR   Z  208 ? 1.5145 0.8041 1.8555 0.1492  -0.0170 0.0445  208 THR   Z N   
45801 C  CA  . THR   Z  208 ? 1.4569 0.8419 1.8886 0.1497  0.0008  0.0915  208 THR   Z CA  
45802 C  C   . THR   Z  208 ? 1.5100 0.8369 1.8964 0.1889  0.0087  0.1088  208 THR   Z C   
45803 O  O   . THR   Z  208 ? 1.5708 0.8539 1.8912 0.1984  0.0096  0.1607  208 THR   Z O   
45804 C  CB  . THR   Z  208 ? 1.4684 0.8332 1.9377 0.1038  0.0117  0.1197  208 THR   Z CB  
45805 O  OG1 . THR   Z  208 ? 1.4443 0.7456 1.9417 0.0077  -0.0468 0.0952  208 THR   Z OG1 
45806 C  CG2 . THR   Z  208 ? 1.4507 0.8369 1.9614 0.0864  0.0022  0.1383  208 THR   Z CG2 
45807 N  N   . LYS   Z  209 ? 1.5207 0.9584 1.8920 0.1849  0.0382  0.1066  209 LYS   Z N   
45808 C  CA  . LYS   Z  209 ? 1.5300 0.9735 1.9238 0.2291  0.0290  0.0625  209 LYS   Z CA  
45809 C  C   . LYS   Z  209 ? 1.4889 1.0104 1.9203 0.2960  0.0074  0.0080  209 LYS   Z C   
45810 O  O   . LYS   Z  209 ? 1.5113 0.9912 2.0097 0.3594  0.0644  -0.0232 209 LYS   Z O   
45811 C  CB  . LYS   Z  209 ? 1.5512 1.0308 1.8900 0.2190  0.0374  0.1282  209 LYS   Z CB  
45812 C  CG  . LYS   Z  209 ? 1.5643 1.0754 1.9794 0.1870  -0.0152 0.1946  209 LYS   Z CG  
45813 C  CD  . LYS   Z  209 ? 1.5911 1.1775 1.9937 0.1857  -0.0008 0.1943  209 LYS   Z CD  
45814 C  CE  . LYS   Z  209 ? 1.6433 1.2359 2.1245 0.1332  0.0275  0.2197  209 LYS   Z CE  
45815 N  NZ  . LYS   Z  209 ? 1.6881 1.2850 2.1629 0.1028  -0.0055 0.2428  209 LYS   Z NZ  
45816 N  N   . ASP   Z  210 ? 1.4825 0.9998 1.9440 0.2753  -0.0021 0.0173  210 ASP   Z N   
45817 C  CA  . ASP   Z  210 ? 1.5055 1.0398 1.9080 0.1575  -0.0408 0.0146  210 ASP   Z CA  
45818 C  C   . ASP   Z  210 ? 1.4996 0.9085 1.8282 0.1978  -0.0940 0.0596  210 ASP   Z C   
45819 O  O   . ASP   Z  210 ? 1.6003 0.8955 1.8642 0.1137  -0.1301 0.1025  210 ASP   Z O   
45820 C  CB  . ASP   Z  210 ? 1.5418 1.1746 1.9452 0.0856  -0.0470 0.0008  210 ASP   Z CB  
45821 C  CG  . ASP   Z  210 ? 1.5513 1.3233 1.9690 -0.0474 -0.0246 -0.0299 210 ASP   Z CG  
45822 O  OD1 . ASP   Z  210 ? 1.6766 1.3734 2.0465 -0.1531 -0.0129 -0.1229 210 ASP   Z OD1 
45823 O  OD2 . ASP   Z  210 ? 1.6341 1.4698 2.0363 -0.1694 -0.0866 0.0414  210 ASP   Z OD2 
45824 N  N   . GLY   Z  211 ? 1.5295 0.9067 1.7576 0.2285  -0.1237 0.0283  211 GLY   Z N   
45825 C  CA  . GLY   Z  211 ? 1.5128 0.9630 1.7109 0.2291  -0.1483 0.0014  211 GLY   Z CA  
45826 C  C   . GLY   Z  211 ? 1.4850 1.0514 1.6742 0.2490  -0.0969 -0.0725 211 GLY   Z C   
45827 O  O   . GLY   Z  211 ? 1.5375 1.0590 1.6852 0.2468  -0.0725 -0.0663 211 GLY   Z O   
45828 N  N   . VAL   Z  212 ? 1.4293 1.0702 1.6632 0.2273  -0.1041 -0.0461 212 VAL   Z N   
45829 C  CA  . VAL   Z  212 ? 1.4297 1.0038 1.6598 0.2009  -0.1045 -0.0203 212 VAL   Z CA  
45830 C  C   . VAL   Z  212 ? 1.3913 1.0103 1.6787 0.1852  -0.1011 -0.0079 212 VAL   Z C   
45831 O  O   . VAL   Z  212 ? 1.3858 0.9992 1.6754 0.1704  -0.1244 -0.0215 212 VAL   Z O   
45832 C  CB  . VAL   Z  212 ? 1.4247 0.9693 1.6190 0.2262  -0.1076 -0.0224 212 VAL   Z CB  
45833 C  CG1 . VAL   Z  212 ? 1.4094 0.9869 1.5899 0.2146  -0.1072 -0.0392 212 VAL   Z CG1 
45834 C  CG2 . VAL   Z  212 ? 1.4415 0.9691 1.6022 0.2525  -0.1133 -0.0167 212 VAL   Z CG2 
45835 N  N   . ARG   Z  213 ? 1.4159 1.0367 1.7239 0.1659  -0.0515 0.0447  213 ARG   Z N   
45836 C  CA  . ARG   Z  213 ? 1.4130 1.0196 1.7832 0.0711  -0.0400 0.0670  213 ARG   Z CA  
45837 C  C   . ARG   Z  213 ? 1.4649 1.0035 1.7626 0.0419  -0.0735 0.0104  213 ARG   Z C   
45838 O  O   . ARG   Z  213 ? 1.4737 1.0746 1.7971 -0.0179 -0.1318 0.0220  213 ARG   Z O   
45839 C  CB  . ARG   Z  213 ? 1.3967 1.0169 1.8678 0.1181  0.0174  0.0755  213 ARG   Z CB  
45840 C  CG  . ARG   Z  213 ? 1.3334 1.1063 1.9212 0.1004  0.0104  0.0931  213 ARG   Z CG  
45841 C  CD  . ARG   Z  213 ? 1.3574 1.1879 2.0422 0.1050  0.0634  0.1211  213 ARG   Z CD  
45842 N  NE  . ARG   Z  213 ? 1.3667 1.1731 2.1252 0.0592  0.0926  0.1405  213 ARG   Z NE  
45843 C  CZ  . ARG   Z  213 ? 1.3325 1.1267 2.1252 0.0776  0.1262  0.1883  213 ARG   Z CZ  
45844 N  NH1 . ARG   Z  213 ? 1.3343 1.2120 2.1474 0.0895  0.1582  0.1170  213 ARG   Z NH1 
45845 N  NH2 . ARG   Z  213 ? 1.2817 1.1117 2.1515 0.0793  0.1167  0.1917  213 ARG   Z NH2 
45846 N  N   . LYS   Z  214 ? 1.5189 1.0241 1.7565 0.0006  -0.1075 0.0328  214 LYS   Z N   
45847 C  CA  . LYS   Z  214 ? 1.5279 0.9577 1.6813 -0.0249 -0.1325 0.0422  214 LYS   Z CA  
45848 C  C   . LYS   Z  214 ? 1.5943 0.8876 1.7301 0.0068  -0.1771 0.0136  214 LYS   Z C   
45849 O  O   . LYS   Z  214 ? 1.6348 0.6317 1.7534 -0.0230 -0.2439 0.0282  214 LYS   Z O   
45850 C  CB  . LYS   Z  214 ? 1.5214 1.0386 1.6758 -0.0195 -0.1185 0.0476  214 LYS   Z CB  
45851 C  CG  . LYS   Z  214 ? 1.4880 1.1067 1.6027 -0.0427 -0.0417 0.0859  214 LYS   Z CG  
45852 C  CD  . LYS   Z  214 ? 1.5152 1.2512 1.5875 -0.0373 -0.0043 0.0688  214 LYS   Z CD  
45853 C  CE  . LYS   Z  214 ? 1.5172 1.2823 1.5414 -0.0684 0.0270  0.0965  214 LYS   Z CE  
45854 N  NZ  . LYS   Z  214 ? 1.5133 1.2905 1.5762 -0.0604 0.0173  0.1346  214 LYS   Z NZ  
45855 N  N   . GLU   Z  215 ? 1.5801 0.8994 1.7464 0.0239  -0.1726 -0.0447 215 GLU   Z N   
45856 C  CA  . GLU   Z  215 ? 1.6030 0.8588 1.7997 0.0545  -0.1476 -0.0666 215 GLU   Z CA  
45857 C  C   . GLU   Z  215 ? 1.5736 0.7583 1.7767 0.0534  -0.1741 -0.0088 215 GLU   Z C   
45858 O  O   . GLU   Z  215 ? 1.5975 0.6331 1.7190 0.0846  -0.1840 0.0619  215 GLU   Z O   
45859 C  CB  . GLU   Z  215 ? 1.6453 0.8721 1.7991 0.0588  -0.1007 -0.0908 215 GLU   Z CB  
45860 C  CG  . GLU   Z  215 ? 1.6589 1.0093 1.8316 0.0606  -0.0681 -0.1137 215 GLU   Z CG  
45861 C  CD  . GLU   Z  215 ? 1.7212 0.9937 1.8605 0.0567  -0.0584 -0.1018 215 GLU   Z CD  
45862 O  OE1 . GLU   Z  215 ? 1.7033 1.2293 1.9180 0.1020  -0.0242 -0.1145 215 GLU   Z OE1 
45863 O  OE2 . GLU   Z  215 ? 1.7344 1.0006 1.8474 0.1159  -0.0643 -0.2240 215 GLU   Z OE2 
45864 N  N   . PHE   Z  216 ? 1.5618 0.7355 1.7895 0.0447  -0.1697 -0.0141 216 PHE   Z N   
45865 C  CA  . PHE   Z  216 ? 1.5044 0.7704 1.7922 0.0785  -0.2088 -0.0215 216 PHE   Z CA  
45866 C  C   . PHE   Z  216 ? 1.5543 0.7365 1.8928 0.1221  -0.2036 -0.0702 216 PHE   Z C   
45867 O  O   . PHE   Z  216 ? 1.5936 0.8618 2.0195 0.0324  -0.2350 -0.0874 216 PHE   Z O   
45868 C  CB  . PHE   Z  216 ? 1.4469 0.7654 1.7524 0.0878  -0.2240 -0.0534 216 PHE   Z CB  
45869 C  CG  . PHE   Z  216 ? 1.4204 0.7975 1.6810 0.0936  -0.2591 -0.0514 216 PHE   Z CG  
45870 C  CD1 . PHE   Z  216 ? 1.4146 0.7998 1.6080 0.0774  -0.2447 -0.0568 216 PHE   Z CD1 
45871 C  CD2 . PHE   Z  216 ? 1.4328 0.9028 1.6398 0.1078  -0.2858 -0.0510 216 PHE   Z CD2 
45872 C  CE1 . PHE   Z  216 ? 1.3893 0.8688 1.5651 0.0730  -0.2422 -0.0552 216 PHE   Z CE1 
45873 C  CE2 . PHE   Z  216 ? 1.4124 0.9665 1.6110 0.1026  -0.2834 -0.0538 216 PHE   Z CE2 
45874 C  CZ  . PHE   Z  216 ? 1.4056 0.9511 1.5574 0.0781  -0.2707 -0.0628 216 PHE   Z CZ  
45875 N  N   . TYR   Z  217 ? 1.4882 0.7668 1.8962 0.1184  -0.2508 -0.0617 217 TYR   Z N   
45876 C  CA  . TYR   Z  217 ? 1.4780 0.7140 1.9153 0.1807  -0.2939 -0.0048 217 TYR   Z CA  
45877 C  C   . TYR   Z  217 ? 1.4757 0.6562 1.8906 0.1989  -0.3395 -0.0080 217 TYR   Z C   
45878 O  O   . TYR   Z  217 ? 1.4593 0.6115 1.9193 0.2524  -0.3657 0.0527  217 TYR   Z O   
45879 C  CB  . TYR   Z  217 ? 1.4539 0.7131 1.9067 0.1886  -0.2894 -0.0129 217 TYR   Z CB  
45880 C  CG  . TYR   Z  217 ? 1.4688 0.7199 1.9150 0.1846  -0.2834 -0.0301 217 TYR   Z CG  
45881 C  CD1 . TYR   Z  217 ? 1.4756 0.7685 1.9709 0.1528  -0.2824 -0.0314 217 TYR   Z CD1 
45882 C  CD2 . TYR   Z  217 ? 1.4648 0.7303 1.8934 0.1851  -0.2891 -0.0158 217 TYR   Z CD2 
45883 C  CE1 . TYR   Z  217 ? 1.4636 0.8194 1.9866 0.1297  -0.2571 -0.0339 217 TYR   Z CE1 
45884 C  CE2 . TYR   Z  217 ? 1.4603 0.7651 1.9303 0.1602  -0.2440 -0.0009 217 TYR   Z CE2 
45885 C  CZ  . TYR   Z  217 ? 1.4534 0.7976 1.9660 0.1333  -0.2202 -0.0287 217 TYR   Z CZ  
45886 O  OH  . TYR   Z  217 ? 1.4086 0.8091 2.0529 0.1437  -0.1978 0.0033  217 TYR   Z OH  
45887 N  N   . GLU   Z  218 ? 1.5325 0.6384 1.9068 0.1690  -0.3313 -0.0168 218 GLU   Z N   
45888 C  CA  . GLU   Z  218 ? 1.5867 0.6047 1.8603 0.1138  -0.3283 -0.0579 218 GLU   Z CA  
45889 C  C   . GLU   Z  218 ? 1.5326 0.5456 1.7628 0.0610  -0.3028 -0.0894 218 GLU   Z C   
45890 O  O   . GLU   Z  218 ? 1.5260 0.3755 1.7437 0.0828  -0.3071 -0.1154 218 GLU   Z O   
45891 C  CB  . GLU   Z  218 ? 1.6416 0.6357 1.8902 0.0938  -0.3723 -0.0319 218 GLU   Z CB  
45892 C  CG  . GLU   Z  218 ? 1.6802 0.6691 1.9323 0.0963  -0.3820 0.0073  218 GLU   Z CG  
45893 C  CD  . GLU   Z  218 ? 1.7134 0.7340 1.9306 0.0930  -0.3785 0.0202  218 GLU   Z CD  
45894 O  OE1 . GLU   Z  218 ? 1.7947 0.6013 1.9958 0.0990  -0.3811 0.0866  218 GLU   Z OE1 
45895 O  OE2 . GLU   Z  218 ? 1.7020 0.7962 1.9748 -0.0399 -0.3888 0.0398  218 GLU   Z OE2 
45896 N  N   . LEU   Z  219 ? 1.5197 0.6807 1.7286 0.0345  -0.2993 -0.1176 219 LEU   Z N   
45897 C  CA  . LEU   Z  219 ? 1.5175 0.7493 1.6873 0.0548  -0.2851 -0.0904 219 LEU   Z CA  
45898 C  C   . LEU   Z  219 ? 1.5745 0.7964 1.6809 0.0528  -0.3249 -0.1387 219 LEU   Z C   
45899 O  O   . LEU   Z  219 ? 1.6181 0.8942 1.6187 0.0873  -0.3297 -0.2019 219 LEU   Z O   
45900 C  CB  . LEU   Z  219 ? 1.5021 0.7336 1.6487 0.0139  -0.2326 -0.0965 219 LEU   Z CB  
45901 C  CG  . LEU   Z  219 ? 1.4549 0.6830 1.6534 0.0080  -0.1847 -0.0713 219 LEU   Z CG  
45902 C  CD1 . LEU   Z  219 ? 1.4382 0.6674 1.6153 0.0226  -0.1698 -0.0603 219 LEU   Z CD1 
45903 C  CD2 . LEU   Z  219 ? 1.4383 0.7415 1.6496 0.0085  -0.1535 -0.0840 219 LEU   Z CD2 
45904 N  N   . LYS   Z  220 ? 1.5969 0.7575 1.7611 0.0243  -0.3472 -0.1607 220 LYS   Z N   
45905 C  CA  . LYS   Z  220 ? 1.6436 0.8195 1.7650 0.0332  -0.3474 -0.1743 220 LYS   Z CA  
45906 C  C   . LYS   Z  220 ? 1.6820 0.8699 1.7655 0.0112  -0.3375 -0.1522 220 LYS   Z C   
45907 O  O   . LYS   Z  220 ? 1.7771 0.8398 1.7893 -0.0386 -0.3138 -0.2407 220 LYS   Z O   
45908 C  CB  . LYS   Z  220 ? 1.6823 0.8345 1.8088 0.0165  -0.3405 -0.1352 220 LYS   Z CB  
45909 C  CG  . LYS   Z  220 ? 1.6960 0.7888 1.8376 0.0151  -0.3655 -0.1482 220 LYS   Z CG  
45910 C  CD  . LYS   Z  220 ? 1.7497 0.7992 1.8326 -0.0241 -0.3561 -0.1338 220 LYS   Z CD  
45911 C  CE  . LYS   Z  220 ? 1.8063 0.7900 1.7985 -0.0318 -0.3630 -0.1676 220 LYS   Z CE  
45912 N  NZ  . LYS   Z  220 ? 1.8669 0.7284 1.8359 -0.0662 -0.3527 -0.2078 220 LYS   Z NZ  
45913 N  N   . ARG   Z  221 ? 1.6926 0.9109 1.7555 0.0348  -0.3788 -0.1234 221 ARG   Z N   
45914 C  CA  . ARG   Z  221 ? 1.7009 0.8943 1.7224 0.0610  -0.3732 -0.1260 221 ARG   Z CA  
45915 C  C   . ARG   Z  221 ? 1.7412 0.8315 1.7225 0.0852  -0.4120 -0.1082 221 ARG   Z C   
45916 O  O   . ARG   Z  221 ? 1.7881 0.8144 1.5560 0.1132  -0.4315 -0.1476 221 ARG   Z O   
45917 C  CB  . ARG   Z  221 ? 1.6884 1.0156 1.6940 0.0398  -0.3919 -0.1559 221 ARG   Z CB  
45918 C  CG  . ARG   Z  221 ? 1.6263 1.0926 1.6735 0.0446  -0.3719 -0.1794 221 ARG   Z CG  
45919 C  CD  . ARG   Z  221 ? 1.6488 1.1405 1.6336 0.0279  -0.3729 -0.1813 221 ARG   Z CD  
45920 N  NE  . ARG   Z  221 ? 1.6637 1.1469 1.6121 0.0265  -0.3887 -0.1855 221 ARG   Z NE  
45921 C  CZ  . ARG   Z  221 ? 1.6263 1.1069 1.5596 0.0103  -0.3721 -0.2704 221 ARG   Z CZ  
45922 N  NH1 . ARG   Z  221 ? 1.6163 1.0652 1.5442 -0.0167 -0.3657 -0.2544 221 ARG   Z NH1 
45923 N  NH2 . ARG   Z  221 ? 1.6305 1.1346 1.5816 -0.0147 -0.3683 -0.2454 221 ARG   Z NH2 
45924 N  N   . ASP   Z  222 ? 1.7412 0.7707 1.8978 0.1145  -0.4225 -0.1339 222 ASP   Z N   
45925 C  CA  . ASP   Z  222 ? 1.7383 0.7612 1.9958 0.1101  -0.4277 -0.1240 222 ASP   Z CA  
45926 C  C   . ASP   Z  222 ? 1.7548 0.6061 2.0776 0.1653  -0.4800 -0.1062 222 ASP   Z C   
45927 O  O   . ASP   Z  222 ? 1.8512 0.3222 2.3243 0.1267  -0.4658 -0.0345 222 ASP   Z O   
45928 C  CB  . ASP   Z  222 ? 1.6219 0.8038 1.9808 0.0700  -0.4142 -0.1557 222 ASP   Z CB  
45929 C  CG  . ASP   Z  222 ? 1.4955 0.7472 2.0231 0.0401  -0.4077 -0.1094 222 ASP   Z CG  
45930 O  OD1 . ASP   Z  222 ? 1.3753 0.8157 1.9543 0.0088  -0.3250 -0.0762 222 ASP   Z OD1 
45931 O  OD2 . ASP   Z  222 ? 1.3999 0.7015 1.9459 0.1305  -0.3962 -0.2146 222 ASP   Z OD2 
45932 O  OXT . ASP   Z  222 ? 1.7715 0.6175 2.2103 0.2316  -0.5672 0.0635  222 ASP   Z OXT 
45933 N  N   . THR   AA 14  ? 1.6092 1.1049 1.0637 -0.1588 -0.0769 0.0901  1   THR   a N   
45934 C  CA  . THR   AA 14  ? 1.6805 1.1405 1.2555 -0.1974 -0.0754 0.0063  1   THR   a CA  
45935 C  C   . THR   AA 14  ? 1.5324 0.9233 1.2093 -0.1565 -0.1641 0.0498  1   THR   a C   
45936 O  O   . THR   AA 14  ? 1.5219 0.9584 1.3184 -0.1428 -0.1816 0.1589  1   THR   a O   
45937 C  CB  . THR   AA 14  ? 1.8429 1.1493 1.4161 -0.1471 -0.0788 0.0210  1   THR   a CB  
45938 O  OG1 . THR   AA 14  ? 2.0114 1.1777 1.5292 -0.2466 0.0549  -0.0720 1   THR   a OG1 
45939 C  CG2 . THR   AA 14  ? 1.9030 1.1928 1.4479 -0.1823 0.0285  -0.0329 1   THR   a CG2 
45940 N  N   . GLN   AA 15  ? 1.5727 0.7967 1.2532 -0.1019 -0.1483 -0.0593 2   GLN   a N   
45941 C  CA  . GLN   AA 15  ? 1.5465 0.7361 1.2371 -0.0280 -0.1914 -0.0582 2   GLN   a CA  
45942 C  C   . GLN   AA 15  ? 1.5172 0.6609 1.2655 0.0362  -0.2148 0.0602  2   GLN   a C   
45943 O  O   . GLN   AA 15  ? 1.4708 0.5818 1.4182 0.1280  -0.2939 0.1547  2   GLN   a O   
45944 C  CB  . GLN   AA 15  ? 1.5579 0.6014 1.2388 -0.0116 -0.1812 -0.1130 2   GLN   a CB  
45945 C  CG  . GLN   AA 15  ? 1.5840 0.6147 1.2843 -0.0332 -0.1279 -0.1961 2   GLN   a CG  
45946 C  CD  . GLN   AA 15  ? 1.5718 0.6570 1.3317 -0.0253 -0.1160 -0.2204 2   GLN   a CD  
45947 O  OE1 . GLN   AA 15  ? 1.5870 0.3050 1.4189 -0.0706 0.0099  -0.2770 2   GLN   a OE1 
45948 N  NE2 . GLN   AA 15  ? 1.5929 0.7312 1.4699 0.0038  -0.0589 -0.3038 2   GLN   a NE2 
45949 N  N   . GLN   AA 16  ? 1.4659 0.5963 1.2544 0.0462  -0.2551 0.0353  3   GLN   a N   
45950 C  CA  . GLN   AA 16  ? 1.4088 0.5480 1.2501 0.0793  -0.2733 0.0572  3   GLN   a CA  
45951 C  C   . GLN   AA 16  ? 1.3941 0.4078 1.2508 0.0689  -0.2762 0.0447  3   GLN   a C   
45952 O  O   . GLN   AA 16  ? 1.3671 0.4438 1.2208 0.0801  -0.3176 0.0920  3   GLN   a O   
45953 C  CB  . GLN   AA 16  ? 1.4129 0.6436 1.3138 0.1301  -0.3125 0.0661  3   GLN   a CB  
45954 C  CG  . GLN   AA 16  ? 1.4231 0.7283 1.3827 0.1124  -0.3052 0.0750  3   GLN   a CG  
45955 C  CD  . GLN   AA 16  ? 1.4423 0.8329 1.4888 0.1666  -0.3129 0.0193  3   GLN   a CD  
45956 O  OE1 . GLN   AA 16  ? 1.4939 0.8666 1.5702 0.1508  -0.2829 -0.0639 3   GLN   a OE1 
45957 N  NE2 . GLN   AA 16  ? 1.4483 0.9938 1.5682 0.1512  -0.3390 0.0151  3   GLN   a NE2 
45958 N  N   . PRO   AA 17  ? 1.3901 0.3452 1.1889 0.1034  -0.2703 0.0319  4   PRO   a N   
45959 C  CA  . PRO   AA 17  ? 1.3757 0.3380 1.1695 0.1065  -0.2665 -0.0051 4   PRO   a CA  
45960 C  C   . PRO   AA 17  ? 1.4360 0.2808 1.1814 0.0965  -0.2532 -0.0387 4   PRO   a C   
45961 O  O   . PRO   AA 17  ? 1.4284 0.3531 1.2551 0.2055  -0.2461 -0.0962 4   PRO   a O   
45962 C  CB  . PRO   AA 17  ? 1.3571 0.3535 1.1661 0.1230  -0.2621 -0.0011 4   PRO   a CB  
45963 C  CG  . PRO   AA 17  ? 1.3533 0.3898 1.1479 0.1305  -0.2583 0.0181  4   PRO   a CG  
45964 C  CD  . PRO   AA 17  ? 1.3572 0.4164 1.1597 0.0900  -0.2556 0.0184  4   PRO   a CD  
45965 N  N   . ILE   AA 18  ? 1.4640 0.2466 1.1707 0.0774  -0.2447 -0.0584 5   ILE   a N   
45966 C  CA  . ILE   AA 18  ? 1.4968 0.2728 1.1371 0.1166  -0.2531 -0.0459 5   ILE   a CA  
45967 C  C   . ILE   AA 18  ? 1.5074 0.3588 1.1348 0.0836  -0.2512 -0.0306 5   ILE   a C   
45968 O  O   . ILE   AA 18  ? 1.5205 0.3230 1.1083 0.0712  -0.2769 0.0776  5   ILE   a O   
45969 C  CB  . ILE   AA 18  ? 1.4454 0.3936 1.1527 0.0984  -0.2505 -0.0785 5   ILE   a CB  
45970 C  CG1 . ILE   AA 18  ? 1.4517 0.3943 1.1243 0.1545  -0.2585 -0.0347 5   ILE   a CG1 
45971 C  CG2 . ILE   AA 18  ? 1.4793 0.4233 1.1788 0.1355  -0.2540 -0.1184 5   ILE   a CG2 
45972 C  CD1 . ILE   AA 18  ? 1.4811 0.3011 1.1307 0.1306  -0.2467 -0.0780 5   ILE   a CD1 
45973 N  N   . VAL   AA 19  ? 1.4775 0.3515 1.1208 0.0890  -0.3026 -0.0626 6   VAL   a N   
45974 C  CA  . VAL   AA 19  ? 1.4811 0.3311 1.1253 0.0755  -0.3159 -0.0628 6   VAL   a CA  
45975 C  C   . VAL   AA 19  ? 1.4925 0.3092 1.1013 0.1107  -0.3106 -0.0529 6   VAL   a C   
45976 O  O   . VAL   AA 19  ? 1.4838 0.3607 1.1059 0.0869  -0.3279 -0.0961 6   VAL   a O   
45977 C  CB  . VAL   AA 19  ? 1.4924 0.4049 1.1199 0.0215  -0.3072 -0.0414 6   VAL   a CB  
45978 C  CG1 . VAL   AA 19  ? 1.5164 0.4115 1.1443 -0.0273 -0.3155 -0.0829 6   VAL   a CG1 
45979 C  CG2 . VAL   AA 19  ? 1.4880 0.4378 1.1246 0.0367  -0.3119 -0.0112 6   VAL   a CG2 
45980 N  N   . THR   AA 20  ? 1.5151 0.2906 1.1039 0.1033  -0.2973 -0.0272 7   THR   a N   
45981 C  CA  . THR   AA 20  ? 1.5322 0.3407 1.1202 0.1095  -0.2729 -0.0207 7   THR   a CA  
45982 C  C   . THR   AA 20  ? 1.4907 0.2960 1.1578 0.1087  -0.2745 -0.0216 7   THR   a C   
45983 O  O   . THR   AA 20  ? 1.4474 0.3324 1.1744 0.0785  -0.2945 -0.0634 7   THR   a O   
45984 C  CB  . THR   AA 20  ? 1.5903 0.3880 1.1245 0.0539  -0.2509 0.0070  7   THR   a CB  
45985 O  OG1 . THR   AA 20  ? 1.6692 0.3899 1.1669 -0.0033 -0.1876 -0.0188 7   THR   a OG1 
45986 C  CG2 . THR   AA 20  ? 1.6034 0.4461 1.1048 0.0695  -0.2336 -0.0482 7   THR   a CG2 
45987 N  N   . GLY   AA 21  ? 1.5054 0.2982 1.1493 0.1175  -0.2552 -0.0179 8   GLY   a N   
45988 C  CA  . GLY   AA 21  ? 1.5404 0.3393 1.1638 0.1277  -0.2842 -0.0010 8   GLY   a CA  
45989 C  C   . GLY   AA 21  ? 1.5614 0.3446 1.1678 0.1543  -0.2780 0.0399  8   GLY   a C   
45990 O  O   . GLY   AA 21  ? 1.6189 0.1958 1.1818 0.1636  -0.2989 -0.0691 8   GLY   a O   
45991 N  N   . THR   AA 22  ? 1.5505 0.4480 1.1717 0.1497  -0.3409 0.0326  9   THR   a N   
45992 C  CA  . THR   AA 22  ? 1.5394 0.5266 1.1874 0.1376  -0.3326 0.0727  9   THR   a CA  
45993 C  C   . THR   AA 22  ? 1.4963 0.4903 1.1829 0.1045  -0.4131 0.1073  9   THR   a C   
45994 O  O   . THR   AA 22  ? 1.5409 0.4998 1.2212 0.1179  -0.4176 0.0802  9   THR   a O   
45995 C  CB  . THR   AA 22  ? 1.6016 0.6271 1.1780 0.2206  -0.2904 0.0215  9   THR   a CB  
45996 O  OG1 . THR   AA 22  ? 1.6270 0.7179 1.2527 0.2315  -0.1770 0.0505  9   THR   a OG1 
45997 C  CG2 . THR   AA 22  ? 1.6118 0.7070 1.1760 0.2463  -0.2850 0.0415  9   THR   a CG2 
45998 N  N   . SER   AA 23  ? 1.4580 0.5527 1.1762 0.0914  -0.4573 0.1458  10  SER   a N   
45999 C  CA  . SER   AA 23  ? 1.4434 0.5664 1.2346 0.0210  -0.4322 0.1459  10  SER   a CA  
46000 C  C   . SER   AA 23  ? 1.4066 0.5017 1.2584 0.0253  -0.3989 0.0770  10  SER   a C   
46001 O  O   . SER   AA 23  ? 1.3453 0.4480 1.3322 -0.0022 -0.3784 0.1652  10  SER   a O   
46002 C  CB  . SER   AA 23  ? 1.4663 0.6229 1.2977 -0.0678 -0.4435 0.2121  10  SER   a CB  
46003 O  OG  . SER   AA 23  ? 1.3882 0.7242 1.3982 -0.0431 -0.5175 0.2922  10  SER   a OG  
46004 N  N   . VAL   AA 24  ? 1.4294 0.4130 1.2508 -0.0015 -0.4350 0.0245  11  VAL   a N   
46005 C  CA  . VAL   AA 24  ? 1.4518 0.4575 1.2273 0.0135  -0.4533 0.0487  11  VAL   a CA  
46006 C  C   . VAL   AA 24  ? 1.4651 0.3690 1.1953 0.0064  -0.4424 -0.0061 11  VAL   a C   
46007 O  O   . VAL   AA 24  ? 1.4517 0.2826 1.1519 -0.0023 -0.4459 -0.0963 11  VAL   a O   
46008 C  CB  . VAL   AA 24  ? 1.4594 0.4633 1.2249 0.0431  -0.4542 0.0443  11  VAL   a CB  
46009 C  CG1 . VAL   AA 24  ? 1.4727 0.4605 1.2563 0.0613  -0.4366 0.0365  11  VAL   a CG1 
46010 C  CG2 . VAL   AA 24  ? 1.4517 0.5539 1.2188 0.0578  -0.4506 0.0863  11  VAL   a CG2 
46011 N  N   . ILE   AA 25  ? 1.4628 0.3950 1.2357 0.0120  -0.4597 0.0050  12  ILE   a N   
46012 C  CA  . ILE   AA 25  ? 1.4724 0.3910 1.2800 0.0085  -0.4433 0.0085  12  ILE   a CA  
46013 C  C   . ILE   AA 25  ? 1.4616 0.3872 1.2880 0.0001  -0.4351 0.0138  12  ILE   a C   
46014 O  O   . ILE   AA 25  ? 1.4888 0.2932 1.3014 0.0295  -0.5061 0.0172  12  ILE   a O   
46015 C  CB  . ILE   AA 25  ? 1.5115 0.3370 1.2894 0.0176  -0.4450 0.0437  12  ILE   a CB  
46016 C  CG1 . ILE   AA 25  ? 1.5235 0.3615 1.2868 -0.0035 -0.4474 0.0164  12  ILE   a CG1 
46017 C  CG2 . ILE   AA 25  ? 1.5551 0.2821 1.2960 0.0218  -0.4231 0.0319  12  ILE   a CG2 
46018 C  CD1 . ILE   AA 25  ? 1.5232 0.3470 1.3212 -0.0091 -0.4598 0.0218  12  ILE   a CD1 
46019 N  N   . SER   AA 26  ? 1.4370 0.4540 1.3506 0.0214  -0.4333 -0.0691 13  SER   a N   
46020 C  CA  . SER   AA 26  ? 1.4456 0.4601 1.3618 0.0331  -0.4442 -0.0755 13  SER   a CA  
46021 C  C   . SER   AA 26  ? 1.4048 0.5044 1.4210 0.0274  -0.4577 -0.1439 13  SER   a C   
46022 O  O   . SER   AA 26  ? 1.3507 0.5256 1.3827 0.0020  -0.4505 -0.1581 13  SER   a O   
46023 C  CB  . SER   AA 26  ? 1.4293 0.4587 1.3642 0.0458  -0.4339 -0.0803 13  SER   a CB  
46024 O  OG  . SER   AA 26  ? 1.4268 0.4964 1.3857 0.0619  -0.4166 -0.0314 13  SER   a OG  
46025 N  N   . MET   AA 27  ? 1.4661 0.5223 1.4389 0.0500  -0.4851 -0.0948 14  MET   a N   
46026 C  CA  . MET   AA 27  ? 1.4805 0.5914 1.4799 0.0802  -0.4654 -0.0313 14  MET   a CA  
46027 C  C   . MET   AA 27  ? 1.5215 0.5723 1.4473 0.0671  -0.4634 0.0284  14  MET   a C   
46028 O  O   . MET   AA 27  ? 1.6104 0.4289 1.5269 0.0986  -0.5345 0.0656  14  MET   a O   
46029 C  CB  . MET   AA 27  ? 1.5095 0.6367 1.5156 0.0507  -0.4849 -0.0500 14  MET   a CB  
46030 C  CG  . MET   AA 27  ? 1.5332 0.7074 1.5280 0.0528  -0.5052 -0.0239 14  MET   a CG  
46031 S  SD  . MET   AA 27  ? 1.5701 0.7574 1.5777 0.0030  -0.5049 -0.0451 14  MET   a SD  
46032 C  CE  . MET   AA 27  ? 1.5572 0.7325 1.6430 0.0231  -0.5094 -0.0398 14  MET   a CE  
46033 N  N   . LYS   AA 28  ? 1.4928 0.6057 1.4739 0.1051  -0.4721 0.0229  15  LYS   a N   
46034 C  CA  . LYS   AA 28  ? 1.4755 0.5966 1.4877 0.0947  -0.4787 0.0120  15  LYS   a CA  
46035 C  C   . LYS   AA 28  ? 1.5185 0.6116 1.5541 0.0799  -0.4986 -0.0416 15  LYS   a C   
46036 O  O   . LYS   AA 28  ? 1.4910 0.6384 1.5348 -0.0145 -0.5388 -0.0951 15  LYS   a O   
46037 C  CB  . LYS   AA 28  ? 1.4513 0.6620 1.4933 0.1232  -0.4623 0.0431  15  LYS   a CB  
46038 C  CG  . LYS   AA 28  ? 1.4099 0.7316 1.4608 0.1238  -0.4538 0.0553  15  LYS   a CG  
46039 C  CD  . LYS   AA 28  ? 1.4198 0.8639 1.4911 0.1336  -0.4243 0.0433  15  LYS   a CD  
46040 C  CE  . LYS   AA 28  ? 1.4385 0.9285 1.4955 0.1216  -0.4332 0.0316  15  LYS   a CE  
46041 N  NZ  . LYS   AA 28  ? 1.4703 1.0408 1.5425 0.1450  -0.3895 0.0179  15  LYS   a NZ  
46042 N  N   . TYR   AA 29  ? 1.5635 0.5676 1.6029 0.0990  -0.5071 -0.0444 16  TYR   a N   
46043 C  CA  . TYR   AA 29  ? 1.5887 0.6509 1.6398 0.1060  -0.5349 -0.0500 16  TYR   a CA  
46044 C  C   . TYR   AA 29  ? 1.5603 0.7680 1.7349 0.1481  -0.5180 -0.0522 16  TYR   a C   
46045 O  O   . TYR   AA 29  ? 1.5675 0.8752 1.7104 0.1079  -0.4864 -0.0915 16  TYR   a O   
46046 C  CB  . TYR   AA 29  ? 1.6330 0.6501 1.6249 0.1210  -0.5522 -0.0419 16  TYR   a CB  
46047 C  CG  . TYR   AA 29  ? 1.6459 0.7070 1.5947 0.0886  -0.5787 -0.0137 16  TYR   a CG  
46048 C  CD1 . TYR   AA 29  ? 1.6353 0.7910 1.5870 0.1028  -0.5797 -0.0117 16  TYR   a CD1 
46049 C  CD2 . TYR   AA 29  ? 1.6386 0.8633 1.5949 0.0881  -0.6440 0.0029  16  TYR   a CD2 
46050 C  CE1 . TYR   AA 29  ? 1.6492 0.8712 1.5727 0.0972  -0.6110 0.0555  16  TYR   a CE1 
46051 C  CE2 . TYR   AA 29  ? 1.6467 0.9155 1.5826 0.0917  -0.6766 0.0556  16  TYR   a CE2 
46052 C  CZ  . TYR   AA 29  ? 1.6732 0.8609 1.5566 0.0420  -0.6525 0.0929  16  TYR   a CZ  
46053 O  OH  . TYR   AA 29  ? 1.6743 0.7929 1.5378 0.0891  -0.7387 0.1084  16  TYR   a OH  
46054 N  N   . ASP   AA 30  ? 1.5942 0.8118 1.7712 0.1322  -0.5637 -0.0834 17  ASP   a N   
46055 C  CA  . ASP   AA 30  ? 1.5695 0.8702 1.8388 0.1483  -0.5849 -0.0776 17  ASP   a CA  
46056 C  C   . ASP   AA 30  ? 1.5749 0.8632 1.8054 0.1619  -0.6054 -0.1140 17  ASP   a C   
46057 O  O   . ASP   AA 30  ? 1.5308 0.9270 1.8663 0.2208  -0.6020 -0.1405 17  ASP   a O   
46058 C  CB  . ASP   AA 30  ? 1.5634 0.8598 1.9396 0.1351  -0.6070 -0.0782 17  ASP   a CB  
46059 C  CG  . ASP   AA 30  ? 1.5964 0.8328 1.9561 0.1336  -0.6033 -0.0490 17  ASP   a CG  
46060 O  OD1 . ASP   AA 30  ? 1.6315 0.9009 2.0415 0.1258  -0.5541 0.0025  17  ASP   a OD1 
46061 O  OD2 . ASP   AA 30  ? 1.5233 0.7363 2.0675 0.1514  -0.6333 -0.0286 17  ASP   a OD2 
46062 N  N   . ASN   AA 31  ? 1.6439 0.8179 1.7576 0.1228  -0.6357 -0.1062 18  ASN   a N   
46063 C  CA  . ASN   AA 31  ? 1.6925 0.8162 1.7660 0.0999  -0.6490 -0.1083 18  ASN   a CA  
46064 C  C   . ASN   AA 31  ? 1.6950 0.8015 1.7473 0.0680  -0.6135 -0.0821 18  ASN   a C   
46065 O  O   . ASN   AA 31  ? 1.8176 0.8257 1.8131 0.0143  -0.5749 -0.0381 18  ASN   a O   
46066 C  CB  . ASN   AA 31  ? 1.7311 0.7934 1.7836 0.1180  -0.7038 -0.1139 18  ASN   a CB  
46067 C  CG  . ASN   AA 31  ? 1.7512 0.8124 1.8387 0.1474  -0.7516 -0.1269 18  ASN   a CG  
46068 O  OD1 . ASN   AA 31  ? 1.8925 0.8385 1.8435 0.1936  -0.7618 -0.1549 18  ASN   a OD1 
46069 N  ND2 . ASN   AA 31  ? 1.7565 0.8446 1.8192 0.1549  -0.7584 -0.1011 18  ASN   a ND2 
46070 N  N   . GLY   AA 32  ? 1.6716 0.6342 1.6830 0.0129  -0.5698 -0.1405 19  GLY   a N   
46071 C  CA  . GLY   AA 32  ? 1.6700 0.5719 1.6215 -0.0017 -0.5349 -0.1426 19  GLY   a CA  
46072 C  C   . GLY   AA 32  ? 1.6600 0.5387 1.5686 -0.0166 -0.5100 -0.1583 19  GLY   a C   
46073 O  O   . GLY   AA 32  ? 1.6702 0.6193 1.5121 -0.0234 -0.5116 -0.1195 19  GLY   a O   
46074 N  N   . VAL   AA 33  ? 1.6777 0.4860 1.5206 -0.0797 -0.4869 -0.1259 20  VAL   a N   
46075 C  CA  . VAL   AA 33  ? 1.6578 0.5530 1.4826 -0.0614 -0.4435 -0.0975 20  VAL   a CA  
46076 C  C   . VAL   AA 33  ? 1.6655 0.5675 1.4513 -0.0478 -0.4531 -0.0809 20  VAL   a C   
46077 O  O   . VAL   AA 33  ? 1.7021 0.4957 1.4878 -0.0706 -0.4428 -0.1099 20  VAL   a O   
46078 C  CB  . VAL   AA 33  ? 1.6836 0.5967 1.4930 -0.0957 -0.4383 -0.1089 20  VAL   a CB  
46079 C  CG1 . VAL   AA 33  ? 1.6888 0.6383 1.5418 -0.1229 -0.4035 -0.1364 20  VAL   a CG1 
46080 C  CG2 . VAL   AA 33  ? 1.6883 0.5960 1.4934 -0.0779 -0.4357 -0.0778 20  VAL   a CG2 
46081 N  N   . ILE   AA 34  ? 1.6051 0.6479 1.4013 0.0304  -0.4340 -0.0847 21  ILE   a N   
46082 C  CA  . ILE   AA 34  ? 1.5563 0.6323 1.3499 0.0798  -0.4948 -0.0684 21  ILE   a CA  
46083 C  C   . ILE   AA 34  ? 1.5173 0.6103 1.3183 0.0950  -0.4684 -0.0981 21  ILE   a C   
46084 O  O   . ILE   AA 34  ? 1.4423 0.6113 1.2841 0.1270  -0.4859 -0.1262 21  ILE   a O   
46085 C  CB  . ILE   AA 34  ? 1.5913 0.5756 1.3943 0.0770  -0.4816 -0.0616 21  ILE   a CB  
46086 C  CG1 . ILE   AA 34  ? 1.6060 0.6226 1.4486 0.0633  -0.5101 -0.0478 21  ILE   a CG1 
46087 C  CG2 . ILE   AA 34  ? 1.5965 0.5154 1.4011 0.1012  -0.4870 -0.0510 21  ILE   a CG2 
46088 C  CD1 . ILE   AA 34  ? 1.6458 0.5828 1.4789 0.0477  -0.5104 -0.0313 21  ILE   a CD1 
46089 N  N   . ILE   AA 35  ? 1.4874 0.5456 1.2528 0.0992  -0.5156 -0.0662 22  ILE   a N   
46090 C  CA  . ILE   AA 35  ? 1.4600 0.5076 1.2733 0.0960  -0.4903 -0.0709 22  ILE   a CA  
46091 C  C   . ILE   AA 35  ? 1.4897 0.5468 1.2104 0.0588  -0.4895 -0.0456 22  ILE   a C   
46092 O  O   . ILE   AA 35  ? 1.4696 0.5680 1.2554 0.1180  -0.5229 0.0001  22  ILE   a O   
46093 C  CB  . ILE   AA 35  ? 1.4446 0.4652 1.2995 0.1046  -0.4997 -0.0587 22  ILE   a CB  
46094 C  CG1 . ILE   AA 35  ? 1.4427 0.4645 1.2862 0.1097  -0.4893 -0.0481 22  ILE   a CG1 
46095 C  CG2 . ILE   AA 35  ? 1.4810 0.4792 1.2955 0.0930  -0.5155 -0.0507 22  ILE   a CG2 
46096 C  CD1 . ILE   AA 35  ? 1.4534 0.4672 1.2609 0.1411  -0.4734 -0.0408 22  ILE   a CD1 
46097 N  N   . ALA   AA 36  ? 1.4419 0.5533 1.2270 0.0633  -0.4841 -0.1588 23  ALA   a N   
46098 C  CA  . ALA   AA 36  ? 1.4310 0.6042 1.2069 0.0518  -0.5040 -0.1943 23  ALA   a CA  
46099 C  C   . ALA   AA 36  ? 1.4428 0.5826 1.1410 0.0654  -0.5143 -0.2329 23  ALA   a C   
46100 O  O   . ALA   AA 36  ? 1.3334 0.5382 1.1279 0.1050  -0.5000 -0.2627 23  ALA   a O   
46101 C  CB  . ALA   AA 36  ? 1.4820 0.6586 1.2610 0.0137  -0.4910 -0.2363 23  ALA   a CB  
46102 N  N   . ALA   AA 37  ? 1.4480 0.6333 1.0697 0.0773  -0.5410 -0.2068 24  ALA   a N   
46103 C  CA  . ALA   AA 37  ? 1.4409 0.7335 1.0754 0.0792  -0.5345 -0.2196 24  ALA   a CA  
46104 C  C   . ALA   AA 37  ? 1.4823 0.7450 1.0181 0.0993  -0.5521 -0.1914 24  ALA   a C   
46105 O  O   . ALA   AA 37  ? 1.4294 0.8132 0.9788 0.1778  -0.5720 -0.1750 24  ALA   a O   
46106 C  CB  . ALA   AA 37  ? 1.4604 0.7552 1.1205 0.0512  -0.5196 -0.2467 24  ALA   a CB  
46107 N  N   . ASP   AA 38  ? 1.5199 0.7416 1.0595 0.1119  -0.5770 -0.2027 25  ASP   a N   
46108 C  CA  . ASP   AA 38  ? 1.5667 0.7012 1.0575 0.0977  -0.5567 -0.1567 25  ASP   a CA  
46109 C  C   . ASP   AA 38  ? 1.6062 0.5579 1.0484 0.1264  -0.5411 -0.1445 25  ASP   a C   
46110 O  O   . ASP   AA 38  ? 1.5657 0.5242 1.0850 0.0495  -0.5564 -0.1394 25  ASP   a O   
46111 C  CB  . ASP   AA 38  ? 1.6600 0.7329 1.1127 0.1466  -0.5984 -0.1171 25  ASP   a CB  
46112 C  CG  . ASP   AA 38  ? 1.7823 0.7704 1.1201 0.2156  -0.5967 -0.0358 25  ASP   a CG  
46113 O  OD1 . ASP   AA 38  ? 1.8392 0.8161 1.1749 0.1741  -0.5477 -0.0768 25  ASP   a OD1 
46114 O  OD2 . ASP   AA 38  ? 1.8431 0.8381 1.0568 0.2139  -0.6699 0.0392  25  ASP   a OD2 
46115 N  N   . ASN   AA 39  ? 1.5970 0.4891 1.0920 0.0852  -0.5076 -0.1060 26  ASN   a N   
46116 C  CA  . ASN   AA 39  ? 1.6416 0.5246 1.1706 0.0500  -0.4685 -0.1066 26  ASN   a CA  
46117 C  C   . ASN   AA 39  ? 1.6388 0.5316 1.1799 0.0446  -0.4446 -0.1009 26  ASN   a C   
46118 O  O   . ASN   AA 39  ? 1.6992 0.5985 1.1494 0.0182  -0.4457 -0.0890 26  ASN   a O   
46119 C  CB  . ASN   AA 39  ? 1.6838 0.5450 1.2015 0.0189  -0.4687 -0.0691 26  ASN   a CB  
46120 C  CG  . ASN   AA 39  ? 1.6653 0.5685 1.3144 -0.0264 -0.4887 -0.0417 26  ASN   a CG  
46121 O  OD1 . ASN   AA 39  ? 1.6533 0.5601 1.3885 -0.0098 -0.4299 -0.0015 26  ASN   a OD1 
46122 N  ND2 . ASN   AA 39  ? 1.6982 0.5817 1.3152 -0.0716 -0.4917 -0.0347 26  ASN   a ND2 
46123 N  N   . LEU   AA 40  ? 1.6482 0.5589 1.1830 0.0172  -0.3864 -0.0712 27  LEU   a N   
46124 C  CA  . LEU   AA 40  ? 1.6547 0.5673 1.1935 0.0288  -0.3620 -0.0553 27  LEU   a CA  
46125 C  C   . LEU   AA 40  ? 1.6198 0.5715 1.1371 0.0488  -0.3214 -0.0564 27  LEU   a C   
46126 O  O   . LEU   AA 40  ? 1.6174 0.5105 1.0933 0.1170  -0.3699 -0.0848 27  LEU   a O   
46127 C  CB  . LEU   AA 40  ? 1.7060 0.5659 1.2699 0.0355  -0.3226 -0.0341 27  LEU   a CB  
46128 C  CG  . LEU   AA 40  ? 1.7304 0.6081 1.3109 0.0677  -0.2784 -0.0291 27  LEU   a CG  
46129 C  CD1 . LEU   AA 40  ? 1.7597 0.4810 1.3112 0.0299  -0.2739 -0.0055 27  LEU   a CD1 
46130 C  CD2 . LEU   AA 40  ? 1.7639 0.6345 1.3482 0.0450  -0.2357 -0.0104 27  LEU   a CD2 
46131 N  N   . GLY   AA 41  ? 1.6254 0.5597 1.1392 0.0175  -0.3317 -0.0487 28  GLY   a N   
46132 C  CA  . GLY   AA 41  ? 1.5816 0.6104 1.1358 0.0008  -0.3093 -0.0313 28  GLY   a CA  
46133 C  C   . GLY   AA 41  ? 1.5750 0.6249 1.1315 0.0046  -0.2650 -0.0172 28  GLY   a C   
46134 O  O   . GLY   AA 41  ? 1.6561 0.7850 1.1574 0.0104  -0.2067 -0.1174 28  GLY   a O   
46135 N  N   . SER   AA 42  ? 1.5264 0.5689 1.1578 0.0208  -0.2637 -0.0202 29  SER   a N   
46136 C  CA  . SER   AA 42  ? 1.5319 0.5349 1.1177 -0.0002 -0.2414 0.0092  29  SER   a CA  
46137 C  C   . SER   AA 42  ? 1.4762 0.4945 1.0923 0.0316  -0.2094 0.0225  29  SER   a C   
46138 O  O   . SER   AA 42  ? 1.4937 0.5466 1.0224 0.0340  -0.2099 0.0291  29  SER   a O   
46139 C  CB  . SER   AA 42  ? 1.5078 0.5379 1.1230 -0.0049 -0.2810 0.0278  29  SER   a CB  
46140 O  OG  . SER   AA 42  ? 1.5174 0.5473 1.1361 -0.0356 -0.2969 0.0613  29  SER   a OG  
46141 N  N   . TYR   AA 43  ? 1.4674 0.5439 1.0825 0.0379  -0.1990 0.0120  30  TYR   a N   
46142 C  CA  . TYR   AA 43  ? 1.4775 0.6506 1.0762 0.0645  -0.2092 -0.0029 30  TYR   a CA  
46143 C  C   . TYR   AA 43  ? 1.4800 0.7177 1.0172 0.0613  -0.2158 0.0586  30  TYR   a C   
46144 O  O   . TYR   AA 43  ? 1.5157 0.8068 1.0915 0.1066  -0.1984 0.0437  30  TYR   a O   
46145 C  CB  . TYR   AA 43  ? 1.4747 0.6415 1.0990 0.0674  -0.2083 0.0026  30  TYR   a CB  
46146 C  CG  . TYR   AA 43  ? 1.4591 0.6776 1.1207 0.0901  -0.2193 0.0277  30  TYR   a CG  
46147 C  CD1 . TYR   AA 43  ? 1.4378 0.7432 1.1331 0.0873  -0.2313 -0.0241 30  TYR   a CD1 
46148 C  CD2 . TYR   AA 43  ? 1.4550 0.6650 1.1038 0.0852  -0.2495 0.0750  30  TYR   a CD2 
46149 C  CE1 . TYR   AA 43  ? 1.4100 0.8268 1.1201 0.0991  -0.2256 0.0427  30  TYR   a CE1 
46150 C  CE2 . TYR   AA 43  ? 1.4387 0.7131 1.1203 0.0754  -0.2318 0.0900  30  TYR   a CE2 
46151 C  CZ  . TYR   AA 43  ? 1.4143 0.7491 1.1092 0.0603  -0.2164 0.0712  30  TYR   a CZ  
46152 O  OH  . TYR   AA 43  ? 1.4049 0.9568 1.1001 -0.0460 -0.1736 0.1107  30  TYR   a OH  
46153 N  N   . GLY   AA 44  ? 1.4568 0.7696 0.9747 0.0469  -0.2401 0.0377  31  GLY   a N   
46154 C  CA  . GLY   AA 44  ? 1.4740 0.7515 1.0320 0.0637  -0.2119 0.0231  31  GLY   a CA  
46155 C  C   . GLY   AA 44  ? 1.5186 0.7212 1.0787 0.0377  -0.2152 0.0277  31  GLY   a C   
46156 O  O   . GLY   AA 44  ? 1.5390 0.4749 1.1223 0.1232  -0.1779 0.0585  31  GLY   a O   
46157 N  N   . SER   AA 45  ? 1.5557 0.7768 1.1148 0.0619  -0.1866 0.0265  32  SER   a N   
46158 C  CA  . SER   AA 45  ? 1.5859 0.8397 1.0843 0.0352  -0.2360 0.0509  32  SER   a CA  
46159 C  C   . SER   AA 45  ? 1.6688 0.7670 1.0466 -0.0382 -0.2644 -0.0144 32  SER   a C   
46160 O  O   . SER   AA 45  ? 1.7674 0.8379 1.1328 -0.0999 -0.3235 -0.0390 32  SER   a O   
46161 C  CB  . SER   AA 45  ? 1.5558 0.9047 1.0842 0.0728  -0.2393 0.1601  32  SER   a CB  
46162 O  OG  . SER   AA 45  ? 1.5765 1.0638 1.1045 0.1531  -0.2016 0.2718  32  SER   a OG  
46163 N  N   . LEU   AA 46  ? 1.7212 0.6516 1.0691 -0.0056 -0.2526 -0.0622 33  LEU   a N   
46164 C  CA  . LEU   AA 46  ? 1.6675 0.5158 1.0693 0.0081  -0.2447 -0.0939 33  LEU   a CA  
46165 C  C   . LEU   AA 46  ? 1.6962 0.4595 1.0755 0.0059  -0.2482 -0.0815 33  LEU   a C   
46166 O  O   . LEU   AA 46  ? 1.6617 0.4875 1.0333 0.0035  -0.2571 -0.0768 33  LEU   a O   
46167 C  CB  . LEU   AA 46  ? 1.6661 0.4679 1.0523 0.0170  -0.2090 -0.0884 33  LEU   a CB  
46168 C  CG  . LEU   AA 46  ? 1.6648 0.4558 1.0542 0.0328  -0.1935 -0.0920 33  LEU   a CG  
46169 C  CD1 . LEU   AA 46  ? 1.6690 0.4187 1.0821 0.0199  -0.1956 -0.1091 33  LEU   a CD1 
46170 C  CD2 . LEU   AA 46  ? 1.6452 0.5006 1.0744 0.0348  -0.1759 -0.0776 33  LEU   a CD2 
46171 N  N   . LEU   AA 47  ? 1.7136 0.4385 1.0711 0.0112  -0.2443 -0.0929 34  LEU   a N   
46172 C  CA  . LEU   AA 47  ? 1.7216 0.5150 1.1051 0.0312  -0.2439 -0.0629 34  LEU   a CA  
46173 C  C   . LEU   AA 47  ? 1.7327 0.5731 1.1414 -0.0251 -0.2523 -0.0441 34  LEU   a C   
46174 O  O   . LEU   AA 47  ? 1.7370 0.4918 1.1387 -0.1004 -0.2695 -0.0896 34  LEU   a O   
46175 C  CB  . LEU   AA 47  ? 1.7312 0.5216 1.0836 0.0571  -0.2568 -0.0584 34  LEU   a CB  
46176 C  CG  . LEU   AA 47  ? 1.7722 0.5328 1.1223 0.0629  -0.2224 -0.0416 34  LEU   a CG  
46177 C  CD1 . LEU   AA 47  ? 1.7968 0.5731 1.0932 0.0627  -0.2375 -0.0360 34  LEU   a CD1 
46178 C  CD2 . LEU   AA 47  ? 1.7684 0.5611 1.1774 0.0832  -0.1876 -0.0817 34  LEU   a CD2 
46179 N  N   . ARG   AA 48  ? 1.7332 0.5624 1.2250 -0.0329 -0.2939 -0.0349 35  ARG   a N   
46180 C  CA  . ARG   AA 48  ? 1.7413 0.6566 1.3041 -0.0282 -0.2506 0.0445  35  ARG   a CA  
46181 C  C   . ARG   AA 48  ? 1.7305 0.7307 1.2041 -0.0745 -0.2930 0.0409  35  ARG   a C   
46182 O  O   . ARG   AA 48  ? 1.7755 0.7805 1.1398 -0.1123 -0.3324 0.0178  35  ARG   a O   
46183 C  CB  . ARG   AA 48  ? 1.7489 0.6518 1.3374 -0.0103 -0.2655 0.0321  35  ARG   a CB  
46184 C  CG  . ARG   AA 48  ? 1.7659 0.7056 1.4505 -0.0334 -0.2296 0.0462  35  ARG   a CG  
46185 C  CD  . ARG   AA 48  ? 1.7973 0.7615 1.5540 0.0453  -0.2227 0.0277  35  ARG   a CD  
46186 N  NE  . ARG   AA 48  ? 1.8181 0.8864 1.6435 -0.0083 -0.2035 0.0681  35  ARG   a NE  
46187 C  CZ  . ARG   AA 48  ? 1.8690 0.9191 1.6816 0.0560  -0.2582 0.0824  35  ARG   a CZ  
46188 N  NH1 . ARG   AA 48  ? 1.8882 0.9492 1.6750 0.1220  -0.3050 0.0789  35  ARG   a NH1 
46189 N  NH2 . ARG   AA 48  ? 1.8874 0.8082 1.7266 0.1083  -0.2884 0.1276  35  ARG   a NH2 
46190 N  N   . PHE   AA 49  ? 1.6769 0.6420 1.2254 -0.0893 -0.3540 0.0725  36  PHE   a N   
46191 C  CA  . PHE   AA 49  ? 1.6895 0.5800 1.2423 -0.1268 -0.3451 0.0738  36  PHE   a CA  
46192 C  C   . PHE   AA 49  ? 1.6985 0.6054 1.3048 -0.1392 -0.3506 0.0701  36  PHE   a C   
46193 O  O   . PHE   AA 49  ? 1.6948 0.6204 1.3206 -0.0924 -0.3151 0.0709  36  PHE   a O   
46194 C  CB  . PHE   AA 49  ? 1.6239 0.5513 1.2124 -0.1322 -0.3724 0.1059  36  PHE   a CB  
46195 C  CG  . PHE   AA 49  ? 1.6216 0.4879 1.1965 -0.1435 -0.3648 0.1324  36  PHE   a CG  
46196 C  CD1 . PHE   AA 49  ? 1.6283 0.4485 1.1818 -0.1718 -0.3701 0.1148  36  PHE   a CD1 
46197 C  CD2 . PHE   AA 49  ? 1.5781 0.4069 1.2040 -0.1707 -0.3857 0.1251  36  PHE   a CD2 
46198 C  CE1 . PHE   AA 49  ? 1.6387 0.4059 1.1784 -0.2019 -0.3517 0.1101  36  PHE   a CE1 
46199 C  CE2 . PHE   AA 49  ? 1.5924 0.3804 1.1915 -0.1830 -0.3809 0.1126  36  PHE   a CE2 
46200 C  CZ  . PHE   AA 49  ? 1.6155 0.3839 1.1910 -0.1941 -0.3751 0.1194  36  PHE   a CZ  
46201 N  N   . ASN   AA 50  ? 1.7979 0.7105 1.2844 -0.1648 -0.3298 0.0851  37  ASN   a N   
46202 C  CA  . ASN   AA 50  ? 1.8100 0.7467 1.3477 -0.1594 -0.3584 0.0886  37  ASN   a CA  
46203 C  C   . ASN   AA 50  ? 1.8555 0.7186 1.3866 -0.1516 -0.3116 0.0936  37  ASN   a C   
46204 O  O   . ASN   AA 50  ? 1.8346 0.8702 1.5399 -0.1279 -0.3244 0.1252  37  ASN   a O   
46205 C  CB  . ASN   AA 50  ? 1.8865 0.7457 1.3909 -0.1775 -0.3536 0.0579  37  ASN   a CB  
46206 C  CG  . ASN   AA 50  ? 1.9406 0.7467 1.3947 -0.1573 -0.3753 0.0706  37  ASN   a CG  
46207 O  OD1 . ASN   AA 50  ? 1.9693 0.6450 1.3524 -0.1717 -0.3703 0.0616  37  ASN   a OD1 
46208 N  ND2 . ASN   AA 50  ? 1.9806 0.7117 1.3912 -0.1972 -0.3931 0.1221  37  ASN   a ND2 
46209 N  N   . GLY   AA 51  ? 1.8471 0.6821 1.3043 -0.1096 -0.2890 0.0858  38  GLY   a N   
46210 C  CA  . GLY   AA 51  ? 1.8745 0.7024 1.3163 -0.0770 -0.2932 0.0659  38  GLY   a CA  
46211 C  C   . GLY   AA 51  ? 1.8770 0.8127 1.2640 -0.0243 -0.2509 0.1113  38  GLY   a C   
46212 O  O   . GLY   AA 51  ? 2.0188 0.8207 1.4069 0.1173  -0.2344 0.0385  38  GLY   a O   
46213 N  N   . VAL   AA 52  ? 1.7867 0.6592 1.3462 -0.0317 -0.2727 0.1386  39  VAL   a N   
46214 C  CA  . VAL   AA 52  ? 1.6821 0.6209 1.3257 -0.0134 -0.3134 0.1571  39  VAL   a CA  
46215 C  C   . VAL   AA 52  ? 1.6736 0.6223 1.3090 0.0174  -0.3475 0.1726  39  VAL   a C   
46216 O  O   . VAL   AA 52  ? 1.6816 0.6052 1.2930 0.0284  -0.3891 0.2058  39  VAL   a O   
46217 C  CB  . VAL   AA 52  ? 1.6321 0.5366 1.3153 -0.0254 -0.3088 0.1218  39  VAL   a CB  
46218 C  CG1 . VAL   AA 52  ? 1.6074 0.4896 1.3232 -0.0518 -0.2948 0.1246  39  VAL   a CG1 
46219 C  CG2 . VAL   AA 52  ? 1.6395 0.5267 1.3331 -0.0039 -0.3002 0.1158  39  VAL   a CG2 
46220 N  N   . GLU   AA 53  ? 1.5821 0.6559 1.2363 0.0392  -0.3466 0.1452  40  GLU   a N   
46221 C  CA  . GLU   AA 53  ? 1.5932 0.6769 1.2258 0.0515  -0.3355 0.1070  40  GLU   a CA  
46222 C  C   . GLU   AA 53  ? 1.5936 0.6230 1.2131 0.0907  -0.3615 0.1360  40  GLU   a C   
46223 O  O   . GLU   AA 53  ? 1.5290 0.5929 1.1946 0.0767  -0.3384 0.1867  40  GLU   a O   
46224 C  CB  . GLU   AA 53  ? 1.6051 0.6612 1.2731 0.0638  -0.3436 0.0902  40  GLU   a CB  
46225 C  CG  . GLU   AA 53  ? 1.5959 0.7609 1.3288 0.0511  -0.3413 0.0521  40  GLU   a CG  
46226 C  CD  . GLU   AA 53  ? 1.6238 0.7761 1.3218 0.0756  -0.3702 -0.0185 40  GLU   a CD  
46227 O  OE1 . GLU   AA 53  ? 1.6047 0.8578 1.2753 0.0635  -0.3477 -0.0480 40  GLU   a OE1 
46228 O  OE2 . GLU   AA 53  ? 1.6239 0.8021 1.3523 0.0760  -0.4391 -0.0697 40  GLU   a OE2 
46229 N  N   . ARG   AA 54  ? 1.6420 0.6529 1.2070 0.1134  -0.3479 0.1915  41  ARG   a N   
46230 C  CA  . ARG   AA 54  ? 1.6780 0.7203 1.1895 0.1301  -0.3679 0.1065  41  ARG   a CA  
46231 C  C   . ARG   AA 54  ? 1.7088 0.6140 1.2599 0.1388  -0.3484 0.0967  41  ARG   a C   
46232 O  O   . ARG   AA 54  ? 1.7055 0.5434 1.2816 0.1300  -0.3056 0.1100  41  ARG   a O   
46233 C  CB  . ARG   AA 54  ? 1.6989 0.7420 1.1400 0.1440  -0.4058 0.1163  41  ARG   a CB  
46234 C  CG  . ARG   AA 54  ? 1.7027 0.8033 1.0807 0.1492  -0.4190 0.1010  41  ARG   a CG  
46235 C  CD  . ARG   AA 54  ? 1.7083 0.8416 1.0222 0.1157  -0.4396 0.1260  41  ARG   a CD  
46236 N  NE  . ARG   AA 54  ? 1.7019 0.8698 0.9760 0.0801  -0.4689 0.1641  41  ARG   a NE  
46237 C  CZ  . ARG   AA 54  ? 1.6826 0.8402 0.9685 0.0720  -0.4802 0.1357  41  ARG   a CZ  
46238 N  NH1 . ARG   AA 54  ? 1.6414 0.8260 0.9804 0.0646  -0.4462 0.1432  41  ARG   a NH1 
46239 N  NH2 . ARG   AA 54  ? 1.7559 0.8406 0.9928 0.0746  -0.5069 0.1243  41  ARG   a NH2 
46240 N  N   . LEU   AA 55  ? 1.7372 0.6270 1.2484 0.1248  -0.3715 0.0663  42  LEU   a N   
46241 C  CA  . LEU   AA 55  ? 1.7012 0.7563 1.2559 0.1062  -0.3479 -0.0101 42  LEU   a CA  
46242 C  C   . LEU   AA 55  ? 1.7545 0.7865 1.2338 0.0397  -0.3281 -0.0277 42  LEU   a C   
46243 O  O   . LEU   AA 55  ? 1.8535 0.9589 1.0566 0.0450  -0.4529 -0.0953 42  LEU   a O   
46244 C  CB  . LEU   AA 55  ? 1.7028 0.6679 1.2417 0.1242  -0.3471 -0.0147 42  LEU   a CB  
46245 C  CG  . LEU   AA 55  ? 1.6923 0.6645 1.1950 0.1239  -0.3529 -0.0554 42  LEU   a CG  
46246 C  CD1 . LEU   AA 55  ? 1.6915 0.6566 1.2128 0.1522  -0.3818 -0.0371 42  LEU   a CD1 
46247 C  CD2 . LEU   AA 55  ? 1.6740 0.6826 1.2164 0.1437  -0.3009 -0.0845 42  LEU   a CD2 
46248 N  N   . ILE   AA 56  ? 1.7113 0.7828 1.2836 0.0187  -0.2873 -0.0479 43  ILE   a N   
46249 C  CA  . ILE   AA 56  ? 1.6414 0.7837 1.2845 0.0532  -0.2695 0.0013  43  ILE   a CA  
46250 C  C   . ILE   AA 56  ? 1.6109 0.7091 1.1909 0.0310  -0.2833 0.0124  43  ILE   a C   
46251 O  O   . ILE   AA 56  ? 1.4782 0.5663 1.2101 0.0716  -0.2773 -0.0312 43  ILE   a O   
46252 C  CB  . ILE   AA 56  ? 1.7181 0.8612 1.2445 -0.0395 -0.2583 0.0075  43  ILE   a CB  
46253 C  CG1 . ILE   AA 56  ? 1.7621 0.9269 1.2562 -0.0331 -0.2151 0.0205  43  ILE   a CG1 
46254 C  CG2 . ILE   AA 56  ? 1.6994 0.8886 1.2906 -0.0741 -0.2248 0.0150  43  ILE   a CG2 
46255 C  CD1 . ILE   AA 56  ? 1.7489 1.0003 1.3014 0.0020  -0.1948 0.0288  43  ILE   a CD1 
46256 N  N   . PRO   AA 57  ? 1.6122 0.7204 1.2358 0.0599  -0.3211 0.0087  44  PRO   a N   
46257 C  CA  . PRO   AA 57  ? 1.6324 0.7271 1.2636 0.0906  -0.3502 0.0429  44  PRO   a CA  
46258 C  C   . PRO   AA 57  ? 1.6499 0.6952 1.3116 0.1124  -0.3608 0.0574  44  PRO   a C   
46259 O  O   . PRO   AA 57  ? 1.5816 0.6820 1.3575 0.1827  -0.3733 0.1075  44  PRO   a O   
46260 C  CB  . PRO   AA 57  ? 1.6485 0.7554 1.2737 0.0948  -0.3826 0.0263  44  PRO   a CB  
46261 C  CG  . PRO   AA 57  ? 1.6591 0.7766 1.2564 0.0874  -0.3646 0.0321  44  PRO   a CG  
46262 C  CD  . PRO   AA 57  ? 1.6328 0.7774 1.2176 0.0577  -0.3422 0.0244  44  PRO   a CD  
46263 N  N   . VAL   AA 58  ? 1.6591 0.6516 1.3511 0.1103  -0.3441 0.0577  45  VAL   a N   
46264 C  CA  . VAL   AA 58  ? 1.6554 0.6537 1.3736 0.0773  -0.3765 0.0470  45  VAL   a CA  
46265 C  C   . VAL   AA 58  ? 1.6396 0.6274 1.3954 0.0482  -0.4053 0.0582  45  VAL   a C   
46266 O  O   . VAL   AA 58  ? 1.5876 0.6211 1.4035 0.0458  -0.4341 0.0029  45  VAL   a O   
46267 C  CB  . VAL   AA 58  ? 1.6369 0.6044 1.3705 0.0990  -0.3699 0.0464  45  VAL   a CB  
46268 C  CG1 . VAL   AA 58  ? 1.6506 0.6274 1.3844 0.1023  -0.3540 0.0207  45  VAL   a CG1 
46269 C  CG2 . VAL   AA 58  ? 1.6225 0.5778 1.3507 0.0867  -0.3563 0.0398  45  VAL   a CG2 
46270 N  N   . GLY   AA 59  ? 1.6874 0.6501 1.4007 0.0611  -0.4574 0.0853  46  GLY   a N   
46271 C  CA  . GLY   AA 59  ? 1.6702 0.6514 1.4328 0.0261  -0.4823 0.0789  46  GLY   a CA  
46272 C  C   . GLY   AA 59  ? 1.6783 0.6519 1.4810 -0.0116 -0.4788 0.0706  46  GLY   a C   
46273 O  O   . GLY   AA 59  ? 1.6487 0.5033 1.4360 -0.0386 -0.5179 0.1370  46  GLY   a O   
46274 N  N   . ASP   AA 60  ? 1.6806 0.6998 1.5772 -0.0079 -0.4918 0.0219  47  ASP   a N   
46275 C  CA  . ASP   AA 60  ? 1.7388 0.7406 1.6112 0.0217  -0.5419 -0.0060 47  ASP   a CA  
46276 C  C   . ASP   AA 60  ? 1.7329 0.7326 1.5701 0.0413  -0.5227 -0.0280 47  ASP   a C   
46277 O  O   . ASP   AA 60  ? 1.8199 0.7209 1.7307 -0.0361 -0.4773 -0.1817 47  ASP   a O   
46278 C  CB  . ASP   AA 60  ? 1.8596 0.8093 1.6486 0.0296  -0.6152 0.0420  47  ASP   a CB  
46279 C  CG  . ASP   AA 60  ? 1.9395 0.8575 1.6894 0.0727  -0.6461 -0.0075 47  ASP   a CG  
46280 O  OD1 . ASP   AA 60  ? 2.0113 0.7884 1.7162 0.0166  -0.7068 -0.0237 47  ASP   a OD1 
46281 O  OD2 . ASP   AA 60  ? 2.0854 1.2137 1.6218 0.1177  -0.7785 0.0001  47  ASP   a OD2 
46282 N  N   . ASN   AA 61  ? 1.6742 0.6530 1.5616 0.0855  -0.4874 0.0073  48  ASN   a N   
46283 C  CA  . ASN   AA 61  ? 1.6277 0.6247 1.5321 0.1046  -0.4877 -0.0248 48  ASN   a CA  
46284 C  C   . ASN   AA 61  ? 1.5597 0.5811 1.4685 0.0622  -0.4444 -0.0316 48  ASN   a C   
46285 O  O   . ASN   AA 61  ? 1.5383 0.3941 1.4306 0.0671  -0.5037 -0.0504 48  ASN   a O   
46286 C  CB  . ASN   AA 61  ? 1.6326 0.6084 1.5708 0.1159  -0.4564 -0.0004 48  ASN   a CB  
46287 C  CG  . ASN   AA 61  ? 1.6570 0.5750 1.5636 0.1145  -0.4368 -0.0059 48  ASN   a CG  
46288 O  OD1 . ASN   AA 61  ? 1.6984 0.6470 1.5540 0.1311  -0.3741 0.0494  48  ASN   a OD1 
46289 N  ND2 . ASN   AA 61  ? 1.6567 0.5238 1.5465 0.1339  -0.4267 -0.0188 48  ASN   a ND2 
46290 N  N   . THR   AA 62  ? 1.5674 0.5992 1.4636 0.0981  -0.4624 -0.0550 49  THR   a N   
46291 C  CA  . THR   AA 62  ? 1.5357 0.5838 1.4563 0.0879  -0.4460 -0.0586 49  THR   a CA  
46292 C  C   . THR   AA 62  ? 1.5228 0.5674 1.4621 0.0602  -0.4748 -0.1240 49  THR   a C   
46293 O  O   . THR   AA 62  ? 1.5097 0.4738 1.4794 0.0502  -0.5163 -0.1264 49  THR   a O   
46294 C  CB  . THR   AA 62  ? 1.5030 0.6356 1.4384 0.0816  -0.4420 -0.0420 49  THR   a CB  
46295 O  OG1 . THR   AA 62  ? 1.5119 0.5826 1.4831 0.0638  -0.4303 -0.0396 49  THR   a OG1 
46296 C  CG2 . THR   AA 62  ? 1.4558 0.7016 1.4345 0.0939  -0.4255 -0.0178 49  THR   a CG2 
46297 N  N   . VAL   AA 63  ? 1.4815 0.5619 1.4724 0.0558  -0.4730 -0.1390 50  VAL   a N   
46298 C  CA  . VAL   AA 63  ? 1.4819 0.5516 1.4564 0.0548  -0.4865 -0.1469 50  VAL   a CA  
46299 C  C   . VAL   AA 63  ? 1.4403 0.5334 1.4343 0.0004  -0.4490 -0.1231 50  VAL   a C   
46300 O  O   . VAL   AA 63  ? 1.4234 0.5676 1.4414 -0.0017 -0.4192 -0.1404 50  VAL   a O   
46301 C  CB  . VAL   AA 63  ? 1.5373 0.5449 1.4838 0.0829  -0.4987 -0.1691 50  VAL   a CB  
46302 C  CG1 . VAL   AA 63  ? 1.5633 0.5500 1.4512 0.0889  -0.4856 -0.1823 50  VAL   a CG1 
46303 C  CG2 . VAL   AA 63  ? 1.5454 0.5354 1.4841 0.0998  -0.5215 -0.1878 50  VAL   a CG2 
46304 N  N   . VAL   AA 64  ? 1.4434 0.5119 1.4226 0.0039  -0.4630 -0.1123 51  VAL   a N   
46305 C  CA  . VAL   AA 64  ? 1.4163 0.5059 1.3861 -0.0078 -0.4160 -0.0904 51  VAL   a CA  
46306 C  C   . VAL   AA 64  ? 1.4375 0.4649 1.3944 -0.0428 -0.4048 -0.0979 51  VAL   a C   
46307 O  O   . VAL   AA 64  ? 1.4755 0.5335 1.3958 -0.0624 -0.3743 -0.1459 51  VAL   a O   
46308 C  CB  . VAL   AA 64  ? 1.3744 0.5145 1.3246 0.0083  -0.4057 -0.0712 51  VAL   a CB  
46309 C  CG1 . VAL   AA 64  ? 1.3924 0.4871 1.2985 0.0039  -0.3553 -0.0274 51  VAL   a CG1 
46310 C  CG2 . VAL   AA 64  ? 1.3585 0.5339 1.3194 0.0524  -0.4218 -0.0450 51  VAL   a CG2 
46311 N  N   . GLY   AA 65  ? 1.4155 0.4441 1.3763 -0.0455 -0.3977 -0.1322 52  GLY   a N   
46312 C  CA  . GLY   AA 65  ? 1.4532 0.3710 1.3512 -0.0788 -0.3962 -0.1194 52  GLY   a CA  
46313 C  C   . GLY   AA 65  ? 1.4837 0.3420 1.3035 -0.0726 -0.3883 -0.1426 52  GLY   a C   
46314 O  O   . GLY   AA 65  ? 1.4706 0.2388 1.3166 -0.0743 -0.3730 -0.2056 52  GLY   a O   
46315 N  N   . ILE   AA 66  ? 1.5022 0.4387 1.2582 -0.0457 -0.3746 -0.1002 53  ILE   a N   
46316 C  CA  . ILE   AA 66  ? 1.5151 0.5407 1.2524 -0.0397 -0.3731 -0.0709 53  ILE   a CA  
46317 C  C   . ILE   AA 66  ? 1.5658 0.5567 1.1428 -0.0214 -0.3528 -0.0488 53  ILE   a C   
46318 O  O   . ILE   AA 66  ? 1.7145 0.6705 1.1588 -0.0520 -0.2873 -0.0400 53  ILE   a O   
46319 C  CB  . ILE   AA 66  ? 1.5018 0.5415 1.2912 -0.0372 -0.3553 -0.0456 53  ILE   a CB  
46320 C  CG1 . ILE   AA 66  ? 1.5046 0.6138 1.3287 0.0033  -0.3366 -0.0541 53  ILE   a CG1 
46321 C  CG2 . ILE   AA 66  ? 1.5090 0.5369 1.2963 0.0083  -0.3389 -0.0272 53  ILE   a CG2 
46322 C  CD1 . ILE   AA 66  ? 1.5220 0.6842 1.3341 -0.0504 -0.3470 -0.0148 53  ILE   a CD1 
46323 N  N   . SER   AA 67  ? 1.5404 0.5295 1.1914 -0.0093 -0.3979 -0.0418 54  SER   a N   
46324 C  CA  . SER   AA 67  ? 1.5311 0.5599 1.1421 0.0137  -0.4135 0.0059  54  SER   a CA  
46325 C  C   . SER   AA 67  ? 1.5119 0.3302 1.1347 -0.0301 -0.3918 0.0217  54  SER   a C   
46326 O  O   . SER   AA 67  ? 1.5025 0.2082 1.1722 -0.0961 -0.4024 0.0780  54  SER   a O   
46327 C  CB  . SER   AA 67  ? 1.5107 0.6229 1.0926 -0.0101 -0.3912 0.0268  54  SER   a CB  
46328 O  OG  . SER   AA 67  ? 1.5510 0.7852 1.0706 0.0129  -0.3864 0.0498  54  SER   a OG  
46329 N  N   . GLY   AA 68  ? 1.4840 0.3770 1.0917 -0.0196 -0.4218 0.0995  55  GLY   a N   
46330 C  CA  . GLY   AA 68  ? 1.4792 0.3667 1.0692 -0.0540 -0.4150 0.0842  55  GLY   a CA  
46331 C  C   . GLY   AA 68  ? 1.4874 0.3122 1.0746 -0.0392 -0.4061 0.0804  55  GLY   a C   
46332 O  O   . GLY   AA 68  ? 1.4154 0.2693 1.0619 -0.1198 -0.4373 0.0144  55  GLY   a O   
46333 N  N   . ASP   AA 69  ? 1.4936 0.3645 1.1416 -0.0154 -0.4152 0.0220  56  ASP   a N   
46334 C  CA  . ASP   AA 69  ? 1.4824 0.4867 1.1887 -0.0088 -0.3735 0.0064  56  ASP   a CA  
46335 C  C   . ASP   AA 69  ? 1.5227 0.5171 1.1617 0.0225  -0.3524 0.0087  56  ASP   a C   
46336 O  O   . ASP   AA 69  ? 1.4618 0.5049 1.1683 -0.0354 -0.3251 -0.0143 56  ASP   a O   
46337 C  CB  . ASP   AA 69  ? 1.5055 0.4868 1.2634 0.0109  -0.4325 -0.0238 56  ASP   a CB  
46338 C  CG  . ASP   AA 69  ? 1.4665 0.4803 1.3554 0.0324  -0.4684 -0.0450 56  ASP   a CG  
46339 O  OD1 . ASP   AA 69  ? 1.6166 0.4285 1.4133 0.1221  -0.4661 -0.0943 56  ASP   a OD1 
46340 O  OD2 . ASP   AA 69  ? 1.5596 0.5505 1.4747 -0.0631 -0.5060 0.0578  56  ASP   a OD2 
46341 N  N   . ILE   AA 70  ? 1.5911 0.5758 1.1662 0.0518  -0.3261 -0.0180 57  ILE   a N   
46342 C  CA  . ILE   AA 70  ? 1.5973 0.5444 1.1671 0.0393  -0.3522 -0.0370 57  ILE   a CA  
46343 C  C   . ILE   AA 70  ? 1.5801 0.5047 1.1499 0.0868  -0.3523 -0.0425 57  ILE   a C   
46344 O  O   . ILE   AA 70  ? 1.6238 0.5494 1.2506 0.1372  -0.3683 -0.0391 57  ILE   a O   
46345 C  CB  . ILE   AA 70  ? 1.6379 0.6084 1.1438 0.0238  -0.3634 -0.0397 57  ILE   a CB  
46346 C  CG1 . ILE   AA 70  ? 1.6605 0.6307 1.1658 0.0269  -0.3841 -0.0843 57  ILE   a CG1 
46347 C  CG2 . ILE   AA 70  ? 1.6627 0.5768 1.1602 0.0121  -0.3537 -0.0419 57  ILE   a CG2 
46348 C  CD1 . ILE   AA 70  ? 1.6657 0.6410 1.1827 0.0330  -0.4001 -0.1162 57  ILE   a CD1 
46349 N  N   . SER   AA 71  ? 1.5710 0.4446 1.0630 0.0592  -0.3331 -0.0777 58  SER   a N   
46350 C  CA  . SER   AA 71  ? 1.5820 0.3877 1.0517 0.0991  -0.3270 -0.0688 58  SER   a CA  
46351 C  C   . SER   AA 71  ? 1.5257 0.5281 0.9670 0.0520  -0.3340 -0.0861 58  SER   a C   
46352 O  O   . SER   AA 71  ? 1.5436 0.5379 0.9280 0.0953  -0.3368 -0.1224 58  SER   a O   
46353 C  CB  . SER   AA 71  ? 1.5704 0.3022 1.0738 0.1100  -0.3013 -0.0916 58  SER   a CB  
46354 O  OG  . SER   AA 71  ? 1.6208 0.2239 1.0713 0.0878  -0.2695 -0.1213 58  SER   a OG  
46355 N  N   . ASP   AA 72  ? 1.5191 0.4271 1.0170 0.0233  -0.3524 -0.0951 59  ASP   a N   
46356 C  CA  . ASP   AA 72  ? 1.4999 0.4336 1.0835 0.0151  -0.3417 -0.1121 59  ASP   a CA  
46357 C  C   . ASP   AA 72  ? 1.5057 0.4227 1.0665 -0.0107 -0.3507 -0.0800 59  ASP   a C   
46358 O  O   . ASP   AA 72  ? 1.4380 0.4456 1.0631 -0.0507 -0.3826 -0.1508 59  ASP   a O   
46359 C  CB  . ASP   AA 72  ? 1.5403 0.4460 1.1298 0.0006  -0.3016 -0.1025 59  ASP   a CB  
46360 C  CG  . ASP   AA 72  ? 1.5266 0.4578 1.1880 -0.0034 -0.3119 -0.1282 59  ASP   a CG  
46361 O  OD1 . ASP   AA 72  ? 1.5693 0.4302 1.2722 -0.0160 -0.2794 -0.0988 59  ASP   a OD1 
46362 O  OD2 . ASP   AA 72  ? 1.5521 0.4359 1.1868 -0.0301 -0.2545 -0.1454 59  ASP   a OD2 
46363 N  N   . MET   AA 73  ? 1.5214 0.4415 1.0072 0.0182  -0.3563 -0.0482 60  MET   a N   
46364 C  CA  . MET   AA 73  ? 1.5325 0.4416 1.0674 0.0328  -0.3658 -0.0126 60  MET   a CA  
46365 C  C   . MET   AA 73  ? 1.5237 0.3928 1.1178 0.0885  -0.3751 -0.0217 60  MET   a C   
46366 O  O   . MET   AA 73  ? 1.5908 0.2737 1.1499 0.0742  -0.3878 0.0112  60  MET   a O   
46367 C  CB  . MET   AA 73  ? 1.5686 0.4634 1.1063 0.0013  -0.3879 -0.0315 60  MET   a CB  
46368 C  CG  . MET   AA 73  ? 1.6046 0.5087 1.1347 0.0165  -0.4210 -0.0365 60  MET   a CG  
46369 S  SD  . MET   AA 73  ? 1.7013 0.5002 1.1730 0.0310  -0.4693 -0.0522 60  MET   a SD  
46370 C  CE  . MET   AA 73  ? 1.6809 0.6143 1.1134 0.0327  -0.4317 -0.1009 60  MET   a CE  
46371 N  N   . GLN   AA 74  ? 1.5285 0.3059 1.1091 0.0841  -0.3790 0.0555  61  GLN   a N   
46372 C  CA  . GLN   AA 74  ? 1.5386 0.3590 1.1158 0.0818  -0.3602 0.0974  61  GLN   a CA  
46373 C  C   . GLN   AA 74  ? 1.5480 0.4444 1.1258 0.0329  -0.3607 0.0477  61  GLN   a C   
46374 O  O   . GLN   AA 74  ? 1.5730 0.4331 1.2601 0.0864  -0.3520 0.0257  61  GLN   a O   
46375 C  CB  . GLN   AA 74  ? 1.5357 0.3057 1.0831 0.1089  -0.3719 0.1326  61  GLN   a CB  
46376 C  CG  . GLN   AA 74  ? 1.5613 0.2874 1.0934 0.1009  -0.3757 0.1356  61  GLN   a CG  
46377 C  CD  . GLN   AA 74  ? 1.5636 0.3192 1.0986 0.0909  -0.3794 0.1161  61  GLN   a CD  
46378 O  OE1 . GLN   AA 74  ? 1.5705 0.3793 1.1007 0.0924  -0.4255 0.1654  61  GLN   a OE1 
46379 N  NE2 . GLN   AA 74  ? 1.6147 0.3785 1.1140 0.0796  -0.3527 0.0869  61  GLN   a NE2 
46380 N  N   . HIS   AA 75  ? 1.5384 0.4340 1.1405 0.0335  -0.3563 0.0956  62  HIS   a N   
46381 C  CA  . HIS   AA 75  ? 1.5495 0.4622 1.1744 0.0567  -0.3385 0.0682  62  HIS   a CA  
46382 C  C   . HIS   AA 75  ? 1.5463 0.4974 1.1876 0.0697  -0.3535 0.0451  62  HIS   a C   
46383 O  O   . HIS   AA 75  ? 1.5837 0.5580 1.2063 0.1967  -0.3355 0.0095  62  HIS   a O   
46384 C  CB  . HIS   AA 75  ? 1.5480 0.4408 1.1810 0.0422  -0.3351 0.0781  62  HIS   a CB  
46385 C  CG  . HIS   AA 75  ? 1.5205 0.4015 1.2341 0.0582  -0.3229 0.0575  62  HIS   a CG  
46386 N  ND1 . HIS   AA 75  ? 1.5122 0.4115 1.2699 0.0597  -0.3448 0.0063  62  HIS   a ND1 
46387 C  CD2 . HIS   AA 75  ? 1.4963 0.3514 1.2494 0.0578  -0.3119 0.0492  62  HIS   a CD2 
46388 C  CE1 . HIS   AA 75  ? 1.4887 0.4511 1.2694 0.0483  -0.3153 0.0253  62  HIS   a CE1 
46389 N  NE2 . HIS   AA 75  ? 1.4860 0.3758 1.2557 0.0705  -0.3420 0.0341  62  HIS   a NE2 
46390 N  N   . ILE   AA 76  ? 1.5357 0.5052 1.1912 0.0697  -0.3610 0.0449  63  ILE   a N   
46391 C  CA  . ILE   AA 76  ? 1.5569 0.5218 1.2490 0.0963  -0.3478 0.0117  63  ILE   a CA  
46392 C  C   . ILE   AA 76  ? 1.6302 0.5172 1.2559 0.0960  -0.3562 0.0188  63  ILE   a C   
46393 O  O   . ILE   AA 76  ? 1.6901 0.4275 1.4468 0.0784  -0.3376 0.0160  63  ILE   a O   
46394 C  CB  . ILE   AA 76  ? 1.5734 0.5040 1.2510 0.0940  -0.3693 -0.0117 63  ILE   a CB  
46395 C  CG1 . ILE   AA 76  ? 1.5762 0.5119 1.2438 0.0567  -0.3864 -0.0229 63  ILE   a CG1 
46396 C  CG2 . ILE   AA 76  ? 1.5714 0.4737 1.2586 0.1037  -0.3827 -0.0285 63  ILE   a CG2 
46397 C  CD1 . ILE   AA 76  ? 1.5877 0.5306 1.2333 -0.0034 -0.3876 -0.0169 63  ILE   a CD1 
46398 N  N   . GLU   AA 77  ? 1.6342 0.5896 1.2611 0.1159  -0.3609 -0.0180 64  GLU   a N   
46399 C  CA  . GLU   AA 77  ? 1.6671 0.6848 1.2322 0.0972  -0.3961 -0.0257 64  GLU   a CA  
46400 C  C   . GLU   AA 77  ? 1.6567 0.6880 1.1972 0.1321  -0.4094 -0.0713 64  GLU   a C   
46401 O  O   . GLU   AA 77  ? 1.6804 0.6666 1.1612 0.1389  -0.4453 -0.1032 64  GLU   a O   
46402 C  CB  . GLU   AA 77  ? 1.7019 0.7636 1.2265 0.0948  -0.3777 -0.0133 64  GLU   a CB  
46403 C  CG  . GLU   AA 77  ? 1.7395 0.8526 1.2433 0.0557  -0.3880 -0.0440 64  GLU   a CG  
46404 C  CD  . GLU   AA 77  ? 1.7607 1.0119 1.3000 0.0363  -0.3244 -0.0452 64  GLU   a CD  
46405 O  OE1 . GLU   AA 77  ? 1.7133 1.0245 1.3364 0.0710  -0.3214 0.0363  64  GLU   a OE1 
46406 O  OE2 . GLU   AA 77  ? 1.7761 0.8933 1.4308 -0.1200 -0.3049 -0.0437 64  GLU   a OE2 
46407 N  N   . ARG   AA 78  ? 1.6683 0.6694 1.2152 0.1132  -0.4061 -0.0829 65  ARG   a N   
46408 C  CA  . ARG   AA 78  ? 1.7054 0.6305 1.2551 0.1170  -0.4116 -0.0216 65  ARG   a CA  
46409 C  C   . ARG   AA 78  ? 1.6757 0.5481 1.2158 0.0313  -0.4245 -0.0229 65  ARG   a C   
46410 O  O   . ARG   AA 78  ? 1.7292 0.6151 1.3041 0.1383  -0.4310 0.0090  65  ARG   a O   
46411 C  CB  . ARG   AA 78  ? 1.7031 0.7461 1.2519 0.1641  -0.3978 -0.0496 65  ARG   a CB  
46412 C  CG  . ARG   AA 78  ? 1.7354 0.8875 1.2975 0.1233  -0.3425 -0.0079 65  ARG   a CG  
46413 C  CD  . ARG   AA 78  ? 1.7660 1.1217 1.3666 0.1870  -0.4196 0.0345  65  ARG   a CD  
46414 N  NE  . ARG   AA 78  ? 1.8152 1.3734 1.3435 0.2253  -0.4282 0.0584  65  ARG   a NE  
46415 C  CZ  . ARG   AA 78  ? 1.7852 1.4939 1.4656 0.3396  -0.4769 0.0884  65  ARG   a CZ  
46416 N  NH1 . ARG   AA 78  ? 1.8491 1.5275 1.5902 0.3970  -0.4736 0.0448  65  ARG   a NH1 
46417 N  NH2 . ARG   AA 78  ? 1.8550 1.6368 1.5470 0.2907  -0.4012 -0.0068 65  ARG   a NH2 
46418 N  N   . LEU   AA 79  ? 1.6140 0.3866 1.2394 0.0262  -0.4399 -0.0575 66  LEU   a N   
46419 C  CA  . LEU   AA 79  ? 1.5989 0.3583 1.2684 0.0258  -0.4121 -0.0323 66  LEU   a CA  
46420 C  C   . LEU   AA 79  ? 1.6013 0.3569 1.2938 -0.0043 -0.4287 0.0220  66  LEU   a C   
46421 O  O   . LEU   AA 79  ? 1.5773 0.3122 1.3472 0.0142  -0.4491 0.0879  66  LEU   a O   
46422 C  CB  . LEU   AA 79  ? 1.6149 0.3730 1.2714 0.0661  -0.3716 -0.0252 66  LEU   a CB  
46423 C  CG  . LEU   AA 79  ? 1.6354 0.3839 1.2481 0.0889  -0.3570 -0.0004 66  LEU   a CG  
46424 C  CD1 . LEU   AA 79  ? 1.6773 0.4789 1.2201 0.0551  -0.2989 0.0202  66  LEU   a CD1 
46425 C  CD2 . LEU   AA 79  ? 1.6487 0.3387 1.2506 0.0885  -0.3451 0.0297  66  LEU   a CD2 
46426 N  N   . LEU   AA 80  ? 1.5967 0.4520 1.2662 -0.0001 -0.4228 -0.0138 67  LEU   a N   
46427 C  CA  . LEU   AA 80  ? 1.5811 0.5566 1.2997 0.0029  -0.4092 -0.0235 67  LEU   a CA  
46428 C  C   . LEU   AA 80  ? 1.6226 0.5594 1.3313 -0.0091 -0.3501 -0.0172 67  LEU   a C   
46429 O  O   . LEU   AA 80  ? 1.6117 0.6361 1.4629 0.0158  -0.3427 -0.0850 67  LEU   a O   
46430 C  CB  . LEU   AA 80  ? 1.5548 0.5683 1.2358 -0.0105 -0.4142 -0.0035 67  LEU   a CB  
46431 C  CG  . LEU   AA 80  ? 1.5138 0.5603 1.2200 -0.0088 -0.3999 -0.0175 67  LEU   a CG  
46432 C  CD1 . LEU   AA 80  ? 1.5203 0.5503 1.1735 0.0044  -0.3878 0.0005  67  LEU   a CD1 
46433 C  CD2 . LEU   AA 80  ? 1.5052 0.5866 1.2386 -0.0242 -0.4000 -0.0270 67  LEU   a CD2 
46434 N  N   . LYS   AA 81  ? 1.6807 0.6750 1.3291 -0.0268 -0.3135 0.0206  68  LYS   a N   
46435 C  CA  . LYS   AA 81  ? 1.7498 0.7854 1.3319 0.0183  -0.3164 0.0987  68  LYS   a CA  
46436 C  C   . LYS   AA 81  ? 1.7249 0.7142 1.3594 0.1001  -0.3082 0.1549  68  LYS   a C   
46437 O  O   . LYS   AA 81  ? 1.6805 0.7748 1.3758 0.1146  -0.3208 0.1830  68  LYS   a O   
46438 C  CB  . LYS   AA 81  ? 1.8147 0.9048 1.2845 -0.0081 -0.2637 0.1147  68  LYS   a CB  
46439 C  CG  . LYS   AA 81  ? 1.9293 0.9806 1.2603 -0.0079 -0.1950 0.1412  68  LYS   a CG  
46440 C  CD  . LYS   AA 81  ? 2.0102 1.0833 1.2854 0.0291  -0.1300 0.1080  68  LYS   a CD  
46441 C  CE  . LYS   AA 81  ? 2.0142 1.1172 1.4040 -0.0295 -0.0743 0.0243  68  LYS   a CE  
46442 N  NZ  . LYS   AA 81  ? 2.0832 1.1907 1.4434 -0.0003 -0.0790 0.0595  68  LYS   a NZ  
46443 N  N   . ASP   AA 82  ? 1.7510 0.7061 1.3523 0.1361  -0.3117 0.1730  69  ASP   a N   
46444 C  CA  . ASP   AA 82  ? 1.7869 0.6823 1.4226 0.1299  -0.3123 0.1564  69  ASP   a CA  
46445 C  C   . ASP   AA 82  ? 1.6829 0.6404 1.4188 0.0825  -0.3895 0.1095  69  ASP   a C   
46446 O  O   . ASP   AA 82  ? 1.6435 0.7213 1.6667 0.1952  -0.3603 0.0378  69  ASP   a O   
46447 C  CB  . ASP   AA 82  ? 1.8591 0.8967 1.4801 0.1554  -0.3347 0.2872  69  ASP   a CB  
46448 C  CG  . ASP   AA 82  ? 2.0215 0.9403 1.6245 0.0846  -0.3551 0.3136  69  ASP   a CG  
46449 O  OD1 . ASP   AA 82  ? 2.1059 1.0773 1.5870 0.2047  -0.3510 0.5977  69  ASP   a OD1 
46450 O  OD2 . ASP   AA 82  ? 2.2033 1.4458 1.7253 0.1000  -0.1988 0.3592  69  ASP   a OD2 
46451 N  N   . LEU   AA 83  ? 1.5925 0.5618 1.3242 0.1179  -0.3828 0.0103  70  LEU   a N   
46452 C  CA  . LEU   AA 83  ? 1.6175 0.6056 1.3403 0.1131  -0.3538 -0.0304 70  LEU   a CA  
46453 C  C   . LEU   AA 83  ? 1.6375 0.5450 1.3498 0.0734  -0.3636 -0.0132 70  LEU   a C   
46454 O  O   . LEU   AA 83  ? 1.5881 0.6535 1.4788 0.0925  -0.3148 -0.0190 70  LEU   a O   
46455 C  CB  . LEU   AA 83  ? 1.5875 0.6604 1.2837 0.0872  -0.3260 -0.0292 70  LEU   a CB  
46456 C  CG  . LEU   AA 83  ? 1.5930 0.7274 1.2749 0.1022  -0.3317 -0.0323 70  LEU   a CG  
46457 C  CD1 . LEU   AA 83  ? 1.5779 0.7090 1.2473 0.1196  -0.3391 -0.0141 70  LEU   a CD1 
46458 C  CD2 . LEU   AA 83  ? 1.5903 0.7772 1.3129 0.1317  -0.3368 -0.0342 70  LEU   a CD2 
46459 N  N   . VAL   AA 84  ? 1.6223 0.4744 1.3626 0.0844  -0.3706 -0.0458 71  VAL   a N   
46460 C  CA  . VAL   AA 84  ? 1.6118 0.5891 1.3763 0.0884  -0.4059 -0.0611 71  VAL   a CA  
46461 C  C   . VAL   AA 84  ? 1.6356 0.5983 1.3598 0.0792  -0.4047 -0.0549 71  VAL   a C   
46462 O  O   . VAL   AA 84  ? 1.7104 0.5200 1.4553 0.0821  -0.3747 -0.0555 71  VAL   a O   
46463 C  CB  . VAL   AA 84  ? 1.6184 0.6067 1.3844 0.0542  -0.4055 -0.0711 71  VAL   a CB  
46464 C  CG1 . VAL   AA 84  ? 1.6266 0.5813 1.3981 0.0650  -0.4180 -0.0767 71  VAL   a CG1 
46465 C  CG2 . VAL   AA 84  ? 1.6052 0.6518 1.4255 0.0067  -0.3836 -0.0077 71  VAL   a CG2 
46466 N  N   . THR   AA 85  ? 1.6391 0.5873 1.2228 0.0453  -0.4601 -0.0613 72  THR   a N   
46467 C  CA  . THR   AA 85  ? 1.6897 0.5740 1.2542 0.0455  -0.4861 -0.0551 72  THR   a CA  
46468 C  C   . THR   AA 85  ? 1.7184 0.6896 1.2488 0.0701  -0.4273 -0.0478 72  THR   a C   
46469 O  O   . THR   AA 85  ? 1.7318 0.7339 1.3685 0.1480  -0.3959 -0.1209 72  THR   a O   
46470 C  CB  . THR   AA 85  ? 1.6906 0.5597 1.1776 0.0611  -0.5024 -0.0715 72  THR   a CB  
46471 O  OG1 . THR   AA 85  ? 1.6710 0.4751 1.1570 -0.0013 -0.5623 -0.0756 72  THR   a OG1 
46472 C  CG2 . THR   AA 85  ? 1.6982 0.6140 1.2407 0.0203  -0.5114 -0.0344 72  THR   a CG2 
46473 N  N   . GLU   AA 86  ? 1.7334 0.5805 1.2828 0.0755  -0.3855 -0.0209 73  GLU   a N   
46474 C  CA  . GLU   AA 86  ? 1.7314 0.5787 1.3158 0.0508  -0.3841 -0.0622 73  GLU   a CA  
46475 C  C   . GLU   AA 86  ? 1.7318 0.5312 1.2499 0.0530  -0.3646 -0.0761 73  GLU   a C   
46476 O  O   . GLU   AA 86  ? 1.7532 0.5845 1.2444 0.0768  -0.2898 -0.0878 73  GLU   a O   
46477 C  CB  . GLU   AA 86  ? 1.7778 0.6222 1.3089 0.0230  -0.3971 -0.0437 73  GLU   a CB  
46478 C  CG  . GLU   AA 86  ? 1.8343 0.7171 1.3380 0.0036  -0.4431 -0.0543 73  GLU   a CG  
46479 C  CD  . GLU   AA 86  ? 1.8506 0.7816 1.4064 -0.0090 -0.4569 -0.0338 73  GLU   a CD  
46480 O  OE1 . GLU   AA 86  ? 1.9872 0.7613 1.4597 0.0450  -0.4858 -0.0822 73  GLU   a OE1 
46481 O  OE2 . GLU   AA 86  ? 1.8886 0.9029 1.3818 0.0755  -0.4671 -0.0233 73  GLU   a OE2 
46482 N  N   . ASN   AA 87  ? 1.6706 0.5041 1.1984 0.1008  -0.3735 -0.0675 74  ASN   a N   
46483 C  CA  . ASN   AA 87  ? 1.6717 0.5093 1.1932 0.1271  -0.3991 -0.0942 74  ASN   a CA  
46484 C  C   . ASN   AA 87  ? 1.7001 0.4425 1.2822 0.1464  -0.3820 -0.1075 74  ASN   a C   
46485 O  O   . ASN   AA 87  ? 1.7534 0.4441 1.4163 0.1560  -0.3155 -0.1255 74  ASN   a O   
46486 C  CB  . ASN   AA 87  ? 1.6535 0.5296 1.1063 0.1369  -0.4414 -0.1023 74  ASN   a CB  
46487 C  CG  . ASN   AA 87  ? 1.6535 0.5417 1.0946 0.1343  -0.4604 -0.1166 74  ASN   a CG  
46488 O  OD1 . ASN   AA 87  ? 1.6409 0.5031 1.0448 0.1521  -0.5133 -0.0977 74  ASN   a OD1 
46489 N  ND2 . ASN   AA 87  ? 1.6859 0.6132 1.1251 0.1391  -0.4909 -0.1000 74  ASN   a ND2 
46490 N  N   . ALA   AA 88  ? 1.6982 0.4387 1.2689 0.1407  -0.4071 -0.0807 75  ALA   a N   
46491 C  CA  . ALA   AA 88  ? 1.7055 0.4516 1.3264 0.1553  -0.4585 -0.0606 75  ALA   a CA  
46492 C  C   . ALA   AA 88  ? 1.6988 0.4606 1.3690 0.1030  -0.4796 -0.0343 75  ALA   a C   
46493 O  O   . ALA   AA 88  ? 1.7250 0.5691 1.4475 0.1426  -0.5480 -0.0040 75  ALA   a O   
46494 C  CB  . ALA   AA 88  ? 1.7172 0.4225 1.2841 0.1527  -0.4749 -0.0086 75  ALA   a CB  
46495 N  N   . TYR   AA 89  ? 1.6292 0.4607 1.4088 0.1237  -0.4696 -0.0015 76  TYR   a N   
46496 C  CA  . TYR   AA 89  ? 1.6180 0.4791 1.4157 0.1325  -0.4600 -0.0322 76  TYR   a CA  
46497 C  C   . TYR   AA 89  ? 1.5976 0.5690 1.4627 0.1360  -0.4361 -0.0335 76  TYR   a C   
46498 O  O   . TYR   AA 89  ? 1.5551 0.6102 1.4042 0.1459  -0.4387 -0.0529 76  TYR   a O   
46499 C  CB  . TYR   AA 89  ? 1.6060 0.4393 1.3423 0.1382  -0.4254 -0.0420 76  TYR   a CB  
46500 C  CG  . TYR   AA 89  ? 1.6030 0.4283 1.3304 0.1386  -0.4051 0.0093  76  TYR   a CG  
46501 C  CD1 . TYR   AA 89  ? 1.6243 0.4352 1.3490 0.1425  -0.3955 0.0428  76  TYR   a CD1 
46502 C  CD2 . TYR   AA 89  ? 1.5833 0.4356 1.2624 0.1127  -0.3934 0.0132  76  TYR   a CD2 
46503 C  CE1 . TYR   AA 89  ? 1.6191 0.4749 1.3347 0.1315  -0.3928 0.0639  76  TYR   a CE1 
46504 C  CE2 . TYR   AA 89  ? 1.5748 0.4359 1.2679 0.1049  -0.3896 0.0418  76  TYR   a CE2 
46505 C  CZ  . TYR   AA 89  ? 1.6049 0.4577 1.2817 0.1123  -0.3802 0.0612  76  TYR   a CZ  
46506 O  OH  . TYR   AA 89  ? 1.5946 0.4548 1.2921 0.1293  -0.3975 0.0544  76  TYR   a OH  
46507 N  N   . ASP   AA 90  ? 1.6087 0.5453 1.6131 0.1601  -0.4556 -0.0772 77  ASP   a N   
46508 C  CA  . ASP   AA 90  ? 1.6362 0.5536 1.6959 0.1621  -0.4410 -0.1138 77  ASP   a CA  
46509 C  C   . ASP   AA 90  ? 1.6367 0.5437 1.7092 0.1727  -0.4124 -0.0794 77  ASP   a C   
46510 O  O   . ASP   AA 90  ? 1.6397 0.3764 1.7021 0.1915  -0.4113 -0.0632 77  ASP   a O   
46511 C  CB  . ASP   AA 90  ? 1.6317 0.6186 1.6982 0.1660  -0.4258 -0.1399 77  ASP   a CB  
46512 C  CG  . ASP   AA 90  ? 1.6151 0.6972 1.7325 0.1802  -0.4334 -0.1438 77  ASP   a CG  
46513 O  OD1 . ASP   AA 90  ? 1.6756 0.8620 1.7721 0.1474  -0.3633 -0.1424 77  ASP   a OD1 
46514 O  OD2 . ASP   AA 90  ? 1.5523 0.6339 1.7104 0.2568  -0.3829 -0.0828 77  ASP   a OD2 
46515 N  N   . ASN   AA 91  ? 1.6092 0.5679 1.7254 0.1531  -0.4339 -0.0748 78  ASN   a N   
46516 C  CA  . ASN   AA 91  ? 1.5880 0.5956 1.7042 0.1534  -0.4441 -0.0539 78  ASN   a CA  
46517 C  C   . ASN   AA 91  ? 1.6252 0.5490 1.7456 0.1576  -0.4801 -0.0363 78  ASN   a C   
46518 O  O   . ASN   AA 91  ? 1.5309 0.3815 1.7658 0.2073  -0.5150 -0.0010 78  ASN   a O   
46519 C  CB  . ASN   AA 91  ? 1.5640 0.6183 1.6005 0.1643  -0.4540 -0.0164 78  ASN   a CB  
46520 C  CG  . ASN   AA 91  ? 1.5365 0.6953 1.5932 0.1652  -0.4503 0.0068  78  ASN   a CG  
46521 O  OD1 . ASN   AA 91  ? 1.5924 0.7833 1.5985 0.1965  -0.3993 -0.0649 78  ASN   a OD1 
46522 N  ND2 . ASN   AA 91  ? 1.5256 0.6721 1.5602 0.1509  -0.4833 0.0855  78  ASN   a ND2 
46523 N  N   . PRO   AA 92  ? 1.6618 0.6407 1.8288 0.2139  -0.4915 -0.0039 79  PRO   a N   
46524 C  CA  . PRO   AA 92  ? 1.7653 0.7401 1.8245 0.1711  -0.5348 -0.0214 79  PRO   a CA  
46525 C  C   . PRO   AA 92  ? 1.7954 0.6784 1.8125 0.2070  -0.5276 -0.0355 79  PRO   a C   
46526 O  O   . PRO   AA 92  ? 1.9346 0.9117 1.7860 0.1819  -0.4946 -0.0882 79  PRO   a O   
46527 C  CB  . PRO   AA 92  ? 1.7882 0.7625 1.8970 0.1832  -0.5233 -0.0347 79  PRO   a CB  
46528 C  CG  . PRO   AA 92  ? 1.7991 0.7038 1.8890 0.1852  -0.5019 -0.0464 79  PRO   a CG  
46529 C  CD  . PRO   AA 92  ? 1.7135 0.7339 1.8258 0.1845  -0.4822 -0.0460 79  PRO   a CD  
46530 N  N   . LEU   AA 93  ? 1.7568 0.6168 1.8007 0.2581  -0.5574 -0.0402 80  LEU   a N   
46531 C  CA  . LEU   AA 93  ? 1.7247 0.6559 1.8285 0.2395  -0.5512 -0.0175 80  LEU   a CA  
46532 C  C   . LEU   AA 93  ? 1.6922 0.6571 1.7530 0.2269  -0.5271 -0.0526 80  LEU   a C   
46533 O  O   . LEU   AA 93  ? 1.7254 0.5811 1.6922 0.2980  -0.5337 -0.0443 80  LEU   a O   
46534 C  CB  . LEU   AA 93  ? 1.6917 0.6233 1.8576 0.2861  -0.5501 -0.0300 80  LEU   a CB  
46535 C  CG  . LEU   AA 93  ? 1.7276 0.5875 1.9259 0.2812  -0.5779 -0.0272 80  LEU   a CG  
46536 C  CD1 . LEU   AA 93  ? 1.6910 0.5630 1.9160 0.3008  -0.5957 -0.0423 80  LEU   a CD1 
46537 C  CD2 . LEU   AA 93  ? 1.7566 0.6656 1.9532 0.2887  -0.6005 -0.0277 80  LEU   a CD2 
46538 N  N   . ALA   AA 94  ? 1.6903 0.6726 1.7107 0.2168  -0.5371 -0.0794 81  ALA   a N   
46539 C  CA  . ALA   AA 94  ? 1.7061 0.6414 1.6572 0.2095  -0.5127 -0.0271 81  ALA   a CA  
46540 C  C   . ALA   AA 94  ? 1.7268 0.6651 1.6310 0.1991  -0.5308 -0.0062 81  ALA   a C   
46541 O  O   . ALA   AA 94  ? 1.7198 0.6840 1.5798 0.2111  -0.5513 0.0070  81  ALA   a O   
46542 C  CB  . ALA   AA 94  ? 1.7108 0.5991 1.6344 0.2165  -0.4957 -0.0608 81  ALA   a CB  
46543 N  N   . ASP   AA 95  ? 1.7759 0.7184 1.6548 0.1978  -0.5550 0.0223  82  ASP   a N   
46544 C  CA  . ASP   AA 95  ? 1.8052 0.6916 1.6879 0.1758  -0.5626 0.0179  82  ASP   a CA  
46545 C  C   . ASP   AA 95  ? 1.8222 0.7074 1.6966 0.1276  -0.5405 -0.0075 82  ASP   a C   
46546 O  O   . ASP   AA 95  ? 1.9268 0.7821 1.6976 0.1140  -0.5587 -0.0280 82  ASP   a O   
46547 C  CB  . ASP   AA 95  ? 1.8731 0.8025 1.6816 0.1746  -0.5657 0.0290  82  ASP   a CB  
46548 C  CG  . ASP   AA 95  ? 1.9781 0.8567 1.8247 0.2505  -0.5542 0.0646  82  ASP   a CG  
46549 O  OD1 . ASP   AA 95  ? 2.0206 0.8919 1.8551 0.3391  -0.5608 0.0506  82  ASP   a OD1 
46550 O  OD2 . ASP   AA 95  ? 2.0599 0.8888 1.8203 0.2466  -0.4963 0.0844  82  ASP   a OD2 
46551 N  N   . ALA   AA 96  ? 1.7819 0.7564 1.7123 0.1056  -0.5372 -0.0386 83  ALA   a N   
46552 C  CA  . ALA   AA 96  ? 1.7833 0.8305 1.7618 0.1556  -0.5144 -0.0444 83  ALA   a CA  
46553 C  C   . ALA   AA 96  ? 1.7432 0.8589 1.7851 0.1579  -0.4532 -0.0353 83  ALA   a C   
46554 O  O   . ALA   AA 96  ? 1.7977 0.8802 1.7971 0.1879  -0.4277 0.0115  83  ALA   a O   
46555 C  CB  . ALA   AA 96  ? 1.7717 0.8529 1.7938 0.1799  -0.5280 -0.0617 83  ALA   a CB  
46556 N  N   . GLU   AA 97  ? 1.6768 0.8863 1.8356 0.1464  -0.4235 -0.0494 84  GLU   a N   
46557 C  CA  . GLU   AA 97  ? 1.6349 0.9543 1.8297 0.1341  -0.3921 -0.0811 84  GLU   a CA  
46558 C  C   . GLU   AA 97  ? 1.6168 0.9446 1.8001 0.1173  -0.3766 -0.0775 84  GLU   a C   
46559 O  O   . GLU   AA 97  ? 1.5930 1.0344 1.7591 0.1696  -0.3772 -0.0477 84  GLU   a O   
46560 C  CB  . GLU   AA 97  ? 1.6795 0.9741 1.8736 0.1054  -0.3544 -0.1339 84  GLU   a CB  
46561 C  CG  . GLU   AA 97  ? 1.6760 1.0684 1.9655 0.1276  -0.3573 -0.1768 84  GLU   a CG  
46562 C  CD  . GLU   AA 97  ? 1.7571 1.0952 2.0108 0.1624  -0.3777 -0.1672 84  GLU   a CD  
46563 O  OE1 . GLU   AA 97  ? 1.7307 1.2942 2.1213 0.2021  -0.3361 -0.2860 84  GLU   a OE1 
46564 O  OE2 . GLU   AA 97  ? 1.7210 1.2328 2.1065 0.0671  -0.3751 -0.2818 84  GLU   a OE2 
46565 N  N   . GLU   AA 98  ? 1.6745 0.8365 1.7739 0.1045  -0.3702 -0.0421 85  GLU   a N   
46566 C  CA  . GLU   AA 98  ? 1.6596 0.8099 1.7288 0.1070  -0.3367 -0.0150 85  GLU   a CA  
46567 C  C   . GLU   AA 98  ? 1.6071 0.7714 1.7041 0.0521  -0.3477 -0.0354 85  GLU   a C   
46568 O  O   . GLU   AA 98  ? 1.5888 0.7831 1.6136 0.0914  -0.3309 -0.1001 85  GLU   a O   
46569 C  CB  . GLU   AA 98  ? 1.7151 0.7735 1.7776 0.1158  -0.3738 0.0317  85  GLU   a CB  
46570 C  CG  . GLU   AA 98  ? 1.7396 0.7991 1.8074 0.1492  -0.3498 0.0724  85  GLU   a CG  
46571 C  CD  . GLU   AA 98  ? 1.7360 0.7173 1.8533 0.1500  -0.3428 0.1050  85  GLU   a CD  
46572 O  OE1 . GLU   AA 98  ? 1.7326 0.6386 1.8099 0.1600  -0.3562 0.1240  85  GLU   a OE1 
46573 O  OE2 . GLU   AA 98  ? 1.7646 0.7065 1.8324 0.1093  -0.3468 0.1960  85  GLU   a OE2 
46574 N  N   . ALA   AA 99  ? 1.5951 0.7282 1.7527 0.0445  -0.3406 -0.0440 86  ALA   a N   
46575 C  CA  . ALA   AA 99  ? 1.5680 0.7268 1.7353 0.0444  -0.3670 -0.0426 86  ALA   a CA  
46576 C  C   . ALA   AA 99  ? 1.4997 0.7095 1.7270 0.1043  -0.3982 -0.0852 86  ALA   a C   
46577 O  O   . ALA   AA 99  ? 1.4904 0.6680 1.7013 0.1382  -0.4182 -0.0735 86  ALA   a O   
46578 C  CB  . ALA   AA 99  ? 1.5851 0.8041 1.7325 0.0215  -0.3652 -0.0383 86  ALA   a CB  
46579 N  N   . LEU   AA 100 ? 1.5177 0.6872 1.6702 0.1004  -0.3841 -0.1399 87  LEU   a N   
46580 C  CA  . LEU   AA 100 ? 1.5305 0.6373 1.5966 0.0829  -0.3459 -0.1771 87  LEU   a CA  
46581 C  C   . LEU   AA 100 ? 1.5637 0.5708 1.5585 0.1055  -0.3133 -0.2128 87  LEU   a C   
46582 O  O   . LEU   AA 100 ? 1.5278 0.4531 1.5922 0.0163  -0.3029 -0.2241 87  LEU   a O   
46583 C  CB  . LEU   AA 100 ? 1.5506 0.6439 1.5308 0.1288  -0.3749 -0.1846 87  LEU   a CB  
46584 C  CG  . LEU   AA 100 ? 1.5854 0.6384 1.4702 0.1574  -0.4213 -0.1822 87  LEU   a CG  
46585 C  CD1 . LEU   AA 100 ? 1.6118 0.5869 1.4124 0.1999  -0.4384 -0.2052 87  LEU   a CD1 
46586 C  CD2 . LEU   AA 100 ? 1.5579 0.6297 1.4668 0.1571  -0.4195 -0.1618 87  LEU   a CD2 
46587 N  N   . GLU   AA 101 ? 1.5758 0.5434 1.5645 0.1341  -0.3025 -0.2095 88  GLU   a N   
46588 C  CA  . GLU   AA 101 ? 1.5682 0.5829 1.5801 0.1170  -0.3053 -0.2014 88  GLU   a CA  
46589 C  C   . GLU   AA 101 ? 1.5693 0.6434 1.5811 0.1414  -0.3302 -0.1567 88  GLU   a C   
46590 O  O   . GLU   AA 101 ? 1.5507 0.7934 1.5741 0.1230  -0.3040 -0.1967 88  GLU   a O   
46591 C  CB  . GLU   AA 101 ? 1.5764 0.5831 1.6078 0.1505  -0.2872 -0.2155 88  GLU   a CB  
46592 C  CG  . GLU   AA 101 ? 1.5846 0.6018 1.6561 0.1609  -0.2786 -0.1959 88  GLU   a CG  
46593 C  CD  . GLU   AA 101 ? 1.5841 0.5819 1.6701 0.1597  -0.2642 -0.2149 88  GLU   a CD  
46594 O  OE1 . GLU   AA 101 ? 1.6156 0.5057 1.7117 0.2074  -0.2049 -0.2348 88  GLU   a OE1 
46595 O  OE2 . GLU   AA 101 ? 1.6025 0.6206 1.6922 0.1600  -0.2402 -0.2009 88  GLU   a OE2 
46596 N  N   . PRO   AA 102 ? 1.5522 0.5776 1.5640 0.1428  -0.3704 -0.0710 89  PRO   a N   
46597 C  CA  . PRO   AA 102 ? 1.5444 0.5355 1.5005 0.0996  -0.3403 -0.0507 89  PRO   a CA  
46598 C  C   . PRO   AA 102 ? 1.4989 0.4773 1.4960 0.1099  -0.3040 -0.0182 89  PRO   a C   
46599 O  O   . PRO   AA 102 ? 1.5457 0.3888 1.4509 0.1488  -0.3061 0.0436  89  PRO   a O   
46600 C  CB  . PRO   AA 102 ? 1.5289 0.5904 1.5128 0.0876  -0.3566 -0.0540 89  PRO   a CB  
46601 C  CG  . PRO   AA 102 ? 1.5530 0.5536 1.5695 0.1091  -0.3765 -0.0529 89  PRO   a CG  
46602 C  CD  . PRO   AA 102 ? 1.5673 0.5616 1.5952 0.1243  -0.3903 -0.0747 89  PRO   a CD  
46603 N  N   . SER   AA 103 ? 1.4971 0.4676 1.4606 0.0955  -0.3099 -0.0210 90  SER   a N   
46604 C  CA  . SER   AA 103 ? 1.4054 0.5186 1.4438 0.1053  -0.2838 -0.0436 90  SER   a CA  
46605 C  C   . SER   AA 103 ? 1.4071 0.5835 1.4257 0.1202  -0.3185 -0.0644 90  SER   a C   
46606 O  O   . SER   AA 103 ? 1.3864 0.5126 1.4066 0.1178  -0.2943 -0.0762 90  SER   a O   
46607 C  CB  . SER   AA 103 ? 1.4116 0.5368 1.4165 0.1110  -0.2687 -0.0183 90  SER   a CB  
46608 O  OG  . SER   AA 103 ? 1.3615 0.5552 1.4222 0.1053  -0.2705 0.0692  90  SER   a OG  
46609 N  N   . TYR   AA 104 ? 1.4192 0.6037 1.4572 0.1109  -0.3438 -0.0408 91  TYR   a N   
46610 C  CA  . TYR   AA 104 ? 1.3948 0.6993 1.4663 0.1019  -0.3478 -0.0672 91  TYR   a CA  
46611 C  C   . TYR   AA 104 ? 1.3806 0.6858 1.4030 0.0877  -0.3475 -0.0380 91  TYR   a C   
46612 O  O   . TYR   AA 104 ? 1.3672 0.6890 1.3690 0.0563  -0.3243 -0.0124 91  TYR   a O   
46613 C  CB  . TYR   AA 104 ? 1.4298 0.6939 1.5048 0.0901  -0.3444 -0.0701 91  TYR   a CB  
46614 C  CG  . TYR   AA 104 ? 1.4370 0.7339 1.5722 0.0978  -0.3316 -0.1164 91  TYR   a CG  
46615 C  CD1 . TYR   AA 104 ? 1.4315 0.7734 1.5834 0.1016  -0.3117 -0.1481 91  TYR   a CD1 
46616 C  CD2 . TYR   AA 104 ? 1.4781 0.6594 1.6275 0.0969  -0.3417 -0.1462 91  TYR   a CD2 
46617 C  CE1 . TYR   AA 104 ? 1.4296 0.7226 1.6030 0.0843  -0.2756 -0.1788 91  TYR   a CE1 
46618 C  CE2 . TYR   AA 104 ? 1.4786 0.6263 1.6594 0.0831  -0.3050 -0.1957 91  TYR   a CE2 
46619 C  CZ  . TYR   AA 104 ? 1.4486 0.6311 1.6697 0.0972  -0.2946 -0.2159 91  TYR   a CZ  
46620 O  OH  . TYR   AA 104 ? 1.3942 0.6202 1.6821 0.0480  -0.2846 -0.2525 91  TYR   a OH  
46621 N  N   . ILE   AA 105 ? 1.3467 0.6749 1.3884 0.0997  -0.3754 -0.0294 92  ILE   a N   
46622 C  CA  . ILE   AA 105 ? 1.3554 0.6805 1.3633 0.1043  -0.3865 -0.0541 92  ILE   a CA  
46623 C  C   . ILE   AA 105 ? 1.3582 0.6334 1.3980 0.0882  -0.3655 -0.0732 92  ILE   a C   
46624 O  O   . ILE   AA 105 ? 1.3547 0.7394 1.4635 0.1076  -0.3606 -0.1281 92  ILE   a O   
46625 C  CB  . ILE   AA 105 ? 1.3502 0.6898 1.3565 0.1185  -0.4083 -0.0363 92  ILE   a CB  
46626 C  CG1 . ILE   AA 105 ? 1.3921 0.7215 1.4002 0.1051  -0.4177 -0.0062 92  ILE   a CG1 
46627 C  CG2 . ILE   AA 105 ? 1.3562 0.6675 1.2928 0.1212  -0.4097 -0.0040 92  ILE   a CG2 
46628 C  CD1 . ILE   AA 105 ? 1.4037 0.8048 1.4274 0.1053  -0.4408 0.0014  92  ILE   a CD1 
46629 N  N   . PHE   AA 106 ? 1.3751 0.5994 1.4202 0.0652  -0.3760 -0.1204 93  PHE   a N   
46630 C  CA  . PHE   AA 106 ? 1.4215 0.6313 1.3936 0.1110  -0.3919 -0.1134 93  PHE   a CA  
46631 C  C   . PHE   AA 106 ? 1.3625 0.5298 1.4066 0.0948  -0.3802 -0.1211 93  PHE   a C   
46632 O  O   . PHE   AA 106 ? 1.3598 0.5534 1.4268 0.0912  -0.3896 -0.1250 93  PHE   a O   
46633 C  CB  . PHE   AA 106 ? 1.4419 0.6466 1.3782 0.1162  -0.3786 -0.0660 93  PHE   a CB  
46634 C  CG  . PHE   AA 106 ? 1.5061 0.6823 1.3308 0.1497  -0.3778 -0.0589 93  PHE   a CG  
46635 C  CD1 . PHE   AA 106 ? 1.5245 0.6484 1.2841 0.1643  -0.3945 -0.0150 93  PHE   a CD1 
46636 C  CD2 . PHE   AA 106 ? 1.5025 0.6935 1.3321 0.1718  -0.3680 -0.0239 93  PHE   a CD2 
46637 C  CE1 . PHE   AA 106 ? 1.4742 0.6512 1.2720 0.2256  -0.4080 -0.0310 93  PHE   a CE1 
46638 C  CE2 . PHE   AA 106 ? 1.4742 0.6881 1.3191 0.1900  -0.3730 -0.0356 93  PHE   a CE2 
46639 C  CZ  . PHE   AA 106 ? 1.4779 0.6641 1.2792 0.2105  -0.3884 -0.0025 93  PHE   a CZ  
46640 N  N   . GLU   AA 107 ? 1.3968 0.5103 1.4498 0.0738  -0.3547 -0.1491 94  GLU   a N   
46641 C  CA  . GLU   AA 107 ? 1.4559 0.5748 1.4308 0.0614  -0.3187 -0.1311 94  GLU   a CA  
46642 C  C   . GLU   AA 107 ? 1.4364 0.4936 1.4147 0.0995  -0.2931 -0.1461 94  GLU   a C   
46643 O  O   . GLU   AA 107 ? 1.4972 0.3372 1.4107 0.1124  -0.2861 -0.1299 94  GLU   a O   
46644 C  CB  . GLU   AA 107 ? 1.4654 0.6722 1.5126 0.0726  -0.2631 -0.1430 94  GLU   a CB  
46645 C  CG  . GLU   AA 107 ? 1.5274 0.7540 1.5181 0.0030  -0.2716 -0.1246 94  GLU   a CG  
46646 C  CD  . GLU   AA 107 ? 1.5581 0.7846 1.5862 -0.0794 -0.3005 -0.1615 94  GLU   a CD  
46647 O  OE1 . GLU   AA 107 ? 1.5945 0.8431 1.5571 -0.0629 -0.3070 -0.1839 94  GLU   a OE1 
46648 O  OE2 . GLU   AA 107 ? 1.6309 0.8065 1.6964 -0.1832 -0.3171 -0.1960 94  GLU   a OE2 
46649 N  N   . TYR   AA 108 ? 1.4154 0.5023 1.3867 0.0877  -0.2639 -0.1826 95  TYR   a N   
46650 C  CA  . TYR   AA 108 ? 1.4196 0.4475 1.3252 0.0975  -0.2386 -0.1919 95  TYR   a CA  
46651 C  C   . TYR   AA 108 ? 1.4302 0.4456 1.3326 0.1029  -0.2398 -0.2110 95  TYR   a C   
46652 O  O   . TYR   AA 108 ? 1.4147 0.3282 1.2876 0.1010  -0.2184 -0.3018 95  TYR   a O   
46653 C  CB  . TYR   AA 108 ? 1.4197 0.4235 1.3237 0.0834  -0.2387 -0.1952 95  TYR   a CB  
46654 C  CG  . TYR   AA 108 ? 1.4335 0.3790 1.2431 0.0696  -0.2213 -0.1975 95  TYR   a CG  
46655 C  CD1 . TYR   AA 108 ? 1.4278 0.3740 1.2583 0.0429  -0.2047 -0.1997 95  TYR   a CD1 
46656 C  CD2 . TYR   AA 108 ? 1.4239 0.3367 1.2350 0.0522  -0.2204 -0.1921 95  TYR   a CD2 
46657 C  CE1 . TYR   AA 108 ? 1.4372 0.3125 1.2387 0.0341  -0.1914 -0.2263 95  TYR   a CE1 
46658 C  CE2 . TYR   AA 108 ? 1.4241 0.3623 1.2113 0.0463  -0.2120 -0.2046 95  TYR   a CE2 
46659 C  CZ  . TYR   AA 108 ? 1.3881 0.3307 1.2436 0.0289  -0.1849 -0.2064 95  TYR   a CZ  
46660 O  OH  . TYR   AA 108 ? 1.4086 0.3046 1.2854 0.0038  -0.1560 -0.2181 95  TYR   a OH  
46661 N  N   . LEU   AA 109 ? 1.4353 0.4570 1.3001 0.1041  -0.2729 -0.1889 96  LEU   a N   
46662 C  CA  . LEU   AA 109 ? 1.4149 0.4621 1.2736 0.1069  -0.2761 -0.1588 96  LEU   a CA  
46663 C  C   . LEU   AA 109 ? 1.3592 0.3828 1.2950 0.1378  -0.2943 -0.1635 96  LEU   a C   
46664 O  O   . LEU   AA 109 ? 1.3831 0.2306 1.2768 0.2030  -0.2526 -0.1467 96  LEU   a O   
46665 C  CB  . LEU   AA 109 ? 1.3983 0.5252 1.2815 0.1051  -0.2814 -0.1800 96  LEU   a CB  
46666 C  CG  . LEU   AA 109 ? 1.4138 0.5888 1.2759 0.1132  -0.3030 -0.1682 96  LEU   a CG  
46667 C  CD1 . LEU   AA 109 ? 1.4089 0.6226 1.2855 0.1037  -0.3370 -0.1613 96  LEU   a CD1 
46668 C  CD2 . LEU   AA 109 ? 1.4091 0.6123 1.2890 0.1309  -0.2891 -0.1771 96  LEU   a CD2 
46669 N  N   . ALA   AA 110 ? 1.3907 0.3790 1.2530 0.0977  -0.3025 -0.1239 97  ALA   a N   
46670 C  CA  . ALA   AA 110 ? 1.3859 0.4097 1.2402 0.0973  -0.3168 -0.1123 97  ALA   a CA  
46671 C  C   . ALA   AA 110 ? 1.3982 0.5012 1.2052 0.0896  -0.3045 -0.1160 97  ALA   a C   
46672 O  O   . ALA   AA 110 ? 1.4289 0.3926 1.1718 0.0675  -0.3064 -0.1731 97  ALA   a O   
46673 C  CB  . ALA   AA 110 ? 1.3926 0.4121 1.2663 0.0941  -0.3015 -0.0945 97  ALA   a CB  
46674 N  N   . THR   AA 111 ? 1.3492 0.5016 1.1596 0.1188  -0.3241 -0.0968 98  THR   a N   
46675 C  CA  . THR   AA 111 ? 1.3068 0.5543 1.1425 0.1117  -0.3253 -0.0785 98  THR   a CA  
46676 C  C   . THR   AA 111 ? 1.3028 0.5612 1.1263 0.1224  -0.3353 -0.0406 98  THR   a C   
46677 O  O   . THR   AA 111 ? 1.2333 0.6605 1.1631 0.1049  -0.3537 -0.0308 98  THR   a O   
46678 C  CB  . THR   AA 111 ? 1.3027 0.5580 1.1414 0.1144  -0.3166 -0.1075 98  THR   a CB  
46679 O  OG1 . THR   AA 111 ? 1.2951 0.5176 1.1322 0.1239  -0.3379 -0.1254 98  THR   a OG1 
46680 C  CG2 . THR   AA 111 ? 1.3238 0.6175 1.1149 0.1077  -0.2954 -0.1361 98  THR   a CG2 
46681 N  N   . VAL   AA 112 ? 1.3084 0.5396 1.1172 0.1423  -0.3500 -0.0161 99  VAL   a N   
46682 C  CA  . VAL   AA 112 ? 1.3123 0.5927 1.1084 0.1119  -0.3416 -0.0062 99  VAL   a CA  
46683 C  C   . VAL   AA 112 ? 1.4107 0.5419 1.1498 0.0522  -0.3147 -0.0193 99  VAL   a C   
46684 O  O   . VAL   AA 112 ? 1.4249 0.4175 1.1370 0.0144  -0.3335 -0.0729 99  VAL   a O   
46685 C  CB  . VAL   AA 112 ? 1.3101 0.5936 1.1217 0.1557  -0.3527 0.0334  99  VAL   a CB  
46686 C  CG1 . VAL   AA 112 ? 1.3127 0.6188 1.1022 0.1734  -0.3553 0.0584  99  VAL   a CG1 
46687 C  CG2 . VAL   AA 112 ? 1.3351 0.5844 1.1397 0.1559  -0.3306 -0.0116 99  VAL   a CG2 
46688 N  N   . MET   AA 113 ? 1.4412 0.5720 1.1794 -0.0007 -0.2969 -0.0100 100 MET   a N   
46689 C  CA  . MET   AA 113 ? 1.4650 0.5910 1.1985 0.0227  -0.2457 0.0638  100 MET   a CA  
46690 C  C   . MET   AA 113 ? 1.4426 0.5651 1.1847 -0.0409 -0.2325 0.0470  100 MET   a C   
46691 O  O   . MET   AA 113 ? 1.4094 0.4978 1.2945 -0.1328 -0.2467 0.1769  100 MET   a O   
46692 C  CB  . MET   AA 113 ? 1.4733 0.5936 1.2045 0.0124  -0.2075 0.0576  100 MET   a CB  
46693 C  CG  . MET   AA 113 ? 1.5103 0.6261 1.1966 0.0735  -0.1410 0.0581  100 MET   a CG  
46694 S  SD  . MET   AA 113 ? 1.5822 0.6498 1.1963 0.1108  -0.0859 0.0405  100 MET   a SD  
46695 C  CE  . MET   AA 113 ? 1.6048 0.6461 1.2275 0.0646  -0.0785 0.0661  100 MET   a CE  
46696 N  N   . TYR   AA 114 ? 1.4526 0.5272 1.1839 -0.0078 -0.2624 -0.0221 101 TYR   a N   
46697 C  CA  . TYR   AA 114 ? 1.4114 0.5433 1.1519 0.0056  -0.2345 -0.0831 101 TYR   a CA  
46698 C  C   . TYR   AA 114 ? 1.3996 0.5947 1.1256 0.0443  -0.2977 -0.0642 101 TYR   a C   
46699 O  O   . TYR   AA 114 ? 1.2961 0.5368 1.1107 -0.0425 -0.3243 -0.0876 101 TYR   a O   
46700 C  CB  . TYR   AA 114 ? 1.4327 0.5299 1.1619 0.0258  -0.2142 -0.1171 101 TYR   a CB  
46701 C  CG  . TYR   AA 114 ? 1.4144 0.5556 1.1414 0.0407  -0.1908 -0.1531 101 TYR   a CG  
46702 C  CD1 . TYR   AA 114 ? 1.3838 0.5759 1.1158 0.0270  -0.1934 -0.1238 101 TYR   a CD1 
46703 C  CD2 . TYR   AA 114 ? 1.3988 0.5774 1.1244 0.0549  -0.1981 -0.1555 101 TYR   a CD2 
46704 C  CE1 . TYR   AA 114 ? 1.3484 0.5849 1.0946 0.0210  -0.1873 -0.1493 101 TYR   a CE1 
46705 C  CE2 . TYR   AA 114 ? 1.3656 0.5710 1.1164 0.0403  -0.2071 -0.1615 101 TYR   a CE2 
46706 C  CZ  . TYR   AA 114 ? 1.3444 0.5789 1.0997 0.0208  -0.1900 -0.1516 101 TYR   a CZ  
46707 O  OH  . TYR   AA 114 ? 1.3084 0.5633 1.0908 -0.0039 -0.1942 -0.1726 101 TYR   a OH  
46708 N  N   . GLN   AA 115 ? 1.4683 0.5880 1.1785 0.0573  -0.2987 -0.0657 102 GLN   a N   
46709 C  CA  . GLN   AA 115 ? 1.5086 0.7170 1.1675 0.0638  -0.3404 -0.1271 102 GLN   a CA  
46710 C  C   . GLN   AA 115 ? 1.5700 0.6189 1.1715 0.0905  -0.2818 -0.1051 102 GLN   a C   
46711 O  O   . GLN   AA 115 ? 1.5450 0.6805 1.2334 0.0806  -0.2953 -0.0229 102 GLN   a O   
46712 C  CB  . GLN   AA 115 ? 1.6591 0.7406 1.1566 0.0956  -0.3559 -0.1185 102 GLN   a CB  
46713 C  CG  . GLN   AA 115 ? 1.7496 0.8502 1.1666 0.0998  -0.3339 -0.2153 102 GLN   a CG  
46714 C  CD  . GLN   AA 115 ? 1.8822 0.8941 1.1965 -0.0070 -0.3075 -0.1843 102 GLN   a CD  
46715 O  OE1 . GLN   AA 115 ? 1.9735 1.1180 1.2143 -0.0155 -0.2778 -0.3082 102 GLN   a OE1 
46716 N  NE2 . GLN   AA 115 ? 1.9378 1.0679 1.1430 -0.0698 -0.2770 -0.3089 102 GLN   a NE2 
46717 N  N   . ARG   AA 116 ? 1.4870 0.4766 1.1963 0.0980  -0.2990 -0.1236 103 ARG   a N   
46718 C  CA  . ARG   AA 116 ? 1.4701 0.5081 1.1528 0.0704  -0.2873 -0.1380 103 ARG   a CA  
46719 C  C   . ARG   AA 116 ? 1.4311 0.5555 1.1382 0.0394  -0.2822 -0.0860 103 ARG   a C   
46720 O  O   . ARG   AA 116 ? 1.4380 0.5402 1.1104 0.0014  -0.3330 -0.0929 103 ARG   a O   
46721 C  CB  . ARG   AA 116 ? 1.4509 0.4339 1.1509 0.0866  -0.2810 -0.1120 103 ARG   a CB  
46722 C  CG  . ARG   AA 116 ? 1.4451 0.3475 1.1951 0.1099  -0.2785 -0.1629 103 ARG   a CG  
46723 C  CD  . ARG   AA 116 ? 1.4101 0.3796 1.2133 0.1430  -0.2663 -0.1342 103 ARG   a CD  
46724 N  NE  . ARG   AA 116 ? 1.4205 0.3316 1.2202 0.1422  -0.2777 -0.1300 103 ARG   a NE  
46725 C  CZ  . ARG   AA 116 ? 1.4530 0.4089 1.2165 0.1581  -0.2739 -0.1490 103 ARG   a CZ  
46726 N  NH1 . ARG   AA 116 ? 1.4061 0.4045 1.2329 0.1977  -0.2806 -0.1739 103 ARG   a NH1 
46727 N  NH2 . ARG   AA 116 ? 1.4391 0.5202 1.2169 0.1824  -0.2515 -0.1476 103 ARG   a NH2 
46728 N  N   . ARG   AA 117 ? 1.4296 0.5784 1.1423 0.0382  -0.2590 -0.0607 104 ARG   a N   
46729 C  CA  . ARG   AA 117 ? 1.4060 0.6232 1.0990 0.0749  -0.2441 -0.0378 104 ARG   a CA  
46730 C  C   . ARG   AA 117 ? 1.3579 0.5418 1.0951 0.0860  -0.2440 -0.0217 104 ARG   a C   
46731 O  O   . ARG   AA 117 ? 1.3541 0.5883 1.0991 0.0830  -0.2516 0.0076  104 ARG   a O   
46732 C  CB  . ARG   AA 117 ? 1.3851 0.7158 1.1057 0.0635  -0.2123 -0.0292 104 ARG   a CB  
46733 C  CG  . ARG   AA 117 ? 1.4172 0.7652 1.1028 0.0643  -0.1971 -0.0227 104 ARG   a CG  
46734 C  CD  . ARG   AA 117 ? 1.4026 0.7659 1.1349 0.0612  -0.1873 -0.0025 104 ARG   a CD  
46735 N  NE  . ARG   AA 117 ? 1.3976 0.7778 1.1393 0.0287  -0.1793 -0.0112 104 ARG   a NE  
46736 C  CZ  . ARG   AA 117 ? 1.3648 0.7534 1.1214 0.0073  -0.1840 -0.0345 104 ARG   a CZ  
46737 N  NH1 . ARG   AA 117 ? 1.3541 0.7529 1.1283 0.0160  -0.1899 0.0541  104 ARG   a NH1 
46738 N  NH2 . ARG   AA 117 ? 1.3618 0.7435 1.1316 -0.0332 -0.2045 -0.0665 104 ARG   a NH2 
46739 N  N   . SER   AA 118 ? 1.3778 0.4917 1.1131 0.0566  -0.2530 -0.0154 105 SER   a N   
46740 C  CA  . SER   AA 118 ? 1.4191 0.4357 1.1207 0.0600  -0.2586 -0.0273 105 SER   a CA  
46741 C  C   . SER   AA 118 ? 1.4062 0.4519 1.1272 0.0840  -0.2722 -0.0072 105 SER   a C   
46742 O  O   . SER   AA 118 ? 1.4108 0.3992 1.1411 0.1143  -0.2884 0.0417  105 SER   a O   
46743 C  CB  . SER   AA 118 ? 1.4392 0.4223 1.1146 0.0342  -0.2410 -0.0749 105 SER   a CB  
46744 O  OG  . SER   AA 118 ? 1.4853 0.3040 1.1040 0.0019  -0.2033 -0.1119 105 SER   a OG  
46745 N  N   . LYS   AA 119 ? 1.4646 0.5373 1.1320 0.0828  -0.2587 0.0198  106 LYS   a N   
46746 C  CA  . LYS   AA 119 ? 1.4888 0.6209 1.1683 0.0440  -0.2839 0.0356  106 LYS   a CA  
46747 C  C   . LYS   AA 119 ? 1.4061 0.6318 1.1657 0.0460  -0.3189 0.0631  106 LYS   a C   
46748 O  O   . LYS   AA 119 ? 1.3691 0.5784 1.1346 0.0454  -0.4135 0.0109  106 LYS   a O   
46749 C  CB  . LYS   AA 119 ? 1.6181 0.7419 1.2218 0.0225  -0.2584 0.1296  106 LYS   a CB  
46750 C  CG  . LYS   AA 119 ? 1.7367 0.7537 1.2996 0.0112  -0.2080 0.1247  106 LYS   a CG  
46751 C  CD  . LYS   AA 119 ? 1.8059 0.8363 1.3864 -0.0569 -0.1766 0.2391  106 LYS   a CD  
46752 C  CE  . LYS   AA 119 ? 1.8453 0.9202 1.4943 -0.1488 -0.1616 0.2882  106 LYS   a CE  
46753 N  NZ  . LYS   AA 119 ? 1.8330 0.9198 1.5457 -0.1842 -0.1255 0.3655  106 LYS   a NZ  
46754 N  N   . MET   AA 120 ? 1.4517 0.6245 1.2048 0.0444  -0.3087 0.0729  107 MET   a N   
46755 C  CA  . MET   AA 120 ? 1.4686 0.6652 1.2204 0.0579  -0.2834 0.0441  107 MET   a CA  
46756 C  C   . MET   AA 120 ? 1.4715 0.6351 1.2176 0.0673  -0.2867 0.0557  107 MET   a C   
46757 O  O   . MET   AA 120 ? 1.5041 0.6359 1.3091 0.1045  -0.2982 0.0772  107 MET   a O   
46758 C  CB  . MET   AA 120 ? 1.4786 0.7568 1.2223 0.0177  -0.3132 0.0255  107 MET   a CB  
46759 C  CG  . MET   AA 120 ? 1.4853 0.7553 1.2129 -0.0281 -0.3321 0.0159  107 MET   a CG  
46760 S  SD  . MET   AA 120 ? 1.5547 0.6756 1.2520 0.0074  -0.3394 -0.0112 107 MET   a SD  
46761 C  CE  . MET   AA 120 ? 1.4466 0.7223 1.2512 -0.0074 -0.3831 0.0093  107 MET   a CE  
46762 N  N   . ASN   AA 121 ? 1.4517 0.6023 1.1836 0.0536  -0.2713 0.0352  108 ASN   a N   
46763 C  CA  . ASN   AA 121 ? 1.4536 0.6139 1.1952 0.0278  -0.2591 0.0234  108 ASN   a CA  
46764 C  C   . ASN   AA 121 ? 1.4486 0.5612 1.2546 0.0072  -0.2847 0.0319  108 ASN   a C   
46765 O  O   . ASN   AA 121 ? 1.4115 0.5562 1.2513 0.0018  -0.3001 0.0182  108 ASN   a O   
46766 C  CB  . ASN   AA 121 ? 1.4429 0.6129 1.1791 0.0357  -0.2294 0.0270  108 ASN   a CB  
46767 C  CG  . ASN   AA 121 ? 1.4350 0.6928 1.1806 0.0476  -0.2231 0.0301  108 ASN   a CG  
46768 O  OD1 . ASN   AA 121 ? 1.3718 0.7192 1.0848 0.1031  -0.2277 0.0572  108 ASN   a OD1 
46769 N  ND2 . ASN   AA 121 ? 1.4569 0.6438 1.1851 0.0117  -0.2104 0.0481  108 ASN   a ND2 
46770 N  N   . PRO   AA 122 ? 1.5524 0.5918 1.3111 -0.0604 -0.2833 0.0369  109 PRO   a N   
46771 C  CA  . PRO   AA 122 ? 1.5976 0.5316 1.2913 -0.0583 -0.3034 -0.0072 109 PRO   a CA  
46772 C  C   . PRO   AA 122 ? 1.6025 0.4700 1.2761 -0.0168 -0.3352 -0.0458 109 PRO   a C   
46773 O  O   . PRO   AA 122 ? 1.6086 0.6122 1.3816 -0.0770 -0.2499 -0.0655 109 PRO   a O   
46774 C  CB  . PRO   AA 122 ? 1.6221 0.5769 1.3168 -0.1081 -0.2719 -0.0021 109 PRO   a CB  
46775 C  CG  . PRO   AA 122 ? 1.6065 0.6095 1.2977 -0.1032 -0.3173 -0.0016 109 PRO   a CG  
46776 C  CD  . PRO   AA 122 ? 1.5262 0.5849 1.3152 -0.0900 -0.3167 0.0518  109 PRO   a CD  
46777 N  N   . LEU   AA 123 ? 1.6588 0.4361 1.3204 0.0282  -0.3948 -0.1206 110 LEU   a N   
46778 C  CA  . LEU   AA 123 ? 1.6647 0.4539 1.3199 0.0350  -0.3727 -0.1089 110 LEU   a CA  
46779 C  C   . LEU   AA 123 ? 1.6385 0.4335 1.3299 0.0595  -0.3417 -0.1154 110 LEU   a C   
46780 O  O   . LEU   AA 123 ? 1.6140 0.3306 1.3773 0.0683  -0.3510 -0.1137 110 LEU   a O   
46781 C  CB  . LEU   AA 123 ? 1.6713 0.4397 1.3127 0.0341  -0.3755 -0.1232 110 LEU   a CB  
46782 C  CG  . LEU   AA 123 ? 1.6409 0.4397 1.2390 0.0404  -0.3664 -0.1397 110 LEU   a CG  
46783 C  CD1 . LEU   AA 123 ? 1.6761 0.3741 1.2368 0.0317  -0.3702 -0.1550 110 LEU   a CD1 
46784 C  CD2 . LEU   AA 123 ? 1.5889 0.4304 1.2311 0.0313  -0.3967 -0.1347 110 LEU   a CD2 
46785 N  N   . TRP   AA 124 ? 1.6536 0.4934 1.2782 0.0731  -0.3111 -0.0955 111 TRP   a N   
46786 C  CA  . TRP   AA 124 ? 1.5894 0.5057 1.2230 0.0366  -0.3301 -0.0628 111 TRP   a CA  
46787 C  C   . TRP   AA 124 ? 1.5440 0.4407 1.1798 0.0013  -0.2877 -0.0813 111 TRP   a C   
46788 O  O   . TRP   AA 124 ? 1.5831 0.3420 1.0924 -0.1003 -0.3434 -0.0537 111 TRP   a O   
46789 C  CB  . TRP   AA 124 ? 1.6026 0.5736 1.2565 0.0670  -0.2964 -0.0330 111 TRP   a CB  
46790 C  CG  . TRP   AA 124 ? 1.6024 0.5485 1.2301 0.0584  -0.3108 -0.0651 111 TRP   a CG  
46791 C  CD1 . TRP   AA 124 ? 1.6040 0.5302 1.2692 0.0386  -0.2990 -0.0429 111 TRP   a CD1 
46792 C  CD2 . TRP   AA 124 ? 1.6350 0.5288 1.2381 0.1004  -0.2870 -0.0269 111 TRP   a CD2 
46793 N  NE1 . TRP   AA 124 ? 1.5752 0.6378 1.2292 0.0715  -0.3282 0.0065  111 TRP   a NE1 
46794 C  CE2 . TRP   AA 124 ? 1.5900 0.5477 1.2274 0.0573  -0.3063 -0.0404 111 TRP   a CE2 
46795 C  CE3 . TRP   AA 124 ? 1.6506 0.5610 1.2349 0.1086  -0.2889 -0.0237 111 TRP   a CE3 
46796 C  CZ2 . TRP   AA 124 ? 1.6340 0.6138 1.2135 0.0655  -0.2800 -0.0123 111 TRP   a CZ2 
46797 C  CZ3 . TRP   AA 124 ? 1.6620 0.5633 1.2276 0.1039  -0.2691 -0.0168 111 TRP   a CZ3 
46798 C  CH2 . TRP   AA 124 ? 1.6598 0.5725 1.2114 0.0797  -0.2648 -0.0284 111 TRP   a CH2 
46799 N  N   . ASN   AA 125 ? 1.5150 0.3679 1.1478 -0.0070 -0.3165 -0.1098 112 ASN   a N   
46800 C  CA  . ASN   AA 125 ? 1.4921 0.4076 1.1481 0.0287  -0.3045 -0.1399 112 ASN   a CA  
46801 C  C   . ASN   AA 125 ? 1.4775 0.3839 1.1741 0.0378  -0.2993 -0.1785 112 ASN   a C   
46802 O  O   . ASN   AA 125 ? 1.5097 0.4010 1.2196 0.0475  -0.2205 -0.2203 112 ASN   a O   
46803 C  CB  . ASN   AA 125 ? 1.5109 0.4396 1.1176 0.0748  -0.3385 -0.1318 112 ASN   a CB  
46804 C  CG  . ASN   AA 125 ? 1.5111 0.4672 1.1479 0.0713  -0.3367 -0.1437 112 ASN   a CG  
46805 O  OD1 . ASN   AA 125 ? 1.5465 0.4265 1.1413 0.0890  -0.3397 -0.1324 112 ASN   a OD1 
46806 N  ND2 . ASN   AA 125 ? 1.5259 0.5559 1.1561 0.1124  -0.3536 -0.1719 112 ASN   a ND2 
46807 N  N   . ALA   AA 126 ? 1.4446 0.4510 1.2229 0.0270  -0.3383 -0.1598 113 ALA   a N   
46808 C  CA  . ALA   AA 126 ? 1.4460 0.5247 1.2339 0.0117  -0.3397 -0.1332 113 ALA   a CA  
46809 C  C   . ALA   AA 126 ? 1.4519 0.4482 1.2355 -0.0462 -0.3406 -0.1218 113 ALA   a C   
46810 O  O   . ALA   AA 126 ? 1.4126 0.3923 1.1948 -0.0768 -0.3932 -0.0714 113 ALA   a O   
46811 C  CB  . ALA   AA 126 ? 1.4608 0.5406 1.2745 -0.0246 -0.3346 -0.1130 113 ALA   a CB  
46812 N  N   . ILE   AA 127 ? 1.4393 0.4492 1.2615 -0.0632 -0.3300 -0.1278 114 ILE   a N   
46813 C  CA  . ILE   AA 127 ? 1.4551 0.5306 1.2824 -0.0563 -0.3530 -0.0860 114 ILE   a CA  
46814 C  C   . ILE   AA 127 ? 1.4624 0.4712 1.2429 -0.0810 -0.3587 -0.1469 114 ILE   a C   
46815 O  O   . ILE   AA 127 ? 1.4671 0.4243 1.2561 -0.1132 -0.3389 -0.1619 114 ILE   a O   
46816 C  CB  . ILE   AA 127 ? 1.4327 0.5402 1.3256 -0.0926 -0.3503 -0.0654 114 ILE   a CB  
46817 C  CG1 . ILE   AA 127 ? 1.4315 0.5935 1.3448 -0.1061 -0.3757 -0.0405 114 ILE   a CG1 
46818 C  CG2 . ILE   AA 127 ? 1.4420 0.5797 1.3522 -0.0628 -0.3264 -0.0426 114 ILE   a CG2 
46819 C  CD1 . ILE   AA 127 ? 1.4363 0.6292 1.3377 -0.1174 -0.3799 -0.0565 114 ILE   a CD1 
46820 N  N   . ILE   AA 128 ? 1.5054 0.4813 1.2524 -0.0465 -0.3818 -0.1767 115 ILE   a N   
46821 C  CA  . ILE   AA 128 ? 1.5134 0.5446 1.2841 -0.0051 -0.3788 -0.1691 115 ILE   a CA  
46822 C  C   . ILE   AA 128 ? 1.5331 0.5036 1.2410 -0.0141 -0.3734 -0.2139 115 ILE   a C   
46823 O  O   . ILE   AA 128 ? 1.5417 0.5073 1.2220 -0.0465 -0.3932 -0.2199 115 ILE   a O   
46824 C  CB  . ILE   AA 128 ? 1.5539 0.5666 1.2944 -0.0117 -0.4082 -0.1735 115 ILE   a CB  
46825 C  CG1 . ILE   AA 128 ? 1.5940 0.5997 1.3096 -0.0034 -0.4119 -0.1429 115 ILE   a CG1 
46826 C  CG2 . ILE   AA 128 ? 1.5540 0.6045 1.3333 0.0064  -0.4043 -0.1657 115 ILE   a CG2 
46827 C  CD1 . ILE   AA 128 ? 1.6287 0.5952 1.3419 0.0066  -0.4237 -0.1506 115 ILE   a CD1 
46828 N  N   . VAL   AA 129 ? 1.5458 0.4897 1.2311 -0.0003 -0.3807 -0.2078 116 VAL   a N   
46829 C  CA  . VAL   AA 129 ? 1.5293 0.5130 1.2441 0.0253  -0.3888 -0.1973 116 VAL   a CA  
46830 C  C   . VAL   AA 129 ? 1.5124 0.4437 1.2193 0.0412  -0.3624 -0.2094 116 VAL   a C   
46831 O  O   . VAL   AA 129 ? 1.5066 0.4749 1.1987 0.0375  -0.3634 -0.2389 116 VAL   a O   
46832 C  CB  . VAL   AA 129 ? 1.5507 0.5060 1.2745 0.0325  -0.4113 -0.2064 116 VAL   a CB  
46833 C  CG1 . VAL   AA 129 ? 1.5463 0.5421 1.2916 0.0400  -0.4613 -0.2021 116 VAL   a CG1 
46834 C  CG2 . VAL   AA 129 ? 1.5332 0.5276 1.3260 0.0459  -0.3905 -0.1882 116 VAL   a CG2 
46835 N  N   . ALA   AA 130 ? 1.5586 0.4283 1.2200 0.0699  -0.3507 -0.1862 117 ALA   a N   
46836 C  CA  . ALA   AA 130 ? 1.5416 0.5061 1.2966 0.1056  -0.3621 -0.1182 117 ALA   a CA  
46837 C  C   . ALA   AA 130 ? 1.5713 0.5244 1.3343 0.1547  -0.3548 -0.1191 117 ALA   a C   
46838 O  O   . ALA   AA 130 ? 1.6057 0.5331 1.3557 0.1967  -0.3247 -0.0721 117 ALA   a O   
46839 C  CB  . ALA   AA 130 ? 1.5748 0.5503 1.2733 0.0987  -0.3591 -0.1247 117 ALA   a CB  
46840 N  N   . GLY   AA 131 ? 1.5692 0.5677 1.3404 0.1713  -0.3613 -0.0892 118 GLY   a N   
46841 C  CA  . GLY   AA 131 ? 1.6001 0.6230 1.3250 0.2111  -0.4002 -0.0821 118 GLY   a CA  
46842 C  C   . GLY   AA 131 ? 1.5991 0.6207 1.3006 0.2289  -0.4207 -0.0718 118 GLY   a C   
46843 O  O   . GLY   AA 131 ? 1.6402 0.5355 1.1747 0.2721  -0.4500 -0.0814 118 GLY   a O   
46844 N  N   . VAL   AA 132 ? 1.5745 0.6860 1.3425 0.2802  -0.4667 -0.0727 119 VAL   a N   
46845 C  CA  . VAL   AA 132 ? 1.5454 0.6942 1.3817 0.2683  -0.5066 -0.0439 119 VAL   a CA  
46846 C  C   . VAL   AA 132 ? 1.5631 0.6845 1.4232 0.2580  -0.4922 -0.0449 119 VAL   a C   
46847 O  O   . VAL   AA 132 ? 1.5843 0.7242 1.3989 0.2203  -0.5300 -0.0271 119 VAL   a O   
46848 C  CB  . VAL   AA 132 ? 1.5381 0.6482 1.4160 0.2750  -0.5327 -0.0113 119 VAL   a CB  
46849 C  CG1 . VAL   AA 132 ? 1.5088 0.7119 1.4408 0.2661  -0.5603 0.0079  119 VAL   a CG1 
46850 C  CG2 . VAL   AA 132 ? 1.5439 0.6380 1.4147 0.2873  -0.5299 -0.0052 119 VAL   a CG2 
46851 N  N   . GLN   AA 133 ? 1.5600 0.7114 1.4743 0.2500  -0.4630 -0.0952 120 GLN   a N   
46852 C  CA  . GLN   AA 133 ? 1.5746 0.7421 1.4987 0.2584  -0.4541 -0.1244 120 GLN   a CA  
46853 C  C   . GLN   AA 133 ? 1.6048 0.7934 1.4770 0.2640  -0.4804 -0.1104 120 GLN   a C   
46854 O  O   . GLN   AA 133 ? 1.5852 0.7643 1.4029 0.3362  -0.4702 -0.0522 120 GLN   a O   
46855 C  CB  . GLN   AA 133 ? 1.5500 0.7437 1.5286 0.2482  -0.4202 -0.1523 120 GLN   a CB  
46856 C  CG  . GLN   AA 133 ? 1.5253 0.6799 1.5305 0.2564  -0.4021 -0.1876 120 GLN   a CG  
46857 C  CD  . GLN   AA 133 ? 1.5503 0.6297 1.5072 0.2595  -0.3887 -0.2420 120 GLN   a CD  
46858 O  OE1 . GLN   AA 133 ? 1.5294 0.5314 1.5522 0.2788  -0.4082 -0.2599 120 GLN   a OE1 
46859 N  NE2 . GLN   AA 133 ? 1.5783 0.6455 1.5011 0.1986  -0.4079 -0.2593 120 GLN   a NE2 
46860 N  N   . SER   AA 134 ? 1.6160 0.7633 1.5228 0.2561  -0.5008 -0.0872 121 SER   a N   
46861 C  CA  . SER   AA 134 ? 1.6715 0.7839 1.5300 0.2477  -0.5191 -0.0491 121 SER   a CA  
46862 C  C   . SER   AA 134 ? 1.7032 0.7226 1.5484 0.2029  -0.5183 -0.1209 121 SER   a C   
46863 O  O   . SER   AA 134 ? 1.8351 0.6449 1.5537 0.2155  -0.5550 -0.1365 121 SER   a O   
46864 C  CB  . SER   AA 134 ? 1.6558 0.7963 1.5625 0.2200  -0.5155 -0.0390 121 SER   a CB  
46865 O  OG  . SER   AA 134 ? 1.6671 0.9867 1.5882 0.2154  -0.4843 0.0230  121 SER   a OG  
46866 N  N   . ASN   AA 135 ? 1.7009 0.7171 1.5614 0.1825  -0.4885 -0.1440 122 ASN   a N   
46867 C  CA  . ASN   AA 135 ? 1.7145 0.7173 1.5986 0.1410  -0.4720 -0.1528 122 ASN   a CA  
46868 C  C   . ASN   AA 135 ? 1.6467 0.6875 1.6380 0.0858  -0.5012 -0.1102 122 ASN   a C   
46869 O  O   . ASN   AA 135 ? 1.6357 0.6712 1.6929 0.0855  -0.5308 -0.1177 122 ASN   a O   
46870 C  CB  . ASN   AA 135 ? 1.7268 0.7740 1.6247 0.1392  -0.4135 -0.1624 122 ASN   a CB  
46871 C  CG  . ASN   AA 135 ? 1.7551 0.7583 1.5748 0.1586  -0.3615 -0.1786 122 ASN   a CG  
46872 O  OD1 . ASN   AA 135 ? 1.7766 0.7908 1.5336 0.1379  -0.3217 -0.1843 122 ASN   a OD1 
46873 N  ND2 . ASN   AA 135 ? 1.7964 0.8444 1.6118 0.1265  -0.2858 -0.2160 122 ASN   a ND2 
46874 N  N   . GLY   AA 136 ? 1.6336 0.6869 1.6089 0.0691  -0.5071 -0.0998 123 GLY   a N   
46875 C  CA  . GLY   AA 136 ? 1.6388 0.8027 1.5986 0.0581  -0.5051 -0.1627 123 GLY   a CA  
46876 C  C   . GLY   AA 136 ? 1.6126 0.8325 1.6248 0.0442  -0.4966 -0.1284 123 GLY   a C   
46877 O  O   . GLY   AA 136 ? 1.6302 0.8237 1.6509 -0.0249 -0.5058 -0.1317 123 GLY   a O   
46878 N  N   . ASP   AA 137 ? 1.5510 0.8543 1.6173 0.0316  -0.4652 -0.1387 124 ASP   a N   
46879 C  CA  . ASP   AA 137 ? 1.5077 0.7803 1.6746 -0.0161 -0.4263 -0.1502 124 ASP   a CA  
46880 C  C   . ASP   AA 137 ? 1.5375 0.7293 1.6725 0.0065  -0.4386 -0.1527 124 ASP   a C   
46881 O  O   . ASP   AA 137 ? 1.5587 0.8033 1.7192 -0.0105 -0.4238 -0.1030 124 ASP   a O   
46882 C  CB  . ASP   AA 137 ? 1.4964 0.7631 1.6649 -0.0256 -0.3873 -0.1374 124 ASP   a CB  
46883 C  CG  . ASP   AA 137 ? 1.4981 0.7485 1.6956 -0.0597 -0.3722 -0.1515 124 ASP   a CG  
46884 O  OD1 . ASP   AA 137 ? 1.5764 0.6410 1.8045 -0.1634 -0.3962 -0.2047 124 ASP   a OD1 
46885 O  OD2 . ASP   AA 137 ? 1.5488 0.7521 1.6640 -0.0370 -0.2906 -0.1205 124 ASP   a OD2 
46886 N  N   . GLN   AA 138 ? 1.4719 0.7259 1.6858 0.0079  -0.4302 -0.1486 125 GLN   a N   
46887 C  CA  . GLN   AA 138 ? 1.4730 0.7167 1.6888 0.0308  -0.4345 -0.0992 125 GLN   a CA  
46888 C  C   . GLN   AA 138 ? 1.4564 0.5810 1.6360 0.0421  -0.3912 -0.0936 125 GLN   a C   
46889 O  O   . GLN   AA 138 ? 1.3956 0.4906 1.6771 0.0526  -0.3402 -0.0725 125 GLN   a O   
46890 C  CB  . GLN   AA 138 ? 1.4371 0.7316 1.7140 0.0312  -0.4416 -0.1188 125 GLN   a CB  
46891 C  CG  . GLN   AA 138 ? 1.4147 0.8134 1.7570 0.0287  -0.4530 -0.1366 125 GLN   a CG  
46892 C  CD  . GLN   AA 138 ? 1.4011 0.8722 1.8462 0.0092  -0.4570 -0.1789 125 GLN   a CD  
46893 O  OE1 . GLN   AA 138 ? 1.3501 1.0063 1.8941 0.0042  -0.3975 -0.2026 125 GLN   a OE1 
46894 N  NE2 . GLN   AA 138 ? 1.3879 0.8414 1.8866 0.0287  -0.4588 -0.1904 125 GLN   a NE2 
46895 N  N   . PHE   AA 139 ? 1.4768 0.5704 1.7016 0.0253  -0.3773 -0.1064 126 PHE   a N   
46896 C  CA  . PHE   AA 139 ? 1.5882 0.6385 1.6298 0.0395  -0.3994 -0.1161 126 PHE   a CA  
46897 C  C   . PHE   AA 139 ? 1.6070 0.6062 1.6149 0.0556  -0.4193 -0.0762 126 PHE   a C   
46898 O  O   . PHE   AA 139 ? 1.6297 0.6497 1.6150 0.0967  -0.4144 -0.0761 126 PHE   a O   
46899 C  CB  . PHE   AA 139 ? 1.6244 0.6388 1.6129 0.0449  -0.4184 -0.1444 126 PHE   a CB  
46900 C  CG  . PHE   AA 139 ? 1.6368 0.6687 1.5574 0.0463  -0.3908 -0.1521 126 PHE   a CG  
46901 C  CD1 . PHE   AA 139 ? 1.6470 0.6443 1.5386 0.0530  -0.3804 -0.1530 126 PHE   a CD1 
46902 C  CD2 . PHE   AA 139 ? 1.6290 0.7067 1.5716 0.0389  -0.3566 -0.1482 126 PHE   a CD2 
46903 C  CE1 . PHE   AA 139 ? 1.6276 0.6111 1.5127 0.0333  -0.3565 -0.1634 126 PHE   a CE1 
46904 C  CE2 . PHE   AA 139 ? 1.6418 0.7170 1.5211 0.0292  -0.3258 -0.1525 126 PHE   a CE2 
46905 C  CZ  . PHE   AA 139 ? 1.6399 0.6586 1.5230 0.0237  -0.3279 -0.1582 126 PHE   a CZ  
46906 N  N   . LEU   AA 140 ? 1.5792 0.5905 1.5713 0.0282  -0.3728 -0.0820 127 LEU   a N   
46907 C  CA  . LEU   AA 140 ? 1.5854 0.5048 1.5014 -0.0172 -0.3246 -0.0460 127 LEU   a CA  
46908 C  C   . LEU   AA 140 ? 1.5205 0.3925 1.4642 -0.0610 -0.2808 -0.0675 127 LEU   a C   
46909 O  O   . LEU   AA 140 ? 1.5731 0.4760 1.5159 -0.0699 -0.1972 -0.0870 127 LEU   a O   
46910 C  CB  . LEU   AA 140 ? 1.5933 0.5381 1.4880 -0.0505 -0.3339 -0.0353 127 LEU   a CB  
46911 C  CG  . LEU   AA 140 ? 1.5991 0.5799 1.4658 -0.0399 -0.3224 -0.0302 127 LEU   a CG  
46912 C  CD1 . LEU   AA 140 ? 1.6283 0.5614 1.4617 -0.0574 -0.3362 -0.0166 127 LEU   a CD1 
46913 C  CD2 . LEU   AA 140 ? 1.5934 0.6076 1.5240 -0.0730 -0.3150 -0.0115 127 LEU   a CD2 
46914 N  N   . ARG   AA 141 ? 1.5206 0.3450 1.4208 -0.0363 -0.3038 -0.1045 128 ARG   a N   
46915 C  CA  . ARG   AA 141 ? 1.5254 0.4235 1.3925 -0.0052 -0.2734 -0.1004 128 ARG   a CA  
46916 C  C   . ARG   AA 141 ? 1.5397 0.4359 1.4139 0.0142  -0.2832 -0.1348 128 ARG   a C   
46917 O  O   . ARG   AA 141 ? 1.6227 0.3904 1.4544 0.0152  -0.2603 -0.1041 128 ARG   a O   
46918 C  CB  . ARG   AA 141 ? 1.5129 0.4576 1.3282 0.0202  -0.2453 -0.0819 128 ARG   a CB  
46919 C  CG  . ARG   AA 141 ? 1.4908 0.4728 1.3111 0.0247  -0.2395 -0.0999 128 ARG   a CG  
46920 C  CD  . ARG   AA 141 ? 1.4797 0.5228 1.2826 0.0079  -0.2520 -0.1291 128 ARG   a CD  
46921 N  NE  . ARG   AA 141 ? 1.4733 0.5529 1.2574 0.0025  -0.2364 -0.1551 128 ARG   a NE  
46922 C  CZ  . ARG   AA 141 ? 1.4582 0.6192 1.2360 -0.0169 -0.2189 -0.1750 128 ARG   a CZ  
46923 N  NH1 . ARG   AA 141 ? 1.4382 0.6656 1.2391 -0.0176 -0.2028 -0.1793 128 ARG   a NH1 
46924 N  NH2 . ARG   AA 141 ? 1.4704 0.6534 1.2317 -0.0222 -0.2110 -0.1661 128 ARG   a NH2 
46925 N  N   . TYR   AA 142 ? 1.4768 0.4856 1.3677 0.0314  -0.3132 -0.1778 129 TYR   a N   
46926 C  CA  . TYR   AA 142 ? 1.4246 0.5838 1.3628 -0.0001 -0.3259 -0.2270 129 TYR   a CA  
46927 C  C   . TYR   AA 142 ? 1.3919 0.4776 1.3513 0.0142  -0.2789 -0.2580 129 TYR   a C   
46928 O  O   . TYR   AA 142 ? 1.4127 0.6162 1.3653 -0.0154 -0.2552 -0.2871 129 TYR   a O   
46929 C  CB  . TYR   AA 142 ? 1.3673 0.6021 1.3562 -0.0090 -0.3451 -0.1638 129 TYR   a CB  
46930 C  CG  . TYR   AA 142 ? 1.3156 0.6851 1.2881 -0.0320 -0.3658 -0.1608 129 TYR   a CG  
46931 C  CD1 . TYR   AA 142 ? 1.2901 0.7849 1.2911 -0.0465 -0.3570 -0.1308 129 TYR   a CD1 
46932 C  CD2 . TYR   AA 142 ? 1.2968 0.6958 1.2630 -0.0386 -0.3951 -0.1762 129 TYR   a CD2 
46933 C  CE1 . TYR   AA 142 ? 1.3195 0.7917 1.2830 -0.0135 -0.3383 -0.1201 129 TYR   a CE1 
46934 C  CE2 . TYR   AA 142 ? 1.2825 0.7554 1.2345 -0.0379 -0.3983 -0.1692 129 TYR   a CE2 
46935 C  CZ  . TYR   AA 142 ? 1.2655 0.7709 1.2451 0.0007  -0.3981 -0.1188 129 TYR   a CZ  
46936 O  OH  . TYR   AA 142 ? 1.2665 0.8794 1.2571 0.0145  -0.4257 0.0046  129 TYR   a OH  
46937 N  N   . VAL   AA 143 ? 1.3843 0.3540 1.2900 -0.0006 -0.3189 -0.2455 130 VAL   a N   
46938 C  CA  . VAL   AA 143 ? 1.3974 0.4404 1.2477 -0.0246 -0.3216 -0.1885 130 VAL   a CA  
46939 C  C   . VAL   AA 143 ? 1.4072 0.3161 1.2047 -0.0633 -0.2949 -0.2038 130 VAL   a C   
46940 O  O   . VAL   AA 143 ? 1.3888 0.2671 1.1926 -0.0877 -0.3254 -0.1903 130 VAL   a O   
46941 C  CB  . VAL   AA 143 ? 1.4359 0.4413 1.2726 -0.0469 -0.3679 -0.1793 130 VAL   a CB  
46942 C  CG1 . VAL   AA 143 ? 1.4757 0.4907 1.2915 -0.0816 -0.3726 -0.1616 130 VAL   a CG1 
46943 C  CG2 . VAL   AA 143 ? 1.4440 0.4520 1.2439 -0.0352 -0.3623 -0.1638 130 VAL   a CG2 
46944 N  N   . ASN   AA 144 ? 1.4027 0.3191 1.1616 -0.0658 -0.2441 -0.1688 131 ASN   a N   
46945 C  CA  . ASN   AA 144 ? 1.4083 0.3889 1.1702 -0.0555 -0.2013 -0.1317 131 ASN   a CA  
46946 C  C   . ASN   AA 144 ? 1.3806 0.3421 1.1743 -0.0516 -0.1894 -0.1179 131 ASN   a C   
46947 O  O   . ASN   AA 144 ? 1.3713 0.3720 1.2143 -0.0775 -0.1564 -0.1499 131 ASN   a O   
46948 C  CB  . ASN   AA 144 ? 1.4378 0.4017 1.1436 -0.0802 -0.1834 -0.0984 131 ASN   a CB  
46949 C  CG  . ASN   AA 144 ? 1.4626 0.4030 1.1573 -0.0780 -0.1634 -0.0738 131 ASN   a CG  
46950 O  OD1 . ASN   AA 144 ? 1.4722 0.4379 1.1231 -0.0481 -0.1279 -0.0670 131 ASN   a OD1 
46951 N  ND2 . ASN   AA 144 ? 1.4628 0.4108 1.1338 -0.0909 -0.1538 -0.0663 131 ASN   a ND2 
46952 N  N   . LEU   AA 145 ? 1.3895 0.3667 1.1807 -0.0241 -0.2030 -0.0812 132 LEU   a N   
46953 C  CA  . LEU   AA 145 ? 1.3792 0.3629 1.1822 0.0008  -0.2076 -0.0545 132 LEU   a CA  
46954 C  C   . LEU   AA 145 ? 1.3845 0.3377 1.1684 -0.0028 -0.2293 -0.0828 132 LEU   a C   
46955 O  O   . LEU   AA 145 ? 1.3487 0.4276 1.0849 0.0705  -0.2657 -0.1339 132 LEU   a O   
46956 C  CB  . LEU   AA 145 ? 1.3763 0.3005 1.2184 -0.0034 -0.1902 0.0313  132 LEU   a CB  
46957 C  CG  . LEU   AA 145 ? 1.3872 0.3148 1.2287 -0.0305 -0.1855 0.0578  132 LEU   a CG  
46958 C  CD1 . LEU   AA 145 ? 1.3628 0.2557 1.2107 -0.0485 -0.2123 0.1161  132 LEU   a CD1 
46959 C  CD2 . LEU   AA 145 ? 1.4063 0.2560 1.2267 -0.0280 -0.1761 0.0720  132 LEU   a CD2 
46960 N  N   . LEU   AA 146 ? 1.4315 0.3669 1.1939 0.0185  -0.1833 -0.0308 133 LEU   a N   
46961 C  CA  . LEU   AA 146 ? 1.4647 0.3950 1.2011 0.0557  -0.1702 -0.0783 133 LEU   a CA  
46962 C  C   . LEU   AA 146 ? 1.4544 0.3450 1.2075 0.0311  -0.1911 -0.0786 133 LEU   a C   
46963 O  O   . LEU   AA 146 ? 1.4340 0.2927 1.2078 0.0157  -0.2003 -0.0836 133 LEU   a O   
46964 C  CB  . LEU   AA 146 ? 1.4689 0.4009 1.2415 0.0647  -0.1309 -0.0681 133 LEU   a CB  
46965 C  CG  . LEU   AA 146 ? 1.4865 0.4296 1.2557 0.0963  -0.1399 -0.0631 133 LEU   a CG  
46966 C  CD1 . LEU   AA 146 ? 1.4838 0.4494 1.3047 0.1052  -0.1189 -0.0102 133 LEU   a CD1 
46967 C  CD2 . LEU   AA 146 ? 1.4853 0.3911 1.2067 0.1195  -0.1301 -0.0778 133 LEU   a CD2 
46968 N  N   . GLY   AA 147 ? 1.4645 0.3950 1.1872 0.0028  -0.2067 -0.0690 134 GLY   a N   
46969 C  CA  . GLY   AA 147 ? 1.4552 0.4701 1.2150 0.0223  -0.1960 -0.0820 134 GLY   a CA  
46970 C  C   . GLY   AA 147 ? 1.4656 0.5065 1.2266 0.0015  -0.1948 -0.0820 134 GLY   a C   
46971 O  O   . GLY   AA 147 ? 1.3810 0.5958 1.2132 -0.0049 -0.1893 -0.0604 134 GLY   a O   
46972 N  N   . VAL   AA 148 ? 1.5049 0.5181 1.2341 -0.0211 -0.2092 -0.0913 135 VAL   a N   
46973 C  CA  . VAL   AA 148 ? 1.4732 0.5489 1.2662 0.0052  -0.2060 -0.0833 135 VAL   a CA  
46974 C  C   . VAL   AA 148 ? 1.4521 0.5480 1.3244 0.0505  -0.2188 -0.0952 135 VAL   a C   
46975 O  O   . VAL   AA 148 ? 1.4853 0.5864 1.3368 0.0339  -0.2112 -0.1258 135 VAL   a O   
46976 C  CB  . VAL   AA 148 ? 1.4748 0.5398 1.2610 -0.0040 -0.2291 -0.0450 135 VAL   a CB  
46977 C  CG1 . VAL   AA 148 ? 1.4606 0.5549 1.2665 -0.0008 -0.2147 -0.0336 135 VAL   a CG1 
46978 C  CG2 . VAL   AA 148 ? 1.5051 0.5448 1.2424 -0.0018 -0.2304 -0.0381 135 VAL   a CG2 
46979 N  N   . THR   AA 149 ? 1.4706 0.5351 1.3235 0.0473  -0.1934 -0.1252 136 THR   a N   
46980 C  CA  . THR   AA 149 ? 1.4796 0.5841 1.3179 0.0028  -0.2230 -0.1276 136 THR   a CA  
46981 C  C   . THR   AA 149 ? 1.5467 0.4338 1.3120 0.0066  -0.2319 -0.1391 136 THR   a C   
46982 O  O   . THR   AA 149 ? 1.5917 0.4008 1.3627 -0.0288 -0.1491 -0.1537 136 THR   a O   
46983 C  CB  . THR   AA 149 ? 1.4606 0.6147 1.3029 0.0353  -0.2409 -0.1587 136 THR   a CB  
46984 O  OG1 . THR   AA 149 ? 1.3955 0.7536 1.3540 0.0252  -0.2126 -0.1583 136 THR   a OG1 
46985 C  CG2 . THR   AA 149 ? 1.4742 0.6263 1.2946 0.0210  -0.2407 -0.1367 136 THR   a CG2 
46986 N  N   . TYR   AA 150 ? 1.5730 0.3077 1.3259 0.0045  -0.2605 -0.1143 137 TYR   a N   
46987 C  CA  . TYR   AA 150 ? 1.5652 0.4316 1.3658 -0.0150 -0.2561 -0.1357 137 TYR   a CA  
46988 C  C   . TYR   AA 150 ? 1.5786 0.3506 1.4045 -0.0303 -0.2795 -0.1081 137 TYR   a C   
46989 O  O   . TYR   AA 150 ? 1.6441 0.2555 1.4191 -0.0867 -0.2637 -0.1664 137 TYR   a O   
46990 C  CB  . TYR   AA 150 ? 1.5625 0.4478 1.3769 0.0140  -0.2591 -0.1111 137 TYR   a CB  
46991 C  CG  . TYR   AA 150 ? 1.6073 0.4320 1.3807 0.0302  -0.2654 -0.1378 137 TYR   a CG  
46992 C  CD1 . TYR   AA 150 ? 1.6257 0.3642 1.4029 0.0306  -0.2762 -0.1743 137 TYR   a CD1 
46993 C  CD2 . TYR   AA 150 ? 1.6380 0.4099 1.3602 0.0301  -0.2789 -0.1281 137 TYR   a CD2 
46994 C  CE1 . TYR   AA 150 ? 1.6472 0.3672 1.3602 0.0354  -0.2794 -0.1731 137 TYR   a CE1 
46995 C  CE2 . TYR   AA 150 ? 1.6418 0.3398 1.3356 0.0215  -0.2972 -0.1330 137 TYR   a CE2 
46996 C  CZ  . TYR   AA 150 ? 1.6464 0.3269 1.3335 0.0529  -0.2588 -0.1482 137 TYR   a CZ  
46997 O  OH  . TYR   AA 150 ? 1.6107 0.3417 1.3557 0.1121  -0.2755 -0.0681 137 TYR   a OH  
46998 N  N   . SER   AA 151 ? 1.5638 0.4531 1.4060 -0.0197 -0.2804 -0.0646 138 SER   a N   
46999 C  CA  . SER   AA 151 ? 1.5249 0.5720 1.4490 0.0000  -0.2944 -0.0471 138 SER   a CA  
47000 C  C   . SER   AA 151 ? 1.5244 0.5710 1.4351 -0.0135 -0.2879 0.0169  138 SER   a C   
47001 O  O   . SER   AA 151 ? 1.5620 0.6233 1.4763 0.0307  -0.2350 0.0547  138 SER   a O   
47002 C  CB  . SER   AA 151 ? 1.5220 0.6187 1.5137 0.0167  -0.2859 -0.1250 138 SER   a CB  
47003 O  OG  . SER   AA 151 ? 1.6559 0.8116 1.4857 0.0030  -0.3172 -0.1486 138 SER   a OG  
47004 N  N   . SER   AA 152 ? 1.5322 0.5646 1.4435 -0.0265 -0.3369 0.0344  139 SER   a N   
47005 C  CA  . SER   AA 152 ? 1.5330 0.6465 1.4032 -0.0571 -0.3828 0.0192  139 SER   a CA  
47006 C  C   . SER   AA 152 ? 1.4762 0.5576 1.4157 -0.0348 -0.3724 0.0519  139 SER   a C   
47007 O  O   . SER   AA 152 ? 1.5678 0.6808 1.3458 -0.0490 -0.3354 0.0634  139 SER   a O   
47008 C  CB  . SER   AA 152 ? 1.4962 0.7090 1.4256 -0.0326 -0.4208 -0.0415 139 SER   a CB  
47009 O  OG  . SER   AA 152 ? 1.5688 0.8420 1.4567 -0.1351 -0.4502 -0.0711 139 SER   a OG  
47010 N  N   . PRO   AA 153 ? 1.4276 0.4918 1.4049 0.0048  -0.3615 0.0778  140 PRO   a N   
47011 C  CA  . PRO   AA 153 ? 1.4184 0.5062 1.4031 0.0143  -0.3701 0.0509  140 PRO   a CA  
47012 C  C   . PRO   AA 153 ? 1.4124 0.4295 1.3657 0.0027  -0.4025 0.0079  140 PRO   a C   
47013 O  O   . PRO   AA 153 ? 1.3589 0.4046 1.3434 0.0061  -0.4116 -0.0233 140 PRO   a O   
47014 C  CB  . PRO   AA 153 ? 1.4283 0.5011 1.4393 0.0143  -0.3605 0.0879  140 PRO   a CB  
47015 C  CG  . PRO   AA 153 ? 1.4199 0.5585 1.4600 0.0148  -0.3413 0.0881  140 PRO   a CG  
47016 C  CD  . PRO   AA 153 ? 1.4111 0.5438 1.4474 0.0107  -0.3344 0.0813  140 PRO   a CD  
47017 N  N   . THR   AA 154 ? 1.4532 0.4246 1.3037 0.0111  -0.3968 0.0134  141 THR   a N   
47018 C  CA  . THR   AA 154 ? 1.5069 0.4342 1.2831 0.0021  -0.3841 -0.0512 141 THR   a CA  
47019 C  C   . THR   AA 154 ? 1.4851 0.4736 1.3230 -0.0410 -0.3706 -0.0725 141 THR   a C   
47020 O  O   . THR   AA 154 ? 1.4692 0.6150 1.2764 -0.0970 -0.3357 -0.1365 141 THR   a O   
47021 C  CB  . THR   AA 154 ? 1.5301 0.4349 1.2754 0.0486  -0.3939 -0.0644 141 THR   a CB  
47022 O  OG1 . THR   AA 154 ? 1.5480 0.2406 1.3055 0.0772  -0.4130 -0.1432 141 THR   a OG1 
47023 C  CG2 . THR   AA 154 ? 1.5264 0.4323 1.3044 0.0556  -0.4003 -0.0794 141 THR   a CG2 
47024 N  N   . LEU   AA 155 ? 1.5152 0.4185 1.3217 -0.0479 -0.3564 -0.0889 142 LEU   a N   
47025 C  CA  . LEU   AA 155 ? 1.5371 0.4816 1.3223 -0.0085 -0.3738 -0.1133 142 LEU   a CA  
47026 C  C   . LEU   AA 155 ? 1.5220 0.3653 1.3518 0.0029  -0.4088 -0.1805 142 LEU   a C   
47027 O  O   . LEU   AA 155 ? 1.5397 0.2992 1.3517 0.0232  -0.4542 -0.2065 142 LEU   a O   
47028 C  CB  . LEU   AA 155 ? 1.6238 0.4720 1.3457 0.0035  -0.3735 -0.1055 142 LEU   a CB  
47029 C  CG  . LEU   AA 155 ? 1.6771 0.5443 1.3838 0.0249  -0.3202 -0.0637 142 LEU   a CG  
47030 C  CD1 . LEU   AA 155 ? 1.7295 0.5463 1.4424 0.0495  -0.3314 -0.0800 142 LEU   a CD1 
47031 C  CD2 . LEU   AA 155 ? 1.6803 0.5208 1.4239 -0.0147 -0.2841 -0.0074 142 LEU   a CD2 
47032 N  N   . ALA   AA 156 ? 1.5166 0.3619 1.3484 0.0007  -0.4300 -0.2228 143 ALA   a N   
47033 C  CA  . ALA   AA 156 ? 1.5615 0.3755 1.3556 0.0238  -0.4074 -0.2209 143 ALA   a CA  
47034 C  C   . ALA   AA 156 ? 1.5614 0.3292 1.3131 0.0679  -0.3809 -0.2269 143 ALA   a C   
47035 O  O   . ALA   AA 156 ? 1.5997 0.2372 1.3049 0.0980  -0.3722 -0.2342 143 ALA   a O   
47036 C  CB  . ALA   AA 156 ? 1.5630 0.3848 1.3349 0.0053  -0.4256 -0.2104 143 ALA   a CB  
47037 N  N   . THR   AA 157 ? 1.5612 0.3807 1.3617 0.0859  -0.3656 -0.2162 144 THR   a N   
47038 C  CA  . THR   AA 157 ? 1.5769 0.4534 1.3319 0.0518  -0.3700 -0.1819 144 THR   a CA  
47039 C  C   . THR   AA 157 ? 1.5758 0.4892 1.3736 0.1277  -0.3761 -0.1070 144 THR   a C   
47040 O  O   . THR   AA 157 ? 1.6544 0.5397 1.4281 0.0875  -0.3526 -0.1908 144 THR   a O   
47041 C  CB  . THR   AA 157 ? 1.5745 0.4569 1.2916 0.0420  -0.3692 -0.2104 144 THR   a CB  
47042 O  OG1 . THR   AA 157 ? 1.5770 0.3007 1.2878 0.0078  -0.3707 -0.1700 144 THR   a OG1 
47043 C  CG2 . THR   AA 157 ? 1.5301 0.4805 1.2486 0.0455  -0.3812 -0.1997 144 THR   a CG2 
47044 N  N   . GLY   AA 158 ? 1.6065 0.6055 1.3284 0.1170  -0.3534 -0.0251 145 GLY   a N   
47045 C  CA  . GLY   AA 158 ? 1.6090 0.6210 1.3469 0.1127  -0.3197 -0.0394 145 GLY   a CA  
47046 C  C   . GLY   AA 158 ? 1.6221 0.5951 1.3923 0.1190  -0.2992 -0.0322 145 GLY   a C   
47047 O  O   . GLY   AA 158 ? 1.6197 0.5805 1.4925 0.1342  -0.2425 -0.0743 145 GLY   a O   
47048 N  N   . PHE   AA 159 ? 1.5880 0.6227 1.3303 0.1165  -0.2593 0.0462  146 PHE   a N   
47049 C  CA  . PHE   AA 159 ? 1.5297 0.6996 1.3180 0.0619  -0.2581 0.0466  146 PHE   a CA  
47050 C  C   . PHE   AA 159 ? 1.5419 0.6229 1.3150 0.0619  -0.2783 0.0607  146 PHE   a C   
47051 O  O   . PHE   AA 159 ? 1.4949 0.8420 1.4729 -0.0352 -0.2687 0.0502  146 PHE   a O   
47052 C  CB  . PHE   AA 159 ? 1.5240 0.7601 1.3151 0.0836  -0.2203 0.1089  146 PHE   a CB  
47053 C  CG  . PHE   AA 159 ? 1.5459 0.7014 1.3640 0.0855  -0.1683 0.1454  146 PHE   a CG  
47054 C  CD1 . PHE   AA 159 ? 1.5478 0.6897 1.4258 0.0678  -0.1583 0.1350  146 PHE   a CD1 
47055 C  CD2 . PHE   AA 159 ? 1.5390 0.7877 1.3727 0.0911  -0.1316 0.1491  146 PHE   a CD2 
47056 C  CE1 . PHE   AA 159 ? 1.5827 0.6309 1.4341 0.0503  -0.1470 0.1833  146 PHE   a CE1 
47057 C  CE2 . PHE   AA 159 ? 1.5488 0.7116 1.3784 0.0496  -0.1292 0.1913  146 PHE   a CE2 
47058 C  CZ  . PHE   AA 159 ? 1.5636 0.6739 1.4232 0.0696  -0.1606 0.1725  146 PHE   a CZ  
47059 N  N   . GLY   AA 160 ? 1.5599 0.5860 1.2581 0.0104  -0.2587 0.0461  147 GLY   a N   
47060 C  CA  . GLY   AA 160 ? 1.5649 0.5848 1.2913 0.0199  -0.2590 0.0104  147 GLY   a CA  
47061 C  C   . GLY   AA 160 ? 1.5736 0.4930 1.2845 0.0203  -0.2489 -0.0539 147 GLY   a C   
47062 O  O   . GLY   AA 160 ? 1.5864 0.3096 1.4218 0.0388  -0.2550 -0.0818 147 GLY   a O   
47063 N  N   . ALA   AA 161 ? 1.5890 0.5318 1.2746 0.0365  -0.2391 -0.0782 148 ALA   a N   
47064 C  CA  . ALA   AA 161 ? 1.6154 0.5540 1.2867 0.0249  -0.2236 -0.0762 148 ALA   a CA  
47065 C  C   . ALA   AA 161 ? 1.6355 0.5609 1.3117 0.0084  -0.2066 -0.0670 148 ALA   a C   
47066 O  O   . ALA   AA 161 ? 1.6324 0.5559 1.4302 0.0182  -0.1659 -0.0693 148 ALA   a O   
47067 C  CB  . ALA   AA 161 ? 1.6279 0.6686 1.2652 0.0425  -0.2169 -0.0964 148 ALA   a CB  
47068 N  N   . HIS   AA 162 ? 1.6592 0.5977 1.2603 0.0399  -0.2311 -0.0638 149 HIS   a N   
47069 C  CA  . HIS   AA 162 ? 1.6985 0.5932 1.2773 0.0450  -0.2752 -0.0542 149 HIS   a CA  
47070 C  C   . HIS   AA 162 ? 1.7007 0.4866 1.3280 0.0239  -0.2907 -0.0463 149 HIS   a C   
47071 O  O   . HIS   AA 162 ? 1.7390 0.5703 1.4546 -0.0306 -0.2299 -0.0606 149 HIS   a O   
47072 C  CB  . HIS   AA 162 ? 1.7583 0.5588 1.2479 0.0921  -0.2768 -0.0520 149 HIS   a CB  
47073 C  CG  . HIS   AA 162 ? 1.8034 0.6012 1.2069 0.1226  -0.2778 -0.0121 149 HIS   a CG  
47074 N  ND1 . HIS   AA 162 ? 1.8256 0.5755 1.1833 0.1158  -0.2496 0.0169  149 HIS   a ND1 
47075 C  CD2 . HIS   AA 162 ? 1.8313 0.6274 1.2050 0.1420  -0.2616 -0.0140 149 HIS   a CD2 
47076 C  CE1 . HIS   AA 162 ? 1.8570 0.5381 1.1719 0.1339  -0.2493 0.0049  149 HIS   a CE1 
47077 N  NE2 . HIS   AA 162 ? 1.8475 0.5961 1.1285 0.1562  -0.2576 0.0080  149 HIS   a NE2 
47078 N  N   . MET   AA 163 ? 1.6238 0.4611 1.3207 0.0264  -0.3565 -0.0341 150 MET   a N   
47079 C  CA  . MET   AA 163 ? 1.5974 0.4702 1.2930 0.0595  -0.3853 -0.0008 150 MET   a CA  
47080 C  C   . MET   AA 163 ? 1.5806 0.5233 1.2926 0.0263  -0.4498 -0.0045 150 MET   a C   
47081 O  O   . MET   AA 163 ? 1.6378 0.4095 1.3700 -0.0071 -0.4684 0.0170  150 MET   a O   
47082 C  CB  . MET   AA 163 ? 1.6088 0.5254 1.2602 0.1030  -0.3950 -0.0038 150 MET   a CB  
47083 C  CG  . MET   AA 163 ? 1.5919 0.6317 1.2505 0.1529  -0.3847 -0.0245 150 MET   a CG  
47084 S  SD  . MET   AA 163 ? 1.5970 0.7569 1.2988 0.2239  -0.3896 -0.0640 150 MET   a SD  
47085 C  CE  . MET   AA 163 ? 1.6207 0.6715 1.3486 0.2205  -0.3773 -0.0237 150 MET   a CE  
47086 N  N   . ALA   AA 164 ? 1.5342 0.5225 1.2358 0.0353  -0.4834 -0.0016 151 ALA   a N   
47087 C  CA  . ALA   AA 164 ? 1.5091 0.4763 1.2238 0.0057  -0.4672 0.0084  151 ALA   a CA  
47088 C  C   . ALA   AA 164 ? 1.4846 0.4950 1.2356 0.0183  -0.4707 0.0036  151 ALA   a C   
47089 O  O   . ALA   AA 164 ? 1.4432 0.5000 1.2749 -0.0025 -0.4301 -0.0165 151 ALA   a O   
47090 C  CB  . ALA   AA 164 ? 1.4981 0.4996 1.2019 -0.0190 -0.4935 0.0126  151 ALA   a CB  
47091 N  N   . ASN   AA 165 ? 1.4344 0.5297 1.2284 0.0233  -0.4372 -0.0065 152 ASN   a N   
47092 C  CA  . ASN   AA 165 ? 1.4282 0.6123 1.2507 0.0239  -0.4342 -0.0203 152 ASN   a CA  
47093 C  C   . ASN   AA 165 ? 1.4232 0.6189 1.2907 0.0261  -0.4519 -0.0204 152 ASN   a C   
47094 O  O   . ASN   AA 165 ? 1.4448 0.5631 1.2745 0.0408  -0.4863 0.0331  152 ASN   a O   
47095 C  CB  . ASN   AA 165 ? 1.4322 0.7324 1.2325 0.0122  -0.4077 -0.0350 152 ASN   a CB  
47096 C  CG  . ASN   AA 165 ? 1.4401 0.7866 1.1939 0.0056  -0.3865 -0.1133 152 ASN   a CG  
47097 O  OD1 . ASN   AA 165 ? 1.3806 0.9108 1.1680 0.0552  -0.4104 -0.1114 152 ASN   a OD1 
47098 N  ND2 . ASN   AA 165 ? 1.4542 0.9746 1.1391 0.0252  -0.3770 -0.0925 152 ASN   a ND2 
47099 N  N   . PRO   AA 166 ? 1.4064 0.6059 1.3379 0.0239  -0.4400 -0.1132 153 PRO   a N   
47100 C  CA  . PRO   AA 166 ? 1.4419 0.5709 1.3539 0.0264  -0.4473 -0.1463 153 PRO   a CA  
47101 C  C   . PRO   AA 166 ? 1.4153 0.5783 1.3770 0.0180  -0.4578 -0.1595 153 PRO   a C   
47102 O  O   . PRO   AA 166 ? 1.4241 0.6026 1.4545 -0.0057 -0.4392 -0.1737 153 PRO   a O   
47103 C  CB  . PRO   AA 166 ? 1.4369 0.5662 1.3554 0.0196  -0.4467 -0.1430 153 PRO   a CB  
47104 C  CG  . PRO   AA 166 ? 1.4068 0.5599 1.3517 0.0308  -0.4354 -0.1274 153 PRO   a CG  
47105 C  CD  . PRO   AA 166 ? 1.4117 0.5659 1.3400 0.0399  -0.4196 -0.1182 153 PRO   a CD  
47106 N  N   . LEU   AA 167 ? 1.4233 0.6000 1.3575 0.0158  -0.4722 -0.1583 154 LEU   a N   
47107 C  CA  . LEU   AA 167 ? 1.4141 0.6278 1.3669 0.0006  -0.4865 -0.1656 154 LEU   a CA  
47108 C  C   . LEU   AA 167 ? 1.4060 0.6336 1.3892 0.0034  -0.5195 -0.1578 154 LEU   a C   
47109 O  O   . LEU   AA 167 ? 1.4164 0.5616 1.4975 -0.0305 -0.5452 -0.1725 154 LEU   a O   
47110 C  CB  . LEU   AA 167 ? 1.4131 0.6445 1.3218 -0.0062 -0.5057 -0.1691 154 LEU   a CB  
47111 C  CG  . LEU   AA 167 ? 1.4062 0.6444 1.2655 -0.0072 -0.5065 -0.1599 154 LEU   a CG  
47112 C  CD1 . LEU   AA 167 ? 1.4259 0.6408 1.2517 -0.0147 -0.5044 -0.1655 154 LEU   a CD1 
47113 C  CD2 . LEU   AA 167 ? 1.4023 0.6517 1.2643 -0.0030 -0.5334 -0.1527 154 LEU   a CD2 
47114 N  N   . LEU   AA 168 ? 1.4256 0.6260 1.3461 0.0183  -0.4952 -0.1706 155 LEU   a N   
47115 C  CA  . LEU   AA 168 ? 1.4303 0.6148 1.3434 0.0115  -0.4797 -0.1836 155 LEU   a CA  
47116 C  C   . LEU   AA 168 ? 1.3936 0.6620 1.3931 0.0153  -0.4792 -0.1747 155 LEU   a C   
47117 O  O   . LEU   AA 168 ? 1.3987 0.5958 1.4391 -0.0069 -0.4989 -0.1691 155 LEU   a O   
47118 C  CB  . LEU   AA 168 ? 1.4464 0.5603 1.3070 0.0305  -0.4614 -0.1754 155 LEU   a CB  
47119 C  CG  . LEU   AA 168 ? 1.4710 0.5198 1.2697 0.0611  -0.4533 -0.1785 155 LEU   a CG  
47120 C  CD1 . LEU   AA 168 ? 1.4595 0.4972 1.2599 0.0682  -0.4467 -0.1540 155 LEU   a CD1 
47121 C  CD2 . LEU   AA 168 ? 1.4997 0.4868 1.2679 0.0560  -0.4616 -0.1972 155 LEU   a CD2 
47122 N  N   . ARG   AA 169 ? 1.3899 0.7278 1.3967 0.0135  -0.4532 -0.1448 156 ARG   a N   
47123 C  CA  . ARG   AA 169 ? 1.3712 0.7774 1.4438 -0.0080 -0.4414 -0.1406 156 ARG   a CA  
47124 C  C   . ARG   AA 169 ? 1.3947 0.8022 1.4015 -0.0198 -0.4863 -0.1055 156 ARG   a C   
47125 O  O   . ARG   AA 169 ? 1.3445 0.8700 1.3800 -0.0674 -0.5318 -0.1135 156 ARG   a O   
47126 C  CB  . ARG   AA 169 ? 1.3461 0.7495 1.4575 0.0045  -0.4483 -0.1608 156 ARG   a CB  
47127 C  CG  . ARG   AA 169 ? 1.3537 0.7351 1.5009 0.0050  -0.4214 -0.1973 156 ARG   a CG  
47128 C  CD  . ARG   AA 169 ? 1.3698 0.6526 1.5322 0.0311  -0.4196 -0.2171 156 ARG   a CD  
47129 N  NE  . ARG   AA 169 ? 1.3685 0.7065 1.5753 0.0222  -0.4291 -0.2524 156 ARG   a NE  
47130 C  CZ  . ARG   AA 169 ? 1.3343 0.6678 1.6142 0.0562  -0.4110 -0.2199 156 ARG   a CZ  
47131 N  NH1 . ARG   AA 169 ? 1.3236 0.6413 1.5754 -0.0047 -0.4077 -0.2154 156 ARG   a NH1 
47132 N  NH2 . ARG   AA 169 ? 1.2669 0.7724 1.6572 0.0212  -0.4027 -0.2566 156 ARG   a NH2 
47133 N  N   . LYS   AA 170 ? 1.4716 0.7840 1.3734 0.0025  -0.4608 -0.0702 157 LYS   a N   
47134 C  CA  . LYS   AA 170 ? 1.5432 0.8476 1.4561 -0.0620 -0.4674 -0.0780 157 LYS   a CA  
47135 C  C   . LYS   AA 170 ? 1.5787 0.8721 1.4745 -0.0484 -0.4733 -0.0701 157 LYS   a C   
47136 O  O   . LYS   AA 170 ? 1.6080 1.0101 1.4610 -0.1040 -0.5019 -0.1081 157 LYS   a O   
47137 C  CB  . LYS   AA 170 ? 1.6027 0.8323 1.4906 -0.0362 -0.4678 -0.0744 157 LYS   a CB  
47138 C  CG  . LYS   AA 170 ? 1.6312 0.8096 1.5482 -0.0579 -0.4868 -0.0678 157 LYS   a CG  
47139 C  CD  . LYS   AA 170 ? 1.6517 0.7940 1.5627 -0.0729 -0.4867 -0.0781 157 LYS   a CD  
47140 C  CE  . LYS   AA 170 ? 1.6942 0.8276 1.6202 -0.1083 -0.5085 -0.0860 157 LYS   a CE  
47141 N  NZ  . LYS   AA 170 ? 1.7348 0.7996 1.6782 -0.1318 -0.5169 -0.0888 157 LYS   a NZ  
47142 N  N   . VAL   AA 171 ? 1.6230 0.8487 1.4999 -0.0459 -0.4671 -0.0831 158 VAL   a N   
47143 C  CA  . VAL   AA 171 ? 1.6312 0.7828 1.5135 -0.0776 -0.4597 -0.0767 158 VAL   a CA  
47144 C  C   . VAL   AA 171 ? 1.6386 0.7553 1.5914 -0.0663 -0.4357 -0.0891 158 VAL   a C   
47145 O  O   . VAL   AA 171 ? 1.6223 0.7726 1.6039 -0.1057 -0.4473 -0.1671 158 VAL   a O   
47146 C  CB  . VAL   AA 171 ? 1.6476 0.7490 1.4967 -0.0884 -0.4728 -0.0766 158 VAL   a CB  
47147 C  CG1 . VAL   AA 171 ? 1.6552 0.7161 1.5093 -0.1070 -0.4826 -0.0842 158 VAL   a CG1 
47148 C  CG2 . VAL   AA 171 ? 1.6315 0.7617 1.4632 -0.0752 -0.4618 -0.0427 158 VAL   a CG2 
47149 N  N   . VAL   AA 172 ? 1.6410 0.6605 1.6221 -0.0803 -0.4198 -0.0828 159 VAL   a N   
47150 C  CA  . VAL   AA 172 ? 1.6547 0.7035 1.6736 -0.0350 -0.3680 -0.0830 159 VAL   a CA  
47151 C  C   . VAL   AA 172 ? 1.6398 0.5710 1.6926 -0.0299 -0.3661 -0.0905 159 VAL   a C   
47152 O  O   . VAL   AA 172 ? 1.6214 0.3480 1.6591 -0.0197 -0.3403 -0.0774 159 VAL   a O   
47153 C  CB  . VAL   AA 172 ? 1.6636 0.7298 1.7275 -0.0467 -0.3553 -0.0354 159 VAL   a CB  
47154 C  CG1 . VAL   AA 172 ? 1.6762 0.7623 1.7727 -0.0217 -0.3679 -0.0243 159 VAL   a CG1 
47155 C  CG2 . VAL   AA 172 ? 1.6686 0.8040 1.6878 -0.0253 -0.3511 -0.0414 159 VAL   a CG2 
47156 N  N   . ASP   AA 173 ? 1.6491 0.6409 1.6884 -0.0237 -0.3399 -0.0776 160 ASP   a N   
47157 C  CA  . ASP   AA 173 ? 1.6877 0.8117 1.6481 0.0061  -0.3843 -0.0834 160 ASP   a CA  
47158 C  C   . ASP   AA 173 ? 1.6785 0.8610 1.6593 -0.0089 -0.4003 -0.1177 160 ASP   a C   
47159 O  O   . ASP   AA 173 ? 1.6198 0.8063 1.6945 0.0819  -0.4202 -0.1637 160 ASP   a O   
47160 C  CB  . ASP   AA 173 ? 1.7328 0.8960 1.6590 -0.0737 -0.3853 -0.0884 160 ASP   a CB  
47161 C  CG  . ASP   AA 173 ? 1.8056 0.9300 1.6183 -0.1206 -0.3731 -0.0299 160 ASP   a CG  
47162 O  OD1 . ASP   AA 173 ? 1.8144 1.0784 1.6329 -0.1174 -0.3592 -0.0048 160 ASP   a OD1 
47163 O  OD2 . ASP   AA 173 ? 1.7984 0.9312 1.6482 -0.2264 -0.4118 -0.1162 160 ASP   a OD2 
47164 N  N   . ARG   AA 174 ? 1.6447 0.9331 1.7478 -0.0058 -0.4249 -0.0753 161 ARG   a N   
47165 C  CA  . ARG   AA 174 ? 1.6584 1.0433 1.7471 -0.0520 -0.3713 -0.1052 161 ARG   a CA  
47166 C  C   . ARG   AA 174 ? 1.7294 1.0342 1.8223 -0.0611 -0.3957 -0.0978 161 ARG   a C   
47167 O  O   . ARG   AA 174 ? 1.8662 1.1008 1.8190 -0.1269 -0.3913 -0.1060 161 ARG   a O   
47168 C  CB  . ARG   AA 174 ? 1.6269 1.1792 1.8184 -0.0544 -0.3637 -0.0414 161 ARG   a CB  
47169 C  CG  . ARG   AA 174 ? 1.5835 1.2588 1.8670 -0.0464 -0.3223 -0.0009 161 ARG   a CG  
47170 C  CD  . ARG   AA 174 ? 1.5573 1.2448 1.8640 -0.0502 -0.2895 0.0323  161 ARG   a CD  
47171 N  NE  . ARG   AA 174 ? 1.4916 1.3172 1.8186 -0.0294 -0.2401 0.0667  161 ARG   a NE  
47172 C  CZ  . ARG   AA 174 ? 1.4119 1.2974 1.8296 -0.0029 -0.2390 0.0951  161 ARG   a CZ  
47173 N  NH1 . ARG   AA 174 ? 1.4372 1.3819 1.8001 -0.0333 -0.1671 0.0615  161 ARG   a NH1 
47174 N  NH2 . ARG   AA 174 ? 1.3435 1.3146 1.7640 -0.0361 -0.2244 0.1128  161 ARG   a NH2 
47175 N  N   . GLU   AA 175 ? 1.7379 1.0516 1.9029 -0.0129 -0.3577 -0.1191 162 GLU   a N   
47176 C  CA  . GLU   AA 175 ? 1.7217 1.0837 1.9016 0.0738  -0.3452 -0.1363 162 GLU   a CA  
47177 C  C   . GLU   AA 175 ? 1.6695 0.9417 1.8756 0.0981  -0.3119 -0.1878 162 GLU   a C   
47178 O  O   . GLU   AA 175 ? 1.7223 0.9915 1.8138 0.1586  -0.3405 -0.2086 162 GLU   a O   
47179 C  CB  . GLU   AA 175 ? 1.7865 1.2442 1.8784 0.0410  -0.2721 -0.1366 162 GLU   a CB  
47180 C  CG  . GLU   AA 175 ? 1.9094 1.2579 1.9715 0.0163  -0.2870 -0.1056 162 GLU   a CG  
47181 C  CD  . GLU   AA 175 ? 1.9161 1.4257 2.0087 0.0059  -0.3172 -0.0675 162 GLU   a CD  
47182 O  OE1 . GLU   AA 175 ? 2.0006 1.4354 2.0821 -0.0343 -0.2406 -0.1027 162 GLU   a OE1 
47183 O  OE2 . GLU   AA 175 ? 2.0687 1.3525 1.9182 -0.0197 -0.4267 0.0584  162 GLU   a OE2 
47184 N  N   . SER   AA 176 ? 1.6794 0.8554 1.8472 0.1051  -0.3043 -0.2188 163 SER   a N   
47185 C  CA  . SER   AA 176 ? 1.7221 0.9536 1.8485 0.0708  -0.3298 -0.2172 163 SER   a CA  
47186 C  C   . SER   AA 176 ? 1.6792 0.9439 1.8264 0.0714  -0.3683 -0.1992 163 SER   a C   
47187 O  O   . SER   AA 176 ? 1.7455 1.0008 1.8838 0.0789  -0.4212 -0.1617 163 SER   a O   
47188 C  CB  . SER   AA 176 ? 1.7551 1.0058 1.8496 0.0612  -0.2862 -0.2264 163 SER   a CB  
47189 O  OG  . SER   AA 176 ? 1.7297 1.0518 1.8528 0.0959  -0.2830 -0.2050 163 SER   a OG  
47190 N  N   . ASP   AA 177 ? 1.6111 0.9494 1.8208 0.0428  -0.4090 -0.1623 164 ASP   a N   
47191 C  CA  . ASP   AA 177 ? 1.5874 0.9526 1.8178 0.0495  -0.4240 -0.1582 164 ASP   a CA  
47192 C  C   . ASP   AA 177 ? 1.5350 0.8273 1.8419 0.0509  -0.4349 -0.2263 164 ASP   a C   
47193 O  O   . ASP   AA 177 ? 1.5767 0.7484 1.8545 0.0257  -0.4295 -0.2691 164 ASP   a O   
47194 C  CB  . ASP   AA 177 ? 1.5594 1.0289 1.8000 0.0666  -0.4750 -0.0988 164 ASP   a CB  
47195 C  CG  . ASP   AA 177 ? 1.5786 1.0685 1.8205 0.0606  -0.4935 -0.0581 164 ASP   a CG  
47196 O  OD1 . ASP   AA 177 ? 1.5868 1.1289 1.9032 0.0091  -0.5044 -0.0629 164 ASP   a OD1 
47197 O  OD2 . ASP   AA 177 ? 1.5211 1.1867 1.8049 0.0997  -0.5143 -0.0880 164 ASP   a OD2 
47198 N  N   . ILE   AA 178 ? 1.4607 0.7890 1.8130 0.0946  -0.4096 -0.2151 165 ILE   a N   
47199 C  CA  . ILE   AA 178 ? 1.4349 0.7534 1.7713 0.1188  -0.4216 -0.2311 165 ILE   a CA  
47200 C  C   . ILE   AA 178 ? 1.4597 0.7885 1.8090 0.1035  -0.4481 -0.1969 165 ILE   a C   
47201 O  O   . ILE   AA 178 ? 1.4151 0.8409 1.7800 0.0921  -0.4993 -0.1970 165 ILE   a O   
47202 C  CB  . ILE   AA 178 ? 1.4184 0.6969 1.7596 0.1473  -0.3945 -0.2358 165 ILE   a CB  
47203 C  CG1 . ILE   AA 178 ? 1.4101 0.6163 1.7319 0.1682  -0.3670 -0.2744 165 ILE   a CG1 
47204 C  CG2 . ILE   AA 178 ? 1.4500 0.7347 1.7342 0.1204  -0.4170 -0.2156 165 ILE   a CG2 
47205 C  CD1 . ILE   AA 178 ? 1.3966 0.5807 1.7323 0.1916  -0.3407 -0.2865 165 ILE   a CD1 
47206 N  N   . PRO   AA 179 ? 1.4661 0.7690 1.8528 0.1109  -0.4381 -0.1773 166 PRO   a N   
47207 C  CA  . PRO   AA 179 ? 1.5013 0.7553 1.8931 0.1098  -0.4528 -0.1490 166 PRO   a CA  
47208 C  C   . PRO   AA 179 ? 1.5434 0.7643 1.8627 0.0578  -0.4878 -0.1044 166 PRO   a C   
47209 O  O   . PRO   AA 179 ? 1.5222 0.6950 1.9232 0.0886  -0.5215 -0.0879 166 PRO   a O   
47210 C  CB  . PRO   AA 179 ? 1.5076 0.8215 1.9447 0.0998  -0.4286 -0.1685 166 PRO   a CB  
47211 C  CG  . PRO   AA 179 ? 1.4611 0.8426 1.9270 0.1325  -0.4034 -0.1672 166 PRO   a CG  
47212 C  CD  . PRO   AA 179 ? 1.4544 0.8086 1.8668 0.1181  -0.4191 -0.1766 166 PRO   a CD  
47213 N  N   . LYS   AA 180 ? 1.5816 0.7692 1.8705 -0.0141 -0.4742 -0.0495 167 LYS   a N   
47214 C  CA  . LYS   AA 180 ? 1.6091 0.7554 1.8631 -0.0035 -0.4962 -0.0355 167 LYS   a CA  
47215 C  C   . LYS   AA 180 ? 1.5272 0.6167 1.7999 0.0046  -0.5521 0.0553  167 LYS   a C   
47216 O  O   . LYS   AA 180 ? 1.5309 0.5724 1.7279 0.0432  -0.6069 0.1231  167 LYS   a O   
47217 C  CB  . LYS   AA 180 ? 1.6755 0.8056 1.8684 -0.0421 -0.4210 -0.0358 167 LYS   a CB  
47218 C  CG  . LYS   AA 180 ? 1.7193 0.8557 1.9077 -0.0875 -0.3722 -0.0648 167 LYS   a CG  
47219 C  CD  . LYS   AA 180 ? 1.7021 0.8669 1.8993 -0.1378 -0.3222 -0.0956 167 LYS   a CD  
47220 C  CE  . LYS   AA 180 ? 1.6898 0.8612 1.9352 -0.1819 -0.2981 -0.1138 167 LYS   a CE  
47221 N  NZ  . LYS   AA 180 ? 1.7029 0.8336 1.9493 -0.1997 -0.2882 -0.1524 167 LYS   a NZ  
47222 N  N   . THR   AA 181 ? 1.4986 0.5934 1.8011 0.0302  -0.5469 0.0874  168 THR   a N   
47223 C  CA  . THR   AA 181 ? 1.5118 0.6878 1.7963 0.0302  -0.5461 0.0755  168 THR   a CA  
47224 C  C   . THR   AA 181 ? 1.5497 0.7430 1.7596 0.0601  -0.5660 0.0998  168 THR   a C   
47225 O  O   . THR   AA 181 ? 1.5983 0.7609 1.8353 0.0731  -0.5356 0.0710  168 THR   a O   
47226 C  CB  . THR   AA 181 ? 1.4922 0.7261 1.7928 -0.0328 -0.5430 0.0740  168 THR   a CB  
47227 O  OG1 . THR   AA 181 ? 1.4683 0.8395 1.7842 -0.1146 -0.4816 0.0837  168 THR   a OG1 
47228 C  CG2 . THR   AA 181 ? 1.4841 0.7161 1.7648 -0.0527 -0.5495 0.0845  168 THR   a CG2 
47229 N  N   . THR   AA 182 ? 1.5590 0.7434 1.7531 0.0572  -0.6239 0.0685  169 THR   a N   
47230 C  CA  . THR   AA 182 ? 1.5340 0.7528 1.7243 0.0400  -0.6669 0.0650  169 THR   a CA  
47231 C  C   . THR   AA 182 ? 1.5129 0.7801 1.6979 0.0422  -0.7055 0.0337  169 THR   a C   
47232 O  O   . THR   AA 182 ? 1.4187 0.6539 1.6399 -0.0370 -0.6948 -0.0347 169 THR   a O   
47233 C  CB  . THR   AA 182 ? 1.5790 0.7205 1.7386 0.0514  -0.7022 0.0839  169 THR   a CB  
47234 O  OG1 . THR   AA 182 ? 1.6263 0.7214 1.7070 0.0646  -0.7091 0.0886  169 THR   a OG1 
47235 C  CG2 . THR   AA 182 ? 1.5691 0.7260 1.7696 0.0575  -0.7217 0.0958  169 THR   a CG2 
47236 N  N   . VAL   AA 183 ? 1.4736 0.8397 1.6964 0.0082  -0.7097 0.0470  170 VAL   a N   
47237 C  CA  . VAL   AA 183 ? 1.4947 0.7945 1.6656 0.0208  -0.6699 0.0524  170 VAL   a CA  
47238 C  C   . VAL   AA 183 ? 1.5606 0.7877 1.6477 0.0232  -0.6646 0.0504  170 VAL   a C   
47239 O  O   . VAL   AA 183 ? 1.5520 0.6449 1.6220 -0.0038 -0.6301 -0.0335 170 VAL   a O   
47240 C  CB  . VAL   AA 183 ? 1.5296 0.8048 1.6492 0.0608  -0.6976 0.0831  170 VAL   a CB  
47241 C  CG1 . VAL   AA 183 ? 1.4959 0.8051 1.6813 0.0411  -0.7376 0.0733  170 VAL   a CG1 
47242 C  CG2 . VAL   AA 183 ? 1.5241 0.7939 1.6497 0.0914  -0.6458 0.1187  170 VAL   a CG2 
47243 N  N   . GLN   AA 184 ? 1.5982 0.8156 1.6059 0.0377  -0.6787 0.0620  171 GLN   a N   
47244 C  CA  . GLN   AA 184 ? 1.6994 0.8394 1.6015 0.0514  -0.5983 0.0842  171 GLN   a CA  
47245 C  C   . GLN   AA 184 ? 1.7171 0.7735 1.6087 0.0302  -0.5625 0.0521  171 GLN   a C   
47246 O  O   . GLN   AA 184 ? 1.7802 0.7541 1.5645 0.0131  -0.4545 -0.0143 171 GLN   a O   
47247 C  CB  . GLN   AA 184 ? 1.7165 0.9757 1.6565 0.0326  -0.6228 0.0886  171 GLN   a CB  
47248 C  CG  . GLN   AA 184 ? 1.7935 1.0586 1.6737 0.0266  -0.6122 0.1359  171 GLN   a CG  
47249 C  CD  . GLN   AA 184 ? 1.7697 1.0992 1.7078 0.0333  -0.5907 0.1286  171 GLN   a CD  
47250 O  OE1 . GLN   AA 184 ? 1.7542 1.2311 1.7298 0.0155  -0.5786 0.1098  171 GLN   a OE1 
47251 N  NE2 . GLN   AA 184 ? 1.8029 1.1363 1.7218 -0.0096 -0.6040 0.1558  171 GLN   a NE2 
47252 N  N   . VAL   AA 185 ? 1.7179 0.6738 1.6397 0.0093  -0.5759 0.0778  172 VAL   a N   
47253 C  CA  . VAL   AA 185 ? 1.6576 0.6292 1.6233 -0.0391 -0.5770 0.0542  172 VAL   a CA  
47254 C  C   . VAL   AA 185 ? 1.7109 0.5707 1.5941 -0.0297 -0.6138 0.0748  172 VAL   a C   
47255 O  O   . VAL   AA 185 ? 1.6619 0.5987 1.5894 -0.0437 -0.6388 0.1071  172 VAL   a O   
47256 C  CB  . VAL   AA 185 ? 1.6531 0.5612 1.6354 -0.0657 -0.5730 0.0852  172 VAL   a CB  
47257 C  CG1 . VAL   AA 185 ? 1.6057 0.6486 1.5926 -0.0843 -0.5273 0.1162  172 VAL   a CG1 
47258 C  CG2 . VAL   AA 185 ? 1.6301 0.5321 1.6536 -0.0681 -0.5717 0.1076  172 VAL   a CG2 
47259 N  N   . ALA   AA 186 ? 1.6573 0.5622 1.5877 0.0231  -0.6418 0.0688  173 ALA   a N   
47260 C  CA  . ALA   AA 186 ? 1.6420 0.4959 1.5595 0.0186  -0.6043 0.0179  173 ALA   a CA  
47261 C  C   . ALA   AA 186 ? 1.6703 0.4882 1.5422 -0.0135 -0.5838 0.0084  173 ALA   a C   
47262 O  O   . ALA   AA 186 ? 1.6791 0.5231 1.5634 0.0053  -0.5745 0.0117  173 ALA   a O   
47263 C  CB  . ALA   AA 186 ? 1.6227 0.5323 1.5548 0.0416  -0.5862 -0.0085 173 ALA   a CB  
47264 N  N   . GLU   AA 187 ? 1.6557 0.5442 1.5178 -0.0013 -0.6114 0.0139  174 GLU   a N   
47265 C  CA  . GLU   AA 187 ? 1.6979 0.6398 1.4826 0.0047  -0.5864 0.0203  174 GLU   a CA  
47266 C  C   . GLU   AA 187 ? 1.7082 0.6530 1.4871 0.0329  -0.5659 0.0315  174 GLU   a C   
47267 O  O   . GLU   AA 187 ? 1.6809 0.7014 1.5446 -0.0169 -0.5048 0.0158  174 GLU   a O   
47268 C  CB  . GLU   AA 187 ? 1.7478 0.7010 1.4339 0.0096  -0.5784 0.0119  174 GLU   a CB  
47269 C  CG  . GLU   AA 187 ? 1.7709 0.7399 1.4131 0.0227  -0.5549 -0.0159 174 GLU   a CG  
47270 C  CD  . GLU   AA 187 ? 1.8387 0.7102 1.4416 0.0105  -0.5600 -0.0096 174 GLU   a CD  
47271 O  OE1 . GLU   AA 187 ? 1.8842 0.5738 1.4849 -0.0262 -0.5286 -0.0266 174 GLU   a OE1 
47272 O  OE2 . GLU   AA 187 ? 1.8566 0.7301 1.4527 0.0047  -0.6132 -0.0081 174 GLU   a OE2 
47273 N  N   . GLU   AA 188 ? 1.6856 0.7792 1.5144 0.0101  -0.5997 0.0580  175 GLU   a N   
47274 C  CA  . GLU   AA 188 ? 1.7174 0.7592 1.5689 0.0234  -0.5579 0.0954  175 GLU   a CA  
47275 C  C   . GLU   AA 188 ? 1.7057 0.6853 1.6173 0.0390  -0.4861 0.1519  175 GLU   a C   
47276 O  O   . GLU   AA 188 ? 1.7118 0.7197 1.6219 0.0617  -0.4357 0.2307  175 GLU   a O   
47277 C  CB  . GLU   AA 188 ? 1.7376 0.8461 1.6374 -0.0157 -0.5609 0.0656  175 GLU   a CB  
47278 C  CG  . GLU   AA 188 ? 1.8209 0.8957 1.6806 -0.0455 -0.5346 0.0190  175 GLU   a CG  
47279 C  CD  . GLU   AA 188 ? 1.8163 1.0061 1.8040 -0.0898 -0.5305 0.0003  175 GLU   a CD  
47280 O  OE1 . GLU   AA 188 ? 1.8417 0.9433 1.7854 -0.0523 -0.5054 -0.0898 175 GLU   a OE1 
47281 O  OE2 . GLU   AA 188 ? 1.8486 0.9750 1.9988 -0.0532 -0.4779 0.0766  175 GLU   a OE2 
47282 N  N   . ALA   AA 189 ? 1.6544 0.6051 1.6436 0.0610  -0.4635 0.1683  176 ALA   a N   
47283 C  CA  . ALA   AA 189 ? 1.5750 0.7032 1.6257 0.0733  -0.4753 0.1550  176 ALA   a CA  
47284 C  C   . ALA   AA 189 ? 1.5842 0.6742 1.5958 0.0421  -0.4487 0.1282  176 ALA   a C   
47285 O  O   . ALA   AA 189 ? 1.4854 0.8955 1.6418 0.1126  -0.4463 0.1384  176 ALA   a O   
47286 C  CB  . ALA   AA 189 ? 1.5450 0.6630 1.6754 0.0856  -0.4631 0.1368  176 ALA   a CB  
47287 N  N   . ILE   AA 190 ? 1.5200 0.6459 1.4797 0.1019  -0.4850 0.1354  177 ILE   a N   
47288 C  CA  . ILE   AA 190 ? 1.5221 0.5818 1.4167 0.1034  -0.4578 0.1315  177 ILE   a CA  
47289 C  C   . ILE   AA 190 ? 1.5715 0.6615 1.3498 0.0980  -0.4816 0.0830  177 ILE   a C   
47290 O  O   . ILE   AA 190 ? 1.5411 0.7374 1.3915 0.1210  -0.4675 0.0161  177 ILE   a O   
47291 C  CB  . ILE   AA 190 ? 1.5276 0.5792 1.4073 0.0817  -0.4383 0.1602  177 ILE   a CB  
47292 C  CG1 . ILE   AA 190 ? 1.5309 0.5299 1.3865 0.0704  -0.4285 0.1889  177 ILE   a CG1 
47293 C  CG2 . ILE   AA 190 ? 1.5335 0.5334 1.4166 0.0837  -0.4175 0.1608  177 ILE   a CG2 
47294 C  CD1 . ILE   AA 190 ? 1.5298 0.5275 1.3540 0.0777  -0.3937 0.2040  177 ILE   a CD1 
47295 N  N   . VAL   AA 191 ? 1.5702 0.7112 1.3648 0.1196  -0.5113 0.0900  178 VAL   a N   
47296 C  CA  . VAL   AA 191 ? 1.5807 0.7458 1.3510 0.0913  -0.5016 0.0990  178 VAL   a CA  
47297 C  C   . VAL   AA 191 ? 1.5927 0.7301 1.3723 0.0649  -0.4961 0.0704  178 VAL   a C   
47298 O  O   . VAL   AA 191 ? 1.6247 0.5888 1.3490 0.0530  -0.4810 0.0371  178 VAL   a O   
47299 C  CB  . VAL   AA 191 ? 1.5840 0.7685 1.3248 0.0566  -0.5092 0.0704  178 VAL   a CB  
47300 C  CG1 . VAL   AA 191 ? 1.5695 0.8325 1.2448 0.0201  -0.5581 0.0418  178 VAL   a CG1 
47301 C  CG2 . VAL   AA 191 ? 1.5993 0.7789 1.3183 0.0706  -0.5074 0.1260  178 VAL   a CG2 
47302 N  N   . ASN   AA 192 ? 1.6209 0.6788 1.3800 0.0420  -0.5093 0.0384  179 ASN   a N   
47303 C  CA  . ASN   AA 192 ? 1.6427 0.6728 1.3666 0.0634  -0.4948 0.0117  179 ASN   a CA  
47304 C  C   . ASN   AA 192 ? 1.6482 0.6040 1.3546 0.1223  -0.4744 0.0073  179 ASN   a C   
47305 O  O   . ASN   AA 192 ? 1.6921 0.6111 1.3540 0.1321  -0.4303 -0.0320 179 ASN   a O   
47306 C  CB  . ASN   AA 192 ? 1.6660 0.6853 1.3909 0.0301  -0.4940 0.0266  179 ASN   a CB  
47307 C  CG  . ASN   AA 192 ? 1.6486 0.6861 1.4000 0.0030  -0.4614 0.0384  179 ASN   a CG  
47308 O  OD1 . ASN   AA 192 ? 1.6278 0.7746 1.4424 -0.0361 -0.4222 0.0751  179 ASN   a OD1 
47309 N  ND2 . ASN   AA 192 ? 1.6674 0.7370 1.3752 0.0037  -0.4721 0.0178  179 ASN   a ND2 
47310 N  N   . ALA   AA 193 ? 1.6267 0.5510 1.3383 0.1448  -0.4894 0.0348  180 ALA   a N   
47311 C  CA  . ALA   AA 193 ? 1.6048 0.5090 1.2994 0.1381  -0.4646 0.0172  180 ALA   a CA  
47312 C  C   . ALA   AA 193 ? 1.6222 0.4937 1.2895 0.1306  -0.4437 0.0243  180 ALA   a C   
47313 O  O   . ALA   AA 193 ? 1.6126 0.4944 1.3835 0.1615  -0.4076 0.0310  180 ALA   a O   
47314 C  CB  . ALA   AA 193 ? 1.5784 0.5283 1.2649 0.1261  -0.4805 0.0160  180 ALA   a CB  
47315 N  N   . MET   AA 194 ? 1.6411 0.5107 1.2744 0.1407  -0.4511 0.0323  181 MET   a N   
47316 C  CA  . MET   AA 194 ? 1.6884 0.5664 1.2627 0.1200  -0.4089 0.0252  181 MET   a CA  
47317 C  C   . MET   AA 194 ? 1.7577 0.5757 1.1941 0.1405  -0.3942 0.0522  181 MET   a C   
47318 O  O   . MET   AA 194 ? 1.7882 0.5919 1.0626 0.2028  -0.4170 0.1330  181 MET   a O   
47319 C  CB  . MET   AA 194 ? 1.7119 0.5785 1.3254 0.0970  -0.3977 0.0554  181 MET   a CB  
47320 C  CG  . MET   AA 194 ? 1.7096 0.5607 1.4196 0.0971  -0.3489 0.0617  181 MET   a CG  
47321 S  SD  . MET   AA 194 ? 1.7541 0.4870 1.3707 0.1013  -0.3125 0.0428  181 MET   a SD  
47322 C  CE  . MET   AA 194 ? 1.8043 0.6036 1.4530 0.0400  -0.2650 0.0990  181 MET   a CE  
47323 N  N   . ARG   AA 195 ? 1.7526 0.6316 1.2514 0.0971  -0.3895 0.0397  182 ARG   a N   
47324 C  CA  . ARG   AA 195 ? 1.7644 0.6317 1.2661 0.0755  -0.3972 0.0180  182 ARG   a CA  
47325 C  C   . ARG   AA 195 ? 1.7326 0.6037 1.2444 0.1064  -0.3972 -0.0225 182 ARG   a C   
47326 O  O   . ARG   AA 195 ? 1.7652 0.6367 1.2750 0.1472  -0.3796 -0.0065 182 ARG   a O   
47327 C  CB  . ARG   AA 195 ? 1.7624 0.6831 1.3080 0.0313  -0.4044 0.0317  182 ARG   a CB  
47328 C  CG  . ARG   AA 195 ? 1.7707 0.7211 1.3166 0.0152  -0.3917 -0.0147 182 ARG   a CG  
47329 C  CD  . ARG   AA 195 ? 1.7853 0.7953 1.3400 0.0046  -0.4167 -0.0022 182 ARG   a CD  
47330 N  NE  . ARG   AA 195 ? 1.7794 0.8238 1.3955 -0.0117 -0.4200 0.0217  182 ARG   a NE  
47331 C  CZ  . ARG   AA 195 ? 1.7851 0.7419 1.4629 -0.0478 -0.4036 0.0517  182 ARG   a CZ  
47332 N  NH1 . ARG   AA 195 ? 1.7910 0.7796 1.5074 -0.0496 -0.3896 0.0862  182 ARG   a NH1 
47333 N  NH2 . ARG   AA 195 ? 1.8254 0.7401 1.4987 -0.1230 -0.3776 0.0227  182 ARG   a NH2 
47334 N  N   . VAL   AA 196 ? 1.6762 0.5730 1.1922 0.1151  -0.4387 -0.0577 183 VAL   a N   
47335 C  CA  . VAL   AA 196 ? 1.6229 0.6131 1.1828 0.1468  -0.4467 -0.0528 183 VAL   a CA  
47336 C  C   . VAL   AA 196 ? 1.6241 0.6083 1.2133 0.1409  -0.4586 -0.0382 183 VAL   a C   
47337 O  O   . VAL   AA 196 ? 1.5332 0.7041 1.2899 0.1552  -0.4811 -0.0529 183 VAL   a O   
47338 C  CB  . VAL   AA 196 ? 1.5883 0.6500 1.1790 0.1464  -0.4566 -0.0776 183 VAL   a CB  
47339 C  CG1 . VAL   AA 196 ? 1.5806 0.7270 1.1698 0.1544  -0.4170 -0.0433 183 VAL   a CG1 
47340 C  CG2 . VAL   AA 196 ? 1.5914 0.6627 1.1672 0.1341  -0.4508 -0.0964 183 VAL   a CG2 
47341 N  N   . LEU   AA 197 ? 1.6095 0.5538 1.2052 0.2211  -0.4654 0.0028  184 LEU   a N   
47342 C  CA  . LEU   AA 197 ? 1.6214 0.5599 1.1823 0.2266  -0.4603 0.0036  184 LEU   a CA  
47343 C  C   . LEU   AA 197 ? 1.6665 0.5032 1.2059 0.2038  -0.4181 0.0080  184 LEU   a C   
47344 O  O   . LEU   AA 197 ? 1.6455 0.3939 1.2549 0.1939  -0.4163 -0.0370 184 LEU   a O   
47345 C  CB  . LEU   AA 197 ? 1.6688 0.5629 1.1827 0.2898  -0.4665 0.0172  184 LEU   a CB  
47346 C  CG  . LEU   AA 197 ? 1.7062 0.5448 1.1845 0.3080  -0.4615 0.0144  184 LEU   a CG  
47347 C  CD1 . LEU   AA 197 ? 1.7471 0.5556 1.1360 0.3278  -0.4744 -0.0079 184 LEU   a CD1 
47348 C  CD2 . LEU   AA 197 ? 1.7268 0.5866 1.1680 0.2863  -0.4455 0.0218  184 LEU   a CD2 
47349 N  N   . TYR   AA 198 ? 1.6520 0.5816 1.2055 0.1660  -0.4200 0.0128  185 TYR   a N   
47350 C  CA  . TYR   AA 198 ? 1.6608 0.6505 1.2125 0.1436  -0.4084 0.0024  185 TYR   a CA  
47351 C  C   . TYR   AA 198 ? 1.6114 0.6490 1.1809 0.1481  -0.4456 0.0262  185 TYR   a C   
47352 O  O   . TYR   AA 198 ? 1.6221 0.6709 1.1508 0.2122  -0.4749 0.0825  185 TYR   a O   
47353 C  CB  . TYR   AA 198 ? 1.6548 0.7541 1.1978 0.1225  -0.4219 -0.0052 185 TYR   a CB  
47354 C  CG  . TYR   AA 198 ? 1.6788 0.8412 1.2412 0.1325  -0.3946 -0.0353 185 TYR   a CG  
47355 C  CD1 . TYR   AA 198 ? 1.6387 0.9286 1.2765 0.1457  -0.3687 -0.0555 185 TYR   a CD1 
47356 C  CD2 . TYR   AA 198 ? 1.6755 0.8632 1.2471 0.1464  -0.4021 -0.0457 185 TYR   a CD2 
47357 C  CE1 . TYR   AA 198 ? 1.6154 0.9504 1.2858 0.1796  -0.3819 -0.0928 185 TYR   a CE1 
47358 C  CE2 . TYR   AA 198 ? 1.6629 0.9332 1.2808 0.1891  -0.3993 -0.0489 185 TYR   a CE2 
47359 C  CZ  . TYR   AA 198 ? 1.6186 0.9592 1.2600 0.2204  -0.3735 -0.0838 185 TYR   a CZ  
47360 O  OH  . TYR   AA 198 ? 1.5854 1.0367 1.2631 0.2438  -0.3876 -0.0612 185 TYR   a OH  
47361 N  N   . TYR   AA 199 ? 1.6177 0.6363 1.2171 0.1396  -0.4717 0.0169  186 TYR   a N   
47362 C  CA  . TYR   AA 199 ? 1.6106 0.6301 1.2560 0.1316  -0.4741 0.0078  186 TYR   a CA  
47363 C  C   . TYR   AA 199 ? 1.5674 0.5489 1.2948 0.1055  -0.4728 0.0434  186 TYR   a C   
47364 O  O   . TYR   AA 199 ? 1.5169 0.5027 1.3333 0.0692  -0.4964 0.0765  186 TYR   a O   
47365 C  CB  . TYR   AA 199 ? 1.5987 0.5802 1.2528 0.1555  -0.4771 -0.0426 186 TYR   a CB  
47366 C  CG  . TYR   AA 199 ? 1.6111 0.5484 1.2142 0.2007  -0.4600 -0.0880 186 TYR   a CG  
47367 C  CD1 . TYR   AA 199 ? 1.6235 0.5269 1.1854 0.2244  -0.4838 -0.0929 186 TYR   a CD1 
47368 C  CD2 . TYR   AA 199 ? 1.6061 0.5520 1.2136 0.2424  -0.4884 -0.1063 186 TYR   a CD2 
47369 C  CE1 . TYR   AA 199 ? 1.6576 0.5457 1.1474 0.2585  -0.4735 -0.0712 186 TYR   a CE1 
47370 C  CE2 . TYR   AA 199 ? 1.6388 0.5798 1.1831 0.2529  -0.4809 -0.1034 186 TYR   a CE2 
47371 C  CZ  . TYR   AA 199 ? 1.6613 0.5781 1.1817 0.2580  -0.4691 -0.0780 186 TYR   a CZ  
47372 O  OH  . TYR   AA 199 ? 1.6851 0.5972 1.1627 0.2350  -0.4626 -0.1070 186 TYR   a OH  
47373 N  N   . ARG   AA 200 ? 1.5625 0.5238 1.2954 0.1076  -0.4606 0.0489  187 ARG   a N   
47374 C  CA  . ARG   AA 200 ? 1.5931 0.5650 1.2670 0.0940  -0.4339 0.0399  187 ARG   a CA  
47375 C  C   . ARG   AA 200 ? 1.6010 0.6071 1.3048 0.0739  -0.4232 0.0110  187 ARG   a C   
47376 O  O   . ARG   AA 200 ? 1.5459 0.6910 1.3177 0.0693  -0.4203 0.0230  187 ARG   a O   
47377 C  CB  . ARG   AA 200 ? 1.5993 0.5729 1.2774 0.0969  -0.4195 0.0191  187 ARG   a CB  
47378 C  CG  . ARG   AA 200 ? 1.6283 0.5840 1.3302 0.0438  -0.3968 -0.0091 187 ARG   a CG  
47379 C  CD  . ARG   AA 200 ? 1.6470 0.5675 1.3187 0.0485  -0.4170 0.0071  187 ARG   a CD  
47380 N  NE  . ARG   AA 200 ? 1.6694 0.5045 1.3304 0.0080  -0.4082 -0.0026 187 ARG   a NE  
47381 C  CZ  . ARG   AA 200 ? 1.6332 0.4449 1.3197 0.0263  -0.4121 0.0521  187 ARG   a CZ  
47382 N  NH1 . ARG   AA 200 ? 1.6510 0.3896 1.2905 0.0158  -0.4172 0.0709  187 ARG   a NH1 
47383 N  NH2 . ARG   AA 200 ? 1.6351 0.4294 1.3903 0.0414  -0.3901 0.0186  187 ARG   a NH2 
47384 N  N   . ASP   AA 201 ? 1.6293 0.6064 1.2430 0.1018  -0.4661 0.0147  188 ASP   a N   
47385 C  CA  . ASP   AA 201 ? 1.6426 0.6410 1.2027 0.1189  -0.4565 -0.0420 188 ASP   a CA  
47386 C  C   . ASP   AA 201 ? 1.6195 0.6191 1.1694 0.1231  -0.4768 -0.0897 188 ASP   a C   
47387 O  O   . ASP   AA 201 ? 1.7015 0.7190 1.1373 0.1039  -0.4074 -0.1146 188 ASP   a O   
47388 C  CB  . ASP   AA 201 ? 1.6642 0.6594 1.2208 0.1496  -0.4555 -0.0274 188 ASP   a CB  
47389 C  CG  . ASP   AA 201 ? 1.6398 0.6906 1.2005 0.1388  -0.4550 -0.0089 188 ASP   a CG  
47390 O  OD1 . ASP   AA 201 ? 1.7107 0.7400 1.2050 0.2510  -0.4215 0.0908  188 ASP   a OD1 
47391 O  OD2 . ASP   AA 201 ? 1.7886 0.5797 1.0922 -0.0722 -0.3992 -0.1583 188 ASP   a OD2 
47392 N  N   . ALA   AA 202 ? 1.6019 0.5308 1.1842 0.1287  -0.4667 -0.1172 189 ALA   a N   
47393 C  CA  . ALA   AA 202 ? 1.6287 0.5745 1.2192 0.1368  -0.4341 -0.1022 189 ALA   a CA  
47394 C  C   . ALA   AA 202 ? 1.6084 0.5648 1.2104 0.1847  -0.3889 -0.0184 189 ALA   a C   
47395 O  O   . ALA   AA 202 ? 1.6601 0.4609 1.1098 0.2878  -0.3669 0.0217  189 ALA   a O   
47396 C  CB  . ALA   AA 202 ? 1.6060 0.6179 1.2727 0.1363  -0.4607 -0.1066 189 ALA   a CB  
47397 N  N   . ARG   AA 203 ? 1.6221 0.5346 1.3150 0.1829  -0.3654 -0.0037 190 ARG   a N   
47398 C  CA  . ARG   AA 203 ? 1.6231 0.5153 1.3620 0.1676  -0.3815 -0.1025 190 ARG   a CA  
47399 C  C   . ARG   AA 203 ? 1.6034 0.5089 1.3070 0.1403  -0.3906 -0.1144 190 ARG   a C   
47400 O  O   . ARG   AA 203 ? 1.6292 0.4914 1.2835 0.1829  -0.3806 -0.0664 190 ARG   a O   
47401 C  CB  . ARG   AA 203 ? 1.6046 0.4908 1.3953 0.2095  -0.4092 -0.1278 190 ARG   a CB  
47402 C  CG  . ARG   AA 203 ? 1.6277 0.5773 1.4765 0.2425  -0.4402 -0.1111 190 ARG   a CG  
47403 C  CD  . ARG   AA 203 ? 1.5905 0.6604 1.5104 0.2103  -0.4676 -0.0544 190 ARG   a CD  
47404 N  NE  . ARG   AA 203 ? 1.5372 0.8990 1.6290 0.2176  -0.4720 -0.1999 190 ARG   a NE  
47405 C  CZ  . ARG   AA 203 ? 1.5017 0.9055 1.6464 0.2413  -0.5445 -0.2159 190 ARG   a CZ  
47406 N  NH1 . ARG   AA 203 ? 1.4760 1.0002 1.6615 0.2343  -0.5626 -0.2492 190 ARG   a NH1 
47407 N  NH2 . ARG   AA 203 ? 1.5411 0.7645 1.6604 0.3054  -0.5522 -0.1824 190 ARG   a NH2 
47408 N  N   . SER   AA 204 ? 1.6613 0.5581 1.2574 0.0982  -0.3607 -0.1417 191 SER   a N   
47409 C  CA  . SER   AA 204 ? 1.7119 0.5173 1.2163 0.0745  -0.3783 -0.1366 191 SER   a CA  
47410 C  C   . SER   AA 204 ? 1.8023 0.4888 1.1892 0.0501  -0.4191 -0.1435 191 SER   a C   
47411 O  O   . SER   AA 204 ? 1.8619 0.5289 1.1998 0.1011  -0.4567 -0.1648 191 SER   a O   
47412 C  CB  . SER   AA 204 ? 1.7158 0.6145 1.2061 0.0528  -0.3505 -0.1420 191 SER   a CB  
47413 O  OG  . SER   AA 204 ? 1.6709 0.6615 1.1688 0.0891  -0.3208 -0.1989 191 SER   a OG  
47414 N  N   . SER   AA 205 ? 1.8441 0.4835 1.2026 0.0100  -0.4533 -0.1360 192 SER   a N   
47415 C  CA  . SER   AA 205 ? 1.8457 0.5496 1.1944 -0.0177 -0.4532 -0.1779 192 SER   a CA  
47416 C  C   . SER   AA 205 ? 1.8853 0.4574 1.1246 -0.0736 -0.4832 -0.1907 192 SER   a C   
47417 O  O   . SER   AA 205 ? 1.7990 0.3403 1.0397 -0.0729 -0.5813 -0.2199 192 SER   a O   
47418 C  CB  . SER   AA 205 ? 1.8041 0.5691 1.2344 0.0178  -0.4050 -0.1298 192 SER   a CB  
47419 O  OG  . SER   AA 205 ? 1.8313 0.6064 1.2800 0.0647  -0.4277 -0.1260 192 SER   a OG  
47420 N  N   . ARG   AA 206 ? 1.8961 0.5609 1.1070 -0.0777 -0.4420 -0.1334 193 ARG   a N   
47421 C  CA  . ARG   AA 206 ? 1.8410 0.6798 1.2047 -0.0565 -0.4274 -0.1064 193 ARG   a CA  
47422 C  C   . ARG   AA 206 ? 1.8098 0.6977 1.2245 -0.0152 -0.3650 -0.1223 193 ARG   a C   
47423 O  O   . ARG   AA 206 ? 1.8030 0.5449 1.2243 0.0253  -0.3732 -0.1142 193 ARG   a O   
47424 C  CB  . ARG   AA 206 ? 1.9245 0.8005 1.2065 -0.0945 -0.4098 -0.1434 193 ARG   a CB  
47425 C  CG  . ARG   AA 206 ? 1.9525 0.8930 1.1644 -0.0858 -0.4387 -0.1442 193 ARG   a CG  
47426 C  CD  . ARG   AA 206 ? 1.9919 1.0262 1.1166 -0.0598 -0.3837 -0.1141 193 ARG   a CD  
47427 N  NE  . ARG   AA 206 ? 2.0073 1.1416 1.0468 -0.0493 -0.4009 -0.0981 193 ARG   a NE  
47428 C  CZ  . ARG   AA 206 ? 2.0145 1.3255 0.9524 -0.0814 -0.4368 -0.1007 193 ARG   a CZ  
47429 N  NH1 . ARG   AA 206 ? 2.0220 1.4246 0.9525 -0.0852 -0.4040 -0.0778 193 ARG   a NH1 
47430 N  NH2 . ARG   AA 206 ? 1.9900 1.4500 1.0375 -0.0778 -0.4643 -0.0480 193 ARG   a NH2 
47431 N  N   . ASN   AA 207 ? 1.8263 0.6691 1.1456 0.0032  -0.3392 -0.0575 194 ASN   a N   
47432 C  CA  . ASN   AA 207 ? 1.8271 0.7309 1.0803 0.0166  -0.3823 0.0584  194 ASN   a CA  
47433 C  C   . ASN   AA 207 ? 1.7745 0.6542 1.0775 0.0037  -0.3706 0.0896  194 ASN   a C   
47434 O  O   . ASN   AA 207 ? 1.8167 0.7296 1.1011 -0.0325 -0.3923 0.1181  194 ASN   a O   
47435 C  CB  . ASN   AA 207 ? 1.8211 0.8530 1.0813 0.0153  -0.3573 0.0753  194 ASN   a CB  
47436 C  CG  . ASN   AA 207 ? 1.8732 0.9294 1.1056 0.0730  -0.3137 0.0748  194 ASN   a CG  
47437 O  OD1 . ASN   AA 207 ? 1.9108 0.7922 1.0486 0.1234  -0.4199 0.2116  194 ASN   a OD1 
47438 N  ND2 . ASN   AA 207 ? 1.9105 1.1044 1.1471 0.0482  -0.3510 0.0836  194 ASN   a ND2 
47439 N  N   . PHE   AA 208 ? 1.7424 0.6465 1.0246 -0.0156 -0.4240 0.0964  195 PHE   a N   
47440 C  CA  . PHE   AA 208 ? 1.6904 0.6724 1.0791 0.0000  -0.4034 0.0791  195 PHE   a CA  
47441 C  C   . PHE   AA 208 ? 1.6905 0.6718 1.1053 0.0118  -0.3909 0.0607  195 PHE   a C   
47442 O  O   . PHE   AA 208 ? 1.6849 0.7207 1.1196 0.0032  -0.4382 0.0139  195 PHE   a O   
47443 C  CB  . PHE   AA 208 ? 1.6420 0.6017 1.1038 0.0017  -0.4407 0.0602  195 PHE   a CB  
47444 C  CG  . PHE   AA 208 ? 1.6756 0.5588 1.0796 0.0235  -0.4794 0.0378  195 PHE   a CG  
47445 C  CD1 . PHE   AA 208 ? 1.6843 0.5907 1.0752 0.0079  -0.5081 0.0220  195 PHE   a CD1 
47446 C  CD2 . PHE   AA 208 ? 1.6460 0.5337 1.0804 0.0179  -0.5200 0.0370  195 PHE   a CD2 
47447 C  CE1 . PHE   AA 208 ? 1.6835 0.5940 1.1299 0.0036  -0.5094 -0.0052 195 PHE   a CE1 
47448 C  CE2 . PHE   AA 208 ? 1.6435 0.5124 1.1132 0.0258  -0.5228 0.0252  195 PHE   a CE2 
47449 C  CZ  . PHE   AA 208 ? 1.6859 0.5266 1.1502 0.0091  -0.5259 0.0008  195 PHE   a CZ  
47450 N  N   . SER   AA 209 ? 1.7053 0.6434 1.1814 -0.0110 -0.3479 0.0337  196 SER   a N   
47451 C  CA  . SER   AA 209 ? 1.7201 0.6634 1.2415 -0.0004 -0.3659 0.0274  196 SER   a CA  
47452 C  C   . SER   AA 209 ? 1.6890 0.6134 1.2648 -0.0289 -0.3851 -0.0183 196 SER   a C   
47453 O  O   . SER   AA 209 ? 1.7450 0.4379 1.2765 -0.0726 -0.3631 -0.0682 196 SER   a O   
47454 C  CB  . SER   AA 209 ? 1.7050 0.6874 1.2857 -0.0376 -0.3376 0.0458  196 SER   a CB  
47455 O  OG  . SER   AA 209 ? 1.6904 0.7038 1.3165 -0.0416 -0.3439 0.0798  196 SER   a OG  
47456 N  N   . LEU   AA 210 ? 1.6733 0.6672 1.2832 -0.0343 -0.4042 -0.0318 197 LEU   a N   
47457 C  CA  . LEU   AA 210 ? 1.6675 0.7179 1.2956 -0.0673 -0.4101 -0.0427 197 LEU   a CA  
47458 C  C   . LEU   AA 210 ? 1.6924 0.7233 1.3017 -0.0659 -0.4343 -0.0403 197 LEU   a C   
47459 O  O   . LEU   AA 210 ? 1.7545 0.7057 1.3788 -0.1071 -0.4082 0.0076  197 LEU   a O   
47460 C  CB  . LEU   AA 210 ? 1.6806 0.6623 1.3044 -0.0533 -0.3987 -0.0421 197 LEU   a CB  
47461 C  CG  . LEU   AA 210 ? 1.6725 0.6958 1.3188 -0.0362 -0.3994 -0.0242 197 LEU   a CG  
47462 C  CD1 . LEU   AA 210 ? 1.6867 0.7009 1.3317 -0.0406 -0.3869 -0.0242 197 LEU   a CD1 
47463 C  CD2 . LEU   AA 210 ? 1.6665 0.7389 1.3110 -0.0455 -0.4330 -0.0118 197 LEU   a CD2 
47464 N  N   . ALA   AA 211 ? 1.6705 0.7435 1.2882 -0.0799 -0.4733 -0.0791 198 ALA   a N   
47465 C  CA  . ALA   AA 211 ? 1.6441 0.7618 1.3186 -0.0658 -0.5176 -0.0706 198 ALA   a CA  
47466 C  C   . ALA   AA 211 ? 1.6042 0.7450 1.3543 -0.0540 -0.5530 -0.0733 198 ALA   a C   
47467 O  O   . ALA   AA 211 ? 1.4880 0.5898 1.4141 -0.1038 -0.5303 -0.1209 198 ALA   a O   
47468 C  CB  . ALA   AA 211 ? 1.6723 0.8275 1.3299 -0.0939 -0.5177 -0.0930 198 ALA   a CB  
47469 N  N   . ILE   AA 212 ? 1.6556 0.7923 1.3580 -0.0162 -0.5568 -0.0473 199 ILE   a N   
47470 C  CA  . ILE   AA 212 ? 1.6625 0.8209 1.3814 0.0450  -0.5611 -0.0272 199 ILE   a CA  
47471 C  C   . ILE   AA 212 ? 1.7023 0.8002 1.4266 0.0461  -0.5560 0.0040  199 ILE   a C   
47472 O  O   . ILE   AA 212 ? 1.7978 0.9253 1.4586 0.0000  -0.5336 0.0678  199 ILE   a O   
47473 C  CB  . ILE   AA 212 ? 1.6984 0.8289 1.3815 0.1147  -0.6009 -0.0254 199 ILE   a CB  
47474 C  CG1 . ILE   AA 212 ? 1.7436 0.8274 1.3397 0.1182  -0.6143 -0.0269 199 ILE   a CG1 
47475 C  CG2 . ILE   AA 212 ? 1.6926 0.8778 1.4079 0.1445  -0.6076 -0.0052 199 ILE   a CG2 
47476 C  CD1 . ILE   AA 212 ? 1.7756 0.8231 1.3564 0.1519  -0.6576 -0.0221 199 ILE   a CD1 
47477 N  N   . ILE   AA 213 ? 1.6704 0.8594 1.4537 0.0668  -0.5333 0.0058  200 ILE   a N   
47478 C  CA  . ILE   AA 213 ? 1.6414 0.9016 1.5159 0.1007  -0.5512 -0.0271 200 ILE   a CA  
47479 C  C   . ILE   AA 213 ? 1.6396 0.9320 1.5823 0.1030  -0.5568 -0.0483 200 ILE   a C   
47480 O  O   . ILE   AA 213 ? 1.6626 1.0462 1.5334 0.1390  -0.5844 -0.0143 200 ILE   a O   
47481 C  CB  . ILE   AA 213 ? 1.5810 0.8679 1.5427 0.1047  -0.5484 -0.0417 200 ILE   a CB  
47482 C  CG1 . ILE   AA 213 ? 1.5787 0.8475 1.5354 0.1196  -0.5526 -0.0515 200 ILE   a CG1 
47483 C  CG2 . ILE   AA 213 ? 1.5739 0.8451 1.5408 0.1255  -0.5917 0.0008  200 ILE   a CG2 
47484 C  CD1 . ILE   AA 213 ? 1.5414 0.8291 1.5399 0.1171  -0.5300 -0.0606 200 ILE   a CD1 
47485 N  N   . ASP   AA 214 ? 1.6763 0.8695 1.6168 0.1091  -0.6035 -0.0943 201 ASP   a N   
47486 C  CA  . ASP   AA 214 ? 1.6853 0.8918 1.6982 0.0868  -0.6252 -0.1416 201 ASP   a CA  
47487 C  C   . ASP   AA 214 ? 1.6809 0.8817 1.6968 0.0571  -0.6229 -0.1628 201 ASP   a C   
47488 O  O   . ASP   AA 214 ? 1.7131 0.9720 1.6229 0.0103  -0.6271 -0.1337 201 ASP   a O   
47489 C  CB  . ASP   AA 214 ? 1.8140 0.9430 1.7054 0.1411  -0.6696 -0.1518 201 ASP   a CB  
47490 C  CG  . ASP   AA 214 ? 1.8124 1.0332 1.8005 0.1669  -0.6776 -0.1654 201 ASP   a CG  
47491 O  OD1 . ASP   AA 214 ? 1.9234 1.0312 1.8864 0.2154  -0.6597 -0.1627 201 ASP   a OD1 
47492 O  OD2 . ASP   AA 214 ? 1.8883 1.0262 1.8624 0.1799  -0.6774 -0.1861 201 ASP   a OD2 
47493 N  N   . LYS   AA 215 ? 1.6628 0.7433 1.7040 0.0493  -0.6233 -0.1792 202 LYS   a N   
47494 C  CA  . LYS   AA 215 ? 1.6153 0.7759 1.6880 0.0851  -0.5973 -0.1515 202 LYS   a CA  
47495 C  C   . LYS   AA 215 ? 1.6277 0.7762 1.7417 0.0896  -0.6124 -0.1223 202 LYS   a C   
47496 O  O   . LYS   AA 215 ? 1.6510 0.7539 1.7247 0.1336  -0.6187 0.0115  202 LYS   a O   
47497 C  CB  . LYS   AA 215 ? 1.5880 0.7495 1.6833 0.1070  -0.6033 -0.1432 202 LYS   a CB  
47498 C  CG  . LYS   AA 215 ? 1.5601 0.7688 1.6758 0.1277  -0.6066 -0.1183 202 LYS   a CG  
47499 C  CD  . LYS   AA 215 ? 1.6028 0.8379 1.6892 0.1715  -0.5783 -0.0790 202 LYS   a CD  
47500 C  CE  . LYS   AA 215 ? 1.5966 0.8910 1.7099 0.1642  -0.5607 -0.0677 202 LYS   a CE  
47501 N  NZ  . LYS   AA 215 ? 1.6113 0.9762 1.7478 0.1845  -0.5309 -0.0439 202 LYS   a NZ  
47502 N  N   . ASN   AA 216 ? 1.6544 0.7588 1.7958 0.0594  -0.5850 -0.1640 203 ASN   a N   
47503 C  CA  . ASN   AA 216 ? 1.6678 0.7719 1.8812 0.0676  -0.5958 -0.1067 203 ASN   a CA  
47504 C  C   . ASN   AA 216 ? 1.7704 0.8919 1.8916 0.0752  -0.5446 -0.0599 203 ASN   a C   
47505 O  O   . ASN   AA 216 ? 1.7866 0.9587 1.8966 0.1224  -0.5217 0.0377  203 ASN   a O   
47506 C  CB  . ASN   AA 216 ? 1.6835 0.7805 1.9753 0.0634  -0.6206 -0.1397 203 ASN   a CB  
47507 C  CG  . ASN   AA 216 ? 1.6217 0.7987 2.0458 0.0622  -0.6209 -0.2165 203 ASN   a CG  
47508 O  OD1 . ASN   AA 216 ? 1.6264 0.6600 2.1169 0.0190  -0.6266 -0.1614 203 ASN   a OD1 
47509 N  ND2 . ASN   AA 216 ? 1.6196 0.8178 2.0707 0.0194  -0.6637 -0.2504 203 ASN   a ND2 
47510 N  N   . THR   AA 217 ? 1.8093 0.9531 1.8178 0.0834  -0.4700 -0.0581 204 THR   a N   
47511 C  CA  . THR   AA 217 ? 1.8663 1.0632 1.7818 0.0633  -0.4705 -0.0291 204 THR   a CA  
47512 C  C   . THR   AA 217 ? 1.8261 1.0776 1.7381 0.1176  -0.4625 -0.0242 204 THR   a C   
47513 O  O   . THR   AA 217 ? 1.8262 1.1315 1.7431 0.1553  -0.4304 -0.0503 204 THR   a O   
47514 C  CB  . THR   AA 217 ? 1.9336 1.1011 1.7328 0.0347  -0.4414 -0.0379 204 THR   a CB  
47515 O  OG1 . THR   AA 217 ? 1.9975 1.1252 1.7741 0.0209  -0.3516 -0.0197 204 THR   a OG1 
47516 C  CG2 . THR   AA 217 ? 1.9649 1.2083 1.7473 0.0262  -0.4696 -0.0379 204 THR   a CG2 
47517 N  N   . GLY   AA 218 ? 1.7241 1.0580 1.7483 0.1451  -0.4832 0.0113  205 GLY   a N   
47518 C  CA  . GLY   AA 218 ? 1.6998 0.9521 1.6683 0.1952  -0.4866 0.0245  205 GLY   a CA  
47519 C  C   . GLY   AA 218 ? 1.6702 0.8476 1.6120 0.1334  -0.4934 -0.0068 205 GLY   a C   
47520 O  O   . GLY   AA 218 ? 1.6821 0.7527 1.5935 0.3070  -0.4457 -0.0629 205 GLY   a O   
47521 N  N   . LEU   AA 219 ? 1.6778 0.7501 1.6187 0.1327  -0.5042 0.0025  206 LEU   a N   
47522 C  CA  . LEU   AA 219 ? 1.7278 0.5539 1.5891 0.1139  -0.5132 0.0200  206 LEU   a CA  
47523 C  C   . LEU   AA 219 ? 1.7041 0.6074 1.5381 0.1102  -0.5442 0.0558  206 LEU   a C   
47524 O  O   . LEU   AA 219 ? 1.7212 0.4877 1.4527 0.0896  -0.5471 -0.0539 206 LEU   a O   
47525 C  CB  . LEU   AA 219 ? 1.7090 0.5388 1.6523 0.1243  -0.5426 0.0622  206 LEU   a CB  
47526 C  CG  . LEU   AA 219 ? 1.7096 0.5553 1.6833 0.1152  -0.5356 0.0465  206 LEU   a CG  
47527 C  CD1 . LEU   AA 219 ? 1.7548 0.5842 1.6830 0.0613  -0.5356 0.0723  206 LEU   a CD1 
47528 C  CD2 . LEU   AA 219 ? 1.6906 0.5679 1.6846 0.0961  -0.5239 0.0923  206 LEU   a CD2 
47529 N  N   . THR   AA 220 ? 1.6760 0.6152 1.4503 0.0765  -0.5215 0.0605  207 THR   a N   
47530 C  CA  . THR   AA 220 ? 1.6802 0.6641 1.4269 0.0610  -0.5048 0.0696  207 THR   a CA  
47531 C  C   . THR   AA 220 ? 1.6823 0.6815 1.4166 0.0941  -0.4462 0.0505  207 THR   a C   
47532 O  O   . THR   AA 220 ? 1.7155 0.6714 1.4661 0.1320  -0.4238 0.0628  207 THR   a O   
47533 C  CB  . THR   AA 220 ? 1.6833 0.7047 1.4247 0.0441  -0.5081 0.0614  207 THR   a CB  
47534 O  OG1 . THR   AA 220 ? 1.6557 0.6656 1.4822 0.0020  -0.5221 0.0557  207 THR   a OG1 
47535 C  CG2 . THR   AA 220 ? 1.6866 0.7166 1.4009 0.0319  -0.5188 0.0782  207 THR   a CG2 
47536 N  N   . PHE   AA 221 ? 1.7116 0.6855 1.3634 0.0968  -0.4343 0.0906  208 PHE   a N   
47537 C  CA  . PHE   AA 221 ? 1.7191 0.7253 1.3227 0.1094  -0.4408 0.1255  208 PHE   a CA  
47538 C  C   . PHE   AA 221 ? 1.7245 0.8025 1.2639 0.1006  -0.4759 0.1316  208 PHE   a C   
47539 O  O   . PHE   AA 221 ? 1.7909 0.8191 1.3158 0.1050  -0.4937 0.1881  208 PHE   a O   
47540 C  CB  . PHE   AA 221 ? 1.7188 0.7105 1.2941 0.1191  -0.4336 0.1306  208 PHE   a CB  
47541 C  CG  . PHE   AA 221 ? 1.7594 0.7414 1.2183 0.1326  -0.4344 0.1362  208 PHE   a CG  
47542 C  CD1 . PHE   AA 221 ? 1.7634 0.7933 1.1912 0.1423  -0.4343 0.1524  208 PHE   a CD1 
47543 C  CD2 . PHE   AA 221 ? 1.7270 0.7812 1.2182 0.1358  -0.4297 0.1215  208 PHE   a CD2 
47544 C  CE1 . PHE   AA 221 ? 1.7338 0.8684 1.1729 0.1256  -0.4520 0.1108  208 PHE   a CE1 
47545 C  CE2 . PHE   AA 221 ? 1.6928 0.8499 1.2426 0.1391  -0.4199 0.1088  208 PHE   a CE2 
47546 C  CZ  . PHE   AA 221 ? 1.7083 0.9023 1.1809 0.1233  -0.4234 0.0702  208 PHE   a CZ  
47547 N  N   . LYS   AA 222 ? 1.7014 0.7942 1.2404 0.0915  -0.4954 0.0855  209 LYS   a N   
47548 C  CA  . LYS   AA 222 ? 1.6887 0.8273 1.2601 0.0613  -0.4898 0.0489  209 LYS   a CA  
47549 C  C   . LYS   AA 222 ? 1.6647 0.8699 1.2308 0.0588  -0.4598 -0.0061 209 LYS   a C   
47550 O  O   . LYS   AA 222 ? 1.6203 0.8636 1.2097 0.0931  -0.3940 -0.0176 209 LYS   a O   
47551 C  CB  . LYS   AA 222 ? 1.7126 0.8263 1.3323 0.0492  -0.4553 0.0308  209 LYS   a CB  
47552 C  CG  . LYS   AA 222 ? 1.7184 0.8534 1.4443 0.0764  -0.4237 0.0439  209 LYS   a CG  
47553 C  CD  . LYS   AA 222 ? 1.6706 0.9240 1.5236 0.0639  -0.4059 0.0066  209 LYS   a CD  
47554 C  CE  . LYS   AA 222 ? 1.6894 0.9911 1.5863 0.1137  -0.4066 -0.0076 209 LYS   a CE  
47555 N  NZ  . LYS   AA 222 ? 1.6888 1.0308 1.6060 0.1221  -0.4318 -0.0629 209 LYS   a NZ  
47556 N  N   . LYS   AA 223 ? 1.6745 0.9061 1.2085 0.0332  -0.4848 0.0247  210 LYS   a N   
47557 C  CA  . LYS   AA 223 ? 1.6647 0.9859 1.2402 0.0165  -0.4841 0.0229  210 LYS   a CA  
47558 C  C   . LYS   AA 223 ? 1.6857 0.9848 1.2304 -0.0720 -0.5211 -0.0032 210 LYS   a C   
47559 O  O   . LYS   AA 223 ? 1.6803 0.9966 1.2834 -0.1348 -0.5479 0.0022  210 LYS   a O   
47560 C  CB  . LYS   AA 223 ? 1.6700 0.9821 1.2499 0.0339  -0.4879 0.0594  210 LYS   a CB  
47561 C  CG  . LYS   AA 223 ? 1.6337 0.9795 1.2848 0.0341  -0.5073 0.0496  210 LYS   a CG  
47562 C  CD  . LYS   AA 223 ? 1.6160 1.1118 1.3584 -0.0149 -0.4897 0.1198  210 LYS   a CD  
47563 C  CE  . LYS   AA 223 ? 1.5966 1.1881 1.3709 -0.0276 -0.5166 0.1092  210 LYS   a CE  
47564 N  NZ  . LYS   AA 223 ? 1.5916 1.2140 1.3370 -0.0401 -0.5022 0.1384  210 LYS   a NZ  
47565 N  N   . ASN   AA 224 ? 1.6844 0.9859 1.2493 -0.0637 -0.4904 -0.0210 211 ASN   a N   
47566 C  CA  . ASN   AA 224 ? 1.7423 1.0291 1.1942 -0.0628 -0.4831 -0.0202 211 ASN   a CA  
47567 C  C   . ASN   AA 224 ? 1.8040 1.0006 1.1657 -0.0488 -0.5162 -0.1008 211 ASN   a C   
47568 O  O   . ASN   AA 224 ? 1.8153 1.0120 1.2162 -0.1042 -0.5519 -0.1599 211 ASN   a O   
47569 C  CB  . ASN   AA 224 ? 1.8171 1.0783 1.2125 -0.0245 -0.4841 0.0400  211 ASN   a CB  
47570 C  CG  . ASN   AA 224 ? 1.8110 1.0852 1.2080 -0.0342 -0.4601 0.1198  211 ASN   a CG  
47571 O  OD1 . ASN   AA 224 ? 1.8755 1.1569 1.2732 0.0639  -0.4388 0.2273  211 ASN   a OD1 
47572 N  ND2 . ASN   AA 224 ? 1.8436 1.0559 1.2049 0.0034  -0.4297 0.1827  211 ASN   a ND2 
47573 N  N   . LEU   AA 225 ? 1.8052 0.9796 1.1449 -0.0115 -0.5252 -0.0855 212 LEU   a N   
47574 C  CA  . LEU   AA 225 ? 1.7731 0.9711 1.1375 0.0149  -0.5578 -0.1145 212 LEU   a CA  
47575 C  C   . LEU   AA 225 ? 1.8134 0.9930 1.1800 0.0501  -0.5498 -0.1218 212 LEU   a C   
47576 O  O   . LEU   AA 225 ? 1.7524 1.0022 1.2735 0.1066  -0.5199 -0.1649 212 LEU   a O   
47577 C  CB  . LEU   AA 225 ? 1.7414 0.9495 1.1590 0.0410  -0.5604 -0.1183 212 LEU   a CB  
47578 C  CG  . LEU   AA 225 ? 1.7837 0.8590 1.1524 0.0481  -0.5784 -0.0948 212 LEU   a CG  
47579 C  CD1 . LEU   AA 225 ? 1.7966 0.8649 1.1157 0.0782  -0.5932 -0.0889 212 LEU   a CD1 
47580 C  CD2 . LEU   AA 225 ? 1.7549 0.8676 1.2108 0.0830  -0.5464 -0.0927 212 LEU   a CD2 
47581 N  N   . GLN   AA 226 ? 1.8088 1.0309 1.2364 0.0197  -0.5771 -0.1340 213 GLN   a N   
47582 C  CA  . GLN   AA 226 ? 1.8027 1.0581 1.2926 0.0286  -0.5230 -0.1591 213 GLN   a CA  
47583 C  C   . GLN   AA 226 ? 1.7751 1.1027 1.3935 -0.0069 -0.5451 -0.1640 213 GLN   a C   
47584 O  O   . GLN   AA 226 ? 1.8057 1.2494 1.3487 -0.0900 -0.6442 -0.1960 213 GLN   a O   
47585 C  CB  . GLN   AA 226 ? 1.8008 1.1411 1.2853 0.0231  -0.5091 -0.1512 213 GLN   a CB  
47586 C  CG  . GLN   AA 226 ? 1.8087 1.1616 1.2939 0.0130  -0.4787 -0.1797 213 GLN   a CG  
47587 C  CD  . GLN   AA 226 ? 1.8006 1.1875 1.3698 0.0229  -0.4558 -0.1883 213 GLN   a CD  
47588 O  OE1 . GLN   AA 226 ? 1.7966 1.1737 1.4641 -0.0034 -0.4235 -0.2284 213 GLN   a OE1 
47589 N  NE2 . GLN   AA 226 ? 1.8212 1.1738 1.4221 0.0253  -0.4838 -0.1977 213 GLN   a NE2 
47590 N  N   . VAL   AA 227 ? 1.8130 0.9840 1.4508 -0.0410 -0.4834 -0.1528 214 VAL   a N   
47591 C  CA  . VAL   AA 227 ? 1.8154 1.0097 1.5041 -0.0541 -0.4749 -0.0926 214 VAL   a CA  
47592 C  C   . VAL   AA 227 ? 1.8197 0.9431 1.5354 -0.0915 -0.5423 -0.0658 214 VAL   a C   
47593 O  O   . VAL   AA 227 ? 1.8175 0.8250 1.5091 -0.1077 -0.5574 -0.0409 214 VAL   a O   
47594 C  CB  . VAL   AA 227 ? 1.8199 1.0444 1.3616 -0.1088 -0.4282 -0.1096 214 VAL   a CB  
47595 C  CG1 . VAL   AA 227 ? 1.8203 1.0787 1.3687 -0.1300 -0.3980 -0.0983 214 VAL   a CG1 
47596 C  CG2 . VAL   AA 227 ? 1.8213 1.0050 1.3986 -0.1412 -0.3650 -0.1266 214 VAL   a CG2 
47597 N  N   . GLU   AA 228 ? 1.7688 0.9997 1.6240 -0.0547 -0.5380 -0.0398 215 GLU   a N   
47598 C  CA  . GLU   AA 228 ? 1.8115 1.1449 1.6342 -0.0210 -0.5829 -0.0762 215 GLU   a CA  
47599 C  C   . GLU   AA 228 ? 1.8279 1.1886 1.6185 -0.0677 -0.6198 -0.1329 215 GLU   a C   
47600 O  O   . GLU   AA 228 ? 1.8891 1.2961 1.6761 -0.0205 -0.5562 -0.2366 215 GLU   a O   
47601 C  CB  . GLU   AA 228 ? 1.7846 1.1660 1.7477 0.0015  -0.5928 -0.0068 215 GLU   a CB  
47602 C  CG  . GLU   AA 228 ? 1.7915 1.3161 1.8311 0.0641  -0.5486 -0.0063 215 GLU   a CG  
47603 C  CD  . GLU   AA 228 ? 1.8034 1.3560 1.9428 0.0863  -0.4971 0.0328  215 GLU   a CD  
47604 O  OE1 . GLU   AA 228 ? 1.8331 1.4788 2.0300 0.1572  -0.5083 -0.0710 215 GLU   a OE1 
47605 O  OE2 . GLU   AA 228 ? 1.8173 1.6776 2.0827 0.1319  -0.4069 0.0385  215 GLU   a OE2 
47606 N  N   . ASN   AA 229 ? 1.9474 1.1976 1.6029 -0.0422 -0.6777 -0.1347 216 ASN   a N   
47607 C  CA  . ASN   AA 229 ? 1.9838 1.1618 1.5580 -0.0392 -0.7121 -0.1488 216 ASN   a CA  
47608 C  C   . ASN   AA 229 ? 1.9438 1.0873 1.5011 -0.0555 -0.6905 -0.1920 216 ASN   a C   
47609 O  O   . ASN   AA 229 ? 2.0098 0.9661 1.3846 -0.1394 -0.7610 -0.2083 216 ASN   a O   
47610 C  CB  . ASN   AA 229 ? 1.9591 1.2045 1.6139 -0.0386 -0.7426 -0.1275 216 ASN   a CB  
47611 C  CG  . ASN   AA 229 ? 1.9800 1.2330 1.6761 -0.0385 -0.7536 -0.0828 216 ASN   a CG  
47612 O  OD1 . ASN   AA 229 ? 2.0872 1.3559 1.7363 -0.0254 -0.6758 -0.1085 216 ASN   a OD1 
47613 N  ND2 . ASN   AA 229 ? 1.9848 1.1749 1.6949 -0.0816 -0.6961 -0.0823 216 ASN   a ND2 
47614 N  N   . MET   AA 230 ? 1.9676 0.9551 1.4159 -0.0149 -0.6742 -0.1748 217 MET   a N   
47615 C  CA  . MET   AA 230 ? 1.9111 0.8751 1.4444 0.0144  -0.5892 -0.1581 217 MET   a CA  
47616 C  C   . MET   AA 230 ? 1.9511 0.8914 1.3779 0.0296  -0.5387 -0.1710 217 MET   a C   
47617 O  O   . MET   AA 230 ? 2.0089 1.0568 1.4051 0.0149  -0.5274 -0.2610 217 MET   a O   
47618 C  CB  . MET   AA 230 ? 1.8962 0.8407 1.4930 0.0414  -0.5744 -0.1230 217 MET   a CB  
47619 C  CG  . MET   AA 230 ? 1.8808 0.8133 1.5328 0.0381  -0.5627 -0.0966 217 MET   a CG  
47620 S  SD  . MET   AA 230 ? 1.8699 0.6748 1.5580 -0.0057 -0.5203 -0.0791 217 MET   a SD  
47621 C  CE  . MET   AA 230 ? 1.9001 0.5604 1.5570 0.0062  -0.4992 0.0104  217 MET   a CE  
47622 N  N   . LYS   AA 231 ? 1.9356 0.8810 1.4096 0.0343  -0.5001 -0.1544 218 LYS   a N   
47623 C  CA  . LYS   AA 231 ? 1.9059 0.8391 1.3730 0.0682  -0.4951 -0.0725 218 LYS   a CA  
47624 C  C   . LYS   AA 231 ? 1.8976 0.6851 1.3034 0.0435  -0.4946 -0.1062 218 LYS   a C   
47625 O  O   . LYS   AA 231 ? 1.7989 0.6336 1.3012 0.0492  -0.4775 -0.1444 218 LYS   a O   
47626 C  CB  . LYS   AA 231 ? 1.9252 0.9022 1.4364 0.0854  -0.4624 -0.0285 218 LYS   a CB  
47627 C  CG  . LYS   AA 231 ? 1.9432 0.9396 1.4645 0.1341  -0.4493 0.0445  218 LYS   a CG  
47628 C  CD  . LYS   AA 231 ? 1.9567 1.0038 1.4964 0.1529  -0.4182 0.0921  218 LYS   a CD  
47629 C  CE  . LYS   AA 231 ? 1.9834 0.9515 1.4600 0.1683  -0.4403 0.1422  218 LYS   a CE  
47630 N  NZ  . LYS   AA 231 ? 2.0099 0.9378 1.4518 0.1825  -0.4363 0.1881  218 LYS   a NZ  
47631 N  N   . TRP   AA 232 ? 1.8830 0.7207 1.3302 0.0654  -0.4709 -0.0761 219 TRP   a N   
47632 C  CA  . TRP   AA 232 ? 1.8631 0.8064 1.3656 0.0630  -0.4946 -0.0731 219 TRP   a CA  
47633 C  C   . TRP   AA 232 ? 1.9307 0.8440 1.4091 0.0381  -0.4789 -0.1208 219 TRP   a C   
47634 O  O   . TRP   AA 232 ? 1.9301 0.8198 1.5109 0.0543  -0.4402 -0.1666 219 TRP   a O   
47635 C  CB  . TRP   AA 232 ? 1.8527 0.7809 1.3268 0.0865  -0.5269 -0.0267 219 TRP   a CB  
47636 C  CG  . TRP   AA 232 ? 1.8204 0.7807 1.3168 0.0964  -0.5164 -0.0245 219 TRP   a CG  
47637 C  CD1 . TRP   AA 232 ? 1.8052 0.8160 1.3350 0.1203  -0.5302 0.0353  219 TRP   a CD1 
47638 C  CD2 . TRP   AA 232 ? 1.8100 0.8243 1.3293 0.1220  -0.5115 0.0003  219 TRP   a CD2 
47639 N  NE1 . TRP   AA 232 ? 1.7905 0.8622 1.3365 0.0863  -0.5284 0.0531  219 TRP   a NE1 
47640 C  CE2 . TRP   AA 232 ? 1.7885 0.8335 1.3160 0.0909  -0.5319 0.0198  219 TRP   a CE2 
47641 C  CE3 . TRP   AA 232 ? 1.7996 0.7985 1.3092 0.1158  -0.5208 -0.0282 219 TRP   a CE3 
47642 C  CZ2 . TRP   AA 232 ? 1.7398 0.9242 1.3284 0.0919  -0.5481 0.0492  219 TRP   a CZ2 
47643 C  CZ3 . TRP   AA 232 ? 1.7408 0.7804 1.3332 0.1260  -0.5384 0.0013  219 TRP   a CZ3 
47644 C  CH2 . TRP   AA 232 ? 1.7402 0.8063 1.3664 0.0928  -0.5279 -0.0209 219 TRP   a CH2 
47645 N  N   . ASP   AA 233 ? 2.0133 0.7898 1.3630 -0.0074 -0.4857 -0.1822 220 ASP   a N   
47646 C  CA  . ASP   AA 233 ? 2.0705 0.8117 1.3970 -0.0520 -0.5148 -0.2064 220 ASP   a CA  
47647 C  C   . ASP   AA 233 ? 2.0782 0.7473 1.3772 -0.0553 -0.4885 -0.2669 220 ASP   a C   
47648 O  O   . ASP   AA 233 ? 2.1946 0.6897 1.4064 -0.1008 -0.4821 -0.3930 220 ASP   a O   
47649 C  CB  . ASP   AA 233 ? 2.0951 0.8589 1.4468 -0.0723 -0.5466 -0.1805 220 ASP   a CB  
47650 C  CG  . ASP   AA 233 ? 2.1601 0.9074 1.4588 -0.0673 -0.5284 -0.2058 220 ASP   a CG  
47651 O  OD1 . ASP   AA 233 ? 2.1907 0.9243 1.4853 -0.1122 -0.5028 -0.2203 220 ASP   a OD1 
47652 O  OD2 . ASP   AA 233 ? 2.1662 0.8826 1.5427 -0.0539 -0.5415 -0.1320 220 ASP   a OD2 
47653 N  N   . PHE   AA 234 ? 2.0439 0.7174 1.3750 -0.0833 -0.5019 -0.2576 221 PHE   a N   
47654 C  CA  . PHE   AA 234 ? 1.9903 0.7384 1.3628 -0.0584 -0.5104 -0.2409 221 PHE   a CA  
47655 C  C   . PHE   AA 234 ? 1.9878 0.6995 1.3552 -0.0459 -0.4921 -0.2055 221 PHE   a C   
47656 O  O   . PHE   AA 234 ? 1.9702 0.6773 1.4258 0.0506  -0.4662 -0.2538 221 PHE   a O   
47657 C  CB  . PHE   AA 234 ? 1.9862 0.7197 1.3531 -0.0592 -0.5208 -0.2638 221 PHE   a CB  
47658 C  CG  . PHE   AA 234 ? 1.9693 0.7295 1.2998 -0.0203 -0.4948 -0.2692 221 PHE   a CG  
47659 C  CD1 . PHE   AA 234 ? 1.9838 0.7392 1.2436 -0.0129 -0.4897 -0.2653 221 PHE   a CD1 
47660 C  CD2 . PHE   AA 234 ? 1.9586 0.7014 1.2813 0.0116  -0.4761 -0.2910 221 PHE   a CD2 
47661 C  CE1 . PHE   AA 234 ? 1.9587 0.7337 1.2135 -0.0040 -0.4710 -0.2613 221 PHE   a CE1 
47662 C  CE2 . PHE   AA 234 ? 1.9365 0.7277 1.2420 0.0227  -0.4701 -0.2891 221 PHE   a CE2 
47663 C  CZ  . PHE   AA 234 ? 1.9239 0.7176 1.2244 -0.0011 -0.4810 -0.2955 221 PHE   a CZ  
47664 N  N   . ALA   AA 235 ? 1.9510 0.7101 1.3234 -0.0265 -0.4968 -0.1359 222 ALA   a N   
47665 C  CA  . ALA   AA 235 ? 1.9488 0.6942 1.3380 -0.0032 -0.4721 -0.1155 222 ALA   a CA  
47666 C  C   . ALA   AA 235 ? 1.9818 0.6199 1.3787 -0.0195 -0.4895 -0.1133 222 ALA   a C   
47667 O  O   . ALA   AA 235 ? 1.9795 0.4799 1.5244 -0.0201 -0.4914 -0.1443 222 ALA   a O   
47668 C  CB  . ALA   AA 235 ? 1.9599 0.7176 1.3163 -0.0064 -0.4523 -0.0540 222 ALA   a CB  
47669 N  N   . LYS   AA 236 ? 2.0080 0.6806 1.3720 -0.0053 -0.4855 -0.1078 223 LYS   a N   
47670 C  CA  . LYS   AA 236 ? 2.0470 0.7726 1.3806 0.0434  -0.4448 -0.1155 223 LYS   a CA  
47671 C  C   . LYS   AA 236 ? 2.0367 0.7191 1.3979 0.0832  -0.4770 -0.1587 223 LYS   a C   
47672 O  O   . LYS   AA 236 ? 2.0735 0.6893 1.3597 0.0644  -0.4721 -0.2573 223 LYS   a O   
47673 C  CB  . LYS   AA 236 ? 2.0784 0.8626 1.3626 0.0636  -0.4191 -0.0992 223 LYS   a CB  
47674 C  CG  . LYS   AA 236 ? 2.0802 0.9109 1.3984 0.0580  -0.4208 -0.0930 223 LYS   a CG  
47675 C  CD  . LYS   AA 236 ? 2.1487 0.9647 1.3855 0.0446  -0.4068 -0.1355 223 LYS   a CD  
47676 C  CE  . LYS   AA 236 ? 2.1451 1.0663 1.4246 0.0162  -0.4379 -0.1241 223 LYS   a CE  
47677 N  NZ  . LYS   AA 236 ? 2.1031 1.1504 1.4289 0.0224  -0.4058 -0.1150 223 LYS   a NZ  
47678 N  N   . ASP   AA 237 ? 2.0298 0.6993 1.4581 0.0242  -0.4967 -0.1183 224 ASP   a N   
47679 C  CA  . ASP   AA 237 ? 2.0838 0.6840 1.5259 0.0478  -0.5115 -0.0801 224 ASP   a CA  
47680 C  C   . ASP   AA 237 ? 2.0551 0.6543 1.5312 0.0489  -0.4948 -0.0532 224 ASP   a C   
47681 O  O   . ASP   AA 237 ? 2.0645 0.7338 1.5957 0.0809  -0.5355 0.1014  224 ASP   a O   
47682 C  CB  . ASP   AA 237 ? 2.0928 0.7109 1.6010 0.0123  -0.4946 -0.0568 224 ASP   a CB  
47683 C  CG  . ASP   AA 237 ? 2.1718 0.7478 1.5988 -0.0005 -0.5068 -0.0310 224 ASP   a CG  
47684 O  OD1 . ASP   AA 237 ? 2.1580 0.6881 1.6871 -0.0265 -0.5228 0.0518  224 ASP   a OD1 
47685 O  OD2 . ASP   AA 237 ? 2.2561 0.7462 1.5745 0.0081  -0.5272 -0.0399 224 ASP   a OD2 
47686 N  N   . ILE   AA 238 ? 2.0323 0.6519 1.4317 0.0435  -0.4799 -0.0087 225 ILE   a N   
47687 C  CA  . ILE   AA 238 ? 2.0284 0.6629 1.4272 0.0762  -0.4559 0.0202  225 ILE   a CA  
47688 C  C   . ILE   AA 238 ? 2.0474 0.6808 1.4217 0.0827  -0.4066 0.0462  225 ILE   a C   
47689 O  O   . ILE   AA 238 ? 2.1095 0.5360 1.3574 0.2005  -0.4403 0.1687  225 ILE   a O   
47690 C  CB  . ILE   AA 238 ? 1.9608 0.7001 1.3949 0.0330  -0.4736 0.0047  225 ILE   a CB  
47691 C  CG1 . ILE   AA 238 ? 1.9400 0.6565 1.4150 0.0154  -0.4876 -0.0355 225 ILE   a CG1 
47692 C  CG2 . ILE   AA 238 ? 1.9462 0.6795 1.3978 0.0335  -0.4730 -0.0139 225 ILE   a CG2 
47693 C  CD1 . ILE   AA 238 ? 1.8907 0.6423 1.3998 -0.0008 -0.4936 -0.0262 225 ILE   a CD1 
47694 N  N   . LYS   AA 239 ? 2.0765 0.6998 1.4873 0.1298  -0.4255 0.0339  226 LYS   a N   
47695 C  CA  . LYS   AA 239 ? 2.0545 0.8674 1.5161 0.1297  -0.4074 0.0334  226 LYS   a CA  
47696 C  C   . LYS   AA 239 ? 2.0827 0.8007 1.4900 0.1003  -0.3882 0.0246  226 LYS   a C   
47697 O  O   . LYS   AA 239 ? 2.1072 0.8886 1.5074 0.0510  -0.3720 0.0201  226 LYS   a O   
47698 C  CB  . LYS   AA 239 ? 2.1111 0.9672 1.5376 0.1265  -0.4262 -0.0157 226 LYS   a CB  
47699 C  CG  . LYS   AA 239 ? 2.1486 1.0999 1.5576 0.1593  -0.4313 0.0259  226 LYS   a CG  
47700 C  CD  . LYS   AA 239 ? 2.2003 1.1552 1.6291 0.1317  -0.4854 0.0290  226 LYS   a CD  
47701 C  CE  . LYS   AA 239 ? 2.2629 1.2352 1.6437 0.1407  -0.4877 0.0736  226 LYS   a CE  
47702 N  NZ  . LYS   AA 239 ? 2.2832 1.2351 1.7046 0.1294  -0.4651 0.0987  226 LYS   a NZ  
47703 N  N   . GLY   AA 240 ? 2.0814 0.6622 1.4032 0.1278  -0.3850 0.0160  227 GLY   a N   
47704 C  CA  . GLY   AA 240 ? 2.0553 0.5959 1.3967 0.1572  -0.3845 -0.0264 227 GLY   a CA  
47705 C  C   . GLY   AA 240 ? 2.0124 0.4334 1.3855 0.1569  -0.4264 -0.0157 227 GLY   a C   
47706 O  O   . GLY   AA 240 ? 2.1052 0.2728 1.3667 0.0506  -0.4269 -0.0338 227 GLY   a O   
47707 N  N   . TYR   AA 241 ? 1.9971 0.5268 1.3394 0.1635  -0.4385 -0.0605 228 TYR   a N   
47708 C  CA  . TYR   AA 241 ? 1.9464 0.5220 1.3148 0.1459  -0.4854 -0.0736 228 TYR   a CA  
47709 C  C   . TYR   AA 241 ? 1.9752 0.5673 1.3094 0.1442  -0.4892 -0.0330 228 TYR   a C   
47710 O  O   . TYR   AA 241 ? 2.0196 0.6126 1.3152 0.1737  -0.4753 -0.0365 228 TYR   a O   
47711 C  CB  . TYR   AA 241 ? 1.9233 0.4751 1.2732 0.1483  -0.4592 -0.0864 228 TYR   a CB  
47712 C  CG  . TYR   AA 241 ? 1.8577 0.5856 1.2790 0.1593  -0.4865 -0.1308 228 TYR   a CG  
47713 C  CD1 . TYR   AA 241 ? 1.8954 0.6417 1.3133 0.1544  -0.4827 -0.0853 228 TYR   a CD1 
47714 C  CD2 . TYR   AA 241 ? 1.8617 0.6196 1.2602 0.1300  -0.4922 -0.1451 228 TYR   a CD2 
47715 C  CE1 . TYR   AA 241 ? 1.9040 0.7046 1.3727 0.1879  -0.4805 -0.1045 228 TYR   a CE1 
47716 C  CE2 . TYR   AA 241 ? 1.8594 0.6801 1.3174 0.1486  -0.4832 -0.1447 228 TYR   a CE2 
47717 C  CZ  . TYR   AA 241 ? 1.8770 0.6657 1.3796 0.2056  -0.4908 -0.1225 228 TYR   a CZ  
47718 O  OH  . TYR   AA 241 ? 1.9215 0.6971 1.4450 0.2531  -0.4871 -0.1440 228 TYR   a OH  
47719 N  N   . GLY   AA 242 ? 1.9870 0.5798 1.3192 0.1541  -0.5189 -0.0456 229 GLY   a N   
47720 C  CA  . GLY   AA 242 ? 1.9599 0.5923 1.3437 0.1372  -0.5351 -0.0635 229 GLY   a CA  
47721 C  C   . GLY   AA 242 ? 1.9567 0.6338 1.3808 0.1637  -0.5638 -0.1014 229 GLY   a C   
47722 O  O   . GLY   AA 242 ? 1.9656 0.6324 1.3949 0.1834  -0.5892 -0.0791 229 GLY   a O   
47723 N  N   . THR   AA 243 ? 1.9409 0.6479 1.4393 0.1575  -0.5603 -0.1304 230 THR   a N   
47724 C  CA  . THR   AA 243 ? 1.9406 0.6559 1.4823 0.1468  -0.5594 -0.1602 230 THR   a CA  
47725 C  C   . THR   AA 243 ? 1.9516 0.7041 1.5076 0.1808  -0.5228 -0.1172 230 THR   a C   
47726 O  O   . THR   AA 243 ? 1.9942 0.6113 1.5213 0.2423  -0.5222 -0.0589 230 THR   a O   
47727 C  CB  . THR   AA 243 ? 1.9340 0.5790 1.4918 0.1409  -0.5630 -0.2134 230 THR   a CB  
47728 O  OG1 . THR   AA 243 ? 1.9348 0.5634 1.4823 0.1476  -0.5198 -0.2464 230 THR   a OG1 
47729 C  CG2 . THR   AA 243 ? 1.9268 0.5503 1.5035 0.1230  -0.5549 -0.2079 230 THR   a CG2 
47730 N  N   . GLN   AA 244 ? 1.9350 0.7217 1.5365 0.1345  -0.4926 -0.1676 231 GLN   a N   
47731 C  CA  . GLN   AA 244 ? 2.0043 0.7861 1.5928 0.1132  -0.4104 -0.1767 231 GLN   a CA  
47732 C  C   . GLN   AA 244 ? 2.0236 0.8226 1.6509 0.0905  -0.4386 -0.1593 231 GLN   a C   
47733 O  O   . GLN   AA 244 ? 2.0576 0.7572 1.6837 0.1076  -0.4135 -0.1021 231 GLN   a O   
47734 C  CB  . GLN   AA 244 ? 1.9769 0.7925 1.5824 0.1209  -0.3819 -0.1775 231 GLN   a CB  
47735 C  CG  . GLN   AA 244 ? 2.0267 0.8360 1.5942 0.1340  -0.3546 -0.1756 231 GLN   a CG  
47736 C  CD  . GLN   AA 244 ? 2.0166 0.8414 1.5942 0.1352  -0.2938 -0.1701 231 GLN   a CD  
47737 O  OE1 . GLN   AA 244 ? 2.0334 0.8292 1.5764 0.1815  -0.2808 -0.1266 231 GLN   a OE1 
47738 N  NE2 . GLN   AA 244 ? 2.0379 0.8837 1.5447 0.1570  -0.2832 -0.1732 231 GLN   a NE2 
47739 N  N   . LYS   AA 245 ? 2.1377 0.9075 1.6773 0.0106  -0.4491 -0.2105 232 LYS   a N   
47740 C  CA  . LYS   AA 245 ? 2.1575 0.9550 1.7429 -0.0493 -0.4800 -0.2250 232 LYS   a CA  
47741 C  C   . LYS   AA 245 ? 2.1850 0.9690 1.7451 -0.1386 -0.4869 -0.2402 232 LYS   a C   
47742 O  O   . LYS   AA 245 ? 2.1968 0.9785 1.7210 -0.2239 -0.4896 -0.3081 232 LYS   a O   
47743 C  CB  . LYS   AA 245 ? 2.1886 0.9515 1.7458 -0.0250 -0.5006 -0.2219 232 LYS   a CB  
47744 C  CG  . LYS   AA 245 ? 2.1702 0.8718 1.7456 -0.0024 -0.5270 -0.2241 232 LYS   a CG  
47745 C  CD  . LYS   AA 245 ? 2.1750 0.8587 1.6783 0.0184  -0.5461 -0.2164 232 LYS   a CD  
47746 C  CE  . LYS   AA 245 ? 2.1689 0.8379 1.6456 0.0247  -0.5771 -0.2084 232 LYS   a CE  
47747 N  NZ  . LYS   AA 245 ? 2.2112 0.8402 1.6607 0.0372  -0.5936 -0.2213 232 LYS   a NZ  
47748 N  N   . ILE   AA 246 ? 2.2126 1.0627 1.9204 -0.1866 -0.4620 -0.2574 233 ILE   a N   
47749 C  CA  . ILE   AA 246 ? 2.2125 1.1689 1.9180 -0.1815 -0.4176 -0.2576 233 ILE   a CA  
47750 C  C   . ILE   AA 246 ? 2.1561 1.1705 2.0633 -0.1737 -0.4330 -0.2500 233 ILE   a C   
47751 O  O   . ILE   AA 246 ? 2.0956 1.2883 2.1404 -0.2158 -0.4442 -0.2625 233 ILE   a O   
47752 C  CB  . ILE   AA 246 ? 2.1972 1.1627 1.9567 -0.2029 -0.4387 -0.3190 233 ILE   a CB  
47753 C  CG1 . ILE   AA 246 ? 2.1658 1.2710 1.9385 -0.1968 -0.3811 -0.3417 233 ILE   a CG1 
47754 C  CG2 . ILE   AA 246 ? 2.1818 1.0386 1.9455 -0.2079 -0.3986 -0.3413 233 ILE   a CG2 
47755 C  CD1 . ILE   AA 246 ? 2.1782 1.2673 1.9850 -0.1521 -0.3622 -0.3728 233 ILE   a CD1 
47756 O  OXT . ILE   AA 246 ? 2.1620 1.1319 2.1421 -0.1152 -0.4260 -0.2932 233 ILE   a OXT 
47757 N  N   . THR   BA 1   ? 1.6790 0.7010 1.3082 -0.0356 -0.3194 0.0941  1   THR   b N   
47758 C  CA  . THR   BA 1   ? 1.6481 0.6779 1.2607 0.0171  -0.3508 0.0581  1   THR   b CA  
47759 C  C   . THR   BA 1   ? 1.6351 0.5356 1.1924 0.0409  -0.3215 0.1127  1   THR   b C   
47760 O  O   . THR   BA 1   ? 1.6063 0.4992 1.1834 0.0726  -0.3255 0.1203  1   THR   b O   
47761 C  CB  . THR   BA 1   ? 1.6267 0.6818 1.2600 0.0463  -0.3727 0.0606  1   THR   b CB  
47762 O  OG1 . THR   BA 1   ? 1.6661 0.7634 1.3125 0.0568  -0.4234 0.0724  1   THR   b OG1 
47763 C  CG2 . THR   BA 1   ? 1.6001 0.6990 1.1867 0.0221  -0.3756 0.0654  1   THR   b CG2 
47764 N  N   . SER   BA 2   ? 1.6752 0.4900 1.1845 0.0531  -0.3134 0.1002  2   SER   b N   
47765 C  CA  . SER   BA 2   ? 1.7001 0.5305 1.1360 0.0363  -0.2965 0.0510  2   SER   b CA  
47766 C  C   . SER   BA 2   ? 1.6680 0.5138 1.0907 0.0258  -0.2844 0.0171  2   SER   b C   
47767 O  O   . SER   BA 2   ? 1.7103 0.3904 1.0497 -0.0343 -0.2811 -0.0462 2   SER   b O   
47768 C  CB  . SER   BA 2   ? 1.7170 0.5239 1.1281 0.0244  -0.2811 0.0581  2   SER   b CB  
47769 O  OG  . SER   BA 2   ? 1.7255 0.5464 1.1584 0.0563  -0.2985 0.0701  2   SER   b OG  
47770 N  N   . ILE   BA 3   ? 1.6734 0.4846 1.0453 0.0289  -0.3050 0.0163  3   ILE   b N   
47771 C  CA  . ILE   BA 3   ? 1.6455 0.5147 1.0907 0.0184  -0.2626 0.0819  3   ILE   b CA  
47772 C  C   . ILE   BA 3   ? 1.6341 0.5446 1.0934 0.0347  -0.2510 0.0186  3   ILE   b C   
47773 O  O   . ILE   BA 3   ? 1.6438 0.4999 1.0660 0.0864  -0.1966 0.0518  3   ILE   b O   
47774 C  CB  . ILE   BA 3   ? 1.6353 0.4741 1.0787 0.0309  -0.2388 0.1186  3   ILE   b CB  
47775 C  CG1 . ILE   BA 3   ? 1.5937 0.4413 1.1074 0.0505  -0.2526 0.1759  3   ILE   b CG1 
47776 C  CG2 . ILE   BA 3   ? 1.6308 0.5194 1.1468 0.0201  -0.2411 0.1410  3   ILE   b CG2 
47777 C  CD1 . ILE   BA 3   ? 1.5750 0.4410 1.0810 0.0677  -0.2355 0.1922  3   ILE   b CD1 
47778 N  N   . MET   BA 4   ? 1.6478 0.6059 1.0910 0.0260  -0.2207 0.0417  4   MET   b N   
47779 C  CA  . MET   BA 4   ? 1.6235 0.7130 1.1552 0.0500  -0.2126 0.0303  4   MET   b CA  
47780 C  C   . MET   BA 4   ? 1.6178 0.7109 1.1529 0.0262  -0.2160 0.0206  4   MET   b C   
47781 O  O   . MET   BA 4   ? 1.5976 0.7550 1.1625 0.0179  -0.2187 -0.0073 4   MET   b O   
47782 C  CB  . MET   BA 4   ? 1.6471 0.7237 1.1685 0.0638  -0.1731 0.0123  4   MET   b CB  
47783 C  CG  . MET   BA 4   ? 1.6498 0.7892 1.2375 0.0715  -0.1338 0.0565  4   MET   b CG  
47784 S  SD  . MET   BA 4   ? 1.6378 0.7508 1.3084 0.0837  -0.0924 0.0600  4   MET   b SD  
47785 C  CE  . MET   BA 4   ? 1.6596 0.7512 1.2487 0.0817  -0.1198 0.0744  4   MET   b CE  
47786 N  N   . ALA   BA 5   ? 1.6623 0.7117 1.1428 0.0619  -0.2327 0.0141  5   ALA   b N   
47787 C  CA  . ALA   BA 5   ? 1.7036 0.6855 1.1533 0.0430  -0.2030 0.0073  5   ALA   b CA  
47788 C  C   . ALA   BA 5   ? 1.7245 0.6656 1.1180 0.0170  -0.1835 -0.0029 5   ALA   b C   
47789 O  O   . ALA   BA 5   ? 1.7066 0.6113 1.1306 0.0376  -0.1676 -0.0425 5   ALA   b O   
47790 C  CB  . ALA   BA 5   ? 1.6874 0.6993 1.1431 0.0421  -0.2072 0.0019  5   ALA   b CB  
47791 N  N   . VAL   BA 6   ? 1.7552 0.6911 1.1105 -0.0161 -0.1881 -0.0061 6   VAL   b N   
47792 C  CA  . VAL   BA 6   ? 1.7151 0.6823 1.1426 -0.0219 -0.1940 -0.0042 6   VAL   b CA  
47793 C  C   . VAL   BA 6   ? 1.6798 0.6725 1.1433 -0.0053 -0.2072 -0.0168 6   VAL   b C   
47794 O  O   . VAL   BA 6   ? 1.7055 0.5181 1.1583 0.0200  -0.2245 -0.0588 6   VAL   b O   
47795 C  CB  . VAL   BA 6   ? 1.7134 0.7045 1.1487 -0.0324 -0.1807 -0.0164 6   VAL   b CB  
47796 C  CG1 . VAL   BA 6   ? 1.7221 0.7345 1.1656 -0.0410 -0.1812 -0.0433 6   VAL   b CG1 
47797 C  CG2 . VAL   BA 6   ? 1.7150 0.7277 1.1284 -0.0231 -0.1834 -0.0057 6   VAL   b CG2 
47798 N  N   . THR   BA 7   ? 1.7047 0.6990 1.1062 0.0305  -0.2037 0.0523  7   THR   b N   
47799 C  CA  . THR   BA 7   ? 1.7661 0.7072 1.1244 0.0005  -0.1517 0.1156  7   THR   b CA  
47800 C  C   . THR   BA 7   ? 1.8347 0.7441 1.1189 0.0146  -0.0995 0.1216  7   THR   b C   
47801 O  O   . THR   BA 7   ? 1.8660 0.8399 1.1757 -0.0474 -0.1049 0.0958  7   THR   b O   
47802 C  CB  . THR   BA 7   ? 1.7830 0.6704 1.0571 0.0389  -0.1576 0.1740  7   THR   b CB  
47803 O  OG1 . THR   BA 7   ? 1.7256 0.5849 1.0893 0.0995  -0.1858 0.2538  7   THR   b OG1 
47804 C  CG2 . THR   BA 7   ? 1.7490 0.7149 1.0336 0.0254  -0.1432 0.1142  7   THR   b CG2 
47805 N  N   . PHE   BA 8   ? 1.8359 0.7050 1.1201 0.0178  -0.0787 0.0913  8   PHE   b N   
47806 C  CA  . PHE   BA 8   ? 1.8764 0.7957 1.1149 0.0203  -0.0926 0.1037  8   PHE   b CA  
47807 C  C   . PHE   BA 8   ? 1.8738 0.8138 1.1236 0.0326  -0.0971 0.1131  8   PHE   b C   
47808 O  O   . PHE   BA 8   ? 1.8724 0.9199 1.1075 0.0147  -0.0721 0.0581  8   PHE   b O   
47809 C  CB  . PHE   BA 8   ? 1.8796 0.8341 1.1416 0.0149  -0.0803 0.1114  8   PHE   b CB  
47810 C  CG  . PHE   BA 8   ? 1.9483 0.7816 1.1461 -0.0043 -0.1035 0.0954  8   PHE   b CG  
47811 C  CD1 . PHE   BA 8   ? 1.9375 0.7509 1.1493 0.0013  -0.0875 0.0613  8   PHE   b CD1 
47812 C  CD2 . PHE   BA 8   ? 2.0003 0.7284 1.1804 -0.0171 -0.1075 0.1419  8   PHE   b CD2 
47813 C  CE1 . PHE   BA 8   ? 1.9411 0.7474 1.1462 0.0000  -0.0924 0.1322  8   PHE   b CE1 
47814 C  CE2 . PHE   BA 8   ? 2.0133 0.7107 1.1569 -0.0198 -0.0945 0.1628  8   PHE   b CE2 
47815 C  CZ  . PHE   BA 8   ? 1.9765 0.7373 1.1639 -0.0181 -0.1053 0.1711  8   PHE   b CZ  
47816 N  N   . LYS   BA 9   ? 1.9103 0.8315 1.1264 0.0405  -0.1221 0.1501  9   LYS   b N   
47817 C  CA  . LYS   BA 9   ? 1.9626 0.8786 1.1321 0.0131  -0.1288 0.2185  9   LYS   b CA  
47818 C  C   . LYS   BA 9   ? 1.9681 0.8046 1.1343 0.0410  -0.1664 0.3096  9   LYS   b C   
47819 O  O   . LYS   BA 9   ? 1.9584 0.7583 1.1253 0.0640  -0.1845 0.4061  9   LYS   b O   
47820 C  CB  . LYS   BA 9   ? 2.0190 0.9081 1.1315 -0.0066 -0.0956 0.2300  9   LYS   b CB  
47821 C  CG  . LYS   BA 9   ? 2.0130 1.0170 1.1404 -0.0309 -0.1067 0.1729  9   LYS   b CG  
47822 C  CD  . LYS   BA 9   ? 2.0571 1.1502 1.1665 -0.0257 -0.0663 0.0821  9   LYS   b CD  
47823 C  CE  . LYS   BA 9   ? 2.1012 1.2200 1.1348 0.0155  -0.0708 0.0974  9   LYS   b CE  
47824 N  NZ  . LYS   BA 9   ? 2.1403 1.2971 1.1240 0.0236  -0.0377 0.0407  9   LYS   b NZ  
47825 N  N   . ASP   BA 10  ? 1.9767 0.8466 1.1911 0.0074  -0.1530 0.3271  10  ASP   b N   
47826 C  CA  . ASP   BA 10  ? 2.0928 0.7902 1.2142 0.0010  -0.1240 0.3030  10  ASP   b CA  
47827 C  C   . ASP   BA 10  ? 2.0738 0.7785 1.2285 -0.0135 -0.1368 0.2721  10  ASP   b C   
47828 O  O   . ASP   BA 10  ? 2.0786 0.8370 1.2021 -0.0884 -0.1342 0.2701  10  ASP   b O   
47829 C  CB  . ASP   BA 10  ? 2.1245 0.8092 1.2338 -0.0458 -0.0699 0.3025  10  ASP   b CB  
47830 C  CG  . ASP   BA 10  ? 2.2018 0.9580 1.2403 -0.0655 -0.0986 0.2763  10  ASP   b CG  
47831 O  OD1 . ASP   BA 10  ? 2.1725 1.1325 1.2641 0.0046  -0.0913 0.1997  10  ASP   b OD1 
47832 O  OD2 . ASP   BA 10  ? 2.2134 1.0492 1.3744 -0.1107 -0.0435 0.2810  10  ASP   b OD2 
47833 N  N   . GLY   BA 11  ? 2.0145 0.7389 1.1694 -0.0430 -0.1516 0.2104  11  GLY   b N   
47834 C  CA  . GLY   BA 11  ? 1.9272 0.6920 1.1908 -0.0502 -0.2013 0.1776  11  GLY   b CA  
47835 C  C   . GLY   BA 11  ? 1.8293 0.6854 1.1826 -0.0474 -0.2423 0.1730  11  GLY   b C   
47836 O  O   . GLY   BA 11  ? 1.7791 0.8091 1.3104 -0.0705 -0.2322 0.2070  11  GLY   b O   
47837 N  N   . VAL   BA 12  ? 1.7820 0.5502 1.1211 -0.1075 -0.2209 0.1265  12  VAL   b N   
47838 C  CA  . VAL   BA 12  ? 1.7372 0.5452 1.0698 -0.0795 -0.2203 0.1029  12  VAL   b CA  
47839 C  C   . VAL   BA 12  ? 1.7344 0.5142 1.0198 -0.0789 -0.1976 0.0891  12  VAL   b C   
47840 O  O   . VAL   BA 12  ? 1.8112 0.4013 1.0706 -0.0624 -0.1941 0.1034  12  VAL   b O   
47841 C  CB  . VAL   BA 12  ? 1.7194 0.5272 1.0808 -0.0679 -0.2177 0.1117  12  VAL   b CB  
47842 C  CG1 . VAL   BA 12  ? 1.7174 0.4961 1.0818 -0.0659 -0.2087 0.1296  12  VAL   b CG1 
47843 C  CG2 . VAL   BA 12  ? 1.7157 0.5631 1.0714 -0.0718 -0.2112 0.1242  12  VAL   b CG2 
47844 N  N   . ILE   BA 13  ? 1.6903 0.5295 0.9815 -0.0259 -0.1865 0.0712  13  ILE   b N   
47845 C  CA  . ILE   BA 13  ? 1.6888 0.5329 0.9827 -0.0154 -0.1907 0.0484  13  ILE   b CA  
47846 C  C   . ILE   BA 13  ? 1.6627 0.5490 0.9529 -0.0007 -0.2070 0.0256  13  ILE   b C   
47847 O  O   . ILE   BA 13  ? 1.5905 0.6315 0.9125 0.0032  -0.2320 -0.0010 13  ILE   b O   
47848 C  CB  . ILE   BA 13  ? 1.6991 0.4934 0.9821 0.0107  -0.1681 0.0878  13  ILE   b CB  
47849 C  CG1 . ILE   BA 13  ? 1.7311 0.5158 0.9879 0.0194  -0.1637 0.1052  13  ILE   b CG1 
47850 C  CG2 . ILE   BA 13  ? 1.6816 0.5019 1.0174 0.0001  -0.1473 0.0642  13  ILE   b CG2 
47851 C  CD1 . ILE   BA 13  ? 1.7492 0.5115 0.9618 0.0294  -0.1734 0.1179  13  ILE   b CD1 
47852 N  N   . LEU   BA 14  ? 1.6761 0.5926 0.9836 0.0071  -0.2240 0.0119  14  LEU   b N   
47853 C  CA  . LEU   BA 14  ? 1.6878 0.6388 0.9774 0.0294  -0.2271 0.0120  14  LEU   b CA  
47854 C  C   . LEU   BA 14  ? 1.6957 0.6788 0.9664 0.0415  -0.2081 -0.0213 14  LEU   b C   
47855 O  O   . LEU   BA 14  ? 1.7079 0.6588 0.9925 0.0171  -0.2080 0.0134  14  LEU   b O   
47856 C  CB  . LEU   BA 14  ? 1.6659 0.6745 0.9879 0.0136  -0.2426 0.0025  14  LEU   b CB  
47857 C  CG  . LEU   BA 14  ? 1.6367 0.7305 1.0184 0.0291  -0.2497 0.0097  14  LEU   b CG  
47858 C  CD1 . LEU   BA 14  ? 1.6726 0.7829 1.0179 0.0249  -0.2607 0.0302  14  LEU   b CD1 
47859 C  CD2 . LEU   BA 14  ? 1.6185 0.7293 1.0353 0.0063  -0.2421 -0.0049 14  LEU   b CD2 
47860 N  N   . GLY   BA 15  ? 1.7550 0.6529 0.9236 0.0434  -0.1987 -0.0734 15  GLY   b N   
47861 C  CA  . GLY   BA 15  ? 1.7526 0.6611 0.8520 0.0515  -0.2035 -0.0815 15  GLY   b CA  
47862 C  C   . GLY   BA 15  ? 1.7045 0.6462 0.8191 0.0715  -0.2077 -0.1195 15  GLY   b C   
47863 O  O   . GLY   BA 15  ? 1.6816 0.6097 0.6966 0.1039  -0.2548 -0.1512 15  GLY   b O   
47864 N  N   . ALA   BA 16  ? 1.6823 0.7376 0.8454 0.0618  -0.1886 -0.1229 16  ALA   b N   
47865 C  CA  . ALA   BA 16  ? 1.7044 0.7815 0.8621 0.0521  -0.1594 -0.0840 16  ALA   b CA  
47866 C  C   . ALA   BA 16  ? 1.6910 0.7532 0.8832 0.0331  -0.1371 -0.0714 16  ALA   b C   
47867 O  O   . ALA   BA 16  ? 1.6395 0.8037 0.8749 0.0032  -0.1604 -0.0769 16  ALA   b O   
47868 C  CB  . ALA   BA 16  ? 1.7103 0.7366 0.9027 0.0463  -0.1408 -0.0853 16  ALA   b CB  
47869 N  N   . ASP   BA 17  ? 1.7129 0.6392 0.9830 0.0364  -0.1304 -0.0808 17  ASP   b N   
47870 C  CA  . ASP   BA 17  ? 1.7061 0.6619 1.0785 0.0371  -0.0834 -0.0844 17  ASP   b CA  
47871 C  C   . ASP   BA 17  ? 1.6396 0.6793 1.1726 -0.0233 -0.0728 -0.0278 17  ASP   b C   
47872 O  O   . ASP   BA 17  ? 1.5974 0.7116 1.2248 0.0022  -0.0515 -0.0290 17  ASP   b O   
47873 C  CB  . ASP   BA 17  ? 1.7817 0.6774 1.0872 0.0218  -0.0779 -0.0759 17  ASP   b CB  
47874 C  CG  . ASP   BA 17  ? 1.8333 0.6806 1.0818 0.0258  -0.0811 -0.0472 17  ASP   b CG  
47875 O  OD1 . ASP   BA 17  ? 1.8315 0.7356 1.1956 0.0742  -0.0573 -0.0412 17  ASP   b OD1 
47876 O  OD2 . ASP   BA 17  ? 1.8840 0.6196 1.0960 0.0323  -0.1005 -0.0800 17  ASP   b OD2 
47877 N  N   . SER   BA 18  ? 1.6322 0.5549 1.1968 -0.0123 -0.0361 -0.0521 18  SER   b N   
47878 C  CA  . SER   BA 18  ? 1.6321 0.5017 1.2270 0.0180  -0.0506 -0.0608 18  SER   b CA  
47879 C  C   . SER   BA 18  ? 1.5919 0.4702 1.2192 0.0255  -0.0441 -0.0850 18  SER   b C   
47880 O  O   . SER   BA 18  ? 1.6097 0.3519 1.1887 -0.0010 -0.0096 -0.1493 18  SER   b O   
47881 C  CB  . SER   BA 18  ? 1.6614 0.5169 1.2276 0.0559  -0.0245 -0.0525 18  SER   b CB  
47882 O  OG  . SER   BA 18  ? 1.7382 0.4860 1.2525 0.0748  -0.0534 -0.0289 18  SER   b OG  
47883 N  N   . ARG   BA 19  ? 1.5718 0.5569 1.2507 0.0149  -0.0236 -0.0393 19  ARG   b N   
47884 C  CA  . ARG   BA 19  ? 1.5723 0.6923 1.2240 0.0559  -0.0776 -0.0445 19  ARG   b CA  
47885 C  C   . ARG   BA 19  ? 1.5751 0.6400 1.1507 0.0297  -0.1334 -0.0687 19  ARG   b C   
47886 O  O   . ARG   BA 19  ? 1.5748 0.6593 1.1238 0.0304  -0.0712 -0.0972 19  ARG   b O   
47887 C  CB  . ARG   BA 19  ? 1.5872 0.7005 1.2708 0.0442  -0.1458 -0.0397 19  ARG   b CB  
47888 C  CG  . ARG   BA 19  ? 1.5530 0.7798 1.2545 0.0865  -0.2120 -0.0265 19  ARG   b CG  
47889 C  CD  . ARG   BA 19  ? 1.5248 0.8079 1.2338 0.1252  -0.2334 -0.0816 19  ARG   b CD  
47890 N  NE  . ARG   BA 19  ? 1.5156 0.8835 1.2045 0.1485  -0.2691 -0.1288 19  ARG   b NE  
47891 C  CZ  . ARG   BA 19  ? 1.4852 0.9428 1.1707 0.1385  -0.2771 -0.1850 19  ARG   b CZ  
47892 N  NH1 . ARG   BA 19  ? 1.5053 0.9458 1.1925 0.1340  -0.2779 -0.1598 19  ARG   b NH1 
47893 N  NH2 . ARG   BA 19  ? 1.4519 1.0185 1.1654 0.1148  -0.2865 -0.1840 19  ARG   b NH2 
47894 N  N   . THR   BA 20  ? 1.5414 0.6252 1.1284 0.0130  -0.1149 -0.0419 20  THR   b N   
47895 C  CA  . THR   BA 20  ? 1.5231 0.6150 1.1447 0.0031  -0.0871 -0.0169 20  THR   b CA  
47896 C  C   . THR   BA 20  ? 1.5507 0.5946 1.1379 0.0012  -0.0642 0.0009  20  THR   b C   
47897 O  O   . THR   BA 20  ? 1.5507 0.5518 1.1593 0.0069  -0.0662 0.0053  20  THR   b O   
47898 C  CB  . THR   BA 20  ? 1.5278 0.6383 1.1351 -0.0118 -0.0559 -0.0486 20  THR   b CB  
47899 O  OG1 . THR   BA 20  ? 1.4812 0.5189 1.1567 -0.0493 -0.0547 -0.0834 20  THR   b OG1 
47900 C  CG2 . THR   BA 20  ? 1.5310 0.6999 1.1675 0.0003  -0.0806 -0.0359 20  THR   b CG2 
47901 N  N   . THR   BA 21  ? 1.5542 0.5548 1.0900 0.0437  -0.0803 0.0215  21  THR   b N   
47902 C  CA  . THR   BA 21  ? 1.5591 0.5816 1.1128 0.0388  -0.0741 0.0605  21  THR   b CA  
47903 C  C   . THR   BA 21  ? 1.5642 0.5106 1.1125 0.0616  -0.0708 0.1096  21  THR   b C   
47904 O  O   . THR   BA 21  ? 1.5669 0.4844 1.1931 0.0305  -0.0233 0.1006  21  THR   b O   
47905 C  CB  . THR   BA 21  ? 1.5254 0.5990 1.0791 0.0153  -0.0924 0.0770  21  THR   b CB  
47906 O  OG1 . THR   BA 21  ? 1.5153 0.5685 1.0115 0.0257  -0.1015 0.0824  21  THR   b OG1 
47907 C  CG2 . THR   BA 21  ? 1.5486 0.6178 1.0814 0.0093  -0.0942 0.0616  21  THR   b CG2 
47908 N  N   . THR   BA 22  ? 1.5956 0.5181 1.1578 0.0789  -0.0803 0.1535  22  THR   b N   
47909 C  CA  . THR   BA 22  ? 1.6419 0.6217 1.1449 0.0907  -0.1463 0.1815  22  THR   b CA  
47910 C  C   . THR   BA 22  ? 1.6503 0.6323 1.1806 0.1027  -0.1561 0.2165  22  THR   b C   
47911 O  O   . THR   BA 22  ? 1.7028 0.6943 1.1964 0.1754  -0.1805 0.2339  22  THR   b O   
47912 C  CB  . THR   BA 22  ? 1.6746 0.5876 1.1385 0.0793  -0.1740 0.2147  22  THR   b CB  
47913 O  OG1 . THR   BA 22  ? 1.6841 0.6107 1.1636 0.0501  -0.1810 0.2576  22  THR   b OG1 
47914 C  CG2 . THR   BA 22  ? 1.6977 0.6265 1.1278 0.0871  -0.2011 0.2090  22  THR   b CG2 
47915 N  N   . GLY   BA 23  ? 1.6493 0.6958 1.1674 0.0819  -0.1649 0.2354  23  GLY   b N   
47916 C  CA  . GLY   BA 23  ? 1.6328 0.6963 1.1368 0.0972  -0.1629 0.2123  23  GLY   b CA  
47917 C  C   . GLY   BA 23  ? 1.6231 0.7167 1.1314 0.0984  -0.1920 0.1979  23  GLY   b C   
47918 O  O   . GLY   BA 23  ? 1.5909 0.7877 1.1122 0.0974  -0.1935 0.1770  23  GLY   b O   
47919 N  N   . ALA   BA 24  ? 1.6533 0.6964 1.1382 0.0931  -0.1543 0.1635  24  ALA   b N   
47920 C  CA  . ALA   BA 24  ? 1.6836 0.6782 1.1287 0.0993  -0.1454 0.1756  24  ALA   b CA  
47921 C  C   . ALA   BA 24  ? 1.6727 0.6569 1.0980 0.1108  -0.1628 0.1632  24  ALA   b C   
47922 O  O   . ALA   BA 24  ? 1.7242 0.5286 1.0718 0.1694  -0.2198 0.1684  24  ALA   b O   
47923 C  CB  . ALA   BA 24  ? 1.6888 0.6787 1.1486 0.0998  -0.1215 0.1713  24  ALA   b CB  
47924 N  N   . TYR   BA 25  ? 1.6709 0.6778 1.0973 0.1011  -0.1612 0.1568  25  TYR   b N   
47925 C  CA  . TYR   BA 25  ? 1.6670 0.6887 1.1055 0.0990  -0.1492 0.1634  25  TYR   b CA  
47926 C  C   . TYR   BA 25  ? 1.6905 0.6851 1.1179 0.0721  -0.1117 0.1918  25  TYR   b C   
47927 O  O   . TYR   BA 25  ? 1.6786 0.7332 1.1694 0.0766  -0.0690 0.2573  25  TYR   b O   
47928 C  CB  . TYR   BA 25  ? 1.6412 0.6842 1.1027 0.1009  -0.1541 0.1784  25  TYR   b CB  
47929 C  CG  . TYR   BA 25  ? 1.6165 0.7109 1.0682 0.0908  -0.1781 0.1320  25  TYR   b CG  
47930 C  CD1 . TYR   BA 25  ? 1.6084 0.7442 1.0877 0.1047  -0.1773 0.1399  25  TYR   b CD1 
47931 C  CD2 . TYR   BA 25  ? 1.6153 0.7598 1.0151 0.0687  -0.2028 0.0743  25  TYR   b CD2 
47932 C  CE1 . TYR   BA 25  ? 1.5943 0.7636 1.0818 0.0955  -0.1846 0.0969  25  TYR   b CE1 
47933 C  CE2 . TYR   BA 25  ? 1.6071 0.7822 1.0204 0.0693  -0.1930 0.0587  25  TYR   b CE2 
47934 C  CZ  . TYR   BA 25  ? 1.5907 0.7863 1.0539 0.0825  -0.1940 0.0685  25  TYR   b CZ  
47935 O  OH  . TYR   BA 25  ? 1.5646 0.7839 1.0437 0.0997  -0.1982 0.0682  25  TYR   b OH  
47936 N  N   . ILE   BA 26  ? 1.6855 0.7458 1.1066 0.0823  -0.0928 0.1427  26  ILE   b N   
47937 C  CA  . ILE   BA 26  ? 1.6907 0.7810 1.1141 0.0682  -0.1089 0.1705  26  ILE   b CA  
47938 C  C   . ILE   BA 26  ? 1.6948 0.8261 1.1385 0.0371  -0.1120 0.1659  26  ILE   b C   
47939 O  O   . ILE   BA 26  ? 1.6766 0.8096 1.0969 0.0462  -0.1502 0.1760  26  ILE   b O   
47940 C  CB  . ILE   BA 26  ? 1.6783 0.7789 1.1316 0.0532  -0.1017 0.1364  26  ILE   b CB  
47941 C  CG1 . ILE   BA 26  ? 1.6510 0.7354 1.1290 0.0743  -0.1079 0.1567  26  ILE   b CG1 
47942 C  CG2 . ILE   BA 26  ? 1.6835 0.8015 1.1755 0.0495  -0.0931 0.1647  26  ILE   b CG2 
47943 C  CD1 . ILE   BA 26  ? 1.6277 0.7612 1.1372 0.0687  -0.1089 0.1364  26  ILE   b CD1 
47944 N  N   . ALA   BA 27  ? 1.7165 0.8523 1.1753 0.0407  -0.0930 0.1465  27  ALA   b N   
47945 C  CA  . ALA   BA 27  ? 1.6996 0.8574 1.1970 0.0236  -0.0892 0.1705  27  ALA   b CA  
47946 C  C   . ALA   BA 27  ? 1.6519 0.7833 1.2531 0.0316  -0.0938 0.1815  27  ALA   b C   
47947 O  O   . ALA   BA 27  ? 1.6569 0.8102 1.2254 0.0042  -0.0718 0.2098  27  ALA   b O   
47948 C  CB  . ALA   BA 27  ? 1.6969 0.9416 1.1898 0.0432  -0.0956 0.1571  27  ALA   b CB  
47949 N  N   . ASN   BA 28  ? 1.6740 0.6401 1.2550 0.0577  -0.0744 0.1991  28  ASN   b N   
47950 C  CA  . ASN   BA 28  ? 1.7099 0.5991 1.2745 0.0260  -0.0413 0.1750  28  ASN   b CA  
47951 C  C   . ASN   BA 28  ? 1.7472 0.4544 1.2675 0.0373  -0.0215 0.1845  28  ASN   b C   
47952 O  O   . ASN   BA 28  ? 1.7867 0.2779 1.2320 0.0185  0.0018  0.1515  28  ASN   b O   
47953 C  CB  . ASN   BA 28  ? 1.6946 0.5746 1.3015 -0.0116 -0.0195 0.1653  28  ASN   b CB  
47954 C  CG  . ASN   BA 28  ? 1.6779 0.5190 1.3825 -0.0086 -0.0056 0.1550  28  ASN   b CG  
47955 O  OD1 . ASN   BA 28  ? 1.6874 0.5528 1.4403 -0.0596 0.0436  0.1613  28  ASN   b OD1 
47956 N  ND2 . ASN   BA 28  ? 1.6208 0.6002 1.4433 0.0620  -0.0110 0.1117  28  ASN   b ND2 
47957 N  N   . ARG   BA 29  ? 1.7379 0.4279 1.2266 0.0556  -0.0551 0.1607  29  ARG   b N   
47958 C  CA  . ARG   BA 29  ? 1.7194 0.4861 1.2678 0.0200  -0.0872 0.1375  29  ARG   b CA  
47959 C  C   . ARG   BA 29  ? 1.7190 0.5338 1.2607 0.0403  -0.1060 0.1417  29  ARG   b C   
47960 O  O   . ARG   BA 29  ? 1.7331 0.6138 1.3219 0.0318  -0.1223 0.0601  29  ARG   b O   
47961 C  CB  . ARG   BA 29  ? 1.6698 0.4728 1.2651 0.0133  -0.1113 0.1824  29  ARG   b CB  
47962 C  CG  . ARG   BA 29  ? 1.6780 0.4913 1.2918 -0.0131 -0.1210 0.1898  29  ARG   b CG  
47963 C  CD  . ARG   BA 29  ? 1.6904 0.4637 1.2852 -0.0377 -0.1142 0.1694  29  ARG   b CD  
47964 N  NE  . ARG   BA 29  ? 1.6926 0.4728 1.2914 -0.0455 -0.1164 0.1636  29  ARG   b NE  
47965 C  CZ  . ARG   BA 29  ? 1.6799 0.5529 1.2966 -0.0624 -0.1089 0.1484  29  ARG   b CZ  
47966 N  NH1 . ARG   BA 29  ? 1.7006 0.5522 1.3042 -0.0723 -0.1065 0.1185  29  ARG   b NH1 
47967 N  NH2 . ARG   BA 29  ? 1.6590 0.6477 1.3177 -0.0519 -0.1237 0.1632  29  ARG   b NH2 
47968 N  N   . VAL   BA 30  ? 1.6727 0.5316 1.2709 0.0325  -0.1192 0.1509  30  VAL   b N   
47969 C  CA  . VAL   BA 30  ? 1.6640 0.4996 1.3028 0.0172  -0.1348 0.1508  30  VAL   b CA  
47970 C  C   . VAL   BA 30  ? 1.6130 0.5361 1.3229 -0.0231 -0.1263 0.0939  30  VAL   b C   
47971 O  O   . VAL   BA 30  ? 1.5508 0.5882 1.3528 -0.0692 -0.0802 0.1377  30  VAL   b O   
47972 C  CB  . VAL   BA 30  ? 1.6494 0.4806 1.2994 0.0696  -0.1428 0.1967  30  VAL   b CB  
47973 C  CG1 . VAL   BA 30  ? 1.6689 0.4956 1.3062 0.0926  -0.1424 0.2022  30  VAL   b CG1 
47974 C  CG2 . VAL   BA 30  ? 1.6615 0.4876 1.3013 0.1120  -0.1823 0.2276  30  VAL   b CG2 
47975 N  N   . THR   BA 31  ? 1.6431 0.4628 1.3431 -0.0631 -0.1229 0.0647  31  THR   b N   
47976 C  CA  . THR   BA 31  ? 1.7382 0.4162 1.4177 -0.0553 -0.1273 0.0133  31  THR   b CA  
47977 C  C   . THR   BA 31  ? 1.7885 0.4850 1.4294 -0.0546 -0.1200 0.0481  31  THR   b C   
47978 O  O   . THR   BA 31  ? 1.9170 0.2929 1.5773 -0.0667 0.0504  -0.0762 31  THR   b O   
47979 C  CB  . THR   BA 31  ? 1.7289 0.3445 1.3936 -0.0310 -0.1530 0.0250  31  THR   b CB  
47980 O  OG1 . THR   BA 31  ? 1.8185 0.3621 1.4169 -0.0048 -0.1436 0.0565  31  THR   b OG1 
47981 C  CG2 . THR   BA 31  ? 1.6587 0.4174 1.3916 -0.0118 -0.1478 0.0334  31  THR   b CG2 
47982 N  N   . ASP   BA 32  ? 1.7935 0.4520 1.5342 -0.0566 -0.1107 0.1224  32  ASP   b N   
47983 C  CA  . ASP   BA 32  ? 1.7895 0.5725 1.5358 -0.0751 -0.1524 0.1547  32  ASP   b CA  
47984 C  C   . ASP   BA 32  ? 1.7528 0.5663 1.5023 -0.1003 -0.1960 0.1257  32  ASP   b C   
47985 O  O   . ASP   BA 32  ? 1.8525 0.7849 1.4347 -0.1630 -0.2100 0.0560  32  ASP   b O   
47986 C  CB  . ASP   BA 32  ? 1.7862 0.6260 1.5833 -0.1229 -0.1703 0.1772  32  ASP   b CB  
47987 C  CG  . ASP   BA 32  ? 1.8062 0.6885 1.6309 -0.1252 -0.1914 0.2255  32  ASP   b CG  
47988 O  OD1 . ASP   BA 32  ? 1.8089 0.6169 1.6041 -0.0838 -0.1544 0.1426  32  ASP   b OD1 
47989 O  OD2 . ASP   BA 32  ? 1.8264 0.6916 1.7469 -0.1095 -0.2575 0.3924  32  ASP   b OD2 
47990 N  N   . LYS   BA 33  ? 1.6912 0.6437 1.4330 -0.0675 -0.2581 0.1424  33  LYS   b N   
47991 C  CA  . LYS   BA 33  ? 1.6837 0.5685 1.3762 -0.0390 -0.2729 0.1012  33  LYS   b CA  
47992 C  C   . LYS   BA 33  ? 1.7159 0.4037 1.3982 -0.0157 -0.2170 0.0465  33  LYS   b C   
47993 O  O   . LYS   BA 33  ? 1.7546 0.2651 1.4152 0.0141  -0.1533 -0.0299 33  LYS   b O   
47994 C  CB  . LYS   BA 33  ? 1.6443 0.5906 1.3549 -0.0586 -0.2973 0.1077  33  LYS   b CB  
47995 C  CG  . LYS   BA 33  ? 1.6268 0.6196 1.3403 -0.0258 -0.2791 0.0855  33  LYS   b CG  
47996 C  CD  . LYS   BA 33  ? 1.6218 0.6169 1.3177 -0.0183 -0.2378 0.0776  33  LYS   b CD  
47997 C  CE  . LYS   BA 33  ? 1.6236 0.6367 1.3296 0.0198  -0.2055 0.0818  33  LYS   b CE  
47998 N  NZ  . LYS   BA 33  ? 1.6340 0.6393 1.2955 0.0273  -0.1896 0.0468  33  LYS   b NZ  
47999 N  N   . LEU   BA 34  ? 1.7389 0.3921 1.4163 -0.0123 -0.2127 0.0616  34  LEU   b N   
48000 C  CA  . LEU   BA 34  ? 1.7495 0.4866 1.4085 -0.0108 -0.1951 0.1548  34  LEU   b CA  
48001 C  C   . LEU   BA 34  ? 1.7482 0.4419 1.4675 -0.0019 -0.1820 0.1828  34  LEU   b C   
48002 O  O   . LEU   BA 34  ? 1.7514 0.3778 1.6355 0.0322  -0.0911 0.2771  34  LEU   b O   
48003 C  CB  . LEU   BA 34  ? 1.7481 0.4967 1.4013 -0.0044 -0.2010 0.1602  34  LEU   b CB  
48004 C  CG  . LEU   BA 34  ? 1.7326 0.5121 1.3836 0.0030  -0.1807 0.1483  34  LEU   b CG  
48005 C  CD1 . LEU   BA 34  ? 1.7320 0.5771 1.3978 -0.0009 -0.1557 0.1640  34  LEU   b CD1 
48006 C  CD2 . LEU   BA 34  ? 1.7239 0.5545 1.4066 0.0153  -0.2007 0.1301  34  LEU   b CD2 
48007 N  N   . THR   BA 35  ? 1.6928 0.5839 1.3729 -0.0053 -0.1970 0.1643  35  THR   b N   
48008 C  CA  . THR   BA 35  ? 1.6667 0.6442 1.2847 -0.0429 -0.2736 0.1801  35  THR   b CA  
48009 C  C   . THR   BA 35  ? 1.6762 0.6207 1.2575 -0.0546 -0.2804 0.1856  35  THR   b C   
48010 O  O   . THR   BA 35  ? 1.6210 0.4434 1.2554 0.0971  -0.2785 0.2774  35  THR   b O   
48011 C  CB  . THR   BA 35  ? 1.6899 0.7208 1.2786 -0.1070 -0.2938 0.1734  35  THR   b CB  
48012 O  OG1 . THR   BA 35  ? 1.7088 0.7779 1.2897 -0.1500 -0.3015 0.1838  35  THR   b OG1 
48013 C  CG2 . THR   BA 35  ? 1.7152 0.6381 1.2389 -0.1432 -0.2952 0.1863  35  THR   b CG2 
48014 N  N   . ARG   BA 36  ? 1.6521 0.6323 1.2675 -0.0618 -0.3325 0.1373  36  ARG   b N   
48015 C  CA  . ARG   BA 36  ? 1.7147 0.6119 1.3397 -0.0383 -0.3615 0.1004  36  ARG   b CA  
48016 C  C   . ARG   BA 36  ? 1.6978 0.5726 1.3308 -0.0359 -0.3460 0.1300  36  ARG   b C   
48017 O  O   . ARG   BA 36  ? 1.7281 0.5861 1.2941 0.0392  -0.3603 0.1788  36  ARG   b O   
48018 C  CB  . ARG   BA 36  ? 1.7642 0.6986 1.4106 -0.0808 -0.3486 0.1114  36  ARG   b CB  
48019 C  CG  . ARG   BA 36  ? 1.8280 0.7544 1.4847 -0.0525 -0.4261 0.1242  36  ARG   b CG  
48020 C  CD  . ARG   BA 36  ? 1.8868 0.8154 1.6362 -0.1108 -0.4258 0.0785  36  ARG   b CD  
48021 N  NE  . ARG   BA 36  ? 1.9400 0.8012 1.6779 -0.0756 -0.4600 0.0570  36  ARG   b NE  
48022 C  CZ  . ARG   BA 36  ? 1.9219 0.8550 1.6935 -0.0048 -0.4894 0.0753  36  ARG   b CZ  
48023 N  NH1 . ARG   BA 36  ? 1.9365 0.9115 1.6924 -0.0818 -0.4994 0.0875  36  ARG   b NH1 
48024 N  NH2 . ARG   BA 36  ? 1.9213 0.9663 1.5955 0.0374  -0.5060 0.1003  36  ARG   b NH2 
48025 N  N   . VAL   BA 37  ? 1.6945 0.5408 1.2920 -0.0497 -0.3451 0.1299  37  VAL   b N   
48026 C  CA  . VAL   BA 37  ? 1.7415 0.5777 1.2680 -0.0448 -0.3341 0.1364  37  VAL   b CA  
48027 C  C   . VAL   BA 37  ? 1.8326 0.5914 1.2500 -0.0577 -0.3436 0.1576  37  VAL   b C   
48028 O  O   . VAL   BA 37  ? 1.9107 0.4892 1.1912 -0.0576 -0.4054 0.2313  37  VAL   b O   
48029 C  CB  . VAL   BA 37  ? 1.7529 0.5295 1.2383 -0.0503 -0.3412 0.1371  37  VAL   b CB  
48030 C  CG1 . VAL   BA 37  ? 1.7371 0.4993 1.2231 -0.0656 -0.3340 0.1044  37  VAL   b CG1 
48031 C  CG2 . VAL   BA 37  ? 1.7415 0.5767 1.2316 -0.0503 -0.3360 0.1411  37  VAL   b CG2 
48032 N  N   . HIS   BA 38  ? 1.8420 0.5487 1.2522 -0.0594 -0.3024 0.1705  38  HIS   b N   
48033 C  CA  . HIS   BA 38  ? 1.8211 0.5480 1.3365 -0.0516 -0.2919 0.1930  38  HIS   b CA  
48034 C  C   . HIS   BA 38  ? 1.8316 0.5114 1.3997 -0.0809 -0.2224 0.1530  38  HIS   b C   
48035 O  O   . HIS   BA 38  ? 1.8693 0.4923 1.5224 -0.0624 -0.1899 0.1850  38  HIS   b O   
48036 C  CB  . HIS   BA 38  ? 1.8236 0.6249 1.3380 -0.0305 -0.3418 0.2363  38  HIS   b CB  
48037 C  CG  . HIS   BA 38  ? 1.7876 0.6615 1.2976 -0.0213 -0.3893 0.3416  38  HIS   b CG  
48038 N  ND1 . HIS   BA 38  ? 1.7720 0.6545 1.2877 -0.0245 -0.4081 0.3557  38  HIS   b ND1 
48039 C  CD2 . HIS   BA 38  ? 1.8385 0.6541 1.3142 -0.0486 -0.2932 0.4757  38  HIS   b CD2 
48040 C  CE1 . HIS   BA 38  ? 1.7723 0.6921 1.2330 -0.0330 -0.3767 0.4135  38  HIS   b CE1 
48041 N  NE2 . HIS   BA 38  ? 1.8017 0.6828 1.2079 -0.0351 -0.3590 0.4321  38  HIS   b NE2 
48042 N  N   . ASP   BA 39  ? 1.8249 0.6077 1.3473 -0.1333 -0.1709 0.1822  39  ASP   b N   
48043 C  CA  . ASP   BA 39  ? 1.8373 0.6292 1.3516 -0.1505 -0.1648 0.1757  39  ASP   b CA  
48044 C  C   . ASP   BA 39  ? 1.7969 0.5783 1.2985 -0.1150 -0.1601 0.2064  39  ASP   b C   
48045 O  O   . ASP   BA 39  ? 1.8534 0.3273 1.2742 -0.1416 -0.1661 0.3002  39  ASP   b O   
48046 C  CB  . ASP   BA 39  ? 1.8745 0.6600 1.4295 -0.1073 -0.1298 0.2178  39  ASP   b CB  
48047 C  CG  . ASP   BA 39  ? 1.9069 0.7106 1.4780 -0.1638 -0.1111 0.2086  39  ASP   b CG  
48048 O  OD1 . ASP   BA 39  ? 2.0080 0.8311 1.5632 -0.1604 -0.0470 0.3174  39  ASP   b OD1 
48049 O  OD2 . ASP   BA 39  ? 1.8990 0.7790 1.4792 -0.0937 -0.1689 0.2188  39  ASP   b OD2 
48050 N  N   . LYS   BA 40  ? 1.8019 0.5599 1.2332 -0.1388 -0.1997 0.1437  40  LYS   b N   
48051 C  CA  . LYS   BA 40  ? 1.8168 0.5220 1.2046 -0.0673 -0.1901 0.0934  40  LYS   b CA  
48052 C  C   . LYS   BA 40  ? 1.7538 0.4511 1.1364 -0.0161 -0.2121 0.0586  40  LYS   b C   
48053 O  O   . LYS   BA 40  ? 1.7492 0.4956 1.1598 0.0362  -0.2541 0.0244  40  LYS   b O   
48054 C  CB  . LYS   BA 40  ? 1.8540 0.5375 1.1673 -0.1169 -0.2239 0.0689  40  LYS   b CB  
48055 C  CG  . LYS   BA 40  ? 1.8887 0.6123 1.1851 -0.1421 -0.2062 0.0404  40  LYS   b CG  
48056 C  CD  . LYS   BA 40  ? 1.9433 0.6432 1.1784 -0.1913 -0.2172 0.0571  40  LYS   b CD  
48057 C  CE  . LYS   BA 40  ? 1.9775 0.7098 1.2035 -0.1981 -0.1924 0.0524  40  LYS   b CE  
48058 N  NZ  . LYS   BA 40  ? 2.0459 0.7127 1.2641 -0.1431 -0.2380 0.0738  40  LYS   b NZ  
48059 N  N   . ILE   BA 41  ? 1.6994 0.4564 1.1429 0.0100  -0.2365 0.0683  41  ILE   b N   
48060 C  CA  . ILE   BA 41  ? 1.6652 0.4956 1.1338 -0.0107 -0.2587 0.0766  41  ILE   b CA  
48061 C  C   . ILE   BA 41  ? 1.6554 0.4115 1.1024 -0.0242 -0.2352 0.0670  41  ILE   b C   
48062 O  O   . ILE   BA 41  ? 1.5947 0.3652 1.1143 -0.0099 -0.2246 0.0975  41  ILE   b O   
48063 C  CB  . ILE   BA 41  ? 1.6406 0.5402 1.1488 -0.0085 -0.2269 0.1247  41  ILE   b CB  
48064 C  CG1 . ILE   BA 41  ? 1.6748 0.5424 1.2094 0.0179  -0.2082 0.1659  41  ILE   b CG1 
48065 C  CG2 . ILE   BA 41  ? 1.6216 0.5410 1.1318 -0.0390 -0.2373 0.1013  41  ILE   b CG2 
48066 C  CD1 . ILE   BA 41  ? 1.6800 0.5634 1.2065 0.0194  -0.2030 0.1588  41  ILE   b CD1 
48067 N  N   . TRP   BA 42  ? 1.6498 0.4149 1.0515 -0.0205 -0.2798 0.0646  42  TRP   b N   
48068 C  CA  . TRP   BA 42  ? 1.6499 0.4477 1.0526 -0.0023 -0.3120 0.0267  42  TRP   b CA  
48069 C  C   . TRP   BA 42  ? 1.6808 0.3882 1.0620 0.0182  -0.3060 0.0194  42  TRP   b C   
48070 O  O   . TRP   BA 42  ? 1.6765 0.2828 1.0365 0.0742  -0.3102 0.0025  42  TRP   b O   
48071 C  CB  . TRP   BA 42  ? 1.6329 0.4498 1.0495 -0.0252 -0.3018 0.0376  42  TRP   b CB  
48072 C  CG  . TRP   BA 42  ? 1.6396 0.3991 1.0803 -0.0226 -0.3337 0.0639  42  TRP   b CG  
48073 C  CD1 . TRP   BA 42  ? 1.6763 0.3548 1.1622 -0.0467 -0.3261 0.0578  42  TRP   b CD1 
48074 C  CD2 . TRP   BA 42  ? 1.6263 0.4119 1.0942 -0.0491 -0.3512 0.0901  42  TRP   b CD2 
48075 N  NE1 . TRP   BA 42  ? 1.6396 0.3970 1.1985 -0.0316 -0.3437 0.0514  42  TRP   b NE1 
48076 C  CE2 . TRP   BA 42  ? 1.6477 0.3702 1.1455 -0.0483 -0.3559 0.0816  42  TRP   b CE2 
48077 C  CE3 . TRP   BA 42  ? 1.6092 0.4750 1.1470 -0.0208 -0.3482 0.1008  42  TRP   b CE3 
48078 C  CZ2 . TRP   BA 42  ? 1.6445 0.4112 1.1746 -0.0384 -0.3554 0.1135  42  TRP   b CZ2 
48079 C  CZ3 . TRP   BA 42  ? 1.6279 0.4747 1.2039 -0.0539 -0.3106 0.1201  42  TRP   b CZ3 
48080 C  CH2 . TRP   BA 42  ? 1.6404 0.4341 1.2055 -0.0295 -0.3410 0.1306  42  TRP   b CH2 
48081 N  N   . CYS   BA 43  ? 1.6900 0.4125 1.1220 0.0402  -0.3002 0.0517  43  CYS   b N   
48082 C  CA  . CYS   BA 43  ? 1.6733 0.4892 1.2047 0.0057  -0.2816 0.0791  43  CYS   b CA  
48083 C  C   . CYS   BA 43  ? 1.7029 0.4384 1.2293 -0.0161 -0.2901 0.0859  43  CYS   b C   
48084 O  O   . CYS   BA 43  ? 1.7023 0.3554 1.2590 0.0052  -0.2809 0.1390  43  CYS   b O   
48085 C  CB  . CYS   BA 43  ? 1.6563 0.5617 1.2162 0.0283  -0.2743 0.0839  43  CYS   b CB  
48086 S  SG  . CYS   BA 43  ? 1.6096 0.6035 1.3199 0.0516  -0.3002 0.1908  43  CYS   b SG  
48087 N  N   . CYS   BA 44  ? 1.7252 0.4247 1.2444 -0.0153 -0.2875 0.0585  44  CYS   b N   
48088 C  CA  . CYS   BA 44  ? 1.7733 0.4111 1.2427 -0.0071 -0.2638 0.0149  44  CYS   b CA  
48089 C  C   . CYS   BA 44  ? 1.7187 0.3378 1.2236 -0.0339 -0.2812 -0.0240 44  CYS   b C   
48090 O  O   . CYS   BA 44  ? 1.7497 0.2101 1.2344 -0.0540 -0.2352 -0.0437 44  CYS   b O   
48091 C  CB  . CYS   BA 44  ? 1.8303 0.3640 1.2843 0.0015  -0.2369 -0.0136 44  CYS   b CB  
48092 S  SG  . CYS   BA 44  ? 1.9448 0.5220 1.3339 0.0240  -0.0989 0.0260  44  CYS   b SG  
48093 N  N   . ARG   BA 45  ? 1.7095 0.3832 1.1568 -0.0866 -0.2971 -0.0498 45  ARG   b N   
48094 C  CA  . ARG   BA 45  ? 1.6551 0.4981 1.1566 -0.1093 -0.3058 -0.0274 45  ARG   b CA  
48095 C  C   . ARG   BA 45  ? 1.5986 0.4978 1.0942 -0.1304 -0.2622 -0.0211 45  ARG   b C   
48096 O  O   . ARG   BA 45  ? 1.6111 0.5183 1.0517 -0.1249 -0.2595 -0.0256 45  ARG   b O   
48097 C  CB  . ARG   BA 45  ? 1.6608 0.5505 1.2347 -0.1412 -0.3254 -0.0134 45  ARG   b CB  
48098 C  CG  . ARG   BA 45  ? 1.6633 0.5479 1.2594 -0.1628 -0.3400 -0.0542 45  ARG   b CG  
48099 C  CD  . ARG   BA 45  ? 1.6818 0.5501 1.2523 -0.1803 -0.3149 -0.1026 45  ARG   b CD  
48100 N  NE  . ARG   BA 45  ? 1.6510 0.5249 1.2827 -0.2189 -0.3198 -0.1252 45  ARG   b NE  
48101 C  CZ  . ARG   BA 45  ? 1.5741 0.4810 1.2636 -0.2558 -0.2940 -0.1734 45  ARG   b CZ  
48102 N  NH1 . ARG   BA 45  ? 1.6089 0.4959 1.1812 -0.2847 -0.2858 -0.2340 45  ARG   b NH1 
48103 N  NH2 . ARG   BA 45  ? 1.5694 0.4865 1.3041 -0.3138 -0.2702 -0.1623 45  ARG   b NH2 
48104 N  N   . SER   BA 46  ? 1.5813 0.5536 1.0828 -0.0870 -0.2483 0.0154  46  SER   b N   
48105 C  CA  . SER   BA 46  ? 1.5609 0.5861 1.0612 -0.0051 -0.2346 0.0799  46  SER   b CA  
48106 C  C   . SER   BA 46  ? 1.5712 0.5504 1.0460 -0.0017 -0.2674 0.0793  46  SER   b C   
48107 O  O   . SER   BA 46  ? 1.5747 0.6005 0.9892 -0.0051 -0.2887 0.0339  46  SER   b O   
48108 C  CB  . SER   BA 46  ? 1.5316 0.5422 1.0463 0.0065  -0.2242 0.1146  46  SER   b CB  
48109 O  OG  . SER   BA 46  ? 1.5638 0.5922 1.0708 0.0062  -0.1634 0.1470  46  SER   b OG  
48110 N  N   . GLY   BA 47  ? 1.5790 0.5272 1.0704 -0.0138 -0.2570 0.0847  47  GLY   b N   
48111 C  CA  . GLY   BA 47  ? 1.5818 0.5447 1.0841 -0.0385 -0.2139 0.0943  47  GLY   b CA  
48112 C  C   . GLY   BA 47  ? 1.5653 0.5513 1.1295 -0.0807 -0.2025 0.1336  47  GLY   b C   
48113 O  O   . GLY   BA 47  ? 1.5680 0.6361 1.1591 -0.2050 -0.1671 0.1282  47  GLY   b O   
48114 N  N   . SER   BA 48  ? 1.5688 0.4977 1.1135 -0.0752 -0.1982 0.1788  48  SER   b N   
48115 C  CA  . SER   BA 48  ? 1.5937 0.5202 1.1373 -0.0797 -0.2131 0.1581  48  SER   b CA  
48116 C  C   . SER   BA 48  ? 1.5613 0.5089 1.1628 -0.0579 -0.2443 0.1817  48  SER   b C   
48117 O  O   . SER   BA 48  ? 1.5549 0.5880 1.2822 0.0059  -0.2522 0.1468  48  SER   b O   
48118 C  CB  . SER   BA 48  ? 1.6277 0.4928 1.1681 -0.1138 -0.1584 0.1456  48  SER   b CB  
48119 O  OG  . SER   BA 48  ? 1.6693 0.4412 1.2633 -0.1840 -0.0896 0.1334  48  SER   b OG  
48120 N  N   . ALA   BA 49  ? 1.5454 0.5126 1.1611 -0.0024 -0.2986 0.1726  49  ALA   b N   
48121 C  CA  . ALA   BA 49  ? 1.5423 0.4913 1.2010 0.0014  -0.3188 0.1874  49  ALA   b CA  
48122 C  C   . ALA   BA 49  ? 1.5605 0.5940 1.1638 -0.0159 -0.3409 0.1339  49  ALA   b C   
48123 O  O   . ALA   BA 49  ? 1.5533 0.5871 1.2594 0.0179  -0.4108 0.1115  49  ALA   b O   
48124 C  CB  . ALA   BA 49  ? 1.5480 0.4260 1.1976 -0.0001 -0.3167 0.1918  49  ALA   b CB  
48125 N  N   . ALA   BA 50  ? 1.5815 0.5620 1.1523 -0.0165 -0.3243 0.1473  50  ALA   b N   
48126 C  CA  . ALA   BA 50  ? 1.5879 0.5322 1.2193 -0.0253 -0.3084 0.1283  50  ALA   b CA  
48127 C  C   . ALA   BA 50  ? 1.5435 0.6047 1.2320 -0.0391 -0.2779 0.0553  50  ALA   b C   
48128 O  O   . ALA   BA 50  ? 1.6072 0.6131 1.3933 0.0090  -0.2134 0.0736  50  ALA   b O   
48129 C  CB  . ALA   BA 50  ? 1.6069 0.6212 1.1913 -0.0497 -0.3190 0.0972  50  ALA   b CB  
48130 N  N   . ASP   BA 51  ? 1.5418 0.5114 1.1802 -0.0163 -0.2837 -0.0093 51  ASP   b N   
48131 C  CA  . ASP   BA 51  ? 1.5437 0.5228 1.1777 -0.0109 -0.2857 -0.0525 51  ASP   b CA  
48132 C  C   . ASP   BA 51  ? 1.5326 0.6180 1.1546 -0.0304 -0.2766 -0.0447 51  ASP   b C   
48133 O  O   . ASP   BA 51  ? 1.5241 0.6361 1.1393 -0.0253 -0.2886 -0.0894 51  ASP   b O   
48134 C  CB  . ASP   BA 51  ? 1.5270 0.5373 1.1922 -0.0078 -0.2759 -0.0726 51  ASP   b CB  
48135 C  CG  . ASP   BA 51  ? 1.5552 0.5412 1.1770 0.0076  -0.2918 -0.1035 51  ASP   b CG  
48136 O  OD1 . ASP   BA 51  ? 1.5859 0.4826 1.2264 0.0254  -0.2906 -0.1320 51  ASP   b OD1 
48137 O  OD2 . ASP   BA 51  ? 1.5186 0.5837 1.3087 -0.0401 -0.2845 -0.1276 51  ASP   b OD2 
48138 N  N   . THR   BA 52  ? 1.5331 0.5560 1.1557 0.0212  -0.2616 -0.0096 52  THR   b N   
48139 C  CA  . THR   BA 52  ? 1.5395 0.6076 1.1710 0.0046  -0.3264 -0.0112 52  THR   b CA  
48140 C  C   . THR   BA 52  ? 1.6228 0.5734 1.2025 0.0003  -0.3168 -0.0046 52  THR   b C   
48141 O  O   . THR   BA 52  ? 1.6820 0.5564 1.2219 -0.0198 -0.3406 0.0148  52  THR   b O   
48142 C  CB  . THR   BA 52  ? 1.5100 0.5964 1.1575 -0.0324 -0.3938 -0.0149 52  THR   b CB  
48143 O  OG1 . THR   BA 52  ? 1.5139 0.6573 1.1502 -0.0341 -0.4464 0.0089  52  THR   b OG1 
48144 C  CG2 . THR   BA 52  ? 1.4574 0.6247 1.1316 -0.0181 -0.3991 0.0312  52  THR   b CG2 
48145 N  N   . GLN   BA 53  ? 1.6192 0.5564 1.1765 -0.0469 -0.3088 -0.0444 53  GLN   b N   
48146 C  CA  . GLN   BA 53  ? 1.6248 0.5782 1.1825 -0.0528 -0.2880 -0.0117 53  GLN   b CA  
48147 C  C   . GLN   BA 53  ? 1.6617 0.5432 1.1572 -0.0549 -0.2855 0.0205  53  GLN   b C   
48148 O  O   . GLN   BA 53  ? 1.6876 0.4983 1.2787 -0.0788 -0.2936 0.0082  53  GLN   b O   
48149 C  CB  . GLN   BA 53  ? 1.6210 0.6145 1.1448 -0.0329 -0.2677 -0.0041 53  GLN   b CB  
48150 C  CG  . GLN   BA 53  ? 1.6555 0.6108 1.1430 -0.0421 -0.2490 -0.0092 53  GLN   b CG  
48151 C  CD  . GLN   BA 53  ? 1.6551 0.6158 1.1959 0.0076  -0.2073 0.0004  53  GLN   b CD  
48152 O  OE1 . GLN   BA 53  ? 1.7387 0.7739 1.1698 -0.0225 -0.1952 -0.0426 53  GLN   b OE1 
48153 N  NE2 . GLN   BA 53  ? 1.6972 0.5292 1.2413 -0.0074 -0.2069 0.0193  53  GLN   b NE2 
48154 N  N   . ALA   BA 54  ? 1.6653 0.4653 1.1176 -0.0498 -0.3107 0.0021  54  ALA   b N   
48155 C  CA  . ALA   BA 54  ? 1.6627 0.4599 1.0909 -0.0514 -0.3246 0.0040  54  ALA   b CA  
48156 C  C   . ALA   BA 54  ? 1.6636 0.5335 1.0749 -0.0414 -0.3250 0.0260  54  ALA   b C   
48157 O  O   . ALA   BA 54  ? 1.7527 0.5389 1.1423 0.0478  -0.3051 0.0832  54  ALA   b O   
48158 C  CB  . ALA   BA 54  ? 1.6774 0.3930 1.0910 -0.0724 -0.3011 -0.0311 54  ALA   b CB  
48159 N  N   . ILE   BA 55  ? 1.5942 0.5191 1.0767 -0.0203 -0.3109 0.0474  55  ILE   b N   
48160 C  CA  . ILE   BA 55  ? 1.5672 0.5455 1.0923 -0.0221 -0.2965 0.0416  55  ILE   b CA  
48161 C  C   . ILE   BA 55  ? 1.5553 0.5434 1.0923 -0.0478 -0.3035 0.0390  55  ILE   b C   
48162 O  O   . ILE   BA 55  ? 1.5208 0.5874 1.0921 -0.0291 -0.3523 0.0894  55  ILE   b O   
48163 C  CB  . ILE   BA 55  ? 1.5320 0.5473 1.0735 -0.0110 -0.2905 0.0542  55  ILE   b CB  
48164 C  CG1 . ILE   BA 55  ? 1.5401 0.5647 1.0598 0.0186  -0.2779 0.0563  55  ILE   b CG1 
48165 C  CG2 . ILE   BA 55  ? 1.5357 0.5669 1.0812 -0.0020 -0.2983 0.0412  55  ILE   b CG2 
48166 C  CD1 . ILE   BA 55  ? 1.5368 0.5918 1.0682 0.0020  -0.2732 0.0489  55  ILE   b CD1 
48167 N  N   . ALA   BA 56  ? 1.5722 0.5186 1.0959 -0.0446 -0.2943 0.0357  56  ALA   b N   
48168 C  CA  . ALA   BA 56  ? 1.5809 0.5715 1.1258 -0.0435 -0.2508 0.0500  56  ALA   b CA  
48169 C  C   . ALA   BA 56  ? 1.5852 0.6306 1.1547 -0.0812 -0.2484 -0.0039 56  ALA   b C   
48170 O  O   . ALA   BA 56  ? 1.6230 0.7008 1.1863 -0.0406 -0.2289 0.0385  56  ALA   b O   
48171 C  CB  . ALA   BA 56  ? 1.5600 0.5459 1.1436 -0.0544 -0.2375 0.0770  56  ALA   b CB  
48172 N  N   . ASP   BA 57  ? 1.5863 0.6121 1.1520 -0.0668 -0.2540 0.0099  57  ASP   b N   
48173 C  CA  . ASP   BA 57  ? 1.6395 0.5626 1.2075 -0.0418 -0.2562 0.0005  57  ASP   b CA  
48174 C  C   . ASP   BA 57  ? 1.6080 0.5129 1.1454 -0.0787 -0.2799 -0.0201 57  ASP   b C   
48175 O  O   . ASP   BA 57  ? 1.6316 0.4919 1.2511 -0.0154 -0.2872 -0.0235 57  ASP   b O   
48176 C  CB  . ASP   BA 57  ? 1.7035 0.5462 1.2234 -0.0597 -0.2907 -0.0257 57  ASP   b CB  
48177 C  CG  . ASP   BA 57  ? 1.7903 0.4558 1.2835 -0.0301 -0.2669 -0.0614 57  ASP   b CG  
48178 O  OD1 . ASP   BA 57  ? 1.8998 0.4217 1.2764 -0.0097 -0.2692 -0.1487 57  ASP   b OD1 
48179 O  OD2 . ASP   BA 57  ? 1.8932 0.2349 1.3114 -0.0206 -0.2139 -0.0063 57  ASP   b OD2 
48180 N  N   . ILE   BA 58  ? 1.6198 0.3868 1.0558 -0.0904 -0.3126 -0.0275 58  ILE   b N   
48181 C  CA  . ILE   BA 58  ? 1.6253 0.4203 1.0575 -0.1127 -0.2769 -0.0551 58  ILE   b CA  
48182 C  C   . ILE   BA 58  ? 1.6327 0.5777 1.1120 -0.1243 -0.3138 -0.0419 58  ILE   b C   
48183 O  O   . ILE   BA 58  ? 1.6974 0.6080 1.2168 -0.0822 -0.3136 -0.1174 58  ILE   b O   
48184 C  CB  . ILE   BA 58  ? 1.6214 0.4149 1.0158 -0.1118 -0.2795 -0.0820 58  ILE   b CB  
48185 C  CG1 . ILE   BA 58  ? 1.6170 0.4475 1.0114 -0.1294 -0.2770 -0.1033 58  ILE   b CG1 
48186 C  CG2 . ILE   BA 58  ? 1.6170 0.4169 0.9791 -0.1208 -0.2745 -0.0933 58  ILE   b CG2 
48187 C  CD1 . ILE   BA 58  ? 1.6244 0.4927 0.9900 -0.1276 -0.2500 -0.1015 58  ILE   b CD1 
48188 N  N   . VAL   BA 59  ? 1.6215 0.5368 1.1051 -0.1050 -0.3075 -0.0263 59  VAL   b N   
48189 C  CA  . VAL   BA 59  ? 1.6382 0.6164 1.1018 -0.0901 -0.2911 0.0410  59  VAL   b CA  
48190 C  C   . VAL   BA 59  ? 1.6204 0.6705 1.0709 -0.0959 -0.3074 0.0604  59  VAL   b C   
48191 O  O   . VAL   BA 59  ? 1.6434 0.7204 1.1769 -0.0325 -0.2717 0.0630  59  VAL   b O   
48192 C  CB  . VAL   BA 59  ? 1.6341 0.5778 1.1003 -0.1008 -0.2913 0.0789  59  VAL   b CB  
48193 C  CG1 . VAL   BA 59  ? 1.6142 0.5963 1.1106 -0.1029 -0.3002 0.0798  59  VAL   b CG1 
48194 C  CG2 . VAL   BA 59  ? 1.6352 0.5985 1.1317 -0.1174 -0.2832 0.0714  59  VAL   b CG2 
48195 N  N   . GLN   BA 60  ? 1.5958 0.6947 1.0307 -0.1048 -0.3423 0.0943  60  GLN   b N   
48196 C  CA  . GLN   BA 60  ? 1.5940 0.6813 1.0834 -0.1127 -0.3342 0.0991  60  GLN   b CA  
48197 C  C   . GLN   BA 60  ? 1.6450 0.6518 1.1181 -0.1377 -0.3255 0.1144  60  GLN   b C   
48198 O  O   . GLN   BA 60  ? 1.6420 0.4472 1.2884 -0.1988 -0.2892 0.0556  60  GLN   b O   
48199 C  CB  . GLN   BA 60  ? 1.5711 0.7772 1.0805 -0.1036 -0.3564 0.1417  60  GLN   b CB  
48200 C  CG  . GLN   BA 60  ? 1.5406 0.8312 1.1441 -0.1111 -0.3507 0.1720  60  GLN   b CG  
48201 C  CD  . GLN   BA 60  ? 1.5261 0.9127 1.1746 -0.1036 -0.4178 0.2125  60  GLN   b CD  
48202 O  OE1 . GLN   BA 60  ? 1.5643 1.0303 1.1036 -0.1226 -0.3904 0.2363  60  GLN   b OE1 
48203 N  NE2 . GLN   BA 60  ? 1.5265 0.9392 1.2487 -0.1483 -0.3601 0.2248  60  GLN   b NE2 
48204 N  N   . TYR   BA 61  ? 1.7005 0.5582 1.1139 -0.0996 -0.3082 0.0946  61  TYR   b N   
48205 C  CA  . TYR   BA 61  ? 1.7681 0.5716 1.1462 -0.0602 -0.3048 0.0714  61  TYR   b CA  
48206 C  C   . TYR   BA 61  ? 1.7761 0.6394 1.0962 -0.0448 -0.3314 0.0256  61  TYR   b C   
48207 O  O   . TYR   BA 61  ? 1.8914 0.6525 1.1796 0.0208  -0.3465 0.0286  61  TYR   b O   
48208 C  CB  . TYR   BA 61  ? 1.7488 0.5828 1.1510 -0.0468 -0.3000 0.0686  61  TYR   b CB  
48209 C  CG  . TYR   BA 61  ? 1.7860 0.6186 1.2222 -0.0125 -0.2686 0.0519  61  TYR   b CG  
48210 C  CD1 . TYR   BA 61  ? 1.7703 0.6601 1.2462 -0.0244 -0.3015 -0.0010 61  TYR   b CD1 
48211 C  CD2 . TYR   BA 61  ? 1.8447 0.5941 1.2066 -0.0044 -0.2200 0.0565  61  TYR   b CD2 
48212 C  CE1 . TYR   BA 61  ? 1.8360 0.7349 1.2391 -0.0211 -0.2812 -0.0357 61  TYR   b CE1 
48213 C  CE2 . TYR   BA 61  ? 1.9172 0.6670 1.1764 -0.0151 -0.2156 0.0100  61  TYR   b CE2 
48214 C  CZ  . TYR   BA 61  ? 1.9096 0.7282 1.2017 -0.0487 -0.2375 -0.0415 61  TYR   b CZ  
48215 O  OH  . TYR   BA 61  ? 2.0606 0.8235 1.1600 -0.0475 -0.2268 -0.1017 61  TYR   b OH  
48216 N  N   . HIS   BA 62  ? 1.8139 0.5320 1.0365 -0.0477 -0.3447 0.0016  62  HIS   b N   
48217 C  CA  . HIS   BA 62  ? 1.8416 0.5644 1.0968 -0.0083 -0.3249 -0.0225 62  HIS   b CA  
48218 C  C   . HIS   BA 62  ? 1.8639 0.5845 1.1290 -0.0106 -0.3343 0.0116  62  HIS   b C   
48219 O  O   . HIS   BA 62  ? 1.8939 0.6939 1.2344 0.0925  -0.3548 -0.0181 62  HIS   b O   
48220 C  CB  . HIS   BA 62  ? 1.8500 0.6017 1.0799 -0.0162 -0.2806 -0.0528 62  HIS   b CB  
48221 C  CG  . HIS   BA 62  ? 1.8975 0.6615 1.1135 0.0261  -0.2314 -0.1038 62  HIS   b CG  
48222 N  ND1 . HIS   BA 62  ? 1.9457 0.6710 1.2073 0.0587  -0.2074 -0.1072 62  HIS   b ND1 
48223 C  CD2 . HIS   BA 62  ? 1.8820 0.6784 1.1590 0.0572  -0.2120 -0.0655 62  HIS   b CD2 
48224 C  CE1 . HIS   BA 62  ? 1.9417 0.6973 1.2439 0.0748  -0.1443 -0.0504 62  HIS   b CE1 
48225 N  NE2 . HIS   BA 62  ? 1.9170 0.7357 1.1615 0.0523  -0.1685 -0.0264 62  HIS   b NE2 
48226 N  N   . LEU   BA 63  ? 1.8274 0.5172 1.1137 0.0231  -0.3459 0.0553  63  LEU   b N   
48227 C  CA  . LEU   BA 63  ? 1.7733 0.5494 1.1151 0.0209  -0.3722 0.0488  63  LEU   b CA  
48228 C  C   . LEU   BA 63  ? 1.7089 0.6132 1.1429 -0.0038 -0.3676 0.0385  63  LEU   b C   
48229 O  O   . LEU   BA 63  ? 1.7124 0.4676 1.1527 -0.0373 -0.3188 0.0130  63  LEU   b O   
48230 C  CB  . LEU   BA 63  ? 1.7517 0.5333 1.0863 0.0167  -0.4009 0.0611  63  LEU   b CB  
48231 C  CG  . LEU   BA 63  ? 1.6961 0.5626 1.0303 0.0164  -0.4151 0.0530  63  LEU   b CG  
48232 C  CD1 . LEU   BA 63  ? 1.6821 0.5619 1.0385 0.0322  -0.4078 0.0592  63  LEU   b CD1 
48233 C  CD2 . LEU   BA 63  ? 1.6952 0.5435 1.0466 0.0277  -0.3996 0.0339  63  LEU   b CD2 
48234 N  N   . GLU   BA 64  ? 1.6678 0.6071 1.1301 -0.0107 -0.3398 0.0997  64  GLU   b N   
48235 C  CA  . GLU   BA 64  ? 1.6731 0.5991 1.1642 -0.0042 -0.3223 0.1239  64  GLU   b CA  
48236 C  C   . GLU   BA 64  ? 1.6291 0.6473 1.1689 -0.0235 -0.3184 0.0641  64  GLU   b C   
48237 O  O   . GLU   BA 64  ? 1.6357 0.6187 1.2090 0.0036  -0.3587 0.0480  64  GLU   b O   
48238 C  CB  . GLU   BA 64  ? 1.7131 0.6141 1.1614 0.0489  -0.3338 0.1413  64  GLU   b CB  
48239 C  CG  . GLU   BA 64  ? 1.7388 0.6422 1.2115 0.0287  -0.3526 0.0996  64  GLU   b CG  
48240 C  CD  . GLU   BA 64  ? 1.7732 0.6744 1.2253 0.0821  -0.3658 0.0959  64  GLU   b CD  
48241 O  OE1 . GLU   BA 64  ? 1.8305 0.7360 1.2023 0.1074  -0.4069 0.0806  64  GLU   b OE1 
48242 O  OE2 . GLU   BA 64  ? 1.8394 0.6653 1.3037 0.0999  -0.3025 0.0991  64  GLU   b OE2 
48243 N  N   . LEU   BA 65  ? 1.6228 0.5404 1.1540 -0.0465 -0.3336 0.0919  65  LEU   b N   
48244 C  CA  . LEU   BA 65  ? 1.6409 0.5790 1.1728 -0.0310 -0.3267 0.0664  65  LEU   b CA  
48245 C  C   . LEU   BA 65  ? 1.6507 0.6743 1.1623 -0.0102 -0.3348 0.0467  65  LEU   b C   
48246 O  O   . LEU   BA 65  ? 1.6372 0.7229 1.1736 0.0458  -0.3935 -0.0024 65  LEU   b O   
48247 C  CB  . LEU   BA 65  ? 1.6522 0.5437 1.1822 -0.0319 -0.3157 0.0726  65  LEU   b CB  
48248 C  CG  . LEU   BA 65  ? 1.6937 0.5916 1.2053 -0.0146 -0.3128 0.0442  65  LEU   b CG  
48249 C  CD1 . LEU   BA 65  ? 1.7059 0.6238 1.2532 -0.0384 -0.3043 0.0543  65  LEU   b CD1 
48250 C  CD2 . LEU   BA 65  ? 1.6972 0.5684 1.1932 -0.0140 -0.3324 0.0279  65  LEU   b CD2 
48251 N  N   . TYR   BA 66  ? 1.6574 0.5649 1.1569 0.0413  -0.3061 0.0655  66  TYR   b N   
48252 C  CA  . TYR   BA 66  ? 1.6667 0.5453 1.1778 0.0771  -0.3098 0.0779  66  TYR   b CA  
48253 C  C   . TYR   BA 66  ? 1.7067 0.6409 1.1700 0.0851  -0.3399 0.1265  66  TYR   b C   
48254 O  O   . TYR   BA 66  ? 1.6882 0.7135 1.1290 0.1113  -0.3684 0.1719  66  TYR   b O   
48255 C  CB  . TYR   BA 66  ? 1.6493 0.4991 1.2043 0.1269  -0.3031 0.0708  66  TYR   b CB  
48256 C  CG  . TYR   BA 66  ? 1.6410 0.4068 1.2290 0.1498  -0.3042 0.0575  66  TYR   b CG  
48257 C  CD1 . TYR   BA 66  ? 1.6640 0.3667 1.2335 0.1654  -0.3050 0.0589  66  TYR   b CD1 
48258 C  CD2 . TYR   BA 66  ? 1.6401 0.3949 1.2429 0.1564  -0.2957 0.0503  66  TYR   b CD2 
48259 C  CE1 . TYR   BA 66  ? 1.6553 0.3801 1.2845 0.1643  -0.3098 0.0436  66  TYR   b CE1 
48260 C  CE2 . TYR   BA 66  ? 1.6387 0.3826 1.2686 0.1543  -0.3020 0.0519  66  TYR   b CE2 
48261 C  CZ  . TYR   BA 66  ? 1.6736 0.3834 1.2769 0.1545  -0.2970 0.0500  66  TYR   b CZ  
48262 O  OH  . TYR   BA 66  ? 1.6720 0.4397 1.3699 0.1295  -0.3248 0.0064  66  TYR   b OH  
48263 N  N   . THR   BA 67  ? 1.7179 0.6971 1.0917 0.0485  -0.3167 0.1767  67  THR   b N   
48264 C  CA  . THR   BA 67  ? 1.7467 0.6551 1.1127 0.0122  -0.3323 0.1909  67  THR   b CA  
48265 C  C   . THR   BA 67  ? 1.7574 0.6466 1.1763 -0.0022 -0.3411 0.2061  67  THR   b C   
48266 O  O   . THR   BA 67  ? 1.8240 0.6116 1.2669 0.0034  -0.3541 0.2278  67  THR   b O   
48267 C  CB  . THR   BA 67  ? 1.7152 0.7041 1.0541 -0.0144 -0.3210 0.2080  67  THR   b CB  
48268 O  OG1 . THR   BA 67  ? 1.7054 0.6846 0.9891 0.0082  -0.3356 0.2418  67  THR   b OG1 
48269 C  CG2 . THR   BA 67  ? 1.7237 0.7289 1.0830 -0.0304 -0.3014 0.2307  67  THR   b CG2 
48270 N  N   . SER   BA 68  ? 1.7308 0.5715 1.2043 -0.0202 -0.3486 0.1989  68  SER   b N   
48271 C  CA  . SER   BA 68  ? 1.7768 0.5778 1.2504 -0.0039 -0.3588 0.1550  68  SER   b CA  
48272 C  C   . SER   BA 68  ? 1.7727 0.5726 1.2701 -0.0136 -0.3389 0.1085  68  SER   b C   
48273 O  O   . SER   BA 68  ? 1.8258 0.5740 1.3550 -0.0692 -0.3297 0.0843  68  SER   b O   
48274 C  CB  . SER   BA 68  ? 1.8080 0.5758 1.2508 -0.0221 -0.3637 0.0772  68  SER   b CB  
48275 O  OG  . SER   BA 68  ? 1.8079 0.6935 1.3513 -0.0377 -0.2823 0.0163  68  SER   b OG  
48276 N  N   . GLN   BA 69  ? 1.8066 0.5195 1.2544 -0.0077 -0.3088 0.1535  69  GLN   b N   
48277 C  CA  . GLN   BA 69  ? 1.8108 0.5856 1.3191 0.0028  -0.2736 0.1642  69  GLN   b CA  
48278 C  C   . GLN   BA 69  ? 1.7970 0.6668 1.3895 -0.0224 -0.2920 0.1105  69  GLN   b C   
48279 O  O   . GLN   BA 69  ? 1.8371 0.7498 1.6107 0.0450  -0.2884 0.1747  69  GLN   b O   
48280 C  CB  . GLN   BA 69  ? 1.8362 0.5618 1.2945 0.0190  -0.3134 0.2051  69  GLN   b CB  
48281 C  CG  . GLN   BA 69  ? 1.8338 0.5652 1.3233 0.0363  -0.3378 0.2744  69  GLN   b CG  
48282 C  CD  . GLN   BA 69  ? 1.8734 0.5945 1.3160 0.0622  -0.3595 0.3383  69  GLN   b CD  
48283 O  OE1 . GLN   BA 69  ? 1.8757 0.6746 1.3194 0.0914  -0.3532 0.4183  69  GLN   b OE1 
48284 N  NE2 . GLN   BA 69  ? 1.8210 0.6117 1.3141 0.0993  -0.3386 0.3197  69  GLN   b NE2 
48285 N  N   . TYR   BA 70  ? 1.7270 0.6570 1.3617 -0.0037 -0.2781 0.1161  70  TYR   b N   
48286 C  CA  . TYR   BA 70  ? 1.7388 0.6749 1.3364 0.0378  -0.2906 0.0945  70  TYR   b CA  
48287 C  C   . TYR   BA 70  ? 1.7256 0.6606 1.3192 0.0055  -0.2867 0.1102  70  TYR   b C   
48288 O  O   . TYR   BA 70  ? 1.6891 0.6588 1.2846 -0.0013 -0.2547 0.1248  70  TYR   b O   
48289 C  CB  . TYR   BA 70  ? 1.7020 0.6377 1.2755 0.0632  -0.3182 0.0751  70  TYR   b CB  
48290 C  CG  . TYR   BA 70  ? 1.7122 0.6684 1.2702 0.1090  -0.3586 0.0471  70  TYR   b CG  
48291 C  CD1 . TYR   BA 70  ? 1.7203 0.7098 1.2497 0.1310  -0.3766 0.0181  70  TYR   b CD1 
48292 C  CD2 . TYR   BA 70  ? 1.6949 0.6836 1.2031 0.1194  -0.3642 0.0234  70  TYR   b CD2 
48293 C  CE1 . TYR   BA 70  ? 1.7104 0.6940 1.2454 0.1372  -0.4025 -0.0022 70  TYR   b CE1 
48294 C  CE2 . TYR   BA 70  ? 1.6892 0.6463 1.2019 0.1433  -0.3715 0.0202  70  TYR   b CE2 
48295 C  CZ  . TYR   BA 70  ? 1.7022 0.6703 1.1753 0.1267  -0.3854 -0.0319 70  TYR   b CZ  
48296 O  OH  . TYR   BA 70  ? 1.6739 0.5899 1.1660 0.1324  -0.4254 -0.0584 70  TYR   b OH  
48297 N  N   . GLY   BA 71  ? 1.7223 0.6654 1.3545 -0.0144 -0.3020 0.0935  71  GLY   b N   
48298 C  CA  . GLY   BA 71  ? 1.7524 0.6536 1.3496 -0.0221 -0.3002 0.0934  71  GLY   b CA  
48299 C  C   . GLY   BA 71  ? 1.7728 0.6562 1.2985 -0.0572 -0.2816 0.1119  71  GLY   b C   
48300 O  O   . GLY   BA 71  ? 1.7472 0.6408 1.2865 -0.0552 -0.2509 0.0918  71  GLY   b O   
48301 N  N   . THR   BA 72  ? 1.8068 0.6332 1.2676 -0.1056 -0.2931 0.1428  72  THR   b N   
48302 C  CA  . THR   BA 72  ? 1.7962 0.6039 1.1891 -0.1197 -0.3224 0.2099  72  THR   b CA  
48303 C  C   . THR   BA 72  ? 1.7729 0.5230 1.1324 -0.0832 -0.3544 0.2224  72  THR   b C   
48304 O  O   . THR   BA 72  ? 1.8190 0.4075 1.0557 -0.0921 -0.3822 0.3950  72  THR   b O   
48305 C  CB  . THR   BA 72  ? 1.7851 0.5684 1.2054 -0.1478 -0.3024 0.1928  72  THR   b CB  
48306 O  OG1 . THR   BA 72  ? 1.8045 0.6620 1.3004 -0.2413 -0.2866 0.1180  72  THR   b OG1 
48307 C  CG2 . THR   BA 72  ? 1.7696 0.5805 1.2252 -0.1437 -0.2872 0.1793  72  THR   b CG2 
48308 N  N   . PRO   BA 73  ? 1.8027 0.5308 1.0861 -0.0393 -0.3648 0.1923  73  PRO   b N   
48309 C  CA  . PRO   BA 73  ? 1.7812 0.5172 1.1075 -0.0174 -0.3611 0.1949  73  PRO   b CA  
48310 C  C   . PRO   BA 73  ? 1.7783 0.4615 1.0977 -0.0157 -0.3617 0.2395  73  PRO   b C   
48311 O  O   . PRO   BA 73  ? 1.8178 0.3918 1.0257 0.0231  -0.3335 0.3810  73  PRO   b O   
48312 C  CB  . PRO   BA 73  ? 1.7731 0.5119 1.0647 -0.0168 -0.3611 0.1487  73  PRO   b CB  
48313 C  CG  . PRO   BA 73  ? 1.7865 0.5257 1.0820 -0.0088 -0.3373 0.1392  73  PRO   b CG  
48314 C  CD  . PRO   BA 73  ? 1.7944 0.5533 1.0959 -0.0165 -0.3480 0.1656  73  PRO   b CD  
48315 N  N   . SER   BA 74  ? 1.7651 0.4570 1.1527 0.0052  -0.3446 0.2567  74  SER   b N   
48316 C  CA  . SER   BA 74  ? 1.7554 0.4540 1.1443 0.0204  -0.3118 0.2270  74  SER   b CA  
48317 C  C   . SER   BA 74  ? 1.7534 0.4067 1.1409 0.0084  -0.2863 0.1887  74  SER   b C   
48318 O  O   . SER   BA 74  ? 1.7328 0.4136 1.1076 -0.0138 -0.2386 0.1575  74  SER   b O   
48319 C  CB  . SER   BA 74  ? 1.7516 0.4265 1.0928 0.0206  -0.3277 0.2349  74  SER   b CB  
48320 O  OG  . SER   BA 74  ? 1.7314 0.3438 1.0894 0.0326  -0.3548 0.2834  74  SER   b OG  
48321 N  N   . THR   BA 75  ? 1.7823 0.4153 1.2092 -0.0027 -0.2630 0.1581  75  THR   b N   
48322 C  CA  . THR   BA 75  ? 1.7521 0.4011 1.1930 -0.0100 -0.2799 0.1357  75  THR   b CA  
48323 C  C   . THR   BA 75  ? 1.6902 0.2978 1.1865 0.0118  -0.3072 0.1306  75  THR   b C   
48324 O  O   . THR   BA 75  ? 1.6822 0.2442 1.2194 -0.0195 -0.3011 0.1577  75  THR   b O   
48325 C  CB  . THR   BA 75  ? 1.7769 0.3876 1.2168 -0.0072 -0.2555 0.1304  75  THR   b CB  
48326 O  OG1 . THR   BA 75  ? 1.8297 0.2783 1.3991 -0.0888 -0.1498 0.0895  75  THR   b OG1 
48327 C  CG2 . THR   BA 75  ? 1.7677 0.4305 1.1390 -0.0074 -0.2649 0.1932  75  THR   b CG2 
48328 N  N   . GLU   BA 76  ? 1.6868 0.3458 1.1804 0.0036  -0.3420 0.0780  76  GLU   b N   
48329 C  CA  . GLU   BA 76  ? 1.6713 0.4435 1.1903 0.0032  -0.3366 0.0376  76  GLU   b CA  
48330 C  C   . GLU   BA 76  ? 1.6574 0.4481 1.2122 0.0312  -0.3583 0.0187  76  GLU   b C   
48331 O  O   . GLU   BA 76  ? 1.6568 0.3227 1.1741 0.0019  -0.3444 -0.0607 76  GLU   b O   
48332 C  CB  . GLU   BA 76  ? 1.6788 0.5924 1.2642 0.0259  -0.3722 -0.0328 76  GLU   b CB  
48333 C  CG  . GLU   BA 76  ? 1.7371 0.7282 1.3029 0.0272  -0.3128 -0.0619 76  GLU   b CG  
48334 C  CD  . GLU   BA 76  ? 1.7474 0.8800 1.4171 0.0644  -0.3322 -0.1159 76  GLU   b CD  
48335 O  OE1 . GLU   BA 76  ? 1.8263 1.0227 1.5823 -0.0484 -0.2374 -0.0723 76  GLU   b OE1 
48336 O  OE2 . GLU   BA 76  ? 1.7909 0.8722 1.4556 0.0777  -0.3520 -0.1340 76  GLU   b OE2 
48337 N  N   . THR   BA 77  ? 1.6466 0.4766 1.2447 -0.0034 -0.3812 0.0320  77  THR   b N   
48338 C  CA  . THR   BA 77  ? 1.6150 0.5865 1.2198 0.0074  -0.4172 0.0459  77  THR   b CA  
48339 C  C   . THR   BA 77  ? 1.6025 0.5120 1.1827 -0.0097 -0.3643 0.0891  77  THR   b C   
48340 O  O   . THR   BA 77  ? 1.5816 0.4932 1.1984 -0.0085 -0.3954 0.1359  77  THR   b O   
48341 C  CB  . THR   BA 77  ? 1.6176 0.5841 1.2599 -0.0052 -0.4445 0.0188  77  THR   b CB  
48342 O  OG1 . THR   BA 77  ? 1.6172 0.6366 1.2998 0.0181  -0.4686 -0.0342 77  THR   b OG1 
48343 C  CG2 . THR   BA 77  ? 1.6096 0.6027 1.2720 0.0168  -0.4423 -0.0092 77  THR   b CG2 
48344 N  N   . ALA   BA 78  ? 1.6229 0.4658 1.1417 -0.0007 -0.3584 0.1066  78  ALA   b N   
48345 C  CA  . ALA   BA 78  ? 1.6231 0.5173 1.0972 0.0084  -0.3549 0.1064  78  ALA   b CA  
48346 C  C   . ALA   BA 78  ? 1.6316 0.5532 1.0792 -0.0195 -0.3278 0.1058  78  ALA   b C   
48347 O  O   . ALA   BA 78  ? 1.6561 0.6636 1.0641 -0.0064 -0.3369 0.0873  78  ALA   b O   
48348 C  CB  . ALA   BA 78  ? 1.6200 0.4924 1.0885 -0.0090 -0.3560 0.1241  78  ALA   b CB  
48349 N  N   . ALA   BA 79  ? 1.6373 0.4942 1.0644 -0.0279 -0.3110 0.1318  79  ALA   b N   
48350 C  CA  . ALA   BA 79  ? 1.6736 0.4519 1.0461 0.0394  -0.3019 0.1614  79  ALA   b CA  
48351 C  C   . ALA   BA 79  ? 1.6949 0.4086 1.0702 0.0391  -0.2770 0.1438  79  ALA   b C   
48352 O  O   . ALA   BA 79  ? 1.7446 0.4041 1.0519 0.0227  -0.2671 0.1305  79  ALA   b O   
48353 C  CB  . ALA   BA 79  ? 1.6526 0.3966 1.0431 0.0407  -0.3190 0.2147  79  ALA   b CB  
48354 N  N   . SER   BA 80  ? 1.6882 0.4463 1.0678 0.0671  -0.2636 0.1451  80  SER   b N   
48355 C  CA  . SER   BA 80  ? 1.7076 0.4892 1.0715 0.0476  -0.2592 0.1235  80  SER   b CA  
48356 C  C   . SER   BA 80  ? 1.6921 0.4119 1.1135 0.0401  -0.2783 0.1120  80  SER   b C   
48357 O  O   . SER   BA 80  ? 1.6471 0.2960 1.1542 0.0279  -0.2581 0.1113  80  SER   b O   
48358 C  CB  . SER   BA 80  ? 1.7254 0.5127 1.0985 0.0740  -0.2473 0.0980  80  SER   b CB  
48359 O  OG  . SER   BA 80  ? 1.7931 0.5105 1.0897 0.0787  -0.2456 0.0445  80  SER   b OG  
48360 N  N   . VAL   BA 81  ? 1.7242 0.4484 1.1036 -0.0005 -0.2784 0.0922  81  VAL   b N   
48361 C  CA  . VAL   BA 81  ? 1.8010 0.4795 1.1055 -0.0098 -0.2911 0.0402  81  VAL   b CA  
48362 C  C   . VAL   BA 81  ? 1.8186 0.4394 1.0367 -0.0146 -0.2949 -0.0144 81  VAL   b C   
48363 O  O   . VAL   BA 81  ? 1.8669 0.4028 1.0079 0.0014  -0.2854 -0.0824 81  VAL   b O   
48364 C  CB  . VAL   BA 81  ? 1.8374 0.5327 1.1399 -0.0525 -0.2854 0.0463  81  VAL   b CB  
48365 C  CG1 . VAL   BA 81  ? 1.8385 0.5768 1.1283 -0.0591 -0.2837 0.0653  81  VAL   b CG1 
48366 C  CG2 . VAL   BA 81  ? 1.8639 0.5145 1.1758 -0.0530 -0.3001 0.0281  81  VAL   b CG2 
48367 N  N   . PHE   BA 82  ? 1.7550 0.3976 1.0657 -0.0276 -0.3195 -0.0203 82  PHE   b N   
48368 C  CA  . PHE   BA 82  ? 1.6849 0.3528 0.9719 -0.0763 -0.3430 -0.0664 82  PHE   b CA  
48369 C  C   . PHE   BA 82  ? 1.6934 0.2231 0.9841 -0.0323 -0.3499 -0.0475 82  PHE   b C   
48370 O  O   . PHE   BA 82  ? 1.6672 0.2000 1.0366 -0.0084 -0.3820 -0.0324 82  PHE   b O   
48371 C  CB  . PHE   BA 82  ? 1.6425 0.3244 0.9714 -0.1029 -0.3593 -0.0714 82  PHE   b CB  
48372 C  CG  . PHE   BA 82  ? 1.6232 0.3108 0.9612 -0.1085 -0.3926 -0.0567 82  PHE   b CG  
48373 C  CD1 . PHE   BA 82  ? 1.6626 0.2881 0.9222 -0.1183 -0.4015 -0.0213 82  PHE   b CD1 
48374 C  CD2 . PHE   BA 82  ? 1.6450 0.3604 0.9737 -0.1298 -0.3654 -0.0511 82  PHE   b CD2 
48375 C  CE1 . PHE   BA 82  ? 1.6614 0.3067 0.9317 -0.1150 -0.4069 0.0091  82  PHE   b CE1 
48376 C  CE2 . PHE   BA 82  ? 1.6438 0.4060 0.9548 -0.1249 -0.3686 -0.0215 82  PHE   b CE2 
48377 C  CZ  . PHE   BA 82  ? 1.6642 0.3793 0.9204 -0.1400 -0.3738 0.0011  82  PHE   b CZ  
48378 N  N   . LYS   BA 83  ? 1.6876 0.2434 0.9986 0.0085  -0.3399 -0.0663 83  LYS   b N   
48379 C  CA  . LYS   BA 83  ? 1.6805 0.3531 1.0481 0.0234  -0.3001 -0.0533 83  LYS   b CA  
48380 C  C   . LYS   BA 83  ? 1.7094 0.4611 1.0347 0.0195  -0.2865 -0.0488 83  LYS   b C   
48381 O  O   . LYS   BA 83  ? 1.7680 0.3702 1.0218 -0.0332 -0.2593 -0.1082 83  LYS   b O   
48382 C  CB  . LYS   BA 83  ? 1.6764 0.4303 1.1091 0.0689  -0.3057 -0.0719 83  LYS   b CB  
48383 C  CG  . LYS   BA 83  ? 1.6910 0.5000 1.1858 0.0827  -0.2701 -0.0617 83  LYS   b CG  
48384 C  CD  . LYS   BA 83  ? 1.6936 0.6349 1.3319 0.1377  -0.2340 -0.0960 83  LYS   b CD  
48385 C  CE  . LYS   BA 83  ? 1.7345 0.7330 1.3803 0.1333  -0.2148 -0.1610 83  LYS   b CE  
48386 N  NZ  . LYS   BA 83  ? 1.7455 0.8207 1.4932 0.1645  -0.2074 -0.0681 83  LYS   b NZ  
48387 N  N   . GLU   BA 84  ? 1.7079 0.4766 1.0815 0.0071  -0.2796 -0.0838 84  GLU   b N   
48388 C  CA  . GLU   BA 84  ? 1.7112 0.5857 1.1008 0.0188  -0.2436 -0.1109 84  GLU   b CA  
48389 C  C   . GLU   BA 84  ? 1.7220 0.5527 1.0556 -0.0036 -0.2182 -0.0684 84  GLU   b C   
48390 O  O   . GLU   BA 84  ? 1.7407 0.4810 1.0033 -0.0147 -0.2806 -0.0729 84  GLU   b O   
48391 C  CB  . GLU   BA 84  ? 1.7157 0.5840 1.2189 0.0562  -0.1984 -0.1137 84  GLU   b CB  
48392 C  CG  . GLU   BA 84  ? 1.7124 0.7082 1.3131 0.0808  -0.1467 -0.1557 84  GLU   b CG  
48393 C  CD  . GLU   BA 84  ? 1.7102 0.7528 1.3275 0.0347  -0.1479 -0.2388 84  GLU   b CD  
48394 O  OE1 . GLU   BA 84  ? 1.7481 0.9886 1.4229 0.0869  -0.0130 -0.2486 84  GLU   b OE1 
48395 O  OE2 . GLU   BA 84  ? 1.6558 0.6063 1.3808 0.0007  -0.0704 -0.2453 84  GLU   b OE2 
48396 N  N   . LEU   BA 85  ? 1.6848 0.5354 1.0182 0.0188  -0.2755 -0.0114 85  LEU   b N   
48397 C  CA  . LEU   BA 85  ? 1.7008 0.5930 0.9724 0.0088  -0.2783 0.0051  85  LEU   b CA  
48398 C  C   . LEU   BA 85  ? 1.7176 0.6237 1.0090 -0.0242 -0.2652 0.0495  85  LEU   b C   
48399 O  O   . LEU   BA 85  ? 1.7171 0.7719 0.9736 0.0050  -0.2070 0.0250  85  LEU   b O   
48400 C  CB  . LEU   BA 85  ? 1.6864 0.6025 0.9305 0.0052  -0.3086 0.0265  85  LEU   b CB  
48401 C  CG  . LEU   BA 85  ? 1.6868 0.6070 0.9021 -0.0039 -0.3234 0.0087  85  LEU   b CG  
48402 C  CD1 . LEU   BA 85  ? 1.6785 0.6355 0.9178 0.0029  -0.3213 0.0152  85  LEU   b CD1 
48403 C  CD2 . LEU   BA 85  ? 1.7058 0.6233 0.8918 0.0003  -0.3129 0.0016  85  LEU   b CD2 
48404 N  N   . CYS   BA 86  ? 1.7052 0.5409 1.0063 -0.0558 -0.2765 0.0942  86  CYS   b N   
48405 C  CA  . CYS   BA 86  ? 1.6660 0.5303 0.9594 -0.0453 -0.2773 0.1259  86  CYS   b CA  
48406 C  C   . CYS   BA 86  ? 1.6491 0.3869 0.9547 -0.0247 -0.2934 0.1382  86  CYS   b C   
48407 O  O   . CYS   BA 86  ? 1.6283 0.5403 0.8476 -0.0310 -0.2994 0.1829  86  CYS   b O   
48408 C  CB  . CYS   BA 86  ? 1.6778 0.4710 0.9477 -0.0642 -0.2695 0.1547  86  CYS   b CB  
48409 S  SG  . CYS   BA 86  ? 1.7132 0.4986 0.9847 -0.1505 -0.2579 0.1954  86  CYS   b SG  
48410 N  N   . TYR   BA 87  ? 1.6698 0.3882 0.9431 -0.0099 -0.3031 0.1627  87  TYR   b N   
48411 C  CA  . TYR   BA 87  ? 1.6792 0.3753 0.9456 -0.0022 -0.2973 0.1836  87  TYR   b CA  
48412 C  C   . TYR   BA 87  ? 1.7192 0.4573 0.9519 0.0503  -0.3194 0.1766  87  TYR   b C   
48413 O  O   . TYR   BA 87  ? 1.7352 0.3519 1.0015 0.0439  -0.3647 0.1681  87  TYR   b O   
48414 C  CB  . TYR   BA 87  ? 1.6473 0.4098 0.9081 -0.0149 -0.3062 0.1452  87  TYR   b CB  
48415 C  CG  . TYR   BA 87  ? 1.6554 0.3935 0.8946 -0.0200 -0.3040 0.1482  87  TYR   b CG  
48416 C  CD1 . TYR   BA 87  ? 1.6521 0.3948 0.8789 -0.0188 -0.3051 0.1562  87  TYR   b CD1 
48417 C  CD2 . TYR   BA 87  ? 1.6640 0.4348 0.9170 -0.0209 -0.2859 0.1293  87  TYR   b CD2 
48418 C  CE1 . TYR   BA 87  ? 1.6631 0.4462 0.8792 0.0024  -0.2800 0.1336  87  TYR   b CE1 
48419 C  CE2 . TYR   BA 87  ? 1.6764 0.4399 0.9254 -0.0316 -0.2786 0.1415  87  TYR   b CE2 
48420 C  CZ  . TYR   BA 87  ? 1.6843 0.4143 0.8972 -0.0056 -0.2820 0.1325  87  TYR   b CZ  
48421 O  OH  . TYR   BA 87  ? 1.6726 0.4219 0.8863 0.0026  -0.2984 0.1375  87  TYR   b OH  
48422 N  N   . GLU   BA 88  ? 1.6979 0.5381 1.0304 0.0205  -0.3506 0.1102  88  GLU   b N   
48423 C  CA  . GLU   BA 88  ? 1.7301 0.6774 1.0362 0.0771  -0.3192 0.0932  88  GLU   b CA  
48424 C  C   . GLU   BA 88  ? 1.7420 0.6617 1.0746 0.0918  -0.3017 0.1336  88  GLU   b C   
48425 O  O   . GLU   BA 88  ? 1.7746 0.7011 1.0630 0.1060  -0.3294 0.2020  88  GLU   b O   
48426 C  CB  . GLU   BA 88  ? 1.7431 0.6860 1.0913 0.0615  -0.3200 0.0422  88  GLU   b CB  
48427 C  CG  . GLU   BA 88  ? 1.7500 0.7799 1.1295 0.1095  -0.3299 0.0117  88  GLU   b CG  
48428 C  CD  . GLU   BA 88  ? 1.8157 0.8519 1.1455 0.1221  -0.2661 -0.0209 88  GLU   b CD  
48429 O  OE1 . GLU   BA 88  ? 1.8319 0.8885 1.1390 0.1628  -0.3050 -0.0248 88  GLU   b OE1 
48430 O  OE2 . GLU   BA 88  ? 1.8249 0.9315 1.1803 0.1722  -0.2809 -0.1014 88  GLU   b OE2 
48431 N  N   . ASN   BA 89  ? 1.7147 0.6570 1.1335 0.0785  -0.2928 0.1301  89  ASN   b N   
48432 C  CA  . ASN   BA 89  ? 1.6622 0.6479 1.1505 0.0445  -0.3084 0.0935  89  ASN   b CA  
48433 C  C   . ASN   BA 89  ? 1.6468 0.6199 1.2221 0.0520  -0.3436 0.1326  89  ASN   b C   
48434 O  O   . ASN   BA 89  ? 1.6736 0.6522 1.1691 0.0835  -0.4124 0.1933  89  ASN   b O   
48435 C  CB  . ASN   BA 89  ? 1.6925 0.6156 1.1378 0.0139  -0.2936 0.0721  89  ASN   b CB  
48436 C  CG  . ASN   BA 89  ? 1.7033 0.5942 1.1611 -0.0112 -0.2656 0.0918  89  ASN   b CG  
48437 O  OD1 . ASN   BA 89  ? 1.7268 0.5610 1.1919 -0.0398 -0.2247 0.0472  89  ASN   b OD1 
48438 N  ND2 . ASN   BA 89  ? 1.7064 0.6134 1.1512 0.0043  -0.2569 0.0999  89  ASN   b ND2 
48439 N  N   . LYS   BA 90  ? 1.6614 0.5368 1.3269 0.0261  -0.3044 0.1436  90  LYS   b N   
48440 C  CA  . LYS   BA 90  ? 1.6870 0.5013 1.3244 0.0126  -0.2576 0.1791  90  LYS   b CA  
48441 C  C   . LYS   BA 90  ? 1.7125 0.5644 1.2094 -0.0063 -0.2606 0.1649  90  LYS   b C   
48442 O  O   . LYS   BA 90  ? 1.7034 0.6063 1.1943 0.0987  -0.2761 0.2494  90  LYS   b O   
48443 C  CB  . LYS   BA 90  ? 1.6927 0.3780 1.3736 -0.0003 -0.2488 0.1679  90  LYS   b CB  
48444 C  CG  . LYS   BA 90  ? 1.6947 0.4086 1.4024 0.0017  -0.2350 0.1778  90  LYS   b CG  
48445 C  CD  . LYS   BA 90  ? 1.6831 0.4485 1.3937 0.0175  -0.2624 0.1771  90  LYS   b CD  
48446 C  CE  . LYS   BA 90  ? 1.7125 0.3831 1.4257 0.0001  -0.2601 0.2245  90  LYS   b CE  
48447 N  NZ  . LYS   BA 90  ? 1.6787 0.4986 1.4289 0.0049  -0.2948 0.2304  90  LYS   b NZ  
48448 N  N   . ASP   BA 91  ? 1.7584 0.6243 1.2008 -0.0416 -0.2251 0.1677  91  ASP   b N   
48449 C  CA  . ASP   BA 91  ? 1.8190 0.6314 1.1610 -0.0250 -0.2303 0.1428  91  ASP   b CA  
48450 C  C   . ASP   BA 91  ? 1.8092 0.6589 1.1544 -0.1434 -0.2310 0.0807  91  ASP   b C   
48451 O  O   . ASP   BA 91  ? 1.8214 0.7236 1.1641 -0.1250 -0.3181 0.0523  91  ASP   b O   
48452 C  CB  . ASP   BA 91  ? 1.9514 0.6817 1.1441 0.0207  -0.2326 0.1361  91  ASP   b CB  
48453 C  CG  . ASP   BA 91  ? 1.9779 0.7186 1.2130 0.0724  -0.1609 0.1907  91  ASP   b CG  
48454 O  OD1 . ASP   BA 91  ? 2.1025 0.6619 1.1258 0.1210  -0.1492 0.2133  91  ASP   b OD1 
48455 O  OD2 . ASP   BA 91  ? 2.1172 0.8049 1.1572 0.0930  -0.1682 0.1927  91  ASP   b OD2 
48456 N  N   . ASN   BA 92  ? 1.8057 0.6086 1.1428 -0.1115 -0.2556 0.0983  92  ASN   b N   
48457 C  CA  . ASN   BA 92  ? 1.8087 0.6248 1.1938 -0.1478 -0.2439 0.0763  92  ASN   b CA  
48458 C  C   . ASN   BA 92  ? 1.7390 0.5723 1.2101 -0.1520 -0.2566 0.0472  92  ASN   b C   
48459 O  O   . ASN   BA 92  ? 1.7832 0.5822 1.4030 -0.1987 -0.2834 0.0379  92  ASN   b O   
48460 C  CB  . ASN   BA 92  ? 1.8558 0.6947 1.2071 -0.1829 -0.2294 0.0284  92  ASN   b CB  
48461 C  CG  . ASN   BA 92  ? 1.9292 0.7806 1.2786 -0.2048 -0.1682 -0.0365 92  ASN   b CG  
48462 O  OD1 . ASN   BA 92  ? 1.9823 0.6394 1.4335 -0.2707 -0.2026 -0.0652 92  ASN   b OD1 
48463 N  ND2 . ASN   BA 92  ? 1.9893 0.7771 1.3525 -0.1768 -0.1855 -0.0150 92  ASN   b ND2 
48464 N  N   . LEU   BA 93  ? 1.6721 0.5663 1.2142 -0.1264 -0.2518 0.0394  93  LEU   b N   
48465 C  CA  . LEU   BA 93  ? 1.6100 0.5801 1.1802 -0.1281 -0.2974 0.0393  93  LEU   b CA  
48466 C  C   . LEU   BA 93  ? 1.5060 0.5866 1.1871 -0.1811 -0.2816 0.0372  93  LEU   b C   
48467 O  O   . LEU   BA 93  ? 1.5185 0.6154 1.2400 -0.2373 -0.3386 -0.0734 93  LEU   b O   
48468 C  CB  . LEU   BA 93  ? 1.6043 0.6312 1.1615 -0.1107 -0.3105 0.0430  93  LEU   b CB  
48469 C  CG  . LEU   BA 93  ? 1.5982 0.6415 1.1305 -0.1161 -0.3261 0.0349  93  LEU   b CG  
48470 C  CD1 . LEU   BA 93  ? 1.6291 0.6039 1.1905 -0.1041 -0.2988 0.0512  93  LEU   b CD1 
48471 C  CD2 . LEU   BA 93  ? 1.5848 0.6115 1.0651 -0.1221 -0.3683 0.0291  93  LEU   b CD2 
48472 N  N   . THR   BA 94  ? 1.5495 0.5577 1.1387 -0.1556 -0.2779 0.0371  94  THR   b N   
48473 C  CA  . THR   BA 94  ? 1.5586 0.5485 1.0976 -0.1436 -0.2384 0.0595  94  THR   b CA  
48474 C  C   . THR   BA 94  ? 1.5991 0.4646 1.1139 -0.1008 -0.2339 0.0799  94  THR   b C   
48475 O  O   . THR   BA 94  ? 1.6263 0.3657 1.1298 -0.0988 -0.1896 0.1572  94  THR   b O   
48476 C  CB  . THR   BA 94  ? 1.5770 0.5966 1.1002 -0.1301 -0.2533 0.0841  94  THR   b CB  
48477 O  OG1 . THR   BA 94  ? 1.6124 0.5804 1.1231 -0.1418 -0.2274 0.1080  94  THR   b OG1 
48478 C  CG2 . THR   BA 94  ? 1.5865 0.6418 1.0839 -0.1794 -0.2668 0.0731  94  THR   b CG2 
48479 N  N   . ALA   BA 95  ? 1.5717 0.4744 1.1365 -0.0389 -0.2131 0.0248  95  ALA   b N   
48480 C  CA  . ALA   BA 95  ? 1.5776 0.5390 1.0857 0.0116  -0.2286 0.0147  95  ALA   b CA  
48481 C  C   . ALA   BA 95  ? 1.5774 0.4962 1.0675 0.0435  -0.2143 -0.0512 95  ALA   b C   
48482 O  O   . ALA   BA 95  ? 1.5388 0.6038 1.0823 0.0360  -0.2524 -0.0254 95  ALA   b O   
48483 C  CB  . ALA   BA 95  ? 1.5955 0.5350 1.0765 0.0064  -0.2144 0.0289  95  ALA   b CB  
48484 N  N   . GLY   BA 96  ? 1.6243 0.4653 1.0670 0.0322  -0.2588 -0.0867 96  GLY   b N   
48485 C  CA  . GLY   BA 96  ? 1.6199 0.4645 1.0731 0.0480  -0.2640 -0.0778 96  GLY   b CA  
48486 C  C   . GLY   BA 96  ? 1.6406 0.4169 1.0939 0.0586  -0.2706 -0.0665 96  GLY   b C   
48487 O  O   . GLY   BA 96  ? 1.6513 0.4746 1.1068 0.0775  -0.2483 -0.0105 96  GLY   b O   
48488 N  N   . ILE   BA 97  ? 1.6247 0.4006 1.0782 0.0449  -0.2597 -0.0734 97  ILE   b N   
48489 C  CA  . ILE   BA 97  ? 1.6429 0.4653 1.0846 0.0387  -0.2656 -0.0300 97  ILE   b CA  
48490 C  C   . ILE   BA 97  ? 1.6720 0.3932 1.0601 0.0173  -0.2647 -0.0620 97  ILE   b C   
48491 O  O   . ILE   BA 97  ? 1.6861 0.3095 1.0567 -0.0145 -0.2319 -0.1190 97  ILE   b O   
48492 C  CB  . ILE   BA 97  ? 1.6493 0.4797 1.0643 0.0310  -0.2808 -0.0290 97  ILE   b CB  
48493 C  CG1 . ILE   BA 97  ? 1.6743 0.5066 1.0588 0.0425  -0.2845 -0.0035 97  ILE   b CG1 
48494 C  CG2 . ILE   BA 97  ? 1.6486 0.5293 1.0975 0.0227  -0.2839 0.0071  97  ILE   b CG2 
48495 C  CD1 . ILE   BA 97  ? 1.6849 0.4888 1.0886 0.0416  -0.2880 -0.0091 97  ILE   b CD1 
48496 N  N   . ILE   BA 98  ? 1.6898 0.4549 1.0731 0.0008  -0.2527 -0.0273 98  ILE   b N   
48497 C  CA  . ILE   BA 98  ? 1.7317 0.6017 1.1119 0.0016  -0.2778 0.0236  98  ILE   b CA  
48498 C  C   . ILE   BA 98  ? 1.7003 0.6294 1.1391 0.0011  -0.2808 0.0767  98  ILE   b C   
48499 O  O   . ILE   BA 98  ? 1.7145 0.7153 1.2202 -0.0212 -0.2424 0.1087  98  ILE   b O   
48500 C  CB  . ILE   BA 98  ? 1.7886 0.6372 1.1063 0.0346  -0.2897 0.0189  98  ILE   b CB  
48501 C  CG1 . ILE   BA 98  ? 1.7900 0.6705 1.1112 0.0330  -0.2988 0.0891  98  ILE   b CG1 
48502 C  CG2 . ILE   BA 98  ? 1.7943 0.7027 1.1440 0.0515  -0.3272 0.0136  98  ILE   b CG2 
48503 C  CD1 . ILE   BA 98  ? 1.7819 0.6790 1.0973 0.0117  -0.3093 0.0858  98  ILE   b CD1 
48504 N  N   . VAL   BA 99  ? 1.6451 0.6918 1.1032 -0.0047 -0.2971 0.1063  99  VAL   b N   
48505 C  CA  . VAL   BA 99  ? 1.6612 0.6949 1.0523 -0.0323 -0.2864 0.0958  99  VAL   b CA  
48506 C  C   . VAL   BA 99  ? 1.6682 0.6624 1.0530 -0.0359 -0.2706 0.1399  99  VAL   b C   
48507 O  O   . VAL   BA 99  ? 1.6723 0.7184 0.9947 -0.0629 -0.2874 0.2334  99  VAL   b O   
48508 C  CB  . VAL   BA 99  ? 1.6794 0.6385 1.0478 -0.0505 -0.2885 0.1044  99  VAL   b CB  
48509 C  CG1 . VAL   BA 99  ? 1.7162 0.6692 1.0544 -0.0770 -0.2998 0.1642  99  VAL   b CG1 
48510 C  CG2 . VAL   BA 99  ? 1.6481 0.6910 1.0434 -0.0360 -0.3039 0.0948  99  VAL   b CG2 
48511 N  N   . ALA   BA 100 ? 1.6329 0.6420 1.0707 -0.0277 -0.2493 0.0903  100 ALA   b N   
48512 C  CA  . ALA   BA 100 ? 1.6650 0.7728 1.0629 -0.0126 -0.2614 0.0373  100 ALA   b CA  
48513 C  C   . ALA   BA 100 ? 1.6831 0.7667 1.0697 -0.0211 -0.2656 0.0104  100 ALA   b C   
48514 O  O   . ALA   BA 100 ? 1.6910 0.7935 1.0561 0.0310  -0.3241 -0.0023 100 ALA   b O   
48515 C  CB  . ALA   BA 100 ? 1.6595 0.8051 1.0870 -0.0079 -0.2328 0.0348  100 ALA   b CB  
48516 N  N   . GLY   BA 101 ? 1.6904 0.8704 1.0700 0.0122  -0.2879 0.0042  101 GLY   b N   
48517 C  CA  . GLY   BA 101 ? 1.7380 0.8953 1.1039 -0.0241 -0.2830 0.0162  101 GLY   b CA  
48518 C  C   . GLY   BA 101 ? 1.8353 0.9802 1.0947 -0.0215 -0.3016 -0.0031 101 GLY   b C   
48519 O  O   . GLY   BA 101 ? 1.8435 1.1193 1.0202 -0.0609 -0.2880 -0.0309 101 GLY   b O   
48520 N  N   . TYR   BA 102 ? 1.9217 1.0035 1.1484 -0.0315 -0.3080 0.0317  102 TYR   b N   
48521 C  CA  . TYR   BA 102 ? 1.9629 1.0995 1.1474 -0.0224 -0.3183 0.0427  102 TYR   b CA  
48522 C  C   . TYR   BA 102 ? 1.9642 1.1115 1.2508 -0.0362 -0.3253 0.0151  102 TYR   b C   
48523 O  O   . TYR   BA 102 ? 1.9989 1.0753 1.2354 -0.0771 -0.2432 0.0232  102 TYR   b O   
48524 C  CB  . TYR   BA 102 ? 1.9791 1.0151 1.1461 -0.0177 -0.3051 0.0650  102 TYR   b CB  
48525 C  CG  . TYR   BA 102 ? 1.9907 0.9721 1.1541 -0.0377 -0.3107 0.0739  102 TYR   b CG  
48526 C  CD1 . TYR   BA 102 ? 2.0189 0.9625 1.0590 -0.0005 -0.3209 0.0878  102 TYR   b CD1 
48527 C  CD2 . TYR   BA 102 ? 2.0167 1.0141 1.1585 -0.0562 -0.3198 0.1330  102 TYR   b CD2 
48528 C  CE1 . TYR   BA 102 ? 2.0568 0.9767 1.0483 -0.0135 -0.3336 0.0803  102 TYR   b CE1 
48529 C  CE2 . TYR   BA 102 ? 2.0327 1.0170 1.1387 -0.0781 -0.3484 0.0990  102 TYR   b CE2 
48530 C  CZ  . TYR   BA 102 ? 2.0516 1.0195 1.0078 -0.0281 -0.3779 0.1394  102 TYR   b CZ  
48531 O  OH  . TYR   BA 102 ? 2.1037 1.0837 1.0465 -0.0294 -0.3710 0.2246  102 TYR   b OH  
48532 N  N   . ASP   BA 103 ? 1.9796 1.3451 1.3908 0.0096  -0.3325 0.0044  103 ASP   b N   
48533 C  CA  . ASP   BA 103 ? 2.0579 1.2755 1.4122 -0.0697 -0.3302 0.0948  103 ASP   b CA  
48534 C  C   . ASP   BA 103 ? 2.0193 1.1927 1.4699 -0.0443 -0.4062 0.3111  103 ASP   b C   
48535 O  O   . ASP   BA 103 ? 2.0221 1.1737 1.3200 -0.0014 -0.4300 0.4120  103 ASP   b O   
48536 C  CB  . ASP   BA 103 ? 2.0556 1.3993 1.5526 -0.0396 -0.3161 0.0078  103 ASP   b CB  
48537 C  CG  . ASP   BA 103 ? 2.0589 1.5467 1.6006 -0.1180 -0.3080 -0.1909 103 ASP   b CG  
48538 O  OD1 . ASP   BA 103 ? 2.0398 1.4084 1.8645 -0.2058 -0.3024 -0.0658 103 ASP   b OD1 
48539 O  OD2 . ASP   BA 103 ? 1.9595 1.8563 1.5554 -0.1566 -0.2390 -0.0458 103 ASP   b OD2 
48540 N  N   . ASP   BA 104 ? 1.9962 1.1575 1.5365 -0.0148 -0.4179 0.2552  104 ASP   b N   
48541 C  CA  . ASP   BA 104 ? 2.0540 1.1837 1.5606 0.0303  -0.3859 0.3347  104 ASP   b CA  
48542 C  C   . ASP   BA 104 ? 2.0364 1.1186 1.5744 0.1103  -0.3714 0.4011  104 ASP   b C   
48543 O  O   . ASP   BA 104 ? 1.9601 1.0641 1.5452 0.2000  -0.4344 0.4957  104 ASP   b O   
48544 C  CB  . ASP   BA 104 ? 2.1121 1.1899 1.6493 -0.0083 -0.3890 0.3141  104 ASP   b CB  
48545 C  CG  . ASP   BA 104 ? 2.1987 1.3014 1.7339 -0.0717 -0.3000 0.2531  104 ASP   b CG  
48546 O  OD1 . ASP   BA 104 ? 2.3007 1.4875 1.7980 -0.1016 -0.3591 0.1343  104 ASP   b OD1 
48547 O  OD2 . ASP   BA 104 ? 2.1885 1.2190 1.7532 -0.1425 -0.4278 0.2616  104 ASP   b OD2 
48548 N  N   . LYS   BA 105 ? 2.0906 1.1457 1.6049 0.1167  -0.3315 0.3945  105 LYS   b N   
48549 C  CA  . LYS   BA 105 ? 2.0976 1.1902 1.6488 0.0950  -0.2955 0.3402  105 LYS   b CA  
48550 C  C   . LYS   BA 105 ? 2.0824 1.1866 1.6133 0.0792  -0.3272 0.2996  105 LYS   b C   
48551 O  O   . LYS   BA 105 ? 2.0654 1.3300 1.6405 0.0506  -0.3968 0.3976  105 LYS   b O   
48552 C  CB  . LYS   BA 105 ? 2.1599 1.2673 1.7498 0.1120  -0.2236 0.2955  105 LYS   b CB  
48553 C  CG  . LYS   BA 105 ? 2.1727 1.3426 1.8634 0.0734  -0.1617 0.2075  105 LYS   b CG  
48554 C  CD  . LYS   BA 105 ? 2.1854 1.4247 1.9821 0.0175  -0.0909 0.1162  105 LYS   b CD  
48555 C  CE  . LYS   BA 105 ? 2.2023 1.4137 2.0479 -0.0095 -0.0999 0.1027  105 LYS   b CE  
48556 N  NZ  . LYS   BA 105 ? 2.1961 1.4386 2.0934 -0.0303 -0.0846 0.0735  105 LYS   b NZ  
48557 N  N   . ASN   BA 106 ? 2.0395 1.1081 1.5364 0.0614  -0.3184 0.2254  106 ASN   b N   
48558 C  CA  . ASN   BA 106 ? 1.9862 1.0676 1.4055 0.1091  -0.3520 0.1912  106 ASN   b CA  
48559 C  C   . ASN   BA 106 ? 1.9461 0.8982 1.4140 0.0286  -0.3712 0.2052  106 ASN   b C   
48560 O  O   . ASN   BA 106 ? 1.8756 0.8671 1.2590 0.0518  -0.4045 0.1010  106 ASN   b O   
48561 C  CB  . ASN   BA 106 ? 2.0024 1.1410 1.3886 0.1021  -0.4250 0.1307  106 ASN   b CB  
48562 C  CG  . ASN   BA 106 ? 2.0407 1.1863 1.3623 0.1323  -0.4877 0.0634  106 ASN   b CG  
48563 O  OD1 . ASN   BA 106 ? 2.0557 1.2968 1.3695 0.1265  -0.5357 0.0098  106 ASN   b OD1 
48564 N  ND2 . ASN   BA 106 ? 2.0493 1.1761 1.3656 0.1603  -0.5350 0.0768  106 ASN   b ND2 
48565 N  N   . LYS   BA 107 ? 1.9455 0.8075 1.4609 0.0064  -0.3716 0.1916  107 LYS   b N   
48566 C  CA  . LYS   BA 107 ? 1.9966 0.7730 1.4293 -0.0607 -0.3150 0.1383  107 LYS   b CA  
48567 C  C   . LYS   BA 107 ? 2.0199 0.7398 1.4614 -0.0746 -0.3069 0.1478  107 LYS   b C   
48568 O  O   . LYS   BA 107 ? 2.0191 0.4860 1.5432 -0.2133 -0.3044 0.1566  107 LYS   b O   
48569 C  CB  . LYS   BA 107 ? 1.9956 0.8528 1.3505 -0.0636 -0.2880 0.1500  107 LYS   b CB  
48570 C  CG  . LYS   BA 107 ? 2.0443 0.8596 1.3288 -0.0722 -0.2616 0.1620  107 LYS   b CG  
48571 C  CD  . LYS   BA 107 ? 2.0693 0.9600 1.3704 -0.0974 -0.2201 0.1297  107 LYS   b CD  
48572 C  CE  . LYS   BA 107 ? 2.0945 0.9983 1.3878 -0.0795 -0.2345 0.1409  107 LYS   b CE  
48573 N  NZ  . LYS   BA 107 ? 2.1225 1.0680 1.3998 -0.1176 -0.2173 0.1284  107 LYS   b NZ  
48574 N  N   . GLY   BA 108 ? 2.0106 0.7725 1.3366 -0.0723 -0.3058 0.0873  108 GLY   b N   
48575 C  CA  . GLY   BA 108 ? 1.9495 0.7264 1.2472 -0.0541 -0.3115 0.0094  108 GLY   b CA  
48576 C  C   . GLY   BA 108 ? 1.9010 0.7160 1.1505 -0.0121 -0.3504 -0.0139 108 GLY   b C   
48577 O  O   . GLY   BA 108 ? 1.8953 0.7761 1.1358 -0.0307 -0.3372 -0.0362 108 GLY   b O   
48578 N  N   . GLU   BA 109 ? 1.8611 0.7067 1.1406 0.0212  -0.3312 -0.0170 109 GLU   b N   
48579 C  CA  . GLU   BA 109 ? 1.8055 0.7695 1.1192 0.0747  -0.3552 -0.0056 109 GLU   b CA  
48580 C  C   . GLU   BA 109 ? 1.7743 0.6955 1.1054 0.0751  -0.3377 -0.0358 109 GLU   b C   
48581 O  O   . GLU   BA 109 ? 1.7444 0.6696 1.1329 0.1184  -0.3524 -0.0132 109 GLU   b O   
48582 C  CB  . GLU   BA 109 ? 1.7915 0.8093 1.1624 0.1031  -0.3948 -0.0390 109 GLU   b CB  
48583 C  CG  . GLU   BA 109 ? 1.7984 0.9215 1.2043 0.1182  -0.4220 -0.0433 109 GLU   b CG  
48584 C  CD  . GLU   BA 109 ? 1.8194 1.0472 1.1711 0.1577  -0.4533 -0.1119 109 GLU   b CD  
48585 O  OE1 . GLU   BA 109 ? 1.7771 1.2632 1.1664 0.2837  -0.4928 -0.1616 109 GLU   b OE1 
48586 O  OE2 . GLU   BA 109 ? 1.8175 1.0818 1.2555 0.1725  -0.4449 -0.0850 109 GLU   b OE2 
48587 N  N   . VAL   BA 110 ? 1.7738 0.6416 1.0315 0.1066  -0.3389 -0.0480 110 VAL   b N   
48588 C  CA  . VAL   BA 110 ? 1.7414 0.5816 1.0376 0.0363  -0.2932 -0.0101 110 VAL   b CA  
48589 C  C   . VAL   BA 110 ? 1.6729 0.5424 1.0749 0.0505  -0.2968 -0.0214 110 VAL   b C   
48590 O  O   . VAL   BA 110 ? 1.6590 0.4372 1.0356 0.1058  -0.3219 -0.0557 110 VAL   b O   
48591 C  CB  . VAL   BA 110 ? 1.7611 0.5706 1.0453 -0.0075 -0.2824 -0.0198 110 VAL   b CB  
48592 C  CG1 . VAL   BA 110 ? 1.7670 0.6174 1.0400 -0.0151 -0.2804 -0.0031 110 VAL   b CG1 
48593 C  CG2 . VAL   BA 110 ? 1.7717 0.5787 1.0352 -0.0302 -0.2878 0.0387  110 VAL   b CG2 
48594 N  N   . TYR   BA 111 ? 1.6997 0.6127 1.0572 0.0500  -0.2862 0.0101  111 TYR   b N   
48595 C  CA  . TYR   BA 111 ? 1.6918 0.6008 1.0658 0.0367  -0.2880 0.0104  111 TYR   b CA  
48596 C  C   . TYR   BA 111 ? 1.6572 0.5065 1.0789 -0.0190 -0.2812 0.0107  111 TYR   b C   
48597 O  O   . TYR   BA 111 ? 1.6374 0.5848 1.1131 0.0195  -0.2718 0.0241  111 TYR   b O   
48598 C  CB  . TYR   BA 111 ? 1.7346 0.5821 1.0701 0.0447  -0.2921 0.0247  111 TYR   b CB  
48599 C  CG  . TYR   BA 111 ? 1.7667 0.5103 1.0735 -0.0061 -0.2973 0.0450  111 TYR   b CG  
48600 C  CD1 . TYR   BA 111 ? 1.7661 0.4786 1.1418 -0.0615 -0.2972 0.0173  111 TYR   b CD1 
48601 C  CD2 . TYR   BA 111 ? 1.7558 0.4909 1.0603 -0.0322 -0.3074 0.0339  111 TYR   b CD2 
48602 C  CE1 . TYR   BA 111 ? 1.7796 0.4289 1.2000 -0.0587 -0.3247 -0.0210 111 TYR   b CE1 
48603 C  CE2 . TYR   BA 111 ? 1.7421 0.4195 1.1220 -0.0565 -0.3323 -0.0045 111 TYR   b CE2 
48604 C  CZ  . TYR   BA 111 ? 1.7714 0.3103 1.1788 -0.0429 -0.3488 -0.0088 111 TYR   b CZ  
48605 O  OH  . TYR   BA 111 ? 1.8554 0.2229 1.2524 -0.0557 -0.3320 -0.0616 111 TYR   b OH  
48606 N  N   . THR   BA 112 ? 1.6385 0.4647 1.0348 0.0135  -0.3343 0.0302  112 THR   b N   
48607 C  CA  . THR   BA 112 ? 1.6034 0.5111 1.0055 0.0085  -0.3461 0.0353  112 THR   b CA  
48608 C  C   . THR   BA 112 ? 1.5892 0.4863 1.0153 0.0012  -0.3300 0.0450  112 THR   b C   
48609 O  O   . THR   BA 112 ? 1.6075 0.5036 1.0152 0.0210  -0.2774 0.0303  112 THR   b O   
48610 C  CB  . THR   BA 112 ? 1.5945 0.4850 0.9898 0.0444  -0.3875 0.0650  112 THR   b CB  
48611 O  OG1 . THR   BA 112 ? 1.6031 0.4613 1.0297 0.0803  -0.3846 0.0439  112 THR   b OG1 
48612 C  CG2 . THR   BA 112 ? 1.6197 0.4776 1.0234 0.0114  -0.3715 0.0515  112 THR   b CG2 
48613 N  N   . ILE   BA 113 ? 1.5770 0.4726 1.0014 -0.0526 -0.3195 0.0439  113 ILE   b N   
48614 C  CA  . ILE   BA 113 ? 1.6153 0.5706 1.0109 -0.0666 -0.2983 0.0309  113 ILE   b CA  
48615 C  C   . ILE   BA 113 ? 1.6212 0.6192 0.9791 -0.0521 -0.3190 0.0326  113 ILE   b C   
48616 O  O   . ILE   BA 113 ? 1.6165 0.6979 0.9477 -0.0346 -0.2960 -0.0133 113 ILE   b O   
48617 C  CB  . ILE   BA 113 ? 1.6553 0.5655 1.0298 -0.0773 -0.3150 0.0487  113 ILE   b CB  
48618 C  CG1 . ILE   BA 113 ? 1.7152 0.6012 1.0753 -0.0582 -0.3300 0.0730  113 ILE   b CG1 
48619 C  CG2 . ILE   BA 113 ? 1.6548 0.5685 1.0296 -0.0693 -0.3166 0.0520  113 ILE   b CG2 
48620 C  CD1 . ILE   BA 113 ? 1.7752 0.5893 1.1064 -0.0636 -0.3331 0.0633  113 ILE   b CD1 
48621 N  N   . PRO   BA 114 ? 1.6541 0.5804 1.0134 -0.0486 -0.3273 0.0366  114 PRO   b N   
48622 C  CA  . PRO   BA 114 ? 1.6788 0.5454 1.0636 -0.0305 -0.3064 0.0232  114 PRO   b CA  
48623 C  C   . PRO   BA 114 ? 1.7284 0.5800 1.0508 -0.0172 -0.2971 0.0414  114 PRO   b C   
48624 O  O   . PRO   BA 114 ? 1.7483 0.5705 1.0812 -0.0097 -0.2392 0.0598  114 PRO   b O   
48625 C  CB  . PRO   BA 114 ? 1.6441 0.6399 1.0741 -0.0394 -0.3220 0.0241  114 PRO   b CB  
48626 C  CG  . PRO   BA 114 ? 1.6681 0.5837 1.0521 -0.0473 -0.3101 0.0298  114 PRO   b CG  
48627 C  CD  . PRO   BA 114 ? 1.6571 0.5960 1.0448 -0.0780 -0.3203 0.0163  114 PRO   b CD  
48628 N  N   . LEU   BA 115 ? 1.7407 0.5715 1.0490 -0.0042 -0.3066 0.0361  115 LEU   b N   
48629 C  CA  . LEU   BA 115 ? 1.7375 0.6080 1.0417 0.0222  -0.2758 0.0245  115 LEU   b CA  
48630 C  C   . LEU   BA 115 ? 1.7660 0.6130 1.1288 0.1134  -0.2369 0.1294  115 LEU   b C   
48631 O  O   . LEU   BA 115 ? 1.7398 0.8083 1.0775 0.1368  -0.2893 0.0880  115 LEU   b O   
48632 C  CB  . LEU   BA 115 ? 1.6860 0.6215 1.0729 -0.0112 -0.2569 0.0421  115 LEU   b CB  
48633 C  CG  . LEU   BA 115 ? 1.6872 0.6551 1.0339 -0.0158 -0.2910 0.0686  115 LEU   b CG  
48634 C  CD1 . LEU   BA 115 ? 1.6753 0.7209 1.0769 -0.0349 -0.2693 0.0632  115 LEU   b CD1 
48635 C  CD2 . LEU   BA 115 ? 1.6640 0.6640 0.9887 -0.0249 -0.3077 0.0902  115 LEU   b CD2 
48636 N  N   . GLY   BA 116 ? 1.7770 0.3702 1.1633 0.0934  -0.2316 0.1224  116 GLY   b N   
48637 C  CA  . GLY   BA 116 ? 1.8067 0.4544 1.2323 0.0963  -0.1964 0.0916  116 GLY   b CA  
48638 C  C   . GLY   BA 116 ? 1.8689 0.4402 1.1973 0.0668  -0.1946 -0.0358 116 GLY   b C   
48639 O  O   . GLY   BA 116 ? 1.9593 0.2359 1.2418 -0.0386 -0.2766 -0.0796 116 GLY   b O   
48640 N  N   . GLY   BA 117 ? 1.8557 0.4105 1.2658 -0.0105 -0.1936 -0.0223 117 GLY   b N   
48641 C  CA  . GLY   BA 117 ? 1.7387 0.3856 1.2763 -0.0520 -0.2194 -0.0770 117 GLY   b CA  
48642 C  C   . GLY   BA 117 ? 1.6820 0.3875 1.3159 -0.0417 -0.2024 -0.0981 117 GLY   b C   
48643 O  O   . GLY   BA 117 ? 1.5772 0.3467 1.3752 -0.1262 -0.2292 -0.1622 117 GLY   b O   
48644 N  N   . SER   BA 118 ? 1.6018 0.4505 1.2641 -0.0362 -0.2352 -0.0788 118 SER   b N   
48645 C  CA  . SER   BA 118 ? 1.5801 0.4267 1.2507 -0.0093 -0.2091 -0.0586 118 SER   b CA  
48646 C  C   . SER   BA 118 ? 1.5706 0.4181 1.2548 0.0120  -0.2206 -0.0166 118 SER   b C   
48647 O  O   . SER   BA 118 ? 1.5722 0.4295 1.2345 0.0255  -0.2189 0.0688  118 SER   b O   
48648 C  CB  . SER   BA 118 ? 1.5540 0.4592 1.2439 -0.0067 -0.2165 -0.1109 118 SER   b CB  
48649 O  OG  . SER   BA 118 ? 1.5586 0.3966 1.2288 -0.0713 -0.2172 -0.1929 118 SER   b OG  
48650 N  N   . VAL   BA 119 ? 1.5668 0.3987 1.2222 0.0017  -0.2036 -0.0197 119 VAL   b N   
48651 C  CA  . VAL   BA 119 ? 1.5854 0.4072 1.2385 -0.0009 -0.2053 0.0068  119 VAL   b CA  
48652 C  C   . VAL   BA 119 ? 1.5808 0.4533 1.2479 -0.0199 -0.2075 0.0081  119 VAL   b C   
48653 O  O   . VAL   BA 119 ? 1.5893 0.5570 1.3490 -0.0649 -0.1980 0.0360  119 VAL   b O   
48654 C  CB  . VAL   BA 119 ? 1.6176 0.4111 1.2339 0.0132  -0.2032 0.0288  119 VAL   b CB  
48655 C  CG1 . VAL   BA 119 ? 1.6110 0.4178 1.2090 0.0461  -0.1868 0.0175  119 VAL   b CG1 
48656 C  CG2 . VAL   BA 119 ? 1.6491 0.4506 1.2252 -0.0055 -0.1951 0.0367  119 VAL   b CG2 
48657 N  N   . HIS   BA 120 ? 1.5862 0.4636 1.2270 -0.0070 -0.2079 0.0184  120 HIS   b N   
48658 C  CA  . HIS   BA 120 ? 1.6325 0.4740 1.2241 0.0065  -0.1911 -0.0099 120 HIS   b CA  
48659 C  C   . HIS   BA 120 ? 1.6505 0.4464 1.2581 0.0110  -0.1850 0.0162  120 HIS   b C   
48660 O  O   . HIS   BA 120 ? 1.6410 0.4966 1.3643 -0.0003 -0.1904 -0.0039 120 HIS   b O   
48661 C  CB  . HIS   BA 120 ? 1.6470 0.4773 1.2235 0.0164  -0.2055 0.0050  120 HIS   b CB  
48662 C  CG  . HIS   BA 120 ? 1.6785 0.4523 1.2446 0.0234  -0.1883 0.0042  120 HIS   b CG  
48663 N  ND1 . HIS   BA 120 ? 1.6654 0.4614 1.2813 0.0240  -0.2158 -0.0194 120 HIS   b ND1 
48664 C  CD2 . HIS   BA 120 ? 1.6756 0.4470 1.2900 0.0475  -0.2066 -0.0028 120 HIS   b CD2 
48665 C  CE1 . HIS   BA 120 ? 1.6801 0.4850 1.3014 0.0324  -0.1782 -0.0116 120 HIS   b CE1 
48666 N  NE2 . HIS   BA 120 ? 1.6784 0.4556 1.3429 0.0413  -0.1764 -0.0120 120 HIS   b NE2 
48667 N  N   . LYS   BA 121 ? 1.6999 0.4127 1.2141 0.0020  -0.1964 0.0102  121 LYS   b N   
48668 C  CA  . LYS   BA 121 ? 1.7141 0.4712 1.1610 -0.0094 -0.2502 0.0043  121 LYS   b CA  
48669 C  C   . LYS   BA 121 ? 1.6709 0.4308 1.1440 0.0236  -0.2643 0.0314  121 LYS   b C   
48670 O  O   . LYS   BA 121 ? 1.6430 0.5353 1.2449 0.0401  -0.2651 0.0137  121 LYS   b O   
48671 C  CB  . LYS   BA 121 ? 1.7251 0.4498 1.1207 -0.0134 -0.2571 -0.0476 121 LYS   b CB  
48672 C  CG  . LYS   BA 121 ? 1.7482 0.4794 1.0828 -0.0713 -0.2659 -0.0815 121 LYS   b CG  
48673 C  CD  . LYS   BA 121 ? 1.7425 0.4692 1.0413 -0.0893 -0.2650 -0.0755 121 LYS   b CD  
48674 C  CE  . LYS   BA 121 ? 1.7670 0.5420 1.0572 -0.1343 -0.2387 -0.0804 121 LYS   b CE  
48675 N  NZ  . LYS   BA 121 ? 1.7811 0.5425 1.0942 -0.1882 -0.2380 -0.1113 121 LYS   b NZ  
48676 N  N   . LEU   BA 122 ? 1.6589 0.4900 1.1159 0.0331  -0.2462 0.1184  122 LEU   b N   
48677 C  CA  . LEU   BA 122 ? 1.6812 0.5023 1.0587 0.0129  -0.2297 0.1423  122 LEU   b CA  
48678 C  C   . LEU   BA 122 ? 1.7258 0.5197 1.0416 -0.0052 -0.2594 0.1986  122 LEU   b C   
48679 O  O   . LEU   BA 122 ? 1.7191 0.5758 1.0452 -0.0304 -0.2511 0.3619  122 LEU   b O   
48680 C  CB  . LEU   BA 122 ? 1.7123 0.4392 1.0721 0.0013  -0.2162 0.1127  122 LEU   b CB  
48681 C  CG  . LEU   BA 122 ? 1.7128 0.3896 1.0763 0.0076  -0.2026 0.0945  122 LEU   b CG  
48682 C  CD1 . LEU   BA 122 ? 1.7081 0.4373 1.0513 0.0357  -0.2079 0.0773  122 LEU   b CD1 
48683 C  CD2 . LEU   BA 122 ? 1.7023 0.3954 1.0864 0.0208  -0.2221 0.0872  122 LEU   b CD2 
48684 N  N   . PRO   BA 123 ? 1.7219 0.4508 1.0352 -0.0253 -0.2342 0.2043  123 PRO   b N   
48685 C  CA  . PRO   BA 123 ? 1.7254 0.4623 1.0180 -0.0140 -0.2396 0.1810  123 PRO   b CA  
48686 C  C   . PRO   BA 123 ? 1.7159 0.4250 1.0157 -0.0133 -0.2168 0.1440  123 PRO   b C   
48687 O  O   . PRO   BA 123 ? 1.7413 0.2599 0.9781 0.0325  -0.2343 0.1645  123 PRO   b O   
48688 C  CB  . PRO   BA 123 ? 1.7372 0.4890 1.0135 -0.0379 -0.2454 0.1961  123 PRO   b CB  
48689 C  CG  . PRO   BA 123 ? 1.7271 0.5136 1.0333 -0.0276 -0.2522 0.1959  123 PRO   b CG  
48690 C  CD  . PRO   BA 123 ? 1.7152 0.4932 1.0324 -0.0289 -0.2459 0.1749  123 PRO   b CD  
48691 N  N   . TYR   BA 124 ? 1.6991 0.4748 1.0051 0.0142  -0.2376 0.1542  124 TYR   b N   
48692 C  CA  . TYR   BA 124 ? 1.7009 0.5646 1.0155 -0.0045 -0.2669 0.1683  124 TYR   b CA  
48693 C  C   . TYR   BA 124 ? 1.6834 0.5299 1.0064 -0.0323 -0.2530 0.1443  124 TYR   b C   
48694 O  O   . TYR   BA 124 ? 1.6967 0.6061 1.0777 -0.0240 -0.2050 0.1704  124 TYR   b O   
48695 C  CB  . TYR   BA 124 ? 1.6971 0.5870 1.0476 0.0345  -0.2576 0.1854  124 TYR   b CB  
48696 C  CG  . TYR   BA 124 ? 1.6991 0.5879 1.1286 0.0348  -0.2728 0.1861  124 TYR   b CG  
48697 C  CD1 . TYR   BA 124 ? 1.7011 0.6506 1.1900 0.0468  -0.2876 0.1856  124 TYR   b CD1 
48698 C  CD2 . TYR   BA 124 ? 1.6380 0.6048 1.2188 0.0722  -0.2711 0.1491  124 TYR   b CD2 
48699 C  CE1 . TYR   BA 124 ? 1.6828 0.6261 1.2323 0.0863  -0.2788 0.1959  124 TYR   b CE1 
48700 C  CE2 . TYR   BA 124 ? 1.6671 0.5912 1.2564 0.0817  -0.2534 0.1649  124 TYR   b CE2 
48701 C  CZ  . TYR   BA 124 ? 1.6805 0.4751 1.2555 0.0316  -0.2398 0.1693  124 TYR   b CZ  
48702 O  OH  . TYR   BA 124 ? 1.7235 0.4144 1.1797 0.0838  -0.2065 0.1421  124 TYR   b OH  
48703 N  N   . ALA   BA 125 ? 1.6947 0.5632 0.9907 -0.0559 -0.2639 0.0763  125 ALA   b N   
48704 C  CA  . ALA   BA 125 ? 1.6606 0.6174 0.9580 -0.0306 -0.3172 0.0504  125 ALA   b CA  
48705 C  C   . ALA   BA 125 ? 1.6831 0.5973 0.9272 -0.0140 -0.3008 0.0468  125 ALA   b C   
48706 O  O   . ALA   BA 125 ? 1.6823 0.6499 0.8431 0.0213  -0.2886 0.0664  125 ALA   b O   
48707 C  CB  . ALA   BA 125 ? 1.6880 0.5904 0.9654 -0.0304 -0.3138 0.0631  125 ALA   b CB  
48708 N  N   . ILE   BA 126 ? 1.7037 0.5396 1.0197 -0.0420 -0.2823 0.0180  126 ILE   b N   
48709 C  CA  . ILE   BA 126 ? 1.6800 0.5295 1.0680 -0.0572 -0.2737 0.0258  126 ILE   b CA  
48710 C  C   . ILE   BA 126 ? 1.6348 0.4822 1.0747 -0.0595 -0.2883 0.0497  126 ILE   b C   
48711 O  O   . ILE   BA 126 ? 1.6731 0.5612 1.0872 -0.0633 -0.2390 0.0768  126 ILE   b O   
48712 C  CB  . ILE   BA 126 ? 1.6709 0.5686 1.0841 -0.0372 -0.2647 -0.0137 126 ILE   b CB  
48713 C  CG1 . ILE   BA 126 ? 1.6498 0.6819 1.1403 -0.0492 -0.2822 -0.0358 126 ILE   b CG1 
48714 C  CG2 . ILE   BA 126 ? 1.6566 0.5470 1.0983 -0.0466 -0.2372 -0.0066 126 ILE   b CG2 
48715 C  CD1 . ILE   BA 126 ? 1.6456 0.6819 1.1493 -0.0462 -0.2938 -0.0205 126 ILE   b CD1 
48716 N  N   . ALA   BA 127 ? 1.6488 0.4267 1.0867 -0.0579 -0.3062 0.0423  127 ALA   b N   
48717 C  CA  . ALA   BA 127 ? 1.6708 0.4638 1.0878 -0.0594 -0.2898 0.0486  127 ALA   b CA  
48718 C  C   . ALA   BA 127 ? 1.6472 0.4646 1.1198 -0.0692 -0.2645 0.0231  127 ALA   b C   
48719 O  O   . ALA   BA 127 ? 1.6413 0.4006 1.0201 -0.1224 -0.3110 -0.0855 127 ALA   b O   
48720 C  CB  . ALA   BA 127 ? 1.6512 0.4354 1.1062 0.0183  -0.2825 0.1005  127 ALA   b CB  
48721 N  N   . GLY   BA 128 ? 1.6685 0.4736 1.1648 -0.0648 -0.2676 0.0978  128 GLY   b N   
48722 C  CA  . GLY   BA 128 ? 1.6482 0.5643 1.1619 -0.0429 -0.2528 0.0780  128 GLY   b CA  
48723 C  C   . GLY   BA 128 ? 1.6497 0.5634 1.1754 -0.0243 -0.2135 0.0215  128 GLY   b C   
48724 O  O   . GLY   BA 128 ? 1.7228 0.6392 1.1362 -0.0554 -0.2224 -0.0776 128 GLY   b O   
48725 N  N   . SER   BA 129 ? 1.6239 0.5666 1.1742 -0.0002 -0.1694 0.0165  129 SER   b N   
48726 C  CA  . SER   BA 129 ? 1.6189 0.5642 1.1610 -0.0294 -0.1583 0.0241  129 SER   b CA  
48727 C  C   . SER   BA 129 ? 1.6585 0.5376 1.1722 -0.0279 -0.1349 0.0255  129 SER   b C   
48728 O  O   . SER   BA 129 ? 1.6850 0.6168 1.2735 -0.0924 -0.0829 0.0507  129 SER   b O   
48729 C  CB  . SER   BA 129 ? 1.6366 0.4898 1.1296 -0.0226 -0.1501 0.0227  129 SER   b CB  
48730 O  OG  . SER   BA 129 ? 1.6552 0.4638 1.1361 -0.0010 -0.1227 0.0331  129 SER   b OG  
48731 N  N   . GLY   BA 130 ? 1.6300 0.4680 1.1889 -0.0395 -0.1493 0.0319  130 GLY   b N   
48732 C  CA  . GLY   BA 130 ? 1.5913 0.4347 1.1640 -0.0150 -0.1526 0.0608  130 GLY   b CA  
48733 C  C   . GLY   BA 130 ? 1.6393 0.4004 1.0912 -0.0316 -0.1841 0.0641  130 GLY   b C   
48734 O  O   . GLY   BA 130 ? 1.5636 0.4026 1.0526 0.0306  -0.1984 0.0679  130 GLY   b O   
48735 N  N   . SER   BA 131 ? 1.6366 0.4534 1.0953 0.0126  -0.2014 0.1007  131 SER   b N   
48736 C  CA  . SER   BA 131 ? 1.6865 0.5596 1.0976 -0.0384 -0.2668 0.1140  131 SER   b CA  
48737 C  C   . SER   BA 131 ? 1.7201 0.4746 1.0998 0.0268  -0.2437 0.0034  131 SER   b C   
48738 O  O   . SER   BA 131 ? 1.7599 0.4274 1.0964 0.0344  -0.2335 -0.0367 131 SER   b O   
48739 C  CB  . SER   BA 131 ? 1.7153 0.5771 1.0772 -0.0541 -0.2598 0.1188  131 SER   b CB  
48740 O  OG  . SER   BA 131 ? 1.7469 0.7258 1.0444 -0.1262 -0.3268 0.1488  131 SER   b OG  
48741 N  N   . THR   BA 132 ? 1.7093 0.5205 1.0752 0.0783  -0.2347 0.0047  132 THR   b N   
48742 C  CA  . THR   BA 132 ? 1.6643 0.5966 1.1259 0.0544  -0.2231 -0.0018 132 THR   b CA  
48743 C  C   . THR   BA 132 ? 1.6505 0.5636 1.1316 0.0567  -0.2034 0.0106  132 THR   b C   
48744 O  O   . THR   BA 132 ? 1.6958 0.5741 1.1415 0.0499  -0.2516 0.0067  132 THR   b O   
48745 C  CB  . THR   BA 132 ? 1.6502 0.7069 1.1413 0.1133  -0.2608 0.0153  132 THR   b CB  
48746 O  OG1 . THR   BA 132 ? 1.6568 0.7661 1.1709 0.1374  -0.2661 -0.0091 132 THR   b OG1 
48747 C  CG2 . THR   BA 132 ? 1.6329 0.7306 1.1371 0.1293  -0.2664 0.0193  132 THR   b CG2 
48748 N  N   . PHE   BA 133 ? 1.6565 0.4695 1.1106 0.0514  -0.1857 0.0141  133 PHE   b N   
48749 C  CA  . PHE   BA 133 ? 1.6311 0.4442 1.1072 0.0567  -0.1673 0.0308  133 PHE   b CA  
48750 C  C   . PHE   BA 133 ? 1.6148 0.4194 1.1011 0.0629  -0.1193 0.0462  133 PHE   b C   
48751 O  O   . PHE   BA 133 ? 1.6181 0.3497 1.1510 0.1195  0.0146  0.0481  133 PHE   b O   
48752 C  CB  . PHE   BA 133 ? 1.6343 0.4368 1.0940 0.0653  -0.1747 0.0104  133 PHE   b CB  
48753 C  CG  . PHE   BA 133 ? 1.6596 0.5172 1.1008 0.0885  -0.1991 0.0034  133 PHE   b CG  
48754 C  CD1 . PHE   BA 133 ? 1.6894 0.5182 1.0907 0.0849  -0.2110 0.0071  133 PHE   b CD1 
48755 C  CD2 . PHE   BA 133 ? 1.6447 0.5017 1.0937 0.0818  -0.1965 0.0275  133 PHE   b CD2 
48756 C  CE1 . PHE   BA 133 ? 1.7033 0.5228 1.0886 0.0905  -0.2048 0.0153  133 PHE   b CE1 
48757 C  CE2 . PHE   BA 133 ? 1.6520 0.5590 1.0912 0.1003  -0.2066 0.0285  133 PHE   b CE2 
48758 C  CZ  . PHE   BA 133 ? 1.6724 0.5654 1.0769 0.0950  -0.2099 0.0310  133 PHE   b CZ  
48759 N  N   . ILE   BA 134 ? 1.5979 0.4235 1.0415 0.0510  -0.1502 0.0729  134 ILE   b N   
48760 C  CA  . ILE   BA 134 ? 1.6311 0.4197 1.0443 0.0453  -0.1674 0.0756  134 ILE   b CA  
48761 C  C   . ILE   BA 134 ? 1.6463 0.3422 1.0269 0.0413  -0.1793 0.1179  134 ILE   b C   
48762 O  O   . ILE   BA 134 ? 1.6706 0.3206 1.0549 0.1001  -0.1852 0.1200  134 ILE   b O   
48763 C  CB  . ILE   BA 134 ? 1.6057 0.4561 1.0189 0.0401  -0.1768 0.0751  134 ILE   b CB  
48764 C  CG1 . ILE   BA 134 ? 1.5992 0.4702 1.0460 0.0347  -0.1952 0.0568  134 ILE   b CG1 
48765 C  CG2 . ILE   BA 134 ? 1.6126 0.4479 0.9795 0.0450  -0.1726 0.0767  134 ILE   b CG2 
48766 C  CD1 . ILE   BA 134 ? 1.5918 0.4788 1.0454 0.0427  -0.1921 0.0732  134 ILE   b CD1 
48767 N  N   . TYR   BA 135 ? 1.6503 0.3222 1.0217 0.0211  -0.1851 0.1174  135 TYR   b N   
48768 C  CA  . TYR   BA 135 ? 1.6605 0.3683 1.0248 0.0325  -0.2162 0.1081  135 TYR   b CA  
48769 C  C   . TYR   BA 135 ? 1.6933 0.4029 1.0406 -0.0028 -0.2315 0.1043  135 TYR   b C   
48770 O  O   . TYR   BA 135 ? 1.6965 0.2279 1.0276 -0.0500 -0.2501 0.0269  135 TYR   b O   
48771 C  CB  . TYR   BA 135 ? 1.6706 0.4330 1.0388 0.0393  -0.1918 0.0901  135 TYR   b CB  
48772 C  CG  . TYR   BA 135 ? 1.7013 0.4808 1.0710 0.0547  -0.1982 0.0522  135 TYR   b CG  
48773 C  CD1 . TYR   BA 135 ? 1.7196 0.5304 1.0551 0.0926  -0.2067 0.0520  135 TYR   b CD1 
48774 C  CD2 . TYR   BA 135 ? 1.6904 0.5673 1.0982 0.0520  -0.2044 -0.0175 135 TYR   b CD2 
48775 C  CE1 . TYR   BA 135 ? 1.7570 0.6426 1.0388 0.1165  -0.1976 0.0131  135 TYR   b CE1 
48776 C  CE2 . TYR   BA 135 ? 1.7369 0.6538 1.1000 0.0707  -0.1790 -0.0596 135 TYR   b CE2 
48777 C  CZ  . TYR   BA 135 ? 1.7314 0.7505 1.1045 0.1263  -0.2037 0.0027  135 TYR   b CZ  
48778 O  OH  . TYR   BA 135 ? 1.8978 0.7746 1.2226 0.0991  -0.1432 -0.0756 135 TYR   b OH  
48779 N  N   . GLY   BA 136 ? 1.7317 0.4133 1.0354 -0.0197 -0.2395 0.0666  136 GLY   b N   
48780 C  CA  . GLY   BA 136 ? 1.7541 0.5043 0.9992 -0.0130 -0.2344 0.0655  136 GLY   b CA  
48781 C  C   . GLY   BA 136 ? 1.6950 0.5028 0.9927 0.0205  -0.2785 0.1039  136 GLY   b C   
48782 O  O   . GLY   BA 136 ? 1.7885 0.4153 0.9649 0.0814  -0.2528 0.1698  136 GLY   b O   
48783 N  N   . TYR   BA 137 ? 1.6868 0.5755 1.0093 -0.0106 -0.2867 0.0587  137 TYR   b N   
48784 C  CA  . TYR   BA 137 ? 1.6522 0.6558 0.9508 -0.0059 -0.3070 0.0204  137 TYR   b CA  
48785 C  C   . TYR   BA 137 ? 1.6073 0.6947 0.9598 0.0058  -0.3344 0.0601  137 TYR   b C   
48786 O  O   . TYR   BA 137 ? 1.5785 0.7821 0.9116 -0.0506 -0.3132 0.0062  137 TYR   b O   
48787 C  CB  . TYR   BA 137 ? 1.6563 0.6541 0.9369 0.0049  -0.3046 -0.0087 137 TYR   b CB  
48788 C  CG  . TYR   BA 137 ? 1.7171 0.6968 0.8933 -0.0151 -0.3049 -0.0376 137 TYR   b CG  
48789 C  CD1 . TYR   BA 137 ? 1.7535 0.7510 0.8761 -0.0445 -0.3345 -0.0707 137 TYR   b CD1 
48790 C  CD2 . TYR   BA 137 ? 1.7460 0.7099 0.9096 -0.0341 -0.2990 -0.0419 137 TYR   b CD2 
48791 C  CE1 . TYR   BA 137 ? 1.7678 0.7985 0.8833 -0.0599 -0.3263 -0.0669 137 TYR   b CE1 
48792 C  CE2 . TYR   BA 137 ? 1.7638 0.7836 0.8749 -0.0194 -0.2956 -0.0557 137 TYR   b CE2 
48793 C  CZ  . TYR   BA 137 ? 1.7633 0.7976 0.8608 -0.0516 -0.3156 -0.0721 137 TYR   b CZ  
48794 O  OH  . TYR   BA 137 ? 1.7703 0.9500 0.8513 -0.0494 -0.3137 -0.0517 137 TYR   b OH  
48795 N  N   . CYS   BA 138 ? 1.6013 0.6851 0.9875 0.0294  -0.3147 0.0549  138 CYS   b N   
48796 C  CA  . CYS   BA 138 ? 1.6292 0.6937 1.0061 0.0299  -0.2838 0.1297  138 CYS   b CA  
48797 C  C   . CYS   BA 138 ? 1.6471 0.7094 1.0797 0.0570  -0.2914 0.1483  138 CYS   b C   
48798 O  O   . CYS   BA 138 ? 1.7441 0.8173 1.1137 -0.0434 -0.2263 0.2497  138 CYS   b O   
48799 C  CB  . CYS   BA 138 ? 1.6193 0.6215 0.9892 0.0337  -0.2706 0.1554  138 CYS   b CB  
48800 S  SG  . CYS   BA 138 ? 1.6080 0.6163 0.9997 0.0072  -0.2012 0.1097  138 CYS   b SG  
48801 N  N   . ASP   BA 139 ? 1.6374 0.6755 1.1068 0.0781  -0.2733 0.1233  139 ASP   b N   
48802 C  CA  . ASP   BA 139 ? 1.6504 0.6765 1.1196 0.0900  -0.3034 0.0941  139 ASP   b CA  
48803 C  C   . ASP   BA 139 ? 1.6922 0.6820 1.1523 0.1272  -0.3339 0.0393  139 ASP   b C   
48804 O  O   . ASP   BA 139 ? 1.7038 0.7363 1.1373 0.1536  -0.3533 0.0106  139 ASP   b O   
48805 C  CB  . ASP   BA 139 ? 1.6150 0.6263 1.1611 0.0834  -0.3242 0.0984  139 ASP   b CB  
48806 C  CG  . ASP   BA 139 ? 1.6168 0.6806 1.1847 0.0830  -0.3343 0.1390  139 ASP   b CG  
48807 O  OD1 . ASP   BA 139 ? 1.5713 0.6866 1.1648 0.0828  -0.3460 0.1979  139 ASP   b OD1 
48808 O  OD2 . ASP   BA 139 ? 1.5488 0.7229 1.2419 0.1182  -0.3905 0.0863  139 ASP   b OD2 
48809 N  N   . LYS   BA 140 ? 1.7365 0.7356 1.1384 0.1473  -0.3342 -0.0091 140 LYS   b N   
48810 C  CA  . LYS   BA 140 ? 1.7666 0.8122 1.1063 0.1154  -0.3531 0.0086  140 LYS   b CA  
48811 C  C   . LYS   BA 140 ? 1.8208 0.7140 1.0206 0.1371  -0.3966 -0.0053 140 LYS   b C   
48812 O  O   . LYS   BA 140 ? 1.9475 0.6921 0.9778 0.1754  -0.3623 0.0446  140 LYS   b O   
48813 C  CB  . LYS   BA 140 ? 1.7520 0.8275 1.1788 0.1210  -0.3481 -0.0605 140 LYS   b CB  
48814 C  CG  . LYS   BA 140 ? 1.7073 0.9014 1.2749 0.0723  -0.3569 -0.0951 140 LYS   b CG  
48815 C  CD  . LYS   BA 140 ? 1.7204 0.9838 1.3195 0.0861  -0.3825 -0.1328 140 LYS   b CD  
48816 C  CE  . LYS   BA 140 ? 1.7202 0.9745 1.3789 0.0651  -0.4153 -0.2007 140 LYS   b CE  
48817 N  NZ  . LYS   BA 140 ? 1.7315 1.0064 1.4294 0.0566  -0.4402 -0.2443 140 LYS   b NZ  
48818 N  N   . ASN   BA 141 ? 1.8159 0.6883 1.0105 0.1127  -0.3690 0.0390  141 ASN   b N   
48819 C  CA  . ASN   BA 141 ? 1.8478 0.8549 1.0055 0.0648  -0.3293 0.0062  141 ASN   b CA  
48820 C  C   . ASN   BA 141 ? 1.8575 0.8661 1.0432 0.0736  -0.3038 -0.0135 141 ASN   b C   
48821 O  O   . ASN   BA 141 ? 1.8751 0.9007 1.0779 0.0329  -0.2473 -0.0087 141 ASN   b O   
48822 C  CB  . ASN   BA 141 ? 1.8415 0.8399 1.0477 0.0715  -0.2911 -0.0099 141 ASN   b CB  
48823 C  CG  . ASN   BA 141 ? 1.9168 0.8926 1.0201 0.0133  -0.2459 -0.0918 141 ASN   b CG  
48824 O  OD1 . ASN   BA 141 ? 1.9702 0.9064 1.1665 -0.0597 -0.1705 -0.0103 141 ASN   b OD1 
48825 N  ND2 . ASN   BA 141 ? 1.9199 0.9961 0.9890 -0.0074 -0.3300 -0.0877 141 ASN   b ND2 
48826 N  N   . PHE   BA 142 ? 1.8714 0.8596 1.0749 0.0572  -0.3037 -0.0521 142 PHE   b N   
48827 C  CA  . PHE   BA 142 ? 1.8693 0.8433 1.1449 0.0222  -0.3242 -0.0012 142 PHE   b CA  
48828 C  C   . PHE   BA 142 ? 1.8482 0.8674 1.1134 -0.0342 -0.3536 -0.0691 142 PHE   b C   
48829 O  O   . PHE   BA 142 ? 1.8844 0.7255 1.0165 -0.0202 -0.4425 -0.0817 142 PHE   b O   
48830 C  CB  . PHE   BA 142 ? 1.8700 0.8230 1.2020 0.0485  -0.2990 -0.0220 142 PHE   b CB  
48831 C  CG  . PHE   BA 142 ? 1.8017 0.8123 1.2544 0.0249  -0.3349 0.0231  142 PHE   b CG  
48832 C  CD1 . PHE   BA 142 ? 1.7968 0.7730 1.2494 0.0370  -0.3317 0.0480  142 PHE   b CD1 
48833 C  CD2 . PHE   BA 142 ? 1.8242 0.7743 1.2613 0.0681  -0.3715 0.0496  142 PHE   b CD2 
48834 C  CE1 . PHE   BA 142 ? 1.7553 0.7716 1.2330 0.0353  -0.3580 0.0910  142 PHE   b CE1 
48835 C  CE2 . PHE   BA 142 ? 1.7795 0.7616 1.2232 0.0471  -0.3821 0.0749  142 PHE   b CE2 
48836 C  CZ  . PHE   BA 142 ? 1.7705 0.7458 1.2283 0.0568  -0.3777 0.0859  142 PHE   b CZ  
48837 N  N   . ARG   BA 143 ? 1.9026 0.9440 1.1687 -0.0205 -0.3199 -0.0121 143 ARG   b N   
48838 C  CA  . ARG   BA 143 ? 1.9189 1.0313 1.2146 0.0340  -0.3372 -0.0263 143 ARG   b CA  
48839 C  C   . ARG   BA 143 ? 1.9342 1.0108 1.2125 0.1112  -0.3527 0.0164  143 ARG   b C   
48840 O  O   . ARG   BA 143 ? 1.8293 0.9811 1.2865 0.1959  -0.3122 0.0542  143 ARG   b O   
48841 C  CB  . ARG   BA 143 ? 1.9814 1.1400 1.2342 -0.0117 -0.2859 -0.0437 143 ARG   b CB  
48842 C  CG  . ARG   BA 143 ? 2.0165 1.2002 1.3347 -0.0674 -0.2296 -0.1273 143 ARG   b CG  
48843 C  CD  . ARG   BA 143 ? 2.0406 1.3468 1.4104 -0.0781 -0.1406 -0.1399 143 ARG   b CD  
48844 N  NE  . ARG   BA 143 ? 2.0352 1.3605 1.4723 -0.0876 -0.0569 -0.1377 143 ARG   b NE  
48845 C  CZ  . ARG   BA 143 ? 2.0907 1.3380 1.4762 -0.0874 -0.0042 -0.1631 143 ARG   b CZ  
48846 N  NH1 . ARG   BA 143 ? 2.1249 1.3419 1.4490 -0.0622 -0.0046 -0.1872 143 ARG   b NH1 
48847 N  NH2 . ARG   BA 143 ? 2.0948 1.2888 1.4735 -0.0679 0.0157  -0.1700 143 ARG   b NH2 
48848 N  N   . GLU   BA 144 ? 1.9419 1.0622 1.1318 0.1187  -0.4281 0.0271  144 GLU   b N   
48849 C  CA  . GLU   BA 144 ? 1.9545 1.0492 1.1103 0.0705  -0.4545 0.0399  144 GLU   b CA  
48850 C  C   . GLU   BA 144 ? 1.9993 0.9755 1.0521 0.0598  -0.5167 0.0154  144 GLU   b C   
48851 O  O   . GLU   BA 144 ? 2.0383 1.0588 1.0625 0.0254  -0.5301 -0.0049 144 GLU   b O   
48852 C  CB  . GLU   BA 144 ? 1.9551 0.9950 1.1088 0.0907  -0.4776 0.0480  144 GLU   b CB  
48853 C  CG  . GLU   BA 144 ? 1.9787 0.9954 1.1299 0.0981  -0.4506 0.0193  144 GLU   b CG  
48854 C  CD  . GLU   BA 144 ? 1.9595 1.0327 1.2138 0.0945  -0.4820 0.0184  144 GLU   b CD  
48855 O  OE1 . GLU   BA 144 ? 2.0352 1.1253 1.2385 0.0967  -0.4341 -0.0002 144 GLU   b OE1 
48856 O  OE2 . GLU   BA 144 ? 2.0740 1.0381 1.0928 0.1183  -0.5101 0.0395  144 GLU   b OE2 
48857 N  N   . ASN   BA 145 ? 2.0357 0.9203 1.0682 0.1019  -0.5099 0.0070  145 ASN   b N   
48858 C  CA  . ASN   BA 145 ? 2.0678 0.9083 1.0570 0.1156  -0.4853 -0.0002 145 ASN   b CA  
48859 C  C   . ASN   BA 145 ? 2.0908 0.8005 1.0083 0.1108  -0.4733 0.0454  145 ASN   b C   
48860 O  O   . ASN   BA 145 ? 2.1016 0.7470 1.0156 0.1486  -0.4489 0.0590  145 ASN   b O   
48861 C  CB  . ASN   BA 145 ? 2.0887 1.0205 1.1116 0.1032  -0.5361 -0.0093 145 ASN   b CB  
48862 C  CG  . ASN   BA 145 ? 2.1010 1.0816 1.1907 0.1074  -0.5198 -0.0456 145 ASN   b CG  
48863 O  OD1 . ASN   BA 145 ? 2.1128 1.2318 1.3474 0.0734  -0.4780 -0.0638 145 ASN   b OD1 
48864 N  ND2 . ASN   BA 145 ? 2.0598 1.0825 1.2166 0.0933  -0.5686 -0.0235 145 ASN   b ND2 
48865 N  N   . MET   BA 146 ? 2.0783 0.7446 1.0207 0.1276  -0.4053 0.0676  146 MET   b N   
48866 C  CA  . MET   BA 146 ? 2.0843 0.6783 1.0226 0.0933  -0.3513 0.1299  146 MET   b CA  
48867 C  C   . MET   BA 146 ? 2.1260 0.5958 1.0170 0.1124  -0.3590 0.1614  146 MET   b C   
48868 O  O   . MET   BA 146 ? 2.0757 0.5128 1.0364 0.0488  -0.3567 0.2364  146 MET   b O   
48869 C  CB  . MET   BA 146 ? 2.1256 0.6941 1.0356 0.1343  -0.3290 0.1409  146 MET   b CB  
48870 C  CG  . MET   BA 146 ? 2.1472 0.6575 1.0251 0.1671  -0.3175 0.1429  146 MET   b CG  
48871 S  SD  . MET   BA 146 ? 2.1788 0.5870 1.0505 0.2241  -0.2253 0.1525  146 MET   b SD  
48872 C  CE  . MET   BA 146 ? 2.1632 0.6155 1.0644 0.1843  -0.2693 0.1018  146 MET   b CE  
48873 N  N   . SER   BA 147 ? 2.1160 0.5645 1.0142 0.0499  -0.3229 0.2352  147 SER   b N   
48874 C  CA  . SER   BA 147 ? 2.1819 0.5725 1.0409 0.0339  -0.2879 0.2957  147 SER   b CA  
48875 C  C   . SER   BA 147 ? 2.1492 0.6420 1.0787 0.0184  -0.2902 0.2512  147 SER   b C   
48876 O  O   . SER   BA 147 ? 2.1417 0.6584 1.0463 -0.0684 -0.2665 0.2231  147 SER   b O   
48877 C  CB  . SER   BA 147 ? 2.2171 0.5625 1.0117 0.0309  -0.2827 0.3570  147 SER   b CB  
48878 O  OG  . SER   BA 147 ? 2.2247 0.5874 1.0208 0.0430  -0.2479 0.4021  147 SER   b OG  
48879 N  N   . LYS   BA 148 ? 2.1249 0.7324 1.1378 0.0017  -0.2475 0.2808  148 LYS   b N   
48880 C  CA  . LYS   BA 148 ? 2.0800 0.8415 1.1664 0.0306  -0.2329 0.2836  148 LYS   b CA  
48881 C  C   . LYS   BA 148 ? 2.0828 0.8702 1.2484 0.0445  -0.2234 0.2265  148 LYS   b C   
48882 O  O   . LYS   BA 148 ? 2.1402 0.9735 1.2081 0.0828  -0.2322 0.2020  148 LYS   b O   
48883 C  CB  . LYS   BA 148 ? 2.0327 0.8411 1.1916 0.0552  -0.2090 0.2720  148 LYS   b CB  
48884 C  CG  . LYS   BA 148 ? 2.0061 0.8633 1.1821 0.0887  -0.1912 0.2167  148 LYS   b CG  
48885 C  CD  . LYS   BA 148 ? 1.9857 0.9207 1.2270 0.0815  -0.1469 0.1565  148 LYS   b CD  
48886 C  CE  . LYS   BA 148 ? 1.9497 0.9679 1.2659 0.0763  -0.1313 0.1035  148 LYS   b CE  
48887 N  NZ  . LYS   BA 148 ? 1.9704 1.0212 1.3218 0.0577  -0.0895 0.0632  148 LYS   b NZ  
48888 N  N   . GLU   BA 149 ? 2.1194 0.9441 1.2252 -0.0226 -0.2120 0.2346  149 GLU   b N   
48889 C  CA  . GLU   BA 149 ? 2.1146 0.9228 1.3125 -0.0427 -0.2204 0.2419  149 GLU   b CA  
48890 C  C   . GLU   BA 149 ? 2.0907 0.9260 1.2352 -0.0601 -0.2270 0.2005  149 GLU   b C   
48891 O  O   . GLU   BA 149 ? 2.0661 0.8540 1.3399 -0.1051 -0.2216 0.2117  149 GLU   b O   
48892 C  CB  . GLU   BA 149 ? 2.1975 1.0180 1.3307 -0.0669 -0.2070 0.2332  149 GLU   b CB  
48893 C  CG  . GLU   BA 149 ? 2.2329 1.0361 1.5175 -0.0909 -0.1834 0.2368  149 GLU   b CG  
48894 C  CD  . GLU   BA 149 ? 2.3154 1.0338 1.6829 -0.0712 -0.2062 0.1805  149 GLU   b CD  
48895 O  OE1 . GLU   BA 149 ? 2.3433 0.9969 1.7353 -0.0621 -0.2705 0.1651  149 GLU   b OE1 
48896 O  OE2 . GLU   BA 149 ? 2.4713 0.9548 1.8716 -0.0922 -0.1936 0.0552  149 GLU   b OE2 
48897 N  N   . GLU   BA 150 ? 2.0900 0.8545 1.0849 -0.0271 -0.2368 0.2099  150 GLU   b N   
48898 C  CA  . GLU   BA 150 ? 2.0477 0.9033 1.0216 -0.0431 -0.2114 0.1597  150 GLU   b CA  
48899 C  C   . GLU   BA 150 ? 2.0041 0.9421 1.0141 -0.0580 -0.1650 0.0589  150 GLU   b C   
48900 O  O   . GLU   BA 150 ? 2.0082 1.0363 0.8589 -0.0871 -0.1289 0.1119  150 GLU   b O   
48901 C  CB  . GLU   BA 150 ? 2.0903 0.8966 0.9897 -0.0066 -0.2435 0.1598  150 GLU   b CB  
48902 C  CG  . GLU   BA 150 ? 2.1670 0.9669 0.9968 -0.0200 -0.2401 0.1248  150 GLU   b CG  
48903 C  CD  . GLU   BA 150 ? 2.1849 1.0271 0.9676 -0.0118 -0.2636 0.0469  150 GLU   b CD  
48904 O  OE1 . GLU   BA 150 ? 2.1906 1.0147 1.0013 -0.0214 -0.2955 -0.0001 150 GLU   b OE1 
48905 O  OE2 . GLU   BA 150 ? 2.2597 1.2327 0.9491 -0.0708 -0.3054 0.0269  150 GLU   b OE2 
48906 N  N   . THR   BA 151 ? 1.9439 0.8667 0.9612 -0.0412 -0.1451 0.1420  151 THR   b N   
48907 C  CA  . THR   BA 151 ? 1.8905 0.7928 0.9545 -0.0277 -0.1587 0.1549  151 THR   b CA  
48908 C  C   . THR   BA 151 ? 1.8466 0.8437 0.9845 -0.0219 -0.1462 0.1107  151 THR   b C   
48909 O  O   . THR   BA 151 ? 1.7932 0.9103 0.9411 0.0417  -0.1958 0.0938  151 THR   b O   
48910 C  CB  . THR   BA 151 ? 1.8866 0.7425 0.9176 -0.0705 -0.1632 0.1908  151 THR   b CB  
48911 O  OG1 . THR   BA 151 ? 1.8936 0.6423 0.9182 -0.0822 -0.1751 0.1690  151 THR   b OG1 
48912 C  CG2 . THR   BA 151 ? 1.8748 0.7276 0.9139 -0.0562 -0.1758 0.1778  151 THR   b CG2 
48913 N  N   . VAL   BA 152 ? 1.8565 0.7983 0.9536 -0.0318 -0.1611 0.1379  152 VAL   b N   
48914 C  CA  . VAL   BA 152 ? 1.8689 0.8867 0.9984 -0.0215 -0.1806 0.1102  152 VAL   b CA  
48915 C  C   . VAL   BA 152 ? 1.9283 0.8923 1.0829 -0.0383 -0.1406 0.0691  152 VAL   b C   
48916 O  O   . VAL   BA 152 ? 1.9386 0.9623 1.0910 -0.0287 -0.1703 0.0712  152 VAL   b O   
48917 C  CB  . VAL   BA 152 ? 1.8968 0.9109 0.9824 -0.0096 -0.1737 0.1406  152 VAL   b CB  
48918 C  CG1 . VAL   BA 152 ? 1.8799 0.9349 1.0231 -0.0098 -0.1515 0.1265  152 VAL   b CG1 
48919 C  CG2 . VAL   BA 152 ? 1.8834 0.9119 0.9537 0.0144  -0.2087 0.1441  152 VAL   b CG2 
48920 N  N   . ASP   BA 153 ? 1.9663 0.8367 1.1106 -0.0356 -0.1165 0.0418  153 ASP   b N   
48921 C  CA  . ASP   BA 153 ? 1.9403 0.8229 1.1190 -0.0623 -0.0793 0.0540  153 ASP   b CA  
48922 C  C   . ASP   BA 153 ? 1.8966 0.6397 1.1326 -0.0410 -0.0944 0.0246  153 ASP   b C   
48923 O  O   . ASP   BA 153 ? 1.9214 0.6769 1.1691 -0.0487 -0.0227 0.1016  153 ASP   b O   
48924 C  CB  . ASP   BA 153 ? 1.9492 0.8621 1.1249 -0.0585 -0.0837 0.0404  153 ASP   b CB  
48925 C  CG  . ASP   BA 153 ? 1.9644 0.9397 1.1731 -0.0590 -0.0505 0.0377  153 ASP   b CG  
48926 O  OD1 . ASP   BA 153 ? 1.9479 0.9629 1.1681 -0.0756 -0.0240 0.0413  153 ASP   b OD1 
48927 O  OD2 . ASP   BA 153 ? 1.9804 1.0407 1.1774 -0.0128 -0.0528 0.0311  153 ASP   b OD2 
48928 N  N   . PHE   BA 154 ? 1.9036 0.4963 1.0677 -0.0277 -0.1547 0.0158  154 PHE   b N   
48929 C  CA  . PHE   BA 154 ? 1.8572 0.5103 1.0592 0.0079  -0.1641 0.0070  154 PHE   b CA  
48930 C  C   . PHE   BA 154 ? 1.9047 0.6097 1.0674 0.0017  -0.1705 -0.0381 154 PHE   b C   
48931 O  O   . PHE   BA 154 ? 1.9831 0.6236 1.1107 0.0036  -0.1644 -0.0222 154 PHE   b O   
48932 C  CB  . PHE   BA 154 ? 1.8541 0.5033 1.0019 0.0099  -0.2175 0.0066  154 PHE   b CB  
48933 C  CG  . PHE   BA 154 ? 1.8012 0.4926 1.0027 0.0480  -0.2182 -0.0156 154 PHE   b CG  
48934 C  CD1 . PHE   BA 154 ? 1.8005 0.4957 1.0510 0.0476  -0.1987 -0.0649 154 PHE   b CD1 
48935 C  CD2 . PHE   BA 154 ? 1.7773 0.4721 1.0509 0.0586  -0.2193 -0.0249 154 PHE   b CD2 
48936 C  CE1 . PHE   BA 154 ? 1.7682 0.5616 1.1137 0.0430  -0.1718 -0.1032 154 PHE   b CE1 
48937 C  CE2 . PHE   BA 154 ? 1.7580 0.4863 1.1035 0.0456  -0.2029 -0.0491 154 PHE   b CE2 
48938 C  CZ  . PHE   BA 154 ? 1.7585 0.5013 1.1372 0.0305  -0.1898 -0.0991 154 PHE   b CZ  
48939 N  N   . ILE   BA 155 ? 1.8718 0.6146 1.0784 -0.0431 -0.1655 0.0192  155 ILE   b N   
48940 C  CA  . ILE   BA 155 ? 1.8180 0.6811 1.0891 -0.0141 -0.1759 0.0565  155 ILE   b CA  
48941 C  C   . ILE   BA 155 ? 1.8031 0.6758 1.0654 -0.0163 -0.1315 0.0621  155 ILE   b C   
48942 O  O   . ILE   BA 155 ? 1.7809 0.6152 1.1556 -0.0226 -0.1262 0.1086  155 ILE   b O   
48943 C  CB  . ILE   BA 155 ? 1.8279 0.6801 1.0761 -0.0318 -0.1797 0.0861  155 ILE   b CB  
48944 C  CG1 . ILE   BA 155 ? 1.8295 0.6654 1.0624 -0.0288 -0.1919 0.1387  155 ILE   b CG1 
48945 C  CG2 . ILE   BA 155 ? 1.7951 0.6935 1.0920 -0.0456 -0.1782 0.0629  155 ILE   b CG2 
48946 C  CD1 . ILE   BA 155 ? 1.8282 0.6608 1.0540 -0.0472 -0.2045 0.2007  155 ILE   b CD1 
48947 N  N   . LYS   BA 156 ? 1.8462 0.7468 1.0465 -0.0112 -0.1172 0.0490  156 LYS   b N   
48948 C  CA  . LYS   BA 156 ? 1.8612 0.7926 1.0306 0.0040  -0.0757 0.0234  156 LYS   b CA  
48949 C  C   . LYS   BA 156 ? 1.8536 0.8033 1.0054 -0.0532 -0.0777 -0.0674 156 LYS   b C   
48950 O  O   . LYS   BA 156 ? 1.8438 0.7792 1.0184 -0.0417 -0.0776 -0.0980 156 LYS   b O   
48951 C  CB  . LYS   BA 156 ? 1.9212 0.7962 1.0335 0.0224  -0.0525 0.0267  156 LYS   b CB  
48952 C  CG  . LYS   BA 156 ? 1.9373 0.7641 1.0362 0.0564  -0.0257 0.0243  156 LYS   b CG  
48953 C  CD  . LYS   BA 156 ? 2.0048 0.7438 1.0150 0.0508  -0.0268 0.0070  156 LYS   b CD  
48954 C  CE  . LYS   BA 156 ? 2.0543 0.7447 1.0147 0.0372  -0.0162 0.0052  156 LYS   b CE  
48955 N  NZ  . LYS   BA 156 ? 2.1111 0.7391 1.0156 0.0437  -0.0114 -0.0162 156 LYS   b NZ  
48956 N  N   . HIS   BA 157 ? 1.8644 0.8303 0.9685 -0.0361 -0.0930 -0.0567 157 HIS   b N   
48957 C  CA  . HIS   BA 157 ? 1.9143 0.8354 1.0234 -0.0558 -0.0866 -0.0550 157 HIS   b CA  
48958 C  C   . HIS   BA 157 ? 1.8927 0.8584 1.0211 -0.1007 -0.1062 -0.0583 157 HIS   b C   
48959 O  O   . HIS   BA 157 ? 1.9287 0.9071 1.0246 -0.1591 -0.1317 0.0054  157 HIS   b O   
48960 C  CB  . HIS   BA 157 ? 1.9375 0.7873 1.0437 -0.0480 -0.0897 -0.1058 157 HIS   b CB  
48961 C  CG  . HIS   BA 157 ? 1.9806 0.8346 1.1010 -0.0145 -0.0505 -0.1609 157 HIS   b CG  
48962 N  ND1 . HIS   BA 157 ? 2.0198 0.7872 1.0954 -0.0029 -0.0306 -0.1956 157 HIS   b ND1 
48963 C  CD2 . HIS   BA 157 ? 1.9897 0.8770 1.1310 0.0470  -0.0155 -0.1684 157 HIS   b CD2 
48964 C  CE1 . HIS   BA 157 ? 2.0361 0.8905 1.1012 0.0355  -0.0250 -0.2088 157 HIS   b CE1 
48965 N  NE2 . HIS   BA 157 ? 2.0270 0.8960 1.1302 0.0537  -0.0031 -0.1663 157 HIS   b NE2 
48966 N  N   . SER   BA 158 ? 1.8569 0.7750 0.9805 -0.0904 -0.1801 -0.0099 158 SER   b N   
48967 C  CA  . SER   BA 158 ? 1.8008 0.7601 0.9519 -0.1030 -0.2328 0.0145  158 SER   b CA  
48968 C  C   . SER   BA 158 ? 1.7820 0.7105 0.9838 -0.0486 -0.2409 0.0082  158 SER   b C   
48969 O  O   . SER   BA 158 ? 1.7415 0.7108 0.8884 0.0050  -0.3233 -0.0172 158 SER   b O   
48970 C  CB  . SER   BA 158 ? 1.7219 0.7806 0.9052 -0.1191 -0.2800 0.0463  158 SER   b CB  
48971 O  OG  . SER   BA 158 ? 1.7353 0.7643 0.8587 -0.1538 -0.2701 0.1126  158 SER   b OG  
48972 N  N   . LEU   BA 159 ? 1.7204 0.7278 0.9905 -0.0426 -0.2296 0.0469  159 LEU   b N   
48973 C  CA  . LEU   BA 159 ? 1.6763 0.6966 0.9967 0.0183  -0.2112 0.0746  159 LEU   b CA  
48974 C  C   . LEU   BA 159 ? 1.6916 0.6395 1.0304 -0.0196 -0.1472 0.0252  159 LEU   b C   
48975 O  O   . LEU   BA 159 ? 1.6925 0.6761 1.0516 0.0019  -0.1589 0.0194  159 LEU   b O   
48976 C  CB  . LEU   BA 159 ? 1.6891 0.7098 1.0271 0.0047  -0.1970 0.0903  159 LEU   b CB  
48977 C  CG  . LEU   BA 159 ? 1.7113 0.6914 1.0646 0.0153  -0.2063 0.1040  159 LEU   b CG  
48978 C  CD1 . LEU   BA 159 ? 1.7182 0.6744 1.1188 0.0235  -0.1955 0.0962  159 LEU   b CD1 
48979 C  CD2 . LEU   BA 159 ? 1.6981 0.6998 1.0638 0.0477  -0.2042 0.1018  159 LEU   b CD2 
48980 N  N   . SER   BA 160 ? 1.6522 0.5622 1.0325 0.0065  -0.1464 0.0373  160 SER   b N   
48981 C  CA  . SER   BA 160 ? 1.6390 0.6029 1.0830 0.0250  -0.1116 0.0411  160 SER   b CA  
48982 C  C   . SER   BA 160 ? 1.6106 0.5405 1.1049 0.0321  -0.1372 0.0071  160 SER   b C   
48983 O  O   . SER   BA 160 ? 1.5804 0.3422 1.1623 -0.0286 -0.0854 0.0365  160 SER   b O   
48984 C  CB  . SER   BA 160 ? 1.6710 0.6795 1.0927 0.0931  -0.0826 0.0321  160 SER   b CB  
48985 O  OG  . SER   BA 160 ? 1.7353 0.7305 1.1607 0.1244  -0.0386 -0.0093 160 SER   b OG  
48986 N  N   . GLN   BA 161 ? 1.6343 0.4933 1.0809 -0.0050 -0.1711 -0.0058 161 GLN   b N   
48987 C  CA  . GLN   BA 161 ? 1.6333 0.5354 1.0229 -0.0329 -0.1894 -0.0055 161 GLN   b CA  
48988 C  C   . GLN   BA 161 ? 1.6666 0.5587 1.0228 -0.0767 -0.1744 0.0010  161 GLN   b C   
48989 O  O   . GLN   BA 161 ? 1.6956 0.6632 0.9999 -0.0555 -0.1946 0.0376  161 GLN   b O   
48990 C  CB  . GLN   BA 161 ? 1.6410 0.5835 0.9907 0.0170  -0.2070 -0.0346 161 GLN   b CB  
48991 C  CG  . GLN   BA 161 ? 1.6345 0.6352 1.0010 0.0569  -0.2237 -0.0643 161 GLN   b CG  
48992 C  CD  . GLN   BA 161 ? 1.6423 0.6201 0.9569 0.0389  -0.2114 -0.1341 161 GLN   b CD  
48993 O  OE1 . GLN   BA 161 ? 1.6584 0.5933 0.9442 0.0528  -0.2164 -0.2041 161 GLN   b OE1 
48994 N  NE2 . GLN   BA 161 ? 1.6534 0.5455 0.9499 0.0423  -0.2283 -0.1710 161 GLN   b NE2 
48995 N  N   . ALA   BA 162 ? 1.6736 0.4664 1.0248 -0.1002 -0.1822 0.0868  162 ALA   b N   
48996 C  CA  . ALA   BA 162 ? 1.6663 0.4853 1.0128 -0.1124 -0.2249 0.1139  162 ALA   b CA  
48997 C  C   . ALA   BA 162 ? 1.6519 0.5432 1.0034 -0.1452 -0.2340 0.0974  162 ALA   b C   
48998 O  O   . ALA   BA 162 ? 1.6914 0.6308 0.9366 -0.2046 -0.2936 0.0726  162 ALA   b O   
48999 C  CB  . ALA   BA 162 ? 1.6731 0.4981 1.0514 -0.0857 -0.2257 0.1210  162 ALA   b CB  
49000 N  N   . ILE   BA 163 ? 1.6447 0.5339 0.9834 -0.1018 -0.2254 0.1438  163 ILE   b N   
49001 C  CA  . ILE   BA 163 ? 1.6178 0.5516 1.0597 -0.0504 -0.1771 0.1636  163 ILE   b CA  
49002 C  C   . ILE   BA 163 ? 1.6230 0.5514 1.1004 -0.0570 -0.1524 0.0533  163 ILE   b C   
49003 O  O   . ILE   BA 163 ? 1.6004 0.3920 1.1664 -0.0339 -0.0983 0.0996  163 ILE   b O   
49004 C  CB  . ILE   BA 163 ? 1.6319 0.6199 1.0798 -0.0205 -0.1603 0.2380  163 ILE   b CB  
49005 C  CG1 . ILE   BA 163 ? 1.6576 0.6159 1.1535 -0.0325 -0.1507 0.2413  163 ILE   b CG1 
49006 C  CG2 . ILE   BA 163 ? 1.6470 0.6162 1.0846 -0.0003 -0.1461 0.2749  163 ILE   b CG2 
49007 C  CD1 . ILE   BA 163 ? 1.6662 0.6472 1.1806 -0.0379 -0.1336 0.2563  163 ILE   b CD1 
49008 N  N   . LYS   BA 164 ? 1.6455 0.5880 1.0532 0.0041  -0.1705 0.0554  164 LYS   b N   
49009 C  CA  . LYS   BA 164 ? 1.6911 0.6089 1.0849 0.0434  -0.1720 0.0341  164 LYS   b CA  
49010 C  C   . LYS   BA 164 ? 1.7208 0.5339 1.1081 0.0539  -0.1815 0.0244  164 LYS   b C   
49011 O  O   . LYS   BA 164 ? 1.7509 0.4309 1.2058 0.0860  -0.1718 -0.0917 164 LYS   b O   
49012 C  CB  . LYS   BA 164 ? 1.7017 0.5779 1.0997 0.0286  -0.1702 0.0298  164 LYS   b CB  
49013 C  CG  . LYS   BA 164 ? 1.7362 0.5590 1.1506 0.0070  -0.1953 0.0297  164 LYS   b CG  
49014 C  CD  . LYS   BA 164 ? 1.7633 0.6223 1.1552 0.0071  -0.2093 0.0186  164 LYS   b CD  
49015 C  CE  . LYS   BA 164 ? 1.8108 0.6434 1.1458 0.0084  -0.2141 -0.0348 164 LYS   b CE  
49016 N  NZ  . LYS   BA 164 ? 1.8283 0.6538 1.1475 -0.0125 -0.2076 -0.0479 164 LYS   b NZ  
49017 N  N   . TRP   BA 165 ? 1.7003 0.5583 1.1359 0.0819  -0.2221 0.0389  165 TRP   b N   
49018 C  CA  . TRP   BA 165 ? 1.7604 0.5261 1.1042 0.0717  -0.2576 0.0462  165 TRP   b CA  
49019 C  C   . TRP   BA 165 ? 1.7765 0.5598 1.0685 0.0578  -0.2541 0.0887  165 TRP   b C   
49020 O  O   . TRP   BA 165 ? 1.8424 0.5939 1.1394 0.0718  -0.2560 0.1383  165 TRP   b O   
49021 C  CB  . TRP   BA 165 ? 1.7749 0.5135 1.0861 0.0752  -0.2819 0.0196  165 TRP   b CB  
49022 C  CG  . TRP   BA 165 ? 1.8338 0.5743 1.0764 0.1024  -0.2924 0.0117  165 TRP   b CG  
49023 C  CD1 . TRP   BA 165 ? 1.8517 0.5896 1.0228 0.0869  -0.2870 -0.0114 165 TRP   b CD1 
49024 C  CD2 . TRP   BA 165 ? 1.8897 0.6272 1.0419 0.1078  -0.3013 -0.0570 165 TRP   b CD2 
49025 N  NE1 . TRP   BA 165 ? 1.8620 0.6038 1.0437 0.0984  -0.2831 -0.0308 165 TRP   b NE1 
49026 C  CE2 . TRP   BA 165 ? 1.8634 0.5925 1.0534 0.0912  -0.3234 -0.0547 165 TRP   b CE2 
49027 C  CE3 . TRP   BA 165 ? 1.9363 0.5968 1.0544 0.0933  -0.2989 -0.0663 165 TRP   b CE3 
49028 C  CZ2 . TRP   BA 165 ? 1.8430 0.6182 1.0683 0.0575  -0.3527 -0.0925 165 TRP   b CZ2 
49029 C  CZ3 . TRP   BA 165 ? 1.9279 0.5917 1.0676 0.0588  -0.3209 -0.0783 165 TRP   b CZ3 
49030 C  CH2 . TRP   BA 165 ? 1.8808 0.5939 1.0800 0.0649  -0.3381 -0.1054 165 TRP   b CH2 
49031 N  N   . ASP   BA 166 ? 1.7632 0.5557 1.0408 0.0516  -0.2664 0.0973  166 ASP   b N   
49032 C  CA  . ASP   BA 166 ? 1.7341 0.5287 1.0489 0.0251  -0.2840 0.0984  166 ASP   b CA  
49033 C  C   . ASP   BA 166 ? 1.7300 0.4370 1.0329 0.0391  -0.2988 0.0760  166 ASP   b C   
49034 O  O   . ASP   BA 166 ? 1.6948 0.2587 0.9810 0.0390  -0.3940 0.0696  166 ASP   b O   
49035 C  CB  . ASP   BA 166 ? 1.7530 0.5497 1.0295 0.0407  -0.2688 0.0909  166 ASP   b CB  
49036 C  CG  . ASP   BA 166 ? 1.7887 0.6423 1.0348 -0.0013 -0.2616 0.0672  166 ASP   b CG  
49037 O  OD1 . ASP   BA 166 ? 1.7951 0.5589 1.1303 -0.0074 -0.2133 0.1085  166 ASP   b OD1 
49038 O  OD2 . ASP   BA 166 ? 1.8042 0.6414 1.0264 0.0065  -0.2609 0.0686  166 ASP   b OD2 
49039 N  N   . GLY   BA 167 ? 1.6902 0.4684 1.0385 0.0444  -0.3029 0.0763  167 GLY   b N   
49040 C  CA  . GLY   BA 167 ? 1.6584 0.4943 1.1133 0.0413  -0.2711 0.0660  167 GLY   b CA  
49041 C  C   . GLY   BA 167 ? 1.6654 0.4479 1.1322 0.0528  -0.2687 0.1123  167 GLY   b C   
49042 O  O   . GLY   BA 167 ? 1.6440 0.2780 1.1028 0.1109  -0.2558 0.1347  167 GLY   b O   
49043 N  N   . SER   BA 168 ? 1.6574 0.4804 1.1355 0.0471  -0.2546 0.1234  168 SER   b N   
49044 C  CA  . SER   BA 168 ? 1.6825 0.5426 1.0855 -0.0155 -0.2420 0.0827  168 SER   b CA  
49045 C  C   . SER   BA 168 ? 1.6751 0.5555 1.1033 -0.0201 -0.2685 0.1065  168 SER   b C   
49046 O  O   . SER   BA 168 ? 1.7241 0.4450 1.1973 -0.0133 -0.2549 0.2284  168 SER   b O   
49047 C  CB  . SER   BA 168 ? 1.6932 0.6207 1.0017 -0.0459 -0.2321 0.0984  168 SER   b CB  
49048 O  OG  . SER   BA 168 ? 1.7238 0.6116 0.9399 -0.0128 -0.2472 0.1063  168 SER   b OG  
49049 N  N   . SER   BA 169 ? 1.5988 0.5132 1.0932 -0.0181 -0.2549 0.1077  169 SER   b N   
49050 C  CA  . SER   BA 169 ? 1.5512 0.4935 1.0556 -0.0093 -0.2634 0.0819  169 SER   b CA  
49051 C  C   . SER   BA 169 ? 1.5478 0.5993 1.0747 0.0002  -0.2500 0.0856  169 SER   b C   
49052 O  O   . SER   BA 169 ? 1.5414 0.6401 1.0912 0.0626  -0.2489 0.1116  169 SER   b O   
49053 C  CB  . SER   BA 169 ? 1.5768 0.4480 1.0283 -0.0399 -0.2754 0.0539  169 SER   b CB  
49054 O  OG  . SER   BA 169 ? 1.6102 0.4084 0.9778 -0.0409 -0.2771 0.0316  169 SER   b OG  
49055 N  N   . GLY   BA 170 ? 1.5137 0.6027 1.0793 0.0406  -0.2250 0.0988  170 GLY   b N   
49056 C  CA  . GLY   BA 170 ? 1.5306 0.6322 1.0915 0.0492  -0.2034 0.1138  170 GLY   b CA  
49057 C  C   . GLY   BA 170 ? 1.5411 0.6537 1.0889 0.0658  -0.1756 0.1690  170 GLY   b C   
49058 O  O   . GLY   BA 170 ? 1.4399 0.6585 1.0012 0.0634  -0.2047 0.2779  170 GLY   b O   
49059 N  N   . GLY   BA 171 ? 1.5776 0.7042 1.1392 0.0805  -0.1332 0.1432  171 GLY   b N   
49060 C  CA  . GLY   BA 171 ? 1.6685 0.6509 1.1759 0.0458  -0.1520 0.0987  171 GLY   b CA  
49061 C  C   . GLY   BA 171 ? 1.7295 0.6696 1.1302 0.0384  -0.1535 0.0467  171 GLY   b C   
49062 O  O   . GLY   BA 171 ? 1.7951 0.5933 1.2040 0.0055  -0.1671 0.0476  171 GLY   b O   
49063 N  N   . VAL   BA 172 ? 1.7090 0.6581 1.1189 0.0466  -0.1398 -0.0088 172 VAL   b N   
49064 C  CA  . VAL   BA 172 ? 1.7179 0.6171 1.0870 0.0285  -0.1277 -0.0377 172 VAL   b CA  
49065 C  C   . VAL   BA 172 ? 1.7158 0.6011 1.0915 0.0001  -0.1482 -0.0424 172 VAL   b C   
49066 O  O   . VAL   BA 172 ? 1.7618 0.5454 1.0776 -0.0630 -0.1436 -0.0122 172 VAL   b O   
49067 C  CB  . VAL   BA 172 ? 1.6829 0.6525 1.1202 0.0207  -0.0961 -0.0423 172 VAL   b CB  
49068 C  CG1 . VAL   BA 172 ? 1.7008 0.6153 1.1336 0.0459  -0.0734 -0.0569 172 VAL   b CG1 
49069 C  CG2 . VAL   BA 172 ? 1.6961 0.7082 1.1121 0.0138  -0.0923 -0.0633 172 VAL   b CG2 
49070 N  N   . ILE   BA 173 ? 1.7206 0.6330 1.1063 0.0050  -0.1560 -0.0181 173 ILE   b N   
49071 C  CA  . ILE   BA 173 ? 1.7129 0.6779 1.1161 0.0038  -0.1665 0.0284  173 ILE   b CA  
49072 C  C   . ILE   BA 173 ? 1.6755 0.6773 1.1007 -0.0115 -0.1729 0.0116  173 ILE   b C   
49073 O  O   . ILE   BA 173 ? 1.6395 0.6945 1.1210 -0.0370 -0.1250 -0.0350 173 ILE   b O   
49074 C  CB  . ILE   BA 173 ? 1.7258 0.7181 1.1107 -0.0184 -0.1824 0.0594  173 ILE   b CB  
49075 C  CG1 . ILE   BA 173 ? 1.7398 0.7362 1.1359 -0.0117 -0.1963 0.1039  173 ILE   b CG1 
49076 C  CG2 . ILE   BA 173 ? 1.7295 0.7227 1.1328 -0.0077 -0.1565 0.0680  173 ILE   b CG2 
49077 C  CD1 . ILE   BA 173 ? 1.7685 0.7793 1.1188 -0.0140 -0.2082 0.1047  173 ILE   b CD1 
49078 N  N   . ARG   BA 174 ? 1.6671 0.6196 1.1146 -0.0178 -0.2023 0.0210  174 ARG   b N   
49079 C  CA  . ARG   BA 174 ? 1.6534 0.6306 1.1501 -0.0160 -0.2414 0.0716  174 ARG   b CA  
49080 C  C   . ARG   BA 174 ? 1.6605 0.5926 1.1054 -0.0272 -0.2605 0.0683  174 ARG   b C   
49081 O  O   . ARG   BA 174 ? 1.6374 0.4326 1.0279 0.0119  -0.3244 0.0858  174 ARG   b O   
49082 C  CB  . ARG   BA 174 ? 1.6562 0.5831 1.1912 0.0027  -0.2584 0.0529  174 ARG   b CB  
49083 C  CG  . ARG   BA 174 ? 1.6578 0.5295 1.2455 0.0007  -0.2753 0.0396  174 ARG   b CG  
49084 C  CD  . ARG   BA 174 ? 1.6809 0.4677 1.2744 0.0416  -0.2804 0.0357  174 ARG   b CD  
49085 N  NE  . ARG   BA 174 ? 1.7503 0.3750 1.2588 0.0686  -0.3040 0.0677  174 ARG   b NE  
49086 C  CZ  . ARG   BA 174 ? 1.7653 0.3726 1.3157 0.0401  -0.3028 0.1058  174 ARG   b CZ  
49087 N  NH1 . ARG   BA 174 ? 1.7957 0.4092 1.3440 -0.0144 -0.2581 0.1097  174 ARG   b NH1 
49088 N  NH2 . ARG   BA 174 ? 1.7769 0.3481 1.3183 0.0446  -0.3053 0.1273  174 ARG   b NH2 
49089 N  N   . MET   BA 175 ? 1.6762 0.7094 1.0480 -0.0082 -0.3037 0.1027  175 MET   b N   
49090 C  CA  . MET   BA 175 ? 1.6723 0.8247 1.0277 -0.0063 -0.3164 0.1001  175 MET   b CA  
49091 C  C   . MET   BA 175 ? 1.6401 0.8284 1.0349 0.0029  -0.3147 0.1265  175 MET   b C   
49092 O  O   . MET   BA 175 ? 1.6486 0.8711 1.0132 -0.0598 -0.3763 0.1393  175 MET   b O   
49093 C  CB  . MET   BA 175 ? 1.7306 0.8615 1.0042 0.0005  -0.2947 0.0982  175 MET   b CB  
49094 C  CG  . MET   BA 175 ? 1.7441 0.8605 0.9760 0.0130  -0.2864 0.0965  175 MET   b CG  
49095 S  SD  . MET   BA 175 ? 1.7287 1.0044 0.8712 0.0716  -0.3514 0.1819  175 MET   b SD  
49096 C  CE  . MET   BA 175 ? 1.7575 0.9123 0.8853 0.0736  -0.3394 0.1767  175 MET   b CE  
49097 N  N   . VAL   BA 176 ? 1.6657 0.8440 1.0286 0.0277  -0.2983 0.1257  176 VAL   b N   
49098 C  CA  . VAL   BA 176 ? 1.6738 0.8499 1.0715 0.0379  -0.2624 0.1477  176 VAL   b CA  
49099 C  C   . VAL   BA 176 ? 1.6592 0.8422 1.0802 0.0646  -0.2399 0.1425  176 VAL   b C   
49100 O  O   . VAL   BA 176 ? 1.7072 0.8960 1.0665 0.0921  -0.1242 0.1522  176 VAL   b O   
49101 C  CB  . VAL   BA 176 ? 1.6544 0.8324 1.0875 0.0711  -0.2460 0.1490  176 VAL   b CB  
49102 C  CG1 . VAL   BA 176 ? 1.6346 0.8466 1.1028 0.1045  -0.2553 0.1686  176 VAL   b CG1 
49103 C  CG2 . VAL   BA 176 ? 1.6451 0.9060 1.1270 0.0671  -0.2467 0.1567  176 VAL   b CG2 
49104 N  N   . VAL   BA 177 ? 1.7137 0.7878 1.1223 0.0577  -0.2190 0.1473  177 VAL   b N   
49105 C  CA  . VAL   BA 177 ? 1.7491 0.7624 1.1142 0.0557  -0.2316 0.1633  177 VAL   b CA  
49106 C  C   . VAL   BA 177 ? 1.7149 0.7546 1.1131 0.0393  -0.2498 0.1735  177 VAL   b C   
49107 O  O   . VAL   BA 177 ? 1.7665 0.8231 1.1027 -0.0239 -0.2791 0.2185  177 VAL   b O   
49108 C  CB  . VAL   BA 177 ? 1.7642 0.7287 1.0991 0.0586  -0.2441 0.1694  177 VAL   b CB  
49109 C  CG1 . VAL   BA 177 ? 1.7873 0.6683 1.0864 0.0633  -0.2501 0.1584  177 VAL   b CG1 
49110 C  CG2 . VAL   BA 177 ? 1.7365 0.7810 1.1039 0.0799  -0.2284 0.1406  177 VAL   b CG2 
49111 N  N   . LEU   BA 178 ? 1.7196 0.7772 1.1391 0.0499  -0.2358 0.1275  178 LEU   b N   
49112 C  CA  . LEU   BA 178 ? 1.7630 0.7616 1.1905 0.0344  -0.2091 0.0977  178 LEU   b CA  
49113 C  C   . LEU   BA 178 ? 1.8222 0.7285 1.2103 0.0471  -0.2198 0.1190  178 LEU   b C   
49114 O  O   . LEU   BA 178 ? 1.8133 0.6760 1.2451 0.0600  -0.2018 0.1548  178 LEU   b O   
49115 C  CB  . LEU   BA 178 ? 1.7180 0.7235 1.1680 0.0739  -0.2357 0.0634  178 LEU   b CB  
49116 C  CG  . LEU   BA 178 ? 1.6494 0.6805 1.1656 0.1201  -0.2378 0.0745  178 LEU   b CG  
49117 C  CD1 . LEU   BA 178 ? 1.6542 0.6615 1.1531 0.1367  -0.2581 0.0898  178 LEU   b CD1 
49118 C  CD2 . LEU   BA 178 ? 1.6390 0.6378 1.1346 0.1329  -0.2512 0.0616  178 LEU   b CD2 
49119 N  N   . THR   BA 179 ? 1.8956 0.7725 1.2647 -0.0039 -0.1849 0.1294  179 THR   b N   
49120 C  CA  . THR   BA 179 ? 1.9319 0.8374 1.2438 -0.0172 -0.2047 0.1078  179 THR   b CA  
49121 C  C   . THR   BA 179 ? 1.9699 0.8407 1.2754 -0.0267 -0.1796 0.1330  179 THR   b C   
49122 O  O   . THR   BA 179 ? 1.9886 0.8364 1.3674 -0.0594 -0.1747 0.0885  179 THR   b O   
49123 C  CB  . THR   BA 179 ? 1.9310 0.8551 1.2813 -0.0096 -0.1726 0.0980  179 THR   b CB  
49124 O  OG1 . THR   BA 179 ? 1.9550 0.8236 1.3024 -0.0641 -0.1417 0.0781  179 THR   b OG1 
49125 C  CG2 . THR   BA 179 ? 1.9443 0.8394 1.2785 0.0462  -0.1677 0.1171  179 THR   b CG2 
49126 N  N   . ALA   BA 180 ? 1.9610 0.9253 1.2168 -0.0435 -0.1764 0.1391  180 ALA   b N   
49127 C  CA  . ALA   BA 180 ? 1.9663 0.9444 1.1868 -0.0328 -0.1921 0.1797  180 ALA   b CA  
49128 C  C   . ALA   BA 180 ? 1.9908 0.9931 1.2248 -0.0678 -0.1717 0.1975  180 ALA   b C   
49129 O  O   . ALA   BA 180 ? 2.0288 0.9886 1.2350 -0.0717 -0.1281 0.1837  180 ALA   b O   
49130 C  CB  . ALA   BA 180 ? 1.9600 1.0040 1.2125 -0.0303 -0.2192 0.1554  180 ALA   b CB  
49131 N  N   . ALA   BA 181 ? 1.9813 1.0406 1.2437 -0.0619 -0.1584 0.1882  181 ALA   b N   
49132 C  CA  . ALA   BA 181 ? 1.9665 1.0559 1.3181 -0.0942 -0.1816 0.2298  181 ALA   b CA  
49133 C  C   . ALA   BA 181 ? 1.9070 0.9714 1.3063 -0.0839 -0.1644 0.2711  181 ALA   b C   
49134 O  O   . ALA   BA 181 ? 1.8192 1.0702 1.3845 -0.0766 -0.1739 0.2207  181 ALA   b O   
49135 C  CB  . ALA   BA 181 ? 1.9557 1.0596 1.3306 -0.0797 -0.1689 0.2389  181 ALA   b CB  
49136 N  N   . GLY   BA 182 ? 1.8875 0.8488 1.2960 -0.0606 -0.2099 0.2557  182 GLY   b N   
49137 C  CA  . GLY   BA 182 ? 1.8640 0.7081 1.3327 -0.0592 -0.2332 0.2685  182 GLY   b CA  
49138 C  C   . GLY   BA 182 ? 1.8451 0.6668 1.3247 -0.0648 -0.2663 0.2372  182 GLY   b C   
49139 O  O   . GLY   BA 182 ? 1.8104 0.6175 1.3296 -0.0208 -0.2919 0.3271  182 GLY   b O   
49140 N  N   . VAL   BA 183 ? 1.8364 0.5517 1.2770 -0.1168 -0.2582 0.2378  183 VAL   b N   
49141 C  CA  . VAL   BA 183 ? 1.8545 0.5124 1.2730 -0.1296 -0.2172 0.2249  183 VAL   b CA  
49142 C  C   . VAL   BA 183 ? 1.8326 0.5959 1.2433 -0.1114 -0.2042 0.2701  183 VAL   b C   
49143 O  O   . VAL   BA 183 ? 1.8514 0.4443 1.2971 -0.0983 -0.2116 0.2909  183 VAL   b O   
49144 C  CB  . VAL   BA 183 ? 1.8661 0.4271 1.2732 -0.1529 -0.2095 0.2401  183 VAL   b CB  
49145 C  CG1 . VAL   BA 183 ? 1.8776 0.4368 1.2540 -0.1236 -0.2009 0.2316  183 VAL   b CG1 
49146 C  CG2 . VAL   BA 183 ? 1.8498 0.4114 1.2896 -0.1674 -0.2031 0.2550  183 VAL   b CG2 
49147 N  N   . GLU   BA 184 ? 1.8732 0.6128 1.1947 -0.0585 -0.1956 0.2219  184 GLU   b N   
49148 C  CA  . GLU   BA 184 ? 1.9048 0.6772 1.2418 -0.0427 -0.1688 0.1736  184 GLU   b CA  
49149 C  C   . GLU   BA 184 ? 1.8626 0.6403 1.2439 -0.0560 -0.1512 0.1490  184 GLU   b C   
49150 O  O   . GLU   BA 184 ? 1.8393 0.6271 1.2860 -0.0739 -0.1256 0.0374  184 GLU   b O   
49151 C  CB  . GLU   BA 184 ? 1.9685 0.6665 1.2191 -0.0141 -0.1762 0.1947  184 GLU   b CB  
49152 C  CG  . GLU   BA 184 ? 1.9919 0.7148 1.2103 -0.0120 -0.1603 0.1830  184 GLU   b CG  
49153 C  CD  . GLU   BA 184 ? 2.0595 0.7686 1.2119 -0.0121 -0.1599 0.1642  184 GLU   b CD  
49154 O  OE1 . GLU   BA 184 ? 2.0671 0.8084 1.2379 -0.0210 -0.1236 0.1530  184 GLU   b OE1 
49155 O  OE2 . GLU   BA 184 ? 2.0829 0.8413 1.2497 0.0161  -0.1963 0.1085  184 GLU   b OE2 
49156 N  N   . ARG   BA 185 ? 1.8327 0.7430 1.2996 -0.0784 -0.1347 0.1338  185 ARG   b N   
49157 C  CA  . ARG   BA 185 ? 1.8280 0.7498 1.2691 -0.1302 -0.1116 0.1615  185 ARG   b CA  
49158 C  C   . ARG   BA 185 ? 1.7835 0.7602 1.2860 -0.1417 -0.1013 0.1531  185 ARG   b C   
49159 O  O   . ARG   BA 185 ? 1.8115 0.6489 1.3615 -0.1665 -0.0592 0.1478  185 ARG   b O   
49160 C  CB  . ARG   BA 185 ? 1.8524 0.7928 1.2284 -0.1506 -0.0995 0.1659  185 ARG   b CB  
49161 C  CG  . ARG   BA 185 ? 1.8821 0.8215 1.2495 -0.1756 -0.0729 0.1339  185 ARG   b CG  
49162 C  CD  . ARG   BA 185 ? 1.8879 0.9537 1.2528 -0.1771 -0.0839 0.0772  185 ARG   b CD  
49163 N  NE  . ARG   BA 185 ? 1.9429 1.0887 1.2796 -0.1560 -0.0741 0.0133  185 ARG   b NE  
49164 C  CZ  . ARG   BA 185 ? 1.9329 1.1309 1.2831 -0.1402 -0.0867 0.0433  185 ARG   b CZ  
49165 N  NH1 . ARG   BA 185 ? 1.9415 1.1252 1.2025 -0.1211 -0.1080 0.0451  185 ARG   b NH1 
49166 N  NH2 . ARG   BA 185 ? 1.8900 1.2410 1.2896 -0.0646 -0.0726 0.0745  185 ARG   b NH2 
49167 N  N   . LEU   BA 186 ? 1.7435 0.7567 1.2601 -0.1385 -0.1169 0.1114  186 LEU   b N   
49168 C  CA  . LEU   BA 186 ? 1.7300 0.7511 1.2892 -0.1494 -0.1159 0.0968  186 LEU   b CA  
49169 C  C   . LEU   BA 186 ? 1.7239 0.7916 1.2380 -0.1428 -0.1187 0.0838  186 LEU   b C   
49170 O  O   . LEU   BA 186 ? 1.6634 0.7552 1.2500 -0.0632 -0.1022 0.0411  186 LEU   b O   
49171 C  CB  . LEU   BA 186 ? 1.7494 0.7109 1.2978 -0.1612 -0.1156 0.0907  186 LEU   b CB  
49172 C  CG  . LEU   BA 186 ? 1.7657 0.6988 1.3155 -0.1684 -0.0990 0.1117  186 LEU   b CG  
49173 C  CD1 . LEU   BA 186 ? 1.7552 0.7007 1.3352 -0.1577 -0.1005 0.1135  186 LEU   b CD1 
49174 C  CD2 . LEU   BA 186 ? 1.7679 0.7857 1.3580 -0.1757 -0.0781 0.1278  186 LEU   b CD2 
49175 N  N   . ILE   BA 187 ? 1.7417 0.8742 1.3115 -0.1103 -0.1105 0.0854  187 ILE   b N   
49176 C  CA  . ILE   BA 187 ? 1.8145 0.8781 1.3397 -0.1052 -0.0914 0.1183  187 ILE   b CA  
49177 C  C   . ILE   BA 187 ? 1.8690 0.9116 1.3170 -0.0998 -0.0644 0.1114  187 ILE   b C   
49178 O  O   . ILE   BA 187 ? 1.9018 0.8924 1.3305 -0.1071 -0.0421 0.1238  187 ILE   b O   
49179 C  CB  . ILE   BA 187 ? 1.8150 0.9067 1.3898 -0.0994 -0.1125 0.1457  187 ILE   b CB  
49180 C  CG1 . ILE   BA 187 ? 1.8204 0.8612 1.4096 -0.1156 -0.1049 0.1431  187 ILE   b CG1 
49181 C  CG2 . ILE   BA 187 ? 1.8512 0.9759 1.3950 -0.0840 -0.0873 0.1510  187 ILE   b CG2 
49182 C  CD1 . ILE   BA 187 ? 1.8095 0.8365 1.4100 -0.1082 -0.1123 0.1691  187 ILE   b CD1 
49183 N  N   . PHE   BA 188 ? 1.9033 0.9289 1.3349 -0.1271 -0.0484 0.1098  188 PHE   b N   
49184 C  CA  . PHE   BA 188 ? 1.8839 0.9355 1.2941 -0.0802 -0.0548 0.1180  188 PHE   b CA  
49185 C  C   . PHE   BA 188 ? 1.9023 0.9021 1.3311 -0.0365 -0.0464 0.1003  188 PHE   b C   
49186 O  O   . PHE   BA 188 ? 1.8959 0.8147 1.3233 0.0549  -0.0867 0.2107  188 PHE   b O   
49187 C  CB  . PHE   BA 188 ? 1.9141 0.9386 1.1945 -0.0821 -0.0663 0.0655  188 PHE   b CB  
49188 C  CG  . PHE   BA 188 ? 1.9017 1.0250 1.1074 -0.0772 -0.0795 0.0552  188 PHE   b CG  
49189 C  CD1 . PHE   BA 188 ? 1.9099 1.1103 1.1324 -0.0908 -0.0342 0.0203  188 PHE   b CD1 
49190 C  CD2 . PHE   BA 188 ? 1.9290 1.0405 1.0740 -0.0641 -0.0793 0.0280  188 PHE   b CD2 
49191 C  CE1 . PHE   BA 188 ? 1.9269 1.1299 1.1697 -0.0533 -0.0443 0.0120  188 PHE   b CE1 
49192 C  CE2 . PHE   BA 188 ? 1.9484 0.9929 1.0923 -0.0505 -0.0780 0.0031  188 PHE   b CE2 
49193 C  CZ  . PHE   BA 188 ? 1.9693 1.0546 1.1097 -0.0502 -0.0548 -0.0024 188 PHE   b CZ  
49194 N  N   . TYR   BA 189 ? 1.9170 0.9976 1.3223 -0.0326 -0.0332 0.0560  189 TYR   b N   
49195 C  CA  . TYR   BA 189 ? 1.9260 1.0351 1.2888 -0.0569 -0.0869 0.0370  189 TYR   b CA  
49196 C  C   . TYR   BA 189 ? 2.0009 1.0418 1.3527 -0.0768 -0.1393 0.0225  189 TYR   b C   
49197 O  O   . TYR   BA 189 ? 2.0524 0.9240 1.3871 -0.1350 -0.1689 0.0530  189 TYR   b O   
49198 C  CB  . TYR   BA 189 ? 1.9315 1.0983 1.2553 -0.0490 -0.0686 0.0036  189 TYR   b CB  
49199 C  CG  . TYR   BA 189 ? 1.9279 1.0789 1.2223 -0.0242 -0.0460 -0.0086 189 TYR   b CG  
49200 C  CD1 . TYR   BA 189 ? 1.9445 1.0893 1.2687 -0.0336 -0.0523 -0.0482 189 TYR   b CD1 
49201 C  CD2 . TYR   BA 189 ? 1.9004 1.0573 1.1780 -0.0053 -0.0540 -0.0356 189 TYR   b CD2 
49202 C  CE1 . TYR   BA 189 ? 1.9293 1.0839 1.2872 -0.0363 -0.0437 0.0259  189 TYR   b CE1 
49203 C  CE2 . TYR   BA 189 ? 1.8873 1.0477 1.1959 0.0017  -0.0378 0.0187  189 TYR   b CE2 
49204 C  CZ  . TYR   BA 189 ? 1.8892 1.0639 1.2367 -0.0160 -0.0531 -0.0045 189 TYR   b CZ  
49205 O  OH  . TYR   BA 189 ? 1.8352 1.0562 1.2706 0.0026  -0.0521 -0.0181 189 TYR   b OH  
49206 N  N   . PRO   BA 190 ? 2.0071 0.9312 1.4416 -0.0847 -0.2001 -0.0008 190 PRO   b N   
49207 C  CA  . PRO   BA 190 ? 1.9835 0.9201 1.4754 -0.0547 -0.2048 -0.0177 190 PRO   b CA  
49208 C  C   . PRO   BA 190 ? 1.9744 1.0588 1.5044 -0.0029 -0.1196 -0.0419 190 PRO   b C   
49209 O  O   . PRO   BA 190 ? 1.9196 1.2674 1.5319 0.0050  -0.1596 -0.0439 190 PRO   b O   
49210 C  CB  . PRO   BA 190 ? 2.0054 0.9399 1.4666 -0.0600 -0.2243 -0.0256 190 PRO   b CB  
49211 C  CG  . PRO   BA 190 ? 1.9781 0.8622 1.4845 -0.0808 -0.2316 0.0150  190 PRO   b CG  
49212 C  CD  . PRO   BA 190 ? 1.9807 0.8901 1.4715 -0.0834 -0.2265 0.0337  190 PRO   b CD  
49213 N  N   . ASP   BA 191 ? 1.9477 1.0480 1.5568 -0.0238 -0.1169 -0.0840 191 ASP   b N   
49214 C  CA  . ASP   BA 191 ? 1.8956 1.0913 1.5754 -0.0338 -0.1057 -0.1120 191 ASP   b CA  
49215 C  C   . ASP   BA 191 ? 1.9705 1.1365 1.4812 0.0327  -0.0612 -0.0643 191 ASP   b C   
49216 O  O   . ASP   BA 191 ? 2.0090 1.2482 1.3835 0.0911  -0.0663 -0.0731 191 ASP   b O   
49217 C  CB  . ASP   BA 191 ? 1.8797 1.0079 1.6746 -0.0780 -0.1384 -0.1652 191 ASP   b CB  
49218 C  CG  . ASP   BA 191 ? 1.7857 0.9399 1.7998 -0.0934 -0.1519 -0.2015 191 ASP   b CG  
49219 O  OD1 . ASP   BA 191 ? 1.7564 0.9378 1.7949 -0.0293 -0.1460 -0.2455 191 ASP   b OD1 
49220 O  OD2 . ASP   BA 191 ? 1.7210 1.0551 1.9784 -0.1708 -0.2063 -0.1686 191 ASP   b OD2 
49221 N  N   . GLU   BA 192 ? 1.9703 1.1451 1.3909 0.0406  -0.0272 -0.0357 192 GLU   b N   
49222 C  CA  . GLU   BA 192 ? 1.9886 1.2596 1.3638 0.0631  -0.0298 -0.0639 192 GLU   b CA  
49223 C  C   . GLU   BA 192 ? 1.9760 1.2277 1.3049 0.0782  -0.0477 -0.0810 192 GLU   b C   
49224 O  O   . GLU   BA 192 ? 2.0583 1.3908 1.3247 0.0533  -0.1032 -0.1436 192 GLU   b O   
49225 C  CB  . GLU   BA 192 ? 1.9680 1.2868 1.3828 0.1136  -0.0181 -0.0372 192 GLU   b CB  
49226 C  CG  . GLU   BA 192 ? 1.9752 1.4656 1.3977 0.1209  -0.0427 -0.0547 192 GLU   b CG  
49227 C  CD  . GLU   BA 192 ? 1.9934 1.5013 1.4618 0.1204  -0.0710 -0.0173 192 GLU   b CD  
49228 O  OE1 . GLU   BA 192 ? 2.0284 1.7643 1.3662 0.0758  -0.1399 -0.1086 192 GLU   b OE1 
49229 O  OE2 . GLU   BA 192 ? 1.9632 1.5366 1.6622 0.0159  -0.0309 0.0149  192 GLU   b OE2 
49230 N  N   . TYR   BA 193 ? 1.9090 1.1314 1.3002 0.1068  -0.0588 -0.0373 193 TYR   b N   
49231 C  CA  . TYR   BA 193 ? 1.8864 1.0546 1.2872 0.1075  -0.1054 -0.0076 193 TYR   b CA  
49232 C  C   . TYR   BA 193 ? 1.9025 1.0599 1.3190 0.0325  -0.1170 -0.0171 193 TYR   b C   
49233 O  O   . TYR   BA 193 ? 1.8832 1.1151 1.2042 0.0606  -0.1774 0.0084  193 TYR   b O   
49234 C  CB  . TYR   BA 193 ? 1.8306 1.0315 1.2540 0.1106  -0.1050 0.0262  193 TYR   b CB  
49235 C  CG  . TYR   BA 193 ? 1.7725 1.0129 1.2105 0.0875  -0.0752 -0.0582 193 TYR   b CG  
49236 C  CD1 . TYR   BA 193 ? 1.7908 1.0660 1.2356 0.0493  -0.0423 -0.0547 193 TYR   b CD1 
49237 C  CD2 . TYR   BA 193 ? 1.7514 0.9725 1.2070 0.0891  -0.0352 -0.0673 193 TYR   b CD2 
49238 C  CE1 . TYR   BA 193 ? 1.7790 1.1193 1.2590 0.0207  -0.0978 -0.1103 193 TYR   b CE1 
49239 C  CE2 . TYR   BA 193 ? 1.7458 0.9932 1.2262 0.0562  -0.0782 -0.1166 193 TYR   b CE2 
49240 C  CZ  . TYR   BA 193 ? 1.7812 1.0525 1.2471 0.0346  -0.0948 -0.0843 193 TYR   b CZ  
49241 O  OH  . TYR   BA 193 ? 1.8012 1.2138 1.3250 0.0568  -0.1931 -0.0693 193 TYR   b OH  
49242 N  N   . GLU   BA 194 ? 1.9417 0.9921 1.4041 0.0298  -0.1316 -0.0023 194 GLU   b N   
49243 C  CA  . GLU   BA 194 ? 1.9924 0.9708 1.4529 0.0655  -0.1331 -0.0069 194 GLU   b CA  
49244 C  C   . GLU   BA 194 ? 2.0567 0.9916 1.4488 0.1222  -0.1069 -0.0452 194 GLU   b C   
49245 O  O   . GLU   BA 194 ? 1.9881 1.0887 1.4775 0.0942  -0.0773 -0.0467 194 GLU   b O   
49246 C  CB  . GLU   BA 194 ? 1.9944 0.9036 1.4835 0.0536  -0.1324 0.0355  194 GLU   b CB  
49247 C  CG  . GLU   BA 194 ? 2.0279 0.9303 1.4671 0.0378  -0.1190 0.0762  194 GLU   b CG  
49248 C  CD  . GLU   BA 194 ? 2.0472 1.0314 1.4401 0.0556  -0.1060 0.1163  194 GLU   b CD  
49249 O  OE1 . GLU   BA 194 ? 2.1313 0.9430 1.3142 0.0880  -0.0339 0.2158  194 GLU   b OE1 
49250 O  OE2 . GLU   BA 194 ? 2.0598 1.2476 1.4911 0.0796  -0.0202 0.0375  194 GLU   b OE2 
49251 N  N   . GLN   BA 195 ? 2.0754 1.0058 1.4544 0.0893  -0.1027 -0.0369 195 GLN   b N   
49252 C  CA  . GLN   BA 195 ? 2.0762 1.1423 1.4347 0.0665  -0.1285 -0.0714 195 GLN   b CA  
49253 C  C   . GLN   BA 195 ? 2.0250 1.1871 1.4299 0.0787  -0.1254 -0.1573 195 GLN   b C   
49254 O  O   . GLN   BA 195 ? 2.1103 1.3658 1.3663 0.0990  -0.0772 -0.1098 195 GLN   b O   
49255 C  CB  . GLN   BA 195 ? 2.0813 1.1555 1.4347 0.0463  -0.1125 -0.0190 195 GLN   b CB  
49256 C  CG  . GLN   BA 195 ? 2.1241 1.1870 1.4720 0.0392  -0.0842 0.0109  195 GLN   b CG  
49257 C  CD  . GLN   BA 195 ? 2.1256 1.2612 1.5798 0.1425  -0.0875 0.0215  195 GLN   b CD  
49258 O  OE1 . GLN   BA 195 ? 2.2357 1.1736 1.5566 0.0959  -0.0617 0.1683  195 GLN   b OE1 
49259 N  NE2 . GLN   BA 195 ? 2.2140 1.3977 1.5900 0.0903  -0.0654 0.0588  195 GLN   b NE2 
49260 N  N   . LEU   BA 196 ? 1.9797 1.1911 1.4984 0.0365  -0.1332 -0.2260 196 LEU   b N   
49261 C  CA  . LEU   BA 196 ? 2.0234 1.3455 1.4723 0.0704  -0.1565 -0.2384 196 LEU   b CA  
49262 C  C   . LEU   BA 196 ? 2.0399 1.4427 1.5112 0.0262  -0.1068 -0.3022 196 LEU   b C   
49263 O  O   . LEU   BA 196 ? 2.1136 1.6271 1.4858 0.1638  -0.0947 -0.2451 196 LEU   b O   
49264 C  CB  . LEU   BA 196 ? 1.9298 1.1941 1.5187 -0.0136 -0.2071 -0.2029 196 LEU   b CB  
49265 C  CG  . LEU   BA 196 ? 1.8993 1.1715 1.4760 0.0067  -0.2143 -0.2081 196 LEU   b CG  
49266 C  CD1 . LEU   BA 196 ? 1.9046 1.0732 1.5314 -0.0113 -0.2446 -0.2140 196 LEU   b CD1 
49267 C  CD2 . LEU   BA 196 ? 1.8820 1.2098 1.4499 -0.0263 -0.2107 -0.2183 196 LEU   b CD2 
49268 O  OXT . LEU   BA 196 ? 2.1678 1.7060 1.3862 0.1177  -0.1126 -0.2887 196 LEU   b OXT 
49269 MG MG  . MG    CA .   ? 1.4127 0.7715 1.0268 -0.2980 -0.1286 -0.4355 301 MG    G MG  
49270 C  C5  . A1H71 DA .   ? 1.5561 0.8079 1.5269 -0.0134 -0.4020 -0.2541 301 A1H71 H C5  
49271 C  C6  . A1H71 DA .   ? 1.5430 0.7946 1.4911 -0.0089 -0.4213 -0.3068 301 A1H71 H C6  
49272 C  C7  . A1H71 DA .   ? 1.5493 0.8300 1.4438 -0.0547 -0.4119 -0.3168 301 A1H71 H C7  
49273 C  C8  . A1H71 DA .   ? 1.5698 0.7572 1.4631 -0.0371 -0.3710 -0.3269 301 A1H71 H C8  
49274 C  C15 . A1H71 DA .   ? 1.3581 0.6109 1.6868 0.1534  -0.2470 -0.1812 301 A1H71 H C15 
49275 C  C17 . A1H71 DA .   ? 1.1757 0.8847 1.0935 0.0567  -0.1414 -0.1188 301 A1H71 H C17 
49276 C  C21 . A1H71 DA .   ? 1.5328 0.6136 1.5365 0.0827  -0.2367 -0.3787 301 A1H71 H C21 
49277 C  C28 . A1H71 DA .   ? 1.6529 0.7115 1.6687 -0.0645 -0.2668 -0.1958 301 A1H71 H C28 
49278 C  C19 . A1H71 DA .   ? 1.1789 0.8836 1.0783 0.0589  -0.1409 -0.1170 301 A1H71 H C19 
49279 C  C18 . A1H71 DA .   ? 1.1764 0.8699 1.0882 0.0547  -0.1448 -0.1179 301 A1H71 H C18 
49280 C  C16 . A1H71 DA .   ? 1.1729 0.8717 1.1047 0.0528  -0.1456 -0.1207 301 A1H71 H C16 
49281 C  C14 . A1H71 DA .   ? 1.4399 0.5030 1.6851 0.1958  -0.2416 -0.1858 301 A1H71 H C14 
49282 O  O20 . A1H71 DA .   ? 1.4625 0.5562 1.7428 0.2487  -0.2876 -0.0656 301 A1H71 H O20 
49283 N  N13 . A1H71 DA .   ? 1.5279 0.5219 1.6284 0.1458  -0.2178 -0.2863 301 A1H71 H N13 
49284 C  C12 . A1H71 DA .   ? 1.5305 0.5620 1.5311 0.1064  -0.2458 -0.3541 301 A1H71 H C12 
49285 C  C23 . A1H71 DA .   ? 1.5105 0.6202 1.5536 0.1042  -0.2005 -0.3809 301 A1H71 H C23 
49286 O  O22 . A1H71 DA .   ? 1.6295 0.6252 1.5722 -0.0328 -0.2490 -0.4379 301 A1H71 H O22 
49287 C  C11 . A1H71 DA .   ? 1.6253 0.5287 1.4922 0.0366  -0.2864 -0.4147 301 A1H71 H C11 
49288 O  O24 . A1H71 DA .   ? 1.5420 0.6903 1.4243 0.0598  -0.2636 -0.4386 301 A1H71 H O24 
49289 N  N10 . A1H71 DA .   ? 1.6253 0.6104 1.4698 0.0317  -0.3091 -0.3886 301 A1H71 H N10 
49290 C  C9  . A1H71 DA .   ? 1.6779 0.6840 1.5008 0.0064  -0.2776 -0.3421 301 A1H71 H C9  
49291 C  C25 . A1H71 DA .   ? 1.6510 0.5332 1.5943 -0.0414 -0.2786 -0.3221 301 A1H71 H C25 
49292 O  O26 . A1H71 DA .   ? 1.6989 0.3580 1.6329 -0.0806 -0.1904 -0.2852 301 A1H71 H O26 
49293 N  N27 . A1H71 DA .   ? 1.6738 0.5782 1.5973 -0.0872 -0.2621 -0.3040 301 A1H71 H N27 
49294 N  N4  . A1H71 DA .   ? 1.5480 0.8371 1.6162 -0.0381 -0.3400 -0.2060 301 A1H71 H N4  
49295 C  C3  . A1H71 DA .   ? 1.5495 0.8502 1.5174 0.0092  -0.3159 -0.1803 301 A1H71 H C3  
49296 O  O37 . A1H71 DA .   ? 1.4797 0.7569 1.3751 0.0312  -0.3946 -0.1079 301 A1H71 H O37 
49297 C  C2  . A1H71 DA .   ? 1.5584 0.9136 1.5727 0.0095  -0.3096 -0.1765 301 A1H71 H C2  
49298 C  C1  . A1H71 DA .   ? 1.6076 0.8305 1.5791 0.0380  -0.2704 -0.1426 301 A1H71 H C1  
49299 O  OG1 . A1H71 DA .   ? 1.5504 1.0233 1.6637 0.1050  -0.2247 -0.1483 301 A1H71 H OG1 
49300 C  CB  . A1H71 DA .   ? 1.5347 1.2373 1.6101 0.1476  -0.2009 -0.1123 301 A1H71 H CB  
49301 C  CG2 . A1H71 DA .   ? 1.5411 1.2216 1.5682 0.1316  -0.2107 -0.1107 301 A1H71 H CG2 
49302 C  CA  . A1H71 DA .   ? 1.5836 1.2807 1.5711 0.1381  -0.2413 -0.0250 301 A1H71 H CA  
49303 C  C   . A1H71 DA .   ? 1.5758 1.2360 1.5269 0.1155  -0.2680 -0.0588 301 A1H71 H C   
49304 O  O   . A1H71 DA .   ? 1.5966 1.1760 1.5618 0.1685  -0.2491 0.0381  301 A1H71 H O   
49305 N  N   . A1H71 DA .   ? 1.6341 1.3253 1.6628 0.1864  -0.2167 -0.0077 301 A1H71 H N   
49306 C  C29 . A1H71 DA .   ? 1.6661 0.6849 1.6519 -0.2074 -0.2748 -0.1079 301 A1H71 H C29 
49307 C  C30 . A1H71 DA .   ? 1.2578 0.8562 1.2242 0.0230  -0.1795 -0.0876 301 A1H71 H C30 
49308 C  C35 . A1H71 DA .   ? 1.2576 0.8479 1.2127 0.0208  -0.1785 -0.0813 301 A1H71 H C35 
49309 C  C34 . A1H71 DA .   ? 1.2495 0.8452 1.2049 0.0210  -0.1731 -0.0790 301 A1H71 H C34 
49310 C  C33 . A1H71 DA .   ? 1.2458 0.8557 1.2111 0.0237  -0.1687 -0.0823 301 A1H71 H C33 
49311 C  C32 . A1H71 DA .   ? 1.2486 0.8674 1.2240 0.0259  -0.1699 -0.0892 301 A1H71 H C32 
49312 C  C31 . A1H71 DA .   ? 1.2556 0.8684 1.2324 0.0255  -0.1752 -0.0920 301 A1H71 H C31 
49313 MG MG  . MG    EA .   ? 2.1455 0.4702 1.2772 0.2654  0.4069  0.1648  302 MG    H MG  
49314 MG MG  . MG    FA .   ? 1.9900 0.6343 1.3224 0.3953  -0.1092 -0.3439 301 MG    I MG  
49315 C  C5  . A1H71 GA .   ? 1.5022 0.7555 1.5346 0.0123  -0.5319 0.0274  301 A1H71 K C5  
49316 C  C6  . A1H71 GA .   ? 1.5763 0.8650 1.5304 0.0056  -0.5245 0.0168  301 A1H71 K C6  
49317 C  C7  . A1H71 GA .   ? 1.6049 0.8038 1.4639 -0.0019 -0.5549 0.0656  301 A1H71 K C7  
49318 C  C8  . A1H71 GA .   ? 1.6394 0.6753 1.4320 -0.0111 -0.5694 0.0679  301 A1H71 K C8  
49319 C  C15 . A1H71 GA .   ? 1.8693 0.5501 1.1004 -0.0541 -0.5753 -0.0319 301 A1H71 K C15 
49320 C  C17 . A1H71 GA .   ? 1.3584 0.8140 1.1379 -0.1437 -0.2832 0.1159  301 A1H71 K C17 
49321 C  C21 . A1H71 GA .   ? 1.7571 0.5498 1.2226 -0.0004 -0.5801 0.0116  301 A1H71 K C21 
49322 C  C28 . A1H71 GA .   ? 1.5494 0.6521 1.4837 -0.0787 -0.4617 -0.0132 301 A1H71 K C28 
49323 C  C19 . A1H71 GA .   ? 1.3964 0.8716 1.1360 -0.1830 -0.2858 0.1402  301 A1H71 K C19 
49324 C  C18 . A1H71 GA .   ? 1.3829 0.8351 1.1449 -0.1575 -0.2960 0.1406  301 A1H71 K C18 
49325 C  C16 . A1H71 GA .   ? 1.3490 0.7832 1.1466 -0.1203 -0.2940 0.1166  301 A1H71 K C16 
49326 C  C14 . A1H71 GA .   ? 1.8066 0.4234 1.1936 -0.0530 -0.5952 -0.0437 301 A1H71 K C14 
49327 O  O20 . A1H71 GA .   ? 1.8622 0.3867 1.1514 -0.0980 -0.6841 -0.0600 301 A1H71 K O20 
49328 N  N13 . A1H71 GA .   ? 1.7724 0.4825 1.2353 -0.0926 -0.5962 -0.0264 301 A1H71 K N13 
49329 C  C12 . A1H71 GA .   ? 1.7551 0.5286 1.2049 -0.0625 -0.6254 -0.0074 301 A1H71 K C12 
49330 C  C23 . A1H71 GA .   ? 1.7727 0.6055 1.2461 0.0006  -0.5465 -0.0137 301 A1H71 K C23 
49331 O  O22 . A1H71 GA .   ? 1.7317 0.5915 1.1966 0.0020  -0.5750 0.0820  301 A1H71 K O22 
49332 C  C11 . A1H71 GA .   ? 1.7111 0.5493 1.2378 -0.0622 -0.6553 0.0795  301 A1H71 K C11 
49333 O  O24 . A1H71 GA .   ? 1.5722 0.6217 1.1354 -0.0871 -0.7811 0.0792  301 A1H71 K O24 
49334 N  N10 . A1H71 GA .   ? 1.6837 0.5705 1.2675 -0.0559 -0.6269 0.0637  301 A1H71 K N10 
49335 C  C9  . A1H71 GA .   ? 1.6613 0.5952 1.4043 -0.0596 -0.5499 0.0806  301 A1H71 K C9  
49336 C  C25 . A1H71 GA .   ? 1.6272 0.5465 1.4332 -0.0933 -0.5514 0.0449  301 A1H71 K C25 
49337 O  O26 . A1H71 GA .   ? 1.6461 0.5684 1.5274 -0.1218 -0.5215 0.0632  301 A1H71 K O26 
49338 N  N27 . A1H71 GA .   ? 1.5902 0.5721 1.4936 -0.0942 -0.4855 0.0046  301 A1H71 K N27 
49339 N  N4  . A1H71 GA .   ? 1.4802 0.7002 1.5304 -0.0081 -0.5220 0.0763  301 A1H71 K N4  
49340 C  C3  . A1H71 GA .   ? 1.4834 0.5751 1.5470 -0.1326 -0.4622 0.0682  301 A1H71 K C3  
49341 O  O37 . A1H71 GA .   ? 1.5278 0.4234 1.4770 -0.1151 -0.5668 -0.0311 301 A1H71 K O37 
49342 C  C2  . A1H71 GA .   ? 1.5174 0.6814 1.5189 -0.1006 -0.4719 0.0530  301 A1H71 K C2  
49343 C  C1  . A1H71 GA .   ? 1.5187 0.6467 1.4918 -0.0975 -0.4491 0.0110  301 A1H71 K C1  
49344 O  OG1 . A1H71 GA .   ? 1.5151 0.6622 1.5323 -0.1396 -0.4407 -0.0253 301 A1H71 K OG1 
49345 C  CB  . A1H71 GA .   ? 1.5331 0.6522 1.5034 -0.1468 -0.4790 -0.0946 301 A1H71 K CB  
49346 C  CG2 . A1H71 GA .   ? 1.5210 0.6445 1.5064 -0.1059 -0.4981 -0.0854 301 A1H71 K CG2 
49347 C  CA  . A1H71 GA .   ? 1.5933 0.6877 1.4705 -0.1523 -0.4801 -0.1243 301 A1H71 K CA  
49348 C  C   . A1H71 GA .   ? 1.6162 0.6638 1.4495 -0.1424 -0.4842 -0.1153 301 A1H71 K C   
49349 O  O   . A1H71 GA .   ? 1.5941 0.5949 1.3864 -0.1628 -0.5180 -0.1510 301 A1H71 K O   
49350 N  N   . A1H71 GA .   ? 1.6398 0.6900 1.5209 -0.1604 -0.4677 -0.1142 301 A1H71 K N   
49351 C  C29 . A1H71 GA .   ? 1.5109 0.7002 1.4397 -0.0007 -0.4472 -0.0362 301 A1H71 K C29 
49352 C  C30 . A1H71 GA .   ? 1.2831 0.6542 1.1605 -0.0016 -0.3270 0.0418  301 A1H71 K C30 
49353 C  C35 . A1H71 GA .   ? 1.2730 0.6504 1.1508 0.0023  -0.3248 0.0389  301 A1H71 K C35 
49354 C  C34 . A1H71 GA .   ? 1.2655 0.6559 1.1606 -0.0023 -0.3197 0.0341  301 A1H71 K C34 
49355 C  C33 . A1H71 GA .   ? 1.2677 0.6660 1.1765 -0.0123 -0.3159 0.0315  301 A1H71 K C33 
49356 C  C32 . A1H71 GA .   ? 1.2804 0.6717 1.1846 -0.0171 -0.3186 0.0361  301 A1H71 K C32 
49357 C  C31 . A1H71 GA .   ? 1.2859 0.6631 1.1763 -0.0111 -0.3246 0.0414  301 A1H71 K C31 
49358 MG MG  . MG    HA .   ? 0.9106 0.6602 1.8715 0.1965  -0.2537 0.3539  302 MG    K MG  
49359 MG MG  . MG    IA .   ? 1.5347 0.5149 1.1306 -0.0418 -0.1689 -0.4186 201 MG    N MG  
49360 C  C5  . A1H71 JA .   ? 1.7601 0.6744 1.5582 -0.1905 -0.3683 0.0705  301 A1H71 V C5  
49361 C  C6  . A1H71 JA .   ? 1.7666 0.7224 1.5830 -0.1631 -0.2989 0.1340  301 A1H71 V C6  
49362 C  C7  . A1H71 JA .   ? 1.7226 0.7196 1.6059 -0.1581 -0.3213 0.1580  301 A1H71 V C7  
49363 C  C8  . A1H71 JA .   ? 1.7423 0.6417 1.5494 -0.0904 -0.3480 0.2014  301 A1H71 V C8  
49364 C  C15 . A1H71 JA .   ? 1.5211 0.4182 1.5065 -0.0066 -0.3839 0.0162  301 A1H71 V C15 
49365 C  C17 . A1H71 JA .   ? 1.2018 0.7699 1.1424 0.0366  -0.2237 0.1197  301 A1H71 V C17 
49366 C  C21 . A1H71 JA .   ? 1.5898 0.5767 1.5702 0.0895  -0.3315 0.0924  301 A1H71 V C21 
49367 C  C28 . A1H71 JA .   ? 1.5850 0.6210 1.5007 0.0177  -0.4555 0.2332  301 A1H71 V C28 
49368 C  C19 . A1H71 JA .   ? 1.2088 0.7674 1.1338 0.0418  -0.2249 0.1211  301 A1H71 V C19 
49369 C  C18 . A1H71 JA .   ? 1.2054 0.7607 1.1398 0.0351  -0.2212 0.1206  301 A1H71 V C18 
49370 C  C16 . A1H71 JA .   ? 1.1954 0.7607 1.1460 0.0301  -0.2196 0.1198  301 A1H71 V C16 
49371 C  C14 . A1H71 JA .   ? 1.5557 0.4955 1.5512 0.0108  -0.3340 0.0487  301 A1H71 V C14 
49372 O  O20 . A1H71 JA .   ? 1.5665 0.6075 1.6005 -0.0888 -0.2971 -0.0425 301 A1H71 V O20 
49373 N  N13 . A1H71 JA .   ? 1.5968 0.4096 1.5377 0.0075  -0.3578 0.0334  301 A1H71 V N13 
49374 C  C12 . A1H71 JA .   ? 1.6333 0.5243 1.5457 0.0558  -0.3309 0.0879  301 A1H71 V C12 
49375 C  C23 . A1H71 JA .   ? 1.6152 0.6770 1.5669 0.1499  -0.3105 0.0837  301 A1H71 V C23 
49376 O  O22 . A1H71 JA .   ? 1.6949 0.6114 1.5583 0.0931  -0.2429 0.1664  301 A1H71 V O22 
49377 C  C11 . A1H71 JA .   ? 1.6822 0.5290 1.5719 -0.0238 -0.3494 0.1607  301 A1H71 V C11 
49378 O  O24 . A1H71 JA .   ? 1.5437 0.6276 1.5167 -0.0274 -0.3748 0.1357  301 A1H71 V O24 
49379 N  N10 . A1H71 JA .   ? 1.7001 0.5440 1.5313 0.0088  -0.3513 0.1977  301 A1H71 V N10 
49380 C  C9  . A1H71 JA .   ? 1.6998 0.6009 1.5420 -0.0334 -0.3741 0.1919  301 A1H71 V C9  
49381 C  C25 . A1H71 JA .   ? 1.6448 0.4817 1.5633 -0.0486 -0.4003 0.1935  301 A1H71 V C25 
49382 O  O26 . A1H71 JA .   ? 1.6532 0.3499 1.5517 -0.0549 -0.3688 0.2352  301 A1H71 V O26 
49383 N  N27 . A1H71 JA .   ? 1.5862 0.5098 1.5718 -0.0567 -0.4266 0.2053  301 A1H71 V N27 
49384 N  N4  . A1H71 JA .   ? 1.7415 0.6897 1.5296 -0.1417 -0.4316 0.0884  301 A1H71 V N4  
49385 C  C3  . A1H71 JA .   ? 1.6577 0.7843 1.4132 -0.0092 -0.4919 0.1742  301 A1H71 V C3  
49386 O  O37 . A1H71 JA .   ? 1.8355 0.8575 1.2247 -0.0374 -0.5314 0.1996  301 A1H71 V O37 
49387 C  C2  . A1H71 JA .   ? 1.6571 0.8194 1.4427 0.0132  -0.4361 0.2147  301 A1H71 V C2  
49388 C  C1  . A1H71 JA .   ? 1.6052 0.7678 1.4030 0.0888  -0.4469 0.2118  301 A1H71 V C1  
49389 O  OG1 . A1H71 JA .   ? 1.6291 0.8707 1.4466 0.1779  -0.4204 0.2868  301 A1H71 V OG1 
49390 C  CB  . A1H71 JA .   ? 1.6506 0.9546 1.4936 0.2344  -0.4063 0.2251  301 A1H71 V CB  
49391 C  CG2 . A1H71 JA .   ? 1.5680 1.0107 1.5717 0.2629  -0.4220 0.2199  301 A1H71 V CG2 
49392 C  CA  . A1H71 JA .   ? 1.7171 0.9437 1.5567 0.1771  -0.3310 0.1462  301 A1H71 V CA  
49393 C  C   . A1H71 JA .   ? 1.6906 0.8351 1.5783 0.0989  -0.3255 0.1382  301 A1H71 V C   
49394 O  O   . A1H71 JA .   ? 1.7694 0.6881 1.5200 0.1691  -0.3516 0.0004  301 A1H71 V O   
49395 N  N   . A1H71 JA .   ? 1.7321 0.9470 1.6170 0.1938  -0.3359 0.1149  301 A1H71 V N   
49396 C  C29 . A1H71 JA .   ? 1.6217 0.6661 1.4144 -0.0268 -0.4813 0.2486  301 A1H71 V C29 
49397 C  C30 . A1H71 JA .   ? 1.2073 0.7124 1.1789 -0.0219 -0.1993 0.1009  301 A1H71 V C30 
49398 C  C35 . A1H71 JA .   ? 1.2137 0.7086 1.1779 -0.0248 -0.2016 0.0971  301 A1H71 V C35 
49399 C  C34 . A1H71 JA .   ? 1.2147 0.7121 1.1805 -0.0253 -0.2066 0.0932  301 A1H71 V C34 
49400 C  C33 . A1H71 JA .   ? 1.2085 0.7191 1.1822 -0.0226 -0.2094 0.0929  301 A1H71 V C33 
49401 C  C32 . A1H71 JA .   ? 1.2034 0.7244 1.1837 -0.0195 -0.2070 0.0971  301 A1H71 V C32 
49402 C  C31 . A1H71 JA .   ? 1.2053 0.7233 1.1850 -0.0193 -0.2019 0.1012  301 A1H71 V C31 
49403 MG MG  . MG    KA .   ? 0.9904 2.4080 1.4324 -0.2298 -0.0715 -0.0370 302 MG    V MG  
49404 C  C5  . A1H71 LA .   ? 1.6493 0.3786 1.5177 0.1650  -0.0190 -0.1479 301 A1H71 Y C5  
49405 C  C6  . A1H71 LA .   ? 1.6929 0.5189 1.4802 0.0786  0.0130  -0.1386 301 A1H71 Y C6  
49406 C  C7  . A1H71 LA .   ? 1.6863 0.5919 1.4295 0.1187  -0.0109 -0.1440 301 A1H71 Y C7  
49407 C  C8  . A1H71 LA .   ? 1.7181 0.6725 1.4154 0.0613  -0.0090 -0.1891 301 A1H71 Y C8  
49408 C  C15 . A1H71 LA .   ? 1.9773 0.6422 1.0973 0.2019  -0.1000 -0.4045 301 A1H71 Y C15 
49409 C  C17 . A1H71 LA .   ? 1.2558 0.8363 1.0014 -0.0291 -0.0461 -0.1040 301 A1H71 Y C17 
49410 C  C21 . A1H71 LA .   ? 1.8670 0.7078 1.2324 0.1488  -0.0144 -0.3841 301 A1H71 Y C21 
49411 C  C28 . A1H71 LA .   ? 1.5802 0.6472 1.4938 0.0604  -0.0069 -0.1817 301 A1H71 Y C28 
49412 C  C19 . A1H71 LA .   ? 1.3153 0.8732 0.9939 -0.0629 -0.0461 -0.1102 301 A1H71 Y C19 
49413 C  C18 . A1H71 LA .   ? 1.2896 0.8504 0.9970 -0.0457 -0.0323 -0.1172 301 A1H71 Y C18 
49414 C  C16 . A1H71 LA .   ? 1.2340 0.8163 1.0034 -0.0137 -0.0312 -0.1104 301 A1H71 Y C16 
49415 C  C14 . A1H71 LA .   ? 1.9454 0.6029 1.1551 0.1648  -0.0668 -0.4108 301 A1H71 Y C14 
49416 O  O20 . A1H71 LA .   ? 1.9645 0.6038 1.0835 0.1728  0.0162  -0.3980 301 A1H71 Y O20 
49417 N  N13 . A1H71 LA .   ? 1.9044 0.6210 1.1862 0.1101  -0.0721 -0.4005 301 A1H71 Y N13 
49418 C  C12 . A1H71 LA .   ? 1.8666 0.6959 1.2364 0.0910  -0.0281 -0.3716 301 A1H71 Y C12 
49419 C  C23 . A1H71 LA .   ? 1.8574 0.7240 1.2195 0.1598  -0.0074 -0.3425 301 A1H71 Y C23 
49420 O  O22 . A1H71 LA .   ? 1.7389 0.8130 1.1716 0.1224  0.0186  -0.4818 301 A1H71 Y O22 
49421 C  C11 . A1H71 LA .   ? 1.9058 0.6353 1.2838 0.0564  -0.0627 -0.3714 301 A1H71 Y C11 
49422 O  O24 . A1H71 LA .   ? 1.9428 0.7038 1.3245 -0.0168 -0.0042 -0.3889 301 A1H71 Y O24 
49423 N  N10 . A1H71 LA .   ? 1.8590 0.6953 1.3879 0.0184  -0.0654 -0.2864 301 A1H71 Y N10 
49424 C  C9  . A1H71 LA .   ? 1.7440 0.6418 1.3994 0.0446  -0.0276 -0.2195 301 A1H71 Y C9  
49425 C  C25 . A1H71 LA .   ? 1.6494 0.6237 1.4554 0.0351  -0.0081 -0.1966 301 A1H71 Y C25 
49426 O  O26 . A1H71 LA .   ? 1.5874 0.7552 1.4032 0.0570  0.1077  -0.1453 301 A1H71 Y O26 
49427 N  N27 . A1H71 LA .   ? 1.5948 0.6013 1.4750 0.0416  -0.0018 -0.2114 301 A1H71 Y N27 
49428 N  N4  . A1H71 LA .   ? 1.6381 0.3444 1.5291 0.1867  -0.0215 -0.1666 301 A1H71 Y N4  
49429 C  C3  . A1H71 LA .   ? 1.6361 0.3979 1.4947 0.1056  -0.0316 -0.1623 301 A1H71 Y C3  
49430 O  O37 . A1H71 LA .   ? 1.6786 0.4253 1.4982 0.0631  -0.0455 -0.1438 301 A1H71 Y O37 
49431 C  C2  . A1H71 LA .   ? 1.6565 0.5644 1.4938 0.0647  -0.0345 -0.1287 301 A1H71 Y C2  
49432 C  C1  . A1H71 LA .   ? 1.6266 0.6102 1.4775 0.0402  -0.0239 -0.1632 301 A1H71 Y C1  
49433 O  OG1 . A1H71 LA .   ? 1.6384 0.6464 1.5017 -0.0225 -0.0634 -0.1246 301 A1H71 Y OG1 
49434 C  CB  . A1H71 LA .   ? 1.6355 0.7053 1.4915 -0.0688 -0.0503 -0.0992 301 A1H71 Y CB  
49435 C  CG2 . A1H71 LA .   ? 1.6291 0.7321 1.5020 -0.0134 -0.0361 -0.1353 301 A1H71 Y CG2 
49436 C  CA  . A1H71 LA .   ? 1.6488 0.7317 1.4719 -0.0827 -0.0516 -0.0916 301 A1H71 Y CA  
49437 C  C   . A1H71 LA .   ? 1.6407 0.6868 1.4534 -0.0943 -0.0236 -0.0704 301 A1H71 Y C   
49438 O  O   . A1H71 LA .   ? 1.6342 0.5695 1.3958 -0.0904 0.0000  -0.0306 301 A1H71 Y O   
49439 N  N   . A1H71 LA .   ? 1.6738 0.7385 1.5113 -0.1353 -0.0519 -0.0792 301 A1H71 Y N   
49440 C  C29 . A1H71 LA .   ? 1.5686 0.6789 1.5423 0.1465  0.0101  -0.1663 301 A1H71 Y C29 
49441 C  C30 . A1H71 LA .   ? 1.1444 0.7903 1.0839 0.0832  0.0176  -0.0942 301 A1H71 Y C30 
49442 C  C35 . A1H71 LA .   ? 1.1360 0.7876 1.0821 0.0920  0.0153  -0.0928 301 A1H71 Y C35 
49443 C  C34 . A1H71 LA .   ? 1.1326 0.7974 1.0978 0.0925  0.0069  -0.0902 301 A1H71 Y C34 
49444 C  C33 . A1H71 LA .   ? 1.1378 0.8114 1.1143 0.0830  -0.0007 -0.0877 301 A1H71 Y C33 
49445 C  C32 . A1H71 LA .   ? 1.1489 0.8163 1.1147 0.0730  0.0014  -0.0897 301 A1H71 Y C32 
49446 C  C31 . A1H71 LA .   ? 1.1497 0.8029 1.0979 0.0736  0.0114  -0.0936 301 A1H71 Y C31 
49447 MG MG  . MG    MA .   ? 1.4149 1.3891 0.9322 -0.0517 -0.1822 0.1106  302 MG    Y MG  
49448 MG MG  . MG    NA .   ? 1.5459 0.5880 2.5542 -0.5486 0.0801  -0.4065 301 MG    Z MG  
# 
